[{"uniquename":"PMID:9765482","title":"A map of interactions between the proteins of a retrotransposon.","citation":"J Virol 1998 Nov;72(11):9318-22","abstract":"The yeast two-hybrid system and in vitro binding assays were used to characterize 54 potential interactions between the proteins of Tf1, an LTR-retrotransposon found in Schizosaccharomyces pombe. The Tf1 integrase (IN) protein was found to interact strongly with itself and not with other control proteins. In addition, the IN core domain interacted strongly with itself and full-length IN. Interestingly, the two-hybrid analysis detected an interaction between the RNase H domain of reverse transcriptase and IN. The biological implications of these interactions are discussed.","authors":"Steele SJ, Levin HL","authors_abbrev":"Steele SJ et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1998-10-10","publication_year":"1998","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25760713","title":"Improved crystallization and diffraction of caffeine-induced death suppressor protein 1 (Cid1).","citation":"Acta Crystallogr F Struct Biol Commun 2015 Mar;71(Pt 3):346-53","abstract":"The post-transcriptional addition of uridines to the 3'-end of RNAs is an important regulatory process that is critical for coding and noncoding RNA stability. In fission yeast and metazoans this untemplated 3'-uridylylation is catalysed by a single family of terminal uridylyltransferases (TUTs) whose members are adapted to specific RNA targets. In Schizosaccharomyces pombe the TUT Cid1 is responsible for the uridylylation of polyadenylated mRNAs, targeting them for destruction. In metazoans, the Cid1 orthologues ZCCHC6 and ZCCHC11 uridylate histone mRNAs, targeting them for degradation, but also uridylate microRNAs, altering their maturation. Cid1 has been studied as a model TUT that has provided insights into the larger and more complex metazoan enzyme system. In this paper, two strategies are described that led to improvements both in the crystallogenesis of Cid1 and in the resolution of diffraction by ∼1.5 Å. These advances have allowed high-resolution crystallographic studies of this TUT system to be initiated.","doi":"10.1107/S2053230X15001351","authors":"Yates LA, Durrant BP, Barber M, Harlos K, Fleurdépine S, Norbury CJ, Gilbert RJ","authors_abbrev":"Yates LA et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-03-12","publication_year":"2015","canto_session_key":"3392671102f6bfa6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-28 12:59:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-28 12:59:15","canto_added_date":"2015-03-13 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19D5.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-03-28"},{"uniquename":"PMID:25356547","title":"A complex network of interactions between mitotic kinases, phosphatases and ESCRT proteins regulates septation and membrane trafficking in S. pombe.","citation":"PLoS One 2014;9(10):e111789","abstract":"Cytokinesis and cell separation are critical events in the cell cycle. We show that Endosomal Sorting Complex Required for Transport (ESCRT) genes are required for cell separation in Schizosaccharomyces pombe. We identify genetic interactions between ESCRT proteins and polo and aurora kinases and Cdc14 phosphatase that manifest as impaired growth and exacerbated defects in septation, suggesting that the encoded proteins function together to control these processes. Furthermore, we observed defective endosomal sorting in mutants of plo1, ark1 and clp1, as has been reported for ESCRT mutants, consistent with a role for these kinases in the control of ESCRT function in membrane traffic. Multiple observations indicate functional interplay between polo and ESCRT components: firstly, two-hybrid in vivo interactions are reported between Plo1p and Sst4p, Vps28p, Vps25p, Vps20p and Vps32p; secondly, co-immunoprecipitation of human homologues of Vps20p, Vps32p, Vps24p and Vps2p by human Plk1; and thirdly, in vitro phosphorylation of budding yeast Vps32p and Vps20p by polo kinase. Two-hybrid analyses also identified interactions between Ark1p and Vps20p and Vps32p, and Clp1p and Vps28p. These experiments indicate a network of interactions between ESCRT proteins, plo1, ark1 and clp1 that coordinate membrane trafficking and cell separation in fission yeast.","doi":"10.1371/journal.pone.0111789","authors":"Bhutta MS, Roy B, Gould GW, McInerny CJ","authors_abbrev":"Bhutta MS et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-10-31","publication_year":"2014","canto_session_key":"a15216784fcaa950","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chris McInerny","canto_first_approved_date":"2016-08-23 18:04:19","canto_approved_date":"2022-01-25 08:34:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-27 09:40:33","canto_added_date":"2014-11-01 01:15:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Chris McInerny","community_curator":true,"annotation_count":50,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":181,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1142.07c","SPAC1B3.07c","SPBC4B4.06","SPAC2G11.06","SPBC3B9.09","SPAC23C11.16","SPAC11H11.01","SPAC19A8.05c","SPBC215.14c","SPAC24C9.08","SPAC4F8.01","SPAC1782.09c","SPCC320.13c"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2016-08-23"},{"uniquename":"PMID:16158300","title":"A fluorimetric assay for cortisol.","citation":"Anal Bioanal Chem 2005 Sep;383(2):182-6","abstract":"A simple, rapid and sensitive fluorimetric assay for the quantitative determination of cortisol is reported. The assay is based on the formation of a fluorescent dye when cortisol is incubated with a mixture of sulfuric acid and acetic acid. The fluorescence spectrum recorded for the resulting dye shows a maximum extinction at 475 nm and a maximum emission at 525 nm. The solvent 2-methyl-4-pentanone was used for extraction and was found to act as a fluorescence amplifier. A limit of detection of 2.7 muM was achieved, making it possible to forego solvent evaporation. The assay suffers minor interference from 11-deoxycortisol which exhibits low fluorescence at lambda (ex): 460 nm; lambda (em): 505 nm. Typical standard deviations were below 4%. We validated the assay using a biotransformation with recombinant Schizosaccharomyces pombe which regioselectively hydroxylates 11-deoxycortisol to cortisol. The method described herein is suitable for preliminary screening of microorganisms capable of steroid hydroxylation.","authors":"Appel D, Schmid RD, Dragan CA, Bureik M, Urlacher VB","authors_abbrev":"Appel D et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-09-15","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17912366","title":"Deletion of genes implicated in protecting the integrity of male germ cells has differential effects on the incidence of DNA breaks and germ cell loss.","citation":"PLoS One 2007 Oct 03;2(10):e989","abstract":"Infertility affects approximately 20% of couples in Europe and in 50% of cases the problem lies with the male partner. The impact of damaged DNA originating in the male germ line on infertility is poorly understood but may increase miscarriage. Mouse models allow us to investigate how deficiencies in DNA repair/damage response pathways impact on formation and function of male germ cells. We have investigated mice with deletions of ERCC1 (excision repair cross-complementing gene 1), MSH2 (MutS homolog 2, involved in mismatch repair pathway), and p53 (tumour suppressor gene implicated in elimination of germ cells with DNA damage).\nWe demonstrate for the first time that depletion of ERCC1 or p53 from germ cells results in an increased incidence of unrepaired DNA breaks in pachytene spermatocytes and increased numbers of caspase-3 positive (apoptotic) germ cells. Sertoli cell-only tubules were detected in testes from mice lacking expression of ERCC1 or MSH2 but not p53. The number of sperm recovered from epididymes was significantly reduced in mice lacking testicular ERCC1 and 40% of sperm contained DNA breaks whereas the numbers of sperm were not different to controls in adult Msh2 -/- or p53 -/- mice nor did they have significantly compromised DNA.\nThese data have demonstrated that deletion of Ercc1, Msh2 and p53 can have differential but overlapping affects on germ cell function and sperm production. These findings increase our understanding of the ways in which gene mutations can have an impact on male fertility.","authors":"Paul C, Povey JE, Lawrence NJ, Selfridge J, Melton DW, Saunders PT","authors_abbrev":"Paul C et al.","pubmed_publication_date":"03 Oct 2007","pubmed_entrez_date":"2007-10-04","publication_year":"2007","canto_session_key":"e22e6a8d667d3cae","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-06-30 16:20:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34532559","title":"Systematic Quantification of GFP-tagged Protein Foci in  Schizosaccharomyces pombe  Nuclei.","citation":"Bio Protoc 2018 Dec 20;8(24):e3117","abstract":"DNA damage repair proteins form foci in response to DNA damaging agents. The efficiency and integrity of the DNA repair pathway of a particular eukaryotic (mutant) strain is usually determined by the number of foci formed compared with their wild-type counterpart. Conventionally, focus number is determined visually, and this low accuracy may obscure the identification of a weaker phenotype, particularly when the output is low. Here, using the homologous recombination protein Rhp54 as an example, we present a protocol that can increase the consistency of foci identification among samples and can significantly improve the efficiency of foci quantification for large sample sizes. A similar method can be applied to other foci-forming proteins.","doi":"10.21769/BioProtoc.3117","authors":"Lim KK, Chen ES","authors_abbrev":"Lim KK et al.","pubmed_publication_date":"20 Dec 2018","pubmed_entrez_date":"2021-09-17","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-09-19 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:41123941","title":"Fission yeast Pdk1 kinase regulates cytokinesis and eisosomes.","citation":"Mol Biol Cell 2025 Oct 22;:mbcE25070330","abstract":"The conserved phosphoinositide-dependent protein kinase PDK1 regulates cell growth and stress signaling in eukaryotes. In the fission yeast  S. pombe , Pdk1 has been linked to cytokinesis, which could point to new functions for this kinase family. Here, we discovered that Pdk1 localizes to eisosomes, which create invaginations in the plasma membrane, in addition to the spindle pole body (SPB). Pdk1 promotes phosphorylation of the core eisosome protein Pil1 and regulates eisosome length. Dysregulated eisosomes are not responsible for cytokinesis defects previously observed in  pdk1∆  cells. Instead, we found that Pdk1 regulates localization of the anillin-like protein Mid1 and the protein kinase Sid2, which promotes cytokinesis as part of the septation initiation network (SIN). Our combined results provide insights into the role of Pdk1 in eisosomes and cytokinesis, which extend the functions of this conserved protein kinase family beyond canonical growth control pathways.","doi":"10.1091/mbc.E25-07-0330","authors":"Chrupcala ML, Flynn MJ, Moseley JB","authors_abbrev":"Chrupcala ML et al.","pubmed_publication_date":"22 Oct 2025","pubmed_entrez_date":"2025-10-22","publication_year":"2025","canto_session_key":"7b31dbe64800f42c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10694511","title":"yam8(+), a Schizosaccharomyces pombe gene, is a potential homologue of the Saccharomyces cerevisiae MID1 gene encoding a stretch-activated Ca(2+)-permeable channel.","citation":"Biochem Biophys Res Commun 2000 Mar 05;269(1):265-9","abstract":"The Saccharomyces cerevisiae MID1 gene encodes a stretch-activated Ca(2+)-permeable channel. In a protein database, we found a Schizosaccharomyces pombe gene whose predicted protein shows 26% identical and 62% similar to the Mid1 channel in amino acid sequence. cDNA derived from this gene, designated yam8(+), was isolated by reverse transcription-polymerase chain reaction (RT-PCR). Further analysis showed that the Yam8 protein consists of 486 amino acids and has 6 hydrophobic segments. The yam8(+) cDNA, placed under the S. cerevisiae TDH3 promoter, partially complemented the mating pheromone-induced death (mid) phenotype of the S. cerevisiae mid1 mutant. The expression of the yam8(+) cDNA in the mid1 mutant cells partially remediated the mid phenotype and resulted in a slight increase in Ca(2+) uptake activity. These findings suggest that Yam8 is a potential homologue of Mid1.","authors":"Tasaka Y, Nakagawa Y, Sato C, Mino M, Uozumi N, Murata N, Muto S, Iida H","authors_abbrev":"Tasaka Y et al.","pubmed_publication_date":"05 Mar 2000","pubmed_entrez_date":"2000-03-01","publication_year":"2000","canto_session_key":"4b32e8af291e9ad0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-08-04 14:48:06","canto_approved_date":"2026-03-26 22:36:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 14:47:53","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F5.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:26425801","title":"Molecular identification and physiological characterization of yeasts, lactic acid bacteria and acetic acid bacteria isolated from heap and box cocoa bean fermentations in West Africa.","citation":"Int J Food Microbiol 2016 Jan 04;216:69-78","abstract":"Yeast, lactic acid bacteria (LAB) and acetic acid bacteria (AAB) populations, isolated from cocoa bean heap and box fermentations in West Africa, have been investigated. The fermentation dynamicswere determined by viable counts, and 106 yeasts, 105 LAB and 82 AAB isolateswere identified by means of rep-PCR grouping and sequencing of the rRNA genes. During the box fermentations, the most abundant species were Saccharomyces cerevisiae, Candida ethanolica, Lactobacillus fermentum, Lactobacillus plantarum, Acetobacter pasteurianus and Acetobacter syzygii, while S. cerevisiae, Schizosaccharomyces pombe, Hanseniaspora guilliermondii, Pichia manshurica, C. ethanolica, Hanseniaspora uvarum, Lb. fermentum, Lb. plantarum, A. pasteurianus and Acetobacter lovaniensis were identified in the heap fermentations. Furthermore, the most abundant species were molecularly characterized by analyzing the rep-PCR profiles. Strains grouped according to the type of fermentations and their progression during the transformation process were also highlighted. The yeast, LAB and AAB isolates were physiologically characterized to determine their ability to grow at different temperatures, as well as at different pH, and ethanol concentrations, tolerance to osmotic stress, and lactic acid and acetic acid inhibition. Temperatures of 45 °C, a pH of 2.5 to 3.5, 12% (v/v) ethanol and high concentrations of lactic and acetic acid have a significant influence on the growth of yeasts, LAB and AAB. Finally, the yeastswere screened for enzymatic activity, and the S. cerevisiae, H. guilliermondii, H. uvarumand C. ethanolica species were shown to possess several enzymes that may impact the quality of the final product.","doi":"10.1016/j.ijfoodmicro.2015.09.004","authors":"Visintin S, Alessandria V, Valente A, Dolci P, Cocolin L","authors_abbrev":"Visintin S et al.","pubmed_publication_date":"04 Jan 2016","pubmed_entrez_date":"2015-10-02","publication_year":"2016","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2016-01-30 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18775730","title":"Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation.","citation":"J Mol Biol 2008 Nov 14;383(3):693-712","abstract":"Deleted in Split hand/Split foot 1 (DSS1) was previously identified as a novel 12-O-tetradecanoylphorbol-13-acetate (TPA)-inducible gene with possible involvement in early event of mouse skin carcinogenesis. The mechanisms by which human DSS1 (HsDSS1) exerts its biological effects via regulation of the ubiquitin-proteasome system (UPS) are currently unknown. Here, we demonstrated that HsDSS1 regulates the human proteasome by associating with it in the cytosol and nucleus via the RPN3/S3 subunit of the 19S regulatory particle (RP). Molecular anatomy of HsDSS1 revealed an RPN3/S3-interacting motif (R3IM), located at amino acid residues 15 to 21 of the NH(2) terminus. Importantly, negative charges of the R3IM motif were demonstrated to be required for proteasome interaction and binding to poly-ubiquitinated substrates. Indeed, the R3IM motif of HsDSS1 protein alone was sufficient to replace the ability of intact HsDSS1 protein to pull down proteasome complexes and protein substrates with high-molecular mass ubiquitin conjugates. Interestingly, this interaction is highly conserved throughout evolution from humans to nematodes. Functional study, lowering the levels of the endogenous HsDSS1 using siRNA, indicates that the R3IM/proteasome complex binds and targets p53 for ubiquitin-mediated degradation via gankyrin-MDM2/HDM2 pathway. Most significantly, this work indicates that the R3IM motif of HsDSS1, in conjunction with the complexes of 19S RP and 20S core particle (CP), regulates proteasome interaction through RPN3/S3 molecule, and utilizes a specific subset of poly-ubiquitinated p53 as a substrate.","doi":"10.1016/j.jmb.2008.08.044","authors":"Wei SJ, Williams JG, Dang H, Darden TA, Betz BL, Humble MM, Chang FM, Trempus CS, Johnson K, Cannon RE, Tennant RW","authors_abbrev":"Wei SJ et al.","pubmed_publication_date":"14 Nov 2008","pubmed_entrez_date":"2008-09-09","publication_year":"2008","canto_session_key":"eff115cd2c6eb902","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-30 11:01:33","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-30 11:01:28","canto_added_date":"2016-09-21 00:18:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.02","SPBC119.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-09-30"},{"uniquename":"PMID:39473172","title":"Mrc1 Claspin  is essential for heterochromatin maintenance in Schizosaccharomyces pombe.","citation":"Genes Cells 2024 Oct 29;","abstract":"In eukaryotes, maintenance of heterochromatin structure that represses gene expression during cell proliferation is essential for guaranteeing cell identity. However, how heterochromatin is maintained and transmitted to the daughter cells remains elusive. In this study, we constructed a reporter system to study the maintenance of heterochromatin in the subtelomeric region of the fission yeast, Schizosaccharomyces pombe. We demonstrated that once subtelomeric heterochromatin was established, it tended to be maintained as a metastable structure through cell proliferation. Using this system, we screened an S. pombe genome-wide gene deletion library for subtelomeric heterochromatin maintenance factors and identified 57 genes related to various cellular processes, in addition to well-characterized heterochromatin factors. We focused on Mrc1 Claspin , a mediator of DNA replication checkpoint. We found that Mrc1 maintains heterochromatin structure not only at the subtelomeres but also at the pericentromeres and mating-type regions. Furthermore, we showed that Mrc1 is required for the localization of Snf2/Hdac-containing Repressor Complex (SHREC) and the maintenance of hypoacetylation state of histone H3K14. This study complements the recent discoveries that Mrc1 functions as a histone H3-H4 chaperone in heterochromatin maintenance.","doi":"10.1111/gtc.13175","authors":"Kawakami K, Ueno Y, Hayama N, Tanaka K","authors_abbrev":"Kawakami K et al.","pubmed_publication_date":"29 Oct 2024","pubmed_entrez_date":"2024-10-30","publication_year":"2024","canto_session_key":"56553adbd54cc6fe","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-10-31 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC694.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:14970237","title":"Requirement of the SCFPop1/Pop2 Ubiquitin Ligase for Degradation of the Fission Yeast S Phase Cyclin Cig2.","citation":"J Biol Chem 2004 Apr 30;279(18):18974-80","abstract":"Two multiprotein E3 (ubiquitin-protein ligase) ubiquitin ligases, the SCF (Skp1-Cullin-1-F-box) and the APC/C (anaphase promoting complex/cyclosome), are vital in ensuring the temporal order of the cell cycle. Particularly, timely destruction of cyclins via these two E3s is essential for down-regulation of cyclin-dependent kinase. In general, G(1) and S phase cyclins are ubiquitylated by the SCF, whereas ubiquitylation of mitotic cyclins is catalyzed by the APC/C. Here we show that fission yeast S phase cyclin Cig2 is ubiquitylated and degraded via both the SCF and the APC/C. Cig2 instability during G(2) and M phase is dependent upon the SCF complex, whereas the APC/C is responsible for Cig2 destruction during anaphase and G(1), thereby ensuring a spike pattern of Cig2 levels, peaking only at S phase. Two F-box/WD proteins Pop1 and Pop2, homologues of budding yeast Cdc4 and human Fbw7, are responsible for Cig2 instability. Pop1 binds Cig2 in vivo. An in vitro binding assay shows that an internal 93 amino acid residues comprising a part of the cyclin box are necessary and sufficient for this binding. Cig2 phosphorylation is also required for interaction with Pop1. We previously showed that transcriptional oscillation of cig2(+) requires Pop1 and Pop2 function. SCF(Pop1/Pop2) therefore regulates Cig2 levels in a dual manner, transcriptionally and post-translationally. Our results also highlight a collaborative action of the APC/C and the SCF toward the common substrate Cig2. This type of composite degradation control may be more general as the regulatory mechanism in other complex systems.","authors":"Yamano H, Kominami K, Harrison C, Kitamura K, Katayama S, Dhut S, Hunt T, Toda T","authors_abbrev":"Yamano H et al.","pubmed_publication_date":"30 Apr 2004","pubmed_entrez_date":"2004-02-19","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1718.01","SPAPB2B4.03","SPBC14C8.07c","SPAC4D7.03","SPBC32F12.09"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:15126629","title":"Suppression of a mitotic mutant by tRNA-Ala anticodon mutations that produce a dominant defect in late mitosis.","citation":"J Cell Sci 2004 May 01;117(Pt 11):2283-93","abstract":"Cold-sensitive dominant mutants scn1 and scn2 of Schizosaccharomyces pombe were isolated by their ability to suppress temperature-sensitive cut9-665 defective in an essential subunit (human Apc6/budding yeast Cdc16 ortholog) of anaphase promoting complex/cyclosome (APC/C). APC/C mutants were defective in metaphase/anaphase transition, whereas single scn mutants showed the delay in anaphase spindle elongation at 20 degrees C. The scn mutants lost viability because of chromosome missegregation, and were sensitive to a tubulin poison. To understand the scn phenotypes, mutant genes were identified. Surprisingly, scn1 and scn2 have the same substitution in the anticodon of two different tRNA-Ala (UGC) genes. UGC was altered to UGU so that the binding of the tRNA-Ala to the ACA Thr codon in mRNA became possible. As cut9-665 contained an Ala535Thr substitution, wild-type Cut9 protein was probably produced in scn mutants. Indeed, plasmid carrying tRNA-Ala (UGU) conferred cold-sensitivity to wild-type and suppressed cut9-665 in a dominant fashion. The previously identified scn1(+) (renamed as scn3(+)) turned out to be a high copy suppressor for scn1 and scn2. These are the first tRNA mutants that cause a mitotic defect.","authors":"Kimata Y, Yanagida M","authors_abbrev":"Kimata Y et al.","pubmed_publication_date":"01 May 2004","pubmed_entrez_date":"2004-05-06","publication_year":"2004","canto_session_key":"d51f6cb3611bc670","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-05-15 14:24:23","canto_approved_date":"2022-02-02 17:59:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-15 14:24:12","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25B2.05","SPAC688.13","SPCTRNATHR.10","SPBC26H8.07c","SPATRNAALA.02","SPATRNAALA.03","SPBTRNATHR.06","SPAC6F12.15c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2014-05-15"},{"uniquename":"PMID:18242152","title":"Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts.","citation":"DNA Repair (Amst) 2008 Mar 01;7(3):439-51","abstract":"Eukaryotes are endowed with multiple specialized DNA polymerases, some (if not all) of which are believed to play important roles in the tolerance of base damage during DNA replication. Among these DNA polymerases, Rev1 protein (a deoxycytidyl transferase) from vertebrates interacts with several other specialized polymerases via a highly conserved C-terminal region. The present studies assessed whether these interactions are retained in more experimentally tractable model systems, including yeasts, flies, and the nematode C. elegans. We observed a physical interaction between Rev1 protein and other Y-family polymerases in the fruit fly Drosophila melanogaster. However, despite the fact that the C-terminal region of Drosophila and yeast Rev1 are conserved from vertebrates to a similar extent, such interactions were not observed in Saccharomyces cerevisiae or Schizosaccharomyces pombe. With respect to regions in specialized DNA polymerases that are required for interaction with Rev1, we find predicted disorder to be an underlying structural commonality. The results of this study suggest that special consideration should be exercised when making mechanistic extrapolations regarding translesion DNA synthesis from one eukaryotic system to another.","doi":"10.1016/j.dnarep.2007.11.016","authors":"Kosarek JN, Woodruff RV, Rivera-Begeman A, Guo C, D'Souza S, Koonin EV, Walker GC, Friedberg EC","authors_abbrev":"Kosarek JN et al.","pubmed_publication_date":"01 Mar 2008","pubmed_entrez_date":"2008-02-05","publication_year":"2008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12D12.09","SPBC1347.01c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12045216","title":"From Cdc2 to Cdk1: when did the cell cycle kinase join its cyclin partner?","citation":"J Cell Sci 2002 Jun 15;115(Pt 12):2461-4","abstract":"The idea that Cdc2 and cyclins play a key role in the control of the G2/M transition of the cell cycle came largely from genetic analysis of fission yeast and physiological studies of clam, frog, sea urchin and starfish eggs and oocytes. However, it took a long time to realise that Cdc2 and cyclins form a stoichiometric complex and that a cyclin subunit is necessary for the Cdc2 subunit to gain its protein kinase activity. Cyclins were first recognized as proteins whose abundance oscillates during the early cell cycles of marine invertebrate eggs and their connection with MPF (maturation-promoting factor), the entity defined in frog and starfish oocytes whose activity controls entry into M phase, was far from clear at first. Indeed, it was a long time before MPF was shown to be a protein kinase, and direct proof that MPF is a heterodimer comprising one molecule of cyclin and one molecule of Cdc2 was finally obtained only when the Cdc2-associated component of purified starfish MPF was sequenced and found to be cyclin B. When this fundamental discovery was confirmed in vertebrates and mammalian members of the Cdc2 family were also shown to bind cyclins, Cdc2 became Cdk1, the first cyclin-dependent protein kinase.","authors":"Dorée M, Hunt T","authors_abbrev":"Dorée M et al.","pubmed_publication_date":"15 Jun 2002","pubmed_entrez_date":"2002-06-05","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9034326","title":"Mitochondrial DNA polymerases from yeast to man: a new family of polymerases.","citation":"Gene 1997 Jan 31;185(1):147-52","abstract":"We report the sequence of a 4.5-kb cDNA clone isolated from a human melanoma library which bears high amino acid sequence identity to the yeast mitochondrial (mt) DNA polymerase (Mip1p). This cDNA contains a 3720-bp open reading frame encoding a predicted 140-kDa polypeptide that is 43% identical to Mip1p. The N-terminal part of the sequence contains a 13 glutamine stretch encoded by a CAG trinucleotide repeat which is not found in the other DNA polymerases gamma (Pol gamma). Multiple amino acid sequence alignments with Pol gamma from Saccharomyces cerevisiae, Schizosaccharomyces pombe, Pichia pastoris, Drosophila melanogaster, Xenopus laevis and Mus musculus show that these DNA polymerases form a family strongly conserved from yeast to man and are only loosely related to the Family A DNA polymerases.","authors":"Lecrenier N, Van Der Bruggen P, Foury F","authors_abbrev":"Lecrenier N et al.","pubmed_publication_date":"31 Jan 1997","pubmed_entrez_date":"1997-01-31","publication_year":"1997","canto_session_key":"a8550e1925592843","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-20 15:56:22","canto_approved_date":"2019-11-20 15:56:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-20 15:56:14","canto_added_date":"2012-02-24 05:53:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.22"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-11-20"},{"uniquename":"EMBL:SPD89231","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23893486","title":"Integration profiling of gene function with dense maps of transposon integration.","citation":"Genetics 2013 Oct;195(2):599-609","abstract":"Understanding how complex networks of genes integrate to produce dividing cells is an important goal that is limited by the difficulty in defining the function of individual genes. Current resources for the systematic identification of gene function such as siRNA libraries and collections of deletion strains are costly and organism specific. We describe here integration profiling, a novel approach to identify the function of eukaryotic genes based upon dense maps of transposon integration. As a proof of concept, we used the transposon Hermes to generate a library of 360,513 insertions in the genome of Schizosaccharomyces pombe. On average, we obtained one insertion for every 29 bp of the genome. Hermes integrated more often into nucleosome free sites and 33% of the insertions occurred in ORFs. We found that ORFs with low integration densities successfully identified the genes that are essential for cell division. Importantly, the nonessential ORFs with intermediate levels of insertion correlated with the nonessential genes that have functions required for colonies to reach full size. This finding indicates that integration profiles can measure the contribution of nonessential genes to cell division. While integration profiling succeeded in identifying genes necessary for propagation, it also has the potential to identify genes important for many other functions such as DNA repair, stress response, and meiosis.","doi":"10.1534/genetics.113.152744","authors":"Guo Y, Park JM, Cui B, Humes E, Gangadharan S, Hung S, FitzGerald PC, Hoe KL, Grewal SI, Craig NL, Levin HL","authors_abbrev":"Guo Y et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-07-30","publication_year":"2013","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7723827","title":"A kinase from fission yeast responsible for blocking mitosis in S phase.","citation":"Nature 1995 Apr 27;374(6525):817-9","abstract":"In virtually all eukaryotes, mitosis starts after the completion of DNA synthesis. This orderly process is ensured by the checkpoint mechanism that blocks the onset of mitosis while DNA is being synthesized or is damaged. In the fission yeast Schizosaccharomyces pombe, this mechanism involves some rad+ and hus+ genes. However, it is not known how the checkpoint system monitors these events. Recently a multicopy suppressor of a temperature-sensitive DNA polymerase-alpha mutant was isolated. This gene, named cds1+ (checking DNA synthesis), encodes a typical protein kinase. Here we report that this protein kinase is a key component of the DNA replication-monitoring S/G2 checkpoint system. Our data suggest that its primary role is to monitor DNA synthesis by interacting with DNA polymerase alpha and send a signal to block the onset of mitosis while DNA synthesis is in progress.","authors":"Murakami H, Okayama H","authors_abbrev":"Murakami H et al.","pubmed_publication_date":"27 Apr 1995","pubmed_entrez_date":"1995-04-27","publication_year":"1995","canto_session_key":"be17835283cd3a90","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-29 15:27:57","canto_approved_date":"2021-01-06 15:53:16","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-09-29 15:25:06","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC1F7.05","SPAC1952.07","SPAC3H5.06c","SPCC18B5.11c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-09-29"},{"uniquename":"PMID:7812047","title":"Inhibition of G2/M progression in Schizosaccharomyces pombe by a mutant calmodulin kinase II with constitutive activity.","citation":"Mol Biol Cell 1994 Jul;5(7):785-95","abstract":"Intracellular signaling by the second messenger Ca2+ through its receptor calmodulin (CaM) regulates cell function via the activation of CaM-dependent enzymes. Previous studies have shown that cell cycle progression at G1/S and G2/M is sensitive to intracellular CaM levels. However, little is known about the CaM-regulated enzymes involved. Protein phosphorylation has been shown to be important for cell-cycle regulation. Because CaM regulates several protein kinases, and at least one protein phosphatase, our studies are focusing on the roles of these enzymes within the cell cycle. As an initial approach to this problem, cDNAs encoding either normal or mutant calcium/calmodulin kinase II (CaMKII) have been expressed in Schizosaccharomyces pombe. The results show that overexpression of a constitutively active mutant CaMKII caused cell-cycle arrest in G2. Arrest was associated with a failure to activate the p34/cdc2 protein kinase. Expression of the mutant CaMKII in strains of S. pombe with altered timing of mitosis revealed that this effect is not mediated either by cdc25+ or wee1+, suggesting that CaMKII may regulate G2/M progression by another mechanism.","authors":"Rasmussen C, Rasmussen G","authors_abbrev":"Rasmussen C et al.","pubmed_publication_date":"Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_session_key":"20fca8dd4c242ca2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-01-07 20:22:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-07 20:19:42","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-01-07"},{"uniquename":"PMID:23697806","title":"A genome-wide resource of cell cycle and cell shape genes of fission yeast.","citation":"Open Biol 2013 May 22;3(5):130053","abstract":"To identify near complete sets of genes required for the cell cycle and cell shape, we have visually screened a genome-wide gene deletion library of 4843 fission yeast deletion mutants (95.7% of total protein encoding genes) for their effects on these processes. A total of 513 genes have been identified as being required for cell cycle progression, 276 of which have not been previously described as cell cycle genes. Deletions of a further 333 genes lead to specific alterations in cell shape and another 524 genes result in generally misshapen cells. Here, we provide the first eukaryotic resource of gene deletions, which describes a near genome-wide set of genes required for the cell cycle and cell shape.","doi":"10.1098/rsob.130053","authors":"Hayles J, Wood V, Jeffery L, Hoe KL, Kim DU, Park HO, Salas-Pino S, Heichinger C, Nurse P","authors_abbrev":"Hayles J et al.","pubmed_publication_date":"22 May 2013","pubmed_entrez_date":"2013-05-24","publication_year":"2013","canto_session_key":"92f886cfd47bd5e7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-06-30 10:31:29","canto_approved_date":"2023-11-16 17:33:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-30 10:29:54","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"file_curator_name":"Valerie Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11245,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_23697806_phaf.tsv"}],"genes":["SPAP19A11.05c","SPAC19G12.16c","SPBP4G3.02","SPAC1556.05c","SPBC14F5.09c","SPBC16G5.07c","SPCC830.10","SPCC70.09c","SPBP8B7.12c","SPCPB1C11.01","SPBC23E6.07c","SPAC22A12.01c","SPAC1834.04","SPBC83.08","SPAC13G7.13c","SPCC1223.04c","SPAPJ698.03c","SPAC186.06","SPCC1672.12c","SPBC14C8.11c","SPBC3D6.08c","SPCC1442.01","SPCC16C4.14c","SPAC22F3.08c","SPBC146.05c","SPCC18B5.06","SPBC1198.05","SPAC17C9.03","SPBC4F6.10","SPBC1778.07","SPBC106.18","SPBC9B6.08","SPBC27B12.02","SPCC24B10.02c","SPAC222.04c","SPBC18H10.15","SPBC839.02","SPBC887.17","SPAC29A4.04c","SPBC211.07c","SPBC8D2.18c","SPAC2E12.03c","SPBC11B10.09","SPCC16C4.05","SPAC31A2.09c","SPCC1919.03c","SPBC19C2.15c","SPBC29A10.05","SPAC3H1.08c","SPAC222.13c","SPCC1450.06c","SPCC1919.09","SPAC637.07","SPBC582.07c","SPAC637.08","SPAC343.08c","SPBC26H8.05c","SPAC4G9.03","SPAC19G12.10c","SPAC12B10.11","SPAC15A10.06","SPBC25H2.03","SPAC1610.04","SPAC24H6.03","SPBPJ4664.04","SPBC660.07","SPAC9G1.13c","SPCC1795.01c","SPBC337.10c","SPAC1002.02","SPAC30D11.06c","SPBC146.06c","SPBC24C6.11","SPBC1773.04","SPCC553.08c","SPBC713.07c","SPBC557.05","SPBC1289.03c","SPBC646.05c","SPBC211.03c","SPAC1556.07","SPAC26A3.16","SPCC14G10.02","SPBC405.06","SPAC637.13c","SPBC1105.13c","SPAC12G12.09","SPAC23A1.18c","SPBC16C6.08c","SPAC19D5.07","SPAC13G6.07c","SPAC17G8.13c","SPAC4H3.14c","SPAC24H6.02c","SPBC947.10","SPAPB17E12.09","SPAC9E9.13","SPAC2C4.11c","SPBC21C3.08c","SPAC1635.01","SPAC2F3.17c","SPBC428.19c","SPBC1348.04","SPAC22A12.11","SPBC16G5.05c","SPAC17D4.02","SPBC1604.10","SPAC29B12.06c","SPAC1D4.01","SPBC409.12c","SPCC1223.01","SPBC646.15c","SPAC328.06","SPAC4F10.05c","SPAC13G6.05c","SPAC6G10.02c","SPAC4F10.14c","SPBC216.07c","SPAC12G12.10","SPAC31G5.05c","SPAC16E8.06c","SPAC10F6.01c","SPBC25B2.06c","SPBC839.11c","SPAC222.09","SPAC3F10.17","SPBC1773.12","SPBC29A10.02","SPAC12G12.11c","SPBC25B2.07c","SPAC644.07","SPAPYUK71.03c","SPBPB21E7.05","SPAC17A2.04c","SPAC1B3.10c","SPBC9B6.10","SPBC1778.09","SPBC725.02","SPAP14E8.04","SPBC839.09c","SPCC1442.08c","SPAC1952.03","SPAC26F1.07","SPBC1773.05c","SPCC1742.01","SPAC29B12.13","SPAPB1E7.03","SPAC977.09c","SPBC115.03","SPAC16E8.16","SPBC530.11c","SPBC2G5.07c","SPAC56E4.04c","SPAC23G3.10c","SPAC31A2.16","SPBC21.04","SPCC24B10.19c","SPAC25A8.03c","SPCC4E9.02","SPBC16D10.03","SPCC330.09","SPBP4H10.14c","SPAC1834.03c","SPBC32H8.11","SPCC1795.12c","SPBC26H8.02c","SPBC25B2.11","SPCC584.01c","SPAC823.04","SPAC4F10.20","SPBC1539.10","SPBC1685.11","SPAC26H5.12","SPBC3F6.03","SPCC285.11","SPAC2F7.10","SPAC10F6.13c","SPBC23G7.05","SPAC1952.11c","SPAC23H4.16c","SPBC36.11","SPAC2E1P5.04c","SPAC25B8.01","SPBC8D2.19","SPCC16A11.10c","SPCC320.12","SPBC776.08c","SPCC306.02c","SPBC2F12.12c","SPCC18.17c","SPBC1703.15c","SPCC1906.02c","SPCC794.04c","SPAC23H3.09c","SPCC663.08c","SPBC2D10.08c","SPAC25B8.11","SPBC83.19c","SPCC1450.11c","SPCC18.11c","SPBC211.02c","SPAPJ760.03c","SPCC1494.08c","SPCC663.14c","SPBC30D10.16","SPBPB2B2.19c","SPBC1685.04","SPCC285.13c","SPAC23C4.03","SPCC895.05","SPAPJ695.01c","SPAC2G11.03c","SPBC14C8.02","SPBC582.05c","SPBC23E6.02","SPAC30D11.02c","SPCC1682.16","SPCC4G3.04c","SPBC16E9.12c","SPAC12G12.01c","SPBC685.06","SPCC364.07","SPBC4B4.10c","SPAC1142.07c","SPCC736.02","SPAC31A2.02","SPBC25B2.09c","SPBC32H8.07","SPAC3A11.08","SPCC970.04c","SPAC10F6.04","SPAC23C4.07","SPAPB17E12.03","SPAC24H6.13","SPAC10F6.10","SPBC23G7.15c","SPCC1442.14c","SPCC1672.11c","SPBC354.01","SPAC688.09","SPCC320.07c","SPCC794.03","SPCC13B11.04c","SPBC13E7.02","SPBC582.03","SPAC1687.22c","SPAPB24D3.01","SPAC19G12.14","SPCPB16A4.06c","SPBC1683.06c","SPBP19A11.06","SPAC15E1.10","SPAC6G9.09c","SPAC22H10.07","SPAPB1A10.07c","SPBPB2B2.16c","SPAC323.01c","SPCC1494.02c","SPAC11H11.06","SPAC23D3.01","SPAC26A3.05","SPBC30B4.07c","SPBP4G3.03","SPAC19B12.07c","SPBC16E9.17c","SPBP4H10.19c","SPAC17C9.14","SPAC890.08","SPAC1687.01","SPAC21E11.06","SPAC9.13c","SPCC1450.08c","SPBC83.16c","SPCC70.02c","SPBC30D10.12c","SPCC1020.06c","SPAC23H4.02","SPBC1A4.07c","SPAC29B12.07","SPAC14C4.01c","SPAC890.02c","SPBC1604.03c","SPAC18G6.13","SPAC1783.07c","SPBC2G2.15c","SPAC2F7.13c","SPCC1235.10c","SPCC757.07c","SPCC1450.07c","SPAC637.04","SPAC926.03","SPAC1002.10c","SPBC336.12c","SPBC56F2.03","SPAC23H4.06","SPBC800.03","SPBC21H7.02","SPBC17G9.11c","SPAC23H4.12","SPCC1259.07","SPAC343.10","SPBC19G7.13","SPAC631.01c","SPCC1840.01c","SPBC16A3.04","SPCC1322.07c","SPAC1782.05","SPAC823.03","SPAC3H5.09c","SPAC17G6.07c","SPAPB24D3.04c","SPBC17A3.04c","SPBC2G2.04c","SPBC3B9.14c","SPAC1527.02","SPAC1006.06","SPAC2H10.02c","SPAC14C4.02c","SPAC22A12.03c","SPAC1071.10c","SPAC6B12.10c","SPBC342.06c","SPAC821.10c","SPAC23H3.08c","SPBP8B7.31","SPAC27F1.05c","SPCC663.09c","SPAC2G11.02","SPAC664.10","SPBC18E5.11c","SPBC3H7.03c","SPAC17H9.13c","SPBC211.06","SPCC584.02","SPBC1711.03","SPAC513.06c","SPBC1105.12","SPCC16A11.01","SPBC725.13c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determining the functional distinction of the fission yeast cell cycle \"start\" molecules Res1 and Res2.","citation":"Mol Biol Cell 1996 Dec;7(12):1967-76","abstract":"In Schizosaccharomyces pombe the \"start\" of the cell cycle is regulated by two parallel, functionally overlapping complexes composed of Res1-Cdc10 and Res2-Cdc10. Res1 and Res2 are structurally very homologous and are required for the start of the mitotic and meiotic cycle, respectively. We have addressed the question which parts of the proteins are essential for function and determine the functional specificity. Several discrete domains in the nonconserved C-terminal region are essential for the mitotic and meiotic start function and determine the functional specificity independently of the structurally conserved motifs at the N-terminal end and in the center. One of these domains in Res2 restricts Res2 to interact only with Rep2. Res2 without this domain behaves like a functional chimera having the properties of Res2 and Res1. Likewise, internally truncated forms of Res1 lacking the centrally located ankyrin repeats and adjacent sequences can partially suppress the meiotic defect in res2- cells. These truncated Res1 molecules behave like functional chimeras with the properties of Res1 and Res2.","authors":"Sturm S, Okayama H","authors_abbrev":"Sturm S et al.","pubmed_publication_date":"Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC725.16","SPBC2F12.11c","SPAC22F3.09c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"Pfam:PF15458","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A2.08c","YKR022C"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38534780","title":"Effects of  rpl1001  Gene Deletion on Cell Division of Fission Yeast and Its Molecular Mechanism.","citation":"Curr Issues Mol Biol 2024 Mar 18;46(3):2576-2597","abstract":"The  rpl1001  gene encodes 60S ribosomal protein L10, which is involved in intracellular protein synthesis and cell growth. However, it is not yet known whether it is involved in the regulation of cell mitosis dynamics. This study focuses on the growth, spore production, cell morphology, the dynamics of microtubules, chromosomes, actin, myosin, and mitochondria of fission yeast ( Schizosaccharomyces pombe ) to investigate the impact of  rpl1001  deletion on cell mitosis. RNA-Seq and bioinformatics analyses were also used to reveal key genes, such as  hsp16 ,  mfm1  and  isp3 , and proteasome pathways. The results showed that  rpl1001  deletion resulted in slow cell growth, abnormal spore production, altered cell morphology, and abnormal microtubule number and length during interphase. The cell dynamics of the  rpl1001Δ  strain showed that the formation of a monopolar spindle leads to abnormal chromosome segregation with increased rate of spindle elongation in anaphase of mitosis, decreased total time of division, prolonged formation time of actin and myosin loops, and increased expression of mitochondrial proteins. Analysis of the RNA-Seq sequencing results showed that the proteasome pathway, up-regulation of  isp3 , and down-regulation of  mfm1  and  mfm2  in the  rpl1001Δ  strain were the main factors underpinning the increased number of spore production. Also, in the  rpl1001Δ  strain, down-regulation of  dis1  caused the abnormal microtubule and chromosome dynamics, and down-regulation of  hsp16  and  pgk1  were the key genes affecting the delay of actin ring and myosin ring formation. This study reveals the effect and molecular mechanism of  rpl1001  gene deletion on cell division, which provides the scientific basis for further clarifying the function of the Rpl1001 protein in cell division.","doi":"10.3390/cimb46030164","authors":"Yu W, Yuan R, Liu M, Liu K, Ding X, Hou Y","authors_abbrev":"Yu W et al.","pubmed_publication_date":"18 Mar 2024","pubmed_entrez_date":"2024-03-27","publication_year":"2024","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-28 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19819763","title":"Mms1-Mms22 complex protects genome integrity in Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2009 Dec 03;8(12):1390-9","abstract":"Mms1 and Mms22 are subunits of an Rtt101-based E3 ubiquitin ligase required for replication of damaged DNA templates in Saccharomyces cerevisiae. The function and evolutionary conservation of this DNA repair module are unknown. Here we report the characterization of an Mms1 ortholog in Schizosaccharomyces pombe. Fission yeast Mms1 was discovered through its physical association with S. pombe Mms22 (also known as Mus7). Loss of S. pombe Mms1 results in the accumulation of spontaneous DNA damage, mitotic delay, and hypersensitivity to genotoxins such as camptothecin that perturb replisome progression. Homologous recombination repair proteins Rhp51 and Rad22 (Rad51 and Rad52 orthologs, respectively) are critical for survival in the absence of Mms1; however, there is no such requirement for Mus81-Eme1 Holliday junction resolvase that is essential for recovery from broken replication forks. Mms1 and Mms22 mutants share similar phenotypes and are genetically epistatic under unperturbed growth conditions and following exposure to genotoxins. From these data we conclude that an evolutionary conserved Mms1-Mms22 complex is required for replication of damaged DNA in fission yeast.","doi":"10.1016/j.dnarep.2009.09.008","authors":"Dovey CL, Aslanian A, Sofueva S, Yates JR, Russell P","authors_abbrev":"Dovey CL et al.","pubmed_publication_date":"03 Dec 2009","pubmed_entrez_date":"2009-10-13","publication_year":"2009","canto_session_key":"3c220139c7579fa2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_approved_date":"2018-07-19 10:45:29","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-03-27 21:30:47","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6B12.02c","SPCC1259.13","SPAC3H8.05c","SPCC18B5.11c","SPCC4G3.05c","SPAC30D11.10","SPAC2G11.12","SPAC644.14c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-03-27"},{"uniquename":"PMID:17304213","title":"Genome-wide localization of pre-RC sites and identification of replication origins in fission yeast.","citation":"EMBO J 2007 Mar 07;26(5):1327-39","abstract":"DNA replication of eukaryotic chromosomes initiates at a number of discrete loci, called replication origins. Distribution and regulation of origins are important for complete duplication of the genome. Here, we determined locations of Orc1 and Mcm6, components of pre-replicative complex (pre-RC), on the whole genome of Schizosaccharomyces pombe using a high-resolution tiling array. Pre-RC sites were identified in 460 intergenic regions, where Orc1 and Mcm6 colocalized. By mapping of 5-bromo-2'-deoxyuridine (BrdU)-incorporated DNA in the presence of hydroxyurea (HU), 307 pre-RC sites were identified as early-firing origins. In contrast, 153 pre-RC sites without BrdU incorporation were considered to be late and/or inefficient origins. Inactivation of replication checkpoint by Cds1 deletion resulted in BrdU incorporation with HU specifically at the late origins. Early and late origins tend to distribute separately in large chromosome regions. Interestingly, pericentromeric heterochromatin and the silent mating-type locus replicated in the presence of HU, whereas the inner centromere or subtelomeric heterochromatin did not. Notably, MCM did not bind to inner centromeres where origin recognition complex was located. Thus, replication is differentially regulated in chromosome domains.","authors":"Hayashi M, Katou Y, Itoh T, Tazumi A, Yamada Y, Takahashi T, Nakagawa T, Shirahige K, Masukata H","authors_abbrev":"Hayashi M et al.","pubmed_publication_date":"07 Mar 2007","pubmed_entrez_date":"2007-02-17","publication_year":"2007","canto_session_key":"81273ae262ec56f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-08-28 13:36:25","canto_approved_date":"2019-08-28 13:36:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-08-28 13:36:19","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.15","SPCC18B5.11c","SPBC211.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-08-28"},{"uniquename":"PMID:10200602","title":"[Molecular functions of cofilin which regulates reorganization of actin cytoskeleton].","citation":"Seikagaku 1999 Feb;71(2):101-14","abstract":"","authors":"Moriyama K, Aizawa H, Iida K, Yahara I","authors_abbrev":"Moriyama K et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-04-14","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25733668","title":"Shu1 is a cell-surface protein involved in iron acquisition from heme in Schizosaccharomyces pombe.","citation":"J Biol Chem 2015 Apr 17;290(16):10176-90","abstract":"Iron is an essential metal cofactor that is required for many biological processes. Eukaryotic cells have consequently developed different strategies for its acquisition. Until now, Schizosaccharomyces pombe was known to use reductive iron uptake and siderophore-bound iron transport to scavenge iron from the environment. Here, we report the identification of a gene designated shu1(+) that encodes a protein that enables S. pombe to take up extracellular heme for cell growth. When iron levels are low, the transcription of shu1(+) is induced, although its expression is repressed when iron levels rise. The iron-dependent down-regulation of shu1(+) requires the GATA-type transcriptional repressor Fep1, which strongly associates with a proximal promoter region of shu1(+) in vivo in response to iron repletion. HA4-tagged Shu1 localizes to the plasma membrane in cells expressing a functional shu1(+)-HA4 allele. When heme biosynthesis is selectively blocked in mutated S. pombe cells, their ability to acquire exogenous hemin or the fluorescent heme analog zinc mesoporphyrin IX is dependent on the expression of Shu1. Further analysis by absorbance spectroscopy and hemin-agarose pulldown assays showed that Shu1 interacts with hemin, with a KD of ∼2.2 μm. Taken together, results reported here revealed that S. pombe possesses an unexpected pathway for heme assimilation, which may also serve as a source of iron for cell growth.","doi":"10.1074/jbc.M115.642058","authors":"Mourer T, Jacques JF, Brault A, Bisaillon M, Labbé S","authors_abbrev":"Mourer T et al.","pubmed_publication_date":"17 Apr 2015","pubmed_entrez_date":"2015-03-04","publication_year":"2015","canto_session_key":"d17a6f8397b4b058","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-28 21:40:12","canto_approved_date":"2024-06-22 12:23:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-15 09:50:02","canto_added_date":"2015-03-05 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.07c","SPAC2F3.09","SPAC23E2.01","SPAC1F7.08","SPAC1142.05","SPAC1F8.02c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-01-28"},{"uniquename":"PMID:41445307","title":"The Power of Yeast.","citation":"Yeast 2025 Dec;42(12):303-310","abstract":"Yeasts have been intimately connected with human civilization for millennia, originally used for fermentation in food and beverage production. This article explores the multifaceted roles of yeasts-particularly Saccharomyces cerevisiae-as both a model organism and a cell factory. The historical journey of yeast research is chronicled from early fermentation practices to its central role in the molecular biology revolution. Notable discoveries using yeast have led to numerous Nobel Prizes, demonstrating its power in elucidating fundamental biological processes such as the eukaryal cell cycle, protein trafficking, transcription, and autophagy. The deep conservation of cellular pathways between yeast and humans, such as AMPK/Snf1 and TORC1/Tor1 signaling, further underscores yeast's value in biomedical research. Beyond its use in basic science, S. cerevisiae has become a preferred host for industrial biotechnology due to its genetic tractability, safety status, and ability to scale fermentation processes. Yeast has been engineered to produce a broad range of chemicals, fuels, and pharmaceuticals. Advanced tools in metabolic engineering-including genome-scale metabolic models, multi-omics analyses, and adaptive laboratory evolution-have driven remarkable improvements in yield, productivity, and strain robustness. These tools also offer insights into fundamental metabolic regulation and cellular adaptation. As the article discusses, yeast has not only illuminated the molecular workings of eukaryal life but also transformed industrial biotechnology. Its legacy and continued evolution affirm its indispensable role in science and technology.","doi":"10.1002/yea.70009","authors":"Nielsen J","authors_abbrev":"Nielsen J","pubmed_publication_date":"Dec 2025","pubmed_entrez_date":"2025-12-25","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-12-26 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41729970","title":"The RPA-binding domain and the KKRK motif in Rad26ATRIP cooperate at the perturbed DNA replication fork for initiating checkpoint signalling.","citation":"PLoS Genet 2026 Feb 23;22(2):e1012052","abstract":"Rad26 is the homolog of human ATRIP and budding yeast Ddc2 in Schizosaccharomyces pombe. Like ATRIP and Ddc2, Rad26 works with Rad3ATR/Mec1 to initiate checkpoint signalling in response to perturbed DNA replication and various types of DNA damage. To better understand the checkpoint initiation mechanism in fission yeast, we carried out genetic and biochemical analyses on the N-terminus of Rad26. Although Rad26 homologs do not share much sequence similarity, we demonstrate that, like ATRIP and Ddc2, Rad26 possesses a replication protein A (RPA) binding domain (RBD) in its N-terminus, suggesting a highly conserved mechanism. Elimination of the RBD in Rad26, however, only moderately affects the checkpoint signalling and cellular resistance to genotoxins. Rad26 has a short KKRK sequence in the N-terminal region, a motif conserved in Ddc2 that binds DNA and is crucial for the checkpoint function in budding yeast. Mutations of this motif in Rad26 cause only a minor defect in the checkpoint. However, simultaneous mutations of the RBD and the KKRK motif nearly eliminate the Rad3ATR kinase signalling at the perturbed replication fork. This suggests that the two functional units of Rad26 cooperate to initiate the DNA replication checkpoint. On the contrary, the simultaneous mutations of Rad26 only moderately or minimally sensitize the cell to different types of DNA damage. We hypothesize that the checkpoint initiation at the DNA damage site in fission yeast may follow a different mechanism that depends less on the two functional units of Rad26.","doi":"10.1371/journal.pgen.1012052","authors":"Xu YJ, Gao A, Dev K, Zheng Y, Alyahya MY, Pasam S, Kaur G, Zhou C","authors_abbrev":"Xu YJ et al.","pubmed_publication_date":"23 Feb 2026","pubmed_entrez_date":"2026-02-23","publication_year":"2026","canto_session_key":"5e99a1452ceb5cf9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yongjie Xu","canto_first_approved_date":"2026-04-16 06:13:54","canto_approved_date":"2026-04-16 06:13:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-04-04 21:48:23","canto_added_date":"2026-02-24 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":109,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Yongjie Xu","community_curator":true,"annotation_count":37,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.08","SPCC1259.13","SPBC660.13c","SPAC694.06c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2026-04-16"},{"uniquename":"PMID:26340438","title":"Regulation of contractile ring formation and septation in Schizosaccharomyces pombe.","citation":"Curr Opin Microbiol 2015 Dec;28:46-52","abstract":"The fission yeast Schizosaccharomyces pombe has become a powerful model organism for cytokinesis studies, propelled by pioneering genetic screens in the 1980s and 1990s. S. pombe cells are rod-shaped and divide similarly to mammalian cells, utilizing a medially-placed actin-and myosin-based contractile ring. A cell wall division septum is deposited behind the constricting ring, forming the new ends of each daughter cell. Here we discuss recent advances in our understanding of the regulation of contractile ring formation through formin proteins and the role of the division septum in S. pombe cell division.","doi":"10.1016/j.mib.2015.08.001","authors":"Willet AH, McDonald NA, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-09-05","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-09-06 00:19:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24003116","title":"Zinc finger protein Loz1 is required for zinc-responsive regulation of gene expression in fission yeast.","citation":"Proc Natl Acad Sci U S A 2013 Sep 17;110(38):15371-6","abstract":"In Schizosaccharomyces pombe, alcohol dehydrogenase 1 (Adh1) is an abundant zinc-requiring enzyme that catalyses the conversion of acetaldehyde to ethanol during fermentation. In a zinc-replete cell, adh1 is highly expressed. However, in zinc-limited cells, adh1 gene expression is repressed, and cells induce the expression of an alternative alcohol dehydrogenase encoded by the adh4 gene. In our studies examining this zinc-dependent switch in alcohol dehydrogenase gene expression, we isolated an adh1Δ strain containing a partial loss of function mutation that resulted in higher levels of adh4 transcripts in zinc-replete cells. This mutation also led to the aberrant expression of other genes that are typically regulated by zinc. Using linkage analysis, we have mapped the position of this mutation to a single gene called Loss Of Zinc sensing 1 (loz1). Loz1 is a 55-kDa protein that contains a double C2H2-type zinc finger domain. The mapped mutation that disrupts Loz1 function leads to an arginine to glycine substitution in the second zinc finger domain, suggesting that the double zinc finger domain is important for Loz1 function. We show that loz1Δ cells hyperaccumulate zinc and that Loz1 is required for gene repression in zinc-replete cells. We also have found that Loz1 negatively autoregulates its own expression. We propose that Loz1 is a unique metalloregulatory factor that plays a central role in zinc homeostasis in S. pombe.","doi":"10.1073/pnas.1300853110","authors":"Corkins ME, May M, Ehrensberger KM, Hu YM, Liu YH, Bloor SD, Jenkins B, Runge KW, Bird AJ","authors_abbrev":"Corkins ME et al.","pubmed_publication_date":"17 Sep 2013","pubmed_entrez_date":"2013-09-05","publication_year":"2013","canto_session_key":"7cec44eee583f82d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mark Corkins","canto_first_approved_date":"2018-01-12 15:45:05","canto_approved_date":"2024-01-11 21:35:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-30 18:48:34","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Mark Corkins","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC13B11.01","SPCC13B11.02c","SPBC16D10.06","SPAC25B8.19c","SPBC1348.06c","SPAC5H10.06c","SPAC22H10.13","SPAC977.05c","SPBPB2B2.15","SPNCRNA.1710"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2018-01-12"},{"uniquename":"EMBL:AB039861","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17937917","title":"Structural insight into AMPK regulation: ADP comes into play.","citation":"Structure 2007 Oct;15(10):1285-95","abstract":"The AMP-activated protein kinase (AMPK), a sensor of cellular energy status found in all eukaryotes, responds to changes in intracellular adenosine nucleotide levels resulting from metabolic stresses. Here we describe crystal structures of a heterotrimeric regulatory core fragment from Schizosaccharomyces pombe AMPK in complex with ADP, ADP/AMP, ADP/ATP, and 5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranotide (AICAR phosphate, or ZMP), a well-characterized AMPK activator. Prior crystallographic studies had revealed a single site in the gamma subunit that binds either ATP or AMP within Bateman domain B. Here we show that ZMP binds at this site, mimicking the binding of AMP. An analogous site in Bateman domain A selectively accommodates ADP, which binds in a distinct manner that also involves direct ligation to elements from the beta subunit. These observations suggest a possible role for ADP in regulating AMPK response to changes in cellular energy status.","authors":"Jin X, Townley R, Shapiro L","authors_abbrev":"Jin X et al.","pubmed_publication_date":"Oct 2007","pubmed_entrez_date":"2007-10-17","publication_year":"2007","canto_session_key":"262db1ff3a0a0b79","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-01 15:16:43","canto_approved_date":"2023-03-01 15:16:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-01 15:16:36","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.08c","SPCC74.03c","SPCC1919.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-03-01","pdb_entries":[{"pdb_id":"2qre","gene_chains":[{"gene_uniquename":"SPCC74.03c","chain":"A/C","position":"440-576"},{"gene_uniquename":"SPCC1919.03c","chain":"B/D","position":"203-298"},{"gene_uniquename":"SPAC1556.08c","chain":"E/G","position":"3-334"}],"title":"Crystal structure of the adenylate sensor from AMP-activated protein kinase in complex with 5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranotide (ZMP)","entry_authors":"Jin X,Townley R,Shapiro L","entry_authors_abbrev":"Jin X et al.","reference_uniquename":"PMID:17937917","experimental_method":"X-ray","resolution":"3.01"},{"pdb_id":"2qr1","gene_chains":[{"gene_uniquename":"SPCC74.03c","chain":"A/C","position":"440-576"},{"gene_uniquename":"SPCC1919.03c","chain":"B/D","position":"203-298"},{"gene_uniquename":"SPAC1556.08c","chain":"E/G","position":"3-334"}],"title":"Crystal structure of the adenylate sensor from AMP-activated protein kinase in complex with ADP","entry_authors":"Jin X,Townley R,Shapiro L","entry_authors_abbrev":"Jin X et al.","reference_uniquename":"PMID:17937917","experimental_method":"X-ray","resolution":"2.7"},{"pdb_id":"2qrd","gene_chains":[{"gene_uniquename":"SPCC74.03c","chain":"A/C","position":"440-576"},{"gene_uniquename":"SPCC1919.03c","chain":"B/D","position":"203-298"},{"gene_uniquename":"SPAC1556.08c","chain":"E/G","position":"3-334"}],"title":"Crystal Structure of the Adenylate Sensor from AMP-activated Protein Kinase in complex with ADP and ATP","entry_authors":"Jin X,Townley R,Shapiro L","entry_authors_abbrev":"Jin X et al.","reference_uniquename":"PMID:17937917","experimental_method":"X-ray","resolution":"2.41"},{"pdb_id":"2qrc","gene_chains":[{"gene_uniquename":"SPCC74.03c","chain":"A/C","position":"440-576"},{"gene_uniquename":"SPCC1919.03c","chain":"B/D","position":"203-298"},{"gene_uniquename":"SPAC1556.08c","chain":"E/G","position":"3-334"}],"title":"Crystal structure of the adenylate sensor from AMP-activated protein kinase in complex with ADP and AMP","entry_authors":"Jin X,Townley R,Shapiro L","entry_authors_abbrev":"Jin X et al.","reference_uniquename":"PMID:17937917","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:15601851","title":"Molecular and cellular dissection of mating-type switching steps in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2005 Jan;25(1):303-11","abstract":"A strand-specific imprint (break) controls mating-type switching in fission yeast. By introducing a thiamine repressible promoter upstream of the mat1 locus, we can force transcription through the imprinted region, erasing the imprint and inhibiting further mating-type switching, in a reversible manner. Starting from a synchronized, virgin M-cell population, we show that the site- and strand-specific break is formed when DNA replication intermediates appear at mat1 during the first S phase. The formation of the break is concomitant with a replication fork pause and binding of the Swi1 protein at mat1 until early G(2) and then rapidly disappears. Upon its formation, the break remains stable throughout the cell cycle and triggers mating-type switching during the second S phase. Finally, we have recreated the mating-type switching pedigree at the molecular and single-cell levels, allowing for the first time separation between the establishment of imprinting and its developmental fate.","authors":"Holmes AM, Kaykov A, Arcangioli B","authors_abbrev":"Holmes AM et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-12-17","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4044680","title":"Growth in cell length in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1985 Apr;75:357-76","abstract":"The cylindrical cells of Schizosaccharomyces pombe grow in length by extension at the ends and not the middle. At the beginning of the cell cycle, growth is restricted to the 'old end', which existed in the previous cycle. Later on, the 'new end', formed from the septum, starts to grow at a point in the cycle that we have called NETO ('new end take-off'). Fluorescence microscopy on cells stained with Calcofluor has been used to study NETO in size mutants, in blocked cdc mutants and with different growth temperatures and media. In wild-type cells (strain 972) NETO happens at 0.34 of the cycle with a cell length of 9.5 microns. With size mutants that are smaller at division, NETO takes place at the same size (9.0-9.5 microns) but this is not achieved until later in the cycle. Another control operates in larger size mutants since NETO occurs at the same stage of the cycle (about 0.32) as in wild type but at a larger cell size. This control is probably a requirement to have completed an event in early G2, since most cdc mutant cells blocked before this point in the cycle do not show NETO whereas most of those blocked in late G2 do show it. We conclude that NETO only happens if: (1) the cell length is greater than a critical value of 9.0-9.5 microns; and (2) the cell has traversed the first 0.3-0.35 of the cycle and passed early G2. NETO is delayed in poor media, in which cell size is also reduced. Temperature has little effect on NETO under steady-state conditions, but there is a transient delay for some hours after a temperature shift. NETO is later in another wild-type strain, 132. Time-lapse photomicrography was used to follow the rates of length growth in single cells. Wild-type cells showed two linear segments during the first 75% of the cycle. There was a rate-change point (RCP), coincident with NETO, where the rate of total length extension increased by 35%. This increase was not due simply to the start of new-end growth, since old-end growth slowed down in some cells at the RCP. cdc 11.123 is a mutant in which septation and division is blocked at 35 degrees C but nuclear division continues.(ABSTRACT TRUNCATED AT 400 WORDS)","authors":"Mitchison JM, Nurse P","authors_abbrev":"Mitchison JM et al.","pubmed_publication_date":"Apr 1985","pubmed_entrez_date":"1985-04-01","publication_year":"1985","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15383525","title":"Taz1 binding to a fission yeast model telomere: formation of telomeric loops and higher order structures.","citation":"J Biol Chem 2004 Dec 03;279(49):50764-72","abstract":"Similar to its human homologues TRF1 and TRF2, fission yeast Taz1 protein is a component of telomeric chromatin regulating proper telomere maintenance. As mammalian TRF1 and TRF2 proteins have been shown to directly bind telomeric DNA to form protein arrays and looped structures, termed t-loops, the ability of Taz1p to act on fission yeast telomeric DNA in similar ways was examined using purified protein and model DNA templates. When incubated with Taz1p, model telomeres containing 3' single-stranded telomeric overhangs formed t-loops at a frequency approaching 13%. Termini with blunt ends and non-telomeric overhangs were deficient in t-loop formation. In addition, we observed arrays of multiple Taz1p molecules bound to the telomeric regions, resembling the pattern of TRF1 binding. The presence of t-loops larger than the telomeric tract, a high frequency of end-bound DNAs and a donut shape of the Taz1p complex suggest that Taz1p binds the 3' overhang then extrudes a loop that grows in size as the donut slides along the duplex DNA. Based on these in vitro results we discuss possible general implications for fission yeast telomere dynamics.","authors":"Tomaska L, Willcox S, Slezakova J, Nosek J, Griffith JD","authors_abbrev":"Tomaska L et al.","pubmed_publication_date":"03 Dec 2004","pubmed_entrez_date":"2004-09-24","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.07c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:22247558","title":"Role of Cdc14 in timing the end of cell division: Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine.","citation":"J Biol Chem 2012 Jan 13;287(3):1670","abstract":"","doi":"10.1074/jbc.P111.281105","authors":"","authors_abbrev":"","pubmed_publication_date":"13 Jan 2012","pubmed_entrez_date":"2012-01-17","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21544955","title":"Modelling gene and protein regulatory networks with answer set programming.","citation":"Int J Data Min Bioinform 2011;5(2):209-29","abstract":"Recently, many approaches to model regulatory networks have been proposed in the systems biology domain. However, the task is far from being solved. In this paper, we propose an Answer Set Programming (ASP)-based approach to model interaction networks. We build a general ASP framework that describes the network semantics and allows modelling specific networks with little effort. ASP provides a rich and flexible toolbox that allows expanding the framework with desired features. In this paper, we tune our framework to mimic Boolean network behaviour and apply it to model the Budding Yeast and Fission Yeast cell cycle networks. The obtained steady states of these networks correspond to those of the Boolean networks.","authors":"Fayruzov T, Janssen J, Vermeir D, Cornelis C, De Cock M","authors_abbrev":"Fayruzov T et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-05-06","publication_year":"2011","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23163955","title":"Analysis of stress-induced duplex destabilization (SIDD) properties of replication origins, genes and intergenes in the fission yeast, Schizosaccharomyces pombe.","citation":"BMC Res Notes 2012 Nov 19;5:643","abstract":"Replication and transcription, the two key functions of DNA, require unwinding of the DNA double helix. It has been shown that replication origins in the budding yeast, Saccharomyces cerevisiae contain an easily unwound stretch of DNA. We have used a recently developed method for determining the locations and degrees of stress-induced duplex destabilization (SIDD) for all the reported replication origins in the genome of the fission yeast, Schizosaccharomyces pombe.\nWe have found that the origins are more susceptible to SIDD as compared to the non-origin intergenic regions (NOIRs) and genes. SIDD analysis of many known origins in other eukaryotes suggests that SIDD is a common property of replication origins. Interestingly, the previously shown deletion-dependent changes in the activities of the origins of the ura4 origin region on chromosome 3 are paralleled by changes in SIDD properties, suggesting SIDD's role in origin activity. SIDD profiling following in silico deletions of some origins suggests that many of the closely spaced S. pombe origins could be clusters of two or three weak origins, similar to the ura4 origin region.\nSIDD appears to be a highly conserved, functionally important property of replication origins in S. pombe and other organisms. The distinctly low SIDD scores of origins and the long range effects of genetic alterations on SIDD properties provide a unique predictive potential to the SIDD analysis. This could be used in exploring different aspects of structural and functional organization of origins including interactions between closely spaced origins.","doi":"10.1186/1756-0500-5-643","authors":"Yadav MP, Padmanabhan S, Tripathi VP, Mishra RK, Dubey DD","authors_abbrev":"Yadav MP et al.","pubmed_publication_date":"19 Nov 2012","pubmed_entrez_date":"2012-11-21","publication_year":"2012","canto_session_key":"7de65253495d383a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-12-23 11:16:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-29 12:56:17","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC106.16","SPAC3C7.09","SPAPB1E7.03","SPAC5D6.06c","SPBPB2B2.05","SPCC1672.04c","SPBC1685.06","SPAC18G6.15","SPAC212.08c","SPAC607.03c","SPCC63.10c","SPAC4G9.05","SPAC9.13c","SPBC3D6.02","SPCC61.05","SPAC31A2.07c","SPAC12G12.12","SPCC5E4.03c","SPBC1709.05","SPAC24H6.02c","SPCC1259.05c","SPCC736.04c","SPAC56F8.09","SPAC1A6.05c","SPAC521.02","SPCC757.04","SPBC1683.05","SPBC3H7.08c","SPBC651.08c","SPAC23H4.18c","SPBC216.06c","SPAC1952.05","SPAC1002.19","SPCC338.04","SPCC584.11c","SPBC3D6.05","SPBC1711.13","SPAC3H8.09c","SPAC56F8.08","SPBC405.07","SPCC1322.16","SPAC23G3.04","SPBC651.09c","SPBC887.10","SPAC1952.07","SPBC16D10.05","SPBP8B7.23","SPBC3D6.04c","SPCC285.11","SPAC32A11.03c","SPCC24B10.19c","SPCC1322.15","SPAC630.06c","SPCC1494.06c","SPBC36.03c","SPAC6B12.05c","SPAP7G5.02c","SPCP31B10.04","SPBPB10D8.04c","SPCC1450.11c","SPAC17A2.08c","SPCC569.03","SPCC553.12c","SPAC20H4.11c","SPCC1672.03c","SPAPB15E9.03c","SPBC646.16","SPAC11D3.11c","SPAC1A6.04c","SPCC1223.12c","SPAC30D11.13","SPCC736.03c","SPCC757.06","SPAC222.17","SPAC11D3.09","SPBC354.09c","SPCC1827.03c","SPCC962.06c","SPCC794.10","SPCC162.06c","SPBC646.15c","SPBC146.09c","SPAC24B11.14","SPBC1685.11","SPBC776.03","SPBC800.11","SPBC17G9.05","SPCC31H12.07","SPAC13G7.07","SPCC548.07c","SPAC1A6.06c","SPAC222.18","SPAC7D4.13c","SPBC12C2.12c","SPCC285.10c","SPCC13B11.03c","SPCC1235.16","SPAP7G5.06","SPAPB15E9.02c","SPAC1296.02","SPAC607.04","SPBC15C4.04c","SPAC23G3.07c","SPAC26F1.12c","SPBC1604.09c","SPCC663.15c","SPBC947.04","SPBC115.03","SPCC1020.09","SPBC2G5.03","SPAC21E11.03c","SPBC800.04c","SPBP22H7.06","SPCC553.09c","SPAC1D4.06c","SPAC24H6.01c","SPAC664.09","SPAC664.14","SPAP11E10.02c","SPAC11D3.08c","SPCC162.11c","SPCC794.09c","SPAC607.05","SPBC32F12.09","SPAC3A12.13c","SPAC17H9.20","SPBC23G7.04c","SPBC12D12.08c","SPBC409.17c","SPAC18G6.06","SPAC20G8.01","SPAC15F9.02","SPAC9.06c","SPBC1683.03c","SPBC19G7.13","SPBP8B7.22","SPAC22A12.16","SPAC13G6.13","SPAC23E2.01","SPAC30D11.12","SPAC3A12.14","SPBC16D10.06","SPAC22A12.01c","SPAC186.09","SPBC32F12.03c","SPBPJ4664.01","SPCC1259.03","SPCC1795.12c","SPAC23A1.04c","SPAC7D4.12c","SPAC222.11","SPAC16C9.02c","SPAC4H3.14c","SPBC12C2.13c","SPBC800.03","SPBC887.09c","SPCC24B10.03","SPCC553.01c","SPCP31B10.03c","SPBC23G7.05","SPAC1296.03c","SPAC30D11.14c","SPBC146.10","SPAC977.07c","SPAC4G9.06c","SPCC663.14c","SPAC9.11","SPCC576.10c","SPAC13D6.03c","SPCC364.07","SPAP8A3.03","SPAC630.09c","SPBC646.09c","SPAC1D4.08","SPCC338.18","SPAC1B9.02c","SPBC1683.06c","SPBC16E9.12c","SPAC3H1.10","SPAC3A12.12","SPCC297.05","SPAPB17E12.10c","SPCC794.06","SPCC1393.14","SPCC645.09","SPBC1706.01","SPBC1685.10","SPBC1348.05","SPAC23C11.04c","SPCC622.06c","SPAC1002.18","SPAC2F7.14c","SPCC777.06c","SPAC17A2.09c","SPBC23G7.10c","SPCC794.03","SPAC23G3.08c","SPAP7G5.05","SPAC1556.01c","SPAC13G7.08c","SPAC22F3.02","SPBC530.12c","SPBPB10D8.05c","SPBPB2B2.06c","SPBC17G9.09","SPCC1235.13","SPAPB17E12.04c","SPAC1002.15c","SPAC222.15","SPAC11D3.03c","SPAC56E4.05","SPBC216.07c","SPAC21E11.04","SPCC1529.01","SPCC338.17c","SPAP27G11.06c","SPCC16C4.04","SPCC736.02","SPAC13D6.01","SPBC30B4.05","SPAC7D4.11c","SPBP23A10.13","SPAC3A12.02","SPAP7G5.03","SPBC1711.11","SPBC17G9.08c","SPAC9.07c","SPAC22H12.05c","SPBC1734.02c","SPAPB1E7.08c","SPBC947.03c","SPBC1711.03","SPBP26C9.02c","SPBC2G5.02c","SPBPB10D8.06c","SPCC1672.06c","SPCC31H12.08c","SPCC757.05c","SPAC24H6.08","SPAC24H6.09","SPAC212.11","SPBC800.12c","SPBC29A3.07c","SPBC16E9.17c","SPAC23G3.05c","SPBC119.17","SPAC1296.05c","SPBC1604.08c","SPCC162.12","SPBC409.10","SPAC57A10.14","SPCC24B10.04","SPCC4B3.20","SPAC4G9.14","SPAC9.12c","SPBC2G5.07c","SPBC29A10.08","SPBC1685.07c","SPBC3D6.03c","SPBP23A10.15c","SPCC1235.06","SPAC630.07c","SPCC1259.04","SPCC757.12","SPBC1709.07","SPBC12D12.07c","SPCC338.02","SPBC776.02c","SPAC4C5.03","SPAC4C5.01","SPAC9.08c","SPAC13C5.07","SPAC3H1.11","SPCC1919.06c","SPAC186.07c","SPAC750.02c","SPAC6B12.16","SPAC11D3.10","SPAC1687.01","SPBP4H10.14c","SPBC651.03c","SPAC1B9.03c","SPBC359.05","SPBP35G2.08c","SPCC1259.15c","SPAC1296.04","SPAC25A8.03c","SPBC19C2.13c","SPAC11D3.04c","SPAC57A10.05c","SPAC31A2.05c","SPCC330.19c","SPAC3C7.10","SPBC365.14c","SPAPB17E12.08","SPAC1250.04c","SPBC1685.08","SPBC23G7.09","SPBC947.12","SPAC6B12.07c","SPBP4H10.15","SPCC970.05","SPAC4C5.02c","SPAC227.16c","SPAC13G7.06","SPAC664.15","SPAC6B12.06c","SPBC15C4.05","SPBC1773.14","SPBC1773.15","SPBC146.11c","SPBC31A8.01c","SPAC32A11.02c","SPBC32F12.08c","SPAPB17E12.09","SPBC409.05","SPCC1281.07c","SPCC1672.07","SPAC12G12.13c","SPBC14C8.02","SPAC4A8.15c","SPAC56F8.16","SPCC1682.13","SPCC24B10.02c","SPCC794.07","SPBC359.04c","SPAC31A2.06","SPCC757.11c","SPBC119.03","SPCC622.07","SPCC1183.12","SPAC6B12.08","SPAC1D4.04","SPCC757.10","SPAC6B12.15","SPCC622.11","SPAC1002.16c","SPAC1D4.05c","SPAC23A1.05","SPBC32F12.04","SPBC409.06","SPCC285.13c","SPAC9G1.03c","SPBC1683.02","SPCC736.10c","SPBC29A3.08","SPAC630.10","SPAC664.02c","SPAC343.12","SPCC13B11.02c","SPCC584.02"],"gene_count":351,"ltp_gene_count":0,"approved_date":"2014-07-29"},{"uniquename":"PMID:15364564","title":"SAM domains can utilize similar surfaces for the formation of polymers and closed oligomers.","citation":"J Mol Biol 2004 Oct 01;342(5):1353-8","abstract":"The mitogen-activated protein kinase (MAPK) Byr2 and its activator Ste4 are involved in the mating pheromone response pathway of Schizosaccharomyces pombe and interact via their SAM domains. SAM domains can self-associate to form higher-order structures, including dimers, polymers and closed oligomers. Ste4-SAM is adjacent to a trimeric leucine zipper domain and we have shown previously that the two domains together (Ste4-LZ-SAM) bind to a monomeric Byr2-SAM with high affinity (Kd approximately 20 nM), forming a 3:1 complex. Here, we map the surfaces of Byr2-SAM and Ste4-SAM that is involved the interaction. A set of 38 mutants of Byr2-SAM and 33 mutants of Ste4-SAM were prepared, covering most of the protein surfaces. These mutants were purified and screened for binding, yielding a map of residues that are required for binding and a complementary map of residues that are not required. We find that the interface maps to regions of the SAM domains that are known to be important for the formation of SAM polymers. These results indicate that SAM domains can create a variety of oligomeric architectures utilizing common binding surfaces.","authors":"Ramachander R, Bowie JU","authors_abbrev":"Ramachander R et al.","pubmed_publication_date":"01 Oct 2004","pubmed_entrez_date":"2004-09-15","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.04c","SPBC1D7.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:21336311","title":"Calcineurin ensures a link between the DNA replication checkpoint and microtubule-dependent polarized growth.","citation":"Nat Cell Biol 2011 Mar;13(3):234-42","abstract":"Microtubules are central to eukaryotic cell morphogenesis. Microtubule plus-end tracking proteins (+TIPs) transport polarity factors to the cell cortex, thereby playing a key role in both microtubule dynamics and cell polarity. However, the signalling pathway linking +TIPs to cell polarity control remains elusive. Here we show that the fission yeast checkpoint kinase Cds1 (Chk2 homologue) delays the transition of growth polarity from monopolar to bipolar (termed NETO; new-end take-off). The +TIPs CLIP170 homologue Tip1 and kinesin Tea2 are responsible for this delay, which is accompanied by a reduction in microtubule dynamics at the cell tip. Remarkably, microtubule stabilization occurs asymmetrically, prominently at the non-growing cell end, which induces abnormal accumulation of the polarity factor Tea1. Importantly, NETO delay requires activation of calcineurin, which is carried out by Cds1, resulting in Tip1 dephosphorylation. Thus, our study establishes a critical link between calcineurin and checkpoint-dependent cell morphogenesis.","doi":"10.1038/ncb2166","authors":"Kume K, Koyano T, Kanai M, Toda T, Hirata D","authors_abbrev":"Kume K et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-02-22","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1604.20c","SPAC18G6.15","SPAC3C7.12","SPCC18B5.11c","SPBP4H10.04"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:34525330","title":"Increased fidelity of protein synthesis extends lifespan.","citation":"Cell Metab 2021 Nov 02;33(11):2288-2300.e12","abstract":"Loss of proteostasis is a fundamental process driving aging. Proteostasis is affected by the accuracy of translation, yet the physiological consequence of having fewer protein synthesis errors during multi-cellular organismal aging is poorly understood. Our phylogenetic analysis of RPS23, a key protein in the ribosomal decoding center, uncovered a lysine residue almost universally conserved across all domains of life, which is replaced by an arginine in a small number of hyperthermophilic archaea. When introduced into eukaryotic RPS23 homologs, this mutation leads to accurate translation, as well as heat shock resistance and longer life, in yeast, worms, and flies. Furthermore, we show that anti-aging drugs such as rapamycin, Torin1, and trametinib reduce translation errors, and that rapamycin extends further organismal longevity in RPS23 hyperaccuracy mutants. This implies a unified mode of action for diverse pharmacological anti-aging therapies. These findings pave the way for identifying novel translation accuracy interventions to improve aging.","doi":"10.1016/j.cmet.2021.08.017","authors":"Martinez-Miguel VE, Lujan C, Espie-Caullet T, Martinez-Martinez D, Moore S, Backes C, Gonzalez S, Galimov ER, Brown AEX, Halic M, Tomita K, Rallis C, von der Haar T, Cabreiro F, Bjedov I","authors_abbrev":"Martinez-Miguel VE et al.","pubmed_publication_date":"02 Nov 2021","pubmed_entrez_date":"2021-09-15","publication_year":"2021","canto_session_key":"c21d3d9a0fff1799","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-11-05 08:13:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C11.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11967172","title":"Genome sequencing: and then there were six.","citation":"Curr Biol 2002 Apr 16;12(8):R294-6","abstract":"The genome of the fission yeast Schizosaccharomyces pombe has been sequenced, bringing the number of sequenced eukaryotic genomes to six. Analysis of the sequence predicts only 4824 protein coding genes, the smallest number yet recorded for a free-living eukaryote.","authors":"MacNeill SA","authors_abbrev":"MacNeill SA","pubmed_publication_date":"16 Apr 2002","pubmed_entrez_date":"2002-04-23","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15731009","title":"Ste20/GCK kinase Nak1/Orb3 polarizes the actin cytoskeleton in fission yeast during the cell cycle.","citation":"J Cell Sci 2005 Mar 01;118(Pt 5):1033-44","abstract":"Polar growth is a crucial process during cell morphogenesis. The microtubule and actin cytoskeletons, and vesicular transport are tightly regulated to direct cellular growth and to generate specific cell forms. We demonstrate here that the Ste20-related protein kinase Nak1/Orb3 is required in fission yeast to polarize the actin cytoskeleton at the tips of the cells and for cell separation, and so is involved in controlling both cell shape and late stages of cytokinesis. The localization of the Nak1/Orb3 kinase to the cell tips, a medial ring and the spindle-pole bodies changes during the cell cycle, and the accumulation of F-actin at the cell tips is dependent on Nak1/Orb3 kinase. The phosphorylation of Nak1/Orb3 is periodic during the cell cycle and could be part of a mechanism that relocalizes a constitutively active kinase from the cell tips to the middle of the cell, thereby coordinating reorganization of the actin cytoskeleton and regulation of cell separation with cell-cycle progression.","authors":"Leonhard K, Nurse P","authors_abbrev":"Leonhard K et al.","pubmed_publication_date":"01 Mar 2005","pubmed_entrez_date":"2005-02-26","publication_year":"2005","canto_session_key":"d6654eb8043399ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-07-19 10:00:16","canto_approved_date":"2023-12-27 20:33:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-31 10:05:18","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":27,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC17F3.02","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-07-19"},{"uniquename":"PMID:12715160","title":"The phospholipase B homolog Plb1 is a mediator of osmotic stress response and of nutrient-dependent repression of sexual differentiation in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2003 Apr;269(1):116-25","abstract":"Although phospholipase B (PLB) enzymes have been described in eukaryotes from yeasts to mammals, their biological functions are poorly understood. Here we describe the characterization of plb1, one of five genes predicted to encode PLB homologs in the fission yeast, Schizosaccharomyces pombe. The plb1 gene is dispensable under normal growth conditions but required for viability in high-osmolarity media and for normal osmotic stress-induced gene expression. Unlike mutants defective in function for the stress-activated MAP kinase Spc1, plb1Delta cells are not hypersensitive to oxidative or temperature stresses, nor do they undergo a G2-specific arrest in response to osmotic stress. In addition to defects in osmotic stress response, plb1Delta cells exhibit a cold-sensitive defect in nutrient-mediated mating repression, a phenotype reminiscent of mutants in the cyclic AMP (cAMP) pathway. We show that, like plb1Delta cells, mutants in the cAMP pathway are defective for growth in high-osmolarity media, demonstrating a previously unrecognized role for the cAMP pathway in osmotic stress response. Furthermore, we show that gain-of function in the cAMP pathway can rescue the osmosensitive growth defect of plb1Delta cells, suggesting that the cAMP pathway is a potential downstream target of the actions of Plb1 in S. pombe.","authors":"Yang P, Du H, Hoffman CS, Marcus S","authors_abbrev":"Yang P et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-04-26","publication_year":"2003","canto_session_key":"85b46136eb31ff35","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 13:32:16","canto_approved_date":"2021-02-08 09:38:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-25 22:16:19","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1A6.04c","SPBC19C7.03","SPBC215.05","SPCC1753.02c","SPAC24B11.06c","SPBC106.10","SPAC8C9.03","SPAC23H3.13c"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2018-06-10"},{"uniquename":"PMID:25473118","title":"Regulation of Rho-GEF Rgf3 by the arrestin Art1 in fission yeast cytokinesis.","citation":"Mol Biol Cell 2015 Feb 01;26(3):453-66","abstract":"Rho GTPases, activated by guanine nucleotide exchange factors (GEFs), are essential regulators of polarized cell growth, cytokinesis, and many other cellular processes. However, the regulation of Rho-GEFs themselves is not well understood. Rgf3 is an essential GEF for Rho1 GTPase in fission yeast. We show that Rgf3 protein levels and localization are regulated by arrestin-related protein Art1. art1∆ cells lyse during cell separation with a thinner and defective septum. As does Rgf3, Art1 concentrates to the contractile ring starting at early anaphase and spreads to the septum during and after ring constriction. Art1 localization depends on its C-terminus, and Art1 is important for maintaining Rgf3 protein levels. Biochemical experiments reveal that the Rgf3 C-terminus binds to Art1. Using an Rgf3 conditional mutant and mislocalization experiments, we found that Art1 and Rgf3 are interdependent for localization to the division site. As expected, active Rho1 levels at the division site are reduced in art1∆ and rgf3 mutant cells. Taken together, these data reveal that the arrestin family protein Art1 regulates the protein levels and localization of the Rho-GEF Rgf3, which in turn modulates active Rho1 levels during fission yeast cytokinesis.","doi":"10.1091/mbc.E14-07-1252","authors":"Davidson R, Laporte D, Wu JQ","authors_abbrev":"Davidson R et al.","pubmed_publication_date":"01 Feb 2015","pubmed_entrez_date":"2014-12-05","publication_year":"2015","canto_session_key":"8ebbc7dc165ca3b5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-03 06:56:08","canto_approved_date":"2022-05-19 16:24:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-29 13:12:15","canto_added_date":"2014-12-06 01:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.06c","SPAC1F7.04","SPBC19G7.08c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-01-03"},{"uniquename":"PMID:23237949","title":"A chromatin switch for chromosome condensation.","citation":"Dev Cell 2012 Dec 11;23(6):1127-8","abstract":"Reporting in Molecular Cell, Tanaka et al. (2012) show that the Ku heterodimer recruits the condensin complex for retrotransposon clustering in Schizosacchromyces pombe. Histone H3 acetylation on lysine 56 blocks Ku binding and modulates this regulation of genome organization during the cell cycle and in response to DNA damage.","doi":"10.1016/j.devcel.2012.11.016","authors":"Bilodeau S, Côté J","authors_abbrev":"Bilodeau S et al.","pubmed_publication_date":"11 Dec 2012","pubmed_entrez_date":"2012-12-15","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24116866","title":"Kinetic isotope effects support the twisted amide mechanism of Pin1 peptidyl-prolyl isomerase.","citation":"Biochemistry 2013 Nov 05;52(44):7707-13","abstract":"The Pin1 peptidyl-prolyl isomerase catalyzes isomerization of pSer/pThr-Pro motifs in regulating the cell cycle. Peptide substrates, Ac-Phe-Phe-phosphoSer-Pro-Arg-p-nitroaniline, were synthesized in unlabeled form, and with deuterium-labeled Ser-d3 and Pro-d7 amino acids. Kinetic data were collected as a function of Pin1 concentration to measure kinetic isotope effects (KIEs) on catalytic efficiency (kcat/Km). The normal secondary (2°) KIE value measured for the Ser-d3 substrate (kH/kD = 1.6 ± 0.2) indicates that the serine carbonyl does not rehybridize from sp(2) to sp(3) in the rate-determining step, ruling out a nucleophilic addition mechanism. The normal 2° KIE can be explained by hyperconjugation between Ser α-C-H/D and C═O and release of steric strain upon rotation of the amide bond from cis to syn-exo. The inverse 2° KIE value (kH/kD = 0.86 ± 0.08) measured for the Pro-d7 substrate indicates rehybridization of the prolyl nitrogen from sp(2) to sp(3) during the rate-limiting step of isomerization. No solvent kinetic isotope was measured by NMR exchange spectroscopy (kH2O/kD2O = 0.92 ± 0.12), indicating little or no involvement of exchangeable protons in the mechanism. These results support the formation of a simple twisted amide transition state as the mechanism for peptidyl prolyl isomerization catalyzed by Pin1. A model of the reaction mechanism is presented using crystal structures of Pin1 with ground state analogues and an inhibitor that resembles a twisted amide transition state.","doi":"10.1021/bi400700b","authors":"Mercedes-Camacho AY, Mullins AB, Mason MD, Xu GG, Mahoney BJ, Wang X, Peng JW, Etzkorn FA","authors_abbrev":"Mercedes-Camacho AY et al.","pubmed_publication_date":"05 Nov 2013","pubmed_entrez_date":"2013-10-15","publication_year":"2013","canto_session_key":"828252c7389ca3c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-04-27 15:51:46","canto_approved_date":"2021-04-27 15:51:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-27 15:51:39","canto_added_date":"2020-12-09 15:41:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16C4.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-04-27"},{"uniquename":"PMID:19286778","title":"De novo biosynthesis of vanillin in fission yeast (Schizosaccharomyces pombe) and baker's yeast (Saccharomyces cerevisiae).","citation":"Appl Environ Microbiol 2009 May;75(9):2765-74","abstract":"Vanillin is one of the world's most important flavor compounds, with a global market of 180 million dollars. Natural vanillin is derived from the cured seed pods of the vanilla orchid (Vanilla planifolia), but most of the world's vanillin is synthesized from petrochemicals or wood pulp lignins. We have established a true de novo biosynthetic pathway for vanillin production from glucose in Schizosaccharomyces pombe, also known as fission yeast or African beer yeast, as well as in baker's yeast, Saccharomyces cerevisiae. Productivities were 65 and 45 mg/liter, after introduction of three and four heterologous genes, respectively. The engineered pathways involve incorporation of 3-dehydroshikimate dehydratase from the dung mold Podospora pauciseta, an aromatic carboxylic acid reductase (ACAR) from a bacterium of the Nocardia genus, and an O-methyltransferase from Homo sapiens. In S. cerevisiae, the ACAR enzyme required activation by phosphopantetheinylation, and this was achieved by coexpression of a Corynebacterium glutamicum phosphopantetheinyl transferase. Prevention of reduction of vanillin to vanillyl alcohol was achieved by knockout of the host alcohol dehydrogenase ADH6. In S. pombe, the biosynthesis was further improved by introduction of an Arabidopsis thaliana family 1 UDP-glycosyltransferase, converting vanillin into vanillin beta-D-glucoside, which is not toxic to the yeast cells and thus may be accumulated in larger amounts. These de novo pathways represent the first examples of one-cell microbial generation of these valuable compounds from glucose. S. pombe yeast has not previously been metabolically engineered to produce any valuable, industrially scalable, white biotech commodity.","doi":"10.1128/AEM.02681-08","authors":"Hansen EH, Møller BL, Kock GR, Bünner CM, Kristensen C, Jensen OR, Okkels FT, Olsen CE, Motawia MS, Hansen J","authors_abbrev":"Hansen EH et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-03-17","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5030076","title":"Photoreactivation in the yeast Schizosaccharomyces pombe.","citation":"Photochem Photobiol 1972 Apr;15(4):367-73","abstract":"","authors":"Fabre F","authors_abbrev":"Fabre F","pubmed_publication_date":"Apr 1972","pubmed_entrez_date":"1972-04-01","publication_year":"1972","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17192844","title":"The end1 gene of Schizosaccharomyces pombe coding for a DNase is identical with the pnu1 gene coding for an RNase.","citation":"Yeast 2007 Jan;24(1):11-6","abstract":"The DNA nuclease activity encoded by the end1 gene, and its inactivation by mutation, was described in connection with the characterization of DNA topoisomerases in the fission yeast Schizosaccharomyces pombe (Uemura and Yanagida, 1984). Subsequently, end1 mutant strains were used for the preparation of cell extracts for the study of enzymes and intermediates involved in DNA metabolism. The molecular identification of the end1 gene and its identity with the pnu1 gene is presented. The end1-458 mutation alters glycine to glutamate in the conserved motif TGPYLP. The pnu1 gene codes for an RNase that is induced by nitrogen starvation (Nakashima et al., 2002b). Thus, the End1/Pnu1 protein, like related mitochondrial proteins in other organisms, is an example of a sugar-non-specific nuclease. The analysis of strains carrying a pnu1 deletion revealed no defects in meiotic recombination and spore viability.","authors":"Sakem B, Kohli J","authors_abbrev":"Sakem B et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2006-12-29","publication_year":"2007","canto_session_key":"8bda08ab65cfc49b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-03 22:18:14","canto_approved_date":"2023-07-03 22:28:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-03 22:18:08","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-07-03"},{"uniquename":"PMID:15292231","title":"Regulation of Swi6/HP1-dependent heterochromatin assembly by cooperation of components of the mitogen-activated protein kinase pathway and a histone deacetylase Clr6.","citation":"J Biol Chem 2004 Oct 08;279(41):42850-9","abstract":"A study of gene silencing within the mating-type region of fission yeast defines two distinct pathways responsible for the establishment of heterochromatin assembly. One is RNA interference-dependent and acts on centromere-homologous repeats (cenH). The other is a stochastic Swi6 (the fission yeast HP1 homolog)-dependent mechanism that is not fully understood. Here we find that activating transcription factor (Atf1) and Pcr1, the fission yeast bZIP transcription factors homologous to human ATF-2, are crucial for proper histone deacetylation of both H3 and H4. This deacetylation is a prerequisite for subsequent H3 lysine 9 methylation and Swi6-dependent heterochromatin assembly across the rest of the silent mating-type (mat) region lacking the RNA interference-dependent cenH repeat. Moreover, Atf1 and Pcr1 can form complexes with both a histone deacetylase, Clr6, and Swi6, and clr6 mutations affected the H3/H4 acetylation patterns, similar to the atf1 and pcr1 deletion mutant phenotypes at the endogenous mat loci and at the ctt1+ promoter region surrounding ATF/CRE-binding site. These data suggest that Atf1 and Pcr1 participate in an early step essential for heterochromatin assembly at the mat locus and silencing of transcriptional targets of Atf1. Furthermore, a phosphorylation event catalyzed by the conserved mitogen-activated protein kinase pathway is important for regulation of heterochromatin silencing by Atf1 and Pcr1. These findings suggest a role for the mitogen-activated protein kinase pathway and histone deacetylase in Swi6-based heterochromatin assembly.","authors":"Kim HS, Choi ES, Shin JA, Jang YK, Park SD","authors_abbrev":"Kim HS et al.","pubmed_publication_date":"08 Oct 2004","pubmed_entrez_date":"2004-08-05","publication_year":"2004","canto_session_key":"48b52c7ce19007bd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-21 08:04:45","canto_approved_date":"2024-03-26 10:24:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-14 12:30:14","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":35,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPBC36.05c","SPBC800.03","SPBC29B5.01","SPCC1322.13","SPAC21E11.03c","SPBC1711.02","SPAC6F12.09","SPBC428.08c","SPAC664.01c","SPAC24B11.06c"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2024-03-21"},{"uniquename":"PMID:15964812","title":"Distinct requirements for Pot1 in limiting telomere length and maintaining chromosome stability.","citation":"Mol Cell Biol 2005 Jul;25(13):5567-78","abstract":"The fission yeast Pot1 (protection of telomeres) protein binds to the single-stranded extensions at the ends of telomeres, where its presence is critical for the maintenance of linear chromosomes. Homologs of Pot1 have been identified in a wide variety of eukaryotes, including plants, animals, and humans. We now show that Pot1 plays dual roles in telomere length regulation and chromosome end protection. Using a series of Pot1 truncation mutants, we have defined distinct areas of the protein required for chromosome stability and for limiting access to telomere ends by telomerase. We provide evidence that a large portion of Pot1, including the N-terminal DNA binding domain and amino acids close to the C terminus, is essential for its protective function. C-terminal Pot1 fragments were found to exert a dominant-negative effect by displacing endogenous Pot1 from telomeres. Reducing telomere-bound Pot1 in this manner resulted in dramatic lengthening of the telomere tract. Upon further reduction of Pot1 at telomeres, the opposite phenotype was observed: loss of telomeric DNA and chromosome end fusions. Our results demonstrate that cells must carefully regulate the amount of telomere-bound Pot1 to differentiate between allowing access to telomerase and catastrophic loss of telomeres.","authors":"Bunch JT, Bae NS, Leonardi J, Baumann P","authors_abbrev":"Bunch JT et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-06-21","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36951111","title":"Homologous recombination suppresses transgenerational DNA end resection and chromosomal instability in fission yeast.","citation":"Nucleic Acids Res 2023 Apr 24;51(7):3205-3222","abstract":"Chromosomal instability (CIN) drives cell-to-cell heterogeneity, and the development of genetic diseases, including cancer. Impaired homologous recombination (HR) has been implicated as a major driver of CIN, however, the underlying mechanism remains unclear. Using a fission yeast model system, we establish a common role for HR genes in suppressing DNA double-strand break (DSB)-induced CIN. Further, we show that an unrepaired single-ended DSB arising from failed HR repair or telomere loss is a potent driver of widespread CIN. Inherited chromosomes carrying a single-ended DSB are subject to cycles of DNA replication and extensive end-processing across successive cell divisions. These cycles are enabled by Cullin 3-mediated Chk1 loss and checkpoint adaptation. Subsequent propagation of unstable chromosomes carrying a single-ended DSB continues until transgenerational end-resection leads to fold-back inversion of single-stranded centromeric repeats and to stable chromosomal rearrangements, typically isochromosomes, or to chromosomal loss. These findings reveal a mechanism by which HR genes suppress CIN and how DNA breaks that persist through mitotic divisions propagate cell-to-cell heterogeneity in the resultant progeny.","doi":"10.1093/nar/gkad160","authors":"Pai CC, Durley SC, Cheng WC, Chiang NY, Peters J, Kasparek T, Blaikley E, Wee BY, Walker C, Kearsey SE, Buffa F, Murray JM, Humphrey TC","authors_abbrev":"Pai CC et al.","pubmed_publication_date":"24 Apr 2023","pubmed_entrez_date":"2023-03-23","publication_year":"2023","canto_session_key":"33a9a0889692ed36","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-03-24 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18667534","title":"Activation of the DNA damage checkpoint in mutants defective in DNA replication initiation.","citation":"Mol Biol Cell 2008 Oct;19(10):4374-82","abstract":"In the fission yeast, Schizosaccharomyces pombe, blocks to DNA replication elongation trigger the intra-S phase checkpoint that leads to the activation of the Cds1 kinase. Cds1 is required to both prevent premature entry into mitosis and to stabilize paused replication forks. Interestingly, although Cds1 is essential to maintain the viability of mutants defective in DNA replication elongation, mutants defective in DNA replication initiation require the Chk1 kinase. This suggests that defects in DNA replication initiation can lead to activation of the DNA damage checkpoint independent of the intra-S phase checkpoint. This might result from reduced origin firing that leads to an increase in replication fork stalling or replication fork collapse that activates the G2 DNA damage checkpoint. We refer to the Chk1-dependent, Cds1-independent phenotype as the rid phenotype (for replication initiation defective). Chk1 is active in rid mutants, and rid mutant viability is dependent on the DNA damage checkpoint, and surprisingly Mrc1, a protein required for activation of Cds1. Mutations in Mrc1 that prevent activation of Cds1 have no effect on its ability to support rid mutant viability, suggesting that Mrc1 has a checkpoint-independent role in maintaining the viability of mutants defective in DNA replication initiation.","authors":"Yin L, Locovei AM, D'Urso G","authors_abbrev":"Yin L et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-08-01","publication_year":"2008","canto_session_key":"89cfa03ed6856c05","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-04-20 14:01:36","canto_approved_date":"2018-04-20 14:01:36","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-04-20 14:01:19","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":27,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPAC8E11.02c","SPBC25H2.13c","SPCC4G3.05c","SPBC685.09","SPCC1259.13","SPBC30D10.04","SPAC8F11.07c","SPAC14C4.13","SPBC216.05","SPBC29A10.15","SPBC14C8.07c","SPBC1734.02c","SPBC336.04","SPAC2G11.12","SPCC18B5.11c","SPBC342.05","SPAC1952.07","SPAC664.07c","SPBC216.06c","SPAC694.06c","SPAC9E9.08"],"gene_count":22,"ltp_gene_count":22,"approved_date":"2018-04-20"},{"uniquename":"PMID:34360997","title":"The Active Mechanism of Nucleosome Depletion by Poly(dA:dT) Tracts In Vivo.","citation":"Int J Mol Sci 2021 Jul 30;22(15)","abstract":"Poly(dA:dT) tracts cause nucleosome depletion in many species, e.g., at promoters and replication origins. Their intrinsic biophysical sequence properties make them stiff and unfavorable for nucleosome assembly, as probed by in vitro nucleosome reconstitution. The mere correlation between nucleosome depletion over poly(dA:dT) tracts in in vitro reconstituted and in in vivo chromatin inspired an intrinsic nucleosome exclusion mechanism in vivo that is based only on DNA and histone properties. However, we compile here published and new evidence that this correlation does not reflect mechanistic causation. (1) Nucleosome depletion over poly(dA:dT) in vivo is not universal, e.g., very weak in  S. pombe . (2) The energy penalty for incorporating poly(dA:dT) tracts into nucleosomes is modest (<10%) relative to ATP hydrolysis energy abundantly invested by chromatin remodelers. (3) Nucleosome depletion over poly(dA:dT) is much stronger in vivo than in vitro if monitored without MNase and (4) actively maintained in vivo. (5)  S. cerevisiae  promoters evolved a strand-biased poly(dA) versus poly(dT) distribution. (6) Nucleosome depletion over poly(dA) is directional in vivo. (7) The ATP dependent chromatin remodeler RSC preferentially and directionally displaces nucleosomes towards 5' of poly(dA). Especially distribution strand bias and displacement directionality would not be expected for an intrinsic mechanism. Together, this argues for an in vivo mechanism where active and species-specific read out of intrinsic sequence properties, e.g., by remodelers, shapes nucleosome organization.","doi":"10.3390/ijms22158233","authors":"Barnes T, Korber P","authors_abbrev":"Barnes T et al.","pubmed_publication_date":"30 Jul 2021","pubmed_entrez_date":"2021-08-07","publication_year":"2021","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2021-08-09 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26702831","title":"Oligomerization but Not Membrane Bending Underlies the Function of Certain F-BAR Proteins in Cell Motility and Cytokinesis.","citation":"Dev Cell 2015 Dec 21;35(6):725-36","abstract":"F-BAR proteins function in diverse cellular processes by linking membranes to the actin cytoskeleton. Through oligomerization, multiple F-BAR domains can bend membranes into tubules, though the physiological importance of F-BAR-to-F-BAR assemblies is not yet known. Here, we investigate the F-BAR domain of the essential cytokinetic scaffold, Schizosaccharomyces pombe Cdc15, during cytokinesis. Challenging a widely held view that membrane deformation is a fundamental property of F-BARs, we report that the Cdc15 F-BAR binds, but does not deform, membranes in vivo or in vitro, and six human F-BAR domains-including those from Fer and RhoGAP4-share this property. Nevertheless, tip-to-tip interactions between F-BAR dimers are critical for Cdc15 oligomerization and high-avidity membrane binding, stabilization of contractile ring components at the medial cortex, and the fidelity of cytokinesis. F-BAR oligomerization is also critical for Fer and RhoGAP4 physiological function, demonstrating its broad importance to F-BAR proteins that function without membrane bending.","doi":"10.1016/j.devcel.2015.11.023","authors":"McDonald NA, Vander Kooi CW, Ohi MD, Gould KL","authors_abbrev":"McDonald NA et al.","pubmed_publication_date":"21 Dec 2015","pubmed_entrez_date":"2015-12-26","publication_year":"2015","canto_session_key":"13c8454e4e123cb3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2018-03-08 12:46:37","canto_approved_date":"2026-02-01 18:48:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-20 16:50:19","canto_added_date":"2015-12-27 01:19:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":111,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kathy Gould","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.05","SPBC83.18c","SPBC11C11.02","SPCC4B3.15","SPAP8A3.08","SPAC4F8.13c","SPAC1F5.04c","SPCC645.05c","SPAC20G8.05c","SPCC645.06c","SPAC6F6.08c","SPBC4F6.12","SPAC24B11.11c","SPBC19G7.05c","SPCC1840.02c","SPAC1782.09c"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2018-03-08"},{"uniquename":"PMID:1332977","title":"Functional dissection of the phosphorylated termini of fission yeast DNA topoisomerase II.","citation":"J Cell Biol 1992 Dec;119(5):1023-36","abstract":"Fission Yeast DNA topoisomerase II (165 kD) consists of an enzymatically active 125-kD core, approximately 10-kD NH2-terminal and 30-kD COOH-terminal domains. The question addressed in the present study is what is the role of the topo II termini. Although deletion of either the NH2 or the COOH terminus is viable, deletion of both termini is lethal; the termini share an essential role for viability. We show here that topo II phosphorylation sites are localized in the terminal domains, but dephosphorylated topo II is still active. The topo II terminal sequences are required for nuclear localization; topo II double terminal deletion mutants are deficient for nuclear targeting, whereas wild-type and single deletion mutant topo IIs are transported into the nucleus with different efficiencies. Functional subdomains in the NH2 terminus are further dissected; we identified a 15 amino acid nuclear localization sequence (NLS) which is essential for viability and nuclear localization when the COOH terminus is deleted. This NLS could be substituted with SV-40 large T-antigen NLS. Two other functional subdomains were found; a non-essential acidic stretch which is phosphorylated and apparently enhances the nuclear localization and an essential hydrophilic stretch of unknown function. Motifs similar to these three NH2-terminal subdomains are also found in the COOH terminus. Our results support the possibility that phosphorylation of topo II does not play an essential role in fission yeast.","authors":"Shiozaki K, Yanagida M","authors_abbrev":"Shiozaki K et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"b7d7c9ccb439768b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-07-06 15:30:49","canto_approved_date":"2025-09-04 10:10:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-06 15:30:39","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":54,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_1332977_phaf.tsv"}],"genes":["SPBC1A4.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-07-06"},{"uniquename":"PMID:21325896","title":"G1/S transcription and the DNA synthesis checkpoint: common regulatory mechanisms.","citation":"Cell Cycle 2011 Mar 15;10(6):912-5","abstract":"When DNA replication is challenged, cells activate a DNA-synthesis checkpoint blocking cell cycle progression until they are able to overcome the replication defects. In fission yeast, Cds1 is the effector kinase of this checkpoint, inhibiting M phase entry through inactivation of the phosphatase Cdc25, stabilizing stalled replication forks to prevent deleterious DNA structures and triggering transcriptional activation of S-phase genes. The MBF complex controls the transcription of genes required for the S phase and Yox1, a homeodomain-containing protein, binds and represses MBF-dependent transcription at the end of S phase in a cell cycle-regulated manner. Interestingly, when the DNA synthesis checkpoint is activated, Yox1 is phosphorylated by Cds1 resulting in the abrogation of its binding to MBF. As a consequence, MBF-dependent transcription is maintained active until cells are able to overcome the replication challenge. Thus, Yox1 couples normal cell cycle regulation and the DNA synthesis checkpoint in a single transcriptional complex.","authors":"Ivanova T, Gómez-Escoda B, Hidalgo E, Ayté J","authors_abbrev":"Ivanova T et al.","pubmed_publication_date":"15 Mar 2011","pubmed_entrez_date":"2011-02-18","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9490631","title":"F-actin distribution and function during sexual differentiation in Schizosaccharomyces pombe.","citation":"J Cell Sci 1998 Apr;111 ( Pt 7):867-76","abstract":"Sexual differentiation in Schizosaccharomyces pombe is induced from the G1 phase of the cell cycle by nitrogen starvation and the presence of mating pheromones. We describe the distribution of F-actin during sexual differentiation. Cortical F-actin dots have previously been shown to be restricted to one end of the rod shaped cell during the G1 phase of the cell cycle. Within half an hour of nitrogen starvation the distribution of cortical F-actin dots switched from being monopolar to bipolar. This was then reversed as the F-actin cytoskeleton repolarized so that cortical F-actin dots accumulated towards the projection tip at one end of the cell. Following cell fusion, F-actin dots were randomly scattered during the horsetail movement that precedes meiosis I and remained scattered until prometaphase or metaphase of meiosis II, when they concentrated around the nucleus. F-actin was seen on the lagging face of the nuclei which faced the partner nucleus during anaphase B of meiosis II. Early on in this anaphase F-actin was also seen on the opposite side of the nucleus, near the spindle pole body. F-actin accumulated within the spores in the mature ascus. Treatment with the actin depolymerising drug Latrunculin A showed that F-actin is required for cell fusion and spore formation. Latrunculin A treatment extended all stages from karyogamy to meiosis I. The S. pombe homologue of the actin binding protein profilin, Cdc3, was shown to be required for conjugation. Cdc3 co-localized with the formin related molecule Fus1 at the projection tip. The polarization of F-actin cortical dots to the projection tip was unaffected in the cdc3.124 mutant, but cdc3.124 mutant cells were unable to break down the cell walls between the two cells following agglutination.","authors":"Petersen J, Nielsen O, Egel R, Hagan IM","authors_abbrev":"Petersen J et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-05-20","publication_year":"1998","canto_session_key":"240021077c897136","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-09-07 17:51:16","canto_approved_date":"2026-01-31 17:23:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-07 17:51:06","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.15c","SPBC32H8.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-09-07"},{"uniquename":"PMID:38449372","title":"Regulation of sexual differentiation initiation in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2024 Mar 06;","abstract":"The fission yeast Schizosaccharomyces pombe is an excellent model organism to explore cellular events owing to rich tools in genetics, molecular biology, cellular biology, and biochemistry. S. pombe proliferates continuously when nutrients are abundant, but arrests in G1 phase upon depletion of nutrients such as nitrogen and glucose. When cells of opposite mating types are present, cells conjugate, fuse, undergo meiosis, and finally form four spores. This sexual differentiation process in S. pombe has been studied extensively. To execute sexual differentiation, the glucose-sensing cAMP-PKA pathway, nitrogen-sensing TOR and SAPK pathways are crucial, and the MAPK cascade is essential for pheromone sensing. These signals regulate ste11 at the transcriptional and translational levels, and Ste11 is modified in multiple ways. This review summarizes the initiation of sexual differentiation in S. pombe based on results I have helped to obtain including the work of many excellent researchers.","doi":"10.1093/bbb/zbae019","authors":"Kawamukai M","authors_abbrev":"Kawamukai M","pubmed_publication_date":"06 Mar 2024","pubmed_entrez_date":"2024-03-07","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-03-09 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC17H9.09c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:27397687","title":"Distinct Functions of Argonaute Slicer in siRNA Maturation and Heterochromatin Formation.","citation":"Mol Cell 2016 Jul 21;63(2):191-205","abstract":"Small-RNA (sRNA)-guided transcriptional gene silencing by Argonaute (Ago)-containing complexes is fundamental to genome integrity and epigenetic inheritance. The RNA cleavage (\"Slicer\") activity of Argonaute has been implicated in both sRNA maturation and target RNA cleavage. Typically, Argonaute slices and releases the passenger strand of duplex sRNA to generate active silencing complexes, but it remains unclear whether slicing of target nascent RNAs, or other RNAi components, also contributes to downstream transcriptional silencing. Here, we develop a strategy for loading the fission yeast Ago1 with a single-stranded sRNA guide, which bypasses the requirement for slicer activity in generation of active silencing complexes. We show that slicer-defective Ago1 can mediate secondary sRNA generation, H3K9 methylation, and silencing similar to or better than wild-type and associates with chromatin more efficiently. The results define an ancient and minimal sRNA-mediated chromatin silencing mechanism, which resembles the germline-specific sRNA-dependent transcriptional silencing pathways in Drosophila and mammals.","doi":"10.1016/j.molcel.2016.05.039","authors":"Jain R, Iglesias N, Moazed D","authors_abbrev":"Jain R et al.","pubmed_publication_date":"21 Jul 2016","pubmed_entrez_date":"2016-07-12","publication_year":"2016","canto_session_key":"9221fb8cf31525e6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-13 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27002163","title":"Laser microsurgery reveals conserved viscoelastic behavior of the kinetochore.","citation":"J Cell Biol 2016 Mar 28;212(7):767-76","abstract":"Accurate chromosome segregation depends on proper kinetochore-microtubule attachment. Upon microtubule interaction, kinetochores are subjected to forces generated by the microtubules. In this work, we used laser ablation to sever microtubules attached to a merotelic kinetochore, which is laterally stretched by opposing pulling forces exerted by microtubules, and inferred the mechanical response of the kinetochore from its length change. In both mammalian PtK1 cells and in the fission yeast Schizosaccharomyces pombe, kinetochores shortened after microtubule severing. Interestingly, the inner kinetochore-centromere relaxed faster than the outer kinetochore. Whereas in fission yeast all kinetochores relaxed to a similar length, in PtK1 cells the more stretched kinetochores remained more stretched. Simple models suggest that these differences arise because the mechanical structure of the mammalian kinetochore is more complex. Our study establishes merotelic kinetochores as an experimental model for studying the mechanical response of the kinetochore in live cells and reveals a viscoelastic behavior of the kinetochore that is conserved in yeast and mammalian cells.","doi":"10.1083/jcb.201506011","authors":"Cojoc G, Roscioli E, Zhang L, García-Ulloa A, Shah JV, Berns MW, Pavin N, Cimini D, Tolić IM, Gregan J","authors_abbrev":"Cojoc G et al.","pubmed_publication_date":"28 Mar 2016","pubmed_entrez_date":"2016-03-23","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22093953","title":"Hypertrophy hypothesis as an alternative explanation of the phenomenon of replicative aging of yeast.","citation":"FEMS Yeast Res 2012 Feb;12(1):97-101","abstract":"This paper summarizes numerous arguments demonstrating that the hypothesis of accumulation of the senescence factor, which was the basis for introducing yeast to the group of model organisms of gerontology, finds no experimental support. Among several candidates for the role of the causative agents of replicative aging, only one - hypertrophy - always accompanies symptoms of aging, not only in Saccharomyces cerevisiae, but also in Schizosaccharomyces pombe.","doi":"10.1111/j.1567-1364.2011.00759.x","authors":"Biliński T, Zadrąg-Tęcza R, Bartosz G","authors_abbrev":"Biliński T et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-11-19","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34843421","title":"SWI/SNF and RSC remodeler complexes bind to MBF-dependent genes.","citation":"Cell Cycle 2021 Dec;20(24):2652-2661","abstract":"In fission yeast, MBF-dependent transcription is required for cells to complete S phase. The MBF transcription factor is regulated through a complex feedback mechanism that involves the co-repressors Yox1 and Nrm1 that are loaded onto MBF at the end of S phase, while positive transactivation is achieved through the constitutive binding of the co-activator Rep2. Here we show that Rep2 is required to fully recruit the chromatin remodelers SWI/SNF and RSC to MBF-regulated promoters. On the contrary, Nrm1 and Yox1, when bound to the MBF complex, block the approximation of these chromatin remodelers to MBF-regulated promoters. We propose that SWI/SNF and RSC are recruited to MBF-regulated genes, and RSC together with SAGA complex are important to regulate the G1-to-S transcriptional wave. Mutants of these remodeler complexes are highly sensitive when cells are exposed to insults that challenge DNA synthesis.","doi":"10.1080/15384101.2021.2008203","authors":"González-Medina A, Pazo E, Hidalgo E, Ayté J","authors_abbrev":"González-Medina A et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-11-29","publication_year":"2021","canto_session_key":"767db9a035ebea70","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-01 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20807799","title":"The recruitment of acetylated and unacetylated tropomyosin to distinct actin polymers permits the discrete regulation of specific myosins in fission yeast.","citation":"J Cell Sci 2010 Oct 01;123(Pt 19):3235-43","abstract":"Tropomyosin (Tm) is a conserved dimeric coiled-coil protein, which forms polymers that curl around actin filaments in order to regulate actomyosin function. Acetylation of the Tm N-terminal methionine strengthens end-to-end bonds, which enhances actin binding as well as the ability of Tm to regulate myosin motor activity in both muscle and non-muscle cells. In this study we explore the function of each Tm form within fission yeast cells. Electron microscopy and live cell imaging revealed that acetylated and unacetylated Tm associate with distinct actin structures within the cell, and that each form has a profound effect upon the shape and integrity of the polymeric actin filament. We show that, whereas Tm acetylation is required to regulate the in vivo motility of class II myosins, acetylated Tm had no effect on the motility of class I and V myosins. These findings illustrate a novel Tm-acetylation-state-dependent mechanism for regulating specific actomyosin cytoskeletal interactions.","doi":"10.1242/jcs.069971","authors":"Coulton AT, East DA, Galinska-Rakoczy A, Lehman W, Mulvihill DP","authors_abbrev":"Coulton AT et al.","pubmed_publication_date":"01 Oct 2010","pubmed_entrez_date":"2010-09-03","publication_year":"2010","canto_session_key":"ff16db44d9ab6882","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-18 14:28:14","canto_approved_date":"2022-06-17 06:12:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-06 10:20:09","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"vw253 cam.ac.uk","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC1215.02c","SPCC16C4.12","SPCC645.05c","SPAC27F1.02c","SPAC4A8.05c"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2018-06-18"},{"uniquename":"PMID:8930897","title":"Spatial organization of the Nim1-Wee1-Cdc2 mitotic control network in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1996 Nov;7(11):1749-58","abstract":"In Schizosaccharomyces pombe the onset of mitosis is regulated by a network of protein kinases and phosphatases. The M-phase inducing Cdc2-Cdc13 cyclin-dependent kinase is inhibited by Wee1 tyrosine kinase and activated by Cdc25 phosphatase. Wee1 is negatively regulated by Nim1 protein kinase. Here, we describe investigations aimed at better understanding the role of Nim1 in the mitotic control. The most important finding to emerge from these studies is that Wee1 and Nim1 have different patterns of intracellular localization. Immunofluorescence confocal microscopy has revealed that Nim1 is localized in the cytoplasm, whereas it substrate Wee1 is predominantly localized in the nucleus. Previous studies showed that the Cdc2-Cdc13 complex is located in the nucleus. Diversion of Nim1 to the nucleus, accomplished by addition of the SV40 nuclear localization signal, caused the advancement of M, confirming that Nim1 has restricted access to Wee1 in vivo. We propose that the intracellular distribution of Nim1 and Wee1 may serve to coordinate the regulation of nuclear Cdc2-Cdc13 with cytoplasmic growth.","authors":"Wu L, Shiozaki K, Aligue R, Russell P","authors_abbrev":"Wu L et al.","pubmed_publication_date":"Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30625250","title":"Kinetochores, cohesin, and DNA breaks: Controlling meiotic recombination within pericentromeres.","citation":"Yeast 2019 Mar;36(3):121-127","abstract":"In meiosis, DNA break formation and repair are essential for the formation of crossovers between homologous chromosomes. Without crossover formation, faithful meiotic chromosome segregation and sexual reproduction cannot occur. Crossover formation is initiated by the programmed, meiosis-specific introduction of numerous DNA double-strand breaks, after which specific repair pathways promote recombination between homologous chromosomes. Despite its crucial nature, meiotic recombination is fraud with danger: When positioned or repaired inappropriately, DNA breaks can have catastrophic consequences on genome stability of the resulting gametes. As such, DNA break formation and repair needs to be carefully controlled. Within centromeres and surrounding regions (i.e., pericentromeres), meiotic crossover recombination is repressed in organisms ranging from yeast to humans, and a failure to do so is implicated in chromosome missegregation and developmental aneuploidy. (Peri)centromere sequence identity and organization diverge considerably across eukaryotes, yet suppression of meiotic DNA break formation and repair appear universal. Here, we discuss emerging work that has used budding and fission yeast systems to study the mechanisms underlying pericentromeric suppression of DNA break formation and repair. We particularly highlight a role for the kinetochore, a universally conserved, centromere-associated structure essential for chromosome segregation, in suppressing (peri)centromeric DNA break formation and repair. We discuss the current understanding of kinetochore-associated and chromosomal factors involved in this regulation and suggest future avenues of research.","doi":"10.1002/yea.3366","authors":"Kuhl LM, Vader G","authors_abbrev":"Kuhl LM et al.","pubmed_publication_date":"Mar 2019","pubmed_entrez_date":"2019-01-10","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-01-11 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19222572","title":"High environmental iron concentrations stimulate adhesion and invasive growth of Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 2009 Apr;293(1):130-4","abstract":"We have found that a high iron concentration in solid complete cultivation medium potentiates cell-cell and cell-surface adhesion of the fission yeast Schizosaccharomyces pombe. Spotted giant colonies grown on iron-rich media were found to be more compact and more resistant to washing than those grown on plates with a standard iron content. Furthermore, we have documented that excess environmental iron stimulates the invasive growth of S. pombe (and Saccharomyces cerevisiae). Three-dimensional, branched, washing-resistant structures composed mostly of elongated, but separate fission yeast cells, were formed within the solid agar medium. The degree of both adhesion and invasion displayed a specific, iron concentration-dependent response. Our results suggest a novel link between iron availability and the intensively studied and important fungal virulence factors, adhesion and invasion.","doi":"10.1111/j.1574-6968.2009.01515.x","authors":"Prevorovský M, Stanurová J, Půta F, Folk P","authors_abbrev":"Prevorovský M et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-02-19","publication_year":"2009","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30584685","title":"The fission yeast Greatwall-Endosulfine pathway is required for proper quiescence/G 0  phase entry and maintenance.","citation":"Genes Cells 2019 Feb;24(2):172-186","abstract":"Cell proliferation and cellular quiescence/G 0  phase must be regulated in response to intra-/extracellular environments, and such regulation is achieved by the orchestration of protein kinases and protein phosphatases. Here, we investigated fission yeast potential orthologs (Cek1, Ppk18 and Ppk31) of the metazoan Greatwall kinase (Gwl), which inhibits type-2A protein phosphatase with B55 subunit (PP2A B55  ) by phosphorylating and activating the PP2A B55  inhibitors, α-endosulfine/ARPP-19 (Ensa/ARPP-19). Gwl and Ensa/ARPP-19 regulate mitosis; however, we found Ppk18, Cek1 and Mug134/Igo1, the counterpart of Ensa/ARPP-19, are not essential for normal mitosis but regulate nitrogen starvation (-N)-induced proper G 0  entry and maintenance. Genetic and biochemical analyses indicated that the conserved Gwl site (serine 64) was phosphorylated in the G 0  phase in a Ppk18-dependent manner, and the phosphorylated Mug134/Igo1 inhibited PP2A B55  in vitro. The alanine substitution of the serine 64 caused defects in G 0  entry and maintenance as well as the mug134/igo1 +  deletion. These results indicate that PP2A B55  activity must be regulated properly to establish the G 0  phase. Consistently, simultaneous deletion of the B55 gene with mug134/igo1 +  partially rescued the Mug134/Igo1 mutant phenotype. We suggest that in fission yeast, PP2A B55  regulation by the Ppk18-Mug134/Igo1 pathway is required for G 0  entry and establishment of robust viability during the G 0  phase.","doi":"10.1111/gtc.12665","authors":"Aono S, Haruna Y, Watanabe YH, Mochida S, Takeda K","authors_abbrev":"Aono S et al.","pubmed_publication_date":"Feb 2019","pubmed_entrez_date":"2018-12-26","publication_year":"2019","canto_session_key":"379299ba8e094571","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-12-27 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14701739","title":"Coordination of DNA damage responses via the Smc5/Smc6 complex.","citation":"Mol Cell Biol 2004 Jan;24(2):662-74","abstract":"The detection of DNA damage activates DNA repair pathways and checkpoints to allow time for repair. Ultimately, these responses must be coordinated to ensure that cell cycle progression is halted until repair is completed. Several multiprotein complexes containing members of the structural maintenance of chromosomes family of proteins have been described, including the condensin and cohesin complexes, that are critical for chromosomal organization. Here we show that the Smc5/Smc6 (Smc5/6) complex is required for a coordinated response to DNA damage and normal chromosome integrity. Fission yeast cells lacking functional Smc6 initiate a normal checkpoint response to DNA damage, culminating in the phosphorylation and activation of the Chk1 protein kinase. Despite this, cells enter a lethal mitosis, presumably without completion of DNA repair. Another subunit of the complex, Nse1, is a conserved member of this complex and is also required for this response. We propose that the failure to maintain a checkpoint response stems from the lack of ongoing DNA repair or from defective chromosomal organization, which is the signal to maintain a checkpoint arrest. The Smc5/6 complex is fundamental to genome integrity and may function with the condensin and cohesin complexes in a coordinated manner.","authors":"Harvey SH, Sheedy DM, Cuddihy AR, O'Connell MJ","authors_abbrev":"Harvey SH et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2004-01-01","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC5E4.06","SPCC550.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU012793","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24945319","title":"CPF-associated phosphatase activity opposes condensin-mediated chromosome condensation.","citation":"PLoS Genet 2014 Jun;10(6):e1004415","abstract":"Functional links connecting gene transcription and condensin-mediated chromosome condensation have been established in species ranging from prokaryotes to vertebrates. However, the exact nature of these links remains misunderstood. Here we show in fission yeast that the 3' end RNA processing factor Swd2.2, a component of the Cleavage and Polyadenylation Factor (CPF), is a negative regulator of condensin-mediated chromosome condensation. Lack of Swd2.2 does not affect the assembly of the CPF but reduces its association with chromatin. This causes only limited, context-dependent effects on gene expression and transcription termination. However, CPF-associated Swd2.2 is required for the association of Protein Phosphatase 1 PP1(Dis2) with chromatin, through an interaction with Ppn1, a protein that we identify as the fission yeast homologue of vertebrate PNUTS. We demonstrate that Swd2.2, Ppn1 and PP1Dis2 form an independent module within the CPF, which provides an essential function in the absence of the CPF-associated Ssu72 phosphatase. We show that Ppn1 and Ssu72, like Swd2.2, are also negative regulators of condensin-mediated chromosome condensation. We conclude that Swd2.2 opposes condensin-mediated chromosome condensation by facilitating the function of the two CPF-associated phosphatases PP1 and Ssu72.","doi":"10.1371/journal.pgen.1004415","authors":"Vanoosthuyse V, Legros P, van der Sar SJ, Yvert G, Toda K, Le Bihan T, Watanabe Y, Hardwick K, Bernard P","authors_abbrev":"Vanoosthuyse V et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-06-20","publication_year":"2014","canto_session_key":"ea1aba50125a8d9b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Vincent Vanoosthuyse","canto_first_approved_date":"2016-09-03 17:13:48","canto_approved_date":"2026-01-30 14:38:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-03-26 12:26:21","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":39,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Vincent Vanoosthuyse","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.11c","SPAC3G9.04","SPAC17A2.13c","SPAC227.08c","SPAC22G7.10","SPBC6B1.04","SPBC1709.08","SPCC74.02c","SPAC4A8.12c","SPAC17A5.09c","SPAC57A7.04c","SPBC776.02c","SPBC146.03c","SPCC16C4.03","SPCC31H12.05c","SPBC354.10","SPBC11B10.10c","SPAC824.04","SPAC1F3.01","SPBC1703.14c","SPAC20H4.03c","SPAC12G12.14c","SPAC6G9.10c","SPBC28F2.12","SPAC6B12.13","SPBC336.07","SPBP4H10.06c","SPAC16.02c","SPAC12G12.04","SPAC8E11.02c","SPCC736.07c","SPAC1071.02","SPBC337.03","SPBC3B8.03","SPBC21D10.05c","SPBC1706.01","SPAC19G12.15c","SPAC227.15","SPAC4F10.04","SPBC11C11.08","SPBC1709.15c","SPBC660.15","SPCC306.03c","SPBC2G5.07c","SPBC16E9.12c","SPBC649.05","SPAC1071.01c","SPAC12G12.13c","SPBC646.04","SPBC3B9.11c","SPAC17G6.16c","SPBC21H7.05"],"gene_count":52,"ltp_gene_count":21,"approved_date":"2016-09-03"},{"uniquename":"PMID:19293826","title":"Force- and length-dependent catastrophe activities explain interphase microtubule organization in fission yeast.","citation":"Mol Syst Biol 2009;5:241","abstract":"The cytoskeleton is essential for the maintenance of cell morphology in eukaryotes. In fission yeast, for example, polarized growth sites are organized by actin, whereas microtubules (MTs) acting upstream control where growth occurs. Growth is limited to the cell poles when MTs undergo catastrophes there and not elsewhere on the cortex. Here, we report that the modulation of MT dynamics by forces as observed in vitro can quantitatively explain the localization of MT catastrophes in Schizosaccharomyces pombe. However, we found that it is necessary to add length-dependent catastrophe rates to make the model fully consistent with other previously measured traits of MTs. We explain the measured statistical distribution of MT-cortex contact times and re-examine the curling behavior of MTs in unbranched straight tea1Delta cells. Importantly, the model demonstrates that MTs together with associated proteins such as depolymerizing kinesins are, in principle, sufficient to mark the cell poles.","doi":"10.1038/msb.2008.76","authors":"Foethke D, Makushok T, Brunner D, Nédélec F","authors_abbrev":"Foethke D et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-03-19","publication_year":"2009","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12521308","title":"Pap1-dependent regulation of the GSTII gene from the fission yeast.","citation":"Mol Cells 2002 Dec 31;14(3):431-6","abstract":"The genomic DNA encoding a second glutathione S-transferase (GSTII) was previously isolated from the fission yeast Schizosaccharomyces pombe. Its expression was shown to be induced by menadione, mercuric chloride, o-dinitrobenzene, and NO-generating S-nitroso-N-acetylpenicillamine using the GSTII-lacZ fusion harboring the 910 bp upstream region from the translational initiation point. In this study, the additional fusion plasmids pGST50-590 and pGST50-6R-590 were constructed to carry the 590 bp upstream region in the vectors YEp357 and YEp367R, respectively. The synthesis of beta-galactosidase from the fusion plasmid pGST50-590 was about 3-fold higher than that from the fusion plasmid pGST50-F, indicating the presence of negatively activating sequence in the -910 to approximately -590 region. It was also enhanced by the same agents, which induced the synthesis of beta-galactosidase from the fusion plasmid pGST50-F. The synthesis of beta-galactosidase from both fusion plasmids pGST50-F and pGST50-590 was enhanced by the overexpressed Pap1 protein. The synthesis of beta-galactosidase from the two YEp367R derivatives pGST50-6R-F and pGST50-6R-590 was greatly decreased in the Pap1-negative strain TP108-3C. These results propose the Pap1-dependent regulation of the GSTII gene from the fission yeast.","authors":"Lim CJ, Cho YW, Sa JH, Lim HW, Kim HG, Kim SJ, Park EH","authors_abbrev":"Lim CJ et al.","pubmed_publication_date":"31 Dec 2002","pubmed_entrez_date":"2003-01-11","publication_year":"2002","canto_session_key":"5b8582e6ff3b58fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:57:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-03 16:15:24","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC965.07c","SPAC15E1.09","SPAC1783.07c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2014-11-03"},{"uniquename":"PMID:8668127","title":"Identification of the DNA damage-responsive elements of the rhp51+ gene, a recA and RAD51 homolog from the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1996 May 23;251(2):167-75","abstract":"The Schizosaccharomyces pombe rhp51+ gene encodes a recombinational repair protein that shares significant sequence identities with the bacterial RecA and the Saccharomyces cerevisiae RAD51 protein. Levels of rhp51+ mRNA increase following several types of DNA damage or inhibition of DNA synthesis. An rhp51::ura4 fusion gene was used to identify the cis-acting promoter elements involved in regulating rhp51+ expression in response to DNA damage. Two elements, designated DRE1 and DRE2 (for damage-responsive element), match a decamer consensus URS (upstream repressing sequence) found in the promoters of many other DNA repair and metabolism genes from S. cerevisiae. However, our results show that DRE1 and DRE2 each function as a UAS (upstream activating sequence) rather than a URS and are also required for DNA-damage inducibility of the gene. A 20-bp fragment located downstream of both DRE1 and DRE2 is responsible for URS function. The DRE1 and DRE2 elements cross-competed for binding to two proteins of 45 and 59 kDa. DNase I footprint analysis suggests that DRE1 and DRE2 bind to the same DNA-binding proteins. These results suggest that the DRE-binding proteins may play an important role in the DNA-damage inducibility of rhp51+ expression.","authors":"Jang YK, Jin YH, Shim YS, Kim MJ, Yoo EJ, Choi IS, Lee JS, Seong RH, Hong SH, Park SD","authors_abbrev":"Jang YK et al.","pubmed_publication_date":"23 May 1996","pubmed_entrez_date":"1996-05-23","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1454522","title":"Fission yeast cdc21+ belongs to a family of proteins involved in an early step of chromosome replication.","citation":"Nucleic Acids Res 1992 Nov 11;20(21):5571-7","abstract":"The cdc21+ gene of Schizosaccharomyces pombe was originally identified in a screen for cdc mutants affecting S phase and nuclear division. Here we show that the cdc21+ gene product belongs to a family of proteins implicated in DNA replication. These include the Saccharomyces cerevisiae MCM2 and MCM3 proteins, which are needed for the efficient function of certain replication origins, and S.cerevisiae CDC46, which is required for the initiation of chromosome replication. The cdc21 mutant is defective in the mitotic maintenance of some plasmids, like mcm2 and mcm3. The mutant arrests with a single nucleus containing two genome equivalents of DNA, and maintains a cytoplasmic microtubular configuration. Activation of most, but not all, replication origins in the mutant may result in failure to replicate a small proportion of the genome, and this could explain the arrest phenotypes. Using the polymerase chain reaction technique, we have identified new cdc21(+)-related genes in S.cerevisiae, S.pombe and Xenopus laevis. Our results suggest that individual members of the cdc21(+)-related family are highly conserved in evolution.","authors":"Coxon A, Maundrell K, Kearsey SE","authors_abbrev":"Coxon A et al.","pubmed_publication_date":"11 Nov 1992","pubmed_entrez_date":"1992-11-11","publication_year":"1992","canto_session_key":"f42a10cdf2e50a0b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-06-09 13:56:55","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-10-16 14:10:34","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-10-16"},{"uniquename":"PMID:4711455","title":"Ultrastructural changes of the fission yeast (Schizosaccharomyces pombe) during ascospore formation.","citation":"Arch Mikrobiol 1973 Apr 08;91(1):1-10","abstract":"","authors":"Yoo BY, Calleja GB, Johnson BF","authors_abbrev":"Yoo BY et al.","pubmed_publication_date":"08 Apr 1973","pubmed_entrez_date":"1973-04-08","publication_year":"1973","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30922219","title":"A genome-wide analysis of carbon catabolite repression in Schizosaccharomyces pombe.","citation":"BMC Genomics 2019 Mar 29;20(1):251","abstract":"Optimal glucose metabolism is central to the growth and development of cells. In microbial eukaryotes, carbon catabolite repression (CCR) mediates the preferential utilization of glucose, primarily by repressing alternate carbon source utilization. In fission yeast, CCR is mediated by transcriptional repressors Scr1 and the Tup/Ssn6 complex, with the Rst2 transcription factor important for activation of gluconeogenesis and sexual differentiation genes upon derepression. Through genetic and genome-wide methods, this study aimed to comprehensively characterize CCR in fission yeast by identifying the genes and biological processes that are regulated by Scr1, Tup/Ssn6 and Rst2, the core CCR machinery.\nThe transcriptional response of fission yeast to glucose-sufficient or glucose-deficient growth conditions in wild type and CCR mutant cells was determined by RNA-seq and ChIP-seq. Scr1 was found to regulate genes involved in carbon metabolism, hexose uptake, gluconeogenesis and the TCA cycle. Surprisingly, a role for Scr1 in the suppression of sexual differentiation was also identified, as homothallic scr1 deletion mutants showed ectopic meiosis in carbon and nitrogen rich conditions. ChIP-seq characterised the targets of Tup/Ssn6 and Rst2 identifying regulatory roles within and independent of CCR. Finally, a subset of genes bound by all three factors was identified, implying that regulation of certain loci may be modulated in a competitive fashion between the Scr1, Tup/Ssn6 repressors and the Rst2 activator.\nBy identifying the genes directly and indirectly regulated by Scr1, Tup/Ssn6 and Rst2, this study comprehensively defined the gene regulatory networks of CCR in fission yeast and revealed the transcriptional complexities governing this system.","doi":"10.1186/s12864-019-5602-8","authors":"Vassiliadis D, Wong KH, Andrianopoulos A, Monahan BJ","authors_abbrev":"Vassiliadis D et al.","pubmed_publication_date":"29 Mar 2019","pubmed_entrez_date":"2019-03-30","publication_year":"2019","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-03-31 01:00:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18B11.10","SPAC6F12.02","SPBC1D7.02c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:15272162","title":"Structure, crystal packing and molecular dynamics of the calponin-homology domain of Schizosaccharomyces pombe Rng2.","citation":"Acta Crystallogr D Biol Crystallogr 2004 Aug;60(Pt 8):1396-403","abstract":"Schizosaccharomyces pombe Rng2 is an IQGAP protein that is essential for the assembly of an actomyosin ring during cytokinesis. Rng2 contains an amino-terminal calponin-homology (CH) domain, 11 IQ repeats and a RasGAP-homology domain. CH domains are known mainly for their ability to bind F-actin, although they have other ligands in vivo and there are only few examples of actin-binding single CH domains. The structures of several CH domains have already been reported, but this is only the third report of an actin-binding protein that contains a single CH domain (the structures of calponin and EB1 have been reported previously). The 2.21 A resolution crystal structure of the amino-terminal 190 residues of Rng2 from Br- and Hg-derivatives includes 40 residues (150-190) carboxyl-terminal to the CH domain that resemble neither the extended conformation seen in utrophin, nor the compact conformation seen in fimbrin, although residues 154-160 form an unstructured coil which adopts a substructure similar to dystrophin residues 240-246 in the carboxyl-terminal portion of the CH2 domain. This region wraps around the stretch of residues that would be equivalent to the proposed actin-binding site ABS1 and ABS2 from dystrophin. This distinctive feature is absent from previously published CH-domain structures. Another feature revealed by comparing the two derivatives is the presence of two loop conformations between Tyr92 and Arg99.","authors":"Wang CH, Balasubramanian MK, Dokland T","authors_abbrev":"Wang CH et al.","pubmed_publication_date":"Aug 2004","pubmed_entrez_date":"2004-07-24","publication_year":"2004","canto_session_key":"eaf2c807ad7dbf6c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-01 07:47:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-30 07:21:54","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F8.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-30","pdb_entries":[{"pdb_id":"1p2x","gene_chains":[{"gene_uniquename":"SPAC4F8.13c","chain":"A","position":"32-190"}],"title":"CRYSTAL STRUCTURE OF THE CALPONIN-HOMOLOGY DOMAIN OF RNG2 FROM SCHIZOSACCHAROMYCES POMBE","entry_authors":"Wang C-H,Balasubramanian MK,Dokland T","entry_authors_abbrev":"Wang C-H et al.","reference_uniquename":"PMID:15272162","experimental_method":"X-ray","resolution":"2.21"},{"pdb_id":"1p5s","gene_chains":[{"gene_uniquename":"SPAC4F8.13c","chain":"A","position":"1-190"}],"title":"STRUCTURE AND FUNCTION OF THE CALPONIN-HOMOLOGY DOMAIN OF AN IQGAP PROTEIN FROM SCHIZOSACCHAROMYCES POMBE","entry_authors":"Wang CH,Balasubramanian MK,Dokland T","entry_authors_abbrev":"Wang CH et al.","reference_uniquename":"PMID:15272162","experimental_method":"X-ray","resolution":"2.22"}]},{"uniquename":"GO_REF:0000108","title":"Automatic assignment of GO terms using logical inference, based on on inter-ontology links.","abstract":"GO terms are automatically assigned based on inter-ontology links to generate inferred annotations. Annotations from Molecular Function to Biological Process can be propagated, as well as between Biological Process and Cellular Component. Annotations that are created using this inference method receive either the evidence code ECO:0000366 (evidence based on logical inference from automatic annotation used in automatic assertion) or ECO:0000364 (evidence based on logical inference from manual annotation used in automatic assertion), depending on whether the source annotation has a manual or automatic evidence code. Both of these codes map up to the GO Inferred from Electronic Annotation (IEA) evidence code.","authors":"GOA curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11G11.07","SPNCRNA.6405","SPAC105.03c","SPAC32A11.03c","SPAC13G7.10","SPBC25H2.16c","SPBC30D10.21","SPAC8E11.04c","SPMIT.01","SPBP4H10.08","SPBC725.10","SPBC365.16","SPAC23C4.11","SPAC22F3.13","SPAC17G8.09","SPAC6C3.06c","SPAC1527.02","SPBC839.06","SPAC26F1.13c","SPAC3A12.15","SPAC4G8.11c","SPAC11E3.08c","SPAC328.01c","SPAC29A4.19c","SPCC825.04c","SPBC36B7.02","SPAC4D7.13","SPBC2D10.10c","SPAC1F5.03c","SPCC613.10","SPBC16H5.06","SPAC139.02c","SPBC1271.11","SPNCRNA.7186","SPAC17H9.01","SPAC1F8.01","SPCC962.01","SPBP8B7.28c","SPAC23A1.04c","SPAC26A3.13c","SPBC2G5.01","SPAC17A2.13c","SPCC16A11.09c","SPBC14C8.07c","SPCC1494.11c","SPCC1020.14","SPAP27G11.03","SPBC1604.07","SPCC895.04c","SPAC869.03c","SPCC330.01c","SPAC23C4.19","SPBC887.12","SPBC30D10.06","SPNCRNA.7236","SPNCRNA.2529","SPAC27E2.08","SPBC336.11","SPBC1683.12","SPAC6F12.09","SPNCRNA.7042","SPAC1039.04","SPBC2F12.17","SPBC32H8.03","SPNCRNA.7463","SPBC18A7.02c","SPBC16A3.14","SPNCRNA.7383","SPBC776.02c","SPCC162.11c","SPAC1687.11","SPCC1322.16","SPAC110.02","SPNCRNA.1669","SPAC23H4.18c","SPAC23A1.15c","SPBC4.02c","SPCP25A2.02c","SPAC6F6.17","SPCC1840.10","SPBC29A10.13","SPAC139.03","SPAC6B12.08","SPBC25D12.05","SPBC25H2.13c","SPCC1020.09","SPAPB15E9.03c","SPBC9B6.02c","SPBC577.13","SPBC409.08","SPBC409.20c","SPAC167.08","SPBP35G2.11c","SPBC947.02","SPMIT.09","SPBC342.05","SPBC2G2.02","SPAC2F3.10","SPAC3A11.06","SPCC320.08","SPBC609.05","SPCC16C4.03","SPAC19D5.09c","SPCC1259.05c","SPAC17G6.07c","SPAC1B3.15c","SPCC1620.01c","SPCC1753.05","SPAC17G6.15c","SPBP35G2.03c","SPCC1682.11c","SPAC139.06","SPBC27B12.14","SPBC11G11.04","SPCC24B10.22","SPAC22G7.06c","SPAC1002.16c","SPMIT.11","SPAC19A8.07c","SPAC328.09","SPAC9.04","SPCC1739.09c","SPBC1289.02c","SPBC6B1.09c","SPAC30.04c","SPAC4G8.09","SPCC757.04","SPBC725.17c","SPBC800.13","SPBPB8B6.02c","SPAC227.14","SPBC8D2.02c","SPCC1442.08c","SPCC320.13c","SPBC3B9.10","SPAC15A10.15","SPAC26H5.07c","SPBC691.05c","SPBC18H10.16","SPAC521.04c","SPCC584.11c","SPBC4B4.08","SPAC17C9.16c","SPCC1235.13","SPCC1672.04c","SPAC14C4.01c","SPBC28F2.12","SPBC354.03","SPAC18B11.08c","SPMIT.07","SPCC306.04c","SPAC12B10.09","SPBC16C6.08c","SPCC794.11c","SPAC9.09","SPBC1289.17","SPAC1093.03","SPCC18.17c","SPCC14G10.03c","SPCC548.06c","SPAC4H3.06","SPAC31A2.13c","SPAC23C11.09","SPMIT.04","SPAC22G7.02","SPAC3G9.05","SPAC1782.06c","SPNCRNA.3283","SPAC22E12.17c","SPAC1296.02","SPNCRNA.2777","SPBC15D4.07c","SPBC1348.14c","SPAC4G8.13c","SPCC18B5.08c","SPBC8D2.06","SPBC25B2.02c","SPBC9B6.05c","SPAC5D6.13","SPAC4H3.01","SPCC23B6.03c","SPCC576.17c","SPBC18H10.06c","SPAC1F8.02c","SPCC576.04","SPCC18.02","SPAPB1A10.07c","SPCC737.02c","SPAC1B3.16c","SPBC1652.02","SPAC3A12.12","SPBC3E7.04c","SPAC1399.05c","SPCC18.11c","SPAC14C4.13","SPBC609.04","SPBC16G5.15c","SPAC24C9.16c","SPCC1795.02c","SPBC582.05c","SPNCRNA.2479","SPAC26A3.05","SPCC622.14","SPCC1322.12c","SPBC3E7.11c","SPAC4G9.10","SPAC3A12.17c","SPAC3G6.02","SPCC777.02","SPCC594.05c","SPBC13G1.08c","SPAC22E12.05c","SPCC330.06c","SPCC297.04c","SPAC25H1.02","SPCP1E11.06","SPNCRNA.2656","SPAC2G11.14","SPAC22F3.07c","SPAC6G10.05c","SPAC13D1.01c","SPAC11D3.11c","SPAC630.11","SPBC1709.02c","SPMIT.05","SPAC1B2.04","SPBC3H7.04","SPAC4A8.08c","SPBC19C7.06","SPNCRNA.3411","SPCC16A11.08","SPAC227.09","SPCC1672.11c","SPCC306.05c","SPBC106.05c","SPBC8D2.07c","SPBC106.02c","SPAC1B1.01","SPAC11D3.18c","SPBC1289.04c","SPBC23G7.13c","SPBC530.12c","SPBC216.05","SPAPB21F2.02","SPAC9G1.08c","SPBC16C6.06","SPAC23H3.05c","SPCC338.10c","SPAC2H10.02c","SPAC23D3.10c","SPBC1E8.04","SPNCRNA.4841","SPNCRNA.7125","SPBC651.10","SPAC23C4.13","SPAC3G9.04","SPAC2E1P3.03c","SPCC1235.14","SPBC25H2.04c","SPAC1B2.02c","SPNCRNA.3131","SPBC29A3.18"],"gene_count":262,"ltp_gene_count":0},{"uniquename":"PMID:31250307","title":"Genetic and Cytological Methods to Study ESCRT Cell Cycle Function in Fission Yeast.","citation":"Methods Mol Biol 2019;1998:239-250","abstract":"The fission yeast Schizosaccharomyces pombe, an ascomycete fungus, is an established model organism for studying eukaryotic molecular and cellular events such as the cell cycle due to its powerful genetics, a sequenced genome, and the ease of molecular manipulation (Wood et al., Nature 415:871-880, 2002; Hoffman et al., Genetics 201:403-423, 2015). This chapter describes genetic and cytological methods to study endosomal sorting complex required for transport (ESCRT) function during the cell cycle in fission yeast. These include tetrad analysis to allow the creation of double mutants to test for genetic interactions by synthetic phenotype characterization, such as cellular growth and the analysis of division septa by calcofluor-white staining.","doi":"10.1007/978-1-4939-9492-2_18","authors":"Rezig IM, Bremner SK, Bhutta MS, Salt IP, Gould GW, McInerny CJ","authors_abbrev":"Rezig IM et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-06-29","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-07-01 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18658154","title":"Ers1, a rapidly diverging protein essential for RNA interference-dependent heterochromatic silencing in Schizosaccharomyces pombe.","citation":"J Biol Chem 2008 Sep 19;283(38):25770-3","abstract":"Centromeric silencing and heterochromatin formation in Schizosaccharomyces pombe require the RNA interference (RNAi) machinery. Three factors that mediate this mechanism have been identified: 1) the RNA-dependent RNA polymerase complex RdRC, 2) the Argonaute-containing RITS (RNA-induced initiation of transcriptional silencing) complex, and 3) the endoribonuclease Dicer ortholog Dcr1. S. pombe mutants lacking a new factor described here, Ers1, are completely defective in RNAi-dependent silencing of centromeric regions but, importantly, not in RNAi-independent silencing at the mat3M or tel2R loci. ers1Delta cells likewise fail to convert centromeric pre-small interfering RNA transcripts into small interfering RNAs, are defective in histone H3 Lys(9) methylation, and are unable to recruit the RITS complex to centromeric sequences. Surprisingly, Ers1 lacks obvious orthologs outside of the genus Schizosaccharomyces. Within this group, it is diverging rapidly, raising the possibility that it is coevolving with target RNA elements.","doi":"10.1074/jbc.C800140200","authors":"Rougemaille M, Shankar S, Braun S, Rowley M, Madhani HD","authors_abbrev":"Rougemaille M et al.","pubmed_publication_date":"19 Sep 2008","pubmed_entrez_date":"2008-07-29","publication_year":"2008","canto_session_key":"0eeecc7d59bfbbce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-09 16:57:16","canto_approved_date":"2024-06-09 16:57:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-09 16:56:52","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1393.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-06-09"},{"uniquename":"PMID:16541024","title":"Protein phosphatase 2A protects centromeric sister chromatid cohesion during meiosis I.","citation":"Nature 2006 May 04;441(7089):53-61","abstract":"Segregation of homologous maternal and paternal centromeres to opposite poles during meiosis I depends on post-replicative crossing over between homologous non-sister chromatids, which creates chiasmata and therefore bivalent chromosomes. Destruction of sister chromatid cohesion along chromosome arms due to proteolytic cleavage of cohesin's Rec8 subunit by separase resolves chiasmata and thereby triggers the first meiotic division. This produces univalent chromosomes, the chromatids of which are held together by centromeric cohesin that has been protected from separase by shugoshin (Sgo1/MEI-S332) proteins. Here we show in both fission and budding yeast that Sgo1 recruits to centromeres a specific form of protein phosphatase 2A (PP2A). Its inactivation causes loss of centromeric cohesin at anaphase I and random segregation of sister centromeres at the second meiotic division. Artificial recruitment of PP2A to chromosome arms prevents Rec8 phosphorylation and hinders resolution of chiasmata. Our data are consistent with the notion that efficient cleavage of Rec8 requires phosphorylation of cohesin and that this is blocked by PP2A at meiosis I centromeres.","authors":"Riedel CG, Katis VL, Katou Y, Mori S, Itoh T, Helmhart W, Gálová M, Petronczki M, Gregan J, Cetin B, Mudrak I, Ogris E, Mechtler K, Pelletier L, Buchholz F, Shirahige K, Nasmyth K","authors_abbrev":"Riedel CG et al.","pubmed_publication_date":"04 May 2006","pubmed_entrez_date":"2006-03-17","publication_year":"2006","canto_session_key":"18cbd65c4f603fdb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-03-17 20:27:34","canto_approved_date":"2026-02-17 15:30:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-12 12:08:49","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.03c","SPAP8A3.09c","SPAC6F12.12","SPAC15A10.15","SPAC823.15","SPAC23C11.05","SPCC1322.12c","SPBC16H5.07c","SPCC188.02","SPBC29A10.14"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2021-03-17"},{"uniquename":"PMID:12019258","title":"A 160-bp palindrome is a Rad50.Rad32-dependent mitotic recombination hotspot in Schizosaccharomyces pombe.","citation":"Genetics 2002 May;161(1):461-8","abstract":"Palindromic sequences can form hairpin and cruciform structures that pose a threat to genome integrity. We found that a 160-bp palindrome (an inverted repeat of 80 bp) conferred a mitotic recombination hotspot relative to a control nonpalindromic sequence when inserted into the ade6 gene of Schizosaccharomyces pombe. The hotspot activity of the palindrome, but not the basal level of recombination, was abolished by a rad50 deletion, by a rad50S \"separation of function\" mutation, or by a rad32-D25A mutation in the nuclease domain of the Rad32 protein, an Mre11 homolog. We propose that upon extrusion of the palindrome the Rad50.Rad32 nuclease complex recognizes and cleaves the secondary structure thus formed and generates a recombinogenic break in the DNA.","authors":"Farah JA, Hartsuiker E, Mizuno K, Ohta K, Smith GR","authors_abbrev":"Farah JA et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-05-23","publication_year":"2002","canto_session_key":"37a883806f3d3302","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-17 14:29:45","canto_approved_date":"2025-05-19 15:59:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-17 14:29:40","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC1556.01c","SPAC13C5.07"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-06-17"},{"uniquename":"PMID:27167753","title":"Nucleation and spreading of a heterochromatic domain in fission yeast.","citation":"Nat Commun 2016 May 11;7:11518","abstract":"Outstanding questions in the chromatin field bear on how large heterochromatin domains are formed in space and time. Positive feedback, where histone-modifying enzymes are attracted to chromosomal regions displaying the modification they catalyse, is believed to drive the formation of these domains; however, few quantitative studies are available to assess this hypothesis. Here we quantified the de novo establishment of a naturally occurring ∼20-kb heterochromatin domain in fission yeast through single-cell analyses, measuring the kinetics of heterochromatin nucleation in a region targeted by RNAi and its subsequent expansion. We found that nucleation of heterochromatin is stochastic and can take from one to ten cell generations. Further silencing of the full region takes another one to ten generations. Quantitative modelling of the observed kinetics emphasizes the importance of local feedback, where a nucleosome-bound enzyme modifies adjacent nucleosomes, combined with a feedback where recruited enzymes can act at a distance.","doi":"10.1038/ncomms11518","authors":"Obersriebnig MJ, Pallesen EM, Sneppen K, Trusina A, Thon G","authors_abbrev":"Obersriebnig MJ et al.","pubmed_publication_date":"11 May 2016","pubmed_entrez_date":"2016-05-12","publication_year":"2016","canto_session_key":"eccad790de2fec12","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-05-13 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26921242","title":"Centromere localization and function of Mis18 requires Yippee-like domain-mediated oligomerization.","citation":"EMBO Rep 2016 Apr;17(4):496-507","abstract":"Mis18 is a key regulator responsible for the centromere localization of the CENP-A chaperone Scm3 in Schizosaccharomyces pombe and HJURP in humans, which establishes CENP-A chromatin that defines centromeres. The molecular and structural determinants of Mis18 centromere targeting remain elusive. Here, by combining structural, biochemical, and yeast genetic studies, we show that the oligomerization of S. pombe Mis18, mediated via its conserved N-terminal Yippee-like domain, is crucial for its centromere localization and function. The crystal structure of the N-terminal Yippee-like domain reveals a fold containing a cradle-shaped pocket that is implicated in protein/nucleic acid binding, which we show is required for Mis18 function. While the N-terminal Yippee-like domain forms a homodimer in vitro and in vivo, full-length Mis18, including the C-terminal α-helical domain, forms a homotetramer in vitro We also show that the Yippee-like domains of human Mis18α/Mis18β interact to form a heterodimer, implying a conserved structural theme for Mis18 regulation.","doi":"10.15252/embr.201541520","authors":"Subramanian L, Medina-Pritchard B, Barton R, Spiller F, Kulasegaran-Shylini R, Radaviciute G, Allshire RC, Arockia Jeyaprakash A","authors_abbrev":"Subramanian L et al.","pubmed_publication_date":"Apr 2016","pubmed_entrez_date":"2016-02-28","publication_year":"2016","canto_session_key":"4359a750d5773b4f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Bethan Medina-Pritchard","canto_first_approved_date":"2019-06-02 16:50:47","canto_approved_date":"2024-04-03 12:45:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-31 10:06:40","canto_added_date":"2016-02-29 01:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Bethan Medina-Pritchard","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-06-02","pdb_entries":[{"pdb_id":"5hj0","gene_chains":[{"gene_uniquename":"SPCC970.12","chain":"A/B/C","position":"1-120"}],"title":"Crystal Structure of Mis18 'Yippee-like' Domain","entry_authors":"Medina-Pritchard B,Subramanian L,Allshire R,Arockia Jeyaprakash A","entry_authors_abbrev":"Medina-Pritchard B et al.","reference_uniquename":"PMID:26921242","experimental_method":"X-ray","resolution":"2.64"}]},{"uniquename":"PMID:25002088","title":"Fungal membrane organization: the eisosome concept.","citation":"Annu Rev Microbiol 2014;68:377-93","abstract":"The fungal plasma membrane is organized into specialized domains that vary in size, stability, and composition. Membrane compartment of Can1(MCC)/eisosome domains that were recently discovered in the budding yeast Saccharomyces cerevisiae are interesting because they represent a novel type of membrane domain that is important for plasma membrane organization, sphingolipid homeostasis, and cell wall morphogenesis. The MCC portion was identified as stable punctate patches that correspond to furrows in the plasma membrane that are about 300 nm long and 50 nm deep. These domains contain integral membrane proteins, including the tetraspan proteins Sur7 and Nce102. The eisosome portion includes proteins peripherally associated with the cytoplasmic side of the MCC, including the Bin/amphiphysin/Rvs-domain proteins Pil1 and Lsp1, which assemble into filaments that curve the membrane to form the furrows. By comparing MCC/eisosome domains in diverse fungi, researchers are identifying common features that further our understanding of their unique biogenesis, structure, and function.","doi":"10.1146/annurev-micro-091313-103507","authors":"Douglas LM, Konopka JB","authors_abbrev":"Douglas LM et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-07-09","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-09-12 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16362914","title":"Comparative analysis of cell cycle regulated genes in eukaryotes.","citation":"Genome Inform 2005;16(1):125-31","abstract":"We compared microarray experiments on cell cycle of three model eukaryotes: budding and fission yeast and human cells. Only 112 orthologous groups were cyclic in the three model organisms. The common set of cyclic orthologs includes many taking part in the cell cycle progression, like cyclin B homologs, CDC5, SCH9, DSK2, ZPR1. Proteins involved in DNA replication included histones, some checkpoint kinases and some proteins regulating DNA damage and repair. Conserved cyclic proteins involved in cytokinesis included myosins and kinesins. Many groups of genes related to translation and other metabolic processes were also cyclic in all three organisms. This reflects rebuilding of cellular components after the replication and changes of metabolism during the cell cycle. Many genes important in cell cycle control are not cyclic or not conserved. This includes transcription factors implicated in the regulation of budding yeast cell cycle. The partially overlapping roles of regulatory proteins might allow the evolutionary substitution of components of cell cycle.","authors":"Dyczkowski J, Vingron M","authors_abbrev":"Dyczkowski J et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-12-20","publication_year":"2005","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1819501","title":"Mitotic checkpoint control in fission yeast.","citation":"Cold Spring Harb Symp Quant Biol 1991;56:409-16","abstract":"","authors":"Enoch T, Gould KL, Nurse P","authors_abbrev":"Enoch T et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30357405","title":"Complex Portal 2018: extended content and enhanced visualization tools for macromolecular complexes.","citation":"Nucleic Acids Res 2019 Jan 08;47(D1):D550-D558","abstract":"The Complex Portal (www.ebi.ac.uk/complexportal) is a manually curated, encyclopaedic database that collates and summarizes information on stable, macromolecular complexes of known function. It captures complex composition, topology and function and links out to a large range of domain-specific resources that hold more detailed data, such as PDB or Reactome. We have made several significant improvements since our last update, including improving compliance to the FAIR data principles by providing complex-specific, stable identifiers that include versioning. Protein complexes are now available from 20 species for download in standards-compliant formats such as PSI-XML, MI-JSON and ComplexTAB or can be accessed via an improved REST API. A component-based JS front-end framework has been implemented to drive a new website and this has allowed the use of APIs from linked services to import and visualize information such as the 3D structure of protein complexes, its role in reactions and pathways and the co-expression of complex components in the tissues of multi-cellular organisms. A first draft of the complete complexome of Saccharomyces cerevisiae is now available to browse and download.","doi":"10.1093/nar/gky1001","authors":"Meldal BHM, Bye-A-Jee H, Gajdoš L, Hammerová Z, Horácková A, Melicher F, Perfetto L, Pokorný D, Lopez MR, Türková A, Wong ED, Xie Z, Casanova EB, Del-Toro N, Koch M, Porras P, Hermjakob H, Orchard S","authors_abbrev":"Meldal BHM et al.","pubmed_publication_date":"08 Jan 2019","pubmed_entrez_date":"2018-10-26","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16169489","title":"Novel genes required for meiotic chromosome segregation are identified by a high-throughput knockout screen in fission yeast.","citation":"Curr Biol 2005 Sep 20;15(18):1663-9","abstract":"Two rounds of chromosome segregation after only a single round of DNA replication enable the production of haploid gametes from diploid precursors during meiosis. To identify genes involved in meiotic chromosome segregation, we developed an efficient strategy to knock out genes in the fission yeast on a large scale. We used this technique to delete 180 functionally uncharacterized genes whose expression is upregulated during meiosis. Deletion of two genes, sgo1 and mde2, caused massive chromosome missegregation. sgo1 is required for retention of centromeric sister-chromatid cohesion after anaphase I. We show here that mde2 is required for formation of the double-strand breaks necessary for meiotic recombination.","authors":"Gregan J, Rabitsch PK, Sakem B, Csutak O, Latypov V, Lehmann E, Kohli J, Nasmyth K","authors_abbrev":"Gregan J et al.","pubmed_publication_date":"20 Sep 2005","pubmed_entrez_date":"2005-09-20","publication_year":"2005","canto_session_key":"08caaf0d4ea1eb4b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-03-06 15:43:13","canto_approved_date":"2025-09-04 06:30:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-06 15:42:50","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":150,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_16169489_phaf.tsv"}],"genes":["SPBC27B12.04c","SPAC25A8.02","SPAC27D7.05c","SPAC3A11.10c","SPBC15D4.02","SPBC4C3.04c","SPCC24B10.16c","SPCC11E10.03","SPAC4H3.03c","SPBC651.04","SPCC1442.02","SPAC13G7.09c","SPAC959.06c","SPBP35G2.02","SPAC6B12.16","SPAC31G5.18c","SPAC17A5.16","SPBC26H8.13c","SPBC32F12.08c","SPCC1223.13","SPAC1687.07","SPBC28E12.04","SPAC8C9.04","SPBC725.10","SPBC409.11","SPBC3E7.05c","SPBC83.04","SPAC18G6.12c","SPAC18G6.09c","SPBP4H10.10","SPBC6B1.04","SPAC17A2.07c","SPBC11C11.01","SPBC56F2.01","SPAP27G11.12","SPAC4D7.11","SPBC1539.02","SPAPB17E12.08","SPAC1039.08","SPAC688.06c","SPAC6G9.16c","SPBP8B7.30c","SPAC652.01","SPAC15A10.10","SPBC660.08","SPCC4B3.02c","SPAC17A5.05c","SPAC1556.06","SPBC18H10.07","SPCPJ732.03","SPAC57A7.13","SPBC19C2.10","SPBC31F10.08","SPAC12B10.10","SPAC11G7.05c","SPAC806.08c","SPBC428.07","SPAC25H1.05","SPAC1687.09","SPCC895.04c","SPAC15A10.07","SPBC1652.01","SPAC11D3.10","SPCC645.12c","SPBP22H7.04","SPBC27.03","SPAC8F11.08c","SPBC16E9.08","SPBC16C6.04","SPCC1620.07c","SPAC12B10.13","SPAC167.05","SPAC212.03","SPAC1002.18","SPBC428.04","SPBC18E5.13","SPAC17G6.13","SPCC1259.14c","SPBC19G7.04","SPAC24H6.08","SPCC417.12","SPAC17G6.17","SPBC1271.03c","SPAC29E6.07","SPCC553.01c","SPACUNK4.11c","SPAC17H9.03c","SPAC1F8.02c","SPBC13E7.06","SPBC21D10.08c","SPBC651.12c","SPBPB2B2.08","SPCC1739.04c","SPAC4G9.07","SPCC594.06c","SPAC12G12.09","SPBP23A10.14c","SPAC6C3.05","SPBC651.07","SPBP35G2.03c","SPAC17A5.09c","SPAC29A4.17c","SPBC31F10.15c","SPBC17G9.06c","SPBC30B4.03c","SPBC713.09","SPAC16A10.08c","SPBC409.17c","SPAC7D4.13c","SPCC4E9.01c","SPBC83.03c","SPAC30.03c","SPAC11D3.03c","SPBC1271.01c","SPBC15D4.11c","SPAC1F8.05","SPAC16E8.05c","SPBC1347.03","SPBC405.05","SPCC1393.02c","SPAPB1A10.08","SPBC28E12.01c","SPAC1565.02c","SPAC343.11c","SPBC36B7.06c","SPAC17A5.11","SPAC14C4.01c","SPAC17A5.18c","SPAC17G8.12","SPCC1442.13c","SPCC320.06","SPAC5D6.02c","SPAC17G8.09","SPAC14C4.08","SPAC6C3.02c","SPCC191.06","SPAC30D11.09","SPBC21C3.20c","SPBP8B7.28c","SPBC582.06c","SPCC191.01","SPAC19B12.10","SPAC3H8.04","SPCC613.11c","SPBC651.06","SPCC330.04c","SPAC4A8.02c","SPBC337.06c","SPAP27G11.02","SPBP8B7.13","SPBC17D11.01","SPCC622.19","SPAC140.04","SPAC1687.10"],"gene_count":154,"ltp_gene_count":153,"approved_date":"2014-03-06"},{"uniquename":"PMID:33280247","title":"The phosphatase inhibitor Sds23 promotes symmetric spindle positioning in fission yeast.","citation":"Cytoskeleton (Hoboken) 2020 Dec;77(12):544-557","abstract":"A hallmark of cell division in eukaryotic cells is the formation and elongation of a microtubule (MT)-based mitotic spindle. Proper positioning of the spindle is critical to ensure equal segregation of the genetic material to the resulting daughter cells. Both the timing of spindle elongation and constriction of the actomyosin contractile ring must be precisely coordinated to prevent missegregation or damage to the genetic material during cellular division. Here, we show that Sds23, an inhibitor of protein phosphatases, contributes to proper positioning of elongating spindles in fission yeast cells. We found that sds23∆ mutant cells exhibit asymmetric spindles that initially elongate asymmetrically toward one end of the dividing cell. Spindle asymmetry in sds23∆ cells results from a defect that is distinct from previously identified mechanisms, including MT protrusions and enlarged vacuoles. Combined with our previous work, this study demonstrates that Sds23, an inhibitor of PP2A-family protein phosphatases, promotes proper positioning of both the bipolar spindle and cytokinetic ring during fission yeast cell division. These two steps ensure the overall symmetry and fidelity of the cell division process.","doi":"10.1002/cm.21648","authors":"Schutt KL, Moseley JB","authors_abbrev":"Schutt KL et al.","pubmed_publication_date":"Dec 2020","pubmed_entrez_date":"2020-12-06","publication_year":"2020","canto_session_key":"72f6ce1ee2f8b315","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-12-08 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC646.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23093924","title":"Linkers of cell polarity and cell cycle regulation in the fission yeast protein interaction network.","citation":"PLoS Comput Biol 2012;8(10):e1002732","abstract":"The study of gene and protein interaction networks has improved our understanding of the multiple, systemic levels of regulation found in eukaryotic and prokaryotic organisms. Here we carry out a large-scale analysis of the protein-protein interaction (PPI) network of fission yeast (Schizosaccharomyces pombe) and establish a method to identify 'linker' proteins that bridge diverse cellular processes - integrating Gene Ontology and PPI data with network theory measures. We test the method on a highly characterized subset of the genome consisting of proteins controlling the cell cycle, cell polarity and cytokinesis and identify proteins likely to play a key role in controlling the temporal changes in the localization of the polarity machinery. Experimental inspection of one such factor, the polarity-regulating RNB protein Sts5, confirms the prediction that it has a cell cycle dependent regulation. Detailed bibliographic inspection of other predicted 'linkers' also confirms the predictive power of the method. As the method is robust to network perturbations and can successfully predict linker proteins, it provides a powerful tool to study the interplay between different cellular processes.","doi":"10.1371/journal.pcbi.1002732","authors":"Vaggi F, Dodgson J, Bajpai A, Chessel A, Jordán F, Sato M, Carazo-Salas RE, Csikász-Nagy A","authors_abbrev":"Vaggi F et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-10-25","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPAB1289","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16263721","title":"Hsk1-Dfp1/Him1, the Cdc7-Dbf4 kinase in Schizosaccharomyces pombe, associates with Swi1, a component of the replication fork protection complex.","citation":"J Biol Chem 2005 Dec 30;280(52):42536-42","abstract":"The protein kinase Hsk1 is essential for DNA replication in Schizosaccharomyces pombe. It associates with Dfp1/Him1 to form an active complex equivalent to the Cdc7-Dbf4 protein kinase in Saccharomyces cerevisiae. Swi1 and Swi3 are subunits of the replication fork protection complex in S. pombe that is homologous to the Tof1-Csm3 complex in S. cerevisiae. The fork protection complex helps to preserve the integrity of stalled replication forks and is important for activation of the checkpoint protein kinase Cds1 in response to fork arrest. Here we describe physical and genetic interactions involving Swi1 and Hsk1-Dfp1/Him1. Dfp1/Him1 was identified in a yeast two-hybrid screen with Swi1. Hsk1 and Dfp1/Him1 both co-immunoprecipitate with Swi1. Swi1 is required for growth of a temperature-sensitive hsk1 (hsk1ts) mutant at its semi-permissive temperature. Hsk1ts cells accumulate Rad22 (Rad52 homologue) DNA repair foci at the permissive temperature, as previously observed in swi1 cells, indicating that abnormal single-stranded DNA regions form near the replication fork in hsk1ts cells. hsk1ts cells were also unable to properly delay S-phase progression in the presence of a DNA alkylating agent and were partially defective in mating type switching. These data suggest that Hsk1-Dfp1/Him1 and Swi1-Swi3 complexes have interrelated roles in stabilization of arrested replication forks.","authors":"Matsumoto S, Ogino K, Noguchi E, Russell P, Masai H","authors_abbrev":"Matsumoto S et al.","pubmed_publication_date":"30 Dec 2005","pubmed_entrez_date":"2005-11-03","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4.04c","SPCC550.13","SPCC1259.13","SPBC216.06c","SPBC776.12c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:12237853","title":"What similarity between human and fission yeast proteins is required for orthology?","citation":"Yeast 2002 Sep 30;19(13):1125-6","abstract":"","authors":"Lenaers G, Pelloquin L, Olichon A, Emorine LJ, Guillou E, Delettre C, Hamel CP, Ducommun B, Belenguer P","authors_abbrev":"Lenaers G et al.","pubmed_publication_date":"30 Sep 2002","pubmed_entrez_date":"2002-09-19","publication_year":"2002","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8341608","title":"Nucleotide sequence of the Schizosaccharomyces pombe 25S ribosomal RNA and its phylogenetic implications.","citation":"Nucleic Acids Res 1993 Jul 11;21(14):3322","abstract":"","authors":"Lapeyre B, Michot B, Feliu J, Bachellerie JP","authors_abbrev":"Lapeyre B et al.","pubmed_publication_date":"11 Jul 1993","pubmed_entrez_date":"1993-07-11","publication_year":"1993","canto_session_key":"0fc11a02fab7f8f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-02-02 04:18:39","canto_approved_date":"2019-02-02 04:18:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-02 04:18:26","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC694.05c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-02-02"},{"uniquename":"PMID:14596912","title":"The protein kinase kin1, the fission yeast orthologue of mammalian MARK/PAR-1, localises to new cell ends after mitosis and is important for bipolar growth.","citation":"FEBS Lett 2003 Nov 06;554(1-2):45-9","abstract":"The kin1 protein kinase of the fission yeast Schizosaccharomyces pombe is a member of the PAR-1/MARK (partitioning-defective 1/microtubule-associated protein/microtubule affinity-regulating kinase) family important in eukaryotic cell polarity and cytoskeletal dynamics. We show here that kin1 plays a role in establishing the characteristic rod-shaped morphology of fission yeast. Cells in which kin1 was deleted are viable but are impaired in growth, and are rounded at one end or both ends. They are monopolar because after mitosis they fail to activate bipolar growth, and are delayed in cytokinesis, resulting in a high proportion of septated cells often with multiple septa. This phenotype can be partially rescued by heterologous expression of human MARKs, which restore bipolar growth in most cells, but do not correct the delay in cytokinesis. Using chromosomal epitope tagging, we show that kin1p localises to the cell ends, except during mitosis when it disappears from cell ends. After mitosis, kin1p first reappears at the new cell end. Overexpression of kin1 results in a loss of polarity, with partially or fully rounded cells. From these results we suggest that kin1 is required to direct the growth machinery to the cell ends.","authors":"Drewes G, Nurse P","authors_abbrev":"Drewes G et al.","pubmed_publication_date":"06 Nov 2003","pubmed_entrez_date":"2003-11-05","publication_year":"2003","canto_session_key":"51fd8f8f17004d6a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-29 08:31:08","canto_approved_date":"2026-04-02 15:36:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-20 09:12:36","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.03c","SPCC1223.06","SPBC4F6.06"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-08-29"},{"uniquename":"PMID:29199950","title":"Ragulator and GATOR1 complexes promote fission yeast growth by attenuating TOR complex 1 through Rag GTPases.","citation":"Elife 2017 Dec 04;6","abstract":"TOR complex 1 (TORC1) is an evolutionarily conserved protein kinase complex that promotes cellular macromolecular synthesis and suppresses autophagy. Amino-acid-induced activation of mammalian TORC1 is initiated by its recruitment to the RagA/B-RagC/D GTPase heterodimer, which is anchored to lysosomal membranes through the Ragulator complex. We have identified in the model organism  Schizosaccharomyces pombe  a Ragulator-like complex that tethers the Gtr1-Gtr2 Rag heterodimer to the membranes of vacuoles, the lysosome equivalent in yeasts. Unexpectedly, the Ragulator-Rag complex is not required for the vacuolar targeting of TORC1, but the complex plays a crucial role in attenuating TORC1 activity independently of the Tsc1-Tsc2 complex, a known negative regulator of TORC1 signaling. The GATOR1 complex, which functions as Gtr1 GAP, is essential for the TORC1 attenuation by the Ragulator-Rag complex, suggesting that Gtr1 GDP -Gtr2 on vacuolar membranes moderates TORC1 signaling for optimal cellular response to nutrients.","doi":"10.7554/eLife.30880","authors":"Chia KH, Fukuda T, Sofyantoro F, Matsuda T, Amai T, Shiozaki K","authors_abbrev":"Chia KH et al.","pubmed_publication_date":"04 Dec 2017","pubmed_entrez_date":"2017-12-05","publication_year":"2017","canto_session_key":"07fb3e57038e972d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomoyuki Fukuda","canto_first_approved_date":"2018-01-28 17:37:38","canto_approved_date":"2024-04-04 09:18:23","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-12-18 07:06:44","canto_added_date":"2017-12-06 01:15:15","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":283,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Tomoyuki Fukuda","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.07c","SPBC12D12.03","SPCC777.05","SPCC4G3.08","SPBC29A10.17","HGNC:29796","SPBC26H8.04c","SPBC428.16c","SPAC23H3.03c","SPAC15F9.02","SPBC337.13c","SPAC1B9.02c","SPAC11E3.05","HGNC:26068","SPAC12G12.01c","SPBC215.15","HGNC:15606","SPAC57A7.11","SPBC18H10.20c","SPAC22F3.13","SPAC630.13c","SPAC23D3.16","HGNC:33772","SPBC1778.05c","SPAC222.19","SPAC869.11","SPAC11G7.02","SPBC543.04"],"gene_count":24,"ltp_gene_count":23,"approved_date":"2018-01-28"},{"uniquename":"PMID:7808414","title":"Analysis of a histone H2A variant from fission yeast: evidence for a role in chromosome stability.","citation":"Mol Gen Genet 1994 Dec 01;245(5):628-35","abstract":"We have isolated and characterised the pht1 gene from the fission yeast Schizosaccharomyces pombe. The sequence of the predicted translation product has revealed a striking similarity to the family of H2A.F/Z histone variant proteins, which have been found in a variety of different organisms. Cells deleted for the pht1 gene locus grow slowly, exhibit an altered colony morphology, increased resistance to heat shock and show a significant decrease in the fidelity of segregation of an S. pombe minichromosome. We propose that the histone H2A variant encoded by the pht1 gene is important for chromosomal structure and function, possibly including a role in controlling the fidelity of chromosomal segregation during mitosis.","authors":"Carr AM, Dorrington SM, Hindley J, Phear GA, Aves SJ, Nurse P","authors_abbrev":"Carr AM et al.","pubmed_publication_date":"01 Dec 1994","pubmed_entrez_date":"1994-12-01","publication_year":"1994","canto_session_key":"c8d07f311b06a96a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-05 10:55:55","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-01 14:43:22","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-01"},{"uniquename":"PMID:41296734","title":"ATG2 is a triglyceride transfer protein.","citation":"Proc Natl Acad Sci U S A 2025 Dec 02;122(48):e2517469122","abstract":"Bridge-like lipid transfer proteins (BLTPs) are established to function in phospholipid transport between bilayers at organelle-organelle contact sites. However, the BLTP ATG2A also associates with lipid droplets in cells, which present a unique phospholipid monolayer topology and which are composed of many additional types of lipids. Whether BLTPs are active in this environment and which lipid species are substrates for transport has been unknown. Here, we use synthetic organelles with bilayers (liposomes), monolayers (artificial lipid droplets), or a mixture of the two membrane structures to demonstrate the tight binding of ATG2 specifically to monolayers via its collection of COOH-terminal amphipathic helices. This stable binding enables ATG2 to transfer phospholipids much more effectively. Unexpectedly, the neutral lipid triacylglycerol is also rapidly transported, with kinetics similar to those of phospholipid transport. Lipidomics of purified ATG2A suggests that a similar transfer of both phospholipids and triacylglycerol occurs in cells. Our work implies that BLTPs likely collect on LDs as part of a broad lipid homeostasis program, which will include the movement of both phospholipids and neutral lipids.","doi":"10.1073/pnas.2517469122","authors":"Korfhage JL, Elhan H, Wan N, Lu Y, Kauffmann L, Pilli G, Fuller DM, Rios AM, Reinisch KM, Maddipati KR, Thiam AR, Melia TJ","authors_abbrev":"Korfhage JL et al.","pubmed_publication_date":"02 Dec 2025","pubmed_entrez_date":"2025-11-26","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC31E1.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:4610086","title":"Tellurite reduction in Schizosaccharomyces pombe.","citation":"J Gen Microbiol 1974 Aug;83(2):389-92","abstract":"","authors":"Smith DG","authors_abbrev":"Smith DG","pubmed_publication_date":"Aug 1974","pubmed_entrez_date":"1974-08-01","publication_year":"1974","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38169665","title":"DPred_3S: identifying dihydrouridine (D) modification on three species epitranscriptome based on multiple sequence-derived features.","citation":"Front Genet 2023;14:1334132","abstract":" Introduction:  Dihydrouridine (D) is a conserved modification of tRNA among all three life domains. D modification enhances the flexibility of a single nucleotide base in the spatial structure and is disease- and evolution-associated. Recent studies have also suggested the presence of dihydrouridine on mRNA.  Methods:  To identify D in epitranscriptome, we provided a prediction framework named \"DPred_3S\" based on the machine learning approach for three species D epitranscriptome, which used epitranscriptome sequencing data as training data for the first time.  Results:  The optimal features were evaluated by the F-score and integration of different features; our model achieved area under the receiver operating characteristic curve (AUROC) scores 0.955, 0.946, and 0.905 for  Saccharomyces cerevisiae ,  Escherichia coli , and  Schizosaccharomyces pombe , respectively. The performances of different machine learning algorithms were also compared in this study.  Discussion:  The high performances of our model suggest the D sites can be distinguished based on their surrounding sequence, but the lower performance of cross-species prediction may be limited by technique preferences.","doi":"10.3389/fgene.2023.1334132","authors":"Ren J, Chen X, Zhang Z, Shi H, Wu S","authors_abbrev":"Ren J et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2024-01-03","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-01-05 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15328083","title":"The melaminophenyl arsenicals melarsoprol and melarsen oxide interfere with thiamine metabolism in the fission yeast Schizosaccharomyces pombe.","citation":"Antimicrob Agents Chemother 2004 Sep;48(9):3268-71","abstract":"The melaminophenyl arsenical melarsoprol is the main drug used against late-stage sleeping sickness caused by Trypanosoma brucei subspecies. Its active metabolite in the human body is melarsen oxide. Here, it is shown that this metabolite inhibits growth of the fission yeast Schizosaccharomyces pombe and that its toxicity can be abolished efficiently by thiamine (vitamin B(1)), thiamine analogues, and the pyrimidine moiety of the thiamine molecule. Uptake of melarsen oxide is mediated by a membrane protein (car1p), which is involved in the uptake of thiamine and its pyrimidine moiety. Melarsoprol is taken up by cells in a thiamine- and car1p-dependent manner but is not toxic to cells.","authors":"Schweingruber ME","authors_abbrev":"Schweingruber ME","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-08-26","publication_year":"2004","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11058134","title":"Mutant alleles of Schizosaccharomyces pombe rad9(+) alter hydroxyurea resistance, radioresistance and checkpoint control.","citation":"Nucleic Acids Res 2000 Nov 01;28(21):4340-9","abstract":"Schizosaccharomyces pombe rad9 mutations can render cells sensitive to hydroxyurea (HU), gamma-rays and UV light and eliminate associated checkpoint controls. In vitro mutagenesis was performed on S.pombe rad9 and altered alleles were transplaced into the genome to ascertain the functional significance of five groups of evolutionarily conserved amino acids. Most targeted regions were changed to alanines, whereas rad9-S3 encodes a protein devoid of 22 amino acids normally present in yeast but absent from mammalian Rad9 proteins. We examined whether these rad9 alleles confer radiation and HU sensitivity and whether the sensitivities correlate with checkpoint control deficiencies. One rad9 mutant allele was fully active, whereas four others demonstrated partial loss of function. rad9-S1, which contains alterations in a BH3-like domain, conferred HU resistance but increased sensitivity to gamma-rays and UV light, without affecting checkpoint controls. rad9-S2 reduced gamma-ray sensitivity marginally, without altering other phenotypes. Two alleles, rad9-S4 and rad9-S5, reduced HU sensitivity, radiosensitivity and caused aberrant checkpoint function. HU-induced checkpoint control could not be uncoupled from drug resistance. These results establish unique as well as overlapping functional domains within Rad9p and provide evidence that requirements of the protein for promoting resistance to radiation and HU are not identical.","authors":"Hang H, Rauth SJ, Hopkins KM, Lieberman HB","authors_abbrev":"Hang H et al.","pubmed_publication_date":"01 Nov 2000","pubmed_entrez_date":"2000-11-01","publication_year":"2000","canto_session_key":"fbb30df4ab796e5b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-08 15:01:10","canto_approved_date":"2021-02-08 09:24:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-08 15:01:00","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-08"},{"uniquename":"PMID:27350684","title":"Mutant allele of rna14 in fission yeast affects pre-mRNA splicing.","citation":"J Genet 2016 Jun;95(2):389-97","abstract":"Spliceosome and 3'-end processing complexes are necessary for the precursor mRNA (pre-mRNA) maturation. Spliceosome complex removes noncoding introns, while 3'-end processing involves in cleavage and addition of poly(A) tails to the nascent transcript. Rna14 protein in budding yeast has been implicated in cleavage and polyadenylation of mRNA in the nucleus but their role in the pre-mRNA splicing has not been studied. Here, we report the isolation of a mutant allele of rna14 in fission yeast, Schizosaccharomyces pombe that exhibits reduction in protein level of Chk1 at the nonpermissive temperature, primarily due to the defects in posttranscriptional processing. Reverse transcriptase-polymerase chain reaction analysis reveals defective splicing of the chk1(+) transcript at the nonpermissive temperature. Apart from chk1(+), the splicing of some other genes were also found to be defective at the nonpermissive temperature suggesting that Rna14 might be involved in pre-mRNA splicing. Subsequently, genetic interaction of Rna14 with prp1 and physical interactions with Prp28 suggest that the Rna14 might be part of a larger protein complex responsible for the pre-mRNA maturation.","authors":"Yadav S, Sonkar A, Ahamad N, Ahmed S","authors_abbrev":"Yadav S et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-06-29","publication_year":"2016","canto_session_key":"bb51c9f75714cc60","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shakil Ahmed","canto_first_approved_date":"2016-08-01 14:18:11","canto_approved_date":"2026-01-31 14:14:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-01 06:33:41","canto_added_date":"2016-06-30 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Shakil Ahmed","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPBC20F10.06","SPCC338.17c","SPBC26H8.07c","SPAC6F12.17","SPCC63.11","SPBC6B1.07"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2016-08-01"},{"uniquename":"PMID:19763952","title":"Top2 SUMO conjugation in yeast cell lysates.","citation":"Methods Mol Biol 2009;582:209-19","abstract":"DNA topoisomerase II (Topo II), named Top2 in budding and fission yeast, is a conserved target of the SUMO modification pathway, with SUMO-conjugated forms of Topo II accumulating specifically during mitosis in both yeast and vertebrate cells (Bachant et al., Mol Cell 9, 1169-82, 2002; Azuma et al., J Cell Biol 163, 477-87, 2003; Dawlaty et al., Cell 133, 103-15, 2008). As with many SUMO substrates, the functional significance of this modification is still incompletely understood and, perhaps surprisingly, better characterized in vertebrates than yeasts. It seems likely, however, that continued analysis of yeast Top2 SUMO modification will reveal commonalities with vertebrate cells, leading to a deeper understanding of how sumoylation regulates Topo II function. Toward this end, we describe a protocol for analyzing yeast Top2 SUMO conjugates in vivo.","doi":"10.1007/978-1-60761-340-4_16","authors":"Baldwin M, Bachant J","authors_abbrev":"Baldwin M et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-09-19","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35713287","title":"SAIBR: a simple, platform-independent method for spectral autofluorescence correction.","citation":"Development 2022 Jul 15;149(14)","abstract":"Biological systems are increasingly viewed through a quantitative lens that demands accurate measures of gene expression and local protein concentrations. CRISPR/Cas9 gene tagging has enabled increased use of fluorescence to monitor proteins at or near endogenous levels under native regulatory control. However, owing to typically lower expression levels, experiments using endogenously tagged genes run into limits imposed by autofluorescence (AF). AF is often a particular challenge in wavelengths occupied by commonly used fluorescent proteins (GFP, mNeonGreen). Stimulated by our work in C. elegans, we describe and validate Spectral Autofluorescence Image Correction By Regression (SAIBR), a simple platform-independent protocol and FIJI plug-in to correct for autofluorescence using standard filter sets and illumination conditions. Validated for use in C. elegans embryos, starfish oocytes and fission yeast, SAIBR is ideal for samples with a single dominant AF source; it achieves accurate quantitation of fluorophore signal, and enables reliable detection and quantification of even weakly expressed proteins. Thus, SAIBR provides a highly accessible low-barrier way to incorporate AF correction as standard for researchers working on a broad variety of cell and developmental systems.","doi":"10.1242/dev.200545","authors":"Rodrigues NTL, Bland T, Borrego-Pinto J, Ng K, Hirani N, Gu Y, Foo S, Goehring NW","authors_abbrev":"Rodrigues NTL et al.","pubmed_publication_date":"15 Jul 2022","pubmed_entrez_date":"2022-06-17","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-06-22 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29974182","title":"A current view on long noncoding RNAs in yeast and filamentous fungi.","citation":"Appl Microbiol Biotechnol 2018 Sep;102(17):7319-7331","abstract":"Long noncoding RNAs (lncRNAs) are crucial players in epigenetic regulation. They were initially discovered in human, yet they emerged as common factors involved in a number of central cellular processes in several eukaryotes. For example, in the past decade, research on lncRNAs in yeast has steadily increased. Several examples of lncRNAs were described in Saccharomyces cerevisiae and Schizosaccharomyces pombe. Also, screenings for lncRNAs in ascomycetes were performed and, just recently, the first full characterization of a lncRNA was performed in the filamentous fungus Trichoderma reesei. In this review, we provide a broad overview about currently known fugal lncRNAs. We make an attempt to categorize them according to their functional context, regulatory strategies or special properties. Moreover, the potential of lncRNAs as a biotechnological tool is discussed.","doi":"10.1007/s00253-018-9187-y","authors":"Till P, Mach RL, Mach-Aigner AR","authors_abbrev":"Till P et al.","pubmed_publication_date":"Sep 2018","pubmed_entrez_date":"2018-07-06","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-07-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2078560","title":"A fission yeast genome project.","citation":"New Biol 1990 Oct;2(10):929","abstract":"","authors":"","authors_abbrev":"","pubmed_publication_date":"Oct 1990","pubmed_entrez_date":"1990-10-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31503417","title":"Whole-Genome Sequencing of Yeast Cells.","citation":"Curr Protoc Mol Biol 2019 Sep;128(1):e103","abstract":"The budding yeast, Saccharomyces cerevisiae, has been widely used for genetic studies of fundamental cellular functions. The isolation and analysis of yeast mutants is a commonly used and powerful technique to identify the genes that are involved in a process of interest. Furthermore, natural genetic variation among wild yeast strains has been studied for analysis of polygenic traits by quantitative trait loci mapping. Whole-genome sequencing, often combined with bulk segregant analysis, is a powerful technique that helps determine the identity of mutations causing a phenotype. Here, we describe protocols for the construction of libraries for S. cerevisiae whole-genome sequencing. We also present a bioinformatic pipeline to determine the genetic variants in a yeast strain using whole-genome sequencing data. This pipeline can also be used for analyzing Schizosaccharomyces pombe mutants. © 2019 by John Wiley & Sons, Inc. Basic Protocol 1: Generation of haploid spores for bulk segregant analysis Basic Protocol 2: Extraction of genomic DNA from yeast cells Basic Protocol 3: Shearing of genomic DNA for library preparation Basic Protocol 4: Construction and amplification of DNA libraries Support Protocol 1: Annealing oligonucleotides for forming Y-adapters Support Protocol 2: Size selection and cleanup using SPRI beads Basic Protocol 5: Identification of genomic variants from sequencing data.","doi":"10.1002/cpmb.103","authors":"Gopalakrishnan R, Winston F","authors_abbrev":"Gopalakrishnan R et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-09-11","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-09-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26547444","title":"Immuno-capture of UVDE generated 3'-OH ends at UV photoproducts.","citation":"DNA Repair (Amst) 2015 Dec;36:156-161","abstract":"A strategy amenable to the genome-wide study of DNA damage and repair kinetics is described. The ultraviolet damage endonuclease (UVDE) generates 3'-OH ends at the two major UV induced DNA lesions, cyclobutane pyrimidine dimers (CPDs) and 6,4 pyrimidine-pyrimidone dimers (6,4 PPs), allowing for their capture after biotin end-labeling. qPCR amplification of biotinylated DNA enables parallel measuring of DNA damage in several loci, which can then be combined with high-throughput screening of cell survival to test genotoxic reagents. Alternatively, a library of captured sequences could be generated for a genome wide study of damage sites and large-scale assessment of repair kinetics in different regions of the genome, using next-generation sequencing. The assay is suitable to study any DNA lesion that can be converted into 3'-OH by UVDE, or other enzymes. Toward these goals, we compared UVDE with the classical T4 endonuclease V (T4V) assay. We showed that there is a linear correlation between UV dose, 3'-OH formation and capture by immunoprecipitation, together with its potential application for in vivo studies.","doi":"10.1016/j.dnarep.2015.09.019","authors":"Peyresaubes F, D'Amours A, Leduc F, Grégoire MC, Boissonneault G, Conconi A","authors_abbrev":"Peyresaubes F et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-11-09","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-08-20 00:16:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12514100","title":"Checkpoint activation regulates mutagenic translesion synthesis.","citation":"Genes Dev 2003 Jan 01;17(1):64-76","abstract":"Cells have evolved checkpoint responses to arrest or delay the cell cycle, activate DNA repair networks, or induce apoptosis after genomic perturbation. Cells have also evolved the translesion synthesis processes to tolerate genomic lesions by either error-free or error-prone repair. Here, we show that after a replication perturbation, cells exhibit a mutator phenotype, which can be significantly affected by mutations in the checkpoint elements Cds1 and Rad17 or translesion synthesis polymerases DinB and Polzeta. Cells respond to genomic perturbation by up-regulation of DinB in a checkpoint activation-dependent manner. Moreover, association of DinB with chromatin is dependent on functional Rad17, and DinB physically interacts with the checkpoint-clamp components Hus1 and Rad1. Thus, translesion synthesis is a part of the checkpoint response.","authors":"Kai M, Wang TS","authors_abbrev":"Kai M et al.","pubmed_publication_date":"01 Jan 2003","pubmed_entrez_date":"2003-01-07","publication_year":"2003","canto_session_key":"25c44b9071bd33a2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-12 10:38:11","canto_approved_date":"2024-04-02 16:19:29","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-03-03 15:08:32","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC1952.07","SPAC14C4.13","SPAC20G4.04c","SPCC18B5.11c","SPCC553.07c","SPAC688.10","SPCC1259.13","SPAC664.07c","SPAC9E9.08","SPAC3H5.06c","SPBC16A3.11"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2017-01-12"},{"uniquename":"PMID:28794351","title":"Unexpected roles of a shugoshin protein at subtelomeres.","citation":"Genes Genet Syst 2018 Jan 20;92(3):127-133","abstract":"A chromosome is composed of structurally and functionally distinct domains. Telomeres, which are located at the ends of linear chromosomes, play crucial roles in genome stability. Although substantial knowledge of telomeres has been accumulated, the regulation and function of subtelomeres, which are the domains adjacent to telomeres, remain largely unknown. In this review, I describe recent discoveries about the multiple roles of a shugoshin family protein, Sgo2, which is localized at centromeres in mitosis and contributes to precise chromosome segregation, in defining chromatin structure and functions of the subtelomeres in fission yeast. Sgo2 becomes enriched at the subtelomeres, particularly during G 2  phase, and is essential for the formation of a highly condensed subtelomeric chromatin body called the knob. Furthermore, Sgo2 maintains the expression levels of subtelomeric genes and the timing of DNA replication at subtelomeric late origins.","doi":"10.1266/ggs.17-00016","authors":"Kanoh J","authors_abbrev":"Kanoh J","pubmed_publication_date":"20 Jan 2018","pubmed_entrez_date":"2017-08-11","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-08-12 00:15:23","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25377082","title":"Enhanced deacidification activity in Schizosaccharomyces pombe by genome shuffling.","citation":"Yeast 2015 Feb;32(2):317-25","abstract":"A problem frequently occurring in making some kinds of wines, particularly Vitis quinquangularis Rehd wine, is the presence of malic acid at high concentrations, which is detrimental to the quality of wines. Thus, there is a need of the ways for effectively reducing the malic acid levels in wine. This study aimed to generate shuffled fusants of Schizosaccharomyces pombe with enhanced deacidification activity for reducing the excessive malic acid content in wine. Sz. pombe CGMCC 2.1628 was used as the original strain. The starting mutant population was generated by UV treatment. The mutants with higher deacidification activity were selected and subjected to recursive protoplast fusion. The resulting fusants were screened by using the indicator of malic acid concentration of fermentation supernatants on 96-well microtitre plates, measured with bromocresol green. After three rounds of genome shuffling, the best-performing fusant, named GS3-1, was obtained. Its deacidification activity (consumed 4.78 g/l malic acid within 10 days) was increased by 225.2% as compared to that of original strain. In the Vitis quinquangularis Rehd wine fermentation test, GS3-1 consumed 4.0 g/l malic acid during the whole cycle of fermentation, providing up to 185.7% improvement in malic acid consumption compared with that of the original strain. This study shows that GS3-1 has great potential for improving the quality of Vitis quinquangularis Rehd wine.","doi":"10.1002/yea.3053","authors":"Ding S, Zhang Y, Zhang J, Zeng W, Yang Y, Guan J, Pan L, Li W","authors_abbrev":"Ding S et al.","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2014-11-08","publication_year":"2015","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2014-11-09 01:15:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37317152","title":"The Life of  Saccharomyces  and Non- Saccharomyces  Yeasts in Drinking Wine.","citation":"Microorganisms 2023 Apr 30;11(5)","abstract":"Drinking wine is a processed beverage that offers high nutritional and health benefits. It is produced from grape must, which undergoes fermentation by yeasts (and sometimes lactic acid bacteria) to create a product that is highly appreciated by consumers worldwide. However, if only one type of yeast, specifically  Saccharomyces cerevisiae , was used in the fermentation process, the resulting wine would lack aroma and flavor and may be rejected by consumers. To produce wine with a desirable taste and aroma, non- Saccharomyces  yeasts are necessary. These yeasts contribute volatile aromatic compounds that significantly impact the wine's final taste. They promote the release of primary aromatic compounds through a sequential hydrolysis mechanism involving several glycosidases unique to these yeasts. This review will discuss the unique characteristics of these yeasts ( Schizosaccharomyces pombe ,  Pichia kluyveri ,  Torulaspora delbrueckii ,  Wickerhamomyces anomalus ,  Metschnikowia pulcherrima ,  Hanseniaspora vineae ,  Lachancea thermotolerans ,  Candida stellata , and others) and their impact on wine fermentations and co-fermentations. Their existence and the metabolites they produce enhance the complexity of wine flavor, resulting in a more enjoyable drinking experience.","doi":"10.3390/microorganisms11051178","authors":"Maicas S, Mateo JJ","authors_abbrev":"Maicas S et al.","pubmed_publication_date":"30 Apr 2023","pubmed_entrez_date":"2023-06-15","publication_year":"2023","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2023-06-16 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30297429","title":"Cryo-ET reveals the macromolecular reorganization of  S. pombe  mitotic chromosomes in vivo.","citation":"Proc Natl Acad Sci U S A 2018 Oct 23;115(43):10977-10982","abstract":"Chromosomes condense during mitosis in most eukaryotes. This transformation involves rearrangements at the nucleosome level and has consequences for transcription. Here, we use cryo-electron tomography (cryo-ET) to determine the 3D arrangement of nuclear macromolecular complexes, including nucleosomes, in frozen-hydrated  Schizosaccharomyces pombe  cells. Using 3D classification analysis, we did not find evidence that nucleosomes resembling the crystal structure are abundant. This observation and those from other groups support the notion that a subset of fission yeast nucleosomes may be partially unwrapped in vivo. In both interphase and mitotic cells, there is also no evidence of monolithic structures the size of Hi-C domains. The chromatin is mingled with two features: pockets, which are positions free of macromolecular complexes; and \"megacomplexes,\" which are multimegadalton globular complexes like preribosomes. Mitotic chromatin is more crowded than interphase chromatin in subtle ways. Nearest-neighbor distance analyses show that mitotic chromatin is more compacted at the oligonucleosome than the dinucleosome level. Like interphase, mitotic chromosomes contain megacomplexes and pockets. This uneven chromosome condensation helps explain a longstanding enigma of mitosis: a subset of genes is up-regulated.","doi":"10.1073/pnas.1720476115","authors":"Cai S, Chen C, Tan ZY, Huang Y, Shi J, Gan L","authors_abbrev":"Cai S et al.","pubmed_publication_date":"23 Oct 2018","pubmed_entrez_date":"2018-10-10","publication_year":"2018","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2018-10-11 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25395321","title":"pREPORT: a multi-readout transcription reporter vector for fission yeast.","citation":"Yeast 2015 Feb;32(2):327-34","abstract":"Transcription factors are prominent regulators of gene expression that execute responses to various intracellular and extracellular stimuli. Recombinant transcription reporter systems can be conveniently used to study the DNA binding preferences and regulatory activity of a transcription factor under a range of conditions. Several reporter genes have been used to study transcription regulation in the fission yeast Schizosaccharomyces pombe. Each of these reporters has distinct advantages, such as high sensitivity or ease of use, and limitations, such as prohibitive costs or use of hazardous substances. To combine the strengths and mitigate the weaknesses of individual reporter genes, we have created pREPORT, a flexible multi-readout transcription reporter vector for fission yeast that employs an enhanced GFP-lacZ fusion and a customizable minimal promoter. With pREPORT, gene expression driven by the transcription factor of interest can be quantified in a number of ways, both in live cells and in vitro, using a single reporter construct.","doi":"10.1002/yea.3055","authors":"Převorovský M","authors_abbrev":"Převorovský M","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2014-11-15","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-11-16 01:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39833470","title":"Structures of aberrant spliceosome intermediates on their way to disassembly.","citation":"Nat Struct Mol Biol 2025 Jan 20;","abstract":"Intron removal during pre-mRNA splicing is of extraordinary complexity and its disruption causes a vast number of genetic diseases in humans. While key steps of the canonical spliceosome cycle have been revealed by combined structure-function analyses, structural information on an aberrant spliceosome committed to premature disassembly is not available. Here, we report two cryo-electron microscopy structures of post-B act  spliceosome intermediates from Schizosaccharomyces pombe primed for disassembly. We identify the DEAH-box helicase-G-patch protein pair (Gih35-Gpl1, homologous to human DHX35-GPATCH1) and show how it maintains catalytic dormancy. In both structures, Gpl1 recognizes a remodeled active site introduced by an overstabilization of the U5 loop I interaction with the 5' exon leading to a single-nucleotide insertion at the 5' splice site. Remodeling is communicated to the spliceosome surface and the Ntr1 complex that mediates disassembly is recruited. Our data pave the way for a targeted analysis of splicing quality control.","doi":"10.1038/s41594-024-01480-7","authors":"Soni K, Horvath A, Dybkov O, Schwan M, Trakansuebkul S, Flemming D, Wild K, Urlaub H, Fischer T, Sinning I","authors_abbrev":"Soni K et al.","pubmed_publication_date":"20 Jan 2025","pubmed_entrez_date":"2025-01-20","publication_year":"2025","canto_session_key":"173716a70c23fb6b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-01-22 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F8.12c","SPBC3E7.14","SPBC11G11.06c","SPAC20H4.06c","SPAC20H4.09","SPAC57A10.03","SPCC364.02c","SPBC19C2.14","SPAC27D7.07c","SPBC31F10.11c","SPBC4B4.05","SPBC6B1.10","SPBC18H10.10c","SPAC17A2.08c","SPAC3A12.11c","SPBC215.12","SPBP22H7.07","SPBC211.02c","SPAC2C4.03c","SPCC550.02c","SPBC24C6.11","SPBC13E7.01","SPBC337.06c","SPAC644.12","SPAC4A8.09c","SPBC1289.11","SPBC646.02","SPAC26A3.08","SPCC188.11","SPAC29A4.08c","SPBC28F2.04c","SPBC3E7.13c","SPAC1486.03c"],"gene_count":33,"ltp_gene_count":33,"pdb_entries":[{"pdb_id":"9esi","gene_chains":[{"gene_uniquename":"SPBP22H7.07","chain":"K","position":"1-473"},{"gene_uniquename":"SPAC17A2.08c","chain":"n","position":"1-361"},{"gene_uniquename":"SPAC29A4.08c","chain":"S/T/U/V","position":"1-488"},{"gene_uniquename":"SPAC2C4.03c","chain":"G","position":"1-115"},{"gene_uniquename":"SPAC4A8.09c","chain":"b","position":"1-293"},{"gene_uniquename":"SPAC4F8.12c","chain":"A","position":"1-2363"},{"gene_uniquename":"SPAC27D7.07c","chain":"F","position":"1-117"},{"gene_uniquename":"SPBC6B1.10","chain":"a","position":"1-558"},{"gene_uniquename":"SPBC3E7.13c","chain":"Y","position":"1-229"},{"gene_uniquename":"SPBC3E7.14","chain":"I","position":"1-78"},{"gene_uniquename":"SPCC364.02c","chain":"e","position":"1-384"},{"gene_uniquename":"SPCC550.02c","chain":"M","position":"1-354"},{"gene_uniquename":"SPBC18H10.10c","chain":"p","position":"1-299"},{"gene_uniquename":"SPBC24C6.11","chain":"O","position":"1-146"},{"gene_uniquename":"SPBC4B4.05","chain":"J","position":"1-77"},{"gene_uniquename":"SPBC215.12","chain":"B","position":"1-984"},{"gene_uniquename":"SPBC646.02","chain":"N","position":"1-1284"},{"gene_uniquename":"SPBC1289.11","chain":"C","position":"1-340"},{"gene_uniquename":"SPAC644.12","chain":"W","position":"1-757"},{"gene_uniquename":"SPBC337.06c","chain":"Q","position":"1-265"},{"gene_uniquename":"SPAC57A10.03","chain":"d","position":"1-155"},{"gene_uniquename":"SPAC3A12.11c","chain":"P","position":"1-388"},{"gene_uniquename":"SPBC31F10.11c","chain":"R","position":"1-674"},{"gene_uniquename":"SPCC188.11","chain":"L","position":"1-557"},{"gene_uniquename":"SPAC26A3.08","chain":"E","position":"1-147"},{"gene_uniquename":"SPAC20H4.09","chain":"z","position":"1-647"},{"gene_uniquename":"SPAC20H4.06c","chain":"y","position":"1-534"},{"gene_uniquename":"SPBC13E7.01","chain":"c","position":"1-887"},{"gene_uniquename":"SPBC211.02c","chain":"X","position":"1-790"},{"gene_uniquename":"SPBC28F2.04c","chain":"Z","position":"1-187"},{"gene_uniquename":"SPBC11G11.06c","chain":"H","position":"1-84"},{"gene_uniquename":"SPAC1486.03c","chain":"m","position":"1-797"},{"gene_uniquename":"SPBC19C2.14","chain":"D","position":"1-97"}],"title":"Structure of a B-state intermediate committed to discard (Bd-II state)","entry_authors":"Soni K,Wild K,Sinning I","entry_authors_abbrev":"Soni K et al.","reference_uniquename":"PMID:39833470","experimental_method":"EM","resolution":"3.1"},{"pdb_id":"9esh","gene_chains":[{"gene_uniquename":"SPBP22H7.07","chain":"K","position":"1-473"},{"gene_uniquename":"SPAC29A4.08c","chain":"S/T/U/V","position":"1-488"},{"gene_uniquename":"SPAC2C4.03c","chain":"G","position":"1-115"},{"gene_uniquename":"SPAC4A8.09c","chain":"b","position":"1-293"},{"gene_uniquename":"SPAC4F8.12c","chain":"A","position":"1-2363"},{"gene_uniquename":"SPAC27D7.07c","chain":"F","position":"1-117"},{"gene_uniquename":"SPBC6B1.10","chain":"a","position":"1-558"},{"gene_uniquename":"SPBC3E7.13c","chain":"Y","position":"1-229"},{"gene_uniquename":"SPBC3E7.14","chain":"I","position":"1-78"},{"gene_uniquename":"SPCC550.02c","chain":"M","position":"1-354"},{"gene_uniquename":"SPBC24C6.11","chain":"O","position":"1-146"},{"gene_uniquename":"SPBC4B4.05","chain":"J","position":"1-77"},{"gene_uniquename":"SPBC215.12","chain":"B","position":"1-984"},{"gene_uniquename":"SPBC646.02","chain":"N","position":"1-1284"},{"gene_uniquename":"SPBC1289.11","chain":"C","position":"1-340"},{"gene_uniquename":"SPAC644.12","chain":"W","position":"1-757"},{"gene_uniquename":"SPBC337.06c","chain":"Q","position":"1-265"},{"gene_uniquename":"SPAC57A10.03","chain":"d","position":"1-155"},{"gene_uniquename":"SPAC3A12.11c","chain":"P","position":"1-388"},{"gene_uniquename":"SPBC31F10.11c","chain":"R","position":"1-674"},{"gene_uniquename":"SPCC188.11","chain":"L","position":"1-557"},{"gene_uniquename":"SPAC26A3.08","chain":"E","position":"1-147"},{"gene_uniquename":"SPAC20H4.09","chain":"z","position":"1-647"},{"gene_uniquename":"SPAC20H4.06c","chain":"y","position":"1-534"},{"gene_uniquename":"SPBC13E7.01","chain":"c","position":"1-887"},{"gene_uniquename":"SPBC211.02c","chain":"X","position":"1-790"},{"gene_uniquename":"SPBC28F2.04c","chain":"Z","position":"1-187"},{"gene_uniquename":"SPBC11G11.06c","chain":"H","position":"1-84"},{"gene_uniquename":"SPAC1486.03c","chain":"m","position":"1-797"},{"gene_uniquename":"SPBC19C2.14","chain":"D","position":"1-97"}],"title":"Structure of a B-state intermediate committed to discard (Bd-I state)","entry_authors":"Soni K,Wild K,Sinning I","entry_authors_abbrev":"Soni K et al.","reference_uniquename":"PMID:39833470","experimental_method":"EM","resolution":"3.2"}]},{"uniquename":"PMID:10940030","title":"Spy1, a histidine-containing phosphotransfer signaling protein, regulates the fission yeast cell cycle through the Mcs4 response regulator.","citation":"J Bacteriol 2000 Sep;182(17):4868-74","abstract":"Common histidine-to-aspartate (His-to-Asp) phosphorelay signaling systems involve three types of signaling components: a sensor His kinase, a response regulator, and a histidine-containing phosphotransfer (HPt) protein. In the fission yeast Schizosaccharomyces pombe, two response regulators, Mcs4 and Prr1, have been identified recently, and it was shown that they are involved in the signal transduction implicated in stress responses. Furthermore, Mcs4 appears to be involved in mitotic cell-cycle control. However, neither the HPt phosphotransmitter nor His kinase has been characterized in S. pombe. In this study, we identified a gene encoding an HPt phosphotransmitter, named Spy1 (S. pombe YPD1-like protein). The spy1(+) gene showed an ability to complement a mutational lesion of the Saccharomyces cerevisiae YPD1 gene, which is involved in an osmosensing signal transduction. The result from yeast two-hybrid analysis indicated that Spy1 interacts with Mcs4. To gain insight into the function of Spy1, a series of genetic analyses were conducted. The results provided evidence that Spy1, together with Mcs4, plays a role in regulation of the G(2)/M cell cycle progression. Spy1-deficient cells appear to be precocious in the entry to M phase. In the proposed model, Spy1 modulates Mcs4 in a negative manner, presumably through a direct His-to-Asp phosphorelay, operating upstream of the Sty1 mitogen-activated protein kinase cascade.","authors":"Aoyama K, Mitsubayashi Y, Aiba H, Mizuno T","authors_abbrev":"Aoyama K et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-08-12","publication_year":"2000","canto_session_key":"271bdc638a89c8fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-03 15:28:34","canto_approved_date":"2021-10-21 20:52:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-13 16:51:51","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC725.02","SPBC215.05","SPAC24B11.06c","SPBC887.10","SPCC757.07c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2017-08-03"},{"uniquename":"PMID:9382823","title":"Cell-cycle signaling: Atm displays its many talents.","citation":"Curr Biol 1997 Dec 01;7(12):R789-92","abstract":"The discovery of multiple signaling cascades downstream of Atm may lead to a clearer understanding of the diverse defects seen in ataxia-telangiectasia. These pathways - which include evolutionarily conserved Chk1 and Atr, and non-conserved p21, p53 and AbI - guard genomic integrity after DNA damage.","authors":"Westphal CH","authors_abbrev":"Westphal CH","pubmed_publication_date":"01 Dec 1997","pubmed_entrez_date":"1998-02-21","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-11-26 01:21:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15886085","title":"The Schizosaccharomyces pombe imprint--nick or ribonucleotide(s)?","citation":"Curr Biol 2005 May 10;15(9):R326-7; author reply R327","abstract":"","authors":"Vengrova S, Dalgaard JZ","authors_abbrev":"Vengrova S et al.","pubmed_publication_date":"10 May 2005","pubmed_entrez_date":"2005-05-12","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21119765","title":"Cytoskeletal dynamics in fission yeast: a review of models for polarization and division.","citation":"HFSP J 2010 Jun;4(3-4):122-30","abstract":"We review modeling studies concerning cytoskeletal activity of fission yeast. Recent models vary in length and time scales, describing a range of phenomena from cellular morphogenesis to polymer assembly. The components of cytoskeleton act in concert to mediate cell-scale events and interactions such as polarization. The mathematical models reduce these events and interactions to their essential ingredients, describing the cytoskeleton by its bulk properties. On a smaller scale, models describe cytoskeletal subcomponents and how bulk properties emerge.","doi":"10.2976/1.3385659","authors":"Drake T, Vavylonis D","authors_abbrev":"Drake T et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-12-02","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41068765","title":"Proteasome regulation of petite-negativity in fission yeast.","citation":"BMC Biol 2025 Oct 09;23(1):302","abstract":"Mitochondria carry out essential functions in eukaryotic cells. The mitochondrial genome encodes factors critical to support oxidative phosphorylation and mitochondrial protein import necessary for these functions. However, organisms like budding yeast can readily lose their mitochondrial genome, yielding respiration-deficient petite mutants. The fission yeast Schizosaccharomyces pombe is petite-negative, but some nuclear mutations enable the loss of its mitochondrial genome.\nptp1-1 is a partial loss of function mutation of the proteasome that enables growth of cells devoid of mitochondrial DNA through a mechanism that is independent of mitochondrial membrane potential rescue and associated with proteasome-dependent regulation of mitochondrial protein import precursors and the oxidative stress response.","doi":"10.1186/s12915-025-02409-2","authors":"Amberg KL, Hao L, Cranz-Mileva S, Zaratiegui M","authors_abbrev":"Amberg KL et al.","pubmed_publication_date":"09 Oct 2025","pubmed_entrez_date":"2025-10-10","publication_year":"2025","canto_session_key":"1451dc417735a0d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mikel Zaratiegui","canto_first_approved_date":"2025-11-07 09:10:32","canto_approved_date":"2025-12-23 13:13:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-10-10 16:14:27","canto_added_date":"2025-10-10 14:54:41","annotation_curators":[{"name":"Mikel Zaratiegui","community_curator":true,"annotation_count":20,"orcid":"0000-0002-0342-0268","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.13","SPAC222.12c","SPBP19A11.03c","SPAC14C4.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2025-11-07"},{"uniquename":"PMID:28929213","title":"To finish things well: cysteine methylation ensures selective GTPase membrane localization and signalling.","citation":"Curr Genet 2018 Apr;64(2):341-344","abstract":"Isoprenylcysteine-O-Carboxyl Methyltransferase (ICMT) catalyzes the final step in the prenylation process of different proteins including members of the Ras superfamily of GTPases. While cysteine methylation is essential in mammalian cells for growth, membrane association, and signalling by Ras and Rho GTPases, its role during signal transduction events in simple eukaryotes like yeasts appears irrelevant. By using a multidisciplinary approach our group has recently shown that, contrary to this initial assumption, in the fission yeast Schizosaccharomyces pombe ICMT activity encoded by the Mam4 gene is not only important to promote selective plasma membrane targeting of Ras and specific Rho GTPases, but also to allow precise downstream signalling to the mitogen-activated protein kinase and target of rapamycin pathways in response to diverse environmental cues. Thus, the dynamic regulation of in vivo methylation as a modulator of GTPase localization and function is an evolutionary conserved mechanism, making fission yeast an appealing model organism to study the regulation of this process.","doi":"10.1007/s00294-017-0756-x","authors":"Cansado J","authors_abbrev":"Cansado J","pubmed_publication_date":"Apr 2018","pubmed_entrez_date":"2017-09-21","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-09-22 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25764183","title":"Condensin HEAT subunits required for DNA repair, kinetochore/centromere function and ploidy maintenance in fission yeast.","citation":"PLoS One 2015;10(3):e0119347","abstract":"Condensin, a central player in eukaryotic chromosomal dynamics, contains five evolutionarily-conserved subunits. Two SMC (structural maintenance of chromosomes) subunits contain ATPase, hinge, and coiled-coil domains. One non-SMC subunit is similar to bacterial kleisin, and two other non-SMC subunits contain HEAT (similar to armadillo) repeats. Here we report isolation and characterization of 21 fission yeast (Schizosaccharomyces pombe) mutants for three non-SMC subunits, created using error-prone mutagenesis that resulted in single-amino acid substitutions. Beside condensation, segregation, and DNA repair defects, similar to those observed in previously isolated SMC and cnd2 mutants, novel phenotypes were observed for mutants of HEAT-repeats containing Cnd1 and Cnd3 subunits. cnd3-L269P is hypersensitive to the microtubule poison, thiabendazole, revealing defects in kinetochore/centromere and spindle assembly checkpoints. Three cnd1 and three cnd3 mutants increased cell size and doubled DNA content, thereby eliminating the haploid state. Five of these mutations reside in helix B of HEAT repeats. Two non-SMC condensin subunits, Cnd1 and Cnd3, are thus implicated in ploidy maintenance.","doi":"10.1371/journal.pone.0119347","authors":"Xu X, Nakazawa N, Yanagida M","authors_abbrev":"Xu X et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-13","publication_year":"2015","canto_session_key":"b1ccbcba410b2133","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xingya Xu","canto_first_approved_date":"2019-05-30 12:43:47","canto_approved_date":"2019-07-24 14:59:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-17 19:51:49","canto_added_date":"2015-03-14 01:15:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Xingya Xu","community_curator":true,"annotation_count":65,"orcid":"0000-0002-3728-2633","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.02c","SPAC1687.20c","SPBC776.13","SPCC895.07","SPCC736.14","SPCC306.03c","SPBP4H10.06c","SPCC188.03","SPBC146.03c","SPBC20F10.06"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2019-05-30"},{"uniquename":"PMID:29703785","title":"A Cloning-Free Method for CRISPR/Cas9-Mediated Genome Editing in Fission Yeast.","citation":"G3 (Bethesda) 2018 May 31;8(6):2067-2077","abstract":"The CRISPR/Cas9 system, which relies on RNA-guided DNA cleavage to induce site-specific DNA double-strand breaks, is a powerful tool for genome editing. This system has been successfully adapted for the fission yeast  Schizosaccharomyces pombe  by expressing Cas9 and the single-guide RNA (sgRNA) from a plasmid. In the procedures published to date, the cloning step that introduces a specific sgRNA target sequence into the plasmid is the most tedious and time-consuming. To increase the efficiency of applying the CRISPR/Cas9 system in fission yeast, we here developed a cloning-free procedure that uses gap repair in fission yeast cells to assemble two linear DNA fragments, a gapped Cas9-encoding plasmid and a PCR-amplified sgRNA insert, into a circular plasmid. Both fragments contain only a portion of the  ura4  or  bsdMX  marker so that only the correctly assembled plasmid can confer uracil prototrophy or blasticidin resistance. We show that this gap-repair-based and cloning-free CRISPR/Cas9 procedure permits rapid and efficient point mutation knock-in, endogenous N-terminal tagging, and genomic sequence deletion in fission yeast.","doi":"10.1534/g3.118.200164","authors":"Zhang XR, He JB, Wang YZ, Du LL","authors_abbrev":"Zhang XR et al.","pubmed_publication_date":"31 May 2018","pubmed_entrez_date":"2018-04-29","publication_year":"2018","canto_session_key":"a97d6e9961598b42","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-05-01 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010377","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19301326","title":"Shotgun proteomic analysis of the microsomal fraction of eukaryotic cells using a two-dimensional reversed-phase x ion-pair reversed-phase HPLC setup.","citation":"J Sep Sci 2009 Apr;32(8):1165-74","abstract":"A RPxIP-RP HPLC separation scheme was combined with on-line ESI-IT tandem MS or off-line MALDI tandem TOF MS and applied to the analysis of eukaryotic subcellular proteomes. Previous proteomic studies [1] were complemented by the approval of the approach to eukaryotic proteomes using the fission yeast Schizosaccharomyces pombe. The major focus was set to the analysis of primary human hepatocyte microsomes, representing a compartment of high interest due to its involvement in xenobiotic detoxification and cholesterol homeostasis. Of the 588 proteins identified from two donors, 24% are involved in cholesterol homeostasis or xenobiotic/lipid metabolism. Up to 50% of the identified proteins belong to the group of membrane proteins, difficult to investigate using gel-based proteomic approaches. We further demonstrated the reproducibility and comparability of the approach and reduced the amount of sample load by almost 70% with only minor loss of information about the proteins identified in the samples. The presented study clearly demonstrates the good applicability of the experimental setup to the analysis of subcellular proteomes including large membrane fractions, where only low amounts of sample material are available.","doi":"10.1002/jssc.200800619","authors":"Wörner M, Melchior K, Delmotte N, Hwang KH, Monostory K, Huber CG, Bernhardt R","authors_abbrev":"Wörner M et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-03-21","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12359063","title":"Yeast protein kinase C.","citation":"J Biochem 2002 Oct;132(4):513-7","abstract":"The mammalian protein kinase C (PKC) superfamily plays regulatory roles in many different cellular processes. However, due to the many members that exist in cells, it is very complicated to present experimental evidence of the particular function of each member. In contrast, yeasts have only one or two PKC members and genetic tools have unveiled their role as main regulators of cell integrity. In this review, we will discuss the function of yeast protein kinase C homologues, their mechanism of activation and the signalling pathways that they regulate in two model yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe.","authors":"Perez P, Calonge TM","authors_abbrev":"Perez P et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-10-03","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27050258","title":"Cloning, expression, purification and crystallization of Schizosaccharomyces pombe Set7, a putative histone methyltransferase.","citation":"Acta Crystallogr F Struct Biol Commun 2016 Apr;72(Pt 4):263-8","abstract":"Dysfunction of histone-modifying enzymes affects chromatin regulation and is involved in carcinogenesis, tumour progression and other diseases. Histone methyltransferases are a family of key histone-modifying enzymes, but their structures, functions and mechanisms are incompletely understood, thus constraining drug-design efforts. Here, preliminary steps towards structure-function studies of Schizosaccharomyces pombe Set7, a putative histone methyltransferase and the first yeast full-length SET-domain-containing protein to be studied using X-ray crystallography, are reported. The methods from cloning to X-ray diffraction and phasing are discussed and the results will aid in prospective studies of histone-modifying enzymes.","doi":"10.1107/S2053230X16003794","authors":"Mevius DE, Shen Y, Morishita M, di Luccio E","authors_abbrev":"Mevius DE et al.","pubmed_publication_date":"Apr 2016","pubmed_entrez_date":"2016-04-07","publication_year":"2016","canto_session_key":"c302597e5638100a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-06-08 10:11:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-06-08 10:11:51","canto_added_date":"2016-04-08 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC297.04c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2016-06-08"},{"uniquename":"PMID:30359777","title":"A case of severe trichothiodystrophy 3 in a neonate due to mutation in the GTF2H5 gene: Clinical report.","citation":"Eur J Med Genet 2019 Sep;62(9):103557","abstract":"Trichothiodystrophy (TTD) is a group of predominantly autosomal recessive disorders characterized by sulfur-deficient brittle hair. Clinical features of TTD consist of variable neuroectodermal symptoms including ichthyosis, nail abnormalities, mental retardation, short stature, decreased fertility and proneness to infections. Approximately half of the reported patients with TTD have clinical and cellular photosensitivity associated with mutations in three subunits (ERCC3, ERCC2, GTF2H5) of the basal transcription factor TFHII, which is involved in transcription and nucleotide excision repair. We report on a case of a male neonate with a novel GTF2H5 gene mutation, detected by whole exome sequencing. The GTF2H5 gene's role is to provide stability to the entire TFHII complex. The reported patient was born at 33 weeks' gestation from a pregnancy complicated by intrauterine growth restriction and premature rupture of membranes. His main clinical problems included severe congenital ichthyosis and proneness to infections with episodes of multiorgan failure. The infant's history displays the most severe clinical manifestations among patients with GTF2H5 gene mutations that have so far been reported.","doi":"10.1016/j.ejmg.2018.10.009","authors":"Michalska E, Koppolu A, Dobrzańska A, Płoski R, Gruszfeld D","authors_abbrev":"Michalska E et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2018-10-26","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.15"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8476210","title":"Creation of ultra-rare restriction sites in intact eucaryotic chromosomes mediated by bacterial methylases: an approach to sequencing and analyzing tumor and normal genomes.","citation":"Anticancer Res 1993;13(1):17-20","abstract":"The limited restriction of eucaryotic chromosomes would facilitate our understanding of the aberrant genomes of genetic diseases and cancer. We have described methods for methylating eucaryotic chromosomes embedded in agarose plugs. We now describe how Cla I methylase can be utilized in a methylation-dependent restriction cleavage with Dpn I to restrict eucaryotic genomes into a limited number of fragments. We have restricted the genomes of Saccharomyces cerevisiae at four sites and cleaved the three chromosomes of Schizosaccharomyces pombe into eleven fragments. Unlike the recently published methodologies using DNA sequences inserted into procaryotic and eucaryotic genomes, the methodologies described here use unaltered eucaryotic genomes for highly limited restriction. This methodology has applications in speeding, simplifying, and reducing the cost of sequencing the human genome.","authors":"Wilson WW, Mebane EW, Hoffman RM","authors_abbrev":"Wilson WW et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012585","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34339868","title":"The roles of assembly factors in mammalian mitoribosome biogenesis.","citation":"Mitochondrion 2021 Sep;60:70-84","abstract":"As ancient bacterial endosymbionts of eukaryotic cells, mitochondria have retained their own circular DNA as well as protein translation system including mitochondrial ribosomes (mitoribosomes). In recent years, methodological advancements in cryoelectron microscopy and mass spectrometry have revealed the extent of the evolutionary divergence of mitoribosomes from their bacterial ancestors and their adaptation to the synthesis of 13 mitochondrial DNA encoded oxidative phosphorylation complex subunits. In addition to the structural data, the first assembly pathway maps of mitoribosomes have started to emerge and concomitantly also the assembly factors involved in this process to achieve fully translational competent particles. These transiently associated factors assist in the intricate assembly process of mitoribosomes by enhancing protein incorporation, ribosomal RNA folding and modification, and by blocking premature or non-native protein binding, for example. This review focuses on summarizing the current understanding of the known mammalian mitoribosome assembly factors and discussing their possible roles in the assembly of small or large mitoribosomal subunits.","doi":"10.1016/j.mito.2021.07.008","authors":"Hilander T, Jackson CB, Robciuc M, Bashir T, Zhao H","authors_abbrev":"Hilander T et al.","pubmed_publication_date":"Sep 2021","pubmed_entrez_date":"2021-08-02","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1347.13c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9180692","title":"Molecular analysis of hus1+, a fission yeast gene required for S-M and DNA damage checkpoints.","citation":"Mol Gen Genet 1997 Apr 28;254(4):389-99","abstract":"The structure of hus1+, a Schizosaccharomyces pombe gene required for S-M and DNA damage checkpoints, has been determined. Expression of hus1+ requires splicing of five exons, including a microexon that is only 13 nucleotides long. hus1+ is predicted to encode a 33 kDa protein with no similarity to sequences in any database, including the entire S. cerevisiae genome. Yeast strains disrupted for the hus1+ gene are viable but checkpoint-defective. Polyclonal antibodies were raised against bacterially expressed Hus1 protein, and used to study Hus1 regulation. Hus1 protein levels are not affected by S-phase arrest, and are not altered by mutations in other checkpoint genes, suggesting that Hus1 is not regulated at the transcriptional or translational levels.","authors":"Kostrub CF, al-Khodairy F, Ghazizadeh H, Carr AM, Enoch T","authors_abbrev":"Kostrub CF et al.","pubmed_publication_date":"28 Apr 1997","pubmed_entrez_date":"1997-04-28","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G4.04c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"EMBL:D89161","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15659165","title":"A constitutively active GPCR retains its G protein specificity and the ability to form dimers.","citation":"Mol Microbiol 2005 Jan;55(2):482-97","abstract":"G protein-coupled receptors (GPCRs) are cell surface proteins which help to regulate the physiology of all the major organ systems within higher eukaryotes. They are stimulated by multiple ligands and activate a range of effector molecules to bring about changes in cell behaviour. The use of constitutively active mutants (CAMs) of GPCRs has enabled a better understanding of receptor activation as CAMs exhibit ligand-independent signalling negating the use of ligands. Here we introduce the fission yeast Schizosaccharomyces pombe as a host for producing CAMs, by describing the isolation and characterization of constitutive mutants of the P-factor receptor (Mam2). One mutant Mam2[P261L] contained a single-amino-acid substitution (Pro261 to Leu) within a region of high homology in GPCRs. Substitution of this proline leads to an 18-fold increase in ligand-independent signalling. We utilized Mam2[P261L] to investigate CAM activity by demonstrating that Mam2[P261L] is efficiently trafficked to the cell surface where it can form fully functional oligomeric complexes with the native receptor. Mam2[P261L] also retains the G protein specificity (RG-profile) of the native receptor and only induces constitutive signalling in the same G proteins. Finally, evidence is provided to indicate that CAM activity results from a reduction in the kinetics of G protein binding. This is the first time that S. pombe has been utilized for isolating and characterizing CAMs and the techniques employed will complement the current systems available for studying these important receptors.","authors":"Ladds G, Davis K, Das A, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2005-01-22","publication_year":"2005","canto_session_key":"1bdef2cd0551c52","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-12 16:46:42","canto_approved_date":"2020-12-13 11:39:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-05 12:29:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1296.03c","SPBC24C6.06","SPAC11H11.04"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2017-07-12"},{"uniquename":"EMBL:AU013287","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5797092","title":"[Biochemical proterties of Schizosaccharomyces plmbe depending on culture conditions and on the action of inhibitors. II. Composition of the cell walls].","citation":"Biochim Biophys Acta 1969 Jun 10;176(4):803-12","abstract":"","authors":"Deshusses J, Berthoud S, Posternak T","authors_abbrev":"Deshusses J et al.","pubmed_publication_date":"10 Jun 1969","pubmed_entrez_date":"1969-06-10","publication_year":"1969","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-01-02 05:53:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24026504","title":"Rapid, efficient and precise allele replacement in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 2014 May;60(2):109-19","abstract":"Gene targeting provides a powerful tool to modify endogenous loci to contain specific mutations, insertions and deletions. Precise allele replacement, with no other chromosomal changes (e.g., insertion of selectable markers or heterologous promoters), maintains physiologically relevant context. Established methods for precise allele replacement in fission yeast employ two successive rounds of transformation and homologous recombination and require genotyping at each step. The relative efficiency of homologous recombination is low and a high rate of false positives during the second round of gene targeting further complicates matters. We report that pop-in, pop-out allele replacement circumvents these problems. We present data for 39 different allele replacements, involving simple and complex modifications at seven different target loci, that illustrate the power and utility of the approach. We also developed and validated a rapid, efficient process for precise allele replacement that requires only one round each of transformation and genotyping. We show that this process can be applied in population scale to an individual target locus, without genotyping, to identify clones with an altered phenotype (targeted forward genetics). It is therefore suitable for saturating, in situ, locus-specific mutation screens (e.g., of essential or non-essential genes and regulatory DNA elements) within normal chromosomal context.","doi":"10.1007/s00294-013-0406-x","authors":"Gao J, Kan F, Wagnon JL, Storey AJ, Protacio RU, Davidson MK, Wahls WP","authors_abbrev":"Gao J et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2013-09-13","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD255","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20207534","title":"RNAi-dependent formation of heterochromatin and its diverse functions.","citation":"Curr Opin Genet Dev 2010 Apr;20(2):134-41","abstract":"Expression profiling of eukaryotic genomes has revealed widespread transcription outside the confines of protein-coding genes, leading to production of antisense and non-coding RNAs (ncRNAs). Studies in Schizosaccharomyces pombe and multicellular organisms suggest that transcription and ncRNAs provide a framework for the assembly of heterochromatin, which has been linked to various chromosomal processes. In addition to gene regulation, heterochromatin is crucial for centromere function, cell fate determination as well as transcriptional and posttranscriptional silencing of repetitive DNA elements. Recently, heterochromatin factors have been shown to suppress antisense RNAs at euchromatic loci. These findings define conserved pathways that probably have major impact on the epigenetic regulation of eukaryotic genomes.","doi":"10.1016/j.gde.2010.02.003","authors":"Grewal SI","authors_abbrev":"Grewal SI","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-03-09","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33539828","title":"Reciprocal relation between reporter gene transcription and translation efficiency in fission yeast.","citation":"Plasmid 2021 May;115:102557","abstract":"The fission yeast, Schizosaccharomyces pombe, is an excellent model for basic research but is not useful for commercial scale protein expression due to lack of strong expression vectors. Earlier, we showed that the lsd90 promoter elicited significantly greater GFP expression level than the adh1 and nmt1 promoters, albeit in different vector backbones. Here, we have systematically investigated the contribution of selectable markers, LEU2 and URA3m to GFP expression: while LEU2 elicited very low expression, the URA3m gene, with truncated promoter, elicited much greater GFP expression level with all promoters. Paradoxically, an inverse correlation was observed between the GFP transcription and translation efficiency. This system can be useful for understanding the factors governing recombinant gene expression and optimization of protein production.","doi":"10.1016/j.plasmid.2021.102557","authors":"Srivastava S, Kaur S, Verma HK, Rani S, Thakur M, Haldar S, Singh J","authors_abbrev":"Srivastava S et al.","pubmed_publication_date":"May 2021","pubmed_entrez_date":"2021-02-04","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-02-06 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006812","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27345571","title":"The fission yeast CENP-B protein Abp1 prevents pervasive transcription of repetitive DNA elements.","citation":"Biochim Biophys Acta 2016 Oct;1859(10):1314-21","abstract":"It is well established that eukaryotic genomes are pervasively transcribed producing cryptic unstable transcripts (CUTs). However, the mechanisms regulating pervasive transcription are not well understood. Here, we report that the fission yeast CENP-B homolog Abp1 plays an important role in preventing pervasive transcription. We show that loss of abp1 results in the accumulation of CUTs, which are targeted for degradation by the exosome pathway. These CUTs originate from different types of genomic features, but the highest increase corresponds to Tf2 retrotransposons and rDNA repeats, where they map along the entire elements. In the absence of abp1, increased RNAPII-Ser5P occupancy is observed throughout the Tf2 coding region and, unexpectedly, RNAPII-Ser5P is enriched at rDNA repeats. Loss of abp1 also results in Tf2 derepression and increased nucleolus size. Altogether these results suggest that Abp1 prevents pervasive RNAPII transcription of repetitive DNA elements (i.e., Tf2 and rDNA repeats) from internal cryptic sites.","doi":"10.1016/j.bbagrm.2016.06.009","authors":"Daulny A, Mejía-Ramírez E, Reina O, Rosado-Lugo J, Aguilar-Arnal L, Auer H, Zaratiegui M, Azorin F","authors_abbrev":"Daulny A et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-06-28","publication_year":"2016","canto_session_key":"eb21ceb3aad6f1a7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-06-29 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPJ760.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20083904","title":"Dynamic regulation of heterochromatin function via phosphorylation of HP1-family proteins.","citation":"Epigenetics 2010 Jan 01;5(1):30-3","abstract":"Heterochromatin is characterized by methylation of histone H3 at lysine 9, which is recognized by well-conserved HP1-family proteins. Heterochromatin participates in various chromosome functions, which include transcriptional gene silencing and sister-chromatid cohesion. These heterochromatic functions are carried out by various effector proteins that associate with HP1-family proteins; however, the regulation of this association with the effectors is not well understood. Recently, we showed that phosphorylation of the fission-yeast HP1 homolog Swi6 regulates the association of the transcriptional regulators differentially and changes the transcriptional activity of heterochromatin, without affecting sister-chromatid cohesion. This study, together with another study performed using other systems, indicates that phosphorylation of HP1/Swi6 provides a dynamic pathway for the differential regulation of heterochromatin in response to inter- and intracellular signals.","authors":"Shimada A, Murakami Y","authors_abbrev":"Shimada A et al.","pubmed_publication_date":"01 Jan 2010","pubmed_entrez_date":"2010-01-20","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30808655","title":"Transcriptional gene silencing requires dedicated interaction between HP1 protein Chp2 and chromatin remodeler Mit1.","citation":"Genes Dev 2019 May 01;33(9-10):565-577","abstract":"Heterochromatin protein 1 (HP1) proteins are key factors of eukaryotic heterochromatin that coordinate chromatin compaction and transcriptional gene silencing. Through their multivalency they act as adaptors between histone H3 Lys9 di/trimethyl marks in chromatin and effector complexes that bind to the HP1 chromoshadow domain. Most organisms encode for multiple HP1 isoforms and the molecular mechanisms that underpin their diverse functions in genome regulation remain poorly understood. In fission yeast, the two HP1 proteins Chp2 and Swi6 assume distinct roles and Chp2 is tightly associated with the nucleosome remodeling and deacetylation complex SHREC. Here we show that Chp2 directly engages the SHREC nucleosome remodeler subunit Mit1. The crystal structure of the interaction interface reveals an extraordinarily extensive and specific interaction between the chromoshadow domain of Chp2 and the N terminus of Mit1. The integrity of this interface is critical for high affinity binding and for heterochromatin formation. Comparison with Swi6 shows that the Chp2-Mit1 interface is highly selective and thereby provides the molecular basis for the functional specialization of an HP1 isoform.","doi":"10.1101/gad.320440.118","authors":"Leopold K, Stirpe A, Schalch T","authors_abbrev":"Leopold K et al.","pubmed_publication_date":"01 May 2019","pubmed_entrez_date":"2019-02-28","publication_year":"2019","canto_session_key":"c6eb113b9c286ef6","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-03-01 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16C6.10","SPBP35G2.10","SPAC664.01c"],"gene_count":3,"ltp_gene_count":3,"pdb_entries":[{"pdb_id":"6fto","gene_chains":[{"gene_uniquename":"SPBC16C6.10","chain":"A/B","position":"315-380"},{"gene_uniquename":"SPBP35G2.10","chain":"C","position":"1-81"}],"title":"Crystal structure of the Chp2 chromoshadow domain in complex with N-terminal domain of chromatin remodeler Mit1","entry_authors":"Leopold K,Schalch T","entry_authors_abbrev":"Leopold K et al.","reference_uniquename":"PMID:30808655","experimental_method":"X-ray","resolution":"1.6"}]},{"uniquename":"PMID:42048249","title":"Pathways of rDNA copy number homeostasis in Schizosaccharomyces pombe.","citation":"G3 (Bethesda) 2026 Apr 28;","abstract":"Fragile sites across the genome pose an increased risk of genetic instability. The rDNA repeats are particularly at risk due to highly repetitive sequences, replication transcription collisions, polar replication fork barriers, and late DNA replication. In this study, we examine mechanisms of rDNA homeostasis in fission yeast. We monitor the effects of an artificially contracted rDNA array, assess the responses to genome-wide alkylation damage, and identify genetic pathways that affect rDNA copy number. We find that a reduced rDNA array leads to a decreased growth rate, smaller cell size, and increased genotoxic sensitivity to alkylation damage from MMS. We also observe that in response to chronic MMS exposure, normal rDNA arrays contract in a time/concentration-dependent manner. We show that rDNA copy number is affected by the fork protection complex (FPC), fork licensing proteins, chromatin modifiers, and DDK kinase. These results confirm that the rDNA repeats are a genome fragile site that is particularly sensitive to perturbations in DNA replication.","doi":"10.1093/g3journal/jkag093","authors":"Jones CE, Yuan JP, Forsburg SL","authors_abbrev":"Jones CE et al.","pubmed_publication_date":"28 Apr 2026","pubmed_entrez_date":"2026-04-28","publication_year":"2026","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2026-04-28 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4937781","title":"New method for extraction of ribonucleic acid and polyribosomes from Schizosaccharomyces pombe.","citation":"J Bacteriol 1971 Sep;107(3):659-63","abstract":"A new method for extracting ribosomal ribonucleic acid (RNA) and polyribosomes from Schizosaccharomyces pombe, a fission yeast, has been developed. Cells grown in the presence of 2-deoxyglucose were found to be more sensitive to the action of Glusulase; a short period of treatment (10 to 20 min) at 0 C was sufficient to convert the cells to osmotically sensitive structures. From these, ribosomal RNA and polyribosomes were readily prepared.","authors":"Birnboim HC","authors_abbrev":"Birnboim HC","pubmed_publication_date":"Sep 1971","pubmed_entrez_date":"1971-09-01","publication_year":"1971","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011250","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17724078","title":"Break-induced loss of heterozygosity in fission yeast: dual roles for homologous recombination in promoting translocations and preventing de novo telomere addition.","citation":"Mol Cell Biol 2007 Nov;27(21):7745-57","abstract":"Loss of heterozygosity (LOH), a causal event in tumorigenesis, frequently encompasses multiple genetic loci and whole chromosome arms. However, the mechanisms leading to such extensive LOH are poorly understood. We investigated the mechanisms of DNA double-strand break (DSB)-induced extensive LOH by screening for auxotrophic marker loss approximately 25 kb distal to an HO endonuclease break site within a nonessential minichromosome in Schizosaccharomyces pombe. Extensive break-induced LOH was infrequent, resulting from large translocations through both allelic crossovers and break-induced replication. These events required the homologous recombination (HR) genes rad32(+), rad50(+), nbs1(+), rhp51(+), rad22(+), rhp55(+), rhp54(+), and mus81(+). Surprisingly, LOH was still observed in HR mutants, which resulted predominantly from de novo telomere addition at the break site. De novo telomere addition was most frequently observed in rad22Delta and rhp55Delta backgrounds, which disrupt HR following end resection. Further, levels of de novo telomere addition, while increased in ku70Delta rhp55Delta strains, were reduced in exo1Delta rhp55Delta and an rhp55Delta strain overexpressing rhp51. These findings support a model in which HR prevents de novo telomere addition at DSBs by competing for resected ends. Together, these results suggest that the mechanisms of break-induced LOH may be predicted from the functional status of the HR machinery.","authors":"Cullen JK, Hussey SP, Walker C, Prudden J, Wee BY, Davé A, Findlay JS, Savory AP, Humphrey TC","authors_abbrev":"Cullen JK et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-08-29","publication_year":"2007","canto_session_key":"a18a95950fc2c521","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-06-24 14:31:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-06-24 14:31:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":61,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPCC126.02c","SPCC4G3.05c","SPAC13C5.07","SPAC1556.01c","SPCC1183.05c","SPAC3C7.03c","SPBC6B1.09c","SPAC30D11.10","SPBC29A10.05","SPAC15A10.03c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2016-06-24"},{"uniquename":"PMID:7816619","title":"Cloning of cDNAs from Arabidopsis thaliana that encode putative protein phosphatase 2C and a human Dr1-like protein by transformation of a fission yeast mutant.","citation":"Nucleic Acids Res 1994 Dec 11;22(24):5296-301","abstract":"We characterized three Arabidopsis thaliana cDNA clones that could rescue the sterile phenotype of the Schizosaccharomyces pombe pde1 mutant, which is defective in cAMP phosphodiesterase. The first clone had a coding capacity of 399 amino acids that is 35% identical with rat protein phosphatase 2C (PP2C). The second had a coding capacity of 159 amino acids that is 41% identical with human Dr1. Dr1 has been shown to interact with TATA-binding protein (TBP) and block its ability to activate transcription. The third encoded Arabidopsis TBP itself. Saccharomyces cerevisiae TBP also could suppress the sterile phenotype if expressed in S.pombe pde1 cells, but overexpression of S.pombe TBP could do so very poorly. These observations suggest preliminarily that PP2C may counteract cAMP-dependent protein kinase in fission yeast cells, and that the heterologous TBPs and Dr1 may interfere with the general transcription factors of S.pombe so that the gene expression in the host cell becomes affirmative of sexual development. Furthermore, the identification of a Dr1-like protein in A.thaliana strongly argues for the ubiquity of this protein among eukaryotic genera and for a conserved mechanism to regulate transcription initiation that involves Dr1.","authors":"Kuromori T, Yamamoto M","authors_abbrev":"Kuromori T et al.","pubmed_publication_date":"11 Dec 1994","pubmed_entrez_date":"1994-12-11","publication_year":"1994","canto_session_key":"a0660529b64eed1b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 14:41:25","canto_session_submitted_date":"2012-03-03 14:41:10","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC285.09c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:25530312","title":"Modulating the level of the Rpb7 subunit of RNA polymerase II affects cell separation in Schizosaccharomyces pombe.","citation":"Res Microbiol 2015 Jan;166(1):20-7","abstract":"The rpb7(+) gene encodes the seventh largest subunit of RNA polymerase II and is essential for survival of yeast cells. To gain insight into its functions, we expressed rpb7(+) under the control of the nmt1 promoter and investigated its role in regulating multiple phenotypes in Schizosaccharomyces pombe. We observed that low rpb7(+) levels resulted in slow growth of cells under optimum growth conditions. However, no growth defect was observed under different stress conditions tested in this study. Our results also showed that the most prominent phenotype of cells expressing reduced rpb7(+) is a defect in cell separation. Quantitative real-time PCR analysis further revealed that the transcription of specific cell septation genes was significantly reduced in these cells. Collectively, results presented in this study highlight the distinct role of Rpb7p in regulating cell separation in S. pombe.","doi":"10.1016/j.resmic.2014.12.002","authors":"Kumar D, Sharma N","authors_abbrev":"Kumar D et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-12-23","publication_year":"2015","canto_session_key":"a5bf802fb871f24d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-08 15:31:00","canto_approved_date":"2026-02-14 10:02:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-29 11:17:29","canto_added_date":"2014-12-24 01:15:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPACUNK4.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-08"},{"uniquename":"PMID:18593478","title":"Evolution of SET-domain protein families in the unicellular and multicellular Ascomycota fungi.","citation":"BMC Evol Biol 2008 Jul 01;8:190","abstract":"The evolution of multicellularity is accompanied by the occurrence of differentiated tissues, of organismal developmental programs, and of mechanisms keeping the balance between proliferation and differentiation. Initially, the SET-domain proteins were associated exclusively with regulation of developmental genes in metazoa. However, finding of SET-domain genes in the unicellular yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe suggested that SET-domain proteins regulate a much broader variety of biological programs. Intuitively, it is expected that the numbers, types, and biochemical specificity of SET-domain proteins of multicellular versus unicellular forms would reflect the differences in their biology. However, comparisons across the unicellular and multicellular domains of life are complicated by the lack of knowledge of the ancestral SET-domain genes. Even within the crown group, different biological systems might use the epigenetic 'code' differently, adapting it to organism-specific needs. Simplifying the model, we undertook a systematic phylogenetic analysis of one monophyletic fungal group (Ascomycetes) containing unicellular yeasts, Saccharomycotina (hemiascomycetes), and a filamentous fungal group, Pezizomycotina (euascomycetes).\nSystematic analysis of the SET-domain genes across an entire eukaryotic phylum has outlined clear distinctions in the SET-domain gene collections in the unicellular and in the multicellular (filamentous) relatives; diversification of SET-domain gene families has increased further with the expansion and elaboration of multicellularity in animal and plant systems. We found several ascomycota-specific SET-domain gene groups; each was unique to either Saccharomycotina or Pezizomycotina fungi. Our analysis revealed that the numbers and types of SET-domain genes in the Saccharomycotina did not reflect the habitats, pathogenicity, mechanisms of sexuality, or the ability to undergo morphogenic transformations. However, novel genes have appeared for functions associated with the transition to multicellularity. Descendents of most of the SET-domain gene families found in the filamentous fungi could be traced in the genomes of extant animals and plants, albeit as more complex structural forms.\nSET-domain genes found in the filamentous species but absent from the unicellular sister group reflect two alternative evolutionary events: deletion from the yeast genomes or appearance of novel structures in filamentous fungal groups. There were no Ascomycota-specific SET-domain gene families (i.e., absent from animal and plant genomes); however, plants and animals share SET-domain gene subfamilies that do not exist in the fungi. Phylogenetic and gene-structure analyses defined several animal and plant SET-domain genes as sister groups while those of fungal origin were basal to them. Plants and animals also share SET-domain subfamilies that do not exist in fungi.","doi":"10.1186/1471-2148-8-190","authors":"Veerappan CS, Avramova Z, Moriyama EN","authors_abbrev":"Veerappan CS et al.","pubmed_publication_date":"01 Jul 2008","pubmed_entrez_date":"2008-07-03","publication_year":"2008","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24425750","title":"Expanding proteome coverage with orthogonal-specificity α-lytic proteases.","citation":"Mol Cell Proteomics 2014 Mar;13(3):823-35","abstract":"Bottom-up proteomics studies traditionally involve proteome digestion with a single protease, trypsin. However, trypsin alone does not generate peptides that encompass the entire proteome. Alternative proteases have been explored, but most have specificity for charged amino acid side chains. Therefore, additional proteases that improve proteome coverage through cleavage at sequences complementary to trypsin's may increase proteome coverage. We demonstrate the novel application of two proteases for bottom-up proteomics: wild type α-lytic protease (WaLP) and an active site mutant of WaLP, M190A α-lytic protease (MaLP). We assess several relevant factors, including MS/MS fragmentation, peptide length, peptide yield, and protease specificity. When data from separate digestions with trypsin, LysC, WaLP, and MaLP were combined, proteome coverage was increased by 101% relative to that achieved with trypsin digestion alone. To demonstrate how the gained sequence coverage can yield additional post-translational modification information, we show the identification of a number of novel phosphorylation sites in the Schizosaccharomyces pombe proteome and include an illustrative example from the protein MPD2 wherein two novel sites are identified, one in a tryptic peptide too short to identify and the other in a sequence devoid of tryptic sites. The specificity of WaLP and MaLP for aliphatic amino acid side chains was particularly valuable for coverage of membrane protein sequences, which increased 350% when the data from trypsin, LysC, WaLP, and MaLP were combined.","doi":"10.1074/mcp.M113.034710","authors":"Meyer JG, Kim S, Maltby DA, Ghassemian M, Bandeira N, Komives EA","authors_abbrev":"Meyer JG et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-01-16","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8125945","title":"Expression, purification, crystallization, and preliminary x-ray analysis of casein kinase-1 from Schizosaccharomyces pombe.","citation":"J Biol Chem 1994 Mar 11;269(10):7304-9","abstract":"The catalytic domain of Schizosaccharomyces pombe casein kinase-1 (the product of the cki1 gene) has been overexpressed in Escherichia coli, purified by chromatographic methods, characterized in vitro, and crystallized in the presence and absence of nucleotide substrate. The best crystals belong to the trigonal space group P3(1)21 or its enantiomorph, have unit cell parameters a = b = 79 A, c = 121 A, and diffract x-rays to 2.0-A resolution. Kinetic characterization of the purified catalytic domain and other C-terminal deletion mutants of Cki1 suggests that it is subject to two forms of regulation. One mechanism involves autophosphorylation, and results in a 4-fold decrease in the affinity for protein substrate. In contrast, truncation of intact Cki1 results in a 3-fold activation in its catalytic rate. This activation may arise from the removal of an inhibitory domain present in the intact enzyme.","authors":"Carmel G, Leichus B, Cheng X, Patterson SD, Mirza U, Chait BT, Kuret J","authors_abbrev":"Carmel G et al.","pubmed_publication_date":"11 Mar 1994","pubmed_entrez_date":"1994-03-11","publication_year":"1994","canto_session_key":"bf91b3d35250e1bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-02 21:15:04","canto_approved_date":"2022-02-07 19:37:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-22 12:52:02","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-02"},{"uniquename":"PMID:29970827","title":"Recent Insights on Alzheimer's Disease Originating from Yeast Models.","citation":"Int J Mol Sci 2018 Jul 03;19(7)","abstract":"In this review article, yeast model-based research advances regarding the role of Amyloid-&beta; (A&beta;), Tau and frameshift Ubiquitin UBB +1  in Alzheimer’s disease (AD) are discussed. Despite having limitations with regard to intercellular and cognitive AD aspects, these models have clearly shown their added value as complementary models for the study of the molecular aspects of these proteins, including their interplay with AD-related cellular processes such as mitochondrial dysfunction and altered proteostasis. Moreover, these yeast models have also shown their importance in translational research, e.g., in compound screenings and for AD diagnostics development. In addition to well-established  Saccharomyces cerevisiae  models, new upcoming  Schizosaccharomyces pombe ,  Candida glabrata  and  Kluyveromyces lactis  yeast models for Aβ and Tau are briefly described. Finally, traditional and more innovative research methodologies, e.g., for studying protein oligomerization/aggregation, are highlighted.","doi":"10.3390/ijms19071947","authors":"Seynnaeve D, Vecchio MD, Fruhmann G, Verelst J, Cools M, Beckers J, Mulvihill DP, Winderickx J, Franssens V","authors_abbrev":"Seynnaeve D et al.","pubmed_publication_date":"03 Jul 2018","pubmed_entrez_date":"2018-07-05","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-07-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16615884","title":"The meiotic chromosomal bouquet: SUN collects flowers.","citation":"Cell 2006 Apr 07;125(1):19-21","abstract":"In the early stages of meiosis, all the telomeres in the cell attach to the nuclear envelope and gather near the centrosome. This polarized chromosomal array is known as the bouquet, as the clustered telomeres resemble the gathered stems of a floral arrangement. In this issue of Cell, Chikashige et al. (2006) provide intriguing clues about the molecular details underlying this conserved meiotic event.","authors":"Tomita K, Cooper JP","authors_abbrev":"Tomita K et al.","pubmed_publication_date":"07 Apr 2006","pubmed_entrez_date":"2006-04-18","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11854409","title":"The multiprotein exocyst complex is essential for cell separation in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2002 Feb;13(2):515-29","abstract":"Schizosaccharomyces pombe cells divide by medial fission through the use of an actomyosin-based contractile ring. A mulitlayered division septum is assembled in concert with ring constriction. Finally, cleavage of the inner layer of the division septum results in the liberation of daughter cells. Although numerous studies have focused on actomyosin ring and division septum assembly, little information is available on the mechanism of cell separation. Here we describe a mutant, sec8-1, that is defective in cell separation but not in other aspects of cytokinesis. sec8-1 mutants accumulate about 100-nm vesicles and have reduced secretion of acid phosphatase, suggesting that they are defective in exocytosis. Sec8p is a component of the exocyst complex. Using biochemical methods, we show that Sec8p physically interacts with other members of the exocyst complex, including Sec6p, Sec10p, and Exo70p. These exocyst proteins localize to regions of active exocytosis-at the growing ends of interphase cells and in the medial region of cells undergoing cytokinesis-in an F-actin-dependent and exocytosis-independent manner. Analysis of a number of mutations in various exocyst components has established that these components are essential for cell viability. Interestingly, all exocyst mutants analyzed appear to be able to elongate and to assemble division septa but are defective for cell separation. We therefore propose that the fission yeast exocyst is involved in targeting of enzymes responsible for septum cleavage. We further propose that cell elongation and division septum assembly can continue with minimal levels of exocyst function.","authors":"Wang H, Tang X, Liu J, Trautmann S, Balasundaram D, McCollum D, Balasubramanian MK","authors_abbrev":"Wang H et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-02-21","publication_year":"2002","canto_session_key":"515169773959f90f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-17 20:01:43","canto_approved_date":"2022-11-10 19:45:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-18 20:48:29","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.20","SPBC336.12c","SPCC970.09","SPAC27F1.02c","SPAC1F5.04c","SPCC1235.10c","SPAC13F5.06c","SPAC20G8.05c"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2018-06-17"},{"uniquename":"PMID:4471996","title":"Anaerobic growth and formation of respiration-deficient mutants of various species of yeasts.","citation":"FEBS Lett 1974 Sep 01;45(1):263-6","abstract":"","authors":"Subík J, Kolarov J, Kovác L","authors_abbrev":"Subík J et al.","pubmed_publication_date":"01 Sep 1974","pubmed_entrez_date":"1974-09-01","publication_year":"1974","canto_session_key":"663fdce0ca219537","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-17 13:07:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-17 13:07:44","canto_added_date":"2013-01-17 13:04:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-01-17"},{"uniquename":"PMID:26670050","title":"Regulation of mRNA Levels by Decay-Promoting Introns that Recruit the Exosome Specificity Factor Mmi1.","citation":"Cell Rep 2015 Dec 22;13(11):2504-2515","abstract":"In eukaryotic cells, inefficient splicing is surprisingly common and leads to the degradation of transcripts with retained introns. How pre-mRNAs are committed to nuclear decay is unknown. Here, we uncover a mechanism by which specific intron-containing transcripts are targeted for nuclear degradation in fission yeast. Sequence elements within these \"decay-promoting\" introns co-transcriptionally recruit the exosome specificity factor Mmi1, which induces degradation of the unspliced precursor and leads to a reduction in the levels of the spliced mRNA. This mechanism negatively regulates levels of the RNA helicase DDX5/Dbp2 to promote cell survival in response to stress. In contrast, fast removal of decay-promoting introns by co-transcriptional splicing precludes Mmi1 recruitment and relieves negative expression regulation. We propose that decay-promoting introns facilitate the regulation of gene expression. Based on the identification of multiple additional Mmi1 targets, including mRNAs, long non-coding RNAs, and sn/snoRNAs, we suggest a general role in RNA regulation for Mmi1 through transcript degradation.","doi":"10.1016/j.celrep.2015.11.026","authors":"Kilchert C, Wittmann S, Passoni M, Shah S, Granneman S, Vasiljeva L","authors_abbrev":"Kilchert C et al.","pubmed_publication_date":"22 Dec 2015","pubmed_entrez_date":"2015-12-17","publication_year":"2015","canto_session_key":"c757e60bdb79c5cb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Cornelia Kilchert","canto_first_approved_date":"2017-11-20 16:08:48","canto_approved_date":"2024-03-21 16:51:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-08-27 07:39:30","canto_added_date":"2015-12-18 01:20:22","annotation_curators":[{"name":"Cornelia Kilchert","community_curator":true,"annotation_count":176,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC56E4.07","SPAC6B12.16","SPAC27D7.13c","SPCC613.12c","SPNCRNA.577","SPCC1322.03","SPAC22A12.04c","SPAC25G10.04c","SPAC24C9.13c","SPNCRNA.1696","SPAC13G7.02c","SPBP8B7.16c","SPCC757.02c","SPBC36.11","SPCC1393.07c","SPBC29A10.14","SPAC1039.03","SPAPB1E7.06c","SPBP8B7.15c","SPAC4G9.07","SPBC337.12","SPAC8E11.02c","SPBC1652.01","SPAC23C4.11","SPACUNK4.08","SPCC11E10.01","SPBP4G3.02","SPCC1223.12c","SPAC27D7.05c","SPBC887.14c","SPCC320.07c","SPAC32A11.01","SPAC4G8.08","SPCC1442.04c","SPBC119.14","SPBC19C7.07c","SPAC1556.06","SPAC22H10.13","SPCC4E9.01c","SPBC26H8.10","SPBC16E9.11c","SPBC1734.10c","SPAC869.08","SPNCRNA.1529","SPBC839.09c","SPBC1347.12","SPBC2D10.13","SPAC1F3.04c","SPAC1B2.05","SPBC2G2.09c","SPBC27B12.07","SPBC19G7.17","SPCC1795.07","SPCC569.07","SPNCRNA.1303","SPBC3E7.02c","SPBC2D10.06","SPBC23G7.14","SPBC216.02","SPBC32H8.11","SPCC1020.01c","SPNCRNA.850","SPBP4G3.03","SPBC14F5.11c","SPAC6G9.13c","SPAC19B12.11c","SPBP8B7.04","SPAC25B8.14","SPAC664.06","SPNCRNA.1608","SPAC29A4.12c","SPNCRNA.1271","SPAP7G5.03","SPAC1705.02","SPCC830.09c","SPBC725.02","SPBC582.03","SPAC13A11.03","SPAC1834.06c","SPNCRNA.585","SPCC1840.12","SPBC577.05c","SPAC1687.17c","SPBC1683.04","SPAC1783.06c","SPNCRNA.1712","SPAC13F5.01c","SPBC839.06","SPCC70.06","SPAC6C3.05","SPBC29A10.02","SPCC16A11.06c","SPBC25B2.11","SPBC646.17c","SPCC1183.05c","SPAC5D6.01","SPBC1718.02","SPNCRNA.1405","SPBC609.04","SPAC11E3.10","SPAC3H1.04c","SPAC6B12.15","SPAC31G5.10","SPAC688.09","SPAC10F6.03c","SPAC4F10.08","SPNCRNA.1224","SPAC18B11.07c","SPCC338.18","SPBC1604.10","SPBC359.01","SPBC1861.03","SPBC577.02","SPBC1289.13c","SPBC660.16","SPAC22F3.12c","SPAC19A8.01c","SPNCRNA.1330","SPNCRNA.584","SPAC57A10.04","SPNCRNA.1613","SPCC70.09c","SPAC57A10.08c","SPAC1F8.06","SPAC17A5.18c","SPBC16A3.08c","SPCC1235.04c","SPBC27B12.04c","SPAC3G9.13c","SPAC227.17c","SPNCRNA.1273","SPBC3E7.14","SPAC4G8.09","SPNCRNA.103","SPAC6F6.16c","SPBC4B4.11","SPAC1071.13","SPCC736.12c","SPBC21H7.02","SPAC27E2.10c","SPBC582.06c","SPCC970.02","SPAC12G12.13c","SPNCRNA.1005","SPCC737.04","SPAC3C7.06c","SPCC188.04c","SPAC13G6.08","SPAC23C4.07","SPBPB21E7.04c","SPAC4H3.08","SPAC1F7.06","SPBC405.02c","SPAC343.06c","SPAC13G7.11","SPCC4G3.10c","SPBC9B6.03","SPBC21D10.12","SPNCRNA.1366","SPCC1906.01","SPAC3A11.06","SPCC18.14c","SPCC970.07c","SPAC1250.05","SPAC1F3.01","SPAC9E9.14","SPNCRNA.1289"],"gene_count":167,"ltp_gene_count":10,"approved_date":"2017-11-20"},{"uniquename":"PMID:30446867","title":"Clinical and molecular characterization of non-syndromic retinal dystrophy due to c.175G>A mutation in ceroid lipofuscinosis neuronal 3 (CLN3).","citation":"Doc Ophthalmol 2019 Feb;138(1):55-70","abstract":"Mutation of the CLN3 gene, associated with juvenile neuronal ceroid lipofuscinosis, has recently been associated with late-onset, non-syndromic retinal dystrophy. Herein we describe the multimodal imaging, immunological and systemic features of an adult with compound heterozygous CLN3 mutations.\nA 50-year-old female with non-syndromic retinal dystrophy from the age of 36 years underwent multimodal retinal imaging, electroretinography, neuroimaging, immunological studies and genetic testing. CLN3 transcripts were amplified from patient leukocytes by reverse transcriptase polymerase chain reaction and characterized by Sanger sequencing.\nVisual acuity declined to 6/12 and 6/76 due to asymmetrical central scotoma. ERG responses became electronegative and patient's serum contained anti-retinal antibodies. Final visual acuity stabilized at 6/60 bilaterally 3 years after peri-ocular steroid and rituximab infusion. Genetic testing revealed compound heterozygous CLN3 mutations: the 1.02 kb deletion and a novel missense mutation (c.175G>A). In silico, analyses predicted the c.175G>A mutation disrupted an exonic splice enhancer site in exon 3. In patient leukocytes, CLN3 expression was reduced and novel CLN3 transcripts lacking exon 3 were detected.\nOur case study shows that (1) non-syndromic CLN3 disease leads to rod and delayed primary cone degeneration resulting in constricting peripheral field and enlarging central scotoma and, (2) the c.175G>A CLN3 mutation, altered splicing of the CLN3 gene. Overall, we provide comprehensive clinical characterization of a patient with non-syndromic CLN3 disease.","doi":"10.1007/s10633-018-9665-7","authors":"Chen FK, Zhang X, Eintracht J, Zhang D, Arunachalam S, Thompson JA, Chelva E, Mallon D, Chen SC, McLaren T, Lamey T, De Roach J, McLenachan S","authors_abbrev":"Chen FK et al.","pubmed_publication_date":"Feb 2019","pubmed_entrez_date":"2018-11-18","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC607.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17211681","title":"Iron homeostasis in the fission yeast Schizosaccharomyces pombe.","citation":"Biometals 2007 Jun;20(3-4):523-37","abstract":"Schizosaccharomyces pombe has acquisition processes for iron, an essential nutrient. One pathway consists to produce, excrete, and capture siderophore-iron complexes. A second pathway requires enzymatic reduction of ferric iron at the cell surface prior to uptake by a permease-oxidase complex. Genes encoding proteins involved in iron assimilation are transcriptionally regulated as a function of iron availability. Under high iron conditions, the GATA-type regulator Fep1 represses the expression of iron uptake genes. The repressor function of Fep1 requires the presence of the Tup11 or Tup12 transcriptional co-repressor. Under low iron conditions, two regulatory mechanisms occur. First, the iron transport genes are highly induced. Second, there is a transcription factor cascade implicating the heteromeric CCAAT-binding complex that turns off a set of genes encoding iron-utilizing proteins, presumably to avoid a futile expenditure of energy in producing iron-using proteins that lack the necessary cofactor to function. Thus, collectively, these regulatory responses to variations in iron concentrations ensure that iron is present within cells for essential biochemical reactions, yet prevent the accumulation of iron or iron-using proteins to deleterious levels.","authors":"Labbé S, Pelletier B, Mercier A","authors_abbrev":"Labbé S et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-01-11","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36190253","title":"Genetic Screen for Identification of Multicopy Suppressors in Schizosaccharomyces pombe.","citation":"J Vis Exp 2022 Sep 13;(187)","abstract":"Identification of genetic interactions is a powerful tool to decipher the functions of gene(s) by providing insights into their functional relationships with other genes and organization into biological pathways and processes. Although the majority of the genetic screens were initially developed in Saccharomyces cerevisiae, a complementary platform for carrying out these genetic screens has been provided by Schizosaccharomyces pombe. One of the common approaches used to identify genetic interactions is by overexpression of clones from a genome-wide, high-copy-number plasmid library in a loss-of-function mutant, followed by selection of clones that suppress the mutant phenotype. This paper describes a protocol for carrying out this 'multicopy suppression'-based genetic screen in S. pombe. This screen has helped identify multicopy suppressor(s) of the genotoxic stress-sensitive phenotype associated with the absence of the Ell1 transcription elongation factor in S. pombe. The screen was initiated by transformation of the query ell1 null mutant strain with a high-copy-number S. pombe cDNA plasmid library and selecting the suppressors on EMM2 plates containing 4-nitroquinoline 1-oxide (4-NQO), a genotoxic stress-inducing compound. Subsequently, plasmid was isolated from two shortlisted suppressor colonies and digested by restriction enzymes to release the insert DNA. Plasmids releasing an insert DNA fragment were retransformed into the ell1 deletion strain to confirm the ability of these suppressor plasmid clones to restore growth of the ell1 deletion mutant in the presence of 4-NQO and other genotoxic compounds. Those plasmids showing a rescue of the deletion phenotype were sequenced to identify the gene(s) responsible for suppression of the ell1 deletion-associated genotoxic stress-sensitive phenotype.","doi":"10.3791/63967","authors":"Bhardwaj V, Sweta K, Gyala D, Sharma N","authors_abbrev":"Bhardwaj V et al.","pubmed_publication_date":"13 Sep 2022","pubmed_entrez_date":"2022-10-03","publication_year":"2022","canto_session_key":"95342e64bf5b7acd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-10-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37714149","title":"Direct recruitment of Mis18 to interphase spindle pole bodies promotes CENP-A chromatin assembly.","citation":"Curr Biol 2023 Oct 09;33(19):4187-4201.e6","abstract":"CENP-A chromatin specifies mammalian centromere identity, and its chaperone HJURP replenishes CENP-A when recruited by the Mis18 complex (Mis18C) via M18BP1/KNL2 to CENP-C at kinetochores during interphase. However, the Mis18C recruitment mechanism remains unresolved in species lacking M18BP1, such as fission yeast. Fission yeast centromeres cluster at G2 spindle pole bodies (SPBs) when CENP-A Cnp1  is replenished and where Mis18C also localizes. We show that SPBs play an unexpected role in concentrating Mis18C near centromeres through the recruitment of Mis18 by direct binding to the major SPB linker of nucleoskeleton and cytoskeleton (LINC) component Sad1. Mis18C recruitment by Sad1 is important for CENP-A Cnp1  chromatin establishment and acts in parallel with a CENP-C-mediated Mis18C recruitment pathway to maintain centromeric CENP-A Cnp1  but operates independently of Sad1-mediated centromere clustering. SPBs therefore provide a non-chromosomal scaffold for both Mis18C recruitment and centromere clustering during G2. This centromere-independent Mis18-SPB recruitment provides a mechanism that governs de novo CENP-A Cnp1  chromatin assembly by the proximity of appropriate sequences to SPBs and highlights how nuclear spatial organization influences centromere identity.","doi":"10.1016/j.cub.2023.08.063","authors":"London N, Medina-Pritchard B, Spanos C, Rappsilber J, Jeyaprakash AA, Allshire RC","authors_abbrev":"London N et al.","pubmed_publication_date":"09 Oct 2023","pubmed_entrez_date":"2023-09-15","publication_year":"2023","canto_session_key":"c2ebaefaac28acb1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-09-17 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12D12.01","SPCC970.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:32585128","title":"Nascent Transcript Folding Plays a Major Role in Determining RNA Polymerase Elongation Rates.","citation":"Mol Cell 2020 Aug 06;79(3):488-503.e11","abstract":"Transcription elongation rates influence RNA processing, but sequence-specific regulation is poorly understood. We addressed this in vivo, analyzing RNAPI in S. cerevisiae. Mapping RNAPI by Miller chromatin spreads or UV crosslinking revealed 5' enrichment and strikingly uneven local polymerase occupancy along the rDNA, indicating substantial variation in transcription speed. Two features of the nascent transcript correlated with RNAPI distribution: folding energy and GC content in the transcription bubble. In vitro experiments confirmed that strong RNA structures close to the polymerase promote forward translocation and limit backtracking, whereas high GC in the transcription bubble slows elongation. A mathematical model for RNAPI elongation confirmed the importance of nascent RNA folding in transcription. RNAPI from S. pombe was similarly sensitive to transcript folding, as were S. cerevisiae RNAPII and RNAPIII. For RNAPII, unstructured RNA, which favors slowed elongation, was associated with faster cotranscriptional splicing and proximal splice site use, indicating regulatory significance for transcript folding.","doi":"10.1016/j.molcel.2020.06.002","authors":"Turowski TW, Petfalski E, Goddard BD, French SL, Helwak A, Tollervey D","authors_abbrev":"Turowski TW et al.","pubmed_publication_date":"06 Aug 2020","pubmed_entrez_date":"2020-06-26","publication_year":"2020","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2020-06-27 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28893786","title":"Novel Cell-Killing Mechanisms of Hydroxyurea and the Implication toward Combination Therapy for the Treatment of Fungal Infections.","citation":"Antimicrob Agents Chemother 2017 Nov;61(11)","abstract":"We have previously reported that an  erg11  mutation affecting ergosterol synthesis and a  hem13  mutation in the heme synthesis pathway significantly sensitize the fission yeast  Schizosaccharomyces pombe  to hydroxyurea (HU) (1, 2). Here we show that treatment with inhibitors of Erg11 and heme biosynthesis phenocopies the two mutations in sensitizing wild-type cells to HU. Importantly, HU synergistically interacts with the heme biosynthesis inhibitor sampangine and several Erg11 inhibitors, the antifungal azoles, in causing cell lethality. Since the synergistic drug interactions are also observed in the phylogenetically divergent  Saccharomyces cerevisiae  and the opportunistic fungal pathogen  Candida albicans , the synergism is likely conserved in eukaryotes. Interestingly, our genetic data for  S. pombe  has also led to the discovery of a robust synergism between sampangine and the azoles in  C. albicans  Thus, combinations of HU, sampangine, and the azoles can be further studied as a new method for the treatment of fungal infections.","doi":"10.1128/AAC.00734-17","authors":"Singh A, Agarwal A, Xu YJ","authors_abbrev":"Singh A et al.","pubmed_publication_date":"Nov 2017","pubmed_entrez_date":"2017-09-13","publication_year":"2017","canto_session_key":"2387f6fc60a25ed8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yongjie Xu","canto_first_approved_date":"2017-09-29 12:43:24","canto_approved_date":"2017-09-29 13:21:46","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-09-22 01:11:42","canto_added_date":"2017-09-14 00:15:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Yongjie Xu","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13A11.02c","SPAC222.11","SPBC216.05"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-09-29"},{"uniquename":"PMID:8939847","title":"Cell cycle control of DNA replication.","citation":"Science 1996 Dec 06;274(5293):1659-64","abstract":"The initiation of DNA replication in eukaryotic cells is a highly regulated process that leads to the duplication of the genetic information for the next cell generation. This requires the ordered assembly of many proteins at the origins of DNA replication to form a competent, pre-replicative chromosomal state. In addition to this competent complex, at least two cell cycle regulated protein kinase pathways are required to affect a transition to a post-replicative chromosomal state. Protein kinases required to establish mitosis prevent re-replication of the DNA. As cells exit mitosis, the cell cycle is reset, allowing the establishment of a new, competent replication state.","authors":"Stillman B","authors_abbrev":"Stillman B","pubmed_publication_date":"06 Dec 1996","pubmed_entrez_date":"1996-12-06","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8887550","title":"Rho 1 GTPase activates the (1-3)beta-D-glucan synthase and is involved in Schizosaccharomyces pombe morphogenesis.","citation":"EMBO J 1996 Sep 02;15(17):4584-91","abstract":"The Schizosaccharomyces pombe Cdc42 and Rho1 GTPases were tested for their ability to complement the cwg2-1 mutant phenotype of a decrease in (1-3)beta-D-glucan synthase activity when grown at the non-permissive temperature. Only Rho1 is able to partly complement the defect in glucan synthase associated with the cwg2-1 mutation. Moreover, overexpression of the rho1 gene in wild-type S.pombe cells causes aberrant morphology with loss of polarity and cells with several septa. Under this condition (1-3)beta-D-glucan synthase activity is increased four times, but is still dependent on GTP. When S.pombe is transformed with constitutively active rho1 mutant alleles (rho1-G15V or rho1-Q64L), cells stop growing and show a very thick cell wall with hardly any septum. Under this condition the level of (1-3)beta-D-glucan synthase activity is at least 20 times higher than wild-type and is independent of GTP. Neither cdc42+ nor the cdc42-V12G or cdc42-Q61L constitutively active mutant alleles affect (1-3)beta-D-glucan synthase activity when overexpressed in S.pombe. Cells overproducing Rho1 are hypersensitive to inhibitors of cell wall biosynthesis or to cell wall degrading enzymes. We conclude that Rho1 GTPase directly activates (1-3)beta-D-glucan synthase and regulates S.pombe morphogenesis.","authors":"Arellano M, Durán A, Pérez P","authors_abbrev":"Arellano M et al.","pubmed_publication_date":"02 Sep 1996","pubmed_entrez_date":"1996-09-02","publication_year":"1996","canto_session_key":"0e9fdcae51e973b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 19:16:51","canto_approved_date":"2021-10-05 17:07:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-05 12:02:26","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.03","SPAC1F7.04","SPBC19G7.05c","SPAC2E1P5.04c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2019-01-30"},{"uniquename":"PMID:15615848","title":"RNA-dependent RNA polymerase is an essential component of a self-enforcing loop coupling heterochromatin assembly to siRNA production.","citation":"Proc Natl Acad Sci U S A 2005 Jan 04;102(1):152-7","abstract":"In fission yeast, factors involved in the RNA interference (RNAi) pathway including Argonaute, Dicer, and RNA-dependent RNA polymerase are required for heterochromatin assembly at centromeric repeats and the silent mating-type region. Previously, we have shown that RNA-induced initiation of transcriptional gene silencing (RITS) complex containing the Argonaute protein and small interfering RNAs (siRNAs) localizes to heterochromatic loci and collaborates with heterochromatin assembly factors via a self-enforcing RNAi loop mechanism to couple siRNA generation with heterochromatin formation. Here, we investigate the role of RNA-dependent RNA polymerase (Rdp1) and its polymerase activity in the assembly of heterochromatin. We find that Rdp1, similar to RITS, localizes to all known heterochromatic loci, and its localization at centromeric repeats depends on components of RITS and Dicer as well as heterochromatin assembly factors including Clr4/Suv39h and Swi6/HP1 proteins. We show that a point mutation within the catalytic domain of Rdp1 abolished its RNA-dependent RNA polymerase activity and resulted in the loss of transcriptional silencing and heterochromatin at centromeres, together with defects in mitotic chromosome segregation and telomere clustering. Moreover, the RITS complex in the rdp1 mutant does not contain siRNAs, and is delocalized from centromeres. These results not only implicate Rdp1 as an essential component of a self-enforcing RNAi loop but also ascribe a critical role for its RNA-dependent RNA polymerase activity in siRNA production necessary for heterochromatin formation.","authors":"Sugiyama T, Cam H, Verdel A, Moazed D, Grewal SI","authors_abbrev":"Sugiyama T et al.","pubmed_publication_date":"04 Jan 2005","pubmed_entrez_date":"2004-12-24","publication_year":"2005","canto_session_key":"c8412d1610d7fb9b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-08-25 10:04:33","canto_approved_date":"2025-09-02 17:02:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-07-21 13:58:49","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPCC736.11","SPAC6F12.09","SPBC83.03c","SPCC188.13c","SPAC18G6.02c","SPAC664.01c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2022-08-25"},{"uniquename":"PMID:33217381","title":"Sample Preparation and Imaging Conditions Affect mEos3.2 Photophysics in Fission Yeast Cells.","citation":"Biophys J 2021 Jan 05;120(1):21-34","abstract":"Photoconvertible fluorescent proteins (PCFPs) are widely used in super-resolution microscopy and studies of cellular dynamics. However, our understanding of their photophysics is still limited, hampering their quantitative application. For example, we do not know the optimal sample preparation methods or imaging conditions to count protein molecules fused to PCFPs by single-molecule localization microscopy in live and fixed cells. We also do not know how the behavior of PCFPs in live cells compares with fixed cells. Therefore, we investigated how formaldehyde fixation influences the photophysical properties of the popular green-to-red PCFP mEos3.2 in fission yeast cells under a wide range of imaging conditions. We estimated photophysical parameters by fitting a three-state model of photoconversion and photobleaching to the time course of fluorescence signal per yeast cell expressing mEos3.2. We discovered that formaldehyde fixation makes the fluorescence signal, photoconversion rate, and photobleaching rate of mEos3.2 sensitive to the buffer conditions likely by permeabilizing the yeast cell membrane. Under some imaging conditions, the time-integrated mEos3.2 signal per yeast cell is similar in live cells and fixed cells imaged in buffer at pH 8.5 with 1 mM DTT, indicating that light chemical fixation does not destroy mEos3.2 molecules. We also discovered that 405-nm irradiation drove some red-state mEos3.2 molecules to enter an intermediate dark state, which can be converted back to the red fluorescent state by 561-nm illumination. Our findings provide a guide to quantitatively compare conditions for imaging mEos3.2-tagged molecules in yeast cells. Our imaging assay and mathematical model are easy to implement and provide a simple quantitative approach to measure the time-integrated signal and the photoconversion and photobleaching rates of fluorescent proteins in cells.","doi":"10.1016/j.bpj.2020.11.006","authors":"Sun M, Hu K, Bewersdorf J, Pollard TD","authors_abbrev":"Sun M et al.","pubmed_publication_date":"05 Jan 2021","pubmed_entrez_date":"2020-11-20","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-11-22 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26393661","title":"Managing Single-Stranded DNA during Replication Stress in Fission Yeast.","citation":"Biomolecules 2015 Sep 18;5(3):2123-39","abstract":"Replication fork stalling generates a variety of responses, most of which cause an increase in single-stranded DNA. ssDNA is a primary signal of replication distress that activates cellular checkpoints. It is also a potential source of genome instability and a substrate for mutation and recombination. Therefore, managing ssDNA levels is crucial to chromosome integrity. Limited ssDNA accumulation occurs in wild-type cells under stress. In contrast, cells lacking the replication checkpoint cannot arrest forks properly and accumulate large amounts of ssDNA. This likely occurs when the replication fork polymerase and helicase units are uncoupled. Some cells with mutations in the replication helicase (mcm-ts) mimic checkpoint-deficient cells, and accumulate extensive areas of ssDNA to trigger the G2-checkpoint. Another category of helicase mutant (mcm4-degron) causes fork stalling in early S-phase due to immediate loss of helicase function. Intriguingly, cells realize that ssDNA is present, but fail to detect that they accumulate ssDNA, and continue to divide. Thus, the cellular response to replication stalling depends on checkpoint activity and the time that replication stress occurs in S-phase. In this review we describe the signs, signals, and symptoms of replication arrest from an ssDNA perspective. We explore the possible mechanisms for these effects. We also advise the need for caution when detecting and interpreting data related to the accumulation of ssDNA.","doi":"10.3390/biom5032123","authors":"Sabatinos SA, Forsburg SL","authors_abbrev":"Sabatinos SA et al.","pubmed_publication_date":"18 Sep 2015","pubmed_entrez_date":"2015-09-23","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-09-25 00:19:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19047361","title":"Dual functions for the Schizosaccharomyces pombe inositol kinase Ipk1 in nuclear mRNA export and polarized cell growth.","citation":"Eukaryot Cell 2009 Feb;8(2):134-46","abstract":"The inositol 1,3,4,5,6-pentakisphosphate (IP(5)) 2-kinase (Ipk1) catalyzes the production of inositol hexakisphosphate (IP(6)) in eukaryotic cells. Previous studies have shown that IP(6) is required for efficient nuclear mRNA export in the budding yeast Saccharomyces cerevisiae. Here, we report the first functional analysis of ipk1(+) in Schizosaccharomyces pombe. S. pombe Ipk1 (SpIpk1) is unique among Ipk1 orthologues in that it harbors a novel amino (N)-terminal domain with coiled-coil structural motifs similar to those of BAR (Bin-amphiphysin-Rvs) domain proteins. Mutants with ipk1(+) deleted (ipk1Delta) had mRNA export defects as well as pleiotropic defects in polarized growth, cell morphology, endocytosis, and cell separation. The SpIpk1 catalytic carboxy-terminal domain was required to rescue these defects, and the mRNA export block was genetically linked to SpDbp5 function and, likely, IP(6) production. However, the overexpression of the N-terminal domain alone also inhibited these functions in wild-type cells. This revealed a distinct noncatalytic function for the N-terminal domain. To test for connections with other inositol polyphosphates, we also analyzed whether the loss of asp1(+) function, encoding an IP(6) kinase downstream of Ipk1, had an effect on ipk1Delta cells. The asp1Delta mutant alone did not block mRNA export, and its cell morphology, polarized growth, and endocytosis defects were less severe than those of ipk1Delta cells. Moreover, ipk1Delta asp1Delta double mutants had altered inositol polyphosphate levels distinct from those of the ipk1Delta mutant. This suggested novel roles for asp1(+) upstream of ipk1(+). We propose that IP(6) production is a key signaling linchpin for regulating multiple essential cellular processes.","doi":"10.1128/EC.00279-08","authors":"Sarmah B, Wente SR","authors_abbrev":"Sarmah B et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-12-03","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1193145","title":"Morphometric analysis of yeast cells. IV. Increase of the cylindrical diameter of Schizosaccharomyces pombe during the cell cycle.","citation":"Exp Cell Res 1975 Oct 01;95(1):154-8","abstract":"","authors":"Johnson BF, Lu C","authors_abbrev":"Johnson BF et al.","pubmed_publication_date":"01 Oct 1975","pubmed_entrez_date":"1975-10-01","publication_year":"1975","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007741","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4183732","title":"[Biochemical properties of Schizosaccharomyces pombe dending on culture conditions and on the action of inhibitors. 3. Cellular respirations].","citation":"Biochim Biophys Acta 1969 Jun 10;176(4):813-7","abstract":"","authors":"Paranjapye VN, Deshusses J, Posternak T","authors_abbrev":"Paranjapye VN et al.","pubmed_publication_date":"10 Jun 1969","pubmed_entrez_date":"1969-06-10","publication_year":"1969","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9839953","title":"Differences in in vivo acceptor specificity of two galactosyltransferases, the gmh3+ and gma12+ gene products from Schizosaccharomyces pombe.","citation":"Eur J Biochem 1998 Nov 01;257(3):630-7","abstract":"In the fission yeast Schizosaccharomyces pombe, gmh1+, gmh2+ and gmh3+ genes encode alpha-1,2-galactosyltransferase homologues. In an in vitro galactosyltransferase assay, the gmh3+ gene product showed galactose transfer activity toward a-methyl-D-mannoside as an acceptor. The disruption of gma12+, the major galactosyltransferase gene [Chappell, T. G., Hajibagheri, M. A. N., Ayscough, K., Pierce, M. & Warren, G. (1994) Mol. Biol. Cell 5, 519-528], and of gmh3+ in S. pombe caused decreases in the total remaining galactosyltransferase activity and cell surface galactose content. Disruption of gma12+ and gmh3+ also caused an increase in electrophoretic mobility of acid phosphatase, indicating their involvement in the galactosylation of cell surface glycoproteins. The gmh3delta gma12delta double mutant cells had more severe galactose-less phenotypes than single gene mutant cells. HPLC analysis of O-linked mannoprotein oligosaccharides from wild-type and disrupted strains revealed that the gma12+ gene product is responsible for the galactosylation of O-linked oligosaccharide, whereas gmh3+ has no involvement in the process. In contrast, both the gmh3+ and gma12+ gene products are involved in the galactosylation of the N-linked core oligosaccharide Man9GlcNAc2. From these results, it is evident that there are some functional differences between the enzymes in the process of galactosylation. It appears that the gmh3+ gene product transfers galactose to N-linked oligosaccharide, while the gma12+ gene product transfers galactose to both N-linked and O-linked oligosaccharides.","authors":"Yoko-o T, Roy SK, Jigami Y","authors_abbrev":"Yoko-o T et al.","pubmed_publication_date":"01 Nov 1998","pubmed_entrez_date":"1998-12-05","publication_year":"1998","canto_session_key":"92bb4e6ba2d974fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-06-03 13:26:36","canto_approved_date":"2025-10-07 07:00:29","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-01-09 17:15:54","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.06c","SPCC736.04c","SPAC5H10.11","SPAC5H10.13c","SPBP4G3.02"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2019-06-03"},{"uniquename":"PMID:16233721","title":"Production of recombinant human lysosomal acid lipase in Schizosaccharomyces pombe: development of a fed-batch fermentation and purification process.","citation":"J Biosci Bioeng 2004;98(5):366-73","abstract":"A fed-batch fermentation process has been developed to enable the production of large quantities of recombinant human lysosomal acid lipase (hLAL; EC 3.1.1.13), in Schizosaccharomyces pombe, for preclinical studies as a potential enzyme therapy drug. Recombinant S. pombe, clone ASP397-21, expressed enzymatically active hLAL in the secreted form. A feedback fed-batch system was used to determine the optimal feed rate of a 50% glucose solution used as the carbon source. The feed rate of the glucose solution was calculated by a computer-aided system according to the equation; F=q(sf)(VX)/S(in) (q(sf), specific substrate feed rate [gram substrate/gram dry cell weight/h]; V, volume of culture broth [l]; X, cell density [gram dry cell weight/l]; S(in), concentration of growth limiting substrate in feed solution [gram substrate/gram feed solution]). At the time of the initial consumption of glucose in the batch-phase culture, the nutrient supply was automatically initiated by means of monitoring the respiratory quotient change. The obtained profile of the feed rate was applied to the feed forward control fermentation. Finally, the cells were grown up to >50 g dry cell weight/l, and the hLAL expression level was approximately 16,000 U/l. Expressed hLAL protein was purified in a two-step process by hydrophobic interaction and anion exchange chromatographies. Purified recombinant hLAL exhibited a 90-150 kDa broad band upon SDS-PAGE with specific activity of about 300 U/mg. After endoglycosidase H treatment, the band converged to 45 kDa, equal to the calculated molecular weight, suggesting that hLAL produced in S. pombe was hyper-glycosylated. N-terminal analysis of de-glycosylated hLAL revealed that the signal sequence of hLAL was correctly processed in S. pombe.","authors":"Ikeda S, Nikaido K, Araki K, Yoshitake A, Kumagai H, Isoai A","authors_abbrev":"Ikeda S et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2005-10-20","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11069892","title":"Characterization of fission yeast cohesin: essential anaphase proteolysis of Rad21 phosphorylated in the S phase.","citation":"Genes Dev 2000 Nov 01;14(21):2757-70","abstract":"Cohesin complex acts in the formation and maintenance of sister chromatid cohesion during and after S phase. Budding yeast Scc1p/Mcd1p, an essential subunit, is cleaved and dissociates from chromosomes in anaphase, leading to sister chromatid separation. Most cohesin in higher eukaryotes, in contrast, is dissociated from chromosomes well before anaphase. The universal role of cohesin during anaphase thus remains to be determined. We report here initial characterization of four putative cohesin subunits, Psm1, Psm3, Rad21, and Psc3, in fission yeast. They are essential for sister chromatid cohesion. Immunoprecipitation demonstrates stable complex formation of Rad21 with Psm1 and Psm3 but not with Psc3. Chromatin immunoprecipitation shows that cohesin subunits are enriched in broad centromere regions and that the level of centromere-associated Rad21 did not change from metaphase to anaphase, very different from budding yeast. In contrast, Rad21 containing similar cleavage sites to those of Scc1p/Mcd1p is cleaved specifically in anaphase. This cleavage is essential, although the amount of cleaved product is very small (<5%). Mis4, another sister chromatid cohesion protein, plays an essential role for loading Rad21 on chromatin. A simple model is presented to explain the specific behavior of fission yeast cohesin and why only a tiny fraction of Rad21 is sufficient to be cleaved for normal anaphase.","authors":"Tomonaga T, Nagao K, Kawasaki Y, Furuya K, Murakami A, Morishita J, Yuasa T, Sutani T, Kearsey SE, Uhlmann F, Nasmyth K, Yanagida M","authors_abbrev":"Tomonaga T et al.","pubmed_publication_date":"01 Nov 2000","pubmed_entrez_date":"2000-11-09","publication_year":"2000","canto_session_key":"8ba2dcc4ee76f79b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-09-22 18:27:18","canto_approved_date":"2024-05-02 07:54:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-13 15:05:24","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPBC14C8.01c","SPAC10F6.09c","SPAC17H9.20","SPAC31A2.05c","SPBC29A10.04"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-09-22"},{"uniquename":"PMID:21822463","title":"EXTRACTION AND ANALYSIS OF ACTIN NETWORKS BASED ON OPEN ACTIVE CONTOUR MODELS.","citation":"Proc IEEE Int Symp Biomed Imaging 2011 Mar 30;2011:1334-1340","abstract":"Network structures formed by actin filaments are present in many kinds of fluorescence microscopy images. In order to quantify the conformations and dynamics of such actin filaments, we propose a fully automated method to extract actin networks from images and analyze network topology. The method handles well intersecting filaments and, to some extent, overlapping filaments. First we automatically initialize a large number of Stretching Open Active Contours (SOACs) from ridge points detected by searching for plus-to-minus sign changes in the gradient map of the image. These initial SOACs then elongate simultaneously along the bright center-lines of filaments by minimizing an energy function. During their evolution, they may merge or stop growing, thus forming a network that represents the topology of the filament ensemble. We further detect junction points in the network and break the SOACs at junctions to obtain \"SOAC segments\". These segments are then re-grouped using a graph-cut spectral clustering method to represent the configuration of actin filaments. The proposed approach is generally applicable to extracting intersecting curvilinear structures in noisy images. We demonstrate its potential using two kinds of data: (1) actin filaments imaged by Total Internal Reflection Fluorescence Microscopy (TIRFM) in vitro; (2) actin cytoskeleton networks in fission yeast imaged by spinning disk confocal microscopy.","authors":"Xu T, Li H, Shen T, Ojkic N, Vavylonis D, Huang X","authors_abbrev":"Xu T et al.","pubmed_publication_date":"30 Mar 2011","pubmed_entrez_date":"2011-08-09","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23512483","title":"Making an effective switch at the kinetochore by phosphorylation and dephosphorylation.","citation":"Chromosoma 2013 Jun;122(3):135-58","abstract":"The kinetochore, the proteinaceous structure on the mitotic centromere, functions as a mechanical latch that hooks onto microtubules to support directional movement of chromosomes. The structure also brings in a number of signaling molecules, such as kinases and phosphatases, which regulate microtubule dynamics and cell cycle progression. Erroneous microtubule attachment is destabilized by Aurora B-mediated phosphorylation of multiple microtubule-binding protein complexes at the kinetochore, such as the KMN network proteins and the Ska/Dam1 complex, while Plk-dependent phosphorylation of BubR1 stabilizes kinetochore-microtubule attachment by recruiting PP2A-B56. Spindle assembly checkpoint (SAC) signaling, which is activated by unattached kinetochores and inhibits the metaphase-to-anaphase transition, depends on kinetochore recruitment of the kinase Bub1 through Mps1-mediated phosphorylation of the kinetochore protein KNL1 (also known as Blinkin in mammals, Spc105 in budding yeast, and Spc7 in fission yeast). Recruitment of protein phosphatase 1 to KNL1 is necessary to silence the SAC upon bioriented microtubule attachment. One of the key unsolved questions in the mitosis field is how a mechanical change at the kinetochore upon microtubule attachment is converted to these and other chemical signals that control microtubule attachment and the SAC. Rapid progress in the field is revealing the existence of an intricate signaling network created right on the kinetochore. Here we review the current understanding of phosphorylation-mediated regulation of kinetochore functions and discuss how this signaling network generates an accurate switch that turns on and off the signaling output in response to kinetochore-microtubule attachment.","doi":"10.1007/s00412-013-0401-5","authors":"Funabiki H, Wynne DJ","authors_abbrev":"Funabiki H et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-03-21","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:24054","SPCC1020.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12665553","title":"Linear element formation and their role in meiotic sister chromatid cohesion and chromosome pairing.","citation":"J Cell Sci 2003 May 01;116(Pt 9):1719-31","abstract":"Fission yeast does not form synaptonemal complexes in meiotic prophase. Instead, linear elements appear that resemble the axial cores of other eukaryotes. They have been proposed to be minimal structures necessary for proper meiotic chromosome functions. We examined linear element formation in meiotic recombination deficient mutants. The rec12, rec14 and meu13 mutants showed altered linear element formation. Examination of rec12 and other mutants deficient in the initiation of meiotic recombination revealed that occurrence of meiosis-specific DNA breaks is not a precondition for the formation of linear elements. The rec11 and rec8 mutants exhibited strongly impaired linear elements with morphologies specific for these meiotic cohesin mutants. The rec10 and rec16/rep1 mutants lack linear elements completely. The region specificity of loss of recombination in the rec8, rec10 and rec11 mutants can be explained by their defects in linear element formation. Investigation of the rec10 mutant showed that linear elements are basically dispensable for sister chromatid cohesion, but contribute to full level pairing of homologous chromosomes.","authors":"Molnar M, Doll E, Yamamoto A, Hiraoka Y, Kohli J","authors_abbrev":"Molnar M et al.","pubmed_publication_date":"01 May 2003","pubmed_entrez_date":"2003-04-01","publication_year":"2003","canto_session_key":"6c56e65013931544","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-05-29 11:54:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-29 11:54:14","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1753.03c","SPBC32F12.02","SPBC29A10.14","SPBC21B10.12","SPBC1711.14","SPAC25G10.04c","SPAC222.15","SPAC17A5.11","SPCC4E9.01c","SPBC2D10.06"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-05-29"},{"uniquename":"PMID:16734665","title":"RNA interference effector proteins localize to mobile cytoplasmic puncta in Schizosaccharomyces pombe.","citation":"Traffic 2006 Aug;7(8):1032-44","abstract":"Ago1, Dcr1 and Rdp1 are the core components of the RNA interference (RNAi) apparatus in the fission yeast Schizosaccharomyces pombe. They function in distinct gene-silencing pathways that direct homology-dependent degradation of mRNA and modification of chromatin. In addition, Ago1 and Dcr1 regulate enactment of Cdc2-dependent cell cycle checkpoints. The ability of the RNAi apparatus to perform multiple roles in these divergent pathways is sure to require dynamic localization of Ago1, Dcr1 and/or Rdp1. Although limited information is available, comprehensive studies regarding the relative localizations of Ago1, Dcr1 and Rdp1 are lacking. To this end, we employed live-cell imaging and immunoelectron microscopy to study the intracellular localizations of these proteins. In contrast to previous reports, our study results indicate that the bulk of Ago1 and Dcr1 form stable complexes and are associated with large, mobile, highly dynamic cytoplasmic elements. The majority of Rdp1 is localized to the nucleus, but a pool of Rdp1 is associated with the same cytoplasmic structures. The movements of these structures were dependent upon ATP and intact microtubules. Recruitment of the RNAi core proteins to these structures was not dependent upon siRNAs. Together, our data indicate that the enzymes required for the initiation and effector phases of RNA-dependent gene silencing are concentrated in a common intracellular location, an arrangement that would be expected to result in highly efficient post-transcriptional gene silencing.","authors":"Carmichael JB, Stoica C, Parker H, McCaffery JM, Simmonds AJ, Hobman TC","authors_abbrev":"Carmichael JB et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-06-01","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.11","SPAC1B1.01","SPCC188.13c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:38968290","title":"Regulators of rDNA array morphology in fission yeast.","citation":"PLoS Genet 2024 Jul 05;20(7):e1011331","abstract":"Nucleolar morphology is a well-established indicator of ribosome biogenesis activity that has served as the foundation of many screens investigating ribosome production. Missing from this field of study is a broad-scale investigation of the regulation of ribosomal DNA morphology, despite the essential role of rRNA gene transcription in modulating ribosome output. We hypothesized that the morphology of rDNA arrays reflects ribosome biogenesis activity. We established GapR-GFP, a prokaryotic DNA-binding protein that recognizes transcriptionally-induced overtwisted DNA, as a live visual fluorescent marker for quantitative analysis of rDNA organization in Schizosaccharomyces pombe. We found that the morphology-which we refer to as spatial organization-of the rDNA arrays is dynamic throughout the cell cycle, under glucose starvation, RNA pol I inhibition, and TOR activation. Screening the haploid S. pombe Bioneer deletion collection for spatial organization phenotypes revealed large ribosomal protein (RPL) gene deletions that alter rDNA organization. Further work revealed RPL gene deletion mutants with altered rDNA organization also demonstrate resistance to the TOR inhibitor Torin1. A genetic analysis of signaling pathways essential for this resistance phenotype implicated many factors including a conserved MAPK, Pmk1, previously linked to extracellular stress responses. We propose RPL gene deletion triggers altered rDNA morphology due to compensatory changes in ribosome biogenesis via multiple signaling pathways, and we further suggest compensatory responses may contribute to human diseases such as ribosomopathies. Altogether, GapR-GFP is a powerful tool for live visual reporting on rDNA morphology under myriad conditions.","doi":"10.1371/journal.pgen.1011331","authors":"Cockrell AJ, Lange JJ, Wood C, Mattingly M, McCroskey SM, Bradford WD, Conkright-Fincham J, Weems L, Guo MS, Gerton JL","authors_abbrev":"Cockrell AJ et al.","pubmed_publication_date":"05 Jul 2024","pubmed_entrez_date":"2024-07-05","publication_year":"2024","canto_session_key":"9692abfe7a18eb4c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-07-05 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22474355","title":"Heterochromatin protein 1 homologue Swi6 acts in concert with Ers1 to regulate RNAi-directed heterochromatin assembly.","citation":"Proc Natl Acad Sci U S A 2012 Apr 17;109(16):6159-64","abstract":"In fission yeast, the RNAi pathway is required for centromeric heterochromatin assembly. siRNAs derived from centromeric transcripts are incorporated into the RNA-induced transcriptional silencing (RITS) complex and direct it to nascent homologous transcripts. The RNA-induced transcriptional silencing-bound nascent transcripts further recruit the RNA-directed RNA polymerase complex (RDRC) to promote dsRNA synthesis and siRNA production. Heterochromatin coated with Swi6/Heterochromain Protein 1 is then formed following recruitment of chromatin modification machinery. Swi6 is also required for the upstream production of siRNA, although the mechanism for this has remained obscure. Here, we demonstrate that Swi6 recruits RDRC to heterochromatin through Ers1, an RNAi factor intermediate. An ers1(+) mutant allele (ers1-C62) was identified in a genetic screen for mutants that alleviate centromeric silencing, and this phenotype was suppressed by overexpression of either the Hrr1 RDRC subunit or Clr4 histone H3-K9 methyltransferase. Ers1 physically interacts with Hrr1, and loss of Ers1 impairs RDRC centromeric localization. Although Ers1 failed to bind Clr4, a direct interaction with Swi6 was detected, and centromeric localization of Swi6 was enhanced by Clr4 overexpression in ers1-C62 cells. Consistent with this, deletion of swi6(+) reduced centromeric localization of Ers1 and RDRC. Moreover, tethering of Ers1 or Hrr1 to centromeric heterochromatin partially bypassed Swi6 function. These findings demonstrate an alternative mechanism for RDRC recruitment and explain the essential role of Swi6/Heterochromain Protein 1 in RNAi-directed heterochromatin assembly.","doi":"10.1073/pnas.1116972109","authors":"Hayashi A, Ishida M, Kawaguchi R, Urano T, Murakami Y, Nakayama J","authors_abbrev":"Hayashi A et al.","pubmed_publication_date":"17 Apr 2012","pubmed_entrez_date":"2012-04-05","publication_year":"2012","canto_session_key":"52a35f8f6a41d529","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Aki Hayashi","canto_first_approved_date":"2024-03-13 17:52:05","canto_approved_date":"2025-04-24 12:20:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-13 15:55:56","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Aki Hayashi","community_curator":true,"annotation_count":1,"orcid":"0000-0003-1953-1664","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.04c","SPCC11E10.08","SPAC140.03","SPCC736.11","SPBC428.08c","SPBC83.03c","SPCC1393.05","SPBC2G2.09c","SPCC1739.03","SPAC664.01c","SPAC6F12.09","SPBC16C6.10","SPCC613.12c","SPCC970.07c","SPAC18G6.02c","SPCC188.13c","SPCC663.12"],"gene_count":17,"ltp_gene_count":9,"approved_date":"2024-03-13"},{"uniquename":"PMID:14690539","title":"Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments.","citation":"BMC Biochem 2003 Dec 23;4:18","abstract":"Riboflavin synthase catalyzes the transformation of 6,7-dimethyl-8-ribityllumazine into riboflavin in the last step of the riboflavin biosynthetic pathway. Gram-negative bacteria and certain yeasts are unable to incorporate riboflavin from the environment and are therefore absolutely dependent on endogenous synthesis of the vitamin. Riboflavin synthase is therefore a potential target for the development of antiinfective drugs.\nA cDNA sequence from Schizosaccharomyces pombe comprising a hypothetical open reading frame with similarity to riboflavin synthase of Escherichia coli was expressed in a recombinant E. coli strain. The recombinant protein is a homotrimer of 23 kDa subunits as shown by sedimentation equilibrium centrifugation. The protein sediments at an apparent velocity of 4.1 S at 20 degrees C. The amino acid sequence is characterized by internal sequence similarity indicating two similar folding domains per subunit. The enzyme catalyzes the formation of riboflavin from 6,7-dimethyl-8-ribityllumazine at a rate of 158 nmol mg(-1) min(-1) with an apparent KM of 5.7 microM. 19F NMR protein perturbation experiments using fluorine-substituted intermediate analogs show multiple signals indicating that a given ligand can be bound in at least 4 different states. 19F NMR signals of enzyme-bound intermediate analogs were assigned to ligands bound by the N-terminal respectively C-terminal folding domain on basis of NMR studies with mutant proteins.\nRiboflavin synthase of Schizosaccharomyces pombe is a trimer of identical 23-kDa subunits. The primary structure is characterized by considerable similarity of the C-terminal and N-terminal parts. Riboflavin synthase catalyzes a mechanistically complex dismutation of 6,7-dimethyl-8-ribityllumazine affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. The 19F NMR data suggest large scale dynamic mobility in the trimeric protein which may play an important role in the reaction mechanism.","authors":"Fischer M, Schott AK, Kemter K, Feicht R, Richter G, Illarionov B, Eisenreich W, Gerhardt S, Cushman M, Steinbacher S, Huber R, Bacher A","authors_abbrev":"Fischer M et al.","pubmed_publication_date":"23 Dec 2003","pubmed_entrez_date":"2003-12-24","publication_year":"2003","canto_session_key":"c861ab1d9c530008","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-02 15:51:33","canto_approved_date":"2025-07-11 07:58:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-02 15:51:26","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1450.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-07-02"},{"uniquename":"PMID:17173056","title":"Heterochromatin revisited.","citation":"Nat Rev Genet 2007 Jan;8(1):35-46","abstract":"The formation of heterochromatin, which requires methylation of histone H3 at lysine 9 and the subsequent recruitment of chromodomain proteins such as heterochromatin protein HP1, serves as a model for the role of histone modifications and chromatin assembly in epigenetic control of the genome. Recent studies in Schizosaccharomyces pombe indicate that heterochromatin serves as a dynamic platform to recruit and spread a myriad of regulatory proteins across extended domains to control various chromosomal processes, including transcription, chromosome segregation and long-range chromatin interactions.","authors":"Grewal SI, Jia S","authors_abbrev":"Grewal SI et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2006-12-19","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42052570","title":"G-patch proteins: important regulators of pre-mRNA splicing and ribosome biogenesis.","citation":"Front Cell Dev Biol 2026;14:1750689","abstract":"Pre-mRNA splicing is a fundamental step in eukaryotic gene expression, carried out by the spliceosome. This large and dynamic ribonucleoprotein complex undergoes extensive structural rearrangements during each splicing event. Similarly, ribosome biogenesis is a highly regulated process that requires precise control at every stage, from the transcription of pre-rRNA through its chemical modification and cleavage to the final assembly of mature ribosomal subunits. Central to the regulation of both pre-mRNA splicing and ribosome biogenesis are RNA helicases and their cofactors, notably G-patch proteins. The predominance of G-patch proteins in eukaryotes underscores their evolutionary importance in the increasing complexity of RNA processing and ribosome biogenesis. This review summarizes recent findings on the molecular functions and regulatory roles of various G-patch proteins in the yeasts  S. cerevisiae  and  S. pombe , as well as in humans. Growing evidence indicates that these proteins act as critical cofactors of RNA helicases involved in splicing, facilitating the dynamic transitions required for spliceosome activation, catalysis, and disassembly. Beyond splicing, these proteins also contribute to the regulation of ribosome biogenesis and other aspects of RNA metabolism. Dysregulation or mutation of G-patch proteins have been shown to cause aberrant mRNA maturation, altered splicing patterns, impaired ribosome assembly, and genomic instability. Such perturbations are associated with a range of human diseases, including cancer progression. Despite the essential roles of G-patch proteins in regulating pre-mRNA splicing and ribosome biogenesis, the precise molecular functions and interaction networks of many G-patch proteins remain poorly understood. Future studies aimed at elucidating the mechanisms by which these proteins coordinate RNA processing and ribosome biogenesis are therefore essential. Such investigations may help uncover the molecular basis of G-patch protein-associated diseases and reveal new potential targets for therapeutic intervention.","doi":"10.3389/fcell.2026.1750689","authors":"Karika LO, Cipakova I, Hronska L, Cipak L","authors_abbrev":"Karika LO et al.","pubmed_publication_date":"2026","pubmed_entrez_date":"2026-04-29","publication_year":"2026","canto_session_key":"9ac460a0511cf313","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-29 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D85544","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36739478","title":"Vast heterogeneity in cytoplasmic diffusion rates revealed by nanorheology and Doppelgänger simulations.","citation":"Biophys J 2023 Mar 07;122(5):767-783","abstract":"The cytoplasm is a complex, crowded, actively driven environment whose biophysical characteristics modulate critical cellular processes such as cytoskeletal dynamics, phase separation, and stem cell fate. Little is known about the variance in these cytoplasmic properties. Here, we employed particle-tracking nanorheology on genetically encoded multimeric 40 nm nanoparticles (GEMs) to measure diffusion within the cytoplasm of individual fission yeast (Schizosaccharomyces pombe) cellscells. We found that the apparent diffusion coefficients of individual GEM particles varied over a 400-fold range, while the differences in average particle diffusivity among individual cells spanned a 10-fold range. To determine the origin of this heterogeneity, we developed a Doppelgänger simulation approach that uses stochastic simulations of GEM diffusion that replicate the experimental statistics on a particle-by-particle basis, such that each experimental track and cell had a one-to-one correspondence with their simulated counterpart. These simulations showed that the large intra- and inter-cellular variations in diffusivity could not be explained by experimental variability but could only be reproduced with stochastic models that assume a wide intra- and inter-cellular variation in cytoplasmic viscosity. The simulation combining intra- and inter-cellular variation in viscosity also predicted weak nonergodicity in GEM diffusion, consistent with the experimental data. To probe the origin of this variation, we found that the variance in GEM diffusivity was largely independent of factors such as temperature, the actin and microtubule cytoskeletons, cell-cyle stage, and spatial locations, but was magnified by hyperosmotic shocks. Taken together, our results provide a striking demonstration that the cytoplasm is not \"well-mixed\" but represents a highly heterogeneous environment in which subcellular components at the 40 nm size scale experience dramatically different effective viscosities within an individual cell, as well as in different cells in a genetically identical population. These findings carry significant implications for the origins and regulation of biological noise at cellular and subcellular levels.","doi":"10.1016/j.bpj.2023.01.040","authors":"Garner RM, Molines AT, Theriot JA, Chang F","authors_abbrev":"Garner RM et al.","pubmed_publication_date":"07 Mar 2023","pubmed_entrez_date":"2023-02-05","publication_year":"2023","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2023-02-06 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33913187","title":"Characterization of the nanomechanical properties of the fission yeast (Schizosaccharomyces pombe) cell surface by atomic force microscopy.","citation":"Yeast 2021 Aug;38(8):480-492","abstract":"Variations in cell wall composition and biomechanical properties can contribute to the cellular plasticity required during complex processes such as polarized growth and elongation in microbial cells. This study utilizes atomic force microscopy (AFM) to map the cell surface topography of fission yeast, Schizosaccharomyces pombe, at the pole regions and to characterize the biophysical properties within these regions under physiological, hydrated conditions. High-resolution images acquired from AFM topographic scanning reveal decreased surface roughness at the cell poles. Force extension curves acquired by nanoindentation probing with AFM cantilever tips under low applied force revealed increased cell wall deformation and decreased cellular stiffness (cellular spring constant) at cell poles (17 ± 4 mN/m) relative to the main body of the cell that is not undergoing growth and expansion (44 ± 10 mN/m). These findings suggest that the increased deformation and decreased stiffness at regions of polarized growth at fission yeast cell poles provide the plasticity necessary for cellular extension. This study provides a direct biophysical characterization of the S. pombe cell surface by AFM, and it provides a foundation for future investigation of how the surface topography and local nanomechanical properties vary during different cellular processes.","doi":"10.1002/yea.3564","authors":"Gibbs E, Hsu J, Barth K, Goss JW","authors_abbrev":"Gibbs E et al.","pubmed_publication_date":"Aug 2021","pubmed_entrez_date":"2021-04-29","publication_year":"2021","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2021-05-01 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12112233","title":"Schizosaccharomyces pombe spPABP, a homologue of Saccharomyces cerevisiae Pab1p, is a non-essential, shuttling protein that facilitates mRNA export.","citation":"Yeast 2002 Jun 30;19(9):803-10","abstract":"Poly(A)-binding proteins play important roles in mRNA metabolism in eukaryotic cells. We examined the role of the Schizosaccharomyces pombe homologue of the Saccharomyces cerevisiae poly(A)-binding protein, Pab1p, in cellular growth and mRNA export. In contrast to PAB1, the sppabp gene is not essential for cellular viability. Like the human hPABP1 protein, spPABP is cytoplasmically localized and can shuttle between the nucleus and the cytoplasm. We found that a spPABP-GFP fusion protein expressed from a multicopy plasmid could suppress the growth and mRNA export defect of rae1-16 7 nup184-1 synthetic lethal mutations. However, about 20-25% of cells in the population exhibited a pronounced nuclear accumulation of poly(A)(+) RNA. The same cells also localized the spPABP-GFP fusion to the nucleus, suggesting that the shuttling ability of spPABP is related to its function in mRNA export. When a heterologous nuclear export activity from spMex67p was fused to spPABP-GFP fusion protein, it overcame the nuclear retention but did not increase nuclear mRNA export. We discuss the implications of these observations in relation to how spPABP could function in mRNA export. Published in 2002 by John Wiley & Sons, Ltd.","authors":"Thakurta AG, Ho Yoon J, Dhar R","authors_abbrev":"Thakurta AG et al.","pubmed_publication_date":"30 Jun 2002","pubmed_entrez_date":"2002-07-12","publication_year":"2002","canto_session_key":"dbe08e175eeaa405","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-12-15 15:33:06","canto_approved_date":"2019-01-11 17:19:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-15 15:32:55","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP27G11.10c","SPBC16A3.05c","SPAC57A7.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-12-15"},{"uniquename":"PMID:3447747","title":"Acid phosphatase deficient mutants of Schizosaccharomyces pombe are defective in tyrosine uptake.","citation":"Curr Genet 1986;11(2):113-7","abstract":"The uptake of tyrosine and arginine into wild type and acid phosphatase deficient mutants (pho 1) of Schizosaccharomyces pombe was investigated. All 11 pho 1-alleles tested exhibited a reduced tyrosine uptake and impaired uptake cosegregated with the lack of acid phosphatase activity. Kinetic analyses using wild type cells grown in high phosphate medium (acid phosphatase repressed) and low phosphate medium (acid phosphatase derepressed) showed staturation kinetics for tyrosine with a KM of about 2 x 10(-4) M for both media and a V of about 5 nmol min-1 mg-1 and 2 nmol min-1 mg-1 for derepressed and repressed cells respectively. The pho 1-118 strain completely lacked this saturable uptake system for tyrosine. Preliminary evidence suggests that tyrosine uptake may be via a general amino acid permease system and we conclude that mutations in the structural gene of acid phosphatase which abolish enzyme activity lead to a loss of this uptake system. In contrast to tyrosine, arginine uptake seems not to be significantly affected either by different acid phosphatase levels in wild type cells or by the pho 1-118 mutation.","authors":"Coddington A, Schweingruber ME","authors_abbrev":"Coddington A et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_session_key":"c5f265d4d87176f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-10 14:16:02","canto_approved_date":"2021-03-04 16:03:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-06-28 10:33:09","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-10"},{"uniquename":"PMID:21151105","title":"CENP-B preserves genome integrity at replication forks paused by retrotransposon LTR.","citation":"Nature 2011 Jan 06;469(7328):112-5","abstract":"Centromere-binding protein B (CENP-B) is a widely conserved DNA binding factor associated with heterochromatin and centromeric satellite repeats. In fission yeast, CENP-B homologues have been shown to silence long terminal repeat (LTR) retrotransposons by recruiting histone deacetylases. However, CENP-B factors also have unexplained roles in DNA replication. Here we show that a molecular function of CENP-B is to promote replication-fork progression through the LTR. Mutants have increased genomic instability caused by replication-fork blockage that depends on the DNA binding factor switch-activating protein 1 (Sap1), which is directly recruited by the LTR. The loss of Sap1-dependent barrier activity allows the unhindered progression of the replication fork, but results in rearrangements deleterious to the retrotransposon. We conclude that retrotransposons influence replication polarity through recruitment of Sap1 and transposition near replication-fork blocks, whereas CENP-B counteracts this activity and promotes fork stability. Our results may account for the role of LTR in fragile sites, and for the association of CENP-B with pericentromeric heterochromatin and tandem satellite repeats.","doi":"10.1038/nature09608","authors":"Zaratiegui M, Vaughn MW, Irvine DV, Goto D, Watt S, Bähler J, Arcangioli B, Martienssen RA","authors_abbrev":"Zaratiegui M et al.","pubmed_publication_date":"06 Jan 2011","pubmed_entrez_date":"2010-12-15","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1105.04c","SPAC9E9.10c","SPCC1672.02c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:9258669","title":"A recombinationally repressed region between mat2 and mat3 loci shares homology to centromeric repeats and regulates directionality of mating-type switching in fission yeast.","citation":"Genetics 1997 Aug;146(4):1221-38","abstract":"Cells of the fission yeast Schizosaccharomyces pombe switch mating type by replacing genetic information at the transcriptionally active mat1 locus with sequences copied from one of two closely linked silent loci, mat2-P or mat3-M. By a process referred to as directionality of switching, cells predominantly switch to the opposite mat1 allele; the mat1-P allele preferentially recombines with mat3, while mat1-M selects the mat2. In contrast to efficient recombination at mat1, recombination within the adjoining mat2-mat3 interval is undetectable. We defined the role of sequences between mat2 and mat3, designated the K-region, in directionality as well as recombinational suppression. Cloning and sequencing analysis revealed that a part of the K-region is homologous to repeat sequences present at centromeres, which also display transcriptional and recombinational suppression. Replacement of 7.5 kb of the K-region with the ura4+ gene affected directionality in a variegated manner. Analysis of the swi6-mod locus, which was previously shown to affect directionality, in K delta::ura4+ strains suggested the existence of at least two overlapping directionality mechanisms. Our work furthers the model that directionality is regulated by cell-type-specific organization of the heterochromatin-like structure in the mating-type region and provides evidence that the K-region contributes to silencing of the mat2-mat3 interval.","authors":"Grewal SI, Klar AJ","authors_abbrev":"Grewal SI et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24249577","title":"Long noncoding RNA-based chromatin control of germ cell differentiation: a yeast perspective.","citation":"Chromosome Res 2013 Dec;21(6-7):653-63","abstract":"Germ cell differentiation, the cellular process by which a diploid progenitor cell produces by meiotic divisions haploid cells, is conserved from the unicellular yeasts to mammals. Over the recent years, yeast germ cell differentiation process has proven to be a powerful biological system to identify and study several long noncoding RNAs (lncRNAs) that play a central role in regulating cellular differentiation by acting directly on chromatin. Remarkably, in the well-studied budding yeast Saccharomyces cerevisiae and fission yeast Schizosaccharomyces pombe, the lncRNA-based chromatin regulations of germ cell differentiation are quite different. In this review, we present an overview of these regulations by focusing on the mechanisms and their respective functions both in S. cerevisiae and in S. pombe. Part of these lncRNA-based chromatin regulations may be conserved in other eukaryotes and play critical roles either in the context of germ cell differentiation or, more generally, in the development of multicellular organisms.","doi":"10.1007/s10577-013-9393-5","authors":"Hiriart E, Verdel A","authors_abbrev":"Hiriart E et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-20","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10388810","title":"Identification and characterization of Schizosaccharomyces pombe asp1(+), a gene that interacts with mutations in the Arp2/3 complex and actin.","citation":"Genetics 1999 Jul;152(3):895-908","abstract":"The Arp2/3 complex is an essential component of the actin cytoskeleton in yeast and is required for the movement of actin patches. In an attempt to identify proteins that interact with this complex in the fission yeast Schizosaccharomyces pombe, we sought high-copy suppressors of the S. pombe arp3-c1 mutant, and have identified one, which we have termed asp1(+). The asp1(+) open reading frame (ORF) predicts a highly conserved protein of 921 amino acids with a molecular mass of 106 kD that does not contain motifs of known function. Neither asp1(+) nor its apparent Saccharomyces cerevisiae ortholog, VIP1, are essential genes. However, disruption of asp1(+) leads to altered morphology and growth properties at elevated temperatures and defects in polarized growth. The asp1 disruption strain also is hypersensitive to Ca+ ions and to low pH conditions. Although Asp1p is not stably associated with the Arp2/3 complex nor localized in any discrete structure within the cytoplasm, the asp1 disruption mutant was synthetically lethal with mutations in components of the Arp2/3 complex, arp3-c1 and sop2-1, as well as with a mutation in actin, act1-48. Moreover, the vip1 disruption strain showed a negative genetic interaction with a las17Delta strain. We conclude that Asp1p/Vip1p is important for the function of the cortical actin cytoskeleton.","authors":"Feoktistova A, McCollum D, Ohi R, Gould KL","authors_abbrev":"Feoktistova A et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-02","publication_year":"1999","canto_session_key":"1fecc0470053ec75","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-26 14:16:55","canto_approved_date":"2021-09-27 12:35:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-19 15:31:36","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.03","SPCC1672.06c","SPAC4A8.15c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-10-26"},{"uniquename":"PMID:20299449","title":"A chromodomain switch mediated by histone H3 Lys 4 acetylation regulates heterochromatin assembly.","citation":"Genes Dev 2010 Apr 01;24(7):647-52","abstract":"Chromodomain proteins (Chp1/Chp2/Swi6/Clr4) bind to methylated H3K9 (H3K9me) and regulate pericentric heterochromatin in fission yeast. Chp1 and Clr4 (H3K9-HMT), bind transcriptionally active heterochromatin, whereas Chp2/Swi6 (HP1 homologs) are recruited during the inactive state. We show that H3K4 acetylation (H3K4ac) plays a role in the transition of dimethylated H3K9 (H3K9me2) occupancy from Chp1/Clr4 to Chp2/Swi6. H3K4ac, mediated by Mst1, is enriched at pericentromeres concomitantly with heterochromatin reassembly. H3K4R (Lys --> Arg) mutation increases Chp1 and decreases Chp2/Swi6 pericentric occupancy and exhibits centromeric desilencing. Consistent with structural data, H3K4ac specifically reduces Chp1/Clr4 affinity to H3K9me. We propose that H3K4ac mediates a chromodomain switch from Chp1/Clr4 to Swi6/Chp2 to allow heterochromatin reassembly.","doi":"10.1101/gad.1881710","authors":"Xhemalce B, Kouzarides T","authors_abbrev":"Xhemalce B et al.","pubmed_publication_date":"01 Apr 2010","pubmed_entrez_date":"2010-03-20","publication_year":"2010","canto_session_key":"5339c3839d6a7634","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-09 09:16:13","canto_approved_date":"2024-09-27 16:58:31","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-01-08 15:21:42","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":21,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.02c","SPBC1105.11c","SPAC1834.04","SPBC16D10.07c","SPCC306.04c","SPAC1952.05","SPBC800.03","SPAC17G8.13c","SPAC1783.04c","SPCC338.17c","SPCC132.02","SPBC16C6.10","SPBC342.06c","SPAC29A4.20","SPBC8D2.04","SPBC36.05c","SPAC664.01c","SPBC428.08c","SPAC139.06","SPAC3G9.07c","SPAC637.12c","SPBC28F2.12"],"gene_count":22,"ltp_gene_count":14,"approved_date":"2016-02-09"},{"uniquename":"PMID:17363370","title":"HULC, a histone H2B ubiquitinating complex, modulates heterochromatin independent of histone methylation in fission yeast.","citation":"J Biol Chem 2007 May 11;282(19):14065-72","abstract":"Heterochromatin in fission yeast is targeted dynamically by opposing chromatin-modifying activities capable of alleviating or promoting transcriptional gene silencing. In this study, we report the biochemical and genetic characterization of a ubiquitin-conjugating enzyme Rhp6 (a homolog of budding yeast Rad6), which has been shown to negatively affect stability of heterochromatic structures. We show that Rhp6 is a component of the multisubunit protein complex (termed HULC) that also contains two RING finger proteins Rfp1 and Rfp2, sharing homology with budding yeast Bre1 protein and a unique serine-rich protein Shf1. HULC is required for ubiquitination of histone H2B at lysine 119 (H2B-K119), and it localizes to heterochromatic sequences. Moreover, our analyses suggest that Rhp6-induced changes in heterochromatic silencing are mediated predominantly through H2B ubiquitination (ubH2B), and they correlate with increased RNA polymerase II levels at repeat elements embedded within heterochromatin domains. Interestingly, heterochromatic derepression caused by Rhp6 occurs independently of the involvement of HULC subunits and ubH2B in methylation of histone H3 at lysine 4 (H3K4me). These analyses implicate ubH2B in modulation of heterochromatin, which has important implications for dynamics and many functions associated with heterochromatic structures.","authors":"Zofall M, Grewal SI","authors_abbrev":"Zofall M et al.","pubmed_publication_date":"11 May 2007","pubmed_entrez_date":"2007-03-17","publication_year":"2007","canto_session_key":"6e4bd6933c454826","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-09-20 16:53:57","canto_approved_date":"2022-07-21 16:38:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-13 12:33:25","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":40,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.09","SPAC664.01c","SPAC22F8.12c","SPBC28F2.12","SPCC970.10c","SPCC1919.15","SPAC18B11.07c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2021-09-20"},{"uniquename":"PMID:39662905","title":"Mutations in the 5' untranslated region fine-tune the translational control of heterologously expressed genes.","citation":"Genes Genet Syst 2024 Dec 12;","abstract":"Strict control of the expression levels of heterologously introduced protein-coding genes is important for the functional analysis of the protein of interest and its effective use in new situations. For this purpose, various promoters with different expression strengths, codon optimization, and expression stimulation by low molecular weight compounds are commonly used. However, methods to control protein expression levels by combining regulation of translation efficiency have not been studied in detail. We previously observed relatively high basal expression of Cre, when it was heterologously expressed in fission yeast. Here, we used a fission yeast strain that is susceptible to centromere disruption and thus highly sensitive to Cre levels and report successful fine-tuning of heterologous Cre expression by modulating the Cre translation efficiency. To inhibit Cre translation initiation, we generated two mutations in the 5' untranslated region of the Cre mRNAs which both interfered with the scanning process of start codon recognition, mediated by the specialized ribosomal subunits. These mutations successfully reduced the levels of exogenously expressed Cre to different degrees in fission yeast. Combining them with different promoter strengths allowed us to conduct centromere-disruption experiments in fission yeast. Our data indicate that modification of translational control is an additional tool in heterologous gene expression.","doi":"10.1266/ggs.24-00188","authors":"Kuse R, Ishii K","authors_abbrev":"Kuse R et al.","pubmed_publication_date":"12 Dec 2024","pubmed_entrez_date":"2024-12-11","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-12-13 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:865481","title":"Protoplast fusion of Schizosaccharomyces pombe Auxotrophic mutants of identical mating-type.","citation":"Mol Gen Genet 1977 Feb 28;151(1):77-81","abstract":"Protoplasts of methionine- and lysine-requiring h- mutants isolated from the L972 h- strain of Schizosaccharomyces pombe were fused. The protoplasts were obtained from the cells with enzymes produced by Trichoderma viride. When a mixture of the protoplasts was treated with 30% PEG 4000 solution containing 10 mM CaCl2, cell fusion and complementation was attained with a frequency of 0.17%. Both fusion partners were recovered among the spores after crossing of the fusion products with the strain M210 ade6 h+. Cytological and haploidization examinations showed that the fusion cells are not heterokaryons, and that the increased amount of genetic material is situated in one nucleus.","authors":"Sipiczki M, Ferenczy L","authors_abbrev":"Sipiczki M et al.","pubmed_publication_date":"28 Feb 1977","pubmed_entrez_date":"1977-02-28","publication_year":"1977","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22375066","title":"AMPK phosphorylation by Ssp1 is required for proper sexual differentiation in fission yeast.","citation":"J Cell Sci 2012 Jun 01;125(Pt 11):2655-64","abstract":"The AMP-activated protein kinase (AMPK) is a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes. Here, we report that fission yeast cells lacking AMPK activity are unable to advance entry into mitosis in response to nitrogen starvation and cannot undergo proper G1 arrest and cell differentiation. We also show that AMPK is important in the promotion of the nuclear localization and accumulation of the Ste11 transcription factor. As in animal cells, the fission yeast CaMKK ortholog (Ssp1) phosphorylates and activates the catalytic subunit of AMPK (Ssp2) in its activation loop (Thr189) when cells are starved for nitrogen or glucose. Interestingly, we found that the phosphorylation of Ssp2 on Thr189 is required for nuclear accumulation of AMPK. Our data demonstrate the existence of a signal transduction pathway activated by nutrient starvation that triggers Ssp2 phosphorylation and AMPK redistribution from the cytoplasm to the nucleus. This pathway is important to advance fission cells into mitosis and to establish a timely pre-Start G1 cell cycle arrest for mating.","doi":"10.1242/jcs.098533","authors":"Valbuena N, Moreno S","authors_abbrev":"Valbuena N et al.","pubmed_publication_date":"01 Jun 2012","pubmed_entrez_date":"2012-03-01","publication_year":"2012","canto_session_key":"5a6fef3458353ae1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 12:20:38","canto_approved_date":"2026-04-08 07:15:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-26 09:43:08","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":41,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPCC297.03","SPCC1919.03c","SPCC74.03c","SPAC1556.08c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-10-31"},{"uniquename":"PMID:12917337","title":"Retention but not recruitment of Crb2 at double-strand breaks requires Rad1 and Rad3 complexes.","citation":"Mol Cell Biol 2003 Sep;23(17):6150-8","abstract":"The fission yeast checkpoint protein Crb2, related to budding yeast Rad9 and human 53BP1 and BRCA1, has been suggested to act as an adapter protein facilitating the phosphorylation of specific substrates by Rad3-Rad26 kinase. To further understand its role in checkpoint signaling, we examined its localization in live cells by using fluorescence microscopy. In response to DNA damage, Crb2 localizes to distinct nuclear foci, which represent sites of DNA double-strand breaks (DSBs). Crb2 colocalizes with Rad22 at persistent foci, suggesting that Crb2 is retained at sites of DNA damage during repair. Damage-induced Crb2 foci still form in cells defective in Rad1, Rad3, and Rad17 complexes, but these foci do not persist as long as in wild-type cells. Our results suggest that Crb2 functions at the sites of DNA damage, and its regulated persistent localization at damage sites may be involved in facilitating DNA repair and/or maintaining the checkpoint arrest while DNA repair is under way.","authors":"Du LL, Nakamura TM, Moser BA, Russell P","authors_abbrev":"Du LL et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-08-15","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9632794","title":"Myb-related Schizosaccharomyces pombe cdc5p is structurally and functionally conserved in eukaryotes.","citation":"Mol Cell Biol 1998 Jul;18(7):4097-108","abstract":"Schizosaccharomyces pombe cdc5p is a Myb-related protein that is essential for G2/M progression. To explore the structural and functional conservation of Cdc5 throughout evolution, we isolated Cdc5-related genes and cDNAs from Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, and Homo sapiens. Supporting the notion that these Cdc5 gene family members are functionally homologous to S. pombe cdc5(+), human and fly Cdc5 cDNAs are capable of complementing the temperature-sensitive lethality of the S. pombe cdc5-120 mutant. Furthermore, S. cerevisiae CEF1 (S. cerevisiae homolog of cdc5(+)), like S. pombe cdc5(+), is essential during G2/M. The location of the cdc5-120 mutation, as well as mutational analyses of Cef1p, indicate that the Myb repeats of cdc5p and Cef1p are important for their function in vivo. However, we found that unlike in c-Myb, single residue substitutions of glycines for hydrophobic residues within the Myb repeats of Cef1p, which are essential for maintaining structure of the Myb domain, did not impair Cef1p function in vivo. Rather, multiple W-to-G substitutions were required to inactivate Cef1p, and many of the substitution mutants were found to confer temperature sensitivity. Although it is possible that Cef1p acts as a transcriptional activator, we have demonstrated that Cef1p is not involved in transcriptional activation of a class of G2/M-regulated genes typified by SWI5. Collectively, these results suggest that Cdc5 family members participate in a novel pathway to regulate G2/M progression.","authors":"Ohi R, Feoktistova A, McCann S, Valentine V, Look AT, Lipsick JS, Gould KL","authors_abbrev":"Ohi R et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-06-25","publication_year":"1998","canto_session_key":"a0b6500f8359d8f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-03 09:56:15","canto_approved_date":"2019-01-03 09:56:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-03 09:55:58","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.12"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-01-03"},{"uniquename":"PMID:24190807","title":"The genetic fine structure of nonsense suppressors in Schizosaccharomyces pombe : I. sup3 and sup9.","citation":"Curr Genet 1979 Dec;1(1):45-61","abstract":"Meiotic and mitotic fine-structure maps of two efficient UGA suppressors of Schizosaccharomyces pombe which are known (sup3-e) or inferred (sup9-e) to code for two serine tRNAs carrying the mutant anticodon U*CA (Kohli et al. 1979a, b, Rafalski et al. 1979) are presented. Maps based on spontaneous meiotic, spontaneous mitotic and MMS induced mitotic recombination between the primary site of the anticodon mutation and a number of inactivating second-site mutations are similar. Specific marker effects, which drastically increase the frequency of spontaneous meiotic and mitotic recombination in crosses involving one or the other of four exceptional sites (including the anticodon sites of both sup3-e and sup9-e), disappear when mapping is based on MMS induced mitotic recombination. The meiotic marker effect characterizing the anticodon site of one of the two efficient UGA suppressors (sup3-e) also disappears upon further mutation to an inefficient UAA suppressor allele (sup3-i), as shown by its absence in a fine-structure map based on meiotic recombination between the anticodon mutation of this ochre suppressor allele and a new set of inactivating second-site mutations derived from it.","doi":"10.1007/BF00413306","authors":"Hofer F, Hollenstein H, Janner F, Minet M, Thuriaux P, Leupold U","authors_abbrev":"Hofer F et al.","pubmed_publication_date":"Dec 1979","pubmed_entrez_date":"2013-11-06","publication_year":"1979","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 06:09:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23681661","title":"Unbiased segregation of fission yeast chromosome 2 strands to daughter cells.","citation":"Chromosome Res 2013 May;21(3):297-309","abstract":"The base complementarity feature (Watson and Crick in Nature 171(4356):737-738, 1953) and the rule of semi-conservative mode of DNA replication (Messelson and Stahl in Proc Natl Acad Sci U S A 44:671-682, 1958) dictate that two identical replicas of the parental chromosome are produced during replication. In principle, the inherent strand sequence differences could generate nonequivalent daughter chromosome replicas if one of the two strands were epigenetically imprinted during replication to effect silencing/expression of developmentally important genes. Indeed, inheritance of such a strand- and site-specific imprint confers developmental asymmetry to fission yeast sister cells by a phenomenon called mating/cell-type switching. Curiously, location of DNA strands with respect to each other at the centromere is fixed, and as a result, their selected segregation to specific sister chromatid copies occurs in eukaryotic cells. The yeast system provides a unique opportunity to determine the significance of such biased strand distribution to sister chromatids. We determined whether the cylindrical-shaped yeast cell distributes the specific chromosomal strand to the same cellular pole in successive cycles of cell division. By observing the pattern of recurrent mating-type switching in progenies of individual cells by microscopic analyses, we found that chromosome 2 strands are distributed by the random mode in successive cell divisions. We also exploited unusual \"hotspot\" recombination features of this system to investigate whether there is selective segregation of strands such that oldest Watson-containing strands co-segregate in the diploid cell at mitosis. Our data suggests that chromosome 2 strands are segregated independently to those of the homologous chromosome.","doi":"10.1007/s10577-013-9352-1","authors":"Klar AJ, Bonaduce MJ","authors_abbrev":"Klar AJ et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-05-18","publication_year":"2013","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9021126","title":"Heat-shock response in Schizosaccharomyces pombe cells lacking cyclic AMP-dependent phosphorylation.","citation":"Curr Genet 1997 Feb;31(2):112-8","abstract":"Heat sensitivity at 48 degrees C was determined in log-phase cultures of control and pka1-disrupted cells of the fission yeast Schizosaccharomyces pombe grown at 25 degrees C. Cells devoid of protein kinase A exhibited a considerable heat-shock resistance as compared to control cells. Addition of cAMP to control cells prompted a further decrease in viability during heat shock. This effect was not observed with pka1-disrupted cells, suggesting that cAMP-dependent phosphorylation is involved in modulation of the heat-shock response. When control or pka1-disrupted cells were grown at 25 degrees C and then shifted to 37 degrees C they acquired thermo-tolerance to a subsequent treatment at 48 degrees C both in the absence and in the presence of exogenous cAMP. Inhibition of protein synthesis during the adaptive treatment did not block the development of thermo-tolerance. However, the arrest in translation significantly prevented trehalose accumulation in control cells but only slightly affected trehalose increase in pka1-disrupted cells. These data indicate that heat resistance may be established in growing cells of S. pombe by at least two independent post-translational mechanisms: a decrease in cAMP-dependent protein phosphorylation and a hitherto unknown process which may be independent of trehalose accumulation.","authors":"Fernández J, Soto T, Vicente-Soler J, Cansado J, Gacto M","authors_abbrev":"Fernández J et al.","pubmed_publication_date":"Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12773390","title":"The role of Ppe1/PP6 phosphatase for equal chromosome segregation in fission yeast kinetochore.","citation":"EMBO J 2003 Jun 02;22(11):2752-63","abstract":"Mis12 is a kinetochore protein essential for equal chromosome segregation and is evolutionarily conserved from yeast to human. In this study, we report the isolation and characterization of suppressors of the mis12 mutant in fission yeast. Our results indicate that Mis12 is negatively regulated by a highly conserved protein phosphatase Ppe1 (scSit4/dmPPV/hPP6) or its bound partner Ekc1 (scSAP), and it is positively regulated by a counteracting kinase Gsk3. Mass spectrometry analysis shows that at least two sites in Mis12 are phosphorylated. This mechanism of suppression occurs at the level of localization recovery of Mis12 to the kinetochore chromatin. Consistently, Mis12 and a subpopulation of Ppe1/Ekc1 were found to behave like non-histone-type chromatin-associating proteins in the chromatin fractionation assay. Mutant analysis of Ppe1 and Ekc1 revealed that they are important for faithful chromosome segregation, as the mutants exhibited unequal chromosome segregation similar to mis12 in the presence of a low concentration of tubulin poison. Ppe1/PP6 directly or indirectly modulates kinetochore chromatin protein Mis12 to ensure progression into normal anaphase.","authors":"Goshima G, Iwasaki O, Obuse C, Yanagida M","authors_abbrev":"Goshima G et al.","pubmed_publication_date":"02 Jun 2003","pubmed_entrez_date":"2003-05-30","publication_year":"2003","canto_session_key":"1beda591c5c5e770","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-04-23 16:59:38","canto_approved_date":"2024-03-28 12:53:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-10-10 10:51:21","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.04c","SPAC1687.15","SPBC1105.17","SPCC663.01c","SPCC1739.12"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-04-23"},{"uniquename":"PMID:22740629","title":"α-Actinin and fimbrin cooperate with myosin II to organize actomyosin bundles during contractile-ring assembly.","citation":"Mol Biol Cell 2012 Aug;23(16):3094-110","abstract":"The actomyosin contractile ring assembles through the condensation of a broad band of nodes that forms at the cell equator in fission yeast cytokinesis. The condensation process depends on actin filaments that interconnect nodes. By mutating or titrating actin cross-linkers α-actinin Ain1 and fimbrin Fim1 in live cells, we reveal that both proteins are involved in node condensation. Ain1 and Fim1 stabilize the actin cytoskeleton and modulate node movement, which prevents nodes and linear structures from aggregating into clumps and allows normal ring formation. Our computer simulations modeling actin filaments as semiflexible polymers reproduce the experimental observations and provide a model of how actin cross-linkers work with other proteins to regulate actin-filament orientations inside actin bundles and organize the actin network. As predicted by the simulations, doubling myosin II Myo2 level rescues the node condensation defects caused by Ain1 overexpression. Taken together, our work supports a cooperative process of ring self-organization driven by the interaction between actin filaments and myosin II, which is progressively stabilized by the cross-linking proteins.","doi":"10.1091/mbc.E12-02-0123","authors":"Laporte D, Ojkic N, Vavylonis D, Wu JQ","authors_abbrev":"Laporte D et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-06-29","publication_year":"2012","canto_session_key":"b6cddd232070dbc1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1778.06c","SPAC15A10.08","SPBC21.06c","SPCC1739.11c","SPAC20G8.05c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"EMBL:AU010799","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35228260","title":"Growth-rate-dependent and nutrient-specific gene expression resource allocation in fission yeast.","citation":"Life Sci Alliance 2022 May;5(5)","abstract":"Cellular resources are limited and their relative allocation to gene expression programmes determines physiological states and global properties such as the growth rate. Here, we determined the importance of the growth rate in explaining relative changes in protein and mRNA levels in the simple eukaryote  Schizosaccharomyces pombe  grown on non-limiting nitrogen sources. Although expression of half of fission yeast genes was significantly correlated with the growth rate, this came alongside wide-spread nutrient-specific regulation. Proteome and transcriptome often showed coordinated regulation but with notable exceptions, such as metabolic enzymes. Genes positively correlated with growth rate participated in every level of protein production apart from RNA polymerase II-dependent transcription. Negatively correlated genes belonged mainly to the environmental stress response programme. Critically, metabolic enzymes, which represent ∼55-70% of the proteome by mass, showed mostly condition-specific regulation. In summary, we provide a rich account of resource allocation to gene expression in a simple eukaryote, advancing our basic understanding of the interplay between growth-rate-dependent and nutrient-specific gene expression.","doi":"10.26508/lsa.202101223","authors":"Kleijn IT, Martínez-Segura A, Bertaux F, Saint M, Kramer H, Shahrezaei V, Marguerat S","authors_abbrev":"Kleijn IT et al.","pubmed_publication_date":"May 2022","pubmed_entrez_date":"2022-03-01","publication_year":"2022","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-03-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29866182","title":"RNAi-dependent heterochromatin assembly in fission yeast Schizosaccharomyces pombe requires heat-shock molecular chaperones Hsp90 and Mas5.","citation":"Epigenetics Chromatin 2018 Jun 04;11(1):26","abstract":"Heat-shock molecular chaperone proteins (Hsps) promote the loading of small interfering RNA (siRNA) onto RNA interference (RNAi) effector complexes. While the RNAi process is coupled with heterochromatin assembly in several model organisms, it remains unclear whether the Hsps contribute to epigenetic gene regulation. In this study, we used the fission yeast Schizosaccharomyces pombe as a model organism and investigated the roles of Hsp90 and Mas5 (a nucleocytoplasmic type-I Hsp40 protein) in RNAi-dependent heterochromatin assembly.\nUsing a genetic screen and biochemical analyses, we identified Hsp90 and Mas5 as novel silencing factors. Mutations in the genes encoding these factors caused derepression of silencing at the pericentromere, where heterochromatin is assembled in an RNAi-dependent manner, but not at the subtelomere, where RNAi is dispensable. The mutations also caused a substantial reduction in the level of dimethylation of histone H3 at Lys9 at the pericentromere, where association of the Argonaute protein Ago1 was also abrogated. Consistently, siRNA corresponding to the pericentromeric repeats was undetectable in these mutant cells. In addition, levels of Tas3, which is a protein in the RNA-induced transcriptional silencing complex along with Ago1, were reduced in the absence of Mas5.\nOur results suggest that the Hsps Hsp90 and Mas5 contribute to RNAi-dependent heterochromatin assembly. In particular, Mas5 appears to be required to stabilize Tas3 in vivo. We infer that impairment of Hsp90 and Hsp40 also may affect the integrity of the epigenome in other organisms.","doi":"10.1186/s13072-018-0199-8","authors":"Okazaki K, Kato H, Iida T, Shinmyozu K, Nakayama JI, Murakami Y, Urano T","authors_abbrev":"Okazaki K et al.","pubmed_publication_date":"04 Jun 2018","pubmed_entrez_date":"2018-06-06","publication_year":"2018","canto_session_key":"c57e1d4a37ec567b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroaki Kato","canto_first_approved_date":"2018-06-20 14:54:56","canto_approved_date":"2024-02-02 20:31:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-18 05:34:25","canto_added_date":"2018-06-07 00:15:03","annotation_curators":[{"name":"Hiroaki Kato","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.04c","SPCC1739.13","SPCC736.11","SPAC13G7.02c","SPBC1734.11","SPBC83.03c","SPAC140.03","SPBC405.06","SPAC212.11"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2018-06-20"},{"uniquename":"EMBL:SPC04180","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20435771","title":"Iron-dependent remodeling of fungal metabolic pathways associated with ferrichrome biosynthesis.","citation":"Appl Environ Microbiol 2010 Jun;76(12):3806-17","abstract":"The fission yeast Schizosaccharomyces pombe excretes and accumulates the hydroxamate-type siderophore ferrichrome. The sib1(+) and sib2(+) genes encode, respectively, a siderophore synthetase and an l-ornithine N(5)-oxygenase that participate in ferrichrome biosynthesis. In the present report, we demonstrate that sib1(+) and sib2(+) are repressed by the GATA-type transcriptional repressor Fep1 in response to high levels of iron. We further found that the loss of Fep1 results in increased ferrichrome production. We showed that a sib1Delta sib2Delta mutant strain exhibits a severe growth defect on iron-poor media. We determined that two metabolic pathways are involved in biosynthesis of ornithine, an obligatory precursor of ferrichrome. Ornithine is produced by hydrolysis of arginine by the Car1 and Car3 proteins. Although car3(+) was constitutively expressed, car1(+) transcription levels were repressed upon exposure to iron, with a concomitant decrease of Car1 arginase activity. Ornithine is also generated by transformation of glutamate, which itself is produced by two separate biosynthetic pathways which are transcriptionally regulated by iron in an opposite fashion. In one pathway, the glutamate dehydrogenase Gdh1, which produces glutamate from 2-ketoglutarate, was repressed under iron-replete conditions in a Fep1-dependent manner. The other pathway involves two coupled enzymes, glutamine synthetase Gln1 and Fe-S cluster-containing glutamate synthase Glt1, which were both repressed under iron-limiting conditions but were expressed under iron-replete conditions. Collectively, these results indicate that under conditions of iron deprivation, yeast remodels metabolic pathways linked to ferrichrome synthesis in order to limit iron utilization without compromising siderophore production and its ability to sequester iron from the environment.","doi":"10.1128/AEM.00659-10","authors":"Mercier A, Labbé S","authors_abbrev":"Mercier A et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-05-04","publication_year":"2010","canto_session_key":"3bbe58d3273dc0d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-15 08:03:54","canto_approved_date":"2025-03-12 16:01:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-13 02:27:52","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23E2.01","SPAC23G3.02c","SPBC16E9.01c","SPBP26C9.02c","SPCC622.12c","SPCC645.03c","SPAC23G3.03","SPAC3H1.07","SPAPB1E7.07","SPCC777.09c","SPAC23H4.06"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2017-09-15"},{"uniquename":"PMID:35622527","title":"Phase separation of Dri1 contributes to heterochromatin formation in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2022;2022","abstract":"The RNA binding protein Dri1 facilitates heterochromatin assembly via the RNAi pathway and histone deacetylases (HDAC). Dri1 contains an intrinsically disordered region (IDR) and three zinc fingers at its C-terminus, which are important for its role in heterochromatin silencing. Both IDR and zinc fingers have been implicated in mediating liquid-liquid phase separation (LLPS). In this study, we investigated the phase separation properties of Dri1. We observed that Dri1 undergoes phase separation  in vitro  . Dri1 also exhibits liquid-like behavior  in vivo  . Combined with our previous findings, our data support a model in which the phase-separated condensates formed by Dri1 may help recruit RNAi components and HDAC to mediate heterochromatin assembly.","doi":"10.17912/micropub.biology.000559","authors":"Ban H, Sun W, Chen Y, Li F","authors_abbrev":"Ban H et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-05-27","publication_year":"2022","canto_session_key":"30a0aa3d564584f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2025-01-07 12:14:24","canto_approved_date":"2025-01-07 12:14:25","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-01-01 12:26:46","canto_added_date":"2022-05-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.04c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2025-01-07"},{"uniquename":"PMID:14625560","title":"Hsk1-Dfp1 is required for heterochromatin-mediated cohesion at centromeres.","citation":"Nat Cell Biol 2003 Dec;5(12):1111-6","abstract":"Heterochromatin performs a central role in chromosome segregation and stability by promoting cohesion at centromeres. Establishment of both heterochromatin-mediated silencing and cohesion requires passage through S phase, although the mechanism is unknown. Here we demonstrate that Schizosaccharomyces pombe Hsk1 (CDC7), a conserved Dbf4-dependent protein kinase (DDK) that regulates replication initiation, interacts with and phosphorylates the heterochromatin protein 1 (HP1) equivalent Swi6 (ref. 6). Hsk1 and its regulatory subunit Dfp1 function downstream of Swi6 localization to promote heterochromatin function and cohesion specifically at centromeres. This role for Hsk1-Dfp1 is separable from its replication initiation activity, providing a temporal link between S phase and centromere cohesion that is mediated by heterochromatin.","authors":"Bailis JM, Bernard P, Antonelli R, Allshire RC, Forsburg SL","authors_abbrev":"Bailis JM et al.","pubmed_publication_date":"Dec 2003","pubmed_entrez_date":"2003-11-20","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c","SPAC17H9.20","SPBC776.12c","SPCC550.13"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:17213188","title":"Regulation of the nuclear poly(A)-binding protein by arginine methylation in fission yeast.","citation":"J Biol Chem 2007 Mar 09;282(10):7552-62","abstract":"Two structurally different poly(A)-binding proteins (PABP) bind the poly(A) tract of mRNAs in most mammalian cells: PABPC in the cytoplasm and PABP2/PABPN1 in the nucleus. Whereas yeast orthologs of the cytoplasmic PABP are characterized, a gene product homologous to mammalian PABP2 has not been identified in yeast. We report here the identification of a homolog of PABP2 as an arginine methyltransferase 1 (RMT1)-associated protein in fission yeast. The product of the Schizosaccharomyces pombe pab2 gene encodes a nonessential nuclear protein and demonstrates specific poly(A) binding in vitro. Consistent with a functional role in poly(A) tail metabolism, mRNAs from pab2-null cells displayed hyperadenylated 3'-ends. We also show that arginine residues within the C-terminal arginine-rich domain of Pab2 are modified by RMT1-dependent methylation. Whereas the arginine methylated and unmethylated forms of Pab2 behaved similarly in terms of subcellular localization, poly(A) binding, and poly(A) tail length control; Pab2 oligomerization levels were markedly increased when Pab2 was not methylated. Significantly, Pab2 overexpression reduced growth rate, and this growth inhibitory effect was exacerbated in rmt1-null cells. Our results indicate that the main cellular function of Pab2 is in poly(A) tail length control and support a biological role for arginine methylation in the regulation of Pab2 oligomerization.","authors":"Perreault A, Lemieux C, Bachand F","authors_abbrev":"Perreault A et al.","pubmed_publication_date":"09 Mar 2007","pubmed_entrez_date":"2007-01-11","publication_year":"2007","canto_session_key":"b83f0d4242c0daee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-19 15:36:12","canto_approved_date":"2022-01-18 15:35:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-19 15:36:06","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC890.07c","SPBC8D2.10c","SPBC16H5.11c","SPBC20F10.01","SPBC16E9.12c","SPBC18H10.12c","SPBC530.06c","SPAC140.02","SPBC582.05c","SPBC16C6.11","SPCC5E4.06"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2017-07-19"},{"uniquename":"PMID:19273088","title":"AMPK/SNF1 structure: a menage a trois of energy-sensing.","citation":"Front Biosci (Landmark Ed) 2009 Jan 01;14(2):596-610","abstract":"The AMP-activated protein kinase (AMPK) is the critical component of a highly conserved signalling pathway found in all eukaryotes that plays a key role in regulating metabolic processes in response to variations in energy supply and demand. AMPK protects cells from stresses that decrease cellular energy charge (i.e increase the AMP:ATP ratio) by initiating a shift in metabolism towards the generation of ATP while simultaneously down regulating pathways that consume ATP. The role of AMPK as an energy sensor extends beyond the cell and it is now apparent that it is a key regulator of whole-body energy homeostasis. These functions have stimulated considerable interest in AMPK as a promising target to treat metabolic disorders such as obesity and Type 2 diabetes. Recently, crystal structures of heterotrimeric core fragments and individual domains of AMPK from mammals, Schizosaccharomyces pombe and Saccharomyces cerevisiae have been solved. Together they provide an impressive insight into the molecular interactions involved in regulating kinase activity, heterotrimeric assembly, glycogen binding, and binding of the regulatory nucleotides AMP and ATP.","authors":"Scott JW, Oakhill JS, van Denderen BJ","authors_abbrev":"Scott JW et al.","pubmed_publication_date":"01 Jan 2009","pubmed_entrez_date":"2009-03-11","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7548845","title":"Cyclins of the fission yeast Schizosaccharomyces pombe.","citation":"Semin Cell Biol 1995 Apr;6(2):73-8","abstract":"Five cyclin-like genes, cig1, cig2/cyc17, mcs2, puc1 and cdc13, have been discovered in S. pombe to date. It is not yet clear what their functions are or even whether they are all involved with control of the cell cycle. Conflicting data for cig1 and cig2/cyc17 have obscured analysis of their function and cig1 remains largely uncharacterized, although clues to the role of cig2/cyc17 have emerged. There is genetic data available for the more distant cyclin homologue mcs2, which has an essential although as yet unspecified role. Puc1 may be involved in regulation of exit from the cell cycle. The first cyclin to be discovered, and the best understood, is cdc13 which with cdc2 promotes mitosis. Studies of the roles of cdc2 and cdc13 in the overall ordering of the cell cycle suggest that cdc13 and probably other cyclins are key regulators, maintaining the order of S phase and mitosis during the cell cycle.","authors":"Fisher D, Nurse P","authors_abbrev":"Fisher D et al.","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15949817","title":"A logical circuit for the regulation of fission yeast growth modes.","citation":"J Theor Biol 2005 Nov 21;237(2):210-8","abstract":"Growth of fission yeast at the ends of its cylindrical cells switches from a monopolar to a bipolar mode, before it ceases during mitosis and cell division. Here we assume that these growth modes correspond to three stable states of an underlying regulatory circuit, which is a relatively simple and to a large degree autonomous subsystem of an otherwise complex cellular control system. We develop a switch-like logical circuit based on three elements defined as binary variables. Effects of circuit variables on each other are expressed in terms of logical operations. We analyse this circuit for its behavior (\"phenotypes\") after removing single or multiple operations (\"mutants\"). Known fission yeast polarity mutants such as those defective in the switch to bipolar growth can be classified based on these predicted 'phenotypes'. Differences in growth patterns between daughter cells in different bipolar growth mutants are also predicted by the circuit model. The model presented here should provide a useful framework to guide future experiments into mechanisms of cellular polarity. This paper illustrates the usefulness of simple logical circuits to describe and dissect features of complex regulatory processes such as the fission yeast growth patterns in both wild type and mutant cells.","authors":"Bähler J, Svetina S","authors_abbrev":"Bähler J et al.","pubmed_publication_date":"21 Nov 2005","pubmed_entrez_date":"2005-06-14","publication_year":"2005","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32065211","title":"A computational platform to identify origins of replication sites in eukaryotes.","citation":"Brief Bioinform 2021 Mar 22;22(2):1940-1950","abstract":"The locations of the initiation of genomic DNA replication are defined as origins of replication sites (ORIs), which regulate the onset of DNA replication and play significant roles in the DNA replication process. The study of ORIs is essential for understanding the cell-division cycle and gene expression regulation. Accurate identification of ORIs will provide important clues for DNA replication research and drug development by developing computational methods. In this paper, the first integrated predictor named iORI-Euk was built to identify ORIs in multiple eukaryotes and multiple cell types. In the predictor, seven eukaryotic (Homo sapiens, Mus musculus, Drosophila melanogaster, Arabidopsis thaliana, Pichia pastoris, Schizosaccharomyces pombe and Kluyveromyces lactis) ORI data was collected from public database to construct benchmark datasets. Subsequently, three feature extraction strategies which are k-mer, binary encoding and combination of k-mer and binary were used to formulate DNA sequence samples. We also compared the different classification algorithms' performance. As a result, the best results were obtained by using support vector machine in 5-fold cross-validation test and independent dataset test. Based on the optimal model, an online web server called iORI-Euk (http://lin-group.cn/server/iORI-Euk/) was established for the novel ORI identification.","doi":"10.1093/bib/bbaa017","authors":"Dao FY, Lv H, Zulfiqar H, Yang H, Su W, Gao H, Ding H, Lin H","authors_abbrev":"Dao FY et al.","pubmed_publication_date":"22 Mar 2021","pubmed_entrez_date":"2020-02-18","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12637524","title":"Zinc finger protein Prz1 regulates Ca2+ but not Cl- homeostasis in fission yeast. Identification of distinct branches of calcineurin signaling pathway in fission yeast.","citation":"J Biol Chem 2003 May 16;278(20):18078-84","abstract":"Calcineurin is an important mediator that connects the Ca(2+)-dependent signaling to various cellular responses in a wide variety of cell types and organisms. In budding yeast, activated calcineurin exerts its function mainly by regulating the Crz1p/Tcn1 transcription factor. Here, we cloned the fission yeast prz1(+) gene, which encodes a zinc finger transcription factor highly homologous to Crz1/Tcn1. Similar to the results in budding yeast, calcineurin dephosphorylated Prz1 and resulted in the trans-location of Prz1 from the cytoplasm to the nucleus. Prz1 expression was stimulated by high extracellular Ca(2+) in a calcineurin-dependent fashion. However, unlike in budding yeast, the prz1-null cells did not show any phenotype similar to those previously reported in calcineurin deletion such as aberrant cell morphology, mating defect, or hypersensitivity to Cl(-). Instead, the prz1-null cells showed hypersensitivity to Ca(2+), consistent with a dramatic decrease in transcription of Pmc1 Ca(2+) pump. Interestingly, overexpression of Prz1 did not suppress the Cl(-) hypersensitivity of calcineurin deletion, and overexpression of Pmp1 MAPK phosphatase suppressed the Cl(-) hypersensitivity of calcineurin deletion but not the Ca(2+) hypersensitivity of prz1 deletion. In addition, mutations in the its2(+)/cps1(+), its8(+), and its10(+)/cdc7(+) genes that showed synthetic lethal genetic interaction with calcineurin deletion did not exhibit synthetic lethality with the prz1 deletion. Our results suggest that calcineurin activates at least two distinct signaling branches, i.e. the Prz1-dependent transcriptional regulation and an unknown mechanism, which functions antagonistically with the Pmk1 MAPK pathway.","authors":"Hirayama S, Sugiura R, Lu Y, Maeda T, Kawagishi K, Yokoyama M, Tohda H, Giga-Hama Y, Shuntoh H, Kuno T","authors_abbrev":"Hirayama S et al.","pubmed_publication_date":"16 May 2003","pubmed_entrez_date":"2003-03-15","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPBC21.06c","SPAC4G8.13c","SPBC1685.01","SPBC839.08c","SPAC19G12.14","SPBC19G7.05c","SPAC18G6.03"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:11788722","title":"Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination.","citation":"Nucleic Acids Res 2002 Jan 15;30(2):581-91","abstract":"A functional homolog (rhp23) of human HHR23A and Saccharomyces cerevisiae RAD23 was cloned from the fission yeast Schizosaccharomyces pombe and characterized. Consistent with the role of Rad23 homologs in nucleotide excision repair, rhp23 mutant cells are moderately sensitive to UV light but demonstrate wild-type resistance to gamma-rays and hydroxyurea. Expression of the rhp23, RAD23 or HHR23A cDNA restores UV resistance to the mutant, indicating that rhp23 is a functional homolog of the human and S.cerevisiae genes. The rhp23::ura4 mutation also causes a delay in the G2 phase of the cell cycle which is corrected when rhp23, RAD23 or HHR23A cDNA is expressed. Rhp23 is present throughout the cell but is located predominantly in the nucleus, and the nuclear levels of Rhp23 decrease around the time of S phase in the cell cycle. Rhp23 is ubiquitinated at low levels, but overexpression of the rhp23 cDNA induces a large increase in ubiquitination of other proteins. Consistent with a role in protein ubiquitination, Rhp23 binds ubiquitin, as determined by two-hybrid analysis. Thus, the rhp23 gene plays a role not only in nucleotide excision repair but also in cell cycle regulation and the ubiquitination pathways.","authors":"Elder RT, Song XQ, Chen M, Hopkins KM, Lieberman HB, Zhao Y","authors_abbrev":"Elder RT et al.","pubmed_publication_date":"15 Jan 2002","pubmed_entrez_date":"2002-01-15","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.16","SPAC6G10.11c","SPBC2D10.12","SPAC11G7.04","SPAC1805.12c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:4708672","title":"Regulation of the biosynthesis of purine nucleotides in Schizosaccharomyces pombe. 3. Kinetic studies of adenylosuccinate synthetase.","citation":"Biochim Biophys Acta 1973 May 05;309(1):1-10","abstract":"","authors":"Nagy M, Djembo-Taty M, Heslot","authors_abbrev":"Nagy M et al.","pubmed_publication_date":"05 May 1973","pubmed_entrez_date":"1973-05-05","publication_year":"1973","canto_session_key":"033d6975c01e682b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-04-25 10:16:28","canto_approved_date":"2020-01-17 19:30:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-24 10:50:04","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC144.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-25"},{"uniquename":"PMID:16951255","title":"S. pombe CLASP needs dynein, not EB1 or CLIP170, to induce microtubule instability and slows polymerization rates at cell tips in a dynein-dependent manner.","citation":"Genes Dev 2006 Sep 01;20(17):2421-36","abstract":"The Schizosaccharomyces pombe CLIP170-associated protein (CLASP) Peg1 was identified in a screen for mutants with spindle formation defects and a screen for molecules that antagonized EB1 function. The conditional peg1.1 mutant enabled us to identify key features of Peg1 function. First, Peg1 was required to form a spindle and astral microtubules, yet destabilized interphase microtubules. Second, Peg1 was required to slow the polymerization rate of interphase microtubules that establish end-on contact with the cortex at cell tips. Third, Peg1 antagonized the action of S. pombe CLIP170 (Tip1) and EB1 (Mal3). Fourth, although Peg1 resembled higher eukaryotic CLASPs by physically associating with both Mal3 and Tip1, neither Tip1 nor Mal3 was required for Peg1 to destabilize interphase microtubules or for it to associate with microtubules. Conversely, neither Mal3 nor Tip1 required Peg1 to associate with microtubules or cell tips. Consistently, while mal3.Delta and tip1.Delta disrupted linear growth, corrupting peg1 (+) did not. Fifth, peg1.1 phenotypes resembled those arising from deletion of the single heavy or both light chains of fission yeast dynein. Furthermore, all interphase phenotypes arising from peg1 (+) manipulation relied on dynein function. Thus, the impact of S. pombe CLASP on interphase microtubule behavior is more closely aligned to dynein than EB1 or CLIP170.","authors":"Grallert A, Beuter C, Craven RA, Bagley S, Wilks D, Fleig U, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"01 Sep 2006","pubmed_entrez_date":"2006-09-05","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPAC3C7.12","SPAC1093.06c","SPAC3G9.12","SPCC1223.06"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:12018860","title":"The 5'-flanking AT-rich sequence of thioredoxin gene involved in high-frequency transformation of the fission yeast.","citation":"Mol Cells 2002 Apr 30;13(2):347-50","abstract":"During the cloning of a genomic DNA encoding mitochondrial thioredoxin (TRX) from the fission yeast Schizosaccharomyces pombe, its 5' flanking sequence was involved in the high-frequency of transformation. The recombinant plasmid pYEX that was constructed in the 2 mu plasmid-derived vector pYES2 gave rise to a significant high-frequency of transformation in S. pombe, compared to the vector alone. Plasmid pYEX contains 1,090 bp 5'-flanking sequences of the TRX gene that are ahead of the open-reading frame. Similar 5'-flanking sequences, which were inserted in the lacZ fusion vector YEp357R that contained the 2 mu origin of replication, also gave a high-frequency of transformation. Dissection of the 5'-flanking sequence of the TRX gene by the HindIII restriction site showed that the 782 bp flanking sequence (5' upstream of the HindIII site) was responsible for the high-frequency of transformation by the 2 mu plasmid-derived vector DNAs. The putative sequence that is involved in the high-frequency of transformation contains a very high ratio of A-T pairs. No known functions were assigned on the sequence, which was estimated from the GenBank database.","authors":"Lee YJ, Kim D, Park EH, Lim CJ","authors_abbrev":"Lee YJ et al.","pubmed_publication_date":"30 Apr 2002","pubmed_entrez_date":"2002-05-23","publication_year":"2002","canto_session_key":"83db51f7f2d505e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-01-07 13:19:38","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-07 13:19:27","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-01-07"},{"uniquename":"PMID:33440639","title":"Fission Yeast Methylenetetrahydrofolate Reductase Ensures Mitotic and Meiotic Chromosome Segregation Fidelity.","citation":"Int J Mol Sci 2021 Jan 11;22(2)","abstract":"Methylenetetrahydrofolate reductase (MTHFR) is a key enzyme in the folate metabolic pathway, and its loss of function through polymorphisms is often associated with human conditions, including cancer, congenital heart disease, and Down syndrome. MTHFR is also required in the maintenance of heterochromatin, a crucial determinant of genomic stability and precise chromosomal segregation. Here, we characterize the function of a fission yeast gene  met11 +  , which encodes a protein that is highly homologous to the mammalian MTHFR. We show that, although  met11 +   is not essential for viability, its disruption increases chromosome missegregation and destabilizes constitutive heterochromatic regions at pericentromeric, sub-telomeric and ribosomal DNA (rDNA) loci. Transcriptional silencing at these sites were disrupted, which is accompanied by the reduction in enrichment of histone H3 lysine 9 dimethylation (H3K9me2) and binding of the heterochromatin protein 1 (HP1)-like Swi6. The  met11  null mutant also dominantly disrupts meiotic fidelity, as displayed by reduced sporulation efficiency and defects in proper partitioning of the genetic material during meiosis. Interestingly, the faithful execution of these meiotic processes is synergistically ensured by cooperation among Met11, Rec8, a meiosis-specific cohesin protein, and the shugoshin protein Sgo1, which protects Rec8 from untimely cleavage. Overall, our results suggest a key role for Met11 in maintaining pericentromeric heterochromatin for precise genetic inheritance during mitosis and meiosis.","doi":"10.3390/ijms22020639","authors":"Lim KK, Teo HY, Tan YY, Zeng YB, Lam UTF, Choolani M, Chen ES","authors_abbrev":"Lim KK et al.","pubmed_publication_date":"11 Jan 2021","pubmed_entrez_date":"2021-01-14","publication_year":"2021","canto_session_key":"b59167f5948e00d7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-01-16 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30397105","title":"The multitasking polyA tail: nuclear RNA maturation, degradation and export.","citation":"Philos Trans R Soc Lond B Biol Sci 2018 Nov 05;373(1762)","abstract":"A polyA (pA) tail is an essential modification added to the 3' ends of a wide range of RNAs at different stages of their metabolism. Here, we describe the main sources of polyadenylation and outline their underlying biochemical interactions within the nuclei of budding yeast  Saccharomyces cerevisiae , human cells and, when relevant, the fission yeast  Schizosaccharomyces pombe  Polyadenylation mediated by the  S. cerevisiae  Trf4/5 enzymes, and their human homologues PAPD5/7, typically leads to the 3'-end trimming or complete decay of non-coding RNAs. By contrast, the primary function of canonical pA polymerases (PAPs) is to produce stable and nuclear export-competent mRNAs. However, this dichotomy is becoming increasingly blurred, at least in  S. pombe  and human cells, where polyadenylation mediated by canonical PAPs may also result in transcript decay.This article is part of the theme issue '5' and 3' modifications controlling RNA degradation'.","doi":"10.1098/rstb.2018.0169","authors":"Tudek A, Lloret-Llinares M, Jensen TH","authors_abbrev":"Tudek A et al.","pubmed_publication_date":"05 Nov 2018","pubmed_entrez_date":"2018-11-07","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-08 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11579556","title":"[Diversity of DNA recognition by transcription factors].","citation":"Tanpakushitsu Kakusan Koso 2001 Aug;46(11 Suppl):1602-7","abstract":"","authors":"Shimizu T, Hakoshima T","authors_abbrev":"Shimizu T et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-10-03","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8565064","title":"How fission yeast fission in the middle.","citation":"Cell 1996 Jan 26;84(2):191-4","abstract":"In fission yeast, we propose that the division plane may be positioned by the position of the premitotic nucleus, perhaps by a signal emanating from the nucleus. Gene products involved in the assembly of the ring and its temporal and spatial controls are beginning to be characterized. Some of these, such as mid1p, may be involved in signals that position the division site. In animal cells, the division site may be determined by analogous signals emanating from the mitotic asters (Rappaport, 1986). We speculate that the signals defined in fission yeast will help identify signals that determine the division plane in all kinds of eukaryotes.","authors":"Chang F, Nurse P","authors_abbrev":"Chang F et al.","pubmed_publication_date":"26 Jan 1996","pubmed_entrez_date":"1996-01-26","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17509158","title":"Meiosis specific coiled-coil proteins in Shizosaccharomyces pombe.","citation":"Cell Div 2007 May 18;2:14","abstract":"Many meiosis-specific proteins in Schizosaccharomyces pombe contain coiled-coil motifs which play essential roles for meiotic progression. For example, the coiled-coil motifs present in Meu13 and Mcp7 are required for their function as a putative recombinase cofactor complex during meiotic recombination. Mcp6/Hrs1 and Mcp5/Num1 control horsetail chromosome movement by astral microtubule organization and anchoring dynein respectively. Dhc1 and Ssm4 are also required for horsetail chromosome movement. It is clear from these examples that the coiled-coil motif in these proteins plays an important role during the progression of cells through meiosis. However, there are still many unanswered questions on how these proteins operate. In this paper, we briefly review recent studies on the meiotic coiled-coil proteins in Sz. pombe.","authors":"Ohtaka A, Saito TT, Okuzaki D, Nojima H","authors_abbrev":"Ohtaka A et al.","pubmed_publication_date":"18 May 2007","pubmed_entrez_date":"2007-05-19","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22121899","title":"Genome-wide mapping of histone modifications and mass spectrometry reveal H4 acetylation bias and H3K36 methylation at gene promoters in fission yeast.","citation":"Epigenomics 2010 Jun;2(3):377-93","abstract":"To map histone modifications with unprecedented resolution both globally and locus-specifically, and to link modification patterns to gene expression.\nUsing correlations between quantitative mass spectrometry and chromatin immunoprecipitation/microarray analyses, we have mapped histone post-translational modifications in fission yeast (Schizosaccharomyces pombe).\nAcetylations at lysine 9, 18 and 27 of histone H3 give the best positive correlations with gene expression in this organism. Using clustering analysis and gene ontology search tools, we identified promoter histone modification patterns that characterize several classes of gene function. For example, gene promoters of genes involved in cytokinesis have high H3K36me2 and low H3K4me2, whereas the converse pattern is found ar promoters of gene involved in positive regulation of the cell cycle. We detected acetylation of H4 preferentially at lysine 16 followed by lysine 12, 8 and 5. Our analysis shows that this H4 acetylation bias in the coding regions is dependent upon gene length and linked to gene expression. Our analysis also reveals a role for H3K36 methylation at gene promoters where it functions in a crosstalk between the histone methyltransferase Set2(KMT3) and the histone deacetylase Clr6, which removes H3K27ac leading to repression of transcription.\nHistone modification patterns could be linked to gene expression in fission yeast.","doi":"10.2217/epi.10.18","authors":"Sinha I, Buchanan L, Rönnerblad M, Bonilla C, Durand-Dubief M, Shevchenko A, Grunstein M, Stewart AF, Ekwall K","authors_abbrev":"Sinha I et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2011-11-30","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7828877","title":"The Schizosaccharomyces pombe pka1 gene, encoding a homolog of cAMP-dependent protein kinase.","citation":"Gene 1994 Dec 30;151(1-2):215-20","abstract":"We have isolated 16 independent Schizosaccharomyces pombe cDNA clones that suppress the temperature-sensitive (ts) phenotype of a Saccharomyces cerevisiae strain containing the dominant-negative RAS2val19ala22 allele. Fourteen of these cDNAs encode Sz. pombe Ras1. The other two clones encode the C-terminal region of a protein we have named Pka1. We have cloned the pka1 gene from a Sz. pombe genomic library. It contains an uninterrupted open reading frame encoding a 512-amino-acid (aa) protein. The C-terminal region (aa 200-512) of Pka1 is 51-63% identical to cAMP-dependent protein kinase (Pka) catalytic subunits from other eukaryotes. Production of Pka1 suppresses the ts phenotypes exhibited by Sa. cerevisiae ras1-ras2ts or cyr1ts strains. Furthermore, overproduction of Pka1 in Sz. pombe results in a sterile phenotype and an abnormal morphology similar to that exhibited by cells in which the cAMP pathway is constitutively activated. These observations suggest that pka1 encodes the Sz. pombe Pka catalytic subunit.","authors":"Yu G, Li J, Young D","authors_abbrev":"Yu G et al.","pubmed_publication_date":"30 Dec 1994","pubmed_entrez_date":"1994-12-30","publication_year":"1994","canto_session_key":"3e77900660eb91a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-05-02 16:15:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-02 16:14:24","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-02"},{"uniquename":"PMID:7592316","title":"Papulacandin B resistance in budding and fission yeasts: isolation and characterization of a gene involved in (1,3)beta-D-glucan synthesis in Saccharomyces cerevisiae.","citation":"J Bacteriol 1995 Oct;177(20):5732-9","abstract":"Papulacandin B, an antifungal agent that interferes with the synthesis of yeast cell wall (1,3)beta-D-glucan, was used to isolate resistant mutants in Schizosaccharomyces pombe and Saccharomyces cerevisiae. The resistance to papulacandin B always segregated as a recessive character that defines a single complementation group in both yeasts (pbr1+ and PBR1, respectively). Determination of several kinetic parameters of (1,3)beta-D-glucan synthase activity revealed no differences between S. pombe wild-type and pbr1 mutant strains except in the 50% inhibitory concentration for papulacandin B of the synthases (about a 50-fold increase in mutant activity). Inactivation of the synthase activity of both yeasts after in vivo treatment with the antifungal agent showed that mutant synthases were more resistant than the corresponding wild-type ones. Detergent dissociation of the S. pombe synthase into soluble and particulate fractions and subsequent reconstitution indicated that the resistance character of pbr1 mutants resides in the particulate fraction of the enzyme. Cloning and sequencing of PBR1 from S. cerevisiae revealed a gene identical to others recently reported (FKS1, ETG1, CWH53, and CND1). Its disruption leads to reduced levels of both (1,3)beta-D-glucan synthase activity and the alkali-insoluble cell wall fraction. Transformants containing the PBR1 gene reverse the defect in (1,3)beta-D-glucan synthase. It is concluded that Pbr1p is probably part of the (1,3)beta-D-glucan synthase complex.","authors":"Castro C, Ribas JC, Valdivieso MH, Varona R, del Rey F, Duran A","authors_abbrev":"Castro C et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_session_key":"0490db63e6b533b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-24 18:38:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 13:59:56","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-08"},{"uniquename":"PMID:10721711","title":"Fission yeast contains an rDNA binding activity that interacts specifically with regulatory sequences for ribosomal RNA synthesis.","citation":"Gene 2000 Jan 25;242(1-2):183-92","abstract":"Basal level transcriptional initiation of fission yeast ribosomal RNA genes is dependent on the core ribosomal RNA gene promoter and is stimulated by an upstream rDNA promoter element and by regulatory sequences located in its approximately 3.5 kb intergenic rDNA spacer. A Schizosaccharomyces pombe sequence-specific rDNA binding activity was characterized that interacted with the upstream rDNA promoter region and that associated with required RNA polymerase I transcription components in initial fractionation steps. The rDNA binding activity was further purified and found to specifically associate with a region of the rDNA promoter between -80 and -56. The promoter region required for stable binding correlates with that mediating activated levels of transcriptional initiation. This rDNA binding activity stimulates in vitro rRNA synthesis supported by templates bearing this upstream promoter domain but not by templates lacking it.","authors":"Guo A, Chen L, Zhao A, Boukghalter B, Pape L","authors_abbrev":"Guo A et al.","pubmed_publication_date":"25 Jan 2000","pubmed_entrez_date":"2000-03-18","publication_year":"2000","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27856494","title":"The dynamic landscape of fission yeast meiosis alternative-splice isoforms.","citation":"Genome Res 2017 Jan;27(1):145-156","abstract":"Alternative splicing increases the diversity of transcriptomes and proteomes in metazoans. The extent to which alternative splicing is active and functional in unicellular organisms is less understood. Here, we exploit a single-molecule long-read sequencing technique and develop an open-source software program called SpliceHunter to characterize the transcriptome in the meiosis of fission yeast. We reveal 14,353 alternative splicing events in 17,669 novel isoforms at different stages of meiosis, including antisense and read-through transcripts. Intron retention is the major type of alternative splicing, followed by alternate \"intron in exon.\" Seven hundred seventy novel transcription units are detected; 53 of the predicted proteins show homology in other species and form theoretical stable structures. We report the complexity of alternative splicing along isoforms, including 683 intra-molecularly co-associated intron pairs. We compare the dynamics of novel isoforms based on the number of supporting full-length reads with those of annotated isoforms and explore the translational capacity and quality of novel isoforms. The evaluation of these factors indicates that the majority of novel isoforms are unlikely to be both condition-specific and translatable but consistent with the possibility of biologically functional novel isoforms. Moreover, the co-option of these unusual transcripts into newly born genes seems likely. Together, the results of this study highlight the diversity and dynamics at the isoform level in the sexual development of fission yeast.","doi":"10.1101/gr.208041.116","authors":"Kuang Z, Boeke JD, Canzar S","authors_abbrev":"Kuang Z et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2016-11-19","publication_year":"2017","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2016-11-21 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22377633","title":"Remarkably high rate of DNA amplification promoted by the mating-type switching mechanism in Schizosaccharomyces pombe.","citation":"Genetics 2012 May;191(1):285-9","abstract":"A novel mating-type switching-defective mutant showed a highly unstable rearrangement at the mating-type locus (mat1) in fission yeast. The mutation resulted from local amplification of a 134-bp DNA fragment by the mat1-switching phenomenon. We speculate that the rolling-circle-like replication and homologous recombination might be the general mechanisms for local genome region expansion.","doi":"10.1534/genetics.112.138727","authors":"Yu C, Bonaduce MJ, Klar AJ","authors_abbrev":"Yu C et al.","pubmed_publication_date":"May 2012","pubmed_entrez_date":"2012-03-02","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB009602","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39328910","title":"The  Schizosaccharomyces pombe  ornithine-N 5 -oxygenase Sib2 interacts with the N 5 -transacetylase Sib3 in the ferrichrome biosynthetic pathway.","citation":"Front Microbiol 2024;15:1467397","abstract":"The fission yeast  Schizosaccharomyces pombe  produces the hydroxamate-type siderophore ferrichrome (Fc). The biosynthesis of Fc requires the Fc synthase Sib1, the ornithine-N 5 -oxygenase Sib2, and the N 5 -hydroxyornithine-N 5 -transacetylase Sib3. In this study, we demonstrate the critical importance of the His 248  residue of Sib3 in Fc production. Cells expressing a  sib3H248A  mutant allele fail to grow in iron-poor media without Fc supplementation. These  sib3H248A  mutant cells are consistently unable to promote Fc-dependent growth of  Saccharomyces cerevisiae  cells in cross-feeding experiments. Green fluorescent protein (GFP)-tagged wild-type Sib3 and mutant Sib3H248A exhibit a pancellular distribution. Coimmunoprecipitation assays revealed that both wild-type and Sib3H248A physically interact with Sib2. Further analysis identified a minimal C-terminal region from amino acids 290-334 of Sib3 that is required for interaction with Sib2. Deletion mapping analysis identified two regions of Sib2 as being required for its association with Sib3. The first region encompasses amino acids 1-135, and the second region corresponds to amino acids 281-358 of Sib2. Taken together, these results describe the first example of a physical interaction between an ornithine-N 5 -oxygenase and an N 5 -hydroxyornithine-N 5 -transacetylase controlling the biosynthesis of a hydroxamate-type siderophore.","doi":"10.3389/fmicb.2024.1467397","authors":"Mbuya B, Plante S, Ammar F, Brault A, Labbé S","authors_abbrev":"Mbuya B et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-09-27","publication_year":"2024","canto_session_key":"ba2392f1eaae0e18","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-09-27 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10829083","title":"Analysis of telomerase catalytic subunit mutants in vivo and in vitro in Schizosaccharomycespombe.","citation":"Proc Natl Acad Sci U S A 2000 Jun 06;97(12):6367-72","abstract":"The chromosome end-replicating enzyme telomerase is composed of a template-containing RNA subunit, a reverse transcriptase (TERT), and additional proteins. The importance of conserved amino acid residues in Trt1p, the TERT of Schizosaccharomyces pombe, was tested. Mutation to alanine of the proposed catalytic aspartates in reverse transcriptase motifs A and C and of conserved amino acids in motifs 1 and B' resulted in defective growth, progressive loss of telomeric DNA, and loss of detectable telomerase enzymatic activity in vitro. Mutation of the phenylalanine (F) in the conserved FYxTE of telomerase-specific motif T had no phenotype in vivo or in vitro whereas mutation of a conserved amino acid in RT motif 2 had an intermediate effect. In addition to identifying single amino acids of TERT required for telomere maintenance in the fission yeast, this work provides useful tools for S. pombe telomerase research: a functional epitope-tagged version of Trt1p that allows detection of the protein even in crude cellular extracts, and a convenient and robust in vitro enzymatic activity assay based on immunopurification of telomerase.","authors":"Haering CH, Nakamura TM, Baumann P, Cech TR","authors_abbrev":"Haering CH et al.","pubmed_publication_date":"06 Jun 2000","pubmed_entrez_date":"2000-06-01","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12783882","title":"Rpn5 is a conserved proteasome subunit and required for proper proteasome localization and assembly.","citation":"J Biol Chem 2003 Aug 15;278(33):30669-76","abstract":"Proper function of the 26 S proteasome requires assembly of the regulatory complex, which is composed of the lid and base subcomplexes. We characterized Rpn5, a lid subunit, in fission yeast. We show that Rpn5 associates with the proteasome rpn5. Deletion (rpn5Delta) exacerbates the growth defects in proteasome mutants, leading to mitotic abnormalities, which correlate with accumulation of polyubiquitinated proteins, such as Cut2/securin. Rpn5 expression is tightly controlled; both overexpression and deletion of rpn5 impair proteasome functions. The proteasome is assembled around the inner nuclear membrane in wild-type cells; however, in rpn5Delta cells, proteasome subunits are improperly assembled and/or localized. In the lid mutants, Rpn5 is mislocalized in the cytosol, while in the base mutants, Rpn5 can enter the nucleus, but is left in the nucleoplasm, and not assembled into the nuclear membrane. These results suggest that Rpn5 is a dosage-dependent proteasome regulator and plays a role in mediating proper proteasome assembly. Moreover, the Rpn5 assembly may be a cooperative process that involves at least two steps: 1) nuclear import and 2) subsequent assembly into the nuclear membrane. The former step requires other components of the lid, while the latter requires the base. Human Rpn5 rescues the phenotypes associated with rpn5Delta and is incorporated into the yeast proteasome, suggesting that Rpn5 functions are highly conserved.","authors":"Yen HC, Espiritu C, Chang EC","authors_abbrev":"Yen HC et al.","pubmed_publication_date":"15 Aug 2003","pubmed_entrez_date":"2003-06-05","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC607.05","SPBP19A11.03c","SPAC1420.03","SPAPB8E5.02c","SPBC4.07c","SPAC637.10c","SPBC16G5.01","SPBC16C6.07c","SPAC31G5.13"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:10036243","title":"Regulation of the start of DNA replication in Schizosaccharomyces pombe.","citation":"J Cell Sci 1999 Mar;112 ( Pt 6):939-46","abstract":"Cells of Schizosaccharomyces pombe were grown in minimal medium with different nitrogen sources under steady-state conditions, with doubling times ranging from 2.5 to 14 hours. Flow cytometry and fluorescence microscopy confirmed earlier findings that at rapid growth rates, the G1 phase was short and cell separation occurred at the end of S phase. For some nitrogen sources, the growth rate was greatly decreased, the G1 phase occupied 30-50% of the cell cycle, and cell separation occurred in early G1. In contrast, other nitrogen sources supported low growth rates without any significant increase in G1 duration. The method described allows manipulation of the length of G1 and the relative cell cycle position of S phase in wild-type cells. Cell mass was measured by flow cytometry as scattered light and as protein-associated fluorescence. The extensions of G1 were not related to cell mass at entry into S phase. Our data do not support the hypothesis that the cells must reach a certain fixed, critical mass before entry into S. We suggest that cell mass at the G1/S transition point is variable and determined by a set of molecular parameters. In the present experiments, these parameters were influenced by the different nitrogen sources in a way that was independent of the actual growth rate.","authors":"Carlson CR, Grallert B, Stokke T, Boye E","authors_abbrev":"Carlson CR et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-02-26","publication_year":"1999","canto_session_key":"0fb69ef0f10965a2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-01 08:05:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-01 08:05:08","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-01"},{"uniquename":"PMID:38442274","title":"Set2 regulates Ccp1 and Swc2 to ensure centromeric stability by retargeting CENP-A.","citation":"Nucleic Acids Res 2024 Mar 05;","abstract":"Precise positioning of the histone-H3 variant, CENP-A, ensures centromere stability and faithful chromosomal segregation. Mislocalization of CENP-A to extra-centromeric loci results in aneuploidy and compromised cell viability associated with formation of ectopic kinetochores. The mechanism that retargets mislocalized CENP-A back to the centromere is unclarified. We show here that the downregulation of the histone H3 lysine 36 (H3K36) methyltransferase Set2 can preserve centromere localization of a temperature-sensitive mutant cnp1-1 Schizosaccharomyces pombe CENP-A (SpCENP-A) protein and reverse aneuploidy by redirecting mislocalized SpCENP-A back to centromere from ribosomal DNA (rDNA) loci, which serves as a sink for the delocalized SpCENP-A. Downregulation of set2 augments Swc2 (SWR1 complex DNA-binding module) expression and releases histone chaperone Ccp1 from the centromeric reservoir. Swc2 and Ccp1 are directed to the rDNA locus to excavate the SpCENP-Acnp1-1, which is relocalized to the centromere in a manner dependent on canonical SpCENP-A loaders, including Mis16, Mis17 and Mis18, thereby conferring cell survival and safeguarding chromosome segregation fidelity. Chromosome missegregation is a severe genetic instability event that compromises cell viability. This mechanism thus promotes CENP-A presence at the centromere to maintain genomic stability.","doi":"10.1093/nar/gkae084","authors":"Lim KK, Lam UTF, Li Y, Zeng YB, Yang H, Chen ES","authors_abbrev":"Lim KK et al.","pubmed_publication_date":"05 Mar 2024","pubmed_entrez_date":"2024-03-05","publication_year":"2024","canto_session_key":"6d2dcc154c6b21ed","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-06 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16141239","title":"Endocytosis in fission yeast is spatially associated with the actin cytoskeleton during polarised cell growth and cytokinesis.","citation":"J Cell Sci 2005 Sep 15;118(Pt 18):4231-42","abstract":"In the fission yeast, Schizosaccharomyces pombe, uptake of the fluorescent styryl dye FM4-64 via the endocytic pathway to the vacuole was localised to the poles of growing, interphase cells and to the cell equator during cell division, regions of cell wall deposition that are rich in actin. When the pattern of growth or the plane of cytokinesis was altered, the relationship between the actin cytoskeleton and the site of endocytosis was maintained. Transfer of the label to the vacuolar membrane was dependent upon the Rab GTPase Ypt7 and, hence, vesicle fusion. Endocytic vesicles transiently colocalised with actin patches and endocytosis was inhibited in mutants that affected actin patch integrity and by the actin inhibitor latrunculin A. Concentrations of latrunculin that removed actin cables but left patches unaffected had no effect on endocytosis at the poles, but abolished endocytosis at the cell equator. Equatorial, but not polar, endocytosis was also inhibited in cells lacking the formin For3 (which have selectively destabilised actin cables), in mutants of the exocyst complex and in cells treated with brefeldin A. Differential effects on endocytosis at the cell poles and equator were also observed in the actin mutant cps8 and the Arp2/3 complex mutant arp2. The redirection of endocytosis from the cell poles to the cell equator in M phase coincided with the anaphase separation of sister chromatids and was abolished in the septation initiation network (SIN) mutants cdc7, sid1 and sid2, demonstrating that the spatial reorganisation of the endocytic pathway in the S. pombe cell cycle requires a functional SIN pathway. We conclude that endocytosis in fission yeast has two distinct components, both of which are actin-based, but which are mechanistically distinct, as well as being spatially and temporally separated in the S. pombe cell cycle.","authors":"Gachet Y, Hyams JS","authors_abbrev":"Gachet Y et al.","pubmed_publication_date":"15 Sep 2005","pubmed_entrez_date":"2005-09-06","publication_year":"2005","canto_session_key":"08d41b8c55934bfd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-26 16:06:09","canto_approved_date":"2025-12-11 13:26:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-22 16:48:37","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.12c","SPCC970.09","SPAC9G1.09","SPBC32H8.12c","SPCC895.05","SPCC584.05","SPBC1604.20c","SPAC11H11.06","SPBC405.04c","SPAC24B11.11c","SPBC21.06c"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2018-01-26"},{"uniquename":"PMID:16489217","title":"Schizosaccharomyces pombe Git1 is a C2-domain protein required for glucose activation of adenylate cyclase.","citation":"Genetics 2006 May;173(1):49-61","abstract":"Schizosaccharomyces pombe senses environmental glucose through a cAMP-signaling pathway, activating cAMP-dependent protein kinase A (PKA). This requires nine git (glucose insensitive transcription) genes that encode adenylate cyclase, the PKA catalytic subunit, and seven \"upstream\" proteins required for glucose-triggered adenylate cyclase activation, including three heterotrimeric G-protein subunits and its associated receptor. We describe here the cloning and characterization of the git1+ gene. Git1 is distantly related to a small group of uncharacterized fungal proteins, including a second S. pombe protein that is not functionally redundant with Git1, as well as to members of the UNC-13/Munc13 protein family. Mutations in git1+ demonstrate functional roles for the two most highly conserved regions of the protein, the C2 domain and the MHD2 Munc homology domain. Cells lacking Git1 are viable, but display phenotypes associated with cAMP-signaling defects, even in strains expressing a mutationally activated G alpha-subunit, which activates adenylate cyclase. These cells possess reduced basal cAMP levels and fail to mount a cAMP response to glucose. In addition, Git1 and adenylate cyclase physically interact and partially colocalize in the cell. Thus, Git1 is a critical component of the S. pombe glucose/cAMP pathway.","authors":"Kao RS, Morreale E, Wang L, Ivey FD, Hoffman CS","authors_abbrev":"Kao RS et al.","pubmed_publication_date":"May 2006","pubmed_entrez_date":"2006-02-21","publication_year":"2006","canto_session_key":"45ffde2cb6f9e878","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-28 11:28:48","canto_approved_date":"2026-04-08 08:07:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-28 11:28:40","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21C3.20c","SPAC11E3.02c","SPBC19C7.03","SPAC23H3.13c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-09-28"},{"uniquename":"PMID:20559027","title":"Homolog pairing during meiosis: dyneins on the move.","citation":"Cell Cycle 2010 Jun 01;9(11):2060","abstract":"","authors":"Arumugam P","authors_abbrev":"Arumugam P","pubmed_publication_date":"01 Jun 2010","pubmed_entrez_date":"2010-06-19","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21376600","title":"Temporal control of contractile ring assembly by Plo1 regulation of myosin II recruitment by Mid1/anillin.","citation":"Curr Biol 2011 Mar 22;21(6):473-9","abstract":"In eukaryotes, cytokinesis generally involves an actomyosin ring, the contraction of which promotes daughter cell segregation. Assembly of the contractile ring is tightly controlled in space and time. In the fission yeast, contractile ring components are first organized by the anillin-like protein Mid1 into medial cortical nodes. These nodes then coalesce laterally into a functional contractile ring. Although Mid1 is present at the medial cortex throughout G2, recruitment of contractile ring components to nodes starts only at mitotic onset, indicating that this event is cell-cycle regulated. Polo kinases are key temporal coordinators of mitosis and cytokinesis, and the Polo-like kinase Plo1 is known to activate Mid1 nuclear export at mitotic onset, coupling division plane specification to nuclear position. Here we provide evidence that Plo1 also triggers the recruitment of contractile ring components into medial cortical nodes. Plo1 binds at least two independent sites on Mid1, including a consensus site phosphorylated by Cdc2. Plo1 phosphorylates several residues within the first 100 amino acids of Mid1, which directly interact with the IQGAP Rng2, and influences the timing of myosin II recruitment. Plo1 thereby facilitates contractile ring assembly at mitotic onset.","doi":"10.1016/j.cub.2011.02.003","authors":"Almonacid M, Celton-Morizur S, Jakubowski JL, Dingli F, Loew D, Mayeux A, Chen JS, Gould KL, Clifford DM, Paoletti A","authors_abbrev":"Almonacid M et al.","pubmed_publication_date":"22 Mar 2011","pubmed_entrez_date":"2011-03-08","publication_year":"2011","canto_session_key":"adc0f6d0a5166829","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-12 14:59:53","canto_approved_date":"2026-03-31 17:53:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-09 15:03:40","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":42,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.13c","SPCC4B3.15","SPAC23C11.16","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2024-04-12"},{"uniquename":"PMID:29043645","title":"A Chromatin Fiber Analysis Pipeline to Model DNA Synthesis and Structures in Fission Yeast.","citation":"Methods Mol Biol 2018;1672:509-526","abstract":"Chromatin fibers, first described by Jackson and Pombo (J Cell Biol 140(6):1285-1295, 1998) are prepared from cells lysed on glass coverslips, and require minimal equipment to produce. Since the DNA is not previously treated with denaturing agents, proteins are left intact and may be used to model other DNA-based processes. Such an analysis can be daunting, without a rigorous method for analysis. We describe a pipeline for chromatin fiber use to model DNA replication complexes. Full protocols for chromatin fiber preparation and staining are presented. Further, we have developed an analysis algorithm for One Dimensional Data-Boolean Logic Operations Binning System (ODD-BLOBS). This freely available software defines replication and protein tracts, measures their lengths, and then correlates replicated areas with protein distributions. Our methods and analysis are tested in Schizosaccharomyces pombe (fission yeast) but may be applied to model replication structures across multiple organisms.","doi":"10.1007/978-1-4939-7306-4_34","authors":"Sabatinos SA, Green MD","authors_abbrev":"Sabatinos SA et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2017-10-19","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-10-20 00:15:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27890612","title":"In vitro reconstitution and biochemical analyses of the Schizosaccharomyces pombe nucleosome.","citation":"Biochem Biophys Res Commun 2017 Jan 22;482(4):896-901","abstract":"Schizosaccharomyces pombe, which has a small genome but shares many physiological functions with higher eukaryotes, is a useful single-cell, model eukaryotic organism. In particular, many features concerning chromatin structure and dynamics, including heterochromatin, centromeres, telomeres, and DNA replication origins, are well conserved between S. pombe and higher eukaryotes. However, the S. pombe nucleosome, the fundamental structural unit of chromatin, has not been reconstituted in vitro. In the present study, we established the method to purify S. pombe histones H2A, H2B, H3, and H4, and successfully reconstituted the S. pombe nucleosome in vitro. Our thermal stability assay and micrococcal nuclease treatment assay revealed that the S. pombe nucleosome is markedly unstable and its DNA ends are quite accessible, as compared to the canonical human nucleosome. These findings are important to understand the mechanisms of epigenetic genomic DNA regulation in fission yeast.","doi":"10.1016/j.bbrc.2016.11.130","authors":"Koyama M, Nagakura W, Tanaka H, Kujirai T, Chikashige Y, Haraguchi T, Hiraoka Y, Kurumizaka H","authors_abbrev":"Koyama M et al.","pubmed_publication_date":"22 Jan 2017","pubmed_entrez_date":"2016-11-29","publication_year":"2017","canto_session_key":"97974af394db2b84","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-11-30 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.06c","SPAC1834.03c","SPBC1105.11c","SPCC622.09"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"GO_REF:0000078","title":"Representation for the transport or vesicle-mediated transport of a chemical from and/or to a cell component as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the transport or vesicle-mediated transport of a chemical entity (ChEBI) from and/or to a cellular component as a biological process. The underlying equivalence axiom templates are \"GO:0006810 and 'transports or maintains localization of' some X [ and 'has_target_start_location' some F] [ and 'has_target_end_location' some T]\" (transport) and \"GO:0016192 and 'transports or maintains localization of' some X [ and 'has_target_start_location' some F] [ and 'has_target_end_location' some T]\" (vesicle-mediated transport), where F and T are cellular components and X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22561704","title":"Regulation of cell cycle and stress responses under nitrosative stress in Schizosaccharomyces pombe.","citation":"Free Radic Biol Med 2012 Jun 1;52(11-12):2186-200","abstract":"Nitric oxide (NO) acts as a signaling molecule in numerous physiological processes but excess production generates nitrosative stress in cells. The exact protective mechanism used by cells to combat nitrosative stress is unclear. In this study, the fission yeast Schizosaccharomyces pombe has been used as a model system to explore cell cycle regulation and stress responses under nitrosative stress. Exposure to an NO donor results in mitotic delay in cells through G2/M checkpoint activation and initiates rereplication. Western blot analysis of phosphorylated Cdc2 revealed that the G2/M block in the cell cycle was due to retention of its inactive phosphorylated form. Interestingly, nitrosative stress results in inactivation of Cdc25 through S-nitrosylation that actually leads to cell cycle delay. From differential display analysis, we identified plo1, spn4, and rga5, three cell cycle-related genes found to be differentially expressed under nitrosative stress. Exposure to nitrosative stress also results in abnormal septation and cytokinesis in S. pombe. In summary we propose a novel molecular mechanism of cell cycle control under nitrosative stress based on our experimental results and bioinformatics analysis.","doi":"10.1016/j.freeradbiomed.2012.03.026","authors":"Majumdar U, Biswas P, Subhra Sarkar T, Maiti D, Ghosh S","authors_abbrev":"Majumdar U et al.","pubmed_publication_date":"1 Jun 2012","pubmed_entrez_date":"2012-05-08","publication_year":"2012","canto_session_key":"4c3ae230fa3c6f4d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-01-08 17:58:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-23 15:46:43","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPBC17F3.01c","SPAC1783.07c","SPAC9G1.11c","SPAC24H6.05","SPBC11B10.09"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2015-11-23"},{"uniquename":"PMID:16148042","title":"Cytokinesis depends on the motor domains of myosin-II in fission yeast but not in budding yeast.","citation":"Mol Biol Cell 2005 Nov;16(11):5346-55","abstract":"Budding yeast possesses one myosin-II, Myo1p, whereas fission yeast has two, Myo2p and Myp2p, all of which contribute to cytokinesis. We find that chimeras consisting of Myo2p or Myp2p motor domains fused to the tail of Myo1p are fully functional in supporting budding yeast cytokinesis. Remarkably, the tail alone of budding yeast Myo1p localizes to the contractile ring, supporting both its constriction and cytokinesis. In contrast, fission yeast Myo2p and Myp2p require both the catalytic head domain as well as tail domains for function, with the tails providing distinct functions (Bezanilla and Pollard, 2000). Myo1p is the first example of a myosin whose cellular function does not require a catalytic motor domain revealing a novel mechanism of action for budding yeast myosin-II independent of actin binding and ATPase activity.","authors":"Lord M, Laves E, Pollard TD","authors_abbrev":"Lord M et al.","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-09-09","publication_year":"2005","canto_session_key":"511fe9bebeaede79","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-03 07:11:58","canto_approved_date":"2023-07-05 11:34:48","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2021-01-01 17:19:00","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-01-03"},{"uniquename":"PMID:37371519","title":"Quantifying Yeast Microtubules and Spindles Using the Toolkit for Automated Microtubule Tracking (TAMiT).","citation":"Biomolecules 2023 Jun 04;13(6)","abstract":"Fluorescently labeled proteins absorb and emit light, appearing as Gaussian spots in fluorescence imaging. When fluorescent tags are added to cytoskeletal polymers such as microtubules, a line of fluorescence and even non-linear structures results. While much progress has been made in techniques for imaging and microscopy, image analysis is less well-developed. Current analysis of fluorescent microtubules uses either manual tools, such as kymographs, or automated software. As a result, our ability to quantify microtubule dynamics and organization from light microscopy remains limited. Despite the development of automated microtubule analysis tools for in vitro studies, analysis of images from cells often depends heavily on manual analysis. One of the main reasons for this disparity is the low signal-to-noise ratio in cells, where background fluorescence is typically higher than in reconstituted systems. Here, we present the Toolkit for Automated Microtubule Tracking (TAMiT), which automatically detects, optimizes, and tracks fluorescent microtubules in living yeast cells with sub-pixel accuracy. Using basic information about microtubule organization, TAMiT detects linear and curved polymers using a geometrical scanning technique. Images are fit via an optimization problem for the microtubule image parameters that are solved using non-linear least squares in Matlab. We benchmark our software using simulated images and show that it reliably detects microtubules, even at low signal-to-noise ratios. Then, we use TAMiT to measure monopolar spindle microtubule bundle number, length, and lifetime in a large dataset that includes several  S. pombe  mutants that affect microtubule dynamics and bundling. The results from the automated analysis are consistent with previous work and suggest a direct role for CLASP/Cls1 in bundling spindle microtubules. We also illustrate automated tracking of single curved astral microtubules in  S. cerevisiae , with measurement of dynamic instability parameters. The results obtained with our fully-automated software are similar to results using hand-tracked measurements. Therefore, TAMiT can facilitate automated analysis of spindle and microtubule dynamics in yeast cells.","doi":"10.3390/biom13060939","authors":"Ansari S, Gergely ZR, Flynn P, Li G, Moore JK, Betterton MD","authors_abbrev":"Ansari S et al.","pubmed_publication_date":"04 Jun 2023","pubmed_entrez_date":"2023-06-28","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-06-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16849797","title":"A survey of all 11 ABC transporters in fission yeast: two novel ABC transporters are required for red pigment accumulation in a Schizosaccharomyces pombe adenine biosynthetic mutant.","citation":"Microbiology (Reading) 2006 Aug;152(Pt 8):2309-2321","abstract":"ATP-binding cassette (ABC) proteins transport a wide variety of substrates, including sugars, amino acids, metal ions, lipids, peptides and proteins, across membranes, and most ABC proteins contain transmembrane domains (ABC transporters). Sequencing of the Schizosaccharomyces pombe genome has allowed identification of all genes encoding ABC transporters in fission yeast. To date, six such genes have been characterized, and an additional five genes encoding ABC transporters were identified from the genome sequence. In an attempt to characterize all of the ABC transporters in fission yeast, all 11 genes were disrupted. While all the genes were found to be dispensable for cell viability, some disruptants lacked apparent phenotypes. GFP-tagged ABC transporters were localized to membranes as follows: plasma membrane (2), vacuolar membrane (4), mitochondrial membrane (2), endoplasmic reticulum membrane (2), and endosome and Golgi membranes (1). Two Cluster II. 1 proteins, Abc2p (SPAC3F10.11c) and Abc4p (SPAC30.04c), were found to be localized to vacuolar membranes, and to be responsible for accumulation of a characteristic red pigment in the vacuole of an adenine biosynthetic mutant. The doubly disrupted mutant abc2 Delta abc4 Delta exhibited drug sensitivity, and a decreased accumulation of monochlorobimane, suggesting that both of the proteins encoded by these genes are involved in detoxification of xenobiotics, and vacuolar sequestration of glutathione S-conjugates.","doi":"10.1099/mic.0.28952-0","authors":"Iwaki T, Giga-Hama Y, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-07-20","publication_year":"2006","canto_session_key":"408bb296257afbcf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-13 22:08:04","canto_approved_date":"2022-06-16 07:34:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-08 15:59:47","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":62,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.09c","SPAC30.04c","SPAC9E9.12c","SPBC9B6.09c","SPAC15A10.01","SPAC1B3.14","SPCC663.03","SPBC25B2.02c","SPBC359.05","SPAPB24D3.09c","SPCC18B5.01c","SPAC3F10.11c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2017-09-13"},{"uniquename":"PMID:15893732","title":"Negative control contributes to an extensive program of meiotic splicing in fission yeast.","citation":"Mol Cell 2005 May 13;18(4):491-8","abstract":"Despite a high frequency of introns in the fission yeast Schizosaccharomyces pombe, regulated splicing is virtually unknown. We present evidence that splicing constitutes a major mechanism for controlling gene expression during meiosis, as 12 of 96 transcripts tested, which encode known components as well as previously uncharacterized ORFs, retain introns until specific times during differentiation. The meiotically spliced pre-mRNAs include two cyclins, rem1 (discovered by Ayte and Nurse) and crs1. Consistent with the use of regulated splicing to block protein production, expression of crs1 in vegetative cells is toxic. Analyses of gene chimeras indicate that splicing is prevented in mitotically growing cells via inhibition, in contrast to the positive control of meiotic splicing in budding yeast. Most strikingly, splicing of crs1 and rem1 is regulated by sequences located outside the coding regions, far from the target introns, a phenomenon previously observed only in metazoans.","authors":"Averbeck N, Sunder S, Sample N, Wise JA, Leatherwood J","authors_abbrev":"Averbeck N et al.","pubmed_publication_date":"13 May 2005","pubmed_entrez_date":"2005-05-17","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2G2.09c","SPAC222.15","SPCC1919.11","SPAC4G9.05","SPBC21C3.18","SPBC1778.04","SPBC1198.12","SPAPB17E12.09","SPBC32H8.06","SPBC29A10.14","SPAC6G10.06"],"gene_count":11,"ltp_gene_count":0},{"uniquename":"PMID:16076563","title":"Roles of base excision repair enzymes Nth1p and Apn2p from Schizosaccharomyces pombe in processing alkylation and oxidative DNA damage.","citation":"DNA Repair (Amst) 2005 Nov 21;4(11):1270-80","abstract":"Schizosaccharomyces pombe Nthpl, an ortholog of the endonuclease III family, is the sole bifunctional DNA glycosylase encoded in its genome. The enzyme removes oxidative pyrimidine and incises 3' to the apurinic/apyrimidinic (AP) site, leaving 3'-alpha,beta-unsaturated aldehyde. Analysis of nth1 cDNA revealed an intronless structure including 5'- and 3'-untranslated regions. An Nth1p-green fluorescent fusion protein was predominantly localized in the nuclei of yeast cells, indicating a nuclear function. Deletion of nth1 confirmed that Nth1p is responsible for the majority of activity for thymine glycol and AP site incision in the absence of metal ions, while nth1 mutants exhibit hypersensitivity to methylmethanesulfonate (MMS). Complementation of sensitivity by heterologous expression of various DNA glycosylases showed that the methyl-formamidopyrimidine (me-fapy) and/or AP sites are plausible substrates for Nth1p in repairing MMS damage. Apn2p, the major AP endonuclease in S. pombe, also greatly contributes to the repair of MMS damage. Deletion of nth1 from an apn2 mutant resulted in tolerance to MMS damage, indicating that Nth1p-induced 3'-blocks are responsible for MMS sensitivity in apn2 mutants. Overexpression of Apn2p in nth1 mutants failed to suppress MMS sensitivity. These results indicate that Nth1p, not Apn2p, primarily incises AP sites and that the resultant 3'-blocks are removed by the 3'-phosphodiesterase activity of Apn2p. Nth1p is dispensable for cell survival against low levels of oxidative stress, but wild-type yeast became more sensitive than the nth1 mutant at high levels. Overexpression of Nth1p in heavily damaged cells probably induced cell death via the formation of 3'-blocked single-strand breaks.","authors":"Sugimoto T, Igawa E, Tanihigashi H, Matsubara M, Ide H, Ikeda S","authors_abbrev":"Sugimoto T et al.","pubmed_publication_date":"21 Nov 2005","pubmed_entrez_date":"2005-08-04","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3D6.10","SPAC30D11.07"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:1515675","title":"A gene encoding a protein with seven zinc finger domains acts on the sexual differentiation pathways of Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1992 Jul;3(7):721-34","abstract":"Byr3 was selected as a multicopy suppressor of the sporulation defects of diploid Schizosaccharomyces pombe cells that lack ras1. Like cells mutant at byr1 and byr2, two genes that encode putative protein kinases and that in multiple copies are also suppressors of the sporulation defects of ras1 null diploid cells, cells mutant at byr3 are viable but defective in conjugation. Nucleic acid sequence indicates byr3 has the capacity to encode a protein with seven zinc finger binding domains, similar in structure to the cellular nucleic acid binding protein (CNBP), a human protein that was identified on the basis of its ability to bind DNA. Expression of CNBP in yeast can partially suppress conjugation defects of cells lacking byr3.","authors":"Xu HP, Rajavashisth T, Grewal N, Jung V, Riggs M, Rodgers L, Wigler M","authors_abbrev":"Xu HP et al.","pubmed_publication_date":"Jul 1992","pubmed_entrez_date":"1992-07-01","publication_year":"1992","canto_session_key":"4ebd3c0f10daf88d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-09-23 16:41:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-23 09:56:37","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC1D7.05","SPAC1D4.13","SPAC13D6.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2013-09-23"},{"uniquename":"PMID:19041767","title":"Insig regulates HMG-CoA reductase by controlling enzyme phosphorylation in fission yeast.","citation":"Cell Metab 2008 Dec;8(6):522-31","abstract":"Insig functions as a central regulator of cellular cholesterol homeostasis by controlling activity of HMG-CoA reductase (HMGR) in cholesterol synthesis. Insig both accelerates the degradation of HMGR and suppresses HMGR transcription through the SREBP-Scap pathway. The fission yeast Schizosaccharomyces pombe encodes homologs of Insig, HMGR, SREBP, and Scap, called ins1(+), hmg1(+), sre1(+), and scp1(+). Here, we characterize fission yeast Insig and demonstrate that Ins1 is dedicated to regulation of Hmg1, but not the Sre1-Scp1 pathway. Using a sterol-sensing domain mutant of Hmg1, we demonstrate that Ins1 binding to Hmg1 inhibits enzyme activity by promoting phosphorylation of the Hmg1 active site, which increases the K(M) for NADPH. Ins1-dependent phosphorylation of Hmg1 requires the MAP kinase Sty1/Spc1, and Hmg1 phosphorylation is physiologically regulated by nutrient stress. Thus, in fission yeast, Insig regulates sterol synthesis by a different mechanism than in mammalian cells, controlling HMGR phosphorylation in response to nutrient supply.","doi":"10.1016/j.cmet.2008.09.004","authors":"Burg JS, Powell DW, Chai R, Hughes AL, Link AJ, Espenshade PJ","authors_abbrev":"Burg JS et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-12-02","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPCC162.09c","SPCC306.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:18030666","title":"Mutations in deoxyribonucleotide biosynthesis pathway cause spreading of silencing across heterochromatic barriers at the mating-type region of the fission yeast.","citation":"Yeast 2008 Feb;25(2):117-28","abstract":"The mat2,3-region of Schizosaccharomyces pombe is flanked by two inverted repeat elements, IRL and IRR, which define the boundaries of the silent domain resulting from heterochromatin assembly in the region. We employed a genetic screen to isolate factors whose mutations allowed spreading of heterochromatin across boundary elements. Surprisingly, this screen revealed that mutations in the genes required for deoxyribonucleotide biosynthesis, cdc22 (encoding the large subunit of ribonucleotide reductase) and tds1 (putative thymidylate synthase), cause silencing of marker genes inserted outside of the silent domain. Chromatin-immunoprecipitation analysis showed that histone H3 lysine 9 methylation modification, an epigenetic mark associated with gene silencing, is enriched by two- to three-fold in the cdc22 mutant as compared to the level found in the wild-type strain in regions outside the silent domain. The spreading of heterochromatin across barriers required functional Atf1/Pcr1, ATF-CREB family proteins, but not the RNA-interference Dcr1, Ago1, or Rdp1 factors, previously implicated in silencing. These results implicate the deoxyribonucleotide biosynthesis pathway in limiting epigenetic controls at barrier elements at the mating-type region, but the mechanism remains unknown.","authors":"Singh G, Klar AJ","authors_abbrev":"Singh G et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2007-11-22","publication_year":"2008","canto_session_key":"a5af9fd629607a18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-09 19:01:18","canto_approved_date":"2023-03-09 19:01:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-28 16:38:47","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15E1.04","SPAC664.01c","SPAC1F7.05","SPBC2D10.17","SPBC800.03","SPBC29B5.01","SPBC428.08c","SPAC21E11.03c","SPAC1B3.17"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2023-03-09"},{"uniquename":"PMID:16946276","title":"Mechanisms of copper loading on the Schizosaccharomyces pombe copper amine oxidase 1 expressed in Saccharomyces cerevisiae.","citation":"Microbiology (Reading) 2006 Sep;152(Pt 9):2819-2830","abstract":"Copper amine oxidases (CAOs) are found in almost every living kingdom. Although Saccharomyces cerevisiae is one of the few yeast species that lacks an endogenous CAO, heterologous gene expression of CAOs from other organisms produces a functional enzyme. To begin to characterize their function and mechanisms of copper acquisition, two putative cao(+) genes from Schizosaccharomyces pombe were expressed in S. cerevisiae. Expression of spao1(+) resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. On the other hand, expression of spao2(+) failed to produce an active CAO. Using a functional spao1(+)-GFP fusion allele, the SPAO1 protein was localized in the cytosol. Under copper-limiting conditions, yeast cells harbouring deletions of the MAC1, CTR1 and CTR3 genes were defective in amine oxidase activity. Likewise, atx1Delta null cells exhibited no CAO activity, while ccc2Delta mutant cells exhibited decreased levels of amine oxidase activity, and mutations in cox17Delta and ccs1Delta did not cause any defects in this activity. Copper-deprived S. cerevisiae cells expressing spao1(+) required a functional atx1(+) gene for growth on minimal medium containing ethylamine as the sole nitrogen source. Under these conditions, the inability of the atx1Delta cells to utilize ethylamine correlated with the lack of SPAO1 activity, in spite of the efficient expression of the protein. Cells carrying a disrupted ccc2Delta allele exhibited only weak growth on ethylamine medium containing a copper chelator. The results of these studies reveal that expression of the heterologous spao1(+) gene in S. cerevisiae is required for its growth in medium containing ethylamine as the sole nitrogen source, and that expression of an active Schiz. pombe SPAO1 protein in S. cerevisiae depends on the acquisition of copper through the high-affinity copper transporters Ctr1 and Ctr3, and the copper chaperone Atx1.","doi":"10.1099/mic.0.28998-0","authors":"Laliberté J, Labbé S","authors_abbrev":"Laliberté J et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-09-02","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2E1P3.04"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"EMBL:AU006701","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27501521","title":"Analysis of biophysical and functional consequences of tropomyosin-fluorescent protein fusions.","citation":"FEBS Lett 2016 Sep;590(18):3111-21","abstract":"The dynamic nature of actin polymers is modulated to facilitate a diverse range of cellular processes. These dynamic properties are determined by different isoforms of tropomyosin which are recruited to distinct subpopulations of actin polymers to differentially regulate their functional properties. This makes tropomyosin an attractive target for labelling discrete actin populations. We have assessed the effect of different fluorescent labelling strategies for this protein. Although tropomyosin-fluorescent fusions decorate actin in vivo, they are either nonfunctional or perturb regulation of actin nucleation and cell cycle timings. Thus, conclusions and physiological relevance should be carefully evaluated when using tropomyosin fusions.","doi":"10.1002/1873-3468.12346","authors":"Brooker HR, Geeves MA, Mulvihill DP","authors_abbrev":"Brooker HR et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-08-09","publication_year":"2016","canto_session_key":"4722f0259f7052e4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-08-10 00:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPBC32H8.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9826747","title":"Schizosaccharomyces pombe rad32 protein: a phosphoprotein with an essential phosphoesterase motif required for repair of DNA double strand breaks.","citation":"Nucleic Acids Res 1998 Dec 01;26(23):5261-9","abstract":"The Schizosaccharomyces pombe Rad32 protein is required for repair of DNA double strand breaks, minichromosome stability and meiotic recombination. We show here that the Rad32 protein is phosphorylated in a cell cycle-dependent manner and during meiosis. The phosphorylation is not dependent on the checkpoint protein Rad3. Analysis of a partially purified protein preparation indicates that Rad32 is likely to act in a complex. Characterisation of the rad32-1 mutation and site-directed mutagenesis indicate that three aspartate residues in the conserved phosphoesterase motifs are important for both mitotic and meiotic functions, namely response to UV and ionising radiation and spore viability.","authors":"Wilson S, Tavassoli M, Watts FZ","authors_abbrev":"Wilson S et al.","pubmed_publication_date":"01 Dec 1998","pubmed_entrez_date":"1998-11-25","publication_year":"1998","canto_session_key":"4770a22740e77442","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-18 14:02:14","canto_approved_date":"2021-06-08 17:00:47","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-04-15 15:16:40","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":84,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC13C5.07","SPAC3G6.06c","SPAC30D11.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-04-18"},{"uniquename":"PMID:19736319","title":"Proper timing of cytokinesis is regulated by Schizosaccharomyces pombe Etd1.","citation":"J Cell Biol 2009 Sep 07;186(5):739-53","abstract":"Cytokinesis must be initiated only after chromosomes have been segregated in anaphase and must be terminated once cleavage is completed. We show that the fission yeast protein Etd1 plays a central role in both of these processes. Etd1 activates the guanosine triphosphatase (GTPase) Spg1 to trigger signaling through the septum initiation network (SIN) pathway and onset of cytokinesis. Spg1 is activated in late anaphase when spindle elongation brings spindle pole body (SPB)-localized Spg1 into proximity with its activator Etd1 at cell tips, ensuring that cytokinesis is only initiated when the spindle is fully elongated. Spg1 is active at just one of the two SPBs during cytokinesis. When the actomyosin ring finishes constriction, the SIN triggers disappearance of Etd1 from the half of the cell with active Spg1, which then triggers Spg1 inactivation. Asymmetric activation of Spg1 is crucial for timely inactivation of the SIN. Together, these results suggest a mechanism whereby cell asymmetry is used to monitor cytoplasmic partitioning to turn off cytokinesis signaling.","doi":"10.1083/jcb.200902116","authors":"García-Cortés JC, McCollum D","authors_abbrev":"García-Cortés JC et al.","pubmed_publication_date":"07 Sep 2009","pubmed_entrez_date":"2009-09-09","publication_year":"2009","canto_session_key":"358a49422d80513c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-08 13:28:31","canto_approved_date":"2022-07-28 11:44:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-02 15:54:53","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPAC24B11.11c","SPBC21.06c","SPAC1006.08","SPAC1565.06c","SPBC20F10.06"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2021-01-08"},{"uniquename":"PMID:17703206","title":"A protocol for isolation and visualization of yeast nuclei by scanning electron microscopy (SEM).","citation":"Nat Protoc 2007;2(8):1943-53","abstract":"This protocol details methods for the isolation of yeast nuclei from budding yeast (Saccharomyces cerevisiae) and fission yeast (Schizosaccharomyces pombe), immuno-gold labeling of proteins and visualization by field emission scanning electron microscopy (FESEM). This involves the removal of the yeast cell wall and isolation of the nucleus from within, followed by subsequent processing for high-resolution microscopy. The nuclear isolation step can be performed in two ways: enzymatic treatment of yeast cells to rupture the cell wall and generate spheroplasts (cells that have partially lost their cell wall and their characteristic shape), followed by isolation of the nuclei by centrifugation or homogenization; and whole cell freezing followed by manual cell rupture and centrifugation. This protocol has been optimized for the visualization of the yeast nuclear envelope (NE), nuclear pore complexes (NPCs) and associated cyto-skeletal structures. Samples once processed for FESEM can be stored under vacuum for weeks, allowing considerable time for image acquisition.","authors":"Kiseleva E, Allen TD, Rutherford SA, Murray S, Morozova K, Gardiner F, Goldberg MW, Drummond SP","authors_abbrev":"Kiseleva E et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-08-19","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17449726","title":"A family of poly(U) polymerases.","citation":"RNA 2007 Jun;13(6):860-7","abstract":"The GLD-2 family of poly(A) polymerases add successive AMP monomers to the 3' end of specific RNAs, forming a poly(A) tail. Here, we identify a new group of GLD-2-related nucleotidyl transferases from Arabidopsis, Schizosaccharomyces pombe, Caenorhabditis elegans, and humans. Like GLD-2, these enzymes are template independent and add nucleotides to the 3' end of an RNA substrate. However, these new enzymes, which we refer to as poly(U) polymerases, add poly(U) rather than poly(A) to their RNA substrates.","authors":"Kwak JE, Wickens M","authors_abbrev":"Kwak JE et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-04-24","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19D5.03"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:32064568","title":"A convenient new method for reproducible fed-batch fermentation of fission yeast Schizosaccharomyces pombe.","citation":"Biotechnol Lett 2020 Jun;42(6):937-943","abstract":"Development of an open-loop fed-batch protocol for highly reproducible fermentation of fission yeast that starts from batch cultures instead of glucose-limited aerobic chemostat cultures.\nThese data demonstrate the usefulness of the proposed strategy. It is expected that by variation of only two parameters (the total amount of glucose fed in the initial phase and the time frame of the starvation phase) the protocol can easily be adapted to other microbes.","doi":"10.1007/s10529-020-02840-1","authors":"Scomparin A, Bureik M","authors_abbrev":"Scomparin A et al.","pubmed_publication_date":"Jun 2020","pubmed_entrez_date":"2020-02-18","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36330920","title":"A proto-telomere is elongated by telomerase in a shelterin-dependent manner in quiescent fission yeast cells.","citation":"Nucleic Acids Res 2022 Nov 11;50(20):11682-11695","abstract":"Telomere elongation is coupled with genome replication, raising the question of the repair of short telomeres in post-mitotic cells. We investigated the fate of a telomere-repeat capped end that mimics a single short telomere in quiescent fission yeast cells. We show that telomerase is able to elongate this single short telomere during quiescence despite the binding of Ku to the proto-telomere. While Taz1 and Rap1 repress telomerase in vegetative cells, both shelterin proteins are required for efficient telomere extension in quiescent cells, underscoring a distinct mode of telomerase control. We further show that Rad3ATR and Tel1ATM are redundantly required for telomere elongation in quiescence through the phosphorylation of Ccq1 and that Rif1 and its associated-PP1 phosphatases negatively regulate telomerase activity by opposing Ccq1 phosphorylation. The distinct mode of telomerase regulation in quiescent fission yeast cells may be relevant to that in human stem and progenitor cells.","doi":"10.1093/nar/gkac986","authors":"Vaurs M, Audry J, Runge KW, Géli V, Coulon S","authors_abbrev":"Vaurs M et al.","pubmed_publication_date":"11 Nov 2022","pubmed_entrez_date":"2022-11-04","publication_year":"2022","canto_session_key":"38e2f944ebb30468","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-11-06 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23957011","title":"Robust cell size checkpoint from spatiotemporal positive feedback loop in fission yeast.","citation":"Biomed Res Int 2013;2013:910941","abstract":"Cells must maintain appropriate cell size during proliferation. Size control may be regulated by a size checkpoint that couples cell size to cell division. Biological experimental data suggests that the cell size is coupled to the cell cycle in two ways: the rates of protein synthesis and the cell polarity protein kinase Pom1 provide spatial information that is used to regulate mitosis inhibitor Wee1. Here a mathematical model involving these spatiotemporal regulations was developed and used to explore the mechanisms underlying the size checkpoint in fission yeast. Bifurcation analysis shows that when the spatiotemporal regulation is coupled to the positive feedback loops (active Cdc2 promotes its activator, Cdc25, and suppress its inhibitor, Wee1), the mitosis-promoting factor (MPF) exhibits a bistable steady-state relationship with the cell size. The switch-like response from the positive feedback loops naturally generates the cell size checkpoint. Further analysis indicated that the spatial regulation provided by Pom1 enhances the robustness of the size checkpoint in fission yeast. This was consistent with experimental data.","doi":"10.1155/2013/910941","authors":"Yan J, Ni X, Yang L","authors_abbrev":"Yan J et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-08-20","publication_year":"2013","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9256078","title":"Cloning and characterization of the S. pombe gene efc25+, a new putative guanine nucleotide exchange factor.","citation":"Gene 1997 Jul 09;193(2):203-10","abstract":"We report the cloning and characterization of a new S. pombe gene, efc25+, for 'exchange factor Cdc25-like'. The C-terminal region of the predicted product of this gene displays high sequence homology with a number of guanine nucleotide exchange factors for Ras. These include Cdc25 of Saccharomyces cerevisiae, Cdc25 of Saccharomyces kluyveri, Csc25 of Candida albicans, Sdc25 of S. cerevisiae and Ste6 of Schizosaccharomyces pombe. Disruption of efc25+ resulted in cells with a spherical shape reminiscent of the abnormal morphological phenotype of ras1 deletion mutants. However, unlike ras1 null mutants, strains deleted for efc25+ were proficient for mating and sporulation. This differs from the only other Ras1 exchange factor characterized so far in S. pombe, the Ste6 protein, whose deletion results in defects in mating and sporulation but not in cell shape. We hypothesize that Efc25 is an exchange factor for Ras1 and that it is involved in a signaling pathway different from that involving Ste6.","authors":"Tratner I, Fourticq-Esqueöute A, Tillit J, Baldacci G","authors_abbrev":"Tratner I et al.","pubmed_publication_date":"09 Jul 1997","pubmed_entrez_date":"1997-07-09","publication_year":"1997","canto_session_key":"269451d6e6e14cee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-03-11 15:51:17","canto_approved_date":"2023-12-27 20:30:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-11 15:51:08","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-03-11"},{"uniquename":"PMID:7774573","title":"Dominant mutants identify new roles for p34cdc2 in mitosis.","citation":"EMBO J 1995 May 15;14(10):2155-65","abstract":"A large number of dominant mutants have been generated in the fission yeast cdc2 gene, causing lethality when expressed in wild-type cells. The mutants interfere with distinct aspects of p34cdc2 function, producing one of four different phenotypes: mitotic arrest, multiple rounds of S phase in the absence of mitosis, premature mitosis or G2 arrest. The mitotic mutants DL41, DL45 and DL50 are characterized in this paper. Over-expression of DL41 or DL45 causes mitotic arrest, specifically interfering with sister chromatid separation, without preventing spindle elongation. This suggests a role for p34cdc2 in triggering sister chromatid separation at anaphase. DL41 and DL45 also cause abnormal septum formation, suggesting that p34cdc2 may also be involved in regulating this process in fission yeast. These mitotic aspects of p34cdc2 function may involve interaction with p13suc1, since increased expression of suc1 partially suppresses DL41 and DL45. Over-expression of DL50 causes premature mitotic entry in cells that have not completed S phase, resulting in lethality. DL41, DL45 and DL50 correspond to mutation of p34cdc2 residues predicted to be on the surface of the protein, identifying potential sites of interaction with mitotic regulators of p3cdc2, and these residues are conserved amongst cdc2 proteins found in other eukaryotes.","authors":"Labib K, Craven RA, Crawford K, Nurse P","authors_abbrev":"Labib K et al.","pubmed_publication_date":"15 May 1995","pubmed_entrez_date":"1995-05-15","publication_year":"1995","canto_session_key":"2bfae567526bc0ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-03-26 12:53:12","canto_approved_date":"2022-05-31 07:06:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-20 13:57:36","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":25,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.14c","SPBC11B10.09","SPAC24H6.05","SPBC582.03"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-03-26"},{"uniquename":"PMID:16246721","title":"The nucleation and maintenance of heterochromatin by a histone deacetylase in fission yeast.","citation":"Mol Cell 2005 Oct 28;20(2):173-85","abstract":"Posttranslational modifications of histones play an essential role in heterochromatin assembly. Whereas the role of Clr4/Suv39h-mediated methylation of histone H3 at lysine 9 (H3K9) in heterochromatin assembly is well studied, the exact function of histone deacetylases (HDACs) in this process is unclear. We show that Clr3, a fission yeast homolog of mammalian class II HDACs, acts in a distinct pathway parallel to RNAi-directed heterochromatin nucleation to recruit Clr4 and mediate H3K9 methylation at the silent mating-type region and centromeres. At the mat locus, Clr3 is recruited at a specific site through a mechanism involving ATF/CREB family proteins. Once recruited, Clr3 spreads across the 20 kb silenced domain that requires its own HDAC activity and heterochromatin proteins including Swi6/HP1. We also demonstrate that Clr3 contributes to heterochromatin maintenance by stabilizing H3K9 trimethylation and by preventing histone modifications associated with active transcription, and that it limits RNA polymerase II accessibility to naturally silenced repeats at heterochromatin domains.","authors":"Yamada T, Fischle W, Sugiyama T, Allis CD, Grewal SI","authors_abbrev":"Yamada T et al.","pubmed_publication_date":"28 Oct 2005","pubmed_entrez_date":"2005-10-26","publication_year":"2005","canto_session_key":"dfd513564cb0ad94","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-31 23:03:54","canto_approved_date":"2024-03-04 14:01:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-25 17:27:05","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC21E11.03c","SPBC16C6.10","SPAC18G6.02c","SPCC188.13c","SPBC29B5.01","SPCC962.02c","SPAC664.01c","SPBC16D10.07c","SPBC800.03","SPBC428.08c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2024-01-31"},{"uniquename":"PMID:22840999","title":"Should I stay or should I go? Chromodomain proteins seal the fate of heterochromatic transcripts in fission yeast.","citation":"Mol Cell 2012 Jul 27;47(2):153-5","abstract":"In this issue of Molecular Cell, Ishida et al. (2012) and Keller et al. (2012) show distinct outcomes for heterochromatic RNAs that bind different chromodomain proteins; Chp1 tethers transcripts to centromeres, whereas Swi6(HP1)-bound transcripts are evicted from chromatin and destroyed.","doi":"10.1016/j.molcel.2012.07.007","authors":"Creamer KM, Partridge JF","authors_abbrev":"Creamer KM et al.","pubmed_publication_date":"27 Jul 2012","pubmed_entrez_date":"2012-07-31","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31785604","title":"Metabolism of phospholipids in the yeast Schizosaccharomyces pombe.","citation":"Yeast 2020 Jan;37(1):73-92","abstract":"The fission yeast Schizosaccharomyces pombe is an important model organism for the study of fundamental questions in eukaryotic cell and molecular biology. A plethora of cellular processes are membrane associated and/or dependent on the proper functioning of cellular membranes. Phospholipids are not only the basic building blocks of cellular membranes; they also serve as precursors to numerous signaling molecules. In this review, we describe the biosynthetic pathways leading to major S. pombe phospholipids, how these pathways are regulated, and what is known about degradation and turnover of fission yeast phospholipids. This review also addresses the synthesis, regulation and the role of water-soluble phospholipid precursors. The last chapter of the review is devoted to the use of S. pombe for the biotechnological production of value-added lipid molecules.","doi":"10.1002/yea.3451","authors":"Holič R, Pokorná L, Griač P","authors_abbrev":"Holič R et al.","pubmed_publication_date":"Jan 2020","pubmed_entrez_date":"2019-12-01","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-12-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24631047","title":"Refining network reconstruction based on functional reliability.","citation":"J Theor Biol 2014 Jul 21;353:170-8","abstract":"Reliable functioning is crucial for the survival and development of the genetic regulatory networks in living cells and organisms. This functional reliability is an important feature of the networks and reflects the structural features that have been embedded in the regulatory networks by evolution. In this paper, we integrate this reliability into network reconstruction. We introduce the concept of dependency probability to measure the dependency of functional reliability on network edges. We also propose a method to estimate the dependency probability and select edges with high contributions to functional reliability. We use two real examples, the regulatory network of the cell cycle of the budding yeast and that of the fission yeast, to demonstrate that the proposed method improves network reconstruction. In addition, the dependency probability is robust in calculation and can be easily implemented in practice.","doi":"10.1016/j.jtbi.2014.02.041","authors":"Zhang Y, Ouyang Q, Geng Z","authors_abbrev":"Zhang Y et al.","pubmed_publication_date":"21 Jul 2014","pubmed_entrez_date":"2014-03-18","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC10688","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18255266","title":"Activation of the cell integrity pathway is channelled through diverse signalling elements in fission yeast.","citation":"Cell Signal 2008 Apr;20(4):748-57","abstract":"MAPK Pmk1p is the central element of a cascade involved in the maintenance of cell integrity and other functions in Schizosaccharomyces pombe. Pmk1p becomes activated by multiple stressing situations and also during cell separation. GTPase Rho2p acts upstream of the protein kinase C homolog Pck2p to activate the Pmk1 signalling pathway through direct interaction with MAPKKK Mkh1p. In this work we analyzed the functional significance of both Rho2p and Pck2p in the transduction of various stress signals by the cell integrity pathway. The results indicate that basal Pmk1p activity can be positively regulated by alternative mechanisms which are independent on the control by Rho2p and/or Pck2p. Unexpectedly, Pck1p, another protein kinase C homolog, negatively modulates Pmk1p basal activity by an unknown mechanism. Moreover, different elements appear to regulate the stress-induced activation of Pmk1p depending on the nature of the triggering stimuli. Whereas Pmk1p activation induced by hyper- or hypotonic stresses is channeled through Rho2p-Pck2p, other stressors, like glucose deprivation or cell wall disturbance, are transduced via other pathways in addition to that of Rho2p-Pck2p. On the contrary, Pmk1p activation observed during cell separation or after treatment with hydrogen peroxide does not involve Rho2p-Pck2p. Finally, Pck2p function is critical to maintain a Pmk1p basal activity that allows Pmk1p activation induced by heat stress. These data demonstrate the existence of a complex signalling network modulating Pmk1p activation in response to a variety of stresses in fission yeast.","doi":"10.1016/j.cellsig.2007.12.017","authors":"Barba G, Soto T, Madrid M, Núñez A, Vicente J, Gacto M, Cansado J, Yeast Physiology Group","authors_abbrev":"Barba G et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_session_key":"2237c543f02b6647","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16600899","title":"The RNA polymerase III-dependent family of genes in hemiascomycetes: comparative RNomics, decoding strategies, transcription and evolutionary implications.","citation":"Nucleic Acids Res 2006;34(6):1816-35","abstract":"We present the first comprehensive analysis of RNA polymerase III (Pol III) transcribed genes in ten yeast genomes. This set includes all tRNA genes (tDNA) and genes coding for SNR6 (U6), SNR52, SCR1 and RPR1 RNA in the nine hemiascomycetes Saccharomyces cerevisiae, Saccharomyces castellii, Candida glabrata, Kluyveromyces waltii, Kluyveromyces lactis, Eremothecium gossypii, Debaryomyces hansenii, Candida albicans, Yarrowia lipolytica and the archiascomycete Schizosaccharomyces pombe. We systematically analysed sequence specificities of tRNA genes, polymorphism, variability of introns, gene redundancy and gene clustering. Analysis of decoding strategies showed that yeasts close to S.cerevisiae use bacterial decoding rules to read the Leu CUN and Arg CGN codons, in contrast to all other known Eukaryotes. In D.hansenii and C.albicans, we identified a novel tDNA-Leu (AAG), reading the Leu CUU/CUC/CUA codons with an unusual G at position 32. A systematic 'p-distance tree' using the 60 variable positions of the tRNA molecule revealed that most tDNAs cluster into amino acid-specific sub-trees, suggesting that, within hemiascomycetes, orthologous tDNAs are more closely related than paralogs. We finally determined the bipartite A- and B-box sequences recognized by TFIIIC. These minimal sequences are nearly conserved throughout hemiascomycetes and were satisfactorily retrieved at appropriate locations in other Pol III genes.","authors":"Marck C, Kachouri-Lafond R, Lafontaine I, Westhof E, Dujon B, Grosjean H","authors_abbrev":"Marck C et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-04-08","publication_year":"2006","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19956604","title":"Scalable steady state analysis of Boolean biological regulatory networks.","citation":"PLoS One 2009 Dec 01;4(12):e7992","abstract":"Computing the long term behavior of regulatory and signaling networks is critical in understanding how biological functions take place in organisms. Steady states of these networks determine the activity levels of individual entities in the long run. Identifying all the steady states of these networks is difficult due to the state space explosion problem.\nIn this paper, we propose a method for identifying all the steady states of Boolean regulatory and signaling networks accurately and efficiently. We build a mathematical model that allows pruning a large portion of the state space quickly without causing any false dismissals. For the remaining state space, which is typically very small compared to the whole state space, we develop a randomized traversal method that extracts the steady states. We estimate the number of steady states, and the expected behavior of individual genes and gene pairs in steady states in an online fashion. Also, we formulate a stopping criterion that terminates the traversal as soon as user supplied percentage of the results are returned with high confidence.\nThis method identifies the observed steady states of boolean biological networks computationally. Our algorithm successfully reported the G1 phases of both budding and fission yeast cell cycles. Besides, the experiments suggest that this method is useful in identifying co-expressed genes as well. By analyzing the steady state profile of Hedgehog network, we were able to find the highly co-expressed gene pair GL1-SMO together with other such pairs.\nSource code of this work is available at http://bioinformatics.cise.ufl.edu/palSteady.html twocolumnfalse].","doi":"10.1371/journal.pone.0007992","authors":"Ay F, Xu F, Kahveci T","authors_abbrev":"Ay F et al.","pubmed_publication_date":"01 Dec 2009","pubmed_entrez_date":"2009-12-04","publication_year":"2009","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011299","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10906331","title":"Isolation and cloning of four subunits of a fission yeast TFIIIC complex that includes an ortholog of the human regulatory protein TFIIICbeta.","citation":"J Biol Chem 2000 Oct 06;275(40):31480-7","abstract":"Eukaryotic tRNA genes are controlled by proximal and downstream elements that direct transcription by RNA polymerase (pol) III. Transcription factors (TFs) that reside near the initiation site are related in Saccharomyces cerevisiae and humans, while those that reside at or downstream of the B box share no recognizable sequence relatedness. Human TFIIICbeta is a transcriptional regulator that exhibits no homology to S. cerevisiae sequences on its own. We cloned an essential Schizosaccharomyces pombe gene that encodes a protein, Sfc6p, with homology to the S. cerevisiae TFIIIC subunit, TFC6p, that extends to human TFIIICbeta. We also isolated and cloned S. pombe homologs of three other TFIIIC subunits, Sfc3p, Sfc4p, and Sfc1p, the latter two of which are conserved from S. cerevisiae to humans, while the former shares homology with the S. cerevisiae B box-binding homolog only. Sfc6p is a component of a sequence-specific DNA-binding complex that also contains the B box-binding homolog, Sfc3p. Immunoprecipitation of Sfc3p further revealed that Sfc1p, Sfc3p, Sfc4p, and Sfc6p are associated in vivo and that the isolated Sfc3p complex is active for pol III-mediated transcription of a S. pombe tRNA gene in vitro. These results establish a link between the downstream pol III TFs in yeast and humans.","authors":"Huang Y, Hamada M, Maraia RJ","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"06 Oct 2000","pubmed_entrez_date":"2000-07-25","publication_year":"2000","canto_session_key":"e84045bb5d4dfe2e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-05-24 18:56:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 16:56:58","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21H7.05","SPCC16C4.14c","SPBC336.07","SPAC144.09c","SPAC6F12.11c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-09-11"},{"uniquename":"PMID:27697832","title":"Rad51 and Rad54 promote noncrossover recombination between centromere repeats on the same chromatid to prevent isochromosome formation.","citation":"Nucleic Acids Res 2016 Dec 15;44(22):10744-10757","abstract":"Centromeres consist of DNA repeats in many eukaryotes. Non-allelic homologous recombination (HR) between them can result in gross chromosomal rearrangements (GCRs). In fission yeast, Rad51 suppresses isochromosome formation that occurs between inverted repeats in the centromere. However, how the HR enzyme prevents homology-mediated GCRs remains unclear. Here, we provide evidence that Rad51 with the aid of the Swi/Snf-type motor protein Rad54 promotes non-crossover recombination between centromere repeats to prevent isochromosome formation. Mutations in Rad51 and Rad54 epistatically increased the rates of isochromosome formation and chromosome loss. In sharp contrast, these mutations decreased gene conversion between inverted repeats in the centromere. Remarkably, analysis of recombinant DNAs revealed that rad51 and rad54 increase the proportion of crossovers. In the absence of Rad51, deletion of the structure-specific endonuclease Mus81 decreased both crossovers and isochromosomes, while the cdc27/pol32-D1 mutation, which impairs break-induced replication, did not. We propose that Rad51 and Rad54 promote non-crossover recombination between centromere repeats on the same chromatid, thereby suppressing crossover between non-allelic repeats on sister chromatids that leads to chromosomal rearrangements. Furthermore, we found that Rad51 and Rad54 are required for gene silencing in centromeres, suggesting that HR also plays a role in the structure and function of centromeres.","authors":"Onaka AT, Toyofuku N, Inoue T, Okita AK, Sagawa M, Su J, Shitanda T, Matsuyama R, Zafar F, Takahashi TS, Masukata H, Nakagawa T","authors_abbrev":"Onaka AT et al.","pubmed_publication_date":"15 Dec 2016","pubmed_entrez_date":"2016-10-05","publication_year":"2016","canto_session_key":"f76448cf5f73c99d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tako Nakagawa","canto_first_approved_date":"2019-01-31 11:07:16","canto_approved_date":"2023-09-29 04:46:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-02 08:02:18","canto_added_date":"2016-10-07 00:15:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tako Nakagawa","community_curator":true,"annotation_count":37,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC30D11.10","SPBC1734.02c","SPAC15A10.03c","SPBC428.08c","SPCC4G3.05c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2019-01-31"},{"uniquename":"PMID:9032282","title":"Genes encoding farnesyl cysteine carboxyl methyltransferase in Schizosaccharomyces pombe and Xenopus laevis.","citation":"Mol Cell Biol 1997 Mar;17(3):1543-51","abstract":"The mam4 mutation of Schizosaccharomyces pombe causes mating deficiency in h- cells but not in h+ cells. h- cells defective in mam4 do not secrete active mating pheromone M-factor. We cloned mam4 by complementation. The mam4 gene encodes a protein of 236 amino acids, with several potential membrane-spanning domains, which is 44% identical with farnesyl cysteine carboxyl methyltransferase encoded by STE14 and required for the modification of a-factor in Saccharomyces cerevisiae. Analysis of membrane fractions revealed that mam4 is responsible for the methyltransferase activity in S. pombe. Cells defective in mam4 produced farnesylated but unmethylated cysteine and small peptides but no intact M-factor. These observations strongly suggest that the mam4 gene product is farnesyl cysteine carboxyl methyltransferase that modifies M-factor. Furthermore, transcomplementation of S. pombe mam4 allowed us to isolate an apparent homolog of mam4 from Xenopus laevis (Xmam4). In addition to its sequence similarity to S. pombe mam4, the product of Xmam4 was shown to have a farnesyl cysteine carboxyl methyltransferase activity in S. pombe cells. The isolation of a vertebrate gene encoding farnesyl cysteine carboxyl methyltransferase opens the way to in-depth studies of the role of methylation in a large body of proteins, including Ras superfamily proteins.","authors":"Imai Y, Davey J, Kawagishi-Kobayashi M, Yamamoto M","authors_abbrev":"Imai Y et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_session_key":"8622e3e232348e8d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-01-04 21:59:20","canto_approved_date":"2026-03-02 18:55:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-14 15:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.03","SPAC10F6.12c","SPAPB8E5.05","SPAC513.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-01-04"},{"uniquename":"PMID:23862021","title":"The C-terminus of S. pombe DDK subunit Dfp1 is required for meiosis-specific transcription and cohesin cleavage.","citation":"Biol Open 2013 Jul 15;2(7):728-38","abstract":"The DDK complex is a conserved kinase complex, consisting of a catalytic subunit, Hsk1 (Cdc7), and its regulatory subunit Dfp1 (Dbf4). This kinase is essential for DNA replication. In this work, we show that dfp1-r35, which truncates the Dfp1 C-terminus zinc finger, causes severe meiotic defects, including reduced spore viability, reduced formation of programmed double strand breaks, altered expression of meiotic genes, and disrupted chromosome segregation. There is a high frequency of dyad formation. Mutants are also defective in the phosphorylation and degradation of the meiotic cohesion, Rec8, resulting in a failure to proceed through the MII division. These defects are more pronounced in a haploid meiosis model than in a normal diploid meiosis. Thus, several critical meiotic functions are linked specifically to the C-terminus of Dfp1, which may target specific substrates for phosphorylation by Hsk1.","doi":"10.1242/bio.20135173","authors":"Le AH, Mastro TL, Forsburg SL","authors_abbrev":"Le AH et al.","pubmed_publication_date":"15 Jul 2013","pubmed_entrez_date":"2013-07-18","publication_year":"2013","canto_session_key":"1445a23bf68725db","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPBC776.12c","SPBC21.06c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:35179192","title":"Shaping centromeres to resist mitotic spindle forces.","citation":"J Cell Sci 2022 Feb 15;135(4)","abstract":"The centromere serves as the binding site for the kinetochore and is essential for the faithful segregation of chromosomes throughout cell division. The point centromere in yeast is encoded by a ∼115 bp specific DNA sequence, whereas regional centromeres range from 6-10 kbp in fission yeast to 5-10 Mbp in humans. Understanding the physical structure of centromere chromatin (pericentromere in yeast), defined as the chromatin between sister kinetochores, will provide fundamental insights into how centromere DNA is woven into a stiff spring that is able to resist microtubule pulling forces during mitosis. One hallmark of the pericentromere is the enrichment of the structural maintenance of chromosome (SMC) proteins cohesin and condensin. Based on studies from population approaches (ChIP-seq and Hi-C) and experimentally obtained images of fluorescent probes of pericentromeric structure, as well as quantitative comparisons between simulations and experimental results, we suggest a mechanism for building tension between sister kinetochores. We propose that the centromere is a chromatin bottlebrush that is organized by the loop-extruding proteins condensin and cohesin. The bottlebrush arrangement provides a biophysical means to transform pericentromeric chromatin into a spring due to the steric repulsion between radial loops. We argue that the bottlebrush is an organizing principle for chromosome organization that has emerged from multiple approaches in the field.","doi":"10.1242/jcs.259532","authors":"Lawrimore J, Bloom K","authors_abbrev":"Lawrimore J et al.","pubmed_publication_date":"15 Feb 2022","pubmed_entrez_date":"2022-02-18","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-02-20 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26264592","title":"RNA polymerase II CTD phospho-sites Ser5 and Ser7 govern phosphate homeostasis in fission yeast.","citation":"RNA 2015 Oct;21(10):1770-80","abstract":"Phosphorylation of the tandem YSPTSPS repeats of the RNA polymerase II CTD inscribes an informational code that orchestrates eukaryal mRNA synthesis. Here we interrogate the role of the CTD in phosphate homeostasis in fission yeast. Expression of Pho1 acid phosphatase, which is repressed during growth in phosphate-rich medium and induced by phosphate starvation, is governed strongly by CTD phosphorylation status, but not by CTD repeat length. Inability to place a Ser7-PO4 mark (as in S7A) results in constitutive derepression of Pho1 expression in phosphate-replete medium. In contrast, indelible installation of a Ser7-PO4 mimetic (as in S7E) hyper-represses Pho1 in phosphate-replete cells and inhibits Pho1 induction during starvation. Pho1 phosphatase is derepressed by ablation of the CTD Ser5-PO4 mark, achieved either by mutating Ser5 in all consensus heptads to alanine, or replacing all Pro6 residues with alanine. We find that Ser5 status is a tunable determinant of Pho1 regulation, i.e., serial decrements in the number of consensus Ser5 heptads from seven to two elicits a progressive increase in Pho1 expression in phosphate-replete medium. Pho1 is also derepressed by hypomorphic mutations of the CTD kinase Cdk9. Inactivation of the CTD phosphatase Ssu72 attenuates Pho1 induction in wild-type cells and blocks Pho1 derepression in S7A cells. These experiments implicate Ser5, Pro6, and Ser7 as component letters of a CTD coding \"word\" that transduces a repressive transcriptional signal via serine phosphorylation.","doi":"10.1261/rna.052555.115","authors":"Schwer B, Sanchez AM, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2015-08-13","publication_year":"2015","canto_session_key":"bb24b96b242a33a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2024-02-28 15:20:48","canto_approved_date":"2024-05-13 13:03:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-27 17:15:07","canto_added_date":"2015-08-14 00:19:35","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":77,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.06c","SPAC3G9.04","SPBC28F2.12","SPNCRNA.1712","SPAC1F3.01","SPBP4G3.02","SPBC32H8.10","SPBC27B12.11c","SPBC8E4.01c"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2024-02-28"},{"uniquename":"PMID:37043046","title":"An essential role for the Ino80 chromatin remodeling complex in regulation of gene expression during cellular quiescence.","citation":"Chromosome Res 2023 Apr 12;31(2):14","abstract":"Cellular quiescence is an important physiological state both in unicellular and multicellular eukaryotes. Quiescent cells are halted for proliferation and stop the cell cycle at the G 0  stage. Using fission yeast as a model organism, we have previously found that several subunits of a conserved chromatin remodeling complex, Ino80C (INOsitol requiring nucleosome remodeling factor), are required for survival in quiescence. Here, we demonstrate that Ino80C has a key function in the regulation of gene expression in G 0  cells. We show that null mutants for two Ino80C subunits, Iec1 and Ies2, a putative subunit Arp42, a null mutant for the histone variant H2A.Z, and a null mutant for the Inositol kinase Asp1 have very similar phenotypes in quiescence. These mutants show reduced transcription genome-wide and specifically fail to activate 149 quiescence genes, of which many are localized to the subtelomeric regions. Using spike in normalized ChIP-seq experiments, we show that there is a global reduction of H2A.Z levels in quiescent wild-type cells but not in iec1∆ cells and that a subtelomeric chromosome boundary element is strongly affected by Ino80C. Based on these observations, we propose a model in which Ino80C is evicting H2A.Z from chromatin in quiescent cells, thereby inactivating the subtelomeric boundary element, leading to a reorganization of the chromosome structure and activation of genes required to survive in quiescence.","doi":"10.1007/s10577-023-09723-x","authors":"Zahedi Y, Zeng S, Ekwall K","authors_abbrev":"Zahedi Y et al.","pubmed_publication_date":"12 Apr 2023","pubmed_entrez_date":"2023-04-12","publication_year":"2023","canto_session_key":"d1a4145ce0a5ee2d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-04-13 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:D89106","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11359920","title":"Regulation of initiation of S phase, replication checkpoint signaling, and maintenance of mitotic chromosome structures during S phase by Hsk1 kinase in the fission yeast.","citation":"Mol Biol Cell 2001 May;12(5):1257-74","abstract":"Hsk1, Saccharomyces cerevisiae Cdc7-related kinase in Shizosaccharomyces pombe, is required for G1/S transition and its kinase activity is controlled by the regulatory subunit Dfp1/Him1. Analyses of a newly isolated temperature-sensitive mutant, hsk1-89, reveal that Hsk1 plays crucial roles in DNA replication checkpoint signaling and maintenance of proper chromatin structures during mitotic S phase through regulating the functions of Rad3 (ATM)-Cds1 and Rad21 (cohesin), respectively, in addition to expected essential roles for initiation of mitotic DNA replication through phosphorylating Cdc19 (Mcm2). Checkpoint defect in hsk1-89 is indicated by accumulation of cut cells at 30 degrees C. hsk1-89 displays synthetic lethality in combination with rad3 deletion, indicating that survival of hsk1-89 depends on Rad3-dependent checkpoint pathway. Cds1 kinase activation, which normally occurs in response to early S phase arrest by nucleotide deprivation, is largely impaired in hsk1-89. Furthermore, Cds1-dependent hyperphosphorylation of Dfp1 in response to hydroxyurea arrest is eliminated in hsk1-89, suggesting that sufficient activation of Hsk1-Dfp1 kinase is required for S phase entry and replication checkpoint signaling. hsk1-89 displays apparent defect in mitosis at 37 degrees C leading to accumulation of cells with near 2C DNA content and with aberrant nuclear structures. These phenotypes are similar to those of rad21-K1 and are significantly enhanced in a hsk1-89 rad21-K1 double mutant. Consistent with essential roles of Rad21 as a component for the cohesin complex, sister chromatid cohesion is partially impaired in hsk1-89, suggesting a possibility that infrequent origin firing of the mutant may affect the cohesin functions during S phase.","authors":"Takeda T, Ogino K, Tatebayashi K, Ikeda H, Arai Ki, Masai H","authors_abbrev":"Takeda T et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-22","publication_year":"2001","canto_session_key":"51ea31a1f9fbdb80","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-11-13 10:35:01","canto_approved_date":"2022-01-04 09:48:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-03 15:38:30","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":40,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.12c","SPCC1259.13","SPBC16A3.11","SPCC18B5.11c","SPAC1F7.05","SPCC338.17c","SPAC24H6.05","SPBC14C8.07c","SPBC4.04c","SPBC216.05","SPCC550.13","SPCC16A11.17"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2018-11-13"},{"uniquename":"PMID:20129049","title":"Nuclear poly(a)-binding proteins and nuclear degradation: take the mRNA and run?","citation":"Mol Cell 2010 Jan 15;37(1):3-5","abstract":"Recent work from Lemay et al. (2010) in this issue of Molecular Cell reveals a role for a nuclear poly(A)-binding protein in promoting degradation of small nucleolar RNAs (snoRNAs) by the nuclear exosome.","doi":"10.1016/j.molcel.2009.12.029","authors":"Libri D","authors_abbrev":"Libri D","pubmed_publication_date":"15 Jan 2010","pubmed_entrez_date":"2010-02-05","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14723223","title":"Sulphate metabolism of selenate-resistant Schizosaccharomyces pombe mutants.","citation":"J Gen Appl Microbiol 2003 Oct;49(5):271-8","abstract":"Selenate-resistant mutants were obtained from several strains of Schizosaccharomyces pombe. The obtained mutants all belonged to the same genetic complementation group. They were low in sulphate uptake activity and in ATP sulphurylase activity. They grew on medium containing sulphite, thiosulphate, cysteine or glutathione but not methionine as the sole source of sulphur. From these results, the mutants were concluded to carry mutations in the ATP sulphurylase gene. Inability of the mutants to utilize methionine as a sulphur source is rationalized by the absence of the reverse transsulphurylation pathway in this organism; wild type strains must utilize methionine as a sulphur source after it is degraded to give rise to sulphate.","authors":"Bánszky L, Simonics T, Maráz A","authors_abbrev":"Bánszky L et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2004-01-16","publication_year":"2003","canto_session_key":"f0a7d941bbb343e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-15 16:12:46","canto_approved_date":"2024-08-01 15:48:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-04 17:29:05","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-15"},{"uniquename":"PMID:23211526","title":"Cdc42 oscillations in yeasts.","citation":"Sci Signal 2012 Dec 04;5(253):pe53","abstract":"A fundamental problem in cell biology is how cells define one or several discrete sites of polarity. Through mechanisms involving positive and negative feedback, the small Rho-family guanosine triphosphatase Cdc42 breaks symmetry in round budding yeast cells to define a single site of polarized cell growth. However, it is not clear how cells can define multiple sites of polarization concurrently. We discuss a study in which rod-shaped fission yeast cells, which naturally polarize growth at their two cell ends, exhibited oscillations of Cdc42 activity between these sites. We compare these findings with similar oscillatory behavior of Cdc42 detected in budding yeast cells and discuss the possible mechanism and functional outputs of these oscillations.","doi":"10.1126/scisignal.2003630","authors":"Bendezú FO, Martin SG","authors_abbrev":"Bendezú FO et al.","pubmed_publication_date":"04 Dec 2012","pubmed_entrez_date":"2012-12-06","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20421495","title":"RNAi and heterochromatin repress centromeric meiotic recombination.","citation":"Proc Natl Acad Sci U S A 2010 May 11;107(19):8701-5","abstract":"During meiosis, the formation of viable haploid gametes from diploid precursors requires that each homologous chromosome pair be properly segregated to produce an exact haploid set of chromosomes. Genetic recombination, which provides a physical connection between homologous chromosomes, is essential in most species for proper homologue segregation. Nevertheless, recombination is repressed specifically in and around the centromeres of chromosomes, apparently because rare centromeric (or pericentromeric) recombination events, when they do occur, can disrupt proper segregation and lead to genetic disabilities, including birth defects. The basis by which centromeric meiotic recombination is repressed has been largely unknown. We report here that, in fission yeast, RNAi functions and Clr4-Rik1 (histone H3 lysine 9 methyltransferase) are required for repression of centromeric recombination. Surprisingly, one mutant derepressed for recombination in the heterochromatic mating-type region during meiosis and several mutants derepressed for centromeric gene expression during mitotic growth are not derepressed for centromeric recombination during meiosis. These results reveal a complex relation between types of repression by heterochromatin. Our results also reveal a previously undemonstrated role for RNAi and heterochromatin in the repression of meiotic centromeric recombination and, potentially, in the prevention of birth defects by maintenance of proper chromosome segregation during meiosis.","doi":"10.1073/pnas.0914160107","authors":"Ellermeier C, Higuchi EC, Phadnis N, Holm L, Geelhood JL, Thon G, Smith GR","authors_abbrev":"Ellermeier C et al.","pubmed_publication_date":"11 May 2010","pubmed_entrez_date":"2010-04-28","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c","SPCC188.13c","SPBC800.03","SPAC25G10.04c","SPAC664.01c","SPAC17A5.11","SPBC16C6.10","SPBC29A10.14"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:22020225","title":"Fungal Smn and Spf30 homologues are mainly present in filamentous fungi and genomes with many introns: implications for spinal muscular atrophy.","citation":"Gene 2012 Jan 10;491(2):135-41","abstract":"Spinal muscular atrophy is an important rare genetic disease characterized by the loss of motor neurons, where the main gene responsible is smn1. Orthologous genes have only been characterized in a single fungal genome: Schizosaccharomyces pombe. We have searched for putative SMN orthologues in publically available fungal genomes, finding that they are predominately present in filamentous fungi. SMN binding partners and the SPF30 SMN paralogue, which are all involved in mRNA splicing, were found to be present in a similar but non-identical subset of fungal genomes. The Saccharomycces cerevisiae yeast genome contains neither smn1 orthologues nor paralogues and it has been suggested that this might be related to the low number of introns in this yeast. Here we have tested this hypothesis by looking at other fungal genomes. Significantly, we find that fungal genomes with high numbers of introns also possess an SMN orthologue or at least its paralogue, SPF30.","doi":"10.1016/j.gene.2011.10.006","authors":"Mier P, Pérez-Pulido AJ","authors_abbrev":"Mier P et al.","pubmed_publication_date":"10 Jan 2012","pubmed_entrez_date":"2011-10-25","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12084712","title":"Mus81-Eme1 and Rqh1 involvement in processing stalled and collapsed replication forks.","citation":"J Biol Chem 2002 Sep 06;277(36):32753-9","abstract":"The processing of stalled replication forks and the repair of collapsed replication forks are essential functions in all organisms. In fission yeast DNA junctions at stalled replication forks appear to be processed by either the Rqh1 DNA helicase or Mus81-Eme1 endonuclease. Accordingly, we show that the hypersensitivity to agents that cause replication fork stalling of mus81, eme1, and rqh1 mutants is suppressed by a Holliday junction resolvase (RusA), as is the synthetic lethality of a mus81(-) rqh1(-) double mutant. Recombinant Mus81-Eme1, purified from Escherichia coli, readily cleaves replication fork structures but cleaves synthetic Holliday junctions relatively poorly in vitro. From these data we propose that Mus81-Eme1 can process stalled replication forks before they have regressed to form a Holliday junction. We also implicate Mus81-Eme1 and Rqh1 in the repair of collapsed replication forks. Here Mus81-Eme1 and Rqh1 seem to function on different substrates because RusA can substitute for Mus81-Eme1 but not Rqh1.","authors":"Doe CL, Ahn JS, Dixon J, Whitby MC","authors_abbrev":"Doe CL et al.","pubmed_publication_date":"06 Sep 2002","pubmed_entrez_date":"2002-06-27","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPAPB1E7.06c","SPCC4G3.05c","SPBC1703.14c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:16243027","title":"Telomere binding protein Taz1 establishes Swi6 heterochromatin independently of RNAi at telomeres.","citation":"Curr Biol 2005 Oct 25;15(20):1808-19","abstract":"The telomere is a specialized heterochromatin conserved among eukaryotes. However, it remains unknown how heterochromatin protein 1 (HP1) is recruited to telomeres and how telomere heterochromatin is formed. In fission yeast, the RNAi (RNA interference)-RITS (RNA-induced initiation of transcriptional silencing) pathway initiates heterochromatin formation at the centromeres and the silent mat locus by using common DNA sequences, the dg and dh repeats, as the templates for small interfering RNA (siRNA).\nWe found that telomeric repeats are sufficient for the establishment of Swi6 (a fission-yeast HP1 homolog) heterochromatin, and the establishment requires Taz1, a telomere binding protein of the TRF family. Additionally, Swi6 heterochromatin is established by a part of the subtelomere that contains sequences highly homologous to that of the dh repeat, and it is strikingly destabilized by the deletion of both Taz1 and RNAi-RITS. Transcripts from the telomeric dh-homologous region were specifically associated with RITS, and deletion of the telomeric dh-homologous region showed the phenotype similar to that of the rnai mutant in terms of the telomeric silencing, indicating that the RNAi-RITS pathway acts at the telomeric dh-homologous region to establish Swi6 heterochromatin. Furthermore, we found that Taz1 establishes Swi6 heterochromatin independently of the telomeric repeats and the RNAi-RITS pathway at the subtelomeres.\nThe telomere heterochromatin is regulated by at least two factors: One is Taz1, which is telomere specific, and the other is RNAi-RITS, which is commonly used at the constitutive heterochromatin regions.","authors":"Kanoh J, Sadaie M, Urano T, Ishikawa F","authors_abbrev":"Kanoh J et al.","pubmed_publication_date":"25 Oct 2005","pubmed_entrez_date":"2005-10-26","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011508","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28272970","title":"Wee1 and Cdc25: Tools, pathways, mechanisms, questions.","citation":"Cell Cycle 2017 Apr 03;16(7):599-600","abstract":"","doi":"10.1080/15384101.2017.1302229","authors":"Moseley JB","authors_abbrev":"Moseley JB","pubmed_publication_date":"03 Apr 2017","pubmed_entrez_date":"2017-03-09","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-03-10 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:28924043","title":"Dynamic regulation of Cdr1 kinase localization and phosphorylation during osmotic stress.","citation":"J Biol Chem 2017 Nov 10;292(45):18457-18468","abstract":"Environmental conditions modulate cell cycle progression in many cell types. A key component of the eukaryotic cell cycle is the protein kinase Wee1, which inhibits the cyclin-dependent kinase Cdk1 in yeast through human cells. In the fission yeast  Schizosaccharomyces pombe , the protein kinase Cdr1 is a mitotic inducer that promotes mitotic entry by phosphorylating and inhibiting Wee1. Cdr1 and Wee1 both localize to punctate structures, termed nodes, on the medial cortex, but it has been unknown whether node localization can be altered by physiological signals. Here we investigated how environmental conditions regulate Cdr1 signaling for cell division. Osmotic stress induced hyperphosphorylation of the mitotic inducer Cdr1 for several hours, and cells delayed division for the same time period. This stress-induced hyperphosphorylation required both Cdr1 autophosphorylation and the stress-activated protein kinase Sty1. During osmotic stress, Cdr1 exited cortical nodes and localized in the cytoplasm. Using a series of truncation mutants, we mapped a C-terminal domain that is necessary and sufficient for Cdr1 node localization and found that Sty1 directly phosphorylates this domain  in vitro  Sty1 was not required for Cdr1 exit from nodes, indicating the existence of additional regulatory signals. Both Cdr1 phosphorylation and node localization returned to basal levels when cells adapted to osmotic conditions and resumed cell cycle progression. In summary, we identified a mechanism that prevents Cdr1 colocalization with its inhibitory target Wee1 during osmotic stress. Dynamic regulation of protein localization to cortical nodes might represent a strategy to modulate entry into mitosis under differing environmental conditions.","doi":"10.1074/jbc.M117.793034","authors":"Opalko HE, Moseley JB","authors_abbrev":"Opalko HE et al.","pubmed_publication_date":"10 Nov 2017","pubmed_entrez_date":"2017-09-20","publication_year":"2017","canto_session_key":"d1eebaf912739707","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hannah Opalko","canto_first_approved_date":"2018-11-02 16:34:25","canto_approved_date":"2025-09-03 15:08:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-23 17:43:54","canto_added_date":"2017-09-21 00:15:13","annotation_curators":[{"name":"Hannah Opalko","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":30,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.08","SPAC644.06c","SPAC57A10.02","SPAC24B11.06c","SPCC18B5.03"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-11-02"},{"uniquename":"PMID:22537629","title":"Replication: DNA building block synthesis on demand.","citation":"Curr Biol 2012 Apr 24;22(8):R271-2","abstract":"Correct regulation of DNA nucleotide biosynthesis is emerging as a key issue of importance for genome integrity. The fission yeast Spd1 protein can modulate the activity of ribonucleotide reductase (RNR) by at least three different mechanisms. Now a paper reports that Spd1 turnover is linked to ongoing DNA synthesis.","doi":"10.1016/j.cub.2012.03.019","authors":"Holmberg C, Nielsen O","authors_abbrev":"Holmberg C et al.","pubmed_publication_date":"24 Apr 2012","pubmed_entrez_date":"2012-04-28","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32204793","title":"Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex.","citation":"Elife 2020 Mar 24;9","abstract":"Although Rad51 is the key protein in homologous recombination (HR), a major DNA double-strand break repair pathway, several auxiliary factors interact with Rad51 to promote productive HR. We present an interdisciplinary characterization of the interaction between Rad51 and Swi5-Sfr1, a conserved auxiliary factor. Two distinct sites within the intrinsically disordered N-terminus of Sfr1 (Sfr1N) were found to cooperatively bind Rad51. Deletion of this domain impaired Rad51 stimulation in vitro and rendered cells sensitive to DNA damage. By contrast, amino acid-substitution mutants, which had comparable biochemical defects, could promote DNA repair, suggesting that Sfr1N has another role in addition to Rad51 binding. Unexpectedly, the DNA repair observed in these mutants was dependent on Rad55-Rad57, another auxiliary factor complex hitherto thought to function independently of Swi5-Sfr1. When combined with the finding that they form a higher-order complex, our results imply that Swi5-Sfr1 and Rad55-Rad57 can collaboratively stimulate Rad51 in  Schizosaccharomyces pombe .","doi":"10.7554/eLife.52566","authors":"Argunhan B, Sakakura M, Afshar N, Kurihara M, Ito K, Maki T, Kanamaru S, Murayama Y, Tsubouchi H, Takahashi M, Takahashi H, Iwasaki H","authors_abbrev":"Argunhan B et al.","pubmed_publication_date":"24 Mar 2020","pubmed_entrez_date":"2020-03-25","publication_year":"2020","canto_session_key":"616a9b2185a857ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Bilge Argunhan","canto_first_approved_date":"2020-04-23 10:03:41","canto_approved_date":"2025-07-02 05:53:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-17 06:14:59","canto_added_date":"2020-03-26 01:15:03","annotation_curators":[{"name":"Bilge Argunhan","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.07","SPAC20H4.07","SPAC644.14c","SPAC3C7.03c","SPBC409.03"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-04-23"},{"uniquename":"PMID:21684186","title":"Deciphering the RNA polymerase II CTD code in fission yeast.","citation":"Mol Cell 2011 Jul 22;43(2):311-8","abstract":"The RNA polymerase II carboxy-terminal domain (CTD) consists of tandem Y(1)S(2)P(3)T(4)S(5)P(6)S(7) repeats. Dynamic remodeling of the CTD, especially its serine phosphorylation pattern, conveys informational cues about the transcription apparatus to a large ensemble of CTD-binding proteins. Our genetic dissection of fission yeast CTD function provides insights to the \"CTD code.\" Two concepts stand out. First, the Ser2 requirement for transcription during sexual differentiation is bypassed by subtracting Ser7, signifying that imbalance in the phosphorylation array, not absence of a phospho-CTD cue, underlies a CTD-associated pathology. Second, the essentiality of Ser5 for vegetative growth is circumvented by covalently tethering mRNA capping enzymes to the CTD, thus proving that capping enzyme recruitment is a chief function of the Ser5-PO(4) mark. This illustrates that a key \"letter\" in the CTD code can be neutralized by delivering its essential cognate receptor to the transcription complex via an alternative route.","doi":"10.1016/j.molcel.2011.05.024","authors":"Schwer B, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"22 Jul 2011","pubmed_entrez_date":"2011-06-21","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37767365","title":"2A peptide from ERBV-1 efficiently separates endogenous protein domains in the fission yeast  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2023;2023","abstract":"2A peptides are widely used for polycistronic gene expression from vectors. In contrast, the separation of endogenous genes via 2A peptides has been largely unexplored. We show that in fission yeast  Schizosaccharomyces pombe  , the \"cleaving\" efficiency of the 2A peptide from ERBV-1 (Equine rhinitis B virus 1) range from ~70% to ~99% for End4 at different insertion sites. Our results suggest a high \"cleaving\" efficiency as well as considerable variation for using 2A peptide to separate endogenous protein domains in fission yeast. Verification of the \"cleaving\" efficiency of 2A peptides is advised for its application.","doi":"10.17912/micropub.biology.000941","authors":"Ren Y, Lin Q, Berro J","authors_abbrev":"Ren Y et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-09-28","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-09-28 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27901072","title":"Characterisation of functional domains in fission yeast Ams2 that are required for core histone gene transcription.","citation":"Sci Rep 2016 Nov 30;6:38111","abstract":"Histone gene expression is regulated in a cell cycle-dependent manner, with a peak at S phase, which is crucial for cell division and genome integrity. However, the detailed mechanisms by which expression of histone genes are tightly regulated remain largely unknown. Fission yeast Ams2, a GATA-type zinc finger motif-containing factor, is required for activation of S phase-specific core histone gene transcription. Here we report the molecular characterisation of Ams2. We show that the zinc finger motif in Ams2 is necessary to bind the histone gene promoter region and to activate histone gene transcription. An N-terminal region of Ams2 acts as a self-interaction domain. Intriguingly, N-terminally truncated Ams2 binds to the histone gene promoters, but does not fully activate histone gene transcription. These observations imply that Ams2 self-interactions are required for efficient core histone gene transcription. Moreover, we show that Ams2 interacts with Teb1, which itself binds to the core histone gene promoters. We discuss the relationships between Ams2 domains and efficient transcription of the core histone genes in fission yeast.","doi":"10.1038/srep38111","authors":"Takayama Y, Shirai M, Masuda F","authors_abbrev":"Takayama Y et al.","pubmed_publication_date":"30 Nov 2016","pubmed_entrez_date":"2016-12-01","publication_year":"2016","canto_session_key":"b33dcb999a87be71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-07 13:24:21","canto_approved_date":"2026-01-29 14:03:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-07 13:24:02","canto_added_date":"2016-12-03 01:15:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":59,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC550.13","SPBC1105.11c","SPAC13G7.10","SPAC1834.03c","SPAC1834.04","SPBC8D2.03c","SPCC622.09","SPCC622.08c","SPBC1105.17","SPCC290.04","SPBC1105.12","SPBC8D2.04"],"gene_count":12,"ltp_gene_count":4,"approved_date":"2018-03-07"},{"uniquename":"PMID:28717002","title":"Human ribonuclease H1 resolves R-loops and thereby enables progression of the DNA replication fork.","citation":"J Biol Chem 2017 Sep 15;292(37):15216-15224","abstract":"Faithful DNA replication is essential for genome stability. To ensure accurate replication, numerous complex and redundant replication and repair mechanisms function in tandem with the core replication proteins to ensure DNA replication continues even when replication challenges are present that could impede progression of the replication fork. A unique topological challenge to the replication machinery is posed by RNA-DNA hybrids, commonly referred to as R-loops. Although R-loops play important roles in gene expression and recombination at immunoglobulin sites, their persistence is thought to interfere with DNA replication by slowing or impeding replication fork progression. Therefore, it is of interest to identify DNA-associated enzymes that help resolve replication-impeding R-loops. Here, using DNA fiber analysis, we demonstrate that human ribonuclease H1 (RNH1) plays an important role in replication fork movement in the mammalian nucleus by resolving R-loops. We found that RNH1 depletion results in accumulation of RNA-DNA hybrids, slowing of replication forks, and increased DNA damage. Our data uncovered a role for RNH1 in global DNA replication in the mammalian nucleus. Because accumulation of RNA-DNA hybrids is linked to various human cancers and neurodegenerative disorders, our study raises the possibility that replication fork progression might be impeded, adding to increased genomic instability and contributing to disease.","doi":"10.1074/jbc.M117.787473","authors":"Parajuli S, Teasley DC, Murali B, Jackson J, Vindigni A, Stewart SA","authors_abbrev":"Parajuli S et al.","pubmed_publication_date":"15 Sep 2017","pubmed_entrez_date":"2017-07-19","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21511999","title":"Comparative functional genomics of the fission yeasts.","citation":"Science 2011 May 20;332(6032):930-6","abstract":"The fission yeast clade--comprising Schizosaccharomyces pombe, S. octosporus, S. cryophilus, and S. japonicus--occupies the basal branch of Ascomycete fungi and is an important model of eukaryote biology. A comparative annotation of these genomes identified a near extinction of transposons and the associated innovation of transposon-free centromeres. Expression analysis established that meiotic genes are subject to antisense transcription during vegetative growth, which suggests a mechanism for their tight regulation. In addition, trans-acting regulators control new genes within the context of expanded functional modules for meiosis and stress response. Differences in gene content and regulation also explain why, unlike the budding yeast of Saccharomycotina, fission yeasts cannot use ethanol as a primary carbon source. These analyses elucidate the genome structure and gene regulation of fission yeast and provide tools for investigation across the Schizosaccharomyces clade.","doi":"10.1126/science.1203357","authors":"Rhind N, Chen Z, Yassour M, Thompson DA, Haas BJ, Habib N, Wapinski I, Roy S, Lin MF, Heiman DI, Young SK, Furuya K, Guo Y, Pidoux A, Chen HM, Robbertse B, Goldberg JM, Aoki K, Bayne EH, Berlin AM, Desjardins CA, Dobbs E, Dukaj L, Fan L, FitzGerald MG, French C, Gujja S, Hansen K, Keifenheim D, Levin JZ, Mosher RA, Müller CA, Pfiffner J, Priest M, Russ C, Smialowska A, Swoboda P, Sykes SM, Vaughn M, Vengrova S, Yoder R, Zeng Q, Allshire R, Baulcombe D, Birren BW, Brown W, Ekwall K, Kellis M, Leatherwood J, Levin H, Margalit H, Martienssen R, Nieduszynski CA, Spatafora JW, Friedman N, Dalgaard JZ, Baumann P, Niki H, Regev A, Nusbaum C","authors_abbrev":"Rhind N et al.","pubmed_publication_date":"20 May 2011","pubmed_entrez_date":"2011-04-23","publication_year":"2011","canto_session_key":"b6d009e44fd8353e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-23 17:56:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-06 12:10:32","canto_added_date":"2012-02-24 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conservation of organisation and function between nonhomologous regional centromeres.","citation":"Nat Commun 2019 May 28;10(1):2343","abstract":"Despite the conserved essential function of centromeres, centromeric DNA itself is not conserved. The histone-H3 variant, CENP-A, is the epigenetic mark that specifies centromere identity. Paradoxically, CENP-A normally assembles on particular sequences at specific genomic locations. To gain insight into the specification of complex centromeres, here we take an evolutionary approach, fully assembling genomes and centromeres of related fission yeasts. Centromere domain organization, but not sequence, is conserved between Schizosaccharomyces pombe, S. octosporus and S. cryophilus with a central CENP-A Cnp1  domain flanked by heterochromatic outer-repeat regions. Conserved syntenic clusters of tRNA genes and 5S rRNA genes occur across the centromeres of S. octosporus and S. cryophilus, suggesting conserved function. Interestingly, nonhomologous centromere central-core sequences from S. octosporus and S. cryophilus are recognized in S. pombe, resulting in cross-species establishment of CENP-A Cnp1  chromatin and functional kinetochores. Therefore, despite the lack of sequence conservation, Schizosaccharomyces centromere DNA possesses intrinsic conserved properties that promote assembly of CENP-A chromatin.","doi":"10.1038/s41467-019-09824-4","authors":"Tong P, Pidoux AL, Toda NRT, Ard R, Berger H, Shukla M, Torres-Garcia J, Müller CA, Nieduszynski CA, Allshire RC","authors_abbrev":"Tong P et al.","pubmed_publication_date":"28 May 2019","pubmed_entrez_date":"2019-05-30","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-05-31 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10357655","title":"[Phylogenetic preservation of genetic study stocks of Schizosaccharomyces pombe].","citation":"Tanpakushitsu Kakusan Koso 1999 Mar;44(3):282-4","abstract":"","authors":"Shimoda C","authors_abbrev":"Shimoda C","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-06-05","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31978045","title":"Optogenetics reveals Cdc42 local activation by scaffold-mediated positive feedback and Ras GTPase.","citation":"PLoS Biol 2020 Jan;18(1):e3000600","abstract":"Local activity of the small GTPase Cdc42 is critical for cell polarization. Whereas scaffold-mediated positive feedback was proposed to break symmetry of budding yeast cells and produce a single zone of Cdc42 activity, the existence of similar regulation has not been probed in other organisms. Here, we address this problem using rod-shaped cells of fission yeast Schizosaccharomyces pombe, which exhibit zones of active Cdc42-GTP at both cell poles. We implemented the CRY2-CIB1 optogenetic system for acute light-dependent protein recruitment to the plasma membrane, which allowed to directly demonstrate positive feedback. Indeed, optogenetic recruitment of constitutively active Cdc42 leads to co-recruitment of the guanine nucleotide exchange factor (GEF) Scd1 and endogenous Cdc42, in a manner dependent on the scaffold protein Scd2. We show that Scd2 function is dispensable when the positive feedback operates through an engineered interaction between the GEF and a Cdc42 effector, the p21-activated kinase 1 (Pak1). Remarkably, this rewired positive feedback confers viability and allows cells to form 2 zones of active Cdc42 even when otherwise essential Cdc42 activators are lacking. These cells further revealed that the small GTPase Ras1 plays a role in both localizing the GEF Scd1 and promoting its activity, which potentiates the positive feedback. We conclude that scaffold-mediated positive feedback, gated by Ras activity, confers robust polarization for rod-shape formation.","doi":"10.1371/journal.pbio.3000600","authors":"Lamas I, Merlini L, Vještica A, Vincenzetti V, Martin SG","authors_abbrev":"Lamas I et al.","pubmed_publication_date":"Jan 2020","pubmed_entrez_date":"2020-01-25","publication_year":"2020","canto_session_key":"cb3e2a895f69824b","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-05-22 21:25:15","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2170949","title":"Nucleotide sequence of S. pombe inorganic pyrophosphatase.","citation":"Nucleic Acids Res 1990 Oct 11;18(19):5888","abstract":"","authors":"Kawasaki I, Adachi N, Ikeda H","authors_abbrev":"Kawasaki I et al.","pubmed_publication_date":"11 Oct 1990","pubmed_entrez_date":"1990-10-11","publication_year":"1990","canto_session_key":"573c1e9eb1c16c66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 22:13:11","canto_approved_date":"2019-01-07 22:13:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 22:12:52","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:5338970","title":"Growth of the fission yeast, Schizosaccharomyces pombe, with late, eccentric, lytic fission in an unbalanced medium.","citation":"J Bacteriol 1967 Jul;94(1):192-5","abstract":"Growth of Schizosaccharomyces pombe in batch cultures in a commercial defined medium was found to be normal until the last generation before the stationary phase. Approximately one-half the progeny of the last division lysed. Lysis occurred at breaks in the cell wall at cell-plates whose fission was eccentric. Normal culture cycle patterns were obtained when the medium was balanced by addition of either 0.20 mg of l-asparagine per ml or 5.0 mg of KH(2)PO(4) per ml, or both. The lytic effect of growth in the unbalanced medium was compared with similar effects of growth in 2-deoxyglucose. These studies with 2-deoxyglucose in the balanced medium confirmed earlier cytological observations (lysis at all growing points), but showed that the similarities were superficial.","authors":"Johnson BF","authors_abbrev":"Johnson BF","pubmed_publication_date":"Jul 1967","pubmed_entrez_date":"1967-07-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28555368","title":"A mutated dph3 gene causes sensitivity of Schizosaccharomyces pombe cells to cytotoxic agents.","citation":"Curr Genet 2017 Dec;63(6):1081-1091","abstract":"Dph3 is involved in diphthamide modification of the eukaryotic translation elongation factor eEF2 and in Elongator-mediated modifications of tRNAs, where a 5-methoxycarbonyl-methyl moiety is added to wobble uridines. Lack of such modifications affects protein synthesis due to inaccurate translation of mRNAs at ribosomes. We have discovered that integration of markers at the msh3 locus of Schizosaccharomyces pombe impaired the function of the nearby located dph3 gene. Such integrations rendered cells sensitive to the cytotoxic drugs hydroxyurea and methyl methanesulfonate. We constructed dph3 and msh3 strains with mutated ATG start codons (ATGmut), which allowed investigating drug sensitivity without potential interference by marker insertions. The dph3-ATGmut and a dph3::loxP-ura4-loxM gene disruption strain, but not msh3-ATGmut, turned out to be sensitive to hydroxyurea and methyl methanesulfonate, likewise the strains with cassettes integrated at the msh3 locus. The fungicide sordarin, which inhibits diphthamide modified eEF2 of Saccharomyces cerevisiae, barely affected survival of wild type and msh3Δ S. pombe cells, while the dph3Δ mutant was sensitive. The msh3-ATG mutation, but not dph3Δ or the dph3-ATG mutation caused a defect in mating-type switching, indicating that the ura4 marker at the dph3 locus did not interfere with Msh3 function. We conclude that Dph3 is required for cellular resistance to the fungicide sordarin and to the cytotoxic drugs hydroxyurea and methyl methanesulfonate. This is likely mediated by efficient translation of proteins in response to DNA damage and replication stress.","doi":"10.1007/s00294-017-0711-x","authors":"Villahermosa D, Knapp K, Fleck O","authors_abbrev":"Villahermosa D et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-05-31","publication_year":"2017","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-06-01 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20948174","title":"The selective elimination of messenger RNA underlies the mitosis-meiosis switch in fission yeast.","citation":"Proc Jpn Acad Ser B Phys Biol Sci 2010;86(8):788-97","abstract":"The cellular programs for meiosis and mitosis must be strictly distinguished but the mechanisms controlling the entry to meiosis remain largely elusive in higher organisms. In contrast, recent analyses in yeast have shed new light on the mechanisms underlying the mitosis-meiosis switch. In this review, the current understanding of these mechanisms in the fission yeast Schizosaccharomyces pombe is discussed. Meiosis-inducing signals in this microbe emanating from environmental conditions including the nutrient status converge on the activity of an RRM-type RNA-binding protein, Mei2. This protein plays pivotal roles in both the induction and progression of meiosis and has now been found to govern the meiotic program in a quite unexpected manner. Fission yeast contains an RNA degradation system that selectively eliminates meiosis-specific mRNAs during the mitotic cell cycle. Mmi1, a novel RNA-binding protein of the YTH-family, is essential for this process. Mei2 tethers Mmi1 and thereby stabilizes the transcripts necessary for the progression of meiosis.","authors":"Yamamoto M","authors_abbrev":"Yamamoto M","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-10-16","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1372994","title":"p107wee1 is a dual-specificity kinase that phosphorylates p34cdc2 on tyrosine 15.","citation":"Proc Natl Acad Sci U S A 1992 Apr 01;89(7):2917-21","abstract":"p107wee1 is a protein kinase that functions as a dose-dependent inhibitor of mitosis through its interactions with p34cdc2 in Schizosaccharomyces pombe. To characterize the kinase activity of p107wee1, its carboxyl-terminal catalytic domain was purified to homogeneity from overproducing insect cells. The apparent molecular mass of the purified protein (p37wee1KD) was determined to be approximately 37 kDa by gel filtration, consistent with it being a monomer. Serine and tyrosine kinase activities cofiltered with p37wee1KD, demonstrating that p107wee1 is a dual-specificity kinase. In vitro, p107wee1 phosphorylated p34cdc2 on Tyr-15 only when p34cdc2 was complexed with cyclin. Neither monomeric p34cdc2 nor a peptide containing Tyr-15 was able to substitute for the p34cdc2/cyclin complex in this assay. Furthermore, the phosphorylation of p34cdc2 by p107wee1 in vitro inhibited the histone H1 kinase activity of p34cdc2. These results indicate that p107wee1 functions as a mitotic inhibitor by directly phosphorylating p34cdc2 on Tyr-15 and that the preferred substrate for phosphorylation is the p34cdc2/cyclin complex.","authors":"Parker LL, Atherton-Fessler S, Piwnica-Worms H","authors_abbrev":"Parker LL et al.","pubmed_publication_date":"01 Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"42f024cd9e96cf6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-03-29 16:53:23","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-04-19 11:27:12","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.14c","SPBC11B10.09","SPCC18B5.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-04-19"},{"uniquename":"PMID:2355921","title":"Cloning and analysis of a gene involved in DNA repair and recombination, the rad1 gene of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1990 Jul;10(7):3750-60","abstract":"We have cloned the rad1 gene of Schizosaccharomyces pombe by complementation of the rad1-1 mutant, which is deficient in DNA repair and recombination. The coding region of the gene is 582 base pairs long and contains no introns. The predicted product is a strongly acidic, 22-kilodalton protein containing 194 amino acid residues. This gene does not exhibit significant homology to any other known repair gene. The major transcription start site is at 27 base pairs upstream of the putative start codon. Insertion mutagenesis revealed that besides the coding region, at least 151 base pairs of 5'-flanking sequence are required for full complementing activity. A strain carrying a null allele of rad1 was constructed and found to have a phenotype closely similar to that of the rad1-1 mutant. Expression in Escherichia coli of the coding region yielded a protein product of a size close to that predicted from the DNA sequence. This product reacted with antibodies raised against a synthetic peptide with a sequence from that predicted for the protein product. We have localized the rad1 gene to NotI fragment E of the S. pombe genome.","authors":"Sunnerhagen P, Seaton BL, Nasim A, Subramani S","authors_abbrev":"Sunnerhagen P et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_session_key":"67c549267bcaf84f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-01-28 17:33:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 12:45:13","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-25"},{"uniquename":"PMID:21113731","title":"The FN3 and BRCT motifs in the exomer component Chs5p define a conserved module that is necessary and sufficient for its function.","citation":"Cell Mol Life Sci 2011 Sep;68(17):2907-17","abstract":"Chs5p is a component of the exomer, a coat complex required to transport the chitin synthase Chs3p from the trans-Golgi network to the plasma membrane. The Chs5p N-terminal region exhibits fibronectin type III (FN3) and BRCT domains. FN3 domains are present in proteins that mediate adhesion processes, whereas BRCT domains are involved in DNA repair. Several fungi--including Schizosaccharomyces pombe, which has no detectable amounts of chitin--have proteins similar to Chs5p. Here we show that the FN3 and BRCT motifs in Chs5p behave as a module that is necessary and sufficient for Chs5p localization and for cargo delivery. The N-terminal regions of S. cerevisiae Chs5p and S. pombe Cfr1p are interchangeable in terms of Golgi localization, but not in terms of exomer assembly, showing that the conserved function of this module is protein retention in this organelle and that the interaction between the exomer components is organism-specific.","doi":"10.1007/s00018-010-0596-z","authors":"Martín-García R, de León N, Sharifmoghadam MR, Curto MÁ, Hoya M, Bustos-Sanmamed P, Valdivieso MH","authors_abbrev":"Martín-García R et al.","pubmed_publication_date":"Sep 2011","pubmed_entrez_date":"2010-11-30","publication_year":"2011","canto_session_key":"a059f85434b62eb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Henar Valdivieso","canto_first_approved_date":"2013-07-02 07:52:52","canto_approved_date":"2025-09-04 09:27:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-24 16:45:17","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Henar Valdivieso","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-07-02"},{"uniquename":"PMID:15568976","title":"Closing mitosis: the functions of the Cdc14 phosphatase and its regulation.","citation":"Annu Rev Genet 2004;38:203-32","abstract":"Completion of the cell cycle requires the temporal and spatial coordination of chromosome segregation with mitotic spindle disassembly and cytokinesis. In budding yeast, the protein phosphatase Cdc14 is a key regulator of these late mitotic events. Here, we review the functions of Cdc14 and how this phosphatase is regulated to accomplish the coupling of mitotic processes. We also discuss the function and regulation of Cdc14 in other eukaryotes, emphasizing conserved features.","authors":"Stegmeier F, Amon A","authors_abbrev":"Stegmeier F et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-12-01","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010843","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23087209","title":"The kinesin-14 Klp2 is negatively regulated by the SIN for proper spindle elongation and telophase nuclear positioning.","citation":"Mol Biol Cell 2012 Dec;23(23):4592-600","abstract":"In Schizosaccharomyces pombe, a late mitotic kinase pathway called the septation initiation network (SIN) triggers cytokinesis. Here we show that the SIN is also involved in regulating anaphase spindle elongation and telophase nuclear positioning via inhibition of Klp2, a minus end-directed kinesin-14. Klp2 is known to localize to microtubules (MTs) and have roles in interphase nuclear positioning, mitotic chromosome alignment, and nuclear migration during karyogamy (nuclear fusion during mating). We observe SIN-dependent disappearance of Klp2 from MTs in anaphase, and we find that this is mediated by direct phosphorylation of Klp2 by the SIN kinase Sid2, which abrogates loading of Klp2 onto MTs by inhibiting its interaction with Mal3 (EB1 homologue). Disruption of Klp2 MT localization is required for efficient anaphase spindle elongation. Furthermore, when cytokinesis is delayed, SIN inhibition of Klp2 acts in concert with microtubules emanating from the equatorial microtubule-organizing center to position the nuclei away from the cell division site. These results reveal novel functions of the SIN in regulating the MT cytoskeleton and suggest that the SIN may have broader functions in regulating cellular organization in late mitosis than previously realized.","doi":"10.1091/mbc.E12-07-0532","authors":"Mana-Capelli S, McLean JR, Chen CT, Gould KL, McCollum D","authors_abbrev":"Mana-Capelli S et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-10-23","publication_year":"2012","canto_session_key":"cd48646c620974e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dannel McCollum","canto_first_approved_date":"2014-08-29 14:04:36","canto_approved_date":"2025-09-04 06:21:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-02 07:19:29","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Dannel McCollum","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPAC1093.06c","SPAC664.10","SPAC18G6.15","SPAC4A8.05c","SPBC19G7.05c","SPAC24B11.11c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2014-08-29"},{"uniquename":"PMID:25831518","title":"Molecular coevolution of a sex pheromone and its receptor triggers reproductive isolation in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 2015 Apr 07;112(14):4405-10","abstract":"The diversification of sex pheromones is regarded as one of the causes of prezygotic isolation that results in speciation. In the fission yeast Schizosaccharomyces pombe, the molecular recognition of a peptide pheromone by its receptor plays an essential role in sexual reproduction. We considered that molecular coevolution of a peptide-mating pheromone, M factor, and its receptor, Map3, might be realized by experimentally diversifying these proteins. Here, we report the successful creation of novel mating-type pairs by searching for map3 suppressor mutations that rescued the sterility of M-factor mutants that were previously isolated. Several strong suppressors were found to also recognize WT M factor. The substituted residues of these Map3 suppressors were mapped to F204, F214, and E249, which are likely to be critical residues for M-factor recognition. These critical residues were systematically substituted with each of the other amino acids by in vitro mutagenesis. Ultimately, we successfully obtained three novel mating-type pairs constituting reproductive groups. These novel mating-type pairs could not conjugate with WT maters. Furthermore, no flow of chromosomally integrated drug-resistance genes occurred between the novel and the WT mating pairs, showing that each experimentally created reproductive group [e.g., M factor(V5H) and Map3(F214H)] was isolated from the WT group. In conclusion, we have succeeded in creating an artificial reproductive group that is isolated from the WT group. In keeping with the biological concept of species, the artificial reproductive group is a new species.","doi":"10.1073/pnas.1501661112","authors":"Seike T, Nakamura T, Shimoda C","authors_abbrev":"Seike T et al.","pubmed_publication_date":"07 Apr 2015","pubmed_entrez_date":"2015-04-02","publication_year":"2015","canto_session_key":"85f3e68940957230","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-06-08 09:42:02","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-06-08 09:41:53","canto_added_date":"2015-04-03 00:18:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":52,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB8E5.05","SPAC3F10.10c","SPBPJ4664.03","SPAC513.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-06-08"},{"uniquename":"PMID:10090724","title":"Association of Chk1 with 14-3-3 proteins is stimulated by DNA damage.","citation":"Genes Dev 1999 Mar 15;13(6):675-85","abstract":"The protein kinase Chk1 is required for cell cycle arrest in response to DNA damage. We have found that the 14-3-3 proteins Rad24 and Rad25 physically interact with Chk1 in fission yeast. Association of Chk1 with 14-3-3 proteins is stimulated in response to DNA damage. DNA damage results in phosphorylation of Chk1 and the 14-3-3 proteins bind preferentially to the phosphorylated form. Genetic analysis has independently implicated both Rad24 and Rad25 in the DNA-damage checkpoint pathway. We suggest that DNA damage-dependent association of phosphorylated Chk1 with 14-3-3 proteins mediates an important step along the DNA-damage checkpoint pathway, perhaps by directing Chk1 to a particular substrate or to a particular location within the cell. An additional role for 14-3-3 proteins in the DNA-damage checkpoint has been suggested based on the observation that human Chk1 can phosphorylate Cdc25C in vitro creating a 14-3-3 binding site. Our results suggest that in fission yeast the interaction between the 14-3-3 proteins and Cdc25 does not require Chk1 function and is unaffected by DNA damage, in sharp contrast to the interaction between the 14-3-3 proteins and Chk1.","authors":"Chen L, Liu TH, Walworth NC","authors_abbrev":"Chen L et al.","pubmed_publication_date":"15 Mar 1999","pubmed_entrez_date":"1999-03-25","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC8E11.02c","SPAC17A2.13c","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:26384663","title":"Nbr1, a Receptor for ESCRT-Dependent Endosomal Microautophagy in Fission Yeast.","citation":"Mol Cell 2015 Sep 17;59(6):887-9","abstract":"In this issue of Molecular Cell, Liu et al. (2015) report that fission yeast Nbr1, sharing a partial homology to the mammalian macroautophagy receptor NBR1, acts as a receptor for ESCRT-dependent endosomal microautophagy that delivers two hydrolytic enzymes from the cytosol to the vacuole.","doi":"10.1016/j.molcel.2015.09.004","authors":"Mizushima N","authors_abbrev":"Mizushima N","pubmed_publication_date":"17 Sep 2015","pubmed_entrez_date":"2015-09-20","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-09-21 00:18:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22573177","title":"Chromatin architectures at fission yeast transcriptional promoters and replication origins.","citation":"Nucleic Acids Res 2012 Aug;40(15):7176-89","abstract":"We have used micrococcal nuclease (MNase) digestion followed by deep sequencing in order to obtain a higher resolution map than previously available of nucleosome positions in the fission yeast, Schizosaccharomyces pombe. Our data confirm an unusually short average nucleosome repeat length, ∼152 bp, in fission yeast and that transcriptional start sites (TSSs) are associated with nucleosome-depleted regions (NDRs), ordered nucleosome arrays downstream and less regularly spaced upstream nucleosomes. In addition, we found enrichments for associated function in four of eight groups of genes clustered according to chromatin configurations near TSSs. At replication origins, our data revealed asymmetric localization of pre-replication complex (pre-RC) proteins within large NDRs-a feature that is conserved in fission and budding yeast and is therefore likely to be conserved in other eukaryotic organisms.","doi":"10.1093/nar/gks351","authors":"Givens RM, Lai WK, Rizzo JM, Bard JE, Mieczkowski PA, Leatherwood J, Huberman JA, Buck MJ","authors_abbrev":"Givens RM et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-05-11","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16611237","title":"Modulation of Alp4 function in Schizosaccharomyces pombe induces novel phenotypes that imply distinct functions for nuclear and cytoplasmic gamma-tubulin complexes.","citation":"Genes Cells 2006 Apr;11(4):319-36","abstract":"The gamma-tubulin complex acts as a nucleation unit for microtubule assembly. It remains unknown, however, how spatial and temporal regulation of the complex activity affects microtubule-mediated cellular processes. Alp4 is one of the essential components of the S. pombe gamma-tubulin complex. We show here that overproduction of a carboxy-terminal form of Alp4 (Alp4C) and its derivatives tagged to a nuclear localization signal or to a nuclear export signal affect localization of gamma-tubulin complexes and induces novel phenotypes that reflect distinct functions of nuclear and cytoplasmic gamma-tubulin complexes. Nuclear Alp4C induces a Wee1-dependent G2 delay, reduces the levels of the gamma-tubulin complex at the spindle pole body, and results in defects in mitotic progression including spindle assembly, cytoplasmic microtubule disassembly, and chromosome segregation. In contrast, cytoplasmic Alp4C induces oscillatory nuclear movement and affects levels of cell polarity markers, Bud6 and Tip1, at the cell ends. These results demonstrate that regulation of nuclear gamma-tubulin complex activity is essential for cell cycle progression through the G2/M boundary and M phase, whereas regulation of cytoplasmic gamma-tubulin complex activity is important for nuclear positioning and cell polarity control during interphase.","authors":"Masuda H, Toda T, Miyamoto R, Haraguchi T, Hiraoka Y","authors_abbrev":"Masuda H et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-04-14","publication_year":"2006","canto_session_key":"a42509fe62ac69ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-13 12:17:38","canto_approved_date":"2023-03-15 17:22:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-26 12:52:25","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":55,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPCC18B5.03","SPBC582.03","SPAC15A10.16","SPBC365.15","SPAC24H6.05","SPCC1223.06","SPBC428.20c"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2015-11-13"},{"uniquename":"PMID:31810592","title":"Investigation of mechanisms of toxicity and exclusion by transporters of the preservatives triclosan and propylparaben using batteries of Schizosaccharomyces pombe strains.","citation":"Environ Res 2020 Apr;183:108983","abstract":"Triclosan (TCS) and propylparaben (PPB) are antimicrobials widely used. They present many similarities in their applications and also in their human and environmental health risks. In order to investigate the mechanisms of toxic action and the efflux pumps involved in their detoxication, we used a strategy with batteries of Schizosaccharomyces pombe yeast strains, either defective in cell signalling, in detoxification pumps, or in cell surveillance mechanisms. Yeast were exposed up to 20 h in solid medium or in liquid medium in 96-well plates. The mechanisms of action investigated were spindle defects (mph1), stress (pmk1), DNA interference (rad3) or diverse effects (MDR-sup). The efflux pumps investigated were Bfr1, Pmd1, Mfs1 and Caf5 or the Pap1 transcription factor. Here we show that TCS was 75 times more toxic than PPB in the wild type fission yeast. More oxidative stress and less protection by exclusion pumps were observed for TCS than for PPB. The cytotoxicity produced by TCS decreased from bfr1>mfs1>pmd1 > pap1 and caf5A deficient strains. In contrast, cytotoxic concentrations of PPB caused only a mild stress. The protection provided for PPB by the transporters was more marked than for TCS, decreasing from Pmd1, Caf5, Mfs1 and Bfr1. Furthermore, microtubule and DNA interferences were revealed for PPB, according to the cytotoxicity of mph1 and rad3 defective cells, respectively. As both compounds present complex adverse effects at concentrations close to exposure, and their combination clearly causes a strong potentiation, more exhaustive controls and regulations in their use should be considered.","doi":"10.1016/j.envres.2019.108983","authors":"Álvarez-Herrera C, Maisanaba S, Repetto G","authors_abbrev":"Álvarez-Herrera C et al.","pubmed_publication_date":"Apr 2020","pubmed_entrez_date":"2019-12-08","publication_year":"2020","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7498729","title":"Hot spots of recombination in fission yeast: inactivation of the M26 hot spot by deletion of the ade6 promoter and the novel hotspot ura4-aim.","citation":"Genetics 1995 Jun;140(2):469-78","abstract":"The M26 mutation in the ade6 gene of Schizosaccharomyces pombe creates a hot spot of meiotic recombination. A single base substitution, the M26 mutation is situated within the open reading frame, near the 5' end. It has previously been shown that the heptanucleotide sequence 5' ATGACGT 3', which includes the M26 mutation, is required for hot spot activity. The 510-bp ade6-delXB deletion encompasses the promoter and the first 23 bp of the open reading frame, ending 112 bp upstream of M26. Deletion of the promoter in cis to M26 abolishes hot spot activity, while deletion in trans to M26 has no effect. Homozygous deletion of the promoter also eliminates M26 hot spot activity, indicating that the heterology created through deletion of the promoter per se is not responsible for the loss of hot spot activity. Thus, DNA sequences other than the heptanucleotide 5' ATGACGT 3', which must be located at the 5' end of the ade6 gene, appear to be required for hot spot activity. While the M26 hotspot stimulates crossovers associated with M26 conversion, it does not affect the crossover frequency in the intervals adjacent to ade6. The flanking marker ura4-aim, a heterology created by insertion of the ura4+ gene upstream of ade6, turned out to be a hot spot itself. It shows disparity of conversion with preferential loss of the insertion. The frequency of conversion at ura4-aim is reduced when the M26 hot spot is active 15 kb away, indicating competition for recombination factors by hot spots in close proximity.","authors":"Zahn-Zabal M, Lehmann E, Kohli J","authors_abbrev":"Zahn-Zabal M et al.","pubmed_publication_date":"Jun 1995","pubmed_entrez_date":"1995-06-01","publication_year":"1995","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:13818217","title":"[Characteristics of the fermentation of wood hydrolysates by Schizosaccharomyces Pombe].","citation":"Tr Inst Biol 1959;6:203-11","abstract":"","authors":"DRUBLIANETS EE, TKACHENKO NI, IVANOVA ZT","authors_abbrev":"DRUBLIANETS EE et al.","pubmed_publication_date":"1959","pubmed_entrez_date":"1959-01-01","publication_year":"1959","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27648579","title":"A histone H3K9M mutation traps histone methyltransferase Clr4 to prevent heterochromatin spreading.","citation":"Elife 2016 Sep 20;5","abstract":"Histone lysine-to-methionine (K-to-M) mutations are associated with multiple cancers, and they function in a dominant fashion to block the methylation of corresponding lysines on wild type histones. However, their mechanisms of function are controversial. Here we show that in fission yeast, introducing the K9M mutation into one of the three histone H3 genes dominantly blocks H3K9 methylation on wild type H3 across the genome. In addition, H3K9M enhances the interaction of histone H3 tail with the H3K9 methyltransferase Clr4 in a SAM (S-adenosyl-methionine)-dependent manner, and Clr4 is trapped at nucleation sites to prevent its spreading and the formation of large heterochromatin domains. We further determined the crystal structure of an H3K9M peptide in complex with human H3K9 methyltransferase G9a and SAM, which reveales that the methionine side chain had enhanced van der Waals interactions with G9a. Therefore, our results provide a detailed mechanism by which H3K9M regulates H3K9 methylation.","doi":"10.7554/eLife.17903","authors":"Shan CM, Wang J, Xu K, Chen H, Yue JX, Andrews S, Moresco JJ, Yates JR, Nagy PL, Tong L, Jia S","authors_abbrev":"Shan CM et al.","pubmed_publication_date":"20 Sep 2016","pubmed_entrez_date":"2016-09-21","publication_year":"2016","canto_session_key":"f08c0f4e1a2f2ba5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Songtao Jia","canto_first_approved_date":"2016-12-20 14:17:46","canto_approved_date":"2020-07-09 16:02:18","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-10-05 21:48:37","canto_added_date":"2016-09-22 00:15:15","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":81,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Songtao Jia","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.04","SPAC18G6.02c","SPBC16C6.10","SPCC622.16c","SPAC664.01c","SPAC1834.04","SPBC428.08c","SPBC1105.11c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-12-20"},{"uniquename":"PMID:25512493","title":"Regulation of the Rhp26ERCC6/CSB chromatin remodeler by a novel conserved leucine latch motif.","citation":"Proc Natl Acad Sci U S A 2014 Dec 30;111(52):18566-71","abstract":"CSB/ERCC6 (Cockayne syndrome B protein/excision repair cross-complementation group 6), a member of a subfamily of SWI2/SNF2 (SWItch/sucrose nonfermentable)-related chromatin remodelers, plays crucial roles in gene expression and the maintenance of genome integrity. Here, we report the mechanism of the autoregulation of Rhp26, which is the homolog of CSB/ERCC6 in Schizosaccharomyces pombe. We identified a novel conserved protein motif, termed the \"leucine latch,\" at the N terminus of Rhp26. The leucine latch motif mediates the autoinhibition of the ATPase and chromatin-remodeling activities of Rhp26 via its interaction with the core ATPase domain. Moreover, we found that the C terminus of the protein counteracts this autoinhibition and that both the N- and C-terminal regions of Rhp26 are needed for its proper function in DNA repair in vivo. The presence of the leucine latch motif in organisms ranging from yeast to humans suggests a conserved mechanism for the autoregulation of CSB/ERCC6 despite the otherwise highly divergent nature of the N- and C-terminal regions.","doi":"10.1073/pnas.1420227112","authors":"Wang L, Limbo O, Fei J, Chen L, Kim B, Luo J, Chong J, Conaway RC, Conaway JW, Ranish JA, Kadonaga JT, Russell P, Wang D","authors_abbrev":"Wang L et al.","pubmed_publication_date":"30 Dec 2014","pubmed_entrez_date":"2014-12-17","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCP25A2.02c","SPBC19C7.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:23348717","title":"Essential role of Ubr11, but not Ubr1, as an N-end rule ubiquitin ligase in Schizosaccharomyces pombe.","citation":"Yeast 2013 Jan;30(1):1-11","abstract":"The N-end rule pathway degrades proteins bearing a destabilization-inducing amino acid at the N-terminus. In this proteolytic system, Ubr ubiquitin ligases recognize and ubiquitylate substrates intended for degradation. Schizosaccharomyces pombe has two similar Ubr proteins, Ubr1 and Ubr11. Both proteins have unique roles in various cellular processes, although the ubr1∆ strain shows more severe defects. However, their involvement in the N-end rule pathway is unclear, and even the N-end rule pathway-dependent proteolytic activity has not been demonstrated in Sz. pombe. Here, we show that: (a) Sz. pombe has the N-end rule pathway in which only Ubr11, but not Ubr1, is responsible; and (b) the C-terminal fragment of the meiotic cohesin Rec8 (denoted as Rec8c) generated by separase-mediated cleavage is an endogenous substrate of the N-end rule pathway. Forced overexpression of stable Rec8c was deleterious in mitosis and caused a loss of the mini-chromosome. In unperturbed mitosis without overexpression, the rate of mini-chromosome loss was five-fold higher in the ubr11∆ strain. Since Rec8 is normally produced in meiosis, we examined whether meiosis and sporulation were affected in the ubr11∆ strain. In unperturbed meiosis, chromosome segregation occurred almost normally and viable spores were produced in the ubr11∆ cells, irrespective of the presence of undegraded endogenous Rec8c peptides.","doi":"10.1002/yea.2936","authors":"Fujiwara H, Tanaka N, Yamashita I, Kitamura K","authors_abbrev":"Fujiwara H et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2013-01-26","publication_year":"2013","canto_session_key":"9b739862e4c2c98b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-01 14:22:17","canto_approved_date":"2025-09-02 21:41:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-04 12:13:40","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPAC18B11.07c","SPAC15A10.11","SPAC3C7.07c","SPBC4.07c","SPBC19C7.02"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-09-01"},{"uniquename":"PMID:12865439","title":"Delineating the position of rad4+/cut5+ within the DNA-structure checkpoint pathways in Schizosaccharomyces pombe.","citation":"J Cell Sci 2003 Sep 01;116(Pt 17):3519-29","abstract":"The fission yeast BRCT domain protein Rad4/Cut5 is required for genome integrity checkpoint responses and DNA replication. Here we address the position at which Rad4/Cut5 acts within the checkpoint response pathways. Rad4 is shown to act upstream of the effector kinases Chk1 and Cds1, as both Chk1 phosphorylation and Cds1 kinase activity require functional Rad4. Phosphorylation of Rad9, Rad26 and Hus1 in response to either DNA damage or inhibition of DNA replication are independent of Rad4/Cut5 checkpoint function. Further we show that a novel, epitope-tagged allele of rad4+/cut5+ acts as a dominant suppressor of the checkpoint deficiencies of rad3-, rad26- and rad17- mutants. Suppression results in the restoration of mitotic arrest and is dependent upon the remaining checkpoint Rad proteins and the two effector kinases. High-level expression of the rad4+/cut5+ allele in rad17 mutant cells restores the nuclear localization of Rad9, but this does not fully account for the observed suppression. We conclude from these data that Rad4/Cut5 acts with Rad3, Rad26 and Rad17 to effect the checkpoint response, and a model for its function is discussed.","authors":"Harris S, Kemplen C, Caspari T, Chan C, Lindsay HD, Poitelea M, Carr AM, Price C","authors_abbrev":"Harris S et al.","pubmed_publication_date":"01 Sep 2003","pubmed_entrez_date":"2003-07-17","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.13","SPBC216.05","SPAC9E9.08","SPAC23C4.18c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:8138176","title":"Mutations in rik1, clr2, clr3 and clr4 genes asymmetrically derepress the silent mating-type loci in fission yeast.","citation":"Genetics 1994 Jan;136(1):53-64","abstract":"In Schizosaccharomyces pombe the mating-type information is stored at two transcriptionally silent loci (mat2 and mat3). The region between these sites (K region) is inert for meiotic crossing over. The mating-type genes (M or P) are expressed only when present at a third, active locus (mat1). We have earlier shown that the positional regulation of P genes is based on repression at the silent site, caused by elements in the flanking DNA sequences. In this study we have mutagenized a sterile mat1 deleted strain and selected for cells that are able to conjugate. Recessive mutations of this type should define genes encoding trans-acting factors involved in repression of the silent mating-type loci. Before this work mutations in two genes, clr1 and swi6, had been shown to allow both expression of the silent loci and recombination in the K region. The sensitivity of the present selection is demonstrated by the isolation of new mutations that derepress one or both of the silent loci (M-mating or bi-mating). The frequency of M-mating mutants was almost two orders of magnitude higher than that of bi-mating mutants and in all mutants analyzed mat3-M expression was significantly higher than mat2-P expression. The mutations define three new genes, clr2, clr3 and clr4. In addition we show that the rik1 mutant previously known to allow recombination in the K region also depresses the silent loci.","authors":"Ekwall K, Ruusala T","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_session_key":"ff818420fe6b352b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-12 07:22:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-12 07:22:18","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.17","SPBC428.08c","SPBC800.03","SPAC664.01c","SPCC11E10.08","SPBC2D10.17"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-08-12"},{"uniquename":"PMID:24699916","title":"Mechanism of chromosomal DNA replication initiation and replication fork stabilization in eukaryotes.","citation":"Sci China Life Sci 2014 May;57(5):482-7","abstract":"Chromosomal DNA replication is one of the central biological events occurring inside cells. Due to its large size, the replication of genomic DNA in eukaryotes initiates at hundreds to tens of thousands of sites called DNA origins so that the replication could be completed in a limited time. Further, eukaryotic DNA replication is sophisticatedly regulated, and this regulation guarantees that each origin fires once per S phase and each segment of DNA gets duplication also once per cell cycle. The first step of replication initiation is the assembly of pre-replication complex (pre-RC). Since 1973, four proteins, Cdc6/Cdc18, MCM, ORC and Cdt1, have been extensively studied and proved to be pre-RC components. Recently, a novel pre-RC component called Sap1/Girdin was identified. Sap1/Girdin is required for loading Cdc18/Cdc6 to origins for pre-RC assembly in the fission yeast and human cells, respectively. At the transition of G1 to S phase, pre-RC is activated by the two kinases, cyclindependent kinase (CDK) and Dbf4-dependent kinase (DDK), and subsequently, RPA, primase-polα, PCNA, topoisomerase, Cdc45, polδ, and polɛ are recruited to DNA origins for creating two bi-directional replication forks and initiating DNA replication. As replication forks move along chromatin DNA, they frequently stall due to the presence of a great number of replication barriers on chromatin DNA, such as secondary DNA structures, protein/DNA complexes, DNA lesions, gene transcription. Stalled forks must require checkpoint regulation for their stabilization. Otherwise, stalled forks will collapse, which results in incomplete DNA replication and genomic instability. This short review gives a concise introduction regarding the current understanding of replication initiation and replication fork stabilization.","doi":"10.1007/s11427-014-4631-4","authors":"Wu L, Liu Y, Kong D","authors_abbrev":"Wu L et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2014-04-05","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24623719","title":"The fission yeast spore is coated by a proteinaceous surface layer comprising mainly Isp3.","citation":"Mol Biol Cell 2014 May;25(10):1549-59","abstract":"The spore is a dormant cell that is resistant to various environmental stresses. As compared with the vegetative cell wall, the spore wall has a more extensive structure that confers resistance on spores. In the fission yeast Schizosaccharomyces pombe, the polysaccharides glucan and chitosan are major components of the spore wall; however, the structure of the spore surface remains unknown. We identify the spore coat protein Isp3/Meu4. The isp3 disruptant is viable and executes meiotic nuclear divisions as efficiently as the wild type, but isp3∆ spores show decreased tolerance to heat, digestive enzymes, and ethanol. Electron microscopy shows that an electron-dense layer is formed at the outermost region of the wild-type spore wall. This layer is not observed in isp3∆ spores. Furthermore, Isp3 is abundantly detected in this layer by immunoelectron microscopy. Thus Isp3 constitutes the spore coat, thereby conferring resistance to various environmental stresses.","doi":"10.1091/mbc.E13-12-0731","authors":"Fukunishi K, Miyakubi K, Hatanaka M, Otsuru N, Hirata A, Shimoda C, Nakamura T","authors_abbrev":"Fukunishi K et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2014-03-14","publication_year":"2014","canto_session_key":"7e9f944dba7b4ea2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-16 22:29:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-16 22:29:18","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F8.05","SPAC19G12.03","SPAC13G6.12c","SPBC1709.01"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-12-16"},{"uniquename":"PMID:3169239","title":"Two changes of the same nucleotide confer resistance to diuron and antimycin in the mitochondrial cytochrome b gene of Schizosaccharomyces pombe.","citation":"FEBS Lett 1988 Sep 12;237(1-2):31-4","abstract":"Diuron (3-(3,4-dichlorophenyl)-1,1-dimethylurea) and antimycin, both inhibitors of mitochondrial respiration, block electron flow between cytochromes b and c1. Mutants resistant to either drug have been selected using Schizosaccharomyces pombe strains with an extrachromosomally inherited mutator. In analogy to Saccharomyces cerevisiae these mutational sites were assumed to map in the cytochrome b gene. DNA sequence analysis showed that two changes in the same nucleotide are responsible for resistance to antimycin and diuron. Analysis of resistant and sensitive progeny of crosses between the mutants and the wild type confirmed the correlation between mutational alteration and resistant phenotype.","authors":"Weber S, Wolf K","authors_abbrev":"Weber S et al.","pubmed_publication_date":"12 Sep 1988","pubmed_entrez_date":"1988-09-12","publication_year":"1988","canto_session_key":"00df665b88c640d5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-05-10 14:19:45","canto_approved_date":"2024-04-03 16:08:04","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-09-24 14:54:15","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMIT.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-05-10"},{"uniquename":"PMID:37873420","title":"Delineating yeast cleavage and polyadenylation signals using deep learning.","citation":"bioRxiv 2023 Oct 13;","abstract":"3'-end cleavage and polyadenylation is an essential process for eukaryotic mRNA maturation. In yeast species, the polyadenylation signals that recruit the processing machinery are degenerate and remain poorly characterized compared to well-defined regulatory elements in mammals. Especially, recent deep sequencing experiments showed extensive cleavage heterogeneity for some mRNAs in  Saccharomyces cerevisiae  and uncovered the polyA motif differences between  S. cerevisiae  vs.  Schizosaccharomyces pombe  . The findings raised the fundamental question of how polyadenylation signals are formed in yeast. Here we addressed this question by developing deep learning models to deconvolute degenerate  cis  -regulatory elements and quantify their positional importance in mediating yeast polyA site formation, cleavage heterogeneity, and strength. In  S. cerevisiae  , cleavage heterogeneity is promoted by the depletion of U-rich elements around polyA sites as well as multiple occurrences of upstream UA-rich elements. Sites with high cleavage heterogeneity show overall lower strength. The site strength and tandem site distances modulate alternative polyadenylation (APA) under the diauxic stress. Finally, we developed a deep learning model to reveal the distinct motif configuration of  S. pombe  polyA sites which show more precise cleavage than  S. cerevisiae  . Altogether, our deep learning models provide unprecedented insights into polyA site formation across yeast species.","doi":"10.1101/2023.10.10.561764","authors":"Stroup EK, Ji Z","authors_abbrev":"Stroup EK et al.","pubmed_publication_date":"13 Oct 2023","pubmed_entrez_date":"2023-10-24","publication_year":"2023","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2023-10-24 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14234806","title":"ELECTRON MICROSCOPY OF A FISSION YEAST, SCHIZOSACCHAROMYCES POMBE.","citation":"J Bacteriol 1964 Nov;88(5):1459-66","abstract":"Maclean, Norman (University of Edinburgh, Edinburgh, Scotland). Electron microscopy of a fission yeast, Schizosaccharomyces pombe. J. Bacteriol. 88:1459-1466. 1964.-The structure of the fission yeast, Schizosaccharomyces pombe, was studied electron microscopically, with potassium permanganate and osmium tetroxide as fixatives. The cell was found to be bounded by a cell wall, 1,000 to 2,000 A thick, and a cell membrane. A layer of material was found between the cell membrane and the wall. The central nucleus, 2 to 3 mu in diameter, was bounded by a nuclear membrane, seen in some pictures to be double. Osmium tetroxide fixation revealed a granular body within the nucleus, identified as a nucleolus. Cytoplasmic structures included numerous vacuoles (probably normally containing lipid), a number of membranes and vesicles (which may represent a poorly organized mitochondrial system), and numerous granules (probably representing ribosomes).","authors":"MACLEAN N","authors_abbrev":"MACLEAN N","pubmed_publication_date":"Nov 1964","pubmed_entrez_date":"1964-11-01","publication_year":"1964","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31712578","title":"DNA sequence differences are determinants of meiotic recombination outcome.","citation":"Sci Rep 2019 Nov 11;9(1):16446","abstract":"Meiotic recombination is essential for producing healthy gametes, and also generates genetic diversity. DNA double-strand break (DSB) formation is the initiating step of meiotic recombination, producing, among other outcomes, crossovers between homologous chromosomes (homologs), which provide physical links to guide accurate chromosome segregation. The parameters influencing DSB position and repair are thus crucial determinants of reproductive success and genetic diversity. Using Schizosaccharomyces pombe, we show that the distance between sequence polymorphisms across homologs has a strong impact on meiotic recombination rate. The closer the sequence polymorphisms are to each other across the homologs the fewer recombination events were observed. In the immediate vicinity of DSBs, sequence polymorphisms affect the frequency of intragenic recombination events (gene conversions). Additionally, and unexpectedly, the crossover rate of flanking markers tens of kilobases away from the sequence polymorphisms was affected by their relative position to each other amongst the progeny having undergone intragenic recombination. A major regulator of this distance-dependent effect is the MutSα-MutLα complex consisting of Msh2, Msh6, Mlh1, and Pms1. Additionally, the DNA helicases Rqh1 and Fml1 shape recombination frequency, although the effects seen here are largely independent of the relative position of the sequence polymorphisms.","doi":"10.1038/s41598-019-52907-x","authors":"Brown SD, Mpaulo SJ, Asogwa MN, Jézéquel M, Whitby MC, Lorenz A","authors_abbrev":"Brown SD et al.","pubmed_publication_date":"11 Nov 2019","pubmed_entrez_date":"2019-11-13","publication_year":"2019","canto_session_key":"fc76162e4e6ace33","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alexander Lorenz","canto_first_approved_date":"2021-06-28 15:36:43","canto_approved_date":"2024-07-23 16:02:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-25 10:03:20","canto_added_date":"2019-11-14 01:15:04","annotation_curators":[{"name":"Alexander Lorenz","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPBC1703.04","SPAC19G12.02c","SPCC285.16c","SPAC8F11.03","SPCC1322.13","SPAC9.05","SPBC19G7.01c"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2021-06-28"},{"uniquename":"PMID:2586486","title":"Isolation and initial characterization of a Schizosaccharomyces pombe mutant exhibiting temperature-dependent radiation sensitivity due to a mutation in a previously unidentified rad locus.","citation":"Mol Gen Genet 1989 Sep;218(3):554-8","abstract":"We have isolated a mutant of the yeast Schizosaccharomyces pombe which exhibits sensitivity to UV light when grown at either 30 degrees or 37 degrees C, as compared to the parental wild-type strain. This increased sensitivity is more pronounced when cells are grown at 37 degrees C. The mutant is also sensitive to 18 MeV electrons at the high temperature. Tetrad analysis of spores generated by crossing the mutant and a Rad+ strain revealed that sensitivity to both types of radiation cosegregate 2:2, relative to wild-type resistance, indicating that a single altered chromosomal locus is responsible for the radiation sensitivities observed. In addition, analysis of spores resulting from crosses between the mutant and all other known S. pombe rad mutants indicates that the temperature-dependent sensitivity described in this report is mediated by a mutation in a previously unidentified rad locus.","authors":"Lieberman HB, Riley R, Martel M","authors_abbrev":"Lieberman HB et al.","pubmed_publication_date":"Sep 1989","pubmed_entrez_date":"1989-09-01","publication_year":"1989","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36481249","title":"Critical role of Wat1/Pop3 in regulating the TORC1 signalling pathway in fission yeast S. pombe.","citation":"Fungal Genet Biol 2023 Jan;164:103764","abstract":"The target of rapamycin (TOR), a major pathway for the regulation of cell growth and proliferation is conserved from yeast to humans. Fission yeast contains two tor complexes, TORC1 is crucial for cell growth while TORC2 gets activated under stress conditions. Pop3/Wat1, a mammalian Lst8 ortholog is an important component of both TOR complexes and has been implicated in the oxidative stress response pathway. Here in this study, the genetic interaction analysis revealed a synthetic lethal interaction of wat1 with tor2-287 mutant cells. Co-immunoprecipitation analysis revealed Wat1 interacts with TORC1 components Tor2, Mip1, and Tco89 while wat1-17 mutant protein fails to interact with these proteins. In the absence of Wat1, the cells arrest at G1 phase with reduced cell size at non-permissive temperature reminiscent of tor2-287 mutant phenotype. Similarly, inactivation of Wat1 results in the failure of TORC1 mediated phosphorylation of Psk1 and Rps602, leading to dysregulation of amino acid permeases and delocalization of Gaf1, a DNA binding transcription factor. Overall, we have hypothesized that Wat1/Pop3 is required to execute the function of TORC1.","doi":"10.1016/j.fgb.2022.103764","authors":"Panigrahi L, Anjum S, Ahmed S","authors_abbrev":"Panigrahi L et al.","pubmed_publication_date":"Jan 2023","pubmed_entrez_date":"2022-12-08","publication_year":"2023","canto_session_key":"0f9e5e33d1984340","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shakil Ahmed","canto_first_approved_date":"2023-04-13 17:26:54","canto_approved_date":"2023-04-13 17:26:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-04-11 07:59:49","canto_added_date":"2022-12-10 01:15:04","annotation_curators":[{"name":"Shakil Ahmed","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.07c","SPAC869.11","SPAC57A7.11","SPCC1902.01","SPAC1039.09","SPAPB1E7.12","SPBC21B10.05c","SPCC4G3.08","SPAP7G5.06","SPCC162.12"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2023-04-13"},{"uniquename":"PMID:2245912","title":"stf1: non-wee mutations epistatic to cdc25 in the fission yeast Schizosaccharomyces pombe.","citation":"Genetics 1990 Oct;126(2):309-15","abstract":"In Schizosaccharomyces pombe, cdc25 is a cell cycle regulated inducer of mitosis. wee1 and phenotypically wee alleles of cdc2 are epistatic to cdc25. Mutant alleles of a new locus, stf1 (suppressor of twenty-five), identified in a reversion analysis of conditionally lethal cdr1-76 cdc25-22 and cdr2-96 cdc25-22 double mutant strains, also suppress both temperature-sensitive and gene disruption alleles of cdc25. These mutants, by themselves, are phenotypically indistinguishable from wild type strains; hence they represent the first known mutations that are epistatic to cdc25 and do not display a wee phenotype. stf1 genetically interacts with other elements of mitotic control in S. pombe. stf1-1 is additive with wee1-50, cdc2-1w and cdc2-3w for suppression of cdc25-22. Also, like wee1- and cdc2-w, stf1- suppression of cdc25 is reversed by overexpression of the putative type 1 protein phosphatase bws1+/dis2+. Interaction with various mutants and plasmid overexpression experiments suggest that stf1 does not operate either upstream or downstream of wee1. Similarly, it does not operate through cdc25 since it rescues the disruption. stf1 appears to encode an important new element of mitotic control.","authors":"Hudson JD, Feilotter H, Young PG","authors_abbrev":"Hudson JD et al.","pubmed_publication_date":"Oct 1990","pubmed_entrez_date":"1990-10-01","publication_year":"1990","canto_session_key":"27524319ad84c25c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2020-06-25 14:50:30","canto_approved_date":"2024-03-18 17:05:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-05 14:13:53","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":42,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC11B10.09","SPBC582.03","SPAC644.06c","SPAC57A10.02","SPBC649.05","SPBC776.02c","SPBC1734.14c","SPAC24H6.05"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2020-06-25"},{"uniquename":"PMID:16845379","title":"Regulation of cytokinesis by spindle-pole bodies.","citation":"Nat Cell Biol 2006 Aug;8(8):891-3","abstract":"In the fission yeast Schizosaccharomyces pombe, cytokinesis is thought to be controlled by the daughter spindle-pole body (SPB) through a regulatory pathway named the septation initiation network (SIN). Here, we demonstrate that laser ablation of both, but not a single SPB, results in failure of cytokinesis. Ablation of only the daughter SPB often leads to activation of the SIN on the mother SPB and successful cytokinesis. Thus, either SPB can drive cytokinesis.","authors":"Magidson V, Chang F, Khodjakov A","authors_abbrev":"Magidson V et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-07-18","publication_year":"2006","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33791858","title":"Negative control of cytokinesis by stress-activated MAPK signaling.","citation":"Curr Genet 2021 Oct;67(5):715-721","abstract":"Mitogen-activated protein kinase (MAPK) signalling pathways regulate multiple cellular functions in eukaryotic organisms in response to environmental cues, including the dynamic remodeling of the actin cytoskeleton. The fission yeast S. pombe is an optimal model to investigate the conserved regulatory mechanisms of cytokinesis, which relies in an actomyosin-based contractile ring (CAR) that prompts the physical separation of daughter cells during cellular division. Our group has recently shown that p38 MAPK ortholog Sty1, the core component of the stress-activated pathway (SAPK), negatively modulates CAR assembly and integrity in S. pombe during actin cytoskeletal damage induced with Latrunculin A and in response to environmental stress. This response involves downregulation of protein levels of the formin For3, which assembles actin filaments for cables and the CAR, likely through an ubiquitin-mediated degradation mechanism. Contrariwise, Sty1 function positively reinforces CAR assembly during stress in the close relative dimorphic fission yeast S. japonicus. The opposite effect of SAPK signaling on CAR integrity may represent an evolutionary refined adaptation to cope with the marked differences in cytokinesis onset in both fission yeast species.","doi":"10.1007/s00294-021-01155-6","authors":"Madrid M, Gómez-Gil E, Cansado J","authors_abbrev":"Madrid M et al.","pubmed_publication_date":"Oct 2021","pubmed_entrez_date":"2021-04-01","publication_year":"2021","canto_session_key":"b0f76c14b6c49834","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-04-03 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33536435","title":"Conserved strategies of RNA polymerase I hibernation and activation.","citation":"Nat Commun 2021 Feb 03;12(1):758","abstract":"RNA polymerase (Pol) I transcribes the ribosomal RNA precursor in all eukaryotes. The mechanisms 'activation by cleft contraction' and 'hibernation by dimerization' are unique to the regulation of this enzyme, but structure-function analysis is limited to baker's yeast. To understand whether regulation by such strategies is specific to this model organism or conserved among species, we solve three cryo-EM structures of Pol I from Schizosaccharomyces pombe in different functional states. Comparative analysis of structural models derived from high-resolution reconstructions shows that activation is accomplished by a conserved contraction of the active center cleft. In contrast to current beliefs, we find that dimerization of the S. pombe polymerase is also possible. This dimerization is achieved independent of the 'connector' domain but relies on two previously undescribed interfaces. Our analyses highlight the divergent nature of Pol I transcription systems from their counterparts and suggest conservation of regulatory mechanisms among organisms.","doi":"10.1038/s41467-021-21031-8","authors":"Heiss FB, Daiß JL, Becker P, Engel C","authors_abbrev":"Heiss FB et al.","pubmed_publication_date":"03 Feb 2021","pubmed_entrez_date":"2021-02-04","publication_year":"2021","canto_session_key":"bdb4af95ebaefdfb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-17 17:12:23","canto_approved_date":"2025-12-21 22:22:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 17:12:16","canto_added_date":"2021-02-06 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.07","SPCC1259.03","SPBC1289.07c","SPBC1718.03","SPBC4C3.05c","SPAC23C4.15","SPCC1020.04c","SPAC1B3.12c","SPBC14C8.12","SPAC1687.01","SPBC19C2.03","SPBC3B9.07c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2023-02-17","pdb_entries":[{"pdb_id":"7aod","gene_chains":[{"gene_uniquename":"SPAC1B3.12c","chain":"J/V","position":"1-71"},{"gene_uniquename":"SPBC3B9.07c","chain":"G/S","position":"1-173"},{"gene_uniquename":"SPBC1289.07c","chain":"C/O","position":"1-348"},{"gene_uniquename":"SPCC1259.03","chain":"I/U","position":"1-119"},{"gene_uniquename":"SPBC4C3.05c","chain":"A/M","position":"1-1689"},{"gene_uniquename":"SPCC1020.04c","chain":"F/R","position":"1-142"},{"gene_uniquename":"SPBC19C2.03","chain":"L/X","position":"1-63"},{"gene_uniquename":"SPAC1687.01","chain":"K/W","position":"1-125"},{"gene_uniquename":"SPAC23C4.15","chain":"E/Q","position":"1-210"},{"gene_uniquename":"SPBC14C8.12","chain":"H/T","position":"1-125"},{"gene_uniquename":"SPBC1718.03","chain":"D/P","position":"1-147"},{"gene_uniquename":"SPBP23A10.07","chain":"B/N","position":"1-1174"}],"title":"Schizosaccharomyces pombe RNA polymerase I (dimer)","entry_authors":"Heiss F,Daiss J,Becker P,Engel C","entry_authors_abbrev":"Heiss F et al.","reference_uniquename":"PMID:33536435","experimental_method":"EM","resolution":"4.5"},{"pdb_id":"7aoe","gene_chains":[{"gene_uniquename":"SPAC1B3.12c","chain":"J","position":"1-71"},{"gene_uniquename":"SPBC3B9.07c","chain":"G","position":"1-173"},{"gene_uniquename":"SPBC1289.07c","chain":"C","position":"1-348"},{"gene_uniquename":"SPCC1259.03","chain":"I","position":"1-119"},{"gene_uniquename":"SPBC4C3.05c","chain":"A","position":"1-1689"},{"gene_uniquename":"SPCC1020.04c","chain":"F","position":"1-142"},{"gene_uniquename":"SPBC19C2.03","chain":"L","position":"1-63"},{"gene_uniquename":"SPAC1687.01","chain":"K","position":"1-125"},{"gene_uniquename":"SPAC23C4.15","chain":"E","position":"1-210"},{"gene_uniquename":"SPBC14C8.12","chain":"H","position":"1-125"},{"gene_uniquename":"SPBC1718.03","chain":"D","position":"1-147"},{"gene_uniquename":"SPBP23A10.07","chain":"B","position":"1-1174"}],"title":"Schizosaccharomyces pombe RNA polymerase I (elongation complex)","entry_authors":"Heiss F,Daiss J,Becker P,Engel C","entry_authors_abbrev":"Heiss F et al.","reference_uniquename":"PMID:33536435","experimental_method":"EM","resolution":"3.9"},{"pdb_id":"7aoc","gene_chains":[{"gene_uniquename":"SPAC1B3.12c","chain":"J","position":"1-71"},{"gene_uniquename":"SPBC3B9.07c","chain":"G","position":"1-173"},{"gene_uniquename":"SPBC1289.07c","chain":"C","position":"1-348"},{"gene_uniquename":"SPCC1259.03","chain":"I","position":"1-119"},{"gene_uniquename":"SPBC4C3.05c","chain":"A","position":"1-1689"},{"gene_uniquename":"SPCC1020.04c","chain":"F","position":"1-142"},{"gene_uniquename":"SPBC19C2.03","chain":"L","position":"1-63"},{"gene_uniquename":"SPAC1687.01","chain":"K","position":"1-125"},{"gene_uniquename":"SPAC23C4.15","chain":"E","position":"1-210"},{"gene_uniquename":"SPBC14C8.12","chain":"H","position":"1-125"},{"gene_uniquename":"SPBC1718.03","chain":"D","position":"1-147"},{"gene_uniquename":"SPBP23A10.07","chain":"B","position":"1-1174"}],"title":"Schizosaccharomyces pombe RNA polymerase I (monomer)","entry_authors":"Heiss F,Daiss J,Becker P,Engel C","entry_authors_abbrev":"Heiss F et al.","reference_uniquename":"PMID:33536435","experimental_method":"EM","resolution":"3.84"}]},{"uniquename":"PMID:30503616","title":"Centromere DNA Destabilizes H3 Nucleosomes to Promote CENP-A Deposition during the Cell Cycle.","citation":"Curr Biol 2018 Dec 17;28(24):3924-3936.e4","abstract":"Active centromeres are defined by the presence of nucleosomes containing CENP-A, a histone H3 variant, which alone is sufficient to direct kinetochore assembly. Once assembled at a location, CENP-A chromatin and kinetochores are maintained at that location through a positive feedback loop where kinetochore proteins recruited by CENP-A promote deposition of new CENP-A following replication. Although CENP-A chromatin itself is a heritable entity, it is normally associated with specific sequences. Intrinsic properties of centromeric DNA may favor the assembly of CENP-A rather than H3 nucleosomes. Here we investigate histone dynamics on centromere DNA. We show that during S phase, histone H3 is deposited as a placeholder at fission yeast centromeres and is subsequently evicted in G2, when we detect deposition of the majority of new CENP-A Cnp1 . We also find that centromere DNA has an innate property of driving high rates of turnover of H3-containing nucleosomes, resulting in low nucleosome occupancy. When placed at an ectopic chromosomal location in the absence of any CENP-A Cnp1  assembly, centromere DNA appears to retain its ability to impose S phase deposition and G2 eviction of H3, suggesting that features within centromere DNA program H3 dynamics. Because RNA polymerase II (RNAPII) occupancy on this centromere DNA coincides with H3 eviction in G2, we propose a model in which RNAPII-coupled chromatin remodeling promotes replacement of H3 with CENP-A Cnp1  nucleosomes.","doi":"10.1016/j.cub.2018.10.049","authors":"Shukla M, Tong P, White SA, Singh PP, Reid AM, Catania S, Pidoux AL, Allshire RC","authors_abbrev":"Shukla M et al.","pubmed_publication_date":"17 Dec 2018","pubmed_entrez_date":"2018-12-04","publication_year":"2018","canto_session_key":"a4e62346e10ec01f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-02-05 16:32:52","canto_approved_date":"2019-02-05 16:32:52","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-02-04 16:30:08","canto_added_date":"2018-12-08 01:15:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.04","SPBC1105.17","SPAC1834.03c","SPAC1834.04","SPBC1105.11c","SPBC8D2.03c","SPBC28F2.12","SPBC1105.12"],"gene_count":8,"ltp_gene_count":2,"approved_date":"2019-02-05"},{"uniquename":"PMID:11226171","title":"Novel functional requirements for non-homologous DNA end joining in Schizosaccharomyces pombe.","citation":"EMBO J 2001 Jan 15;20(1-2):210-21","abstract":"DNA double strand break (DSB) repair by non-homologous end joining (NHEJ) in mammalian cells requires the Ku70-Ku80 heterodimer, the DNA-PK catalytic subunit DNA-PKcs, as well as DNA ligase IV and Xrcc4. NHEJ of plasmid DSBs in Saccharomyces cerevisiae requires Ku, Xrcc4 and DNA ligase IV, as well as Mre11, Rad50, Xrs2 and DNA damage checkpoint proteins. Saccharomyces cerevisiae Ku is also required for telomere length maintenance and transcriptional silencing. We have characterized NHEJ in Schizosaccharomyces pombe using an extrachromosomal assay and find that, as anticipated, it is Ku70 and DNA ligase IV dependent. Unexpectedly, we find that Rad32, Rad50 (the S.pombe homologues of Mre11 and Rad50, respectively) and checkpoint proteins are not required for NHEJ. Furthermore, although S.pombe Ku70 is required for maintenance of telomere length, it is dispensable for transcriptional silencing at telomeres and is located throughout the nucleus rather than concentrated at the telomeres. Together, these results provide insight into the mechanism of NHEJ and contrast significantly with recent studies in S.cerevisiae.","authors":"Manolis KG, Nimmo ER, Hartsuiker E, Carr AM, Jeggo PA, Allshire RC","authors_abbrev":"Manolis KG et al.","pubmed_publication_date":"15 Jan 2001","pubmed_entrez_date":"2001-02-28","publication_year":"2001","canto_session_key":"149d8ab5ac0f3ce8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-04-20 16:26:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-04-20 16:26:36","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.02","SPBC216.05","SPCC1259.13","SPAC15A10.03c","SPCC126.02c","SPBC342.05","SPCC23B6.03c","SPCC1183.05c","SPCC18B5.11c","SPAC14C4.13","SPAC13C5.07","SPAC1556.01c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2016-04-20"},{"uniquename":"PMID:7622618","title":"Fission yeast TPR-family protein nuc2 is required for G1-arrest upon nitrogen starvation and is an inhibitor of septum formation.","citation":"J Cell Sci 1995 Mar;108 ( Pt 3):895-905","abstract":"Fission yeast nuc2+ gene encodes a protein of a tetratricopeptide repeat (TPR) family which is conserved throughout evolution. We previously showed that nuc2 is required for exit from the mitotic metaphase. In this study, we present evidence which shows that nuc2 has two additional roles in the cell cycle. We showed that the nuc2 mutant is sterile even at the permissive temperature and septation occurs in the absence of chromosome separation at the restrictive temperature. The nuc2 mutant fails to arrest at the G1 phase upon nitrogen starvation at the permissive temperature which is a prerequisite for conjugation. Upon starvation, however, the nuc2 mutant ceased division normally and induced starvation-dependent gene expression. Therefore, the nuc2 mutant is deficient only for failure to block DNA replication upon starvation. At the lower restrictive temperature, the nuc2 mutant showed a 'cut' phenotype where septation and cytokinesis takes place without the completion of mitosis. Ectopic overexpression of the nuc2+ gene caused multiple rounds of S and M phases in the complete absence of septum formation. We propose that nuc2 is a novel cell cycle regulator essential for three events; firstly for exit from mitosis, secondly for DNA replication restraint under nutrient starvation and thirdly for inhibition of septation and cytokinesis until the completion of mitosis.","authors":"Kumada K, Su S, Yanagida M, Toda T","authors_abbrev":"Kumada K et al.","pubmed_publication_date":"Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_session_key":"dbb001257ca2e7c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-03 14:30:48","canto_approved_date":"2026-01-29 12:20:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-18 16:28:33","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.01c","SPAC27D7.03c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2017-01-03"},{"uniquename":"PMID:17322402","title":"Shugoshin enables tension-generating attachment of kinetochores by loading Aurora to centromeres.","citation":"Genes Dev 2007 Feb 15;21(4):420-35","abstract":"Fission yeast shugoshin Sgo1 is meiosis specific and cooperates with protein phosphatase 2A to protect centromeric cohesin at meiosis I. The other shugoshin-like protein Sgo2, which requires the heterochromatin protein Swi6/HP1 for full viability, plays a crucial role for proper chromosome segregation at both mitosis and meiosis; however, the underlying mechanisms are totally elusive. We here demonstrate that, unlike Sgo1, Sgo2 is dispensable for centromeric protection of cohesin. Instead, Sgo2 interacts with Bir1/Survivin and promotes Aurora kinase complex localization to the pericentromeric region, to correct erroneous attachment of kinetochores and thereby enable tension-generating attachment. Forced localization of Bir1 to centromeres partly restored the defects of sgo2Delta. This newly identified interaction of shugoshin with Survivin is conserved between mitosis and meiosis and presumably across eukaryotes. We propose that ensuring bipolar attachment of kinetochores is the primary role of shugoshin and the role of cohesion protection might have codeveloped to facilitate this process.","authors":"Kawashima SA, Tsukahara T, Langegger M, Hauf S, Kitajima TS, Watanabe Y","authors_abbrev":"Kawashima SA et al.","pubmed_publication_date":"15 Feb 2007","pubmed_entrez_date":"2007-02-27","publication_year":"2007","canto_session_key":"f2dfea149f8db02b","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.15","SPAC664.01c","SPCC962.02c","SPAC15A10.15","SPCC320.13c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:3561486","title":"Differentiated parental DNA strands confer developmental asymmetry on daughter cells in fission yeast.","citation":"Nature 1987 Apr 2;326(6112):466-70","abstract":"The two strands of the DNA molecule are complementary but not identical. Hence, upon semiconservative replication, different parental DNA strands are segregated to daughter cells. A molecular analysis suggests that the process of fission yeast mating-type interconversion uses asymmetry of the DNA strands to generate a regular lineage of cellular differentiation.","authors":"Klar AJ","authors_abbrev":"Klar AJ","pubmed_publication_date":"2 Apr 1987","pubmed_entrez_date":"1987-04-02","publication_year":"1987","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7975894","title":"Mating pheromone-induced expression of the mat1-Pm gene of Schizosaccharomyces pombe: identification of signalling components and characterization of upstream controlling elements.","citation":"Yeast 1994 Jun;10(6):757-70","abstract":"Transcription of the mat1-Pm gene of Schizosaccharomyces pombe controlling entry into meiosis is stimulated by the mating pheromone, M-factor. We have studied its expression by monitoring beta-galactosidase activity in cells carrying a plasmid-borne mat1-Pm/lacZ fusion construct. Stimulation required the M-factor receptor (Map3) and other proteins (Gpa1, Byr1, Byr2 and Spk1) thought to be involved in propagating the pheromone signal within the cell. Mutational activation of gpa1 encoding an alpha subunit of the receptor-coupled heterotrimeric G protein causes full expression of mat1-Pm even in the absence of pheromone, suggesting that Gpa1 is a key signal transmitter. Furthermore, an activated ras1val17 mutant exhibited a much stronger level of induction than wild-type cells, though full expression needs M-factor treatment. Deletion analysis of the mat1-Pm promoter region identified a stretch of 21 bp that is shown to play a critical role in controlling expression. This region lies just upstream of a TATA-like box and contains a TR-box (TTCTTTGTTY) motif which is the recognition site of a putative transcription factor Ste11. Point mutations in the TR-box motif abolished the expression of mat1-Pm/lacZ. Almost no expression of mat1-Pm was detected in a ste11 deletion mutant, whereas overproduction of Ste11 greatly increased the expression.","authors":"Aono T, Yanai H, Miki F, Davey J, Shimoda C","authors_abbrev":"Aono T et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_session_key":"f3a65af2138844d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-18 15:45:04","canto_approved_date":"2025-09-02 17:19:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-31 11:10:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMTR.02","SPBC32C12.02","SPAC17H9.09c","SPAC31G5.09c","SPCC1442.01","SPAC23E2.03c","SPAC1565.04c","SPAC1D4.13","SPAC144.13c","SPBC1D7.05","SPAC3F10.10c","SPBC24C6.06"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2018-04-18"},{"uniquename":"PMID:19571361","title":"Variety in intracellular diffusion during the cell cycle.","citation":"Phys Biol 2009 Jul 01;6(2):025015","abstract":"During the cell cycle, the organization of the cytoskeletal network undergoes dramatic changes. In order to reveal possible changes of the viscoelastic properties in the intracellular space during the cell cycle we investigated the diffusion of endogenous lipid granules within the fission yeast Schizosaccharomyces Pombe using optical tweezers. The cell cycle was divided into interphase and mitotic cell division, and the mitotic cell division was further subdivided in its stages. During all stages of the cell cycle, the granules predominantly underwent subdiffusive motion, characterized by an exponent alpha that is also linked to the viscoelastic moduli of the cytoplasm. The exponent alpha was significantly smaller during interphase than during any stage of the mitotic cell division, signifying that the cytoplasm was more elastic during interphase than during division. We found no significant differences in the subdiffusive exponents from granules measured in different stages of cell division. Also, our results for the exponent displayed no significant dependence on the position of the granule within the cell. The observation that the cytoplasm is more elastic during interphase than during mitotic cell division is consistent with the fact that elastic cytoskeletal elements such as microtubules are less abundantly present during cell division than during interphase.","doi":"10.1088/1478-3975/6/2/025015","authors":"Selhuber-Unkel C, Yde P, Berg-Sørensen K, Oddershede LB","authors_abbrev":"Selhuber-Unkel C et al.","pubmed_publication_date":"01 Jul 2009","pubmed_entrez_date":"2009-07-03","publication_year":"2009","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15177023","title":"CLIP-170 family members: a motor-driven ride to microtubule plus ends.","citation":"Dev Cell 2004 Jun;6(6):746-8","abstract":"CLIP-170 family proteins regulate microtubule plus end dynamics. Two reports published in this issue of Developmental Cell show that Bik1 and tip1p, the CLIP-170-like proteins of budding and fission yeast, are carried to microtubule plus ends by kinesin motor proteins. These findings indicate a complex interplay between microtubule-associated proteins and suggest a novel mechanism by which kinesin proteins stabilize microtubules.","authors":"Maekawa H, Schiebel E","authors_abbrev":"Maekawa H et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-06-05","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF14640","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:28464","SPBP22H7.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26821940","title":"Boolean Models of Biological Processes Explain Cascade-Like Behavior.","citation":"Sci Rep 2016 Jan 29;7:20067","abstract":"Biological networks play a key role in determining biological function and therefore, an understanding of their structure and dynamics is of central interest in systems biology. In Boolean models of such networks, the status of each molecule is either \"on\" or \"off\" and along with the molecules interact with each other, their individual status changes from \"on\" to \"off\" or vice-versa and the system of molecules in the network collectively go through a sequence of changes in state. This sequence of changes is termed a biological process. In this paper, we examine the common perception that events in biomolecular networks occur sequentially, in a cascade-like manner, and ask whether this is likely to be an inherent property. In further investigations of the budding and fission yeast cell-cycle, we identify two generic dynamical rules. A Boolean system that complies with these rules will automatically have a certain robustness. By considering the biological requirements in robustness and designability, we show that those Boolean dynamical systems, compared to an arbitrary dynamical system, statistically present the characteristics of cascadeness and sequentiality, as observed in the budding and fission yeast cell- cycle. These results suggest that cascade-like behavior might be an intrinsic property of biological processes.","doi":"10.1038/srep20067","authors":"Chen H, Wang G, Simha R, Du C, Zeng C","authors_abbrev":"Chen H et al.","pubmed_publication_date":"29 Jan 2016","pubmed_entrez_date":"2016-01-30","publication_year":"2016","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2016-01-31 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11832950","title":"RanGAP mediates GTP hydrolysis without an arginine finger.","citation":"Nature 2002 Feb 07;415(6872):662-6","abstract":"GTPase-activating proteins (GAPs) increase the rate of GTP hydrolysis on guanine nucleotide-binding proteins by many orders of magnitude. Studies with Ras and Rho have elucidated the mechanism of GAP action by showing that their catalytic machinery is both stabilized by GAP binding and complemented by the insertion of a so-called 'arginine finger' into the phosphate-binding pocket. This has been proposed as a universal mechanism for GAP-mediated GTP hydrolysis. Ran is a nuclear Ras-related protein that regulates both transport between the nucleus and cytoplasm during interphase, and formation of the mitotic spindle and/or nuclear envelope in dividing cells. Ran-GTP is hydrolysed by the combined action of Ran-binding proteins (RanBPs) and RanGAP. Here we present the three-dimensional structure of a Ran-RanBP1-RanGAP ternary complex in the ground state and in a transition-state mimic. The structure and biochemical experiments show that RanGAP does not act through an arginine finger, that the basic machinery for fast GTP hydrolysis is provided exclusively by Ran and that correct positioning of the catalytic glutamine is essential for catalysis.","authors":"Seewald MJ, Körner C, Wittinghofer A, Vetter IR","authors_abbrev":"Seewald MJ et al.","pubmed_publication_date":"07 Feb 2002","pubmed_entrez_date":"2002-02-08","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22E12.07"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"1k5g","gene_chains":[{"gene_uniquename":"SPAC22E12.07","chain":"C/F/I/L","position":"1-386"}],"title":"Crystal structure of Ran-GDP-AlFx-RanBP1-RanGAP complex","entry_authors":"Seewald MJ,Koerner C,Wittinghofer A,Vetter IR","entry_authors_abbrev":"Seewald MJ et al.","reference_uniquename":"PMID:11832950","experimental_method":"X-ray","resolution":"3.1"},{"pdb_id":"1k5d","gene_chains":[{"gene_uniquename":"SPAC22E12.07","chain":"C/F/I/L","position":"1-386"}],"title":"Crystal structure of Ran-GPPNHP-RanBP1-RanGAP complex","entry_authors":"Seewald MJ,Koerner C,Wittinghofer A,Vetter IR","entry_authors_abbrev":"Seewald MJ et al.","reference_uniquename":"PMID:11832950","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:23459708","title":"The prefoldin bud27 mediates the assembly of the eukaryotic RNA polymerases in an rpb5-dependent manner.","citation":"PLoS Genet 2013;9(2):e1003297","abstract":"The unconventional prefoldin URI/RMP, in humans, and its orthologue in yeast, Bud27, have been proposed to participate in the biogenesis of the RNA polymerases. However, this role of Bud27 has not been confirmed and is poorly elucidated. Our data help clarify the mechanisms governing biogenesis of the three eukaryotic RNA pols. We show evidence that Bud27 is the first example of a protein that participates in the biogenesis of the three eukaryotic RNA polymerases and the first example of a protein modulating their assembly instead of their nuclear transport. In addition we demonstrate that the role of Bud27 in RNA pols biogenesis depends on Rpb5. In fact, lack of BUD27 affects growth and leads to a substantial accumulation of the three RNA polymerases in the cytoplasm, defects offset by the overexpression of RPB5. Supporting this, our data demonstrate that the lack of Bud27 affects the correct assembly of Rpb5 and Rpb6 to the three RNA polymerases, suggesting that this process occurs in the cytoplasm and is a required step prior to nuclear import. Also, our data support the view that Rpb5 and Rpb6 assemble somewhat later than the rest of the complexes. Furthermore, Bud27 Rpb5-binding but not PFD-binding domain is necessary for RNA polymerases biogenesis. In agreement, we also demonstrate genetic interactions between BUD27, RPB5, and RPB6. Bud27 shuttles between the nucleus and the cytoplasm in an Xpo1-independent manner, and also independently of microtubule polarization and possibly independently of its association with the RNA pols. Our data also suggest that the role of Bud27 in RNA pols biogenesis is independent of the chaperone prefoldin (PFD) complex and of Iwr1. Finally, the role of URI seems to be conserved in humans, suggesting conserved mechanisms in RNA pols biogenesis.","doi":"10.1371/journal.pgen.1003297","authors":"Mirón-García MC, Garrido-Godino AI, García-Molinero V, Hernández-Torres F, Rodríguez-Navarro S, Navarro F","authors_abbrev":"Mirón-García MC et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-03-06","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.07c","HGNC:13236"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21429938","title":"Functional interactions of Rec24, the fission yeast ortholog of mouse Mei4, with the meiotic recombination-initiation complex.","citation":"J Cell Sci 2011 Apr 15;124(Pt 8):1328-38","abstract":"A physical connection between each pair of homologous chromosomes is crucial for reductional chromosome segregation during the first meiotic division and therefore for successful meiosis. Connection is provided by recombination (crossing over) initiated by programmed DNA double-strand breaks (DSBs). Although the topoisomerase-like protein Spo11 makes DSBs and is evolutionarily conserved, how Spo11 (Rec12 in fission yeast) is regulated to form DSBs at the proper time and place is poorly understood. Several additional (accessory) proteins for DSB formation have been inferred in different species from yeast to mice. Here, we show that Rec24 is a bona fide accessory protein in Schizosaccharomyces pombe. Rec24 is required genome-wide for crossing-over and is recruited to meiotic chromosomes during prophase in a Rec12-independent manner forming foci on linear elements (LinEs), structurally related to the synaptonemal complex of other eukaryotes. Stabilization of Rec24 on LinEs depends on another accessory protein, Rec7, with which Rec24 forms complexes in vivo. We propose that Rec24 marks LinE-associated recombination sites, that stabilization of its binding by Rec7 facilitates the loading or activation of Rec12, and that only stabilized complexes containing Rec24 and Rec7 promote DSB formation. Based on the recent report of Rec24 and Rec7 conservation, interaction between Rec24 and Rec7 might be widely conserved in DSB formation.","doi":"10.1242/jcs.079194","authors":"Bonfils S, Rozalén AE, Smith GR, Moreno S, Martín-Castellanos C","authors_abbrev":"Bonfils S et al.","pubmed_publication_date":"15 Apr 2011","pubmed_entrez_date":"2011-03-25","publication_year":"2011","canto_session_key":"e0b19b097d1d703d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-04-22 13:22:26","canto_approved_date":"2020-04-22 13:39:28","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-04-22 13:39:20","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPAC13C5.07","HGNC:43638","SPAC1952.15c","SPCC1753.03c","SPAC25G10.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-04-22"},{"uniquename":"PMID:118371","title":"Reversion of nonsense mutants induced by 4-nitroquinoline-1-oxide in Schizosaccharomyces pombe.","citation":"Mutat Res 1979 Nov;63(1):11-9","abstract":"We have studied the reversion of 8 nonsense alleles located in 7 different genes of Schizosaccharomyces pombe using 4-nitroquinoline-1-oxide (NQO) as a mutagenic agent. The nonsense mutants of S. pombe have been classified according to their suppressibility by defined opal and ochre suppressors into a class of efficiently suppressed opal and a class of inefficiency suppressed ochre mutants. The UGA alleles tested all revert consistently with NQO, in agreement with the high specificity of this mutagen for G-residues reported for bacteria and yeast. The UAA alleles show a lack or a low level of reversion with NQO. This low level of reversion is due to the low level of non-G-specific transversions at A sites of the UAA triplet. Within each class of nonsense mutants the extent of induction is site-dependent. We conclude that NQO acts predominantly on G-residues in S. pombe.","authors":"Janner F, Flury F, Leupold U","authors_abbrev":"Janner F et al.","pubmed_publication_date":"Nov 1979","pubmed_entrez_date":"1979-11-01","publication_year":"1979","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3955656","title":"cdc25+ functions as an inducer in the mitotic control of fission yeast.","citation":"Cell 1986 Apr 11;45(1):145-53","abstract":"In the fission yeast S. pombe the cdc25+ gene function is required to initiate mitosis. We have cloned the cdc25+ gene and have found that increased cdc25+ expression causes mitosis to initiate at a reduced cell size. This shows that cdc25+ functions as a dosage-dependent inducer in mitotic control, the first such mitotic control element to be specifically identified. DNA sequencing of the cdc25+ gene has shown that it can encode a protein of MW 67,000. Evidence is described showing that cdc25+ functions to counteract the activity of the mitotic inhibitor wee1+, and indicating that both mitotic control elements act independently to regulate the initiation of mitosis.","authors":"Russell P, Nurse P","authors_abbrev":"Russell P et al.","pubmed_publication_date":"11 Apr 1986","pubmed_entrez_date":"1986-04-11","publication_year":"1986","canto_session_key":"d059583508b7eaab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-21 14:39:32","canto_approved_date":"2019-06-14 13:14:13","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-19 14:11:35","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-11-21"},{"uniquename":"PMID:32541066","title":"RecQ DNA Helicase Rqh1 Promotes Rad3 ATR  Kinase Signaling in the DNA Replication Checkpoint Pathway of Fission Yeast.","citation":"Mol Cell Biol 2020 Aug 14;40(17)","abstract":"Rad3 is the orthologue of ATR and the sensor kinase of the DNA replication checkpoint in  Schizosaccharomyces pombe  Under replication stress, it initiates checkpoint signaling at the forks necessary for maintaining genome stability and cell survival. To better understand the checkpoint initiation process, we have carried out a genetic screen in fission yeast by random mutation of the genome, looking for mutants defective in response to the replication stress induced by hydroxyurea. In addition to the previously reported mutant with a C-to-Y change at position 307 encoded by  tel2  ( tel2-C307Y  mutant) (Y.-J. Xu, S. Khan, A. C. Didier, M. Wozniak, et al., Mol Cell Biol 39:e00175-19, 2019, https://doi.org/10.1128/MCB.00175-19), this screen has identified six mutations in  rqh1  encoding a RecQ DNA helicase. Surprisingly, these  rqh1  mutations, except for a start codon mutation, are all in the helicase domain, indicating that the helicase activity of Rqh1 plays an important role in the replication checkpoint. In support of this notion, integration of two helicase-inactive mutations or deletion of  rqh1  generated a similar Rad3 signaling defect, and heterologous expression of human RECQ1, BLM, and RECQ4 restored the Rad3 signaling and partially rescued a  rqh1  helicase mutant. Therefore, the replication checkpoint function of Rqh1 is highly conserved, and mutations in the helicase domain of these human enzymes may cause the checkpoint defect and contribute to the cancer predisposition syndromes.","doi":"10.1128/MCB.00145-20","authors":"Ahamad N, Khan S, Xu YJ","authors_abbrev":"Ahamad N et al.","pubmed_publication_date":"14 Aug 2020","pubmed_entrez_date":"2020-06-17","publication_year":"2020","canto_session_key":"0ac1f18b32a38610","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yongjie Xu","canto_first_approved_date":"2026-06-16 13:24:19","canto_approved_date":"2026-06-24 06:22:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-06-01 16:04:50","canto_added_date":"2020-06-18 00:15:06","annotation_curators":[{"name":"Nafees Ahamad","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":78,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Yongjie Xu","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.13c","SPAC9.05","SPBC216.05","SPAC23A1.19c","SPCC1259.13","SPAC694.06c","SPBC25D12.04","SPAC2G11.12","SPAC20H4.04","SPCC18B5.11c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2026-06-16"},{"uniquename":"PMID:6121661","title":"The mitochondrial adenosine triphosphatase of Acanthamoeba castellanii. Partial characterization and changes in activity during exponential growth.","citation":"Comp Biochem Physiol B 1982;71(3):495-500","abstract":"1. The mitochondrial adenosine triphosphatase (ATPase) of Acanthamoeba castellanii is Mg2+-requiring (optimum cation: ATP ratio of 1.5) and has two pH optima of activity (at pH 6.6 and 8.1). 2. ATPase activity of submitochondrial particles is effectively inhibited by twelve different inhibitors of energy conservation suggesting similarities in inhibitor-binding sites to other previously characterized complexes. 3. Gel filtration by passage through Sephadex G-50 increases ATPase activity of submitochondrial particles between 1.5 and 3.5 fold indicating the presence of a low molecular weight inhibitor protein. 4. After removal of the inhibitor protein, sensitivity to inhibitors of energy conservation decreases by between 1.5 and 14 fold. Crude F1-inhibitor preparations from A. castellanii, Schizosaccharomyces pombe, Tetrahymena pyriformis and bovine heart also inhibit ATPase activity. 5. Large variations in ATPase activity, F1-inhibitor protein activity, and amounts of immunologically-determined ATPase protein were observed during exponential growth, and the correlation between changes in these measurements is discussed. 6. The results are also discussed highlighting the similarities between the mitochondrial ATPase of A. castellanii and other mitochondrial ATPases.","authors":"Edwards SW, Evans JB, Lloyd D","authors_abbrev":"Edwards SW et al.","pubmed_publication_date":"1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30026545","title":"Structure of the replication regulator Sap1 reveals functionally important interfaces.","citation":"Sci Rep 2018 Jul 19;8(1):10930","abstract":"The mechanism by which specific protein-DNA complexes induce programmed replication fork stalling in the eukaryotic genome remains poorly understood. In order to shed light on this process we carried out structural investigations on the essential fission yeast protein Sap1. Sap1 was identified as a protein involved in mating-type switching in Schizosaccharomyces pombe, and has been shown to be involved in programmed replication fork stalling. Interestingly, Sap1 assumes two different DNA binding modes. At the mating-type locus dimers of Sap1 bind the SAS1 sequence in a head-to-head arrangement, while they bind to replication fork blocking sites at rDNA and Tf2 transposons in a head-to-tail mode. In this study, we have solved the crystal structure of the Sap1 DNA binding domain and we observe that Sap1 molecules interact in the crystal using a head-to-tail arrangement that is compatible with DNA binding. We find that Sap1 mutations which alleviate replication-fork blockage at Tf2 transposons in CENP-B mutants map to the head-to-tail interface. Furthermore, several other mutations introduced in this interface are found to be lethal. Our data suggests that essential functions of Sap1 depend on its head-to-tail oligomerization.","doi":"10.1038/s41598-018-29198-9","authors":"Jørgensen MM, Ekundayo B, Zaratiegui M, Skriver K, Thon G, Schalch T","authors_abbrev":"Jørgensen MM et al.","pubmed_publication_date":"19 Jul 2018","pubmed_entrez_date":"2018-07-21","publication_year":"2018","canto_session_key":"487eeff6dd0bb3e7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-08-13 10:48:24","canto_approved_date":"2022-01-19 13:05:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-13 10:03:30","canto_added_date":"2018-07-23 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.02c","SPBC1105.04c","SPAC9E9.10c","SPAPJ760.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-08-13","pdb_entries":[{"pdb_id":"6exu","gene_chains":[{"gene_uniquename":"SPCC1672.02c","chain":"A","position":"18-133"}],"title":"Crystal structure of the DNA binding domain of fission yeast Sap1","entry_authors":"Ekundayo B,Joergensen M,Schalch T","entry_authors_abbrev":"Ekundayo B et al.","reference_uniquename":"PMID:30026545","experimental_method":"X-ray","resolution":"1.409"},{"pdb_id":"6ext","gene_chains":[{"gene_uniquename":"SPCC1672.02c","chain":"A","position":"18-133"}],"title":"Crystal structure of the DNA binding domain of fission yeast Sap1","entry_authors":"Ekundayo B,Joergensen M,Schalch T","entry_authors_abbrev":"Ekundayo B et al.","reference_uniquename":"PMID:30026545","experimental_method":"X-ray","resolution":"1.5"}]},{"uniquename":"EMBL:SPU76637","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15970692","title":"New end take off: regulating cell polarity during the fission yeast cell cycle.","citation":"Cell Cycle 2005 Aug;4(8):1046-9","abstract":"Cell polarization is a major event of the cell cycle and underlies the function of most cells. Cell polarity is often achieved through the coordinated organization of the microtubule and act in cytoskeletons. Dramatic changes in cell polarization occur during the cell cycle and are subject to regulation by cell cycle controls. Cells of the fission yeast Schizosaccharomyces pombe grow by tip extension in a cell cycle-controlled manner. During G2 phase, these cells exhibit a transition in cell polarization known as New End Take Off (NETO), in which monopolar cells initiate bipolar growth. Dynamic microtubules contribute to this process by depositing at cell ends the microtubule plus end proteins tea1p and tea4p, which are necessary for NETO. We discuss here how these proteins may recruit for 3p, a formin responsible for actin nucleation, as well as two other actin binding proteins, bud6p and sla2p, to initiate cell polarization at the new end of the cell. Thus, the study of NETO is revealing a mechanism by which the plus ends of microtubules regulate the spatial organization of actin.","authors":"Martin SG, Chang F","authors_abbrev":"Martin SG et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-06-23","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16429127","title":"Genomic mapping of single-stranded DNA in hydroxyurea-challenged yeasts identifies origins of replication.","citation":"Nat Cell Biol 2006 Feb;8(2):148-55","abstract":"During DNA replication one or both strands transiently become single stranded: first at the sites where initiation of DNA synthesis occurs (known as origins of replication) and subsequently on the lagging strands of replication forks as discontinuous Okazaki fragments are generated. We report a genome-wide analysis of single-stranded DNA (ssDNA) formation in the presence of hydroxyurea during DNA replication in wild-type and checkpoint-deficient rad53 Saccharomyces cerevisiae cells. In wild-type cells, ssDNA was first observed at a subset of replication origins and later 'migrated' bi-directionally, suggesting that ssDNA formation is associated with continuously moving replication forks. In rad53 cells, ssDNA was observed at virtually every known origin, but remained there over time, suggesting that replication forks stall. Telomeric regions seemed to be particularly sensitive to the loss of Rad53 checkpoint function. Replication origins in Schizosaccharomyces pombe were also mapped using our method.","authors":"Feng W, Collingwood D, Boeck ME, Fox LA, Alvino GM, Fangman WL, Raghuraman MK, Brewer BJ","authors_abbrev":"Feng W et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-01-24","publication_year":"2006","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19273851","title":"Recombination at DNA replication fork barriers is not universal and is differentially regulated by Swi1.","citation":"Proc Natl Acad Sci U S A 2009 Mar 24;106(12):4770-5","abstract":"DNA replication stress has been implicated in the etiology of genetic diseases, including cancers. It has been proposed that genomic sites that inhibit or slow DNA replication fork progression possess recombination hotspot activity and can form potential fragile sites. Here we used the fission yeast, Schizosaccharomyces pombe, to demonstrate that hotspot activity is not a universal feature of replication fork barriers (RFBs), and we propose that most sites within the genome that form RFBs do not have recombination hotspot activity under nonstressed conditions. We further demonstrate that Swi1, the TIMELESS homologue, differentially controls the recombination potential of RFBs, switching between being a suppressor and an activator of recombination in a site-specific fashion.","doi":"10.1073/pnas.0807739106","authors":"Pryce DW, Ramayah S, Jaendling A, McFarlane RJ","authors_abbrev":"Pryce DW et al.","pubmed_publication_date":"24 Mar 2009","pubmed_entrez_date":"2009-03-11","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.06c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:26896331","title":"Conserved and Diverged Functions of the Calcineurin-Activated Prz1 Transcription Factor in Fission Yeast.","citation":"Genetics 2016 Apr;202(4):1365-75","abstract":"Gene regulation in response to intracellular calcium is mediated by the calcineurin-activated transcription factor Prz1 in the fission yeast Schizosaccharomyces pombe Genome-wide studies of the Crz1 and CrzA fungal orthologs have uncovered numerous target genes involved in conserved and species-specific cellular processes. In contrast, very few target genes of Prz1 have been published. This article identifies an extensive list of genes using transcriptome and ChIP-chip analyses under inducing conditions of Prz1, including CaCl2 and tunicamycin treatment, as well as a ∆pmr1 genetic background. We identified 165 upregulated putative target genes of Prz1 in which the majority contained a calcium-dependent response element in their promoters, similar to that of the Saccharomyces cerevisiae ortholog Crz1 These genes were functionally enriched for Crz1-conserved processes such as cell-wall biosynthesis. Overexpression of prz1(+)increased resistance to the cell-wall degradation enzyme zymolyase, likely from upregulation of theO-mannosyltransferase encoding gene omh1(+) Loss of omh1(+)abrogates this phenotype. We uncovered a novel inhibitory role in flocculation for Prz1. Loss of prz1(+)resulted in constitutive flocculation and upregulation of genes encoding the flocculins Gsf2 and Pfl3, as well as the transcription factor Cbf12. The constitutive flocculation of the ∆prz1 strain was abrogated by the loss of gsf2(+) or cbf12(+) This study reveals that Prz1 functions as a positive and negative transcriptional regulator of genes involved in cell-wall biosynthesis and flocculation, respectively. Moreover, comparison of target genes between Crz1/CrzA and Prz1 indicate some conservation in DNA-binding specificity, but also substantial rewiring of the calcineurin-mediated transcriptional regulatory network.","doi":"10.1534/genetics.115.184218","authors":"Chatfield-Reed K, Vachon L, Kwon EJ, Chua G","authors_abbrev":"Chatfield-Reed K et al.","pubmed_publication_date":"Apr 2016","pubmed_entrez_date":"2016-02-21","publication_year":"2016","canto_session_key":"51e5a16b29a56a78","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-22 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1742.01","SPAC4G8.13c","SPBC19C7.12c","SPAC8F11.10c","SPCC1223.13"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:12888492","title":"Fep1 represses expression of the fission yeast Schizosaccharomyces pombe siderophore-iron transport system.","citation":"Nucleic Acids Res 2003 Aug 01;31(15):4332-44","abstract":"When iron repletes, Schizosaccharomyces pombe cells repress transcription of genes encoding components involved in the reductive iron transport system. Fep1 mediates this transcriptional control by interacting specifically with GATA-type cis-acting elements. To further investigate the role that Fep1 plays in iron homeostasis, we searched for additional Fep1-regulated genes. We found that str1+ is subject to negative transcriptional regulation, which is exerted through binding of Fep1 to a single GATA element in the str1+ promoter. Introduction of str1+ into a Saccharomyces cerevisiae fet3Delta arn1-4Delta strain led to assimilation of iron from ferrichrome, revealing that Str1 functions as a siderophore-iron transporter in S.pombe. We also identified two additional target genes of Fep1, named str2+ and str3+. We demonstrate that the str1+, str2+ and str3+ genes share a common promoter element, 5'-(A/T)GATAA-3'. We found that the N-terminal 241 residue segment of Fep1 expressed in Escherichia coli specifically interacts with the 5'-(A/T)GATAA-3' element present in each of these promoters. Consistent with this, constitutive high level str1+, str2+ and str3+ gene expression was observed in a fep1Delta mutant strain. Taken together, these results demonstrate that Fep1 occupies a central role in coordinating transcriptional regulation of genes encoding components of the reductive and non-reductive iron transport systems in fission yeast.","authors":"Pelletier B, Beaudoin J, Philpott CC, Labbé S","authors_abbrev":"Pelletier B et al.","pubmed_publication_date":"01 Aug 2003","pubmed_entrez_date":"2003-07-31","publication_year":"2003","canto_session_key":"77214573d0c216fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-15 08:11:32","canto_approved_date":"2022-11-10 13:59:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-06-12 10:31:37","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.09","SPAC23E2.01","SPCC61.01c","SPAC1F7.08","SPAC1F8.03c","SPAC1F7.07c"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2017-09-15"},{"uniquename":"PMID:36174923","title":"Schizosaccharomyces pombe MAP kinase Sty1 promotes survival of Δppr10 cells with defective mitochondrial protein synthesis.","citation":"Int J Biochem Cell Biol 2022 Nov;152:106308","abstract":"Deletion of the Schizosaccharomyces pombe pentatricopeptide repeat gene ppr10 severely impairs mitochondrial translation, resulting in defective oxidative phosphorylation (OXPHOS). ppr10 deletion also induces iron starvation response, resulting in increased reactive oxygen species (ROS) production and reduced viability under fermentative conditions. S. pombe has two principal stress-response pathways, which are mediated by the mitogen-activated protein kinase Sty1 and the basic leucine zipper transcription factor Pap1, respectively. In this study, we examined the roles of Sty1 and Pap1 in the cellular response to the mitochondrial translation defect caused by ppr10 deletion. We found that ppr10 deletion resulted in two waves of stress protein activation. The early response occurred in exponential phase and resulted in the expression of a subset of stress proteins including Gst2 and Obr1. The upregulation of some of these stress proteins in Δppr10 cells in early response is dependent on the basal nuclear levels of Sty1 or Pap1. The late response occurred in early stationary phase and coincided with the stable localization of Sty1 and Pap1 in the nucleus, presumably resulting in persistent activation of a large set of stress proteins. Deletion of sty1 in Δppr10 cells caused severe defects in cell division and growth, and further impaired cell viability. Deletion of the mitochondrial superoxide dismutase gene sod2 whose expression is controlled by Sty1 severely inhibited the growth of Δppr10 cells. Overexpression of sod2 improves the viability of Δppr10 cells. Our results support an important role for Sty1 in counteracting stress induced by ppr10 deletion under fermentative growth conditions.","doi":"10.1016/j.biocel.2022.106308","authors":"Hu Y, Luo Y, Yin D, Zhao L, Wang Y, Yao R, Zhang P, Wu X, Li M, Hidalgo E, Huang Y","authors_abbrev":"Hu Y et al.","pubmed_publication_date":"Nov 2022","pubmed_entrez_date":"2022-09-29","publication_year":"2022","canto_session_key":"0ff28f78db735798","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2022-11-07 11:34:23","canto_approved_date":"2022-12-01 16:10:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-06 13:51:48","canto_added_date":"2022-10-01 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC354.12","SPBC3F6.03","SPCC1442.16c","SPCC663.08c","SPAC1783.07c","SPCC757.07c","SPCC965.07c","SPAC821.10c","SPBC609.04","SPAC24B11.06c","SPBC106.02c","SPBC3E7.02c","SPBC106.19","SPAC1486.01","SPAP8A3.04c","SPBC215.05","SPAC3C7.14c","SPAC22H10.13","SPAC688.04c","SPCC576.03c","SPBC32F12.03c","SPCC1281.07c","SPBC1105.14"],"gene_count":23,"ltp_gene_count":10,"approved_date":"2022-11-07"},{"uniquename":"PMID:17401136","title":"The role and aims of the FYSSION project.","citation":"Brief Funct Genomic Proteomic 2007 Mar;6(1):3-7","abstract":"FYSSION is a resource for researchers working on the fission yeast Schizosaccharomyces pombe. It currently comprises libraries of temperature-sensitive mutants in essential genes, and insertional mutants in non-essential genes, available for screening by visiting workers. Here we outline methods for constructing and using the libraries, and describe future prospects for functional genomics of this organism, here and elsewhere.","authors":"Armstrong J, Bone N, Dodgson J, Beck T","authors_abbrev":"Armstrong J et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-04-03","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26687354","title":"DNA Entry into and Exit out of the Cohesin Ring by an Interlocking Gate Mechanism.","citation":"Cell 2015 Dec 17;163(7):1628-40","abstract":"Structural maintenance of chromosome (SMC) complexes are proteinaceous rings that embrace DNA to enable vital chromosomal functions. The ring is formed by two SMC subunits, closed at a pair of ATPase heads, whose interaction is reinforced by a kleisin subunit. Using biochemical analysis of fission-yeast cohesin, we find that a similar series of events facilitates both topological entrapment and release of DNA. DNA-sensing lysines trigger ATP hydrolysis to open the SMC head interface, whereas the Wapl subunit disengages kleisin, but only after ATP rebinds. This suggests an interlocking gate mechanism for DNA transport both into and out of the cohesin ring. The entry direction is facilitated by a cohesin loader that appears to fold cohesin to expose the DNA sensor. Our results provide a model for dynamic DNA binding by all members of the SMC family and explain how lysine acetylation of cohesin establishes enduring sister chromatid cohesion.","doi":"10.1016/j.cell.2015.11.030","authors":"Murayama Y, Uhlmann F","authors_abbrev":"Murayama Y et al.","pubmed_publication_date":"17 Dec 2015","pubmed_entrez_date":"2015-12-22","publication_year":"2015","canto_session_key":"74dade3ace393390","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Frank Uhlmann","canto_first_approved_date":"2017-11-02 12:45:36","canto_approved_date":"2025-09-03 16:53:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-29 16:56:39","canto_added_date":"2015-12-23 01:19:29","annotation_curators":[{"name":"Frank Uhlmann","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.02","SPBC428.17c","SPAC10F6.09c","SPCC338.17c","SPAC31A2.05c","SPBC29A10.04","SPAC1687.18c","SPAC17H9.20"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-11-02"},{"uniquename":"PMID:41917004","title":"Nucleophagy is promoted by two autophagy receptors and inhibited by chromatin-nuclear envelope tethering in fission yeast.","citation":"Nat Commun 2026 Mar 31;","abstract":"Selective autophagy of the nucleus, known as nucleophagy, targets nuclear components for degradation. The molecular mechanisms underlying nucleophagy remain inadequately understood. In this study, we identify a nucleophagy receptor, Npr1, in the fission yeast Schizosaccharomyces pombe. Npr1 is an Atg8-binding multi-transmembrane protein localized to the outer nuclear membrane. It functions redundantly with another autophagy receptor, Epr1, to promote nitrogen starvation-induced nucleophagy. In the absence of both Npr1 and Epr1, starved cells exhibit abnormal nuclear morphology and reduced survival. During nucleophagy, the nuclear envelope (NE) forms outward protrusions where Atg8 co-localizes with Npr1 and/or Epr1. These protrusions subsequently detach from the NE, resulting in the formation of autophagosomes that contain nucleophagy cargo. Notably, artificially enhancing chromatin association with the inner nuclear membrane leads to NE protrusions that fail to detach, thereby aborting nucleophagy. Our findings provide mechanistic insights into nucleophagy and suggest that abortive nucleophagy protects chromatin from degradation.","doi":"10.1038/s41467-026-71237-x","authors":"Ma ZH, Pan ZQ, Jiang ZD, Shao GC, Hua Y, Suo F, Zou CX, Jiang YF, Dong MQ, Du LL","authors_abbrev":"Ma ZH et al.","pubmed_publication_date":"31 Mar 2026","pubmed_entrez_date":"2026-03-31","publication_year":"2026","canto_session_key":"17f564867a9d1ed8","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-06-01 06:32:19","canto_added_date":"2026-04-01 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26880539","title":"Biosynthesis of fluorescent CdS nanocrystals with semiconductor properties: Comparison of microbial and plant production systems.","citation":"J Biotechnol 2016 Apr 10;223:13-23","abstract":"This study investigated fission yeast (Schizosaccharomyces pombe) and hairy roots of tomato (Solanum lycopersicum) as in vitro production vehicles for biological synthesis of CdS quantum dots. Cd added during the mid-growth phase of the cultures was detoxified within the biomass into inorganic sulphide-containing complexes with the quantum confinement properties of semiconductor nanocrystals. Significant differences were found between the two host systems in terms of nanoparticle production kinetics, yield and quality. The much slower growth rate of hairy roots compared with yeast is a disadvantage for commercial scaled-up production. Nanoparticle extraction from the biomass was less effective for the roots: 19% of the Cd present in the hairy roots was recovered after extraction compared with 34% for the yeast. The overall yield of CdS quantum dots was also lower for the roots: relative to the amount of Cd taken up into the biomass, 8.5% was recovered in yeast gel filtration fractions exhibiting quantum dot properties whereas the result for hairy roots was only 0.99%. Yeast-produced CdS crystallites were somewhat smaller with diameters of approximately 2-6 nm compared with those of 4-10nm obtained from the roots. The average ratio of inorganic sulphide to Cd for the purified and size-fractionated particles was 0.44 for the yeast and 1.6 for the hairy roots. Despite the limitations associated with hairy roots in terms of culture kinetics and product yield, this system produced CdS nanoparticles with enhanced photostability and 3.7-13-fold higher fluorescence quantum efficiency compared with those generated by yeast. This work demonstrates that the choice of cellular host can have a significant effect on nanoparticle functional properties as well as on the bioprocessing aspects of biological quantum dot synthesis.","doi":"10.1016/j.jbiotec.2016.02.018","authors":"Al-Shalabi Z, Doran PM","authors_abbrev":"Al-Shalabi Z et al.","pubmed_publication_date":"10 Apr 2016","pubmed_entrez_date":"2016-02-17","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-02-19 01:15:23","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10196225","title":"Regions of Byr4, a regulator of septation in fission yeast, that bind Spg1 or Cdc16 and form a two-component GTPase-activating protein with Cdc16.","citation":"J Biol Chem 1999 Apr 16;274(16):11339-43","abstract":"In the fission yeast Schizosaccharomyces pombe, septation and constriction of the actomyosin ring for cell division are positively regulated by the Spg1 GTPase, a member of the Ras superfamily. Spg1 is negatively regulated by Byr4 and Cdc16, which together form a two-component GTPase-activating protein for the Spg1 GTPase. To better understand how Byr4 regulates septation, Byr4 mutants were tested for in vitro functions. This analysis revealed that Byr4 contained one Cdc16-binding site and four Spg1-binding sites (SBS), designated SBS1-SBS4. Although mutants with a single SBS bound Spg1 and inhibited GTP dissociation, the equilibrium binding affinity of these mutants was 28-280-fold weaker than Byr4. Because some Byr4 mutants with multiple SBSs bound Spg1 tighter than the corresponding mutants with a single SBS, multiple SBSs probably interact to cause the high affinity binding of Byr4 to Spg1. A region of Byr4 that bound Spg1, SBS4, and the region that bound Cdc16, Cdc16-binding site, was necessary and sufficient to form Cdc16-dependent Spg1GAP activity that was similar to that of wild-type Byr4 with Cdc16.","authors":"Furge KA, Cheng QC, Jwa M, Shin S, Song K, Albright CF","authors_abbrev":"Furge KA et al.","pubmed_publication_date":"16 Apr 1999","pubmed_entrez_date":"1999-04-10","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC222.10c","SPAC6F6.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:2839305","title":"Deficiency in both type I and type II DNA topoisomerase activities differentially affect rRNA and ribosomal protein synthesis in Schizosaccharomyces pombe.","citation":"Curr Genet 1988 Apr;13(4):305-14","abstract":"The synthesis of rRNA and r-proteins was studied in temperature-sensitive topoisomerase mutants of the fisson yeast Schizosaccharomyces pombe. To reduce the severity of heatshock response seen in the wild type strain, slow temperature shift-up of the cultures was used to inactivate the mutant topoisomerases. It was found that the temperature shift caused a large preferential reduction of rRNA synthesis in the top1top2 double mutant. In contrast, no preferential inhibition of rRNA synthesis was observed in top1 or top2 single mutants, although some reduction in the total RNA synthesis was observed in the top2 mutant. Thus, as observed with Saccharomyces cerevisiae (Brill et al. 1987), relaxation of supercoiled DNA structures by either topoisomerase I or II appears to be essential for efficient transcription of rRNA genes. Analysis of r-protein synthesis indicated that there were small decreases in the differential synthesis rates of r-proteins after temperature shift-up in the top1top2 mutant, but the observed negative effects on r-protein synthesis was much smaller than that on rRNA synthesis, and degradation of the newly synthesized r-proteins was observed. These observations indicate the apparent lack of tight coupling between rRNA and r-protein synthesis in S. pombe under these experimental conditions.","authors":"Yamagishi M, Nomura M","authors_abbrev":"Yamagishi M et al.","pubmed_publication_date":"Apr 1988","pubmed_entrez_date":"1988-04-01","publication_year":"1988","canto_session_key":"925f034befc20574","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-12-22 16:46:25","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-20 14:16:53","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.03c","SPBC1703.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-20"},{"uniquename":"PMID:9488736","title":"Fission yeast mitotic regulator Dsk1 is an SR protein-specific kinase.","citation":"J Biol Chem 1998 Mar 06;273(10):5963-9","abstract":"Intricate interplay may exist between pre-mRNA splicing and the cell division cycle, and fission yeast Dsk1 appears to play a role in such a connection. Previous genetic analyses have implicated Dsk1 in the regulation of chromosome segregation at the metaphase/anaphase transition. Yet, its protein sequence suggests that Dsk1 may function as a kinase specific for SR proteins, a family of pre-mRNA splicing factors containing arginine-serine repeats. Using an in vitro system with purified components, we showed that Dsk1 phosphorylated human and yeast SR proteins with high specificity. The Dsk1-phosphorylated SF2/ASF protein was recognized strongly by a monoclonal antibody (mAb104) known to bind the in vivo phosphoepitope shared by SR proteins, indicating that the phosphorylation sites resided in the RS domain. Moreover, the fission yeast U2AF65 homolog, Prp2/Mis11 protein, was phosphorylated more efficiently by Dsk1 than by a human SR protein-specific kinase, SRPK1. Thus, these in vitro results suggest that Dsk1 is a fission yeast SR protein-specific kinase, and Prp2/Mis11 is likely an in vivo target for Dsk1. Together with previous genetic data, the studies support the notion that Dsk1 may play a role in coordinating pre-mRNA splicing and the cell division cycle.","authors":"Tang Z, Yanagida M, Lin RJ","authors_abbrev":"Tang Z et al.","pubmed_publication_date":"06 Mar 1998","pubmed_entrez_date":"1998-04-16","publication_year":"1998","canto_session_key":"b08eb33b3cfbe948","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-23 17:32:35","canto_approved_date":"2023-12-24 11:07:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-26 14:26:06","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.07","SPBC530.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-03-23"},{"uniquename":"PMID:12842031","title":"UCS proteins: managing the myosin motor.","citation":"Curr Biol 2003 Jul 01;13(13):R525-7","abstract":"Recent studies indicate that myosin molecular motors interact inside cells with proteins containing a conserved 'UCS' domain. This appears to ensure proper folding of myosin heads so that they can perform their ATP-dependent actin-based motor functions.","authors":"Yu Q, Bernstein SI","authors_abbrev":"Yu Q et al.","pubmed_publication_date":"01 Jul 2003","pubmed_entrez_date":"2003-07-05","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8552099","title":"Schizosaccharomyces pombe pcr1+ encodes a CREB/ATF protein involved in regulation of gene expression for sexual development.","citation":"Mol Cell Biol 1996 Feb;16(2):704-11","abstract":"The Schizosaccharomyces pombe pcr1 gene encodes a bZIP protein that apparently belongs to the cyclic AMP response element (CRE)-binding protein/activating transcription factor family. The deduced pcr1 gene product consists of 171 amino acid residues and is most similar to the mammalian CRE-BP1. A glutathione S-transferase-Pcr1 fusion protein produced in Escherichia coli was able to bind specifically to the CRE motif in vitro. Analysis with anti-Pcr1 serum suggested that Pcr1 is included in the major CRE-binding factors present in the S. pombe cell extract. Disruption of the pcr1 gene was not lethal, but the disruptant showed cold-sensitive growth on rich medium. The disruptant was also inefficient in mating and sporulation, though it was not completely sterile. Expression of the ste11 gene, which encodes a key transcription factor for sexual development, was greatly reduced in the disruptant, and overexpression of ste11+ suppressed the deficiency of the pcr1 disruptant in sexual development. It has been shown that expression of ste11 is negatively regulated by cyclic AMP-dependent protein kinase (PKA) and that the loss of PKA activity results in ectopic sexual development. Disruption of pcr1 blocked ectopic sexual development. Furthermore, disruption of pcr1 reduced expression of fbp1, a glucose-repressible gene negatively regulated by PKA. These results suggest that Pcr1 is a putative transcriptional regulator whose activity may be controlled by PKA. Alternatively, its activity may be independent of PKA, and full induction of ste11 and fbp1 expression requires the function of Pcr1 in addition to elimination of the repression by PKA.","authors":"Watanabe Y, Yamamoto M","authors_abbrev":"Watanabe Y et al.","pubmed_publication_date":"Feb 1996","pubmed_entrez_date":"1996-02-01","publication_year":"1996","canto_session_key":"aefacb75b8af3f8a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-07-20 17:04:19","canto_approved_date":"2024-03-29 09:19:06","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-08-04 11:09:57","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPBC1198.14c","SPAC21E11.03c","SPBC106.10"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-07-20"},{"uniquename":"PMID:2827111","title":"Cloning and sequencing of Schizosaccharomyces pombe DNA topoisomerase I gene, and effect of gene disruption.","citation":"Nucleic Acids Res 1987 Dec 10;15(23):9727-39","abstract":"We cloned the structural gene topl+ for Schizosaccharomyces pombe DNA topoisomerase I (topo I) by hybridization. An eight-fold increase of topo I relaxing activity was obtained in S. pombe cells transformed with multicopy plasmid with topl+ insert. Nucleotide sequence determination showed a hypothetical coding frame interrupted by two short introns, encoding a 812 residue polypeptide (M.W. 94,000), 43 residues longer than and 47% homologous to Saccharomyces cerevisiae topo I. We show that the topl (null) strain made by gene disruption is viable, although its generation time is 20% longer than that of wild type. The topl locus is mapped in the long arm of chromosome II, using the Leu+ marker integrated with the cloned topl+ sequence. We constructed a double mutant topl (null) top2 (ts) and found its defective phenotype similar to that of previously obtained topl (heat sensitive) top2 (ts). The other double mutant topl (null) top2 (cs), however, was lethal. Our results suggest that topl+ gene of S. pombe is dispensable only if topo II activity is abundant.","authors":"Uemura T, Morino K, Uzawa S, Shiozaki K, Yanagida M","authors_abbrev":"Uemura T et al.","pubmed_publication_date":"10 Dec 1987","pubmed_entrez_date":"1987-12-10","publication_year":"1987","canto_session_key":"d21f20d1d014ccba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-06 09:16:33","canto_approved_date":"2024-03-29 10:12:51","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-01-28 11:40:07","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1703.14c","SPBC1A4.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-10-06"},{"uniquename":"PMID:12242291","title":"Phosphorylation of eukaryotic initiation factor 2 by heme-regulated inhibitor kinase-related protein kinases in Schizosaccharomyces pombe is important for fesistance to environmental stresses.","citation":"Mol Cell Biol 2002 Oct;22(20):7134-46","abstract":"Protein synthesis is regulated by the phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) in response to different environmental stresses. One member of the eIF2alpha kinase family, heme-regulated inhibitor kinase (HRI), is activated under heme-deficient conditions and blocks protein synthesis, principally globin, in mammalian erythroid cells. We identified two HRI-related kinases from Schizosaccharomyces pombe which have full-length homology with mammalian HRI. The two HRI-related kinases, named Hri1p and Hri2p, exhibit autokinase and kinase activity specific for Ser-51 of eIF2alpha, and both activities were inhibited in vitro by hemin, as previously described for mammalian HRI. Overexpression of Hri1p, Hri2p, or the human eIF2alpha kinase, double-stranded-RNA-dependent protein kinase (PKR), impeded growth of S. pombe due to elevated phosphorylation of eIF2alpha. Cells from strains with deletions of the hri1(+) and hri2(+) genes, individually or in combination, exhibited a reduced growth rate when exposed to heat shock or to arsenic compounds. Measurements of in vivo phosphorylation of eIF2alpha suggest that Hri1p and Hri2p differentially phosphorylate eIF2alpha in response to these stress conditions. These results demonstrate that HRI-related enzymes are not unique to vertebrates and suggest that these eIF2alpha kinases are important participants in diverse stress response pathways in some lower eukaryotes.","authors":"Zhan K, Vattem KM, Bauer BN, Dever TE, Chen JJ, Wek RC","authors_abbrev":"Zhan K et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-09-21","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G9.09c","SPAC222.07c","SPAC20G4.03c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:9421521","title":"Holliday junction resolvase in Schizosaccharomyces pombe has identical endonuclease activity to the CCE1 homologue YDC2.","citation":"Nucleic Acids Res 1998 Jan 15;26(2):594-601","abstract":"A novel Holliday junction resolving activity has been identified in fractionated cell extracts of the fission yeast Schizosaccharomyces pombe . The enzyme catalyses endonucleolytic cleavage of Holliday junction-containing chi DNA and synthetic four-way DNA junctions. The activity cuts with high specificity a synthetic four-way junction containing a 12 bp core of homologous sequences but has no activity on another four-way junction (with a fixed crossover point), a three-way junction, linear duplex DNA or duplex DNA containing six mismatched nucleotides in the centre. The major cleavage sites map as single nicks in the vicinity of the crossover point, 3' of a thymidine residue. These data indicate that the activity has a strong DNA structure selectivity as well as a limited sequence preference; features similar to the Holliday junction resolving enzymes RuvC of Escherichia coli and the mitochondrial CCE1 (cruciform-cuttingenzyme 1) of Saccharomyces cerevisiae. A putative homologue of CCE1 in S.pombe (YDC2_SCHPO) has been identified through a search of the sequence database. The open reading frame of this gene has been cloned and the encoded protein, YDC2, expressed in E.coli . The purified recombinant YDC2 exhibits Holliday junction resolvase activity and is, therefore, a functional S.pombe homologue of CCE1. The resolvase YDC2 shows the same substrate specificity and produces identical cleavage sites as the activity obtained from S. pombe cells. Both YDC2 and the cellular activity cleave Holliday junctions in both orientations to give nicks that can be ligated in vitro. The partially purified Holliday junction resolving enzyme in fission yeast is biochemically indistinguishable from recombinant YDC2 and appears to be the same protein.","authors":"Oram M, Keeley A, Tsaneva I","authors_abbrev":"Oram M et al.","pubmed_publication_date":"15 Jan 1998","pubmed_entrez_date":"1998-02-28","publication_year":"1998","canto_session_key":"1fe134924a2f43d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-09-02 10:59:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-02 10:59:15","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-02"},{"uniquename":"PMID:25103242","title":"Actin cable distribution and dynamics arising from cross-linking, motor pulling, and filament turnover.","citation":"Mol Biol Cell 2014 Oct 01;25(19):3006-16","abstract":"The growth of fission yeast relies on the polymerization of actin filaments nucleated by formin For3p, which localizes at tip cortical sites. These actin filaments bundle to form actin cables that span the cell and guide the movement of vesicles toward the cell tips. A big challenge is to develop a quantitative understanding of these cellular actin structures. We used computer simulations to study the spatial and dynamical properties of actin cables. We simulated individual actin filaments as semiflexible polymers in three dimensions composed of beads connected with springs. Polymerization out of For3p cortical sites, bundling by cross-linkers, pulling by type V myosin, and severing by cofilin are simulated as growth, cross-linking, pulling, and turnover of the semiflexible polymers. With the foregoing mechanisms, the model generates actin cable structures and dynamics similar to those observed in live-cell experiments. Our simulations reproduce the particular actin cable structures in myoVΔ cells and predict the effect of increased myosin V pulling. Increasing cross-linking parameters generates thicker actin cables. It also leads to antiparallel and parallel phases with straight or curved cables, consistent with observations of cells overexpressing α-actinin. Finally, the model predicts that clustering of formins at cell tips promotes actin cable formation.","doi":"10.1091/mbc.E14-05-0965","authors":"Tang H, Laporte D, Vavylonis D","authors_abbrev":"Tang H et al.","pubmed_publication_date":"01 Oct 2014","pubmed_entrez_date":"2014-08-09","publication_year":"2014","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2014-08-13 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9614178","title":"Heat stress activates fission yeast Spc1/StyI MAPK by a MEKK-independent mechanism.","citation":"Mol Biol Cell 1998 Jun;9(6):1339-49","abstract":"Fission yeast Spc1/StyI MAPK is activated by many environmental insults including high osmolarity, oxidative stress, and heat shock. Spc1/StyI is activated by Wis1, a MAPK kinase (MEK), which is itself activated by Wik1/Wak1/Wis4, a MEK kinase (MEKK). Spc1/StyI is inactivated by the tyrosine phosphatases Pyp1 and Pyp2. Inhibition of Pyp1 was recently reported to play a crucial role in the oxidative stress and heat shock responses. These conclusions were based on three findings: 1) osmotic, oxidative, and heat stresses activate Spc1/StyI in wis4 cells; 2) oxidative stress and heat shock activate Spc1/StyI in cells that express Wis1AA, in which MEKK consensus phosphorylation sites were replaced with alanine; and 3) Spc1/StyI is maximally activated in Deltapyp1 cells. Contrary to these findings, we report: 1) Spc1/StyI activation by osmotic stress is greatly reduced in wis4 cells; 2) wis1-AA and Deltawis1 cells have identical phenotypes; and 3) all forms of stress activate Spc1/StyI in Deltapyp1 cells. We also report that heat shock, but not osmotic or oxidative stress, activate Spc1 in wis1-DD cells, which express Wis1 protein that has the MEKK consensus phosphorylation sites replaced with aspartic acid. Thus osmotic and oxidative stress activate Spc1/StyI by a MEKK-dependent process, whereas heat shock activates Spc1/StyI by a novel mechanism that does not require MEKK activation or Pyp1 inhibition.","authors":"Shiozaki K, Shiozaki M, Russell P","authors_abbrev":"Shiozaki K et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-06-17","publication_year":"1998","canto_session_key":"93eee643544f462e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-09-14 16:09:22","canto_approved_date":"2022-02-02 17:18:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-30 10:17:29","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26F1.10c","SPBC409.07c","SPAC24B11.06c","SPAC9G1.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-09-14"},{"uniquename":"PMID:20739711","title":"Cooperation between the septins and the actomyosin ring and role of a cell-integrity pathway during cell division in fission yeast.","citation":"Genetics 2010 Nov;186(3):897-915","abstract":"A major question about cytokinesis concerns the role of the septin proteins, which localize to the division site in all animal and fungal cells but are essential for cytokinesis only in some cell types. For example, in Schizosaccharomyces pombe, four septins localize to the division site, but deletion of the four genes produces only a modest delay in cell separation. To ask if the S. pombe septins function redundantly in cytokinesis, we conducted a synthetic-lethal screen in a septin-deficient strain and identified seven mutations. One mutation affects Cdc4, a myosin light chain that is an essential component of the cytokinetic actomyosin ring. Five others cause frequent cell lysis during cell separation and map to two loci. These mutations and their dosage suppressors define a signaling pathway (including Rho1 and a novel arrestin) for repairing cell-wall damage. The seventh mutation affects the poorly understood RNA-binding protein Scw1 and severely delays cell separation when combined either with a septin mutation or with a mutation affecting the septin-interacting, anillin-like protein Mid2, suggesting that Scw1 functions in a pathway parallel to that of the septins. Taken together, our results suggest that the S. pombe septins participate redundantly in one or more pathways that cooperate with the actomyosin ring during cytokinesis and that a septin defect causes septum defects that can be repaired effectively only when the cell-integrity pathway is intact.","doi":"10.1534/genetics.110.119842","authors":"Wu JQ, Ye Y, Wang N, Pollard TD, Pringle JR","authors_abbrev":"Wu JQ et al.","pubmed_publication_date":"Nov 2010","pubmed_entrez_date":"2010-08-27","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC645.07","SPAC1006.06","SPBC1289.04c","SPAPYUG7.03c","SPBC12D12.04c","SPCC645.05c","SPAC4F10.11","SPBC30B4.01c","SPCC645.06c","SPCC16C4.07","SPAC4A8.05c","SPAC1F7.04","SPAP8A3.08","SPBC19G7.08c","SPAC9G1.11c"],"gene_count":15,"ltp_gene_count":15},{"uniquename":"PMID:31102246","title":"Chitin Synthesis and Degradation in Fungi: Biology and Enzymes.","citation":"Adv Exp Med Biol 2019;1142:153-167","abstract":"Chitin is one of the most important carbohydrates of the fungal cell wall, and is synthesized by chitin synthases. Chitin can be degraded by chitinases, which are important virulence factors in pathogenic fungi. Knowledge about the biosynthesis and degradation of chitin, and the enzymes responsible, has accumulated in recent years. In this review, we analyze the amino acid sequences of chitin synthases from several typical fungi. These enzymes can be divided into seven groups. While the different chitin synthases from a single fungus share a low degree of similarity, the same type of chitin synthase from different fungi shows high similarity. The number of chitinase genes in fungi display wide variation, from a single gene in Schizosaccharomyces pombe, to 36 genes in Trichoderma virens. Chitinases from different fungi can be divided into four groups. The functions of chitin synthases and chitinases in several typical fungi are summarized, and the crystal structures of chitinases and chitinase modification are also discussed.","doi":"10.1007/978-981-13-7318-3_8","authors":"Yang J, Zhang KQ","authors_abbrev":"Yang J et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-05-19","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28652406","title":"Deciphering the role of the signal- and Sty1 kinase-dependent phosphorylation of the stress-responsive transcription factor Atf1 on gene activation.","citation":"J Biol Chem 2017 Aug 18;292(33):13635-13644","abstract":"Adaptation to stress triggers the most dramatic shift in gene expression in fission yeast ( Schizosaccharomyces pombe ), and this response is driven by signaling via the MAPK Sty1. Upon activation, Sty1 accumulates in the nucleus and stimulates expression of hundreds of genes via the nuclear transcription factor Atf1, including expression of  atf1  itself. However, the role of stress-induced, Sty1-mediated Atf1 phosphorylation in transcriptional activation is unclear. To this end, we expressed Atf1 phosphorylation mutants from a constitutive promoter to uncouple Atf1 activity from endogenous, stress-activated Atf1 expression. We found that cells expressing a nonphosphorylatable Atf1 variant are sensitive to oxidative stress because of impaired transcription of a subset of stress genes whose expression is also controlled by another transcription factor, Pap1. Furthermore, cells expressing a phospho-mimicking Atf1 mutant display enhanced stress resistance, and although expression of the Pap1-dependent genes still relied on stress induction, another subset of stress-responsive genes was constitutively expressed in these cells. We also observed that, in cells expressing the phospho-mimicking Atf1 mutant, the presence of Sty1 was completely dispensable, with all stress defects of Sty1-deficient cells being suppressed by expression of the Atf1 mutant. We further demonstrated that Sty1-mediated Atf1 phosphorylation does not stimulate binding of Atf1 to DNA but, rather, establishes a platform of interactions with the basal transcriptional machinery to facilitate transcription initiation. In summary, our results provide evidence that Atf1 phosphorylation by the MAPK Sty1 is required for oxidative stress responses in fission yeast cells by promoting transcription initiation.","doi":"10.1074/jbc.M117.794339","authors":"Salat-Canela C, Paulo E, Sánchez-Mir L, Carmona M, Ayté J, Oliva B, Hidalgo E","authors_abbrev":"Salat-Canela C et al.","pubmed_publication_date":"18 Aug 2017","pubmed_entrez_date":"2017-06-28","publication_year":"2017","canto_session_key":"57346d6578962342","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Claudia Salat-Canela","canto_first_approved_date":"2020-05-30 15:40:03","canto_approved_date":"2026-06-26 07:53:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2022-03-16 16:56:34","canto_added_date":"2017-06-29 00:15:15","annotation_curators":[{"name":"Claudia Salat-Canela","community_curator":true,"annotation_count":57,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC21E11.03c","SPBC215.05","SPBC29B5.01","SPBC106.02c","SPAP8A3.04c","SPAC24B11.06c","SPAC1783.07c","SPBC3F6.03","SPCC757.07c","SPCC1442.10c"],"gene_count":10,"ltp_gene_count":5,"approved_date":"2020-05-30"},{"uniquename":"EMBL:AU006588","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25675824","title":"[Telomere maintenance by DNA damage sensor kinases, ATM and ATR].","citation":"Seikagaku 2014 Dec;86(6):812-6","abstract":"","authors":"Yamazaki H, Ishikawa F","authors_abbrev":"Yamazaki H et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2015-02-14","publication_year":"2014","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2015-03-25 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1152857","title":"On some properties of five mutator alleles in Schizosaccharomyces pombe.","citation":"Mutat Res 1975 Jul;29(1):155-7","abstract":"","authors":"Munz P","authors_abbrev":"Munz P","pubmed_publication_date":"Jul 1975","pubmed_entrez_date":"1975-07-01","publication_year":"1975","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2847913","title":"Involvement of cdc13+ in mitotic control in Schizosaccharomyces pombe: possible interaction of the gene product with microtubules.","citation":"EMBO J 1988 Aug;7(8):2321-7","abstract":"Previous genetic studies have shown that the fission yeast cdc13+ gene product interacts closely with the cdc2+ protein kinase during mitosis. Here, we have cloned the cdc13+ gene from a S. pombe gene bank by complementation of the temperature-sensitive defect of a cdc13-117 mutant strain. The complementing activity was localized to a 1.9-kb XbaI-NsiI DNA fragment, and nucleotide sequencing revealed a 1446-bp open reading frame. The predicted amino acid sequence contained 482 residues and was not homologous to any protein in a protein database. The cdc13+ gene function was confirmed to be essential for cell division since cells carrying a cdc13 null allele arrested with a cdc phenotype. However, unlike any existing temperature-sensitive cdc13 mutants, cdc13 null mutants arrested in G2 without septa or condensed chromosomes indicating that cdc13+ gene function is required at or prior to the initiation of mitotis. cdc13-117 mutant strains were found to be hypersensitive to the tubulin inhibitor thiabendazole. This observation suggests that the cdc13+ gene product, which is required for mitotic initiation, may interact with microtubules.","authors":"Booher R, Beach D","authors_abbrev":"Booher R et al.","pubmed_publication_date":"Aug 1988","pubmed_entrez_date":"1988-08-01","publication_year":"1988","canto_session_key":"f8a41c2a00c1e3eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-06-20 11:48:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-19 15:32:47","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-19"},{"uniquename":"PMID:15707942","title":"A high-throughput screen utilizing the fluorescence of riboflavin for identification of lumazine synthase inhibitors.","citation":"Anal Biochem 2005 Mar 01;338(1):124-30","abstract":"A high-throughput screening method based on the competitive binding of a lumazine synthase inhibitor and riboflavin to the active site of Schizosaccharomyces pombe lumazine synthase was developed. This assay is sensitive, simple, and robust. During assay development, all of the known active inhibitors tested were positively identified. Preliminary high-throughput screening in 384-well format resulted in a Z factor of 0.7. The approach utilizes a thermodynamic assay to bypass the problems associated with the instabilities of both lumazine synthase substrates that complicate the use of a kinetic assay in a high-throughput format, and it removes the time element from the assay, thus simplifying the procedure.","authors":"Chen J, Illarionov B, Bacher A, Fischer M, Haase I, Georg G, Ye QZ, Ma Z, Cushman M","authors_abbrev":"Chen J et al.","pubmed_publication_date":"01 Mar 2005","pubmed_entrez_date":"2005-02-15","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26432830","title":"MitoMiner v3.1, an update on the mitochondrial proteomics database.","citation":"Nucleic Acids Res 2016 Jan 04;44(D1):D1258-61","abstract":"Mitochondrial proteins remain the subject of intense research interest due to their implication in an increasing number of different conditions including mitochondrial and metabolic disease, cancer, and neuromuscular degenerative and age-related disorders. However, the mitochondrial proteome has yet to be accurately and comprehensively defined, despite many studies. To support mitochondrial research, we developed MitoMiner (http://mitominer.mrc-mbu.cam.ac.uk), a freely accessible mitochondrial proteomics database. MitoMiner integrates different types of subcellular localisation evidence with protein information from public resources, and so provides a comprehensive central resource for data on mitochondrial protein localisation. Here we report important updates to the database including the addition of subcellular immunofluorescent staining results from the Human Protein Atlas, computational predictions of mitochondrial targeting sequences, and additional large-scale mass-spectrometry and GFP tagging data sets. This evidence is shared across the 12 species in MitoMiner (now including Schizosaccharomyces pombe) by homology mapping. MitoMiner provides multiple ways of querying the data including simple text searches, predefined queries and custom queries created using the interactive QueryBuilder. For remote programmatic access, API's are available for several programming languages. This combination of data and flexible querying makes MitoMiner a unique platform to investigate mitochondrial proteins, with application in mitochondrial research and prioritising candidate mitochondrial disease genes.","doi":"10.1093/nar/gkv1001","authors":"Smith AC, Robinson AJ","authors_abbrev":"Smith AC et al.","pubmed_publication_date":"04 Jan 2016","pubmed_entrez_date":"2015-10-04","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-10-05 00:18:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPPROREVI","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3035538","title":"Analysis and in vivo disruption of the gene coding for calmodulin in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1987 Jun;84(11):3580-4","abstract":"Calmodulin is a low molecular weight calcium-binding protein that modulates many enzyme systems in eukaryotes. We have cloned the gene encoding calmodulin from the fission yeast, Schizosaccharomyces pombe, by using synthetic oligonucleotide probes that correspond to three distinct regions of Tetrahymena calmodulin. A 1.6-kilobase (kb) DNA fragment that hybridized to all of them contains a gene whose deduced product possesses 74% amino acid homology with bovine calmodulin. This gene, which is unique in the S. pombe genome and is named cam1, encodes 149 amino acids excluding the first methionine and is transcribed into mRNA of 1.2-kb length. It has an intron that apparently starts immediately after the initiation codon and is 126 bp long. S. pombe calmodulin exhibits more homology to vertebrate calmodulin than to that of the budding yeast, Saccharomyces cerevisiae. Gene disruption experiments revealed that cam1 gene function is essential for vegetative growth of S. pombe. Spores bearing disrupted cam1 halt growth soon after germination and rarely carry out the first cell division, indicating that calmodulin does not exist in excess in those cells.","authors":"Takeda T, Yamamoto M","authors_abbrev":"Takeda T et al.","pubmed_publication_date":"Jun 1987","pubmed_entrez_date":"1987-06-01","publication_year":"1987","canto_session_key":"82fb197db757d6eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-08-24 13:41:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-08-15 13:28:12","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-08-15"},{"uniquename":"PMID:40923761","title":"Intrinsically disordered region of Clr4/Suv39 regulates its enzymatic activity and ensures heterochromatin spreading.","citation":"Nucleic Acids Res 2025 Sep 05;53(17)","abstract":"Methylation of histone H3 at lysine 9 (H3K9me), a hallmark of heterochromatin, is catalyzed by Clr4/Suv39. Clr4/Suv39 contains two conserved domains-an N-terminal chromodomain and a C-terminal catalytic domain-connected by an intrinsically disordered region (IDR). Several mechanisms have been proposed to regulate Clr4/Suv39 activity, but how it is regulated under physiological conditions remains largely unknown. We found that the N-terminus of Clr4 interacts with its C-terminal catalytic domain and represses its enzymatic activity. Detailed biochemical analyses revealed that basic amino acid residues in the IDR are involved in this interaction. Amino acid substitutions of these residues weakened this interaction, thereby promoting Clr4 activity in vitro. Interestingly, cells expressing mutant Clr4 with these substitutions showed a silencing defect, which suggested additional roles of the IDR in vivo. Genetic analysis revealed that the IDR functions in H3K9me spreading and that this activity is functionally linked to the RNAi pathway. We also showed that Clr4 binds to RNAs via the IDR and that RNA attenuates Clr4 autoinhibition in vitro. Furthermore, the IDR was found to contribute to the targeting of nucleosomal substrates in vitro. These results reveal a novel function of the Clr4/Suv39 IDR in regulating its enzymatic activity and heterochromatin spreading.","doi":"10.1093/nar/gkaf878","authors":"Nakamura R, Hayashi A, Nakagawa R, Yoshimura Y, Horikoshi N, Kurumizaka H, Nakayama JI","authors_abbrev":"Nakamura R et al.","pubmed_publication_date":"05 Sep 2025","pubmed_entrez_date":"2025-09-09","publication_year":"2025","canto_session_key":"0aabc4b956895db7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-ichi Nakayama","canto_first_approved_date":"2026-04-07 08:31:14","canto_approved_date":"2026-04-07 08:31:14","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-03-10 01:41:24","canto_added_date":"2025-09-09 23:25:04","annotation_curators":[{"name":"Jun-ichi Nakayama","community_curator":true,"annotation_count":38,"orcid":"0000-0002-5597-8239","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":51,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPBC29B5.01","SPAC21E11.03c","SPCC11E10.08","SPCC736.11"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2026-04-07"},{"uniquename":"PMID:20679488","title":"Requirement for the phospho-H2AX binding module of Crb2 in double-strand break targeting and checkpoint activation.","citation":"Mol Cell Biol 2010 Oct;30(19):4722-31","abstract":"Activation of DNA damage checkpoints requires the rapid accumulation of numerous factors to sites of genomic lesions, and deciphering the mechanisms of this targeting is central to our understanding of DNA damage response. Histone modification has recently emerged as a critical element for the correct localization of damage response proteins, and one key player in this context is the fission yeast checkpoint mediator Crb2. Accumulation of Crb2 at ionizing irradiation-induced double-strand breaks (DSBs) requires two distinct histone marks, dimethylated H4 lysine 20 (H4K20me2) and phosphorylated H2AX (pH2AX). A tandem tudor motif in Crb2 directly binds H4K20me2, and this interaction is required for DSB targeting and checkpoint activation. Similarly, pH2AX is required for Crb2 localization to DSBs and checkpoint control. Crb2 can directly bind pH2AX through a pair of C-terminal BRCT repeats, but the functional significance of this binding has been unclear. Here we demonstrate that loss of its pH2AX-binding activity severely impairs the ability of Crb2 to accumulate at ionizing irradiation-induced DSBs, compromises checkpoint signaling, and disrupts checkpoint-mediated cell cycle arrest. These impairments are similar to that reported for abolition of pH2AX or mutation of the H4K20me2-binding tudor motif of Crb2. Intriguingly, a combined ablation of its two histone modification binding modules yields a strikingly additive reduction in Crb2 activity. These observations argue that binding of the Crb2 BRCT repeats to pH2AX is critical for checkpoint activity and provide new insight into the mechanisms of chromatin-mediated genome stability.","doi":"10.1128/MCB.00404-10","authors":"Sanders SL, Arida AR, Phan FP","authors_abbrev":"Sanders SL et al.","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2010-08-04","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.08c","SPCC18B5.03","SPAC19G12.06c","SPBC342.05"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"EMBL:SP32583","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7746853","title":"Regulation and mechanisms of gene amplification.","citation":"Philos Trans R Soc Lond B Biol Sci 1995 Jan 30;347(1319):49-56","abstract":"Amplification in rodent cells usually involves bridge-breakage-fusion (BBF) cycles initiated either by end-to-end fusion of sister chromatids, or by chromosome breakage. In contrast, in human cells, resistance to the antimetabolite N-(phosphonacetyl)-L-aspartate (PALA) can be mediated by several different mechanisms that lead to overexpression of the target enzyme carbamyl-P synthetase, aspartate transcarbamylase, dihydro-orotase (CAD). Mechanisms involving BBF cycles account for only a minority of CAD amplification events in the human fibrosarcoma cell line HT 1080. Here, formation of a 2p isochromosome and overexpression of CAD by other types of amplification events (and even without amplification) are much more prevalent. Broken DNA is recognized by mammalian cells with intact damage-recognition pathways, as a signal to arrest or to die. Loss of these pathways by, for example, loss of p53 or pRb tumour suppressor function, or by increased expression of ras and myc oncogenes, causes non-permissive rat and human cells to become permissive both for amplification and for other manifestations of DNA damage. In cells that are already permissive, amplification can be stimulated by overexpressing oncogenes such as c-myc or ras, or by damaging DNA in a variety of ways. To supplement genetic analysis of amplification in mammalian cells, an amplification selection has been established in Schizosaccharomyces pombe. Selection with LiCl yields cells with amplified sod2 genes in structures related to those observed in mammalian cells. The effect on amplification in S. pombe can now be tested for any mutation in a gene involved in repair of damaged DNA or in normal cellular responses to DNA damage.","authors":"Smith KA, Agarwal ML, Chernov MV, Chernova OB, Deguchi Y, Ishizaka Y, Patterson TE, Poupon MF, Stark GR","authors_abbrev":"Smith KA et al.","pubmed_publication_date":"30 Jan 1995","pubmed_entrez_date":"1995-01-30","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11238887","title":"Roles of the mitotic inhibitors Wee1 and Mik1 in the G(2) DNA damage and replication checkpoints.","citation":"Mol Cell Biol 2001 Mar;21(5):1499-508","abstract":"The G(2) DNA damage and DNA replication checkpoints in many organisms act through the inhibitory phosphorylation of Cdc2 on tyrosine-15. This phosphorylation is catalyzed by the Wee1/Mik1 family of kinases. However, the in vivo role of these kinases in checkpoint regulation has been unclear. We show that, in the fission yeast Schizosaccharomyces pombe, Mik1 is a target of both checkpoints and that the regulation of Mik1 is, on its own, sufficient to delay mitosis in response to the checkpoints. Mik1 appears to have two roles in the DNA damage checkpoint; one in the establishment of the checkpoint and another in its maintenance. In contrast, Wee1 does not appear to be involved in the establishment of either checkpoint.","authors":"Rhind N, Russell P","authors_abbrev":"Rhind N et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-03-10","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC11E3.09"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:42015185","title":"Contributions of DNA mechanics and trans-regulation to nucleosome positioning in Schizosaccharomyces pombe and its role in co-transcriptional splicing.","citation":"Epigenetics Chromatin 2026 Apr 21;","abstract":"","doi":"10.1186/s13072-026-00675-0","authors":"Liu G, Cang J, Du Z, Cui X, Zhao H, Liu J","authors_abbrev":"Liu G et al.","pubmed_publication_date":"21 Apr 2026","pubmed_entrez_date":"2026-04-22","publication_year":"2026","canto_session_key":"3952b406522f804c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733398","title":"Live Imaging of Chromosome Segregation during Meiosis in the Fission Yeast  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Sep 01;2017(9):pdb.prot091769","abstract":"This protocol describes the live observation of chromosome segregation during fission yeast meiosis. To visualize one chromosome of interest, the  lac  operator ( lacO  array) is integrated at its centromere-proximal locus, and the  lac  repressor (lacI)-GFP fusion protein is expressed in a haploid strain. This haploid strain, in which mCherry-tagged tubulin is also expressed exogenously to monitor meiotic progression, is crossed with a nonlabeled haploid strain to induce meiosis. GFP and mCherry signals in resulting zygotes are observed by a fluorescent microscopy during the progression of meiosis.","doi":"10.1101/pdb.prot091769","authors":"Yamashita A, Sakuno T, Watanabe Y, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"01 Sep 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21185791","title":"Simultaneous determination of D-amino acids by the coupling method of D-amino acid oxidase with high-performance liquid chromatography.","citation":"J Chromatogr B Analyt Technol Biomed Life Sci 2011 Nov 01;879(29):3190-5","abstract":"An enzymatic assay system of D-amino acids was established using the D-amino acid oxidase of Schizosaccharomyces pombe. In this method, the enzyme converts the D-amino acids to the corresponding α-keto acids, which are then reacted with 1,2-diamino-4,5-methylenedioxybenzene (DMB) in an organic solvent. The resultant fluorescent compounds are separated and quantified by high-performance liquid chromatography (HPLC). Use of an organic solvent following the α-keto acid modification with DMB prevents the non-enzymatic deamination of L-amino acids, which are generally present at much higher concentrations than D-amino acids in biological samples. With this method, D-Glu, D-Asn, D-Gln, D-Ala, D-Val, D-Leu, D-Phe, and D-Ile can be quantified in the order of micromolar, and other D-amino acids except D-Asp can be assayed within a sensitivity range of 50-100 μM. The established enzymatic method was used to analyze the d-amino acid contents in human urine. The concentration of D-Ser obtained using this enzymatic method (223 μM) was in good agreement with that obtained using the conventional HPLC method (198 μM). The enzymatic method also demonstrated that the human urine contained 5.45 μM of d-Ala and 0.91 μM of D-Asn. Both D-amino acids were difficult to be identified using the conventional method, because the large signals from L-amino acids masked those from d-amino acids. The enzymatic method that we have developed can circumvent this problem.","doi":"10.1016/j.jchromb.2010.12.005","authors":"Kato S, Kito Y, Hemmi H, Yoshimura T","authors_abbrev":"Kato S et al.","pubmed_publication_date":"01 Nov 2011","pubmed_entrez_date":"2010-12-28","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19563103","title":"Replication initiation point mapping: approach and implications.","citation":"Methods Mol Biol 2009;521:105-20","abstract":"Duplication of eukaryotic chromosomes begins from multiple sites called origins of replication, with DNA synthesis proceeding bidirectionally away from the origin. There is little detailed information available pertaining to whether replication initiates at specific sites or anywhere within a given origin. The development of replication initiation point (RIP) mapping has made it possible to map start sites for DNA synthesis at the nucleotide level. The key step in RIP mapping is the purification of nascent DNA, which is initiated by small RNA primers. For the removal of broken DNA fragments, we utilize lambda-exonuclease, which digests DNA, but leaves nascent strands intact as long as they have the RNA primer still attached. RIP mapping is a sensitive technique and has been successfully applied to single copy loci in both budding and fission yeast, archaebacteria, and human cells. Studies in yeast have shown that the binding site for the initiator, the origin recognition complex (ORC), lies immediately adjacent to the replication start point, which suggests that ORC directs the initiation machinery to a distinct site. Here, we present a detailed step-by-step protocol for RIP mapping of replication origins in budding yeast.","doi":"10.1007/978-1-60327-815-7_6","authors":"Das-Bradoo S, Bielinsky AK","authors_abbrev":"Das-Bradoo S et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16540522","title":"Nuclear RanGAP is required for the heterochromatin assembly and is reciprocally regulated by histone H3 and Clr4 histone methyltransferase in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2006 Jun;17(6):2524-36","abstract":"Although the Ran GTPase-activating protein RanGAP mainly functions in the cytoplasm, several lines of evidence indicate a nuclear function of RanGAP. We found that Schizosaccharomyces pombe RanGAP, SpRna1, bound the core of histone H3 (H3) and enhanced Clr4-mediated H3-lysine 9 (K9) methylation. This enhancement was not observed for methylation of the H3-tail containing K9 and was independent of SpRna1-RanGAP activity, suggesting that SpRna1 itself enhances Clr4-mediated H3-K9 methylation via H3. Although most SpRna1 is in the cytoplasm, some cofractionated with H3. Sprna1(ts) mutations caused decreases in Swi6 localization and H3-K9 methylation at all three heterochromatic regions of S. pombe. Thus, nuclear SpRna1 seems to be involved in heterochromatin assembly. All core histones bound SpRna1 and inhibited SpRna1-RanGAP activity. In contrast, Clr4 abolished the inhibitory effect of H3 on the RanGAP activity of SpRna1 but partially affected the other histones. SpRna1 formed a trimeric complex with H3 and Clr4, suggesting that nuclear SpRna1 is reciprocally regulated by histones, especially H3, and Clr4 on the chromatin to function for higher order chromatin assembly. We also found that SpRna1 formed a stable complex with Xpo1/Crm1 plus Ran-GTP, in the presence of H3.","authors":"Nishijima H, Nakayama J, Yoshioka T, Kusano A, Nishitani H, Shibahara K, Nishimoto T","authors_abbrev":"Nishijima H et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-03-17","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.06c","SPCC622.08c","SPBC8D2.04","SPCC622.09","SPBC428.08c","SPAC1834.03c","SPBC8D2.03c","SPAC1805.17","SPAC1834.04","SPAC22E12.07"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:29358048","title":"Establishment of DNA-DNA Interactions by the Cohesin Ring.","citation":"Cell 2018 Jan 25;172(3):465-477.e15","abstract":"The ring-shaped structural maintenance of chromosome (SMC) complexes are multi-subunit ATPases that topologically encircle DNA. SMC rings make vital contributions to numerous chromosomal functions, including mitotic chromosome condensation, sister chromatid cohesion, DNA repair, and transcriptional regulation. They are thought to do so by establishing interactions between more than one DNA. Here, we demonstrate DNA-DNA tethering by the purified fission yeast cohesin complex. DNA-bound cohesin efficiently and topologically captures a second DNA, but only if that is single-stranded DNA (ssDNA). Like initial double-stranded DNA (dsDNA) embrace, second ssDNA capture is ATP-dependent, and it strictly requires the cohesin loader complex. Second-ssDNA capture is relatively labile but is converted into stable dsDNA-dsDNA cohesion through DNA synthesis. Our study illustrates second-DNA capture by an SMC complex and provides a molecular model for the establishment of sister chromatid cohesion.","doi":"10.1016/j.cell.2017.12.021","authors":"Murayama Y, Samora CP, Kurokawa Y, Iwasaki H, Uhlmann F","authors_abbrev":"Murayama Y et al.","pubmed_publication_date":"25 Jan 2018","pubmed_entrez_date":"2018-01-24","publication_year":"2018","canto_session_key":"94ca468a0f015cd5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-04-17 08:57:09","canto_approved_date":"2023-08-29 06:39:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-24 09:25:50","canto_added_date":"2018-01-25 01:15:16","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.17c","SPCC1753.01c","SPCC23B6.05c","SPCC338.17c","SPBC660.13c","SPBC29A10.04","SPAC10F6.09c","SPAC1687.18c","SPAC31A2.05c","SPAC110.02","SPAC17H9.20"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2018-04-17"},{"uniquename":"PMID:28204585","title":"A short splicing isoform of HBS1L links the cytoplasmic exosome and SKI complexes in humans.","citation":"Nucleic Acids Res 2017 Feb 28;45(4):2068-2080","abstract":"The exosome complex is a major eukaryotic exoribonuclease that requires the SKI complex for its activity in the cytoplasm. In yeast, the Ski7 protein links both complexes, whereas a functional equivalent of the Ski7 has remained unknown in the human genome. Proteomic analysis revealed that a previously uncharacterized short splicing isoform of HBS1L (HBS1LV3) is the long-sought factor linking the exosome and SKI complexes in humans. In contrast, the canonical HBS1L variant, HBS1LV1, which acts as a ribosome dissociation factor, does not associate with the exosome and instead interacts with the mRNA surveillance factor PELOTA. Interestingly, both HBS1LV1 and HBS1LV3 interact with the SKI complex and HBS1LV1 seems to antagonize SKI/exosome supercomplex formation. HBS1LV3 contains a unique C-terminal region of unknown structure, with a conserved RxxxFxxxL motif responsible for exosome binding and may interact with the exosome core subunit RRP43 in a way that resembles the association between Rrp6 RNase and Rrp43 in yeast. HBS1LV3 or the SKI complex helicase (SKI2W) depletion similarly affected the transcriptome, deregulating multiple genes. Furthermore, half-lives of representative upregulated mRNAs were increased, supporting the involvement of HBS1LV3 and SKI2W in the same mRNA degradation pathway, essential for transcriptome homeostasis in the cytoplasm.","doi":"10.1093/nar/gkw862","authors":"Kalisiak K, Kuliński TM, Tomecki R, Cysewski D, Pietras Z, Chlebowski A, Kowalska K, Dziembowski A","authors_abbrev":"Kalisiak K et al.","pubmed_publication_date":"28 Feb 2017","pubmed_entrez_date":"2017-02-17","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1919.05","SPCC550.03c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:18547878","title":"Radiation induction of delayed recombination in Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2008 Aug 02;7(8):1250-61","abstract":"Ionizing radiation is known to induce delayed chromosome and gene mutations in the descendants of the irradiated tissue culture cells. Molecular mechanisms of such delayed mutations are yet to be elucidated, since high genomic complexity of mammalian cells makes it difficult to analyze. We now tested radiation induction of delayed recombination in the fission yeast Schizosaccharomyces pombe by monitoring the frequency of homologous recombination after X-irradiation. A reporter with 200 bp tandem repeats went through spontaneous recombination at a frequency of 1.0 x 10(-4), and the frequency increased dose-dependently to around 10 x 10(-4) at 500 Gy of X-irradiation. Although the repair of initial DNA damage was thought to be completed before the restart of cell division cycle, the elevation of the recombination frequency persisted for 8-10 cell generations after irradiation (delayed recombination). The delayed recombination suggests that descendants of the irradiated cells keep a memory of the initial DNA damage which upregulates recombination machinery for 8-10 generations even in the absence of DNA double-strand breaks (DSBs). Since radical scavengers were ineffective in inhibiting the delayed recombination, a memory by continuous production of DNA damaging agents such as reactive oxygen species (ROS) was excluded. Recombination was induced in trans in a reporter on chromosome III by a DNA DSB at a site on chromosome I, suggesting the untargeted nature of delayed recombination. Interestingly, Rad22 foci persisted in the X-irradiated population in parallel with the elevation of the recombination frequency. These results suggest that the epigenetic damage memory induced by DNA DSB upregulates untargeted and delayed recombination in S. pombe.","doi":"10.1016/j.dnarep.2008.04.006","authors":"Takeda J, Uematsu N, Shiraishi S, Toyoshima M, Matsumoto T, Niwa O","authors_abbrev":"Takeda J et al.","pubmed_publication_date":"02 Aug 2008","pubmed_entrez_date":"2008-06-13","publication_year":"2008","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15297457","title":"On the slowing of S phase in response to DNA damage in fission yeast.","citation":"J Biol Chem 2004 Oct 15;279(42):43574-80","abstract":"Eukaryotic cells slow their progression through S phase upon DNA damage. The mechanism that leads to this slowing is called the intra-S-phase checkpoint. Previous studies demonstrated that in the fission yeast Schizosaccharomyces pombe this checkpoint is mediated by a pathway that includes Rad3 (similar to human ATR and ATM) and Cds1 (similar to human Chk1 and Chk2). Here we present evidence that a major downstream target of this pathway is the cyclin-dependent kinase, Cdc2. We also present evidence suggesting that the intra-S-phase checkpoint makes a relatively minor contribution to the survival of cells with damaged DNA.","authors":"Kumar S, Huberman JA","authors_abbrev":"Kumar S et al.","pubmed_publication_date":"15 Oct 2004","pubmed_entrez_date":"2004-08-07","publication_year":"2004","canto_session_key":"59258724594b2b0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-22 11:24:57","canto_approved_date":"2022-09-24 13:57:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-17 09:28:16","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPCC18B5.11c","SPBC336.12c","SPBC660.14","SPAC24H6.05","SPBC216.05","SPBC11B10.09"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-12-22"},{"uniquename":"PMID:33010152","title":"A genetic screen for suppressors of hyper-repression of the fission yeast PHO regulon by Pol2 CTD mutation T4A implicates inositol 1-pyrophosphates as agonists of precocious lncRNA transcription termination.","citation":"Nucleic Acids Res 2020 Nov 04;48(19):10739-10752","abstract":"Fission yeast phosphate homeostasis genes are repressed in phosphate-rich medium by transcription of upstream lncRNAs that interferes with activation of the flanking mRNA promoters. lncRNA control of PHO gene expression is influenced by the Thr4 phospho-site in the RNA polymerase II CTD and the 3' processing/termination factors CPF and Rhn1, mutations of which result in hyper-repression of the PHO regulon. Here, we performed a forward genetic screen for mutations that de-repress Pho1 acid phosphatase expression in CTD-T4A cells. Sequencing of 18 independent STF (Suppressor of Threonine Four) isolates revealed, in every case, a mutation in the C-terminal pyrophosphatase domain of Asp1, a bifunctional inositol pyrophosphate (IPP) kinase/pyrophosphatase that interconverts 5-IP7 and 1,5-IP8. Focused characterization of two STF strains identified 51 coding genes coordinately upregulated vis-à-vis the parental T4A strain, including all three PHO regulon genes (pho1, pho84, tgp1). Whereas these STF alleles-asp1-386(Stop) and asp1-493(Stop)-were lethal in a wild-type CTD background, they were viable in combination with mutations in CPF and Rhn1, in which context Pho1 was also de-repressed. Our findings implicate Asp1 pyrophosphatase in constraining 1,5-IP8 or 1-IP7 synthesis by Asp1 kinase, without which 1-IPPs can accumulate to toxic levels that elicit precocious termination by CPF/Rhn1.","doi":"10.1093/nar/gkaa776","authors":"Garg A, Shuman S, Schwer B","authors_abbrev":"Garg A et al.","pubmed_publication_date":"04 Nov 2020","pubmed_entrez_date":"2020-10-03","publication_year":"2020","canto_session_key":"a6782fab5fd233d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Angad Garg","canto_first_approved_date":"2022-12-01 12:45:29","canto_approved_date":"2023-04-03 11:46:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-30 10:11:47","canto_added_date":"2020-10-05 00:15:05","annotation_curators":[{"name":"Angad Garg","community_curator":true,"annotation_count":65,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.03","SPCC1672.06c","SPCC74.02c","SPBC776.02c","SPAC3G9.04","SPBC28F2.12","SPBC3B9.11c","SPAC824.04","SPBP4G3.02"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2022-12-01"},{"uniquename":"PMID:36062570","title":"RMDisease V2.0: an updated database of genetic variants that affect RNA modifications with disease and trait implication.","citation":"Nucleic Acids Res 2023 Jan 06;51(D1):D1388-D1396","abstract":"Recent advances in epitranscriptomics have unveiled functional associations between RNA modifications (RMs) and multiple human diseases, but distinguishing the functional or disease-related single nucleotide variants (SNVs) from the majority of 'silent' variants remains a major challenge. We previously developed the RMDisease database for unveiling the association between genetic variants and RMs concerning human disease pathogenesis. In this work, we present RMDisease v2.0, an updated database with expanded coverage. Using deep learning models and from 873 819 experimentally validated RM sites, we identified a total of 1 366 252 RM-associated variants that may affect (add or remove an RM site) 16 different types of RNA modifications (m6A, m5C, m1A, m5U, Ψ, m6Am, m7G, A-to-I, ac4C, Am, Cm, Um, Gm, hm5C, D and f5C) in 20 organisms (human, mouse, rat, zebrafish, maize, fruit fly, yeast, fission yeast, Arabidopsis, rice, chicken, goat, sheep, pig, cow, rhesus monkey, tomato, chimpanzee, green monkey and SARS-CoV-2). Among them, 14 749 disease- and 2441 trait-associated genetic variants may function via the perturbation of epitranscriptomic markers. RMDisease v2.0 should serve as a useful resource for studying the genetic drivers of phenotypes that lie within the epitranscriptome layer circuitry, and is freely accessible at: www.rnamd.org/rmdisease2.","doi":"10.1093/nar/gkac750","authors":"Song B, Wang X, Liang Z, Ma J, Huang D, Wang Y, de Magalhães JP, Rigden DJ, Meng J, Liu G, Chen K, Wei Z","authors_abbrev":"Song B et al.","pubmed_publication_date":"06 Jan 2023","pubmed_entrez_date":"2022-09-05","publication_year":"2023","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2022-09-08 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12684881","title":"A defect in a fatty acyl-CoA synthetase gene, lcf1+, results in a decrease in viability after entry into the stationary phase in fission yeast.","citation":"Mol Genet Genomics 2003 Jul;269(4):437-42","abstract":"An intriguing mutant was isolated in Schizosaccharomyces pombe, which is defective in the maintenance of viability after entry into the stationary phase. In the logarithmic growth phase, the mutant cells grow at the same rate as the parental cells. Upon the onset of the stationary phase, however, the mutant cells lose viability very rapidly. It was found that this phenotype was due to a mutational lesion in the lcf1+ gene, which encodes a long-chain fatty acyl-CoA synthetase. The lcf1Deltamutant shows pleiotropic phenotypes, in that they are also sensitive to high temperature (37 degrees C) and to high salt concentrations (0.9 M KCl) in the medium. Based on the fact that Lcf1 is highly homologous to Faa1 and Faa4 of Saccharomyces cerevisiae, both of which have previously been suggested to play roles in the maintenance of endogenous acyl-CoA pools, the possible function of Lcf1 in S. pombe is discussed.","authors":"Oshiro T, Aiba H, Mizuno T","authors_abbrev":"Oshiro T et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-04-10","publication_year":"2003","canto_session_key":"3afd4a567ba06463","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-08-02 16:09:17","canto_approved_date":"2022-02-07 17:09:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-26 19:10:07","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18H10.02","SPAC24B11.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-08-02"},{"uniquename":"PMID:25510862","title":"Three-dimensional eukaryotic genomic organization is strongly correlated with codon usage expression and function.","citation":"Nat Commun 2014 Dec 16;5:5876","abstract":"It has been shown that the distribution of genes in eukaryotic genomes is not random; however, formerly reported relations between gene function and genomic organization were relatively weak. Previous studies have demonstrated that codon usage bias is related to all stages of gene expression and to protein function. Here we apply a novel tool for assessing functional relatedness, codon usage frequency similarity (CUFS), which measures similarity between genes in terms of codon and amino acid usage. By analyzing chromosome conformation capture data, describing the three-dimensional (3D) conformation of the DNA, we show that the functional similarity between genes captured by CUFS is directly and very strongly correlated with their 3D distance in Saccharomyces cerevisiae, Schizosaccharomyces pombe, Arabidopsis thaliana, mouse and human. This emphasizes the importance of three-dimensional genomic localization in eukaryotes and indicates that codon usage is tightly linked to genome architecture.","doi":"10.1038/ncomms6876","authors":"Diament A, Pinter RY, Tuller T","authors_abbrev":"Diament A et al.","pubmed_publication_date":"16 Dec 2014","pubmed_entrez_date":"2014-12-17","publication_year":"2014","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2014-12-18 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22020070","title":"DNA replication: failures and inverted fusions.","citation":"Semin Cell Dev Biol 2011 Oct;22(8):866-74","abstract":"DNA replication normally follows the rules passed down from Watson and Crick: the chromosome duplicates as dictated by its antiparallel strands, base-pairing and leading and lagging strand differences. Real-life replication is more complicated, fraught with perils posed by chromosome damage for one, and by transcription of genes and by other perils that disrupt progress of the DNA replication machinery. Understanding the replication fork, including DNA structures, associated replisome and its regulators, is key to understanding how cells overcome perils and minimize error. Replication fork error leads to genome rearrangements and, potentially, cell death. Interest in the replication fork and its errors has recently gained added interest by the results of deep sequencing studies of human genomes. Several pathologies are associated with sometimes-bizarre genome rearrangements suggestive of elaborate replication fork failures. To try and understand the links between the replication fork, its failure and genome rearrangements, we discuss here phases of fork behavior (stall, collapse, restart and fork failures leading to rearrangements) and analyze two examples of instability from our own studies; one in fission yeast and the other in budding yeast.","doi":"10.1016/j.semcdb.2011.10.008","authors":"Carr AM, Paek AL, Weinert T","authors_abbrev":"Carr AM et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-10-25","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5362333","title":"Linear synthesis of sucrase and phosphatases during the cell cycle of Schizosaccharomyces pombe.","citation":"J Cell Sci 1969 Sep;5(2):373-91","abstract":"","authors":"Mitchison JM, Creanor J","authors_abbrev":"Mitchison JM et al.","pubmed_publication_date":"Sep 1969","pubmed_entrez_date":"1969-09-01","publication_year":"1969","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10430904","title":"Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region.","citation":"Proc Natl Acad Sci U S A 1999 Aug 03;96(16):9112-7","abstract":"The cellular target of leptomycin B (LMB), a nuclear export inhibitor, has been identified as CRM1 (exportin 1), an evolutionarily conserved receptor for the nuclear export signal of proteins. However, the mechanism by which LMB inhibits CRM1 still remains unclear. CRM1 in a Schizosaccharomyces pombe mutant showing extremely high resistance to LMB had a single amino acid replacement at Cys-529 with Ser. The mutant gene, named crm1-K1, conferred LMB resistance on wild-type S. pombe, and Crm1-K1 no longer bound biotinylated LMB. (1)H NMR analysis showed that LMB bound N-acetyl-L-cysteine methyl ester through a Michael-type addition, consistent with the idea that LMB binds covalently via its alpha, beta-unsaturated delta-lactone to the sulfhydryl group of Cys-529. When HeLa cells were cultured with biotinylated LMB, the only cellular protein bound covalently was CRM1. Inhibition by N-ethylmaleimide (NEM), an alkylating agent, of CRM1-mediated nuclear export probably was caused by covalent binding of the electrophilic structure in NEM to the sulfhydryl group of Cys-529, because the crm1-K1 mutant showed the normal rate for the export of Rev nuclear export signal-bearing proteins in the presence of not only LMB but also NEM. These results show that the single cysteine residue determines LMB sensitivity and is selectively alkylated by LMB, leading to CRM1 inactivation.","authors":"Kudo N, Matsumori N, Taoka H, Fujiwara D, Schreiner EP, Wolff B, Yoshida M, Horinouchi S","authors_abbrev":"Kudo N et al.","pubmed_publication_date":"03 Aug 1999","pubmed_entrez_date":"1999-08-04","publication_year":"1999","canto_session_key":"e57eb8f19a92186","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-28 10:37:35","canto_approved_date":"2022-01-04 18:28:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-04-27 16:27:46","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-06-28"},{"uniquename":"EMBL:SPORF3","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40918427","title":"A Tetracycline-Inducible Promoter Replacement System for  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2025;2025","abstract":"Inducible promoters are essential tools for regulating gene expression. In fission yeast, various inducible promoter systems have been developed over the years, aiding gene function studies. A key challenge with existing promoters is their high expression in the \"off \" state, with most systems showing only about a 10-fold difference between \"on\" and \"off\" conditions. A recent study introduced the  PenotetS  tetracycline promoter system, achieving nearly a 100-fold dynamic range. However, it was not designed to replace endogenous promoters. In this work, we have adapted the  PenotetS  system to enable the replacement of gene promoters directly at their endogenous genomic locations.","doi":"10.17912/micropub.biology.001759","authors":"Bashir S, Sivakumar S, Rhind N","authors_abbrev":"Bashir S et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-09-08","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-09-09 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10079327","title":"Systematic mutagenesis of the fission yeast Srp54 protein.","citation":"Curr Genet 1999 Mar;35(2):88-102","abstract":"The signal recognition particle (SRP) is a ribonucleoprotein required for targeting a subset of nascent pre-secretory proteins to the endoplasmic reticulum membrane. Of the six SRP polypeptides, the most highly conserved is Srp54p, a modular protein consisting of an amino-terminal (N) domain of unknown function, a central GTPase (G) domain, and a carboxyl-terminal (M) domain implicated in the recognition of both signal sequences and SRP RNA. To identify regions of Srp54p that interact with other SRP subunits or regulatory proteins, we carried out systematic mutagenesis of the fission yeast homolog, principally using a \"clustered charged-to-alanine\" strategy. Of the 35 alleles examined, 13 are unable to support growth, two confer cold-sensitivity, five confer heat-sensitivity, and 15 produce no discernible phenotype. The lethal and conditional mutations map throughout the protein to several conserved regions, confirming that these motifs play critical roles in Srp54p function. The effects of the amino-acid substitutions are analyzed with reference to the recently determined tertiary structures of the N/G domain and the intact protein from a thermophilic bacterium.","authors":"Martínez-Force E, Lakhe-Reddy S, Wise JA","authors_abbrev":"Martínez-Force E et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-03-18","publication_year":"1999","canto_session_key":"265b5ed439aaa802","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-08-18 14:29:22","canto_approved_date":"2023-10-01 16:44:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-16 13:38:19","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":68,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_10079327_phaf.tsv"}],"genes":["SPCC188.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-08-18"},{"uniquename":"PMID:10582238","title":"The 26S proteasome of the fission yeast Schizosaccharomyces pombe.","citation":"Philos Trans R Soc Lond B Biol Sci 1999 Sep 29;354(1389):1523-32","abstract":"The 26S proteasome is the multiprotein complex that degrades proteins that have been marked for destruction by the ubiquitin pathway. It is made up of two multisubunit complexes, the 20S catalytic core and the 19S regulatory complex. We describe the isolation and characterization of conditional mutants in the regulatory complex and their use to investigate interactions between different subunits. In addition we have investigated the localization of the 26S proteasome in fission yeast, by immunofluorescence in fixed cells and live cells with the use of a GFP-tagged subunit. Surprisingly, we find that in mitotic cells the 26S proteasome occupies a discrete intracellular compartment, the nuclear periphery. Electron microscopic analysis demonstrates that the complex resides inside the nuclear envelope. During meiosis the localization showed a more dynamic distribution. In meiosis I the proteasome remained around the nuclear periphery. However, during meiosis II there was a dramatic relocalization: initially, the signal occupied the area between the dividing nuclei, but at the end of mitosis the signal dispersed, returning to the nuclear periphery on ascospore formation. This observation implies that the nuclear periphery is a major site of proteolysis in yeast during mitotic growth and raises important questions about the function of the 26S proteasome in protein degradation.","authors":"Wilkinson CR, Penney M, McGurk G, Wallace M, Gordon C","authors_abbrev":"Wilkinson CR et al.","pubmed_publication_date":"29 Sep 1999","pubmed_entrez_date":"1999-12-03","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7836841","title":"Radiation checkpoints in model systems.","citation":"Int J Radiat Biol 1994 Dec;66(6 Suppl):S133-9","abstract":"The response to DNA damaging agents includes a delay to progression through the cell cycle. Irradiation of premitotic cells causes a delay to mitosis and irradiation of G1 and S phase cells causes a delay to DNA synthesis. These delays have become known as checkpoints. The mechanisms that mediate the mitotic (or G2) checkpoint delay have recently come under study in yeast model systems. Work in the eukaryotic organisms S. cerevisiae and S. pombe has identified at least seven proteins controlling the interactions between DNA damage and cell cycle progression. Genetic analysis of this checkpoint pathway has identified substantial overlap with the feedback controls that co-ordinate progression through the cell cycle. Molecular analysis has revealed structural conservation between these highly diverged yeasts, which suggests that similar proteins may act in related pathways in mammalian cells. In addition, the rad24 and rad25 genes of S. pombe (which are involved in the radiation checkpoint) encode functionally overlapping essential proteins that are highly conserved in mammalian cells. Studies of checkpoints in the yeasts may therefore help to define the signal pathways that control cell cycle delay in mammalian cells following irradiation, some of which have been proposed to be deficient in A-T cells.","authors":"Carr AM","authors_abbrev":"Carr AM","pubmed_publication_date":"Dec 1994","pubmed_entrez_date":"1994-12-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7667093","title":"The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1.","citation":"Nucleic Acids Res 1995 Aug 25;23(16):3168-73","abstract":"The chromo domain was originally identified as a protein sequence motif common to the Drosophila chromatin proteins, Polycomb (Pc) and heterochromatin protein 1 [HP1; Paro and Hogness (1991) Proc. Natl. Acad. Sci. USA, 88, 263-267; Paro (1990) Trends Genet., 6, 416-421]. Here we describe a second chromo domain-like motif in HP1. Subsequent refined searches identified further examples of this chromo domain variant which all occur in proteins that also have an N-terminally located chromo domain. Due to its relatedness to the chromo domain, and its occurrence in proteins that also have a classical chromo domain, we call the variant the 'chromo shadow domain'. Chromo domain-containing proteins can therefore be divided into two classes depending on the presence, for example in HP1, or absence, for example in Pc, of the chromo shadow domain. We have also found examples of proteins which have two classical chromo domains. The Schizosaccharomyces pombe SWI6 protein, involved in repression of the silent mating-type loci, is a member of the chromo shadow group. The similar modular architecture of SpSW16, HP1 and HP1-like proteins supports the model that the specificity of action of chromatin proteins is generated by combinations of protein modules.","authors":"Aasland R, Stewart AF","authors_abbrev":"Aasland R et al.","pubmed_publication_date":"25 Aug 1995","pubmed_entrez_date":"1995-08-25","publication_year":"1995","canto_session_key":"5a68bb72b2e74712","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 19:07:17","canto_approved_date":"2018-12-22 19:07:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 19:04:47","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:18197241","title":"urg1: a uracil-regulatable promoter system for fission yeast with short induction and repression times.","citation":"PLoS One 2008 Jan 16;3(1):e1428","abstract":"The fission yeast Schizosaccharomyces pombe is a popular genetic model organism with powerful experimental tools. The thiamine-regulatable nmt1 promoter and derivatives, which take >15 hours for full induction, are most commonly used for controlled expression of ectopic genes. Given the short cell cycle of fission yeast, however, a promoter system that can be rapidly regulated, similar to the GAL system for budding yeast, would provide a key advantage for many experiments.\nWe used S. pombe microarrays to identify three neighbouring genes (urg1, urg2, and urg3) whose transcript levels rapidly and strongly increased in response to uracil, a condition which otherwise had little effect on global gene expression. We cloned the promoter of urg1 (uracil-regulatable gene) to create several PCR-based gene targeting modules for replacing native promoters with the urg1 promoter (Purg1) in the normal chromosomal locations of genes of interest. The kanMX6 and natMX6 markers allow selection under urg1 induced and repressed conditions, respectively. Some modules also allow N-terminal tagging of gene products placed under urg1 control. Using pom1 as a proof-of-principle, we observed a maximal increase of Purg1-pom1 transcripts after uracil addition within less than 30 minutes, and a similarly rapid decrease after uracil removal. The induced and repressed transcriptional states remained stable over 24-hour periods. RT-PCR comparisons showed that both induced and repressed Purg1-pom1 transcript levels were lower than corresponding P3nmt1-pom1 levels (wild-type nmt1 promoter) but higher than P81nmt1-pom1 levels (weak nmt1 derivative).\nWe exploited the urg1 promoter system to rapidly induce pom1 expression at defined cell-cycle stages, showing that ectopic pom1 expression leads to cell branching in G2-phase but much less so in G1-phase. The high temporal resolution provided by the urg1 promoter should facilitate experimental design and improve the genetic toolbox for the fission yeast community.","doi":"10.1371/journal.pone.0001428","authors":"Watt S, Mata J, López-Maury L, Marguerat S, Burns G, Bähler J","authors_abbrev":"Watt S et al.","pubmed_publication_date":"16 Jan 2008","pubmed_entrez_date":"2008-01-17","publication_year":"2008","canto_session_key":"abfd5c139060b066","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-11-01 09:45:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-25 14:30:57","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1002.17c","SPAC1002.18","SPAC2F7.03c","SPAC1002.19","SPAC24H6.05"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2013-09-25"},{"uniquename":"PMID:1522142","title":"Cytoskeletal and DNA structure abnormalities result from bypass of requirement for the cdc10 start gene in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1992 Mar;101 ( Pt 3):517-28","abstract":"The cdc10 gene of the fission yeast S. pombe is required for traverse of the start control in late G1 and commitment to the mitotic cell cycle. To increase our understanding of the events which occur at start, a pseudoreversion analysis was undertaken to identify genes whose products may interact with cdc10 or bypass the requirement for it. A single gene, sct1+ (suppressor of cdc ten), has been identified, mutation of which suppresses all conditional alleles and a null allele of cdc10. Bypass of the requirement for cdc10+ function by sct1-1 mutations leads to pleiotropic defects, including microtubule, microfilament and nuclear structural abnormalities. Our data suggest that sct1 encodes a protein that is dependent upon cdc10+ either for its normal function or expression, or is a component of a checkpoint that monitors execution of p85cdc10 function.","authors":"Marks J, Fankhauser C, Reymond A, Simanis V","authors_abbrev":"Marks J et al.","pubmed_publication_date":"Mar 1992","pubmed_entrez_date":"1992-03-01","publication_year":"1992","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC725.16","SPBC336.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:26793708","title":"The Golgin Family of Coiled-Coil Tethering Proteins.","citation":"Front Cell Dev Biol 2015;3:86","abstract":"The golgins are a family of predominantly coiled-coil proteins that are localized to the Golgi apparatus. Golgins are present in all eukaryotes, suggesting an evolutionary conserved function. Golgins are anchored to the Golgi membrane by their carboxy terminus and are predicted to adopt an extended conformation that projects into the surrounding cytoplasm. This arrangement is ideal for the capture or tethering of nearby membranes or cytoskeletal elements. Golgin-mediated tethering is thought to be important for vesicular traffic at the Golgi apparatus, the maintenance of Golgi architecture, as well as the positioning of the Golgi apparatus within cells. In addition to acting as tethers, some golgins can also sequester various factors at the Golgi membrane, allowing for the spatiotemporal regulation of downstream cellular functions. Although it is now established that golgins are membrane and cytoskeleton tethers, the mechanisms underlying tethering remain poorly defined. Moreover, the importance of golgin-mediated tethering in a physiological context remains to be fully explored. This review will describe our current understanding of golgin function, highlighting recent progress that has been made, and goes on to discuss outstanding questions and potential avenues for future research with regard to this family of conserved Golgi-associated proteins.","doi":"10.3389/fcell.2015.00086","authors":"Witkos TM, Lowe M","authors_abbrev":"Witkos TM et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2016-01-22","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27D7.02c","SPBC365.11","SPBC119.12","SPBC365.07c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:22370953","title":"Promotion of glycerol utilization using ethanol and 1-propanol in Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2012 Jul;95(2):441-9","abstract":"The fission yeast Schizosaccharomyces pombe does not grow in media containing glycerol as a sole carbon source but uses glycerol in the presence of ethanol. Ethanol, but not glycerol, triggered upregulation of gld1+ and fbp1+ during glucose starvation even though gld1+ and fbp1+ are essential for growth on glycerol. This upregulation occurred at a very low concentration of ethanol. The transcriptional regulation of gld1+ was tested in the presence of various alcohols, and both ethanol and 1-propanol were found to induce gld1+ and to support growth in glycerol-containing media. We suggest that S. pombe has a novel ethanol and/or 1-propanol recognition mechanism that upregulates glycerol utilization during glucose starvation.","doi":"10.1007/s00253-012-3971-x","authors":"Matsuzawa T, Hara F, Tohda H, Uemura H, Takegawa K","authors_abbrev":"Matsuzawa T et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-02-29","publication_year":"2012","canto_session_key":"427e90edfa319072","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_approved_date":"2016-07-06 07:38:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-05 00:27:52","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.14c","SPAC13F5.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-07-05"},{"uniquename":"PMID:22665807","title":"Multisite phosphoregulation of Cdc25 activity refines the mitotic entrance and exit switches.","citation":"Proc Natl Acad Sci U S A 2012 Jun 19;109(25):9899-904","abstract":"Cyclin-dependent kinase 1 (Cdk1) kinase dephosphorylation and activation by Cdc25 phosphatase are essential for mitotic entry. Activated Cdk1 phosphorylates Cdc25 and other substrates, further activating Cdc25 to form a positive feedback loop that drives the abrupt G2/mitosis switch. Conversely, mitotic exit requires Cdk1 inactivation and reversal of Cdk1 substrate phosphorylation. This dephosphorylation is mediated, in part, by Clp1/Cdc14, a Cdk1-antagonizing phosphatase, which reverses Cdk1 phosphorylation of itself, Cdc25, and other Cdk1 substrates. Thus, Cdc25 phosphoregulation is essential for proper G2-M transition, and its contributions to cell cycle control have been modeled based on studies using Xenopus and human cell extracts. Because cell extract systems only approximate in vivo conditions where proteins interact within dynamic cellular environments, here, we use Schizosaccharomyces pombe to characterize, both experimentally and mathematically, the in vivo contributions of Cdk1-mediated phosphorylation of Cdc25 to the mitotic transition. Through comprehensive mapping of Cdk1 phosphosites on Cdc25 and characterization of phosphomutants, we show that Cdc25 hyperphosphorylation by Cdk1 governs Cdc25 catalytic activation, the precision of mitotic entry, and unvarying cell length but not Cdc25 localization or abundance. We propose a mathematical model that explains Cdc25 regulation by Cdk1 through a distributive and disordered phosphorylation mechanism that ultrasensitively activates Cdc25. We also show that Clp1/Cdc14 dephosphorylation of Cdk1 sites on Cdc25 controls the proper timing of cell division, a mechanism that is likely due to the double negative feedback loop between Clp1/Cdc14 and Cdc25 that controls the abruptness of the mitotic exit switch.","doi":"10.1073/pnas.1201366109","authors":"Lu LX, Domingo-Sananes MR, Huzarska M, Novak B, Gould KL","authors_abbrev":"Lu LX et al.","pubmed_publication_date":"19 Jun 2012","pubmed_entrez_date":"2012-06-06","publication_year":"2012","canto_session_key":"a8928db520ace5a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2017-12-04 20:50:46","canto_approved_date":"2026-01-15 09:23:51","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-11-27 19:33:30","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.06c","SPAC1782.09c","SPCC18B5.03","SPBC582.03","SPAC57A10.02","SPAC24H6.05","SPBC11B10.09"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-12-04"},{"uniquename":"PMID:3861928","title":"Direct selection of mutants influencing gene conversion in the yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1985;199(3):365-71","abstract":"In Schizosaccharomyces pombe, a suppressor-active mutation at the anticodon site of the tRNASerUCA gene sup3 leads to opal (UGA)-specific suppression. Second-site mutations (rX) in sup3 inactivate the suppressor. The sup3-UGA, rX double mutants are genetically unstable in meiotic selfings, due to the intergenic transfer of information between sup3 and the unlinked genes sup9 and sup12 (Hofer et al. 1979; Munz and Leupold 1981; Munz et al. 1982). These three genes have considerable sequence homology over about 200 base pairs (Hottinger et al. 1982). Mutants showing a decrease or an increase of the meiotic instability at sup3 have been selected. One mutation (rec3-8) increases both the genetic instability and the frequency of intragenic recombination in sup3 by one order of magnitude. It has no effect on the stability of the nonsense alleles arg1-230 (UAA), ade6-704 and ural1-61 (UGA) or on the frequency of crossing-over between sup3 and the closely linked gene cdc8. The existence of a common genetic control over intragenic recombination and genetic instability at sup3 provides a direct way of selecting for rec mutants in homothallic haploid strains of S. pombe carrying a suppressor-inactive allele of sup3. It also supports the hypothesis that the instability of mutant alleles of this gene is due to chromosome mispairing at meiosis allowing sup3 to pair with sup9 or sup12 and then to undergo recombination by gene conversion restoring the suppressor-active allele sup3-UGA from the suppressor-inactive allele sup3-UGA, rX.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Thuriaux P","authors_abbrev":"Thuriaux P","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28679701","title":"Setting up  Schizosaccharomyces pombe  Crosses/Matings.","citation":"Cold Spring Harb Protoc 2017 Jul 05;2017(7):pdb.prot091694","abstract":"Here we provide methods for setting up standard crosses with  Schizosaccharomyces pombe  strains. All strain genotypes and pedigrees should be recorded in a laboratory strain book. Matings between two haploid strains of interest are induced on solid medium poor in nitrogen. Usually, sporulation agar (SPA) plates are preferred, but for difficult matings it is advisable to try several mating media in parallel because one medium might allow for more efficient mating. Protoplast fusion can be used to produce zygotes from sterile mutants that fail to mate.","doi":"10.1101/pdb.prot091694","authors":"Ekwall K, Thon G","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"05 Jul 2017","pubmed_entrez_date":"2017-07-07","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-08 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1824697","title":"Alpha subunit of mitochondrial F1-ATPase from the fission yeast. Deduced sequence of the wild type and identification of a mutation that alters apparent negative cooperativity.","citation":"J Biol Chem 1991 Jan 05;266(1):287-93","abstract":"The nuclear gene atp1 encoding the mitochondrial ATP synthase alpha subunit of the fission yeast Schizosaccharomyces pombe was sequenced. It contains a 1,608-base pair-long open reading frame interrupted by two introns of 175 and 269 base pairs, located near the 5'-end of the gene. The initiation site of transcription AAAC was located 60 nucleotides upstream of the translation initiation codon. The deduced polypeptide sequence contains a 27-amino acid residue presequence, presumably involved in mitochondrial targeting, preceding a mature protein of 509 amino acid residues. The atp1 alleles from mutant A2313 (Bouty, M., and Goffeau, A. (1982) Eur. J. Biochem. 125, 471-477) and its related phenotypic revertant R351 (Falson, P., Di Pietro, A., Darbouret, D., Jault, J. M., Gautheron, D. C., Boutry, M., and Goffeau, A. (1987) Biochem. Biophys. Res. Commun. 148, 1182-1188) were also cloned and sequenced. A single nonsense mutation CAA-TAA (Gln173-stop) in mutant A2313 became a missense mutation TAA-TTA (stop-Leucine) in revertant R351. Glutamine 173 is located in the first putative element of the nucleotide binding site. Its substitution by a leucine residue appears responsible for the lower enzyme affinity toward ADP and for the loss of cooperativity of F1-ATPase activity.","authors":"Falson P, Maffey L, Conrath K, Boutry M","authors_abbrev":"Falson P et al.","pubmed_publication_date":"05 Jan 1991","pubmed_entrez_date":"1991-01-05","publication_year":"1991","canto_session_key":"00f542dd6c29c6f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-02-05 16:18:55","canto_approved_date":"2024-12-11 09:25:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-30 14:04:34","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-05"},{"uniquename":"PMID:15075260","title":"pdf1, a palmitoyl protein thioesterase 1 Ortholog in Schizosaccharomyces pombe: a yeast model of infantile Batten disease.","citation":"Eukaryot Cell 2004 Apr;3(2):302-10","abstract":"Infantile Batten disease is a severe neurodegenerative storage disorder caused by mutations in the human PPT1 (palmitoyl protein thioesterase 1) gene, which encodes a lysosomal hydrolase that removes fatty acids from lipid-modified proteins. PPT1 has orthologs in many species, including lower organisms and plants, but not in Saccharomyces cerevisiae. The fission yeast Schizosaccharomyces pombe contains a previously uncharacterized open reading frame (SPBC530.12c) that encodes the S. pombe Ppt1p ortholog fused in frame to a second enzyme that is highly similar to a previously cloned mouse dolichol pyrophosphatase (Dolpp1p). In the present study, we characterized this interesting gene (designated here as pdf1, for palmitoyl protein thioesterase-dolichol pyrophosphate phosphatase fusion 1) through deletion of the open reading frame and complementation by plasmids bearing mutations in various regions of the pdf1 sequence. Strains bearing a deletion of the entire pdf1 open reading frame are nonviable and are rescued by a pdf1 expression plasmid. Inactivating mutations in the Dolpp1p domain do not rescue the lethality, whereas mutations in the Ppt1p domain result in cells that are viable but abnormally sensitive to sodium orthovanadate and elevated extracellular pH. The latter phenotypes have been previously associated with class C and class D vacuolar protein sorting (vps) mutants and vacuolar membrane H(+)-ATPase (vma) mutants in S. cerevisiae. Importantly, the Ppt1p-deficient phenotype is complemented by the human PPT1 gene. These results indicate that the function of PPT1 has been widely conserved throughout evolution and that S. pombe may serve as a genetically tractable model for the study of human infantile Batten disease.","authors":"Cho SK, Hofmann SL","authors_abbrev":"Cho SK et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-04-13","publication_year":"2004","canto_session_key":"67ea8121a7c3e6f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-16 14:49:24","canto_approved_date":"2023-07-10 17:30:27","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2012-10-15 08:57:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC530.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-06-16"},{"uniquename":"PMID:17957823","title":"Spatial controls for growth zone formation during the fission yeast cell cycle.","citation":"Yeast 2008 Jan;25(1):59-69","abstract":"Because of its regular shape, fission yeast is becoming an increasingly important organism in the study of cellular morphogenesis. Genetic experiments with mutants and drug treatment studies with wild-type cells have revealed the importance of microtubules in controlling new growth zone formation. It is believed that microtubules exert this role by delivering to cell ends a 'dynamic landmark' protein, tea1p, which promotes actin polymerization and growth zone formation. Here we present a simple model for fission yeast morphogenesis that describes the interplay between these two cytoskeletal elements. An essential assumption of the model is that actin polymerization is a self-reinforcing process: filamentous actin promotes its own formation from globular actin subunits via regulatory molecules. In our model, microtubules stimulate actin polymerization by delivering a component of the autocatalytic actin-assembly feedback loop (not by delivering a de novo inducer of actin polymerization). We show that the model captures all the characteristic features of polarized growth in fission yeast during normal mitotic cycles. We categorize the types of growth patterns that can exist in the model and show that they correspond to the major classes of morphogenetic mutants (monopolar, orb, banana and tea). Based on these results, we propose that fission yeast cells have specific size ranges in which they can exhibit two or more different stable patterns of growth.","authors":"Csikász-Nagy A, Gyorffy B, Alt W, Tyson JJ, Novák B","authors_abbrev":"Csikász-Nagy A et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-10-25","publication_year":"2008","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7840612","title":"Kinetic studies of gluconate pathway enzymes from Schizosaccharomyces pombe.","citation":"Arch Biochem Biophys 1995 Jan 10;316(1):163-8","abstract":"Glucose dehydrogenase and gluconate kinase which catalyze two-step reactions of the gluconate pathway have been purified from Schizosaccharomyces pombe. Their steady-state kinetic studies were undertaken. The yeast glucose dehydrogenase requires NADP+ as an obligatory coenzyme and mediates the oxidation of D-glucose to D-gluconate via an ordered Bi Bi mechanism with NADP+ as the leading substrate. Kinetic constants for the dehydrogenase reactions have been measured. The yeast gluconate kinase requires Mg2+ as an activator. The phosphorylation catalyzed by the fission yeast gluconate kinase has been studied kinetically at a fixed concentration of Mg2+. The initial velocity and product inhibition results are consistent with a rapid equilibrium random Bi Bi mechanism with the formation of an abortive enzyme-ADP-gluconate complex. Dissociation constants of the two substrates, ATP and D-gluconate from various binary and ternary enzymic complexes, have been determined.","authors":"Tsai CS, Shi JL, Ye HG","authors_abbrev":"Tsai CS et al.","pubmed_publication_date":"10 Jan 1995","pubmed_entrez_date":"1995-01-10","publication_year":"1995","canto_session_key":"47d4b775a0310633","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-11-25 16:06:04","canto_approved_date":"2025-02-20 08:52:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-25 16:05:36","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.12","SPBC660.16"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-11-25"},{"uniquename":"PMID:17724773","title":"Expression of Candida albicans Sfu1 in fission yeast complements the loss of the iron-regulatory transcription factor Fep1 and requires Tup co-repressors.","citation":"Yeast 2007 Oct;24(10):883-900","abstract":"The opportunistic pathogenic yeast Candida albicans contains a gene which encodes a putative member of the iron-regulatory GATA factor protein family. This protein, referred to as suppressor of ferric uptake (Sfu1), has two Cys(2)/Cys(2)-type zinc finger domains separated by a conserved Cys-rich region. In Schizosaccharomyces pombe, the GATA-type transcription factor Fe protein 1 (Fep1) represses target gene expression when iron levels exceed those needed by the cell. To ascertain the functional similarity between Sfu1 and Fep1, the C. albicans Sfu1 was expressed in Sz. pombe cells lacking the endogenous fep1(+) gene. We determined that Sfu1 is capable of suppressing iron-related phenotypes of fep1Delta mutant cells. Using a functional SFU1-GFP fusion allele, the Sfu1 protein was localized to the nucleus under both iron-replete and iron-starved conditions. Sfu1 effectively regulated the expression of genes encoding components of the reductive and non-reductive iron transport systems. Furthermore, the iron-responsive regulation mediated by Sfu1 was GATA-dependent. The N-terminal 250 amino acid segment of Sfu1 expressed in and purified from Escherichia coli specifically associated with the hexanucleotide sequence AGATAA in an iron-dependent manner. On the other hand, expression of the full-length C. albicans Sfu1 in Sz. pombe fep1Delta tup11Delta tup12Delta triple mutant cells failed to repress target gene expression under conditions of high iron concentration. Using two-hybrid analysis, we demonstrated that Tup11 and Tup12 physically interacted with Sfu1. Taken together, these results reveal a remarkable functional conservation between Sfu1 from C. albicans and Fep1 from Sz. pombe in their ability to sense excess iron and respond by repressing target gene transcription.","authors":"Pelletier B, Mercier A, Durand M, Peter C, Jbel M, Beaudoin J, Labbé S","authors_abbrev":"Pelletier B et al.","pubmed_publication_date":"Oct 2007","pubmed_entrez_date":"2007-08-29","publication_year":"2007","canto_session_key":"2aae6dc12bba6a1d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-05 08:46:05","canto_approved_date":"2019-06-05 08:46:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-06-05 08:45:59","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23E2.01","SPAC630.14c","SPAC18B11.10"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2019-06-05"},{"uniquename":"PMID:2210373","title":"Cloning of the Schizosaccharomyces pombe TFIID gene reveals a strong conservation of functional domains present in Saccharomyces cerevisiae TFIID.","citation":"Genes Dev 1990 Jul;4(7):1141-8","abstract":"The gene encoding the Schizosaccharomyces pombe TATA box-binding factor (TFIID) was cloned and sequenced. The gene contains three introns and codes for a polypeptide of 231 amino acids. The cDNA-expressed protein showed both TATA box-binding and basal transcription activities. The carboxy-terminal three-quarters of S. pombe TFIID shares an extraordinary degree of amino acid sequence homology with a corresponding region of Saccharomyces cerevisiae TFIID that has been shown to be necessary and sufficient for TATA box-binding and basal transcription activities. In contrast, the amino-terminal regions of the S. pombe and S. cerevisiae TFIIDs differ markedly in amino acid sequence and composition. Structure and function relationships of TFIID are discussed in light of these data.","authors":"Hoffmann A, Horikoshi M, Wang CK, Schroeder S, Weil PA, Roeder RG","authors_abbrev":"Hoffmann A et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_session_key":"1e2777b4fae054d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-07-27 10:40:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-17 16:59:09","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29E6.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-01-17"},{"uniquename":"PMID:22921967","title":"Formation of pyranoanthocyanins by Schizosaccharomyces pombe during the fermentation of red must.","citation":"Int J Food Microbiol 2012 Sep 17;159(1):47-53","abstract":"Schizosaccharomyces pombe is a non-Saccharomyces yeast strain that can ferment grape musts with high sugar contents - but it also has other metabolic and physiological properties that render it of great interest to wine biotechnologists. This work compares the production of pyranoanthocyanins by S. pombe, Saccharomyces cerevisiae and Saccharomyces uvarum during fermentation. Total pyranoanthocyanins ranged from 11.9 to 19.4 mg/l depending on the strain of S. pombe used. On average, S. pombe produced more pyruvic acid than did either Saccharomyces species; as a consequence it also formed more vitisin A-type pigments. S. pombe 938 produced the largest quantity of vitisin A (11.03±0.82 mg/l). The formation of large amounts of pyranoanthocyanins intensifies the post-fermentation colour of wines somewhat, a phenomenon that helps them maintain their colour over ageing as the natural grape anthocyanins become degraded. Some of the S. pombe strains showed hydroxycinnamate decarboxylase activity, which favours the formation of vinylphenolic pyranoanthocyanins. Fermentation with S. pombe therefore provides an interesting way of increasing the overall pyranoanthocyanin content of red wines, and of stabilising their colour during ageing.","doi":"10.1016/j.ijfoodmicro.2012.08.007","authors":"Morata A, Benito S, Loira I, Palomero F, González MC, Suárez-Lepe JA","authors_abbrev":"Morata A et al.","pubmed_publication_date":"17 Sep 2012","pubmed_entrez_date":"2012-08-28","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30737734","title":"Established and Upcoming Yeast Expression Systems.","citation":"Methods Mol Biol 2019;1923:1-74","abstract":"Yeast was the first microorganism used by mankind for biotransformation of feedstock that laid the foundations of industrial biotechnology. Long historical use, vast amount of data, and experience paved the way for Saccharomyces cerevisiae as a first yeast cell factory, and still it is an important expression platform as being the production host for several large volume products. Continuing special needs of each targeted product and different requirements of bioprocess operations have led to identification of different yeast expression systems. Modern bioprocess engineering and advances in omics technology, i.e., genomics, transcriptomics, proteomics, secretomics, and interactomics, allow the design of novel genetic tools with fine-tuned characteristics to be used for research and industrial applications. This chapter focuses on established and upcoming yeast expression platforms that have exceptional characteristics, such as the ability to utilize a broad range of carbon sources or remarkable resistance to various stress conditions. Besides the conventional yeast S. cerevisiae, established yeast expression systems including the methylotrophic yeasts Pichia pastoris and Hansenula polymorpha, the dimorphic yeasts Arxula adeninivorans and Yarrowia lipolytica, the lactose-utilizing yeast Kluyveromyces lactis, the fission yeast Schizosaccharomyces pombe, and upcoming yeast platforms, namely, Kluyveromyces marxianus, Candida utilis, and Zygosaccharomyces bailii, are compiled with special emphasis on their genetic toolbox for recombinant protein production.","doi":"10.1007/978-1-4939-9024-5_1","authors":"Gündüz Ergün B, Hüccetoğulları D, Öztürk S, Çelik E, Çalık P","authors_abbrev":"Gündüz Ergün B et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-02-10","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-02-11 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7769002","title":"A novel essential fission yeast gene pad1+ positively regulates pap1(+)-dependent transcription and is implicated in the maintenance of chromosome structure.","citation":"J Cell Sci 1995 Feb;108 ( Pt 2):569-79","abstract":"Fission yeast pap1+ gene encodes an AP-1-like transcription factor, whose overexpression can confer resistance to staurosporine, a protein kinase inhibitor. We have previously identified a target gene (p25) for pap1+, and shown that, crm1+, which is required for maintenance of higher order chromosome structure, negatively regulates pap1-dependent transcription. In this study, we have characterized a novel gene, pad1+, which was isolated as a multicopy plasmid capable of conferring staurosporine-resistance. We showed that high copy pad1+ induces transcriptional activation of the p25 gene and that the induction by pad1+ is dependent on the pap1+ gene. Furthermore, a cis-element analysis of the 5'-region of the p25 gene showed that two elements (an AP-1 site and a 14 bp palindrome sequence) where pap1 binds in vitro is essential for the induction by pad1+. These results indicate that pad1 can positively regulate pap1-dependent transcription. Through an electromobility shift assay we showed that overexpression of pad1+ is not capable of enhancing the DNA-binding activity of pap1 directly. The pad1+ gene encodes a 35 kDa protein that has significant identity (68%) to Caenorhabditis elegans F37A4.5, and is also similar to mouse Mov34 and human C6.1A. Gene disruption experiments have demonstrated that pad1+ is essential for viability. A disruption mutant of pad1+ obtained after spore germination exhibited an elongated cell body with abberantly folded chromosomes. A mitotic plasmid loss experiment also produced similar cells having an abnormal chromosome structure. These suggest that pad1+ may play an important role in higher order chromosome structure. Taken concurrently with our previous results, two essential genes pad1+ and crm1+ regulate pap1-dependent transcription; pad1+ and crm1+ are positive and negative regulators, respectively.","authors":"Shimanuki M, Saka Y, Yanagida M, Toda T","authors_abbrev":"Shimanuki M et al.","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_session_key":"54de4db66c7dfe2e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-16 09:14:32","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-06-13 13:06:24","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC31G5.09c","SPAC3C7.14c","SPAC31G5.13"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2013-06-13"},{"uniquename":"PMID:11909965","title":"Fission yeast Mad3p is required for Mad2p to inhibit the anaphase-promoting complex and localizes to kinetochores in a Bub1p-, Bub3p-, and Mph1p-dependent manner.","citation":"Mol Cell Biol 2002 Apr;22(8):2728-42","abstract":"The spindle checkpoint delays the metaphase-to-anaphase transition in response to spindle and kinetochore defects. Genetic screens in budding yeast identified the Mad and Bub proteins as key components of this conserved regulatory pathway. Here we present the fission yeast homologue of Mad3p. Cells devoid of mad3(+) are unable to arrest their cell cycle in the presence of microtubule defects. Mad3p coimmunoprecipitates Bub3p, Mad2p, and the spindle checkpoint effector Slp1/Cdc20p. We demonstrate that Mad3p function is required for the overexpression of Mad2p to result in a metaphase arrest. Mad1p, Bub1p, and Bub3p are not required for this arrest. Thus, Mad3p appears to have a crucial role in transducing the inhibitory \"wait anaphase\" signal to the anaphase-promoting complex (APC). Mad3-green fluorescent protein (GFP) is recruited to unattached kinetochores early in mitosis and accumulates there upon prolonged checkpoint activation. For the first time, we have systematically studied the dependency of Mad3/BubR1 protein recruitment to kinetochores. We find Mad3-GFP kinetochore localization to be dependent upon Bub1p, Bub3p, and the Mph1p kinase, but not upon Mad1p or Mad2p. We discuss the implications of these findings in the context of our current understanding of spindle checkpoint function.","authors":"Millband DN, Hardwick KG","authors_abbrev":"Millband DN et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-03-23","publication_year":"2002","canto_session_key":"71284b5f82561435","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-05-15 09:07:40","canto_approved_date":"2024-11-29 07:45:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-11 17:09:58","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.01c","SPAC821.08c","SPBC20F10.06","SPBC26H8.07c","SPCC1322.12c","SPBC3D6.04c","SPAC25G10.07c","SPAC23H3.08c","SPBC106.01"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2019-05-15"},{"uniquename":"PMID:26401015","title":"Nucleosome competition reveals processive acetylation by the SAGA HAT module.","citation":"Proc Natl Acad Sci U S A 2015 Oct 06;112(40):E5461-70","abstract":"The Spt-Ada-Gcn5 acetyltransferase (SAGA) coactivator complex hyperacetylates histone tails in vivo in a manner that depends upon histone 3 lysine 4 trimethylation (H3K4me3), a histone mark enriched at promoters of actively transcribed genes. SAGA contains a separable subcomplex known as the histone acetyltransferase (HAT) module that contains the HAT, Gcn5, bound to Sgf29, Ada2, and Ada3. Sgf29 contains a tandem Tudor domain that recognizes H3K4me3-containing peptides and is required for histone hyperacetylation in vivo. However, the mechanism by which H3K4me3 recognition leads to lysine hyperacetylation is unknown, as in vitro studies show no effect of the H3K4me3 modification on histone peptide acetylation by Gcn5. To determine how H3K4me3 binding by Sgf29 leads to histone hyperacetylation by Gcn5, we used differential fluorescent labeling of histones to monitor acetylation of individual subpopulations of methylated and unmodified nucleosomes in a mixture. We find that the SAGA HAT module preferentially acetylates H3K4me3 nucleosomes in a mixture containing excess unmodified nucleosomes and that this effect requires the Tudor domain of Sgf29. The H3K4me3 mark promotes processive, multisite acetylation of histone H3 by Gcn5 that can account for the different acetylation patterns established by SAGA at promoters versus coding regions. Our results establish a model for Sgf29 function at gene promoters and define a mechanism governing crosstalk between histone modifications.","doi":"10.1073/pnas.1508449112","authors":"Ringel AE, Cieniewicz AM, Taverna SD, Wolberger C","authors_abbrev":"Ringel AE et al.","pubmed_publication_date":"06 Oct 2015","pubmed_entrez_date":"2015-09-25","publication_year":"2015","canto_session_key":"49fe99dfe092c9fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-03-26 10:21:57","canto_approved_date":"2025-04-11 14:07:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-16 22:53:56","canto_added_date":"2016-04-15 00:15:15","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.03c","SPAC1834.04","SPBC28F2.10c","SPBC1921.07c","SPCC24B10.08c","SPAC1952.05"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2018-03-26"},{"uniquename":"PMID:11294914","title":"Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast.","citation":"Mol Biol Cell 2001 Apr;12(4):1161-75","abstract":"We tested the ability of 87 profilin point mutations to complement temperature-sensitive and null mutations of the single profilin gene of the fission yeast Schizosaccharomyces pombe. We compared the biochemical properties of 13 stable noncomplementing profilins with an equal number of complementing profilin mutants. A large quantitative database revealed the following: 1) in a profilin null background fission yeast grow normally with profilin mutations having >10% of wild-type affinity for actin or poly-L-proline, but lower affinity for either ligand is incompatible with life; 2) in the cdc3-124 profilin ts background, fission yeast function with profilin having only 2-5% wild-type affinity for actin or poly-L-proline; and 3) special mutations show that the ability of profilin to catalyze nucleotide exchange by actin is an essential function. Thus, poly-L-proline binding, actin binding, and actin nucleotide exchange are each independent requirements for profilin function in fission yeast.","authors":"Lu J, Pollard TD","authors_abbrev":"Lu J et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-04-11","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4A8.15c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:18418059","title":"The Flp1/Clp1 phosphatase cooperates with HECT-type Pub1/2 protein-ubiquitin ligases in Schizosaccharomyces pombe.","citation":"Cell Cycle 2008 May 01;7(9):1269-76","abstract":"The Schizosaccharomyces pombe Flp1p serine-threonine phosphatase is required for the degradation of the mitotic inducer Cdc25p at the end of mitosis. Cdc25p degradation prevents Cdc2p-tyrosine 15 dephosphorylation and, thus, contributes to the timely inactivation of mitotic CDK-associated kinase activity. Both RING- and HECT-type protein-ubiquitin ligases are involved in Cdc25p destabilization. Flp1p function is required for Cdc25p ubiquitination via anaphase-promoting complex/cyclosome or APC/C (RING-type) and the absence of Pub1p (HECT-type) stabilizes the mitotic inducer. In the present report, we study the functional relationship of Flp1p with Pub1p and Pub2p HECT-type-protein ubiquitin ligases. We show that Flp1p is required for the rapid degradation of Cdc25p while Pub1p is responsible for the long-term destabilization of the mitotic inducer. Accordingly, flp1 and pub1 mutants have a strong genetic interaction, correlating defects in the coordination of mitosis and cytokinesis with the stabilization of hyperactive Cdc25p. However, we also show that Flp1 and Pub2p proteins functionally interact in vivo suggesting that both proteins belong to the same regulatory network in S. pombe cells. Thus Flp1p appears to have an important role in integrating HECT- and RING-type ubiquitin ligases in cell cycle control.","authors":"Esteban V, Sacristán M, Andrés S, Bueno A","authors_abbrev":"Esteban V et al.","pubmed_publication_date":"01 May 2008","pubmed_entrez_date":"2008-04-18","publication_year":"2008","canto_session_key":"79d1187d9569663f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-09 11:18:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-30 12:47:39","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11G7.02","SPAC1782.09c","SPBC26H8.07c","SPAC24H6.05","SPAC1805.15c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2015-01-30"},{"uniquename":"PMID:27538348","title":"Set3 contributes to heterochromatin integrity by promoting transcription of subunits of Clr4-Rik1-Cul4 histone methyltransferase complex in fission yeast.","citation":"Sci Rep 2016 Aug 19;6:31752","abstract":"Heterochromatin formation in fission yeast depends on RNAi machinery and histone-modifying enzymes. One of the key histone-modifying complexes is Clr4-Rik1-Cul4 methyltransferase complex (CLRC), which mediates histone H3K9 methylation, a hallmark for heterochromatin. CLRC is composed of the Clr4 histone methyltransferase, Rik1, Raf1, Raf2 and Pcu4. However, transcriptional regulation of the CLRC subunits is not well understood. In this study, we identified Set3, a core subunit of the Set3/Hos2 histone deacetylase complex (Set3C), as a contributor to the integrity and silencing of heterochromatin at centromeres, telomeres and silent mating-type locus. This novel role of Set3 relies on its PHD finger, but is independent of deacetylase activity or structural integrity of Set3C. Set3 is not located to the centromeric region. Instead, Set3 is targeted to the promoters of clr4(+) and rik1(+), probably through its PHD finger. Set3 promotes transcription of clr4(+) and rik1(+). Consistently, the protein levels of Clr4 and Rik1 were reduced in the set3Δ mutant. The heterochromatin silencing defect in the set3Δ mutant could be rescued by overexpressing of clr4(+) or rik1(+). Our study suggests transcriptional activation of essential heterochromatin factors underlies the tight regulation of heterochromatin integrity.","doi":"10.1038/srep31752","authors":"Yu Y, Zhou H, Deng X, Wang W, Lu H","authors_abbrev":"Yu Y et al.","pubmed_publication_date":"19 Aug 2016","pubmed_entrez_date":"2016-08-20","publication_year":"2016","canto_session_key":"b6055c42bedc6e07","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-23 09:19:10","canto_approved_date":"2024-07-23 09:19:10","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-05 10:06:19","canto_added_date":"2016-08-22 00:15:12","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":80,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.03","SPBC83.03c","SPAC140.03","SPCC11E10.08","SPCC663.12","SPAC212.11","SPAC6F12.09","SPAC22E12.11c","SPAC5H10.06c","SPCC1235.09","SPCC736.11","SPCC1393.10","SPAC3A11.08","SPCC613.12c","SPAC3G9.07c","SPAC22E12.19","SPCC188.13c","SPAC18G6.02c","SPCC970.07c","SPAC1250.04c","SPBC428.08c","SPAC13G7.07"],"gene_count":22,"ltp_gene_count":8,"approved_date":"2024-07-23"},{"uniquename":"PMID:23583778","title":"The four canonical tpr subunits of human APC/C form related homo-dimeric structures and stack in parallel to form a TPR suprahelix.","citation":"J Mol Biol 2013 Nov 15;425(22):4236-48","abstract":"The anaphase-promoting complex or cyclosome (APC/C) is a large E3 RING-cullin ubiquitin ligase composed of between 14 and 15 individual proteins. A striking feature of the APC/C is that only four proteins are involved in directly recognizing target proteins and catalyzing the assembly of a polyubiquitin chain. All other subunits, which account for >80% of the mass of the APC/C, provide scaffolding functions. A major proportion of these scaffolding subunits are structurally related. In metazoans, there are four canonical tetratricopeptide repeat (TPR) proteins that form homo-dimers (Apc3/Cdc27, Apc6/Cdc16, Apc7 and Apc8/Cdc23). Here, we describe the crystal structure of the N-terminal homo-dimerization domain of Schizosaccharomyces pombe Cdc23 (Cdc23(Nterm)). Cdc23(Nterm) is composed of seven contiguous TPR motifs that self-associate through a related mechanism to those of Cdc16 and Cdc27. Using the Cdc23(Nterm) structure, we generated a model of full-length Cdc23. The resultant \"V\"-shaped molecule docks into the Cdc23-assigned density of the human APC/C structure determined using negative stain electron microscopy (EM). Based on sequence conservation, we propose that Apc7 forms a homo-dimeric structure equivalent to those of Cdc16, Cdc23 and Cdc27. The model is consistent with the Apc7-assigned density of the human APC/C EM structure. The four canonical homo-dimeric TPR proteins of human APC/C stack in parallel on one side of the complex. Remarkably, the uniform relative packing of neighboring TPR proteins generates a novel left-handed suprahelical TPR assembly. This finding has implications for understanding the assembly of other TPR-containing multimeric complexes.","doi":"10.1016/j.jmb.2013.04.004","authors":"Zhang Z, Chang L, Yang J, Conin N, Kulkarni K, Barford D","authors_abbrev":"Zhang Z et al.","pubmed_publication_date":"15 Nov 2013","pubmed_entrez_date":"2013-04-16","publication_year":"2013","canto_session_key":"b768e60d030fb784","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-02-17 17:41:02","canto_approved_date":"2023-02-17 17:41:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 17:40:55","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1347.10","SPAC6F12.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-02-17","pdb_entries":[{"pdb_id":"3zn3","gene_chains":[{"gene_uniquename":"SPAC6F12.14","chain":"A","position":"19-301"}],"title":"N-terminal domain of S. pombe Cdc23 APC subunit","entry_authors":"Zhang Z,Yang J,Conin N,Kulkarni K,Barford D","entry_authors_abbrev":"Zhang Z et al.","reference_uniquename":"PMID:23583778","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:14699070","title":"ago1 and dcr1, two core components of the RNA interference pathway, functionally diverge from rdp1 in regulating cell cycle events in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2004 Mar;15(3):1425-35","abstract":"In the fission yeast Schizosaccharomyces pombe, three genes that function in the RNA interference (RNAi) pathway, ago1+, dcr1+, and rdp1+, have recently been shown to be important for timely formation of heterochromatin and accurate chromosome segregation. In the present study, we present evidence that null mutants for ago1+ and dcr1+ but not rdp1+, exhibit abnormal cytokinesis, cell cycle arrest deficiencies, and mating defects. Subsequent analyses showed that ago1+ and dcr1+ are required for regulated hyperphosphorylation of Cdc2 when encountering genotoxic insults. Because rdp1+ is dispensable for this process, the functions of ago1+ and dcr1+ in this pathway are presumably independent of their roles in RNAi-mediated heterochromatin formation and chromosome segregation. This was further supported by the finding that ago1+ is a multicopy suppressor of the S-M checkpoint deficiency and cytokinesis defects associated with loss of Dcr1 function, but not for the chromosome segregation defects of this mutant. Accordingly, we conclude that Dcr1-dependent production of small interfering RNAs is not required for enactment and/or maintenance of certain cell cycle checkpoints and that Ago1 and Dcr1 functionally diverge from Rdp1 to control cell cycle events in fission yeast. Finally, exogenous expression of hGERp95/EIF2C2/hAgo2, a human Ago1 homolog implicated in posttranscriptional gene silencing, compensated for the loss of ago1+ function in S. pombe. This suggests that PPD proteins may also be important for regulation of cell cycle events in higher eukaryotes.","authors":"Carmichael JB, Provost P, Ekwall K, Hobman TC","authors_abbrev":"Carmichael JB et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2003-12-31","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.11","SPCC188.13c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:22705791","title":"Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling.","citation":"Nat Struct Mol Biol 2012 Jun 17;19(7):693-700","abstract":"The Mre11-Rad50-Nbs1 (MRN) complex tethers, processes and signals DNA double-strand breaks, promoting genomic stability. To understand the functional architecture of MRN, we determined the crystal structures of the Schizosaccharomyces pombe Mre11 dimeric catalytic domain alone and in complex with a fragment of Nbs1. Two Nbs1 subunits stretch around the outside of the nuclease domains of Mre11, with one subunit additionally bridging and locking the Mre11 dimer via a highly conserved asymmetrical binding motif. Our results show that Mre11 forms a flexible dimer and suggest that Nbs1 not only is a checkpoint adaptor but also functionally influences Mre11-Rad50. Clinical mutations in Mre11 are located along the Nbs1-interaction sites and weaken the Mre11-Nbs1 interaction. However, they differentially affect DNA repair and telomere maintenance in Saccharomyces cerevisiae, potentially providing insight into their different human disease pathologies.","doi":"10.1038/nsmb.2323","authors":"Schiller CB, Lammens K, Guerini I, Coordes B, Feldmann H, Schlauderer F, Möckel C, Schele A, Strässer K, Jackson SP, Hopfner KP","authors_abbrev":"Schiller CB et al.","pubmed_publication_date":"17 Jun 2012","pubmed_entrez_date":"2012-06-19","publication_year":"2012","canto_session_key":"669b2243a78396bd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-04-18 14:09:28","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-02-26 17:04:18","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.09c","SPAC13C5.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-02-26","pdb_entries":[{"pdb_id":"4fbk","gene_chains":[{"gene_uniquename":"SPBC6B1.09c","chain":"A/B","position":"474-531"},{"gene_uniquename":"SPAC13C5.07","chain":"A/B","position":"15-413"}],"title":"Crystal structure of a covalently fused Nbs1-Mre11 complex with one manganese ion per active site","entry_authors":"Schiller CB,Lammens K,Hopfner KP","entry_authors_abbrev":"Schiller CB et al.","reference_uniquename":"PMID:22705791","experimental_method":"X-ray","resolution":"2.379"},{"pdb_id":"4fbq","gene_chains":[{"gene_uniquename":"SPBC6B1.09c","chain":"A/B","position":"474-531"},{"gene_uniquename":"SPAC13C5.07","chain":"A/B","position":"15-413"}],"title":"Crystal structure of a covalently fused Nbs1-Mre11 complex with two manganese ions per active site","entry_authors":"Schiller CB,Lammens K,Hopfner KP","entry_authors_abbrev":"Schiller CB et al.","reference_uniquename":"PMID:22705791","experimental_method":"X-ray","resolution":"2.5"},{"pdb_id":"4fbw","gene_chains":[{"gene_uniquename":"SPBC6B1.09c","chain":"C/D","position":"474-531"},{"gene_uniquename":"SPAC13C5.07","chain":"A/B","position":"7-413"}],"title":"Crystal structure of an unfused Mre11-Nbs1 complex with two manganese ions per active site","entry_authors":"Schiller CB,Lammens K,Hopfner KP","entry_authors_abbrev":"Schiller CB et al.","reference_uniquename":"PMID:22705791","experimental_method":"X-ray","resolution":"2.2"},{"pdb_id":"4fcx","gene_chains":[{"gene_uniquename":"SPAC13C5.07","chain":"A/B","position":"15-413"}],"title":"S.pombe Mre11 apoenzym","entry_authors":"Schiller CB,Lammens K,Hopfner KP","entry_authors_abbrev":"Schiller CB et al.","reference_uniquename":"PMID:22705791","experimental_method":"X-ray","resolution":"3.0"}]},{"uniquename":"PMID:27126383","title":"The long life of an endocytic patch that misses AP-2.","citation":"Curr Genet 2016 Nov;62(4):765-770","abstract":"Endocytosis is the process by which cells regulate extracellular fluid uptake and internalize molecules bound to their plasma membrane. This process requires the generation of protein-coated vesicles. In clathrin-mediated endocytosis (CME) the assembly polypeptide 2 (AP-2) adaptor facilitates rapid endocytosis of some plasma membrane receptors by mediating clathrin recruitment to the endocytic site and by connecting cargoes to the clathrin coat. While this adaptor is essential for early embryonic development in mammals, initial results suggested that it is dispensable for endocytosis in unicellular eukaryotes. The drastic effect of depleting AP-2 in metazoa and the mild effect of deleting AP-2 subunits in Saccharomyces cerevisiae have prevented a detailed analysis of the dynamics of endocytic patches in the absence of this adaptor. Using live-cell imaging of Schizosaccharomyces pombe endocytic sites we have shown that eliminating AP-2 perturbs the dynamics of endocytic patches beyond the moment of coat assembly. These perturbations affect the cell growth pattern and cell wall synthesis. Our results highlight the importance of using different model organisms to address the study of conserved aspects of CME.","authors":"de León N, Valdivieso MH","authors_abbrev":"de León N et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-04-30","publication_year":"2016","canto_session_key":"de1f5a1e93721296","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-07-20 21:56:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-20 21:55:46","canto_added_date":"2016-05-01 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2016-07-20"},{"uniquename":"PMID:33562654","title":"A Trans-Omics Comparison Reveals Common Gene Expression Strategies in Four Model Organisms and Exposes Similarities and Differences between Them.","citation":"Cells 2021 Feb 05;10(2)","abstract":"The ultimate goal of gene expression regulation is on the protein level. However, because the amounts of mRNAs and proteins are controlled by their synthesis and degradation rates, the cellular amount of a given protein can be attained by following different strategies. By studying omics data for six expression variables (mRNA and protein amounts, plus their synthesis and decay rates), we previously demonstrated the existence of common expression strategies (CESs) for functionally related genes in the yeast  Saccharomyces cerevisiae . Here we extend that study to two other eukaryotes: the yeast  Schizosaccharomyces pombe  and cultured human HeLa cells. We also use genomic data from the model prokaryote  Escherichia coli  as an external reference. We show that six-variable profiles (6VPs) can be constructed for every gene and that these 6VPs are similar for genes with similar functions in all the studied organisms. The differences in 6VPs between organisms can be used to establish their phylogenetic relationships. The analysis of the correlations among the six variables supports the hypothesis that most gene expression control occurs in actively growing organisms at the transcription rate level, and that translation plays a minor role. We propose that living organisms use CESs for the genes acting on the same physiological pathways, especially for those belonging to stable macromolecular complexes, but CESs have been modeled by evolution to adapt to the specific life circumstances of each organism.","doi":"10.3390/cells10020334","authors":"Forés-Martos J, Forte A, García-Martínez J, Pérez-Ortín JE","authors_abbrev":"Forés-Martos J et al.","pubmed_publication_date":"05 Feb 2021","pubmed_entrez_date":"2021-02-10","publication_year":"2021","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-02-12 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12684838","title":"High-efficiency electroporation by freezing intact yeast cells with addition of calcium.","citation":"Curr Genet 2003 Jun;43(3):206-11","abstract":"We developed a novel freezing method to generate competent cells of Schizosaccharomyces pombe and Saccharomyces cerevisiae prior to electroporation. Freezing the intact cells in sorbitol with the addition of calcium at -80 degrees C allowed us to improve the transformation efficiency after freezing and thawing. The optimum concentration of CaCl(2) was found to be 5-10 mM. The addition of other cations had no effect on the efficiency, while the addition of calcium meant that a broad concentration of sorbitol (0.6-2.5 M) could be used, independent of strain. Moreover, increasing the cell concentration to 2 x 10(9) cells/ml during an applied electric pulse further increased the efficiency after freezing and resulted in a wide range of electric field strength (9.0-11.5 kV/cm). Therefore, there was no need to optimize both the concentration of cryoprotectant and the electric field strength of the applied pulse. This procedure for electroporation allows the frozen competent cells to be stored long-term without any significant loss of efficiency.","authors":"Suga M, Hatakeyama T","authors_abbrev":"Suga M et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-04-10","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25748652","title":"Diffusible crosslinkers generate directed forces in microtubule networks.","citation":"Cell 2015 Mar 12;160(6):1159-68","abstract":"Cytoskeletal remodeling is essential to eukaryotic cell division and morphogenesis. The mechanical forces driving the restructuring are attributed to the action of molecular motors and the dynamics of cytoskeletal filaments, which both consume chemical energy. By contrast, non-enzymatic filament crosslinkers are regarded as mere friction-generating entities. Here, we experimentally demonstrate that diffusible microtubule crosslinkers of the Ase1/PRC1/Map65 family generate directed microtubule sliding when confined between partially overlapping microtubules. The Ase1-generated forces, directly measured by optical tweezers to be in the piconewton-range, were sufficient to antagonize motor-protein driven microtubule sliding. Force generation is quantitatively explained by the entropic expansion of confined Ase1 molecules diffusing within the microtubule overlaps. The thermal motion of crosslinkers is thus harnessed to generate mechanical work analogous to compressed gas propelling a piston in a cylinder. As confinement of diffusible proteins is ubiquitous in cells, the associated entropic forces are likely of importance for cellular mechanics beyond cytoskeletal networks.","doi":"10.1016/j.cell.2015.01.051","authors":"Lansky Z, Braun M, Lüdecke A, Schlierf M, ten Wolde PR, Janson ME, Diez S","authors_abbrev":"Lansky Z et al.","pubmed_publication_date":"12 Mar 2015","pubmed_entrez_date":"2015-03-10","publication_year":"2015","canto_session_key":"e55c296ccb00bca4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-05-14 00:19:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21148298","title":"A meiotic gene regulatory cascade driven by alternative fates for newly synthesized transcripts.","citation":"Mol Biol Cell 2011 Jan 01;22(1):66-77","abstract":"To determine the relative importance of transcriptional regulation versus RNA processing and turnover during the transition from proliferation to meiotic differentiation in the fission yeast Schizosaccharomyces pombe, we analyzed temporal profiles and effects of RNA surveillance factor mutants on expression of 32 meiotic genes. A comparison of nascent transcription with steady-state RNA accumulation reveals that the vast majority of these genes show a lag between maximal RNA synthesis and peak RNA accumulation. During meiosis, total RNA levels parallel 3' processing, which occurs in multiple, temporally distinct waves that peak from 3 to 6 h after meiotic induction. Most early genes and one middle gene, mei4, share a regulatory mechanism in which a specialized RNA surveillance factor targets newly synthesized transcripts for destruction. Mei4p, a member of the forkhead transcription factor family, in turn regulates a host of downstream genes. Remarkably, a spike in transcription is observed for less than one-third of the genes surveyed, and even these show evidence of RNA-level regulation. In aggregate, our findings lead us to propose that a regulatory cascade driven by changes in processing and stability of newly synthesized transcripts operates alongside the well-known transcriptional cascade as fission yeast cells enter meiosis.","doi":"10.1091/mbc.E10-05-0448","authors":"Cremona N, Potter K, Wise JA","authors_abbrev":"Cremona N et al.","pubmed_publication_date":"01 Jan 2011","pubmed_entrez_date":"2010-12-15","publication_year":"2011","canto_session_key":"d447dedb8ad51634","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30956973","title":"Role of pheromone recognition systems in creating new species of fission yeast.","citation":"Microb Cell 2019 Mar 11;6(4):209-211","abstract":"Many species, from mammals to microorganisms, release sex pheromones to attract a potential partner of the opposite sex. The combination of a pheromone and its corresponding receptor determines the species-specific ability of males and females to recognize each other, and therefore causes reproductive isolation. This barrier, which has arisen to restrict gene flow between mating pairs, might facilitate reproductive isolation leading to incipient speciation, but how do new combinations of pheromone and receptor evolve? Our recent study demonstrated an \"asymmetric\" pheromone recognition system in the fission yeast  Schizosaccharomyces pombe : among the two pheromone/receptor pairs in this yeast, recognition between one pair is stringent, while that between the other pair is rather relaxed. We speculate that the asymmetric properties of these pheromone recognition systems are beneficial for gradual evolution resulting in reproductive isolation in yeasts.","doi":"10.15698/mic2019.04.675","authors":"Seike T, Shimoda C","authors_abbrev":"Seike T et al.","pubmed_publication_date":"11 Mar 2019","pubmed_entrez_date":"2019-04-09","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-04-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22959349","title":"Telomere-nuclear envelope dissociation promoted by Rap1 phosphorylation ensures faithful chromosome segregation.","citation":"Curr Biol 2012 Oct 23;22(20):1932-7","abstract":"Efficient chromosomal movements are important for the fidelity of chromosome segregation during mitosis; however, movements are constrained during interphase by tethering of multiple domains to the nuclear envelope (NE). Higher eukaryotes undergo open mitosis accompanied by NE breakdown, enabling chromosomes to be released from the NE, whereas lower eukaryotes undergo closed mitosis, in which NE breakdown does not occur. Although the chromosomal movements in closed mitosis are thought to be restricted compared to open mitosis, the cells overcome this problem by an unknown mechanism that enables accurate chromosome segregation. Here, we report the spatiotemporal regulation of telomeres in Schizosaccharomyces pombe closed mitosis. We found that the telomeres, tethered to the NE during interphase, are transiently dissociated from the NE during mitosis. This dissociation from the NE is essential for accurate chromosome segregation because forced telomere tethering to the NE causes frequent chromosome loss. The phosphorylation of the telomere protein Rap1 during mitosis, primarily by Cdc2, impedes the interaction between Rap1 and Bqt4, a nuclear membrane protein, thereby inducing telomere dissociation from the NE. We propose that the telomere dissociation from the NE promoted by Rap1 phosphorylation is critical for the fidelity of chromosome segregation in closed mitosis.","doi":"10.1016/j.cub.2012.08.019","authors":"Fujita I, Nishihara Y, Tanaka M, Tsujii H, Chikashige Y, Watanabe Y, Saito M, Ishikawa F, Hiraoka Y, Kanoh J","authors_abbrev":"Fujita I et al.","pubmed_publication_date":"23 Oct 2012","pubmed_entrez_date":"2012-09-11","publication_year":"2012","canto_session_key":"67c7ee73b6bc39ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junko Kanoh","canto_first_approved_date":"2018-08-29 15:49:06","canto_approved_date":"2025-09-03 18:35:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-30 18:59:17","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Junko Kanoh","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.10","SPAC6G9.13c","SPAC1002.06c","SPAC19G12.13c","SPBC1778.02","SPBC11B10.09","SPAC16A10.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-08-29"},{"uniquename":"PMID:29439406","title":"Site-Specific Cleavage by Topoisomerase 2: A Mark of the Core Centromere.","citation":"Int J Mol Sci 2018 Feb 10;19(2)","abstract":"In addition to its roles in transcription and replication, topoisomerase 2 (topo 2) is crucial in shaping mitotic chromosomes and in ensuring the orderly separation of sister chromatids. As well as its recruitment throughout the length of the mitotic chromosome, topo 2 accumulates at the primary constriction. Here, following cohesin release, the enzymatic activity of topo 2 acts to remove residual sister catenations. Intriguingly, topo 2 does not bind and cleave all sites in the genome equally; one preferred site of cleavage is within the core centromere. Discrete topo 2-centromeric cleavage sites have been identified in α-satellite DNA arrays of active human centromeres and in the centromere regions of some protozoans. In this study, we show that topo 2 cleavage sites are also a feature of the centromere in  Schizosaccharomyces pombe , the metazoan  Drosophila melanogaster  and in another vertebrate species,  Gallus gallus  (chicken). In vertebrates, we show that this site-specific cleavage is diminished by depletion of CENP-I, an essential constitutive centromere protein. The presence, within the core centromere of a wide range of eukaryotes, of precise sites hypersensitive to topo 2 cleavage suggests that these mark a fundamental and conserved aspect of this functional domain, such as a non-canonical secondary structure.","doi":"10.3390/ijms19020534","authors":"Mills WE, Spence JM, Fukagawa T, Farr CJ","authors_abbrev":"Mills WE et al.","pubmed_publication_date":"10 Feb 2018","pubmed_entrez_date":"2018-02-15","publication_year":"2018","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2018-02-28 22:13:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35443188","title":"Septin filament compaction into rings requires the anillin Mid2 and contractile ring constriction.","citation":"Cell Rep 2022 Apr 19;39(3):110722","abstract":"Septin filaments assemble into high-order molecular structures that associate with membranes, acting as diffusion barriers and scaffold proteins crucial for many cellular processes. How septin filaments organize in such structures is still not understood. Here, we used fission yeast to explore septin filament organization during cell division and its cell cycle regulation. Live-imaging and polarization microscopy analysis uncovered that septin filaments are initially recruited as a diffuse meshwork surrounding the acto-myosin contractile ring (CR) in anaphase, which undergoes compaction into two rings when CR constriction is initiated. We found that the anillin-like protein Mid2 is necessary to promote this compaction step, possibly acting as a bundler for septin filaments. Moreover, Mid2-driven septin compaction requires inputs from the septation initiation network as well as CR constriction and the β(1,3)-glucan synthase Bgs1. This work highlights that anillin-mediated septin ring assembly is under strict cell cycle control.","doi":"10.1016/j.celrep.2022.110722","authors":"Arbizzani F, Mavrakis M, Hoya M, Ribas JC, Brasselet S, Paoletti A, Rincon SA","authors_abbrev":"Arbizzani F et al.","pubmed_publication_date":"19 Apr 2022","pubmed_entrez_date":"2022-04-20","publication_year":"2022","canto_session_key":"8cf1ed63b9952b4d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-04-22 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22122047","title":"Roles of RNAi in chromatin regulation and epigenetic inheritance.","citation":"Epigenomics 2010 Oct;2(5):613-26","abstract":"Rapid progress in our understanding of chromatin regulation has fueled considerable interest in epigenetic mechanisms governing the stable inheritance of chromatin states. Findings from several systems reveal small RNAs of the RNAi pathway as critical determinants of epigenetic gene silencing. Notably, recent investigations into the mechanisms of RNAi-mediated heterochromatin assembly in the fission yeast Schizosaccharomyces pombe have yielded new insights regarding the roles of RNAi in chromatin regulation and epigenetic inheritance.","doi":"10.2217/epi.10.46","authors":"Cam HP","authors_abbrev":"Cam HP","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2011-11-30","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33568651","title":"Replication dynamics of recombination-dependent replication forks.","citation":"Nat Commun 2021 Feb 10;12(1):923","abstract":"Replication forks restarted by homologous recombination are error prone and replicate both strands semi-conservatively using Pol δ. Here, we use polymerase usage sequencing to visualize in vivo replication dynamics of HR-restarted forks at an S. pombe replication barrier, RTS1, and model replication by Monte Carlo simulation. We show that HR-restarted forks synthesise both strands with Pol δ for up to 30 kb without maturing to a δ/ε configuration and that Pol α is not used significantly on either strand, suggesting the lagging strand template remains as a gap that is filled in by Pol δ later. We further demonstrate that HR-restarted forks progress uninterrupted through a fork barrier that arrests canonical forks. Finally, by manipulating lagging strand resection during HR-restart by deleting pku70, we show that the leading strand initiates replication at the same position, signifying the stability of the 3' single strand in the context of increased resection.","doi":"10.1038/s41467-021-21198-0","authors":"Naiman K, Campillo-Funollet E, Watson AT, Budden A, Miyabe I, Carr AM","authors_abbrev":"Naiman K et al.","pubmed_publication_date":"10 Feb 2021","pubmed_entrez_date":"2021-02-11","publication_year":"2021","canto_session_key":"3e0515d51b776f10","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tony Carr","canto_first_approved_date":"2021-03-15 15:43:50","canto_approved_date":"2022-11-05 22:02:47","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2021-03-09 15:39:01","canto_added_date":"2021-02-13 01:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tony Carr","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.02","SPAC3H5.06c","SPCC23B6.05c","SPCC126.02c","SPAC22F8.07c","SPBC336.06c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2021-03-15"},{"uniquename":"PMID:8202381","title":"Fission yeast gene structure and recognition.","citation":"Nucleic Acids Res 1994 May 11;22(9):1750-9","abstract":"A database of 210 Schizosaccharomyces pombe DNA sequences (524,794 bp) was extracted from GenBank (release number 81.0) and examined by a number of methods in order to characterize statistical features of these sequences that might serve as signals or constraints for messenger RNA splicing. The statistical information compiled includes splicing signal (donor, acceptor and branch site) profiles, translational initiation start profile, exon/intron length distributions, ORF distribution, CDS size distribution, codon usage table, and 6-tuple distribution. The information content of the various signals are also presented. A rule-based interactive computer program for finding introns called INTRON.PLOT has been developed and was used to successfully analyze 7 newly sequenced genes.","authors":"Zhang MQ, Marr TG","authors_abbrev":"Zhang MQ et al.","pubmed_publication_date":"11 May 1994","pubmed_entrez_date":"1994-05-11","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15791259","title":"Fission yeast Mes1p ensures the onset of meiosis II by blocking degradation of cyclin Cdc13p.","citation":"Nature 2005 Mar 24;434(7032):529-33","abstract":"Meiosis is a special form of nuclear division to generate eggs, sperm and spores in eukaryotes. Meiosis consists of the first (MI) and the second (MII) meiotic divisions, which occur consecutively. MI is reductional, in which homologous chromosomes derived from parents segregate. MI is supported by an elaborate mechanism involving meiosis-specific cohesin and its protector. MII is equational, in which replicated sister-chromatids separate as in mitosis. MII is generally considered to mimic mitosis in mechanism. However, fission yeast Mes1p is essential for MII but dispensable for mitosis. The mes1-B44 mutant arrests before MII. Transcription of mes1 is low in vegetative cells and boosted in a narrow window between late MI and late MII. The mes1 mRNA undergoes meiosis-specific splicing. Here we show that Mes1p is a factor that suppresses the degradation of cyclin Cdc13p at anaphase I. Mes1p binds to Slp1p, an activator of APC/C (anaphase promoting complex/cyclosome), and counteracts its function to engage Cdc13p in proteolysis. Inhibition of APC/C-dependent degradation of Cdc13p by Mes1p was reproduced in a Xenopus egg extract. We therefore propose that Mes1p has a key function in saving a sufficient level of MPF (M-phase-promoting factor) activity required for the execution of MII.","authors":"Izawa D, Goto M, Yamashita A, Yamano H, Yamamoto M","authors_abbrev":"Izawa D et al.","pubmed_publication_date":"24 Mar 2005","pubmed_entrez_date":"2005-03-26","publication_year":"2005","canto_session_key":"d5580f5ec3f29d85","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-05-10 14:54:13","canto_approved_date":"2023-01-26 10:32:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-12 17:17:10","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC821.08c","SPAPB2B4.03","SPBC14C8.01c","SPAC5D6.08c","SPBC582.03","SPBC1198.12"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2016-05-10"},{"uniquename":"PMID:31941401","title":"Atg38-Atg8 interaction in fission yeast establishes a positive feedback loop to promote autophagy.","citation":"Autophagy 2020 Nov;16(11):2036-2051","abstract":"Macroautophagy (autophagy) is driven by the coordinated actions of core autophagy-related (Atg) proteins. Atg8, the core Atg protein generally considered acting most downstream, has recently been shown to interact with other core Atg proteins via their Atg8-family-interacting motifs (AIMs). However, the extent, functional consequence, and evolutionary conservation of such interactions remain inadequately understood. Here, we show that, in the fission yeast  Schizosaccharomyces pombe , Atg38, a subunit of the phosphatidylinositol 3-kinase (PtdIns3K) complex I, interacts with Atg8 via an AIM, which is highly conserved in Atg38 proteins of fission yeast species, but not conserved in Atg38 proteins of other species. This interaction recruits Atg38 to Atg8 on the phagophore assembly site (PAS) and consequently enhances PAS accumulation of the PtdIns3K complex I and Atg proteins acting downstream of the PtdIns3K complex I, including Atg8. The disruption of the Atg38-Atg8 interaction leads to the reduction of autophagosome size and autophagic flux. Remarkably, the loss of this interaction can be compensated by an artificial Atg14-Atg8 interaction. Our findings demonstrate that the Atg38-Atg8 interaction in fission yeast establishes a positive feedback loop between Atg8 and the PtdIns3K complex I to promote efficient autophagosome formation, underscore the prevalence and diversity of AIM-mediated connections within the autophagic machinery, and reveal unforeseen flexibility of such connections.  Abbreviations : AIM: Atg8-family-interacting motif; AP-MS: affinity purification coupled with mass spectrometry; Atg: autophagy-related; FLIP: fluorescence loss in photobleaching; PAS: phagophore assembly site;  PB: piggyBac ; PE: phosphatidylethanolamine; PtdIns3K: phosphatidylinositol 3-kinase; PtdIns3P: phosphatidylinositol 3-phosphate.","doi":"10.1080/15548627.2020.1713644","authors":"Yu ZQ, Sun LL, Jiang ZD, Liu XM, Zhao D, Wang HT, He WZ, Dong MQ, Du LL","authors_abbrev":"Yu ZQ et al.","pubmed_publication_date":"Nov 2020","pubmed_entrez_date":"2020-01-17","publication_year":"2020","canto_session_key":"cd18b7b226e58591","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Zhong-Qiu Yu","canto_first_approved_date":"2020-02-29 17:18:01","canto_approved_date":"2024-11-30 09:49:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-29 16:11:02","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Zhong-Qiu Yu","community_curator":true,"annotation_count":84,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC10F6.11c","SPBC405.05","SPBC1711.11","SPBC119.07","SPBC4B4.10c","SPBC660.08","SPAC25A8.02","SPBC15D4.07c","SPAC823.16c","HGNC:19692","SPBC18H10.19","SPBP8B7.24c","SPAC4F10.07c","SPAC20G8.10c","SPAC458.05","SPBC31E1.01c"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2020-02-29"},{"uniquename":"PMID:24662054","title":"The Mi-2 homolog Mit1 actively positions nucleosomes within heterochromatin to suppress transcription.","citation":"Mol Cell Biol 2014 Jun;34(11):2046-61","abstract":"Mit1 is the putative chromatin remodeling subunit of the fission yeast Snf2/histone deacetylase (HDAC) repressor complex (SHREC) and is known to repress transcription at regions of heterochromatin. However, how Mit1 modifies chromatin to silence transcription is largely unknown. Here we report that Mit1 mobilizes histone octamers in vitro and requires ATP hydrolysis and conserved chromatin tethering domains, including a previously unrecognized chromodomain, to remodel nucleosomes and silence transcription. Loss of Mit1 remodeling activity results in nucleosome depletion at specific DNA sequences that display low intrinsic affinity for the histone octamer, but its contribution to antagonizing RNA polymerase II (Pol II) access and transcription is not restricted to these sites. Genetic epistasis analyses demonstrate that SHREC subunits and the transcription-coupled Set2 histone methyltransferase, which is involved in suppression of cryptic transcription at actively transcribed regions, cooperate to silence heterochromatic transcripts. In addition, we have demonstrated that Mit1's remodeling activity contributes to SHREC function independently of Clr3's histone deacetylase activity on histone H3 K14. We propose that Mit1 is a chromatin remodeling factor that cooperates with the Clr3 histone deacetylase of SHREC and other chromatin modifiers to stabilize heterochromatin structure and to prevent access to the transcriptional machinery.","doi":"10.1128/MCB.01609-13","authors":"Creamer KM, Job G, Shanker S, Neale GA, Lin YC, Bartholomew B, Partridge JF","authors_abbrev":"Creamer KM et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-03-26","publication_year":"2014","canto_session_key":"1ced65ea728cb6e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-15 16:13:12","canto_approved_date":"2025-12-11 10:13:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-15 16:12:49","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPBC428.08c","SPAC18G6.02c","SPAC17G8.13c","SPAC1952.05","SPCC306.04c","SPAC29B12.02c","SPBC800.03","SPBC16C6.10","SPBP35G2.10"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2017-02-15"},{"uniquename":"PMID:18789407","title":"Small RNA-directed heterochromatin formation in the context of development: what flies might learn from fission yeast.","citation":"Biochim Biophys Acta 2009 Jan;1789(1):3-16","abstract":"A link between the RNAi system and heterochromatin formation has been established in several model organisms including Schizosaccharomyces pombe and Arabidopsis thaliana. However, the data to support a role for small RNAs and the associated machinery in transcriptional gene silencing in animal systems is more tenuous. Using the S. pombe system as a model, we analyze the role of small RNA pathway components and associated small RNAs in regulating transposable elements and potentially directing heterochromatin formation at these elements in Drosophila melanogaster.","doi":"10.1016/j.bbagrm.2008.08.002","authors":"Huisinga KL, Elgin SC","authors_abbrev":"Huisinga KL et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2008-09-16","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3545224","title":"Mutagenicity studies on tiopronin.","citation":"Arzneimittelforschung 1986 Nov;36(11):1601-4","abstract":"alpha-Mercaptopropionylglycine (tiopronin, Mucolysin), a drug endowed with an interesting mucolytic activity, was tested for mutagenicity by means of the following in vitro and in vivo tests: mutagenesis on S. typhimurium with and without metabolic activation, genetic mutation on S. pombe P1 with and without metabolic activation, gene conversion on S. cerevisiae D4 with and without metabolic activation, urinary assay in the mouse with S. cerevisiae D4, host mediated assay in the mouse with S. cerevisiae D4 and micronucleus test in the mouse. On the basis of the results obtained tiopronin proved to be free of mutagenic activity.","authors":"Dubini F, Sezzano P, Berti MA, Coppi G","authors_abbrev":"Dubini F et al.","pubmed_publication_date":"Nov 1986","pubmed_entrez_date":"1986-11-01","publication_year":"1986","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12377123","title":"Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine.","citation":"Structure 2002 Oct;10(10):1371-81","abstract":"Riboflavin synthase catalyzes the disproportionation of 6,7-dimethyl-8-ribityllumazine affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. We have determined the structure of riboflavin synthase from Schizosaccharomyces pombe in complex with the substrate analog, 6-carboxyethyl-7-oxo-8-ribityllumazine at 2.1 A resolution. In contrast to the homotrimeric solution state of native riboflavin synthase, we found the enzyme to be monomeric in the crystal structure. Structural comparison of the riboflavin synthases of S. pombe and Escherichia coli suggests oligomer contact sites and delineates the catalytic site for dimerization of the substrate and subsequent fragmentation of the pentacyclic intermediate. The pentacyclic substrate dimer was modeled into the proposed active site, and its stereochemical features were determined. The model suggests that the substrate molecule at the C-terminal domain donates a four-carbon unit to the substrate molecule bound at the N-terminal domain of an adjacent subunit in the oligomer.","authors":"Gerhardt S, Schott AK, Kairies N, Cushman M, Illarionov B, Eisenreich W, Bacher A, Huber R, Steinbacher S, Fischer M","authors_abbrev":"Gerhardt S et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-10-16","publication_year":"2002","canto_session_key":"6b4c90e2409bba97","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-07-25 15:21:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-25 14:27:46","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1450.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-25","pdb_entries":[{"pdb_id":"1kzl","gene_chains":[{"gene_uniquename":"SPCC1450.13c","chain":"A","position":"1-208"}],"title":"Riboflavin Synthase from S.pombe bound to Carboxyethyllumazine","entry_authors":"Gerhardt S,Schott AK,Kairies N,Cushman M,Illarionov B,Eisenreich W,Bacher A,Huber R,Steinbacher S,Fischer M","entry_authors_abbrev":"Gerhardt S et al.","reference_uniquename":"PMID:12377123","experimental_method":"X-ray","resolution":"2.1"}]},{"uniquename":"PMID:9819352","title":"The novel murine calmodulin-binding protein Sha1 disrupts mitotic spindle and replication checkpoint functions in fission yeast.","citation":"J Cell Sci 1998 Dec 18;111 ( Pt 24):3609-19","abstract":"Entry into mitosis is normally blocked in eukaryotic cells that have not completed replicative DNA synthesis; this 'S-M' checkpoint control is fundamental to the maintenance of genomic integrity. Mutants of the fission yeast Schizosaccharomyces pombe defective in the S-M checkpoint fail to arrest the cell cycle when DNA replication is inhibited and hence attempt mitosis and cell division with unreplicated chromosomes, resulting in the 'cut' phenotype. In an attempt to identify conserved molecules involved in the S-M checkpoint we have screened a regulatable murine cDNA library in S. pombe and have identified cDNAs that induce the cut phenotype in cells arrested in S phase by hydroxyurea. One such cDNA encodes a novel protein with multiple calmodulin-binding motifs that, in addition to its effects on the S-M checkpoint, perturbed mitotic spindle functions, although spindle pole duplication was apparently normal. Both aspects of the phenotype induced by this cDNA product, which we term Sha1 (for spindle and hydroxyurea checkpoint abnormal), were suppressed by simultaneous overexpression of calmodulin. Sha1 is structurally related to the product of the Drosophila gene abnormal spindle (asp). These data suggest that calmodulin-binding protein(s) are important in the co-ordination of mitotic spindle functions with mitotic entry in fission yeast, and probably also in multicellular eukaryotes.","authors":"Craig R, Norbury C","authors_abbrev":"Craig R et al.","pubmed_publication_date":"18 Dec 1998","pubmed_entrez_date":"1998-11-20","publication_year":"1998","canto_session_key":"ad663f2f5e5f3dc3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-11-24 13:01:03","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-24 13:00:57","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-11-24"},{"uniquename":"PMID:11870212","title":"Kinesins klp5(+) and klp6(+) are required for normal chromosome movement in mitosis.","citation":"J Cell Sci 2002 Mar 01;115(Pt 5):931-40","abstract":"Proper mitotic chromosome segregation requires dynamic interactions between spindle microtubules and kinetochores. Here we demonstrate that two related fission yeast kinesins, klp5(+) and klp6(+), are required for normal chromosome segregation in mitosis. Null mutants frequently lack a normal metaphase chromosome alignment. Chromosome pairs move back and forth along the spindle for an extended period prior to sister chromatid separation, a phenotype reminiscent of the loss of CENP-E in metazoans. Ultimately, sister chromatids segregate, regardless of chromosome position along the spindle, and viable daughter cells are usually produced. The initiation of anaphase B is sometimes delayed, but the rate of spindle elongation is similar to wildtype. Despite a delay, anaphase B often begins before anaphase A is completed. The klp5Delta and klp6Delta null mutants are synthetically lethal with a deletion of the spindle assembly checkpoint gene, bub1(+), several mutants in components of the anaphase promoting complex, and a cold sensitive allele of the kinetochore and microtubule-binding protein, Dis1p. Klp5p-GFP and Klp6p-GFP localize to kinetochores from prophase to the onset of anaphase A, but relocalize to the spindle midzone during anaphase B. These data indicate that Klp5p and Klp6p are kinetochore kinesins required for normal chromosome movement in prometaphase.","authors":"West RR, Malmstrom T, McIntosh JR","authors_abbrev":"West RR et al.","pubmed_publication_date":"01 Mar 2002","pubmed_entrez_date":"2002-03-01","publication_year":"2002","canto_session_key":"e75b1422bd29e157","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-31 11:38:52","canto_approved_date":"2019-11-05 15:37:59","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-10-30 18:40:44","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.15c","SPBC2F12.13","SPAC24H6.05","SPCC1322.12c","SPCC736.14"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-10-31"},{"uniquename":"PMID:24904045","title":"Genomic evidence for adaptation by gene duplication.","citation":"Genome Res 2014 Aug;24(8):1356-62","abstract":"Gene duplication is widely believed to facilitate adaptation, but unambiguous evidence for this hypothesis has been found in only a small number of cases. Although gene duplication may increase the fitness of the involved organisms by doubling gene dosage or neofunctionalization, it may also result in a simple division of ancestral functions into daughter genes, which need not promote adaptation. Hence, the general validity of the adaptation by gene duplication hypothesis remains uncertain. Indeed, a genome-scale experiment found similar fitness effects of deleting pairs of duplicate genes and deleting individual singleton genes from the yeast genome, leading to the conclusion that duplication rarely results in adaptation. Here we contend that the above comparison is unfair because of a known duplication bias among genes with different fitness contributions. To rectify this problem, we compare homologous genes from the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe. We discover that simultaneously deleting a duplicate gene pair in S. cerevisiae reduces fitness significantly more than deleting their singleton counterpart in S. pombe, revealing post-duplication adaptation. The duplicates-singleton difference in fitness effect is not attributable to a potential increase in gene dose after duplication, suggesting that the adaptation is owing to neofunctionalization, which we find to be explicable by acquisitions of binary protein-protein interactions rather than gene expression changes. These results provide genomic evidence for the role of gene duplication in organismal adaptation and are important for understanding the genetic mechanisms of evolutionary innovation.","doi":"10.1101/gr.172098.114","authors":"Qian W, Zhang J","authors_abbrev":"Qian W et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-06-07","publication_year":"2014","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40668850","title":"The heme-regulated inhibitor kinase Hri1 is activated in response to aminolevulinic acid deficiency in Schizosaccharomyces pombe.","citation":"PLoS Genet 2025 Jul;21(7):e1011797","abstract":"A key mechanism for regulating the initiation of protein synthesis in response to various stresses involves the phosphorylation of the α subunit of eukaryotic initiation factor 2 (eIF2α). Schizosaccharomyces pombe possesses three distinct eIF2α kinases: Hri1, Hri2, and Gcn2. Using a strain that is unable to synthesize heme de novo (hem1Δ), global transcriptome analysis reveals that among the genes encoding these kinases, hri1+ is the most strongly induced under δ-aminolevulinate (ALA)-limiting conditions. The induction of hri1+ consistently correlates with increased eIF2α phosphorylation and a reduction in global protein translation in ALA-starved hem1Δ cells. In contrast, hem1Δ cells lacking hri1+ (hri1Δ) exhibit poor eIF2α phosphorylation under the same stress conditions. When ALA-starved hem1Δ hri1Δ cells are subsequently transferred to a medium supplemented with exogenous hemin, they exhibit impaired growth compared to ALA-starved hem1Δ cells expressing the endogenous hri1+ allele or hem1Δ hri1Δ hri2Δ gcn2Δ cells expressing functional hri1+ and hri1+-GFP alleles. Consistent with its role as a heme-sensing eIF2α kinase, further analysis by absorbance spectroscopy demonstrates that Hri1 binds to hemin, with an equilibrium dissociation constant (KD) of 0.11 µM. In contrast, a truncated form of Hri1 (from residues 1-185) fails to interact with hemin. Taken together, these findings provide the first report of a fungal eIF2α kinase being activated in response to stress directly linked to a defect in heme homeostasis.","doi":"10.1371/journal.pgen.1011797","authors":"Plante S, Brault A, Avino M, Sakouhi H, Lo Ying Ping F, Vahsen T, Labbé S","authors_abbrev":"Plante S et al.","pubmed_publication_date":"Jul 2025","pubmed_entrez_date":"2025-07-16","publication_year":"2025","canto_session_key":"51999fe60729ef45","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-16 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7625281","title":"A species-specific interaction of rad51 and rad52 proteins in eukaryotes.","citation":"Adv Biophys 1995;31:93-100","abstract":"The structures and properties of the Rad51 and Rad52 proteins in eukaryotes are described. Both proteins form a complex and are responsible for recombination and repair reactions. The N-terminal region of the Rad51 protein interacts with the C-terminal region of the Rad52 protein. Species-specific interaction is probably essential for the functioning of these genes.","authors":"Ogawa T, Shinohara A, Ikeya T","authors_abbrev":"Ogawa T et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39969966","title":"Intracellular diffusion in the cytoplasm increases with cell size in fission yeast.","citation":"Mol Biol Cell 2025 Feb 19;:mbcE24110488","abstract":"Diffusion in the cytoplasm can greatly impact cellular processes, yet regulation of macromolecular diffusion remains poorly understood. There is increasing evidence that cell size affects the density and macromolecular composition of the cytoplasm. Here, we studied whether cell size affects diffusion at the scale of macromolecules tens of microns in diameter. We analyzed the diffusive motions of intracellular genetically-encoded multimeric 40 nm nanoparticles (cytGEMs) in the cytoplasm of the fission yeast  Schizosaccharomyces pombe . Using cell size mutants, we showed that cytGEMs diffusion coefficients decreased in smaller cells and increased in larger cells. This increase in diffusion in large cells may be due to a decrease in the DNA-to-Cytoplasm ratio, as diffusion was not affected in large multinucleate cytokinesis mutant cells. In investigating the underlying causes of altered cytGEMs diffusion, we found that the proteomes of large and small cells exhibited size-specific changes, including the sub-scaling of ribosomal proteins in large cells. Comparison with a similar dataset from human cells revealed that features of size-dependent proteome remodeling were conserved. These studies demonstrate that cell size is an important parameter in determining the biophysical properties and the composition of the cytoplasm.","doi":"10.1091/mbc.E24-11-0488","authors":"Tan C, Lanz MC, Swaffer M, Skotheim J, Chang F","authors_abbrev":"Tan C et al.","pubmed_publication_date":"19 Feb 2025","pubmed_entrez_date":"2025-02-19","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-02-20 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24798735","title":"The novel proteins Rng8 and Rng9 regulate the myosin-V Myo51 during fission yeast cytokinesis.","citation":"J Cell Biol 2014 May 12;205(3):357-75","abstract":"The myosin-V family of molecular motors is known to be under sophisticated regulation, but our knowledge of the roles and regulation of myosin-Vs in cytokinesis is limited. Here, we report that the myosin-V Myo51 affects contractile ring assembly and stability during fission yeast cytokinesis, and is regulated by two novel coiled-coil proteins, Rng8 and Rng9. Both rng8Δ and rng9Δ cells display similar defects as myo51Δ in cytokinesis. Rng8 and Rng9 are required for Myo51's localizations to cytoplasmic puncta, actin cables, and the contractile ring. Myo51 puncta contain multiple Myo51 molecules and walk continuously on actin filaments in rng8(+) cells, whereas Myo51 forms speckles containing only one dimer and does not move efficiently on actin tracks in rng8Δ. Consistently, Myo51 transports artificial cargos efficiently in vivo, and this activity is regulated by Rng8. Purified Rng8 and Rng9 form stable higher-order complexes. Collectively, we propose that Rng8 and Rng9 form oligomers and cluster multiple Myo51 dimers to regulate Myo51 localization and functions.","doi":"10.1083/jcb.201308146","authors":"Wang N, Lo Presti L, Zhu YH, Kang M, Wu Z, Martin SG, Wu JQ","authors_abbrev":"Wang N et al.","pubmed_publication_date":"12 May 2014","pubmed_entrez_date":"2014-05-07","publication_year":"2014","canto_session_key":"85219fa3fd50b9ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jian-Qiu Wu","canto_first_approved_date":"2018-07-01 07:55:52","canto_approved_date":"2023-05-17 15:55:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-30 09:16:05","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":41,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jian-Qiu Wu","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC550.11","SPAC4H3.14c","SPAC4A8.05c","SPAC4F10.10c","SPBC1773.10c","SPAC926.03","SPCC645.05c","SPAC1556.07","SPBC2D10.14c","SPCC1919.10c","SPAC4A8.15c","SPAC13G6.12c","SPBP8B7.02","SPAC12G12.07c","SPAC23H3.09c","SPAC11H11.06","SPAC15A10.08"],"gene_count":17,"ltp_gene_count":8,"approved_date":"2018-07-01"},{"uniquename":"PMID:16361266","title":"A novel experimental approach for systematic identification of box H/ACA snoRNAs from eukaryotes.","citation":"Nucleic Acids Res 2005 Dec 15;33(22):e194","abstract":"Box H/ACA snoRNAs represent an abundant group of small non-coding RNAs mainly involved in the pseudouridylation of rRNAs and/or snRNAs in eukaryotes and Archaea. In this study, we describe a novel experimental method for systematic identification of box H/ACA snoRNAs from eukaryotes. In the specialized cDNA libraries constructed by this method with total cellular RNAs from human blood cells, the high efficiency of cloning for diverse box H/ACA snoRNAs was achieved and seven novel species of this snoRNA family were identified from human for the first time. Furthermore, the novel method has been successfully applied for the identification of the box H/ACA snoRNAs from Drosophila and the fission yeast, demonstrating a powerful ability for systematic analysis of box H/ACA snoRNAs in a broad spectrum of eukaryotes.","authors":"Gu AD, Zhou H, Yu CH, Qu LH","authors_abbrev":"Gu AD et al.","pubmed_publication_date":"15 Dec 2005","pubmed_entrez_date":"2005-12-20","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15135075","title":"Analysis of the S. pombe signalling scaffold protein Cdc11p reveals an essential role for the N-terminal domain in SIN signalling.","citation":"FEBS Lett 2004 May 07;565(1-3):176-80","abstract":"The initiation of cytokinesis in the fission yeast Schizosaccharomyces pombe is signalled by the septation initiation network (SIN). Signalling originates from the spindle pole body (SPB), where SIN proteins are anchored by a scaffold composed of cdc11p and sid4p. Cdc11p links the other SIN proteins to sid4p and the SPB. Homologues of cdc11p have been identified in Saccharomyes cerevisiae (Nud1p) and human cells (Centriolin). We have defined functional domains of cdc11p by analysis of deletion mutants. We demonstrate that the C-terminal end of cdc11p is necessary for SPB localisation. We also show that the N-terminal domain is necessary and sufficient for signal transduction, since tethering of this domain to the SPB will substitute for cdc11p in SIN function.","authors":"Krapp A, Cano E, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"07 May 2004","pubmed_entrez_date":"2004-05-12","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12725533","title":"Structural genomics of lipid signaling domains.","citation":"Oncol Res 2003;13(6-10):421-8","abstract":"Signaling domains have been identified by the analysis of data derived from biochemical studies, molecular cloning, or genetic studies. With the availability of genomic information from many organisms and the improved sensitivity in homology detection techniques, many new domains are being identified. In an attempt to understand biochemical and biological function of these domains, we have started a small-scale structural genomics, or structural biology with genomic approach. Two examples from our recent work are steroidogenic acute regulatory protein (StAR)-related lipid-transfer (START) domain and inositol polyphosphate 5-phosphatase catalytic (IPP5C) domain. Crystal structure of human MLN64-START domain revealed a hollowed-out protein containing a hydrophobic tunnel just large enough to bind one molecule of cholesterol and completely exclude it from solvent. This structure suggests that the START domain is a classical type of lipid transporter. On the contrary, the function of IPP5C domain has been extensively studied for a long time, but its catalytic mechanism, positional selectivity, and diverse substrate specificity remained mysterious due to the unavailability of three-dimensional structure. With the structural genomic approach, the first structure of IPP5C domain was solved from a S. pombe protein that is now known as SPsynaptojanin and the structure gave us answers to some of these questions.","authors":"Tsujishita Y","authors_abbrev":"Tsujishita Y","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-05-03","publication_year":"2003","canto_session_key":"2ad3b1701e57c350","canto_annotation_status":"APPROVED","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-08 17:12:49","canto_approved_date":"2019-11-08 17:12:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-08 17:12:43","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9E9.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-11-08"},{"uniquename":"PMID:24928510","title":"Glucose activates TORC2-Gad8 protein via positive regulation of the cAMP/cAMP-dependent protein kinase A (PKA) pathway and negative regulation of the Pmk1 protein-mitogen-activated protein kinase pathway.","citation":"J Biol Chem 2014 Aug 01;289(31):21727-37","abstract":"The target of rapamycin (TOR) kinase belongs to the highly conserved eukaryotic family of phosphatidylinositol 3-kinase-related kinases. TOR proteins are found at the core of two evolutionary conserved complexes, known as TORC1 and TORC2. In fission yeast, TORC2 is dispensable for proliferation under optimal growth conditions but is required for starvation and stress responses. TORC2 has been implicated in a wide variety of functions; however, the signals that regulate TORC2 activity have so far remained obscure. TORC2 has one known direct substrate, the AGC kinase Gad8, which is related to AKT in human cells. Gad8 is phosphorylated by TORC2 at Ser-546 (equivalent to AKT Ser-473), leading to its activation. Here, we show that glucose is necessary and sufficient to induce Gad8 Ser-546 phosphorylation in vivo and Gad8 kinase activity in vitro. The glucose signal that activates TORC2-Gad8 is mediated via the cAMP/PKA pathway, a major glucose-sensing pathway. By contrast, Pmk1, similar to human extracellular signal-regulated kinases and a major stress-induced mitogen activated protein kinase (MAPK) in fission yeast, inhibits TORC2-dependent Gad8 phosphorylation and activation. Inhibition of TORC2-Gad8 also occurs in response to ionic or osmotic stress, in a manner dependent on the cAMP/PKA and Pmk1-MAPK signaling pathways. Our findings highlight the significance of glucose availability in regulation of TORC2-Gad8 and indicate a novel link between the cAMP/PKA, Pmk1/MAPK, and TORC2-Gad8 signaling.","doi":"10.1074/jbc.M114.573824","authors":"Cohen A, Kupiec M, Weisman R","authors_abbrev":"Cohen A et al.","pubmed_publication_date":"01 Aug 2014","pubmed_entrez_date":"2014-06-15","publication_year":"2014","canto_session_key":"63373b8b600ffce2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronit Weisman","canto_first_approved_date":"2020-06-08 14:16:10","canto_approved_date":"2023-01-03 15:56:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-02 12:21:47","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":58,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Ronit Weisman","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC297.03","SPBC12D12.04c","SPBC23E6.08","SPBC32H8.07","SPAC23H3.13c","SPCC24B10.07","SPCC285.09c","SPCC1753.02c","SPCC74.03c","SPAC16.01","SPBC106.10","SPBC30D10.10c","SPBC16G5.15c","SPBC119.08"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2020-06-08"},{"uniquename":"PMID:26931605","title":"The price of independence: cell separation in fission yeast.","citation":"World J Microbiol Biotechnol 2016 Apr;32(4):65","abstract":"The ultimate goal of cell division is to give rise to two viable independent daughter cells. A tight spatial and temporal regulation between chromosome segregation and cytokinesis ensures the viability of the daughter cells. Schizosaccharomyces pombe, commonly known as fission yeast, has become a leading model organism for studying essential and conserved mechanisms of the eukaryotic cell division process. Like many other eukaryotic cells it divides by binary fission and the cleavage furrow undergoes ingression due to the contraction of an actomyosin ring. In contrast to mammalian cells, yeasts as cell-walled organisms, also need to form a division septum made of cell wall material to complete the process of cytokinesis. The division septum is deposited behind the constricting ring and it will constitute the new ends of the daughter cells. Cell separation also involves cell wall degradation and this process should be precisely regulated to avoid cell lysis. In this review, we will give a brief overview of the whole cytokinesis process in fission yeast, from the positioning and assembly of the contractile ring to the final step of cell separation, and the problems generated when these processes are not precise.","doi":"10.1007/s11274-016-2021-8","authors":"Martín-García R, Santos B","authors_abbrev":"Martín-García R et al.","pubmed_publication_date":"Apr 2016","pubmed_entrez_date":"2016-03-03","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-03-06 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7476442","title":"Genetic and biochemical analysis of Cdc42p function in Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Methods Enzymol 1995;256:281-90","abstract":"","authors":"Posada J, Miller PJ, McCullough J, Ziman M, Johnson DI","authors_abbrev":"Posada J et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17986863","title":"The Gcn2 kinase as a cell cycle regulator.","citation":"Cell Cycle 2007 Nov 15;6(22):2768-72","abstract":"Cell cycle progression through G1 phase is of particular importance because this is the phase where the decision to embark on another cell cycle is made. An aberrant G1/S transition often leads to cell cycle deregulation and cancer development. Therefore, there is a complex regulatory network to ensure timely entry into S phase, coordinating initiation of DNA replication with growth and stress signals. We have studied the response of fission yeast cells to ultraviolet (UV) irradiation in G1 phase and identified a Gcn2-dependent checkpoint that delays entry into S phase. UV irradiation activates Gcn2 which, in turn, phosphorylates the translation initiation factor eIF2alpha and depresses translation. Phosphorylation of eIF2alpha is a well-known response to various forms of stress, but whether or how this response is causing the specific cell cycle effects is not known. Here we discuss the relationships between Gcn2 activity, eIF2alpha phosphorylation, translation downregulation and cell cycle delay.","authors":"Grallert B, Boye E","authors_abbrev":"Grallert B et al.","pubmed_publication_date":"15 Nov 2007","pubmed_entrez_date":"2007-11-08","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41996234","title":"Dose-dependent mitochondrial H 2 O 2  signaling drives toxicity or stress adaptation and longevity in fission yeast.","citation":"Cell Rep 2026 Apr 16;45(4):117277","abstract":"The spatiotemporal dynamics of hydrogen peroxide (H 2 O 2 ) signaling and its effects on gene expression and cell fitness remain unclear. Using fission yeast, we applied genetic tools to control and monitor intracellular H 2 O 2  levels. We expressed the H 2 O 2  biosensor HyPer7 in four subcellular compartments, overexpressed D-amino acid oxidase (Dao1) in specific locations to induce localized H 2 O 2  production, and modulated H 2 O 2  detoxification or sensing. H 2 O 2  concentrations showed 2- to 5-fold reductions across membranes, and D-amino acid treatments generated nanomolar H 2 O 2  levels in Dao1-expressing cells. Mitochondrial-targeted Dao1 produced H 2 O 2  fluxes capable of reaching the nucleus. While high mitochondrial H 2 O 2  disrupted mitochondrial morphology and respiration, lower levels triggered antioxidant defenses, enhancing stress resistance and longevity. These findings establish a quantitative framework for mitochondrial H 2 O 2  signaling and demonstrate that localized redox signals from mitochondria can either promote or impair cellular fitness depending on their intensity.","doi":"10.1016/j.celrep.2026.117277","authors":"de Cubas L, Crevatin MF, Vega M, Boronat S, Ayté J, Hidalgo E","authors_abbrev":"de Cubas L et al.","pubmed_publication_date":"16 Apr 2026","pubmed_entrez_date":"2026-04-17","publication_year":"2026","canto_session_key":"e7f105a75ddafcf2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-17 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22139915","title":"The telomeric transcriptome of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2012 Apr;40(7):2995-3005","abstract":"Eukaryotic telomeres are transcribed into telomeric repeat-containing RNA (TERRA). Telomeric transcription has been documented in mammals, birds, zebra fish, plants and budding yeast. Here we show that the chromosome ends of Schizosaccharomyces pombe produce distinct RNA species. As with budding yeast and mammals, S. pombe contains G-rich TERRA molecules and subtelomeric RNA species transcribed in the opposite direction of TERRA (ARRET). Moreover, fission yeast chromosome ends produce two novel RNA species: C-rich telomeric repeat-containing transcripts (ARIA) and subtelomeric transcripts complementary to ARRET (αARRET). RNA polymerase II (RNAPII) associates with pombe chromosome ends in vivo and the telomeric factor Rap1 negatively regulates this association, as well as the cellular accumulation of RNA emanating from chromosome ends. We also show that the RNAPII subunit Rpb7 and the non-canonical poly(A) polymerases Cid12 and Cid14 are involved in the regulation of TERRA, ARIA, ARRET and αARRET transcripts. We confirm the evolutionary conservation of telomere transcription, and reveal intriguing similarities and differences in the composition and regulation of telomeric transcripts among model organisms.","doi":"10.1093/nar/gkr1153","authors":"Bah A, Wischnewski H, Shchepachev V, Azzalin CM","authors_abbrev":"Bah A et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2011-12-06","publication_year":"2012","canto_session_key":"88220312b9269e43","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-11 14:44:15","canto_approved_date":"2022-04-01 14:04:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-19 15:15:32","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.06","SPACUNK4.06c","SPBC1778.02","SPAC17H9.01","SPAC19D5.03","SPAC12G12.13c","SPBC543.03c","SPCC663.12"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2013-10-11"},{"uniquename":"PMID:2537310","title":"Essential roles of the RNA polymerase I largest subunit and DNA topoisomerases in the formation of fission yeast nucleolus.","citation":"J Cell Biol 1989 Feb;108(2):243-53","abstract":"A temperature-sensitive lethal mutant nuc1-632 of Schizosaccharomyces pombe shows marked reduction in macromolecular synthesis and a defective nuclear phenotype with an aberrant nucleolus, indicating a structural role of the nuc1+ gene product in nucleolar organization. We cloned the nuc1+ gene by transformation and found that it appears to encode the largest subunit of RNA polymerase I. We raised antisera against nuc1+ fusion polypeptides and detected a polypeptide (approximately 190 kD and 2 x 10(4) copies/cell) in the S. pombe nuclear fraction. By immunofluorescence microscopy, anti-nuc1+ antibody revealed intense staining at a particular nuclear domain previously defined as the nucleolus. The nucleolar immunofluorescence by anti-nuc1+ was faded in nuc1-632 at restrictive temperature and dramatically diminished in the absence of DNA topoisomerases I and II. Thus active RNA polymerase I appears to be required for the formation of the nucleolus as its major component, and DNA topoisomerases appear to be required for the folding of rDNA and RNA polymerase I molecules into the functional organization of nucleolar genes.","authors":"Hirano T, Konoha G, Toda T, Yanagida M","authors_abbrev":"Hirano T et al.","pubmed_publication_date":"Feb 1989","pubmed_entrez_date":"1989-02-01","publication_year":"1989","canto_session_key":"dfcd11b5fda97a5f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-07-26 16:17:47","canto_approved_date":"2026-01-29 16:59:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-20 08:30:27","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4C3.05c","SPBC1703.14c","SPBC1A4.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-07-26"},{"uniquename":"PMID:26291501","title":"Mechanics and morphogenesis of fission yeast cells.","citation":"Curr Opin Microbiol 2015 Dec;28:36-45","abstract":"The integration of biochemical and biomechanical elements is at the heart of morphogenesis. While animal cells are relatively soft objects which shape and mechanics is mostly regulated by cytoskeletal networks, walled cells including those of plants, fungi and bacteria are encased in a rigid cell wall which resist high internal turgor pressure. How these particular mechanical properties may influence basic cellular processes, such as growth, shape and division remains poorly understood. Recent work using the model fungal cell fission yeast, Schizosaccharomyces pombe, highlights important contribution of cell mechanics to various morphogenesis processes. We envision this genetically tractable system to serve as a novel standard for the mechanobiology of walled cell.","doi":"10.1016/j.mib.2015.07.010","authors":"Davì V, Minc N","authors_abbrev":"Davì V et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-08-21","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-08-22 00:18:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1819509","title":"stf1: a new suppressor of the mitotic control gene, cdc25, in Schizosaccharomyces pombe.","citation":"Cold Spring Harb Symp Quant Biol 1991;56:599-604","abstract":"A novel element in the mitotic control, stf1, has been identified genetically by its ability to rescue cdc25-22 as well as a gene disruption of cdc25. This is the first phenotypically non-wee mutation shown to do so. stf1-1 functions additively with cdc2-1w, cdc2-3w, or wee1-6 to rescue cdc25. The available data are consistent with the wild-type gene product operating either on the same pathway as cdc25 or to stimulate cdc2 by a pathway independent of cdc25 or wee1. The stf1 gene has been cloned and sequenced and encodes a putative protein of 50-65 kD, depending on whether a potential intron is present. It is a novel protein with no homology detected in the current data bases. When challenged with hydroxyurea, stf1-1 acts additively with cdc2-3w in rescuing cdc25 mutants and in allowing mitosis to occur without DNA synthesis. It does not appear to play a role in the nutritional sensing pathway nor in the pathway mediating radiation-induced G2 delay.","authors":"Hudson JD, Feilotter H, Lingner C, Rowley R, Young PG","authors_abbrev":"Hudson JD et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_session_key":"7f57a6ddd92b9b94","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-11-03 10:14:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-03 10:14:07","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC649.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-03"},{"uniquename":"PMID:8211184","title":"U2AF homolog required for splicing in vivo.","citation":"Science 1993 Oct 22;262(5133):573-5","abstract":"Several fission yeast temperature-sensitive mutants defective in pre-mRNA processing (prp- mutants) at the nonpermissive temperature have been identified. Here, the prp2+ gene has been cloned by its ability to complement the temperature-sensitive growth defect of a prp2- mutant. The gene also corrects the pre-mRNA splicing defect of prp2- mutants and encodes a 59-kilodalton polypeptide (PRP2). A molecular characterization indicates that PRP2 is a previously uncharacterized yeast splicing factor with extensive similarity to the mammalian splicing factor U2AF65. Thus, this study provides evidence that a U2AF homolog participates in RNA processing in vivo.","authors":"Potashkin J, Naik K, Wentz-Hunter K","authors_abbrev":"Potashkin J et al.","pubmed_publication_date":"22 Oct 1993","pubmed_entrez_date":"1993-10-22","publication_year":"1993","canto_session_key":"26c650fccd11e213","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-06-27 14:28:15","canto_approved_date":"2021-11-04 13:50:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-27 14:28:10","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.07","SPBC26H8.07c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-06-27"},{"uniquename":"PMID:32059768","title":"Size-Dependent Increase in RNA Polymerase II Initiation Rates Mediates Gene Expression Scaling with Cell Size.","citation":"Curr Biol 2020 Apr 06;30(7):1217-1230.e7","abstract":"Cell size varies during the cell cycle and in response to external stimuli. This requires the tight coordination, or \"scaling,\" of mRNA and protein quantities with the cell volume in order to maintain biomolecule concentrations and cell density. Evidence in cell populations and single cells indicates that scaling relies on the coordination of mRNA transcription rates with cell size. Here, we use a combination of single-molecule fluorescence in situ hybridization (smFISH), time-lapse microscopy, and mathematical modeling in single fission yeast cells to uncover the precise molecular mechanisms that control transcription rates scaling with cell size. Linear scaling of mRNA quantities is apparent in single fission yeast cells during a normal cell cycle. Transcription of both constitutive and periodic genes is a Poisson process with transcription rates scaling with cell size and without evidence for transcriptional off states. Modeling and experimental data indicate that scaling relies on the coordination of RNA polymerase II (RNAPII) transcription initiation rates with cell size and that RNAPII is a limiting factor. We show using real-time quantitative imaging that size increase is accompanied by a rapid concentration-independent recruitment of RNAPII onto chromatin. Finally, we find that, in multinucleated cells, scaling is set at the level of single nuclei and not the entire cell, making the nucleus a determinant of scaling. Integrating our observations in a mechanistic model of RNAPII-mediated transcription, we propose that scaling of gene expression with cell size is the consequence of competition between genes for limiting RNAPII.","doi":"10.1016/j.cub.2020.01.053","authors":"Sun XM, Bowman A, Priestman M, Bertaux F, Martinez-Segura A, Tang W, Whilding C, Dormann D, Shahrezaei V, Marguerat S","authors_abbrev":"Sun XM et al.","pubmed_publication_date":"06 Apr 2020","pubmed_entrez_date":"2020-02-16","publication_year":"2020","canto_session_key":"934c9e88c393b2ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"XI-MING SUN","canto_first_approved_date":"2021-03-31 13:00:49","canto_approved_date":"2021-03-31 13:00:49","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-03-31 12:55:39","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"XI-MING SUN","community_curator":true,"annotation_count":30,"orcid":"0000-0002-5796-6020","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPYUG7.04c","SPBC28F2.12","SPBC20F10.08c","SPAC23G3.02c","SPCC1442.10c","SPAC25G10.09c","SPCC18B5.03","SPAC1002.19","SPBC146.13c","SPBC887.04c","SPAC23G3.01","SPAC24H6.05","SPAPYUG7.03c","SPAC2F7.03c","SPAC6G10.12c","SPAC16E8.01","SPBC4C3.12","SPCC1739.11c","SPBC16G5.15c","SPAC19G12.06c"],"gene_count":20,"ltp_gene_count":8,"approved_date":"2021-03-31"},{"uniquename":"PMID:28733416","title":"Genetic Interaction Screens in  Schizosaccharomyces pombe  Using the Pombe Epistasis Mapper (PEM) System and a Manual Colony Replicator.","citation":"Cold Spring Harb Protoc 2018 Feb 01;2018(2)","abstract":"In laboratories in which a colony-replicating robot is not available, manual replication provides a good, low-cost alternative for genetic interaction screening using the Pombe Epistasis Mapper (PEM) system. The protocol presented here describes the minimum number of steps required to identify genetic interactions. First, a query deletion is introduced to a library of deletion mutants by mating. Through a series of subsequent selection steps, single and double mutants are isolated and analyzed.","doi":"10.1101/pdb.prot091967","authors":"Colson I, Hartsuiker E","authors_abbrev":"Colson I et al.","pubmed_publication_date":"01 Feb 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16179942","title":"Mal3, the fission yeast EB1 homologue, cooperates with Bub1 spindle checkpoint to prevent monopolar attachment.","citation":"EMBO Rep 2005 Dec;6(12):1194-200","abstract":"Bipolar microtubule attachment is central to genome stability. Here, we investigate the mitotic role of the fission yeast EB1 homologue Mal3. Mal3 shows dynamic inward movement along the spindle, initial emergence at the spindle pole body (SPB) and translocation towards the equatorial plane, followed by sudden disappearance. Deletion of Mal3 results in early mitotic delay, which is dependent on the Bub1, but not the Mad2, spindle checkpoint. Consistently, Bub1, but not Mad2, shows prolonged kinetochore localization. Double mutants between mal3 and a subset of checkpoint mutants, including bub1, bub3, mad3 and mph1, but not mad1 or mad2, show massive chromosome mis-segregation defects. In mal3bub1 mutants, both sister centromeres tend to remain in close proximity to one of the separating SPBs. Further analysis indicates that mis-segregated centromeres are exclusively associated with the mother SPB. Mal3, therefore, has a role in preventing monopolar attachment in cooperation with the Bub1/Bub3/Mad3/Mph1-dependent checkpoint.","authors":"Asakawa K, Toya M, Sato M, Kanai M, Kume K, Goshima T, Garcia MA, Hirata D, Toda T","authors_abbrev":"Asakawa K et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-09-24","publication_year":"2005","canto_session_key":"83c3ce6ba08ef0ba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-22 15:30:35","canto_approved_date":"2024-04-24 16:19:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-31 07:15:35","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H3.08c","SPBC106.01","SPCC1322.12c","SPBC20F10.06","SPCC1795.01c","SPAC18G6.15"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-09-22"},{"uniquename":"PMID:10648612","title":"The Rpb6 subunit of fission yeast RNA polymerase II is a contact target of the transcription elongation factor TFIIS.","citation":"Mol Cell Biol 2000 Feb;20(4):1263-70","abstract":"The Rpb6 subunit of RNA polymerase II is one of the five subunits common to three forms of eukaryotic RNA polymerase. Deletion and truncation analyses of the rpb6 gene in the fission yeast Schizosaccharomyces pombe indicated that Rpb6, consisting of 142 amino acid residues, is an essential protein for cell viability, and the essential region is located in the C-terminal half between residues 61 and 139. After random mutagenesis, a total of 14 temperature-sensitive mutants were isolated, each carrying a single (or double in three cases and triple in one) mutation. Four mutants each carrying a single mutation in the essential region were sensitive to 6-azauracil (6AU), which inhibits transcription elongation by depleting the intracellular pool of GTP and UTP. Both 6AU sensitivity and temperature-sensitive phenotypes of these rpb6 mutants were suppressed by overexpression of TFIIS, a transcription elongation factor. In agreement with the genetic studies, the mutant RNA polymerases containing the mutant Rpb6 subunits showed reduced affinity for TFIIS, as measured by a pull-down assay of TFIIS-RNA polymerase II complexes using a fusion form of TFIIS with glutathione S-transferase. Moreover, the direct interaction between TFIIS and RNA polymerase II was competed by the addition of Rpb6. Taken together, the results lead us to propose that Rpb6 plays a role in the interaction between RNA polymerase II and the transcription elongation factor TFIIS.","authors":"Ishiguro A, Nogi Y, Hisatake K, Muramatsu M, Ishihama A","authors_abbrev":"Ishiguro A et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-01-29","publication_year":"2000","canto_session_key":"ea0f1b494668093f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-04-14 09:10:47","canto_approved_date":"2023-05-16 07:54:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-04-13 16:15:25","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20H4.03c","SPCC1020.04c","SPBC18H10.11c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2022-04-14"},{"uniquename":"PMID:19606215","title":"Calnexin regulates apoptosis induced by inositol starvation in fission yeast.","citation":"PLoS One 2009 Jul 16;4(7):e6244","abstract":"Inositol is a precursor of numerous phospholipids and signalling molecules essential for the cell. Schizosaccharomyces pombe is naturally auxotroph for inositol as its genome does not have a homologue of the INO1 gene encoding inositol-1-phosphate synthase, the enzyme responsible for inositol biosynthesis. In this work, we demonstrate that inositol starvation in S. pombe causes cell death with apoptotic features. This apoptotic death is dependent on the metacaspase Pca1p and is affected by the UPR transducer Ire1p. Previously, we demonstrated that calnexin is involved in apoptosis induced by ER stress. Here, we show that cells expressing a lumenal version of calnexin exhibit a 2-fold increase in the levels of apoptosis provoked by inositol starvation. This increase is reversed by co-expression of a calnexin mutant spanning the transmembrane domain and C-terminal cytosolic tail. Coherently, calnexin is physiologically cleaved at the end of its lumenal domain, under normal growth conditions when cells approach stationary phase. This cleavage suggests that the two naturally produced calnexin fragments are needed to continue growth into stationary phase and to prevent cell death. Collectively, our observations indicate that calnexin takes part in at least two apoptotic pathways in S. pombe, and suggest that the cleavage of calnexin has regulatory roles in apoptotic processes involving calnexin.","doi":"10.1371/journal.pone.0006244","authors":"Guérin R, Beauregard PB, Leroux A, Rokeach LA","authors_abbrev":"Guérin R et al.","pubmed_publication_date":"16 Jul 2009","pubmed_entrez_date":"2009-07-17","publication_year":"2009","canto_session_key":"ed1e6e11b1c4abfa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-18 16:17:25","canto_approved_date":"2024-03-28 17:21:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-03-14 11:27:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.04","SPAC3C7.11c","SPAC167.01"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-02-18"},{"uniquename":"PMID:24424027","title":"Torin1-mediated TOR kinase inhibition reduces Wee1 levels and advances mitotic commitment in fission yeast and HeLa cells.","citation":"J Cell Sci 2014 Mar 15;127(Pt 6):1346-56","abstract":"The target of rapamycin (TOR) kinase regulates cell growth and division. Rapamycin only inhibits a subset of TOR activities. Here we show that in contrast to the mild impact of rapamycin on cell division, blocking the catalytic site of TOR with the Torin1 inhibitor completely arrests growth without cell death in Schizosaccharomyces pombe. A mutation of the Tor2 glycine residue (G2040D) that lies adjacent to the key Torin-interacting tryptophan provides Torin1 resistance, confirming the specificity of Torin1 for TOR. Using this mutation, we show that Torin1 advanced mitotic onset before inducing growth arrest. In contrast to TOR inhibition with rapamycin, regulation by either Wee1 or Cdc25 was sufficient for this Torin1-induced advanced mitosis. Torin1 promoted a Polo and Cdr2 kinase-controlled drop in Wee1 levels. Experiments in human cell lines recapitulated these yeast observations: mammalian TOR (mTOR) was inhibited by Torin1, Wee1 levels declined and mitotic commitment was advanced in HeLa cells. Thus, the regulation of the mitotic inhibitor Wee1 by TOR signalling is a conserved mechanism that helps to couple cell cycle and growth controls.","doi":"10.1242/jcs.146373","authors":"Atkin J, Halova L, Ferguson J, Hitchin JR, Lichawska-Cieslar A, Jordan AM, Pines J, Wellbrock C, Petersen J","authors_abbrev":"Atkin J et al.","pubmed_publication_date":"15 Mar 2014","pubmed_entrez_date":"2014-01-16","publication_year":"2014","canto_session_key":"4c442ec29a4ab68a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC23C11.16","SPAC57A10.02"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:19910488","title":"Centromeric localization of dispersed Pol III genes in fission yeast.","citation":"Mol Biol Cell 2010 Jan 15;21(2):254-65","abstract":"The eukaryotic genome is a complex three-dimensional entity residing in the nucleus. We present evidence that Pol III-transcribed genes such as tRNA and 5S rRNA genes can localize to centromeres and contribute to a global genome organization. Furthermore, we find that ectopic insertion of Pol III genes into a non-Pol III gene locus results in the centromeric localization of the locus. We show that the centromeric localization of Pol III genes is mediated by condensin, which interacts with the Pol III transcription machinery, and that transcription levels of the Pol III genes are negatively correlated with the centromeric localization of Pol III genes. This centromeric localization of Pol III genes initially observed in interphase becomes prominent during mitosis, when chromosomes are condensed. Remarkably, defective mitotic chromosome condensation by a condensin mutation, cut3-477, which reduces the centromeric localization of Pol III genes, is suppressed by a mutation in the sfc3 gene encoding the Pol III transcription factor TFIIIC subunit, sfc3-1. The sfc3-1 mutation promotes the centromeric localization of Pol III genes. Our study suggests there are functional links between the process of the centromeric localization of dispersed Pol III genes, their transcription, and the assembly of condensed mitotic chromosomes.","authors":"Iwasaki O, Tanaka A, Tanizawa H, Grewal SI, Noma K","authors_abbrev":"Iwasaki O et al.","pubmed_publication_date":"15 Jan 2010","pubmed_entrez_date":"2009-11-14","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC146.03c","SPBC336.07","SPBC13E7.10c","SPBC2G5.07c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:15809028","title":"Microtubule tips redirect actin assembly.","citation":"Dev Cell 2005 Apr;8(4):458-9","abstract":"In fission yeast, a protein complex that rides on the plus end of growing microtubules regulates establishment of new sites of actin cable assembly, necessary for cell growth, from one to both ends of the rod-shaped cells. Martin et al. describe a direct molecular link between the microtubule tip complex and the formin for3p, the nucleator for assembly of actin cables, which is necessary for this regulatory switch.","authors":"Bretscher A","authors_abbrev":"Bretscher A","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-04-06","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9763441","title":"The role of topoisomerase II in meiotic chromosome condensation and segregation in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1998 Oct;9(10):2739-50","abstract":"Topoisomerase II is able to break and rejoin double-strand DNA. It controls the topological state and forms and resolves knots and catenanes. Not much is known about the relation between the chromosome segregation and condensation defects as found in yeast top2 mutants and the role of topoisomerase II in meiosis. We studied meiosis in a heat-sensitive top2 mutant of Schizosaccharomyces pombe. Topoisomerase II is not required until shortly before meiosis I. The enzyme is necessary for condensation shortly before the first meiotic division but not for early meiotic prophase condensation. DNA replication, prophase morphology, and dynamics of the linear elements are normal in the top2 mutant. The top2 cells are not able to perform meiosis I. Arrested cells have four spindle pole bodies and two spindles but only one nucleus, suggesting that the arrest is nonregulatory. Finally, we show that the arrest is partly solved in a top2 rec7 double mutant, indicating that topoisomerase II functions in the segregation of recombined chromosomes. We suggest that the inability to decatenate the replicated DNA is the primary defect in top2. This leads to a loss of chromatin condensation shortly before meiosis I, failure of sister chromatid separation, and a nonregulatory arrest.","authors":"Hartsuiker E, Bähler J, Kohli J","authors_abbrev":"Hartsuiker E et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-10-08","publication_year":"1998","canto_session_key":"47b71fe7814ad693","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-11 15:40:39","canto_approved_date":"2026-01-29 16:38:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-11 15:40:32","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1753.03c","SPBC1A4.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-05-11"},{"uniquename":"PMID:27692365","title":"Contributions of Microtubule Dynamic Instability and Rotational Diffusion to Kinetochore Capture.","citation":"Biophys J 2017 Feb 07;112(3):552-563","abstract":"Microtubule dynamic instability allows search and capture of kinetochores during spindle formation, an important process for accurate chromosome segregation during cell division. Recent work has found that microtubule rotational diffusion about minus-end attachment points contributes to kinetochore capture in fission yeast, but the relative contributions of dynamic instability and rotational diffusion are not well understood. We have developed a biophysical model of kinetochore capture in small fission-yeast nuclei using hybrid Brownian dynamics/kinetic Monte Carlo simulation techniques. With this model, we have studied the importance of dynamic instability and microtubule rotational diffusion for kinetochore capture, both to the lateral surface of a microtubule and at or near its end. Over a range of biologically relevant parameters, microtubule rotational diffusion decreased capture time, but made a relatively small contribution compared to dynamic instability. At most, rotational diffusion reduced capture time by 25%. Our results suggest that while microtubule rotational diffusion can speed up kinetochore capture, it is unlikely to be the dominant physical mechanism for typical conditions in fission yeast. In addition, we found that when microtubules undergo dynamic instability, lateral captures predominate even in the absence of rotational diffusion. Counterintuitively, adding rotational diffusion to a dynamic microtubule increases the probability of end-on capture.","doi":"10.1016/j.bpj.2016.09.006","authors":"Blackwell R, Sweezy-Schindler O, Edelmaier C, Gergely ZR, Flynn PJ, Montes S, Crapo A, Doostan A, McIntosh JR, Glaser MA, Betterton MD","authors_abbrev":"Blackwell R et al.","pubmed_publication_date":"07 Feb 2017","pubmed_entrez_date":"2016-10-04","publication_year":"2017","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2016-10-07 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19666000","title":"Casein kinase II is required for the spindle assembly checkpoint by regulating Mad2p in fission yeast.","citation":"Biochem Biophys Res Commun 2009 Oct 23;388(3):529-32","abstract":"The spindle checkpoint is a surveillance mechanism that ensures the fidelity of chromosome segregation in mitosis. Here we show that fission yeast casein kinase II (CK2) is required for this checkpoint function. In the CK2 mutants mitosis occurs in the presence of a spindle defect, and the spindle checkpoint protein Mad2p fails to localize to unattached kinetochores. The CK2 mutants are sensitive to the microtubule depolymerising drug thiabendazole, which is counteracted by ectopic expression of mad2+. The level of Mad2p is low in the CK2 mutants. These results suggest that CK2 has a role in the spindle checkpoint by regulating Mad2p.","doi":"10.1016/j.bbrc.2009.08.030","authors":"Shimada M, Yamamoto A, Murakami-Tonami Y, Nakanishi M, Yoshida T, Aiba H, Murakami H","authors_abbrev":"Shimada M et al.","pubmed_publication_date":"23 Oct 2009","pubmed_entrez_date":"2009-08-12","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18550796","title":"Live observation of forespore membrane formation in fission yeast.","citation":"Mol Biol Cell 2008 Aug;19(8):3544-53","abstract":"Sporulation in the fission yeast Schizosaccharomyces pombe is a unique biological process in that the plasma membrane of daughter cells is assembled de novo within the mother cell cytoplasm. A double unit membrane called the forespore membrane (FSM) is constructed dynamically during meiosis. To obtain a dynamic view of FSM formation, we visualized FSM in living cells by using green fluorescent protein fused with Psy1, an FSM-resident protein, together with the nucleus or microtubules. The assembly of FSM initiates in prophase II, and four FSMs in a cell expand in a synchronous manner at the same rate throughout meiosis II. After the meiosis II completes, FSMs continue to expand until closure to form the prespore, a spore precursor. Prespores are initially ellipsoidal, and eventually become spheres. FSM formation was also observed in the sporulation-deficient mutants spo3, spo14, and spo15. In the spo15 mutant, the initiation of FSM formation was completely blocked. In the spo3 mutant, the FSM expanded normally during early meiosis II, but it was severely inhibited during late and postmeiosis, whereas in the spo14 mutant, membrane expansion was more severely inhibited throughout meiosis II. These observations suggest that FSM expansion is composed of two steps, early meiotic FSM expansion and late and post meiotic FSM expansion. Possible regulatory mechanisms of FSM formation in fission yeast are discussed.","authors":"Nakamura T, Asakawa H, Nakase Y, Kashiwazaki J, Hiraoka Y, Shimoda C","authors_abbrev":"Nakamura T et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-06-14","publication_year":"2008","canto_session_key":"33226bef0daaac44","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-18 03:26:23","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-18 03:26:11","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC607.10","SPBC800.05c","SPBC3H7.01","SPAC1F3.06c","SPCC825.03c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2015-12-18"},{"uniquename":"PMID:32628831","title":"Proteomics Using Protease Alternatives to Trypsin Benefits from Sequential Digestion with Trypsin.","citation":"Anal Chem 2020 Jul 21;92(14):9523-9527","abstract":"Trypsin is the most used enzyme in proteomics. Nevertheless, proteases with complementary cleavage specificity have been applied in special circumstances. In this work, we analyzed the characteristics of five protease alternatives to trypsin for protein identification and sequence coverage when applied to  S. pombe  whole cell lysates. The specificity of the protease heavily impacted the number of proteins identified. Proteases with higher specificity led to the identification of more proteins than proteases with lower specificity. However, AspN, GluC, chymotrypsin, and proteinase K largely benefited from being paired with trypsin in sequential digestion, as had been shown by us for elastase before. In the most extreme case, predigesting with trypsin improves the number of identified proteins for proteinase K by 731%. Trypsin predigestion also improved the protein identifications of other proteases, AspN (+62%), GluC (+80%), and chymotrypsin (+21%). Interestingly, the sequential digest with trypsin and AspN yielded even a higher number of protein identifications than digesting with trypsin alone.","doi":"10.1021/acs.analchem.0c00478","authors":"Dau T, Bartolomucci G, Rappsilber J","authors_abbrev":"Dau T et al.","pubmed_publication_date":"21 Jul 2020","pubmed_entrez_date":"2020-07-07","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-07-08 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15294892","title":"Enforcement of late replication origin firing by clusters of short G-rich DNA sequences.","citation":"J Biol Chem 2004 Oct 01;279(40):42337-44","abstract":"Previous studies in budding yeast suggested that the default firing time of most DNA replication origins is early in S phase and that origins can be forced to fire later by proximity to certain cis-acting sequences. However, these cis-acting sequences were not well defined. We have attempted to characterize cis-acting sequences that affect replication timing in the fission yeast. We identified a stretch of 200 bp that was sufficient to compel nearby origins to fire late. The 200-bp stretch was able to force an origin to fire late whether adjacent to the origin or approximately 800 bp away in opposite orientation. The stretch contains a cluster of three close matches to a G-rich, 10-bp late consensus sequence (LCS). The three LCS elements cooperate with each other and with other sequences within the 200-bp stretch to enforce late replication. Although only a few origins that fire in very late S phase have been identified in fission yeast, all of them are located close to a cluster of LCS elements.","authors":"Yompakdee C, Huberman JA","authors_abbrev":"Yompakdee C et al.","pubmed_publication_date":"01 Oct 2004","pubmed_entrez_date":"2004-08-06","publication_year":"2004","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23966866","title":"Mediator directs co-transcriptional heterochromatin assembly by RNA interference-dependent and -independent pathways.","citation":"PLoS Genet 2013;9(8):e1003677","abstract":"Heterochromatin at the pericentromeric repeats in fission yeast is assembled and spread by an RNAi-dependent mechanism, which is coupled with the transcription of non-coding RNA from the repeats by RNA polymerase II. In addition, Rrp6, a component of the nuclear exosome, also contributes to heterochromatin assembly and is coupled with non-coding RNA transcription. The multi-subunit complex Mediator, which directs initiation of RNA polymerase II-dependent transcription, has recently been suggested to function after initiation in processes such as elongation of transcription and splicing. However, the role of Mediator in the regulation of chromatin structure is not well understood. We investigated the role of Mediator in pericentromeric heterochromatin formation and found that deletion of specific subunits of the head domain of Mediator compromised heterochromatin structure. The Mediator head domain was required for Rrp6-dependent heterochromatin nucleation at the pericentromere and for RNAi-dependent spreading of heterochromatin into the neighboring region. In the latter process, Mediator appeared to contribute to efficient processing of siRNA from transcribed non-coding RNA, which was required for efficient spreading of heterochromatin. Furthermore, the head domain directed efficient transcription in heterochromatin. These results reveal a pivotal role for Mediator in multiple steps of transcription-coupled formation of pericentromeric heterochromatin. This observation further extends the role of Mediator to co-transcriptional chromatin regulation.","doi":"10.1371/journal.pgen.1003677","authors":"Oya E, Kato H, Chikashige Y, Tsutsumi C, Hiraoka Y, Murakami Y","authors_abbrev":"Oya E et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-08-23","publication_year":"2013","canto_session_key":"f272d815230dcb0f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.13c","SPAC5D6.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:22580457","title":"Pat(ting) boosts meiosis.","citation":"Cell Cycle 2012 May 15;11(10):1876-7","abstract":"","doi":"10.4161/cc.20513","authors":"Tachibana-Konwalski K","authors_abbrev":"Tachibana-Konwalski K","pubmed_publication_date":"15 May 2012","pubmed_entrez_date":"2012-05-15","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22912768","title":"Rhn1, a nuclear protein, is required for suppression of meiotic mRNAs in mitotically dividing fission yeast.","citation":"PLoS One 2012;7(8):e42962","abstract":"In the fission yeast Schizosaccharomyces pombe, many meiotic mRNAs are transcribed during mitosis and meiosis and selectively eliminated in mitotic cells. However, this pathway for mRNA decay, called the determinant of selective removal (DSR)-Mmi1 system, targets only some of the numerous meiotic mRNAs that are transcribed in mitotic cells. Here we describe Rhn1, a nuclear protein involved in meiotic mRNA suppression in vegetative fission yeast. Rhn1 is homologous to budding yeast Rtt103 and localizes to one or a few discrete nuclear dots in growing vegetative cells. Rhn1 colocalizes with a pre-mRNA 3'-end processing factor, Pcf11, and with the 5'-3' exoribonuclease, Dhp1; moreover, Rhn1 coimmunoprecipitates with Pcf11. Loss of rhn1 results in elevated sensitivity to high temperature, to thiabendazole (TBZ), and to UV. Interestingly, meiotic mRNAs--including moa1(+), mcp5(+), and mug96(+)--accumulate in mitotic rhn1Δ cells. Accumulation of meiotic mRNAs also occurs in strains lacking Lsk1, a kinase that phosphorylates serine 2 (Ser-2) in the C-terminal domain (CTD) of RNA polymerase II (Pol II), and in strains lacking Sen1, an ATP-dependent 5'-3' RNA/DNA helicase: notably, both Lsk1 and Sen1 have been implicated in termination of Pol II-dependent transcription. Furthermore, RNAi knockdown of cids-2, a Caenorhabditis elegans ortholog of rhn1(+), leads to elevated expression of a germline-specific gene, pgl-1, in somatic cells. These results indicate that Rhn1 contributes to the suppression of meiotic mRNAs in vegetative fission yeast and that the mechanism by which Rhn1 downregulates germline-specific transcripts may be conserved in unicellular and multicellular organisms.","doi":"10.1371/journal.pone.0042962","authors":"Sugiyama T, Sugioka-Sugiyama R, Hada K, Niwa R","authors_abbrev":"Sugiyama T et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-23","publication_year":"2012","canto_session_key":"7da99c40d10d0680","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-03-23 16:10:30","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-03-19 15:48:57","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.01","SPBC1271.06c","SPAC19G12.06c","SPAC26A3.12c","SPAC6G9.10c","SPBPB10D8.02c","SPBC31F10.05","SPAC212.08c","SPBC29A10.02","SPBC337.03","SPBC32H8.11","SPBPB10D8.01","SPBPB2B2.06c","SPAC750.07c","SPAC1006.03c","SPAC19D5.06c","SPAC4G9.04c","SPBC32C12.02","SPBC1289.14","SPAC2F3.15","SPBC29A10.14","SPAC27D7.13c"],"gene_count":22,"ltp_gene_count":7,"approved_date":"2013-03-19"},{"uniquename":"PMID:138078","title":"A cytoplasmic gene for partial suppression of a nuclear pleiotropic respiratory deficient mutant in the petite negative yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1976 Nov 24;149(1):101-9","abstract":"The nuclear pleiotropic respiratory-deficient mutant pet1 (previously M126) exhibits cytochromes aa3 and b deficiencies accompanied by loss of the oligomycin-sensitivity of the mitochondrial ATPase. The mutant pet1, unable to grow on glycerol, growth on glucose. The latter phenotypic trait symbolized by ANAS-D, exhibits a high frequency (2 to 4 X 10(5)) Of spontaneous suppression into Antimycin A-resistant strains. Mutagenesis with MnCl2 increases by a factor of 10(2) the frequency of ANAR-D derivatives. This suppression is partial since none of the suppressed strains is able to grow on glycerol even when respiratory functions and cytochromes activities are restored as in the pet1 [SUP2] strain. In the latter strain it is concluded that the extralocus suppressor gene [SUP2] is responsible for the ANAR-D trait. Tetrad analysis in a cross homozygous for pet1 demonstrates a non-Mendelian segregation pattern for the SUP2 suppressor gene. In stable diploids, homozygous for pet1, the [SUP2] suppressor exhibits a mitotic segregation pattern. Furthermore the transmission of the [SUP2] gene is decreased by ethidium bromide treatment. Therefore, the [SUP2] suppressor gene responsible for partial suppression of the nuclear pleiotropic phenotype in mutant pet1 is of cytoplasmic heredity.","authors":"Colson AM, Labaille F, Goffeau A","authors_abbrev":"Colson AM et al.","pubmed_publication_date":"24 Nov 1976","pubmed_entrez_date":"1976-11-24","publication_year":"1976","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34613787","title":"Counting actin in contractile rings reveals novel contributions of cofilin and type II myosins to fission yeast cytokinesis.","citation":"Mol Biol Cell 2022 May 15;33(6):ar51","abstract":"Cytokinesis by animals, fungi, and amoebas depends on actomyosin contractile rings, which are stabilized by continuous turnover of actin filaments. Remarkably little is known about the amount of polymerized actin in contractile rings, so we used low concentrations of GFP-Lifeact to count total polymerized actin molecules in the contractile rings of live fission yeast cells. Contractile rings of wild-type cells accumulated polymerized actin molecules at 4900/min to a peak number of ∼198,000 followed by a loss of actin at 5400/min throughout ring constriction. In  adf1-M3  mutant cells with cofilin that severs actin filaments poorly, contractile rings accumulated polymerized actin at twice the normal rate and eventually had almost twofold more actin along with a proportional increase in type II myosins Myo2, Myp2, and formin Cdc12. Although 30% of  adf1-M3  mutant cells failed to constrict their rings fully, the rest lost actin from the rings at the wild-type rates. Mutations of type II myosins Myo2 and Myp2 reduced contractile ring actin filaments by half and slowed the rate of actin loss from the rings.","doi":"10.1091/mbc.E21-08-0376","authors":"Malla M, Pollard TD, Chen Q","authors_abbrev":"Malla M et al.","pubmed_publication_date":"15 May 2022","pubmed_entrez_date":"2021-10-06","publication_year":"2022","canto_session_key":"8bbc6f872ab18094","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Qian Chen","canto_first_approved_date":"2021-12-13 11:45:21","canto_approved_date":"2024-01-19 15:11:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-11-30 22:00:35","canto_added_date":"2021-10-08 00:15:04","annotation_curators":[{"name":"Qian Chen","community_curator":true,"annotation_count":4,"orcid":"0000-0002-2768-6570","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.06c","SPBC32H8.12c","SPAC4A8.05c","SPAC1F5.04c","SPCC895.05","SPCC645.05c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2021-12-13"},{"uniquename":"PMID:6763550","title":"Differential survival as an indicator of potential mutagenicity using repair deficient strains of Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Can J Genet Cytol 1982;24(6):771-5","abstract":"A method is presented to screen chemicals for potential mutagenicity on the basis of their ability to cause more killing in cells of repair-deficient yeast than in wild type cells. Two species were chosen in the event that one might be more sensitive to certain chemicals. The strains used were RAD+ and rad6 derivatives of Saccharomyces cerevisiae and RAD+ and rad3 derivatives of Schizosaccharomyces pombe. This report describes the test system and results for 12 known, direct-acting mutagens (i.e., not requiring mammalian metabolic activation). These compounds showed more lethality in one or both of the repair-deficient strains, indicating that they induce damage to DNA which is subject to repair in wild type cells. Advantages of this system include the use of eukaryotic yeast cells which can be manipulated as easily as bacteria, and that exogenous enzymes (S9) can be added for metabolic activation. Growing yeast cells can activate certain promutagens, and preliminary experiments showed positive responses for diethylnitrosamine and 2-acetylaminofluorene without the addition of S9.","authors":"Nestmann ER, Stephen ER, Kowbel DJ, Nasim A","authors_abbrev":"Nestmann ER et al.","pubmed_publication_date":"1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23438742","title":"Rheostat-ing mitosis.","citation":"Chem Biol 2013 Feb 21;20(2):142-3","abstract":"Ark1, the unique Aurora kinase in Schizosaccharomyces pombe, regulates multiple aspects of mitosis. In this issue of Chemistry & Biology, Kawashima and colleagues report the discovery and validation of a fungal Ark1 inhibitor, which they employ to evaluate the mitotic outputs of endogenous Ark1 signaling.","doi":"10.1016/j.chembiol.2013.02.001","authors":"Eyers PA","authors_abbrev":"Eyers PA","pubmed_publication_date":"21 Feb 2013","pubmed_entrez_date":"2013-02-27","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23005832","title":"Binary threshold networks as a natural null model for biological networks.","citation":"Phys Rev E Stat Nonlin Soft Matter Phys 2012 Aug;86(2 Pt 2):026114","abstract":"Spin models of neural networks and genetic networks are considered elegant as they are accessible to statistical mechanics tools for spin glasses and magnetic systems. However, the conventional choice of variables in spin systems may cause problems in some models when parameter choices are unrealistic from a biological perspective. Obviously, this may limit the role of a model as a template model for biological systems. Perhaps less obviously, also ensembles of random networks are affected and may exhibit different critical properties. We consider here a prototypical network model that is biologically plausible in its local mechanisms. We study a discrete dynamical network with two characteristic properties: Nodes with binary states 0 and 1, and a modified threshold function with Θ(0)(0)=0. We explore the critical properties of random networks of such nodes and find a critical connectivity K(c)=2.0 with activity vanishing at the critical point. Finally, we observe that the present model allows a more natural implementation of recent models of budding yeast and fission yeast cell-cycle control networks.","authors":"Rybarsch M, Bornholdt S","authors_abbrev":"Rybarsch M et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-09-26","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD253","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8895665","title":"The ORC1 homolog orp1 in fission yeast plays a key role in regulating onset of S phase.","citation":"Genes Dev 1996 Oct 15;10(20):2644-54","abstract":"In a screen for new cell-cycle genes in Schizosaccharomyces pombe we have isolated cdc30, which is identical to orp1, a putative homolog of the Saccharomyces cerevisiae ORC1 gene. Analysis of the temperature-sensitive orp1-4 and the orp1(delta) mutants indicates that orp1 is required at the onset of S phase for an early step of DNA replication. Orp1p is found in the nucleus and is present at a constant level throughout the cell cycle. Genetic interactions occur between orp1 and cdc18 and cdc21 (an MCM homolog). Orp1p forms protein complexes with both cdc18p and cdc21p in vivo, suggesting that interactions between these proteins and ORC are important for controlling the initiation of DNA replication at the onset of S phase. The orp1 gene is also required for the control that prevents entry into mitosis in the absence of DNA replication, suggesting a role for ORC in this checkpoint pathway.","authors":"Grallert B, Nurse P","authors_abbrev":"Grallert B et al.","pubmed_publication_date":"15 Oct 1996","pubmed_entrez_date":"1996-10-15","publication_year":"1996","canto_session_key":"fbf3d843a4ea7343","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-06-08 15:53:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-10-16 14:00:42","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPBC29A10.15","SPBC14C8.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-10-16"},{"uniquename":"PMID:23607342","title":"Monoclonal antibodies recognize gly-leu-phe-gly repeat of nucleoporin nup98 of tetrahymena, yeasts, and humans.","citation":"Monoclon Antib Immunodiagn Immunother 2013 Apr;32(2):81-90","abstract":"Nucleoporin Nup98, an essential component of the nuclear pore complex, has multifunctional roles in nuclear functions including transcriptional regulation and nucleocytoplasmic transport. These functions mostly depend on a Gly-Leu-Phe-Gly (GLFG) sequence appearing repetitively in the N-terminal region of Nup98. As the GLFG sequence is well conserved among Nup98s from a wide variety of species including humans, yeasts, and ciliates such as Tetrahymena thermophila, a specific antibody that recognizes the GLFG sequence is expected to detect various Nup98s from a wide-range of species. To generate monoclonal antibodies specific to the GLFG repeat of Nup98, we used two synthetic polypeptides derived from the macronuclear Nup98 of T. thermophila as an antigen. We obtained two monoclonal antibodies (MAbs), 13C2 and 21A10, that recognize Nup98s in indirect immunofluorescence staining and Western blot analysis of T. thermophila. Peptide array analysis of these monoclonal antibodies located the position of their epitopes at or near GLFG residues: the epitope recognized by the 13C2 MAb is FGxxN (x being any amino acid), and the epitope recognized by the 21A10 MAb is GLF. As expected by their epitopes, these monoclonal antibodies also recognize Nup98 homologs expressed by human cells and the yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae, indicating that 13C2 and 21A10 MAbs recognize Nup98 epitopes common to phylogenetically distinct organisms. Thus, these MAbs are useful in studying a wide variety of biological phenomena that involve Nup98, ranging from ciliate nuclear dimorphism to NUP98-related human leukemia.","doi":"10.1089/mab.2012.0118","authors":"Iwamoto M, Asakawa H, Ohtsuki C, Osakada H, Koujin T, Hiraoka Y, Haraguchi T","authors_abbrev":"Iwamoto M et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2013-04-24","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23143934","title":"Does copper stress lead to spindle misposition-dependent cell cycle arrest?","citation":"Genet Mol Res 2012 Oct 25;11(4):3824-34","abstract":"Because of its specific electrochemical properties, copper is an essential heavy metal for living organisms. As with other heavy metals, high levels can provoke damage. We examined gene expression under copper stress in wild-type fission yeast (Schizosaccharomyces pombe) through differential display. After the EC(50) concentration of CuSO(4) was determined as 50 μM, total RNA was isolated from cells treated or not with copper. The expression level of SPCC1682.13, ppk1, SPBC2F12.05c, and adg2 genes increased significantly under copper stress. Considering the functions of these genes are related to the cell cycle, cell division and chromosome dynamics, we hypothesize that retardation of the cell cycle under copper stress is relevant to the events that depend on the functions of these genes.","doi":"10.4238/2012.October.25.1","authors":"Tarhan C, Sarikaya AT","authors_abbrev":"Tarhan C et al.","pubmed_publication_date":"25 Oct 2012","pubmed_entrez_date":"2012-11-13","publication_year":"2012","canto_session_key":"4f0ce622af2df7cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-01 12:20:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-09 07:51:56","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2F12.05c","SPCC1682.13","SPAC110.01","SPAC19G12.16c"],"gene_count":4,"ltp_gene_count":0,"approved_date":"2014-03-09"},{"uniquename":"PMID:28193728","title":"Mobile Introns Shape the Genetic Diversity of Their Host Genes.","citation":"Genetics 2017 Apr;205(4):1641-1648","abstract":"Self-splicing introns populate several highly conserved protein-coding genes in fungal and plant mitochondria. In fungi, many of these introns have retained their ability to spread to intron-free target sites, often assisted by intron-encoded endonucleases that initiate the homing process. Here, leveraging population genomic data from  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe , and  Lachancea kluyveri , we expose nonrandom patterns of genetic diversity in exons that border self-splicing introns. In particular, we show that, in all three species, the density of single nucleotide polymorphisms increases as one approaches a mobile intron. Through multiple lines of evidence, we rule out relaxed purifying selection as the cause of uneven nucleotide diversity. Instead, our findings implicate intron mobility as a direct driver of host gene diversity. We discuss two mechanistic scenarios that are consistent with the data: either endonuclease activity and subsequent error-prone repair have left a mutational footprint on the insertion environment of mobile introns or nonrandom patterns of genetic diversity are caused by exonic coconversion, which occurs when introns spread to empty target sites via homologous recombination. Importantly, however, we show that exonic coconversion can only explain diversity gradients near intron-exon boundaries if the conversion template comes from outside the population. In other words, there must be pervasive and ongoing horizontal gene transfer of self-splicing introns into extant fungal populations.","doi":"10.1534/genetics.116.199059","authors":"Repar J, Warnecke T","authors_abbrev":"Repar J et al.","pubmed_publication_date":"Apr 2017","pubmed_entrez_date":"2017-02-15","publication_year":"2017","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2017-02-16 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38287013","title":"A universal metabolite repair enzyme removes a strong inhibitor of the TCA cycle.","citation":"Nat Commun 2024 Jan 29;15(1):846","abstract":"A prevalent side-reaction of succinate dehydrogenase oxidizes malate to enol-oxaloacetate (OAA), a metabolically inactive form of OAA that is a strong inhibitor of succinate dehydrogenase. We purified from cow heart mitochondria an enzyme (OAT1) with OAA tautomerase (OAT) activity that converts enol-OAA to the physiological keto-OAA form, and determined that it belongs to the highly conserved and previously uncharacterized Fumarylacetoacetate_hydrolase_domain-containing protein family. From all three domains of life, heterologously expressed proteins were shown to have strong OAT activity, and ablating the OAT1 homolog caused significant growth defects. In Escherichia coli, expression of succinate dehydrogenase was necessary for OAT1-associated growth defects to occur, and ablating OAT1 caused a significant increase in acetate and other metabolites associated with anaerobic respiration. OAT1 increased the succinate dehydrogenase reaction rate by 35% in in vitro assays with physiological concentrations of both succinate and malate. Our results suggest that OAT1 is a universal metabolite repair enzyme that is required to maximize aerobic respiration efficiency by preventing succinate dehydrogenase inhibition.","doi":"10.1038/s41467-024-45134-0","authors":"Zmuda AJ, Kang X, Wissbroecker KB, Freund Saxhaug K, Costa KC, Hegeman AD, Niehaus TD","authors_abbrev":"Zmuda AJ et al.","pubmed_publication_date":"29 Jan 2024","pubmed_entrez_date":"2024-01-29","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21C3.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32374858","title":"CRISPR-Cas12a system in fission yeast for multiplex genomic editing and CRISPR interference.","citation":"Nucleic Acids Res 2020 Jun 04;48(10):5788-5798","abstract":"The CRISPR-Cas12a is a class II, type V clustered regularly interspaced short palindromic repeat (CRISPR) system with both RNase and DNase activity. Compared to the CRISPR-Cas9 system, it recognizes T-rich PAM sequences and has the advantage of multiplex genomic editing. Here, in fission yeast Schizosaccharomyces pombe, we successfully implemented the CRISPR-Cas12a system for versatile genomic editing and manipulation. In addition to the rrk1 promoter, we used new pol II promoters from endogenous coding genes to express crRNA for Cas12a and obtained a much higher editing efficiency. This new design expands the promoter choices for potential applications in fission yeast and other organisms. In addition, we expressed a gRNA array using a strong constitutive pol II promoter. The array transcript is processed by Cas12a itself to release multiple mature crRNAs. With this construct, multiplex genomic editing of up to three loci was achieved from a single yeast transformation. We also built a CRISPR interference system using a DNase-dead Cas12a to significantly repress endogenous gene expression. Our study provides the first CRISPR-Cas12a toolkit for efficient and rapid genomic gene editing and regulation in fission yeast.","doi":"10.1093/nar/gkaa329","authors":"Zhao Y, Boeke JD","authors_abbrev":"Zhao Y et al.","pubmed_publication_date":"04 Jun 2020","pubmed_entrez_date":"2020-05-07","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-05-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19197239","title":"Tdp1 protects against oxidative DNA damage in non-dividing fission yeast.","citation":"EMBO J 2009 Mar 18;28(6):632-40","abstract":"In humans, a mutation in the tyrosyl-DNA phosphodiesterase (Tdp1) is responsible for the recessively inherited syndrome spinocerebellar ataxia with axonal neuropathy (SCAN1). Tdp1 is a well-conserved DNA repair enzyme, which processes modified 3' phospho-DNA adducts in vitro. Here, we report that in the yeast Schizosaccharomyces pombe, tdp1 mutant cells progressively accumulate DNA damage and rapidly lose viability in a physiological G0/quiescent state. Remarkably, this effect is independent of topoisomerase I function. Moreover, we provide evidence that Tdp1, with the polynucleotide kinase (Pnk1), processes the same naturally occurring 3'-ends, produced from oxidative DNA damage in G0. We also found that one half of the dead cells lose their nuclear DNA. Nuclear DNA degradation is genetically programmed and mainly depends on the two DNA damage checkpoint responses, ATM/Tel1 and ATR/Rad3, reminiscent to programmed cell death. Diminishing the respiration rate or treating cells with a low concentration of antioxidants rescues the quiescent tdp1 mutant cells. These findings suggest that mitochondrial respiration causes neuronal cell death in the SCAN1 syndrome and in other neurological disorders.","doi":"10.1038/emboj.2009.9","authors":"Ben Hassine S, Arcangioli B","authors_abbrev":"Ben Hassine S et al.","pubmed_publication_date":"18 Mar 2009","pubmed_entrez_date":"2009-02-07","publication_year":"2009","canto_session_key":"7f04828e04705cea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-07-23 16:43:20","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-06-08 14:48:34","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":31,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1703.14c","SPAC23C11.04c","SPCP31B10.05","SPBC216.05","SPBC800.07c","SPCC23B6.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2012-06-08"},{"uniquename":"PMID:25302077","title":"Evolutionarily conserved genetic interactions with budding and fission yeast MutS identify orthologous relationships in mismatch repair-deficient cancer cells.","citation":"Genome Med 2014;6(9):68","abstract":"The evolutionarily conserved DNA mismatch repair (MMR) system corrects base-substitution and insertion-deletion mutations generated during erroneous replication. The mutation or inactivation of many MMR factors strongly predisposes to cancer, where the resulting tumors often display resistance to standard chemotherapeutics. A new direction to develop targeted therapies is the harnessing of synthetic genetic interactions, where the simultaneous loss of two otherwise non-essential factors leads to reduced cell fitness or death. High-throughput screening in human cells to directly identify such interactors for disease-relevant genes is now widespread, but often requires extensive case-by-case optimization. Here we asked if conserved genetic interactors (CGIs) with MMR genes from two evolutionary distant yeast species (Saccharomyces cerevisiae and Schizosaccharomyzes pombe) can predict orthologous genetic relationships in higher eukaryotes.\nHigh-throughput screening was used to identify genetic interaction profiles for the MutSα and MutSβ heterodimer subunits (msh2Δ, msh3Δ, msh6Δ) of fission yeast. Selected negative interactors with MutSβ (msh2Δ/msh3Δ) were directly analyzed in budding yeast, and the CGI with SUMO-protease Ulp2 further examined after RNA interference/drug treatment in MSH2-deficient and -proficient human cells.\nThis study identified distinct genetic profiles for MutSα and MutSβ, and supports a role for the latter in recombinatorial DNA repair. Approximately 28% of orthologous genetic interactions with msh2Δ/msh3Δ are conserved in both yeasts, a degree consistent with global trends across these species. Further, the CGI between budding/fission yeast msh2 and SUMO-protease Ulp2 is maintained in human cells (MSH2/SENP6), and enhanced by Olaparib, a PARP inhibitor that induces the accumulation of single-strand DNA breaks. This identifies SENP6 as a promising new target for the treatment of MMR-deficient cancers.\nOur findings demonstrate the utility of employing evolutionary distance in tractable lower eukaryotes to predict orthologous genetic relationships in higher eukaryotes. Moreover, we provide novel insights into the genome maintenance functions of a critical DNA repair complex and propose a promising targeted treatment for MMR deficient tumors.","doi":"10.1186/s13073-014-0068-4","authors":"Tosti E, Katakowski JA, Schaetzlein S, Kim HS, Ryan CJ, Shales M, Roguev A, Krogan NJ, Palliser D, Keogh MC, Edelmann W","authors_abbrev":"Tosti E et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-10-11","publication_year":"2014","canto_session_key":"92d24f2c79038ae3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-10-12 00:15:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9556367","title":"Length growth in fission yeast: is growth exponential?--No.","citation":"Microbiology (Reading) 1998 Feb;144 ( Pt 2):265-266","abstract":"","doi":"10.1099/00221287-144-2-265","authors":"Mitchison JM, Sveiczer A, Novak B","authors_abbrev":"Mitchison JM et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-04-29","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15702387","title":"Growth temperature affects accumulation of exogenous fatty acids and fatty acid composition in Schizosaccharomyces pombe.","citation":"Antonie Van Leeuwenhoek 2004 Nov;86(4):349-54","abstract":"The incorporation of exogenously supplied fatty acids, palmitic acid, palmitoleic acid, oleic acid and linoleic acid, was examined in the yeast Schizosaccharomyces pombe at two growth temperatures, 20 degrees C and 30 degrees C. Fatty acids supplied to S. pombe in the growth medium were found to be preferentially incorporated into the cells, becoming a dominant species. The relative increase in exogenous fatty acids in cells came at the expense of endogenous oleic acid as a proportion of total fatty acids. Lowering the temperature at which the yeast were grown resulted in decreased levels of incorporation of the fatty acids palmitic acid, palmitoleic acid and linoleic acid compared to cells supplemented at 30 degrees C. In addition, the relative amount of the endogenously produced unsaturated fatty acid oleic acid, while greatly reduced compared to unsupplemented cells, was increased in cells supplemented with fatty acids at 20 degrees C compared to supplemented cells at 30 degrees C. The differential production of oleic acid in S. pombe cells indicates that regulation of unsaturated fatty acid levels, possibly by control of the stearoyl-CoA desaturase, is an important control point in membrane composition in response to temperature and diet in this species.","authors":"McDonough VM, Roth TM","authors_abbrev":"McDonough VM et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2005-02-11","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17328741","title":"The calnexin-independent state does not compensate for all calnexin functions in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2007 Mar;7(2):196-208","abstract":"In the yeast Schizosaccharomyces pombe, the molecular chaperone calnexin (Cnx1p) has been shown to be essential for viability. However, we recently reported that, under certain circumstances, S. pombe cells are able to survive in the absence of calnexin/Cnx1p, indicating that an inducible pathway can complement the calnexin/Cnx1p essential function(s). This calnexin-independent state (Cin) is transmitted by a nonchromosomal proteinaceous element exhibiting several prion-like properties. To assess to what extent the Cin state compensates for the absence of calnexin/Cnx1p, the Cin strain was further characterized. Cin cells exhibited cell-wall defects, sensitivity to heat shock, as well as higher secretion levels of a model glycoprotein. Together, these results indicate that the Cin state does not compensate for all calnexin/Cnx1p functions. Reintroduction of plasmid-borne cnx1(+) partially rescued most but not all of the phenotypes displayed by Cin cells. Interestingly, Cin cells in stationary phase exhibited increased levels of caspase activation, and this phenotype was not suppressed by the reintroduction of cnx1(+), suggesting that cells in the Cin state are subjected to a stress other than the absence of calnexin/Cnx1p.","authors":"Turcotte C, Roux A, Beauregard PB, Guérin R, Sénéchal P, Hajjar F, Rokeach LA","authors_abbrev":"Turcotte C et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-03-03","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21859475","title":"Differential patterns of intronic and exonic DNA regions with respect to RNA polymerase II occupancy, nucleosome density and H3K36me3 marking in fission yeast.","citation":"Genome Biol 2011 Aug 22;12(8):R82","abstract":"The generation of mature mRNAs involves interconnected processes, including transcription by RNA polymerase II (Pol II), modification of histones, and processing of pre-mRNAs through capping, intron splicing, and polyadenylation. These processes are thought to be integrated, both spatially and temporally, but it is unclear how these connections manifest at a global level with respect to chromatin patterns and transcription kinetics. We sought to clarify the relationships between chromatin, transcription and splicing using multiple genome-wide approaches in fission yeast.\nTo investigate these functional interdependencies, we determined Pol II occupancy across all genes using high-density tiling arrays. We also performed ChIP-chip on the same array platform to globally map histone H3 and its H3K36me3 modification, complemented by formaldehyde-assisted isolation of regulatory elements (FAIRE). Surprisingly, Pol II occupancy was higher in introns than in exons, and this difference was inversely correlated with gene expression levels at a global level. Moreover, introns showed distinct distributions of histone H3, H3K36me3 and FAIRE signals, similar to those at promoters and terminators. These distinct transcription and chromatin patterns of intronic regions were most pronounced in poorly expressed genes.\nOur findings suggest that Pol II accumulates at the 3' ends of introns, leading to substantial transcriptional delays in weakly transcribed genes. We propose that the global relationship between transcription, chromatin remodeling, and splicing may reflect differences in local nuclear environments, with highly expressed genes being associated with abundant processing factors that promote effective intron splicing and transcriptional elongation.","doi":"10.1186/gb-2011-12-8-r82","authors":"Wilhelm BT, Marguerat S, Aligianni S, Codlin S, Watt S, Bähler J","authors_abbrev":"Wilhelm BT et al.","pubmed_publication_date":"22 Aug 2011","pubmed_entrez_date":"2011-08-24","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25866389","title":"Rewiring of cellular division site selection in evolution of fission yeasts.","citation":"Curr Biol 2015 May 04;25(9):1187-94","abstract":"Strategies to position the division apparatus exhibit a bewildering diversity [1], but how these mechanisms evolve remains virtually unknown. Here, we explore the plasticity of division site positioning in fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. We demonstrate that, whereas both species divide in the middle, only S. pombe uses the anillin Mid1 as a primary nucleus-derived cue to assemble the actomyosin ring at the equatorial cortex. We trace this variance to the divergence in subcellular targeting of Mid1 and show that duplication of an ancestral anillin early in the Schizosaccharomyces lineage may have led to subfunctionalization of the Mid1 orthologs. In contrast to S. pombe, medial assembly of the actomyosin ring in mitotic S. japonicus relies on the cortical anchor protein Cdc15 regulated by the tip-localized kinase Pom1. Our data suggest that division site placement is determined by cortical positioning of the actomyosin-plasma membrane linkers and that both identity of the linker and control of its subcellular targeting are highly modular.","doi":"10.1016/j.cub.2015.02.056","authors":"Gu Y, Yam C, Oliferenko S","authors_abbrev":"Gu Y et al.","pubmed_publication_date":"04 May 2015","pubmed_entrez_date":"2015-04-14","publication_year":"2015","canto_session_key":"17ae8f0715f87731","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Snezhana Oliferenko","canto_first_approved_date":"2015-07-29 16:51:36","canto_approved_date":"2024-04-02 17:29:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-02 14:00:45","canto_added_date":"2015-04-15 00:19:11","annotation_curators":[{"name":"Snezhana Oliferenko","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-07-29"},{"uniquename":"PMID:15800968","title":"The first two-dimensional reference map of the fission yeast, Schizosaccharomyces pombe proteins.","citation":"Proteomics 2005 Apr;5(6):1574-9","abstract":"Cytosolic proteins of Schizosaccharomyces pombe were separated by two-dimensional (2-D) gel electrophoresis, to construct the first 2-D reference map. In the pI range 4-7, more than 500 spots were detected by silver staining, and 70 different proteins corresponding to 111 spots were identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry and tandem mass spectrometry, where necessary. In the pI range 6-9, approximately 330 spots were detected, and 31 proteins corresponding to 38 spots were identified by mass spectrometry. More than 50% of the identified proteins were involved in amino acid, carbohydrate or nucleotide metabolism, and energy production. A second large group of identified proteins comprises heat shock and other stress related proteins and chaperones.","authors":"Sun N, Jang J, Lee S, Kim S, Lee S, Hoe KL, Chung KS, Kim DU, Yoo HS, Won M, Song KB","authors_abbrev":"Sun N et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-04-01","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23442799","title":"Dma/RNF8 proteins are evolutionarily conserved E3 ubiquitin ligases that target septins.","citation":"Cell Cycle 2013 Mar 15;12(6):1000-8","abstract":"The budding yeast proteins Dma1 and Dma2 are members of the unique FHA-RING domain protein family and are linked to mitotic regulation and septin organization by ill-defined mechanisms. We show that Dma2 has ubiquitin ligase activity, and that septins Shs1 and Cdc11 are likely direct in vivo targets. We further propose that human RNF8, rather than Chfr, is the mammalian Dma homolog. As in yeast, RNF8 localizes to the centrosomes and cell division sites and promotes ubiquitylation of the septin SEPT7, whose depletion increases cell division anomalies. Together, these findings reveal evolutionary and functional conservation of Dma proteins, and suggest that RNF8 maintains genome stability through independent, yet analogous, nuclear and cytoplasmic ubiquitylation activities.","doi":"10.4161/cc.23947","authors":"Chahwan R, Gravel S, Matsusaka T, Jackson SP","authors_abbrev":"Chahwan R et al.","pubmed_publication_date":"15 Mar 2013","pubmed_entrez_date":"2013-02-28","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G8.10c","HGNC:10071"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29453312","title":"Inhibition of Ras activity coordinates cell fusion with cell-cell contact during yeast mating.","citation":"J Cell Biol 2018 Apr 02;217(4):1467-1483","abstract":"In the fission yeast  Schizosaccharomyces pombe , pheromone signaling engages a signaling pathway composed of a G protein-coupled receptor, Ras, and a mitogen-activated protein kinase (MAPK) cascade that triggers sexual differentiation and gamete fusion. Cell-cell fusion requires local cell wall digestion, which relies on an initially dynamic actin fusion focus that becomes stabilized upon local enrichment of the signaling cascade on the structure. We constructed a live-reporter of active Ras1 (Ras1-guanosine triphosphate [GTP]) that shows Ras activity at polarity sites peaking on the fusion structure before fusion. Remarkably, constitutive Ras1 activation promoted fusion focus stabilization and fusion attempts irrespective of cell pairing, leading to cell lysis. Ras1 activity was restricted by the guanosine triphosphatase-activating protein Gap1, which was itself recruited to sites of Ras1-GTP and was essential to block untimely fusion attempts. We propose that negative feedback control of Ras activity restrains the MAPK signal and couples fusion with cell-cell engagement.","doi":"10.1083/jcb.201708195","authors":"Merlini L, Khalili B, Dudin O, Michon L, Vincenzetti V, Martin SG","authors_abbrev":"Merlini L et al.","pubmed_publication_date":"02 Apr 2018","pubmed_entrez_date":"2018-02-18","publication_year":"2018","canto_session_key":"129db89392d735c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Laura Merlini","canto_first_approved_date":"2018-04-19 16:28:52","canto_approved_date":"2026-02-17 14:55:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-22 10:53:01","canto_added_date":"2018-02-28 22:13:53","annotation_curators":[{"name":"Laura Merlini","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":41,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.03","SPAC1D4.13","SPAC3F10.10c","SPCC1442.01","SPAC17H9.09c","SPBC646.12c","SPAC22F3.12c","SPAC20G4.02c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2018-04-19"},{"uniquename":"PMID:16200533","title":"Three novel antibiotic marker cassettes for gene disruption and marker switching in Schizosaccharomyces pombe.","citation":"Yeast 2005 Oct 15;22(13):1013-9","abstract":"The ease of construction of multiple mutant strains in Schizosaccharomyces pombe is limited by the number of available genetic markers. We describe here three new cassettes for PCR-mediated gene disruption that can be used in combination with commonly used fission yeast markers to make multiple gene deletions. The natMX6, hphMX6 and bleMX6 markers give rise to resistance towards the antibiotics nourseothricin (NAT), hygromycin B and phleomycin, respectively. The cassettes are composed of exogenous sequences to increase the frequency of integration at targeted loci, and have a structure similar to the commonly used pFA6a-kanMX6 modular plasmid system. This allows a simple exchange of the kanMX6 marker in existing strains with any of the three new cassettes. Alternatively, oligonucleotide primers designed for the modular kanMX6 cassettes can be used to make the transforming PCR fragments for gene disruption. We illustrate the construction of a mutant strain with six independent gene disruptions, using the novel antibiotic cassettes in combination with existing genetic markers.","authors":"Hentges P, Van Driessche B, Tafforeau L, Vandenhaute J, Carr AM","authors_abbrev":"Hentges P et al.","pubmed_publication_date":"15 Oct 2005","pubmed_entrez_date":"2005-10-04","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38825008","title":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity.","citation":"J Biol Chem 2024 May 31;:107430","abstract":"The nuclear envelope (NE) is a permeable barrier that maintains nuclear-cytoplasmic compartmentalization and ensures nuclear function; however, it ruptures in various situations such as mechanical stress and mitosis. Although the protein components for sealing a ruptured NE have been identified, the mechanism by which lipid components are involved in this process remains to be elucidated. Here, we found that an inner nuclear membrane (INM) protein Bqt4 directly interacts with phosphatidic acid (PA) and serves as a platform for NE maintenance in the fission yeast Schizosaccharomyces pombe. The intrinsically disordered region (IDR) of Bqt4, proximal to the transmembrane domain, binds to PA and forms a solid aggregate in vitro. Excessive accumulation of Bqt4 IDR in INM results in membrane overproliferation and lipid droplet formation in the nucleus, leading to centromere dissociation from the NE and chromosome missegregation. Our findings suggest that Bqt4 IDR controls nuclear membrane homeostasis by recruiting PA to the INM, thereby maintaining the structural integrity of the NE.","doi":"10.1016/j.jbc.2024.107430","authors":"Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y","authors_abbrev":"Hirano Y et al.","pubmed_publication_date":"31 May 2024","pubmed_entrez_date":"2024-06-02","publication_year":"2024","canto_session_key":"e1b1536bc0389824","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Hirano","canto_first_approved_date":"2025-04-22 12:12:59","canto_approved_date":"2026-06-26 08:46:14","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-17 10:20:53","canto_added_date":"2024-06-03 23:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yasuhiro Hirano","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC594.07c","SPBC19C7.10","SPBC365.12c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2025-04-22"},{"uniquename":"PMID:30635402","title":"Casein kinase II-dependent phosphorylation of DNA topoisomerase II suppresses the effect of a catalytic topo II inhibitor, ICRF-193, in fission yeast.","citation":"J Biol Chem 2019 Mar 08;294(10):3772-3782","abstract":"DNA topoisomerase II (topo II) regulates the topological state of DNA and is necessary for DNA replication, transcription, and chromosome segregation. Topo II has essential functions in cell proliferation and therefore is a critical target of anticancer drugs. In this study, using Phos-tag SDS-PAGE analysis in fission yeast ( Schizosaccharomyces pombe ), we identified casein kinase II (Cka1/CKII)-dependent phosphorylation at the C-terminal residues Ser 1363  and Ser 1364  in topo II. We found that this phosphorylation decreases the inhibitory effect of an anticancer catalytic inhibitor of topo II, ICRF-193, on mitosis. Consistent with the constitutive activity of Cka1/CKII, Ser 1363  and Ser 1364  phosphorylation of topo II was stably maintained throughout the cell cycle. We demonstrate that ICRF-193-induced chromosomal mis-segregation is further exacerbated in two temperature-sensitive mutants,  cka1-372  and  cka1/orb5-19 , of the catalytic subunit of CKII or in the topo II nonphosphorylatable alanine double mutant  top2-S1363A,S1364A  but not in cells of the phosphomimetic glutamate double mutant  top2-S1363E,S1364E  Our results suggest that Ser 1363  and Ser 1364  in topo II are targeted by Cka1/CKII kinase and that their phosphorylation facilitates topo II ATPase activity in the N-terminal region, which regulates protein turnover on chromosome DNA. Because CKII-mediated phosphorylation of the topo II C-terminal domain appears to be evolutionarily conserved, including in humans, we propose that attenuation of CKII-controlled topo II phosphorylation along with catalytic topo II inhibition may promote anticancer effects.","doi":"10.1074/jbc.RA118.004955","authors":"Nakazawa N, Arakawa O, Ebe M, Yanagida M","authors_abbrev":"Nakazawa N et al.","pubmed_publication_date":"08 Mar 2019","pubmed_entrez_date":"2019-01-13","publication_year":"2019","canto_session_key":"884c35ae47e3fec8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Norihiko Nakazawa","canto_first_approved_date":"2019-02-06 17:11:45","canto_approved_date":"2025-09-03 12:53:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-25 16:26:03","canto_added_date":"2019-01-14 01:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Norihiko Nakazawa","community_curator":true,"annotation_count":7,"orcid":"0000-0001-8386-0812","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.11","SPBC1A4.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-02-06"},{"uniquename":"PMID:27698242","title":"Analysis of Schizosaccharomyces pombe Heterochromatin-Associated Short Interfering RNAs.","citation":"Cold Spring Harb Protoc 2016 Oct 03;2016(10)","abstract":"An important aspect of RNAi-mediated heterochromatin assembly is the production of short interfering RNAs (siRNAs) in cis at the heterochromatic target. These populations of small RNAs (20-30 nt) can be detected via northern blot analysis with radiolabeled RNA probes corresponding to the siRNAs. Most heterochromatin-associated siRNAs originate from both strands of the pericentromeric dg and dh repeats. Thus, production of RNA probes by in vitro transcription utilizes a DNA template with sequences corresponding to either dg or dh repeats. Alternatively, radiolabeled DNA probes, which are somewhat easier to prepare, may be used. A control probe against a small RNA, such as a tRNA, may also be prepared for loading. More recently genome-scale analysis using next-generation sequencing platforms has enabled the detection of rare siRNAs at sites other than the major heterochromatin domains. This protocol describes procedures for the extraction of small RNAs from Schizosaccharomyces pombe and their detection by northern blot analysis.","doi":"10.1101/pdb.prot091520","authors":"Zhang K","authors_abbrev":"Zhang K","pubmed_publication_date":"03 Oct 2016","pubmed_entrez_date":"2016-10-05","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-10-07 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31494498","title":"Pyranoanthocyanins in bilberry (Vaccinium myrtillus L.) wines fermented with Schizosaccharomyces pombe and their evolution during aging.","citation":"Food Chem 2020 Feb 01;305:125438","abstract":"Fifteen vitisin A-type pyranoanthocyanins (vAPs) were determined in bilberry wines fermented with Saccharomyces cerevisiae and Schizosaccharomyces pombe by HPLC-DAD and UPLC-DAD-ESI-MS/MS. The fermentation involving S. pombe enhanced the production of vAPs compared to the fermentation with pure S. cerevisiae. The formation of vAPs correlated significantly with the decrease in the content of monomeric anthocyanins and pyruvic acid during 12 months of aging. vAPs were more stable than their corresponding monomeric anthocyanins. Methylation in the B-ring and glycosylation with galactose and arabinose further improved the stability of vAPs. Aging for 12 months led to depletion of pyruvic acid and reduction of over 50% of monomeric anthocyanins. The content of vAPs increased by 26-54% during the first six months of aging, followed by a 2.2-10.2% reduction over the following six months. More residual pyruvic acid in S. pombe wines after fermentation consequently enhanced the generation of vAPs during aging.","doi":"10.1016/j.foodchem.2019.125438","authors":"Liu S, Laaksonen O, Yang W, Zhang B, Yang B","authors_abbrev":"Liu S et al.","pubmed_publication_date":"01 Feb 2020","pubmed_entrez_date":"2019-09-09","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2019-09-10 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40878921","title":"Endocytic patch dynamics are differentially regulated at distinct cell sites in fission yeast.","citation":"J Cell Sci 2025 Aug 29;","abstract":"Endocytosis promotes polarity and growth in eukaryotes. In Schizosaccharomyces pombe fission yeast, endocytosis occurs at the polarized cell ends and division site and at the non-polarized cell sides. Our characterization of endocytic actin patches show that they are differentially regulated. The patches at the cell ends and division site internalize successfully while those at the sides are weak and erratic. The major regulator of cell polarity, Cdc42, and its target Pak1 kinase only localize to the cell ends and division site. We find that these proteins regulate assembly and internalization of patches at these sites but not at the cell sides. Moreover, Cdc42 specifically activated by the GEF Gef1 promotes proper patch dynamics. Endocytosis requires phosphorylation of the Type I Myosin Myo1 by the Pak1 kinase. Myo1 localizes to the cell ends, division site, and the cell sides. We find that unlike Cdc42 and Pak1, Myo1 also promotes patch assembly at the cell sides. Our data indicate that while Myo1 can globally promote branched actin assembly, successful endocytic patch dynamics and internalization at polarized sites require Cdc42 and Pak1 kinase.","doi":"10.1242/jcs.263873","authors":"Campbell BF, Kalathil D, Patel UJ, Williams AR, Das ME","authors_abbrev":"Campbell BF et al.","pubmed_publication_date":"29 Aug 2025","pubmed_entrez_date":"2025-08-29","publication_year":"2025","canto_session_key":"a70e961228c29e62","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-08-29 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26240178","title":"The fission yeast cytokinetic contractile ring regulates septum shape and closure.","citation":"J Cell Sci 2015 Oct 01;128(19):3672-81","abstract":"During cytokinesis, fission yeast and other fungi and bacteria grow a septum that divides the cell in two. In fission yeast closure of the circular septum hole by the β-glucan synthases (Bgs) and other glucan synthases in the plasma membrane is tightly coupled to constriction of an actomyosin contractile ring attached to the membrane. It is unknown how septum growth is coordinated over scales of several microns to maintain septum circularity. Here, we documented the shapes of ingrowing septum edges by measuring the roughness of the edges, a measure of the deviation from circularity. The roughness was small, with spatial correlations indicative of spatially coordinated growth. We hypothesized that Bgs-mediated septum growth is mechanosensitive and coupled to contractile ring tension. A mathematical model showed that ring tension then generates almost circular septum edges by adjusting growth rates in a curvature-dependent fashion. The model reproduced experimental roughness statistics and showed that septum synthesis sets the mean closure rate. Our results suggest that the fission yeast cytokinetic ring tension does not set the constriction rate but regulates septum closure by suppressing roughness produced by inherently stochastic molecular growth processes.","doi":"10.1242/jcs.166926","authors":"Thiyagarajan S, Munteanu EL, Arasada R, Pollard TD, O'Shaughnessy B","authors_abbrev":"Thiyagarajan S et al.","pubmed_publication_date":"01 Oct 2015","pubmed_entrez_date":"2015-08-05","publication_year":"2015","canto_session_key":"696c020115766283","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-06 00:19:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26275423","title":"Inner Kinetochore Protein Interactions with Regional Centromeres of Fission Yeast.","citation":"Genetics 2015 Oct;201(2):543-61","abstract":"Centromeres of the fission yeast Schizosaccharomyces pombe lack the highly repetitive sequences that make most other \"regional\" centromeres refractory to analysis. To map fission yeast centromeres, we applied H4S47C-anchored cleavage mapping and native and cross-linked chromatin immunoprecipitation with paired-end sequencing. H3 nucleosomes are nearly absent from the central domain, which is occupied by centromere-specific H3 (cenH3 or CENP-A) nucleosomes with two H4s per particle that are mostly unpositioned and are more widely spaced than nucleosomes elsewhere. Inner kinetochore proteins CENP-A, CENP-C, CENP-T, CENP-I, and Scm3 are highly enriched throughout the central domain except at tRNA genes, with no evidence for preferred kinetochore assembly sites. These proteins are weakly enriched and less stably incorporated in H3-rich heterochromatin. CENP-A nucleosomes protect less DNA from nuclease digestion than H3 nucleosomes, while CENP-T protects a range of fragment sizes. Our results suggest that CENP-T particles occupy linkers between CENP-A nucleosomes and that classical regional centromeres differ from other centromeres by the absence of CENP-A nucleosome positioning.","doi":"10.1534/genetics.115.179788","authors":"Thakur J, Talbert PB, Henikoff S","authors_abbrev":"Thakur J et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2015-08-16","publication_year":"2015","canto_session_key":"dbcc669ae67615f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Steven Henikoff","canto_first_approved_date":"2015-10-13 20:32:42","canto_approved_date":"2025-09-03 16:21:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-08 22:11:08","canto_added_date":"2015-08-17 00:18:53","annotation_curators":[{"name":"Steven Henikoff","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.03c","SPBC8D2.03c","SPBC1105.17","SPBC800.13","SPAC1687.20c","SPAPB1A10.02","SPBC1861.01c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2015-10-13"},{"uniquename":"PMID:34017941","title":"Recombination and biased segregation of mitochondrial genomes during crossing and meiosis of different  Schizosaccharomyces pombe  strains.","citation":"MicroPubl Biol 2021 May 17;2021","abstract":"During meiosis, tethering of parental mitochondria to opposite cell poles inhibits the mixing of mitochondria with different genomes and ensures uniparental inheritance in thestandard laboratory strain of fission yeast. We here investigate mitochondrial inheritance in crosses between natural isolates using tetrad dissection and next-generation sequencing. We find that colonies grown from single spores can sometimes carry a mix of mitochondrial genotypes, that mitochondrial genomes can recombine during meiosis, that in some cases tetrads do not follow the 2:2 segregation pattern, and that certain crosses may feature a weak bias towards one of the parents. Together, these findings paint a more nuanced picture of mitochondrial inheritance in the wild.","doi":"10.17912/micropub.biology.000390","authors":"Kamrad S, Rodríguez-López M, Dey S, Hoti M, Wallace H, Ralser M, Bähler J","authors_abbrev":"Kamrad S et al.","pubmed_publication_date":"17 May 2021","pubmed_entrez_date":"2021-05-21","publication_year":"2021","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2021-05-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7850425","title":"Cell division. Septins in common?","citation":"Curr Biol 1994 Oct 01;4(10):907-10","abstract":"Two apparently quite distinct processes, cytokinesis in animal cells and in budding yeast cells, have been shown to involve proteins of the same family, the septins, suggesting that the two may not be so different after all.","authors":"Sanders SL, Field CM","authors_abbrev":"Sanders SL et al.","pubmed_publication_date":"01 Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPO310560","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39865413","title":"Conformational dynamics in specialized C 2 H 2  zinc finger domains enable zinc-responsive gene repression in S. pombe.","citation":"Protein Sci 2025 Feb;34(2):e70044","abstract":"Loz1 is a zinc-responsive transcription factor in fission yeast that maintains cellular zinc homeostasis by repressing the expression of genes required for zinc uptake in high zinc conditions. Previous deletion analysis of Loz1 found a region containing two tandem C 2 H 2  zinc-fingers and an upstream \"accessory domain\" rich in histidine, lysine, and arginine residues to be sufficient for zinc-dependent DNA binding and gene repression. Here we report unexpected biophysical properties of this pair of seemingly classical C 2 H 2  zinc fingers. Isothermal titration calorimetry and NMR spectroscopy reveal two distinct zinc binding events localized to the zinc fingers. NMR spectra reveal complex dynamic behavior in this zinc-responsive region spanning time scales from fast 10 -12 -10 -10  to slow >10 0  s. Slow exchange due to cis-trans isomerization of the TGERP linker results in the doubling of many signals in the protein. Conformational exchange on the 10 -3  s timescale throughout the first zinc finger distinguishes it from the second and is linked to a weaker affinity for zinc. These findings reveal a mechanism of zinc sensing by Loz1 and illuminate how the protein's rough free-energy landscape enables zinc sensing, DNA binding and regulated gene expression.","doi":"10.1002/pro.70044","authors":"Wadhwa V, Jamshidi C, Stachowski K, Bird AJ, Foster MP","authors_abbrev":"Wadhwa V et al.","pubmed_publication_date":"Feb 2025","pubmed_entrez_date":"2025-01-26","publication_year":"2025","canto_session_key":"e94c5c417ab40958","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-07-16 09:05:42","canto_approved_date":"2025-07-16 09:05:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-07-12 17:16:25","canto_added_date":"2025-01-28 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.19c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-07-16"},{"uniquename":"PMID:16085480","title":"Division-plane positioning: microtubules strike back.","citation":"Curr Biol 2005 Aug 09;15(15):R595-7","abstract":"Two groups have recently developed physical techniques to manipulate the position of the nucleus in fission yeast. Their studies reveal how microtubules confine the nucleus to the cell center, and indicate how the position of the cleavage plane during cell division is coordinated with that of the nucleus.","authors":"Mendoza M, Norden C, Barral Y","authors_abbrev":"Mendoza M et al.","pubmed_publication_date":"09 Aug 2005","pubmed_entrez_date":"2005-08-09","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9003295","title":"Isolation of novel pre-mRNA splicing mutants of Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1996 Nov 27;253(1-2):118-27","abstract":"New prp (pre-mRNA processing) mutants of the fission yeast Schizosaccharomyces pombe were isolated from a bank of 700 mutants that were either temperature sensitive (ts-) or cold sensitive (cs-) for growth. The bank was screened by Northern blot analysis with probes complementary to S. pombe U6 small nuclear RNA (sn RNA), the gene for which has a splicesomal (mRNA-type) intron. We identified 12 prp mutants that accumulated the U6 snRNA precursor at the nonpermissive temperature. All such mutants were also found to have defects in an early step of TFIID pre-mRNA splicing at the nonpermissive temperature. Complementation analyses showed that seven of the mutants belong to six new complementation groups designated as prp8 and prp10-prp14, whereas the five other mutants were classified into the known complementation groups prp1, prp2 and prp3. Interestingly, some of the isolated prp mutants produced elongated cells at the nonpermissive temperature, which is a phenotype typical of cell division cycle (cdc) mutants. Based on these findings, we propose that some of the wild-type products from these prp+ genes play important roles in the cellular processes of pre-mRNA splicing and cell cycle progression.","authors":"Urushiyama S, Tani T, Ohshima Y","authors_abbrev":"Urushiyama S et al.","pubmed_publication_date":"27 Nov 1996","pubmed_entrez_date":"1996-11-27","publication_year":"1996","canto_session_key":"5fc5dcfda8548024","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2016-08-08 10:46:23","canto_approved_date":"2026-01-31 14:15:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-27 17:02:28","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":71,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_9003295_phaf.tsv"}],"genes":["SPBC19C2.01","SPAC29E6.02","SPSNRNA.04","SPBC146.07","SPAC2G11.14","SPAC3A12.11c","SPCC10H11.01","SPBC1711.17","SPAC27F1.09c","SPSNRNA.06","SPBC6B1.07","SPAPJ698.03c"],"gene_count":12,"ltp_gene_count":9,"approved_date":"2016-08-08"},{"uniquename":"PMID:17352737","title":"The fission yeast DASH complex is essential for satisfying the spindle assembly checkpoint induced by defects in the inner-kinetochore proteins.","citation":"Genes Cells 2007 Mar;12(3):311-28","abstract":"Spindle assembly checkpoint (SAC) is an evolutionarily conserved surveillance system for chromosome missegregation. We isolated fission yeast Hos2, a component of the Dam1/DASH complex, as a multicopy suppressor of temperature-sensitive (ts) growth of nnf1-495 mutant that exhibits the minichromosome instability (mis) phenotype, producing lethal aneuploids without prominent mitotic delay. It remains elusive why SAC is satisfied in mis mutants despite the occurrence of missegregation. We found that Hos2 binds to the inner-kinetochore regions in both prometaphase and metaphase. Hos2 is essential for kinetochore localization of Dis1, a microtubule (MT) associated Dis1/XMAP215/TOG family protein that is required for proper MT dynamics. Cells lacking DASH exhibit cold-sensitive (cs) growth with the defective in sister-chromatid disjoining (dis) phenotype, which is characterized by hyper-condensed sister-chromatid pairs and elongated spindle MTs. Although DASH-deficient cells are viable at high temperatures, DASH-deletion transforms all the inner-kinetochore mis mutants so far tested into a constitutively active state of SAC, leading to the dis phenotype. We also discovered that Hos2 over-expression commonly suppresses growth retardation in a variety of inner-kinetochore mutants. These genetic interactions highlight the DASH-action(s) in satisfying SAC when aneuploids are formed during mitosis in the inner-kinetochore-defective mis mutants.","authors":"Kobayashi Y, Saitoh S, Ogiyama Y, Soejima S, Takahashi K","authors_abbrev":"Kobayashi Y et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-03-14","publication_year":"2007","canto_session_key":"be0d5c94b70a919d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-04-23 15:06:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-11 16:40:10","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.02c","SPBC409.09c","SPCC736.14","SPAC1805.07c","SPAC1687.20c","SPAC27F1.04c","SPCC970.12","SPAC29E6.04","SPAC3G9.07c","SPBC1105.17","SPBC409.04c","SPBC21.01"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2015-02-11"},{"uniquename":"PMID:21295010","title":"Mitochondrial localization of fission yeast manganese superoxide dismutase is required for its lysine acetylation and for cellular stress resistance and respiratory growth.","citation":"Biochem Biophys Res Commun 2011 Mar 04;406(1):42-6","abstract":"Manganese-dependent superoxide dismutase (MnSOD) is localized in the mitochondria and is important for oxidative stress resistance. Although transcriptional regulation of MnSOD has been relatively well studied, much less is known about the protein's posttranslational regulation. In budding yeast, MnSOD is activated after mitochondrial import by manganese ion incorporation. Here we characterize posttranslational modification of MnSOD in the fission yeast Schizosaccharomyces pombe. Fission yeast MnSOD is acetylated at the 25th lysine residue. This acetylation was diminished by deletion of N-terminal mitochondrial targeting sequence, suggesting that MnSOD is acetylated after import into mitochondria. Mitochondrial localization of MnSOD is not essential for the enzyme activity, but is crucial for oxidative stress resistance and growth under respiratory conditions of fission yeast. These results suggest that, unlike the situation in budding yeast, S. pombe MnSOD is already active even before mitochondrial localization; nonetheless, mitochondrial localization is critical to allow the cell to cope with reactive oxygen species generated inside or outside of mitochondria.","doi":"10.1016/j.bbrc.2011.01.103","authors":"Takahashi H, Suzuki T, Shirai A, Matsuyama A, Dohmae N, Yoshida M","authors_abbrev":"Takahashi H et al.","pubmed_publication_date":"04 Mar 2011","pubmed_entrez_date":"2011-02-08","publication_year":"2011","canto_session_key":"336033f42dff3d97","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Minoru Yoshida","canto_first_approved_date":"2014-06-03 12:43:26","canto_approved_date":"2022-02-02 13:47:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-10 16:18:39","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":94,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Minoru Yoshida","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.13c","SPAC29A4.20","SPAC1952.05","SPAC1486.01","SPAC139.06"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-06-03"},{"uniquename":"PMID:33468217","title":"Rbm10 facilitates heterochromatin assembly via the Clr6 HDAC complex.","citation":"Epigenetics Chromatin 2021 Jan 19;14(1):8","abstract":"Splicing factors have recently been shown to be involved in heterochromatin formation, but their role in controlling heterochromatin structure and function remains poorly understood. In this study, we identified a fission yeast homologue of human splicing factor RBM10, which has been linked to TARP syndrome. Overexpression of Rbm10 in fission yeast leads to strong global intron retention. Rbm10 also interacts with splicing factors in a pattern resembling that of human RBM10, suggesting that the function of Rbm10 as a splicing regulator is conserved. Surprisingly, our deep-sequencing data showed that deletion of Rbm10 caused only minor effect on genome-wide gene expression and splicing. However, the mutant displays severe heterochromatin defects. Further analyses indicated that the heterochromatin defects in the mutant did not result from mis-splicing of heterochromatin factors. Our proteomic data revealed that Rbm10 associates with the histone deacetylase Clr6 complex and chromatin remodelers known to be important for heterochromatin silencing. Deletion of Rbm10 results in significant reduction of Clr6 in heterochromatin. Our work together with previous findings further suggests that different splicing subunits may play distinct roles in heterochromatin regulation.","doi":"10.1186/s13072-021-00382-y","authors":"Weigt M, Gao Q, Ban H, He H, Mastrobuoni G, Kempa S, Chen W, Li F","authors_abbrev":"Weigt M et al.","pubmed_publication_date":"19 Jan 2021","pubmed_entrez_date":"2021-01-20","publication_year":"2021","canto_session_key":"2c3138a3a4b94cfc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Fei Li","canto_first_approved_date":"2021-03-19 16:04:06","canto_approved_date":"2025-09-03 11:40:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-11 22:42:20","canto_added_date":"2021-01-22 01:15:05","annotation_curators":[{"name":"Fei Li","community_curator":true,"annotation_count":39,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30B4.04c","SPBC12C2.10c","SPAC57A7.13","SPAC29B12.01","SPAC23E2.02","SPAC23G3.04","SPBC31F10.13c","SPAC2F7.08c","SPBP23A10.05","SPBC365.10","SPAC23H3.10","SPAC1071.06","SPBP8B7.19","SPCC663.05c","SPAC664.02c","SPAC3G6.01","SPAC1F7.01c","SPAC23G3.10c","SPAC23G3.07c","SPBP4H10.06c","SPBC36.05c","SPAC23H4.12","SPAC6B12.05c","SPCC1620.14c","SPCC188.07","SPBC15D4.03","SPAC25B8.02","SPAC17G6.10","SPAC29A4.18","SPCC1259.07","SPCC306.03c","SPAC23D3.09","SPBP23A10.08"],"gene_count":33,"ltp_gene_count":33,"approved_date":"2021-03-19"},{"uniquename":"PMID:27347039","title":"Identification of novel biomarkers for preeclampsia on the basis of differential expression network analysis.","citation":"Exp Ther Med 2016 Jul;12(1):201-207","abstract":"Preeclampsia (PE) is a severe pregnancy complication, which is a leading cause of maternal and fetal mortality. The present study aimed to screen potential biomarkers for the diagnosis and prediction of PE and to investigate the underlying mechanisms of PE development based on the differential expression network (DEN). The microarray datasets E-GEOD-6573 and E-GEOD-48424 were downloaded from the European Bioinformatics Institute database. Differentially expressed genes (DEGs) between the PE and normal groups were screened by Significant Analysis of Microarrays with the cutoff value of a |log2 fold change| of >2, and a false discovery rate of <0.05. The DEN was constructed based on the differential and non-differential interactions observed. In addition, genes with higher connectivity degrees in the DEN were identified on the basis of centrality analysis, while disease genes were also extracted from the DEN. In order to understand the functional roles of genes in DEN, Gene Ontology (GO) and pathway enrichment analyses were performed. The present results indicated that a total of 225 genes were considered as DEGs in the PE group, while 466 nodes and 314 gene interactions were involved in the DEN. Among these 466 nodes, 4 nodes with higher degrees were identified, including ubiquitin C ( UBC ), small ubiquitin-like modifier 1 ( SUMO1 ),  SUMO2  and RAD21 homolog ( S. pombe ) ( RAD21 ). Notably,  UBC  was also found to be a disease gene.  UBC ,  RAD21 ,  SUMO2  and  SUMO1  were markedly enriched in the regulation of programmed cell death, as well as in the regulation of apoptosis, cell cycle and chromosomal part. In conclusion, based on these results, we suggest that  UBC ,  RAD21 ,  SUMO2  and  SUMO1  may be reliable biomarkers for the prediction of the development and progression of PE.","authors":"Wu Y, Fu X, Wang L","authors_abbrev":"Wu Y et al.","pubmed_publication_date":"Jul 2016","pubmed_entrez_date":"2016-06-28","publication_year":"2016","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2016-06-29 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9894913","title":"Cloning of caf1+, caf2+ and caf4+ from Schizosaccharomyces pombe: their involvement in multidrug resistance, UV and pH sensitivity.","citation":"Mol Gen Genet 1998 Dec;260(5):434-43","abstract":"We previously identified four nuclear genes (caf1+ to caf4+) in Schizosaccharomyces pombe, mutations in which can confer caffeine resistance. Here we report the cloning and sequencing of caf1+, caf2+ and caf4+. All three genes are allelic to genes (hba1+, crm1+ and trr1+, respectively) involved in multidrug resistance mechanisms or in stress response systems. In agreement with this the caffeine-resistant mutants caf1(hba1)-21, caf2(crm1)-3 and caf4(trr1)-83 are also resistant to brefeldin. Disruption of caf1(hba1)+ and caf4(trr1)+ makes cells sensitive to high pH. The overlapping ranges of pleiotropic effects and the genetic interaction detected between caf1(hba1)+ and caf2(crm1)+ suggest that the three genes function in interlinked systems.","authors":"Benko Z, Sipiczki M, Carr AM","authors_abbrev":"Benko Z et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1999-01-23","publication_year":"1998","canto_session_key":"f28ef4b4272d1303","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-02 13:52:04","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-06-12 17:55:56","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.17","SPBC3F6.03","SPBC365.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-06-12"},{"uniquename":"PMID:15503870","title":"Analysis of human GPCRs in fission yeast.","citation":"Curr Opin Drug Discov Devel 2004 Sep;7(5):683-91","abstract":"G protein-coupled receptors (GPCRs) regulate diverse biological processes in all eukaryotes, including yeast, insects, plants and humans. This evolutionary conservation allows an almost unrestricted interchange of signaling components between different cell types. A large number of model systems have been developed for the study of GPCRs, and yeasts provide one of the more attractive hosts since they are amenable to both genetic and biochemical manipulation, while their robustness, low cost and lack of endogenous GPCRs are ideal starting points for the development of assays suitable for high-throughput screening. The purpose of this review is to introduce readers to the possibilities of using the fission yeast Schizosaccharomyces pombe for analysis of GPCRs. We describe the endogenous signaling pathways, the development of assays for heterologous GPCRs, and some of the technology available to elucidate GPCR structure and activity.","authors":"Ladds G, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-10-27","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012817","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.133","SPNCRNA.134","SPNCRNA.62"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:11861551","title":"Schizosaccharomyces pombe Bir1p, a nuclear protein that localizes to kinetochores and the spindle midzone, is essential for chromosome condensation and spindle elongation during mitosis.","citation":"Genetics 2002 Feb;160(2):445-56","abstract":"The inhibitor of apoptosis (IAP) family of proteins contains a subset of members characterized by the presence of highly conserved baculoviral IAP repeat (BIR) domains. Recent work has shown that some of these BIR-domain proteins play a prominent role in the regulation of cell division, in particular at the stage of chromosome segregation and cytokinesis. We and others have shown that the Schizosaccharomyces pombe BIR-domain protein, Bir1p/Pbh1p/Cut17p, is important for the regulation of mitosis. Here we further characterize S. pombe Bir1p using methods of cell biology and genetics. We show that Bir1p is dispersed throughout the nucleus during the cell cycle. In addition, a significant part of Bir1p is also detected at the kinetochores and the spindle midzone during mitosis and meiosis. Time-lapse microscopy studies suggest that Bir1p relocates from the kinetochores to the spindle at the end of anaphase A. Bir1p colocalizes with the S. pombe Aurora kinase homolog Aim1p, a protein essential for mitosis, at the kinetochores as well as the spindle midzone during mitosis, and functional Bir1p is essential for localization of Aim1p to the kinetochores and the spindle midzone. Analyses of bir1 conditional mutants revealed that Bir1p is essential for chromosome condensation during mitosis. In addition, anaphase cells show the presence of lagging chromosomes and a defect in spindle elongation. We conclude that Bir1p is important for multiple processes that occur during mitosis in S. pombe.","authors":"Rajagopalan S, Balasubramanian MK","authors_abbrev":"Rajagopalan S et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-02-28","publication_year":"2002","canto_session_key":"d3646296251ff27d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-07 16:53:19","canto_approved_date":"2024-03-27 14:50:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-07 16:53:13","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.13c","SPCC962.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-11-07"},{"uniquename":"PMID:12802505","title":"Malo-ethanolic fermentation in Saccharomyces and Schizosaccharomyces.","citation":"Curr Genet 2003 Sep;43(6):379-91","abstract":"Yeast species are divided into the K(+) or K(-) groups, based on their ability or inability to metabolise tricarboxylic acid (TCA) cycle intermediates as sole carbon or energy source. The K(-) group of yeasts includes strains of Saccharomyces, Schizosaccharomyces pombe and Zygosaccharomyces bailii, which is capable of utilising TCA cycle intermediates only in the presence of glucose or other assimilable carbon sources. Although grouped together, these yeasts have significant differences in their abilities to degrade malic acid. Typically, strains of Saccharomyces are regarded as inefficient metabolisers of extracellular malic acid, whereas strains of Sch. pombe and Z. bailii can effectively degrade high concentrations of malic acid. The ability of a yeast strain to degrade extracellular malic acid is dependent on both the efficient transport of the dicarboxylic acid and the efficacy of the intracellular malic enzyme. The malic enzyme converts malic acid into pyruvic acid, which is further metabolised to ethanol and carbon dioxide under fermentative conditions via the so-called malo-ethanolic (ME) pathway. This review focuses on the enzymes involved in the ME pathway in Sch. pombe and Saccharomyces species, with specific emphasis on the malate transporter and the intracellular malic enzyme.","authors":"Volschenk H, van Vuuren HJ, Viljoen-Bloom M","authors_abbrev":"Volschenk H et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-06-13","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31269446","title":"CPF Recruitment to Non-canonical Transcription Termination Sites Triggers Heterochromatin Assembly and Gene Silencing.","citation":"Cell Rep 2019 Jul 02;28(1):267-281.e5","abstract":"In eukaryotic genomes, heterochromatin is targeted by RNAi machinery and/or by pathways requiring RNA elimination and transcription termination factors. However, a direct connection between termination machinery and RNA polymerase II (RNAPII) transcriptional activity at heterochromatic loci has remained elusive. Here, we show that, in fission yeast, the conserved cleavage and polyadenylation factor (CPF) is a key component involved in RNAi-independent assembly of constitutive and facultative heterochromatin domains and that CPF is broadly required to silence genes regulated by Clr4 SUV39H . Remarkably, CPF is recruited to non-canonical termination sites within the body of genes by the YTH family RNA-binding protein Mmi1 and is required for RNAPII transcription termination and facultative heterochromatin assembly. CPF loading by Mmi1 also promotes the selective termination of long non-coding RNAs that regulate gene expression in cis. These analyses delineate a mechanism in which CPF loaded onto non-canonical termination sites specifies targets of heterochromatin assembly and gene silencing.","doi":"10.1016/j.celrep.2019.05.107","authors":"Vo TV, Dhakshnamoorthy J, Larkin M, Zofall M, Thillainadesan G, Balachandran V, Holla S, Wheeler D, Grewal SIS","authors_abbrev":"Vo TV et al.","pubmed_publication_date":"02 Jul 2019","pubmed_entrez_date":"2019-07-04","publication_year":"2019","canto_session_key":"9835916579ea9c49","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tommy Vo","canto_first_approved_date":"2020-01-08 14:13:15","canto_approved_date":"2025-07-02 16:23:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-23 20:22:06","canto_added_date":"2019-07-05 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":44,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tommy Vo","community_curator":true,"annotation_count":21,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.01c","SPAC22G7.10","SPAC16A10.07c","SPAC12G12.14c","SPCC736.11","SPAC227.08c","SPBC1709.15c","SPBC660.15","SPCC188.07","SPAC6F12.17","SPBC428.08c","SPBC28F2.12","SPBC776.02c","SPAC4G9.04c","SPAC6F6.17","SPBC1709.08","SPAC17G6.16c","SPBC646.04","SPCC74.02c","SPAC3G9.04","SPBC3B9.11c","SPAC824.04","SPCC736.12c"],"gene_count":22,"ltp_gene_count":22,"approved_date":"2020-01-08"},{"uniquename":"PMID:34436165","title":"The PPIP5K Family Member Asp1 Controls Inorganic Polyphosphate Metabolism in  S. pombe .","citation":"J Fungi (Basel) 2021 Jul 31;7(8)","abstract":"Inorganic polyphosphate (polyP) which is ubiquitously present in both prokaryotic and eukaryotic cells, consists of up to hundreds of orthophosphate residues linked by phosphoanhydride bonds. The biological role of this polymer is manifold and diverse and in fungi ranges from cell cycle control, phosphate homeostasis and virulence to post-translational protein modification. Control of polyP metabolism has been studied extensively in the budding yeast  Saccharomyces cerevisiae.  In this yeast, a specific class of inositol pyrophosphates (IPPs), named IP 7 , made by the IP6K family member Kcs1 regulate polyP synthesis by associating with the SPX domains of the vacuolar transporter chaperone (VTC) complex. To assess if this type of regulation was evolutionarily conserved, we determined the elements regulating polyP generation in the distantly related fission yeast  Schizosaccharomyces pombe . Here, the VTC machinery is also essential for polyP generation. However, and in contrast to  S. cerevisiae , a different IPP class generated by the bifunctional PPIP5K family member Asp1 control polyP metabolism. The analysis of Asp1 variant  S. pombe  strains revealed that cellular polyP levels directly correlate with Asp1-made IP 8  levels, demonstrating a dose-dependent regulation. Thus, while the mechanism of polyP synthesis in yeasts is conserved, the IPP player regulating polyP metabolism is diverse.","doi":"10.3390/jof7080626","authors":"Pascual-Ortiz M, Walla E, Fleig U, Saiardi A","authors_abbrev":"Pascual-Ortiz M et al.","pubmed_publication_date":"31 Jul 2021","pubmed_entrez_date":"2021-08-26","publication_year":"2021","canto_session_key":"e9275c33a7042e3a","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-08-28 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1672.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8424869","title":"PCR used to determine mating type in S. pombe.","citation":"Biotechniques 1993 Jan;14(1):18","abstract":"","authors":"Sunnerhagen P","authors_abbrev":"Sunnerhagen P","pubmed_publication_date":"Jan 1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33825974","title":"Linear elements are stable structures along the chromosome axis in fission yeast meiosis.","citation":"Chromosoma 2021 Sep;130(2-3):149-162","abstract":"The structure of chromosomes dramatically changes upon entering meiosis to ensure the successful progression of meiosis-specific events. During this process, a multilayer proteinaceous structure called a synaptonemal complex (SC) is formed in many eukaryotes. However, in the fission yeast Schizosaccharomyces pombe, linear elements (LinEs), which are structures related to axial elements of the SC, form on the meiotic cohesin-based chromosome axis. The structure of LinEs has been observed using silver-stained electron micrographs or in immunofluorescence-stained spread nuclei. However, the fine structure of LinEs and their dynamics in intact living cells remain to be elucidated. In this study, we performed live cell imaging with wide-field fluorescence microscopy as well as 3D structured illumination microscopy (3D-SIM) of the core components of LinEs (Rec10, Rec25, Rec27, Mug20) and a linE-binding protein Hop1. We found that LinEs form along the chromosome axis and elongate during meiotic prophase. 3D-SIM microscopy revealed that Rec10 localized to meiotic chromosomes in the absence of other LinE proteins, but shaped into LinEs only in the presence of all three other components, the Rec25, Rec27, and Mug20. Elongation of LinEs was impaired in double-strand break-defective rec12 -  cells. The structure of LinEs persisted after treatment with 1,6-hexanediol and showed slow fluorescence recovery from photobleaching. These results indicate that LinEs are stable structures resembling axial elements of the SC.","doi":"10.1007/s00412-021-00757-w","authors":"Ding DQ, Matsuda A, Okamasa K, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"Sep 2021","pubmed_entrez_date":"2021-04-07","publication_year":"2021","canto_session_key":"0e16556e33d4d7d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Da-Qiao Ding","canto_first_approved_date":"2021-06-15 12:33:40","canto_approved_date":"2021-09-13 16:09:34","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-06-09 00:55:24","canto_added_date":"2021-04-10 00:15:06","annotation_curators":[{"name":"Da-Qiao Ding","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPBC1718.02","SPAC25G10.04c","SPBC36B7.06c","SPAC17A5.18c","SPBC577.05c","SPAC110.02"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2021-06-15"},{"uniquename":"PMID:8154183","title":"Accurate initiation of mRNA synthesis in extracts from Schizosaccharomyces pombe, Kluyveromyces lactis and Candida glabrata.","citation":"Yeast 1993 Dec;9(12):1331-4","abstract":"We demonstrate the successful adaptation to other yeast species of a protocol previously described for production of transcriptionally active whole cell extracts from Saccharomyces cerevisiae (Woontner and Jaehning, 1990, J. Biol. Chem. 265, 8979-8982). Extracts prepared from Schizosaccharomyces pombe, Kluyveromyces lactis and Candida glabrata were all capable of initiating transcription from a template containing the S. cerevisiae CYC1 TATA box fused to a G-less cassette. Transcription in all of the extracts was sensitive to inhibition by alpha-amanitin, indicating that it was catalysed by RNA polymerase II, and was dramatically stimulated by the chimeric activator GAL4/VP16. The different extracts used different subsets of a group of three initiation sites.","authors":"Woontner M, Jaehning JA","authors_abbrev":"Woontner M et al.","pubmed_publication_date":"Dec 1993","pubmed_entrez_date":"1993-12-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29930085","title":"Local and global Cdc42 guanine nucleotide exchange factors for fission yeast cell polarity are coordinated by microtubules and the Tea1-Tea4-Pom1 axis.","citation":"J Cell Sci 2018 Jul 19;131(14)","abstract":"The conserved Rho-family GTPase Cdc42 plays a central role in eukaryotic cell polarity. The rod-shaped fission yeast  Schizosaccharomyces pombe  has two Cdc42 guanine nucleotide exchange factors (GEFs), Scd1 and Gef1, but little is known about how they are coordinated in polarized growth. Although the microtubule cytoskeleton is normally not required for polarity maintenance in fission yeast, we show here that when  scd1  function is compromised, disruption of microtubules or the polarity landmark proteins Tea1, Tea4 or Pom1 leads to disruption of polarized growth. Instead, cells adopt an isotropic-like pattern of growth, which we term PORTLI growth. Surprisingly, PORTLI growth is caused by spatially inappropriate activity of Gef1. Although most Cdc42 GEFs are membrane associated, we find that Gef1 is a broadly distributed cytosolic protein rather than a membrane-associated protein at cell tips like Scd1. Microtubules and the Tea1-Tea4-Pom1 axis counteract inappropriate Gef1 activity by regulating the localization of the Cdc42 GTPase-activating protein Rga4. Our results suggest a new model of fission yeast cell polarity regulation, involving coordination of 'local' (Scd1) and 'global' (Gef1) Cdc42 GEFs via microtubules and microtubule-dependent polarity landmarks.","doi":"10.1242/jcs.216580","authors":"Tay YD, Leda M, Goryachev AB, Sawin KE","authors_abbrev":"Tay YD et al.","pubmed_publication_date":"19 Jul 2018","pubmed_entrez_date":"2018-06-23","publication_year":"2018","canto_session_key":"3d43cf9a14d68a43","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ken Sawin","canto_first_approved_date":"2018-08-13 10:45:58","canto_approved_date":"2024-04-03 16:26:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-02 07:11:00","canto_added_date":"2018-06-24 00:15:04","annotation_curators":[{"name":"Ken Sawin","community_curator":true,"annotation_count":24,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1706.01","SPBC800.05c","SPAC24H6.09","SPCC1223.06","SPBC1604.14c","SPAC110.03","SPBC11B10.09","SPAC16E8.09","SPCC18B5.03","SPCC1840.02c","SPCC970.09","SPAC2F7.03c","SPBC28E12.03","SPBC32H8.12c"],"gene_count":14,"ltp_gene_count":10,"approved_date":"2018-08-13"},{"uniquename":"PMID:10958988","title":"Cell cycle G2 arrest induced by HIV-1 Vpr in fission yeast (Schizosaccharomyces pombe) is independent of cell death and early genes in the DNA damage checkpoint.","citation":"Virus Res 2000 Jul;68(2):161-73","abstract":"HIV-1 Vpr induces cell cycle G2 arrest, morphological changes and cell death in human and fission yeast cells. The cellular targets for G2 arrest were expected to be the inhibitory phosphorylation sites of Cdc2, as G2 arrest correlates with hyperphosphorylation and decreased activity of Cdc2 in both human and fission yeast cells. In this study, we present direct evidence of genetic suppression of Vpr-induced G2 arrest by cdc2 mutations. Mutations in cdc2 (cdc2-1w and cdc2-3w) reduce the ability of Vpr to induce G2 arrest. A strain with a mutation changing the Tyr15 of Cdc2 to the non-phosphorylated Phe (Y15F) eliminated Vpr-induced G2 arrest indicating that Tyr15 of Cdc2 is the sole target for induction of G2 arrest by Vpr. Although the G2 arrest induced by DNA damage also proceeds through phosphorylation of Tyr15, the rad1, rad3, rad9 and rad17 mutations, which eliminate the G2 checkpoint for DNA damage, did not block the G2 arrest induced by Vpr. Furthermore, Vpr expression did not alter sensitivity of these rad mutants to UV radiation. Thus, the pathways for the induction of G2 arrest by DNA damage and Vpr are not identical. Interestingly, Vpr still induces cell death and morphological changes in the Y15F Cdc2 strain indicating that G2 arrest is not required for morphological changes and cell death. This conclusion was further supported by the observation that mutations in Vpr, which have lost their ability to induce G2 arrest, retained the ability to kill cells.","authors":"Elder RT, Yu M, Chen M, Edelson S, Zhao Y","authors_abbrev":"Elder RT et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-08-26","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23438755","title":"A chemical biology strategy to analyze rheostat-like protein kinase-dependent regulation.","citation":"Chem Biol 2013 Feb 21;20(2):262-71","abstract":"Protein kinases may function more like variable rheostats rather than two-state switches. However, we lack approaches to properly analyze this aspect of kinase-dependent regulation. To address this, we develop a strategy in which a kinase inhibitor is identified using genetics-based screens, kinase mutations that confer resistance are characterized, and dose-dependent responses of isogenic drug-sensitive and resistant cells to inhibitor treatments are compared. This approach has the advantage that function of wild-type kinase, rather than mutants, is examined. To develop this approach, we focus on Ark1, the fission yeast member of the conserved Aurora kinase family. Applying this approach reveals that proper chromosome compaction in fission yeast needs high Ark1 activity, while other processes depend on significantly lower activity levels. Our strategy is general and can be used to examine the functions of other molecular rheostats.","doi":"10.1016/j.chembiol.2013.01.003","authors":"Kawashima SA, Takemoto A, Nurse P, Kapoor TM","authors_abbrev":"Kawashima SA et al.","pubmed_publication_date":"21 Feb 2013","pubmed_entrez_date":"2013-02-27","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC776.02c","SPCC320.13c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:16252696","title":"Features of coding and noncoding sequences based on 3-tuple distributions.","citation":"Yi Chuan Xue Bao 2005 Oct;32(10):1018-26","abstract":"The origin of non-coding sequences, especially introns,is an outstanding issue that has been receiving continuous debate for the last two decades. In the current work we use a mathematical model to characterize DNA sequences and find that the 3-tuple distributions in different reading frames of a given coding sequence differ sharply from each other, while they are almost identical to each other in introns or other non-coding sequences. SREs (Symmetric relative entropies) decrease progressively from coding sequences of primitive prokaryotes to those of advanced eukaryotes and from non-coding sequences of low eukaryotes to those of high eukaryotes with a correlation coefficient of 0.86. In silico evolution experiments show that SREs typical of higher eukaryotic introns can be achieved from prokaryotic coding sequences as the mutation ratio reaches 2/100. The fact that (a total of 25 introns) from all three different genomes S. pombe, C. elegans and H. sapiens searched are found to share high sequence identity with coding regions indicates that at least some introns may have come directly from CDS (coding sequences). We suggest that SREs may be a useful feature for evolutionary study.","authors":"Fu Q, Qian MP, Chen LB, Zhu YX","authors_abbrev":"Fu Q et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-10-29","publication_year":"2005","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27585850","title":"Hydroxyurea Induces Cytokinesis Arrest in Cells Expressing a Mutated Sterol-14α-Demethylase in the Ergosterol Biosynthesis Pathway.","citation":"Genetics 2016 Nov;204(3):959-973","abstract":"Hydroxyurea (HU) has been used for the treatment of multiple diseases, such as cancer. The therapeutic effect is generally believed to be due to the suppression of ribonucleotide reductase (RNR), which slows DNA polymerase movement at replication forks and induces an S phase cell cycle arrest in proliferating cells. Although aberrant mitosis and DNA damage generated at collapsed forks are the likely causes of cell death in the mutants with defects in replication stress response, the mechanism underlying the cytotoxicity of HU in wild-type cells remains poorly understood. While screening for new fission yeast mutants that are sensitive to replication stress, we identified a novel mutation in the erg11 gene encoding the enzyme sterol-14α-demethylase in the ergosterol biosynthesis pathway that dramatically sensitizes the cells to chronic HU treatment. Surprisingly, HU mainly arrests the erg11 mutant cells in cytokinesis, not in S phase. Unlike the reversible S phase arrest in wild-type cells, the cytokinesis arrest induced by HU is relatively stable and occurs at low doses of the drug, which likely explains the remarkable sensitivity of the mutant to HU. We also show that the mutation causes sterol deficiency, which may predispose the cells to the cytokinesis arrest and lead to cell death. We hypothesize that in addition to the RNR, HU may have a secondary unknown target(s) inside cells. Identification of such a target(s) may greatly improve the chemotherapies that employ HU or help to expand the clinical usage of this drug for additional pathological conditions.","doi":"10.1534/genetics.116.191536","authors":"Xu YJ, Singh A, Alter GM","authors_abbrev":"Xu YJ et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-09-03","publication_year":"2016","canto_session_key":"2fe26fc19315e3a3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-09-04 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC25D12.04","SPCC1259.13","SPBC216.05"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:34389684","title":"Genetic screen for suppression of transcriptional interference identifies a gain-of-function mutation in Pol2 termination factor Seb1.","citation":"Proc Natl Acad Sci U S A 2021 Aug 17;118(33)","abstract":"The system of long noncoding RNA (lncRNA)-mediated transcriptional interference that represses fission yeast phosphate homoeostasis gene  pho1  provides a sensitive readout of genetic influences on cotranscriptional 3'-processing and termination and a tool for discovery of regulators of this phase of the Pol2 transcription cycle. Here, we conducted a genetic screen for relief of transcriptional interference that unveiled a mechanism by which Pol2 termination is enhanced via a gain-of-function mutation, G476S, in the RNA-binding domain of an essential termination factor, Seb1. The genetic and physical evidence for gain-of-function is compelling: 1)  seb1-G476S  de-represses  pho1  and  tgp1 , both of which are subject to lncRNA-mediated transcriptional interference; 2)  seb1-G476S  elicits precocious lncRNA transcription termination in response to lncRNA 5'-proximal poly(A) signals; 3)  seb1-G476S  derepression of  pho1  is effaced by loss-of-function mutations in cleavage and polyadenylation factor (CPF) subunits and termination factor Rhn1; 4) synthetic lethality of  seb1-G476S  with  pho1  derepressive mutants  rpb1-CTD-S7A  and  aps1 ∆ is rescued by CPF/Rhn1 loss-of-function alleles; and 5)  seb1-G476S  elicits an upstream shift in poly(A) site preference in several messenger RNA genes. A crystal structure of the Seb1-G476S RNA-binding domain indicates potential for gain of contacts from Ser476 to RNA nucleobases. To our knowledge, this is a unique instance of a gain-of-function phenotype in a eukaryal transcription termination protein.","doi":"10.1073/pnas.2108105118","authors":"Schwer B, Garg A, Jacewicz A, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"17 Aug 2021","pubmed_entrez_date":"2021-08-14","publication_year":"2021","canto_session_key":"67f8ea3e5c1c1bfc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Angad Garg","canto_first_approved_date":"2022-01-17 18:35:25","canto_approved_date":"2024-06-20 14:19:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-19 12:31:56","canto_added_date":"2021-08-16 00:15:05","annotation_curators":[{"name":"Angad Garg","community_curator":true,"annotation_count":66,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G6.14","SPAC222.09","SPBC776.02c","SPBP4G3.02","SPCC1795.03","SPBC3B9.11c","SPBC3H7.15","SPBC337.03","SPCC1393.08","SPCC14G10.04","SPAC688.04c","SPNCRNA.1698","SPBC215.05","SPAC3G9.04","SPBPB8B6.05c","SPCC74.02c","SPAC824.04","SPBC2F12.03c","SPBP8B7.16c","SPCC338.14","SPNCRNA.1712","SPBC28F2.12","SPBC1683.10c","SPCC1672.06c"],"gene_count":24,"ltp_gene_count":11,"approved_date":"2022-01-17","pdb_entries":[{"pdb_id":"7mi2","gene_chains":[{"gene_uniquename":"SPAC222.09","chain":"A","position":"388-539"}],"title":"Seb1-G476S RNA binding domain","entry_authors":"Jacewicz A,Shuman S","entry_authors_abbrev":"Jacewicz A et al.","reference_uniquename":"PMID:34389684","experimental_method":"X-ray","resolution":"1.4"}]},{"uniquename":"PMID:22173095","title":"Reduced protein stability of human DJ-1/PARK7 L166P, linked to autosomal recessive Parkinson disease, is due to direct endoproteolytic cleavage by the proteasome.","citation":"Biochim Biophys Acta 2012 Feb;1823(2):524-33","abstract":"Parkinson's disease (PD) is characterized by dopaminergic dysfunction and degeneration. DJ-1/PARK7 mutations have been linked with a familial form of early onset PD. In this study, we found that human DJ-1 wild type and the missense mutants M26I, R98Q, A104T and D149A were stable proteins in cells, only the L166P mutant was unstable. In parallel, the former were not degraded and the L166P mutant was directly degraded in vitro by proteasome-mediated endoproteolytic cleavage. Furthermore, genetic evidence in fission yeast showed the direct involvement of proteasome in the degradation of human DJ-1 L166P and the corresponding L169P mutant of SPAC22E12.03c, the human orthologue of DJ-1 in Schizosaccharomyces Pombe, as their protein levels were increased at restrictive temperature in fission yeast (mts4 and pts1-732) harboring temperature sensitive mutations in proteasomal subunits. In total, our results provide evidence that direct proteasomal endoproteolytic cleavage of DJ-1 L166P is the mechanism of degradation contributing to the loss-of-function of the mutant protein, a property not shared by other DJ-1 missense mutants associated with PD.","doi":"10.1016/j.bbamcr.2011.11.010","authors":"Alvarez-Castelao B, Muñoz C, Sánchez I, Goethals M, Vandekerckhove J, Castaño JG","authors_abbrev":"Alvarez-Castelao B et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-12-17","publication_year":"2012","canto_session_key":"cd959543ef54eb92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-31 22:03:09","canto_approved_date":"2024-12-04 20:49:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-27 13:49:11","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.03c","SPAC4A8.13c","SPBP19A11.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-10-31"},{"uniquename":"PMID:9790887","title":"Purification and characterization of pyruvate kinase from Schizosaccharomyces pombe: evidence for an unusual quaternary structure.","citation":"Protein Expr Purif 1998 Nov;14(2):247-53","abstract":"Earlier attempts to purify and characterize nonrecombinant pyruvate kinase from Schizosaccharomyces pombe proved difficult due to problems associated with the instability of the protein. The enzyme has been overexpressed in Saccharomyces cerevisiae strain AH22, permitting studies to determine the conditions required to stabilize the enzyme during purification. Recombinant S. pombe pyruvate kinase was purified by a combination of ion-exchange chromatography and gel filtration. The purified enzyme showed sigmoidal kinetics with respect to PEP; in the presence of FBP, the kinetics were restored to Michaelis-Menten behavior. With respect to ADP, the Hill coefficient was not affected by FBP. Determination of the molecular mass of the purified enzyme by ultracentrifugation showed that it behaved as a dimer-tetramer system with a Kd of approximately 1 microM.","authors":"Nairn J, Duncan D, Gray LM, Urquhart G, Binnie M, Byron O, Fothergill-Gilmore LA, Price NC","authors_abbrev":"Nairn J et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1998-10-29","publication_year":"1998","canto_session_key":"51e6761e98119281","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-01 10:45:09","canto_approved_date":"2025-05-19 08:16:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-01 10:45:02","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4H3.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-01"},{"uniquename":"PMID:23962284","title":"The Schizosaccharomyces pombe fusion gene hal3 encodes three distinct activities.","citation":"Mol Microbiol 2013 Oct;90(2):367-82","abstract":"Saccharomyces cerevisiae Hal3 and Vhs3 are moonlighting proteins, forming an atypical heterotrimeric decarboxylase (PPCDC) required for CoA biosynthesis, and regulating cation homeostasis by inhibition of the Ppz1 phosphatase. The Schizosaccharomyces pombe ORF SPAC15E1.04 (renamed as Sp hal3) encodes a protein whose amino-terminal half is similar to Sc Hal3 whereas its carboxyl-terminal half is related to thymidylate synthase (TS). We show that Sp Hal3 and/or its N-terminal domain retain the ability to bind to and modestly inhibit in vitro S. cerevisiae Ppz1 as well as its S. pombe homolog Pzh1, and also exhibit PPCDC activity in vitro and provide PPCDC function in vivo, indicating that Sp Hal3 is a monogenic PPCDC in fission yeast. Whereas the Sp Hal3 N-terminal domain partially mimics Sc Hal3 functions, the entire protein and its carboxyl-terminal domain rescue the S. cerevisiae cdc21 mutant, thus proving TS function. Additionally, we show that the 70 kDa Sp Hal3 protein is not proteolytically processed under diverse forms of stress and that, as predicted, Sp hal3 is an essential gene. Therefore, Sp hal3 represents a fusion event that joined three different functional activities in the same gene. The possible advantage derived from this surprising combination of essential proteins is discussed.","doi":"10.1111/mmi.12370","authors":"Molero C, Petrényi K, González A, Carmona M, Gelis S, Abrie JA, Strauss E, Ramos J, Dombradi V, Hidalgo E, Ariño J","authors_abbrev":"Molero C et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-08-22","publication_year":"2013","canto_session_key":"5694c1e2978a9fd3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-28 16:09:01","canto_approved_date":"2022-07-09 11:43:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-28 13:19:17","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15E1.04","SPAC57A7.08","SPAC15A10.16"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2017-03-28"},{"uniquename":"PMID:15569158","title":"The Sec14 family glycerophospholipid-transfer protein is required for structural integrity of the spindle pole body during meiosis in fission yeast.","citation":"Genes Cells 2004 Dec;9(12):1275-86","abstract":"The fission yeast spo20+ gene encodes a glycerophospholipid-transfer protein. spo20 mutants are unable to assemble the forespore membrane properly. Here we studied the structural integrity of the spindle pole body (SPB) in spo20-H6 mutants during meiosis. Meiotic cells expressing a GFP-tagged SPB marker protein, Spo15-GFP, showed an excess number of SPBs, some of which were not localized to the spindle poles and were termed 'pseudo-SPBs'. Formation of spindles for meiosis I was significantly delayed in spo20-H6 cells, although the morphology of spindles and segregation of the sister chromatids seemed normal. The SPB of spo20-H6 contained meiosis-specific outer plaques, though outermost layers were less evident. Time-lapse studies of spo20-H6 cells showed that the pseudo-SPBs originated from normal SPBs at the spindle poles during meiosis I. Among the SPB components tested, Spo15, Spo13, Sad1 and Cut12 were localized to the pseudo-SPBs, but Sid4 was not always present. Alp4, a component of the gamma-tubulin complex, was also present in about 40% of the pseudo-SPBs. The forespore membranes initiated from both the SPBs and the pseudo-SPBs. We conclude that Spo20 plays a role in maintaining the structural integrity of the meiotic SPB, besides supplying membrane vesicles for forespore membrane assembly.","authors":"Nakase Y, Nakamura T, Okazaki K, Hirata A, Shimoda C","authors_abbrev":"Nakase Y et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-12-01","publication_year":"2004","canto_session_key":"a7840af580454a74","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-07-20 14:24:55","canto_approved_date":"2026-03-06 10:02:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-27 15:17:03","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.15","SPAC3H8.10"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-07-20"},{"uniquename":"PMID:36122598","title":"Metabolic engineering of Schizosaccharomyces pombe for itaconic acid production.","citation":"J Biotechnol 2022 Nov 10;358:111-117","abstract":"The economical production of value-added chemicals from renewable biomass is a promising aspect of producing a sustainable economy. Itaconic acid (IA) is a high value-added compound that is expected to be an alternative to petroleum-based chemicals. In this study, we developed a metabolic engineering strategy for the large-scale production of IA from glucose using the fission yeast Schizosaccharomyces pombe. Heterologous expression of the cis-aconitic acid decarboxylase (CAD) gene from Aspergillus terreus, which encodes cis-aconitate decarboxylase in the cytosol, led to the production of 0.132 g/L of IA. We demonstrated that mitochondrial localization of CAD enhanced the production of IA. To prevent the leakage of carbon flux from the TCA cycle, we generated a strain in which the endogenous malate exporter, citrate lyase, and citrate transporter genes were disrupted. A titer of 1.110 g/L of IA was obtained from a culture of this strain started with 50 g/L of glucose. By culturing the multiple mutant strain at increased cell density, we succeeded in enhancing the IA production to 1.555 g/L. The metabolic engineering strategies presented in this study have the potential to improve the titer of the biosynthesis of derivatives of intermediates of the TCA cycle.","doi":"10.1016/j.jbiotec.2022.09.006","authors":"Fujie N, Ito M, Kishida M, Hirata Y, Kondo A, Tanaka T","authors_abbrev":"Fujie N et al.","pubmed_publication_date":"10 Nov 2022","pubmed_entrez_date":"2022-09-19","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-09-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7660126","title":"The chromodomain protein Swi6: a key component at fission yeast centromeres.","citation":"Science 1995 Sep 08;269(5229):1429-31","abstract":"Centromeres attach chromosomes to the spindle during mitosis, thereby ensuring the equal distribution of chromosomes into daughter cells. Transcriptionally silent heterochromatin of unknown function is associated with centromeres in many organisms. In the fission yeast Schizosaccharomyces pombe, the silent mating-type loci, centromeres, and telomeres are assembled into silent heterochromatin-like domains. The Swi6 chromodomain protein affects this silencing, and now it is shown that Swi6p localizes with these three chromosomal regions. In cells lacking Swi6p, centromeres lag on the spindle during anaphase and chromosomes are lost at high rates. Thus, Swi6p is located at fission yeast centromeres and is required for their proper function.","authors":"Ekwall K, Javerzat JP, Lorentz A, Schmidt H, Cranston G, Allshire R","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"08 Sep 1995","pubmed_entrez_date":"1995-09-08","publication_year":"1995","canto_session_key":"50433449a8dcdfe6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-03-23 17:39:16","canto_approved_date":"2024-01-21 18:07:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 15:31:04","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-03-23"},{"uniquename":"PMID:30877183","title":"Yeast epigenetics: the inheritance of histone modification states.","citation":"Biosci Rep 2019 May 31;39(5)","abstract":" Saccharomyces cerevisiae  (budding yeast) and  Schizosaccharomyces pombe  (fission yeast) are two of the most recognised and well-studied model systems for epigenetic regulation and the inheritance of chromatin states. Their silent loci serve as a proxy for heterochromatic chromatin in higher eukaryotes, and as such both species have provided a wealth of information on the mechanisms behind the establishment and maintenance of epigenetic states, not only in yeast, but in higher eukaryotes. This review focuses specifically on the role of histone modifications in governing telomeric silencing in  S. cerevisiae  and centromeric silencing in  S. pombe  as examples of genetic loci that exemplify epigenetic inheritance. We discuss the recent advancements that for the first time provide a mechanistic understanding of how heterochromatin, dictated by histone modifications specifically, is preserved during S-phase. We also discuss the current state of our understanding of yeast nucleosome dynamics during DNA replication, an essential component in delineating the contribution of histone modifications to epigenetic inheritance.","doi":"10.1042/BSR20182006","authors":"O'Kane CJ, Hyland EM","authors_abbrev":"O'Kane CJ et al.","pubmed_publication_date":"31 May 2019","pubmed_entrez_date":"2019-03-17","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-03-18 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:X74275","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26484169","title":"Data for chromosome contacts and matched transcription profiles at three cell cycle phases in the fission yeast.","citation":"Genom Data 2015 Jun;4:12-6","abstract":"The data described in this article pertains to Grand et al. (2014), \"Chromosome conformation maps in fission yeast reveal cell cycle dependent sub nuclear structure\" [1]. Temperature sensitive Schizosaccharomyces pombe cell division cycle (cdc) mutants, which are induced by a shift in temperature to 36 °C, were chosen for the analysis of genome structure in the G1 phase, G2 phase and mitotic anaphase of the cell cycle. Chromatin and total RNA were isolated from the same cell culture following synchronization. Two biological replicates were analyzed for each condition. The global, three-dimensional organization of the chromosomes was captured at high resolution using Genome Conformation Capture (GCC). GCC libraries and RNA samples were sequenced using an Illumina Hi-Seq 2000 platform (Beijing Genomics Institute (China)). DNA sequences were processed using the Topography suite v1.19 [2] to obtain chromosome contact frequency matrices. RNA sequences were processed using the Cufflinks pipeline [3] to measure gene transcript levels and how these varied between the conditions. All sequence data, processed GCC and transcriptome files are available under the Gene Expression Omnibus (GEO) accession number GSE52287 (http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE52287).","doi":"10.1016/j.gdata.2015.01.005","authors":"Grand RS, O'Sullivan JM","authors_abbrev":"Grand RS et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-10-21","publication_year":"2015","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2015-10-22 00:19:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20624220","title":"Kin1 is a plasma membrane-associated kinase that regulates the cell surface in fission yeast.","citation":"Mol Microbiol 2010 Sep;77(5):1186-202","abstract":"Cell morphogenesis is a complex process that depends on cytoskeleton and membrane organization, intracellular signalling and vesicular trafficking. The rod shape of the fission yeast Schizosaccharomyces pombe and the availability of powerful genetic tools make this species an excellent model to study cell morphology. Here we have investigated the function of the conserved Kin1 kinase. Kin1-GFP associates dynamically with the plasma membrane at sites of active cell surface remodelling and is present in the membrane fraction. Kin1Δ null cells show severe defects in cell wall structure and are unable to maintain a rod shape. To explore Kin1 primary function, we constructed an ATP analogue-sensitive allele kin1-as1. Kin1 inhibition primarily promotes delocalization of plasma membrane-associated markers of actively growing cell surface regions. Kin1 itself is depolarized and its mobility is strongly reduced. Subsequently, amorphous cell wall material accumulates at the cell surface, a phenotype that is dependent on vesicular trafficking, and the cell wall integrity mitogen-activated protein kinase pathway is activated. Deletion of cell wall integrity mitogen-activated protein kinase components reduces kin1Δ hypersensitivity to stresses such as those induced by Calcofluor white and SDS. We propose that Kin1 is required for a tight link between the plasma membrane and the cell wall.","doi":"10.1111/j.1365-2958.2010.07281.x","authors":"Cadou A, Couturier A, Le Goff C, Soto T, Miklos I, Sipiczki M, Xie L, Paulson JR, Cansado J, Le Goff X","authors_abbrev":"Cadou A et al.","pubmed_publication_date":"Sep 2010","pubmed_entrez_date":"2010-07-14","publication_year":"2010","canto_session_key":"34d6329cd65525e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-05 16:01:03","canto_approved_date":"2025-12-21 11:38:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-05 16:00:55","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.02c","SPBC336.12c","SPBC1289.01c","SPBC1685.01","SPCC1739.11c","SPBC119.08","SPBC4F6.06","SPAC17G8.14c","SPBC12D12.04c","SPCC825.03c","SPAC24H6.05","SPAC688.11","SPAC16.01","SPBC244.01c","SPBC19G7.05c","SPCC895.05"],"gene_count":16,"ltp_gene_count":11,"approved_date":"2015-10-05"},{"uniquename":"PMID:21693583","title":"A calmodulin-related light chain from fission yeast that functions with myosin-I and PI 4-kinase.","citation":"J Cell Sci 2011 Jul 15;124(Pt 14):2466-77","abstract":"Fission yeast myosin-I (Myo1p) not only associates with calmodulin, but also employs a second light chain called Cam2p. cam2Δ cells exhibit defects in cell polarity and growth consistent with a loss of Myo1p function. Loss of Cam2p leads to a reduction in Myo1p levels at endocytic patches and a 50% drop in the rates of Myo1p-driven actin filament motility. Thus, Cam2p plays a significant role in Myo1p function. However, further studies indicated the existence of an additional Cam2p-binding partner. Cam2p was still present at cortical patches in myo1Δ cells (or in myo1-IQ2 mutants, which lack an intact Cam2p-binding motif), whereas a cam2 null (cam2Δ) suppressed cytokinesis defects of an essential light chain (ELC) mutant known to be impaired in binding to PI 4-kinase (Pik1p). Binding studies revealed that Cam2p and the ELC compete for Pik1p. Cortical localization of Cam2p in the myo1Δ background relied on its association with Pik1p, whereas overexpression studies indicated that Cam2p, in turn, contributes to Pik1p function. The fact that the Myo1p-associated defects of a cam2Δ mutant are more potent than those of a myo1-IQ2 mutant suggests that myosin light chains can contribute to actomyosin function both directly and indirectly (via phospholipid synthesis at sites of polarized growth).","doi":"10.1242/jcs.067850","authors":"Sammons MR, James ML, Clayton JE, Sladewski TE, Sirotkin V, Lord M","authors_abbrev":"Sammons MR et al.","pubmed_publication_date":"15 Jul 2011","pubmed_entrez_date":"2011-06-23","publication_year":"2011","canto_session_key":"00c35706b38fef88","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-03 07:21:48","canto_approved_date":"2025-05-27 20:20:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-02 03:43:04","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.16c","SPAC29A4.05","SPCC645.05c","SPBC146.13c","SPAP8A3.08"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2021-01-03"},{"uniquename":"PMID:22264160","title":"A chemical genetic approach for covalent inhibition of analogue-sensitive aurora kinase.","citation":"ACS Chem Biol 2012 Apr 20;7(4):723-31","abstract":"The perturbation of protein kinases with small organic molecules is a powerful approach to dissect kinase function in complex biological systems. Covalent kinase inhibitors that target thiols in the ATP binding pocket of the kinase domain proved to be ideal reagents for the investigation of highly dynamic cellular processes. However, due to the covalent inhibitors' possible off-target reactivities, it is required that the overall shape of the inhibitor as well as the intrinsic reactivity of the electrophile are precisely tuned to favor the reaction with only the desired cysteine. Here we report on the design and biological characterization of covalent anilinoquinazolines as potent inhibitors of genetically engineered Aurora kinase in fission yeast.","doi":"10.1021/cb200465c","authors":"Koch A, Rode HB, Richters A, Rauh D, Hauf S","authors_abbrev":"Koch A et al.","pubmed_publication_date":"20 Apr 2012","pubmed_entrez_date":"2012-01-24","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:13992376","title":"[Research on the role of myoinositol in the cellular biology of Schizosaccharomyces pombe Lindner].","citation":"Arch Mikrobiol 1962;44:113-51","abstract":"","authors":"SCHOPFER WH, POSTERNAK T, WUSTENFELD D","authors_abbrev":"SCHOPFER WH et al.","pubmed_publication_date":"1962","pubmed_entrez_date":"1962-01-01","publication_year":"1962","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8114737","title":"Sap1, a protein that binds to sequences required for mating-type switching, is essential for viability in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1994 Mar;14(3):2058-65","abstract":"The pattern of mating-type switching in cell pedigrees of the fission yeast Schizosaccharomyces pombe is dictated by the inheritance of specific DNA chains at the mating-type locus (mat1). The recombination event essential for switching is initiated by a site-specific double-strand break at mat1. The switch-activating protein, Sap1, binds in vitro to a mat1 cis-acting site that was shown earlier to be essential for efficient mating-type switching. We isolated the sap1 gene by using oligonucleotides corresponding to the amino acid sequence of purified Sap1 protein. The sequence of that gene predicted a 30-kDa protein with no significant homology to other canonical DNA-binding protein motifs. To facilitate its biochemical characterization, Sap1 was expressed in Escherichia coli. The protein expressed in bacteria displayed the same DNA-binding specificities as the protein purified from S. pombe. Interestingly, analysis of a sap1 null mutation showed that the gene is essential for growth even in a strain in which mating-type switching is prohibited because of a defect in generation of the double-strand break. Thus, the sap1 gene product implicated in mating-type switching is shown to be essential for cell viability.","authors":"Arcangioli B, Copeland TD, Klar AJ","authors_abbrev":"Arcangioli B et al.","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_session_key":"01124f7664962ed7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-28 17:33:34","canto_approved_date":"2022-02-07 19:49:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-23 15:04:52","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-28"},{"uniquename":"PMID:23900842","title":"A physiologically required G protein-coupled receptor (GPCR)-regulator of G protein signaling (RGS) interaction that compartmentalizes RGS activity.","citation":"J Biol Chem 2013 Sep 20;288(38):27327-27342","abstract":"G protein-coupled receptors (GPCRs) can interact with regulator of G protein signaling (RGS) proteins. However, the effects of such interactions on signal transduction and their physiological relevance have been largely undetermined. Ligand-bound GPCRs initiate by promoting exchange of GDP for GTP on the Gα subunit of heterotrimeric G proteins. Signaling is terminated by hydrolysis of GTP to GDP through intrinsic GTPase activity of the Gα subunit, a reaction catalyzed by RGS proteins. Using yeast as a tool to study GPCR signaling in isolation, we define an interaction between the cognate GPCR (Mam2) and RGS (Rgs1), mapping the interaction domains. This reaction tethers Rgs1 at the plasma membrane and is essential for physiological signaling response. In vivo quantitative data inform the development of a kinetic model of the GTPase cycle, which extends previous attempts by including GPCR-RGS interactions. In vivo and in silico data confirm that GPCR-RGS interactions can impose an additional layer of regulation through mediating RGS subcellular localization to compartmentalize RGS activity within a cell, thus highlighting their importance as potential targets to modulate GPCR signaling pathways.","doi":"10.1074/jbc.M113.497826","authors":"Croft W, Hill C, McCann E, Bond M, Esparza-Franco M, Bennett J, Rand D, Davey J, Ladds G","authors_abbrev":"Croft W et al.","pubmed_publication_date":"20 Sep 2013","pubmed_entrez_date":"2013-08-01","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F3.12c","SPAC11H11.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12836412","title":"[Triggering cell mitosis in higher eukaryotes].","citation":"Med Sci (Paris) 2003 Mar;19(3):299-307","abstract":"Dramatic changes of cell organisation occur at onset of mitosis. Genetic analysis of fission yeast and physiological studies of vertebrate and invertebrate oocytes showed that activation of cyclin B-cdc2 kinase triggers mitosis. Nevertheless, upstream mechanisms responsible for this activation remain largely unknown in somatic cells of higher eukaryotes. This review discusses possible pathways and mechanisms involved in triggering onset of mitosis in such cells, including inhibitory checkpoint mechanisms that detect defects in structural organisation of the cell.","authors":"Dorée M","authors_abbrev":"Dorée M","pubmed_publication_date":"Mar 2003","pubmed_entrez_date":"2003-07-03","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26702823","title":"F-BAR/EFC Domain Proteins: Some Assembly Required.","citation":"Dev Cell 2015 Dec 21;35(6):664-6","abstract":"Polymeric spirals of crescent-shaped BAR-domain superfamily proteins are touted to girdle eukaryotic phospholipid bilayers into narrow tubules for trafficking and membrane remodeling events. But McDonald et al. (2015) in this issue of Developmental Cell question whether this broadly held view and conceptually appealing mechanism for membrane sculpting is really overhyped.","doi":"10.1016/j.devcel.2015.12.003","authors":"Traub LM","authors_abbrev":"Traub LM","pubmed_publication_date":"21 Dec 2015","pubmed_entrez_date":"2015-12-26","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-05-19 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10369755","title":"Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis.","citation":"J Mol Biol 1999 Jun 18;289(4):691-9","abstract":"The effects that the inhibitors inositol hexakisphosphate and benzene tri-, tetra- and hexacarboxylates have on the phosphoglycerate mutases from Saccharomyces cerevisiae and Schizosaccharomyces pombe have been determined. Their Kivalues have been calculated, and the ability of the inhibitors to protect the enzymes against limited proteolysis investigated. These biochemical data have been placed in a structural context by the solution of the crystal structures of S. cerevisiae phosphoglycerate mutase soaked with inositol hexakisphosphate or benzene hexacarboxylate. These large polyanionic compounds bind to the enzyme so as to block the entrance to the active-site cleft. They form multiple interactions with the enzyme, consistent with their low Kivalues, and afford good protection against limited proteolysis of the C-terminal region by thermolysin. The inositol compound is more efficacious because of its greater number of negative charges. The S. pombe phosphoglycerate mutase that is inherently lacking a comparable C-terminal region has higher Kivalues for the compounds tested. Moreover, the S. pombe enzyme is less sensititive to proteolysis, and the presence or absence of the inhibitor molecules has little effect on susceptibility to proteolysis.","authors":"Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA","authors_abbrev":"Rigden DJ et al.","pubmed_publication_date":"18 Jun 1999","pubmed_entrez_date":"1999-06-17","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9024686","title":"Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast.","citation":"J Cell Biol 1997 Feb 10;136(3):545-53","abstract":"Saccharomyces cerevisiae cells lacking the MDM12 gene product display temperature-sensitive growth and possess abnormally large, round mitochondria that are defective for inheritance by daughter buds. Analysis of the wild-type MDM12 gene revealed its product to be a 31-kD polypeptide that is homologous to a protein of the fission yeast Schizosaccharomyces pombe. When expressed in S. cerevisiae, the S. pombe Mdm12p homolog conferred a dominant-negative phenotype of giant mitochondria and aberrant mitochondrial distribution, suggesting partial functional conservation of Mdm12p activity between budding and fission yeast. The S. cerevisiae Mdm12p was localized by indirect immunofluorescence microscopy and by subcellular fractionation and immunodetection to the mitochondrial outer membrane and displayed biochemical properties of an integral membrane protein. Mdm12p is the third mitochondrial outer membrane protein required for normal mitochondrial morphology and distribution to be identified in S. cerevisiae and the first such mitochondrial component that is conserved between two different species.","authors":"Berger KH, Sogo LF, Yaffe MP","authors_abbrev":"Berger KH et al.","pubmed_publication_date":"10 Feb 1997","pubmed_entrez_date":"1997-02-10","publication_year":"1997","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.17c","SPBC2F12.13","SPBC28F2.06c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:39601909","title":"Fission yeast Bsd1 is required for ER stress response in Ire1 independent manner.","citation":"Mol Biol Rep 2024 Nov 27;52(1):19","abstract":"Endoplasmic reticulum plays a central role in protein folding and cellular detoxification. NEDD4, a HECT E3 ubiquitin ligase, has been implicated in endoplasmic reticulum stress in humans. In this study, we have explored the role of S. pombe Bsd1, an ortholog of mammalian Ndfip1 (NEDD4 interacting protein 1) in tunicamycin-induced stress response pathway.\nBsd1, an ortholog of mammalian NEDD4 interacting protein 1 (Ndfip1) plays a protective role against tunicamycin-induced ER stress. The confocal microscopy using GFP tagged Bsd1 revealed its localization to the membrane, with a more pronounced signal in the presence of tunicamycin. Additionally, the expression analysis showed a two-fold increase in the expression of Bsd1 after 4 h exposure to tunicamycin. Furthermore, acridine orange/ ethidium bromide staining and MTT assay revealed an increase in apoptotic cell death in bsd1Δ as compared to wild type cells after treatment with ER stressors. Compared to the wild type, we observed punctate FM4-64 staining in bsd1Δ cells in the presence of tunicamycin suggesting a significant loss of vacuolar structures. In a genetic interaction analysis, we observed enhanced sensitivity of tunicamycin in bsd1Δ ire1Δ double mutant as compared to each single mutant, suggesting the role of Bsd1 in the tunicamycin-induced ER stress response might be independent of the Ire1 pathway.\nOur study has implicated the role of fission yeast Bsd1 in ER stress response in an Ire1 independent pathway. Further, we have shown its role in apoptotic cell death and the maintenance of vacuolar structures.","doi":"10.1007/s11033-024-10121-7","authors":"Mahapatra PP, Ahmed S","authors_abbrev":"Mahapatra PP et al.","pubmed_publication_date":"27 Nov 2024","pubmed_entrez_date":"2024-11-27","publication_year":"2024","canto_session_key":"0639ddd6e2750840","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shakil Ahmed","canto_first_approved_date":"2025-01-15 10:57:55","canto_approved_date":"2025-12-11 17:51:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-01-02 10:43:49","canto_added_date":"2024-11-28 00:25:04","annotation_curators":[{"name":"Shakil Ahmed","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC328.07c","SPAC167.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2025-01-15"},{"uniquename":"EMBL:AU009297","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7957098","title":"Fission yeast cut5 links nuclear chromatin and M phase regulator in the replication checkpoint control.","citation":"EMBO J 1994 Nov 15;13(22):5319-29","abstract":"Fission yeast temperature-sensitive cut5 (cell untimely torn) mutants are defective in initiation and/or elongation of DNA replication but allow mitosis and cell division at a restrictive temperature. We show that the cut5 protein (identical to rad4) (i) is an essential component of the replication checkpoint system but not the DNA damage checkpoint, and (ii) negatively regulates the activation of M phase kinase at mitotic entry. Even if the replication checkpoint has been activated previously, cut5 mutations allow mitosis and cell division after shift to 36 degrees C. Transcription of cut5+ is not under the control of the START gene cdc10+. The cut5 protein is enriched in the nucleus, consisting of repeating domains. An essential domain which resembles the proto-oncoprotein Ect2 has a strong negative effect on the entry into mitosis when overexpressed. Expression of the cut5 mutant phenotype requires the function of the M phase regulator genes cdc2+, cdc25+ and cdc13+. The cut5 protein forms a novel, essential link between DNA synthesis and M phase activation in the replication checkpoint control pathway.","authors":"Saka Y, Fantes P, Sutani T, McInerny C, Creanor J, Yanagida M","authors_abbrev":"Saka Y et al.","pubmed_publication_date":"15 Nov 1994","pubmed_entrez_date":"1994-11-15","publication_year":"1994","canto_session_key":"d8cd69d2eda564a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-22 17:06:55","canto_approved_date":"2022-02-24 12:07:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-20 15:00:26","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":27,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPAC24H6.05","SPBC14C8.07c","SPCC16A11.17","SPBC11B10.09","SPCC18B5.03","SPBC582.03","SPAC23C4.18c","SPBC336.12c","SPAC20G8.01"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-12-22"},{"uniquename":"PMID:28287547","title":"Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast.","citation":"J Vis Exp 2017 Feb 20;(120)","abstract":"Cytokinesis, the final step in cell division is critical for maintaining genome integrity. Proper cytokinesis is important for cell differentiation and development. Cytokinesis involves a series of events that are well coordinated in time and space. Cytokinesis involves the formation of an actomyosin ring at the division site, followed by ring constriction, membrane furrow formation and extra cellular matrix remodeling. The fission yeast, Schizosaccharomyces pombe (S. pombe) is a well-studied model system that has revealed with substantial clarity the initial events in cytokinesis. However, we do not understand clearly how different cytokinetic events are coordinated spatiotemporally. To determine this, one needs to analyze the different cytokinetic events in great details in both time and in space. Here we describe a microscopy approach to examine different cytokinetic events in live cells. With this approach it is possible to time different cytokinetic events and determine the time of recruitment of different proteins during cytokinesis. In addition, we describe protocols to compare protein localization, and distribution at the site of cell division. This is a basic protocol to study cytokinesis in fission yeast and can also be used for other yeasts and fungal systems.","doi":"10.3791/55109","authors":"Wei B, Hercyk BS, Habiyaremye J, Das M","authors_abbrev":"Wei B et al.","pubmed_publication_date":"20 Feb 2017","pubmed_entrez_date":"2017-03-14","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-03-15 01:15:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23148219","title":"Insertions within the actin core of actin-related protein 3 (Arp3) modulate branching nucleation by Arp2/3 complex.","citation":"J Biol Chem 2013 Jan 04;288(1):487-97","abstract":"The Arp2/3 (actin-related protein 2/3) complex nucleates branched actin filaments involved in multiple cellular functions, including endocytosis and cellular motility. Two subunits (Arp2 and Arp3) in this seven-subunit assembly are closely related to actin and upon activation of the complex form a \"cryptic dimer\" that stably mimics an actin dimer to nucleate a new filament. Both Arps contain a shared actin core structure, and each Arp contains multiple insertions of unknown function at conserved positions within the core. Here we characterize three key insertions within the actin core of Arp3 and show that each one plays a distinct role in modulating Arp2/3 function. The β4/β5 insert mediates interactions of Arp2/3 complex with actin filaments and \"dampers\" the nucleation activity of the complex. The Arp3 hydrophobic plug plays an important role in maintaining the integrity of the complex but is not absolutely required for formation of the daughter filament nucleus. Deletion of the αK/β15 insert did not constitutively activate the complex, as previously hypothesized. Instead, it abolished in vitro nucleation activity and caused defects in endocytic actin patch assembly in fission yeast, indicating a role for the αK/β15 insert in the activated state of the complex. Biochemical characterization of each mutant revealed steps in the nucleation pathway influenced by each Arp3-specific insert to provide new insights into the structural basis of activation of the complex.","doi":"10.1074/jbc.M112.406744","authors":"Liu SL, May JR, Helgeson LA, Nolen BJ","authors_abbrev":"Liu SL et al.","pubmed_publication_date":"04 Jan 2013","pubmed_entrez_date":"2012-11-14","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.15c","SPAC630.03","SPBC32H8.12c","SPAC11H11.06"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"TreeFam:TF314067","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:6997","SPBC19G7.06","SPAC11E3.06","HGNC:6995","HGNC:6996","HGNC:6993"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8287474","title":"Position effect variegation at fission yeast centromeres.","citation":"Cell 1994 Jan 14;76(1):157-69","abstract":"Chromatin structure at Schizosaccharomyces pombe centromeres is unusual. The insertion of the ura4 gene within these centromeres resulted in genetically identical cells mosaic for its expression. Placement of the ade6 gene within cen1 or cen3 resulted in red-white sectored colonies, demonstrating the instability of gene expression. The occurrence of pink colonies implied that intermediate levels of repression were established. Repression of both genes within centromeres was temperature sensitive. The chromatin structure of the ura4 gene at centromeres was altered, suggesting that the unusual chromatin encroaches into the gene and inhibits normal expression. These repressive effects at S. pombe centromeres resemble the classical phenomenon of position effect variegation imposed by Drosophila heterochromatin on nearby genes. However, since the epigenetic states can be set at intermediate levels of expression, a purely euchromatin-heterochromatin dichotomy does not apply. A model for the epigenetic regulation of genes placed within S. pombe centromeres is presented.","authors":"Allshire RC, Javerzat JP, Redhead NJ, Cranston G","authors_abbrev":"Allshire RC et al.","pubmed_publication_date":"14 Jan 1994","pubmed_entrez_date":"1994-01-14","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21885283","title":"Distinct roles for F-BAR proteins Cdc15p and Bzz1p in actin polymerization at sites of endocytosis in fission yeast.","citation":"Curr Biol 2011 Sep 13;21(17):1450-9","abstract":"Genetic analyses of budding and fission yeast identified >50 proteins that assemble at sites of clathrin-mediated endocytosis in structures called actin patches. These proteins include clathrin, clathrin-interacting proteins, actin binding proteins, and peripheral membrane proteins such as F-BAR proteins. Many questions remain regarding the interactions of these proteins, particularly the participation of F-BAR proteins in the assembly of actin filaments.\nOur microscopic and genetic interaction experiments on fission yeast show that F-BAR proteins Cdc15p and Bzz1p accumulate in two distinct zones on invaginating membrane tubules and interact with Myo1p and Wsp1p, nucleation-promoting factors for Arp2/3 complex. The two F-BAR proteins peak prior to movement of the actin patch and their accumulation in actin patches depends on the nucleation-promoting factors. At their peak local concentrations, we estimated the stoichiometries of the proteins in actin patches to be one Bzz1p per two Wsp1p and one Cdc15p per Myo1p. Purified Bzz1p has two SH3 domains that interact with Wsp1p and stimulate actin polymerization by Arp2/3 complex. Cells lacking either Cdc15p or Bzz1p assemble 3- to 5-fold less actin in patches (in spite of normal levels of Wsp1p, Myo1p, and Arp2/3 complex), and patches move shorter distances from the plasma membrane.\nWe propose that during clathrin-mediated endocytosis, F-BAR proteins interact with nucleation-promoting factors to stimulate Arp2/3 complex in two different zones along the invaginating tubule. We further propose that polymerization of actin filaments in these two zones contributes to membrane scission.","doi":"10.1016/j.cub.2011.07.046","authors":"Arasada R, Pollard TD","authors_abbrev":"Arasada R et al.","pubmed_publication_date":"13 Sep 2011","pubmed_entrez_date":"2011-09-03","publication_year":"2011","canto_session_key":"1c9a3835487bb72e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-11-03 12:54:58","canto_approved_date":"2026-03-23 14:58:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-31 17:28:02","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.16","SPBC11C11.02","SPBC12C2.05c","SPBC32H8.12c","SPBC146.13c","SPAC20G8.05c","SPAC4F10.15c","SPBC4C3.06","SPBC23G7.08c","SPAC13A11.01c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2017-11-03"},{"uniquename":"PMID:28541282","title":"Tailing and degradation of Argonaute-bound small RNAs protect the genome from uncontrolled RNAi.","citation":"Nat Commun 2017 May 25;8:15332","abstract":"RNAi is a conserved mechanism in which small RNAs induce silencing of complementary targets. How Argonaute-bound small RNAs are targeted for degradation is not well understood. We show that the adenyl-transferase Cid14, a member of the TRAMP complex, and the uridyl-transferase Cid16 add non-templated nucleotides to Argonaute-bound small RNAs in fission yeast. The tailing of Argonaute-bound small RNAs recruits the 3'-5' exonuclease Rrp6 to degrade small RNAs. Failure in degradation of Argonaute-bound small RNAs results in accumulation of 'noise' small RNAs on Argonaute and targeting of diverse euchromatic genes by RNAi. To protect themselves from uncontrolled RNAi, cid14Δ cells exploit the RNAi machinery and silence genes essential for RNAi itself, which is required for their viability. Our data indicate that surveillance of Argonaute-bound small RNAs by Cid14/Cid16 and the exosome protects the genome from uncontrolled RNAi and reveal a rapid RNAi-based adaptation to stress conditions.","doi":"10.1038/ncomms15332","authors":"Pisacane P, Halic M","authors_abbrev":"Pisacane P et al.","pubmed_publication_date":"25 May 2017","pubmed_entrez_date":"2017-05-26","publication_year":"2017","canto_session_key":"50f2e165a05393f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mario Halic","canto_first_approved_date":"2018-02-15 16:33:18","canto_approved_date":"2025-11-23 09:25:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-06 10:39:47","canto_added_date":"2017-05-27 00:15:14","annotation_curators":[{"name":"Mario Halic","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC12G12.13c","SPAC17H9.01","SPAC6F12.09","SPCC188.13c","SPCC736.11","SPCC663.12","SPBC29A10.09c","SPAC1F3.01"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-02-15"},{"uniquename":"PMID:38651884","title":"Identification and characterization of a novel antifungal compound tubeimoside I targeting cell wall.","citation":"Microbiol Spectr 2024 Apr 23;:e0404723","abstract":"","doi":"10.1128/spectrum.04047-23","authors":"Liu Q, Zhong Z, Zheng S, Chu Y, Sakamoto N, Kuno T, Fang Y","authors_abbrev":"Liu Q et al.","pubmed_publication_date":"23 Apr 2024","pubmed_entrez_date":"2024-04-23","publication_year":"2024","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2024-04-23 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22083275","title":"N-glycans are not required for the efficient degradation of the mutant Saccharomyces cerevisiae CPY* in Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2012 Feb;93(4):1609-18","abstract":"In eukaryotic cells, aberrant proteins generated in the endoplasmic reticulum (ER) are degraded by the ER-associated degradation (ERAD) pathway. Here, we report on the ERAD pathway of the fission yeast Schizosaccharomyces pombe. We constructed and expressed Saccharomyces cerevisiae wild-type CPY (ScCPY) and CPY-G255R mutant (ScCPY*) in S. pombe. While ScCPY was glycosylated and efficiently transported to the vacuoles in S. pombe, ScCPY* was retained in the ER and was not processed to the matured form in these cells. Cycloheximide chase experiments revealed that ScCPY* was rapidly degraded in S. pombe, and its degradation depended on Hrd1p and Ubc7p homologs. We also found that Mnl1p and Yos9p, proteins that are essential for ERAD in S. cerevisiae, were not required for ScCPY* degradation in S. pombe. Moreover, the null-glycosylation mutant of ScCPY, CPY*0000, was rapidly degraded by the ERAD pathway. These results suggested that N-linked oligosaccharides are not important for the recognition of luminal proteins for ERAD in S. pombe cells.","doi":"10.1007/s00253-011-3662-z","authors":"Mukaiyama H, Kodera M, Tanaka N, Takegawa K","authors_abbrev":"Mukaiyama H et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-11-16","publication_year":"2012","canto_session_key":"52554d50cb755138","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-23 21:22:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-31 15:33:19","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.10c","SPBC28F2.08c","SPBP16F5.04","SPBC17D11.02c","SPBC14F5.07","SPBC365.08c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2015-03-31"},{"uniquename":"PMID:24841299","title":"Targeted gene deletion in Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2014;1163:45-73","abstract":"Gene deletion is an important element in the functional characterization of gene and protein function. Efficient tools for gene deletion have been developed in the model yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, all of which rely on the replacement of the endogenous gene of interest with a selectable marker gene by homologous recombination. In order to minimize incidental recombination events between DNA sequences within the marker gene and a chromosomal sequence, gene deletion cassettes consisting entirely of heterologous DNA sequences are preferred. The gene deletion cassettes, which are composed of the marker gene flanked by short DNA segments homologous to the chromosomal sequences lying to the left and right of the gene to be deleted, are generated by PCR and mediate highly efficient one-step gene deletion events. Incorporation of loxP sites flanking the marker gene allows Cre recombinase-mediated rescue, so that the marker can be reused for the next gene deletion. This is particularly useful for the characterization of gene families in S. cerevisiae. The one-step gene deletion method is not limited to the elimination of individual genes, but can also be used for the removal of chromosomal segments exceeding 100 kbp in length. Here we describe a comprehensive set of gene deletion cassettes and outline their use in S. cerevisiae and S. pombe.","doi":"10.1007/978-1-4939-0799-1_5","authors":"Hegemann JH, Heick SB, Pöhlmann J, Langen MM, Fleig U","authors_abbrev":"Hegemann JH et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-05-21","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20391777","title":"[The alp1-1315 mutation of the tubulin-folding cofactor D gene delays the mitosis initiation in cdc25-22 mutant cells of Schizosaccharomyces pombe].","citation":"Genetika 2010 Mar;46(3):332-9","abstract":"Tubulin-folding cofactor D is necessary for the assembly of tubulin heterodimers and, possibly, plays additional roles in the cell. The effects of cofactor D, microtubules, and/or tubulin dimers on the mitosis initiation were studied in Schizosaccharomyces pombe. It was found for the first time that S. pombe cells with the alp1-1315 and cdc25-22 mutations remained highly viable at 36 degrees C for 8 h, in contrast to cells with the alp1-1315 mutation alone. The progression of cdc25-22 alp1-1315 cells through mitosis after a cell division arrest at 36 degrees C was described. When transferred to 25 degrees C, cdc25-22 alp1-1315 cells displayed a lag of approximately 30 min in Plo1-GFP appearance in the spindle pole body (SPB), 1 h in chromosome condensation, and 75 min in spindle formation. Thus, the initiation of mitosis in cdc25-22 alp1-1315 cells was delayed as compared with cdc25-22 cells. Since treatment of cdc25-22 cells with a microtubule-destabilizing drug during an arrest is known to cause a premitotic arrest with low activity of the mitosis-promoting factor (MPF), it was assumed that an impaired integrity of microtubules and/or lack of tubulin dimers in the nucleus were responsible for the delayed mitosis initiation in cdc25-22 alp1-1315 cells and in cdc25-22 cells treated with a microtubule-destabilizing drug. The progression through mitosis after a cdc25-22 arrest was extremely slow in cdc25-22 alp1-1315 cells, which was attributed to the de novo formation of tubulin dimers.","authors":"Fedianina OS","authors_abbrev":"Fedianina OS","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2010-04-16","publication_year":"2010","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42024429","title":"Mitochondrial NADP+-isocitrate dehydrogenase Idp1 involves CoQ biosynthesis in parallel with NAD kinase Pos5.","citation":"Biosci Biotechnol Biochem 2026 Apr 23;","abstract":"Mitochondrial NADPH is synthesized by isocitrate dehydrogenase (Idp1) from NADP+ and NAD kinase (Pos5) from NADH. Coenzyme Q levels in Schizosaccharomyces pombe were decreased by deletion of idp1 and further lowered by deletion of pos5. The NADP+/NADPH ratio of the ∆idp1 strain shifted to an oxidized state. The mitochondrial NADPH pool and its redox state are critical for CoQ biosynthesis.","doi":"10.1093/bbb/zbag059","authors":"Nishihara S, Matsuo Y, Kawamukai M","authors_abbrev":"Nishihara S et al.","pubmed_publication_date":"23 Apr 2026","pubmed_entrez_date":"2026-04-23","publication_year":"2026","canto_session_key":"04a777c263e3def5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_first_approved_date":"2026-05-22 09:21:48","canto_approved_date":"2026-05-22 09:21:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-05-08 06:59:19","canto_added_date":"2026-04-23 23:25:05","annotation_curators":[{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC323.01c","SPAC56F8.04c","SPAC6G10.08"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2026-05-22"},{"uniquename":"PMID:16950927","title":"Glutathione reductase and a mitochondrial thioredoxin play overlapping roles in maintaining iron-sulfur enzymes in fission yeast.","citation":"Eukaryot Cell 2006 Nov;5(11):1857-65","abstract":"In the fission yeast Schizosaccharomyces pombe, the pgr1+ gene encoding glutathione (GSH) reductase (GR) is essentially required for cell survival. Depletion of GR caused proliferation arrest at the G1 phase of the cell cycle under aerobic conditions. Multicopy suppressors that restore growth were screened, and one effective suppressor was found to be the trx2+ gene, encoding a mitochondrial thioredoxin. This suggests that GR is critically required for some mitochondrial function(s). We found that GR resides in both cytosolic and organellar fractions of the cell. Depletion of GR lowered the respiration rate and the activity of oxidation-labile Fe-S enzymes such as mitochondrial aconitase and cytosolic sulfite reductase. Trx2 did not reverse the high ratio of oxidized glutathione to GSH or the low respiration rate observed in GR-depleted cells. However, it brought the activity of oxidation-labile Fe-S enzymes to a normal level, suggesting that the maintenance of Fe-S enzymes is a critical factor in the survival of S. pombe. The activity of succinate dehydrogenase, an oxidation-insensitive Fe-S enzyme, however, was not affected by GR depletion, suggesting that GR is not required for the biogenesis of the Fe-S cluster. The total iron content was greatly increased by GR depletion and was brought to a nearly normal level by Trx2. These results indicate that the essentiality of GR in the aerobic growth of S. pombe is derived from its role in maintaining oxidation-labile Fe-S enzymes and iron homeostasis.","authors":"Song JY, Cha J, Lee J, Roe JH","authors_abbrev":"Song JY et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-09-05","publication_year":"2006","canto_session_key":"ee61fc6c50ece502","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-02 17:20:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-06 11:15:52","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.07c","SPBC17A3.07","SPAC7D4.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-11-06"},{"uniquename":"PMID:27966061","title":"UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.","citation":"Cell Stress Chaperones 2017 Jan;22(1):143-154","abstract":"As a result of exposure to stress conditions, mutations, or defects during synthesis, cellular proteins are prone to misfold. To cope with such partially denatured proteins, cells mount a regulated transcriptional response involving the Hsf1 transcription factor, which drives the synthesis of molecular chaperones and other stress-relieving proteins. Here, we show that the fission yeast Schizosaccharomyces pombe orthologues of human BAG-1, Bag101, and Bag102, are Hsp70 co-chaperones that associate with 26S proteasomes. Only a subgroup of Hsp70-type chaperones, including Ssa1, Ssa2, and Sks2, binds Bag101 and Bag102 and key residues in the Hsp70 ATPase domains, required for interaction with Bag101 and Bag102, were identified. In humans, BAG-1 overexpression is typically observed in cancers. Overexpression of bag101 and bag102 in fission yeast leads to a strong growth defect caused by triggering Hsp70 to release and activate the Hsf1 transcription factor. Accordingly, the bag101-linked growth defect is alleviated in strains containing a reduced amount of Hsf1 but aggravated in hsp70 deletion strains. In conclusion, we propose that the fission yeast UBL/BAG proteins release Hsf1 from Hsp70, leading to constitutive Hsf1 activation and growth defects.","doi":"10.1007/s12192-016-0751-z","authors":"Poulsen EG, Kampmeyer C, Kriegenburg F, Johansen JV, Hofmann K, Holmberg C, Hartmann-Petersen R","authors_abbrev":"Poulsen EG et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2016-12-15","publication_year":"2017","canto_session_key":"1912f002dd642ee1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_first_approved_date":"2017-01-12 14:57:37","canto_approved_date":"2024-06-09 15:39:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-19 08:54:55","canto_added_date":"2016-12-16 01:19:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":31,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.02c","SPAC13G7.02c","SPCC1739.13","SPBC16G5.11c","SPAC57A7.12","SPBC1709.05","SPBC16D10.08c","SPBP19A11.03c","SPAC2E12.02","SPBC530.03c","SPBC16E9.16c"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2017-01-12"},{"uniquename":"PMID:8536960","title":"Extragenic suppressors of Schizosaccharomyces pombe rad9 mutations uncouple radioresistance and hydroxyurea sensitivity from cell cycle checkpoint control.","citation":"Genetics 1995 Sep;141(1):107-17","abstract":"Schizosaccharomyces pombe cells that contain a mutation within rad9 are sensitive to ionizing radiation, UV light and hydroxyurea, relative to wild-type strains. In addition, the mutants are moderately hypomutable by UV and unable to delay initiation of mitosis after treatment with radiation or hydroxyurea. Three radioresistant derivatives of rad9::ura4 cells were isolated, and each contained a single unique extragenic suppressor responsible for the acquired resistance. The suppressor loci also conferred radioresistance upon cells containing rad9-192, which differs from rad9+ by a single base pair change. The suppressors additionally enhanced the radioresistance of cells containing rad3-136, a mutation that leads to phenotypes similar to those mediated by rad9::ura4. None of the derivatives of rad9::ura4 cells recovered the ability to delay cycling in G2 after exposure to ionizing radiation or UV light. All three suppressor derivatives, relative to the parental rad9::ura4 strain, also exhibited a moderate increase in resistance to the DNA replication inhibitor hydroxyurea without gaining the ability to stop progression into mitosis despite the inhibition of DNA synthesis. Results are discussed in terms of models to explain the putative role of rad9 and the suppressor genes in promoting radioresistance and mediating checkpoint controls responsive to DNA damage or incomplete DNA replication.","authors":"Lieberman HB","authors_abbrev":"Lieberman HB","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.07c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"EMBL:AU007532","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1662986","title":"An additional homolog of the fission yeast cdc25+ gene occurs in humans and is highly expressed in some cancer cells.","citation":"New Biol 1991 Oct;3(10):959-68","abstract":"The gene cdc25+ is a mitotic inducer controlling transition from the G2 to the M phase of the cell cycle in the fission yeast, Schizosaccharomyces pombe. Using phenotypic complementation of a mutant of S. pombe, we have cloned a human homolog (CDC25Hu2) of the cdc25+ gene that differs markedly in structure from CDC25 (referred to here as CDC25Hu1), the first such homolog to be isolated. The carboxyl-terminal region of p63CDC25Hu2 shares significant sequence similarity with cdc25 protein homologs from other eukaryotes and possesses full complementation activity. CDC25Hu2 is expressed in human cell lines 10 to 100 times more than CDC25Hu1, and its expression is particularly high in some cancers, including SV40-transformed fibroblasts. Whereas CDC25Hu1 is predominantly expressed in G2, CDC25Hu2 is expressed throughout the cell cycle with a moderate increase in G2. Thus, at least two homologs of the cdc25 gene exist and are both expressed in human cells. The implications of CDC25Hu2 overexpression in some cancer cells are discussed.","authors":"Nagata A, Igarashi M, Jinno S, Suto K, Okayama H","authors_abbrev":"Nagata A et al.","pubmed_publication_date":"Oct 1991","pubmed_entrez_date":"1991-10-01","publication_year":"1991","canto_session_key":"47296fe85ec80501","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 12:14:24","canto_session_submitted_date":"2012-03-03 12:13:58","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"EMBL:AU009172","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2987072","title":"Hepatic triglyceride lipase and lipoprotein lipase activities in post-heparin plasma of patients with various cancers.","citation":"Jpn J Cancer Res 1985 Mar;76(3):202-7","abstract":"The total post-heparin lipolytic activity (PHLA) and hepatic triglyceride lipase (HTGL) and lipoprotein lipase (LPL) activities in post-heparin plasma of patients with various cancers were measured. In patients with cancers, PHLA was similar to that of controls, but the HTGL activity was decreased and the LPL activity was increased. Thus, in cancer patients the ratios of HTGL to PHLA were lower, and the ratios of LPL to PHLA were higher than in controls. No correlation was found between the plasma lipid level and HTGL or LPL activity.","authors":"Masuno H, Shiosaka T, Itoh Y, Onji M, Ohta Y, Okuda H","authors_abbrev":"Masuno H et al.","pubmed_publication_date":"Mar 1985","pubmed_entrez_date":"1985-03-01","publication_year":"1985","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23H4.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9843572","title":"The protein kinase Cdr2, related to Nim1/Cdr1 mitotic inducer, regulates the onset of mitosis in fission yeast.","citation":"Mol Biol Cell 1998 Dec;9(12):3321-34","abstract":"Cdc2-Cyclin B, the protein kinase that catalyzes the onset of mitosis, is subject to multiple forms of regulation. In the fission yeast Schizosaccharomyces pombe and most other species, a key mode of Cdc2-Cyclin B regulation is the inhibitory phosphorylation of Cdc2 on tyrosine-15. This phosphorylation is catalyzed by the protein kinases Wee1 and Mik1 and removed by the phosphatase Cdc25. These proteins are also regulated, a notable example being the inhibition of Wee1 by the protein kinase Nim1/Cdr1. The temperature-sensitive mutation cdc25-22 is synthetic lethal with nim1/cdr1 mutations, suggesting that a synthetic lethal genetic screen could be used to identify novel mitotic regulators. Here we describe that such a screen has identified cdr2(+), a gene that has an important role in the mitotic control. Cdr2 is a 775 amino acid protein kinase that is closely related to Nim1 and mitotic control proteins in budding yeast. Deletion of cdr2 causes a G2-M delay that is more severe than that caused by nim1/cdr1 mutations. Genetic studies are consistent with a model in which Cdr2 negatively regulates Wee1. This model is supported by experiments showing that Cdr2 associates with the N-terminal regulatory domain of Wee1 in cell lysates and phosphorylates Wee1 in vitro. Thus, Cdr2 is a novel mitotic control protein that appears to regulate Wee1.","authors":"Kanoh J, Russell P","authors_abbrev":"Kanoh J et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1998-12-08","publication_year":"1998","canto_session_key":"55f39e07322aab36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-05-19 22:48:01","canto_approved_date":"2022-08-31 15:14:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-26 13:05:34","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC644.06c","SPAC24H6.05","SPBC11B10.09","SPBC15D4.03","SPAC57A10.02","SPCC18B5.03"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-05-19"},{"uniquename":"PMID:20727920","title":"Human 20α-hydroxysteroid dehydrogenase (AKR1C1)-dependent biotransformation with recombinant fission yeast Schizosaccharomyces pombe.","citation":"J Biotechnol 2010 Oct 01;150(1):161-70","abstract":"While phase I and phase II drug metabolites are important for drug development and toxicity studies, e.g. in the context of metabolites in safety testing (MIST), they are often not commercially available and their classical chemical synthesis can be cumbersome. Therefore, a biotechnological production of drug metabolites using microorganisms that recombinantly express human enzymes has been established in recent years. However, no whole-cell biotransformations that make use of human aldo-keto reductases (AKRs) have yet been reported. In this study, we have functionally expressed human AKR1C1 (20α-hydroxysteroid dehydrogenase) in the fission yeast Schizosaccharomyces pombe and demonstrate the ability of the resulting yeast strain to efficiently catalyze the reduction of progesterone or dydrogesterone to 20α-dihydroprogesterone (20α-DHP) and 20α-dihydrodydrogesterone (20α-DHD), respectively. The formation of any by-products or the occurrence of a back reaction were not detected. Seven other steroids with a 20-keto group (pregnenolone, 17α-hydroxyprogesterone, 11-deoxycortisol, cortisol, 11-deoxycorticosterone, corticosterone, and aldosterone) were not reduced by this system. At shaking flask scale we obtained conversion rates of 90 (±26) μM/d 20α-DHP and 244 (±93) μM/d 20α-dihydrodydrogesterone (20α-DHD), respectively. In a fed-batch fermentation under optimized reaction conditions an average 20α-DHP production rate of 300 μM/d was determined for a total biotransformation time of 72 h. We thus established an AKR-dependent whole-cell biotransformation process that can be used for production of human AKR metabolites on a large scale.","doi":"10.1016/j.jbiotec.2010.08.004","authors":"Naumann JM, Messinger J, Bureik M","authors_abbrev":"Naumann JM et al.","pubmed_publication_date":"01 Oct 2010","pubmed_entrez_date":"2010-08-24","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12711670","title":"The versatile thymine DNA-glycosylase: a comparative characterization of the human, Drosophila and fission yeast orthologs.","citation":"Nucleic Acids Res 2003 May 01;31(9):2261-71","abstract":"Human thymine-DNA glycosylase (TDG) is well known to excise thymine and uracil from G.T and G.U mismatches, respectively, and was therefore proposed to play a central role in the cellular defense against genetic mutation through spontaneous deamination of 5-methylcytosine and cytosine. In this study, we characterized two newly discovered orthologs of TDG, the Drosophila melanogaster Thd1p and the Schizosaccharomyces pombe Thp1p proteins, with an objective to address the function of this subfamily of uracil-DNA glycosylases from an evolutionary perspective. A systematic biochemical comparison of both enzymes with human TDG revealed a number of biologically significant facts. (i) All eukaryotic TDG orthologs have broad and species-specific substrate spectra that include a variety of damaged pyrimidine and purine bases; (ii) the common most efficiently processed substrates of all are uracil and 3,N4- ethenocytosine opposite guanine and 5-fluorouracil in any double-stranded DNA context; (iii) 5-methylcytosine and thymine derivatives are processed with an appreciable efficiency only by the human and the Drosophila enzymes; (iv) none of the proteins is able to hydrolyze a non-damaged 5'-methylcytosine opposite G; and (v) the double strand and mismatch dependency of the enzymes varies with the substrate and is not a stringent feature of this subfamily of DNA glycosylases. These findings advance our current view on the role of TDG proteins and document that they have evolved with high structural flexibility to counter a broad range of DNA base damage in accordance with the specific needs of individual species.","authors":"Hardeland U, Bentele M, Jiricny J, Schär P","authors_abbrev":"Hardeland U et al.","pubmed_publication_date":"01 May 2003","pubmed_entrez_date":"2003-04-25","publication_year":"2003","canto_session_key":"bf60fcf77109a3b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-02 20:54:47","canto_approved_date":"2023-07-02 20:54:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-02 20:54:36","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC965.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-07-02"},{"uniquename":"PMID:19204807","title":"Comparative evolutionary histories of the fungal chitinase gene family reveal non-random size expansions and contractions due to adaptive natural selection.","citation":"Evol Bioinform Online 2008 Mar 18;4:47-60","abstract":"Gene duplication and loss play an important role in the evolution of novel functions and for shaping an organism's gene content. Recently, it was suggested that stress-related genes frequently are exposed to duplications and losses, while growth-related genes show selection against change in copy number. The fungal chitinase gene family constitutes an interesting case study of gene duplication and loss, as their biological roles include growth and development as well as more stress-responsive functions. We used genome sequence data to analyze the size of the chitinase gene family in different fungal taxa, which range from 1 in Batrachochytrium dendrobatidis and Schizosaccharomyces pombe to 20 in Hypocrea jecorina and Emericella nidulans, and to infer their phylogenetic relationships. Novel chitinase subgroups are identified and their phylogenetic relationships with previously known chitinases are discussed. We also employ a stochastic birth and death model to show that the fungal chitinase gene family indeed evolves non-randomly, and we identify six fungal lineages where larger-than-expected expansions (Pezizomycotina, H. jecorina, Gibberella zeae, Uncinocarpus reesii, E. nidulans and Rhizopus oryzae), and two contractions (Coccidioides immitis and S. pombe) potentially indicate the action of adaptive natural selection. The results indicate that antagonistic fungal-fungal interactions are an important process for soil borne ascomycetes, but not for fungal species that are pathogenic in humans. Unicellular growth is correlated with a reduction of chitinase gene copy numbers which emphasizes the requirement of the combined action of several chitinases for filamentous growth.","authors":"Karlsson M, Stenlid J","authors_abbrev":"Karlsson M et al.","pubmed_publication_date":"18 Mar 2008","pubmed_entrez_date":"2009-02-11","publication_year":"2008","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR24341","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:3343","SPAC1F3.07c","HGNC:3342"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:27451393","title":"Role of Inner Nuclear Membrane Protein Complex Lem2-Nur1 in Heterochromatic Gene Silencing.","citation":"J Biol Chem 2016 Sep 16;291(38):20021-9","abstract":"Heterochromatin in the fission yeast Schizosaccharomyces pombe is clustered at the nuclear periphery and interacts with a number of nuclear membrane proteins. However, the significance and the factors that sequester heterochromatin at the nuclear periphery are not fully known. Here, we report that an inner nuclear membrane protein complex Lem2-Nur1 is essential for heterochromatin-mediated gene silencing. We found that Lem2 is physically associated with another inner nuclear membrane protein, Nur1, and deletion of either lem2 or nur1 causes silencing defect at centromeres, telomeres, and rDNA loci. We analyzed the genome-wide association of Lem2 using ChIP sequencing and we found that it binds to the central core region of centromeres, in striking contrast to Chp1, a component of pericentromeric heterochromatin, which binds H3K9me-rich chromatin in neighboring sequences. The recruitment of Lem2 and Nur1 to silent regions of the genome is dependent on H3K9 methyltransferase, Clr4. Finally, we show that the Lem2-Nur1 complex regulates the local balance between the underln]Snf2/HDAC-containing repressor complex (SHREC) histone deacetylase complex and the anti-silencing protein Epe1. These findings uncover a novel role for Lem2-Nur1 as a key functional link between localization at the nuclear periphery and heterochromatin-mediated gene silencing.","doi":"10.1074/jbc.M116.743211","authors":"Banday S, Farooq Z, Rashid R, Abdullah E, Altaf M","authors_abbrev":"Banday S et al.","pubmed_publication_date":"16 Sep 2016","pubmed_entrez_date":"2016-07-25","publication_year":"2016","canto_session_key":"a8575ebe13d91e58","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-02-01 08:39:07","canto_approved_date":"2022-07-29 14:32:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-30 18:15:04","canto_added_date":"2016-07-29 00:15:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPCC4G3.11","SPBC2D10.17","SPAC18G6.10","SPCC622.16c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2018-02-01"},{"uniquename":"PMID:41218563","title":"Responses to nutrient starvation in the fission yeast Schizosaccharomyces pombe.","citation":"Microbiol Res 2025 Nov 07;303:128387","abstract":"In nature, nutrient-poor environments are more common than exposure to nutrient-rich environments, and living organisms have developed countermeasures to survive nutrient starvation. Increasing research has revealed beneficial aspects of starvation for an individual's life, including lifespan extension. The fission yeast Schizosaccharomyces pombe is a model unicellular eukaryotic organism and has greatly contributed to the understanding of various cellular processes, including the cell cycle, cell morphology, sexual development, cell lifespan, and nutritional responses. Traditionally, research on starvation in fission yeast has focused on glucose starvation and nitrogen starvation. Recently, studies on cellular responses to the starvation of various nutrients, such as phosphorus, sulfur, iron, zinc, copper, and amino acids have been reported, revealing similarities and differences among the various types of nutrient starvation. In fission yeast, Ecl proteins, which are conserved among fungi, can sense the starvation of multiple nutrients. These proteins also repress the target of rapamycin complex 1 (TORC1), which is conserved across eukaryotes. They channel a variety of starvation signals into common cellular responses, such as growth arrest, sexual differentiation, autophagy, and lifespan extension. This review summarizes and discusses the signaling mechanisms involved in the initial cellular responses of fission yeast to the starvation of various nutrients.","doi":"10.1016/j.micres.2025.128387","authors":"Ohtsuka H, Shimasaki T, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"07 Nov 2025","pubmed_entrez_date":"2025-11-11","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-11-13 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7867797","title":"The use of mass spectrometry to examine the formation and hydrolysis of the phosphorylated form of phosphoglycerate mutase.","citation":"FEBS Lett 1995 Feb 13;359(2-3):192-4","abstract":"Electrospray mass spectrometry has been used to study the formation and hydrolysis of the phosphorylated forms of two phosphoglycerate mutases. The half-life of the enzyme from Saccharomyces cerevisiae was 35 min at 20 degrees C in 10 mM ammonium bicarbonate, pH 8.0. Addition of 1 mM 2-phosphoglycollate reduced this value by at least 100-fold. The phosphorylated form of the enzyme from Schizosaccharomyces pombe was much less stable with a half-life of less than 1 min. The results are discussed in terms of the kinetic properties of the enzymes. Mass spectrometry would appear to be a powerful method to study the formation and breakdown of phosphorylated proteins, processes which are of widespread significance in regulatory mechanisms.","authors":"Nairn J, Krell T, Coggins JR, Pitt AR, Fothergill-Gilmore LA, Walter R, Price NC","authors_abbrev":"Nairn J et al.","pubmed_publication_date":"13 Feb 1995","pubmed_entrez_date":"1995-02-13","publication_year":"1995","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30420864","title":"A Critical Assessment of 60 Years of Maize Intragenic Recombination.","citation":"Front Plant Sci 2018;9:1560","abstract":"Until the mid-1950s, it was believed that genetic crossovers did not occur within genes. Crossovers occurred between genes, the \"beads on a string\" model. Then in 1956, Seymour Benzer published his classic paper describing crossing over within a gene, intragenic recombination. This result from a bacteriophage gene prompted Oliver Nelson to study intragenic recombination in the maize  Waxy  locus. His studies along with subsequent work by others working with maize and other organisms described the outcomes of intragenic recombination and provided some of the earliest evidence that genes, not intergenic regions, were recombination hotspots. High-throughput genotyping approaches have since replaced single gene intragenic studies for characterizing the outcomes of recombination. These large-scale studies confirm that genes, or more generally genic regions, are the most active recombinogenic regions, and suggested a pattern of crossovers similar to the budding yeast  Saccharomyces cerevisiae . In  S. cerevisiae  recombination is initiated by double-strand breaks (DSBs) near transcription start sites (TSSs) of genes producing a polarity gradient where crossovers preferentially resolve at the 5' end of genes. Intragenic studies in maize yielded less evidence for either polarity or for DSBs near TSSs initiating recombination and in certain respects resembled  Schizosaccharomyces pombe  or mouse. These different perspectives highlight the need to draw upon the strengths of different approaches and caution against relying on a single model system or approach for understanding recombination.","doi":"10.3389/fpls.2018.01560","authors":"Okagaki RJ, Dukowic-Schulze S, Eggleston WB, Muehlbauer GJ","authors_abbrev":"Okagaki RJ et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-11-14","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-15 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25807481","title":"The Paf1 complex represses small-RNA-mediated epigenetic gene silencing.","citation":"Nature 2015 Apr 09;520(7546):248-252","abstract":"RNA interference (RNAi) refers to the ability of exogenously introduced double-stranded RNA to silence expression of homologous sequences. Silencing is initiated when the enzyme Dicer processes the double-stranded RNA into small interfering RNAs (siRNAs). Small RNA molecules are incorporated into Argonaute-protein-containing effector complexes, which they guide to complementary targets to mediate different types of gene silencing, specifically post-transcriptional gene silencing and chromatin-dependent gene silencing. Although endogenous small RNAs have crucial roles in chromatin-mediated processes across kingdoms, efforts to initiate chromatin modifications in trans by using siRNAs have been inherently difficult to achieve in all eukaryotic cells. Using fission yeast, here we show that RNAi-directed heterochromatin formation is negatively controlled by the highly conserved RNA polymerase-associated factor 1 complex (Paf1C). Temporary expression of a synthetic hairpin RNA in Paf1C mutants triggers stable heterochromatin formation at homologous loci, effectively silencing genes in trans. This repressed state is propagated across generations by the continual production of secondary siRNAs, independently of the synthetic hairpin RNA. Our data support a model in which Paf1C prevents targeting of nascent transcripts by the siRNA-containing RNA-induced transcriptional silencing complex and thereby epigenetic gene silencing, by promoting efficient transcription termination and rapid release of the RNA from the site of transcription. We show that although compromised transcription termination is sufficient to initiate the formation of bi-stable heterochromatin by trans-acting siRNAs, impairment of both transcription termination and nascent transcript release is imperative to confer stability to the repressed state. Our work uncovers a novel mechanism for small-RNA-mediated epigenome regulation and highlights fundamental roles for Paf1C and the RNAi machinery in building epigenetic memory.","doi":"10.1038/nature14337","authors":"Kowalik KM, Shimada Y, Flury V, Stadler MB, Batki J, Bühler M","authors_abbrev":"Kowalik KM et al.","pubmed_publication_date":"09 Apr 2015","pubmed_entrez_date":"2015-03-26","publication_year":"2015","canto_session_key":"b0df891c82756b72","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-27 01:15:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11152071","title":"Differential uptake of fumarate by Candida utilis and Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2000 Dec;54(6):792-8","abstract":"The dicarboxylic acid fumarate is an important intermediate in cellular processes and also serves as a precursor for the commercial production of fine chemicals such as L-malate. Yeast species differ remarkably in their ability to degrade extracellular dicarboxylic acids and to utilise them as their only source of carbon. In this study we have shown that the yeast Candida utilis effectively degraded extracellular fumarate and L-malate, but glucose or other assimilable carbon sources repressed the transport and degradation of these dicarboxylic acids. The transport of both dicarboxylic acids was shown to be strongly inducible by either fumarate or L-malate while kinetic studies suggest that the two dicarboxylic acids are transported by the same transporter protein. In contrast, Schizosaccharomyces pombe effectively degraded extracellular L-malate, but not fumarate, in the presence of glucose or other assimilable carbon sources. The Sch. pombe malate transporter was unable to transport fumarate, although fumarate inhibited the uptake of L-malate.","authors":"Saayman M, van Vuuren HJ, van Zyl WH, Viljoen-Bloom M","authors_abbrev":"Saayman M et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2001-01-11","publication_year":"2000","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26243668","title":"Mto2 multisite phosphorylation inactivates non-spindle microtubule nucleation complexes during mitosis.","citation":"Nat Commun 2015 Aug 05;6:7929","abstract":"Microtubule nucleation is highly regulated during the eukaryotic cell cycle, but the underlying molecular mechanisms are largely unknown. During mitosis in fission yeast Schizosaccharomyces pombe, cytoplasmic microtubule nucleation ceases simultaneously with intranuclear mitotic spindle assembly. Cytoplasmic nucleation depends on the Mto1/2 complex, which binds and activates the γ-tubulin complex and also recruits the γ-tubulin complex to both centrosomal (spindle pole body) and non-centrosomal sites. Here we show that the Mto1/2 complex disassembles during mitosis, coincident with hyperphosphorylation of Mto2 protein. By mapping and mutating multiple Mto2 phosphorylation sites, we generate mto2-phosphomutant strains with enhanced Mto1/2 complex stability, interaction with the γ-tubulin complex and microtubule nucleation activity. A mutant with 24 phosphorylation sites mutated to alanine, mto2[24A], retains interphase-like behaviour even in mitotic cells. This provides a molecular-level understanding of how phosphorylation 'switches off' microtubule nucleation complexes during the cell cycle and, more broadly, illuminates mechanisms regulating non-centrosomal microtubule nucleation.","doi":"10.1038/ncomms8929","authors":"Borek WE, Groocock LM, Samejima I, Zou J, de Lima Alves F, Rappsilber J, Sawin KE","authors_abbrev":"Borek WE et al.","pubmed_publication_date":"05 Aug 2015","pubmed_entrez_date":"2015-08-06","publication_year":"2015","canto_session_key":"2e55ad5ebdc74411","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-07 00:20:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC902.06","SPCC417.07c","SPBC32F12.04"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11172711","title":"The fission yeast Taz1 protein protects chromosomes from Ku-dependent end-to-end fusions.","citation":"Mol Cell 2001 Jan;7(1):55-63","abstract":"A paramount role of telomeres is to prevent chromosome fusions. The fission yeast Taz1 protein regulates diverse telomere functions but is not essential for growth under stress-free conditions. Strikingly, however, taz1(-) cells exhibit lethal telomere fusions when subjected to nitrogen starvation, a treatment that induces an uncommitted G1 state. These fusions are formed by Ku-dependent nonhomologous end joining. Fusions also occur during normal growth in taz1(-) cells that lack rad22(+), a gene involved in homologous recombination. Our data suggest a model whereby taz1(-) telomeres are exposed to the prevailing mode of DNA repair, which is dictated by the cell cycle. Thus, Taz1 caps chromosome ends and provides the telomerespecific interaction that prevents Ku from treating telomeres as double-strand breaks.","authors":"Ferreira MG, Cooper JP","authors_abbrev":"Ferreira MG et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-02-15","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1183.05c","SPAC30D11.10","SPAC16A10.07c","SPCC126.02c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:36370456","title":"The cohesin complex of yeasts: sister chromatid cohesion and beyond.","citation":"FEMS Microbiol Rev 2023 Jan 16;47(1)","abstract":"Each time a cell divides, it needs to duplicate the genome and then separate the two copies. In eukaryotes, which usually have more than one linear chromosome, this entails tethering the two newly replicated DNA molecules, a phenomenon known as sister chromatid cohesion (SCC). Cohesion ensures proper chromosome segregation to separate poles during mitosis. SCC is achieved by the presence of the cohesin complex. Besides its canonical function, cohesin is essential for chromosome organization and DNA damage repair. Surprisingly, yeast cohesin is loaded in G1 before DNA replication starts but only acquires its binding activity during DNA replication. Work in microorganisms, such as Saccharomyces cerevisiae and Schizosaccharomyces pombe has greatly contributed to the understanding of cohesin composition and functions. In the last few years, much progress has been made in elucidating the role of cohesin in chromosome organization and compaction. Here, we discuss the different functions of cohesin to ensure faithful chromosome segregation and genome stability during the mitotic cell division in yeast. We describe what is known about its composition and how DNA replication is coupled with SCC establishment. We also discuss current models for the role of cohesin in chromatin loop extrusion and delineate unanswered questions about the activity of this important, conserved complex.","doi":"10.1093/femsre/fuac045","authors":"Choudhary K, Kupiec M","authors_abbrev":"Choudhary K et al.","pubmed_publication_date":"16 Jan 2023","pubmed_entrez_date":"2022-11-12","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-11-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.11","SPAC694.06c","SPBC902.02c","SPBC947.11c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:4998252","title":"Inhibition of mitochondrial protein synthesis in vivo by erythromycin in Schizosaccharomyces pombe and Saccharomyces cerevisiae.","citation":"Mol Gen Genet 1971;111(3):235-41","abstract":"","authors":"Michel R, Schweyen RJ, Kaudewitz F","authors_abbrev":"Michel R et al.","pubmed_publication_date":"1971","pubmed_entrez_date":"1971-01-01","publication_year":"1971","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26583750","title":"The ATPases of cohesin interface with regulators to modulate cohesin-mediated DNA tethering.","citation":"Elife 2015 Nov 19;4","abstract":"Cohesin tethers together regions of DNA, thereby mediating higher order chromatin organization that is critical for sister chromatid cohesion, DNA repair and transcriptional regulation. Cohesin contains a heterodimeric ATP-binding Cassette (ABC) ATPase comprised of Smc1 and Smc3 ATPase active sites. These ATPases are required for cohesin to bind DNA. Cohesin's DNA binding activity is also promoted by the Eco1 acetyltransferase and inhibited by Wpl1. Recently we showed that after cohesin stably binds DNA, a second step is required for DNA tethering. This second step is also controlled by Eco1 acetylation. Here, we use genetic and biochemical analyses to show that this second DNA tethering step is regulated by cohesin ATPase. Furthermore, our results also suggest that Eco1 promotes cohesion by modulating the ATPase cycle of DNA-bound cohesin in a state that is permissive for DNA tethering and refractory to Wpl1 inhibition.","doi":"10.7554/eLife.11315","authors":"Çamdere G, Guacci V, Stricklin J, Koshland D","authors_abbrev":"Çamdere G et al.","pubmed_publication_date":"19 Nov 2015","pubmed_entrez_date":"2015-11-20","publication_year":"2015","canto_session_key":"ba190692ba0c52c8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-06-26 16:51:39","canto_approved_date":"2024-03-28 17:40:56","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-09-01 10:51:50","canto_added_date":"2015-11-21 01:19:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.20","SPBC29A10.04","SPCC338.17c","SPAC31A2.05c","SPAC1687.18c","SPAC10F6.09c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-06-26"},{"uniquename":"PMID:22497938","title":"Microtubule organization: a pericentriolar material-like structure in yeast meiosis.","citation":"Curr Biol 2012 Apr 10;22(7):R229-31","abstract":"During meiotic prophase in fission yeast, the nucleus undergoes dramatic oscillatory movements. A newly identified structure, the radial microtubule organizing center (rMTOC), mediates these movements and shares some of the features of the pericentriolar material in higher eukaryotes.","doi":"10.1016/j.cub.2012.02.036","authors":"Dammermann A, Cipak L, Gregan J","authors_abbrev":"Dammermann A et al.","pubmed_publication_date":"10 Apr 2012","pubmed_entrez_date":"2012-04-14","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41413211","title":"Histone H2B monoubiquitylation regulates elongation-to-termination transition in RNA polymerase II transcription.","citation":"Commun Biol 2025 Dec 18;8(1):1781","abstract":"RNA Polymerase II (Pol II) transcription is tightly regulated across initiation, elongation, and termination, with key transitions at initiation-to-elongation and elongation-to-termination. While elongation and termination are well-studied, their transition remains unclear. Using chromatin immunoprecipitation (ChIP) and sequencing, we show in Schizosaccharomyces pombe that Cdk9, with its cyclin partner Pch1, disengages from the elongation complex as Pol II nears the cleavage and polyadenylation signal (CPS), while Dis2 (PP1 ortholog) binding increases beyond the CPS, showing an inverse relationship with Cdk9. ChIP-seq analysis reveals histone H2B monoubiquitylation (H2Bub1) regulates Cdk9 occupancy, promoting its recruitment during elongation and dissociation at the CPS, mirroring pSpt5 distribution. Dis2, a pSpt5 phosphatase, exhibits an inverse pattern, decreasing with H2Bub1 loss (htb1-K119R) and increasing with persistent H2Bub1 (ubp8Δ). H2Bub1 perturbations inversely affect Pol II CTD Tyr1/Ser2 phosphorylation, Ser2 kinase Lsk1, mRNA 3'-end processing factors (Pfs2, Pla1), and termination factors (Rhn1, Pcf11)-H2Bub1 loss reduces recruitment, while its persistence enhances occupancy. These findings align with a model in which H2Bub1 loss disrupts termination, whereas its sustained presence reinforces it. Collectively, our findings suggest that H2Bub1-mediated Cdk9 eviction at the CPS facilitates Dis2 binding, pSpt5 dephosphorylation, Pol II slowing, and efficient termination, revealing a yet unknown regulatory paradigm in transcription.","doi":"10.1038/s42003-025-09196-0","authors":"Bandyopadhyay T, Basu B, Parua PK","authors_abbrev":"Bandyopadhyay T et al.","pubmed_publication_date":"18 Dec 2025","pubmed_entrez_date":"2025-12-18","publication_year":"2025","canto_session_key":"3987075b9563871b","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-20 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3287619","title":"Yeast: an experimental organism for modern biology.","citation":"Science 1988 Jun 10;240(4858):1439-43","abstract":"The yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe have become popular and successful model systems for understanding eukaryotic biology at the cellular and molecular levels. The reasons for this success are experimental tractability, especially in applying classical and molecular genetic methods to associate genes with proteins and functions within the cell.","authors":"Botstein D, Fink GR","authors_abbrev":"Botstein D et al.","pubmed_publication_date":"10 Jun 1988","pubmed_entrez_date":"1988-06-10","publication_year":"1988","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22437499","title":"Structure of the mitotic checkpoint complex.","citation":"Nature 2012 Mar 21;484(7393):208-13","abstract":"In mitosis, the spindle assembly checkpoint (SAC) ensures genome stability by delaying chromosome segregation until all sister chromatids have achieved bipolar attachment to the mitotic spindle. The SAC is imposed by the mitotic checkpoint complex (MCC), whose assembly is catalysed by unattached chromosomes and which binds and inhibits the anaphase-promoting complex/cyclosome (APC/C), the E3 ubiquitin ligase that initiates chromosome segregation. Here, using the crystal structure of Schizosaccharomyces pombe MCC (a complex of mitotic spindle assembly checkpoint proteins Mad2, Mad3 and APC/C co-activator protein Cdc20), we reveal the molecular basis of MCC-mediated APC/C inhibition and the regulation of MCC assembly. The MCC inhibits the APC/C by obstructing degron recognition sites on Cdc20 (the substrate recruitment subunit of the APC/C) and displacing Cdc20 to disrupt formation of a bipartite D-box receptor with the APC/C subunit Apc10. Mad2, in the closed conformation (C-Mad2), stabilizes the complex by optimally positioning the Mad3 KEN-box degron to bind Cdc20. Mad3 and p31(comet) (also known as MAD2L1-binding protein) compete for the same C-Mad2 interface, which explains how p31(comet) disrupts MCC assembly to antagonize the SAC. This study shows how APC/C inhibition is coupled to degron recognition by co-activators.","doi":"10.1038/nature10896","authors":"Chao WC, Kulkarni K, Zhang Z, Kong EH, Barford D","authors_abbrev":"Chao WC et al.","pubmed_publication_date":"21 Mar 2012","pubmed_entrez_date":"2012-03-23","publication_year":"2012","canto_session_key":"ad3bb22deefbbb4b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-11-29 08:06:23","canto_approved_date":"2025-12-16 18:53:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-28 19:22:48","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.08c","SPCC1795.01c","SPBC20F10.06","SPAC23H3.08c","SPBC3D6.04c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2024-11-29","pdb_entries":[{"pdb_id":"4aez","gene_chains":[{"gene_uniquename":"SPBC20F10.06","chain":"B/E/H","position":"1-203"},{"gene_uniquename":"SPCC1795.01c","chain":"C/F/I","position":"1-223"},{"gene_uniquename":"SPAC821.08c","chain":"A/D/G","position":"88-488"}],"title":"Crystal Structure of Mitotic Checkpoint Complex","entry_authors":"Kulkarni KA,Chao WCH,Zhang Z,Barford D","entry_authors_abbrev":"Kulkarni KA et al.","reference_uniquename":"PMID:22437499","experimental_method":"X-ray","resolution":"2.3"}]},{"uniquename":"PMID:23485968","title":"A conformational switch in HP1 releases auto-inhibition to drive heterochromatin assembly.","citation":"Nature 2013 Apr 18;496(7445):377-81","abstract":"A hallmark of histone H3 lysine 9 (H3K9)-methylated heterochromatin, conserved from the fission yeast Schizosaccharomyces pombe to humans, is its ability to spread to adjacent genomic regions. Central to heterochromatin spread is heterochromatin protein 1 (HP1), which recognizes H3K9-methylated chromatin, oligomerizes and forms a versatile platform that participates in diverse nuclear functions, ranging from gene silencing to chromosome segregation. How HP1 proteins assemble on methylated nucleosomal templates and how the HP1-nucleosome complex achieves functional versatility remain poorly understood. Here we show that binding of the key S. pombe HP1 protein, Swi6, to methylated nucleosomes drives a switch from an auto-inhibited state to a spreading-competent state. In the auto-inhibited state, a histone-mimic sequence in one Swi6 monomer blocks methyl-mark recognition by the chromodomain of another monomer. Auto-inhibition is relieved by recognition of two template features, the H3K9 methyl mark and nucleosomal DNA. Cryo-electron-microscopy-based reconstruction of the Swi6-nucleosome complex provides the overall architecture of the spreading-competent state in which two unbound chromodomain sticky ends appear exposed. Disruption of the switch between the auto-inhibited and spreading-competent states disrupts heterochromatin assembly and gene silencing in vivo. These findings are reminiscent of other conditionally activated polymerization processes, such as actin nucleation, and open up a new class of regulatory mechanisms that operate on chromatin in vivo.","doi":"10.1038/nature12032","authors":"Canzio D, Liao M, Naber N, Pate E, Larson A, Wu S, Marina DB, Garcia JF, Madhani HD, Cooke R, Schuck P, Cheng Y, Narlikar GJ","authors_abbrev":"Canzio D et al.","pubmed_publication_date":"18 Apr 2013","pubmed_entrez_date":"2013-03-15","publication_year":"2013","canto_session_key":"bb91629881ce3356","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3442819","title":"Molecular cloning of a ribosomal protein gene from the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1986;10(5):365-70","abstract":"Using the structural gene for the ribosomal protein L3 from Saccharomyces cerevisiae as a probe, we isolated a homologous fragment from genomic DNA of Schizosaccharomyces pombe. Analysis of the plasmid carrying this fragment by hybridization selection and 2D-electrophoresis revealed a 31 kDa ribosomal protein. Transformation of the vector pDB248x containing this fragment into Schizosaccharomyces pombe leads to an increased level of mRNA suggesting that we have cloned the entire and actively transcribed gene.","authors":"Nischt R, Thüroff E, Küfer NF","authors_abbrev":"Nischt R et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_session_key":"30ff0b6f66c4e312","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-02-26 14:55:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-02-26 14:55:01","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-02-26"},{"uniquename":"PMID:9620780","title":"The chromo and SET domains of the Clr4 protein are essential for silencing in fission yeast.","citation":"Nat Genet 1998 Jun;19(2):192-5","abstract":"Heritable inactivation of specific regions of the genome is a widespread, possibly universal phenomenon for gene regulation in eukaryotes. Self-perpetuating, clonally inherited chromatin structure has been proposed as the explanation for such phenomena as position-effect variegation (PEV) and control of segment determination and differentiation in flies, X-chromosome inactivation and parental imprinting in mammals, gene silencing by paramutation in maize and silencing of the mating-type loci in yeasts. We have now found that the clr4 gene, which is essential for silencing of centromeres and the mating-type loci in Schizosaccharomyces pombe, encodes a protein with high homology to the product of Su(var)3-9, a gene affecting PEV in Drosophila. Like Su(var)3-9p, Clr4p contains SET and chromo domains, motifs found in proteins that modulate chromatin structure. Site-directed mutations in the conserved residues of the chromo domain confirm that it is required for proper silencing and directional switching of the mating type, like SET domain. Surprisingly, RNA differential display experiments demonstrated that clr4+ can mediate transcriptional activation of certain other loci. These results show that clr4 plays a critical role in silencing at mating-type loci and centromeres through the organization of repressive chromatin structure and demonstrate a new, activator function for Clr4p.","authors":"Ivanova AV, Bonaduce MJ, Ivanov SV, Klar AJ","authors_abbrev":"Ivanova AV et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-06-10","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23576550","title":"The dual role of fission yeast Tbc1/cofactor C orchestrates microtubule homeostasis in tubulin folding and acts as a GAP for GTPase Alp41/Arl2.","citation":"Mol Biol Cell 2013 Jun;24(11):1713-24, S1-8","abstract":"Supplying the appropriate amount of correctly folded α/β-tubulin heterodimers is critical for microtubule dynamics. Formation of assembly-competent heterodimers is remarkably elaborate at the molecular level, in which the α- and β-tubulins are separately processed in a chaperone-dependent manner. This sequential step is performed by the tubulin-folding cofactor pathway, comprising a specific set of regulatory proteins: cofactors A-E. We identified the fission yeast cofactor: the orthologue of cofactor C, Tbc1. In addition to its roles in tubulin folding, Tbc1 acts as a GAP in regulating Alp41/Arl2, a highly conserved small GTPase. Of interest, the expression of GDP- or GTP-bound Alp41 showed the identical microtubule loss phenotype, suggesting that continuous cycling between these forms is important for its functions. In addition, we found that Alp41 interacts with Alp1(D), the orthologue of cofactor D, specifically when in the GDP-bound form. Intriguingly, Alp1(D) colocalizes with microtubules when in excess, eventually leading to depolymerization, which is sequestered by co-overproducing GDP-bound Alp41. We present a model of the final stages of the tubulin cofactor pathway that includes a dual role for both Tbc1 and Alp1(D) in opposing regulation of the microtubule.","doi":"10.1091/mbc.E12-11-0792","authors":"Mori R, Toda T","authors_abbrev":"Mori R et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-04-12","publication_year":"2013","canto_session_key":"a2c14f18afef292a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2015-08-25 13:31:13","canto_approved_date":"2026-02-01 09:50:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-20 06:54:12","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Takashi Toda","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.05c","SPBC800.05c","SPBC16A3.15c","SPAC1786.03","SPBC11C11.04c","SPAC328.08c","SPAC22H10.10"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2015-08-25"},{"uniquename":"PMID:28171751","title":"Response to Zambon et al.","citation":"Curr Biol 2017 Feb 06;27(3):R101-R102","abstract":"Stimulated by our 2015 Current Biology paper [1], Zambon et al. reinvestigated how three myosin isoforms participate in the formation and constriction of the contractile ring in fission yeast. Our paper presented evidence that these myosin isoforms have distinct roles: \"Conventional myosin-II Myo2 is crucial to ring assembly, unconventional myosin-II Myp2 is most important for ring constriction, and type V myosin Myo51 aids the other two myosins.\" Zambon et al. used different markers to reexamine the contributions of the three myosins to cytokinesis and concluded \"that Myo2p is the major motor involved in ring contraction in S. pombe.\" Here, we show that most of the differences observed by Zambon et al. can be attributed to their use of the Rlc1p-3GFP marker, which genetically interacts with myo2-E1.","doi":"10.1016/j.cub.2016.12.025","authors":"Laplante C, Pollard TD","authors_abbrev":"Laplante C et al.","pubmed_publication_date":"06 Feb 2017","pubmed_entrez_date":"2017-02-08","publication_year":"2017","canto_session_key":"2e412f93fc3a909d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-10 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30099677","title":"Genome-wide evidences of bisphenol a toxicity using Schizosaccharomyces pombe.","citation":"Arch Pharm Res 2018 Aug;41(8):830-837","abstract":"To clarify reliable toxic mechanisms of bisphenol A (BPA), an endocrine disrupting chemical, we approached an alternative animal and whole genome analyses with the yeast knockout library (YKO) of Schizosaccharomyces pombe. As results, the 50% growth inhibition concentrations (GI 50 ) of BPA was approximately 600 μM and the YKO-three step screening revealed the top 10 target candidate genes including dbp2, utp18, srs1, tif224, use1, qcr1, etc. The screening results were confirmed in human embryonic stem cell (hES)-derived hepatic cells and HepG2 human liver cancer cells. We found BPA down-regulated UQCRC, the human orthlog of S. pombe- qcr1, as a part of the mitochondrial respiratory chain, in HepG2 cells and hESs during cell differentiation into hepatic cells. Therefore, BPA may induce mitochondrial dysfunction and disruption of differentiation by suppressing UQCRC1.","doi":"10.1007/s12272-018-1058-7","authors":"Kim DM, Heo J, Lee DW, Tsuji M, Yang M","authors_abbrev":"Kim DM et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-08-13","publication_year":"2018","canto_session_key":"76cdad6ff72bfdb0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-09-24 15:43:48","canto_approved_date":"2018-09-24 15:43:48","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-09-24 15:43:41","canto_added_date":"2018-08-15 00:15:04","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_30099677_phaf.tsv"}],"genes":["SPBC839.09c","SPAC1F7.03","SPBC119.17","SPAC26H5.13c","SPBC23E6.06c","SPAC18G6.14c","SPCC16C4.18c","SPBC1271.13","SPBC646.07c","SPAC23C11.09","SPCC191.02c","SPAP27G11.13c","SPAC21E11.06","SPCC18.05c","SPAC1B3.18c","SPBC106.06","SPAC1B1.03c","SPCC4G3.07c","SPAC21E11.07","SPAC2F3.04c","SPAC29A4.15","SPAC343.14c","SPBC29A3.06","SPAC17G6.07c","SPBC3B9.02c","SPBP23A10.15c","SPBP8B7.16c","SPAC17C9.13c"],"gene_count":28,"ltp_gene_count":0,"approved_date":"2018-09-24"},{"uniquename":"PMID:16176106","title":"[Expression of SARS spike gene in Shizomycete pombe].","citation":"Sheng Wu Gong Cheng Xue Bao 2005 Jul;21(4):638-41","abstract":"The viral spike protein is the main surface antigen of the coronavirus, and it could be useful in the research of clinical diagnosis, SARS vaccine and the structure biology.According to the analysis of the main antigen of the SARS spike protein, 5 fragments of the whole spike gene were cloned, and ligated to the vector pNMT1. Through electroporation transformantion to TCP1, the recombinant S. pombe strains capable of expressing the 5 fragments were constructed. SDS-PAGE or Western blot analysis of the induced expression products demonstrated that the 5 recombinant proteins were expressed in the fission yeast respectively.","authors":"Wu ZX, Zheng WL, Zhang B, Shi YX, Wen-Li","authors_abbrev":"Wu ZX et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-09-24","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17508131","title":"Isolation of a novel complex of the SWI/SNF family from Schizosaccharomyces pombe and its effects on in vitro transcription in nucleosome arrays.","citation":"Mol Cell Biochem 2007 Sep;303(1-2):131-9","abstract":"The family of ATP-dependent chromatin-remodeling factors plays a central role in eukaryotic transcriptional regulation. These complexes can alter the structure of chromatin by mechanisms that involve nucleosome sliding, dissociation, or replacement over a specific promoter. The SWI/SNF chromatin-remodeling complex is required for transcriptional activation or repression in a subset of genes. In the present study we have isolated the spSWI/SNF complex from Schizosaccharomyces pombe, which has at least seven subunits among them spSwi1-like and the catalytic subunit spBrg1. These subunits are homologues to Swi1 and Swi2/Snf2, respectively in Sacharomyces cerevisiae. Moreover, we have demonstrated that spSWI/SNF is able to promote in vitro transcription by RNA polymerase II (RNAPII) in a reconstituted system. In our transcription assays with cellular extracts of Sc. pombe we did not observe inhibition when alpha-Swi1 antibodies were utilized, indicating that other chromatin-remodeling complexes may allow transcription in Sc. pombe.","authors":"Bernal G, Maldonado E","authors_abbrev":"Bernal G et al.","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-05-18","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC30B4.04c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:20375067","title":"Fission yeast Rad26ATRIP delays spindle-pole-body separation following interphase microtubule damage.","citation":"J Cell Sci 2010 May 01;123(Pt 9):1537-45","abstract":"The conserved fission yeast protein Rad26(ATRIP) preserves genomic stability by occupying central positions within DNA-structure checkpoint pathways. It is also required for proper cellular morphology, chromosome stability and following treatment with microtubule poisons. Here, we report that mutation of a putative nuclear export sequence in Rad26(ATRIP) disrupted its cytoplasmic localization in untreated cells and conferred abnormal cellular morphology, minichromosome instability and sensitivity to microtubule poisons without affecting DNA-structure checkpoint signaling. This mutation also disrupted a delay to spindle-pole-body separation that occurred following microtubule damage in G(2). Together, these results demonstrate that Rad26(ATRIP) participates in two genetically defined checkpoint pathways--one that responds to genomic damage and the other to microtubule damage. This response to microtubule damage delays spindle-pole-body separation and, in doing so, might preserve both cellular morphology and chromosome stability.","doi":"10.1242/jcs.049478","authors":"Herring M, Davenport N, Stephan K, Campbell S, White R, Kark J, Wolkow TD","authors_abbrev":"Herring M et al.","pubmed_publication_date":"01 May 2010","pubmed_entrez_date":"2010-04-09","publication_year":"2010","canto_session_key":"176bac49e2ab2fbf","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPBC26H8.07c","SPAC9E9.08","SPBC216.05"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:10544281","title":"Relationship between the subcellular localization and structures of catalytic domains of FKBP-type PPIases.","citation":"J Biochem 1999 Nov;126(5):879-88","abstract":"The Schizosaccharomyces pombe gene, fkp39(+), encoding a homolog of FKBP(FK506 binding protein)-type peptidyl prolyl cis-trans isomerase (PPIase), was isolated and the primary structure was determined. This gene product (SpFkbp39p) showed PPIase enzymatic activity in a chymotrypsin-dependent enzyme assay involving recombinant SpFkbp39p. Comparison of the primary structures of the catalytic domains of FKBPs, including SpFkbp39p, revealed that FKBPs could be classified into four groups. This categorization corresponding to the known subcellular localization of the FKBPs, makes the prediction of the subcellular localization of FKBPs based on their primary structures feasible. SpFkbp39p was considered to be a member of the nuclear-type FKBP group from this relationship between primary structure and subcellular localization. An immunofluorescence assay against HA-epitope-tagged SpFkbp39p revealed that SpFkbp39p is localized to the nucleus, as predicted. Residues conserved in a \"group-specific\" manner in the catalytic domain were mapped to their corresponding three-dimensional positions; these \"group-specific\" residues were located in close proximity in distinct regions mostly on the protein surface, which implies the presence of \"group-specific\" regulatory functional regions. We also found that nuclear-type FKBPs, including SpFkbp39p, have two highly conserved domains other than catalytic ones, with further basic and acidic charged regions, especially in the case of nuclear-type FKBPs. This is the first report indicating that there is a rule for the relationship between the subcellular localization and structure of the catalytic domain of a FKBP.","authors":"Himukai R, Kuzuhara T, Horikoshi M","authors_abbrev":"Himukai R et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-11-02","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1347.02"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:27729451","title":"Cdc24 Is Essential for Long-range End Resection in the Repair of Double-stranded DNA Breaks.","citation":"J Biol Chem 2016 Nov 25;291(48):24961-24973","abstract":"Double-stranded DNA breaks (DSBs) are highly detrimental DNA lesions, which may be repaired by the homologous recombination-mediated repair pathway. The 5' to 3' direction of long-range end resection on one DNA strand, in which 3'-single-stranded DNA overhangs are created from broken DNA ends, is an essential step in this pathway. Dna2 has been demonstrated as an essential nuclease in this event, but the molecular mechanism of how Dna2 is recruited to DNA break sites in vivo has not been elucidated. In this study, a novel recombination factor called Cdc24 was identified in fission yeast. We demonstrated that Cdc24 localizes to DNA break sites during the repair of DNA breaks and is an essential factor in long-range end resection. We also determined that Cdc24 plays a direct role in recruiting Dna2 to DNA break sites through its interaction with Dna2 and replication protein A (RPA). Further, this study revealed that RPA acts as the foundation for assembling the machinery for long-range end resection by its essential role in recruiting Cdc24 and Dna2 to DNA break sites. These results define Cdc24 as an essential factor for long-range end resection in the repair of DSBs, opening the door for further investigations into the enzymes involved in long-range end resection for DSB repair.","authors":"Zhang H, Hua Y, Li R, Kong D","authors_abbrev":"Zhang H et al.","pubmed_publication_date":"25 Nov 2016","pubmed_entrez_date":"2016-10-13","publication_year":"2016","canto_session_key":"13b6f989def8efa6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Daochun Kong","canto_first_approved_date":"2016-11-17 16:21:30","canto_approved_date":"2026-01-29 16:35:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-28 13:58:58","canto_added_date":"2016-10-14 00:15:13","annotation_curators":[{"name":"Daochun Kong","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":62,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8F11.07c","SPAC2G11.12","SPBC660.13c","SPBC29A10.05","SPBC16D10.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-11-17"},{"uniquename":"PMID:19349280","title":"Thioredoxin-related Protein 32 is an arsenite-regulated Thiol Reductase of the proteasome 19 S particle.","citation":"J Biol Chem 2009 May 29;284(22):15233-45","abstract":"Perturbation of the cytoplasmic protein folding environment by exposure to oxidative stress-inducing As(III)-containing compounds challenges the ubiquitin-proteasome system. Here we report on mass spectrometric analysis of As(III)-induced changes in the proteasome's composition in samples prepared by stable isotope labeling with amino acids in cell culture, using mammalian cells in which TRP32 (thioredoxin-related protein of 32 kDa; also referred to as TXNL1) was identified as a novel subunit of the 26 S proteasome. Quantitative genetic interaction mapping, using the epistatic miniarray profiling approach, identified a functional connection between TRP32 and the proteasome. Deletion of txl1, the Schizosaccharomyces pombe homolog of TRP32, results in a slow growth phenotype when combined with deletion of cut8, a gene required for normal proteasome localization. Deletion analysis in vivo, chemical cross-linking, and manipulation of the ATP concentration in vitro during proteasome immunopurification revealed that the C-terminal domain of mammalian TRP32 binds the 19 S regulatory particle in proximity to the proteasome substrate binding site. Thiol modification with polyethylene glycol-maleimide showed disulfide bond formation at the active site of TRP32 in cells exposed to As(III). Pulse-chase labeling showed that TRP32 is a stable protein whose half-life of >6 h is surprisingly reduced to 1 h upon exposure of cells to As(III). These findings reveal a previously undescribed thiol reductase at the proteasome's regulatory particle.","doi":"10.1074/jbc.M109.002121","authors":"Wiseman RL, Chin KT, Haynes CM, Stanhill A, Xu CF, Roguev A, Krogan NJ, Neubert TA, Ron D","authors_abbrev":"Wiseman RL et al.","pubmed_publication_date":"29 May 2009","pubmed_entrez_date":"2009-04-08","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10771645","title":"[Functional genomics and pharmacogenomics using a model organism. Schzosaccharomyces pombe].","citation":"Tanpakushitsu Kakusan Koso 2000 Apr;45(6 Suppl):868-73","abstract":"","authors":"Kuno T, Sugiura R, Shuntoh H","authors_abbrev":"Kuno T et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-04-20","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6457634","title":"Comparative study of an adenosine triphosphatase trigger-fused lipid vesicle and other vesicle forms of dimyristoylphosphatidylcholine.","citation":"Biochemistry 1981 Sep 15;20(19):5576-86","abstract":"Several known forms of bilayer vesicles of dimyristoylphosphatidylcholine exhibit the gel to liquid-crystalline phase transition in the temperature range convenient for membrane enzyme reconstitution studies. This warrants a systematic investigation of their physical characteristics and their phase transition behaviors. We have employed electron microscopy, gel chromatography, 31P nuclear magnetic resonance, differential scanning microcalorimetry, and fluorescence spectroscopy to determine several physical parameters of the limiting size microvesicle (260 +/- 40 A), the larger vesicle form (900 +/- 100A) of Enoch and Strittmatter [Enoch, H. G., & Strittmatter, P. (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 145], the multilamellar vesicle, and, in particular, an ATPase-trigger-fused macrovesicle (950 +/- 200 A). This latter vesicle form was produced by a spontaneous fusion of the complex of the plasma membrane ATPase of Schizosaccharomyces pombe and the lipid microvesicles at a low ratio of enzyme to vesicle concentrations, and at a low temperature (around 10 degrees C). The ATPase-trigger-fused vesicles are unilamellar and have an intact ionic permeation barrier at 30 degrees C and a gel to liquid-crystalline transition temperature at 24.4 degrees C with a transition heat of 5.64 kcal/mol. Thus, this vesicle form should be a valuable tool for studying possible proton-pumping activity of this ATPase. In contrast to data found in the literature, which show lack of the pretransition for unilamellar microvesicles, we have observed the pretransition around 15 degrees C for all the vesicle forms examined. Moreover, the transition widths of unilamellar vesicles are much broader than those of the multilamellar vesicles, suggesting that in the latter system interlayer interactions may contribute to the cooperativity of the transition.","authors":"Dufour JP, Nunnally R, Buhle L, Tsong TY","authors_abbrev":"Dufour JP et al.","pubmed_publication_date":"15 Sep 1981","pubmed_entrez_date":"1981-09-15","publication_year":"1981","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4164882","title":"A new fixation method for Schizosaccharomyces pombe.","citation":"Exp Cell Res 1967 Apr;46(1):215-20","abstract":"","authors":"Schmitter RE, Barker DC","authors_abbrev":"Schmitter RE et al.","pubmed_publication_date":"Apr 1967","pubmed_entrez_date":"1967-04-01","publication_year":"1967","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37156916","title":"Fast and accurate protein structure search with Foldseek.","citation":"Nat Biotechnol 2024 Feb;42(2):243-246","abstract":"As structure prediction methods are generating millions of publicly available protein structures, searching these databases is becoming a bottleneck. Foldseek aligns the structure of a query protein against a database by describing tertiary amino acid interactions within proteins as sequences over a structural alphabet. Foldseek decreases computation times by four to five orders of magnitude with 86%, 88% and 133% of the sensitivities of Dali, TM-align and CE, respectively.","doi":"10.1038/s41587-023-01773-0","authors":"van Kempen M, Kim SS, Tumescheit C, Mirdita M, Lee J, Gilchrist CLM, Söding J, Steinegger M","authors_abbrev":"van Kempen M et al.","pubmed_publication_date":"Feb 2024","pubmed_entrez_date":"2023-05-08","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16C4.04","YGR134W","HGNC:22965","SPAC23H4.16c","SPAC343.01c","SPAC922.04","SPAC1687.14c","SPBC19F8.04c","HGNC:1867","HGNC:7530","HGNC:26434"],"gene_count":6,"ltp_gene_count":0},{"uniquename":"PMID:20022232","title":"Discovery of the mitotic selective chromatid segregation phenomenon and its implications for vertebrate development.","citation":"Curr Opin Cell Biol 2010 Feb;22(1):81-7","abstract":"The asymmetric cell division process is required for cellular differentiation and embryonic development. Recent evidence obtained in Drosophila and C. elegans suggest that this process occurs by non-equivalent distribution of proteins or mRNA (intrinsic factors) to daughter cells, or by their differential exposure to cell extrinsic factors. In contrast, haploid fission yeast sister cells developmentally differ by inheriting sister chromatids that are differentiated by epigenetic means. Specifically, the act of DNA replication at the mating-type locus in yeast switches it's alternate alleles only in one specific member of chromosome 2 sister chromatids in nearly every chromosome replication cycle. To employ this kind of mechanism for cellular differentiation, strictly based on Watson-Crick structure of DNA in diploid organism, selective segregation mechanism is required to coordinate distribution of potentially differentiated sister chromatids to daughter cells. Genetic evidence to this postulate was fortuitously provided by the analysis of mitotic recombinants of chromosome 7 in mouse cells. Remarkably, the biased segregation occurs in some cell types but not in others and the process seems to be chromosome-specific. This review summarizes the discovery of selective chromatid segregation phenomenon and it suggests that such a process of Somatic Sister chromatid Imprinting and Selective chromatid Segregation (SSIS model) might explain development in eukaryotes, such as that of the body axis left-right visceral organs laterality specification in mice.","doi":"10.1016/j.ceb.2009.11.006","authors":"Armakolas A, Koutsilieris M, Klar AJ","authors_abbrev":"Armakolas A et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2009-12-22","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22146300","title":"Overexpression limits of fission yeast cell-cycle regulators in vivo and in silico.","citation":"Mol Syst Biol 2011 Dec 06;7:556","abstract":"Cellular systems are generally robust against fluctuations of intracellular parameters such as gene expression level. However, little is known about expression limits of genes required to halt cellular systems. In this study, using the fission yeast Schizosaccharomyces pombe, we developed a genetic 'tug-of-war' (gTOW) method to assess the overexpression limit of certain genes. Using gTOW, we determined copy number limits for 31 cell-cycle regulators; the limits varied from 1 to >100. Comparison with orthologs of the budding yeast Saccharomyces cerevisiae suggested the presence of a conserved fragile core in the eukaryotic cell cycle. Robustness profiles of networks regulating cytokinesis in both yeasts (septation-initiation network (SIN) and mitotic exit network (MEN)) were quite different, probably reflecting differences in their physiologic functions. Fragility in the regulation of GTPase spg1 was due to dosage imbalance against GTPase-activating protein (GAP) byr4. Using the gTOW data, we modified a mathematical model and successfully reproduced the robustness of the S. pombe cell cycle with the model.","doi":"10.1038/msb.2011.91","authors":"Moriya H, Chino A, Kapuy O, Csikász-Nagy A, Novák B","authors_abbrev":"Moriya H et al.","pubmed_publication_date":"06 Dec 2011","pubmed_entrez_date":"2011-12-08","publication_year":"2011","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8853553","title":"Schizosaccharomyces pombe is more sensitive to pressure stress than Saccharomyces cerevisiae.","citation":"Cell Struct Funct 1996 Jun;21(3):167-74","abstract":"The effects of hydrostatic pressure on ultrastructure, microtubules and microfilaments of Schizosaccharomyces pombe were investigated by fluorescence microscopy, conventional electron microscopy and immunoelectron microscopy. Cells were treated with hydrostatic pressure from 0.1 to 400 MPa for 10 min at room temperature. The nuclear membrane was disrupted at above 100 MPa. At 150 MPa the matrixes of mitochondria had an electron dense area. At 250 MPa the cytoplasmic substances changed dramatically, the cellular organelles could hardly be detected and the fragmented nuclear membrane was barely visible. The fluorescence in alpha-tubulin was lost in most of the cells at 100 MPa. The gold particles for anti alpha-tubulin were not visible in the cells at the same level. Cell cycle specific actin distribution was lost even at 50 MPa, although actin dots localized at the central region remained unchanged. Thick actin cables appeared at 100 MPa. Complete depolymerization of F-actin was observed at 150 MPa. These results suggest that S. pombe cells were more sensitive than Saccharomyces cerevisiae cells. The damage to microtubules and nuclear membrane caused by hydrostatic pressure was though to be followed by breakdown of nuclear division apparatus and the inhibition of nuclear division. This damage might contribute to the frequent formation of polyploidy in S. pombe.","authors":"Sato M, Kobori H, Ishijima SA, Feng ZH, Hamada K, Shimada S, Osumi M","authors_abbrev":"Sato M et al.","pubmed_publication_date":"Jun 1996","pubmed_entrez_date":"1996-06-01","publication_year":"1996","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21083140","title":"Biotechnological synthesis of drug metabolites using human cytochrome P450 isozymes heterologously expressed in fission yeast.","citation":"Bioanalysis 2009 Jul;1(4):821-30","abstract":"Cytochrome P450 mono-oxygenases (CYPs) are the major enzymes involved in the metabolism of drugs and poisons in humans. The variation of their activity - due to genetic polymorphisms or enzyme inhibition/induction - potentially increases the risk of side effects or toxicity. Studies on CYP-dependent metabolism are important in drug-development or toxicity studies. Reference standards of drug metabolites required for such studies, especially in the context of metabolites in safety testing (MIST), are often not commercially available and their classical chemical synthesis can be cumbersome. Recently, a biotechnological approach using human CYP isozymes heterologously expressed in fission yeast was developed for the synthesis of drug metabolites. Among other aspects, this approach has the distinct advantages that the reactions run under mild conditions and that only the final product must be isolated and characterized. This review overviews the first practical applications of this new approach and discusses the selection of substrates, metabolites and fission yeast strains as well as important aspects of incubation, product isolation and clean-up.","doi":"10.4155/bio.09.53","authors":"Peters FT, Bureik M, Maurer HH","authors_abbrev":"Peters FT et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2010-11-19","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23770679","title":"Microtubules and Alp7-Alp14 (TACC-TOG) reposition chromosomes before meiotic segregation.","citation":"Nat Cell Biol 2013 Jul;15(7):786-96","abstract":"Tethering kinetochores at spindle poles facilitates their efficient capture and segregation by microtubules at mitotic onset in yeast. During meiotic prophase of fission yeast, however, kinetochores are detached from the poles, which facilitates meiotic recombination but may cause a risk of chromosome mis-segregation during meiosis. How cells circumvent this dilemma remains unclear. Here we show that an extensive microtubule array assembles from the poles at meiosis I onset and retrieves scattered kinetochores towards the poles to prevent chromosome drift. Moreover, the microtubule-associated protein complex Alp7-Alp14 (the fission yeast orthologues of mammalian TACC-TOG) is phosphorylated by Polo kinase, which promotes its meiosis-specific association to the outer kinetochore complex Nuf2-Ndc80 of scattered kinetochores, thereby assisting in capturing remote kinetochores. Although TOG was recently characterized as a microtubule polymerase, Dis1 (the other TOG orthologue in fission yeast), together with the Dam1 complex, plays a role in microtubule shortening to pull kinetochores polewards. Thus, microtubules and their binding proteins uniquely reconstitute chromosome configuration during meiosis.","doi":"10.1038/ncb2782","authors":"Kakui Y, Sato M, Okada N, Toda T, Yamamoto M","authors_abbrev":"Kakui Y et al.","pubmed_publication_date":"Jul 2013","pubmed_entrez_date":"2013-06-18","publication_year":"2013","canto_session_key":"6c1cc5fd9503d415","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2019-10-18 17:03:31","canto_approved_date":"2024-04-04 07:27:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-03 12:44:33","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Masamitsu Sato","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC890.02c","SPAC23C11.16","SPAC27F1.04c","SPCC895.07","SPAC664.10","SPAC3A11.14c","SPCC736.14","SPAC589.08c","SPBC26H8.07c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2019-10-18"},{"uniquename":"PMID:8890636","title":"[MCM protein complex in fission yeast].","citation":"Tanpakushitsu Kakusan Koso 1996 Sep;41(12 Suppl):1777-83","abstract":"","authors":"Adachi Y","authors_abbrev":"Adachi Y","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20855961","title":"Spo5 phosphorylation is essential for its own timely degradation and for successful meiosis in Schizosaccharomyces pombe.","citation":"Cell Cycle 2010 Sep 15;9(18):3751-60","abstract":"Protein phosphorylation is pivotal for meiotic progression, but little is known about its regulatory mechanisms. We show that before meiosis I, the meiosis-specific Schizosaccharomyces pombe protein Spo5 is phosphorylated in vivo on T29, T55, S59 and/or T63. In a mutant strain expressing Spo5 fused to green fluorescent protein with alanine substitutions of these amino acid sites (GFP; Spo5-4A-GFP), the timely degradation of Spo5 at meiosis II was not observed. Additionally, Spo5-4A-GFP signals were retained after metaphase II and were localized to the nucleus. This was accompanied by the nuclear mislocalization of Psy1, a marker of the forespore membrane (FSM), and the generation of empty cells, in which cytoplasm had leaked from the ruptured membrane, as well as by the appearance of asci harboring deformed spores. Indeed, thin-section electron microscopy (TEM) revealed fragile-looking spo5-4A-GFP ascospores with ruffled spore walls. In contrast, a mutant strain expressing a constitutively-phosphorylated form of Spo5 (Spo5-4D-GFP) was phenotypically indistinguishable from a strain expressing wild-type (WT) protein (Spo5-WT-GFP). Taken together, these results indicate that Spo5 phosphorylation ensures the timely degradation of Spo5 during meiosis and the proper localization of Psy1, leading to the production of viable spores with robust FSMs and strong walls.","authors":"Okuzaki D, Kasama T, Hirata A, Ohtaka A, Kakegawa R, Nojima H","authors_abbrev":"Okuzaki D et al.","pubmed_publication_date":"15 Sep 2010","pubmed_entrez_date":"2010-09-22","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10209119","title":"F-box/WD-repeat proteins pop1p and Sud1p/Pop2p form complexes that bind and direct the proteolysis of cdc18p.","citation":"Curr Biol 1999 Apr 08;9(7):373-6","abstract":"Ubiquitin-dependent proteolysis plays an important role in cell-cycle control [1] [2]. In budding yeast, the protein Skp1p, the cullin-family member Cdc53p, and the F-box/WD-repeat protein Cdc4p form the SCFCdc4p ubiquitin ligase complex, which targets the cyclin-dependent kinase (Cdk) inhibitor Sic1p for proteolysis [3] [4] [5] [6] [7] [8]. Sic1p is recruited to the SCFCdc4p complex by binding to the WD-repeat region of Cdc4p [5] [6], while Skp1p binds to the F-box of Cdc4p [9]. In fission yeast, two distinct Cdc4p-related proteins, Pop1p/Ste16p [10] [11] and the recently identified Sud1p/Pop2p [12], regulate the stability of the replication initiator Cdc18p and the Cdk inhibitor Rum1p. We show here that, despite their structural and functional similarities, the pop1 and pop2 genes fail to complement each other's deletion phenotypes, indicating that they perform non-redundant, but potentially interdependent, functions in proteolysis. Consistent with this hypothesis, Pop1p and Pop2p formed heterooligomeric complexes when overexpressed, and binding of Cdc18p to Pop2p was dependent on Pop1p. The Pop1p-Pop2p interaction was mediated by the amino-terminal domain of Pop2p which, when fused to full-length Pop1p, rescued the phenotype of a Deltapop1Deltapop2 double mutant. Thus, close physical proximity of two distinct F-box/WD-repeat proteins directs proteolysis mediated by the SCFPop ubiquitin ligase complex.","authors":"Wolf DA, McKeon F, Jackson PK","authors_abbrev":"Wolf DA et al.","pubmed_publication_date":"08 Apr 1999","pubmed_entrez_date":"1999-04-21","publication_year":"1999","canto_session_key":"08be22c66e5ceddc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-08-07 14:58:25","canto_approved_date":"2024-04-02 11:55:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-08-07 15:42:43","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":35,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPBC1718.01","SPBC32F12.09","SPAC4D7.03"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2019-08-07"},{"uniquename":"PMID:17072893","title":"Simplified primer design for PCR-based gene targeting and microarray primer database: two web tools for fission yeast.","citation":"Yeast 2006 Oct 15;23(13):921-8","abstract":"PCR-based gene targeting is a popular method for manipulating yeast genes in their normal chromosomal locations. The manual design of primers, however, can be cumbersome and error-prone. We have developed a straightforward web-based tool that applies user-specified inputs to automate and simplify the task of primer selection for deletion, tagging and/or regulated expression of genes in Schizosaccharomyces pombe. This tool, named PPPP (for Pombe PCR Primer Programs), is available at http://www.sanger.ac.uk/PostGenomics/S_pombe/software/. We also present a searchable Microarray Primer Database to retrieve the sequences and accompanying information for primers and PCR products used to build our in-house Sz. pombe microarrays. This database contains information on both coding and intergenic regions to provide context for the microarray data, and it should be useful also for other applications, such as quantitative PCR. The database can be accessed at http://www.sanger.ac.uk/PostGenomics/S_pombe/microarray/.","authors":"Penkett CJ, Birtle ZE, Bähler J","authors_abbrev":"Penkett CJ et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28725905","title":"Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe-2S] cluster binding.","citation":"Metallomics 2017 Aug 16;9(8):1096-1105","abstract":"The fission yeast Schizosaccharomyces pombe expresses the CCAAT-binding factor Php4 in response to iron deprivation. Php4 forms a transcription complex with Php2, Php3, and Php5 to repress the expression of iron proteins as a means to economize iron usage. Previous in vivo results demonstrate that the function and location of Php4 are regulated in an iron-dependent manner by the cytosolic CGFS type glutaredoxin Grx4. In this study, we aimed to biochemically define these protein-protein and protein-metal interactions. Grx4 was found to bind a [2Fe-2S] cluster with spectroscopic features similar to other CGFS glutaredoxins. Grx4 and Php4 also copurify as a complex with a [2Fe-2S] cluster that is spectroscopically distinct from the cluster on Grx4 alone. In vitro titration experiments suggest that these Fe-S complexes may not be interconvertible in the absence of additional factors. Furthermore, conserved cysteines in Grx4 (Cys172) and Php4 (Cys221 and Cys227) are necessary for Fe-S cluster binding and stable complex formation. Together, these results show that Grx4 controls Php4 function through binding of a bridging [2Fe-2S] cluster.","doi":"10.1039/c7mt00144d","authors":"Dlouhy AC, Beaudoin J, Labbé S, Outten CE","authors_abbrev":"Dlouhy AC et al.","pubmed_publication_date":"16 Aug 2017","pubmed_entrez_date":"2017-07-21","publication_year":"2017","canto_session_key":"bf93b4fe64c69a4b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-07-22 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16E9.01c","SPBC26H8.06"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:24747783","title":"Isolation of cellular lipid droplets: two purification techniques starting from yeast cells and human placentas.","citation":"J Vis Exp 2014 Apr 01;(86)","abstract":"Lipid droplets are dynamic organelles that can be found in most eukaryotic and certain prokaryotic cells. Structurally, the droplets consist of a core of neutral lipids surrounded by a phospholipid monolayer. One of the most useful techniques in determining the cellular roles of droplets has been proteomic identification of bound proteins, which can be isolated along with the droplets. Here, two methods are described to isolate lipid droplets and their bound proteins from two wide-ranging eukaryotes: fission yeast and human placental villous cells. Although both techniques have differences, the main method-- density gradient centrifugation--is shared by both preparations. This shows the wide applicability of the presented droplet isolation techniques. In the first protocol, yeast cells are converted into spheroplasts by enzymatic digestion of their cell walls. The resulting spheroplasts are then gently lysed in a loose-fitting homogenizer. Ficoll is added to the lysate to provide a density gradient, and the mixture is centrifuged three times. After the first spin, the lipid droplets are localized to the white-colored floating layer of the centrifuge tubes along with the endoplasmic reticulum (ER), the plasma membrane, and vacuoles. Two subsequent spins are used to remove these other three organelles. The result is a layer that has only droplets and bound proteins. In the second protocol, placental villous cells are isolated from human term placentas by enzymatic digestion with trypsin and DNase I. The cells are homogenized in a loose-fitting homogenizer. Low-speed and medium-speed centrifugation steps are used to remove unbroken cells, cellular debris, nuclei, and mitochondria. Sucrose is added to the homogenate to provide a density gradient and the mixture is centrifuged to separate the lipid droplets from the other cellular fractions. The purity of the lipid droplets in both protocols is confirmed by Western Blot analysis. The droplet fractions from both preps are suitable for subsequent proteomic and lipidomic analysis.","doi":"10.3791/50981","authors":"Mannik J, Meyers A, Dalhaimer P","authors_abbrev":"Mannik J et al.","pubmed_publication_date":"01 Apr 2014","pubmed_entrez_date":"2014-04-22","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11606526","title":"Characterization of Schizosaccharomyces pombe mcm7(+) and cdc23(+) (MCM10) and interactions with replication checkpoints.","citation":"Genetics 2001 Oct;159(2):471-86","abstract":"MCM proteins are required for the proper regulation of DNA replication. We cloned fission yeast mcm7(+) and showed it is essential for viability; spores lacking mcm7(+) begin S phase later than wild-type cells and arrest with an apparent 2C DNA content. We isolated a novel temperature-sensitive allele, mcm7-98, and also characterized two temperature-sensitive alleles of the fission yeast homolog of MCM10, cdc23(+). mcm7-98 and both cdc23ts alleles arrest with damaged chromosomes and an S phase delay. We find that mcm7-98 is synthetically lethal with the other mcmts mutants but does not interact genetically with either cdc23ts allele. However, cdc23-M36 interacts with mcm4ts. Unlike other mcm mutants or cdc23, mcm7-98 is synthetically lethal with checkpoint mutants Deltacds1, Deltachk1, or Deltarad3, suggesting chromosomal defects even at permissive temperature. Mcm7p is a nuclear protein throughout the cell cycle, and its localization is dependent on the other MCM proteins. Our data suggest that the Mcm3p-Mcm5p dimer interacts with the Mcm4p-Mcm6p-Mcm7p core complex through Mcm7p.","authors":"Liang DT, Forsburg SL","authors_abbrev":"Liang DT et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-10-19","publication_year":"2001","canto_session_key":"4b4b351e3a8818f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-06 16:11:14","canto_approved_date":"2021-04-16 12:40:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-10-31 14:44:07","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1682.02c","SPAC23C4.18c","SPCC18B5.11c","SPAC2G11.12","SPAC1B2.05","SPBC29A10.15","SPBC1347.10","SPCC16A11.17","SPBC776.12c","SPBC216.05","SPBC4.04c","SPBC211.04c","SPCC1259.13","SPCC18B5.03","SPBC25D12.03c"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2015-02-06"},{"uniquename":"PMID:21625337","title":"Rab small GTPase emerges as a regulator of TOR complex 2.","citation":"Small GTPases 2010 Nov;1(3):180-182","abstract":"In diverse eukaryotic species from yeast to human, TOR (Target Of Rapamycin) protein kinase operates in signaling pathways that link extracellular stimuli to the control of cell growth and metabolism. TOR kinase functions in two distinct protein complexes, TOR complex 1 (TORC1) and 2 (TORC2). While TORC1 is known to be under the control of the Ras-like small GTPase Rheb, our knowledge about TORC2 regulation is very limited. We thus set out to identify TORC2 activators through genetic approaches in the fission yeast Schizosaccharomyces pombe. Here we briefly review our study that has identified a Rab-family GTPase, Ryh1 and its GEF (guanine nucleotide exchange factor) as positive regulators of TORC2 signaling in S. pombe. Considering the evolutionary conservation of the TOR pathways, it is conceivable that Rabfamily GTPases also play a role in the regulation of human TORC2 in cellular proliferation and insulin signaling.","authors":"Tatebe H, Shiozaki K","authors_abbrev":"Tatebe H et al.","pubmed_publication_date":"Nov 2010","pubmed_entrez_date":"2011-06-01","publication_year":"2010","canto_session_key":"accfa2517bd25ee1","canto_annotation_status":"APPROVED","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_first_approved_date":"2021-06-04 02:34:42","canto_approved_date":"2021-06-04 02:34:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-03 15:04:40","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.07c","SPCC777.08c","SPBC30D10.10c","SPAC4C5.02c","SPBC23E6.08","SPAC1851.04c"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2021-06-04"},{"uniquename":"PMID:24897379","title":"Fra2 is a co-regulator of Fep1 inhibition in response to iron starvation.","citation":"PLoS One 2014;9(6):e98959","abstract":"Iron is required for several metabolic functions involved in cellular growth. Although several players involved in iron transport have been identified, the mechanisms by which iron-responsive transcription factors are controlled are still poorly understood. In Schizosaccharomyces pombe, the Fep1 transcription factor represses genes involved in iron acquisition in response to high levels of iron. In contrast, when iron levels are low, Fep1 becomes inactive and loses its ability to associate with chromatin. Although the molecular basis by which Fep1 is inactivated under iron starvation remains unknown, this process requires the monothiol glutaredoxin Grx4. Here, we demonstrate that Fra2 plays a role in the negative regulation of Fep1 activity. Disruption of fra2+ (fra2Δ) led to a constitutive repression of the fio1+ gene transcription. Fep1 was consistently active and constitutively bound to its target gene promoters in cells lacking fra2+. A constitutive activation of Fep1 was also observed in a php4Δ fra2Δ double mutant strain in which the behavior of Fep1 is freed of its transcriptional regulation by Php4. Microscopic analyses of cells expressing a functional Fra2-Myc13 protein revealed that Fra2 localized throughout the cells with a significant proportion of Fra2 being observed within the nuclei. Further analysis by coimmunoprecipitation showed that Fra2, Fep1 and Grx4 are associated in a heteroprotein complex. Bimolecular fluorescence complementation experiments brought further evidence that an interaction between Fep1 and Fra2 occurs in the nucleus. Taken together, results reported here revealed that Fra2 plays a role in the Grx4-mediated pathway that inactivates Fep1 in response to iron deficiency.","doi":"10.1371/journal.pone.0098959","authors":"Jacques JF, Mercier A, Brault A, Mourer T, Labbé S","authors_abbrev":"Jacques JF et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-06-05","publication_year":"2014","canto_session_key":"7847b131bedea4d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-02 07:17:54","canto_approved_date":"2022-06-01 14:52:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-02 07:17:46","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.08","SPBC16E9.01c","SPBC16E9.06c","SPAC23E2.01","SPAC22G7.01c","SPAC8C9.11","SPCC4B3.11c","SPBC26H8.06"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2016-09-02"},{"uniquename":"PMID:16407405","title":"Cip1 and Cip2 are novel RNA-recognition-motif proteins that counteract Csx1 function during oxidative stress.","citation":"Mol Biol Cell 2006 Mar;17(3):1176-83","abstract":"Eukaryotic cells reprogram their global patterns of gene expression in response to stress. Recent studies in Schizosaccharomyces pombe showed that the RNA-binding protein Csx1 plays a central role in controlling gene expression during oxidative stress. It does so by stabilizing atf1(+) mRNA, which encodes a subunit of a bZIP transcription factor required for gene expression during oxidative stress. Here, we describe two related proteins, Cip1 and Cip2, that were identified by multidimensional protein identification technology (MudPIT) as proteins that coprecipitate with Csx1. Cip1 and Cip2 are cytoplasmic proteins that have RNA recognition motifs (RRMs). Neither protein is essential for viability, but a cip1Delta cip2Delta strain grows poorly and has altered cellular morphology. Genetic epistasis studies and whole genome expression profiling show that Cip1 and Cip2 exert posttranscriptional control of gene expression in a manner that is counteracted by Csx1. Notably, the sensitivity of csx1Delta cells to oxidative stress and their inability to induce expression of Atf1-dependent genes are partially rescued by cip1Delta and cip2Delta mutations. This study emphasizes the importance of a modulated mRNA stability in the eukaryotic stress response pathways and adds new information to the role of RNA-binding proteins in the oxidative stress response.","authors":"Martín V, Rodríguez-Gabriel MA, McDonald WH, Watt S, Yates JR, Bähler J, Russell P","authors_abbrev":"Martín V et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-01-13","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC12G12.03","SPBC29B5.01","SPAC17A2.09c","SPBC16A3.18"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:17276356","title":"Dap1/PGRMC1 binds and regulates cytochrome P450 enzymes.","citation":"Cell Metab 2007 Feb;5(2):143-9","abstract":"Cytochrome P450 enzymes are heme-dependent monoxygenases that play a central role in human physiology. Despite the numerous physiological processes that P450 enzymes impact, the electron donors P450 oxidoreductase and cytochrome b5 are the only proteins known to interact with and modulate the activity of ER microsomal P450s. Here, we report that Dap1/PGRMC1 is required for ER P450 function in yeast and humans. We show that S. pombe Dap1 is a hemoprotein that binds and positively regulates Cyp51A1 and Cyp61A1, two P450s required for sterol biosynthesis. Similarly, loss of human PGRMC1 reduces activity of Cyp51A1, blocking cholesterol synthesis and increasing production of toxic sterol intermediates. PGRMC1 stably binds Cyp51A1 and human P450s from three additional families including Cyp3A4, which metabolizes pharmaceutical compounds. These findings demonstrate that PGRMC1 is required for P450 activity and suggest that interindividual variation in PGRMC1 function may impact multiple biochemical pathways and drug metabolism.","authors":"Hughes AL, Powell DW, Bard M, Eckstein J, Barbuch R, Link AJ, Espenshade PJ","authors_abbrev":"Hughes AL et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-02-06","publication_year":"2007","canto_session_key":"b45eb4ced4f20d69","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-05-02 11:26:03","canto_approved_date":"2024-10-01 06:31:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-02 11:25:57","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13A11.02c","SPAC23A1.03","SPAC25B8.01","SPAC19A8.04"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2024-05-02"},{"uniquename":"PMID:35172472","title":"Knockdown of vps54 aggravates tamoxifen-induced cytotoxicity in fission yeast.","citation":"Genomics Inform 2021 Dec;19(4):e39","abstract":"Tamoxifen (TAM) is an anticancer drug used to treat estrogen receptor (ER)‒positive breast cancer. However, its ER-independent cytotoxic and antifungal activities have prompted debates on its mechanism of action. To achieve a better understanding of the ER-independent antifungal action mechanisms of TAM, we systematically identified TAM-sensitive genes through microarray screening of the heterozygous gene deletion library in fission yeast (Schizosaccharomyces pombe). Secondary confirmation was followed by a spotting assay, finally yielding 13 TAM-sensitive genes under the drug-induced haploinsufficient condition. For these 13 TAM-sensitive genes, we conducted a comparative analysis of their Gene Ontology (GO) 'biological process' terms identified from other genome-wide screenings of the budding yeast deletion library and the MCF7 breast cancer cell line. Several TAM-sensitive genes overlapped between the yeast strains and MCF7 in GO terms including 'cell cycle' (cdc2, rik1, pas1, and leo1), 'signaling' (sck2, oga1, and cki3), and 'vesicle-mediated transport' (SPCC126.08c, vps54, sec72, and tvp15), suggesting their roles in the ER-independent cytotoxic effects of TAM. We recently reported that the cki3 gene with the 'signaling' GO term was related to the ER-independent antifungal action mechanisms of TAM in yeast. In this study, we report that haploinsufficiency of the essential vps54 gene, which encodes the GARP complex subunit, significantly aggravated TAM sensitivity and led to an enlarged vesicle structure in comparison with the SP286 control strain. These results strongly suggest that the vesicle-mediated transport process might be another action mechanism of the ER-independent antifungal or cytotoxic effects of TAM.","doi":"10.5808/gi.21049","authors":"Lee S, Nam M, Lee AR, Baek ST, Kim MJ, Kim JS, Kong AH, Lee M, Lee SJ, Kim SY, Kim DU, Hoe KL","authors_abbrev":"Lee S et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2022-02-16","publication_year":"2021","canto_session_key":"ae593bb3040d3c61","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Miyoung Nam","canto_first_approved_date":"2024-07-02 05:01:04","canto_approved_date":"2024-07-02 05:01:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-02 05:00:57","canto_added_date":"2022-02-20 01:15:04","annotation_curators":[{"name":"Miyoung Nam","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.08c","SPBC16A3.08c","SPAC30.01c","SPBC1709.05","SPBC13E7.08c","SPBC646.11","SPCC11E10.08","SPAC2F3.10","SPAC22E12.14c","SPBC11B10.09","SPAC1805.05","SPAC6F12.04","SPAC19E9.03"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2024-07-02"},{"uniquename":"PMID:11792803","title":"The S. pombe aurora-related kinase Ark1 associates with mitotic structures in a stage dependent manner and is required for chromosome segregation.","citation":"J Cell Sci 2001 Dec;114(Pt 24):4371-84","abstract":"Metazoans contain three aurora-related kinases. Aurora A is required for spindle formation while aurora B is required for chromosome condensation and cytokinesis. Less is known about the function of aurora C. S. pombe contains a single aurora-related kinase, Ark1. Although Ark1 protein levels remained constant as cells progressed through the mitotic cell cycle, its distribution altered during mitosis and meiosis. Throughout G2 Ark1 was concentrated in one to three nuclear foci that were not associated with the spindle pole body/centromere complex. Following commitment to mitosis Ark1 associated with chromatin and was particularly concentrated at several sites including kinetochores/centromeres. Kinetochore/centromere association diminished during anaphase A, after which it was distributed along the spindle. The protein became restricted to a small central zone that transiently enlarged as the spindle extended. As in many other systems mitotic fission yeast cells exhibit a much greater degree of phosphorylation of serine 10 of histone H3 than interphase cells. A number of studies have linked this modification with chromosome condensation. Ark1 immuno-precipitates phosphorylated serine 10 of histone H3 in vitro. This activity was highest in mitotic extracts. The absence of the histone H3 phospho-serine 10 epitope from mitotic cells in which the ark1(+) gene had been deleted (ark1.Delta1); the inability of these cells to resolve their chromosomes during anaphase and the co-localisation of this phospho-epitope with Ark1 early in mitosis, all suggest that Ark1 phosphorylates serine 10 of histone H3 in vivo. ark1.Delta1 cells also exhibited a reduction in kinetochore activity and a minor defect in spindle formation. Thus the enzyme activity, localisation and phenotype arising from our manipulations of this single fission yeast aurora kinase family member suggest that this single kinase is executing functions that are separately implemented by distinct aurora A and aurora B kinases in higher systems.","authors":"Petersen J, Paris J, Willer M, Philippe M, Hagan IM","authors_abbrev":"Petersen J et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2002-01-17","publication_year":"2001","canto_session_key":"c0af69aa51ff9eff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-01-29 14:23:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-12 16:07:00","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.13c","SPBC1105.11c","SPAC1834.04","SPBC8D2.04"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-10-12"},{"uniquename":"PMID:16988108","title":"The meiotic bouquet promotes homolog interactions and restricts ectopic recombination in Schizosaccharomyces pombe.","citation":"Genetics 2006 Sep;174(1):167-77","abstract":"Chromosome architecture undergoes extensive, programmed changes as cells enter meiosis. A highly conserved change is the clustering of telomeres at the nuclear periphery to form the \"bouquet\" configuration. In the fission yeast Schizosaccharomyces pombe the bouquet and associated nuclear movement facilitate initial interactions between homologs. We show that Bqt2, a meiosis-specific protein required for bouquet formation, is required for wild-type levels of homolog pairing and meiotic allelic recombination. Both gene conversion and crossing over are reduced and exhibit negative interference in bqt2Delta mutants, reflecting reduced homolog pairing. While both the bouquet and nuclear movement promote pairing, only the bouquet restricts ectopic recombination (that between dispersed repetitive DNA). We discuss mechanisms by which the bouquet may prevent deleterious translocations by restricting ectopic recombination.","authors":"Davis L, Smith GR","authors_abbrev":"Davis L et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-09-22","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23836910","title":"Structural and functional analysis of transmembrane segment IV of the salt tolerance protein Sod2.","citation":"J Biol Chem 2013 Aug 23;288(34):24609-24","abstract":"Sod2 is the plasma membrane Na(+)/H(+) exchanger of the fission yeast Schizosaccharomyces pombe. It provides salt tolerance by removing excess intracellular sodium (or lithium) in exchange for protons. We examined the role of amino acid residues of transmembrane segment IV (TM IV) ((126)FPQINFLGSLLIAGCITSTDPVLSALI(152)) in activity by using alanine scanning mutagenesis and examining salt tolerance in sod2-deficient S. pombe. Two amino acids were critical for function. Mutations T144A and V147A resulted in defective proteins that did not confer salt tolerance when reintroduced into S. pombe. Sod2 protein with other alanine mutations in TM IV had little or no effect. T144D and T144K mutant proteins were inactive; however, a T144S protein was functional and provided lithium, but not sodium, tolerance and transport. Analysis of sensitivity to trypsin indicated that the mutations caused a conformational change in the Sod2 protein. We expressed and purified TM IV (amino acids 125-154). NMR analysis yielded a model with two helical regions (amino acids 128-142 and 147-154) separated by an unwound region (amino acids 143-146). Molecular modeling of the entire Sod2 protein suggested that TM IV has a structure similar to that deduced by NMR analysis and an overall structure similar to that of Escherichia coli NhaA. TM IV of Sod2 has similarities to TM V of the Zygosaccharomyces rouxii Na(+)/H(+) exchanger and TM VI of isoform 1 of mammalian Na(+)/H(+) exchanger. TM IV of Sod2 is critical to transport and may be involved in cation binding or conformational changes of the protein.","doi":"10.1074/jbc.M113.483065","authors":"Ullah A, Kemp G, Lee B, Alves C, Young H, Sykes BD, Fliegel L","authors_abbrev":"Ullah A et al.","pubmed_publication_date":"23 Aug 2013","pubmed_entrez_date":"2013-07-10","publication_year":"2013","canto_session_key":"2225bf5e95a71d70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-10-31 13:57:24","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-12-03 17:28:09","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":65,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-03","pdb_entries":[{"pdb_id":"2m7x","gene_chains":[{"gene_uniquename":"SPAC977.10","chain":"A","position":"125-154"}],"title":"Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2","entry_authors":"Ullah A,Kemp G,Lee B,Alves C,Young H,Sykes BD,Fliegel L","entry_authors_abbrev":"Ullah A et al.","reference_uniquename":"PMID:23836910","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:19675567","title":"The structural basis of tail-anchored membrane protein recognition by Get3.","citation":"Nature 2009 Sep 17;461(7262):361-6","abstract":"Targeting of newly synthesized membrane proteins to the endoplasmic reticulum is an essential cellular process. Most membrane proteins are recognized and targeted co-translationally by the signal recognition particle. However, nearly 5% of membrane proteins are 'tail-anchored' by a single carboxy-terminal transmembrane domain that cannot access the co-translational pathway. Instead, tail-anchored proteins are targeted post-translationally by a conserved ATPase termed Get3. The mechanistic basis for tail-anchored protein recognition or targeting by Get3 is not known. Here we present crystal structures of yeast Get3 in 'open' (nucleotide-free) and 'closed' (ADP.AlF(4)(-)-bound) dimer states. In the closed state, the dimer interface of Get3 contains an enormous hydrophobic groove implicated by mutational analyses in tail-anchored protein binding. In the open state, Get3 undergoes a striking rearrangement that disrupts the groove and shields its hydrophobic surfaces. These data provide a molecular mechanism for nucleotide-regulated binding and release of tail-anchored proteins during their membrane targeting by Get3.","doi":"10.1038/nature08319","authors":"Mateja A, Szlachcic A, Downing ME, Dobosz M, Mariappan M, Hegde RS, Keenan RJ","authors_abbrev":"Mateja A et al.","pubmed_publication_date":"17 Sep 2009","pubmed_entrez_date":"2009-08-14","publication_year":"2009","canto_session_key":"2851af55099e8be4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-12-20 05:36:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-19 21:37:07","canto_added_date":"2016-12-19 21:36:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1142.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-12-19","pdb_entries":[{"pdb_id":"2woo","gene_chains":[{"gene_uniquename":"SPAC1142.06","chain":"A/B/C/D/E/F","position":"1-329"}],"title":"Nucleotide-free form of S. pombe Get3","entry_authors":"Mateja A,Szlachcic A,Downing ME,Dobosz M,Mariappan M,Hegde RS,Keenan RJ","entry_authors_abbrev":"Mateja A et al.","reference_uniquename":"PMID:19675567","experimental_method":"X-ray","resolution":"3.006"}]},{"uniquename":"PMID:469945","title":"Genetic and enzymatic characterization of conditional lethal mutants of the yeast Schizosaccharomyces pombe with a temperature-sensitive DNA ligase.","citation":"J Mol Biol 1979 May 25;130(3):273-84","abstract":"","authors":"Nasmyth KA","authors_abbrev":"Nasmyth KA","pubmed_publication_date":"25 May 1979","pubmed_entrez_date":"1979-05-25","publication_year":"1979","canto_session_key":"bc9bf657991111ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-08 09:08:44","canto_approved_date":"2022-05-02 07:02:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-24 14:31:39","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-09-08"},{"uniquename":"PMID:24152550","title":"Genome-wide analysis of poly(A) site selection in Schizosaccharomyces pombe.","citation":"RNA 2013 Dec;19(12):1617-31","abstract":"Polyadenylation of pre-mRNAs, a critical step in eukaryotic gene expression, is mediated by cis elements collectively called the polyadenylation signal. Genome-wide analysis of such polyadenylation signals was missing in fission yeast, even though it is an important model organism. We demonstrate that the canonical AATAAA motif is the most frequent and functional polyadenylation signal in Schizosaccharomyces pombe. Using analysis of RNA-Seq data sets from cells grown under various physiological conditions, we identify 3' UTRs for nearly 90% of the yeast genes. Heterogeneity of cleavage sites is common, as is alternative polyadenylation within and between conditions. We validated the computationally identified sequence elements likely to promote polyadenylation by functional assays, including qRT-PCR and 3'RACE analysis. The biological importance of the AATAAA motif is underlined by functional analysis of the genes containing it. Furthermore, it has been shown that convergent genes require trans elements, like cohesin for efficient transcription termination. Here we show that convergent genes lacking cohesin (on chromosome 2) are generally associated with longer overlapping mRNA transcripts. Our bioinformatic and experimental genome-wide results are summarized and can be accessed and customized in a user-friendly database Pomb(A).","doi":"10.1261/rna.040675.113","authors":"Schlackow M, Marguerat S, Proudfoot NJ, Bähler J, Erban R, Gullerova M","authors_abbrev":"Schlackow M et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-10-25","publication_year":"2013","canto_session_key":"79e0f10fff40bd75","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-03-11 17:50:25","canto_approved_date":"2020-03-11 17:50:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-11 17:42:20","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2020-03-11"},{"uniquename":"PMID:34958661","title":"Arf6 anchors Cdr2 nodes at the cell cortex to control cell size at division.","citation":"J Cell Biol 2022 Feb 07;221(2)","abstract":"Fission yeast cells prevent mitotic entry until a threshold cell surface area is reached. The protein kinase Cdr2 contributes to this size control system by forming multiprotein nodes that inhibit Wee1 at the medial cell cortex. Cdr2 node anchoring at the cell cortex is not fully understood. Through a genomic screen, we identified the conserved GTPase Arf6 as a component of Cdr2 signaling. Cells lacking Arf6 failed to divide at a threshold surface area and instead shifted to volume-based divisions at increased overall size. Arf6 stably localized to Cdr2 nodes in its GTP-bound but not GDP-bound state, and its guanine nucleotide exchange factor (GEF), Syt22, was required for both Arf6 node localization and proper size at division. In arf6Δ mutants, Cdr2 nodes detached from the membrane and exhibited increased dynamics. These defects were enhanced when arf6Δ was combined with other node mutants. Our work identifies a regulated anchor for Cdr2 nodes that is required for cells to sense surface area.","doi":"10.1083/jcb.202109152","authors":"Opalko HE, Miller KE, Kim HS, Vargas-Garcia CA, Singh A, Keogh MC, Moseley JB","authors_abbrev":"Opalko HE et al.","pubmed_publication_date":"07 Feb 2022","pubmed_entrez_date":"2021-12-27","publication_year":"2022","canto_session_key":"b793085c4da3e210","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"James Moseley","canto_first_approved_date":"2022-06-30 18:17:18","canto_approved_date":"2026-02-14 08:46:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-06-23 14:42:32","canto_added_date":"2021-12-29 01:15:04","annotation_curators":[{"name":"James Moseley","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.06c","SPAC57A10.02","SPAC4F8.13c","SPBC1539.08","SPCC4B3.15","SPAC24H6.05","SPCC18B5.03","SPAP8A3.08","SPAC2F7.03c","SPAC11E3.11c","SPAC23C11.10","SPBC21D10.05c"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2022-06-30"},{"uniquename":"PMID:33775921","title":"Deletion of the non-essential Rpb9 subunit of RNA polymerase II results in pleiotropic phenotypes in Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta Proteins Proteom 2021 Jul;1869(7):140654","abstract":"Schizosaccharomyces pombe RNA polymerase II comprises twelve different subunits. Its Rpb9 subunit comprises 113 amino acids, and is the only non-essential subunit of S. pombe RNA polymerase II. However, its functions have not been studied in S. pombe. The results presented in this study demonstrate that Rpb9 is involved in regulating growth under optimum and certain stress conditions in S. pombe. To further address the role (s) of various domains of this subunit in regulating these phenotypes, deletion mutant analysis was done. We observed that the region spanning 1-74 amino acids, encompassing the amino-terminal zinc finger domain and the linker region of Rpb9 was able to rescue the phenotypes associated with rpb9 + deletion. We also demonstrate that the functions of this subunit are only partially conserved among yeast and humans. Our computational biology approaches provide a structural basis for the differential role of various Rpb9 domains in S. pombe. Furthermore, using these tools we show that there has been a co-evolution of the interaction residues between the Rpb9 subunit and the two largest subunits of RNA polymerase II, allowing for a more stringent organism-specific packing. Taken together, our results have provided functional and structural insights into the Rpb9 subunit of S. pombe.","doi":"10.1016/j.bbapap.2021.140654","authors":"Bhardwaj V, Vishwakarma P, Lynn A, Sharma N","authors_abbrev":"Bhardwaj V et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-03-29","publication_year":"2021","canto_session_key":"332ec190c658db98","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nimisha Sharma","canto_first_approved_date":"2021-05-19 08:57:14","canto_approved_date":"2021-05-19 08:57:14","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-05-08 07:56:57","canto_added_date":"2021-03-31 00:15:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":35,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Nimisha Sharma","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPYUG7.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-05-19"},{"uniquename":"EMBL:SPD186","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28612052","title":"A CRISPR/Cas9-based method and primer design tool for seamless genome editing in fission yeast.","citation":"Wellcome Open Res 2016;1:19","abstract":"In the fission yeast  Schizosaccharomyces pombe  the prevailing approach for gene manipulations is based on homologous recombination of a PCR product that contains genomic target sequences and a selectable marker. The CRISPR/Cas9 system has recently been implemented in fission yeast, which allows for seamless genome editing without integration of a selection marker or leaving any other genomic 'scars'. The published method involves manual design of the single guide RNA (sgRNA), and digestion of a large plasmid with a problematic restriction enzyme to clone the sgRNA. To increase the efficiency of this approach, we have established and optimized a PCR-based system to clone the sgRNA without restriction enzymes into a plasmid with a dominant  natMX6  (nourseothricin) selection marker. We also provide a web-tool, CRISPR4P, to support the design of the sgRNAs and the primers required for the entire process of seamless DNA deletion. Moreover, we report the preparation of G1-synchronized and cryopreserved  S. pombe  cells, which greatly increases the efficiency and speed for transformations, and may also facilitate standard gene manipulations. Applying this optimized CRISPR/Cas9-based approach, we have successfully deleted over 80 different non-coding RNA genes, which are generally lowly expressed, and have inserted 7 point mutations in 4 different genomic regions.","doi":"10.12688/wellcomeopenres.10038.3","authors":"Rodríguez-López M, Cotobal C, Fernández-Sánchez O, Borbarán Bravo N, Oktriani R, Abendroth H, Uka D, Hoti M, Wang J, Zaratiegui M, Bähler J","authors_abbrev":"Rodríguez-López M et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2017-06-15","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-06-16 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15317843","title":"Schizosaccharomyces pombe RanGAP homolog, SpRna1, is required for centromeric silencing and chromosome segregation.","citation":"Mol Biol Cell 2004 Nov;15(11):4960-70","abstract":"We isolated 11 independent temperature-sensitive (ts) mutants of Schizosaccharomyces pombe RanGAP, SpRna1 that have several amino acid changes in the conserved domains of RanGAP. Resulting Sprna1ts showed a strong defect in mitotic chromosome segregation, but did not in nucleocytoplasmic transport and microtubule formation. In addition to Sprna1+ and Spksp1+, the clr4+ (histone H3-K9 methyltransferase), the S. pombe gene, SPAC25A8.01c, designated snf2SR+ (a member of the chromatin remodeling factors, Snf2 family with DNA-dependent ATPase activity), but not the spi1+ (S. pombe Ran homolog), rescued a lethality of Sprna1ts. Both Clr4 and Snf2 were reported to be involved in heterochromatin formation essential for building the centromeres. Consistently, Sprna1ts was defective in gene-silencing at the centromeres. But a silencing at the telomere, another heterochromatic region, was normal in all of Sprna1ts strains, indicating SpRna1 in general did not function for a heterochromatin formation. snf2SR+ rescued a centromeric silencing defect and Deltaclr4+ was synthetic lethal with Sprna1ts. Taken together, SpRna1 was suggested to function for constructing the centromeres, by cooperating with Clr4 and Snf2SR. Loss of SpRna1 activity, therefore, caused chromosome missegregation.","authors":"Kusano A, Yoshioka T, Nishijima H, Nishitani H, Nishimoto T","authors_abbrev":"Kusano A et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-08-20","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c","SPAC25A8.01c","SPAC22E12.07","SPBC16E9.13"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:39527206","title":"ChIPmentation for Epigenomic Analysis in Fission Yeast.","citation":"Methods Mol Biol 2025;2862:255-266","abstract":"Histone modifications and transcription factor-DNA interactions regulate vital processes such as transcription, recombination, repair, and accurate chromosome segregation. Chromatin immunoprecipitation followed by sequencing (ChIP-Seq) has been instrumental in studying genome-wide distribution of DNA-bound or chromatin-associated factors and histone posttranslational modifications (PTMs). Here, we describe a ChIPmentation protocol adapted for fission yeast, Schizosaccharomyces pombe. This method merges Tn5 mediated tagmentation with existing ChIP protocols, resulting in lower sample input requirements with significant reduction in hands-on time and sample preparation costs.","doi":"10.1007/978-1-0716-4168-2_18","authors":"Dewornu FS, Tong P, Torres-Garcia S, Pidoux A, Allshire R, Shukla M","authors_abbrev":"Dewornu FS et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16285526","title":"Protein amino acid composition of plasma membranes affects membrane fluidity and thereby ethanol tolerance in a self-flocculating fusant of Schizosaccharomyces pombe and Saccharomyces cerevisiae.","citation":"Sheng Wu Gong Cheng Xue Bao 2005 Sep;21(5):809-13","abstract":"A combination of three amino acids including 1.0 g/L isoleucine, 0.5 g/L methionine and 2.0 g/L phenylalanine was found to enhance ethanol tolerance of a self-flocculating fusant of Schizosaccharomyces pombe and Saccharomyces cerevisiae. When subjected to 20% (V/V) ethanol for 9 h at 30 degrees C, all cells died whereas 57% remained viable for the cells grown in the presence of the three amino acids. Based on the analysis of protein amino acid composition of plasma membranes and the determination of plasma membrane fluidity by measuring fluorescence anisotropy using diphenylhexatriene as a probe, it was found that the significantly increased ethanol tolerance of cells grown with the three amino acids was due to the incorporation of the supplementary amino acids into the plasma membranes, thus resulting in enhanced ability of the plasma membranes to efficiently counteract the fluidizing effect of ethanol when subjected to ethanol stress. This is the first time to report that plasma membrane fluidity can be influenced by protein amino acid composition of plasma membranes.","authors":"Hu CK, Bai FW, An LJ","authors_abbrev":"Hu CK et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-11-16","publication_year":"2005","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39719362","title":"A novel method for telomere length detection in fission yeast.","citation":"FEMS Yeast Res 2024 Dec 24;","abstract":"Fission yeast is the ideal model organism for studying telomere maintenance in higher eukaryotes. Telomere length has been directly correlated with life expectancy and the onset of aging-related diseases in mammals. In this study, we developed a novel simple, and reproducible method to measure the telomere length, by investigating the effect of Caffeine and Cisplatin on the telomere length in fission yeast. Hydroxyurea synchronized fission yeast cells were exposed to 62 μM Cisplatin and 8.67 mM Caffeine treatments for 2 hours then their telomere lengths were evaluated with two different methods. first: the quantitative PCR assay was used as a confirmative method where telomere length was determined relative to a single copy gene in the genome. Second: the newly developed method standard PCR/ImageJ assay assessed the telomere length based on the amplified PCR band intensity using a set of telomere primers, reflecting telomeric sequence availability in the genome. Both methods show a significant decrease and a notable telomere lengthening in response to Cisplatin and Caffeine treatments respectively. The finding supports the accuracy and productivity of the standard PCR/ImageJ assay as it can serve as a quick screening tool to study the effect of suspected chemotherapeutic and anti-aging drugs on telomere length in fission yeast.","doi":"10.1093/femsyr/foae040","authors":"Mohamed HABE, Agus HH, Palabiyik B","authors_abbrev":"Mohamed HABE et al.","pubmed_publication_date":"24 Dec 2024","pubmed_entrez_date":"2024-12-24","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-12-26 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20221439","title":"Detoxification of multiple heavy metals by a half-molecule ABC transporter, HMT-1, and coelomocytes of Caenorhabditis elegans.","citation":"PLoS One 2010 Mar 05;5(3):e9564","abstract":"Developing methods for protecting organisms in metal-polluted environments is contingent upon our understanding of cellular detoxification mechanisms. In this regard, half-molecule ATP-binding cassette (ABC) transporters of the HMT-1 subfamily are required for cadmium (Cd) detoxification. HMTs have conserved structural architecture that distinguishes them from other ABC transporters and allows the identification of homologs in genomes of different species including humans. We recently discovered that HMT-1 from the simple, unicellular organism, Schizosaccharomyces pombe, SpHMT1, acts independently of phytochelatin synthase (PCS) and detoxifies Cd, but not other heavy metals. Whether HMTs from multicellular organisms confer tolerance only to Cd or also to other heavy metals is not known.\nUsing molecular genetics approaches and functional in vivo assays we showed that HMT-1 from a multicellular organism, Caenorhabditis elegans, functions distinctly from its S. pombe counterpart in that in addition to Cd it confers tolerance to arsenic (As) and copper (Cu) while acting independently of pcs-1. Further investigation of hmt-1 and pcs-1 revealed that these genes are expressed in different cell types, supporting the notion that hmt-1 and pcs-1 operate in distinct detoxification pathways. Interestingly, pcs-1 and hmt-1 are co-expressed in highly endocytic C. elegans cells with unknown function, the coelomocytes. By analyzing heavy metal and oxidative stress sensitivities of the coelomocyte-deficient C. elegans strain we discovered that coelomocytes are essential mainly for detoxification of heavy metals, but not of oxidative stress, a by-product of heavy metal toxicity.\nWe established that HMT-1 from the multicellular organism confers tolerance to multiple heavy metals and is expressed in liver-like cells, the coelomocytes, as well as head neurons and intestinal cells, which are cell types that are affected by heavy metal poisoning in humans. We also showed that coelomocytes are involved in detoxification of heavy metals. Therefore, the HMT-1-dependent detoxification pathway and coelomocytes of C. elegans emerge as novel models for studies of heavy metal-promoted diseases.","doi":"10.1371/journal.pone.0009564","authors":"Schwartz MS, Benci JL, Selote DS, Sharma AK, Chen AG, Dang H, Fares H, Vatamaniuk OK","authors_abbrev":"Schwartz MS et al.","pubmed_publication_date":"05 Mar 2010","pubmed_entrez_date":"2010-03-12","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11E3.03","SPCC737.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:28040778","title":"Latrunculin A-Induced Perturbation of the Actin Cytoskeleton Mediates Pap1p-Dependent Induction of the Caf5p Efflux Pump in  Schizosaccharomyces pombe .","citation":"G3 (Bethesda) 2017 Feb 09;7(2):723-730","abstract":"As part of an earlier study aimed at uncovering gene products with roles in defending against latrunculin A (LatA)-induced cytoskeletal perturbations, we identified three members of the oxidative stress response pathway: the Pap1p AP-1-like transcription factor, the Imp1p α-importin, and the Caf5p efflux pump. In this report, we characterize the pathway further and show that Pap1p translocates from the cytoplasm to the nucleus in an Imp1p-dependent manner upon LatA treatment. Moreover, preventing this translocation, through the addition of a nuclear export signal (NES), confers the same characteristic LatA-sensitive phenotype exhibited by  pap1 Δ cells. Lastly, we show that the  caf5  gene is induced upon exposure to LatA and that Pap1p is required for this transcriptional upregulation. Importantly, the expression of  trr1 , a Pap1p target specifically induced in response to oxidative stress, is not significantly altered by LatA treatment. Taken together, these results suggest a model in which LatA-mediated cytoskeletal perturbations are sensed, triggering the Imp1p-dependent translocation of Pap1p to the nucleus and the induction of the  caf5  gene (independently of oxidative stress).","doi":"10.1534/g3.116.037903","authors":"Asadi F, Chakraborty B, Karagiannis J","authors_abbrev":"Asadi F et al.","pubmed_publication_date":"09 Feb 2017","pubmed_entrez_date":"2017-01-02","publication_year":"2017","canto_session_key":"fc15115a28fd455c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-01-05 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29192674","title":"Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway.","citation":"Cell Res 2018 Jan;28(1):111-125","abstract":"Short-chain fatty acids and their corresponding acyl-CoAs sit at the crossroads of metabolic pathways and play important roles in diverse cellular processes. They are also precursors for protein post-translational lysine acylation modifications. A noteworthy example is the newly identified lysine 2-hydroxyisobutyrylation (K hib ) that is derived from 2-hydroxyisobutyrate and 2-hydroxyisobutyryl-CoA. Histone K hib  has been shown to be associated with active gene expression in spermatogenic cells. However, the key elements that regulate this post-translational lysine acylation pathway remain unknown. This has hindered characterization of the mechanisms by which this modification exerts its biological functions. Here we show that Esa1p in budding yeast and its homologue Tip60 in human could add K hib  to substrate proteins both in vitro and in vivo. In addition, we have identified HDAC2 and HDAC3 as the major enzymes to remove K hib . Moreover, we report the first global profiling of K hib  proteome in mammalian cells, identifying 6 548 K hib  sites on 1 725 substrate proteins. Our study has thus discovered both the \"writers\" and \"erasers\" for histone K hib  marks, and major K hib  protein substrates. These results not only illustrate the landscape of this new lysine acylation pathway, but also open new avenues for studying diverse functions of cellular metabolites associated with this pathway.","doi":"10.1038/cr.2017.149","authors":"Huang H, Luo Z, Qi S, Huang J, Xu P, Wang X, Gao L, Li F, Wang J, Zhao W, Gu W, Chen Z, Dai L, Dai J, Zhao Y","authors_abbrev":"Huang H et al.","pubmed_publication_date":"Jan 2018","pubmed_entrez_date":"2017-12-02","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC637.12c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:14527420","title":"Generating crossovers by resolution of nicked Holliday junctions: a role for Mus81-Eme1 in meiosis.","citation":"Mol Cell 2003 Sep;12(3):761-74","abstract":"The double Holliday junction (dHJ) is generally regarded to be a key intermediate of meiotic recombination, whose resolution is critical for the formation of crossover recombinants. In fission yeast, the Mus81-Eme1 endonuclease has been implicated in resolving dHJs. Consistent with this role, we show that Mus81-Eme1 is required for generating meiotic crossovers. However, purified Mus81-Eme1 prefers to cleave junctions that mimic those formed during the transition from double-strand break to dHJ. Crucially, these junctions are cleaved by Mus81-Eme1 in precisely the right orientation to guarantee the formation of a crossover every time. These data demonstrate how crossovers could arise without forming or resolving dHJs using an enzyme that is widely conserved amongst eukaryotes.","authors":"Osman F, Dixon J, Doe CL, Whitby MC","authors_abbrev":"Osman F et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-10-07","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12087160","title":"Identification and characterization of transcription factor IIIA from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2002 Jul 01;30(13):2772-81","abstract":"Transcription factor IIIA (TFIIIA) is specifically required for transcription of 5S rRNA genes and is the archetypal C2H2 zinc finger protein. All known vertebrate TFIIIAs have a similar organization: nine zinc fingers, followed by a C-terminal domain of unknown structure. The zinc fingers of Saccharomyces cerevisiae TFIIIA are interrupted between fingers eight and nine by an 81-amino acid spacer. Aside from the amino acids required for zinc finger folding, TFIIIAs from different species are remarkably divergent, whereas the natural binding site, the internal control region of the 5S rRNA gene, is well conserved. We now describe the identification and characterization of TFIIIA from Schizosaccharomyces pombe. This protein is organized differently from its known homologs, in that it contains eight closely spaced zinc fingers, a ninth zinc finger missing a C-terminal Zn2+-coordinating histidine, a 53- amino acid spacer, and an unprecedented tenth zinc finger. We have confirmed the identity of this divergent protein as TFIIIA by showing that it binds specifically and with high affinity to the S.pombe 5S rRNA gene. Comparison of DNase I protection patterns produced by TFIIIA from multiple species suggests a novel mode of DNA recognition by the S.pombe protein. Recombinant S.pombe TFIIIA was also shown to support specific transcription of the 5S rRNA gene in vitro.","authors":"Schulman DB, Setzer DR","authors_abbrev":"Schulman DB et al.","pubmed_publication_date":"01 Jul 2002","pubmed_entrez_date":"2002-06-28","publication_year":"2002","canto_session_key":"77e19b7f7e8218d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-21 09:04:20","canto_approved_date":"2021-01-21 09:12:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-21 09:04:10","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC144.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-01-21"},{"uniquename":"PMID:12524335","title":"Genetic and biochemical basis for viability of yeast lacking mitochondrial genomes.","citation":"Genetics 2002 Dec;162(4):1595-604","abstract":"Yme1p, an ATP-dependent protease localized in the mitochondrial inner membrane, is required for the growth of yeast lacking an intact mitochondrial genome. Specific dominant mutations in the genes encoding the alpha- and gamma-subunits of the mitochondrial F(1)F(0)-ATPase suppress the slow-growth phenotype of yeast that simultaneously lack Yme1p and mitochondrial DNA. F(1)F(0)-ATPase activity is reduced in yeast lacking Yme1p and is restored in yme1 strains bearing suppressing mutations in F(1)-ATPase structural genes. Mitochondria isolated from yme1 yeast generated a membrane potential upon the addition of succinate, but unlike mitochondria isolated either from wild-type yeast or from yeast bearing yme1 and a suppressing mutation, were unable to generate a membrane potential upon the addition of ATP. Nuclear-encoded F(0) subunits accumulate in yme1 yeast lacking mitochondrial DNA; however, deletion of genes encoding those subunits did not suppress the requirement of yme1 yeast for intact mitochondrial DNA. In contrast, deletion of INH1, which encodes an inhibitor of the F(1)F(0)-ATPase, partially suppressed the growth defect of yme1 yeast lacking mitochondrial DNA. We conclude that Yme1p is in part responsible for assuring sufficient F(1)F(0)-ATPase activity to generate a membrane potential in mitochondria lacking mitochondrial DNA and propose that Yme1p accomplishes this by catalyzing the turnover of protein inhibitors of the F(1)F(0)-ATPase.","authors":"Kominsky DJ, Brownson MP, Updike DL, Thorsness PE","authors_abbrev":"Kominsky DJ et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2003-01-14","publication_year":"2002","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC70.02c","SPCC965.04c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:32246346","title":"Epigenetic manipulation of filamentous fungi for biotechnological applications: a systematic review.","citation":"Biotechnol Lett 2020 Jun;42(6):885-904","abstract":"The study of the epigenetic regulation of gene function has reached pivotal importance in life sciences in the last decades. The mechanisms and effects of processes such as DNA methylation, histone posttranslational modifications and non-coding RNAs, as well as their impact on chromatin structure and dynamics, are clearly involved in physiology homeostasis in plants, animals and microorganisms. In the fungal kingdom, studies on the model yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe contributed enormously to the elucidation of the eukaryote epigenetic landscape. Epigenetic regulation plays a central role in the expression of virulence attributes of human pathogens such as Candida albicans. In this article, we review the most recent studies on the effects of drugs capable of altering epigenetic states and on the impact of chromatin structure-related genes deletion in filamentous fungi. Emphasis is given on plant and insect pathogens, endophytes, secondary metabolites and cellulases/xylanases producing species.","doi":"10.1007/s10529-020-02871-8","authors":"Poças-Fonseca MJ, Cabral CG, Manfrão-Netto JHC","authors_abbrev":"Poças-Fonseca MJ et al.","pubmed_publication_date":"Jun 2020","pubmed_entrez_date":"2020-04-05","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-04-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16415366","title":"A role for the septation initiation network in septum assembly revealed by genetic analysis of sid2-250 suppressors.","citation":"Genetics 2006 Apr;172(4):2101-12","abstract":"In the fission yeast Schizosaccharomyces pombe the septation initiation network (SIN) is required for stabilization of the actomyosin ring in late mitosis as well as for ring constriction and septum deposition. In a genetic screen for suppressors of the SIN mutant sid2-250, we isolated a mutation, ace2-35, in the transcription factor Ace2p. Both ace2Delta and ace2-35 show defects in cell separation, and both can rescue the growth defects of some SIN mutants at low restrictive temperatures, where the SIN single mutants lyse at the time of cytokinesis. By detailed analysis of the formation and constriction of the actomyosin ring and septum in the sid2-250 mutant at low restrictive temperatures, we show that the lysis phenotype of the sid2-250 mutant is likely due to a weak cell wall and septum combined with enzymatic activity of septum-degrading enzymes. Consistent with the recent findings that Ace2p controls transcription of genes involved in cell separation, we show that disruption of some of these genes can also rescue sid2-250 mutants. Consistent with SIN mutants having defects in septum formation, many SIN mutants can be rescued at the low restrictive temperature by the osmotic stabilizer sorbitol. The small GTPase Rho1 is known to promote cell wall formation, and we find that Rho1p expressed from a multi-copy plasmid can also rescue sid2-250 at the low restrictive temperature. Together these results suggest that the SIN has a role in promoting proper cell wall formation at the division septa.","authors":"Jin QW, Zhou M, Bimbo A, Balasubramanian MK, McCollum D","authors_abbrev":"Jin QW et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-01-18","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9G1.11c","SPCC970.09","SPBC244.01c","SPAC1565.06c","SPAC6G10.12c","SPAC821.09","SPAPYUG7.03c","SPCC188.02","SPAC16A10.04","SPAC23C4.08","SPAC9G1.09","SPAC1F7.04","SPCC1739.11c","SPAC24B11.11c","SPBC428.13c","SPAC14C4.09","SPAC6F12.12","SPBC16A3.01","SPBC21.06c","SPBC24C6.07"],"gene_count":20,"ltp_gene_count":20},{"uniquename":"PMID:9251041","title":"Use of green fluorescent protein for intracellular protein localization in living fission yeast cells.","citation":"Methods Enzymol 1997;283:459-71","abstract":"","authors":"Nabeshima K, Saitoh S, Yanagida M","authors_abbrev":"Nabeshima K et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17456468","title":"The plant homeodomain fingers of fission yeast Msc1 exhibit E3 ubiquitin ligase activity.","citation":"J Biol Chem 2007 Jun 22;282(25):18397-18406","abstract":"The DNA damage checkpoint pathway governs how cells regulate cell cycle progression in response to DNA damage. A screen for suppressors of a fission yeast chk1 mutant defective in the checkpoint pathway identified a novel Schizosaccharomyces pombe protein, Msc1. Msc1 contains 3 plant homeodomain (PHD) finger motifs, characteristically defined by a C4HC3 consensus similar to RING finger domains. PHD finger domains in viral proteins and in the cellular protein kinase MEKK1 (mitogen-activated protein kinase/extracellular signal-regulated kinase kinase kinase 1) have been implicated as ubiquitin E3 protein ligases that affect protein stability. The close structural relationship of PHD fingers to RING fingers suggests that other PHD domain-containing proteins might share this activity. We show that each of the three PHD fingers of Msc1 can act as ubiquitin E3 ligases, reporting for the first time that PHD fingers from a nuclear protein exhibit E3 ubiquitin ligase activity. The function of the PHD fingers of Msc1 is needed to rescue the DNA damage sensitivity of a chk1Delta strain. Msc1 co-precipitates Rhp6, the S. pombe homologue of the human ubiquitin-conjugating enzyme Ubc2. Strikingly, deletion of msc1 confers complete suppression of the slow growth phenotype, UV and hydroxyurea sensitivities of an rhp6 deletion strain and restores deficient histone H3 methylation observed in the rhp6Delta mutant. We speculate that the target of the E3 ubiquitin ligase activity of Msc1 is likely to be a chromatin-associated protein.","doi":"10.1074/jbc.M700729200","authors":"Dul BE, Walworth NC","authors_abbrev":"Dul BE et al.","pubmed_publication_date":"22 Jun 2007","pubmed_entrez_date":"2007-04-26","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC343.11c","SPCC1259.13","SPAC18B11.07c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:7483844","title":"Biochemical similarity of Schizosaccharomyces pombe ras1 protein with RAS2 protein of Saccharomyces cervisiae.","citation":"Yeast 1995 Jul;11(9):801-8","abstract":"Schizosaccharomyces pombe contains single ras oncogene homologue, ras1, that functions in the signal transduction pathway conducting the cell's mating processes. To understand the biochemical basis of yeast ras proteins, we have purified the ras1 protein and compared the major biochemical constants with those of RAS2 protein from Saccharomyces cerevisiae and mammalian ras proteins. The purified ras1 protein showed a remarkably high Kd value for GDP binding (178 nM) and for binding with ATP. In contrast, the Kd value for GTP binding and the rate of GTPase activity were 64 nM and 77 x 10(-6) s-1 at 37 degrees C, respectively; both were higher than normal p21ras protein, but at the same level as the RAS2 protein. We directly measured rate of GTP binding and GDP binding which were 3.9 x 10(-3) s-1 and 1.8 x 10(-3) s-1 at 30 degrees C, respectively. On the other hand, exchange rates between bound and free nucleotides remained almost constant throughout the tested combination of GTP and GDP, and were several-fold lower than the binding rate. These results suggest that the release of the guanine nucleotide is the rate-limiting step in the ras-GTP/GDP cycle. As a whole, the biochemical properties of the ras1 protein are close to those of the RAS2 protein, although these two proteins function differently in the signal transduction pathway in the cells.","authors":"Onozawa T, Danjoh I, Fujiyama A","authors_abbrev":"Onozawa T et al.","pubmed_publication_date":"Jul 1995","pubmed_entrez_date":"1995-07-01","publication_year":"1995","canto_session_key":"2aa0a060b6a540d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-02-07 18:38:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-31 22:59:08","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-31"},{"uniquename":"PMID:17535257","title":"Two-step, extensive alterations in the transcriptome from G0 arrest to cell division in Schizosaccharomyces pombe.","citation":"Genes Cells 2007 May;12(5):677-92","abstract":"Body cells in multicellular organisms are in the G0 state, in which cells are arrested and terminally differentiated. To understand how the G0 state is maintained, the genes that are specifically expressed or repressed in G0 must be identified, as they control G0. In the fission yeast Schizosaccharomyces pombe, haploid cells are completely arrested under nitrogen source starvation with high viability. We examined the global transcriptome of G0 cells and cells on the course to resume vegetative growth. Approximately 20% of the transcripts of approximately 5000 genes increased or decreased more than fourfold in the two-step transitions that occur prior to replication. Of the top 30 abundant transcripts in G0, 23 were replaced by ribosome- and translation-related transcripts in the dividing vegetative state. Eight identified clusters with distinct alteration patterns of approximately 2700 transcripts were annotated by Gene Ontology. Disruption of 53 genes indicated that nine of them were necessary to support the proper G0 state. These nine genes included two C2H2 zinc finger transcription factors, a cyclin-like protein implicated in phosphorylation of RNA polymerase II, two putative autophagy regulators, a G-protein activating factor, and two CBS domain proteins, possibly involved in AMP-activated kinase.","authors":"Shimanuki M, Chung SY, Chikashige Y, Kawasaki Y, Uehara L, Tsutsumi C, Hatanaka M, Hiraoka Y, Nagao K, Yanagida M","authors_abbrev":"Shimanuki M et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-05-31","publication_year":"2007","canto_session_key":"a9239ad887c0b6b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-09-29 09:45:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-09-29 09:43:21","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-09-29"},{"uniquename":"PMID:22645654","title":"Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing.","citation":"Open Biol 2011 Dec;1(4):110023","abstract":"Condensin is required for chromosome dynamics and diverse DNA metabolism. How condensin works, however, is not well understood. Condensin contains two structural maintenance of chromosomes (SMC) subunits with the terminal globular domains connected to coiled-coil that is interrupted by the central hinge. Heterotrimeric non-SMC subunits regulate SMC. We identified a novel fission yeast SMC hinge mutant, cut14-Y1, which displayed defects in DNA damage repair and chromosome segregation. It contains an amino acid substitution at a conserved hinge residue of Cut14/SMC2, resulting in diminished DNA binding and annealing. A replication protein A mutant, ssb1-418, greatly alleviated the repair and mitotic defects of cut14-Y1. Ssb1 protein formed nucleolar foci in cut14-Y1 cells, but the number of foci was diminished in cut14-Y1 ssb1-418 double mutants. Consistent with the above results, Ssb1 protein bound to single-strand DNA was removed by condensin or the SMC dimer through DNA reannealing in vitro. Similarly, RNA hybridized to DNA may be removed by the SMC dimer. Thus, condensin may wind up DNA strands to unload chromosomal components after DNA repair and prior to mitosis. We show that 16 suppressor mutations of cut14-Y1 were all mapped within the hinge domain, which surrounded the original L543 mutation site.","doi":"10.1098/rsob.110023","authors":"Akai Y, Kurokawa Y, Nakazawa N, Tonami-Murakami Y, Suzuki Y, Yoshimura SH, Iwasaki H, Shiroiwa Y, Nakamura T, Shibata E, Yanagida M","authors_abbrev":"Akai Y et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2012-05-31","publication_year":"2011","canto_session_key":"aedeeafb353d00c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Norihiko Nakazawa","canto_first_approved_date":"2017-11-26 02:17:51","canto_approved_date":"2025-09-04 07:18:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-07 07:11:25","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Norihiko Nakazawa","community_curator":true,"annotation_count":37,"orcid":"0000-0001-8386-0812","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPCC1259.13","SPCC188.03","SPCC4G3.05c","SPBC646.14c","SPBC216.05","SPBC336.04","SPAC20G4.04c","SPBC776.13","SPBC216.06c","SPBC3E7.08c","SPAC1952.07","SPAC1F7.05","SPCC126.02c","SPBP4H10.06c","SPCC18B5.11c","SPBC660.13c","SPAC9E9.08","SPAC30D11.10","SPBC342.05","SPAC8E11.02c","SPCC306.03c","SPBC146.03c","SPAC664.07c","SPAC14C4.13","SPAC17A2.13c"],"gene_count":26,"ltp_gene_count":26,"approved_date":"2017-11-26"},{"uniquename":"EMBL:SPC05276","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8790914","title":"Identification and phylogenetic classification of eleven putative P-type calcium transport ATPase genes in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Biosci Rep 1996 Apr;16(2):75-85","abstract":"Calcium is an essential second messenger in yeast metabolism and physiology. So far, only four genes coding for calcium translocating ATPases had been discovered in yeast. The recent completion of the yeast Saccharomyces cerevisiae genome allowed us to identify six new putative Ca(++)-ATPases encoding genes. Protein sequence homology analysis and phylogenetic classification of all putative Ca(++)-ATPase gene products from the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe reveal three clusters of homologous proteins. Two of them comprises seven proteins which might belong to a new class of P-type ATPases of unknown subcellular location and of unknown physiological function.","authors":"Catty P, Goffeau A","authors_abbrev":"Catty P et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12548977","title":"[The different effects of CaM inhibitors of phenothiazines on the proliferation of Saccharomyces cerevisiae and Schizosaccharomyces pombe].","citation":"Shi Yan Sheng Wu Xue Bao 2000 Jun;33(2):141-9","abstract":"Low concentration of phenothiazines apparently stimulated the proliferation of S. pombe, the cell density incubated for 54 hours by preincubating the cells with 20 mumol/L trifluoperazine (TFP) in the EMM-Ca medium was two times more than the control. The stimulation was more obvious with lowing the concentration of calcium in the culture medium, TFP cooperated and complemented with calcium in stimulating the proliferation of S. pombe. When the original inoculated cell density was 5 x 10(6) cells/ml or during the logarithm period of growth curve, the proliferation of S. pombe wasn't affected by the low concentration of TFP. While when the concentration of TFP was increased to 100 mumol/L, the promotion effect of TFP on proliferation of S. pombe declined obviously and the proliferation of S. pombe was inhibited completely when TFP up to 200 mumol/L. The cell proliferation also could be inhibited by CaM antagonist W7 and W7-agarose, the inhibition was increased with increasing the concentration of antagonist. On the other hand, 20 mumol/L TFP used by the same method as above arrested the cell division cycle of Saccharomyces cerevisiae at a single G2 + M nuclei stage, the cells was penetrated easily by TFP, the fluorescence in cells was very obvious when TFP was 20 mumol/L, but it was difficult to penetrat by TFP in the cells of S. pombe and the Ca2+ influx of S. pombe could be induced rapidly by 20 mumol/L TFP. In this article, the cause of different effects of TFP on cell proliferation of S. pombe and S. cerevisiae was discussed, it was due to the difference of penetration of TFP and stimulation by calcium in the two kinds of cells.","authors":"Lu L, Jiang AQ, Yuan S, Yin LH, Huang WY, Fan WS","authors_abbrev":"Lu L et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2003-01-29","publication_year":"2000","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16981199","title":"Site-specific recombination systems for the genetic manipulation of eukaryotic genomes.","citation":"Genesis 2006 Oct;44(10):465-76","abstract":"Site-specific recombination systems, such as the bacteriophage Cre-lox and yeast FLP-FRT systems, have become valuable tools for the rearrangement of DNA in higher eukaryotes. As a first step to expanding the repertoire of recombination tools, we screened recombination systems derived from the resolvase/invertase family for site-specific recombinase activity in the fission yeast Schizosaccharomyces pombe. Here, we report that seven recombination systems, four from the small serine resolvase subfamily (CinH, ParA, Tn1721, and Tn5053) and three from the large serine resolvase subfamily (Bxb1, TP901-1, and U153), can catalyze site-specific deletion in S. pombe. Those from the large serine resolvase subfamily were also capable of site-specific integration and inversion. In all cases, the recombination events were precise. Functional operation of these recombination systems in the fission yeast holds promise that they may be further developed as recombination tools for the site-specific rearrangement of plant and animal genomes.","authors":"Thomson JG, Ow DW","authors_abbrev":"Thomson JG et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-09-19","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12960401","title":"Intra-G1 arrest in response to UV irradiation in fission yeast.","citation":"Proc Natl Acad Sci U S A 2003 Sep 16;100(19):10758-63","abstract":"G1 is a crucial phase of cell growth because the decision to begin another mitotic cycle is made during this period. Occurrence of DNA damage in G1 poses a particular challenge, because replication of damaged DNA can be deleterious and because no sister chromatid is present to provide a template for recombinational repair. We therefore have studied the response of Schizosaccharomyces pombe cells to UV irradiation in early G1 phase. We find that irradiation results in delayed progression through G1, as manifested most critically in the delayed formation of the pre-replication complex. This delay does not have the molecular hallmarks of known checkpoint responses: it is independent of the checkpoint proteins Rad3, Cds1, and Chk1 and does not elicit inhibitory phosphorylation of Cdc2. Irradiated cells eventually progress into S phase and arrest in early S by a rad3- and cds1-dependent mechanism, most likely the intra-S checkpoint. Caffeine alleviates both the intra-G1- and intra-S-phase delays. We suggest that intra-G1 delay may be widely conserved and discuss significance and possible mechanisms.","authors":"Nilssen EA, Synnes M, Kleckner N, Grallert B, Boye E","authors_abbrev":"Nilssen EA et al.","pubmed_publication_date":"16 Sep 2003","pubmed_entrez_date":"2003-09-10","publication_year":"2003","canto_session_key":"df173adeebbaeb75","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-10-19 15:21:04","canto_approved_date":"2023-04-08 18:16:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-19 15:20:58","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC14C8.07c","SPBC216.05","SPBC11B10.09","SPCC1259.13","SPAPB2B4.03"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2015-10-19"},{"uniquename":"PMID:14986133","title":"A description of the Mei2-like protein family; structure, phylogenetic distribution and biological context.","citation":"Dev Genes Evol 2004 Mar;214(3):149-58","abstract":"The Schizosaccharomyces pombe Mei2 gene encodes an RNA recognition motif (RRM) protein that stimulates meiosis upon binding a specific non-coding RNA and subsequent accumulation in a \"mei2-dot\" in the nucleus. We present here the first systematic characterization of the family of proteins with characteristic Mei2-like amino acid sequences. Mei2-like proteins are an ancient eukaryotic protein family with three identifiable RRMs. The C-terminal RRM (RRM3) is unique to Mei2-like proteins and is the most highly conserved of the three RRMs. RRM3 also contains conserved sequence elements at its C-terminus not found in other RRM domains. Single copy Mei2-like genes are present in some fungi, in alveolates such as Paramecium and in the early branching eukaryote Entamoeba histolytica, while plants contain small families of Mei2-like genes. While the C-terminal RRM is highly conserved between plants and fungi, indicating conservation of molecular mechanisms, plant Mei2-like genes have changed biological context to regulate various aspects of developmental pattern formation.","authors":"Jeffares DC, Phillips MJ, Moore S, Veit B","authors_abbrev":"Jeffares DC et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-02-27","publication_year":"2004","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9278510","title":"Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase.","citation":"Science 1997 Sep 05;277(5331):1495-7","abstract":"Arrest of the cell cycle at the G2 checkpoint, induced by DNA damage, requires inhibitory phosphorylation of the kinase Cdc2 in both fission yeast and human cells. The kinase Wee1 and the phosphatase Cdc25, which regulate Cdc2 phosphorylation, were evaluated as targets of Chk1, a kinase essential for the checkpoint. Fission yeast cdc2-3w Deltacdc25 cells, which express activated Cdc2 and lack Cdc25, were responsive to Wee1 but insensitive to Chk1 and irradiation. Expression of large amounts of Chk1 produced the same phenotype as did loss of the cdc25 gene in cdc2-3w cells. Cdc25 associated with Chk1 in vivo and was phosphorylated when copurified in Chk1 complexes. These findings identify Cdc25, but not Wee1, as a target of the DNA damage checkpoint.","authors":"Furnari B, Rhind N, Russell P","authors_abbrev":"Furnari B et al.","pubmed_publication_date":"05 Sep 1997","pubmed_entrez_date":"1997-09-05","publication_year":"1997","canto_session_key":"f3b2e78baad1483c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-03-07 14:18:08","canto_approved_date":"2019-06-14 12:22:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-09-21 10:58:33","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPCC18B5.03","SPCC1259.13","SPBC660.14","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-03-07"},{"uniquename":"PMID:10366596","title":"A cytoplasmic dynein heavy chain is required for oscillatory nuclear movement of meiotic prophase and efficient meiotic recombination in fission yeast.","citation":"J Cell Biol 1999 Jun 14;145(6):1233-49","abstract":"Meiotic recombination requires pairing of homologous chromosomes, the mechanisms of which remain largely unknown. When pairing occurs during meiotic prophase in fission yeast, the nucleus oscillates between the cell poles driven by astral microtubules. During these oscillations, the telomeres are clustered at the spindle pole body (SPB), located at the leading edge of the moving nucleus and the rest of each chromosome dangles behind. Here, we show that the oscillatory nuclear movement of meiotic prophase is dependent on cytoplasmic dynein. We have cloned the gene encoding a cytoplasmic dynein heavy chain of fission yeast. Most of the cells disrupted for the gene show no gross defect during mitosis and complete meiosis to form four viable spores, but they lack the nuclear movements of meiotic prophase. Thus, the dynein heavy chain is required for these oscillatory movements. Consistent with its essential role in such nuclear movement, dynein heavy chain tagged with green fluorescent protein (GFP) is localized at astral microtubules and the SPB during the movements. In dynein-disrupted cells, meiotic recombination is significantly reduced, indicating that the dynein function is also required for efficient meiotic recombination. In accordance with the reduced recombination, which leads to reduced crossing over, chromosome missegregation is increased in the mutant. Moreover, both the formation of a single cluster of centromeres and the colocalization of homologous regions on a pair of homologous chromosomes are significantly inhibited in the mutant. These results strongly suggest that the dynein-driven nuclear movements of meiotic prophase are necessary for efficient pairing of homologous chromosomes in fission yeast, which in turn promotes efficient meiotic recombination.","authors":"Yamamoto A, West RR, McIntosh JR, Hiraoka Y","authors_abbrev":"Yamamoto A et al.","pubmed_publication_date":"14 Jun 1999","pubmed_entrez_date":"1999-06-15","publication_year":"1999","canto_session_key":"9b3c0d00dc3aedb7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-12-16 12:54:17","canto_approved_date":"2024-06-28 13:02:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-27 16:11:07","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPAC458.04c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-12-16"},{"uniquename":"PMID:18248428","title":"The pap1(+) gene of fission yeast is transcriptionally regulated by nitrosative and nutritional stress.","citation":"FEMS Microbiol Lett 2008 Mar;280(2):176-81","abstract":"In the current work, regulation of the pap1(+) gene was investigated by the use of the pap1(+)-lacZ fusion gene and semi-quantitative reverse transcriptase-PCR. The synthesis of beta-galactosidase from the pap1(+)-lacZ fusion gene was significantly enhanced by nitric oxide (NO)-generating sodium nitroprusside (SNP) and nitrogen starvation. However, the induction by SNP and nitrogen starvation was observed to be much less in the Pap1p-negative cells harboring the fusion gene. Exogenous NO was more effectively scavenged in the Pap1p-positive cells than in the Pap1p-negative cells. Oxidative stress such as superoxide anion, hydrogen peroxide and cadmium could not give rise to an effect on the synthesis of beta-galactosidase from the fusion gene. The pap1(+) mRNA level was elevated in the wild-type cells by SNP and nitrogen starvation. Catalase activity, a major enzyme positively regulated by Pap1p, was significantly increased only in the Pap1p-positive cells by SNP. In brief, it is demonstrated that transcription of the Schizosaccharomyces pombe pap1(+) gene is positively regulated by nitrosative and nutritional stress in a Pap1p-dependent manner.","doi":"10.1111/j.1574-6968.2007.01056.x","authors":"Kim HJ, Jung HY, Lim CJ","authors_abbrev":"Kim HJ et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-02-06","publication_year":"2008","canto_session_key":"6f00daf0235c513e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-10 15:05:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-10 15:05:46","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-12-10"},{"uniquename":"PMID:10220000","title":"DNA sequencing and analysis of a 40 kb region from the right arm of chromosome II from Schizosaccharomyces pombe.","citation":"Yeast 1999 Mar 30;15(5):419-26","abstract":"We have determined the complete nucleotide sequence of a 39,648 bp segment, contained in cosmid c32F12, derived from the right arm of chromosome II from the fission yeast Schizosaccharomyces pombe. Computer analysis of the sequence revealed the presence of 15 non-overlapping open reading-frames (ORFs) longer than 300 bp and one tRNA-Thr gene. Six ORFs correspond to the previously known rec14+, tug1+, rum1+, pch1+, gpd1+ and cyr1+ genes. Five ORFs code for putative proteins with significant homology to proteins from other organisms. SPBC32F12.01c shows considerable similarity to human neutral sphingomyelinase, whereas SPBC32F12.03c, SPBC32F12.10 and SPBC32F12.14 exhibit strong homology to glutathione peroxidase, phosphoglucomutase and ubiquitin protein ligase E-3 components from various organisms, respectively. The four remaining ORFs identified show weak or non-significant homology to previously sequenced genes. The nucleotide sequence has been submitted to the EMBL database under Accession Number AL023796.","authors":"Sánchez M, del Rey F, Domínguez A, Moreno S, Revuelta JL","authors_abbrev":"Sánchez M et al.","pubmed_publication_date":"30 Mar 1999","pubmed_entrez_date":"1999-04-29","publication_year":"1999","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15650694","title":"Transcriptional regulation of the Schizosaccharomyces pombe gene encoding glutathione S-transferase I by a transcription factor Pap1.","citation":"J Microbiol 2004 Dec;42(4):353-6","abstract":"In a previous study, a gst gene was isolated from the fission yeast Schizosaccharomyces pombe. This gene was dubbed gst I, and was characterized using the gstI-lacZ fusion plasmid pYSH2000. In this work, four additional fusion plasmids, pYSHSD1, pYSHSD2, pYSHSD3 and pYSHSD4, were constructed, in order to carry (respectively) 770, 551, 358 and 151 bp upstream regions from the translational initiation point. The sequence responsible for induction by aluminum, mercury and hydrogen peroxide was located in the range between -1,088 and -770 bp upstream of the S. pombe gst I gene. The same region was identified to contain the nucleotide sequence responsible for regulation by Pap1, and has one putative Pap1 binding site, TTACGTAT, located in the range between -954 approximately -947 bp upstream of the gst I gene. Negatively acting sequences are located between -1,088 and -151 bp. These findings imply that the Pap1 protein is involved in basal and inducible transcription of the gst I gene in the fission yeast S. pombe.","authors":"Kim HG, Kim BC, Kim K, Park EH, Lim CJ","authors_abbrev":"Kim HG et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2005-01-15","publication_year":"2004","canto_session_key":"aa227d6105947e03","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-26 08:24:53","canto_approved_date":"2024-03-28 18:23:19","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-11-26 08:24:47","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC191.09c","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-26"},{"uniquename":"EMBL:AU007393","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15835347","title":"Optical micromanipulations inside yeast cells.","citation":"Appl Opt 2005 Apr 10;44(11):2001-7","abstract":"We present a combination of nonlinear microscopy and optical trapping applied to three-dimensional imaging and manipulation of intracellular structures in living cells. We use Titanium-sapphire laser pulses for nonlinear microscopy of the nuclear envelope and the microtubules marked with green fluorescent protein in fission yeast. The same laser source is also used to trap small lipid granules naturally present in the cell. The trapped granule is used as a handle to exert a pushing force on the cell nucleus. The granule is moved in a raster-scanning fashion to cover the area of the nucleus and hence displace the nucleus away from its normal position in the center of the cell. Such indirect manipulations of an organelle (e.g., nucleus) can be useful when direct trapping of the chosen organelle is disadvantageous or inefficient. We show that nonlinear microscopy and optical manipulation can be performed without substantial damage or heating of the cell. We present this method as an important tool in cell biology for manipulation of specific structures, as an alternative to genetic and biochemical methods. This technique can be applied to several fundamental problems in cell biology, including the mechanism of nuclear positioning and the spatial coordination of nuclear and cell division.","authors":"Sacconi L, Tolić-Nørrelykke IM, Stringari C, Antolini R, Pavone FS","authors_abbrev":"Sacconi L et al.","pubmed_publication_date":"10 Apr 2005","pubmed_entrez_date":"2005-04-20","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21089614","title":"[Analysis of the regulatory mechanism for the constitutive splicing using molecular genetics in fission yeast].","citation":"Tanpakushitsu Kakusan Koso 2009 Dec;54(16 Suppl):2038-43","abstract":"","authors":"Haraguchi N, Tani T","authors_abbrev":"Haraguchi N et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2010-11-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPSUM1","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR22765","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3A12.03c","SPAC57A7.09","HGNC:18126","HGNC:10057"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:36439849","title":"Screening low-methanol and high-aroma produced yeasts for cider fermentation by transcriptive characterization.","citation":"Front Microbiol 2022;13:1042613","abstract":"The commercial active dry yeast strains used for cider production in China are far behind the requirements of the cider industry development in recent decades. In this study, eight yeasts, including  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe ,  Pichia bruneiensis , and  Pichia kudriavzevii , were screened and assessed by growth performance, methanol production, aroma analysis, and their transcriptive characterization.  Saccharomyces cerevisiae  strains WFC-SC-071 and WFC-SC-072 were identified as promising alternatives for cider production. Strains WFC-SC-071 and WFC-SC-072 showed an excellent growth capacity characterized by 91.6 and 88.8% sugar utilization, respectively. Methanol production by both strains was below 200 mg/L. Key aroma compounds imparting cider appreciably characteristic aroma increased in cider fermented by strains WFC-SC-071 and WFC-SC-072. RT-qPCR analysis suggested that most genes associated with growth capacity, carbohydrate uptake, and aroma production were upregulated in WFC-SC-071 and WFC-SC-072. Overall, two  Saccharomyces cerevisiae  strains are the optimal starters for cider production to enable the diversification of cider, satisfy the differences in consumer demand, and promote cider industry development.","doi":"10.3389/fmicb.2022.1042613","authors":"Liu L, Zhao PT, Hu CY, Tian D, Deng H, Meng YH","authors_abbrev":"Liu L et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-11-28","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-11-29 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2837764","title":"Small ribonucleoproteins in Schizosaccharomyces pombe and Yarrowia lipolytica homologous to signal recognition particle.","citation":"Proc Natl Acad Sci U S A 1988 Jun;85(12):4315-9","abstract":"We have partially purified ribonucleoproteins (RNPs) from Schizosaccharomyces pombe and Yarrowia lipolytica with properties resembling those of mammalian signal recognition particle (SRP). In both species of yeast we have identified a single major RNA species in the size range of SRP RNA (256 nucleotides in S. pombe and 270 nucleotides in Y. lipolytica) present in postribosomal salt extracts of the cytoplasm. The RNPs containing these RNAs sediment in sucrose gradients at 11 S and 10 S for S. pombe and Y. lipolytica, respectively. Analysis of genomic clones of these RNAs has revealed that (i) they are encoded by single copy genes; (ii) they share two short conserved sequences that match the A and B boxes defined for polymerase III promoters; (iii) they can be folded into secondary structures that closely match that defined by phylogenetic analysis of higher eukaryotic SRP RNAs; and (iv) they show primary sequence conservation in short regions predicted to be single stranded. Both of the yeast RNAs bind under stringent conditions to canine SRP proteins. Most importantly, RNase protection of the S. pombe RNA by the individual canine SRP proteins, p19 and p68/72, shows that the proteins recognize homologous elements of the mammalian and yeast RNA. Taken together these data suggest strongly that we have identified yeast SRP homologues.","authors":"Poritz MA, Siegel V, Hansen W, Walter P","authors_abbrev":"Poritz MA et al.","pubmed_publication_date":"Jun 1988","pubmed_entrez_date":"1988-06-01","publication_year":"1988","canto_session_key":"cf0619f59726aa6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-06-09 15:17:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-09 15:17:24","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.98"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-09"},{"uniquename":"PMID:8978688","title":"Fission yeast Cut1 and Cut2 are essential for sister chromatid separation, concentrate along the metaphase spindle and form large complexes.","citation":"EMBO J 1996 Dec 02;15(23):6617-28","abstract":"Fission yeast Schizosaccharomyces pombe temperature-sensitive (ts) cut1 mutants fail to separate sister chromatids in anaphase but the cells continue to divide, leading to bisection of the undivided nucleus (the cut phenotype). If cytokinesis is blocked, replication continues, forming a giant nucleus with polyploid chromosomes. We show here that the phenotype of ts cut2-364 is highly similar to that of cut1 and that the functions of the gene products of cut1+ and cut2+ are closely interrelated. The cut1+ and cut2+ genes are essential for viability and interact genetically. Cut1 protein concentrates along the short spindle in metaphase as does Cut2. Cut1 (approximately 200 kDa) and Cut2 (42 kDa) associate, as shown by immunoprecipitation, and co-sediment as large complexes (30 and 40S) in sucrose gradient centrifugation. Their behavior in the cell cycle is strikingly different, however: Cut2 is degraded in anaphase by the same proteolytic machinery used for the destruction of cyclin B, whereas Cut1 exists throughout the cell cycle. The essential function of the Cut1-Cut2 complex which ensures sister chromatid separation may be regulated by Cut2 proteolysis. The C-terminal region of Cut1 is evolutionarily conserved and similar to that of budding yeast Esp1, filamentous fungi BimB and a human protein.","authors":"Funabiki H, Kumada K, Yanagida M","authors_abbrev":"Funabiki H et al.","pubmed_publication_date":"02 Dec 1996","pubmed_entrez_date":"1996-12-02","publication_year":"1996","canto_session_key":"ec89f0bd010d8a38","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-09-06 13:56:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-04 14:48:36","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c","SPCC1739.11c","SPBC14C8.01c","SPCC5E4.04"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-09-04"},{"uniquename":"PMID:25519804","title":"Nonsense codon suppression in fission yeast due to mutations of tRNA(Ser.11) and translation release factor Sup35 (eRF3).","citation":"Curr Genet 2015 May;61(2):165-73","abstract":"In the fission yeast Schizosaccharomyces pombe, sup9 mutations can suppress the termination of translation at nonsense (stop) codons. We localized sup9 physically to the spctrnaser.11 locus and confirmed that one allele (sup9-UGA) alters the anticodon of a serine tRNA. We also found that another purported allele is not allelic. Instead, strains with that suppressor (renamed sup35-F592S) have a single base pair substitution (T1775C) that introduces an amino acid substitution in the Sup35 protein (Sup35-F592S). Reduced functionality of Sup35 (eRF3), the ubiquitous guanine nucleotide-responsive translation release factor of eukaryotes, increases read-through of stop codons. Tetrad dissection revealed that suppression is tightly linked to (inseparable from) the sup35-F592S mutation and that there are no additional extragenic modifiers. The Mendelian inheritance indicates that the Sup35-F592S protein does not adopt an infectious amyloid state ([PSI (+)] prion) to affect suppression, consistent with recent evidence that fission yeast Sup35 does not form prions. We also report that sup9-UGA and sup35-F592S exhibit different strengths of suppression for opal stop codons of ade6-M26 and ade6-M375. We discuss possible mechanisms for the variation in suppressibility exhibited by the two alleles.","doi":"10.1007/s00294-014-0465-7","authors":"Protacio RU, Storey AJ, Davidson MK, Wahls WP","authors_abbrev":"Protacio RU et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2014-12-19","publication_year":"2015","canto_session_key":"466c4197f9cf80c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Reine Protacio","canto_first_approved_date":"2015-08-10 09:45:12","canto_approved_date":"2021-11-22 17:25:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-07-30 15:16:47","canto_added_date":"2014-12-20 01:16:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Reine Protacio","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC584.04","SPCTRNASER.11","SPCC1322.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-08-10"},{"uniquename":"PMID:11230130","title":"Fission yeast Pom1p kinase activity is cell cycle regulated and essential for cellular symmetry during growth and division.","citation":"EMBO J 2001 Mar 01;20(5):1064-73","abstract":"Schizosaccharomyces pombe cells grow from both ends during most of interphase and divide symmetrically into two daughter cells. The pom1 gene, encoding a member of the Dyrk family of protein kinases, has been identified through a mutant showing abnormal cellular morphogenesis. Here we show that Pom1p kinase activity is cell cycle regulated in correlation with the state of cellular symmetry: the activity is high during symmetrical growth and division, but lower when cells grow at just one end. Point mutations in the catalytic domain lead to asymmetry during both cell growth and division, whilst cells overexpressing Pom1p form additional growing ends. Manipulations of kinase activity indicate a negative role for Pom1p in microtubule growth at cell ends. Pom1p is present in a large protein complex and requires its non-catalytic domain to localize to the cell periphery and its kinase activity to localize to cell ends. These data establish that Pom1p kinase activity plays an important role in generating cellular symmetry and suggest that there may be related roles of homologous protein kinases ubiquitously present in all eukaryotes.","authors":"Bähler J, Nurse P","authors_abbrev":"Bähler J et al.","pubmed_publication_date":"01 Mar 2001","pubmed_entrez_date":"2001-03-07","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F7.03c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:8052229","title":"Structural analyses of DNA fragments integrated by illegitimate recombination in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1994 Jul 25;244(2):111-9","abstract":"In order to elucidate the mechanisms of illegitimate recombination in eukaryotes, we have studied the structure of DNA fragments integrated by illegitimate recombination into the genome of fission yeast. Nonhomologous recombination was rarely identified when a long region of homology with the chromosomal leu1+ gene was present in the introduced leu1::ura4+ DNA fragment; but a decrease in length of homology leads to an increase in the ratio of non-homologous to homologous recombination events. The introduced DNA fragments were integrated into different sites in the chromosomes by nonhomologous recombination. The results suggested that there are multiple modes of integration; most events simply involve both ends of the fragments, while in other cases, fragments were integrated in a more complicated manner, probably via circularization or multimerization. To analyze the mechanism of the major type of integration, DNA fragments containing the recombination junctions of three recombinants were amplified by inverted polymerase chain reaction (IPCR) and their nucleotide sequences were determined. There was no obvious homology between introduced DNA and chromosomal DNA at these recombination sites. Furthermore it was found that each terminal region of the introduced DNA was deleted, but that there were no or very small deletions in the target sites of chromosomal DNA. Two models are proposed to explain the mechanism of nonhomologous integration.","authors":"Tatebayashi K, Kato J, Ikeda H","authors_abbrev":"Tatebayashi K et al.","pubmed_publication_date":"25 Jul 1994","pubmed_entrez_date":"1994-07-25","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22583368","title":"Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis.","citation":"Biochemistry 2012 Jun 05;51(22):4377-89","abstract":"Monothiol glutaredoxins (Grxs) with a signature CGFS active site and BolA-like proteins have recently emerged as novel players in iron homeostasis. Elegant genetic and biochemical studies examining the functional and physical interactions of CGFS Grxs in the fungi Saccharomyces cerevisiae and Schizosaccharomyces pombe have unveiled their essential roles in intracellular iron signaling, iron trafficking, and the maturation of Fe-S cluster proteins. Biophysical and biochemical analyses of the [2Fe-2S] bridging interaction between CGFS Grxs and a BolA-like protein in S. cerevisiae provided the first molecular-level understanding of the iron regulation mechanism in this model eukaryote and established the ubiquitous CGFS Grxs and BolA-like proteins as novel Fe-S cluster-binding regulatory partners. Parallel studies focused on Escherichia coli and human homologues for CGFS Grxs and BolA-like proteins have supported the studies in yeast and provided additional clues about their involvement in cellular iron metabolism. Herein, we review recent progress in uncovering the cellular and molecular mechanisms by which CGFS Grxs and BolA-like proteins help regulate iron metabolism in both eukaryotic and prokaryotic organisms.","authors":"Li H, Outten CE","authors_abbrev":"Li H et al.","pubmed_publication_date":"05 Jun 2012","pubmed_entrez_date":"2012-05-16","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28366743","title":"Different Functionality of Cdc20 Binding Sites within the Mitotic Checkpoint Complex.","citation":"Curr Biol 2017 Apr 24;27(8):1213-1220","abstract":"The mitotic checkpoint is a cellular safeguard that prevents chromosome missegregation in eukaryotic cells [1, 2]. Suboptimal functioning may foster chromosome missegregation in cancer cells [3]. Checkpoint signaling produces the \"mitotic checkpoint complex\" (MCC), which prevents anaphase by targeting Cdc20, the activator of the anaphase-promoting complex/cyclosome (APC/C). Recent biochemical and structural studies revealed that the human MCC binds two Cdc20 molecules, one (Cdc20 M ) through well-characterized, cooperative binding to Mad2 and Mad3/BubR1 (forming the \"core MCC\") and the other one (Cdc20 A ) through additional binding sequences in Mad3/BubR1 [4-6]. Here, we dissect the different functionality of these sites in vivo. We show in fission yeast that, at low Cdc20 concentrations, Cdc20 M  binding is sufficient for checkpoint activity and Cdc20 A  binding becomes dispensable. Cdc20 A  binding is mediated by the conserved Mad3 ABBA-KEN2-ABBA motif [7, 8], which we find additionally required for binding of the MCC to the APC/C and for MCC disassembly. Strikingly, deletion of the APC/C subunit Apc15 mimics mutations in this motif, revealing a shared function. This function of Apc15 may be masked in human cells by independent mediators of MCC-APC/C binding. Our data provide important in vivo support for the recent structure-based models and functionally dissect three elements of Cdc20 inhibition: (1) sequestration of Cdc20 in the core MCC, sufficient at low Cdc20 concentrations; (2) inhibition of a second Cdc20 through the Mad3 C terminus, independent of Mad2 binding to this Cdc20 molecule; and (3) occupancy of the APC/C with full MCC, where Mad3 and Apc15 are involved.","doi":"10.1016/j.cub.2017.03.007","authors":"Sewart K, Hauf S","authors_abbrev":"Sewart K et al.","pubmed_publication_date":"24 Apr 2017","pubmed_entrez_date":"2017-04-04","publication_year":"2017","canto_session_key":"cb1516626fc1f680","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silke Hauf","canto_first_approved_date":"2020-06-10 13:08:09","canto_approved_date":"2024-04-04 07:21:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-01 13:04:43","canto_added_date":"2017-04-05 00:15:12","annotation_curators":[{"name":"Katharina Sewart","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null},{"name":"Silke Hauf","community_curator":true,"annotation_count":6,"orcid":"0000-0001-5938-721X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.15c","SPCC1322.12c","SPAC821.08c","SPCC1795.01c","SPAC23H3.08c","SPBC83.04","SPBC25H2.13c","SPAC19G12.01c","SPBC20F10.06","SPBC3D6.04c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2020-06-10"},{"uniquename":"PMID:16176104","title":"[Continuous ethanol fermentation using self-flocculating yeast in multi-stage suspended bioreactors coupled with directly recycling of waste distillage].","citation":"Sheng Wu Gong Cheng Xue Bao 2005 Jul;21(4):628-32","abstract":"A fermentation system composed of four airlift suspended-bed bioreactors in series and with a total working volume of 4800 mL was established. Continuous ethanol fermentation using self-flocculating yeast SPSC01, a fusant from Saccharomyces cerevisiae and Schizosaccharomyces pombe, and two-stage enzymatic hydrolyte of dry milling corn powder, was continuously run for 120 days. All of the backset distillage collected after distilling the final beer was used to mix the corn powder and no any other wastes except the solid residue of corn powder was discharged from the fermentation system, which guaranteed the distillage to be recycled at its maximum. The experimental results revealed that both ethanol and residual sugar in the final beer could be maintained relatively stable with their average levels of 93.6 and 7.9 g/L, respectively when the fermentation system was operated at the dilution rate of 0.05 h(-1). Parameter oscillations reported previously were also observed for the first and second bioreactors, but were effectively attenuated thereafter, which indicated that high yeast cell concentrations resulted from the self-immobilization of this special self-flocculating strain contributed to damp these oscillations. The monitoring of residual nitrogen and phosphor indicated that the accumulations of these nutritional elements occurred and the amount of these inorganic salts supplemented in the substrate should be decreased properly.","authors":"Yan Z, Zi LH, Li N, Wang F, Bai FW","authors_abbrev":"Yan Z et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-09-24","publication_year":"2005","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"TreeFam:TF106376","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC777.12c","HGNC:25237","HGNC:15487"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10330167","title":"Basis for the checkpoint signal specificity that regulates Chk1 and Cds1 protein kinases.","citation":"Mol Cell Biol 1999 Jun;19(6):4262-9","abstract":"Six checkpoint Rad proteins (Rad1, Rad3, Rad9, Rad17, Rad26, and Hus1) are needed to regulate checkpoint protein kinases Chk1 and Cds1 in fission yeast. Chk1 is required to prevent mitosis when DNA is damaged by ionizing radiation (IR), whereas either kinase is sufficient to prevent mitosis when DNA replication is inhibited by hydroxyurea (HU). Checkpoint Rad proteins are required for IR-induced phosphorylation of Chk1 and HU-induced activation of Cds1. IR activates Cds1 only during the DNA synthesis (S) phase, whereas HU induces Chk1 phosphorylation only in cds1 mutants. Here, we investigate the basis of the checkpoint signal specificity of Chk1 phosphorylation and Cds1 activation. We show that IR fails to induce Chk1 phosphorylation in HU-arrested cells. Release from the HU arrest following IR causes substantial Chk1 phosphorylation. These and other data indicate that Cds1 prevents Chk1 phosphorylation in HU-arrested cells, which suggests that Cds1 actively suppresses a repair process that leads to Chk1 phosphorylation. Cds1 becomes more highly concentrated in the nucleus only during the S phase of the cell cycle. This finding correlates with S-phase specificity of IR-induced activation of Cds1. However, constitutive nuclear localization of Cds1 does not enhance IR-induced activation of Cds1. This result suggests that Cds1 activation requires DNA structures or protein activities that are present only during S phase. These findings help to explain how Chk1 and Cds1 respond to different checkpoint signals.","authors":"Brondello JM, Boddy MN, Furnari B, Russell P","authors_abbrev":"Brondello JM et al.","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-05-18","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10523629","title":"DNA damage and replication checkpoints in fission yeast require nuclear exclusion of the Cdc25 phosphatase via 14-3-3 binding.","citation":"Mol Cell Biol 1999 Nov;19(11):7410-9","abstract":"In fission yeast as well as in higher eukaryotic organisms, entry into mitosis is delayed in cells containing damaged or unreplicated DNA. This is accomplished in part by maintaining the Cdc25 phosphatase in a phosphorylated form that binds 14-3-3 proteins. In this study, we generated a mutant of fission yeast Cdc25 that is severely impaired in its ability to bind 14-3-3 proteins. Loss of both the DNA damage and replication checkpoints was observed in fission yeast cells expressing the 14-3-3 binding mutant. These findings indicate that 14-3-3 binding to Cdc25 is required for fission yeast cells to arrest their cell cycle in response to DNA damage and replication blocks. Furthermore, the 14-3-3 binding mutant localized almost exclusively to the nucleus, unlike wild-type Cdc25, which localized to both the cytoplasm and the nucleus. Nuclear accumulation of wild-type Cdc25 was observed when fission yeast cells were treated with leptomycin B, indicating that Cdc25 is actively exported from the nucleus. Nuclear exclusion of wild-type Cdc25 was observed upon overproduction of Rad 24, one of the two fission yeast 14-3-3 proteins, indicating that one function of Rad 24 is to keep Cdc25 out of the nucleus. In support of this conclusion, Rad 24 overproduction did not alter the nuclear location of the 14-3-3 binding mutant. These results indicate that 14-3-3 binding contributes to the nuclear exclusion of Cdc25 and that the nuclear exclusion of Cdc25 is required for a normal checkpoint response to both damaged and unreplicated DNA.","authors":"Zeng Y, Piwnica-Worms H","authors_abbrev":"Zeng Y et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-10-19","publication_year":"1999","canto_session_key":"a820cd9476653a92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-04 11:31:40","canto_approved_date":"2024-06-26 08:50:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-14 19:42:06","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC8E11.02c","SPAC24H6.05","SPBC660.14"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-01-04"},{"uniquename":"PMID:10959826","title":"Cytokinesis: Sid signals septation.","citation":"Curr Biol 2000 Jul 27;10(15):R547-50","abstract":"","authors":"Sawin KE","authors_abbrev":"Sawin KE","pubmed_publication_date":"27 Jul 2000","pubmed_entrez_date":"2000-08-26","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23577148","title":"Paralogous ribosomal protein l32-1 and l32-2 in fission yeast may function distinctively in cellular proliferation and quiescence by changing the ratio of rpl32 paralogs.","citation":"PLoS One 2013;8(4):e60689","abstract":"Fission yeast cells express Rpl32-2 highly while Rpl32-1 lowly in log phase; in contrast, expression of Rpl32-1 raises and reaches a peak level while Rpl32-2 is downregulated to a low basic level when cells enter into stationary phase. Overexpression of Rpl32-1 inhibits cell growth while overexpression of Rpl32-2 does not. Deleting rpl32-2 impairs cell growth more severely than deleting rpl32-1 does. Cell growth impaired by deleting either paralog can be rescued completely by reintroducing rpl32-2, but only partly by rpl32-1. Overexpression of Rpl32-1 inhibits cell division, yielding 4c DNA and multiple septa, while overexpressed Rpl32-2 promotes it. Transcriptomics analysis proved that Rpl32 paralogs regulate expression of a subset of genes related with cell division and stress response in a distinctive way. This functional difference of the two paralogs is due to their difference of 95(th) amino acid residue. The significance of a competitive inhibition between Rpl32 paralogs on their expression is discussed.","doi":"10.1371/journal.pone.0060689","authors":"Sun L, Yang X, Chen F, Li R, Li X, Liu Z, Gu Y, Gong X, Liu Z, Wei H, Huang Y, Yuan S","authors_abbrev":"Sun L et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-04-12","publication_year":"2013","canto_session_key":"044c729eb7c1855b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16C6.11","SPAC3H5.10"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:35439849","title":"Identification of Schizosaccharomyces pombe ird Mutants Resistant to Glucose Suppression and Oxidative Stress.","citation":"Folia Biol (Praha) 2021;67(5-6):163-173","abstract":"Glucose is both the favourite carbon and energy source and acts as a hormone that plays a regulating role in many biological processes. Calorie restriction extends the lifespan in many organisms, including Schizosaccharomyces pombe, while uptake of high glucose leads to undesired results, such as diabetes and aging. In this study, sequence analysis of Schizosaccharomyces pombe ird5 and ird11 mutants was performed using next-generation sequencing techniques and a total of 20 different mutations were detected. ird11 is resistant to oxidative stress without calorie restriction, whereas ird5 displays an adaptive response against oxidative stress. We selected nine candidate mutations located in the non-coding (6) and coding (3) region among a total of 20 different mutations. The nine candidate mutations, which are thought to be responsible for ird5 and ird11 mutant phenotypes, were investigated via forward and backward mutations by using various cloning techniques. The results of this study provide report-like information that will contribute to understanding the relationship between glucose sensing/ signalling and oxidative stress response components.","authors":"Yilmazer M, Bayrak B, Kartal B, Uzuner SK, Palabiyik B","authors_abbrev":"Yilmazer M et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2022-04-19","publication_year":"2021","canto_session_key":"d222cb6185a0bc23","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-04-21 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25306921","title":"Dss1 is a 26S proteasome ubiquitin receptor.","citation":"Mol Cell 2014 Nov 06;56(3):453-461","abstract":"The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome. The proteasome subunits Rpn10 and Rpn13 are known to bind ubiquitin, but genetic and biochemical data suggest the existence of at least one other substrate receptor. Here, we show that the phylogenetically conserved proteasome subunit Dss1 (Sem1) binds ubiquitin chains linked by K63 and K48. Atomic resolution data show that Dss1 is disordered and binds ubiquitin by binding sites characterized by acidic and hydrophobic residues. The complementary binding region in ubiquitin is composed of a hydrophobic patch formed by I13, I44, and L69 flanked by two basic regions. Mutations in the ubiquitin-binding site of Dss1 cause growth defects and accumulation of ubiquitylated proteins.","doi":"10.1016/j.molcel.2014.09.008","authors":"Paraskevopoulos K, Kriegenburg F, Tatham MH, Rösner HI, Medina B, Larsen IB, Brandstrup R, Hardwick KG, Hay RT, Kragelund BB, Hartmann-Petersen R, Gordon C","authors_abbrev":"Paraskevopoulos K et al.","pubmed_publication_date":"06 Nov 2014","pubmed_entrez_date":"2014-10-14","publication_year":"2014","canto_session_key":"a6d8f45c20c2227d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-08-21 11:40:35","canto_approved_date":"2025-04-16 20:18:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-19 05:33:34","canto_added_date":"2015-02-28 01:16:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC342.04","SPAC637.10c","SPCC16A11.16c","SPAC26A3.16","SPBC2D10.12","SPBP19A11.03c","SPAC3G6.02","SPBC337.08c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-08-21"},{"uniquename":"PMID:21273250","title":"Dissection of the relative contribution of the Schizosaccharomyces pombe Ctr4 and Ctr5 proteins to the copper transport and cell surface delivery functions.","citation":"Microbiology (Reading) 2011 Apr;157(Pt 4):1021-1031","abstract":"The Ctr1 family of proteins mediates high-affinity copper (Cu) acquisition in eukaryotic organisms. In the fission yeast Schizosaccharomyces pombe, Cu uptake is carried out by a heteromeric complex formed by the Ctr4 and Ctr5 proteins. Unlike human and Saccharomyces cerevisiae Ctr1 proteins, Ctr4 and Ctr5 are unable to function independently in Cu acquisition. Instead, both proteins physically interact with each other to form a Ctr4-Ctr5 heteromeric complex, and are interdependent for secretion to the plasma membrane and Cu transport activity. In this study, we used S. cerevisiae mutants that are defective in high-affinity Cu uptake to dissect the relative contribution of Ctr4 and Ctr5 to the Cu transport function. Functional complementation and localization assays show that the conserved Met-X(3)-Met motif in transmembrane domain 2 of the Ctr5 protein is dispensable for the functionality of the Ctr4-Ctr5 complex, whereas the Met-X(3)-Met motif in the Ctr4 protein is essential for function and for localization of the hetero-complex to the plasma membrane. Moreover, Ctr4/Ctr5 chimeric proteins reveal unique properties found either in Ctr4 or in Ctr5, and are sufficient for Cu uptake on the cell surface of Sch. pombe cells. Functional chimeras contain the Ctr4 central and Ctr5 carboxyl-terminal domains (CTDs). We propose that the Ctr4 central domain mediates Cu transport in this hetero-complex, whereas the Ctr5 CTD functions in the regulation of trafficking of the Cu transport complex to the cell surface.","doi":"10.1099/mic.0.046854-0","authors":"Beaudoin J, Thiele DJ, Labbé S, Puig S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2011-01-29","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20024080","title":"Metabolic profiling of the fission yeast S. pombe: quantification of compounds under different temperatures and genetic perturbation.","citation":"Mol Biosyst 2010 Jan;6(1):182-98","abstract":"Metabolomics is a rapidly growing branch of post-genomic chemical biology. The fission yeast Schizosaccharomyces pombe is an excellent eukaryotic model organism. Although the entire S. pombe genome has been sequenced and detailed transcriptomic analyses were performed, little metabolic profiling has been done. Here we report the first global semi-quantitative analysis of the S. pombe metabolome using liquid chromatography high-resolution mass spectrometry. Procedures to obtain metabolic compounds from S. pombe extracts were established. One hundred and twenty-three distinct metabolites were identified while approximately 1900 peaks from the approximately 6000 observed were assigned. A software system (MZviewer) was developed to visualize semi-quantitative metabolome data using a dynamically generated scatter plot. We examined the metabolome of S. pombe cells exponentially grown in synthetic culture medium (EMM2) at two different temperatures, 26 degrees C and 36 degrees C. The profiles were similar except for varying amounts of certain amino acids and a significant increase in several compounds at 36 degrees C, such as trehalose (200-fold), glycerophosphoethanolamine (50-fold), arabitol (16-fold), ribulose (8-fold), and ophthalmic acid (5-fold). Reproducibility was demonstrated using a deletion mutant sib1Delta that lacked ferrichrome synthetase and showed no significant metabolic effects except the disappearance of the hexapeptide ferrichrome and the appearance of a putative dipeptide precursor. Taking advantage of the metabolic profile similarity at 26 degrees C and 36 degrees C, we analyzed the metabolome of a temperature-sensitive hcs1-143 mutant defective in the HMG-CoA synthase. As expected, HMG-CoA was decreased. In addition, extensive secondary metabolic effects, including a decrease in urea cycle intermediates and an increase in acetylated compounds, were observed. These findings confirm that S. pombe can be applied as an appropriate model to monitor metabolic responses to environmental conditions as well as genetic perturbations.","doi":"10.1039/b908784b","authors":"Pluskal T, Nakamura T, Villar-Briones A, Yanagida M","authors_abbrev":"Pluskal T et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-12-22","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25090107","title":"The RFTS domain of Raf2 is required for Cul4 interaction and heterochromatin integrity in fission yeast.","citation":"PLoS One 2014;9(8):e104161","abstract":"Centromeric heterochromatin assembly in fission yeast is critical for faithful chromosome segregation at mitosis. Its assembly requires a concerted pathway of events whereby the RNA interference (RNAi) pathway guides H3K9 methylation to target sequences. H3K9 methylation, a hallmark of heterochromatin structure, is mediated by the single histone methyltransferase Clr4 (equivalent to metazoan Suv3-9), a component of the CLRC complex. Loss of or defects in CLRC components disrupts heterochromatin formation due to loss of H3K9 methylation, thus an intact, fully functional CLRC complex is required for heterochromatin integrity. Despite its importance, little is known about the contribution of the CLRC component Raf2 to H3K9 methylation and heterochromatin assembly. We demonstrate that Raf2 is concentrated at centromeres and contrary to other analyses, we find that loss of Raf2 does not affect CENP-ACnp1 localisation or recruitment to centromeres. Our sequence alignments show that Raf2 contains a Replication Foci Targeting Sequence (RFTS) domain homologous to the RFTS domain of the human DNA methyltransferase DNMT1. We show that the Raf2 RFTS domain is required for centromeric heterochromatin formation as its mutation disrupts H3K9 methylation but not the processing of centromeric transcripts into small interfering RNAs (siRNAs) by the RNAi pathway. Analysis of biochemical interactions demonstrates that the RFTS domain mediates an interaction between Raf2 and the CLRC component Cul4. We conclude that the RFTS domain of Raf2 is a protein interaction module that plays an important role in heterochromatin formation at centromeres.","doi":"10.1371/journal.pone.0104161","authors":"White SA, Buscaino A, Sanchez-Pulido L, Ponting CP, Nowicki MW, Allshire RC","authors_abbrev":"White SA et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-08-05","publication_year":"2014","canto_session_key":"3977287ead48ffc4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-08-06 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3A11.08","SPCC970.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12095692","title":"Characterization of a fission yeast subunit of an RNA polymerase I essential transcription initiation factor, SpRrn7h/TAF(I)68, that bridges yeast and mammals: association with SpRrn11h and the core ribosomal RNA gene promoter.","citation":"Gene 2002 May 29;291(1-2):187-201","abstract":"Production of eukaryotic ribosomal RNAs (rRNAs) entails sequence-specific recognition of regulatory sequences in the rRNA gene promoter. A putative subunit of the Schizosaccharomyces pombe essential transcription initiation factor for rRNA synthesis has been identified that shares homology with both murine TAF(I)68 and Saccharomyces cerevisiae Rrn7p, subunits of their species' transcription initiation factor. Affinity purified putative SpRrn7h and associated factors, including a putative Rrn11p homolog, SpRrn11h, bear RNA polymerase I transcription initiation factor activity, and recombinant SpRrn7h associates with S. pombe core rDNA promoter sequences. In the first widespread search for putative homologs of SpRrn7h/murine TAF(I)68, and SpRrn11h/murine TAF(I)48, multiple ones were identified across eukaryotes. Analysis of residues conserved between the fission yeast and murine essential initiation factor subunits aided in these identifications. Sequences in the core rRNA gene promoter contributing to transcriptional activation were investigated, including a perfect TATAAA element located at -35.","authors":"Boukhgalter B, Liu M, Guo A, Tripp M, Tran K, Huynh C, Pape L","authors_abbrev":"Boukhgalter B et al.","pubmed_publication_date":"29 May 2002","pubmed_entrez_date":"2002-07-04","publication_year":"2002","canto_session_key":"a321fd3e3c26eb98","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-12 18:38:27","canto_approved_date":"2024-06-12 18:38:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 18:38:16","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.09c","SPAC18G6.11c","SPBC725.17c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2024-06-12"},{"uniquename":"PMID:1525863","title":"Construction of a tetracycline-inducible promoter in Schizosaccharomyces pombe.","citation":"Curr Genet 1992 Apr;21(4-5):345-9","abstract":"We have developed a tightly repressed Schizosaccharomyces pombe promoter which can be efficiently induced by Tetracycline. This promoter is a derivative of the plant viral cauliflower mosaic virus 35S promoter which normally functions as a strong constitutive promoter in S. pombe. Location of three binding sites for the Tn10-encoded Tet repressor in the vicinity of the TATA-box of the CaMV 35S promoter led to a tight repression of promoter activity in the presence of the Tet repressor protein. Up to a 400-fold induction was observed after addition of the inducer Tetracycline, which inactivates the operator-binding capacity of the repressor.","authors":"Faryar K, Gatz C","authors_abbrev":"Faryar K et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9401022","title":"cps1+, a Schizosaccharomyces pombe gene homolog of Saccharomyces cerevisiae FKS genes whose mutation confers hypersensitivity to cyclosporin A and papulacandin B.","citation":"J Bacteriol 1997 Dec;179(24):7653-62","abstract":"The Schizosaccharomyces pombe cps1-12 (for chlorpropham supersensitive) mutant strain was originally isolated as hypersensitive to the spindle poison isopropyl N-3-chlorophenyl carbamate (chlorpropham) (J. Ishiguro and Y. Uhara, Jpn. J. Genet. 67:97-109, 1992). We have found that the cps1-12 mutation also confers (i) hypersensitivity to the immunosuppressant cyclosporin A (CsA), (ii) hypersensitivity to the drug papulacandin B, which specifically inhibits 1,3-beta-D-glucan synthesis both in vivo and in vitro, and (iii) thermosensitive growth at 37 degrees C. Under any of these restrictive treatments, cells swell up and finally lyse. With an osmotic stabilizer, cells do not lyse, but at 37 degrees C they become multiseptated and multibranched. The cps1-12 mutant, grown at a restrictive temperature, showed an increase in sensitivity to lysis by enzymatic cell wall degradation, in in vitro 1,3-beta-D-glucan synthase activity (173% in the absence of GTP in the reaction), and in cell wall biosynthesis (130% of the wild-type amount). Addition of Ca2+ suppresses hypersensitivity to papulacandin B and septation and branching phenotypes. All of these data suggest a relationship between the cps1+ gene and cell wall synthesis. A DNA fragment containing the cps1+ gene was cloned, and sequence analysis indicated that it encodes a predicted membrane protein of 1,729 amino acids with 15 to 16 transmembrane domains. S. pombe cps1p has overall 55% sequence identity with Fks1p or Fks2p, proposed to be catalytic or associated subunits of Saccharomyces cerevisiae 1,3-beta-D-glucan synthase. Thus, the cps1+ product might be a catalytic or an associated copurifying subunit of the fission yeast 1,3-beta-D-glucan synthase that plays an essential role in cell wall synthesis.","authors":"Ishiguro J, Saitou A, Durán A, Ribas JC","authors_abbrev":"Ishiguro J et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1997-12-24","publication_year":"1997","canto_session_key":"bbcbdad5461798f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-02-08 20:12:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-05 15:24:42","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-05"},{"uniquename":"PMID:2571422","title":"Genetic interactions in the control of mitosis in fission yeast.","citation":"Curr Genet 1989 Jul;16(1):1-6","abstract":"","authors":"MacNeill SA, Nurse P","authors_abbrev":"MacNeill SA et al.","pubmed_publication_date":"Jul 1989","pubmed_entrez_date":"1989-07-01","publication_year":"1989","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11297516","title":"Its8, a fission yeast homolog of Mcd4 and Pig-n, is involved in GPI anchor synthesis and shares an essential function with calcineurin in cytokinesis.","citation":"J Biol Chem 2001 Apr 27;276(17):13579-86","abstract":"In fission yeast, calcineurin is required for cytokinesis and ion homeostasis; however, most of its physiological roles remain obscure. To identify genes that share an essential function with calcineurin, we screened for mutations that confer sensitivity to the calcineurin inhibitor FK506 and high temperature and isolated the mutant its8-1. its8(+) encodes a homolog of the budding yeast MCD4 and human Pig-n that are involved in glycosylphosphatidylinositol (GPI) anchor synthesis. Consistently, reduced inositol labeling of proteins suggested impaired GPI anchor synthesis in its8-1 mutants. The temperature upshift induced a further decrease in inositol labeling and caused dramatic increases in the frequency of septation in its8-1 mutants. BE49385A, an inhibitor of MCD4 and Pig-n, also increased the septation index of the wild-type cell. Osmotic stabilization suppressed these morphological defects, indicating that cell wall weakness caused by impaired GPI anchor synthesis resulted in abnormal cytokinesis. Furthermore, calcineurin-deleted cells exhibited hypersensitivity to BE49385A, and FK506 exacerbated the cytokinesis defects of the its8-1 mutant. Thus, calcineurin and Its8 may share an essential function in cytokinesis and cell viability through the regulation of cell wall integrity.","authors":"Yada T, Sugiura R, Kita A, Itoh Y, Lu Y, Hong Y, Kinoshita T, Shuntoh H, Kuno T","authors_abbrev":"Yada T et al.","pubmed_publication_date":"27 Apr 2001","pubmed_entrez_date":"2001-04-12","publication_year":"2001","canto_session_key":"c8545ae2b64f06c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-02-12 21:02:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-30 13:53:46","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPBC839.08c","SPBC119.08","SPBC19G7.05c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-04-30"},{"uniquename":"PMID:31626996","title":"Multiplexed proteome profiling of carbon source perturbations in two yeast species with SL-SP3-TMT.","citation":"J Proteomics 2020 Jan 06;210:103531","abstract":"Saccharomyces cerevisiae and Schizosaccharomyces pombe are the most commonly studied yeast model systems, yet comparisons of global proteome remodeling between these yeast species are scarce. Here, we profile the proteomes of S. cerevisiae and S. pombe cultured with either glucose or pyruvate as the sole carbon source to define common and distinctive alterations in the protein landscape across species. In addition, we develop an updated streamlined-tandem mass tag (SL-TMT) strategy that substitutes chemical-based precipitation with more versatile bead-based protein aggregation method (SP3) prior to enzymatic digestion and TMT labeling. Our new workflow, SL-SP3-TMT, allow for near-complete proteome profiles in a single experiment for each species. The data reveal expected alterations in protein abundance and differences between species, highlighted complete canonical biochemical pathways, and provided insight into previously uncharacterized proteins. The techniques used herein, namely SL-SP3-TMT, can be applied to virtually any experiment aiming to study remodeling of the proteome using a high-throughput, comprehensive, yet streamlined mass spectrometry-based strategy. SIGNIFICANCE: Saccharomyces cerevisiae and Schizosaccharomyces pombe are single-celled eukaryotes that diverged from a common ancestor over a period of 100 million years, such that evolution has driven fundamental differences between the two species. Cellular metabolism and the regulation thereof are vital for living organisms. Here, we hypothesize that large scale proteomic alterations are prevalent upon the substitution of glucose with another carbon source, in this case pyruvate. To efficiently process our samples, we developed an updated streamlined-tandem mass tag (SL-TMT) strategy with more versatile bead-based protein aggregation. The data revealed expected alterations in protein abundance and illustrated differences between species. We highlighted complete canonical biochemical pathways and provided insight into previously uncharacterized proteins.","doi":"10.1016/j.jprot.2019.103531","authors":"Paulo JA, Navarrete-Perea J, Gygi SP","authors_abbrev":"Paulo JA et al.","pubmed_publication_date":"06 Jan 2020","pubmed_entrez_date":"2019-10-19","publication_year":"2020","canto_session_key":"1a487fae53abc65f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-01-29 13:57:04","canto_approved_date":"2021-01-29 13:57:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-29 13:56:57","canto_added_date":"2019-10-20 00:15:05","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":608,"orcid":"0000-0001-6330-7526","file_type":"qualitative_gene_expression","file_name":"PMID_31626996_Paulo_qualitative_expression.txt"}],"genes":["SPAC1952.09c","SPBC13E7.10c","SPBC1734.15","SPCC5E4.05c","SPAPB18E9.04c","SPBC3H7.06c","SPBC609.01","SPCPB1C11.03","SPAC23A1.02c","SPCC4G3.10c","SPBC1198.06c","SPAC25G10.05c","SPBC646.06c","SPAP8A3.07c","SPCC14G10.01","SPBC119.06","SPAC13G7.13c","SPAC1296.03c","SPAC17C9.06","SPBC14C8.05c","SPCC576.01c","SPCC4B3.02c","SPCC1795.06","SPAC1782.11","SPAC17H9.08","SPAC821.10c","SPAC11D3.02c","SPAC29B12.10c","SPCC622.14","SPAC4A8.04","SPBC21D10.06c","SPBC16A3.06","SPAC607.04","SPBPB2B2.06c","SPBP16F5.08c","SPAC23E2.03c","SPCC1235.16","SPBC1773.07c","SPBC3B9.18c","SPCC1223.12c","SPAC4H3.08","SPBC31F10.10c","SPAC23A1.08c","SPBC19G7.03c","SPBC1683.01","SPCC188.13c","SPAC11H11.03c","SPBP23A10.16","SPBC2G2.05","SPBC685.03","SPBC1683.11c","SPAC29B12.08","SPAC6F12.04","SPAC186.04c","SPCC576.04","SPAC29A4.12c","SPAC22A12.06c","SPAC11D3.01c","SPAC1F7.05","SPAC4G9.11c","SPCC16A11.15c","SPCC162.10","SPAC56F8.06c","SPAC13F5.07c","SPAC890.08","SPCC1753.02c","SPBC1539.10","SPAC26A3.16","SPBC18H10.13","SPBC1A4.01","SPAC4F10.17","SPAC3A12.07","SPAC26A3.01","SPAC3A12.08","SPAC22A12.02c","SPBP26C9.02c","SPAPB24D3.06c","SPCC285.07c","SPBC2F12.17","SPCC663.13c","SPBC8D2.02c","SPCC1682.06","SPBC1198.02","SPBC19C7.09c","SPAC8C9.17c","SPBC2A9.02","SPBC1105.14","SPCC663.02","SPCC757.07c","SPCC1281.07c","SPAC4F8.14c","SPBC3E7.12c","SPAPB1E7.10","SPBC887.17","SPAC13A11.06","SPCC1739.07","SPAC890.05","SPBC27B12.01c","SPAC17G6.12","SPAC17A2.04c","SPBC1773.05c","SPAC869.09","SPAC22G7.11c","SPAP7G5.06","SPAC227.04","SPCC31H12.02c","SPBC337.07c","SPAC1D4.04","SPCC61.03","SPAC1142.05","SPAPB8E5.04c","SPBC1D7.05","SPCC338.06c","SPAC6F6.13c","SPAC31G5.19","SPBC21B10.14","SPBC25H2.08c","SPBC725.03","SPBC1683.06c","SPAC521.02","SPBC19C2.01","SPCC320.07c","SPAP27G11.08c","SPAC23D3.14c","SPCC1223.14","SPBC1709.10c","SPBC577.10","SPAC977.16c","SPAC2G11.12","SPAC513.07","SPAC18G6.01c","SPBC14C8.19","SPCC757.02c","SPBC106.10","SPAC4G9.06c","SPBC16D10.04c","SPCC330.21","SPAC630.06c","SPAC343.07","SPAC12B10.11","SPBPB2B2.13","SPBC15D4.03","SPAC977.17","SPAC20H4.04","SPBC359.06","SPAC19D5.02c","SPCC1393.12","SPBC23E6.03c","SPCC4B3.04c","SPAC31A2.02","SPCC569.09","SPCC1235.13","SPAC27D7.03c","SPBC530.09c","SPBC725.07","SPAC1687.01","SPBC660.07","SPAC24C9.13c","SPBC1677.03c","SPCPJ732.03","SPCC548.07c","SPBC16A3.13","SPAPB8E5.10","SPAC32A11.02c","SPAC26A3.11","SPBC1289.14","SPCC965.12","SPAC13C5.04","SPBC3H7.03c","SPAPB2B4.02","SPBC19F8.01c","SPBC1718.06","SPBC460.04c","SPAC4G9.12","SPCC320.05","SPCC548.06c","SPBC1711.18","SPCC4B3.07","SPBC29B5.02c","SPBC365.12c","SPAC3A11.03","SPAC607.02c","SPAC20H4.11c","SPCC1223.02","SPBC2G2.04c","SPAC926.03","SPAC521.05","SPBC19G7.18c","SPAC630.11","SPAC977.14c","SPBC11G11.03","SPAPB24D3.08c","SPCC320.11c","SPAC3F10.10c","SPAC4F8.05c","SPBC32F12.03c","SPBC1677.02","SPCC1183.12","SPCC1322.03","SPAC25B8.13c","SPAC750.01","SPCC1672.04c","SPAC5H10.03","SPBC29A10.02","SPAC823.07","SPBC428.07","SPAC14C4.05c","SPBC2G2.01c","SPAC8F11.09c","SPBC19G7.19","SPAC869.10c","SPBC839.06","SPBC21H7.02","SPBP4G3.02","SPAC19A8.16","SPAC4G9.05","SPBPB21E7.11","SPAC24B11.13","SPAC637.10c","SPCC550.09","SPBC25B2.08","SPBC31A8.01c","SPBC56F2.15","SPCC594.04c","SPAC1B3.16c","SPAC23D3.08","SPBC1683.07","SPCC777.10c","SPCC794.04c","SPAC29A4.17c","SPAC2F7.06c","SPAC3F10.08c","SPAC18G6.06","SPCC16C4.07","SPAPB17E12.10c","SPBC16E9.16c","SPCC737.04","SPAC644.05c","SPBC365.04c","SPAC105.02c","SPBP4H10.10","SPBC27.03","SPAC57A7.05","SPBC12D12.02c","SPAC4D7.02c","SPCC338.12","SPBC19C7.04c","SPAC644.08","SPAC3C7.13c","SPAC4A8.15c","SPAC11D3.16c","SPBC460.01c","SPAC1006.04c","SPAC664.13","SPBC543.02c","SPBC13A2.04c","SPAC18B11.04","SPAC6G9.14","SPCC14G10.03c","SPBP16F5.04","SPCC1827.05c","SPAC4F10.08","SPAC16E8.03","SPCC1884.02","SPBC1685.13","SPBC23G7.06c","SPAC13F5.03c","SPBC24C6.09c","SPBC28F2.05c","SPAPJ691.02","SPCC1682.01","SPBC543.05c","SPBC29A3.18","SPAC23G3.07c","SPCC1020.01c","SPAC1039.11c","SPAP8A3.04c","SPBC26H8.01","SPAC637.03","SPCC191.01","SPAC1782.07","SPBC23E6.06c","SPBC216.01c","SPBC28E12.02","SPBC3B9.06c","SPCC23B6.02c","SPAC3C7.05c","SPAC4H3.10c","SPAC5H10.01","SPAC3H1.07","SPAC26H5.08c","SPBC3H7.09","SPBC36.04","SPBC428.03c","SPAC7D4.06c","SPBC530.10c","SPAC24C9.06c","SPAC17D4.01","SPBC18E5.01","SPAC144.13c","SPAC23D3.10c","SPAC26A3.14c","SPAC806.03c","SPCC1739.08c","SPAC1F7.08","SPAC24H6.13","SPCC830.08c","SPAC139.05","SPAC5H10.06c","SPAC1565.04c","SPBC6B1.05c","SPBC776.15c","SPAC57A7.13","SPBPB2B2.12c","SPCC1020.07","SPBC32H8.04c","SPAC30C2.04","SPCP31B10.06","SPBC1778.05c","SPBPB7E8.01","SPBC15D4.15","SPBC3E7.07c","SPCC18.09c","SPBC25B2.02c","SPBC2G2.17c","SPBC428.10","SPCC970.11c","SPBC1861.06c","SPCC1183.10","SPBC83.04","SPBC725.01","SPCC338.18","SPAC1527.01","SPCC1827.03c","SPBC16E9.05","SPCC1827.06c","SPBPB21E7.01c","SPBC1198.14c","S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Heat Stress Alters the Physical State and Structure of Membranes in Triacylglycerol-Deficient Fission Yeast,  Schizosaccharomyces pombe .","citation":"Cells 2024 Sep 13;13(18)","abstract":"We investigated whether the elimination of two major enzymes responsible for triacylglycerol synthesis altered the structure and physical state of organelle membranes under mild heat shock conditions in the fission yeast,  Schizosaccharomyces pombe . Our study revealed that key intracellular membrane structures, lipid droplets, vacuoles, the mitochondrial network, and the cortical endoplasmic reticulum were all affected in mutant fission yeast cells under mild heat shock but not under normal growth conditions. We also obtained direct evidence that triacylglycerol-deficient cells were less capable than wild-type cells of adjusting their membrane physical properties during thermal stress. The production of thermoprotective molecules, such as HSP16 and trehalose, was reduced in the mutant strain. These findings suggest that an intact system of triacylglycerol metabolism significantly contributes to membrane protection during heat stress.","doi":"10.3390/cells13181543","authors":"Gudmann P, Gombos I, Péter M, Balogh G, Török Z, Vígh L, Glatz A","authors_abbrev":"Gudmann P et al.","pubmed_publication_date":"13 Sep 2024","pubmed_entrez_date":"2024-09-27","publication_year":"2024","canto_session_key":"d179dc008cb95789","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-09-27 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15155581","title":"Chk1 activation requires Rad9 S/TQ-site phosphorylation to promote association with C-terminal BRCT domains of Rad4TOPBP1.","citation":"Genes Dev 2004 May 15;18(10):1154-64","abstract":"To gain insight into the function and organization of proteins assembled on the DNA in response to genotoxic insult we investigated the phosphorylation of the Schizosaccharomyces pombe PCNA-like checkpoint protein Rad9. C-terminal T412/S423 phosphorylation of Rad9 by Rad3(ATR) occurs in S phase without replication stress. Rad3(ATR) and Tel1(ATM) phosphorylate these same residues, plus additional ones, in response to DNA damage. In S phase and after damage, only Rad9 phosphorylated on T412/S423, but not unphosphorylated Rad9, associates with a two-BRCT-domain region of the essential Rad4(TOPBP1) protein. Rad9-Rad4(TOPBP1) interaction is required to activate the Chk1 damage checkpoint but not the Cds1 replication checkpoint. When the Rad9-T412/S423 are phosphorylated, Rad4(TOPBP1) coprecipitates with Rad3(ATR), suggesting that phosphorylation coordinates formation of an active checkpoint complex.","authors":"Furuya K, Poitelea M, Guo L, Caspari T, Carr AM","authors_abbrev":"Furuya K et al.","pubmed_publication_date":"15 May 2004","pubmed_entrez_date":"2004-05-25","publication_year":"2004","canto_session_key":"839bb5efe129c7dc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-10-04 16:35:09","canto_approved_date":"2023-10-19 16:27:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-12 15:07:28","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":53,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPAC664.07c","SPCC18B5.11c","SPAC23C4.18c","SPBC216.05","SPBC342.05","SPCC1259.13","SPCC23B6.03c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2019-10-04"},{"uniquename":"PMID:23770370","title":"Structure of the second RRM domain of Nrd1, a fission yeast MAPK target RNA binding protein, and implication for its RNA recognition and regulation.","citation":"Biochem Biophys Res Commun 2013 Jul 19;437(1):12-7","abstract":"Negative regulator of differentiation 1 (Nrd1) is known as a negative regulator of sexual differentiation in fission yeast. Recently, it has been revealed that Nrd1 also regulates cytokinesis, in which physical separation of the cell is achieved by a contractile ring comprising many proteins including actin and myosin. Cdc4, a myosin II light chain, is known to be required for cytokinesis. Nrd1 binds and stabilizes Cdc4 mRNA, and thereby suppressing the cytokinesis defects of the cdc4 mutants. Interestingly, Pmk1 MAPK phosphorylates Nrd1, resulting in markedly reduced RNA binding activity. Furthermore, Nrd1 localizes to stress granules in response to various stresses, and Pmk1 phosphorylation enhances the localization. Nrd1 consists of four RRM domains, although the mechanism by which Pmk1 regulates the RNA binding activity of Nrd1 is unknown. In an effort to delineate the relationship between Nrd1 structure and function, we prepared each RNA binding domain of Nrd1 and examined RNA binding to chemically synthesized oligo RNA using NMR. The structure of the second RRM domain of Nrd1 was determined and the RNA binding site on the second RRM domain was mapped by NMR. A plausible mechanism pertaining to the regulation of RNA binding activity by phosphorylation is also discussed.","doi":"10.1016/j.bbrc.2013.06.008","authors":"Kobayashi A, Kanaba T, Satoh R, Fujiwara T, Ito Y, Sugiura R, Mishima M","authors_abbrev":"Kobayashi A et al.","pubmed_publication_date":"19 Jul 2013","pubmed_entrez_date":"2013-06-18","publication_year":"2013","canto_session_key":"4e6d88673cb45fbe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-08-20 20:08:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-01 13:26:48","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-08-01","pdb_entries":[{"pdb_id":"2rt3","gene_chains":[{"gene_uniquename":"SPAC2F7.11","chain":"A","position":"188-284"}],"title":"Solution structure of the second RRM domain of Nrd1","entry_authors":"Kobayashi A,Kanaba T,Mishima M","entry_authors_abbrev":"Kobayashi A et al.","reference_uniquename":"PMID:23770370","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:20805322","title":"The mitosis-to-interphase transition is coordinated by cross talk between the SIN and MOR pathways in Schizosaccharomyces pombe.","citation":"J Cell Biol 2010 Sep 06;190(5):793-805","abstract":"The mechanisms that regulate cytoskeletal remodeling during the transition between mitosis and interphase are poorly understood. In fission yeast the MOR pathway promotes actin polarization to cell tips in interphase, whereas the SIN signaling pathway drives actomyosin ring assembly and cytokinesis. We show that the SIN inhibits MOR signaling in mitosis by interfering with Nak1 kinase-mediated activation of the most downstream MOR component, the NDR family kinase Orb6. Inactivation of the MOR may be a key function of the SIN because attenuation of MOR signaling rescued the cytokinetic defects of SIN mutants and allowed weak SIN signaling to trigger ectopic cytokinesis. Furthermore, failure to inhibit the MOR is toxic when the cell division apparatus is compromised. Together, our results reveal a mutually antagonistic relationship between the SIN and MOR pathways, which is important for completion of cytokinesis and coordination of cytoskeletal remodeling at the mitosis-to-interphase transition.","doi":"10.1083/jcb.201002055","authors":"Ray S, Kume K, Gupta S, Ge W, Balasubramanian M, Hirata D, McCollum D","authors_abbrev":"Ray S et al.","pubmed_publication_date":"06 Sep 2010","pubmed_entrez_date":"2010-09-01","publication_year":"2010","canto_session_key":"f4425b94136060a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-10-23 15:03:06","canto_approved_date":"2026-01-31 15:31:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-01 10:50:46","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":70,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":4,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPAC821.12","SPBP19A11.04c","SPAC4A8.15c","SPAC6F6.08c","SPAC24H6.05","SPAC20G8.05c","SPBC428.13c","SPCC1739.11c","SPAC1565.06c","SPBC17F3.02","SPCC18B5.03","SPBC21.06c","SPAC1834.06c","SPBC24C6.07","SPAC9G1.09","SPAC24B11.11c"],"gene_count":17,"ltp_gene_count":17,"approved_date":"2017-10-23"},{"uniquename":"PMID:31000521","title":"Overlapping Roles in Chromosome Segregation for Heterochromatin Protein 1 (Swi6) and DDK in  Schizosaccharomyces pombe .","citation":"Genetics 2019 Jun;212(2):417-430","abstract":"Fission yeast Swi6 is a human HP1 homolog that plays important roles in multiple cellular processes. In addition to its role in maintaining heterochromatin silencing, Swi6 is required for cohesin enrichment at the pericentromere. Loss of Swi6 leads to abnormal mitosis, including defects in the establishment of bioriented sister kinetochores and microtubule attachment. Swi6 interacts with Dfp1, a regulatory subunit of DBF4-dependent kinase (DDK), and failure to recruit Dfp1 to the pericentromere results in late DNA replication. Using the  dfp1-3A  mutant allele, which specifically disrupts Swi6-Dfp1 association, we investigated how interaction between Swi6 and Dfp1 affects chromosome dynamics. We find that disrupting the interaction between Swi6 and Dfp1 delays mitotic progression in a spindle assembly checkpoint-dependent manner. Artificially tethering Dfp1 back to the pericentromere is sufficient to restore normal spindle length and rescue segregation defects in  swi6 -deleted cells. However, Swi6 is necessary for centromeric localization of Rad21-GFP independent of DDK. Our data indicate that DDK contributes to mitotic chromosome segregation in pathways that partly overlap with, but can be separated from both, Swi6 and the other HP1 homolog, Chp2.","doi":"10.1534/genetics.119.302125","authors":"Shen KF, Forsburg SL","authors_abbrev":"Shen KF et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-04-20","publication_year":"2019","canto_session_key":"8ac46a804d130afe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kuo-Fang Shen","canto_first_approved_date":"2020-03-05 14:54:46","canto_approved_date":"2025-09-03 12:28:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-03 16:38:35","canto_added_date":"2019-04-21 00:15:04","annotation_curators":[{"name":"Kuo-Fang Shen","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAP14E8.02","SPAC18G6.02c","SPBC16C6.10","SPBC1105.17","SPBC20F10.06","SPAC664.01c","SPCC550.13"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2020-03-05"},{"uniquename":"PMID:26124291","title":"A stable microtubule array drives fission yeast polarity reestablishment upon quiescence exit.","citation":"J Cell Biol 2015 Jul 06;210(1):99-113","abstract":"Cells perpetually face the decision to proliferate or to stay quiescent. Here we show that upon quiescence establishment, Schizosaccharomyces pombe cells drastically rearrange both their actin and microtubule (MT) cytoskeletons and lose their polarity. Indeed, while polarity markers are lost from cell extremities, actin patches and cables are reorganized into actin bodies, which are stable actin filament-containing structures. Astonishingly, MTs are also stabilized and rearranged into a novel antiparallel bundle associated with the spindle pole body, named Q-MT bundle. We have identified proteins involved in this process and propose a molecular model for Q-MT bundle formation. Finally and importantly, we reveal that Q-MT bundle elongation is involved in polarity reestablishment upon quiescence exit and thereby the efficient return to the proliferative state. Our work demonstrates that quiescent S. pombe cells assemble specific cytoskeleton structures that improve the swiftness of the transition back to proliferation.","doi":"10.1083/jcb.201502025","authors":"Laporte D, Courtout F, Pinson B, Dompierre J, Salin B, Brocard L, Sagot I","authors_abbrev":"Laporte D et al.","pubmed_publication_date":"06 Jul 2015","pubmed_entrez_date":"2015-07-01","publication_year":"2015","canto_session_key":"433d2f2e8d0427b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-09-03 16:39:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-07 10:57:28","canto_added_date":"2015-07-02 00:20:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.15c","SPAC18G6.15","SPAC3C7.12","SPBC902.06","SPAPB1A10.09","SPAPJ760.02c","SPAC664.10","SPCC895.07","SPBC1778.06c","SPCC417.07c","SPAC631.01c","SPAC890.02c","SPCC1223.06","SPAC3G9.12","SPBC2F12.13","SPCC736.14","SPBC800.05c"],"gene_count":17,"ltp_gene_count":11,"approved_date":"2016-07-07"},{"uniquename":"PMID:14757838","title":"Fission yeast Arp6 is required for telomere silencing, but functions independently of Swi6.","citation":"Nucleic Acids Res 2004;32(2):736-41","abstract":"The actin-related proteins (Arps), which are subdivided into at least eight subfamilies, are conserved from yeast to humans. A member of the Arp6 subfamily in Drosophila, Arp4/Arp6, co-localizes with heterochromatin protein 1 (HP1) in pericentric heterochromatin. Fission yeast Schizosaccharomyces pombe possesses both an HP1 homolog and an Arp6 homolog. However, the function of S.pombe Arp6 has not been characterized yet. We found that deletion of arp6(+) impaired telomere silencing, but did not affect centromere silencing. Chromatin immunoprecipitation assays revealed that Arp6 bound to the telomere region. However, unlike Drosophila Arp4/Arp6, S.pombe Arp6 was distributed throughout nuclei. The binding of Arp6 to telomere DNA was not affected by deletion of swi6(+). Moreover, the binding of Swi6 to telomere ends was not affected by deletion of arp6(+). These results suggest that Arp6 and Swi6 function independently at telomere ends. We propose that the Arp6-mediated repression mechanism works side by side with Swi6-based telomere silencing in S.pombe.","authors":"Ueno M, Murase T, Kibe T, Ohashi N, Tomita K, Murakami Y, Uritani M, Ushimaru T, Harata M","authors_abbrev":"Ueno M et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-02-06","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19285940","title":"Sumoylation of RecQ helicase controls the fate of dysfunctional telomeres.","citation":"Mol Cell 2009 Mar 13;33(5):559-69","abstract":"Genome stability depends upon the RecQ helicases, which are conserved from bacteria to man, but little is known about how their myriad activities are regulated. Fission yeast lacking the telomere protein Taz1 (mammalian TRF1/TRF2 ortholog) lose many hallmarks of telomeres, including accurate replication and local protection from DNA repair reactions. Here we show that the RecQ homolog, Rqh1, is sumoylated. Surprisingly, Rqh1 acts on taz1Delta telomeres in a deleterious way, promoting telomere breakage and entanglement. Mutation of Rqh1 sumoylation sites rescues taz1Delta cells from these hazards without dramatically affecting nontelomeric Rqh1 functions. The prominence of Rqh1 in the etiology of several different telomere defects supports the idea that they originate from a common underlying lesion--aberrant processing of the stalled telomeric replication forks that accumulate in the absence of Taz1. Our work underscores the principle that RecQ helicases are \"double-edged swords\" whose activity, while necessary for maintaining genome-wide stability, must be vigilantly controlled.","doi":"10.1016/j.molcel.2009.01.027","authors":"Rog O, Miller KM, Ferreira MG, Cooper JP","authors_abbrev":"Rog O et al.","pubmed_publication_date":"13 Mar 2009","pubmed_entrez_date":"2009-03-17","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21050209","title":"3D visualization of subcellular structures of Schizosaccharomyces pombe by hard X-ray tomography.","citation":"J Microsc 2010 Oct;240(1):14-20","abstract":"Cellular structures of the fission yeast, Schizosaccharomyces pombe, were examined by using hard X-ray tomography. Since cells are nearly transparent to hard X-rays, Zernike phase contrast and heavy metal staining were introduced to improve image contrast. Through using such methods, images taken at 8 keV displayed sufficient contrast for observing cellular structures. The cell wall, the intracellular organelles and the entire structural organization of the whole cells were visualized in three-dimensional at a resolution better than 100 nm. Comparison between phase contrast and absorption contrast was also made, indicating the obvious advantage of phase contrast for cellular imaging at this energy. Our results demonstrate that hard X-ray tomography with Zernike phase contrast is suitable for cellular imaging. Its unique abilities make it have potential to become a useful tool for revealing structural information from cells, especially thick eukaryotic cells.","doi":"10.1111/j.1365-2818.2010.03379.x","authors":"Yang Y, Li W, Liu G, Zhang X, Chen J, Wu W, Guan Y, Xiong Y, Tian Y, Wu Z","authors_abbrev":"Yang Y et al.","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2010-11-06","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24336750","title":"Feedback regulation of SIN by Etd1 and Rho1 in fission yeast.","citation":"Genetics 2014 Feb;196(2):455-70","abstract":"In fission yeast, the septation initiation network (SIN) is thought to promote cytokinesis by downstream activation of Rho1, a conserved GTPase that controls cell growth and division. Here we show that Etd1 and PP2A-Pab1, antagonistic regulators of SIN, are Rho1 regulators. Our genetic and biochemical studies indicate that a C-terminal region of Etd1 may activate Rho1 by directly binding it, whereas an N-terminal domain confers its ability to localize at the growing tips and the division site where Rho1 functions. In opposition to Etd1, our results indicate that PP2A-Pab1 inhibits Rho1. The SIN cascade is upstream-regulated by the Spg1 GTPase. In the absence of Etd1, activity of Spg1 drops down prematurely, thereby inactivating SIN. Interestingly, we find that ectopic activation of Rho1 restores Spg1 activity in Etd1-depleted cells. By using a cytokinesis block strategy, we show that Rho1 is essential to feedback-activate Spg1 during actomyosin ring constriction. Therefore, activation of Spg1 by Rho1, which in turn is regulated by Etd1, uncovers a novel feedback loop mechanism that ensures SIN activity while cytokinesis is progressing.","doi":"10.1534/genetics.113.155218","authors":"Alcaide-Gavilán M, Lahoz A, Daga RR, Jimenez J","authors_abbrev":"Alcaide-Gavilán M et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-12-17","publication_year":"2014","canto_session_key":"44a48bf9af11b88a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC17F3.01c","SPCC645.06c","SPAC1565.06c","SPAC1006.08","SPAC227.07c","SPBC3F6.05","SPAC1F7.04","SPCC645.07"],"gene_count":8,"ltp_gene_count":7},{"uniquename":"PMID:11344166","title":"Essential role of Sna41/Cdc45 in loading of DNA polymerase alpha onto minichromosome maintenance proteins in fission yeast.","citation":"J Biol Chem 2001 Jul 13;276(28):26189-96","abstract":"Assembly of replication complexes at the replication origins is strictly regulated. Cdc45p is known to be a part of the active replication complexes. In Xenopus egg extracts, Cdc45p was shown to be required for loading of DNA polymerase alpha onto chromatin. The fission yeast cdc45 homologue was identified as a suppressor for nda4 and named sna41. Nevertheless, it is not known how Cdc45p facilitates loading of DNA polymerase alpha onto chromatin, particularly to prereplicative complexes. To gain novel insight into the function of this protein in fission yeast, we characterized the fission yeast Cdc45 homologue, Sna41p. We have constructed C-terminally epitope-tagged Sna41p and Pol alpha p and replaced the endogenous genes with the corresponding tagged genes. Analyses of protein-protein interactions in vivo by the use of these tagged strains revealed the following: Sna41p interacts with Pol alpha p throughout the cell cycle, whereas it interacts with Mis5p/Mcm6p in the chromatin fractions at the G(1)-S boundary through S phase. In an initiation-defective sna41 mutant, sna41(goa1), interaction of Pol alpha p with Mis5p is not observed, although Pol alpha p loading onto the chromatin that occurs before G(1) START is not affected. These results show that fission yeast Sna41p facilitates the loading of Pol alpha p onto minichromosome maintenance proteins. Our results are consistent with a model in which loading of Pol alpha p onto replication origins occurs through two steps, namely, loading onto chromatin at preSTART and association with prereplicative complexes at G(1)-S through Sna41p, which interacts with minichromosome maintenance proteins in a cell cycle-dependent manner.","authors":"Uchiyama M, Griffiths D, Arai K, Masai H","authors_abbrev":"Uchiyama M et al.","pubmed_publication_date":"13 Jul 2001","pubmed_entrez_date":"2001-05-10","publication_year":"2001","canto_session_key":"3f8f5cce464b7ae1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-11-13 14:00:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-09-09 07:50:48","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC211.04c","SPAC3H5.06c","SPAC17D4.02","SPAC6B12.10c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-09-09"},{"uniquename":"PMID:10036242","title":"Caffeine can override the S-M checkpoint in fission yeast.","citation":"J Cell Sci 1999 Mar;112 ( Pt 6):927-37","abstract":"The replication checkpoint (or 'S-M checkpoint') control prevents progression into mitosis when DNA replication is incomplete. Caffeine has been known for some time to have the capacity to override the S-M checkpoint in animal cells. We show here that caffeine also disrupts the S-M checkpoint in the fission yeast Schizosaccharomyces pombe. By contrast, no comparable effects of caffeine on the S. pombe DNA damage checkpoint were seen. S. pombe cells arrested in early S phase and then exposed to caffeine lost viability rapidly as they attempted to enter mitosis, which was accompanied by tyrosine dephosphorylation of Cdc2. Despite this, the caffeine-induced loss of viability was not blocked in a temperature-sensitive cdc2 mutant incubated at the restrictive temperature, although catastrophic mitosis was prevented under these conditions. This suggests that, in addition to S-M checkpoint control, a caffeine-sensitive function may be important for maintenance of cell viability during S phase arrest. The lethality of a combination of caffeine with the DNA replication inhibitor hydroxyurea was suppressed by overexpression of Cds1 or Chk1, protein kinases previously implicated in S-M checkpoint control and recovery from S phase arrest. In addition, the same combination of drugs was specifically tolerated in cells overexpressing either of two novel S. pombe genes isolated in a cDNA library screen. These findings should allow further molecular investigation of the regulation of S phase arrest, and may provide a useful system with which to identify novel drugs that specifically abrogate the checkpoint control.","authors":"Wang SW, Norbury C, Harris AL, Toda T","authors_abbrev":"Wang SW et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-02-26","publication_year":"1999","canto_session_key":"e464a50ec363f029","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-07-02 17:15:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-21 17:30:32","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.04","SPAC19D5.03","SPAC31G5.13","SPCC18B5.11c","SPBC11B10.09","SPBC25D12.04","SPCC1259.13"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2014-11-21"},{"uniquename":"EMBL:AJ632013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.47"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU008968","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7590175","title":"The aniline blue fluorochrome specifically stains the septum of both live and fixed Schizosaccharomyces pombe cells.","citation":"FEMS Microbiol Lett 1995 Oct 15;132(3):215-9","abstract":"A novel method is described which uses aniline blue for the specific fluorescent staining of the septa of dividing cells of the fission yeast, Schizosaccharomyces pombe. It gives the same results with live and fixed cells. In fixed or, more generally, dead cells there is no staining of the cytoplasm: this renders aniline blue superior to other dyes previously used to stain the septum of S. pombe. This feature allows quantitative analysis of the septum index for fixed samples and, therefore, makes aniline blue the stain of choice for cell cycle kinetic studies.","authors":"Kippert F, Lloyd D","authors_abbrev":"Kippert F et al.","pubmed_publication_date":"15 Oct 1995","pubmed_entrez_date":"1995-10-15","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19750219","title":"The role of specific checkpoint-induced S-phase transcripts in resistance to replicative stress.","citation":"PLoS One 2009 Sep 11;4(9):e6944","abstract":"Checkpoint activation during S phase modulates transcription. In response to replication arrest, the fission yeast Cds1 checkpoint kinase maintains the normal S-phase transcriptional program by regulating MBF, the S-phase transcription factor. We show that similar regulation occurs in response to DNA damage during S-phase. We test the relative contributions to replication-stress resistance of transcriptional regulation and the two other major checkpoint functions: cell-cycle arrest and fork stabilization. We show that, although transcriptional regulation provides only modest resistance relative to fork stabilization, it contributes significantly to cell survival. Finally, we investigate the roles of two specific transcripts: mik1 and mrc1. These results demonstrate the general importance of checkpoint regulation of G1/S transcription in response to replicative stress and elucidate the specific roles of Mik1 and Mrc1 in the checkpoint.","doi":"10.1371/journal.pone.0006944","authors":"Dutta C, Rhind N","authors_abbrev":"Dutta C et al.","pubmed_publication_date":"11 Sep 2009","pubmed_entrez_date":"2009-09-15","publication_year":"2009","canto_session_key":"9f08d3ae91aed786","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-05-14 13:16:08","canto_approved_date":"2021-01-05 17:14:49","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-05-14 13:16:04","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":40,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.09","SPBC660.14","SPAC694.06c","SPCC18B5.11c","SPBC216.05","SPAC1F7.05","SPBC336.12c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-05-14"},{"uniquename":"EMBL:U66716","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9880916","title":"Genetic control of fission yeast cell wall synthesis: the genes involved in wall biogenesis and their interactions in Schizosaccharomyces pombe.","citation":"Genes Genet Syst 1998 Aug;73(4):181-91","abstract":"The fungal cell wall is an essential structure which protects cells from various environmental stresses such as hyper- or hypo-osmosis, and endows them with specific morphology in response to their life or cell division cycle. In addition, the cell wall has a variety of enzymatic activities per se, which are required for nutritional uptake, secretion, and cell adhesion including mating processes. In addition to these cytological interests, clinical demands to clarify the regulatory mechanisms of cell wall synthesis have been increasing, since the cell wall is a unique and effective target of antifungal agents. However, the molecular mechanisms are poorly understood at present, although the role of several signal transduction pathways have recently been implicated in regulation. In this review, the author focuses on genes and their interactions which are involved in fission yeast cell wall biogenesis.","authors":"Ishiguro J","authors_abbrev":"Ishiguro J","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1999-01-09","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25361970","title":"PomBase 2015: updates to the fission yeast database.","citation":"Nucleic Acids Res 2015 Jan;43(Database issue):D656-61","abstract":"PomBase (http://www.pombase.org) is the model organism database for the fission yeast Schizosaccharomyces pombe. PomBase provides a central hub for the fission yeast community, supporting both exploratory and hypothesis-driven research. It provides users easy access to data ranging from the sequence level, to molecular and phenotypic annotations, through to the display of genome-wide high-throughput studies. Recent improvements to the site extend annotation specificity, improve usability and allow for monthly data updates. Both in-house curators and community researchers provide manually curated data to PomBase. The genome browser provides access to published high-throughput data sets and the genomes of three additional Schizosaccharomyces species (Schizosaccharomyces cryophilus, Schizosaccharomyces japonicus and Schizosaccharomyces octosporus).","doi":"10.1093/nar/gku1040","authors":"McDowall MD, Harris MA, Lock A, Rutherford K, Staines DM, Bähler J, Kersey PJ, Oliver SG, Wood V","authors_abbrev":"McDowall MD et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-11-02","publication_year":"2015","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2014-11-03 01:15:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1668885","title":"Protein phosphatases in cell division: how vital are they?","citation":"Princess Takamatsu Symp 1991;22:137-44","abstract":"In contrast to the wealth of information on cellular function of protein kinases, many of which are known to be the products of proto-oncogenes, little is known about how protein dephosphorylation is involved in growth control of normal and malignant cells. In the present study, roles of protein phosphatases in cell division cycle control were examined by molecular genetic approaches using a lower eukaryote, the fission yeast Schizosaccharomyces pombe. Nine protein phosphatase genes have been so far identified and characterized in this organism. Each of two (dis2+, sds21+, and ppa1+, ppa2+) gene products is highly similar to mammalian type 1 and 2A ser/thr phosphatases, respectively. The ppx1+ product is an intermediate of type 1 and 2A, while the ppb1+ product is similar to Ca(2+)-dependent type 2B. At least two protein tyrosine phosphatase genes (pyp1+ and pyp2+) exist. The cdc25 protein is now established to be a tyrosine phosphatase that activates cdc2 kinase. Some of these phosphatase genes are interrelated but have distinct, essential functions in cell cycle control. Missense mutations, deletions or high dosage expression of these phosphatase genes affect entry into and exit from mitosis, mitotic chromosome disjunction, cell size and cell shape. They seem to interact with the main regulators of mitosis, cdc2, cdc13/cyclin, cdc25 and weel, or with mitotic structural components, such as condensed chromosomes or the spindle apparatus. We show that the product of an essential gene, sds22+, is an important, positive factor in controlling the expression and modulating the activity of dis2 phosphatase.","authors":"Yanagida M, Yamano H, Stone EM, Kinoshita N, Yoshida T, Shiozaki K","authors_abbrev":"Yanagida M et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1717994","title":"Cloning of a human cDNA encoding a CDC2-related kinase by complementation of a budding yeast cdc28 mutation.","citation":"Proc Natl Acad Sci U S A 1991 Oct 15;88(20):9006-10","abstract":"We have cloned two different human cDNAs that can complement cdc28 mutations of budding yeast Saccharomyces cerevisiae. One corresponds to a gene encoding human p34CDC2 kinase, and the other to a gene (CDK2; cell division kinase) that has not been characterized previously. The CDK2 protein is highly homologous to p34CDC2 kinase (65% identical) and more significantly is homologous to Xenopus Eg1 kinase (89% identical), suggesting that CDK2 is the human homolog of Eg1. The human CDC2 and CDK2 genes were both able to complement the inviability of a null allele of S. cerevisiae CDC28. This result indicates that the CDK2 protein has a biological activity closely related to the CDC28 and p34CDC2 kinases. However, CDK2 was unable to complement cdc2 mutants in fission yeast Schizosaccharomyces pombe under the condition where the human CDC2 gene could complement them. CDK2 mRNA appeared late in G1 or in early S phase, slightly before CDC2 mRNA, after growth stimulation in normal human fibroblast cells. These results suggest that in human cells, two different CDC2-like kinases may regulate the cell cycle at distinct stages.","authors":"Ninomiya-Tsuji J, Nomoto S, Yasuda H, Reed SI, Matsumoto K","authors_abbrev":"Ninomiya-Tsuji J et al.","pubmed_publication_date":"15 Oct 1991","pubmed_entrez_date":"1991-10-15","publication_year":"1991","canto_session_key":"629b7c683708e9ba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 12:21:39","canto_session_submitted_date":"2012-03-03 12:21:18","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:21387406","title":"Rec10- and Rec12-independent recombination in meiosis of Schizosaccharomyces pombe.","citation":"Yeast 2011 May;28(5):405-21","abstract":"The Rec10 protein, a component of the linear elements forming along sister chromatids in meiotic prophase of Schizosaccharomyces pombe, plays an important role in the activation of Rec12 for double-strand break formation, and thus the initiation of recombination between homologous chromosomes. Recombination between homologous chromosomes was moderately reduced in homozygous crosses of the C-terminal truncation mutant rec10-155 and strongly in the full deletion allele rec10-175. Both alleles were also tested in two assays for intrachromosomal recombination (PS1 and VL1) and showed only slight reductions, while deletion of rec12 led to a 13-fold reduction. The even stronger reductions in rec10 rec12 double deletion crosses indicate partially redundant functions of Rec10 and Rec12 in the initiation of intrachromosomal recombination. A low level of double-strand breaks has been detected in rec10-175 meiosis at the mbs1 hotspot of recombination, and spore viability in the double mutant was also lower than in the single-deletion mutants. Low levels of apparent crossover and conversion between homologous chromosomes in the absence of Rec12 have been quantified using a newly developed assay. The results also indicate that the functions of Rec10 differ in several respects from those of its distant homologue Red1 in Saccharomyces cerevisiae, including interactions with Hop1 and Mek1 for promotion of recombination between homologues at the expense of sister chromatid recombination.","doi":"10.1002/yea.1847","authors":"Mallela S, Latypov V, Kohli J","authors_abbrev":"Mallela S et al.","pubmed_publication_date":"May 2011","pubmed_entrez_date":"2011-03-10","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25G10.04c","SPAC17A5.11"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:31147736","title":"Unravelling nuclear size control.","citation":"Curr Genet 2019 Dec;65(6):1281-1285","abstract":"Correlation between nuclear and cell size, the nucleocytoplasmic ratio, is a cellular phenomenon that has been reported throughout eukaryotes for more than a century but the mechanisms that achieve it are not well understood. Here, we review work that has shed light on the cellular processes involved in nuclear size control. These studies have implicated nucleocytoplasmic transport, LINC complexes, RNA processing, regulation of nuclear envelope expansion and partitioning of importin α in nuclear size control, moving us closer to a mechanistic understanding of this phenomenon.","doi":"10.1007/s00294-019-00999-3","authors":"Cantwell H, Nurse P","authors_abbrev":"Cantwell H et al.","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-06-01","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-06-01 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7763928","title":"Estimation of the energetic biomass yield and efficiency of oxidative phosphorylation in cell-recycle cultures of Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 1993 Jul;39(4-5):609-14","abstract":"The energetics of growth of the fission yeast Schizosaccharomyces pombe was studied in continuous high-cell concentration cultures using a cell-recycle fermentor. Under non-O2-limited conditions, steady-states were obtained at various specific growth rates (partial cell-recycle) with purely oxidative (glucose limitation) or respiro-fermentative (glucose excess) metabolic behaviour. The stoichiometry of biomass synthesis was established from the elemental composition of the cells and measurements of all the specific metabolic rates, i.e. consumption of glucose and O2 and production of CO2, ethanol and other products. The theoretical yield factor for biomass on glucose was YG,X = 0.85 C-mol.C-mol-1 and maintenance requirements were negligible. Assuming a constant coupling between energy generation and biomass formation for both respirative and respiro-fermentative breakdown of glucose, the biomass yield from ATP (YATP) and the efficiency of oxidative phosphorylation (P/O ratio) could be determined as 9.8 g biomass.mol ATP and 1.28 mol ATP.atom of O2, respectively.","authors":"Humberto de Queiroz J, Uribelarrea JL, Pareilleux A","authors_abbrev":"Humberto de Queiroz J et al.","pubmed_publication_date":"Jul 1993","pubmed_entrez_date":"1993-07-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10370238","title":"First the CDKs, now the DDKs.","citation":"Trends Cell Biol 1999 Jul;9(7):249-52","abstract":"In budding yeast, Dbf4p and Cdc7p control initiation of DNA synthesis. They form a protein kinase - Cdc7p being the catalytic subunit and Dbf4p a cyclin-like molecule that activates the kinase in late G1 phase. Dbf4p also targets Cdc7p to origins of replication, where probable substrates include certain Mcm proteins. Recent studies have identified Dbf4p- and Cdc7p-related proteins in fission yeast and metazoans. These homologues also phosphorylate Mcm proteins and could have a similar function to that of Dbf4p-Cdc7p in budding yeast. Thus, it seems likely that, like the cyclin-dependent kinases (CDKs), the Dbf4p-Cdc7p activity is conserved in all eukaryotes.","authors":"Johnston LH, Masai H, Sugino A","authors_abbrev":"Johnston LH et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-06-17","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:895714","title":"Evidence for second \"prereplicative G2\" repair mechanism, specific for gamma-induced damage, in wild-type Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1977 Jul 20;154(2):129-33","abstract":"The major part of the substantial gamma-resistance of wild-type Schizosaccharomyces pombe appears to be due to prereplicative recombinational repair mechanisms. The existence of a second \"prereplicative G2\" repair pathway, specific for gamma-induced damage, has now been deduced from studies of the effect of the repair inhibitor caffeine on gamma-irradiated G1 phase and G2 phase cells. only G2 cells are additionally inactivated on exposure to caffeine after gamma-irradiation. This shows that both known caffeine-sensitive gamma-repair processes (Gentner and wener, Molec. gen. Genet. 145, 1-5 [1976]) are dependent on the presence of a duplicated genome (2c) at the time of radiation exposure. Pathway I is the known \"prereplicative G2\" repair process (Fabre, Radiation Res. 56, 528-539 [1973]) which is involved in both UV- and gamma-repair, and which requires post-irradiation protein synthesis for activity. Pathway II represents a second distinct \"prereplicative G2\" repair mechanism; it differs from the first in that it is specific for repair of gamma-induced damage and appears to be constitutive.","authors":"Gentner NE","authors_abbrev":"Gentner NE","pubmed_publication_date":"20 Jul 1977","pubmed_entrez_date":"1977-07-20","publication_year":"1977","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26447128","title":"An Ancient Yeast for Young Geneticists: A Primer on the Schizosaccharomyces pombe Model System.","citation":"Genetics 2015 Oct;201(2):403-23","abstract":"The fission yeast Schizosaccharomyces pombe is an important model organism for the study of eukaryotic molecular and cellular biology. Studies of S. pombe, together with studies of its distant cousin, Saccharomyces cerevisiae, have led to the discovery of genes involved in fundamental mechanisms of transcription, translation, DNA replication, cell cycle control, and signal transduction, to name but a few processes. However, since the divergence of the two species approximately 350 million years ago, S. pombe appears to have evolved less rapidly than S. cerevisiae so that it retains more characteristics of the common ancient yeast ancestor, causing it to share more features with metazoan cells. This Primer introduces S. pombe by describing the yeast itself, providing a brief description of the origins of fission yeast research, and illustrating some genetic and bioinformatics tools used to study protein function in fission yeast. In addition, a section on some key differences between S. pombe and S. cerevisiae is included for readers with some familiarity with budding yeast research but who may have an interest in developing research projects using S. pombe.","doi":"10.1534/genetics.115.181503","authors":"Hoffman CS, Wood V, Fantes PA","authors_abbrev":"Hoffman CS et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2015-10-09","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-10-10 00:18:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12760046","title":"Controlling S-phase onset in fission yeast.","citation":"Cold Spring Harb Symp Quant Biol 2000;65:323-32","abstract":"","authors":"Lygerou Z, Nurse P","authors_abbrev":"Lygerou Z et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2003-05-23","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21057634","title":"Rga4, a Rho-GAP from fission yeast: Finding specificity within promiscuity.","citation":"Commun Integr Biol 2010 Sep;3(5):436-9","abstract":"Regulation by signaling molecules of pathways involved in determining cell size and shape is fundamental to understand morphogenesis. In eukaryotic cells, Rho GTPases modulate cellular events by acting as molecular switches. GTPase Activating Proteins (GAPs) control the fine-tuning of Rho GTPase activity as downregulators that promote their inactive state. We use Schizosaccharomyces pombe as a model to unveil key mechanisms underlying processes of general significance. Rga4, one of the nine RhoGAPs present in the fission yeast, is a key factor in the control of cell polarity and morphogenesis by negatively regulating the activity of the essential Rho GTPase Cdc42. We have demonstrated that Rga4 is also a GAP for Rho2 GTPase, which acts upstream of the Pmk1 cell integrity MAP kinase pathway and positively regulates cell integrity and cell separation. Our findings suggest that Rga4 control of both Cdc42 and Rho2 function is rather independent, thus providing a good example of regulatory specificity. Additionally, we describe multiple GAPs that can downregulate Pmk1 activity in a Rho2-dependent and independent fashion. These studies corroborate the existence of a sophisticated regulatory network by which different RhoGAPs modulate differentially the activity of Rho GTPases, and the existence of different inputs for the Pmk1 cell integrity MAP kinase pathway.","doi":"10.4161/cib.3.5.12284","authors":"Cansado J, Soto T, Gacto M, Pérez P","authors_abbrev":"Cansado J et al.","pubmed_publication_date":"Sep 2010","pubmed_entrez_date":"2010-11-09","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28E12.03","SPBC119.08"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7621821","title":"The calnexin homologue cnx1+ in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain.","citation":"EMBO J 1995 Jul 03;14(13):3064-72","abstract":"Secretory proteins become folded by the action of a number of molecular chaperones soon after they enter the endoplasmic reticulum (ER). In mammalian cells, the ER membrane protein calnexin has been shown to be a molecular chaperone involved in the folding of secretory proteins and in the assembly of cell surface receptor complexes. We have used a PCR strategy to identify the Schizosaccharomyces pombe calnexin homologue, cnx1+. The cnx1+ encoded protein, Cnx1, was shown to be a calcium binding type I integral membrane glycoprotein. At its 5' end, the cnx1+ gene has consensus heat shock transcriptional control elements and was inducible by heat shock and by the calcium ionophore A23187. Unlike the sequence-related Saccharomyces cerevisiae CNE1 gene, the S.pombe cnx1+ gene was essential for cell viability. The full-length Cnx1 protein was able to complement the cnx1+ gene disruption but the full-length mammalian calnexin could not. The ER lumenal domain of Cnx1, which was secreted from cells, was capable of complementing the cnx1::ura4 lethal phenotype. The equivalent region of mammalian calnexin has been shown to possess molecular chaperone activity. It is possible that the lethal phenotype is caused by the absence of this chaperone activity in the S.pombe cnx1+ gene disruption.","authors":"Parlati F, Dignard D, Bergeron JJ, Thomas DY","authors_abbrev":"Parlati F et al.","pubmed_publication_date":"03 Jul 1995","pubmed_entrez_date":"1995-07-03","publication_year":"1995","canto_session_key":"60b3b61056143fa0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-04 10:05:03","canto_approved_date":"2024-03-30 08:21:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 10:04:47","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:24560576","title":"Homeostatic actin cytoskeleton networks are regulated by assembly factor competition for monomers.","citation":"Curr Biol 2014 Mar 03;24(5):579-85","abstract":"Controlling the quantity and size of organelles through competition for a limited supply of components is quickly emerging as an important cellular regulatory mechanism. Cells assemble diverse actin filament (F-actin) networks for fundamental processes including division, motility, and polarization. F-actin polymerization is tightly regulated by activation of assembly factors such as the Arp2/3 complex and formins at specific times and places. We directly tested an additional hypothesis that diverse F-actin networks are in homeostasis, whereby competition for actin monomers (G-actin) is critical for regulating F-actin network size. Here we show that inhibition of Arp2/3 complex in the fission yeast Schizosaccharomyces pombe not only depletes Arp2/3-complex-mediated endocytic actin patches, but also induces a dramatic excess of formin-assembled F-actin. Conversely, disruption of formin increases the density of Arp2/3-complex-mediated patches. Furthermore, modification of actin levels significantly perturbs the fission yeast actin cytoskeleton. Increasing actin favors Arp2/3-complex-mediated actin assembly, whereas decreasing actin favors formin-mediated contractile rings. Therefore, the specific actin concentration in a cell is critical, and competition for G-actin helps regulate the proper amount of F-actin assembly for diverse processes.","doi":"10.1016/j.cub.2014.01.072","authors":"Burke TA, Christensen JR, Barone E, Suarez C, Sirotkin V, Kovar DR","authors_abbrev":"Burke TA et al.","pubmed_publication_date":"03 Mar 2014","pubmed_entrez_date":"2014-02-25","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11800554","title":"Role of the DNA repair nucleases Rad13, Rad2 and Uve1 of Schizosaccharomyces pombe in mismatch correction.","citation":"J Mol Biol 2001 Oct 19;313(2):241-53","abstract":"Repair of mismatched DNA occurs mainly by the long-patch mismatch repair (MMR) pathway, requiring Msh2 and Pms1. In Schizosaccharomyces pombe mismatches can be repaired by a short-patch repair system, containing nucleotide excision repair (NER) factors. We studied mismatch correction efficiency in cells with inactivated DNA repair nucleases Rad13, Rad2 or Uve1 in MMR proficient and deficient background. Rad13 incises 3' of damaged DNA during NER. Rad2 has a function in the Uve1-dependent repair of DNA damages and in replication. Loss of Rad13 caused a strong reduction of short-patch processing of mismatches formed during meiotic recombination. Mitotic mutation rates were increased, but not to the same extent as in the NER mutant swi10, which is defective in 5' incision. The difference might be caused by an additional role of Rad13 in base excision repair or due to partial redundancy with other 3' endonucleases. Meiotic mismatch repair was not or only slightly affected in rad2 and uve1 mutants. In addition, inactivation of uve1 caused only weak effects on mutation avoidance. Mutation rates were elevated when rad2 was mutated, but not further increased in swi10 rad2 and rad13 rad2 double mutants, indicating an epistatic relationship. However, the mutation spectra of rad2 were different from that of swi10 and rad13. Thus, the function of Rad2 in mutation avoidance is rather independent of NER. rad13, swi10 and rad2, but not uve1 mutants were sensitive to the DNA-damaging agent methyl methane sulphonate. Cell survival was further reduced in the double mutants swi10 rad2, rad13 rad2 and, surprisingly, swi10 rad13. These data confirm that NER and Rad2 act in distinct damage repair pathways and further indicate that the function of Rad13 in repair of alkylated bases is partially independent of NER.","authors":"Kunz C, Fleck O","authors_abbrev":"Kunz C et al.","pubmed_publication_date":"19 Oct 2001","pubmed_entrez_date":"2002-01-22","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.02c","SPBC19C7.09c","SPAC3G6.06c","SPBC4F6.15c","SPBC19G7.01c","SPBC3E7.08c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:39565189","title":"A systematic quantitative approach comprehensively defines domain-specific functional pathways linked to Schizosaccharomyces pombe heterochromatin regulation.","citation":"Nucleic Acids Res 2024 Nov 20;","abstract":"Heterochromatin plays a critical role in regulating gene expression and maintaining genome integrity. While structural and enzymatic components have been linked to heterochromatin establishment, a comprehensive view of the underlying pathways at diverse heterochromatin domains remains elusive. Here, we developed a systematic approach to identify factors involved in heterochromatin silencing at pericentromeres, subtelomeres and the silent mating type locus in Schizosaccharomyces pombe. Using quantitative measures, iterative genetic screening and domain-specific heterochromatin reporters, we identified 369 mutants with different degrees of reduced or enhanced silencing. As expected, mutations in the core heterochromatin machinery globally decreased silencing. However, most other mutants exhibited distinct qualitative and quantitative profiles that indicate heterochromatin domain-specific functions, as seen for example for metabolic pathways affecting primarily subtelomere silencing. Moreover, similar phenotypic profiles revealed shared functions for subunits within complexes. We further discovered that the uncharacterized protein Dhm2 plays a crucial role in heterochromatin maintenance, affecting the inheritance of H3K9 methylation and the clonal propagation of the repressed state. Additionally, Dhm2 loss resulted in delayed S-phase progression and replication stress. Collectively, our systematic approach unveiled a landscape of domain-specific heterochromatin regulators controlling distinct states and identified Dhm2 as a previously unknown factor linked to heterochromatin inheritance and replication fidelity.","doi":"10.1093/nar/gkae1024","authors":"Muhammad A, Sarkadi Z, Mazumder A, Ait Saada A, van Emden T, Capella M, Fekete G, Suma Sreechakram VN, Al-Sady B, Lambert SAE, Papp B, Barrales RR, Braun S","authors_abbrev":"Muhammad A et al.","pubmed_publication_date":"20 Nov 2024","pubmed_entrez_date":"2024-11-20","publication_year":"2024","canto_session_key":"d0f5602e777b7b69","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-11-22 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36831186","title":"Interplays of AMPK and TOR in Autophagy Regulation in Yeast.","citation":"Cells 2023 Feb 04;12(4)","abstract":"Cells survey their environment and need to balance growth and anabolism with stress programmes and catabolism towards maximum cellular bioenergetics economy and survival. Nutrient-responsive pathways, such as the mechanistic target of rapamycin (mTOR) interact and cross-talk, continuously, with stress-responsive hubs such as the AMP-activated protein kinase (AMPK) to regulate fundamental cellular processes such as transcription, protein translation, lipid and carbohydrate homeostasis. Especially in nutrient stresses or deprivations, cells tune their metabolism accordingly and, crucially, recycle materials through autophagy mechanisms. It has now become apparent that autophagy is pivotal in lifespan, health and cell survival as it is a gatekeeper of clearing damaged macromolecules and organelles and serving as quality assurance mechanism within cells. Autophagy is hard-wired with energy and nutrient levels as well as with damage-response, and yeasts have been instrumental in elucidating such connectivities. In this review, we briefly outline cross-talks and feedback loops that link growth and stress, mainly, in the fission yeast  Schizosaccharomyces pombe , a favourite model in cell and molecular biology.","doi":"10.3390/cells12040519","authors":"Alao JP, Legon L, Dabrowska A, Tricolici AM, Kumar J, Rallis C","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"04 Feb 2023","pubmed_entrez_date":"2023-02-25","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-02-26 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37163016","title":"Membrane binding of endocytic myosin-1s is inhibited by a class of ankyrin repeat proteins.","citation":"bioRxiv 2023 Apr 27;","abstract":"Fission yeast long-tailed myosin-1 binds Ank1. Ank1 ankyrin repeats associate with the Myo1 lever arm and Ank1 acidic tail binds the Myo1 TH1 domain to inhibit Myo1 membrane binding. Ank1 orthologs exists in budding yeast (Ank1) and humans (OSTF1).","doi":"10.1101/2023.04.26.538419","authors":"Willet AH, Chen JS, Ren L, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"27 Apr 2023","pubmed_entrez_date":"2023-05-10","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC105.02c","HGNC:8510"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29134248","title":"The ancient claudin Dni2 facilitates yeast cell fusion by compartmentalizing Dni1 into a membrane subdomain.","citation":"Cell Mol Life Sci 2018 May;75(9):1687-1706","abstract":"Dni1 and Dni2 facilitate cell fusion during mating. Here, we show that these proteins are interdependent for their localization in a plasma membrane subdomain, which we have termed the mating fusion domain. Dni1 compartmentation in the domain is required for cell fusion. The contribution of actin, sterol-dependent membrane organization, and Dni2 to this compartmentation was analysed, and the results showed that Dni2 plays the most relevant role in the process. In turn, the Dni2 exit from the endoplasmic reticulum depends on Dni1. These proteins share the presence of a cysteine motif in their first extracellular loop related to the claudin GLWxxC(8-10 aa)C signature motif. Structure-function analyses show that mutating each Dni1 conserved cysteine has mild effects, and that only simultaneous elimination of several cysteines leads to a mating defect. On the contrary, eliminating each single cysteine and the C-terminal tail in Dni2 abrogates Dni1 compartmentation and cell fusion. Sequence alignments show that claudin trans-membrane helixes bear small-XXX-small motifs at conserved positions. The fourth Dni2 trans-membrane helix tends to form homo-oligomers in Escherichia plasma membrane, and two concatenated small-XXX-small motifs are required for efficient oligomerization and for Dni2 export from the yeast endoplasmic reticulum. Together, our results strongly suggest that Dni2 is an ancient claudin that blocks Dni1 diffusion from the intercellular region where two plasma membranes are in close proximity, and that this function is required for Dni1 to facilitate cell fusion.","doi":"10.1007/s00018-017-2709-4","authors":"Curto MÁ, Moro S, Yanguas F, Gutiérrez-González C, Valdivieso MH","authors_abbrev":"Curto MÁ et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2017-11-15","publication_year":"2018","canto_session_key":"611cd009f8477dea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Henar Valdivieso","canto_first_approved_date":"2018-06-22 10:00:49","canto_approved_date":"2026-02-26 14:26:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-11 15:35:27","canto_added_date":"2017-11-16 01:15:13","annotation_curators":[{"name":"Henar Valdivieso","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1919.10c","SPAC688.11","SPAC20G4.02c","SPBC4.01","SPAC31G5.07"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-06-22"},{"uniquename":"EMBL:AJ632006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.40"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9366552","title":"A globular complex formation by Nda1 and the other five members of the MCM protein family in fission yeast.","citation":"Genes Cells 1997 Jul;2(7):467-79","abstract":"In the fission yeast Schizosaccharomyces pombe, Nda1, Nda4, Mis5 and Cdc21 proteins belong to the MCM (minichromosome maintenance) protein family which is thought to have six members. Each MCM member is required for the early stages of DNA replication, and has a well-conserved central 200-amino acid domain containing a putative ATP binding motif. However, the precise molecular functions of MCM proteins are not yet clear.\nWe investigated the physical interaction of Nda1 protein with the other fission yeast MCM proteins using specific antibodies. Immunoprecipitation of Nda1 protein leads to the co-precipitation of all the other members of the fission yeast MCM protein family. We purified the MCM protein complex by a combination of column chromatography. The native molecular weight of the MCM complex was estimated by gel filtration to be 560 kDa. The purified fraction contained nearly equal quantities of the six MCM proteins. Electron microscope observation showed that the MCM complex has a globular shape with a central cavity.\nWe have developed a procedure to purify fission yeast MCM proteins in a native hetero-oligomeric complex form for the first time, which opens an avenue to further biochemical analysis.","authors":"Adachi Y, Usukura J, Yanagida M","authors_abbrev":"Adachi Y et al.","pubmed_publication_date":"Jul 1997","pubmed_entrez_date":"1997-07-01","publication_year":"1997","canto_session_key":"d4342cabcb218e1b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2012-09-20 13:50:04","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-07-20 14:42:53","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPCC1682.02c","SPBC4.04c","SPCC16A11.17","SPBC211.04c","SPBC25D12.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2012-07-20"},{"uniquename":"PMID:11223945","title":"Subtelomeric sequence from the right arm of Schizosaccharomyces pombe chromosome I contains seven permease genes.","citation":"Yeast 2001 Mar 15;18(4):355-61","abstract":"The sequence has been determined of 80 888 bp of contiguous subtelomeric DNA, including the isp5 gene, from the right arm of chromosome I of Schizosaccharomyces pombe; 27 open reading frames (ORFs) longer than 100 codons are present, giving a density of one gene per 3.0 kb. Seven of the predicted proteins are members of the major facilitator superfamily (MFS) of transport proteins, including four amino acid permease homologues, bringing this family of amino acid permease sequences to 17 in Sz. pombe, and a phylogenetic analysis is presented. Also encoded is an allantoate permease homologue, a sulphate permease homologue and a probable urea active transporter. Predicted non-membrane proteins include a 1-aminocyclopropane-1-carboxylate deaminase (ACC deaminase), a class III aminotransferase, serine acetyltransferase, protein-L-isoaspartate O-methyltransferase, alpha-glucosidase, alpha-galactosidase, esterase/lipase, oxidoreductase of the short-chain dehydrogenase/reductase (SDR) family, aldehyde dehydrogenase, formamidase, amidase, flavohaemoprotein, a putative translation initiation inhibitor and a protein with similarity to a filamentous fungal conidiation-specific protein. The remaining six ORFs are likely to encode proteins, either because they have sequence similarity with hypothetical proteins or because they are known to be transcribed. Introns are scarce in the sequenced region: only three ORFs contain introns, with only one having multiple introns. The sequenced region also contains a single Tf1 transposon long terminal repeat (LTR). The sequence is derived from cosmid clones c869, c922 and c1039 and has been submitted to the EMBL database under entries SPAC869 (Accession No. AL132779), SPAC922 (AL133522) and SPAC1039 (AL133521).","authors":"Hunt C, Moore K, Xiang Z, Hurst SM, McDougall RC, Rajandream MA, Barrell BG, Gwilliam R, Wood V, Lyne MH, Aves SJ","authors_abbrev":"Hunt C et al.","pubmed_publication_date":"15 Mar 2001","pubmed_entrez_date":"2001-02-27","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28096973","title":"A fission yeast cell-based system for multidrug resistant HIV-1 proteases.","citation":"Cell Biosci 2017;7:5","abstract":"","doi":"10.1186/s13578-016-0131-5","authors":"Benko Z, Liang D, Li G, Elder RT, Sarkar A, Takayama J, Ghosh AK, Zhao RY","authors_abbrev":"Benko Z et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-01-19","publication_year":"2017","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2017-01-19 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10454605","title":"Repair of apurinic/apyrimidinic sites by UV damage endonuclease; a repair protein for UV and oxidative damage.","citation":"Nucleic Acids Res 1999 Aug 01;27(15):3096-103","abstract":"UV damage endonuclease (UVDE) initiates a novel form of excision repair by introducing a nick imme-diately 5\" to UV-induced cyclobutane pyrimidine dimers or 6-4 photoproducts. Here, we report that apurinic/apyrimidinic (AP) sites are also nicked by Neurospora crassa and Schizosaccharomyces pombe UVDE. UVDE introduces a nick immediately 5\" to the AP site leaving a 3\"-OH and a 5\"-phosphate AP. Apyrimidinic sites are more effectively nicked by UVDE than apurinic sites. UVDE also possesses 3\"-repair activities for AP sites nicked by AP lyase and for 3\"-phosphoglycolate produced by bleomycin. The Uvde gene introduced into Escherichia coli cells lacking two types of AP endonuclease, Exo III and Endo IV, gave the host cells resistance to methylmethane sulfonate and t-butyl hydroperoxide. We identified two AP endonuclease activities in S.pombe cell extracts. Besides cyclobutane pyrimidine dimers and 6-4 photoproducts, N. crassa UVDE also nicks Dewar photoproducts. Thus, UVDE is able to repair both of the major forms of DNA damage in living organisms: UV-induced DNA lesions and AP sites.","authors":"Kanno S, Iwai S, Takao M, Yasui A","authors_abbrev":"Kanno S et al.","pubmed_publication_date":"01 Aug 1999","pubmed_entrez_date":"1999-08-24","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11313465","title":"Threonine-11, phosphorylated by Rad3 and atm in vitro, is required for activation of fission yeast checkpoint kinase Cds1.","citation":"Mol Cell Biol 2001 May;21(10):3398-404","abstract":"Fission yeast Cds1 is phosphorylated and activated when DNA replication is interrupted by nucleotide starvation or DNA damage. Cds1 enforces the S-M checkpoint that couples mitosis (M) to the completion of DNA synthesis (S). Cds1 also controls replicational stress tolerance mechanisms. Cds1 is regulated by a group of proteins that includes Rad3, a kinase related to human checkpoint kinase ATM (ataxia telangiectasia mutated). ATM phosphorylates serine or threonine followed by glutamine (SQ or TQ). Here we show that in vitro, Rad3 and ATM phosphorylate the N-terminal domain of Cds1 at the motif T(11)Q(12). Substitution of threonine-11 with alanine (T11A) abolished Cds1 activation that occurs when DNA replication is inhibited by hydroxyurea (HU) treatment. The cds1-T11A mutant was profoundly sensitive to HU, although not quite as sensitive as a cds1(-) null mutant. Cds1(T11A) was unable to enforce the S-M checkpoint. These results strongly suggest that Rad3-dependent phosphorylation of Cds1 at threonine-11 is required for Cds1 activation and function.","authors":"Tanaka K, Boddy MN, Chen XB, McGowan CH, Russell P","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-04-21","publication_year":"2001","canto_session_key":"52d9059eb1a6c990","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2017-03-17 15:46:00","canto_approved_date":"2023-06-15 15:47:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-17 20:17:43","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPCC1259.13","SPCC18B5.03","SPCC18B5.11c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-03-17"},{"uniquename":"PMID:26729909","title":"Use of the BioGRID Database for Analysis of Yeast Protein and Genetic Interactions.","citation":"Cold Spring Harb Protoc 2016 Jan 04;2016(1):pdb.prot088880","abstract":"The BioGRID database is an extensive repository of curated genetic and protein interactions for the budding yeast Saccharomyces cerevisiae, the fission yeast Schizosaccharomyces pombe, and the yeast Candida albicans SC5314, as well as for several other model organisms and humans. This protocol describes how to use the BioGRID website to query genetic or protein interactions for any gene of interest, how to visualize the associated interactions using an embedded interactive network viewer, and how to download data files for either selected interactions or the entire BioGRID interaction data set.","doi":"10.1101/pdb.prot088880","authors":"Oughtred R, Chatr-aryamontri A, Breitkreutz BJ, Chang CS, Rust JM, Theesfeld CL, Heinicke S, Breitkreutz A, Chen D, Hirschman J, Kolas N, Livstone MS, Nixon J, O'Donnell L, Ramage L, Winter A, Reguly T, Sellam A, Stark C, Boucher L, Dolinski K, Tyers M","authors_abbrev":"Oughtred R et al.","pubmed_publication_date":"04 Jan 2016","pubmed_entrez_date":"2016-01-06","publication_year":"2016","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2016-01-07 01:19:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37158439","title":"The fission yeast cytokinetic ring component Fic1 promotes septum formation.","citation":"Biol Open 2023 May 15;12(5)","abstract":"In Schizosaccharomyces pombe, septum formation is coordinated with cytokinetic ring constriction but the mechanisms linking these events are unclear. In this study, we explored the role of the cytokinetic ring component Fic1, first identified by its interaction with the F-BAR protein Cdc15, in septum formation. We found that the fic1 phospho-ablating mutant, fic1-2A, is a gain-of-function allele that suppresses myo2-E1, the temperature-sensitive allele of the essential type-II myosin, myo2. This suppression is achieved by the promotion of septum formation and required Fic1's interaction with the F-BAR proteins Cdc15 and Imp2. Additionally, we found that Fic1 interacts with Cyk3 and that this interaction was likewise required for Fic1's role in septum formation. Fic1, Cdc15, Imp2, and Cyk3 are the orthologs of the Saccharomyces cerevisiae ingression progression complex, which stimulates the chitin synthase Chs2 to promote primary septum formation. However, our findings indicate that Fic1 promotes septum formation and cell abscission independently of the S. pombe Chs2 ortholog. Thus, while similar complexes exist in the two yeasts that each promote septation, they appear to have different downstream effectors.","doi":"10.1242/bio.059957","authors":"Rossi AM, Bohnert KA, Gould KL","authors_abbrev":"Rossi AM et al.","pubmed_publication_date":"15 May 2023","pubmed_entrez_date":"2023-05-09","publication_year":"2023","canto_session_key":"5e4169b314b92367","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Anthony Rossi","canto_first_approved_date":"2023-06-19 13:09:39","canto_approved_date":"2026-02-14 09:50:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-09 15:16:59","canto_added_date":"2023-05-10 00:15:04","annotation_curators":[{"name":"Anthony Rossi","community_curator":true,"annotation_count":55,"orcid":"0000-0003-3787-8573","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.05c","SPCC645.05c","SPBC83.18c","SPBC1709.01","SPAP8A3.08","SPAC9G1.06c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2023-06-19"},{"uniquename":"PMID:22276125","title":"Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast.","citation":"PLoS One 2012;7(1):e29683","abstract":"We have previously identified the RNA recognition motif (RRM)-type RNA-binding protein Nrd1 as an important regulator of the posttranscriptional expression of myosin in fission yeast. Pmk1 MAPK-dependent phosphorylation negatively regulates the RNA-binding activity of Nrd1. Here, we report the role of Nrd1 in stress-induced RNA granules. Nrd1 can localize to poly(A)-binding protein (Pabp)-positive RNA granules in response to various stress stimuli, including heat shock, arsenite treatment, and oxidative stress. Interestingly, compared with the unphosphorylatable Nrd1, Nrd1(DD) (phosphorylation-mimic version of Nrd1) translocates more quickly from the cytoplasm to the stress granules in response to various stimuli; this suggests that the phosphorylation of Nrd1 by MAPK enhances its localization to stress-induced cytoplasmic granules. Nrd1 binds to Cpc2 (fission yeast RACK) in a phosphorylation-dependent manner and deletion of Cpc2 affects the formation of Nrd1-positive granules upon arsenite treatment. Moreover, the depletion of Nrd1 leads to a delay in Pabp-positive RNA granule formation, and overexpression of Nrd1 results in an increased size and number of Pabp-positive granules. Interestingly, Nrd1 deletion induced resistance to sustained stresses and enhanced sensitivity to transient stresses. In conclusion, our results indicate that Nrd1 plays a role in stress-induced granule formation, which affects stress resistance in fission yeast.","doi":"10.1371/journal.pone.0029683","authors":"Satoh R, Tanaka A, Kita A, Morita T, Matsumura Y, Umeda N, Takada M, Hayashi S, Tani T, Shinmyozu K, Sugiura R","authors_abbrev":"Satoh R et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-01-26","publication_year":"2012","canto_session_key":"294ca361d2d1a19b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F7.11","SPAC6B12.15"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:41924654","title":"Identification and characterization of  Schizosaccharomyces pombe  splicing mutants.","citation":"MicroPubl Biol 2026;2026","abstract":"Pre-mRNA splicing is carried out by the spliceosome, a dynamic complex of five small nuclear ribonucleoprotein particles (snRNPs). Several genetic screens have been conducted in  Schizosaccharomyces pombe  to identify pre-mRNA splicing mutants and spliceosome components  .  However, some pre-mRNA splicing mutants have yet to be assigned to a gene and in certain cases, the mutations within genes have not been identified and phenotypes compared. Here, we have identified new mutations in the U4/U6.U5 tri-snRNP component  dim1  and assigned  prp6  and  prp7  mutants to  snu13  and  brl1  , respectively, revealing roles for these factors in pre-mRNA splicing.","doi":"10.17912/micropub.biology.002096","authors":"Nicholas LL, Suo F, Hanna SM, Du LL, Gould KL","authors_abbrev":"Nicholas LL et al.","pubmed_publication_date":"2026","pubmed_entrez_date":"2026-04-02","publication_year":"2026","canto_session_key":"a16f1c08069f559b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-02 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2328720","title":"The developmental fate of fission yeast cells is determined by the pattern of inheritance of parental and grandparental DNA strands.","citation":"EMBO J 1990 May;9(5):1407-15","abstract":"A key feature for development consists of producing sister cells that differ in their potential for cellular differentiation. Following two cell divisions, a haploid Schizosaccharomyces pombe cell produces one cell in four 'granddaughters' with a changed mating cell type, implying nonequivalence of sister cells in each of two consecutive cell divisions. The observed pattern of switching is analogous to the mammalian 'stem cell' lineage by which a cell produces one daughter like itself while the other daughter is advanced in its developmental program. It is tested here whether sisters differ because of unequal distribution of cytoplasmic and/or nuclear components to them or due to inheriting a specific parental DNA chain at the mating type locus. Only the DNA strand-segregation model predicts that those cells engineered to contain an inverted tandem duplication of the mating type locus should produce equivalent sisters. Consequently, two 'cousins' in four related granddaughter cells should switch. The results verified the prediction, thus establishing that all cells otherwise fully possess the potential to switch. Therefore, the program of cell type change in S.pombe cell lineages is determined by the pattern of DNA strand inheritance at the mating type locus. A specific DNA sequence present at the mating type locus is postulated to be the cause of developmental asymmetry between sister cells. A general model for cellular differentiation is proposed in which the act of DNA replication itself is hypothesized to produce developmentally nonequivalent sister genomes.","authors":"Klar AJ","authors_abbrev":"Klar AJ","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37521138","title":"Prolongation of mitosis is associated with enhanced endogenous DNA damage in fission yeast.","citation":"MicroPubl Biol 2023;2023","abstract":"Mitosis is usually shorter than other phases of the cell cycle and maintains a consistent duration despite variations in cell size and spindle size. This suggests the existence of a compensatory mechanism that ensures a short duration, possibly as a protective measure against irreversible damage, such as DNA damage. To explore the link between prolonged mitosis and DNA damage, we develop a microscopy-based assay utilizing Rad52-GFP as a marker for mitotic DNA damage. Through this assay, we provide evidence that mutants with prolonged mitosis exhibit increased Rad52 puncta, indicating an elevation in endogenous DNA damage.","doi":"10.17912/micropub.biology.000911","authors":"Jain I, Tran PT","authors_abbrev":"Jain I et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-07-31","publication_year":"2023","canto_session_key":"05b46f2bdda626fc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-08-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2082935","title":"Yeast as a model system for understanding the control of DNA replication in Eukaryotes.","citation":"Bioessays 1990 Oct;12(10):457-63","abstract":"In the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, the initiation of DNA replication is controlled at a point called START. At this point, the cellular environment is assessed; only if conditions are appropriate do cells traverse START, thus becoming committed to initiate DNA replication and complete the remainder of the cell cycle. The cdc2+/CDC28+ gene, encoding the protein kinase p34, is a key element in this complex control. The identification of structural and functional homologues of p34 suggests that it has a role in the control of DNA replication in all eukaryotes. The WHI1+, CLN1+ and CLN2+ gene products, identified in S. cerevisiae, are positive regulators that function at START and may interact with p34. Determining how passing the START control point leads to the initiation of DNA replication is a major outstanding challenge in cell cycle studies.","authors":"Bartlett R, Nurse P","authors_abbrev":"Bartlett R et al.","pubmed_publication_date":"Oct 1990","pubmed_entrez_date":"1990-10-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31566560","title":"TORC2-Gad8-dependent myosin phosphorylation modulates regulation by calcium.","citation":"Elife 2019 Sep 30;8","abstract":"Cells respond to changes in their environment through signaling networks that modulate cytoskeleton and membrane organization to coordinate cell-cycle progression, polarized cell growth and multicellular development. Here, we define a novel regulatory mechanism by which the motor activity and function of the fission yeast type one myosin, Myo1, is modulated by TORC2-signalling-dependent phosphorylation. Phosphorylation of the conserved serine at position 742 (S742) within the neck region changes both the conformation of the neck region and the interactions between Myo1 and its associating calmodulin light chains. S742 phosphorylation thereby couples the calcium and TOR signaling networks that are involved in the modulation of myosin-1 dynamics to co-ordinate actin polymerization and membrane reorganization at sites of endocytosis and polarised cell growth in response to environmental and cell-cycle cues.","doi":"10.7554/eLife.51150","authors":"Baker K, Gyamfi IA, Mashanov GI, Molloy JE, Geeves MA, Mulvihill DP","authors_abbrev":"Baker K et al.","pubmed_publication_date":"30 Sep 2019","pubmed_entrez_date":"2019-10-01","publication_year":"2019","canto_session_key":"be141355a289357a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-10-02 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37758508","title":"Revised fission yeast gene and allele nomenclature guidelines for machine readability.","citation":"Genetics 2023 Nov 01;225(3)","abstract":"Standardized nomenclature for genes, gene products, and isoforms is crucial to prevent ambiguity and enable clear communication of scientific data, facilitating efficient biocuration and data sharing. Standardized genotype nomenclature, which describes alleles present in a specific strain that differ from those in the wild-type reference strain, is equally essential to maximize research impact and ensure that results linking genotypes to phenotypes are Findable, Accessible, Interoperable, and Reusable (FAIR). In this publication, we extend the fission yeast clade gene nomenclature guidelines to support the curation efforts at PomBase (www.pombase.org), the Schizosaccharomyces pombe Model Organism Database. This update introduces nomenclature guidelines for noncoding RNA genes, following those set forth by the Human Genome Organisation Gene Nomenclature Committee. Additionally, we provide a significant update to the allele and genotype nomenclature guidelines originally published in 1987, to standardize the diverse range of genetic modifications enabled by the fission yeast genetic toolbox. These updated guidelines reflect a community consensus between numerous fission yeast researchers. Adoption of these rules will improve consistency in gene and genotype nomenclature, and facilitate machine-readability and automated entity recognition of fission yeast genes and alleles in publications or datasets. In conclusion, our updated guidelines provide a valuable resource for the fission yeast research community, promoting consistency, clarity, and FAIRness in genetic data sharing and interpretation.","doi":"10.1093/genetics/iyad143","authors":"Lera-Ramírez M, Bähler J, Mata J, Rutherford K, Hoffman CS, Lambert S, Oliferenko S, Martin SG, Gould KL, Du LL, Sabatinos SA, Forsburg SL, Nielsen O, Nurse P, Wood V","authors_abbrev":"Lera-Ramírez M et al.","pubmed_publication_date":"01 Nov 2023","pubmed_entrez_date":"2023-09-27","publication_year":"2023","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2023-09-28 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24870957","title":"Identification of the binding site of the quinone-head group in mitochondrial Coq10 by photoaffinity labeling.","citation":"Biochemistry 2014 Jun 24;53(24):3995-4003","abstract":"Mitochondrial Coq10 is a ubiquinone (UQ)-binding protein that is a member of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain superfamily. Deletion of the COQ10 gene was previously shown to cause a marked respiratory defect in Saccharomyces cerevisiae and Schizosaccharomyces pombe, which indicated that Coq10 may support efficient electron transfer between the respiratory complexes; however, its physiological role remains elusive. To elucidate the role of Coq10, we attempted to identify the binding site of UQ in recombinant S. pombe Coq10 expressed in an Escherichia coli cell membrane through photoaffinity labeling with the photoreactive UQ probe, UQ-1, in combination with biotinylation of the labeled peptide by means of the so-called click chemistry. Comprehensive proteomic analyses revealed that the quinone-head ring of UQ-1 specifically binds to the N-terminal region of Phe39–Lys45 of Coq10, which corresponds to the ligand-binding pocket of many proteins containing the START domain. The labeling was completely suppressed in the presence of an excess amount of artificial short-chain UQ analogues, such as UQ2. In the Phe39Ala and Pro41Ala mutants, the extents of labeling were ∼40 and ∼60%, respectively, of that of wild-type Coq10. While Coq10 has been thought to bind UQ, our work first provides the direct evidence of Coq10 accommodating the quinone-head ring of UQ in its START domain. On the basis of these results, the physiological role of Coq10 has been discussed.","authors":"Murai M, Matsunobu K, Kudo S, Ifuku K, Kawamukai M, Miyoshi H","authors_abbrev":"Murai M et al.","pubmed_publication_date":"24 Jun 2014","pubmed_entrez_date":"2014-05-30","publication_year":"2014","canto_session_key":"04595e357310e2d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-22 15:28:41","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-22 15:28:34","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-22"},{"uniquename":"PMID:27325741","title":"Ctp1-dependent clipping and resection of DNA double-strand breaks by Mre11 endonuclease complex are not genetically separable.","citation":"Nucleic Acids Res 2016 Sep 30;44(17):8241-9","abstract":"Homologous recombination (HR) repair of programmed meiotic double-strand breaks (DSBs) requires endonucleolytic clipping of Rec12(Spo11)-oligonucleotides from 5' DNA ends followed by resection to generate invasive 3' single-stranded DNA tails. The Mre11-Rad50-Nbs1 (MRN) endonuclease and Ctp1 (CtIP and Sae2 ortholog) are required for both activities in fission yeast but whether they are genetically separable is controversial. Here, we investigate the mitotic DSB repair properties of Ctp1 C-terminal domain (ctp1-CD) mutants that were reported to be specifically clipping deficient. These mutants are sensitive to many clastogens, including those that create DSBs devoid of covalently bound proteins. These sensitivities are suppressed by genetically eliminating Ku nonhomologous end-joining (NHEJ) protein, indicating that Ctp1-dependent clipping by MRN is required for Ku removal from DNA ends. However, this rescue requires Exo1 resection activity, implying that Ctp1-dependent resection by MRN is defective in ctp1-CD mutants. The ctp1-CD mutants tolerate one but not multiple broken replication forks, and they are highly reliant on the Chk1-mediated cell cycle checkpoint arrest, indicating that HR repair is inefficient. We conclude that the C-terminal domain of Ctp1 is required for both efficient clipping and resection of DSBs by MRN and these activities are mechanistically similar.","doi":"10.1093/nar/gkw557","authors":"Jensen KL, Russell P","authors_abbrev":"Jensen KL et al.","pubmed_publication_date":"30 Sep 2016","pubmed_entrez_date":"2016-06-22","publication_year":"2016","canto_session_key":"61c5a0ac6ec56979","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_approved_date":"2016-07-21 16:15:49","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-08 22:10:40","canto_added_date":"2016-06-23 00:15:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":61,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.06c","SPAC20G8.01","SPCC1259.13","SPBC543.03c","SPCC338.08","SPBC29A10.05"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-07-08"},{"uniquename":"PMID:37664590","title":"Meiotic recombination is confirmed to be unusually high in the fission yeast  Schizosaccharomyces pombe .","citation":"iScience 2023 Sep 15;26(9):107614","abstract":"In most eukaryotes, meiotic crossovers (COs) are limited to 1-3 per chromosome, and are prevented from occurring close to one another by CO interference. The fission yeast  Schizosaccharomyces pombe , an exception to these general rules, was reported to have the highest CO number per chromosome and no or weak interference. However, global CO frequency was indirectly estimated, calling for confirmation. Here, we used an innovative strategy to determine COs genome-wide in  S. pombe . We confirmed weak CO interference, acting at physical distances compatible with the patterning of recombination precursors. We revealed a slight co-variation in CO number between chromosomes, suggesting that a limiting pro-CO factor varies between meiocytes. CO number per chromosome varies proportionally with chromosome size, with the three chromosomes having, on average, 15.9, 12.5, and 7.0 COs, respectively. This reinforces  S. pombe 's status as the eukaryote with the highest CO number per chromosome described to date.","doi":"10.1016/j.isci.2023.107614","authors":"Lian Q, Maestroni L, Gaudin M, Llorente B, Mercier R","authors_abbrev":"Lian Q et al.","pubmed_publication_date":"15 Sep 2023","pubmed_entrez_date":"2023-09-04","publication_year":"2023","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2023-09-05 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7985419","title":"Cloning and sequencing of Schizosaccharomyces pombe car1 gene encoding arginase. Expression of the arginine anabolic and catabolic genes in response to arginine and related metabolites.","citation":"Yeast 1994 Jul;10(7):923-33","abstract":"We report here the cloning and sequencing of the gene encoding arginase (car1) from Schizosaccharomyces pombe. Since no arginase-less strain exists in this organism, we cloned the gene by functional complementation of a car1 mutant strain from Saccharomyces cerevisiae. The S. pombe car1 gene encodes a 323 amino acids polypeptide sharing identity with arginases from different organisms. Measurements of arg3, arg11 and car1 mRNA under different growth conditions confirm the very weak repression by arginine of the two anabolic genes and show that the induction of arginase synthesis operates at a transcriptional level. The promoter of S. pombe car1 gene does not contain the 'arginine boxes' defined as the target of the ARGR-MCM1 proteins in the promoters of the arginine co-regulated genes in S. cerevisiae. The heterologous expression of S. pombe car1 gene in S. cerevisiae is independent of the ARGRII gene product (ArgRIIp/Arg81p). Determination of arginine, ornithine and citrulline intracellular concentrations shows the efficiency of the different controls operating in S. cerevisiae, and also indicates that in S. pombe enzyme compartmentation is not always sufficient to control the arginine metabolic flux.","authors":"Van Huffel C, Dubois E, Messenguy F","authors_abbrev":"Van Huffel C et al.","pubmed_publication_date":"Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_session_key":"1c3046e2adef8eb0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-10-28 15:20:11","canto_approved_date":"2025-03-11 19:57:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-28 15:20:02","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP26C9.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-28"},{"uniquename":"PANTHER:PTHR31492","canto_curator_role":"PomBase","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAP11E10.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10620772","title":"Identification and transcription control of fission yeast genes repressed by an ammonium starvation growth arrest.","citation":"Yeast 2000 Jan 15;16(1):23-33","abstract":"In fission yeast Schizosaccharomyces pombe, ammonium starvation induces a growth arrest, a cell cycle exit in G(1) and a further switch to meiosis. This process is regulated by the cAMP-dependent protein kinase and the Wis1-dependent MAP kinase cascade, and downstream transcription factors. In order to understand how cells adapt their genetic programme to the switch from mitotic cycling to starvation, a differential transcript analysis comparing mRNA from exponentially growing and ammonium-starved cells was performed. Genes repressed by this stimulus mainly concern cell growth, i.e. protein synthesis and global metabolism. Comparison of the expression of two of them, the ribosomal proteins Rps6 and TCTP, in many different growing conditions, evidenced a strong correlation, suggesting that their transcriptions are coordinately regulated. Nevertheless, by repeating the ammonium starvation on strains constitutively activated for the PKA pathway (Deltacgs1), or unable to activate the Wis1-dependent MAP kinase pathway (Deltawis1), or with both characteristics (Deltacgs1+Deltawis1), the transcriptional inhibition was found to be governed either by the PKA pathway, or by the Wis1 pathway, or by both. These results suggest that during the switch from exponential growth to ammonium starvation, cell homeostasis is maintained by downregulating the transcription of the most expressed genes by a PKA and a Wis1-dependent process. Accession Nos for the S30 and L14 ribosomal protein cDNA sequences are AJ2731 and AJ2732, respectively.","authors":"Bonnet C, Perret E, Dumont X, Picard A, Caput D, Lenaers G","authors_abbrev":"Bonnet C et al.","pubmed_publication_date":"15 Jan 2000","pubmed_entrez_date":"2000-01-06","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8889801","title":"RCC1 in the Ran pathway.","citation":"J Biochem 1996 Aug;120(2):207-14","abstract":"RCC1 is a chromosomal protein that functions as a GEF of the nuclear G protein Ran, which GTPase activity is enhanced by RNA1 located in the cytoplasm. RCC1 has no preference for GTP or GDP-bound Ran, so that GTP-Ran formation in vivo is regulated by relative concentrations of GTP/GDP and regulatory proteins interacting with RCC1, Ran, and RNA1. Proteins possessing the special Ran-binding motif have been found to be conserved in species ranging from yeasts to mammalians. The finding of RanBP2/NUP358 clearly indicates the involvement of the Ran pathway in the nuclear pore transport function, in agreement with the finding that both rcc1- and rna1- show defects in this process. However, loss of RCC1 induces premature initiation of mitosis, resulting in G1 arrest with the micronuclei possessing mitotic condensed chromosomes. How both the cell cycle and nucleocytoplasmic transport are regulated by the RCC1-Ran pathway is a major question.","authors":"Seki T, Hayashi N, Nishimoto T","authors_abbrev":"Seki T et al.","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40875251","title":"Biostimulants in plant brassinosteroid hormone receptor BRI1 activation-a new system to evaluate activation capacity.","citation":"FEBS J 2025 Aug 28;","abstract":"The search for innovative and alternative chemical methods to manage plant growth is an ever-increasing reality. Biostimulants, products of biological origin, have shown promise in improving various agronomic characteristics and boosting yield. However, the selection and characterization of biostimulant matrices is a complex process that requires rigorous evaluation adapted to the specific needs of each plant. Because mixtures of biologically active compounds are present in biostimulants, efficient methods are required to characterize their potential mode of action. In this study, a new approach was developed to assess the biological activity of biostimulants by activating specific plant receptors involved in key physiological processes. It is based on the heterologous expression in fission yeast of brassinosteroid receptor protein Brassinosteroid Insensitive 1 (BRI1), which is involved in plant growth and development, and its specific activation by brassinolide (BL). The method involves the identification of highly expressed genes in response to BL activation of the BRI1 receptor, to generate a GFP reporter gene system that is switched on when biostimulants activate the BRI1 receptor. The biostimulants selected for testing were hydrolysates of animal origin. The results not only revealed variations in BRI1 activation among biostimulants, but also highlighted that samples from the same origin exhibit different BRI1 activation capacities depending on their processing methods. This new method enables direct classification of the mode of action of biostimulants by assessing their ability to activate specific plant receptors, providing a valuable resource for biostimulant research and development.","doi":"10.1111/febs.70235","authors":"Marquina M, Ricart-Fort M, Díaz-Parra R, López-Avilés S, Yance T, Quirós P, Contreras E, Salaet I, Atares S, Aligué R","authors_abbrev":"Marquina M et al.","pubmed_publication_date":"28 Aug 2025","pubmed_entrez_date":"2025-08-28","publication_year":"2025","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2025-08-28 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3327609","title":"Immunological homologies between ribosomal proteins amongst lower eukaryotes.","citation":"Curr Genet 1986;10(7):537-44","abstract":"Polyclonal antibodies were raised against the purified ribosomal proteins L1 and L2, the 5S rRNA binding protein L3, all from Saccharomyces cerevisiae, and against L1 and L2 from Schizosaccharomyces pombe (numbering according to Otaka and Osawa 1981; Otaka et al. 1983, respectively). For clarity prefixes Sc and Sp have been added to the numbering of proteins derived from S. cerevisiae and S. pombe, respectively. Ribosomal proteins from these yeasts and from Kluyveromyces marxianus, Rhodotorula glutinis, the slime mold Dictyostelium discoideum and the protozoan Tetrahymena thermophila were checked for antigenic cross-reactivity by the immunoblot technique. Anti-ScL1 bound to the largest ribosomal proteins of all organisms but not with equal strength. A fast migrating protein band from R. glutinis was also reactive. Anti-ScL2 reacted strongly with L2 or analogous proteins derived exclusively from the yeasts. Anti-ScL3 cross-reacted only with one protein band from K. marxianus, whereas anti-SpL1 cross-reacted with L1 or its analogues from the other organisms, but also with proteins of lower molecular weight. In S. cerevisiae, these proteins are located exclusively on the small ribosomal subunit. L2 or analogous ribosomal proteins of all organisms were recognized by anti-SpL2 but additionally the ribosomal protein YL28 of S. cerevisiae and fast migrating proteins of T. thermophila exhibited anti-SpL2 binding.","authors":"Kreutzfeldt C, Neumann T, Dierig A","authors_abbrev":"Kreutzfeldt C et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011026","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.122"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15957215","title":"Mitotic spindle pulls but fails to separate chromosomes in type II DNA topoisomerase mutants: uncoordinated mitosis.","citation":"EMBO J 1986 May;5(5):1003-10","abstract":"The fission yeast top2 locus is defined by five temperature-sensitive mutations that cause heat-labile activity of type II DNA topoisomerase in the cell extracts. We show that the top2 locus is a structural gene for type II topoisomerase by cloning a genomic DNA fragment that complements top2. The top2 mutants at restrictive temperature produce abnormal chromosomes at the time of mitosis; these are transiently extended into filamentous structures along with the elongating mitotic spindle but are not separated. A primary defect in top2 appears to be the formation of aberrant mitotic chromosomes inseparable by the force generated by the spindle apparatus. Consistently, the top2 cells that become lethal during mitosis contain a catenated dimer of an ARS plasmid. DNA and RNA continue to be synthesized if cytokinesis is blocked. Uncoordinated mitosis, that is the occurrence of spindle dynamics without chromosome separation, is revealed in top2, and is discussed in relation to mitotic regulation. Different phenotypes between top2 and top1-top2 described in the present paper can be explained by a previously proposed hypothesis that type II topoisomerase has dual in vivo functions: one that decatenates and unknots duplex DNAs is essential in mitosis, whereas the other which relaxes supercoils is required throughout the cell cycle if type I topoisomerase is absent.","authors":"Uemura T, Tanagida M","authors_abbrev":"Uemura T et al.","pubmed_publication_date":"May 1986","pubmed_entrez_date":"1986-05-01","publication_year":"1986","canto_session_key":"08c090c708be03da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-05-31 18:15:31","canto_approved_date":"2026-01-29 16:42:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-22 09:00:34","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.03c","SPBC1703.14c","SPCC1739.11c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-05-31"},{"uniquename":"PMID:22446625","title":"Telomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes.","citation":"Nature 2012 Mar 25;484(7393):260-4","abstract":"In most eukaryotes, the progressive loss of chromosome-terminal DNA sequences is counteracted by the enzyme telomerase, a reverse transcriptase that uses part of an RNA subunit as template to synthesize telomeric repeats. Many cancer cells express high telomerase activity, and mutations in telomerase subunits are associated with degenerative syndromes including dyskeratosis congenita and aplastic anaemia. The therapeutic value of altering telomerase activity thus provides ample impetus to study the biogenesis and regulation of this enzyme in human cells and model systems. We have previously identified a precursor of the fission yeast telomerase RNA subunit (TER1) and demonstrated that the mature 3'-end is generated by the spliceosome in a single cleavage reaction akin to the first step of splicing. Directly upstream and partly overlapping with the spliceosomal cleavage site is a putative binding site for Sm proteins. Sm and like-Sm (LSm) proteins belong to an ancient family of RNA-binding proteins represented in all three domains of life. Members of this family form ring complexes on specific sets of target RNAs and have critical roles in their biogenesis, function and turnover. Here we demonstrate that the canonical Sm ring and the Lsm2-8 complex sequentially associate with fission yeast TER1. The Sm ring binds to the TER1 precursor, stimulates spliceosomal cleavage and promotes the hypermethylation of the 5'-cap by Tgs1. Sm proteins are then replaced by the Lsm2-8 complex, which promotes the association with the catalytic subunit and protects the mature 3'-end of TER1 from exonucleolytic degradation. Our findings define the sequence of events that occur during telomerase biogenesis and characterize roles for Sm and Lsm complexes as well as for the methylase Tgs1.","doi":"10.1038/nature10924","authors":"Tang W, Kannan R, Blanchette M, Baumann P","authors_abbrev":"Tang W et al.","pubmed_publication_date":"25 Mar 2012","pubmed_entrez_date":"2012-03-27","publication_year":"2012","canto_session_key":"dbd591582523acd1","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11G11.06c","SPAC2F3.17c","SPBC29A3.14c","SPCC285.12","SPBC20F10.09","SPCC1840.10","SPNCRNA.214","SPBC9B6.05c","SPAC2C4.03c","SPBC3E7.14","SPCC1620.01c","SPAC26A3.08","SPBC30D10.06"],"gene_count":13,"ltp_gene_count":13},{"uniquename":"PMID:34928384","title":"Mutation and selection explain why many eukaryotic centromeric DNA sequences are often A + T rich.","citation":"Nucleic Acids Res 2022 Jan 11;50(1):579-596","abstract":"We have used chromosome engineering to replace native centromeric DNA with different test sequences at native centromeres in two different strains of the fission yeast Schizosaccharomyces pombe and have discovered that A + T rich DNA, whether synthetic or of bacterial origin, will function as a centromere in this species. Using genome size as a surrogate for the inverse of effective population size (Ne) we also show that the relative A + T content of centromeric DNA scales with Ne across 43 animal, fungal and yeast (Opisthokonta) species. This suggests that in most of these species the A + T content of the centromeric DNA is determined by a balance between selection and mutation. Combining the experimental results and the evolutionary analyses allows us to conclude that A + T rich DNA of almost any sequence will function as a centromere in most Opisthokonta species. The fact that many G/C to A/T substitutions are unlikely to be selected against may contribute to the rapid evolution of centromeric DNA. We also show that a neo-centromere sequence is not simply a weak version of native centromeric DNA and suggest that neo-centromeres require factors either for their propagation or establishment in addition to those required by native centromeres.","doi":"10.1093/nar/gkab1219","authors":"Barbosa AC, Xu Z, Karari K, Williams W, Hauf S, Brown WRA","authors_abbrev":"Barbosa AC et al.","pubmed_publication_date":"11 Jan 2022","pubmed_entrez_date":"2021-12-20","publication_year":"2022","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2021-12-22 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30110338","title":"The binding of Chp2's chromodomain to methylated H3K9 is essential for Chp2's role in heterochromatin assembly in fission yeast.","citation":"PLoS One 2018;13(8):e0201101","abstract":"The binding of heterochromatin protein 1 (HP1) to lysine 9-methylated histone H3 (H3K9me) is an essential step in heterochromatin assembly. Chp2, an HP1-family protein in the fission yeast Schizosaccharomyces pombe, is required for heterochromatic silencing. Chp2 recruits SHREC, a multifunctional protein complex containing the nucleosome remodeler Mit1 and the histone deacetylase Clr3. Although the targeting of SHREC to chromatin is thought to occur via two distinct modules regulated by the SHREC components Chp2 and Clr2, it is not clear how Chp2's chromatin binding regulates SHREC function. Here, we show that H3K9me binding by Chp2's chromodomain (CD) is essential for Chp2's silencing function and for SHREC's targeting to chromatin. Cells expressing a Chp2 mutant with defective H3K9me binding (Chp2-W199A) have a silencing defect, with a phenotype similar to that of chp2-null cells. Genetic analysis using a synthetic silencing system revealed that a Chp2 mutant and SHREC-component mutants had similar phenotypes, suggesting that Chp2's function also affects SHREC's chromatin binding. Size-exclusion chromatography of native protein complexes showed that Chp2-CD's binding of H3K9me3 ensures Clr3's chromatin binding, and suggested that SHREC's chromatin binding is mediated by separable functional modules. Interestingly, we found that the stability of the Chp2 protein depended on the Clr3 protein's histone deacetylase activity. Our findings demonstrate that Chp2's H3K9me binding is critical for SHREC function and that the two modules within the SHREC complex are interdependent.","doi":"10.1371/journal.pone.0201101","authors":"Maksimov V, Oya E, Tanaka M, Kawaguchi T, Hachisuka A, Ekwall K, Bjerling P, Nakayama JI","authors_abbrev":"Maksimov V et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-08-16","publication_year":"2018","canto_session_key":"f0f3b1ee8e5bd5bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-ichi Nakayama","canto_first_approved_date":"2018-09-04 15:20:41","canto_approved_date":"2025-04-24 15:36:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-22 08:17:10","canto_added_date":"2018-08-17 00:15:04","annotation_curators":[{"name":"Jun-ichi Nakayama","community_curator":true,"annotation_count":2,"orcid":"0000-0002-5597-8239","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPBC1105.11c","SPBP35G2.10","SPBC2D10.17","SPBC16C6.10","SPAC1834.04","SPBC8D2.04","SPAC1B3.17"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2018-09-04"},{"uniquename":"PMID:21504829","title":"Yeast SREBP cleavage activation requires the Golgi Dsc E3 ligase complex.","citation":"Mol Cell 2011 Apr 22;42(2):160-71","abstract":"Mammalian lipid homeostasis requires proteolytic activation of membrane-bound sterol regulatory element binding protein (SREBP) transcription factors through sequential action of the Golgi Site-1 and Site-2 proteases. Here we report that while SREBP function is conserved in fungi, fission yeast employs a different mechanism for SREBP cleavage. Using genetics and biochemistry, we identified four genes defective for SREBP cleavage, dsc1-4, encoding components of a transmembrane Golgi E3 ligase complex with structural homology to the Hrd1 E3 ligase complex involved in endoplasmic reticulum-associated degradation. The Dsc complex binds SREBP and cleavage requires components of the ubiquitin-proteasome pathway: the E2-conjugating enzyme Ubc4, the Dsc1 RING E3 ligase, and the proteasome. dsc mutants display conserved aggravating genetic interactions with components of the multivesicular body pathway in fission yeast and budding yeast, which lacks SREBP. Together, these data suggest that the Golgi Dsc E3 ligase complex functions in a post-ER pathway for protein degradation.","doi":"10.1016/j.molcel.2011.02.035","authors":"Stewart EV, Nwosu CC, Tong Z, Roguev A, Cummins TD, Kim DU, Hayles J, Park HO, Hoe KL, Powell DW, Krogan NJ, Espenshade PJ","authors_abbrev":"Stewart EV et al.","pubmed_publication_date":"22 Apr 2011","pubmed_entrez_date":"2011-04-21","publication_year":"2011","canto_session_key":"ff6fc192a2bc990a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2017-03-13 16:43:32","canto_approved_date":"2022-08-30 07:02:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-23 18:26:03","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Peter Espenshade","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC364.02c","SPBC354.03","SPAC1782.11","SPCC1223.12c","SPCC16C4.13c","SPCP20C8.03","SPAC1F8.06","SPAC31A2.14","SPBC17A3.10","SPAC1142.06","SPCC548.05c","SPAC23H3.13c","SPAC11G7.01","SPAC25B8.05","SPBC16A3.02c","SPACUNK12.02c","SPAC5D6.04","SPAC3H8.05c","SPBC12D12.06","SPAC13G7.11","SPAC26A3.07c","SPBC18H10.07","SPAC57A10.06","SPAC31A2.11c","SPAC1952.02","SPBC216.01c","SPBC6B1.03c","SPAC6G9.14","SPAC19A8.04","SPCC1393.13","SPAC922.05c","SPBC30B4.03c","SPAC24C9.15c","SPAP7G5.05","SPBC4F6.10","SPCC594.07c","SPBC409.11","SPBC8D2.17","SPAC513.03","SPCC1739.07","SPAC144.06","SPBC18H10.18c","SPCC74.06","SPCC1620.11","SPCC320.03","SPAC1805.07c","SPAC1782.08c","SPAP32A8.03c","SPCC895.05","SPAC1A6.03c","SPAC12B10.04","SPBC1778.10c","SPBC9B6.03","SPBC685.04c","SPAC57A7.07c","SPCC126.04c","SPAC23A1.09","SPBC13A2.04c","SPAC1D4.06c","SPBC691.03c","SPCP1E11.03","SPAC29B12.08","SPBC21C3.01c","SPCC613.12c","SPAC17A5.08","SPBC11G11.01","SPBPJ4664.03","SPBC119.08","SPAC3C7.10","SPAC227.01c","SPCC777.13","SPAC869.04","SPBPB7E8.01","SPCC285.05","SPBC1921.05","SPCC594.04c","SPCC31H12.04c","SPAC139.01c","SPAC3A11.10c","SPAC12B10.10","SPCC1235.01","SPAC343.12","SPAC1039.04","SPCC757.10","SPBC119.02","SPBC1709.13c","SPBC577.12","SPCC24B10.13","SPAC22F8.11","SPBC16A3.16","SPAC1527.02","SPCC1739.10","SPBP4G3.03","SPAC17G6.17","SPBC3B8.07c","SPAC30.01c","SPAC1610.01","SPCC1450.08c","SPBC16G5.01","SPAC23C4.03","SPBC1539.08","SPAC3H8.09c","SPCC1020.10","SPAP8A3.07c","SPBC582.10c","SPAC3A12.06c","SPBC21C3.14c","SPBC800.07c","SPCPB1C11.01","SPAC823.09c","SPAC20H4.04","SPAC750.01","SPAPJ691.02","SPBC23G7.15c","SPCP20C8.01c","SPBC3E7.05c","SPBC1289.06c","SPAC1782.07","SPAC22E12.14c","SPBC725.07","SPAC637.09","SPAPB8E5.10","SPAC26F1.10c","SPAC15A10.06","SPBC32H8.02c","SPAC644.11c","SPBC800.05c","SPBC2D10.05","SPAC694.04c","SPAC11E3.08c","SPAC3G6.05","SPAC1805.10","SPBC29A3.04","SPCC4B3.08","SPBC19C2.09","SPCC663.15c","SPAC1556.08c","SPAC3G6.01","SPAC1705.02","SPAC19G12.16c","SPAC1B3.03c","SPBC4.01","SPBC16G5.11c","SPAC30D11.07","SPAC20H4.02","SPCC794.11c","SPCC794.01c","SPAC2C4.07c","SPAC4H3.04c","SPBC21B10.07","SPAC17G6.06","SPBC725.10","SPAC30D11.11","SPAC694.02","SPCC1450.05c","SPAC4G8.13c","SPAC4H3.05","SPBC16H5.11c","SPCC1739.06c","SPCC364.03","SPBC1778.05c","SPBC26H8.05c","SPCC18.14c","SPAC20G4.02c","SPAC1039.02","SPAC57A7.08","SPAC23C4.09c","SPAC186.06","SPBC2G5.02c","SPCC1682.06","SPBP8B7.09c","SPCC191.11","SPBC902.06","SPBC19G7.05c","SPCC1682.08c","SPBC365.20c","SPBC31A8.01c","SPCC285.11","SPAC1F5.08c","SPAC227.18","SPBC29A10.16c","SPBC32H8.11","SPCC965.13","SPAC4G9.10","SPAC23G3.02c","SPBC4B4.06","SPAC1610.02c","SPBC839.05c","SPCC1183.11","SPBC30B4.04c","SPAC4D7.03","SPAC13G7.12c","SPCC1450.11c","SPCC162.12","SPCC162.06c","SPAC328.04","SPBC29A10.01","SPBC12C2.03c","SPAC6G9.03c","SPAC13G7.04c","SPAC3F10.11c","SPBC1289.13c","SPAC25H1.05","SPAC23A1.03","SPBC1347.02","SPBC337.03","SPAPB1A10.15","SPAC1527.03","SPBC17G9.10","SPCC794.09c","SPBC2F12.11c","SPAC1399.04c","SPAC1805.02c","SPBC887.16","SPAC19D5.01","SPAC4D7.11","SPCC794.07","SPCC1494.05c","SPBC15D4.07c","SPAC15A10.16","SPAC6C3.08","SPAC30C2.04","SPBC1A4.05","SPAC17G6.03","SPAPB1E7.06c","SPBC1718.07c","SPAC23C11.04c","SPAPB1E7.04c","SPBC1861.03","SPCC306.11","SPAC458.02c","SPCC1322.03","SPAC1142.02c","SPBP35G2.14","SPAC15A10.10","SPAC3A12.12","SPCC1235.11","SPCC962.04","SPAC1A6.09c","SPBC32H8.08c","SPAC23A1.06c","SPAC31A2.09c","SPCC1322.08","SPBC2G2.06c","SPBC18H10.08c","SPBC12D12.07c","SPBC651.03c","SPAC19A8.03","SPAC4F10.14c","SPBP8B7.06","SPAC1565.07c","SPAC186.04c","SPCP1E11.10","SPBC660.11","SPCC132.04c","SPAC30D11.06c","SPBC119.12","SPAPB1A11.03","SPBC36.07","SPBC20F10.10","SPBC12C2.05c","SPBC2G2.10c","SPBC30D10.04","SPAC222.07c","SPBC713.09","SPBC2F12.05c","SPAC27D7.03c","SPBC18H10.12c","SPAC22H12.01c","SPAC1952.09c","SPBC17G9.08c","SPCC364.06","SPAC1071.02","SPBC27B12.05","SPAC29A4.17c","SPAC1556.07","SPAC24C9.14","SPAC13A11.04c","SPAC22H10.02","SPAC5H10.07","SPAC11E3.15","SPAC12G12.09","SPCC550.03c","SPBC354.08c","SPBC365.07c","SPCC594.01","SPBC428.07","SPCC1450.16c","SPCC61.03","SPAC16E8.05c","SPCP1E11.05c","SPAC732.02c","SPAC19A8.14","SPBC725.14","SPCC1682.15","SPAC323.07c","SPAC5H10.01","SPAC1F7.08","SPBC1348.03","SPBC14C8.05c","SPCC330.12c","SPAC4A8.14","SPACUNK4.16c","SPCC306.02c","SPBC13E7.06","SPAC23D3.10c","SPBC56F2.08c","SPAC8C9.12c","SPBC800.03","SPBC1709.09","SPAC4A8.09c","SPAC1805.01c","SPAC9E9.09c","SPAC29A4.13","SPAC17H9.08","SPBC25H2.05","SPBC31F10.15c","SPAC10F6.04","SPBC354.10","SPAC21E11.04","SPAC57A10.12c","SPAC3G9.11c","SPAC15E1.06","SPAC19A8.11c","SPAC17G6.05c","SPAC630.09c","SPAC17A2.13c","SPBC30B4.06c","SPCC576.02","SPAC750.08c","SPAC6G9.16c","SPBC1709.18","SPBPB2B2.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hydrolysis and efflux: current knowledge and unanswered questions.","citation":"Autophagy 2019 Feb;15(2):212-227","abstract":"Hydrolysis within the vacuole in yeast and the lysosome in mammals is required for the degradation and recycling of a multitude of substrates, many of which are delivered to the vacuole/lysosome by autophagy. In humans, defects in lysosomal hydrolysis and efflux can have devastating consequences, and contribute to a class of diseases referred to as lysosomal storage disorders. Despite the importance of these processes, many of the proteins and regulatory mechanisms involved in hydrolysis and efflux are poorly understood. In this review, we describe our current knowledge of the vacuolar/lysosomal degradation and efflux of a vast array of substrates, focusing primarily on what is known in the yeast  Saccharomyces cerevisiae . We also highlight many unanswered questions, the answers to which may lead to new advances in the treatment of lysosomal storage disorders.  Abbreviations : Ams1: α-mannosidase; Ape1: aminopeptidase I; Ape3: aminopeptidase Y; Ape4: aspartyl aminopeptidase; Atg: autophagy related; Cps1: carboxypeptidase S; CTNS: cystinosin, lysosomal cystine transporter; CTSA: cathepsin A; CTSD: cathepsin D; Cvt: cytoplasm-to-vacuole targeting; Dap2: dipeptidyl aminopeptidase B; GS-bimane: glutathione- S -bimane; GSH: glutathione; LDs: lipid droplets; MVB: multivesicular body; PAS: phagophore assembly site; Pep4: proteinase A; PolyP: polyphosphate; Prb1: proteinase B; Prc1: carboxypeptidase Y; V-ATPase: vacuolar-type proton-translocating ATPase; VTC: vacuolar transporter chaperone.","doi":"10.1080/15548627.2018.1545821","authors":"Parzych KR, Klionsky DJ","authors_abbrev":"Parzych KR et al.","pubmed_publication_date":"Feb 2019","pubmed_entrez_date":"2018-11-14","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24C9.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15068790","title":"Rsp1p, a J domain protein required for disassembly and assembly of microtubule organizing centers during the fission yeast cell cycle.","citation":"Dev Cell 2004 Apr;6(4):497-509","abstract":"Regulation of microtubule organizing centers (MTOCs) orchestrates the reorganization of the microtubule (MT) cytoskeleton. In the fission yeast Schizosaccharomyces pombe, an equatorial MTOC (eMTOC) at the cell division site disassembles after cytokinesis, and multiple interphase MTOCs (iMTOCs) appear on the nucleus. Here, we show that, upon eMTOC disassembly, small satellites carrying MTOC components such as the gamma-tubulin complex travel in both directions along interphase MTs. We identify rsp1p, an MTOC protein required for eMTOC disassembly. In rsp1 loss-of-function mutants, the eMTOC persists and organizes an abnormal microtubule aster, while iMTOCs and satellites are greatly reduced. Conversely, rsp1p overexpression inhibits eMTOC formation. Rsp1p is a J domain protein that interacts with an hsp70. Thus, our findings suggest a model in which rsp1p is part of a chaperone-based mechanism that disassembles the eMTOC into satellites, contributing to the dynamic redistribution of MTOC components for organization of interphase microtubules.","authors":"Zimmerman S, Tran PT, Daga RR, Niwa O, Chang F","authors_abbrev":"Zimmerman S et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-04-08","publication_year":"2004","canto_session_key":"081f29c16c8596ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-07-14 08:00:19","canto_approved_date":"2026-06-08 22:08:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-07-14 07:59:57","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":25,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.04c","SPBC11B10.05c","SPAC13G7.02c","SPBC365.15"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2022-07-14"},{"uniquename":"PMID:8412690","title":"Translation elongation factor 3: a fungus-specific translation factor?","citation":"Mol Microbiol 1993 Aug;9(3):411-8","abstract":"Fungi appear to be unique in their requirement for a third soluble translation elongation factor. This factor, designated elongation factor 3 (EF-3), was first described in the yeast Saccharomyces cerevisiae and has subsequently been identified in a wide range of fungal species including Candida albicans and Schizosaccharomyces pombe. EF-3 exhibits ribosome-dependent ATPase and GTPase activities that are not intrinsic to the fungal ribosome, but which are essential for translation elongation. Recent studies on the structure of EF-3 from several fungal species have shown that it consists of a repeated domain, with each domain containing the expected putative ATP- and GTP-binding motifs. Overall, EF-3 shows striking amino acid similarity to members of the ATP-binding Cassette (ABC) family of membrane-associated transport proteins although EF-3 is not itself directly membrane-associated. Regions of the EF-3 polypeptide also show structural homology with other translation-associated factors including aminoacyl-tRNA synthetases and the Escherichia coli ribosomal protein S5. While the precise role of EF-3 in the translation elongation cycle remains to be defined, recent evidence suggests that it may be involved in optimizing accuracy during mRNA decoding at the ribosomal A site. Furthermore, the essential nature of EF-3 with respect to the fungal cell indicates that it may be an effective antifungal target. Its apparently ubiquitous occurrence throughout the fungal kingdom also suggests that it may be a useful fungal taxonomic marker.","authors":"Belfield GP, Tuite MF","authors_abbrev":"Belfield GP et al.","pubmed_publication_date":"Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19446322","title":"Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base.","citation":"Cell 2009 May 29;137(5):887-99","abstract":"The central protease of eukaryotes, the 26S proteasome, has a 20S proteolytic core particle (CP) and an attached 19S regulatory particle (RP). The RP is further subdivided into lid and base subcomplexes. Little is known about RP assembly. Here, we show that four conserved assembly factors govern biogenesis of the yeast RP base. Nas2 forms a complex with the Rpt4 and Rpt5 ATPases and enhances 26S proteasome formation in vivo and in vitro. Other RP subcomplexes contain Hsm3, which is related to mammalian proteasome subunit S5b. Hsm3 also contributes to base assembly. Larger Hsm3-containing complexes include two additional proteins, Nas6 and Rpn14, which function as assembly chaperones as well. Specific deletion combinations affecting these four factors cause severe perturbations to RP assembly. Our results demonstrate that proteasomal RP biogenesis requires multiple, functionally overlapping chaperones and suggest a model in which subunits form specific subcomplexes that then assemble into the base.","doi":"10.1016/j.cell.2009.04.061","authors":"Funakoshi M, Tomko RJ, Kobayashi H, Hochstrasser M","authors_abbrev":"Funakoshi M et al.","pubmed_publication_date":"29 May 2009","pubmed_entrez_date":"2009-05-19","publication_year":"2009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011749","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9034194","title":"Regulation of telomere length and function by a Myb-domain protein in fission yeast.","citation":"Nature 1997 Feb 20;385(6618):744-7","abstract":"Telomeres, the specialized nucleoprotein structures that comprise the ends of eukaryotic chromosomes, are essential for complete replication, and regulation of their length has been a focus of research on tumorigenesis. In the budding yeast Saccharomyces cerevisiae, the protein Rap1p binds to telomeric DNA and functions in the regulation of telomere length. A human telomere protein, hTRF (human TTAGGG repeat factor) binds the telomere sequence in vitro and localizes to telomeres cytologically, but its functions are not yet known. Here we use a genetic screen to identify a telomere protein in fission yeast, Taz1p (telomere-associated in Schizosaccharomyces pombe), that shares homology to the Myb proto-oncogene DNA-binding domain with hTRF. Disruption or deletion of the taz1+ gene causes a massive increase in telomere length. Taz1p is required for the repression of telomere-adjacent gene expression and for normal meiosis or sporulation. It may be a negative regulator of the telomere-replicating enzyme, telomerase, or may protect against activation of telomerase-independent pathways of telomere elongation.","authors":"Cooper JP, Nimmo ER, Allshire RC, Cech TR","authors_abbrev":"Cooper JP et al.","pubmed_publication_date":"20 Feb 1997","pubmed_entrez_date":"1997-02-20","publication_year":"1997","canto_session_key":"4213fca1125312b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-11 11:38:05","canto_approved_date":"2026-02-22 14:30:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-09 18:04:51","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-12-11"},{"uniquename":"PMID:2181274","title":"Identification of Schizosaccharomyces pombe transcription factor PGA4, which binds cooperatively to Saccharomyces cerevisiae GAL4-binding sites.","citation":"Mol Cell Biol 1990 Apr;10(4):1432-8","abstract":"When the DNA-binding site for the Saccharomyces cerevisiae transcription activator GAL4 is placed upstream of the Schizosaccharomyces pombe ADH1 TATA box, transcription of the ADH1 gene is activated in S. pombe in vivo by an endogenous transcription factor. In vitro studies show that this S. pombe protein, PGA4, binds specifically to DNA containing a GAL4 site and that when two GAL4 sites are present, this protein binds cooperatively. Cooperating binding of PGA4 to DNA is favored if the GAL4 sites are separated by an integral number of turns of the DNA helix.","authors":"Ruden DM","authors_abbrev":"Ruden DM","pubmed_publication_date":"Apr 1990","pubmed_entrez_date":"1990-04-01","publication_year":"1990","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22306284","title":"Metabolic remodeling in iron-deficient fungi.","citation":"Biochim Biophys Acta 2012 Sep;1823(9):1509-20","abstract":"Eukaryotic cells contain dozens, perhaps hundreds, of iron-dependent proteins, which perform critical functions in nearly every major cellular process. Nutritional iron is frequently available to cells in only limited amounts; thus, unicellular and higher eukaryotes have evolved mechanisms to cope with iron scarcity. These mechanisms have been studied at the molecular level in the model eukaryotes Saccharomyces cerevisiae and Schizosaccharomyces pombe, as well as in some pathogenic fungi. Each of these fungal species exhibits metabolic adaptations to iron deficiency that serve to reduce the cell's reliance on iron. However, the regulatory mechanisms that accomplish these adaptations differ greatly between fungal species. This article is part of a Special Issue entitled: Cell Biology of Metals.","doi":"10.1016/j.bbamcr.2012.01.012","authors":"Philpott CC, Leidgens S, Frey AG","authors_abbrev":"Philpott CC et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-02-07","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8862522","title":"A connection between pre-mRNA splicing and the cell cycle in fission yeast: cdc28+ is allelic with prp8+ and encodes an RNA-dependent ATPase/helicase.","citation":"Mol Biol Cell 1996 Jul;7(7):1083-94","abstract":"The fission-yeast gene cdc28+ was originally identified in a screen for temperature-sensitive mutants that exhibit a cell-division cycle arrest and was found to be required for mitosis. We undertook a study of this gene to understand more fully the general requirements for entry into mitosis. Cells carrying the conditional lethal cdc28-P8 mutation divide once and arrest in G2 after being shifted to the restrictive temperature. We cloned the cdc28+ gene by complementation of the temperature-sensitive growth arrest in cdc28-P8. DNA sequence analysis indicated that cdc28+ encodes a member of the DEAH-box family of putative RNA-dependent ATPases or helicases. The Cdc28 protein is most similar to the Prp2, Prp16, and Prp22 proteins from budding yeast, which are required for the splicing of mRNA precursors. Consistent with this similarity, the cdc28-P8 mutant accumulates unspliced precursors at the restrictive temperature. Independently, we isolated a temperature-sensitive pre-mRNA splicing mutant prp8-1 that exhibits a cell-cycle phenotype identical to that of cdc28-P8. We have shown that cdc28 and prp8 are allelic. These results suggest a connection between pre-mRNA splicing and progression through the cell cycle.","authors":"Lundgren K, Allan S, Urushiyama S, Tani T, Ohshima Y, Frendewey D, Beach D","authors_abbrev":"Lundgren K et al.","pubmed_publication_date":"Jul 1996","pubmed_entrez_date":"1996-07-01","publication_year":"1996","canto_session_key":"190db567d6fe649a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-05-29 15:21:45","canto_approved_date":"2026-01-29 12:49:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-20 14:56:58","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.01","SPBC6B1.07","SPBC146.07","SPSNRNA.06","SPBP22H7.07","SPAC29E6.08"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2014-05-29"},{"uniquename":"EMBL:D89114","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23195958","title":"Anaphase-promoting complex/cyclosome-mediated proteolysis of Ams2 in the G1 phase ensures the coupling of histone gene expression to DNA replication in fission yeast.","citation":"J Biol Chem 2013 Jan 11;288(2):928-37","abstract":"Histone transcription and deposition are tightly regulated with the DNA replication cycle to maintain genetic integrity. Ams2 is a GATA-containing transcription factor responsible for core histone gene expression and for CENP-A loading at centromeres in fission yeast. Ams2 levels are cell cycle-regulated, and after the S phase Ams2 is degraded by the SCF(pof3) ubiquitin ligase; however, the regulation of Ams2 in G(1) or meiosis is poorly understood. Here we show that another ubiquitin ligase, the anaphase-promoting complex/cyclosome (APC/C) targets Ams2 for destruction in G(1). Ubiquitylation and destruction of Ams2 is dependent upon a coactivator Cdh1/Ste9 and the KEN box in the C terminus of Ams2. We also find that stabilization of Ams2 sensitizes cells to the anti-microtubule drug thiabendazole and the histone deacetylase inhibitor tricostatin A when a histone deacetylase gene hst4 is deleted, suggesting that histone acetylation together with Ams2 stability ensures the coupling of mitosis to DNA replication. Furthermore, in meiosis, the failure of the APC/C-mediated destruction of Ams2 is deleterious, and pre-meiotic DNA replication is barely completed. These data suggest that Ams2 destruction via both the APC/C and the SCF ubiquitin ligases underlies the coordination of histone expression and DNA replication.","doi":"10.1074/jbc.M112.410241","authors":"Trickey M, Fujimitsu K, Yamano H","authors_abbrev":"Trickey M et al.","pubmed_publication_date":"11 Jan 2013","pubmed_entrez_date":"2012-12-01","publication_year":"2013","canto_session_key":"57f575f9cbaf2c11","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC290.04","SPAC1783.04c","SPAC144.13c","SPCC1259.13"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:8730105","title":"Heterologous expression of the human cyclin-dependent kinase inhibitor p21Cip1 in the fission yeast, Schizosaccharomyces pombe reveals a role for PCNA in the chk1+ cell cycle checkpoint pathway.","citation":"Mol Biol Cell 1996 Apr;7(4):651-62","abstract":"Fission yeast cells expressing the human gene encoding the cyclin-dependent kinase inhibitor protein p21Cip1 were severely compromised for cell cycle progress. The degree of cell cycle inhibition was related to the level of p21Cip1 expression. Inhibited cells had a 2C DNA content and were judged by cytology and pulsed field gel electrophoresis to be in the G2 phase of the cell cycle. p21Cip1 accumulated in the nucleus and was associated with p34cdc2 and PCNA. Thus, p21Cip1 interacts with the same targets in fission yeast as in mammalian cells. Elimination of p34cdc2 binding by mutation within the cyclin-dependent kinase binding domain of p21Cip1 exaggerated the cell cycle delay phenotype. By contrast, elimination of PCNA binding by mutation within the PCNA-binding domain completely abolished the cell cycle inhibitory effects. Yeast cells expressing wild-type p21Cip1 and the mutant form that is unable to bind p34cdc2 showed enhanced sensitivity to UV. Cell cycle inhibition by p21Cip1 was largely abolished by deletion of the chk1+ gene that monitors radiation damage and was considerably enhanced in cells deleted for the rad3+ gene that monitors both DNA damage and the completion of DNA synthesis. Overexpression of PCNA also resulted in cell cycle arrest in G2 and this phenotype was also abolished by deletion of chk1+ and enhanced in cells deleted for rad3+. These results formally establish a link between PCNA and the products of the rad3+ and chk1+ checkpoint genes.","authors":"Tournier S, Leroy D, Goubin F, Ducommun B, Hyams JS","authors_abbrev":"Tournier S et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_session_key":"51714dbc5142f104","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-01-15 16:22:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-01-15 16:16:17","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.09"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2016-01-15"},{"uniquename":"PMID:18628834","title":"Featured organism: Schizosaccharomyces pombe, the fission yeast.","citation":"Comp Funct Genomics 2002;3(2):194-204","abstract":"Schizosaccharomyces pombe, the fission yeast, has long been a crucial model for the study of the eukaryote cell cycle. We take a look at this important yeast, whose genome has recently been completed, featuring comments from Valerie Wood, Jürg Bähler, Ramsay McFarlane, Susan Forsburg, Iain Hagan and Paul Nurse on the implications of having the complete sequence and future prospects for pombe genomics.","doi":"10.1002/cfg.92","authors":"Wixon J","authors_abbrev":"Wixon J","pubmed_publication_date":"2002","pubmed_entrez_date":"2008-07-17","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25263959","title":"Structural and functional insights into the N-terminus of Schizosaccharomyces pombe Cdc5.","citation":"Biochemistry 2014 Oct 21;53(41):6439-51","abstract":"The spliceosome is a dynamic macromolecular machine composed of five small nuclear ribonucleoparticles (snRNPs), the NineTeen Complex (NTC), and other proteins that catalyze the removal of introns mature to form the mature message. The NTC, named after its founding member Saccharomyces cerevisiae Prp19, is a conserved spliceosome subcomplex composed of at least nine proteins. During spliceosome assembly, the transition to an active spliceosome correlates with stable binding of the NTC, although the mechanism of NTC function is not understood. Schizosaccharomyces pombe Cdc5, a core subunit of the NTC, is an essential protein required for pre-mRNA splicing. The highly conserved Cdc5 N-terminus contains two canonical Myb (myeloblastosis) repeats (R1 and R2) and a third domain (D3) that was previously classified as a Myb-like repeat. Although the N-terminus of Cdc5 is required for its function, how R1, R2, and D3 each contribute to functionality is unclear. Using a combination of yeast genetics, structural approaches, and RNA binding assays, we show that R1, R2, and D3 are all required for the function of Cdc5 in cells. We also show that the N-terminus of Cdc5 binds RNA in vitro. Structural and functional analyses of Cdc5-D3 show that, while this domain does not adopt a Myb fold, Cdc5-D3 preferentially binds double-stranded RNA. Our data suggest that the Cdc5 N-terminus interacts with RNA structures proposed to be near the catalytic core of the spliceosome.","doi":"10.1021/bi5008639","authors":"Collier SE, Voehler M, Peng D, Ohi R, Gould KL, Reiter NJ, Ohi MD","authors_abbrev":"Collier SE et al.","pubmed_publication_date":"21 Oct 2014","pubmed_entrez_date":"2014-09-30","publication_year":"2014","canto_session_key":"cd72aac7fa27eae4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-10-01 00:15:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.12","SPSNRNA.06","SPAC29E6.02"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:25826296","title":"5-Alkyl-1,2,3,4-tetrahydroquinolines, new membrane-interacting lipophilic metabolites produced by combined culture of Streptomyces nigrescens and Tsukamurella pulmonis.","citation":"Org Lett 2015 Apr 17;17(8):1918-21","abstract":"Eight novel 5-alkyl-1,2,3,4-tetrahydroquinolines (5aTHQs) bearing different side chains have been isolated from a combined culture of Streptomyces nigrescens HEK616 and Tsukamurella pulmonis TP-B0596. The chemical structures including the absolute configuration were elucidated by spectroscopic analysis and total synthesis. 5aTHQs inhibited the growth of wild-type fission yeast while only weakly inhibiting the growth of several mutant strains synthesizing premature ergosterol. These results demonstrate that 5aTHQs are novel antifungals that may target cell membranes.","doi":"10.1021/acs.orglett.5b00607","authors":"Sugiyama R, Nishimura S, Ozaki T, Asamizu S, Onaka H, Kakeya H","authors_abbrev":"Sugiyama R et al.","pubmed_publication_date":"17 Apr 2015","pubmed_entrez_date":"2015-04-01","publication_year":"2015","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2015-04-02 00:18:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22682874","title":"Sensor and effector kinases in DNA damage checkpoint regulate capacity for homologous recombination repair of fission yeast in G2 phase.","citation":"DNA Repair (Amst) 2012 Aug 01;11(8):666-75","abstract":"Although the G2/M DNA damage checkpoint is currently viewed as a set of coordinated cellular responses affecting both cell cycle progression and non-cell cycle targets, the relative contributions of the two target categories to DNA repair and cell survival after exposure to ionizing radiation have not been clearly addressed. We investigated how rad3 (ATR ortholog) or chk1/cds1 (CHK1/CHK2 orthologs) null mutations change the kinetics of double-strand break (DSB) repair in Schizosaccharomyces pombe cells under conditions of forced G2 arrest. After 200-Gy γ-ray irradiation, DSBs were repaired in rad3Δ cdc25-22 or chk1Δ cds1Δ cdc25-22 cells, almost as efficiently as in cdc25-22 cells at the restrictive temperature. In contrast, little repair was observed in the checkpoint-deficient cells up to 4h after higher-dose (500Gy) irradiation, whereas repair was still efficient in the control cdc25-22 cells. Immediate loss of viability appeared not be responsible for the repair defect after the higher dose, since both checkpoint-proficient and deficient cells with cdc25-22 allele synchronously resumed cycling with a similar time course when released to the permissive temperature 4h after irradiation. Recruitment of repair proteins Rad11 (Rpa1 ortholog), Rad22 (Rad52 ortholog), and Rhp54 (Rad54 ortholog) to the damage sites was not significantly impaired in the checkpoint-deficient cells, whereas their release was profoundly delayed. Our results suggest that sensor and effector kinases in the damage checkpoint machinery affect the efficiency of repair downstream of, or in parallel with the core repair reaction.","doi":"10.1016/j.dnarep.2012.05.006","authors":"Yasuhira S, Saito T, Maesawa C, Masuda T","authors_abbrev":"Yasuhira S et al.","pubmed_publication_date":"01 Aug 2012","pubmed_entrez_date":"2012-06-12","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC24H6.05","SPBC216.05","SPCC1259.13"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:19666198","title":"Enhancement of survival of probiotic and non-probiotic lactic acid bacteria by yeasts in fermented milk under non-refrigerated conditions.","citation":"Int J Food Microbiol 2009 Sep 30;135(1):34-8","abstract":"The effects of yeasts on the survival of probiotic and non-probiotic lactic acid bacteria (LAB) were studied in fermented milk under non-refrigerated conditions (30 degrees C) with a view to develop ambient-stable fermented milk with live LAB. Five yeasts tested (Saccharomyces bayanus, Williopsis saturnus var. saturnus, Yarrowia lipolytica, Candida kefyr and Kluyveromyces marxianus) enhanced the survival of Lactobacillus bulgaricus (but not Streptococcus thermophilus) in a mixed yoghurt culture in yoghurt by approximately 10(2) to 10(5)-fold. Seven yeasts examined (Candida krusei, Geotrichum candidum, Pichia subpelliculosa, Kloeckera apiculata, Pichia membranifaciens, Schizosaccharomyces pombe and Y. lipolytica) improved the survival of Lactobacillus rhamnosus in fermented milk by approximately10(3) to 10(6)-fold. W. saturnus var. saturnus enhanced the survival of Lactobacillus acidophilus, L. rhamnosus (probiotic) and Lactobacillus reuteri by up to 10(6)-fold, but the same yeast failed to improve the survival of Lactobacillus johnsonii (probiotic), S. thermophilus and L. bulgaricus in fermented milk. These results provide definitive evidence that yeasts possess stability-enhancing effects on LAB and that the specific effects of yeasts on LAB stability vary with yeasts as well as with LAB. However, the molecular mechanism of such interaction of yeasts with LAB remains to be found.","doi":"10.1016/j.ijfoodmicro.2009.07.017","authors":"Liu SQ, Tsao M","authors_abbrev":"Liu SQ et al.","pubmed_publication_date":"30 Sep 2009","pubmed_entrez_date":"2009-08-12","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25774833","title":"The telomere bouquet regulates meiotic centromere assembly.","citation":"Nat Cell Biol 2015 Apr;17(4):458-69","abstract":"The role of the conserved meiotic telomere bouquet has been enigmatic for over a century. We showed previously that disruption of the fission yeast bouquet impairs spindle formation in approximately half of meiotic cells. Surprisingly, bouquet-deficient meiocytes with functional spindles harbour chromosomes that fail to achieve spindle attachment. Kinetochore proteins and the centromeric histone H3 variant Cnp1 fail to localize to those centromeres that exhibit spindle attachment defects in the bouquet's absence. The HP1 orthologue Swi6 also fails to bind these centromeres, suggesting that compromised pericentromeric heterochromatin underlies the kinetochore defects. We find that centromeres are prone to disassembly during meiosis, but this is reversed by localization of centromeres to the telomere-proximal microenvironment, which is conducive to heterochromatin formation and centromere reassembly. Accordingly, artificially tethering a centromere to a telomere rescues the tethered centromere but not other centromeres. These results reveal an unanticipated level of control of centromeres by telomeres.","doi":"10.1038/ncb3132","authors":"Klutstein M, Fennell A, Fernández-Álvarez A, Cooper JP","authors_abbrev":"Klutstein M et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-03-17","publication_year":"2015","canto_session_key":"1e5d35a735b173da","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-18 01:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9236781","title":"The Schizosaccharomyces pombe mam1 gene encodes an ABC transporter mediating secretion of M-factor.","citation":"Mol Gen Genet 1997 Jun;255(2):226-36","abstract":"In the fission yeast Schizosaccharomyces pombe, cells of opposite mating type communicate via diffusible peptide pheromones prior to mating. We have cloned the S. pombe mam1 gene, which encodes a 1336-amino acid protein belonging to the ATP-binding cassette (ABC) superfamily. The mam1 gene is only expressed in M cells and the gene product is responsible for the secretion of the mating pheromone. M-factor, a nonapeptide that is S-farnesylated and carboxy-methylated on its C-terminal cysteine residue. The predicted Mam1 protein is highly homologous to mammalian multiple drug-resistance proteins and to the Saccharomyces cerevisiae STE6 gene product, which mediates export of a-factor mating pheromone. We show that STE6 can also mediate secretion of M-factor in S. pombe.","authors":"Christensen PU, Davey J, Nielsen O","authors_abbrev":"Christensen PU et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"bb1e1e8de651f26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-13 17:15:36","canto_approved_date":"2021-05-22 19:03:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-16 22:37:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25B2.02c","SPAC513.03","SPBC32C12.02","SPAPB8E5.05","SPBPJ4664.03"],"gene_count":5,"ltp_gene_count":1,"approved_date":"2017-02-13"},{"uniquename":"EMBL:AU006661","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29125939","title":"Regulation of microbial growth by turgor pressure.","citation":"Curr Opin Microbiol 2018 Apr;42:62-70","abstract":"Rapid changes in environmental osmolarity are a natural aspect of microbial lifestyles. The change in turgor pressure resulting from an osmotic shock alters the mechanical forces within the cell envelope, and can impact cell growth across a range of timescales, through a variety of mechanical mechanisms. Here, we first summarize measurements of turgor pressure in various organisms. We then review how the combination of microfluidic flow cells and quantitative image analysis has driven discovery of the diverse ways in which turgor pressure mechanically regulates bacterial growth, independent of the effect of cytoplasmic crowding. In Gram-positive, rod-shaped bacteria, reductions in turgor pressure cause decreased growth rate. Moreover, a hypoosmotic shock, which increases turgor pressure and membrane tension, leads to transient inhibition of cell-wall growth via electrical depolarization. By contrast, Gram-negative Escherichia coli is remarkably insensitive to changes in turgor. We discuss the extent to which turgor pressure impacts processes such as cell division that alter cell shape, in particular that turgor facilitates millisecond-scale daughter-cell separation in many Actinobacteria and eukaryotic fission yeast. This diverse set of responses showcases the potential for using osmotic shocks to interrogate how mechanical perturbations affect cellular processes.","doi":"10.1016/j.mib.2017.10.015","authors":"Rojas ER, Huang KC","authors_abbrev":"Rojas ER et al.","pubmed_publication_date":"Apr 2018","pubmed_entrez_date":"2017-11-11","publication_year":"2018","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2017-11-12 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8246883","title":"The amiloride resistance gene, car1, of Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1993 Nov;241(3-4):298-304","abstract":"Amiloride, an inhibitor of various sodium transporters, is toxic to Schizosaccharomyces pombe at low concentration in minimal but not in rich media. Amiloride-resistant mutants were isolated and shown to represent a new locus (car1 for changed amiloride resistance) on chromosome I. The car1 gene was cloned and sequenced. Sequence analysis revealed an open reading frame of 526 amino acids with a predicted molecular weight of 58,545 Da. It has 52% hydrophobic residues and belongs to the class of 12-transmembrane-domain transport proteins. Gene disruption of car1 results in increased amiloride resistance. car1 has sequence similarity to proteins from Candida associated with resistance to benomyl, methotrexate and cycloheximide. No single physiologically identifiable component of sodium transport appeared to be lost. We propose that car1 serves an uptake function, perhaps as a symport with an unknown substrate and this carrier may transport amiloride into the cell. Further, we suggest that amiloride toxicity at low concentrations is not due to its effect on sodium transport but, rather, depends on intracellular interference with an unknown biosynthetic pathway.","authors":"Jia ZP, McCullough N, Wong L, Young PG","authors_abbrev":"Jia ZP et al.","pubmed_publication_date":"Nov 1993","pubmed_entrez_date":"1993-11-01","publication_year":"1993","canto_session_key":"31832f59322d8b26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-29 12:55:55","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-25 14:02:58","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A2.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-25"},{"uniquename":"PMID:37191320","title":"Hva22, a REEP family protein in fission yeast, promotes reticulophagy in collaboration with a receptor protein.","citation":"Autophagy 2023 Oct;19(10):2657-2667","abstract":"The endoplasmic reticulum (ER) undergoes selective autophagy called reticulophagy or ER-phagy. Multiple reticulon- and receptor expression enhancing protein (REEP)-like ER-shaping proteins, including budding yeast Atg40, serve as reticulophagy receptors that stabilize the phagophore on the ER by interacting with phagophore-conjugated Atg8. Additionally, they facilitate phagophore engulfment of the ER by remodeling ER morphology. We reveal that Hva22, a REEP family protein in fission yeast, promotes reticulophagy without Atg8-binding capacity. The role of Hva22 in reticulophagy can be replaced by expressing Atg40 independently of its Atg8-binding ability. Conversely, adding an Atg8-binding sequence to Hva22 enables it to substitute for Atg40 in budding yeast. Thus, the phagophore-stabilizing and ER-shaping activities, both of which Atg40 solely contains, are divided between two separate factors, receptors and Hva22, respectively, in fission yeast. Abbreviations:  AIM: Atg8-family interacting motif; Atg: autophagy related; DTT: dithiothreitol; ER: endoplasmic reticulum GFP: green fluorescent protein; NAA: 1-naphthaleneacetic acid; REEP: receptor expression enhancing protein; RFP: red fluorescent protein; UPR: unfolded protein response.","doi":"10.1080/15548627.2023.2214029","authors":"Fukuda T, Saigusa T, Furukawa K, Inoue K, Yamashita SI, Kanki T","authors_abbrev":"Fukuda T et al.","pubmed_publication_date":"Oct 2023","pubmed_entrez_date":"2023-05-16","publication_year":"2023","canto_session_key":"2d8412a36a34689a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomoyuki Fukuda","canto_first_approved_date":"2023-06-13 15:43:30","canto_approved_date":"2025-09-04 12:46:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-13 03:49:06","canto_added_date":"2023-05-17 00:15:04","annotation_curators":[{"name":"Tomoyuki Fukuda","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1539.04","SPBC31A8.01c","SPAC222.14c","SPCC1620.07c","SPBC30D10.09c","SPCC830.08c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2023-06-13"},{"uniquename":"PMID:12132578","title":"Cloning and characterization of the kinesin-related protein, Krp1p, in Schizosaccharomyces pombe.","citation":"Mol Cells 2002 Jun 30;13(3):389-98","abstract":"Kinesin have been cloned in many organisms. They played important roles in the transport of cell organelles, polarized growth, and secretion. We report here the identification of a kinesin-related protein in Schizosaccharomyces pombe, which was named kinesin-related protein (Krplp). The primer sequences were driven from the highly conserved area of the kinesin genes in other organisms. We cloned kinesin genes from S. pombe using the PCR technique. Sequence analysis revealed that krp1+ has a 1,665 bp open-reading frame (ORF) that encoded a protein that consisted of 554 amino acids with a molecular weight of 61,900. It is homologous to the proteins that belong to the kinesin heavy chain (KHC) superfamily [GenBank accession No. AF156966 (genomic DNA) and AF247188 (mRNA)]. To characterize Krplp, the gene was disrupted and overexpressed in S. pombe. Cells that contained a krp1+ null allele were viable. Overexpression of Krp1p resulted in the inhibition of mitotic growth; cells became elongated, branched, and formed aberrant septa. To identify proteins that interact with Krplp, the yeast two-hybrid system was used. As a result, the novel protein, designated kinesin associated protein (Kap1p), was identified and showed structural homology to the proteins of the myosin family (GenBank accession No. AF351206). The data from the overexpression and two-hybrid study of Krplp may provide information that Krplp can have roles in cytokinesis with myosin.","authors":"Jeong JW, Rhee DK, Cho SY, Hae KL, Kim DU, Won M, Kim HB","authors_abbrev":"Jeong JW et al.","pubmed_publication_date":"30 Jun 2002","pubmed_entrez_date":"2002-07-23","publication_year":"2002","canto_session_key":"f0cb00d1d6a5715f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-02-28 17:57:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-20 11:16:52","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.07","SPBC28F2.10c","SPAC22E12.09c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-08-20"},{"uniquename":"PMID:16893973","title":"Meiotic cohesins modulate chromosome compaction during meiotic prophase in fission yeast.","citation":"J Cell Biol 2006 Aug 14;174(4):499-508","abstract":"The meiotic cohesin Rec8 is required for the stepwise segregation of chromosomes during the two rounds of meiotic division. By directly measuring chromosome compaction in living cells of the fission yeast Schizosaccharomyces pombe, we found an additional role for the meiotic cohesin in the compaction of chromosomes during meiotic prophase. In the absence of Rec8, chromosomes were decompacted relative to those of wild-type cells. Conversely, loss of the cohesin-associated protein Pds5 resulted in hypercompaction. Although this hypercompaction requires Rec8, binding of Rec8 to chromatin was reduced in the absence of Pds5, indicating that Pds5 promotes chromosome association of Rec8. To explain these observations, we propose that meiotic prophase chromosomes are organized as chromatin loops emanating from a Rec8-containing axis: the absence of Rec8 disrupts the axis, resulting in disorganized chromosomes, whereas reduced Rec8 loading results in a longitudinally compacted axis with fewer attachment points and longer chromatin loops.","authors":"Ding DQ, Sakurai N, Katou Y, Itoh T, Shirahige K, Haraguchi T, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"14 Aug 2006","pubmed_entrez_date":"2006-08-09","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40424131","title":"Formation of giant ER sheets by pentadecanoic acid causes lipotoxicity in fission yeast.","citation":"Proc Natl Acad Sci U S A 2025 Jun 03;122(22):e2422126122","abstract":"Excess amounts of saturated fatty acids (FAs) are toxic to organisms, a condition termed lipotoxicity, which is often accompanied by pleiotropic cellular and tissue dysfunction. Here, we show that pentadecanoic acid (C15:0) exerts toxicity on the fission yeast  Schizosaccharomyces pombe  by generating an aberrantly planar endoplasmic reticulum (ER) structure, which we named a \"giant ER sheet.\" Untargeted lipidomics revealed that C15:0 is incorporated into complex lipids depending on an acyl-CoA ligase Lcf1 and an acyl-CoA transferase Slc1, thereby increasing the saturation level of the acyl chains. The toxicity and giant ER sheet formation were abolished by deleting  lcf1  or  slc1  gene, indicating that the incorporation of C15:0 into glycerophospholipids causes giant ER sheet formation. The giant ER sheets disrupted the correct migration of Mid1, a protein determining the cell division site, and physically blocked septum formation, hindering correct cell separation. Our results suggest that the ER is the primary site targeted by saturated FAs, leading to lipotoxicity.","doi":"10.1073/pnas.2422126122","authors":"Hoshikawa Y, Shirota N, Tsugawa H, Kimura S, Matsuyama A, Yashiroda Y, Kakeya H, Arita M, Iizumi R, Yoshida M, Nishimura S","authors_abbrev":"Hoshikawa Y et al.","pubmed_publication_date":"03 Jun 2025","pubmed_entrez_date":"2025-05-27","publication_year":"2025","canto_session_key":"b262b1ecfc2ddf80","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shinichi Nishimura","canto_first_approved_date":"2026-04-07 07:36:14","canto_approved_date":"2026-04-07 07:36:16","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-02-16 08:17:28","canto_added_date":"2025-05-27 23:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":25,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Shinichi Nishimura","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18H10.02","SPAC1851.02","SPCC1281.06c","SPAC13G7.05","SPBC776.05","SPCP1E11.05c","SPAC1687.16c","SPAC1783.02c","SPBC27B12.03c","SPAC19A8.04","SPAC1952.13","SPBC776.14","SPBC16E9.05","SPAC20G4.07c","SPBC3H7.05c","SPBC16A3.10","SPAC20G8.07c","SPCC1235.15","SPBP4H10.11c","SPBC428.14"],"gene_count":20,"ltp_gene_count":20,"approved_date":"2026-04-07"},{"uniquename":"PMID:12383265","title":"Cold induces stress-activated protein kinase-mediated response in the fission yeast Schizosaccharomyces pombe.","citation":"Eur J Biochem 2002 Oct;269(20):5056-65","abstract":"In the fission yeast Schizosaccharomyces pombe the Wak1p/Win1p-Wis1p-Sty1p stress-activated protein kinase (SAPK) pathway relays environmental signals to the transcriptional machinery and modulates gene expression via a cascade of protein phosphorylation. Cells of S. pombe subjected to cold shock (transfer from 28 degrees C to 15 degrees C) transiently activated the Sty1p mitogen-activated protein kinase (MAPK) by phosphorylation. Induction of this response was completely abolished in cells disrupted in the upstream response regulator Mcs4p. The cold-triggered Sty1p activation was partially dependent on Wak1p MAPKKK and fully dependent on Wis1p MAPKK suggesting that the signal transmission follows a branched pathway, with the redundant MAPKKK Win1p as alternative transducer to Wis1p, which subsequently activates the effector Sty1p MAPK. Also, the bZIP transcription factor Atf1p became phosphorylated in a Sty1p-dependent way during the cold shock and this phosphorylation was found responsible for the increased expression of gpd1+, ctt1+, tps1+ and ntp1+ genes. Strains deleted in transcription factors Atf1p or Pcr1p were unable to grow upon incubation at low temperature whereas those disrupted in any member of the SAPK pathway were able to do so. These data reveal that S. pombe responds to cold by inducing the SAPK pathway. However, such activation is dispensable for yeast growth in cold conditions, supporting that the presence of Atf1/Pcr1 heterodimers, rather than an operative SAPK pathway, is critical to ensure yeast growth at low temperature by an as yet undefined mechanism.","authors":"Soto T, Beltrán FF, Paredes V, Madrid M, Millar JB, Vicente-Soler J, Cansado J, Gacto M","authors_abbrev":"Soto T et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-10-18","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC29B5.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:17389875","title":"Sorting out interphase microtubules.","citation":"Mol Syst Biol 2007;3:95","abstract":"","authors":"Carazo-Salas R, Nurse P","authors_abbrev":"Carazo-Salas R et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-03-29","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31699326","title":"Yeast models of neurodegenerative diseases.","citation":"Prog Mol Biol Transl Sci 2019;168:351-379","abstract":"The yeast Saccharomyces cerevisiae has been used to develop a wide range of highly tractable living models of the major human neurodegenerative diseases. Yet even though this microorganism lacks neuron-specific structures and processes, these models have provided new insights into the underlying disease mechanisms. Furthermore, they have allowed new therapeutic targets to be identified as well as providing a means of identifying potential therapeutic agents using high throughput cell-based screens. In this article, the benefits and limitations of S. cerevisiae-based neurodegenerative disease models are explored. Consideration is also given to future opportunities the exploitation of these models present, including the use of other yeast species such as Schizosaccharomyces pombe.","doi":"10.1016/bs.pmbts.2019.07.001","authors":"Tuite MF","authors_abbrev":"Tuite MF","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-11-09","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-11-10 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21825074","title":"Multispan mitochondrial outer membrane protein Ugo1 follows a unique Mim1-dependent import pathway.","citation":"J Cell Biol 2011 Aug 08;194(3):397-405","abstract":"The mitochondrial outer membrane (MOM) harbors several multispan proteins that execute various functions. Despite their importance, the mechanisms by which these proteins are recognized and inserted into the outer membrane remain largely unclear. In this paper, we address this issue using yeast mitochondria and the multispan protein Ugo1. Using a specific insertion assay and analysis by native gel electrophoresis, we show that the import receptor Tom70, but not its partner Tom20, is involved in the initial recognition of the Ugo1 precursor. Surprisingly, the import pore formed by the translocase of the outer membrane complex appears not to be required for the insertion process. Conversely, the multifunctional outer membrane protein mitochondrial import 1 (Mim1) plays a central role in mediating the insertion of Ugo1. Collectively, these results suggest that Ugo1 is inserted into the MOM by a novel pathway in which Tom70 and Mim1 contribute to the efficiency and selectivity of the process.","doi":"10.1083/jcb.201102041","authors":"Papic D, Krumpe K, Dukanovic J, Dimmer KS, Rapaport D","authors_abbrev":"Papic D et al.","pubmed_publication_date":"08 Aug 2011","pubmed_entrez_date":"2011-08-10","publication_year":"2011","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6B12.12"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19057642","title":"Inter-species complementation of the translocon beta subunit requires only its transmembrane domain.","citation":"PLoS One 2008;3(12):e3880","abstract":"In eukaryotes, proteins enter the secretory pathway through the translocon pore of the endoplasmic reticulum. This protein translocation channel is composed of three major subunits, called Sec61alpha, beta and gamma in mammals. Unlike the other subunits, the beta subunit is dispensable for translocation and cell viability in all organisms studied. Intriguingly, the knockout of the Sec61beta encoding genes results in different phenotypes in different species. Nevertheless, the beta subunit shows a high level of sequence homology across species, suggesting the conservation of a biological function that remains ill-defined. To address its cellular roles, we characterized the homolog of Sec61beta in the fission yeast Schizosaccharomyces pombe (Sbh1p). Here, we show that the knockout of sbh1(+) results in severe cold sensitivity, increased sensitivity to cell-wall stress, and reduced protein secretion at 23 degrees C. Sec61beta homologs from Saccharomyces cerevisiae and human complement the knockout of sbh1(+) in S. pombe. As in S. cerevisiae, the transmembrane domain (TMD) of S. pombe Sec61beta is sufficient to complement the phenotypes resulting from the knockout of the entire encoding gene. Remarkably, the TMD of Sec61beta from S. cerevisiae and human also complement the gene knockouts in both yeasts. Together, these observations indicate that the TMD of Sec61beta exerts a cellular function that is conserved across species.","doi":"10.1371/journal.pone.0003880","authors":"Leroux A, Rokeach LA","authors_abbrev":"Leroux A et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-12-06","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33475456","title":"Maf1 limits RNA polymerase III-directed transcription to preserve genomic integrity and extend lifespan.","citation":"Cell Cycle 2021 Feb;20(3):247-255","abstract":"A key to longevity assurance is the nutrient-sensing mTOR pathway. Inhibition of mTOR extends lifespan in a variety of organisms. However, the downstream effectors of the mTOR pathway for lifespan regulation are elusive. In a recent report, we described the role of Maf1 as a critical lifespan regulator downstream of the mTOR pathway in fission yeast. Maf1 is the master negative regulator of RNA polymerase III-directed transcription (e.g. tRNAs and 5S rRNAs) and is regulated by mTOR-mediated phosphorylation. We demonstrated that Maf1 is required for lifespan extension under calorie restriction or when mTOR is inhibited. We also showed that Maf1 prevents DNA damage at tRNA genes, which appears to contribute to lifespan maintenance by Maf1. Here we highlight these observations and present additional results to discuss the role of the mTOR-Maf1-Pol III axis in promoting genomic integrity in the face of DNA replication-transcription conflicts in order to maintain normal lifespan.","doi":"10.1080/15384101.2021.1874697","authors":"Noguchi C, Wang L, Shetty M, Mell JC, Sell C, Noguchi E","authors_abbrev":"Noguchi C et al.","pubmed_publication_date":"Feb 2021","pubmed_entrez_date":"2021-01-21","publication_year":"2021","canto_session_key":"a7d2055a561975e9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-01-23 01:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31G5.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:4282900","title":"The cell cycle in the fission yeast Schizosaccharomyces pombe: changes in activity of magnesium dependent ATP'ase and in total internal magnesium in relation to cell division.","citation":"Z Allg Mikrobiol 1974;14(8):727-9","abstract":"","authors":"Duffus JH, Paterson LJ","authors_abbrev":"Duffus JH et al.","pubmed_publication_date":"1974","pubmed_entrez_date":"1974-01-01","publication_year":"1974","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17526735","title":"Mek1 kinase is regulated to suppress double-strand break repair between sister chromatids during budding yeast meiosis.","citation":"Mol Cell Biol 2007 Aug;27(15):5456-67","abstract":"Mek1 is a meiosis-specific kinase in budding yeast which promotes recombination between homologous chromosomes by suppressing double-strand break (DSB) repair between sister chromatids. Previous work has shown that in the absence of the meiosis-specific recombinase gene, DMC1, cells arrest in prophase due to unrepaired DSBs and that Mek1 kinase activity is required in this situation to prevent repair of the breaks using sister chromatids. This work demonstrates that Mek1 is activated in response to DSBs by autophosphorylation of two conserved threonines, T327 and T331, in the Mek1 activation loop. Using a version of Mek1 that can be conditionally dimerized during meiosis, Mek1 function was shown to be promoted by dimerization, perhaps as a way of enabling autophosphorylation of the activation loop in trans. A putative HOP1-dependent dimerization domain within the C terminus of Mek1 has been identified. Dimerization alone, however, is insufficient for activation, as DSBs and Mek1 recruitment to the meiosis-specific chromosomal core protein Red1 are also necessary. Phosphorylation of S320 in the activation loop inhibits sister chromatid repair specifically in dmc1Delta-arrested cells. Ectopic dimerization of Mek1 bypasses the requirement for S320 phosphorylation, suggesting this phosphorylation is necessary for maintenance of Mek1 dimers during checkpoint-induced arrest.","authors":"Niu H, Li X, Job E, Park C, Moazed D, Gygi SP, Hollingsworth NM","authors_abbrev":"Niu H et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-05-29","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5929396","title":"The mutagenic activity of N-nitroso-N-methylurethane and N-nitroso-N-ethylurethane in Schizosaccharomyces pombe.","citation":"Mutat Res 1966 Apr;3(2):152-7","abstract":"","authors":"Guglielminetti R, Bonatti S, Loprieno N","authors_abbrev":"Guglielminetti R et al.","pubmed_publication_date":"Apr 1966","pubmed_entrez_date":"1966-04-01","publication_year":"1966","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39485795","title":"A meiotic driver hijacks an epigenetic reader to disrupt mitosis in noncarrier offspring.","citation":"Proc Natl Acad Sci U S A 2024 Nov 05;121(45):e2408347121","abstract":"Killer meiotic drivers (KMDs) are selfish genetic elements that distort Mendelian inheritance by selectively killing meiotic products lacking the KMD element, thereby promoting their own propagation. Although KMDs have been found in diverse eukaryotes, only a limited number of them have been characterized at the molecular level, and their killing mechanisms remain largely unknown. In this study, we identify that a gene previously deemed essential for cell survival in the fission yeast  Schizosaccharomyces pombe  is a single-gene KMD. This gene,  tdk1 , kills nearly all  tdk1Δ  progeny in a  tdk1+  ×  tdk1Δ  cross. By analyzing polymorphisms of  tdk1  among natural strains, we identify a resistant haplotype, HT3. This haplotype lacks killing ability yet confers resistance to killing by the wild-type  tdk1 . Proximity labeling experiments reveal an interaction between Tdk1, the protein product of  tdk1 , and the epigenetic reader Bdf1. Interestingly, the nonkilling Tdk1-HT3 variant does not interact with Bdf1. Cryoelectron microscopy further elucidated the binding interface between Tdk1 and Bdf1, pinpointing mutations within Tdk1-HT3 that disrupt this interface. During sexual reproduction, Tdk1 forms stable Bdf1-binding nuclear foci in all spores after meiosis. These foci persist in germinated  tdk1Δ  progeny and impede chromosome segregation during mitosis by generating aberrant chromosomal adhesions. This study identifies a KMD that masquerades as an essential gene and reveals the molecular mechanism by which this KMD hijacks cellular machinery to execute killing. Additionally, we unveil that losing the hijacking ability is an evolutionary path for this single-gene KMD to evolve into a nonkilling resistant haplotype.","doi":"10.1073/pnas.2408347121","authors":"Hua Y, Zhang J, Yang MY, Zhang FY, Ren JY, Lyu XH, Ding Y, Suo F, Shao GC, Li J, Dong MQ, Ye K, Du LL","authors_abbrev":"Hua Y et al.","pubmed_publication_date":"05 Nov 2024","pubmed_entrez_date":"2024-11-01","publication_year":"2024","canto_session_key":"c40f69f244d75cea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yu Hua","canto_first_approved_date":"2025-01-10 12:29:24","canto_approved_date":"2025-01-10 12:29:24","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-12-26 14:42:23","canto_added_date":"2024-11-02 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":26,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Yu Hua","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.04c","SPCC1450.02","SPAC631.02","SPCC569.03"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2025-01-10","pdb_entries":[{"pdb_id":"9ja5","gene_chains":[{"gene_uniquename":"SPCC330.04c","chain":"A/A/B/B/C/C/D/D/E/E/F/F","position":"211-357"},{"gene_uniquename":"SPCC1450.02","chain":"A/A/B/B/C/C/D/D/E/E/F/F","position":"372-554"}],"title":"Cryo-EM structure of Tdk1-Bdf1 complex","entry_authors":"Zhang J,Ye K","entry_authors_abbrev":"Zhang J et al.","reference_uniquename":"PMID:39485795","experimental_method":"EM","resolution":"2.7"}]},{"uniquename":"PMID:9203581","title":"Fission yeast WD-repeat protein pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the S-phase initiator Cdc18.","citation":"Genes Dev 1997 Jun 15;11(12):1548-60","abstract":"In fission yeast, maintenance of genome ploidy is controlled by at least two mechanisms. One operates through the Cdc2/Cdc13 kinase, which also involves the CDK inhibitor Rum1, and the other through the S-phase regulator Cdc18. By screening for sterile mutants that show increased ploidy, we have identified a new gene, pop1+, in mutants that become polyploid. The pop1 mutation shows a synthetic lethal interaction with the temperature-sensitive cdc2 or cdc13 mutation. In a pop1 mutant Rum1 and Cdc18 proteins become accumulated to high levels. The high ploidy phenotype in the pop1 mutant is dependent on the presence of the rum1+ gene, whereas the accumulation of Cdc18 is independent of Rum1. The predicted sequence of the Pop1 protein indicates that it belongs to a WD-repeat family with highest homology to budding yeast Cdc4, which participates in the ubiquitin-dependent pathway. Consistent with this notion, in a mutant of the 26S proteasome, higher molecular weight forms of Rum1 and Cdc18 are accumulated corresponding to polyubiquitination of these proteins. In the pop1 mutant, however, no ubiquitinated forms of these proteins are detected. Finally we show that Pop1 binds Cdc18 in vivo. We propose that Pop1 functions as a recognition factor for Rum1 and Cdc18, which are subsequently ubiquitinated and targeted to the 26S proteasome for degradation.","authors":"Kominami K, Toda T","authors_abbrev":"Kominami K et al.","pubmed_publication_date":"15 Jun 1997","pubmed_entrez_date":"1997-06-15","publication_year":"1997","canto_session_key":"0a51c60ef15caeb9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-08 22:21:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-05 13:49:31","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC337.08c","SPBC14C8.07c","SPBC1718.01","SPBC32F12.09","SPBC582.03","SPBC12D12.04c","SPBC16G5.01"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-05-05"},{"uniquename":"PMID:24298023","title":"Characterization and in vivo functional analysis of the Schizosaccharomyces pombe ICLN gene.","citation":"Mol Cell Biol 2014 Feb;34(4):595-605","abstract":"During the early steps of snRNP biogenesis, the survival motor neuron (SMN) complex acts together with the methylosome, an entity formed by the pICln protein, WD45, and the PRMT5 methyltransferase. To expand our understanding of the functional relationship between pICln and SMN in vivo, we performed a genetic analysis of an uncharacterized Schizosaccharomyces pombe pICln homolog. Although not essential, the S. pombe ICln (SpICln) protein is important for optimal yeast cell growth. The human ICLN gene complements the Δicln slow-growth phenotype, demonstrating that the identified SpICln sequence is the bona fide human homolog. Consistent with the role of human pICln inferred from in vitro experiments, we found that the SpICln protein is required for optimal production of the spliceosomal snRNPs and for efficient splicing in vivo. Genetic interaction approaches further demonstrate that modulation of ICln activity is unable to compensate for growth defects of SMN-deficient cells. Using a genome-wide approach and reverse transcription (RT)-PCR validation tests, we also show that splicing is differentially altered in Δicln cells. Our data are consistent with the notion that splice site selection and spliceosome kinetics are highly dependent on the concentration of core spliceosomal components.","doi":"10.1128/MCB.01407-13","authors":"Barbarossa A, Antoine E, Neel H, Gostan T, Soret J, Bordonné R","authors_abbrev":"Barbarossa A et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-12-04","publication_year":"2014","canto_session_key":"1bfbcff2428f3678","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-27 15:33:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-01-20 15:08:19","canto_added_date":"2014-01-15 16:20:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC63.08c","SPAC1610.01","SPBC1703.10","SPAC26A3.08","SPAC2G11.08c","SPCC594.01","SPSNRNA.01","SPAC27D7.07c","SPSNRNA.05","SPAC2C4.03c","SPBC11G11.06c","SPSNRNA.06","SPBC4B4.05","SPSNRNA.02","SPBC3E7.14","SPBC649.04","SPBC19C2.14","SPSNRNA.04"],"gene_count":18,"ltp_gene_count":5,"approved_date":"2014-01-20"},{"uniquename":"PMID:39695245","title":"Single-Molecule Tracking dataset for histone H3 (hht1) from live and fixed cells of Schizosaccharomyces pombe.","citation":"Sci Data 2024 Dec 18;11(1):1393","abstract":"Single-molecule tracking provides direct real-time measurements of protein dynamics in live cells with high spatiotemporal resolution. In the last decade, this method has been adopted by several labs to understand the dynamics of DNA replication, transcription, telomerase, chromatin remodeling, etc. in a variety of model systems (bacteria, yeast S. cerevisiae, cell lines, embryo). However, it has not been employed for the yeast Schizosaccharomyces pombe, despite being a valuable model system. Here, we present single-molecule tracking datasets for chromatin-bound histone H3 (Hht1) in live and fixed cells and freely diffusing GFP in S. pombe nuclei to benchmark the diffusion parameters (diffusion coefficient, mean squared displacement, fraction of bound molecules, residence time). These parameters will be used to differentiate chromatin-bound molecules from unbound (free) molecules of any protein. It will be a valuable resource for any lab that starts employing this method for studying protein dynamics. This dataset can also be used to validate the performance of various tracking software and as a training dataset for machine learning-based automated tracking.","doi":"10.1038/s41597-024-04258-0","authors":"Kumari A, Podh NK, Sen S, Kashyap K, Islam S, Gupta A, Rajakumara E, Nambiar M, Mehta G","authors_abbrev":"Kumari A et al.","pubmed_publication_date":"18 Dec 2024","pubmed_entrez_date":"2024-12-18","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-12-20 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36830746","title":"Opposing Roles of FACT for Euchromatin and Heterochromatin in Yeast.","citation":"Biomolecules 2023 Feb 16;13(2)","abstract":"DNA is stored in the nucleus of a cell in a folded state; however, only the necessary genetic information is extracted from the required group of genes. The key to extracting genetic information is chromatin ambivalence. Depending on the chromosomal region, chromatin is characterized into low-density \"euchromatin\" and high-density \"heterochromatin\", with various factors being involved in its regulation. Here, we focus on chromatin regulation and gene expression by the yeast FACT complex, which functions in both euchromatin and heterochromatin. FACT is known as a histone H2A/H2B chaperone and was initially reported as an elongation factor associated with RNA polymerase II. In budding yeast, FACT activates promoter chromatin by interacting with the transcriptional activators SBF/MBF via the regulation of G1/S cell cycle genes. In fission yeast, FACT plays an important role in the formation of higher-order chromatin structures and transcriptional repression by binding to Swi6, an HP1 family protein, at heterochromatin. This FACT property, which refers to the alternate chromatin-regulation depending on the binding partner, is an interesting phenomenon. Further analysis of nucleosome regulation within heterochromatin is expected in future studies.","doi":"10.3390/biom13020377","authors":"Takahata S, Murakami Y","authors_abbrev":"Takahata S et al.","pubmed_publication_date":"16 Feb 2023","pubmed_entrez_date":"2023-02-25","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-02-26 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c","SPAC57A10.09c","SPBC428.08c","SPBC609.05","SPBP8B7.19"],"gene_count":5,"ltp_gene_count":0},{"uniquename":"PMID:9727008","title":"The Pad1+ gene encodes a subunit of the 26 S proteasome in fission yeast.","citation":"J Biol Chem 1998 Sep 11;273(37):23938-45","abstract":"We have isolated a fission yeast mutant, mts5-1, in a screen for mutations that confer both methyl 2-benzimidazolecarbamate resistance (MBCR) and temperature sensitivity (ts) on Schizosaccharomyces pombe. This screen has previously isolated mutations in the 26 S proteasome subunits Mts2, Mts3, and Mts4. We show that the mutation in the mts5-1 strain occurs in the pad1(+) gene. pad1(+) was originally isolated on a multicopy plasmid that was capable of conferring staurosporine resistance on a wild type strain. mts5-1/pad1-1 has a similar phenotype to 26 S proteasome mutants previously isolated in the same screen and we show that Pad1 interacts genetically with two of these subunits, Mts3 and Mts4. In this study we describe the identification of Pad1 as a subunit of the 26 S proteasome in fission yeast.","authors":"Penney M, Wilkinson C, Wallace M, Javerzat JP, Ferrell K, Seeger M, Dubiel W, McKay S, Allshire R, Gordon C","authors_abbrev":"Penney M et al.","pubmed_publication_date":"11 Sep 1998","pubmed_entrez_date":"1998-09-03","publication_year":"1998","canto_session_key":"834e87683256f8a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-01 12:11:27","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-14 15:39:55","canto_added_date":"2012-02-24 05:53:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.13","SPBC16G5.01","SPBP19A11.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-04-14"},{"uniquename":"EMBL:U26014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.31"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28768202","title":"Dual RNA Processing Roles of Pat1b via Cytoplasmic Lsm1-7 and Nuclear Lsm2-8 Complexes.","citation":"Cell Rep 2017 Aug 01;20(5):1187-1200","abstract":"Pat1 RNA-binding proteins, enriched in processing bodies (P bodies), are key players in cytoplasmic 5' to 3' mRNA decay, activating decapping of mRNA in complex with the Lsm1-7 heptamer. Using co-immunoprecipitation and immunofluorescence approaches coupled with RNAi, we provide evidence for a nuclear complex of Pat1b with the Lsm2-8 heptamer, which binds to the spliceosomal U6 small nuclear RNA (snRNA). Furthermore, we establish the set of interactions connecting Pat1b/Lsm2-8/U6 snRNA/SART3 and additional U4/U6.U5 tri-small nuclear ribonucleoprotein particle (tri-snRNP) components in Cajal bodies, the site of snRNP biogenesis. RNA sequencing following Pat1b depletion revealed the preferential upregulation of mRNAs normally found in P bodies and enriched in 3' UTR AU-rich elements. Changes in >180 alternative splicing events were also observed, characterized by skipping of regulated exons with weak donor sites. Our data demonstrate the dual role of a decapping enhancer in pre-mRNA processing as well as in mRNA decay via distinct nuclear and cytoplasmic Lsm complexes.","doi":"10.1016/j.celrep.2017.06.091","authors":"Vindry C, Marnef A, Broomhead H, Twyffels L, Ozgur S, Stoecklin G, Llorian M, Smith CW, Mata J, Weil D, Standart N","authors_abbrev":"Vindry C et al.","pubmed_publication_date":"01 Aug 2017","pubmed_entrez_date":"2017-08-03","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC119.13c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26130711","title":"Two separable functions of Ctp1 in the early steps of meiotic DNA double-strand break repair.","citation":"Nucleic Acids Res 2015 Sep 03;43(15):7349-59","abstract":"Meiotic programmed DNA double-strand break (DSB) repair is essential for crossing-over and viable gamete formation and requires removal of Spo11-oligonucleotide complexes from 5' ends (clipping) and their resection to generate invasive 3'-end single-stranded DNA (resection). Ctp1 (Com1, Sae2, CtIP homolog) acting with the Mre11-Rad50-Nbs1 (MRN) complex is required in both steps. We isolated multiple S. pombe ctp1 mutants deficient in clipping but proficient in resection during meiosis. Remarkably, all of the mutations clustered in or near the conserved CxxC or RHR motif in the C-terminal portion. The mutants tested, like ctp1Δ, were clipping-deficient by both genetic and physical assays-. But, unlike ctp1Δ, these mutants were recombination-proficient for Rec12 (Spo11 homolog)-independent break-repair and resection-proficient by physical assay. We conclude that the intracellular Ctp1 C-terminal portion is essential for clipping, while the N-terminal portion is sufficient for DSB end-resection. This conclusion agrees with purified human CtIP resection and endonuclease activities being independent. Our mutants provide intracellular evidence for separable functions of Ctp1. Some mutations truncate Ctp1 in the same region as one of the CtIP mutations linked to the Seckel and Jawad severe developmental syndromes, suggesting that these syndromes are caused by a lack of clipping at DSB ends that require repair.","doi":"10.1093/nar/gkv644","authors":"Ma L, Milman N, Nambiar M, Smith GR","authors_abbrev":"Ma L et al.","pubmed_publication_date":"03 Sep 2015","pubmed_entrez_date":"2015-07-02","publication_year":"2015","canto_session_key":"f137dd00ee869867","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Gerald Smith","canto_first_approved_date":"2017-11-20 15:52:02","canto_approved_date":"2024-07-23 16:07:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-27 17:38:03","canto_added_date":"2015-07-03 00:20:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":50,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Gerald Smith","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-11-20"},{"uniquename":"PMID:22096330","title":"Intracellular scavenging activity of Trolox (6-hydroxy-2,5,7,8-tetramethylchromane-2-carboxylic acid) in the fission yeast, Schizosaccharomyces pombe.","citation":"J Nat Sci Biol Med 2010 Jul;1(1):16-21","abstract":"The ability of Trolox (6-hydroxy-2,5,7,8-tetramethylchromane-2-carboxylic acid), a water-soluble vitamin E analogue, to prevent oxidative damages is well characterized, but the mechanisms underlying it remain unclear. The protective effect of Trolox pre-treatment on H(2)O(2)-induced toxicity might be attributed to the decreased cellular permeability to H(2)O(2) or in vitro scavenging activity of Trolox, induction of antioxidant enzymes or the direct scavenging activity of Trolox. The results obtained rule out the first and second possibilities and intracellular scavenging activity was found to be the mechanism whereby Trolox confers protection. This was confirmed by measuring protein oxidation (levels), and the observed decrease in proteasomal activity indicated that the decrease in protein carbonyls was due to Trolox scavenging activity rather than proteasome activation. In conclusion, the intracellular scavenging activity of Trolox is a key protective mechanism against H(2)O(2). These findings obtained in Schizosaccharomyces pombe, a good model organism for eukaryotic cells, can be used as standard protocols for investigating the antioxidant activity of pure or complex potential antioxidants.","doi":"10.4103/0976-9668.71667","authors":"Hamad I, Arda N, Pekmez M, Karaer S, Temizkan G","authors_abbrev":"Hamad I et al.","pubmed_publication_date":"Jul 2010","pubmed_entrez_date":"2011-11-19","publication_year":"2010","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11453250","title":"Functional analysis of RNA polymerase II Rpb3 mutants of the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 2001 Jun;39(4):210-21","abstract":"The RNA polymerase II (Pol II) of Schizosaccharomyces pombe is composed of 12 subunits. Subunit Rpb3 has sequence homology with the N-terminal domain of the prokaryotic alpha subunit, which plays a key role in RNA polymerase assembly. Together with the Rpb2 (the beta homologue) and Rpb11 (the second alpha homologue) subunits, Rpb3 constitutes a core subassembly (Rpb2-Rpb3-Rpb11) which corresponds to the the alpha2beta assembly intermediate of prokaryotic RNA polymerase. For the functional mapping of Rpb3, we made a collection of 12 heat-sensitive (Ts) or cold-sensitive (Cs) S. pombe mutants, each carrying a single mutation in one of the four conserved regions of Rpb3. The altered functions of six representative Pol II mutants containing the mutant Rpb3 were analyzed in vitro using an improved version of the GAL4-VP16 activator-dependent transcription system catalyzed by S. pombe cell extracts. The transcription activity by the extracts from Rpb3 mutants decreased to varying extents after heat treatment; but the extracts from Rpb3 mutants which had mutations in the eukaryote-specific conserved regions B and C regained their activity by the addition of GAL4-VP16, to a larger extent than those from the region A and D mutants. We propose that both terminal regions (A and D) play important roles in RNA polymerase assembly, while the central portion (regions B and C) is involved in activated transcription.","authors":"Mitobe J, Mitsuzawa H, Ishihama A","authors_abbrev":"Mitobe J et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-07-17","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1442.10c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:40741990","title":"Pedigree Painter (pepa): a tool for the visualization of genetic inheritance in chromosomal context.","citation":"Bioinformatics 2025 Aug 02;41(8)","abstract":"Data visualization is increasingly important in genomics, enabling researchers to uncover inheritance and recombination patterns across generations. While most existing tools focus on ancestry prediction, they lack functionality for analyzing known ancestries in controlled settings, such as determining parental contributions to offspring genomes. To address this gap, I developed pepa, a lightweight, deterministic, modular tool that visualizes and quantifies genomic inheritance, designed for beginner and advanced users.\npepa is a program for processing VCF files, assigning ancestries to homozygous SNPs, and clustering them into biologically meaningful regions. It generates human-readable comparison tables and visualizes inheritance patterns with chromosome paintings through R. Tested on fission yeast, pepa revealed non-uniform recombination patterns, with chromosomes largely inherited from one parent and seemingly random recombination. Quantitative analyses showed differences in parental contributions at the nucleotide and gene levels, with some offspring inheriting similar percentages from parents. However, the painted chromosomes revealed that even offspring with similar percentages from one parent rarely inherit the same genomic region, highlighting the importance of this tool in drawing biologically meaningful insights. pepa provides an accessible and powerful solution for analyzing genomic inheritance, bridging experimental and computational biology. Its modular design and minimal dependencies allow adaptation to diverse organisms, facilitating intuitive visualization and quantitative insights into recombination dynamics.","doi":"10.1093/bioinformatics/btaf428","authors":"Pozzi A","authors_abbrev":"Pozzi A","pubmed_publication_date":"02 Aug 2025","pubmed_entrez_date":"2025-07-31","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-07-31 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10091325","title":"Cloning and overexpression in Escherichia coli of the gene encoding dihydroxyacetone kinase isoenzyme I from Schizosaccharomyces pombe, and its application to dihydroxyacetone phosphate production.","citation":"Appl Microbiol Biotechnol 1999 Feb;51(2):193-200","abstract":"The gene dak1 encoding a dihydroxyacetone kinase (DHAK) isoenzyme I, one of two isoenzymes in the Schizosaccharomyces pombe IFO 0354 strain, was cloned and sequenced. The dak1 gene comprises 1743 bp and encodes a protein of 62,245 Da. The deduced amino acid sequence showed a similarity to a putative DHAK of Saccharomyces cerevisiae and DHAK of Citrobacter freundii. The dak1 gene was expressed at a high level in Escherichia coli, and the recombinant enzyme was purified to homogeneity and characterized. The acetone powder of recombinant E. coli cells was used to produce dihydroxyacetone phosphate.","authors":"Itoh N, Tujibata Y, Liu JQ","authors_abbrev":"Itoh N et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-03-26","publication_year":"1999","canto_session_key":"06c4d8895a9200b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-02-28 14:38:05","canto_approved_date":"2026-05-27 12:26:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-11 18:28:17","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-02-28"},{"uniquename":"PMID:22252817","title":"A genomewide screen in Schizosaccharomyces pombe for genes affecting the sensitivity of antifungal drugs that target ergosterol biosynthesis.","citation":"Antimicrob Agents Chemother 2012 Apr;56(4):1949-59","abstract":"We performed a genomewide screen for altered sensitivity to antifungal drugs, including clotrimazole and terbinafine, that target ergosterol biosynthesis using a Schizosaccharomyces pombe gene deletion library consisting of 3,004 nonessential haploid deletion mutants. We identified 109 mutants that were hypersensitive and 11 mutants that were resistant to these antifungals. Proteins whose absence rendered cells sensitive to these antifungals were classified into various functional categories, including ergosterol biosynthesis, membrane trafficking, histone acetylation and deacetylation, ubiquitination, signal transduction, ribosome biosynthesis and assembly, regulation of transcription and translation, cell wall organization and biogenesis, mitochondrion function, amino acid metabolism, nucleic acid metabolism, lipid metabolism, meiosis, and other functions. Also, proteins whose absence rendered cells resistant to these antifungals were classified into functional categories including mitochondrion function, ubiquitination, membrane trafficking, cell polarity, chromatin remodeling, and some unknown functions. Furthermore, the 109 sensitive mutants were tested for sensitivity to micafungin, another antifungal drug that inhibits (1,3)-β-D-glucan synthase, and 57 hypersensitive mutants were identified, suggesting that these mutants were defective in cell wall integrity. Altogether, our findings in fission yeast have shed light on molecular pathways associated with the cellular response to ergosterol biosynthesis inhibitors and may provide useful information for developing strategies aimed at sensitizing cells to these drugs.","doi":"10.1128/AAC.05126-11","authors":"Fang Y, Hu L, Zhou X, Jaiseng W, Zhang B, Takami T, Kuno T","authors_abbrev":"Fang Y et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-01-19","publication_year":"2012","canto_session_key":"0ba10364dffea95a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-24 13:28:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-24 13:28:05","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":457,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_22252817_phaf.tsv"}],"genes":["SPBC36.06c","SPAC30D11.05","SPBC359.06","SPBC21C3.20c","SPAC767.01c","SPBC27B12.10c","SPAC1556.02c","SPCC1235.15","SPCC1739.01","SPCC24B10.08c","SPAC1687.05","SPAC6F6.03c","SPBC2A9.11c","SPCC794.11c","SPAC6F6.01","SPAC22F8.03c","SPBC106.10","SPAC1786.01c","SPAC25B8.01","SPAC1D4.05c","SPBC691.03c","SPAC823.16c","SPBC31F10.09c","SPAC3A11.02","SPAC19A8.11c","SPBC21B10.13c","SPAC31A2.13c","SPAC17H9.19c","SPAC1527.02","SPBC15D4.15","SPBC19G7.16","SPBC947.04","SPBP23A10.05","SPBC713.08","SPBC2F12.11c","SPBC725.10","SPCC126.13c","SPAC4G8.08","SPCC794.03","SPCC1795.03","SPAC23C11.14","SPCC794.10","SPBC651.11c","SPAC4G8.10","SPCC162.10","SPBC16C6.03c","SPBC119.08","SPAC26A3.07c","SPAC869.11","SPAC3A12.17c","SPAC227.01c","SPBP16F5.07","SPCC622.14","SPCC1753.02c","SPAC1805.14","SPAC3H5.10","SPCC31H12.08c","SPAC1142.07c","SPAC110.02","SPBC25D12.06","SPAPB1E7.02c","SPAC23H3.06","SPCC63.02c","SPAC3A12.10","SPBC1861.05","SPBC660.05","SPBC25H2.16c","SPAC57A10.08c","SPBC1271.12","SPBC106.07c","SPCC736.09c","SPAC144.06","SPAC12G12.03","SPAC20G4.07c","SPAC30.02c","SPAC17H9.10c","SPAC13A11.04c","SPCC970.10c","SPAC4F10.04","SPBC215.04","SPBC3B8.03","SPAC19B12.08","SPBC1709.14","SPAC16.01","SPBC14F5.10c","SPAC23C11.08","SPBC27B12.08","SPAC9G1.12","SPAC688.11","SPBC365.14c","SPBC21D10.09c","SPAC1071.11","SPBC36.07","SPBC31F10.02","SPAC56E4.07","SPCC1223.01","SPAC1556.05c","SPAC644.14c","SPBC28F2.10c","SPCC757.09c","SPCC1442.05c","SPBC15D4.10c","SPCC1020.07","SPAC2G11.03c","SPAC11G7.02","SPAC15A10.11","SPCC297.05","SPAC23H3.13c","SPBC691.04","SPAC16C9.05","SPBC577.12","SPBC29A3.14c","SPCP1E11.04c","SPAC3H1.07","SPAC24H6.10c","SPAC15A10.03c","SPAC1F8.06","SPBP35G2.14","SPBC14C8.17c","SPCC338.08","SPBC32H8.07","SPBC146.09c"],"gene_count":122,"ltp_gene_count":0,"approved_date":"2014-07-24"},{"uniquename":"PMID:24256289","title":"Spatial control of mitotic commitment in fission yeast.","citation":"Biochem Soc Trans 2013 Dec;41(6):1766-71","abstract":"The activation of the Cdk1 (cyclin-dependent kinase 1)-cyclin B complex to promote commitment to mitosis is controlled by the phosphorylation status of the Cdk1 catalytic subunit. Cdk1 phosphorylation by Wee1 kinases blocks activation until Cdc25 (cell division cycle 25) phosphatases remove this phosphate to drive division. Feedback inhibition of Wee1 and promotion of Cdc25 activities by the newly activated Cdk1-cyclin B complexes ensure that the transition from interphase to mitosis is a rapid and complete bi-stable switch. Although this level of molecular understanding of the mitotic commitment switch has been clear for over two decades, it is still unclear how the switch is engaged to promote division at the right time for a particular context. We discuss recent work in fission yeast that shows how the spatial organization of signalling networks, in particular events on the centrosome equivalent, the spindle pole body, plays a key role in ensuring that the timing of cell division is coupled to environmental cues.","doi":"10.1042/BST20130190","authors":"Hagan IM, Grallert A","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9242669","title":"A novel protein, Psp1, essential for cell cycle progression of Schizosaccharomyces pombe is phosphorylated by Cdc2-Cdc13 upon entry into G0-like stationary phase of cell growth.","citation":"J Biol Chem 1997 Aug 08;272(32):19993-20002","abstract":"A novel gene, psp1(+), which functionally complements a temperature-sensitive mutant defective in cell cycle progression both in G1/S and G2/M has been isolated from the genomic and cDNA libraries of Schizosaccharomyces pombe. Disruption of this gene is lethal for cell growth at 30 degrees C indicating that it is an essential gene for vegetative cell growth. Western analysis of the protein by polyclonal antibody made from glutathione S-transferase-Psp1 fusion protein indicated that the Psp1 protein exists in two different molecular weight forms depending on the growth state of the cell. In vitro experiments with a phosphatase showed that this difference is due to phosphorylation. The dephosphorylated form of the protein is dominant in actively growing cells whereas the phosphorylated form becomes the major species when cells enter the stationary phase. The Cdc2-Cdc13 complex is shown to phosphorylate the GST-Psp1 fusion protein in vitro, and site-directed mutagenesis and phosphoamino acid analysis indicated that the serine residue at position 333 in the carboxyl-terminal region is required for phosphorylation. In situ fluorescein isothiocyanate-conjugated antibody staining showed that this protein tends to be localized to both ends of the cell upon entry into the stationary phase of cell growth. However, overexpression of the novel protein Psp1 in actively growing cells inhibits cell growth causing accumulation of DNA (4n or 8n). Thus we speculate that Psp1 can function at both G1/S and G2/M phases complementing the defect of the new mutant we have isolated. It is likely that Psp1 is required both for proper DNA replication and for the process of mitosis.","authors":"Jang YJ, Won M, Chung KS, Kim DU, Hoe KL, Park C, Yoo HS","authors_abbrev":"Jang YJ et al.","pubmed_publication_date":"08 Aug 1997","pubmed_entrez_date":"1997-08-08","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC646.13","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8557102","title":"Stress signal, mediated by a Hog1-like MAP kinase, controls sexual development in fission yeast.","citation":"FEBS Lett 1996 Jan 15;378(3):207-12","abstract":"We identified the phh1+ gene that encodes a MAP kinase as the effector of Wis1 MAP kinase kinase in fission yeast, which is highly homologous with HOG1 of S. cerevisiae. Heterothalic phh1 dsiruptant is phenotypically indistinguishable from wis1 deletion mutant, both displaying the same extent of partial sterility and enhanced sensitivity to a variety of stress. In phh1 disruptant, nitrogen starvation-induced expression of ste11+, a key controller of sexual differentiation, is markedly diminished. Ectopic expression of ste11+ effectively restores fertility, but not stress resistance, to the phh1 disruptant. These data show that stress signal, mediated by a MAP kinase, is required for efficient start of sexual differentiation.","authors":"Kato T, Okazaki K, Murakami H, Stettler S, Fantes PA, Okayama H","authors_abbrev":"Kato T et al.","pubmed_publication_date":"15 Jan 1996","pubmed_entrez_date":"1996-01-15","publication_year":"1996","canto_session_key":"a505689e6c78deee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-12 17:39:05","canto_approved_date":"2022-02-02 17:22:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-03 09:32:50","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC24H6.05","SPAC1D4.13","SPAC24B11.06c","SPBC32C12.02"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-12-12"},{"uniquename":"PMID:35205301","title":"Initiator-Directed Transcription: Fission Yeast Nmtl Initiator Directs Preinitiation Complex Formation and Transcriptional Initiation.","citation":"Genes (Basel) 2022 Jan 28;13(2)","abstract":"The initiator element is a core promoter element encompassing the transcription start site, which is found in yeast,  Drosophila , and human promoters. This element is observed in TATA-less promoters. Several studies have defined transcription factor requirements and additional cofactors that are needed for transcription initiation of initiator-containing promoters. However, those studies have been performed with additional core promoters in addition to the initiator. In this work, we have defined the pathway of preinitiation complex formation on the fission yeast nmt1 gene promoter, which contains a functional initiator with striking similarity to the initiator of the human dihydrofolate reductase (hDHFR) gene and to the factor requirement for transcription initiation of the nmt1 gene promoter. The results show that the nmt1 gene promoter possesses an initiator encompassing the transcription start site, and several conserved base positions are required for initiator function. A preinitiation complex formation on the nmt1 initiator can be started by TBP/TFIIA or TBP/TFIIB, but not TBP alone, and afterwards follows the same pathway as preinitiation complex formation on TATA-containing promoters. Transcription initiation is dependent on the general transcription factors TBP, TFIIB, TFIIE, TFIIF, TFIIH, RNA polymerase II, Mediator, and a cofactor identified as transcription cofactor for initiator function (TCIF), which is a high-molecular-weight protein complex of around 500 kDa. However, the TAF subunits of TFIID were not required for the nmt1 initiator transcription, as far as we tested. We also demonstrate that other initiators of the nmt1/hDHFR family can be transcribed in fission yeast whole-cell extracts.","doi":"10.3390/genes13020256","authors":"Rojas DA, Urbina F, Valenzuela-Pérez L, Leiva L, Miralles VJ, Maldonado E","authors_abbrev":"Rojas DA et al.","pubmed_publication_date":"28 Jan 2022","pubmed_entrez_date":"2022-02-25","publication_year":"2022","canto_session_key":"7146a12784aa25c4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-02-27 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3138659","title":"Codon usage patterns in Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melanogaster and Homo sapiens; a review of the considerable within-species diversity.","citation":"Nucleic Acids Res 1988 Sep 12;16(17):8207-11","abstract":"The genetic code is degenerate, but alternative synonymous codons are generally not used with equal frequency. Since the pioneering work of Grantham's group it has been apparent that genes from one species often share similarities in codon frequency; under the \"genome hypothesis\" there is a species-specific pattern to codon usage. However, it has become clear that in most species there are also considerable differences among genes. Multivariate analyses have revealed that in each species so far examined there is a single major trend in codon usage among genes, usually from highly biased to more nearly even usage of synonymous codons. Thus, to represent the codon usage pattern of an organism it is not sufficient to sum over all genes as this conceals the underlying heterogeneity. Rather, it is necessary to describe the trend among genes seen in that species. We illustrate these trends for six species where codon usage has been examined in detail, by presenting the pooled codon usage for the 10% of genes at either end of the major trend. Closely-related organisms have similar patterns of codon usage, and so the six species in Table 1 are representative of wider groups. For example, with respect to codon usage, Salmonella typhimurium closely resembles E. coli, while all mammalian species so far examined (principally mouse, rat and cow) largely resemble humans.","authors":"Sharp PM, Cowe E, Higgins DG, Shields DC, Wolfe KH, Wright F","authors_abbrev":"Sharp PM et al.","pubmed_publication_date":"12 Sep 1988","pubmed_entrez_date":"1988-09-12","publication_year":"1988","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12876765","title":"Localization of calmodulin in budding yeast and fission yeast using green fluorescent protein.","citation":"Methods Enzymol 1999;302:87-102","abstract":"","authors":"Flory MR, Davis TN","authors_abbrev":"Flory MR et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"2003-07-25","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2076550","title":"A mutated swi4 gene causes duplications in the mating-type region of Schizosaccharomyces pombe.","citation":"Curr Genet 1990 Dec;18(6):501-9","abstract":"Efficient mating-type (MT) switching in homothallic strains of Schizosaccharomyces pombe is significantly reduced if they have a mutation in any of the eleven known swi genes. The swi4 mutation causes heterothallic as well as homothallic segregants, both of which have duplications in the MT region. In contrast to homothallic strains, h+ swi4 strains yield only a few duplications. The duplications originate in the process of MT switching, presumably by mistakes in the resolution of DNA intermediates. They always consist of one cassette and one of the intervening sequences, L and K respectively. Strains with up to seven cassettes in the MT region were found. The possible modes of their origins are discussed.","authors":"Fleck O, Heim L, Gutz H","authors_abbrev":"Fleck O et al.","pubmed_publication_date":"Dec 1990","pubmed_entrez_date":"1990-12-01","publication_year":"1990","canto_session_key":"77cbd4768ce15b4e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-01 13:36:52","canto_approved_date":"2022-02-07 19:21:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-30 16:26:35","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8F11.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-01"},{"uniquename":"PMID:7893167","title":"Asparagine-linked glycosylation in Schizosaccharomyces pombe: functional conservation of the first step in oligosaccharide-lipid assembly.","citation":"Arch Biochem Biophys 1995 Mar 10;317(2):487-96","abstract":"The gene gpt encoding uridine diphosphate N-acetyl-D-glucosamine:dolichol phosphate N-acetylglucosaminylphosphoryltransferase (L-G1PT) was isolated by screening a Schizosaccharomyces pombe genomic DNA library in lambda phage under low-stringency hybridization using the Saccharomyces cerevisiae gene ALG7 as probe. Sequencing 2.4 kb of S. pombe DNA revealed a 1338-bp open reading frame (ORF) encoding a hydrophobic protein of 446 amino acids with a predicted molecular weight of 49,852. The S. pombe protein was 50% identical to the S. cerevisiae protein and 43% identical to the protein from Chinese hamster ovary (CHO) cells. Overexpression of the gpt gene in S. pombe cells increased resistance to tunicamycin 25-fold and increased the specific activity of the enzyme in isolated cell membranes 13-fold. This was accompanied by a 50-fold increase in poly(A)+ RNA hybridizing to the gpt probe. Northern analysis indicated a single 1.8-kb message is transcribed from the gpt gene. The gpt gene is essential for viability of S. pombe. Cells containing a disrupted ORF could be rescued by an expression plasmid containing either the intact S. pombe gpt ORF or the CHO L-G1PT cDNA. The S. pombe gpt gene was mapped to chromosome 2 near top1 and ade1.","authors":"Zou J, Scocca JR, Krag SS","authors_abbrev":"Zou J et al.","pubmed_publication_date":"10 Mar 1995","pubmed_entrez_date":"1995-03-10","publication_year":"1995","canto_session_key":"b2ba58a5b035015f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-06-12 12:54:24","canto_approved_date":"2024-06-30 20:03:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-14 09:27:38","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC15D4.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-06-12"},{"uniquename":"EMBL:AU008309","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39040524","title":"Arsenite treatment induces Hsp90 aggregatesdistinct from conventional stress granules in fission yeast.","citation":"Microb Cell 2024;11:242-253","abstract":"Various stress conditions, such as heat stress (HS) and oxidative stress, can cause biomolecular condensates represented by stress granules (SGs) via liquid-liquid phase separation. We have previously shown that Hsp90 forms aggregates in response to HS and that Hsp90 aggregates transiently co-localize with SGs as visualized by Pabp. Here, we showed that arsenite, one of the well-described SG-inducing stimuli, induces Hsp90 aggregates distinct from conventional SGs in fission yeast. Arsenite induced Hsp90 granules in a dose-dependent manner, and these granules were significantly diminished by the co-treatment with a ROS scavenger N-acetyl cysteine (NAC), indicating that ROS are required for the formation of Hsp90 granules upon arsenite stress. Notably, Hsp90 granules induced by arsenite do not overlap with conventional SGs as represented by eIF4G or Pabp, while HS-induced Hsp90 granules co-localize with SGs. Nrd1, an RNA-binding protein known as a HS-induced SG component, was recruited into Hsp90 aggregates but not to the conventional SGs upon arsenite stress. The non-phosphorylatable eIF2α mutants significantly delayed the Hsp90 granule formation upon arsenite treatment. Importantly, inhibition of Hsp90 by geldanamycin impaired the Hsp90 granule formation and reduced the arsenite tolerance. Collectively, arsenite stimulates two types of distinct aggregates, namely conventional SGs and a novel type of aggregates containing Hsp90 and Nrd1, wherein Hsp90 plays a role as a center for aggregation, and stress-specific compartmentalization of biomolecular condensates.","doi":"10.15698/mic2024.07.829","authors":"Tomimoto N, Takasaki T, Sugiura R","authors_abbrev":"Tomimoto N et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-07-23","publication_year":"2024","canto_session_key":"d80ab8ad5c96cd35","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-07-23 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30332655","title":"Paxillin-Mediated Recruitment of Calcineurin to the Contractile Ring Is Required for the Correct Progression of Cytokinesis in Fission Yeast.","citation":"Cell Rep 2018 Oct 16;25(3):772-783.e4","abstract":"Paxillin is a scaffold protein that participates in focal adhesion signaling in mammalian cells. Fission yeast paxillin ortholog, Pxl1, is required for contractile actomyosin ring (CAR) integrity and collaborates with the β-glucan synthase Bgs1 in septum formation. We show here that Pxl1's main function is to recruit calcineurin (CN) phosphatase to the actomyosin ring; and thus the absence of either Pxl1 or calcineurin causes similar cytokinesis defects. In turn, CN participates in the dephosphorylation of the Cdc15 F-BAR protein, which recruits and concentrates Pxl1 at the CAR. Our findings suggest the existence of a positive feedback loop between Pxl1 and CN and establish that Pxl1 is a crucial component of the CN signaling pathway during cytokinesis.","doi":"10.1016/j.celrep.2018.09.062","authors":"Martín-García R, Arribas V, Coll PM, Pinar M, Viana RA, Rincón SA, Correa-Bordes J, Ribas JC, Pérez P","authors_abbrev":"Martín-García R et al.","pubmed_publication_date":"16 Oct 2018","pubmed_entrez_date":"2018-10-18","publication_year":"2018","canto_session_key":"296b721850a6d19b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pilar Perez","canto_first_approved_date":"2019-03-06 16:36:34","canto_approved_date":"2025-04-21 18:56:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-06 09:53:51","canto_added_date":"2018-10-19 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":71,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pilar Perez","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.12","SPBC83.18c","SPAC20G8.05c","SPCC830.06","SPBC11C11.02","SPBC19G7.05c","SPBP4H10.04","SPCC1281.01","SPCC1840.02c","SPAC4G8.13c"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2019-03-06"},{"uniquename":"EMBL:AU006593","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19487457","title":"The S. pombe mitotic regulator Cut12 promotes spindle pole body activation and integration into the nuclear envelope.","citation":"J Cell Biol 2009 Jun 01;185(5):875-88","abstract":"The fission yeast spindle pole body (SPB) comprises a cytoplasmic structure that is separated from an ill-defined nuclear component by the nuclear envelope. Upon mitotic commitment, the nuclear envelope separating these domains disperses as the two SPBs integrate into a hole that forms in the nuclear envelope. The SPB component Cut12 is linked to cell cycle control, as dominant cut12.s11 mutations suppress the mitotic commitment defect of cdc25.22 cells and elevated Cdc25 levels suppress the monopolar spindle phenotype of cut12.1 loss of function mutations. We show that the cut12.1 monopolar phenotype arises from a failure to activate and integrate the new SPB into the nuclear envelope. The activation of the old SPB was frequently delayed, and its integration into the nuclear envelope was defective, resulting in leakage of the nucleoplasm into the cytoplasm through large gaps in the nuclear envelope. We propose that these activation/integration defects arise from a local deficiency in mitosis-promoting factor activation at the new SPB.","doi":"10.1083/jcb.200812108","authors":"Tallada VA, Tanaka K, Yanagida M, Hagan IM","authors_abbrev":"Tallada VA et al.","pubmed_publication_date":"01 Jun 2009","pubmed_entrez_date":"2009-06-03","publication_year":"2009","canto_session_key":"473f08550050fe95","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-07-07 11:57:49","canto_approved_date":"2026-01-31 15:31:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-24 14:29:24","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC649.05","SPAC24H6.05","SPAC1786.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-07-07"},{"uniquename":"PMID:27423862","title":"An IF-FISH Approach for Covisualization of Gene Loci and Nuclear Architecture in Fission Yeast.","citation":"Methods Enzymol 2016;574:167-180","abstract":"Recent genomic studies have revealed that chromosomal structures are formed by a hierarchy of organizing processes ranging from gene associations, including interactions among enhancers and promoters, to topologically associating domain formations. Gene associations identified by these studies can be characterized by microscopic analyses. Fission yeast is a model organism, in which gene associations have been broadly mapped across the genome, although many of those associations have not been further examined by cell biological approaches. To address the technically challenging process of the visualization of associating gene loci in the fission yeast nuclei, we provide, in detail, an IF-FISH procedure that allows for covisualizing both gene loci and nuclear structural markers such as the nuclear membrane and nucleolus.","doi":"10.1016/bs.mie.2016.04.003","authors":"Kim KD, Iwasaki O, Noma K","authors_abbrev":"Kim KD et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-07-18","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-07-19 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29411923","title":"Sac1, a lipid phosphatase at the interface of vesicular and nonvesicular transport.","citation":"Traffic 2018 May;19(5):301-318","abstract":"The lipid phosphatase Sac1 dephosphorylates phosphatidylinositol 4-phosphate (PI4P), thereby holding levels of this crucial membrane signaling molecule in check. Sac1 regulates multiple cellular processes, including cytoskeletal organization, membrane trafficking and cell signaling. Here, we review the structure and regulation of Sac1, its roles in cell signaling and development and its links to health and disease. Remarkably, many of the diverse roles attributed to Sac1 can be explained by the recent discovery of its requirement at membrane contact sites, where its consumption of PI4P is proposed to drive interorganelle transfer of other cellular lipids, thereby promoting normal lipid homeostasis within cells.","doi":"10.1111/tra.12554","authors":"Del Bel LM, Brill JA","authors_abbrev":"Del Bel LM et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-02-08","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30733343","title":"Twenty years of Mediator complex structural studies.","citation":"Biochem Soc Trans 2019 Feb 28;47(1):399-410","abstract":"Mediator is a large multiprotein complex conserved in all eukaryotes that plays an essential role in transcriptional regulation. Mediator comprises 25 subunits in yeast and 30 subunits in humans that form three main modules and a separable four-subunit kinase module. For nearly 20 years, because of its size and complexity, Mediator has posed a formidable challenge to structural biologists. The first two-dimensional electron microscopy (EM) projection map of Mediator leading to the canonical view of its division in three topological modules named Head, Middle and Tail, was published in 1999. Within the last few years, optimization of Mediator purification combined with technical and methodological advances in cryo-electron microscopy (cryo-EM) have revealed unprecedented details of Mediator subunit organization, interactions with RNA polymerase II and parts of its core structure at high resolution. To celebrate the twentieth anniversary of the first Mediator EM reconstruction, we look back on the structural studies of Mediator complex from a historical perspective and discuss them in the light of our current understanding of its role in transcriptional regulation.","doi":"10.1042/BST20180608","authors":"Verger A, Monté D, Villeret V","authors_abbrev":"Verger A et al.","pubmed_publication_date":"28 Feb 2019","pubmed_entrez_date":"2019-02-09","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1417859","title":"The synthesis of cadystins, heavy metal chelating peptides, is induced in the fission yeast by wounds of the cell wall or by incubation with chitosan.","citation":"Biochem Biophys Res Commun 1992 Oct 15;188(1):388-94","abstract":"It has been shown that heavy metal administration induced the synthesis of cadystins, the small metal chelating peptide with the general structure of (gamma-glu-cys)n-gly, in the fission yeast and in plants. Besides heavy metals, wounds to the cell surface or the incubation with chitosan induced the cadystin synthesis in the fission yeast. Under these induction conditions, the membrane permeability of the fission yeast significantly increased suggesting the structural alteration of the membrane. In these induction, the synthesized cadystins formed complexes with the cellular zinc ions together with or without glutathione.","authors":"Hayashi Y, Morikawa S, Kawabata M, Hotta Y","authors_abbrev":"Hayashi Y et al.","pubmed_publication_date":"15 Oct 1992","pubmed_entrez_date":"1992-10-15","publication_year":"1992","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33572424","title":"Label-Free Quantitative Phosphoproteomics of the Fission Yeast  Schizosaccharomyces pombe  Using Strong Anion Exchange- and Porous Graphitic Carbon-Based Fractionation Strategies.","citation":"Int J Mol Sci 2021 Feb 09;22(4)","abstract":"The phosphorylation of proteins modulates various functions of proteins and plays an important role in the regulation of cell signaling. In recent years, label-free quantitative (LFQ) phosphoproteomics has become a powerful tool to analyze the phosphorylation of proteins within complex samples. Despite the great progress, the studies of protein phosphorylation are still limited in throughput, robustness, and reproducibility, hampering analyses that involve multiple perturbations, such as those needed to follow the dynamics of phosphoproteomes. To address these challenges, we introduce here the LFQ phosphoproteomics workflow that is based on Fe-IMAC phosphopeptide enrichment followed by strong anion exchange (SAX) and porous graphitic carbon (PGC) fractionation strategies. We applied this workflow to analyze the whole-cell phosphoproteome of the fission yeast  Schizosaccharomyces pombe . Using this strategy, we identified 8353 phosphosites from which 1274 were newly identified. This provides a significant addition to the  S. pombe  phosphoproteome. The results of our study highlight that combining of PGC and SAX fractionation strategies substantially increases the robustness and specificity of LFQ phosphoproteomics. Overall, the presented LFQ phosphoproteomics workflow opens the door for studies that would get better insight into the complexity of the protein kinase functions of the fission yeast  S. pombe .","doi":"10.3390/ijms22041747","authors":"Sivakova B, Jurcik J, Lukacova V, Selicky T, Cipakova I, Barath P, Cipak L","authors_abbrev":"Sivakova B et al.","pubmed_publication_date":"09 Feb 2021","pubmed_entrez_date":"2021-02-12","publication_year":"2021","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-02-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10649286","title":"Ultradian clocks in eukaryotic microbes: from behavioural observation to functional genomics.","citation":"Bioessays 2000 Jan;22(1):16-22","abstract":"Period homeostasis is the defining characteristic of a biological clock. Strict period homeostasis is found for the ultradian clocks of eukaryotic microbes. In addition to being temperature-compensated, the period of these rhythms is unaffected by differences in nutrient composition or changes in other environmental variables. The best-studied examples of ultradian clocks are those of the ciliates Paramecium tetraurelia and Tetrahymena sp. and of the fission yeast, Schizosaccharomyces pombe. In these single cell eukaryotes, up to seven different parameters display ultradian rhythmicity with the same, species- and strain-specific period. In fission yeast, the molecular genetic analysis of ultradian clock mechanisms has begun with the systematic analysis of mutants in identified candidate genes. More than 40 \"clock mutants\" have already been identified, most of them affected in components of major regulatory and signalling pathways. These results indicate a high degree of complexity for a eukaryotic clock mechanism. BioEssays 22:16-22, 2000.","authors":"Kippert F, Hunt P","authors_abbrev":"Kippert F et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-29","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27684088","title":"Ordering Single Cells and Single Embryos in 3D Confinement: A New Device for High Content Screening.","citation":"J Vis Exp 2016 Sep 18;(115)","abstract":"Biological cells are usually observed on flat (2D) surfaces. This condition is not physiological, and phenotypes and shapes are highly variable. Screening based on cells in such environments have therefore serious limitations: cell organelles show extreme phenotypes, cell morphologies and sizes are heterogeneous and/or specific cell organelles cannot be properly visualized. In addition, cells in vivo are located in a 3D environment; in this situation, cells show different phenotypes mainly because of their interaction with the surrounding extracellular matrix of the tissue. In order to standardize and generate order of single cells in a physiologically-relevant 3D environment for cell-based assays, we report here the microfabrication and applications of a device for in vitro 3D cell culture. This device consists of a 2D array of microcavities (typically 10(5) cavities/cm(2)), each filled with single cells or embryos. Cell position, shape, polarity and internal cell organization become then normalized showing a 3D architecture. We used replica molding to pattern an array of microcavities, 'eggcups', onto a thin polydimethylsiloxane (PDMS) layer adhered on a coverslip. Cavities were covered with fibronectin to facilitate adhesion. Cells were inserted by centrifugation. Filling percentage was optimized for each system allowing up to 80%. Cells and embryos viability was confirmed. We applied this methodology for the visualization of cellular organelles, such as nucleus and Golgi apparatus, and to study active processes, such as the closure of the cytokinetic ring during cell mitosis. This device allowed the identification of new features, such as periodic accumulations and inhomogeneities of myosin and actin during the cytokinetic ring closure and compacted phenotypes for Golgi and nucleus alignment. We characterized the method for mammalian cells, fission yeast, budding yeast, C. elegans with specific adaptation in each case. Finally, the characteristics of this device make it particularly interesting for drug screening assays and personalized medicine.","doi":"10.3791/51880","authors":"Wollrab V, Caballero D, Thiagarajan R, Riveline D","authors_abbrev":"Wollrab V et al.","pubmed_publication_date":"18 Sep 2016","pubmed_entrez_date":"2016-09-30","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-10-01 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19132115","title":"The fission yeast model for the lysosomal storage disorder Batten disease predicts disease severity caused by mutations in CLN3.","citation":"Dis Model Mech 2009;2(1-2):84-92","abstract":"The function of the CLN3 protein, which is mutated in patients with the neurodegenerative lysosomal storage disorder Batten disease, has remained elusive since it was identified 13 years ago. Here, we exploited the Schizosaccharomyces pombe model to gain new insights into CLN3 function. We modelled all missense mutations of CLN3 in the orthologous protein Btn1p, as well as a series of targeted mutations, and assessed trafficking and the ability of the mutant proteins to rescue four distinct phenotypes of btn1Delta cells. Mutating the C-terminal cysteine residues of Btn1p caused it to be internalised into the vacuole, providing further evidence that this protein functions from pre-vacuole compartments. Mutations in the lumenal regions of the multi-spanning membrane protein, especially in the third lumenal domain which contains a predicted amphipathic helix, had the most significant impact on Btn1p function, indicating that these domains of CLN3 are functionally important. Only one mutant protein was able to rescue the cell curving phenotype (p.Glu295Lys), and since this mutation is associated with a very protracted disease progression, this phenotype could be used to predict the disease severity of novel mutations in CLN3. The ability to predict disease phenotypes in S. pombe confirms this yeast as an invaluable tool to understanding Batten disease.","doi":"10.1242/dmm.000851","authors":"Haines RL, Codlin S, Mole SE","authors_abbrev":"Haines RL et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-01-10","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17069919","title":"Phenotypes and fed-batch fermentation of ubiquinone-overproducing fission yeast using ppt1 gene.","citation":"J Biotechnol 2007 Jan 30;128(1):120-31","abstract":"Ubiquinone (UQ), a component of the electron transfer system in many organisms, has been widely used for pharmaceuticals and cosmetics. In this study, we cloned and overexpressed the full-length ppt1 (MTppt1) gene, which encodes p-hydroxybenzoate:polyprenyltransferase and ERppt1 gene, which was modified to be localized on endoplasmic reticulum in fission yeast. The yeast MTppt1 and ERppt1 transgenic lines showed about 3.7 and 5.1 times increment in UQ content and the recombinant yeasts with a higher UQ level are more resistant to H(2)O(2), Cu(2+) and NaCl, and interestingly their growth was also faster than the wild type at lower temperature. For large-scale cultivation, the direct feedback control of glucose using an on-line ethanol concentration monitor for ubiquinone production of yeast ERppt1 by high-cell-density fermentation was investigated and the fermentation parameters (e.g., dissolved oxygen, pH, ethanol concentration, oxygen uptake rate, carbon dioxide evolution rate and respiration quotient) were also discussed. After 90 h cultures, the yeast dry cell weight reached 57 gl(-1) and the ubiquinone yield reached 23 mgl(-1). In addition, plasmid stability was maintained at high level throughout the fermentation.","authors":"Zhang D, Shrestha B, Niu W, Tian P, Tan T","authors_abbrev":"Zhang D et al.","pubmed_publication_date":"30 Jan 2007","pubmed_entrez_date":"2006-10-31","publication_year":"2007","canto_session_key":"f582522c2ba539f5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-02 19:07:44","canto_approved_date":"2024-09-08 11:31:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-02 19:07:37","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC56F8.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-07-02"},{"uniquename":"PMID:10429181","title":"The metaphase to anaphase transition: a case of productive destruction.","citation":"Eur J Biochem 1999 Jul;263(1):14-9","abstract":"The metaphase to anaphase transition is a point of no return; the duplicated sister chromatids segregate to the future daughter cells, and any mistake in this process may be deleterious to both progeny. At the heart of this process lies the anaphase inhibitor, which must be degraded in order for this transition to take place. The degradation of the anaphase inhibitor occurs via the ubiquitin-degradation pathway, and it involves the activity of the cyclosome/anaphase promoting complex (APC). The fidelity of the metaphase to anaphase transition is ensured by several different regulatory mechanisms that modulate the activity of the cyclosome/APC. Great advancements have been made in this field in the past few years, but many questions still remain to be answered.","authors":"Farr KA, Cohen-Fix O","authors_abbrev":"Farr KA et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-08-03","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26037463","title":"Functional expression of a heterologous nickel-dependent, ATP-independent urease in Saccharomyces cerevisiae.","citation":"Metab Eng 2015 Jul;30:130-140","abstract":"In microbial processes for production of proteins, biomass and nitrogen-containing commodity chemicals, ATP requirements for nitrogen assimilation affect product yields on the energy producing substrate. In Saccharomyces cerevisiae, a current host for heterologous protein production and potential platform for production of nitrogen-containing chemicals, uptake and assimilation of ammonium requires 1 ATP per incorporated NH3. Urea assimilation by this yeast is more energy efficient but still requires 0.5 ATP per NH3 produced. To decrease ATP costs for nitrogen assimilation, the S. cerevisiae gene encoding ATP-dependent urease (DUR1,2) was replaced by a Schizosaccharomyces pombe gene encoding ATP-independent urease (ure2), along with its accessory genes ureD, ureF and ureG. Since S. pombe ure2 is a Ni(2+)-dependent enzyme and Saccharomyces cerevisiae does not express native Ni(2+)-dependent enzymes, the S. pombe high-affinity nickel-transporter gene (nic1) was also expressed. Expression of the S. pombe genes into dur1,2Δ S. cerevisiae yielded an in vitro ATP-independent urease activity of 0.44±0.01 µmol min(-1) mg protein(-1) and restored growth on urea as sole nitrogen source. Functional expression of the Nic1 transporter was essential for growth on urea at low Ni(2+) concentrations. The maximum specific growth rates of the engineered strain on urea and ammonium were lower than those of a DUR1,2 reference strain. In glucose-limited chemostat cultures with urea as nitrogen source, the engineered strain exhibited an increased release of ammonia and reduced nitrogen content of the biomass. Our results indicate a new strategy for improving yeast-based production of nitrogen-containing chemicals and demonstrate that Ni(2+)-dependent enzymes can be functionally expressed in S. cerevisiae.","doi":"10.1016/j.ymben.2015.05.003","authors":"Milne N, Luttik MAH, Cueto Rojas HF, Wahl A, van Maris AJA, Pronk JT, Daran JM","authors_abbrev":"Milne N et al.","pubmed_publication_date":"Jul 2015","pubmed_entrez_date":"2015-06-04","publication_year":"2015","canto_session_key":"96e686a671a5b58a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-10-26 12:58:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-21 19:41:18","canto_added_date":"2015-06-05 00:19:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3A12.09c","SPAC29A4.13","SPAC1952.11c","SPCPB16A4.05c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-10-21"},{"uniquename":"PMID:21900489","title":"The filament-forming protein Pil1 assembles linear eisosomes in fission yeast.","citation":"Mol Biol Cell 2011 Nov;22(21):4059-67","abstract":"The cortical cytoskeleton mediates a range of cellular activities such as endocytosis, cell motility, and the maintenance of cell rigidity. Traditional polymers, including actin, microtubules, and septins, contribute to the cortical cytoskeleton, but additional filament systems may also exist. In yeast cells, cortical structures called eisosomes generate specialized domains termed MCCs to cluster specific proteins at sites of membrane invaginations. Here we show that the core eisosome protein Pil1 forms linear cortical filaments in fission yeast cells and that purified Pil1 assembles into filaments in vitro. In cells, Pil1 cortical filaments are excluded from regions of cell growth and are independent of the actin and microtubule cytoskeletons. Pil1 filaments assemble slowly at the cell cortex and appear stable by time-lapse microscopy and fluorescence recovery after photobleaching. This stability does not require the cell wall, but Pil1 and the transmembrane protein Fhn1 colocalize and are interdependent for localization to cortical filaments. Increased Pil1 expression leads to cytoplasmic Pil1 rods that are stable and span the length of cylindrical fission yeast cells. We propose that Pil1 is a novel component of the yeast cytoskeleton, with implications for the role of filament assembly in the spatial organization of cells.","doi":"10.1091/mbc.E11-07-0605","authors":"Kabeche R, Baldissard S, Hammond J, Howard L, Moseley JB","authors_abbrev":"Kabeche R et al.","pubmed_publication_date":"Nov 2011","pubmed_entrez_date":"2011-09-09","publication_year":"2011","canto_session_key":"d6adc62efa09cfdc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"James Moseley","canto_approved_date":"2012-10-22 07:45:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-10-19 13:59:51","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"James Moseley","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.13","SPAC3C7.02c","SPCC736.15","SPAC15A10.09c","SPAC637.13c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2012-10-19"},{"uniquename":"EMBL:AU014161","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29259000","title":"Genes Important for  Schizosaccharomyces pombe  Meiosis Identified Through a Functional Genomics Screen.","citation":"Genetics 2018 Feb;208(2):589-603","abstract":"Meiosis is a specialized cell division that generates gametes, such as eggs and sperm. Errors in meiosis result in miscarriages and are the leading cause of birth defects; however, the molecular origins of these defects remain unknown. Studies in model organisms are beginning to identify the genes and pathways important for meiosis, but the parts list is still poorly defined. Here we present a comprehensive catalog of genes important for meiosis in the fission yeast,  Schizosaccharomyces pombe  Our genome-wide functional screen surveyed all nonessential genes for roles in chromosome segregation and spore formation. Novel genes important at distinct stages of the meiotic chromosome segregation and differentiation program were identified. Preliminary characterization implicated three of these genes in centrosome/spindle pole body, centromere, and cohesion function. Our findings represent a near-complete parts list of genes important for meiosis in fission yeast, providing a valuable resource to advance our molecular understanding of meiosis.","doi":"10.1534/genetics.117.300527","authors":"Blyth J, Makrantoni V, Barton RE, Spanos C, Rappsilber J, Marston AL","authors_abbrev":"Blyth J et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2017-12-21","publication_year":"2018","canto_session_key":"b31214a9635efb8b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Julie Blyth","canto_first_approved_date":"2018-01-18 16:25:19","canto_approved_date":"2025-12-12 18:56:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-18 16:25:12","canto_added_date":"2017-12-22 01:15:16","annotation_curators":[{"name":"Julie Blyth","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":659,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_29259000_phaf.tsv"}],"genes":["SPBC31F10.05","SPBC1703.08c","SPAC17H9.11","SPAC2C4.08","SPAC26F1.09","SPAC513.06c","SPCC1235.15","SPAC644.08","SPCC1223.12c","SPAC57A7.08","SPAC12G12.13c","SPBC23G7.16","SPAP11E10.02c","SPBC119.12","SPBC660.11","SPBC106.04","SPBC215.04","SPAC664.01c","SPAC1002.15c","SPAC1805.04","SPAC589.11","SPBP4H10.12","SPAC20G8.10c","SPAC25G10.04c","SPAC5D6.02c","SPAC14C4.10c","SPBC651.10","SPAC17A5.08","SPBC16E9.15","SPCC1183.12","SPAC2C4.05","SPAC683.03","SPCC584.13","SPCC663.03","SPAC1D4.11c","SPAC16E8.01","SPAC30.03c","SPBC27B12.10c","SPAC8E11.07c","SPBC30D10.04","SPCC794.10","SPBC18E5.14c","SPAC1782.05","SPAC3G6.13c","SPAC57A10.06","SPAPB1A11.03","SPAC630.13c","SPBC577.02","SPCC895.05","SPAC27D7.14c","SPBC19G7.04","SPAPB8E5.02c","SPBC1105.04c","SPAC23C4.02","SPAC23C11.10","SPAC1486.01","SPAC3C7.12","SPBC2G2.05","SPAC4G9.06c","SPAC25B8.10","SPCC594.06c","SPBC2D10.17","SPBC13E7.07","SPAC16A10.03c","SPAC1142.03c","SPAC1F5.09c","SPAC1D4.06c","SPCC1795.06","SPAC9G1.10c","SPAC688.13","SPCC757.12","SPAC3H1.05","SPCC1682.16","SPBC23E6.05","SPAC4D7.07c","SPAC1851.02","SPBC21C3.18","SPAC14C4.08","SPAC4C5.01","SPBC19F8.08","SPAC11G7.04","SPAC4A8.06c","SPCC364.01","SPAC630.15","SPBPB2B2.13","SPCC553.01c","SPAC3A12.13c","SPAC23A1.04c","SPBC26H8.03","SPAPB17E12.04c","SPCC613.06","SPBC1921.07c","SPAC890.07c","SPAC6G10.11c","SPAC630.09c","SPBC32F12.12c","SPAC24B11.08c","SPBC12D12.06","SPAC8F11.02c","SPACUNK4.16c","SPAC24C9.14","SPAC1250.03","SPCC1672.06c","SPBC29A3.03c","SPAC664.15","SPBC28E12.06c","SPAC26F1.08c","SPAC26A3.16","SPAC24H6.10c","SPBC3B8.02","SPBC18E5.13","SPAC4D7.03","SPBC28F2.10c","SPBC2D10.16","SPBC29A10.14","SPBC25H2.15","SPAC31G5.11","SPAC23C4.16c","SPAC869.11","SPAC4G9.12","SPAC19B12.07c","SPBC29B5.03c","SPAC1F8.01","SPBC11C11.07","SPAC22H10.13","SPAC15E1.06","SPCC965.05c","SPAC3H8.03","SPBC83.19c","SPCC417.07c","SPAC688.11","SPAC24C9.08","SPAC22F3.10c","SPAC1002.14","SPBC713.08","SPAC4H3.06","SPAC29A4.17c","SPAC607.10","SPBC2A9.13","SPAC22H10.04","SPCC4G3.13c","SPBC32F12.08c","SPAC1F7.11c","SPAC6F6.09","SPCP20C8.01c","SPBC56F2.11","SPCC1235.03","SPAC139.01c","SPAC1296.04","SPAC3A12.06c","SPBC1709.05","SPAC3A12.08","SPAC977.11","SPAC3C7.14c","SPCC31H12.03c","SPAP7G5.03","SPBC29A3.07c","SPAC22F3.07c","SPAC1296.03c","SPAC22E12.05c","SPCC16C4.20c","SPAC1565.01","SPBP8B7.13","SPBC1921.01c","SPAC22A12.14c","SPBC29A3.13","SPAC23C11.15","SPBC215.06c","SPBC18E5.01","SPAC458.05","SPAC4G9.20c","SPAC57A7.15c","SPCC1753.05","SPBC1347.02","SPAC26A3.07c","SPAC20G8.07c","SPBC25B2.02c","SPAC227.14","SPAC30.02c","SPAC15E1.09","SPAC31G5.07","SPAC13G7.11","SPAC2F7.03c","SPBC29A10.10c","SPAC1952.15c","SPBC16A3.07c","SPAC3C7.06c","SPCC18.06c","SPAC227.05","SPCC63.02c","SPAC1F7.10","SPBC17G9.08c","SPCC1235.14","SPAC20G4.02c","SPAC24B11.12c","SPAC9E9.11","SPBC29A10.09c","SPAC17A5.05c","SPCC553.08c","SPAC22E12.14c","SPAC22G7.01c","SPAC19D5.06c","SPBC14C8.11c","SPBC649.03","SPAC1783.05","SPAC1002.20","SPAC29B12.13","SPAC25B8.17","SPBC56F2.14","SPAC27D7.03c","SPAC12B10.14c","SPBC11C11.09c","SPAC22E12.18","SPAC22A12.07c","SPBP35G2.07","SPAC959.08","SPCC1393.10","SPAC29A4.14c","SPAC4D7.11","SPCC736.15","SPAC19D5.11c","SPBC23G7.15c","SPBC18H10.04c","SPBC365.03c","SPAC1486.04c","SPAC23C4.11","SPBC1539.06","SPAC2F3.18c","SPAC22A12.03c","SPAC10F6.08c","SPBC1778.05c","SPAC1805.07c","SPBC11B10.05c","SPAC23E2.01","SPAC8C9.04","SPBC651.12c","SPBC106.01","SPBC30B4.02c","SPAPB17E12.02","SPAC6G10.12c","SPAC27D7.02c","SPAC2C4.09","SPAC23H4.10c","SPBC31F10.14c","SPCC584.03c","SPAC17A5.18c","SPAC144.04c","SPBC1271.07c","SPAC23H3.03c","SPBC16C6.05","SPAC3G9.04","SPAC767.01c","SPBC1289.06c","SPBC18H10.15","SPBC106.17c","SPCC1442.04c","SPAC343.20","SPCC4B3.08","SPAC105.03c","SPBC342.04","SPAC227.03c","SPCC18B5.03","SPBC11B10.10c","SPAC31F12.01","SPBC4B4.07c","SPBP18G5.03","SPBC2D10.20","SPBC3H7.09","SPAC6G9.04","SPCC794.09c","SPBC3D6.08c","SPBC23G7.14","SPCC338.16","SPAC1002.06c","SPCC825.01","SPBC106.05c","SPAC8E11.01c","SPAC26A3.01","SPBC29A3.21","SPAC56F8.02","SPAC823.17","SPBC4F6.06","SPAC24C9.16c","SPBP16F5.05c","SPAC3F10.13","SPBC16C6.02c","SPBC2F12.11c","SPBC16D10.06","SPCC550.11","SPBC4C3.04c","SPAC17A5.11","SPAC1556.05c","SPAC19A8.10","SPCC1322.03","SPCC191.06","SPBC19G7.02","SPAC664.02c","SPCC1020.11c","SPCC830.10","SPCC31H12.08c","SPAC23G3.08c","SPCC16C4.10","SPBC2G5.06c","SPBC28F2.02","SPAC30D11.01c","SPBC1861.03","SPCC1450.02","SPCC11E10.06c","SPBC21C3.11","SPAC3F10.17","SPAC57A10.12c","SPAC821.07c","SPBC19C2.02","SPBC3B8.04c","SPBC24C6.05","SPBC428.04","SPCC18.01c","SPAC1851.03","SPAC18G6.15","SPCC364.03","SPAC17C9.14","SPBC1711.08","SPBC1685.13","SPBC83.04","SPCC1682.15","SPAC1039.09","SPCC736.08","SPBC1D7.04","SPAC17A2.09c","SPCC70.03c","SPAC1B1.02c","SPBC713.09","SPBC1604.20c","SPCC4B3.02c","SPAC227.10","SPBC354.04","SPAC664.10","SPAC1786.04","SPBC354.13","SPAC18B11.08c","SPCC645.07","SPA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of interactions among the Cef1p-Prp19p-associated splicing complex.","citation":"RNA 2002 Jun;8(6):798-815","abstract":"Schizosaccharomyces pombe (Sp) Cdc5p and its Saccharomyces cerevisiae (Sc) ortholog, Cef1p, are essential components of the spliceosome. In S. cerevisiae, a subcomplex of the spliceosome that includes Cef1p can be isolated on its own; this has been termed the nineteen complex (Ntc) because it contains Prp19p. Components of the Ntc include Cef1p, Snt309p, Syf2p/Ntc31p, Ntc30p/lsy1p, Ntc20p and at least six unidentified proteins. We recently identified approximately 30 proteins that copurified with Cdc5p and Cef1p. Previously unidentified S. pombe proteins in this purification were called Cwfs for complexed with five and novel S. cerevisiae proteins were called Cwcs for complexed with Cef1p. Using these proteomics data coupled with available information regarding Ntc composition, we have investigated protein identities and interactions among Ntc components. Our data indicate that Cwc2p, Prp46p, Clf1p, and Syf1p most likely represent Ntc40p, Ntc50p, Ntc77p, and Ntc90p, respectively. We show that Sc Cwc2p interacts with Prp19p and is involved in pre-mRNA splicing. Sp cwf2+, the homolog of Sc CWC2, is allelic with the previously identified Sp prp3+. We present evidence that Sp Cwf7p, an essential protein with obvious homologs in many eukaryotes but not S. cerevisiae, is a functional counterpart of Sc Snt309p and binds Sp Cwf8p (a homolog of Sc Prp19p). Further, our data indicate that a mutation in the U-box of Prp19p disrupts these numerous protein interactions causing Cef1p degradation and Ntc instability.","authors":"Ohi MD, Gould KL","authors_abbrev":"Ohi MD et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-06-29","publication_year":"2002","canto_session_key":"d0b13d10196c5101","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2025-03-31 06:32:37","canto_approved_date":"2025-03-31 15:14:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-31 06:32:31","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC31F10.11c","SPCC550.02c","SPBC211.02c","SPAC3A12.11c","SPBC28F2.04c","SPBP22H7.07","SPAC29A4.08c","SPAC644.12"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2025-03-31"},{"uniquename":"EMBL:AU010612","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20801936","title":"Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes.","citation":"Genes Dev 2010 Sep 15;24(18):2019-30","abstract":"We reported previously that the stability of all mammalian phosphatidylinositol 3-kinase-related protein kinases (PIKKs) depends on their interaction with Tel2, the ortholog of yeast Tel2 and Caenorhabditis elegans Clk-2. Here we provide evidence that Tel2 acts with Hsp90 in the maturation of PIKK complexes. Quantitative immunoblotting showed that the abundance of Tel2 is low compared with the PIKKs, and Tel2 preferentially bound newly synthesized ATM, ATR, mTOR, and DNA-PKcs. Tel2 complexes contained, in addition to Tti1-Tti2, the Hsp90 chaperone, and inhibition of Hsp90 interfered with the interaction of Tel2 with the PIKKs. Analysis of in vivo labeled nascent protein complexes showed that Tel2 and Hsp90 mediate the formation of the mTOR TORC1 and TORC2 complexes and the association of ATR with ATRIP. The structure of yeast Tel2, reported here, shows that Tel2 consists of HEAT-like helical repeats that assemble into two separate α-solenoids. Through mutagenesis, we identify a surface patch of conserved residues involved in binding to the Tti1-Tti2 complex in vitro. In vivo, mutation of this conserved patch affects cell growth, levels of PIKKs, and ATM/ATR-mediated checkpoint signaling, highlighting the importance of Tti1-Tti2 binding to the function of Tel2. Taken together, our data suggest that the Tel2-Tti1-Tti2 complex is a PIKK-specific cochaperone for Hsp90.","doi":"10.1101/gad.1956410","authors":"Takai H, Xie Y, de Lange T, Pavletich NP","authors_abbrev":"Takai H et al.","pubmed_publication_date":"15 Sep 2010","pubmed_entrez_date":"2010-08-31","publication_year":"2010","canto_session_key":"1aeb3dcae9f7b9db","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2016-09-30 11:10:39","canto_approved_date":"2023-09-08 12:21:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-09-06 04:45:22","canto_added_date":"2016-09-21 00:19:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC458.03","SPBC1604.17c","SPCC622.13c"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2016-09-30"},{"uniquename":"PMID:10050047","title":"Disruption of the YRB2 gene retards nuclear protein export, causing a profound mitotic delay, and can be rescued by overexpression of XPO1/CRM1.","citation":"J Biochem 1999 Mar;125(3):574-85","abstract":"Disruption of the YRB2 gene encoding a nuclear Ran-binding protein homologous to Yrb1p/RanBP1 makes Saccharomyces cerevisiae cold sensitive for colony-formation, but not for growth in liquid medium. Schizosaccharomyces pombe Hba1p, which is homologous to Saccharomyces cerevisiae Yrb2p, rescued the cold sensitivity of Deltayrb2 cells. When released from an alpha factor block, Deltayrb2 cells underwent a prolonged delay at the short spindle stage of mitosis with a normal level of Clb/p34(CDC28) kinase activity, but there was no chromosome loss, this being consistent with the finding that Deltayrb2 was synthetic lethal with neither Deltamad1 nor Deltamad3. The cold sensitive colony-formation of Deltayrb2 cells was rescued by both XPO1/CRM1 and GSP1, but not CDC5, carried on a multicopy vector. XPO1/CRM1 rescued Deltayrb2 even in a single copy. Consistent with such a tight functional interaction, Xpo1p/Crm1p directly bound to Yrb2p, but not Yrb1p, and Deltayrb2 cells were found to have a defect in nuclear export signal (NES)-dependent nuclear protein export. From these results together, the ability of Xpo1/Crm1p to export NES-proteins is suggested to be enhanced by both Yrb2p and Gsp1p, and thereby disruption of YRB2 retards nuclear protein export, resulting in the mitotic delay.","authors":"Noguchi E, Saitoh Yh, Sazer S, Nishimoto T","authors_abbrev":"Noguchi E et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-03-02","publication_year":"1999","canto_session_key":"90a92a5cefa38275","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 17:23:01","canto_session_submitted_date":"2012-03-03 17:22:43","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC365.13c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:15157888","title":"In vivo labeling of fission yeast DNA with thymidine and thymidine analogs.","citation":"Methods 2004 Jul;33(3):213-9","abstract":"In vivo labeling of DNA with thymidine and thymidine analogs has long been a cornerstone of replication studies. Unfortunately, yeast lack a thymidine salvage pathway and thus do not incorporate exogenous thymidine. Specifically, yeast neither efficiently take up exogenous thymidine from their growth media nor phosphorylate it to thymidylate, the precursor of dTTP. We have overcome these problems in fission yeast by expressing the human equilibrative nucleoside transporter 1 (hENT1) along with herpes simplex virus thymidine kinase (tk). hENT1 tk cells are healthy and efficiently incorporate exogenous thymidine and thymidine analogs. We present protocols for labeling DNA with tritiated thymidine, for in situ detection of incorporated BrdU by immunofluorescence, for double labeling with CldU and IdU, for CsCl gradient separation of IdU-labeled DNA, and for using hENT1 and tk as both positive and negative selection markers.","authors":"Sivakumar S, Porter-Goff M, Patel PK, Benoit K, Rhind N","authors_abbrev":"Sivakumar S et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18684335","title":"Yeast cell factories for fine chemical and API production.","citation":"Microb Cell Fact 2008 Aug 07;7:25","abstract":"This review gives an overview of different yeast strains and enzyme classes involved in yeast whole-cell biotransformations. A focus was put on the synthesis of compounds for fine chemical and API (= active pharmaceutical ingredient) production employing single or only few-step enzymatic reactions. Accounting for recent success stories in metabolic engineering, the construction and use of synthetic pathways was also highlighted. Examples from academia and industry and advances in the field of designed yeast strain construction demonstrate the broad significance of yeast whole-cell applications. In addition to Saccharomyces cerevisiae, alternative yeast whole-cell biocatalysts are discussed such as Candida sp., Cryptococcus sp., Geotrichum sp., Issatchenkia sp., Kloeckera sp., Kluyveromyces sp., Pichia sp. (including Hansenula polymorpha = P. angusta), Rhodotorula sp., Rhodosporidium sp., alternative Saccharomyces sp., Schizosaccharomyces pombe, Torulopsis sp., Trichosporon sp., Trigonopsis variabilis, Yarrowia lipolytica and Zygosaccharomyces rouxii.","doi":"10.1186/1475-2859-7-25","authors":"Pscheidt B, Glieder A","authors_abbrev":"Pscheidt B et al.","pubmed_publication_date":"07 Aug 2008","pubmed_entrez_date":"2008-08-08","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16306692","title":"Mitochondrial ABC transporter Atm1p is required for protection against oxidative stress and vacuolar functions in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2005 Nov;69(11):2109-16","abstract":"A potential correlation between mitochondrial and vacuolar functions is known to exit in yeast. Fission yeast atm1(+), SPAC15A10.01, encodes a putative half-type ABC transporter with an N-terminal mitochondrial-targeting signal. In an attempt to evaluate the possible involvement of mitochondrion in vacuole function, a functional analysis of atm1(+) was performed by gene disruption. Growth of the atm1 mutant was inhibited in the presence of oxidizing agents, and S. cerevisiae Atm1p was found to complement this growth defect. atm1Delta cells exhibited defects in fluid-phase endocytosis and vacuolar fusion under hypotonic stress. GFP-tagged Atm1p was observed to be localized in the mitochondria. These data strongly suggest that fission yeast Atm1p was not only involved in protection against oxidative stress, but also played a role in vacuolar functions.","authors":"Iwaki T, Fujita Y, Tanaka N, Giga-Hama Y, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-11-25","publication_year":"2005","canto_session_key":"adc299cf891cc44d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-05 16:22:38","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-05 16:22:31","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-05"},{"uniquename":"PMID:27117417","title":"Single-Molecule Imaging Reveals a Collapsed Conformational State for DNA-Bound Cohesin.","citation":"Cell Rep 2016 May 03;15(5):988-998","abstract":"Cohesin is essential for the hierarchical organization of the eukaryotic genome and plays key roles in many aspects of chromosome biology. The conformation of cohesin bound to DNA remains poorly defined, leaving crucial gaps in our understanding of how cohesin fulfills its biological functions. Here, we use single-molecule microscopy to directly observe the dynamic and functional characteristics of cohesin bound to DNA. We show that cohesin can undergo rapid one-dimensional (1D) diffusion along DNA, but individual nucleosomes, nucleosome arrays, and other protein obstacles significantly restrict its mobility. Furthermore, we demonstrate that DNA motor proteins can readily push cohesin along DNA, but they cannot pass through the interior of the cohesin ring. Together, our results reveal that DNA-bound cohesin has a central pore that is substantially smaller than anticipated. These findings have direct implications for understanding how cohesin and other SMC proteins interact with and distribute along chromatin.","doi":"10.1016/j.celrep.2016.04.003","authors":"Stigler J, Çamdere GÖ, Koshland DE, Greene EC","authors_abbrev":"Stigler J et al.","pubmed_publication_date":"03 May 2016","pubmed_entrez_date":"2016-04-28","publication_year":"2016","canto_session_key":"483e7c2fbe4884c3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-23 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9348105","title":"DNA replication and order of cell cycle events: a role for protein isoprenylation?","citation":"Biol Chem 1997 Sep;378(9):963-73","abstract":"When the aya1+ gene is mutated, Schizosaccharomyces pombe cells become unable to react appropriately to a delay in DNA replication. Instead of stalling the cell cycle to allow completion of DNA synthesis, they proceed unperturbed towards mitosis and attempt to segregate the still unreplicated chromosomes. As a result, the genetic material segregates unevenly and the nuclei assume a mitotic catastrophe phenotype, characterized by torn chromosomes (cut), anucleated cells and scattered chromosomes. Interestingly, the aya1 phenotype can be suppressed by overexpression of either the catalytic subunit of S. pombe DNA polymerase alpha or of a novel protein called hur1 +p. The latter bears significant homology to the core of the human Rab escort protein, which belongs to a family of factors necessary to the post-translational isoprenylation of proteins like Ras, Rab and lamin B. When isoprenylation is chemically inhibited with R-limonene (a monoterpene derived from orange rind), wild type S. pombe cells become insensitive to an S phase delay, in a manner strongly reminiscent of aya1 mutants. Moreover, overexpression of hur1 +p in wild type cells rescues the failing checkpoint function. We propose that there is a strong correlation between the aya1 phenotype, S-M phase checkpoint function, and isoprenylation events in fission yeast.","authors":"Galli I, Uchiyama M, Wang TS","authors_abbrev":"Galli I et al.","pubmed_publication_date":"Sep 1997","pubmed_entrez_date":"1997-11-05","publication_year":"1997","canto_session_key":"cbdf7941bca5798b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-11-05 15:08:06","canto_approved_date":"2019-11-05 15:08:06","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-11-05 15:07:53","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC336.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-11-05"},{"uniquename":"PMID:39775128","title":"FLCCR is a fluorescent reporter system that quantifies the duration of different cell cycle phases at the single-cell level in fission yeast.","citation":"PLoS Biol 2025 Jan;23(1):e3002969","abstract":"Fission yeast is an excellent model system that has been widely used to study the mechanism that control cell cycle progression. However, there is a lack of tools that allow to measure with high precision the duration of the different phases of the cell cycle in individual cells. To circumvent this problem, we have developed a fluorescent reporter that allows the quantification of the different phases of the cell cycle at the single-cell level in most genetic backgrounds. To prove the accuracy of this fluorescent reporter, we have tested the reporter in strains known to have a delay in the G1/S or G2/M transitions, confirming the strength and versatility of the system. An advantage of this reporter is that it eliminates the need for culture synchronization, avoiding stressing the cells. Using this reporter, we show that unperturbed cells lacking Sty1 have a standard cell cycle length and distribution and that the extended length of these cells is due to their increased cell growth rate but not to alterations in their cell cycle progression.","doi":"10.1371/journal.pbio.3002969","authors":"Murciano-Julià G, Francos-Cárdenas M, Salat-Canela C, Hidalgo E, Ayté J","authors_abbrev":"Murciano-Julià G et al.","pubmed_publication_date":"Jan 2025","pubmed_entrez_date":"2025-01-08","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-01-09 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23695164","title":"Cross-species protein interactome mapping reveals species-specific wiring of stress response pathways.","citation":"Sci Signal 2013 May 21;6(276):ra38","abstract":"The fission yeast Schizosaccharomyces pombe has more metazoan-like features than the budding yeast Saccharomyces cerevisiae, yet it has similarly facile genetics. We present a large-scale verified binary protein-protein interactome network, \"StressNet,\" based on high-throughput yeast two-hybrid screens of interacting proteins classified as part of stress response and signal transduction pathways in S. pombe. We performed systematic, cross-species interactome mapping using StressNet and a protein interactome network of orthologous proteins in S. cerevisiae. With cross-species comparative network studies, we detected a previously unidentified component (Snr1) of the S. pombe mitogen-activated protein kinase Sty1 pathway. Coimmunoprecipitation experiments showed that Snr1 interacted with Sty1 and that deletion of snr1 increased the sensitivity of S. pombe cells to stress. Comparison of StressNet with the interactome network of orthologous proteins in S. cerevisiae showed that most of the interactions among these stress response and signaling proteins are not conserved between species but are \"rewired\"; orthologous proteins have different binding partners in both species. In particular, transient interactions connecting proteins in different functional modules were more likely to be rewired than conserved. By directly testing interactions between proteins in one yeast species and their corresponding binding partners in the other yeast species with yeast two-hybrid assays, we found that about half of the interactions that are traditionally considered \"conserved\" form modified interaction interfaces that may potentially accommodate novel functions.","doi":"10.1126/scisignal.2003350","authors":"Das J, Vo TV, Wei X, Mellor JC, Tong V, Degatano AG, Wang X, Wang L, Cordero NA, Kruer-Zerhusen N, Matsuyama A, Pleiss JA, Lipkin SM, Yoshida M, Roth FP, Yu H","authors_abbrev":"Das J et al.","pubmed_publication_date":"21 May 2013","pubmed_entrez_date":"2013-05-23","publication_year":"2013","canto_session_key":"e060bb20c665a6ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tommy Vo","canto_first_approved_date":"2016-12-29 16:54:46","canto_approved_date":"2023-03-10 19:42:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-29 09:06:19","canto_added_date":"2013-05-26 22:10:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Tommy Vo","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC589.08c","SPCC4F11.02","SPBC1685.01","SPAC821.07c","SPAC19G12.03","SPAC959.10","SPBC3E7.02c","SPCC330.13","SPAC12B10.02c","SPCC757.09c","SPAC1F8.07c","SPAP27G11.09c","SPCC1739.11c","SPBC211.02c","SPBC800.03","SPCC895.05","SPBC725.04","SPAC31A2.11c","SPCC330.05c","SPAC2C4.15c","SPAC664.15","SPCC74.06","SPAC23H3.06","SPBC691.02c","SPAC890.02c","SPAC824.08","SPAC27D7.03c","SPBC2D10.09","SPAC19A8.10","SPAC17G6.09","SPAC22F8.08","SPAC23A1.14c","SPAC1565.04c","SPBC1734.06","SPCC548.05c","SPAC8C9.17c","SPBC543.07","SPBC27.01c","SPBC1921.03c","SPAC8C9.03","SPAC19A8.14","SPCC1672.07","SPAC5H10.09c","SPBC839.07","SPAC3C7.03c","SPBC30D10.05c","SPBC651.10","SPBC354.03","SPBC211.04c","SPBC119.04","SPBC32F12.08c","SPAC26A3.16","SPCC364.02c","SPCC663.04","SPBC1718.07c","SPAC29B12.06c","SPAC26A3.17c","SPAC3A12.10","SPCC830.05c","SPAC15A10.03c","SPAC17G6.14c","SPAC20H4.07","SPBC1D7.05","SPAC644.14c","SPBC14F5.12c","SPAC2F7.02c","SPAC222.08c","SPBC29B5.01","SPAC29B12.04","SPAC3C7.12","SPAC637.12c","SPAC1D4.11c","SPAC25G10.08","SPBC21B10.05c","SPBC887.10","SPAC222.11","SPBC342.05","SPBC13E7.08c","SPBC26H8.01","SPCC24B10.13","SPBC4C3.06","SPAC4G8.10","SPAC31G5.09c","SPBC146.04","SPAC17A5.10","SPBC3D6.11c","SPAC1F3.02c","SPBC119.05c","SPBC337.13c","SPAC688.04c","SPAC30D11.10","SPAC688.11","SPBC725.02","SPBC14F5.05c","SPCC1223.06","SPAC17G8.10c","SPAC27D7.04","SPBC29A3.16","SPAC11E3.08c","SPAC14C4.05c","SPBC25H2.09","SPBP4H10.21c","SPBC3B8.11","SPAC644.13c","SPAC1805.16c","SPAC20H4.08","SPBC31E1.05","SPBC365.12c","SPAC9G1.02","SPAC17H9.04c","SPCC4G3.17","SPCC830.11c","SPBC1347.10","SPBC16A3.11","SPAC328.04","SPAPB1E7.12","SPCC162.08c","SPBC26H8.06","SPAC17D4.03c","SPBC13G1.03c","SPBC16E9.01c","SPAC19A8.07c","SPBC215.15","SPBC16E9.14c","SPAC3H5.10","SPAC19D5.01","SPAC23A1.15c","SPAC1D4.13","SPAC23A1.02c","SPAC227.18","SPBC12D12.01","SPAC3A12.12","SPAC6F12.04","SPBC2D10.11c","SPAC1002.17c","SPAC23D3.06c","SPAC11H11.06","SPAC26H5.05","SPBC428.14","SPAC26H5.09c","SPAC806.06c","SPBC146.07","SPBC1773.05c","SPCC31H12.03c","SPCC962.03c","SPBC685.09","SPAC227.13c","SPBC11B10.10c","SPBC725.13c","SPCC18.07","SPBC28F2.07","SPCC895.07","SPBC582.03","SPBC8D2.20c","SPAC24B11.06c","SPBC14F5.09c","SPBC3B9.01","SPBC56F2.07c","SPAC1834.11c","SPAC9E9.10c","SPAC227.06","SPAC3C7.02c","SPAC343.11c","SPAC7D4.04","SPBC31F10.11c","SPCC16C4.13c","SPAC1142.06","SPAC3H5.05c","SPBC3F6.03","SPAC806.07","SPBC19C2.05","SPBC409.07c","SPBC19G7.15","SPAC16A10.05c","SPBC119.09c","SPBC1604.20c","SPBC1706.01","SPBC215.14c","SPBC21C3.10c","SPAC24C9.14","SPBC27.08c","SPAC10F6.11c","SPBC1105.04c","SPBC32H8.12c","SPAC19G12.04","SPBC646.05c","SPBC317.01","SPBC12C2.07c","SPBC23E6.10c","SPCC338.13","SPCC1322.12c","SPAC13G7.02c","SPAC4H3.11c","SPBC725.07","SPBC428.05c","SPAP8A3.06","SPCC1795.01c","SPBC651.05c","SPCC4B3.06c","SPAC343.09"],"gene_count":200,"ltp_gene_count":2,"approved_date":"2016-12-29"},{"uniquename":"PMID:21169418","title":"Systematic screen of Schizosaccharomyces pombe deletion collection uncovers parallel evolution of the phosphate signal transduction pathway in yeasts.","citation":"Eukaryot Cell 2011 Feb;10(2):198-206","abstract":"The phosphate signal transduction (PHO) pathway, which regulates genes in response to phosphate starvation, is well defined in Saccharomyces cerevisiae. We asked whether the PHO pathway was the same in the distantly related fission yeast Schizosaccharomyces pombe. We screened a deletion collection for mutants aberrant in phosphatase activity, which is primarily a consequence of pho1(+) transcription. We identified a novel zinc finger-containing protein (encoded by spbc27b12.11c(+)), which we have named pho7(+), that is essential for pho1(+) transcriptional induction during phosphate starvation. Few of the S. cerevisiae genes involved in the PHO pathway appear to be involved in the regulation of the phosphate starvation response in S. pombe. Only the most upstream genes in the PHO pathway in S. cerevisiae (ADO1, DDP1, and PPN1) share a similar role in both yeasts. Because ADO1 and DDP1 regulate ATP and IP(7) levels, we hypothesize that the ancestor of these yeasts must have sensed similar metabolites in response to phosphate starvation but have evolved distinct mechanisms in parallel to sense these metabolites and induce phosphate starvation genes.","doi":"10.1128/EC.00216-10","authors":"Henry TC, Power JE, Kerwin CL, Mohammed A, Weissman JS, Cameron DM, Wykoff DD","authors_abbrev":"Henry TC et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2010-12-21","publication_year":"2011","canto_session_key":"cd89718416a84ef2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-02-22 17:43:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-02-23 10:44:58","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.11c","SPAC13G6.14","SPCC757.10","SPAC1071.04c","SPAC4F10.04","SPBC8E4.01c","SPAC4C5.02c","SPCC338.14","SPBC27B12.11c","SPCC1672.06c","SPBC106.10","SPAC17H9.04c","SPAC2F7.08c","SPBC713.07c","SPAC13G7.06","SPBP4G3.02","SPCC1393.13","SPAC23H3.13c","SPAC1D4.06c"],"gene_count":19,"ltp_gene_count":17,"approved_date":"2015-02-23"},{"uniquename":"PMID:25066056","title":"Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation.","citation":"Cell Metab 2014 Sep 02;20(3):448-57","abstract":"Dolichol is an obligate carrier of glycans for N-linked protein glycosylation, O-mannosylation, and GPI anchor biosynthesis. cis-prenyltransferase (cis-PTase) is the first enzyme committed to the synthesis of dolichol. However, the proteins responsible for mammalian cis-PTase activity have not been delineated. Here we show that Nogo-B receptor (NgBR) is a subunit required for dolichol synthesis in yeast, mice, and man. Moreover, we describe a family with a congenital disorder of glycosylation caused by a loss of function mutation in the conserved C terminus of NgBR-R290H and show that fibroblasts isolated from patients exhibit reduced dolichol profiles and enhanced accumulation of free cholesterol identically to fibroblasts from mice lacking NgBR. Mutation of NgBR-R290H in man and orthologs in yeast proves the importance of this evolutionarily conserved residue for mammalian cis-PTase activity and function. Thus, these data provide a genetic basis for the essential role of NgBR in dolichol synthesis and protein glycosylation.","doi":"10.1016/j.cmet.2014.06.016","authors":"Park EJ, Grabińska KA, Guan Z, Stránecký V, Hartmannová H, Hodaňová K, Barešová V, Sovová J, Jozsef L, Ondrušková N, Hansíková H, Honzík T, Zeman J, Hůlková H, Wen R, Kmoch S, Sessa WC","authors_abbrev":"Park EJ et al.","pubmed_publication_date":"02 Sep 2014","pubmed_entrez_date":"2014-07-29","publication_year":"2014","canto_session_key":"0e630b9e0c38e790","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kariona Grabinska","canto_first_approved_date":"2015-04-22 11:46:45","canto_approved_date":"2025-08-14 20:26:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-30 18:41:08","canto_added_date":"2014-07-30 15:29:29","annotation_curators":[{"name":"Kariona Grabinska","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2A9.06c","SPAC4D7.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-04-22"},{"uniquename":"PMID:27535724","title":"Unique properties of multiple tandem copies of the M26 recombination hotspot in mitosis and meiosis in Schizosaccharomyces pombe.","citation":"Gene 2016 Nov 15;593(1):185-192","abstract":"The M26 hotspot of the fission yeast Schizosaccharomyces pombe is one of the best-characterized eukaryotic hotspots of recombination. The hotspot requires a seven bp sequence, ATGACGT, that serves as a binding site for the Atf1-Pcr1 transcription factor, which is also required for activity. The M26 hotspot is active in meiosis but not mitosis and is active in some but not all chromosomal contexts and not on a plasmid. A longer palindromic version of M26, ATGACGTCAT, shows significantly greater activity than the seven bp sequence. Here, we tested whether the properties of the seven bp sequence were also true of the longer sequence by placing one, two, or three copies of the sequence into the ade6 gene, where M26 was originally discovered. These constructs were tested for activity when located on a plasmid or on a chromosome in mitosis and meiosis. We found that two copies of the 10bp M26 motif on a chromosome were significantly more active for meiotic recombination than one, but no further increase was observed with three copies. However, three copies of M26 on a chromosome created an Atf1-dependent mitotic recombination hotspot. When located on a plasmid, M26 also appears to behave as a mitotic recombination hotspot; however, this behavior most likely results from Atf1-dependent inter-allelic complementation between the plasmid and chromosomal ade6 alleles.","doi":"10.1016/j.gene.2016.08.022","authors":"Steiner WW, Recor CL, Zakrzewski BM","authors_abbrev":"Steiner WW et al.","pubmed_publication_date":"15 Nov 2016","pubmed_entrez_date":"2016-08-19","publication_year":"2016","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2016-08-20 00:15:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16467379","title":"Actin-depolymerizing protein Adf1 is required for formation and maintenance of the contractile ring during cytokinesis in fission yeast.","citation":"Mol Biol Cell 2006 Apr;17(4):1933-45","abstract":"The role of the actin-depolymerizing factor (ADF)/cofilin-family protein Adf1 in cytokinesis of fission yeast cells was studied. Adf1 was required for accumulation of actin at the division site by depolymerizing actin at the cell ends, assembly of the contractile ring through severing actin filaments, and maintenance of the contractile ring once formed. Genetic and cytological analyses suggested that it collaborates with profilin and capping protein in the mitotic reorganization of the actin cytoskeleton. Furthermore, it was unexpectedly found that Adf1 and myosin-II also collaborate in assembling the contractile ring. Tropomyosin was shown to antagonize the function of Adf1 in the contractile ring. We propose that formation and maintenance of the contractile ring are achieved by a balanced collaboration of these proteins.","authors":"Nakano K, Mabuchi I","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-02-10","publication_year":"2006","canto_session_key":"eaf900e1140bdecb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-06-30 13:52:24","canto_approved_date":"2023-02-03 21:10:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-30 13:25:37","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":74,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPAC4A8.15c","SPAC27F1.02c","SPBC21.06c","SPAP8A3.08","SPBC24C6.07","SPAC20G4.06c","SPAC12B10.07","SPCC645.05c","SPAC631.01c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2017-06-30"},{"uniquename":"PMID:21151114","title":"Dicer associates with chromatin to repress genome activity in Schizosaccharomyces pombe.","citation":"Nat Struct Mol Biol 2011 Jan;18(1):94-9","abstract":"In the fission yeast S. pombe, the RNA interference (RNAi) pathway is required to generate small interfering RNAs (siRNAs) that mediate heterochromatic silencing of centromeric repeats. Here, we demonstrate that RNAi also functions to repress genomic elements other than constitutive heterochromatin. Using DNA adenine methyltransferase identification (DamID), we show that the RNAi proteins Dcr1 and Rdp1 physically associate with some euchromatic genes, noncoding RNA genes and retrotransposon long terminal repeats, and that this association is independent of the Clr4 histone methyltransferase. Physical association of RNAi with chromatin is sufficient to trigger a silencing response but not to assemble heterochromatin. The mode of silencing at the newly identified RNAi targets is consistent with a co-transcriptional gene silencing model, as proposed earlier, and functions with trace amounts of siRNAs. We anticipate that similar mechanisms could also be operational in other eukaryotes.","doi":"10.1038/nsmb.1935","authors":"Woolcock KJ, Gaidatzis D, Punga T, Bühler M","authors_abbrev":"Woolcock KJ et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-12-15","publication_year":"2011","canto_session_key":"e64102699ced97dc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-05 11:32:33","canto_approved_date":"2021-10-21 21:50:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-11 11:53:10","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":53,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.09","SPBC428.08c","SPAC664.01c","SPCC188.13c","SPCC736.11"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-01-05"},{"uniquename":"EMBL:SPO132376","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18245881","title":"Novel algorithm for coexpression detection in time-varying microarray data sets.","citation":"IEEE/ACM Trans Comput Biol Bioinform 2008;5(1):120-135","abstract":"When analyzing the results of microarray experiments, biologists generally use unsupervised categorization tools. However, such tools regard each time point as an independent dimension and utilize the Euclidean distance to compute the similarities between expressions. Furthermore, some of these methods require the number of clusters to be determined in advance, which is clearly impossible in the case of a new dataset. Therefore, this study proposes a novel scheme, designated as the Variation-based Coexpression Detection (VCD) algorithm, to analyze the trends of expressions based on their variation over time. The proposed algorithm has two advantages. First, it is unnecessary to determine the number of clusters in advance since the algorithm automatically detects those genes whose profiles are grouped together and creates patterns for these groups. Second, the algorithm features a new measurement criterion for calculating the degree of change of the expressions between adjacent time points and evaluating their trend similarities. Three real-world microarray datasets are employed to evaluate the performance of the proposed algorithm.","doi":"10.1109/tcbb.2007.1052","authors":"Yin ZX, Chiang JH","authors_abbrev":"Yin ZX et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-02-05","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15246429","title":"Building the centromere: from foundation proteins to 3D organization.","citation":"Trends Cell Biol 2004 Jul;14(7):359-68","abstract":"At each mitosis, accurate segregation of every chromosome is ensured by the assembly of a kinetochore at each centromeric locus. Six foundation kinetochore proteins that assemble hierarchically and co-dependently have been identified in vertebrates. CENP-A, Mis12, CENP-C, CENP-H and CENP-I localize to a core domain of centromeric chromatin. The sixth protein, CENP-B, although not essential in higher eukaryotes, has homologues in fission yeast that bind pericentric DNA and are essential for heterochromatin formation. Foundation kinetochore proteins have various roles and mutual interactions, and their associations with centromeric DNA and heterochromatin create structural domains that support the different functions of the centromere. Advances in molecular and microscopic techniques, coupled with rare centromere variants, have enabled us to gain fresh insights into the linear and 3D organization of centromeric chromatin.","authors":"Amor DJ, Kalitsis P, Sumer H, Choo KH","authors_abbrev":"Amor DJ et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-07-13","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008572","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:K00570","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPRRNA.36"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:27417392","title":"Identification of an ATP-controlled allosteric switch that controls actin filament nucleation by Arp2/3 complex.","citation":"Nat Commun 2016 Jul 15;7:12226","abstract":"Nucleation of branched actin filaments by Arp2/3 complex is tightly regulated to control actin assembly in cells. Arp2/3 complex activation involves conformational changes brought about by ATP, Nucleation Promoting Factor (NPF) proteins, actin filaments and NPF-recruited actin monomers. To understand how these factors promote activation, we must first understand how the complex is held inactive in their absence. Here we demonstrate that the Arp3 C-terminal tail is a structural switch that prevents Arp2/3 complex from adopting an active conformation. The interaction between the tail and a hydrophobic groove in Arp3 blocks movement of Arp2 and Arp3 into an activated filament-like (short pitch) conformation. Our data indicate ATP binding destabilizes this interaction via an allosteric link between the Arp3 nucleotide cleft and the hydrophobic groove, thereby promoting the short-pitch conformation. Our results help explain how Arp2/3 complex is locked in an inactive state without activators and how autoinhibition is relieved.","doi":"10.1038/ncomms12226","authors":"Rodnick-Smith M, Liu SL, Balzer CJ, Luan Q, Nolen BJ","authors_abbrev":"Rodnick-Smith M et al.","pubmed_publication_date":"15 Jul 2016","pubmed_entrez_date":"2016-07-16","publication_year":"2016","canto_session_key":"78d4c709a724e7a7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-09-13 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.03","SPAC11H11.06"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:SPD276","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23376070","title":"Fission yeast LAMMER kinase Lkh1 regulates the cell cycle by phosphorylating the CDK-inhibitor Rum1.","citation":"Biochem Biophys Res Commun 2013 Mar 01;432(1):80-5","abstract":"In eukaryotes, LAMMER kinases are involved in various cellular events, including the cell cycle. However, no attempt has been made to investigate the mechanisms that underlie the involvement of LAMMER kinase. In this study, we performed a functional analysis of LAMMER kinase using the fission yeast, Schizosaccharomyces pombe. FACS analyses revealed that deletion of the gene that encodes the LAMMER kinase Lkh1 made mutant cells pass through the G1/S phase faster than their wild-type counterparts. Co-immunoprecipitation and an in vitro kinase assay also revealed that Lkh1 can interact with and phosphorylate Rum1 to activate this molecule as a cyclin-dependent kinase inhibitor, which blocks cell cycle progression from the G1 phase to the S phase. Peptide mass fingerprinting and kinase assay with Rum1(T110A) confirmed T110 as the Lkh1-dependent phosphorylation residue. In this report we present for the first time a positive acting mechanism that is responsible for the CKI activity of Rum1, in which the LAMMER kinase-mediated phosphorylation of Rum1 is involved.","doi":"10.1016/j.bbrc.2013.01.082","authors":"Yu EY, Lee JH, Kang WH, Park YH, Kim L, Park HM","authors_abbrev":"Yu EY et al.","pubmed_publication_date":"01 Mar 2013","pubmed_entrez_date":"2013-02-05","publication_year":"2013","canto_session_key":"66e0e290038b101f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-09-06 16:55:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-09 08:27:26","canto_added_date":"2013-05-03 15:26:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.09","SPBC336.12c","SPAC1D4.11c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2013-05-09"},{"uniquename":"PMID:33529549","title":"Chiasmata and the kinetochore component Dam1 are crucial for elimination of erroneous chromosome attachments and centromere oscillation at meiosis I.","citation":"Open Biol 2021 Feb;11(2):200308","abstract":"Establishment of proper chromosome attachments to the spindle requires elimination of erroneous attachments, but the mechanism of this process is not fully understood. During meiosis I, sister chromatids attach to the same spindle pole (mono-oriented attachment), whereas homologous chromosomes attach to opposite poles (bi-oriented attachment), resulting in homologous chromosome segregation. Here, we show that chiasmata that link homologous chromosomes and kinetochore component Dam1 are crucial for elimination of erroneous attachments and oscillation of centromeres between the spindle poles at meiosis I in fission yeast. In chiasma-forming cells, Mad2 and Aurora B kinase, which provides time for attachment correction and destabilizes erroneous attachments, respectively, caused elimination of bi-oriented attachments of sister chromatids, whereas in chiasma-lacking cells, they caused elimination of mono-oriented attachments. In chiasma-forming cells, in addition, homologous centromere oscillation was coordinated. Furthermore, Dam1 contributed to attachment elimination in both chiasma-forming and chiasma-lacking cells, and drove centromere oscillation. These results demonstrate that chiasmata alter attachment correction patterns by enabling error correction factors to eliminate bi-oriented attachment of sister chromatids, and suggest that Dam1 induces elimination of erroneous attachments. The coincidental contribution of chiasmata and Dam1 to centromere oscillation also suggests a potential link between centromere oscillation and attachment elimination.","doi":"10.1098/rsob.200308","authors":"Wakiya M, Nishi E, Kawai S, Yamada K, Katsumata K, Hirayasu A, Itabashi Y, Yamamoto A","authors_abbrev":"Wakiya M et al.","pubmed_publication_date":"Feb 2021","pubmed_entrez_date":"2021-02-02","publication_year":"2021","canto_session_key":"4899d62746d85c40","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ayumu Yamamoto","canto_first_approved_date":"2023-06-19 14:36:41","canto_approved_date":"2024-04-27 17:34:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-03 08:55:55","canto_added_date":"2021-02-04 01:15:06","annotation_curators":[{"name":"Ayumu Yamamoto","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC589.08c","SPAC17A5.11","SPBC20F10.06","SPBP35G2.03c","SPCC320.13c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2023-06-19"},{"uniquename":"PMID:10490609","title":"Clustered adenine/thymine stretches are essential for function of a fission yeast replication origin.","citation":"Mol Cell Biol 1999 Oct;19(10):6699-709","abstract":"We have determined functional elements required for autonomous replication of the Schizosaccharomyces pombe ars2004 that acts as an intrinsic chromosomal replication origin. Internal deletion analysis of a 940-bp fragment (ars2004M) showed three regions, I to III, to be required for autonomously replicating sequence (ARS) activity. Eight-base-pair substitutions in the 40-bp region I, composed of arrays of adenines on a DNA strand, resulted in a great reduction of ARS activity. Substitutions of region I with synthetic sequences showed that no specific sequence but rather repeats of three or more consecutive adenines or thymines, without interruption by guanine or cytosine, are required for the ARS activity. The 65-bp region III contains 11 repeats of the AAAAT sequence, while the 165-bp region II has short adenine or thymine stretches and a guanine- and cytosine-rich region which enhances ARS activity. All three regions in ars2004M can be replaced with 40-bp poly(dA/dT) fragments without reduction of ARS activity. Although spacer regions in the ars2004M enhance ARS activity, all could be deleted when an 40-bp poly(dA/dT) fragment was added in place of region I. Our results suggest that the origin activity of fission yeast replicators depends on the number of adenine/thymine stretches, the extent of their clustering, and presence of certain replication-enhancing elements.","authors":"Okuno Y, Satoh H, Sekiguchi M, Masukata H","authors_abbrev":"Okuno Y et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-09-22","publication_year":"1999","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17369611","title":"Regulation of histone H3 lysine 56 acetylation in Schizosaccharomyces pombe.","citation":"J Biol Chem 2007 May 18;282(20):15040-7","abstract":"In Saccharomyces cerevisiae, acetylation of lysine 56 (Lys-56) in the globular domain of histone H3 plays an important role in response to genotoxic agents that interfere with DNA replication. However, the regulation and biological function of this modification are poorly defined in other eukaryotes. Here we show that Lys-56 acetylation in Schizosaccharomyces pombe occurs transiently during passage through S-phase and is normally removed in G(2). Genotoxic agents that cause DNA double strand breaks during replication elicit a delay in deacetylation of histone H3 Lys-56. In addition, mutant cells that cannot acetylate Lys-56 are acutely sensitive to genotoxic agents that block DNA replication. Moreover, we show that Spbc342.06cp, a previously uncharacterized open reading frame, encodes the functional homolog of S. cerevisiae Rtt109, and that this protein acetylates H3 Lys-56 both in vitro and in vivo. Altogether, our results indicate that both the regulation of histone H3 Lys-56 acetylation by its histone acetyltransferase and histone deacetylase and its role in the DNA damage response are conserved among two distantly related yeast model organisms.","authors":"Xhemalce B, Miller KM, Driscoll R, Masumoto H, Jackson SP, Kouzarides T, Verreault A, Arcangioli B","authors_abbrev":"Xhemalce B et al.","pubmed_publication_date":"18 May 2007","pubmed_entrez_date":"2007-03-21","publication_year":"2007","canto_session_key":"9b5edbe6f0efcb45","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-28 08:19:10","canto_approved_date":"2024-02-29 18:53:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-08 16:27:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.11c","SPBC8D2.04","SPAC1834.04","SPBC342.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-10-28"},{"uniquename":"PMID:24018691","title":"Functional expression of Schizosaccharomyces pombe Vba2p in the vacuolar membrane of Saccharomyces cerevisiae.","citation":"Biosci Biotechnol Biochem 2013;77(9):1988-90","abstract":"A vacuolar membrane protein, Vba2p of Schizosaccharomyces pombe, is involved in basic amino acid uptake by intact cells. Here we found evidence that Vba2p mediated ATP-dependent lysine uptake by vacuolar membrane vesicles of Saccharomyces cerevisiae. Vba2p was also responsible for quinidine sensitivity, and the addition of lysine improved cell growth on quinidine-containing media. These findings should be useful for further characterization of Vba2p.","authors":"Pongcharoen P, Kawano-Kawada M, Iwaki T, Sugimoto N, Sekito T, Akiyama K, Takegawa K, Kakinuma Y","authors_abbrev":"Pongcharoen P et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-09-11","publication_year":"2013","canto_session_key":"084c3a752e6472f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-21 15:12:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-04 16:39:25","canto_added_date":"2013-09-30 13:21:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC460.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-04"},{"uniquename":"PMID:7548847","title":"Control of signal transduction and morphogenesis by Ras.","citation":"Semin Cell Biol 1995 Apr;6(2):89-94","abstract":"The single Ras homologue (Ras1) of S. pombe regulates two distinct processes: (1) Signal transduction through a MAP kinase-like protein kinase cascade in response to mating pheromones. In this pathway Ras1 interacts with the protein kinase Byr2 and leads to its activation in conjunction with a signal from the receptor-coupled, heterotrimeric G protein. (2) Polarized cell growth both during the cell cycle and during directed cell extension towards a mating partner. Ras1 interacts with Ral1/Scd1, a putative guanine-nucleotide-exchange factor, which could activate Cdc42, Rho-like GTP-binding protein. Cdc42 may regulate the dynamics of the actin cytoskeleton.","authors":"Hughes DA","authors_abbrev":"Hughes DA","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15837798","title":"Efficient formation of bipolar microtubule bundles requires microtubule-bound gamma-tubulin complexes.","citation":"J Cell Biol 2005 Apr 25;169(2):297-308","abstract":"The mechanism for forming linear microtubule (MT) arrays in cells such as neurons, polarized epithelial cells, and myotubes is not well understood. A simpler bipolar linear array is the fission yeast interphase MT bundle, which in its basic form contains two MTs that are bundled at their minus ends. Here, we characterize mto2p as a novel fission yeast protein required for MT nucleation from noncentrosomal gamma-tubulin complexes (gamma-TuCs). In interphase mto2Delta cells, MT nucleation was strongly inhibited, and MT bundling occurred infrequently and only when two MTs met by chance in the cytoplasm. In wild-type 2, we observed MT nucleation from gamma-TuCs bound along the length of existing MTs. We propose a model on how these nucleation events can more efficiently drive the formation of bipolar MT bundles in interphase. Key to the model is our observation of selective antiparallel binding of MTs, which can both explain the generation and spatial separation of multiple bipolar bundles.","authors":"Janson ME, Setty TG, Paoletti A, Tran PT","authors_abbrev":"Janson ME et al.","pubmed_publication_date":"25 Apr 2005","pubmed_entrez_date":"2005-04-20","publication_year":"2005","canto_session_key":"f43a3b416d8fede7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-07-14 08:07:47","canto_approved_date":"2022-07-14 08:07:47","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-07-14 08:07:40","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":8,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.05c","SPCC1223.02","SPCC1223.06","SPAC15A10.16","SPAC3C7.12","SPCC417.07c","SPAC18G6.15","SPAPB1A10.09","SPBC800.05c","SPBC11C11.04c","SPBC365.15","SPBC428.01c","SPBC428.20c","SPBC902.06","SPBC19C2.05"],"gene_count":15,"ltp_gene_count":2,"approved_date":"2022-07-14"},{"uniquename":"EMBL:AF047464","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1193166","title":"A study of the chromosomes of the yeast Schizosaccharomyces pombe by light and electron microscopy.","citation":"Exp Cell Res 1975 Nov;96(1):15-22","abstract":"","authors":"Fischer P, Binder M, Wintersberger U","authors_abbrev":"Fischer P et al.","pubmed_publication_date":"Nov 1975","pubmed_entrez_date":"1975-11-01","publication_year":"1975","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15671491","title":"Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human.","citation":"J Biochem 2004 Dec;136(6):805-12","abstract":"Cleavage of the 5'-cap structure is involved in the major 5'-to-3' and nonsense-mediated mRNA decay pathways, and the protein complex consisting of Dcp1 and Dcp2 has been identified as the species responsible for the decapping reaction in Saccharomyces cerevisiae and human. Although in vitro studies indicate that Dcp2 is catalytically an active component, the role of Dcp1 in the decapping reaction remains to be explored in organisms other than budding yeast. To elucidate the Dcp1-dependent decapping mechanisms, we identified the homologues of S. cerevisiae Dcp1 (ScDcp1) in higher eukaryotes and analyzed their functions in the different species. The phenotypes of slow growth and mRNA stabilization induced by Scdcp1-gene disruption in budding yeast could be suppressed by the Shizosaccharomyces pombe SpDcp1 but not by the human homologue hDcp1. In contrast, the same phenotypes caused by Spdcp1-gene disruption in fission yeast were effectively complemented by hDcp1 and its partial sequence comparable to SpDcp1. These results indicate that not only Dcp2 but also Dcp1 plays an indispensable role in mRNA-decay pathway and that the characteristics of Dcp1-dependent decapping reaction in fission yeast hold an intermediate position in the evolution of mRNA-decay machinery from budding yeast to mammals.","authors":"Sakuno T, Araki Y, Ohya Y, Kofuji S, Takahashi S, Hoshino S, Katada T","authors_abbrev":"Sakuno T et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2005-01-27","publication_year":"2004","canto_session_key":"784a98102f711f7f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-10-30 17:08:41","canto_approved_date":"2024-03-24 21:01:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-30 17:06:23","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.21","SPAC19A8.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-10-30"},{"uniquename":"PMID:39911909","title":"Alpha-Synuclein Fails to Form Aggregates in Endocytosis-Defective Fission Yeast Strains, ∆  myo1  and ∆  end4 .","citation":"MicroPubl Biol 2025;2025","abstract":"Alpha-Synuclein (α-Syn) is a soluble neuronal protein whose aggregation is one of the hallmarks of Parkinson's disease (PD). We previously developed a fission yeast model of PD that recapitulates α-Syn aggregation upon high-level expression of human α-Syn. Here, we show that α-Syn aggregate formation in yeast requires Myo1 and End4 , proteins essential for the early steps of endocytosis. α-Syn expression levels in Δ  myo1  and  ∆end4  cells were comparable to wild-type cells, suggesting that defects in endocytosis disrupt α-Syn aggregation. These findings highlight the critical role of endocytosis in α-Syn aggregation and PD pathology.","doi":"10.17912/micropub.biology.001479","authors":"Takasaki T, Yamada R, Sugimoto Y, Sugiura R","authors_abbrev":"Takasaki T et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-02-06","publication_year":"2025","canto_session_key":"c89552191cdfd9a6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-02-07 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21359180","title":"Phosphorylation of the MBF repressor Yox1p by the DNA replication checkpoint keeps the G1/S cell-cycle transcriptional program active.","citation":"PLoS One 2011 Feb 16;6(2):e17211","abstract":"In fission yeast Schizosaccharomyces pombe G1/S cell-cycle regulated transcription depends upon MBF. A negative feedback loop involving Nrm1p and Yox1p bound to MBF leads to transcriptional repression as cells exit G1 phase. However, activation of the DNA replication checkpoint response during S phase results in persistent expression of MBF-dependent genes.\nThis report shows that Yox1p binding to MBF is Nrm1-dependent and that Yox1p and Nrm1p require each other to bind and repress MBF targets. In response to DNA replication stress both Yox1p and Nrm1p dissociate from MBF at promoters leading to de-repression of MBF targets. Inactivation of Yox1p is an essential part of the checkpoint response. Cds1p (human Chk2p) checkpoint protein kinase-dependent phosphorylation of Yox1p promotes its dissociation from the MBF transcription factor. We establish that phosphorylation of Yox1p at Ser114, Thr115 is required for maximal checkpoint-dependent activation of the G1/S cell-cycle transcriptional program.\nThis study shows that checkpoint-dependent phosphorylation of Yox1p at Ser114, Thr115 results in de-repression of the MBF transcriptional program. The remodeling of the cell cycle transcriptional program by the DNA replication checkpoint is likely to comprise an important mechanism for the avoidance of genomic instability.","doi":"10.1371/journal.pone.0017211","authors":"Caetano C, Klier S, de Bruin RA","authors_abbrev":"Caetano C et al.","pubmed_publication_date":"16 Feb 2011","pubmed_entrez_date":"2011-03-02","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F3.09c","SPBC21B10.13c","SPCC18B5.11c","SPBC16A3.07c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:37291367","title":"Yeast diversity in pit mud and related volatile compounds in fermented grains of chinese strong-flavour liquor.","citation":"AMB Express 2023 Jun 08;13(1):56","abstract":"Chinese strong-flavour liquor is produced via a traditional solid-state fermentation strategy facilitated by live microorganisms in pit mud-based cellars. For the present analysis, pit mud samples from different spatial locations within fermentation cellars were collected, and the yeast communities therein were assessed via culture-based and denaturing gradient gel electrophoresis (DGGE) approaches. These analyses revealed significant differences in the composition of yeast communities present in different layers of pit mud. In total, 29 different yeast species were detected, and principal component analyses revealed clear differences in microbial diversity in pit mud samples taken from different cellar locations. Culture-dependent strategies similarly detected 20 different yeast species in these samples. However, while Geotrichum silvicola, Torulaspora delbrueckii, Hanseniaspora uvarum, Saturnispora silvae, Issatchenkia orientalis, Candida mucifera, Kazachstania barnettii, Cyberlindnera jadinii, Hanseniaspora spp., Alternaria tenuissima, Cryptococcus laurentii, Metschnikowia spp., and Rhodotorula dairenensis were detected via a PCR-DGGE approach, they were not detectable in culture-dependent analyses. In contrast, culture-based approaches led to the identification of Schizosaccharomyces pombe and Debaryomyces hansenii in these pit mud samples, whereas they were not detected using DGGE fingerprints profiles. An additional HS-SPME-GC-MS-based analysis of the volatile compounds present in fermented grains samples led to the identification of 66 such compounds, with the highest levels of volatile acids, esters, and alcohols being detected in fermented grains from lower layer samples. A canonical correspondence analysis (CCA) suggested they were significant correlations between pit mud yeast communities and associated volatile compounds in fermented grains.","doi":"10.1186/s13568-023-01562-7","authors":"Shoubao Y, Jie Y, TingTing S, Jiaquan G, Cuie S","authors_abbrev":"Shoubao Y et al.","pubmed_publication_date":"08 Jun 2023","pubmed_entrez_date":"2023-06-08","publication_year":"2023","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2023-06-10 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009904","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23795300","title":"Yeast rises to the occasion.","citation":"Elife 2013 Jun 18;2:e00933","abstract":"Genetic analyses of 15 species of yeast have shed new light on the divergence of gene regulation during evolution, with significant changes occurring after an event in which a whole genome was duplicated.","doi":"10.7554/eLife.00933","authors":"Ragan MA","authors_abbrev":"Ragan MA","pubmed_publication_date":"18 Jun 2013","pubmed_entrez_date":"2013-06-25","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30240645","title":"S-Adenosylmethionine Synthetase Is Required for Cell Growth, Maintenance of G0 Phase, and Termination of Quiescence in Fission Yeast.","citation":"iScience 2018 Jul 27;5:38-51","abstract":"S-adenosylmethionine is an important compound, because it serves as the methyl donor in most methyl transfer reactions, including methylation of proteins, nucleic acids, and lipids. However, cellular defects in the genetic disruption of S-adenosylmethionine synthesis are not well understood. Here, we report the isolation and characterization of temperature-sensitive mutants of fission yeast S-adenosylmethionine synthetase (Sam1). Levels of S-adenosylmethionine and methylated histone H3 were greatly diminished in sam1 mutants. sam1 mutants stopped proliferating in vegetative culture and arrested specifically in G2 phase without cell elongation. Furthermore, sam1 mutants lost viability during nitrogen starvation-induced G0 phase quiescence. After release from the G0 state, sam1 mutants could neither increase in cell size nor re-initiate DNA replication in the rich medium. Sam1 is thus required for cell growth and proliferation, and maintenance of and exit from quiescence. sam1 mutants lead to broad cellular and drug response defects, as expected, since S. pombe contains more than 90 S-adenosylmethionine-dependent methyltransferases.","doi":"10.1016/j.isci.2018.06.011","authors":"Hayashi T, Teruya T, Chaleckis R, Morigasaki S, Yanagida M","authors_abbrev":"Hayashi T et al.","pubmed_publication_date":"27 Jul 2018","pubmed_entrez_date":"2018-09-22","publication_year":"2018","canto_session_key":"6d6dbc2ba59f2e7b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takeshi Hayashi","canto_first_approved_date":"2018-10-19 16:02:49","canto_approved_date":"2018-10-19 16:02:50","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-10-12 00:38:05","canto_added_date":"2018-09-23 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Takeshi Hayashi","community_curator":true,"annotation_count":53,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14F5.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-19"},{"uniquename":"PMID:1549128","title":"Schizosaccharomyces pombe sxa1+ and sxa2+ encode putative proteases involved in the mating response.","citation":"Mol Cell Biol 1992 Apr;12(4):1827-34","abstract":"The Schizosaccharomyces pombe sxa1 and sxa2 mutants showed an exaggerated response to mating pheromones, producing excessively long conjugation tubes and exhibiting mating deficiency. This phenotype was similar to phenotypes of cells bearing an activated allele of ras1, such as ras1Val-17 or ras1Leu-66, and phenotypes of cells defective in gap1. However, genetic evidence suggested that the sxa1 and sxa2 gene products are not directly involved in the Ras1 pathway. The gene products of sxa1 and sxa2, as deduced from their nucleotide sequences, were homologous to aspartyl proteases and serine carboxypeptidases, respectively. The sxa1 gene function was required for efficient mating only in h+ cells, although even disruption of sxa1 did not completely abolish the mating ability. Conversely, the sxa2 gene function was required only in h- cells. Wild-type cells produced a diffusible substance, which may be the sxa2 gene product itself, that could confer fertility to sxa2 mutant cells placed at a distance. These observations are consistent with the possibility that the sxa gene products are involved in degradation or processing of the mating pheromones and that their loss cause a persistent response to the pheromones.","authors":"Imai Y, Yamamoto M","authors_abbrev":"Imai Y et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"9ddea08e60ffe505","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-03-29 13:14:51","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-08-16 13:39:35","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"vw253@cam.ac.uk","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1296.03c","SPAC26A3.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-08-16"},{"uniquename":"EMBL:AU013816","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16325501","title":"The fission yeast MO25 protein functions in polar growth and cell separation.","citation":"Eur J Cell Biol 2005 Dec;84(12):915-26","abstract":"Proteins of the MO25 family are widely conserved but their function has not been characterized in detail. Human MO25 is a cofactor of LKB1, a conserved protein kinase with roles in cell polarity in nematodes, flies and mammalian cells. Furthermore, the budding yeast MO25 homologue, Hym1, is important for cell separation and morphogenesis. We have characterized Pmo25p, the MO25 homologue in the fission yeast Schizosaccharomyces pombe. Pmo25p is an essential protein required for polar growth; in its absence the actin cytoskeleton becomes depolarized and cells adopt a round morphology. In addition, pmo25 mutants are defective in cell separation. Both functions of Pmo25p appear to be mediated by the Orb6p-Mob2p kinase complex. Pmo25p shows no distinct localization during interphase, but it is recruited to one of the two spindle pole bodies during anaphase and to the division site during cytokinesis. The septation initiation network (SIN) regulates the localization of Pmo25p, suggesting that it regulates Pmo25p function during cell division.","authors":"Mendoza M, Redemann S, Brunner D","authors_abbrev":"Mendoza M et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-12-06","publication_year":"2005","canto_session_key":"bc9efc288e644f66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-21 08:53:37","canto_approved_date":"2024-01-15 10:02:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-01 12:13:17","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9G1.11c","SPAC1834.06c","SPCC970.04c","SPAC24H6.05","SPAC24B11.11c","SPAC821.12","SPAC6F6.08c","SPAC9G1.09","SPBC21.06c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-10-21"},{"uniquename":"PMID:16112668","title":"Shugoshin, a guardian for sister chromatid segregation.","citation":"Exp Cell Res 2005 Oct 15;310(1):1-9","abstract":"To ensure sister chromatids to be equally transmitted to daughter cells, it is imperative that physical association of sister chromatids is maintained during S, G2, and early mitosis until the onset of anaphase. Cohesion of sister chromatids in eukaryotes is largely achieved by the cohesin complex. In vertebrates, cohesin molecules are dissociated from chromosome arms but not from centromeres during prophase by the so-called prophase pathway. Although it remains unclear what is the molecular basis by which centromeric cohesin is retained, a flurry of recent studies have shed light on a family of proteins named Shugoshin (Sgo) that are evolutionarily conserved across eukaryotes. Sgo1 functions as a protector of centromeric cohesin during meiosis in yeast and during mitosis in high eukaryotes. Suppression of Sgo1 function results in premature separation of sister chromatids in both meiosis and mitosis. The discovery of members of the Sgo family may help to explain how centromeric cohesin is protected from dissociation from DNA until the onset of anaphase. Given the importance of chromosome cohesion in the maintenance of genomic stability, further characterization of Sgo1 and related molecules may also open up new avenues of research for developing new strategies for cancer intervention.","authors":"Wang X, Dai W","authors_abbrev":"Wang X et al.","pubmed_publication_date":"15 Oct 2005","pubmed_entrez_date":"2005-08-23","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17948055","title":"The JmjC domain protein Epe1 prevents unregulated assembly and disassembly of heterochromatin.","citation":"EMBO J 2007 Nov 14;26(22):4670-82","abstract":"Heterochromatin normally has prescribed chromosomal positions and must not encroach on adjacent regions. We demonstrate that the fission yeast protein Epe1 stabilises silent chromatin, preventing the oscillation of heterochromatin domains. Epe1 loss leads to two contrasting phenotypes: alleviation of silencing within heterochromatin and expansion of silent chromatin into neighbouring euchromatin. Thus, we propose that Epe1 regulates heterochromatin assembly and disassembly, thereby affecting heterochromatin integrity, centromere function and chromosome segregation fidelity. Epe1 regulates the extent of heterochromatin domains at the level of chromatin, not via the RNAi pathway. Analysis of an ectopically silenced site suggests that heterochromatin oscillation occurs in the absence of heterochromatin boundaries. Epe1 requires predicted iron- and 2-oxyglutarate (2-OG)-binding residues for in vivo function, indicating that it is probably a 2-OG/Fe(II)-dependent dioxygenase. We suggest that, rather than being a histone demethylase, Epe1 may be a protein hydroxylase that affects the stability of a heterochromatin protein, or protein-protein interaction, to regulate the extent of heterochromatin domains. Thus, Epe1 ensures that heterochromatin is restricted to the domains to which it is targeted by RNAi.","authors":"Trewick SC, Minc E, Antonelli R, Urano T, Allshire RC","authors_abbrev":"Trewick SC et al.","pubmed_publication_date":"14 Nov 2007","pubmed_entrez_date":"2007-10-20","publication_year":"2007","canto_session_key":"273b40e887289b97","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-20 02:28:17","canto_approved_date":"2024-04-23 16:06:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-16 17:57:08","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.16c","SPCC188.13c","SPAC664.01c","SPAC23G3.01","SPBC428.08c","SPCC11E10.08"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-10-20"},{"uniquename":"PMID:26443240","title":"PKA antagonizes CLASP-dependent microtubule stabilization to re-localize Pom1 and buffer cell size upon glucose limitation.","citation":"Nat Commun 2015 Oct 07;6:8445","abstract":"Cells couple growth with division and regulate size in response to nutrient availability. In rod-shaped fission yeast, cell-size control occurs at mitotic commitment. An important regulator is the DYRK-family kinase Pom1, which forms gradients from cell poles and inhibits the mitotic activator Cdr2, itself localized at the medial cortex. Where and when Pom1 modulates Cdr2 activity is unclear as Pom1 medial cortical levels remain constant during cell elongation. Here we show that Pom1 re-localizes to cell sides upon environmental glucose limitation, where it strongly delays mitosis. This re-localization is caused by severe microtubule destabilization upon glucose starvation, with microtubules undergoing catastrophe and depositing the Pom1 gradient nucleator Tea4 at cell sides. Microtubule destabilization requires PKA/Pka1 activity, which negatively regulates the microtubule rescue factor CLASP/Cls1/Peg1, reducing CLASP's ability to stabilize microtubules. Thus, PKA signalling tunes CLASP's activity to promote Pom1 cell side localization and buffer cell size upon glucose starvation.","doi":"10.1038/ncomms9445","authors":"Kelkar M, Martin SG","authors_abbrev":"Kelkar M et al.","pubmed_publication_date":"07 Oct 2015","pubmed_entrez_date":"2015-10-08","publication_year":"2015","canto_session_key":"8ad14ac446a38d4f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2021-03-24 16:57:33","canto_approved_date":"2025-09-03 15:45:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-11 12:17:11","canto_added_date":"2015-10-09 00:18:52","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.07c","SPBC19C7.03","SPAC3C7.12","SPCC1753.02c","SPAC24B11.06c","SPBC1604.20c","SPBC106.10","SPBC409.07c","SPBC1706.01","SPBC30D10.10c","SPAC18G6.15","SPCC285.09c","SPAC3G9.12","SPAC2F7.03c","SPAC23H3.13c"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2021-03-24"},{"uniquename":"PMID:18759114","title":"Effects of decreased specific glutathione reductase activity in a chromate-tolerant mutant of Schizosaccharomyces pombe.","citation":"Folia Microbiol (Praha) 2008;53(4):308-14","abstract":"A chromate-tolerant mutant chr1-663T bearing a stable one-gene mutation and its parental strain 6chr(+) were used to investigate the background of Cr(VI) tolerance in the fission yeast Schizosaccharomyces pombe. The mutant chr1-663T displayed a significantly decreased specific glutathione reductase (GR) activity coded by the pgr1 (+) gene compared with its parental strain. Transformants of the mutant chr1-663T with a nonintegrative pUR18N vector expressing the pgr1 (+) gene exhibited the same Cr(VI) sensitivity and specific GR activity as their parental strain, demonstrating the importance of the GR-NADPH system in Cr(VI) tolerance. Transformants, nevertheless, exhibited an increased intracellular peroxide concentration, a decreased Cr(VI)-reducing and HO*-producing ability, which suggested an unbalanced oxidoreduction state of cells and partial complementation of the GR function. No mutation was found in the sequences of the pgr1 (+) and the pap1 (+) (transcriptional regulatory gene of GR) genes of the Cr(VI)-tolerant mutant by sequence analysis.","doi":"10.1007/s12223-008-0048-4","authors":"Koósz Z, Gazdag Z, Miklós I, Benko Z, Belágyi J, Antal J, Meleg B, Pesti M","authors_abbrev":"Koósz Z et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-09-02","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10325412","title":"Substrate specificity of ultraviolet DNA endonuclease (UVDE/Uve1p) from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1999 Jun 01;27(11):2256-64","abstract":"Schizosaccharomyces pombe ultraviolet DNA endonuclease (UVDE or Uve1p) has been shown to cleave 5' to UV light-induced cyclobutane pyrimidine dimers (CPDs) and pyrimidine-pyrimidone (6-4) photoproducts (6-4PP). This endonuclease is believed to function in the initial step in an alternative excision repair pathway for the removal of DNA damage caused by exposure to UV light. An active truncated form of this protein, Delta228-Uve1p, has been successfully overexpressed, affinity purified and partially characterized. In the present study we present data from a detailed substrate specificity trial. We have determined that the substrate range of Uve1p is much greater than was originally believed. We demonstrate that this DNA damage repair protein is capable of recognizing an array of UV-induced DNA photoproducts (cis-syn-, trans-syn I- and trans-syn II CPDs, 6-4PP and Dewar isomers) that cause varying degrees of distortion in a duplex DNA molecule. We also demonstrate that Uve1p recognizes non-UV-induced DNA damage, such as platinum-DNA GG diadducts, uracil, dihydrouracil and abasic sites. This is the first time that a single DNA repair endonuclease with the ability to recognize such a diverse range of lesions has been described. This study suggests that Uve1p and the alternative excision repair pathway may participate broadly in the repair of DNA damage.","authors":"Avery AM, Kaur B, Taylor JS, Mello JA, Essigmann JM, Doetsch PW","authors_abbrev":"Avery AM et al.","pubmed_publication_date":"01 Jun 1999","pubmed_entrez_date":"1999-05-15","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23598797","title":"Lipid droplet organelle distribution in populations of dividing cells studied by simulation.","citation":"Phys Biol 2013 Jun;10(3):036007","abstract":"One of the key questions in cell biology is how organelles are passed from parent to daughter cells. To help address this question, I used Brownian dynamics to simulate lipid droplets as model organelles in populations of dividing cells. Lipid droplets are dynamic bodies that can form both de novo and by fission, they can also be depleted. The quantitative interplay among these three events is unknown but would seem crucial for controlling droplet distribution in populations of dividing cells. Surprisingly, of the three main events studied: biogenesis, fission, and depletion, the third played the key role in maintaining droplet organelle number-and to a lesser extent volume-in populations of dividing cells where formation events would have seemed paramount. In the case of lipid droplets, this provides computational evidence that they must be sustained, most likely through contacts with the endoplasmic reticulum. The findings also agree with video microscopy experiments over much shorter timescales where droplet depletion in fission yeast cells was not observed. In general, this work shows that organelle maintenance is invaluable and lack thereof cannot necessarily be compensated for by organelle formation. This study provides a time-accurate, physical-based template for long-term cell division studies.","doi":"10.1088/1478-3975/10/3/036007","authors":"Dalhaimer P","authors_abbrev":"Dalhaimer P","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-04-20","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15965643","title":"Functional characterization of Schizosaccharomyces pombe neutral trehalase altered in phosphorylatable serine residues.","citation":"Arch Microbiol 2005 Sep;183(6):394-400","abstract":"The activation of neutral trehalase (Ntp1) by metabolic and physical stresses in Schizosaccharomyces pombe is dependent on protein kinases Pka1 or Sck1. Mutant ntp1 alleles altered for potentially phosphorylatable serine residues within the regulatory domain of the enzyme were integrated under the control of the native promoter in an ntp1-deleted background. The trehalase variants were expressed to a level similar to that of wild type trehalase from control cells. Wild type trehalase protein accumulated and became activated upon stress while a single change in the evolutionary conserved perfect consensus site for Pka1-dependent phosphorylation (Ser71), as well as point mutations in two other putative phosphorylation sites (Ser6, Ser51), produced inactive trehalases unresponsive to stress. Trehalose content in the trehalase mutated strains increased upon salt stress to a level comparable to that shown by an ntp1-deleted mutant. When exposed to heat shock, trehalose hyperaccumulated in the ntp1-null strain lacking trehalase protein and this phenotype was shown by some (Ser71), but not all, strains with serine mutated trehalases. The mutant trehalases retained the ability to form complexes with trehalose-6-phosphate synthase. These data support a role of potentially phosphorylated specific sites for the activation of S. pombe neutral trehalase and for the heat shock-induced accumulation of trehalose.","authors":"Franco A, Soto T, Madrid M, Vicente-Soler J, Gacto M, Cansado J","authors_abbrev":"Franco A et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-06-21","publication_year":"2005","canto_session_key":"b8bb1e848770c3be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-30 22:27:29","canto_approved_date":"2019-10-29 13:46:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 22:27:17","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.07","SPAC328.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-30"},{"uniquename":"PMID:9303312","title":"Control of S-phase periodic transcription in the fission yeast mitotic cycle.","citation":"EMBO J 1997 Aug 01;16(15):4676-88","abstract":"In fission yeast, passage through START and into S-phase requires cyclin-dependent kinase (CDK) activity and the periodic transcription of genes essential for S-phase ('S-phase transcription'). Here we investigate the control of this transcription in the mitotic cell cycle. We demonstrate that the periodicity of S-phase transcription is likely to be controlled independently of CDK activity. This contrasts with the equivalent system in budding yeast. Furthermore, the CDK function required for S-phase acts after the onset of S-phase transcription and after the accumulation of cdc18p, a critical target of this transcriptional machinery. We investigate the role of individual components of the S-phase transcriptional machinery, cdc10p, res1p, res2p and rep2p, and define a new role for res2p, previously demonstrated to be important in the meiotic cycle, in switching off S-phase transcription during G2 of the mitotic cycle. We show that the presence of the in vitro bandshift activity DSC1, conventionally thought to represent the active complex, requires res2p and correlates with inactive transcription. We suggest that S-phase transcription is controlled by both activation and repression, and that res2p represses transcription in G2 of the cell cycle as a part of the DSC1 complex.","authors":"Baum B, Wuarin J, Nurse P","authors_abbrev":"Baum B et al.","pubmed_publication_date":"01 Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"2467c1608e001a46","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-06-07 21:15:06","canto_approved_date":"2024-07-23 17:02:45","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-05-04 14:24:49","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":53,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.16","SPAC1F7.05","SPBC336.12c","SPBC11B10.09","SPBC14C8.07c","SPCC4E9.02","SPAC22F3.09c","SPAC24H6.05","SPAPB2B4.03","SPBC2F12.11c","SPBC582.03"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2018-06-07"},{"uniquename":"PMID:20300182","title":"Plasmid construction using recombination activity in the fission yeast Schizosaccharomyces pombe.","citation":"PLoS One 2010 Mar 11;5(3):e9652","abstract":"Construction of plasmids is crucial in modern genetic manipulation. As of now, the common method for constructing plasmids is to digest specific DNA sequences with restriction enzymes and to ligate the resulting DNA fragments with DNA ligase. Another potent method to construct plasmids, known as gap-repair cloning (GRC), is commonly used in the budding yeast Saccharomyces cerevisiae. GRC makes use of the homologous recombination activity that occurs within the yeast cells. Due to its flexible design and efficiency, GRC has been frequently used for constructing plasmids with complex structures as well as genome-wide plasmid collections. Although there have been reports indicating GRC feasibility in the fission yeast Schizosaccharomyces pombe, this species is not commonly used for GRC as systematic studies of reporting GRC efficiency in S. pombe have not been performed till date.\nWe investigated GRC efficiency in S. pombe in this study. We first showed that GRC was feasible in S. pombe by constructing a plasmid that contained the LEU2 auxotrophic marker gene in vivo and showed sufficient efficiency with short homology sequences (>25 bp). No preference was shown for the sequence length from the cut site in the vector plasmid. We next showed that plasmids could be constructed in a proper way using 3 DNA fragments with 70% efficiency without any specific selections being made. The GRC efficiency with 3 DNA fragments was dramatically increased >95% in lig4Delta mutant cell, where non-homologous end joining is deficient. Following this approach, we successfully constructed plasmid vectors with leu1+, ade6+, his5+, and lys1+ markers with the low-copy stable plasmid pDblet as a backbone by applying GRC in S. pombe.\nWe concluded that GRC was sufficiently feasible in S. pombe for genome-wide gene functional analysis as well as for regular plasmid construction. Plasmids with different markers constructed in this research are available from NBRP-yeast (http://yeast.lab.nig.ac.jp/).","doi":"10.1371/journal.pone.0009652","authors":"Chino A, Watanabe K, Moriya H","authors_abbrev":"Chino A et al.","pubmed_publication_date":"11 Mar 2010","pubmed_entrez_date":"2010-03-20","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42068117","title":"Cost-Effective Solid-State NMR Of Fungal Glucans: A Case Study On Schizosaccharomyces pombe.","citation":"Chemistry 2026 May 02;:e71081","abstract":"Solid-state NMR provides molecular-level insights into fungal cell walls, but full  13 C-enrichment is costly and limits biological replication. Here, we show that 10%  13 C-glucose labeling in Schizosaccharomyces pombe is sufficient to resolve the major carbohydrate resonances and quantify glucan composition with high reproducibility. We then examined cell wall composition at two temperatures, both in whole cells and in extracted wall fractions. Interestingly, whole cell spectra indicated minor, nonsignificant changes with temperature, while extracted walls revealed differences between the rigid glucan matrices with β-1,3-glucan especially enriched at 36          ∘    C    $^{\\circ }{\\rm C}$     . Together, these results establish low-level  13 C labeling as a cost-effective strategy for fungal solid-state NMR and highlight the complementary strengths of whole cell and extracted wall-level analysis in uncovering how the effect of elevated temperature is encoded in cell wall architecture.","doi":"10.1002/chem.71081","authors":"Singh A, Massam-Wu T, Balasubramanian M, Chow WY","authors_abbrev":"Singh A et al.","pubmed_publication_date":"02 May 2026","pubmed_entrez_date":"2026-05-02","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-05-02 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30501007","title":"Functional and structural characterization of a novel catechol-O-methyltransferase from Schizosaccharomyces pombe.","citation":"IUBMB Life 2019 Mar;71(3):330-339","abstract":"Catechol-O-methyltransferase (COMT 1  ) catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to various catechol substrates. COMTs play vital roles in physiological processes in animals, plants, and fungi, as well as bacteria, and have essential application values in industry. spCOMT is a probable COMT from Schizosaccharomyces pombe. It has an extraordinary intracellular distribution different from other homologs and would thus be predicted to perform a distinct physiological function. In this report, recombinant spCOMT was purified and kinetically characterized for the first time. The enzymology assays indicate that spCOMT is a metal-dependent enzyme and belongs to class I OMTs. In addition, the crystal structures of apo-spCOMT and SAM-complexed spCOMT were also presented, revealing that spCOMT possesses a conserved SAM-binding site and Mg 2+  pocket, but a distinct substrate pocket was not present in homologs. The mutagenesis ITC analysis revealed the SAM recognition characteristics of spCOMT. Based on all of the above findings, we speculated about the putative substrates' characteristics and the substrate recognition mechanisms of spCOMT. This work will help in elucidating the physiological functions of spCOMT in S. pombe. © 2018 IUBMB Life, 71(3):330-339, 2019.","doi":"10.1002/iub.1977","authors":"Wang Q, Teng M, Li X","authors_abbrev":"Wang Q et al.","pubmed_publication_date":"Mar 2019","pubmed_entrez_date":"2018-12-01","publication_year":"2019","canto_session_key":"27b9d6bc5aa14ffa","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-12-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15623550","title":"DNA replication origins in the Schizosaccharomyces pombe genome.","citation":"Proc Natl Acad Sci U S A 2005 Jan 11;102(2):337-42","abstract":"Origins of DNA replication in Schizosaccharomyces pombe lack a specific consensus sequence analogous to the Saccharomyces cerevisiae autonomously replicating sequence (ARS) consensus, raising the question of how they are recognized by the replication machinery. Because all well characterized S. pombe origins are located in intergenic regions, we analyzed the sequence properties and biological activity of such regions. The AT content of intergenes is very high ( approximately 70%), and runs of A's or T's occur with a significantly greater frequency than expected. Additionally, the two DNA strands in intergenes display compositional asymmetry that strongly correlates with the direction of transcription of flanking genes. Importantly, the sequence properties of known S. pombe origins of DNA replication are similar to those of intergenes in general. In functional studies, we assayed the in vivo origin activity of 26 intergenes in a 68-kb region of S. pombe chromosome 2. We also assayed the origin activity of sets of randomly chosen intergenes with the same length or AT content. Our data demonstrate that at least half of intergenes have potential origin activity and that the relative ability of an intergene to function as an origin is governed primarily by AT content and length. We propose a stochastic model for initiation of DNA replication in the fission yeast. In this model, the number of AT tracts in a given sequence is the major determinant of its probability of binding SpORC and serving as a replication origin. A similar model may explain some features of origins of DNA replication in metazoans.","authors":"Dai J, Chuang RY, Kelly TJ","authors_abbrev":"Dai J et al.","pubmed_publication_date":"11 Jan 2005","pubmed_entrez_date":"2004-12-30","publication_year":"2005","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33180846","title":"Topoisomerase activity is linked to altered nucleosome positioning and transcriptional regulation in the fission yeast fbp1 gene.","citation":"PLoS One 2020;15(11):e0242348","abstract":"Chromatin structure, including nucleosome positioning, has a fundamental role in transcriptional regulation through influencing protein-DNA interactions. DNA topology is known to influence chromatin structure, and in doing so, can also alter transcription. However, detailed mechanism(s) linking transcriptional regulation events to chromatin structure that is regulated by changes in DNA topology remain to be well defined. Here we demonstrate that nucleosome positioning and transcriptional output from the fission yeast fbp1 and prp3 genes are altered by excess topoisomerase activity. Given that lncRNAs (long noncoding RNAs) are transcribed from the fbp1 upstream region and are important for fbp1 gene expression, we hypothesized that local changes in DNA topological state caused by topoisomerase activity could alter lncRNA and fbp1 transcription. In support of this, we found that topoisomerase overexpression caused destabilization of positioned nucleosomes within the fbp1 promoter region, which was accompanied by aberrant fbp1 transcription. Similarly, the direct recruitment of topoisomerase, but not a catalytically inactive form, to the promoter region of fbp1 caused local changes in nucleosome positioning that was also accompanied by altered fbp1 transcription. These data indicate that changes in DNA topological state induced by topoisomerase activity could lead to altered fbp1 transcription through modulating nucleosome positioning.","doi":"10.1371/journal.pone.0242348","authors":"Asada R, Senmatsu S, Montpetit B, Hirota K","authors_abbrev":"Asada R et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-11-12","publication_year":"2020","canto_session_key":"c06905ef2cb5d9c2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-11-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9290054","title":"[Molecular cloning and characterization of cDNA of the rpc10+ gene encoding the smallest subunit of nuclear RNA polymerases of Schizosaccharomyces pombe].","citation":"Bioorg Khim 1997 May;23(5):441-8","abstract":"The full-length cDNA of the rpc10+ gene encoding mini-subunit Rpc10, which is common for all three nuclear RNA polymerases of the fission yeast Schizosaccharomyces pombe, was cloned and sequenced. The Rpc10 subunit of Sz. pombe and its homologs from S. cerevisiae and H. sapiens are positively charged proteins with a highly conserved C-terminal region and an invariant zinc-binding domain (Zn-finger) of a typical amino acid composition: YxCx2Cx12RCx2CGxR. Functional tests of heterospecific complementation, using tetrad analysis or plasmid shuffling, showed that the Rpc10 subunit of Sz. pombe can successfully replace the homologous ABC10 alpha subunit in nuclear RNA polymerases I-III of S. cerevisiae.","authors":"Shpakovskiĭ GV, Lebedenko EN","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"89fd82f771526fda","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-11 17:18:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 17:04:53","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-11"},{"uniquename":"PMID:17192851","title":"A flexible protein linker improves the function of epitope-tagged proteins in Saccharomyces cerevisiae.","citation":"Yeast 2007 Jan;24(1):39-45","abstract":"Epitope tagging permits the detection of proteins when protein-specific antibodies are not available. However, the epitope tag can reduce the function of the tagged protein. Here we describe a cassette that can be used to introduce an eight amino acid flexible linker between multiple Myc epitopes and the open reading frame of a given gene. We show that inserting the linker improves the in vivo ability of the telomerase subunits Est2p and Est1p to maintain telomere length. The methods used here are generally applicable to improve the function of tagged proteins in both Saccharomyces cerevisiae and Schizosaccharomyces pombe.","authors":"Sabourin M, Tuzon CT, Fisher TS, Zakian VA","authors_abbrev":"Sabourin M et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2006-12-29","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39446564","title":"Exploring the Roles of Lem2 and Bqt4 in Lipid Metabolism for Nuclear Envelope Maintenance: A Novel Perspective.","citation":"J Biochem 2024 Oct 24;","abstract":"The nuclear envelope (NE) is a double-membrane structure critical for genome maintenance and cellular function, composed of the inner and outer nuclear membranes. In fission yeast, the inner nuclear membrane (INM) proteins Lem2 and Bqt4 are essential for maintaining NE integrity. The study published by Hiraoka group (Hirano et al. 2023) explores the interactions between Lem2 and Bqt4 with lipid synthesis enzymes, addressing their roles in NE maintenance. The authors identified Lem2- and Bqt4-binding proteins using immunoprecipitation and mass spectrometry, revealing that Lem2 interacts with lipid synthesis enzymes, while Bqt4 binds to an enzyme that involves in glucosylceramide synthesis. These findings suggest that Lem2 and Bqt4 independently contribute to NE structure and its integrity through distinct lipid metabolic pathways, highlighting their complementary roles in nuclear membrane homeostasis. This study represents a significant step forward in the field of NE biology to unravel the complexities of nuclear membrane dynamics.","doi":"10.1093/jb/mvae072","authors":"Ishiguro KI","authors_abbrev":"Ishiguro KI","pubmed_publication_date":"24 Oct 2024","pubmed_entrez_date":"2024-10-24","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-10-24 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28281664","title":"Genetic interactions and functional analyses of the fission yeast gsk3 and amk2 single and double mutants defective in TORC1-dependent processes.","citation":"Sci Rep 2017 Mar 10;7:44257","abstract":"The Target of Rapamycin (TOR) signalling network plays important roles in aging and disease. The AMP-activated protein kinase (AMPK) and the Gsk3 kinase inhibit TOR during stress. We performed genetic interaction screens using synthetic genetic arrays (SGA) with gsk3 and amk2 as query mutants, the latter encoding the regulatory subunit of AMPK. We identified 69 negative and 82 positive common genetic interactors, with functions related to cellular growth and stress. The 120 gsk3-specific negative interactors included genes functioning in translation and ribosomes. The 215 amk2-specific negative interactors included genes functioning in chromatin silencing and DNA damage repair. Both amk2- and gsk3-specific interactors were enriched in phenotype categories related to abnormal cell size and shape. We also performed SGA screen with the amk2 gsk3 double mutant as a query. Mutants sensitive to 5-fluorouracil, an anticancer drug are under-represented within the 305 positive interactors specific for the amk2 gsk3 query. The triple-mutant SGA screen showed higher number of negative interactions than the double mutant SGA screens and uncovered additional genetic network information. These results reveal common and specialized roles of AMPK and Gsk3 in mediating TOR-dependent processes, indicating that AMPK and Gsk3 act in parallel to inhibit TOR function in fission yeast.","doi":"10.1038/srep44257","authors":"Rallis C, Townsend S, Bähler J","authors_abbrev":"Rallis C et al.","pubmed_publication_date":"10 Mar 2017","pubmed_entrez_date":"2017-03-11","publication_year":"2017","canto_session_key":"e80e3736b70fa4b5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"StJohn Townsend","canto_first_approved_date":"2021-05-11 16:11:59","canto_approved_date":"2021-05-12 08:02:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-07 09:18:28","canto_added_date":"2017-03-12 01:15:14","annotation_curators":[{"name":"StJohn Townsend","community_curator":true,"annotation_count":27,"orcid":"0000-0002-4745-7118","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.04","SPCC4G3.13c","SPAC1610.01","SPAC4A8.09c","SPBC1778.05c","SPBC354.03","SPCC1884.02","SPBC29A3.01","SPBC12C2.02c","SPAC13C5.05c","SPBC2G2.03c","SPAC3H8.02","SPAC30.02c","SPAC328.06","SPAC6F6.03c","SPCC569.06","SPCC1919.03c","SPBC215.08c","SPAC890.07c","SPAC343.09","SPBC530.11c","SPAC144.02","SPCC13B11.01","SPAC30C2.06c","SPCC18.10","SPBC1105.02c","SPBC1685.08","SPBC3B9.13c","SPAPB1E7.12","SPCC320.07c","SPAC17G6.05c","SPCC777.09c","SPAC9G1.06c","SPBC25B2.04c","SPBC1703.03c","SPBC15D4.07c","SPBC3H7.12","SPAC22E12.11c","SPBC354.14c","SPBC336.01","SPBC3B9.06c","SPAC9G1.02","SPAC3A12.13c","SPAPB1E7.06c","SPAC3H1.09c","SPBC36B7.02","SPAC27E2.01","SPAC3H1.08c","SPAC29B12.03","SPCC1795.01c","SPAC23C11.10","SPCC31H12.03c","SPBC14F5.11c","SPAC57A7.04c","SPAC644.15","SPBC14F5.10c","SPAC167.01","SPBC13A2.04c","SPAC7D4.12c","SPBC1604.08c","SPAPYUG7.02c","SPCC613.06","SPAC22F3.08c","SPCC584.01c","SPBC16A3.08c","SPBC106.02c","SPBC31F10.12","SPBC13G1.14c","SPBP8B7.24c","SPBP8B7.18c","SPAC959.04c","SPBC11B10.06","SPAC664.01c","SPBC14C8.16c","SPBC32F12.02","SPBC428.05c","SPAC343.04c","SPCC757.02c","SPBC1539.10","SPAC1250.02","SPAPB1A10.07c","SPAPJ760.03c","SPAC12G12.03","SPBC2D10.16","SPBC16A3.19","SPAC16E8.18","SPAC3A11.08","SPAC10F6.05c","SPAC4D7.03","SPBC21C3.07c","SPCC594.06c","SPAC19B12.06c","SPBC16E9.03c","SPBC1604.02c","SPAC664.02c","SPAC20H4.05c","SPBC18H10.11c","SPBC3H7.10","SPAC9G1.12","SPAC922.05c","SPCC1020.03","SPCC970.02","SPBC12D12.06","SPBC119.04","SPAC513.03","SPBC30B4.04c","SPBC4C3.12","SPAC1071.02","SPCC1259.11c","SPAC1834.05","SPCC1020.07","SPAC1296.02","SPBC27B12.10c","SPBC651.02","SPAC6G9.12","SPBC577.02","SPBC651.11c","SPAC31A2.12","SPCC18B5.03","SPCC777.13","SPAC17A5.09c","SPCC1672.06c","SPAC23D3.09","SPAC1F5.05c","SPBC16H5.13","SPAC144.03","SPAC212.04c","SPBC17D11.08","SPAC31G5.18c","SPCC1393.02c","SPAC3F10.11c","SPCC63.08c","SPCC613.03","SPBC31F10.07","SPBC13G1.08c","SPBC11G11.05","SPBC23G7.06c","SPCC548.04","SPBC13G1.12","SPBC16A3.03c","SPBC25H2.08c","SPBC21C3.14c","SPBC16A3.01","SPBC19F8.03c","SPCC553.04","SPBC800.03","SPBC32F12.01c","SPAC823.10c","SPCC777.07","SPAC17C9.05c","SPAC694.04c","SPBC691.04","SPAPB8E5.04c","SPAC23H4.10c","SPBC1718.03","SPCC1020.01c","SPAC19A8.05c","SPBC29A10.02","SPBC2G2.01c","SPAP27G11.08c","SPCC1259.02c","SPAC926.03","SPAPJ696.02","SPBC12D12.04c","SPAC1782.11","SPCC16C4.09","SPBC23G7.08c","SPAC17G6.04c","SPAC664.03","SPBC365.16","SPBC1734.12c","SPCC18B5.09c","SPAC1B3.03c","SPAC144.11","SPACUNK4.16c","SPAC25B8.17","SPAC1F5.08c","SPCC895.06","SPAC23E2.01","SPAC607.02c","SPAC11E3.08c","SPAC5D6.02c","SPAC13C5.03","SPBPB21E7.05","SPBC30B4.03c","SPBC2D10.13","SPBC1271.14","SPAC17C9.15c","SPBC1683.09c","SPAC227.18","SPAC1639.02c","SPAC227.01c","SPAC926.06c","SPBC11G11.02c","SPCC16A11.03c","SPAC13A11.01c","SPCC1442.02","SPBC17G9.02c","SPBC354.10","SPBC4.02c","SPAC13G7.03","SPAC1296.04","SPBC19F8.08","SPAC630.11","SPBC1734.06","SPBC29A3.03c","SPAPYUG7.06","SPAC13G6.03","SPCC1902.02","SPAC13G6.02c","SPAC15E1.06","SPBC3H7.09","SPBC354.04","SPCC736.11","SPAC11H11.01","SPCC320.03","SPBC1306.02","SPBC4F6.08c","SPAC9G1.07","SPAC23C11.02c","SPCC794.02","SPAPB2B4.02","SPBP8B7.11","SPAC1805.07c","SPAC1782.09c","SPBC1539.06","SPAC22H10.09","SPAC1F3.09","SPAC23H3.06","SPBC16D10.08c","SPBC2G5.02c","SPBC30D10.16","SPBC2G2.10c","SPAC144.06","SPBP4H10.13","SPBC15D4.10c","SPAC4H3.03c","SPBC1711.03","SPAPB17E12.08","SPBC1778.07","SPCC1259.09c","SPCPB16A4.06c","SPBP35G2.07","SPBC83.10","SPCC24B10.08c","SPAC18G6.10","SPAC2F7.17","SPBC215.02","SPBC651.03c","SPAC1142.03c","SPAC24C9.05c","SPCC1442.04c","SPBC106.10","SPCC1020.10","SPAC26F1.01","SPCC736.02","SPBC3B8.10c","SPBC8D2.02c","SPAC19G12.05","SPBC1685.04","SPAC1687.15","SPCC1393.08","SPBC1685.02c","SPAC9E9.08","SPAC9E9.09c","SPCC613.02","SPCC320.12","SPBC36.04","SPAC24H6.09","SPAC11E3.03","SPBC428.08c","SPBC409.19c","SPAC1F7.08","SPBC8D2.18c","SPBC405.04c","SPBC1604.20c","SPBC4F6.05c","SPBC337.16","SPAC8F11.02c","SPCC63.04","SPAC25B8.13c","SPCC737.09c","SPAC607.09c","SPBC12C2.09c","SPCC16A11.15c","SPBPB2B2.09c","SPCC970.05","SPBC16C6.06","SPBC19G7.18c","SPCC794.15","SPAC4G9.16c","SPBC1A4.04","SPAC823.03","SPBC215.03c","SPCC777.10c","SPAC6G10.11c","SPCC1223.11","SPCC895.09c","SPBC16A3.10","SPAC1556.02c","SPAC3G9.07c","SPAC13D6.03c","SPCC24B10.13","SPBC11C11.07","SPAC24H6.07","SPAC5H10.06c","SPBC12C2.03c","SPBC16A3.17c","SPCC1442.15c","SPCC1259.08","SPAC26A3.09c","SPAC6G9.14","SPAC14C4.16","SPBC25B2.08","SPAC18G6.02c","SPBC25H2.16c","SPAC31G5.17c","SPAC13A11.05","SPAC27D7.08c","SPBC1289.14","SPCC1235.11","SPCC162.12","SPCC1020.11c","SPBCPT2R1.08c","SPBC27B12.11c","SPBC83.03c","SPBC23G7.16","SPBC336.03","SPAC22F8.11","SPAC12B10.12c","SPAC17A5.07c","SPBC17G9.08c","SPBC31F10.14c","SPBC2G5.06c","SPAC27F1.08","SPAC7D4.03c","SPAC27E2.03c","SPAC1B3.16c","SPCC16A11.08","SPAC750.05c","SP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Assignment and Biological Evaluation of BE-14106 Unveils the Importance of One Acetate Unit for the Antifungal Activity of Polyene Macrolactams.","citation":"J Nat Prod 2016 Jul 22;79(7):1877-80","abstract":"Heronamides are a class of potent antifungal metabolites produced by marine-derived actinomycetes. The number of hydroxy groups and the stereochemistry of the two hydroxylated methine carbons are important for the activity of heronamide C, whereas the effect of the hydrocarbon chains is not known. In this study, the stereochemistry and the biological activity of BE-14106, another member of the heronamide class of antibiotics, isolated from an actinomycete Actinoalloteichus cyanogriseus IFM 11549 was investigated. Spectroscopic analysis coupled with photo- and O2-induced conversion revealed that BE-14106 and the heronamides had the same stereochemistry. BE-14106 showed potent growth inhibition against fission yeast cells with an MIC value of 0.50 μM (0.21 μg/mL), being 4 times less potent than heronamide C, which revealed the importance of the structure of the hydrocarbon tail for the activity.","doi":"10.1021/acs.jnatprod.6b00250","authors":"Fujita K, Sugiyama R, Nishimura S, Ishikawa N, Arai MA, Ishibashi M, Kakeya H","authors_abbrev":"Fujita K et al.","pubmed_publication_date":"22 Jul 2016","pubmed_entrez_date":"2016-06-23","publication_year":"2016","canto_session_key":"4b65f6ed0fc03f6b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-06-29 14:56:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-06-29 14:56:15","canto_added_date":"2016-06-24 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2016-06-29"},{"uniquename":"PMID:4355200","title":"Oligomycin resistance of mitochondrial adenosine triphosphatase in a pleiotropic chromosomal mutant of a \"petite-negative\" yeast, Schizosaccharomyces pombe.","citation":"J Biol Chem 1973 Oct 25;248(20):7097-105","abstract":"","authors":"Goffeau A, Landry Y, Foury F, Briquet M, Colson AM","authors_abbrev":"Goffeau A et al.","pubmed_publication_date":"25 Oct 1973","pubmed_entrez_date":"1973-10-25","publication_year":"1973","canto_session_key":"894801f4247ffc32","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-02-26 16:12:01","canto_approved_date":"2021-02-26 16:12:01","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-02-26 16:11:50","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2021-02-26"},{"uniquename":"PMID:2959907","title":"Resolution of DNA molecules greater than 5 megabases by contour-clamped homogeneous electric fields.","citation":"Nucleic Acids Res 1987 Oct 12;15(19):7865-76","abstract":"Excellent resolution of chromosomal DNA molecules from Saccharomyces cerevisiae, Candida albicans and Schizosaccharomyces pombe has been obtained using alternating contour-clamped homogeneous electric field (CHEF) gel electrophoresis. The largest of these molecules is greater than 5 Mb in size and is resolved after 130 hours in a 0.6% agarose gel at a field strength of 1.3 V/cm and a switching interval of 1 hour. Separation of concatamers of phage lambda DNA reveals four regions of resolution in alternating CHEF gel electrophoresis. There are two regions of good resolution in which mobility approximates a linear function of molecular weight. These are separated by a region of lower resolution and bounded at high molecular weights by a region of little or no resolution. The four regions are of practical and possibly theoretical importance.","authors":"Vollrath D, Davis RW","authors_abbrev":"Vollrath D et al.","pubmed_publication_date":"12 Oct 1987","pubmed_entrez_date":"1987-10-12","publication_year":"1987","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39527192","title":"Ultrastructure Expansion Microscopy (U-ExM) of the Fission Yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2025;2862:47-59","abstract":"Among widely used super-resolution microscopy techniques, including stimulated emission depletion (STED), photoactivated localization microscopy (PALM), and stochastic optical reconstruction microscopy (STORM), expansion microscopy (ExM) is unique in achieving increased resolution through a physical manipulation of the actual sample rather than optics or postprocessing. Originally developed for applications in neuroscience, ExM now has a solid foothold across many fields and model systems, and has been adapted to work for organisms with cell walls, including budding and fission yeasts, through the inclusion of a pre-expansion enzymatic digestion step. A variant of the ExM technique optimized for preserving the architecture of protein complexes, ultrastructure expansion microscopy (U-ExM), enables super-resolution imaging of full 3D volumes at increased throughput using conventional microscopes and can be readily combined with commonly used antibodies, dyes, and stains. Here, we present its application to the fission yeast Schizosaccharomyces pombe.","doi":"10.1007/978-1-0716-4168-2_4","authors":"Mikus F, Dey G","authors_abbrev":"Mikus F et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011801","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7628693","title":"p93dis1, which is required for sister chromatid separation, is a novel microtubule and spindle pole body-associating protein phosphorylated at the Cdc2 target sites.","citation":"Genes Dev 1995 Jul 01;9(13):1572-85","abstract":"Fission yeast cold-sensitive (cs) dis1 mutants are defective in sister chromatid separation. The dis1+ gene was isolated by chromosome walking. The null mutant showed the same phenotype as that of cs mutants. The dis1+ gene product was identified as a novel 93-kD protein, and its localization was determined by use of anti-dis1 antibodies and green fluorescent protein (GFP) tagged to the carboxyl end of p93dis1. The tagged p93dis1 in living cells localizes along cytoplasmic microtubule arrays in interphase and the elongating anaphase spindle in mitosis, but association with the short metaphase spindle microtubules is strikingly reduced. In the spindle, the tagged p93dis1 is enriched at the spindle pole bodies (SPBs). Time-lapse video images of single cells support the localization shift of p93dis1 to the SPBs in metaphase and spindle microtubules in anaphase. The carboxy-terminal fragment, which is essential for Dis1 function, accumulates around the mitotic SPB. We propose that these localization shifts of p93dis1 in mitosis facilitates sister chromatid separation by affecting SPB and anaphase spindle function.","authors":"Nabeshima K, Kurooka H, Takeuchi M, Kinoshita K, Nakaseko Y, Yanagida M","authors_abbrev":"Nabeshima K et al.","pubmed_publication_date":"01 Jul 1995","pubmed_entrez_date":"1995-07-01","publication_year":"1995","canto_session_key":"5e794b46834f6222","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-03-07 15:55:16","canto_approved_date":"2021-11-07 19:48:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-30 18:33:47","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.14","SPBC776.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-03-07"},{"uniquename":"PMID:1842344","title":"The substrates of the cdc2 kinase.","citation":"Semin Cell Biol 1991 Aug;2(4):261-70","abstract":"The eukaryotic cell cycle is characterized by two major events, DNA replication (S phase) and mitosis (M phase). According to the current paradigm of the cell cycle as a cdc2 cycle, both of these events are driven by serine-threonine specific protein kinases encoded by functional homologs of the fission yeast cdc2 gene. To understand how cdc2 kinases function, it is necessary to identify their physiological substrates and to determine how phosphorylation of these substrates promotes cell cycle progression. Definitive information about substrates relevant to early stages of the cell cycle (G1 and S phases) remains scarce, but several likely physiological targets of the mitotic cdc2 kinase have recently been identified. Current evidence indicates that cdc2 kinase may trigger entry of cells into mitosis not only by initiating important regulatory pathways but also by direct phosphorylation of abundant structural proteins.","authors":"Nigg EA","authors_abbrev":"Nigg EA","pubmed_publication_date":"Aug 1991","pubmed_entrez_date":"1991-08-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41227381","title":"The  BUD31  Homologous Gene in  Schizosaccharomyces pombe  Is Evolutionarily Conserved and Can Be Linked to Cellular Processes Regulated by the TOR Pathway.","citation":"Cells 2025 Nov 05;14(21)","abstract":"The human  BUD31  gene has been associated with various processes including cancer. To better understand its function, we used genetic methods to study  Schizosaccharomyces pombe  cells lacking the  BUD31  homologous gene ( cwf14 ) and performed sequence analysis using bioinformatics methods. Mutant cells lacking the  cwf14  gene showed cell size and division defects, altered stress response, rapamycin sensitivity, enhanced chronological aging, and increased sporulation tendency. These processes are known to be regulated by the TOR pathway. The  cwf14 -TOR link was also supported by further experiments. We demonstrated that most protein-coding genes affected by  cwf14  deletion are upregulated, encode hydrolases, oxidoreductases, and are often involved in transport. GO enrichment drew our attention to genes related to nitrogen transport, while additional data pointed to a nutrient/nitrogen (N) sensing problem. Although Cwf14 protein is associated with spliceosome complex, most genes affected by the absence of  cwf14  do not contain introns, suggesting that they are influenced indirectly by the  cwf14  gene. In silico experiments have revealed that  BUD31  orthologous genes are found from yeast to humans, are evolutionarily conserved with a high degree of sequence identity, conserved motifs, and structures. Since the human gene partially complemented the mutant phenotype of  S. pombe  cells, indicating functional homology, our data can help better understand pathological mechanisms observed in human cancer cells.","doi":"10.3390/cells14211736","authors":"Vig I, Acs-Szabo L, Benkő Z, Bagelova Polakova S, Papp LA, Gregan J, Miklós I","authors_abbrev":"Vig I et al.","pubmed_publication_date":"05 Nov 2025","pubmed_entrez_date":"2025-11-13","publication_year":"2025","canto_session_key":"3643245a806aa41f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-01-23 10:45:59","canto_approved_date":"2026-01-23 10:45:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-01-22 09:47:04","canto_added_date":"2025-11-14 00:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.07c","SPBC24C6.11","SPBC30D10.10c","SPAC1142.08"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2026-01-23"},{"uniquename":"PMID:15601865","title":"Structural and functional analysis of essential pre-mRNA splicing factor Prp19p.","citation":"Mol Cell Biol 2005 Jan;25(1):451-60","abstract":"U-box-containing Prp19p is an integral component of the Prp19p-associated complex (the nineteen complex, or NTC) that is essential for activation of the spliceosome. Prp19p makes numerous protein-protein contacts with other NTC components and is required for NTC stability. Here we show that Prp19p forms a tetramer in vitro and in vivo and we map the domain required for its oligomerization to a central tetrameric coiled-coil. Biochemical and in vivo analyses are consistent with Prp19p tetramerization providing an interaction surface for a single copy of its binding partner, Cef1p. Electron microscopy showed that the isolated Prp19p tetramer is an elongated particle consisting of four globular WD40 domains held together by a central stalk consisting of four N-terminal U-boxes and four coiled-coils. These structural and functional data provide a basis for understanding the role of Prp19p as a key architectural component of the NTC.","authors":"Ohi MD, Vander Kooi CW, Rosenberg JA, Ren L, Hirsch JP, Chazin WJ, Walz T, Gould KL","authors_abbrev":"Ohi MD et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-12-17","publication_year":"2005","canto_session_key":"7eac5353ab8b141d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-03 16:28:05","canto_approved_date":"2023-09-25 17:10:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-03 16:27:58","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29A4.08c","SPAC644.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-07-03"},{"uniquename":"PMID:12050150","title":"Physical interaction between recombinational proteins Rhp51 and Rad22 in Schizosaccharomyces pombe.","citation":"J Biol Chem 2002 Aug 16;277(33):30264-70","abstract":"In eukaryotes, Rad51 and Rad52 are two key components of homologous recombination and recombinational repair. These two proteins interact with each other. Here we investigated the role of interaction between Rhp51 and Rad22, the fission yeast homologs of Rad51 and Rad52, respectively, on the function of each protein. We identified a direct association between the two proteins and their self-interactions both in vivo and in vitro. We also determined the binding domains of each protein that mediate these interactions. To characterize the role of Rhp51-Rad22 interaction, we used random mutagenesis to identify the mutants Rhp51 and Rad22, which cannot interact each other. Interestingly, we found that mutant Rhp51 protein, which cannot interact with either Rad22 or Rti1 (G282D), lost its DNA repair ability. In contrast, mutant Rad22 proteins, which cannot specifically bind to Rhp51 (S379L and P381L), maintained their DNA repair ability. These results suggest that the interaction between Rhp51 and Rad22 is crucial for the recombinational repair function of Rhp51. However, the significance of this interaction on the function of Rad22 remains to be characterized further.","authors":"Kim WJ, Park EJ, Lee H, Seong RH, Park SD","authors_abbrev":"Kim WJ et al.","pubmed_publication_date":"16 Aug 2002","pubmed_entrez_date":"2002-06-07","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC30D11.10"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11950879","title":"Control of localization of a spindle checkpoint protein, Mad2, in fission yeast.","citation":"J Cell Sci 2002 Apr 15;115(Pt 8):1603-10","abstract":"To ensure accurate chromosome segregation, the spindle checkpoint delays the onset of sister chromatid separation when the spindle is not attached to a kinetochore. Mad2, a component of the checkpoint, targets fission yeast Slp1/budding yeast Cdc20/human p55CDC and prevents it from promoting proteolysis, which is a prerequisite to sister chromatid separation. The protein is localized to unattached kinetochores in higher eukaryotes, and it is thought to be required for activation of the checkpoint as well. In this study, Mad2 and its target Slp1 were visualized in a tractable organism, fission yeast Schizosaccharomyces pombe. When cells were arrested at a prometaphase-like stage, the Mad2-Slp1 complex was stable and the two proteins were colocalized to unattached kinetochores. When the spindle attachment was completed, the complex was no longer detectable and only Mad2 was found associated to the spindle. These results would suggest that unattached kinetochores provide sites for assembly of the Mad2-Slp1 complex. During interphase, Mad2 was localized to the nuclear periphery as well as to the chromatin domain. This localization was abolished in a yeast strain lacking Mad1, a protein that physically interacts with Mad2. Mad1 may anchor Mad2 to the nuclear membrane and regulate its entry into the nucleus.","authors":"Ikui AE, Furuya K, Yanagida M, Matsumoto T","authors_abbrev":"Ikui AE et al.","pubmed_publication_date":"15 Apr 2002","pubmed_entrez_date":"2002-04-16","publication_year":"2002","canto_session_key":"2d9b10ae9f560c52","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-09-14 16:51:55","canto_approved_date":"2024-11-29 07:39:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-18 09:01:54","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.08c","SPBC106.09","SPBC3D6.04c","SPAC25G10.07c","SPBC26H8.07c","SPAC17C9.01c","SPBC20F10.06"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-09-14"},{"uniquename":"PMID:11156975","title":"Characterization of rec7, an early meiotic recombination gene in Schizosaccharomyces pombe.","citation":"Genetics 2001 Feb;157(2):519-32","abstract":"rec7 is involved in intra- and intergenic meiotic recombination in all tested regions of the genome of the fission yeast Schizosaccharomyces pombe. Segregational analysis in a rec7 gene disruption mutant revealed frequent occurrence of two-spored asci. Spores giving rise to diploid colonies were shown to derive from skipping of the second meiotic division. Nondisjunction of homologous chromosomes at the first meiotic division was also frequent. The cytological structures and processes, such as formation of linear elements, pairing of homologous chromosomes, and clustering of telomeres and centromeres, are regular in the mutant. Northern blot experiments revealed meiosis-specific expression of rec7. Screening of a meiotic cDNA library also identified transcripts from the opposite strand in the rec7 region. A Rec7-GFP fusion protein was localized in the nucleus of whole cells before karyogamy, during prophase, and after meiosis I. On spreads of prophase nuclei approximately 50 foci of Rec7-GFP were counted. Some of the observed phenotypes of the disruption mutant and the N-terminal sequence homology suggest that Rec7p is a functional homolog of Rec114p of Saccharomyces cerevisiae. The observed phenotypes of the disruption and the appearance of Rec7-GFP in mating haploid cells and after meiosis I are consistent with Rec7p functions before, during, and after meiotic prophase.","authors":"Molnar M, Parisi S, Kakihara Y, Nojima H, Yamamoto A, Hiraoka Y, Bozsik A, Sipiczki M, Kohli J","authors_abbrev":"Molnar M et al.","pubmed_publication_date":"Feb 2001","pubmed_entrez_date":"2001-02-07","publication_year":"2001","canto_session_key":"ebada95bbfff8409","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-07-13 14:41:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-13 14:41:40","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.131","SPCC1753.03c","SPNCRNA.132","SPNCRNA.69"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2015-07-13"},{"uniquename":"PMID:40716740","title":"TORC2 and MAPK signaling pathways regulate mitochondrial degradation induced by iron starvation in Schizosaccharomyces pombe.","citation":"J Biol Chem 2025 Jul 25;:110524","abstract":"Iron is essential for life as it participates in metabolic processes, including DNA synthesis, respiration, and photosynthesis. In this study, we show that iron starvation induced by 2,2'-dithiodipyl (DIP) causes mitochondrial dysfunction, impairs mitochondrial function, including mitochondrial membrane potential (ΔΨ m ) and respiration, and induces mitochondrial degradation in the vacuole of Schizosaccharomyces pombe. The DIP-induced mitochondrial degradation is independent of components of the core autophagy machinery and the ESCRT machinery examined here. We demonstrate that the target of rapamycin complex 2 (TORC2) and its sole target, the AGC kinase Gad8, and the mitogen-activated protein kinase (MAPK) Sty1 play positive roles in regulating iron starvation-induced mitochondrial degradation. The reduction in the level of mitochondrial degradation in Δgad8 cells could be restored to wild-type-like levels by treating Δgad8 cells with chloramphenicol (CAP) and NaN 3 , two inhibitors of mitochondrial respiration, and by deleting genes, encoding components important for mitochondrial electron transport chain (ETC). Disruption of Ca 2+  signaling through deletion of genes encoding the Ca 2+  channel proteins Yam8 and Cch1 and the regulatory subunit of calcineurin Cnb1 also restored mitochondrial degradation in Δgad8 cells. Our results suggest that the Sty1 MAPK participates with TORC2-Gad8 signaling in regulating DIP-induced mitochondrial degradation. Our results also suggest that TORC2-Gad8 signaling regulates iron starvation-induced mitochondrial degradation through regulation of mitochondrial respiration and Ca 2+  signaling.","doi":"10.1016/j.jbc.2025.110524","authors":"Li R, Shang J, Huang Y","authors_abbrev":"Li R et al.","pubmed_publication_date":"25 Jul 2025","pubmed_entrez_date":"2025-07-27","publication_year":"2025","canto_session_key":"7d5f11132a2d99b8","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-29 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9211982","title":"Ultrastructural changes in the Schizosaccharomyces pombe nucleolus following the disruption of the gar2+ gene, which encodes a nucleolar protein structurally related to nucleolin.","citation":"Chromosoma 1997 Jun;105(7-8):542-52","abstract":"The nucleolar protein gar2, from the fission yeast Schizosaccharomyces pombe, is the functional homolog of NSR1 from Saccharomyces cerevisiae, and is structurally related to nucleolin from vertebrates. By immunocytochemistry at the electron microscope level, we show that gar2 co-localizes with RNA polymerase I and the gar1 protein along the dense fibrillar component of the nucleolus in a wild-type strain of S. pombe, suggesting that gar2 is involved in the transcription and/or in the early steps of maturation of the ribosomal RNAs. Since the effects of disruption of the gar2+ gene might also shed light on the role of the gar2 protein, we analyzed the ultrastructure of the nucleolus of a gar2-disruption mutant. The nucleolus of the gar2- mutant is dramatically reorganized when compared with that of the wild-type gar2+ strain: a truncated protein containing the NH2-terminus of the gar2 protein is accumulated in an unusual nucleolar \"dense body\". Our results also suggest that the NH2-terminus might be sufficient for nucleolar localization via interaction with specific nucleolar components and support the hypothesis that gar2 in wild-type S. pombe interacts with nascent pre-rRNA via its two RNA-binding domains in combination with the glycine/arginine-rich domain. We also report that disruption of the gar2+ gene results in a mutant that is defective in cytokinesis and nuclear division.","authors":"Léger-Silvestre I, Gulli MP, Noaillac-Depeyre J, Faubladier M, Sicard H, Caizergues-Ferrer M, Gas N","authors_abbrev":"Léger-Silvestre I et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"cbaaa61496b71364","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-05-08 10:58:17","canto_approved_date":"2025-02-25 14:46:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-19 12:14:22","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC140.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-05-08"},{"uniquename":"PMID:17428646","title":"Solubilization and characterization of a cell wall-bound trehalase from ascospores of the fission yeast Schizosaccharomyces pombe.","citation":"Microbiol Res 2009;164(3):304-11","abstract":"The genome of the fission yeast Schizosaccharomyces pombe lacks sequence homologs to ath1 genes coding for acid trehalases in other yeasts or filamentous fungi. However, acid trehalase activity is present at the spore stage in the life cycle of the fission yeast. The enzyme responsible for this activity behaves as a surface enzyme covalently linked to the spore cell walls in both wild-type and ntp1 mutant strains devoid of neutral trehalase. Lytic treatment of particulated cell wall fractions allowed the solubilization of the enzyme into an active form. We have characterized this soluble enzyme and found that its kinetic parameters, optimum pH and temperature, thermal denaturation and salt responses are closely similar to other conventional acid trehalases. Hence, this rather unusual enzyme can be recognized as acid trehalase by its biochemical properties although it does not share genetic homology with other known acid trehalases. The potential role of such acid trehalase in the mobilization of trehalose is discussed.","authors":"Vicente-Soler J, Soto T, Madrid M, Núñez A, Cansado J, Gacto M","authors_abbrev":"Vicente-Soler J et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2007-04-13","publication_year":"2009","canto_session_key":"4b3cc8104329f094","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-31 15:38:16","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-31 15:38:10","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-03-31"},{"uniquename":"PMID:16819157","title":"Involvement of Moc1 in sexual development and survival of Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2006 Jul;70(7):1740-9","abstract":"The moc1 gene in Schizosaccharomyces pombe was found as to overcome sterility caused by high expression of adenylyl cyclase. The moc1 gene was found to be identical with sds23 and psp1. Although psp1 has been reported to be essential for growth, sds23 has not been. To clarify this apparent discrepancy, we first assessed independently the phenotypes of the moc1 disruptant. We confirmed that the deletion mutant of moc1 is sterile, sensitive to high salt, and grows slowly at higher and lower temperatures, and that mutant cells are elongated. Besides these phenotypes, we found that viability of the moc1 disruptant was rapidly lost at the stationary phase. We confirmed that the Moc1 protein is phosphorylated in the stationary phase and also under nitrogen-starved conditions. We examined the significance of this phosphorylation of Moc1 by creating the S333A or S333D mutant Moc1. Interestingly, while S333D mutant Moc1 is lower in inducing sexual development, S333A mutant Moc1 is higher in this than the wild type, suggesting that phosphorylation of Moc1 affects sexual development. The other phenotypes, such as sensitivity to high salt and higher temperature and elongation of cells, were not affected by mutation of S333A nor S333D. We found that Moc1-GFP localized to both the cytosol and the nucleus during mitotic growth, but accumulated in the nucleus in mating cells and then enriched in spores, and that this localization shift was negatively regulated by the cAMP pathway. This and the observations above suggest that nuclear localized Moc1 is an inducer of sexual development. Thus, in addition to the roles of moc1/sds23/psp1 in mitosis and stress response, it is also important for the survival and sexual development of fission yeast, but phosphorylation of Moc1 only affects the sexual development.","authors":"Yakura M, Ishikura Y, Adachi Y, Kawamukai M","authors_abbrev":"Yakura M et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-07-05","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC646.13"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:35289847","title":"A vacuolar membrane protein Vsb1p contributes to the vacuolar compartmentalization of basic amino acids in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2022 May 24;86(6):763-769","abstract":"Accumulation levels of Arg, Lys, and His in vacuoles of Schizosaccharomyces pombe cells were drastically decreased by the disruption of SPAC24H6.11c (vsb1+) gene identified by a homology search with the VSB1 gene of Saccharomyces cerevisiae. The Vsb1p fused with green fluorescent protein particularly localized at vacuolar membranes in S. pombe cells. Overexpression of vsb1+ markedly increased vacuolar levels of basic amino acids; however, overexpression of the vsb1D174A mutant did not affect the levels of these amino acids. These results suggest that the vsb1+ contributes to the accumulation of basic amino acids into the vacuoles of S. pombe, and the aspartate residue in the putative first transmembrane domain conserved among fungal homologs is crucial for the function of Vsb1p.","doi":"10.1093/bbb/zbac041","authors":"Ohnishi S, Kawano-Kawada M, Yamamoto Y, Akiyama K, Sekito T","authors_abbrev":"Ohnishi S et al.","pubmed_publication_date":"24 May 2022","pubmed_entrez_date":"2022-03-15","publication_year":"2022","canto_session_key":"d3dd600a0d523fcc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-03-17 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.11c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:20576575","title":"Design, synthesis, and docking of highly hypolipidemic agents: Schizosaccharomyces pombe as a new model for evaluating alpha-asarone-based HMG-CoA reductase inhibitors.","citation":"Bioorg Med Chem 2010 Jun 15;18(12):4238-48","abstract":"A series of alpha-asarone-based analogues was designed by conducting docking experiments with published crystal structures of human HMG-CoA reductase. Indeed, synthesis and evaluation of this series showed a highly hypocholesterolemic in vivo activity in a murine model, as predicted by previous docking studies. In agreement with this model, the polar groups attached to the benzene ring could play a key role in the enzyme binding and probably also in its biological activity, mimicking the HMG-moiety of the natural substrate. The hypolipidemic action mechanism of these compounds was investigated by developing a simple, efficient, and novel model for determining HMG-CoA reductase inhibition. The partial purification of the enzyme from Schizosaccharomyces pombe allowed for testing of alpha-asarone- and fibrate-based analogues, resulting in positive and significant inhibitory activity.","doi":"10.1016/j.bmc.2010.04.096","authors":"Argüelles N, Sánchez-Sandoval E, Mendieta A, Villa-Tanaca L, Garduño-Siciliano L, Jiménez F, Cruz Mdel C, Medina-Franco JL, Chamorro-Cevallos G, Tamariz J","authors_abbrev":"Argüelles N et al.","pubmed_publication_date":"15 Jun 2010","pubmed_entrez_date":"2010-06-26","publication_year":"2010","canto_session_key":"cb9c73e25b3add19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-05 14:55:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 14:54:59","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC162.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-05"},{"uniquename":"PMID:34085593","title":"Multiplexed suppression of TOR complex 1 induces autophagy during starvation.","citation":"Autophagy 2021 Jul;17(7):1794-1795","abstract":"Target of rapamycin complex 1 (TORC1) promotes cellular anabolism and suppresses macroautophagy/autophagy. In mammalian cells starved of amino acid, the GATOR1 complex, a negative regulator of TORC1, is released from its inhibitor GATOR2 and inactivates TORC1. We have recently identified the evolutionarily conserved GATOR2 components in fission yeast including Sea3, an ortholog of mammalian WDR59, but, unexpectedly, Sea3 acts as a part of GATOR1 to suppress TORC1. Moreover, fission yeast GATOR1 is not required for the amino-acid starvation-induced TORC1 attenuation, which is instead mediated by the Gcn2 pathway. Conversely, absence of a nitrogen source suppresses TORC1 in a manner dependent on GATOR1 as well as the Tsc1-Tsc2 complex, whose mammalian equivalent functions as a growth-factor sensitive TORC1 inhibitor. Thus, the evolutionarily conserved signaling modules are utilized differently between fission yeast and mammals to control TORC1 activity and autophagy.","doi":"10.1080/15548627.2021.1938915","authors":"Fukuda T, Shiozaki K","authors_abbrev":"Fukuda T et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-06-04","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-06-06 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC36B7.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24340529","title":"Rad52 protein function study by fluorescence tagging.","citation":"Rev Med Chir Soc Med Nat Iasi 2013;117(2):444-9","abstract":"Rad52 protein plays a significant role in DNA lesions repair by homologous recombination in eukariotic cells. Human Rad52 function somewhat overlaps with BRCA2 and has a role in cell survival in the absence of BRCA1-BRCA2 mediated recombination. Additional Rad52 function analysis and intracellular localization studies are probably necessary. We present a method for Rad22 protein tagging, a Schizosaccharomyces pombe Rad52 homologue, by Crerecombinase-mediated cassette exchange (RMCE) using the versatile pAW8 plasmid. Rad22 protein was C-termini yEGFP tagged; the resulting strain was analyzed by fluorescence microscopy. The yEGFP signal was observed (Rad22 foci) for 7.5 microM camptothecin, 0.005% methyl methanesulfonate, and 4 mM hydroxyurea treated cells. The RMCE method was efficient, and the presence of tagged Rad22 protein was confirmed by Western-Blot and fluorescence microscopy.","authors":"Bordeianu G, Petrescu-Danila E, Ungureanu D, Stoica B, Stanescu R, Cernomaz A, Rusu M","authors_abbrev":"Bordeianu G et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-12-18","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8168486","title":"A zinc finger protein controls the onset of premeiotic DNA synthesis of fission yeast in a Mei2-independent cascade.","citation":"EMBO J 1994 Apr 15;13(8):1881-7","abstract":"In the fission yeast Schizosaccharomyces pombe, meiosis is initiated by the action of Mei2 in a complex cascade activated following conjugation. We have isolated a new gene named rep1+ that is required for the initiation of premeiotic DNA synthesis. rep1+ encodes a 53 kDa protein with one zinc finger motif that is essential for function, and effectively rescues a null mutant of the res1+ gene but only partially a temperature-sensitive mutant of the cdc10+ gene, both of which are required for the onset of mitotic, as well as premeiotic, S phase. Deletion of rep1+ has no apparent effects on the mitotic cell cycle or conjugation, but blocks the initiation of premeiotic DNA synthesis. However, this defect is partially suppressed when rapidly growing cells are induced to conjugate, indicating that the rep1+ function is at least partly substituted by those of the genes controlling the 'start' of the mitotic cell cycle. The rep1 null mutant fails to induce the res2+ gene, a newly identified res1+ homolog cooperating with Cdc10 and acting for the onset of mitotic and premeiotic DNA synthesis, as well as for meiotic division. The rep1+ gene itself is induced moderately during nitrogen starvation but highly during conjugation, and this induction is dependent on both ste11+ and mating pheromones but independent of mei2+. Thus, rep1+ controls the initiation of premeiotic DNA synthesis via induction and/or activation of Res2 and some other essential factors in a cascade independent of Mei2.","authors":"Sugiyama A, Tanaka K, Okazaki K, Nojima H, Okayama H","authors_abbrev":"Sugiyama A et al.","pubmed_publication_date":"15 Apr 1994","pubmed_entrez_date":"1994-04-15","publication_year":"1994","canto_session_key":"09631fcd6f5087f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-25 16:26:59","canto_approved_date":"2023-03-15 20:12:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-09 17:48:21","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.06","SPAC22F3.09c","SPBC336.12c","SPAC27D7.03c","SPAC23H3.13c","SPBC32C12.02","SPBC725.16"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2019-01-25"},{"uniquename":"PMID:8299939","title":"Region-specific activators of meiotic recombination in Schizosaccharomyces pombe.","citation":"Genes Dev 1994 Jan;8(2):203-10","abstract":"Schizosaccharomyces pombe rec mutants were previously isolated on the basis of their deficiency in meiotic recombination at the ade6 locus. We surveyed their meiotic recombination deficiencies at and between other loci. In rec10 mutants recombinant frequencies in the approximately 2-Mb region surrounding the ade6 locus were reduced 10- to 100-fold, but recombinant frequencies at or between nine other unlinked loci were reduced < 3-fold. The rec10 mutations are recessive and are on chromosome I; the ade6 region is on chromosome III. These results indicate that the rec10 gene product is required for activation of meiotic recombination in the approximately 2-Mb region surrounding ade6 but not in the other regions surveyed. Similar ade6 regional specificities were observed for rec8 and rec11. We infer that there are multiple activators of meiotic recombination, each specific for a limited set of loci, and we discuss how these regional activators may work.","authors":"DeVeaux LC, Smith GR","authors_abbrev":"DeVeaux LC et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_session_key":"539cf73d35899f8b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-30 12:25:59","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-29 14:00:12","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPCC1322.13","SPAC25G10.04c","SPCC1753.03c","SPCC4E9.01c","SPBC21B10.12"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2014-07-29"},{"uniquename":"PMID:34731638","title":"The histone chaperone FACT facilitates heterochromatin spreading by regulating histone turnover and H3K9 methylation states.","citation":"Cell Rep 2021 Nov 02;37(5):109944","abstract":"Heterochromatin formation requires three distinct steps: nucleation, self-propagation (spreading) along the chromosome, and faithful maintenance after each replication cycle. Impeding any of those steps induces heterochromatin defects and improper gene expression. The essential histone chaperone FACT (facilitates chromatin transcription) has been implicated in heterochromatin silencing, but the mechanisms by which FACT engages in this process remain opaque. Here, we pinpoint its function to the heterochromatin spreading process in fission yeast. FACT impairment reduces nucleation-distal H3K9me3 and HP1/Swi6 accumulation at subtelomeres and derepresses genes in the vicinity of heterochromatin boundaries. FACT promotes spreading by repressing heterochromatic histone turnover, which is crucial for the H3K9me2 to me3 transition that enables spreading. FACT mutant spreading defects are suppressed by removal of the H3K9 methylation antagonist Epe1. Together, our study identifies FACT as a histone chaperone that promotes heterochromatin spreading and lends support to the model that regulated histone turnover controls the propagation of repressive methylation marks.","doi":"10.1016/j.celrep.2021.109944","authors":"Murawska M, Greenstein RA, Schauer T, Olsen KCF, Ng H, Ladurner AG, Al-Sady B, Braun S","authors_abbrev":"Murawska M et al.","pubmed_publication_date":"02 Nov 2021","pubmed_entrez_date":"2021-11-03","publication_year":"2021","canto_session_key":"48003915c37d2609","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Magdalena Murawska","canto_first_approved_date":"2021-12-07 17:21:18","canto_approved_date":"2026-01-30 12:58:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-11-24 15:58:50","canto_added_date":"2021-11-05 01:15:04","annotation_curators":[{"name":"Magdalena Murawska","community_curator":true,"annotation_count":45,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25A8.01c","SPBC8D2.04","SPBC609.05","SPBC800.03","SPBP8B7.19","SPBC1105.11c","SPCC622.16c","SPBC428.08c","SPAC664.01c","SPBC13E7.08c","SPAC22F3.09c","SPAC1834.04","SPAC664.03","SPAC17G8.13c"],"gene_count":14,"ltp_gene_count":10,"approved_date":"2021-12-07"},{"uniquename":"PMID:25330182","title":"Characterization of the nuclear import mechanism of the CCAAT-regulatory subunit Php4.","citation":"PLoS One 2014;9(10):e110721","abstract":"Php4 is a nucleo-cytoplasmic shuttling protein that accumulates in the nucleus during iron deficiency. When present in the nucleus, Php4 associates with the CCAAT-binding protein complex and represses genes encoding iron-using proteins. Here, we show that nuclear import of Php4 is independent of the other subunits of the CCAAT-binding complex. Php4 nuclear import relies on two functionally independent nuclear localization sequences (NLSs) that are located between amino acid residues 171 to 174 (KRIR) and 234 to 240 (KSVKRVR). Specific substitutions of basic amino acid residues to alanines within these sequences are sufficient to abrogate nuclear targeting of Php4. The two NLSs are biologically redundant and are sufficient to target a heterologous reporter protein to the nucleus. Under low-iron conditions, a functional GFP-Php4 protein is only partly targeted to the nucleus in imp1Δ and sal3Δ mutant cells. We further found that cells expressing a temperature-sensitive mutation in cut15 exhibit increased cytosolic accumulation of Php4 at the nonpermissive temperature. Further analysis by pull-down experiments revealed that Php4 is a cargo of the karyopherins Imp1, Cut15 and Sal3. Collectively, these results indicate that Php4 can be bound by distinct karyopherins, connecting it into more than one nuclear import pathway.","doi":"10.1371/journal.pone.0110721","authors":"Khan MG, Jacques JF, Beaudoin J, Labbé S","authors_abbrev":"Khan MG et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-10-21","publication_year":"2014","canto_session_key":"afd6e918c42cd94a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-12-24 01:27:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1840.03","SPBC16E9.01c","SPBC1604.08c","SPCC962.03c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:11255251","title":"In situ localization of beta-glucans in the cell wall of Schizosaccharomyces pombe.","citation":"Yeast 2001 Mar 30;18(5):433-44","abstract":"The chemical composition of the cell wall of Sz. pombe is known as beta-1,3-glucan, beta-1,6-glucan, alpha-1,3-glucan and alpha-galactomannan; however, the three-dimensional interactions of those macromolecules have not yet been clarified. Transmission electron microscopy reveals a three-layered structure: the outer layer is electron-dense, the adjacent layer is less dense, and the third layer bordering the cell membrane is dense. In intact cells of Sz. pombe, the high-resolution scanning electron microscope reveals a surface completely filled with alpha-galactomannan particles. To better understand the organization of the cell wall and to complement our previous studies, we set out to locate the three different types of beta-glucan by immuno-electron microscopy. Our results suggest that the less dense layer of the cell wall contains mainly beta-1,6-branched beta-1,3-glucan. Occasionally a line of gold particles can be seen, labelling fine filaments radiating from the cell membrane to the alpha-galactomannan layer, suggesting that some of the radial filaments contain beta-1,6-branched beta-1,3-glucan. beta-1,6-glucan is preferentially located underneath the alpha-galactomannan layer. Linear beta-1,3-glucan is exclusively located in the primary septum of dividing cells. beta-1,6-glucan only labels the secondary septum and does not co-localize with linear beta-1,3-glucan, while beta-1,6-branched beta-1,3-glucan is present in both septa. Linear beta-1,3-glucan is present from early stages of septum formation and persists until the septum is completely formed; then just before cell division the label disappears. From these results we suggest that linear beta-1,3-glucan is involved in septum formation and perhaps the separation of the two daughter cells. In addition, we frequently found beta-1,6-glucan label on the Golgi apparatus, on small vesicles and underneath the cell membrane. These results give fresh evidence for the hypothesis that beta-1,6-glucan is synthesized in the endoplasmic reticulum-Golgi system and exported to the cell membrane.","authors":"Humbel BM, Konomi M, Takagi T, Kamasawa N, Ishijima SA, Osumi M","authors_abbrev":"Humbel BM et al.","pubmed_publication_date":"30 Mar 2001","pubmed_entrez_date":"2001-03-20","publication_year":"2001","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39104724","title":"Understanding the molecular mechanisms of human diseases: the benefits of fission yeasts.","citation":"Microb Cell 2024;11:288-311","abstract":"The role of model organisms such as yeasts in life science research is crucial. Although the baker's yeast ( Saccharomyces cerevisiae ) is the most popular model among yeasts, the contribution of the fission yeasts ( Schizosaccharomyces ) to life science is also indisputable. Since both types of yeasts share several thousands of common orthologous genes with humans, they provide a simple research platform to investigate many fundamental molecular mechanisms and functions, thereby contributing to the understanding of the background of human diseases. In this review, we would like to highlight the many advantages of fission yeasts over budding yeasts. The usefulness of fission yeasts in virus research is shown as an example, presenting the most important research results related to the Human Immunodeficiency Virus Type 1 (HIV-1) Vpr protein. Besides, the potential role of fission yeasts in the study of prion biology is also discussed. Furthermore, we are keen to promote the uprising model yeast  Schizosaccharomyces japonicus , which is a dimorphic species in the fission yeast genus. We propose the hyphal growth of  S. japonicus  as an unusual opportunity as a model to study the invadopodia of human cancer cells since the two seemingly different cell types can be compared along fundamental features. Here we also collect the latest laboratory protocols and bioinformatics tools for the fission yeasts to highlight the many possibilities available to the research community. In addition, we present several limiting factors that everyone should be aware of when working with yeast models.","doi":"10.15698/mic2024.08.833","authors":"Acs-Szabo L, Papp LA, Miklos I","authors_abbrev":"Acs-Szabo L et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-08-06","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-08-06 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12136010","title":"Role of the Tsc1-Tsc2 complex in signaling and transport across the cell membrane in the fission yeast Schizosaccharomyces pombe.","citation":"Genetics 2002 Jul;161(3):1053-63","abstract":"Heterozygous inactivation of either human TSC1 or TSC2 causes tuberous sclerosis (TSC), in which development of benign tumors, hamartomas, occurs via a two-hit mechanism. In this study, fission yeast genes homologous to TSC1 and TSC2 were identified, and their protein products were shown to physically interact like the human gene products. Strains lacking tsc1(+) or tsc2(+) were defective in uptake of nutrients from the environment. An amino acid permease, which is normally positioned on the plasma membrane, aggregated in the cytoplasm or was confined in vacuole-like structures in Deltatsc1 and Deltatsc2 strains. Deletion of tsc1(+) or tsc2(+) also caused a defect in conjugation. When a limited number of the cells were mixed, they conjugated poorly. The conjugation efficiency was improved by increased cell density. Deltatsc1 cells were not responsive to a mating pheromone, P-factor, suggesting that Tsc1 has an important role in the signal cascade for conjugation. These results indicate that the fission yeast Tsc1-Tsc2 complex plays a role in the regulation of protein trafficking and suggest a similar function for the human proteins. We also show that fission yeast Int6 is involved in a similar process, but functions in an independent genetic pathway.","authors":"Matsumoto S, Bandyopadhyay A, Kwiatkowski DJ, Maitra U, Matsumoto T","authors_abbrev":"Matsumoto S et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-07-24","publication_year":"2002","canto_session_key":"57c51248f25d451b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-09-06 10:58:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-06-13 09:25:09","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.13c","SPCC1322.13","SPBC11B10.02c","SPBC646.09c","SPAC22F3.13","SPBC359.03c","SPAP7G5.04c","SPAC144.03","SPBC1A4.02c","SPAC1296.03c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2012-06-13"},{"uniquename":"EMBL:AU011168","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21862693","title":"Production of ibuprofen acyl glucosides by human UGT2B7.","citation":"Drug Metab Dispos 2011 Dec;39(12):2174-81","abstract":"UDP-glycosyltransferases (UGTs) are an important group of enzymes that participate in phase II metabolism of xenobiotics and use the cofactor UDP-glucuronic acid for the production of glucuronides. When acting on molecules bearing a carboxylic acid they can form acyl glucuronides, a group of metabolites that has gained significant interest in recent years because of concerns about their potential role in drug toxicity. In contrast, reports about the production of drug acyl glucosides (which might also display high reactivity) have been scarce. In this study, we discovered the formation of acyl glycoside metabolites of R- and S-ibuprofen (Ibu) by human liver microsomes supplied with the cofactor UDP-glucose. Subsequently, human UGT2B7*1 and UGT2B7*2 recombinantly expressed in fission yeast Schizosaccharomyces pombe could be shown to catalyze these reactions. Moreover, we could enhance the glucoside production rate in fission yeast by overexpressing the fission yeast gene SPCC1322.04, a potential UDP-glucose pyrophosphorylase (UGPase), but not by overexpression of SPCC794.10, and therefore suggest to name this gene fyu1 for fission yeast UGPase1. It was interesting to note that pronounced differences between the two polymorphic UGT2B7 variants were observed with respect to acyl glucoside production. Finally, using the metabolic precursor [(13)C(6)]glucose, we demonstrated the production of stable isotope-labeled reference standards of Ibu acyl glucoside and Ibu acyl glucuronide by whole-cell biotransformation in fission yeast.","doi":"10.1124/dmd.111.041640","authors":"Buchheit D, Dragan CA, Schmitt EI, Bureik M","authors_abbrev":"Buchheit D et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-08-25","publication_year":"2011","canto_session_key":"9cf99a4f4e22efa4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-12-10 12:54:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-17 17:14:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1322.04","SPCC794.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-02-17"},{"uniquename":"PMID:3735426","title":"Inactivation of nonsense suppressor transfer RNA genes in Schizosaccharomyces pombe. Intergenic conversion and hot spots of mutation.","citation":"J Mol Biol 1986 Apr 05;188(3):343-53","abstract":"Intergenic conversion is a mechanism for the concerted evolution of repeated DNA sequences. A new approach for the isolation of intergenic convertants of serine tRNA genes in the yeast Schizosaccharomyces pombe is described. Contrary to a previous scheme, the intergenic conversion events studied in this case need not result in functional tRNA genes. The procedure utilizes crosses of strains that are homozygous for an active UGA suppressor tRNA gene, and the resulting progeny spores are screened for loss of suppressor activity. In this way, intergenic convertants of a tRNA gene are identified that inherit varying stretches of DNA sequence from either of two other tRNA genes. The information transferred between genes includes anticodon and intron sequences. Two of the three tRNA genes involved in these information transfers are located on different chromosomes. The results indicate that intergenic conversion is a conservative process. No infidelity is observed in the nucleotide sequence transfers. This provides further evidence for the hypothesis that intergenic conversion and allelic conversion are the result of the same molecular mechanism. The screening procedure for intergenic revertants also yields spontaneous mutations that inactivate the suppressor tRNA gene. Point mutations and insertions of A occur at various sites at low frequency. In contrast, A insertions at one specific site occur with high frequency in each of the three tRNA genes. This new type of mutation hot spot is found also in vegetative cells.","authors":"Heyer WD, Munz P, Amstutz H, Aebi R, Gysler C, Schuchert P, Szankasi P, Leupold U, Kohli J, Gamulin V","authors_abbrev":"Heyer WD et al.","pubmed_publication_date":"05 Apr 1986","pubmed_entrez_date":"1986-04-05","publication_year":"1986","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ632012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.46"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25942548","title":"Cytokinesis: does Mid1 have an identity crisis?","citation":"Curr Biol 2015 May 04;25(9):R364-6","abstract":"New work shows the anillin-related protein Mid1 does not position the cytokinetic ring in the fission yeast Schizosaccharomyces japonicus, unlike its role in S. pombe. Further analysis suggests the conserved function of Mid1-like anillin proteins may be in scaffolding, not positioning, the cytokinetic ring.","doi":"10.1016/j.cub.2015.03.017","authors":"Moseley JB","authors_abbrev":"Moseley JB","pubmed_publication_date":"04 May 2015","pubmed_entrez_date":"2015-05-06","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-05-07 00:19:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18354497","title":"The fission yeast homologue of CENP-B, Abp1, regulates directionality of mating-type switching.","citation":"EMBO J 2008 Apr 09;27(7):1029-38","abstract":"In fission yeast, mating-type switching involves replacing genetic information contained at the expressed mat1 locus by that of either the mat2P or mat3M donor loci. Donor selection is nonrandom, as mat1P cells preferentially use mat3M for switching, whereas mat1M cells use mat2P. Switching directionality is determined by the cell-type-specific distribution of the Swi2-Swi5 complex that, in mat1P cells, localises to mat3M and, only in mat1M cells, spreads to mat2P in a heterochromatin-dependent manner. Mechanisms regulating spreading of Swi2-Swi5 across heterochromatin are not fully understood. Here, we show that the fission yeast homologue of CENP-B, Abp1, binds to the silent domain of the mating-type locus and regulates directionality of switching. Deletion of abp1 prevents utilisation of mat2P, as when heterochromatin is disrupted and spreading of Swi2-Swi5 is impaired. Our results show that, indeed, deletion of abp1 abolishes spreading of Swi2-Swi5 to mat2P. However, in abp1Delta cells, heterochromatin organisation at the mating-type locus is preserved, indicating that Abp1 is actually required for efficient spreading of Swi2-Swi5 through heterochromatin. Cbh1 and Cbh2, which are also homologous to CENP-B, have only a minor contribution to the regulation of directionality of switching, which is in contrast with the strong effects observed for Abp1.","doi":"10.1038/emboj.2008.53","authors":"Aguilar-Arnal L, Marsellach FX, Azorín F","authors_abbrev":"Aguilar-Arnal L et al.","pubmed_publication_date":"09 Apr 2008","pubmed_entrez_date":"2008-03-21","publication_year":"2008","canto_session_key":"6960ce3c7a8f53d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-02 11:45:34","canto_approved_date":"2022-07-09 02:42:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-21 16:30:51","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.05c","SPBC14F5.12c","SPBC1105.04c","SPAC1142.03c","SPBC428.08c","SPAC9E9.10c","SPAC664.01c","SPBC409.03"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2017-03-02"},{"uniquename":"PMID:15027197","title":"[Effect of superexpression of DNA-binding protein heterochromatin Abp1p on frequency of loss of minichromosomes and growth of Schizosaccharomyces pombe with mutations of the gene coding cofactor D].","citation":"Genetika 2004 Jan;40(1):26-36","abstract":"Mitotic chromosome segregation is partly determined by interaction between microtubules (MTs) and the kinetochores of sister chromatids. The precise mechanism of the interaction between kinetochores and MTs remains unclear. This process has been studied in fission yeast Schizosaccharomyces pombe by analyzing interaction between genes encoding kinetochore components, such as DNA-binding protein Abp1p, and genes whose protein products affect the dynamics of MTs, such as cofactor D of tubulin dimer assembly. Analysis of cell growth and minichromosome loss frequency has demonstrated that mutations in the gene of cofactor D, especially mutation tsm1-512, increase the rate of minichromosome loss and the sensitivity to changes in Abp1p concentration in cells compared to wild-type cells Probably, mutations alp1-1315 and tsm1-512 of the cofactor D gene cause defects in the kinetochore-MT interaction.","authors":"Fedianina OS, Grishchuk EL","authors_abbrev":"Fedianina OS et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2004-03-19","publication_year":"2004","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12842472","title":"Structural variation in PWWP domains.","citation":"J Mol Biol 2003 Jul 11;330(3):571-6","abstract":"The PWWP domain is a ubiquitous eukaryotic protein module characterised by a region of sequence similarity of approximately 80 amino acids containing a highly conserved PWWP motif. It is frequently found in proteins associated with chromatin. We have determined the structure of a PWWP domain from the S. pombe protein SPBC215.07c using NMR spectroscopy. The structure is composed of a five stranded beta barrel followed by two alpha helices. Comparison to the recently reported structure of a homologous domain from the mammalian DNA methyltransferase Dnmt3b reveals substantial differences both in the C-terminal helical region and in the PWWP motif.","authors":"Slater LM, Allen MD, Bycroft M","authors_abbrev":"Slater LM et al.","pubmed_publication_date":"11 Jul 2003","pubmed_entrez_date":"2003-07-05","publication_year":"2003","canto_session_key":"93316c6acff6c864","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-04 22:17:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 22:17:19","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC215.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04","pdb_entries":[{"pdb_id":"1h3z","gene_chains":[{"gene_uniquename":"SPBC215.07c","chain":"A","position":"118-225"}],"title":"Solution structure of a PWWP domain from Schizosaccharomyces Pombe","entry_authors":"Slater LM,Allen MD,Bycroft M","entry_authors_abbrev":"Slater LM et al.","reference_uniquename":"PMID:12842472","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:9473044","title":"Coordination of initiation of nuclear division and initiation of cell division in Schizosaccharomyces pombe: genetic interactions of mutations.","citation":"J Bacteriol 1998 Feb;180(4):892-900","abstract":"sep1+ encodes a Schizosaccharomyces pombe homolog of the HNF-3/forkhead family of the tissue-specific and developmental gene regulators identified in higher eukaryotes. Its mutant allele sep1-1 causes a defect in cytokinesis and confers a mycelial morphology. Here we report on genetic interactions of sep1-1 with the M-phase initiation mutations wee1-, cdc2-1w, and cdc25-22. The double mutants sep1-1 wee1- and sep1-1 cdc2-1w form dikaryon cells at high frequency, which is due to nuclear division in the absence of cell division. The dikaryosis is reversible and suppressible by cdc25-22. We propose that the genes wee1+, cdc2+, cdc25+, and sep1+ form a regulatory link between the initiation of mitosis and the initiation of cell division.","authors":"Grallert A, Grallert B, Ribar B, Sipiczki M","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-02-24","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC4C3.12","SPCC18B5.03","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:27165118","title":"fhl1 gene of the fission yeast regulates transcription of meiotic genes and nitrogen starvation response, downstream of the TORC1 pathway.","citation":"Curr Genet 2017 Feb;63(1):91-101","abstract":"Environmental changes, such as nutrient limitation or starvation induce different signal transducing pathways, which require coordinated cooperation of several genes. Our previous data revealed that the fhl1 fork-head type transcription factor of the fission yeast could be involved in sporulation, which was typically induced under poor conditions. Since the exact role of Fhl1 in this process was not known, we wanted to identify its downstream targets and to investigate its possible cooperation with another known regulator of sporulation. Gene expression and Northern blot analysis of the fhl1∆ mutant strain revealed the target genes involved in mating and sporulation. Our results also showed that Fhl1 could regulate nutrient sensing, the transporter and permease genes. Since the majority of these genes belonged to the nitrogen starvation response, the possible cooperation of fhl1 and tor2 was also investigated. Comparison of their microarray data and the expression of fhl1  +  from a strong promoter in the tor2-ts mutant cells suggested that one part of the target genes are commonly regulated by Fhl1 and Tor2. Since the expression of fhl1  +  from a strong promoter could rescue rapamycin and temperature sensitivity and suppressed the hyper-sporulation defect of the tor2-ts mutant cells, we believe that Fhl1 acts in TOR signaling, downstream of Tor2. Thus, this work shed light on certain novel details of the regulation of the sexual processes and a new member of the TOR pathway, but further experiments are needed to confirm the involvement of Fhl1 in nutrient sensing.","doi":"10.1007/s00294-016-0607-1","authors":"Pataki E, Weisman R, Sipiczki M, Miklos I","authors_abbrev":"Pataki E et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-05-12","publication_year":"2017","canto_session_key":"4847e0de3cb01075","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ida Miklos","canto_first_approved_date":"2018-03-26 12:50:28","canto_approved_date":"2024-02-23 17:38:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-05 11:28:04","canto_added_date":"2016-05-13 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ida Miklos","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1142.08","SPBC216.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-26"},{"uniquename":"EMBL:SPC09362","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20545767","title":"Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms.","citation":"Genes Cells 2010 Jun;15(7):661-9","abstract":"The nucleoporin Nup98 is an essential component of the nuclear pore complex. This peripheral nucleoporin with its Gly-Leu-Phe-Gly (GLFG) repeat domain contributes to nuclear-cytoplasmic trafficking, including mRNA export. In addition, accumulating studies indicate that Nup98 plays roles in several important biological events such as gene expression, mitotic checkpoint, and pathogenesis. Nup98 is well conserved among organisms belonging to the fungi and animal kingdoms. These kingdoms belong to the eukaryotic supergroup Opisthokonta. However, there is considerable diversity in the Nup98 orthologs expressed in organisms belonging to other eukaryotic supergroups. Intriguingly, in ciliates, a unicellular organism having two functionally distinct nuclei, GLFG-Nup98 is present in one of the nuclei and a distinct Nup98 ortholog is present in the other nucleus, and these different Nup98s participate in a nucleus-selective transport mechanism. In this review, we focus on Nup98 function and discuss how this nucleoporin has evolved in eukaryotic kingdoms.","doi":"10.1111/j.1365-2443.2010.01415.x","authors":"Iwamoto M, Asakawa H, Hiraoka Y, Haraguchi T","authors_abbrev":"Iwamoto M et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-06-16","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-08-22 16:46:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36309474","title":"Resorcinol alleviates alpha-terpineol-induced cell death in Schizosaccharomyces pombe via increased activity of the antioxidant enzyme Sod2.","citation":"FEMS Yeast Res 2022 Nov 11;22(1)","abstract":"Alpha-terpineol, popular monoterpenoid alcohol, is known to cause cytotoxicity in a few cancer cells or to have antioxidant activity, but underlying mechanisms or apoptotic processes in yeast cell death should be understood. We used the fission yeast (Schizosaccharomyces pombe) as a unicellular model to monitor cellular toxicology and physiological mechanisms for the involvement of alpha-terpineol in cell death. Alpha-terpineol caused Reactive oxygen species (ROS) overproduction and following cytotoxicity and apoptosis in a dose-dependent manner. The effect of oxidative stress was proved using sod1 and sod2 mutants (antioxidant-limited cells), and the results showed that apoptosis was caused by alpha-terpineol-driven oxidation. In addition, resorcinol, a herbal extract from medicinal plants, showed protective activity against alpha-terpineol cytotoxicity. Survival rates, apoptotic cell death ratios, oxidation levels, and antioxidant gene expressions were completely altered; surprisingly sod1 and sod2 levels dramatically increased. However, sod2 was highly upregulated in response to resorcinol treatment with alpha-terpineol. The potential role of the Sod2 enzyme was proved using sod2 mutant cells that do not have a mitochondrial radical-clearing activity. Consequently, the dose-dependent and ROS-mediated cytotoxic/apoptotic effects of alpha-terpineol and the Sod2-dependent protective and antioxidant effects of resorcinol were demonstrated in unicellular model organism S. pombe by this study.","doi":"10.1093/femsyr/foac052","authors":"Agus HH, Cetin A, Ozdemir N, Ozbay MG, Caglar MA, Sariyildiz MA, Yildiz U","authors_abbrev":"Agus HH et al.","pubmed_publication_date":"11 Nov 2022","pubmed_entrez_date":"2022-10-29","publication_year":"2022","canto_session_key":"03c103010e04efb9","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-10-31 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1486.01","SPAC821.10c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:21981922","title":"A Pre-mRNA degradation pathway that selectively targets intron-containing genes requires the nuclear poly(A)-binding protein.","citation":"Mol Cell 2011 Oct 07;44(1):108-19","abstract":"General discard pathways eliminate unprocessed and irregular pre-mRNAs to control the quality of gene expression. In contrast to such general pre-mRNA decay, we describe here a nuclear pre-mRNA degradation pathway that controls the expression of select intron-containing genes. We show that the fission yeast nuclear poly(A)-binding protein, Pab2, and the nuclear exosome subunit, Rrp6, are the main factors involved in this polyadenylation-dependent pre-mRNA degradation pathway. Transcriptome analysis and intron swapping experiments revealed that inefficient splicing is important to dictate susceptibility to Pab2-dependent pre-mRNA decay. We also show that negative splicing regulation can promote the poor splicing efficiency required for this pre-mRNA decay pathway, and in doing so, we identified a mechanism of cross-regulation between paralogous ribosomal proteins through nuclear pre-mRNA decay. Our findings unveil a layer of regulation in the nucleus in which the turnover of specific pre-mRNAs, besides the turnover of mature mRNAs, is used to control gene expression.","doi":"10.1016/j.molcel.2011.06.035","authors":"Lemieux C, Marguerat S, Lafontaine J, Barbezier N, Bähler J, Bachand F","authors_abbrev":"Lemieux C et al.","pubmed_publication_date":"07 Oct 2011","pubmed_entrez_date":"2011-10-11","publication_year":"2011","canto_session_key":"073a79f341c124df","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-11-22 11:39:43","canto_approved_date":"2025-07-04 13:50:50","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-11-22 11:35:54","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9G1.03c","SPAC1F3.01","SPAC13G6.12c","SPBC3H7.06c","SPAC6G9.13c","SPAP8A3.05","SPBC16E9.12c","SPAC12G12.13c","SPBC26H8.10","SPAC16E8.16","SPBC30D10.18c","SPAC6F12.16c","SPAC1250.05"],"gene_count":13,"ltp_gene_count":8,"approved_date":"2023-11-22"},{"uniquename":"PMID:22264709","title":"TUBA1A mutation-associated lissencephaly: case report and review of the literature.","citation":"Pediatr Neurol 2012 Feb;46(2):127-31","abstract":"Lissencephaly is a disorder of neuronal migration resulting in abnormal cerebral cortical sulcation and gyration. Affected children present with microcephaly, developmental delay, and early-onset epileptic seizures. Recently, de novo missense mutations in the tubulin α-1A (TUBA1A) gene were identified as causing a distinctive radiologic phenotype comprising of posteriorly predominant lissencephaly with dysgenetic corpus callosum, cerebellar and brainstem hypoplasia, and more recently, polymicrogyria. We describe a 14-month-old girl with TUBA1A mutation-associated lissencephaly, and summarize the clinical and neuroradiologic findings of 19 cases in the literature.","doi":"10.1016/j.pediatrneurol.2011.11.017","authors":"Sohal AP, Montgomery T, Mitra D, Ramesh V","authors_abbrev":"Sohal AP et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2012-01-24","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPBC800.05c","SPBC26H8.07c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"InterPro:IPR007527","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:40427594","title":"Molecular and Biophysical Perspectives on Dormancy Breaking: Lessons from Yeast Spore.","citation":"Biomolecules 2025 May 11;15(5)","abstract":"Dormancy is a physiological state that enables cells to survive under adverse conditions by halting their proliferation while retaining the capacity to resume growth when conditions become favorable. This remarkable transition between dormant and proliferative states occurs across a wide range of species, including bacteria, fungi, plants, and tardigrades. Among these organisms, yeast cells have emerged as powerful model systems for elucidating the molecular and biophysical principles governing dormancy and dormancy breaking. In this review, we provide a comprehensive summary of current knowledge on the molecular mechanisms underlying cellular dormancy, with particular focus on the two major model yeasts:  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe . Recent advances in multifaceted approaches-such as single-cell RNA-seq, proteomic analysis, and live-cell imaging-have revealed dynamic changes in gene expression, proteome composition, and viability. Furthermore, insights into the biophysical properties of the cytoplasm have offered new understanding of dormant cell regulation through changes in cytoplasmic fluidity. These properties contribute to both the remarkable stability of dormant cells and their capacity to exit dormancy upon environmental cues, deepening our understanding of fundamental cellular survival strategies across diverse species.","doi":"10.3390/biom15050701","authors":"Sakai K, Kondo Y, Aoki K, Goto Y","authors_abbrev":"Sakai K et al.","pubmed_publication_date":"11 May 2025","pubmed_entrez_date":"2025-05-28","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-05-28 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10725227","title":"A fission yeast general translation factor reveals links between protein synthesis and cell cycle controls.","citation":"J Cell Sci 2000 Apr;113 ( Pt 8):1447-58","abstract":"In two independent screens we isolated fission yeast mutations with phenotypes suggesting defects in B-cyclin function or expression. These mutations define a single gene which we call ded1. We show that ded1 encodes a general translation factor that is related in sequence and function to RNA helicases required for translation in other species. Levels of the B-cyclins Cig2 and Cdc13 are dramatically reduced upon inactivation of Ded1, and this reduction is independent of degradation by the anaphase promoting complex. When a ded1 mutant is grown under semi-restrictive conditions, the translation of Cig2 (and to a lesser extent Cdc13), is impaired relative to other proteins. We show that B-cyclin translation is specifically inhibited upon nitrogen starvation of wild-type cells, when B-cyclin/Cdc2 inactivation is a prerequisite for G(1) arrest and subsequent mating. Our data suggest that translational inhibition of B-cyclin expression represents a third mechanism, in addition to cyclin degradation and Rum1 inhibition, that contributes to Cdc2 inactivation as cells exit from the mitotic cell cycle and prepare for meiosis.","authors":"Grallert B, Kearsey SE, Lenhard M, Carlson CR, Nurse P, Boye E, Labib K","authors_abbrev":"Grallert B et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-03-22","publication_year":"2000","canto_session_key":"5e98db8475cc3f3a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-09-04 16:37:39","canto_approved_date":"2024-07-02 12:00:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-07 14:15:01","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":30,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPAPB2B4.03","SPCC1795.11","SPCC16A11.17","SPAC17C9.01c","SPAC1F7.05","SPBC14C8.07c","SPBC4.04c","SPBC32F12.09","SPBC11B10.09"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2018-09-04"},{"uniquename":"PMID:32496538","title":"Cdk9 and H2Bub1 signal to Clr6-CII/Rpd3S to suppress aberrant antisense transcription.","citation":"Nucleic Acids Res 2020 Jul 27;48(13):7154-7168","abstract":"Mono-ubiquitylation of histone H2B (H2Bub1) and phosphorylation of elongation factor Spt5 by cyclin-dependent kinase 9 (Cdk9) occur during transcription by RNA polymerase II (RNAPII), and are mutually dependent in fission yeast. It remained unclear whether Cdk9 and H2Bub1 cooperate to regulate the expression of individual genes. Here, we show that Cdk9 inhibition or H2Bub1 loss induces intragenic antisense transcription of ∼10% of fission yeast genes, with each perturbation affecting largely distinct subsets; ablation of both pathways de-represses antisense transcription of over half the genome. H2Bub1 and phospho-Spt5 have similar genome-wide distributions; both modifications are enriched, and directly proportional to each other, in coding regions, and decrease abruptly around the cleavage and polyadenylation signal (CPS). Cdk9-dependence of antisense suppression at specific genes correlates with high H2Bub1 occupancy, and with promoter-proximal RNAPII pausing. Genetic interactions link Cdk9, H2Bub1 and the histone deacetylase Clr6-CII, while combined Cdk9 inhibition and H2Bub1 loss impair Clr6-CII recruitment to chromatin and lead to decreased occupancy and increased acetylation of histones within gene coding regions. These results uncover novel interactions between co-transcriptional histone modification pathways, which link regulation of RNAPII transcription elongation to suppression of aberrant initiation.","doi":"10.1093/nar/gkaa474","authors":"Sansó M, Parua PK, Pinto D, Svensson JP, Pagé V, Bitton DA, MacKinnon S, Garcia P, Hidalgo E, Bähler J, Tanny JC, Fisher RP","authors_abbrev":"Sansó M et al.","pubmed_publication_date":"27 Jul 2020","pubmed_entrez_date":"2020-06-05","publication_year":"2020","canto_session_key":"6186ba197a53e798","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pabitra Parua","canto_first_approved_date":"2020-07-21 13:19:22","canto_approved_date":"2024-03-28 15:38:17","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-07-17 18:21:08","canto_added_date":"2020-06-06 00:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pabitra Parua","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.15","SPAC16C9.05","SPCC188.13c","SPAC23C4.19","SPBC28F2.12","SPCC306.04c","SPAC17A5.14","SPCC970.10c","SPAC29B12.02c","SPBC32H8.10","SPAC1F3.01","SPAC3G6.01","SPCC622.09"],"gene_count":13,"ltp_gene_count":11,"approved_date":"2020-07-21"},{"uniquename":"PMID:28942089","title":"Biochemical Basis for Distinct Roles of the Heterochromatin Proteins Swi6 and Chp2.","citation":"J Mol Biol 2017 Nov 24;429(23):3666-3677","abstract":"Heterochromatin protein 1 (HP1) family proteins are conserved chromatin binding proteins involved in gene silencing, chromosome packaging, and chromosome segregation. These proteins recognize histone H3 lysine 9 methylated tails via their chromodomain and recruit additional ligand proteins with diverse activities through their dimerization domain, the chromoshadow domain. Species that have HP1 proteins possess multiple paralogs that perform non-overlapping roles in vivo. How different HP1 proteins, which are highly conserved, perform different functions is not well understood. Here, we use the two Schizosaccharomyces pombe HP1 paralogs, Swi6 and Chp2, as model systems to compare and contrast their biophysical properties. We find that Swi6 and Chp2 have similar dimerization and oligomerization equilibria, and that Swi6 binds slightly (~3-fold) more strongly to nucleosomes than Chp2. Furthermore, while Swi6 binding to the H3K9me3 mark is regulated by a previously described auto-inhibition mechanism, the binding of Chp2 to the H3K9me3 mark is not analogously regulated. In the context of chromoshadow domain interactions, we show using a newly identified peptide sequence from the Clr3 histone deacetylase and a previously identified sequence from the protein Shugoshin that the Swi6 chromoshadow domain binds both ligands more strongly than the Chp2. Overall, our findings uncover quantitative differences in how Swi6 and Chp2 interact with nucleosomal and non-nucleosomal ligands and qualitative differences in how their assembly on nucleosomes is regulated. These findings provide a biochemical framework to explain the varied functions of Chp2 and Swi6 in vivo.","doi":"10.1016/j.jmb.2017.09.012","authors":"Isaac RS, Sanulli S, Tibble R, Hornsby M, Ravalin M, Craik CS, Gross JD, Narlikar GJ","authors_abbrev":"Isaac RS et al.","pubmed_publication_date":"24 Nov 2017","pubmed_entrez_date":"2017-09-25","publication_year":"2017","canto_session_key":"ab844974df585e5e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-09-26 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP35G2.03c","SPBC16C6.10","SPAC664.01c","SPBC800.03","SPAC1834.04"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:11942607","title":"Studies in fission yeast on mechanisms of cell division site placement.","citation":"Cell Struct Funct 2001 Dec;26(6):539-44","abstract":"One fundamental problem in cytokinesis is how the plane of cell division is established. In this review, we describe our studies on searching for \"signals\" that position the cell division plane, using fission yeast Schizosaccharomyces pombe. First, we take a genetic approach to determine how the nucleus may position the contractile ring in fission yeast. mid1p appears to link the position of the ring with the nuclear position, as it is required for proper placement of the contractile ring and is localized in a band at the cell surface overlying the nucleus. Second, we study how microtubules may function in the establishment of cell polarity at the cell tips. tea1p may be deposited on the cell surface by microtubules and function to recruit proteins involved in making actin structures. These studies suggest how microtubules may direct the assembly of the contractile ring in animal cells.","authors":"Chang F","authors_abbrev":"Chang F","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2002-04-11","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25355954","title":"The contractile ring coordinates curvature-dependent septum assembly during fission yeast cytokinesis.","citation":"Mol Biol Cell 2015 Jan 01;26(1):78-90","abstract":"The functions of the actin-myosin-based contractile ring in cytokinesis remain to be elucidated. Recent findings show that in the fission yeast Schizosaccharomyces pombe, cleavage furrow ingression is driven by polymerization of cell wall fibers outside the plasma membrane, not by the contractile ring. Here we show that one function of the ring is to spatially coordinate septum cell wall assembly. We develop an improved method for live-cell imaging of the division apparatus by orienting the rod-shaped cells vertically using microfabricated wells. We observe that the septum hole and ring are circular and centered in wild-type cells and that in the absence of a functional ring, the septum continues to ingress but in a disorganized and asymmetric manner. By manipulating the cleavage furrow into different shapes, we show that the ring promotes local septum growth in a curvature-dependent manner, allowing even a misshapen septum to grow into a more regular shape. This curvature-dependent growth suggests a model in which contractile forces of the ring shape the septum cell wall by stimulating the cell wall machinery in a mechanosensitive manner. Mechanical regulation of the cell wall assembly may have general relevance to the morphogenesis of walled cells.","doi":"10.1091/mbc.E14-10-1441","authors":"Zhou Z, Munteanu EL, He J, Ursell T, Bathe M, Huang KC, Chang F","authors_abbrev":"Zhou Z et al.","pubmed_publication_date":"01 Jan 2015","pubmed_entrez_date":"2014-10-31","publication_year":"2015","canto_session_key":"424b5faf419aa674","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-11-01 01:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR13288","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.04","HGNC:16944"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37597513","title":"A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle.","citation":"Mol Cell 2023 Sep 07;83(17):3108-3122.e13","abstract":"General protein folding is mediated by chaperones that utilize ATP hydrolysis to regulate client binding and release. Zinc-finger protein 1 (Zpr1) is an essential ATP-independent chaperone dedicated to the biogenesis of eukaryotic translation elongation factor 1A (eEF1A), a highly abundant GTP-binding protein. How Zpr1-mediated folding is regulated to ensure rapid Zpr1 recycling remains an unanswered question. Here, we use yeast genetics and microscopy analysis, biochemical reconstitution, and structural modeling to reveal that folding of eEF1A by Zpr1 requires GTP hydrolysis. Furthermore, we identify the highly conserved altered inheritance of mitochondria 29 (Aim29) protein as a Zpr1 co-chaperone that recognizes eEF1A in the GTP-bound, pre-hydrolysis conformation. This interaction dampens Zpr1⋅eEF1A GTPase activity and facilitates client exit from the folding cycle. Our work reveals that a bespoke ATP-independent chaperone system has mechanistic similarity to ATPase chaperones but unexpectedly relies on client GTP hydrolysis to regulate the chaperone-client interaction.","doi":"10.1016/j.molcel.2023.07.028","authors":"McQuown AJ, Nelliat AR, Reif D, Sabbarini IM, Membreno BS, Wu CC, Denic V","authors_abbrev":"McQuown AJ et al.","pubmed_publication_date":"07 Sep 2023","pubmed_entrez_date":"2023-08-19","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2C4.04c","SPAC15A10.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU012873","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31472097","title":"The role of Rsv1 in the transcriptional regulation of genes involved in sugar metabolism for long-term survival.","citation":"FEBS J 2020 Mar;287(5):878-896","abstract":"Glucose limitation is a major stress condition that cells must respond to by altering their metabolism to ensure survival. Rsv1 is a zinc finger protein previously shown to be required for survival during stationary phase. In this study, we present a novel mechanism regulated by Rsv1 in the fission yeast Schizosaccharomyces pombe that is involved in altering glucose metabolic flux. We found that rsv1 gene expression is induced by Rst2 and Atf1, two transcription factors regulated by the cAMP-dependent protein kinase (PKA) pathway and the mitogen-activated protein kinase (MAPK) cascade, respectively. The downstream target genes of Rsv1 were identified by genome-wide ChIP sequencing of Rsv1-bound DNA sites and RNA sequencing analysis of Rsv1-dependent transcripts that were differentially expressed under glucose starvation. Rsv1 directly regulated the expression of at least 21 genes that mostly encode transporters and proteins related to sugar metabolism. Among these, gcd1, which encodes glucose dehydrogenase in the gluconate shunt for the pentose phosphate pathway, was most remarkably repressed by Rsv1. The defect in survival of Δrsv1 mutant under glucose starvation condition was mitigated by additional deletion of a gcd1, idn1, or a gene for a putative lactonase (SPCC16c4.10), suggesting the critical importance of downregulating the gluconate shunt and pentose phosphate pathway for long-term survival. These results show an intricate response to glucose starvation: increasing the synthesis of a transcription factor via two signal transduction pathways, which sheds light on the importance of remodeling a metabolic circuit to secure glucose for cell survival.","doi":"10.1111/febs.15052","authors":"Kim EJ, Cho YJ, Chung WH, Roe JH","authors_abbrev":"Kim EJ et al.","pubmed_publication_date":"Mar 2020","pubmed_entrez_date":"2019-09-01","publication_year":"2020","canto_session_key":"83e1d99558bcf5ac","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-09-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.09","SPCC794.01c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:9529614","title":"Genetic analysis of protein tyrosine phosphatases.","citation":"Curr Opin Genet Dev 1998 Feb;8(1):112-26","abstract":"Genetic analysis has enhanced our understanding of the biological roles of many protein tyrosine kinases (PTKs). More recently, studies utilizing both spontaneous mutants and mutants induced by homologous recombination techniques have begun to yield key insights into the role of specific protein tyrosine phosphatases (PTPs) and to suggest how PTKs and PTPs interact. Specific PTPs in Saccharomyces cerevesiae and Schizomyces pombe regulate MAP kinase pathways. Several Drosophila receptor PTPs control axonal targeting pathways, whereas the non-receptor PTP Corkscrew (Csw), plays an essential positive signaling role in multiple developmental pathways directed by receptor PTKs. The vertebrate homolog of Csw, SHP-2, also is required for growth factor signaling and normal development. Finally, very recent studies of other mammalian PTPs suggest that they have critical roles in processes as diverse as hematopoiesis and liver and pituitary development.","authors":"Van Vactor D, O'Reilly AM, Neel BG","authors_abbrev":"Van Vactor D et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-04-08","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12932737","title":"Motifs in Schizosaccharomyces pombe ars3002 important for replication origin activity in Saccharomyces cerevisiae.","citation":"Plasmid 2003 Sep;50(2):113-9","abstract":"Ars3002 is an efficient single-copy replication origin in the fission yeast, Schizosaccharomyces pombe. In a previous study, we tested the effects of consecutive approximately 50-bp deletions throughout ars3002 on the replication efficiency of those origins in S. pombe. Here we report the results of our use of the same approximately 50-bp deletions to test the hypothesis that some of the cis-acting sequences important for replication origin activity in fission yeast might be conserved in the evolutionarily distant budding yeast, Saccharomyces cerevisiae. We found that in most cases there was no correlation between the effects of particular mutations in S. pombe and in S. cerevisiae. We conclude that it is unlikely that any of the cis-acting sequences recognised by homologous replication proteins is conserved between these two yeast species.","authors":"Antunes DF, Kim SM, Huberman JA, de Morais MA","authors_abbrev":"Antunes DF et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-08-23","publication_year":"2003","canto_session_key":"75163acb6e6e28bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 15:33:36","canto_approved_date":"2019-01-07 15:33:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 15:33:30","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:12934001","title":"RNAi extends its reach.","citation":"Science 2003 Aug 22;301(5636):1060-1","abstract":"","authors":"Matzke M, Matzke AJ","authors_abbrev":"Matzke M et al.","pubmed_publication_date":"22 Aug 2003","pubmed_entrez_date":"2003-08-23","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16303567","title":"A large-scale screen in S. pombe identifies seven novel genes required for critical meiotic events.","citation":"Curr Biol 2005 Nov 22;15(22):2056-62","abstract":"Meiosis is a specialized form of cell division by which sexually reproducing diploid organisms generate haploid gametes. During a long prophase, telomeres cluster into the bouquet configuration to aid chromosome pairing, and DNA replication is followed by high levels of recombination between homologous chromosomes (homologs). This recombination is important for the reductional segregation of homologs at the first meiotic division; without further replication, a second meiotic division yields haploid nuclei. In the fission yeast Schizosaccharomyces pombe, we have deleted 175 meiotically upregulated genes and found seven genes not previously reported to be critical for meiotic events. Three mutants (rec24, rec25, and rec27) had strongly reduced meiosis-specific DNA double-strand breakage and recombination. One mutant (tht2) was deficient in karyogamy, and two (bqt1 and bqt2) were deficient in telomere clustering, explaining their defects in recombination and segregation. The moa1 mutant was delayed in premeiotic S phase progression and nuclear divisions. Further analysis of these mutants will help elucidate the complex machinery governing the special behavior of meiotic chromosomes.","authors":"Martín-Castellanos C, Blanco M, Rozalén AE, Pérez-Hidalgo L, García AI, Conde F, Mata J, Ellermeier C, Davis L, San-Segundo P, Smith GR, Moreno S","authors_abbrev":"Martín-Castellanos C et al.","pubmed_publication_date":"22 Nov 2005","pubmed_entrez_date":"2005-11-24","publication_year":"2005","canto_session_key":"9c71d0d270b64c23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-28 08:31:11","canto_approved_date":"2025-12-04 15:48:31","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-07-16 08:09:03","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":80,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.07","SPAC6G9.04","SPAC1952.15c","SPAC1002.06c","SPBC2G2.09c","SPBC29A10.14","SPAC25H1.03","SPBC216.02","SPCC1235.12c","SPAC17A5.11","SPAC823.16c","SPBC146.11c","SPBC29A10.02","SPAC4F10.07c","SPAC56E4.05","SPAC1610.04","SPAC13A11.03","SPAC14C4.08","SPCC645.11c","SPCC417.06c","SPBC577.05c","SPBC4B4.10c","SPAC15E1.07c","SPBC3H7.09","SPAC343.09","SPAC17A5.18c","SPBC146.10","SPBC31E1.01c","SPBC1773.09c","SPBP35G2.03c","SPAC16A10.07c","SPAC343.07","SPCC16C4.17","SPCC11E10.03","SPCC1682.03c","SPBC27.02c","SPAC6G9.13c","SPBC28F2.07"],"gene_count":38,"ltp_gene_count":36,"approved_date":"2015-04-28"},{"uniquename":"PMID:26448451","title":"Biostimulation of Oil Sands Process-Affected Water with Phosphate Yields Removal of Sulfur-Containing Organics and Detoxification.","citation":"Environ Sci Technol 2015 Nov 03;49(21):13012-20","abstract":"The ability to mitigate toxicity of oil sands process-affected water (OSPW) for return into the environment is an important issue for effective tailings management in Alberta, Canada. OSPW toxicity has been linked to classical naphthenic acids (NAs), but the toxic contribution of other acid-extractable organics (AEOs) remains unknown. Here, we examine the potential for in situ bioremediation of OSPW AEOs by indigenous algae. Phosphate biostimulation was performed in OSPW to promote the growth of indigenous photosynthetic microorganisms and subsequent toxicity and chemical changes were determined. After 12 weeks, the AEO fraction of phosphate-biostimulated OSPW was significantly less toxic to the fission yeast Schizosaccharomyces pombe than unstimulated OSPW. Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) analysis of the AEO fraction in phosphate-biostimulated OSPW showed decreased levels of SO3 class compounds, including a subset that may represent linear arylsulfonates. A screen with S. pombe transcription factor mutant strains for growth sensitivity to the AEO fraction or sodium dodecylbenzenesulfonate revealed a mode of toxic action consistent with oxidative stress and detrimental effects on cellular membranes. These findings demonstrate a potential algal-based in situ bioremediation strategy for OSPW AEOs and uncover a link between toxicity and AEOs other than classical NAs.","doi":"10.1021/acs.est.5b01391","authors":"Quesnel DM, Oldenburg TB, Larter SR, Gieg LM, Chua G","authors_abbrev":"Quesnel DM et al.","pubmed_publication_date":"03 Nov 2015","pubmed_entrez_date":"2015-10-09","publication_year":"2015","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2015-10-10 00:18:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40085054","title":"A Key Role of the EMC Complex for Mitochondrial Respiration and Quiescence in Fission Yeasts.","citation":"Yeast 2025 Mar 14;","abstract":"In eukaryotes, oxygen consumption is mainly driven by the respiratory activity of mitochondria, which generates most of the cellular energy that sustains life. This parameter provides direct information about mitochondrial activity of all aerobic biological systems. Using the Seahorse analyzer instrument, we show here that deletion of the oca3/emc2 gene (oca3Δ) encoding the Emc2 subunit of the ER membrane complex (EMC), a conserved chaperone/insertase that aids membrane protein biogenesis in the ER, severely affects oxygen consumption rates and quiescence survival in Schizosaccharomyces pombe yeast cells. Remarkably, the respiratory defect of the oca3Δ mutation (EMC dysfunction) is rescued synergistically by disruption of ergosterol biosynthesis (erg5Δ) and the action of the membrane fluidizing agent tween 20, suggesting a direct role of membrane fluidity and sterol composition in mitochondrial respiration in the fission yeast.","doi":"10.1002/yea.3998","authors":"Berraquero M, Tallada VA, Jimenez J","authors_abbrev":"Berraquero M et al.","pubmed_publication_date":"14 Mar 2025","pubmed_entrez_date":"2025-03-14","publication_year":"2025","canto_session_key":"bdb63ba80496b152","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-03-15 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2328721","title":"Identification of ras-related, YPT family genes in Schizosaccharomyces pombe.","citation":"EMBO J 1990 May;9(5):1417-22","abstract":"Screening for genes homologous to ras in Schizosaccharomyces pombe resulted in the isolation of a homolog of Saccharomyces cerevisiae YPT1. This S. pombe gene, named ypt3, has a coding capacity of 214 amino acids interrupted by two introns, and is essential for cell growth. Two more YPT1 homologs were isolated from S. pombe using a part of the ypt3 gene as the probe. One of them, named ypt1, is highly homologous to S. cerevisiae YPT1 and mouse ypt1 and is essential for cell growth. This gene has four introns and encodes 203 amino acids. Its cDNA placed downstream of the S. cerevisiae GAL7 promoter could complement S. cerevisiae ypt1-, indicating that Sp ypt1 and Sc YPT1 are functionally homologous. The other isolate, named ryh1, and a fourth homolog, ypt2, have been characterized by Gallwitz and co-workers. The ypt1, ypt2 and ypt3 genes, but not ryh1, constitute a family, their products having double cysteine as their C terminus and serine in place of a glycine residue highly conserved in ras proteins (mammalian Gly-12 or S. pombe Gly-17). The physiological roles of these genes appear to be distinct because each of them is indispensable for cell growth.","authors":"Miyake S, Yamamoto M","authors_abbrev":"Miyake S et al.","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_session_key":"b05aa0892640b958","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-20 16:27:14","canto_approved_date":"2021-04-13 16:47:40","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-05 16:29:14","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.03","SPBC1703.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-02-20"},{"uniquename":"PMID:40481005","title":"Fermentative factors shape transcriptional response of Lachancea thermotolerans and wine acidification.","citation":"NPJ Sci Food 2025 Jun 06;9(1):97","abstract":"Climate change is affecting grape must composition by increasing sugars and reducing organic acids, leading to sluggish fermentations and lower wine quality. Among biological solutions, Lachancea thermotolerans is widely studied for its ability to improve acidity through lactic acid production. This study evaluated how biotic and abiotic factors relevant to climate change influence both wine acidification and the transcriptomic response of L. thermotolerans. We assessed the effects of varying sugar concentrations, pH levels, and organic/inorganic nitrogen ratios, individually and combined. Additionally, we examined how fermentative partners (Saccharomyces cerevisiae and Schizosaccharomyces pombe) affect L. thermotolerans during co-fermentations. Results showed enhanced lactic acid production under high sugar and low organic nitrogen, with Sch. pombe promoting acidification and S. cerevisiae reducing it. These findings provide key insights into the metabolic response of L. thermotolerans and highlight the need to manage fermentation conditions and microbial interactions to improve wine quality in the face of climate change.","doi":"10.1038/s41538-025-00467-y","authors":"Vicente J, Benito S, Marquina D, Santos A","authors_abbrev":"Vicente J et al.","pubmed_publication_date":"06 Jun 2025","pubmed_entrez_date":"2025-06-06","publication_year":"2025","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2025-06-07 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9111315","title":"Human Bak induces cell death in Schizosaccharomyces pombe with morphological changes similar to those with apoptosis in mammalian cells.","citation":"Mol Cell Biol 1997 May;17(5):2468-74","abstract":"Apoptosis as a form of programmed cell death (PCD) in multicellular organisms is a well-established genetically controlled process that leads to elimination of unnecessary or damaged cells. Recently, PCD has also been described for unicellular organisms as a process for the socially advantageous regulation of cell survival. The human Bcl-2 family member Bak induces apoptosis in mammalian cells which is counteracted by the Bcl-x(L) protein. We show that Bak also kills the unicellular fission yeast Schizosaccharomyces pombe and that this is inhibited by coexpression of human Bcl-x(L). Moreover, the same critical BH3 domain of Bak that is required for induction of apoptosis in mammalian cells is also required for inducing death in yeast. This suggests that Bak kills mammalian and yeast cells by similar mechanisms. The phenotype of the Bak-induced death in yeast involves condensation and fragmentation of the chromatin as well as dissolution of the nuclear envelope, all of which are features of mammalian apoptosis. These data suggest that the evolutionarily conserved metazoan PCD pathway is also present in unicellular yeast.","authors":"Ink B, Zörnig M, Baum B, Hajibagheri N, James C, Chittenden T, Evan G","authors_abbrev":"Ink B et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1657593","title":"The Schizosaccharomyces pombe mam2 gene encodes a putative pheromone receptor which has a significant homology with the Saccharomyces cerevisiae Ste2 protein.","citation":"EMBO J 1991 Dec;10(12):3743-51","abstract":"The fission yeast Schizosaccharomyces pombe has two mating-types, h+ (P) and h- (M). The mam2 mutant exhibits an h(-)-specific sterile phenotype. Nucleotide sequencing of the mam2 gene isolated from an S. pombe genomic library revealed an open reading frame composed of 348 amino acids. The deduced mam2 product is a hydrophobic protein of 39 kDa that has significant sequence similarity (26.3% for identical amino acids) with the transmembrane domains of the Saccharomyces cerevisiae STE2 product, the alpha-pheromone receptor. Hydropathicity analysis suggests that the Mam2 protein contains seven possible membrane-spanning domains and a carboxy-terminal hydrophilic region. The mam2 gene was disrupted and found to be non-essential for growth. An h- haploid strain harbouring this disrupted null allele failed to respond to the pheromone of h+ cells, P-factor. These observations imply that the mam2 gene encodes a receptor for P-factor. Transcription of mam2 was induced only when strains containing functional mat1-M allele were cultured under conditions of nitrogen starvation. The mam2 gene was also transcribed in h+/h- diploid strains. The fact that the map1/mam2 homozygous diploid cells are incapable of sporulation implies that the pheromone signalling system is necessary for sporulation in diploid cells.","authors":"Kitamura K, Shimoda C","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"1065390df3fc736f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-11 20:54:04","canto_approved_date":"2021-10-04 15:14:40","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-02-16 16:07:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.06","SPAC11H11.04"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2018-06-11"},{"uniquename":"PMID:15533944","title":"Interaction of checkpoint proteins Hus1/Rad1/Rad9 with DNA base excision repair enzyme MutY homolog in fission yeast, Schizosaccharomyces pombe.","citation":"J Biol Chem 2005 Jan 07;280(1):408-17","abstract":"The DNA glycosylase MutY homolog (MYH) is responsible for removing adenines misincorporated opposite DNA strands containing guanine or 7,8-dihydro-8-oxoguanine by base excision repair thereby preventing G:C to T:A mutations. MYH has been shown to interact with the proliferating cell nuclear antigen (PCNA) in both human and fission yeast Schizosaccharomyces pombe systems. Here we show that S. pombe (Sp) MYH physically interacts with all subunits of the PCNA-like checkpoint protein heterotrimer, SpRad9/SpRad1/SpHus1, in yeast extracts and when the individual subunits are expressed in bacteria. The SpHus1 and SpPCNA binding sites are located in discrete regions of SpMYH. Immunoprecipitation assays reveal that the interaction between SpHus1 and SpMYH increases dramatically after hydrogen peroxide treatment, and this increase in the SpHus1-SpMYH interaction correlates with the presence of SpHus1 phosphorylation. In contrast, the interaction between SpPCNA and SpMYH after hydrogen peroxide treatment remains nearly unchanged. SpMYH associates with SpHus1 in a complex of approximately 450 kDa, the reported native molecular mass of the SpRad9/SpRad1/SpHus1-MYC complex. A larger portion of SpMYH shifts to the 150-500-kDa regions after hydrogen peroxide treatment in comparison with untreated extracts. SpHus1 phosphorylation is substantially reduced in SpMYH Delta cells after hydrogen peroxide treatment. These data suggest that MYH may act as an adaptor to recruit checkpoint proteins to the DNA lesions.","authors":"Chang DY, Lu AL","authors_abbrev":"Chang DY et al.","pubmed_publication_date":"07 Jan 2005","pubmed_entrez_date":"2004-11-10","publication_year":"2005","canto_session_key":"7b4c9e930c511158","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-03-05 08:53:07","canto_approved_date":"2021-03-09 08:49:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-03 16:56:22","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPAC664.07c","SPBC336.04","SPBC16D10.09","SPAC26A3.02","SPAC20G4.04c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-03-05"},{"uniquename":"PMID:2165074","title":"Higher-order chromosome structure in yeast.","citation":"J Cell Sci 1990 May;96 ( Pt 1):1-3","abstract":"","authors":"Yanagida M","authors_abbrev":"Yanagida M","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12058077","title":"A polymer model for large-scale chromatin organization in lower eukaryotes.","citation":"Mol Biol Cell 2002 Jun;13(6):2157-69","abstract":"A quantitative model of large-scale chromatin organization was applied to nuclei of fission yeast Schizosaccharomyces pombe (meiotic prophase and G2 phase), budding yeast Saccharomyces cerevisiae (young and senescent cells), Drosophila (embryonic cycles 10 and 14, and polytene tissues) and Caenorhabditis elegans (G1 phase). The model is based on the coil-like behavior of chromosomal fibers and the tight packing of discrete chromatin domains in a nucleus. Intrachromosomal domains are formed by chromatin anchoring to nuclear structures (e.g., the nuclear envelope). The observed sizes for confinement of chromatin diffusional motion are similar to the estimated sizes of corresponding domains. The model correctly predicts chromosome configurations (linear, Rabl, loop) and chromosome associations (homologous pairing, centromere and telomere clusters) on the basis of the geometrical constraints imposed by nuclear size and shape. Agreement between the model predictions and literature observations supports the notion that the average linear density of the 30-nm chromatin fiber is approximately 4 nucleosomes per 10 nm contour length.","authors":"Ostashevsky J","authors_abbrev":"Ostashevsky J","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-06-12","publication_year":"2002","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32406497","title":"Establishing correct kinetochore-microtubule attachments in mitosis and meiosis.","citation":"Essays Biochem 2020 Sep 04;64(2):277-287","abstract":"Faithful chromosome segregation in mitosis and meiosis requires that chromosomes properly attach to spindle microtubules. Initial kinetochore-microtubule attachments are often incorrect and rely on error correction mechanisms to release improper attachments, allowing the formation of new attachments. Aurora B kinase and, in mammalian germ cells, Aurora C kinase function as the enzymatic component of the Chromosomal Passenger Complex (CPC), which localizes to the inner centromere/kinetochore and phosphorylates kinetochore proteins for microtubule release during error correction. In this review, we discuss recent findings of the molecular pathways that regulate the chromosomal localization of Aurora B and C kinases in human cell lines, mice, fission yeast, and budding yeast. We also discuss differences in the importance of localization pathways between mitosis and meiosis.","doi":"10.1042/EBC20190072","authors":"Cairo G, Lacefield S","authors_abbrev":"Cairo G et al.","pubmed_publication_date":"04 Sep 2020","pubmed_entrez_date":"2020-05-15","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-05-16 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1322.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:36376357","title":"A new negative feedback mechanism for MAPK pathway inactivation through Srk1 MAPKAP kinase.","citation":"Sci Rep 2022 Nov 14;12(1):19501","abstract":"The fission yeast mitogen-activated kinase (MAPK) Sty1 is essential for cell survival in response to different environmental insults. In unstimulated cells, Sty1 forms an inactive ternary cytoplasmatic complex with the MAPKK Wis1 and the MAPKAP kinase Srk1. Wis1 phosphorylates and activates Sty1, inducing the nuclear translocation of the complex. Once in the nucleus, Sty1 phosphorylates and activates Srk1, which in turns inhibits Cdc25 and cell cycle progression, before being degraded in a proteasome-dependent manner. In parallel, active nuclear Sty1 activates the transcription factor Atf1, which results in the expression of stress response genes including pyp2 (a MAPK phosphatase) and srk1. Despite its essentiality in response to stress, persistent activation of the MAPK pathway can be deleterious and induces cell death. Thus, timely pathway inactivation is essential to ensure an appropriate response and cell viability. Here, uncover a role for the MAPKAP kinase Srk1 as an essential component of a negative feedback loop regulating the Sty1 pathway through phosphorylation and inhibition of the Wis1 MAPKK. This feedback regulation by a downstream kinase in the pathway highlights an additional mechanism for fine-tuning of MAPK signaling. Thus, our results indicate that Srk1 not only facilitates the adaptation to stress conditions by preventing cell cycle progression, but also plays an instrumental role regulating the upstream kinases in the stress MAPK pathway.","doi":"10.1038/s41598-022-23970-8","authors":"Marquina M, Lambea E, Carmona M, Sánchez-Marinas M, López-Aviles S, Ayte J, Hidalgo E, Aligue R","authors_abbrev":"Marquina M et al.","pubmed_publication_date":"14 Nov 2022","pubmed_entrez_date":"2022-11-14","publication_year":"2022","canto_session_key":"4a873cf629f88b33","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-11-17 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2630560","title":"Actin is associated with the formation of the cell wall in reverting protoplasts of the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1989 Dec;94 ( Pt 4):635-46","abstract":"To clarify the involvement of actin in the formation of the yeast cell wall, reverting protoplasts of Schizosaccharomyces pombe were used as a simple model system. Actin of reverting protoplasts was labeled with rhodamine-conjugated phalloidin and observed by conventional fluorescence microscopy and laser scanning confocal microscopy. A close spatial as well as temporal relationship between actin and cell wall formation was observed in protoplast reversion. That is, the site of actin 'dots' in the reverting protoplasts coincided with the site of new wall formation and the timing of rearrangement of actin coincided with the initiation of cell wall formation and with the timing of cell wall expansion. Treatment of reverting protoplasts with cytochalasin D (CD) further clarified the close relationship between actin and cell wall organization. The effect of CD was dose dependent. A high dose of CD caused the absence of actin as well as the complete inhibition of cell wall formation. A low dose of CD caused weakly stained unlocalized actin, which induced grossly aberrant cell wall deposition as well as substantial changes in the morphology of the reverting protoplasts. These results demonstrated that actin is associated with initiation of cell wall formation, the proper deposition of cell wall materials, and maintaining the normal morphology of reverting protoplasts. Scanning electron microscopy revealed the presence of a fibrillar net structure on the surface of non-treated control reverting protoplasts. However, the absence of a fibrillar network on the surface of reverting protoplasts was observed in the presence of a high concentration of CD. Lack of localization of microfibrils as well as poor development of the fibrillar network were also observed in the presence of a low concentration of CD. Recovery experiments confirmed the close relationship between actin and cell wall formation.","authors":"Kobori H, Yamada N, Taki A, Osumi M","authors_abbrev":"Kobori H et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17658285","title":"Coupling of double-stranded RNA synthesis and siRNA generation in fission yeast RNAi.","citation":"Mol Cell 2007 Aug 03;27(3):449-61","abstract":"The fission yeast centromeric repeats are transcribed and ultimately processed into small interfering RNAs (siRNAs) that are required for heterochromatin formation. siRNA generation requires dsRNA synthesis by the RNA-directed RNA polymerase complex (RDRC) and processing by the Dicer ribonuclease. Here we show that Dcr1, the fission yeast Dicer, is physically associated with RDRC. Dcr1 generates siRNAs in an ATP-dependent manner that requires its conserved N-terminal helicase domain. Furthermore, C-terminal truncations of Dcr1 that abolish its interaction with RDRC, but can generate siRNA in vitro, abolish siRNA generation and heterochromatic gene silencing in vivo. Finally, reconstitution experiments show that the association of Dcr1 with RDRC strongly stimulates the dsRNA synthesis activity of RDRC. Our results suggest that heterochromatic dsRNA synthesis and siRNA generation are physically coupled processes. This coupling has implications for cis-restriction of siRNA-mediated heterochromatin assembly and for mechanisms that give rise to siRNA strand polarity.","authors":"Colmenares SU, Buker SM, Buhler M, Dlakić M, Moazed D","authors_abbrev":"Colmenares SU et al.","pubmed_publication_date":"03 Aug 2007","pubmed_entrez_date":"2007-07-31","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2170029","title":"Distinct, essential roles of type 1 and 2A protein phosphatases in the control of the fission yeast cell division cycle.","citation":"Cell 1990 Oct 19;63(2):405-15","abstract":"The activities of type 1 protein phosphatase (PP1) and 2A (PP2A) have distinct, essential roles in cell cycle control. Two previously identified PP1 genes (dis2+ and sds21+) and two PP2A genes (ppa1+ and ppa2+), highly homologous to mammalian PP2A, have been isolated from fission yeast. Only double gene disruption of both PP2A genes results in lethality, as is the case for PP1 genes. By fractionating and assaying PPases in wild-type, various deletion, and point mutant strains, the decrease of PP1 or PP2A activity is shown to cause mitotic defects, exhibiting strikingly different cell cycle phenotypes: cold-sensitive mutations in the same amino acid lesion of PP1 and PP2A produce chromosome nondisjunction and premature mitosis, respectively. Consistently, PP1 and PP2A genes cannot be functionally substituted. Although the overall levels of PP1 and PP2A activities do not fluctuate during the cell cycle, subpopulations might be regulated.","authors":"Kinoshita N, Ohkura H, Yanagida M","authors_abbrev":"Kinoshita N et al.","pubmed_publication_date":"19 Oct 1990","pubmed_entrez_date":"1990-10-19","publication_year":"1990","canto_session_key":"760d48a1560efbfc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 14:22:36","canto_approved_date":"2023-12-23 15:41:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-05 16:21:27","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":31,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.02c","SPBC16H5.07c","SPCC31H12.05c","SPAC823.15"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-09-17"},{"uniquename":"PMID:5969223","title":"[Importance of after-treatment for fixation of radiation damage (experiments with Schizosaccharomyces pombe with fast neutrons and soft X rays)].","citation":"Radiol Clin Biol 1966;35(6):353-7","abstract":"","authors":"Blattmann H","authors_abbrev":"Blattmann H","pubmed_publication_date":"1966","pubmed_entrez_date":"1966-01-01","publication_year":"1966","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2665944","title":"Regulation of p34cdc2 protein kinase during mitosis.","citation":"Cell 1989 Jul 28;58(2):361-72","abstract":"The cell-cycle timing of mitosis in fission yeast is determined by the cdc25+ gene product activating the p34cdc2 protein kinase leading to mitotic initiation. Protein kinase activity remains high in metaphase and then declines during anaphase. Activation of the protein kinase also requires the cyclin homolog p56cdc13, which also functions post activation at a later stage of mitosis. The continuing function of p56cdc13 during mitosis is consistent with its high level until the metaphase/anaphase transition. At anaphase the p56cdc13 level falls dramatically just before the decline in p34cdc2 protein kinase activity. The behavior of p56cdc13 is similar to that observed for cyclins in oocytes. p13suc1 interacts closely with p34cdc2; it is required during the process of mitosis and may play a role in the inactivation of the p34cdc2 protein kinase. Therefore, the cdc25+, cdc13+, and suc1+ gene products are important for regulating p34cdc2 protein kinase activity during entry into, progress through, and exit from mitosis.","authors":"Moreno S, Hayles J, Nurse P","authors_abbrev":"Moreno S et al.","pubmed_publication_date":"28 Jul 1989","pubmed_entrez_date":"1989-07-28","publication_year":"1989","canto_session_key":"8759012da61b3559","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-28 22:12:14","canto_approved_date":"2026-01-31 15:50:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-18 10:37:49","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPBC11B10.09","SPBC1734.14c","SPBC582.03","SPAC24H6.05"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-04-28"},{"uniquename":"PMID:15166138","title":"A novel gene, msa1, inhibits sexual differentiation in Schizosaccharomyces pombe.","citation":"Genetics 2004 May;167(1):77-91","abstract":"Sexual differentiation in the fission yeast Schizosaccharomyces pombe is triggered by nutrient starvation or by the presence of mating pheromones. We identified a novel gene, msa1, which encodes a 533-aa putative RNA-binding protein that inhibits sexual differentiation. Disruption of the msa1 gene caused cells to hypersporulate. Intracellular levels of msa1 RNA and Msa1 protein diminished after several hours of nitrogen starvation. Genetic analysis suggested that the function of msa1 is independent of the cAMP pathway and stress-responsive pathway. Deletion of the ras1 gene in diploid cells inhibited sporulation and in haploid cells decreased expression of mating-pheromone-induced genes such as mei2, mam2, ste11, and rep1; simultaneous deletion of msa1 reversed both phenotypes. Overexpression of msa1 decreased activated Ras1(Val17)-induced expression of mam2. Phenotypic hypersporulation was similar between cells with deletion of only rad24 and both msa1 and rad24, but simultaneous deletion of msa1 and msa2/nrd1 additively increased hypersporulation. Therefore, we suggest that the primary function of Msa1 is to negatively regulate sexual differentiation by controlling the expression of Ste11-regulated genes, possibly through the pheromone-signaling pathway.","authors":"Jeong HT, Ozoe F, Tanaka K, Nakagawa T, Matsuda H, Kawamukai M","authors_abbrev":"Jeong HT et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-05-29","publication_year":"2004","canto_session_key":"9f2a88f45c75895b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-27 14:07:44","canto_approved_date":"2024-03-28 18:09:46","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-05-06 15:59:59","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPAC8C9.03","SPAC27D7.03c","SPAC13G7.13c","SPAC11H11.04","SPBC106.10","SPAC2F7.11","SPCC285.09c","SPAC8E11.02c","SPBC32C12.02","SPBC19C7.03","SPAC24B11.06c","SPBC2D10.06"],"gene_count":13,"ltp_gene_count":9,"approved_date":"2015-04-27"},{"uniquename":"PMID:2065658","title":"A specific DNA sequence is required for high frequency of recombination in the ade6 gene of fission yeast.","citation":"EMBO J 1991 Aug;10(8):2157-63","abstract":"The point mutation M26 in the ade6 gene of Schizosaccharomyces pombe increases recombination frequency by an order of magnitude in comparison with other mutations in the same gene. The hypothesis is tested that this hot spot of recombination requires a specific nucleotide sequence at the M26 site. The DNA sequence is altered systematically by in vitro mutagenesis, and the resulting sequences are introduced into the ade6 gene in vivo by gene replacement. It results that any change of the heptanucleotide ATGACGT leads to loss of high frequency of recombination. Thus this oligonucleotide sequence is necessary for high frequency of recombination, but it seems not to be sufficient.","authors":"Schuchert P, Langsford M, Käslin E, Kohli J","authors_abbrev":"Schuchert P et al.","pubmed_publication_date":"Aug 1991","pubmed_entrez_date":"1991-08-01","publication_year":"1991","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34246071","title":"Biochemical properties of fission yeast homologous recombination enzymes.","citation":"Curr Opin Genet Dev 2021 Dec;71:19-26","abstract":"Homologous recombination (HR) is a universal phenomenon conserved from viruses to humans. The mechanisms of HR are essentially the same in humans and simple unicellular eukaryotes like yeast. Two highly diverged yeast species, Saccharomyces cerevisiae and Schizosaccharomyces pombe, have proven exceptionally useful in understanding the fundamental mechanisms of eukaryotic HR by serving as a source for unique biological insights and also complementing each other. Here, we will review the features of S. pombe HR mechanisms in comparison to S. cerevisiae and other model organisms. Particular emphasis will be put on the biochemical characterization of HR mechanisms uncovered using S. pombe proteins.","doi":"10.1016/j.gde.2021.06.006","authors":"Tsubouchi H, Argunhan B, Iwasaki H","authors_abbrev":"Tsubouchi H et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-07-10","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-07-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9271112","title":"Phylogenetic relationships of fungal cytochromes c.","citation":"Yeast 1997 Aug;13(10):985-90","abstract":"The CYC1 gene encoding cytochrome c in the yeast Candida albicans was cloned by complementation of a cytochrome c-deficient mutant of Saccharomyces cerevisiae, and its DNA sequence was determined. The analysis of the amino acid sequences of cytochrome c from 14 fungal species and two isoforms from S. cerevisiae revealed sequences unique to fungi, and revealed a phylogenetic relationship with a pronounced divergence between Schizosaccharomyces pombe and other ascomycetous budding yeast.","authors":"Janbon G, Rustchenko EP, Klug S, Scherer S, Sherman F","authors_abbrev":"Janbon G et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18951025","title":"The SIN kinase Sid2 regulates cytoplasmic retention of the S. pombe Cdc14-like phosphatase Clp1.","citation":"Curr Biol 2008 Oct 28;18(20):1594-9","abstract":"Cdc14-family phosphatases play a conserved role in promoting mitotic exit and cytokinesis by dephosphorylating substrates of cyclin-dependent kinase (Cdk). Cdc14-family phosphatases have been best studied in yeast (for review, see [1, 2]), where budding yeast Cdc14 and its fission yeast homolog Clp1 are regulated partly by their localization; both proteins are thought to be sequestered in the nucleolus in interphase. Cdc14 and Clp1 are released from the nucleolus in mitosis, and in late mitosis conserved signaling pathways termed the mitotic exit network (MEN) and the septation initiation network (SIN) keeps Cdc14 and Clp1, respectively, out of the nucleolus through an unknown mechanism [3-6]. Here we show that the most downstream SIN component, the Ndr-family kinase Sid2, maintains Clp1 in the cytoplasm in late mitosis by phosphorylating Clp1 directly and thereby creating binding sites for the 14-3-3 protein Rad24. Mutation of the Sid2 phosphorylation sites on Clp1 disrupts the Clp1-Rad24 interaction and causes Clp1 to return prematurely to the nucleolus during cytokinesis. Loss of Clp1 from the cytoplasm in telophase renders cells sensitive to perturbation of the actomyosin ring but does not affect other Clp1 functions. Because all components of this pathway are conserved, this might be a broadly conserved mechanism for regulation of Cdc14-family phosphatases.","doi":"10.1016/j.cub.2008.08.067","authors":"Chen CT, Feoktistova A, Chen JS, Shim YS, Clifford DM, Gould KL, McCollum D","authors_abbrev":"Chen CT et al.","pubmed_publication_date":"28 Oct 2008","pubmed_entrez_date":"2008-10-28","publication_year":"2008","canto_session_key":"b5b9e2e7b7d1213e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-02 14:09:50","canto_approved_date":"2025-03-24 16:53:11","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-02-27 08:48:45","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":39,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPCC736.14","SPCC645.05c","SPAC8E11.02c","SPCC4B3.15","SPAC20G8.05c","SPAC1782.09c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-10-02"},{"uniquename":"PMID:19410539","title":"Frodos found: Behold the CENP-a \"Ring\" bearers.","citation":"Cell 2009 May 01;137(3):409-12","abstract":"CENP-A is a histone H3-like protein specific to centromeres that is essential for kinetochore formation and accurate chromosome segregation in eukaryotes. Recent studies (Dunleavy et al., 2009; Foltz et al., 2009; Perpelescu et al., 2009; Pidoux et al., 2009; Williams et al., 2009) analyze CENP-A binding proteins required for the recruitment of CENP-A to centromeres in humans and in fission yeast, bringing us closer to understanding how centromere identity is faithfully propagated.","doi":"10.1016/j.cell.2009.04.035","authors":"Mellone BG, Zhang W, Karpen GH","authors_abbrev":"Mellone BG et al.","pubmed_publication_date":"01 May 2009","pubmed_entrez_date":"2009-05-05","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010415","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17072889","title":"Double-strand break repair and homologous recombination in Schizosaccharomyces pombe.","citation":"Yeast 2006 Oct 15;23(13):963-76","abstract":"The study of double-strand break repair and homologous recombination in Saccharomyces cerevisiae meiosis has provided important information about the mechanisms involved. However, it has become clear that the resulting recombination models are only partially applicable to repair in mitotic cells, where crossover formation is suppressed. In recent years our understanding of double-strand break repair and homologous recombination in Schizosaccharomyces pombe has increased significantly, and the identification of novel pathways and genes with homologues in higher eukaryotes has increased its value as a model organism for double-strand break repair. In this review we will focus on the involvement of homologous recombination and repair in different aspects of genome stability in Sz. pombe meiosis, replication and telomere maintenance. We will also discuss anti-recombination pathways (that suppress crossover formation), non-homologous end-joining, single-strand annealing and factors that influence the choice and prevalence of the different repair pathways in Sz. pombe.","authors":"Raji H, Hartsuiker E","authors_abbrev":"Raji H et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32032353","title":"Dramatically diverse Schizosaccharomyces pombe wtf meiotic drivers all display high gamete-killing efficiency.","citation":"PLoS Genet 2020 Feb;16(2):e1008350","abstract":"Meiotic drivers are selfish alleles that can force their transmission into more than 50% of the viable gametes made by heterozygotes. Meiotic drivers are known to cause infertility in a diverse range of eukaryotes and are predicted to affect the evolution of genome structure and meiosis. The wtf gene family of Schizosaccharomyces pombe includes both meiotic drivers and drive suppressors and thus offers a tractable model organism to study drive systems. Currently, only a handful of wtf genes have been functionally characterized and those genes only partially reflect the diversity of the wtf gene family. In this work, we functionally test 22 additional wtf genes for meiotic drive phenotypes. We identify eight new drivers that share between 30-90% amino acid identity with previously characterized drivers. Despite the vast divergence between these genes, they generally drive into >85% of gametes when heterozygous. We also identify three wtf genes that suppress other wtf drivers, including two that also act as autonomous drivers. Additionally, we find that wtf genes do not underlie a weak (64% allele transmission) meiotic driver on chromosome 1. Finally, we find that some Wtf proteins have expression or localization patterns that are distinct from the poison and antidote proteins encoded by drivers and suppressors, suggesting some wtf genes may have non-meiotic drive functions. Overall, this work expands our understanding of the wtf gene family and the burden selfish driver genes impose on S. pombe.","doi":"10.1371/journal.pgen.1008350","authors":"Bravo Núñez MA, Sabbarini IM, Eickbush MT, Liang Y, Lange JJ, Kent AM, Zanders SE","authors_abbrev":"Bravo Núñez MA et al.","pubmed_publication_date":"Feb 2020","pubmed_entrez_date":"2020-02-08","publication_year":"2020","canto_session_key":"cf34c0340e2dff28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maria Angelica Bravo Nunez","canto_first_approved_date":"2020-04-16 16:08:19","canto_approved_date":"2025-09-03 11:32:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-03 20:02:19","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"Maria Angelica Bravo Nunez","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1450.08c","SPCC1739.15","SPAC2E12.05","SPCC285.07c","SPCC1906.04","SPCC1183.10","SPCC736.05","SPCC794.02","SPCC970.11c","SPCC548.03c","SPCC663.17","SPCC1906.03","SPCC162.04c","SPCC1281.08","SPCC1919.06c","SPCC1620.02","SPCC663.02"],"gene_count":17,"ltp_gene_count":9,"approved_date":"2020-04-16"},{"uniquename":"PMID:30475921","title":"A suppressor of a wtf poison-antidote meiotic driver acts via mimicry of the driver's antidote.","citation":"PLoS Genet 2018 Nov;14(11):e1007836","abstract":"Meiotic drivers are selfish alleles that subvert gametogenesis to increase their transmission into progeny. Drivers impose a fitness cost, putting pressure on the genome to evolve suppressors. Here we investigate the wtf gene family from Schizosaccharomyces pombe, previously shown to contain meiotic drivers in wild isolates. We discovered that wtf13 found in lab stocks is a meiotic driver. wtf13 kills spores that do not inherit it by generating both a diffusible poison and a spore-specific antidote. Additionally, we demonstrate that wtf13 is suppressed by another wtf gene, wtf18-2, that arose spontaneously in the lab and makes only an antidote. Wtf18-2 does not act indiscriminately to prevent spore destruction. Instead, it rescues only the spores that inherit wtf18-2. In this way, wtf18-2 selfishly gains a transmission advantage of its own while dampening the drive of wtf13. This establishes a novel paradigm for meiotic drive suppressors and provides insight into the mechanisms and evolution of drive systems.","doi":"10.1371/journal.pgen.1007836","authors":"Bravo Núñez MA, Lange JJ, Zanders SE","authors_abbrev":"Bravo Núñez MA et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-11-27","publication_year":"2018","canto_session_key":"6c6dece2e0762651","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maria Angelica Bravo Nunez","canto_first_approved_date":"2019-01-16 10:33:33","canto_approved_date":"2025-12-23 12:50:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-01 14:33:53","canto_added_date":"2018-11-28 01:15:05","annotation_curators":[{"name":"Maria Angelica Bravo Nunez","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC285.07c","SPCC162.04c","SPCC1906.03","SPCC1620.02"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2019-01-16"},{"uniquename":"PMID:16641370","title":"Postreplication repair and PCNA modification in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2006 Jul;17(7):2976-85","abstract":"Ubiquitination of proliferating cell nuclear antigen (PCNA) plays a crucial role in regulating replication past DNA damage in eukaryotes, but the detailed mechanisms appear to vary in different organisms. We have examined the modification of PCNA in Schizosaccharomyces pombe. We find that, in response to UV irradiation, PCNA is mono- and poly-ubiquitinated in a manner similar to that in Saccharomyces cerevisiae. However in undamaged Schizosaccharomyces pombe cells, PCNA is ubiquitinated in S phase, whereas in S. cerevisiae it is sumoylated. Furthermore we find that, unlike in S. cerevisiae, mutants defective in ubiquitination of PCNA are also sensitive to ionizing radiation, and PCNA is ubiquitinated after exposure of cells to ionizing radiation, in a manner similar to the response to UV-irradiation. We show that PCNA modification and cell cycle checkpoints represent two independent signals in response to DNA damage. Finally, we unexpectedly find that PCNA is ubiquitinated in response to DNA damage when cells are arrested in G2.","authors":"Frampton J, Irmisch A, Green CM, Neiss A, Trickey M, Ulrich HD, Furuya K, Watts FZ, Carr AM, Lehmann AR","authors_abbrev":"Frampton J et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-04-28","publication_year":"2006","canto_session_key":"9acbc08512cc3f3b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-03-09 14:36:58","canto_approved_date":"2022-08-01 15:37:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-22 08:56:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC11E3.04c","SPAC644.14c","SPCC338.05c","SPBC216.05","SPBC16D10.09","SPAC13G6.01c","SPBC1734.06"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-03-09"},{"uniquename":"PMID:24186062","title":"Epigenetically induced paucity of histone H2A.Z stabilizes fission-yeast ectopic centromeres.","citation":"Nat Struct Mol Biol 2013 Dec;20(12):1397-406","abstract":"In most eukaryotes, centromeres are epigenetically defined by nucleosomes that contain the histone H3 variant centromere protein A (CENP-A). Specific targeting of the CENP-A-loading chaperone to the centromere is vital for stable centromere propagation; however, the existence of ectopic centromeres (neocentromeres) indicates that this chaperone can function in different chromatin environments. The mechanism responsible for accommodating the CENP-A chaperone at noncentromeric regions is poorly understood. Here, we report the identification of transient, immature neocentromeres in Schizosaccharomyces pombe that show reduced association with the CENP-A chaperone Scm3, owing to persistence of the histone H2A variant H2A.Z. After the acquisition of adjacent heterochromatin or relocation of the immature neocentromeres to subtelomeric regions, H2A.Z was depleted and Scm3 was replenished, thus leading to subsequent stabilization of the neocentromeres. These findings provide new insights into histone variant-mediated epigenetic control of neocentromere establishment.","doi":"10.1038/nsmb.2697","authors":"Ogiyama Y, Ohno Y, Kubota Y, Ishii K","authors_abbrev":"Ogiyama Y et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-05","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29234671","title":"A new role for the nuclear basket network.","citation":"Microb Cell 2017 Nov 27;4(12):423-425","abstract":"Our view of the nuclear pore complexes (NPCs) as gateways between the nuclear and cytoplasmic compartments has been largely expanded in recent years. NPCs have now demonstrated roles in genome regulation and maintenance from single cells to multicellular organisms. Both NPC proteins as well as components of the NPC basket act as dynamic scaffolds for silencing factors, and chromatin and cell cycle regulators. Components of the NPC basket also couple mRNA production and export, and prevent the exit of unprocessed mRNAs from the nucleus. Our recent work describes a novel function of the fission yeast nuclear basket component - the translocated promoter region (TPR) nucleoporin Alm1 - in proper localization of the proteasome to the nuclear envelope. Here we discuss how regulation of proteasome localization to the nuclear envelope by Alm1 is key to maintain kinetochores homeostasis and proper chromosome segregation.","doi":"10.15698/mic2017.12.604","authors":"Gallardo P, Salas-Pino S, Daga RR","authors_abbrev":"Gallardo P et al.","pubmed_publication_date":"27 Nov 2017","pubmed_entrez_date":"2017-12-14","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-12-15 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1486.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1508697","title":"Cloning of the gene for ribosomal protein S13 from the fission yeast Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1992 Aug 11;20(15):4094","abstract":"","authors":"Marks J, Simanis V","authors_abbrev":"Marks J et al.","pubmed_publication_date":"11 Aug 1992","pubmed_entrez_date":"1992-08-11","publication_year":"1992","canto_session_key":"03060dd37ac11344","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-04-20 17:07:11","canto_session_submitted_date":"2012-04-20 17:05:56","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-04-20"},{"uniquename":"PMID:28054638","title":"Functional constraints on adaptive evolution of protein ubiquitination sites.","citation":"Sci Rep 2017 Jan 05;7:39949","abstract":"It is still unclear whether there exist functional constraints on the evolution of protein ubiquitination sites, because most previous studies regarded all protein ubiquitination sites as a whole or only focused on limited structural properties. We tried to clarify the relation between functional constraints and ubiquitination sites evolution. We investigated the evolutionary conservation of human ubiquitination sites in a broad evolutionary scale from G. gorilla to S. pombe, and we found that in organisms originated after the divergence of vertebrate, ubiquitination sites are more conserved than their flanking regions, while the opposite tendency is observed before this divergence time. By grouping the ubiquitination proteins into different functional categories, we confirm that many functional constraints like certain molecular functions, protein tissue expression specificity and protein connectivity in protein-protein interaction network enhance the evolutionary conservation of ubiquitination sites. Furthermore, by analyzing the gains of ubiquitination sites at different divergence time and their functional characters, we validate that the emergences of ubiquitination sites at different evolutionary time were also affected by the uncovered functional constraints. The above results suggest that functional constraints on the adaptive evolution of ubiquitination sites increase the opportunity for ubiquitination to synthetically regulate various cellular and developmental processes during evolution.","doi":"10.1038/srep39949","authors":"Lu L, Li Y, Liu Z, Liang F, Guo F, Yang S, Wang D, He Y, Xiong J, Li D, He F","authors_abbrev":"Lu L et al.","pubmed_publication_date":"05 Jan 2017","pubmed_entrez_date":"2017-01-06","publication_year":"2017","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2017-01-07 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15454577","title":"The GIN4 family kinase, Cdr2p, acts independently of septins in fission yeast.","citation":"J Cell Sci 2004 Oct 15;117(Pt 22):5293-302","abstract":"Two relatives of the GIN4 protein kinase family, Cdr1p and Cdr2p, exist in the yeast Schizosaccharomyces pombe. Although in Saccharomyces cerevisiae GIN4-related kinases influence septin ring organization and septin rings influence the localization and function of GIN4-related protein kinases, it is unknown whether this relationship is conserved in S. pombe. Here, we have probed the relationship between Cdr2p activity and septins and find that Cdr2p and septins are functionally independent. Cdr2p localizes in a cortical band overlying the nucleus during interphase, whose dimension is proportional to cell length, and to a medial ring structure in late mitosis. Both localizations are septin-independent and disrupted by treatment with filipin. Structure/function analysis indicates that the intracellular targeting domain of Cdr2p is largely contained within its non-catalytic C-terminus. Cdr2 protein kinase activity, while unimportant for its localization, is critical for its cell cycle function. Our data indicate that Cdr2p functions at two positions within the cell at discrete cell cycle stages to influence the timing of mitotic entry and cytokinesis, respectively.","authors":"Morrell JL, Nichols CB, Gould KL","authors_abbrev":"Morrell JL et al.","pubmed_publication_date":"15 Oct 2004","pubmed_entrez_date":"2004-09-30","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A10.02"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:29782206","title":"Active transport of cytoophidia in Schizosaccharomyces pombe.","citation":"FASEB J 2018 Nov;32(11):5891-5898","abstract":"The metabolic enzyme cytidine triphosphate synthase has recently been found to form micrometer-sized filamentous structures termed cytoophidia, which are evolutionarily conserved across prokaryotes and eukaryotes. The cytoophidium represents a novel type of membraneless organelle and behaves dynamically inside the cell. The question of how cytoophidia transport is mediated, however, remains unanswered. For the first time, we detected in this study the active transport of cytoophidia, taking advantage of the fission yeast Schizosaccharomyces pombe as an excellent model for studying membraneless organelles. We demonstrated that actin filaments, not microtubules, are responsible for this transport. Furthermore, we determined that Myo52, a type of myosin V, is required for the active transport of cytoophidia. These results reveal the major players critical to the dynamics of cytoophidia and extend our understanding of intracellular transport of membraneless organelles.-Li, H., Ye, F., Ren, J.-Y., Wang, P.-Y., Du, L.-L., Liu, J.-L. Active transport of cytoophidia in Schizosaccharomyces pombe.","doi":"10.1096/fj.201800045RR","authors":"Li H, Ye F, Ren JY, Wang PY, Du LL, Liu JL","authors_abbrev":"Li H et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-05-22","publication_year":"2018","canto_session_key":"32c79e9290b05138","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-05-23 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24014766","title":"Structural and functional characterization of the N terminus of Schizosaccharomyces pombe Cwf10.","citation":"Eukaryot Cell 2013 Nov;12(11):1472-89","abstract":"The spliceosome is a dynamic macromolecular machine that catalyzes the removal of introns from pre-mRNA, yielding mature message. Schizosaccharomyces pombe Cwf10 (homolog of Saccharomyces cerevisiae Snu114 and human U5-116K), an integral member of the U5 snRNP, is a GTPase that has multiple roles within the splicing cycle. Cwf10/Snu114 family members are highly homologous to eukaryotic translation elongation factor EF2, and they contain a conserved N-terminal extension (NTE) to the EF2-like portion, predicted to be an intrinsically unfolded domain. Using S. pombe as a model system, we show that the NTE is not essential, but cells lacking this domain are defective in pre-mRNA splicing. Genetic interactions between cwf10-ΔNTE and other pre-mRNA splicing mutants are consistent with a role for the NTE in spliceosome activation and second-step catalysis. Characterization of Cwf10-NTE by various biophysical techniques shows that in solution the NTE contains regions of both structure and disorder. The first 23 highly conserved amino acids of the NTE are essential for its role in splicing but when overexpressed are not sufficient to restore pre-mRNA splicing to wild-type levels in cwf10-ΔNTE cells. When the entire NTE is overexpressed in the cwf10-ΔNTE background, it can complement the truncated Cwf10 protein in trans, and it immunoprecipitates a complex similar in composition to the late-stage U5.U2/U6 spliceosome. These data show that the structurally flexible NTE is capable of independently incorporating into the spliceosome and improving splicing function, possibly indicating a role for the NTE in stabilizing conformational rearrangements during a splice cycle.","doi":"10.1128/EC.00140-13","authors":"Livesay SB, Collier SE, Bitton DA, Bähler J, Ohi MD","authors_abbrev":"Livesay SB et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-09-10","publication_year":"2013","canto_session_key":"23eb2cb1b340e956","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-07-09 17:09:49","canto_approved_date":"2024-12-23 22:14:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-09 17:09:31","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":76,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.09","SPAC2C4.03c","SPBC1289.11","SPAC644.12","SPCC550.02c","SPCP1E11.07c","SPBC11C11.08","SPAC16.02c","SPAC22F8.10c","SPBC32F12.05c","SPBC211.02c","SPBC146.05c","SPBC8D2.09c","SPBP22H7.07","SPAC30D11.09","SPAC27F1.09c","SPAC3H5.04","SPBC31F10.11c","SPAC4A8.09c","SPAC23H3.02c","SPAC3A12.11c","SPAC27D7.07c","SPCC962.06c","SPBC19C2.14","SPAC29A4.06c","SPCC1620.10","SPAC4D7.13","SPBC3E7.13c","SPBC6B1.10","SPAC19G12.07c","SPAC26A3.08","SPBC16H5.10c","SPCC188.11","SPBC4B4.05","SPAC9.03c","SPAC22A12.09c","SPAC29A4.08c","SPAC57A10.03","SPBC18H10.10c","SPCC777.14","SPBC4B4.09","SPBC36.09","SPBC215.12","SPAPJ698.03c","SPAC4F8.12c","SPBC11G11.06c","SPBC146.07","SPAC9.13c","SPBC6B1.07","SPBC646.02","SPAC10F6.02c","SPBC1861.08c","SPBC24C6.11","SPBC19C2.01","SPBC3E7.14","SPBC530.14c","SPCC1795.11","SPBC337.06c","SPBC13E7.01","SPAC29E6.02","SPBC1711.17","SPBC28F2.04c"],"gene_count":62,"ltp_gene_count":59,"approved_date":"2024-07-09"},{"uniquename":"EMBL:AU009111","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23453865","title":"Nuclear organisation and RNAi in fission yeast.","citation":"Curr Opin Cell Biol 2013 Jun;25(3):372-7","abstract":"Over the last decade, the fission yeast Schizosaccharomyces pombe has been used extensively for investigating RNA interference (RNAi)-mediated heterochromatin assembly. However, only recently have studies begun to shed light on the 3D organisation of chromatin and the RNAi machinery in the fission yeast nucleus. These studies indicate association of repressive and active chromatin with different regions of the nuclear periphery, similar to other model organisms, and clustering of functionally related genomic features. Unexpectedly, RNAi factors were shown to associate with nuclear pores and were implicated in the regulation of genomic features outside of the well-studied heterochromatic regions. Nuclear organisation is likely to contribute to substrate specificity of the RNAi pathway. However, further studies are required to elucidate the exact mechanisms and functional importance of this nuclear organisation.","doi":"10.1016/j.ceb.2013.02.004","authors":"Woolcock KJ, Bühler M","authors_abbrev":"Woolcock KJ et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-03-05","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009538","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27261767","title":"Use of Schizosaccharomyces strains for wine fermentation-Effect on the wine composition and food safety.","citation":"Int J Food Microbiol 2016 Sep 02;232:63-72","abstract":"Schizosaccharomyces was initially considered as a spoilage yeast because of the production of undesirable metabolites such as acetic acid, hydrogen sulfide, or acetaldehyde, but it currently seems to be of great value in enology.o ced Nevertheless, Schizosaccharomyces can reduce all of the malic acid in must, leading to malolactic fermentation. Malolactic fermentation is a highly complicated process in enology and leads to a higher concentration of biogenic amines, so the use of Schizosaccharomyces pombe can be an excellent tool for assuring wine safety. Schizosaccharomyces also has much more potential than only reducing the malic acid content, such as increasing the level of pyruvic acid and thus the vinylphenolic pyranoanthocyanin content. Until now, few commercial strains have been available and little research on the selection of appropriate yeast strains with such potential has been conducted. In this study, selected and wild Sc. pombe strains were used along with a Saccharomyces cerevisiae strain to ferment red grape must. The results showed significant differences in several parameters including non-volatile and volatile compounds, anthocyanins, biogenic amines and sensory parameters.","doi":"10.1016/j.ijfoodmicro.2016.05.023","authors":"Mylona AE, Del Fresno JM, Palomero F, Loira I, Bañuelos MA, Morata A, Calderón F, Benito S, Suárez-Lepe JA","authors_abbrev":"Mylona AE et al.","pubmed_publication_date":"02 Sep 2016","pubmed_entrez_date":"2016-06-05","publication_year":"2016","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2016-06-06 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PB_REF:0000005","title":"Allele Comments","abstract":"PomBase curators record comments relevant to alleles, but not suitable for inclusion in allele names or descriptions, encountered in the literature, personal communications, or other resources.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39016088","title":"The effect of centromere protein Fta2 phosphorylation during meiosis.","citation":"Yi Chuan 2024 Jul;46(7):552-559","abstract":"During meiosis, defects in cohesin localization within the centromere region can result in various diseases. Accurate cohesin localization depends on the Mis4-Ssl3 loading complex. Although it is known that cohesin completes the loading process with the help of the loading complex, the mechanisms underlying its localization in the centromere region remain unclear. Previous studies suggest cohesin localization in the centromere is mediated by phosphorylation of centromeric proteins. In this study, we focused on the Fta2 protein, a component of the Sim4 centromere protein complex. Using bioinformatics methods, potential phosphorylation sites were identified, and  fta2-9A  and  fta2-9D  mutants were constructed in  Schizosaccharomyces pombe . The phenotypes of these mutants were characterized through testing thiabendazole (TBZ) sensitivity and fluorescent microscopy localization. Results indicated that Fta2 phosphorylation did not impact mitosis but affected chromosome segregation during meiosis. This study suggests that Fta2 phosphorylation is vital for meiosis and may be related to the specific localization of cohesin during this process.","doi":"10.16288/j.yczz.24-038","authors":"Ni ZH, Min Y, Ma LL, Watanabe Y","authors_abbrev":"Ni ZH et al.","pubmed_publication_date":"Jul 2024","pubmed_entrez_date":"2024-07-17","publication_year":"2024","canto_session_key":"43f9f82f0a5c5c77","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2024-09-27 07:30:40","canto_approved_date":"2025-01-31 11:02:30","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-09-26 10:20:37","canto_added_date":"2024-07-17 23:25:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-09-27"},{"uniquename":"PMID:16262791","title":"Identification of novel single amino acid changes that result in hyperactivation of the unique GTPase, Rheb, in fission yeast.","citation":"Mol Microbiol 2005 Nov;58(4):1074-86","abstract":"Rheb GTPase is a key player in the control of growth, cell cycle and nutrient uptake that is conserved from yeast to humans. To further our understanding of the Rheb pathway, we sought to identify hyperactivating mutations in the Schizosaccharomyces pombe Rheb, Rhb1. Hyperactive forms of Rhb1 were found to result from single amino acid changes at valine-17, serine-21, lysine-120 or asparagine-153. Expression of these mutants confers resistance to canavanine and thialysine, phenotypes which are similar to phenotypes exhibited by cells lacking the Tsc1/Tsc2 complex that negatively regulates Rhb1. The thialysine-resistant phenotype of the hyperactive Rhb1 mutants is suppressed by a second mutation in the effector domain. Purified mutant proteins exhibit dramatically decreased binding of GDP, while their GTP binding is not drastically affected. In addition, some of the mutant proteins show significantly decreased GTPase activities. Thus the hyperactivating mutations are expected to result in an increase in the GTP-bound/GDP-bound ratio of Rhb1. By using the hyperactive mutant, Rhb1(K120R), we have been able to demonstrate that Rhb1 interacts with Tor2, one of the two S. pombe TOR (Target of Rapamycin) proteins. These fission yeast results provide the first evidence for a GTP-dependent association of Rheb with Tor.","authors":"Urano J, Comiso MJ, Guo L, Aspuria PJ, Deniskin R, Tabancay AP, Kato-Stankiewicz J, Tamanoi F","authors_abbrev":"Urano J et al.","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-11-03","publication_year":"2005","canto_session_key":"722def8c5161e3f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 16:54:28","canto_approved_date":"2024-01-11 17:05:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-04-19 14:47:24","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":72,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.13c","SPBC428.16c","SPBC216.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-10-31"},{"uniquename":"PMID:9501995","title":"Identification and characterization of a novel trans-membrane protein gene, pdh1, from Schizosaccharomyces pombe.","citation":"DNA Res 1997 Dec 31;4(6):393-6","abstract":"We have cloned a new gene, pdh1, from genomic DNA of fission yeast Schizosaccharomyces pombe. pdh1 is actively transcribed as 1400-nucleotide mRNA in vegetatively growing cells and can code for a 226 amino acid polypeptide (pdh1p). Computational structural prediction has revealed that the pdh1p is a highly hydrophobic protein with seven transmembrane domains. The prediction has also detected a possible C-kinase phosphorylation site within the longest hydrophilic loop.","authors":"Iha H, Takimoto M, Danjoh I, Fujiyama A","authors_abbrev":"Iha H et al.","pubmed_publication_date":"31 Dec 1997","pubmed_entrez_date":"1998-03-21","publication_year":"1997","canto_session_key":"67f9c24d83f9e084","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-29 21:28:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 20:45:32","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1235.08c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-04-29"},{"uniquename":"PMID:3032144","title":"Mitochondrial introns as mobile genetic elements: the role of intron-encoded proteins.","citation":"Basic Life Sci 1986;40:5-27","abstract":"Introns of organelle genes share distinctive RNA secondary structures that allow their classification into two known families. These structures are believed to play an essential role in splicing, and members of both structural classes have recently been shown to perform self-splicing reactions in vitro. In lower eukaryotes, many structured introns also contain long internal open reading frames (ORFs), which are able to code for hydrophilic proteins. Several properties of self-splicing structured introns suggest that they resemble mobile genetic elements, even though no actual transposition event involving these introns has yet been found. We report here on the characterization of two intron-encoded proteins that strongly support this attractive idea. First, we show that the class I intron of the 21S ribosomal RNA (rRNA) gene of Saccharomyces cerevisiae omega+ strains (rl intron) encodes a specific transposase. This protein has been partially purified from Escherichia coli cells that overexpress it from an artificial universal code equivalent to the rl intronic ORF. The omega transposase shows a double-strand endonuclease activity in vitro. This activity creates a 4-bp staggered cut with 3' OH overhangs within a specific sequence of the 21S rRNA gene of omega- strains. It is precisely within this sequence that the rl intron inserts by a duplicative transposition. Second, we report on the synthesis, in E. coli, of a putative reverse transcriptase encoded by the class II intron of the cytochrome b gene of Schizosaccharomyces pombe. This synthesis was obtained from E. coli expression vectors, using the class II intronic ORF linked to an artificial initiator sequence. As further support of the idea that structured introns are mobile, we show, from a systematic screening of introns in various yeast species, that the rl intron has transposed into the ATPase subunit 9 gene of Kluyveromyces fragilis. Structural features observed at the new intron homing site may be relevant to the transposition event.","authors":"Dujon B, Colleaux L, Jacquier A, Michel F, Monteilhet C","authors_abbrev":"Dujon B et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22887981","title":"Contractile-ring assembly in fission yeast cytokinesis: Recent advances and new perspectives.","citation":"Cytoskeleton (Hoboken) 2012 Oct;69(10):751-63","abstract":"The fission yeast Schizosaccharomyces pombe is an excellent model organism to study cytokinesis. Here, we review recent advances on contractile-ring assembly in fission yeast. First, we summarize the assembly of cytokinesis nodes, the precursors of a normal contractile ring. IQGAP Rng2 and myosin essential light chain Cdc4 are recruited by the anillin-like protein Mid1, followed by the addition of other cytokinesis node proteins. Mid1 localization on the plasma membrane is stabilized by interphase node proteins. Second, we discuss proteins and processes that contribute to the search, capture, pull, and release mechanism of contractile-ring assembly. Actin filaments nucleated by formin Cdc12, the motor activity of myosin-II, the stiffness of the actin network, and severing of actin filaments by cofilin all play essential roles in contractile-ring assembly. Finally, we discuss the Mid1-independent pathway for ring assembly, and the possible mechanisms underlying the ring maturation and constriction. Collectively, we provide an overview of the current understanding of contractile-ring assembly and uncover future directions in studying cytokinesis in fission yeast.","doi":"10.1002/cm.21052","authors":"Lee IJ, Coffman VC, Wu JQ","authors_abbrev":"Lee IJ et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-14","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9693066","title":"Cloning of the fatty acid synthetase beta subunit from fission yeast, coexpression with the alpha subunit, and purification of the intact multifunctional enzyme complex.","citation":"Protein Expr Purif 1998 Aug;13(3):403-13","abstract":"We have cloned and sequenced the fission yeast (Schizosaccharomyces pombe) fas1+ gene, which encodes the fatty acid synthetase (FAS) beta subunit, by applying a PCR technique to conserved regions in the beta subunit of the alpha6beta6 types of FAS among different organisms. The deduced amino acid sequence of the Fas1 polypeptide, consisting of 2073 amino acids (Mr = 230,616), exhibits the 48.1% identity with the beta subunit from the budding yeast (Saccharomyces cerevisiae). This subunit, with five different catalytic activities, bears four distinct domains, while the alpha subunit, the sequence of which was previously reported by Saitoh et al. (S. Saitoh et al., 1996, J. Cell Biol. 134, 949-961), carries three domains. We have developed a co-expression system of the FAS alpha and beta subunits by cotransformation of two expression vectors, containing the lsd1+/fas2+ gene and the fas1+ gene, into fission yeast cells. The isolated FAS complex showed quite high specific activity, of more than 4000 mU/mg, suggesting complete purification. Its molecular weight was determined by dynamic light scattering and ultracentrifugation analysis to be 2.1-2.4 x 10(6), and one molecule of the FAS complex was found to contain approximately six FMN molecules. These results indicate that the FAS complex from S. pombe forms a heterododecameric alpha6beta6 structure. Electron micrographs of the negatively stained molecule suggest that the complex adopts a unique barrel-shaped cage architecture.","authors":"Niwa H, Katayama E, Yanagida M, Morikawa K","authors_abbrev":"Niwa H et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-08-07","publication_year":"1998","canto_session_key":"3e8456a6d6a5d6a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-13 23:13:25","canto_approved_date":"2026-01-22 14:47:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-13 23:05:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.09c","SPAC4A8.11c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-12-13"},{"uniquename":"PMID:11349150","title":"Pot1, the putative telomere end-binding protein in fission yeast and humans.","citation":"Science 2001 May 11;292(5519):1171-5","abstract":"Telomere proteins from ciliated protozoa bind to the single-stranded G-rich DNA extensions at the ends of macronuclear chromosomes. We have now identified homologous proteins in fission yeast and in humans. These Pot1 (protection of telomeres) proteins each bind the G-rich strand of their own telomeric repeat sequence, consistent with a direct role in protecting chromosome ends. Deletion of the fission yeast pot1+ gene has an immediate effect on chromosome stability, causing rapid loss of telomeric DNA and chromosome circularization. It now appears that the protein that caps the ends of chromosomes is widely dispersed throughout the eukaryotic kingdom.","authors":"Baumann P, Cech TR","authors_abbrev":"Baumann P et al.","pubmed_publication_date":"11 May 2001","pubmed_entrez_date":"2001-05-12","publication_year":"2001","canto_session_key":"0afc32dc747285ae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-01-07 14:11:02","canto_approved_date":"2022-07-27 12:26:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-25 07:59:02","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPAC26H5.06"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-01-07"},{"uniquename":"PMID:35746791","title":"A Novel Class of HIV-1 Inhibitors Targeting the Vpr-Induced G2-Arrest in Macrophages by New Yeast- and Cell-Based High-Throughput Screening.","citation":"Viruses 2022 Jun 16;14(6)","abstract":"The human immunodeficiency virus type 1 (HIV-1) accessory protein, Vpr, arrests the cell cycle of the G2 phase, and this Vpr-mediated G2 arrest is implicated in an efficient HIV-1 spread in monocyte-derived macrophages. Here, we screened new candidates for Vpr-targeting HIV-1 inhibitors by using fission yeast- and mammalian cell-based high-throughput screening. First, fission yeast strains expressing the HIV-1 Vpr protein were generated and then treated for 48 h with 20 μM of a synthetic library, including 140,000 chemical compounds. We identified 268 compounds that recovered the growth of Vpr-overexpressing yeast. The selected compounds were then tested in mammalian cells, and those displaying high cytotoxicity were excluded from further cell cycle analysis and imaging-based screening. A flow cytometry analysis confirmed that seven compounds recovered from the Vpr-induced G2 arrest. The cell toxicity and inhibitory effect of HIV-1 replication in human monocyte-derived macrophages (MDM) were examined, and three independent structural compounds, VTD227, VTD232, and VTD263, were able to inhibit HIV-1 replication in MDM. Furthermore, we showed that VTD227, but not VTD232 and VTD263, can directly bind to Vpr. Our results indicate that three new compounds and their derivatives represent new drugs targeting HIV-1 replication and can be potentially used in clinics to improve the current antiretroviral therapy.","doi":"10.3390/v14061321","authors":"Sato H, Murakami T, Matsuura R, Abe M, Matsuoka S, Yashiroda Y, Yoshida M, Akari H, Nagasawa Y, Takei M, Aida Y","authors_abbrev":"Sato H et al.","pubmed_publication_date":"16 Jun 2022","pubmed_entrez_date":"2022-06-24","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-06-26 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31657618","title":"A Genome-Wide Screen for Wortmannin-Resistant Mutants in  Schizosaccharomyces pombe:  The Phosphorylation-Impaired Mutants Are Resistant to Signaling Defect.","citation":"DNA Cell Biol 2019 Dec;38(12):1427-1436","abstract":"Complex human diseases such as metabolic disorders, cancer, neurodegenerative diseases, and mitochondrial dysfunctions arise from the biochemical or genetic defects in various cellular processes. Therefore, it is important to understand which metabolic processes are affected by which cellular impairment. Because genome-wide screening of mutant collections (haploid/diploid deletion library) provides important clues for the understanding of conserved biological processes and for finding potential target genes, we screened the haploid mutant collection of  Schizosaccharomyces pombe  with wortmannin that inhibits phosphatidylinositol-3-kinase signaling. Using genome-wide screening, we determined that 52 mutants were resistant to this chemical. When 52 genes that are deleted in these mutants were grouped in 41 different biological processes, we found that 37 of them have human orthologues and 4 genes were associated with human metabolic disorders. In addition, when we examined the pathways in which these 52 genes function, we determined that 9 genes were related to phosphorylation process. These results might provide new insights for better understanding of certain human diseases.","doi":"10.1089/dna.2019.5003","authors":"Yılmazer M, Kartal B, Tarhan Ç, Özarabacı I, Akçaalan S, Özkan E, Karaer Uzuner S, Arıcan E, Palabıyık B","authors_abbrev":"Yılmazer M et al.","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-10-29","publication_year":"2019","canto_session_key":"61b5b08d53bec31b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-06-22 09:05:19","canto_approved_date":"2024-11-28 16:44:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-22 09:05:13","canto_added_date":"2019-10-30 01:15:04","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":61,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC13G1.08c","SPBC24C6.10c","SPAP27G11.10c","SPBC26H8.01","SPBC17A3.05c","SPAC20G4.03c","SPCC1840.10","SPCC188.12","SPBC106.08c","SPCC1322.05c","SPBC19G7.18c","SPAC227.17c","SPCC1020.07","SPAPB8E5.06c","SPAC926.05c","SPBC1604.02c","SPAC1687.15","SPBC146.10","SPBC354.15","SPCC576.02","SPAC9E9.13","SPBC4C3.09","SPBC8D2.18c","SPBC3E7.01","SPCC70.10","SPAC26F1.03","SPCC970.06","SPAC4G8.11c","SPBC21C3.18","SPAC14C4.15c","SPAC869.02c","SPBC725.12","SPBP8B7.27","SPAC31G5.04","SPCC1620.12c","SPBC16G5.15c","SPAC926.03","SPBC1711.03","SPBC27B12.08","SPCC1682.01","SPAC4D7.01c","SPAC222.07c","SPBC146.12","SPBC18H10.15","SPBC29A3.10c","SPBPB21E7.05","SPBC18H10.13","SPAC12B10.15c","SPBC1685.11","SPBC56F2.09c","SPAC22A12.11","SPBC21D10.07"],"gene_count":52,"ltp_gene_count":52,"approved_date":"2023-06-22"},{"uniquename":"PMID:25197549","title":"Practical strategies for the evaluation of high-affinity protein/nucleic acid interactions.","citation":"J Nucleic Acids Investig 2013 Jan 01;4(1):19-28","abstract":"The quantitative evaluation of binding interactions between proteins and nucleic acids is highly sensitive to a variety of experimental conditions. Optimization of these conditions is critical for obtaining high quality, reproducible data, particularly in the context of very high affinity interactions. Here, we discuss the practical considerations involved in optimizing the apparent binding constant of an interaction as measured by two common quantitative assays, electrophoretic mobility shift assay and double-filter binding when measuring extremely tight protein/nucleic acid interactions with sub-nanomolar binding affinities. We include specific examples from two telomere end-binding protein systems,  Schizo -saccharomyces pombe  Pot1 and  Saccharomyces cerevisiae  Cdc13, to demonstrate potential experimental pitfalls and some useful strategies for optimization.","authors":"Altschuler SE, Lewis KA, Wuttke DS","authors_abbrev":"Altschuler SE et al.","pubmed_publication_date":"01 Jan 2013","pubmed_entrez_date":"2014-09-09","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-09-12 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010419","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7398887","title":"The proteinase inhibitor phenylmethylsulfonyl fluoride protects xanthine transport in Schizosaccharomyces pombe against inactivation by ammonium ions.","citation":"FEBS Lett 1980 Jun 30;115(2):289-92","abstract":"","authors":"Seipel S, Reichert U","authors_abbrev":"Seipel S et al.","pubmed_publication_date":"30 Jun 1980","pubmed_entrez_date":"1980-06-30","publication_year":"1980","canto_session_key":"84185b4eb8040a0a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-05 17:05:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-03 14:36:11","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-09-03"},{"uniquename":"EMBL:AU009260","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41463313","title":"Combinatorial Antimicrobial Effects of Imidazolium-Based Ionic Liquids and Antifungals on Model Fungal Organisms.","citation":"Biomolecules 2025 Nov 27;15(12)","abstract":"Ionic Liquids (IL) are a unique class of molten salts, with specific formulations exhibiting antimicrobial properties. Several recent studies have highlighted the ability of ILs to form micelles, permeabilize the plasma membrane, and destabilize cellular structure, ultimately initiating cell death. Moreover, while these membrane-destabilizing properties are cytotoxic to most cellular organisms at high concentrations, their membrane destabilization capability at lower concentrations may lead to improvements in drug delivery for combinatorial therapies against specific microbes. Work presented in this study aimed to identify a synergistic relationship between ILs, 1-n-Hexyl-3-methylimidazolium chloride (HMIM[Cl]) and 1-Methyl-3-n-octylimidazolium chloride (OMIM[Cl]), and antifungal drugs (AF), Clotrimazole, Ketoconazole, Fluconazole, and Itraconazole, with the hypothesis that in a combinatory setting there should be improved AF efficacy against model fungal organisms:  S. boulardii ,  S. cerevisiae ,  S. pombe , and  C. albicans . Several complementary assays were used to identify the combined effects of IL + AF treatment, including Kirby-Bauer tests and minimum inhibitory concentrations (MIC) assays to establish antimicrobial effects, and flow cytometry to evaluate cell wall permeability. Finally, we demonstrate that at low concentrations, the ILs tested in this study are capable of improving the effectiveness of current antifungal compounds at concentrations not cytotoxic to human cells.","doi":"10.3390/biom15121657","authors":"Calixto JG, Fetz PR, Ammerman D, Flores YR, Caputo GA, Vaden TD, Carone BR","authors_abbrev":"Calixto JG et al.","pubmed_publication_date":"27 Nov 2025","pubmed_entrez_date":"2025-12-30","publication_year":"2025","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2025-12-31 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33693625","title":"Dri1 mediates heterochromatin assembly via RNAi and histone deacetylation.","citation":"Genetics 2021 May 17;218(1)","abstract":"Heterochromatin, a transcriptionally silenced chromatin domain, is important for genome stability and gene expression. Histone 3 lysine 9 methylation (H3K9me) and histone hypoacetylation are conserved epigenetic hallmarks of heterochromatin. In fission yeast, RNA interference (RNAi) plays a key role in H3K9 methylation and heterochromatin silencing. However, how RNAi machinery and histone deacetylases (HDACs) are coordinated to ensure proper heterochromatin assembly is still unclear. Previously, we showed that Dpb4, a conserved DNA polymerase epsilon subunit, plays a key role in the recruitment of HDACs to heterochromatin during S phase. Here, we identified a novel RNA-binding protein Dri1 that interacts with Dpb4. GFP-tagged Dri1 forms distinct foci mostly in the nucleus, showing a high degree of colocalization with Swi6/Heterochromatin Protein 1. Deletion of dri1+ leads to defects in silencing, H3K9me, and heterochromatic siRNA generation. We also showed that Dri1 physically associates with heterochromatic transcripts, and is required for the recruitment of the RNA-induced transcriptional silencing (RITS) complex via interacting with the complex. Furthermore, loss of Dri1 decreases the association of the Sir2 HDAC with heterochromatin. We further demonstrated that the C-terminus of Dri1 that includes an intrinsically disordered (IDR) region and three zinc fingers is crucial for its role in silencing. Together, our evidences suggest that Dri1 facilitates heterochromatin assembly via the RNAi pathway and HDAC.","doi":"10.1093/genetics/iyab032","authors":"Ban H, Sun W, Chen YH, Chen Y, Li F","authors_abbrev":"Ban H et al.","pubmed_publication_date":"17 May 2021","pubmed_entrez_date":"2021-03-11","publication_year":"2021","canto_session_key":"09b96530a975cab0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Fei Li","canto_first_approved_date":"2021-05-12 13:49:29","canto_approved_date":"2023-05-03 12:48:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-04 22:36:45","canto_added_date":"2021-03-13 01:15:07","annotation_curators":[{"name":"Fei Li","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPBC3D6.09","SPBC16D10.07c","SPAC18G6.02c","SPAC17H9.04c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2021-05-12"},{"uniquename":"PMID:22431512","title":"RNAi keeps Atf1-bound stress response genes in check at nuclear pores.","citation":"Genes Dev 2012 Apr 01;26(7):683-92","abstract":"RNAi pathways are prevalent throughout the eukaryotic kingdom and are well known to regulate gene expression on a post-transcriptional level in the cytoplasm. Less is known about possible functions of RNAi in the nucleus. In the fission yeast Schizosaccharomyces pombe, RNAi is crucial to establish and maintain centromeric heterochromatin and functions to repress genome activity by a chromatin silencing mechanism referred to as cotranscriptional gene silencing (CTGS). Mechanistic details and the physiological relevance of CTGS are unknown. Here we show that RNAi components interact with chromatin at nuclear pores to keep stress response genes in check. We demonstrate that RNAi-mediated CTGS represses stress-inducible genes by degrading mRNAs under noninduced conditions. Under chronic heat stress conditions, a Dicer thermoswitch deports Dicer to the cytoplasm, thereby disrupting CTGS and enabling expression of genes implicated in the acquisition of thermotolerance. Taken together, our work highlights a role for nuclear pores and the stress response transcription factor Atf1 in coordinating the interplay between the RNAi machinery and the S. pombe genome and uncovers a novel mode of RNAi regulation in response to an environmental cue.","doi":"10.1101/gad.186866.112","authors":"Woolcock KJ, Stunnenberg R, Gaidatzis D, Hotz HR, Emmerth S, Barraud P, Bühler M","authors_abbrev":"Woolcock KJ et al.","pubmed_publication_date":"01 Apr 2012","pubmed_entrez_date":"2012-03-21","publication_year":"2012","canto_session_key":"083c3fcd870879b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-11-20 16:57:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-09-16 14:38:31","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17G9.04c","SPCC736.11","SPCC188.13c","SPAC6F12.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2013-09-16"},{"uniquename":"PMID:9572143","title":"Fission yeast Taz1 protein is required for meiotic telomere clustering and recombination.","citation":"Nature 1998 Apr 23;392(6678):828-31","abstract":"The alignment of homologous chromosomes during meiosis is essential for their recombination and segregation. Telomeres form and protect the ends of eukaryotic linear chromosomes, and are composed of tandem repeats of a simple DNA sequence and the proteins that bind to these repeats. A role for telomeres in meiosis was suspected from observations of telomere clustering in meiotic cells, and has now been supported experimentally by the dramatic rearrangement of telomere locations during premeiotic stages in fission yeast. Here we show that the fission yeast telomere protein, Taz1, is required for stable association between telomeres and spindle pole bodies during meiotic prophase. In the absence of Taz1, telomere clustering at the spindle pole bodies is disrupted, meiotic recombination is reduced, and both spore viability and the ability of zygotes to re-enter mitosis are impaired to a level that would be expected if chromosome segregation were occurring randomly. Such telomeric association mediated by telomere-specific proteins may also be important for proper chromosome alignment and recombination during meiosis in humans.","authors":"Cooper JP, Watanabe Y, Nurse P","authors_abbrev":"Cooper JP et al.","pubmed_publication_date":"23 Apr 1998","pubmed_entrez_date":"1998-05-08","publication_year":"1998","canto_session_key":"1a585ba6a181c2ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-10 07:56:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-10 07:56:02","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-10"},{"uniquename":"PMID:4838162","title":"Regulatory and physicochemical properties of two isoenzymes of malate dehydrogenase from Schizosaccharo-myces pombe.","citation":"Biochim Biophys Acta 1974 Apr 25;341(2):465-83","abstract":"","authors":"Flury U, Heer B, Fiechter A","authors_abbrev":"Flury U et al.","pubmed_publication_date":"25 Apr 1974","pubmed_entrez_date":"1974-04-25","publication_year":"1974","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26519304","title":"High-Speed Super-Resolution Imaging of Live Fission Yeast Cells.","citation":"Methods Mol Biol 2016;1369:45-57","abstract":"We describe a step-by-step method for high-speed fluorescence photoactivation localization microscopy (FPALM) of live fission yeast cells. The resolution with this method is tenfold better than spinning disk confocal microscopy.","doi":"10.1007/978-1-4939-3145-3_4","authors":"Laplante C, Huang F, Bewersdorf J, Pollard TD","authors_abbrev":"Laplante C et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-11-01","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-02 01:19:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33527595","title":"Trimethylguanosine synthase 1 (Tgs1) is involved in Swi6/HP1-independent siRNA production and establishment of heterochromatin in fission yeast.","citation":"Genes Cells 2021 Apr;26(4):203-218","abstract":"In fission yeast, siRNA generated by RNA interference (RNAi) factors plays critical roles in establishment and maintenance of heterochromatin. To achieve efficient siRNA synthesis, RNAi factors assemble on heterochromatin via association with Swi6, a homologue of heterochromatin protein 1 (HP1), and heterochromatic noncoding RNA (hncRNA) retained on chromatin. In addition, spliceosomes formed on hncRNA introns recruit RNAi factors to hncRNA and heterochromatin. Small nuclear RNAs, components of the spliceosome, have a trimethylguanosine (TMG) cap that is generated by Tgs1-dependent hypermethylation of the normal m7G cap; this cap is required for efficient splicing of some mRNAs in budding yeast and Drosophila. In this study, we found that loss of Tgs1 in fission yeast destabilizes centromeric heterochromatin. Tgs1 was required for Swi6-independent siRNA synthesis, as well as for the establishment of centromeric heterochromatin. Loss of Tgs1 affected the splicing efficiency of hncRNA introns in the absence of Swi6. Furthermore, some hncRNAs have a TMG cap, and we found that loss of Tgs1 diminished the chromatin binding of these hncRNAs. Together, these results suggest that the Tgs1-dependent TMG cap plays critical roles in establishment of heterochromatin by ensuring spliceosome-dependent recruitment of RNAi factors and regulating the binding between chromatin and hncRNA.","doi":"10.1111/gtc.12833","authors":"Yu H, Tsuchida M, Ando M, Hashizaki T, Shimada A, Takahata S, Murakami Y","authors_abbrev":"Yu H et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2021-02-02","publication_year":"2021","canto_session_key":"bd6b7d66fe77314f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-02-04 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16781175","title":"A phylogenomic analysis of the Ascomycota.","citation":"Fungal Genet Biol 2006 Oct;43(10):715-25","abstract":"An automated procedure was developed to extract orthologous sequences from fungal genomes and incorporate them into phylogenomic analyses in a timely and efficient manner. This approach involves parsing an all versus all BLASTP search of 17 proteomes and creating a similarity matrix from e-values, which is then used to cluster proteins into related groups by means of a Markov Clustering algorithm. After performing this analysis at different stringency levels, 854 single copy protein clusters, which were ubiquitously distributed in all 17 proteomes, were identified. These clusters were culled to include only those clusters where all proteins had best hits to and received hits from a protein within the same cluster. The final data set included gapless alignments for 781 clusters of orthologous sequences that were concatenated into one super alignment containing 195,664 amino acid characters. Neighbor-joining distance and maximum likelihood analyses resulted in identical topologies and all except one node received 100% bootstrap support. The node supporting Stagonospora nodorum's position received 83% support or higher; it was also the only taxon differentially resolved in the maximum parsimony analyses. All analyses resolved the two derived subphyla Pezizomycotina and Saccharomycotina, and Schizosaccharomyces pombe as an early diverging lineage of the Ascomycota. Importantly, these analyses resolved the Leotiomycetes as the sister group to the Sordariomycetes, a region of the Ascomycota phylogeny that has remained problematic in molecular phylogenetic studies of more limited character sampling. Additional phylogenetic analyses which included orthologous sequences from an unannotated ascomycotan genome (e.g., Coccidioides immitis) and subsets of orthologs with different characteristics supported this topology. Phylogenetic analyses of the 595 orthologs which included C. immitis resulted in an identical topology to the previous 781 ortholog analysis and correctly placed C. immitis in the Eurotiomycetes. This demonstrated the correct identification of orthologs and the ability to incorporate unannotated genomic data into a common phylogenetic analysis.","authors":"Robbertse B, Reeves JB, Schoch CL, Spatafora JW","authors_abbrev":"Robbertse B et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-06-20","publication_year":"2006","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22119525","title":"SIN-inhibitory phosphatase complex promotes Cdc11p dephosphorylation and propagates SIN asymmetry in fission yeast.","citation":"Curr Biol 2011 Dec 06;21(23):1968-78","abstract":"Cytokinesis in many eukaryotes involves the function of an actomyosin-based contractile ring. In fission yeast, actomyosin ring maturation and stability require a conserved signaling pathway termed the SIN (septation initiation network). The SIN consists of a GTPase (Spg1p) and three protein kinases, all of which localize to the mitotic spindle pole bodies (SPBs). Two of the SIN kinases, Cdc7p and Sid1p, localize asymmetrically to the newly duplicated SPB in late anaphase. How this asymmetry is achieved is not understood, although it is known that their symmetric localization impairs cytokinesis.\nHere we characterize a new Forkhead-domain-associated protein, Csc1p, and identify SIN-inhibitory PP2A complex (SIP), which is crucial for the establishment of SIN asymmetry. Csc1p localizes to both SPBs early in mitosis, is lost from the SPB that accumulates Cdc7p, and instead accumulates at the SPB lacking Cdc7p. Csc1p is required for the dephosphorylation of the SIN scaffolding protein Cdc11p and is thereby required for the recruitment of Byr4p, a component of the GTPase-activating subunit for Spg1p, to the SPB.\nBecause Cdc7p does not bind to GDP-Spg1p, we propose that the SIP-mediated Cdc11p dephosphorylation and the resulting recruitment of Byr4p are among the earliest steps in the establishment of SIN asymmetry.","doi":"10.1016/j.cub.2011.10.051","authors":"Singh NS, Shao N, McLean JR, Sevugan M, Ren L, Chew TG, Bimbo A, Sharma R, Tang X, Gould KL, Balasubramanian MK","authors_abbrev":"Singh NS et al.","pubmed_publication_date":"06 Dec 2011","pubmed_entrez_date":"2011-11-29","publication_year":"2011","canto_session_key":"feac1fe40f21f7a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Janel McLean","canto_first_approved_date":"2016-09-05 08:57:54","canto_approved_date":"2026-02-14 09:48:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-21 16:10:27","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Janel McLean","community_curator":true,"annotation_count":51,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4H3.11c","SPAC6F6.08c","SPBC16A3.15c","SPAC20G8.05c","SPBC27B12.04c","SPBC1773.01","SPBC365.12c","SPAC22A12.07c","SPAC6F6.15","SPCC736.15","SPAC31F12.01","SPAC9.09","SPAC24H6.04","SPAC1F5.02","SPAP8A3.09c","SPBC12C2.06","SPBC1921.05","SPAPB1A10.08","SPAC30C2.08","SPBC3D6.15","SPBC146.14c","SPBC18E5.06","SPAC1F12.07","SPBC646.09c","SPBC244.01c","SPBC16G5.05c","SPAC1486.04c","SPAC22A12.16","SPCC645.14c","SPCC1322.13","SPAC1834.04","SPAC23G3.11","SPAC1006.07","SPAC24B11.11c","SPAC1834.02","SPBC14F5.03c","SPBC2G5.05","SPCC1235.14","SPBC28F2.03","SPAC22H12.01c","SPAC25B8.12c","SPBC1778.06c","SPAC1782.05","SPAC23C11.09","SPBPJ4664.04","SPAC24H6.05","SPBC3D6.02","SPCC1840.03","SPAC26F1.03","SPBC12C2.08","SPAC1F12.02c","SPAC3A11.12c","SPAC3H8.04","SPAC56F8.05c","SPCC645.08c","SPBC13A2.04c","SPBC215.08c","SPAC607.05","SPAC29A4.15","SPAPYUK71.03c","SPAC27F1.07","SPBC582.07c","SPBC1703.07","SPBC8D2.06","SPACUNK4.07c","SPAC1783.05","SPBC3E7.02c","SPBC29A10.01","SPBC428.02c","SPAC3C7.08c","SPAP8A3.07c","SPCC1183.02","SPBC776.03","SPCC794.12c","SPAC110.04c","SPBC1703.13c","SPBP4H10.17c","SPBC3F6.02c","SPBC30D10.13c","SPAC6F12.12","SPCC1450.04","SPAC20G8.09c","SPACUNK4.10","SPCC364.07","SPAC6B12.15","SPBC8E4.01c","SPCC338.15","SPBC582.03","SPBC26H8.07c","SPAC22F8.05","SPCC777.09c","SPAC1635.01","SPCC550.11","SPCC188.02","SPAC222.12c","SPBC336.10c","SPAC2G11.07c","SPBC215.09c","SPAC21E11.08","SPAC2C4.10c","SPBC18E5.02c","SPAPB17E12.05","SPCC1682.05c","SPAC17G8.06c","SPBC800.05c","SPAC9E9.07c","SPAC10F6.06","SPBC20F10.01","SPBC21.06c","SPAC9E9.04","SPBC21C3.08c","SPBC1A4.08c","SPCC1393.12","SPAC222.10c","SPCC757.09c","SPBC17D1.06","SPCPB16A4.03c","SPCC1020.06c","SPBC56F2.09c","SPBC3H7.13","SPCC24B10.21","SPAC23C11.05","SPAC4F8.07c","SPAC9.07c","SPAC9E9.09c","SPBC3B9.01","SPAC17H9.14c","SPAC6F12.10c","SPBC660.16","SPAC1705.03c","SPAC4G9.11c","SPAC1786.02","SPAC977.14c","SPBC1604.05","SPCC1322.16","SPAC1F3.06c","SPBC19C2.07","SPCC576.03c","SPBC119.01","SPAC1D4.04","SPBC21D10.12","SPBC337.05c","SPCC1322.14c","SPBC106.06","SPAC22H10.04","SPAC19B12.01","SPAC1142.04","SPAC3C7.11c","SPBC16H5.07c","SPBC1703.10","SPBC17D11.07c","SPBC365.13c","SPCC1739.11c","SPAC18G6.06","SPAC222.14c","SPAC26A3.05","SPAC19A8.15","SPAC823.15","SPAC20G8.06","SPAC227.07c","SPBC215.05","SPBC8D2.18c","SPBC56F2.08c","SPAC27E2.03c","SPBC9B6.04c","SPCC306.09c"],"gene_count":166,"ltp_gene_count":16,"approved_date":"2016-09-05"},{"uniquename":"PMID:27988464","title":"Synthesis and biological screening of novel 2-morpholinoquinoline nucleus clubbed with 1,2,4-oxadiazole motifs.","citation":"Eur J Med Chem 2017 Jan 27;126:894-909","abstract":"Novel series of 2-morpholinoquinoline scaffolds (6a-n), containing the 1,2,4-oxadiazole and moiety, was designed and synthesized in good yield (76-86%). The synthesized compounds were screened for their preliminary in vitro antimicrobial activity against a panel of pathogenic strains of bacteria and fungi. Molecular docking and pharmacokinetic study were carried out for the prepared compounds. The cytotoxicity of the synthesized compounds was tested at different concentrations using bioassay of S. pombe cells at the cellular level. The effect of synthesized compounds on the DNA integrity of S. pombe was observed on agarose gel. Compounds 6d, 6e, 6g, 6h, 6j and 6n exhibited excellent antimicrobial potency as compared to the standard drugs (i.e Ampicillin, Norfloxacin, Chloramphenicol, Ciprofloxacin). Compounds 6d, 6e, 6g, 6k and 6n were found to have significant antifungal activity as compared to griseofulvin. Compounds 6f, 6i, 6k, 6l were found very less cytotoxic, while compounds 6d, 6e, 6g, 6h were found to exhibit maximum toxicity. The rest of the synthesized compounds were found to be moderately toxic.","doi":"10.1016/j.ejmech.2016.12.016","authors":"Karad SC, Purohit VB, Thummar RP, Vaghasiya BK, Kamani RD, Thakor P, Thakkar VR, Thakkar SS, Ray A, Raval DK","authors_abbrev":"Karad SC et al.","pubmed_publication_date":"27 Jan 2017","pubmed_entrez_date":"2016-12-19","publication_year":"2017","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2016-12-20 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11408570","title":"Characterization of a novel human SMC heterodimer homologous to the Schizosaccharomyces pombe Rad18/Spr18 complex.","citation":"Mol Biol Cell 2001 Jun;12(6):1583-94","abstract":"The structural maintenance of chromosomes (SMC) protein encoded by the fission yeast rad18 gene is involved in several DNA repair processes and has an essential function in DNA replication and mitotic control. It has a heterodimeric partner SMC protein, Spr18, with which it forms the core of a multiprotein complex. We have now isolated the human orthologues of rad18 and spr18 and designated them hSMC6 and hSMC5. Both proteins are about 1100 amino acids in length and are 27-28% identical to their fission yeast orthologues, with much greater identity within their N- and C-terminal globular domains. The hSMC6 and hSMC5 proteins interact to form a tight complex analogous to the yeast Rad18/Spr18 heterodimer. In proliferating human cells the proteins are bound to both chromatin and the nucleoskeleton. In addition, we have detected a phosphorylated form of hSMC6 that localizes to interchromatin granule clusters. Both the total level of hSMC6 and its phosphorylated form remain constant through the cell cycle. Both hSMC5 and hSMC6 proteins are expressed at extremely high levels in the testis and associate with the sex chromosomes in the late stages of meiotic prophase, suggesting a possible role for these proteins in meiosis.","authors":"Taylor EM, Moghraby JS, Lees JH, Smit B, Moens PB, Lehmann AR","authors_abbrev":"Taylor EM et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-06-16","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12442905","title":"Regulation of the manganese-containing superoxide dismutase gene from fission yeast.","citation":"Mol Cells 2002 Oct 31;14(2):300-4","abstract":"The manganese superoxide dismutase (MnSOD) is a mitochondrial enzyme that dismutates a potentially toxic superoxide radical into hydrogen peroxide and dioxygen. To study the regulation of the Schizosaccharomyces pombe MnSOD gene, the 943 bp upstream region was fused into the promoterless beta-galactosidase gene of the shuttle vector YEp357, which resulted in the fusion plasmid pMS14. Restriction mapping and nucleotide sequencing confirmed its construction. The synthesis of beta-galactosidase from the fusion plasmid was induced by aluminum chloride, menadione, cadmium chloride, manganese chloride, and hydrogen peroxide. It was also induced by NO-generating S-nitroso-N-acetylpenicillamine (SNAP). However, cupric chloride and zinc chloride did not affect the synthesis of beta-galactosidase from the fusion plasmid. The beta-galactosidase synthesis appeared to be independent of the Pap1 protein. These results suggest that some metals, oxidative stress, and nitric oxide regulate the S. pombe MnSOD gene.","authors":"Jung HI, Lee YY, Lim HW, Ahn KS, Park EH, Lim CJ","authors_abbrev":"Jung HI et al.","pubmed_publication_date":"31 Oct 2002","pubmed_entrez_date":"2002-11-22","publication_year":"2002","canto_session_key":"6a89fc9a4ec07ab6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:56:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 10:05:29","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC1486.01"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-11-05"},{"uniquename":"PMID:31889253","title":"Use of tRNA-Mediated Suppression to Assess RNA Chaperone Function.","citation":"Methods Mol Biol 2020;2106:107-120","abstract":"La proteins have well-established roles in the maturation of RNA polymerase III transcripts, including pre-tRNAs. In addition to protecting the 3' end of pre-tRNAs from exonuclease digestion, La proteins also promote the native fold of the pre-tRNA using RNA chaperone activity. tRNA-mediated suppression in the fission yeast S. pombe has been an invaluable tool in determining the mechanistic basis by which La proteins promote the maturation of defective pre-tRNAs that benefit from RNA chaperone activity. More recently, tRNA-mediated suppression has been adapted to test for RNA chaperone function in the La-related proteins and in the promoting of tRNA function by tRNA modification enzymes. Thus tRNA-mediated suppression can be a useful assay for the investigation of various proteins hypothesized to promote tRNA folding through RNA chaperone related activities.","doi":"10.1007/978-1-0716-0231-7_6","authors":"Porat J, Bayfield MA","authors_abbrev":"Porat J et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-01-01","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013516","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15537537","title":"Heterochromatin regulates cell type-specific long-range chromatin interactions essential for directed recombination.","citation":"Cell 2004 Nov 12;119(4):469-80","abstract":"Mating-type switching in Schizosaccharomyces pombe involves replacing genetic information at the expressed mat1 locus with sequences copied from one of two silent donor loci, mat2-P or mat3-M, located within a 20-kb heterochromatic domain. Donor selection is dictated by cell type: mat2 is the preferred donor in M cells, and mat3 is the preferred donor in P cells. Here we show that a recombination-promoting complex (RPC) containing Swi2 and Swi5 proteins exhibits cell type-specific localization pattern at the silent mating-type region and this differential localization modulates donor preference during mating-type switching. In P cells, RPC localization is restricted to a recombination enhancer located adjacent to mat3, but in M cells, RPC spreads in cis across the entire silent mating-type interval in a heterochromatin-dependent manner. Our analyses implicate heterochromatin in long-range regulatory interactions and suggest that heterochromatin imposes at the mating-type region structural organization that is important for the donor-choice mechanism.","authors":"Jia S, Yamada T, Grewal SI","authors_abbrev":"Jia S et al.","pubmed_publication_date":"12 Nov 2004","pubmed_entrez_date":"2004-11-13","publication_year":"2004","canto_session_key":"60a2109be6c06e32","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-10 13:55:12","canto_approved_date":"2024-07-10 13:55:12","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-10 13:55:04","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":21,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.02c","SPAC664.01c","SPBC428.08c","SPBC16C6.10","SPBC409.03","SPAC1142.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2024-07-10"},{"uniquename":"PMID:21802294","title":"Divergent strategies for controlling the nuclear membrane satisfy geometric constraints during nuclear division.","citation":"Curr Biol 2011 Aug 09;21(15):1314-9","abstract":"Eukaryotes segregate chromosomes in \"open\" or \"closed\" mitosis, depending on whether their nuclear envelopes (NEs) break down or remain intact. Here we show that the control of the nuclear surface area may determine the choice between these two modes. The dividing nucleus does not expand its surface in the fission yeast Schizosaccharomyces japonicus, confining the mitotic spindle and causing it to buckle. The NE ruptures in anaphase, releasing the compressive stress and allowing chromosome segregation. Blocking the NE expansion in the related species Schizosaccharomyces pombe that undergoes closed mitosis induces spindle buckling and collapse in the absence of an intrinsic NE rupture mechanism. We propose that scaling considerations could have shaped the evolution of eukaryotic mitosis by necessitating either nuclear surface expansion or the NE breakdown.","doi":"10.1016/j.cub.2011.06.052","authors":"Yam C, He Y, Zhang D, Chiam KH, Oliferenko S","authors_abbrev":"Yam C et al.","pubmed_publication_date":"09 Aug 2011","pubmed_entrez_date":"2011-08-02","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29663033","title":"How long does telomerase extend telomeres? Regulation of telomerase release and telomere length homeostasis.","citation":"Curr Genet 2018 Dec;64(6):1177-1181","abstract":"Telomerase, the enzyme that replenishes telomeres, is essential for most eukaryotes to maintain their generations. Telomere length homeostasis is achieved via a balance between telomere lengthening by telomerase, and erosion over successive cell divisions. Impaired telomerase regulation leads to shortened telomeres and can cause defects in tissue maintenance. Telomeric DNA is composed of a repetitive sequence, which recruits the protective protein complex, shelterin. Shelterin, together with chromatin remodelling proteins, shapes the heterochromatic structure at the telomere and protects chromosome ends. Shelterin also provides a foothold for telomerase to be recruited and facilitates telomere extension. Such mechanisms of telomere recruitment and activation are conserved from unicellular eukaryotes to humans, with the rate of telomere extension playing an important role in determining the length maintained. Telomerase can be processive, adding multiple telomeric repeats before dissociating. However, a question remains: how does telomerase determine the number of repeats to add? In this review, I will discuss about how telomerase can monitor telomere extension using fission yeast as a model. I propose a model whereby the accumulation of the Pot1 complex on the synthesised telomere single-strand counteracts retention of telomerase via chromatin proteins and the similar system may be conserved in mammals.","doi":"10.1007/s00294-018-0836-6","authors":"Tomita K","authors_abbrev":"Tomita K","pubmed_publication_date":"Dec 2018","pubmed_entrez_date":"2018-04-18","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-04-19 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18239448","title":"Cut1/separase-dependent roles of multiple phosphorylation of fission yeast cohesion subunit Rad21 in post-replicative damage repair and mitosis.","citation":"Cell Cycle 2008 Mar 15;7(6):765-76","abstract":"Cohesin is a multiprotein complex essential for sister-chromatid cohesion. It plays a pivotal role in proper chromosome segregation and DNA damage repair. The mitotic behavior of cohesin is controlled through its phosphorylation, which possibly induces the dissociation of cohesin from chromosomes and enhances its susceptibility to separase. Here, we report using mass spectrometry and anti-phospho antibodies that the central domain of Rad21, the separase-target subunit of Schizosaccharomyces pombe cohesin, is regulated by various kinase-induced phosphorylation at nine residues, indicating the multiple roles for S. pombe cohesin. In vegetative and non-dividing G(0) cells, Rad21 is phosphorylated by unknown S/TP-consensus kinases, in mitotic and non-mitotic cells by polo/Plo1 and CDK, and in DNA-damaged cells by Rad3/ATR. While mitotic phosphorylation is implicated in the dissociation of Rad21 and its cleavage by separase in anaphase, the Rad3/ATR-dependent damage-induced phosphorylation occurs intensively at the time of repair completion, and only in post-replicative cells. This damage-induced Rad21 phosphorylation is involved in the recovery process of cells from checkpoint arrest, and needed for the removal of cohesin by separase after the completion of damage repair. These complex phospho-regulations of Rad21 indicate the functional significance of cohesin in cell adaptation to a variety of cellular conditions.","authors":"Adachi Y, Kokubu A, Ebe M, Nagao K, Yanagida M","authors_abbrev":"Adachi Y et al.","pubmed_publication_date":"15 Mar 2008","pubmed_entrez_date":"2008-02-02","publication_year":"2008","canto_session_key":"e9657df71075feff","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14972679","title":"Two fission yeast homologs of Drosophila Mei-S332 are required for chromosome segregation during meiosis I and II.","citation":"Curr Biol 2004 Feb 17;14(4):287-301","abstract":"Meiosis produces haploid gametes from diploid progenitor cells. This reduction is achieved by two successive nuclear divisions after one round of DNA replication. Correct chromosome segregation during the first division depends on sister kinetochores being oriented toward the same spindle pole while homologous kinetochores must face opposite poles. Segregation during the second division depends on retention of sister chromatid cohesion between centromeres until the onset of anaphase II, which in Drosophila melanogaster depends on a protein called Mei-S332 that binds to centromeres.\nWe report the identification of two homologs of Mei-S332 in fission yeast using a knockout screen. Together with their fly ortholog they define a protein family conserved from fungi to mammals. The two identified genes, sgo1 and sgo2, are required for retention of sister centromere cohesion between meiotic divisions and kinetochore orientation during meiosis I, respectively. The amount of meiotic cohesin's Rec8 subunit retained at centromeres after meiosis I is reduced in Deltasgo1, but not in Deltasgo2, cells, and Sgo1 appears to regulate cleavage of Rec8 by separase. Both Sgo1 and Sgo2 proteins localize to centromere regions. The abundance of Sgo1 protein normally declines after the first meiotic division, but extending its expression by altering its 3'UTR sequences does not greatly affect meiosis II. Its mere presence within the cell might therefore be insufficient to protect centromeric cohesion.\nA conserved protein family based on Mei-S332 has been identified. The two fission yeast homologs are implicated in meiosis I kinetochore orientation and retention of centromeric sister chromatid cohesion until meiosis II.","authors":"Rabitsch KP, Gregan J, Schleiffer A, Javerzat JP, Eisenhaber F, Nasmyth K","authors_abbrev":"Rabitsch KP et al.","pubmed_publication_date":"17 Feb 2004","pubmed_entrez_date":"2004-02-20","publication_year":"2004","canto_session_key":"27b51a588fa236c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-02-16 10:11:02","canto_approved_date":"2021-06-10 15:00:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-02-16 10:10:56","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.04","SPAC15A10.15","SPBC29A10.14","SPBP35G2.03c","SPCC4E9.01c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2021-02-16"},{"uniquename":"PMID:35618415","title":"Native RNA sequencing in fission yeast reveals frequent alternative splicing isoforms.","citation":"Genome Res 2022 May 26;32(6):1215-27","abstract":"The unicellular yeast  Schizosaccharomyces pombe  (fission yeast) retains many of the splicing features observed in humans and is thus an excellent model to study the basic mechanisms of splicing. Nearly half the genes contain introns, but the impact of alternative splicing in gene regulation and proteome diversification remains largely unexplored. Here we leverage Oxford Nanopore Technologies native RNA sequencing (dRNA), as well as ribosome profiling data, to uncover the full range of polyadenylated transcripts and translated open reading frames. We identify 332 alternative isoforms affecting the coding sequences of 262 different genes, 97 of which occur at frequencies higher than 20%, indicating that functional alternative splicing in  S. pombe  is more prevalent than previously suspected. Intron retention events make about 80% of the cases; these events may be involved in the regulation of gene expression and, in some cases, generate novel protein isoforms, as supported by ribosome profiling data in 18 of the intron retention isoforms. One example is the  rpl22  gene, in which intron retention is associated with the translation of a protein of only 13 amino acids. We also find that lowly expressed transcripts tend to have longer poly(A) tails than highly expressed transcripts, highlighting an interdependence between poly(A) tail length and transcript expression level. Finally, we discover 214 novel transcripts that are not annotated, including 158 antisense transcripts, some of which also show translation evidence. The methodologies described in this work open new opportunities to study the regulation of splicing in a simple eukaryotic model.","doi":"10.1101/gr.276516.121","authors":"Montañés JC, Huertas M, Moro SG, Blevins WR, Carmona M, Ayté J, Hidalgo E, Albà MM","authors_abbrev":"Montañés JC et al.","pubmed_publication_date":"26 May 2022","pubmed_entrez_date":"2022-05-26","publication_year":"2022","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2022-05-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1396704","title":"Altered plasma membrane H(+)-ATPase from the Dio-9-resistant pma1-2 mutant of Schizosaccharomyces pombe.","citation":"Eur J Biochem 1992 Oct 01;209(1):275-9","abstract":"The pma1-2 mutation affecting the plasma membrane H(+)-ATPase of Schizosaccharomyces pombe has been selected for resistance to the antibiotic Dio-9. In membrane fractions purified from glucose-starved cells, the mutant ATPase activity is reduced by 96%, is insensitive to inhibition by vanadate and has a pH profile displaced in the acidic pH range when compared to the wild type. The maximum velocity of the H(+)-ATPase activity of plasma membranes from glucose-activated pma1-2 cells is activated 20-fold. This is in striking contrast with the wild-type ATPase activity, the maximal velocity of which is not affected by glucose. However, similar to the wild-type enzyme, glucose activation of the pma1-2 mutant H(+)-ATPase reduces the Km for MgATP 9-2 mM and shifts the optimal pH from 4.8 to 6.0-6.5. The pma1-2 mutation modifies Lys250 to a threonine, which is highly conserved in fungal and plant H(+)-ATPases. These results, compared to those reported for mutations of neighbour residues in yeast or mammalian P-type ATPases, suggest that Lys250 could play a significant role, not only in phosphate binding and/or in the E1P-E2P conformational isomerisation, but also in glucose activation of the H(+)-ATPase.","authors":"Ghislain M, De Sadeleer M, Goffeau A","authors_abbrev":"Ghislain M et al.","pubmed_publication_date":"01 Oct 1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_session_key":"d9f75c80dc374265","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-01 13:34:47","canto_approved_date":"2022-08-24 15:27:16","canto_session_submitted_date":"2012-11-30 12:20:32","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-01"},{"uniquename":"PMID:26477989","title":"Fission yeast meets a legend in Kobe: report of the Eighth International Fission Yeast Meeting.","citation":"Genes Cells 2015 Dec;20(12):967-71","abstract":"The Eighth International Fission Yeast Meeting, which was held at Ikuta Shrine Hall in Kobe, Japan, from 21 to 26 June 2015, was attended by 327 fission yeast researchers from 25 countries (190 overseas and 137 domestic participants). At this meeting, 124 talks were held and 145 posters were presented. In addition, newly developed database tools were introduced to the community during a workshop. Researchers shared cutting-edge knowledge across broad fields of study, ranging from molecules to evolution, derived from the superior model organism commonly used within the fission yeast community. Intensive discussions and constructive suggestions generated in this meeting will surely advance the understanding of complex biological systems in fission yeast, extending to general eukaryotes.","doi":"10.1111/gtc.12307","authors":"Asakawa H, Yamamoto TG, Hiraoka Y","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-10-20","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-10-21 00:18:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28914606","title":"Nanoscale architecture of the  Schizosaccharomyces pombe  contractile ring.","citation":"Elife 2017 Sep 15;6","abstract":"The contractile ring is a complex molecular apparatus which physically divides many eukaryotic cells. Despite knowledge of its protein composition, the molecular architecture of the ring is not known. Here we have applied super-resolution microscopy and FRET to determine the nanoscale spatial organization of  Schizosaccharomyces pombe  contractile ring components relative to the plasma membrane. Similar to other membrane-tethered actin structures, we find proteins localize in specific layers relative to the membrane. The most membrane-proximal layer (0-80 nm) is composed of membrane-binding scaffolds, formin, and the tail of the essential myosin-II. An intermediate layer (80-160 nm) consists of a network of cytokinesis accessory proteins as well as multiple signaling components which influence cell division. Farthest from the membrane (160-350 nm) we find F-actin, the motor domains of myosins, and a major F-actin crosslinker. Circumferentially within the ring, multiple proteins proximal to the membrane form clusters of different sizes, while components farther from the membrane are uniformly distributed. This comprehensive organizational map provides a framework for understanding contractile ring function.","doi":"10.7554/eLife.28865","authors":"McDonald NA, Lind AL, Smith SE, Li R, Gould KL","authors_abbrev":"McDonald NA et al.","pubmed_publication_date":"15 Sep 2017","pubmed_entrez_date":"2017-09-16","publication_year":"2017","canto_session_key":"a9fe75ac65f6d5f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2017-10-10 15:11:28","canto_approved_date":"2025-03-17 15:58:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-27 18:06:59","canto_added_date":"2017-09-17 00:15:14","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.06","SPAC4F10.11","SPBC11C11.02","SPAC1782.09c","SPAC9G1.11c","SPAC1F5.04c","SPAC17G8.14c","SPBC16A3.01","SPAC3G9.05","SPCC4B3.15","SPAC2F7.03c","SPBC83.18c","SPAC4F8.13c","SPAC9G1.06c","SPCC645.06c","SPAC12B10.10","SPBC1A4.05","SPAC8E11.02c","SPBC1604.14c","SPAC926.03","SPAC20G8.05c","SPAC26A3.09c","SPBC1778.06c","SPBC2D10.14c","SPBC23G7.08c","SPBC4F6.12","SPBP4H10.04","SPAC24B11.11c","SPCC645.05c","SPBC32H8.12c","SPAC4A8.05c","SPAC31A2.16"],"gene_count":32,"ltp_gene_count":32,"approved_date":"2017-10-10"},{"uniquename":"PMID:10606652","title":"Sequence-specific binding of Taz1p dimers to fission yeast telomeric DNA.","citation":"Nucleic Acids Res 2000 Jan 15;28(2):527-33","abstract":"The fission yeast (Schizosaccharomyces pombe) taz1 gene encodes a telomere-associated protein. It contains a single copy of a Myb-like motif termed the telobox that is also found in the human telomere binding proteins TRF1 and TRF2, and Tbf1p, a protein that binds to sequences found within the sub-telomeric regions of budding yeast (Saccharomyces cerevisiae) chromosomes. Taz1p was synthesised in vitro and shown to bind to a fission yeast telomeric DNA fragment in a sequence specific manner that required the telobox motif. Like the mammalian TRF proteins, Taz1p bound to DNA as a preformed homodimer. The isolated Myb-like domain was also capable of sequence specific DNA binding, although with less specificity than the full-length dimer. Surprisingly, a protein extract produced from a taz1- fission yeast strain still contained the major telomere binding activity (complex I) we have characterised previously, suggesting that there could be other abundant telomere binding proteins in fission yeast. One candidate, SpX, was also synthesised in vitro, but despite the presence of two telobox domains, no sequence specific binding to telomeric DNA was detected.","authors":"Spink KG, Evans RJ, Chambers A","authors_abbrev":"Spink KG et al.","pubmed_publication_date":"15 Jan 2000","pubmed_entrez_date":"1999-12-22","publication_year":"2000","canto_session_key":"b6d4a3823d6a5eb1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-24 13:16:19","canto_approved_date":"2022-02-02 14:26:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-24 13:16:12","canto_added_date":"2012-02-24 05:52:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.07c","SPAC13G7.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-04-24"},{"uniquename":"PMID:36793083","title":"The SAGA histone acetyltransferase module targets SMC5/6 to specific genes.","citation":"Epigenetics Chromatin 2023 Feb 16;16(1):6","abstract":"Structural Maintenance of Chromosomes (SMC) complexes are molecular machines driving chromatin organization at higher levels. In eukaryotes, three SMC complexes (cohesin, condensin and SMC5/6) play key roles in cohesion, condensation, replication, transcription and DNA repair. Their physical binding to DNA requires accessible chromatin.\nWe performed a genetic screen in fission yeast to identify novel factors required for SMC5/6 binding to DNA. We identified 79 genes of which histone acetyltransferases (HATs) were the most represented. Genetic and phenotypic analyses suggested a particularly strong functional relationship between the SMC5/6 and SAGA complexes. Furthermore, several SMC5/6 subunits physically interacted with SAGA HAT module components Gcn5 and Ada2. As Gcn5-dependent acetylation facilitates the accessibility of chromatin to DNA-repair proteins, we first analysed the formation of DNA-damage-induced SMC5/6 foci in the Δgcn5 mutant. The SMC5/6 foci formed normally in Δgcn5, suggesting SAGA-independent SMC5/6 localization to DNA-damaged sites. Next, we used Nse4-FLAG chromatin-immunoprecipitation (ChIP-seq) analysis in unchallenged cells to assess SMC5/6 distribution. A significant portion of SMC5/6 accumulated within gene regions in wild-type cells, which was reduced in Δgcn5 and Δada2 mutants. The drop in SMC5/6 levels was also observed in gcn5-E191Q acetyltransferase-dead mutant.\nOur data show genetic and physical interactions between SMC5/6 and SAGA complexes. The ChIP-seq analysis suggests that SAGA HAT module targets SMC5/6 to specific gene regions and facilitates their accessibility for SMC5/6 loading.","doi":"10.1186/s13072-023-00480-z","authors":"Mahrik L, Stefanovie B, Maresova A, Princova J, Kolesar P, Lelkes E, Faux C, Helmlinger D, Prevorovsky M, Palecek JJ","authors_abbrev":"Mahrik L et al.","pubmed_publication_date":"16 Feb 2023","pubmed_entrez_date":"2023-02-16","publication_year":"2023","canto_session_key":"d351bbb0a4c9383c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Barbora Štefanovie","canto_first_approved_date":"2023-03-09 11:30:12","canto_approved_date":"2023-03-14 17:49:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-21 07:46:37","canto_added_date":"2023-02-17 01:15:05","annotation_curators":[{"name":"Barbora Štefanovie","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":103,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1861.07","SPAC1B3.16c","SPBC337.08c","SPAC8C9.04","SPCC31H12.08c","SPCC594.01","SPAC23C11.04c","SPBC582.06c","SPAC167.05","SPAC4F10.13c","SPBC3D6.08c","SPBC582.05c","SPAC5D6.06c","SPAC29B12.05c","SPBC902.03","SPCC364.07","SPBC16A3.19","SPAC15E1.05c","SPBC12D12.06","SPAC12B10.12c","SPBC649.03","SPAC1039.08","SPCC1450.02","SPBC20F10.05","SPBC29A10.10c","SPAC17A5.07c","SPCC550.15c","SPBC31F10.10c","SPAC8C9.03","SPAC9E9.08","SPBC557.02c","SPAC2G11.13","SPAC26A3.02","SPAC3G9.08","SPBC27B12.09c","SPBC20F10.04c","SPBC14F5.09c","SPAC328.10c","SPAC630.13c","SPAC1952.05","SPBC19C7.02","SPAC2F3.15","SPBC651.10","SPCC306.04c","SPBC2G2.13c","SPAC56F8.02","SPBC839.03c","SPBC28F2.10c","SPCC285.13c","SPCP31B10.05","SPAC25A8.01c","SPAC3G6.06c","SPAC513.04","SPAC694.06c","SPBC1921.07c","SPCC74.02c","SPBC21D10.10","SPAC14C4.02c","SPAC11E3.08c","SPCC417.08","SPAC13A11.04c","SPAC15E1.02c","SPAC1805.04","SPAC17H9.19c","SPBC26H8.05c","SPAC23A1.19c","SPCC1753.05","SPAC17H9.10c","SPCC23B6.03c","SPAC16A10.06c","SPCC23B6.01c","SPBC1347.08c","SPCC553.01c","SPCC645.04","SPAPB1A10.09","SPCC895.07","SPAC30D11.07","SPAC4G9.02","SPBC3B8.10c","SPAC343.12","SPBC21B10.13c","SPAC222.04c","SPBC3D6.10","SPAC57A10.02","SPAC1556.01c","SPAC4H3.05","SPCC24B10.08c","SPBC32F12.11"],"gene_count":88,"ltp_gene_count":83,"approved_date":"2023-03-09"},{"uniquename":"PMID:38359013","title":"Correction: Fission Yeast CSL Transcription Factors: Mapping Their Target Genes and Biological Roles.","citation":"PLoS One 2024;19(2):e0299200","abstract":"[This corrects the article DOI: 10.1371/journal.pone.0137820.].","doi":"10.1371/journal.pone.0299200","authors":"Převorovský M, Oravcová M, Tvarůžková J, Zach R, Folk P, Půta F, Bähler J","authors_abbrev":"Převorovský M et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-02-15","publication_year":"2024","canto_session_key":"a3de75bdb576bfd5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-20 18:20:43","canto_approved_date":"2024-02-20 18:20:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-16 13:11:20","canto_added_date":"2024-02-16 00:25:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPCC736.08"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2024-02-20"},{"uniquename":"PMID:26744419","title":"Control of heterochromatin localization and silencing by the nuclear membrane protein Lem2.","citation":"Genes Dev 2016 Jan 15;30(2):133-48","abstract":"Transcriptionally silent chromatin localizes to the nuclear periphery, which provides a special microenvironment for gene repression. A variety of nuclear membrane proteins interact with repressed chromatin, yet the functional role of these interactions remains poorly understood. Here, we show that, in Schizosaccharomyces pombe, the nuclear membrane protein Lem2 associates with chromatin and mediates silencing and heterochromatin localization. Unexpectedly, we found that these functions can be separated and assigned to different structural domains within Lem2, excluding a simple tethering mechanism. Chromatin association and tethering of centromeres to the periphery are mediated by the N-terminal LEM (LAP2-Emerin-MAN1) domain of Lem2, whereas telomere anchoring and heterochromatin silencing require exclusively its conserved C-terminal MSC (MAN1-Src1 C-terminal) domain. Particularly, silencing by Lem2 is epistatic with the Snf2/HDAC (histone deacetylase) repressor complex SHREC at telomeres, while its necessity can be bypassed by deleting Epe1, a JmjC protein with anti-silencing activity. Furthermore, we found that loss of Lem2 reduces heterochromatin association of SHREC, which is accompanied by increased binding of Epe1. This reveals a critical function of Lem2 in coordinating these antagonistic factors at heterochromatin. The distinct silencing and localization functions mediated by Lem2 suggest that these conserved LEM-containing proteins go beyond simple tethering to play active roles in perinuclear silencing.","doi":"10.1101/gad.271288.115","authors":"Barrales RR, Forn M, Georgescu PR, Sarkadi Z, Braun S","authors_abbrev":"Barrales RR et al.","pubmed_publication_date":"15 Jan 2016","pubmed_entrez_date":"2016-01-09","publication_year":"2016","canto_session_key":"db997f5a4f033da9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sigurd Braun","canto_first_approved_date":"2019-01-31 17:58:27","canto_approved_date":"2026-01-12 13:07:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-28 17:45:09","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":56,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Sigurd Braun","community_curator":true,"annotation_count":43,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.16c","SPBCPT2R1.08c","SPAC212.11","SPCC1620.07c","SPBC582.04c","SPAC16A10.07c","SPBC800.03","SPBC428.08c","SPAC1851.03","SPCC4G3.11","SPAC14C4.05c","SPCC737.03c","SPBC2D10.17","SPAC18G6.10","SPAC18G6.02c","SPCC895.07","SPAC17G8.13c","SPBC29B5.01","SPBC2G2.14","SPBC16D10.07c"],"gene_count":20,"ltp_gene_count":16,"approved_date":"2019-01-31"},{"uniquename":"PMID:10454995","title":"Schizosaccharomyces pombe replication and repair proteins: proliferating cell nuclear antigen (PCNA).","citation":"Methods 1999 Jul;18(3):335-48, 324","abstract":"Schizosaccharomyces pombe has a cell cycle progression with distinctive phases that serves as a perfect model system for investigating DNA replication and repair of eukaryotic cells. Here, we use proliferating cell nuclear antigen (PCNA) of S. pombe to demonstrate how the function of this protein in both DNA replication and repair can be assessed by genetic and biochemical approaches. We describe a method of introducing site-specific mutations into the fission yeast PCNA gene pcn1(+). The in vivo effects of these pcn1 mutants in a strain with a null pcn1 background are described and their in vitro biochemical properties are characterized. Mutants described here are those that are defective in enhancing processivity of DNA polymerase delta, show temperature-sensitive growth, and have increased sensitivity to hydroxyurea (HU), UV and gamma irradiation, and methyl methanesulfonate (MMS). Three mutants that show reduced growth rate in vivo and decreased capacity to enhance polymerase delta DNA synthetic activity and processivity in vitro-pcn1-1, pcn1-5, and pcn1-26-are described as examples of using a genetic approach to identify the biochemical function of replication proteins. One cold-sensitive growth allele, pcn1-3, that has a recessive cold-sensitive cdc phenotype and shows sensitivity to HU and UV and gamma irradiation is used as an example of using the genetic approach to reveal the function of replication proteins in repair. The power of combining both biochemical and genetic disciplines is emphasized. Methods for site-directed mutagenesis, in vitro analysis of mutant proteins, and in vivo characterization of mutants in response to UV or gamma irradiation, MMS, HU, and temperature, as well as genetic epistasis are described. Locations of functionally significant residues on the PCNA tertiary structure are summarized.","authors":"Arroyo MP, Wang TS","authors_abbrev":"Arroyo MP et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-08-24","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12402243","title":"Molecular and structural characterization of the spindle pole bodies in the fission yeast Schizosaccharomyces japonicus var japonicus.","citation":"Yeast 2002 Nov;19(15):1335-50","abstract":"The structure and localization of the microtubule organization centres (MTOCs) of the fission yeast Schizosaccharomyces japonicus var. japonicus were examined by fluorescence microscopy and electron microscopy. Spindle pole bodies (SPBs), which are the fungal equivalent of centrosomes, of Sz. japonicus were visualized by immunofluorescent staining using a monoclonal anti-gamma-tubulin antibody. The behaviour of the SPBs during the cell cycle mostly coincided with previous reports on the most widely used fission yeast Schizosaccharomyces pombe. We cloned the gamma-tubulin gene from Sz. japonicus by PCR using redundant sets of primers corresponding to conserved regions of known gamma-tubulins. The predicted amino acid sequence of Sz. japonicus gamma-tubulin was most similar to the Sz. pombe gamma-tubulin. Under the electron microscope, the SPBs of Sz. japonicus were detected as electron-dense multilayered structures located just outside the nuclear envelope. The SPBs of Sz. japonicus were composed of three electron-dense layers and were surrounded by fuzzy material. Each layer showed structural changes according to the progression of the cell cycle. In mitotic cells, the SPBs were located on the fenestrae of the nuclear envelopes through which the mitotic spindle microtubules ran into the nucleoplasm. Our results show that Sz. japonicus is a very potent and attractive organism for the investigation of the microtubule nucleation system and morphogenesis in yeasts. The Accession No. for the nucleotide sequence of the Sz. japonicus gtb1(+) gene is AF159163.","authors":"Horio T, Kimura N, Basaki A, Tanaka Y, Noguchi T, Akashi T, Tanaka K","authors_abbrev":"Horio T et al.","pubmed_publication_date":"Nov 2002","pubmed_entrez_date":"2002-10-29","publication_year":"2002","canto_session_key":"eb026482cb19dfb9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-04-24 10:21:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-04-24 08:41:19","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-04-24"},{"uniquename":"PMID:7680030","title":"Ionic channels in the plasma membrane of Schizosaccharomyces pombe: evidence from patch-clamp measurements.","citation":"J Bioenerg Biomembr 1993 Feb;25(1):43-53","abstract":"Patch-clamp studies of the yeast Schizosaccharomyces pombe reveal that the plasma membrane contains a voltage-gated channel mildly selective for potassium over sodium, lithium, and chloride. The channel exhibits several conductances with a maximum of 153 pS. The channel gates in the region of physiologically relevant voltages, being closed at hyperpolarizing and open at depolarizing voltages. It is not inhibited by tetraethylammonium, quinine, or quinidine applied from the cytoplasmic side of the membrane; similarly, ATP and stretch have no effect. The frequency of its occurrence in patches implies that about 35 channels of this kind are present in the plasma membrane of a single cell.","authors":"Vacata V, Höfer M, Larsson HP, Lecar H","authors_abbrev":"Vacata V et al.","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000114","title":"Manual transfer of experimentally-verified manual GO annotation data to homologous complexes by curator judgment of sequence, composition and function similarity","abstract":"Method for transferring manual annotations to an entry based on a curator's judgment of its similarity to a putative homolog that has annotations that are supported with experimental evidence. Annotations are created when a curator judges that the sequence, composition and function of a complex shows high similarity to another complex that has annotation(s) supported by experimental evidence (and therefore display one of the evidence codes ECO:0000353 [IPI] or ECO:0005543). Annotations resulting from the transfer of GO terms display the ECO:0005610, ECO:0005544 or ECO:0005546 evidence codes and include an accession for the complex from which the annotation was projected in the 'with/from' field (column 8). This field MUST contain a Complex Portal accession identifier. Putative homologs are chosen using information combined from a variety of complementary sources. Potential homologs are initially identified using sequence similarity search programs such as BLAST. Homologous relationships are then verified manually using a combination of resources including sequence analysis tools, phylogenetic and comparative genomics databases such as Ensembl Compara, INPARANOID and OrthoMCL, as well as other specialised databases such as species-specific collections (e.g. HGNC's HCOP). In all cases curators check the alignments for each complex component and use their experience to assess whether similarity is considered to be strong enough to infer that the two proteins have a common function so that they can confidently project an annotation. While there is no fixed cut-off point in percentage sequence similarity, generally proteins which have greater than 70% identity that covers greater than 90% of the length of both proteins are examined further. Whilst we expect subunit composition to be conserved between closely related species, this is not an absolute rule and orthologous complexes may differ if a subunit cannot be traced in one species or is experimentally shown not to be present. When there is evidence of multiple paralogs for a single species, multiple variants of the complex can be inferred.","authors":"Birgit Meldal and Sandra Orchard (1). (1) European Bioinformatics Institute (EBI), Hinxton, Cambridgeshire, United Kingdom","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28632741","title":"Aging, mortality, and the fast growth trade-off of Schizosaccharomyces pombe.","citation":"PLoS Biol 2017 Jun;15(6):e2001109","abstract":"Replicative aging has been demonstrated in asymmetrically dividing unicellular organisms, seemingly caused by unequal damage partitioning. Although asymmetric segregation and inheritance of potential aging factors also occur in symmetrically dividing species, it nevertheless remains controversial whether this results in aging. Based on large-scale single-cell lineage data obtained by time-lapse microscopy with a microfluidic device, in this report, we demonstrate the absence of replicative aging in old-pole cell lineages of Schizosaccharomyces pombe cultured under constant favorable conditions. By monitoring more than 1,500 cell lineages in 7 different culture conditions, we showed that both cell division and death rates are remarkably constant for at least 50-80 generations. Our measurements revealed that the death rate per cellular generation increases with the division rate, pointing to a physiological trade-off with fast growth under balanced growth conditions. We also observed the formation and inheritance of Hsp104-associated protein aggregates, which are a potential aging factor in old-pole cell lineages, and found that these aggregates exhibited a tendency to preferentially remain at the old poles for several generations. However, the aggregates were eventually segregated from old-pole cells upon cell division and probabilistically allocated to new-pole cells. We found that cell deaths were typically preceded by sudden acceleration of protein aggregation; thus, a relatively large amount of protein aggregates existed at the very ends of the dead cell lineages. Our lineage tracking analyses, however, revealed that the quantity and inheritance of protein aggregates increased neither cellular generation time nor cell death initiation rates. Furthermore, our results demonstrated that unusually large amounts of protein aggregates induced by oxidative stress exposure did not result in aging; old-pole cells resumed normal growth upon stress removal, despite the fact that most of them inherited significant quantities of aggregates. These results collectively indicate that protein aggregates are not a major determinant of triggering cell death in S. pombe and thus cannot be an appropriate molecular marker or index for replicative aging under both favorable and stressful environmental conditions.","doi":"10.1371/journal.pbio.2001109","authors":"Nakaoka H, Wakamoto Y","authors_abbrev":"Nakaoka H et al.","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2017-06-21","publication_year":"2017","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2017-06-22 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26510788","title":"Escape from Mitotic Arrest: An Unexpected Connection Between Microtubule Dynamics and Epigenetic Regulation of Centromeric Chromatin in Schizosaccharomyces pombe.","citation":"Genetics 2015 Dec;201(4):1467-78","abstract":"Accurate chromosome segregation is necessary to ensure genomic integrity. Segregation depends on the proper functioning of the centromere, kinetochore, and mitotic spindle microtubules and is monitored by the spindle assembly checkpoint (SAC). In the fission yeast Schizosaccharomyces pombe, defects in Dis1, a microtubule-associated protein that influences microtubule dynamics, lead to mitotic arrest as a result of an active SAC and consequent failure to grow at low temperature. In a mutant dis1 background (dis1-288), loss of function of Msc1, a fission yeast homolog of the KDM5 family of proteins, suppresses the growth defect and promotes normal mitosis. Genetic analysis implicates a histone deacetylase (HDAC)-linked pathway in suppression because HDAC mutants clr6-1, clr3∆, and sir2∆, though not hos2∆, also promote normal mitosis in the dis1-288 mutant. Suppression of the dis phenotype through loss of msc1 function requires the spindle checkpoint protein Mad2 and is limited by the presence of the heterochromatin-associated HP1 protein homolog Swi6. We speculate that alterations in histone acetylation promote a centromeric chromatin environment that compensates for compromised dis1 function by allowing for successful kinetochore-microtubule interactions that can satisfy the SAC. In cells arrested in mitosis by mutation of dis1, loss of function of epigenetic determinants such as Msc1 or specific HDACs can promote cell survival. Because the KDM5 family of proteins has been implicated in human cancers, an appreciation of the potential role of this family of proteins in chromosome segregation is warranted.","doi":"10.1534/genetics.115.181792","authors":"George AA, Walworth NC","authors_abbrev":"George AA et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-10-30","publication_year":"2015","canto_session_key":"8cfc4cc05f46bb23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Anuja George","canto_first_approved_date":"2016-02-12 12:25:59","canto_approved_date":"2026-01-31 13:04:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-30 21:33:22","canto_added_date":"2015-10-31 01:19:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":46,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Anuja George","community_curator":true,"annotation_count":8,"orcid":"0000-0003-2643-6307","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.14","SPBC1709.11c","SPAC664.01c","SPAC11E3.01c","SPCC895.07","SPAC3G9.07c","SPBC800.03","SPBC16D10.07c","SPAC343.11c","SPBC36.05c","SPAC23C11.15","SPBC20F10.06"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2016-02-12"},{"uniquename":"PMID:26511279","title":"Meiotic cohesin-based chromosome structure is essential for homologous chromosome pairing in Schizosaccharomyces pombe.","citation":"Chromosoma 2016 Jun;125(2):205-14","abstract":"Chromosome structure is dramatically altered upon entering meiosis to establish chromosomal architectures necessary for the successful progression of meiosis-specific events. An early meiotic event involves the replacement of the non-SMC mitotic cohesins with their meiotic equivalents in most part of the chromosome, forming an axis on meiotic chromosomes. We previously demonstrated that the meiotic cohesin complex is required for chromosome compaction during meiotic prophase in the fission yeast Schizosaccharomyces pombe. These studies revealed that chromosomes are elongated in the absence of the meiotic cohesin subunit Rec8 and shortened in the absence of the cohesin-associated protein Pds5. In this study, using super-resolution structured illumination microscopy, we found that Rec8 forms a linear axis on chromosomes, which is required for the organized axial structure of chromatin during meiotic prophase. In the absence of Pds5, the Rec8 axis is shortened whereas chromosomes are widened. In rec8 or pds5 mutants, the frequency of homologous chromosome pairing is reduced. Thus, Rec8 and Pds5 play an essential role in building a platform to support the chromosome architecture necessary for the spatial alignment of homologous chromosomes.","doi":"10.1007/s00412-015-0551-8","authors":"Ding DQ, Matsuda A, Okamasa K, Nagahama Y, Haraguchi T, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2015-10-30","publication_year":"2016","canto_session_key":"6652a810a426bf5d","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-10-31 01:19:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5041874","title":"Glucose superrepressed and derepressed respiratory mutants in a \"petite-negative\" yeast: Schizosaccharomyces pombe 972h.","citation":"Biochem Biophys Res Commun 1972 Jul 11;48(1):153-60","abstract":"","authors":"Foury F, Goffeau A","authors_abbrev":"Foury F et al.","pubmed_publication_date":"11 Jul 1972","pubmed_entrez_date":"1972-07-11","publication_year":"1972","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8226914","title":"Single-stranded DNA binding activity of C1-tetrahydrofolate synthase enzymes.","citation":"J Biol Chem 1993 Nov 15;268(32):23792-8","abstract":"In eukaryotes C1-5,6,7,8-tetrahydrofolate (THF) synthase is a trifunctional enzyme that catalyzes the interconversion of reduced forms of folate to supply activated one-carbon units required for a variety of metabolic pathways. The enzymatic activities include 10-formyl-THF synthetase (EC 6.3.4.3), 5,10-methenyl-THF cyclohydrolase (EC 3.5.4.9), and 5,10-methylene-THF dehydrogenase (EC 1.5.1.5). In bacteria separate, monofunctional or bifunctional polypeptides catalyze the same reactions. We have purified C1-THF synthase from the fission yeast Schizosaccharomyces pombe and found its physical and enzymatic properties similar to those of other eukaryotic C1-THF synthase enzymes. Unexpectedly, the S. pombe enzyme bound strongly (Keq = 100 pM) to single-stranded DNA, but not to double-stranded DNA or to RNA. The binding was sequence-independent, apparently not cooperative, and not detectably inhibited by C1-THF synthase substrates or cofactors. Trifunctional cytoplasmic enzyme from Saccharomyces cerevisiae and monofunctional (synthetase) enzyme from Clostridium acidiurici also bound tightly to single-stranded DNA, while bifunctional (dehydrogenase and cyclohydrolase) enzyme from Escherichia coli did not, suggesting that single-stranded DNA binding is a conserved function of the synthetase domain of C1-THF synthase enzymes.","authors":"Wahls WP, Song JM, Smith GR","authors_abbrev":"Wahls WP et al.","pubmed_publication_date":"15 Nov 1993","pubmed_entrez_date":"1993-11-15","publication_year":"1993","canto_session_key":"80a894e329fdc13b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-07-31 13:32:35","canto_approved_date":"2024-04-25 15:23:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 13:32:28","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC839.16"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:18449558","title":"Sites of strong Rec12/Spo11 binding in the fission yeast genome are associated with meiotic recombination and with centromeres.","citation":"Chromosoma 2008 Oct;117(5):431-44","abstract":"Meiotic recombination arises from Rec12/Spo11-dependent formation of DNA double-strand breaks (DSBs) and their subsequent repair. We identified Rec12-binding peaks across the Schizosaccharomyces pombe genome using chromatin immunoprecipitation after reversible formaldehyde cross-linking combined with whole-genome DNA microarrays. Strong Rec12 binding coincided with previously identified DSBs at the recombination hotspots ura4A, mbs1, and mbs2 and correlated with DSB formation at a new site. In addition, Rec12 binding corresponded to eight novel conversion hotspots and correlated with crossover density in segments of chromosome I. Notably, Rec12 binding inversely correlated with guanine-cytosine (GC) content, contrary to findings in Saccharomyces cerevisiae. Although both replication origins and Rec12-binding sites preferred AT-rich gene-free regions, they seemed to exclude each other. We also uncovered a connection between binding sites of Rec12 and meiotic cohesin Rec8. Rec12-binding peaks lay often within 2.5 kb of a Rec8-binding peak. Rec12 binding showed preference for large intergenic regions and was found to bind preferentially near to genes expressed strongly in meiosis. Surprisingly, Rec12 binding was also detected in centromeric core regions, which raises the intriguing possibility that Rec12 plays additional roles in meiotic chromosome dynamics.","doi":"10.1007/s00412-008-0159-3","authors":"Ludin K, Mata J, Watt S, Lehmann E, Bähler J, Kohli J","authors_abbrev":"Ludin K et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-05-02","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20688779","title":"Genome-wide mapping of nuclear mitochondrial DNA sequences links DNA replication origins to chromosomal double-strand break formation in Schizosaccharomyces pombe.","citation":"Genome Res 2010 Sep;20(9):1250-61","abstract":"Chromosomal double-strand breaks (DSBs) threaten genome integrity and repair of these lesions is often mutagenic. How and where DSBs are formed is a major question conveniently addressed in simple model organisms like yeast. NUMTs, nuclear DNA sequences of mitochondrial origin, are present in most eukaryotic genomes and probably result from the capture of mitochondrial DNA (mtDNA) fragments into chromosomal breaks. NUMT formation is ongoing and was reported to cause de novo human genetic diseases. Study of NUMTs is likely to contribute to the understanding of naturally occurring chromosomal breaks. We show that Schizosaccharomyces pombe NUMTs are exclusively located in noncoding regions with no preference for gene promoters and, when located into promoters, do not affect gene transcription level. Strikingly, most noncoding regions comprising NUMTs are also associated with a DNA replication origin (ORI). Chromatin immunoprecipitation experiments revealed that chromosomal NUMTs are probably not acting as ORI on their own but that mtDNA insertions occurred directly next to ORIs, suggesting that these loci may be prone to DSB formation. Accordingly, induction of excessive DNA replication origin firing, a phenomenon often associated with human tumor formation, resulted in frequent nucleotide deletion events within ORI3001 subtelomeric chromosomal locus, illustrating a novel aspect of DNA replication-driven genomic instability. How mtDNA is fragmented is another important issue that we addressed by sequencing experimentally induced NUMTs. This highlighted regions of S. pombe mtDNA prone to breaking. Together with an analysis of human NUMTs, we propose that these fragile sites in mtDNA may correspond to replication pause sites.","doi":"10.1101/gr.104513.109","authors":"Lenglez S, Hermand D, Decottignies A","authors_abbrev":"Lenglez S et al.","pubmed_publication_date":"Sep 2010","pubmed_entrez_date":"2010-08-07","publication_year":"2010","canto_session_key":"dfeb2f3343e55e17","canto_annotation_status":"APPROVED","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_first_approved_date":"2014-04-04 10:09:42","canto_approved_date":"2025-10-04 07:06:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-19 10:16:19","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-04-04"},{"uniquename":"EMBL:AU013877","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26902262","title":"Regulating retrotransposon activity through the use of alternative transcription start sites.","citation":"EMBO Rep 2016 May;17(5):753-68","abstract":"Retrotransposons, the ancestors of retroviruses, have the potential for gene disruption and genomic takeover if not kept in check. Paradoxically, although host cells repress these elements by multiple mechanisms, they are transcribed and are even activated under stress conditions. Here, we describe a new mechanism of retrotransposon regulation through transcription start site (TSS) selection by altered nucleosome occupancy. We show that Fun30 chromatin remodelers cooperate to maintain a high level of nucleosome occupancy at retrotransposon-flanking long terminal repeat (LTR) elements. This enforces the use of a downstream TSS and the production of a truncated RNA incapable of reverse transcription and retrotransposition. However, in stressed cells, nucleosome occupancy at LTR elements is reduced, and the TSS shifts to allow for productive transcription. We propose that controlled retrotransposon transcription from a nonproductive TSS allows for rapid stress-induced activation, while preventing uncontrolled transposon activity in the genome.","doi":"10.15252/embr.201541866","authors":"Persson J, Steglich B, Smialowska A, Boyd M, Bornholdt J, Andersson R, Schurra C, Arcangioli B, Sandelin A, Nielsen O, Ekwall K","authors_abbrev":"Persson J et al.","pubmed_publication_date":"May 2016","pubmed_entrez_date":"2016-02-24","publication_year":"2016","canto_session_key":"d783c7b746270302","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-01-25 17:37:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1235.05c","SPAC25A8.01c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:18682829","title":"Meiotic recombination hotspots of fission yeast are directed to loci that express non-coding RNA.","citation":"PLoS One 2008 Aug 06;3(8):e2887","abstract":"Polyadenylated, mRNA-like transcripts with no coding potential are abundant in eukaryotes, but the functions of these long non-coding RNAs (ncRNAs) are enigmatic. In meiosis, Rec12 (Spo11) catalyzes the formation of dsDNA breaks (DSBs) that initiate homologous recombination. Most meiotic recombination is positioned at hotspots, but knowledge of the mechanisms is nebulous. In the fission yeast genome DSBs are located within 194 prominent peaks separated on average by 65-kbp intervals of DNA that are largely free of DSBs.\nWe compared the genome-wide distribution of DSB peaks to that of polyadenylated ncRNA molecules of the prl class. DSB peaks map to ncRNA loci that may be situated within ORFs, near the boundaries of ORFs and intergenic regions, or most often within intergenic regions. Unconditional statistical tests revealed that this colocalization is non-random and robust (P<or=5.5 x 10(-8)). Furthermore, we tested and rejected the hypothesis that the ncRNA loci and DSB peaks localize preferentially, but independently, to a third entity on the chromosomes.\nMeiotic DSB hotspots are directed to loci that express polyadenylated ncRNAs. This reveals an unexpected, possibly unitary mechanism for what directs meiotic recombination to hotspots. It also reveals a likely biological function for enigmatic ncRNAs. We propose specific mechanisms by which ncRNA molecules, or some aspect of RNA metabolism associated with ncRNA loci, help to position recombination protein complexes at DSB hotspots within chromosomes.","doi":"10.1371/journal.pone.0002887","authors":"Wahls WP, Siegel ER, Davidson MK","authors_abbrev":"Wahls WP et al.","pubmed_publication_date":"06 Aug 2008","pubmed_entrez_date":"2008-08-07","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14614509","title":"DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA.","citation":"Nature 2003 Nov 13;426(6963):198-203","abstract":"Telomeres, specialized protein-DNA complexes that cap the ends of linear chromosomes, are essential for protecting chromosomes from degradation and end-to-end fusions. The Pot1 (protection of telomeres 1) protein is a widely distributed eukaryotic end-capping protein, having been identified in fission yeast, microsporidia, plants and animals. Schizosaccharomyces pombe Pot1p is essential for telomere maintenance, and human POT1 has been implicated in telomerase regulation. Pot1 binds telomeric single-stranded DNA (ssDNA) with exceptionally high sequence specificity, the molecular basis of which has been unknown. Here we describe the 1.9-A-resolution crystal structure of the amino-terminal DNA-binding domain of S. pombe Pot1p complexed with ssDNA. The protein adopts an oligonucleotide/oligosaccharide-binding (OB) fold with two loops that protrude to form a clamp for ssDNA binding. The structure explains the sequence specificity of binding: in the context of the Pot1 protein, DNA self-recognition involving base-stacking and unusual G-T base pairs compacts the DNA. Any sequence change disrupts the ability of the DNA to form this structure, preventing it from contacting the array of protein hydrogen-bonding groups. The structure also explains how Pot1p avoids binding the vast excess of RNA in the nucleus.","authors":"Lei M, Podell ER, Baumann P, Cech TR","authors_abbrev":"Lei M et al.","pubmed_publication_date":"13 Nov 2003","pubmed_entrez_date":"2003-11-14","publication_year":"2003","canto_session_key":"227c34f04889af15","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-14 21:37:31","canto_approved_date":"2023-02-16 19:09:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-14 21:37:23","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26H5.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-14","pdb_entries":[{"pdb_id":"1qzh","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A/B/C/D/E/F","position":"2-185"}],"title":"Crystal structure of Pot1 (protection of telomere)- ssDNA complex","entry_authors":"Lei M,Podell ER,Baumann P,Cech TR","entry_authors_abbrev":"Lei M et al.","reference_uniquename":"PMID:14614509","experimental_method":"X-ray","resolution":"2.4"},{"pdb_id":"1qzg","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A/B","position":"2-185"}],"title":"Crystal structure of Pot1 (protection of telomere)- ssDNA complex","entry_authors":"Lei M,Podell ER,Baumann P,Cech TR","entry_authors_abbrev":"Lei M et al.","reference_uniquename":"PMID:14614509","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:34534388","title":"Identification of ksg1 mutation showing long-lived phenotype in fission yeast.","citation":"Genes Cells 2021 Dec;26(12):967-978","abstract":"Fission yeast is a good model organism for the study of lifespan. To elucidate the mechanism, we screened for long-lived mutants. We found a nonsense mutation in the ksg1 +  gene, which encodes an ortholog of mammalian PDK1 (phosphoinositide-dependent protein kinase). The mutation was in the PH domain of Ksg1 and caused defect in membrane localization and protein stability. Analysis of the ksg1 mutant revealed that the reduced amounts and/or activity of the Ksg1 protein are responsible for the increased lifespan. Ksg1 is essential for growth and known to phosphorylate multiple substrates, but the substrate responsible for the long-lived phenotype of ksg1 mutation is not yet known. Genetic analysis showed that deletion of pck2 suppressed the long-lived phenotype of ksg1 mutant, suggesting that Pck2 might be involved in the lifespan extension caused by ksg1 mutation.","doi":"10.1111/gtc.12897","authors":"Matsui K, Okamoto K, Hasegawa T, Ohtsuka H, Shimasaki T, Ihara K, Goto Y, Aoki K, Aiba H","authors_abbrev":"Matsui K et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-09-17","publication_year":"2021","canto_session_key":"77d28232979d22af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_first_approved_date":"2021-09-22 14:53:00","canto_approved_date":"2021-09-22 14:53:00","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-09-21 04:41:03","canto_added_date":"2021-09-19 00:15:05","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":1,"orcid":"0000-0002-7775-0446","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.04c","SPCC576.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-09-22"},{"uniquename":"PMID:11166217","title":"Timing is everything: regulation of mitotic exit and cytokinesis by the MEN and SIN.","citation":"Trends Cell Biol 2001 Feb;11(2):89-95","abstract":"Proper completion of mitosis requires careful coordination of numerous cellular events. It is crucial, for example, that cells do not initiate spindle disassembly and cytokinesis until chromosomes have been properly segregated. Cells have developed numerous safeguards or checkpoints to delay exit from mitosis and initiation of the next cell cycle in response to defects in late mitosis. In this review, we discuss recent work on two homologous signaling pathways in budding and fission yeast, termed the mitotic exit network (MEN) and septation initiation network (SIN), respectively, that are essential for coordinating completion of mitosis and cytokinesis with other mitotic events.","authors":"McCollum D, Gould KL","authors_abbrev":"McCollum D et al.","pubmed_publication_date":"Feb 2001","pubmed_entrez_date":"2001-02-13","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30451685","title":"Lipidation-independent vacuolar functions of Atg8 rely on its noncanonical interaction with a vacuole membrane protein.","citation":"Elife 2018 Nov 19;7","abstract":"The ubiquitin-like protein Atg8, in its lipidated form, plays central roles in autophagy. Yet, remarkably, Atg8 also carries out lipidation-independent functions in non-autophagic processes. How Atg8 performs its moonlighting roles is unclear. Here we report that in the fission yeast  Schizosaccharomyces pombe  and the budding yeast  Saccharomyces cerevisiae , the lipidation-independent roles of Atg8 in maintaining normal morphology and functions of the vacuole require its interaction with a vacuole membrane protein Hfl1 (homolog of human TMEM184 proteins). Crystal structures revealed that the Atg8-Hfl1 interaction is not mediated by the typical Atg8-family-interacting motif (AIM) that forms an intermolecular β-sheet with Atg8. Instead, the Atg8-binding regions in Hfl1 proteins adopt a helical conformation, thus representing a new type of AIMs (termed helical AIMs here). These results deepen our understanding of both the functional versatility of Atg8 and the mechanistic diversity of Atg8 binding.","doi":"10.7554/eLife.41237","authors":"Liu XM, Yamasaki A, Du XM, Coffman VC, Ohsumi Y, Nakatogawa H, Wu JQ, Noda NN, Du LL","authors_abbrev":"Liu XM et al.","pubmed_publication_date":"19 Nov 2018","pubmed_entrez_date":"2018-11-20","publication_year":"2018","canto_session_key":"577d9d669e38039c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xiao-Min Du","canto_first_approved_date":"2018-12-12 14:54:09","canto_approved_date":"2025-07-02 05:50:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-13 14:55:25","canto_added_date":"2018-11-21 01:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":61,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Xiao-Min Du","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.06c","SPBP8B7.24c","SPBC6B1.05c","SPBC3B9.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-12-12","pdb_entries":[{"pdb_id":"6aaf","gene_chains":[{"gene_uniquename":"SPBP8B7.24c","chain":"A","position":"1-116"},{"gene_uniquename":"SPAC30D11.06c","chain":"B","position":"386-409"}],"title":"Crystal structure of fission yeast Atg8 complexed with the helical AIM of Hfl1.","entry_authors":"Yamasaki A,Noda NN","entry_authors_abbrev":"Yamasaki A et al.","reference_uniquename":"PMID:30451685","experimental_method":"X-ray","resolution":"2.197"}]},{"uniquename":"PMID:29433856","title":"Studying anti-oxidative properties of inclusion complexes of α-lipoic acid with γ-cyclodextrin in single living fission yeast by confocal Raman microspectroscopy.","citation":"Spectrochim Acta A Mol Biomol Spectrosc 2018 May 15;197:237-243","abstract":"α-lipoic acid (ALA) is an essential cofactor for many enzyme complexes in aerobic metabolism, especially in mitochondria of eukaryotic cells where respiration takes place. It also has excellent anti-oxidative properties. The acid has two stereo-isomers, R- and S- lipoic acid (R-LA and S-LA), but only the R-LA has biological significance and is exclusively produced in our body. A mutant strain of fission yeast, Δdps1, cannot synthesize coenzyme Q10, which is essential during yeast respiration, leading to oxidative stress. Therefore, it shows growth delay in the minimal medium. We studied anti-oxidant properties of ALA in its free form and their inclusion complexes with γ-cyclodextrin using this mutant yeast model. Both free forms R- and S-LA as well as 1:1 inclusion complexes with γ-cyclodextrin recovered growth of Δdps1 depending on the concentration and form. However, it has no effect on the growth of wild type fission yeast strain at all. Raman microspectroscopy was employed to understand the anti-oxidant property at the molecular level. A sensitive Raman band at 1602cm -1  was monitored with and without addition of ALAs. It was found that 0.5mM and 1.0mM concentrations of ALAs had similar effect in both free and inclusion forms. At 2.5mM ALAs, free forms inhibited the growth while inclusion complexes helped in recovered. 5.0mM ALA showed inhibitory effect irrespective of form. Our results suggest that the Raman band at 1602cm -1  is a good measure of oxidative stress in fission yeast.","doi":"10.1016/j.saa.2018.02.011","authors":"Noothalapati H, Ikarashi R, Iwasaki K, Nishida T, Kaino T, Yoshikiyo K, Terao K, Nakata D, Ikuta N, Ando M, Hamaguchi HO, Kawamukai M, Yamamoto T","authors_abbrev":"Noothalapati H et al.","pubmed_publication_date":"15 May 2018","pubmed_entrez_date":"2018-02-14","publication_year":"2018","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2018-02-14 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24357230","title":"Cell migration and division in amoeboid-like fission yeast.","citation":"Biol Open 2014 Jan 15;3(1):108-15","abstract":"Yeast cells are non-motile and are encased in a cell wall that supports high internal turgor pressure. The cell wall is also essential for cellular morphogenesis and cell division. Here, we report unexpected morphogenetic changes in a Schizosaccharomyces pombe mutant defective in cell wall biogenesis. These cells form dynamic cytoplasmic protrusions caused by internal turgor pressure and also exhibit amoeboid-like cell migration resulting from repeated protrusive cycles. The cytokinetic ring responsible for cell division in wild-type yeast often fails in these cells; however, they were still able to divide using a ring-independent alternative mechanism relying on extrusion of the cell body through a hole in the cell wall. This mechanism of cell division may resemble an ancestral mode of division in the absence of cytokinetic machinery. Our findings highlight how a single gene change can lead to the emergence of different modes of cell growth, migration and division.","doi":"10.1242/bio.20136783","authors":"Flor-Parra I, Bernal M, Zhurinsky J, Daga RR","authors_abbrev":"Flor-Parra I et al.","pubmed_publication_date":"15 Jan 2014","pubmed_entrez_date":"2013-12-21","publication_year":"2014","canto_session_key":"2abadc3566985929","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29770351","title":"A Microfluidic Device for Massively Parallel, Whole-lifespan Imaging of Single Fission Yeast Cells.","citation":"Bio Protoc 2018 Apr 05;8(7)","abstract":"Whole-lifespan single-cell analysis has greatly increased our understanding of fundamental cellular processes such as cellular aging. To observe individual cells across their entire lifespan, all progeny must be removed from the growth medium, typically via manual microdissection. However, manual microdissection is laborious, low-throughput, and incompatible with fluorescence microscopy. Here, we describe assembly and operation of the multiplexed-Fission Yeast Lifespan Microdissector (multFYLM), a high-throughput microfluidic device for rapidly acquiring single-cell whole-lifespan imaging. multFYLM captures approximately one thousand rod-shaped fission yeast cells from up to six different genetic backgrounds or treatment regimens. The immobilized cells are fluorescently imaged for over a week, while the progeny cells are removed from the device. The resulting datasets yield high-resolution multi-channel images that record each cell's replicative lifespan. We anticipate that the multFYLM will be broadly applicable for single-cell whole-lifespan studies in the fission yeast ( Schizosaccharomyces pombe ) and other symmetrically-dividing unicellular organisms.","doi":"10.21769/BioProtoc.2783","authors":"Jones SK, Spivey EC, Rybarski JR, Finkelstein IJ","authors_abbrev":"Jones SK et al.","pubmed_publication_date":"05 Apr 2018","pubmed_entrez_date":"2018-05-18","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-05-19 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38408667","title":"A strategy for the investigation of toxic mechanisms and protection by efflux pumps using Schizosaccharomyces pombe strains: Application to rotenone.","citation":"Sci Total Environ 2024 Feb 24;:171253","abstract":"Effects not related with the inhibition of complex I of the mitochondrial electron transport chain are studied in S. pombe, which lacks it. This study aims: First, the use of a strategy with S. pombe strains to investigate the toxicity, mechanisms of action, interactions and detoxication by efflux pumps. Second, to investigate the mechanisms of toxic action of rotenone. In the dose-response assessment, the yeast presented a good correlation with the toxicity in Daphnia magna for 15 chemicals. In the mechanistic study, the mph1Δ strain presented marked specificity to the interaction with microtubules by carbendazim. DNA damage caused by hydroxyurea, an inhibitor of deoxynucleotide synthesis, was identified with marked specificity with the rad3Δ strain. The sty1Δ strain was very sensitive to the oxidative and osmotic stress induced by hydrogen peroxide and potassium chloride, respectively, being more sensitive to oxidative stress than the pap1Δ strain. The protection by exclusion pumps was also evaluated. Rotenone presented low toxicity in S. pombe due to the lack of its main target, and the marked protection by the exclusion transporters Bfr1, Pmd1, Caf5 and Mfs1. Marked cellular stress was detected. Finally, the toxicity of rotenone could be potentiated by the fungicide carbendazim and the antimetabolite hydroxyurea. In conclusion, the use of S. pombe strains is a valid strategy to: a) assess global toxicity; b) investigate the main mechanisms of toxic action, particularly spindle and DNA interferences, and osmotic and oxidative stress not related to complex I inhibition; c) explore the detoxication by efflux pumps; and d) evaluate possible chemical interactions. Therefore, it should be useful for the investigation of adverse outcome pathways.","doi":"10.1016/j.scitotenv.2024.171253","authors":"Álvarez-Herrera C, Maisanaba S, Ruíz-Cabello ML, Rojas R, Repetto G","authors_abbrev":"Álvarez-Herrera C et al.","pubmed_publication_date":"24 Feb 2024","pubmed_entrez_date":"2024-02-26","publication_year":"2024","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2024-02-28 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19752195","title":"Meiotic DNA double-strand break repair requires two nucleases, MRN and Ctp1, to produce a single size class of Rec12 (Spo11)-oligonucleotide complexes.","citation":"Mol Cell Biol 2009 Nov;29(22):5998-6005","abstract":"Programmed DNA double-strand breaks (DSBs) in meiosis are formed by Spo11 (Rec12 in fission yeast), a topoisomerase II-like protein, which becomes covalently attached to DNA 5' ends. For DSB repair through homologous recombination, the protein must be removed from these DNA ends. We show here that Rec12 is endonucleolytically removed from DSB ends attached to a short oligonucleotide (Rec12-oligonucleotide complex), as is Spo11 in budding yeast. Fission yeast, however, has only one size class of Rec12-oligonucleotide complexes, whereas budding yeast has two size classes, suggesting different endonucleolytic regulatory mechanisms. Rec12-oligonucleotide generation strictly requires Ctp1 (Sae2 nuclease homolog), the Rad32 (Mre11) nuclease domain, and Rad50 of the MRN complex. Surprisingly, Nbs1 is not strictly required, indicating separable roles for the MRN subunits. On the basis of these and other data, we propose that Rad32 nuclease has the catalytic site for Rec12-oligonucleotide generation and is activated by Ctp1, which plays an additional role in meiotic recombination.","doi":"10.1128/MCB.01127-09","authors":"Milman N, Higuchi E, Smith GR","authors_abbrev":"Milman N et al.","pubmed_publication_date":"Nov 2009","pubmed_entrez_date":"2009-09-16","publication_year":"2009","canto_session_key":"b2cf102d334e3cc1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-03-10 15:48:34","canto_approved_date":"2023-01-06 16:00:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-10 15:48:20","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13C5.07","SPBC29A10.05","SPAC25G10.04c","SPBC6B1.09c","SPCC338.08","SPAC1556.01c","SPAC17A5.11"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-03-10"},{"uniquename":"PMID:24177583","title":"Genetic studies of purine breakdown in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1984 Feb;8(2):99-105","abstract":"Purines such as hypoxanthine, xanthine, uric acid, allantoin and allantoic acid serve as sole nitrogen sources for the yeast Schizosaccharomyces pombe. A number of classes of mutants unable to use purines have been isolated and genetically analysed. Mutants in the urol gene lack uricase, all1 lack allantoinase, ala1 lack allantoicase whilst in ure1, ure2, ure3 and ure4 genes lack urease activity. Mutants in four hyp genes are unable to convert hypoxanthine to uric acid whilst mutation in xan1 results in impaired growth with xanthine. hyp5 strains are unable to convert both hypoxanthine and xanthine to uric acid. The mutations are recessive and none of the loci are linked to each other. The possible catalytic steps involved are discussed.","doi":"10.1007/BF00420225","authors":"Kinghorn JR, Fluri R","authors_abbrev":"Kinghorn JR et al.","pubmed_publication_date":"Feb 1984","pubmed_entrez_date":"2013-11-02","publication_year":"1984","canto_session_key":"06b55ebb33ef8187","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-09-22 18:08:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-21 15:07:46","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.09","SPAC1F7.09c","SPAC1952.11c","SPCC576.01c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2016-09-21"},{"uniquename":"PMID:24256267","title":"The links between chromatin spatial organization and biological function.","citation":"Biochem Soc Trans 2013 Dec;41(6):1634-9","abstract":"During the last few years, there has been a rapid increase in our knowledge of how chromatin is organized inside the nucleus. Techniques such as FISH (fluorescence in situ hybridization) have proved that chromosomes organize themselves in so-called CTs (chromosome territories). In addition, newly developed 3C (chromatin conformation capture) techniques have revealed that certain chromosomal regions tend to interact with adjacent regions on either the same chromosome or adjacent chromosomes, and also that regions in close proximity are replicated simultaneously. Furthermore, transcriptionally repressed or active areas occupy different nuclear compartments. Another new technique, named DamID (DNA adenine methyltransferase identification), has strengthened the notion that transcriptionally repressed genes are often found in close association with the nuclear membrane, whereas transcriptionally active regions are found in the more central regions of the nucleus. However, in response to various stimuli, transcriptionally repressed regions are known to relocalize from the nuclear lamina to the interior of the nucleus, leading to a concomitant up-regulation of otherwise silenced genes. Taken together, these insights are of great interest for the relationship between chromosomal spatial organization and genome function. In the present article, we review recent advances in this field with a focus on mammalian cells and the eukaryotic model organism Schizosaccharomyces pombe.","doi":"10.1042/BST20130213","authors":"Rodriguez A, Bjerling P","authors_abbrev":"Rodriguez A et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36613592","title":"The Greatwall-Endosulfine Switch Accelerates Autophagic Flux during the Cell Divisions Leading to G1 Arrest and Entry into Quiescence in Fission Yeast.","citation":"Int J Mol Sci 2022 Dec 21;24(1)","abstract":"Entry into quiescence in the fission yeast  Schizosaccharomyces pombe  is induced by nitrogen starvation. In the absence of nitrogen, proliferating fission yeast cells divide twice without cell growth and undergo cell cycle arrest in G1 before becoming G0 quiescent cells. Under these conditions, autophagy is induced to produce enough nitrogen for the two successive cell divisions that take place before the G1 arrest. In parallel to the induction of autophagy, the Greatwall-Endosulfine switch is activated upon nitrogen starvation to down-regulate protein phosphatase PP2A/B55 activity, which is essential for cell cycle arrest in G1 and implementation of the quiescent program. Here we show that, although inactivation of PP2A/B55 by the Greatwall-Endosulfine switch is not required to promote autophagy initiation, it increases autophagic flux at least in part by upregulating the expression of a number of autophagy-related genes.","doi":"10.3390/ijms24010148","authors":"Vázquez-Bolado A, López-San Segundo R, García-Blanco N, Rozalén AE, González-Álvarez D, Suárez MB, Pérez-Hidalgo L, Moreno S","authors_abbrev":"Vázquez-Bolado A et al.","pubmed_publication_date":"21 Dec 2022","pubmed_entrez_date":"2023-01-08","publication_year":"2022","canto_session_key":"0b105945ceff7c6f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-01-09 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8610150","title":"Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes.","citation":"Proc Natl Acad Sci U S A 1996 Apr 02;93(7):2958-63","abstract":"Hsubc9, a human gene encoding a ubiquitin-conjugating enzyme, has been cloned. The 18-kDa HsUbc9 protein is homologous to the ubiquitin-conjugating enzymes Hus5 of Schizosaccharomyces pombe and Ubc9 of Saccharomyces cerevisiae. The Hsubc9 gene complements a ubc9 mutation of S. cerevisiae. It has been mapped to chromosome 16p13.3 and is expressed in many human tissues, with the highest levels in testis and thymus. According to the Ga14 two-hybrid system analysis, HsUbc9 protein interacts with human recombination protein Rad51. A mouse homolog, Mmubc9, encodes an amino acid sequence that is identical to the human protein. In mouse spermatocytes, MmUbc9 protein, like Rad51 protein, localizes in synaptonemal complexes, which suggests that Ubc9 protein plays a regulatory role in meiosis.","authors":"Kovalenko OV, Plug AW, Haaf T, Gonda DK, Ashley T, Ward DC, Radding CM, Golub EI","authors_abbrev":"Kovalenko OV et al.","pubmed_publication_date":"02 Apr 1996","pubmed_entrez_date":"1996-04-02","publication_year":"1996","canto_session_key":"a71539671c66d432","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-01-08 14:27:52","canto_approved_date":"2018-01-08 14:27:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-08 14:27:43","canto_added_date":"2012-02-24 05:53:56","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.13","SPAC644.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-01-08"},{"uniquename":"PMID:19625445","title":"Role for RACK1 orthologue Cpc2 in the modulation of stress response in fission yeast.","citation":"Mol Biol Cell 2009 Sep;20(18):3996-4009","abstract":"The receptor of activated C kinase (RACK1) is a protein highly conserved among eukaryotes. In mammalian cells, RACK1 functions as an adaptor to favor protein kinase C (PKC)-mediated phosphorylation and subsequent activation of c-Jun NH(2)-terminal kinase mitogen-activated protein kinase. Cpc2, the RACK1 orthologue in the fission yeast Schizosaccharomyces pombe, is involved in the control of G2/M transition and interacts with Pck2, a PKC-type protein member of the cell integrity Pmk1 mitogen-activated protein kinase (MAPK) pathway. Both RACK1 and Cpc2 are structural components of the 40S ribosomal subunit, and recent data suggest that they might be involved in the control of translation. In this work, we present data supporting that Cpc2 negatively regulates the cell integrity transduction pathway by favoring translation of the tyrosine-phosphatases Pyp1 and Pyp2 that deactivate Pmk1. In addition, Cpc2 positively regulates the synthesis of the stress-responsive transcription factor Atf1 and the cytoplasmic catalase, a detoxificant enzyme induced by treatment with hydrogen peroxide. These results provide for the first time strong evidence that the RACK1-type Cpc2 protein controls from the ribosome the extent of the activation of MAPK cascades, the cellular defense against oxidative stress, and the progression of the cell cycle by regulating positively the translation of specific gene products involved in key biological processes.","authors":"Núñez A, Franco A, Madrid M, Soto T, Vicente J, Gacto M, Cansado J","authors_abbrev":"Núñez A et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-07-24","publication_year":"2009","canto_session_key":"1450287ab46a1564","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-20 16:53:34","canto_approved_date":"2021-09-29 08:14:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-15 21:35:43","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":83,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.04c","SPBC409.07c","SPCC576.03c","SPAC2G11.07c","SPBP4H10.04","SPCC757.07c","SPAC19D5.01","SPAC1783.07c","SPBC3F6.03","SPAC6B12.15","SPCC4F11.02","SPBC1685.01","SPBC119.08","SPAC24B11.06c","SPAC3G9.09c","SPAC26F1.10c","SPBC29B5.01"],"gene_count":17,"ltp_gene_count":11,"approved_date":"2020-11-20"},{"uniquename":"PMID:1944368","title":"The involvement of reactive oxygen species in the direct-acting mutagenicity of wine.","citation":"Mutat Res 1991 Nov;251(1):115-21","abstract":"The Ara forward mutagenicity assay with Salmonella typhimurium detected wine as a strong mutagen in the absence of mammalian microsomal activation and/or glycosidase activities, in agreement with previous findings. The standard amount (50 microliters) of S9 fraction in the preincubation mutagenesis test abolished most of the mutagenic activity of red wine in the Ara assay. The S9 fraction exerted the same inactivating capacity on hydrogen peroxide and coffee, a complex mixture generating H2O2. Catalase was identified as the putative S9 component responsible for its inactivating capacity. This specific scavenger for H2O2 abolished around 90% of the mutagenicity of red wine. The suppressing effect of catalase was much less noticeable in white and rose wines. Phenolics are proposed to be responsible for the direct-acting mutagenicity of wine through an auto-oxidative process leading to the production of H2O2.","authors":"Ariza RR, Pueyo C","authors_abbrev":"Ariza RR et al.","pubmed_publication_date":"Nov 1991","pubmed_entrez_date":"1991-11-01","publication_year":"1991","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-09-09 08:54:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35939705","title":"Cohesin ATPase activities regulate DNA binding and coiled-coil configuration.","citation":"Proc Natl Acad Sci U S A 2022 Aug 16;119(33):e2208004119","abstract":"The cohesin complex is required for sister chromatid cohesion and genome compaction. Cohesin coiled coils (CCs) can fold at break sites near midpoints to bring head and hinge domains, located at opposite ends of coiled coils, into proximity. Whether ATPase activities in the head play a role in this conformational change is yet to be known. Here, we dissected functions of cohesin ATPase activities in cohesin dynamics in  Schizosaccharomyces pombe . Isolation and characterization of cohesin ATPase temperature-sensitive (ts) mutants indicate that both ATPase domains are required for proper chromosome segregation. Unbiased screening of spontaneous suppressor mutations rescuing the temperature lethality of cohesin ATPase mutants identified several suppressor hotspots in cohesin that located outside of ATPase domains. Then, we performed comprehensive saturation mutagenesis targeted to these suppressor hotspots. Large numbers of the identified suppressor mutations indicated several different ways to compensate for the ATPase mutants: 1) Substitutions to amino acids with smaller side chains in coiled coils at break sites around midpoints may enable folding and extension of coiled coils more easily; 2) substitutions to arginine in the DNA binding region of the head may enhance DNA binding; or 3) substitutions to hydrophobic amino acids in coiled coils, connecting the head and interacting with other subunits, may alter conformation of coiled coils close to the head. These results reflect serial structural changes in cohesin driven by its ATPase activities potentially for packaging DNAs.","doi":"10.1073/pnas.2208004119","authors":"Xu X, Kanai R, Wang L, Yanagida M","authors_abbrev":"Xu X et al.","pubmed_publication_date":"16 Aug 2022","pubmed_entrez_date":"2022-08-08","publication_year":"2022","canto_session_key":"914380d0d7df1e28","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-08-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC01909","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15380085","title":"Protein degradation: recognition of ubiquitinylated substrates.","citation":"Curr Biol 2004 Sep 21;14(18):R754-6","abstract":"A cell-free system has been developed in budding yeast that provides direct evidence that the Dsk2/Dph1, Rad23/Rhp23 and Rpn10/Pus1 multi-ubiquitin-binding proteins, long implicated in substrate recognition and presentation to the 26S proteasome, actually fulfil such a role.","authors":"Hartmann-Petersen R, Gordon C","authors_abbrev":"Hartmann-Petersen R et al.","pubmed_publication_date":"21 Sep 2004","pubmed_entrez_date":"2004-09-24","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC06944","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31431504","title":"The TOR pathway modulates cytoophidium formation in  Schizosaccharomyces pombe .","citation":"J Biol Chem 2019 Oct 04;294(40):14686-14703","abstract":"CTP synthase (CTPS) has been demonstrated to form evolutionarily-conserved filamentous structures termed cytoophidia whose exact cellular functions remain unclear, but they may play a role in intracellular compartmentalization. We have previously shown that the mammalian target of rapamycin complex 1 (mTORC1)-S6K1 pathway mediates cytoophidium assembly in mammalian cells. Here, using the fission yeast  Schizosaccharomyces pombe  as a model of a unicellular eukaryote, we demonstrate that the target of rapamycin (TOR)-signaling pathway regulates cytoophidium formation (from the  S. pombe  CTPS ortholog Cts1) also in  S. pombe  Conducting a systematic analysis of all viable single TOR subunit-knockout mutants and of several major downstream effector proteins, we found that Cts1 cytoophidia are significantly shortened and often dissociate when TOR is defective. We also found that the activities of the downstream effector kinases of the TORC1 pathway, Sck1, Sck2, and Psk1 S6, as well as of the S6K/AGC kinase Gad8, the major downstream effector kinase of the TORC2 pathway, are necessary for proper cytoophidium filament formation. Interestingly, we observed that the Crf1 transcriptional corepressor for ribosomal genes is a strong effector of Cts1 filamentation. Our findings connect TOR signaling, a major pathway required for cell growth, with the compartmentalization of the essential nucleotide synthesis enzyme CTPS, and we uncover differences in the regulation of its filamentation among higher multicellular and unicellular eukaryotic systems.","doi":"10.1074/jbc.RA119.009913","authors":"Andreadis C, Hulme L, Wensley K, Liu JL","authors_abbrev":"Andreadis C et al.","pubmed_publication_date":"04 Oct 2019","pubmed_entrez_date":"2019-08-22","publication_year":"2019","canto_session_key":"bd55441ed5240880","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-08-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12589443","title":"Isolation and characterisation of a calnexin homologue, clxA, from Aspergillus niger.","citation":"Mol Genet Genomics 2003 Feb;268(5):684-91","abstract":"We describe the isolation of a gene (clxA) encoding calnexin from laboratory and industrial strains of Aspergillus niger. Calnexin is a chaperone, which specifically recognises monoglucosylated glycoproteins in the endoplasmic reticulum, and is thus an essential component of the process that assesses the folded state of nascent secreted glycoproteins. Manipulation of chaperones has previously been adopted in attempts to overcome some of the problems associated with the secretion of heterologous proteins from filamentous fungi. The A. niger clxA gene encodes a 562-residue protein with strong homology to the calnexin of Schizosaccharomyces pombe. The clxAgene product complements a S. pombe cnx1 mutant. Motifs associated with genes controlled via the Unfolded Protein Response (UPR) were identified by sequence homology in the promoter of clxA. Steady-state levels of clxA mRNA were elevated in a strain expressing bovine prochymosin fused to the catalytic domain of glucoamylase. The ORF is punctuated by four introns, and contains two sets of four repeated peptide motifs that are characteristic of the calnexin family, together with a putative membrane-spanning domain. Deletion studies indicate that clxA is not an essential gene in A. niger.","authors":"Wang H, Entwistle J, Morlon E, Archer DB, Peberdy JF, Ward M, Jeenes DJ","authors_abbrev":"Wang H et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-02-18","publication_year":"2003","canto_session_key":"994db43e72ed84f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-01-18 20:53:35","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-01-18 19:53:05","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.11c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2017-01-18"},{"uniquename":"PMID:7499258","title":"Cloning and functional analysis of the ndk1 gene encoding nucleoside-diphosphate kinase in Schizosaccharomyces pombe.","citation":"J Biol Chem 1995 Nov 17;270(46):27859-64","abstract":"We cloned the ndk1 gene encoding a subunit of nucleoside-diphosphate kinase (NDK) from Schizosaccharomyces pombe, by using polymerase chain reaction. The deduced ndk1 gene product has 151 amino acid residues and is approximately 60% identical with both Saccharomyces cerevisiae and mammalian NDKs. The gene product exhibited NDK activity and cross-reacted with antibodies raised against rat NDK. Disruption of ndk1 greatly reduced the cellular NDK activity but caused no obvious phenotype in cell growth and sexual development of the organism. However, a mutated allele of ndk1 could inhibit sexual development in a dominant-negative manner. This allele carried a point mutation in cysteine 116, which locates next to the putative active center histidine 117, and the mutant gene product showed no NDK activity. Gene expression inducible in response to mating pheromone signaling was decreased in cells carrying the dominant-negative allele. Cases have been reported in higher eukaryotes in which NDK appears to play a more sophisticated role than a simple catalyst in cell physiology, and the results of this study suggest that S. pombe NDK may also perform such a role in regulation of sexual development in the fission yeast.","authors":"Izumiya H, Yamamoto M","authors_abbrev":"Izumiya H et al.","pubmed_publication_date":"17 Nov 1995","pubmed_entrez_date":"1995-11-17","publication_year":"1995","canto_session_key":"fdb914c5d5d12458","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-27 16:11:02","canto_approved_date":"2022-03-17 13:07:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-26 09:58:58","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC806.07","SPAC1296.03c","SPMTR.01","SPAC27D7.03c","SPMTR.02"],"gene_count":6,"ltp_gene_count":1,"approved_date":"2015-02-27"},{"uniquename":"PMID:2406130","title":"A mutation in a single gene of Schizosaccharomyces pombe affects the expression of several snRNAs and causes defects in RNA processing.","citation":"EMBO J 1990 Feb;9(2):525-34","abstract":"A bank of temperature sensitive (ts-) mutants of Schizosaccharomyces pombe was screened for snRNA expression mutants using an oligodeoxynucleotide that recognizes U2 RNA. One mutant with a novel phenotype was identified that has reduced steady-state levels of the spliceosomal snRNAs U1, U2, U4, U5 and U6. In addition, the mutant exhibits a temperature-dependent accumulation of aberrant U2 and U4 transcripts elongated at their 3' end. The steady-state concentration of the RNA component of RNase P is also reduced in the mutant, whereas the amount of U3 RNA, 7SL RNA, tRNA, rRNA and mRNA are the same as wild-type. Pre-mRNA, pre-tRNA and U6 RNA precursor processing are impaired in the mutant. Genetic analysis demonstrates that the snRNA defects are tightly linked to the ts- growth defect and are recessive. We have named this mutant snm1 to indicate a defect in snRNA maintenance. The data on snm1 suggest that a single trans-acting factor is essential for the maintenance of steady-state levels of several snRNAs and for proper 3' end formation of U2 and U4 RNAs.","authors":"Potashkin J, Frendewey D","authors_abbrev":"Potashkin J et al.","pubmed_publication_date":"Feb 1990","pubmed_entrez_date":"1990-02-01","publication_year":"1990","canto_session_key":"3f99f4c4c350c480","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-01-20 15:02:51","canto_approved_date":"2026-01-29 17:18:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-20 15:02:43","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.04","SPSNRNA.02","SPSNRNA.01","SPSNRNA.03","SPSNRNA.05","SPNCRNA.98","SPSNRNA.06","SPNCRNA.128","SPBC119.11c"],"gene_count":9,"ltp_gene_count":1,"approved_date":"2014-01-20"},{"uniquename":"PMID:29289567","title":"The Affinity of the S9.6 Antibody for Double-Stranded RNAs Impacts the Accurate Mapping of R-Loops in Fission Yeast.","citation":"J Mol Biol 2018 Feb 02;430(3):272-284","abstract":"R-loops, which result from the formation of stable DNA:RNA hybrids, can both threaten genome integrity and act as physiological regulators of gene expression and chromatin patterning. To characterize R-loops in fission yeast, we used the S9.6 antibody-based DRIPc-seq method to sequence the RNA strand of R-loops and obtain strand-specific R-loop maps at near nucleotide resolution. Surprisingly, preliminary DRIPc-seq experiments identified mostly RNase H-resistant but exosome-sensitive RNAs that mapped to both DNA strands and resembled RNA:RNA hybrids (dsRNAs), suggesting that dsRNAs form widely in fission yeast. We confirmed in vitro that S9.6 can immuno-precipitate dsRNAs and provide evidence that dsRNAs can interfere with its binding to R-loops. dsRNA elimination by RNase III treatment prior to DRIPc-seq allowed the genome-wide and strand-specific identification of genuine R-loops that responded in vivo to RNase H levels and displayed classical features associated with R-loop formation. We also found that most transcripts whose levels were altered by in vivo manipulation of RNase H levels did not form detectable R-loops, suggesting that prolonged manipulation of R-loop levels could indirectly alter the transcriptome. We discuss the implications of our work in the design of experimental strategies to probe R-loop functions.","doi":"10.1016/j.jmb.2017.12.016","authors":"Hartono SR, Malapert A, Legros P, Bernard P, Chédin F, Vanoosthuyse V","authors_abbrev":"Hartono SR et al.","pubmed_publication_date":"02 Feb 2018","pubmed_entrez_date":"2018-01-01","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-01-02 01:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16802154","title":"Enhanced productivity of protease-sensitive heterologous proteins by disruption of multiple protease genes in the fission yeast Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2006 Nov;73(2):404-20","abstract":"The creation of protease-deficient mutants to avoid product degradation is one of the current strategies employed to improve productivity and secretion efficiency of heterologous protein expression. We previously constructed a set of single protease-deficient mutants of the fission yeast Schizosaccharomyces pombe by respective disruption of 52 protease genes, and we succeeded in confirming useful disruptants (Idiris et al., Yeast 23:83-99, 2006). In the present study, we attempted multiple deletions of 13 protease genes, single deletions of which were previously confirmed as being beneficial for reducing extracellular product degradation. Using PCR-based gene replacement, a series of multiple deletion strains was constructed by multiple disruption of a maximum of seven protease genes. Effects of the resultant multiple deletion strains on heterologous expression were then measured by practical expression of a proteolytically sensitive model protein, the human growth hormone (hGH). Time profiles of hGH secretion from each resultant mutant demonstrated significantly enhanced hGH productivity with processing of the multiple protease deletions. The data clearly indicated that disruption of multiple protease genes in the fission yeast is an effective method for controlling proteolytic degradation of heterologous proteins particularly susceptible to proteases.","authors":"Idiris A, Tohda H, Bi KW, Isoai A, Kumagai H, Giga-Hama Y","authors_abbrev":"Idiris A et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-06-28","publication_year":"2006","canto_session_key":"72fdbcb425faf443","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-15 23:58:02","canto_approved_date":"2019-10-16 00:14:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-15 23:57:51","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.01","SPAC19B12.08","SPAC23H4.09","SPBC18E5.12c","SPAC22G7.01c","SPBC14C8.03","SPCC1259.10","SPAC4F10.02","SPAC1296.03c","SPBC18A7.01","SPBC1711.12","SPAP14E8.04","SPAC4A8.04"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2016-02-15"},{"uniquename":"PMID:10561610","title":"Protection against thermal denaturation by trehalose on the plasma membrane H+-ATPase from yeast. Synergetic effect between trehalose and phospholipid environment.","citation":"Eur J Biochem 1999 Dec;266(2):660-4","abstract":"Yeast cells have had to develop mechanisms in order to protect themselves from chemical and physical agents of the environment to which they are exposed. One of these physical agents is thermal variation. Some yeast cells are known to accumulate high concentrations of trehalose when submitted to heat shock. In this work, we have studied the effect of trehalose on the protection against thermal inactivation of purified plasma membrane H+-ATPase from Schizosaccharomyces pombe, in the solubilized and in the reconstituted state. We observed that after 1 min of incubation at 51 degrees C in the presence of 1 M trehalose, about 50% of soluble enzyme remains active. In the same conditions, but in the absence of trehalose, the activity was completely abolished. The t0.5 for the enzyme inactivation increased from 10 to 50 s after reconstitution into asolectin liposomes. Curiously, in the presence of 1 M trehalose, the t0.5 for inactivation of the reconstituted enzyme was further increased to higher than 300 s, regardless of whether trehalose was added inside or outside the liposome. Additionally, the concentration that confers 50% for the protection by trehalose (K0.5) decreased from 0.5 M, in the solubilized state, to 0.04 M in the reconstituted state, suggesting a synergetic effect between sugar and lipids. Gel electrophoresis revealed that the pattern of H+-ATPase cleavage by trypsin changed when 1 M trehalose was present in the buffer. It is suggested that both in a soluble and in a phospholipid environment, accumulation of trehalose leads to a more heat-stable conformation of the enzyme, probably an E2-like form.","authors":"Felix CF, Moreira CC, Oliveira MS, Sola-Penna M, Meyer-Fernandes JR, Scofano HM, Ferreira-Pereira A","authors_abbrev":"Felix CF et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-11-24","publication_year":"1999","canto_session_key":"3a1661e31e817163","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-31 15:44:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-31 15:44:46","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-03-31"},{"uniquename":"PMID:38998544","title":"Effects of Heterologous Expression of Genes Related L-Malic acid Metabolism in  Saccharomyces uvarum  on Flavor Substances Production in Wine.","citation":"Foods 2024 Jun 27;13(13)","abstract":"During malolactic fermentation (MLF) of vinification, the harsh L-malic acid undergoes transformation into the milder L-lactic acid, and via decarboxylation reactions it is catalyzed by malolactic enzymes in LAB. The use of bacterial malolactic starter cultures, which usually present challenges in the industry as the suboptimal conditions after alcoholic fermentation (AF), including nutrient limitations, low temperatures, acidic pH levels, elevated alcohol, and sulfur dioxide concentrations after AF, lead to \"stuck\" or \"sluggish\" MLF and spoilage of wines.  Saccharomyces uvarum  has interesting oenological properties and provides a stronger aromatic intensity than  Saccharomyces cerevisiae  in AF. In the study, the biological pathways of deacidification were constructed in  S. uvarum , which made the  S. uvarum  carry out the AF and MLF simultaneously, as different genes encoding malolactic enzyme ( mleS  or  mleA ), malic enzyme ( MAE2 ), and malate permease ( melP  or  MAE1 ) from  Schizosaccharomyces pombe ,  Lactococcus lactis ,  Oenococcus oeni , and  Lactobacillus plantarum  were heterologously expressed. For further inquiry, the effect of L-malic acid metabolism on the flavor balance in wine, the related flavor substances, higher alcohols, and esters production, were detected. Of all the recombinants, the strains WYm1S N  with coexpression of malate permease gene  MAE1  from  S. pombe  and malolactic enzyme gene  mleS  from  L. lactis  and WYm1m2 with coexpression of gene  MAE1  and malate permease gene  MAE2  from  S. pombe  could reduce the L-malic acid contents to about 1 g/L, and in which the mutant WYm1S N  exhibited the best effect on the flavor quality improvement.","doi":"10.3390/foods13132038","authors":"Li P, Song W, Wang Y, Li X, Wu S, Li B, Zhang C","authors_abbrev":"Li P et al.","pubmed_publication_date":"27 Jun 2024","pubmed_entrez_date":"2024-07-13","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-07-13 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20946944","title":"A novel combined approach to detect androgenic activities with yeast based assays in Schizosaccharomyces pombe and Saccharomyces cerevisiae.","citation":"Toxicol Lett 2010 Dec 15;199(3):410-5","abstract":"We describe the construction and validation of novel test systems for detecting androgenic activities using a combination of the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. By applying the reporter enhanced Green Fluorescent Protein (EGFP) the incubation time could be reduced to only 24h if compared to the classical β-galactosidase reporter (48 h). Both yeast systems were validated by analyzing the effects of seven androgens as well as five anti-androgens. One androgen (stanozolol) could be detected ten times more sensitive in S. cerevisiae than in S. pombe. Three of the five anti-androgenic substances showed no or only a slight effect in both yeast assays. The other two anti-androgens could be detected much better in S. pombe. Additionally, we could show that both yeast assays tolerated 10% urine within the media and still were capable to detect dihydrotestosterone at a concentration of 10(-8)M suggesting the use of the assays for applied doping pre-screening. In summary, the novel androgen-sensitive yeast assays have a large potential for various applications, e.g. as pre-screening in doping analysis or cattle feeding. A combination of both assays, exploiting these two phylogenetic very different yeasts, allows detection of the activity of a wide range of androgenic substances.","doi":"10.1016/j.toxlet.2010.10.007","authors":"Wolf S, Rataj F, Zierau O, Ostermann K, Diel P, Parr MK, Vollmer G, Rödel G","authors_abbrev":"Wolf S et al.","pubmed_publication_date":"15 Dec 2010","pubmed_entrez_date":"2010-10-16","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25392422","title":"tRFdb: a database for transfer RNA fragments.","citation":"Nucleic Acids Res 2015 Jan;43(Database issue):D141-5","abstract":"We have created tRFdb, the first database of transfer RNA fragments (tRFs), available at http://genome.bioch.virginia.edu/trfdb/. With over 100 small RNA libraries analyzed, the database currently contains the sequences and read counts of the three classes of tRFs for eight species: R. sphaeroides, S. pombe, D. melanogaster, C. elegans, Xenopus, zebra fish, mouse and human, for a total of 12,877 tRFs. The database can be searched by tRF ID or tRF sequence, and the results can be limited by organism. The search results show the genome coordinates and names of the tRNAs the sequence may derive from, and there are links for the sequence of the tRF and parental tRNA, and links for the read counts in all the corresponding small RNA libraries. As a case study for how this database may be used, we have shown that a certain class of tRFs, tRF-1s, is highly upregulated in B-cell malignancies.","doi":"10.1093/nar/gku1138","authors":"Kumar P, Mudunuri SB, Anaya J, Dutta A","authors_abbrev":"Kumar P et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-11-14","publication_year":"2015","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2014-11-15 01:16:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24467403","title":"The yeast actin cytoskeleton.","citation":"FEMS Microbiol Rev 2014 Mar;38(2):213-27","abstract":"The actin cytoskeleton is a complex network of dynamic polymers, which plays an important role in various fundamental cellular processes, including maintenance of cell shape, polarity, cell division, cell migration, endocytosis, vesicular trafficking, and mechanosensation. Precise spatiotemporal assembly and disassembly of actin structures is regulated by the coordinated activity of about 100 highly conserved accessory proteins, which nucleate, elongate, cross-link, and sever actin filaments. Both in vivo studies in a wide range of organisms from yeast to metazoans and in vitro studies of purified proteins have helped shape the current understanding of actin dynamics and function. Molecular genetics, genome-wide functional analysis, sophisticated real-time imaging, and ultrastructural studies in concert with biochemical analysis have made yeast an attractive model to understand the actin cytoskeleton, its molecular dynamics, and physiological function. Studies of the yeast actin cytoskeleton have contributed substantially in defining the universal mechanism regulating actin assembly and disassembly in eukaryotes. Here, we review some of the important insights generated by the study of actin cytoskeleton in two important yeast models the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe.","doi":"10.1111/1574-6976.12064","authors":"Mishra M, Huang J, Balasubramanian MK","authors_abbrev":"Mishra M et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-01-29","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16096639","title":"Taz1, Rap1 and Rif1 act both interdependently and independently to maintain telomeres.","citation":"EMBO J 2005 Sep 07;24(17):3128-35","abstract":"Telomere protection and maintenance are accomplished through the coordinated actions of telomere-specific DNA binding proteins and their interacting partners. The fission yeast ortholog of human TRF1/2, Taz1, binds telomeric DNA and regulates numerous aspects of telomere function. Here, we ask which aspects of Taz1 function are mediated through its interacting proteins, Rap1 and Rif1. We demonstrate that rap1+ deletion phenocopies some, but not all, aspects of taz1Delta telomere dysfunction, while Rif1 exhibits a very different functional spectrum. Rap1 acts in a Taz1-dependent pathway to prevent chromosome end fusions and regulate telomeric 3' overhang formation, while Rif1 is dispensable for these functions. Telomerase inhibition by Taz1 is mediated by two separate pathways, one involving Rap1 and the other involving Rif1. In contrast, Taz1 is uniquely required to prevent chromosomal entanglements and missegregation at cold temperatures. Strikingly, while rap1+ deletion exacerbates the cold sensitivity of taz1Delta cells, rif1+ deletion restores full viability. Thus, Rap1 and Rif1 are each required for a subset of the functions of Taz1, but each acquires Taz1-independent functions in its absence. Furthermore, Taz1 can function independently of its known binding partners.","authors":"Miller KM, Ferreira MG, Cooper JP","authors_abbrev":"Miller KM et al.","pubmed_publication_date":"07 Sep 2005","pubmed_entrez_date":"2005-08-13","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.17","SPBC1A4.03c","SPBC1778.02","SPAC16A10.07c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:12207036","title":"The fission yeast RPA21 subunit of RNA polymerase I: an evolutionarily conserved subunit interacting with ribosomal DNA (rDNA) transcription factor Rrn3p for recruitment to rDNA promoter.","citation":"Genes Genet Syst 2002 Jun;77(3):147-57","abstract":"Recruitment of RNA polymerases to the cognate promoter is a key step for the transcription initiation of specific genes in eukaryotes. Recently, RNA polymerase I (pol I) of Saccharomyces cerevisiae was shown to be recruited to the rDNA promoter via interaction between Rrn3p, a conserved transcription factor for rDNA, and A43, a subunit specific to pol I. The question of whether a similar interaction for pol I recruitment is conserved in other eukaryotes remains to be answered. We show here that Schizosaccharomyces pombe rpa21(+) encodes a protein of apparent molecular mass 21 kD which shows 36% identity to the A43 subunit of pol I in S. cerevisiae, and that rpa21(+) is essential for cell growth. To gain further insight into the functions of RPA21, we isolated a total of 22 temperature-sensitive (ts) mutants of rpa21(+) and found that most of the substitutions causing the ts phenotype are clustered in the N-terminal half of RPA21. The ts mutants showed a markedly reduced amount of primary transcripts of rDNA immediately after temperature shift-up. Over-expression of S. pombe rrn3(+) in the ts mutants suppressed the growth defect in an allele-specific manner. Therefore, we conclude that S. pombe RPA21 plays a functional role similar to that of A43 in S. cerevisiae and that the mechanism of recruitment of pol I to the rDNA promoter by the interaction of a specific pol I subunit with Rrn3p is evolutionarily conserved.","authors":"Imazawa Y, Hisatake K, Nakagawa K, Muramatsu M, Nogi Y","authors_abbrev":"Imazawa Y et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-09-11","publication_year":"2002","canto_session_key":"b9099784b5cb5119","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-07 21:43:17","canto_approved_date":"2023-01-19 15:34:26","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2018-05-29 17:00:17","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.07c","SPAC18G6.11c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-07"},{"uniquename":"PMID:20736315","title":"Specific replication origins promote DNA amplification in fission yeast.","citation":"J Cell Sci 2010 Sep 15;123(Pt 18):3047-51","abstract":"To ensure equal replication of the genome in every eukaryotic cell cycle, replication origins fire only once each S phase and do not fire after passive replication. Failure in these controls can lead to local amplification, contributing to genome instability and the development of cancer. To identify features of replication origins important for such amplification, we have investigated origin firing and local genome amplification in the presence of excess helicase loaders Cdc18 and Cdt1 in fission yeast. We find that S phase controls are attenuated and coordination of origin firing is lost, resulting in local amplification. Specific origins are necessary for amplification but act only within a permissive chromosomal context. Origins associated with amplification are highly AT-rich, fire efficiently and early during mitotic S phase, and are located in large intergenic regions. We propose that these features predispose replication origins to re-fire within a single S phase, or to remain active after passive replication.","doi":"10.1242/jcs.067470","authors":"Kiang L, Heichinger C, Watt S, Bähler J, Nurse P","authors_abbrev":"Kiang L et al.","pubmed_publication_date":"15 Sep 2010","pubmed_entrez_date":"2010-08-26","publication_year":"2010","canto_session_key":"28cd0018d09ab78f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-06-28 21:36:53","canto_approved_date":"2022-07-26 16:44:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-06 15:24:57","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jacky Hayles","community_curator":true,"annotation_count":1,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.18","SPAP14E8.02","SPBC14C8.07c","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2018-06-28"},{"uniquename":"PMID:38692277","title":"A dynamin superfamily-like pseudoenzyme coordinates with MICOS to promote cristae architecture.","citation":"Curr Biol 2024 Apr 24;","abstract":"Mitochondrial cristae architecture is crucial for optimal respiratory function of the organelle. Cristae shape is maintained in part by the mitochondrial contact site and cristae organizing system (MICOS) complex. While MICOS is required for normal cristae morphology, the precise mechanistic role of each of the seven human MICOS subunits, and how the complex coordinates with other cristae-shaping factors, has not been fully determined. Here, we examine the MICOS complex in Schizosaccharomyces pombe, a minimal model whose genome only encodes for four core subunits. Using an unbiased proteomics approach, we identify a poorly characterized inner mitochondrial membrane protein that interacts with MICOS and is required to maintain cristae morphology, which we name Mmc1. We demonstrate that Mmc1 works in concert with MICOS to promote normal mitochondrial morphology and respiratory function. Mmc1 is a distant relative of the dynamin superfamily of proteins (DSPs), GTPases, which are well established to shape and remodel membranes. Similar to DSPs, Mmc1 self-associates and forms high-molecular-weight assemblies. Interestingly, however, Mmc1 is a pseudoenzyme that lacks key residues required for GTP binding and hydrolysis, suggesting that it does not dynamically remodel membranes. These data are consistent with the model that Mmc1 stabilizes cristae architecture by acting as a scaffold to support cristae ultrastructure on the matrix side of the inner membrane. Our study reveals a new class of proteins that evolved early in fungal phylogeny and is required for the maintenance of cristae architecture. This highlights the possibility that functionally analogous proteins work with MICOS to establish cristae morphology in metazoans.","doi":"10.1016/j.cub.2024.04.028","authors":"Kumar A, Gok MO, Nguyen KN, Connor OM, Reese ML, Wideman JG, Muñoz-Gómez SA, Friedman JR","authors_abbrev":"Kumar A et al.","pubmed_publication_date":"24 Apr 2024","pubmed_entrez_date":"2024-05-01","publication_year":"2024","canto_session_key":"fd0faf273f8c3391","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jonathan Friedman","canto_first_approved_date":"2024-06-27 10:36:10","canto_approved_date":"2025-09-02 17:54:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-26 20:17:39","canto_added_date":"2024-05-02 23:25:05","annotation_curators":[{"name":"Jonathan Friedman","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":38,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1442.05c","SPAC3A11.07","SPBC3E7.05c","SPAC2E1P5.03","SPAC1635.01","SPAC17C9.06","SPAPJ691.03","SPBC25H2.09","SPBC409.19c","SPBC947.15c","SPCC965.04c","SPAC1610.04"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2024-06-27"},{"uniquename":"PMID:10392442","title":"Biotransformation of steroids by the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 1999 Jun 15;15(8):639-45","abstract":"The fungal biotransformation of steroids is of applied interest due to the economic importance of such stereo- and regiospecific reactions and also in the context of ergosterol pathway engineering to produce vitamin D and steroidal products. In Schizosaccharomyces pombe no steroid hydroxylation as is found in filamentous fungi was observed, but a cytosolic NAD(H)/NADP(H)-dependent hydroxysteroid dehydrogenase activity was identified. Progesterone was reduced at the delta 4 double bond (in vivo only) as well as at the C-3 and C-20 keto groups. Testosterone and 4-androstene-3,17-dione were interconverted and 5 alpha-pregnane-3,20-dione and 5 beta-pregnane-3,20-dione were reduced to 3-hydroxy products. The reactions were sometimes reversible and showed regio- and stereo specificity. In S. pombe more than one steroid dehydrogenase homologue is likely to occur, as has been observed in Saccharomyces cerevisiae. Our findings indicate that genes encoding soluble proteins should be examined as candidates for actual steroid dehydrogenase activity.","authors":"Pajic T, Vitas M, Zigon D, Pavko A, Kelly SL, Komel R","authors_abbrev":"Pajic T et al.","pubmed_publication_date":"15 Jun 1999","pubmed_entrez_date":"1999-07-07","publication_year":"1999","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14731730","title":"Signal transduction during mating and meiosis in S. pombe.","citation":"Trends Cell Biol 1993 Feb;3(2):60-5","abstract":"When starved, the fission yeast Schizosaccharomyces pombe responds by producing mating factors or pheromones that signal to cells of the opposite sex to initiate mating. Like its distant relative Saccharomyces cerevisiae, cells of the two mating types of S. pombe each produce a distinct pheromone that binds to receptors on the opposite cell type to induce the morphological changes required for mating. While the pathways are basically very similar in the two yeasts, pheromone signalling in S. pombe differs in several important ways from that of the more familiar budding yeast. In this article, Olaf Nielsen describes the pheromones and their effects in S. pombe, and compares the signalling pathways of the two yeasts.","authors":"Nielsen O","authors_abbrev":"Nielsen O","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19363124","title":"Novel nucleotide sequence motifs that produce hotspots of meiotic recombination in Schizosaccharomyces pombe.","citation":"Genetics 2009 Jun;182(2):459-69","abstract":"In many organisms, including yeasts and humans, meiotic recombination is initiated preferentially at a limited number of sites in the genome referred to as recombination hotspots. Predicting precisely the location of most hotspots has remained elusive. In this study, we tested the hypothesis that hotspots can result from multiple different sequence motifs. We devised a method to rapidly screen many short random oligonucleotide sequences for hotspot activity in the fission yeast Schizosaccharomyces pombe and produced a library of approximately 500 unique 15- and 30-bp sequences containing hotspots. The frequency of hotspots found suggests that there may be a relatively large number of different sequence motifs that produce hotspots. Within our sequence library, we found many shorter 6- to 10-bp motifs that occurred multiple times, many of which produced hotspots when reconstructed in vivo. On the basis of sequence similarity, we were able to group those hotspots into five different sequence families. At least one of the novel hotspots we found appears to be a target for a transcription factor, as it requires that factor for its hotspot activity. We propose that many hotspots in S. pombe, and perhaps other organisms, result from simple sequence motifs, some of which are identified here.","doi":"10.1534/genetics.109.101253","authors":"Steiner WW, Steiner EM, Girvin AR, Plewik LE","authors_abbrev":"Steiner WW et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-04-14","publication_year":"2009","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9649519","title":"Isolation and characterization of new fission yeast cytokinesis mutants.","citation":"Genetics 1998 Jul;149(3):1265-75","abstract":"Schizosaccharomyces pombe is an excellent organism in which to study cytokinesis as it divides by medial fission using an F-actin contractile ring. To enhance our understanding of the cell division process, a large genetic screen was carried out in which 17 genetic loci essential for cytokinesis were identified, 5 of which are novel. Mutants identifying three genes, rng3(+), rng4(+), and rng5(+), were defective in organizing an actin contractile ring. Four mutants defective in septum deposition, septum initiation defective (sid)1, sid2, sid3, and sid4, were also identified and characterized. Genetic analyses revealed that the sid mutants display strong negative interactions with the previously described septation mutants cdc7-24, cdc11-123, and cdc14-118. The rng5(+), sid2(+), and sid3(+) genes were cloned and shown to encode Myo2p (a myosin heavy chain), a protein kinase related to budding yeast Dbf2p, and Spg1p, a GTP binding protein that is a member of the ras superfamily of GTPases, respectively. The ability of Spg1p to promote septum formation from any point in the cell cycle depends on the activity of Sid4p. In addition, we have characterized a phenotype that has not been described previously in cytokinesis mutants, namely the failure to reorganize actin patches to the medial region of the cell in preparation for septum formation.","authors":"Balasubramanian MK, McCollum D, Chang L, Wong KC, Naqvi NI, He X, Sazer S, Gould KL","authors_abbrev":"Balasubramanian MK et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-07-03","publication_year":"1998","canto_session_key":"8eefc547e75398d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-05-28 16:16:46","canto_approved_date":"2026-01-31 11:43:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-19 16:38:18","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":211,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_9649519_phaf.tsv"}],"genes":["SPCC645.05c","SPAC1565.06c","SPCC4B3.15","SPAC4A8.15c","SPAC1F5.04c","SPAP8A3.08","SPAC24B11.11c","SPBC21.06c","SPAC20G8.05c","SPAC27F1.02c","SPCC613.04c","SPBC24C6.07","SPBC244.01c","SPCC1739.11c","SPAC4F8.13c","SPAC9G1.09"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2017-05-28"},{"uniquename":"EMBL:U59386","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21098122","title":"Mre11 nuclease activity and Ctp1 regulate Chk1 activation by Rad3ATR and Tel1ATM checkpoint kinases at double-strand breaks.","citation":"Mol Cell Biol 2011 Feb;31(3):573-83","abstract":"Rad3, the Schizosaccharomyces pombe ortholog of human ATR and Saccharomyces cerevisiae Mec1, activates the checkpoint kinase Chk1 in response to DNA double-strand breaks (DSBs). Rad3(ATR/Mec1) associates with replication protein A (RPA), which binds single-stranded DNA overhangs formed by DSB resection. In humans and both yeasts, DSBs are initially detected and processed by the Mre11-Rad50-Nbs1(Xrs2) (MRN) nucleolytic protein complex in association with the Tel1(ATM) checkpoint kinase and the Ctp1(CtIP/Sae2) DNA-end processing factor; however, in budding yeast, neither Mre11 nuclease activity or Sae2 are required for Mec1 signaling at irreparable DSBs. Here, we investigate the relationship between DNA end processing and the DSB checkpoint response in fission yeast, and we report that Mre11 nuclease activity and Ctp1 are critical for efficient Rad3-to-Chk1 signaling. Moreover, deleting Ctp1 reveals a Tel1-to-Chk1 signaling pathway that bypasses Rad3. This pathway requires Mre11 nuclease activity, the Rad9-Hus1-Rad1 (9-1-1) checkpoint clamp complex, and Crb2 checkpoint mediator. Ctp1 negatively regulates this pathway by controlling MRN residency at DSBs. A Tel1-to-Chk1 checkpoint pathway acting at unresected DSBs provides a mechanism for coupling Chk1 activation to the initial detection of DSBs and suggests that ATM may activate Chk1 by both direct and indirect mechanisms in mammalian cells.","doi":"10.1128/MCB.00994-10","authors":"Limbo O, Porter-Goff ME, Rhind N, Russell P","authors_abbrev":"Limbo O et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2010-11-25","publication_year":"2011","canto_session_key":"2ef9911b1699da5e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2017-03-27 11:33:15","canto_approved_date":"2025-09-04 09:58:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-05 18:05:26","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":74,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPCC338.08","SPBC216.05","SPAC19G12.06c","SPAC13C5.07","SPCC622.08c","SPAC20G4.04c","SPCC23B6.03c","SPBC342.05","SPCC18B5.11c","SPBC6B1.09c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2017-03-27"},{"uniquename":"PMID:30824696","title":"Systematic analysis reveals the prevalence and principles of bypassable gene essentiality.","citation":"Nat Commun 2019 Mar 01;10(1):1002","abstract":"Gene essentiality is a variable phenotypic trait, but to what extent and how essential genes can become dispensable for viability remain unclear. Here, we investigate 'bypass of essentiality (BOE)' - an underexplored type of digenic genetic interaction that renders essential genes dispensable. Through analyzing essential genes on one of the six chromosome arms of the fission yeast Schizosaccharomyces pombe, we find that, remarkably, as many as 27% of them can be converted to non-essential genes by BOE interactions. Using this dataset we identify three principles of essentiality bypass: bypassable essential genes tend to have lower importance, tend to exhibit differential essentiality between species, and tend to act with other bypassable genes. In addition, we delineate mechanisms underlying bypassable essentiality, including the previously unappreciated mechanism of dormant redundancy between paralogs. The new insights gained on bypassable essentiality deepen our understanding of genotype-phenotype relationships and will facilitate drug development related to essential genes.","doi":"10.1038/s41467-019-08928-1","authors":"Li J, Wang HT, Wang WT, Zhang XR, Suo F, Ren JY, Bi Y, Xue YX, Hu W, Dong MQ, Du LL","authors_abbrev":"Li J et al.","pubmed_publication_date":"01 Mar 2019","pubmed_entrez_date":"2019-03-03","publication_year":"2019","canto_session_key":"2553189bcbacd3f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-03-07 10:46:02","canto_approved_date":"2019-03-07 10:46:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-03-07 10:45:40","canto_added_date":"2019-03-04 01:15:04","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":391,"orcid":"0000-0003-4148-4606","file_type":"interaction","file_name":"PMID_30824696_interactions.tab2.txt"}],"genes":["SPAC2G11.12","SPCC24B10.08c","SPCC330.01c","SPAC6F12.11c","SPAC644.07","SPBC19F5.03","SPCC550.14","SPBC947.02","SPBC28F2.06c","SPBC29A10.05","SPBC577.07","SPBC409.12c","SPAC9E9.10c","SPAC1A6.03c","SPBC25B2.08","SPBC3D6.11c","SPBC1604.02c","SPAC23H4.12","SPBC26H8.10","SPAC2F7.07c","SPAC29B12.08","SPBC337.15c","SPBC1703.14c","SPAC4H3.05","SPBC18H10.06c","SPCC16A11.13","SPBC83.07","SPBC27B12.08","SPBP19A11.03c","SPAC6B12.18","SPBC1271.13","SPAC3F10.18c","SPBC16C6.03c","SPAC24B11.06c","SPBC651.12c","SPAC3G6.01","SPCC4B3.17","SPAC23C11.15","SPCC553.01c","SPBC902.04","SPBC8D2.07c","SPBC582.09","SPBC428.01c","SPCC613.11c","SPBC713.02c","SPAP8A3.14c","SPAC25B8.02","SPCC1450.02","SPAC1805.04","SPBC409.03","SPCC1259.07","SPBC16G5.01","SPAC12G12.03","SPAC17A5.07c","SPBP35G2.02","SPBC839.05c","SPBC1773.11c","SPCC1672.06c","SPBC23E6.02","SPBC354.03","SPBC21C3.20c","SPBC336.01","SPAC17A2.14","SPCC18B5.11c","SPAC19G12.17","SPBC15D4.14","SPAC3C7.03c","SPBC19C7.03","SPBC2F12.11c","SPCC74.02c","SPCC338.17c","SPAC20G8.03","SPCC16C4.14c","SPBC16A3.09c","SPBC11B10.07c","SPBC16E9.12c","SPBC409.14c","SPBC651.11c","SPAC23G3.01","SPCC18.04","SPBC4F6.04","SPBC1709.07","SPBC4F6.07c","SPBC1198.04c","SPCC1020.01c","SPCC126.04c","SPBC336.12c","SPAC3H1.04c","SPBC3D6.07","SPBC32H8.10","SPAC9E9.09c","SPCC736.12c","SPAC26H5.07c","SPAC589.08c","SPBC1289.06c","SPBC16A3.07c","SPCC1840.02c","SPCC74.03c","SPAC1D4.14","SPAC18G6.13","SPAC1556.08c","SPBC839.08c","SPAC664.07c","SPAC20H4.07","SPBC11B10.06","SPBC1198.10c","SPBC2D10.06","SPBC21B10.13c","SPCC74.01","SPAP27G11.14c","SPBC428.16c","SPAC30D11.04c","SPAC57A10.08c","SPAC22F8.08","SPBC2G5.06c","SPCC830.11c","SPBC1711.05","SPAC8C9.06c","SPBC17A3.07","SPBC337.06c","SPAC1486.05","SPBC660.15","SPCC188.13c","SPBC216.07c","SPAC26H5.05","SPBC11B10.04c","SPBC725.16","SPAC630.14c","SPBC13E7.03c","SPAC1952.05","SPAC19A8.10","SPBC106.10","SPAC3G9.08","SPBC27B12.01c","SPCC1450.16c","SPAC343.18","SPBC1604.08c","SPBC409.15","SPAC23C4.19","SPAC1B3.05","SPCP1E11.06","SPBC12C2.10c","SPBC106.18","SPAC227.08c","SPACUNK4.16c","SPAC17H9.03c","SPBC337.12","SPBC354.14c","SPBC1734.13","SPBC16C6.02c","SPAC15A10.11","SPBC27B12.12c","SPBC1921.03c","SPBC28F2.10c","SPAC17H9.04c","SPBC365.06","SPCC594.05c","SPAC23H3.05c","SPBC17D1.05","SPBC839.09c","SPBC947.14c","SPBC36.05c","SPBC1921.07c","SPAC144.02","SPBC16A3.18","SPBC365.02c","SPBC19G7.16","SPBC32H8.08c","SPAC1006.03c","SPBC83.06c","SPBC29A3.18","SPBC1706.03","SPCC306.04c","SPBC800.13","SPBC16G5.15c","SPAC17H9.02","SPAC644.14c","SPCC1020.02","SPBC3F6.02c","SPAPB1E7.12","SPBC119.18","SPBC725.08","SPAC29A4.13","SPCC24B10.19c","SPCC4B3.04c","SPCC576.10c","SPBC83.15","SPBC651.03c","SPAC1039.05c","SPAC1687.05","SPBC8D2.15","SPBC16H5.03c","SPCP31B10.05","SPAC22F3.09c","SPBC23G7.12c","SPCC757.09c","SPBC215.01","SPAC4F8.12c","SPBC1703.09","SPBC530.12c","SPBP8B7.23","SPBP19A11.06","SPCC1919.03c","SPSNORNA.52","SPCC18.17c","SPBC800.02","SPBC30D10.04","SPCC736.08","SPAC1A6.06c","SPBC25B2.06c","SPAC23H3.10","SPBC3E7.15c","SPAC4F10.19c","SPBC1306.01c","SPAC22G7.03","SPBC1289.03c","SPCC4G3.15c","SPAC14C4.06c","SPBC14C8.07c","SPAC19A8.13","SPBC28F2.07","SPBC11B10.03","SPBC887.15c","SPBC1734.16c","SPAC13A11.04c","SPBC19C2.11c","SPAC9.05","SPBC19G7.09","SPAC4D7.03","SPBC1685.11"],"gene_count":230,"ltp_gene_count":7,"approved_date":"2019-03-07"},{"uniquename":"PMID:34086083","title":"Expression of Mug14 is regulated by the transcription factor Rst2 through the cAMP-dependent protein kinase pathway in Schizosaccharomyces pombe.","citation":"Curr Genet 2021 Oct;67(5):807-821","abstract":"The cAMP-dependent protein kinase (Pka1) regulates many cellular events, including sexual development and glycogenesis, and response to the limitation of glucose, in Schizosaccharomyces pombe. Despite its importance in many cellular events, the targets of the cAMP/PKA pathway have not been fully investigated. Here, we demonstrate that the expression of mug14 is induced by downregulation of the cAMP/PKA pathway and limitation of glucose. This regulation is dependent on the function of Rst2, a transcription factor that regulates transition from mitosis to meiosis. The loss of the C2H2-type zinc finger domain in Rst2, termed Rst2 (C2H2∆), abolished the induction of Mug14 expression. Upon deletion of the stress starvation response element of the S. pombe (STREP: CCCCTC) sequence, which is a potential binding site of Rst2 on mug14, in the pka1∆ strain, its induction was abolished. The expression of Mug14 was significantly reduced and delayed by the limitation of glucose and also by nitrogen starvation in the rst2∆ strain. Mug14 is known to share a common function with Mde1 and Mta3 in the methionine salvage pathway, but the expression of mde1 and mta3 mRNAs was not enhanced by pka1 deletion and limitation of glucose. We conclude that the expression of Mug14 is upregulated by Rst2 under the control of the cAMP/PKA signaling pathway, which senses the limitation of glucose.","doi":"10.1007/s00294-021-01194-z","authors":"Inamura SI, Tanabe T, Kawamukai M, Matsuo Y","authors_abbrev":"Inamura SI et al.","pubmed_publication_date":"Oct 2021","pubmed_entrez_date":"2021-06-04","publication_year":"2021","canto_session_key":"ebc037f099adf95b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Matsuo","canto_first_approved_date":"2021-06-24 14:02:44","canto_approved_date":"2024-03-20 14:40:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-17 03:35:02","canto_added_date":"2021-06-06 00:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yasuhiro Matsuo","community_curator":true,"annotation_count":54,"orcid":"0000-0002-2858-7179","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16E9.01c","SPBC106.10","SPBC359.06","SPAC20H4.05c","SPBC32C12.02","SPAC9.06c","SPAC6F12.02"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2021-06-24"},{"uniquename":"PMID:32483293","title":"Lem2 and Lnp1 maintain the membrane boundary between the nuclear envelope and endoplasmic reticulum.","citation":"Commun Biol 2020 Jun 01;3(1):276","abstract":"The nuclear envelope (NE) continues to the endoplasmic reticulum (ER). Proper partitioning of NE and ER is crucial for cellular activity, but the key factors maintaining the boundary between NE and ER remain to be elucidated. Here we show that the conserved membrane proteins Lem2 and Lnp1 cooperatively play a crucial role in maintaining the NE-ER membrane boundary in fission yeast Schizosaccharomyces pombe. Cells lacking both Lem2 and Lnp1 caused severe growth defects associated with aberrant expansion of the NE/ER membranes, abnormal leakage of nuclear proteins, and abnormal formation of vacuolar-like structures in the nucleus. Overexpression of the ER membrane protein Apq12 rescued the growth defect associated with membrane disorder caused by the loss of Lem2 and Lnp1. Genetic analysis showed that Apq12 had overlapping functions with Lnp1. We propose that a membrane protein network with Lem2 and Lnp1 acts as a critical factor to maintain the NE-ER boundary.","doi":"10.1038/s42003-020-0999-9","authors":"Hirano Y, Kinugasa Y, Osakada H, Shindo T, Kubota Y, Shibata S, Haraguchi T, Hiraoka Y","authors_abbrev":"Hirano Y et al.","pubmed_publication_date":"01 Jun 2020","pubmed_entrez_date":"2020-06-03","publication_year":"2020","canto_session_key":"883b8d9455a4c2ff","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-06-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15020053","title":"Multiple pathways for telomere tethering: functional implications of subnuclear position for heterochromatin formation.","citation":"Biochim Biophys Acta 2004 Mar 15;1677(1-3):120-8","abstract":"Technical advances in the imaging of GFP derivatives in living cells have improved our ability to determine the position and dynamics of specific chromatin loci. This approach, combined with genetics and functional assays, has shed new light on how nuclear compartments facilitate gene repression in yeast.","authors":"Taddei A, Gasser SM","authors_abbrev":"Taddei A et al.","pubmed_publication_date":"15 Mar 2004","pubmed_entrez_date":"2004-03-17","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084875","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.53"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19761608","title":"Phase Coupled Meta-analysis: sensitive detection of oscillations in cell cycle gene expression, as applied to fission yeast.","citation":"BMC Genomics 2009 Sep 17;10:440","abstract":"Many genes oscillate in their level of expression through the cell division cycle. Previous studies have identified such genes by applying Fourier analysis to cell cycle time course experiments. Typically, such analyses generate p-values; i.e., an oscillating gene has a small p-value, and the observed oscillation is unlikely due to chance. When multiple time course experiments are integrated, p-values from the individual experiments are combined using classical meta-analysis techniques. However, this approach sacrifices information inherent in the individual experiments, because the hypothesis that a gene is regulated according to the time in the cell cycle makes two independent predictions: first, that an oscillation in expression will be observed; and second, that gene expression will always peak in the same phase of the cell cycle, such as S-phase. Approaches that simply combine p-values ignore the second prediction.\nHere, we improve the detection of cell cycle oscillating genes by systematically taking into account the phase of peak gene expression. We design a novel meta-analysis measure based on vector addition: when a gene peaks or troughs in all experiments in the same phase of the cell cycle, the representative vectors add to produce a large final vector. Conversely, when the peaks in different experiments are in various phases of the cycle, vector addition produces a small final vector. We apply the measure to ten genome-wide cell cycle time course experiments from the fission yeast Schizosaccharomyces pombe, and detect many new, weakly oscillating genes.\nA very large fraction of all genes in S. pombe, perhaps one-quarter to one-half, show some cell cycle oscillation, although in many cases these oscillations may be incidental rather than adaptive.","doi":"10.1186/1471-2164-10-440","authors":"Pyne S, Gutman R, Kim CS, Futcher B","authors_abbrev":"Pyne S et al.","pubmed_publication_date":"17 Sep 2009","pubmed_entrez_date":"2009-09-19","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21409593","title":"Regulation and role of an RNA-binding protein Msa2 in controlling the sexual differentiation of fission yeast.","citation":"Curr Genet 2011 Jun;57(3):191-200","abstract":"The msa2/nrd1 gene encodes an RNA-binding protein that negatively regulates sexual differentiation of fission yeast Schizosaccharomyces pombe by repressing the Ste11-regulated genes. However, it is not known how Msa2 regulates sexual differentiation, and to characterize its role, we altered the msa2 gene by inducing point mutations and tested the resulting mutants for their ability to inhibit sexual differentiation and their suppressive effect on a temperature sensitive pat1 mutant. Several amino acids were found to be important, including three phenylalanine residues (F153, F245 and F453) in the three consensus RNA recognition motifs (RRMs) and a threonine residue (T126) that normally functions as a phosphorylation site. Results indicated that Msa2 was negatively regulated by phosphorylation that arose from Spk1-mediated pheromone signaling. Msa2 also regulated the Ste11 protein level coordinating with Cpc2, a ribosomal-associated protein. In addition, Msa2 was detected in stress granules that co-localized with Pabp in the cytosol under conditions of glucose starvation. Msa2 may regulate the translation of Ste11, be a component of stress granules that form in response to glucose starvation, and regulate the sexual differentiation of S. pombe.","doi":"10.1007/s00294-011-0335-5","authors":"Oowatari Y, Jeong H, Tanae K, Nakagawa T, Kawamukai M","authors_abbrev":"Oowatari Y et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-03-17","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F7.11","SPBC19C2.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:20453833","title":"Rad8Rad5/Mms2-Ubc13 ubiquitin ligase complex controls translesion synthesis in fission yeast.","citation":"EMBO J 2010 Jun 16;29(12):2048-58","abstract":"Many DNA lesions cause pausing of replication forks at lesion sites; thus, generating gaps in the daughter strands that are filled-in by post-replication repair (PRR) pathways. In Saccharomyces cerevisiae, PRR involves translesion synthesis (TLS) mediated by Poleta or Polzeta, or Rad5-dependent gap filling through a poorly characterized error-free mechanism. We have developed an assay to monitor error-free and mutagenic TLS across single DNA lesions in Schizosaccharomyces pombe. For both main UV photolesions, we have delineated a major error-free pathway mediated by a distinct combination of TLS polymerases. Surprisingly, these TLS pathways require enzymes needed for poly-ubiquitination of proliferating cell nuclear antigen (PCNA) as well as those required for mono-ubiquitination. For pathways that require several TLS polymerases the poly-ubiquitin chains of PCNA may facilitate their recruitment through specific interactions with their multiple ubiquitin-binding motifs. These error-free TLS pathways may at least partially account for the previously described poly-ubiquitination-dependent error-free branch of PRR. This work highlights major differences in the control of lesion tolerance pathways between S. pombe and S. cerevisiae despite the homologous sets of PRR genes these organisms share.","doi":"10.1038/emboj.2010.87","authors":"Coulon S, Ramasubramanyan S, Alies C, Philippin G, Lehmann A, Fuchs RP","authors_abbrev":"Coulon S et al.","pubmed_publication_date":"16 Jun 2010","pubmed_entrez_date":"2010-05-11","publication_year":"2010","canto_session_key":"a309fa2c0e0a8d62","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-05-12 07:21:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-03-31 16:46:53","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":53,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC553.07c","SPBC1347.01c","SPBC16A3.11","SPBC1734.06","SPAC11E3.04c","SPCC338.05c","SPBC16D10.09","SPAC688.10","SPAC2F7.06c","SPAC13G6.01c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2016-03-31"},{"uniquename":"PMID:24551125","title":"Cell-cycle analyses using thymidine analogues in fission yeast.","citation":"PLoS One 2014;9(2):e88629","abstract":"Thymidine analogues are powerful tools when studying DNA synthesis including DNA replication, repair and recombination. However, these analogues have been reported to have severe effects on cell-cycle progression and growth, the very processes being investigated in most of these studies. Here, we have analyzed the effects of 5-ethynyl-2'-deoxyuridine (EdU) and 5-Chloro-2'-deoxyuridine (CldU) using fission yeast cells and optimized the labelling procedure. We find that both analogues affect the cell cycle, but that the effects can be mitigated by using the appropriate analogue, short pulses of labelling and low concentrations. In addition, we report sequential labelling of two consecutive S phases using EdU and 5-bromo-2'-deoxyuridine (BrdU). Furthermore, we show that detection of replicative DNA synthesis is much more sensitive than DNA-measurements by flow cytometry.","doi":"10.1371/journal.pone.0088629","authors":"Anda S, Boye E, Grallert B","authors_abbrev":"Anda S et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-20","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10648609","title":"Novel WD-repeat protein Mip1p facilitates function of the meiotic regulator Mei2p in fission yeast.","citation":"Mol Cell Biol 2000 Feb;20(4):1234-42","abstract":"In fission yeast, the onset of meiosis is triggered by activation of the RNA-binding protein Mei2p. We screened for a high-copy-number suppressor of the ectopic meiosis induced by expression of an active form of Mei2p. Consequently we isolated a truncated form of a novel gene, named mip1, from a fission yeast genomic library. The mip1 gene encoded a protein of 1,313 amino acids which carried a WD-repeat motif in the C-terminal region and was apparently conserved among eukaryotes. Mip1p was cytoplasmic, and two-hybrid and immunoprecipitation analyses demonstrated that Mip1p was bound to Mei2p in vivo. Genetic evidence indicated that wild-type Mip1p was required for the function of Mei2p to induce meiosis and that the truncated form of it (Mip1-15p) dominantly interfered with Mei2p. Mip1p appeared to be involved also in conjugation, associating with Ste11p, which is a key transcription factor for sexual development. Furthermore, Mip1p was essential for cell growth, to which neither Mei2p nor Ste11p is relevant. These results suggest that Mip1p assists functional expression of a number of proteins required for proliferation and sexual development in fission yeast.","authors":"Shinozaki-Yabana S, Watanabe Y, Yamamoto M","authors_abbrev":"Shinozaki-Yabana S et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-01-29","publication_year":"2000","canto_session_key":"c22385c0fd392e28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-03-30 13:42:50","canto_approved_date":"2019-06-14 08:27:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-30 13:42:44","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMTR.01","SPMTR.02","SPAC27D7.03c","SPAC57A7.11","SPBC32C12.02","SPBC19C2.05"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2015-03-30"},{"uniquename":"PMID:20144990","title":"Fission yeast TORC1 regulates phosphorylation of ribosomal S6 proteins in response to nutrients and its activity is inhibited by rapamycin.","citation":"J Cell Sci 2010 Mar 01;123(Pt 5):777-86","abstract":"Cellular activities are regulated by environmental stimuli through protein phosphorylation. Target of rapamycin (TOR), a serine/threonine kinase, plays pivotal roles in cell proliferation and cell growth in response to nutrient status. In Schizosaccharomyces pombe, TORC1, which contains Tor2, plays crucial roles in nutrient response. Here we find a nitrogen-regulated phosphoprotein, p27, in S. pombe using the phospho-Akt substrate antibody. Response of p27 phosphorylation to nitrogen availability is mediated by TORC1 and the TSC-Rhb1 signaling, but not by TORC2 or other nutrient stress-related pathways. Database and biochemical analyses indicate that p27 is identical to ribosomal protein S6 (Rps6). Ser235 and Ser236 in Rps6 are necessary for Rps6 phosphorylation by TORC1. These Rps6 phosphorylations are dispensable for cell viability. Rps6 phosphorylation by TORC1 also responds to availability of glucose and is inhibited by osmotic and oxidative stresses. Rapamycin inhibits the ability of TORC1 to phosphorylate Rps6, owing to interaction of the rapamycin-FKBP12 complex with the FRB domain in Tor2. Rapamycin also leads to a decrease in cell size in a TORC1-dependent manner. Our findings demonstrate that the nutrient-responsive and rapamycin-sensitive TORC1-S6 signaling exists in S. pombe, and that this pathway plays a role in cell size control.","doi":"10.1242/jcs.060319","authors":"Nakashima A, Sato T, Tamanoi F","authors_abbrev":"Nakashima A et al.","pubmed_publication_date":"01 Mar 2010","pubmed_entrez_date":"2010-02-11","publication_year":"2010","canto_session_key":"12c854f8bde1a0cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-16 15:52:44","canto_approved_date":"2025-09-22 06:27:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-27 14:12:03","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":37,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.03","SPBC12C2.02c","SPAC13G6.07c","SPBC428.16c","SPBC1A4.02c","SPAC3G9.09c","SPAPB1E7.12","SPBC216.07c","SPAC24B11.06c","SPBC839.17c","SPAC630.13c","SPBC30D10.10c"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2018-08-16"},{"uniquename":"PMID:23388053","title":"Transcription-induced chromatin association of RNA surveillance factors mediates facultative heterochromatin formation in fission yeast.","citation":"Genes Cells 2013 Apr;18(4):327-39","abstract":"Facultative heterochromatin is reversibly established and disrupted during differentiation, but its regulation remains mechanistically unclear. Here, we show that two meiotic gene loci in fission yeast, mei4 and ssm4, comprise facultative heterochromatin that is regulated in a developmental stage-dependent manner. This heterochromatin coordinates expression levels by associating with a chromodomain protein Chp1 and an antisilencing factor Epe1. It has been recently shown that an RNA surveillance machinery for eliminating meiotic gene transcripts, which involves a cis-element called the determinant of selective removal (DSR) and transacting factors, Mmi1 and Red1, also participates in heterochromatin formation at the meiotic genes, but the molecular mechanism underlying the process is largely unknown. By dissecting the mei4 gene, we identified a region that promotes DSR-dependent methylation of histone H3 lysine 9 (H3K9). Integration of this mei4 region together with DSR into an unrelated gene results in ectopic H3K9 methylation. Moreover, our results suggest that transcription of these elements induces chromatin association of Mmi1, which, in turn, recruits Red1 interacting with Clr4/Suv39h H3K9 methyltransferase. Mmi1 remains associated in cells lacking Red1, suggesting that the recruitment of Red1 follows the chromatin association of Mmi1. Overall, we provide detailed insights into the facultative heterochromatin regulation in fission yeast.","doi":"10.1111/gtc.12038","authors":"Tashiro S, Asano T, Kanoh J, Ishikawa F","authors_abbrev":"Tashiro S et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2013-02-08","publication_year":"2013","canto_session_key":"d02f07d0bc61a7b7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.16c","SPBC428.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:19563124","title":"Using the DHFR heat-inducible degron for protein inactivation in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2009;521:483-92","abstract":"Inactivating a specific protein in vivo can yield important information about its function. One strategy previously developed in Saccharomyces cerevisiae by the Varshavsky group involves fusing a degron, derived from mouse dihydrofolate reductase, to the N-terminus of the target protein, which thereby confers temperature-sensitive degradation at the restrictive temperature. We describe here the application of this technique in the fission yeast, Schizosaccharomyces pombe.","doi":"10.1007/978-1-60327-815-7_27","authors":"Kearsey SE, Gregan J","authors_abbrev":"Kearsey SE et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26182355","title":"Mitochondrial Tim9 protects Tim10 from degradation by the protease Yme1.","citation":"Biosci Rep 2015 Mar 17;35(3)","abstract":"Translocase of IM (inner membrane; Tim)9 and Tim10 are essential homologue proteins of the mitochondrial intermembrane space (IMS) and form a stable hexameric Tim9-Tim10 complex there. Redox-switch of the four conserved cysteine residues plays a key role during the biogenesis of these proteins and, in turn, the Tim proteins play a vital chaperone-like role during import of mitochondrial membrane proteins. However, the functional mechanism of the small Tim chaperones is far from solved and it is unclear whether the individual proteins play specific roles or the complex functions as a single unit. In the present study, we examined the requirement and role for the individual disulfide bonds of Tim9 on cell viability, complex formation and stability using yeast genetic, biochemical and biophysical methods. Loss of the Tim9 inner disulfide bond led to a temperature-sensitive phenotype and degradation of both Tim9 and Tim10. The growth phenotype could be suppressed by deletion of the mitochondrial i-AAA (ATPases associated with diverse cellular activities) protease Yme1, and this correlates strongly with stabilization of the Tim10 protein regardless of Tim9 levels. Formation of both disulfide bonds is not essential for Tim9 function, but it can facilitate the formation and improve the stability of the hexameric Tim9-Tim10 complex. Furthermore, our results suggest that the primary function of Tim9 is to protect Tim10 from degradation by Yme1 via assembly into the Tim9-Tim10 complex. We propose that Tim10, rather than the hexameric Tim9-Tim10 complex, is the functional form of these proteins.","doi":"10.1042/BSR20150038","authors":"Spiller MP, Guo L, Wang Q, Tran P, Lu H","authors_abbrev":"Spiller MP et al.","pubmed_publication_date":"17 Mar 2015","pubmed_entrez_date":"2015-07-17","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC965.04c","SPAC222.03c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:38523261","title":"MAPK-dependent control of mitotic progression in S. pombe.","citation":"BMC Biol 2024 Mar 25;22(1):71","abstract":"Mitogen-activated protein kinases (MAPKs) preserve cell homeostasis by transducing physicochemical fluctuations of the environment into multiple adaptive responses. These responses involve transcriptional rewiring and the regulation of cell cycle transitions, among others. However, how stress conditions impinge mitotic progression is largely unknown. The mitotic checkpoint is a surveillance mechanism that inhibits mitotic exit in situations of defective chromosome capture, thus preventing the generation of aneuploidies. In this study, we investigate the role of MAPK Pmk1 in the regulation of mitotic exit upon stress.","doi":"10.1186/s12915-024-01865-6","authors":"Iglesias-Romero AB, Soto T, Flor-Parra I, Salas-Pino S, Ruiz-Romero G, Gould KL, Cansado J, Daga RR","authors_abbrev":"Iglesias-Romero AB et al.","pubmed_publication_date":"25 Mar 2024","pubmed_entrez_date":"2024-03-25","publication_year":"2024","canto_session_key":"6f96bb02611c989f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-26 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC119.08","SPAC24B11.06c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:11450987","title":"Signalling apoptosis: a radical approach.","citation":"Redox Rep 2001;6(2):77-90","abstract":"Reactive oxygen species (ROS) are frequently associated with cytotoxicity, often being described as damaging, harmful or toxic. It is generally assumed that, under pathological circumstances, ROS elicit wide-spread and random acts of oxidation. This passive attack of cellular components by ROS, in conditions where oxidative stress is the initiating stimulus for apoptosis, is assumed to simply trigger cell death as a result of cumulative oxidative damage. However, accumulating evidence now suggests that ROS may act as signalling molecules for the initiation and execution of the apoptotic death programme in many, if not all, current models of apoptotic cell death. Signalling by ROS would not appear to be random, as previously assumed, but targeted at specific metabolic and signal transduction cellular components. There is also evidence that the enzymatic generation of ROS may not simply be an unwanted by-product of the primary reaction catalysed, but that ROS may be used as signalling molecules to regulate cellular processes including apoptosis. This view of ROS as signalling molecules (as opposed to toxic metabolites) has been further bolstered by the findings that cellular antioxidants such as glutathione and thioredoxin not only serve to regulate ROS levels but also act as reversible redox modifiers of enzyme function. This review will attempt to delineate the involvement of ROS in apoptosis in light of these recent discoveries and provide evidence for a crucial role for ROS in the initiation and execution of the death process.","authors":"Carmody RJ, Cotter TG","authors_abbrev":"Carmody RJ et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-07-14","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9725898","title":"An alpha-tubulin mutant destabilizes the heterodimer: phenotypic consequences and interactions with tubulin-binding proteins.","citation":"Mol Biol Cell 1998 Sep;9(9):2349-60","abstract":"Many effectors of microtubule assembly in vitro enhance the polymerization of subunits. However, several Saccharomyces cerevisiae genes that affect cellular microtubule-dependent processes appear to act at other steps in assembly and to affect polymerization only indirectly. Here we use a mutant alpha-tubulin to probe cellular regulation of microtubule assembly. tub1-724 mutant cells arrest at low temperature with no assembled microtubules. The results of several assays reported here demonstrate that the heterodimer formed between Tub1-724p and beta-tubulin is less stable than wild-type heterodimer. The unstable heterodimer explains several conditional phenotypes conferred by the mutation. These include the lethality of tub1-724 haploid cells when the beta-tubulin-binding protein Rbl2p is either overexpressed or absent. It also explains why the TUB1/tub1-724 heterozygotes are cold sensitive for growth and why overexpression of Rbl2p rescues that conditional lethality. Both haploid and heterozygous tub1-724 cells are inviable when another microtubule effector, PAC2, is overexpressed. These effects are explained by the ability of Pac2p to bind alpha-tubulin, a complex we demonstrate directly. The results suggest that tubulin-binding proteins can participate in equilibria between the heterodimer and its components.","authors":"Vega LR, Fleming J, Solomon F","authors_abbrev":"Vega LR et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-09-03","publication_year":"1998","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31G5.11","SPBC800.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7613084","title":"Eukaryotic replicators and associated protein complexes.","citation":"Curr Opin Genet Dev 1995 Apr;5(2):162-7","abstract":"In the past year, genetic studies have provided a detailed understanding of the DNA sequence elements that constitute Saccharomyces cerevisiae origins of DNA replication and have identified larger DNA domains that direct DNA replication in both Schizosaccharomyces pombe and human cells. In vivo studies of the proteins associated with S. cerevisiae origins of DNA replication indicate that there are dynamic changes in origin chromatin structure during the cell cycle and suggest that the Cdc7 protein kinase is among the associated proteins.","authors":"Bell SP","authors_abbrev":"Bell SP","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28775153","title":"Screening and purification of natural products from actinomycetes that affect the cell shape of fission yeast.","citation":"J Cell Sci 2017 Sep 15;130(18):3173-3185","abstract":"This study was designed to identify bioactive compounds that alter the cellular shape of the fission yeast  Schizosaccharomyces pombe  by affecting functions involved in the cell cycle or cell morphogenesis. We used a multidrug-sensitive fission yeast strain, SAK950 to screen a library of 657 actinomycete bacteria and identified 242 strains that induced eight different major shape phenotypes in  S. pombe  These include the typical cell cycle-related phenotype of elongated cells, and the cell morphology-related phenotype of rounded cells. As a proof of principle, we purified four of these activities, one of which is a novel compound and three that are previously known compounds, leptomycin B, streptonigrin and cycloheximide. In this study, we have also shown novel effects for two of these compounds, leptomycin B and cycloheximide. The identification of these four compounds and the explanation of the  S. pombe  phenotypes in terms of their known, or predicted bioactivities, confirm the effectiveness of this approach.","doi":"10.1242/jcs.194571","authors":"Lewis RA, Li J, Allenby NEE, Errington J, Hayles J, Nurse P","authors_abbrev":"Lewis RA et al.","pubmed_publication_date":"15 Sep 2017","pubmed_entrez_date":"2017-08-05","publication_year":"2017","canto_session_key":"d24a14abb87caf09","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2019-05-02 15:01:43","canto_approved_date":"2021-01-06 11:20:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-04-25 13:33:09","canto_added_date":"2017-08-06 00:15:14","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":3,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPBC216.05","SPCC18B5.11c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-05-02"},{"uniquename":"PMID:12760061","title":"Analysis of the fission yeast checkpoint Rad proteins.","citation":"Cold Spring Harb Symp Quant Biol 2000;65:451-6","abstract":"","authors":"Caspari T, Davies C, Carr AM","authors_abbrev":"Caspari T et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2003-05-23","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14034177","title":"Qualitative and quantitative studies on the cell wall carbohydrate in yeast, Schizosaccharomyces pombe.","citation":"Chem Pharm Bull (Tokyo) 1962 Jan;10:61-6","abstract":"","authors":"KOGANE F, YANAGITA T","authors_abbrev":"KOGANE F et al.","pubmed_publication_date":"Jan 1962","pubmed_entrez_date":"1962-01-01","publication_year":"1962","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ251862","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.29"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32761854","title":"Meiosis I Kinase Regulators: Conserved Orchestrators of Reductional Chromosome Segregation.","citation":"Bioessays 2020 Oct;42(10):e2000018","abstract":"Research over the last two decades has identified a group of meiosis-specific proteins, consisting of budding yeast Spo13, fission yeast Moa1, mouse MEIKIN, and Drosophila Mtrm, with essential functions in meiotic chromosome segregation. These proteins, which we call meiosis I kinase regulators (MOKIRs), mediate two major adaptations to the meiotic cell cycle to allow the generation of haploid gametes from diploid mother cells. Firstly, they promote the segregation of homologous chromosomes in meiosis I (reductional division) by ensuring that sister kinetochores face towards the same pole (mono-orientation). Secondly, they safeguard the timely separation of sister chromatids in meiosis II (equational division) by counteracting the premature removal of pericentromeric cohesin, and thus prevent the formation of aneuploid gametes. Although MOKIRs bear no obvious sequence similarity, they appear to play functionally conserved roles in regulating meiotic kinases. Here, the known functions of MOKIRs are reviewed and their possible mechanisms of action are discussed. Also see the video abstract here https://youtu.be/tLE9KL89bwk.","doi":"10.1002/bies.202000018","authors":"Galander S, Marston AL","authors_abbrev":"Galander S et al.","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-08-08","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-08-09 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15E1.07c","SPCC1183.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"EMBL:AB029547","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1706437","title":"Sequence changes in both flanking sequences of a pre-tRNA influence the cleavage specificity of RNase P.","citation":"J Mol Biol 1991 Feb 20;217(4):637-48","abstract":"The cleavage specificities of the RNase P holoenzymes from Escherichia coli and the yeast Schizosaccharomyces pombe and of the catalytic M1 RNA from E. coli were analyzed in 5'-processing experiments using a yeast serine pre-tRNA with mutations in both flanking sequences. The template DNAs were obtained by enzymatic reactions in vitro and transcribed with phage SP6 or T7 RNA polymerase. The various mutations did not alter the cleavage specificity of the yeast RNase P holoenzyme; cleavage always occurred predominantly at position G + 1, generating the typical seven base-pair acceptor stem. In contrast, the specificity of the prokaryotic RNase P activities, i.e. the catalytic M1 RNA and the RNase P holoenzyme from E. coli, was influenced by some of the mutated pre-tRNA substrates, which resulted in an unusual cleavage pattern, generating extended acceptor stems. The bases G - 1 and C + 73, forming the eighth base pair in these extended acceptor stems, were an important motif in promoting the unusual cleavage pattern. It was found only in some natural pre-tRNAs, including tRNA(SeCys) from E. coli, and tRNAs(His) from bacteria and chloroplasts. Also, the corresponding mature tRNAs in vivo contain an eight base pair acceptor stem. The presence of the CCA sequence at the 3' end of the tRNA moiety is known to enhance the cleavage efficiency with the catalytic M1 RNA. Surprisingly, the presence or absence of this sequence in two of our substrate mutants drastically altered the cleavage specificity of M1 RNA and of the E. coli holoenzyme, respectively. Possible reasons for the different cleavage specificities of the enzymes, the influence of sequence alterations and the importance of stacking forces in the acceptor stems are discussed.","authors":"Krupp G, Kahle D, Vogt T, Char S","authors_abbrev":"Krupp G et al.","pubmed_publication_date":"20 Feb 1991","pubmed_entrez_date":"1991-02-20","publication_year":"1991","canto_session_key":"41c7105be86158da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 14:04:59","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-20 14:04:39","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.128"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:24400488","title":"[SAGA complex subunit Spt20 involves in the calcineurin-mediated Cl- homeostasis in Schizosaccharomyces pombe].","citation":"Yi Chuan 2013 Sep;35(9):1135-42","abstract":"SAGA (Spt-Ada-Gcn5 acetyltransferase) is a highly conserved protein complex in eukaryotes, which plays a role in many important cellular processes, including transcriptional activation and mRNA exportation. In order to investigate the potential biological function of SAGA subunit, we performed a yeast two-hybrid screen using a core structural subunit of SAGA in fission yeast, Spt20, as the bait. Ppbl, catalytic subunit of calcineruin was identified in the test. Calcineurin is a key regulator of signal transduction. The interaction between Spt20 and Ppb1 was confirmed by yeast two-hybrid assay and co-immunoprecipitation. In S. pombe, ppb1delta was hypersensitive to high concentration of Cl-. In contrast, spt20delta could resist high concentration of Cl-, which maintained normal growth of cells. Fluorescent colocalization analysis showed that Ppb1 was translocated from cytoplasm to nucleus and colocalized with Spt20 upon the increase of extracellular Cl-. Further genetic analysis revealed that loss of spt20+ suppressed the hypersensitive phenotype to Cl- of ppbldelta. Thus, spt20+ and ppb1+ stayed in the same pathway of regulating Cl- homeostasis and spt20+ functioned downstream of ppb1+. Our data suggest that spt20delta is able to resist high concentration of extracellular Cl- and Spt20 involves in the calcineurin-mediated Cl- homeostasis. The aberrant up-regulation of intracellular Cl- is correlated with the diseases like myocardial ischemia reperfusion injury in higher organism. As Spt20 is highly conserved in eukaryotes, it might serve as a potential drug target in Cl- imbalance related diseases.","authors":"Zhou N, Lei BK, Zhou X, Yu Y, Lv H","authors_abbrev":"Zhou N et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2014-01-10","publication_year":"2013","canto_session_key":"a6f09178f6358600","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19412884","title":"Common themes in siRNA-mediated epigenetic silencing pathways.","citation":"Int J Dev Biol 2009;53(2-3):245-57","abstract":"Small interfering RNAs (siRNAs) act through RNA interference (RNAi) pathways to silence gene expression either at the transcriptional or post-transcriptional level. Here, we review mechanisms and functions of siRNA-mediated silencing pathways that promote chromatin modifications in the fission yeast Schizosaccharomyces pombe, plants and animals. In fission yeast, siRNAs are involved in heterochromatin formation and key aspects of the underlying siRNA-dependent pathway have been uncovered. Two RNAi complexes, the RNA-Induced Transcriptional Silencing complex (RITS), which contains a siRNA bound to an Argonaute protein, and the RNA-Directed RNA polymerase Complex (RDRC) are critical components of the pathway. In addition, this pathway implicates non-coding nascent transcripts synthesized by RNA polymerase II (RNApII) and the RNApII itself. In Arabidopsis thaliana, the RNA-directed DNA methylation (RdDM) pathway appears to share a similar set of proteins and enzymatic activities, suggesting that, beyond certain aspects that are specific to each pathway, part of the siRNA-mediated epigenetic silencing mechanisms are conserved between fission yeast and plants. Moreover, in both organisms the pathways target repetitive DNA sequences. This conservation of mechanisms and genomic targets might actually extend to animals as recent investigations revealed the existence of endogenous siRNA-based pathways directed against repetitive DNA sequences in flies and mammals.","doi":"10.1387/ijdb.082691av","authors":"Verdel A, Vavasseur A, Le Gorrec M, Touat-Todeschini L","authors_abbrev":"Verdel A et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-05-05","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7957097","title":"Phosphorylation of dis2 protein phosphatase at the C-terminal cdc2 consensus and its potential role in cell cycle regulation.","citation":"EMBO J 1994 Nov 15;13(22):5310-8","abstract":"We show that the fission yeast dis2 protein phosphatase, which is highly similar to mammalian type 1 phosphatase, is a phosphoprotein containing phosphoserine (phospho-S) and threonine (phospho-T). It has several phosphorylation sites, two of which locate in the C-terminus. Phospho-T was abolished in the alanine substitution mutant at the C-terminal T316, which is conserved as a residue in the cdc2 consensus, TPPR, in a number of type 1-like phosphatases. In G2-arrested cdc2-L7 cells, the degree of T316 phosphorylation was reduced, whereas it was enhanced in metaphase-arrested nuc2-663 mutant cells. Phospho-T was produced in dis2 by fission yeast cdc2 kinase, but not in the substitution mutant A316, indicating that the T316 residue was the site for cdc2 kinase in vitro. Phosphatase activity of wild type dis2 was reduced by incubation with cdc2 kinase, but that of mutant dis2-A316 was not. Phosphorylation of T316 hence has a potential significance in cell cycle control in conjunction with cdc2 kinase activation and inactivation. Overexpression phenotypes of wild type dis2+, sds21+ and mutant dis2-A316, sds21-TPPR genes were consistent with negative regulation of dis2 by phosphorylation. This type of regulation would explain why cells harboring the dis2-11 mutation enter mitosis but fail to exit from it.","authors":"Yamano H, Ishii K, Yanagida M","authors_abbrev":"Yamano H et al.","pubmed_publication_date":"15 Nov 1994","pubmed_entrez_date":"1994-11-15","publication_year":"1994","canto_session_key":"31b52625e666e444","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-08-17 15:37:54","canto_approved_date":"2024-03-28 15:33:03","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-12-04 10:16:07","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC31H12.05c","SPBC11B10.09","SPBC776.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-08-17"},{"uniquename":"PMID:24947016","title":"Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery.","citation":"Nat Commun 2014 Jun 20;5:4192","abstract":"In living organisms, most proteins work in complexes to form multicomponent protein machines. The function of such multicomponent machines is usually addressed by dividing them into a collection of two state systems at equilibrium. Many molecular machines, like Hsp90, work far from equilibrium by utilizing the energy of ATP hydrolysis. In these cases, important information is gained from the observation of the succession of more than two states in a row. We developed a four-colour single-molecule FRET system to observe the succession of states in the heat shock protein 90 (Hsp90) system, consisting of an Hsp90 dimer, the cochaperone p23 and nucleotides. We show that this multicomponent system is a directional ATP-dependent machinery. This reveals a previously undescribed mechanism on how cochaperones can modify Hsp90, namely by strengthening of the coupling between ATP hydrolysis and a kinetic step involved in the Hsp90 system resulting in a stronger directionality.","doi":"10.1038/ncomms5192","authors":"Ratzke C, Hellenkamp B, Hugel T","authors_abbrev":"Ratzke C et al.","pubmed_publication_date":"20 Jun 2014","pubmed_entrez_date":"2014-06-21","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-07-22 00:28:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1264063","title":"Extrachromosomal inheritance in Schizosaccharomyces pombe. I. Evidence for an extrakaryotically inherited mutation conferring resistance to antimycin.","citation":"Mol Gen Genet 1976 Feb 27;144(1):67-73","abstract":"In crosses of [ANTr8] with auxotrophic strains, resistance to antimycin segregates almost 50:50 in random spore analysis with a slight preponderance for the sensitivity allele. Tetrad analysis, however, shows all possible types of tetrads (2:2; 3:1; 1:3; 4:0; 0:4 resistant versus sensitive) with an excess of 2:2 segregations and sectoring of colonies on antimycin medium indicating an extrachromosomal mode of inheritance. The overall ratio of resistant versus sensitive spores is the same as compared with random spore data. Using a mutant blocked in meiosis (mei 1) mitotic segregation of stable diploids is achieved, leading to a ratio of 20% resistant to 80% sensitive clones. Possible reasons for the bias in transmission of the resistance determinant is discussed.","authors":"Wolf K, Burger G, Lang B, Kaudewitz F","authors_abbrev":"Wolf K et al.","pubmed_publication_date":"27 Feb 1976","pubmed_entrez_date":"1976-02-27","publication_year":"1976","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29084364","title":"The natural diversity and ecology of fission yeast.","citation":"Yeast 2018 Mar;35(3):253-260","abstract":"While the fission yeast is a powerful model of eukaryote biology, there have been few studies of quantitative genetics, phenotypic or genetic diversity. Here I survey the small collection of fission yeast diversity research. I discuss what we can infer about the ecology and origins of Schizosaccharomyces pombe from microbiology field studies and the few strains that have been collected.","doi":"10.1002/yea.3293","authors":"Jeffares DC","authors_abbrev":"Jeffares DC","pubmed_publication_date":"Mar 2018","pubmed_entrez_date":"2017-10-31","publication_year":"2018","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2017-11-02 01:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22094428","title":"Evolution of asymmetric damage segregation : a modelling approach.","citation":"Subcell Biochem 2012;57:315-30","abstract":"Mother cell-specific ageing is a well-known phenomenon in budding yeast Saccharomyces cerevisiae. Asymmetric segregation of damage and its accumulation in the mother cell has been proposed as one important mechanism. There are, however, unicellular organisms such as the fission yeast Schizosaccharomyces pombe, which replicates with almost no asymmetry of segregation of damage and the pathogenic yeast Candida albicans, which falls around the middle of the segregation spectrum far from both complete symmetry and complete asymmetry. The ultimate evolutionary cause that determines the way damage segregates in a given organism is not known. Here we develop a mathematical model to examine the selective forces that drive the evolution of asymmetry and discover the conditions in which symmetry is the optimal strategy. Three main processes are included in the model: protein synthesis (growth), protein damage, and degradation of damage. We consider, for the first time, the costs to the cell that might accompany the evolution of asymmetry and incorporate them into the model along with known trade-offs between reproductive and maintenance investments and their energy requirements. The model provides insight into the relationship between ecology and cellular trade-off physiology in the context of unicellular ageing, and applications of the model may extend to multicellular organisms.","doi":"10.1007/978-94-007-2561-4_14","authors":"Rashidi A, Kirkwood TB, Shanley DP","authors_abbrev":"Rashidi A et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2011-11-19","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19570910","title":"A link between aurora kinase and Clp1/Cdc14 regulation uncovered by the identification of a fission yeast borealin-like protein.","citation":"Mol Biol Cell 2009 Aug;20(16):3646-59","abstract":"The chromosomal passenger complex (CPC) regulates various events in cell division. This complex is composed of a catalytic subunit, Aurora B kinase, and three nonenzymatic subunits, INCENP, Survivin, and Borealin. Together, these four subunits interdependently regulate CPC function, and they are highly conserved among eukaryotes. However, a Borealin homologue has never been characterized in the fission yeast, Schizosaccharomyces pombe. Here, we isolate a previously uncharacterized S. pombe protein through association with the Cdc14 phosphatase homologue, Clp1/Flp1, and identify it as a Borealin-like member of the CPC. Nbl1 (novel Borealin-like 1) physically associates with known CPC components, affects the kinase activity and stability of the S. pombe Aurora B homologue, Ark1, colocalizes with known CPC subunits during mitosis, and shows sequence similarity to human Borealin. Further analysis of the Clp1-Nbl1 interaction indicates that Clp1 requires CPC activity for proper accumulation at the contractile ring (CR). Consistent with this, we describe negative genetic interactions between mutant alleles of CPC and CR components. Thus, this study characterizes a fission yeast Borealin homologue and reveals a previously unrecognized connection between the CPC and the process of cytokinesis in S. pombe.","authors":"Bohnert KA, Chen JS, Clifford DM, Vander Kooi CW, Gould KL","authors_abbrev":"Bohnert KA et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-07-03","publication_year":"2009","canto_session_key":"76d4e1bbb7105cb9","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC725.12","SPCC320.13c","SPCC962.02c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU007724","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22918943","title":"Anillin-related protein Mid1p coordinates the assembly of the cytokinetic contractile ring in fission yeast.","citation":"Mol Biol Cell 2012 Oct;23(20):3982-92","abstract":"In fission yeast cells cortical nodes containing the protein Blt1p and several kinases appear early in G2, mature into cytokinetic nodes by adding anillin Mid1p, myosin-II, formin Cdc12p, and other proteins, and condense into a contractile ring by movements that depend on actin and myosin-II. Previous studies concluded that cells without Mid1p lack cytokinetic nodes and assemble rings unreliably from myosin-II strands but left open questions. Why do strands form outside the equatorial region? Why is ring assembly unreliable without Mid1p? We found in Δmid1 cells that Cdc12p accumulates in cytokinetic nodes scattered in the cortex and produces actin filaments that associate with myosin-II, Rng2p, and Cdc15p to form strands located between the nodes. Strands incorporate nodes, and in ~67% of cells, strands slowly close into rings that constrict without the normal ~25-min maturation period. Ring assembly is unreliable and slow without Mid1p because the scattered Cdc12p nodes generate strands spread widely beyond the equator, and growing strands depend on random encounters to merge with other strands into a ring. We conclude that orderly assembly of the contractile ring in wild-type cells depends on Mid1p to recruit myosin-II, Rng2p, and Cdc15p to nodes and to place cytokinetic nodes around the cell equator.","doi":"10.1091/mbc.E12-07-0535","authors":"Saha S, Pollard TD","authors_abbrev":"Saha S et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-25","publication_year":"2012","canto_session_key":"310131206c5ef65d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-18 18:39:04","canto_approved_date":"2019-10-31 11:13:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-17 14:48:37","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.13c","SPAC926.03","SPCC1223.06","SPCC4B3.15","SPCC645.05c","SPAC1F5.04c","SPAC57A10.02","SPBC1A4.05","SPAC20G8.05c"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2019-10-18"},{"uniquename":"PMID:41428730","title":"Mutual, spatially limited control of meiotic DNA break formation by Mre11-Rad50-Nbs1 DNA repair complex and Tel1 (ATM) protein kinase.","citation":"Nucleic Acids Res 2025 Nov 26;53(22)","abstract":"Meiotic recombination is initiated by DNA double-strand breaks (DSBs); factors that control DSB frequencies are important to produce viable progeny. In many organisms, the ATM (Tel1) protein kinase prevents excessive meiotic DSBs, especially nearby DSBs on the same chromatid. Normally, two close DSBs are less frequent than expected from independence, a feature called DSB interference, which is lost in tel1Δ mutants. In the fission yeast Schizosaccharomyces pombe, high-level DSB formation depends on linear elements, Hop1, and meiotic cohesin complexes; we show here that these complexes impart competition between nearby DSB sites. When these complexes are impaired, Tel1 substantially represses DSB formation, and in its absence, two close DSBs on the same chromatid occur frequently and manifest high negative interference. After mitotic DNA damage, the conserved Mre11-Rad50-Nbs1 (MRN) complex is required for DNA resection, and the Tel1 kinase activity is needed to complete DSB repair. We found that during meiosis mre11Δ and rad50Δ mutants, like tel1Δ mutants, lack DSB interference and display highly negative DSB interference in meiotic complex mutants. Thus, MRN at a DSB site appears critical for Tel1 function in meiosis and reveals a complex interplay of positive and negative factors controlling meiotic DSB formation.","doi":"10.1093/nar/gkaf1405","authors":"Hyppa RW, Smith GR","authors_abbrev":"Hyppa RW et al.","pubmed_publication_date":"26 Nov 2025","pubmed_entrez_date":"2025-12-22","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-24 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32915139","title":"Stress-activated MAPK signaling controls fission yeast actomyosin ring integrity by modulating formin For3 levels.","citation":"Elife 2020 Sep 11;9","abstract":"Cytokinesis, which enables the physical separation of daughter cells once mitosis has been completed, is executed in fungal and animal cells by a contractile actin- and myosin-based ring (CAR). In the fission yeast  Schizosaccharomyces pombe,  the formin For3 nucleates actin cables and also co-operates for CAR assembly during cytokinesis. Mitogen-activated protein kinases (MAPKs) regulate essential adaptive responses in eukaryotic organisms to environmental changes. We show that the stress-activated protein kinase pathway (SAPK) and its effector, MAPK Sty1, downregulates CAR assembly in  S. pombe  when its integrity becomes compromised during cytoskeletal damage and stress by reducing For3 levels. Accurate control of For3 levels by the SAPK pathway may thus represent a novel regulatory mechanism of cytokinesis outcome in response to environmental cues. Conversely, SAPK signaling favors CAR assembly and integrity in its close relative  Schizosaccharomyces japonicus,  revealing a remarkable evolutionary divergence of this response within the fission yeast clade.","doi":"10.7554/eLife.57951","authors":"Gómez-Gil E, Martín-García R, Vicente-Soler J, Franco A, Vázquez-Marín B, Prieto-Ruiz F, Soto T, Pérez P, Madrid M, Cansado J","authors_abbrev":"Gómez-Gil E et al.","pubmed_publication_date":"11 Sep 2020","pubmed_entrez_date":"2020-09-11","publication_year":"2020","canto_session_key":"8b5476ba0daf2d2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elisa Gómez Gil","canto_first_approved_date":"2020-10-26 11:34:54","canto_approved_date":"2025-04-18 16:43:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-10-21 10:57:51","canto_added_date":"2020-09-13 00:15:06","annotation_curators":[{"name":"Elisa Gómez Gil","community_curator":true,"annotation_count":43,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.04c","SPAC27F1.02c","SPBC16G5.01","SPAC9G1.02","SPAC1006.09","SPAC24H6.09","SPBC887.10","SPAC24B11.06c","SPCC4F11.02","SPCC895.05","SPAC16E8.09","SPBC29B5.01","SPBC409.07c","SPAC4A8.15c","SPBC32H8.12c","SPAC26F1.10c"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2020-10-26"},{"uniquename":"PMID:27069798","title":"Characterisation of Schizosaccharomyces pombe α-actinin.","citation":"PeerJ 2016;4:e1858","abstract":"The actin cytoskeleton plays a fundamental role in eukaryotic cells. Its reorganization is regulated by a plethora of actin-modulating proteins, such as a-actinin. In higher organisms, α-actinin is characterized by the presence of three distinct structural domains: an N-terminal actin-binding domain and a C-terminal region with EF-hand motif separated by a central rod domain with four spectrin repeats. Sequence analysis has revealed that the central rod domain of α-actinin from the fission yeast Schizosaccharomyces pombe consists of only two spectrin repeats. To obtain a firmer understanding of the structure and function of this unconventional α-actinin, we have cloned and characterized each structural domain. Our results show that this a-actinin isoform is capable of forming dimers and that the rod domain is required for this. However, its actin-binding and cross-linking activity appears less efficient compared to conventional α-actinins. The solved crystal structure of the actin-binding domain indicates that the closed state is stabilised by hydrogen bonds and a salt bridge not present in other α-actinins, which may reduce the affinity for actin.","doi":"10.7717/peerj.1858","authors":"Addario B, Sandblad L, Persson K, Backman L","authors_abbrev":"Addario B et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-04-13","publication_year":"2016","canto_session_key":"e038a0ad35ea7135","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lars Backman","canto_first_approved_date":"2019-11-26 20:15:51","canto_approved_date":"2025-09-03 15:34:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-26 12:03:38","canto_added_date":"2016-04-15 00:15:15","annotation_curators":[{"name":"Lars Backman","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-26","pdb_entries":[{"pdb_id":"5bvr","gene_chains":[{"gene_uniquename":"SPAC15A10.08","chain":"A","position":"1-234"}],"title":"Actin binding domain of alpha-actinin from Schizosaccharomyces pombe","entry_authors":"Persson K,Backman L,Addario B","entry_authors_abbrev":"Persson K et al.","reference_uniquename":"PMID:27069798","experimental_method":"X-ray","resolution":"1.46"}]},{"uniquename":"PMID:9430640","title":"Regulation of the G1 phase of the cell cycle by periodic stabilization and degradation of the p25rum1 CDK inhibitor.","citation":"EMBO J 1998 Jan 15;17(2):482-97","abstract":"In fission yeast, the cyclin-dependent kinase (CDK) inhibitor p25(rum1) is a key regulator of progression through the G1 phase of the cell cycle. We show here that p25(rum1) protein levels are sharply periodic. p25(rum1) begins to accumulate at anaphase, persists in G1 and is destroyed during S phase. p25(rum1 )is stabilized and polyubiquitinated in a mutant defective in the 26S proteasome, suggesting that its degradation normally occurs through the ubiquitin-dependent 26S proteasome pathway. Phosphorylation of p25(rum1 )by cdc2-cyclin complexes at residues T58 and T62 is important to target the protein for degradation. Mutation of one or both of these residues to alanine causes stabilization of p25(rum1) and induces a cell cycle delay in G1 and polyploidization due to occasional re-initiation of DNA replication before mitosis. The CDK-cyclin complex cdc2-cig1, which is insensitive to p25(rum1 )inhibition, seems to be the main kinase that phosphorylates p25(rum1). Phosphorylation of p25(rum1) in S phase and G2 serves as the trigger for p25(rum1) proteolysis. Thus, periodic accumulation and degradation of the CDK inhibitor p25(rum1 )in G1 plays a role in setting a threshold of cyclin levels important in determining the length of the pre-Start G1 phase and in ensuring the correct order of cell cycle events.","authors":"Benito J, Martín-Castellanos C, Moreno S","authors_abbrev":"Benito J et al.","pubmed_publication_date":"15 Jan 1998","pubmed_entrez_date":"1998-02-28","publication_year":"1998","canto_session_key":"e9f007db7b387da3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-05-14 16:31:52","canto_approved_date":"2024-03-04 09:35:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-07 12:53:01","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":16,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16G5.01","SPBC336.12c","SPBC32F12.09","SPCC4E9.02","SPCC18B5.03","SPBC582.03","SPAPB2B4.03","SPBC11B10.09","SPBC29B5.01"],"gene_count":9,"ltp_gene_count":5,"approved_date":"2021-05-14"},{"uniquename":"PMID:18438419","title":"The exonuclease ERI-1 has a conserved dual role in 5.8S rRNA processing and RNAi.","citation":"Nat Struct Mol Biol 2008 May;15(5):531-3","abstract":"The exonuclease ERI-1 negatively regulates RNA interference in Caenorhabditis elegans and Schizosaccharomyces pombe, and is required for production of some C. elegans endogenous small interfering RNAs. We show that ERI-1 performs 3' end processing of the 5.8S ribosomal RNA in both C. elegans and S. pombe. In C. elegans, two protein isoforms of ERI-1 are localized to the cytoplasm, and each has distinct functions in ribosomal RNA processing and negative regulation of RNA interference.","doi":"10.1038/nsmb.1411","authors":"Gabel HW, Ruvkun G","authors_abbrev":"Gabel HW et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-04-29","publication_year":"2008","canto_session_key":"a80ade718347d401","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-11 00:35:24","canto_approved_date":"2017-12-11 00:35:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-12-11 00:35:14","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30B4.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-12-11"},{"uniquename":"PMID:21781055","title":"Zeocin for selection of bleMX6 resistance in fission yeast.","citation":"Biotechniques 2011 Jul;51(1):57-60","abstract":"Complementation of auxotrophic nutrient deficiencies in minimal media is widely used for selection of exogenous gene introduction to fission yeast. However, only a limited number of such selection markers are available. Antibiotic resistance markers are good alternatives, but they typically work well in complete rich medium but not in minimal defined Edinburgh minimal medium (EMM). It would be ideal if both the auxotrophic and antibiotic resistance markers can be used together for molecular genetic analysis. Here we describe the use of Zeocin in Pombe minimal glutamate (PMG) media for selection and maintenance of bleMX6 resistance with a LEU2 auxotrophic marker in fission yeast.","doi":"10.2144/000113706","authors":"Benko Z, Zhao RY","authors_abbrev":"Benko Z et al.","pubmed_publication_date":"Jul 2011","pubmed_entrez_date":"2011-07-26","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27229179","title":"Structure of the intact ATM/Tel1 kinase.","citation":"Nat Commun 2016 May 27;7:11655","abstract":"The ataxia-telangiectasia mutated (ATM) protein is an apical kinase that orchestrates the multifaceted DNA-damage response. Normally, ATM kinase is in an inactive, homodimer form and is transformed into monomers upon activation. Besides a conserved kinase domain at the C terminus, ATM contains three other structural modules, referred to as FAT, FATC and N-terminal helical solenoid. Here we report the first cryo-EM structure of ATM kinase, which is an intact homodimeric ATM/Tel1 from Schizosaccharomyces pombe. We show that two monomers directly contact head-to-head through the FAT and kinase domains. The tandem N-terminal helical solenoid tightly packs against the FAT and kinase domains. The structure suggests that ATM/Tel1 dimer interface and the consecutive HEAT repeats inhibit the binding of kinase substrates and regulators by steric hindrance. Our study provides a structural framework for understanding the mechanisms of ATM/Tel1 regulation as well as the development of new therapeutic agents.","doi":"10.1038/ncomms11655","authors":"Wang X, Chu H, Lv M, Zhang Z, Qiu S, Liu H, Shen X, Wang W, Cai G","authors_abbrev":"Wang X et al.","pubmed_publication_date":"27 May 2016","pubmed_entrez_date":"2016-05-28","publication_year":"2016","canto_session_key":"c86b71780c0f287c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-06-08 10:05:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-06-08 10:05:24","canto_added_date":"2016-05-29 00:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC23B6.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-06-08"},{"uniquename":"PMID:21964262","title":"Production of recombinant proteins by yeast cells.","citation":"Biotechnol Adv 2012;30(5):1108-18","abstract":"Yeasts are widely used in production of recombinant proteins of medical or industrial interest. For each individual product, the most suitable expression system has to be identified and optimized, both on the genetic and fermentative level, by taking into account the properties of the product, the organism and the expression cassette. There is a wide range of important yeast expression hosts including the species Saccharomyces cerevisiae, Pichia pastoris, Hansenula polymorpha, Kluyveromyces lactis, Schizosaccharomyces pombe, Yarrowia lipolytica and Arxula adeninivorans, with various characteristics such as being thermo-tolerant or halo-tolerant, rapidly reaching high cell densities or utilizing unusual carbon sources. Several strains were also engineered to have further advantages, such as humanized glycosylation pathways or lack of proteases. Additionally, with a large variety of vectors, promoters and selection markers to choose from, combined with the accumulated knowledge on industrial-scale fermentation techniques and the current advances in the post-genomic technology, it is possible to design more cost-effective expression systems in order to meet the increasing demand for recombinant proteins and glycoproteins. In this review, the present status of the main and most promising yeast expression systems is discussed.","doi":"10.1016/j.biotechadv.2011.09.011","authors":"Celik E, Calık P","authors_abbrev":"Celik E et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2011-10-04","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39789818","title":"SRPKs Homolog Dsk1 Regulates Homologous Recombination Repair in Schizosaccharomyces pombe.","citation":"Genes Cells 2025 Jan;30(1):e13192","abstract":"Serine-arginine protein kinases (SRPKs) play important roles in diverse biological processes such as alternative splicing and cell cycle. However, the functions of SRPKs in DNA damage response remain unclear. Here we characterized the function of SRPKs homolog Dsk1 in regulating DNA repair in the fission yeast Schizosaccharomyces pombe. We demonstrated that Dsk1 defective mutants of loss of the gene, spacer domain, and kinase activity as well as its overexpression mutant exhibited sensitivities of replication stress. Genetic analysis revealed that the loss of dsk1 +  compromised the efficiency of homologous recombination (HR) repair, and Dsk1 was probably involved in the Rad52- and Rad51-dependent HR repair pathways. Interestingly, Dsk1 translocated into the nucleus upon replication stress and directly interacted with Rad51-mediator Rad52 and phosphorylated Rad52-Ser365 residue. The Rad52-Ser365 phosphorylation-defective mutant was slightly sensitive to replication stress, and the phosphorylation-mimicking mutants exhibited more sensitivities, which were partially correlated with phenotypes of the loss- and gain-of-function of dsk1 + . This study uncovers a potential HR repair regulator Dsk1 in response to replication stress and implies that its homolog SRPKs may have the conserved targets and functions in higher eukaryotes.","doi":"10.1111/gtc.13192","authors":"Lu G, Tang Z, Wu M, Liu L, Opoku M, Bian K, Ruan R, Shang J, Liu J, Feng G","authors_abbrev":"Lu G et al.","pubmed_publication_date":"Jan 2025","pubmed_entrez_date":"2025-01-10","publication_year":"2025","canto_session_key":"0bca2cbb0e3b6375","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Guangchun Lu","canto_first_approved_date":"2025-05-19 15:26:03","canto_approved_date":"2026-06-26 10:57:39","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-30 07:14:45","canto_added_date":"2025-01-11 00:25:04","annotation_curators":[{"name":"Guangchun Lu","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":49,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC530.14c","SPAC11E3.04c","SPAC644.14c","SPCC1259.13","SPBC1734.06","SPCC18B5.11c","SPAC30D11.10"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2025-05-19"},{"uniquename":"PMID:5582422","title":"[Allosteric kinetics of inhibition of the 1st enzyme for the biosynthesis of histidine in S. pombe].","citation":"Bull Soc Chim Biol (Paris) 1967 Dec 18;49(11):1529-35","abstract":"","authors":"Whitehead EP","authors_abbrev":"Whitehead EP","pubmed_publication_date":"18 Dec 1967","pubmed_entrez_date":"1967-12-18","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8224870","title":"Distribution of bent DNA structures in the fission yeast centromere.","citation":"Gene 1993 Oct 15;132(2):247-50","abstract":"To gain a clue as to the functional significance of DNA curvature, we experimentally characterized the distribution of bent DNA structures throughout the 35-kb cen1 sequence, one of the isolated functional centromeric DNA of the fission yeast, Schizosaccharomyces pombe. It was revealed that a relatively large central portion of cen1, covering a 2.2-kb DNA sequence, displays a remarkable DNA curvature.","authors":"Ueki N, Momoi H, Yamada H, Mizuno T","authors_abbrev":"Ueki N et al.","pubmed_publication_date":"15 Oct 1993","pubmed_entrez_date":"1993-10-15","publication_year":"1993","canto_session_key":"d3644e7030f51650","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-02-02 00:01:28","canto_approved_date":"2019-02-02 00:01:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-02 00:01:22","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-02-02"},{"uniquename":"PMID:10593886","title":"Direct activation of the fission yeast PAK Shk1 by the novel SH3 domain protein, Skb5.","citation":"J Biol Chem 1999 Dec 17;274(51):36052-7","abstract":"The p21-activated kinase (PAK) homolog Shk1 is essential for cell viability in the fission yeast Schizosaccharomyces pombe. Roles have been established for Shk1 in the regulation of cell morphology, sexual differentiation, and mitosis in S. pombe. In this report, we describe the genetic and molecular characterization of a novel SH3 domain protein, Skb5, identified as a result of a two-hybrid screen for Shk1 interacting proteins. S. pombe cells carrying a deletion of the skb5 gene exhibit no discernible phenotypic defects under normal growth conditions, but when subjected to hypertonic stress, become spheroidal in shape and growth impaired. Both of these defects can be suppressed by overexpression of the Shk1 modulator, Skb1. The growth inhibition that results from overexpression of Shk1 in S. pombe cells is markedly suppressed by a null mutation in the skb5 gene, suggesting that Skb5 contributes positively to the function of Shk1 in vivo. Consistent with this notion, we show that Skb5 stimulates Shk1 catalytic function in S. pombe cells. Furthermore, and perhaps most significantly, we show that bacterially expressed recombinant Skb5 protein directly stimulates the catalytic activity of recombinant Shk1 kinase in vitro. These and additional data described herein demonstrate that Skb5 is a direct activator of Shk1 in fission yeast.","authors":"Yang P, Pimental R, Lai H, Marcus S","authors_abbrev":"Yang P et al.","pubmed_publication_date":"17 Dec 1999","pubmed_entrez_date":"1999-12-14","publication_year":"1999","canto_session_key":"a6edcf7d02f0562a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-05-30 16:29:34","canto_approved_date":"2019-02-22 10:06:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-02 17:20:59","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.03","SPBC16H5.11c","SPBC1604.14c","SPBC1D7.05","SPCC24B10.13","SPAC17H9.09c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-05-30"},{"uniquename":"PMID:9802206","title":"Comparison of expression systems in the yeasts Saccharomyces cerevisiae, Hansenula polymorpha, Klyveromyces lactis, Schizosaccharomyces pombe and Yarrowia lipolytica. Cloning of two novel promoters from Yarrowia lipolytica.","citation":"Yeast 1998 Oct;14(14):1267-83","abstract":"We have compared expression systems based on autonomously replicating vectors in the yeasts Saccharomyces cerevisiae, Schizosaccharomyces pombe, Kluyveromyces lactis, Hansenula polymorpha and Yarrowia lipolytica in order to identify a more suitable host organism for use in the expression cloning method (Dalbøge and Heldt-Hansen, 1994) in which S. cerevisiae has traditionally been used. The capacity of the expression systems to secrete active forms of six fungal genes encoding the enzymes galactanase, lipase, polygalacturonase, xylanase and two cellulases was examined, as well as glycosylation pattern, plasmid stability and transformation frequency. All of the examined alternative hosts were able to secrete more active enzyme than S. cerevisiae but the relative expression capacity of the individual hosts varied significantly in a gene-dependent manner. One of the most attractive of the alternative host organisms, Y. lipolytica, yielded an increase which ranged from 4.5 times to more than two orders of magnitude. As the initially employed Y. lipolytica XPR2 promoter is unfit in the context of expression cloning, two novel promoter sequences for highly expressed genes present in only one copy on the genome were isolated. Based on sequence homology, the genes were identified as TEF, encoding translation elongation factor-1 alpha and RPS7, encoding ribosomal protein S7. Using the heterologous cellulase II (celII) and xylanase I (xylI) as reporter genes, the effect of the new promoters was measured in qualitative and quantitative assays. Based on the present tests of the new promoters. Y. lipolytica appears as a highly attractive alternative to S. cerevisiae as a host organism for expression cloning.","authors":"Müller S, Sandal T, Kamp-Hansen P, Dalbøge H","authors_abbrev":"Müller S et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-11-05","publication_year":"1998","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011992","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11554925","title":"The RGS domain-containing fission yeast protein, Rgs1p, regulates pheromone signalling and is required for mating.","citation":"Genes Cells 2001 Sep;6(9):789-802","abstract":"When nutritionally starved, the fission yeast Schizosaccharomyces pombe enters a cell differentiation process which leads to mating and meiosis. The Ste11 protein is a key regulator of this differentiation pathway, activating the transcription of mating and meiotic genes upon starvation.\nHere, we describe rgs1, a member of the Regulator of G-protein Signalling (RGS) family, as a novel Ste11 target gene. rgs1 expression requires both an Ste11-mediated nitrogen starvation signal and the pheromone-induced activation of the Byr2/Byr1/Spk1 MAPK pathway. We show that rgs1 deletion results in a sensitivity to pheromone and in a mating defect. Deltargs1 cells initiate the mating pathway normally, undergoing sexual agglutination and G1 arrest, while inducing pheromone-dependent transcription, but then fail to fuse with a mating partner while elongating abnormal conjugation tubes. Endogenous Rgs1 tagged with GFP localizes to the nucleus and cytoplasm, and this localization pattern is not altered during pheromone treatment. Importantly, Rgs1 function requires its C-terminal RGS domain, as well as a central DEP domain and a novel homology domain present in its N-terminal region (Fungal-DR domain).\nThese results demonstrate that rgs1 expression requires nutritional starvation and pheromone signalling. Rgs1 negatively regulates pheromone signalling during mating, acting in a negative feedback loop that is essential for the mating process.","authors":"Pereira PS, Jones NC","authors_abbrev":"Pereira PS et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-09-14","publication_year":"2001","canto_session_key":"092002e50e04b6e9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-12-16 16:35:39","canto_approved_date":"2025-12-14 10:21:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-11 19:40:21","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1D7.05","SPAC22F3.12c","SPAC11H11.04","SPAC1D4.13","SPBC19C7.03","SPBC32C12.02","SPAC1296.03c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2020-12-16"},{"uniquename":"PMID:39527205","title":"Assessing Drug Sensitivity in Fission Yeast Using Half-Maximal Inhibitory Concentration (IC50) Assays.","citation":"Methods Mol Biol 2025;2862:241-253","abstract":"Fission yeast is an excellent model organism in which to study mammalian drug sensitivities. In addition to building a mechanistic picture of drug effect, fission yeast screens may be valuable in determining compounds that show synthetic lethality effects. While compounds might be screened for a variety of phenotypes, an effective method is to detect the proliferative effects of a new compound on a yeast culture. This is traditionally performed in acute viability assays or spot tests; both methods require some knowledge of concentration to observe an effect. Mammalian cell culture experiments that assess proliferation to indicate drug dose and effect are well described. However, differences between S. pombe growth characteristics and mammalian cells mean that importing a mammalian viability assay requires consideration of potential effects on fission yeast biology. We describe the half-maximum inhibitory (IC50) dose as a method of rapid proliferation effect screening. IC50 determination is performed on liquid cultures in 96-well plates and may be developed for initial compound library uses or in synthetic lethality screening of drug effects.","doi":"10.1007/978-1-0716-4168-2_17","authors":"Chhipa MA, Sanayhie SA, Sabatinos SA","authors_abbrev":"Chhipa MA et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36524422","title":"Ultrastructure expansion microscopy reveals the cellular architecture of budding and fission yeast.","citation":"J Cell Sci 2022 Dec 15;135(24)","abstract":"The budding and fission yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe have served as invaluable model organisms to study conserved fundamental cellular processes. Although super-resolution microscopy has in recent years paved the way to a better understanding of the spatial organization of molecules in cells, its wide use in yeasts has remained limited due to the specific know-how and instrumentation required, contrasted with the relative ease of endogenous tagging and live-cell fluorescence microscopy. To facilitate super-resolution microscopy in yeasts, we have extended the ultrastructure expansion microscopy (U-ExM) method to both S. cerevisiae and S. pombe, enabling a 4-fold isotropic expansion. We demonstrate that U-ExM allows imaging of the microtubule cytoskeleton and its associated spindle pole body, notably unveiling the Sfi1p-Cdc31p spatial organization on the appendage bridge structure. In S. pombe, we validate the method by monitoring the homeostatic regulation of nuclear pore complex number through the cell cycle. Combined with NHS-ester pan-labelling, which provides a global cellular context, U-ExM reveals the subcellular organization of these two yeast models and provides a powerful new method to augment the already extensive yeast toolbox. This article has an associated First Person interview with Kerstin Hinterndorfer and Felix Mikus, two of the joint first authors of the paper.","doi":"10.1242/jcs.260240","authors":"Hinterndorfer K, Laporte MH, Mikus F, Tafur L, Bourgoint C, Prouteau M, Dey G, Loewith R, Guichard P, Hamel V","authors_abbrev":"Hinterndorfer K et al.","pubmed_publication_date":"15 Dec 2022","pubmed_entrez_date":"2022-12-16","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-12-17 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013401","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23664927","title":"Biochemical characterization and cooperation with co-chaperones of heat shock protein 90 from Schizosaccharomyces pombe.","citation":"J Biosci Bioeng 2013 Oct;116(4):444-8","abstract":"The characterization of Hsp90 from the fission yeast Schizosaccharomyces pombe was performed. Hsp90 of S. pombe existed as a dimer and exhibited ATP-dependent conformational changes. It captured unfolded proteins in the ATP-free open conformation and protected them from thermal aggregation. Hsp90 of S. pombe was also able to refold thermally denatured firefly luciferase. The co-chaperones Sti1 and Aha1 bound Hsp90 and modulated its activity. Because the affinity of Sti1 was higher than that of Aha1, the effect of Sti1 appeared to dominate when both co-chaperones existed simultaneously.","doi":"10.1016/j.jbiosc.2013.04.020","authors":"Ishida M, Tomomari T, Kanzaki T, Abe T, Oka T, Yohda M","authors_abbrev":"Ishida M et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-05-14","publication_year":"2013","canto_session_key":"398bef3311ab35ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-06 16:26:42","canto_approved_date":"2025-12-04 08:04:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-06 16:26:35","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1711.08","SPCC645.14c","SPAC926.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-10-06"},{"uniquename":"PMID:40957559","title":"A distinct phase of cyclin B (Cdc13) nuclear export at mitotic entry in  Schizosaccharomyces pombe .","citation":"Open Biol 2025 Sep;15(9):250199","abstract":"In eukaryotes, cell division requires coordination between the nucleus and cytoplasm. Entry into cell division is driven by cyclin-dependent kinases (CDKs), which need a cyclin binding partner for their activity. In  Schizosaccharomyces pombe  (fission yeast), the B-type cyclin Cdc13 is essential and sufficient for cell cycle progression and is strongly enriched in the nucleus. Here, we show that a fraction of Cdc13 is exported from the nucleus to the cytoplasm just prior to mitosis. This export could be critical to propagate CDK activity throughout the cell. Mutating three Cdc13 nuclear localization signals (NLSs) led to precocious enrichment of Cdc13 in the cytoplasm but did not accelerate mitotic entry, indicating that the export is not sufficient to trigger entry into mitosis. The export coincides with spindle pole body integration into the nuclear envelope and may be required to coordinate nuclear and cytoplasmic signalling required for this integration. The onset and stop of Cdc13 nuclear export are remarkably abrupt, underscoring that  S. pombe  mitotic entry consists of several switch-like transitions over the course of minutes. Our findings add another instance to the various cyclin nuclear transport events known to occur at critical cell cycle transitions throughout eukaryotes.","doi":"10.1098/rsob.250199","authors":"Chethan SG, Rogers JM, Vijayakumari D, Williams W, Gligorovski V, Rahi SJ, Hauf S","authors_abbrev":"Chethan SG et al.","pubmed_publication_date":"Sep 2025","pubmed_entrez_date":"2025-09-16","publication_year":"2025","canto_session_key":"fd93ca0a6d946399","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-17 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD156","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29596531","title":"Insights into DNA substrate selection by APOBEC3G from structural, biochemical, and functional studies.","citation":"PLoS One 2018;13(3):e0195048","abstract":"Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3 (A3) proteins are a family of cytidine deaminases that catalyze the conversion of deoxycytidine (dC) to deoxyuridine (dU) in single-stranded DNA (ssDNA). A3 proteins act in the innate immune response to viral infection by mutating the viral ssDNA. One of the most well-studied human A3 family members is A3G, which is a potent inhibitor of HIV-1. Each A3 protein prefers a specific substrate sequence for catalysis-for example, A3G deaminates the third dC in the CCCA sequence motif. However, the interaction between A3G and ssDNA is difficult to characterize due to poor solution behavior of the full-length protein and loss of DNA affinity of the truncated protein. Here, we present a novel DNA-anchoring fusion strategy using the protection of telomeres protein 1 (Pot1) which has nanomolar affinity for ssDNA, with which we captured an A3G-ssDNA interaction. We crystallized a non-preferred adenine in the -1 nucleotide-binding pocket of A3G. The structure reveals a unique conformation of the catalytic site loops that sheds light onto how the enzyme scans substrate in the -1 pocket. Furthermore, our biochemistry and virology studies provide evidence that the nucleotide-binding pockets on A3G influence each other in selecting the preferred DNA substrate. Together, the results provide insights into the mechanism by which A3G selects and deaminates its preferred substrates and help define how A3 proteins are tailored to recognize specific DNA sequences. This knowledge contributes to a better understanding of the mechanism of DNA substrate selection by A3G, as well as A3G antiviral activity against HIV-1.","doi":"10.1371/journal.pone.0195048","authors":"Ziegler SJ, Liu C, Landau M, Buzovetsky O, Desimmie BA, Zhao Q, Sasaki T, Burdick RC, Pathak VK, Anderson KS, Xiong Y","authors_abbrev":"Ziegler SJ et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-03-30","publication_year":"2018","canto_session_key":"f6dcaef83c7b04c4","canto_annotation_status":"APPROVED","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_first_approved_date":"2020-01-22 14:43:41","canto_approved_date":"2020-01-22 14:43:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-01-22 14:31:24","canto_added_date":"2018-11-22 16:03:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-01-22","pdb_entries":[{"pdb_id":"6bwy","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A/A/B/B/E/E/G/G","position":"5-174"}],"title":"DNA substrate selection by APOBEC3G","entry_authors":"Ziegler SJ,Buzovetsky O","entry_authors_abbrev":"Ziegler SJ et al.","reference_uniquename":"PMID:29596531","experimental_method":"X-ray","resolution":"2.9"}]},{"uniquename":"GO_REF:0000008","title":"Gene Ontology annotation by the MGI curatorial staff, curated orthology","abstract":"The sequence conservation that permits the establishment of orthology between mouse and rat or mouse and human genes is a strong predictor of the conservation of function for the gene product across these species. Therefore, in instances where a mouse gene product has not been functionally characterized, but its human or rat orthologs have, Mouse Genome Informatics (MGI) curators append the GO terms associated with the orthologous gene(s) to the mouse gene. Only those GO terms assigned by experimental determination to the ortholog of the mouse gene will be adopted by MGI. GO terms that are assigned to the ortholog of the mouse gene computationally (i.e. IEA), will not be transferred to the mouse ortholog. The evidence code represented by this citation is Inferred by Sequence Orthology (ISO).","authors":"Mouse Genome Informatics scientific curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11333218","title":"Requirement for Msh6, but not for Swi4 (Msh3), in Msh2-dependent repair of base-base mismatches and mononucleotide loops in Schizosaccharomyces pombe.","citation":"Genetics 2001 May;158(1):65-75","abstract":"The msh6 mismatch repair gene of Schizosaccharomyces pombe was cloned, sequenced, and inactivated. Strains bearing all combinations of inactivated msh6, msh2, and swi4 (the S. pombe MSH3 ortholog) alleles were tested for their defects in mitotic and meiotic mismatch repair. Mitotic mutation rates were similarly increased in msh6 and msh2 mutants, both for reversion of a base-base substitution as well as of an insertion of one nucleotide in a mononucleotide run. Tetrad analysis and intragenic two-factor crosses revealed that meiotic mismatch repair was affected in msh6 to the same extent as in msh2 background. In contrast, loss of Swi4 likely did not cause a defect in mismatch repair, but rather resulted in reduced recombination frequency. Consistently, a mutated swi4 caused a two- to threefold reduction of recombinants in intergenic crosses, while msh2 and msh6 mutants were not significantly different from wild type. In summary, our study showed that Msh6 plays the same important role as Msh2 in the major mismatch repair pathway of S. pombe, while Swi4 rather functions in recombination.","authors":"Tornier C, Bessone S, Varlet I, Rudolph C, Darmon M, Fleck O","authors_abbrev":"Tornier C et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-03","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC285.16c","SPAC8F11.03","SPBC19G7.01c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23584455","title":"Regulation of Mus81-Eme1 Holliday junction resolvase in response to DNA damage.","citation":"Nat Struct Mol Biol 2013 May;20(5):598-603","abstract":"Structure-specific DNA endonucleases have critical roles during DNA replication, repair and recombination, yet they also have the potential for causing genome instability. Controlling these enzymes may be essential to ensure efficient processing of ad hoc substrates and to prevent random, unscheduled processing of other DNA structures, but it is unknown whether structure-specific endonucleases are regulated in response to DNA damage. Here, we uncover DNA damage-induced activation of Mus81-Eme1 Holliday junction resolvase in fission yeast. This new regulation requires both Cdc2(CDK1)- and Rad3(ATR)-dependent phosphorylation of Eme1. Mus81-Eme1 activation prevents gross chromosomal rearrangements in cells lacking the BLM-related DNA helicase Rqh1. We propose that linking Mus81-Eme1 DNA damage-induced activation to cell-cycle progression ensures efficient resolution of Holliday junctions that escape dissolution by Rqh1-TopIII while preventing unnecessary DNA cleavages.","doi":"10.1038/nsmb.2550","authors":"Dehé PM, Coulon S, Scaglione S, Shanahan P, Takedachi A, Wohlschlegel JA, Yates JR, Llorente B, Russell P, Gaillard PH","authors_abbrev":"Dehé PM et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-04-16","publication_year":"2013","canto_session_key":"c264f5ff5aab84a2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC2G11.12","SPAPB1E7.06c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11069657","title":"bgs2+, a sporulation-specific glucan synthase homologue is required for proper ascospore wall maturation in fission yeast.","citation":"Mol Microbiol 2000 Oct;38(2):308-21","abstract":"The formation of the ascospore cell wall of Schizosaccharomyces pombe requires the co-ordinated activity of enzymes involved in the biosynthesis of its components, such as glucans. We have cloned the bgs2+ gene. bgs2+ belongs to the glucan synthase family of S. pombe and is homologous to the Saccharomyces cerevisiae FKS1 and FKS2 genes. Deletion or overexpression of this gene does not lead to any apparent defect during vegetative growth, but homozygous bgs2Delta diploids do show a sporulation defect. Although meiosis takes place normally, ascospores are unable to mature, and their wall differs from that of wild-type ascospores. Moreover, bgs2Delta zygotes were not able to release ascospores spontaneously, and the ascospores were unable to germinate. We show that expression of bgs2+ is restricted to sporulation and that a bgs2-green fluorescent protein (GFP) fusion protein localizes to the ascospore envelope. The glucan synthase activity in sporulating diploids bearing a bgs2 deletion was diminished in comparison with that of the wild-type diploids, a fact that underscores the importance of the bgs2+ gene and glucan synthesis for the proper formation and maturation of the ascospore wall.","authors":"Martín V, Ribas JC, Carnero E, Durán A, Sánchez Y","authors_abbrev":"Martín V et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-11-09","publication_year":"2000","canto_session_key":"67f41f34003a2a4c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-09 08:21:15","canto_approved_date":"2026-03-31 09:29:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-08 14:52:32","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPAC24C9.07c","SPCC1840.02c","SPAC19B12.03","SPAC13G6.12c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2015-10-09"},{"uniquename":"PMID:9781874","title":"Characterization of the geranylgeranyl transferase type I from Schizosaccharomyces pombe.","citation":"Mol Microbiol 1998 Sep;29(6):1357-67","abstract":"The Schizosaccharomyces pombe cwg2+ gene encodes the beta-subunit of geranylgeranyl transferase I (GGTase I), which participates in the post-translational C-terminal modification of several small GTPases, allowing their targeting to the membrane. Using the two-hybrid system, we have identified the cwp1+ gene that encodes the alpha-subunit of the GGTase I. cwp1p interaction with cwg2p was mapped to amino acids 1-244 or 137-294 but was not restricted to amino acids 137-244. The genomic cwp1+ was isolated and sequenced. It has two putative open reading frames of 677 and 218 bp, separated by a 51 bp intron. The predicted amino acid sequence shows significant similarity to GGTase I alpha-subunits from different species. However, complementation of Saccharomyces cerevisiae ram2-1 mutant by overexpressing the cwp1+ gene was not possible. Expression of both cwg2+ and cwp1+ in Escherichia coli allowed 'in vitro' reconstitution of the GGTase I activity. S. pombe cells expressing the mutant enzyme containing the cwg2-1 mutation do not grow at 37 degrees C, but the growth defect can be suppressed by the addition of sorbitol. Actin immunostaining of the cwg2-1 mutant strain grown at 37 degrees C showed an abnormal distribution of actin patches. The cwg2-1 mutation was identified as a guanine to adenine substitution at nucleotide 604 of the coding region, originating the change A202T in the cwg2p. Deletion of the cwg2 gene is lethal; delta cwg2 spores can divide two or three times before losing viability. Most cells have aberrant morphology and septation defects. Overexpression of the rho1G15VC199R double-mutant allele in S. pombe caused loss of polarity but was not lethal and did not render the (1-3)beta-D-glucan synthase activity independent of GTP. Therefore, geranylgeranylation of rho1p is required for the appropriate function of this GTPase.","authors":"Arellano M, Coll PM, Yang W, Duran A, Tamanoi F, Perez P","authors_abbrev":"Arellano M et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-10-22","publication_year":"1998","canto_session_key":"b7974adcd92cb4d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-27 21:14:07","canto_approved_date":"2022-06-11 08:36:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-05 13:13:03","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.04","SPAC2E1P5.04c","SPAPB1A10.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-07-27"},{"uniquename":"PMID:31116668","title":"Fission yeast TRP channel Pkd2p localizes to the cleavage furrow and regulates cell separation during cytokinesis.","citation":"Mol Biol Cell 2019 Jul 15;30(15):1791-1804","abstract":"Force plays a central role in separating daughter cells during cytokinesis, the last stage of cell division. However, the mechanism of force sensing during cytokinesis remains unknown. Here we discovered that Pkd2p, a putative force-sensing transient receptor potential channel, localizes to the cleavage furrow during cytokinesis of the fission yeast,  Schizosaccharomyces pombe . Pkd2p, whose human homologues are associated with autosomal polycystic kidney disease, is an essential protein whose localization depends on the contractile ring and the secretory pathway. We identified and characterized a novel  pkd2  mutant  pkd2-81KD . The  pkd2  mutant cells show signs of osmotic stress, including temporary shrinking, paused turnover of the cytoskeletal structures, and hyperactivated mitogen-activated protein kinase signaling. During cytokinesis, although the contractile ring constricts more rapidly in the  pkd2  mutant than the wild-type cells (50% higher), the cell separation in the mutant is slower and often incomplete. These cytokinesis defects are also consistent with misregulated turgor pressure. Finally, the  pkd2  mutant exhibits strong genetic interactions with two mutants of the septation initiation network pathway, a signaling cascade essential for cytokinesis. We propose that Pkd2p modulates osmotic homeostasis and is potentially a novel regulator of cytokinesis.","doi":"10.1091/mbc.E18-04-0270","authors":"Morris Z, Sinha D, Poddar A, Morris B, Chen Q","authors_abbrev":"Morris Z et al.","pubmed_publication_date":"15 Jul 2019","pubmed_entrez_date":"2019-05-23","publication_year":"2019","canto_session_key":"f85b178fd2fdb4a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Qian Chen","canto_first_approved_date":"2019-06-05 08:13:43","canto_approved_date":"2026-01-31 14:27:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-24 18:22:52","canto_added_date":"2019-05-24 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":48,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Qian Chen","community_curator":true,"annotation_count":3,"orcid":"0000-0002-2768-6570","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.04c","SPBC428.13c","SPBC19G7.05c","SPAC1F7.03","SPAC24B11.11c","SPAC821.09","SPCC663.14c","SPCC1322.03","SPAC24B11.06c","SPCC645.05c","SPCC1840.02c","SPAC14C4.09"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2019-06-05"},{"uniquename":"PMID:17705537","title":"A new series of 3-alkyl phosphate derivatives of 4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidinedione as inhibitors of lumazine synthase: design, synthesis, and evaluation.","citation":"J Org Chem 2007 Sep 14;72(19):7176-84","abstract":"Lumazine synthase catalyzes the penultimate step in the biosynthesis of riboflavin. A homologous series of three pyrazolopyrimidine analogues of a hypothetical intermediate in the lumazine synthase-catalyzed reaction were synthesized and evaluated as lumazine synthase inhibitors. The key steps of the synthesis were C-5 deprotonation of 4-chloro-2,6-dimethoxypyrimidine, acylation of the resulting anion, and conversion of the product to a pyrazolopyrimidine with hydrazine. Alkylation of the pyrazolopyrimidine with a substituted ribityl iodide and deprotection of the ribityl chain afforded the final set of three products. All three compounds were extremely potent inhibitors of the lumazine synthases of Mycobacterium tuberculosis, Magnaporthe grisea, Candida albicans, and Schizosaccharomyces pombe lumazine synthase, with inhibition constants in the low nanomolar to subnanomolar range. Molecular modeling of one of the homologues bound to Mycobacterium tuberculosis lumazine synthase suggests that both the hypothetical intermediate in the lumazine synthase-catalyzed reaction pathway and the metabolically stable analogues bind similarly.","authors":"Zhang Y, Jin G, Illarionov B, Bacher A, Fischer M, Cushman M","authors_abbrev":"Zhang Y et al.","pubmed_publication_date":"14 Sep 2007","pubmed_entrez_date":"2007-08-21","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9483807","title":"Characterization of a branched-chain amino-acid aminotransferase from Schizosaccharomyces pombe.","citation":"Yeast 1998 Jan 30;14(2):189-94","abstract":"The Saccharomyces cerevisiae genes for the cytosolic and mitochondrial branched-chain amino-acid aminotransferases (BCAT) were isolated recently. These genes show significant homology to mammalian ECA39, originally isolated as a gene regulated by the c-myc oncogene. We now report the isolation of the Schizosaccharomyces pombe eca39/BCAT gene. The S. pombe protein shows 47-52% identity to other eukaryotic BCAT proteins isolated from S. cerevisiae, nematode, mouse and man. A genetic growth assay for BCAT activity was established using an S. cerevisiae strain disrupted in both BCAT isoenzymes. Consequently, the activity of the S. pombe BCAT was demonstrated by genetic and biochemical means. Possible applications of BCAT-encoding genes as selection markers in yeast transformation are proposed.","authors":"Eden A, Benvenisty N","authors_abbrev":"Eden A et al.","pubmed_publication_date":"30 Jan 1998","pubmed_entrez_date":"1998-03-04","publication_year":"1998","canto_session_key":"9a9713c2a4ad85d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-08-22 15:27:59","canto_approved_date":"2024-08-09 18:32:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-22 15:25:39","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-22"},{"uniquename":"PMID:14644438","title":"Cyclophilin sensitivity to sanglifehrin A can be correlated to the same specific tryptophan residue as cyclosporin A.","citation":"FEBS Lett 2003 Dec 04;555(2):335-40","abstract":"Sanglifehrin A (SFA) is a recently discovered immunosuppressant drug that shares its intracellular target with the major immunosuppressant drug cyclosporin A (CsA). Both bind to and inhibit the cyclophilins, a diverse family of proteins found throughout nature that share a conserved catalytic domain. Although they share this common protein target, the mechanism of action of the cyclophilin-SFA complex has been reported as distinct from that of the well-studied cyclophilin-CsA complex. The X-ray structure of a macrolide analogue of SFA's cyclic region complexed with cyclophilin A has recently been resolved, but this left the placement of the linear region of SFA unresolved. Using five cyclophilins from the fission yeast Schizosaccharomyces pombe, and a mutant of one of these proteins, SpCyp3-F128W, we have shown that the sensitivity of cyclophilins to SFA can be correlated to the same specific tryptophan residue that has previously been identified to correlate to CsA sensitivity, and that the tail of SFA may be responsible for mediating this sensitivity.","authors":"Pemberton TJ, Kay JE","authors_abbrev":"Pemberton TJ et al.","pubmed_publication_date":"04 Dec 2003","pubmed_entrez_date":"2003-12-04","publication_year":"2003","canto_session_key":"0adbb6982d555eb2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-22 15:27:53","canto_approved_date":"2023-09-29 20:14:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-22 15:27:45","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.03","SPBC1709.04c","SPBP8B7.25","SPAC57A10.03","SPAC1B3.03c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-10-22"},{"uniquename":"PMID:15356263","title":"The small subunit processome is required for cell cycle progression at G1.","citation":"Mol Biol Cell 2004 Nov;15(11):5038-46","abstract":"Without ribosome biogenesis, translation of mRNA into protein ceases and cellular growth stops. We asked whether ribosome biogenesis is cell cycle regulated in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, and we determined that it is not regulated in the same manner as in metazoan cells. We therefore turned our attention to cellular sensors that relay cell size information via ribosome biogenesis. Our results indicate that the small subunit (SSU) processome, a complex consisting of 40 proteins and the U3 small nucleolar RNA necessary for ribosome biogenesis, is not mitotically regulated. Furthermore, Nan1/Utp17, an SSU processome protein, does not provide a link between ribosome biogenesis and cell growth. However, when individual SSU processome proteins are depleted, cells arrest in the G1 phase of the cell cycle. This arrest was further supported by the lack of staining for proteins expressed in post-G1. Similarly, synchronized cells depleted of SSU processome proteins did not enter G2. This suggests that when ribosomes are no longer made, the cells stall in the G1. Therefore, yeast cells must grow to a critical size, which is dependent upon having a sufficient number of ribosomes during the G1 phase of the cell cycle, before cell division can occur.","authors":"Bernstein KA, Baserga SJ","authors_abbrev":"Bernstein KA et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-09-10","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32520628","title":"Microtubule nucleation promoters Mto1 and Mto2 regulate cytokinesis in fission yeast.","citation":"Mol Biol Cell 2020 Aug 01;31(17):1846-1856","abstract":"Microtubules of the mitotic spindle direct cytokinesis in metazoans but this has not been documented in fungi. We report evidence that microtubule nucleators at the spindle pole body help coordinate cytokinetic furrow formation in fission yeast. The temperature-sensitive  cps1-191  strain (Liu  et al. , 1999) with a D277N substitution in β-glucan synthase 1 (Cps1/Bgs1) was reported to arrest with an unconstricted contractile ring. We discovered that contractile rings in  cps1-191  cells constrict slowly and that an  mto2 S338N   mutation is required with the  bgs1 D277N  mutation to reproduce the  cps1-191  phenotype. Complexes of Mto2 and Mto1 with γ-tubulin regulate microtubule assembly. Deletion of Mto1 along with the  bgs1 D277N   mutation also gives the  cps1-191  phenotype, which is not observed in  mto2 S338N   or  mto1Δ  cells expressing  bgs1  + . Both  mto2 S338N   and  mto1Δ  cells nucleate fewer astral microtubules than normal and have higher levels of Rho1-GTP at the division site than wild-type cells. We report multiple conditions that sensitize  mto1Δ  and  mto2 S338N   cells to furrow ingression phenotypes.","doi":"10.1091/mbc.E19-12-0686","authors":"Dundon SER, Pollard TD","authors_abbrev":"Dundon SER et al.","pubmed_publication_date":"01 Aug 2020","pubmed_entrez_date":"2020-06-11","publication_year":"2020","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-06-12 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21357674","title":"Autoregulation of convergent RNAi genes in fission yeast.","citation":"Genes Dev 2011 Mar 15;25(6):556-68","abstract":"RNAi plays a central role in the regulation of eukaryotic genes. In Schizosaccharomyces pombe fission yeast, RNAi involves the formation of siRNA from dsRNA that acts to establish and maintain heterochromatin over centromeres, telomeres, and mating loci. We showed previously that transient heterochromatin also forms over S. pombe convergent genes (CGs). Remarkably, most RNAi genes are themselves convergent. We demonstrate here that transient heterochromatin formed by the RNAi pathway over RNAi CGs leads to their autoregulation in G1-S. Furthermore, the switching of RNAi gene orientation from convergent to tandem causes loss of their G1-S down-regulation. Surprisingly, yeast mutants with tandemized dcr1, ago1, or clr4 genes display aberrant centromeric heterochromatin, which results in abnormal cell morphology. Our results emphasize the significance of gene orientation for correct RNAi gene expression, and suggest a role for cell cycle-dependent formation of RNAi CG heterochromatin in cellular integrity.","doi":"10.1101/gad.618611","authors":"Gullerova M, Moazed D, Proudfoot NJ","authors_abbrev":"Gullerova M et al.","pubmed_publication_date":"15 Mar 2011","pubmed_entrez_date":"2011-03-02","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9034336","title":"Fission yeast pheromone blocks S-phase by inhibiting the G1 cyclin B-p34cdc2 kinase.","citation":"EMBO J 1997 Feb 03;16(3):534-44","abstract":"Yeast pheromones block cell cycle progression in G1 in order to prepare mating partners for conjugation. We have investigated the mechanism underlying pheromone-induced G1 arrest in the fission yeast Schizosaccharomyces pombe. We find that the G1-specific transcription factor p65cdc10-p72res1/sct1 which controls the expression of S-phase genes is fully activated in pheromone, unlike the analogous control in budding yeast. In contrast, the G1 function of p34cdc2 acting after activation of the G1-specific transcription is blocked. Pheromone inhibits the p34cdc2 kinase associated with both the G1-specific B-type cyclin p45cig2 and the B-type cyclin p56cdc13 and overexpression of p45cig2 or p47cdc13delta90 overcomes the pheromone-induced G1 arrest. G1 arrest is compromised in enlarged cells. We suggest that onset of S-phase is controlled by pheromone inhibiting the B-cyclin-associated kinase in G1, and that increasing cell size contributes to the mechanism for pheromone adaptation. Thus, pheromone in fission and budding yeast acts similarly in inhibiting the G1 cyclin-dependent kinase (CDK), but differs in its effects on the G1/S transcriptional control, suggesting that inhibition of CDKs may be a more general mechanism for the control of G1 progression compared with G1/S transcriptional control.","authors":"Stern B, Nurse P","authors_abbrev":"Stern B et al.","pubmed_publication_date":"03 Feb 1997","pubmed_entrez_date":"1997-02-03","publication_year":"1997","canto_session_key":"5f9739dd2f7a875d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-28 22:23:11","canto_approved_date":"2026-04-08 07:39:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-01 19:37:17","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB2B4.03","SPAC24H6.05","SPBC582.03","SPBC725.16","SPBC336.12c","SPBC11B10.09","SPBC14C8.07c","SPCC1795.06"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2018-04-28"},{"uniquename":"PMID:27037075","title":"Transformation of Schizosaccharomyces pombe: Lithium Acetate/ Dimethyl Sulfoxide Procedure.","citation":"Cold Spring Harb Protoc 2016 Apr 01;2016(4):pdb.prot090969","abstract":"Transformation ofSchizosaccharomyces pombewith DNA requires the conditioning of cells to promote DNA uptake followed by cell growth under conditions that select and maintain the plasmid or integration event. The three main methodologies are electroporation, treatment with lithium cations, and transformation of protoplasts. The lithium acetate method described here is widely used because it is simple and reliable.","doi":"10.1101/pdb.prot090969","authors":"Murray JM, Watson AT, Carr AM","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"01 Apr 2016","pubmed_entrez_date":"2016-04-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-04-04 00:15:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41346620","title":"Yeast vaccine production platform for human and animal infectious diseases.","citation":"Front Immunol 2025;16:1697177","abstract":"Yeasts have contributed to human and animal health through functional antigen production for vaccine formulations. Some yeast-made vaccines have become a reality for humankind because they have reached commercialization (hepatitis B, HPV, and tick parasitosis). Many other vaccine prototypes are under preclinical and clinical evaluations, hoping for their usage soon. Currently, genomes, genetic modification techniques, and industrial vaccine manufacturing have been successfully developed for  Saccharomyces cerevisiae ,  Komagataella phaffii (formerly Pichia pastoris) , and  Hansenula polymorpha . Moreover, several yeast species are under research as prospects for vaccine production systems, such as  Kluyveromyces lactis, Yarrowia lipolytica, Schizosaccharomyces pombe, Saccharomyces boulardii , and  Komagataella phaffii . This review was mainly focused on commercial human and animal vaccines, describing and discussing genetic engineering tools, downstream antigen purification processes, GMP according to regulatory issues, and identifying challenges and future directions on the use of yeast as a vaccine production platform to fight against infectious diseases.","doi":"10.3389/fimmu.2025.1697177","authors":"Ramos-Vega A, Monreal-Escalante E, Bañuelos-Hernández B, Angulo M, Trujillo E, Angulo C","authors_abbrev":"Ramos-Vega A et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-12-05","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-12-06 00:25:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11481672","title":"High efficiency transformation of Schizosaccharomyces pombe pretreated with thiol compounds by electroporation.","citation":"Yeast 2001 Aug;18(11):1015-21","abstract":"A highly efficient method for transformation of the fission yeast Schizosaccharomyces pombe by electroporation has been developed. Significantly higher transformation efficiency was obtained when intact cells grown in SD medium (0.67% Bacto yeast nitrogen base without amino acids, 2% glucose) were pretreated with thiol compounds before an electric pulse was applied to the cells. Among the thiol compounds tested, dithiothreitol (DTT) was the most effective for pretreatment. A high transformation efficiency was obtained when the cells were pretreated with 25 mM DTT at 30 degrees C for 15 min in an osmotically adjusted buffer, since the cells were sensitive to osmotic pressure. It was important to exclude glucose from the DTT pretreatment buffer, as it caused a drastic decrease in efficiency. The optimal cell concentration and amount of DNA during the electric pulse were 1x10(9) cells/ml and 10 ng, respectively. The maximum transformation efficiency, 1.2x10(7) transformants/microg plasmid DNA, was obtained when an electric pulse of 11.0 kV/cm was applied for 5 ms. Furthermore, the high competency of cells pretreated with DTT was maintained by freezing them in a non-permeating cryoprotectant such as sorbitol.","authors":"Suga M, Hatakeyama T","authors_abbrev":"Suga M et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-08-02","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9974219","title":"Enhancement of neutral trehalase activity by oxidative stress in the fission yeast Schizosaccharomyces pombe.","citation":"Fungal Genet Biol 1998 Nov;25(2):79-86","abstract":"Addition of hydrogen peroxide, menadione, or plumbagin to growing cultures of the fission yeast Schizosaccharomyces pombe increased trehalase activity. The effect was inhibited only slightly in the presence of cycloheximide, indicating that the stimulation of trehalase triggered by oxidative stress is mostly due to posttranscriptional activation. Northern blot analysis of trehalase mRNA level revealed that oxidative stress also induces a moderate rise in transcription of trehalase. Mutants disrupted in genes encoding elements of the mitogen-activated protein kinase (MAPK) cascade showed a reduced increase in trehalase activity upon oxidative challenge, which was coincident with a block in transcription of trehalase. Taken together, the results support the idea that the enhancement of trehalase by oxidative stress is due to enzyme activation (via the Pka1/Sck1 phosphorylation pathway) and induction of trehalase mRNA (via the MAPK signaling pathway). In spite of the trehalase increase, a net accumulation of trehalose was noticed during the oxidative stress.","authors":"Fernández J, Soto T, Franco A, Vicente-Soler J, Cansado J, Gacto M","authors_abbrev":"Fernández J et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1999-02-12","publication_year":"1998","canto_session_key":"b6cb6d3911a0b608","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-12 10:31:56","canto_approved_date":"2023-04-05 13:15:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-19 12:09:48","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC887.10","SPBC409.07c","SPBC29B5.01","SPBC660.07","SPAC9G1.02"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-02-12"},{"uniquename":"PMID:8343962","title":"Fission yeast cut5+, required for S phase onset and M phase restraint, is identical to the radiation-damage repair gene rad4+.","citation":"Cell 1993 Jul 30;74(2):383-93","abstract":"Fission yeast cut5 mutants cause cytokinesis in the absence of normal nuclear division. We show here that cut5+ is required for both the onset of S phase and the restraint of M phase before the completion of S phase. The primary defects in cut5 mutants occur prior to S phase, but cells suffer lethal damage during M phase. Mitosis and cytokinesis occur in the presence of hydroxyurea or in the double mutant cdc10-cut5 (the cdc10 mutation alone blocks progression from G1 to S). Gene cloning shows that cut5+ is identical to the fission yeast rad4+ gene, which is similar to human XRCC1. The rad4+/cut5+ gene is unique in its positive role for replication/repair and in its negative role for mitosis/cytokinesis. We propose a single/twin chromatid marking model for rad4+/cut5+ function in cell cycle control.","authors":"Saka Y, Yanagida M","authors_abbrev":"Saka Y et al.","pubmed_publication_date":"30 Jul 1993","pubmed_entrez_date":"1993-07-30","publication_year":"1993","canto_session_key":"d5b7ba156ee750c8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-01 09:36:01","canto_approved_date":"2026-01-29 13:24:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-12 17:11:07","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPAC23C4.18c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-06-01"},{"uniquename":"PMID:10223994","title":"Accumulation of trehalose by overexpression of tps1, coding for trehalose-6-phosphate synthase, causes increased resistance to multiple stresses in the fission yeast schizosaccharomyces pombe.","citation":"Appl Environ Microbiol 1999 May;65(5):2020-4","abstract":"Recent studies have shown that heat shock proteins and trehalose synthesis are important factors in the thermotolerance of the fission yeast Schizosaccharomyces pombe. We examined the effects of trehalose-6-phosphate (trehalose-6P) synthase overexpression on resistance to several stresses in cells of S. pombe transformed with a plasmid bearing the tps1 gene, which codes for trehalose-6P synthase, under the control of the strong thiamine-repressible promoter. Upon induction of trehalose-6P synthase, the elevated levels of intracellular trehalose correlated not only with increased tolerance to heat shock but also with resistance to freezing and thawing, dehydration, osmostress, and toxic levels of ethanol, indicating that trehalose may be the stress metabolite underlying the overlap in induced tolerance to these stresses. Among the isogenic strains transformed with this construct, one in which the gene coding for the trehalose-hydrolyzing enzyme, neutral trehalase, was disrupted accumulated trehalose to a greater extent and was more resistant to the above stresses. Increased trehalose concentration is thus a major determinant of the general stress protection response in S. pombe.","authors":"Soto T, Fernandez J, Vicente-Soler J, Cansado J, Gacto M","authors_abbrev":"Soto T et al.","pubmed_publication_date":"May 1999","pubmed_entrez_date":"1999-05-01","publication_year":"1999","canto_session_key":"b0116284c3e493a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-19 14:53:19","canto_approved_date":"2024-12-04 10:30:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-08-24 14:17:10","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC328.03","SPBC660.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-19"},{"uniquename":"PMID:12867051","title":"COP9 signalosome: a provider of DNA building blocks.","citation":"Curr Biol 2003 Jul 15;13(14):R565-7","abstract":"In fission yeast, the COP9 signalosome is required to activate ribonucleotide reductase for DNA synthesis. This is mediated via the ubiquitin ligase Pcu4, activation of which leads to degradation of the scaffold protein Spd1, which anchors the small ribonucleotide reductase subunit in the nucleus away from the large subunit in the cytoplasm.","authors":"Nielsen O","authors_abbrev":"Nielsen O","pubmed_publication_date":"15 Jul 2003","pubmed_entrez_date":"2003-07-18","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42248458","title":"Ago1 is required for the regulation of mitochondrial translation under heat stress in S. pombe.","citation":"J Biol Chem 2026 Jun 04;:113235","abstract":"Mitochondrial protein synthesis is a critical component of OXPHOS complexes, vital for both mammals and Schizosaccharomyces pombe. In our study, we investigated the effect of heat stress on mitochondria, analyzed the mitochondrial proteome and found that during heat stress, the translation of all mtDNA-encoded transcripts was impaired, leading to a reduction in the steady-state levels of mtDNA-encoded proteins, suggesting that heat stress plays a general role in mitochondrial protein synthesis. We also found that heat stress affects the association of mitochondrial translation initiation factors to mitoribosomal small subunits. Interestingly, ago1 deletion compensates for the heat-induced disruption of the interaction between mitochondrial translation initiation factor and mitoribosomes, leading to partial recovery of both translation and steady-state levels of mtDNA-encoded proteins in S. pombe. Under heat stress, Ago1 accumulates in the mitochondrial matrix. C-terminal truncation ablates this localization and abolishes rescue of translational suppression, confirming mitochondrial targeting is essential for regulatory function. Furthermore, our data demonstrate that Ago1's small RNA-loading related N-terminal domain is required for heat-induced translational suppression and that Ago1 physically engages with mitochondrial RNAs, collectively indicating potential RNA interference (RNAi) activity within mitochondria. These findings provide insight into the regulation of mitochondrial protein synthesis in heat stress.","doi":"10.1016/j.jbc.2026.113235","authors":"Yu M, Xu Y, Lu Y, Li M, Yao Y, Feng G, Huang Y, Shang J","authors_abbrev":"Yu M et al.","pubmed_publication_date":"04 Jun 2026","pubmed_entrez_date":"2026-06-05","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-06 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2494655","title":"Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species.","citation":"Proc Natl Acad Sci U S A 1989 Mar;86(6):1934-8","abstract":"The DNA polymerase chain reaction was developed for in vitro amplification of specific DNA sequences, and it has been used for a wide variety of purposes in several fields. We have developed an application of the polymerase chain reaction that is useful for the isolation of partial cDNA or genomic clones of conserved genes. We used this technique to clone the gene encoding the iron protein subunit (27 kDa) of succinate dehydrogenase (EC 1.3.5.1) from several species, including human, rat, Drosophila melanogaster, Arabidopsis thaliana, Schizosaccharomyces pombe, and Saccharomyces cerevisiae. Mixed oligonucleotide primers corresponding to two conserved regions of the protein were used in conjunction with genomic and cDNA templates in the reaction. The primers contained all possible nucleotide combinations that could encode the corresponding peptide sequences. These oligonucleotide mixtures contained 262,144 (2(18] and 8192 (2(13] unique sequences, respectively. Use of the polymerase chain reaction for homology probing allows one to utilize more complex mixtures of oligonucleotides as probes than is possible with filter hybridization screening techniques. In addition, the polymerase chain reaction offers the advantage of synthesizing the DNA product directly, in some cases obviating the need to construct cDNA or genomic libraries. This application of the polymerase chain reaction should be useful not only for the identification of conserved genes in a variety of species but also for the isolation of previously unknown members of gene families.","authors":"Gould SJ, Subramani S, Scheffler IE","authors_abbrev":"Gould SJ et al.","pubmed_publication_date":"Mar 1989","pubmed_entrez_date":"1989-03-01","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28799013","title":"Phospho-mimicking Atf1 mutants bypass the transcription activating function of the MAP kinase Sty1 of fission yeast.","citation":"Curr Genet 2018 Feb;64(1):97-102","abstract":"Stress-dependent activation of signaling cascades is often mediated by phosphorylation events, but the exact nature and role of these phosphorelays are frequently poorly understood. Here, we review which are the consequences of the stress-dependent phosphorylation of a transcription factor on gene activation. In fission yeast, the MAP kinase Sty1 is activated upon several environmental hazards and promotes cell adaptation and survival, greatly through activation of a gene program mediated by the transcription factor Atf1. Although described decades ago, the role of the phosphorylation of Atf1 by Sty1 is still a matter of debate. We present here a brief review of recent data, obtained through the characterization of several phosphorylation mutant derivatives of Atf1, demonstrating that Atf1 phosphorylation does not stabilize the factor nor stimulates its binding to DNA. Rather, it provides a structural platform of interaction with the transcriptional machinery. Based on these findings, future work will establish how this phosphorylated trans-activation domain promotes the massive gene expression shift allowing cellular adaptation to stress.","doi":"10.1007/s00294-017-0730-7","authors":"Sánchez-Mir L, Salat-Canela C, Paulo E, Carmona M, Ayté J, Oliva B, Hidalgo E","authors_abbrev":"Sánchez-Mir L et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2017-08-12","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-08-13 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC29B5.01"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:15937127","title":"The fission yeast Schizosaccharomyces pombe has two importin-alpha proteins, Imp1p and Cut15p, which have common and unique functions in nucleocytoplasmic transport and cell cycle progression.","citation":"Genetics 2005 Sep;171(1):7-21","abstract":"The nuclear import of classical nuclear localization signal-containing proteins depends on importin-alpha transport receptors. In budding yeast there is a single importin-alpha gene and in higher eukaryotes there are multiple importin-alpha-like genes, but in fission yeast there are two: the previously characterized cut15 and the more recently identified imp1. Like other importin-alpha family members, Imp1p supports nuclear protein import in vitro. In contrast to cut15, imp1 is not essential for viability, but imp1delta mutant cells exhibit a telophase delay and mild temperature-sensitive lethality. Differences in the cellular functions that depend on Imp1p and Cut15p indicate that they each have unique physiological roles. They also have common roles because the imp1delta and the cut15-85 temperature-sensitive mutations are synthetically lethal; overexpression of cut15 partially suppresses the temperature sensitivity, but not the mitotic delay in imp1delta cells; and overexpression of imp1 partially suppresses the mitotic defect in cut15-85 cells but not the loss of viability. Both Imp1p and Cut15p are required for the efficient nuclear import of both an SV40 nuclear localization signal-containing reporter protein and the Pap1p component of the stress response MAP kinase pathway. Imp1p and Cut15p are essential for efficient nuclear protein import in S. pombe.","authors":"Umeda M, Izaddoost S, Cushman I, Moore MS, Sazer S","authors_abbrev":"Umeda M et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-06-07","publication_year":"2005","canto_session_key":"5b1cec4b5c194281","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-26 18:05:59","canto_approved_date":"2026-01-30 13:35:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-22 16:03:53","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.08c","SPCC962.03c","SPAC1783.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-01-26"},{"uniquename":"PMID:1435723","title":"Functional conservation between Schizosaccharomyces pombe ste8 and Saccharomyces cerevisiae STE11 protein kinases in yeast signal transduction.","citation":"Mol Gen Genet 1992 Oct;235(1):122-30","abstract":"In fission yeast (Schizosaccharomyces pombe), the mat1-Pm gene, which is required for entry into meiosis, is expressed in response to a pheromone signal. Cells carrying a mutation in the ste8 gene are unable to induce transcription of mat1-Pm in response to pheromone, suggesting that the ste8 gene product functions in the signal transduction pathway. The ste8+ gene encodes a 659 amino acid putative protein kinase, which is identical to the previously identified byr2 suppressor of the ras1 defect. Furthermore, ste8+ is highly homologous to the Saccharomyces cerevisiae STE11 gene, which functions in signal transduction in budding yeast. Expression of the S. cerevisiae STE11 gene in S. pombe ste8 mutants restores the ability to transcribe mat1-Pm in response to pheromone. Also, such cells become capable of conjugation and sporulation. When mat1-Pm is artifically expressed from a heterologous promoter, ste8 mutant cells will enter meiosis. This demonstrates that the meiotic defect of ste8 mutants is due to the absence of the mat1-Pm gene product.","authors":"Styrkársdóttir U, Egel R, Nielsen O","authors_abbrev":"Styrkársdóttir U et al.","pubmed_publication_date":"Oct 1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_session_key":"b5aa547b2e76978f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-19 06:40:33","canto_approved_date":"2026-04-08 07:12:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-26 09:52:13","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1D7.05","SPBC32C12.02","SPMTR.02"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-05-19"},{"uniquename":"PMID:2226803","title":"The RNA component of RNase P in Schizosaccharomyces species.","citation":"FEBS Lett 1990 Oct 01;271(1-2):189-93","abstract":"In the fission yeast Schizosaccharomyces pombe, the enzyme RNAse P copurifies with two RNAs, K1- and K2-RNA, which are identical except for their termini [1] and which are encoded by a single gene [2]. We have undertaken the cloning of the K-RNA genes in related organisms in order to gain comparative structural information. Because the K-RNA sequence is poorly conserved across species, we have cloned the K-RNA genes in the Schizosaccharomyces species S. malidevorans, S. japonicus, S. versatilis, and S. octosporus. Of the 4 species, only S. octosporus contains a K-RNA gene different from that in S. pombe; the gene diverges by 20%. Based on the two sequences, nuclease protection data and computer analysis, we have proposed a secondary structure model for the K-RNA. Northern analysis shows the K-RNA genes in all four Schizosaccharomyces species to be expressed as two RNAs, as in S. pombe.","authors":"Zimmerly S, Gamulin V, Burkard U, Söll D","authors_abbrev":"Zimmerly S et al.","pubmed_publication_date":"01 Oct 1990","pubmed_entrez_date":"1990-10-01","publication_year":"1990","canto_session_key":"5e2d7e4c46cee11e","canto_annotation_status":"APPROVED","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 14:00:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-20 13:59:58","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.128"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:10922478","title":"Bgs2p, a 1,3-beta-glucan synthase subunit, is essential for maturation of ascospore wall in Schizosaccharomyces pombe.","citation":"FEBS Lett 2000 Jul 28;478(1-2):105-8","abstract":"Previously we have reported that Drc1p/Cps1p, a 1,3-beta-glucan synthase subunit, is essential for division septum assembly in Schizosaccharomyces pombe. In this report, we present evidence that S. pombe Bgs2p, a 1,3-beta-glucan synthase that shows 56% identity to Drc1p/Cps1p, is essential for maturation of ascospore wall in S. pombe, but is not required for vegetative growth. Diploid cells homozygous for the bgs2-null mutation, as well as homothallic bgs2-null mutant haploids undergo meiosis normally. However, a 1, 3-beta-glucan containing spore wall is not assembled in these cells. The spores resulting from meiosis of a bgs2-null mutant lyse upon release from the ascus and are therefore inviable. Using a green fluorescent protein-tagged Bgs2p, we demonstrate that Bgs2p is localized at the periphery of the ascospores during meiosis and sporulation. However, Bgs2p is not detected in vegetative cells. We conclude that Bgs2p is required for 1,3-beta-glucan synthesis during ascospore wall maturation.","authors":"Liu J, Tang X, Wang H, Balasubramanian M","authors_abbrev":"Liu J et al.","pubmed_publication_date":"28 Jul 2000","pubmed_entrez_date":"2000-08-03","publication_year":"2000","canto_session_key":"39eb86b2f670c330","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-01 17:24:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-01 17:24:44","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24C9.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-01"},{"uniquename":"PMID:9700395","title":"Education and research: where are we going?","citation":"Aust Vet J 1998 Jul;76(7):459","abstract":"","authors":"Niethe G","authors_abbrev":"Niethe G","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-08-13","publication_year":"1998","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G4.05c","SPAC1556.02c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:18535234","title":"Molecular biology. Refined view of the ends.","citation":"Science 2008 Jun 06;320(5881):1301-2","abstract":"","doi":"10.1126/science.1159104","authors":"Bianchi A, Shore D","authors_abbrev":"Bianchi A et al.","pubmed_publication_date":"06 Jun 2008","pubmed_entrez_date":"2008-06-07","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010974","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3709687","title":"A second growth state for Schizosaccharomyces pombe.","citation":"Exp Cell Res 1986 Jul;165(1):243-54","abstract":"The kinetics of volume increase in individual cells of Schizosaccharomyces pombe were determined by phase microscopy at osmolalities lower than those reported in the literature. At the highest osmolality, 550 mmol/kg, all cells followed a biphasic pattern of growth, in which cell volumes increased to their maximum values approximately four-fifths of the way through the growth cycle. At lower osmolalities (400-420 mmol/kg), many or most of the cells followed a different growth pattern, with a linear increase in cell volume throughout the cycle. The following evidence indicates that a different regulatory mechanism is responsible for the linear growth pattern: (1) Regulation of cell length and diameter differed for the two cases. During biphasic growth, cell length also increased biphasically and cell diameters remained essentially constant during the cycle, whereas during linear growth, both cell length and diameter increased linearly until formation of the cell plate very late in cycle. (2) The two different growth states were observed for cells growing on two very different kinds of medium. (3) Frequency distributions of the two growth patterns showed that there were two distinct groups of growing cells, with and without a cell volume plateau; these results rule out a single growth state in which plateaus are graded from large to infinitesimally small. (4) Linear regressions fitted to the data for linear growth did not differ significantly from the theoretical model for linear growth without a terminal plateau. These results reveal the operation of a second regulatory system for cell growth in S. pombe at osmolalities closer to those in liquid medium. The occurrence of transitions between the two growth states in successive generations and the agreement between several growth parameters for the two modes suggest that the growth states are closely related.","authors":"Kubitschek HE, Clay KB","authors_abbrev":"Kubitschek HE et al.","pubmed_publication_date":"Jul 1986","pubmed_entrez_date":"1986-07-01","publication_year":"1986","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20349228","title":"3D nanoscale imaging of the yeast, Schizosaccharomyces pombe, by full-field transmission X-ray microscopy at 5.4 keV.","citation":"Anal Bioanal Chem 2010 Jul;397(6):2117-21","abstract":"Three-dimensional (3D) nanoscale structures of the fission yeast, Schizosaccharomyces pombe, can be obtained by full-field transmission hard X-ray microscopy with 30 nm resolution using synchrotron radiation sources. Sample preparation is relatively simple and the samples are portable across various imaging environments, allowing for high-throughput sample screening. The yeast cells were fixed and double-stained with Reynold's lead citrate and uranyl acetate. We performed both absorption contrast and Zernike phase contrast imaging on these cells in order to test this method. The membranes, nucleus, and subcellular organelles of the cells were clearly visualized using absorption contrast mode. The X-ray images of the cells could be used to study the spatial distributions of the organelles in the cells. These results show unique structural information, demonstrating that hard X-ray microscopy is a complementary method for imaging and analyzing biological samples.","doi":"10.1007/s00216-010-3617-8","authors":"Chen J, Yang Y, Zhang X, Andrews JC, Pianetta P, Guan Y, Liu G, Xiong Y, Wu Z, Tian Y","authors_abbrev":"Chen J et al.","pubmed_publication_date":"Jul 2010","pubmed_entrez_date":"2010-03-30","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17287531","title":"Valproic acid affects membrane trafficking and cell-wall integrity in fission yeast.","citation":"Genetics 2007 Apr;175(4):1695-705","abstract":"Valproic acid (VPA) is widely used to treat epilepsy and manic-depressive illness. Although VPA has been reported to exert a variety of biochemical effects, the exact mechanisms underlying its therapeutic effects remain elusive. To gain further insights into the molecular mechanisms of VPA action, a genetic screen for fission yeast mutants that show hypersensitivity to VPA was performed. One of the genes that we identified was vps45+, which encodes a member of the Sec1/Munc18 family that is implicated in membrane trafficking. Notably, several mutations affecting membrane trafficking also resulted in hypersensitivity to VPA. These include ypt3+ and ryh1+, both encoding a Rab family protein, and apm1+, encoding the mu1 subunit of the adaptor protein complex AP-1. More importantly, VPA caused vacuolar fragmentation and inhibited the glycosylation and the secretion of acid phosphatase in wild-type cells, suggesting that VPA affects membrane trafficking. Interestingly, the cell-wall-damaging agents such as micafungin or the inhibition of calcineurin dramatically enhanced the sensitivity of wild-type cells to VPA. Consistently, VPA treatment of wild-type cells enhanced their sensitivity to the cell-wall-digesting enzymes. Altogether, our results suggest that VPA affects membrane trafficking, which leads to the enhanced sensitivity to cell-wall damage in fission yeast.","authors":"Miyatake M, Kuno T, Kita A, Katsura K, Takegawa K, Uno S, Nabata T, Sugiura R","authors_abbrev":"Miyatake M et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-02-09","publication_year":"2007","canto_session_key":"4e67e48d8c2b435b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-06-25 22:32:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-12 09:13:53","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.11","SPBP16F5.07","SPAC4C5.02c","SPAC2G11.03c","SPBP4H10.04","SPAC4G8.13c","SPAC18G6.03","SPAC19G12.10c"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2014-06-12"},{"uniquename":"PMID:22036784","title":"Purification and functional inactivation of the fission yeast MCM(MCM-BP) complex.","citation":"FEBS Lett 2011 Dec 15;585(24):3850-5","abstract":"The MCM (mini-chromosome maintenance) complex is the core of the eukaryotic replicative helicase and comprises six proteins, Mcm2-Mcm7. In humans, a variant form of the complex has Mcm2 replaced by the MCM-BP protein. Recent results suggest that a similar complex exists in fission yeast with an essential role in DNA replication and cell cycle progression. Here, we describe the purification and subunit composition of the fission yeast MCM(Mcb1) complex. Using newly generated temperature-sensitive alleles, we show that loss of MCM(Mcb1) function leads to accumulation of DNA damage, checkpoint activation and cell cycle arrest, and provide evidence for a role for MCM(Mcb1) in meiosis.","doi":"10.1016/j.febslet.2011.10.033","authors":"Li JJ, Schnick J, Hayles J, MacNeill SA","authors_abbrev":"Li JJ et al.","pubmed_publication_date":"15 Dec 2011","pubmed_entrez_date":"2011-11-01","publication_year":"2011","canto_session_key":"bf459e95570deb15","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-06-02 11:37:23","canto_approved_date":"2022-02-03 20:19:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-24 09:54:34","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC1687.04","SPAC1B2.05","SPAC30D11.10","SPCC1682.02c","SPBC25D12.03c","SPBC4.04c","SPCC16A11.17","SPBC211.04c","SPCC1259.13"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2017-06-02"},{"uniquename":"PMID:30389790","title":"Abrogation of glucosidase I-mediated glycoprotein deglucosylation results in a sick phenotype in fission yeasts: Model for the human MOGS-CDG disorder.","citation":"J Biol Chem 2018 Dec 28;293(52):19957-19973","abstract":"Glucosidase I (GI) removes the outermost glucose from protein-linked Glc 3 Man 9 GlcNAc 2  (G3M9) in the endoplasmic reticulum (ER). Individuals with congenital disorders of glycosylation MOGS-CDG bear mutations in the GI-encoding gene ( gls1 ). Although GI absence has been reported to produce lethality in  Schizosaccharomyces pombe  yeasts, here we obtained two viable Δ gls1  mutants, one with a very sick but not lethal phenotype (Δ gls1-S ) and the other with a healthier one (Δ gls1-H ). The sick strain displayed only G3M9 as an ER protein-linked oligosaccharide, whereas the healthier strain had both G3M9 and Man 9 GlcNAc 2  The lipid-linked oligosaccharide patterns of the two strains revealed that the most abundantly formed glycans were G3M9 in Δ gls1-S  and Glc 2 Man 9 GlcNAc 2  in Δ gls1-H , suggesting reduced Alg10p glucosyltransferase activity in the Δ gls1-H  strain. A mutation in the  alg10  +  gene was indeed observed in this strain. Our results indicated that abrogated G3M9 deglucosylation was responsible for the severe defects observed in Δ gls1-S  cells. Further studies disclosed that the defects could not be ascribed to disruption of glycoprotein entrance into calnexin-folding cycles, inhibition of the oligosaccharyltransferase by transfer reaction products, or reduced proteasomal degradation of misfolded glycoproteins. Lack of triglucosylated glycoprotein deglucosylation neither significantly prevented glycan elongation in the Golgi nor modified the overall cell wall monosaccharide composition. Nevertheless, it resulted in a distorted cell wall and in the absence of underlying ER membranes. Furthermore, Golgi expression of human endomannosidase partially restored normal growth in Δ gls1-S  cells. We propose that accumulation of G3M9-bearing glycoproteins is toxic and at least partially responsible for defects observed in MOGS-CDG.","doi":"10.1074/jbc.RA118.004844","authors":"Gallo GL, Valko A, Aramburu SI, Etchegaray E, Völker C, Parodi AJ, D'Alessio C","authors_abbrev":"Gallo GL et al.","pubmed_publication_date":"28 Dec 2018","pubmed_entrez_date":"2018-11-04","publication_year":"2018","canto_session_key":"661292025a8cdee8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Cecilia D'Alessio","canto_first_approved_date":"2019-07-27 11:53:47","canto_approved_date":"2025-09-04 10:02:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-22 12:25:17","canto_added_date":"2018-11-07 01:15:04","annotation_curators":[{"name":"Cecilia D'Alessio","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G10.09","SPAC56F8.06c","SPAC1002.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-07-27"},{"uniquename":"PMID:2320127","title":"Regulation of mitosis by cyclic accumulation of p80cdc25 mitotic inducer in fission yeast.","citation":"Nature 1990 Apr 05;344(6266):549-52","abstract":"The coordination of somatic cell division with cell size must be accomplished by the accumulation of mitotic inducers or the dilution, in the course of cell growth, of mitotic inhibitors. In fission yeast (Schizosaccharomyces pombe), cell size at mitosis is determined by expression of the cdc25+ and nim1+ inducer genes and of the inhibitor gene wee1+, which between them regulate the M-phase protein kinase p34cdc2. We now report that both the phosphoprotein product of cdc25+ (p80cdc25, with apparent relative molecular mass 80,000) and the corresponding messenger RNA increase in concentration as cells proceed through interphase, peaking at mitosis. We propose that the cell-cycle timing of mitosis in somatic cells is regulated by the cyclic accumulation of the cdc25 mitotic inducer, which on reaching a critical level results in activation of p34cdc2 protein kinase. Accumulation of this inducer could play a part in coordinating cell division with growth.","authors":"Moreno S, Nurse P, Russell P","authors_abbrev":"Moreno S et al.","pubmed_publication_date":"05 Apr 1990","pubmed_entrez_date":"1990-04-05","publication_year":"1990","canto_session_key":"1d6c058971c3d808","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_approved_date":"2017-01-06 14:46:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-13 17:06:59","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":4,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC582.03","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-12-13"},{"uniquename":"PMID:30647105","title":"Comparative Genomic Screen in Two Yeasts Reveals Conserved Pathways in the Response Network to Phenol Stress.","citation":"G3 (Bethesda) 2019 Mar 07;9(3):639-650","abstract":"Living organisms encounter various perturbations, and response mechanisms to such perturbations are vital for species survival. Defective stress responses are implicated in many human diseases including cancer and neurodegenerative disorders. Phenol derivatives, naturally occurring and synthetic, display beneficial as well as detrimental effects. The phenol derivatives in this study, butylated hydroxyanisole (BHA), butylated hydroxytoluene (BHT), and bisphenol A (BPA), are widely used as food preservatives and industrial chemicals. Conflicting results have been reported regarding their biological activity and correlation with disease development; understanding the molecular basis of phenol action is a key step for addressing issues relevant to human health. This work presents the first comparative genomic analysis of the genetic networks for phenol stress response in an evolutionary context of two divergent yeasts,  Schizosaccharomyces pombe  and  Saccharomyces cerevisiae  Genomic screening of deletion strain libraries of the two yeasts identified genes required for cellular response to phenol stress, which are enriched in human orthologs. Functional analysis of these genes uncovered the major signaling pathways involved. The results provide a global view of the biological events constituting the defense process, including cell cycle arrest, DNA repair, phenol detoxification by V-ATPases, reactive oxygen species alleviation, and endoplasmic reticulum stress relief through ergosterol and the unfolded protein response, revealing novel roles for these cellular pathways.","doi":"10.1534/g3.118.201000","authors":"Alhoch B, Chen A, Chan E, Elkabti A, Fariña S, Gilbert C, Kang J, King B, Leung K, Levy J, Martin E, Mazer B, McKinney S, Moyzis A, Nurimba M, Ozaki M, Purvis-Roberts K, Rothman JM, Raju S, Selassie C, Smith O, Ticus J, Edwalds-Gilbert G, Negritto MC, Wang R, Tang Z","authors_abbrev":"Alhoch B et al.","pubmed_publication_date":"07 Mar 2019","pubmed_entrez_date":"2019-01-17","publication_year":"2019","canto_session_key":"552b014f7404cd32","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-06-18 16:17:10","canto_approved_date":"2019-06-18 16:17:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-06-18 16:16:27","canto_added_date":"2019-01-18 01:15:04","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":551,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_30647105_phaf.tsv"}],"genes":["SPBC1604.20c","SPBC23G7.06c","SPBC18H10.19","SPAC1687.09","SPBP4H10.13","SPCC1442.07c","SPBC17A3.02","SPBC18H10.09","SPAC13A11.05","SPAC18G6.04c","SPCC1919.03c","SPAC1805.05","SPBC13G1.08c","SPAC1834.03c","SPAC32A11.03c","SPAC10F6.11c","SPBC1778.10c","SPAC13G6.08","SPBC11C11.06c","SPBC2D10.17","SPBC106.01","SPBC2G2.06c","SPBC16G5.06","SPBC1105.05","SPAC1527.03","SPAC227.07c","SPAC4F10.19c","SPBC1271.14","SPAC22E12.19","SPBC11C11.01","SPBC405.06","SPBP22H7.04","SPAC664.02c","SPAC23E2.01","SPBC215.08c","SPBP22H7.08","SPAC13A11.06","SPBC1289.14","SPBC14F5.03c","SPAC3C7.02c","SPAC4A8.09c","SPAC1296.05c","SPAC186.08c","SPCC594.06c","SPBPJ4664.05","SPAC8C9.03","SPBC354.04","SPAC589.04","SPBC725.15","SPAC1805.16c","SPAC1805.04","SPCC663.12","SPBC17A3.06","SPAC458.06","SPBC3H7.14","SPAC1071.06","SPAPB1E7.11c","SPBC17G9.09","SPCC4B3.08","SPCC4F11.03c","SPAC11D3.05","SPAPJ696.01c","SPAC25H1.05","SPAC1687.13c","SPBC2D10.04","SPAC3G6.05","SPAPJ691.03","SPAC31G5.11","SPBC1271.03c","SPAC17G8.07","SPAC824.02","SPBC651.06","SPAC19A8.03","SPAC19G12.13c","SPBC887.04c","SPAC8F11.10c","SPAC1002.03c","SPBP35G2.09","SPAC13G7.09c","SPCC622.19","SPBC32H8.02c","SPAC56F8.14c","SPAC23D3.10c","SPAC1834.04","SPAC23H3.13c","SPBC405.04c","SPAC9E9.17c","SPBC2F12.09c","SPAC1B3.05","SPAC1B3.08","SPCC306.04c","SPAC26A3.02","SPAC821.05","SPBC16E9.12c","SPAC25H1.07","SPCC736.07c","SPCC965.13","SPAC1002.06c","SPCC550.11","SPBC18E5.10","SPBC428.03c","SPBC8D2.02c","SPAC2E1P3.01","SPAC7D4.02c","SPAC12G12.01c","SPAC23G3.05c","SPAC56E4.07","SPAC4G8.11c","SPAC3H1.06c","SPCPB1C11.02","SPAC139.01c","SPAC1783.08c","SPBC32H8.13c","SPBC14F5.10c","SPBC119.12","SPAC18G6.01c","SPBC17G9.12c","SPAC4D7.07c","SPBC32H8.07","SPAC1006.06","SPAC13A11.01c","SPAP7G5.05","SPAC22H10.09","SPBC27.04","SPAC29A4.17c","SPBC1105.14","SPBP35G2.13c","SPAC17G6.03","SPAC4F8.10c","SPAC19G12.02c","SPAC3G6.04","SPAC144.03","SPBC1703.04","SPCC970.07c","SPBC32H8.01c","SPBC18H10.10c","SPBC409.17c","SPBC9B6.07","SPAPB2B4.03","SPAC16.01","SPCP1E11.04c","SPAC57A10.10c","SPAC17A2.06c","SPBC21C3.18","SPBC28F2.08c","SPBC17D11.01","SPAC12B10.12c","SPAC227.11c","SPAP14E8.02","SPAC688.12c","SPAC26H5.05","SPAC1D4.01","SPAC16.04","SPAC30D11.07","SPCP25A2.02c","SPAC8E11.10","SPAC23A1.07","SPBC1711.14","SPCC1223.11","SPBC23E6.01c","SPBC19G7.09","SPAC30D11.04c","SPBC3E7.16c","SPAC8C9.10c","SPAC31G5.17c","SPCC584.11c","SPBC19G7.06","SPBC18E5.09c","SPBC2D10.09","SPAC14C4.12c","SPAC16C9.02c","SPBC23G7.15c","SPCC550.14","SPAC4G9.13c","SPCC553.05c","SPBC29A3.08","SPBC2G2.14","SPCC736.04c","SPAC10F6.16","SPAC17G6.05c","SPBP8B7.08c","SPBC4C3.08","SPBC21B10.04c","SPBC1105.10","SPBC17D11.08","SPAC3F10.02c","SPAC977.17","SPBC11B10.05c","SPBC23G7.04c","SPCC1235.09","SPBC18E5.11c","SPBC409.20c","SPAC23G3.10c","SPCC622.04","SPBC25H2.15","SPAC25H1.03","SPCC126.04c","SPAC8E11.04c","SPBC1711.04","SPBC1778.02","SPBC1683.12","SPBC530.01","SPBP22H7.05c","SPBC11C11.10","SPCC777.02","SPBP23A10.10","SPAC17G8.11c","SPAC9.05","SPBC18H10.04c","SPAC13G6.01c","SPBC1198.09","SPCC645.06c","SPBC21B10.07","SPBP35G2.04c","SPAC222.16c","SPAC27D7.14c","SPAC1B3.10c","SPAC22E12.11c","SPBC11G11.01","SPBC1348.01","SPBC557.04","SPBC354.12","SPBC30D10.09c","SPBC409.11","SPCC1223.03c","SPAC6G9.04","SPAC27D7.03c","SPBC16G5.11c","SPAC11D3.14c","SPAC31G5.03","SPCC11E10.05c","SPBC18E5.08","SPBC31F10.15c","SPBC354.03","SPBC1773.11c","SPBC21B10.03c","SPCC4B3.06c","SPBC902.04","SPAC19A8.04","SPAC13G6.07c","SPBC216.01c","SPBC18E5.07","SPBC18H10.15","SPBC23E6.10c","SPAC23D3.09","SPAC8F11.03","SPAC750.08c","SPAC1805.02c","SPCC553.01c","SPBC3H7.10","SPBC12C2.07c","SPAC977.12","SPBC530.05","SPCC1840.06","SPBC4F6.08c","SPCC1450.12","SPBC29A10.01","SPBC359.06","SPAC21E11.05c","SPAC1952.02","SPCC1682.14","SPAC806.05","SPAC227.10","SPAC167.01","SPCC1259.03","SPBC1703.09","SPBC30D10.16","SPBC119.03","SPAPB1A11.01","SPBC12C2.04","SPAC19G12.16c","SPBC409.19c","SPAPB8E5.08","SPAC1071.09c","SPBC3E7.10","SPAC3H1.07","SPAC15A10.06","SPAC3A11.02","SPBC16G5.13","SPAC1B3.01c","SPBC36.06c","SPAC29A4.11","SPCC364.03","SPBC19G7.03c","SPCC1281.08","SPCC1620.11","SPAC4H3.06","SPBC30B4.06c","SPAPB24D3.04c","SPBC9B6.11c","SPCC23B6.03c","SPAC1486.01","SPCC1223.12c","SPAC19A8.11c","SPAC20H4.02","SPBC106.10","SPBC19C7.05","SPAC3C7.06c","SPAC3G6.13c","SPAC23A1.03","SPAC1783.06c","SPBC8E4.01c","SPAC16E8.17c","SPBC29A10.07","SPAC4A8.04","SPAC3F10.13","SPBP8B7.25","SPBC1D7.05","SPBC409.08","SPCC132.01c","SPCC5E4.05c","SPBC1D7.03","SPBC21B10.13c","SPCC23B6.04c","SPAC6F12.15c","SPAC17H9.14c","SPCC24B10.06","SPAC23H3.14","SPBC19C7.12c","SPBC337.09","SPBC365.16","SPBC902.06","SPBC36B7.03","SPAC25B8.09","SPAC4G9.12","SPBC725.09c","SPAC19G12.08","SPAC3G9.07c","SPBC106.12c","SPAC25A8.02","SPAC8C9.11","SPBC16H5.13","SPAC4D7.02c","SPBC1105.04c","SPBC3D6.04c","SPAC3H5.12c","SPAC13G6.10c","SPBP16F5.02","SPAP27G11.02","SPAC17C9.13c","SPAC1639.01c","SPBC8D2.19","SPBPJ4664.06","SPBC56F2.06","SPAP27G11.10c","SPBC106.04","SPBC31A8.01c","SPAC14C4.06c","SPBC1539.08","SPAC227.17c","SPAC56F8.06c","SPAC1952.12c","SPCC757.10","SPAC30.02c","SPAC458.02c","SPAC1B3.04c","SPAC17A5.08","SPBC31E1.01c","SPAC24B11.12c","SPAC22H12.05c","SPCC285.05","SPCC285.16c","SPBC342.01c","SPAC977.11","SPBC36B7.02","SPBC19F5.01c","SPAC25G10.02","SPAC23C11.15","SPAC227.13c","SPCC1183.11","SPAC17H9.03c","SPAC1687.05","SPAC23C4.06c","SPAPB1E7.02c","SPBC215.11c","SPAC2F7.06c","SPAC11H11.05c","SPBC947.01","SPBC725.14","SPAC27F1.08","SPBC4F6.06","SPBC947.08c","SPBC13G1.04c","SPAC1D4.03c","SPAC10F6.15","SPAC22F3.02","SPBC21.05c","SPCC1020.05","SPAC2G11.06","SPBC660.17c","SPAC2F3.02","SPAC26A3.01","SPAC22F3.03c","SPBC3E7.02c","SPCC1393.03","SPBC4B4.06","SPCC1919.05","SPAC24B11.10c","SPCC1223.04c","SPAC22H10.02","SPAC24C9.15c","SPBC902.03","SPBC19G7.07c","SPBC4F6.12","SPAC27E2.07","SPAC17C9.07","SPAC3H8.05c","SPAC589.12","SPBC106.03","SPAC6G9.14","SPAPB24D3.06c","SPAC9E9.10c","SPAC3H8.07c","SPBC23E6.08","SPBC354.10","SPBC337.07c","SPAC3A11.11c","SPAC328.01c","SPAC26F1.09","SPAC328.10c","SPBC2F12.04","SPCC16C4.06c","SPCC737.06c","SPAC23G3.07c","SPAC23G3.03","SPBC25H2.03","SPAC23A1.02c","SPCC191.10","SPCC1235.15","SPAC607.06c","SPAP8A3.04c","SPAC26A3.04","SPBC18H10.16","SPBC11B10.07c","SPBC1734.06","SPAC22H10.04","SPAC1250.05","SPBC1348.12","SPAC20H4.11c","SPAC26F1.08c","SPAC15F9.01c","SPAC13G6.15c","SPAC1952.05","SPAC1782.06c","SPBC1289.11","SPAC12B10.04","SPBC609.04","SPBC16H5.08c","SPCC188.12","SPBC19G7.04","SPAC6G10.11c","SPBC2G5.01","SPAC4F8.11","SPAC30C2.05","SPBC4B4.10c","SPAC20H4.07","SPBC27B12.06","SPBC839.13c","SPAC9E9.14","SPCC594.01","SPBC19C2.13c","SPBC800.11","SPAC56F8.02","SPAPB2B4.06","SPAC926.02","SPAC4F8.01","SPAC1D4.06c","SPAC3H8.10","SPAC24C9.14","SPAC30D11.12","SPBC32F12.07c","SPBC887.17","SPBC29A3.13","SPBC28F2.10c","SPBC27B12.10c","SPAC6F6.01","SPAC3H5.07","SPAC26A3.09c","SPBC1778.05c","SPBP35G2.06c","SPAC959.07","SPBC29A10.05","SPAC27D7.13c","SPAC8E11.03c","SPAC16E8.09","SPBC19F8.03c","SPBC3F6.05","SPAC23C4.03","SPAC23H4.09","SPBC800.08","SPAC1805.14","SPCC24B10.17","SPBC18H10.18c","SPBC354.07c","SPBC8D2.16c","SPAC29B12.03","SPAC29B12.04","SPAC2H10.01","SPAC212.01c","SPAC30.03c","SPBC32H8.09","SPAC23C4.05c","SPBC409.16c","SPAC19E9.02","SPAC1D4.11c","SPAC17G6.02c","SPAC3H1.14","SPBC336.13c","SPBC1734.07c"],"gene_count":509,"ltp_gene_count":0,"approved_date":"2019-06-18"},{"uniquename":"PMID:11423126","title":"The fission yeast meiotic regulator Mei2p undergoes nucleocytoplasmic shuttling.","citation":"FEBS Lett 2001 Jun 22;499(3):251-5","abstract":"Schizosaccharomyces pombe Mei2p is an RNA-binding protein that switches the cell cycle from mitotic to meiotic. Mei2p forms a unique dot in the nucleus prior to meiosis I, aided by a non-coding RNA molecule termed meiRNA. Here we show that Mei2p intrinsically undergoes nucleocytoplasmic shuttling. Artificial acceleration of nuclear migration of Mei2p advances nuclear dot formation, but meiRNA does not appear to promote the dot formation by modulating the migration rate of Mei2p into the nucleus. Rather, this RNA is likely to facilitate the assembly of Mei2p into a dot structure and trap the protein as such in the nucleus.","authors":"Sato M, Shinozaki-Yabana S, Yamashita A, Watanabe Y, Yamamoto M","authors_abbrev":"Sato M et al.","pubmed_publication_date":"22 Jun 2001","pubmed_entrez_date":"2001-06-26","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27D7.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20123974","title":"Roles of Hop1 and Mek1 in meiotic chromosome pairing and recombination partner choice in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2010 Apr;30(7):1570-81","abstract":"Synaptonemal complex (SC) proteins Hop1 and Mek1 have been proposed to promote homologous recombination in meiosis of Saccharomyces cerevisiae by establishment of a barrier against sister chromatid recombination. Therefore, it is interesting to know whether the homologous proteins play a similar role in Schizosaccharomyces pombe. Unequal sister chromatid recombination (USCR) was found to be increased in hop1 and mek1 single and double deletion mutants in assays for intrachromosomal recombination (ICR). Meiotic intergenic (crossover) and intragenic (conversion) recombination between homologous chromosomes was reduced. Double-strand break (DSB) levels were also lowered. Notably, deletion of hop1 restored DSB repair in rad50S meiosis. This may indicate altered DSB repair kinetics in hop1 and mek1 deletion strains. A hypothesis is advanced proposing transient inhibition of DSB processing by Hop1 and Mek1 and thus providing more time for repair by interaction with the homologous chromosome. Loss of Hop1 and Mek1 would then result in faster repair and more interaction with the sister chromatid. Thus, in S. pombe meiosis, where an excess of sister Holliday junction over homologous Holliday junction formation has been demonstrated, Hop1 and Mek1 possibly enhance homolog interactions to ensure wild-type level of crossover formation rather than inhibiting sister chromatid interactions.","doi":"10.1128/MCB.00919-09","authors":"Latypov V, Rothenberg M, Lorenz A, Octobre G, Csutak O, Lehmann E, Loidl J, Kohli J","authors_abbrev":"Latypov V et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-02-04","publication_year":"2010","canto_session_key":"0f79ae49e7ed5890","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-08-01 12:01:41","canto_approved_date":"2025-05-27 13:36:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-01 12:01:33","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.02","SPAC1556.01c","SPAC14C4.03","SPAC17A5.11"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-08-01"},{"uniquename":"PMID:12724769","title":"Monopolar attachment by Polo.","citation":"Nat Cell Biol 2003 May;5(5):379-82","abstract":"","authors":"Watanabe Y","authors_abbrev":"Watanabe Y","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-05-02","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22746336","title":"RNA interference pathways in fungi: mechanisms and functions.","citation":"Annu Rev Microbiol 2012;66:305-23","abstract":"RNA interference (RNAi) is a conserved eukaryotic gene regulatory mechanism that uses small noncoding RNAs to mediate posttranscriptional/transcriptional gene silencing. The fission yeast Schizosaccharomyces pombe and the filamentous fungus Neurospora crassa have served as important model systems for RNAi research. Studies on these two organisms and other fungi have contributed significantly to our understanding of the mechanisms and functions of RNAi in eukaryotes. In addition, surprisingly diverse RNAi-mediated processes and small RNA biogenesis pathways have been discovered in fungi. In this review, we give an overview of different fungal RNAi pathways with a focus on their mechanisms and functions.","doi":"10.1146/annurev-micro-092611-150138","authors":"Chang SS, Zhang Z, Liu Y","authors_abbrev":"Chang SS et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-07-04","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3005272","title":"Isolation and characterization of the structural gene for secreted acid phosphatase from Schizosaccharomyces pombe.","citation":"J Biol Chem 1986 Feb 25;261(6):2936-41","abstract":"The Schizosaccharomyces pombe acid phosphatase structural gene (PHO 1) was isolated by complementation of an S. pombe acid phosphatase mutant with a wild type S. pombe DNA recombinant plasmid library. Northern analysis indicates that acid phosphatase is encoded by a 1.4-kilobase mRNA of which approximately 100 bases are 3'-poly(A). The gene contains no introns and the 3' and 5' untranslated regions are short. According to DNA and amino acid sequence data, the S. pombe acid phosphatase has a molecular weight of 50,600. An 18-amino acid sequence at the N terminus was found that is similar to previously identified signal peptides in other eukaryotic secretory proteins. This signal peptide is apparently removed during secretion, since it is absent in the mature secreted acid phosphatase. The gene can be induced 2--3-fold by starvation for phosphate. The signals required for this induction are contained on the isolated DNA clone. Although the gene can be expressed in Saccharomyces cerevisiae, secretion is abnormal.","authors":"Elliott S, Chang CW, Schweingruber ME, Schaller J, Rickli EE, Carbon J","authors_abbrev":"Elliott S et al.","pubmed_publication_date":"25 Feb 1986","pubmed_entrez_date":"1986-02-25","publication_year":"1986","canto_session_key":"878b71dfebf4ce34","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-05 09:48:38","canto_approved_date":"2024-04-04 11:55:29","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-06-07 09:41:14","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-09-05"},{"uniquename":"PMID:10982878","title":"PSI-BLAST searches using hidden markov models of structural repeats: prediction of an unusual sliding DNA clamp and of beta-propellers in UV-damaged DNA-binding protein.","citation":"Nucleic Acids Res 2000 Sep 15;28(18):3570-80","abstract":"We have designed hidden Markov models (HMMs) of structurally conserved repeats that, based on pairwise comparisons, are unconserved at the sequence level. To model secondary structure features these HMMs assign higher probabilities of transition to insert or delete states within sequence regions predicted to form loops. HMMs were optimized using a sampling procedure based on the degree of statistical uncertainty associated with parameter estimates. A PSI-BLAST search initialized using a checkpoint-recovered profile derived from simulated sequences emitted by such a HMM can reveal distant structural relationships with, in certain instances, substantially greater sensitivity than a normal PSI-BLAST search. This is illustrated using two examples involving DNA- and RNA-associated proteins with structurally conserved repeats. In the first example a putative sliding DNA clamp protein was detected in the thermophilic bacterium Thermotoga maritima. This protein appears to have arisen by way of a duplicated beta-clamp gene that then acquired features of a PCNA-like clamp, perhaps to perform a PCNA-related function in association with one or more of the many archaeal-like proteins present in this organism. In the second example, beta-propeller domains were predicted in the large subunit of UV-damaged DNA-binding protein and in related proteins, including the large subunit of cleavage-polyadenylation specificity factor, the yeast Rse1p and human SAP130 pre-mRNA splicing factors and the fission yeast Rik1p gene silencing protein.","authors":"Neuwald AF, Poleksic A","authors_abbrev":"Neuwald AF et al.","pubmed_publication_date":"15 Sep 2000","pubmed_entrez_date":"2000-09-13","publication_year":"2000","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11854407","title":"Deletion mutants in COP9/signalosome subunits in fission yeast Schizosaccharomyces pombe display distinct phenotypes.","citation":"Mol Biol Cell 2002 Feb;13(2):493-502","abstract":"The COP9/signalosome complex is highly conserved in evolution and possesses significant structural similarity to the 19S regulatory lid complex of the proteasome. It also shares limited similarity to the translation initiation factor eIF3. The signalosome interacts with multiple cullins in mammalian cells. In the fission yeast Schizosaccharomyces pombe, the Csn1 subunit is required for the removal of covalently attached Nedd8 from Pcu1, one of three S. pombe cullins. It remains unclear whether this activity is required for all the functions ascribed to the signalosome. We previously identified Csn1 and Csn2 as signalosome subunits in S. pombe. csn1 and csn2 null mutants are DNA damage sensitive and exhibit slow DNA replication. Two further putative subunits, Csn4 and Csn5, were identified from the S. pombe genome database. Herein, we characterize null mutations of csn4 and csn5 and demonstrate that both genes are required for removal of Nedd8 from the S. pombe cullin Pcu1 and that their protein products associate with Csn1 and Csn2. However, neither csn4 nor csn5 null mutants share the csn1 and csn2 mutant phenotypes. Our data suggest that the subunits of the signalosome cannot be considered as a distinct functional unit and imply that different subunits of the signalosome mediate distinct functions.","authors":"Mundt KE, Liu C, Carr AM","authors_abbrev":"Mundt KE et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-02-21","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22A12.03c","SPAC1952.12c","SPBC215.03c","SPBC12D12.08c","SPAC222.16c","SPAC17G6.12","SPAPB17E12.04c","SPAC1687.13c"],"gene_count":8,"ltp_gene_count":6},{"uniquename":"PMID:8553071","title":"rad-dependent response of the chk1-encoded protein kinase at the DNA damage checkpoint.","citation":"Science 1996 Jan 19;271(5247):353-6","abstract":"Exposure of eukaryotic cells to agents that generate DNA damage results in transient arrest of progression through the cell cycle. In fission yeast, the DNA damage checkpoint associated with cell cycle arrest before mitosis requires the protein kinase p56chk1. DNA damage induced by ultraviolet light, gamma radiation, or a DNA-alkylating agent has now been shown to result in phosphorylation of p56chk1. This phosphorylation decreased the mobility of p56chk1 on SDS-polyacrylamide gel electrophoresis and was abolished by a mutation in the p56chk1 catalytic domain, suggesting that it might represent autophosphorylation. Phosphorylation of p56chk1 did not occur when other checkpoint genes were inactive. Thus, p56chk1 appears to function downstream of several of the known Schizosaccharomyces pombe checkpoint gene products, including that encoded by rad3+, a gene with sequence similarity to the ATM gene mutated in patients with ataxia telangiectasia. The phosphorylation of p56chk1 provides an assayable biochemical response to activation of the DNA damage checkpoint in the G2 phase of the cell cycle.","authors":"Walworth NC, Bernards R","authors_abbrev":"Walworth NC et al.","pubmed_publication_date":"19 Jan 1996","pubmed_entrez_date":"1996-01-19","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35274979","title":"The Rabl chromosome configuration masks a kinetochore reassembly mechanism in yeast mitosis.","citation":"Mol Biol Cell 2022 May 01;33(5):br8","abstract":"During cell cycle progression in metazoans, the kinetochore is assembled at mitotic onset and disassembled during mitotic exit. Once assembled, the kinetochore complex attached to centromeres interacts directly with the spindle microtubules, the vehicle of chromosome segregation. This reassembly program is assumed to be absent in budding and fission yeast, because most kinetochore proteins are stably maintained at the centromeres throughout the entire cell cycle. Here, we show that the reassembly program of the outer kinetochore at mitotic onset is unexpectedly conserved in the fission yeast  Schizosaccharomyces pombe . We identified this behavior by removing the Rabl chromosome configuration, in which centromeres are permanently associated with the nuclear envelope beneath the spindle pole body during interphase. In addition to having evolutionary implications for kinetochore reassembly, our results aid the understanding of the molecular processes responsible for kinetochore disassembly and assembly during mitotic entry.","doi":"10.1091/mbc.E20-09-0600","authors":"Jiménez-Martín A, Pineda-Santaella A, Pinto-Cruz J, León-Periñán D, García-Sánchez S, Delgado-Gestoso D, Marín-Toral L, Fernández-Álvarez A","authors_abbrev":"Jiménez-Martín A et al.","pubmed_publication_date":"01 May 2022","pubmed_entrez_date":"2022-03-11","publication_year":"2022","canto_session_key":"69214011a8e09c30","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-03-13 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20383139","title":"Shugoshin-PP2A counteracts casein-kinase-1-dependent cleavage of Rec8 by separase.","citation":"Nat Cell Biol 2010 May;12(5):500-6","abstract":"During meiosis, the cohesin complexes that maintain sister chromatid cohesion are lost in a stepwise manner. At meiosis I the cohesin subunit Rec8 is cleaved only along the chromosome arms; until meiosis II it is protected at centromeres by the action of shugoshin (Sgo1)-protein phosphatase 2A (PP2A). Although this regulation hypothetically involves phosphorylation that is antagonized by Sgo1-PP2A, the kinase and substrate that are responsible are as yet unknown. Using a genetic screen for 'anti-shugoshin', we identify Hhp2, an orthologue of casein kinase 1delta/epsilon (CK1), as a factor required for Rec8 cleavage in fission yeast. We show that CK1, rather than a Polo-like kinase that is widely believed to do so, acts as the cohesin kinase to promote this cleavage during meiosis. Crucially, forced localization of excess Hhp2 at the pericentromeric region abrogates the ability of Sgo1-PP2A to protect centromeric Rec8. Thus, our studies prove the key notion that the balance between Rec8 phosphorylation and its dephosphorylation by Sgo1-PP2A regulates the step-wise loss of chromosomal cohesion in meiosis.","doi":"10.1038/ncb2052","authors":"Ishiguro T, Tanaka K, Sakuno T, Watanabe Y","authors_abbrev":"Ishiguro T et al.","pubmed_publication_date":"May 2010","pubmed_entrez_date":"2010-04-13","publication_year":"2010","canto_session_key":"4d3b0d5a0015df91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2018-05-02 14:30:31","canto_approved_date":"2024-04-05 07:43:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-28 11:48:06","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":17,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":39,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3H7.15","SPCC188.02","SPBC29A10.14","SPAC23C4.12","SPBC16H5.07c","SPBP35G2.03c","SPAC23C11.16"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-05-02"},{"uniquename":"EMBL:AU013164","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14623272","title":"Ribosomal proteins S0 and S21 are involved in the stability of 18S rRNA in fission yeast, Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2003 Nov 28;311(4):942-7","abstract":"Stability of ribosomal RNA (rRNA) is not only essential for ribosome biogenesis but also crucial to the maintenance of proper translational level for cell viability. rRNA processing (maturation) is one of the key steps to derive functional rRNA, and to date, a large number of factors involved in this process have been identified. We investigated Rps0 binding proteins in fission yeast, Schizosaccharomyces pombe, and revealed that Rps0p is associated with Rps21 protein, similar to that of our previous observation in human cells. We demonstrated that both rps0(+)s and rps21(+) are essential genes for S. pombe analyzed by tetrad dissection assay. To study the functions of both genes, we established disruption strains transformed with inducible rescue plasmids. Using the strains our studies revealed that the loss of rps0(+)s or rps21(+) led to a deficiency of 40S ribosomal subunit formation. Additional functional studies indicate that this phenomenon is likely to be caused by insufficient 18S rRNA stability. The possible role of Rps0p and Rps21 that contribute to 18S rRNA maturation is further discussed.","authors":"Sato M, Kong CJ, Yoshida H, Nakamura T, Wada A, Shimoda C, Kaneda Y","authors_abbrev":"Sato M et al.","pubmed_publication_date":"28 Nov 2003","pubmed_entrez_date":"2003-11-19","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC18E5.06","SPAPJ698.02c","SPBC685.06"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:20230746","title":"Hsk1- and SCF(Pof3)-dependent proteolysis of S. pombe Ams2 ensures histone homeostasis and centromere function.","citation":"Dev Cell 2010 Mar 16;18(3):385-96","abstract":"Schizosaccharomyces pombe GATA factor Ams2 is responsible for cell cycle-dependent transcriptional activation of all the core histone genes peaking at G1/S phase. Intriguingly, its own protein level also fluctuates concurrently. Here, we show that Ams2 is ubiquitylated and degraded through the SCF (Skp1-Cdc53/Cullin-1-F-box) ubiquitin ligase, in which F box protein Pof3 binds this protein. Ams2 is phosphorylated at multiple sites, which is required for SCF(Pof3)-dependent proteolysis. Hsk1/Cdc7 kinase physically associates with and phosphorylates Ams2. Even mild overexpression of Ams2 induces constitutive histone expression and chromosome instability, and its toxicity is exaggerated when Hsk1 function is compromised. This is partly attributable to abnormal incorporation of canonical H3 into the central CENP-A/Cnp1-rich centromere, thereby reversing specific chromatin structures to apparently normal nucleosomes. We propose that Hsk1 plays a vital role during post S phase in genome stability via SCF(Pof3)-mediated degradation of Ams2, thereby maintaining centromere integrity.","doi":"10.1016/j.devcel.2009.12.024","authors":"Takayama Y, Mamnun YM, Trickey M, Dhut S, Masuda F, Yamano H, Toda T, Saitoh S","authors_abbrev":"Takayama Y et al.","pubmed_publication_date":"16 Mar 2010","pubmed_entrez_date":"2010-03-17","publication_year":"2010","canto_session_key":"1f8813e260d783d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-11 17:21:38","canto_approved_date":"2023-09-19 13:11:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-20 14:14:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.04","SPAC1834.04","SPBC1105.11c","SPBC409.05","SPCC290.04","SPBC8D2.03c","SPCC338.16","SPCC622.08c","SPCC550.13","SPBC776.12c","SPAC19G12.06c","SPBC1105.12","SPCC622.09","SPAC1834.03c"],"gene_count":14,"ltp_gene_count":5,"approved_date":"2017-12-11"},{"uniquename":"EMBL:SPC00076","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40501641","title":"Curcumin targets a circumferential band at the cleavage furrow of dividing fission yeast cells.","citation":"bioRxiv 2025 Jun 03;","abstract":"Curcumin is the active ingredient of one of the most widely used spices in the world for millennia. It is also highly valued as a traditional health supplement in many South Asian countries. It is not surprising that this yellow turmeric has attracted strong attention for its therapeutic potential in recent years. Nevertheless, the molecular and cellular targets of curcumin remain unknown. Here, we took a novel imaging-based approach to determine the intracellular localization of curcumin using the model organism fission yeast  Schizosacchromyces pombe  . We took advantage of the intrinsic fluorescence of curcumin to track its whereabout in yeast cells. Live fluorescence microscopy revealed for the first time that curcumin, at a concentration as low as one micromolar, formed a narrow circumferential band around the equatorial plane of dividing cells within 10 minutes of addition. The intensity of this band increased proportionally to the concentration of curcumin and gradually over time. Inhibition of cell division by the  cdc25  temperature-sensitive mutation inhibited the curcumin band. During cytokinesis, curcumin co-localized with the integrated plasma membrane protein Bgs1 at the cleavage furrow, not with either the contractile ring or the septum markers. Besides fission yeast, such equatorial curcumin band was found in the dividing cells of two other yeasts,  Saccharomyces cerevisiae  and  Candida albicans  . Our study thus discovered that this widely used yellow turmeric targets the cleavage furrow of dividing yeast cells, suggesting that curcumin may have anti-fungal therapeutic potential (223 words).","doi":"10.1101/2025.06.02.657428","authors":"Dias DA, Kulasegaram V, Okorokova-Façanha A, Chen Q","authors_abbrev":"Dias DA et al.","pubmed_publication_date":"03 Jun 2025","pubmed_entrez_date":"2025-06-12","publication_year":"2025","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2025-06-12 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPWDRP","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41366798","title":"Distinct roles of histone H2B ubiquitination at promoters and coding regions of Pol II-transcribed stress genes.","citation":"Genome Biol 2025 Dec 09;26(1):419","abstract":"The histone code, comprised of diverse histone post-translational modifications, intricately regulates nucleosome organization and gene expression. Histone marks also serve as binding sites for a diverse array of protein complexes and enzymes, orchestrating downstream cellular functions. Some modifications are crucial for enabling the complete activation of alternative gene expression programs in response to environmental changes.\nThis study provides insights into the complex histone crosstalk regulating gene expression and underscores the pivotal role of histone ubiquitination in promoting efficient nucleosome dynamics during Pol II transcription.\nThe online version contains supplementary material available at 10.1186/s13059-025-03891-1.","doi":"10.1186/s13059-025-03891-1","authors":"Barrios R, Vega M, Gracia-Domingo R, Boronat S, García-Santamarina S, Tanny JC, Ayté J, Hidalgo E","authors_abbrev":"Barrios R et al.","pubmed_publication_date":"09 Dec 2025","pubmed_entrez_date":"2025-12-10","publication_year":"2025","canto_session_key":"08cf28099244f261","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-11 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PB_REF:0000006","title":"Disease associations from Monarch via human-pombe orthologs","abstract":"Disease associations are created by taking human gene-disease causal and correlated associations created by Monarch (https://monarchinitiative.org) using the MONDO disease ontology (https://mondo.monarchinitiative.org/) and mapping to fission yeast orthologs (https://www.pombase.org/data/orthologs) using the manually maintained fission yeast/human ortholog table.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC27B12.09c","SPAC24C9.12c","SPCC1906.01","SPAC1565.08","SPAPB24D3.09c","SPCC622.12c","SPAC227.16c","SPAC144.06","SPAC29A4.06c","SPBC13G1.03c","SPCC794.07","SPBC354.06","SPAC15E1.08","SPAC1071.06","SPCC613.05c","SPCC188.06c","SPAC1834.10c","SPAC26F1.04c","SPBC16G5.05c","SPAC15A10.01","SPBC31E1.06","SPCC4B3.18","SPAC10F6.03c","SPCC285.04","SPCC1235.05c","SPNCRNA.214","SPAC186.08c","SPAC23C4.17","SPBC16H5.06","SPAC23C11.11","SPAC2G11.10c","SPBC30B4.04c","SPCC13B11.04c","SPBC1773.05c","SPAC22A12.11","SPAC56E4.04c","SPCC338.17c","SPAC22E12.10c","SPBP4H10.04","SPBC1921.01c","SPBC24C6.03","SPAC607.09c","SPAC13G6.05c","SPCC16C4.09","SPMIT.10","SPAC328.08c","SPCC1840.05c","SPAC23D3.09","SPAPB8E5.06c","SPBC1815.01","SPAC23C11.17","SPCC576.07","SPAC6F12.08c","SPAC56E4.02c","SPAC11E3.06","SPAP8A3.12c","SPAC1F3.05","SPAC17H9.03c","SPBC21B10.03c","SPBC16A3.11","SPCC1672.11c","SPAP14E8.03","SPBC14F5.09c","SPAC1D4.10","SPAC17G6.08","SPBC29A3.15c","SPBC3B9.11c","SPAC1039.09","SPBC1604.17c","SPCC188.02","SPAPB17E12.12c","SPAC56F8.04c","SPCC290.03c","SPAC23H3.07c","SPBC2A9.06c","SPAC1006.07","SPBC21C3.01c","SPBP22H7.08","SPCC4B3.03c","SPCC576.14","SPBC649.02","SPCPB1C11.03","SPAC2G11.03c","SPBP19A11.07c","SPCC622.10c","SPBC15D4.11c","SPBC30D10.13c","SPBC16C6.09","SPBC365.02c","SPBC216.06c","SPAC20H4.11c","SPAC9G1.05","SPBC115.01c","SPBC12D12.09","SPAC19D5.02c","SPBC28F2.08c","SPAC1805.06c","SPAC1782.09c","SPBP19A11.06","SPAC13D6.02c","SPBC2G5.05","SPBC30B4.02c","SPAC6G9.16c","SPBC24C6.06","SPAC56F8.02","SPBC342.01c","SPBC8D2.04","SPBC4C3.06","SPCC364.04c","SPAC3H1.05","SPCC1682.11c","SPBC16D10.04c","SPMIT.07","SPAC19B12.05c","SPBC30B4.06c","SPAC24C9.09","SPBC6B1.09c","SPAC20G8.05c","SPAP27G11.07c","SPBC1A4.03c","SPAC17C9.12","SPBC1709.18","SPAC2G11.06","SPAC23G3.12c","SPBC23G7.16","SPAC11E3.02c","SPAC1039.07c","SPAC6F12.12","SPAC1F12.09","SPAC1556.07","SPAC1687.16c","SPBC8D2.18c","SPBC32F12.15","SPAPB17E12.13","SPCC4G3.19","SPCC553.02","SPBC365.14c","SPBC119.10","SPAC23C4.16c","SPAC17D4.04","SPBC543.09","SPBC1539.07c","SPAC644.10","SPAC3A12.05c","SPCC4B3.09c","SPBC660.13c","SPBC28F2.12","SPBC8D2.13","SPCC162.09c","SPAC57A7.13","SPCC338.12","SPAC12B10.09","SPAC26H5.12","SPCP25A2.02c","SPBC25H2.04c","SPAC227.13c","SPAP27G11.02","SPAC22E12.09c","SPAC30C2.07","SPAC644.17c","SPAC6G10.03c","SPAC29E6.01","SPAC6G10.05c","SPAC3C7.12","SPAC20G8.04c","SPBP35G2.10","SPCC4E9.01c","SPAC1851.02","SPBC1198.05","SPBC18E5.12c","SPBC21D10.12","SPBC1347.08c","SPAC18G6.10","SPCC4B3.12","SPCC24B10.12","SPBC1703.04","SPBC19G7.01c","SPCC550.04c","SPAC1F5.07c","SPAC23H3.06","SPAC637.04","SPAC19A8.02","SPAC22E12.03c","SPBC2A9.12","SPBC1604.21c","SPBC4F6.18c","SPAC1093.02","SPBC2D10.18","SPAC823.09c","SPBC17G9.03c","SPAC3H5.05c","SPBC887.12","SPBC947.01","SPBC1198.12","SPBC16C6.12c","SPCC1442.08c","SPAC18G6.04c","SPAC1783.08c","SPCC320.10","SPBC30B4.08","SPBC3B8.03","SPBC3E7.02c","SPBC21H7.06c","SPAC19G12.13c","SPAC2G11.05c","SPAC2E1P5.01c","SPAC23A1.12c","SPAC11D3.18c","SPCC285.16c","SPAC1805.04","SPBC19G7.04","SPBC691.05c","SPCC14G10.03c","SPCC320.05","SPAC22F3.06c","SPCC794.09c","SPCC16C4.14c","SPAC8F11.06","SPAC3C7.13c","SPAC1B3.21","SPAC17D4.02","SPBC12D12.04c","SPAC23A1.15c","SPBC691.02c","SPCC16A11.10c","SPCC613.10","SPCC364.07","SPBPB2B2.06c","SPBC947.05c","SPBC460.01c","SPAC17C9.07","SPCC576.06c","SPCC965.04c","SPBC1105.12","SPBC1703.03c","SPAC31A2.13c","SPAC3A11.05c","SPCC31H12.05c","SPBC776.02c","SPBC8D2.15","SPCC18B5.03","SPBC685.05","SPAC644.14c","SPAC1039.02","SPBC24C6.08c","SPAC16E8.03","SPAPB8E5.07c","SPAC1687.22c","SPCC1827.02c","SPAC23E2.02","SPAC17G6.06","SPBP23A10.08","SPAC343.04c","SPAC10F6.09c","SPAC15F9.01c","SPAC15A10.03c","SPCC757.09c","SPAC14C4.06c","SPAC1486.08","SPAC26A3.09c","SPCC1020.06c","SPBC16C6.13c","SPBC1773.09c","SPAC17A5.06","SPBC17D1.03c","SPAC17A5.15c","SPBC25H2.18","SPAC1142.06","SPAC11E3.12","SPAC24B11.13","SPAC5D6.07c","SPAC24C9.06c","SPAPB1A10.15","SPAC3G6.05","SPAC1486.01","SPCC4B3.11c","SPBC1604.05","SPBC8D2.12c","SPAC1782.11","SPCC1235.11","SPAC19D5.07","SPBC3B9.17","SPBC839.16","SPAC26H5.10c","SPAC19G12.14","SPAC24H6.01c","SPAC1071.03c","SPBC1539.03c","SPAC16A10.03c","SPAC22F3.04","SPAC27E2.06c","SPBP35G2.06c","SPAP27G11.06c","SPCC1322.08","SPBC1105.10","SPBC21C3.13","SPCC18.09c","SPCC794.01c","SPAC16E8.15","SPCC24B10.09","SPAC6F12.05c","SPBC646.07c","SPBC21H7.03c","SPBP35G2.03c","SPCC553.08c","SPAC8F11.03","SPBC543.04","SPCC285.15c","SPBC15D4.04","SPCC1795.03","SPBC1734.02c","SPCC737.02c","SPCC16C4.11","SPAC18G6.07c","SPBPB8B6.03","SPBC14F5.13c","SPAC1687.01","SPAC30.04c","SPBC29A3.07c","SPBC3H7.03c","SPAC29A4.14c","SPAC6B12.10c","SPBC15C4.03","SPBC3H7.12","SPCC1827.03c","SPBP8B7.19","SPBC2F12.05c","SPBC725.15","SPAC14C4.05c","SPAC3F10.04","SPAC17G6.17","SPAC688.03c","SPCC285.14","SPAC1F3.09","SPBC8D2.20c","SPAP27G11.13c","SPBC1604.04","SPCC188.08c","SPCC417.16","SPCC330.12c","SPAC29A4.18","SPAC57A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Protein Analysis in  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Mar 01;2017(3)","abstract":"Biochemical monitoring and interrogation of protein function is a critical component of most fission yeast studies. In particular, its small proteome size, high conservation of core molecular cell biology, and genetic malleability make  Schizosaccharomyces pombe  an excellent model organism in which to use mass spectrometry to conduct proteome-wide approaches. Here we discuss issues encountered during the analysis of fission yeast protein preparations.","doi":"10.1101/pdb.top079806","authors":"Grallert A, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"01 Mar 2017","pubmed_entrez_date":"2017-03-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-03-04 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD218","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18505884","title":"Schizosaccharomyces pombe Bub3 is dispensable for mitotic arrest following perturbed spindle formation.","citation":"Genetics 2008 Jun;179(2):785-92","abstract":"The core proteins of the spindle assembly checkpoint (SAC), Mads, Bubs, and Mps1, first identified in the budding yeast, are thought to be functionally and structurally conserved through evolution. We found that fission yeast Bub3 is dispensable for SAC, as bub3 null mutants blocked mitotic progression when spindle formation was disrupted. Consistently, the bub3 mutation only weakly affected the stability of minichromosome Ch16 compared with other SAC mutants. Fission yeast Rae1 has sequence homology with Bub3. The bub3 rae1 double mutant and rae1 single mutant did not have defective SAC, suggesting that these genes do not have overlapping roles for SAC. Observations of living cells revealed that the duration of the mitotic prometaphase/metaphase was longer in the bub3 mutant and was Mad2 dependent. Further, the bub3 mutant was defective in sister centromere association during metaphase. Together, these findings suggest that fission yeast Bub3 is required for normal spindle dynamics, but not for SAC.","doi":"10.1534/genetics.107.081695","authors":"Tange Y, Niwa O","authors_abbrev":"Tange Y et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-05-29","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22806395","title":"Carboxy-terminal phosphorylation sites in Cdc25 contribute to enforcement of the DNA damage and replication checkpoints in fission yeast.","citation":"Curr Genet 2012 Aug;58(4):217-34","abstract":"In fission yeast and vertebrate cells, Cdc25 phosphatase is the target of checkpoint-mediated response to DNA replication blocks, DNA damage, and extracellular stress. As such, it is a key regulator of cell cycle progress and genomic stability. In fission yeast, phosphorylation of Cdc25 by the checkpoint kinases Cds1 and Chk1 and also Srk1 during stress creates a binding site for the 14-3-3 homolog Rad24; the complex is then exported from the nucleus. Cdc25 contains 12 potential serine/threonine phosphorylation sites that are phosphorylated in vitro by Cds1; 9 reside in the amino terminal half of the protein with the remaining sites are located in the extreme C-terminus. We have previously shown that deletion of the nine amino terminal sites results in degradation of the mutant protein while the checkpoint is enforced by the Mik1 kinase acting on Cdc2 tyrosine-15. Here, we examine the influence of the three C-terminal sites on the negative regulation of Cdc25. These sites are conserved in vertebrates and have been shown to be phosphorylated following DNA damage and replication blocks. We show that these three sites have a role in the negative regulation of Cdc25 following replication arrest, but perhaps more importantly they appear to particularly contribute to regulating the duration, and thus the effectiveness of the arrested state.","doi":"10.1007/s00294-012-0379-1","authors":"Frazer C, Young PG","authors_abbrev":"Frazer C et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-07-19","publication_year":"2012","canto_session_key":"c103f423f714a464","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.14","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:1587485","title":"Versatile shuttle vectors and genomic libraries for use with Schizosaccharomyces pombe.","citation":"Gene 1992 May 01;114(1):59-66","abstract":"We have constructed a variety of pUC-based vectors designed for maintenance in Schizosaccharomyces pombe. These can be used for both gene bank construction and subcloning. Plasmids pUR18 and pUR19 are modifications of pUC vectors containing the Sc. pombe ars1 and ura4 sequences and retaining the lacZ XGal blue-white selection system for screening for DNA inserts. These vectors have been used to construct representative Sc. pombe and Saccharomyces cerevisiae genomic libraries. To assist in the creation of gene deletions, we have constructed another two plasmids. Combined with the technique of partially filling-in 5' overhangs created with restriction enzymes, these plasmids simplify the replacement of all or part of an open reading frame by a functional ura4 gene. Furthermore, such constructs can be excised with SfiI as a linear fragment for use in Sc. pombe transformations. When integrated into the Sc. pombe genome, the site of integration can be easily mapped by pulsed-field gel electrophoresis using the presence of a novel NotI site.","authors":"Barbet N, Muriel WJ, Carr AM","authors_abbrev":"Barbet N et al.","pubmed_publication_date":"01 May 1992","pubmed_entrez_date":"1992-05-01","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26613475","title":"Pulled Polymer Loops as a Model for the Alignment of Meiotic Chromosomes.","citation":"Phys Rev Lett 2015 Nov 13;115(20):208102","abstract":"During recombination, the DNA of parents exchange their genetic information to give rise to a genetically unique offspring. For recombination to occur, homologous chromosomes need to find each other and align with high precision. Fission yeast solves this problem by folding chromosomes in loops and pulling them through the viscous nucleoplasm. We propose a theory of pulled polymer loops to quantify the effect of drag forces on the alignment of chromosomes. We introduce an external force field to the concept of a Brownian bridge and thus solve for the statistics of loop configurations in space.","doi":"10.1103/PhysRevLett.115.208102","authors":"Lin YT, Frömberg D, Huang W, Delivani P, Chacón M, Tolić IM, Jülicher F, Zaburdaev V","authors_abbrev":"Lin YT et al.","pubmed_publication_date":"13 Nov 2015","pubmed_entrez_date":"2015-11-28","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-11-29 01:19:23","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27264871","title":"Taz1-Shelterin Promotes Facultative Heterochromatin Assembly at Chromosome-Internal Sites Containing Late Replication Origins.","citation":"Mol Cell 2016 Jun 16;62(6):862-874","abstract":"Facultative heterochromatin regulates gene expression, but its assembly is poorly understood. Previously, we identified facultative heterochromatin islands in the fission yeast genome and found that RNA elimination machinery promotes island assembly at meiotic genes. Here, we report that Taz1, a component of the telomere protection complex Shelterin, is required to assemble heterochromatin islands at regions corresponding to late replication origins that are sites of double-strand break formation during meiosis. The loss of Taz1 or other Shelterin subunits, including Ccq1 that interacts with Clr4/Suv39h, abolishes heterochromatin at late origins and causes derepression of associated genes. Moreover, the late-origin regulator Rif1 affects heterochromatin at Taz1-dependent islands and subtelomeric regions. We explore the connection between facultative heterochromatin and replication control and show that heterochromatin machinery affects replication timing. These analyses reveal the role of Shelterin in facultative heterochromatin assembly at late origins, which has important implications for genome stability and gene regulation.","doi":"10.1016/j.molcel.2016.04.034","authors":"Zofall M, Smith DR, Mizuguchi T, Dhakshnamoorthy J, Grewal SIS","authors_abbrev":"Zofall M et al.","pubmed_publication_date":"16 Jun 2016","pubmed_entrez_date":"2016-06-07","publication_year":"2016","canto_session_key":"b704434d7c80d369","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-06-09 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c","SPCC622.16c","SPCC188.07","SPAC16A10.07c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:16223485","title":"RNAi-directed assembly of heterochromatin in fission yeast.","citation":"FEBS Lett 2005 Oct 31;579(26):5872-8","abstract":"Heterochromatin is an epigenetically heritable and conserved feature of eukaryotic chromosomes with important roles in chromosome segregation, genome stability, and gene regulation. The formation of heterochromatin involves an ordered array of chromatin changes, including histone deacetylation, histone H3-lysine 9 methylation, and recruitment of histone binding proteins such as Swi6/HP1. Recent discoveries have uncovered a role for the RNA interference (RNAi) pathway in heterochromatin assembly in the fission yeast Schizosaccharomyces pombe and other eukaryotes. Purification of two RNAi complexes, RITS and RDRC, from fission yeast has provided further insight into the mechanism of RNAi-mediated heterochromatin assembly. These discoveries have given rise to a model in which small interfering RNA molecules act as specificity factors that initiate epigenetic chromatin modifications and double strand RNA synthesis at specific chromosome regions.","authors":"Verdel A, Moazed D","authors_abbrev":"Verdel A et al.","pubmed_publication_date":"31 Oct 2005","pubmed_entrez_date":"2005-10-15","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11915517","title":"[Functional analysis of calcineurin-mediated signalling pathway using fission yeast as a model system].","citation":"Nihon Yakurigaku Zasshi 2002 Mar;119(3):155-61","abstract":"Calcineurin (CN), a highly conserved Ca2+/calmodulin-regulated phosphatase, is a critical component of many calcium-regulated processes in mammalian cells, including T cell activation, cardiac hypertrophy, learning and memory. CN is specifically inhibited by the immunosuppressant drugs cyclosporin A and tacrolimus (FK506), and these drugs have served as valuable reagents in identifying the role of CN in a wide variety of cell types. CN may have additional functions in other cell types, and the loss of these functions may contribute to the side effects of these drugs, which include nephrotoxicity and neurotoxicity. A better understanding of the biological roles of CN in different cell types may promote the development of improved strategies for immunosuppression. We have been studying the CN signal transduction pathway in fission yeast because this system is amenable to genetics and has many advantages in terms of relevance to higher systems. Fission yeast has a single gene encoding the catalytic subunit of CN, ppb1+, that is essential for cytokinesis. We have shown that in fission yeast CN plays an essential role in maintaining chloride ion homeostasis and acts antagonistically with the Pmk1 MAP kinase pathway. We also carried out an isolation and a screening for several FK506-sensitive mutants in order to identify genes that share an essential function for viability with CN. Possible roles of these gene products in cellular functions in relation to calcineurin are discussed.","authors":"Sugiura R","authors_abbrev":"Sugiura R","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-28","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34005232","canto_session_key":"7294a085b49feab1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007263","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.121"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24820419","title":"Rho2 palmitoylation is required for plasma membrane localization and proper signaling to the fission yeast cell integrity mitogen- activated protein kinase pathway.","citation":"Mol Cell Biol 2014 Jul;34(14):2745-59","abstract":"The fission yeast small GTPase Rho2 regulates morphogenesis and is an upstream activator of the cell integrity pathway, whose key element, mitogen-activated protein kinase (MAPK) Pmk1, becomes activated by multiple environmental stimuli and controls several cellular functions. Here we demonstrate that farnesylated Rho2 becomes palmitoylated in vivo at cysteine-196 within its carboxyl end and that this modification allows its specific targeting to the plasma membrane. Unlike that of other palmitoylated and prenylated GTPases, the Rho2 control of morphogenesis and Pmk1 activity is strictly dependent upon plasma membrane localization and is not found in other cellular membranes. Indeed, artificial plasma membrane targeting bypassed the Rho2 need for palmitoylation in order to signal. Detailed functional analysis of Rho2 chimeras fused to the carboxyl end from the essential GTPase Rho1 showed that GTPase palmitoylation is partially dependent on the prenylation context and confirmed that Rho2 signaling is independent of Rho GTP dissociation inhibitor (GDI) function. We further demonstrate that Rho2 is an in vivo substrate for DHHC family acyltransferase Erf2 palmitoyltransferase. Remarkably, Rho3, another Erf2 target, negatively regulates Pmk1 activity in a Rho2-independent fashion, thus revealing the existence of cross talk whereby both GTPases antagonistically modulate the activity of this MAPK cascade.","authors":"Sánchez-Mir L, Franco A, Martín-García R, Madrid M, Vicente-Soler J, Soto T, Gacto M, Pérez P, Cansado J","authors_abbrev":"Sánchez-Mir L et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-05-14","publication_year":"2014","canto_session_key":"cb2976e86de18f39","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F12.06","SPAC16.01","SPBC3H7.09","SPAC23C4.08"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:29423855","title":"In Situ Chromatin-Binding Assay Using Epifluorescent Microscopy in S. pombe.","citation":"Methods Mol Biol 2018;1721:155-165","abstract":"Chromatin-associated proteins play critical roles in many cellular processes, including gene expression, epigenetic regulation, DNA repair, recombination, and replication. Especially, epigenetic landscape, shaped by a variety of chromatin-binding proteins, is dynamic and regulated in a context-dependent manner. In situ chromatin-binding assay is a powerful but simple tool to investigate how proteins, such as epigenetic components, associate with chromatin. This approach relies on the fact that chromatin bound proteins are more resistant to detergent extraction. Here, we describe a protocol for the in situ chromatin-binding assay used in Schizosaccaromyces pombe.","doi":"10.1007/978-1-4939-7546-4_14","authors":"Yang J, Li F","authors_abbrev":"Yang J et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007963","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24861625","title":"Hyperactive Cdc2 kinase interferes with the response to broken replication forks by trapping S.pombe Crb2 in its mitotic T215 phosphorylated state.","citation":"Nucleic Acids Res 2014 Jul;42(12):7734-47","abstract":"Although it is well established that Cdc2 kinase phosphorylates the DNA damage checkpoint protein Crb2(53BP1) in mitosis, the full impact of this modification is still unclear. The Tudor-BRCT domain protein Crb2 binds to modified histones at DNA lesions to mediate the activation of Chk1 by Rad3ATR kinase. We demonstrate here that fission yeast cells harbouring a hyperactive Cdc2CDK1 mutation (cdc2.1w) are specifically sensitive to the topoisomerase 1 inhibitor camptothecin (CPT) which breaks DNA replication forks. Unlike wild-type cells, which delay only briefly in CPT medium by activating Chk1 kinase, cdc2.1w cells bypass Chk1 to enter an extended cell-cycle arrest which depends on Cds1 kinase. Intriguingly, the ability to bypass Chk1 requires the mitotic Cdc2 phosphorylation site Crb2-T215. This implies that the presence of the mitotic phosphorylation at Crb2-T215 channels Rad3 activity towards Cds1 instead of Chk1 when forks break in S phase. We also provide evidence that hyperactive Cdc2.1w locks cells in a G1-like DNA repair mode which favours non-homologous end joining over interchromosomal recombination. Taken together, our data support a model such that elevated Cdc2 activity delays the transition of Crb2 from its G1 to its G2 mode by blocking Srs2 DNA helicase and Casein Kinase 1 (Hhp1).","doi":"10.1093/nar/gku452","authors":"Mahyous Saeyd SA, Ewert-Krzemieniewska K, Liu B, Caspari T","authors_abbrev":"Mahyous Saeyd SA et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-05-28","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC543.03c","SPAC4H3.05","SPBC660.14","SPCC126.02c","SPCC18B5.03","SPCC18B5.11c","SPBC342.05","SPCC970.01","SPBC11B10.09","SPCC4G3.05c","SPBC216.05","SPAC2G11.12","SPBC3H7.15","SPCC1259.13","SPAC24H6.05"],"gene_count":15,"ltp_gene_count":15},{"uniquename":"PMID:19804750","title":"DNA double-strand breaks come into focus.","citation":"Cell 2009 Oct 02;139(1):25-7","abstract":"The Mre11-Rad50-Nbs1 (MRN) complex senses DNA double-strand breaks and recruits different repair pathway and checkpoint proteins to break foci. Two new studies (Williams et al., 2009; Lloyd et al., 2009) identify Nbs1 as a key factor in this process and reveal how an N-terminal protein recruitment module in Nbs1 binds to different response factors through shared phosphopeptide motifs.","doi":"10.1016/j.cell.2009.09.017","authors":"Hopfner KP","authors_abbrev":"Hopfner KP","pubmed_publication_date":"02 Oct 2009","pubmed_entrez_date":"2009-10-07","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10079952","title":"[Molecular cloning and characteristics of rpc19+ and rpc40+ Schizosaccharomyces pombe genes, coding for common subunits of nuclear RNA polymerase I and III].","citation":"Bioorg Khim 1998 Dec;24(12):933-7","abstract":"Full-length copies of cDNAs of the rpc19+ and rpc40+ genes encoding the common subunits of nuclear RNA polymerases I and III and the corresponding fragments of chromosomes were isolated from genomic and cDNA libraries of Schizosaccharomyces pombe and characterized. It was established that the cloned genes are located on chromosomes III and II of the fission yeast, respectively. The rpc40+ gene lacks introns, and the rpc19+ gene contains two intervening sequences. The comparison of subunits Rpc19 (125 aa; M 13 722 Da; pI 4.51) and Rpc40 (348 aa; M 39 141 Da; pI 5.40) of Sz. pombe, whose characteristics were deduced from the sequences of their cDNAs, with the orthologous components of other eukaryotes allowed the most conserved structure-functional domains of these proteins to be identified.","authors":"Shpakovskiĭ GV, Shematorova EK","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1999-03-18","publication_year":"1998","canto_session_key":"b25eb4866c2de130","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-29 21:31:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 21:21:58","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1687.01","SPBC1289.07c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-04-29"},{"uniquename":"PMID:4660461","title":"Acid phosphatase in Schizosaccharomyces pombe. I. Regulation and preliminary characterization.","citation":"Biochim Biophys Acta 1972 Dec 29;286(2):363-74","abstract":"","authors":"Dibenedetto G","authors_abbrev":"Dibenedetto G","pubmed_publication_date":"29 Dec 1972","pubmed_entrez_date":"1972-12-29","publication_year":"1972","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31213126","title":"RNA-induced initiation of transcriptional silencing (RITS) complex structure and function.","citation":"RNA Biol 2019 Sep;16(9):1133-1146","abstract":"Heterochromatic regions of the genome are epigenetically regulated to maintain a heritable '\"silent state\"'. In fission yeast and other organisms, epigenetic silencing is guided by nascent transcripts, which are targeted by the RNA interference pathway. The key effector complex of the RNA interference pathway consists of small interfering RNA molecules (siRNAs) associated with Argonaute, assembled into the RNA-induced transcriptional silencing (RITS) complex. This review focuses on our current understanding of how RITS promotes heterochromatin formation, and in particular on the role of Argonaute-containing complexes in many other functions such as quelling, release of RNA polymerases, cellular quiescence and genome defense.","doi":"10.1080/15476286.2019.1621624","authors":"Bhattacharjee S, Roche B, Martienssen RA","authors_abbrev":"Bhattacharjee S et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-06-20","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-06-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21784873","title":"Genome-scale phylogenetic function annotation of large and diverse protein families.","citation":"Genome Res 2011 Nov;21(11):1969-80","abstract":"The Statistical Inference of Function Through Evolutionary Relationships (SIFTER) framework uses a statistical graphical model that applies phylogenetic principles to automate precise protein function prediction. Here we present a revised approach (SIFTER version 2.0) that enables annotations on a genomic scale. SIFTER 2.0 produces equivalently precise predictions compared to the earlier version on a carefully studied family and on a collection of 100 protein families. We have added an approximation method to SIFTER 2.0 and show a 500-fold improvement in speed with minimal impact on prediction results in the functionally diverse sulfotransferase protein family. On the Nudix protein family, previously inaccessible to the SIFTER framework because of the 66 possible molecular functions, SIFTER achieved 47.4% accuracy on experimental data (where BLAST achieved 34.0%). Finally, we used SIFTER to annotate all of the Schizosaccharomyces pombe proteins with experimental functional characterizations, based on annotations from proteins in 46 fungal genomes. SIFTER precisely predicted molecular function for 45.5% of the characterized proteins in this genome, as compared with four current function prediction methods that precisely predicted function for 62.6%, 30.6%, 6.0%, and 5.7% of these proteins. We use both precision-recall curves and ROC analyses to compare these genome-scale predictions across the different methods and to assess performance on different types of applications. SIFTER 2.0 is capable of predicting protein molecular function for large and functionally diverse protein families using an approximate statistical model, enabling phylogenetics-based protein function prediction for genome-wide analyses. The code for SIFTER and protein family data are available at http://sifter.berkeley.edu.","doi":"10.1101/gr.104687.109","authors":"Engelhardt BE, Jordan MI, Srouji JR, Brenner SE","authors_abbrev":"Engelhardt BE et al.","pubmed_publication_date":"Nov 2011","pubmed_entrez_date":"2011-07-26","publication_year":"2011","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27687771","title":"CSL protein regulates transcription of genes required to prevent catastrophic mitosis in fission yeast.","citation":"Cell Cycle 2016 Nov 16;15(22):3082-3093","abstract":"For every eukaryotic cell to grow and divide, intricately coordinated action of numerous proteins is required to ensure proper cell-cycle progression. The fission yeast Schizosaccharomyces pombe has been instrumental in elucidating the fundamental principles of cell-cycle control. Mutations in S. pombe 'cut' (cell untimely torn) genes cause failed coordination between cell and nuclear division, resulting in catastrophic mitosis. Deletion of cbf11, a fission yeast CSL transcription factor gene, triggers a 'cut' phenotype, but the precise role of Cbf11 in promoting mitotic fidelity is not known. We report that Cbf11 directly activates the transcription of the acetyl-coenzyme A carboxylase gene cut6, and the biotin uptake/biosynthesis genes vht1 and bio2, with the former 2 implicated in mitotic fidelity. Cbf11 binds to a canonical, metazoan-like CSL response element (GTGGGAA) in the cut6 promoter. Expression of Cbf11 target genes shows apparent oscillations during the cell cycle using temperature-sensitive cdc25-22 and cdc10-M17 block-release experiments, but not with other synchronization methods. The penetrance of catastrophic mitosis in cbf11 and cut6 mutants is nutrient-dependent. We also show that drastic decrease in biotin availability arrests cell proliferation but does not cause mitotic defects. Taken together, our results raise the possibility that CSL proteins play conserved roles in regulating cell-cycle progression, and they could guide experiments into mitotic CSL functions in mammals.","authors":"Převorovský M, Oravcová M, Zach R, Jordáková A, Bähler J, Půta F, Folk P","authors_abbrev":"Převorovský M et al.","pubmed_publication_date":"16 Nov 2016","pubmed_entrez_date":"2016-10-01","publication_year":"2016","canto_session_key":"817e75f5ee938916","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Martin Převorovský","canto_first_approved_date":"2016-12-19 20:32:40","canto_approved_date":"2024-06-26 09:38:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-14 13:23:11","canto_added_date":"2016-10-02 00:15:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Martin Převorovský","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.08","SPCC1235.02","SPAC56E4.04c","SPAC1B3.16c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-12-19"},{"uniquename":"PMID:23217327","title":"Cowchock syndrome is associated with a mutation in apoptosis-inducing factor.","citation":"Am J Hum Genet 2012 Dec 07;91(6):1095-102","abstract":"Cowchock syndrome (CMTX4) is a slowly progressive X-linked recessive disorder with axonal neuropathy, deafness, and cognitive impairment. The disease locus was previously mapped to an 11 cM region at chromosome X: q24-q26. Exome sequencing of an affected individual from the originally described family identified a missense change c.1478A>T (p.Glu493Val) in AIFM1, the gene encoding apoptosis-inducing factor (AIF) mitochondrion-associated 1. The change is at a highly conserved residue and cosegregated with the phenotype in the family. AIF is an FAD-dependent NADH oxidase that is imported into mitochondria. With apoptotic insults, a N-terminal transmembrane linker is cleaved off, producing a soluble fragment that is released into the cytosol and then transported into the nucleus, where it triggers caspase-independent apoptosis. Another AIFM1 mutation that predicts p.Arg201del has recently been associated with severe mitochondrial encephalomyopathy in two infants by impairing oxidative phosphorylation. The c.1478A>T (p.Glu493Val) mutation found in the family reported here alters the redox properties of the AIF protein and results in increased cell death via apoptosis, without affecting the activity of the respiratory chain complexes. Our findings expand the spectrum of AIF-related disease and provide insight into the effects of AIFM1 mutations.","doi":"10.1016/j.ajhg.2012.10.008","authors":"Rinaldi C, Grunseich C, Sevrioukova IF, Schindler A, Horkayne-Szakaly I, Lamperti C, Landouré G, Kennerson ML, Burnett BG, Bönnemann C, Biesecker LG, Ghezzi D, Zeviani M, Fischbeck KH","authors_abbrev":"Rinaldi C et al.","pubmed_publication_date":"07 Dec 2012","pubmed_entrez_date":"2012-12-11","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26F1.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:31390298","title":"Conserved NDR/LATS kinase controls RAS GTPase activity to regulate cell growth and chronological lifespan.","citation":"Mol Biol Cell 2019 Sep 15;30(20):2598-2616","abstract":"Adaptation to the nutritional environment is critical for all cells. RAS GTPase is a highly conserved GTP-binding protein with crucial functions for cell growth and differentiation in response to environmental conditions. Here, we describe a novel mechanism connecting RAS GTPase to nutrient availability in fission yeast. We report that the conserved NDR/LATS kinase Orb6 responds to nutritional cues and regulates Ras1 GTPase activity. Orb6 increases the protein levels of an Ras1 GTPase activator, the guanine nucleotide exchange factor Efc25, by phosphorylating Sts5, a protein bound to  efc25  mRNA. By manipulating the extent of Orb6-mediated Sts5 assembly into RNP granules, we can modulate Efc25 protein levels, Ras1 GTPase activity, and, as a result, cell growth and cell survival. Thus, we conclude that the Orb6-Sts5-Ras1 regulatory axis plays a crucial role in promoting cell adaptation, balancing the opposing demands of promoting cell growth and extending chronological lifespan.","doi":"10.1091/mbc.E19-03-0172","authors":"Chen C, Rodriguez Pino M, Haller PR, Verde F","authors_abbrev":"Chen C et al.","pubmed_publication_date":"15 Sep 2019","pubmed_entrez_date":"2019-08-08","publication_year":"2019","canto_session_key":"109bcacce0035947","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-08-09 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32621218","title":"The Genome3D Consortium for Structural Annotations of Selected Model Organisms.","citation":"Methods Mol Biol 2020;2165:27-67","abstract":"Genome3D consortium is a collaborative project involving protein structure prediction and annotation resources developed by six world-leading structural bioinformatics groups, based in the United Kingdom (namely Blundell, Murzin, Gough, Sternberg, Orengo, and Jones). The main objective of Genome3D serves as a common portal to provide both predicted models and annotations of proteins in model organisms, using several resources developed by these labs such as CATH-Gene3D, DOMSERF, pDomTHREADER, PHYRE, SUPERFAMILY, FUGUE/TOCATTA, and VIVACE. These resources primarily use SCOP- and/or CATH-based protein domain assignments. Another objective of Genome3D is to compare structural classifications of protein domains in CATH and SCOP databases and to provide a consensus mapping of CATH and SCOP protein superfamilies. CATH/SCOP mapping analyses led to the identification of total of 1429 consensus superfamilies.Currently, Genome3D provides structural annotations for ten model organisms, including Homo sapiens, Arabidopsis thaliana, Mus musculus, Escherichia coli, Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Plasmodium falciparum, Staphylococcus aureus, and Schizosaccharomyces pombe. Thus, Genome3D serves as a common gateway to each structure prediction/annotation resource and allows users to perform comparative assessment of the predictions. It, thus, assists researchers to broaden their perspective on structure/function predictions of their query protein of interest in selected model organisms.","doi":"10.1007/978-1-0716-0708-4_3","authors":"Waman VP, Blundell TL, Buchan DWA, Gough J, Jones D, Kelley L, Murzin A, Pandurangan AP, Sillitoe I, Sternberg M, Torres P, Orengo C","authors_abbrev":"Waman VP et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-07-05","publication_year":"2020","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2020-07-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19745054","title":"Selection for minimization of translational frameshifting errors as a factor in the evolution of codon usage.","citation":"Nucleic Acids Res 2009 Nov;37(20):6799-810","abstract":"In a wide range of genomes, it was observed that the usage of synonymous codons is biased toward specific codons and codon patterns. Factors that are implicated in the selection for codon usage include facilitation of fast and accurate translation. There are two types of translational errors: missense errors and processivity errors. There is considerable evidence in support of the hypothesis that codon usage is optimized to minimize missense errors. In contrast, little is known about the relationship between codon usage and frameshifting errors, an important form of processivity errors, which appear to occur at frequencies comparable to the frequencies of missense errors. Based on the recently proposed pause-and-slip model of frameshifting, we developed Frameshifting Robustness Score (FRS). We used this measure to test if the pattern of codon usage indicates optimization against frameshifting errors. We found that the FRS values of protein-coding sequences from four analyzed genomes (the bacteria Bacillus subtilis and Escherichia coli, and the yeasts Saccharomyces cerevisiae and Schizosaccharomyce pombe) were typically higher than expected by chance. Other properties of FRS patterns observed in B. subtilis, S. cerevisiae and S. pombe, such as the tendency of FRS to increase from the 5'- to 3'-end of protein-coding sequences, were also consistent with the hypothesis of optimization against frameshifting errors in translation. For E. coli, the results of different tests were less consistent, suggestive of a much weaker optimization, if any. Collectively, the results fit the concept of selection against mistranslation-induced protein misfolding being one of the factors shaping the evolution of both coding and non-coding sequences.","doi":"10.1093/nar/gkp712","authors":"Huang Y, Koonin EV, Lipman DJ, Przytycka TM","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"Nov 2009","pubmed_entrez_date":"2009-09-12","publication_year":"2009","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012652","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.80"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12097341","title":"The role of lineage-specific gene family expansion in the evolution of eukaryotes.","citation":"Genome Res 2002 Jul;12(7):1048-59","abstract":"A computational procedure was developed for systematic detection of lineage-specific expansions (LSEs) of protein families in sequenced genomes and applied to obtain a census of LSEs in five eukaryotic species, the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, the nematode Caenorhabditis elegans, the fruit fly Drosophila melanogaster, and the green plant Arabidopsis thaliana. A significant fraction of the proteins encoded in each of these genomes, up to 80% in A. thaliana, belong to LSEs. Many paralogous gene families in each of the analyzed species are almost entirely comprised of LSEs, indicating that their diversification occurred after the divergence of the major lineages of the eukaryotic crown group. The LSEs show readily discernible patterns of protein functions. The functional categories most prone to LSE are structural proteins, enzymes involved in an organism's response to pathogens and environmental stress, and various components of signaling pathways responsible for specificity, including ubiquitin ligase E3 subunits and transcription factors. The functions of several previously uncharacterized, vastly expanded protein families were predicted through in-depth protein sequence analysis, for example, small-molecule kinases and methylases that are expanded independently in the fly and in the nematode. The functions of several other major LSEs remain mysterious; these protein families are attractive targets for experimental discovery of novel, lineage-specific functions in eukaryotes. LSEs seem to be one of the principal means of adaptation and one of the most important sources of organizational and regulatory diversity in crown-group eukaryotes.","authors":"Lespinet O, Wolf YI, Koonin EV, Aravind L","authors_abbrev":"Lespinet O et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-07-05","publication_year":"2002","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9388669","title":"Kexin activation requires both the removal and the destruction of the pro-sequence.","citation":"Biochem Soc Trans 1997 Aug;25(3):445S","abstract":"","authors":"Powner D, Davey J","authors_abbrev":"Powner D et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"843228633c4b7012","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-03-22 19:21:13","canto_approved_date":"2024-08-10 08:51:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-21 15:23:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-03-22"},{"uniquename":"PMID:8203158","title":"A homologous cell-free system for studying protein translocation across the endoplasmic reticulum membrane in fission yeast.","citation":"Yeast 1994 Feb;10(2):159-72","abstract":"We report the development of a homologous in vitro assay system for analysing translocation of proteins across the endoplasmic reticulum (ER) membrane of the fission yeast Schizosaccharomyces pombe. Our protocol for preparing an S. pombe extract capable of translating natural messenger RNAs was modified from a procedure previously used for Saccharomyces cerevisiae, in which cells are lysed in a bead-beater. However, we were unable to prepare fission yeast microsomes active in protein translocation using existing budding yeast protocols. Instead, our most efficient preparations were isolated by fractionating spheroplasts, followed by extensive washing and size exclusion chromatography of the crude membranes. Translocation of two ER-targeted proteins, pre-acid phosphatase from S. pombe and prepro-alpha-factor from S. cerevisiae, was monitored using two distinct assays. First, evidence that a fraction of both proteins was sequestered within membrane-enclosed vesicles was provided by resistance to exogenously added protease. Second, the protected fraction of each protein was converted to a higher molecular weight, glycosylated form; attachment of carbohydrate to the translocated proteins was confirmed by their ability to bind Concanavalin A-Sepharose. Finally, we examined whether proteins could be translocated across fission yeast microsomal membranes after their synthesis was complete. Our results indicate that S. cerevisiae prepro-alpha-factor can be post-translationally imported into the fission yeast ER, while S. pombe pre-acid phosphatase crosses the membrane only by a co-translational mechanism.","authors":"Brennwald P, Wise JA","authors_abbrev":"Brennwald P et al.","pubmed_publication_date":"Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9154834","title":"Discrete roles of the Spc1 kinase and the Atf1 transcription factor in the UV response of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1997 Jun;17(6):3356-63","abstract":"Exposure of mammalian cells to UV irradiation or alkylating agents leads to the activation of the c-Jun N-terminal kinase and p38 stress-activated protein kinase cascades, phosphorylation of c-Jun and ATF-2 bZIP transcription factors, and finally to selective induction of gene expression. This UV response is believed to be crucially important for cell survival, although conclusive evidence is lacking. Here, we address this issue by investigating a homologous UV response pathway in the fission yeast Schizosaccharomyces pombe. In fission yeast cells, UV irradiation induces activation of Spc1 stress-activated protein kinase, which in turn phosphorylates the Atf1 bZIP transcription factor. spc1 mutants are hypersensitive to killing by UV at a level equivalent to some checkpoint rad mutants. Whereas checkpoint rad mutants fail to arrest division in response to DNA damage, spc1 mutants are defective at resuming cell division after UV exposure. Levels of basal and UV-induced transcription of ctt1+, which encodes a catalase believed important for combating oxidative stress caused by UV, are extremely low in spc1 mutants. Atf1 is required for UV-induced transcription of ctt1+, but atf1 mutants are not hypersensitive to killing by UV. This surprising finding is explained by the observation that ctt1+ basal expression is unaffected in atf1 single mutant and spc1 atf1 double mutant cells, suggesting that unphosphorylated Atf1 represses ctt1+ expression in spc1 cells. In fact, the level of UV sensitivity of spc1 atf1 double mutant cells is intermediate between those of the wild type and spc1 mutants. These findings suggest the following. (i) Key properties of UV response mechanisms are remarkably similar in mammals and S. pombe. (ii) Activation of Spc1 kinase greatly enhances survival of UV-irradiated cells. (iii) Induction of gene expression by activation of Atf1 may not be the most important mechanism by which stress-activated kinases function in the UV response.","authors":"Degols G, Russell P","authors_abbrev":"Degols G et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"d4eae3f3d5d8d194","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-04 15:53:06","canto_approved_date":"2020-11-12 17:04:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-29 10:50:03","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC19D5.01","SPCC757.07c","SPAC8E11.02c","SPAC26F1.10c","SPBC29B5.01","SPAC13G6.01c","SPAC24B11.06c","SPAC20G8.01","SPAC1952.07"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2018-10-04"},{"uniquename":"PMID:17190600","title":"Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair.","citation":"Cell 2006 Dec 29;127(7):1361-73","abstract":"Histone lysine methylation has been linked to the recruitment of mammalian DNA repair factor 53BP1 and putative fission yeast homolog Crb2 to DNA double-strand breaks (DSBs), but how histone recognition is achieved has not been established. Here we demonstrate that this link occurs through direct binding of 53BP1 and Crb2 to histone H4. Using X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, we show that, despite low amino acid sequence conservation, both 53BP1 and Crb2 contain tandem tudor domains that interact with histone H4 specifically dimethylated at Lys20 (H4-K20me2). The structure of 53BP1/H4-K20me2 complex uncovers a unique five-residue 53BP1 binding cage, remarkably conserved in the structure of Crb2, that best accommodates a dimethyllysine but excludes a trimethyllysine, thus explaining the methylation state-specific recognition of H4-K20. This study reveals an evolutionarily conserved molecular mechanism of targeting DNA repair proteins to DSBs by direct recognition of H4-K20me2.","authors":"Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, Chen J, Mer G","authors_abbrev":"Botuyan MV et al.","pubmed_publication_date":"29 Dec 2006","pubmed_entrez_date":"2006-12-28","publication_year":"2006","canto_session_key":"52732769f3229ed9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-15 10:30:25","canto_approved_date":"2025-04-11 13:54:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-15 10:29:08","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.12","SPBC342.05","SPAC1834.03c","SPBC8D2.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-15","pdb_entries":[{"pdb_id":"2fhd","gene_chains":[{"gene_uniquename":"SPBC342.05","chain":"A/B/C","position":"358-507"}],"title":"Crystal structure of Crb2 tandem tudor domains","entry_authors":"Lee J,Botuyan MV,Thompson JR,Mer G","entry_authors_abbrev":"Lee J et al.","reference_uniquename":"PMID:17190600","experimental_method":"X-ray","resolution":"2.4"}]},{"uniquename":"PMID:34798057","title":"Transcription-wide mapping of dihydrouridine reveals that mRNA dihydrouridylation is required for meiotic chromosome segregation.","citation":"Mol Cell 2022 Jan 20;82(2):404-419.e9","abstract":"The epitranscriptome has emerged as a new fundamental layer of control of gene expression. Nevertheless, the determination of the transcriptome-wide occupancy and function of RNA modifications remains challenging. Here we have developed Rho-seq, an integrated pipeline detecting a range of modifications through differential modification-dependent rhodamine labeling. Using Rho-seq, we confirm that the reduction of uridine to dihydrouridine (D) by the Dus reductase enzymes targets tRNAs in E. coli and fission yeast. We find that the D modification is also present on fission yeast mRNAs, particularly those encoding cytoskeleton-related proteins, which is supported by large-scale proteome analyses and ribosome profiling. We show that the α-tubulin encoding mRNA nda2 undergoes Dus3-dependent dihydrouridylation, which affects its translation. The absence of the modification on nda2 mRNA strongly impacts meiotic chromosome segregation, resulting in low gamete viability. Applying Rho-seq to human cells revealed that tubulin mRNA dihydrouridylation is evolutionarily conserved.","doi":"10.1016/j.molcel.2021.11.003","authors":"Finet O, Yague-Sanz C, Krüger LK, Tran P, Migeot V, Louski M, Nevers A, Rougemaille M, Sun J, Ernst FGM, Wacheul L, Wery M, Morillon A, Dedon P, Lafontaine DLJ, Hermand D","authors_abbrev":"Finet O et al.","pubmed_publication_date":"20 Jan 2022","pubmed_entrez_date":"2021-11-19","publication_year":"2022","canto_session_key":"d86816507d979037","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Carlo Yague-Sanz","canto_first_approved_date":"2021-12-08 19:18:27","canto_approved_date":"2024-04-04 15:23:39","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-12-02 09:42:14","canto_added_date":"2021-11-21 01:15:03","annotation_curators":[{"name":"Carlo Yague-Sanz","community_curator":true,"annotation_count":23,"orcid":"0000-0002-9941-9703","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16.04","SPBC1709.06","SPAC821.09","SPBC36B7.04","SPBC16A3.15c","SPBC12D12.03","SPBC1A4.08c","SPBC26H8.07c","SPCC777.15"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2021-12-08"},{"uniquename":"PMID:1441756","title":"Sequence of the genes encoding subunits A and B of the vacuolar H(+)-ATPase of Schizosaccharomyces pombe.","citation":"Yeast 1992 Sep;8(9):791-9","abstract":"The genes encoding subunits A (vma1) and B (vma2) of the vacuolar H(+)-ATPase from Schizosaccharomyces pombe were cloned by hybridization to cDNAs of the homologous genes in Neurospora crassa. Both genes are interrupted by introns, two in vma1 and four in vma2. Positions of introns do not appear to be conserved when compared to those of N. crassa. The subunit A gene encodes a single product of 619 amino acids and is not interrupted by the coding sequence for a second product as found for Saccharomyces cerevisiae (Kane, P. K., Yamashiro, C. T., Wolczyk, D. F., Neff, N., Goebl, M., and Stevens, T. H. (1990). Science 250, 651-657).","authors":"Ghislain M, Bowman EJ","authors_abbrev":"Ghislain M et al.","pubmed_publication_date":"Sep 1992","pubmed_entrez_date":"1992-09-01","publication_year":"1992","canto_session_key":"45d96a01b0abfdad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:08:53","canto_approved_date":"2018-12-22 20:08:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 20:08:43","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:15620657","title":"Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and localization of an essential splicing factor in fission yeast.","citation":"Curr Biol 2004 Dec 29;14(24):2283-8","abstract":"Hub1/Ubl5 is a member of the family of ubiquitin-like proteins (UBLs). The tertiary structure of Hub1 is similar to that of ubiquitin; however, it differs from known modifiers in that there is no conserved glycine residue near the C terminus which, in ubiquitin and UBLs, is required for covalent modification of target proteins. Instead, there is a conserved dityrosine motif proximal to the terminal nonconserved amino acid. In S. cerevisiae, high molecular weight adducts can be formed in vivo from Hub1, but the structure of these adducts is not known, and they could be either covalent or noncovalent. The budding yeast HUB1 gene is not essential, but Delta hub1 mutants display defects in mating. Here, we report that fission yeast hub1 is an essential gene, whose loss results in cell cycle defects and inefficient pre-mRNA splicing. A screen for Hub1 interactors identified Snu66, a component of the U4/U6.U5 tri-snRNP splicing complex. Furthermore, overexpression of Snu66 suppresses the lethality of a hub1ts mutant. In cells lacking functional hub1, the nuclear localization of Snu66 is disrupted, suggesting that an important role for Hub1 is the correct subcellular targeting of Snu66, although our data suggest that Hub1 is likely to perform other roles in splicing as well.","authors":"Wilkinson CR, Dittmar GA, Ohi MD, Uetz P, Jones N, Finley D","authors_abbrev":"Wilkinson CR et al.","pubmed_publication_date":"29 Dec 2004","pubmed_entrez_date":"2004-12-29","publication_year":"2004","canto_session_key":"2ff609ae8b8a44e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-06-01 13:14:52","canto_approved_date":"2022-07-26 17:02:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-13 13:26:47","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":35,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.01","SPAC167.03c","SPAC56E4.04c","SPAC8E11.02c","SPAC644.12","SPCC126.03","SPAC29E6.02","SPBC11B10.09","SPBC3B9.07c","SPBC31E1.03","SPBC215.15"],"gene_count":11,"ltp_gene_count":4,"approved_date":"2017-06-01"},{"uniquename":"PMID:16782006","title":"Dynamics of the formin for3p in actin cable assembly.","citation":"Curr Biol 2006 Jun 20;16(12):1161-70","abstract":"Formins are a conserved family of actin nucleators responsible for the assembly of diverse actin structures such as cytokinetic rings and filopodia. In the fission yeast Schizosaccharomyces pombe, the formin for3p is necessary for the formation of actin cables, which are bundles of short parallel actin filaments that regulate cell polarity. These filaments are largely organized with their barbed ends facing the cell tip, where for3p is thought to function in their assembly.\nHere, using a functional for3p-3GFP fusion expressed at endogenous levels, we find that for3p localizes to small dots that appear transiently at cell tips and then move away on actin cables at a rate of 0.3 microm/s. These movements were dependent on the continuous assembly of actin in cables, on the ability of for3p to bind actin within its FH2 domain, and on profilin and bud6p, two formin binding proteins that promote formin activity. Bud6p transiently colocalizes with for3p at the cell tip and stays behind at the cell tip when for3p detaches.\nThese findings suggest a new model for actin cable assembly: a for3p particle is activated and promotes the assembly of a short actin filament at the cell tip for only seconds. For3p and the actin filament may then be released from the cell tip and carried passively into the cell interior by retrograde flow of actin filaments in the cable. These studies reveal a complex and dynamic cycle of formin regulation and actin cable assembly in vivo.","authors":"Martin SG, Chang F","authors_abbrev":"Martin SG et al.","pubmed_publication_date":"20 Jun 2006","pubmed_entrez_date":"2006-06-20","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19563107","title":"Chromatin immunoprecipitation of replication factors moving with the replication fork.","citation":"Methods Mol Biol 2009;521:191-202","abstract":"Replication of chromosomes involves a variety of replication proteins including DNA polymerases, DNA helicases, and other accessory factors. Many of these proteins are known to localize at replication forks and travel with them as components of the replisome complex. Other proteins do not move with replication forks but still play an essential role in DNA replication. Therefore, in order to understand the mechanisms of DNA replication and its controls, it is important to examine localization of each replication factor. Here we describe a chromatin immunoprecipitation (ChIP) method to locate a replication factor at the replication fork. Defining the localization of replication proteins should provide important insight into mechanistic understanding of the regulation of the DNA replication process.","doi":"10.1007/978-1-60327-815-7_10","authors":"Rapp JB, Ansbach AB, Noguchi C, Noguchi E","authors_abbrev":"Rapp JB et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28656962","title":"Negative regulation of EGFR signalling by the human folliculin tumour suppressor protein.","citation":"Nat Commun 2017 Jun 28;8:15866","abstract":"Germline mutations in the Folliculin (FLCN) tumour suppressor gene result in fibrofolliculomas, lung cysts and renal cancers, but the precise mechanisms of tumour suppression by FLCN remain elusive. Here we identify Rab7A, a small GTPase important for endocytic trafficking, as a novel FLCN interacting protein and demonstrate that FLCN acts as a Rab7A GTPase-activating protein. FLCN -/-  cells display slower trafficking of epidermal growth factor receptors (EGFR) from early to late endosomes and enhanced activation of EGFR signalling upon ligand stimulation. Reintroduction of wild-type FLCN, but not tumour-associated FLCN mutants, suppresses EGFR signalling in a Rab7A-dependent manner. EGFR signalling is elevated in FLCN -/-  tumours and the EGFR inhibitor afatinib suppresses the growth of human FLCN -/-  cells as tumour xenografts. The functional interaction between FLCN and Rab7A appears conserved across species. Our work highlights a mechanism explaining, at least in part, the tumour suppressor function of FLCN.","doi":"10.1038/ncomms15866","authors":"Laviolette LA, Mermoud J, Calvo IA, Olson N, Boukhali M, Steinlein OK, Roider E, Sattler EC, Huang D, Teh BT, Motamedi M, Haas W, Iliopoulos O","authors_abbrev":"Laviolette LA et al.","pubmed_publication_date":"28 Jun 2017","pubmed_entrez_date":"2017-06-29","publication_year":"2017","canto_session_key":"12517e47bd2ece51","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-06-08 09:57:32","canto_approved_date":"2023-06-08 09:59:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-04-03 13:49:30","canto_added_date":"2023-04-03 13:33:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC24C6.08c","SPAPB1A10.10c","SPAPB1E7.12","SPAC13G6.07c","SPBC405.04c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2023-06-08"},{"uniquename":"PMID:21976700","title":"Nse1-dependent recruitment of Smc5/6 to lesion-containing loci contributes to the repair defects of mutant complexes.","citation":"Mol Biol Cell 2011 Dec;22(23):4669-82","abstract":"Of the three structural maintenance of chromosomes (SMC) complexes, Smc5/6 remains the most poorly understood. Genetic studies have shown that Smc5/6 mutants are defective in homologous recombination (HR), and consistent with this, Smc5/6 is enriched at lesions. However, Smc5/6 is essential for viability, but HR is not, and the terminal phenotype of null Smc5/6 mutants is mitotic failure. Here we analyze the function of Nse1, which contains a variant RING domain that is characteristic of ubiquitin ligases. Whereas deletion of this domain causes DNA damage sensitivity and mitotic failure, serine mutations in conserved cysteines do not. However, these mutations suppress the DNA damage sensitivity of Smc5/6 hypomorphs but not that of HR mutants and remarkably decrease the recruitment of Smc5/6 to loci containing lesions marked for HR-mediated repair. Analysis of DNA repair pathways in suppressed double mutants suggests that lesions are channeled into recombination-dependent and error-free postreplication repair. Thus the HR defect in Smc5/6 mutants appears to be due to the presence of dysfunctional complexes at lesions rather than to reflect an absolute requirement for Smc5/6 to complete HR.","doi":"10.1091/mbc.E11-03-0272","authors":"Tapia-Alveal C, O'Connell MJ","authors_abbrev":"Tapia-Alveal C et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-10-07","publication_year":"2011","canto_session_key":"c29c5bd54094a6f5","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2022-11-10 18:13:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-10 18:11:25","canto_added_date":"2012-06-12 03:08:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31600629","title":"Evolutionary innovation, fungal cell biology, and the lateral gene transfer of a viral KilA-N domain.","citation":"Curr Opin Genet Dev 2019 Oct;58-59:103-110","abstract":"Fungi are found in diverse ecological niches as primary decomposers, mutualists, or parasites of plants and animals. Although animals and fungi share a common ancestor, fungi dramatically diversified their life cycle, cell biology, and metabolism as they evolved and colonized new niches. This review focuses on a family of fungal transcription factors (Swi4/Mbp1, APSES, Xbp1, Bqt4) derived from the lateral gene transfer of a KilA-N domain commonly found in prokaryotic and eukaryotic DNA viruses. These virus-derived fungal regulators play central roles in cell cycle, morphogenesis, sexual differentiation, and quiescence. We consider the possible origins of KilA-N and how this viral DNA binding domain came to be intimately associated with fungal processes.","doi":"10.1016/j.gde.2019.08.004","authors":"Medina EM, Walsh E, Buchler NE","authors_abbrev":"Medina EM et al.","pubmed_publication_date":"Oct 2019","pubmed_entrez_date":"2019-10-11","publication_year":"2019","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2020-08-19 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18644893","title":"Spindle checkpoint activation at meiosis I advances anaphase II onset via meiosis-specific APC/C regulation.","citation":"J Cell Biol 2008 Jul 28;182(2):277-88","abstract":"During mitosis, the spindle assembly checkpoint (SAC) inhibits the Cdc20-activated anaphase-promoting complex/cyclosome (APC/C(Cdc20)), which promotes protein degradation, and delays anaphase onset to ensure accurate chromosome segregation. However, the SAC function in meiotic anaphase regulation is poorly understood. Here, we examined the SAC function in fission yeast meiosis. As in mitosis, a SAC factor, Mad2, delayed anaphase onset via Slp1 (fission yeast Cdc20) when chromosomes attach to the spindle improperly. However, when the SAC delayed anaphase I, the interval between meiosis I and II shortened. Furthermore, anaphase onset was advanced and the SAC effect was reduced at meiosis II. The advancement of anaphase onset depended on a meiosis-specific, Cdc20-related factor, Fzr1/Mfr1, which contributed to anaphase cyclin decline and anaphase onset and was inefficiently inhibited by the SAC. Our findings show that impacts of SAC activation are not confined to a single division at meiosis due to meiosis-specific APC/C regulation, which has probably been evolved for execution of two meiotic divisions.","doi":"10.1083/jcb.200802053","authors":"Yamamoto A, Kitamura K, Hihara D, Hirose Y, Katsuyama S, Hiraoka Y","authors_abbrev":"Yamamoto A et al.","pubmed_publication_date":"28 Jul 2008","pubmed_entrez_date":"2008-07-23","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41201383","title":"Combinatorial Analyses of Pre-mRNA Splicing-Defective Mutants Reveal Differential Quantitative Requirements for Shelterin in Distinct Telomere Functions.","citation":"Genes Cells 2025 Nov;30(6):e70064","abstract":"Telomeres perform multiple functions to maintain genome stability, including telomere length regulation, chromosome end protection, and meiotic chromosome dynamics. These functions are governed by shelterin, a telomere-binding protein complex. Here, we show that Tls1 and Cay1 act at distinct steps in pre-mRNA splicing, specifically ensuring sufficient protein levels of Schizosaccharomyces pombe shelterin components Rap1 and Poz1, which are critical for telomere maintenance. Accordingly, deletion of tls1 +  and cay1 +  synergistically reduced Rap1 and Poz1 protein levels. Analyses of the phenotypes of single and double tls1∆ and cay1∆ mutants indicated that different telomere functions vary in their dependence on Rap1 levels: telomere length regulation and, to a lesser extent, meiosis require higher protein abundance, whereas chromosome end protection can be sustained with minimal amounts. These findings reveal a hierarchical requirement for Rap1 across telomere functions.","doi":"10.1111/gtc.70064","authors":"Takeuchi M, Otsubo Y, Kanoh J","authors_abbrev":"Takeuchi M et al.","pubmed_publication_date":"Nov 2025","pubmed_entrez_date":"2025-11-07","publication_year":"2025","canto_session_key":"25fc525721d67023","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junko Kanoh","canto_first_approved_date":"2026-02-26 11:06:22","canto_approved_date":"2026-03-06 12:52:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-02-14 16:55:59","canto_added_date":"2025-11-08 00:25:04","annotation_curators":[{"name":"Junko Kanoh","community_curator":true,"annotation_count":26,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.01","SPAC26H5.06","SPAC22F8.10c","SPAC6F6.16c","SPBC31F10.11c","SPCC188.07","SPBC2F12.12c","SPBC337.06c","SPAC29E6.02","SPAC6F6.17","SPAC16A10.07c","SPBC1778.02","SPAC9.03c","SPAC4D7.13","SPAC15A10.15","SPAC19G12.13c","SPBC19C2.08","SPAC29A4.08c","SPCC63.11"],"gene_count":19,"ltp_gene_count":13,"approved_date":"2026-02-26"},{"uniquename":"PMID:39527203","title":"A Rapidly Inducible DNA Double-Strand Break to Monitor Telomere Formation, DNA Repair, and Checkpoint Activation.","citation":"Methods Mol Biol 2025;2862:209-221","abstract":"The study of processes that govern genome integrity has been augmented by the ability to create a precise DNA double-strand break (DSB) in a short period of time that allows the kinetics of DNA metabolism and protein recruitment to be followed. Defined DSBs are made by expressing endonucleases with long recognition sites that are rare or absent in the genome, and require that the endonuclease is only active when induced. Research in this area in Schizosaccharomyces pombe was limited because rapidly inducible promoters were not available until around 2005, and several rapidly inducible DSB systems are now available. Here, we describe a system to rapidly induce a modified I-SceI endonuclease that can generate a DSB 20 min after induction. I-SceI has no recognition sites in the S. pombe genome, allowing the introduction of complex substrates to monitor the effects of a new DSB in real time. This chapter describes how I-SceI can be most efficiently induced and a simple cell length measurement assay to monitor cell cycle checkpoint activation from a single DSB.","doi":"10.1007/978-1-0716-4168-2_15","authors":"Zhang H, Kerr C, Audry J, Runge KW","authors_abbrev":"Zhang H et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31610624","title":"Optimization of a microarray for fission yeast.","citation":"Genomics Inform 2019 Sep;17(3):e28","abstract":"Bar-code (tag) microarrays of yeast gene-deletion collections facilitate the systematic identification of genes required for growth in any condition of interest. Anti-sense strands of amplified bar-codes hybridize with ~10,000 (5,000 each for up- and down-tags) different kinds of sense-strand probes on an array. In this study, we optimized the hybridization processes of an array for fission yeast. Compared to the first version of the array (11 µm, 100K) consisting of three sectors with probe pairs (perfect match and mismatch), the second version (11 µm, 48K) could represent ~10,000 up-/down-tags in quadruplicate along with 1,508 negative controls in quadruplicate and a single set of 1,000 unique negative controls at random dispersed positions without mismatch pairs. For PCR, the optimal annealing temperature (maximizing yield and minimizing extra bands) was 58°C for both tags. Intriguingly, up-tags required 3 higher amounts of blocking oligonucleotides than down-tags. A 1:1 mix ratio between up- and down-tags was satisfactory. A lower temperature (25°C) was optimal for cultivation instead of a normal temperature (30°C) because of extra temperature-sensitive mutants in a subset of the deletion library. Activation of frozen pooled cells for >1 day showed better resolution of intensity than no activation. A tag intensity analysis showed that tag(s) of 4,316 of the 4,526 strains tested were represented at least once; 3,706 strains were represented by both tags, 4,072 strains by up-tags only, and 3,950 strains by down-tags only. The results indicate that this microarray will be a powerful analytical platform for elucidating currently unknown gene functions.","doi":"10.5808/GI.2019.17.3.e28","authors":"Kim DU, Lee M, Han S, Nam M, Lee S, Lee J, Woo J, Kim D, Hoe KL","authors_abbrev":"Kim DU et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-10-15","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-10-16 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011122","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33617628","title":"Implementation of dCas9-mediated CRISPRi in the fission yeast Schizosaccharomyces pombe.","citation":"G3 (Bethesda) 2021 Apr 15;11(4)","abstract":"Controllable and reversible transcriptional repression is an essential method to study gene functions. A systematic knock-down method using catalytically inactive Cas9 (dCas9) was originally established in bacteria. dCas9 forms a ribonucleoprotein with a small guide RNA and uses it to recognize a specific DNA sequence via Watson-Crick base-pairing. When specifically bound to a targeted DNA, dCas9 impairs RNA polymerase activity and represses transcription of that target gene. This technology, CRISPRi, has been implemented in several organisms, but not in Schizosaccharomyces pombe using dCas9. Here, we provide a plasmid that expresses dCas9 and sgRNA in fission yeast. With this plasmid, CRISPRi repressed endogenous gene transcription by as much as 87%. This transcriptional repression method is controllable, reversible, and efficient enough to alter cellular phenotypes. Here, we offer a CRISPRi method to choose proper targeting sequences for transcriptional repression in fission yeast. Implementation of CRISPRi will help to reveal gene functions and to develop tools based on dCas9 technology in S. pombe.","doi":"10.1093/g3journal/jkab051","authors":"Ishikawa K, Soejima S, Masuda F, Saitoh S","authors_abbrev":"Ishikawa K et al.","pubmed_publication_date":"15 Apr 2021","pubmed_entrez_date":"2021-02-22","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-02-24 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19906584","title":"Cell shape and cell division in fission yeast.","citation":"Curr Biol 2009 Sep 15;19(17):R823-7","abstract":"The fission yeast Schizosaccharomyces pombe has served as an important model organism for investigating cellular morphogenesis. This unicellular rod-shaped fission yeast grows by tip extension and divides by medial fission. In particular, microtubules appear to define sites of polarized cell growth by delivering cell polarity factors to the cell tips. Microtubules also position the cell nucleus at the cell middle, marking sites of cell division. Here, we review the microtubule-dependent mechanisms that regulate cell shape and cell division in fission yeast.","doi":"10.1016/j.cub.2009.08.012","authors":"Piel M, Tran PT","authors_abbrev":"Piel M et al.","pubmed_publication_date":"15 Sep 2009","pubmed_entrez_date":"2009-11-13","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPAB475","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15713656","title":"Constitutive activation of the fission yeast pheromone-responsive pathway induces ectopic meiosis and reveals ste11 as a mitogen-activated protein kinase target.","citation":"Mol Cell Biol 2005 Mar;25(5):2045-59","abstract":"In the fission yeast Schizosaccharomyces pombe, meiosis normally takes place in diploid zygotes resulting from conjugation of haploid cells. In the present study, we report that the expression of a constitutively activated version of the pheromone-responsive mitogen-activated protein kinase kinase kinase (MAP3K) Byr2 can induce ectopic meiosis directly in haploid cells. We find that the Ste11 transcription factor becomes constitutively expressed in these cells and that the expression of pheromone-responsive genes no longer depends on nitrogen starvation. Epistasis analysis revealed that these conditions bypassed the requirement for the meiotic activator Mei3. Since Mei3 is normally needed for inactivation of the meiosis-repressing protein kinase Pat1, this finding suggests that the strong Byr2 signal causes inactivation of Pat1 by an alternative mechanism. Consistent with this possibility, we found that haploid meiosis was dramatically reduced when Ste11 was mutated to mimic phosphorylation by Pat1. The mutation of two putative MAPK sites in Ste11 also dramatically reduced the level of haploid meiosis, suggesting that Ste11 is a direct target of Spk1. Supporting this, we show that Spk1 can interact physically with Ste11 and also phosphorylate the transcription factor in vitro. Finally, we demonstrate that ste11 is required for pheromone-induced G1 arrest. Interestingly, when we mutated Ste11 in the sites for Pat1 and Spk1 phosphorylation simultaneously, the cells could still arrest in G1 in response to pheromone, suggesting the existence of yet a third bifurcation of the signaling pathway.","authors":"Kjaerulff S, Lautrup-Larsen I, Truelsen S, Pedersen M, Nielsen O","authors_abbrev":"Kjaerulff S et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-02-17","publication_year":"2005","canto_session_key":"fa2885b9821513e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-15 15:45:11","canto_approved_date":"2026-04-08 07:17:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-04 14:48:12","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMTR.02","SPAC24B11.06c","SPBC19C2.05","SPBC1D7.05","SPAPB8E5.05","SPBC119.04","SPAC1D4.13","SPBC32C12.02","SPAC31G5.09c","SPAC27D7.03c","SPBC660.14"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2018-08-15"},{"uniquename":"PMID:19557351","title":"Nup211, the fission yeast homolog of Mlp1/Tpr, is involved in mRNA export.","citation":"J Microbiol 2009 Jun;47(3):337-43","abstract":"Synthetic lethal mutants have been previously isolated in fission yeast Schizosaccharomyces pombe, which genetically interact with spmex67, in order to identify the genes involved in mRNA export. The nup211 gene was isolated by complementation of the growth defect in one of the synthetic lethal mutants, SLMex2, under synthetic lethal condition. We showed that Nup211, fission yeast homolog of Mlpl/Mlp2/Tpr, is essential for vegetative growth and Nup211-GFP proteins expressed at endogenous level are localized mainly in nuclear periphery. The accumulation of poly(A)(+) RNA in the nucleus is exhibited when expression of nup211 is repressed or over-expressed. These results suggest that the Nup211 protein plays a pivotal role of mRNA export in fission yeast.","doi":"10.1007/s12275-009-0125-7","authors":"Bae JA, Moon D, Yoon JH","authors_abbrev":"Bae JA et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-06-27","publication_year":"2009","canto_session_key":"d98fa58a7d86947b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-08 16:17:19","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-08 16:17:11","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC162.08c","SPBC1921.03c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-12-08"},{"uniquename":"PMID:9751795","title":"All pyruvylated galactose in Schizosaccharomyces pombe N-glycans is present in the terminal disaccharide, 4, 6-O-[(R)-(1-carboxyethylidine)]-Galbeta1,3Galalpha1-.","citation":"Glycobiology 1998 Nov;8(11):1087-95","abstract":"The large N-linked oligosaccharides released from Schizosaccharomyces pombe by endo-beta-N-acetylglucosaminidase H were examined to determine how the negatively chargedpyruvylated galactoses present (Gemmill,T.R., and Trimble,R.B., 1996, J. Biol. Chem ., 271, 25945-25949) were attached to the oligosaccharide chains. Binding of biotinylated human serum amyloid P and peanut agglutinin to native and depyruvylated S.pombe glycoproteins, respectively, indicated that the pyruvylated epitope was likely to be in the beta configuration. Examination by high-field 1H NMR of whole glycans and a disaccharide fragment released from them on partial acid hydrolysis showed that the pyruvylated galactose species was in fact beta1,3-linked to a second galactose, and this occurred an average of five to six times on nominal Gal57Man64GlcNAc N-glycans. The pyruvate-2,(4,6)Gal-beta1,3Gal epitope is chemically similar to acetaldehyde-Galbeta1,3Gal groups found on the glycoproteins from Paramyxovirus-infected bovine kidney cells (Prehm, P., Scheid,A. and Choppin,P.W. ,1979, J. Biol. Chem ., 254, 9669-9677). The 1:1 stoichiometry between pyruvate and beta-linked galactose in these S.pombe glycans indicates that either pyruvate addition to terminal beta1,3Gal is highly efficient or that pyruvylated Gal is transferred en bloc to alpha1,2-linked Gal residues in theN-linked chains. In contradiction to many galactomannan-producing fungi, which add substantial amounts of Gal in the furanose form to their glycoproteins, all detectable Gal in the large S.pombe galactomannans is in the pyranose form, as found in higher eukaryotes. The current work shows that the S.pombe outer chain structure is a poly-alpha1,6Man backbone 2-O-substituted with either Gal or the pyruvylated galactobiose and contains little alpha1,2-linked or 2-O-substituted Man. This is in contrast to the S. cerevisiae outer chain, which is poly-alpha1,6Man substituted with alpha1,2-linked Man sidechains (Ballou,C.E. ,1990, Methods Enzymol , 185, 440-470).","authors":"Gemmill TR, Trimble RB","authors_abbrev":"Gemmill TR et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1998-09-30","publication_year":"1998","canto_session_key":"65446a5a48370c01","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-07 09:47:33","canto_approved_date":"2019-11-07 09:47:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-07 09:47:28","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-11-07"},{"uniquename":"EMBL:AU008923","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.92"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPCDC","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009905","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21179163","title":"Driving the cell cycle with a minimal CDK control network.","citation":"Nature 2010 Dec 23;468(7327):1074-9","abstract":"Control of eukaryotic cell proliferation involves an extended regulatory network, the complexity of which has made it difficult to understand the basic principles of the cell cycle. To investigate the core engine of the mitotic cycle we have generated a minimal control network in fission yeast that efficiently sustains cellular reproduction. Here we demonstrate that orderly progression through the major events of the cell cycle can be driven by oscillation of an engineered monomolecular cyclin-dependent protein kinase (CDK) module lacking much of the canonical regulation. We show further that the CDK oscillator acts as the primary organizer of the cell cycle, imposing timing and directionality to a system of two CDK activity thresholds that define independent cell cycle phases. We propose that this simple core architecture forms the basic control of the eukaryotic cell cycle.","doi":"10.1038/nature09543","authors":"Coudreuse D, Nurse P","authors_abbrev":"Coudreuse D et al.","pubmed_publication_date":"23 Dec 2010","pubmed_entrez_date":"2010-12-24","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10468581","title":"Role for yeast inhibitor of apoptosis (IAP)-like proteins in cell division.","citation":"Proc Natl Acad Sci U S A 1999 Aug 31;96(18):10170-5","abstract":"Inhibitors of apoptosis (IAPs) are a family of proteins that bear baculoviral IAP repeats (BIRs) and regulate apoptosis in vertebrates and Drosophila melanogaster. The yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe both encode a single IAP, designated BIR1 and bir1, respectively, each of which bears two BIRs. In rich medium, BIR1 mutant S. cerevisiae underwent normal vegetative growth and mitosis. Under starvation conditions, however, BIR1 mutant diploids formed spores inefficiently, instead undergoing pseudohyphal differentiation. Most spores that did form failed to survive beyond two divisions after germination. bir1 mutant S. pombe spores also died in the early divisions after spore germination and became blocked at the metaphase/anaphase transition because of an inability to elongate their mitotic spindle. Rather than inhibiting caspase-mediated cell death, yeast IAP proteins have roles in cell division and appear to act in a similar way to the IAPs from Caenorhabditis elegans and the mammalian IAP Survivin.","authors":"Uren AG, Beilharz T, O'Connell MJ, Bugg SJ, van Driel R, Vaux DL, Lithgow T","authors_abbrev":"Uren AG et al.","pubmed_publication_date":"31 Aug 1999","pubmed_entrez_date":"1999-09-01","publication_year":"1999","canto_session_key":"eb0717bf06e648f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-10-15 02:09:01","canto_approved_date":"2018-10-15 02:09:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-15 02:08:46","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC962.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-15"},{"uniquename":"PMID:30858198","title":"Reliable imaging of ATP in living budding and fission yeast.","citation":"J Cell Sci 2019 Apr 17;132(8)","abstract":"Adenosine triphosphate (ATP) is a main metabolite essential for all living organisms. However, our understanding of ATP dynamics within a single living cell is very limited. Here, we optimized the ATP-biosensor QUEEN and monitored the dynamics of ATP with good spatial and temporal resolution in living yeasts. We found stable maintenance of ATP concentration in wild-type yeasts, regardless of carbon sources or cell cycle stages, suggesting that mechanism exists to maintain ATP at a specific concentration. We further found that ATP concentration is not necessarily an indicator of metabolic activity, as there is no clear correlation between ATP level and growth rates. During fission yeast meiosis, we found a reduction in ATP levels, suggesting that ATP homeostasis is controlled by differentiation. The use of QUEEN in yeasts offers an easy and reliable assay for ATP dynamicity and will answer several unaddressed questions about cellular metabolism in eukaryotes.","doi":"10.1242/jcs.230649","authors":"Takaine M, Ueno M, Kitamura K, Imamura H, Yoshida S","authors_abbrev":"Takaine M et al.","pubmed_publication_date":"17 Apr 2019","pubmed_entrez_date":"2019-03-13","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-03-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18675827","title":"The tumor suppressor homolog in fission yeast, myh1(+), displays a strong interaction with the checkpoint gene rad1(+).","citation":"Mutat Res 2008 Sep 26;644(1-2):48-55","abstract":"The DNA glycosylase MutY is strongly conserved in evolution, and homologs are found in most eukaryotes and prokaryotes examined. This protein is implicated in repair of oxidative DNA damage, in particular adenine mispaired opposite 7,8-dihydro-8-oxoguanine. Previous investigations in Escherichia coli, fission yeast, and mammalian cells show an association of mutations in MutY homologs with a mutator phenotype and carcinogenesis. Eukaryotic MutY homologs physically associate with several proteins with a role in replication, DNA repair, and checkpoint signaling, specifically the trimeric 9-1-1 complex. In a genetic investigation of the fission yeast MutY homolog, myh1(+), we show that the myh1 mutation confers a moderately increased UV sensitivity alone and in combination with mutations in several DNA repair genes. The myh1 rad1, and to a lesser degree myh1 rad9, double mutants display a synthetic interaction resulting in enhanced sensitivity to DNA damaging agents and hydroxyurea. UV irradiation of myh1 rad1 double mutants results in severe chromosome segregation defects and visible DNA fragmentation, and a failure to activate the checkpoint. Additionally, myh1 rad1 double mutants exhibit morphological defects in the absence of DNA damaging agents. We also found a moderate suppression of the slow growth and UV sensitivity of rhp51 mutants by the myh1 mutation. Our results implicate fission yeast Myh1 in repair of a wider range of DNA damage than previously thought, and functionally link it to the checkpoint pathway.","doi":"10.1016/j.mrfmmm.2008.07.001","authors":"Jansson K, Warringer J, Farewell A, Park HO, Hoe KL, Kim DU, Hayles J, Sunnerhagen P","authors_abbrev":"Jansson K et al.","pubmed_publication_date":"26 Sep 2008","pubmed_entrez_date":"2008-08-05","publication_year":"2008","canto_session_key":"0735dfd8306ff1b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Per Sunnerhagen","canto_first_approved_date":"2012-07-31 15:05:34","canto_approved_date":"2021-10-07 11:58:00","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-10-07 10:46:36","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":43,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Per Sunnerhagen","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC20G4.04c","SPAC1952.07","SPBC1734.06","SPCC285.16c","SPAC644.14c","SPAC664.07c","SPAC14C4.13","SPAC3G6.06c","SPAC26A3.02","SPBC3E7.08c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2012-07-31"},{"uniquename":"PMID:3516412","title":"The cell cycle control gene cdc2+ of fission yeast encodes a protein kinase potentially regulated by phosphorylation.","citation":"Cell 1986 Apr 25;45(2):261-8","abstract":"The cdc2+ gene function has an important role in controlling the commitment of the fission yeast cell to the mitotic cycle and the timing of mitosis. We have raised antibodies against the cdc2+ protein using synthetic peptides and have demonstrated that it is a 34 kd phosphoprotein with protein kinase activity. The protein level and phosphorylation state remain unchanged during the mitotic cycle of rapidly growing cells. When cells cease to proliferate and arrest in G1 the protein becomes dephosphorylated and loses protein kinase activity. Exit from the mitotic cycle and entry into stationary phase may be controlled in part by modulation of the cdc2 protein kinase activity by changes in its phosphorylation state.","authors":"Simanis V, Nurse P","authors_abbrev":"Simanis V et al.","pubmed_publication_date":"25 Apr 1986","pubmed_entrez_date":"1986-04-25","publication_year":"1986","canto_session_key":"d2e620f2641d569b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-05 15:12:42","canto_approved_date":"2020-01-23 13:31:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-13 16:26:46","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-05"},{"uniquename":"PMID:25952947","title":"An Imaging Flow Cytometry-based approach to analyse the fission yeast cell cycle in fixed cells.","citation":"Methods 2015 Jul 01;82:74-84","abstract":"Fission yeast (Schizosaccharomyces pombe) is an excellent model organism for studying eukaryotic cell division because many of the underlying principles and key regulators of cell cycle biology are conserved from yeast to humans. As such it can be employed as tool for understanding complex human diseases that arise from dis-regulation in cell cycle controls, including cancers. Conventional Flow Cytometry (CFC) is a high-throughput, multi-parameter, fluorescence-based single cell analysis technology. It is widely used for studying the mammalian cell cycle both in the context of the normal and disease states by measuring changes in DNA content during the transition through G1, S and G2/M using fluorescent DNA-binding dyes. Unfortunately analysis of the fission yeast cell cycle by CFC is not straightforward because, unlike mammalian cells, cytokinesis occurs after S-phase meaning that bi-nucleated G1 cells have the same DNA content as mono-nucleated G2 cells and cannot be distinguished using total integrated fluorescence (pulse area). It has been elegantly shown that the width of the DNA pulse can be used to distinguish G2 cells with a single 2C foci versus G1 cells with two 1C foci, however the accuracy of this measurement is dependent on the orientation of the cell as it traverses the laser beam. To this end we sought to improve the accuracy of the fission yeast cell cycle analysis and have developed an Imaging Flow Cytometry (IFC)-based method that is able to preserve the high throughput, objective analysis afforded by CFC in combination with the spatial and morphometric information provide by microscopy. We have been able to derive an analysis framework for subdividing the yeast cell cycle that is based on intensiometric and morphometric measurements and is thus robust against orientation-based miss-classification. In addition we can employ image-based metrics to define populations of septated/bi-nucleated cells and measure cellular dimensions. To our knowledge, this is the first use of IFC to study fission yeast and we are confident that this will provide a springboard for further IFC-based analysis across all aspects of fission yeast biology.","doi":"10.1016/j.ymeth.2015.04.026","authors":"Patterson JO, Swaffer M, Filby A","authors_abbrev":"Patterson JO et al.","pubmed_publication_date":"01 Jul 2015","pubmed_entrez_date":"2015-05-09","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-05-10 00:19:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16751098","title":"Tethering RITS to a nascent transcript initiates RNAi- and heterochromatin-dependent gene silencing.","citation":"Cell 2006 Jun 02;125(5):873-86","abstract":"In the fission yeast Schizosaccharomyces pombe, the RNA-Induced Transcriptional Silencing (RITS) complex has been proposed to target the chromosome via siRNA-dependent base-pairing interactions to initiate heterochromatin formation. Here we show that tethering of the RITS subunit, Tas3, to the RNA transcript of the normally active ura4+ gene silences ura4+ expression. This silencing depends on a functional RNAi pathway, requires the heterochromatin proteins, Swi6/HP1, Clr4/Suv39h, and Sir2, and is accompanied by the generation of ura4+ siRNAs, histone H3-lysine 9 methylation, and Swi6 binding. Furthermore, the ability of the newly generated ura4+ siRNAs to silence a second ura4+ allele in trans is strongly inhibited by the conserved siRNA nuclease, Eri1. Surprisingly, silencing of tethered ura4+, or ura4+ inserted within centromeric heterochromatin, or some of the endogenous centromeric repeat promoters, is not associated with changes in RNA polymerase II occupancy. These findings support a model in which targeting of nascent transcripts by RITS mediates chromatin modifications and suggest that cotranscriptional processing events play a primary role in the silencing mechanism.","authors":"Bühler M, Verdel A, Moazed D","authors_abbrev":"Bühler M et al.","pubmed_publication_date":"02 Jun 2006","pubmed_entrez_date":"2006-06-06","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31072933","title":"Suppressor screening reveals common kleisin-hinge interaction in condensin and cohesin, but different modes of regulation.","citation":"Proc Natl Acad Sci U S A 2019 May 28;116(22):10889-10898","abstract":"Cohesin and condensin play fundamental roles in sister chromatid cohesion and chromosome segregation, respectively. Both consist of heterodimeric structural maintenance of chromosomes (SMC) subunits, which possess a head (containing ATPase) and a hinge, intervened by long coiled coils. Non-SMC subunits (Cnd1, Cnd2, and Cnd3 for condensin; Rad21, Psc3, and Mis4 for cohesin) bind to the SMC heads. Here, we report a large number of spontaneous extragenic suppressors for fission yeast condensin and cohesin mutants, and their sites were determined by whole-genome sequencing. Mutants of condensin's non-SMC subunits were rescued by impairing the SUMOylation pathway. Indeed, SUMOylation of Cnd2, Cnd3, and Cut3 occurs in midmitosis, and Cnd3 K870 SUMOylation functionally opposes Cnd subunits. In contrast, cohesin mutants  rad21  and  psc3  were rescued by loss of the RNA elimination pathway (Erh1, Mmi1, and Red1), and loader mutant  mis4  was rescued by loss of Hrp1-mediated chromatin remodeling. In addition, distinct regulations were discovered for condensin and cohesin hinge mutants. Mutations in the N-terminal helix bundle [containing a helix-turn-helix (HTH) motif] of kleisin subunits (Cnd2 and Rad21) rescue virtually identical hinge interface mutations in cohesin and condensin, respectively. These mutations may regulate kleisin's interaction with the coiled coil at the SMC head, thereby revealing a common, but previously unknown, suppression mechanism between the hinge and the kleisin N domain, which is required for successful chromosome segregation. We propose that in both condensin and cohesin, the head (or kleisin) and hinge may interact and collaboratively regulate the resulting coiled coils to hold and release chromosomal DNAs.","doi":"10.1073/pnas.1902699116","authors":"Xu X, Yanagida M","authors_abbrev":"Xu X et al.","pubmed_publication_date":"28 May 2019","pubmed_entrez_date":"2019-05-11","publication_year":"2019","canto_session_key":"396866ab84f69995","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xingya Xu","canto_first_approved_date":"2019-05-26 13:48:02","canto_approved_date":"2023-09-21 14:42:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-17 20:10:30","canto_added_date":"2019-05-12 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":96,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Xingya Xu","community_curator":true,"annotation_count":84,"orcid":"0000-0002-3728-2633","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.03","SPAC22F8.06","SPAC4C5.04","SPBC146.03c","SPAC1006.03c","SPCC736.12c","SPAC1783.05","SPAC22E12.14c","SPCC338.17c","SPCC576.15c","SPCC1682.16","SPBC776.13","SPAC1B9.02c","SPBC646.16","SPCC306.03c","SPBC16C6.07c","SPBP4H10.06c","SPBC119.01","SPAC2H10.02c","SPAC30D11.13","SPCC663.01c","SPAC1687.05","SPAC13C5.01c","SPAC23D3.07","SPAC637.10c","SPAC31A2.05c","SPAC17H9.20","SPAC10F6.09c","SPBP19A11.03c","SPBC365.06","SPCC1739.12","SPAC31G5.13","SPBC428.17c","SPAC19G12.17","SPBC29A10.04"],"gene_count":35,"ltp_gene_count":35,"approved_date":"2019-05-26"},{"uniquename":"GO_REF:0000107","title":"Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.","abstract":"GO terms from a source species are projected onto one or more target species based on gene orthology obtained from Ensembl Compara. One-to-one, one-to-many and many-to-many orthology relations and anntations are transferred between orthologs that have at least a 40% peptide identity to each other. Only GO annotations with evidence codes ECO:0000314 (IDA), ECO:0000270 (IEP), ECO:0000316 (IGI), ECO:0000315 (IMP), and ECO:0000353 (IPI), or their descendants, are transferred; annotations with a 'NOT' qualifier are not transferred, and neither are annotations to GO:0005515 (protein binding). Annotations that are transferred using this method receive the evidence code ECO:0000265 (sequence orthology evidence used in automatic assertion), which maps up to the GO Inferred from Electronic Annotation (IEA) evidence code.  The model organism database identifier of the annotation source will be indicated in the 'With' column of the GOA association file.","authors":"GOA curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25993311","title":"Casein Kinase 1 and Phosphorylation of Cohesin Subunit Rec11 (SA3) Promote Meiotic Recombination through Linear Element Formation.","citation":"PLoS Genet 2015 May;11(5):e1005225","abstract":"Proper meiotic chromosome segregation, essential for sexual reproduction, requires timely formation and removal of sister chromatid cohesion and crossing-over between homologs. Early in meiosis cohesins hold sisters together and also promote formation of DNA double-strand breaks, obligate precursors to crossovers. Later, cohesin cleavage allows chromosome segregation. We show that in fission yeast redundant casein kinase 1 homologs, Hhp1 and Hhp2, previously shown to regulate segregation via phosphorylation of the Rec8 cohesin subunit, are also required for high-level meiotic DNA breakage and recombination. Unexpectedly, these kinases also mediate phosphorylation of a different meiosis-specific cohesin subunit Rec11. This phosphorylation in turn leads to loading of linear element proteins Rec10 and Rec27, related to synaptonemal complex proteins of other species, and thereby promotes DNA breakage and recombination. Our results provide novel insights into the regulation of chromosomal features required for crossing-over and successful reproduction. The mammalian functional homolog of Rec11 (STAG3) is also phosphorylated during meiosis and appears to be required for fertility, indicating wide conservation of the meiotic events reported here.","doi":"10.1371/journal.pgen.1005225","authors":"Phadnis N, Cipak L, Polakova S, Hyppa RW, Cipakova I, Anrather D, Karvaiova L, Mechtler K, Smith GR, Gregan J","authors_abbrev":"Phadnis N et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-05-21","publication_year":"2015","canto_session_key":"536dc2e074eee139","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juraj Gregan","canto_first_approved_date":"2017-06-14 12:15:11","canto_approved_date":"2024-04-29 09:36:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-09-15 11:01:07","canto_added_date":"2015-05-22 00:19:26","annotation_curators":[{"name":"Juraj Gregan","community_curator":true,"annotation_count":45,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":39,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4E9.01c","SPAC17A5.11","SPBC29A10.14","SPBC3H7.15","SPAC10F6.09c","SPAC23C4.12","SPAC25G10.04c","SPBC577.05c","SPBC29A10.04"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2017-06-14"},{"uniquename":"PMID:41698824","title":"A Temperature Increase Induces Atf1/Pcr1-Dependent Rapid Depletion of Histones in Transcriptionally Activated Gene Bodies in Fission Yeast.","citation":"Genes Cells 2026 Mar;31(2):e70092","abstract":"Transcriptional regulation is central to organisms' response and adaptation to environmental changes. However, the coordination of transcriptional machinery with chromatin when rapid transcriptional changes are needed is largely unknown. Here, we studied the rapid response of histone modifications upon heat treatment of fission yeast Schizosaccharomyces pombe. We observed a significant eviction of H3 in the transcribed regions of upregulated genes, named Hasty Overheat-Triggered Differentially Occupied Genes (HOT-DOGs), including Heat Shock Protein-encoding genes. The loss of H3 in a third of the HOT-DOGs was dependent on the Atf1-Pcr1 transcription factor complex. Furthermore, the H3K9 methyltransferase Clr4 likely modulates the rate of transcription elongation and helps prevent transcriptional read-through beyond polyadenylation sites in these genes. Our results unveiled a novel function of Clr4 in regulating the dynamics of transcription within gene bodies and provided insights into how cells cope with rapid environmental changes while preserving chromatin integrity.","doi":"10.1111/gtc.70092","authors":"Hoshino A, Kajitani T, Oki M, Kakutani T, Inagaki S","authors_abbrev":"Hoshino A et al.","pubmed_publication_date":"Mar 2026","pubmed_entrez_date":"2026-02-16","publication_year":"2026","canto_session_key":"7466a8f8254da528","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-02-18 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9078390","title":"Dissection of fission yeast microtubule associating protein p93Dis1: regions implicated in regulated localization and microtubule interaction.","citation":"Genes Cells 1996 Jul;1(7):633-44","abstract":"Fission yeast microtubule associating protein (MAP) p93Dis1 functions for sister chromatid separation: dis1 mutants fail to separate chromosomes, while the spindle elongates but without cyclin destruction. p93Dis1 localizes along microtubules in interphase cytoplasm, but shifts to the spindle pole body (SPB) and spindle microtubules upon the entry into mitosis. In this study, regions of p93Dis1 were dissected to examine their role.\nNitrocellulose filter blotting shows that recombinant Dis1 binds to bovine brain microtubules in vitro. A basic central region rich in S, T and P is essential for this association. However, the whole p93Dis1 with N- and C-termini containing a conserved repeat motif and heptad repeats, respectively, is necessary for normal microtubule association in vivo. The N-truncated region also binds to microtubules but only to the portions near the SPBs. Overproduction phenotypes indicate that p93Dis1 greatly affects spindle formation and cell morphogenesis. The central region is essential but, by itself, not sufficient for generating such effects.\nWe propose that p93Dis1 consists of three regions which carry distinct properties for localization: the N-region for cell cycle dependent localization, the central region for direct microtubule association, and the C-region for SPB and nuclear localization. The essential role of p93Dis1 is carried out in the C-region, while the N-region acts as a regulator.","authors":"Nakaseko Y, Nabeshima K, Kinoshita K, Yanagida M","authors_abbrev":"Nakaseko Y et al.","pubmed_publication_date":"Jul 1996","pubmed_entrez_date":"1996-07-01","publication_year":"1996","canto_session_key":"d437b51c6564a32a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-11-08 16:22:41","canto_approved_date":"2018-11-08 16:22:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-14 15:42:17","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-11-08"},{"uniquename":"PANTHER:PTHR12903","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F8.02c","HGNC:14037"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28321042","title":"Evaluation of a novel method for measurement of intracellular calcium ion concentration in fission yeast.","citation":"J Toxicol Sci 2017;42(2):159-166","abstract":"The distribution of metal and metalloid species in each of the cell compartments is termed as \"metallome\". It is important to elucidate the molecular mechanism underlying the beneficial or toxic effects exerted by a given metal or metalloid on human health. Therefore, we developed a method to measure intracellular metal ion concentration (particularly, intracellular calcium ion) in fission yeast. We evaluated the effects of nitric acid (HNO 3 ), zymolyase, and westase treatment on cytolysis in fission yeast. Moreover, we evaluated the changes in the intracellular calcium ion concentration in fission yeast in response to treatment with/without micafungin. The fission yeast undergoes lysis when treated with 60% HNO 3 , which is simpler and cheaper compared to the other treatments. Additionally, the intracellular calcium ion concentration in 60% HNO 3 -treated fission yeast was determined by inductively coupled plasma atomic emission spectrometry. This study yields significant information pertaining to measurement of the intracellular calcium ion concentration in fission yeast, which is useful for elucidating the physiological or pathological functions of calcium ion in the biological systems. This study is the first step to obtain perspective view on the effect of the metallome in biological systems.","doi":"10.2131/jts.42.159","authors":"Ogata F, Satoh R, Kita A, Sugiura R, Kawasaki N","authors_abbrev":"Ogata F et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-03-22","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-03-24 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12521310","title":"The Pap1-independent induction by metal ions of a third gene encoding glutathione S-transferase gene from the fission yeast.","citation":"Mol Cells 2002 Dec 31;14(3):444-8","abstract":"A third gene that encodes glutathione S-transferase (GSTIII) was previously cloned from the fission yeast Schizosaccharomyces pombe. Using the GSTIII-lacZ fusion plasmid pGDA-19, its expression was shown to be enhanced by various metal ions. In the present study, four additional fusion plasmids, pGDA-29, pGDA-39, PGDA-49, and pGDA-59, were designed to carry 998, 378, 276, and 115 bp upstream regions from the translational initiation point, respectively. The major activation region was located between -998 and -378 bp upstream of the GSTIII gene. Regulatory sequences that are responsible for the induction by metal ions reside between -998 and -378 bp and between -276 and -115 bp upstream of the gene. The overexpressed Pap1 exerts a repression effect on the GSTIII expression via -998 to approximately -378 bp region, whereas it exerts an activation effect on the GSTIII expression via -270 to approximately -115 bp region. However, the induction of the GSTIII gene by metal ions occurs independent of Pap1.","authors":"Sa JH, Shin YH, Lim HW, Kim K, Park EH, Lim CJ","authors_abbrev":"Sa JH et al.","pubmed_publication_date":"31 Dec 2002","pubmed_entrez_date":"2003-01-11","publication_year":"2002","canto_session_key":"fe620cd046781e01","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-04 14:44:11","canto_approved_date":"2024-03-29 12:58:43","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-12-04 14:44:04","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC688.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-12-04"},{"uniquename":"PMID:35879419","title":"Proteasome-dependent truncation of the negative heterochromatin regulator Epe1 mediates antifungal resistance.","citation":"Nat Struct Mol Biol 2022 Aug;29(8):745-758","abstract":"Epe1 histone demethylase restricts H3K9-methylation-dependent heterochromatin, preventing it from spreading over, and silencing, gene-containing regions in fission yeast. External stress induces an adaptive response allowing heterochromatin island formation that confers resistance on surviving wild-type lineages. Here we investigate the mechanism by which Epe1 is regulated in response to stress. Exposure to caffeine or antifungals results in Epe1 ubiquitylation and proteasome-dependent removal of the N-terminal 150 residues from Epe1, generating truncated Epe1 (tEpe1) which accumulates in the cytoplasm. Constitutive tEpe1 expression increases H3K9 methylation over several chromosomal regions, reducing expression of underlying genes and enhancing resistance. Reciprocally, constitutive non-cleavable Epe1 expression decreases resistance. tEpe1-mediated resistance requires a functional JmjC demethylase domain. Moreover, caffeine-induced Epe1-to-tEpe1 cleavage is dependent on an intact cell integrity MAP kinase stress signaling pathway, mutations in which alter resistance. Thus, environmental changes elicit a mechanism that curtails the function of this key epigenetic modifier, allowing heterochromatin to reprogram gene expression, thereby bestowing resistance to some cells within a population. H3K9me-heterochromatin components are conserved in human and crop-plant fungal pathogens for which a limited number of antifungals exist. Our findings reveal how transient heterochromatin-dependent antifungal resistant epimutations develop and thus inform on how they might be countered.","doi":"10.1038/s41594-022-00801-y","authors":"Yaseen I, White SA, Torres-Garcia S, Spanos C, Lafos M, Gaberdiel E, Yeboah R, El Karoui M, Rappsilber J, Pidoux AL, Allshire RC","authors_abbrev":"Yaseen I et al.","pubmed_publication_date":"Aug 2022","pubmed_entrez_date":"2022-07-25","publication_year":"2022","canto_session_key":"ca7acb07b987c4e7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-07-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ632018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.33"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30044717","title":"Roles of the fission yeast UNC-13/Munc13 protein Ync13 in late stages of cytokinesis.","citation":"Mol Biol Cell 2018 Sep 15;29(19):2259-2279","abstract":"Cytokinesis is a complicated yet conserved step of the cell-division cycle that requires the coordination of multiple proteins and cellular processes. Here we describe a previously uncharacterized protein, Ync13, and its roles during fission yeast cytokinesis. Ync13 is a member of the UNC-13/Munc13 protein family, whose animal homologues are essential priming factors for soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex assembly during exocytosis in various cell types, but no roles in cytokinesis have been reported. We find that Ync13 binds to lipids in vitro and dynamically localizes to the plasma membrane at cell tips during interphase and at the division site during cytokinesis. Deletion of Ync13 leads to defective septation and exocytosis, uneven distribution of cell-wall enzymes and components of cell-wall integrity pathway along the division site and massive cell lysis during cell separation. Interestingly, loss of Ync13 compromises endocytic site selection at the division plane. Collectively, we find that Ync13 has a novel function as an UNC-13/Munc13 protein in coordinating exocytosis, endocytosis, and cell-wall integrity during fission yeast cytokinesis.","doi":"10.1091/mbc.E18-04-0225","authors":"Zhu YH, Hyun J, Pan YZ, Hopper JE, Rizo J, Wu JQ","authors_abbrev":"Zhu YH et al.","pubmed_publication_date":"15 Sep 2018","pubmed_entrez_date":"2018-07-26","publication_year":"2018","canto_session_key":"33c4c7d6daa555cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yihua Zhu","canto_first_approved_date":"2019-05-15 09:23:58","canto_approved_date":"2025-09-03 14:51:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-03 21:28:10","canto_added_date":"2018-07-27 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yihua Zhu","community_curator":true,"annotation_count":40,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.09c","SPBC4F6.12","SPBC19G7.08c","SPBC19G7.05c","SPCC645.05c","SPAC17G8.12","SPBC1778.06c","SPAC18G6.03","SPBC23G7.08c","SPBC12D12.04c","SPAC19G12.14","SPAC6G9.11","SPAC110.03","SPCC645.06c","SPAC821.09","SPAC11E3.02c","SPBC800.10c","SPCC1281.01","SPBC11C11.02","SPCC970.09","SPAC20G8.05c","SPAC6G10.05c","SPCC895.05","SPBC106.20","SPAC23C4.08","SPAC688.11","SPCC1840.02c","SPAC17G8.14c","SPAC1F7.04"],"gene_count":29,"ltp_gene_count":23,"approved_date":"2019-05-15"},{"uniquename":"PMID:12194845","title":"Pseudostructural inhibitors of G protein signaling during development.","citation":"Dev Cell 2002 Aug;3(2):154-5","abstract":"Heterotrimeric G proteins mediate signal transduction pathways to control development in fungal, plant, and animal cells. A recent study in the July issue of Molecular Cell identifies three proteins that, while not displaying sequence similarity to G protein subunits, appear to act as structural mimics of a Gbetagamma dimer to negatively regulate pseudohyphal growth in budding yeast.","authors":"Ivey FD, Hoffman CS","authors_abbrev":"Ivey FD et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-08-27","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8463273","title":"A Ca(2+)-independent protein kinase C from fission yeast.","citation":"J Biol Chem 1993 Apr 05;268(10):7401-6","abstract":"A protein kinase C homologue of Schizosaccharomyces pombe, pkc1+, was isolated from a genomic library by screening with the Saccharomyces cerevisiae PKC1 probe. From its primary sequence and biochemical properties, we conclude that S. pombe pkc1+ encodes a phospholipid-activated Ca(2+)-independent protein kinase, homologous to the delta/epsilon classes of mammalian protein kinase C. Gene disruption experiments show that pkc1+ is not essential for cell viability; however, overexpression of the protein leads to an abnormal cell morphology and a block in cell separation following mitosis suggestive of a role in cell division. In vitro phosphorylation experiments reveal several potential pkc1+ substrates.","authors":"Mazzei GJ, Schmid EM, Knowles JK, Payton MA, Maundrell KG","authors_abbrev":"Mazzei GJ et al.","pubmed_publication_date":"05 Apr 1993","pubmed_entrez_date":"1993-04-05","publication_year":"1993","canto_session_key":"abb52d9d2b18f1e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-26 17:03:43","canto_approved_date":"2020-12-02 11:43:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-26 15:52:39","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.04c","SPAC17G8.14c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2020-11-26"},{"uniquename":"PMID:18457584","title":"Rapid regulation of protein activity in fission yeast.","citation":"BMC Cell Biol 2008 May 05;9:23","abstract":"The fission yeast Schizosaccharomyces pombe is widely-used as a model organism for the study of a broad range of eukaryotic cellular processes such as cell cycle, genome stability and cell morphology. Despite the availability of extensive set of genetic, molecular biological, biochemical and cell biological tools for analysis of protein function in fission yeast, studies are often hampered by the lack of an effective method allowing for the rapid regulation of protein level or protein activity.\nIn order to be able to regulate protein function, we have made use of a previous finding that the hormone binding domain of steroid receptors can be used as a regulatory cassette to subject the activity of heterologous proteins to hormonal regulation. The approach is based on fusing the protein of interest to the hormone binding domain (HBD) of the estrogen receptor (ER). The HBD tag will attract the Hsp90 complex, which can render the fusion protein inactive. Upon addition of estradiol the protein is quickly released from the Hsp90 complex and thereby activated. We have tagged and characterised the induction of activity of four different HBD-tagged proteins. Here we show that the tag provided the means to effectively regulate the activity of two of these proteins.\nThe estradiol-regulatable hormone binding domain provides a means to regulate the function of some, though not all, fission yeast proteins. This system may result in very quick and reversible activation of the protein of interest. Therefore it will be a powerful tool and it will open experimental approaches in fission yeast that have previously not been possible. Since fission yeast is a widely-used model organism, this will be valuable in many areas of research.","doi":"10.1186/1471-2121-9-23","authors":"Bøe CA, Garcia I, Pai CC, Sharom JR, Skjølberg HC, Boye E, Kearsey S, Macneill SA, Tyers MD, Grallert B","authors_abbrev":"Bøe CA et al.","pubmed_publication_date":"05 May 2008","pubmed_entrez_date":"2008-05-07","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29235477","title":"Nucleotide- and Mal3-dependent changes in fission yeast microtubules suggest a structural plasticity view of dynamics.","citation":"Nat Commun 2017 Dec 13;8(1):2110","abstract":"Using cryo-electron microscopy, we characterize the architecture of microtubules assembled from Schizosaccharomyces pombe tubulin, in the presence and absence of their regulatory partner Mal3. Cryo-electron tomography reveals that microtubules assembled from S. pombe tubulin have predominantly B-lattice interprotofilament contacts, with protofilaments skewed around the microtubule axis. Copolymerization with Mal3 favors 13 protofilament microtubules with reduced protofilament skew, indicating that Mal3 adjusts interprotofilament interfaces. A 4.6-Å resolution structure of microtubule-bound Mal3 shows that Mal3 makes a distinctive footprint on the S. pombe microtubule lattice and that unlike mammalian microtubules, S. pombe microtubules do not show the longitudinal lattice compaction associated with EB protein binding and GTP hydrolysis. Our results firmly support a structural plasticity view of microtubule dynamics in which microtubule lattice conformation is sensitive to a variety of effectors and differently so for different tubulins.","doi":"10.1038/s41467-017-02241-5","authors":"von Loeffelholz O, Venables NA, Drummond DR, Katsuki M, Cross R, Moores CA","authors_abbrev":"von Loeffelholz O et al.","pubmed_publication_date":"13 Dec 2017","pubmed_entrez_date":"2017-12-14","publication_year":"2017","canto_session_key":"0702ea6009fcdaf6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-02-11 11:34:48","canto_approved_date":"2018-02-11 11:34:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-10 13:43:58","canto_added_date":"2017-12-15 01:15:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPBC26H8.07c","SPAC18G6.15","SPBC800.05c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-02-11","pdb_entries":[{"pdb_id":"5mjs","gene_chains":[{"gene_uniquename":"SPBC16A3.15c","chain":"E/F/G/H","position":"1-444"},{"gene_uniquename":"SPBC26H8.07c","chain":"A/B/C/J","position":"1-429"},{"gene_uniquename":"SPAC18G6.15","chain":"D","position":"1-143"}],"title":"S. pombe microtubule copolymerized with GTP and Mal3-143","entry_authors":"von Loeffelholz O,Moores C","entry_authors_abbrev":"von Loeffelholz O et al.","reference_uniquename":"PMID:29235477","experimental_method":"EM","resolution":"4.6"}]},{"uniquename":"EMBL:AU009371","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34214524","title":"Formin Cdc12's specific actin assembly properties are tailored for cytokinesis in fission yeast.","citation":"Biophys J 2021 Aug 03;120(15):2984-2997","abstract":"Formins generate unbranched actin filaments by a conserved, processive actin assembly mechanism. Most organisms express multiple formin isoforms that mediate distinct cellular processes and facilitate actin filament polymerization by significantly different rates, but how these actin assembly differences correlate to cellular activity is unclear. We used a computational model of fission yeast cytokinetic ring assembly to test the hypothesis that particular actin assembly properties help tailor formins for specific cellular roles. Simulations run in different actin filament nucleation and elongation conditions revealed that variations in formin's nucleation efficiency critically impact both the probability and timing of contractile ring formation. To probe the physiological importance of nucleation efficiency, we engineered fission yeast formin chimera strains in which the FH1-FH2 actin assembly domains of full-length cytokinesis formin Cdc12 were replaced with the FH1-FH2 domains from functionally and evolutionarily diverse formins with significantly different actin assembly properties. Although Cdc12 chimeras generally support life in fission yeast, quantitative live-cell imaging revealed a range of cytokinesis defects from mild to severe. In agreement with the computational model, chimeras whose nucleation efficiencies are least similar to Cdc12 exhibit more severe cytokinesis defects, specifically in the rate of contractile ring assembly. Together, our computational and experimental results suggest that fission yeast cytokinesis is ideally mediated by a formin with properly tailored actin assembly parameters.","doi":"10.1016/j.bpj.2021.06.023","authors":"Homa KE, Zsolnay V, Anderson CA, O'Connell ME, Neidt EM, Voth GA, Bidone TC, Kovar DR","authors_abbrev":"Homa KE et al.","pubmed_publication_date":"03 Aug 2021","pubmed_entrez_date":"2021-07-02","publication_year":"2021","canto_session_key":"1a49d81b466ed277","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-07-04 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35635990","title":"Biological management of acidity in wine industry: A review.","citation":"Int J Food Microbiol 2022 Aug 16;375:109726","abstract":"Climate change is generating several problems in wine technology. One of the main ones is lack of acidity and difficulties performing malolactic fermentation to stabilize wines before bottling. Among the different available acidity management technologies, such as direct acid addition, ion exchange resins, electro-membrane treatments, or vineyard management, the microbiological option is reliable and deeply studied. The main approach is the increase in malic acid content because of the metabolism of specific Saccharomyces strains and to increase lactic acid because of the metabolism of Lachancea genus. Other non-Saccharomyces yeasts, such as Starmerella bacillaris or Candida stellata can also acidify significantly because of the production of pyruvic or succinic acid. Wine industry needs the removal of malic acid in most red wines before bottling to achieve wine stability. Oenococus oeni performs the malolactic fermentation of red wines on most conditions because of the metabolization of malic acid into lactic acid. However, modern oenology challenges such as high ethanol concentrations, high pH or low levels of malic acid have made researchers to look for other options to reduce potential risks of deviation. Other wine-related microorganisms able to de-acidify malic acid have appeared as interesting alternatives for specific difficult scenarios. Lactiplantibacillus plantarum and Schizosaccharomyces genus make up nowadays the main studied alternatives.","doi":"10.1016/j.ijfoodmicro.2022.109726","authors":"Vicente J, Baran Y, Navascués E, Santos A, Calderón F, Marquina D, Rauhut D, Benito S","authors_abbrev":"Vicente J et al.","pubmed_publication_date":"16 Aug 2022","pubmed_entrez_date":"2022-05-31","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-06-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24660134","title":"Morphological Effects of Natural Products on Schizosaccharomyces pombe Measured by Imaging Flow Cytometry.","citation":"Nat Prod Bioprospect 2014 Feb;4(1):27-35","abstract":"Gaining a full understanding of the mechanisms of action of natural products as therapeutic agents includes observing the effects of natural products on cellular morphology, because abnormal cellular morphology is an important aspect of cellular transformations that occur as part of disease states. In this study a set of natural products was examined in search of small molecules that influence the cylindrical morphology of fission yeast Schizosaccharomyces pombe. Imaging flow cytometry of large populations of S. pombe exposed to natural products captured cell images and revealed changes in mean length and aspect ratio of cells. Several natural products were found to alter S. pombe's morphology relative to control, in terms of elongating cells, shrinking them, or making them more round. These results may facilitate future investigations into methods by which cells establish and maintain specific shapes.\nGaining a full understanding of the mechanisms of action of natural products as therapeutic agents includes observing the effects of natural products on cellular morphology, because abnormal cellular morphology is an important aspect of cellular transformations that occur as part of disease states. In this study a set of natural products was examined in search of small molecules that influence the cylindrical morphology of fission yeast Schizosaccharomyces pombe. Imaging flow cytometry of large populations of S. pombe exposed to natural products captured cell images and revealed changes in mean length and aspect ratio of cells. Several natural products were found to alter S. pombe's morphology relative to control, in terms of elongating cells, shrinking them, or making them more round. These results may facilitate future investigations into methods by which cells establish and maintain specific shapes.","doi":"10.1007/s13659-014-0004-8","authors":"Heisler J, Elvir L, Barnouti F, Charles E, Wolkow TD, Pyati R","authors_abbrev":"Heisler J et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2014-03-25","publication_year":"2014","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19362000","title":"Cofilin dissociates Arp2/3 complex and branches from actin filaments.","citation":"Curr Biol 2009 Apr 14;19(7):537-45","abstract":"Actin-based cellular motility requires spatially and temporally coordinated remodeling of a network of branched actin filaments. This study investigates how cofilin and Arp2/3 complex, two main players in the dendritic nucleation model, interact to produce sharp spatial transitions between densely branched filaments and long, unbranched filaments.\nWe found that cofilin binding reduces both the affinity of actin filaments for Arp2/3 complex and the stability of branches. We used fluorescence spectroscopy to measure the kinetics of cofilin association with filaments and the resulting dissociation of Arp2/3 complex and TIRF microscopy to visualize filament severing and the loss of actin filament branches. Cofilin severs filaments optimally when few actin subunits are occupied but dissociates branches rapidly only at higher occupancies. Effective debranching is nevertheless achieved, as a result of cooperative binding and reduced affinity of Arp2/3 complex for the filament, at cofilin concentrations below those required for direct competition.\nCofilin rapidly dissociates Arp2/3 complex and branches by direct competition for binding sites on the actin filament and by propagation of structural changes in the actin filament that reduce affinity for Arp2/3 complex.","doi":"10.1016/j.cub.2009.02.060","authors":"Chan C, Beltzner CC, Pollard TD","authors_abbrev":"Chan C et al.","pubmed_publication_date":"14 Apr 2009","pubmed_entrez_date":"2009-04-14","publication_year":"2009","canto_session_key":"828bbb188ef55b19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-09-19 17:50:35","canto_approved_date":"2022-09-04 08:40:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-19 17:50:27","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.10c","SPAC20G4.06c","SPAC630.03","SPAC11H11.06","SPBC1778.08c","SPAC17G8.04c","SPAC6G9.07c","SPBC14C8.06"],"gene_count":8,"ltp_gene_count":1,"approved_date":"2017-09-19"},{"uniquename":"PMID:34083046","title":"Function and molecular mechanisms of APE2 in genome and epigenome integrity.","citation":"Mutat Res Rev Mutat Res 2021;787:108347","abstract":"APE2 is a rising vital player in the maintenance of genome and epigenome integrity. In the past several years, a series of studies have shown the critical roles and functions of APE2. We seek to provide the first comprehensive review on several aspects of APE2 in genome and epigenome integrity. We first summarize the distinct functional domains or motifs within APE2 including EEP (endonuclease/exonuclease/phosphatase) domain, PIP box and Zf-GRF motifs from eight species (i.e., Homo sapiens, Mus musculus, Xenopus laevis, Ciona intestinalis, Arabidopsis thaliana, Schizosaccharomyces pombe, Saccharomyces cerevisiae, and Trypanosoma cruzi). Then we analyze various APE2 nuclease activities and associated DNA substrates, including AP endonuclease, 3'-phosphodiesterase, 3'-phosphatase, and 3'-5' exonuclease activities. We also examine several APE2 interaction proteins, including PCNA, Chk1, APE1, Myh1, and homologous recombination (HR) factors such as Rad51, Rad52, BRCA1, BRCA2, and BARD1. Furthermore, we provide insights into the roles of APE2 in various DNA repair pathways (base excision repair, single-strand break repair, and double-strand break repair), DNA damage response (DDR) pathways (ATR-Chk1 and p53-dependent), immunoglobulin class switch recombination and somatic hypermutation, as well as active DNA demethylation. Lastly, we summarize critical functions of APE2 in growth, development, and diseases. In this review, we provide the first comprehensive perspective which dissects all aspects of the multiple-function protein APE2 in genome and epigenome integrity.","doi":"10.1016/j.mrrev.2020.108347","authors":"Lin Y, McMahon A, Driscoll G, Bullock S, Zhao J, Yan S","authors_abbrev":"Lin Y et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-06-04","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-06-06 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1921.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11191205","title":"The Schizosaccharomyces pombe sep15+ gene encodes a protein homologous to the Med8 subunit of the Saccharomyces cerevisiae transcriptional mediator complex.","citation":"Curr Genet 2000 Dec;38(5):227-32","abstract":"We previously described the isolation of mutants defective in cell separation and the identification of 16 sep genes with complex functions. Here we report on the cloning and analysis of sep15+. The deduced amino acid sequence of the Sep15 protein shows significant homology to Med8, a component of the Saccharomyces cerevisiae transcription mediator complex. The mutation sep15-598 confers hyphal morphology and causes temperature-sensitive lethality. Disruption of sep15+ is lethal, indicating that Sep15 exerts an essential function and its role in cell separation is indirect.","authors":"Zilahi E, Miklós I, Sipiczki M","authors_abbrev":"Zilahi E et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2001-02-24","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21.04"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:28643116","title":"Express yourself: how PP2A-B55 Pab1  helps TORC1 talk to TORC2.","citation":"Curr Genet 2018 Feb;64(1):43-51","abstract":"The control of cell fate, growth and proliferation in response to nitrogen availability is a tightly controlled process, with the two TOR complexes (TORC1 and TORC2) and their effectors playing a central role. PP2A-B55 Pab1  has recently been shown to be a key element in this response in fission yeast, where it regulates cell cycle progression and sexual differentiation. Importantly, a recent study from our group has shown that PP2A-B55 Pab1  acts as a mediator between the activities of the two TOR signaling modules, enabling a crosstalk that is required to engage in the differentiation program. In this review, we recapitulate the studies that have led to our current understanding of the interplay between TOR complexes. Moreover, we discuss several aspects of the response to nitrogen availability that still require further attention, and which will be important in the future to fully realize the implications of phosphatase activity in the context of TOR signaling.","doi":"10.1007/s00294-017-0721-8","authors":"Martín R, Lopez-Aviles S","authors_abbrev":"Martín R et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2017-06-24","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-06-25 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19473263","title":"The involvement of the Schizosaccharomyces pombe sep9/spt8 gene in the regulation of septum cleavage.","citation":"FEMS Yeast Res 2009 Aug;9(5):757-67","abstract":"Schizosaccharomyces cells divide by medial septation, followed by enzymatic degradation of parts of the septum (septum cleavage) to allow the sister cells to separate from each other. In a previous study we found that the cell separation mutant sep9-307 was defective in a gene that encodes a protein highly similar in sequence to the Saccharomyces cerevisiae protein Spt8, a subunit of the SAGA complex. Here, we show that the sep9-307 mutation causes a frameshift in translation. The deletion of sep9(+) is not lethal but abolishes normal septum cleavage by reducing the activity of ace2(+), a gene coding for a transcription factor of numerous genes producing proteins for septum cleavage. Indirect evidence indicates that Sep9 might also act directly in the transcription of certain target genes (e.g. eng1(+)) of this regulator. sep9-307 is synthetically lethal with mutations in the cell separation genes sep11/med18(+) and sep15/med8(+), which encode subunits of the general transcription factor mediator. Heterologous expression of SPT8 and the putative Schizosaccharomyces japonicus sep9(+) orthologue cannot substitute for sep9(+). Both Spt8 and the fission yeast proteins have highly acidic (74-76 amino-acid long) N-terminal regions with no sequence conservation.","doi":"10.1111/j.1567-1364.2009.00522.x","authors":"Batta G, Szilagyi Z, Laczik M, Sipiczki M","authors_abbrev":"Batta G et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-05-29","publication_year":"2009","canto_session_key":"e0d72f6e0665c15c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-05-01 20:47:42","canto_approved_date":"2018-05-02 08:16:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-05-01 20:47:34","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCP31B10.03c","SPAC821.09","SPBC21.04","SPAC5D6.05","SPBC14C8.17c","SPAC6G10.12c","SPAPJ760.03c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2018-05-01"},{"uniquename":"PMID:1558757","title":"Centromere and kinetochore structure.","citation":"Curr Opin Cell Biol 1992 Feb;4(1):86-93","abstract":"Recent studies have begun to yield some insight into the structural and regulatory components of centromeres, and new assays have been developed that promise to be of use in advancing our understanding of centromere structure and function. In the budding yeast Saccharomyces cerevisiae new proteins that are required for centromere function have been identified and an in vitro microtubule-binding assay that should assist in dissecting the process of centromere microtubule attachment has been developed. The centromere-specific DNA sequences in the fission yeast Schizosaccharomyces pombe have been identified and partially characterized. In addition, several mammalian centromere proteins have been further characterized, and localization and inhibition studies suggest roles for these proteins in the regulation and assembly of a functional kinetochore.","authors":"Earnshaw WC, Tomkiel JE","authors_abbrev":"Earnshaw WC et al.","pubmed_publication_date":"Feb 1992","pubmed_entrez_date":"1992-02-01","publication_year":"1992","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22405003","title":"Mechanistic insights into the activation of Rad51-mediated strand exchange from the structure of a recombination activator, the Swi5-Sfr1 complex.","citation":"Structure 2012 Mar 07;20(3):440-9","abstract":"Rad51 forms a helical filament on single-stranded DNA and promotes strand exchange between two homologous DNA molecules during homologous recombination. The Swi5-Sfr1 complex interacts directly with Rad51 and stimulates strand exchange. Here we describe structural and functional aspects of the complex. Swi5 and the C-terminal core domain of Sfr1 form an essential activator complex with a parallel coiled-coil heterodimer joined firmly together via two previously uncharacterized leucine-zipper motifs and a bundle. The resultant coiled coil is sharply kinked, generating an elongated crescent-shaped structure suitable for transient binding within the helical groove of the Rad51 filament. The N-terminal region of Sfr1, meanwhile, has an interface for binding of Rad51. Our data suggest that the snug fit resulting from the complementary geometry of the heterodimer activates the Rad51 filament and that the N-terminal domain of Sfr1 plays a role in the efficient recruitment of the Swi5-Sfr1 complex to the Rad51 filaments.","doi":"10.1016/j.str.2012.01.005","authors":"Kuwabara N, Murayama Y, Hashimoto H, Kokabu Y, Ikeguchi M, Sato M, Mayanagi K, Tsutsui Y, Iwasaki H, Shimizu T","authors_abbrev":"Kuwabara N et al.","pubmed_publication_date":"07 Mar 2012","pubmed_entrez_date":"2012-03-13","publication_year":"2012","canto_session_key":"f63b345319dc4c0b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-08-03 13:32:55","canto_approved_date":"2023-01-26 10:17:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-03 13:32:48","canto_added_date":"2012-11-19 00:16:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPBC409.03","SPBC28F2.07"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-08-03","pdb_entries":[{"pdb_id":"3viq","gene_chains":[{"gene_uniquename":"SPBC28F2.07","chain":"A/C","position":"181-299"},{"gene_uniquename":"SPBC409.03","chain":"B/D","position":"1-85"}],"title":"Crystal structure of Swi5-Sfr1 complex from fission yeast","entry_authors":"Kuwabara N,Murayama Y,Hashimoto H,Kokabu Y,Ikeguchi M,Sato M,Mayanagi K,Tsutsui Y,Iwasaki H,Shimizu T","entry_authors_abbrev":"Kuwabara N et al.","reference_uniquename":"PMID:22405003","experimental_method":"X-ray","resolution":"2.2"},{"pdb_id":"3vir","gene_chains":[{"gene_uniquename":"SPBC409.03","chain":"A/B/C/D","position":"1-85"}],"title":"Crystal strcture of Swi5 from fission yeast","entry_authors":"Kuwabara N,Yamada N,Hashimoto H,Sato M,Iwasaki H,Shimizu T","entry_authors_abbrev":"Kuwabara N et al.","reference_uniquename":"PMID:22405003","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:5431621","title":"Effect of high osmotic pressure on DNA synthesis in the fission yeast, Schizosaccharomyces pombe.","citation":"Exp Cell Res 1970 Jul;61(1):213-6","abstract":"","authors":"Duffus JH, Mitchell CJ","authors_abbrev":"Duffus JH et al.","pubmed_publication_date":"Jul 1970","pubmed_entrez_date":"1970-07-01","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30712100","title":"Mixed alcoholic fermentation of Schizosaccharomyces pombe and Lachancea thermotolerans and its influence on mannose-containing polysaccharides wine Composition.","citation":"AMB Express 2019 Feb 02;9(1):17","abstract":"This study researched the winemaking performance of new biotechnology involving the cooperation of Lachancea and Schizosaccharomyces genera in the production of wine. In all fermentations where Lachancea thermotolerans was involved, higher lactic acid concentrations appeared, while all fermentations where Schizosaccharomyces pombe was involved, lower levels in malic acid concentration took place. The sensorial properties of the final wines varied accordingly. Differences in mouthfeel properties and acidity occurred in the different fermentation trials. Fermentations with the highest concentration of hydrolyzed mannose showed the highest mouthfeel properties, but the lack of acidity reduced their overall impression. Wines made from a combination of L. thermotolerans and S. pombe showed the highest overall impression and were preferred by the tasters due to the balance between mouthfeel properties and acidity.","doi":"10.1186/s13568-019-0738-0","authors":"Benito Á, Calderón F, Benito S","authors_abbrev":"Benito Á et al.","pubmed_publication_date":"02 Feb 2019","pubmed_entrez_date":"2019-02-04","publication_year":"2019","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2019-02-05 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25342201","title":"Chromosome conformation maps in fission yeast reveal cell cycle dependent sub nuclear structure.","citation":"Nucleic Acids Res 2014 Nov 10;42(20):12585-99","abstract":"Successful progression through the cell cycle requires spatial and temporal regulation of gene transcript levels and the number, positions and condensation levels of chromosomes. Here we present a high resolution survey of genome interactions in Schizosaccharomyces pombe using synchronized cells to investigate cell cycle dependent changes in genome organization and transcription. Cell cycle dependent interactions were captured between and within S. pombe chromosomes. Known features of genome organization (e.g. the clustering of telomeres and retrotransposon long terminal repeats (LTRs)) were observed throughout the cell cycle. There were clear correlations between transcript levels and chromosomal interactions between genes, consistent with a role for interactions in transcriptional regulation at specific stages of the cell cycle. In silico reconstructions of the chromosome organization within the S. pombe nuclei were made by polymer modeling. These models suggest that groups of genes with high and low, or differentially regulated transcript levels have preferred positions within the S. pombe nucleus. We conclude that the S. pombe nucleus is spatially divided into functional sub-nuclear domains that correlate with gene activity. The observation that chromosomal interactions are maintained even when chromosomes are fully condensed in M phase implicates genome organization in epigenetic inheritance and bookmarking.","doi":"10.1093/nar/gku965","authors":"Grand RS, Pichugina T, Gehlen LR, Jones MB, Tsai P, Allison JR, Martienssen R, O'Sullivan JM","authors_abbrev":"Grand RS et al.","pubmed_publication_date":"10 Nov 2014","pubmed_entrez_date":"2014-10-25","publication_year":"2014","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2014-10-26 00:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012814","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19734689","title":"Cell-cycle independent chromosome condensation in Schizosaccharomyces pombe induced by high hydrostatic pressure treatment.","citation":"Biosci Biotechnol Biochem 2009 Sep;73(9):1956-61","abstract":"We exposed Schizosaccharomyces pombe to high hydrostatic pressure treatment (HPT) of 75 MPa at 28 degrees Celsius for 30 min and then observed that the DAPI-stained chromosomal DNA had shrunk compactly. We termed this phenomenon HPT-induced chromosome condensation (HPT-CC). HPT did not significantly decrease viability. The condensed state was released when HPT cells were cultured at 28 degrees Celsius for 30 min. The condensation was not caused by shrinking of the nuclear envelope, which was visualized by YFP-tagged importin alpha. HPT-CC was cell cycle independent, because it was observed in almost all randomly cultured cells. The condensin complex (Cut3, Cut14, and three other proteins) is responsible for cell cycle dependent CC. Studies with Cut3-YFP and ts mutants of Cut3 and Cut14 confirmed that HPT-CC was independent of condensin molecules. HPT-CC was also observed in Saccharomyces cerevisiae. HPT-CC appears likely to be a temporal stress response to high hydrostatic pressure found at least in yeasts.","authors":"Arai S, Kawarai T, Arai R, Yoshida M, Furukawa S, Ogihara H, Yamasaki M","authors_abbrev":"Arai S et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-09-08","publication_year":"2009","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16598689","title":"The Schizosaccharomyces pombe cfr1+ gene participates in mating through a new pathway that is independent of fus1+.","citation":"Yeast 2006 Apr 15;23(5):375-88","abstract":"Conjugation is a complex event directed to ensure the transfer of genetic material, which is achieved by the union of two cells. In fungi, success of this relevant process requires digestion of the cell wall at the point where both cells have agglutinated and, later, the union of the plasma membranes and nuclei from the mating partners. In order to gain information about cell fusion, we have cloned and disrupted the cfr1+ gene from the fission yeast Schizosaccharomyces pombe. cfr1+ gene is slightly induced at the beginning of mating but Cfr1p protein is degraded soon after the cells are transferred to nitrogen-lacking medium. cfr1Delta mutants present a defect in cell fusion owing to a failure in the digestion of the cell walls between the two parental cells. Finally, cytological and genetic analyses show that cfr1+ acts in a new pathway involved in conjugation that is independent of fus1+, the only gene that has been found to be specifically required for cell fusion during mating in the fission yeast.","authors":"Cartagena-Lirola H, Durán A, Valdivieso MH","authors_abbrev":"Cartagena-Lirola H et al.","pubmed_publication_date":"15 Apr 2006","pubmed_entrez_date":"2006-04-07","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G4.02c","SPAC6G9.12"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:25483891","title":"Mdm31 protein mediates sensitivity to potassium ionophores but does not regulate mitochondrial morphology or phospholipid trafficking in Schizosaccharomyces pombe.","citation":"Yeast 2015 Mar;32(3):345-54","abstract":"Mdm31p is an inner mitochondrial membrane (IMM) protein with unknown function in Saccharomyces cerevisiae. Mutants lacking Mdm31p contain only a few giant spherical mitochondria with disorganized internal structure, altered phospholipid composition and disturbed ion homeostasis, accompanied by increased resistance to the electroneutral K+ /H+ ionophore nigericin. These phenotypes are interpreted as resulting from diverse roles of Mdm31p, presumably in linking mitochondrial DNA (mtDNA) to the machinery involved in segregation of mitochondria, in mediating cation transport across IMM and in phospholipid shuttling between mitochondrial membranes. To investigate which of the roles of Mdm31p are conserved in ascomycetous yeasts, we analysed the Mdm31p orthologue in Schizosaccharomyces pombe. Our results demonstrate that, similarly to its S. cerevisiae counterpart, SpMdm31 is a mitochondrial protein and its absence results in increased resistance to nigericin. However, in contrast to S. cerevisiae, Sz. pombe cells lacking SpMdm31 are also less sensitive to the electrogenic K+ ionophore valinomycin. Moreover, mitochondria of the fission yeast mdm31Δ mutant display no changes in morphology or phospholipid composition. Therefore, in terms of function, the two orthologous proteins appear to have considerably diverged between these two evolutionarily distant yeast species, possibly sharing only their participation in ion homeostasis.","doi":"10.1002/yea.3062","authors":"Ivan B, Lajdova D, Abelovska L, Balazova M, Nosek J, Tomaska L","authors_abbrev":"Ivan B et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2014-12-09","publication_year":"2015","canto_session_key":"df21e2714ebca0b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-10-26 12:33:34","canto_approved_date":"2021-04-16 15:44:08","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-10-13 16:32:52","canto_added_date":"2014-12-10 01:16:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H1.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-26"},{"uniquename":"PMID:15289660","title":"Kinetochore and heterochromatin domains of the fission yeast centromere.","citation":"Chromosome Res 2004;12(6):521-34","abstract":"Fission yeast centromeres are composed of two distinctive chromatin domains. The central domain nucleosomes contain the histone H3-like protein CENP-A(Cnp1). In contrast, the flanking repeats are coated with silent chromatin in which Swi6 (HP1) binds histone H3 methylated on lysine 9 that is induced by the action of the RNA interference pathway on non-coding centromeric transcripts. The overall structure is similar to that of metazoan centromeres where the kinetochore is embedded in surrounding heterochromatin. Kinetochore specific proteins associate with the central domain and affect silencing in that region. The flanking heterochromatin is required to recruit cohesin and mediate tight physical cohesion between sister centromeres. The loss of silencing that accompanies defects in heterochromatin has been invaluable as a tool in the investigation of centromere function. Both the heterochromatin and kinetochore regions are required for the de novo assembly of a functional centromere on DNA constructs, suggesting that heterochromatin may provide an environment that promotes kinetochore assembly within the central domain. The process is clearly epigenetically regulated. Fission yeast kinetochores associate with 2-4 microtubules, and flanking heterochromatin may be required to promote the orientation of multiple microtubule binding sites on one kinetochore towards the same pole and thus prevent merotelic orientation.","authors":"Pidoux AL, Allshire RC","authors_abbrev":"Pidoux AL et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-08-04","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32101485","title":"Aurora B and condensin are dispensable for chromosome arm and telomere separation during meiosis II.","citation":"Mol Biol Cell 2020 Apr 15;31(9):889-905","abstract":"In mitosis, while the importance of kinetochore (KT)-microtubule (MT) attachment has been known for many years, increasing evidence suggests that telomere dysfunctions also perturb chromosome segregation by contributing to the formation of chromatin bridges at anaphase. Recent evidence suggests that Aurora B kinase ensures proper chromosome segregation during mitosis not only by controlling KT-MT attachment but also by regulating telomere and chromosome arm separation. However, whether and how Aurora B governs telomere separation during meiosis has remained unknown. Here, we show that fission yeast Aurora B localizes at telomeres during meiosis I and promotes telomere separation independently of the meiotic cohesin Rec8. In meiosis II, Aurora B controls KT-MT attachment but appears dispensable for telomere and chromosome arm separation. Likewise, condensin activity is nonessential in meiosis II for telomere and chromosome arm separation. Thus, in meiosis, the requirements for Aurora B are distinct at centromeres and telomeres, illustrating the critical differences in the control of chromosome segregation between mitosis and meiosis II.","doi":"10.1091/mbc.E20-01-0021","authors":"Berthezene J, Reyes C, Li T, Coulon S, Bernard P, Gachet Y, Tournier S","authors_abbrev":"Berthezene J et al.","pubmed_publication_date":"15 Apr 2020","pubmed_entrez_date":"2020-02-27","publication_year":"2020","canto_session_key":"514e32e84e92386c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011742","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5591298","title":"Lethal sectoring and the origin of complete nutants in Schizosaccharomyces pombe.","citation":"Mutat Res 1967;4(6):875-8","abstract":"","authors":"Auerbach C","authors_abbrev":"Auerbach C","pubmed_publication_date":"1967","pubmed_entrez_date":"1967-11-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18780734","title":"Cohesin and recombination proteins influence the G1-to-S transition in azygotic meiosis in Schizosaccharomyces pombe.","citation":"Genetics 2008 Oct;180(2):727-40","abstract":"To determine whether recombination and/or sister-chromatid cohesion affect the timing of meiotic prophase events, the horsetail stage and S phase were analyzed in Schizosaccharomyces pombe strains carrying mutations in the cohesin genes rec8 or rec11, the linear element gene rec10, the pairing gene meu13, the double-strand-break formation genes rec6, rec7, rec12, rec14, rec15, and mde2, and the recombination gene dmc1. The double-mutant strains rec8 rec11 and rec8 rec12 were also assayed. Most of the single and both double mutants showed advancement of bulk DNA synthesis, start of nuclear movement (horsetail stage), and meiotic divisions by up to 2 hr. Only mde2 and dmc1 deletion strains showed wild-type timing. Contrasting behavior was observed for rec8 deletions (delayed by 1 hr) compared to a rec8 point mutation (advanced by 1 hr). An hypothesis for the role of cohesin and recombination proteins in the control of the G(1)-to-S transition is proposed. Finally, differences between azygotic meiosis and two other types of fission yeast meiosis (zygotic and pat1-114 meiosis) are discussed with respect to possible control steps in meiotic G(1).","doi":"10.1534/genetics.108.092619","authors":"Doll E, Molnar M, Cuanoud G, Octobre G, Latypov V, Ludin K, Kohli J","authors_abbrev":"Doll E et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-09-11","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4E9.01c","SPBC29A10.14"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9264466","title":"Distinct subunit functions and cell cycle regulated phosphorylation of 20S APC/cyclosome required for anaphase in fission yeast.","citation":"J Cell Sci 1997 Aug;110 ( Pt 15):1793-804","abstract":"We show here that the fission yeast gene products Cut9 and Nuc2 are the subunits of the 20S complex, the putative APC (anaphase promoting complex)/cyclosome which contains ubiquitin ligase activity required for cyclin and Cut2 destruction. The assembly of Cut9 into the 20S complex requires functional Nuc2, and vice versa. The size of fission yeast APC/cyclosome is similar to that of higher eukaryotes, but differs greatly from that (36S) of budding yeast. The 20S complex is present in cells arrested at different stages of the cell cycle, and becomes slightly heavier in mitosis than interphase. Cut9 in the 20S complex is hyperphosphorylated specifically at the time of metaphase. The truncated forms of Cut9 block entry into mitosis, however. The 20S assembly impaired in the cut9 mutant can be restored by elevating the level of a novel gene product Hcnl, similar to budding yeast Cdc26. Furthermore, deletion of protein kinase PKA (Pkal) suppresses the phenotype of the cut9 mutation and reduces phosphorylation of Cut9. In contrast, PP1 (Dis2) phosphatase mutation shows the reverse effect on the phenotype of cut9. The Cut9 subunit is likely to be a target for regulating APC/ cyclosome function through protein-protein interactions and phosphorylation.","authors":"Yamada H, Kumada K, Yanagida M","authors_abbrev":"Yamada H et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"fed93fe54aa51313","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-27 16:09:33","canto_approved_date":"2026-02-06 13:29:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-18 16:55:17","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.12","SPAC6F12.15c","SPBC106.10","SPBC776.02c","SPBC19C7.03","SPAC17C9.01c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-11-27"},{"uniquename":"PMID:29967291","title":"Polymerase pausing induced by sequence-specific RNA-binding protein drives heterochromatin assembly.","citation":"Genes Dev 2018 Jul 01;32(13-14):953-964","abstract":"In  Schizosaccharomyces pombe , transcripts derived from the pericentromeric  dg  and  dh  repeats promote heterochromatin formation via RNAi as well as an RNAi-independent mechanism involving the RNA polymerase II (RNAPII)-associated RNA-binding protein Seb1 and RNA processing activities. We show that Seb1 promotes long-lived RNAPII pauses at pericentromeric repeat regions and that their presence correlates with the heterochromatin-triggering activities of the corresponding  dg  and  dh  DNA fragments. Globally increasing RNAPII stalling by other means induces the formation of novel large ectopic heterochromatin domains. Such ectopic heterochromatin occurs even in cells lacking RNAi. These results uncover Seb1-mediated polymerase stalling as a signal necessary for heterochromatin nucleation.","doi":"10.1101/gad.310136.117","authors":"Parsa JY, Boudoukha S, Burke J, Homer C, Madhani HD","authors_abbrev":"Parsa JY et al.","pubmed_publication_date":"01 Jul 2018","pubmed_entrez_date":"2018-07-04","publication_year":"2018","canto_session_key":"2749633df7963677","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-07-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC222.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19342232","title":"New Rev-export inhibitor from Alpinia galanga and structure-activity relationship.","citation":"Bioorg Med Chem Lett 2009 May 01;19(9):2555-7","abstract":"Bioassay-guided separation by use of the fission yeast expressing NES of Rev, an HIV-1 viral regulatory protein, disclosed 1'-acetoxychavicol acetate (ACA, 1) as a new inhibitor for nuclear export of Rev from the roots of Alpinia galanga. Both analysis for mechanism of action with biotinylated probe (2) and several synthesized analogs established crucial portions in 1 for Rev-export inhibitory activity.","doi":"10.1016/j.bmcl.2009.03.047","authors":"Tamura S, Shiomi A, Kaneko M, Ye Y, Yoshida M, Yoshikawa M, Kimura T, Kobayashi M, Murakami N","authors_abbrev":"Tamura S et al.","pubmed_publication_date":"01 May 2009","pubmed_entrez_date":"2009-04-04","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2120044","title":"Complementation of fission yeast cdc2ts and cdc25ts mutants identifies two cell cycle genes from Drosophila: a cdc2 homologue and string.","citation":"EMBO J 1990 Nov;9(11):3565-71","abstract":"We have exploited the universality of the molecular mechanisms that control entry into mitosis to clone the Drosophila melanogaster homologues of fission yeast Schizosaccharomyces pombe cell division control (cdc) genes by the complementation of temperature sensitive mutations. The Drosophila genes were expressed in S.pombe as cDNAs from the SP6 promoter. Successful recovery of complementing plasmids required that we first 'adapt' pooled plasmids from a Drosophila embryonic cDNA library for propagation in fission yeast by introducing an ars1-LEU2 DNA fragment into the vector. This library was introduced into S.pombe cdc2 and cdc25 mutants, and plasmids isolated carrying cDNAs that complement these mutations. The gene that encodes the Drosophila cdc2 homologue maps to a single locus in the Drosophila genome at 31E on chromosome 2. It is expressed maternally to provide mRNA in syncytial embryos, and appears to be zygotically expressed in mitotically active regions of the cellularized embryo. We have isolated two different cDNAs that complement cdc25-22. One corresponds to a transcript of string, previously described as the Drosophila homologue of cdc25, and the other to a gene that has not been previously characterized.","authors":"Jimenez J, Alphey L, Nurse P, Glover DM","authors_abbrev":"Jimenez J et al.","pubmed_publication_date":"Nov 1990","pubmed_entrez_date":"1990-11-01","publication_year":"1990","canto_session_key":"eff8638ffab34ecb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 13:07:01","canto_session_submitted_date":"2012-03-03 13:04:43","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:8382769","title":"Identification of RNA sequences and structural elements required for assembly of fission yeast SRP54 protein with signal recognition particle RNA.","citation":"Mol Cell Biol 1993 Mar;13(3):1353-62","abstract":"Signal recognition particle (SRP) is a ribonucleoprotein composed of six polypeptides and a single RNA molecule. SRP RNA can be divided into four structural domains, the last of which is the most highly conserved and, in Schizosaccharomyces pombe, is the primary location to which deleterious mutations map. The ability of mammalian SRP54 protein (SRP54p) to bind Escherichia coli 4.5S RNA, a homolog of SRP RNA which contains only domain IV, suggested that SRP54p might interact directly with this region. To determine whether domain IV is critical for SRP54p binding in fission yeast cells, we used a native immunoprecipitation-RNA sequencing assay to test 13 mutant SRP RNAs for the ability to associate with the protein in vivo. The G156A mutation, which alters the 5' residue of the noncanonical first base pair of the domain IV terminal helix and confers a mild conditional growth defect, reduces assembly of the RNA with SRP54p. Mutating either of the two evolutionarily invariant residues in the bulged region 5' to G156 is more deleterious to growth and virtually abolishes SRP54p binding. We conclude that the conservation of nucleotides 154 to 156 is likely to be a consequence of their role as a sequence-specific recognition element for the SRP54 protein. We also tested a series of mutants with nucleotide substitutions in the conserved tetranucleotide loop and adjoining stem of domain IV. Although tetraloop mutations are deleterious to growth, they have little effect on SRP54p binding. Mutations which disrupt the base pair flanking the tetraloop result in conditional growth defects and significantly reduce association with SRP54p. Disruption of the other two base pairs in the short stem adjacent to the tetranucleotide loop has similar but less dramatic effects on SRP54p binding. These data provide the first evidence that both sequence-specific contacts and the structural integrity of domain IV of SRP RNA are important for assembly with SRP54p.","authors":"Selinger D, Brennwald P, Liao X, Wise JA","authors_abbrev":"Selinger D et al.","pubmed_publication_date":"Mar 1993","pubmed_entrez_date":"1993-03-01","publication_year":"1993","canto_session_key":"b1d7c5491a1c7cdb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-06-12 16:39:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-12 16:39:42","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_8382769_phaf.tsv"}],"genes":["SPNCRNA.98","SPCC188.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-12"},{"uniquename":"PMID:2300054","title":"Schizosaccharomyces pombe ras1 and byr1 are functionally related genes of the ste family that affect starvation-induced transcription of mating-type genes.","citation":"Mol Cell Biol 1990 Feb;10(2):549-60","abstract":"We have further investigated the function of the ras1 and byr1 genes, which were previously shown to be critical for sexual differentiation in fission yeast cells. Several physiological similarities between strains containing null alleles of these genes supports the idea that ras1 and byr1 are functionally closely related. Furthermore, we have found that byr1 is allelic to ste1, one of at least 10 genes which when mutated can cause sterility. Since ras1 had previously been found to be allelic to ste5, both ras and byr genes are now clearly shown to be a part of the ste gene family, thus confirming their close functional relationship. The observation that the mating-type loci could overcome the sporulation block of ras1 and byr1 mutant strains prompted investigation of the role of the ras-byr pathway in the induction of the mating-type gene transcripts upon nitrogen starvation. By Northern analysis of RNA preparations from strains carrying wild-type or mutant ras1 alleles and grown to different stages of the growth cycle, we have shown that ras1 plays an important role in inducing the Pi transcript of the mating-type loci and the mei3 gene transcript. These observations provide a molecular basis for the role of the ste gene family, including ras1 and byr1, in meiosis and indicate that further characterization of other ste genes would be very useful for elucidating the mechanism of ras1 function in fission yeast cells.","authors":"Nadin-Davis SA, Nasim A","authors_abbrev":"Nadin-Davis SA et al.","pubmed_publication_date":"Feb 1990","pubmed_entrez_date":"1990-02-01","publication_year":"1990","canto_session_key":"9afd277c286ab6f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-14 21:58:51","canto_approved_date":"2022-01-03 19:33:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-18 13:00:43","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.17c","SPBC119.04","SPAC17H9.09c","SPAC1D4.13","SPMTR.01","SPBC23G7.09","SPMTR.02"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2018-06-14"},{"uniquename":"PMID:11460168","title":"A MAP kinase-dependent actin checkpoint ensures proper spindle orientation in fission yeast.","citation":"Nature 2001 Jul 19;412(6844):352-5","abstract":"The accurate segregation of chromosomes at mitosis depends on a correctly assembled bipolar spindle that exerts balanced forces on each sister chromatid. The integrity of mitotic chromosome segregation is ensured by the spindle assembly checkpoint (SAC) that delays mitosis in response to defective spindle organisation or failure of chromosome attachment. Here we describe a distinct mitotic checkpoint in the fission yeast, Schizosaccharomyces pombe, that monitors the integrity of the actin cytoskeleton and delays sister chromatid separation, spindle elongation and cytokinesis until spindle poles have been properly oriented. This mitotic delay is imposed by a stress-activated mitogen-activated protein (MAP) kinase pathway but is independent of the anaphase-promoting complex (APC).","authors":"Gachet Y, Tournier S, Millar JB, Hyams JS","authors_abbrev":"Gachet Y et al.","pubmed_publication_date":"19 Jul 2001","pubmed_entrez_date":"2001-07-19","publication_year":"2001","canto_session_key":"2f34923cbe339952","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-23 09:25:13","canto_approved_date":"2025-01-31 10:58:44","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-04-16 14:40:58","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":17,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC338.17c","SPAC24H6.05","SPAC19D5.01","SPAC24B11.06c","SPBC20F10.06","SPBC29B5.01","SPBC582.03","SPBC32H8.12c","SPBC14C8.01c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2024-04-23"},{"uniquename":"PMID:27005325","title":"Diverse fission yeast genes required for responding to oxidative and metal stress: Comparative analysis of glutathione-related and other defense gene deletions.","citation":"Genes Cells 2016 Jun;21(6):530-42","abstract":"Living organisms have evolved multiple sophisticated mechanisms to deal with reactive oxygen species. We constructed a collection of twelve single-gene deletion strains of the fission yeast Schizosaccharomyces pombe designed for the study of oxidative and heavy metal stress responses. This collection contains deletions of biosynthetic enzymes of glutathione (Δgcs1 and Δgsa1), phytochelatin (Δpcs2), ubiquinone (Δabc1) and ergothioneine (Δegt1), as well as catalase (Δctt1), thioredoxins (Δtrx1 and Δtrx2), Cu/Zn- and Mn- superoxide dismutases (SODs; Δsod1 and Δsod2), sulfiredoxin (Δsrx1) and sulfide-quinone oxidoreductase (Δhmt2). First, we employed metabolomic analysis to examine the mutants of the glutathione biosynthetic pathway. We found that ophthalmic acid was produced by the same enzymes as glutathione in S. pombe. The identical genetic background of the strains allowed us to assess the severity of the individual gene knockouts by treating the deletion strains with oxidative agents. Among other results, we found that glutathione deletion strains were not particularly sensitive to peroxide or superoxide, but highly sensitive to cadmium stress. Our results show the astonishing diversity in cellular adaptation mechanisms to various types of oxidative and metal stress and provide a useful tool for further research into stress responses.","doi":"10.1111/gtc.12359","authors":"Pluskal T, Sajiki K, Becker J, Takeda K, Yanagida M","authors_abbrev":"Pluskal T et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-03-24","publication_year":"2016","canto_session_key":"619a912c82d69329","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomas Pluskal","canto_first_approved_date":"2017-01-17 10:45:54","canto_approved_date":"2022-06-16 07:13:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-29 22:46:49","canto_added_date":"2016-03-29 00:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":127,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Tomas Pluskal","community_curator":true,"annotation_count":39,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.10c","SPBC2G5.06c","SPAC1486.01","SPAC24B11.06c","SPBC106.02c","SPBC2D10.18","SPBC12D12.07c","SPAC3F10.04","SPAC3H1.10","SPBC1604.01","SPCC757.07c","SPAC821.10c","SPAC7D4.07c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2017-01-17"},{"uniquename":"PMID:27698241","title":"Reporter Gene Silencing Assays in Fission Yeast.","citation":"Cold Spring Harb Protoc 2016 Oct 03;2016(10)","abstract":"Reporter gene silencing assays provide a facile method for assessing the function of heterochromatin in Schizosaccharomyces pombe They use strains containing auxotrophic markers (commonly ura4 +  or ade6 + ) located within a heterochromatic region. Transcriptional silencing of these reporters can be assessed by plating serial dilutions of cells onto minimal agar. In addition, silencing of ura4 +  renders cells resistant to 5-fluoroorotic acid (5-FOA) and ade6 +  silencing results in red colony color on adenine-limiting agar. Various reporters for each of the major heterochromatic domains (telomeres, centromeres, and the mating type locus) are available and, importantly, transcriptional silencing is correlated with the proper function of these regions.","doi":"10.1101/pdb.prot091512","authors":"Cam HP, Whitehall S","authors_abbrev":"Cam HP et al.","pubmed_publication_date":"03 Oct 2016","pubmed_entrez_date":"2016-10-05","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-10-07 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15068886","title":"RNA silencing: a conserved antiviral immunity of plants and animals.","citation":"Virus Res 2004 Jun 01;102(1):109-15","abstract":"RNA silencing is a novel RNA-guided gene regulatory mechanism operational in a wide range of eukaryotic organisms from fission yeast, plants, to mammals. This article reviews the recent progress on aspects of RNA silencing that are related to its biological function as a conserved antiviral immunity of plants and animals, and highlights features of this novel antiviral response in invertebrate animals as compared to the known innate and adaptive immunities. Finally, we discuss evidence that suggests a natural antiviral role for RNA silencing in vertebrates as well as experimental approaches that may facilitate the identification of first mammalian viral suppressors of RNA silencing.","authors":"Ding SW, Li H, Lu R, Li F, Li WX","authors_abbrev":"Ding SW et al.","pubmed_publication_date":"01 Jun 2004","pubmed_entrez_date":"2004-04-08","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21441597","title":"RNA interference and heterochromatin assembly.","citation":"Cold Spring Harb Perspect Biol 2011 Sep 01;3(9):a003731","abstract":"In most eukaryotes, histone and DNA modifications are responsible for the silencing of genes integrated in heterochromatic sequences, as well as the silencing of pericentromeric repeats and transposable elements themselves. But the mechanisms that guide these modifications to heterochromatin during the cell cycle have been elusive. RNA interference takes advantage of heterochromatic transcription to process small RNAs and recruit enzymes required for both histone and DNA modifications, and is one such mechanism that has been identified. The processes are best understood in fission yeast and plants, but recent work in mammalian cells, especially in the germline, suggests these mechanisms may be highly conserved.","doi":"10.1101/cshperspect.a003731","authors":"Volpe T, Martienssen RA","authors_abbrev":"Volpe T et al.","pubmed_publication_date":"01 Sep 2011","pubmed_entrez_date":"2011-03-29","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27003292","title":"A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy.","citation":"Elife 2016 Mar 22;5","abstract":"Cells can enter into a dormant state when faced with unfavorable conditions. However, how cells enter into and recover from this state is still poorly understood. Here, we study dormancy in different eukaryotic organisms and find it to be associated with a significant decrease in the mobility of organelles and foreign tracer particles. We show that this reduced mobility is caused by an influx of protons and a marked acidification of the cytoplasm, which leads to widespread macromolecular assembly of proteins and triggers a transition of the cytoplasm to a solid-like state with increased mechanical stability. We further demonstrate that this transition is required for cellular survival under conditions of starvation. Our findings have broad implications for understanding alternative physiological states, such as quiescence and dormancy, and create a new view of the cytoplasm as an adaptable fluid that can reversibly transition into a protective solid-like state.","doi":"10.7554/eLife.09347","authors":"Munder MC, Midtvedt D, Franzmann T, Nüske E, Otto O, Herbig M, Ulbricht E, Müller P, Taubenberger A, Maharana S, Malinovska L, Richter D, Guck J, Zaburdaev V, Alberti S","authors_abbrev":"Munder MC et al.","pubmed_publication_date":"22 Mar 2016","pubmed_entrez_date":"2016-03-23","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12214219","title":"Cell biology: spinning actin to divide.","citation":"Nature 2002 Sep 05;419(6902):27-8","abstract":"","authors":"Narumiya S, Mabuchi I","authors_abbrev":"Narumiya S et al.","pubmed_publication_date":"05 Sep 2002","pubmed_entrez_date":"2002-09-06","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30759055","title":"Actin turnover ensures uniform tension distribution during cytokinetic actomyosin ring contraction.","citation":"Mol Biol Cell 2019 Apr 01;30(8):933-941","abstract":"In many eukaryotes, cytokinesis is facilitated by the contraction of an actomyosin ring (AMR). The exact mechanisms that lead to this contractility are unknown, although some models posit that actin turnover in the AMR is essential. The effect of reduced actin dynamics during AMR formation has been well studied in Schizosaccharomyces pombe; however, the corresponding effects on AMR contraction are not well understood. By using mutants of the fission yeast actin severing protein Adf1, we observed that contracting AMRs display a \"peeling\" phenotype, where bundles of actin and myosin peel off from one side of the AMR, and are pulled across to the opposite side. This occurs multiple times during cytokinesis and is dependent on the activity of myosins Myo2, Myp2, and Myo51. We found that the distribution of Myo2 in the AMR anticorrelates with the location of peeling events, suggesting that peeling is caused by a nonuniform tension distribution around the AMR, and that one of the roles of actin turnover is to maintain a uniform tension distribution around the AMR.","doi":"10.1091/mbc.E18-08-0511","authors":"Cheffings TH, Burroughs NJ, Balasubramanian MK","authors_abbrev":"Cheffings TH et al.","pubmed_publication_date":"01 Apr 2019","pubmed_entrez_date":"2019-02-14","publication_year":"2019","canto_session_key":"7efc8857a6e0c879","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-02-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40661419","title":"Protocol for the development and use of spike-in control for chromatin immunoprecipitation (ChIP) of chromatin-binding proteins.","citation":"bioRxiv 2025 May 16;","abstract":"Chromatin immunoprecipitation (ChIP) assays provide quantitative information about the genomic localization of chromatin-binding proteins. However, their sensitivity is limited by several technical variables. To generate high-confidence datasets, in this protocol, we used the  Saccharomyces cerevisiae  chromatin as an exogenous spike-in control for the ChIP of two  S. pombe  heterochromatin-associated proteins. This permitted normalization of the ChIP signals based on immunoprecipitation efficiencies across samples. Here, we describe the steps for spike-in control preparation, validation, and its use in data normalization. For complete details on the use and execution of this protocol, please refer to Khanduja et al.  1 .","doi":"10.1101/2025.05.13.653544","authors":"Khanduja JS, Motamedi M","authors_abbrev":"Khanduja JS et al.","pubmed_publication_date":"16 May 2025","pubmed_entrez_date":"2025-07-15","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-07-15 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2299673","title":"An intron-containing Schizosaccharomyces pombe U6 RNA gene can be transcribed by human RNA polymerase III.","citation":"J Mol Biol 1990 Jan 05;211(1):7-9","abstract":"A Schizosaccharomyces pombe U6 small nuclear RNA gene containing an intron has been described. We find that the S. pombe U6 gene is transcribed in a human (HeLa) cell S100 extract with an alpha-amanitin sensitivity characteristic of RNA polymerase III. The S. pombe U6 gene is also transcribed after transfection into human cells. The transcription of vertebrate U6 RNA genes by RNA polymerase III does not require intragenic control elements. The intron of the S. pombe U6 gene disrupts a \"box A\"-like intragenic sequence that is typically an RNA polymerase III transcription control element. This, together with the transcription of the S. pombe U6 gene by human RNA polymerase III, suggests that it is recognized by human U6 gene-specific transcription machinery.","authors":"Kleinschmidt AM, Pederson T, Tani T, Ohshima Y","authors_abbrev":"Kleinschmidt AM et al.","pubmed_publication_date":"05 Jan 1990","pubmed_entrez_date":"1990-01-05","publication_year":"1990","canto_session_key":"40307840db8afdd1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-20 10:06:57","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-20 10:06:42","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-20"},{"uniquename":"PMID:18174443","title":"Heterochromatin and RNAi are required to establish CENP-A chromatin at centromeres.","citation":"Science 2008 Jan 04;319(5859):94-7","abstract":"Heterochromatin is defined by distinct posttranslational modifications on histones, such as methylation of histone H3 at lysine 9 (H3K9), which allows heterochromatin protein 1 (HP1)-related chromodomain proteins to bind. Heterochromatin is frequently found near CENP-A chromatin, which is the key determinant of kinetochore assembly. We have discovered that the RNA interference (RNAi)-directed heterochromatin flanking the central kinetochore domain at fission yeast centromeres is required to promote CENP-A(Cnp1) and kinetochore assembly over the central domain. The H3K9 methyltransferase Clr4 (Suv39); the ribonuclease Dicer, which cleaves heterochromatic double-stranded RNA to small interfering RNA (siRNA); Chp1, a component of the RNAi effector complex (RNA-induced initiation of transcriptional gene silencing; RITS); and Swi6 (HP1) are required to establish CENP-A(Cnp1) chromatin on naïve templates. Once assembled, CENP-A(Cnp1) chromatin is propagated by epigenetic means in the absence of heterochromatin. Thus, another, potentially conserved, role for centromeric RNAi-directed heterochromatin has been identified.","doi":"10.1126/science.1150944","authors":"Folco HD, Pidoux AL, Urano T, Allshire RC","authors_abbrev":"Folco HD et al.","pubmed_publication_date":"04 Jan 2008","pubmed_entrez_date":"2008-01-05","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18697832","title":"Btn1 affects cytokinesis and cell-wall deposition by independent mechanisms, one of which is linked to dysregulation of vacuole pH.","citation":"J Cell Sci 2008 Sep 01;121(Pt 17):2860-70","abstract":"btn1, the Schizosaccharomyces pombe orthologue of the human Batten-disease gene CLN3, is involved in vacuole pH homeostasis. We show that loss of btn1 also results in a defective cell wall marked by sensitivity to zymolyase, a beta-glucanase. The defect can be rescued by expression of Btn1p or CLN3, and the extent of the defect correlates with disease severity. The vacuole and cell-wall defects are linked by a common pH-dependent mechanism, because they are suppressed by growth in acidic pH and a similar glucan defect is also apparent in the V-type H(+) ATPase (v-ATPase) mutants vma1Delta and vma3Delta. Significantly, Btn1p acts as a multicopy suppressor of the cell-wall and other vacuole-related defects of these v-ATPase-null cells. In addition, Btn1p is required in a second, pH-independent, process that affects sites of polarised growth and of cell-wall deposition, particularly at the septum, causing cytokinesis problems under normal growth conditions and eventual cell lysis at 37 degrees C. Thus, Btn1p impacts two independent processes, which suggests that Batten disease is more than a pH-related lysosome disorder.","doi":"10.1242/jcs.030122","authors":"Codlin S, Haines RL, Burden JJ, Mole SE","authors_abbrev":"Codlin S et al.","pubmed_publication_date":"01 Sep 2008","pubmed_entrez_date":"2008-08-14","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19570908","title":"Regulation of fission yeast myosin-II function and contractile ring dynamics by regulatory light-chain and heavy-chain phosphorylation.","citation":"Mol Biol Cell 2009 Sep;20(17):3941-52","abstract":"We investigated the role of regulatory light-chain (Rlc1p) and heavy-chain phosphorylation in controlling fission yeast myosin-II (Myo2p) motor activity and function during cytokinesis. Phosphorylation of Rlc1p leads to a fourfold increase in Myo2p's in vitro motility rate, which ensures effective contractile ring constriction and function. Surprisingly, unlike with smooth muscle and nonmuscle myosin-II, RLC phosphorylation does not influence the actin-activated ATPase activity of Myo2p. A truncated form of Rlc1p lacking its extended N-terminal regulatory region (including phosphorylation sites) supported maximal Myo2p in vitro motility rates and normal contractile ring function. Thus, the unphosphorylated N-terminal extension of Rlc1p can uncouple the ATPase and motility activities of Myo2p. We confirmed the identity of one out of two putative heavy-chain phosphorylation sites previously reported to control Myo2p function and cytokinesis. Although in vitro studies indicated that phosphorylation at Ser-1444 is not needed for Myo2p motor activity, phosphorylation at this site promotes the initiation of contractile ring constriction.","authors":"Sladewski TE, Previs MJ, Lord M","authors_abbrev":"Sladewski TE et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-07-03","publication_year":"2009","canto_session_key":"15a1a89e5c2409e9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-30 11:40:39","canto_approved_date":"2025-05-27 14:28:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-30 11:39:21","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":68,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.05c","SPCC645.05c","SPAC926.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-01-30"},{"uniquename":"PMID:9585505","title":"Regulation of the fission yeast transcription factor Pap1 by oxidative stress: requirement for the nuclear export factor Crm1 (Exportin) and the stress-activated MAP kinase Sty1/Spc1.","citation":"Genes Dev 1998 May 15;12(10):1453-63","abstract":"The fission yeast Sty1 stress-activated MAP kinase is crucial for the cellular response to a variety of stress conditions. Accordingly, sty1- cells are defective in their response to nutrient limitation, lose viability in stationary phase, and are hypersensitive to osmotic stress, oxidative stress, and UV treatment. Some of these phenotypes are caused by Sty1-dependent regulation of the Atf1 transcription factor, which controls both meiosis-specific and osmotic stress-responsive genes. However, in this report we demonstrate that the cellular response to oxidative stress and to treatment with a variety of cytotoxic agents is the result of Sty1 regulation of the Pap1 transcription factor, a bZip protein with structural and DNA binding similarities to the mammalian c-Jun protein. We show that both Sty1 and Pap1 are required for the expression of a number of genes involved in the oxidative stress response and for the expression of two genes, hba2+/bfr1+ and pmd1+, which encode energy-dependent transport proteins involved in multidrug resistance. Furthermore, we demonstrate that Pap1 is regulated by stress-dependent changes in subcellular localization. On imposition of oxidative stress, the Pap1 protein relocalizes from the cytoplasm to the nucleus in a process that is dependent on the Sty1 kinase. This relocalization is the result of regulated protein export, rather than import, and involves the Crm1 (exportin) nuclear export factor and the dcd1+/pim1+ gene that encodes an Ran nucleotide exchange factor.","authors":"Toone WM, Kuge S, Samuels M, Morgan BA, Toda T, Jones N","authors_abbrev":"Toone WM et al.","pubmed_publication_date":"15 May 1998","pubmed_entrez_date":"1998-05-29","publication_year":"1998","canto_session_key":"4b657c6f7edf1a4b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-22 10:31:44","canto_approved_date":"2023-03-15 20:01:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-12 16:27:18","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":59,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3F6.03","SPAC1805.17","SPCC18B5.01c","SPAC1783.07c","SPBC557.03c","SPCC757.07c","SPBC29B5.01","SPAC3C7.14c","SPCC663.03","SPBC409.07c","SPAC24B11.06c","SPBC12D12.07c"],"gene_count":12,"ltp_gene_count":6,"approved_date":"2017-11-22"},{"uniquename":"PMID:11102508","title":"A conserved interaction between Moe1 and Mal3 is important for proper spindle formation in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2000 Dec;11(12):4067-77","abstract":"Moe1 is a conserved fission yeast protein that negatively affects microtubule stability/assembly. We conducted a two-hybrid screen to search for Moe1-binding proteins and isolated Mal3, a homologue of human EB1. We show that Moe1 and Mal3 expressed in bacteria form a complex and that Moe1 and Mal3 expressed in fission yeast cosediment with microtubules. Deletion of either moe1 or mal3 does not result in lethality; however, deletion of both moe1 and mal3 leads to cell death in the cold. The resulting cells appear to die of chromosome missegregation, which correlates with the presence of abnormal spindles. We investigated the cause for the formation of monopolar spindles and found that only one of the two spindle pole bodies (SPBs) contains gamma-tubulin, although both SPBs appear to be equal in size and properly inserted in the nuclear membrane. Moreover, the moe1 mal3 double null mutant in the cold contains abnormally short and abundant interphase microtubule bundles. These data suggest that Moe1 and Mal3 play a role in maintaining proper microtubule dynamics/integrity and distribution of gamma-tubulin to the SPBs during mitosis. Finally, we show that human Moe1 and EB1 can each rescue the phenotype of the moe1 mal3 double null mutant and form a complex, suggesting that these proteins are part of a well-conserved mechanism for regulating spindle functioning.","authors":"Chen CR, Chen J, Chang EC","authors_abbrev":"Chen CR et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-12-05","publication_year":"2000","canto_session_key":"333ca30ce9c2eb22","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-11-20 13:58:03","canto_approved_date":"2023-05-03 16:15:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-15 15:47:52","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC637.07","SPAC15E1.07c","SPAC18G6.15"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2018-11-20"},{"uniquename":"PMID:16428807","title":"Hip3 interacts with the HIRA proteins Hip1 and Slm9 and is required for transcriptional silencing and accurate chromosome segregation.","citation":"J Biol Chem 2006 Mar 31;281(13):8732-9","abstract":"The fission yeast HIRA proteins Hip1 and Slm9 are members of an evolutionarily conserved family of histone chaperones that are implicated in nucleosome assembly. Here we have used single-step affinity purification and mass spectrometry to identify factors that interact with both Hip1 and Slm9. This analysis identified Hip3, a previously uncharacterized 187-kDa protein, with similarity to S. cerevisiae Hir3. Consistent with this, cells disrupted for hip3+ exhibit a range of growth defects that are similar to those associated with loss of Hip1 and Slm9. These include temperature sensitivity, a cell cycle delay, and synthetic lethality with cdc25-22. Furthermore, genetic analysis also indicates that disruption of hip3+ is epistatic with mutation of hip1+ and slm9+. Mutation of hip3+ alleviates transcriptional silencing at several heterochromatic loci, including in the outer (otr) centromeric repeats, indicating that Hip3 is required for the integrity of pericentric heterochromatin. As a result, loss of Hip3 function leads to high levels of minichromosome loss and an increased frequency of lagging chromosomes during mitosis. Importantly, the function of Hip1, Slm9, and Hip3 is not restricted to constitutive heterochromatic loci, since these proteins also repress the expression of a number of genes, including the Tf2 retrotransposons.","authors":"Greenall A, Williams ES, Martin KA, Palmer JM, Gray J, Liu C, Whitehall SK","authors_abbrev":"Greenall A et al.","pubmed_publication_date":"31 Mar 2006","pubmed_entrez_date":"2006-01-24","publication_year":"2006","canto_session_key":"68c59bdaf276c094","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-18 11:19:23","canto_approved_date":"2020-03-11 16:00:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-18 11:19:15","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":79,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.04c","SPBC428.08c","SPCC11E10.08","SPAC24H6.05","SPBC15D4.03","SPBC31F10.13c","SPAC18G6.02c","SPBC3E7.02c","SPBC31F10.14c","SPAC664.01c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2016-04-18"},{"uniquename":"PMID:24385927","title":"The PAF complex and Prf1/Rtf1 delineate distinct Cdk9-dependent pathways regulating transcription elongation in fission yeast.","citation":"PLoS Genet 2013;9(12):e1004029","abstract":"Cyclin-dependent kinase 9 (Cdk9) promotes elongation by RNA polymerase II (RNAPII), mRNA processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved RNAPII elongation factor Spt5 and RNAPII itself, but how these different modifications mediate Cdk9 functions is not known. Here we describe two Cdk9-dependent pathways in the fission yeast Schizosaccharomyces pombe that involve distinct targets and elicit distinct biological outcomes. Phosphorylation of Spt5 by Cdk9 creates a direct binding site for Prf1/Rtf1, a transcription regulator with functional and physical links to the Polymerase Associated Factor (PAF) complex. PAF association with chromatin is also dependent on Cdk9 but involves alternate phosphoacceptor targets. Prf1 and PAF are biochemically separate in cell extracts, and genetic analyses show that Prf1 and PAF are functionally distinct and exert opposing effects on the RNAPII elongation complex. We propose that this opposition constitutes a Cdk9 auto-regulatory mechanism, such that a positive effect on elongation, driven by the PAF pathway, is kept in check by a negative effect of Prf1/Rtf1 and downstream mono-ubiquitylation of histone H2B. Thus, optimal RNAPII elongation may require balanced action of functionally distinct Cdk9 pathways.","doi":"10.1371/journal.pgen.1004029","authors":"Mbogning J, Nagy S, Pagé V, Schwer B, Shuman S, Fisher RP, Tanny JC","authors_abbrev":"Mbogning J et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2014-01-04","publication_year":"2013","canto_session_key":"12051090ffdf63e7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-01-06 16:31:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.07","SPAC3G6.11","SPBC651.09c","SPAC1039.05c","SPAC15A10.03c","SPCC622.09","SPAC31G5.19","SPBC13E7.08c","SPAC2F3.11","SPBC32H8.10","SPBC359.05","SPAC32A11.02c","SPAC23G3.02c","SPAC23C4.19","SPAC2G11.10c","SPAC27D7.14c","SPBC2G2.07c","SPBC17G9.02c","SPAC140.01","SPAC664.03","SPAP8A3.05","SPCC970.10c"],"gene_count":22,"ltp_gene_count":9},{"uniquename":"EMBL:SPD265","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1884996","title":"The proteolytic system of the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 1991 Jun 15;65(2):215-20","abstract":"Proteinase and peptidase activities of the fission yeast Schizosaccharomyces pombe were investigated. Several intracellular proteolytic enzymes were found: two endoproteinases, one carboxypeptidase, one aminopeptidase and one dipeptidyl-aminopeptidase. In addition, proteinase inhibitors were detected. In fresh crude extracts an activation procedure is needed to measure maximal activities of endoproteinases and carboxypeptidase, whose level is markedly dependent on growth medium composition and on growth phase, while aminopeptidase and dipeptidyl-aminopeptidase activities are very little, if at all, regulated by the carbon source.","authors":"Suárez-Rendueles P, Villa L, Arbesú MJ, Escudero B","authors_abbrev":"Suárez-Rendueles P et al.","pubmed_publication_date":"15 Jun 1991","pubmed_entrez_date":"1991-06-15","publication_year":"1991","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16859532","title":"What makes species unique? The contribution of proteins with obscure features.","citation":"Genome Biol 2006;7(7):R57","abstract":"Proteins with obscure features (POFs), which lack currently defined motifs or domains, represent between 18% and 38% of a typical eukaryotic proteome. To evaluate the contribution of this class of proteins to the diversity of eukaryotes, we performed a comparative analysis of the predicted proteomes derived from 10 different sequenced genomes, including budding and fission yeast, worm, fly, mosquito, Arabidopsis, rice, mouse, rat, and human.\nOnly 1,650 protein groups were found to be conserved among these proteomes (BLAST E-value threshold of 10(-6)). Of these, only three were designated as POFs. Surprisingly, we found that, on average, 60% of the POFs identified in these 10 proteomes (44,236 in total) were species specific. In contrast, only 7.5% of the proteins with defined features (PDFs) were species specific (17,554 in total). As a group, POFs appear similar to PDFs in their relative contribution to biological functions, as indicated by their expression, participation in protein-protein interactions and association with mutant phenotypes. However, POF have more predicted disordered structure than PDFs, implying that they may exhibit preferential involvement in species-specific regulatory and signaling networks.\nBecause the majority of eukaryotic POFs are not well conserved, and by definition do not have defined domains or motifs upon which to formulate a functional working hypothesis, understanding their biochemical and biological functions will require species-specific investigations.","authors":"Gollery M, Harper J, Cushman J, Mittler T, Girke T, Zhu JK, Bailey-Serres J, Mittler R","authors_abbrev":"Gollery M et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-07-25","publication_year":"2006","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20404563","title":"High-throughput knockout screen in Schizosaccharomyces pombe identifies a novel gene required for efficient homolog disjunction during meiosis I.","citation":"Cell Cycle 2010 May;9(9):1802-8","abstract":"Meiosis is the process which produces haploid gametes from diploid precursor cells. This reduction of chromosome number is achieved by two successive divisions. Whereas homologs segregate during meiosis I, sister chromatids segregate during meiosis II. To identify novel proteins required for proper segregation of chromosomes during meiosis, we applied a high-throughput knockout technique to delete 87 S. pombe genes whose expression is upregulated during meiosis and analyzed the mutant phenotypes. Using this approach, we identified a new protein, Dil1, which is required to prevent meiosis I homolog non-disjunction. We show that Dil1 acts in the dynein pathway to promote oscillatory nuclear movement during meiosis.","authors":"Rumpf C, Cipak L, Novatchkova M, Li Z, Polakova S, Dudas A, Kovacikova I, Miadokova E, Ammerer G, Gregan J","authors_abbrev":"Rumpf C et al.","pubmed_publication_date":"May 2010","pubmed_entrez_date":"2010-04-21","publication_year":"2010","canto_session_key":"577bf3d48e3ab2d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-09 16:10:26","canto_approved_date":"2022-02-07 16:37:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-02 15:16:29","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.08","SPAC25H1.03","SPAC29A4.11","SPBC83.08","SPAC105.02c","SPAC18G6.10","SPBC4C3.06","SPAC29E6.04","SPAC29B12.07","SPAP27G11.03","SPAC23C11.12","SPBC3E7.13c","SPAC328.02","SPAC17A5.11","SPCC4E9.01c","SPAC13F5.06c","SPCC1795.08c","SPAC20H4.01","SPAC3A11.10c","SPBC31F10.10c","SPBC29A10.02","SPAC10F6.11c","SPAC458.04c","SPBC2F12.05c","SPBC19C7.04c","SPBC119.16c","SPCC1739.10"],"gene_count":27,"ltp_gene_count":22,"approved_date":"2018-03-09"},{"uniquename":"PMID:9378412","title":"Characterization of glucose transport in Schizosaccharomyces pombe.","citation":"Folia Microbiol (Praha) 1997;42(3):225-7","abstract":"","authors":"Heiland S, Lichtenberg-Fraté H, Näschen T, Höfer M","authors_abbrev":"Heiland S et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34423281","title":"Two plasmid modules for introducing the auxin-inducible degron into the fission yeast  Schizosaccharomyces pombe  by PCR-based gene targeting.","citation":"MicroPubl Biol 2021;2021","abstract":"Targeted protein degradation is a powerful approach to study and inhibit protein function  in vivo . Introduction of the auxin-inducible degron (AID) system to the fission yeast  Schizosaccharomyces pombe  was previously reported, but, to the best of our knowledge, no plasmid for constructing AID-tagged fission yeast strains has been described so far. Here, we describe two plasmids that facilitate the introduction of the mini auxin-inducible degron (mAID) tag with a FLAG epitope or GFP by the conventional PCR-based gene targeting method. Our experimental verification indicated that PCR-based mAID tagging is straightforward and that the auxin-degron system is useful for studying essential proteins in  S. pombe .","doi":"10.17912/micropub.biology.000442","authors":"Song X, Xu R, Sugiyama T","authors_abbrev":"Song X et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-08-23","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-08-25 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28784724","title":"Multi-BRCT Domain Protein Brc1 Links Rhp18/Rad18 and γH2A To Maintain Genome Stability during S Phase.","citation":"Mol Cell Biol 2017 Nov 15;37(22)","abstract":"DNA replication involves the inherent risk of genome instability, since replisomes invariably encounter DNA lesions or other structures that stall or collapse replication forks during the S phase. In the fission yeast  Schizosaccharomyces pombe , the multi-BRCT domain protein Brc1, which is related to budding yeast Rtt107 and mammalian PTIP, plays an important role in maintaining genome integrity and cell viability when cells experience replication stress. The C-terminal pair of BRCT domains in Brc1 were previously shown to bind phosphohistone H2A (γH2A) formed by Rad3/ATR checkpoint kinase at DNA lesions; however, the putative scaffold interactions involving the N-terminal BRCT domains 1 to 4 of Brc1 have remained obscure. Here, we show that these domains bind Rhp18/Rad18, which is an E3 ubiquitin protein ligase that has crucial functions in postreplication repair. A missense allele in BRCT domain 4 of Brc1 disrupts binding to Rhp18 and causes sensitivity to replication stress. Brc1 binding to Rhp18 and γH2A are required for the Brc1 overexpression suppression of  smc6-74 , a mutation that impairs the Smc5/6 structural maintenance of chromosomes complex required for chromosome integrity and repair of collapsed replication forks. From these findings, we propose that Brc1 provides scaffolding functions linking γH2A, Rhp18, and Smc5/6 complex at damaged replication forks.","doi":"10.1128/MCB.00260-17","authors":"Reubens MC, Rozenzhak S, Russell P","authors_abbrev":"Reubens MC et al.","pubmed_publication_date":"15 Nov 2017","pubmed_entrez_date":"2017-08-09","publication_year":"2017","canto_session_key":"64e109edfc46b3d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-08-10 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.05c","SPCC622.08c","SPCC5E4.06","SPBC1734.06","SPAC19G12.06c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:19454013","title":"Conserved features of cohesin binding along fission yeast chromosomes.","citation":"Genome Biol 2009;10(5):R52","abstract":"Cohesin holds sister chromatids together to enable their accurate segregation in mitosis. How, and where, cohesin binds to chromosomes are still poorly understood, and recent genome-wide surveys have revealed an apparent disparity between its chromosomal association patterns in different organisms.\nHere, we present the high-resolution analysis of cohesin localization along fission yeast chromosomes. This reveals that several determinants, thought specific for different organisms, come together to shape the overall distribution. Cohesin is detected at chromosomal loading sites, characterized by the cohesin loader Mis4/Ssl3, in regions of strong transcriptional activity. Cohesin also responds to transcription by downstream translocation and accumulation at convergent transcriptional terminators surrounding the loading sites. As cells enter mitosis, a fraction of cohesin leaves chromosomes in a cleavage-independent reaction, while a substantial pool of cohesin dissociates when it is cleaved at anaphase onset. We furthermore observe that centromeric cohesin spreads out onto chromosome arms during mitosis, dependent on Aurora B kinase activity, emphasizing the plasticity of cohesin behavior.\nOur findings suggest that features that were thought to differentiate cohesin between organisms collectively define the overall behavior of fission yeast cohesin. Apparent differences between organisms might reflect an emphasis on different aspects, rather than different principles, of cohesin action.","doi":"10.1186/gb-2009-10-5-r52","authors":"Schmidt CK, Brookes N, Uhlmann F","authors_abbrev":"Schmidt CK et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-05-21","publication_year":"2009","canto_session_key":"2a9bce7ccbdd5c56","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasu Kakui","canto_first_approved_date":"2016-05-05 13:28:44","canto_approved_date":"2025-09-04 09:08:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-12 15:51:19","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Yasu Kakui","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPCC306.03c","SPAC1142.08","SPCC338.17c","SPAC1687.18c","SPBC26H8.07c","SPAC664.01c","SPBC21H7.05","SPBC336.07","SPAC31A2.05c","SPCC320.13c","SPBP4H10.06c"],"gene_count":12,"ltp_gene_count":2,"approved_date":"2016-05-05"},{"uniquename":"PMID:4367962","title":"Characterization of a mutant of Schizosaccharomyces pombe lacking cytochrome b-566.","citation":"Biochim Biophys Acta 1974 Mar 26;333(3):446-59","abstract":"","authors":"Bandlow W, Wolf K, Kaudewitz F, Slater EC","authors_abbrev":"Bandlow W et al.","pubmed_publication_date":"26 Mar 1974","pubmed_entrez_date":"1974-03-26","publication_year":"1974","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8834798","title":"Isolation and characterization of fission yeast mutants defective in the assembly and placement of the contractile actin ring.","citation":"J Cell Sci 1996 Jan;109 ( Pt 1):131-42","abstract":"Fission yeast cells divide by medial cleavage using an actin-based contractile ring. We have conducted a genetic screen for temperature-sensitive mutants defective in the assembly and placement of this actin ring. Six genes necessary for actin ring formation and one gene necessary for placement of the actin ring have now been identified. The genes can be further organized into different phenotypic groups, suggesting that the gene products may have different functions in actin ring formation. Mutants of cdc3 and cdc8, which encode profilin and tropomyosin respectively, display disorganized actin patches in all cells. cdc12 and cdc15 mutants display disorganized actin patches during mitosis, but normal interphase actin patterns. cdc4 and rng2 mutants display disorganized actin cables during mitosis, but normal interphase actin patterns. In mid1 mutants, the actin ring and septum are positioned at random locations and angles on the cell surface, although the nucleus is positioned normally, indicating that the mid1 gene product is required to couple the division site to the position of the nucleus. mid1 mutant cells may reveal a new cell cycle checkpoint in telophase that coordinates cell division and the proper distribution of nuclei. The actin ring forms medially in a beta-tubulin mutant, showing that actin ring formation and placement are not dependent on the mitotic spindle.","authors":"Chang F, Woollard A, Nurse P","authors_abbrev":"Chang F et al.","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"482d360415391124","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-09-14 16:54:26","canto_approved_date":"2026-01-29 17:39:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-07 18:02:59","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.05c","SPAC4A8.15c","SPAC4F8.13c","SPAP8A3.08","SPAC1F5.04c","SPCC4B3.15","SPBC26H8.07c","SPAC27F1.02c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-09-14"},{"uniquename":"PMID:17248858","title":"Further to the Number of Chromosomes in SCHIZOSACCHAROMYCES POMBE.","citation":"Genetics 1978 Sep;90(1):207","abstract":"","authors":"Robinow CF","authors_abbrev":"Robinow CF","pubmed_publication_date":"Sep 1978","pubmed_entrez_date":"1978-09-01","publication_year":"1978","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19366728","title":"Genetic control of cellular quiescence in S. pombe.","citation":"J Cell Sci 2009 May 01;122(Pt 9):1418-29","abstract":"Transition from proliferation to quiescence brings about extensive changes in cellular behavior and structure. However, the genes that are crucial for establishing and/or maintaining quiescence are largely unknown. The fission yeast Schizosaccharomyces pombe is an excellent model in which to study this problem, because it becomes quiescent under nitrogen starvation. Here, we characterize 610 temperature-sensitive mutants, and identify 33 genes that are required for entry into and maintenance of quiescence. These genes cover a broad range of cellular functions in the cytoplasm, membrane and nucleus. They encode proteins for stress-responsive and cell-cycle kinase signaling pathways, for actin-bound and osmo-controlling endosome formation, for RNA transcription, splicing and ribosome biogenesis, for chromatin silencing, for biosynthesis of lipids and ATP, for cell-wall and membrane morphogenesis, and for protein trafficking and vesicle fusion. We specifically highlight Fcp1, a CTD phosphatase of RNA polymerase II, which differentially affects the transcription of genes that are involved in quiescence and proliferation. We propose that the transcriptional role of Fcp1 is central in differentiating quiescence from proliferation.","doi":"10.1242/jcs.046466","authors":"Sajiki K, Hatanaka M, Nakamura T, Takeda K, Shimanuki M, Yoshida T, Hanyu Y, Hayashi T, Nakaseko Y, Yanagida M","authors_abbrev":"Sajiki K et al.","pubmed_publication_date":"01 May 2009","pubmed_entrez_date":"2009-04-16","publication_year":"2009","canto_session_key":"8c6ccb0ae9834279","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-07-12 05:34:11","canto_approved_date":"2023-05-23 15:20:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-12 05:04:44","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":87,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC947.02","SPAC23H4.14","SPAC19B12.05c","SPAC4H3.10c","SPAC4F10.10c","SPAC20G8.09c","SPBC1703.10","SPAC31A2.05c","SPBC19C2.14","SPAC6F12.13c","SPBC11B10.09","SPAC823.12","SPCC777.14","SPBC409.07c","SPCC1672.10","SPAC167.02","SPBC30D10.17c","SPAC959.02","SPAC4F10.15c","SPBC582.03","SPAC26A3.12c","SPAC4F8.14c","SPAC6F6.15","SPAC688.11","SPAPB2B4.03","SPBC19G7.07c","SPCC1442.12","SPBC32F12.09","SPCC297.03","SPAC10F6.03c","SPBC1289.07c","SPAC24B11.06c","SPBC25H2.06c","SPAC1834.01"],"gene_count":34,"ltp_gene_count":33,"approved_date":"2019-07-12"},{"uniquename":"PMID:14617822","title":"A comparative analysis of an orthologous proteomic environment in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Mol Cell Proteomics 2004 Feb;3(2):125-32","abstract":"The sequential application of protein tagging, affinity purification, and mass spectrometry enables highly accurate charting of proteomic environments by the characterization of stable protein assemblies and the identification of subunits that are shared between two or more protein complexes, termed here \"proteomic hyperlinks.\" We have charted the proteomic environments surrounding the histone methyltransferase, Set1, in both yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Although the composition of these nonessential Set1 complexes is remarkably conserved, they differ with respect to their hyperlinks to their proteomic environments. We speculate that conservation of the core components of protein assemblies and variability of hyperlinks represents a general principle in the molecular organization of eukaryotic proteomes.","authors":"Roguev A, Shevchenko A, Schaft D, Thomas H, Stewart AF, Shevchenko A","authors_abbrev":"Roguev A et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2003-11-18","publication_year":"2004","canto_session_key":"3fb770bb21373aad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-04-25 11:31:02","canto_approved_date":"2023-03-16 16:48:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-25 11:30:51","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP19A11.06","SPBC3B9.11c","SPBC13G1.08c","SPCC594.05c","SPBC83.07","SPCC306.04c","SPCC74.02c","SPBC1709.15c","SPCC18.11c","SPAC17G8.09","SPAC12G12.14c","SPAC22G7.10","SPAC3H1.12c","SPAC3G9.04","SPAC1071.01c","SPBC1709.08","SPAC227.08c","SPAC23H3.05c","SPBC18H10.06c","SPAC824.04","SPBC354.03","SPBC776.02c","SPAC17G6.16c"],"gene_count":23,"ltp_gene_count":23,"approved_date":"2018-04-25"},{"uniquename":"PMID:30898439","title":"Inheritance of a Phenotypically Neutral Epimutation Evokes Gene Silencing in Later Generations.","citation":"Mol Cell 2019 May 02;74(3):534-541.e4","abstract":"Small RNAs trigger the formation of epialleles that are silenced across generations. Consequently, RNA-directed epimutagenesis is associated with persistent gene repression. Here, we demonstrate that small interfering RNA-induced epimutations in fission yeast are still inherited even when the silenced gene is reactivated, and descendants can reinstate the silencing phenotype that only occurred in their ancestors. This process is mediated by the deposition of a phenotypically neutral molecular mark composed of tri-methylated histone H3 lysine 9 (H3K9me3). Its stable propagation is coupled to RNAi and requires maximal binding affinity of the Clr4/Suvar39 chromodomain to H3K9me3. In wild-type cells, this mark has no visible impact on transcription but causes gene silencing if RNA polymerase-associated factor 1 complex (Paf1C) activity is impaired. In sum, our results reveal a distinct form of epigenetic memory in which cells acquire heritable, transcriptionally active epialleles that confer gene silencing upon modulation of Paf1C.","doi":"10.1016/j.molcel.2019.02.009","authors":"Duempelmann L, Mohn F, Shimada Y, Oberti D, Andriollo A, Lochs S, Bühler M","authors_abbrev":"Duempelmann L et al.","pubmed_publication_date":"02 May 2019","pubmed_entrez_date":"2019-03-23","publication_year":"2019","canto_session_key":"ab5f5e368e5e68d7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-03-24 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10655214","title":"Functions of fission yeast orp2 in DNA replication and checkpoint control.","citation":"Genetics 2000 Feb;154(2):599-607","abstract":"orp2 is an essential gene of the fission yeast Schizosaccharomyces pombe with 22% identity to budding yeast ORC2. We isolated temperature-sensitive alleles of orp2 using a novel plasmid shuffle based on selection against thymidine kinase. Cells bearing the temperature-sensitive allele orp2-2 fail to complete DNA replication at a restrictive temperature and undergo cell cycle arrest. Cell cycle arrest depends on the checkpoint genes rad1 and rad3. Even when checkpoint functions are wild type, the orp2-2 mutation causes high rates of chromosome and plasmid loss. These phenotypes support the idea that Orp2 is a replication initiation factor. Selective spore germination allowed analysis of orp2 deletion mutants. These experiments showed that in the absence of orp2 function, cells proceed into mitosis despite a lack of DNA replication. This suggests either that the Orp2 protein is a part of the checkpoint machinery or more likely that DNA replication initiation is required to induce the replication checkpoint signal.","authors":"Kiely J, Haase SB, Russell P, Leatherwood J","authors_abbrev":"Kiely J et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-02-03","publication_year":"2000","canto_session_key":"6e16dd2d976beabb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-06-15 14:44:18","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-01 15:43:17","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPBC685.09","SPBC216.05"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-02-01"},{"uniquename":"PMID:39643336","title":"Metagenomic insights into quorum sensing-associated microbial profiling and its correlations with flavor compounds of Maotai-flavor liquor: A case study of stacking fermented grains.","citation":"Food Res Int 2024 Dec;198:115324","abstract":"Stacking fermentation is typical process of Maotai-flavor Baijiu and microbial composition determine content of flavors. To date, the knowledge on the driving force of microbial composition was as yet unknown. Since quorum sensing molecule (QSM) plays an important role in modifying microbial interactions. Therefore, the objectives of the present study were: (1) to describe the microbial profile associated with QSM in stacking grains using metagenomics; (2) to elucidate how QSM shapes microbial interactions and accordingly regulates flavor synthesis. Results indicated that bacterial QSM including AI-2, DSF, and AHL as well as fungal QSM aromatic alcohols and farnesol were prevalent in the stacking fermented grains. Thereinto, AI-2 might be an important driving force of microbial composition due to its highest abundance. AI-2 in Limosilactobacillus fermentum, Pediococcus pentosaceus, and Weissella cibaria perhaps modified microbial interactions together with fungal QSM in Schizosaccharomyces pombe and Pichia membranifaciens. The role of AI-2 was much higher than that of fungal QSM. Furthermore, QSM indirectly influenced the synthesis of important flavors such as ethyl lactate, phenylethanol, and ethyl phenylacetate through the dynamic of microbial composition. Together, this current study for the first time explored the effects of QSM on microbial composition and flavor synthesis in the Baijiu field.","doi":"10.1016/j.foodres.2024.115324","authors":"Li T, Cao W, Li D, Wei C, Yan Y, Zeng X","authors_abbrev":"Li T et al.","pubmed_publication_date":"Dec 2024","pubmed_entrez_date":"2024-12-06","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-12-08 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3010051","title":"The fission yeast cell cycle control gene cdc2: isolation of a sequence suc1 that suppresses cdc2 mutant function.","citation":"Mol Gen Genet 1986 Feb;202(2):291-3","abstract":"A DNA fragment called suc1 has been found to rescue cells mutated in the cell cycle control gene cdc2 of the fission yeast Schizosaccharomyces pombe. The suppressing activity of suc1 is observed when it is present on a multicopy number plasmid. The gene does not hybridize to cdc2 and maps elsewhere in the genome. Its effect is cdc2 allele specific suggesting that it interacts directly with the cdc2 gene function.","authors":"Hayles J, Beach D, Durkacz B, Nurse P","authors_abbrev":"Hayles J et al.","pubmed_publication_date":"Feb 1986","pubmed_entrez_date":"1986-02-01","publication_year":"1986","canto_session_key":"8c1ae1650e2ee012","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-30 14:33:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-30 14:31:46","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1734.14c","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-30"},{"uniquename":"PMID:27259461","title":"TERRA Incognita at chromosome ends.","citation":"EMBO Rep 2016 Jul;17(7):933-4","abstract":"Telomeres are transcribed in long noncoding RNA named TERRA. Although TERRA functions have been extensively investigated, the role of TERRA in telomerase recruitment and regulation is still elusive. In this issue of EMBO  Reports , Moravec  et al  report in  Schizosaccharomyces pombe  that telomere shortening induces the expression of TERRA 1. They show that polyadenylated TERRA molecules specifically associate with the telomerase catalytic subunit and stimulate telomerase‐mediated elongation of the telomere from which the TERRA molecules originate. Strikingly, their results indicate that shaping the 3′ end of telomere transcripts controls telomerase activity.","doi":"10.15252/embr.201642583","authors":"Coulon S, Géli V","authors_abbrev":"Coulon S et al.","pubmed_publication_date":"Jul 2016","pubmed_entrez_date":"2016-06-05","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-11-23 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19643199","title":"The dynamin-related protein Vps1 regulates vacuole fission, fusion and tubulation in the fission yeast, Schizosaccharomyces pombe.","citation":"Fungal Genet Biol 2009 Dec;46(12):927-35","abstract":"Fission yeast cells lacking the dynamin-related protein (DRP) Vps1 had smaller vacuoles with reduced capacity for both fusion and fission in response to hypotonic and hypertonic conditions respectively. vps1Delta cells showed normal vacuolar protein sorting, actin organisation and endocytosis. Over-expression of vps1 transformed vacuoles from spherical to tubular. Tubule formation was enhanced in fission conditions and required the Rab protein Ypt7. Vacuole tubulation by Vps1 was more extensive in the absence of a second DRP, Dnm1. Both dnm1Delta and the double mutant vps1Delta dnm1Delta showed vacuole fission defects similar to that of vps1Delta. Over-expression of vps1 in dnm1Delta, or of dnm1 in vps1Delta failed to rescue this phenotype. Over-expression of dnm1 in wild-type cells, on the other hand, induced vacuole fission. Our results are consistent with a model of vacuole fission in which Vps1 creates a tubule of an appropriate diameter for subsequent scission by Dnm1.","doi":"10.1016/j.fgb.2009.07.008","authors":"Röthlisberger S, Jourdain I, Johnson C, Takegawa K, Hyams JS","authors_abbrev":"Röthlisberger S et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-08-01","publication_year":"2009","canto_session_key":"9bba111aad473ae7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-08 11:52:18","canto_approved_date":"2021-01-08 11:52:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-30 19:48:22","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.08","SPAC767.01c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-01-08"},{"uniquename":"PMID:18243705","title":"Ustilago maydis, a new fungal model system for cell biology.","citation":"Trends Cell Biol 2008 Feb;18(2):61-7","abstract":"The use of fungal model systems, such as Saccharomyces cerevisisae and Schizosaccharomyces pombe, has contributed enormously to our understanding of essential cellular processes in animals. Here, we introduce the corn smut fungus Ustilago maydis as a new model organism for studying cell biological processes. Genome-wide analysis demonstrates that U. maydis is more closely related to humans than to budding yeast, and numerous proteins are shared only by U. maydis and Homo sapiens. Growing evidence suggests that basic principles of long-distance transport, mitosis and motor-based microtubule organization are conserved between U. maydis and humans. The fungus U. maydis, therefore, offers a unique system for the study of certain mammalian processes.","doi":"10.1016/j.tcb.2007.11.008","authors":"Steinberg G, Perez-Martin J","authors_abbrev":"Steinberg G et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2008-02-05","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD192","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007944","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000119","title":"Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs","abstract":"The Alliance of Genome Resources (https://www.alliancegenome.org/) has procedures in place to establish orthology relationships","authors":"The Gene Ontology Consortium","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9427748","title":"pmp1+, a suppressor of calcineurin deficiency, encodes a novel MAP kinase phosphatase in fission yeast.","citation":"EMBO J 1998 Jan 02;17(1):140-8","abstract":"Calcineurin is a highly conserved and ubiquitously expressed Ca2+- and calmodulin-dependent protein phosphatase. The in vivo role of calcineurin, however, is not fully understood. Here, we show that disruption of the calcineurin gene (ppb1(+)) in fission yeast results in a drastic chloride ion (Cl-)-sensitive growth defect and that a high copy number of a novel gene pmp1(+) suppresses this defect. pmp1(+) encodes a phosphatase, most closely related to mitogen-activated protein (MAP) kinase phosphatases of the CL100/MKP-1 family. Pmp1 and calcineurin share an essential function in Cl- homeostasis, cytokinesis and cell viability. Pmp1 phosphatase dephosphorylates Pmk1, the third MAP kinase in fission yeast, in vitro and in vivo, and is bound to Pmk1 in vivo, strongly suggesting that Pmp1 negatively regulates Pmk1 MAP kinase by direct dephosphorylation. Consistently, the deletion of pmk1(+) suppresses the Cl--sensitive growth defect of ppb1 null. Thus, calcineurin and the Pmk1 MAP kinase pathway may play antagonistic functional roles in the Cl- homeostasis.","authors":"Sugiura R, Toda T, Shuntoh H, Yanagida M, Kuno T","authors_abbrev":"Sugiura R et al.","pubmed_publication_date":"02 Jan 1998","pubmed_entrez_date":"1998-02-28","publication_year":"1998","canto_session_key":"3083b0a685ce4150","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-17 15:29:10","canto_approved_date":"2020-11-18 14:39:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-15 07:36:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.01","SPAC1F3.02c","SPBP4H10.04","SPBC119.08","SPBC12D12.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-08-17"},{"uniquename":"PMID:2251111","title":"High-frequency transformation method and library transducing vectors for cloning mammalian cDNAs by trans-complementation of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1990 Nov 25;18(22):6485-9","abstract":"We describe a highly efficient alkali cation method and library transducing vectors for cloning mammalian cDNAs by trans-complementation of fission yeast Schizosaccharomyces pombe mutants. cDNA libraries constructed with the pcD or pcD2 vector are transduced into yeast by cotransfection with a linearized vector, which allows an enhanced homologous recombination between the yeast vector and the library plasmid leading to the efficient formation of concatemers containing pcD molecules. The transformation frequencies obtained by the method are 10(6) colonies per 10(8) cells transfected with 2 micrograms of library and 1 microgram of vector, 50-60% of which contain pcD molecules. The high-efficiency alkali cation method circumvents many of the shortcomings of the spheroplast method generally used for Schiz. pombe transfection. The vectors are maximized for the efficiency of library transduction and minimized for the rearrangements of pcD molecules during propagation in yeast. This system allows rapid screening of multi-million cDNA clone libraries for rare cDNAs in a routine scale of experiments. Using this system, various mammalian cDNAs that are extremely difficult, time-consuming, or unclonable to clone by other methods have been cloned.","authors":"Okazaki K, Okazaki N, Kume K, Jinno S, Tanaka K, Okayama H","authors_abbrev":"Okazaki K et al.","pubmed_publication_date":"25 Nov 1990","pubmed_entrez_date":"1990-11-25","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41848300","title":"Bip1 regulates AMPK signaling in response to endoplasmic reticulum stress.","citation":"FEBS J 2026 Mar 18;","abstract":"The accumulation of misfolded and unfolded proteins within the endoplasmic reticulum (ER) lumen induces ER stress, which in turn triggers various consequences, such as the unfolded protein response (UPR). AMP-activated protein kinase (AMPK) is also a cellular stress sensor. However, the interplay between AMPK and ER stress remains poorly understood. In this study, we report that in the fission yeast Schizosaccharomyces pombe, the deletion of erd2, a central component for the retrieval of ER-resident proteins, leads to the accumulation of the canonical ER luminal chaperone Bip1 in the cytosol. Moreover, we demonstrate that erd2 deletion increases the levels of the AMPK upstream kinase Ssp1 in a Bip1-dependent manner, thereby promoting AMPK phosphorylation. Intriguingly, although these phenotypes are not dependent on UPR, they can also be caused by ER stress. We further identify multiple E3 ubiquitin ligases that are responsible for the regulation of Ssp1 stability, and Bip1 physically interacts with and stabilises Ssp1 by inhibiting ubiquitination of Ssp1. Additionally, we elucidate that AMPK activation, mediated by the stabilised Ssp1, is required to sustain cell viability, particularly in cells lacking Erd2. Collectively, our findings demonstrate the important role of Erd2 in the maintenance of cellular homeostasis and establish a link between ER stress and AMPK signalling.","doi":"10.1111/febs.70496","authors":"Zhu M, Fu C","authors_abbrev":"Zhu M et al.","pubmed_publication_date":"18 Mar 2026","pubmed_entrez_date":"2026-03-18","publication_year":"2026","canto_session_key":"11432340dbb14fc7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-19 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22A12.15c","SPCC297.03","SPBP8B7.22"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:9619628","title":"Identification of sna41 gene, which is the suppressor of nda4 mutation and is involved in DNA replication in Schizosaccharomyces pombe.","citation":"Genes Cells 1998 Mar;3(3):157-66","abstract":"The replication licensing factor limits DNA replication to once in a cell cycle and is thought to contain MCM proteins as its component parts. Six MCM subtypes have been identified in various species. These MCM proteins are thought to bind each other to make a heteromeric complex. The Nda4 protein of Schizosaccharomyces pombe is one of the MCM proteins and is involved in DNA replication.\nThe suppressor mutant of nda4 was isolated and the mutant gene was named sna41. The sna41-912 mutant demonstrated the ts phenotype, with an elongated cell shape at the restrictive temperature. Cells with 1C DNA content accumulated 2 h after shifting up to the restrictive temperature. This result suggests that sna41 is also involved in DNA replication. The sna41 genomic clone was isolated by a complementation of the ts phenotype of the mutant strain and was sequenced. The sna41 gene encodes a protein of 638 amino acids, which has low homology with CDC45 in S. cerevisiae. The gene disruption analysis showed that sna41 gene is essential for viability.\nThe S. pombe sna41 mutation suppresses the nda4-108 mutation. Sna41 is involved in DNA replication and may play some roles in the regulation of DNA replication by the MCM proteins.","authors":"Miyake S, Yamashita S","authors_abbrev":"Miyake S et al.","pubmed_publication_date":"Mar 1998","pubmed_entrez_date":"1998-06-10","publication_year":"1998","canto_session_key":"3766cc15220df0e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-04-10 16:36:29","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-08-09 10:12:05","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPAC17D4.02","SPBC4.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-08-09"},{"uniquename":"EMBL:SPC10297","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11389855","title":"Genetic and molecular characterization of Skb15, a highly conserved inhibitor of the fission yeast PAK, Shk1.","citation":"Mol Cell 2001 May;7(5):1095-101","abstract":"The p21-activated kinase, Shk1, is essential for viability, establishment and maintenance of cell polarity, and proper mating response in the fission yeast, Schizosaccharomyces pombe. Here we describe the characterization of a highly conserved, WD repeat protein, Skb15, which negatively regulates Shk1 in fission yeast. A null mutation in the skb15 gene is lethal and results in deregulation of actin polymerization and localization, microtubule biogenesis, and the cytokinetic machinery, as well as a substantial uncoupling of these processes from the cell cycle. Loss of Skb15 function is suppressed by partial loss of Shk1, demonstrating that negative regulation of Shk1 by Skb15 is required for proper execution of cytoskeletal remodeling and cytokinetic functions. A mouse homolog of Skb15 can substitute for its counterpart in fission yeast, demonstrating that Skb15 protein function has been substantially conserved through evolution.","authors":"Kim HW, Yang P, Qyang Y, Lai H, Du H, Henkel JS, Kumar K, Bao S, Liu M, Marcus S","authors_abbrev":"Kim HW et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-06-08","publication_year":"2001","canto_session_key":"e38dfff0e4fa1169","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-05-31 14:53:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-14 14:14:13","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16C4.08c","SPBC1604.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-10-14"},{"uniquename":"PMID:37720683","title":"ACA-28, an anticancer compound, induces Pap1 nuclear accumulation via ROS-dependent and -independent mechanisms in fission yeast.","citation":"MicroPubl Biol 2023;2023","abstract":"The nucleocytoplasmic transport of proteins is an important mechanism to control cell fate. Pap1 is a fission yeast nucleocytoplasmic shuttling transcription factor of which localization is redox regulated. The nuclear export factor Crm1/exportin negatively regulates Pap1 by exporting it from the nucleus to the cytoplasm. Here, we describe the effect of an anti-cancer compound ACA-28, an improved derivative of 1'-acetoxychavicol acetate (ACA), on the subcellular distribution of Pap1. ACA-28 induced nuclear accumulation of Pap1 more strongly than did ACA. ROS inhibitor N-acetyl-L-cysteine (NAC) partly antagonized the Pap1 nuclear accumulation induced by ACA-28. NAC almost abolished Pap1 nuclear localization upon H  2  O  2  , whereas leptomycin B (LMB)-mediated inhibition of Pap1 nuclear export was resistant to NAC. Collectively, ACA-28-mediated apoptosis in cancer cells may involve ROS-dependent and -independent mechanisms.","doi":"10.17912/micropub.biology.000711","authors":"Takasaki T, Obana R, Fujiwara D, Tomimoto N, Khandakar GI, Satoh R, Sugiura R","authors_abbrev":"Takasaki T et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-09-18","publication_year":"2023","canto_session_key":"e55d21ec27e246c8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-09-19 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11179424","title":"Peroxide sensors for the fission yeast stress-activated mitogen-activated protein kinase pathway.","citation":"Mol Biol Cell 2001 Feb;12(2):407-19","abstract":"The Schizosaccharomyces pombe stress-activated Sty1p/Spc1p mitogen-activated protein (MAP) kinase regulates gene expression through the Atf1p and Pap1p transcription factors, homologs of human ATF2 and c-Jun, respectively. Mcs4p, a response regulator protein, acts upstream of Sty1p by binding the Wak1p/Wis4p MAP kinase kinase kinase. We show that phosphorylation of Mcs4p on a conserved aspartic acid residue is required for activation of Sty1p only in response to peroxide stress. Mcs4p acts in a conserved phospho-relay system initiated by two PAS/PAC domain-containing histidine kinases, Mak2p and Mak3p. In the absence of Mak2p or Mak3p, Sty1p fails to phosphorylate the Atf1p transcription factor or induce Atf1p-dependent gene expression. As a consequence, cells lacking Mak2p and Mak3p are sensitive to peroxide attack in the absence of Prr1p, a distinct response regulator protein that functions in association with Pap1p. The Mak1p histidine kinase, which also contains PAS/PAC repeats, does not regulate Sty1p or Atf1p but is partially required for Pap1p- and Prr1p-dependent transcription. We conclude that the transcriptional response to free radical attack is initiated by at least two distinct phospho-relay pathways in fission yeast.","authors":"Buck V, Quinn J, Soto Pino T, Martin H, Saldanha J, Makino K, Morgan BA, Millar JB","authors_abbrev":"Buck V et al.","pubmed_publication_date":"Feb 2001","pubmed_entrez_date":"2001-02-17","publication_year":"2001","canto_session_key":"95043240cd8d761e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-09-18 15:48:25","canto_approved_date":"2024-04-04 14:44:41","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-09-07 13:42:18","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.14","SPAC27E2.09","SPCC74.06","SPBC887.10","SPBC32F12.03c","SPCC757.07c","SPAC24B11.06c","SPAC9G1.02","SPBC3F6.03","SPAC1834.08","SPBC29B5.01","SPAC19D5.01"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2018-09-18"},{"uniquename":"PMID:11348689","title":"Conserved cAMP signaling cascades regulate fungal development and virulence.","citation":"FEMS Microbiol Rev 2001 May;25(3):349-64","abstract":"Two well characterized signal transduction cascades regulating fungal development and virulence are the MAP kinase and cAMP signaling cascades. Here we review the current state of knowledge on cAMP signaling cascades in fungi. While the processes regulated by cAMP signaling in fungi are as diverse as the fungi themselves, the components involved in signal transduction are remarkably conserved. Fungal cAMP signaling cascades are also quite versatile, which is apparent from the differential regulation of similar biological processes. In this review we compare and contrast cAMP signaling pathways that regulate development in the budding yeast Saccharomyces cerevisiae, the fission yeast Schizosaccharomyces pombe, and differentiation and virulence in the human pathogen Cryptococcus neoformans and the plant pathogen Ustilago maydis. We also present examples of interaction between the cAMP and MAP kinase signaling cascades in the regulation of fungal development and virulence.","authors":"D'Souza CA, Heitman J","authors_abbrev":"D'Souza CA et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-12","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21965289","title":"Nsk1 ensures accurate chromosome segregation by promoting association of kinetochores to spindle poles during anaphase B.","citation":"Mol Biol Cell 2011 Dec;22(23):4486-502","abstract":"Type 1 phosphatase (PP1) antagonizes Aurora B kinase to stabilize kinetochore-microtubule attachments and to silence the spindle checkpoint. We screened for factors that exacerbate the growth defect of Δdis2 cells, which lack one of two catalytic subunits of PP1 in fission yeast, and identified Nsk1, a novel protein required for accurate chromosome segregation. During interphase, Nsk1 resides in the nucleolus but spreads throughout the nucleoplasm as cells enter mitosis. Following dephosphorylation by Clp1 (Cdc14-like) phosphatase and at least one other phosphatase, Nsk1 localizes to the interface between kinetochores and the inner face of the spindle pole body during anaphase. In the absence of Nsk1, some kinetochores become detached from spindle poles during anaphase B. If this occurs late in anaphase B, then the sister chromatids of unclustered kinetochores segregate to the correct daughter cell. These unclustered kinetochores are efficiently captured, retrieved, bioriented, and segregated during the following mitosis, as long as Dis2 is present. However, if kinetochores are detached from a spindle pole early in anaphase B, then these sister chromatids become missegregated. These data suggest Nsk1 ensures accurate chromosome segregation by promoting the tethering of kinetochores to spindle poles during anaphase B.","doi":"10.1091/mbc.E11-07-0608","authors":"Buttrick GJ, Meadows JC, Lancaster TC, Vanoosthuyse V, Shepperd LA, Hoe KL, Kim DU, Park HO, Hardwick KG, Millar JB","authors_abbrev":"Buttrick GJ et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-10-04","publication_year":"2011","canto_session_key":"7d8eddd77bc43a59","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jonathan Millar","canto_first_approved_date":"2016-04-28 05:26:10","canto_approved_date":"2026-01-29 13:08:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-28 08:36:23","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Jonathan Millar","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPAC13G7.07","SPBC776.02c","SPAC11E3.08c","SPAC25A8.01c","SPAC8E11.02c","SPBC651.10","SPAC4G8.11c","SPCC1494.08c","SPAC31A2.13c","SPBC11B10.09","SPAC56F8.04c","SPAC4A8.09c","SPAC644.14c","SPBC651.09c","SPAC1782.09c","SPBC691.04","SPCC895.07","SPAC3G9.01","SPBC902.02c","SPBC20F10.06","SPCC4G3.04c","SPAC1B2.04","SPBC25D12.06","SPCC663.11","SPAC1805.08","SPCC1322.01","SPBC4B4.03","SPBC31F10.13c","SPBC26H8.03","SPAC664.02c","SPBC19C2.14","SPBC31F10.09c","SPBC557.02c","SPCC1795.01c","SPAC12B10.12c","SPBC365.14c","SPAC8E11.07c","SPAC1142.07c","SPAC11G7.02","SPBC19C7.02","SPBC336.13c","SPCC320.13c","SPAC824.02","SPAC31A2.11c","SPBC337.16"],"gene_count":46,"ltp_gene_count":8,"approved_date":"2016-04-28"},{"uniquename":"PMID:1135420","title":"[Studies on the uptake of xanthine by Schizosaccharomyces pombe from the stationary growth phase].","citation":"Protoplasma 1975;84(1-2):127-35","abstract":"1. Cells of Schizosaccharomyces pombe from the stationary growth phase show only a low capacity for the uptake of xanthine. In the presence of 2 muM xanthine, the initial uptake rate is found in the range of 6-10- minus 21 Moles times Cells- minus 1 times Min- minus 1 at 30 degrees C. 2. Preincubation in glucose solution results in a pronounced stimulation of the uptake rate. 3. The stimulating effect of the glucose pretreatment is repressed by cycloheximide, ammonium ions and amino acids. 4. The substrate dependency of the uptake rate shows a saturation kinetics. The Km-value has been determined to 6 muM. The temperature optimum is found in the range of 30 degrees C. 5. Xanthine is only slightly accumulated within the cells against the external concentration. Most of the external xanthine label is stored up in form of xanthosine and guanosine as well as incorporated in nucleic acids.","authors":"Seipel S, Reichert U","authors_abbrev":"Seipel S et al.","pubmed_publication_date":"1975","pubmed_entrez_date":"1975-01-01","publication_year":"1975","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11007487","title":"CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast.","citation":"Cell 2000 Sep 01;102(5):695-704","abstract":"Rod-shaped fission yeast cells grow in a polarized manner, and unlike budding yeast, the correct positioning of the growth sites at cell ends requires interphase microtubules. Here we describe a microtubule guidance mechanism that orients microtubules in the intracellular space along the long axis of the cell, guiding them to their target region at the cell ends. This mechanism involves tip1p, a CLIP170-like protein that localizes to distal tips of cytoplasmic microtubules. In the absence of tip1p, microtubular catastrophe is no longer restricted to cell ends but occurs when microtubules reach any region of the cellular cortex. Thus, tip1p enables microtubules to discriminate different cortical regions and regulates their dynamics accordingly.","authors":"Brunner D, Nurse P","authors_abbrev":"Brunner D et al.","pubmed_publication_date":"01 Sep 2000","pubmed_entrez_date":"2000-09-28","publication_year":"2000","canto_session_key":"8fb498d6aad39666","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-03-26 10:14:30","canto_approved_date":"2025-09-03 10:15:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-31 16:36:44","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":21,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.06","SPAC3C7.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-26"},{"uniquename":"PMID:16679557","title":"alpha-Synuclein fission yeast model: concentration-dependent aggregation without plasma membrane localization or toxicity.","citation":"J Mol Neurosci 2006;28(2):179-91","abstract":"Despite fission yeast's history of modeling salient cellular processes, it has not yet been used to model human neurodegeneration-linked protein misfolding. Because alpha-synuclein misfolding and aggregation are linked to Parkinson's disease (PD), here, we report a fission yeast (Schizosaccharomyces pombe) model that evaluates alpha-synuclein misfolding, aggregation, and toxicity and compare these properties with those recently characterized in budding yeast (Saccharomyces cerevisiae). Wild-type alpha-synuclein and three mutants (A30P, A53T, and A30P/A53T) were expressed with thiamine-repressible promoters (using vectors of increasing promoter strength: pNMT81, pNMT41, and pNMT1) to test directly in living cells the nucleation polymerization hypothesis for alpha-synuclein misfolding and aggregation. In support of the hypothesis, wild-type and A53T alpha-synuclein formed prominent intracellular cytoplasmic inclusions within fission yeast cells in a concentration- and time-dependent manner, whereas A30P and A30P/A53T remained diffuse throughout the cytoplasm. A53T alpha-synuclein formed aggregates faster than wild-type alpha-synuclein and at a lower alpha-synuclein concentration. Unexpectedly, unlike in budding yeast, wild-type and A53T alpha-synuclein did not target to the plasma membrane in fission yeast, not even at low alpha-synuclein concentrations or as a precursor step to forming aggregates. Despite alpha-synuclein's extensive aggregation, it was surprisingly nontoxic to fission yeast. Future genetic dissection might yield molecular insight into this protection against toxicity. We speculate that alpha-synuclein toxicity might be linked to its membrane binding capacity. To conclude, S. pombe and S. cerevisiae model similar yet distinct aspects of alpha-synuclein biology, and both organisms shed insight into alpha-synuclein's role in PD pathogenesis.","authors":"Brandis KA, Holmes IF, England SJ, Sharma N, Kukreja L, DebBurman SK","authors_abbrev":"Brandis KA et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-05-09","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU014259","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPRPB8U3","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17409385","title":"Identification, molecular cloning, and characterization of the sixth subunit of human transcription factor TFIIIC.","citation":"J Biol Chem 2007 Jun 08;282(23):17179-89","abstract":"TFIIIC in yeast and humans is required for transcription of tRNA and 5 S RNA genes by RNA polymerase III. In the yeast Saccharomyces cerevisiae, TFIIIC is composed of six subunits, five of which are conserved in humans. We report the identification, molecular cloning, and characterization of the sixth subunit of human TFIIIC, TFIIIC35, which is related to the smallest subunit of yeast TFIIIC. Human TFIIIC35 does not contain the phosphoglycerate mutase domain of its yeast counterpart, and these two proteins display only limited homology within a 34-amino acid domain. Homologs of the sixth TFIIIC subunit are also identified in other eukaryotes, and their phylogenic evolution is analyzed. Affinity-purified human TFIIIC from an epitope-tagged TFIIIC35 cell line is active in binding to and in transcription of the VA1 gene in vitro. Furthermore, TFIIIC35 specifically interacts with the human TFIIIC subunits TFIIIC63 and, to a lesser extent, TFIIIC90 in vitro. Finally, we determined a limited region in the smallest subunit of yeast TFIIIC that is sufficient for interacting with the yeast TFIIIC subunit ScTfc1 (orthologous to TFIIIC63) and found it to be adjacent to and overlap the 34-amino acid domain that is conserved from yeast to humans.","authors":"Dumay-Odelot H, Marck C, Durrieu-Gaillard S, Lefebvre O, Jourdain S, Prochazkova M, Pflieger A, Teichmann M","authors_abbrev":"Dumay-Odelot H et al.","pubmed_publication_date":"08 Jun 2007","pubmed_entrez_date":"2007-04-06","publication_year":"2007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1250.07","YOR110W"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20699567","title":"Vacuolar amino acid transporter Avt5p is responsible for lithium uptake in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2010;74(8):1719-21","abstract":"The fission yeast Schizosaccharomyces pombe was sensitive to salinity; cell growth was stopped by 0.5 M NaCl and by 10 mM LiCl. The avt5+ gene encodes a vacuolar transporter with a broad specificity for amino acids. We found that the avt5Delta mutant became highly tolerant of Li+ and Na+ in growth. Concanamycin A-sensitive Li+ uptake as well as cellular Li+ content was lower in the avt5 mutant, suggesting a role of Avt5p in cellular uptake of toxic Li+.","authors":"Iwaki T, Sekito T, Kakinuma Y","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-08-12","publication_year":"2010","canto_session_key":"d66b2d02532cfbd6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-12 09:45:46","canto_approved_date":"2023-08-03 09:43:02","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2012-09-28 12:42:47","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-02-12"},{"uniquename":"PMID:20152800","title":"Cleavage-induced termination in U2 snRNA gene expression.","citation":"Biochem Biophys Res Commun 2010 Mar 12;393(3):461-5","abstract":"The maturation of many small nuclear RNAs is dependent on RNase III-like endonuclease mediated cleavage, which generates a loading site for the exosome complex that trims the precursor at its 3' end. Using a temperature sensitive Pac1 nuclease, here we show that the endonuclease cleavage is equally important in terminating the transcription of the U2 snRNA in Schizosaccharomyces pombe. Using a temperature sensitive Dhp1p 5'-->3' exonuclease, we demonstrate that it also is an essential component of the termination pathway. Taken together the results support a \"reversed torpedoes\" model for the termination and maturation of the U2 snRNA; the Pac1 endonuclease cleavage provides entry sites for the 3' and 5' exonuclease activities, leading to RNA maturation in one direction and transcript termination in the other.","doi":"10.1016/j.bbrc.2010.02.023","authors":"Nabavi S, Nazar RN","authors_abbrev":"Nabavi S et al.","pubmed_publication_date":"12 Mar 2010","pubmed_entrez_date":"2010-02-16","publication_year":"2010","canto_session_key":"d2ae7c2d6f8a4b34","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-13 17:39:13","canto_approved_date":"2021-11-23 13:07:33","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-13 17:39:07","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.11c","SPAC26A3.12c","SPSNRNA.02"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-08-13"},{"uniquename":"PMID:15831585","title":"Direct activation of fission yeast adenylate cyclase by the Gpa2 Galpha of the glucose signaling pathway.","citation":"Proc Natl Acad Sci U S A 2005 Apr 26;102(17):6108-13","abstract":"G protein-mediated signaling is implicated in yeast and fungal cAMP pathways. By two-hybrid screens and pull-down experiments, we show that the fission yeast Gpa2 Galpha binds an N-terminal domain of adenylate cyclase, comprising a moderately conserved sequence within a region otherwise poorly related to other fungal adenylate cyclases. Overexpressing this domain in yeast perturbs cAMP signaling, which is restored by Gpa2 coexpression. Mutations affecting this domain, over 1,100 residues from the catalytic domain, alter glucose-triggered cAMP signaling. This is evidence for direct activation of adenylate cyclase by a fungal G protein and suggests a distinct activation mechanism from that of mammals.","authors":"Ivey FD, Hoffman CS","authors_abbrev":"Ivey FD et al.","pubmed_publication_date":"26 Apr 2005","pubmed_entrez_date":"2005-04-16","publication_year":"2005","canto_session_key":"f85ced2727868dc3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-25 19:09:41","canto_approved_date":"2022-02-07 17:52:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-20 09:06:32","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC285.09c","SPBC19C7.03","SPAC23H3.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-09-25"},{"uniquename":"PMID:9046095","title":"The essential Schizosaccharomyces pombe gpil+ gene complements a bakers' yeast GPI anchoring mutant and is required for efficient cell separation.","citation":"Yeast 1997 Feb;13(2):139-50","abstract":"The Schizosaccharomyces pombe gpil+ gene was cloned by complementation of the Saccharomyces cerevisiae gpil mutant, which has temperature-sensitive defects in growth and glycosyl phosphatidylinositol (GPI) membrane anchoring or protein, and which is defective in vitro in the first step in GPI anchor assembly, the formation of n-acetylglucosaminyl phosphatidylinositol (GlcNAc-PI). S. pombe gpil+ encodes a protein with 29% identity to amino acids 87-609 of the S. cerevisiae protein, and is the functional homolog of the S. cerevisiae Gpil protein, for it restores [3H]inositol-labelling of protein and in vitro GlcNAc-PI synthetic activity to both S. cerevisiae gpil and gpil::URA3 cells. Disruption of gpil+ is lethal. Haploid delta gpil+::his7+ spores germinate, but proceed through no more than three rounds of cell division, many cells ceasing growth as binucleate, septate cells with thickened septa. These results indicate that GPI synthesis is an essential function in fission yeast, and suggest that GPI anchoring is also required for completion of cytokinesis.","authors":"Colussi PA, Orlean P","authors_abbrev":"Colussi PA et al.","pubmed_publication_date":"Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_session_key":"b90e1da4e1a8027a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-10-26 13:41:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-10-30 18:36:28","canto_added_date":"2012-02-24 05:53:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-30"},{"uniquename":"PMID:9737975","title":"Role of alpha-subunit of mitochondrial processing peptidase in substrate recognition.","citation":"J Biol Chem 1998 Sep 25;273(39):25158-63","abstract":"Mitochondrial processing peptidase is a heterodimer consisting of alpha-mitochondrial processing peptidase (alpha-MPP) and beta-MPP. We investigated the role of alpha-MPP in substrate recognition using a recombinant yeast MPP. Disruption of amino acid residues between 10 and 129 of the alpha-MPP did not essentially impair binding activity with beta-MPP and processing activity, whereas truncation of the C-terminal 41 amino acids led to a significant loss of binding and processing activity. Several acidic amino acids in the region conserved among the enzymes from various species were mutated to asparagine or glutamine, and effects on processing of the precursors were analyzed. Glu353 is required for processing of malate dehydrogenase, aspartate aminotransferase, and adrenodoxin precursors. Glu377 and Asp378 are needed only for the processing of aspartate aminotransferase and adrenodoxin precursors, both of which have a longer extension peptide than the others studied. However, processing of the yeast alpha-MPP precursor, which has a short extension peptide of nine amino acids, was not affected by these mutations. Thus, effects of substitution of acidic amino acids on the processing differed with the precursor protein and depended on length of the extension peptides. alpha-MPP may function as a substrate-recognizing subunit by interacting mainly with basic amino acids at a region distal to the cleavage site in precursors with a longer extension peptide.","authors":"Shimokata K, Kitada S, Ogishima T, Ito A","authors_abbrev":"Shimokata K et al.","pubmed_publication_date":"25 Sep 1998","pubmed_entrez_date":"1998-09-17","publication_year":"1998","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC18E5.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9133618","title":"Analysis of the decaprenyl diphosphate synthase (dps) gene in fission yeast suggests a role of ubiquinone as an antioxidant.","citation":"J Biochem 1997 Mar;121(3):496-505","abstract":"Schizosaccharomyces pombe produces ubiquinone-10 whose side chain is thought to be provided by the product generated by decaprenyl diphosphate synthase. To understand the mechanism of ubiquinone biosynthesis in S. pombe, we have cloned the gene encoding decaprenyl diphosphate synthase by the combination of PCR amplification of the fragment and subsequent library screening. The determined DNA sequence of the cloned gene, called dps, revealed that the dps gene encodes a 378-amino-acid protein that has the typical conserved regions observed in many polyprenyl diphosphate synthases. Computer-assisted homology search indicated that Dps is 45 and 33% identical with hexaprenyl diphosphate synthase from Saccharomyces cerevisiae and octaprenyl diphosphate synthase from Escherichia coli, respectively. An S. pombe dps-deficient strain was constructed. This disruptant was not able to synthesize ubiquinone and had no detectable decaprenyl diphosphate synthase activity, indicating that the dps gene is unique and responsible for ubiquinone biosynthesis. The S. pombe dps-deficient strain could not grow on either rich medium supplemented with glycerol or on minimal medium supplemented with glucose. The dps-deficient strain required cysteine or glutathione for full growth on the minimal medium. In addition, the dps-deficient strain is more sensitive to H2O2 and Cu2+ than the wild type. These results suggests a role of ubiquinone as an antioxidant in fission yeast cells.","authors":"Suzuki K, Okada K, Kamiya Y, Zhu XF, Nakagawa T, Kawamukai M, Matsuda H","authors_abbrev":"Suzuki K et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_session_key":"169afc7abfd9873e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-01 12:55:37","canto_approved_date":"2026-06-13 13:39:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 18:06:11","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-02-01"},{"uniquename":"PMID:11598020","title":"Establishment and maintenance of sister chromatid cohesion in fission yeast by a unique mechanism.","citation":"EMBO J 2001 Oct 15;20(20):5779-90","abstract":"During S phase, chromatid cohesion is established only between nascent sisters and with faithful pairing along their entire region, but how this is ensured is unknown. Here we report that sister chromatid cohesion is formed and maintained by a unique mechanism. In fission yeast, Eso1p, functioning in close coupling to DNA replication, establishes sister chromatid cohesion whereas the newly identified Cohesin-associated protein Pds5p hinders the establishment of cohesion until counteracted by Eso1p, yet stabilizes cohesion once it is established. Eso1p interacts physically with Pds5p via its Ctf7p/Eco1p-homologous domain.","authors":"Tanaka K, Hao Z, Kai M, Okayama H","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"15 Oct 2001","pubmed_entrez_date":"2001-10-13","publication_year":"2001","canto_session_key":"b449ba7fcde22f63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-05-02 14:08:49","canto_approved_date":"2023-09-13 15:40:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-28 11:46:14","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.02","SPBC14C8.01c","SPAC31A2.05c","SPBC16A3.11","SPCC338.17c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-05-02"},{"uniquename":"PMID:15485909","title":"Rad62 protein functionally and physically associates with the smc5/smc6 protein complex and is required for chromosome integrity and recombination repair in fission yeast.","citation":"Mol Cell Biol 2004 Nov;24(21):9401-13","abstract":"Smc5 and Smc6 proteins form a heterodimeric SMC (structural maintenance of chromosome) protein complex like SMC1-SMC3 cohesin and SMC2-SMC4 condensin, and they associate with non-SMC proteins Nse1 and Nse2 stably and Rad60 transiently. This multiprotein complex plays an essential role in maintaining chromosome integrity and repairing DNA double strand breaks (DSBs). This study characterizes a Schizosaccharomyces pombe mutant rad62-1, which is hypersensitive to methyl methanesulfonate (MMS) and synthetically lethal with rad2 (a feature of recombination mutants). rad62-1 is hypersensitive to UV and gamma rays, epistatic with rhp51, and defective in repair of DSBs. rad62 is essential for viability and genetically interacts with rad60, smc6, and brc1. Rad62 protein physically associates with the Smc5-6 complex. rad62-1 is synthetically lethal with mutations in the genes promoting recovery from stalled replication, such as rqh1, srs2, and mus81, and those involved in nucleotide excision repair like rad13 and rad16. These results suggest that Rad62, like Rad60, in conjunction with the Smc5-6 complex, plays an essential role in maintaining chromosome integrity and recovery from stalled replication by recombination.","authors":"Morikawa H, Morishita T, Kawane S, Iwasaki H, Carr AM, Shinagawa H","authors_abbrev":"Morikawa H et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-16","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4G3.05c","SPAC4H3.05","SPBC1734.06","SPCC5E4.06","SPAC3G6.06c","SPAC2G11.12","SPCC970.01","SPBC20F10.04c","SPBC1921.02","SPBC582.05c","SPBC3E7.08c"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:14551247","title":"Schizosaccharomyces pombe Rdh54 (TID1) acts with Rhp54 (RAD54) to repair meiotic double-strand breaks.","citation":"Mol Biol Cell 2003 Nov;14(11):4707-20","abstract":"We report the characterization of rdh54+, the second fission yeast Schizosaccharomyces pombe Rad54 homolog. rdh54+ shares sequence and functional homology to budding yeast RDH54/TID1. Rdh54p is present during meiosis with appropriate timing for a meiotic recombination factor. It interacts with Rhp51 and the meiotic Rhp51 homolog Dmc1 in yeast two-hybrid assays. Deletion of rdh54+ has no effect on DNA damage repair during the haploid vegetative cell cycle. In meiosis, however, rdh54Delta shows decreased spore viability and homologous recombination with a concomitant increase in sister chromatid exchange. The rdh54Delta single mutant repairs meiotic breaks with similar timing to wild type, suggesting redundancy of meiotic recombination factors. Consistent with this, the rdh54Delta rhp54Delta double mutant fails to repair meiotic double strand breaks. Live cell analysis shows that rdh54Delta rhp54Delta asci do not arrest, but undergo both meiotic divisions with near normal timing, suggesting that failure to repair double strand breaks in S. pombe meiosis does not result in checkpoint arrest.","authors":"Catlett MG, Forsburg SL","authors_abbrev":"Catlett MG et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-10-11","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15A10.03c","SPAC644.14c","SPAC30D11.10","SPBC119.14","SPAC8E11.03c","SPAC22F3.03c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:11919719","title":"The deubiquitinating enzyme Ubp21p of fission yeast stabilizes a mutant form of protein kinase Prp4p.","citation":"Mol Genet Genomics 2002 Mar;267(1):88-95","abstract":"The protein kinase Prp4p of Schizosaccharomyces pombe is involved in control of the formation of active spliceosomes, phosphorylating the spliceosomal component Prp1p. The kinase domain of Prp4p is closely related to cyclin-dependent kinases (CDKs) and mitogen-activated kinases (MAPKs). A mutational analysis of the highly conserved amino acid sequence ALKHP in subdomain XI of this kinase showed that structural features of this sequence are important for the function of the kinase. We identified ubp21 as a high-copy-number suppressor of a mutation in the ALKHP motif. Characterization of this gene revealed that it encodes a deubiquitinating enzyme belonging to the family of ubiquitin-specific processing proteases (Ubps). The results presented in this report are consistent with the notion that the deubiquitinating activity of Ubp21p may be involved in regulating the steady-state levels of proteins including Prp4p.","authors":"Richert K, Schmidt H, Gross T, Käufer F","authors_abbrev":"Richert K et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-29","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC713.02c","SPCC188.08c","SPCC777.14"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23710280","title":"Synthetically engineered rpb1 alleles altering RNA polymerase II carboxy terminal domain phosphorylation induce discrete morphogenetic defects in Schizosaccharomyces pombe.","citation":"Commun Integr Biol 2013 May 01;6(3):e23954","abstract":"In this report the phenotypic effects of systematic site-directed mutations in the fission yeast RNA pol II carboxy terminal domain (CTD) are investigated. Remarkably, we find that alterations in CTD structure and/or phosphorylation result in distinct phenotypic changes related to morphogenetic control. A hypothesis based upon the concepts of \"informational entropy\" and \"algorithmic transformation\" is developed to explicate/rationalize these results.","doi":"10.4161/cib.23954","authors":"Hoffman K, Yoo H, Karagiannis J","authors_abbrev":"Hoffman K et al.","pubmed_publication_date":"01 May 2013","pubmed_entrez_date":"2013-05-28","publication_year":"2013","canto_session_key":"567432104f4cac83","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18272786","title":"Pxl1p, a paxillin-related protein, stabilizes the actomyosin ring during cytokinesis in fission yeast.","citation":"Mol Biol Cell 2008 Apr;19(4):1680-92","abstract":"Paxillins are a family of conserved LIM domain-containing proteins that play important roles in the function and integrity of the actin cytoskeleton. Although paxillins have been extensively characterized by cell biological and biochemical approaches, genetic studies are relatively scarce. Here, we identify and characterize a paxillin-related protein Pxl1p in the fission yeast Schizosaccharomyces pombe. Pxl1p is a component of the fission yeast actomyosin ring, a structure that is essential for cytokinesis. Cells deleted for pxl1 display a novel phenotype characterized by a splitting of the actomyosin ring in late anaphase, leading to the formation of two rings of which only one undergoes constriction. In addition, the rate of actomyosin ring constriction is slower in the absence of Pxl1p. pxl1Delta mutants display strong genetic interactions with mutants defective in IQGAP-related protein Rng2p and mutants defective in components of the fission yeast type II myosin machinery. Collectively, these results suggest that Pxl1p might cooperate with type II myosin and Rng2p-IQGAP to regulate actomyosin ring constriction as well as to maintain its integrity during constriction.","authors":"Ge W, Balasubramanian MK","authors_abbrev":"Ge W et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-02-15","publication_year":"2008","canto_session_key":"37b08171d9751598","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-01-31 17:34:11","canto_approved_date":"2025-12-15 15:08:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-01-31 17:34:02","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.09","SPAC4F10.11","SPBC4F6.12","SPAP8A3.08","SPAC27F1.02c","SPAC1782.09c","SPAC20G8.05c","SPAC4A8.05c","SPCC645.05c","SPCC613.04c","SPBC26H8.07c","SPAC1F5.04c","SPAC821.09","SPAC6G10.12c","SPCC4B3.15","SPAC4A8.15c","SPAC926.03","SPAC4F8.13c"],"gene_count":18,"ltp_gene_count":13,"approved_date":"2018-01-31"},{"uniquename":"PMID:27934687","title":"Preparation of Intracellular Metabolite Extracts from Liquid Schizosaccharomyces pombe Cultures.","citation":"Cold Spring Harb Protoc 2016 Dec 01;2016(12)","abstract":"The success of metabolomic analysis relies heavily on the sample preparation protocol. Here we present a protocol for intracellular metabolite extraction from liquid fission yeast cultures based on rapid quenching in pure methanol at -40°C, bead-beating in 50% methanol for cell disruption, and 10 kDa cutoff ultrafiltration for removal of proteins. Samples are concentrated by vacuum evaporation and resuspended in 50% acetonitrile for mass spectrometric analysis. This protocol is optimal for extraction of polar metabolites such as amino acids, organic acids, nucleotides, sugars, or sugar-phosphates. Its implementation requires <6 h and allows preparation of multiple samples in parallel.","doi":"10.1101/pdb.prot091553","authors":"Pluskal T, Nakamura T, Yanagida M","authors_abbrev":"Pluskal T et al.","pubmed_publication_date":"01 Dec 2016","pubmed_entrez_date":"2016-12-10","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-12-11 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21306563","title":"Specific biomarkers for stochastic division patterns and starvation-induced quiescence under limited glucose levels in fission yeast.","citation":"FEBS J 2011 Apr;278(8):1299-315","abstract":"Glucose as a source of energy is centrally important to our understanding of life. We investigated the cell division-quiescence behavior of the fission yeast Schizosaccharomyces pombe under a wide range of glucose concentrations (0-111 mM). The mode of S. pombe cell division under a microfluidic perfusion system was surprisingly normal under highly diluted glucose concentrations (5.6 mM, 1/20 of the standard medium, within human blood sugar levels). Division became stochastic, accompanied by a curious division-timing inheritance, in 2.2-4.4 mM glucose. A critical transition from division to quiescence occurred within a narrow range of concentrations (2.2-1.7 mM). Under starvation (1.1 mM) conditions, cells were mostly quiescent and only a small population of cells divided. Under fasting (0 mM) conditions, division was immediately arrested with a short chronological lifespan (16 h). When cells were first glucose starved prior to fasting, they possessed a substantially extended lifespan (∼14 days). We employed a quantitative metabolomic approach for S. pombe cell extracts, and identified specific metabolites (e.g. biotin, trehalose, ergothioneine, S-adenosyl methionine and CDP-choline), which increased or decreased at different glucose concentrations, whereas nucleotide triphosphates, such as ATP, maintained high concentrations even under starvation. Under starvation, the level of S-adenosyl methionine increased sharply, accompanied by an increase in methylated amino acids and nucleotides. Under fasting, cells rapidly lost antioxidant and energy compounds, such as glutathione and ATP, but, in fasting cells after starvation, these and other metabolites ensuring longevity remained abundant. Glucose-starved cells became resistant to 40 mM H(2)O(2) as a result of the accumulation of antioxidant compounds.","doi":"10.1111/j.1742-4658.2011.08050.x","authors":"Pluskal T, Hayashi T, Saitoh S, Fujisawa A, Yanagida M","authors_abbrev":"Pluskal T et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2011-02-11","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17452352","title":"Differential regulation of repeated histone genes during the fission yeast cell cycle.","citation":"Nucleic Acids Res 2007;35(10):3223-37","abstract":"The histone genes are highly reiterated in a wide range of eukaryotic genomes. The fission yeast, Schizosaccharomyces pombe, has three pairs of histone H3-H4 genes: hht1+-hhf1+, hht2+-hhf2+ and hht3+-hhf3+. While the deduced amino acid sequences are identical, it remains unknown whether transcriptional regulation differs among the three pairs. Here, we report the transcriptional properties of each H3-H4 gene pair during the cell cycle. The levels of transcripts of hht1+-hhf1+ and hht3+-hhf3+ pairs and hhf2+ are increased at S-phase, while that of hht2+ remains constant throughout the cell cycle. We showed that the GATA-type transcription factor, Ams2, binds to the promoter regions of core histone genes in an AACCCT-box-dependent manner and is required for activation of S-phase-specific transcription. Furthermore, we found that Ams2-depletion stimulates feedback regulation of histone transcripts, mainly up-regulating the basal levels of hht2+-hhf2+ transcription, which are normally down-regulated by Hip1 and Slm9, homologs of the human histone chaperone, HIRA. These observations provide insight into the molecular mechanisms of differential regulation of transcripts from repeated histone genes in the fission yeast.","authors":"Takayama Y, Takahashi K","authors_abbrev":"Takayama Y et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-04-25","publication_year":"2007","canto_session_key":"3e4ec1257970269c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-02 10:03:27","canto_approved_date":"2021-06-11 15:09:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-03-02 10:03:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":45,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31F10.13c","SPBC15D4.03","SPAC631.02","SPAC1834.03c","SPCC290.04","SPBC8D2.03c","SPBC1105.17","SPBC11B10.10c","SPBC8D2.04","SPBC1105.11c","SPAC1834.04","SPBC1105.12"],"gene_count":12,"ltp_gene_count":9,"approved_date":"2018-03-02"},{"uniquename":"PMID:10373519","title":"A Uve1p-mediated mismatch repair pathway in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1999 Jul;19(7):4703-10","abstract":"UV damage endonuclease (Uve1p) from Schizosaccharomyces pombe was initially described as a DNA repair enzyme specific for the repair of UV light-induced photoproducts and proposed as the initial step in an alternative excision repair pathway. Here we present biochemical and genetic evidence demonstrating that Uve1p is also a mismatch repair endonuclease which recognizes and cleaves DNA 5' to the mispaired base in a strand-specific manner. The biochemical properties of the Uve1p-mediated mismatch endonuclease activity are similar to those of the Uve1p-mediated UV photoproduct endonuclease. Mutants lacking Uve1p display a spontaneous mutator phenotype, further confirming the notion that Uve1p plays a role in mismatch repair. These results suggest that Uve1p has a surprisingly broad substrate specificity and may function as a general type of DNA repair protein with the capacity to initiate mismatch repair in certain organisms.","authors":"Kaur B, Fraser JL, Freyer GA, Davey S, Doetsch PW","authors_abbrev":"Kaur B et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-06-22","publication_year":"1999","canto_session_key":"84f3e243eadd49bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-07-10 08:43:54","canto_approved_date":"2025-07-10 08:43:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-07-10 08:43:46","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.09c","SPAC19G12.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2025-07-10"},{"uniquename":"PMID:8649397","title":"Activation and regulation of the Spc1 stress-activated protein kinase in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1996 Jun;16(6):2870-7","abstract":"Spc1, an osmotic-stress-stimulated mitogen-activated protein kinase (MAPK) homolog in the fission yeast Schizosaccharomyces pombe, is required for the induction of mitosis and survival in high-osmolarity conditions. Spc1, also known as Sty1, is activated by Wis1 MAPK kinase and inhibited by Pyp1 tyrosine phosphatase. Spc1 is most closely related to Saccharomyces cerevisiae Hog1 and mammalian p38 kinases. Whereas Hog1 is specifically responsive to osmotic stress, we report here that Spc1 is activated by multiple forms of stress, including high temperature and oxidative stress. In this regard Spc1 is more similar to mammalian p38. Activation of Spc1 is crucial for survival of various forms of stress. Spc1 regulates expression of genes encoding stress-related proteins such as glycerol-3-phosphate dehydrogenase (gpd1+) and trehalose-6-phosphate synthase (tps1+). Spc1 also promotes expression of pyp2+, which encodes a tyrosine phosphatase postulated as a negative regulator of Spc1. This proposal is supported by the finding that Spc1 associates with Pyp2 in vivo and that the amount of Spc1 tyrosine phosphorylation is lower in a Pyp2-overproducing strain than in the wild type. Moreover, the level of stress-stimulated gpd1+ expression is higher in delta pyp2 mutants than in the wild type. These findings demonstrate that Spc1 promotes expression of genes involved in stress survival and that of regulation may be commonly employed to modulate MAPK signal transduction pathways in eukaryotic species.","authors":"Degols G, Shiozaki K, Russell P","authors_abbrev":"Degols G et al.","pubmed_publication_date":"Jun 1996","pubmed_entrez_date":"1996-06-01","publication_year":"1996","canto_session_key":"7482369b55e6cbf6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-09-14 15:29:51","canto_approved_date":"2021-03-04 16:28:03","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-08-08 10:06:59","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC19D5.01","SPBC215.05","SPAC328.03","SPAC26F1.10c","SPAC24B11.06c"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2018-09-14"},{"uniquename":"PMID:39502420","title":"Mitochondrial aspartate aminotransferase (  maa1  ) inactivation causes glutamate-requiring  glu1  mutation in  Schizosaccharomyces   pombe .","citation":"MicroPubl Biol 2024;2024","abstract":"Two genomic genes, which rescue ammonium assimilation defect in the glutamate-requiring  Schizosaccharomyces   pombe glu1  mutant, were identified. The  maa1  , encoding a mitochondrial aspartate aminotransferase, is the causative gene of  glu1  mutation because an inseparable linkage between  maa1  and  glu1  on the chromosome, and also the  glu1  mutant strain has a nonsense mutation within the  maa1  coding region, which is responsible for its defective phenotype. The  yhm2  , a mitochondrial 2-oxoglutarate carrier, was also isolated as a weak multicopy suppressor gene. These findings reiterate the importance of the mitochondria in utilizing the amino acids for cellular nitrogen metabolism.","doi":"10.17912/micropub.biology.001338","authors":"Kitamura K","authors_abbrev":"Kitamura K","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-11-06","publication_year":"2024","canto_session_key":"cc3251094baf47d8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kenji Kitamura","canto_first_approved_date":"2025-04-15 14:16:42","canto_approved_date":"2025-12-31 11:41:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-09 08:42:07","canto_added_date":"2024-11-07 00:25:05","annotation_curators":[{"name":"Kenji Kitamura","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.01","SPATRNASER.03","SPBC83.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2025-04-15"},{"uniquename":"PMID:5550309","title":"A UV-supersensitive mutant in the yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1971;110(2):134-43","abstract":"","authors":"Fabre F","authors_abbrev":"Fabre F","pubmed_publication_date":"1971","pubmed_entrez_date":"1971-01-01","publication_year":"1971","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15175151","title":"A unified nomenclature for protein subunits of mediator complexes linking transcriptional regulators to RNA polymerase II.","citation":"Mol Cell 2004 Jun 04;14(5):553-7","abstract":"","authors":"Bourbon HM, Aguilera A, Ansari AZ, Asturias FJ, Berk AJ, Bjorklund S, Blackwell TK, Borggrefe T, Carey M, Carlson M, Conaway JW, Conaway RC, Emmons SW, Fondell JD, Freedman LP, Fukasawa T, Gustafsson CM, Han M, He X, Herman PK, Hinnebusch AG, Holmberg S, Holstege FC, Jaehning JA, Kim YJ, Kuras L, Leutz A, Lis JT, Meisterernest M, Naar AM, Nasmyth K, Parvin JD, Ptashne M, Reinberg D, Ronne H, Sadowski I, Sakurai H, Sipiczki M, Sternberg PW, Stillman DJ, Strich R, Struhl K, Svejstrup JQ, Tuck S, Winston F, Roeder RG, Kornberg RD","authors_abbrev":"Bourbon HM et al.","pubmed_publication_date":"04 Jun 2004","pubmed_entrez_date":"2004-06-04","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:12:11","annotation_curators":[],"annotation_file_curators":[],"genes":["YHR041C","SPAC17G8.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:27206859","title":"TOR complex 2 localises to the cytokinetic actomyosin ring and controls the fidelity of cytokinesis.","citation":"J Cell Sci 2016 Jul 01;129(13):2613-24","abstract":"The timing of cell division is controlled by the coupled regulation of growth and division. The target of rapamycin (TOR) signalling network synchronises these processes with the environmental setting. Here, we describe a novel interaction of the fission yeast TOR complex 2 (TORC2) with the cytokinetic actomyosin ring (CAR), and a novel role for TORC2 in regulating the timing and fidelity of cytokinesis. Disruption of TORC2 or its localisation results in defects in CAR morphology and constriction. We provide evidence that the myosin II protein Myp2 and the myosin V protein Myo51 play roles in recruiting TORC2 to the CAR. We show that Myp2 and TORC2 are co-dependent upon each other for their normal localisation to the cytokinetic machinery. We go on to show that TORC2-dependent phosphorylation of actin-capping protein 1 (Acp1, a known regulator of cytokinesis) controls CAR stability, modulates Acp1-Acp2 (the equivalent of the mammalian CAPZA-CAPZB) heterodimer formation and is essential for survival upon stress. Thus, TORC2 localisation to the CAR, and TORC2-dependent Acp1 phosphorylation contributes to timely control and the fidelity of cytokinesis and cell division.","doi":"10.1242/jcs.190124","authors":"Baker K, Kirkham S, Halova L, Atkin J, Franz-Wachtel M, Cobley D, Krug K, Maček B, Mulvihill DP, Petersen J","authors_abbrev":"Baker K et al.","pubmed_publication_date":"01 Jul 2016","pubmed_entrez_date":"2016-05-22","publication_year":"2016","canto_session_key":"3c1d722e9eff6055","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-05-23 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21B10.05c","SPAC4A8.05c","SPBC12C2.02c","SPAPYUG7.02c","SPCC4B3.15","SPBC1A4.05","SPAC12B10.07","SPAC631.01c","SPBC30D10.10c","SPBC2D10.14c","SPAC1F5.04c","SPCC24B10.07","SPBP23A10.10"],"gene_count":13,"ltp_gene_count":13},{"uniquename":"PMID:32295063","title":"The Catalytic-Dependent and -Independent Roles of Lsd1 and Lsd2 Lysine Demethylases in Heterochromatin Formation in  Schizosaccharomyces pombe .","citation":"Cells 2020 Apr 13;9(4)","abstract":"In eukaryotes, heterochromatin plays a critical role in organismal development and cell fate acquisition, through regulating gene expression. The evolutionarily conserved lysine-specific demethylases, Lsd1 and Lsd2, remove mono- and dimethylation on histone H3, serving complex roles in gene expression. In the fission yeast  Schizosaccharomyces pombe , null mutations of Lsd1 and Lsd2 result in either severe growth defects or inviability, while catalytic inactivation causes minimal defects, indicating that Lsd1 and Lsd2 have essential functions beyond their known demethylase activity. Here, we show that catalytic mutants of Lsd1 or Lsd2 partially assemble functional heterochromatin at centromeres in RNAi-deficient cells, while the C-terminal truncated alleles of Lsd1 or Lsd2 exacerbate heterochromatin formation at all major heterochromatic regions, suggesting that Lsd1 and Lsd2 repress heterochromatic transcripts through mechanisms both dependent on and independent of their catalytic activities. Lsd1 and Lsd2 are also involved in the establishment and maintenance of heterochromatin. At constitutive heterochromatic regions, Lsd1 and Lsd2 regulate one another and cooperate with other histone modifiers, including the class II HDAC Clr3 and the Sirtuin family protein Sir2 for gene silencing, but not with the class I HDAC Clr6. Our findings explore the roles of lysine-specific demethylases in epigenetic gene silencing at heterochromatic regions.","doi":"10.3390/cells9040955","authors":"Marayati BF, Tucker JF, Cerda DA, Hou TC, Chen R, Sugiyama T, Pease JB, Zhang K","authors_abbrev":"Marayati BF et al.","pubmed_publication_date":"13 Apr 2020","pubmed_entrez_date":"2020-04-17","publication_year":"2020","canto_session_key":"9b4ac98c99b4f86c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ke Zhang","canto_first_approved_date":"2020-10-01 14:24:09","canto_approved_date":"2025-09-03 11:27:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-28 04:52:02","canto_added_date":"2020-04-18 00:15:05","annotation_curators":[{"name":"Ke Zhang","community_curator":true,"annotation_count":118,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":62,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":5,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPBC16D10.07c","SPAC23E2.02","SPBC36.05c","SPCC1322.13","SPBC146.09c","SPCC622.16c","SPCC736.11","SPAC212.11"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2020-10-01"},{"uniquename":"PMID:19606211","title":"Nucleocytoplasmic shuttling of the TACC protein Mia1p/Alp7p is required for remodeling of microtubule arrays during the cell cycle.","citation":"PLoS One 2009 Jul 16;4(7):e6255","abstract":"Microtubule arrays are remodeled as cells proceed through the cell cycle. It is important to understand how remodeling is regulated in time and space. In fission yeast, the conserved microtubule associated TACC/TOG complex plays an important role in organizing microtubules throughout the cell cycle. Here we show that this complex undergoes nucleocytoplasmic shuttling through the nuclear import and export signals located in the TACC protein Mia1p/Alp7p. When the Crm1p-dependent nuclear export signal of Mia1p is disabled, Mia1p accumulates in the nucleus while its partner protein Alp14p/TOG is restricted to the cytoplasm. This leads to defects in assembly of both interphase arrays and the mitotic spindle. Artificial targeting of Alp14p to the nucleus partially rescues the mitotic spindle defects caused by lack of Mia1p nuclear export. Interestingly, the nuclear export sequence of Mia1p appears to overlap with the Alp14p binding site. We propose that intricate regulation of the subcellular distribution of TACC/TOG complexes drives microtubule array remodeling as cells progress through the cell cycle.","doi":"10.1371/journal.pone.0006255","authors":"Ling YC, Vjestica A, Oliferenko S","authors_abbrev":"Ling YC et al.","pubmed_publication_date":"16 Jul 2009","pubmed_entrez_date":"2009-07-17","publication_year":"2009","canto_session_key":"ba7ce39a2e9301af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-06-01 10:47:32","canto_approved_date":"2022-06-01 10:47:32","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-06-01 10:47:25","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":2,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC895.07","SPAC890.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-06-01"},{"uniquename":"PMID:12654901","title":"Mid2p stabilizes septin rings during cytokinesis in fission yeast.","citation":"J Cell Biol 2003 Mar 31;160(7):1083-92","abstract":"Septins are filament-forming proteins with a conserved role in cytokinesis. In the fission yeast Schizosaccharomyces pombe, septin rings appear to be involved primarily in cell-cell separation, a late stage in cytokinesis. Here, we identified a protein Mid2p on the basis of its sequence similarity to S. pombe Mid1p, Saccharomyces cerevisiae Bud4p, and Candida albicans Int1p. Like septin mutants, mid2delta mutants had delays in cell-cell separation. mid2delta mutants were defective in septin organization but not contractile ring closure or septum formation. In wild-type cells, septins assembled first during mitosis in a single ring and during septation developed into double rings that did not contract. In mid2delta cells, septins initially assembled in a single ring but during septation appeared in the cleavage furrow, forming a washer or disc structure. FRAP studies showed that septins are stable in wild-type cells but exchange 30-fold more rapidly in mid2delta cells. Mid2p colocalized with septins and required septins for its localization. A COOH-terminal pleckstrin homology domain of Mid2p was required for its localization and function. No genetic interactions were found between mid2 and the related gene mid1. Thus, these studies identify a new factor responsible for the proper stability and function of septins during cytokinesis.","authors":"Berlin A, Paoletti A, Chang F","authors_abbrev":"Berlin A et al.","pubmed_publication_date":"31 Mar 2003","pubmed_entrez_date":"2003-03-26","publication_year":"2003","canto_session_key":"1021271c94244356","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-10-29 11:32:06","canto_approved_date":"2025-09-03 14:03:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-18 15:29:56","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPAC9G1.11c","SPAPYUG7.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-10-29"},{"uniquename":"PMID:25428589","title":"Long non-coding RNA-mediated transcriptional interference of a permease gene confers drug tolerance in fission yeast.","citation":"Nat Commun 2014 Nov 27;5:5576","abstract":"Most long non-coding RNAs (lncRNAs) encoded by eukaryotic genomes remain uncharacterized. Here we focus on a set of intergenic lncRNAs in fission yeast. Deleting one of these lncRNAs exhibited a clear phenotype: drug sensitivity. Detailed analyses of the affected locus revealed that transcription of the nc-tgp1 lncRNA regulates drug tolerance by repressing the adjacent phosphate-responsive permease gene transporter for glycerophosphodiester 1 (tgp1(+)). We demonstrate that the act of transcribing nc-tgp1 over the tgp1(+) promoter increases nucleosome density, prevents transcription factor access and thus represses tgp1(+) without the need for RNA interference or heterochromatin components. We therefore conclude that tgp1(+) is regulated by transcriptional interference. Accordingly, decreased nc-tgp1 transcription permits tgp1(+) expression upon phosphate starvation. Furthermore, nc-tgp1 loss induces tgp1(+) even in repressive conditions. Notably, drug sensitivity results directly from tgp1(+) expression in the absence of the nc-tgp1 RNA. Thus, transcription of an lncRNA governs drug tolerance in fission yeast.","doi":"10.1038/ncomms6576","authors":"Ard R, Tong P, Allshire RC","authors_abbrev":"Ard R et al.","pubmed_publication_date":"27 Nov 2014","pubmed_entrez_date":"2014-11-28","publication_year":"2014","canto_session_key":"9f0301dcfc800f2a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2023-01-12 17:55:28","canto_approved_date":"2025-01-20 12:14:14","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2022-12-02 12:40:29","canto_added_date":"2014-11-29 01:17:50","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":41,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.1698","SPBC1271.09","SPAC664.01c","SPBC27B12.11c","SPNCRNA.1343","SPAC1F3.01","SPAC1006.03c","SPCC736.11","SPBC428.08c","SPCC188.13c","SPBP4G3.02","SPNCRNA.1712","SPCC736.12c"],"gene_count":13,"ltp_gene_count":11,"approved_date":"2023-01-12"},{"uniquename":"EMBL:AU010947","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37859837","title":"In fission yeast, 65 non-essential mitochondrial proteins related to respiration and stress become essential in low-glucose conditions.","citation":"R Soc Open Sci 2023 Oct;10(10):230404","abstract":"Mitochondria perform critical functions, including respiration, ATP production, small molecule metabolism, and anti-oxidation, and they are involved in a number of human diseases. While the mitochondrial genome contains a small number of protein-coding genes, the vast majority of mitochondrial proteins are encoded by nuclear genes. In fission yeast  Schizosaccharomyces pombe , we screened 457 deletion ( del ) mutants deficient in nuclear-encoded mitochondrial proteins, searching for those that fail to form colonies in culture medium containing low glucose (0.03-0.1%; low-glucose sensitive,  lgs ), but that proliferate in regular 2-3% glucose medium. Sixty-five (14%) of the 457 deletion mutants displayed the  lgs  phenotype. Thirty-three of them are defective either in dehydrogenases, subunits of respiratory complexes, the citric acid cycle, or in one of the nine steps of the CoQ10 biosynthetic pathway. The remaining 32  lgs  mutants do not seem to be directly related to respiration. Fifteen are implicated in translation, and six encode transporters. The remaining 11 function in anti-oxidation, amino acid synthesis, repair of DNA damage, microtubule cytoskeleton, intracellular mitochondrial distribution or unknown functions. These 32 diverse  lgs  genes collectively maintain mitochondrial functions under low (1/20-1/60× normal) glucose concentrations. Interestingly, 30 of them have homologues associated with human diseases.","doi":"10.1098/rsos.230404","authors":"Mori A, Uehara L, Toyoda Y, Masuda F, Soejima S, Saitoh S, Yanagida M","authors_abbrev":"Mori A et al.","pubmed_publication_date":"Oct 2023","pubmed_entrez_date":"2023-10-20","publication_year":"2023","canto_session_key":"ffd6562f14d8240e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shigeaki Saitoh","canto_first_approved_date":"2023-10-31 07:47:52","canto_approved_date":"2025-04-02 18:26:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-30 08:40:55","canto_added_date":"2023-10-20 23:25:04","annotation_curators":[{"name":"Shigeaki Saitoh","community_curator":true,"annotation_count":65,"orcid":"0000-0001-5408-296X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30C2.06c","SPCC162.05","SPCC1672.04c","SPBC18H10.11c","SPBC691.04","SPAC19G12.11","SPBC4F6.08c","SPAC1556.02c","SPAC13F5.03c","SPAC30C2.02","SPBC2G2.07c","SPAC644.07","SPBC800.07c","SPAC22H10.09","SPBPJ4664.01","SPAC637.11","SPBC2G2.08","SPAC1687.12c","SPAC56F8.04c","SPBC30D10.13c","SPBC336.13c","SPAC823.10c","SPBC30B4.06c","SPAC6B12.12","SPAC6G10.08","SPBC119.06","SPAC3A12.12","SPBC3H7.03c","SPAC4G8.11c","SPCC1682.01","SPBC1215.01","SPBC25D12.06","SPBC12C2.01c","SPCC11E10.04","SPAC2F7.17","SPCC1322.01","SPBC29A3.10c","SPBC19F8.04c","SPAC1486.01","SPBC146.12","SPBC337.15c","SPCC613.10","SPBC27.06c","SPBC1709.09","SPBC902.05c","SPBC16H5.06","SPCC306.08c","SPCC330.12c","SPBC1604.02c","SPBC725.10","SPBC12D12.07c","SPBC947.15c","SPBC16A3.03c","SPCC4G3.04c","SPAC1610.02c","SPBP23A10.16","SPBC36.04","SPBC28E12.04","SPAC17H9.08","SPAC8C9.09c","SPCC16A11.07","SPCC320.12","SPBC2D10.18","SPAC1296.02","SPAC222.12c"],"gene_count":65,"ltp_gene_count":65,"approved_date":"2023-10-31"},{"uniquename":"PMID:9154838","title":"A ubiquitin-conjugating enzyme in fission yeast that is essential for the onset of anaphase in mitosis.","citation":"Mol Cell Biol 1997 Jun;17(6):3388-97","abstract":"A cDNA encoding a ubiquitin-conjugating enzyme designated UbcP4 in fission yeast was isolated. Disruption of its genomic gene revealed that it was essential for cell viability. In vivo depletion of the UbcP4 protein demonstrated that it was necessary for cell cycle progression at two phases, G2/M and metaphase/anaphase transitions. The G2 arrest of UbcP4-depleted cells was dependent upon chk1, which mediates checkpoint pathway. UbcP4-depleted cells arrested at metaphase had condensed chromosomes but were defective in separation. However, septum formation and cytokinesis were not restrained during the metaphase arrest. Overexpression of UbcP4 specifically rescued the growth defect of cut9ts cells at a restrictive temperature. cut9 encodes a component of the anaphase-promoting complex (APC) which is required for chromosome segregation at anaphase and moreover is defined as cyclin-specific ubiquitin ligase. Cdc13, a mitotic cyclin in fission yeast, was accumulated in the UbcP4-depleted cells. These results strongly suggested that UbcP4 is a ubiquitin-conjugating enzyme working in conjunction with APC and mediates the ubiquitin pathway for degradation of \"sister chromatid holding protein(s)\" at the onset of anaphase and possibly of mitotic cyclin at the exit of mitosis.","authors":"Osaka F, Seino H, Seno T, Yamao F","authors_abbrev":"Osaka F et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"ab90f75fa22cff89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-03 19:56:56","canto_approved_date":"2021-03-22 15:57:37","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-05-06 08:30:07","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBP16F5.04","SPCC1259.13","SPAC18B11.07c","SPBC119.02","SPCC1259.15c","SPAC6F12.15c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2017-07-03"},{"uniquename":"PMID:40027523","title":"Characterization and comparison of temperature-sensitive  Schizosaccharomyces pombe  mutants of the septation initiation network scaffolds, Cdc11 and Sid4.","citation":"MicroPubl Biol 2025;2025","abstract":"The  Schizosaccharomyces pombe  septation initiation network (SIN) is required for cytokinesis and septation. The SIN includes a protein kinase cascade that is assembled at spindle pole bodies (SPBs) in a cell cycle specific manner on a scaffold consisting of Cdc11 , related to human centriolin, and the a-helical protein Sid4 . Here, we characterized temperature-sensitive  cdc11  and  sid4  mutants isolated in the 1990s. We determined the mutations within each allele, examined their phenotypes, and analyzed their growth compared with previously characterized mutant alleles. The new mutants described here expand the toolkit for studying how the SIN assembles at SPBs.","doi":"10.17912/micropub.biology.001503","authors":"Turner LA, Fletcher AB, Willet AH, Gould KL","authors_abbrev":"Turner LA et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-03-03","publication_year":"2025","canto_session_key":"70b85f781da808f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2025-04-07 14:29:42","canto_approved_date":"2026-01-31 13:44:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-06 00:11:30","canto_added_date":"2025-03-04 00:25:05","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":22,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPCC1739.11c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2025-04-07"},{"uniquename":"PMID:14981292","title":"Characterization of two genes encoding putative cysteine synthase required for cysteine biosynthesis in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2004 Feb;68(2):306-11","abstract":"Cysteine synthase catalyzes the formation of cysteine from O-acetylserine, and is the key enzyme for de novo cysteine biosynthesis in Schizosaccharomyces pombe. An examination of the S. pombe database revealed that two gene products are predicted to encode proteins homologous to eukaryotic cysteine synthases. Disruption of one of these candidates, cys1a+ (SPBC36.04), caused an obvious cysteine auxotrophy, while disruption of cys1b+ (SPAC3A12.17c) had no effect on the growth phenotype. Furthermore, overexpression of cys1b+ did not complement the cysteine auxotrophic phenotype of cys1a mutant cells. These results indicated that cys1a+, not cys1b+, primarily functions in the biosynthesis of cysteine in S. pombe cells. We constructed a bacterial-S. pombe shuttle vector containing cys1a+ as a selective marker gene. The combination of the cysteine auxotroph and new vector could be useful for the expression of a heterologous protein.","authors":"Fujita Y, Takegawa K","authors_abbrev":"Fujita Y et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2004-02-26","publication_year":"2004","canto_session_key":"6c937464226c2d78","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-08-07 14:22:00","canto_approved_date":"2026-02-12 11:40:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 14:03:47","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.04","SPAC3A12.17c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-07"},{"uniquename":"PMID:42129552","title":"SNOR promotes translation restart after dormancy.","citation":"Nature 2026 May 13;","abstract":"Cellular dormancy enables survival during prolonged nutrient limitation by reversibly suppressing protein synthesis 1-4 . How inactive eukaryotic ribosomes are reactivated when nutrients return remains unclear. Here, using high-resolution in situ cryo-electron tomography in Schizosaccharomyces pombe, we identify SNOR, an SBDS domain-containing ribosome-associated factor that binds at the peptidyl transferase centre and contacts the hypusinated loop of eIF5A during glucose depletion-induced dormancy. Rather than acting as a canonical hibernation factor, SNOR licenses dormant ribosomes for rapid translational restart. Upon glucose repletion, SNOR and eIF5A act together to promote efficient recovery of polysomes and exit from dormancy. These findings define a stress-responsive ribosome restart module that couples carbon-source limitation to surveillance of the ribosomal active site and reactivation of protein synthesis.","doi":"10.1038/s41586-026-10530-7","authors":"Gluc M, Rosa H, Bozko M, Turner LA, Prince CR, Peskova Y, Feaga HA, Gould KL, Mattei S, Jomaa A","authors_abbrev":"Gluc M et al.","pubmed_publication_date":"13 May 2026","pubmed_entrez_date":"2026-05-13","publication_year":"2026","canto_session_key":"95356cd09b24545c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-05-14 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1682.14","SPBC16G5.14c","SPBC839.05c","SPAC1687.06c","SPCC1183.08c","SPCC330.14c","SPCC1223.05c","SPAC22A12.04c","SPAC1F7.13c","SPBC11C11.09c","SPAC18G6.14c","SPCC1322.15","SPCC613.06","SPAC3A12.10","SPBC2F12.04","SPBC685.07c","SPCP31B10.07","SPAC31G5.03","SPBC29B5.03c","SPAC694.05c","SPBC1685.09","SPBC839.04","SPAC3G9.03","SPBC18E5.06","SPAC521.05","SPBC405.07","SPBC21C3.19","SPCC663.04","SPAC17G6.06","SPCC576.08c","SPAC890.08","SPAC1783.08c","SPAC6B12.15","SPAC8C9.08","SPCC576.09","SPCC613.05c","SPBC1921.01c","SPAPB1E7.12","SPAPB17E12.13","SPBC29A3.04","SPCC622.18","SPBC685.06","SPAC3H5.05c","SPAC26A3.07c","SPCC962.04","SPBC16D10.11c","SPAC17A5.03","SPAC9G1.03c","SPBC776.01","SPAC1071.07c","SPBC18H10.12c","SPAC1805.13","SPAC26H5.10c","SPBP8B7.03c","SPBC16A3.08c","SPBC577.02","SPBC21C3.13","SPAC6F6.07c","SPAC11G7.04","SPAC22H12.04c","SPAC25G10.06","SPAC11E3.15","SPAC23A1.11","SPAC959.08","SPBC29A3.12","SPBC1685.10","SPAC23C11.02c","SPAC664.05","SPBC106.18","SPAC15E1.03","SPCC1322.11","SPBP22H7.08","SPBC776.11","SPAC19B12.04","SPBC800.04c","SPAC1805.11c","SPAC959.07","SPBC18H10.14","SPAC3H5.10","SPBC18E5.04"],"gene_count":80,"ltp_gene_count":80,"pdb_entries":[{"pdb_id":"9rvu","gene_chains":[{"gene_uniquename":"SPBP22H7.08","chain":"AN","position":"1-147"},{"gene_uniquename":"SPBC29A3.04","chain":"BT","position":"1-259"},{"gene_uniquename":"SPAC17G6.06","chain":"Ae","position":"1-134"},{"gene_uniquename":"SPCC962.04","chain":"AP","position":"1-145"},{"gene_uniquename":"SPAC1687.06c","chain":"By","position":"1-134"},{"gene_uniquename":"SPAC8C9.08","chain":"AI","position":"1-203"},{"gene_uniquename":"SPBC2F12.04","chain":"Bb/A","position":"164-183"},{"gene_uniquename":"SPBC685.07c","chain":"Bl","position":"1-136"},{"gene_uniquename":"SPCP31B10.07","chain":"HE","position":"1-842"},{"gene_uniquename":"SPCC1682.14","chain":"Bd","position":"1-193"},{"gene_uniquename":"SPAC959.08","chain":"Bf","position":"1-160"},{"gene_uniquename":"SPAC23A1.11","chain":"Ba","position":"1-197"},{"gene_uniquename":"SPBC16A3.08c","chain":"H1","position":"1-284"},{"gene_uniquename":"SPBC839.05c","chain":"AU","position":"1-131"},{"gene_uniquename":"SPBC29A3.12","chain":"AM","position":"1-192"},{"gene_uniquename":"SPBC16G5.14c","chain":"AG","position":"1-249"},{"gene_uniquename":"SPBC18H10.12c","chain":"BS","position":"1-251"},{"gene_uniquename":"SPAC664.05","chain":"BX","position":"1-208"},{"gene_uniquename":"SPBC11C11.09c","chain":"BQ","position":"1-294"},{"gene_uniquename":"SPBC1685.09","chain":"Aj","position":"1-56"},{"gene_uniquename":"SPBC1685.10","chain":"Ah","position":"1-83"},{"gene_uniquename":"SPCC1183.08c","chain":"HL","position":"1-216"},{"gene_uniquename":"SPCC330.14c","chain":"Bi","position":"1-149"},{"gene_uniquename":"SPCC576.08c","chain":"AF","position":"1-253"},{"gene_uniquename":"SPCC576.09","chain":"Aa","position":"1-118"},{"gene_uniquename":"SPCC613.05c","chain":"Bt","position":"1-122"},{"gene_uniquename":"SPCC613.06","chain":"BU","position":"1-189"},{"gene_uniquename":"SPAC1805.13","chain":"BY","position":"1-134"},{"gene_uniquename":"SPAC22H12.04c","chain":"AE","position":"1-252"},{"gene_uniquename":"SPBC405.07","chain":"Bu","position":"1-99"},{"gene_uniquename":"SPCC1223.05c","chain":"Bv","position":"1-91"},{"gene_uniquename":"SPBC18E5.06","chain":"Ab","position":"1-87"},{"gene_uniquename":"SPCC663.04","chain":"Bx","position":"1-51"},{"gene_uniquename":"SPAC11G7.04","chain":"BA","position":"78-128"},{"gene_uniquename":"SPAC3H5.05c","chain":"AR","position":"1-139"},{"gene_uniquename":"SPAC22A12.04c","chain":"Ac","position":"1-130"},{"gene_uniquename":"SPAC3G9.03","chain":"Bh","position":"1-139"},{"gene_uniquename":"SPAC19B12.04","chain":"Ak","position":"1-61"},{"gene_uniquename":"SPBC18H10.14","chain":"AT","position":"1-140"},{"gene_uniquename":"SPBC16D10.11c","chain":"AV","position":"1-152"},{"gene_uniquename":"SPAC3A12.10","chain":"Be","position":"1-176"},{"gene_uniquename":"SPAC1F7.13c","chain":"BN","position":"1-253"},{"gene_uniquename":"SPAC31G5.03","chain":"AO","position":"1-152"},{"gene_uniquename":"SPAC23C11.02c","chain":"Ad","position":"1-143"},{"gene_uniquename":"SPAC26A3.07c","chain":"BW","position":"1-174"},{"gene_uniquename":"SPAC25G10.06","chain":"Ai","position":"1-68"},{"gene_uniquename":"SPAC6F6.07c","chain":"AQ","position":"1-151"},{"gene_uniquename":"SPBP8B7.03c","chain":"BP","position":"1-363"},{"gene_uniquename":"SPAC17A5.03","chain":"BO","position":"1-388"},{"gene_uniquename":"SPAC9G1.03c","chain":"Bo","position":"1-109"},{"gene_uniquename":"SPAC26H5.10c","chain":"HI","position":"1-157"},{"gene_uniquename":"SPBC776.11","chain":"Bm","position":"1-148"},{"gene_uniquename":"SPBC21C3.13","chain":"AW","position":"1-144"},{"gene_uniquename":"SPBC29B5.03c","chain":"Bk","position":"1-126"},{"gene_uniquename":"SPAC694.05c","chain":"Af","position":"1-89"},{"gene_uniquename":"SPAC3H5.10","chain":"Bq","position":"1-127"},{"gene_uniquename":"SPCC622.18","chain":"BR","position":"1-195"},{"gene_uniquename":"SPBC18E5.04","chain":"BV","position":"1-221"},{"gene_uniquename":"SPAC11E3.15","chain":"Bg","position":"1-117"},{"gene_uniquename":"SPAC18G6.14c","chain":"AK","position":"1-195"},{"gene_uniquename":"SPAC6B12.15","chain":"Am","position":"1-314"},{"gene_uniquename":"SPBC106.18","chain":"Bj","position":"1-141"},{"gene_uniquename":"SPAPB17E12.13","chain":"Bc","position":"1-187"},{"gene_uniquename":"SPBC776.01","chain":"Bn","position":"1-61"},{"gene_uniquename":"SPAPB1E7.12","chain":"AJ","position":"1-239"},{"gene_uniquename":"SPBC800.04c","chain":"B1","position":"1-94"},{"gene_uniquename":"SPAC959.07","chain":"AH","position":"1-262"},{"gene_uniquename":"SPAC521.05","chain":"AL","position":"1-200"},{"gene_uniquename":"SPBC21C3.19","chain":"HS","position":"1-106"},{"gene_uniquename":"SPCC1322.15","chain":"Bs","position":"1-111"},{"gene_uniquename":"SPAC890.08","chain":"Bp","position":"1-113"},{"gene_uniquename":"SPAC1783.08c","chain":"BZ","position":"1-201"},{"gene_uniquename":"SPBC577.02","chain":"Bw","position":"1-74"},{"gene_uniquename":"SPBC1921.01c","chain":"Br","position":"1-108"},{"gene_uniquename":"SPAC1805.11c","chain":"Ag","position":"1-119"},{"gene_uniquename":"SPAC15E1.03","chain":"B0","position":"1-106"},{"gene_uniquename":"SPAC1071.07c","chain":"AS","position":"1-154"},{"gene_uniquename":"SPBC685.06","chain":"AD","position":"1-292"}],"title":"in situ S. pombe hibernating ribosome after 7 days of glucose depletion","entry_authors":"Rosa H,Gluc M,Jomaa A,Mattei S","entry_authors_abbrev":"Rosa H et al.","reference_uniquename":"PMID:42129552","experimental_method":"EM","resolution":"3.38"},{"pdb_id":"9phc","gene_chains":[{"gene_uniquename":"SPBC29A3.04","chain":"BT","position":"1-259"},{"gene_uniquename":"SPAC1687.06c","chain":"By","position":"1-134"},{"gene_uniquename":"SPBC2F12.04","chain":"Bb","position":"1-187"},{"gene_uniquename":"SPBC685.07c","chain":"Bl","position":"1-136"},{"gene_uniquename":"SPCC1682.14","chain":"Bd","position":"1-193"},{"gene_uniquename":"SPAC959.08","chain":"Bf","position":"1-160"},{"gene_uniquename":"SPAC23A1.11","chain":"Ba","position":"1-197"},{"gene_uniquename":"SPBC18H10.12c","chain":"BS","position":"1-251"},{"gene_uniquename":"SPAC664.05","chain":"BX","position":"1-208"},{"gene_uniquename":"SPBC11C11.09c","chain":"BQ","position":"1-294"},{"gene_uniquename":"SPCC330.14c","chain":"Bi","position":"1-149"},{"gene_uniquename":"SPCC613.05c","chain":"Bt","position":"1-122"},{"gene_uniquename":"SPCC613.06","chain":"BU","position":"1-189"},{"gene_uniquename":"SPAC1805.13","chain":"BY","position":"1-134"},{"gene_uniquename":"SPBC405.07","chain":"Bu","position":"1-99"},{"gene_uniquename":"SPCC1223.05c","chain":"Bv","position":"1-91"},{"gene_uniquename":"SPCC663.04","chain":"Bx","position":"1-51"},{"gene_uniquename":"SPCC1322.11","chain":"Bh","position":"1-139"},{"gene_uniquename":"SPAC3A12.10","chain":"Be","position":"1-176"},{"gene_uniquename":"SPBC839.04","chain":"BN","position":"1-253"},{"gene_uniquename":"SPAC26A3.07c","chain":"BW","position":"1-174"},{"gene_uniquename":"SPBP8B7.03c","chain":"BP","position":"1-363"},{"gene_uniquename":"SPAC17A5.03","chain":"BO","position":"1-388"},{"gene_uniquename":"SPAC9G1.03c","chain":"Bo","position":"1-109"},{"gene_uniquename":"SPBC776.11","chain":"Bm","position":"1-148"},{"gene_uniquename":"SPBC29B5.03c","chain":"Bk","position":"1-126"},{"gene_uniquename":"SPAC3H5.10","chain":"Bq","position":"1-127"},{"gene_uniquename":"SPCC622.18","chain":"BR","position":"1-195"},{"gene_uniquename":"SPBC18E5.04","chain":"BV","position":"1-221"},{"gene_uniquename":"SPAC11E3.15","chain":"Bg","position":"1-117"},{"gene_uniquename":"SPBC106.18","chain":"Bj","position":"1-141"},{"gene_uniquename":"SPAPB17E12.13","chain":"Bc","position":"1-187"},{"gene_uniquename":"SPBC776.01","chain":"Bn","position":"1-61"},{"gene_uniquename":"SPBC800.04c","chain":"B1","position":"1-94"},{"gene_uniquename":"SPBC21C3.19","chain":"HS","position":"1-106"},{"gene_uniquename":"SPCC1322.15","chain":"Bs","position":"1-111"},{"gene_uniquename":"SPAC890.08","chain":"Bp","position":"1-113"},{"gene_uniquename":"SPAC1783.08c","chain":"BZ","position":"1-201"},{"gene_uniquename":"SPBC577.02","chain":"Bw","position":"1-74"},{"gene_uniquename":"SPBC1921.01c","chain":"Br","position":"1-108"},{"gene_uniquename":"SPAC15E1.03","chain":"B0","position":"1-106"}],"title":"In vitro reconstituted complex of purified S. pombe large ribosomal subunit and SNOR","entry_authors":"Gluc M,Jomaa A","entry_authors_abbrev":"Gluc M et al.","reference_uniquename":"PMID:42129552","experimental_method":"EM","resolution":"2.8"}]},{"uniquename":"EMBL:SPD110","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24278218","title":"DNA sequences at a glance.","citation":"PLoS One 2013;8(11):e79922","abstract":"Data summarization and triage is one of the current top challenges in visual analytics. The goal is to let users visually inspect large data sets and examine or request data with particular characteristics. The need for summarization and visual analytics is also felt when dealing with digital representations of DNA sequences. Genomic data sets are growing rapidly, making their analysis increasingly more difficult, and raising the need for new, scalable tools. For example, being able to look at very large DNA sequences while immediately identifying potentially interesting regions would provide the biologist with a flexible exploratory and analytical tool. In this paper we present a new concept, the \"information profile\", which provides a quantitative measure of the local complexity of a DNA sequence, independently of the direction of processing. The computation of the information profiles is computationally tractable: we show that it can be done in time proportional to the length of the sequence. We also describe a tool to compute the information profiles of a given DNA sequence, and use the genome of the fission yeast Schizosaccharomyces pombe strain 972 h(-) and five human chromosomes 22 for illustration. We show that information profiles are useful for detecting large-scale genomic regularities by visual inspection. Several discovery strategies are possible, including the standalone analysis of single sequences, the comparative analysis of sequences from individuals from the same species, and the comparative analysis of sequences from different organisms. The comparison scale can be varied, allowing the users to zoom-in on specific details, or obtain a broad overview of a long segment. Software applications have been made available for non-commercial use at http://bioinformatics.ua.pt/software/dna-at-glance.","doi":"10.1371/journal.pone.0079922","authors":"Pinho AJ, Garcia SP, Pratas D, Ferreira PJ","authors_abbrev":"Pinho AJ et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-11-27","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11693916","title":"Coflocculation of Escherichia coli and Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2001 Oct;57(1-2):175-81","abstract":"Several yeasts, such as Candida utilis, Dekkera bruxellensis, Hanseniaspora guilliermondii, Kloeckera apiculata, Saccharomyces cerevisiae and Schizosaccharomyces pombe, were found to coaggregate with Escherichia coli, but S. pombe showed much less coflocculation than the other yeasts (Peng et al. 2001)). S. pombe is known to have galactose-rich cell walls and we investigated whether this might be responsible for its different behavior by studying the wild-type TP4-1D, with a mannose to galactose ratio of 1 to 1.2, and the glycosylation mutant gms1delta (Man:Gal=1:0). The wild-type induced very low levels of coflocculation (3%) while gms1delta induced a remarkable amount of coflocculation (48%). Coflocculation of the mutant was inhibited by mannose but not affected by galactose or glucose. The S. cerevisiae mnn2 mutant, with a mannan structure similar to gms1delta, also showed a high degree of coflocculation (40%). However, S. cerevisiae mutant mnn9, with a mature core similar to S. pombe, showed decreased coflocculation (21.3%). Both these S. cerevisae mutants were sensitive to mannose inhibition. Coflocculation of E. coli and gms1delta also could be inhibited by gms1delta mannan and plant lectins, such as HHA, GNA and NPA, specific to either alpha-1-3- or alpha-1-6-linked mannosyl units. From these results we conclude that the E. coli lectins may have specificity for alpha-1-6- and alpha-1-3-linked mannose residues either in the outer chain or in the core of S. pombe, but in wild-type strains these mannose residues are shielded by galactose residues.","authors":"Peng X, Sun J, Michiels C, Iserentant D, Verachtert H","authors_abbrev":"Peng X et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-11-06","publication_year":"2001","canto_session_key":"126fe1061f88a098","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-07 14:34:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-25 10:34:49","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-07-25"},{"uniquename":"PMID:10816256","title":"Involvement of PCH family proteins in cytokinesis and actin distribution.","citation":"Microsc Res Tech 2000 Apr 15;49(2):168-72","abstract":"Pombe Cdc15 homology (PCH) proteins constitute an extensive protein family whose members have been found in diverse eukaryotic organisms. These proteins are characterized by the presence of several conserved sequence and structural motifs. Recent studies in yeast and mammalian cultured cells have implicated these proteins in actin-based processes, in particular, cytokinesis. Here we review the recent findings on the in vivo localization, function, and binding partners of PCH family members. We also provide new microscopy data regarding the in vivo dynamics of a budding yeast PCH protein involved in cytokinesis.","authors":"Lippincott J, Li R","authors_abbrev":"Lippincott J et al.","pubmed_publication_date":"15 Apr 2000","pubmed_entrez_date":"2000-05-18","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31285271","title":"Fission Yeast Asc1 Stabilizes the Interaction between Eukaryotic Initiation Factor 3a and Rps0A/uS2 for Protein Synthesis.","citation":"Mol Cell Biol 2019 Oct 01;39(19)","abstract":"Aminoacyl-tRNA synthetase cofactors play important roles in coordinating aminoacylation and translation. In this study, we describe an additional function of the fission yeast  a minoacyl-tRNA  s ynthetase  c ofactor  1  (Asc1) in translation. We found that Asc1 directly binds and stabilizes the interaction between small ribosomal protein Rps0A/uS2 and eukaryotic initiation factor 3a (eIF3a). In the absence of Asc1, the interaction between eIF3a and Rps0A/uS2 was compromised. The interaction between Rps0A/uS2 and eIF3a mediated the 40S ribosomal subunit binding of eIF3 in 43S preinitiation complex formation to stimulate translation initiation. Keeping with this idea, in an  asc1  mutant, the association of mRNA with the 40S ribosomal subunit was defective and protein synthesis was compromised. To show that Asc1 is directly involved in translation, we demonstrate that the addition of recombinant Asc1 is able to rescue the translation defect of the  asc1  mutant in a cell-free system. Furthermore, this function of Asc1 is likely to be evolutionarily conserved, as a similar interaction with eIF3a and Rps0A/uS2 could be identified in the budding yeast  Saccharomyces cerevisiae  and human aminoacyl-tRNA synthetase cofactors. Together, these results identify a function of aminoacyl-tRNA synthetase cofactors in translation preinitiation complex formation, which adds significantly to the expanded functions associated with aminoacyl-tRNA synthetases and their cofactors.","doi":"10.1128/MCB.00161-19","authors":"Wang YT, Chien YC, Hsiao WY, Wang CC, Wang SW","authors_abbrev":"Wang YT et al.","pubmed_publication_date":"01 Oct 2019","pubmed_entrez_date":"2019-07-10","publication_year":"2019","canto_session_key":"312c8af6293e302e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shao-Win Wang","canto_first_approved_date":"2019-08-18 18:14:42","canto_approved_date":"2025-09-02 20:42:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-29 01:25:40","canto_added_date":"2019-07-11 00:15:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Shao-Win Wang","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.15c","SPBC685.06","SPAC17C9.03","SPAC30C2.04","SPAC3G9.09c","SPBC17D11.05","SPBC17A3.04c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2019-08-18"},{"uniquename":"EMBL:SPC01047","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1269534","title":"Anaesthetics delay and accelerate division in the fission yeast Schizosaccharomyces pombe.","citation":"Exp Cell Res 1976 May;99(2):432-5","abstract":"","authors":"Smith HT, Mitchison JM","authors_abbrev":"Smith HT et al.","pubmed_publication_date":"May 1976","pubmed_entrez_date":"1976-05-01","publication_year":"1976","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9599658","title":"Markers of cell polarity during and after nitrogen starvation in Schizosaccharomyces pombe.","citation":"Biochem Cell Biol 1997;75(6):697-708","abstract":"In Schizosaccharomyces pombe, nitrogen starvation induces transient acceleration of cell division and reduction in cell size with a final arrest in G1. The division size control appears to be impaired by mutations in cdr1/nim1 and cdr2, genes that encode protein kinases mediating nutritional control over the mitotic cycle. cdr- cells arrest after fewer rounds of division and are larger than the wild type. Recent work suggests that long-term nitrogen starvation causes S. pombe wild-type cells to become spherical, which suggests loss of cell polarity. cdr mutants retain the elongated shape, indicating a potential difference in cell polarity control relative to the wild type. We examined several markers related to maintenance of cell polarity in S. pombe following nitrogen starvation including cell division scar pattern and actin and microtubule cytoskeleton. Wild-type cells as well as cdr mutants maintained a normal cell division scar pattern throughout nitrogen starvation but cells dividing under these conditions developed a wall malformation in the center of the septum. In cells arrested by nitrogen starvation, actin patches, normally associated with sites of cell wall deposition, were larger and distributed randomly along the cell surface. Cytoplasmic arrays of microtubules, which are thought to be involved in control of the polarity signal, were not visibly affected. The effects were similar in wild-type cells and in cdr- mutants. Upon refeeding, the new growth always reoccurred at the tip zones and there were only small deviations of its direction from the original axis. The results indicate that cell polarity is preserved both in wild-type cells, which arrest in G1 and appear spherical, and in cdr1/nim1 and cdr2 mutants, which arrest in G2 and appear polarized throughout the starvation period.","authors":"Rupes I, Jochová J, Young PG","authors_abbrev":"Rupes I et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16428309","title":"Effects of four oxidants, menadione, 1-chloro-2,4-dinitrobenzene, hydrogen peroxide and cumene hydroperoxide, on fission yeast Schizosaccharmoyces pombe.","citation":"J Biochem 2005 Dec;138(6):797-804","abstract":"Several chemical agents have been used to exert oxidative stress in the study of stress response, but differences in the effects of different reagents have received little attention. To elucidate whether such differences exist, the response of Schizosaccharomyces pombe to menadione (MD), 1-chloro-2,4-dinitrobenzene (CDNB), hydrogen peroxide and cumene hydroperoxide (CHP), which are frequently used to exert oxidative stress, was investigated. Sensitivity to these reagents differed among mutants deficient in genes involved in oxidative stress resistance. N-Acetylcysteine restored resistance to MD, CHP and hydrogen peroxide but did not change sensitivity to CDNB. The induction kinetics of genes induced by oxidative stress differed for each reagent. MD, CDNB and hydrogen peroxide caused a transient induction of genes, but the peak times of induction differed among the reagents. CHP gave quite different kinetics in that the induction continued for up to 2 h. The ctt1(+) gene was not induced by CHP. GSH rapidly decreased in the cells treated with high concentrations of these reagents, but at a low concentration only CDNB decreased GSH. These results indicated that S. pombe responded differently to the oxidative stress exerted by these different reagents.","authors":"Mutoh N, Kawabata M, Kitajima S","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2006-01-24","publication_year":"2005","canto_session_key":"8a653c867356cc80","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-09-03 13:51:12","canto_approved_date":"2024-11-13 09:36:44","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-20 17:41:19","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":23,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC821.10c","SPAC22F3.10c","SPAC8C9.14","SPBC29B5.01","SPCC757.07c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2024-09-03"},{"uniquename":"PMID:23279110","title":"A proline-tyrosine nuclear localization signal (PY-NLS) is required for the nuclear import of fission yeast PAB2, but not of human PABPN1.","citation":"Traffic 2013 Mar;14(3):282-94","abstract":"Nuclear poly(A)-binding proteins (PABPs) are evolutionarily conserved proteins that play key roles in eukaryotic gene expression. In the fission yeast Schizosaccharomyces pombe, the major nuclear PABP, Pab2, functions in the maturation of small nucleolar RNAs as well as in nuclear RNA decay. Despite knowledge about its nuclear functions, nothing is known about how Pab2 is imported into the nucleus. Here, we show that Pab2 contains a proline-tyrosine nuclear localization signal (PY-NLS) that is necessary and sufficient for its nuclear localization and function. Consistent with the role of karyopherin β2 (Kapβ2)-type receptors in the import of PY-NLS cargoes, we show that the fission yeast ortholog of human Kapβ2, Kap104, binds to recombinant Pab2 and is required for Pab2 nuclear localization. The absence of arginine methylation in a basic region N-terminal to the PY-core motif of Pab2 did not affect its nuclear localization. However, in the context of a sub-optimal PY-NLS, we found that Pab2 was more efficiently targeted to the nucleus in the absence of arginine methylation, suggesting that this modification can affect the import kinetics of a PY-NLS cargo. Although a sequence resembling a PY-NLS motif can be found in the human Pab2 ortholog, PABPN1, our results indicate that neither a functional PY-NLS nor Kapβ2 activity are required to promote entry of PABPN1 into the nucleus of human cells. Our findings describe the mechanism by which Pab2 is imported into the nucleus, providing the first example of a PY-NLS import system in fission yeast. In addition, this study suggests the existence of alternative or redundant nuclear import pathways for human PABPN1.","doi":"10.1111/tra.12036","authors":"Mallet PL, Bachand F","authors_abbrev":"Mallet PL et al.","pubmed_publication_date":"Mar 2013","pubmed_entrez_date":"2013-01-03","publication_year":"2013","canto_session_key":"f654fd19770862a4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16E9.12c","SPAC2F3.06c","SPAC890.07c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:SPD135","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10602257","title":"Lethal level overexpression of gamma-tubulin in fission yeast causes mitotic arrest.","citation":"Cell Motil Cytoskeleton 1999 Dec;44(4):284-95","abstract":"gamma-Tubulin is a member of the tubulin superfamily and plays essential roles in microtubule nucleation. While the level of other tubulins, alpha- and beta-tubulin, is strictly regulated in higher eukaryotes and overexpression of beta-tubulin is toxic in yeasts, gamma-tubulin can be overexpressed by fivefold in fission yeast without any obvious defect in growth. Extreme overexpression of gamma-tubulin in mammalian cells caused growth arrest; however, the exact level of gamma-tubulin and the critical level of gamma-tubulin necessary for growth defect were undetermined. We have constructed strains that over- or underexpress gamma-tubulin by placing the gamma-tubulin gene under the control of the inducible nmt1 promoter and its variants. Among these, the weakest promoter was able to produce enough gamma-tubulin to support normal growth when its expression was induced. A strain in which the gamma-tubulin gene was placed under the control of the strongest inducible promoter achieved 160-fold overexpression of gamma-tubulin and its growth was suppressed. Normal cytoplasmic microtubules were mostly lost in gamma-tubulin overexpressing cells and gamma-tubulin was accumulated around the periphery of nuclei. Many of the cells were arrested in mitosis. A small fraction of cells did proceed to undergo nuclear division; however, its process looked either significantly deterred or abnormal. Our results presented here suggest that excess gamma-tubulin disrupts the microtubule array and significantly deters the formation of the mitotic spindle, most likely because of random nucleation of microtubules from excess gamma-tubulin in the cytoplasm.","authors":"Horio T, Basaki A, Takeoka A, Yamato M","authors_abbrev":"Horio T et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-12-22","publication_year":"1999","canto_session_key":"e22af6c37b9446c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-08 20:34:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-08 20:34:50","canto_added_date":"2012-02-24 05:52:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-08"},{"uniquename":"PMID:8244022","title":"Sequence of a fission yeast gene encoding a protein with extensive homology to eukaryotic elongation factor-1 gamma.","citation":"Gene 1993 Nov 30;134(1):119-22","abstract":"A polypeptide with an apparent molecular mass of 23 kDa was identified, that exhibited an affinity to a 491-bp DNA derived from one of the Schizosaccharomyces pombe centromeric DNAs (cen1). After determining its N-terminal amino acid (aa) sequence, a Sz. pombe genomic DNA encompassing the coding sequence of the isolated protein was cloned, and a 2.3-kb genomic DNA region sequenced. Further sequence analysis of cDNA clones, originating from this particular genomic region, confirmed the existence of an open reading frame with a short intron, which encodes a 409-aa protein with striking homology to eukaryotic elongation factor-1 gamma.","authors":"Momoi H, Yamada H, Ueguchi C, Mizuno T","authors_abbrev":"Momoi H et al.","pubmed_publication_date":"30 Nov 1993","pubmed_entrez_date":"1993-11-30","publication_year":"1993","canto_session_key":"b7695286a2394a21","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:49:47","canto_approved_date":"2018-12-22 20:49:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 20:49:41","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:2558289","title":"Cauliflower mosaic virus promoters direct efficient expression of a bacterial G418 resistance gene in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1989 Dec;220(1):95-101","abstract":"A system is presented for transformation of the fission yeast Schizosaccharomyces pombe to resistance against the antibiotic G418. The bacterial resistance gene of the transposon Tn5 is expressed under the control of promoters and transcription terminators from cauliflower mosaic virus (CaMV). The promoter of the S. pombe alcohol dehydrogenase gene has also been used. Transformants can be selected directly on medium containing G418 (up to 1 mg/ml) due to inactivation of G418 by the Tn5 gene product, the aminoglycoside 3'-phosphotransferase (II). The plant viral promoter 35S confers higher resistance to G418 than the 19S promoter. This corresponds to the relative strengths of these promoters in plant cells. The strong plant promoter 35S yields resistance comparable to that obtained with the strong S. pombe promoter from the alcohol dehydrogenase gene. The constructions with the two plant promoters have been used on multicopy shuttle plasmids that replicate autonomously in S. pombe and Escherichia coli. In addition the 35S and the 19S constructions have been inserted into the S. pombe genome where they confer G418 resistance as single copy genes. Since vector sequences are excluded in this case, all the necessary signals for expression of G418 resistance are contained within the DNA fragments containing the plant promoters, the resistance gene and the plant terminators. This transformation system is independent of S. pombe mutants. It may be useful for the transformation of other lower eukaryotes. The activity of the CaMV promoters in S. pombe may be exploited for the expression of plant genes in fission yeast.","authors":"Gmünder H, Kohli J","authors_abbrev":"Gmünder H et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33888556","title":"Meikin synergizes with shugoshin to protect cohesin Rec8 during meiosis I.","citation":"Genes Dev 2021 May 01;35(9-10):692-697","abstract":"The conserved meiosis-specific kinetochore regulator, meikin (Moa1 in fission yeast) plays a central role in establishing meiosis-specific kinetochore function. However, the underlying molecular mechanisms remain elusive. Here, we show how Moa1 regulates centromeric cohesion protection, a function that has been previously attributed to shugoshin (Sgo1). Moa1 is known to associate with Plo1 kinase. We explore Plo1-dependent Rec8 phosphorylation and identify a key phosphorylation site required for cohesion protection. The phosphorylation of Rec8 by Moa1-Plo1 potentiates the activity of PP2A associated with Sgo1. This leads to dephosphorylation of Rec8 at another site, which thereby prevents cleavage of Rec8 by separase.","doi":"10.1101/gad.348052.120","authors":"Ma W, Zhou J, Chen J, Carr AM, Watanabe Y","authors_abbrev":"Ma W et al.","pubmed_publication_date":"01 May 2021","pubmed_entrez_date":"2021-04-23","publication_year":"2021","canto_session_key":"153ada5377adf0b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2021-05-14 18:15:43","canto_approved_date":"2024-10-09 11:10:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-02 13:59:30","canto_added_date":"2021-04-25 00:15:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.06c","SPAC23C11.16","SPBC3H7.15","SPAC17A5.11","SPBC29A10.14","SPCC188.02","SPBC16H5.07c","SPAC15E1.07c","SPBP35G2.03c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2021-05-14"},{"uniquename":"PMID:37446379","title":"Formation of Transient Protein Aggregate-like Centers Is a General Strategy Postponing Degradation of Misfolded Intermediates.","citation":"Int J Mol Sci 2023 Jul 07;24(13)","abstract":"When misfolded intermediates accumulate during heat shock, the protein quality control system promotes cellular adaptation strategies. In  Schizosaccharomyces pombe , thermo-sensitive proteins assemble upon stress into protein aggregate-like centers, PACs, to escape from degradation. The role of this protein deposition strategy has been elusive due to the use of different model systems and reporters, and to the addition of artificial inhibitors, which made interpretation of the results difficult. Here, we compare fission and budding yeast model systems, expressing the same misfolding reporters in experiments lacking proteasome or translation inhibitors. We demonstrate that mild heat shock triggers reversible PAC formation, with the collapse of both reporters and chaperones in a process largely mediated by chaperones. This assembly postpones proteasomal degradation of the misfolding reporters, and their Hsp104-dependent disassembly occurs during stress recovery. Severe heat shock induces formation of cytosolic PACs, but also of nuclear structures resembling nucleolar rings, NuRs, presumably to halt nuclear functions. Our study demonstrates that these distantly related yeasts use very similar strategies to adapt and survive to mild and severe heat shock and that aggregate-like formation is a general cellular scheme to postpone protein degradation and facilitate exit from stress.","doi":"10.3390/ijms241311202","authors":"Boronat S, Cabrera M, Vega M, Alcalá J, Salas-Pino S, Daga RR, Ayté J, Hidalgo E","authors_abbrev":"Boronat S et al.","pubmed_publication_date":"07 Jul 2023","pubmed_entrez_date":"2023-07-14","publication_year":"2023","canto_session_key":"6174b6ceda38fefa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Susanna Boronat","canto_first_approved_date":"2025-01-15 10:52:21","canto_approved_date":"2025-01-23 21:34:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-01-07 12:56:49","canto_added_date":"2023-07-15 00:15:12","annotation_curators":[{"name":"Susanna Boronat","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.13","SPAC1F7.04","SPBC16D10.08c","SPBC1734.11"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2025-01-15"},{"uniquename":"PMID:9407031","title":"Damage and replication checkpoint control in fission yeast is ensured by interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1.","citation":"Genes Dev 1997 Dec 15;11(24):3387-400","abstract":"Fission yeast Cut5/Rad4 plays a unique role in the genome maintenance as it is required for replication, replication checkpoint, and normal UV sensitivity. It is unknown, however, how Cut5 protein is linked to other checkpoint proteins, and what part it plays in replication and UV sensitivity. Here we report that Cut5 interacts with a novel checkpoint protein Crb2 and that this interaction is needed for normal genome maintenance. The carboxyl terminus of Crb2 resembles yeast Rad9 and human 53BP1 and BRCA1. Crb2 is required for checkpoint arrests induced by irradiation and polymerase mutations, but not for those induced by inhibited nucleotide supply. Upon UV damage, Crb2 is transiently modified, probably phosphorylated, with a similar timing of phosphorylation in Chk1 kinase, which is reported to restrain Cdc2 activation. Crb2 modification requires other damage-sensing checkpoint proteins but not Chk1, suggesting that Crb2 acts at the upstream of Chk1. The modified Crb2 exists as a slowly sedimenting form, whereas Crb2 in undamaged cells is in a rapidly sedimenting structure. Cut5 and Crb2 interact with Chk1 in a two-hybrid system. Moreover, moderate overexpression of Chk1 suppresses the phenotypes of cut5 and crb2 mutants. Cut5, Crb2, and Chk1 thus may form a checkpoint sensor-transmitter pathway to arrest the cell cycle.","authors":"Saka Y, Esashi F, Matsusaka T, Mochida S, Yanagida M","authors_abbrev":"Saka Y et al.","pubmed_publication_date":"15 Dec 1997","pubmed_entrez_date":"1998-02-07","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPAC23C4.18c","SPAC13G7.08c","SPAC3H5.06c","SPCC1259.13","SPBC342.05","SPBC336.04"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:40427588","title":"The Insertion Domain of Mti2 Facilitates the Association of Mitochondrial Initiation Factors with Mitoribosomes in  Schizosaccharomyces pombe .","citation":"Biomolecules 2025 May 10;15(5)","abstract":"Translation initiation in mitochondria involves unique mechanisms distinct from those in the cytosol or in bacteria. The  Schizosaccharomyces pombe  mitochondrial translation initiation factor 2 (Mti2) is the ortholog of human MTIF2, which plays a vital role in synthesizing proteins in mitochondria. Here, we investigate the insertion domain of Mti2, which stabilizes its interaction with the ribosome and is crucial for efficient translation initiation. Our results show that the insertion domain is critical for the proper folding and function of Mti2. The absence of the insertion domain disrupts cell growth and affects the expression of genes encoded by mitochondrial DNA. Additionally, we show that Mti2 physically interacts with the small subunits of mitoribosomes (mtSSU), and deletion of the insertion domain dissociates mitochondrial initiation factors from the mitoribosome, reducing the efficiency of mitochondrial translation. Altogether, these findings highlight the conserved role of the insertion domain in facilitating translation initiation in fission yeast and thus reveal shared principles of mitochondrial translation initiation in both fission yeast and humans.","doi":"10.3390/biom15050695","authors":"Luo Y, Bähler J, Huang Y","authors_abbrev":"Luo Y et al.","pubmed_publication_date":"10 May 2025","pubmed_entrez_date":"2025-05-28","publication_year":"2025","canto_session_key":"8fbea0626878ceaa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying  Luo","canto_first_approved_date":"2025-06-11 09:19:28","canto_approved_date":"2026-02-18 09:15:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-10 14:24:26","canto_added_date":"2025-05-28 23:25:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying  Luo","community_curator":true,"annotation_count":41,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.15","SPBC1271.15c","SPMIT.09","SPMIT.10","SPMIT.01","SPBC18E5.13","SPMIT.08","SPMIT.04","SPMIT.05","SPRRNA.02","SPMIT.11","SPAC4F8.02c","SPMIT.07","SPRRNA.01","SPBC1105.03c","SPAC4G9.17c"],"gene_count":16,"ltp_gene_count":3,"approved_date":"2025-06-11"},{"uniquename":"PMID:23355005","title":"Reduction of ribosome level triggers flocculation of fission yeast cells.","citation":"Eukaryot Cell 2013 Mar;12(3):450-9","abstract":"Deletion of ribosomal protein L32 genes resulted in a nonsexual flocculation of fission yeast. Nonsexual flocculation also occurred when two other ribosomal protein genes, rpl21-2 and rpl9-2, were deleted. However, deletion of two nonribosomal protein genes, mpg and fbp, did not cause flocculation. Overall transcript levels of rpl32 in rpl32-1Δ and rpl32-2Δ cells were reduced by 35.9% and 46.9%, respectively, and overall ribosome levels in rpl32-1Δ and rpl32-2Δ cells dropped 31.1% and 27.8%, respectively, compared to wild-type cells. Interestingly, ribosome protein expression levels and ribosome levels were also reduced greatly in sexually flocculating diploid YHL6381/WT (h⁺/h⁻) cells compared to a mixture of YHL6381 (h⁺) and WT (h⁻) nonflocculating haploid cells. Transcriptome analysis indicated that the reduction of ribosomal levels in sexual flocculating cells was caused by more-extensive suppression of ribosomal biosynthesis gene expression, while the reduction of ribosomal levels caused by deleting ribosomal protein genes in nonsexual flocculating cells was due to an imbalance between ribosomal proteins. We propose that once the reduction of ribosomal levels is below a certain threshold value, flocculation is triggered.","doi":"10.1128/EC.00321-12","authors":"Li R, Li X, Sun L, Chen F, Liu Z, Gu Y, Gong X, Liu Z, Wei H, Huang Y, Yuan S","authors_abbrev":"Li R et al.","pubmed_publication_date":"Mar 2013","pubmed_entrez_date":"2013-01-29","publication_year":"2013","canto_session_key":"a245796bce469ae0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12713814","title":"Different frameshift mutation spectra in non-repetitive DNA of MutSalpha- and MutLalpha-deficient fission yeast cells.","citation":"DNA Repair (Amst) 2003 May 13;2(5):571-80","abstract":"A frameshift reversion assay has been established for Schizosaccharomyces pombe, which allows detection of deletions and insertions of nucleotides in a non-repetitive DNA sequence. Compared to wild type, frameshift mutation rates were increased in the mismatch repair (MMR) mutants msh2, msh6, mlh1, and pms1, but not in a swi4 strain (defective in the Msh3 homologue). Rates were also elevated in the DNA nuclease-deficient strains rad2 (defective in the FEN-1 homologue) and exo1. In MutSalpha-deficient strains, msh2 and msh6, most of the reversions were 1bp deletions. In contrast, mlh1 and pms1 mutants, defective in MutLalpha, accumulated significantly more 2bp insertions, preferentially of the type CG to (CG)(2). Such duplications were less frequent in double mutants additionally defective in msh2, msh6, rad2, or exo1. Thus, accumulation of (CG)(2) in MutLalpha-deficient strains depends on the presence of MutSalpha, Rad2 and Exo1.","authors":"Marti TM, Mansour AA, Lehmann E, Fleck O","authors_abbrev":"Marti TM et al.","pubmed_publication_date":"13 May 2003","pubmed_entrez_date":"2003-04-26","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.06c","SPBC29A10.05","SPAC19G12.02c","SPBC1703.04","SPBC19G7.01c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:1855255","title":"Premature initiation of mitosis in yeast lacking RCC1 or an interacting GTPase.","citation":"Cell 1991 Jul 26;66(2):347-60","abstract":"A fission yeast mutant is described in which the onset of mitosis is uncoupled from the completion of DNA replication. pim1 (premature initiation of mitosis) cells can undergo mitotic chromosome condensation and mitotic spindle formation without completion of S phase and without the cdc25 mitotic inducer. The M phase kinase is required for pim1-induced mitosis and becomes activated. pim1 encodes a homolog of the human RCC1 nuclear protein. pim1 mutants are fully rescued by overexpression of spi1, a newly identified essential gene whose predicted product shares 81% identity with human TC4. spi1 and TC4 define a new subclass within the \"ras-like\" GTPase superfamily that is structurally distinct from the ras, rho, or sec4 families. Diploid yeast that carry one wild-type and one disrupted copy of spi1 have multiple satellite nuclei, and mitotic haploidization occurs at very high frequency. spi1 appears to interact with pim1 in the maintenance of a coordinated cell cycle.","authors":"Matsumoto T, Beach D","authors_abbrev":"Matsumoto T et al.","pubmed_publication_date":"26 Jul 1991","pubmed_entrez_date":"1991-07-26","publication_year":"1991","canto_session_key":"e113c7320f53efc5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-07 17:38:06","canto_approved_date":"2020-01-14 17:13:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-28 16:08:51","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC557.03c","SPBC1289.03c","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2015-09-07"},{"uniquename":"PMID:2559092","title":"Nucleoside diphosphokinase, an enzyme with step changes in activity during the cell cycle of the fission yeast Schizosaccharomyces pombe. II. Dissociation of the steps from the DNA-division cycle after induction synchronization.","citation":"J Cell Sci 1989 May;93 ( Pt 1):185-9","abstract":"Synchrony was induced in cultures of the mitotic mutant cdc2.33 of Schizosaccharomyces pombe by shifting up an asynchronous culture to the restrictive temperature for a period of 3.5-4.5 h and then shifting down to the permissive temperature. The resulting synchronous divisions had short cycle times, down to 50% of the normal cycle. The oscillatory control of nucleoside diphosphokinase activity was also synchronized by the shift-down and the activity rose in a step pattern. Unlike the situation in the normal cycle, this step pattern was dissociated from the shortened cell cycle and had a longer period and different phase relations. It may be that the normal entrainment or coupling between the cell cycle and the activity control fails if the cell cycle is too short. The period of the activity control (equal to the protein doubling time at the restrictive temperature) appears to be temperature-compensated.","authors":"Creanor J, Mitchison JM","authors_abbrev":"Creanor J et al.","pubmed_publication_date":"May 1989","pubmed_entrez_date":"1989-05-01","publication_year":"1989","canto_session_key":"db2612d0b960fb71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-03-04 14:32:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-20 10:12:21","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-02-20"},{"uniquename":"PMID:39527189","title":"Dual Luciferase Reporter Assay in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2025;2862:1-6","abstract":"Here, I describe the methods to perform dual luciferase reporter assay in Schizosaccharomyces pombe. The experiment requires the generation of a reporter plasmid construct, with firefly luciferase gene controlled under the genetic element of interest (such as transcriptional promoter or translation initiation signal preceded by a defined promoter) and Renilla luciferase gene expressed under a fixed promoter. S. pombe transformants carrying the plasmids with varied control elements are grown in a selective medium and chilled on ice. Small amounts of cells are pelleted and subjected to the commercially available dual luciferase assay.","doi":"10.1007/978-1-0716-4168-2_1","authors":"Asano K","authors_abbrev":"Asano K","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8314086","title":"The fission yeast mating pheromone P-factor: its molecular structure, gene structure, and ability to induce gene expression and G1 arrest in the mating partner.","citation":"Genes Dev 1994 Feb 01;8(3):328-38","abstract":"Schizosaccharomyces pombe h+ cells secrete a diffusable mating pheromone called P-factor. Here we show that the map2 gene, a defect of which confers h(+)-specific sterility, encodes the precursor of P-factor. We purified P-factor from cells overexpressing map2 and determined its amino acid sequence. P-factor is a peptide of 23 residues, with the sequence Thr-Tyr-Ala-Asp-Phe-Leu-Arg-Ala-Tyr-Gln-Ser- Trp-Asn-Thr-Phe-Val-Asn-Pro-Asp-Arg-Pro-Asn-Leu. A synthetic peptide of this sequence gave the same specific activity and chromatographic profile as the purified P-factor, suggesting that P-factor is unmodified. h- cells starved for nutrition showed a morphological response to P-factor. Transcription of the sxa2 gene, which encodes a protease thought to degrade P-factor, was activated in these cells. The cry1 null mutant, which lacks adenylyl cyclase and has little intracellular cAMP, was susceptible to P-factor even in the presence of nutrients. Combination of the cyr1 and sxa2 mutations enhanced this susceptibility. P-factor induced not only responses toward mating but also arrest of the cell cycle at the G1 phase in h- cyr1 sxa2 cells. This proves that the S. pombe mating pheromone has the ability to arrest cell cycle progression, which has previously been obscured by the usual requirement for mating of nutritional starvation and subsequent growth arrest.","authors":"Imai Y, Yamamoto M","authors_abbrev":"Imai Y et al.","pubmed_publication_date":"01 Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_session_key":"1cfaa3add2d5fd87","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-11 21:13:57","canto_approved_date":"2025-12-12 18:38:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-10 10:16:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC19C7.03","SPCC1795.06","SPBC24C6.06","SPAC1296.03c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-06-11"},{"uniquename":"PMID:12969510","title":"The COG database: an updated version includes eukaryotes.","citation":"BMC Bioinformatics 2003 Sep 11;4:41","abstract":"The availability of multiple, essentially complete genome sequences of prokaryotes and eukaryotes spurred both the demand and the opportunity for the construction of an evolutionary classification of genes from these genomes. Such a classification system based on orthologous relationships between genes appears to be a natural framework for comparative genomics and should facilitate both functional annotation of genomes and large-scale evolutionary studies.\nWe describe here a major update of the previously developed system for delineation of Clusters of Orthologous Groups of proteins (COGs) from the sequenced genomes of prokaryotes and unicellular eukaryotes and the construction of clusters of predicted orthologs for 7 eukaryotic genomes, which we named KOGs after eukaryotic orthologous groups. The COG collection currently consists of 138,458 proteins, which form 4873 COGs and comprise 75% of the 185,505 (predicted) proteins encoded in 66 genomes of unicellular organisms. The eukaryotic orthologous groups (KOGs) include proteins from 7 eukaryotic genomes: three animals (the nematode Caenorhabditis elegans, the fruit fly Drosophila melanogaster and Homo sapiens), one plant, Arabidopsis thaliana, two fungi (Saccharomyces cerevisiae and Schizosaccharomyces pombe), and the intracellular microsporidian parasite Encephalitozoon cuniculi. The current KOG set consists of 4852 clusters of orthologs, which include 59,838 proteins, or approximately 54% of the analyzed eukaryotic 110,655 gene products. Compared to the coverage of the prokaryotic genomes with COGs, a considerably smaller fraction of eukaryotic genes could be included into the KOGs; addition of new eukaryotic genomes is expected to result in substantial increase in the coverage of eukaryotic genomes with KOGs. Examination of the phyletic patterns of KOGs reveals a conserved core represented in all analyzed species and consisting of approximately 20% of the KOG set. This conserved portion of the KOG set is much greater than the ubiquitous portion of the COG set (approximately 1% of the COGs). In part, this difference is probably due to the small number of included eukaryotic genomes, but it could also reflect the relative compactness of eukaryotes as a clade and the greater evolutionary stability of eukaryotic genomes.\nThe updated collection of orthologous protein sets for prokaryotes and eukaryotes is expected to be a useful platform for functional annotation of newly sequenced genomes, including those of complex eukaryotes, and genome-wide evolutionary studies.","authors":"Tatusov RL, Fedorova ND, Jackson JD, Jacobs AR, Kiryutin B, Koonin EV, Krylov DM, Mazumder R, Mekhedov SL, Nikolskaya AN, Rao BS, Smirnov S, Sverdlov AV, Vasudevan S, Wolf YI, Yin JJ, Natale DA","authors_abbrev":"Tatusov RL et al.","pubmed_publication_date":"11 Sep 2003","pubmed_entrez_date":"2003-09-13","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24583182","title":"A novel method for purification of the endogenously expressed fission yeast Set2 complex.","citation":"Protein Expr Purif 2014 May;97:44-9","abstract":"Chromatin-associated proteins are heterogeneously and dynamically composed. To gain a complete understanding of DNA packaging and basic nuclear functions, it is important to generate a comprehensive inventory of these proteins. However, biochemical purification of chromatin-associated proteins is difficult and is accompanied by concerns over complex stability, protein solubility and yield. Here, we describe a new method for optimized purification of the endogenously expressed fission yeast Set2 complex, histone H3K36 methyltransferase. Using the standard centrifugation procedure for purification, approximately half of the Set2 protein separated into the insoluble chromatin pellet fraction, making it impossible to recover the large amounts of soluble Set2. To overcome this poor recovery, we developed a novel protein purification technique termed the filtration/immunoaffinity purification/mass spectrometry (FIM) method, which eliminates the need for centrifugation. Using the FIM method, in which whole cell lysates were filtered consecutively through eight different pore sizes (53-0.8μm), a high yield of soluble FLAG-tagged Set2 was obtained from fission yeast. The technique was suitable for affinity purification and produced a low background. A mass spectrometry analysis of anti-FLAG immunoprecipitated proteins revealed that Rpb1, Rpb2 and Rpb3, which have all been reported previously as components of the budding yeast Set2 complex, were isolated from fission yeast using the FIM method. In addition, other subunits of RNA polymerase II and its phosphatase were also identified. In conclusion, the FIM method is valid for the efficient purification of protein complexes that separate into the insoluble chromatin pellet fraction during centrifugation.","doi":"10.1016/j.pep.2014.02.005","authors":"Suzuki S, Nagao K, Obuse C, Murakami Y, Takahata S","authors_abbrev":"Suzuki S et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2014-03-04","publication_year":"2014","canto_session_key":"22d5a4391544ddaf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-16 11:24:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-02-16 11:24:17","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1105.11c","SPAC23C4.15","SPAC23G3.01","SPAC29B12.02c","SPAC23A1.16c","SPBC28F2.12","SPAC1834.04","SPACUNK4.06c","SPBC337.14","SPBC8D2.04","SPCC1442.10c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2016-02-16"},{"uniquename":"PMID:11166180","title":"Nuclear exclusion of Cdc25 is not required for the DNA damage checkpoint in fission yeast.","citation":"Curr Biol 2001 Jan 09;11(1):50-4","abstract":"Maintenance of genome integrity requires a checkpoint that restrains mitosis in response to DNA damage [1]. This checkpoint is enforced by Chk1, a protein kinase that targets Cdc25 [2--7]. Phosphorylated Cdc25 associates with 14-3-3 proteins, which appear to occlude a nuclear localization signal (NLS) and thereby inhibit Cdc25 nuclear import [6, 8--14]. Proficient checkpoint arrest is thought to require Cdc25 nuclear exclusion, although definitive evidence for this model is lacking. We have tested this hypothesis in fission yeast. We show that elimination of an NLS in Cdc25 causes Cdc25 nuclear exclusion and a mitotic delay, as predicted by the model. Attachment of an exogenous NLS forces nuclear inclusion of Cdc25 in damaged cells. However, forced nuclear localization of Cdc25 fails to override the damage checkpoint. Thus, nuclear exclusion of Cdc25 is unnecessary for checkpoint enforcement. We propose that direct inhibition of Cdc25 phosphatase activity by Chk1, as demonstrated in vitro with fission yeast and human Chk1 [15, 16], is sufficient for proficient checkpoint regulation of Cdc25 and may be the primary mechanism of checkpoint enforcement in fission yeast.","authors":"Lopez-Girona A, Kanoh J, Russell P","authors_abbrev":"Lopez-Girona A et al.","pubmed_publication_date":"09 Jan 2001","pubmed_entrez_date":"2001-02-13","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:38198529","title":"Minimal requirements for the epigenetic inheritance of engineered silent chromatin domains.","citation":"Proc Natl Acad Sci U S A 2024 Jan 16;121(3):e2318455121","abstract":"Mechanisms enabling genetically identical cells to differentially regulate gene expression are complex and central to organismal development and evolution. While gene silencing pathways involving DNA sequence-specific recruitment of histone-modifying enzymes are prevalent in nature, examples of sequence-independent heritable gene silencing are scarce. Studies of the fission yeast  Schizosaccharomyces pombe  indicate that sequence-independent propagation of heterochromatin can occur but requires numerous multisubunit protein complexes and their diverse activities. Such complexity has so far precluded a coherent articulation of the minimal requirements for heritable gene silencing by conventional in vitro reconstitution approaches. Here, we take an unconventional approach to defining these requirements by engineering sequence-independent silent chromatin inheritance in budding yeast  Saccharomyces cerevisiae  cells. The mechanism conferring memory upon these cells is remarkably simple and requires only two proteins, one that recognizes histone H3 lysine 9 methylation (H3K9me) and catalyzes the deacetylation of histone H4 lysine 16 (H4K16), and another that recognizes deacetylated H4K16 and catalyzes H3K9me. Together, these bilingual \"read-write\" proteins form an interdependent positive feedback loop that is sufficient for the transmission of DNA sequence-independent silent information over multiple generations.","doi":"10.1073/pnas.2318455121","authors":"Yuan AH, Moazed D","authors_abbrev":"Yuan AH et al.","pubmed_publication_date":"16 Jan 2024","pubmed_entrez_date":"2024-01-10","publication_year":"2024","canto_session_key":"6c620255b7216586","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-01-11 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20517925","title":"GMF is an evolutionarily developed Adf/cofilin-super family protein involved in the Arp2/3 complex-mediated organization of the actin cytoskeleton.","citation":"Cytoskeleton (Hoboken) 2010 Jun;67(6):373-82","abstract":"Actin-depolymerizing factor (ADF)/cofilin is widely expressed in eukaryotes and plays a central role in reorganizing the actin cytoskeleton by disassembling actin filaments. The ADF-homologous domain (ADF-H) is conserved in several other actin-modulating proteins such as twinfilin, Abp1/drebrin, and coactosin. Although these proteins interact with actin via ADF-H, their effects on actin are not identical to each other. Here, we report a novel ADF/cofilin-super family protein, Gmf1 (Glia maturation factor-like protein 1), from the fission yeast Schizosaccharomyces pombe. Gmf1 is a component of actin patches, which are located on the cell cortex and required for endocytosis, and may be involved in the control of the disassembly of actin patches since its overexpression diminishes them. We provide evidence that Gmf1 binds weakly if at all to actin, but it associates with actin-related protein (Arp) 2/3 complex and suppresses its functions such as the promotion of actin polymerization and branching filaments. Importantly, Arp2/3 complex-suppressing activity is conserved among GMF-family proteins from other organisms. Given the functional plasticity of ADF-H, GMF-family proteins possibly have changed their target from conventional actin to Arps through molecular evolution.","doi":"10.1002/cm.20451","authors":"Nakano K, Kuwayama H, Kawasaki M, Numata O, Takaine M","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-06-03","publication_year":"2010","canto_session_key":"58d4c8cee7e46725","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-20 14:14:10","canto_approved_date":"2022-09-21 18:39:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-08 17:03:27","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.06c","SPAC11H11.06","SPAC6F6.10c","SPAC17H9.11","SPAC17G8.04c","SPAC630.03"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2019-11-20"},{"uniquename":"PMID:15004522","title":"The Cdc48/p97-Ufd1-Npl4 complex: its potential role in coordinating cellular morphogenesis during the M-G1 transition.","citation":"Cell Cycle 2004 Apr;3(4):422-4","abstract":"The AAA ATPase Cdc48/p97 together with its adaptors, Ufd1-Npl4, regulate membrane-related functions and mitotic spindle disassembly by directly binding to membrane-associated proteins or spindle assembly factors, modulating their interactions with membranes or spindles, respectively. Here, we discuss the possibility that the Cdc48/ p97-Ufd1-Npl4 complex has a more general role in mediating morphological transitions as the cell exits mitosis and enters G(1).","authors":"Cao K, Zheng Y","authors_abbrev":"Cao K et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-03-09","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-02-12 01:18:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36413467","title":"Absence of Wee1 alters global transcriptional response to oxidative stress in Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 2022 Nov 25;369(1)","abstract":"Stress response and checkpoint activation are the main determinants of cellular survival in adverse conditions. In Schizosaccharomyces pombe, these are controlled by the Mitogen Activated Protein Kinase Spc1 and the Cyclin dependent Kinase Cdc2 respectively. Cdc2 is regulated positively by Cdc25 and negatively by Wee1. Changes in Cdc2 activity can be sensed by Spc1 resulting in the modulation of mitotic timing by Spc1. Functional cross talks between cell cycle regulation and MAPK machinery during regulation of mitotic timing are well characterised but the presence of similar communication during stress response remains unexplored. In this study we report how the checkpoint activator kinase Wee1 can also influence the transcriptional response to oxidative stress. We show that deletion of Wee1 results in changes in gene expression of the cells, especially with respect to genes whose expression is known to be regulated by Spc1. These differences are seen in unperturbed cells as well as during oxidative stress. Moreover, such variations extend beyond what could be expected to occur due to the known enhanced Spc1 activity of these cells. This is the first depiction of the influence of Wee1 and consequently Cdc2 activity on transcriptional response to oxidative stress.","doi":"10.1093/femsle/fnac110","authors":"Datta S, Ghosal A, Dutta S, Sundaram G","authors_abbrev":"Datta S et al.","pubmed_publication_date":"25 Nov 2022","pubmed_entrez_date":"2022-11-22","publication_year":"2022","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-11-23 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC18B5.03","SPBC887.22"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"EMBL:AU006625","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23963700","title":"Replisome stall events have shaped the distribution of replication origins in the genomes of yeasts.","citation":"Nucleic Acids Res 2013 Nov;41(21):9705-18","abstract":"During S phase, the entire genome must be precisely duplicated, with no sections of DNA left unreplicated. Here, we develop a simple mathematical model to describe the probability of replication failing due to the irreversible stalling of replication forks. We show that the probability of complete genome replication is maximized if replication origins are evenly spaced, the largest inter-origin distances are minimized, and the end-most origins are positioned close to chromosome ends. We show that origin positions in the yeast Saccharomyces cerevisiae genome conform to all three predictions thereby maximizing the probability of complete replication if replication forks stall. Origin positions in four other yeasts-Kluyveromyces lactis, Lachancea kluyveri, Lachancea waltii and Schizosaccharomyces pombe-also conform to these predictions. Equating failure rates at chromosome ends with those in chromosome interiors gives a mean per nucleotide fork stall rate of ∼5 × 10(-8), which is consistent with experimental estimates. Using this value in our theoretical predictions gives replication failure rates that are consistent with data from replication origin knockout experiments. Our theory also predicts that significantly larger genomes, such as those of mammals, will experience a much greater probability of replication failure genome-wide, and therefore will likely require additional compensatory mechanisms.","doi":"10.1093/nar/gkt728","authors":"Newman TJ, Mamun MA, Nieduszynski CA, Blow JJ","authors_abbrev":"Newman TJ et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-08-22","publication_year":"2013","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33534698","title":"Tripartite suppression of fission yeast TORC1 signaling by the GATOR1-Sea3 complex, the TSC complex, and Gcn2 kinase.","citation":"Elife 2021 Feb 03;10","abstract":"Mammalian target of rapamycin complex 1 (TORC1) is controlled by the GATOR complex composed of the GATOR1 subcomplex and its inhibitor, the GATOR2 subcomplex, sensitive to amino acid starvation. Previously, we identified fission yeast GATOR1 that prevents deregulated activation of TORC1 (Chia et al., 2017). Here, we report identification and characterization of GATOR2 in fission yeast. Unexpectedly, the GATOR2 subunit Sea3, an ortholog of mammalian WDR59, is physically and functionally proximal to GATOR1, rather than GATOR2, attenuating TORC1 activity. The fission yeast GATOR complex is dispensable for TORC1 regulation in response to amino acid starvation, which instead activates the Gcn2 pathway to inhibit TORC1 and induce autophagy. On the other hand, nitrogen starvation suppresses TORC1 through the combined actions of the GATOR1-Sea3 complex, the Gcn2 pathway, and the TSC complex, another conserved TORC1 inhibitor. Thus, multiple, parallel signaling pathways implement negative regulation of TORC1 to ensure proper cellular starvation responses.","doi":"10.7554/eLife.60969","authors":"Fukuda T, Sofyantoro F, Tai YT, Chia KH, Matsuda T, Murase T, Morozumi Y, Tatebe H, Kanki T, Shiozaki K","authors_abbrev":"Fukuda T et al.","pubmed_publication_date":"03 Feb 2021","pubmed_entrez_date":"2021-02-03","publication_year":"2021","canto_session_key":"05ebdc773cdd0a9d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomoyuki Fukuda","canto_first_approved_date":"2021-07-09 11:57:12","canto_approved_date":"2024-04-02 17:30:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-28 12:14:25","canto_added_date":"2021-02-05 01:15:06","annotation_curators":[{"name":"Tomoyuki Fukuda","community_curator":true,"annotation_count":64,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":41,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27E2.02","SPAC20G4.03c","SPBC36B7.09","SPAC18G6.05c","SPBC215.15","SPAC23H3.03c","SPBC543.04","SPAC12G12.01c","SPBC337.13c","SPAC630.13c","SPCC11E10.07c","SPAC22F3.13","SPCC1393.08","SPAC11E3.05","SPBC18H10.20c","SPAC15F9.02","SPAC4A8.04","SPCC4G3.08","SPAC222.07c","SPBC29A3.09c","SPBC26H8.04c","SPAC6B12.15","SPAC3G9.09c","SPAC4F8.11"],"gene_count":24,"ltp_gene_count":22,"approved_date":"2021-07-09"},{"uniquename":"PMID:19933844","title":"Fission yeast Iec1-ino80-mediated nucleosome eviction regulates nucleotide and phosphate metabolism.","citation":"Mol Cell Biol 2010 Feb;30(3):657-74","abstract":"Ino80 is an ATP-dependent nucleosome-remodeling enzyme involved in transcription, replication, and the DNA damage response. Here, we characterize the fission yeast Ino80 and find that it is essential for cell viability. We show that the Ino80 complex from fission yeast mediates ATP-dependent nucleosome remodeling in vitro. The purification of the Ino80-associated complex identified a highly conserved complex and the presence of a novel zinc finger protein with similarities to the mammalian transcriptional regulator Yin Yang 1 (YY1) and other members of the GLI-Krüppel family of proteins. Deletion of this Iec1 protein or the Ino80 complex subunit arp8, ies6, or ies2 causes defects in DNA damage repair, the response to replication stress, and nucleotide metabolism. We show that Iec1 is important for the correct expression of genes involved in nucleotide metabolism, including the ribonucleotide reductase subunit cdc22 and phosphate- and adenine-responsive genes. We find that Ino80 is recruited to a large number of promoter regions on phosphate starvation, including those of phosphate- and adenine-responsive genes that depend on Iec1 for correct expression. Iec1 is required for the binding of Ino80 to target genes and subsequent histone loss at the promoter and throughout the body of these genes on phosphate starvation. This suggests that the Iec1-Ino80 complex promotes transcription through nucleosome eviction.","doi":"10.1128/MCB.01117-09","authors":"Hogan CJ, Aligianni S, Durand-Dubief M, Persson J, Will WR, Webster J, Wheeler L, Mathews CK, Elderkin S, Oxley D, Ekwall K, Varga-Weisz PD","authors_abbrev":"Hogan CJ et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2009-11-26","publication_year":"2010","canto_session_key":"f05a121e4791199c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-23 14:53:41","canto_approved_date":"2024-05-21 17:28:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-07 13:41:26","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":96,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25D12.04","SPBC83.08","SPAC222.04c","SPAPB8E5.09","SPBC32H8.12c","SPAC22H12.02","SPAC664.02c","SPAC1F7.05","SPBC1198.02","SPAC144.02","SPAC23A1.03","SPBC365.10","SPCC16C4.20c","SPAC29B12.01","SPBC428.03c","SPBC405.01","SPBP23A10.08","SPAC6B12.05c","SPBP4G3.02","SPCC1259.04","SPAC10F6.08c","SPAC23G3.04"],"gene_count":22,"ltp_gene_count":15,"approved_date":"2018-03-23"},{"uniquename":"PMID:19566341","title":"Noninvasive characterization of the fission yeast cell cycle by monitoring dry mass with digital holographic microscopy.","citation":"J Biomed Opt 2009;14(3):034049","abstract":"Digital holography microscopy (DHM) is an optical technique which provides phase images yielding quantitative information about cell structure and cellular dynamics. Furthermore, the quantitative phase images allow the derivation of other parameters, including dry mass production, density, and spatial distribution. We have applied DHM to study the dry mass production rate and the dry mass surface density in wild-type and mutant fission yeast cells. Our study demonstrates the applicability of DHM as a tool for label-free quantitative analysis of the cell cycle and opens the possibility for its use in high-throughput screening.","doi":"10.1117/1.3147385","authors":"Rappaz B, Cano E, Colomb T, Kühn J, Depeursinge C, Simanis V, Magistretti PJ, Marquet P","authors_abbrev":"Rappaz B et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-02","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22971934","title":"Effects of HIV-1 protease on cellular functions and their potential applications in antiretroviral therapy.","citation":"Cell Biosci 2012 Sep 12;2(1):32","abstract":"Human Immunodeficiency Virus Type 1 (HIV-1) protease inhibitors (PIs) are the most potent class of drugs in antiretroviral therapies. However, viral drug resistance to PIs could emerge rapidly thus reducing the effectiveness of those drugs. Of note, all current FDA-approved PIs are competitive inhibitors, i.e., inhibitors that compete with substrates for the active enzymatic site. This common inhibitory approach increases the likelihood of developing drug resistant HIV-1 strains that are resistant to many or all current PIs. Hence, new PIs that move away from the current target of the active enzymatic site are needed. Specifically, allosteric inhibitors, inhibitors that prohibit PR enzymatic activities through non-competitive binding to PR, should be sought. Another common feature of current PIs is they were all developed based on the structure-based design. Drugs derived from a structure-based strategy may generate target specific and potent inhibitors. However, this type of drug design can only target one site at a time and drugs discovered by this method are often associated with strong side effects such as cellular toxicity, limiting its number of target choices, efficacy, and applicability. In contrast, a cell-based system may provide a useful alternative strategy that can overcome many of the inherited shortcomings associated with structure-based drug designs. For example, allosteric PIs can be sought using a cell-based system without considering the site or mechanism of inhibition. In addition, a cell-based system can eliminate those PIs that have strong cytotoxic effect. Most importantly, a simple, economical, and easy-to-maintained eukaryotic cellular system such as yeast will allow us to search for potential PIs in a large-scaled high throughput screening (HTS) system, thus increasing the chances of success. Based on our many years of experience in using fission yeast as a model system to study HIV-1 Vpr, we propose the use of fission yeast as a possible surrogate system to study the effects of HIV-1 protease on cellular functions and to explore its utility as a HTS system to search for new PIs to battle HIV-1 resistant strains.","doi":"10.1186/2045-3701-2-32","authors":"Yang H, Nkeze J, Zhao RY","authors_abbrev":"Yang H et al.","pubmed_publication_date":"12 Sep 2012","pubmed_entrez_date":"2012-09-14","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16823445","title":"Selective elimination of messenger RNA prevents an incidence of untimely meiosis.","citation":"Nature 2006 Jul 06;442(7098):45-50","abstract":"Much remains unknown about the molecular regulation of meiosis. Here we show that meiosis-specific transcripts are selectively removed if expressed during vegetative growth in fission yeast. These messenger RNAs contain a cis-acting region--which we call the DSR--that confers this removal via binding to a YTH-family protein Mmi1. Loss of Mmi1 function severely impairs cell growth owing to the untimely expression of meiotic transcripts. Microarray analysis reveals that at least a dozen such meiosis-specific transcripts are eliminated by the DSR-Mmi1 system. Mmi1 remains in the form of multiple nuclear foci during vegetative growth. At meiotic prophase these foci precipitate to a single focus, which coincides with the dot formed by the master meiosis-regulator Mei2. A meiotic arrest due to the loss of the Mei2 dot is released by a reduction in Mmi1 activity. We propose that Mei2 turns off the DSR-Mmi1 system by sequestering Mmi1 to the dot and thereby secures stable expression of meiosis-specific transcripts.","authors":"Harigaya Y, Tanaka H, Yamanaka S, Tanaka K, Watanabe Y, Tsutsumi C, Chikashige Y, Hiraoka Y, Yamashita A, Yamamoto M","authors_abbrev":"Harigaya Y et al.","pubmed_publication_date":"06 Jul 2006","pubmed_entrez_date":"2006-07-11","publication_year":"2006","canto_session_key":"1bde96e4328928bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-04-19 10:42:41","canto_approved_date":"2026-04-24 14:07:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-01-09 17:30:41","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":50,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.03","SPAC27D7.03c","SPBC428.07","SPAC6G9.13c","SPAC6B12.16","SPCC70.09c","SPAC27D7.13c","SPBC2G2.09c","SPCC736.12c","SPAC17A5.18c","SPAC1556.06","SPBC29A10.14","SPNCRNA.103","SPBC32H8.11","SPBC29A10.02","SPAC458.04c","SPAC1F3.01"],"gene_count":17,"ltp_gene_count":5,"approved_date":"2017-04-19"},{"uniquename":"PMID:17244888","title":"Propping up our knowledge of G protein signaling pathways: diverse functions of putative noncanonical Gbeta subunits in fungi.","citation":"Sci STKE 2007 Jan 23;2007(370):pe3","abstract":"Heterotrimeric guanine nucleotide-binding proteins, composed of Galpha, Gbeta, and Ggamma subunits, are important mediators of fungal pheromone and nutrient signaling pathways. Most fungal genomes encode two or three functionally distinct Galpha subunits but only a single canonical Gbeta subunit, which does not bind multiple Galpha subunits. Studies in Saccharomyces cerevisiae, Cryptococcus neoformans, and Schizosaccharomyces pombe have identified binding partners for Galpha subunits, which are proposed to be \"noncanonical Gbeta subunits.\" This Perspective reviews these studies, summarizing the strengths and weaknesses of the claims to this designation for these four fungal proteins.","authors":"Hoffman CS","authors_abbrev":"Hoffman CS","pubmed_publication_date":"23 Jan 2007","pubmed_entrez_date":"2007-01-25","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41161311","title":"Dcr1 senses R-loops for RNAPII termination at sites of replication stress and repair pathway choice.","citation":"Mol Cell 2025 Oct 28;","abstract":"Stalled RNA polymerase II (RNAPII) threatens genome integrity, yet how cells resolve transcription blocks at difficult-to-terminate sites is unclear. Leveraging the compact genome of fission yeast and termination defects associated with the non-canonical function of Dcr1, we unravel the recognition and release mechanisms of stalled RNAPII. Through dual recognition, Dcr1 senses the difficult-to-terminate context-stalled RNAPII and accumulated R-loops-and recruits the termination factor Dhp1 to ensure efficient RNAPII release. Failure of this mechanism causes termination defects that impede replication forks, necessitating DNA polymerase delta (DNAPδ)-mediated replication fork restart at stalled sites. Moreover, Dcr1 promotes genome stability by repurposing its hybrid-recognition ability to engage Rad51, thereby biasing DNA repair toward high-fidelity homologous recombination. Our work defines a key chromatin context and mechanisms governing RNAPII termination, establishing Dcr1 as a molecular hub that directly couples the fidelity of transcription termination to the stability of the genome during replication and repair.","doi":"10.1016/j.molcel.2025.10.004","authors":"Wang Z, Zhang Y, Guo T, He M, Xu Y, Bhattacharjee S, Martienssen RA, Ren J","authors_abbrev":"Wang Z et al.","pubmed_publication_date":"28 Oct 2025","pubmed_entrez_date":"2025-10-29","publication_year":"2025","canto_session_key":"6d16c3b2893aabd0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-31 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15659641","title":"The functionally conserved nucleoporins Nup124p from fission yeast and the human Nup153 mediate nuclear import and activity of the Tf1 retrotransposon and HIV-1 Vpr.","citation":"Mol Biol Cell 2005 Apr;16(4):1823-38","abstract":"We report that the fission yeast nucleoporin Nup124p is required for the nuclear import of both, retrotransposon Tf1-Gag as well as the retroviral HIV-1 Vpr. Failure to import Tf1-Gag into the nucleus in a nup124 null mutant resulted in complete loss of Tf1 transposition. Similarly, nuclear import of HIV-1 Vpr was impaired in nup124 null mutant strains and cells became resistant to Vpr's cell-killing activity. On the basis of protein domain similarity, the human nucleoporin Nup153 was identified as a putative homolog of Nup124p. We demonstrate that in vitro-translated Nup124p and Nup153 coimmunoprecipitate Tf1-Gag or HIV-1 Vpr. Though full-length Nup153 was unable to complement the Tf1 transposition defect in a nup124 null mutant, we provide evidence that both nucleoporins share a unique N-terminal domain, Nup124p(AA264-454) and Nup153(AA448-634) that is absolutely essential for Tf1 transposition. Epigenetic overexpression of this domain in a wild-type (nup124(+)) background blocked Tf1 activity implying that sequences from Nup124p and the human Nup153 challenged the same pathway affecting Tf1 transposition. Our results establish a unique relationship between two analogous nucleoporins Nup124p and Nup153 wherein the function of a common domain in retrotransposition is conserved.","authors":"Varadarajan P, Mahalingam S, Liu P, Ng SB, Gandotra S, Dorairajoo DS, Balasundaram D","authors_abbrev":"Varadarajan P et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-01-22","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.04c","HGNC:8062"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:31488849","title":"Roles for DNA polymerase δ in initiating and terminating leading strand DNA replication.","citation":"Nat Commun 2019 Sep 05;10(1):3992","abstract":"Most current evidence indicates that DNA polymerases ε and δ, respectively, perform the bulk of leading and lagging strand replication of the eukaryotic nuclear genome. Given that ribonucleotide and mismatch incorporation rates by these replicases influence somatic and germline patterns of variation, it is important to understand the details and exceptions to this overall division of labor. Using an improved method to map where these replicases incorporate ribonucleotides during replication, here we present evidence that DNA polymerase δ universally participates in initiating leading strand synthesis and that nascent leading strand synthesis switches from Pol ε to Pol δ during replication termination. Ribonucleotide maps from both the budding and fission yeast reveal conservation of these processes. These observations of replisome dynamics provide important insight into the mechanisms of eukaryotic replication and genome maintenance.","doi":"10.1038/s41467-019-11995-z","authors":"Zhou ZX, Lujan SA, Burkholder AB, Garbacz MA, Kunkel TA","authors_abbrev":"Zhou ZX et al.","pubmed_publication_date":"05 Sep 2019","pubmed_entrez_date":"2019-09-07","publication_year":"2019","canto_session_key":"9bcc96b9d033a443","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-09-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"TreeFam:TF103009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16C4.22","YBR278W","HGNC:18755"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34496258","title":"Transcription and chromatin-based surveillance mechanism controls suppression of cryptic antisense transcription.","citation":"Cell Rep 2021 Sep 07;36(10):109671","abstract":"Phosphorylation of the RNA polymerase II C-terminal domain Y 1 S 2 P 3 T 4 S 5 P 6 S 7  consensus sequence coordinates key events during transcription, and its deregulation leads to defects in transcription and RNA processing. Here, we report that the histone deacetylase activity of the fission yeast Hos2/Set3 complex plays an important role in suppressing cryptic initiation of antisense transcription when RNA polymerase II phosphorylation is dysregulated due to the loss of Ssu72 phosphatase. Interestingly, although single Hos2 and Set3 mutants have little effect, loss of Hos2 or Set3 combined with ssu72Δ results in a synergistic increase in antisense transcription globally and correlates with elevated sensitivity to genotoxic agents. We demonstrate a key role for the Ssu72/Hos2/Set3 mechanism in the suppression of cryptic antisense transcription at the 3' end of convergent genes that are most susceptible to these defects, ensuring the fidelity of gene expression within dense genomes of simple eukaryotes.","doi":"10.1016/j.celrep.2021.109671","authors":"Heo DH, Kuś K, Grzechnik P, Tan-Wong SM, Birot A, Kecman T, Nielsen S, Zenkin N, Vasiljeva L","authors_abbrev":"Heo DH et al.","pubmed_publication_date":"07 Sep 2021","pubmed_entrez_date":"2021-09-08","publication_year":"2021","canto_session_key":"be272cabbd73a555","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-09-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC146.07","SPBC16G5.14c","SPAP14E8.02","SPBC16H5.12c","SPAC31G5.17c","SPAC4A8.13c","SPAC12G12.04","SPAC23H4.06","SPAC926.09c","SPAC29A4.04c","SPAC22F8.06","SPAC959.08","SPCC1235.05c","SPAC1071.10c","SPBC3B9.19","SPAC1F3.06c","SPAC589.10c","SPBC646.16","SPBC23G7.12c","SPBC146.09c","SPBP35G2.07","SPBC16H5.10c","SPAC29E6.08","SPCC338.08","SPAC17G6.13","SPAC926.04c","SPACUNK4.07c","SPCC364.03","SPAC4A8.11c","SPBC13G1.02","SPAC607.05","SPAC27F1.09c","SPAC17C9.03","SPAC1527.03","SPAC3H5.10","SPAP8A3.12c","SPAC57A7.10c","SPAC16.02c","SPAC6G10.04c","SPBC16G5.05c","SPAC3G9.07c","SPBC646.11","SPBC776.09","SPBP22H7.08","SPAC1F7.04","SPCC16A11.16c","SPBC3H7.15","SPAC10F6.03c","SPCC622.18","SPAC9E9.07c","SPAC1071.07c","SPCC1259.07","SPAC23C4.15","SPCC576.08c","SPBC3D6.06c","SPBC17A3.04c","SPBC685.07c","SPAC22E12.07","SPBC16E9.12c","SPAC23H3.09c","SPCC576.11","SPAC521.05","SPAC3H5.12c","SPCC613.06","SPCC1322.15","SPAC22G7.06c","SPAC23D3.07","SPAC19A8.15","SPAC1687.22c","SPCC1682.10","SPAC926.08c","SPAC227.07c","SPAC27D7.07c","SPAC16E8.06c","SPAC6G9.09c","SPBC800.05c","SPCC576.09","SPBC56F2.02","SPBC32H8.12c","SPBC1A4.08c","SPAC323.02c","SPBC1105.02c","SPAC11E3.15","SPCC1906.01","SPBC11C11.08","SPAC1687.06c","SPBC16C6.11","SPAC25G10.05c","SPCC613.05c","SPBC17G9.07","SPAC19G12.06c","SPCC1919.09","SPAC4H3.10c","SPBC337.05c","SPAC1F7.05","SPBPJ4664.04","SPAC1834.03c","SPBC3H7.03c","SPBC1685.10","SPAC6B12.15","SPBC4F6.18c","SPBC530.06c","SPAC3G9.04","SPCC736.15","SPBC119.01","SPBC30D10.13c","SPCC622.09","SPAC1783.05","SPBC18E5.04","SPCC74.05","SPBC660.15","SPBC32F12.11","SPAC8E11.02c","SPAC18G6.14c","SPAC21E11.08","SPAC26H5.10c","SPBC106.06","SPAC31G5.13","SPAC17A5.03","SPCC24B10.09","SPAC17G6.06","SPAC2F3.09","SPBC660.16","SPAC1783.08c","SPAC29A4.08c","SPBC11C11.07","SPBC409.06","SPAC750.01","SPAC25G10.08","SPBC29A3.04","SPCC1183.08c","SPAC21E11.03c","SPBC1A4.02c","SPBC29B5.03c","SPAC1834.04","SPAC13G7.02c","SPAC3G9.09c","SPBC17G9.09","SPAC513.01c","SPAC4G9.16c","SPBC16H5.07c","SPBC18H10.14","SPAC694.02","SPCC962.06c","SPAC13G6.02c","SPAC1D4.04","SPBC106.18","SPCC297.03","SPAC32A11.04c","SPCC11E10.08","SPBC530.10c","SPBC1711.12","SPBC1711.06","SPAC806.03c","SPBC29A3.12","SPCP31B10.08c","SPAC1805.13","SPCC1393.03","SPBC16H5.02","SPAC890.08","SPAC17A2.09c","SPBC1734.11","SPAC513.05","SPAC1834.02","SPAC31A2.04c","SPCC576.10c","SPCC1322.05c","SPCC417.08","SPBC11G11.03","SPAPB17E12.13","SPAC23G3.01","SPAC22E12.19","SPBC8D2.06","SPAPJ698.02c","SPBC12D12.03","SPAC22A12.15c","SPCC1223.05c","SPCC1223.08c","SPAC3H5.07","SPAC959.07","SPBC646.07c","SPBC18H10.03","SPCC18.14c","SPAC22E12.11c","SPCC1235.09","SPBC146.14c","SPAC4D7.05","SPAP7G5.05","SPAC26A3.07c","SPAC9G1.12","SPBC1773.12","SPBC31F10.06c","SPBC577.10","SPBC685.06","SPAC23C11.11","SPBC1734.16c","SPAC22H12.04c","SPCC1322.04","SPBC4B4.09","SPCC1682.16","SPBP8B7.06","SPAC15E1.03","SPCC576.03c","SPAC140.02","SPAC1751.03","SPAC24C9.12c","SPBC660.11","SPCC794.07","SPCC1442.10c","SPAC3G6.01","SPBC11B10.10c","SPBC25H2.02","SPBC83.02c","SPBC19F8.08","SPBC36.05c","SPAC3C7.11c","SPBC1709.15c","SPBC646.02","SPAC16E8.15","SPAC328.10c","SPAC1834.01","SPBC106.16","SPBC19F5.04","SPBC2D10.10c","SPBC839.13c","SPAC22E12.13c","SPBC17D11.05","SPAC4F10.10c","SPAC222.12c","SPAC14C4.14","SPBC1815.01","SPBC30B4.02c","SPBC2D10.15c","SPCC1739.13","SPAC328.03","SPCC1795.04c","SPBC839.15c","SPAC139.04c","SPBC16C6.07c","SPBC56F2.12","SPBC839.05c","SPAC1565.08","SPAC11H11.06","SPAPB1E7.12","SPCC13B11.01","SPBC14F5.05c","SPCC1827.03c","SPCC1795.11","SPAC17A5.15c","SPBC2F12.14c","SPBC4C3.07","SPAC16C9.06c","SPBC13G1.01c","SPAC23G3.11","SPBC17D11.07c","SPBC1921.01c","SPAC6F6.07c","SPBC25H2.12c","SPBP8B7.03c","SPAC17A2.13c","SPAC17A2.02c","SPAC22E12.18","SPCPB16A4.05c","SPAC9E9.09c","SPAC1805.11c","SPAC26F1.06","SPBC1703.07","SPAC15E1.04","SPAC664.05","SPBC1709.05","SPBC30D10.18c","SPAC2E1P3.04","SPBP19A11.03c","SPAC56E4.04c","SPBC18H10.12c","SPBC12C2.10c","SPCC5E4.07","SPBC776.11","SPAC16E8.10c","SPAC9G1.03c","SPAC4F8.12c","SPBC21B10.10","SPAC1F8.07c","SPBC2F12.04","SPAC1420.02c"],"gene_count":285,"ltp_gene_count":5},{"uniquename":"PMID:12501321","title":"Characterization of multicopy suppressor genes that complement a defect in the Wis1-Sty1 MAP kinase cascade involved in stress responses in Schizosaccharomyces pombe.","citation":"J Gen Appl Microbiol 1997 Aug;43(4):209-215","abstract":"The Wis1-Sty1 mitogen-activated protein (MAP) kinase cascade is one of the major signaling systems involved in a wide range of stress responses in Schizosaccharomyces pombe. It is known that Deltawis1 and Deltasty1 mutants exhibit highly pleiotropic phenotypes, including a phenotype of temperature sensitivity for growth. In this study, we screened multicopy suppressor genes that allow both the Deltawis1 and Deltasty1 mutants to grow simultaneously at a non-permissive temperature, 37 degrees C. Two such multicopy suppressors were cloned and characterized as sds23(+) and hxk2(+) genes. The former is known to specify a protein that functions as a multicopy suppressor for mutations of the PP1 protein phosphatase and the 20S cyclosome/anaphase-promoting complex (APC), and the latter encodes hexokinase 2. It was revealed that the multicopy sds231 gene restored a defect in the mating efficiency caused by the Deltawis1 and Deltasty1 mutations, whereas the multicopy hxk2(+) gene suppressed a phenotype of heat-shock sensitivity for growth of these mutant cells. These findings are discussed with special reference to the Wis1-Sty1 MAP kinase signaling pathway in S. pombe.","authors":"Yamada H, Ohmiya R, Yamamoto E, Aiba H, Mizuno T","authors_abbrev":"Yamada H et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9404154","title":"[Cell cycle switch from mitotic to meiotic in fission yeast: critical role for an RNA-binding protein].","citation":"Tanpakushitsu Kakusan Koso 1997 Dec;42(16):2581-9","abstract":"","authors":"Watanabe Y, Yamamoto M","authors_abbrev":"Watanabe Y et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1997-12-24","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34157021","title":"An enhancer screen identifies new suppressors of small-RNA-mediated epigenetic gene silencing.","citation":"PLoS Genet 2021 Jun;17(6):e1009645","abstract":"Small non-protein coding RNAs are involved in pathways that control the genome at the level of chromatin. In Schizosaccharomyces pombe, small interfering RNAs (siRNAs) are required for the faithful propagation of heterochromatin that is found at peri-centromeric repeats. In contrast to repetitive DNA, protein-coding genes are refractory to siRNA-mediated heterochromatin formation, unless siRNAs are expressed in mutant cells. Here we report the identification of 20 novel mutant alleles that enable de novo formation of heterochromatin at a euchromatic protein-coding gene by using trans-acting siRNAs as triggers. For example, a single amino acid substitution in the pre-mRNA cleavage factor Yth1 enables siRNAs to trigger silent chromatin formation with unparalleled efficiency. Our results are consistent with a kinetic nascent transcript processing model for the inhibition of small-RNA-directed de novo formation of heterochromatin and lay a foundation for further mechanistic dissection of cellular activities that counteract epigenetic gene silencing.","doi":"10.1371/journal.pgen.1009645","authors":"Shimada Y, Carl SH, Skribbe M, Flury V, Kuzdere T, Kempf G, Bühler M","authors_abbrev":"Shimada Y et al.","pubmed_publication_date":"Jun 2021","pubmed_entrez_date":"2021-06-22","publication_year":"2021","canto_session_key":"4ca761d6d8878091","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-24 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12109160","title":"Isolation and characterization of fission yeast genes involved in transcription regulation of cell cycle events (a short communication).","citation":"Acta Microbiol Immunol Hung 2002;49(2-3):285-7","abstract":"","authors":"Szilágyi Z, Grallert A, Zilahi E, Sipiczki M","authors_abbrev":"Szilágyi Z et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-07-12","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8621436","title":"A conditional lethal mutant in the fission yeast 26 S protease subunit mts3+ is defective in metaphase to anaphase transition.","citation":"J Biol Chem 1996 Mar 08;271(10):5704-11","abstract":"We have isolated a conditional lethal mutant mts3 in the fission yeast Schizosaccharomyces pombe which at the permissive temperature is resistant to the mitotic poison MBC and at the restrictive temperature is defective in metaphase to anaphase transition. The predicted amino acid sequence of mts3+ is 36% identical with the budding yeast gene NIN1. NIN1 cloned into a fission yeast expression vector can rescue both mts3 temperature-sensitive and null alleles demonstrating that NIN1 is the budding yeast homologue of the fission yeast mts3+ gene. The phenotype of the mts3 null is identical with the mts3 ts mutant demonstrating that the phenotype of the mts3 ts mutant is due to loss of mts3+ function. The deduced amino acid sequences of both mts3+ and NIN1 show homology to peptide sequences obtained from subunit 14 of the 26 S protease purified from bovine or human cells.","authors":"Gordon C, McGurk G, Wallace M, Hastie ND","authors_abbrev":"Gordon C et al.","pubmed_publication_date":"08 Mar 1996","pubmed_entrez_date":"1996-03-08","publication_year":"1996","canto_session_key":"1b2540a523d29b62","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-22 16:52:59","canto_approved_date":"2026-01-29 11:51:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-22 16:52:51","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC4.07c","SPBC16G5.01","SPBC11B10.09","SPAC24H6.05"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2018-03-22"},{"uniquename":"PMID:2543188","title":"The phosphoglycerate mutases.","citation":"Adv Enzymol Relat Areas Mol Biol 1989;62:227-313","abstract":"The phosphoglycerate mutase family is generally very well documented with respect to structure, evolution, and mode of action. However, a few individuals in the family remain relatively poorly characterized and will clearly require more detailed study. Furthermore, certain aspects of the detailed behavior of these enzymes are, as yet, incompletely understood and require further investigation. Cofactor-dependent monophosphoglycerate mutase and bisphosphoglycerate mutase are undoubtedly very closely related. Their amino acid sequences are strongly similar, they can form active heterodimers, and they catalyze the same three reactions, albeit at substantially different relative rates. Both enzymes catalyze a ping-pong type of reaction with a phosphohistidine intermediate. The presence of an additional phospho ligand at the active site of monophosphoglycerate mutase helps to explain why this enzyme is better at retaining the 2,3-bisphosphoglycerate intermediate and why it is thus more efficient (by a factor of about 10(3)) at catalyzing the interconversion of 3- and 2-phosphoglycerates. The reason why 1,3-bisphosphoglycerate is a better substrate for bisphosphoglycerate mutase than for monophosphoglycerate mutase (by a factor of about 30) is not yet apparent but presumably relates to the relative positioning of the two phospho-binding sites. Both enzymes are equally good as phosphatases when the reaction is activated by 2-phosphoglycollate. Available evidence indicates that these mutases are similar in many respects to the much smaller, cofactor-dependent monophosphoglycerate mutase from Schizosaccharomyces pombe, but further information is required to define the relationship more precisely. Cofactor-independent monophosphoglycerate mutase belongs to a quite distinct branch of the phosphoglycerate mutase family. It is not known at present whether this branch is related divergently or convergently to the cofactor-dependent monophosphoglycerate mutase/bisphosphoglycerate mutase branch. Existing evidence can be argued both ways. For example, the kinetic evidence shows a ping-pong type of reaction and would be consistent with a phosphohistidine intermediate as encountered in the other mutases. Thus the cofactor-independent enzyme may also have arisen by gene duplication--but, in this case, yielding an enzyme of about twice the size, with slightly different residues at the active site and C-terminal tail. An alternative possibility, of course, is that the two branches of the phosphoglycerate mutase family are quite unrelated in a divergent sense and are little more similar structurally than is, for example, the catalytically similar enzyme phosphoglucomutase.(ABSTRACT TRUNCATED AT 400 WORDS)","authors":"Fothergill-Gilmore LA, Watson HC","authors_abbrev":"Fothergill-Gilmore LA et al.","pubmed_publication_date":"1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22974300","title":"RNA as a structural and regulatory component of the centromere.","citation":"Annu Rev Genet 2012;46:443-53","abstract":"Despite many challenges, great progress has been made in identifying kinetochore proteins and understanding their overall functions relative to spindles and centromeric DNA. In contrast, less is known about the specialized centromeric chromatin environment and how it may be involved in regulating the assembly of kinetochore proteins. Multiple independent lines of evidence have implicated transcription and the resulting RNA as an important part of this process. Here, we summarize recent literature demonstrating the roles of centromeric RNA in regulating kinetochore assembly and maintenance. We also review literature suggesting that the process of centromeric transcription may be as important as the resulting RNA and that such transcription may be involved in recruiting the centromeric histone variant CENH3.","doi":"10.1146/annurev-genet-110711-155419","authors":"Gent JI, Dawe RK","authors_abbrev":"Gent JI et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-09-15","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23071723","title":"DNA polymerase α (swi7) and the flap endonuclease Fen1 (rad2) act together in the S-phase alkylation damage response in S. pombe.","citation":"PLoS One 2012;7(10):e47091","abstract":"Polymerase α is an essential enzyme mainly mediating Okazaki fragment synthesis during lagging strand replication. A specific point mutation in Schizosaccharomyces pombe polymerase α named swi7-1, abolishes imprinting required for mating-type switching. Here we investigate whether this mutation confers any genome-wide defects. We show that the swi7-1 mutation renders cells hypersensitive to the DNA damaging agents methyl methansulfonate (MMS), hydroxyurea (HU) and UV and incapacitates activation of the intra-S checkpoint in response to DNA damage. In addition we show that, in the swi7-1 background, cells are characterized by an elevated level of repair foci and recombination, indicative of increased genetic instability. Furthermore, we detect novel Swi1-, -Swi3- and Pol α- dependent alkylation damage repair intermediates with mobility on 2D-gel that suggests presence of single-stranded regions. Genetic interaction studies showed that the flap endonuclease Fen1 works in the same pathway as Pol α in terms of alkylation damage response. Fen1 was also required for formation of alkylation- damage specific repair intermediates. We propose a model to explain how Pol α, Swi1, Swi3 and Fen1 might act together to detect and repair alkylation damage during S-phase.","doi":"10.1371/journal.pone.0047091","authors":"Koulintchenko M, Vengrova S, Eydmann T, Arumugam P, Dalgaard JZ","authors_abbrev":"Koulintchenko M et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-10-17","publication_year":"2012","canto_session_key":"9d8e022526960ee2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-03-21 12:10:41","canto_approved_date":"2018-03-21 12:10:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-03-21 12:10:35","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":38,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC3G6.06c","SPBC216.06c","SPAC688.10","SPAPB24D3.04c","SPBC30D10.04","SPAC3H5.06c","SPBC3E7.08c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-03-21"},{"uniquename":"PMID:13760","title":"Ammonia assimilation in the fission yeast Schizosaccharomyces pombe 972.","citation":"Arch Microbiol 1977 Jan 11;111(3):265-70","abstract":"Glutamine synthetase (GS) activity of Schizosaccharomyces pombe 972 was high in ammonia-limited cultures, low in phosphate- and sulphate-limited cultures and not detected in glucose-limited cultures. When ammonia was 'pulsed' into an ammonia-limited culture then GS activity decreased at a rate faster than that calculated if enzyme synthesis ceased and enzyme was diluted out by growth. Enzyme activity increased in ammonia-starved, phosphate-limited cultures and in the ammonia 'pulse' system when the added ammonia had been utilised. These increases in enzyme activity were prevented by the presence of 100 mug/ml cycloheximide. GS activity was inversely related to the intracellular concentration of glutamate.","authors":"van Andel JG, Brown CM","authors_abbrev":"van Andel JG et al.","pubmed_publication_date":"11 Jan 1977","pubmed_entrez_date":"1977-01-11","publication_year":"1977","canto_session_key":"570d1c355086e254","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-11-30 15:43:11","canto_approved_date":"2021-10-01 07:03:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-22 15:41:43","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H4.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-11-30"},{"uniquename":"PMID:8698653","title":"Characterization of the heterologous invertase produced by Schizosaccharomyces pombe from the SUC2 gene of Saccharomyces cerevisiae.","citation":"J Appl Bacteriol 1996 Jan;80(1):45-52","abstract":"In order to gain information on the ability of Schizosaccharomyces pombe to process heterologous glycoproteins, the heterologous invertase, obtained from the expression in Schiz. pombe of the SUC2 gene of Saccharomyces cerevisiae, was characterized. In Schiz. pombe the heterologous invertase is secreted into the cell wall and seems to be firmly bound to this structure. After the isolation of the heterologous invertase the study of its enzymatic characteristics revealed that it is more similar to the Sacch. cerevisiae external invertase than to the Schiz. pombe invertase. However, it is glycosylated like the Schiz. pombe invertase since it reacts with the lectin from Bandeiraea simplicifolia seeds conjugated to fluorescein isothiocyanate, which indicates the presence of terminal galactose residues in the enzyme. Moreover, the presence of galactose in the heterologous invertase has been confirmed after analysis of the sugars present in its carbohydrate moiety by gas liquid chromatography.","authors":"Zárate V, Belda F","authors_abbrev":"Zárate V et al.","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"f10454ff1b33d095","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-18 08:37:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-18 08:37:33","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-04-18"},{"uniquename":"PMID:27308471","title":"Dicer in action at replication-transcription collisions.","citation":"Mol Cell Oncol 2015;2(3):e991224","abstract":"Maintaining genome stability at sites of transcription and replication collision is a major challenge to cells. Recently, we have shown that in Schizosaccharomyces pombe Dicer promotes transcription termination at these sites, facilitating DNA replication and preventing replication fork restart that would otherwise occur via homologous recombination at the expense of genome stability. This novel role of Dicer could further explain its previously described role as a tumor suppressor.","doi":"10.4161/23723556.2014.991224","authors":"Ren J, Castel SE, Martienssen RA","authors_abbrev":"Ren J et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2016-06-17","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-06-18 00:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12363027","title":"Differential display analysis of gene expression in yeast.","citation":"Cell Mol Life Sci 2002 Aug;59(8):1241-5","abstract":"RNA differential display (DD) is a powerful and straightforward method that employs random reverse-transcription polymerase chain reaction amplification of mRNA species with electrophoresis for comparative analysis of two or more transcriptomes. The small yeast genome represents a convenient model for studying basic functions of the eukaryotic genome and simultaneously provides valuable information towards further refinement of this technique. Several examples discussed below illustrate how DD coupled with classical yeast genetic approaches may be used for studying transcriptionally regulated genetic systems.","authors":"Ivanova AV, Ivanov SV","authors_abbrev":"Ivanova AV et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-10-05","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5653141","title":"Mechanism of regeneration of yeast protoplasts. V. Formation of the cell wall in Schizosaccharomyces pombe.","citation":"Folia Biol (Praha) 1968;14(1):80-5","abstract":"","authors":"Necas O, Svoboda A, Havelková M","authors_abbrev":"Necas O et al.","pubmed_publication_date":"1968","pubmed_entrez_date":"1968-01-01","publication_year":"1968","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21235504","title":"Cell integrity signaling and response to stress in fission yeast.","citation":"Curr Protein Pept Sci 2010 Dec;11(8):680-92","abstract":"Cellular responses to external signals are regulated by conserved mitogen-activated protein (MAP) kinase signaling cascades. These pathways are triggered by a vast range of stimuli. They phosphorylate numerous proteins, produce significant changes in the gene expression, and regulate diverse processes ranging from proliferation and differentiation to apoptosis in all eukaryotic cells. Three conserved MAP kinase signaling pathways have been identified in the fission yeast Schizosaccharomyces pombe. In this article, we present an overview of two of those pathways that regulate the response of fission yeast to stress and maintain cell integrity. The structure of these signaling modules and the function of the pathways, including the regulation by endogenous inhibitors, are discussed.","authors":"Pérez P, Cansado J","authors_abbrev":"Pérez P et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2011-01-18","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39675008","title":"Protocol to compare relative protein-liposome binding affinity using a fluorescence microscopy-based approach.","citation":"STAR Protoc 2024 Dec 14;6(1):103507","abstract":"Centrifugation-based protein-liposome assays are unsuitable for spontaneously precipitating proteins and have limited quantification capabilities. Here, we present a protocol to compare relative protein-liposome binding affinity using a fluorescence microscopy-based approach. We described steps for fluorescent liposome preparation, fission yeast protein extraction, liposome binding assay, and confocal imaging. We also provided analysis methods for different setups. Although this protocol is established for fission yeast, it can be applied to most non-transmembrane proteins obtained from various in vivo and in vitro systems. For complete details on the use and execution of this protocol, please refer to Hoh et al. 1 .","doi":"10.1016/j.xpro.2024.103507","authors":"Hoh KL, Zhang D","authors_abbrev":"Hoh KL et al.","pubmed_publication_date":"14 Dec 2024","pubmed_entrez_date":"2024-12-15","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-12-17 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9353247","title":"Regulation of the replication initiator protein p65cdc18 by CDK phosphorylation.","citation":"Genes Dev 1997 Nov 01;11(21):2767-79","abstract":"Cyclin-dependent kinases (CDKs) promote the initiation of DNA replication and prevent reinitiation before mitosis, presumably through phosphorylation of key substrates at origins of replication. In fission yeast, the p65cdc18 protein is required to initiate DNA replication and interacts with the origin recognition complex (ORC) and the p34cdc2 CDK. Here we report that p65cdc18 becomes highly phosphorylated as cells undergo the G1 --> S phase transition. This modification is dependent on p34cdc2 protein kinase activity, as well as six consensus CDK phosphorylation sites within the p65cdc18 polypeptide. Genetic interactions between cdc18+ and the S-phase cyclin cig2+ suggest that CDK-dependent phosphorylation antagonizes cdc18+ function in vivo. Using site-directed mutagenesis, we show that phosphorylation at CDK consensus sites directly targets p65cdc18 for rapid degradation and inhibits its replication activity, as strong expression of a constitutively hypophosphorylated mutant form of p65cdc18 results in large amounts of DNA over-replication in vivo. Furthermore, the over-replication phenotype produced by this mutant p65cdc18 is resistant to increased mitotic cyclin/CDK activity, a known inhibitor of over-replication. Therefore, p65cdc18 is the first example of a cellular initiation factor directly regulated in vivo by CDK-dependent phosphorylation and proteolysis. Regulation of p65cdc18 by CDK phosphorylation is likely to contribute to the CDK-driven \"replication switch\" that restricts initiation at eukaryotic origins to once per cell cycle.","authors":"Jallepalli PV, Brown GW, Muzi-Falconi M, Tien D, Kelly TJ","authors_abbrev":"Jallepalli PV et al.","pubmed_publication_date":"01 Nov 1997","pubmed_entrez_date":"1997-11-14","publication_year":"1997","canto_session_key":"d62844597282017d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-08-29 15:22:36","canto_approved_date":"2024-04-03 12:18:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-29 15:22:04","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":40,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB2B4.03","SPBC582.03","SPCC4E9.02","SPBC14C8.07c","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-08-29"},{"uniquename":"PMID:19286980","title":"Phosphatidylethanolamine is required for normal cell morphology and cytokinesis in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2009 May;8(5):790-9","abstract":"To investigate the contributions of phosphatidylethanolamine to the growth and morphogenesis of the fission yeast Schizosaccharomyces pombe, we have characterized three predicted genes in this organism, designated psd1, psd2, and psd3, encoding phosphatidylserine decarboxylases, which catalyze the conversion of phosphatidylserine to phosphatidylethanolamine in both eukaryotic and prokaryotic organisms. S. pombe mutants carrying deletions in any one or two psd genes are viable in complex rich medium and synthetic defined minimal medium. However, mutants carrying deletions in all three psd genes (psd1-3Delta mutants) grow slowly in rich medium and are inviable in minimal medium, indicating that the psd1 to psd3 gene products share overlapping essential cellular functions. Supplementation of growth media with ethanolamine, which can be converted to phosphatidylethanolamine by the Kennedy pathway, restores growth to psd1-3Delta cells in minimal medium, indicating that phosphatidylethanolamine is essential for S. pombe cell growth. psd1-3Delta cells produce lower levels of phosphatidylethanolamine than wild-type cells, even in medium supplemented with ethanolamine, indicating that the Kennedy pathway can only partially compensate for the loss of phosphatidylserine decarboxylase activity in S. pombe. psd1-3Delta cells appear morphologically indistinguishable from wild-type S. pombe cells in medium supplemented with ethanolamine, but when cultured in nonsupplemented medium, they produce high frequencies of abnormally shaped cells as well as cells exhibiting severe septation defects, including multiple, mispositioned, deformed, and misoriented septa. Our results demonstrate that phosphatidylethanolamine is essential for cell growth and for normal cytokinesis and cellular morphogenesis in S. pombe, and they illustrate the usefulness of this model eukaryote for investigating potentially conserved biological and molecular functions of phosphatidylethanolamine.","doi":"10.1128/EC.00029-09","authors":"Luo J, Matsuo Y, Gulis G, Hinz H, Patton-Vogt J, Marcus S","authors_abbrev":"Luo J et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-03-17","publication_year":"2009","canto_session_key":"35ca920e9a2d766f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-10 12:56:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-08-31 15:24:44","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.03","SPBC16E9.18","SPAC31G5.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-08-31"},{"uniquename":"PMID:37200372","title":"Comprehensive mutational analysis of the checkpoint signaling function of Rpa1/Ssb1 in fission yeast.","citation":"PLoS Genet 2023 May;19(5):e1010691","abstract":"Replication protein A (RPA) is a heterotrimeric complex and the major single-strand DNA (ssDNA) binding protein in eukaryotes. It plays important roles in DNA replication, repair, recombination, telomere maintenance, and checkpoint signaling. Because RPA is essential for cell survival, understanding its checkpoint signaling function in cells has been challenging. Several RPA mutants have been reported previously in fission yeast. None of them, however, has a defined checkpoint defect. A separation-of-function mutant of RPA, if identified, would provide significant insights into the checkpoint initiation mechanisms. We have explored this possibility and carried out an extensive genetic screen for Rpa1/Ssb1, the large subunit of RPA in fission yeast, looking for mutants with defects in checkpoint signaling. This screen has identified twenty-five primary mutants that are sensitive to genotoxins. Among these mutants, two have been confirmed partially defective in checkpoint signaling primarily at the replication fork, not the DNA damage site. The remaining mutants are likely defective in other functions such as DNA repair or telomere maintenance. Our screened mutants, therefore, provide a valuable tool for future dissection of the multiple functions of RPA in fission yeast.","doi":"10.1371/journal.pgen.1010691","authors":"Xu YJ, Bhadra S, Mahdi ATA, Dev K, Yurtsever I, Nakamura TM","authors_abbrev":"Xu YJ et al.","pubmed_publication_date":"May 2023","pubmed_entrez_date":"2023-05-18","publication_year":"2023","canto_session_key":"7ad9eb5a73f1bab1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-07-12 08:06:52","canto_approved_date":"2024-04-04 08:39:47","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-07-03 17:12:10","canto_added_date":"2023-05-19 00:15:04","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":78,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.13c","SPCC18B5.11c","SPBC216.05","SPAC664.07c","SPCC1259.13","SPCC23B6.05c","SPAC694.06c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2023-07-12"},{"uniquename":"PMID:7840611","title":"Carbon-13 NMR studies and purification of gluconate pathway enzymes from Schizosaccharomyces pombe.","citation":"Arch Biochem Biophys 1995 Jan 10;316(1):155-62","abstract":"Evidence is presented to show that D-glucose in Schizosaccharomyces pombe can be metabolized via a new alternative route (gluconate pathway) in addition to the regular D-glucose 6-phosphate route. This gluconate pathway consists of two steps: oxidation of D-glucose to D-gluconate by NADP(+)-dependent glucose dehydrogenase and phosphorylation of D-gluconate to 6-phosphogluconate by gluconate kinase. The formation of D-gluconate and 6-phosphogluconate from D-glucose was monitored by 13C nuclear magnetic resonance spectroscopy using D-[1-13C]glucose and D-[U-13C]glucose. The operation of the gluconate pathway was further substantiated by the purification of its two member enzymes, glucose dehydrogenase and gluconate kinase, from the cell-free extract of the fission yeast. Glucose dehydrogenase has been purified (580-fold) to homogeneity by the combined procedures of ammonium sulfate fractionation, Sephadex gel filtration, cation-exchange chromatography, matrex gel chromatography, and agarose-NADP+ affinity chromatography. The purified enzyme is monomeric with a relative molecular weight of 6.65 x 10(4) Da. Gluconate kinase has been purified (410-fold) to near homogeneity by a combination of chromatographic procedures using Bio-gels, matrex gel, and agarose gels. The purified enzyme is monomeric with a relative molecular weight of 2.4 x 10(4) Da. The gluconate pathway presented here provides an alternative route for the D-glucose metabolism in Sch. pombe. Meanwhile, this paper documents another metabolic difference between the fission and budding yeasts.","authors":"Tsai CS, Ye HG, Shi JL","authors_abbrev":"Tsai CS et al.","pubmed_publication_date":"10 Jan 1995","pubmed_entrez_date":"1995-01-10","publication_year":"1995","canto_session_key":"e6d5f75b4f4f35e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-06-29 11:58:25","canto_approved_date":"2025-02-20 08:38:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-29 11:58:03","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.12","SPBC660.16"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-06-29"},{"uniquename":"EMBL:AU010261","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007922","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8766925","title":"Isolation and characterization of pos mutants defective in correct positioning of septum in Schizosaccharomyces pombe.","citation":"Zoolog Sci 1996 Apr;13(2):235-9","abstract":"We have isolated mutants of fission yeast defective in correct positioning of septum. In visual screening, we obtained 16 clones showing unequal septation at restrictive temperature, which were classified into three complementation groups. At restrictive temperature, all the mutants underwent nuclear division normally. In cytokinesis, however, a contractile ring was formed at the site independent of the mitotic spindle. These results suggest that positional information for cytokinesis are not accurately transmitted to the cell equator. Furthermore, all the mutants frequently displayed incorrect orientation and/or distortion of septum, which suggests that the septum positioning is closely related to correct orientation and organization of septum.","authors":"Edamatsu M, Toyoshima YY","authors_abbrev":"Edamatsu M et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28916539","title":"Comparative analysis of alternative polyadenylation in  S. cerevisiae  and  S. pombe .","citation":"Genome Res 2017 Oct;27(10):1685-1695","abstract":"Alternative polyadenylation (APA) is a widespread mechanism that generates mRNA isoforms with distinct properties. Here we have systematically mapped and compared cleavage and polyadenylation sites (PASs) in two yeast species,  S. cerevisiae  and  S. pombe  Although >80% of the mRNA genes in each species were found to display APA,  S. pombe  showed greater 3' UTR size differences among APA isoforms than did  S. cerevisiae  PASs in different locations of gene are surrounded with distinct sequences in both species and are often associated with motifs involved in the Nrd1-Nab3-Sen1 termination pathway. In  S. pombe,  strong motifs surrounding distal PASs lead to higher abundances of long 3' UTR isoforms than short ones, a feature that is opposite in  S. cerevisiae  Differences in PAS placement between convergent genes lead to starkly different antisense transcript landscapes between budding and fission yeasts. In both species, short 3' UTR isoforms are more likely to be expressed when cells are growing in nutrient-rich media, although different gene groups are affected in each species. Significantly, 3' UTR shortening in  S. pombe  coordinates with up-regulation of expression for genes involved in translation during cell proliferation. Using  S. pombe  strains deficient for Pcf11 or Pab2, we show that reduced expression of 3'-end processing factors lengthens 3' UTR, with Pcf11 having a more potent effect than Pab2. Taken together, our data indicate that APA mechanisms in  S. pombe  and  S. cerevisiae  are largely different:  S. pombe  has many of the APA features of higher species, and Pab2 in  S. pombe  has a different role in APA regulation than its mammalian homolog, PABPN1.","doi":"10.1101/gr.222331.117","authors":"Liu X, Hoque M, Larochelle M, Lemay JF, Yurko N, Manley JL, Bachand F, Tian B","authors_abbrev":"Liu X et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-09-17","publication_year":"2017","canto_session_key":"8dc9ee3bf2a79cea","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-09-18 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9891047","title":"Mutator phenotype induced by aberrant replication.","citation":"Mol Cell Biol 1999 Feb;19(2):1126-35","abstract":"We have identified thermosensitive mutants of five Schizosaccharomyces pombe replication proteins that have a mutator phenotype at their semipermissive temperatures. Allele-specific mutants of DNA polymerase delta (poldelta) and mutants of Polalpha, two Poldelta subunits, and ligase exhibited increased rates of deletion of sequences flanked by short direct repeats. Deletion of rad2(+), which encodes a nuclease involved in processing Okazaki fragments, caused an increased rate of duplication of sequences flanked by short direct repeats. The deletion mutation rates of all the thermosensitive replication mutators decreased in a rad2Delta background, suggesting that deletion formation requires Rad2 function. The duplication mutation rate of rad2Delta was also reduced in a thermosensitive polymerase background, but not in a ligase mutator background, which suggests that formation of duplication mutations requires normal DNA polymerization. Thus, although the deletion and duplication mutator phenotypes are distinct, their mutational mechanisms are interdependent. The deletion and duplication replication mutators all exhibited decreased viability in combination with deletion of a checkpoint Rad protein, Rad26. Interestingly, deletion of Cds1, a protein kinase functioning in a checkpoint Rad-mediated reversible S-phase arrest pathway, decreased the viability and exacerbated the mutation rate only in the thermosensitive deletion replication mutators but had no effect on rad2Delta. These findings suggest that aberrant replication caused by allele-specific mutations of these replication proteins can accumulate potentially mutagenic DNA structures. The checkpoint Rad-mediated pathways monitor and signal the aberrant replication in both the deletion and duplication mutators, while Cds1 mediates recovery from aberrant replication and prevents formation of deletion mutations specifically in the thermosensitive deletion replication mutators.","authors":"Liu VF, Bhaumik D, Wang TS","authors_abbrev":"Liu VF et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-01-16","publication_year":"1999","canto_session_key":"b40507851e928932","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-08 11:43:03","canto_approved_date":"2019-12-18 16:15:56","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-04-08 11:42:58","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c","SPBC336.04","SPAC27E2.05","SPBC1734.02c","SPAC9E9.08","SPAC3G6.06c","SPAC20G8.01","SPAC2G11.12","SPBC25H2.13c","SPBC1347.10","SPCC18B5.11c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2015-04-08"},{"uniquename":"PMID:17952063","title":"TOR signalling regulates mitotic commitment through the stress MAP kinase pathway and the Polo and Cdc2 kinases.","citation":"Nat Cell Biol 2007 Nov;9(11):1263-72","abstract":"The coupling of growth to cell cycle progression allows eukaryotic cells to divide at particular sizes depending on nutrient availability. In fission yeast, this coupling involves the Spc1/Sty1 mitogen-activated protein kinase (MAPK) pathway working through Polo kinase recruitment to the spindle pole bodies (SPBs). Here we report that changes in nutrients influence TOR signalling, which modulates Spc1/Sty1 activity. Rapamycin-induced inhibition of TOR signalling advanced mitotic onset, mimicking the reduction in cell size at division seen after shifts to poor nitrogen sources. Gcn2, an effector of TOR signalling and modulator of translation, regulates the Pyp2 phosphatase that in turn modulates Spc1/Sty1 activity. Rapamycin- or nutrient-induced stimulation of Spc1/Sty1 activity promotes Polo kinase SPB recruitment and Cdc2 activation to advance mitotic onset. This advanced mitotic onset is abolished in cells depleted of Gcn2, Pyp2, or Spc1/Sty1 or on blockage of Spc1/Sty1-dependent Polo SPB recruitment. Therefore, TOR signalling modulates mitotic onset through the stress MAPK pathway via the Pyp2 phosphatase.","authors":"Petersen J, Nurse P","authors_abbrev":"Petersen J et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-10-24","publication_year":"2007","canto_session_key":"223cbaaac1c064d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-27 14:13:31","canto_approved_date":"2024-04-03 10:13:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-27 14:13:23","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.10c","SPAC19D5.01","SPBC36B7.09","SPCC18B5.03","SPAC24H6.05","SPAC23C11.16","SPAC3G9.09c","SPAC26F1.10c","SPAC24B11.06c","SPBC29B5.01","SPBC409.07c","SPBC11B10.09"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2016-01-27"},{"uniquename":"PMID:20858896","title":"Activity of a C-terminal plant homeodomain (PHD) of Msc1 is essential for function.","citation":"J Biol Chem 2010 Nov 19;285(47):36828-35","abstract":"Msc1, a member of the Jarid1 family of putative histone demethylases, is required for chromosome stability in fission yeast. Msc1 associates with the Swr1 complex that facilitates deposition of histone H2A.Z into chromatin. To assess the function of Msc1 in the Swr1 complex, domains of Msc1 necessary for interaction with Swr1 were identified. The C-terminal plant homeodomain (PHD) 2 and PHD3 of Msc1 are sufficient to confer association with Swr1 and allow Msc1 to function in the context of kinetochore mutants. On the other hand, a mutant with a single amino acid substitution in PHD2 within the full-length Msc1 protein retains the ability to bind to Swr1 but eliminates the function of Msc1 in combination with kinetochore mutants. Thus, Swr1 association is critical but not sufficient for Msc1 function. An activity of Msc1 that depends on the cysteine residue within PHD2 of Msc1 is likewise critical for function. On the basis of our observation that the PHDs of Msc1 act as E3 ubiquitin ligases and that mutations of cysteine residues within those domains abolish ligase activity, we speculate that the ability of Msc1 to facilitate ubiquitin transfer is critical for the function it mediates through its association with Swr1.","doi":"10.1074/jbc.M110.157792","authors":"Qiu X, Dul BE, Walworth NC","authors_abbrev":"Qiu X et al.","pubmed_publication_date":"19 Nov 2010","pubmed_entrez_date":"2010-09-23","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9G1.13c","SPAPB8E5.09","SPAC11E3.01c","SPBC83.08","SPAC343.11c","SPCC736.14"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:14698245","title":"Heterologous overexpression and purification of four common subunits of nuclear RNA polymerases I, II and III of Schizosaccharomyces pombe.","citation":"J Chromatogr B Analyt Technol Biomed Life Sci 2004 Feb 05;800(1-2):121-6","abstract":"Four subunits of Schizosaccharomyces pombe RNA polymerases I-III shared by all three enzymes (Rpb5, Rpb8, Rpb10 and Rpc10 [Rpb12]) have been overexpressed in Escherichia coli expression vectors pQE or pET as hexahistidine fusions. The recombinant proteins have been purified to near homogeneity using metal-chelate affinity chromatography and gel filtration. Homogeneity and identity of the purified protein preparations was demonstrated by denaturing polyacrylamide gel electrophoresis and TOF-MALDI mass spectrometry. The proteins were obtained in large amounts, and their preparations are currently in use for monoclonal antibody production and physico-chemical studies of these individual components of eukaryotic transcription enzymes.","authors":"Proshkin SA, Shpakovski GV","authors_abbrev":"Proshkin SA et al.","pubmed_publication_date":"05 Feb 2004","pubmed_entrez_date":"2003-12-31","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14704348","title":"The major role of human AP-endonuclease homolog Apn2 in repair of abasic sites in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2004;32(1):115-26","abstract":"The abasic (AP) sites, the major mutagenic and cytotoxic genomic lesions, induced directly by oxidative stress and indirectly after excision of damaged bases by DNA glycosylases, are repaired by AP-endonucleases (APEs). Among two APEs in Saccharomyces cerevisiae, Apn1 provides the major APE activity, and Apn2, the ortholog of the mammalian APE, provides back-up activity. We have cloned apn1 and apn2 genes of Schizosaccharomyces pombe, and have shown that inactivation of Apn2 and not Apn1 sensitizes this fission yeast to alkylation and oxidative damage-inducing agents, which is further enhanced by Apn1 inactivation. We also show that Uve1, present in S.pombe but not in S.cerevisiae, provides the back-up APE activity together with Apn1. We confirmed the presence of APE activity in recombinant Apn2 and in crude cell extracts. Thus S.pombe is distinct from S.cerevisiae, and is similar to mammalian cells in having Apn2 as the major APE.","authors":"Ribar B, Izumi T, Mitra S","authors_abbrev":"Ribar B et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-01-06","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3D6.10","SPCC622.17","SPBC19C7.09c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:15509785","title":"Biochemical interactions between proteins and mat1 cis-acting sequences required for imprinting in fission yeast.","citation":"Mol Cell Biol 2004 Nov;24(22):9813-22","abstract":"DNA recombination required for mating type (mat1) switching in Schizosaccharomyces pombe is initiated by mat1 imprinting. The imprinting event is regulated by mat1 cis-acting elements and by several trans-acting factors, including swi1 (for switch), swi3, swi7, and sap1. swi1 and swi3 were previously shown to function in dictating unidirectional mat1 DNA replication by controlling replication fork movement around the mat1 region and, second, by pausing fork progression around the imprint site. With biochemical studies, we investigated whether the trans-acting factors function indirectly or directly by binding to the mat1 cis-acting sequences. First, we report the identification and DNA sequence of the swi3 gene. swi3 is not essential for viability, and, like the other factors, it exerts a stimulatory effect on imprinting. Second, we showed that only Swi1p and Swi3p interact to form a multiprotein complex and that complex formation did not require their binding to a DNA region defined by the smt-0 mutation. Third, we found that the Swi1p-Swi3p complex physically binds to a region around the imprint site where pausing of replication occurs. Fourth, the protein complex also interacted with the mat1-proximal polar terminator of replication (RTS1). These results suggest that the stimulatory effect of swi1 and swi3 on switching and imprinting occurs through interaction of the Swi1p-Swi3p complex with the mat1 regions.","authors":"Lee BS, Grewal SI, Klar AJ","authors_abbrev":"Lee BS et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-29","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC30D10.04","SPBC216.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7962207","title":"Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins.","citation":"J Cell Sci 1994 Jun;107 ( Pt 6):1671-8","abstract":"We previously reported the identification of human CAP, a protein that is related to the Saccharomyces cerevisiae and Schizosaccharomyces pombe adenylyl cyclase-associated CAP proteins. The two yeast CAP proteins have similar functions: the N-terminal domains are required for the normal function of adenylyl cyclase, while loss of the C-terminal domains result in morphological and nutritional defects that are unrelated to the cAMP pathways. We have amplified and cloned cDNAs from a human glioblastoma library that encode a second CAP-related protein, CAP2. The human CAP and CAP2 proteins are 64% identical. Expression of either human CAP or CAP2 in S. cerevisiae cap- strains suppresses phenotypes associated with deletion of the C-terminal domain of CAP, but does not restore hyper-activation of adenylyl cyclase by RAS2val19. Similarly, expression of either human CAP or CAP2 in S. pombe cap- strains suppresses the morphological and temperature-sensitive phenotypes associated with deletion of the C-terminal domain of CAP in this yeast. In addition, expression of human CAP, but not CAP2, suppresses the propensity to sporulate due to deletion of the N-terminal domain of CAP in S. pombe. This latter observation suggests that human CAP restores normal adenylyl cyclase activity in S. pombe cap- cells. Thus, functional properties of both N-terminal and C-terminal domains are conserved between the human and S. pombe CAP proteins.","authors":"Yu G, Swiston J, Young D","authors_abbrev":"Yu G et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_session_key":"9b0cf5cc09d98b6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 14:57:33","canto_session_submitted_date":"2012-03-03 14:57:16","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC306.09c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:21124977","title":"β(1,3)-glucanosyl-transferase activity is essential for cell wall integrity and viability of Schizosaccharomyces pombe.","citation":"PLoS One 2010 Nov 18;5(11):e14046","abstract":"The formation of the cell wall in Schizosaccharomyces pombe requires the coordinated activity of enzymes involved in the biosynthesis and modification of β-glucans. The β(1,3)-glucan synthase complex synthesizes linear β(1,3)-glucans, which remain unorganized until they are cross-linked to other β(1,3)-glucans and other cell wall components. Transferases of the GH72 family play important roles in cell wall assembly and its rearrangement in Saccharomyces cerevisiae and Aspergillus fumigatus. Four genes encoding β(1,3)-glucanosyl-transferases -gas1(+), gas2(+), gas4(+) and gas5(+)- are present in S. pombe, although their function has not been analyzed.\nHere, we report the characterization of the catalytic activity of gas1p, gas2p and gas5p together with studies directed to understand their function during vegetative growth. From the functional point of view, gas1p is essential for cell integrity and viability during vegetative growth, since gas1Δ mutants can only grow in osmotically supported media, while gas2p and gas5p play a minor role in cell wall construction. From the biochemical point of view, all of them display β(1,3)-glucanosyl-transferase activity, although they differ in their specificity for substrate length, cleavage point and product size. In light of all the above, together with the differences in expression profiles during the life cycle, the S. pombe GH72 proteins may accomplish complementary, non-overlapping functions in fission yeast.\nWe conclude that β(1,3)-glucanosyl-transferase activity is essential for viability in fission yeast, being required to maintain cell integrity during vegetative growth.","doi":"10.1371/journal.pone.0014046","authors":"de Medina-Redondo M, Arnáiz-Pita Y, Clavaud C, Fontaine T, del Rey F, Latgé JP, Vázquez de Aldana CR","authors_abbrev":"de Medina-Redondo M et al.","pubmed_publication_date":"18 Nov 2010","pubmed_entrez_date":"2010-12-03","publication_year":"2010","canto_session_key":"38ae4b1dd6055d00","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-17 18:21:21","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-17 18:21:14","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":37,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.13c","SPBC342.03","SPAC19B12.02c","SPBC29A10.08"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-12-17"},{"uniquename":"EMBL:AB084828","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.16"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29195389","title":"Multiplexed fluctuation-dissipation-theorem calibration of optical tweezers inside living cells.","citation":"Rev Sci Instrum 2017 Nov;88(11):113112","abstract":"In order to apply optical tweezers-based force measurements within an uncharacterized viscoelastic medium such as the cytoplasm of a living cell, a quantitative calibration method that may be applied in this complex environment is needed. We describe an improved version of the fluctuation-dissipation-theorem calibration method, which has been developed to perform in situ calibration in viscoelastic media without prior knowledge of the trapped object. Using this calibration procedure, it is possible to extract values of the medium's viscoelastic moduli as well as the force constant describing the optical trap. To demonstrate our method, we calibrate an optical trap in water, in polyethylene oxide solutions of different concentrations, and inside living fission yeast (S. pombe).","doi":"10.1063/1.5012782","authors":"Yan H, Johnston JF, Cahn SB, King MC, Mochrie SGJ","authors_abbrev":"Yan H et al.","pubmed_publication_date":"Nov 2017","pubmed_entrez_date":"2017-12-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-12-05 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12409291","title":"The Cdc42 binding and scaffolding activities of the fission yeast adaptor protein Scd2.","citation":"J Biol Chem 2003 Jan 10;278(2):843-52","abstract":"The small GTP-binding protein Cdc42, the guanine nucleotide exchange factor Scd1, the p21-activated kinase Shk1, and the adaptor protein Scd2 are involved in the Cdc42-dependent signaling cascade in fission yeast. In the present study, we analyzed the Cdc42 binding and scaffolding activities of Scd2 by co-precipitation assays. We found that two SH3-containing regions, amino acid residues 1-87 (CB1 (Cdc42-binding region 1)) and 110-266 (CB2), of Scd2 can bind to the GTP-bound form of Cdc42. CB2 is cryptic because of the intramolecular binding between the SH3 domain in CB2 (SH3(C)) and the PX domain and binds to Cdc42 only when the Scd2 PB1 domain binds to the PC motif-containing region (residues 760-872) of Scd1. This CB2.Cdc42 association, which would stabilize the open configuration of Scd2, enables the SH3(C) domain to bind to the polyproline motif of Shk1. We also found that the GTP-bound form of Cdc42 binds to the CRIB motif of Shk1 more strongly than to Scd2. Thus, Scd2 functions as a scaffold to form a protein complex, and the GTP-bound Cdc42 might be transferred effectively from the upstream activator Scd1 to the downstream effector Shk1 via Scd2.","authors":"Endo M, Shirouzu M, Yokoyama S","authors_abbrev":"Endo M et al.","pubmed_publication_date":"10 Jan 2003","pubmed_entrez_date":"2002-11-01","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03","SPAC22H10.07","SPBC1604.14c","SPAC16E8.09"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:30975915","title":"The very-long-chain fatty acid elongase Elo2 rescues lethal defects associated with loss of the nuclear barrier function in fission yeast cells.","citation":"J Cell Sci 2019 May 15;132(10)","abstract":"In eukaryotic cells, chromosomes are confined to the nucleus, which is compartmentalized by the nuclear membranes; these are continuous with the endoplasmic reticulum membranes. Maintaining the homeostasis of these membranes is an important cellular activity performed by lipid metabolic enzymes. However, how lipid metabolic enzymes affect nuclear membrane functions remains to be elucidated. We found that the very-long-chain fatty acid elongase Elo2 is located in the nuclear membrane and prevents lethal defects associated with nuclear membrane ruptures in mutants of the nuclear membrane proteins Lem2 and Bqt4 in the fission yeast  Schizosaccharomyces pombe.  Lipid composition analysis shows that t20:0/24:0 phytoceramide (a conjugate of C20:0 phytosphingosine and C24:0 fatty acid) is a major ceramide species in  S. pombe  The quantity of this ceramide is reduced in the absence of Lem2, and restored by increased expression of Elo2. Furthermore, loss of  S. pombe  Elo2 can be rescued by its human orthologs. These results suggest that the conserved very-long-chain fatty acid elongase producing the ceramide component is essential for nuclear membrane integrity and cell viability in eukaryotes.This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.229021","authors":"Kinugasa Y, Hirano Y, Sawai M, Ohno Y, Shindo T, Asakawa H, Chikashige Y, Shibata S, Kihara A, Haraguchi T, Hiraoka Y","authors_abbrev":"Kinugasa Y et al.","pubmed_publication_date":"15 May 2019","pubmed_entrez_date":"2019-04-13","publication_year":"2019","canto_session_key":"021dd77100791f4f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasushi Hiraoka","canto_first_approved_date":"2019-05-15 10:01:52","canto_approved_date":"2025-03-20 17:03:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-05-08 03:13:15","canto_added_date":"2019-04-14 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yasushi Hiraoka","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.03c","SPBC19C7.10","SPAC18G6.10","SPAC1639.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-05-15"},{"uniquename":"EMBL:AU010934","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6402693","title":"Lack of genotoxic properties of the hair-dye component N-methyl-amino-2-nitro-4-N',N'-bis-(2-hydroxyethyl)-aminobenzene, in mammalian cells in vitro, and in yeasts.","citation":"Mutat Res 1983 Feb;116(2):161-8","abstract":"N-Methyl-amino-2-nitro-4-N',N'-bis-(2-hydroxyethyl)-aminobenzene is a hair-dye ingredient. Its potential ability to induce gene mutations, in the yeast S. pombe and in cultured mammalian CH-V79 cells, mitotic gene conversion in the yeast S. cerevisiae, and unscheduled DNA synthesis in cultured human HeLa cells was evaluated. The chemical proved unable to induce detectable genotoxic effects according to these tests. The present data, together with others that show that the chemical is not mutagenic in Salmonella typhimurium or Drosophila, and is not clastogenic in mammalian cytogenetic assays (in vitro or in vivo), strongly support the non-genotoxicity of the chemical.","authors":"Loprieno N, Mariani L, Rusciano D","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"Feb 1983","pubmed_entrez_date":"1983-02-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40848261","title":"Construction of a New Drug and Agrochemical Candidates Screening Platform Utilizing Drug-Hypersensitive Fission Yeast to Discover Overlooked Natural Products.","citation":"J Nat Prod 2025 Aug 23;","abstract":"Natural products exhibiting selective or preferential antifungal activity against fission yeast over budding yeast might contribute greatly to new discoveries in the life sciences and new drug and agrochemical development. However, it is difficult to discover new drug and agrochemical candidates in the fission yeast screening system due to its low drug sensitivity. In this study, we constructed a new antifungal drug and agrochemical candidate screening platform using a drug-hypersensitive fission yeast strain. We executed antifungal activity profiling of our natural compound and microbial libraries against drug-hypersensitive fission yeast and multidrug-sensitive budding yeast. Ultimately, we identified MS-347a as a promising agrochemical candidate due to its excellent activity against the rice blast fungus.","doi":"10.1021/acs.jnatprod.5c00598","authors":"Kimishima A, Negami S, Honma S, Kawashima SA, Yashiroda Y, Fuji SI, Kojima H, Tokiwa T, Sugawara A, Ujie Y, Abe A, Chinen T, Yoshida M, Usui T, Asami Y","authors_abbrev":"Kimishima A et al.","pubmed_publication_date":"23 Aug 2025","pubmed_entrez_date":"2025-08-23","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-08-24 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19571115","title":"Nuclear shape, growth and integrity in the closed mitosis of fission yeast depend on the Ran-GTPase system, the spindle pole body and the endoplasmic reticulum.","citation":"J Cell Sci 2009 Jul 15;122(Pt 14):2464-72","abstract":"The double lipid bilayer of the nuclear envelope (NE) remains intact during closed mitosis. In the fission yeast Schizosaccharomyces pombe, the intranuclear mitotic spindle has envelope-embedded spindle pole bodies (SPB) at its ends. As the spindle elongates and the nucleus divides symmetrically, nuclear volume remains constant but nuclear area rapidly increases by 26%. When Ran-GTPase function is compromised in S. pombe, nuclear division is strikingly asymmetrical and the newly synthesized SPB is preferentially associated with the smaller nucleus, indicative of a Ran-dependent SPB defect that interferes with symmetrical nuclear division. A second defect, which specifically influences the NE, results in breakage of the NE upon spindle elongation. This defect, but not asymmetric nuclear division, is partially rescued by slowing spindle elongation, stimulating endoplasmic reticulum (ER) proliferation or changing conformation of the ER membrane. We propose that redistribution of lipid within the ER-NE network is crucial for mitosis-specific NE changes in both open and closed mitosis.","doi":"10.1242/jcs.049999","authors":"Gonzalez Y, Meerbrey K, Chong J, Torii Y, Padte NN, Sazer S","authors_abbrev":"Gonzalez Y et al.","pubmed_publication_date":"15 Jul 2009","pubmed_entrez_date":"2009-07-03","publication_year":"2009","canto_session_key":"bbbf139e374eabbc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-08 12:10:39","canto_approved_date":"2021-01-08 12:10:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-18 15:15:31","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31A8.01c","SPBC800.05c","SPAC26A3.15c","SPBC557.03c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2021-01-08"},{"uniquename":"PMID:37788281","title":"A dominant negative 14-3-3 mutant in Schizosaccharomyces pombe distinguishes the binding proteins involved in sexual differentiation and check point.","citation":"PLoS One 2023;18(10):e0291524","abstract":"The homothallic fission yeast Schizosaccharomyces pombe undergoes sexual differentiation when starved, but sam (skips the requirement of starvation for mating) mutants such as those carrying mutations in adenylate cyclase (cyr1) or protein kinase A (pka1) mate without starvation. Here, we identified sam3, a dominant negative allele of rad24, encoding one of two 14-3-3 proteins. Genetic mapping and whole-genome sequencing showed that the sam3 mutation comprises a change in nucleotide at position 959 from guanine to adenine, which switches the amino acid at position 185 from glutamic acid to lysine (E185K). We generated the rad24-E185K integrated mutant and its phenotype was similar to that of the sam3 mutant, including calcium sensitivity and UV non-sensitivity, but the phenotype is different from that of the Δrad24 strain. While the UV-sensitive phenotype was observed in the Δrad24 mutant, it was not observed in the sam3 and rad24-E185K mutants. The expression of the rad24-E185K gene in wild type cells induced spore formation in the nutrient rich medium, confirming rad24-E185K is dominant. This dominant effect of rad24-E185K was also observed in Δras1 and Δbyr2 diploid mutants, indicating that rad24-E185K generate stronger phenotype than rad24 null mutants. Ste11, the key transcription factor for sexual differentiation was expressed in sam3 mutants without starvation and it predominantly localized to the nucleus. The Rad24-E185K mutant protein retained its interaction with Check point kinase1 (Chk1), whereas it reduced interaction with Ste11, an RNA binding protein Mei2, and a MAPKKK Byr2, freeing these proteins from negative regulation by Rad24, that account for the sam phenotype and UV non-sensitive phenotype. Glucose depletion in rad24-E185K or Δpka1 Δrad24 double mutation induced haploid meiosis, leading to the formation of spores in haploid. The position of glutamic acid 185 is conserved in all major 14-3-3s; hence, our finding of a dominant negative allele of 14-3-3 is useful for understanding 14-3-3s in other organisms.","doi":"10.1371/journal.pone.0291524","authors":"Ohshima T, Jiajun Z, Fukamachi T, Ohno Y, Senoo H, Matsuo Y, Kawamukai M","authors_abbrev":"Ohshima T et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-10-03","publication_year":"2023","canto_session_key":"aee38813cc53380f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_first_approved_date":"2023-12-15 13:27:02","canto_approved_date":"2024-04-06 13:12:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-13 08:42:07","canto_added_date":"2023-10-03 23:25:04","annotation_curators":[{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPAC17H9.09c","SPAC1D4.13","SPCC1259.13","SPBC32C12.02","SPBC1D7.05","SPBC106.10","SPAC17A2.13c","SPAC27D7.03c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2023-12-15"},{"uniquename":"PMID:16511210","title":"Purification, crystallization and preliminary X-ray diffraction analysis of the histone chaperone cia1 from fission yeast.","citation":"Acta Crystallogr Sect F Struct Biol Cryst Commun 2005 Nov 01;61(Pt 11):971-3","abstract":"In fission yeast, cia1+ is an essential gene that encodes a histone chaperone, a homologue of human CIA (CCG1-interacting factor A) and budding yeast Asf1p (anti-silencing function-1), which both facilitate nucleosome assembly by interacting with the core histones H3/H4. The conserved domain (residues 1-161) of the cia1+-encoded protein was expressed in Escherichia coli, purified to near-homogeneity and crystallized by the sitting-drop vapour-diffusion method. The protein was crystallized in the monoclinic space group C2, with unit-cell parameters a = 79.16, b = 40.53, c = 69.79 A, beta = 115.93 degrees and one molecule per asymmetric unit. The crystal diffracted to beyond 2.10 A resolution using synchrotron radiation.","authors":"Umehara T, Otta Y, Tsuganezawa K, Matsumoto T, Tanaka A, Horikoshi M, Padmanabhan B, Yokoyama S","authors_abbrev":"Umehara T et al.","pubmed_publication_date":"01 Nov 2005","pubmed_entrez_date":"2006-03-03","publication_year":"2005","canto_session_key":"b10d25b23eeacdbe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-09 11:31:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-09 11:31:01","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC663.05c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-09"},{"uniquename":"PMID:10483729","title":"Hexavalent chromium uptake by sensitive and tolerant mutants of Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 1999 Sep 01;178(1):109-15","abstract":"Lysine and leucine auxotrophic, heterothallic (h+, h-) strains of Schizosaccharomyces pombe were used to obtain chromium (VI)-sensitive and -tolerant mutants by ultraviolet radiation-induced and nitrosoguanidine-induced mutagenesis. The minimal inhibitory concentrations of K2Cr2O7 on YEA media were 225 microM for the wild-type strain CW-6, 125 microM for the sensitive mutant CS-6.51 and 275 microM for the tolerant mutant CT-6.66. The mutants exhibited cross-sensitivity of various patterns to Cd2+, Cu2+, Ni2+, Zn2+ and VO3-(4). Cr(VI) was added to the actively growing cultures and the total chromium (TOCr) content of the cells was determined. The sensitive mutant exhibited a high bioaccumulation ability, with a dry biomass of 810 micrograms g-1 after 30 min, while the tolerant mutant had a significantly lower ability than the wild-type strain. In PIPES buffer, washed, lysine-starved biomasses were treated with 75 microM Cr(VI) and after 2 h, the TOCr and the organically bound chromium (OBCr) were determined. Under these conditions, the sensitive and tolerant mutants had the same TOCr content, 50% of which was OBCr. The wild-type strain exhibited a lower TOCr content than that of its mutants and only 35% of this was OBCr. The Cr(VI)-sensitivity was due to a significantly increased uptake of Cr(VI).","authors":"Czakó-Vér K, Batiè M, Raspor P, Sipiczki M, Pesti M","authors_abbrev":"Czakó-Vér K et al.","pubmed_publication_date":"01 Sep 1999","pubmed_entrez_date":"1999-09-14","publication_year":"1999","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18793195","title":"Next-generation sequencing: applications beyond genomes.","citation":"Biochem Soc Trans 2008 Oct;36(Pt 5):1091-6","abstract":"The development of DNA sequencing more than 30 years ago has profoundly impacted biological research. In the last couple of years, remarkable technological innovations have emerged that allow the direct and cost-effective sequencing of complex samples at unprecedented scale and speed. These next-generation technologies make it feasible to sequence not only static genomes, but also entire transcriptomes expressed under different conditions. These and other powerful applications of next-generation sequencing are rapidly revolutionizing the way genomic studies are carried out. Below, we provide a snapshot of these exciting new approaches to understanding the properties and functions of genomes. Given that sequencing-based assays may increasingly supersede microarray-based assays, we also compare and contrast data obtained from these distinct approaches.","doi":"10.1042/BST0361091","authors":"Marguerat S, Wilhelm BT, Bähler J","authors_abbrev":"Marguerat S et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-09-17","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24909977","title":"A histone H3K36 chromatin switch coordinates DNA double-strand break repair pathway choice.","citation":"Nat Commun 2014 Jun 09;5:4091","abstract":"DNA double-strand break (DSB) repair is a highly regulated process performed predominantly by non-homologous end joining (NHEJ) or homologous recombination (HR) pathways. How these pathways are coordinated in the context of chromatin is unclear. Here we uncover a role for histone H3K36 modification in regulating DSB repair pathway choice in fission yeast. We find Set2-dependent H3K36 methylation reduces chromatin accessibility, reduces resection and promotes NHEJ, while antagonistic Gcn5-dependent H3K36 acetylation increases chromatin accessibility, increases resection and promotes HR. Accordingly, loss of Set2 increases H3K36Ac, chromatin accessibility and resection, while Gcn5 loss results in the opposite phenotypes following DSB induction. Further, H3K36 modification is cell cycle regulated with Set2-dependent H3K36 methylation peaking in G1 when NHEJ occurs, while Gcn5-dependent H3K36 acetylation peaks in S/G2 when HR prevails. These findings support an H3K36 chromatin switch in regulating DSB repair pathway choice.","doi":"10.1038/ncomms5091","authors":"Pai CC, Deegan RS, Subramanian L, Gal C, Sarkar S, Blaikley EJ, Walker C, Hulme L, Bernhard E, Codlin S, Bähler J, Allshire R, Whitehall S, Humphrey TC","authors_abbrev":"Pai CC et al.","pubmed_publication_date":"09 Jun 2014","pubmed_entrez_date":"2014-06-10","publication_year":"2014","canto_session_key":"54133fd3f10bcb0d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC17D11.04c","SPAC139.06","SPBC16A3.19","SPAC29B12.02c","SPAC644.14c","SPAC6F6.09","SPAC1952.05"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:41873495","title":"Chemically Synthesized H3K14Ub Unveils Clr4's IDR-Mediated Multivalent Nucleosome Recognition in H3K9 Methylation.","citation":"Angew Chem Int Ed Engl 2026 May 04;65(19):e20817","abstract":"Histone H3 lysine 9 methylation (H3K9me) is a central epigenetic mark governing heterochromatin formation. Although the H3K9 methyltransferase Clr4 has been extensively characterized using short histone peptide substrates, how it recognizes and coordinates different structural domains to engage physiological substrate nucleosomes remains poorly understood. Here, we employed chemical protein synthesis to generate site-specifically ubiquitinated H3K14Ub histones and nucleosomes, enabling quantitative biochemical and structural investigations. Using a CAET handle-assisted strategy, we obtained homogeneous H3K14Ub nucleosomes and demonstrated that ubiquitination enhances Clr4 activity by ∼350-fold on nucleosomes relative to unmodified substrates. Clr4 domain deletion analyses revealed that, the intrinsically disordered region (IDR) of Clr4 is critical for nucleosome binding and ubiquitin-dependent stimulation. Through site-directed photo-crosslinking, we identified specific IDR residues mediating interactions with nucleosomal surfaces. Furthermore, using an isoUb-based synthetic approach, we generated H3K9NleK14Ub nucleosomes and determined cryo-EM structures of Clr4-nucleosome complexes, unveiling multivalent nucleosome recognition by the IDR via four distinct interfaces: the H2A-H2B acidic patch, the H2A/H2B basic groove, the H2B and H3 elbow regions. Methyltransferase activity assays confirmed that mutations disrupting these interfaces impair Clr4 activity. Our study provides mechanistic insights into the ubiquitin-dependent activation mechanism of Clr4, highlighting the power of chemical biology in deciphering epigenetic regulation.","doi":"10.1002/anie.202520817","authors":"Sun M, Du Y, Li Z, Aderjiang A, Xin M, Ai H","authors_abbrev":"Sun M et al.","pubmed_publication_date":"04 May 2026","pubmed_entrez_date":"2026-03-24","publication_year":"2026","canto_session_key":"b371bfeb2c9206d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-05-01 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26472760","title":"Gene essentiality and synthetic lethality in haploid human cells.","citation":"Science 2015 Nov 27;350(6264):1092-6","abstract":"Although the genes essential for life have been identified in less complex model organisms, their elucidation in human cells has been hindered by technical barriers. We used extensive mutagenesis in haploid human cells to identify approximately 2000 genes required for optimal fitness under culture conditions. To study the principles of genetic interactions in human cells, we created a synthetic lethality network focused on the secretory pathway based exclusively on mutations. This revealed a genetic cross-talk governing Golgi homeostasis, an additional subunit of the human oligosaccharyltransferase complex, and a phosphatidylinositol 4-kinase β adaptor hijacked by viruses. The synthetic lethality map parallels observations made in yeast and projects a route forward to reveal genetic networks in diverse aspects of human cell biology.","doi":"10.1126/science.aac7557","authors":"Blomen VA, Májek P, Jae LT, Bigenzahn JW, Nieuwenhuis J, Staring J, Sacco R, van Diemen FR, Olk N, Stukalov A, Marceau C, Janssen H, Carette JE, Bennett KL, Colinge J, Superti-Furga G, Brummelkamp TR","authors_abbrev":"Blomen VA et al.","pubmed_publication_date":"27 Nov 2015","pubmed_entrez_date":"2015-10-17","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18.19c","HGNC:1164"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10648788","title":"Involvement of multiple subunit-subunit contacts in the assembly of RNA polymerase II.","citation":"Nucleic Acids Res 2000 Feb 15;28(4):952-9","abstract":"RNA polymerase II from the fission yeast Schizo-saccharomyces pombe consists of 12 species of subunits, Rpb1-Rpb12. We expressed these subunits, except Rpb4, simultaneously in cultured insect cells with baculovirus expression vectors. For the isolation of subunit complexes formed in the virus-infected cells, a glutathione S -transferase (GST) sequence was fused to the rpb3 cDNA to produce GST-Rpb3 fusion protein and a decahistidine-tag sequence was inserted into the rpb1 cDNA to produce Rpb1H protein. After successive affinity chromatography on glutathione and Ni(2+)columns, complexes consisting of the seven subunits, Rpb1H, Rpb2, GST-Rpb3, Rpb5, Rpb7, Rpb8 and Rpb11, were identified. Omission of the GST-Rpb3 expression resulted in reduced assembly of the Rpb11 into the complex. Direct interaction between Rpb3 and the other six subunits was detected by pairwise coexpression experiments. Coexpression of various combinations of a few subunits revealed that Rpb11 enhances Rpb3-Rpb8 interaction and consequently Rpb8 enhances Rpb1-Rpb3 interaction to some extent. We propose a mechanism in which the assembly of RNA poly-merase II is stabilized through multiple subunit-subunit contacts.","authors":"Kimura M, Ishihama A","authors_abbrev":"Kimura M et al.","pubmed_publication_date":"15 Feb 2000","pubmed_entrez_date":"2000-01-29","publication_year":"2000","canto_session_key":"f2740a7dc68d283d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-03-12 16:50:48","canto_approved_date":"2023-12-11 08:33:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 16:45:25","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.12c","SPBC19C2.03","SPCC1442.10c","SPAC3A12.07","SPBC337.14","SPAPYUG7.04c","SPBC28F2.12","SPAC23C4.15","SPACUNK4.06c","SPCC1020.04c","SPBC14C8.12","SPAC23G3.01"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2015-03-12"},{"uniquename":"PMID:29851559","title":"Metaphase kinetochore movements are regulated by kinesin-8 motors and microtubule dynamic instability.","citation":"Mol Biol Cell 2018 Jun 01;29(11):1332-1345","abstract":"During metaphase, sister chromatids are connected to microtubules extending from the opposite spindle poles via kinetochores to protein complexes on the chromosome. Kinetochores congress to the equatorial plane of the spindle and oscillate around it, with kinesin-8 motors restricting these movements. Yet, the physical mechanism underlying kinetochore movements is unclear. We show that kinetochore movements in the fission yeast Schizosaccharomyces pombe are regulated by kinesin-8-promoted microtubule catastrophe, force-induced rescue, and microtubule dynamic instability. A candidate screen showed that among the selected motors only kinesin-8 motors Klp5/Klp6 are required for kinetochore centering. Kinesin-8 accumulates at the end of microtubules, where it promotes catastrophe. Laser ablation of the spindle resulted in kinetochore movement toward the intact spindle pole in wild-type and klp5Δ cells, suggesting that kinetochore movement is driven by pulling forces. Our theoretical model with Langevin description of microtubule dynamic instability shows that kinesin-8 motors are required for kinetochore centering, whereas sensitivity of rescue to force is necessary for the generation of oscillations. We found that irregular kinetochore movements occur for a broader range of parameters than regular oscillations. Thus, our work provides an explanation for how regulation of microtubule dynamic instability contributes to kinetochore congression and the accompanying movements around the spindle center.","doi":"10.1091/mbc.E17-11-0667","authors":"Klemm AH, Bosilj A, Gluncˇic M, Pavin N, Tolic IM","authors_abbrev":"Klemm AH et al.","pubmed_publication_date":"01 Jun 2018","pubmed_entrez_date":"2018-06-01","publication_year":"2018","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-06-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37815455","title":"Characterization of Pik1 function in fission yeast reveals its conserved role in lipid synthesis and not cytokinesis.","citation":"J Cell Sci 2023 Nov 01;136(21)","abstract":"Phosphatidylinositol (PI)-4-phosphate (PI4P) is a lipid found at the plasma membrane (PM) and Golgi in cells from yeast to humans. PI4P is generated from PI by PI4-kinases and can be converted into PI-4,5-bisphosphate [PI(4,5)P2]. Schizosaccharomyces pombe have two essential PI4-kinases - Stt4 and Pik1. Stt4 localizes to the PM, and its loss from the PM results in a decrease of PM PI4P and PI(4,5)P2. As a result, cells divide non-medially due to disrupted cytokinetic ring-PM anchoring. However, the localization and function of S. pombe Pik1 has not been thoroughly examined. Here, we found that Pik1 localizes exclusively to the trans-Golgi and is required for Golgi PI4P production. We determined that Ncs1 regulates Pik1, but unlike in other organisms, it is not required for Pik1 Golgi localization. When Pik1 function was disrupted, PM PI4P but not PI(4,5)P2 levels were reduced, a major difference compared with Stt4. We conclude that Stt4 is the chief enzyme responsible for producing the PI4P that generates PI(4,5)P2. Also, that cells with disrupted Pik1 do not divide asymmetrically highlights the specific importance of PM PI(4,5)P2 for cytokinetic ring-PM anchoring.","doi":"10.1242/jcs.261415","authors":"Willet AH, Turner LA, Park JS, Ren L, Snider CE, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"01 Nov 2023","pubmed_entrez_date":"2023-10-10","publication_year":"2023","canto_session_key":"2f93fe0b9007bce3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2023-10-14 17:40:53","canto_approved_date":"2025-09-02 18:27:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-12 13:05:37","canto_added_date":"2023-10-10 23:25:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":23,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC577.06c","SPBC2G2.02","SPAC19G12.14","SPAC29A4.05","SPBC146.13c","SPAP8A3.08","SPAC9G1.10c","SPCC794.08","SPAC18B11.04","SPAC3C7.01c","SPAC22E12.16c","SPAC343.19"],"gene_count":12,"ltp_gene_count":6,"approved_date":"2023-10-14"},{"uniquename":"PMID:2725514","title":"Introduction of functional artificial introns into the naturally intronless ura4 gene of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1989 Apr;9(4):1526-35","abstract":"Insertion of a 36-base-pair (bp) synthetic oligonucleotide comprising the sequence 5'-GTAGGT(19N)CTAAT (4N)AG-3' into several different positions within the coding region of the naturally intronless ura4 gene of Schizosaccharomyces pombe leads to an efficiently spliced gene producing a functional product. This suggests that the proper signals within an intron are sufficient to initiate and complete a splicing event independent of the location of the intron in the gene. Point mutations in the 5' junction (5'-GTAGGT-3') and in the putative branch sequence (5'-CTAAT-3') affect splicing efficiency significantly. A G-to-A transition at the first nucleotide at the 5' splice junction (5'-ATAGGT-3') abolishes the use of the authentic splice junction and leads to the increased use of an alternative splice site. No functional product is produced from this transcript. An A-to-G transition of the second A in the putative branch sequence (5'-CTAGT-3') lowers the splicing efficiency drastically, but still results in a functional gene product. Furthermore, extension of the 36-bp intron to introns more than 180 bp in size abolishes splicing, suggesting that the splicing apparatus might be restricted to very short introns. We discuss the possibility that S. pombe introns represent a simple type of eucaryotic intron.","authors":"Gatermann KB, Hoffmann A, Rosenberg GH, Käufer NF","authors_abbrev":"Gatermann KB et al.","pubmed_publication_date":"Apr 1989","pubmed_entrez_date":"1989-04-01","publication_year":"1989","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41739641","title":"Analyses of bent spindles reveal the mechanics of anaphase B in fission yeast.","citation":"Mol Biol Cell 2026 Feb 25;:mbcE25110556","abstract":"The mitotic spindle in the fission yeast  Schizosaccharomyces pombe  is a single bundle of microtubules which elongates to segregate the chromosomes during anaphase B. The mechanical properties of the spindle and the forces driving its elongation remain poorly defined. Here, we analyzed how spindles react to mechanical and genetic perturbations to uncover their mechanical properties. Treatment of cells with osmotic oscillations and blue light led to a consistent phenotype of spindle buckling and breakage in mid-anaphase. The stalling of pole separation and reduced rates of spindle elongation indicated that spindles elongate and buckle under increased mechanical load. The structural integrity of the bent spindles was dependent on Ase1 (PRC1), while the spindle elongation rate was dependent on motor proteins Klp9 (kinesin-6) and Cut7 (kinesin-5). Modeling of bent spindle shapes revealed that most spindles behave mechanically as a beam in which the midzone region is 1-2 times as rigid than the rest of the beam. Upon reaching a threshold size, bent spindles broke at a specific fragile site near the edge of the spindle midzone. Our findings in this simple fission yeast spindle are relevant to the mechanics of more complex metazoan spindles. [Media: see text].","doi":"10.1091/mbc.E25-11-0556","authors":"Real-Calderón P, Fai TG, Daga RR, Lemière J, Chang F","authors_abbrev":"Real-Calderón P et al.","pubmed_publication_date":"25 Feb 2026","pubmed_entrez_date":"2026-02-25","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-02-26 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27253066","title":"Multi-step coordination of telomerase recruitment in fission yeast through two coupled telomere-telomerase interfaces.","citation":"Elife 2016 Jun 02;5","abstract":"Tightly controlled recruitment of telomerase, a low-abundance enzyme, to telomeres is essential for regulated telomere synthesis. Recent studies in human cells revealed that a patch of amino acids in the shelterin component TPP1, called the TEL-patch, is essential for recruiting telomerase to telomeres. However, how TEL-patch-telomerase interaction integrates into the overall orchestration of telomerase regulation at telomeres is unclear. In fission yeast, Tel1(ATM)/Rad3(ATR)-mediated phosphorylation of shelterin component Ccq1 during late S phase is involved in telomerase recruitment through promoting the binding of Ccq1 to a telomerase accessory protein Est1. Here, we identify the TEL-patch in Tpz1(TPP1), mutations of which lead to decreased telomeric association of telomerase, similar to the phosphorylation-defective Ccq1. Furthermore, we find that telomerase action at telomeres requires formation and resolution of an intermediate state, in which the cell cycle-dependent Ccq1-Est1 interaction is coupled to the TEL-patch-Trt1 interaction, to achieve temporally regulated telomerase elongation of telomeres.","doi":"10.7554/eLife.15470","authors":"Hu X, Liu J, Jun HI, Kim JK, Qiao F","authors_abbrev":"Hu X et al.","pubmed_publication_date":"02 Jun 2016","pubmed_entrez_date":"2016-06-03","publication_year":"2016","canto_session_key":"771c4eaaece5b26f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Feng Qiao","canto_approved_date":"2016-07-21 09:32:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-11 08:30:43","canto_added_date":"2016-06-04 00:15:14","annotation_curators":[{"name":"Feng Qiao","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":51,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPAC6F6.16c","SPAC19G12.13c","SPCC188.07","SPBC2D10.13"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-07-11"},{"uniquename":"PMID:17895989","title":"Vesicle-like biomechanics governs important aspects of nuclear geometry in fission yeast.","citation":"PLoS One 2007 Sep 26;2(9):e948","abstract":"It has long been known that during the closed mitosis of many unicellular eukaryotes, including the fission yeast (Schizosaccharomyces pombe), the nuclear envelope remains intact while the nucleus undergoes a remarkable sequence of shape transformations driven by elongation of an intranuclear mitotic spindle whose ends are capped by spindle pole bodies embedded in the nuclear envelope. However, the mechanical basis of these normal cell cycle transformations, and abnormal nuclear shapes caused by intranuclear elongation of microtubules lacking spindle pole bodies, remain unknown. Although there are models describing the shapes of lipid vesicles deformed by elongation of microtubule bundles, there are no models describing normal or abnormal shape changes in the nucleus. We describe here a novel biophysical model of interphase nuclear geometry in fission yeast that accounts for critical aspects of the mechanics of the fission yeast nucleus, including the biophysical properties of lipid bilayers, forces exerted on the nuclear envelope by elongating microtubules, and access to a lipid reservoir, essential for the large increase in nuclear surface area during the cell cycle. We present experimental confirmation of the novel and non-trivial geometries predicted by our model, which has no free parameters. We also use the model to provide insight into the mechanical basis of previously described defects in nuclear division, including abnormal nuclear shapes and loss of nuclear envelope integrity. The model predicts that (i) despite differences in structure and composition, fission yeast nuclei and vesicles with fluid lipid bilayers have common mechanical properties; (ii) the S. pombe nucleus is not lined with any structure with shear resistance, comparable to the nuclear lamina of higher eukaryotes. We validate the model and its predictions by analyzing wild type cells in which ned1 gene overexpression causes elongation of an intranuclear microtubule bundle that deforms the nucleus of interphase cells.","authors":"Lim H W G, Huber G, Torii Y, Hirata A, Miller J, Sazer S","authors_abbrev":"Lim H W G et al.","pubmed_publication_date":"26 Sep 2007","pubmed_entrez_date":"2007-09-27","publication_year":"2007","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34004668","canto_session_key":"e4a818466ab39695","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23953933","title":"Interplays between ATM/Tel1 and ATR/Mec1 in sensing and signaling DNA double-strand breaks.","citation":"DNA Repair (Amst) 2013 Oct;12(10):791-9","abstract":"DNA double-strand breaks (DSBs) are highly hazardous for genome integrity because they have the potential to cause mutations, chromosomal rearrangements and genomic instability. The cellular response to DSBs is orchestrated by signal transduction pathways, known as DNA damage checkpoints, which are conserved from yeasts to humans. These pathways can sense DNA damage and transduce this information to specific cellular targets, which in turn regulate cell cycle transitions and DNA repair. The mammalian protein kinases ATM and ATR, as well as their budding yeast corresponding orthologs Tel1 and Mec1, act as master regulators of the checkpoint response to DSBs. Here, we review the early steps of DSB processing and the role of DNA-end structures in activating ATM/Tel1 and ATR/Mec1 in an orderly and reciprocal manner.","doi":"10.1016/j.dnarep.2013.07.009","authors":"Gobbini E, Cesena D, Galbiati A, Lockhart A, Longhese MP","authors_abbrev":"Gobbini E et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-08-20","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24001781","title":"Sixteen novel mutations in the arylsulfatase A gene causing metachromatic leukodystrophy.","citation":"Gene 2013 Nov 10;530(2):323-8","abstract":"Metachromatic leukodystrophy (MLD) is a lysosomal storage disorder caused mainly by mutations in the arylsulfatase A (ARSA) gene. In this manuscript we report sixteen novel mutations identified in the ARSA gene of fifteen unrelated patients affected with MLD. Of these 16 mutations nine were missense mutations (p.L11Q, p.S44P, p.L81P, p.R84L, p.V177D, p.P284S, p.R288S, p.G301R, p.P425S), three were nonsense mutations (p.Q51X, p.Y149X, p.C156X), three were frame shift mutations (c.28delG, c.105C>A+106_124dup, c.189delC) and one was a splice-site mutation (c.1102-2A>G). In addition, three previously reported mutations were identified on an allelic background different from the one in the original reports. Two mutations, p.G309S and p.E312D, were identified on the background of the so-called pseudodeficiency (Pd) allele while previously they were reported alone. On the other hand, mutation p.R311X was identified in two unrelated patients not in cis with the Pd mutations, as previously reported.","doi":"10.1016/j.gene.2013.08.065","authors":"Luzi P, Rafi MA, Rao HZ, Wenger DA","authors_abbrev":"Luzi P et al.","pubmed_publication_date":"10 Nov 2013","pubmed_entrez_date":"2013-09-05","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBPB10D8.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20740713","title":"Fighting of Casein kinase 1 and PP2A/Shugoshin for cohesins during meiosis I.","citation":"Cell Cycle 2010 Aug 01;9(15):2929-30","abstract":"","authors":"Suja JA","authors_abbrev":"Suja JA","pubmed_publication_date":"01 Aug 2010","pubmed_entrez_date":"2010-08-27","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22907751","title":"CENP-B cooperates with Set1 in bidirectional transcriptional silencing and genome organization of retrotransposons.","citation":"Mol Cell Biol 2012 Oct;32(20):4215-25","abstract":"Regulation of transposable elements (TEs) is critical to the integrity of the host genome. The fission yeast Schizosaccharomyces pombe homologs of mammalian CENP-B perform a host genome surveillance role by controlling Tf2 long terminal repeat (LTR) retrotransposons. However, the mechanisms by which CENP-Bs effect their functions are ill defined. Here, we show that the multifaceted roles of Abp1, the prominent member of fission yeast CENP-Bs, are mediated in part via recognition of a 10-bp AT-rich motif present in most LTRs and require the DNA-binding, transposase, and dimerization domains of Abp1 to maintain transcriptional repression and genome organization. Expression profiling analyses indicated that Abp1 recruits class I/II histone deacetylases (HDACs) to repress Tf2 retrotransposons and genes activated in response to stresses. We demonstrate that class I/II HDACs and sirtuins mediate the clustering of dispersed Tf2 retrotransposons into Tf bodies. Intriguingly, we uncovered an unexpected cooperation between Abp1 and the histone H3K4 methyltransferase Set1 in regulating sense and antisense transcriptional silencing of Tf2 retrotransposons and Tf body integrity. Moreover, Set1-mediated regulation of Tf2 expression and nuclear organization appears to be largely independent of H3K4 methylation. Our study illuminates a molecular pathway involving a transposase-containing transcription factor that cooperates with chromatin modifiers to regulate TE activities.","authors":"Lorenz DR, Mikheyeva IV, Johansen P, Meyer L, Berg A, Grewal SI, Cam HP","authors_abbrev":"Lorenz DR et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-22","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1105.04c","SPCC306.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:29422503","title":"LARP7-like protein Pof8 regulates telomerase assembly and poly(A)+TERRA expression in fission yeast.","citation":"Nat Commun 2018 Feb 08;9(1):586","abstract":"Telomerase is a reverse transcriptase complex that ensures stable maintenance of linear eukaryotic chromosome ends by overcoming the end replication problem, posed by the inability of replicative DNA polymerases to fully replicate linear DNA. The catalytic subunit TERT must be assembled properly with its telomerase RNA for telomerase to function, and studies in Tetrahymena have established that p65, a La-related protein 7 (LARP7) family protein, utilizes its C-terminal xRRM domain to promote assembly of the telomerase ribonucleoprotein (RNP) complex. However, LARP7-dependent telomerase complex assembly has been considered as unique to ciliates that utilize RNA polymerase III to transcribe telomerase RNA. Here we show evidence that fission yeast Schizosaccharomyces pombe utilizes the p65-related protein Pof8 and its xRRM domain to promote assembly of RNA polymerase II-encoded telomerase RNA with TERT. Furthermore, we show that Pof8 contributes to repression of the transcription of noncoding RNAs at telomeres.","doi":"10.1038/s41467-018-02874-0","authors":"Mennie AK, Moser BA, Nakamura TM","authors_abbrev":"Mennie AK et al.","pubmed_publication_date":"08 Feb 2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_session_key":"72c1277f6497035f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Toru Nakamura","canto_first_approved_date":"2018-02-21 19:46:55","canto_approved_date":"2026-01-17 17:49:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-19 14:50:36","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[{"name":"Toru Nakamura","community_curator":true,"annotation_count":102,"orcid":"0000-0001-5752-0814","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G6.17","SPAC19G12.13c","SPAC6F6.17","SPBC29A3.14c","SPBC1778.02","SPBC9B6.05c","SPAC16A10.07c","SPBC2D10.13","SPCC188.07","SPNCRNA.214","SPAC30D11.10"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2018-02-21"},{"uniquename":"PMID:16931764","title":"Argonaute slicing is required for heterochromatic silencing and spreading.","citation":"Science 2006 Aug 25;313(5790):1134-7","abstract":"Small interfering RNA (siRNA) guides dimethylation of histone H3 lysine-9 (H3K9me2) via the Argonaute and RNA-dependent RNA polymerase complexes, as well as base-pairing with either RNA or DNA. We show that Argonaute requires the conserved aspartate-aspartate-histidine motif for heterochromatic silencing and for ribonuclease H-like cleavage (slicing) of target messages complementary to siRNA. In the fission yeast Schizosaccharomyces pombe, heterochromatic repeats are transcribed by polymerase II. We show that H3K9me2 spreads into silent reporter genes when they are embedded within these transcripts and that spreading requires read-through transcription, as well as slicing by Argonaute. Thus, siRNA guides histone modification by basepairing interactions with RNA.","authors":"Irvine DV, Zaratiegui M, Tolia NH, Goto DB, Chitwood DH, Vaughn MW, Joshua-Tor L, Martienssen RA","authors_abbrev":"Irvine DV et al.","pubmed_publication_date":"25 Aug 2006","pubmed_entrez_date":"2006-08-26","publication_year":"2006","canto_session_key":"58586cbbae636cdc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-23 10:16:28","canto_approved_date":"2024-05-23 10:16:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-20 15:51:47","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":26,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.11","SPAC17A2.12","SPAC6F12.09"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2024-05-23"},{"uniquename":"PMID:19343653","title":"Versatile laser-based cell manipulator.","citation":"J Biophotonics 2008 Sep;1(4):299-309","abstract":"Here we describe a two-photon microscope and laser ablation setup combined with optical tweezers. We tested the setup on the fission yeast Schizosaccharomyces pombe, a commonly used model organism. We show that long-term imaging can be achieved without significant photo-bleaching or damage of the sample. The setup can precisely ablate sub-micrometer structures, such as microtubules and mitotic spindles, inside living cells, which remain viable after the manipulation. Longer exposure times lead to ablation, while shorter exposures lead to photo-bleaching of the target structure. We used optical tweezers to trap intracellular particles and to displace the cell nucleus. Two-photon fluorescence imaging of the manipulated cell can be performed simultaneously with trapping. The combination of techniques described here may help to solve a variety of problems in cell biology, such as positioning of organelles and the forces exerted by the cytoskeleton.","doi":"10.1002/jbio.200810026","authors":"Maghelli N, Tolić-Nørrelykke IM","authors_abbrev":"Maghelli N et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2009-04-04","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7958849","title":"A heteromeric protein that binds to a meiotic homologous recombination hot spot: correlation of binding and hot spot activity.","citation":"Genes Dev 1994 Jul 15;8(14):1693-702","abstract":"Homologous recombination hot spots are DNA sites that increase the frequency of recombination in their vicinity. The M26 allele of the ade6 gene in Schizosaccharomyces pombe is the first meiotic hot spot with an identified unique nucleotide sequence. We have purified 40,000-fold a heteromeric protein, containing polypeptides Mts1 (70 kD) and Mts2 (28 kD), that binds to the M26 site. Binding in vitro strictly correlates with hot spot activity in vivo for numerous single base pair substitutions in the vicinity of the M26 site, indicating that Mts1/Mts2 activates the M26 site and promotes a rate-limiting step of meiotic recombination. These and other data suggest that homologous recombination may be regulated primarily by discrete DNA sites and proteins that interact with those sites.","authors":"Wahls WP, Smith GR","authors_abbrev":"Wahls WP et al.","pubmed_publication_date":"15 Jul 1994","pubmed_entrez_date":"1994-07-15","publication_year":"1994","canto_session_key":"2bc77ff7c20e1b16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-28 14:00:36","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-21 14:40:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC21E11.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-21"},{"uniquename":"PMID:15590684","title":"Specificity and mechanism of RNA cap guanine-N2 methyltransferase (Tgs1).","citation":"J Biol Chem 2005 Feb 11;280(6):4021-4","abstract":"The 2,2,7-trimethylguanosine (TMG) cap structure is characteristic of certain eukaryotic small nuclear and small nucleolar RNAs. Prior studies have suggested that cap trimethylation might be contingent on cis-acting elements in the RNA substrate, protein components of a ribonucleoprotein complex, or intracellular localization of the RNA substrate. However, the enzymatic requirements for TMG cap formation remain obscure because TMG synthesis has not been reconstituted in vitro from defined components. Tgs1 is a conserved eukaryal protein that was initially identified as being required for RNA cap trimethylation in vivo in budding yeast. Here we show that purified recombinant fission yeast Tgs1 catalyzes methyl transfer from S-adenosylmethionine (AdoMet) to m7GTP and m7GDP. Tgs1 also methylates the cap analog m(7)GpppA but is unreactive with GTP, GDP, GpppA, m2,2,7GTP, m2,2,7GDP, ATP, CTP, UTP, and ITP. The products of methyl transfer to m7GTP and m7GDP formed under conditions of excess methyl acceptor are 2,7-dimethyl GTP and 2,7-dimethyl GDP, respectively. Under conditions of limiting methyl acceptor, the initial m2,7GDP product is converted to m2,2,7GDP in the presence of excess AdoMet. We conclude that Tgs1 is guanine-specific, that N7 methylation must precede N2 methylation, that Tgs1 acts via a distributive mechanism, and that the chemical steps of TMG synthesis do not require input from RNA or protein cofactors.","authors":"Hausmann S, Shuman S","authors_abbrev":"Hausmann S et al.","pubmed_publication_date":"11 Feb 2005","pubmed_entrez_date":"2004-12-14","publication_year":"2005","canto_session_key":"52a81e6938e2dcac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2012-06-21 15:57:04","canto_session_submitted_date":"2012-06-18 10:48:18","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.15c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-06-18"},{"uniquename":"PMID:8416984","title":"Three-dimensional reconstruction and analysis of mitotic spindles from the yeast, Schizosaccharomyces pombe.","citation":"J Cell Biol 1993 Jan;120(1):141-51","abstract":"Mitotic spindles of Schizosaccharomyces pombe have been studied by EM, using serial cross sections to reconstruct 12 spindles from cells that were ultrarapidly frozen and fixed by freeze substitution. The resulting distributions of microtubules (MTs) have been analyzed by computer. Short spindles contain two kinds of MTs: continuous ones that run from pole to pole and MTs that originate at one pole and end in the body of the spindle. Among the latter there are three pairs of MT bundles that end on fibrous, darkly staining structures that we interpret as kinetochores. The number of MTs ending at each putative kinetochore ranges from two to four; all kinetochore-associated MTs disappear as the spindle elongates from 3-6 microns. At this and greater spindle lengths, there are no continuous MTs, only polar MTs that interdigitate at the spindle midzone, but the spindle continues to elongate. An analysis of the density of neighboring MTs at the midzone of long spindles shows that their most common spacing is approximately 40 nm, center to center, and that there is a preferred angular separation of 90 degrees. Only hints of such square-packing are found at the midzone of short spindles, and near the poles there is no apparent order at any mitotic stage. Our data suggest that the kinetochore MTs (KMTs) do not interact directly with nonkinetochore MTs, but that interdigitating MTs from the two spindle poles do interact to form a mechanically stable bundle that connects the poles. As the spindle elongates, the number of MTs decreases while the mean length of the MTs that remain increases. We conclude that the chromosomes of S. pombe become attached to the spindle by kinetochore MTs, that these MTs disappear as the chromosomes segregate, that increased separation of daughter nuclei is accompanied by a sliding apart of anti-parallel MTs, and that the mitotic processes of S. pombe are much like those in other eukaryotic cells.","authors":"Ding R, McDonald KL, McIntosh JR","authors_abbrev":"Ding R et al.","pubmed_publication_date":"Jan 1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32650974","title":"SpMnn9p and SpAnp1p form a protein complex involved in mannan synthesis in the fission yeast Schizosaccharomyces pombe.","citation":"J Biosci Bioeng 2020 Oct;130(4):335-340","abstract":"The cell walls of yeast cells possess a large mannan structure mainly comprising of a linear α1,6-linked mannose oligomer on the N-linked glycans. The biosynthesis of the mannan is initiated by ScOch1p α1,6-mannosyltransfease, and elongated by the mannan polymerase complexes M-Pol I and II in the Golgi of Saccharomyces cerevisiae. Here, we functionally characterized SpMnn9 and SpAnp1 proteins in the fission yeast Schizosaccharomyces pombe; these proteins are homologs of S. cerevisiae M-Pol II complex proteins ScMnn9p and ScAnp1p. Cells harboring disruptions in Spmnn9 +  and Spanp1 +  genes showed slower growth at 37°C and an increased sensitivity to hygromycin B, characteristic of a glycosylation defect. Results obtained from the acid phosphatase assay and high-performance liquid chromatography analysis of N-linked glycans in Spmnn9Δ and Spanp1Δ mutants suggested that the mannan structure in S. pombe is synthesized sequentially by the α-mannosyltransferases in the order of SpOch1p, SpMnn9p and SpAnp1p. Immunoprecipitation and split YFP analyses demonstrated that SpMnn9p and SpAnp1p form the M-Pol-II like complex. Together, these results provided an improved understanding of the mechanism of mannan synthesis by SpMnn9p and SpAnp1p in S. pombe.","doi":"10.1016/j.jbiosc.2020.06.003","authors":"Ohashi T, Tanaka T, Tanaka N, Takegawa K","authors_abbrev":"Ohashi T et al.","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-07-12","publication_year":"2020","canto_session_key":"734a10ae784c8c6b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2020-07-22 09:40:34","canto_approved_date":"2026-01-25 05:47:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-07-21 02:06:00","canto_added_date":"2020-07-13 00:15:05","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F10.10c","SPAC1006.05c","SPBC1734.04"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-07-22"},{"uniquename":"PMID:11290708","title":"Fission yeast Mog1p homologue, which interacts with the small GTPase Ran, is required for mitosis-to-interphase transition and poly(A)(+) RNA metabolism.","citation":"Genetics 2001 Apr;157(4):1513-22","abstract":"We have cloned and characterized the Schizosaccharomyces pombe gene mog1(+), which encodes a protein with homology to the Saccharomyces cerevisiae Mog1p participating in the Ran-GTPase system. The S. pombe Mog1p is predominantly localized in the nucleus. In contrast to the S. cerevisiae MOG1 gene, the S. pombe mog1(+) gene is essential for cell viability. mog1(+) is required for the mitosis-to-interphase transition, as the mog1-1 mutant arrests at restrictive temperatures as septated, binucleated cells with highly condensed chromosomes and an aberrant nuclear envelope. FACS analysis showed that these cells do not undergo a subsequent round of DNA replication. Surprisingly, also unlike the Delta mog1 mutation in S. cerevisiae, the mog1-1 mutation causes nucleolar accumulation of poly(A)(+) RNA at the restrictive temperature in S. pombe, but the signals do not overlap with the fibrillarin-rich region of the nucleolus. Thus, we found that mog1(+) is required for the mitosis-to-interphase transition and a class of RNA metabolism. In our attempt to identify suppressors of mog1-1, we isolated the spi1(+) gene, which encodes the fission yeast homologue of Ran. We found that overexpression of Spi1p rescues the S. pombe Delta mog1 cells from death. On the basis of these results, we conclude that mog1(+) is involved in the Ran-GTPase system.","authors":"Tatebayashi K, Tani T, Ikeda H","authors_abbrev":"Tatebayashi K et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-04-06","publication_year":"2001","canto_session_key":"01c913b208de3dfb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-01-25 12:30:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-28 14:59:44","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1289.03c","SPCC1840.01c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-28"},{"uniquename":"PMID:28134253","title":"Specialized interfaces of Smc5/6 control hinge stability and DNA association.","citation":"Nat Commun 2017 Jan 30;8:14011","abstract":"The Structural Maintenance of Chromosomes (SMC) complexes: cohesin, condensin and Smc5/6 are involved in the organization of higher-order chromosome structure-which is essential for accurate chromosome duplication and segregation. Each complex is scaffolded by a specific SMC protein dimer (heterodimer in eukaryotes) held together via their hinge domains. Here we show that the Smc5/6-hinge, like those of cohesin and condensin, also forms a toroidal structure but with distinctive subunit interfaces absent from the other SMC complexes; an unusual 'molecular latch' and a functional 'hub'. Defined mutations in these interfaces cause severe phenotypic effects with sensitivity to DNA-damaging agents in fission yeast and reduced viability in human cells. We show that the Smc5/6-hinge complex binds preferentially to ssDNA and that this interaction is affected by both 'latch' and 'hub' mutations, suggesting a key role for these unique features in controlling DNA association by the Smc5/6 complex.","doi":"10.1038/ncomms14011","authors":"Alt A, Dang HQ, Wells OS, Polo LM, Smith MA, McGregor GA, Welte T, Lehmann AR, Pearl LH, Murray JM, Oliver AW","authors_abbrev":"Alt A et al.","pubmed_publication_date":"30 Jan 2017","pubmed_entrez_date":"2017-01-31","publication_year":"2017","canto_session_key":"d6ffc50086d4a7b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-01-18 16:32:13","canto_approved_date":"2023-08-03 11:02:11","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2018-01-15 13:30:30","canto_added_date":"2017-02-01 01:15:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":48,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.02c","SPCC5E4.06"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-01-18","pdb_entries":[{"pdb_id":"5mg8","gene_chains":[{"gene_uniquename":"SPAC14C4.02c","chain":"A/C","position":"366-692"},{"gene_uniquename":"SPCC5E4.06","chain":"B/D","position":"448-720"}],"title":"Crystal structure of the S.pombe Smc5/6 hinge domain","entry_authors":"Alt A,Pearl LH,Oliver AW","entry_authors_abbrev":"Alt A et al.","reference_uniquename":"PMID:28134253","experimental_method":"X-ray","resolution":"2.75"}]},{"uniquename":"PMID:32690950","title":"STEEP mediates STING ER exit and activation of signaling.","citation":"Nat Immunol 2020 Aug;21(8):868-879","abstract":"STING is essential for control of infections and for tumor immunosurveillance, but it can also drive pathological inflammation. STING resides on the endoplasmic reticulum (ER) and traffics following stimulation to the ERGIC/Golgi, where signaling occurs. Although STING ER exit is the rate-limiting step in STING signaling, the mechanism that drives this process is not understood. Here we identify STEEP as a positive regulator of STING signaling. STEEP was associated with STING and promoted trafficking from the ER. This was mediated through stimulation of phosphatidylinositol-3-phosphate (PtdIns(3)P) production and ER membrane curvature formation, thus inducing COPII-mediated ER-to-Golgi trafficking of STING. Depletion of STEEP impaired STING-driven gene expression in response to virus infection in brain tissue and in cells from patients with STING-associated diseases. Interestingly, STING gain-of-function mutants from patients interacted strongly with STEEP, leading to increased ER PtdIns(3)P levels and membrane curvature. Thus, STEEP enables STING signaling by promoting ER exit.","doi":"10.1038/s41590-020-0730-5","authors":"Zhang BC, Nandakumar R, Reinert LS, Huang J, Laustsen A, Gao ZL, Sun CL, Jensen SB, Troldborg A, Assil S, Berthelsen MF, Scavenius C, Zhang Y, Windross SJ, Olagnier D, Prabakaran T, Bodda C, Narita R, Cai Y, Zhang CG, Stenmark H, Doucet CM, Noda T, Guo Z, Goldbach-Mansky R, Hartmann R, Chen ZJ, Enghild JJ, Bak RO, Thomsen MK, Paludan SR","authors_abbrev":"Zhang BC et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-07-22","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC839.19"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPC06392","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.120"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU012818","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23177192","title":"Stable isotope-labeled Raman imaging reveals dynamic proteome localization to lipid droplets in single fission yeast cells.","citation":"Chem Biol 2012 Nov 21;19(11):1373-80","abstract":"Lipid droplets have been hypothesized to be intimately associated with intracellular proteins. However, there is little direct evidence for both spatiotemporal and functional relations between lipid droplets and proteins provided by molecular-level studies on intact cells. Here, we present in vivo time-lapse Raman imaging, coupled with stable-isotope ((13)C) labeling, of single living Schizosaccharomyces pombe cells. Using characteristic Raman bands of proteins and lipids, we dynamically visualized the process by which (13)C-glucose in the medium was assimilated into those intracellular components. Our results show that the proteins newly synthesized from incorporated (13)C-substrate are localized specifically to lipid droplets as the lipid concentration within the cell increases. We demonstrate that the present method offers a unique platform for proteome visualization without the need for tagging individual proteins with fluorescent probes.","doi":"10.1016/j.chembiol.2012.08.020","authors":"Noothalapati Venkata HN, Shigeto S","authors_abbrev":"Noothalapati Venkata HN et al.","pubmed_publication_date":"21 Nov 2012","pubmed_entrez_date":"2012-11-27","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12673626","title":"Characterization and behaviour of alpha-glucan synthase in Schizosaccharomyces pombe as revealed by electron microscopy.","citation":"Yeast 2003 Apr 15;20(5):427-38","abstract":"Alpha-1,3-Glucan is a cell wall component in Schizosaccharomyces pombe and is exclusive to budding yeast. We analysed the ultrastructure of the cell wall in the alpha-glucan synthase mutant mok1 and determined the role of alpha-1,3-glucan in cell wall formation of Sz. pombe. The mok1 mutant cell has an abnormal shape, with swelling at the tip or at the site of the septum. The cell wall is thicker and looser than that of wild-type cells, and the layered structure of the cell wall is broken. The glucan fibrils forming the protoplast retain a fine fibril structure, although their development into bundles is abnormal. We also report the localization of Mok1p by immunoelectron microscopy using high-pressure freeze substitution and SDS-digested freeze-fracture replica labelling methods. The Mok1p is localized on the cell membrane and moves from the cell tip to the medial region during the cell cycle. These results confirm that Mok1p plays an important role in the normal construction of the cell wall and in the primary step of glucan bundle formation, and that it is required for new cell wall synthesis during vegetative growth. These findings suggest that alpha-1,3-glucan is an essential component for cell wall formation in fission yeast.","authors":"Konomi M, Fujimoto K, Toda T, Osumi M","authors_abbrev":"Konomi M et al.","pubmed_publication_date":"15 Apr 2003","pubmed_entrez_date":"2003-04-04","publication_year":"2003","canto_session_key":"0fab6f36545c4102","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-18 17:47:31","canto_approved_date":"2022-09-18 17:47:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-18 17:47:25","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1281.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-09-18"},{"uniquename":"PMID:18790078","title":"Perturbation of HP1 localization and chromatin binding ability causes defects in sister-chromatid cohesion.","citation":"Mutat Res 2008 Nov 17;657(1):48-55","abstract":"Sister-chromatid cohesion, the machinery used in eukaryote organisms to prevent aneuploidy, tethers sister chromatids together after their replication in S phase until mitosis. Previous studies in fission yeast, Drosophila and mammals have demonstrated the requirement for the heterochromatin formation pathway for proper centromeric cohesion. However, the exact role of heterochromatin protein 1 (HP1) in sister-chromatid cohesion in mammals is still unknown. In this study, we disrupted endogenous HP1 expression in HeLa cells using a dominant-negative mutant of HP1beta and wild-type or mutant forms of HP1alpha. We then examined their effects on chromosome alignment, segregation and cohesion. Enforced expression of these constructs leads to frequent chromosome misalignment and missegregation. Mitotic chromosomes from these cells also exhibit a loosened primary constriction and separated sister chromatids. We further demonstrate that alignment of the cohesin proteins around kinetochores was also aberrant and that cohesin complexes bound less tightly in these cells. Unexpectedly, we observed a \"wavy\" chromosome morphology resembling that seen upon depletion of condensin proteins in cells with over-expression of HP1alpha, but not in cells expressing the HP1beta mutant. These results indicate that proper HP1 status is required for sister-chromatid cohesion in mammalian cells, and suggest that HP1alpha might be required for chromosome condensation.","doi":"10.1016/j.mrgentox.2008.08.010","authors":"Inoue A, Hyle J, Lechner MS, Lahti JM","authors_abbrev":"Inoue A et al.","pubmed_publication_date":"17 Nov 2008","pubmed_entrez_date":"2008-09-16","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31366733","title":"Structures of CENP-C cupin domains at regional centromeres reveal unique patterns of dimerization and recruitment functions for the inner pocket.","citation":"J Biol Chem 2019 Sep 20;294(38):14119-14134","abstract":"The successful assembly and regulation of the kinetochore are critical for the equal and accurate segregation of genetic material during the cell cycle. CENP-C (centromere protein C), a conserved inner kinetochore component, has been broadly characterized as a scaffolding protein and is required for the recruitment of multiple kinetochore proteins to the centromere. At its C terminus, CENP-C harbors a conserved cupin domain that has an established role in protein dimerization. Although the crystal structure of the  Saccharomyces cerevisiae  Mif2 CENP-C  cupin domain has been determined, centromeric organization and kinetochore composition vary greatly between  S. cerevisiae  (point centromere) and other eukaryotes (regional centromere). Therefore, whether the structural and functional role of the cupin domain is conserved throughout evolution requires investigation. Here, we report the crystal structures of the  Schizosaccharomyces pombe  and  Drosophila melanogaster  CENP-C cupin domains at 2.52 and 1.81 Å resolutions, respectively. Although the central jelly roll architecture is conserved among the three determined CENP-C cupin domain structures, the cupin domains from organisms with regional centromeres contain additional structural features that aid in dimerization. Moreover, we found that the  S. pombe  Cnp3 CENP-C  jelly roll fold harbors an inner binding pocket that is used to recruit the meiosis-specific protein Moa1. In summary, our results unveil the evolutionarily conserved and unique features of the CENP-C cupin domain and uncover the mechanism by which it functions as a recruitment factor.","doi":"10.1074/jbc.RA119.008464","authors":"Chik JK, Moiseeva V, Goel PK, Meinen BA, Koldewey P, An S, Mellone BG, Subramanian L, Cho US","authors_abbrev":"Chik JK et al.","pubmed_publication_date":"20 Sep 2019","pubmed_entrez_date":"2019-08-02","publication_year":"2019","canto_session_key":"39d20d8889ee33d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-09-27 16:17:20","canto_approved_date":"2023-03-14 18:07:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-09-27 16:17:12","canto_added_date":"2019-08-03 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1861.01c","SPAC15E1.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-09-27","pdb_entries":[{"pdb_id":"6o2d","gene_chains":[{"gene_uniquename":"SPBC1861.01c","chain":"A/B","position":"489-643"}],"title":"Schizosaccharomyces pombe Cnp3 Cupin Domain","entry_authors":"Chik JK,Cho US","entry_authors_abbrev":"Chik JK et al.","reference_uniquename":"PMID:31366733","experimental_method":"X-ray","resolution":"2.52"}]},{"uniquename":"PMID:33624650","title":"Fast confocal Raman imaging via context-aware compressive sensing.","citation":"Analyst 2021 Apr 07;146(7):2348-2357","abstract":"Raman hyperspectral imaging is a powerful method to obtain detailed chemical information about a wide variety of organic and inorganic samples noninvasively and without labels. However, due to the weak, nonresonant nature of spontaneous Raman scattering, acquiring a Raman imaging dataset is time-consuming and inefficient. In this paper we utilize a compressive imaging strategy coupled with a context-aware image prior to improve Raman imaging speed by 5- to 10-fold compared to classic point-scanning Raman imaging, while maintaining the traditional benefits of point scanning imaging, such as isotropic resolution and confocality. With faster data acquisition, large datasets can be acquired in reasonable timescales, leading to more reliable downstream analysis. On standard samples, context-aware Raman compressive imaging (CARCI) was able to reduce the number of measurements by ∼85% while maintaining high image quality (SSIM >0.85). Using CARCI, we obtained a large dataset of chemical images of fission yeast cells, showing that by collecting 5-fold more cells in a given experiment time, we were able to get more accurate chemical images, identification of rare cells, and improved biochemical modeling. For example, applying VCA to nearly 100 cells' data together, cellular organelles were resolved that were not faithfully reconstructed by a single cell's dataset.","doi":"10.1039/d1an00088h","authors":"Hu C, Wang X, Liu L, Fu C, Chu K, Smith ZJ","authors_abbrev":"Hu C et al.","pubmed_publication_date":"07 Apr 2021","pubmed_entrez_date":"2021-02-24","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-02-26 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24514900","title":"Membrane organization and cell fusion during mating in fission yeast requires multipass membrane protein Prm1.","citation":"Genetics 2014 Apr;196(4):1059-76","abstract":"The involvement of Schizosaccharomyces pombe prm1(+) in cell fusion during mating and its relationship with other genes required for this process have been addressed. S. pombe prm1Δ mutant exhibits an almost complete blockade in cell fusion and an abnormal distribution of the plasma membrane and cell wall in the area of cell-cell interaction. The distribution of cellular envelopes is similar to that described for mutants devoid of the Fig1-related claudin-like Dni proteins; however, prm1(+) and the dni(+) genes act in different subpathways. Time-lapse analyses show that in the wild-type S. pombe strain, the distribution of phosphatidylserine in the cytoplasmic leaflet of the plasma membrane undergoes some modification before an opening is observed in the cross wall at the cell-cell contact region. In the prm1Δ mutant, this membrane modification does not take place, and the cross wall between the mating partners is not extensively degraded; plasma membrane forms invaginations and fingers that sometimes collapse/retract and that are sometimes strengthened by the synthesis of cell-wall material. Neither prm1Δ nor prm1Δ dniΔ zygotes lyse after cell-cell contact in medium containing and lacking calcium. Response to drugs that inhibit lipid synthesis or interfere with lipids is different in wild-type, prm1Δ, and dni1Δ strains, suggesting that membrane structure/organization/dynamics is different in all these strains and that Prm1p and the Dni proteins exert some functions required to guarantee correct membrane organization that are critical for cell fusion.","doi":"10.1534/genetics.113.159558","authors":"Curto MÁ, Sharifmoghadam MR, Calpena E, De León N, Hoya M, Doncel C, Leatherwood J, Valdivieso MH","authors_abbrev":"Curto MÁ et al.","pubmed_publication_date":"Apr 2014","pubmed_entrez_date":"2014-02-12","publication_year":"2014","canto_session_key":"6dda6bff1b0363f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Henar Valdivieso","canto_first_approved_date":"2017-02-07 12:30:55","canto_approved_date":"2026-05-25 01:13:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-05 15:53:46","canto_added_date":"2014-02-16 05:46:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Henar Valdivieso","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.09","SPAC6G9.12","SPBC4.01","SPAC20G4.02c","SPAP7G5.03","SPAC31G5.07"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-02-07"},{"uniquename":"PMID:12297001","title":"Transcription of Schizosaccharomyces pombe thioltransferase-1 in response to stress conditions.","citation":"J Biochem Mol Biol 2002 Jul 31;35(4):409-13","abstract":"Thioltransferase, also known as glutaredoxin, is an enzyme that catalyzes the reduction of a variety of disulfide compounds. In Schizosaccharomyces pombe, two thioltransferases were reported and the cDNA of one of the thioltransferases (thioltransferase-1) was cloned. Using a Northern blot assay, we investigated the thioltransferase transcription in response to various stress conditions. When the culture was shifted to a high temperature, the thioltransferase transcription was not significantly changed compared to the unshifted 30 degrees culture. Treatment of zinc chloride to exponentially-growing cells remarkably increased the thioltransferase transcription, whereas the treatment of mercury chloride greatly reduced the transcription. Treatment of hydrogen peroxide and cadmium chloride caused no significant effects on the transcription of the thioltransferase. These results suggest that the transcription of thioltransferase-1 in S. pombe is induced in response to metal stress that is caused by zinc chloride, but not in response to heat stress or oxidative stress that is caused by hydrogen peroxide.","authors":"Kim M, Lim CJ, Kim D","authors_abbrev":"Kim M et al.","pubmed_publication_date":"31 Jul 2002","pubmed_entrez_date":"2002-09-26","publication_year":"2002","canto_session_key":"d4f2d072b42bd751","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-11-07 11:51:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 09:48:06","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.20"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-11-05"},{"uniquename":"PMID:23398982","title":"Role of the fission yeast cell integrity MAPK pathway in response to glucose limitation.","citation":"BMC Microbiol 2013 Feb 11;13:34","abstract":"Glucose is a signaling molecule which regulates multiple events in eukaryotic organisms and the most preferred carbon source in the fission yeast Schizosaccharomyces pombe. The ability of this yeast to grow in the absence of glucose becomes strongly limited due to lack of enzymes of the glyoxylate cycle that support diauxic growth. The stress-activated protein kinase (SAPK) pathway and its effectors, Sty1 MAPK and transcription factor Atf1, play a critical role in the adaptation of fission yeast to grow on alternative non-fermentable carbon sources by inducing the expression of fbp1+ gene, coding for the gluconeogenic enzyme fructose-1,6-bisphosphatase. The cell integrity Pmk1 pathway is another MAPK cascade that regulates various processes in fission yeast, including cell wall construction, cytokinesis, and ionic homeostasis. Pmk1 pathway also becomes strongly activated in response to glucose deprivation but its role during glucose exhaustion and ensuing adaptation to respiratory metabolism is currently unknown.\nWe found that Pmk1 activation in the absence of glucose takes place only after complete depletion of this carbon source and that such activation is not related to an endogenous oxidative stress. Notably, Pmk1 MAPK activation relies on de novo protein synthesis, is independent on known upstream activators of the pathway like Rho2 GTPase, and involves PKC ortholog Pck2. Also, the Glucose/cAMP pathway is required operative for full activation of the Pmk1 signaling cascade. Mutants lacking Pmk1 displayed a partial growth defect in respiratory media which was not observed in the presence of glucose. This phenotype was accompanied by a decreased and delayed expression of transcription factor Atf1 and target genes fbp1+ and pyp2+. Intriguingly, the kinetics of Sty1 activation in Pmk1-less cells was clearly altered during growth adaptation to non-fermentable carbon sources.\nUnknown upstream elements mediate Pck2-dependent signal transduction of glucose withdrawal to the cell integrity MAPK pathway. This signaling cascade reinforces the adaptive response of fission yeast to such nutritional stress by enhancing the activity of the SAPK pathway.","doi":"10.1186/1471-2180-13-34","authors":"Madrid M, Fernández-Zapata J, Sánchez-Mir L, Soto T, Franco A, Vicente-Soler J, Gacto M, Cansado J","authors_abbrev":"Madrid M et al.","pubmed_publication_date":"11 Feb 2013","pubmed_entrez_date":"2013-02-13","publication_year":"2013","canto_session_key":"96f7ea3d68c1073c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11791349","title":"Identification of Schizosaccharomyces pombe genes that encode putative homologues of Saccharomyces cerevisiae mediator complex subunits.","citation":"Acta Microbiol Immunol Hung 2001;48(3-4):519-31","abstract":"The mediator complexes transduce regulatory information from upstream regulatory elements to the transcription machinery in organisms ranging from yeasts to humans. By a genome-wide search we identified 14 ORFs and genes in the genome of the fission yeast Schizosaccharomyces pombe that encode putative homologues of Saccharomyces cerevisiae mediator subunits. The Sch. pombe proteins are smaller and appear to form a mediator of lower complexity, which is consistent with the hypothesized ancient origin of fission yeasts.","authors":"Sipiczki M","authors_abbrev":"Sipiczki M","pubmed_publication_date":"2001","pubmed_entrez_date":"2002-01-17","publication_year":"2001","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30759079","title":"A systematic genetic screen identifies essential factors involved in nuclear size control.","citation":"PLoS Genet 2019 Feb;15(2):e1007929","abstract":"Nuclear size correlates with cell size, but the mechanism by which this scaling is achieved is not known. Here we screen fission yeast gene deletion mutants to identify essential factors involved in this process. Our screen has identified 25 essential factors that alter nuclear size, and our analysis has implicated RNA processing and LINC complexes in nuclear size control. This study has revealed lower and more extreme higher nuclear size phenotypes and has identified global cellular processes and specific structural nuclear components important for nuclear size control.","doi":"10.1371/journal.pgen.1007929","authors":"Cantwell H, Nurse P","authors_abbrev":"Cantwell H et al.","pubmed_publication_date":"Feb 2019","pubmed_entrez_date":"2019-02-14","publication_year":"2019","canto_session_key":"23ea57b8910e06c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2019-06-29 18:49:51","canto_approved_date":"2022-08-29 15:54:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-11 16:00:24","canto_added_date":"2019-02-15 01:15:04","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":30,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.14","SPBC11C11.03","SPAC6G9.02c","SPAC1B3.09c","SPAP8A3.06","SPBC19C2.08","SPAP27G11.13c","SPAC2G11.08c","SPBC21.01","SPBC4B4.05","SPAC1F3.01","SPBC336.08","SPBC428.01c","SPAC1006.02","SPBC12D12.01","SPCC330.10","SPCC1450.13c","SPAC7D4.09c","SPBC18H10.14","SPAC1783.03","SPCC1223.08c","SPBC947.12","SPBC1709.15c","SPBC8D2.09c","SPBC32H8.10","SPAC821.08c","SPBC29A3.04","SPBC30B4.07c","SPBC4.03c"],"gene_count":29,"ltp_gene_count":29,"approved_date":"2019-06-29"},{"uniquename":"PMID:10541858","title":"Rpc19 and Rpc40, two alpha-like subunits shared by nuclear RNA polymerases I and III, are interchangeable between the fission and budding yeasts.","citation":"Curr Genet 1999 Oct;36(4):208-14","abstract":"The cDNAs and genes encoding the common subunits Rpc19 and Rpc40 of nuclear RNA polymerases I and III of Schizosaccharomyces pombe were isolated from cDNA and genomic libraries of the fission yeast and tested for their ability to substitute for the homologous genes in Saccharomyces cerevisiae by heterospecific complementation of corresponding null alleles and temperature-sensitive mutations. The results obtained indicate that both Sz. pombe genes (rpc19(+) and rpc40(+)) are able to replace their S. cerevisiae counterparts in vivo. The primary structure and general organization of both genes were established: rpc40(+) is an intronless gene, while rpc19(+) contains three introns (73, 48 and 77 bp long); rpc19(+) is situated on the long arm of chromosome I and rpc40(+) on the long arm of chromosome II.","authors":"Shpakovski GV, Shematorova EK","authors_abbrev":"Shpakovski GV et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-12-14","publication_year":"1999","canto_session_key":"de09f772ed1edfbe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-30 11:11:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 11:11:49","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1289.07c","SPAC1687.01"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2014-06-30"},{"uniquename":"PMID:23615447","title":"Compartmentalized nodes control mitotic entry signaling in fission yeast.","citation":"Mol Biol Cell 2013 Jun;24(12):1872-81","abstract":"Cell cycle progression is coupled to cell growth, but the mechanisms that generate growth-dependent cell cycle progression remain unclear. Fission yeast cells enter into mitosis at a defined size due to the conserved cell cycle kinases Cdr1 and Cdr2, which localize to a set of cortical nodes in the cell middle. Cdr2 is regulated by the cell polarity kinase Pom1, suggesting that interactions between cell polarity proteins and the Cdr1-Cdr2 module might underlie the coordination of cell growth and division. To identify the molecular connections between Cdr1/2 and cell polarity, we performed a comprehensive pairwise yeast two-hybrid screen. From the resulting interaction network, we found that the protein Skb1 interacted with both Cdr1 and the Cdr1 inhibitory target Wee1. Skb1 inhibited mitotic entry through negative regulation of Cdr1 and localized to both the cytoplasm and a novel set of cortical nodes. Skb1 nodes were distinct structures from Cdr1/2 nodes, and artificial targeting of Skb1 to Cdr1/2 nodes delayed entry into mitosis. We propose that the formation of distinct node structures in the cell cortex controls signaling pathways to link cell growth and division.","doi":"10.1091/mbc.E13-02-0104","authors":"Deng L, Moseley JB","authors_abbrev":"Deng L et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-04-26","publication_year":"2013","canto_session_key":"84eb3730ad79951e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4F11.02","SPAC16C9.07","SPAC16E8.09","SPAC12B10.14c","SPAC110.03","SPBC1604.14c","SPAC24H6.05","SPBC28E12.03","SPAC22H10.07","SPAC1834.06c","SPCC1223.06","SPCC18B5.03","SPBC16H5.11c","SPAC644.06c","SPAC2F7.03c","SPBC23G7.04c","SPAC821.12","SPBP19A11.04c","SPCC24B10.13","SPBC1604.20c","SPAC3C7.12","SPBC17F3.02","SPCC970.04c","SPBC1706.01"],"gene_count":24,"ltp_gene_count":24},{"uniquename":"PMID:22840513","title":"Contributions of turgor pressure, the contractile ring, and septum assembly to forces in cytokinesis in fission yeast.","citation":"Curr Biol 2012 Sep 11;22(17):1601-8","abstract":"A paradigm of cytokinesis in animal cells is that the actomyosin contractile ring provides the primary force to divide the cell. In the fission yeast Schizosaccharomyces pombe, cytokinesis also involves a conserved cytokinetic ring, which has been generally assumed to provide the force for cleavage (see also [5]). However, in contrast to animal cells, cytokinesis in yeast cells also requires the assembly of a cell wall septum, which grows centripetally inward as the ring closes. Fission yeast, like other walled cells, also possess high (MPa) turgor pressure. Here, we show that turgor pressure is an important factor in the mechanics of cytokinesis. Decreasing effective turgor pressure leads to an increase in cleavage rate, suggesting that the inward force generated by the division apparatus opposes turgor pressure. The contractile ring, which is predicted to provide only a tiny fraction of the mechanical stress required to overcome turgor, is largely dispensable for ingression; once septation has started, cleavage can continue in the absence of the contractile ring. Scaling arguments and modeling suggest that the large forces for cytokinesis are not produced by the contractile ring but are driven by the assembly of cell wall polymers in the growing septum.","doi":"10.1016/j.cub.2012.06.042","authors":"Proctor SA, Minc N, Boudaoud A, Chang F","authors_abbrev":"Proctor SA et al.","pubmed_publication_date":"11 Sep 2012","pubmed_entrez_date":"2012-07-31","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11156603","title":"Multiple roles for the yeast SUB2/yUAP56 gene in splicing.","citation":"Genes Dev 2001 Jan 01;15(1):36-41","abstract":"The UAP56 gene has been shown to be required for prespliceosome assembly in mammals. We report here the isolation of the Schizosaccharomyces pombe ortholog of this gene by heterologous complementation of a combined PRP40HA(3)/nam8Delta defect in budding yeast. The Saccharomyces cerevisiae ortholog, YDL084w/SUB2, is also able to suppress this defect. We show that SUB2 is involved in splicing in vivo as well as in vitro. Sub2 defective extracts form a stalled intermediate that contains U2snRNP and can be chased into functional spliceosomes. Our experiments also suggest a role for this protein in events that precede prespliceosome formation. Data reported here as well as in the accompanying papers strongly implicate Sub2p in multiple steps of the spliceosome assembly process.","authors":"Libri D, Graziani N, Saguez C, Boulay J","authors_abbrev":"Libri D et al.","pubmed_publication_date":"01 Jan 2001","pubmed_entrez_date":"2001-01-13","publication_year":"2001","canto_session_key":"8d939ccd33b56651","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-06-12 08:38:37","canto_approved_date":"2018-06-12 08:38:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 08:38:25","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G6.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-12"},{"uniquename":"PMID:15265989","title":"Activation of the pheromone-responsive MAP kinase drives haploid cells to undergo ectopic meiosis with normal telomere clustering and sister chromatid segregation in fission yeast.","citation":"J Cell Sci 2004 Aug 01;117(Pt 17):3875-86","abstract":"Meiosis is a process of importance for sexually reproducing eukaryotic organisms. In the fission yeast Schizosaccharomyces pombe, meiosis normally proceeds in a diploid zygote which is produced by conjugation of haploid cells of opposite mating types. We demonstrate that activation of the pheromone-responsive MAPK, Spk1, by the ectopic expression of a constitutively active form of Byr1 (MAPKK for Spk1) induced the cells to undergo meiosis while in the haploid state. Moreover, the induction of meiosis required Mei2 (a key positive regulator of meiosis), but did not require Mei3; Mei3 is normally required to inactivate the Pat1 kinase (a negative regulator of Mei2) thereby allowing Mei2 to drive meiosis. Therefore, expression of a constitutively active form of Byr1 activates Mei2 without the need of Mei3. In cells induced to undergo meiosis by activating the Spk1 MAPK signaling pathway, telomeres clustered at the spindle pole body (SPB) and centromeres detached normally from the SPB during meiotic prophase, and the cells showed the correct segregation of sister chromatids during meiotic divisions. In contrast, in meiosis induced by inactivation of Pat1, sister chromatids segregate precociously during the first meiotic division. Thus, these results suggest that activation of Spk1 drives meiosis in S. pombe.","authors":"Yamamoto TG, Chikashige Y, Ozoe F, Kawamukai M, Hiraoka Y","authors_abbrev":"Yamamoto TG et al.","pubmed_publication_date":"01 Aug 2004","pubmed_entrez_date":"2004-07-22","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ251853","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPD159","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1960723","title":"Characterization of the POL3 gene product from Schizosaccharomyces pombe indicates inter-species conservation of the catalytic subunit of DNA polymerase delta.","citation":"J Mol Biol 1991 Nov 20;222(2):209-18","abstract":"The Schizosaccharomyces pombe POL3 gene was isolated by sequence homology with a region of the Saccharomyces cerevisiae POL3 gene, the only gene sequenced to date encoding the catalytic subunit of eukaryotic DNA polymerase delta. The fission yeast POL3 gene contains a 52 base-pair (bp) intron and encodes a 3600 bp transcript the 5'-end of which is located 32 bp upstream from the initiation codon. The polypeptides predicted from budding and fission yeast POL3 genes share 52% of conserved amino acid residues and have a 60% identical central region. This structural conservation of the catalytic subunit of DNA polymerases delta is probably related to functional constraints. A portion of the most conserved region was used to raise antibodies against an S. pombe polymerase delta/beta-galactosidase fusion protein expressed in Escherichia coli. The purified antibodies recognized a 123,000 Da protein in S. pombe wild-type cell extracts and inhibited an aphidicolin-sensitive DNA polymerase activity that was distinct from DNA polymerase alpha. The antibodies also detected a 140,000 Da protein in extracts from different proliferating mammalian cells, indicating that the catalytic subunits of DNA polymerase delta are highly conserved between yeast and higher eukaryotes.","authors":"Pignède G, Bouvier D, de Recondo AM, Baldacci G","authors_abbrev":"Pignède G et al.","pubmed_publication_date":"20 Nov 1991","pubmed_entrez_date":"1991-11-20","publication_year":"1991","canto_session_key":"8fd174764097b28e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:31:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 17:11:54","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.04"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-25"},{"uniquename":"PMID:8887647","title":"Fission yeast mal2+ is required for chromosome segregation.","citation":"Mol Cell Biol 1996 Nov;16(11):6169-77","abstract":"By a screen designed to isolate new fission yeast genes required for chromosome segregation, we have identified mal2+. The conditionally lethal mal2-1 allele gives rise to increased loss of a nonessential minichromosome at the permissive temperature and leads to severe missegregation of the chromosomes at the nonpermissive temperature. Cloning by complementation and subsequent sequence analysis revealed that mal2 is a novel protein with a mass of 34 kDa. Cells containing a mal2 null allele were inviable, indicating that mal2+ is an essential gene. Fusion of mal2 protein to the green fluorescent protein (GFP) showed that mal2 was predominantly localized in the nucleus. Sensitivity to microtubule-destabilizing drugs and strong genetic interactions with alpha1-tubulin suggest an interaction of the mal2 protein with the microtubule system. Spindle formation and elongation were not detectably affected in the mal2-1 mutant as determined by indirect immunofluorescence. However, anomalous chromosome movement on the spindle leading to aberrant distribution of the chromosomal material was observed.","authors":"Fleig U, Sen-Gupta M, Hegemann JH","authors_abbrev":"Fleig U et al.","pubmed_publication_date":"Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_session_key":"ec1e2e8292ae5f6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-02 17:46:57","canto_approved_date":"2021-02-11 11:04:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 12:39:40","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPAC25B8.14","SPBC26H8.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-03-02"},{"uniquename":"PMID:20016260","title":"Cdc48 connects with eIF3.","citation":"Cell Cycle 2010 Jan 01;9(1):24-5","abstract":"","authors":"Kriegenburg F, Hartmann-Petersen R","authors_abbrev":"Kriegenburg F et al.","pubmed_publication_date":"01 Jan 2010","pubmed_entrez_date":"2009-12-18","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25010571","title":"Unexpected similarities between the Schizosaccharomyces and human blood metabolomes, and novel human metabolites.","citation":"Mol Biosyst 2014 Oct;10(10):2538-51","abstract":"Metabolomics, a modern branch of chemical biology, provides qualitative and quantitative information about the metabolic states of organisms or cells at the molecular level. Here we report non-targeted, metabolomic analyses of human blood, using liquid chromatography-mass spectrometry (LC-MS). We compared the blood metabolome to the previously reported metabolome of the fission yeast, Schizosaccharomyces pombe. The two metabolomic datasets were highly similar: 101 of 133 compounds identified in human blood (75%) were also present in S. pombe, and 45 of 57 compounds enriched in red blood cells (RBCs) (78%) were also present in yeast. The most abundant metabolites were ATP, glutathione, and glutamine. Apart from these three, the next most abundant metabolites were also involved in energy metabolism, anti-oxidation, and amino acid metabolism. We identified fourteen new blood compounds, eight of which were enriched in RBCs: citramalate, GDP-glucose, trimethyl-histidine, trimethyl-phenylalanine, trimethyl-tryptophan, trimethyl-tyrosine, UDP-acetyl-glucosamine, UDP-glucuronate, dimethyl-lysine, glutamate methyl ester, N-acetyl-(iso)leucine, N-acetyl-glutamate, N2-acetyl-lysine, and N6-acetyl-lysine. Ten of the newly identified blood metabolites were also detected in S. pombe, and ten of the 14 newly identified blood metabolites were methylated or acetylated amino acids. Trimethylated or acetylated free amino acids were also abundant in white blood cells. It may be possible to investigate their physiological roles using yeast genetics.","doi":"10.1039/c4mb00346b","authors":"Chaleckis R, Ebe M, Pluskal T, Murakami I, Kondoh H, Yanagida M","authors_abbrev":"Chaleckis R et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-07-11","publication_year":"2014","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-07-12 00:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15772152","title":"Effects of {gamma}-tubulin complex proteins on microtubule nucleation and catastrophe in fission yeast.","citation":"Mol Biol Cell 2005 Jun;16(6):2719-33","abstract":"Although gamma-tubulin complexes (gamma-TuCs) are known as microtubule (MT) nucleators, their function in vivo is still poorly defined. Mto1p (also known as mbo1p or mod20p) is a gamma-TuC-associated protein that recruits gamma-TuCs specifically to cytoplasmic MT organizing centers (MTOCs) and interphase MTs. Here, we investigated gamma-TuC function by analyzing MT behavior in mto1Delta and alp4 (GCP2 homologue) mutants. These cells have free, extra-long interphase MTs that exhibit abnormal behaviors such as cycles of growth and breakage, MT sliding, treadmilling, and hyperstability. The plus ends of interphase and spindle MTs grow continuously, exhibiting catastrophe defects that are dependent on the CLIP170 tip1p. The minus ends of interphase MTs exhibit shrinkage and pauses. As mto1Delta mutants lack cytoplasmic MTOCs, cytoplasmic MTs arise from spindle or other intranuclear MTs that exit the nucleus. Our findings show that mto1p and gamma-TuCs affect multiple properties of MTs including nucleation, nuclear attachment, plus-end catastrophe, and minus-end shrinkage.","authors":"Zimmerman S, Chang F","authors_abbrev":"Zimmerman S et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-03-18","publication_year":"2005","canto_session_key":"8570af08389340e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-09-06 07:34:47","canto_approved_date":"2024-12-29 16:32:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-29 17:24:03","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.13","SPCC417.07c","SPAC3C7.12","SPCC1223.06","SPBC365.15"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2015-09-06"},{"uniquename":"PMID:93469","title":"A novel class of Schizosaccharomyces pombe mutants, phenotypically unable to grow on glycerol, a respiratory substrate, but still able to oxidize glycerol aerobically [proceedings].","citation":"Arch Int Physiol Biochim 1979 Aug;87(3):641-2","abstract":"","authors":"Vassarotti A, Colson AM","authors_abbrev":"Vassarotti A et al.","pubmed_publication_date":"Aug 1979","pubmed_entrez_date":"1979-08-01","publication_year":"1979","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10769212","title":"Molecular mechanism of myosin-II assembly at the division site in Schizosaccharomyces pombe.","citation":"J Cell Sci 2000 May;113 ( Pt 10):1813-25","abstract":"Schizosaccharomyces pombe cells divide by virtue of the F-actin-based contractile ring (F-actin ring). Two myosin-II heavy chains, Myo2 and Myp2/Myo3, have been localized to the F-actin ring. Here, we investigated the mechanism of myosin-II assembly at the division site in S. pombe cells. First, we showed that Cdc4, an EF-hand protein, appears to be a common myosin light chain associated with both Myo2 and Myo3. Loss of function of both Myo2 and Myo3 caused a defect in F-actin assembly at the division site, like the phenotype of cdc4 null cells. It is suggested that Myo2, Myo3 and Cdc4 function in a cooperative manner in the formation of the F-actin ring during mitosis. Next, we investigated the dynamics of myosin-II during mitosis in S. pombe cells. In early mitosis when accumulation of F-actin cables in the medial region was not yet observed, Myo2 was detected primarily as dots widely located in the medial cortex. Myo2 fibers also became visible following the appearance of the dots. The Myo2 dots and fibers then fused with each other to form a medial cortical network. Some Myo2 dots appeared to be localized with F-actin cables which are also accumulated in the medial region. Finally these structures were packed into a thin contractile ring. In mutant cells that cannot form the F-actin ring such as cdc3(ts), cdc8(ts) and cdc12(ts), Myo2 was able to accumulate as dots in the medial cortex, whereas no accumulation of Myo2 dots was detected in cdc4(ts) cells. Moreover, disruption of F-actin in the cell by applying latrunculin-A did not affect the accumulation of Myo2 dots, suggesting that F-actin is not required for their accumulation. A truncated Myo2 which lacks putative Cdc4-binding sites (Myo2dIQs) was able to rescue myo2 null cells, myo3 null cells, cdc4(ts) mutant cells and cdc4 null cells. The Myo2dIQs could assemble into a normal-shaped ring in these cells. Therefore, its assembly at the division site does not require the function of either Cdc4 or Myo3.","authors":"Motegi F, Nakano K, Mabuchi I","authors_abbrev":"Motegi F et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-04-19","publication_year":"2000","canto_session_key":"b34dc47eaa1f4290","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-11 13:41:08","canto_approved_date":"2025-09-03 10:10:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-11 13:41:01","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.15c","SPBC26H8.07c","SPAC4A8.05c","SPCC645.05c","SPAC1F5.04c","SPAP8A3.08","SPAC27F1.02c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-08-11"},{"uniquename":"PMID:37635373","title":"The longevity and reversibility of quiescence in  Schizosaccharomyces pombe  are dependent upon the HIRA histone chaperone.","citation":"Cell Cycle 2023 Sep;22(17):1921-1936","abstract":"Quiescence (G0) is a reversible non-dividing state that facilitates cellular survival in adverse conditions. Here, we demonstrate that the HIRA histone chaperone complex is required for the reversibility and longevity of nitrogen starvation-induced quiescence in  Schizosaccharomyces pombe . The HIRA protein, Hip1 is not required for entry into G0 or the induction of autophagy. Although  hip1 Δ cells retain metabolic activity in G0, they rapidly lose the ability to resume proliferation. After a short period in G0 (1 day),  hip1 Δ mutants can resume cell growth in response to the restoration of a nitrogen source but do not efficiently reenter the vegetative cell cycle. This correlates with a failure to induce the expression of MBF transcription factor-dependent genes that are critical for S phase. In addition,  hip1 Δ G0 cells rapidly progress to a senescent state in which they can no longer re-initiate growth following nitrogen source restoration. Analysis of a conditional  hip1  allele is consistent with these findings and indicates that HIRA is required for efficient exit from quiescence and prevents an irreversible cell cycle arrest.","doi":"10.1080/15384101.2023.2249705","authors":"Gal C, Cochrane GA, Morgan BA, Rallis C, Bähler J, Whitehall SK","authors_abbrev":"Gal C et al.","pubmed_publication_date":"Sep 2023","pubmed_entrez_date":"2023-08-28","publication_year":"2023","canto_session_key":"543fb168b05450de","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-08-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011798","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28765296","title":"Ethyl Methanesulfonate Mutagenesis in  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Aug 01;2017(8):pdb.prot091736","abstract":"Here we provide an ethyl methanesulfonate (EMS) mutagenesis protocol for  Schizosaccharomyces pombe  cells.","doi":"10.1101/pdb.prot091736","authors":"Ekwall K, Thon G","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"01 Aug 2017","pubmed_entrez_date":"2017-08-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-08-04 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10327407","title":"Preparation of the fission yeast Schizosaccharomyces pombe for ultrastructural and immunocytochemical study.","citation":"Methods Mol Biol 1999;117:183-207","abstract":"","authors":"Hajibagheri MA, Sawin K, Gschmeissner S, Blight K, Upton C","authors_abbrev":"Hajibagheri MA et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-05-18","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21956911","title":"Polyadenylation and beyond: emerging roles for noncanonical poly(A) polymerases.","citation":"Wiley Interdiscip Rev RNA 2010;1(1):142-51","abstract":"The addition of nontemplated nucleotides, particularly adenylyl and uridylyl residues, to the 3' ends of RNA substrates has been the focus of much attention in recent years, and these studies have generated some intriguing surprises. In addition to the well-known canonical poly(A) polymerase (PAP) that polyadenylates mRNAs prior to export from the nucleus to the cytoplasm, a separate class of noncanonical poly(A) polymerases has emerged over the past decade. Studies on various organisms have led to the realization that these noncanonical PAPs, which are conserved from yeast to mammals, play crucial and diverse roles in the regulation of gene expression. Here we review the current knowledge of these enzymes, with an emphasis on the human proteins, and highlight recent discoveries that have implications far beyond the understanding of RNA metabolism itself.","doi":"10.1002/wrna.16","authors":"Schmidt MJ, Norbury CJ","authors_abbrev":"Schmidt MJ et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2011-09-30","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:09:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11160827","title":"Role of fission yeast primase catalytic subunit in the replication checkpoint.","citation":"Mol Biol Cell 2001 Jan;12(1):115-28","abstract":"To investigate the cell cycle checkpoint response to aberrant S phase-initiation, we analyzed mutations of the two DNA primase subunit genes of Schizosaccharomyces pombe, spp1(+) and spp2(+) (S. pombe primase 1 and 2). spp1(+) encodes the catalytic subunit that synthesizes the RNA primer, which is then utilized by Polalpha to synthesize the initiation DNA. Here, we reported the isolation of the fission yeast spp1(+) gene and cDNA and the characterization of Spp1 protein and its cellular localization during the cell cycle. Spp1 is essential for cell viability, and thermosensitive mutants of spp1(+) exhibit an allele-specific abnormal mitotic phenotype. Mutations of spp1(+) reduce the steady-state cellular levels of Spp1 protein and compromised the formation of Polalpha-primase complex. The spp1 mutant displaying an aberrant mitotic phenotype also fails to properly activate the Chk1 checkpoint kinase, but not the Cds1 checkpoint kinase. Mutational analysis of Polalpha has previously shown that activation of the replication checkpoint requires the initiation of DNA synthesis by Polalpha. Together, these have led us to propose that suboptimal cellular levels of polalpha-primase complex due to the allele-specific mutations of Spp1 might not allow Polalpha to synthesize initiation DNA efficiently, resulting in failure to activate a checkpoint response. Thus, a functional Spp1 is required for the Chk1-mediated, but not the Cds1-mediated, checkpoint response after an aberrant initiation of DNA synthesis.","authors":"Griffiths DJ, Liu VF, Nurse P, Wang TS","authors_abbrev":"Griffiths DJ et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-02-13","publication_year":"2001","canto_session_key":"d5830d67c82d45cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-06-28 16:28:09","canto_approved_date":"2026-01-29 16:03:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-13 14:26:29","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":78,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c","SPCC18B5.11c","SPCC1259.13","SPBC17D11.06","SPAC6B12.10c"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2018-06-28"},{"uniquename":"PMID:18183307","title":"Importance of a C-terminal conserved region of Chk1 for checkpoint function.","citation":"PLoS One 2008 Jan 09;3(1):e1427","abstract":"The protein kinase Chk1 is an essential component of the DNA damage checkpoint pathway. Chk1 is phosphorylated and activated in the fission yeast Schizosaccharomyces pombe when cells are exposed to agents that damage DNA. Phosphorylation, kinase activation, and nuclear accumulation are events critical to the ability of Chk1 to induce a transient delay in cell cycle progression. The catalytic domain of Chk1 is well-conserved amongst all species, while there are only a few regions of homology within the C-terminus. A potential pseudosubstrate domain exists in the C-terminus of S. pombe Chk1, raising the possibility that the C-terminus acts to inhibit the catalytic domain through interaction of this domain with the substrate binding site.\nTo evaluate this hypothesis, we characterized mutations in the pseudosubstrate region. Mutation of a conserved aspartic acid at position 469 to alanine or glycine compromises Chk1 function when the mutants are integrated as single copies, demonstrating that this domain of Chk1 is critical for function. Our data does not support, however, the hypothesis that the domain acts to inhibit Chk1 function as other mutations in the amino acids predicted to comprise the pseudosubstrate do not result in constitutive activation of the protein. When expressed in multi-copy, Chk1D469A remains non-functional. In contrast, multi-copy Chk1D469G confers cell survival and imposes a checkpoint delay in response to some, though not all forms of DNA damage.\nThus, we conclude that this C-terminal region of Chk1 is important for checkpoint function and predict that a limiting factor capable of associating with Chk1D469G, but not Chk1D469A, interacts with Chk1 to elicit checkpoint activation in response to a subset of DNA lesions.","doi":"10.1371/journal.pone.0001427","authors":"Palermo C, Hope JC, Freyer GA, Rao H, Walworth NC","authors_abbrev":"Palermo C et al.","pubmed_publication_date":"09 Jan 2008","pubmed_entrez_date":"2008-01-10","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC20G8.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:38133430","title":"Genetic suppressor screen identifies Tgp1 (glycerophosphocholine transporter), Kcs1 (IP 6  kinase), and Plc1 (phospholipase C) as determinants of inositol pyrophosphate toxicosis in fission yeast.","citation":"mBio 2023 Dec 22;:e0306223","abstract":"The inositol pyrophosphate metabolite 1,5-IP 8  governs repression of fission yeast phosphate homeostasis genes  pho1 ,  pho84 , and  tgp1  by lncRNA-mediated transcriptional interference. Asp1 pyrophosphatase mutations that increase IP 8  levels elicit precocious lncRNA termination, leading to derepression of the  PHO  genes. Deletions of the Asp1 pyrophosphatase domain result in growth impairment or lethality via IP 8  agonism of transcription termination. It was assumed that IP 8  toxicity ensues from dysregulation of essential genes. In this study, a suppressor screen revealed that IP 8  toxicosis of Asp1 pyrophosphatase mutants is caused by: (i) a >40-fold increase in the expression of the inessential  tgp1  gene encoding a glycerophosphodiester transporter and (ii) the presence of glycerophosphocholine in the growth medium. The suppressor screen yielded missense mutations in two upstream enzymes of inositol polyphosphate metabolism: the phospholipase C enzyme Plc1 that generates IP 3  and the essential Kcs1 kinase that converts IP 6  to 5-IP 7 , the immediate precursor of IP 8 .","doi":"10.1128/mbio.03062-23","authors":"Bednor L, Sanchez AM, Garg A, Shuman S, Schwer B","authors_abbrev":"Bednor L et al.","pubmed_publication_date":"22 Dec 2023","pubmed_entrez_date":"2023-12-22","publication_year":"2023","canto_session_key":"b2f2007279faafbc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2024-01-01 16:42:42","canto_approved_date":"2024-02-21 18:26:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-26 22:27:53","canto_added_date":"2023-12-23 00:25:05","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":210,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.07c","SPCC70.08c","SPAC1039.02","SPBP4G3.02","SPCC965.07c","SPBC16E9.16c","SPAC22F8.11","SPAC343.12","SPBC1861.01c","SPAC13G7.02c","SPAC750.01","SPAC11D3.05","SPCC1672.06c","SPBC3H7.05c","SPBC25B2.08","SPBPB21E7.04c","SPAC15E1.02c","SPBC26H8.11c","SPAP8A3.04c","SPBPB7E8.01","SPBC29B5.02c","SPBPB2B2.12c","SPCC1183.04c","SPBC354.12","SPBC16D10.06","SPAC21E11.04","SPAPB24D3.08c","SPBC4F6.09","SPCC338.12","SPAC750.05c","SPAC637.03","SPAC11D3.01c","SPAC1002.19","SPBC1271.09","SPBPB2B2.01","SPAC23D3.14c","SPAC17C9.16c","SPBPB10D8.02c","SPCC794.03","SPBC1683.09c","SPAC23D3.12","SPAC13G7.13c","SPCC1020.09","SPBC1271.07c","SPCC548.07c","SPAC1039.09","SPBC725.10","SPAC3G9.04","SPAC22F3.02","SPBC21C3.19","SPAC27D7.03c","SPAC186.05c","SPAC2H10.01","SPBC947.04","SPCC364.06","SPBC1683.01","SPCC970.08","SPBC1861.02","SPAC11D3.19","SPBPB2B2.06c","SPAC1F7.08","SPCC663.08c","SPBC8E4.01c","SPBC106.02c","SPAC1002.17c","SPAC186.01","SPCC1235.14","SPBC36.03c","SPBC8E4.12c"],"gene_count":69,"ltp_gene_count":6,"approved_date":"2024-01-01"},{"uniquename":"PMID:9392077","title":"Measurement of nuclear DNA content in fission yeast by flow cytometry.","citation":"Yeast 1997 Nov;13(14):1329-35","abstract":"Cell division cycle (cdc) mutants of Schizosaccharomyces pombe are arrested at specific points in the cell cycle when grown at restrictive temperature. Flow cytometry of such cells reveals an anomalous increase in the DNA fluorescence signal, which represents a problem in experiments designed to determine the cell cycle arrest point. The increased fluorescence signal is due to cytoplasmic constituents and has been attributed to mitochondrial DNA synthesis (S. Sazer and S. W. Sherwood, J. Cell Sci. 97: 509-516, 1990). Here we have studied the cdc10 mutant by flow cytometry using different DNA-binding fluorochromes and found no evidence that the increased fluorescence signal was caused by mitochondrial DNA synthesis. To determine more accurately the nuclear DNA content we have developed a novel method to remove most of the cytoplasmic material by exposing the cells to Triton X-100 and hypotonic conditions after cell wall digestion. The DNA fluorescence from cells treated in this way was more constant with time of incubation at restrictive temperature in spite of a considerable increase in cell size. With this method we could determine that the recently isolated temperature sensitive orp1 mutant is arrested with a 1C DNA content. Premature and abnormal mitosis ('cut') could be observed for the orp1 mutant after only 4 h at restrictive temperature.","authors":"Carlson CR, Grallert B, Bernander R, Stokke T, Boye E","authors_abbrev":"Carlson CR et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1997-12-10","publication_year":"1997","canto_session_key":"a40f988b2dac73eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-31 16:41:21","canto_approved_date":"2020-06-26 13:35:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-26 16:53:46","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.15","SPBC336.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-01-31"},{"uniquename":"PMID:10653691","title":"Functional conservation of RNA polymerase II in fission and budding yeasts.","citation":"J Mol Biol 2000 Feb 04;295(5):1119-27","abstract":"The complementary DNAs of the 12 subunits of fission yeast (Schizosaccharomyces pombe) RNA polymerase II were expressed from strong promoters in Saccharomyces cerevisiae and tested for heterospecific complementation by monitoring their ability to replace in vivo the null mutants of the corresponding host genes. Rpb1 and Rpb2, the two largest subunits and Rpb8, a small subunit shared by all three polymerases, failed to support growth in S. cerevisiae. The remaining nine subunits were all proficient for heterospecific complementation and led in most cases to a wild-type level of growth. The two alpha-like subunits (Rpb3 and Rpb11), however, did not support growth at high (37 degrees C) or low (25 degrees C) temperatures. In the case of Rpb3, growth was restored by increasing the gene dosage of the host Rpb11 or Rpb10 subunits, confirming previous evidence of a close genetic interaction between these three subunits.","authors":"Shpakovski GV, Gadal O, Labarre-Mariotte S, Lebedenko EN, Miklos I, Sakurai H, Proshkin SA, Van Mullem V, Ishihama A, Thuriaux P","authors_abbrev":"Shpakovski GV et al.","pubmed_publication_date":"04 Feb 2000","pubmed_entrez_date":"2000-02-02","publication_year":"2000","canto_session_key":"40605765a2590bb3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-01-21 09:14:49","canto_approved_date":"2021-01-21 09:14:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-21 09:14:40","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-01-21"},{"uniquename":"PMID:23496905","title":"Nedd8 processing enzymes in Schizosaccharomyces pombe.","citation":"BMC Biochem 2013 Mar 15;14:8","abstract":"Conjugation of the ubiquitin-like modifier Nedd8 to cullins is critical for the function of SCF-type ubiquitin ligases and thus facilitates ubiquitin conjugation and ultimately degradation of SCF substrates, including several cell cycle regulators. Like ubiquitin, Nedd8 is produced as a precursor that must first be processed before it becomes active. In Saccharomyces cerevisiae this is carried out exclusively by the enzyme Yuh1.\nHere we show that in the fission yeast, Schizosaccharomyces pombe, the Yuh1 orthologue, Uch1, is not the sole Nedd8 processing enzyme. Instead it appears that deubiquitylating enzymes can efficiently process the Nedd8 precursor in vivo.\nSeveral enzymes contribute to Nedd8 precursor processing including a number of deubiquitylating enzymes.","doi":"10.1186/1471-2091-14-8","authors":"O'Donoghue JE, Bech-Otschir D, Larsen IB, Wallace M, Hartmann-Petersen R, Gordon C","authors_abbrev":"O'Donoghue JE et al.","pubmed_publication_date":"15 Mar 2013","pubmed_entrez_date":"2013-03-19","publication_year":"2013","canto_session_key":"fb4ffc5eba4ac1e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_approved_date":"2016-12-01 13:10:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-28 08:53:04","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.08c","SPBC17D11.01","SPAC1687.13c","SPBC409.06","SPBC32H8.02c","SPAC17G6.12","SPAC27F1.03c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-11-28"},{"uniquename":"PMID:9258332","title":"Identification and expression of uvi31+, a UV-inducible gene from Schizosaccharomyces pombe.","citation":"Environ Mol Mutagen 1997;30(1):72-81","abstract":"The Schizosaccharomyces pombe uvi31+ gene has been previously isolated as a UV-inducible gene [Lee JK et al. (1994) Biochem Biophys Res Commun 202:1113-1119]. This gene encodes a protein of about 12 kDa with 57% amino acid sequence similarity to Escherichia coli BolA protein which is known to be involved in switching between the cell elongation and septation systems during the cell division cycle. The putative Mlul cell cycle box (MCB), SWI4/6-dependent cell cycle box (SCB), and gear-box elements are found in the upstream region of uvi31+ gene, suggesting that this gene shows the cell cycle-regulated and growth phase-dependent expression. Interestingly, the level of uvi31+ transcript varies throughout the cell cycle, peaking in G1 phase before septation, and also shows the growth phase-dependent pattern during cellular growth, increasing maximally at the diauxic shift phase just before stationary phase. Furthermore, the transcript level of this gene is raised after S phase arrest, and is also increased maximally at 4 hr after UV irradiation of 240 J/m2. These results suggest that the delayed induction of uvi31+ gene after UV irradiation may be caused by cell cycle control of this gene after DNA replication checkpoint arrest. Thus, the uvi31+ gene may play a role in controlling the progress of the cell cycle after DNA damage (UV irradiation).","authors":"Kim SH, Kim M, Lee JK, Kim MJ, Jin YH, Seong RH, Hong SH, Joe CO, Park SD","authors_abbrev":"Kim SH et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_session_key":"a8f6851e40b791f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-11 15:35:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-11 15:35:41","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16E9.06c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-03-11"},{"uniquename":"PMID:39652606","title":"Cbf11 and Mga2 function together to activate transcription of lipid metabolism genes and promote mitotic fidelity in fission yeast.","citation":"PLoS Genet 2024 Dec 09;20(12):e1011509","abstract":"Within a eukaryotic cell, both lipid homeostasis and faithful cell cycle progression are meticulously orchestrated. The fission yeast Schizosaccharomyces pombe provides a powerful platform to study the intricate regulatory mechanisms governing these fundamental processes. In S. pombe, the Cbf11 and Mga2 proteins are transcriptional activators of non-sterol lipid metabolism genes, with Cbf11 also known as a cell cycle regulator. Despite sharing a common set of target genes, little was known about their functional relationship. This study reveals that Cbf11 and Mga2 function together in the same regulatory pathway, critical for both lipid metabolism and mitotic fidelity. Deletion of either gene results in a similar array of defects, including slow growth, dysregulated lipid homeostasis, impaired cell cycle progression (cut phenotype), abnormal cell morphology, perturbed transcriptomic and proteomic profiles, and compromised response to the stressors camptothecin and thiabendazole. Remarkably, the double deletion mutant does not exhibit a more severe phenotype compared to the single mutants. In addition, ChIP-nexus analysis reveals that both Cbf11 and Mga2 bind to nearly identical positions within the promoter regions of target genes. Interestingly, Mga2 binding appears to be dependent on the presence of Cbf11 and Cbf11 likely acts as a tether to DNA, while Mga2 is needed to activate the target genes. In addition, the study explores the distribution of Cbf11 and Mga2 homologs across fungi. The presence of both Cbf11 and Mga2 homologs in Basidiomycota contrasts with Ascomycota, which mostly lack Cbf11 but retain Mga2. This suggests an evolutionary rewiring of the regulatory circuitry governing lipid metabolism and mitotic fidelity. In conclusion, this study offers compelling support for Cbf11 and Mga2 functioning jointly to regulate lipid metabolism and mitotic fidelity in fission yeast.","doi":"10.1371/journal.pgen.1011509","authors":"Marešová A, Grulyová M, Hradilová M, Zemlianski V, Princová J, Převorovský M","authors_abbrev":"Marešová A et al.","pubmed_publication_date":"09 Dec 2024","pubmed_entrez_date":"2024-12-09","publication_year":"2024","canto_session_key":"ebd6c4def00a2f50","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Anna Marešová","canto_first_approved_date":"2025-01-17 10:06:51","canto_approved_date":"2025-01-17 10:06:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-01-07 12:36:22","canto_added_date":"2024-12-10 00:25:06","annotation_curators":[{"name":"Anna Marešová","community_curator":true,"annotation_count":47,"orcid":"0000-0003-0864-7231","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":30,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.11c","SPAC56E4.04c","SPAC22A12.06c","SPCC1450.16c","SPCC1235.02","SPCC736.08","SPBC18H10.02","SPBP4H10.11c","SPAC1B3.16c","SPAC26H5.05","SPAC1786.01c","SPAC926.09c","SPCC1281.06c"],"gene_count":13,"ltp_gene_count":3,"approved_date":"2025-01-17"},{"uniquename":"PMID:29474927","title":"Post-meiotic DNA double-strand breaks are conserved in fission yeast.","citation":"Int J Biochem Cell Biol 2018 May;98:24-28","abstract":"In mammals, spermiogenesis is characterized by transient formation of DNA double-strand breaks (DSBs) in the whole population of haploid spermatids. DSB repair in such haploid context may represent a mutational transition. Using a combination of pulsed-field gel electrophoresis and specific labelling of DSBs at 3'OH DNA ends, we showed that post-meiotic, enzyme-induced DSBs are also observed in the synchronizable pat1-114 mutant of Shizosaccharomyces pombe as well as in a wild-type strain, while DNA repair is observed at later stages. This transient DNA fragmentation arises in the whole cell population and is seemingly independent of the caspase apoptotic pathway. Because histones are still present in spores, the transient DSBs do not require a major change in chromatin structure. These observations confirm the highly-conserved nature of the process in eukaryotes and provide a powerful model to study the underlying mechanism and its impact on the genetic landscape and adaptation.","doi":"10.1016/j.biocel.2018.02.012","authors":"Cavé T, Grégoire MC, Brazeau MA, Boissonneault G","authors_abbrev":"Cavé T et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-02-24","publication_year":"2018","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2018-02-28 22:13:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15329725","title":"Separase-mediated cleavage of cohesin at interphase is required for DNA repair.","citation":"Nature 2004 Aug 26;430(7003):1044-8","abstract":"Sister chromatids are held together by cohesins. At anaphase, separase is activated by degradation of its inhibitory partner, securin. Separase then cleaves cohesins, thus allowing sister chromatid separation. Fission yeast securin (Cut2) has destruction boxes and a separase (Cut1) interaction site in the amino and carboxyl terminus, respectively. Here we show that securin is essential for separase stability and also for proper repair of DNA damaged by ultraviolet, X-ray and gamma-ray irradiation. The cut2(EA2) mutant is defective in the repair of ultraviolet damage lesions, although the DNA damage checkpoint is activated normally. In double mutant analysis of ultraviolet sensitivity, checkpoint kinase chk1 (ref. 9) and excision repair rad13 (ref. 10) mutants were additive with cut2(EA2), whereas recombination repair rhp51 (ref. 11) and cohesin subunit rad21 (ref. 12) mutants were not. Cohesin was hyper-modified on ultraviolet irradiation in a Rad3 kinase-dependent way. Experiments using either mutant cohesin that cannot be cleaved by separase or a protease-dead separase provide evidence that this DNA repair function of securin-separase acts through the cleavage of cohesin. We propose that the securin-separase complex might aid DNA repair by removing local cohesin in interphase cells.","authors":"Nagao K, Adachi Y, Yanagida M","authors_abbrev":"Nagao K et al.","pubmed_publication_date":"26 Aug 2004","pubmed_entrez_date":"2004-08-27","publication_year":"2004","canto_session_key":"310b16bb1a103044","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-03-20 14:35:44","canto_approved_date":"2026-01-31 15:04:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-03 07:48:53","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC644.14c","SPCC338.17c","SPCC5E4.04","SPBC19C7.09c","SPBC3E7.08c","SPAC2G11.12","SPCC18B5.11c","SPBC342.05","SPBC14C8.01c"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2017-03-20"},{"uniquename":"PMID:21187911","title":"Mathematical model of a cell size checkpoint.","citation":"PLoS Comput Biol 2010 Dec 16;6(12):e1001036","abstract":"How cells regulate their size from one generation to the next has remained an enigma for decades. Recently, a molecular mechanism that links cell size and cell cycle was proposed in fission yeast. This mechanism involves changes in the spatial cellular distribution of two proteins, Pom1 and Cdr2, as the cell grows. Pom1 inhibits Cdr2 while Cdr2 promotes the G2 → M transition. Cdr2 is localized in the middle cell region (midcell) whereas the concentration of Pom1 is highest at the cell tips and declines towards the midcell. In short cells, Pom1 efficiently inhibits Cdr2. However, as cells grow, the Pom1 concentration at midcell decreases such that Cdr2 becomes activated at some critical size. In this study, the chemistry of Pom1 and Cdr2 was modeled using a deterministic reaction-diffusion-convection system interacting with a deterministic model describing microtubule dynamics. Simulations mimicked experimental data from wild-type (WT) fission yeast growing at normal and reduced rates; they also mimicked the behavior of a Pom1 overexpression mutant and WT yeast exposed to a microtubule depolymerizing drug. A mechanism linking cell size and cell cycle, involving the downstream action of Cdr2 on Wee1 phosphorylation, is proposed.","doi":"10.1371/journal.pcbi.1001036","authors":"Vilela M, Morgan JJ, Lindahl PA","authors_abbrev":"Vilela M et al.","pubmed_publication_date":"16 Dec 2010","pubmed_entrez_date":"2010-12-29","publication_year":"2010","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26960127","title":"Data collection with a tailored X-ray beam size at 2.69 Å wavelength (4.6 keV): sulfur SAD phasing of Cdc23(Nterm).","citation":"Acta Crystallogr D Struct Biol 2016 Mar;72(Pt 3):403-12","abstract":"The capability to reach wavelengths of up to 3.1 Å at the newly established EMBL P13 beamline at PETRA III, the new third-generation synchrotron at DESY in Hamburg, provides the opportunity to explore very long wavelengths to harness the sulfur anomalous signal for phase determination. Data collection at λ = 2.69 Å (4.6 keV) allowed the crystal structure determination by sulfur SAD phasing of Cdc23(Nterm), a subunit of the multimeric anaphase-promoting complex (APC/C). At this energy, Cdc23(Nterm) has an expected Bijvoet ratio〈|Fanom|〉/〈F〉of 2.2%, with 282 residues, including six cysteines and five methionine residues, and two molecules in the asymmetric unit (65.4 kDa; 12 Cys and ten Met residues). Selectively illuminating two separate portions of the same crystal with an X-ray beam of 50 µm in diameter allowed crystal twinning to be overcome. The crystals diffracted to 3.1 Å resolution, with unit-cell parameters a = b = 61.2, c = 151.5 Å, and belonged to space group P43. The refined structure to 3.1 Å resolution has an R factor of 18.7% and an Rfree of 25.9%. This paper reports the structure solution, related methods and a discussion of the instrumentation.","doi":"10.1107/S2059798315010268","authors":"Cianci M, Groves MR, Barford D, Schneider TR","authors_abbrev":"Cianci M et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2016-03-10","publication_year":"2016","canto_session_key":"a3a23513c2482337","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-02-19 19:04:10","canto_approved_date":"2023-02-19 19:04:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-19 19:03:56","canto_added_date":"2016-12-16 01:19:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F12.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-19","pdb_entries":[{"pdb_id":"5ftp","gene_chains":[{"gene_uniquename":"SPAC6F12.14","chain":"A/B","position":"19-301"}],"title":"sulfur SAD phasing of Cdc23Nterm: data collection with a tailored X- ray beam size at 2.69 A wavelength (4.6 keV)","entry_authors":"Cianci M,Groves MR,Barford D,Schneider TR","entry_authors_abbrev":"Cianci M et al.","reference_uniquename":"PMID:26960127","experimental_method":"X-ray","resolution":"3.1"}]},{"uniquename":"PMID:25176634","title":"Rewiring Mid1p-independent medial division in fission yeast.","citation":"Curr Biol 2014 Sep 22;24(18):2181-2188","abstract":"Correct positioning of the cell division machinery is key to genome stability. Schizosaccharomyces pombe is an attractive organism to study cytokinesis as it, like higher eukaryotes, divides using a contractile actomyosin ring. In S. pombe, many actomyosin ring components assemble at the medial cortex into node-like structures before coalescing into a ring [1, 2]. Assembly of cytokinetic nodes requires Mid1p, which recruits IQGAP-related Rng2p to the division site, after which other node components accumulate at the division site in a characteristic sequence [3-6]. How cytokinetic nodes assemble, whether the order of assembly of ring components is important, and whether Mid1p solely participates in ring positioning are poorly understood. Here, we show that synthetic targeting of IQGAP-related Rng2p, formin-Cdc12p, and myosin II (Myo2p) restores medial division in mid1 mutants, suggesting that ring proteins need not assemble at the division site in an invariant order. Unlike in wild-type cells, actomyosin rings in cells rewired to divide medially in the absence of Mid1p assemble late in anaphase. Furthermore, the rewiring process affects the ability of the actomyosin ring to track the nucleus upon perturbation of nuclear position. Our work reveals the power of synthetic rewiring studies in deciphering roles performed by multifunctional proteins.","doi":"10.1016/j.cub.2014.07.074","authors":"Tao EY, Calvert M, Balasubramanian MK","authors_abbrev":"Tao EY et al.","pubmed_publication_date":"22 Sep 2014","pubmed_entrez_date":"2014-09-02","publication_year":"2014","canto_session_key":"7a8f24914005d660","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-09-03 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1767586","title":"The ade6 gene of the fission yeast Schizosaccharomyces pombe has the same chromatin structure in the chromosome and in plasmids.","citation":"Yeast 1991;7(6):547-58","abstract":"We have analysed the chromatin structure of the ade6 gene of Schizosaccharomyces pombe and its flanking regions both in the chromosome and in plasmids. The chromatin structure is independent of the chromosomal or extrachromosomal location. The ade6 gene contains eight precisely positioned nucleosomes on the 5' half, 'not positioned' nucleosomes around the 3' end and a nuclease-sensitive promoter region. Precisely positioned nucleosomes, but no nuclease-sensitive region were also detected on the ura4 gene in the chromosome and on a plasmid. The results show that S. pombe chromosomal and extrachromosomal genes have chromatin structures similar to those of S. cerevisiae and higher eukaryotes.","authors":"Bernardi F, Koller T, Thoma F","authors_abbrev":"Bernardi F et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-08-01","publication_year":"1991","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15004523","title":"S phase assembly of centromeric heterochromatin and cohesion.","citation":"Cell Cycle 2004 Apr;3(4):416-8","abstract":"Accurate chromosome segregation in mitosis requires cohesion between sister centromeres mediated by heterochromatin. Although establishment of both silent heterochromatin and cohesion require passage through S phase, the mechanism was previously unknown. In our recent paper, we demonstrate that heterochromatin silencing and cohesion at the centromere rely on temporal activation of the conserved S phase protein kinase Hsk1-Dfp1. Hsk1-Dfp1 is needed for heterochromatin assembly downstream of Swi6 binding to chromatin; importantly, this activity is independent of the replication function of Hsk1-Dfp1. This defines a temporal connection between S phase, heterochromatin and cohesion that is independent of replication fork passage.","authors":"Bailis JM, Forsburg SL","authors_abbrev":"Bailis JM et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-03-09","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29903723","title":"Long-read sequencing of nascent RNA reveals coupling among RNA processing events.","citation":"Genome Res 2018 Jul;28(7):1008-1019","abstract":"Pre-mRNA splicing is accomplished by the spliceosome, a megadalton complex that assembles de novo on each intron. Because spliceosome assembly and catalysis occur cotranscriptionally, we hypothesized that introns are removed in the order of their transcription in genomes dominated by constitutive splicing. Remarkably little is known about splicing order and the regulatory potential of nascent transcript remodeling by splicing, due to the limitations of existing methods that focus on analysis of mature splicing products (mRNAs) rather than substrates and intermediates. Here, we overcome this obstacle through long-read RNA sequencing of nascent, multi-intron transcripts in the fission yeast  Schizosaccharomyces pombe  Most multi-intron transcripts were fully spliced, consistent with rapid cotranscriptional splicing. However, an unexpectedly high proportion of transcripts were either fully spliced or fully unspliced, suggesting that splicing of any given intron is dependent on the splicing status of other introns in the transcript. Supporting this, mild inhibition of splicing by a temperature-sensitive mutation in  prp2 , the homolog of vertebrate U2AF65, increased the frequency of fully unspliced transcripts. Importantly, fully unspliced transcripts displayed transcriptional read-through at the polyA site and were degraded cotranscriptionally by the nuclear exosome. Finally, we show that cellular mRNA levels were reduced in genes with a high number of unspliced nascent transcripts during caffeine treatment, showing regulatory significance of cotranscriptional splicing. Therefore, overall splicing of individual nascent transcripts, 3' end formation, and mRNA half-life depend on the splicing status of neighboring introns, suggesting crosstalk among spliceosomes and the polyA cleavage machinery during transcription elongation.","doi":"10.1101/gr.232025.117","authors":"Herzel L, Straube K, Neugebauer KM","authors_abbrev":"Herzel L et al.","pubmed_publication_date":"Jul 2018","pubmed_entrez_date":"2018-06-16","publication_year":"2018","canto_session_key":"83904e22763366c9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-06-17 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23609041","title":"Development of episomal vectors carrying a nourseothricin-resistance marker for use in minimal media for Schizosaccharomyces pombe.","citation":"Yeast 2013 Jun;30(6):219-27","abstract":"In the post-genomic era, an immediate challenge is to assign biological functions to novel proteins encoded by the genome. This challenge requires the use of a simple organism as a genetic tool and a range of new high-throughput techniques. Schizosacchromyces pombe is a powerful model organism used to investigate disease-related genes and provides useful tools for the functional analysis of heterologous genes. To expand the current array of experimental tools, we constructed two series of Sz. pombe expression vectors, i.e. general and Gateway vectors, containing nourseothricin-resistance markers. Vectors carrying nourseothricin-resistance markers possess advantages in that they do not limit the parental strains with auxotrophic mutations with respect to availability for use in clone selection and can be used together with vectors carrying nutrient markers in minimal media. We modified the pSLF173, pSLF273 and pSLF373 vectors carrying a triple haemagglutinin epitope (3×HA) and an Ura4 marker. The vectors described here contain the nmt1 promoter with three different episomal expression strengths for proteins fused with 3×HA, EGFP or DsRed at the N-terminus. These vectors represent an important contribution to the genome-wide investigation of multiple heterologous genes and for functional and genetic analysis of novel human genes.","doi":"10.1002/yea.2955","authors":"Ahn J, Won M, Kyun ML, Kim YS, Jung CR, Im DS, Song KB, Chung KS","authors_abbrev":"Ahn J et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-04-24","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16720577","title":"Fission yeast Mcm10p contains primase activity.","citation":"J Biol Chem 2006 Aug 04;281(31):22248-22260","abstract":"Although Mcm10p is a conserved essential component in eukaryotes required for both the initiation and elongation of DNA chains, its biochemical properties are unknown. Here, we report that the Schizosaccharomyces pombe fission yeast Mcm10 protein contains primase activity. Primases are enzymes that synthesize RNA primers on single-stranded DNA templates that are extended by DNA polymerases. In keeping with this property, Mcm10p supported oligoribonucleotide synthesis of short RNA primers (preferentially initiating synthesis on a dT template) that were extended with dATP by Escherichia coli DNA polymerase I. The C terminus of Mcm10p synthesized RNA, but less efficiently than the full-length protein at low rNTP levels. Mcm10p homologs contain a C-terminal motif found in proteins that polymerize nucleotides. A point mutant within this motif of S. pombe Mcm10p was defective in primer synthesis in vitro, and this mutant failed to support growth in vivo, suggesting that the primase activity of Mcm10p may be essential for cell viability.","doi":"10.1074/jbc.M512997200","authors":"Fien K, Hurwitz J","authors_abbrev":"Fien K et al.","pubmed_publication_date":"04 Aug 2006","pubmed_entrez_date":"2006-05-25","publication_year":"2006","canto_session_key":"569690b2bd88fbb0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-11-13 17:51:30","canto_approved_date":"2021-11-05 15:14:36","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-13 17:51:23","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-13"},{"uniquename":"PMID:19412159","title":"Chaperone-mediated pathway of proteasome regulatory particle assembly.","citation":"Nature 2009 Jun 11;459(7248):861-5","abstract":"The proteasome is a protease that controls diverse processes in eukaryotic cells. Its regulatory particle (RP) initiates the degradation of ubiquitin-protein conjugates by unfolding the substrate and translocating it into the proteasome core particle (CP) to be degraded. The RP has 19 subunits, and their pathway of assembly is not understood. Here we show that in the yeast Saccharomyces cerevisiae three proteins are found associated with RP but not with the RP-CP holoenzyme: Nas6, Rpn14 and Hsm3. Mutations in the corresponding genes confer proteasome loss-of-function phenotypes, despite their virtual absence from the holoenzyme. These effects result from deficient RP assembly. Thus, Nas6, Rpn14 and Hsm3 are RP chaperones. The RP contains six ATPases-the Rpt proteins-and each RP chaperone binds to the carboxy-terminal domain of a specific Rpt. We show in an accompanying study that RP assembly is templated through the Rpt C termini, apparently by their insertion into binding pockets in the CP. Thus, RP chaperones may regulate proteasome assembly by directly restricting the accessibility of Rpt C termini to the CP. In addition, competition between the RP chaperones and the CP for Rpt engagement may explain the release of RP chaperones as proteasomes mature.","doi":"10.1038/nature08063","authors":"Roelofs J, Park S, Haas W, Tian G, McAllister FE, Huo Y, Lee BH, Zhang F, Shi Y, Gygi SP, Finley D","authors_abbrev":"Roelofs J et al.","pubmed_publication_date":"11 Jun 2009","pubmed_entrez_date":"2009-05-05","publication_year":"2009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18.17c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:31149897","title":"The PCNA unloader Elg1 promotes recombination at collapsed replication forks in fission yeast.","citation":"Elife 2019 May 31;8","abstract":"Protein-DNA complexes can impede DNA replication and cause replication fork collapse. Whilst it is known that homologous recombination is deployed in such instances to restart replication, it is unclear how a stalled fork transitions into a collapsed fork at which recombination proteins can load. Previously we established assays in  Schizosaccharomyces pombe  for studying recombination induced by replication fork collapse at the site-specific protein-DNA barrier  RTS1  (Nguyen et al., 2015). Here, we provide evidence that efficient recruitment/retention of two key recombination proteins (Rad51 and Rad52) to  RTS1  depends on unloading of the polymerase sliding clamp PCNA from DNA by Elg1. We also show that, in the absence of Elg1, reduced recombination is partially suppressed by deleting  fbh1  or, to a lesser extent,  srs2 , which encode known anti-recombinogenic DNA helicases. These findings suggest that PCNA unloading by Elg1 is necessary to limit Fbh1 and Srs2 activity, and thereby enable recombination to proceed.","doi":"10.7554/eLife.47277","authors":"Tamang S, Kishkevich A, Morrow CA, Osman F, Jalan M, Whitby MC","authors_abbrev":"Tamang S et al.","pubmed_publication_date":"31 May 2019","pubmed_entrez_date":"2019-06-01","publication_year":"2019","canto_session_key":"68fc7415171678cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Matthew Whitby","canto_first_approved_date":"2019-06-13 13:56:59","canto_approved_date":"2022-04-11 19:37:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-04 08:19:27","canto_added_date":"2019-06-04 00:15:04","annotation_curators":[{"name":"Matthew Whitby","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.01","SPBC16D10.09","SPAC4H3.05","SPAC644.14c","SPBC947.11c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-06-13"},{"uniquename":"PMID:26776521","title":"The Tubulation Activity of a Fission Yeast F-BAR Protein Is Dispensable for Its Function in Cytokinesis.","citation":"Cell Rep 2016 Jan 26;14(3):534-546","abstract":"F-BAR proteins link cellular membranes to the actin cytoskeleton in many biological processes. Here we investigated the function of the Schizosaccharomyces pombe Imp2 F-BAR domain in cytokinesis and find that it is critical for Imp2's role in contractile ring constriction and disassembly. To understand mechanistically how the F-BAR domain functions, we determined its structure, elucidated how it interacts with membranes, and identified an interaction between dimers that allows helical oligomerization and membrane tubulation. Using mutations that block either membrane binding or tubulation, we find that membrane binding is required for Imp2's cytokinetic function but that oligomerization and tubulation, activities often deemed central to F-BAR protein function, are dispensable. Accordingly, F-BARs that do not have the capacity to tubulate membranes functionally substitute for the Imp2 F-BAR, establishing that its major role is as a cell-cycle-regulated bridge between the membrane and Imp2 protein partners, rather than as a driver of membrane curvature.","doi":"10.1016/j.celrep.2015.12.062","authors":"McDonald NA, Takizawa Y, Feoktistova A, Xu P, Ohi MD, Vander Kooi CW, Gould KL","authors_abbrev":"McDonald NA et al.","pubmed_publication_date":"26 Jan 2016","pubmed_entrez_date":"2016-01-19","publication_year":"2016","canto_session_key":"87a94fe39055813d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2016-03-04 10:29:52","canto_approved_date":"2026-01-29 17:33:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-29 21:08:47","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kathy Gould","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.06c","SPAC3G9.05","SPBC11C11.02","SPAC20G8.05c","SPBC83.18c"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2016-03-04","pdb_entries":[{"pdb_id":"5c1f","gene_chains":[{"gene_uniquename":"SPBC11C11.02","chain":"A/B","position":"15-320"}],"title":"Structure of the Imp2 F-BAR domain","entry_authors":"Vander Kooi CW","entry_authors_abbrev":"Vander Kooi CW","reference_uniquename":"PMID:26776521","experimental_method":"X-ray","resolution":"2.3551"}]},{"uniquename":"PMID:32421151","title":"Fission yeast Pak1 phosphorylates anillin-like Mid1 for spatial control of cytokinesis.","citation":"J Cell Biol 2020 Aug 03;219(8)","abstract":"Protein kinases direct polarized growth by regulating the cytoskeleton in time and space and could play similar roles in cell division. We found that the Cdc42-activated polarity kinase Pak1 colocalizes with the assembling contractile actomyosin ring (CAR) and remains at the division site during septation. Mutations in pak1 led to defects in CAR assembly and genetic interactions with cytokinesis mutants. Through a phosphoproteomic screen, we identified novel Pak1 substrates that function in polarized growth and cytokinesis. For cytokinesis, we found that Pak1 regulates the localization of its substrates Mid1 and Cdc15 to the CAR. Mechanistically, Pak1 phosphorylates the Mid1 N-terminus to promote its association with cortical nodes that act as CAR precursors. Defects in Pak1-Mid1 signaling lead to misplaced and defective division planes, but these phenotypes can be rescued by synthetic tethering of Mid1 to cortical nodes. Our work defines a new signaling mechanism driven by a cell polarity kinase that promotes CAR assembly in the correct time and place.","doi":"10.1083/jcb.201908017","authors":"Magliozzi JO, Sears J, Cressey L, Brady M, Opalko HE, Kettenbach AN, Moseley JB","authors_abbrev":"Magliozzi JO et al.","pubmed_publication_date":"03 Aug 2020","pubmed_entrez_date":"2020-05-19","publication_year":"2020","canto_session_key":"0ebee32146cc37c0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-05-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29972885","title":"Dependency relationships within the fission yeast polarity network.","citation":"FEBS Lett 2018 Aug;592(15):2543-2549","abstract":"The ability to regulate polarised cell growth is crucial to maintain the viability of cells. Growth is modulated to facilitate essential cell functions and respond to the external environment. Failure to do so can lead to numerous developmental and disease states, including cancer. We have undertaken a detailed analysis of the regulatory interplay between molecules involved in the regulation and maintenance of polarised cell growth within fission yeast. Internally controlled live cell imaging was used to examine interactions between 10 key polarity proteins. Analysis reveals interplay between the microtubule and actin cytoskeletons, as well as multiple novel dependency pathways and feedback networks between groups of proteins. This study provides important insights into the conserved regulation of polarised cell growth within eukaryotes.","doi":"10.1002/1873-3468.13180","authors":"Johnson M, Mulvihill DP","authors_abbrev":"Johnson M et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-07-05","publication_year":"2018","canto_session_key":"964f548c192976c8","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-07-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF470232","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25612912","title":"A novel X-linked trichothiodystrophy associated with a nonsense mutation in RNF113A.","citation":"J Med Genet 2015 Apr;52(4):269-74","abstract":"Trichothiodystrophy (TTD) is a group of rare autosomal recessive disorders that variably affect a wide range of organs derived from the neuroectoderm. The key diagnostic feature is sparse, brittle, sulfur deficient hair that has a 'tiger-tail' banding pattern under polarising light microscopy.\nWe describe two male cousins affected by TTD associated with microcephaly, profound intellectual disability, sparse brittle hair, aged appearance, short stature, facial dysmorphism, seizures, an immunoglobulin deficiency, multiple endocrine abnormalities, cerebellar hypoplasia and partial absence of the corpus callosum, in the absence of cellular photosensitivity and ichthyosis. Obligate female carriers showed 100% skewed X-chromosome inactivation. Linkage analysis and Sanger sequencing of 737 X-chromosome exons and whole exome sequencing was used to find the responsible gene and mutation.\nLinkage analysis localised the disease allele to a 7.75 Mb interval from Xq23-q25. We identified a nonsense mutation in the highly conserved RNF113A gene (c.901 C>T, p.Q301*). The mutation segregated with the disease in the family and was not observed in over 100,000 control X chromosomes. The mutation markedly reduced RNF113A protein expression in extracts from lymphoblastoid cell lines derived from the affected individuals.\nThe association of RNF113A mutation with non-photosensitive TTD identifies a new locus for these disorders on the X chromosome. The extended phenotype within this family includes panhypopituitarism, cutis marmorata and congenital short oesophagus.","doi":"10.1136/jmedgenet-2014-102418","authors":"Corbett MA, Dudding-Byth T, Crock PA, Botta E, Christie LM, Nardo T, Caligiuri G, Hobson L, Boyle J, Mansour A, Friend KL, Crawford J, Jackson G, Vandeleur L, Hackett A, Tarpey P, Stratton MR, Turner G, Gécz J, Field M","authors_abbrev":"Corbett MA et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-01-24","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC13E7.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:27075176","title":"The F-actin bundler α-actinin Ain1 is tailored for ring assembly and constriction during cytokinesis in fission yeast.","citation":"Mol Biol Cell 2016 Jun 01;27(11):1821-33","abstract":"The actomyosin contractile ring is a network of cross-linked actin filaments that facilitates cytokinesis in dividing cells. Contractile ring formation has been well characterized in Schizosaccharomyces pombe, in which the cross-linking protein α-actinin SpAin1 bundles the actin filament network. However, the specific biochemical properties of SpAin1 and whether they are tailored for cytokinesis are not known. Therefore we purified SpAin1 and quantified its ability to dynamically bind and bundle actin filaments in vitro using a combination of bulk sedimentation assays and direct visualization by two-color total internal reflection fluorescence microscopy. We found that, while SpAin1 bundles actin filaments of mixed polarity like other α-actinins, SpAin1 has lower bundling activity and is more dynamic than human α-actinin HsACTN4. To determine whether dynamic bundling is important for cytokinesis in fission yeast, we created the less dynamic bundling mutant SpAin1(R216E). We found that dynamic bundling is critical for cytokinesis, as cells expressing SpAin1(R216E) display disorganized ring material and delays in both ring formation and constriction. Furthermore, computer simulations of initial actin filament elongation and alignment revealed that an intermediate level of cross-linking best facilitates filament alignment. Together our results demonstrate that dynamic bundling by SpAin1 is important for proper contractile ring formation and constriction.","doi":"10.1091/mbc.E16-01-0010","authors":"Li Y, Christensen JR, Homa KE, Hocky GM, Fok A, Sees JA, Voth GA, Kovar DR","authors_abbrev":"Li Y et al.","pubmed_publication_date":"01 Jun 2016","pubmed_entrez_date":"2016-04-15","publication_year":"2016","canto_session_key":"a4ab4922ffecbd92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jenna Christensen","canto_first_approved_date":"2017-05-19 22:26:04","canto_approved_date":"2023-05-17 15:42:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-02 21:08:00","canto_added_date":"2016-04-17 00:15:19","annotation_curators":[{"name":"Jenna Christensen","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC15A10.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-05-19"},{"uniquename":"PMID:26441355","title":"Actin-Based Transport Adapts Polarity Domain Size to Local Cellular Curvature.","citation":"Curr Biol 2015 Oct 19;25(20):2677-83","abstract":"Intracellular structures and organelles such as the nucleus, the centrosome, or the mitotic spindle typically scale their size to cell size [1]. Similarly, cortical polarity domains built around the active form of conserved Rho-GTPases, such as Cdc42p, exhibit widths that may range over two orders of magnitudes in cells with different sizes and shapes [2-6]. The establishment of such domains typically involves positive feedback loops based on reaction-diffusion and/or actin-mediated vesicle transport [3, 7, 8]. How these elements may adapt polarity domain size to cellular geometry is not known. Here, by tracking the width of successive oscillating Cdc42-GTP domains in fission yeast spores [9], we find that domain width scales with local cell-surface radii of curvature over an 8-fold range, independently of absolute cell volume, surface, or Cdc42-GTP concentration. This local scaling requires formin-nucleated cortical actin cables and the fusion of secretory vesicles transported along these cables with the membrane. These data suggest that reaction-diffusion may set a minimal domain size and that secretory vesicle transport along actin cables may dilute and extend polarity domains to adapt their size to local cell-surface curvature. This work reveals that actin networks may act as micrometric curvature sensors and uncovers a generic morphogenetic principle for how polarity domains define their size according to cell morphologies.","doi":"10.1016/j.cub.2015.08.046","authors":"Bonazzi D, Haupt A, Tanimoto H, Delacour D, Salort D, Minc N","authors_abbrev":"Bonazzi D et al.","pubmed_publication_date":"19 Oct 2015","pubmed_entrez_date":"2015-10-07","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-10-08 00:19:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15466417","title":"Regulation of leucine uptake by tor1+ in Schizosaccharomyces pombe is sensitive to rapamycin.","citation":"Genetics 2005 Feb;169(2):539-50","abstract":"TOR protein kinases are key regulators of cell growth in eukaryotes. TOR is also known as the target protein for the immunosuppressive and potentially anticancer drug rapamycin. The fission yeast Schizosaccharomyces pombe has two TOR homologs. tor1+ is required under starvation and a variety of stresses, while tor2+ is an essential gene. Surprisingly, to date no rapamycin-sensitive TOR-dependent function has been identified in S. pombe. Herein, we show that S. pombe auxotrophs, in particular leucine auxotrophs, are sensitive to rapamycin. This sensitivity is suppressed by deletion of the S. pombe FKBP12 or by introducing a rapamycin-binding defective tor1 allele, suggesting that rapamycin inhibits a tor1p-dependent function. Sensitivity of leucine auxotrophs to rapamycin is observed when ammonia is used as the nitrogen source and can be suppressed by its replacement with proline. Consistently, using radioactive labeled leucine, we show that cells treated with rapamycin or disrupted for tor1+ are defective in leucine uptake when the nitrogen source is ammonia but not proline. Recently, it has been reported that tsc1+ and tsc2+, the S. pombe homologs for the mammalian TSC1 and TSC2, are also defective in leucine uptake. TSC1 and TSC2 may antagonize TOR signaling in mammalian cells and Drosophila. We show that reduction of leucine uptake in tor1 mutants is correlated with decreased expression of three putative amino acid permeases that are also downregulated in tsc1 or tsc2. These findings suggest a possible mechanism for regulation of leucine uptake by tor1p and indicate that tor1p, as well as tsc1p and tsc2p, positively regulates leucine uptake in S. pombe.","authors":"Weisman R, Roitburg I, Nahari T, Kupiec M","authors_abbrev":"Weisman R et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2004-10-07","publication_year":"2005","canto_session_key":"64464dca7a13a142","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-27 14:10:01","canto_approved_date":"2024-07-15 11:48:01","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-06-12 09:00:04","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPBC1A4.02c","SPAC869.10c","SPBC839.17c","SPAP7G5.06","SPAC1039.09","SPAC24B11.06c","SPBC409.07c","SPCC330.05c","SPBC30D10.10c"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2015-04-27"},{"uniquename":"PMID:17284852","title":"Mutational analyses of a single-stranded telomeric DNA binding domain of fission yeast pot1: conflict with X-ray crystallographic structure.","citation":"Biosci Biotechnol Biochem 2007 Feb;71(2):481-90","abstract":"To understand the telomere regulation mechanism in relation to cell aging and cancer, we examined the single-stranded telomeric DNA binding domain (ssDBD) of fission yeast telomere-binding protein Pot1 by constructing a series of deletion mutants. We found that Pot1(1-182) (amino acids 1-182) stably expressed in Escherichia coli without any degradation retained a stable folded structure and functional telomeric DNA binding activity, indicating that Pot1(1-182) corresponds to ssDBD. We investigated the amino acids of Pot1(1-182) involved in single-stranded telomeric DNA recognition by constructing a series of site-directed mutants. Although the previously reported X-ray crystallographic structure suggests that 12 amino acids contact the telomeric DNA, an electrophoretic mobility shift assay and isothermal titration calorimetry analyses of the binding ability of the site-directed mutants indicated that only five amino acids significantly contributed to telomeric DNA recognition. We conclude that the contribution to recognition is quite different in magnitude among the amino acids judged to contact the target by X-ray crystallographic structure.","authors":"Torigoe H, Dohmae N, Hanaoka F, Furukawa A","authors_abbrev":"Torigoe H et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-02-08","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008535","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9738888","title":"Mapping of Rpb3 and Rpb5 contact sites on two large subunits, Rpb1 and Rpb2, of the RNA polymerase II from fission yeast.","citation":"Mol Gen Genet 1998 Jul;259(1):123-9","abstract":"[Rpb1 and Rpb2] Mapping of the contact sites on two large subunits of the fission yeast Schizosaccharomyces pombe RNA polymerase II with two small subunits, Rpb3 and Rpb5, was carried out using the two-hybrid screening system in the budding yeast Saccharomyces cerevisiae. Rpb5 was found to interact with any fragment of Rpb1 that contained the region H, which is conserved among the subunit 1 homologues of all RNA polymerases, including the beta' subunit of prokaryotic RNA polymerases. In agreement with the fact that Rpb5 is shared among all three forms of eukaryotic RNA polymerases, the region H of RNA polymerase I subunit 1 (Rpa190) was also found to interact with Rpb5. On the other hand, two-hybrid screening of Rpb2 fragments from RNA polymerase II indicated the presence of an Rpb3 contact site in the region H which is conserved among the subunit 2 homologues of all RNA polymerases, including the beta subunit of prokaryotic RNA polymerases. Possible functions of the regions H in the subunits 1 and 2 are discussed.","authors":"Miyao T, Honda A, Qu Z, Ishihama A","authors_abbrev":"Miyao T et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-09-17","publication_year":"1998","canto_session_key":"c0001ba99ab29e83","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-06-12 14:01:43","canto_approved_date":"2024-02-07 16:13:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 14:00:44","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1442.10c","SPBC4C3.05c","SPAC23C4.15","SPAC23G3.01","SPBC28F2.12"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-06-12"},{"uniquename":"PMID:24277842","title":"Chemical map of Schizosaccharomyces pombe reveals species-specific features in nucleosome positioning.","citation":"Proc Natl Acad Sci U S A 2013 Dec 10;110(50):20158-63","abstract":"Using a recently developed chemical approach, we have generated a genome-wide map of nucleosomes in vivo in Schizosaccharomyces pombe (S. pombe) at base pair resolution. The shorter linker length previously identified in S. pombe is due to a preponderance of nucleosomes separated by ∼4/5 bp, placing nucleosomes on opposite faces of the DNA. The periodic dinucleotide feature thought to position nucleosomes is equally strong in exons as in introns, demonstrating that nucleosome positioning information can be superimposed on coding information. Unlike the case in Saccharomyces cerevisiae, A/T-rich sequences are enriched in S. pombe nucleosomes, particularly at ±20 bp around the dyad. This difference in nucleosome binding preference gives rise to a major distinction downstream of the transcription start site, where nucleosome phasing is highly predictable by A/T frequency in S. pombe but not in S. cerevisiae, suggesting that the genomes and DNA binding preferences of nucleosomes have coevolved in different species. The poly (dA-dT) tracts affect but do not deplete nucleosomes in S. pombe, and they prefer special rotational positions within the nucleosome, with longer tracts enriched in the 10- to 30-bp region from the dyad. S. pombe does not have a well-defined nucleosome-depleted region immediately upstream of most transcription start sites; instead, the -1 nucleosome is positioned with the expected spacing relative to the +1 nucleosome, and its occupancy is negatively correlated with gene expression. Although there is generally very good agreement between nucleosome maps generated by chemical cleavage and micrococcal nuclease digestion, the chemical map shows consistently higher nucleosome occupancy on DNA with high A/T content.","doi":"10.1073/pnas.1315809110","authors":"Moyle-Heyrman G, Zaichuk T, Xi L, Zhang Q, Uhlenbeck OC, Holmgren R, Widom J, Wang JP","authors_abbrev":"Moyle-Heyrman G et al.","pubmed_publication_date":"10 Dec 2013","pubmed_entrez_date":"2013-11-27","publication_year":"2013","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25402480","title":"RNA cytidine acetyltransferase of small-subunit ribosomal RNA: identification of acetylation sites and the responsible acetyltransferase in fission yeast, Schizosaccharomyces pombe.","citation":"PLoS One 2014;9(11):e112156","abstract":"The eukaryotic small-subunit (SSU) ribosomal RNA (rRNA) has two evolutionarily conserved acetylcytidines. However, the acetylation sites and the acetyltransferase responsible for the acetylation have not been identified. We performed a comprehensive MS-based analysis covering the entire sequence of the fission yeast, Schizosaccharomyces pombe, SSU rRNA and identified two acetylcytidines at positions 1297 and 1815 in the 3' half of the rRNA. To identify the enzyme responsible for the cytidine acetylation, we searched for an S. pombe gene homologous to TmcA, a bacterial tRNA N-acetyltransferase, and found one potential candidate, Nat10. A temperature-sensitive strain of Nat10 with a mutation in the Walker A type ATP-binding motif abolished the cytidine acetylation in SSU rRNA, and the wild-type Nat10 supplemented to this strain recovered the acetylation, providing evidence that Nat10 is necessary for acetylation of SSU rRNA. The Nat10 mutant strain showed a slow-growth phenotype and was defective in forming the SSU rRNA from the precursor RNA, suggesting that cytidine acetylation is necessary for ribosome assembly.","doi":"10.1371/journal.pone.0112156","authors":"Taoka M, Ishikawa D, Nobe Y, Ishikawa H, Yamauchi Y, Terukina G, Nakayama H, Hirota K, Takahashi N, Isobe T","authors_abbrev":"Taoka M et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-11-18","publication_year":"2014","canto_session_key":"47b885e9317af565","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masato Taoka","canto_first_approved_date":"2016-03-30 13:30:29","canto_approved_date":"2019-08-22 16:56:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-11-17 14:49:02","canto_added_date":"2014-11-19 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Masato Taoka","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPRRNA.44","SPRRNA.43","SPAC20G8.09c","SPRRNA.46"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2016-03-30"},{"uniquename":"PMID:20838651","title":"A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity.","citation":"PLoS Biol 2010 Sep 07;8(9)","abstract":"Ubiquitination and deubiquitination are reciprocal processes that tune protein stability, function, and/or localization. The removal of ubiquitin and remodeling of ubiquitin chains is catalyzed by deubiquitinating enzymes (DUBs), which are cysteine proteases or metalloproteases. Although ubiquitination has been extensively studied for decades, the complexity of cellular roles for deubiquitinating enzymes has only recently been explored, and there are still several gaps in our understanding of when, where, and how these enzymes function to modulate the fate of polypeptides. To address these questions we performed a systematic analysis of the 20 Schizosaccharomyces pombe DUBs using confocal microscopy, proteomics, and enzymatic activity assays. Our results reveal that S. pombe DUBs are present in almost all cell compartments, and the majority are part of stable protein complexes essential for their function. Interestingly, DUB partners identified by our study include the homolog of a putative tumor suppressor gene not previously linked to the ubiquitin pathway, and two conserved tryptophan-aspartate (WD) repeat proteins that regulate Ubp9, a DUB that we show participates in endocytosis, actin dynamics, and cell polarity. In order to understand how DUB activity affects these processes we constructed multiple DUB mutants and find that a quintuple deletion of ubp4 ubp5 ubp9 ubp15 sst2/amsh displays severe growth, polarity, and endocytosis defects. This mutant allowed the identification of two common substrates for five cytoplasmic DUBs. Through these studies, a common regulatory theme emerged in which DUB localization and/or activity is modulated by interacting partners. Despite apparently distinct cytoplasmic localization patterns, several DUBs cooperate in regulating endocytosis and cell polarity. These studies provide a framework for dissecting DUB signaling pathways in S. pombe and may shed light on DUB functions in metazoans.","doi":"10.1371/journal.pbio.1000471","authors":"Kouranti I, McLean JR, Feoktistova A, Liang P, Johnson AE, Roberts-Galbraith RH, Gould KL","authors_abbrev":"Kouranti I et al.","pubmed_publication_date":"07 Sep 2010","pubmed_entrez_date":"2010-09-15","publication_year":"2010","canto_session_key":"d2fab1f2b453d796","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-17 20:56:00","canto_approved_date":"2026-02-17 15:40:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-09 19:15:09","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13C5.01c","SPAC23D3.07","SPCC1682.16","SPBC19C2.04c","SPCC1682.12c","SPBC1703.12","SPAC19B12.10","SPAC607.05","SPAC323.02c","SPAC3A11.12c","SPBC119.01","SPCC188.08c","SPBC6B1.06c","SPBC16G5.01","SPAC688.11","SPBC4.07c","SPBP19A11.03c","SPAC22F8.06","SPAC637.10c","SPBC17D11.07c","SPAC31A2.14","SPBP8B7.11","SPBC106.16","SPBC713.02c","SPBC646.16","SPCC1494.05c","SPAC1952.03","HGNC:20080","SPBC18H10.20c","SPAC6G9.08","SPBC577.10","SPBC18H10.08c","SPCC1442.06","SPAC328.06","SPAC6G10.04c","SPAC31A2.04c","SPAC31G5.13","SPBC146.13c","SPBC342.04","SPCC1682.10","SPBC6B1.12c","SPCC16A11.16c","SPAC24C9.14","SPAC12B10.03","SPAC27F1.03c","SPBC23G7.12c","SPBC409.06","SPBP16F5.03c","SPCC126.04c","SPAC1782.01","SPAC6C3.08","SPAC17A5.16","SPAC11G7.02","SPBC1921.07c","SPAC7D4.02c","SPBC4C3.10c","SPBP8B7.21","SPAC13A11.04c","SPAC6B12.12","SPBC582.07c","SPAC3F10.13","SPCC16A11.12c","SPAC4F10.15c","SPCC63.12c","SPAC23G3.08c","SPAC23G3.11","SPAC1565.08","SPBC16C6.07c","SPCC1795.04c","SPCC576.10c","SPAC1420.03","SPAC4A8.13c"],"gene_count":71,"ltp_gene_count":19,"approved_date":"2018-02-17"},{"uniquename":"PMID:16911509","title":"The COX18 gene, involved in mitochondrial biogenesis, is functionally conserved and tightly regulated in humans and fission yeast.","citation":"FEMS Yeast Res 2006 Sep;6(6):869-82","abstract":"The biogenesis of cytochrome c oxidase requires coordination between the nucleus and mitochondria because both these compartments provide the structural subunits of this enzyme. In addition, synthesis, membrane insertion and assembly of the mitochondrially encoded subunits are controlled in a concerted way by numerous nuclear-encoded factors, including Oxa1 and Cox18, which play successive roles in Cox2 assembly in Saccharomyces cerevisiae. These two factors share a weak structural similarity and define two sub-branches of the Oxa1/YidC/Alb3 gene family, whose members facilitate the membrane insertion of various hydrophobic proteins into diverse biological membranes. In this study, we have analyzed a second human and a third fission yeast member of the family. We show, by deletion in the fission yeast genome, as well as expression and functional complementation experiments in both yeasts, that these new genes belong to the COX18 rather than to the OXA1 sub-branch. So far, the fission yeast gene cox18Sp+ is the smallest functional member of this gene family. COX18Hs gives rise to various mRNAs with different coding capacities, and we show that cox18Sp+ and COX18Hs are expressed at a low level and appear to be stringently regulated. This transcriptional control contrasts with the constitutive abundance of the OXA1 mRNAs and might reflect major functional differences between these nevertheless structurally related genes.","authors":"Gaisne M, Bonnefoy N","authors_abbrev":"Gaisne M et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-08-17","publication_year":"2006","canto_session_key":"186afb71f7c18a89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-07 20:28:52","canto_approved_date":"2025-12-06 09:44:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-23 16:06:14","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.03","SPMIT.11","SPCC1442.15c","SPCC1442.14c","SPAC9G1.04","SPCC1442.16c"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2018-08-07"},{"uniquename":"PMID:17641464","title":"Recombinant Schizosaccharomyces pombe Nth1 protein exhibits DNA glycosylase activities for 8-oxo-7,8-dihydroguanine and thymine residues oxidized in the methyl group.","citation":"J Radiat Res 2007 Sep;48(5):417-24","abstract":"Bacteria and eukaryotes possess redundant enzymes that recognize and remove oxidatively damaged bases from DNA through base excision repair. DNA glycosylases remove damaged bases to initiate the base excision repair. The exocyclic methyl group of thymine does not escape oxidative damage to produce 5-formyluracil (5-foU) and 5-hydroxymethyluracil (5-hmU). 5-foU is a potentially mutagenic lesion. A homolog of E. coli endonuclease III (SpNth1) had been identified and characterized in Schizosaccharomyces pombe. In this study, we found that SpNth1 recognizes and removes 5-foU and 5-hmU from DNA with similar efficiency. The specific activities for the removal of 5-foU and 5-hmU were comparable with that for thymine glycol. The expression of SpNth1 reduced the hydrogen peroxide toxicity and the frequency of spontaneous mutations in E. coli nth nei mutant. It was also revealed that SpNth1 had DNA glycosylase activity for removing 8-oxo-7,8-dihydroguanine (8-oxoG) from 8-oxoG/G and 8-oxoG/A mispairs. These results indicated that SpNth1 has a broad substrate specificity and is involved in the base excision repair of 8-oxoG and thymine residues oxidized in the methyl group in S. pombe.","authors":"Yonekura S, Nakamura N, Doi T, Sugiyama H, Yamamoto K, Yonei S, Zhang QM","authors_abbrev":"Yonekura S et al.","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-07-21","publication_year":"2007","canto_session_key":"356822eb6bb51d7e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-10-25 15:07:09","canto_approved_date":"2018-10-25 15:07:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-25 15:06:10","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-25"},{"uniquename":"PMID:22024164","title":"Multiple pathways can bypass the essential role of fission yeast Hsk1 kinase in DNA replication initiation.","citation":"J Cell Biol 2011 Oct 31;195(3):387-401","abstract":"Cdc7/Hsk1 is a conserved kinase required for initiation of DNA replication that potentially regulates timing and locations of replication origin firing. Here, we show that viability of fission yeast hsk1Δ cells can be restored by loss of mrc1, which is required for maintenance of replication fork integrity, by cds1Δ, or by a checkpoint-deficient mutant of mrc1. In these mutants, normally inactive origins are activated in the presence of hydroxyurea and binding of Cdc45 to MCM is stimulated. mrc1Δ bypasses hsk1Δ more efficiently because of its checkpoint-independent inhibitory functions. Unexpectedly, hsk1Δ is viable at 37°C. More DNA is synthesized, and some dormant origins fire in the presence of hydroxyurea at 37°C. Furthermore, hsk1Δ bypass strains grow poorly at 25°C compared with higher temperatures. Our results show that Hsk1 functions for DNA replication can be bypassed by different genetic backgrounds as well as under varied physiological conditions, providing additional evidence for plasticity of the replication program in eukaryotes.","doi":"10.1083/jcb.201107025","authors":"Matsumoto S, Hayano M, Kanoh Y, Masai H","authors_abbrev":"Matsumoto S et al.","pubmed_publication_date":"31 Oct 2011","pubmed_entrez_date":"2011-10-26","publication_year":"2011","canto_session_key":"505fabad6506e06e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-07 15:58:16","canto_approved_date":"2024-04-03 09:02:22","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-06-07 15:58:11","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":46,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC694.06c","SPBC776.12c","SPBC4.04c","SPCC550.13","SPAC17D4.02"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-06-07"},{"uniquename":"PMID:3997783","title":"Buoyant density constancy of Schizosaccharomyces pombe cells.","citation":"J Bacteriol 1985 Jun;162(3):902-4","abstract":"Buoyant densities of cells from exponentially growing cultures of the fission yeast Schizosaccharomyces pombe 972h- with division rates from 0.14 to 0.5 per h were determined by equilibrium centrifugation in Percoll gradients. Buoyant densities were independent of growth rate, with an average value (+/- standard error) of 1.0945 (+/- 0.00037) g/ml. When cells from these cultures were separated by size, mean cell volumes were independent of buoyant density, indicating that buoyant densities also were independent of cell age during the division cycle. These results support the suggestion that most or all kinds of cells that divide by equatorial fission may have similar, evolutionarily conserved mechanisms for regulation of buoyant density.","authors":"Kubitschek HE, Ward RA","authors_abbrev":"Kubitschek HE et al.","pubmed_publication_date":"Jun 1985","pubmed_entrez_date":"1985-06-01","publication_year":"1985","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19581297","title":"Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading.","citation":"J Biol Chem 2009 Aug 28;284(35):23852-9","abstract":"The preproteins targeted to the mitochondria are transported through the translocase of the outer membrane complex. Tom70/Tom71 is a major surface receptor of the translocase of the outer membrane complex for mitochondrial preproteins. The preproteins are escorted to Tom70/Tom71 by molecular chaperones Hsp70 and Hsp90. Here we present the high resolution crystal structures of Tom71 and the protein complexes between Tom71 and the Hsp70/Hsp90 C terminus. The crystal structures indicate that Tom70/Tom71 may exhibit two distinct states. In the closed state, the N-terminal domain of Tom70/Tom71 partially blocks the preprotein-binding pocket. In the open state, the N-terminal domain moves away, and the preprotein-binding pocket is fully exposed. The complex formation between the C-terminal EEVD motif of Hsp70/Hsp90 and Tom71 could lock Tom71 in the open state where the preprotein-binding pocket of Tom71 is ready to receive preproteins. The interactions between Hsp70/Hsp90 and Tom71 N-terminal domain generate conformational changes that may increase the volume of the preprotein-binding pocket. The complex formation of Hsp70/Hsp90 and Tom71 also generates significant domain rearrangement within Tom71, which may position the preprotein-binding pocket closer to Hsp70/Hsp90 to facilitate the preprotein transfer from the molecular chaperone to Tom71. Therefore, molecular chaperone Hsp70/Hsp90 may function to prepare the mitochondrial outer membrane receptor Tom71 for preprotein loading.","doi":"10.1074/jbc.M109.023986","authors":"Li J, Qian X, Hu J, Sha B","authors_abbrev":"Li J et al.","pubmed_publication_date":"28 Aug 2009","pubmed_entrez_date":"2009-07-08","publication_year":"2009","canto_session_key":"340e6244d1796f31","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-02-15 17:26:17","canto_approved_date":"2023-02-16 19:11:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-15 17:25:59","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.04c","SPAC6B12.12","SPCC1739.13","SPAC13G7.02c"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2023-02-15","pdb_entries":[{"pdb_id":"3fp4","gene_chains":[{"gene_uniquename":"SPAC13G7.02c","chain":"Q","position":"633-644"}],"title":"Crystal structure of Tom71 complexed with Ssa1 C-terminal fragment","entry_authors":"Li J,Qian X,Hu J,Sha B","entry_authors_abbrev":"Li J et al.","reference_uniquename":"PMID:19581297","experimental_method":"X-ray","resolution":"2.14"}]},{"uniquename":"PMID:30606933","title":"[The Molecular Basis of Drug Discovery Targeting the Regulatory Mechanism of MAPK Signaling via the Spatial Regulation of RNA-binding Proteins].","citation":"Yakugaku Zasshi 2019;139(1):7-12","abstract":"Mitogen-activated protein kinase (MAPK) is a highly conserved serine/threonine kinase that regulates multiple cellular processes such as cell proliferation, differentiation, apoptosis, and inflammation. Rnc1 has been identified as a regulator of Pmk1 MAPK signaling, a homologue of extracellular signal-regulated kinase (ERK)-1 MAPK in mammals. Rnc1 encodes a K-homology (KH)-type RNA-binding protein (RBP). Previously, it was reported that Rnc1 acts as a negative regulator of Pmk1 MAPK signaling through the mRNA stabilization of Pmp1, the MAPK phosphatase for Pmk1 in our laboratory. We analyzed the spatial regulation of Rnc1 and discovered that Rnc1 is exported from the nucleus by the mRNA-export system. The nuclear export of Rnc1 is important for exerting its function to stabilize Pmp1 mRNA. Therefore, the spatial regulation of Rnc1 affects MAPK signaling activity. We also reported that Nrd1, an RRM-type RBP, plays a critical role in cytokinesis by binding to and stabilizing myosin mRNA. Notably, Rnc1 and Nrd1 localize to stress granules (SGs) in response to various environmental stresses. Moreover, SG formation is inhibited in the Nrd1 or Rnc1 deletion cells, whereas the overproduction of Nrd1 or Rnc1, as well as that of mammalian RBP TIA-1, induces granule formation. These data show that Nrd1 and Rnc1 regulate SG formation as a novel SG component. Alterations of SG formation are linked to neurodegenerative diseases and resistance to anti-cancer drugs, thus conferring remarkable clinical importance to SGs. This review discusses the spatial regulation of RBPs or SG formation as novel targets for drug discovery.","doi":"10.1248/yakushi.18-00189","authors":"Satoh R","authors_abbrev":"Satoh R","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-01-05","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-01-06 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27898700","title":"Sbg1 Is a Novel Regulator for the Localization of the β-Glucan Synthase Bgs1 in Fission Yeast.","citation":"PLoS One 2016;11(11):e0167043","abstract":"Glucan synthases synthesize glucans, complex polysaccharides that are the major components in fungal cell walls and division septa. Studying regulation of glucan synthases is important as they are essential for fungal cell survival and thus popular targets for anti-fungal drugs. Linear 1,3-β-glucan is the main component of primary septum and is synthesized by the conserved β-glucan synthase Bgs1 in fission yeast cytokinesis. It is known that Rho1 GTPase regulates Bgs1 catalytic activity and the F-BAR protein Cdc15 plays a role in Bgs1 delivery to the plasma membrane. Here we characterize a novel protein Sbg1 that is present in a complex with Bgs1 and regulates its protein levels and localization. Sbg1 is essential for contractile-ring constriction and septum formation during cytokinesis. Sbg1 and Bgs1 physically interact and are interdependent for localization to the plasma membrane. Bgs1 is less stable and/or mis-targeted to vacuoles in sbg1 mutants. Moreover, Sbg1 plays an earlier and more important role in Bgs1 trafficking and localization than Cdc15. Together, our data reveal a new mode of regulation for the essential β-glucan synthase Bgs1 by the novel protein Sbg1.","doi":"10.1371/journal.pone.0167043","authors":"Davidson R, Pontasch JA, Wu JQ","authors_abbrev":"Davidson R et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-11-30","publication_year":"2016","canto_session_key":"6710099b122fb72a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jian-Qiu Wu","canto_first_approved_date":"2019-01-04 21:53:21","canto_approved_date":"2024-04-15 11:24:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-10 19:58:53","canto_added_date":"2016-12-01 01:15:11","annotation_curators":[{"name":"Jian-Qiu Wu","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPAC20G8.05c","SPCC970.09","SPBP22H7.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-01-04"},{"uniquename":"PMID:9891039","title":"Fission yeast cdc24 is a replication factor C- and proliferating cell nuclear antigen-interacting factor essential for S-phase completion.","citation":"Mol Cell Biol 1999 Feb;19(2):1038-48","abstract":"At the nonpermissive temperature the fission yeast cdc24-M38 mutant arrests in the cell cycle with incomplete DNA replication as indicated by pulsed-field gel electrophoresis. The cdc24(+) gene encodes a 501-amino-acid protein with no significant homology to any known proteins. The temperature-sensitive cdc24 mutant is effectively rescued by pcn1(+), rfc1(+) (a fission yeast homologue of RFC1), and hhp1(+), which encode the proliferating cell nuclear antigen (PCNA), the large subunit of replication factor C (RFC), and a casein kinase I involved in DNA damage repair, respectively. The Cdc24 protein binds PCNA and RFC1 in vivo, and the domains essential for Cdc24 function and for RFC1 and PCNA binding colocalize in the N-terminal two-thirds of the molecule. In addition, cdc24(+) genetically interacts with the gene encoding the catalytic subunit of DNA polymerase epsilon, which is stimulated by PCNA and RFC, and with those encoding the fission yeast counterparts of Mcm2, Mcm4, and Mcm10. These results indicate that Cdc24 is an RFC- and PCNA-interacting factor required for DNA replication and might serve as a target for regulation.","authors":"Tanaka H, Tanaka K, Murakami H, Okayama H","authors_abbrev":"Tanaka H et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-01-16","publication_year":"1999","canto_session_key":"4dc5dac60241db83","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-03-19 16:24:55","canto_approved_date":"2019-12-17 15:57:37","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-03-19 16:24:51","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4.04c","SPBC25H2.13c","SPBC3H7.15","SPAC1952.07","SPBC23E6.07c","SPAC8F11.07c","SPCC16A11.17","SPBC1347.10","SPBC16D10.09"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2015-03-19"},{"uniquename":"PMID:33330476","title":"Comparative Analysis of the Roles of Non-muscle Myosin-IIs in Cytokinesis in Budding Yeast, Fission Yeast, and Mammalian Cells.","citation":"Front Cell Dev Biol 2020;8:593400","abstract":"The contractile ring, which plays critical roles in cytokinesis in fungal and animal cells, has fascinated biologists for decades. However, the basic question of how the non-muscle myosin-II and actin filaments are assembled into a ring structure to drive cytokinesis remains poorly understood. It is even more mysterious why and how the budding yeast  Saccharomyces cerevisiae , the fission yeast  Schizosaccharomyces pombe , and humans construct the ring structure with one, two, and three myosin-II isoforms, respectively. Here, we provide a comparative analysis of the roles of the non-muscle myosin-IIs in cytokinesis in these three model systems, with the goal of defining the common and unique features and highlighting the major questions regarding this family of proteins.","doi":"10.3389/fcell.2020.593400","authors":"Wang K, Okada H, Bi E","authors_abbrev":"Wang K et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-12-17","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-12-19 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC146.13c","SPAC4A8.05c","SPCC645.05c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:14759138","title":"Gluconic acid consumption in wines by Schizosaccharomyces pombe and its effect on the concentrations of major volatile compounds and polyols.","citation":"J Agric Food Chem 2004 Feb 11;52(3):493-7","abstract":"Schizosaccharomyces pombe 1379 (ATCC 26760) yeast strain in wine substantially increases acetaldehyde and 1,1-diethoxyethane concentrations and to decreases levo-2,3-butanediol, glycerol, acetoin, and gluconic acid concentrations. In this study, S. pombe has been used for the first time to reduce gluconic acid in wine under aerobic conditions. Only acetaldehyde and acetoin exhibited significantly higher levels in the wines containing gluconic acid. The high in vitro specific activity of alcohol dehydrogenase observed may be directly related to the high production of acetaldehyde by the studied fission yeast.","authors":"Peinado RA, Moreno JJ, Maestre O, Ortega JM, Medina M, Mauricio JC","authors_abbrev":"Peinado RA et al.","pubmed_publication_date":"11 Feb 2004","pubmed_entrez_date":"2004-02-05","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26648030","title":"Chromosomal context and replication properties of ARS plasmids in Schizosaccharomyces pombe.","citation":"J Biosci 2015 Dec;40(5):845-53","abstract":"Short, specific DNA sequences called as Autonomously Replicating Sequence (ARS) elements function as plasmid as well as chromosomal replication origins in yeasts. As compared to ARSs, different chromosomal origins vary greatly in their efficiency and timing of replication probably due to their wider chromosomal context. The two Schizosaccharomyces pombe ARS elements, ars727 and ars2004, represent two extremities in their chromosomal origin activity - ars727 is inactive and late replicating, while ars2004 is a highly active, early-firing origin. To determine the effect of chromosomal context on the activity of these ARS elements, we have cloned them with their extended chromosomal context as well as in the context of each other in both orientations and analysed their replication efficiency by ARS and plasmid stability assays. We found that these ARS elements retain their origin activity in their extended/altered context. However, deletion of a 133-bp region of the previously reported ars727- associated late replication enforcing element (LRE) caused advancement in replication timing of the resulting plasmid. These results confirm the role of LRE in directing plasmid replication timing and suggest that the plasmid origin efficiency of ars2004 or ars727 remains unaltered by the extended chromosomal context.","authors":"Pratihar AS, Tripathi VP, Yadav MP, Dubey DD","authors_abbrev":"Pratihar AS et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-12-10","publication_year":"2015","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2015-12-11 01:19:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39094569","title":"The fork protection complex promotes parental histone recycling and epigenetic memory.","citation":"Cell 2024 Jul 26;","abstract":"The inheritance of parental histones across the replication fork is thought to mediate epigenetic memory. Here, we reveal that fission yeast Mrc1 (CLASPIN in humans) binds H3-H4 tetramers and operates as a central coordinator of symmetric parental histone inheritance. Mrc1 mutants in a key connector domain disrupted segregation of parental histones to the lagging strand comparable to Mcm2 histone-binding mutants. Both mutants showed clonal and asymmetric loss of H3K9me-mediated gene silencing. AlphaFold predicted co-chaperoning of H3-H4 tetramers by Mrc1 and Mcm2, with the Mrc1 connector domain bridging histone and Mcm2 binding. Biochemical and functional analysis validated this model and revealed a duality in Mrc1 function: disabling histone binding in the connector domain disrupted lagging-strand recycling while another histone-binding mutation impaired leading strand recycling. We propose that Mrc1 toggles histones between the lagging and leading strand recycling pathways, in part by intra-replisome co-chaperoning, to ensure epigenetic transmission to both daughter cells.","doi":"10.1016/j.cell.2024.07.017","authors":"Charlton SJ, Flury V, Kanoh Y, Genzor AV, Kollenstart L, Ao W, Brøgger P, Weisser MB, Adamus M, Alcaraz N, Delvaux de Fenffe CM, Mattiroli F, Montoya G, Masai H, Groth A, Thon G","authors_abbrev":"Charlton SJ et al.","pubmed_publication_date":"26 Jul 2024","pubmed_entrez_date":"2024-08-02","publication_year":"2024","canto_session_key":"ab073ff22c7e8688","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-08-03 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22056467","title":"Formins filter modified actin subunits during processive elongation.","citation":"J Struct Biol 2012 Jan;177(1):32-9","abstract":"Fission yeast cells reject actin subunits tagged with a fluorescent protein from the cytokinetic contractile ring, so cytokinesis fails and the cells die when the native actin gene is replaced by GFP-actin. The lack of a fluorescent actin probe has prevented a detailed study of actin filament dynamics in contractile rings, and left open questions regarding the mechanism of cytokinesis. To incorporate fluorescent actin into the contractile ring to study its dynamics, we introduced the coding sequence for a tetracysteine motif (FLNCCPGCCMEP) at 10 locations in the fission yeast actin gene and expressed the mutant proteins from the native actin locus in diploid cells with wild-type actin on the other chromosome. We labeled these tagged actins inside live cells with the FlAsH reagent. Cells incorporated some of these labeled actins into actin patches at sites of endocytosis, where Arp2/3 complex nucleates all of the actin filaments. However, the cells did not incorporate any of the FlAsH-actins into the contractile ring. Therefore, formin Cdc12p rejects actin subunits with a tag of ~2 kDa, illustrating the stringent structural requirements for this formin to promote the elongation of actin filament barbed ends as it moves processively along the end of a growing filament.","doi":"10.1016/j.jsb.2011.10.005","authors":"Chen Q, Nag S, Pollard TD","authors_abbrev":"Chen Q et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2011-11-08","publication_year":"2012","canto_session_key":"592669078703fcf9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-10-30 13:49:57","canto_approved_date":"2019-10-30 13:49:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-30 13:49:40","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F5.04c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-10-30"},{"uniquename":"PMID:34288736","title":"Cdc42 GTPase-activating proteins (GAPs) regulate generational inheritance of cell polarity and cell shape in fission yeast.","citation":"Mol Biol Cell 2021 Oct 01;32(20):ar14","abstract":"The highly conserved small GTPase Cdc42 regulates polarized cell growth and morphogenesis from yeast to humans. We previously reported that Cdc42 activation exhibits oscillatory dynamics at cell tips of  Schizosaccharomyces pombe  cells. Mathematical modeling suggests that this dynamic behavior enables a variety of symmetric and asymmetric Cdc42 activation distributions to coexist in cell populations. For individual wild-type cells, however, Cdc42 distribution is initially asymmetrical and becomes more symmetrical as cell volume increases, enabling bipolar growth activation. To explore whether different patterns of Cdc42 activation are possible in vivo, we examined  S. pombe rga4∆  mutant cells, lacking the Cdc42 GTPase-activating protein (GAP) Rga4. We found that monopolar  rga4∆  mother cells divide asymmetrically leading to the emergence of both symmetric and asymmetric Cdc42 distributions in  rga4∆  daughter cells. Motivated by different hypotheses that can mathematically reproduce the unequal fate of daughter cells, we used genetic screening to identify mutants that alter the  rga4∆  phenotype. We found that the unequal distribution of active Cdc42 GTPase is consistent with an unequal inheritance of another Cdc42 GAP, Rga6, in the two daughter cells. Our findings highlight the crucial role of Cdc42 GAP localization in maintaining consistent Cdc42 activation and growth patterns across generations.","doi":"10.1091/mbc.E20-10-0666","authors":"Pino MR, Nuñez I, Chen C, Das ME, Wiley DJ, D'Urso G, Buchwald P, Vavylonis D, Verde F","authors_abbrev":"Pino MR et al.","pubmed_publication_date":"01 Oct 2021","pubmed_entrez_date":"2021-07-21","publication_year":"2021","canto_session_key":"8d7e7ba24e382834","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-07-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17708967","title":"Proteins that bind to double-stranded regions of telomeric DNA.","citation":"Trends Cell Biol 1997 Aug;7(8):317-24","abstract":"In budding yeast, the DNA-binding protein Rap1p orchestrates a negative feedback on regulation of telomere length and the organization of a heterochromatin-like telomeric compartment. Recent studies have led to the identification of functionally related telomeric proteins from fission yeast and mammals. These advances underline the key role played by the proteins that bind to the duplex part of telomeric DNA and reveal an important structural diversity among telomeric proteins.","authors":"Blue C, Marcand S, Gilson E","authors_abbrev":"Blue C et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000069","title":"Representation of transmembrane transport of a chemical as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the transmembrane transport of a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom template is \"GO:0055085 and 'transports or maintains localization of' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26856595","title":"A cohesin-based structural platform supporting homologous chromosome pairing in meiosis.","citation":"Curr Genet 2016 Aug;62(3):499-502","abstract":"The pairing and recombination of homologous chromosomes during the meiotic prophase is necessary for the accurate segregation of chromosomes in meiosis. However, the mechanism by which homologous chromosomes achieve this pairing has remained an open question. Meiotic cohesins have been shown to affect chromatin compaction; however, the impact of meiotic cohesins on homologous pairing and the fine structures of cohesion-based chromatin remain to be determined. A recent report using live-cell imaging and super-resolution microscopy demonstrated that the lack of meiotic cohesins alters the chromosome axis structures and impairs the pairing of homologous chromosomes. These results suggest that meiotic cohesin-based chromosome axis structures are crucial for the pairing of homologous chromosomes.","doi":"10.1007/s00294-016-0570-x","authors":"Ding DQ, Haraguchi T, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"Aug 2016","pubmed_entrez_date":"2016-02-10","publication_year":"2016","canto_session_key":"31589d60a96cbf0e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-11 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39874873","title":"In silico protein structural analysis of PRMT5 and RUVBL1 mutations arising in human cancers.","citation":"Cancer Genet 2025 Jan 17;292-293:49-56","abstract":"DNA double strand breaks (DSBs) can be generated spontaneously during DNA replication and are repaired primarily by Homologous Recombination (HR). However, efficient repair requires chromatin remodeling to allow the recombination machinery access to the break. TIP60 is a complex conserved from yeast to humans that is required for histone acetylation and modulation of HR activity at DSBs. Two enzymatic activities within the TIP60 complex, KAT5 (a histone acetyltransferase) and RUVBL1 (an AAA+ ATPase) are required for efficient HR repair. Post-translational modification of RUVBL1 by the PRMT5 methyltransferase activates the complex acetyltransferase activity and facilitates error free HR repair. In S. pombe a direct interaction between PRMT5 and the acetyltransferase subunit of the TIP60 complex (KAT5) was also identified. The TIP60 complex has been partially solved experimentally in both humans and S. cerevisiae, but not S. pombe. Here, we used in silico protein structure analysis to investigate structural conservation between S. pombe and human PRMT5 and RUVBL1. We found that there is more similarity in structure conservation between S. pombe and human proteins than between S. cerevisiae and human. Next, we queried the COSMIC database to analyze how mutations occurring in human cancers affect the structure and function of these proteins. Artificial intelligence algorithms that predict how likely mutations are to promote cellular transformation and immortalization show that RUVBL1 mutations should have a more drastic effect than PRMT5. Indeed, in silico protein structural analysis shows that PRMT5 mutations are less likely to destabilize enzyme function. Conversely, most RUVBL1 mutations occur in a region required for interaction with its partner (RUVBL2). These data suggests that cancer mutations could destabilize the TIP60 complex. Sequence conservation analysis between S. pombe and humans shows that the residues identified in cancer cells are highly conserved, suggesting that this may be an essential process in eukaryotic DSB repair. These results shed light on mechanisms of DSB repair and also highlight how S. pombe remains a great model system for analyzing DSB repair processes that are tractable in human cells.","doi":"10.1016/j.cancergen.2025.01.002","authors":"Al-Marrawi M, Petreaca RC, Bouley RA","authors_abbrev":"Al-Marrawi M et al.","pubmed_publication_date":"17 Jan 2025","pubmed_entrez_date":"2025-01-28","publication_year":"2025","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2025-01-30 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26212881","title":"Morphogenesis of the Fission Yeast Cell through Cell Wall Expansion.","citation":"Curr Biol 2015 Aug 17;25(16):2150-7","abstract":"The shape of walled cells such as fungi, bacteria, and plants are determined by the cell wall. Models for cell morphogenesis postulate that the effects of turgor pressure and mechanical properties of the cell wall can explain the shapes of these diverse cell types. However, in general, these models await validation through quantitative experiments. Fission yeast Schizosaccharomyces pombe are rod-shaped cells that grow by tip extension and then divide medially through formation of a cell wall septum. Upon cell separation after cytokinesis, the new cell ends adopt a rounded morphology. Here, we show that this shape is generated by a very simple mechanical-based mechanism in which turgor pressure inflates the elastic cell wall in the absence of cell growth. This process is independent of actin and new cell wall synthesis. To model this morphological change, we first estimate the mechanical properties of the cell wall using several approaches. The lateral cell wall behaves as an isotropic elastic material with a Young's modulus of 50 ± 10 MPa inflated by a turgor pressure estimated to be 1.5 ± 0.2 MPa. Based upon these parameters, we develop a quantitative mechanical-based model for new end formation that reveals that the cell wall at the new end expands into its characteristic rounded shape in part because it is softer than the mature lateral wall. These studies provide a simple example of how turgor pressure expands the elastic cell wall to generate a particular cell shape.","doi":"10.1016/j.cub.2015.06.059","authors":"Atilgan E, Magidson V, Khodjakov A, Chang F","authors_abbrev":"Atilgan E et al.","pubmed_publication_date":"17 Aug 2015","pubmed_entrez_date":"2015-07-28","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-07-29 00:21:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8648244","title":"Effect of B-type cyclin over-expression on radiation-induced mitotic delay in the fission yeast.","citation":"Int J Radiat Biol 1996 May;69(5):565-73","abstract":"Exposure to ionizing radiation temporarily blocks eukaryotic cell cycle progression at the G2/M boundary (G2 delay). The delay probably provides time for repair of DNA damage before chromosome segregation and is thus an active response, indicative of a checkpoint control function. Transition from G2 into mitosis is normally controlled by the activity of a cyclin-dependent kinase, cdc2 in the fission yeast (Schizosaccharomyces pombe). Genetic and cell kinetic evidence suggest that irradiation may impose mitotic delay by inactivation of the cdc2 product, p34cdc2. The activity of p34cdc2 in G2 is regulated by phosphorylation and association with a B-type cyclin, the product of the cdc13 gene, p56cdc13. Previous work does not support a major role for changes in phosphorylation of p34cdc2 in the induction of mitotic delay. Alternatively the kinase may be regulated by changes in the activity/availability of p56cdc13. We have therefore tested the effect of high level, episomal expression of the cdc13 gene on the induction of mitotic delay. No influence of this procedure on the duration of delay was detected, either in a wild-type cell cycle background, or the mutants wee1-50 and cdc2-3w, which show abnormal phosphorylation of p34cdc2.","authors":"Rowley R, Zhang J","authors_abbrev":"Rowley R et al.","pubmed_publication_date":"May 1996","pubmed_entrez_date":"1996-05-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:Z46263","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8070408","title":"Telomere-associated chromosome breakage in fission yeast results in variegated expression of adjacent genes.","citation":"EMBO J 1994 Aug 15;13(16):3801-11","abstract":"The sequence requirements for in vivo telomere function in the fission yeast, Schizosaccharomyces pombe, have been investigated. A 258 bp tract of previously characterized cloned fission yeast terminal repeats adjacent to 800 bp of telomere-associated sequences is sufficient to seed new telomeres onto linearized ars-containing plasmids when introduced into cells. The resulting transformants contain unrearranged, acentric, linear episomes. Cloned telomeres, with and without telomere-associated sequences adjacent to the 258 bp terminal repeats, were utilized to introduce chromosome breaks at specific sites in a non-essential minichromosome. Truncated minichromosome derivatives were recovered containing the ura4 or ade6 gene adjacent to a newly formed telomere. These telomeres exert reversible position effects on the expression of the adjacent ura4 or ade6 genes.","authors":"Nimmo ER, Cranston G, Allshire RC","authors_abbrev":"Nimmo ER et al.","pubmed_publication_date":"15 Aug 1994","pubmed_entrez_date":"1994-08-15","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ251855","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19214192","title":"Differential arrival of leading and lagging strand DNA polymerases at fission yeast telomeres.","citation":"EMBO J 2009 Apr 08;28(7):810-20","abstract":"To maintain genomic integrity, telomeres must undergo switches from a protected state to an accessible state that allows telomerase recruitment. To better understand how telomere accessibility is regulated in fission yeast, we analysed cell cycle-dependent recruitment of telomere-specific proteins (telomerase Trt1, Taz1, Rap1, Pot1 and Stn1), DNA replication proteins (DNA polymerases, MCM, RPA), checkpoint protein Rad26 and DNA repair protein Nbs1 to telomeres. Quantitative chromatin immunoprecipitation studies revealed that MCM, Nbs1 and Stn1 could be recruited to telomeres in the absence of telomere replication in S-phase. In contrast, Trt1, Pot1, RPA and Rad26 failed to efficiently associate with telomeres unless telomeres are actively replicated. Unexpectedly, the leading strand DNA polymerase epsilon (Polepsilon) arrived at telomeres earlier than the lagging strand DNA polymerases alpha (Polalpha) and delta (Poldelta). Recruitment of RPA and Rad26 to telomeres matched arrival of DNA Polepsilon, whereas S-phase specific recruitment of Trt1, Pot1 and Stn1 matched arrival of DNA Polalpha. Thus, the conversion of telomere states involves an unanticipated intermediate step where lagging strand synthesis is delayed until telomerase is recruited.","doi":"10.1038/emboj.2009.31","authors":"Moser BA, Subramanian L, Chang YT, Noguchi C, Noguchi E, Nakamura TM","authors_abbrev":"Moser BA et al.","pubmed_publication_date":"08 Apr 2009","pubmed_entrez_date":"2009-02-14","publication_year":"2009","canto_session_key":"88f8cd06ecf00d84","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-05-05 08:26:56","canto_approved_date":"2025-09-03 14:43:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-25 13:11:12","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4.04c","SPAC16A10.07c","SPBC409.12c","SPBC6B1.09c","SPAC3H5.06c","SPBC25H2.13c","SPAC26H5.06","SPBC29A3.14c","SPBC336.04","SPBC660.13c","SPBC1778.02","SPAC9E9.08"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2015-05-05"},{"uniquename":"PMID:41525994","title":"Transcriptional PBR cycles at pericentromeric repeats cause gross chromosomal rearrangements through Rad52-dependent ADR-loop formation.","citation":"Nucleic Acids Res 2026 Jan 05;54(1)","abstract":"Heterochromatin marked by histone H3 lysine 9 (H3K9) methylation represses transcription of pericentromeric repeats, thereby suppressing gross chromosomal rearrangements (GCRs). However, it remains unclear how transcription causes GCRs when heterochromatin is lost. Using fission yeast, we show that transcriptional Pausing-Backtracking-Restart (PBR) cycles accumulate R-loops, leading to GCRs. DNA-RNA immunoprecipitation (DRIP) revealed that loss of Clr4, the H3K9 methyltransferase, increased R-loops at pericentromeric repeats. Overexpression of RNaseH1 in clr4∆ cells reduced both R-loops and GCRs, demonstrating that R-loops cause GCRs. Tfs1/TFIIS and Ubp3, required for transcriptional restart, and Seb1, involved in pausing at pericentromeres, were required for R-loop accumulation and GCRs, implicating PBR cycles in the formation of genotoxic R-loops. We also demonstrate that Rad52 recombinase localizes to pericentromeric repeats and facilitates GCRs in clr4∆ cells. rad52-R45K, which impairs single-strand annealing (SSA), reduced GCRs. A single-stranded DNA (ssDNA) region within an R-loop may anneal to homologous ssDNA to form Annealing-induced DNA-RNA-loops (ADR-loops). Indeed, Rad52 facilitated ADR-loop formation in vitro. Polδ was also involved in GCRs. These data suggest that, when heterochromatin is lost, transcriptional PBR cycles accumulate R-loops at pericentromeric repeats, and Rad52-dependent SSA converts R-loops into ADR-loops followed by Polδ-dependent break-induced replication (BIR), resulting in homology-mediated GCRs.","doi":"10.1093/nar/gkaf1455","authors":"Xu R, Tang C, Wang JN, Motooka D, Tsubouchi H, Iwasaki H, Nakagawa T","authors_abbrev":"Xu R et al.","pubmed_publication_date":"05 Jan 2026","pubmed_entrez_date":"2026-01-12","publication_year":"2026","canto_session_key":"8f5ff81c170793f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takuro Nakagawa","canto_first_approved_date":"2026-05-22 05:54:43","canto_approved_date":"2026-05-22 05:54:43","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-05-12 04:22:47","canto_added_date":"2026-01-14 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":38,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Takuro Nakagawa","community_curator":true,"annotation_count":29,"orcid":"0000-0003-3455-8224","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.02","SPAC3C7.03c","SPBC428.08c","SPBC354.10","SPBP8B7.21","SPAC6G9.10c","SPBC13E7.08c","SPBC1347.01c","SPAC688.10","SPBC336.04","SPAC222.09","SPBC336.06c","SPCC11E10.08","SPAC30D11.10","SPAC17D4.02","SPCC4G3.05c","SPAC644.14c","SPAC20H4.03c","SPBC1734.02c","SPBC3E7.08c","SPAC664.01c","SPCP25A2.02c"],"gene_count":22,"ltp_gene_count":22,"approved_date":"2026-05-22"},{"uniquename":"PMID:40501888","title":"A distinct phase of cyclin B (Cdc13) nuclear export at mitotic entry in  S. pombe .","citation":"bioRxiv 2025 Jun 06;","abstract":"In eukaryotes, cell division requires coordination between the nucleus and cytoplasm. Entry into cell division is driven by cyclin-dependent kinases (CDKs), which need a cyclin binding partner for their activity. In  Schizosaccharomyces pombe  (fission yeast), the B-type cyclin Cdc13 is essential and sufficient for cell cycle progression and is strongly enriched in the nucleus. Here, we show that a fraction of Cdc13 is exported from the nucleus to the cytoplasm just prior to mitosis. This export could be critical to propagate CDK activity throughout the cell. Mutating three Cdc13 nuclear localization signals (NLSs) led to precocious enrichment of Cdc13 in the cytoplasm but did not accelerate mitotic entry, indicating that the export is not sufficient to trigger entry into mitosis. The export coincides with spindle pole body integration into the nuclear envelope and may be required to coordinate nuclear and cytoplasmic signaling required for this integration. The onset and stop of Cdc13 nuclear export are remarkably abrupt, underscoring that  S. pombe  mitotic entry consists of several switch-like transitions over the course of minutes. Our findings add another instance to the various cyclin nuclear transport events known to occur at critical cell cycle transitions throughout eukaryotes.","doi":"10.1101/2025.06.05.658100","authors":"Chethan SG, Rogers JM, Vijayakumari D, Williams W, Gligorovski V, Rahi SJ, Hauf S","authors_abbrev":"Chethan SG et al.","pubmed_publication_date":"06 Jun 2025","pubmed_entrez_date":"2025-06-12","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-06-12 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1448066","title":"Purine biosynthetic genes are required for cadmium tolerance in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1992 Dec;12(12):5301-10","abstract":"Phytochelatins (PCs) are metal-chelating peptides produced in plants and some fungi in response to heavy metal exposure. A Cd-sensitive mutant of the fission yeast Schizosaccharomyces pombe, defective in production of a PC-Cd-sulfide complex essential for metal tolerance, was found to harbor mutations in specific genes of the purine biosynthetic pathway. Genetic analysis of the link between metal complex accumulation and purine biosynthesis enzymes revealed that genetic lesions blocking two segments of the pathway, before and after the IMP branchpoint, are required to produce the Cd-sensitive phenotype. The biochemical functions of these two segments of the pathway are similar, and a model based on the alternate use of a sulfur analog substrate is presented. The novel participation of purine biosynthesis enzymes in the conversion of the PC-Cd complex to the PC-Cd-sulfide complex in the fission yeast raises an intriguing possibility that these same enzymes might have a role in sulfur metabolism in the fission yeast S. pombe, and perhaps in other biological systems.","authors":"Speiser DM, Ortiz DF, Kreppel L, Scheel G, McDonald G, Ow DW","authors_abbrev":"Speiser DM et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"23b994e637b6f0cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-26 12:43:17","canto_approved_date":"2023-01-12 21:15:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-03 13:31:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13","SPAC144.03","SPBC14F5.09c","SPBC409.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-03-26"},{"uniquename":"PMID:25778919","title":"Aurora B prevents chromosome arm separation defects by promoting telomere dispersion and disjunction.","citation":"J Cell Biol 2015 Mar 16;208(6):713-27","abstract":"The segregation of centromeres and telomeres at mitosis is coordinated at multiple levels to prevent the formation of aneuploid cells, a phenotype frequently observed in cancer. Mitotic instability arises from chromosome segregation defects, giving rise to chromatin bridges at anaphase. Most of these defects are corrected before anaphase onset by a mechanism involving Aurora B kinase, a key regulator of mitosis in a wide range of organisms. Here, we describe a new role for Aurora B in telomere dispersion and disjunction during fission yeast mitosis. Telomere dispersion initiates in metaphase, whereas disjunction takes place in anaphase. Dispersion is promoted by the dissociation of Swi6/HP1 and cohesin Rad21 from telomeres, whereas disjunction occurs at anaphase after the phosphorylation of condensin subunit Cnd2. Strikingly, we demonstrate that deletion of Ccq1, a telomeric shelterin component, rescued cell death after Aurora inhibition by promoting the loading of condensin on chromosome arms. Our findings reveal an essential role for telomeres in chromosome arm segregation.","doi":"10.1083/jcb.201407016","authors":"Reyes C, Serrurier C, Gauthier T, Gachet Y, Tournier S","authors_abbrev":"Reyes C et al.","pubmed_publication_date":"16 Mar 2015","pubmed_entrez_date":"2015-03-18","publication_year":"2015","canto_session_key":"fdc3419730dab35f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sylvie Tournier","canto_first_approved_date":"2017-11-14 17:09:42","canto_approved_date":"2017-11-19 15:13:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-20 08:57:04","canto_added_date":"2015-03-19 01:15:36","annotation_curators":[{"name":"Sylvie Tournier","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPCC338.17c","SPCC306.03c","SPCC188.07","SPCC320.13c","SPAC11E3.03","SPBC1778.02"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-11-14"},{"uniquename":"EMBL:AU009658","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7498766","title":"The role of cdc2 and other genes in meiosis in Schizosaccharomyces pombe.","citation":"Genetics 1995 Aug;140(4):1235-45","abstract":"The requirement of the cdc2, cdc13 and cdc25 genes for meiosis in Schizosaccharomyces pombe was investigated using three different conditions to induce meiosis. These genes were known to be required for meiosis II. cdc13 and cdc25 are essential for meiosis I. The cdc2 gene, which is required for the initiation of both mitotic S-phase and M-phase, is essential for premeiotic DNA synthesis and meiosis II. The requirement of cdc2 for meiosis I was unclear. This contrasts with Saccharomyces cerevisiae, where CDC28, the homolog of cdc2, is required for meiosis I but not for premeiotic DNA synthesis. Expression of cdc13 and cdc25 was induced after premeiotic DNA synthesis, reaching a sharp peak before the first nuclear division. Expression of cdc22, encoding the large subunit of ribonucleotide reductase, was also induced but the peak was before premeiotic DNA synthesis. The induction of cdc13 and cdc25 was largely dependent on DNA synthesis and the function of the mei4 gene. The mei4 gene itself was also induced in a DNA synthesis-dependent manner. The chain of gene expression activating cdc25 may be important as part of the mechanism that ensures the dependency of nuclear division on DNA replication during meiosis.","authors":"Iino Y, Hiramine Y, Yamamoto M","authors_abbrev":"Iino Y et al.","pubmed_publication_date":"Aug 1995","pubmed_entrez_date":"1995-08-01","publication_year":"1995","canto_session_key":"d676d3ce9ba0d3fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-29 18:23:15","canto_approved_date":"2019-07-11 22:31:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-03 09:12:04","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPAC24H6.05","SPBC11B10.09","SPBC582.03","SPAC3A12.14","SPBC32H8.11"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2017-04-29"},{"uniquename":"PMID:9190211","title":"Bax- and Bak-induced cell death in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1997 Feb;8(2):325-39","abstract":"The effects of the expression of the human Bcl-2 family proteins Bax, Bak, Bcl-2, and Bcl-XL were examined in the fission yeast Schizosaccharomyces pombe and compared with Bax-induced cell death in mammalian cells. Expression of the proapoptotic proteins Bax and Bak conferred a lethal phenotype in this yeast, which was strongly suppressed by coexpression of the anti-apoptotic protein Bcl-XL. Bcl-2 also partially abrogated Bax-mediated cytotoxicity in S. pombe, whereas a mutant of Bcl-2 (Gly145Ala) that fails to heterodimerize with Bax or block apoptosis in mammalian cells was inactive. However, other features distinguished Bax- and Bak-induced death in S. pombe from animal cell apoptosis. Electron microscopic analysis of S. pombe cells dying in response to Bax or Bak expression demonstrated massive cytosolic vacuolization and multifocal nuclear chromatin condensation, thus distinguishing this form of cell death from the classical morphological features of apoptosis seen in animal cells. Unlike Bax-induced apoptosis in 293 cells that led to the induction of interleukin-1 beta-converting enzyme (ICE)/CED-3-like protease activity, Bax- and Bak-induced cell death in S. pombe was accompanied neither by internucleosomal DNA fragmentation nor by activation of proteases with specificities similar to the ICE/CED-3 family. In addition, the baculovirus protease inhibitor p35, which is a potent inhibitor of ICE/CED-3 family proteases and a blocker of apoptosis in animal cells, failed to prevent cell death induction by Bax or Bak in fission yeast, whereas p35 inhibited Bax-induced cell death in mammalian cells. Taken together, these findings suggest that Bcl-2 family proteins may retain an evolutionarily conserved ability to regulate cell survival and death but also indicate differences in the downstream events that are activated by overexpression of Bax or Bak in divergent cell types.","authors":"Jürgensmeier JM, Krajewski S, Armstrong RC, Wilson GM, Oltersdorf T, Fritz LC, Reed JC, Ottilie S","authors_abbrev":"Jürgensmeier JM et al.","pubmed_publication_date":"Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16691419","title":"Regulation of gene expression and cell division by Polo-like kinases.","citation":"Curr Genet 2006 Aug;50(2):73-80","abstract":"Much scientific research has focused on characterising regulatory pathways and mechanisms responsible for cell integrity, growth and division. This area of study is of direct relevance to human medicine as uncontrolled growth and division underlies many diseases, most strikingly cancer. In cancer cells, normal regulatory mechanisms for growth and division are often altered, or even fail to exist. This review summarises the mechanisms that control the genes and gene products regulating cytokinesis and cell separation in the fission yeast Schizosaccharomyces pombe, as well as highlighting conserved aspects in the budding yeast Saccharomyces cerevisiae and higher eukaryotes. Particular emphasis is put on the role of gene expression, the Polo-like kinases (Plks), and the signal transduction pathways that control these processes.","authors":"Ng SS, Papadopoulou K, McInerny CJ","authors_abbrev":"Ng SS et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-05-13","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18222117","title":"RAC protein induces enzymatic access to the maturing 3'-end of the 25S rRNA in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2008 Apr 04;368(2):374-8","abstract":"In Schizosaccharomyces pombe, interdependency between steps in the processing of the rRNAs is mediated by a large protein complex (RAC) which interacts with the non-conserved transcribed spacers. The RAC complex exhibits no nuclease activity but dramatically alters the efficiency and specificity of Pac1 nuclease cleavage, leading to the removal of the 3' external transcribed spacers (3'ETS) in the maturation of the 3'ETS region. In this study modification exclusion and S1 nuclease were used to probe the RAC protein binding site and any subsequent structural changes in the maturing region. The results indicate that, as previously observed with the ITS1 and ITS2 regions, the upper helical region in the highly conserved extended terminal hairpin constitutes a protein binding site. In turn, this interaction induces a conformational change which affords access to nuclease at the 3'-end of the maturing 25S rRNA sequence.","doi":"10.1016/j.bbrc.2008.01.068","authors":"Spasov K, Nazar RN","authors_abbrev":"Spasov K et al.","pubmed_publication_date":"04 Apr 2008","pubmed_entrez_date":"2008-01-29","publication_year":"2008","canto_session_key":"77a9e27dab9bf08e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-02-22 10:30:54","canto_approved_date":"2024-02-22 10:30:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-22 10:30:43","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6B12.15"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2024-02-22"},{"uniquename":"PMID:20890290","title":"Structure of the Dom34-Hbs1 complex and implications for no-go decay.","citation":"Nat Struct Mol Biol 2010 Oct;17(10):1233-40","abstract":"No-go decay (NGD) targets mRNAs with stalls in translation elongation for endonucleolytic cleavage in a process involving the Dom34 and Hbs1 proteins. The crystal structure of a Schizosaccharomyces pombe Dom34-Hbs1 complex reveals an overall shape similar to that of eRF1-eRF3-GTP and EF-Tu-tRNA-GDPNP. Similarly to eRF1 and GTP binding to eRF3, Dom34 and GTP bind to Hbs1 with strong cooperativity, and Dom34 acts as a GTP-dissociation inhibitor (GDI). A marked conformational change in Dom34 occurs upon binding to Hbs1, leading Dom34 to resemble a portion of a tRNA and to position a conserved basic region in a position expected to be near the peptidyl transferase center. These results support the idea that the Dom34-Hbs1 complex functions to terminate translation and thereby commit mRNAs to NGD. Consistent with this role, NGD at runs of arginine codons, which cause a strong block to elongation, is independent of the Dom34-Hbs1 complex.","doi":"10.1038/nsmb.1922","authors":"Chen L, Muhlrad D, Hauryliuk V, Cheng Z, Lim MK, Shyp V, Parker R, Song H","authors_abbrev":"Chen L et al.","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2010-10-05","publication_year":"2010","canto_session_key":"4a2c0c67da8496f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-30 13:41:13","canto_approved_date":"2021-10-28 13:53:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-30 13:41:05","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25B2.01","SPCC18B5.06","SPCC584.04","SPAC1834.01"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-10-30","pdb_entries":[{"pdb_id":"3mca","gene_chains":[{"gene_uniquename":"SPBC25B2.01","chain":"A","position":"1-592"},{"gene_uniquename":"SPCC18B5.06","chain":"B","position":"1-390"}],"title":"Structure of the Dom34-Hbs1 Complex and implications for its role in No-Go decay","entry_authors":"Chen L,Song H","entry_authors_abbrev":"Chen L et al.","reference_uniquename":"PMID:20890290","experimental_method":"X-ray","resolution":"2.74"}]},{"uniquename":"PMID:34807377","title":"Sequence, structural and functional conservation among the human and fission yeast ELL and EAF transcription elongation factors.","citation":"Mol Biol Rep 2022 Feb;49(2):1303-1320","abstract":"Transcription elongation is a dynamic and tightly regulated step of gene expression in eukaryotic cells. Eleven nineteen Lysine rich Leukemia (ELL) and ELL Associated Factors (EAF) family of conserved proteins are required for efficient RNA polymerase II-mediated transcription elongation. Orthologs of these proteins have been identified in different organisms, including fission yeast and humans.\nCollectively, our work adds ELL-EAF to the increasing list of human-yeast complementation gene pairs, wherein the simpler fission yeast can be used to further enhance our understanding of the role of these proteins in transcription elongation and human disease.","doi":"10.1007/s11033-021-06958-x","authors":"Sweta K, Dabas P, Sharma N","authors_abbrev":"Sweta K et al.","pubmed_publication_date":"Feb 2022","pubmed_entrez_date":"2021-11-22","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-11-24 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24239120","title":"Antagonistic spindle motors and MAPs regulate metaphase spindle length and chromosome segregation.","citation":"Curr Biol 2013 Dec 02;23(23):2423-9","abstract":"Metaphase describes a phase of mitosis where chromosomes are attached and oriented on the bipolar spindle for subsequent segregation at anaphase. In diverse cell types, the metaphase spindle is maintained at characteristic constant length [1-3]. Metaphase spindle length is proposed to be regulated by a balance of pushing and pulling forces generated by distinct sets of spindle microtubules (MTs) and their interactions with motors and MT-associated proteins (MAPs). Spindle length is further proposed to be important for chromosome segregation fidelity, as cells with shorter- or longer-than-normal metaphase spindles, generated through deletion or inhibition of individual mitotic motors or MAPs, showed chromosome segregation defects. To test the force-balance model of spindle length control and its effect on chromosome segregation, we applied fast microfluidic temperature control with live-cell imaging to monitor the effect of deleting or switching off different combinations of antagonistic force contributors in the fission yeast metaphase spindle. We show that the spindle midzone proteins kinesin-5 cut7p and MT bundler ase1p contribute to outward-pushing forces and that the spindle kinetochore proteins kinesin-8 klp5/6p and dam1p contribute to inward-pulling forces. Removing these proteins individually led to aberrant metaphase spindle length and chromosome segregation defects. Removing these proteins in antagonistic combination rescued the defective spindle length and in some combinations also partially rescued chromosome segregation defects.","doi":"10.1016/j.cub.2013.10.023","authors":"Syrovatkina V, Fu C, Tran PT","authors_abbrev":"Syrovatkina V et al.","pubmed_publication_date":"02 Dec 2013","pubmed_entrez_date":"2013-11-19","publication_year":"2013","canto_session_key":"49604a894be35067","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-05-30 17:41:31","canto_approved_date":"2022-11-07 17:08:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-05-30 17:40:51","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":41,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.13","SPAC589.08c","SPAC664.10","SPBC1685.15c","SPBC15D4.01c","SPAC1093.06c","SPBC1604.20c","SPAC3A11.14c","SPAC25G10.07c","SPBC20F10.06","SPAC144.14","SPAC1834.07","SPAPB1A10.09"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2022-05-30"},{"uniquename":"PMID:34006635","title":"Structural basis for p50RhoGAP BCH domain-mediated regulation of Rho inactivation.","citation":"Proc Natl Acad Sci U S A 2021 May 25;118(21)","abstract":"Spatiotemporal regulation of signaling cascades is crucial for various biological pathways, under the control of a range of scaffolding proteins. The BNIP-2 and Cdc42GAP Homology (BCH) domain is a highly conserved module that targets small GTPases and their regulators. Proteins bearing BCH domains are key for driving cell elongation, retraction, membrane protrusion, and other aspects of active morphogenesis during cell migration, myoblast differentiation, and neuritogenesis. We previously showed that the BCH domain of p50RhoGAP (ARHGAP1) sequesters RhoA from inactivation by its adjacent GAP domain; however, the underlying molecular mechanism for RhoA inactivation by p50RhoGAP remains unknown. Here, we report the crystal structure of the BCH domain of p50RhoGAP  Schizosaccharomyces pombe  and model the human p50RhoGAP BCH domain to understand its regulatory function using in vitro and cell line studies. We show that the BCH domain adopts an intertwined dimeric structure with asymmetric monomers and harbors a unique RhoA-binding loop and a lipid-binding pocket that anchors prenylated RhoA. Interestingly, the β5-strand of the BCH domain is involved in an intermolecular β-sheet, which is crucial for inhibition of the adjacent GAP domain. A destabilizing mutation in the β5-strand triggers the release of the GAP domain from autoinhibition. This renders p50RhoGAP active, thereby leading to RhoA inactivation and increased self-association of p50RhoGAP molecules via their BCH domains. Our results offer key insight into the concerted spatiotemporal regulation of Rho activity by BCH domain-containing proteins.","doi":"10.1073/pnas.2014242118","authors":"Chichili VPR, Chew TW, Shankar S, Er SY, Chin CF, Jobichen C, Qiurong Pan C, Zhou Y, Yeong FM, Low BC, Sivaraman J","authors_abbrev":"Chichili VPR et al.","pubmed_publication_date":"25 May 2021","pubmed_entrez_date":"2021-05-19","publication_year":"2021","canto_session_key":"13705ccccd43f5ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-09-05 16:54:33","canto_approved_date":"2022-02-02 16:15:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-05 16:54:27","canto_added_date":"2021-05-21 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1565.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-09-05"},{"uniquename":"EMBL:AU012150","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21528444","title":"Chromatin immunoprecipitation in fission yeast.","citation":"Methods Mol Biol 2011;725:15-28","abstract":"A tremendous amount of information regarding the nature and regulation of heterochromatin has emerged in the past 10 years. This rapid progress is largely due to the development of techniques such as chromatin immunoprecipitation or \"ChIP,\" which allow analysis of chromatin structure. Further technological advances such as microarray analysis and, more recently, deep sequencing technologies, have made ChIP an even more powerful tool. ChIP allows the investigator to identify protein interactions and/or the presence of various chromatin modifications at specific genomic loci.","doi":"10.1007/978-1-61779-046-1_2","authors":"Volpe TA, Demaio J","authors_abbrev":"Volpe TA et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-04-30","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20705238","title":"Homologous recombination restarts blocked replication forks at the expense of genome rearrangements by template exchange.","citation":"Mol Cell 2010 Aug 13;39(3):346-59","abstract":"Template switching induced by stalled replication forks has recently been proposed to underlie complex genomic rearrangements. However, the resulting models are not supported by robust physical evidence. Here, we analyzed replication and recombination intermediates in a well-defined fission yeast system that blocks replication forks. We show that, in response to fork arrest, chromosomal rearrangements result from Rad52-dependent nascent strand template exchange occurring during fork restart. This template exchange occurs by both Rad51-dependent and -independent mechanisms. We demonstrate that Rqh1, the BLM homolog, limits Rad51-dependent template exchange without affecting fork restart. In contrast, we report that the Srs2 helicase promotes both fork restart and template exchange. Our data demonstrate that template exchange occurs during recombination-dependent fork restart at the expense of genome rearrangements.","doi":"10.1016/j.molcel.2010.07.015","authors":"Lambert S, Mizuno K, Blaisonneau J, Martineau S, Chanet R, Fréon K, Murray JM, Carr AM, Baldacci G","authors_abbrev":"Lambert S et al.","pubmed_publication_date":"13 Aug 2010","pubmed_entrez_date":"2010-08-14","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC2G11.12","SPAC30D11.10"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11921100","title":"The mei3 region of the Schizosaccharomyces pombe genome.","citation":"Yeast 2002 Apr;19(6):521-7","abstract":"Expression of the mei3 gene is sufficient to induce meiosis in the fission yeast Schizosaccharomyces pombe. The mei3 gene is located 0.64 Mb from the telomere of the left arm of Sz. pombe chromosome II. We have sequenced and analysed 107 kb of DNA from the mei3 genomic region. The sequence includes 14 known genes (bag1-B, csh3, dps1, gpt1, mei3, mfm3, pac1, prp31, rpl38-1, rpn3, rti1, spa1, spm1 and ubc4) and 26 other open reading frames (ORFs) longer than 100 codons: a density of one protein-coding gene per 2.7 kb. Twenty-one of the 40 ORFs (53%) have introns. In addition there is one lone Tf1 transposon long terminal repeat (LTR), tRNA(Trp) and tRNA(Ser) genes and a 5S rRNA gene. 14 of the novel ORFs show sequence similarities which suggest functions of their products, including a coatomer alpha-subunit, a catechol O-methyltransferase, protein kinase, asparagine synthetase, zinc metalloprotease, acetyltransferase, phosphatidylinositol 4-kinase, inositol polyphosphate phosphatase, GTPase-activating protein, permease, pre-mRNA splicing factor, 20S proteasome component and a thioredoxin-like protein. One predicted protein has similarity to the human Cockayne syndrome protein CSA and one with human GTPase XPA binding protein XAB1. Three ORFs are likely to code for proteins because they have sequence similarity with hypothetical proteins, three encode predicted coiled-coil proteins and four are sequence orphans.","authors":"Aves SJ, Hunt C, Xiang Z, Lyne MH, Wood V, Rajandream MA, Skelton J, Churcher CM, Warren T, Harris D, Gwilliam R, Barrell BG","authors_abbrev":"Aves SJ et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-03-29","publication_year":"2002","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9786952","title":"imp2, a new component of the actin ring in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Biol 1998 Oct 19;143(2):415-27","abstract":"Cytokinesis is the part of the cell cycle in which the cell is cleaved to form two daughter cells. The unicellular yeast, Schizosaccharomyces pombe is an excellent model organism in which to study cell division, since it shows the general features of eukaryotic cell division and is amenable to genetic analysis. In this manuscript we describe the isolation and characterization of a new protein, imp2, which is required for normal septation in fission yeast. imp2, which colocalizes with the medial ring during septation, is structurally similar to a group of proteins including the S. pombe cdc15 and the mouse PSTPIP that are localized to, and thought to be involved in actin ring organization. Cells in which the imp2 gene is deleted or overexpressed have septation and cell separation defects. An analysis of the actin cytoskeleton shows the lack of a medial ring in septating cells that overexpress imp2, and the appearance of abnormal medial ring structures in septated cells that lack imp2. These observations suggest that imp2 destabilizes the medial ring during septation. imp2 also shows genetic interactions with several, previously characterized septation genes, strengthening the conclusion that it plays a role in normal fission yeast septation.","authors":"Demeter J, Sazer S","authors_abbrev":"Demeter J et al.","pubmed_publication_date":"19 Oct 1998","pubmed_entrez_date":"1998-10-24","publication_year":"1998","canto_session_key":"500e6c06108b2c75","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-06 20:56:24","canto_approved_date":"2024-01-19 15:12:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-03 12:37:20","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.02","SPAP8A3.08","SPAC20G8.05c","SPCC1739.11c","SPAC27F1.02c","SPBC557.03c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2019-01-06"},{"uniquename":"PMID:10639364","title":"Discovery of novel antifungal (1,3)-beta-D-glucan synthase inhibitors.","citation":"Antimicrob Agents Chemother 2000 Feb;44(2):368-77","abstract":"The increasing incidence of life-threatening fungal infections has driven the search for new, broad-spectrum fungicidal agents that can be used for treatment and prophylaxis in immunocompromised patients. Natural-product inhibitors of cell wall (1,3)-beta-D-glucan synthase such as lipopeptide pneumocandins and echinocandins as well as the glycolipid papulacandins have been evaluated as potential therapeutics for the last two decades. As a result, MK-0991 (caspofungin acetate; Cancidas), a semisynthetic analogue of pneumocandin B(o), is being developed as a broad-spectrum parenteral agent for the treatment of aspergillosis and candidiasis. This and other lipopeptide antifungal agents have limited oral bioavailability. Thus, we have sought new chemical structures with the mode of action of lipopeptide antifungal agents but with the potential for oral absorption. Results of natural-product screening by a series of newly developed methods has led to the identification of four acidic terpenoid (1,3)-beta-D-glucan synthase inhibitors. Of the four compounds, the in vitro antifungal activity of one, enfumafungin, is comparable to that of L-733560, a close analogue of MK-0991. Like the lipopeptides, enfumafungin specifically inhibits glucan synthesis in whole cells and in (1,3)-beta-D-glucan synthase assays, alters the morphologies of yeasts and molds, and produces a unique response in Saccharomyces cerevisiae strains with point mutations in FKS1, the gene which encodes the large subunit of glucan synthase.","authors":"Onishi J, Meinz M, Thompson J, Curotto J, Dreikorn S, Rosenbach M, Douglas C, Abruzzo G, Flattery A, Kong L, Cabello A, Vicente F, Pelaez F, Diez MT, Martin I, Bills G, Giacobbe R, Dombrowski A, Schwartz R, Morris S, Harris G, Tsipouras A, Wilson K, Kurtz MB","authors_abbrev":"Onishi J et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-01-20","publication_year":"2000","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18282134","title":"Noncoding RNAs and chromatin structure.","citation":"Biochemistry (Mosc) 2007 Dec;72(13):1422-38","abstract":"A number of examples of noncoding RNA-connected chromatin modifications in eukaryotes has been recently revealed. Four cases are under detailed consideration in the present review, namely Xist RNA-dependent X-chromosome inactivation in mammals, roX RNA-dependent hyperactivation of X-chromosome in the fruit fly (in both cases the goal is dosage compensation, equalization of transcription level from two X chromosomes in females and one in males), and two examples of RNAi-connected down-regulation of transcription--siRNA-dependent heterochromatin formation in fission yeast and RdDM (RNA-dependent DNA methylation) in plants (FWA gene regulation in Arabidopsis). Although overall quite different, each phenomenon demonstrates some common features of RNA-driven chromatin modification process, including the role of RNA in aiming of chromatin-modifying protein complexes to their targets and subsequent formation of self-maintaining specific chromatin conformation (DNA methylation, changes in histone code, and binding of self-assembling protein complexes).","authors":"Lavrov SA, Kibanov MV","authors_abbrev":"Lavrov SA et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2008-02-20","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21870280","title":"Studying G2 DNA damage checkpoints using the fission yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2011;782:1-12","abstract":"Using synchronized cells, one can directly measure delay in mitosis brought about by the G2 DNA damage checkpoint in response to exposure to exogenous DNA damaging agents. Scoring mitosis in the fission yeast Schizosaccharomyces pombe is relatively simple. Many techniques exist for synchronizing cells for such assays. We present a detailed explanation of the setup and use of centrifugal elutriation to synchronize cells in G2, exposure of cells to DNA damage, and measurement of mitotic progression and delay.","doi":"10.1007/978-1-61779-273-1_1","authors":"Willis N, Rhind N","authors_abbrev":"Willis N et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-08-27","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007140","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011140","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22456505","title":"A conserved cell growth cycle can account for the environmental stress responses of divergent eukaryotes.","citation":"Mol Biol Cell 2012 May;23(10):1986-97","abstract":"The respiratory metabolic cycle in budding yeast (Saccharomyces cerevisiae) consists of two phases that are most simply defined phenomenologically: low oxygen consumption (LOC) and high oxygen consumption (HOC). Each phase is associated with the periodic expression of thousands of genes, producing oscillating patterns of gene expression found in synchronized cultures and in single cells of slowly growing unsynchronized cultures. Systematic variation in the durations of the HOC and LOC phases can account quantitatively for well-studied transcriptional responses to growth rate differences. Here we show that a similar mechanism-transitions from the HOC phase to the LOC phase-can account for much of the common environmental stress response (ESR) and for the cross-protection by a preliminary heat stress (or slow growth rate) to subsequent lethal heat stress. Similar to the budding yeast metabolic cycle, we suggest that a metabolic cycle, coupled in a similar way to the ESR, in the distantly related fission yeast, Schizosaccharomyces pombe, and in humans can explain gene expression and respiratory patterns observed in these eukaryotes. Although metabolic cycling is associated with the G0/G1 phase of the cell division cycle of slowly growing budding yeast, transcriptional cycling was detected in the G2 phase of the division cycle in fission yeast, consistent with the idea that respiratory metabolic cycling occurs during the phases of the cell division cycle associated with mass accumulation in these divergent eukaryotes.","doi":"10.1091/mbc.E11-11-0961","authors":"Slavov N, Airoldi EM, van Oudenaarden A, Botstein D","authors_abbrev":"Slavov N et al.","pubmed_publication_date":"May 2012","pubmed_entrez_date":"2012-03-30","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:13369173","title":"[Remote hybridization of yeasts. I. Production of hybrids of Saccharomyces cerevisiae (XI strain) and Schizosaccharomyces pombe].","citation":"Mikrobiologiia 1956;25(3):275-8","abstract":"","authors":"KOSIKOV KV","authors_abbrev":"KOSIKOV KV","pubmed_publication_date":"1956","pubmed_entrez_date":"1956-05-01","publication_year":"1956","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11434772","title":"Structural role of the proline residues of the beta-hinge region of p13suc1 as revealed by site-directed mutagenesis and fluorescence studies.","citation":"Biochemistry 2001 Jul 10;40(27):8030-42","abstract":"Site-directed mutagenesis, gel filtration, and fluorescence spectroscopy approaches were used to study the molecular hinge mechanism involved in the beta-strand-exchanged dimer formation of the cyclin-dependent protein kinase regulatory subunit p13(suc1) from Schizosaccharomyces pombe. Single and double mutants of residues Pro-90 and Pro-92 (P90V, P92V, and P90V/P92V) were prepared and assayed. Substitution of Pro-90 prevented dimer formation by arm exchange. However, single point mutations did not affect the two-state unfolding transition of wild-type p13(suc1) at equilibrium (i.e., wild type, DeltaG degrees (0,un) = 7.38 +/- 0.35 kcal mol(-1), vs P90V, DeltaG degrees (0,un) = 6.71 +/- 0.18 kcal mol(-1)). On the contrary, the double mutant unfolded with a complex transition, and the reaction was best described by a three-state model (N <==> I <==> U). Resolution of the state-dependent (native vs denatured) intrinsic fluorescence decay amplitudes of p13(suc1) showed that with P90V/P92V these parameters were affected at [GuHCl] significantly less than with wild-type and single mutant proteins. Moreover, with the latter products, fluorescence quenching measurements at 1 M GuHCl revealed linear Stern-Volmer plots with quenching constants typical of tryptophan residues located in a native environment (1.6 M(-1) < K(SV) < 2.3 M(-1)). Dissimilarly, with P90V/P92V a significant deviation from linearity of the Stern-Volmer plot was obtained. Nonlinear least-squares analysis of these data resolved the significant contribution of highly solvent-accessible emitting species (K(SV) = 26 M(-1)) consistent with large exposure of the tryptophan residues. These results are compatible with the existence of an intermediate unfolding state of the double mutation product. Thus, while single residue substitution studies give support to the primary role of Pro-90 in the p13(suc1) dimer formation by domain swapping, double residue substitution studies indicate the important role of the conserved repeat, Pro-x-Pro, for the proper beta-strand spatial organization and stability.","authors":"Simeoni F, Masotti L, Neyroz P","authors_abbrev":"Simeoni F et al.","pubmed_publication_date":"10 Jul 2001","pubmed_entrez_date":"2001-07-04","publication_year":"2001","canto_session_key":"c5c64d3a46e78632","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-15 22:43:55","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-15 22:43:46","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-15"},{"uniquename":"EMBL:AU013698","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22876198","title":"CDK9 and H2B monoubiquitination: a well-choreographed dance.","citation":"PLoS Genet 2012;8(8):e1002860","abstract":"","doi":"10.1371/journal.pgen.1002860","authors":"Johnsen SA","authors_abbrev":"Johnsen SA","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-10","publication_year":"2012","canto_session_key":"81ebe48c1a65bff0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-11-11 15:48:02","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-11 15:47:55","canto_added_date":"2015-11-11 15:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-11-11"},{"uniquename":"PMID:9857181","title":"Analysis of Rad3 and Chk1 protein kinases defines different checkpoint responses.","citation":"EMBO J 1998 Dec 15;17(24):7239-49","abstract":"Eukaryotic cells respond to DNA damage and S phase replication blocks by arresting cell-cycle progression through the DNA structure checkpoint pathways. In Schizosaccharomyces pombe, the Chk1 kinase is essential for mitotic arrest and is phosphorylated after DNA damage. During S phase, the Cds1 kinase is activated in response to DNA damage and DNA replication blocks. The response of both Chk1 and Cds1 requires the six 'checkpoint Rad' proteins (Rad1, Rad3, Rad9, Rad17, Rad26 and Hus1). We demonstrate that DNA damage-dependent phosphorylation of Chk1 is also cell-cycle specific, occurring primarily in late S phase and G2, but not during M/G1 or early S phase. We have also isolated and characterized a temperature-sensitive allele of rad3. Rad3 functions differently depending on which checkpoint pathway is activated. Following DNA damage, rad3 is required to initiate but not maintain the Chk1 response. When DNA replication is inhibited, rad3 is required for both initiation and maintenance of the Cds1 response. We have identified a strong genetic interaction between rad3 and cds1, and biochemical evidence shows a physical interaction is possible between Rad3 and Cds1, and between Rad3 and Chk1 in vitro. Together, our results highlight the cell-cycle specificity of the DNA structure-dependent checkpoint response and identify distinct roles for Rad3 in the different checkpoint responses.\nATM/ATR/cell-cycle checkpoints/Chk1/Rad3","authors":"Martinho RG, Lindsay HD, Flaggs G, DeMaggio AJ, Hoekstra MF, Carr AM, Bentley NJ","authors_abbrev":"Martinho RG et al.","pubmed_publication_date":"15 Dec 1998","pubmed_entrez_date":"1998-12-19","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPCC18B5.11c","SPBC216.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:12914947","title":"In Schizosaccharomyces pombe chs2p has no chitin synthase activity but is related to septum formation.","citation":"FEBS Lett 2003 Aug 14;549(1-3):176-80","abstract":"Chitin synthesis occurs in most fungi through the action of different chitin synthase (CS) isoenzymes. In Schizosaccharomyces pombe the chs2(+) gene codes for a protein with significant similarity to CS enzymes, but lacking most of the residues considered to be essential for activity, including the QRRRW domain. Here we show that chs2p is a functional protein that localises to the growing edge of the septum but is not a CS enzyme. Strong over-expression is lethal, while moderate expression leads to a severe defect in septum formation. These results suggest that chs2p has remained through evolution to play an alternative role in septation.","authors":"Martín-García R, Durán A, Valdivieso MH","authors_abbrev":"Martín-García R et al.","pubmed_publication_date":"14 Aug 2003","pubmed_entrez_date":"2003-08-14","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1709.01"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:16188891","title":"The integrase of the long terminal repeat-retrotransposon tf1 has a chromodomain that modulates integrase activities.","citation":"J Biol Chem 2005 Nov 25;280(47):39086-94","abstract":"Chromodomains in a variety of proteins mediate the formation of heterochromatin by interacting directly with histone H3, DNA, or RNA. A diverse family of long terminal repeat (LTR)-retrotransposons possesses chromodomains in their integrases (IN), suggesting that the chromodomains may control integration. The LTR-retrotransposon Tf1 of Schizosaccharomyces pombe is highly active and possesses a chromodomain in the COOH terminus of its IN. To test this chromodomain for a role in integration, recombinant INs with and without the chromodomain were assayed for activity in in vitro reactions. The full-length IN had integration activity with oligonucleotide substrates that modeled both the insertion reaction and a reverse reaction known as disintegration. The INs of retroviruses possess an additional activity termed 3' processing that must remove 2-3 nucleotides from the 3' ends of the viral cDNA before insertion can occur. These additional nucleotides are added during reverse transcription because of the position of the minus strand primer downstream of the LTR. The position of the primer for Tf1 suggests no nucleotides are added 3' of the LTR. It was therefore surprising that Tf1 IN was capable of 3' cleavage. The most unexpected result reported here was that the IN lacking the chromodomain had significantly higher activity and substantially reduced substrate specificity. These results reveal that both the activity and specificity of enzymes can be modulated by their chromodomains.","authors":"Hizi A, Levin HL","authors_abbrev":"Hizi A et al.","pubmed_publication_date":"25 Nov 2005","pubmed_entrez_date":"2005-09-29","publication_year":"2005","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26781994","title":"Molecular Combing of Single DNA Molecules on the 10 Megabase Scale.","citation":"Sci Rep 2016 Jan 19;6:19636","abstract":"DNA combing allows the investigation of DNA replication on genomic single DNA molecules, but the lengths that can be analysed have been restricted to molecules of 200-500 kb. We have improved the DNA combing procedure so that DNA molecules can be analysed up to the length of entire chromosomes in fission yeast and up to 12 Mb fragments in human cells. Combing multi-Mb-scale DNA molecules revealed previously undetected origin clusters in fission yeast and shows that in human cells replication origins fire stochastically forming clusters of fired origins with an average size of 370 kb. We estimate that a single human cell forms around 3200 clusters at mid S-phase and fires approximately 100,000 origins to complete genome duplication. The procedure presented here will be adaptable to other organisms and experimental conditions.","doi":"10.1038/srep19636","authors":"Kaykov A, Taillefumier T, Bensimon A, Nurse P","authors_abbrev":"Kaykov A et al.","pubmed_publication_date":"19 Jan 2016","pubmed_entrez_date":"2016-01-20","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17715303","title":"Protection of telomeres by a conserved Stn1-Ten1 complex.","citation":"Proc Natl Acad Sci U S A 2007 Aug 28;104(35):14038-43","abstract":"Telomeres are specialized chromatin structures that protect chromosome ends. Critical among telomere proteins are those that bind the telomeric single-strand DNA (ssDNA) overhangs. These proteins are thought to differ among eukaryotes. Three interacting proteins (Cdc13, Stn1, and Ten1) associate with the telomeric overhang in budding yeast, a single protein known as Pot1 (protection of telomeres-1) performs this function in fission yeast, and a two-subunit complex consisting of POT1 and TPP1 associates with telomeric ssDNA in humans. Cdc13 and Pot1 have related oligonucleotide/oligosaccharide-binding fold (OB-fold) domains that bind the telomeric ssDNA overhang. Here we show that Schizosaccharomyces pombe has Stn1- and Ten1-like proteins that are essential for chromosome end protection. Stn1 orthologs exist in all species that have Pot1, whereas Ten1-like proteins can be found in all fungi. Fission yeast Stn1 and Ten1 localize at telomeres in a manner that correlates with the length of the ssDNA overhang, suggesting that they specifically associate with the telomeric ssDNA. Unlike in budding yeast, in which Cdc13, Stn1, and Ten1 all interact, fission yeast Stn1 and Ten1 associate with each other, but not with Pot1. Our findings suggest that two separate protein complexes are required for chromosome end protection in fission yeast. Structural profiling studies detect OB-fold domains in Stn1 and Ten1 orthologs, indicating that protection of telomeres by multiple proteins with OB-fold domains is conserved in eukaryotic evolution.","authors":"Martín V, Du LL, Rozenzhak S, Russell P","authors_abbrev":"Martín V et al.","pubmed_publication_date":"28 Aug 2007","pubmed_entrez_date":"2007-08-24","publication_year":"2007","canto_session_key":"eaf6b9ac550f1443","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-08 19:29:37","canto_approved_date":"2020-04-02 11:37:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-08 19:29:29","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26H5.06","SPCC126.02c","SPBC216.05","SPBC409.12c","SPCC1393.14"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2015-12-08"},{"uniquename":"PMID:36370267","title":"SILAC-Based Proteomic Analysis of Meiosis in the Fission Yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2023;2603:19-29","abstract":"Stable isotope labeling by amino acids in cell culture (SILAC) provides a powerful tool to quantify proteins and posttranslational modifications. Here we describe how to apply SILAC for protein identification and quantification in synchronous meiotic cultures induced by inactivation of the Pat1 kinase in the fission yeast Schizosaccharomyces pombe.","doi":"10.1007/978-1-0716-2863-8_2","authors":"Anrather D, Polakova SB, Cipak L, Gregan J","authors_abbrev":"Anrather D et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2022-11-12","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-11-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18345014","title":"Roles of the Clr4 methyltransferase complex in nucleation, spreading and maintenance of heterochromatin.","citation":"Nat Struct Mol Biol 2008 Apr;15(4):381-8","abstract":"Heterochromatin assembly, involving methylation of histone H3 lysine 9 (H3K9me), regulates various chromosomal processes. In fission yeast, heterochromatin targeted to specific repeat loci in an RNAi-dependent manner spreads across extended domains to exert regional epigenetic control. The Clr4 methyltransferase complex (ClrC) is responsible for nucleation and spreading of heterochromatin; however, its recruitment to heterochromatic repeats is poorly understood. Here we demonstrate that ClrC components are distributed throughout heterochromatic domains. To nucleate heterochromatin, Rik1, a WD domain-containing subunit of ClrC, is loaded onto the transcribed repeats via RNAi machinery including the RNA-induced transcriptional silencing (RITS) complex. Furthermore, we show that the chromodomain of Clr4 binds specifically to H3K9me that is essential for the spreading of heterochromatin. Our analyses delineate sequential steps for the assembly of heterochromatic domains and suggest that the ability of Clr4 to both 'write' and 'read' H3K9me facilitates heterochromatin maintenance through successive cell divisions.","doi":"10.1038/nsmb.1406","authors":"Zhang K, Mosch K, Fischle W, Grewal SI","authors_abbrev":"Zhang K et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-03-18","publication_year":"2008","canto_session_key":"5f656dfe4953442a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-14 11:46:34","canto_approved_date":"2025-04-18 08:57:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-08-14 11:46:28","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":66,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.08","SPBC428.08c","SPAC3A11.08","SPBC800.03","SPAC1834.04","SPCC188.13c","SPAC6F12.09","SPAC664.01c","SPBC83.03c","SPBC8D2.04","SPCC613.12c","SPAC18G6.02c","SPBC1105.11c","SPCC736.11","SPCC970.07c"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2024-08-14"},{"uniquename":"PMID:35657410","title":"Loss of PPR protein Ppr2 induces ferroptosis-like cell death in Schizosaccharomyces pombe.","citation":"Arch Microbiol 2022 Jun 03;204(7):360","abstract":"Ferroptosis is a form of iron- and lipid peroxidation-mediated programmed cell death that occurs widely in mammalian cells. However, this phenomenon is rarely reported in unicellular eukaryotes. Here, we address whether ferroptosis occurs in the model unicellular eukaryote Schizosaccharomyces pombe (S. pombe). Deletion of the pentatricopeptide repeat (PPR) gene ppr2 encoding as a general mitochondrial translation factor required for mitochondrial translation disrupts iron homeostasis and induces oxidative stress, resulting in loss of cell viability. The small-molecular ferroptosis inhibitors deferoxamine (DFO) and ferrostatin-1 (Fer-1) partially rescued the ppr2 deletion-induced cell death. The amount of malondialdehyde, a lipid peroxidation marker, in Δppr2 cells was higher than that in wild type. Using C11-BODIPY 581/591, an oxidation-sensitive fluorescent lipid peroxidation probe, we showed that Δppr2 cells have a large amount of lipid peroxidation compared to wild-type cells. Deletion of ferric reductase transmembrane component 1 (frp1) encoding S. pombe ferric reductase, which is required for ferric iron uptake, partially rescued the cell death of Δppr2 cells. Our results suggest that ppr2 deletion causes an imbalance in iron homeostasis and redox, leading to ferroptosis-like cell death in S. pombe.","doi":"10.1007/s00203-022-02970-2","authors":"Liu Z, Ebrahim A, Wu X, Li M, Huang Y","authors_abbrev":"Liu Z et al.","pubmed_publication_date":"03 Jun 2022","pubmed_entrez_date":"2022-06-03","publication_year":"2022","canto_session_key":"66ec44c3d78cc17b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying  Luo","canto_first_approved_date":"2025-03-31 12:54:01","canto_approved_date":"2025-07-03 10:49:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-30 14:58:14","canto_added_date":"2022-06-08 00:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying  Luo","community_curator":true,"annotation_count":27,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.09","SPBC16E9.01c","SPAC24C9.06c","SPBC8D2.15","SPAC227.13c","SPAC1F8.03c","SPCC1020.03","SPAC1F8.02c","SPAC1F7.08","SPBC1683.09c","SPAC1F12.10c","SPAC1F7.07c","SPBC18H10.11c"],"gene_count":13,"ltp_gene_count":2,"approved_date":"2025-03-31"},{"uniquename":"PMID:1641333","title":"Phenol-treatment and a homologous pairing-assay.","citation":"Nucleic Acids Res 1992 Jul 25;20(14):3679-84","abstract":"Homologous pairing is a key step in homologous genetic recombination. In the early stage of trials for the identification of homologous pairing-promoting proteins from a fission yeast, Schizosaccharomyces pombe, we treated DNA products with phenol in the presence of a salt for the removal of tightly bound proteins from DNA before the assay, but we found that this treatment caused very efficient protein-independent double-strand formation from complementary single-stranded DNAs. Using an assay including the phenol treatment, we detected another species of apparent homologous pairing-promoting proteins in the nuclei, in addition to a homologous pairing-promoting protein consisting of three components which we reported previously. However, studies involving the use of an assay without the phenol-treatments revealed that the second one was not really a homologous pairing-protein. Thus, the protein-independent double-strand formation by phenol-treatment in the presence of a salt could cause the erroneous identification of homologous pairing-promoting proteins.","authors":"Arai N, Kawasaki K, Iwabuchi M, Shibata T","authors_abbrev":"Arai N et al.","pubmed_publication_date":"25 Jul 1992","pubmed_entrez_date":"1992-07-25","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23128140","title":"Microtubule-binding sites of the CH domain of EB1 and its autoinhibition revealed by NMR.","citation":"Biochim Biophys Acta 2013 Feb;1834(2):499-507","abstract":"End-binding protein 1 (EB1) is one of the best studied plus-end tracking proteins. It is known that EB1 specifically binds the plus ends of microtubules (MTs) and promotes MT growth. EB1 activity is thought to be autoinhibited by an intramolecular interaction. Recent cryo-EM analyses showed that the CH domain of Mal3p (Schizosaccharomyces pombe EB1 homolog) binds to GMPCPP-MT (Sandblad, L. Cell 127 (2006) 1415-24), and strongly binds GTPγS-MT which is proposed to mimic MT plus ends better than GMPCPP-MT (Maurer S.P. et al. Cell 149 (2012) 371-82). Here, we report on the MT binding sites of the CH domain of EB1 as revealed by NMR using the transferred cross-saturation method. In this study, we used GMPCPP-MT and found that the MT binding sites are very similar to the binding site for GTPγS-MT as suggested by cryo-EM (Maurer S.P. et al. Cell 149 (2012) 371-82). Notably, the N-terminal tip of helix α6 of the CH domain did not make contact with GMPCPP-MT, in contrast to the cryo-EM study which showed that it is closely located to a putative switch region of β-tubulin in GTPγS-MT (Maurer S.P. et al. Cell 149 (2012) 371-82). Further, we found that the intramolecular interaction site of EB1 overlaps the MT binding sites, indicating that the MT binding sites are masked by interaction with the C-terminal domain. We propose a structural view of autoinhibition and its release mechanism through competition binding with binding partners such as adenomatous polyposis coli protein.","doi":"10.1016/j.bbapap.2012.10.013","authors":"Kanaba T, Maesaki R, Mori T, Ito Y, Hakoshima T, Mishima M","authors_abbrev":"Kanaba T et al.","pubmed_publication_date":"Feb 2013","pubmed_entrez_date":"2012-11-07","publication_year":"2013","canto_session_key":"413cccbc0ecd978c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-04 19:44:58","canto_approved_date":"2024-01-04 19:44:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-04 19:44:18","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-01-04"},{"uniquename":"PMID:8722178","title":"Cell cycle control of eukaryotic DNA replication.","citation":"Curr Opin Genet Dev 1996 Apr;6(2):208-14","abstract":"A clearer picture of replication control is emerging through the characterization of proteins, such as cdc18/Cdc6 and members of the mini-chromosome maintenance (MCM) protein family, that are involved in the initiation step. Cyclin B dependent kinases have conserved roles in both Saccharomyces cerevisiae and Schizosaccharomyces pombe, switching on DNA replication in G1 and preventing re-replication in G2. A model is suggested where MCMs and CDKs play complementary roles to ensure 'once-per-cell-cycle' replication, with CDKs maintaining a G1 or G2 state, whereas MCMs provide a cis-acting control on chromatin to prevent reinitiation during a single S phase.","authors":"Kearsey SE, Labib K, Maiorano D","authors_abbrev":"Kearsey SE et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22002604","title":"RNAi promotes heterochromatic silencing through replication-coupled release of RNA Pol II.","citation":"Nature 2011 Oct 16;479(7371):135-8","abstract":"Heterochromatin comprises tightly compacted repetitive regions of eukaryotic chromosomes. The inheritance of heterochromatin through mitosis requires RNA interference (RNAi), which guides histone modification during the DNA replication phase of the cell cycle. Here we show that the alternating arrangement of origins of replication and non-coding RNA in pericentromeric heterochromatin results in competition between transcription and replication in Schizosaccharomyces pombe. Co-transcriptional RNAi releases RNA polymerase II (Pol II), allowing completion of DNA replication by the leading strand DNA polymerase, and associated histone modifying enzymes that spread heterochromatin with the replication fork. In the absence of RNAi, stalled forks are repaired by homologous recombination without histone modification.","doi":"10.1038/nature10501","authors":"Zaratiegui M, Castel SE, Irvine DV, Kloc A, Ren J, Li F, de Castro E, Marín L, Chang AY, Goto D, Cande WZ, Antequera F, Arcangioli B, Martienssen RA","authors_abbrev":"Zaratiegui M et al.","pubmed_publication_date":"16 Oct 2011","pubmed_entrez_date":"2011-10-18","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.13c","SPAC644.14c","SPCC736.11"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:15865206","title":"Carbon source-dependent regulation of a second gene encoding glutaredoxin from the fission yeast Schizosaccharomyces pombe.","citation":"Mol Biol Rep 2005 Mar;32(1):15-24","abstract":"Glutaredoxin (Grx), also known as thioltransferase (TTase), is an enzyme that catalyzes the reduction of a variety of disulfide compounds, including protein disulfides, in the presence of reduced glutathione. A second gene encoding Grx (Grx2) was cloned from the chromosomal DNA of the fission yeast Schizosaccharomyces pombe. The determined DNA sequence contains 1645 bp which is able to encode a polypeptide of 110 amino acids with a molecular mass of 12.2 kDa. The genomic DNA consists of 4 exons and 3 introns. The isolated gene was found to produce functional glutaredoxin that could accelerate the growth of the fission yeast, and is highly expressed at the mid- and late exponential phases. Aluminum, cadmium and hydrogen peroxide marginally enhanced the synthesis of beta-galactosidase from the Grx2-lacZ fusion gene. Shifts to lower concentrations (0.2, 0.4 or 0.8%) of D-glucose significantly enhanced the synthesis of beta-galactosidase from the Grx2-lacZ fusion gene. And shifts to sucrose (0.2, 0.4, 0.8 or 1.6%) as a sole carbon source markedly enhanced the synthesis of beta-galactosidase from the Grx2-lacZ fusion gene, the degree of which was inversely dependent on concentration. However, nonfermentable carbon sources reduced the expression of the Grx2 gene due to their growth arrest. The transcription factor Pap1 is not involved in the basal expression and induction of the Grx2 gene. The Grx2 protein was subcellularly localized in the nucleus of the yeast cells. Our results indicate that the Grx2 protein, located in the nucleus, is linked with the yeast growth, and that the gene is regulated by carbon sources.","authors":"Kim HG, Kim JH, Kim BC, Park EH, Lim CJ","authors_abbrev":"Kim HG et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-05-04","publication_year":"2005","canto_session_key":"6766f5a185d5d3cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:30:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-06 14:01:59","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC4F10.20","SPAC15E1.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-11-06"},{"uniquename":"PMID:8654749","title":"Characterisation of Krp1, an endopeptidase that is essential for cell viability in fission yeast.","citation":"Biochem Soc Trans 1995 Nov;23(4):564S","abstract":"","authors":"Powner D, Davis K, Matthews G, Davey J","authors_abbrev":"Powner D et al.","pubmed_publication_date":"Nov 1995","pubmed_entrez_date":"1995-11-01","publication_year":"1995","canto_session_key":"d527fd9cb5fb42a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-03-22 19:32:33","canto_session_submitted_date":"2012-03-22 16:41:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-03-22"},{"uniquename":"EMBL:AU008702","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF154055","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32320462","title":"Sterol biosensor reveals LAM-family Ltc1-dependent sterol flow to endosomes upon Arp2/3 inhibition.","citation":"J Cell Biol 2020 Jun 01;219(6)","abstract":"Sterols are crucial components of biological membranes, which are synthetized in the ER and accumulate in the plasma membrane (PM). Here, by applying a genetically encoded sterol biosensor (D4H), we visualize a sterol flow between PM and endosomes in the fission yeast Schizosaccharomyces pombe. Using time-lapse and correlative light-electron microscopy, we found that inhibition of Arp2/3-dependent F-actin assembly promotes the reversible relocalization of D4H from the PM to internal sterol-rich compartments (STRIC) labeled by synaptobrevin Syb1. Retrograde sterol internalization to STRIC is independent of endocytosis or an intact Golgi, but depends on Ltc1, a LAM/StARkin-family protein localized to ER-PM contact sites. The PM in ltc1Δ cells over-accumulates sterols and upon Arp2/3 inhibition forms extended ER-interacting invaginations, indicating that sterol transfer contributes to PM size homeostasis. Anterograde sterol movement from STRIC is independent of canonical vesicular trafficking but requires Arp2/3, suggesting a novel role for this complex. Thus, transfer routes orthogonal to vesicular trafficking govern the flow of sterols in the cell.","doi":"10.1083/jcb.202001147","authors":"Marek M, Vincenzetti V, Martin SG","authors_abbrev":"Marek M et al.","pubmed_publication_date":"01 Jun 2020","pubmed_entrez_date":"2020-04-23","publication_year":"2020","canto_session_key":"ce86e0783b08ae9a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2020-08-05 12:24:44","canto_approved_date":"2025-09-03 11:29:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-17 15:14:29","canto_added_date":"2020-04-24 00:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":34,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC23B6.01c","SPBC1271.12","SPBC2F12.05c","SPCC970.09","SPBC31F10.16","SPAC17C9.12","SPAC19A8.02","SPBC646.08c","SPBC354.07c","SPAC11H11.06","SPBP16F5.07","SPAC23H4.01c","SPBC16G5.05c","SPBC20F10.07","SPAC6G9.12"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2020-08-05"},{"uniquename":"PMID:12597774","title":"Characterization of SUMO-conjugating enzyme mutants in Schizosaccharomyces pombe identifies a dominant-negative allele that severely reduces SUMO conjugation.","citation":"Biochem J 2003 May 15;372(Pt 1):97-104","abstract":"The phenotypes of mutants defective in the Schizosaccharomyces pombe SUMO (small, ubiquitin-like modifier)-conjugating enzyme Hus5 (the homologue of Ubc9) show that it is required for recovery from S-phase arrest. Unlike the case with ubiquitination, where ligases are required, SUMO-conjugating enzymes are sufficient for substrate recognition and conjugation of SUMO on to target proteins, at least in vitro. Thus SUMO-conjugating enzymes are likely to be important regulators of sumoylation. Here, we report on the characterization of two hus5 alleles. Although hus5.17 and hus5.62 respond in a similar manner to UV and ionizing radiation, they have different responses to the DNA-synthesis inhibitor, hydroxyurea. In addition, SUMO (Pmt3) is mislocalized in hus5.17 cells, but not in hus5.62 mutant cells. The mutations in hus5.62 and hus5.17 map to Ala(129) and the 5' splice site of intron 2 respectively. We have characterized the Hus5.62 protein and shown, in vitro, that it still interacts with SUMO and at least one protein, Rad22, which is a SUMO-modified target. The Hus5.62 protein is also capable of forming a thioester link with SUMO, but it does not function in sumoylation assays, either in the modification of Rad22 or in SUMO chain formation. When overexpressed in wild-type S. pombe cells, the Hus5.62 protein has a dominant-negative effect on sumoylation.","authors":"Ho JC, Watts FZ","authors_abbrev":"Ho JC et al.","pubmed_publication_date":"15 May 2003","pubmed_entrez_date":"2003-02-25","publication_year":"2003","canto_session_key":"b20fa4124e6891de","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-07-10 15:26:50","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-11 16:26:11","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4C5.04","SPBC16H5.03c","SPBC365.06","SPAC30D11.10","SPCC1840.04","SPAC30D11.13"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2013-10-11"},{"uniquename":"PMID:4543091","title":"Enzyme synthesis and potential during induction synchrony in the fission yeast Schizosaccharomyces pombe.","citation":"Exp Cell Res 1973 Nov;82(1):63-72","abstract":"","authors":"Sissons CH, Mitchison JM, Creanor J","authors_abbrev":"Sissons CH et al.","pubmed_publication_date":"Nov 1973","pubmed_entrez_date":"1973-11-01","publication_year":"1973","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9285819","title":"The spindle pole body of Schizosaccharomyces pombe enters and leaves the nuclear envelope as the cell cycle proceeds.","citation":"Mol Biol Cell 1997 Aug;8(8):1461-79","abstract":"The cycle of spindle pole body (SPB) duplication, differentiation, and segregation in Schizosaccharomyces pombe is different from that in some other yeasts. Like the centrosome of vertebrate cells, the SPB of S. pombe spends most of interphase in the cytoplasm, immediately next to the nuclear envelope. Some gamma-tubulin is localized on the SPB, suggesting that it plays a role in the organization of interphase microtubules (MTs), and serial sections demonstrate that some interphase MTs end on or very near to the SPB. gamma-Tubulin is also found on osmiophilic material that lies near the inner surface of the nuclear envelope, immediately adjacent to the SPB, even though there are no MTs in the interphase nucleus. Apparently, the MT initiation activities of gamma-tubulin in S. pombe are regulated. The SPB duplicates in the cytoplasm during late G2 phase, and the two resulting structures are connected by a darkly staining bridge until the mitotic spindle forms. As the cell enters mitosis, the nuclear envelope invaginates beside the SPB, forming a pocket of cytoplasm that accumulates dark amorphous material. The nuclear envelope then opens to form a fenestra, and the duplicated SPB settles into it. Each part of the SPB initiates intranuclear MTs, and then the two structures separate to lie in distinct fenestrae as a bipolar spindle forms. Through metaphase, the SPBs remain in their fenestrae, bound to the polar ends of spindle MTs; at about this time, a small bundle of cytoplasmic MTs forms in association with each SPB. These MTs are situated with one end near to, but not on, the SPBs, and they project into the cytoplasm at an orientation that is oblique to the simple axis. As anaphase proceeds, the nuclear fenestrae close, and the SPBs are extruded back into the cytoplasm. These observations define new fields of enquiry about the control of SPB duplication and the dynamics of the nuclear envelope.","authors":"Ding R, West RR, Morphew DM, Oakley BR, McIntosh JR","authors_abbrev":"Ding R et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20060701","title":"Force and length regulation in the microtubule cytoskeleton: lessons from fission yeast.","citation":"Curr Opin Cell Biol 2010 Feb;22(1):21-8","abstract":"How does a living cell deal with basic concepts of physics such as length and force? The cell has to measure distances and regulate forces to dynamically organize its interior. This is to a large extent based on microtubules (MTs) and motor proteins. Two concepts are emerging from recent studies as key to the positioning of cell components: preferred disassembly of longer MTs and preferred detachment of motors under high load force. The role of these concepts in nuclear centering and nuclear oscillations is coming to light from experimental and theoretical studies in fission yeast. These universal concepts are likely crucial for a variety of cell processes, including nuclear and mitotic spindle positioning, control of spindle length, and chromosome congression on the metaphase plate.","doi":"10.1016/j.ceb.2009.12.011","authors":"Tolić-Nørrelykke IM","authors_abbrev":"Tolić-Nørrelykke IM","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2010-01-12","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10365961","title":"The MAPK kinase Pek1 acts as a phosphorylation-dependent molecular switch.","citation":"Nature 1999 Jun 03;399(6735):479-83","abstract":"The mitogen-activated protein kinase (MAPK) pathway is a highly conserved eukaryotic signalling cascade that converts extracellular signals into various outputs, such as cell growth and differentiation. MAPK is phosphorylated and activated by a specific MAPK kinase (MAPKK): MAPKK is therefore considered to be an activating regulator of MAPK. Pmk1 is a MAPK that regulates cell integrity and which, with calcineurin phosphatase, antagonizes chloride homeostasis in fission yeast. We have now identified Pek1, a MAPKK for Pmk1 MAPK. We show here that Pek1, in its unphosphorylated form, acts as a potent negative regulator of Pmk1 MAPK signalling. Mkh1, an upstream MAPKK kinase (MAPKKK), converts Pek1 from being an inhibitor to an activator. Our results indicate that Pek1 has a dual stimulatory and inhibitory function which depends on its phosphorylation state. This switch-like mechanism could contribute to the all-or-none physiological response mediated by the MAPK signalling pathway.","authors":"Sugiura R, Toda T, Dhut S, Shuntoh H, Kuno T","authors_abbrev":"Sugiura R et al.","pubmed_publication_date":"03 Jun 1999","pubmed_entrez_date":"1999-06-12","publication_year":"1999","canto_session_key":"73410360c651acac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-29 15:55:06","canto_approved_date":"2024-06-28 12:59:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-29 08:43:15","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.01","SPBC543.07","SPAC1F3.02c","SPBC119.08","SPBP4H10.04"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-08-29"},{"uniquename":"PMID:7851743","title":"Mutations which reduce levels of pyruvate dehydrogenase in Schizosaccharomyces pombe cause a requirement for arginine or glutamine.","citation":"FEMS Microbiol Lett 1994 Dec 15;124(3):361-5","abstract":"Forty-four mutants of Schizosaccharomyces pombe were isolated which required supplementation with arginine or glutamine. These mutants appear to define three genes, provisionally named agg1, agg2 and agg3 (arginine, glutamine requiring). Mutants in all three genes were found to have reduced levels of pyruvate dehydrogenase compared to wild-type.","authors":"Cavan G, MacDonald D","authors_abbrev":"Cavan G et al.","pubmed_publication_date":"15 Dec 1994","pubmed_entrez_date":"1994-12-15","publication_year":"1994","canto_session_key":"f92b01e690ab6f7d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-06 17:54:40","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-04-24 16:08:15","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-04-24"},{"uniquename":"PMID:23118915","title":"Stress activated protein kinase pathway modulates homologous recombination in fission yeast.","citation":"PLoS One 2012;7(10):e47987","abstract":"Rad52 is a key player in homologous recombination (HR), a DNA repair pathway that is dedicated to double strand breaks repair and recovery of perturbed replication forks. Here we show that fission yeast Rad52 homologue is phosphorylated when S phase cells are exposed to ROS inducers such as ultraviolet A radiation or hydrogen peroxide, but not to ultraviolet C or camptothecin. Phosphorylation does not depend on kinases Chk1, Rad3, Tel1 or Cdc2, but depends on a functional stress activated protein kinase (SAPK) pathway and can be partially prevented by anti-oxidant treatment. Indeed, cells lacking Sty1, the major fission yeast MAP kinase of the SAPK pathway, do not display Rad52 phosphorylation and have UVA induced Rad52 foci that persist longer if compared to wild type cells. In addition, spontaneous intrachromosomal HR is diminished in cells lacking Sty1 and, more precisely, gene conversion is affected. Moreover, HR induced by site-specific arrest of replication forks is twice less efficient in cells that do not express Sty1. Importantly, impairing HR by deletion of the gene encoding the recombinase Rhp51 leads to Sty1 dependent Rad52 phosphorylation. Thus, SAPK pathway impinges on early step of HR through phosphorylation of Rad52 in cells challenged by oxidative stress or lacking Rhp51 and is required to promote spontaneous gene conversion and recovery from blocked replication forks.","doi":"10.1371/journal.pone.0047987","authors":"Bellini A, Girard PM, Lambert S, Tessier L, Sage E, Francesconi S","authors_abbrev":"Bellini A et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-11-03","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPAC644.14c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9013342","title":"The size control of fission yeast revisited.","citation":"J Cell Sci 1996 Dec;109 ( Pt 12):2947-57","abstract":"An analysis was made of cell length and cycle time in time-lapse films of the fission yeast Schizosaccharomyces pombe using wild-type (WT) cells and those of various mutants. The more important conclusions about 'size controls' are: (1) there is a marker in G2 in WT cells provided by a rate change point (RCP) where the linear rate of length growth increases by approximately 30%. The period before this RCP is dependent on size and can be called a 'sizer'. The period after the RCP is nearly independent of size and can be called a 'timer'. The achievement of a critical threshold size is at or near the RCP which is on average at about 0.3 of the cycle (halfway through G2). This is much earlier than was previously believed. (2) The RCP is at about the time when H1 histone kinase activity and the B type cyclin cdc13 start to rise in preparation for mitosis. The RCP is also associated with other metabolic changes. (3) In wee1 mutants, the mitotic size control is replaced by a G1/S size control which is as strong as the mitotic control. As in WT cells, there is a sizer which precedes the RCP followed by a timer but the RCP is at about the G1/S boundary and has a larger increase (approximately 100%) in rate. (4) cdc25 is not an essential part of the size control at mitosis or at the G1/S boundary. (5) Three further situations have been examined in which the mitotic size control has been abolished. First, induction synchronisation by block and release of cdc2 and cdc10. In the largest oversize-cells which are produced, the RCP is pushed back to the beginning of the cycle. There is no sizer period but only a timer. Second, when both the antagonists wee1 and cdc25 are absent in the double mutant wee1-50 cdc25 delta. In this interesting situation there is apparently no mitotic size control and the cycle times are quantised. Third, in rum1 delta wee1-50 where the normal long G1 in wee1 is much reduced, there is probably no size control either in G1 or in G2 causing a continuous shortening of division length from cycle to cycle.","authors":"Sveiczer A, Novak B, Mitchison JM","authors_abbrev":"Sveiczer A et al.","pubmed_publication_date":"Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC11B10.09","SPAC24H6.05","SPBC32F12.09"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:15529002","title":"Transcriptional regulation of glutathione synthetase in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Cells 2004 Oct 31;18(2):242-8","abstract":"Glutathione (GSH), an important antioxidant involved in the stress response, is synthesized in two sequential reactions involving glutamylcysteine synthetase (GCS), followed by glutathione synthetase (GS). Expression of the unique GS gene in the fission yeast Schizosaccharomyces pombe was previously found to be regulated by nitric oxide and by L-buthionine-(S,R)-sulfoximine (BSO), a specific inhibitor of GCS. In this work, expression of S. pombe GS gene is shown to be induced by menadione (MD), which generates superoxide. The responsible DNA sequence between -365 and -234 bp from the translation start site, was convinced using five GS-lacZ fusion plasmids. Expression of GS gene is also induced by low glucose, fructose and disaccharides, apparently dependent on Pap1 protein; GS mRNA increases in low concentrations of glucose in wild type S. pombe but not in Pap1-negative cells. Although nonfermentable carbon sources such as acetate and ethanol stimulate expression of GS gene, they also arrest the growth of the yeast cells. These results indicate that the biosynthesis of glutathione is regulated by superoxide radicals and carbon source limitation.","authors":"Kim SJ, Kim HG, Kim BC, Park EH, Lim CJ","authors_abbrev":"Kim SJ et al.","pubmed_publication_date":"31 Oct 2004","pubmed_entrez_date":"2004-11-06","publication_year":"2004","canto_session_key":"fcd0b8c6ab5ccb12","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-20 10:42:05","canto_approved_date":"2024-03-29 12:56:05","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-11-20 10:41:58","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC3F10.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-20"},{"uniquename":"PMID:29618061","title":"Histone deacetylation promotes transcriptional silencing at facultative heterochromatin.","citation":"Nucleic Acids Res 2018 Jun 20;46(11):5426-5440","abstract":"It is important to accurately regulate the expression of genes involved in development and environmental response. In the fission yeast Schizosaccharomyces pombe, meiotic genes are tightly repressed during vegetative growth. Despite being embedded in heterochromatin these genes are transcribed and believed to be repressed primarily at the level of RNA. However, the mechanism of facultative heterochromatin formation and the interplay with transcription regulation is not understood. We show genome-wide that HDAC-dependent histone deacetylation is a major determinant in transcriptional silencing of facultative heterochromatin domains. Indeed, mutation of class I/II HDACs leads to increased transcription of meiotic genes and accumulation of their mRNAs. Mechanistic dissection of the pho1 gene where, in response to phosphate, transient facultative heterochromatin is established by overlapping lncRNA transcription shows that the Clr3 HDAC contributes to silencing independently of SHREC, but in an lncRNA-dependent manner. We propose that HDACs promote facultative heterochromatin by establishing alternative transcriptional silencing.","doi":"10.1093/nar/gky232","authors":"Watts BR, Wittmann S, Wery M, Gautier C, Kus K, Birot A, Heo DH, Kilchert C, Morillon A, Vasiljeva L","authors_abbrev":"Watts BR et al.","pubmed_publication_date":"20 Jun 2018","pubmed_entrez_date":"2018-04-05","publication_year":"2018","canto_session_key":"9c63dd7d54df2fb5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-25 08:54:48","canto_approved_date":"2024-06-26 16:59:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-04 09:47:54","canto_added_date":"2018-04-06 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":38,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.1712","SPCC306.04c","SPNCRNA.29","SPAC29B12.02c","SPBC428.08c","SPAC3G9.07c","SPBP35G2.10","SPBC36.05c","SPBP4G3.02","SPAC1F3.01","SPBC800.03","SPAC1A6.06c","SPBC359.06","SPCC736.12c","SPBC2D10.17","SPBC16D10.07c","SPBC1271.09","SPBC28F2.12","SPAC1B3.17","SPAC222.09","SPNCRNA.1698"],"gene_count":21,"ltp_gene_count":11,"approved_date":"2024-01-25"},{"uniquename":"EMBL:SPU77355","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22797921","title":"Heat induction of a novel Rad9 variant from a cryptic translation initiation site reduces mitotic commitment.","citation":"J Cell Sci 2012 Oct 01;125(Pt 19):4487-97","abstract":"Exposure of human cells to heat switches the activating signal of the DNA damage checkpoint from genotoxic to temperature stress. This change reduces mitotic commitment at the expense of DNA break repair. The thermal alterations behind this switch remain elusive despite the successful use of heat to sensitise cancer cells to DNA breaks. Rad9 is a highly conserved subunit of the Rad9-Rad1-Hus1 (9-1-1) checkpoint-clamp that is loaded by Rad17 onto damaged chromatin. At the DNA, Rad9 activates the checkpoint kinases Rad3(ATR) and Chk1 to arrest cells in G2. Using Schizosaccharomyces pombe as a model eukaryote, we discovered a new variant of Rad9, Rad9-M50, whose expression is specifically induced by heat. High temperatures promote alternative translation from a cryptic initiation codon at methionine-50. This process is restricted to cycling cells and is independent of the temperature-sensing mitogen-activated protein kinase (MAPK) pathway. While full-length Rad9 delays mitosis in the presence of DNA lesions, Rad9-M50 functions in a remodelled checkpoint pathway to reduce mitotic commitment at elevated temperatures. This remodelled pathway still relies on Rad1 and Hus1, but acts independently of Rad17. Heat-induction of Rad9-M50 ensures that the kinase Chk1 remains in a hypo-phosphorylated state. Elevated temperatures specifically reverse the DNA-damage-induced modification of Chk1 in a manner dependent on Rad9-M50. Taken together, heat reprogrammes the DNA damage checkpoint at the level of Chk1 by inducing a Rad9 variant that can act outside of the canonical 9-1-1 complex.","doi":"10.1242/jcs.104075","authors":"Janes S, Schmidt U, Ashour Garrido K, Ney N, Concilio S, Zekri M, Caspari T","authors_abbrev":"Janes S et al.","pubmed_publication_date":"01 Oct 2012","pubmed_entrez_date":"2012-07-17","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.13","SPAC664.07c","SPBC216.05","SPCC23B6.03c","SPCC18B5.11c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:31111477","title":"Functional expression and activity screening of all human cytochrome P450 enzymes in fission yeast.","citation":"FEBS Lett 2019 Jun;593(12):1372-1380","abstract":"Here, a complete set of recombinant fission yeast strains that coexpress each of the 57 human cytochrome P450 (CYP) enzymes together with their natural human electron transfer partner(s) was cloned. This strain collection was tested with two luminogenic probe substrates, and 31 human CYPs (including the orphan enzymes CYP2A7, CYP4A22 and CYP20A1) were found to metabolize at least one of these. Since other substrates are known for the remaining enzymes, all human CYPs are now shown to be active. Interestingly, CYP5A1 was found for the first time to work on a substrate other than prostaglandin H 2  , and, moreover, to catalyze an aliphatic hydroxylation reaction that consumes molecular oxygen. Also, the ability of CYP11A1 to catalyze an aryl hydroxylation is another unexpected result.","doi":"10.1002/1873-3468.13441","authors":"Durairaj P, Fan L, Du W, Ahmad S, Mebrahtu D, Sharma S, Ashraf RA, Liu J, Liu Q, Bureik M","authors_abbrev":"Durairaj P et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-05-22","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-05-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25076038","title":"Large scale screening of genetic interaction with sgf73(+) in fission yeast.","citation":"Yi Chuan 2014 Jul;36(7):723-31","abstract":"Genetic interaction (GI) not only suggests functional correlations between different genes in vivo, but also provides clues for understanding the potential biological function of a specific gene. Screening of GI is an important method for understanding GI between different genes. In this study, we selected sgf73⁺ as a query, which encodes a subunit of SAGA (Spt-Ada-Gcn5 acetyltransferase) complex deubiquitination module, to perform a large scale screening of GI in fission yeast. Our data showed that 164 genes had negative GIs whereas 42 genes had positive GIs with sgf73⁺. GO (Gene ontology) analysis indicated that these genes were enriched in several important biological processes, including chromatin modification, DNA damage repair, cellular response to stress, RNA transcription and so on. By using histone modification detection, we showed for the first time that loss of sgf73⁺ led to a decreased level of histone acetylation at H3K9 and H4K16 and an increased level of histone H3K4 methylation. Furthermore, the spot assay results showed that the sgf73∆ cells exhibited increased sensitivity to DNA damage agents, HU and CPT, and sgf73⁺ was involved in responses to hyperoxia stress. All these results suggested that sgf73⁺ plays important roles in chromatin modification, DNA damage repair and hyperoxia responses.","doi":"10.3724/SP.J.1005.2014.0723","authors":"Guo Y, Lei B, Deng X, Yu Y, Lv H","authors_abbrev":"Guo Y et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-07-31","publication_year":"2014","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2014-08-01 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.05c","SPBC56F2.08c","SPAC23A1.19c","SPAC1834.07","SPAC2F3.02","SPAC11E3.01c","SPBC21B10.05c","SPCC132.02","SPAC1B3.02c","SPBC1778.02","SPBC19C7.02","SPAC27F1.06c","SPBC21D10.10","SPBC409.08","SPBC6B1.02","SPBC29A3.14c","SPBC31F10.09c","SPBC651.05c","SPAPYUG7.02c","SPAC15A10.16","SPAC27D7.13c","SPBC83.09c","SPBC713.05","SPBC1685.01","SPBC36B7.08c","SPAC20H4.08","SPAC15E1.07c","SPBC13E7.03c","SPCC1223.01","SPAC12B10.12c","SPBC32H8.11","SPBPB2B2.12c","SPBC23E6.01c","SPCC11E10.08","SPAC26H5.04","SPAC630.13c","SPBC947.10","SPBC1773.11c","SPAC18G6.15","SPBC16D10.07c","SPAC56E4.07","SPAC1093.03","SPBC713.07c","SPAC17G6.03","SPAC1142.08","SPBC1105.11c","SPAPYUG7.03c","SPBC16E9.17c","SPAPJ696.01c","SPAC23H3.05c","SPBC16A3.18","SPAC3A12.03c","SPAC6B12.08","SPBC12D12.02c","SPBC13E7.09","SPAC23D3.09","SPCC306.07c","SPBC409.20c","SPAC644.09","SPAC23C11.08","SPAC26A3.16","SPAC23C4.08","SPAC15E1.03","SPAC3C7.09","SPAC144.17c","SPCC1753.02c","SPAC1D4.06c","SPAC644.14c","SPBC31F10.10c","SPBC11C11.08","SPBC29A10.10c","SPAC2F7.08c","SPBC3H7.13","SPAC823.15","SPAC1142.03c","SPCC4B3.07","SPAC20H4.04","SPBP22H7.05c","SPCC24B10.13","SPBC1685.15c","SPACUNK4.16c","SPAC1805.07c","SPCC126.04c","SPBC428.08c","SPAC1805.05","SPBP4H10.16c","SPBC16H5.11c","SPAC328.06","SPAC3C7.12","SPCC1919.01","SPBC19F8.01c","SPBC337.16","SPBC23E6.03c","SPAC4D7.11","SPAP32A8.03c","SPBC2G2.17c","SPBC646.13","SPAC1F5.09c","SPCC23B6.05c","SPAC31F12.01","SPBC20F10.06","SPAC227.10","SPBC31F10.13c","SPAC8F11.02c","SPCC622.19","SPAC12B10.13","SPAC1687.22c","SPAC31A2.02","SPCC1753.03c","SPAC4A8.09c","SPAC2E1P5.03","SPAC1486.01","SPAPB17E12.04c","SPBC21B10.13c","SPCC594.05c","SPCC645.08c","SPCC794.12c","SPAC17H9.09c","SPAPYUG7.06","SPAC20H4.02","SPBC2D10.11c","SPBC2G2.01c","SPCC18B5.11c","SPBP8B7.10c","SPCC645.13","SPCC736.08","SPAC6G9.10c","SPAC31A2.14","SPAC1639.02c","SPAC3G9.05","SPBC25B2.07c","SPAC20H4.11c","SPAC4G9.14","SPAC139.06","SPBP35G2.10","SPBC4F6.06","SPBC1D7.01","SPAC23C11.14","SPAC6G9.03c","SPAC20G4.01","SPAC8E11.02c","SPAC1565.04c","SPBC31F10.07","SPAC688.14","SPBC28F2.10c","SPAC31G5.09c","SPAC17C9.09c","SPAC6F12.04","SPCC1322.02","SPCC613.01","SPAC29A4.02c","SPAC22F3.08c","SPAC29A4.18","SPBC4B4.03","SPAC57A10.09c","SPBC12C2.08","SPCC970.07c","SPAC23H4.17c","SPAC22F3.03c","SPAC4F10.04","SPCC11E10.07c","SPAC9G1.12","SPBC1604.20c","SPBC1347.02","SPBC2F12.11c","SPAC6F6.01","SPAC25H1.02","SPBC13G1.08c","SPAC16E8.01","SPAC1805.04","SPBC28F2.08c","SPBC2G2.05","SPBC56F2.03","SPAC14C4.05c","SPBC725.15","SPAC664.03","SPBC1105.14","SPAC16C9.05","SPAC1D4.11c","SPAC694.06c","SPAC26F1.10c","SPAC13C5.02","SPCC4B3.12","SPAPB18E9.01","SPAC1F3.02c","SPCC550.11","SPCP25A2.02c","SPBC713.08","SPAC8C9.17c","SPAC6F12.06","SPCC417.06c","SPAC18B11.07c","SPAC23C4.12","SPBP8B7.25","SPBC354.10","SPBC902.02c","SPBC29A3.07c","SPAC1952.05","SPAC821.05","SPBC1718.03","SPBC1D7.05","SPBC23G7.11","SPBC3D6.09"],"gene_count":203,"ltp_gene_count":0},{"uniquename":"EMBL:U80217","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009597","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21253571","title":"H3K9me-independent gene silencing in fission yeast heterochromatin by Clr5 and histone deacetylases.","citation":"PLoS Genet 2011 Jan 06;7(1):e1001268","abstract":"Nucleosomes in heterochromatic regions bear histone modifications that distinguish them from euchromatic nucleosomes. Among those, histone H3 lysine 9 methylation (H3K9me) and hypoacetylation have been evolutionarily conserved and are found in both multicellular eukaryotes and single-cell model organisms such as fission yeast. In spite of numerous studies, the relative contributions of the various heterochromatic histone marks to the properties of heterochromatin remain largely undefined. Here, we report that silencing of the fission yeast mating-type cassettes, which are located in a well-characterized heterochromatic region, is hardly affected in cells lacking the H3K9 methyltransferase Clr4. We document the existence of a pathway parallel to H3K9me ensuring gene repression in the absence of Clr4 and identify a silencing factor central to this pathway, Clr5. We find that Clr5 controls gene expression at multiple chromosomal locations in addition to affecting the mating-type region. The histone deacetylase Clr6 acts in the same pathway as Clr5, at least for its effects in the mating-type region, and on a subset of other targets, notably a region recently found to be prone to neo-centromere formation. The genomic targets of Clr5 also include Ste11, a master regulator of sexual differentiation. Hence Clr5, like the multi-functional Atf1 transcription factor which also modulates chromatin structure in the mating-type region, controls sexual differentiation and genome integrity at several levels. Globally, our results point to histone deacetylases as prominent repressors of gene expression in fission yeast heterochromatin. These deacetylases can act in concert with, or independently of, the widely studied H3K9me mark to influence gene silencing at heterochromatic loci.","doi":"10.1371/journal.pgen.1001268","authors":"Hansen KR, Hazan I, Shanker S, Watt S, Verhein-Hansen J, Bähler J, Martienssen RA, Partridge JF, Cohen A, Thon G","authors_abbrev":"Hansen KR et al.","pubmed_publication_date":"06 Jan 2011","pubmed_entrez_date":"2011-01-22","publication_year":"2011","canto_session_key":"53baccdeeeb092f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-09 09:40:00","canto_approved_date":"2022-07-24 08:47:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-19 11:52:49","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPAC29B12.08","SPBC36.05c","SPBC428.08c","SPCC188.13c","SPBC32C12.02","SPAC664.01c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-02-09"},{"uniquename":"PMID:11897018","title":"The model unicellular eukaryote, Schizosaccharomyces pombe.","citation":"Genome Biol 2002;3(3):COMMENT2003","abstract":"The fission yeast Schizosaccharomyces pombe has long been a model organism for studies of eukaryotic cells, winning renown especially for studies of the cell cycle. Now that its genome has been sequenced, S. pombe is ready to assume its rightful place in the pantheon of small eukaryotic giants.","authors":"Yanagida M","authors_abbrev":"Yanagida M","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-03-19","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28011631","title":"Lipid droplet dynamics during  Schizosaccharomyces pombe  sporulation and their role in spore survival.","citation":"Biol Open 2017 Feb 15;6(2):217-222","abstract":"Upon nitrogen starvation, the fission yeast  Schizosaccharomyces pombe  forms dormant spores; however, the mechanisms by which a spore sustains life without access to exogenous nutrients remain unclear. Lipid droplets are reservoirs of neutral lipids that act as important cellular energy resources. Using live-cell imaging analysis, we found that the lipid droplets of mother cells redistribute to their nascent spores. Notably, this process was actin polymerization-dependent and facilitated by the leading edge proteins of the forespore membrane. Spores lacking triacylglycerol synthesis, which is essential for lipid droplet formation, failed to germinate. Our results suggest that the lipid droplets are important for the sustenance of life in spores.","doi":"10.1242/bio.022384","authors":"Yang HJ, Osakada H, Kojidani T, Haraguchi T, Hiraoka Y","authors_abbrev":"Yang HJ et al.","pubmed_publication_date":"15 Feb 2017","pubmed_entrez_date":"2016-12-25","publication_year":"2017","canto_session_key":"a493fe4ede17fe68","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hui-Ju Yang","canto_first_approved_date":"2017-11-04 23:26:38","canto_approved_date":"2020-11-10 10:58:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-05-23 03:58:08","canto_added_date":"2016-12-26 01:15:11","annotation_curators":[{"name":"Hui-Ju Yang","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1235.15","SPBC776.14","SPAC1F8.05","SPAC1786.01c","SPCC1183.12","SPBC1347.03","SPBC16E9.08","SPCC417.06c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-11-04"},{"uniquename":"PMID:7501454","title":"Studies of Schizosaccharomyces pombe DNA polymerase alpha at different stages of the cell cycle.","citation":"Nucleic Acids Res 1995 Nov 11;23(21):4337-44","abstract":"The status of Schizosaccharomyces pombe (fission yeast) DNA polymerase alpha was investigated at different stages of the cell cycle. S.pombe DNA polymerase alpha is a phosphoprotein, with serine being the exclusive phosphoamino acid. By in vivo pulse labeling experiments DNA polymerase alpha was found to be phosphorylated to a 3-fold higher level in late S phase cells compared with cells in the G2 and M phases, but the steady-state level of phosphorylation did not vary significantly during the cell cycle. Tryptic phosphopeptide mapping demonstrated that the phosphorylation sites of DNA polymerase alpha from late S phase cells were not the same as that from G2/M phase cells. DNA polymerase alpha partially purified from G1/S cells had a different mobility in native gels from that from G2/M phase cells. The partially purified polymerase alpha from G1/S phase cells had a higher affinity for single-stranded DNA than that from G2/M phase cells. Despite the apparent differences in cell cycle-dependent phosphorylation, mobility in native gels and affinity for DNA, the in vitro enzymatic activity of the partially purified DNA polymerase alpha did not appear to vary during the cell cycle. The possible biological significance of these cell cycle-dependent characteristics of DNA polymerase alpha is discussed.","authors":"Park H, Davis R, Wang TS","authors_abbrev":"Park H et al.","pubmed_publication_date":"11 Nov 1995","pubmed_entrez_date":"1995-11-11","publication_year":"1995","canto_session_key":"f5dfe6e677d045d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-21 16:21:08","canto_approved_date":"2025-09-03 13:14:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-21 16:21:02","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-21"},{"uniquename":"PMID:20132843","title":"Challenges of steroid biotransformation with human cytochrome P450 monooxygenase CYP21 using resting cells of recombinant Schizosaccharomyces pombe.","citation":"J Biotechnol 2010 Apr 15;146(4):179-85","abstract":"Since cytochrome P450 monooxygenases enable the regio- and stereo-selective hydroxylation of C-H bonds, they are of outstanding interest for the synthesis of pharmaceuticals and fine chemicals. Nevertheless, for industrial applications of such enzymes, e.g., steroid hydroxylation, several challenges like cofactor and oxygen supply, limited stability and activity, or low substrate solubility have to be overcome. To identify the limiting factors in a P450 catalyzed whole cell biotransformation, 21-hydroxylation of 17-alpha-hydroxyprogesterone in Schizosaccharomyces pombe expressing human CYP21 was chosen as model reaction. We report here that resting cells of this recombinant yeast strain can be used for efficient biotransformation. In the present study, we analyzed the intracellular redox cofactor pool of S. pombe by LC-MS/MS measurements and report the first quantification of the intracellular cofactor pool during P450 hydroxylation. Thereby a limitation caused by the redox cofactor could be excluded for resting cells. In contrary, low substrate solubility and its transport into the cell affect activity. Screening for an appropriate cosolvent identified methanol as the most promising candidate, since it showed the lowest inactivation effect on the biocatalyst. Through permeabilization of the membrane with the detergent tween 80 steroid hydroxylation activity increases, leading to a productivity of 540 microM d(-1) in a final batch experiment under optimized reaction conditions.","doi":"10.1016/j.jbiotec.2010.01.019","authors":"Zehentgruber D, Drăgan CA, Bureik M, Lütz S","authors_abbrev":"Zehentgruber D et al.","pubmed_publication_date":"15 Apr 2010","pubmed_entrez_date":"2010-02-06","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40385371","title":"Characterization of temperature-sensitive alleles of the septation initiation network protein Mob1 in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2025;2025","abstract":" Schizosaccharomyces pombe  Mob1 is the regulatory subunit of the protein kinase Sid2 . The Sid2- Mob1 complex is the most downstream acting component of the septation initiation network (SIN). In the absence of functional Mob1 , cells fail cytokinesis and become multinucleate. Here we characterize a set of temperature-sensitive  mob1  alleles by identifying the mutations within each allele, characterizing the extent of their growth defects, and visualizing the cell defects. Based on structural modeling, we hypothesize that the Mob1 mutations interfere with Mob1 stability and its ability to bind the N-terminal regulatory region of Sid2 .","doi":"10.17912/micropub.biology.001595","authors":"Hanna SM, Willet AH, Gould KL","authors_abbrev":"Hanna SM et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-05-19","publication_year":"2025","canto_session_key":"be4159be8b1b74c8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2025-06-10 15:19:26","canto_approved_date":"2026-01-31 13:00:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-09 19:55:35","canto_added_date":"2025-05-19 23:25:05","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":6,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-06-10"},{"uniquename":"PMID:9832516","title":"Suppressors of cdc25p overexpression identify two pathways that influence the G2/M checkpoint in fission yeast.","citation":"Genetics 1998 Dec;150(4):1361-75","abstract":"Checkpoints maintain the order of cell-cycle events. At G2/M, a checkpoint blocks mitosis in response to damaged or unreplicated DNA. There are significant differences in the checkpoint responses to damaged DNA and unreplicated DNA, although many of the same genes are involved in both responses. To identify new genes that function specifically in the DNA replication checkpoint pathway, we searched for high-copy suppressors of overproducer of Cdc25p (OPcdc25(+)), which lacks a DNA replication checkpoint. Two classes of suppressors were isolated. One class includes a new gene encoding a putative DEAD box helicase, suppressor of uncontrolled mitosis (sum3(+)). This gene negatively regulates the cell-cycle response to stress when overexpressed and restores the checkpoint response by a mechanism that is independent of Cdc2p tyrosine phosphorylation. The second class includes chk1(+) and the two Schizosaccharomyces pombe 14-3-3 genes, rad24(+) and rad25(+), which appear to suppress the checkpoint defect by inhibiting Cdc25p. We show that rad24Delta mutants are defective in the checkpoint response to the DNA replication inhibitor hydroxyurea at 37 degrees and that cds1Delta rad24Delta mutants, like cds1Delta chk1Delta mutants, are entirely checkpoint deficient at 29 degrees. These results suggest that chk1(+) and rad24(+) may function redundantly with cds1(+) in the checkpoint response to unreplicated DNA.","authors":"Forbes KC, Humphrey T, Enoch T","authors_abbrev":"Forbes KC et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1998-12-02","publication_year":"1998","canto_session_key":"dda3e52a2fc3105f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-10-30 16:29:46","canto_approved_date":"2021-01-06 17:35:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-10-30 16:29:38","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":41,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC24H6.05","SPBC216.05","SPAC20G4.04c","SPBC800.09","SPBC215.05","SPAC26F1.10c","SPCC18B5.11c","SPAC17A2.13c","SPCC1795.11","SPBC11B10.09","SPAC8E11.02c"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2019-10-30"},{"uniquename":"PMID:1288848","title":"Enzyme activities of D-glucose metabolism in the fission yeast Schizosaccharomyces pombe.","citation":"Can J Microbiol 1992 Dec;38(12):1313-9","abstract":"The activities of key enzymes that are members of D-glucose metabolic pathways in Schizosaccharomyces pombe undergoing respirative, respirofermentative, and fermentative metabolisms are monitored. The steady-state activities of glycolytic enzymes, except phosphofructokinase, decrease with a reduced efficiency in D-glucose utilization by yeast continuous culture. On the other hand, the enzymic activities of pentose monophosphate pathway reach the maximum when the cell mass production of the cultures is optimum. Enzymes of tricarboxylate cycle exhibit the maximum activities at approximately the washout rate. The steady-state activity of pyruvate dehydrogenase complex increases rapidly when D-glucose is efficiently utilized. By comparison, the activity of pyruvate decarboxylase begins to increase only when ethanol production occurs. Depletion of dissolved oxygen suppresses the activity of pyruvate dehydrogenase complex but facilitates that of pyruvate decarboxylase. Acetate greatly enhances the acetyl CoA synthetase activity. Similarly, ethanol stimulates alcohol dehydrogenase and aldehyde dehydrogenase activities. Evidence for the existence of alcohol dehydrogenase isozymes in the fission yeast is presented.","authors":"Tsai CS, Shi JL, Beehler BW, Beck B","authors_abbrev":"Tsai CS et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"76ae34c2bc13c119","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-23 10:59:28","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-23 10:59:08","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-23"},{"uniquename":"PMID:39132053","title":"Distance-dependent effects on CRISPR/Cas9-mediated genome editing in  Schizosaccharomyces pombe  compromise efficiency and create unsought alleles.","citation":"MicroPubl Biol 2024;2024","abstract":"Discrete DNA sites position meiotic recombination at hotspots. We sought to create four different, 15 bp long, candidate regulatory DNA sites within the  ura4  reporter gene. Each effort employed a fission yeast-optimized CRISPR system (SpEDIT), optimal guide RNA, and one of four homologous recombination templates with 10 to 15 bp substitutions. Remarkably, every Ura  -  transformant analyzed had template-directed, PAM-disabling bp substitutions near (5-6 bp away from) the DSB but no DNA site-generating substitutions at distance (42-56 bp). An unsought novel allele,  ura4-P127*  , has two substitutions (C379T, C380A) that create a stop codon, rendering strains unable to grow without uracil.","doi":"10.17912/micropub.biology.001248","authors":"Protacio RU, Malone EG, Wahls WP","authors_abbrev":"Protacio RU et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-08-12","publication_year":"2024","canto_session_key":"e828264e31f539e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Emory Malone","canto_first_approved_date":"2024-10-02 09:19:18","canto_approved_date":"2024-10-02 09:19:18","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-10-01 17:08:51","canto_added_date":"2024-08-12 23:25:05","annotation_curators":[{"name":"Emory Malone","community_curator":true,"annotation_count":2,"orcid":"0009-0002-9188-2637","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-10-02"},{"uniquename":"EMBL:AF237708","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7498507","title":"Expression, purification and kinetic behaviour of fission yeast low M(r) protein-tyrosine phosphatase.","citation":"FEBS Lett 1995 Nov 20;375(3):235-8","abstract":"A gene named stp1+, coding for a 17.5-kDa protein, that rescues cdc25-22 when overexpressed, has been previously isolated from fission yeast. Here we describe the expression and purification of Stp1 protein as a fusion with the glutathione S-transferase in E. coli and its kinetic characterisation. Stp1 deduced protein sequence shows an high homology to members of a class of cytosolic low M(r) protein phosphatase previously known to exist only in mammalian species. Stp1 has a kinetic behaviour that appears to be intermediate with respect to the two isoenzymatic forms of low M(r) protein tyrosine phosphatases present in mammalian tissues. These differing kinetic characteristics are mainly due to the sequence 45-56 that is spatially close to the active site pocket.","authors":"Modesti A, Cirri P, Raugei G, Carraresi L, Magherini F, Manao G, Camici G, Ramponi G","authors_abbrev":"Modesti A et al.","pubmed_publication_date":"20 Nov 1995","pubmed_entrez_date":"1995-11-20","publication_year":"1995","canto_session_key":"e1c7a123d6b54783","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-26 20:15:08","canto_approved_date":"2020-01-23 13:36:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 14:05:00","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-01-26"},{"uniquename":"PMID:29416031","title":"Cdk9 regulates a promoter-proximal checkpoint to modulate RNA polymerase II elongation rate in fission yeast.","citation":"Nat Commun 2018 Feb 07;9(1):543","abstract":"Post-translational modifications of the transcription elongation complex provide mechanisms to fine-tune gene expression, yet their specific impacts on RNA polymerase II regulation remain difficult to ascertain. Here, in Schizosaccharomyces pombe, we examine the role of Cdk9, and related Mcs6/Cdk7 and Lsk1/Cdk12 kinases, on transcription at base-pair resolution with Precision Run-On sequencing (PRO-seq). Within a minute of Cdk9 inhibition, phosphorylation of Pol II-associated factor, Spt5 is undetectable. The effects of Cdk9 inhibition are more severe than inhibition of Cdk7 and Cdk12, resulting in a shift of Pol II toward the transcription start site (TSS). A time course of Cdk9 inhibition reveals that early transcribing Pol II can escape promoter-proximal regions, but with a severely reduced elongation rate of only ~400 bp/min. Our results in fission yeast suggest the existence of a conserved global regulatory checkpoint that requires Cdk9 kinase activity.","doi":"10.1038/s41467-018-03006-4","authors":"Booth GT, Parua PK, Sansó M, Fisher RP, Lis JT","authors_abbrev":"Booth GT et al.","pubmed_publication_date":"07 Feb 2018","pubmed_entrez_date":"2018-02-09","publication_year":"2018","canto_session_key":"9f1708e0f12f154f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-02-10 01:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8255785","title":"Duplicated region of sequence similarity to the human XRCC1 DNA repair gene in the Schizosaccharomyces pombe rad4/cut5 gene.","citation":"Nucleic Acids Res 1993 Nov 11;21(22):5274","abstract":"","authors":"Lehmann AR","authors_abbrev":"Lehmann AR","pubmed_publication_date":"11 Nov 1993","pubmed_entrez_date":"1993-11-11","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25474051","title":"Effect of white mustard essential oil on the growth of foodborne pathogens and spoilage microorganisms and the effect of food components on its efficacy.","citation":"J Food Prot 2014 Dec;77(12):2062-8","abstract":"Antimicrobial preservative compounds are added to foods to target specific pathogens and spoilage organisms. White mustard essential oil (WMEO) is an extract that contains 4-hydroxybenzyl isothiocyanate, a compound which has been demonstrated to have antimicrobial activity in limited studies. The objective of this research was to determine the in vitro antimicrobial activity of WMEO against gram-positive and gram-negative spoilage and pathogenic bacteria and determine the effect of food components on the antimicrobial activity. The bacteria Escherichia coli, Salmonella enterica serovar Enteritidis, Enterobacter aerogenes, Staphylococcus aureus, Listeria monocytogenes, Bacillus cereus, and Lactobacillus fermentum, as well as the acid- and preservative-resistant yeast Schizosaccharomyces pombe, were evaluated. All microorganisms were inhibited by WMEO at 8.3 g/liter (equivalent to 1,000 mg/liter 4-hydroxybenzyl isothiocyanate). In general, WMEO was more effective against gram-negative than against gram-positive bacteria. Salmonella Enteritidis and S. pombe were the most sensitive, with inhibition at as low as 2.1 g/liter. The effects on growth profiles varied but included increased lag phases and lethality, indicating both bacteriostatic and bactericidal activity. Soybean oil had a negative effect on the efficacy of WMEO against L. monocytogenes, and at 5% soybean oil, the antimicrobial activity against Salmonella Enteritidis was eliminated after 48 h. Sodium caseinate at 1% also negated the antimicrobial effect of WMEO against Salmonella Enteritidis and decreased its effectiveness against L. monocytogenes. The presence of starch had no significant effect on the antimicrobial activity of WMEO against L. monocytogenes and Salmonella Enteritidis. Thus, WMEO is effective against a wide range of microorganisms and has potential to be used in foods, depending upon the target microorganism and food components present.","doi":"10.4315/0362-028X.JFP-14-257","authors":"Monu EA, David JR, Schmidt M, Davidson PM","authors_abbrev":"Monu EA et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-12-05","publication_year":"2014","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2014-12-06 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21453674","title":"pCMV-Leu2/pUCA-Neo, a vector set for screening Schizosaccharomyces pombe transformants expressing heterologous proteins.","citation":"Anal Biochem 2011 Jul 15;414(2):306-8","abstract":"The expression of foreign proteins in the fission yeast, Schizosaccharomyces pombe, is achieved by introducing an expression vector along with a transducing vector containing an autonomously replicating sequence. We created the expression vector pCMV-Leu2, carrying the LEU2 gene, which complements S. pombeleu1-32, and the transducing vector pUCA-Neo, containing a neomycin-resistance gene. Transformants were screened on leucine-deficient solid medium, followed by rescreening on G418-containing medium. Most of the surviving clones in the initial auxotrophic screening were found to be G418 resistant. The utilization of the pCMV-Leu2 and pUCA-Neo plasmid combination may facilitate rapid screening of S. pombe transformants.","doi":"10.1016/j.ab.2011.03.034","authors":"Terazawa Y, Wakiyama M, Yokoyama S","authors_abbrev":"Terazawa Y et al.","pubmed_publication_date":"15 Jul 2011","pubmed_entrez_date":"2011-04-02","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB054532","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10629185","title":"Trk1 and Trk2 define the major K(+) transport system in fission yeast.","citation":"J Bacteriol 2000 Jan;182(2):394-9","abstract":"The trk1(+) gene has been proposed as a component of the K(+) influx system in the fission yeast Schizosaccharomyces pombe. Previous work from our laboratories revealed that trk1 mutants do not show significantly altered content or influx of K(+), although they are more sensitive to Na(+). Genome database searches revealed that S. pombe encodes a putative gene (designated here trk2(+)) that shows significant identity to trk1(+). We have analyzed the characteristics of potassium influx in S. pombe by using trk1 trk2 mutants. Unlike budding yeast, fission yeast displays a biphasic transport kinetics. trk2 mutants do not show altered K(+) transport and exhibit only a slightly reduced Na(+) tolerance. However, trk1 trk2 double mutants fail to grow at low K(+) concentrations and show a dramatic decrease in Rb(+) influx, as a result of loss of the high-affinity transport component. Furthermore, trk1 trk2 cells are very sensitive to Na(+), as would be expected for a strain showing defective potassium transport. When trk1 trk2 cells are maintained in K(+)-free medium, the potassium content remains higher than that of the wild type or trk single mutants. In addition, the trk1 trk2 strain displays increased sensitivity to hygromycin B. These results are consistent with a hyperpolarized state of the plasma membrane. An additional phenotype of cells lacking both Trk components is a failure to grow at acidic pH. In conclusion, the Trk1 and Trk2 proteins define the major K(+) transport system in fission yeast, and in contrast to what is known for budding yeast, the presence of any of these two proteins is sufficient to allow growth at normal potassium levels.","authors":"Calero F, Gómez N, Ariño J, Ramos J","authors_abbrev":"Calero F et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-12","publication_year":"2000","canto_session_key":"be892da3ecd962ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-20 17:03:11","canto_approved_date":"2017-10-20 17:03:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-10-20 17:01:52","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.02c","SPAC1639.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-10-20"},{"uniquename":"PMID:19158787","title":"Small RNAs in transcriptional gene silencing and genome defence.","citation":"Nature 2009 Jan 22;457(7228):413-20","abstract":"Small RNA molecules of about 20-30 nucleotides have emerged as powerful regulators of gene expression and genome stability. Studies in fission yeast and multicellular organisms suggest that effector complexes, directed by small RNAs, target nascent chromatin-bound non-coding RNAs and recruit chromatin-modifying complexes. Interactions between small RNAs and nascent non-coding transcripts thus reveal a new mechanism for targeting chromatin-modifying complexes to specific chromosome regions and suggest possibilities for how the resultant chromatin states may be inherited during the process of chromosome duplication.","doi":"10.1038/nature07756","authors":"Moazed D","authors_abbrev":"Moazed D","pubmed_publication_date":"22 Jan 2009","pubmed_entrez_date":"2009-01-23","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9601091","title":"The fission yeast microtubule cytoskeleton.","citation":"J Cell Sci 1998 Jun;111 ( Pt 12):1603-12","abstract":"The Schizosaccharomyces pombe genome sequencing project (http://www. sanger.ac.uk/Projects/S_pombe/) is nearly complete, and this is likely to generate interest in fission yeast as a model system beyond its traditional strongholds in the study of the cell cycle and sexual differentiation. In many fields S. pombe will offer a useful complement to the more widely studied Saccharomyces cerevisiae, but in some areas the impact of S. pombe may well rival or exceed that of this budding yeast in terms of relevance to higher systems. Because of the considerable differences from the S. cerevisiae microtubule cytoskeleton, studying microtubules in S. pombe is likely to enhance the contribution of model systems to our understanding of the principles and practices of microtubule organisation in eukaryotes in general.","authors":"Hagan IM","authors_abbrev":"Hagan IM","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-05-28","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15452114","title":"Genome-wide analysis of pre-mRNA splicing: intron features govern the requirement for the second-step factor, Prp17 in Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"J Biol Chem 2004 Dec 10;279(50):52437-46","abstract":"Removal of pre-mRNA introns is an essential step in eukaryotic genome interpretation. The spliceosome, a ribonucleoprotein performs this critical function; however, precise roles for many of its proteins remain unknown. Genome-wide consequences triggered by the loss of a specific factor can elucidate its function in splicing and its impact on other cellular processes. We have employed splicing-sensitive DNA microarrays, with yeast open reading frames and intron sequences, to detect changes in splicing efficiency and global expression. Comparison of expression profiles, for intron-containing transcripts, among mutants of two second-step factors, Prp17 and Prp22, reveals their unique and shared effects on global splicing. This analysis enabled the identification of substrates dependent on Prp17. We find a significant Prp17 role in splicing of introns which are longer than 200nts and note its dispensability when introns have a < or =13-nucleotide spacing between their branch point nucleotide and 3 ' splice site. In vitro splicing of substrates with varying branch nucleotide to 3 ' splice site distances supports the differential Prp17 dependencies inferred from the in vivo analysis. Furthermore, we tested the predicted dispensability of Prp17 for splicing short introns in the evolutionarily distant yeast, Schizosaccharomyces pombe, where the genome contains predominantly short introns. SpPrp17 was non-essential at all growth temperatures implying that functional evolution of splicing factors is integrated with genome evolution. Together our studies point to a role for budding yeast Prp17 in splicing of subsets of introns and have predictive value for deciphering the functions of splicing factors in gene expression and regulation in other eukaryotes.","authors":"Sapra AK, Arava Y, Khandelia P, Vijayraghavan U","authors_abbrev":"Sapra AK et al.","pubmed_publication_date":"10 Dec 2004","pubmed_entrez_date":"2004-09-29","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37105950","title":"Self-compatibility in yeast is selected for reproductive assurance not population-level compatibility.","citation":"Evolution 2023 Jun 29;77(7):1647-1658","abstract":"In haploid species, sexual reproduction by selfing lacks the common benefits from recombination and is indistinguishable from asexual reproduction at the genetic level. Nevertheless, the evolution of self-compatibility, known as homothallism in organisms with mating types, has occurred hundreds of times in fungi. Two main hypotheses have been proposed for the evolution of homothallism. First, that homothallism offers reproductive assurance, which is especially important when species have an obligatory sexual phase in their lifecycle. Second, that homothallism is associated with population-level compatibility, increasing the chance of outbreeding. Here, we test these hypotheses using the fission yeast Schizosaccharomyces pombe, which is homothallic by mating-type switching, leveraging natural variation for switching efficiency in this species. Combining empirical tests with cellular automaton simulations, we show that homothallism by switching increases mating success of switching genotypes, but does not affect population-level compatibility. Experiments show that outcrossing is actually reduced under homothallism. This reduction in outcrossing is explained by our simulations, which show that due to local mating, gametes that mated through intraclonal selfing are no longer available for outcrossing. Our results suggest that the recurrent evolution of haploid self-compatibility is likely driven by selection for mating assurance, not to increase the potential for outcrossing.","doi":"10.1093/evolut/qpad076","authors":"Nieuwenhuis BPS, Shraim R, Al Ghaithi H","authors_abbrev":"Nieuwenhuis BPS et al.","pubmed_publication_date":"29 Jun 2023","pubmed_entrez_date":"2023-04-27","publication_year":"2023","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2023-04-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11169754","title":"Functional analysis of the Neurospora crassa PZL-1 protein phosphatase by expression in budding and fission yeast.","citation":"Yeast 2001 Jan 30;18(2):115-24","abstract":"The gene pzl-1 from the filamentous fungus Neurospora crassa encodes a putative Ser/Thr protein phosphatase that is reminiscent of the Ppz1/Ppz2 and Pzh1 phosphatases from Saccharomyces cerevisiae and Schizosaccharomyces pombe, respectively. The entire PZL-1 protein, as well as its carboxyl-terminal domain, have been expressed in Escherichia coli as active protein phosphatases. To characterize its cellular role, PZL-1 was also expressed in Sz. pombe and in S. cerevisiae. Expression of PZL-1 in S. cerevisiae from the PPZ1 promoter was able to rescue the altered sensitivity to caffeine and lithium ions of a ppz1 strain. Furthermore, high copy number expression of PZL-1 alleviated the lytic phenotype of a S. cerevisiae slt2/mpk1 mitogen-activated protein (MAP) kinase mutant, similarly to that described for PPZ1, and mimicked the effects of high levels of Ppz1 on cell growth. Expression of PZL-1 in fission yeast from a weak version of the nmt1 promoter fully rescued the growth defect of a pzh1Delta strain in high potassium, but only partially complemented the sodium-hypertolerant phenotype. Strong overexpression of the N. crassa phosphatase in Sz. pombe affected cell growth and morphology. Therefore, PZL-1 appears to fulfil every known function carried out by its S. cerevisiae counterpart, despite the marked divergence in sequence within their NH(2)-terminal moieties.","authors":"Vissi E, Clotet J, de Nadal E, Barceló A, Bakó E, Gergely P, Dombrádi V, Ariño J","authors_abbrev":"Vissi E et al.","pubmed_publication_date":"30 Jan 2001","pubmed_entrez_date":"2001-02-13","publication_year":"2001","canto_session_key":"637c45dc66766a5a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-03-28 13:38:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-03-28 13:38:41","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-03-28"},{"uniquename":"PMID:30646830","title":"Division of labour: tRNA methylation by the NSun2 tRNA methyltransferases Trm4a and Trm4b in fission yeast.","citation":"RNA Biol 2019 Mar;16(3):249-256","abstract":"Enzymes of the cytosine-5 RNA methyltransferase Trm4/NSun2 family methylate tRNAs at C48 and C49 in multiple tRNAs, as well as C34 and C40 in selected tRNAs. In contrast to most other organisms, fission yeast Schizosaccharomyces pombe carries two Trm4/NSun2 homologs, Trm4a (SPAC17D4.04) and Trm4b (SPAC23C4.17). Here, we have employed tRNA methylome analysis to determine the dependence of cytosine-5 methylation (m 5 C) tRNA methylation in vivo on the two enzymes. Remarkably, Trm4a is responsible for all C48 methylation, which lies in the tRNA variable loop, as well as for C34 in tRNA Leu  CAA  and tRNA Pro  CGG , which are at the anticodon wobble position. Conversely, Trm4b methylates C49 and C50, which both lie in the TΨC-stem. Thus, S. pombe show an unusual separation of activities of the NSun2/Trm4 enzymes that are united in a single enzyme in other eukaryotes like humans, mice and Saccharomyces cerevisiae. Furthermore, in vitro activity assays showed that Trm4a displays intron-dependent methylation of C34, whereas Trm4b activity is independent of the intron. The absence of Trm4a, but not Trm4b, causes a mild resistance of S. pombe to calcium chloride.","doi":"10.1080/15476286.2019.1568819","authors":"Müller M, Samel-Pommerencke A, Legrand C, Tuorto F, Lyko F, Ehrenhofer-Murray AE","authors_abbrev":"Müller M et al.","pubmed_publication_date":"Mar 2019","pubmed_entrez_date":"2019-01-17","publication_year":"2019","canto_session_key":"ea89a58770744181","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ann Ehrenhofer-Murray","canto_first_approved_date":"2022-08-17 13:09:20","canto_approved_date":"2022-08-17 13:09:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-08-17 09:28:47","canto_added_date":"2019-01-18 01:15:04","annotation_curators":[{"name":"Ann Ehrenhofer-Murray","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17D4.04","SPAC23C4.17"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-08-17"},{"uniquename":"PMID:15654094","title":"A novel recombination pathway initiated by the Mre11/Rad50/Nbs1 complex eliminates palindromes during meiosis in Schizosaccharomyces pombe.","citation":"Genetics 2005 Mar;169(3):1261-74","abstract":"DNA palindromes are rare in humans but are associated with meiosis-specific translocations. The conserved Mre11/Rad50/Nbs1 (MRN) complex is likely directly involved in processing palindromes through the homologous recombination pathway of DNA repair. Using the fission yeast Schizosaccharomyces pombe as a model system, we show that a 160-bp palindrome (M-pal) is a meiotic recombination hotspot and is preferentially eliminated by gene conversion. Importantly, this hotspot depends on the MRN complex for full activity and reveals a new pathway for generating meiotic DNA double-strand breaks (DSBs), separately from the Rec12 (ortholog of Spo11) pathway. We show that MRN-dependent DSBs are formed at or near the M-pal in vivo, and in contrast to the Rec12-dependent breaks, they appear early, during premeiotic replication. Analysis of mrn mutants indicates that the early DSBs are generated by the MRN nuclease activity, demonstrating the previously hypothesized MRN-dependent breakage of hairpins during replication. Our studies provide a genetic and physical basis for frequent translocations between palindromes in human meiosis and identify a conserved meiotic process that constantly selects against palindromes in eukaryotic genomes.","authors":"Farah JA, Cromie G, Steiner WW, Smith GR","authors_abbrev":"Farah JA et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-01-18","publication_year":"2005","canto_session_key":"8945fdb7cb39b74b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-17 14:42:32","canto_approved_date":"2020-06-29 15:52:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-06-17 14:42:27","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.01","SPCC4G3.05c","SPAC13C5.07","SPAC17A5.11","SPAC1556.01c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-06-17"},{"uniquename":"PMID:28639147","title":"Rethinking cell-cycle-dependent gene expression in Schizosaccharomyces pombe.","citation":"Antonie Van Leeuwenhoek 2017 Nov;110(11):1485-1491","abstract":"Three studies of gene expression during the division cycle of Schizosaccharomyces pombe led to the proposal that a large number of genes are expressed at particular times during the S. pombe cell cycle. Yet only a small fraction of genes proposed to be expressed in a cell-cycle-dependent manner are reproducible in all three published studies. In addition to reproducibility problems, questions about expression amplitudes, cell-cycle timing of expression, synchronization artifacts, and the problem with methods for synchronizing cells must be considered. These problems and complications prompt the idea that caution should be used before accepting the conclusion that there are a large number of genes expressed in a cell-cycle-dependent manner in S. pombe.","doi":"10.1007/s10482-017-0902-y","authors":"Cooper S","authors_abbrev":"Cooper S","pubmed_publication_date":"Nov 2017","pubmed_entrez_date":"2017-06-23","publication_year":"2017","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2017-06-25 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14643426","title":"Cdc7 kinases (DDKs) and checkpoint responses: lessons from two yeasts.","citation":"Mutat Res 2003 Nov 27;532(1-2):21-7","abstract":"Principally characterized for its requirement in the initiation of DNA replication, compelling evidence from two yeast model organisms now points to a central role for the Dbf4/Cdc7 kinase complex in S-phase checkpoint responses. Among the key findings supporting this view are observations that orthologs Dfp1 (Schizosaccharomyces pombe) and Dbf4 (Saccharomyces cerevisiae) interact with equivalent checkpoint kinases Cds1 and Rad53, respectively, and that mutants for Dbf4 and Cdc7 in these species are sensitive to genotoxic agents. Recently, these findings have been extended through mutational analyses of conserved regions in both Dfp1 and Dbf4, leading to the identification of distinct motifs which mediate cellular responses to DNA damage and replication fork arrest. The present review is a comparative survey of data obtained from studies conducted with S. pombe and S. cerevisae, and a consideration of models for the role played by Dbf4/Cdc7 in checkpoint responses.","authors":"Duncker BP, Brown GW","authors_abbrev":"Duncker BP et al.","pubmed_publication_date":"27 Nov 2003","pubmed_entrez_date":"2003-12-04","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3709432","title":"Unique properties of Cd-binding peptides induced in fission yeast, Schizosaccharomyces pombe.","citation":"Environ Health Perspect 1986 Mar;65:13-9","abstract":"Metallothioneins, a class of low molecular weight cysteine-rich proteins that bind heavy metal ions, have been found in various eucaryotic organisms. When fission yeasts are grown in the presence of high concentration of CdCl2, large amounts of Cd-binding peptides (Cd-BP1 and Cd-BP2) are synthesized. Cd-BP1 (MW 4000) contains 4 mole of small unit peptide (cadystin, MW 771), 6 mole of Cd2+, and 1 mole of the labile sulfide; on the other hand, Cd-BP2 (MW 1800) contains 2 mole of cadystin and 2 mole of Cd2+. While Cd-BP2 shows similarities to mammalian Cd-thioneins in UV and CD spectra, Cd-BP1 has a characteristic shoulder at 265 nm in the UV absorption spectrum and shows two marked Cotton bands at 257 nm (negative) and 275 nm (positive). These characteristics of Cd-BP1 are not found in the other Cd-thioneins. When Cd-BP1 is acidified (pH 2.0) and successively neutralized, a shoulder of 265 nm in the UV spectrum and a Cotton band at 275 nm disappear, and the molecular weight changes from 4000 to 1800, with simultaneous loss of the labile sulfide. While the reconstituted complex without labile sulfide showed the characteristics of Cd-BP2, the reconstituted complex in the presence of labile sulfide indicated partial reconstitution of Cd-BP1. The UV and CD spectra differences between reconstituted and native Cd-BP1 suggest the requirement for some additional molecular architecture including another peptide-Cd2+ interaction. Induction of cadystin synthesis is almost exclusive for Cd, but an exception is a small amount of cadystin also induced by the higher concentration of CuCl2 (2.5 mM).(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Hayashi Y, Nakagawa CW, Murasugi A","authors_abbrev":"Hayashi Y et al.","pubmed_publication_date":"Mar 1986","pubmed_entrez_date":"1986-03-01","publication_year":"1986","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23986474","title":"Mutation of a conserved residue enhances the sensitivity of analogue-sensitised kinases to generate a novel approach to the study of mitosis in fission yeast.","citation":"J Cell Sci 2013 Nov 01;126(Pt 21):5052-61","abstract":"The chemical genetic strategy in which mutational enlargement of the ATP-binding site sensitises of a protein kinase to bulky ATP analogues has proved to be an elegant tool for the generation of conditional analogue-sensitive kinase alleles in a variety of model organisms. Here, we describe a novel substitution mutation in the kinase domain that can enhance the sensitivity of analogue-sensitive kinases. Substitution of a methionine residue to phenylalanine in the +2 position after HRDLKxxN motif of the subdomain VIb within the kinase domain markedly increased the sensitivities of the analogue-sensitive kinases to ATP analogues in three out of five S. pombe kinases (i.e. Plo1, Orb5 and Wee1) that harbor this conserved methionine residue. Kinome alignment established that a methionine residue is found at this site in 5-9% of kinases in key model organisms, suggesting that a broader application of this structural modification may enhance ATP analogue sensitivity of analogue-sensitive kinases in future studies. We also show that the enhanced sensitivity of the wee1.as8 allele in a cdc25.22 background can be exploited to generate highly synchronised mitotic and S phase progression at 36°C. Proof-of-principle experiments show how this novel synchronisation technique will prove of great use in the interrogation of the mitotic or S-phase functions through temperature sensitivity mutation of molecules of interest in fission yeast.","doi":"10.1242/jcs.135301","authors":"Tay YD, Patel A, Kaemena DF, Hagan IM","authors_abbrev":"Tay YD et al.","pubmed_publication_date":"01 Nov 2013","pubmed_entrez_date":"2013-08-30","publication_year":"2013","canto_session_key":"1af71a20816f7f92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-11-11 16:11:54","canto_approved_date":"2025-09-03 20:37:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-11 16:11:45","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c","SPBC19C2.05","SPAC24H6.05","SPAC23C11.11","SPAC6F12.15c","SPCC18B5.03","SPAC23C11.16","SPBC336.12c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2022-11-11"},{"uniquename":"PMID:19910462","title":"Histone variant H2A.Z regulates centromere silencing and chromosome segregation in fission yeast.","citation":"J Biol Chem 2010 Jan 15;285(3):1909-18","abstract":"The incorporation of histone variant H2A.Z into nucleosomes plays essential roles in regulating chromatin structure and gene expression. A multisubunit complex containing chromatin remodeling protein Swr1 is responsible for the deposition of H2A.Z in budding yeast and mammals. Here, we show that the JmjC domain protein Msc1 is a novel component of the fission yeast Swr1 complex and is required for Swr1-mediated incorporation of H2A.Z into nucleosomes at gene promoters. Loss of Msc1, Swr1, or H2A.Z results in loss of silencing at centromeres and defective chromosome segregation, although centromeric levels of CENP-A, a centromere-specific histone H3 variant that is required for setting up the chromatin structure at centromeres, remain unchanged. Intriguingly, H2A.Z is required for the expression of another centromere protein, CENP-C, and overexpression of CENP-C rescues centromere silencing defects associated with H2A.Z loss. These results demonstrate the importance of H2A.Z and CENP-C in maintaining a silenced chromatin state at centromeres.","doi":"10.1074/jbc.M109.058487","authors":"Hou H, Wang Y, Kallgren SP, Thompson J, Yates JR, Jia S","authors_abbrev":"Hou H et al.","pubmed_publication_date":"15 Jan 2010","pubmed_entrez_date":"2009-11-14","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC343.11c","SPBP35G2.13c","SPAPB8E5.09","SPBC83.08","SPCC550.12","SPAC11E3.01c","SPBC11B10.10c","SPBC32H8.12c","SPBP23A10.08","SPAC9G1.13c"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:11359928","title":"Identification of two type V myosins in fission yeast, one of which functions in polarized cell growth and moves rapidly in the cell.","citation":"Mol Biol Cell 2001 May;12(5):1367-80","abstract":"We characterized the novel Schizosaccharomyces pombe genes myo4(+) and myo5(+), both of which encode myosin-V heavy chains. Disruption of myo4 caused a defect in cell growth and led to an abnormal accumulation of secretory vesicles throughout the cytoplasm. The mutant cells were rounder than normal, although the sites for cell polarization were still established. Elongation of the cell ends and completion of septation required more time than in wild-type cells, indicating that Myo4 functions in polarized growth both at the cell ends and during septation. Consistent with this conclusion, Myo4 was localized around the growing cell ends, the medial F-actin ring, and the septum as a cluster of dot structures. In living cells, the dots of green fluorescent protein-tagged Myo4 moved rapidly around these regions. The localization and movement of Myo4 were dependent on both F-actin cables and its motor activity but seemed to be independent of microtubules. Moreover, the motor activity of Myo4 was essential for its function. These results suggest that Myo4 is involved in polarized cell growth by moving with a secretory vesicle along the F-actin cables around the sites for polarization. In contrast, the phenotype of myo5 null cells was indistinguishable from that of wild-type cells. This and other data suggest that Myo5 has a role distinct from that of Myo4.","authors":"Motegi F, Arai R, Mabuchi I","authors_abbrev":"Motegi F et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-22","publication_year":"2001","canto_session_key":"d5706346ead68c77","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-03 07:05:00","canto_approved_date":"2021-01-08 12:12:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-02 10:02:10","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.14c","SPBC26H8.07c","SPCC1919.10c","SPAC27F1.02c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2021-01-03"},{"uniquename":"PMID:25245948","title":"Tls1 regulates splicing of shelterin components to control telomeric heterochromatin assembly and telomere length.","citation":"Nucleic Acids Res 2014 Oct;42(18):11419-32","abstract":"Heterochromatin preferentially forms at repetitive DNA elements through RNAi-mediated targeting of histone-modifying enzymes. It was proposed that splicing factors interact with the RNAi machinery or regulate the splicing of repeat transcripts to directly participate in heterochromatin assembly. Here, by screening the fission yeast deletion library, we comprehensively identified factors required for telomeric heterochromatin assembly, including a novel gene tls1+. Purification of Tls1 and mass spectrometry analysis of its interacting proteins show that Tls1 associates with the spliceosome subunit Brr2. RNA sequencing analysis shows that the splicing of a subset of mRNAs are affected in tls1Δ cells, including mRNAs of shelterin components rap1+ and poz1+. Importantly, replacing rap1+ and poz1+ with their cDNAs significantly alleviated heterochromatin defects of tls1Δ cells, suggesting that the missplicing of shelterin components is the cause of such defects, and that splicing factors regulate telomeric heterochromatin through the proper splicing of heterochromatin factors. In addition to its role in telomeric heterochromatin assembly, Tls1-mediated splicing of shelterin mRNAs also regulates telomere length. Given that its human homologue C9ORF78 also associates with the spliceosome and is overexpressed in multiple cancer cell lines, our results suggest that C9ORF78 overexpression might alter the proper splicing of genes during cancer progression.","doi":"10.1093/nar/gku842","authors":"Wang J, Tadeo X, Hou H, Andrews S, Moresco JJ, Yates JR, Nagy PL, Jia S","authors_abbrev":"Wang J et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-09-24","publication_year":"2014","canto_session_key":"6c6a9502b98a3bdb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Songtao Jia","canto_first_approved_date":"2016-07-22 14:06:56","canto_approved_date":"2024-06-07 12:20:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-11-26 23:24:58","canto_added_date":"2014-09-25 00:15:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":68,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Songtao Jia","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC63.11","SPCC24B10.08c","SPBP35G2.10","SPAC26A3.08","SPBC16D10.07c","SPAC664.01c","SPBC2D10.17","SPCC970.07c","SPAC6F6.16c","SPBC28F2.10c","SPCC61.02","SPBC19C2.14","SPBC26H8.01","SPBC1921.07c","SPAC31G5.18c","SPBC215.12","SPBC3E7.14","SPAC2C4.03c","SPAC6F6.17","SPBC24C6.11","SPCC11E10.08","SPCC188.13c","SPAC16A10.07c","SPAC29A4.08c","SPBC29A3.14c","SPBC646.02","SPBC1778.02","SPCC613.12c","SPAC4F8.12c","SPBC1289.11","SPBC428.08c","SPAC1952.05","SPBC83.09c","SPBC800.03","SPBC211.02c","SPCC736.11","SPAC1D4.01","SPAC19G12.13c","SPAC1B3.17","SPAC9.03c","SPBC31F10.11c","SPAC26H5.06"],"gene_count":42,"ltp_gene_count":40,"approved_date":"2016-07-22"},{"uniquename":"PMID:10494627","title":"The petite mutation in yeasts: 50 years on.","citation":"Int Rev Cytol 2000;194:197-238","abstract":"Fifty years ago it was reported that baker's yeast, Saccharomyces cerevisiae, can form \"petite colonie\" mutants when treated with the DNA-targeting drug acriflavin. To mark the jubilee of studies on cytoplasmic inheritance, a review of the early work will be presented together with some observations on current developments. The primary emphasis is to address the questions of how loss of mtDNA leads to lethality (rho 0-lethality) in petite-negative yeasts and how S. cerevisiae tolerates elimination of mtDNA. Recent investigation have revealed that rho 0-lethality can be suppressed by specific mutations in the alpha, beta, and gamma subunits of the mitochondrial F1-ATPase of the petite-negative yeast Kluyveromyces lactis and by the nuclear ptp alleles in Schizosaccharomyces pombe. In contrast, inactivation of genes coding for F1-ATPase alpha and beta subunits and disruption of AAC2, PGS1/PEL1, and YME1 genes in S. cerevisiae convert this petite-positive yeast into a petite-negative form. Studies on nuclear genes affecting dependence on mtDNA have provided important insight into the functions provided by the mitochondrial genome and the maintenance of structural and functional integrity of the mitochondrial inner membrane.","authors":"Chen XJ, Clark-Walker GD","authors_abbrev":"Chen XJ et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"1999-09-24","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16682204","title":"Cdc25: mechanisms of checkpoint inhibition and recovery.","citation":"Trends Cell Biol 2006 Jun;16(6):285-92","abstract":"Members of the eukaryotic Cdc25 phosphatase family are key targets of the Chk1 and Chk2 checkpoint kinases, which inactivate Cdc25 to halt cell cycle progression when DNA is damaged or incompletely replicated. Now, new kinases that phosphorylate and inactivate Cdc25 are being discovered, including MAPKAP kinase-2, a component of the p38 stress-activated MAP kinase pathway. The roles of other kinases, such as cyclin-dependent kinase, Polo and Aurora A kinase, in controlling the localization or the activation of Cdc25, are controversial. Here, we discuss new data that suggests that different Cdc25 isoforms and regulators of Cdc25 are differentially required for normal cell cycle progression and recovery from checkpoint arrest.","authors":"Karlsson-Rosenthal C, Millar JB","authors_abbrev":"Karlsson-Rosenthal C et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-05-10","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11231572","title":"Role of actin polymerization and actin cables in actin-patch movement in Schizosaccharomyces pombe.","citation":"Nat Cell Biol 2001 Mar;3(3):235-44","abstract":"Factors that are involved in actin polymerization, such as the Arp2/3 complex, have been found to be packaged into discrete, motile, actin-rich foci. Here we investigate the mechanism of actin-patch motility in S. pombe using a fusion of green fluorescent protein (GFP) to a coronin homologue, Crn1p. Actin patches are associated with cables and move with rates of 0.32 microm s(-1) primarily in an undirected manner at cell tips and also in a directed manner along actin cables, often away from cell tips. Patches move more slowly or stop when actin polymerization is attenuated by Latrunculin A or in arp3 and cdc3 (profilin) mutants. In a cdc8 (tropomyosin) mutant, actin cables are absent, and patches move with similar speed but in a non-directed manner. Patches are sites of Arp3-dependent F-actin polymerization in vitro. Rapid F-actin turnover rates in vivo indicate that patches and cables are maintained continuously by actin polymerization. Our studies give rise to a model in which actin patches are centres for actin polymerization that drive their own movement on actin cables using Arp2/3-based actin polymerization.","authors":"Pelham RJ, Chang F","authors_abbrev":"Pelham RJ et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-03-07","publication_year":"2001","canto_session_key":"059994796bee610b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-11 13:51:03","canto_approved_date":"2020-03-29 08:03:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-11 13:50:56","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.03","SPAC4A8.15c","SPAC27F1.02c","SPAC23C4.02","SPAPJ760.02c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-08-11"},{"uniquename":"PMID:19351719","title":"A nucleolar protein allows viability in the absence of the essential ER-residing molecular chaperone calnexin.","citation":"J Cell Sci 2009 May 01;122(Pt 9):1342-51","abstract":"In fission yeast, the ER-residing molecular chaperone calnexin is normally essential for viability. However, a specific mutant of calnexin that is devoid of chaperone function (Deltahcd_Cnx1p) induces an epigenetic state that allows growth of Schizosaccharomyces pombe without calnexin. This calnexin-independent (Cin) state was previously shown to be mediated via a non-chromosomal element exhibiting some prion-like features. Here, we report the identification of a gene whose overexpression induces the appearance of stable Cin cells. This gene, here named cif1(+) for calnexin-independence factor 1, encodes an uncharacterized nucleolar protein. The Cin cells arising from cif1(+) overexpression (Cin(cif1) cells) are genetically and phenotypically distinct from the previously characterized Cin(Deltahcd_cnx1) cells, which spontaneously appear in the presence of the Deltahcd_Cnx1p mutant. Moreover, cif1(+) is not required for the induction or maintenance of the Cin(Deltahcd_cnx1) state. These observations argue for different pathways of induction and/or maintenance of the state of calnexin independence. Nucleolar localization of Cif1p is required to induce the Cin(cif1) state, thus suggesting an unexpected interaction between the vital cellular role of calnexin and a function of the nucleolus.","doi":"10.1242/jcs.040949","authors":"Beauregard PB, Guérin R, Turcotte C, Lindquist S, Rokeach LA","authors_abbrev":"Beauregard PB et al.","pubmed_publication_date":"01 May 2009","pubmed_entrez_date":"2009-04-09","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC364.01","SPAC3C7.11c"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:11421285","title":"Fungal ABC proteins: pleiotropic drug resistance, stress response and cellular detoxification.","citation":"Res Microbiol 2001;152(3-4):375-89","abstract":"A number of prominent genetic diseases are caused by mutations in genes encoding ATP-binding cassette (ABC) proteins (Ambudkar, Gottesmann, 1998). Moreover, several mammalian ABC proteins such as P-glycoprotein (P-gp) (Gottesman et al., 1995) and multidrug-resistance-associated proteins (MRPs) (Cole, Deeley, 1998) have been implicated in multidrug resistance (MDR) phenotypes of tumor cells highly resistant to many different anticancer drugs. The characteristics of MDR phenomena include the initial resistance to a single anticancer drug, followed by the development of cross-resistance to many structurally and functionally unrelated drugs. Similar mechanisms of MDR exist in pathogenic fungi, including Candida and Aspergillus (Vanden Bossche et al., 1998), and also in parasites such as Plasmodium and Leishmania (Ambudkar, Gottesmann, 1998), as well as in many bacterial pathogens (Nikaido, 1998). To dissect the mechanisms of MDR development and to elucidate the physiological functions of ABC proteins, many efforts have been made during the past decade. Importantly, yeast orthologues of mammalian disease genes made this unicellular eukaryote an invaluable model system for studies on the molecular mechanisms of ABC proteins, in order to better understand and perhaps improve treatment of ABC gene-related disease. In this review, we provide an overview of ABC proteins and pleiotropic drug resistance in the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe. Furthermore, we discuss the role of ABC proteins in clinical drug resistance development of certain fungal pathogens.","authors":"Wolfger H, Mamnun YM, Kuchler K","authors_abbrev":"Wolfger H et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-06-26","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19546232","title":"Fbh1 limits Rad51-dependent recombination at blocked replication forks.","citation":"Mol Cell Biol 2009 Sep;29(17):4742-56","abstract":"Controlling the loading of Rad51 onto DNA is important for governing when and how homologous recombination is used. Here we use a combination of genetic assays and indirect immunofluorescence to show that the F-box DNA helicase (Fbh1) functions in direct opposition to the Rad52 orthologue Rad22 to curb Rad51 loading onto DNA in fission yeast. Surprisingly, this activity is unnecessary for limiting spontaneous direct-repeat recombination. Instead it appears to play an important role in preventing recombination when replication forks are blocked and/or broken. When overexpressed, Fbh1 specifically reduces replication fork block-induced recombination, as well as the number of Rad51 nuclear foci that are induced by replicative stress. These abilities are dependent on its DNA helicase/translocase activity, suggesting that Fbh1 exerts its control on recombination by acting as a Rad51 disruptase. In accord with this, overexpression of Fbh1 also suppresses the high levels of recombinant formation and Rad51 accumulation at a site-specific replication fork barrier in a strain lacking the Rad51 disruptase Srs2. Similarly overexpression of Srs2 suppresses replication fork block-induced gene conversion events in an fbh1Delta mutant, although an inability to suppress deletion events suggests that Fbh1 has a distinct functionality, which is not readily substituted by Srs2.","doi":"10.1128/MCB.00471-09","authors":"Lorenz A, Osman F, Folkyte V, Sofueva S, Whitby MC","authors_abbrev":"Lorenz A et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-06-24","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20085751","title":"Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast.","citation":"Biochem Biophys Res Commun 2010 Feb 12;392(3):467-72","abstract":"Mitochondrial monothiol glutaredoxins that bind Fe-S cluster are known to participate in Fe-S cluster assembly. However, their precise role has not been well understood. Among three monothiol glutaredoxins (Grx3, 4, and 5) in Schizosaccharomyces pombe only Grx5 resides in mitochondria. The Deltagrx5 mutant requires cysteine on minimal media, and does not grow on non-fermentable carbon source such as glycerol. We found that the mutant is low in the activity of Fe-S enzymes in mitochondria as well as in the cytoplasm. Screening of multi-copy suppressor of growth defects of the mutant identified isa1(+) gene encoding a putative A-type Fe-S scaffold, in addition to mas5(+) and hsc1(+) genes encoding putative chaperones for Fe-S assembly process. Examination of other scaffold and chaperone genes revealed that isa2(+), but not isu1(+) and ssc1(+), complemented the growth phenotype of Deltagrx5 mutant as isa1(+) did, partly through restoration of Fe-S enzyme activities. The mutant also showed a significant decrease in the amount of mitochondrial DNA. We demonstrated that Grx5 interacts in vivo with Isa1 and Isa2 proteins in mitochondria by observing bimolecular fluorescence complementation. These results indicate that Grx5 plays a central role in Fe-S assembly process through interaction with A-type Fe-S scaffold proteins Isa1 and Isa2, each of which is an essential protein in S. pombe, and supports mitochondrial genome integrity as well as Fe-S assembly.","doi":"10.1016/j.bbrc.2010.01.051","authors":"Kim KD, Chung WH, Kim HJ, Lee KC, Roe JH","authors_abbrev":"Kim KD et al.","pubmed_publication_date":"12 Feb 2010","pubmed_entrez_date":"2010-01-21","publication_year":"2010","canto_session_key":"68251eb642dcce3e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-09 18:44:21","canto_approved_date":"2024-10-25 23:08:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-10 14:28:10","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC227.13c","SPCC645.03c","SPAPB2B4.02","SPBC1709.05","SPBC1734.11","SPBC3B9.17","SPAC15E1.09","SPAC664.11"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2018-03-09"},{"uniquename":"PMID:10577390","title":"CDC7 kinase complex as a molecular switch for DNA replication.","citation":"Front Biosci 1999 Dec 01;4:D834-40","abstract":"Cdc7 kinase and its activator Dbf4 protein, originally identified in budding yeast Saccharomyces cerevisiae, are widely conserved in eukaryotes including fission yeast and human. Dbf4-related activators bind and stimulate kinase activity of Cdc7-like catalytic subunit. Its kinase activity is cell cycle-regulated, mainly through availability of the activation subunit whose level increases at G1/S boundary and is maintained at a high level throughout S phase. MCM2 protein is among physiologically important substrates. Genetic studies in fission yeast indicate that Cdc7-related kinase complex also functions in meiosis, uninduced mutagenesis, DNA replication checkpoint signaling and maintenance of chromatin structures during S phase.","authors":"Masai H, Sato N, Takeda T, Arai K","authors_abbrev":"Masai H et al.","pubmed_publication_date":"01 Dec 1999","pubmed_entrez_date":"1999-11-30","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26990381","title":"Lipid Droplets Form from Distinct Regions of the Cell in the Fission Yeast Schizosaccharomyces pombe.","citation":"Traffic 2016 Jun;17(6):657-69","abstract":"Eukaryotic cells store cholesterol/sterol esters (SEs) and triacylglycerols (TAGs) in lipid droplets, which form from the contiguous endoplasmic reticulum (ER) network. However, it is not known if droplets preferentially form from certain regions of the ER over others. Here, we used fission yeast Schizosaccharomyces pombe cells where the nuclear and cortical/peripheral ER domains are distinguishable by light microscopy to show that SE-enriched lipid droplets form away from the nucleus at the cell tips, whereas TAG-enriched lipid droplets form around the nucleus. Sterols localize to the regions of the cells where droplets enriched in SEs are observed. TAG droplet formation around the nucleus appears to be a strong function of diacylglycerol (DAG) homeostasis with Cpt1p, which coverts DAG into phosphatidylcholine and phosphatidylethanolamine localized exclusively to the nuclear ER. Also, Dgk1p, which converts DAG into phosphatidic acid localized strongly to the nuclear ER over the cortical/peripheral ER. We also show that TAG more readily translocates from the ER to lipid droplets than do SEs. The results augment the standard lipid droplet formation model, which has SEs and TAGs flowing into the same nascent lipid droplet regardless of its biogenesis point in the cell.","doi":"10.1111/tra.12394","authors":"Meyers A, Del Rio ZP, Beaver RA, Morris RM, Weiskittel TM, Alshibli AK, Mannik J, Morrell-Falvey J, Dalhaimer P","authors_abbrev":"Meyers A et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-03-19","publication_year":"2016","canto_session_key":"791d831636b06eee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-04-23 10:14:44","canto_approved_date":"2020-04-23 10:14:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-09 13:29:12","canto_added_date":"2016-03-29 00:15:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G7.05","SPBC3D6.05","SPAC24H6.05","SPBC776.14","SPCC1235.15","SPCP1E11.05c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2020-04-23"},{"uniquename":"PMID:26302002","title":"Cwf16p Associating with the Nineteen Complex Ensures Ordered Exon Joining in Constitutive Pre-mRNA Splicing in Fission Yeast.","citation":"PLoS One 2015;10(8):e0136336","abstract":"Exons are ligated in an ordered manner without the skipping of exons in the constitutive splicing of pre-mRNAs with multiple introns. To identify factors ensuring ordered exon joining in constitutive pre-mRNA splicing, we previously screened for exon skipping mutants in Schizosaccharomyces pombe using a reporter plasmid, and characterized three exon skipping mutants named ods1 (ordered splicing 1), ods2, and ods3, the responsible genes of which encode Prp2/U2AF59, U2AF23, and SF1, respectively. They form an SF1-U2AF59-U2AF23 complex involved in recognition of the branch and 3' splice sites in pre-mRNA. In the present study, we identified a fourth ods mutant, ods4, which was isolated in an exon-skipping screen. The ods4+ gene encodes Cwf16p, which interacts with the NineTeen Complex (NTC), a complex thought to be involved in the first catalytic step of the splicing reaction. We isolated two multi-copy suppressors for the ods4-1 mutation, Srp2p, an SR protein essential for pre-mRNA splicing, and Tif213p, a translation initiation factor, in S. pombe. The overexpression of Srp2p suppressed the exon-skipping phenotype of all ods mutants, whereas Tif213p suppressed only ods4-1, which has a mutation in the translational start codon of the cwf16 gene. We also showed that the decrease in the transcriptional elongation rate induced by drug treatment suppressed exon skipping in ods4-1. We propose that Cwf16p/NTC participates in the early recognition of the branch and 3' splice sites and cooperates with the SF1-U2AF59-U2AF23 complex to maintain ordered exon joining.","doi":"10.1371/journal.pone.0136336","authors":"Sasaki-Haraguchi N, Ikuyama T, Yoshii S, Takeuchi-Andoh T, Frendewey D, Tani T","authors_abbrev":"Sasaki-Haraguchi N et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-08-25","publication_year":"2015","canto_session_key":"9ad8ba2a7f979708","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-26 00:18:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC962.06c","SPBC146.07","SPAC16.02c","SPAC9.13c","SPBC17G9.09","SPAP8A3.06"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PANTHER:PTHR13333","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13G7.11","HGNC:26198"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26301056","title":"Role of Oxidative Stress Response and Trehalose Accumulation in the Longevity of Fission Yeast.","citation":"Jundishapur J Microbiol 2015 Jun;8(6):e16851","abstract":"Glucose is the preferred carbon and energy source in most organisms and plays an active role in the regulation of many biological processes. However, an excess of glucose leads to such undesirable conditions as diabetes and age-related diseases. Since Schizosaccharomyces pombe homologous of many human genes, it offers several advantages for the investigation of the molecular mechanisms underlying human disease and aging studies. We have identified two glucose-repression-resistant mutants (ird5 and ird11) of S. pombe.\nWe aimed to investigate the possible relationship between lifespan extension and oxidative stress response induced by exposure to hydrogen peroxide alongside the trehalose accumulation level by using the two S. pombe mutants (i.e. ird5 and ird11), which are repressed by glucose and are resistant to oxidative stress.\nWe employed trehalose accumulation measurement and colony-forming unit (CFU) counting using the ird mutants in exponential and stationary phases and compared them to the wild type grown in repressed, de-repressed, and stressed conditions to clarify the possible relationship between glucose signaling, oxidative stress response, and lifespan in S. pombe.\nThe lifespan of the ird5 mutant was significantly longer that of either the ird11 mutant or the wild type cells. Under repressed condition, the trehalose content was increased remarkably on the 3rd day of the study in the ird11 mutant and the wild type. Under de-repressed condition, the level of intracellular trehalose was notably increased on the 3rd day in ird11. Under stressed condition, the trehalose level in ird11 was increased on the 3rd day as a pattern similar to that observed in the wild type.\nOur results demonstrated no significant correlation between the ird5 lifespan and the trehalose concentration. Likewise, the correlation between lifespan extension, trehalose accumulation, and cellular resistance to hydrogen peroxide was not significant.","doi":"10.5812/jjm.8(6)2015.16851","authors":"Palabiyik B, Jafari Ghods F","authors_abbrev":"Palabiyik B et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-08-25","publication_year":"2015","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2015-08-26 00:18:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15265040","title":"Structural basis of charge transfer complex formation by riboflavin bound to 6,7-dimethyl-8-ribityllumazine synthase.","citation":"Eur J Biochem 2004 Aug;271(15):3208-14","abstract":"The amino acid residue tryptophan 27 of 6,7-dimethyl-8-ribityllumazine synthase of the yeast Schizosaccharomyces pombe was replaced by tyrosine. The structures of the W27Y mutant protein in complex with riboflavin, the substrate analogue 5-nitroso-6-ribitylamino-2,4(1H,3H)-pyrimidinedione, and the product analogue 6-carboxyethyl-7-oxo-8-ribityllumazine, were determined by X-ray crystallography at resolutions of 2.7-2.8 A. Whereas the indole system of W27 forms a coplanar pi-complex with riboflavin, the corresponding phenyl ring in the W27Y mutant establishes only peripheral contact with the heterocyclic ring system of the bound riboflavin. These findings provide an explanation for the absence of the long wavelength shift in optical absorption spectra of riboflavin bound to the mutant enzyme. The structures of the mutants are important tools for the interpretation of the unusual physical properties of riboflavin in complex with lumazine synthase.","authors":"Koch M, Breithaupt C, GerhardtHaase S, Weber S, Cushman M, Huber R, Bacher A, Fischer M","authors_abbrev":"Koch M et al.","pubmed_publication_date":"Aug 2004","pubmed_entrez_date":"2004-07-22","publication_year":"2004","canto_session_key":"6ac190cbfffb0007","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-06 12:45:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 14:41:07","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-05","pdb_entries":[{"pdb_id":"2a58","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Structure of 6,7-Dimethyl-8-ribityllumazine synthase from Schizosaccharomyces pombe mutant W27Y with bound riboflavin","entry_authors":"Koch M,Breithaupt C,Gerhardt S,Haase I,Weber S,Cushman M,Huber R,Bacher A,Fischer M","entry_authors_abbrev":"Koch M et al.","reference_uniquename":"PMID:15265040","experimental_method":"X-ray","resolution":"2.8"},{"pdb_id":"2a57","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Structure of 6,7-Dimthyl-8-ribityllumazine synthase from Schizosaccharomyces pombe mutant W27Y with bound ligand 6-carboxyethyl-7-oxo-8-ribityllumazine","entry_authors":"Koch M,Breithaupt C,Gerhardt S,Haase I,Weber S,Cushman M,Huber R,Bacher A,Fischer M","entry_authors_abbrev":"Koch M et al.","reference_uniquename":"PMID:15265040","experimental_method":"X-ray","resolution":"2.75"},{"pdb_id":"2a59","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Structure of 6,7-Dimethyl-8-ribityllumazine synthase from Schizosaccharomyces pombe mutant W27Y with bound ligand 5-nitroso-6-ribitylamino-2,4(1H,3H)-pyrimidinedione","entry_authors":"Koch M,Breithaupt C,Gerhardt S,Haase I,Weber S,Cushman M,Huber R,Bacher A,Fischer M","entry_authors_abbrev":"Koch M et al.","reference_uniquename":"PMID:15265040","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:12181326","title":"Characterization of a Schizosaccharomyces pombe strain deleted for a sequence homologue of the human damaged DNA binding 1 (DDB1) gene.","citation":"J Biol Chem 2002 Oct 25;277(43):41183-91","abstract":"Human damaged DNA-binding protein (DDB) is a heterodimer of p48/DDB2 and p127/DDB1 subunits. Mutations in DDB2 are responsible for Xeroderma Pigmentosum group E, but no mutants of mammalian DDB1 have been described. To study DDB1, the Schizosaccharomyces pombe DDB1 sequence homologue (ddb1(+)) was cloned, and a ddb1 deletion strain was constructed. The gene is not essential; however, mutant cells showed a 37% impairment in colony-forming ability, an elongated phenotype, and abnormal nuclei. The ddb1Delta strain was sensitive to UV irradiation, X-rays, methylmethane sulfonate, and thiabendazole, and these sensitivities were compared with those of the well characterized rad13Delta, rhp51Delta, and cds1Delta mutant strains. Ddb1p showed nuclear and nucleolar localization, and the aberrant nuclear structures observed in the ddb1Delta strain suggest a role for Ddb1p in chromosome segregation.","authors":"Zolezzi F, Fuss J, Uzawa S, Linn S","authors_abbrev":"Zolezzi F et al.","pubmed_publication_date":"25 Oct 2002","pubmed_entrez_date":"2002-08-16","publication_year":"2002","canto_session_key":"231f5f6efb2fbea9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-20 13:03:13","canto_approved_date":"2020-06-19 12:51:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-20 13:03:05","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.08c","SPCC18B5.11c","SPAC17H9.10c","SPAC644.14c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-08-20"},{"uniquename":"PMID:18543332","title":"Characterization of a sHsp of Schizosaccharomyces pombe, SpHsp15.8, and the implication of its functional mechanism by comparison with another sHsp, SpHsp16.0.","citation":"Proteins 2009 Jan;74(1):6-17","abstract":"There exist two small heat shock proteins (sHsps) in the fission yeast, Schizosaccharomyces pombe (S. pombe), whose expressions are highly induced by heat stress. We have previously expressed, purified, and characterized one of the sHsps, SpHsp16.0. In this study, we examined the other sHsp, SpHsp15.8. It suppressed the thermal aggregation of citrate synthase (CS) from porcine heart and dithiothreitol-induced aggregation of insulin from bovine pancreas with very high efficiency. Almost one SpHsp15.8 subunit was sufficient to protect one protein molecule from aggregation. Like SpHsp16.0, SpHsp15.8 dissociated into small oligomers and then interacted with denatured substrate proteins. SpHsp16.0 exhibited a clear enthalpy change for denaturation occurring over 60 degrees C in differential scanning calorimetry (DSC). However, we could not observe any significant enthalpy change in the DSC of SpHsp15.8. The difference is likely to be caused by the adhesive characteristics of SpHsp15.8. The oligomer dissociation of SpHsp15.8 and SpHsp16.0 and their interactions with denatured substrate proteins were studied by fluorescence polarization analysis (FPA). Both sHsps exhibited a temperature-dependent decrease of fluorescence polarization, which correlates with the dissociation of large oligomers to small oligomers. The dissociation of the SpHsp15.8 oligomer began at about 35 degrees C and proceeded gradually. On the contrary, the SpHsp16.0 oligomer was stable up to approximately 45 degrees C, but then dissociated into small oligomers abruptly at this temperature. Interestingly, SpHsp16.0 is likely to interact with denatured CS in the dissociated state, while SpHsp15.8 is likely to interact with CS in a large complex. These results suggest that S. pombe utilizes two sHsps that function in different manners, probably to cope with a wide range of temperatures and various denatured proteins.","doi":"10.1002/prot.22132","authors":"Sugino C, Hirose M, Tohda H, Yoshinari Y, Abe T, Giga-Hama Y, Iizuka R, Shimizu M, Kidokoro S, Ishii N, Yohda M","authors_abbrev":"Sugino C et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2008-06-11","publication_year":"2009","canto_session_key":"e3b957e4ca8141d3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-02 19:34:58","canto_approved_date":"2025-08-13 19:04:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-02 19:34:52","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-07-02"},{"uniquename":"PMID:29856841","title":"Genome-wide screen reveals important roles for ESCRT proteins in drug/ion resistance of fission yeast.","citation":"PLoS One 2018;13(6):e0198516","abstract":"To study sodium homeostasis, we performed a genome-wide screen for deletion strains that show resistance to NaCl. We identified 34 NaCl-resistant strains. Among them, the largest group that consists of 10 genes related to membrane trafficking and 7 out of 10 genes are ESCRT proteins which are involved in cargo transportation into luminal vesicles within the multivesicular body. All of the ESCRT related mutants which showed sodium resistance also showed defects in vacuole fusion. To further understand the role of the ESCRT pathway in various ion homeostasis, we examined sensitivity of these ESCRT mutants to various cation salts other than NaCl, including KCl, LiCl, CaCl2, CoCl2, MgCl2, NiSO4 and MnCl2. While these ESCRT mutants showed resistance to LiCl, CoCl2 and MgCl2, they showed sensitivity to KCl, CaCl2, NiSO4 and MnCl2. Then we examined sensitivity of these ESCRT mutants to various drugs which are known to inhibit the growth of fission yeast cells. While these ESCRT mutants were more or equally sensitive to most of the drugs tested as compared to the wild-type cells, they showed resistance to some drugs such as tamoxifen, fluorouracil and amiodarone. These results suggest that the ESCRT pathway plays important roles in drug/ion resistance of fission yeast.","doi":"10.1371/journal.pone.0198516","authors":"Yang Y, Liu Q, Jiang G, Chen S, Zhou L, Sakamoto N, Kuno T, Fang Y, Yao F","authors_abbrev":"Yang Y et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-06-02","publication_year":"2018","canto_session_key":"0e1b57bcd605ab63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yue Fang","canto_first_approved_date":"2018-06-15 14:04:15","canto_approved_date":"2018-06-15 14:04:15","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-06-11 09:17:41","canto_added_date":"2018-06-03 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Yue Fang","community_curator":true,"annotation_count":117,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G6.05c","SPAC4F8.01","SPBC215.14c","SPBC4B4.06","SPAC22A12.06c","SPBC25B2.03","SPAC4G9.11c","SPAC19A8.05c","SPAC57A10.14","SPBC31F10.10c","SPBC1861.07","SPBC28F2.02","SPAC227.15","SPAC30D11.07","SPBC1D7.03","SPAC631.01c","SPAC4G9.10","SPBC16A3.19","SPAC11D3.15","SPAPB1E7.06c","SPAC3H5.12c","SPBC1105.09","SPAC15A10.15","SPBC1718.03","SPBC1778.03c","SPAC1142.07c","SPAC17A2.06c","SPAC3F10.17","SPBC651.05c","SPBC8D2.02c","SPBC3B9.09","SPBC660.07","SPBC16G5.03","SPAC637.10c"],"gene_count":34,"ltp_gene_count":34,"approved_date":"2018-06-15"},{"uniquename":"PMID:14975313","title":"Analysis of genome-wide histone acetylation state and enzyme binding using DNA microarrays.","citation":"Methods Enzymol 2004;376:289-304","abstract":"","authors":"Robyr D, Kurdistani SK, Grunstein M","authors_abbrev":"Robyr D et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-02-21","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26951196","title":"Duplication of the Yeast Spindle Pole Body Once per Cell Cycle.","citation":"Mol Cell Biol 2016 May;36(9):1324-31","abstract":"The yeast spindle pole body (SPB) is the functional equivalent of the mammalian centrosome. Centrosomes and SPBs duplicate exactly once per cell cycle by mechanisms that use the mother structure as a platform for the assembly of the daughter. The conserved Sfi1 and centrin proteins are essential components of the SPB duplication process. Sfi1 is an elongated molecule that has, in its center, 20 to 23 binding sites for the Ca(2+)-binding protein centrin. In the yeastSaccharomyces cerevisiae, all Sfi1 N termini are in contact with the mother SPB whereas the free C termini are distal to it. During S phase and early mitosis, cyclin-dependent kinase 1 (Cdk1) phosphorylation of mainly serine residues in the Sfi1 C termini blocks the initiation of SPB duplication (\"off\" state). Upon anaphase onset, the phosphatase Cdc14 dephosphorylates Sfi1 (\"on\" state) to promote antiparallel and shifted incorporation of cytoplasmic Sfi1 molecules into the half-bridge layer, which thereby elongates into the bridge. The Sfi1 C termini of the two Sfi1 layers localize in the bridge center, whereas the N termini of the newly assembled Sfi1 molecules are distal to the mother SPB. These free Sfi1 N termini then assemble the new SPB in G1phase. Recruitment of Sfi1 molecules into the anaphase SPB and bridge formation were also observed inSchizosaccharomyces pombe, suggesting that the Sfi1 bridge cycle is conserved between the two organisms. Thus, restricting SPB duplication to one event per cell cycle requires only an oscillation between Cdk1 kinase and Cdc14 phosphatase activities. This clockwork regulates the \"on\"/\"off\" state of the Sfi1-centrin receiver.","doi":"10.1128/MCB.00048-16","authors":"Rüthnick D, Schiebel E","authors_abbrev":"Rüthnick D et al.","pubmed_publication_date":"May 2016","pubmed_entrez_date":"2016-03-09","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-03-11 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9829945","title":"Methionine induces sexual development in the fission yeast Schizosaccharomyces pombe via an ste11-dependent signalling pathway.","citation":"J Bacteriol 1998 Dec;180(23):6338-41","abstract":"Methionine added to minimal medium overcomes the repressing effects of ammonium and cyclic AMP (cAMP) on sexual development and efficiently induces mating and sporulation in homothallic strains of Schizosaccharomyces pombe. In heterothallic strains it induces G1 arrest when cells enter stationary phase. We show that methionine reduces the intracellular cAMP pool and induces the expression of at least two cAMP-repressible genes, including fbp1 and ste11. The easiest interpretation of the results is that methionine induces sexual development via a cAMP-dependent ste11 signalling pathway.","authors":"Schweingruber AM, Hilti N, Edenharter E, Schweingruber ME","authors_abbrev":"Schweingruber AM et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1998-11-26","publication_year":"1998","canto_session_key":"819378aa9bbfed84","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-20 14:07:19","canto_approved_date":"2025-03-23 11:52:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 13:55:15","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC56F2.11","SPBC32C12.02","SPBC1198.14c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2013-09-20"},{"uniquename":"PMID:8943330","title":"The fission yeast pmk1+ gene encodes a novel mitogen-activated protein kinase homolog which regulates cell integrity and functions coordinately with the protein kinase C pathway.","citation":"Mol Cell Biol 1996 Dec;16(12):6752-64","abstract":"We have isolated a gene, pmk1+, a third mitogen-activated protein kinase (MAPK) gene homolog from the fission yeast Schizosaccharomyces pombe. The predicted amino acid sequence shows the most homology (63 to 65% identity) to those of budding yeast Saccharomyces Mpk1 and Candida Mkc1. The Pmk1 protein contains phosphorylated tyrosines, and the level of tyrosine phosphorylation was increased in the dsp1 mutant which lacks an attenuating phosphatase for Pmk1. The level of tyrosine phosphorylation appears constant during hypotonic or heat shock treatment. The cells with pmk1 deleted (delta pmk1) are viable but show various defective phenotypes, including cell wall weakness, abnormal cell shape, a cytokinesis defect, and altered sensitivities to cations, such as hypersensitivity to potassium and resistance to sodium. Consistent with a high degree of conservation of amino acid sequence, multicopy plasmids containing the MPK1 gene rescued the defective phenotypes of the delta pmk1 mutant. The frog MAPK gene also suppressed the pmk1 disruptant. The results of genetic analysis indicated that Pmk1 lies on a novel MAPK pathway which does not overlap functionally with the other two MAPK pathways, the Spk1-dependent mating signal pathway and Sty1/Spc1/Phh1-dependent stress-sensing pathway. In Saccharomyces cerevisiae, Mpk1 is involved in cell wall integrity and functions downstream of the protein kinase C homolog. In contrast, in S. pombe, Pmk1 may not act in a linear manner with respect to fission yeast protein kinase C homologs. Interestingly, however, these two pathways are not independent; instead, they regulate cell integrity in a coordinate manner.","authors":"Toda T, Dhut S, Superti-Furga G, Gotoh Y, Nishida E, Sugiura R, Kuno T","authors_abbrev":"Toda T et al.","pubmed_publication_date":"Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_session_key":"bfa0f220c8549343","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-10 12:27:22","canto_approved_date":"2020-01-16 17:19:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-16 07:58:29","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.09c","SPBC1685.01","SPBC12D12.04c","SPAC17G8.14c","SPBC409.07c","SPBC119.08"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-10-10"},{"uniquename":"PMID:10423426","title":"Structural models of the KtrB, TrkH, and Trk1,2 symporters based on the structure of the KcsA K(+) channel.","citation":"Biophys J 1999 Aug;77(2):789-807","abstract":"Three-dimensional computer modeling is used to further investigate the hypothesis forwarded in the accompanying paper of an evolutionary relationship between four related families of K(+) sympoter proteins and the superfamily of K(+) channel proteins. Atomic-scale models are developed for the transmembrane regions of one member from each of the three more distinct symporter families, i.e., a TrkH protein from Escherichia coli, a KtrB protein from Aquifex aeolicus, and a Trk1,2 protein from Schizosaccharomyces pombe. The portions of the four consecutive M1-P-M2 motifs in the symporters that can be aligned with K(+) channel sequences are modeled directly from the recently determined crystal structure of the KcsA K(+) channel from Streptomyces lividans. The remaining portions are developed using our previously accumulated theoretical modeling criteria and principles. Concurrently, the use of these criteria and principles is further supported by the now verified predictions of our previous K(+) channel modeling efforts and the degree to which they are satisfied by the known structure of the KcsA protein. Thus the observed ability of the portions of the symporter models derived from the KcsA crystal structure to also satisfy the theoretical modeling criteria provides additional support for an evolutionary link with K(+) channel proteins. Efforts to further satisfy the criteria and principles suggest that the symporter proteins from fungi and plants (i.e., Trk1,2 and HKT1) form dimeric and/or tetrameric complexes in the membrane. Furthermore, analysis of the atomic-scale models in relation to the sequence conservation within and between the protein families suggests structural details for previously proposed mechanisms for the linked symport of K(+) with Na(+) and H(+). Suggestions are also given for experiments to test these structures and hypotheses.","authors":"Durell SR, Guy HR","authors_abbrev":"Durell SR et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-07-29","publication_year":"1999","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6278259","title":"Cloning of mitochondrial DNA from the petite negative yeast Schizosaccharomyces pombe in the bacterial plasmid pBR322.","citation":"Mol Gen Genet 1981;184(3):465-70","abstract":"The entire mitochondrial (mt) genome of the yeast Schizosaccharomyces pombe (S. pombe) was cloned in the BamHI site of the Escherichia coli plasmid pBR322. Three lines of evidence demonstrate that the complete mtDNA molecule was amplified without rearrangement or partial loss. First, restriction of the hybrid plasmid with BamHI led to the recovery of two fragments corresponding to the linearized plasmid and the BamHI-cut mtDNA. Second, restriction of cloned and native mtDNA with HindIII revealed identical fragments. Third, mitochondrial ribosomal RNA hybridized to the same HindIII fragments from cloned mtDNA and from mtDNA isolated from mitochondria.","authors":"Del Giudice L","authors_abbrev":"Del Giudice L","pubmed_publication_date":"1981","pubmed_entrez_date":"1981-01-01","publication_year":"1981","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25500221","title":"Balance between exocytosis and endocytosis determines the efficacy of sterol-targeting antibiotics.","citation":"Chem Biol 2014 Dec 18;21(12):1690-9","abstract":"Antifungals targeting membrane ergosterol are longstanding, yet indispensable drugs in clinical use. However, the mechanisms by which the cellular membrane domains recognized by these antibiotics are generated remain largely unknown. Here, we demonstrate that the balance between endocytosis and exocytosis in membrane trafficking is a critical factor in the action of sterol-targeting antibiotics. When fission yeast cells were treated with manumycin A, cellular binding and the action of the antifungals filipin, amphotericin B, and theonellamides, all of which are ergosterol-binders, were abolished. Additionally, manumycin A treatment attenuated Cdc42 activity and inhibited exocytosis, while endocytosis was only moderately suppressed. Similar defects in membrane trafficking could be reproduced by heat shock and genetic perturbation, which also abolished the action of the antibiotics. We propose that exocytosis and endocytosis respectively supply and internalize the specific plasma membrane domains recognized by sterol-targeting antibiotics.","doi":"10.1016/j.chembiol.2014.10.014","authors":"Nishimura S, Tokukura M, Ochi J, Yoshida M, Kakeya H","authors_abbrev":"Nishimura S et al.","pubmed_publication_date":"18 Dec 2014","pubmed_entrez_date":"2014-12-16","publication_year":"2014","canto_session_key":"0455bb4f542045e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shinichi Nishimura","canto_first_approved_date":"2020-11-13 11:41:47","canto_approved_date":"2020-11-14 23:37:30","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-11-11 09:04:33","canto_added_date":"2014-12-18 01:15:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Shinichi Nishimura","community_curator":true,"annotation_count":5,"orcid":"0000-0002-5998-3780","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.03","SPCC23B6.04c","SPBC1289.04c","SPAC23C4.08","SPAC17G6.04c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2020-11-13"},{"uniquename":"PMID:9325304","title":"Mts4, a non-ATPase subunit of the 26 S protease in fission yeast is essential for mitosis and interacts directly with the ATPase subunit Mts2.","citation":"J Biol Chem 1997 Oct 10;272(41):25768-77","abstract":"We have isolated a fission yeast gene, mts4(+), by complementation of a temperature-sensitive mutation and show that it encodes subunit 2 (S2) of the 19 S regulatory complex of the 26 S protease. mts4(+) is an essential gene, and we show that loss of this subunit causes cells to arrest in metaphase, illustrating the importance of S2 for mitosis. The Mts4 protein is 48% identical to S2 of the human 26 S protease, and the lethal phenotype of the null mts4 allele can be rescued by the human cDNA encoding S2. We provide genetic and physical evidence to suggest that the Mts4 protein interacts with the product of the mts2(+) gene, an ATPase which has previously been shown to be subunit 4 of the 26 S protease.","authors":"Wilkinson CR, Wallace M, Seeger M, Dubiel W, Gordon C","authors_abbrev":"Wilkinson CR et al.","pubmed_publication_date":"10 Oct 1997","pubmed_entrez_date":"1997-11-05","publication_year":"1997","canto_session_key":"bc2d8e5591c96dcc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-12 07:13:10","canto_approved_date":"2025-05-19 08:32:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 07:12:59","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP19A11.03c","SPBC4.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-12"},{"uniquename":"EMBL:AU014075","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084844","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.32"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29423858","title":"Random Spore Analysis in Fission Yeast.","citation":"Methods Mol Biol 2018;1721:189-195","abstract":"Random spore analysis (RSA) is a tool that allows for the screening of a large number of meiotic products. It requires only a limited effort, and is often the method of choice for constructing strains with unambiguous genotypes. It is also useful to identify the frequency of rare events. Strains are crossed on a nitrogen-limiting medium for three days. Mated cells are observed under the microscope to check for the presence of ripe asci. To release spores from their ascus, a sample of the cross is taken from the mating plate and resuspended in an enzyme solution overnight at 25-29 °C. Spores are then counted using a hemocytometer before plating an appropriate number. Incubation at the appropriate temperature follows until colonies form.","doi":"10.1007/978-1-4939-7546-4_17","authors":"Escorcia W, Forsburg SL","authors_abbrev":"Escorcia W et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22354040","title":"RPA facilitates telomerase activity at chromosome ends in budding and fission yeasts.","citation":"EMBO J 2012 Apr 18;31(8):2034-46","abstract":"In Saccharomyces cerevisiae, the telomerase complex binds to chromosome ends and is activated in late S-phase through a process coupled to the progression of the replication fork. Here, we show that the single-stranded DNA-binding protein RPA (replication protein A) binds to the two daughter telomeres during telomere replication but only its binding to the leading-strand telomere depends on the Mre11/Rad50/Xrs2 (MRX) complex. We further demonstrate that RPA specifically co-precipitates with yKu, Cdc13 and telomerase. The interaction of RPA with telomerase appears to be mediated by both yKu and the telomerase subunit Est1. Moreover, a mutation in Rfa1 that affects both the interaction with yKu and telomerase reduces the dramatic increase in telomere length of a rif1Δ, rif2Δ double mutant. Finally, we show that the RPA/telomerase association and function are conserved in Schizosaccharomyces pombe. Our results indicate that in both yeasts, RPA directly facilitates telomerase activity at chromosome ends.","doi":"10.1038/emboj.2012.40","authors":"Luciano P, Coulon S, Faure V, Corda Y, Bos J, Brill SJ, Gilson E, Simon MN, Géli V","authors_abbrev":"Luciano P et al.","pubmed_publication_date":"18 Apr 2012","pubmed_entrez_date":"2012-02-23","publication_year":"2012","canto_session_key":"be9521cb5c4791ae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"stephane Coulon","canto_first_approved_date":"2016-09-07 08:47:39","canto_approved_date":"2024-03-29 09:39:38","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-09-05 08:26:35","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"stephane Coulon","community_curator":true,"annotation_count":4,"orcid":"0000-0001-8090-914X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.214","SPBC660.13c","SPBC2D10.13","SPBC1778.02","SPAC19G12.13c","SPBC216.05"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-09-07"},{"uniquename":"PMID:8041618","title":"Genetic and biochemical analysis of the fission yeast ribonucleoprotein particle containing a homolog of Srp54p.","citation":"Nucleic Acids Res 1994 Jul 11;22(13):2557-67","abstract":"Mammalian signal recognition particle (SRP), a complex of six polypeptides and one 7SL RNA molecule, is required for targeting nascent presecretory proteins to the endoplasmic reticulum (ER). Earlier work identified a Schizosaccharomyces pombe homolog of human SRP RNA and showed that it is a component of a particle similar in size and biochemical properties to mammalian SRP. The recent cloning of the gene encoding a fission yeast protein homologous to Srp54p has made possible further characterization of the subunit structure, subcellular distribution, and assembly of fission yeast SRP. S. pombe SRP RNA and Srp54p co-sediment on a sucrose velocity gradient and coimmunoprecipitate, indicating that they reside in the same complex. In vitro assays demonstrate that fission yeast Srp54p binds under stringent conditions to E. coli SRP RNA, which consists essentially of domain IV, but not to the full-length cognate RNA nor to an RNA in which domain III has been deleted in an effort to mirror the structure of bacterial homologs. Moreover, the association of S. pombe Srp54p with SRP RNA in vivo is disrupted by conditional mutations not only in domain IV, which contains its binding site, but in domains I and III, suggesting that the particle may assemble cooperatively. The growth defects conferred by mutations throughout SRP RNA can be suppressed by overexpression of Srp54p, and the degree to which growth is restored correlates inversely with the severity of the reduction in protein binding. Conditional mutations in SRP RNA also reduce its sedimentation with the ribosome/membrane pellet during cell fractionation. Finally, immunoprecipitation under native conditions of an SRP-enriched fraction from [35S]-labeled fission yeast cells suggests that five additional polypeptides are complexed with Srp54p; each of these proteins is similar in size to a constituent of mammalian SRP, implying that the subunit structure of this ribonucleoprotein is conserved over vast evolutionary distances.","authors":"Selinger D, Brennwald P, Althoff S, Reich C, Hann B, Walter P, Wise JA","authors_abbrev":"Selinger D et al.","pubmed_publication_date":"11 Jul 1994","pubmed_entrez_date":"1994-07-11","publication_year":"1994","canto_session_key":"6dc5d866eec6a592","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-08-18 13:46:47","canto_approved_date":"2020-10-22 10:18:24","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-11 15:34:34","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.06c","SPNCRNA.98"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-08-18"},{"uniquename":"PMID:12791993","title":"Equatorial retention of the contractile actin ring by microtubules during cytokinesis.","citation":"Science 2003 Jun 06;300(5625):1569-74","abstract":"In most eukaryotes cytokinesis is brought about by a contractile actin ring located at the division plane. Here, in fission yeast the actin ring was found to be required to generate late-mitotic microtubular structures located at the division plane, and these in turn maintained the medial position of the actin ring. When these microtubular structures were disrupted, the actin ring migrated away from the cell middle in a membrane traffic-dependent manner, resulting in asymmetrical cell divisions that led to genomic instability. We propose that these microtubular structures contribute to a checkpoint control that retains the equatorial position of the ring when progression through cytokinesis is delayed.","authors":"Pardo M, Nurse P","authors_abbrev":"Pardo M et al.","pubmed_publication_date":"06 Jun 2003","pubmed_entrez_date":"2003-06-07","publication_year":"2003","canto_session_key":"5b7414d8bc7f80eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-03-24 18:01:11","canto_approved_date":"2026-02-14 09:58:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-09 15:33:14","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":18,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPBC21.06c","SPCC4B3.15","SPAP8A3.08","SPAC926.03","SPAC1F5.04c","SPCC1739.11c","SPBC19G7.05c","SPBC24C6.07","SPAC4F8.13c","SPBC26H8.07c"],"gene_count":11,"ltp_gene_count":5,"approved_date":"2018-03-24"},{"uniquename":"PMID:18662319","title":"Pgt1, a glutathione transporter from the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2008 Sep;8(6):916-29","abstract":"The Schizosaccharomyces pombe ORF, SPAC29B12.10c, a predicted member of the oligopeptide transporter (OPT) family, was identified as a gene encoding the S. pombe glutathione transporter (Pgt1) by a genetic strategy that exploited the requirement of the cys1aDelta strain of S. pombe (which is defective in cysteine biosynthesis) for either cysteine or glutathione, for growth. Disruption of the ORF in the cys1aDelta strain led to an inability to grow on glutathione as a source of cysteine. Cloning and subsequent biochemical characterization of the ORF revealed that a high-affinity transporter for glutathione (K(m)=63 microM) that was found to be localized to the plasma membrane. The transporter was specific for glutathione, as significant inhibition in glutathione uptake could be observed only by either reduced or oxidized glutathione, or glutathione conjugates, but not by dipeptides or tripeptides. Furthermore, although glu-cys-gly, an analogue of glutathione (gamma-glu-cys-gly), could be utilized as a sulphur source, the growth was not Pgt1 dependent. This further underlined the specificity of this transporter for glutathione. The strong repression of pgt1(+) expression by cysteine suggested a role in scavenging glutathione from the extracellular environment for the maintenance of sulphur homeostasis in this yeast.","doi":"10.1111/j.1567-1364.2008.00423.x","authors":"Thakur A, Kaur J, Bachhawat AK","authors_abbrev":"Thakur A et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-07-30","publication_year":"2008","canto_session_key":"6dc480135e507182","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-03 12:55:15","canto_approved_date":"2023-06-19 13:26:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-10-25 08:15:19","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.12","SPAC29B12.10c","SPBC36.04","SPBC29B5.02c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2017-04-03"},{"uniquename":"PMID:10071224","title":"A Schizosaccharomyces pombe gene, ksg1, that shows structural homology to the human phosphoinositide-dependent protein kinase PDK1, is essential for growth, mating and sporulation.","citation":"Mol Gen Genet 1999 Feb;261(1):177-83","abstract":"Fission yeast (Schizosaccharomyces pombe) requires inositol for growth, mating and sporulation. To define putative genes that are involved in the processing and transduction of the inositol signal, mutants that are temperature sensitive for growth and sporulation were selected on a medium containing non-limiting amounts of inositol. Two such mutants (ksg1-208 and ksg1-358) were analyzed, which are impaired in mating and sporulation at 30 degrees C and undergo growth arrest in the G2 phase of the cell cycle at 35 degrees C. The ksg1 gene was isolated by functional complementation. It maps on the left arm of chromosome II and encodes a putative 592-amino acid protein which exhibits good structural homology to a human 3-phosphoinositide-dependent protein kinase (PDK1) and its rat and Drosophila homologues. The two mutants have the same substitution at amino acid position 159: a glycine residue is replaced by glutamic acid. Deletion of the gene is lethal for haploid cells. We propose that ksg1 is involved in one or several phosphoinositide signalling processes that are responsible for control of the life cycle.","authors":"Niederberger C, Schweingruber ME","authors_abbrev":"Niederberger C et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-03-10","publication_year":"1999","canto_session_key":"d4053c742ad4153d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-10 16:29:02","canto_approved_date":"2026-02-24 07:49:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-26 15:52:13","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC576.15c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-10"},{"uniquename":"PMID:39672961","title":"Metabolic rearrangement enables adaptation of microbial growth rate to temperature shifts.","citation":"Nat Microbiol 2024 Dec 13;","abstract":"Temperature is a key determinant of microbial behaviour and survival in the environment and within hosts. At intermediate temperatures, growth rate varies according to the Arrhenius law of thermodynamics, which describes the effect of temperature on the rate of a chemical reaction. However, the mechanistic basis for this behaviour remains unclear. Here we use single-cell microscopy to show that Escherichia coli exhibits a gradual response to temperature upshifts with a timescale of ~1.5 doublings at the higher temperature. The response was largely independent of initial or final temperature and nutrient source. Proteomic and genomic approaches demonstrated that adaptation to temperature is independent of transcriptional, translational or membrane fluidity changes. Instead, an autocatalytic enzyme network model incorporating temperature-sensitive Michaelis-Menten kinetics recapitulates all temperature-shift dynamics through metabolome rearrangement, resulting in a transient temperature memory. The model successfully predicts alterations in the temperature response across nutrient conditions, diverse E. coli strains from hosts with different body temperatures, soil-dwelling Bacillus subtilis and fission yeast. In sum, our model provides a mechanistic framework for Arrhenius-dependent growth.","doi":"10.1038/s41564-024-01841-4","authors":"Knapp BD, Willis L, Gonzalez C, Vashistha H, Jammal-Touma J, Tikhonov M, Ram J, Salman H, Elias JE, Huang KC","authors_abbrev":"Knapp BD et al.","pubmed_publication_date":"13 Dec 2024","pubmed_entrez_date":"2024-12-13","publication_year":"2024","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2024-12-15 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013457","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9927738","title":"Sequence divergence of the RNA polymerase shared subunit ABC14.5 (Rpb8) selectively affects RNA polymerase III assembly in Saccharomyces cerevisiae.","citation":"Nucleic Acids Res 1999 Feb 15;27(4):1047-55","abstract":"ABC14.5 (Rpb8) is a eukaryotic subunit common to all three nuclear RNA polymerases. In Saccharomyces cerevisiae, ABC14.5 (Rpb8) is essential for cell viability, however its function remains unknown. We have cloned and characterised the Schizosaccharomyces pombe rpb8(+) cDNA. We found that S.pombe rpb8, unlike the similarly diverged human orthologue, cannot substitute for S.cerevisiae ABC14. 5 in vivo. To obtain information on the function of this RNA polymerase shared subunit we have used S.pombe rpb8 as a naturally altered molecule in heterologous expression assays in S.cerevisiae. Amino acid residue differences within the 67 N-terminal residues contribute to the functional distinction of the two yeast orthologues in S.cerevisiae. Overexpression of the S.cerevisiae largest subunit of RNA polymerase III C160 (Rpc1) allows S.pombe rpb8 to functionally replace ABC14.5 in S.cerevisiae, suggesting a specific genetic interaction between the S.cerevisiae ABC14.5 (Rpb8) and C160 subunits. We provide further molecular and biochemical evidence showing that the heterologously expressed S.pombe rpb8 molecule selectively affects RNApolymerase III but not RNA polymerase I complex assembly. We also report the identification of a S.cerevisiae ABC14.5-G120D mutant which affects RNA polymerase III.","authors":"Voutsina A, Riva M, Carles C, Alexandraki D","authors_abbrev":"Voutsina A et al.","pubmed_publication_date":"15 Feb 1999","pubmed_entrez_date":"1999-02-03","publication_year":"1999","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29432562","title":"Loss-of-function and gain-of-function mutations in PPP3CA cause two distinct disorders.","citation":"Hum Mol Genet 2018 Apr 15;27(8):1421-1433","abstract":"Calcineurin is a calcium (Ca2+)/calmodulin-regulated protein phosphatase that mediates Ca2+-dependent signal transduction. Here, we report six heterozygous mutations in a gene encoding the alpha isoform of the calcineurin catalytic subunit (PPP3CA). Notably, mutations were observed in different functional domains: in addition to three catalytic domain mutations, two missense mutations were found in the auto-inhibitory (AI) domain. One additional frameshift insertion that caused premature termination was also identified. Detailed clinical evaluation of the six individuals revealed clinically unexpected consequences of the PPP3CA mutations. First, the catalytic domain mutations and frameshift mutation were consistently found in patients with nonsyndromic early onset epileptic encephalopathy. In contrast, the AI domain mutations were associated with multiple congenital abnormalities including craniofacial dysmorphism, arthrogryposis and short stature. In addition, one individual showed severe skeletal developmental defects, namely, severe craniosynostosis and gracile bones (severe bone slenderness and perinatal fractures). Using a yeast model system, we showed that the catalytic and AI domain mutations visibly result in decreased and increased calcineurin signaling, respectively. These findings indicate that different functional effects of PPP3CA mutations are associated with two distinct disorders and suggest that functional approaches using a simple cellular system provide a tool for resolving complex genotype-phenotype correlations.","doi":"10.1093/hmg/ddy052","authors":"Mizuguchi T, Nakashima M, Kato M, Okamoto N, Kurahashi H, Ekhilevitch N, Shiina M, Nishimura G, Shibata T, Matsuo M, Ikeda T, Ogata K, Tsuchida N, Mitsuhashi S, Miyatake S, Takata A, Miyake N, Hata K, Kaname T, Matsubara Y, Saitsu H, Matsumoto N","authors_abbrev":"Mizuguchi T et al.","pubmed_publication_date":"15 Apr 2018","pubmed_entrez_date":"2018-02-13","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22H10.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24173580","title":"The role of chromosomal retention of noncoding RNA in meiosis.","citation":"Chromosome Res 2013 Dec;21(6-7):665-72","abstract":"Meiosis is a process of fundamental importance for sexually reproducing eukaryotes. During meiosis, homologous chromosomes pair with each other and undergo homologous recombination, ultimately producing haploid sets of recombined chromosomes that will be inherited by the offspring. Compared with the extensive progress that has been made in understanding the molecular mechanisms underlying recombination, how homologous sequences pair with each other is still poorly understood. The diversity of the underlying mechanisms of pairing present in different organisms further increases the complexity of this problem. Involvement of meiosis-specific noncoding RNA in the pairing of homologous chromosomes has been found in the fission yeast Schizosaccharomyces pombe. Although different organisms may have developed other or additional systems that are involved in chromosome pairing, the findings in S. pombe will provide new insights into understanding the roles of noncoding RNA in meiosis.","doi":"10.1007/s10577-013-9389-1","authors":"Ding DQ, Haraguchi T, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-01","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10651902","title":"Rho-dependence of Schizosaccharomyces pombe Pck2.","citation":"Genes Cells 2000 Jan;5(1):17-27","abstract":"In metazoans, the HR1 domain, a motif found in a number of proteins including the protein kinase C-related PRKs, is responsible for an interaction with Rho-GTPases. The structural similarity between the Schizosaccaromyces pombe Pck proteins and the mammalian Rho-dependent protein kinase C-related family, has led us to investigate the relationship between the function of Rho and that of Pck1/2.\nRho1 is shown to interact with the conserved N-terminal HR1 domain of Pck1/2 in vitro and in vivo. Lethal overproduction of Rho1 is neutralized by co-expression of the Pck2 HR1 domain, which by itself compromises growth when overproduced. The Pck2-Rho1 interaction has a profound effect on the steady state expression of Pck2 and this is shown to parallel the immunoprecipitated activity and phosphorylation of Pck2 at its activation loop site. It is further shown that Pck2 becomes localized at the septum, where Rho1 is also located.\nThe results demonstrate that the Pck proteins are Rho1 effectors in fission yeast and that the HR1 domain is a universal motif for the Rho-GTPase interaction. Furthermore, the evidence supports the contention that the yeast Pck1 and Pck2 proteins are primitive protein kinases, which in vertebrates have evolved into the two distinct PKC and PRK families.","authors":"Sayers LG, Katayama S, Nakano K, Mellor H, Mabuchi I, Toda T, Parker PJ","authors_abbrev":"Sayers LG et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-29","publication_year":"2000","canto_session_key":"2c526ab305f015c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-27 16:11:50","canto_approved_date":"2022-11-07 17:53:23","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2020-11-27 16:11:42","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.04","SPAC17G8.14c","SPBC12D12.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-11-27"},{"uniquename":"PMID:41560553","title":"Investigations into fission yeast chromosome size determinants.","citation":"J Cell Sci 2026 Jan 21;","abstract":"Mitotic chromosome dimensions differ between species, and they differ between developmental stages within an organism. The physiological determinants of chromosome size remain poorly understood. Here, we investigate chromosome size determinants in the fission yeast Schizosaccharomyces pombe. Super-resolution microscopy and semi-automated measurements reveal that cell or nuclear volume in interphase, or the time spent in mitosis (both previously proposed chromosome size determinants), have little influence on resultant chromosome dimensions. Instead, levels of the chromosomal condensin complex affect chromosome size, with increasing condensin levels resulting in more compact, thinner and shorter, chromosomes. Our observations inform the understanding of how chromosome dimensions are controlled in an organism. They suggest that a chromosome-intrinsic mechanism sets chromosome size, more so than the environment in which chromosomes find themselves in.","doi":"10.1242/jcs.264569","authors":"Wu PS, Fallesen T, Uhlmann F","authors_abbrev":"Wu PS et al.","pubmed_publication_date":"21 Jan 2026","pubmed_entrez_date":"2026-01-21","publication_year":"2026","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2026-01-22 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23859867","title":"A novel mutation in HPRT1 gene causing variant form of Lesch-Nyhan disease.","citation":"Pediatr Neurol 2013 Aug;49(2):e5-7","abstract":"","doi":"10.1016/j.pediatrneurol.2013.03.012","authors":"Borlot F, Aquino CC, Zoratti SR, de Araújo JD, Kulikowski LD, Kim CA","authors_abbrev":"Borlot F et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-07-18","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C11.13c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPOXA1SP3","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11483012","title":"Expression of a VEGF-like protein from Parapoxvirus ovis in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Protein Expr Purif 2001 Aug;22(3):479-83","abstract":"We report on the expression of a VEGF-like protein encoded by Parapoxvirus ovis in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. We show that a lysine residue at amino acid position 2 (K2) is an important determinant for the stability of this protein in S. cerevisiae. Replacement of K2 by an arginine results in stabilization of the protein. This observation suggests that this lysine may be a target for ubiquitinylation, which is a prerequisite for proteasome-mediated protein degradation. Interestingly, in S. pombe the lysine (K2) has no influence on the stability of the protein. This result indicates that the two yeast species exhibit significant differences in their protein degradation pathways.","authors":"Kettner K, Friederichs S, Schlapp T, Rödel G","authors_abbrev":"Kettner K et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-08-03","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12855726","title":"Different roles for the stress-activated protein kinase pathway in the regulation of trehalose metabolism in Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 2003 Jul;149(Pt 7):1745-1752","abstract":"The Wis1p-Sty1p mitogen-activated protein kinase cascade is a major signalling system in the fission yeast Schizosaccharomyces pombe for a wide range of stress responses. It is known that trehalose functions as a protective metabolite to counteract deleterious effects of environmental stresses. Herein it is reported that the expression of genes related to trehalose metabolism in S. pombe, ntp1(+) (neutral trehalase) and tps1(+) [trehalose-6-phosphate (T6P) synthase], is partially regulated by the Sty1p kinase under salt-induced osmotic stress and conditions of slight oxidative stress and is fully dependent on this kinase under severe oxidative stress. This control is carried out through transcription factors Atf1p/Pcr1p during osmotic stress and through Pap1p during exposure to low levels of oxidative stress. However, all three transcription factors are needed for gene expression under conditions of extreme oxidative stress. In addition, a role for Sty1p in the modulation of post-transcriptional activation of trehalase mediated by Pka1p/Sck1p kinases, as well as in the activity of T6P synthase under such stressful conditions has been demonstrated. These results reveal a novel dual action of the Wis1p-Sty1p pathway in the regulation of trehalose metabolism in fission yeast.","doi":"10.1099/mic.0.26279-0","authors":"Paredes V, Franco A, Soto T, Vicente-Soler J, Gacto M, Cansado J","authors_abbrev":"Paredes V et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-07-12","publication_year":"2003","canto_session_key":"70548d974e6b7ebf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-21 13:12:08","canto_approved_date":"2019-10-29 13:20:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-25 21:55:12","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC21E11.03c","SPBC29B5.01","SPAC328.03","SPBC660.07","SPAC24B11.06c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2014-10-21"},{"uniquename":"PMID:36358992","title":"Multi-Layered Regulations on the Chromatin Architectures: Establishing the Tight and Specific Responses of Fission Yeast  fbp1  Gene Transcription.","citation":"Biomolecules 2022 Nov 05;12(11)","abstract":"Transcriptional regulation is pivotal for all living organisms and is required for adequate response to environmental fluctuations and intercellular signaling molecules. For precise regulation of transcription, cells have evolved regulatory systems on the genome architecture, including the chromosome higher-order structure (e.g., chromatin loops), location of transcription factor (TF)-binding sequences, non-coding RNA (ncRNA) transcription, chromatin configuration (e.g., nucleosome positioning and histone modifications), and the topological state of the DNA double helix. To understand how these genome-chromatin architectures and their regulators establish tight and specific responses at the transcription stage, the fission yeast  fbp1  gene has been analyzed as a model system for decades. The fission yeast  fbp1  gene is tightly repressed in the presence of glucose, and this gene is induced by over three orders of magnitude upon glucose starvation with a cascade of multi-layered regulations on various levels of genome and chromatin architecture. In this review article, we summarize the multi-layered transcriptional regulatory systems revealed by the analysis of the fission yeast  fbp1  gene as a model system.","doi":"10.3390/biom12111642","authors":"Asada R, Hirota K","authors_abbrev":"Asada R et al.","pubmed_publication_date":"05 Nov 2022","pubmed_entrez_date":"2022-11-11","publication_year":"2022","canto_session_key":"d6ace7c1f6f32f92","canto_annotation_status":"APPROVED","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_first_approved_date":"2022-11-28 16:36:12","canto_approved_date":"2022-11-28 16:38:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-26 10:46:46","canto_added_date":"2022-11-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F12.02","SPBC3B8.02","SPBC725.11c","SPAC24B11.06c","SPBC29B5.01","SPBC215.04","SPBC1D7.02c","SPBC32H8.07","SPAC18B11.10","SPCC1753.02c","SPAC630.14c","SPBC1198.14c","SPBC19C7.03","SPAC23H3.13c","SPAC23C11.08","SPAC8C9.03","SPBC106.10"],"gene_count":17,"ltp_gene_count":0,"approved_date":"2022-11-28"},{"uniquename":"EMBL:U06929","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33496728","title":"Molecular organization of cytokinesis node predicts the constriction rate of the contractile ring.","citation":"J Cell Biol 2021 Mar 01;220(3)","abstract":"The molecular organization of cytokinesis proteins governs contractile ring function. We used single molecule localization microscopy in live cells to elucidate the molecular organization of cytokinesis proteins and relate it to the constriction rate of the contractile ring. Wild-type fission yeast cells assemble contractile rings by the coalescence of cortical proteins complexes called nodes whereas cells without Anillin/Mid1p (Δmid1) lack visible nodes yet assemble contractile rings competent for constriction from the looping of strands. We leveraged the Δmid1 contractile ring assembly mechanism to determine how two distinct molecular organizations, nodes versus strands, can yield functional contractile rings. Contrary to previous interpretations, nodes assemble in Δmid1 cells. Our results suggest that Myo2p heads condense upon interaction with actin filaments and an excess number of Myo2p heads bound to actin filaments hinders constriction thus reducing the constriction rate. Our work establishes a predictive correlation between the molecular organization of nodes and the behavior of the contractile ring.","doi":"10.1083/jcb.202008032","authors":"Bellingham-Johnstun K, Anders EC, Ravi J, Bruinsma C, Laplante C","authors_abbrev":"Bellingham-Johnstun K et al.","pubmed_publication_date":"01 Mar 2021","pubmed_entrez_date":"2021-01-26","publication_year":"2021","canto_session_key":"28418babe512a732","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Caroline Laplante","canto_first_approved_date":"2021-07-27 15:40:56","canto_approved_date":"2023-03-02 05:59:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-30 14:42:01","canto_added_date":"2021-01-28 01:15:06","annotation_curators":[{"name":"Caroline Laplante","community_curator":true,"annotation_count":21,"orcid":"0000-0001-8980-0271","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAC1F5.04c","SPAC4A8.05c","SPCC895.05","SPAC20G8.05c","SPCC4B3.15","SPBC1215.02c","SPAC4F8.13c"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2021-07-27"},{"uniquename":"PMID:10775038","title":"Binding of 14-3-3beta to the carboxyl terminus of Wee1 increases Wee1 stability, kinase activity, and G2-M cell population.","citation":"Cell Growth Differ 2000 Apr;11(4):211-9","abstract":"Wee1 protein kinase plays an important regulatory role in cell cycle progression. It inhibits Cdc-2 activity by phosphorylating Tyr15 and arrests cells at G2-M phase. In an attempt to understand Wee1 regulation during cell cycle, yeast two-hybrid screening was used to identify Wee1-binding protein(s). Five of the eight positive clones identified encode 14-3-3beta. In vivo binding assay in 293 cells showed that both full-length and NH2-terminal truncated Wee1 bind with 14-3-3beta. The 14-3-3beta binding site was mapped to a COOH-terminal consensus motif, RSVSLT (codons 639 to 646). Binding with 14-3-3beta increases the protein level of full-length Wee1 but not of the truncated Wee1. Accompanying the protein level increases, the kinase activity of Wee1 also increases when coexpressed with 14-3-3beta. Increased Wee1 protein level/enzymatic activity is accountable, at least in part, to an increased Wee1 protein half-life when coexpressed with 14-3-3beta. The protein half-life of the NH2-terminal truncated Wee1 is much longer than that of the full-length protein and is not affected by 14-3-3beta cotransfection. Biologically, 14-3-3beta/Wee1 coexpression increases the cell population at G2-M phase. Thus, Wee1 binding with 14-3-3beta increases its biochemical activity as well as its biological function. The finding reveals a novel mechanism by which 14-3-3 regulates G2-M arrest and suggests that the NH2-terminal domain of Wee1 contains a negative regulatory sequence that determines Wee1 stability.","authors":"Wang Y, Jacobs C, Hook KE, Duan H, Booher RN, Sun Y","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-04-25","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD141","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16002618","title":"The kinesin Klp2 mediates polarization of interphase microtubules in fission yeast.","citation":"Science 2005 Jul 08;309(5732):297-300","abstract":"Fission yeast (Schizosaccharomyces pombe) cells grow longitudinally in a manner dependent on a polarized distribution of their interphase microtubules. We found that this distribution required sliding of microtubules toward the cell center along preexisting microtubules. This sliding was mediated by the minus end-directed kinesin motor Klp2, which helped microtubules to become properly organized with plus ends predominantly oriented toward the cell ends and minus ends toward the cell center. Thus, interphase microtubules in the fission yeast require motor activities for their proper organization.","authors":"Carazo-Salas RE, Antony C, Nurse P","authors_abbrev":"Carazo-Salas RE et al.","pubmed_publication_date":"08 Jul 2005","pubmed_entrez_date":"2005-07-09","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.10"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:1839492","title":"Biosynthesis of beta-glucans in fungi.","citation":"Antonie Van Leeuwenhoek 1991 Aug;60(2):72-81","abstract":"Glucans are the most abundant polysaccharides present in fungi. The present review provides updated information on the structure and synthesis of beta-glucans in fungal cells. Synthesis of these polymers made up of B1,3 chains with a variable degree of B1,6 branching involves several reactions: initiation, chain elongation and branching, of which the most studied one is the elongation step. This reaction, catalyzed by the so-called glucan synthetases, utilizes UDPG as sugar donor. Properties of glucan synthetases are extremely variable depending on the fungal species, and their developmental stage. Because of the importance of these polysaccharides it is anticipated that comprehension of their mechanism of synthesis, is important for the understanding of cell wall assembly and cell growth and morphogenesis, as well as for the design of specific antifungal drugs.","authors":"Ruiz-Herrera J","authors_abbrev":"Ruiz-Herrera J","pubmed_publication_date":"Aug 1991","pubmed_entrez_date":"1991-08-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20118936","title":"Schizosaccharomyces pombe genome-wide nucleosome mapping reveals positioning mechanisms distinct from those of Saccharomyces cerevisiae.","citation":"Nat Struct Mol Biol 2010 Feb;17(2):251-7","abstract":"Positioned nucleosomes limit the access of proteins to DNA and implement regulatory features encoded in eukaryotic genomes. Here we have generated the first genome-wide nucleosome positioning map for Schizosaccharomyces pombe and annotated transcription start and termination sites genome wide. Using this resource, we found surprising differences from the previously published nucleosome organization of the distantly related yeast Saccharomyces cerevisiae. DNA sequence guides nucleosome positioning differently: for example, poly(dA-dT) elements are not enriched in S. pombe nucleosome-depleted regions. Regular nucleosomal arrays emanate more asymmetrically-mainly codirectionally with transcription-from promoter nucleosome-depleted regions, but promoters harboring the histone variant H2A.Z also show regular arrays upstream of these regions. Regular nucleosome phasing in S. pombe has a very short repeat length of 154 base pairs and requires a remodeler, Mit1, that is conserved in humans but is not found in S. cerevisiae. Nucleosome positioning mechanisms are evidently not universal but evolutionarily plastic.","doi":"10.1038/nsmb.1741","authors":"Lantermann AB, Straub T, Strålfors A, Yuan GC, Ekwall K, Korber P","authors_abbrev":"Lantermann AB et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2010-02-02","publication_year":"2010","canto_session_key":"aa8a7699a277028a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2026-03-06 08:19:33","canto_approved_date":"2026-03-06 08:19:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-03-06 08:19:28","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"file_curator_name":"Pascal Carme","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":657,"orcid":"0009-0003-9059-1333","file_type":"PHAF","file_name":"PMID_20118936_phaf.tsv"}],"genes":["SPAC1D4.14","SPAC19A8.03","SPCC622.04","SPAC343.15","SPAC977.17","SPAC186.05c","SPBC1685.01","SPBC725.12","SPAC10F6.16","SPBC16A3.18","SPCC1442.10c","SPBC776.13","SPCC5E4.04","SPCC18B5.11c","SPBC29A3.17","SPAC56E4.05","SPCC18.16c","SPCC1840.07c","SPCC1442.11c","SPBC887.06c","SPCC1281.04","SPAC16.01","SPCC970.08","SPBC119.04","SPBC776.15c","SPAC1093.01","SPAC13C5.04","SPAC1006.05c","SPAC14C4.12c","SPAC29B12.08","SPCC338.18","SPAC823.06","SPCC364.06","SPAPB2B4.05","SPAC29A4.14c","SPAC3C7.05c","SPAC19A8.05c","SPCC4B3.06c","SPAC16A10.04","SPAC30D11.10","SPAC13C5.01c","SPBC365.15","SPAPB18E9.02c","SPAC26F1.10c","SPBC609.02","SPBC577.07","SPBC36.09","SPCC622.11","SPBC3B9.18c","SPCC63.04","SPAC1834.08","SPAC25B8.18","SPCC553.11c","SPBPB21E7.10","SPBP22H7.03","SPAC16.03c","SPAC17H9.19c","SPCC1223.10c","SPCPB16A4.02c","SPAC24B11.09","SPAC3A12.04c","SPAC922.05c","SPAC24B11.14","SPBC2D10.08c","SPBC16A3.05c","SPBC1718.05","SPCC830.04c","SPBC1709.12","SPACUNK4.09","SPAC31G5.09c","SPCC962.06c","SPBC365.20c","SPAC16E8.05c","SPCP20C8.02c","SPBC1271.12","SPAC1006.09","SPBC1773.12","SPAC18G6.09c","SPCC61.02","SPAC22G7.11c","SPCC1442.12","SPBC1685.06","SPBC3E7.08c","SPBC23E6.10c","SPBC1347.12","SPBC3B9.09","SPBC4F6.09","SPBC28F2.10c","SPAC24C9.04","SPAC458.04c","SPAC22E12.13c","SPAC1B1.02c","SPBC36.10","SPAC4G9.05","SPAC26F1.11","SPAC7D4.09c","SPAC23C11.17","SPAC19G12.11","SPAC17H9.04c","SPAC186.06","SPBC18E5.07","SPAC1782.01","SPCC1620.07c","SPAC227.15","SPAC23C4.18c","SPBC354.07c","SPAC823.03","SPCC1183.11","SPCC1902.01","SPAC23C4.02","SPAC1002.01","SPAPB1A10.14","SPAC3A12.14","SPBC4F6.15c","SPAC4F10.17","SPCC736.15","SPAC2F3.10","SPBC83.18c","SPBC12C2.03c","SPCC4F11.04c","SPAC4F10.18","SPBC14C8.14c","SPAC1751.01c","SPAC1610.01","SPBC713.07c","SPBC83.16c","SPBPB2B2.13","SPBC530.06c","SPAC13G6.15c","SPBC3H7.14","SPAC10F6.07c","SPAC26F1.08c","SPCC297.03","SPBC8E4.04","SPAC11D3.17","SPCC1235.02","SPBC359.02","SPAC10F6.05c","SPAC4A8.03c","SPAC15A10.07","SPAC6F12.06","SPBC2A9.03","SPCC4F11.02","SPCC1281.07c","SPCC550.03c","SPAC19A8.12","SPBC337.04","SPBC14C8.01c","SPAC17G6.09","SPBC8D2.14c","SPAC2C4.08","SPBC902.06","SPAC9E9.15","SPCC1672.02c","SPAC3H1.13","SPAC17G8.07","SPAC8C9.04","SPAC4H3.06","SPBC365.14c","SPAC20G4.05c","SPBC28F2.12","SPCC63.10c","SPAC18G6.01c","SPAC25B8.10","SPCC1259.10","SPBC1773.06c","SPBC36B7.05c","SPAC27D7.05c","SPBC3H7.07c","SPCC16A11.11","SPBC18E5.14c","SPBC337.14","SPCC594.05c","SPBC660.08","SPAC21E11.05c","SPAC22H10.11c","SPAC1039.10","SPBC31F10.05","SPBC1734.04","SPCC1827.02c","SPAC31G5.10","SPBC23G7.16","SPAPJ691.02","SPBC530.04","SPAC1565.01","SPCC417.02","SPBC1E8.05","SPCC794.11c","SPACUNK4.11c","SPBC216.06c","SPAC821.07c","SPAC19B12.08","SPCC962.03c","SPAC2F7.08c","SPBC17D1.01","SPBC1D7.03","SPAC1805.05","SPAC22E12.18","SPAC1F7.07c","SPAC959.04c","SPAC17A2.09c","SPCC16A11.08","SPAC24B11.08c","SPAC22H10.06c","SPAC17H9.18c","SPAC637.13c","SPAC24B11.13","SPBP35G2.10","SPCC622.13c","SPAC24H6.01c","SPAC29B12.06c","SPBC11G11.02c","SPBC365.01","SPAC1687.20c","SPBC11C11.01","SPAC22F3.02","SPBC19C7.11","SPCC4G3.16","SPAC22G7.10","SPBC1271.11","SPAC30.01c","SPAC977.05c","SPAC1952.17c","SPBP4H10.21c","SPBP19A11.04c","SPBC1105.10","SPAC19A8.02","SPBC1A4.09","SPBC1718.06","SPBC1734.09","SPBC409.08","SPAC25A8.01c","SPBC336.14c","SPBC3D6.12","SPBC56F2.08c","SPAC3H1.04c","SPAC22H12.05c","SPAC8E11.03c","SPCC1494.08c","SPCC830.09c","SPAC140.04","SPCC13B11.04c","SPBC16E9.08","SPBC16E9.19","SPBC29A3.21","SPAC2F3.16","SPAC4F10.06","SPBC32H8.02c","SPBC354.04","SPAC3F10.02c","SPCC23B6.05c","SPCC18.17c","SPCC1672.11c","SPBC776.10c","SPCP31B10.02","SPBC21C3.04c","SPAC18G6.15","SPAC24C9.11","SPAC24C9.07c","SPAC56F8.14c","SPBC17G9.05","SPAPB1A10.04c","SPBC1289.10c","SPAC186.01","SPAC30C2.08","SPAC1039.07c","SPBC609.05","SPBC3H7.09","SPAC630.14c","SPCC285.17","SPAC3C7.03c","SPCC1919.13c","SPCC1620.09c","SPBC1289.16c","SPAP27G11.15","SPAC12G12.12","SPAC29A4.06c","SPBC3H7.15","SPAC25H1.09","SPBC30D10.11","SPAC3C7.06c","SPAP11E10.02c","SPAC17G6.05c","SPAC19E9.01c","SPBC17A3.05c","SPAC20G4.04c","SPCC1183.06","SPBC28E12.05","SPAC12B10.10","SPCC622.09","SPBC16E9.01c","SPAPB2B4.07","SPBP23A10.08","SPBP19A11.07c","SPBC14C8.02","SPBC2D10.18","SPAC6G9.16c","SPBC25B2.01","SPCC1919.11","SPBC4B4.12c","SPBC1347.11","SPBC19G7.16","SPBC17A3.01c","SPBC2F12.15c","SPCC63.06","SPBP8B7.08c","SPBC409.12c","SPBC409.21","SPAC12B10.11","SPAC7D4.08","SPCC1223.11","SPBC1778.09","SPCC663.09c","SPCC1739.10","SPCC132.02","SPAC1071.02","SPCC1442.15c","SPAC9E9.12c","SPBC530.08","SPBC21C3.10c","SPAC16E8.03","SPAP27G11.09c","SPAC9.11","SPBC31F10.08","SPAC977.13c","SPCC1739.12","SPCC569.07","SPAC4D7.03","SPAC328.07c","SPAC688.09","SPBC25H2.09","SPBC8D2.09c","SPCC24B10.12","SPAC977.03","SPBC1773.11c","SPBC409.17c","SPCC285.09c","SPCC569.03","SPBP35G2.03c","SPCC622.01c","SPAC1399.02","SPCC584.02","SPBC2D10.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protein and neutral lipid composition of lipid droplets isolated from the fission yeast, Schizosaccharomyces pombe.","citation":"J Microbiol 2017 Feb;55(2):112-122","abstract":"Lipid droplets consist of a core of neutral lipids surrounded by a phospholipid monolayer with bound proteins. Much of the information on lipid droplet function comes from proteomic and lipodomic studies that identify the components of droplets isolated from organisms throughout the phylogenetic tree. Here, we add to that important inventory by reporting lipid droplet factors from the fission yeast, Schizosaccharomyces pombe. Unique to this study was the fact that cells were cultured in three different environments: 1) late log growth phase in glucose-based media, 2) stationary phase in glucosebased media, and 3) late log growth phase in media containing oleic acid. We confirmed colocalization of major factors with lipid droplets using live-cell fluorescent microscopy. We also analyzed droplets from each of the three conditions for sterol ester (SE) and triacylglycerol (TAG) content, along with their respective fatty acid compositions. We identified a previously undiscovered lipid droplet protein, Vip1p, which affects droplet size distribution. The results provide further insight into the workings of these ubiquitous organelles.","doi":"10.1007/s12275-017-6205-1","authors":"Meyers A, Chourey K, Weiskittel TM, Pfiffner S, Dunlap JR, Hettich RL, Dalhaimer P","authors_abbrev":"Meyers A et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2017-01-26","publication_year":"2017","canto_session_key":"d9bffe4e11d9e9d0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-01-27 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15631622","title":"Interactions between Cdc42 and the scaffold protein Scd2: requirement of SH3 domains for GTPase binding.","citation":"Biochem J 2005 May 15;388(Pt 1):177-84","abstract":"The multi-domain protein Scd2 acts as a scaffold upon which the small GTPase Cdc42 (cell division cycle 42), its nucleotide-exchange factor Scd1 and the p21-activated kinase Shk1 assemble to regulate cell polarity and the mating response in fission yeast. In the present study, we show using isothermal titration calorimetry that Scd2 binds two molecules of active GTP-bound Cdc42 simultaneously, but independently of one another. The two binding sites have significantly different affinities, 21 nM and 3 microM, suggesting that they play distinct roles in the Shk1 signalling network. Each of the Cdc42-binding sites includes one of the SH3 (Src homology 3) domains of Scd2. Our data indicate that complex formation does not occur in a conventional manner via the conserved SH3 domain ligand-binding surface. Neither of the isolated SH3 domains is sufficient to interact with the GTPase, and they both require adjacent regions to either stabilize their conformations or contribute to the formation of the Cdc42-binding surface. Furthermore, we show that there is no evidence for an intramolecular PX-SH3 domain interaction, which could interfere with SH3 domain function. This work suggests that SH3 domains might contribute directly to signalling through small GTPases and thereby adds another aspect to the diverse nature of SH3 domains as protein-protein-interaction modules.","authors":"Wheatley E, Rittinger K","authors_abbrev":"Wheatley E et al.","pubmed_publication_date":"15 May 2005","pubmed_entrez_date":"2005-01-06","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22H10.07","SPAC110.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:5541005","title":"Specific staining of wall mannan in yeast cells with fluorescein-conjugated concanavalin A.","citation":"J Bacteriol 1971 Jan;105(1):1-5","abstract":"A procedure is given for the coupling of fluorescein isothiocyanate to concanavalin A, a protein which specifically combines with a variety of polysaccharides, and for the subsequent isolation of the reactive conjugate. This fluorescent conjugate stains Saccharomyces cerevisiae but not Schizosaccharomyces pombe or Rhodotorula glutinis. The cell walls of the latter two organisms do not contain branched homopolymers of alpha-linked mannose. Furthermore, the staining of S. cerevisiae is competitively inhibited by either unlabeled concanavalin A or methyl-alpha-d-manno-pyranoside. On the basis of this evidence, it is concluded that the staining of S. cerevisiae results from the specific interaction of the fluorescein-concanavalin A conjugate with the alpha-mannan present in the cell wall of this yeast.","authors":"Tkacz JS, Cybulska EB, Lampen JO","authors_abbrev":"Tkacz JS et al.","pubmed_publication_date":"Jan 1971","pubmed_entrez_date":"1971-01-01","publication_year":"1971","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22572960","title":"Divergence of mitotic strategies in fission yeasts.","citation":"Nucleus 2012;3(3):220-5","abstract":"The aim of mitosis is to produce two daughter nuclei, each containing a chromosome complement identical to that of the mother nucleus. This can be accomplished through a variety of strategies, with \"open\" and \"closed\" modes of mitosis positioned at the opposite ends of the spectrum and a range of intermediate patterns in between. In the \"closed\" mitosis, the nuclear envelope remains intact throughout the nuclear division. In the \"open\" division type, the envelope of the original nucleus breaks down early in mitosis and reassembles around the segregated daughter genomes. In any case, the nuclear membrane has to remodel to accommodate the mitotic spindle assembly, chromosome segregation and formation of the daughter nuclei. We have recently shown that within the fission yeast clade, the mitotic control of the nuclear surface area may determine the choice between the nuclear envelope breakdown and a fully \"closed\" division. Here we discuss our data and argue that comparative cell biology studies using two fission yeast species, Schizosaccharomyces pombe and Schizosaccharomyces japonicus, could provide unprecedented insights into physiology and evolution of mitosis.","doi":"10.4161/nucl.19514","authors":"Gu Y, Yam C, Oliferenko S","authors_abbrev":"Gu Y et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-05-11","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19693008","title":"Histone H2A.Z cooperates with RNAi and heterochromatin factors to suppress antisense RNAs.","citation":"Nature 2009 Sep 17;461(7262):419-22","abstract":"Eukaryotic transcriptomes are characterized by widespread transcription of noncoding and antisense RNAs, which is linked to key chromosomal processes, such as chromatin remodelling, gene regulation and heterochromatin assembly. However, these transcripts can be deleterious, and their accumulation is suppressed by several mechanisms including degradation by the nuclear exosome. The mechanisms by which cells differentiate coding RNAs from transcripts targeted for degradation are not clear. Here we show that the variant histone H2A.Z, which is loaded preferentially at the 5' ends of genes by the Swr1 complex containing a JmjC domain protein, mediates suppression of antisense transcripts in the fission yeast Schizosaccharomyces pombe genome. H2A.Z is partially redundant in this regard with the Clr4 (known as SUV39H in mammals)-containing heterochromatin silencing complex that is also distributed at euchromatic loci, and with RNA interference component Argonaute (Ago1). Loss of Clr4 or Ago1 alone has little effect on antisense transcript levels, but cells lacking either of these factors and H2A.Z show markedly increased levels of antisense RNAs that are normally degraded by the exosome. These analyses suggest that as well as performing other functions, H2A.Z is a component of a genome indexing mechanism that cooperates with heterochromatin and RNAi factors to suppress read-through antisense transcripts.","doi":"10.1038/nature08321","authors":"Zofall M, Fischer T, Zhang K, Zhou M, Cui B, Veenstra TD, Grewal SI","authors_abbrev":"Zofall M et al.","pubmed_publication_date":"17 Sep 2009","pubmed_entrez_date":"2009-08-21","publication_year":"2009","canto_session_key":"ee65028085190b26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-15 19:36:45","canto_approved_date":"2024-12-28 13:32:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-15 19:36:38","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":62,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC550.12","SPCC364.06","SPBC428.08c","SPCC736.11","SPBC36.05c","SPAC22H10.03c","SPAC1F3.01","SPAC9G1.13c","SPAC12G12.13c","SPAC17G8.07","SPAPB8E5.09","SPAC4H3.02c","SPAC11E3.01c","SPBC2D10.11c","SPCC576.13","SPAC343.11c","SPBC32H8.12c","SPCC622.09","SPBC11B10.10c","SPBP35G2.13c","SPBC29A3.05","SPAC664.01c","SPCC11E10.08","SPBC83.08","SPBP23A10.08"],"gene_count":25,"ltp_gene_count":24,"approved_date":"2024-01-15"},{"uniquename":"PMID:2002498","title":"A large number of tRNA genes are symmetrically located in fission yeast centromeres.","citation":"J Mol Biol 1991 Mar 05;218(1):13-7","abstract":"We report here that the fission yeast centromere regions in the three chromosomes contain no less than 36 symmetrically arranged tRNA-coding sequences, and many of them are located within the inner inverted regions that are thought to be essential for the centromere function. There are 11 different species of tRNA-coding sequences, and four of them are identical to those previously known in this organism. This high-density distribution of tRNA genes in the centromere regions is surprising, as the fission yeast centromeres were thought to form transcriptionally inactive structures.","authors":"Takahashi K, Murakami S, Chikashige Y, Niwa O, Yanagida M","authors_abbrev":"Takahashi K et al.","pubmed_publication_date":"05 Mar 1991","pubmed_entrez_date":"1991-03-05","publication_year":"1991","canto_session_key":"27f9c9aaac396f49","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 10:54:53","canto_approved_date":"2019-01-07 10:54:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 10:54:45","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:28697384","title":"Schizosaccharomyces pombe and Saccharomyces cerevisiae yeasts in sequential fermentations: Effect on phenolic acids of fermented Kei-apple (Dovyalis caffra L.) juice.","citation":"Int J Food Microbiol 2017 Sep 18;257:232-237","abstract":"Kei-apple (Dovyalis caffra) is an evergreen tree indigenous to Southern Africa. The fruit contains high concentrations of l-malic acid, ascorbic acid, and phenolic acids. Kei-apple juice was sequentially inoculated with Schizosaccharomyces pombe and Saccharomyces cerevisiae yeasts. A reference fermentation using only S. cerevisiae was included. The fermentation was monitored by recording mass loss. At the end of fermentation, twelve untrained judges conducted free choice aroma profiling on the fruit wines. The Kei-apple juice and wines were analysed for total titratable acidity, total soluble solids, pH, alcohol, l-malic acid, and phenolic acids. Total titratable acidity was ca. 70% lower in Kei-apple wines produced with S. pombe+S. cerevisiae than in Kei-apple juice. Kei-apple wines produced with S. pombe+S. cerevisiae showed substantially lower concentrations of l-malic acid than Kei-apple wines produced with S. cerevisiae only. Wines produced with S. cerevisiae only proved higher in phenolic acid concentrations than wines produced with S. pombe+S. cerevisiae. Chlorogenic acid was the most abundant phenolic acid measured in the Kei-apple wines, followed by protocatechuic acid. Judges described the Kei-apple wines produced with S. pombe+S. cerevisiae as having noticeable off-odours, while wines produced with S. cerevisiae were described as fresh and fruity. Kei-apple wines (S. pombe+S. cerevisiae and S. cerevisiae) were of comparable vegetative and organic character. Saccharomyces cerevisiae produced Kei-apple wine with increased caffeic, chlorogenic, protocatechuic, and sinapic acids, whereas S. pombe+S. cerevisiae produced Kei-apple wines with increased ferulic, and p-coumaric acids and low l-malic acid.","doi":"10.1016/j.ijfoodmicro.2017.07.004","authors":"Minnaar PP, Jolly NP, Paulsen V, Du Plessis HW, Van Der Rijst M","authors_abbrev":"Minnaar PP et al.","pubmed_publication_date":"18 Sep 2017","pubmed_entrez_date":"2017-07-12","publication_year":"2017","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2017-07-13 00:15:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8740421","title":"Sequence of ptb1, a gene for the beta subunit of the type-II geranylgeranyltransferase from the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 1996 Apr;12(5):479-83","abstract":"We have isolated and sequenced the ptb1 gene from the fission yeast Schizosaccharomyces pombe. Sequence analysis suggests that Ptb1 is the beta subunit of the type-II geranylgeranyltransferase that is responsible for geranylgeranylation of the Rab-like YPT proteins in this yeast.","authors":"Godfrey R, Davey J","authors_abbrev":"Godfrey R et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_session_key":"df20362cf2140621","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:51:33","canto_approved_date":"2018-12-22 20:51:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 20:51:27","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:39660919","title":"Efn1 and Efn2 are extracellular 5'-nucleotidases induced during the fission yeast response to phosphate starvation.","citation":"mBio 2024 Dec 11;:e0299224","abstract":" adapts to phosphate starvation by upregulating the expression of a cell surface acid phosphatase that mobilizes inorganic phosphate from the extracellular milieu, as well as transmembrane transporters that take up inorganic phosphate and glycerophosphocholine. This study identifies two paralogous extracellular 5'-nucleotidase enzymes, Efn1 and Efn2, encoded by genes that are highly transcriptionally induced during acute phosphate starvation, as major proteins secreted into the medium by phosphate-starved fission yeast cells. Secreted Efn1 and Efn2 catalyze the release of inorganic phosphate from all ribonucleoside monophosphates, with a preference for CMP. Secretion of Efn1 and Efn2 enables phosphate-starved fission yeast to thrive by using extracellular CMP as a source of inorganic phosphate. The starvation-induced production of extracellular 5'-nucleotidases adds a new layer of pro-adaptive function during phosphate limitation.","doi":"10.1128/mbio.02992-24","authors":"Innokentev A, Sanchez AM, Monetti M, Schwer B, Shuman S","authors_abbrev":"Innokentev A et al.","pubmed_publication_date":"11 Dec 2024","pubmed_entrez_date":"2024-12-11","publication_year":"2024","canto_session_key":"10ab5798d63d82a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2024-12-30 10:20:42","canto_approved_date":"2026-03-05 21:44:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-12 18:31:18","canto_added_date":"2024-12-12 00:25:05","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":30,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPB2B2.06c","SPAC30D11.01c","SPAC26H5.08c","SPAC14C4.09","SPBC428.03c","SPAC13G6.10c","SPAC1002.13c","SPBP4G3.02","SPAPB1E7.04c","SPAC1039.02","SPBC1105.05","SPAC821.09","SPCC18.01c","SPBC29A10.08"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2024-12-30"},{"uniquename":"PMID:22144913","title":"Widespread cotranslational formation of protein complexes.","citation":"PLoS Genet 2011 Dec;7(12):e1002398","abstract":"Most cellular processes are conducted by multi-protein complexes. However, little is known about how these complexes are assembled. In particular, it is not known if they are formed while one or more members of the complexes are being translated (cotranslational assembly). We took a genomic approach to address this question, by systematically identifying mRNAs associated with specific proteins. In a sample of 31 proteins from Schizosaccharomyces pombe that did not contain RNA-binding domains, we found that ∼38% copurify with mRNAs that encode interacting proteins. For example, the cyclin-dependent kinase Cdc2p associates with the rum1 and cdc18 mRNAs, which encode, respectively, an inhibitor of Cdc2p kinase activity and an essential regulator of DNA replication. Both proteins interact with Cdc2p and are key cell cycle regulators. We obtained analogous results with proteins with different structures and cellular functions (kinesins, protein kinases, transcription factors, proteasome components, etc.). We showed that copurification of a bait protein and of specific mRNAs was dependent on the presence of the proteins encoded by the interacting mRNAs and on polysomal integrity. These results indicate that these observed associations reflect the cotranslational interaction between the bait and the nascent proteins encoded by the interacting mRNAs. Therefore, we show that the cotranslational formation of protein-protein interactions is a widespread phenomenon.","doi":"10.1371/journal.pgen.1002398","authors":"Duncan CD, Mata J","authors_abbrev":"Duncan CD et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-12-07","publication_year":"2011","canto_session_key":"e84411bb9f11adc7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-02-17 15:40:04","canto_approved_date":"2020-02-17 15:40:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-02-10 09:23:49","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC342.04","SPAC6G9.08","SPBC1604.20c","SPAC664.02c","SPAC23D3.09","SPAC1782.01","SPBC29B5.01","SPBC19C7.01","SPBC2D10.12","SPBC16G5.01","SPCC550.12","SPBC14C8.07c","SPAC12G12.03","SPCC16A11.16c","SPAC3C7.12","SPBP23A10.08","SPAC11H11.06","SPBC32F12.09","SPAC21E11.03c","SPBC4.07c","SPAC24B11.06c","SPCC1620.14c","SPAC1250.01","SPBC3B9.08c","SPBC11B10.09","SPAC29B12.01","SPAC1071.06","SPAC19D5.01"],"gene_count":28,"ltp_gene_count":0,"approved_date":"2020-02-17"},{"uniquename":"PMID:15246105","title":"2-pyrones possessing antimicrobial and cytotoxic activities.","citation":"Bioorg Med Chem 2004 Aug 01;12(15):4285-99","abstract":"The 2-pyrone sub-unit is found in a number of natural products possessing broad spectrum biological activity. Such compounds are validated as being capable of binding to specific protein domains and able to exert a remarkable range of biological effects. In an effort to identify synthetic 2-pyrones with interesting biological effects, herein we report the synthesis and biological evaluation of 4-substituted-6-methyl-2-pyrones. Synthetic routes to 4-alkyl/alkenyl/aryl/alkynyl-6-methyl-2-pyrones have been developed utilising Sonogashira, Suzuki and Negishi cross-coupling starting from readily available 4-bromo-6-methyl-2-pyrone. Specific conditions for each organometallic protocol were required for successful cross-coupling. In particular, a triethylamine/acetonitrile--base/solvent mixture was crucial to Sonogashira alkynylation of 4-bromo-6-methyl-2-pyrone, whereas thallium carbonate was a mandatory base for the Suzuki cross-coupling of trialkylboranes. The 2-pyrones demonstrate potent inhibitory activity against Bacillus subtilis, Escherichia coli, Staphylococcus aureus, Schizosaccharomyces pombe and Botrytis cinerea. The growth inhibitory activities of selected 2-pyrones were determined in A2780 human ovarian carcinoma and K562 human chronic myelogenous leukaemia cell lines using an in vitro cell culture system (MTT assay). These studies demonstrate that 4-phenylethynyl-, 4-tetrahydropyranylpropargyl ether- and 4-ethynyl-6-methyl-2-pyrones have excellent potential as a new class of anticancer agents.","authors":"Fairlamb IJ, Marrison LR, Dickinson JM, Lu FJ, Schmidt JP","authors_abbrev":"Fairlamb IJ et al.","pubmed_publication_date":"01 Aug 2004","pubmed_entrez_date":"2004-07-13","publication_year":"2004","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4307779","title":"[Biochemical properties of Schizosaccharomyces pombe depending on culture conditions and on the action of inhibitors. I. Study of phospholipids].","citation":"Biochim Biophys Acta 1969 Jun 10;176(4):789-802","abstract":"","authors":"Deshusses J, Cheneval JP, Posternak T","authors_abbrev":"Deshusses J et al.","pubmed_publication_date":"10 Jun 1969","pubmed_entrez_date":"1969-06-10","publication_year":"1969","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30089114","title":"Heterochromatin and RNAi regulate centromeres by protecting CENP-A from ubiquitin-mediated degradation.","citation":"PLoS Genet 2018 Aug;14(8):e1007572","abstract":"Centromere is a specialized chromatin domain that plays a vital role in chromosome segregation. In most eukaryotes, centromere is surrounded by the epigenetically distinct heterochromatin domain. Heterochromatin has been shown to contribute to centromere function, but the precise role of heterochromatin in centromere specification remains elusive. Centromeres in most eukaryotes, including fission yeast (Schizosaccharomyces pombe), are defined epigenetically by the histone H3 (H3) variant CENP-A. In contrast, the budding yeast Saccharomyces cerevisiae has genetically-defined point centromeres. The transition between regional centromeres and point centromeres is considered as one of the most dramatic evolutionary events in centromere evolution. Here we demonstrated that Cse4, the budding yeast CENP-A homolog, can localize to centromeres in fission yeast and partially substitute fission yeast CENP-ACnp1. But overexpression of Cse4 results in its localization to heterochromatic regions. Cse4 is subject to efficient ubiquitin-dependent degradation in S. pombe, and its N-terminal domain dictates its centromere distribution via ubiquitination. Notably, without heterochromatin and RNA interference (RNAi), Cse4 fails to associate with centromeres. We showed that RNAi-dependent heterochromatin mediates centromeric localization of Cse4 by protecting Cse4 from ubiquitin-dependent degradation. Heterochromatin also contributes to the association of native CENP-ACnp1 with centromeres via the same mechanism. These findings suggest that protection of CENP-A from degradation by heterochromatin is a general mechanism used for centromere assembly, and also provide novel insights into centromere evolution.","doi":"10.1371/journal.pgen.1007572","authors":"Yang J, Sun S, Zhang S, Gonzalez M, Dong Q, Chi Z, Chen YH, Li F","authors_abbrev":"Yang J et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-08-09","publication_year":"2018","canto_session_key":"a4bdcc99861b6595","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-07-01 15:23:34","canto_approved_date":"2025-09-03 15:09:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-26 13:51:57","canto_added_date":"2018-08-10 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c","SPBC1105.17","SPBC428.08c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2021-07-01"},{"uniquename":"PMID:38146786","title":"Schizosaccharomyces versatilis represents a distinct evolutionary lineage of fission yeast.","citation":"Yeast 2023 Dec 26;","abstract":"The fission yeast species Schizosaccharomyces japonicus is currently divided into two varieties-S. japonicus var. japonicus and S. japonicus var. versatilis. Here we examine the var. versatilis isolate CBS5679. The CBS5679 genome shows 88% identity to the reference genome of S. japonicus var. japonicus at the coding sequence level, with phylogenetic analyses suggesting that it has split from the S. japonicus lineage 25 million years ago. The CBS5679 genome contains a reciprocal translocation between chromosomes 1 and 2, together with several large inversions. The products of genes linked to the major translocation are associated with 'metabolism' and 'cellular assembly' ontology terms. We further show that CBS5679 does not generate viable progeny with the reference strain of S. japonicus. Although CBS5679 shares closer similarity to the 'type' strain of var. versatilis as compared to S. japonicus, it is not identical to the type strain, suggesting population structure within var. versatilis. We recommend that the taxonomic status of S. japonicus var. versatilis is raised, with it being treated as a separate species, Schizosaccharomyces versatilis.","doi":"10.1002/yea.3919","authors":"Etherington GJ, Gil EG, Haerty W, Oliferenko S, Nieduszynski CA","authors_abbrev":"Etherington GJ et al.","pubmed_publication_date":"26 Dec 2023","pubmed_entrez_date":"2023-12-26","publication_year":"2023","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2023-12-27 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12427731","title":"Nak1, an essential germinal center (GC) kinase regulates cell morphology and growth in Schizosaccharomyces pombe.","citation":"J Biol Chem 2003 Jan 10;278(2):991-7","abstract":"We have identified and characterized Nak1, a 652- amino acid NH(2)-terminal kinase belonging to the group II germinal center kinase (GCK) family, in Schizosaccharomyces pombe. We found that nak1 is essential for cell proliferation. Furthermore, partial repression of nak1, under regulation of an integrated nmt1 promoter, resulted in an aberrant round cellular morphology, actin and microtubule mislocalization, slow growth, and cell division defects. Overexpression of either a kinase-inactive mutant (Nak1(K39R)) or the non-catalytic domain resulted in similar phenotypes, suggesting dominant-negative effects. By deletion analysis, we mapped the region responsible for this dominant-negative effect to the COOH-terminal 99 residues. Furthermore, we found that deletion of the COOH-terminal 99 residues inhibited Nak1 autophosphorylation, and expression of a partially inactive (Nak1(T171A)) or truncated (Nak1(1-562)) protein only weakly suppressed morphological and growth phenotypes, indicating that both kinase and COOH-terminal regions are important for Nak1 function. GFP-Nak1 localized uniformly throughout the cytoplasm, unlike many other proteins which influence cell polarity that preferentially localize to cell ends. Together, our results implicate Nak1 in the regulation of cell polarity, growth, and division and suggest that the COOH-terminal end plays an important role in the regulation of this kinase.","authors":"Huang TY, Markley NA, Young D","authors_abbrev":"Huang TY et al.","pubmed_publication_date":"10 Jan 2003","pubmed_entrez_date":"2002-11-13","publication_year":"2003","canto_session_key":"508a767204d31a98","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-18 16:03:11","canto_approved_date":"2023-12-27 20:32:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-18 16:03:00","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17F3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-18"},{"uniquename":"PMID:13416191","title":"Utilization of inositol, an essential metabolite for Schizosaccharomyces pombe.","citation":"J Bacteriol 1957 Mar;73(3):318-23","abstract":"","authors":"YARBROUGH HF, CLARK FM","authors_abbrev":"YARBROUGH HF et al.","pubmed_publication_date":"Mar 1957","pubmed_entrez_date":"1957-03-01","publication_year":"1957","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26610878","title":"Diagnosis, Prognosis, and Therapy of Transthyretin Amyloidosis.","citation":"J Am Coll Cardiol 2015 Dec 01;66(21):2451-2466","abstract":"Transthyretin amyloidosis is a fatal disorder that is characterized primarily by progressive neuropathy and cardiomyopathy. It occurs in both a mutant form (with autosomal dominant inheritance) and a wild-type form (with predominant cardiac involvement). This article guides clinicians as to when the disease should be suspected, describes the appropriate diagnostic evaluation for those with known or suspected amyloidosis, and reviews the interventions currently available for affected patients.","doi":"10.1016/j.jacc.2015.09.075","authors":"Gertz MA, Benson MD, Dyck PJ, Grogan M, Coelho T, Cruz M, Berk JL, Plante-Bordeneuve V, Schmidt HHJ, Merlini G","authors_abbrev":"Gertz MA et al.","pubmed_publication_date":"01 Dec 2015","pubmed_entrez_date":"2015-11-28","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC285.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9286671","title":"The prp1+ gene required for pre-mRNA splicing in Schizosaccharomyces pombe encodes a protein that contains TPR motifs and is similar to Prp6p of budding yeast.","citation":"Genetics 1997 Sep;147(1):101-15","abstract":"The prp (pre-mRNA processing) mutants of the fission yeast Schizosaccharomyces pombe have a defect in pre-mRNA splicing and accumulate mRNA precursors at a restrictive temperature. One of the prp mutants, prp1-4, also has a defect in poly(A)+ RNA transport. The prp1+ gene encodes a protein of 906 amino acid residues that contains 19 repeats of 34 amino acids termed tetratrico peptide repeat (TPR) motifs, which were proposed to mediate protein-protein interactions. The amino acid sequence of Prp1p shares 29.6% identity and 50.6% similarity with that of the PRP6 protein of Saccharomyces cerevisiae, which is a component of the U4/U6 snRNP required for spliceosome assembly. No functional complementation was observed between S. pombe prp1+ and S. cerevisiae PRP6. We examined synthetic lethality of prp1-4 with the other known prp mutations in S. pombe. The results suggest that Prp1p interacts either physically or functionally with Prp4p, Prp6p and Prp13p. Interestingly, the prp1+ gene was found to be identical with the zer1+ gene that functions in cell cycle control. These results suggest that Prp1p/Zer1p is either directly or indirectly involved in cell cycle progression and/or poly(A)+ RNA nuclear export, in addition to pre-mRNA splicing.","authors":"Urushiyama S, Tani T, Ohshima Y","authors_abbrev":"Urushiyama S et al.","pubmed_publication_date":"Sep 1997","pubmed_entrez_date":"1997-09-01","publication_year":"1997","canto_session_key":"13cff5989c78e70f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-01 13:13:43","canto_approved_date":"2019-10-01 13:58:34","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-04 16:17:37","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.14","SPBC6B1.07","SPSNRNA.06"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-04-01"},{"uniquename":"PMID:23755256","title":"The Sm complex is required for the processing of non-coding RNAs by the exosome.","citation":"PLoS One 2013;8(6):e65606","abstract":"A key question in the field of RNA regulation is how some exosome substrates, such as spliceosomal snRNAs and telomerase RNA, evade degradation and are processed into stable, functional RNA molecules. Typical feature of these non-coding RNAs is presence of the Sm complex at the 3'end of the mature RNA molecule. Here, we report that in Saccharomyces cerevisiae presence of intact Sm binding site is required for the exosome-mediated processing of telomerase RNA from a polyadenylated precursor into its mature form and is essential for its function in elongating telomeres. Additionally, we demonstrate that the same pathway is involved in the maturation of snRNAs. Furthermore, the insertion of an Sm binding site into an unstable RNA that is normally completely destroyed by the exosome, leads to its partial stabilization. We also show that telomerase RNA accumulates in Schizosaccharomyces pombe exosome mutants, suggesting a conserved role for the exosome in processing and degradation of telomerase RNA. In summary, our data provide important mechanistic insight into the regulation of exosome dependent RNA processing as well as telomerase RNA biogenesis.","doi":"10.1371/journal.pone.0065606","authors":"Coy S, Volanakis A, Shah S, Vasiljeva L","authors_abbrev":"Coy S et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-06-12","publication_year":"2013","canto_session_key":"d25fadf89742cef0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F7.14c","SPBC17D1.03c","SPCC1840.11","SPCC757.08","SPBC26H8.10","SPAC22A12.12c","SPBC115.01c","SPBC32H8.12c","SPBC16G5.10"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:9822592","title":"Localization of the 26S proteasome during mitosis and meiosis in fission yeast.","citation":"EMBO J 1998 Nov 16;17(22):6465-76","abstract":"The 26S proteasome is a large multisubunit complex involved in degrading both cytoplasmic and nuclear proteins. We have investigated the localization of this complex in the fission yeast, Schizosaccharomyces pombe. Immunofluorescence microscopy shows a striking localization pattern whereby the proteasome is found predominantly at the nuclear periphery, both in interphase and throughout mitosis. Electron microscopic analysis revealed a concentration of label near the inner side of the nuclear envelope. The localization of green fluorescent protein (GFP)-tagged 26S proteasomes was analyzed in live cells during mitosis and meiosis. Throughout mitosis the proteasome remained predominantly at the nuclear periphery. During meiosis the proteasome was found to undergo dramatic changes in its localization. Throughout the first meiotic division, the signal is more dispersed over the nucleus. During meiosis II, there was a dramatic re-localization, and the signal became restricted to the area between the separating DNA until the end of meiosis when the signal dispersed before returning to the nuclear periphery during spore formation. These findings strongly imply that the nuclear periphery is a major site of protein degradation in fission yeast both in interphase and throughout mitosis. Furthermore they raise interesting questions as to the spatial organization of protein degradation during meiosis.","authors":"Wilkinson CR, Wallace M, Morphew M, Perry P, Allshire R, Javerzat JP, McIntosh JR, Gordon C","authors_abbrev":"Wilkinson CR et al.","pubmed_publication_date":"16 Nov 1998","pubmed_entrez_date":"1998-11-21","publication_year":"1998","canto_session_key":"7399dd02f679f385","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-04-29 21:57:24","canto_approved_date":"2022-07-22 16:21:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-26 19:58:18","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP19A11.03c","SPCC330.05c","SPAC31G5.13","SPBC119.01"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2019-04-29"},{"uniquename":"EMBL:Y07643","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11237600","title":"Solution structure and dynamics of an open beta-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe.","citation":"J Mol Biol 2001 Feb 16;306(2):275-90","abstract":"The structure and backbone dynamics of a double labelled (15N,13C) monomeric, 23.7 kD phosphoglycerate mutase (PGAM) from Schizosaccharomyces pombe have been investigated in solution using NMR spectroscopy. A set of 3125 NOE-derived distance restraints, 148 restraints representing inferred hydrogen bonds and 149 values of (3)J(HNHalpha) were used in the structure calculation. The mean rmsd from the average structure for all backbone atoms from residues 6-205 in the best 21 calculated structures was 0.59 A. The core of the enzyme includes an open, twisted, six-stranded beta-sheet flanked by four alpha-helices and a short 3(10)-helix. An additional smaller domain contains two short antiparallel beta-strands and a further pair of alpha-helices. The C(alpha) atoms of the S. pombe PGAM may be superimposed on their equivalents in one of the four identical subunits of Saccharomyces cerevisiae PGAM with an rmsd of 1.34 A (0.92 A if only the beta-sheet is considered). Small differences between the two structures are attributable partly to the deletion in the S. pombe sequence of a 25 residue loop involved in stabilising the S. cerevisiae tetramer. Analysis of 15N relaxation parameters indicates that PGAM tumbles isotropically with a rotational correlation time of 8.7 ns and displays a range of dynamic features. Of 178 residues analysed, only 77 could be fitted without invoking terms for fast internal motion or chemical exchange, and out of the remainder, 77 required a chemical exchange term. Significantly, 46 of the slowly exchanging (milli- to microsecond) residues lie in helices, and these account for two-thirds of all analysed helix residues. On the contrary, only one beta-sheet residue required an exchange term. In contrast to other analyses of backbone dynamics reported previously, residues in slow exchange appeared to correlate with architectural features of the enzyme rather than congregating close to ligand binding sites.","authors":"Uhrínová S, Uhrín D, Nairn J, Price NC, Fothergill-Gilmore LA, Barlow PN","authors_abbrev":"Uhrínová S et al.","pubmed_publication_date":"16 Feb 2001","pubmed_entrez_date":"2001-03-10","publication_year":"2001","canto_session_key":"6dbd95d4b86181ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-06 08:19:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-05 22:29:30","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26F1.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-05","pdb_entries":[{"pdb_id":"1fzt","gene_chains":[{"gene_uniquename":"SPAC26F1.06","chain":"A","position":"1-211"}],"title":"SOLUTION STRUCTURE AND DYNAMICS OF AN OPEN B-SHEET, GLYCOLYTIC ENZYME-MONOMERIC 23.7 KDA PHOSPHOGLYCERATE MUTASE FROM SCHIZOSACCHAROMYCES POMBE","entry_authors":"Uhrinova S,Uhrin D,Nairn J,Price NC,Fothergill-Gilmore LA","entry_authors_abbrev":"Uhrinova S et al.","reference_uniquename":"PMID:11237600","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:18657499","title":"How telomerase reaches its end: mechanism of telomerase regulation by the telomeric complex.","citation":"Mol Cell 2008 Jul 25;31(2):153-65","abstract":"The telomerase enzyme, which synthesizes telomeric DNA repeats, is regulated in cis at individual chromosome ends by the telomeric protein/DNA complex in a manner dependent on telomere repeat-array length. A dynamic interplay between telomerase-inhibiting factors bound at duplex DNA repeats and telomerase-promoting ones bound at single-stranded terminal DNA overhangs appears to modulate telomerase activity and to be directly related to the transient deprotection of telomeres. We discuss recent advances on the mechanism of telomerase regulation at chromosome ends in both yeast and mammalian systems.","doi":"10.1016/j.molcel.2008.06.013","authors":"Bianchi A, Shore D","authors_abbrev":"Bianchi A et al.","pubmed_publication_date":"25 Jul 2008","pubmed_entrez_date":"2008-07-29","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32958768","title":"Elucidation of the aberrant 3' splice site selection by cancer-associated mutations on the U2AF1.","citation":"Nat Commun 2020 Sep 21;11(1):4744","abstract":"The accurate exclusion of introns by RNA splicing is critical for the production of mature mRNA. U2AF1 binds specifically to the 3´ splice site, which includes an essential AG dinucleotide. Even a single amino acid mutation of U2AF1 can cause serious disease such as certain cancers or myelodysplastic syndromes. Here, we describe the first crystal structures of wild-type and pathogenic mutant U2AF1 complexed with target RNA, revealing the mechanism of 3´ splice site selection, and how aberrant splicing results from clinically important mutations. Unexpected features of this mechanism may assist the future development of new treatments against diseases caused by splicing errors.","doi":"10.1038/s41467-020-18559-6","authors":"Yoshida H, Park SY, Sakashita G, Nariai Y, Kuwasako K, Muto Y, Urano T, Obayashi E","authors_abbrev":"Yoshida H et al.","pubmed_publication_date":"21 Sep 2020","pubmed_entrez_date":"2020-09-22","publication_year":"2020","canto_session_key":"f355b1e8a0b42353","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-20 08:47:42","canto_approved_date":"2023-03-01 18:45:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-18 17:56:46","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.06","SPBC146.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-02-20","pdb_entries":[{"pdb_id":"7c06","gene_chains":[{"gene_uniquename":"SPBC146.07","chain":"B/E/H/K/N/Q/T/W/Z","position":"93-161"},{"gene_uniquename":"SPAP8A3.06","chain":"A/D/G/J/M/P/S/V/Y","position":"1-216"}],"title":"Crystal structure of yeast U2AF1 complex bound to 3' splice site RNA, 5'-UAGGU.","entry_authors":"Yoshida H,Park SY,Urano T,Obayashi E","entry_authors_abbrev":"Yoshida H et al.","reference_uniquename":"PMID:32958768","experimental_method":"X-ray","resolution":"3.02"},{"pdb_id":"7c07","gene_chains":[{"gene_uniquename":"SPBC146.07","chain":"B/E/H/K/N/Q/T/W/Z","position":"93-161"},{"gene_uniquename":"SPAP8A3.06","chain":"A/D/G/J/M/P/S/V/Y","position":"1-216"}],"title":"Crystal structure of yeast U2AF1 complex bound to 5'-AAGGU RNA.","entry_authors":"Yoshida H,Park SY,Urano T,Obayashi E","entry_authors_abbrev":"Yoshida H et al.","reference_uniquename":"PMID:32958768","experimental_method":"X-ray","resolution":"3.2"},{"pdb_id":"7c08","gene_chains":[{"gene_uniquename":"SPBC146.07","chain":"B/E/H/K/N/Q/T/W/Z","position":"93-161"},{"gene_uniquename":"SPAP8A3.06","chain":"A/D/G/J/M/P/S/V/Y","position":"1-216"}],"title":"Crystal structure of S34Y mutant of yeast U2AF1 complex bound to 3' splice site RNA, 5'-UAGGU.","entry_authors":"Yoshida H,Park SY,Urano T,Obayashi E","entry_authors_abbrev":"Yoshida H et al.","reference_uniquename":"PMID:32958768","experimental_method":"X-ray","resolution":"3.35"}]},{"uniquename":"PMID:10567532","title":"Direct binding and In vivo regulation of the fission yeast p21-activated kinase shk1 by the SH3 domain protein scd2.","citation":"Mol Cell Biol 1999 Dec;19(12):8066-74","abstract":"The Ste20/p21-activated kinase homolog Shk1 is essential for viability and required for normal morphology, mating, and cell cycle control in the fission yeast Schizosaccharomyces pombe. Shk1 is regulated by the p21 G protein Cdc42, which has been shown to form a complex with the SH3 domain protein Scd2 (also called Ral3). In this study, we investigated whether Scd2 plays a role in regulating Shk1 function. We found that recombinant Scd2 and Shk1 interact directly in vitro and that they interact in vivo, as determined by the two-hybrid assay and genetic analyses in fission yeast. The second of two N-terminal SH3 domains of Scd2 is both necessary and sufficient for interaction with Shk1. While full-length Scd2 interacted with only the R1 N-terminal regulatory subdomain of Shk1, a C-terminal deletion mutant of Scd2 interacted with both the R1 and R3 subdomains of Shk1, suggesting that the non-SH3 C-terminal domain of Scd2 may be involved in defining specificity in SH3 binding domain recognition. Overexpression of Scd2 stimulated the autophosphorylation activity of wild-type Shk1 in fission yeast but, consistent with results of genetic analyses, did not stimulate the activity of a Shk1 protein lacking the R1 subdomain. Results of additional two-hybrid experiments suggest that Scd2 may stimulate Shk1 catalytic function, at least in part, by positively modulating protein-protein interaction between Cdc42 and Shk1. We propose that Scd2 functions as an organizing center, or scaffold, for the Cdc42 complex in fission yeast and that it acts in concert with Cdc42 to positively regulate Shk1 function.","authors":"Chang E, Bartholomeusz G, Pimental R, Chen J, Lai H, Wang Lh, Yang P, Marcus S","authors_abbrev":"Chang E et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-11-24","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16E8.09","SPAC17H9.09c","SPAC22H10.07","SPAC110.03","SPBC1D7.05","SPBC1604.14c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:31932509","title":" Schizosaccharomyces pombe  DNA translocases Rrp1 and Rrp2 have distinct roles at centromeres and telomeres that ensure genome stability.","citation":"J Cell Sci 2020 Feb 10;133(3)","abstract":"The regulation of telomere and centromere structure and function is essential for maintaining genome integrity.  Schizosaccharomyces pombe  Rrp1 and Rrp2 are orthologues of  Saccharomyces cerevisiae  Uls1, a SWI2/SNF2 DNA translocase and SUMO-targeted ubiquitin ligase. Here, we show that Rrp1 or Rrp2 overproduction leads to chromosome instability and growth defects, a reduction in global histone levels and mislocalisation of centromere-specific histone Cnp1. These phenotypes depend on putative DNA translocase activities of Rrp1 and Rrp2, suggesting that Rrp1 and Rrp2 may be involved in modulating nucleosome dynamics. Furthermore, we confirm that Rrp2, but not Rrp1, acts at telomeres, reflecting a previously described interaction between Rrp2 and Top2. In conclusion, we identify roles for Rrp1 and Rrp2 in maintaining centromere function by modulating histone dynamics, contributing to the preservation of genome stability during vegetative cell growth.","doi":"10.1242/jcs.230193","authors":"Barg-Wojas A, Muraszko J, Kramarz K, Schirmeisen K, Baranowska G, Carr AM, Dziadkowiec D","authors_abbrev":"Barg-Wojas A et al.","pubmed_publication_date":"10 Feb 2020","pubmed_entrez_date":"2020-01-15","publication_year":"2020","canto_session_key":"96e1d963162e627c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26109598","title":"Genetic instability in budding and fission yeast-sources and mechanisms.","citation":"FEMS Microbiol Rev 2015 Nov;39(6):917-67","abstract":"Cells are constantly confronted with endogenous and exogenous factors that affect their genomes. Eons of evolution have allowed the cellular mechanisms responsible for preserving the genome to adjust for achieving contradictory objectives: to maintain the genome unchanged and to acquire mutations that allow adaptation to environmental changes. One evolutionary mechanism that has been refined for survival is genetic variation. In this review, we describe the mechanisms responsible for two biological processes: genome maintenance and mutation tolerance involved in generations of genetic variations in mitotic cells of both Saccharomyces cerevisiae and Schizosaccharomyces pombe. These processes encompass mechanisms that ensure the fidelity of replication, DNA lesion sensing and DNA damage response pathways, as well as mechanisms that ensure precision in chromosome segregation during cell division. We discuss various factors that may influence genome stability, such as cellular ploidy, the phase of the cell cycle, transcriptional activity of a particular region of DNA, the proficiency of DNA quality control systems, the metabolic stage of the cell and its respiratory potential, and finally potential exposure to endogenous or environmental stress.","doi":"10.1093/femsre/fuv028","authors":"Skoneczna A, Kaniak A, Skoneczny M","authors_abbrev":"Skoneczna A et al.","pubmed_publication_date":"Nov 2015","pubmed_entrez_date":"2015-06-26","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-06-27 00:20:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8878833","title":"M-factor, a farnesylated mating factor from the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1996 Aug;24(3):718-23","abstract":"","authors":"Davey J","authors_abbrev":"Davey J","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_session_key":"cd86e784f964b798","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:45:30","canto_session_submitted_date":"2012-02-27 11:09:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:17409354","title":"The peroxiredoxin Tpx1 is essential as a H2O2 scavenger during aerobic growth in fission yeast.","citation":"Mol Biol Cell 2007 Jun;18(6):2288-95","abstract":"Peroxiredoxins are known to interact with hydrogen peroxide (H(2)O(2)) and to participate in oxidant scavenging, redox signal transduction, and heat-shock responses. The two-cysteine peroxiredoxin Tpx1 of Schizosaccharomyces pombe has been characterized as the H(2)O(2) sensor that transduces the redox signal to the transcription factor Pap1. Here, we show that Tpx1 is essential for aerobic, but not anaerobic, growth. We demonstrate that Tpx1 has an exquisite sensitivity for its substrate, which explains its participation in maintaining low steady-state levels of H(2)O(2). We also show in vitro and in vivo that inactivation of Tpx1 by oxidation of its catalytic cysteine to a sulfinic acid is always preceded by a sulfinic acid form in a covalently linked dimer, which may be important for understanding the kinetics of Tpx1 inactivation. Furthermore, we provide evidence that a strain expressing Tpx1.C169S, lacking the resolving cysteine, can sustain aerobic growth, and we show that small reductants can modulate the activity of the mutant protein in vitro, probably by supplying a thiol group to substitute for cysteine 169.","authors":"Jara M, Vivancos AP, Calvo IA, Moldón A, Sansó M, Hidalgo E","authors_abbrev":"Jara M et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-04-06","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC3F6.03","SPCC576.03c","SPAC7D4.07c","SPAC821.10c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:24828577","title":"Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system.","citation":"PLoS One 2014;9(5):e97774","abstract":"Ergothioneine is a small, sulfur-containing metabolite (229 Da) synthesized by various species of bacteria and fungi, which can accumulate to millimolar levels in tissues or cells (e.g. erythrocytes) of higher eukaryotes. It is commonly marketed as a dietary supplement due to its proposed protective and antioxidative functions. In this study we report the genes forming the two-step ergothioneine biosynthetic pathway in the fission yeast, Schizosaccharomyces pombe. We identified the first gene, egt1+ (SPBC1604.01), by sequence homology to previously published genes from Neurospora crassa and Mycobacterium smegmatis. We showed, using metabolomic analysis, that the Δegt1 deletion mutant completely lacked ergothioneine and its precursors (trimethyl histidine/hercynine and hercynylcysteine sulfoxide). Since the second step of ergothioneine biosynthesis has not been characterized in eukaryotes, we examined four putative homologs (Nfs1/SPBC21D10.11c, SPAC11D3.10, SPCC777.03c, and SPBC660.12c) of the corresponding mycobacterial enzyme EgtE. Among deletion mutants of these genes, only one (ΔSPBC660.12c, designated Δegt2) showed a substantial decrease in ergothioneine, accompanied by accumulation of its immediate precursor, hercynylcysteine sulfoxide. Ergothioneine-deficient strains exhibited no phenotypic defects during vegetative growth or quiescence. To effectively study the role of ergothioneine, we constructed an egt1+ overexpression system by replacing its native promoter with the nmt1+ promoter, which is inducible in the absence of thiamine. We employed three versions of the nmt1 promoter with increasing strength of expression and confirmed corresponding accumulations of ergothioneine. We quantified the intracellular concentration of ergothioneine in S. pombe (0.3, 157.4, 41.6, and up to 1606.3 µM in vegetative, nitrogen-starved, glucose-starved, and egt1+-overexpressing cells, respectively) and described its gradual accumulation under long-term quiescence. Finally, we demonstrated that the ergothioneine pathway can also synthesize selenoneine, a selenium-containing derivative of ergothioneine, when the culture medium is supplemented with selenium. We further found that selenoneine biosynthesis involves a novel intermediate compound, hercynylselenocysteine.","doi":"10.1371/journal.pone.0097774","authors":"Pluskal T, Ueno M, Yanagida M","authors_abbrev":"Pluskal T et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-05-16","publication_year":"2014","canto_session_key":"0a152fcef2281eac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomas Pluskal","canto_first_approved_date":"2016-10-26 10:37:37","canto_approved_date":"2024-08-08 07:23:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-22 15:27:04","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tomas Pluskal","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.12c","SPBC1604.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-10-26"},{"uniquename":"PMID:27763253","title":"Fungal Sex: The Ascomycota.","citation":"Microbiol Spectr 2016 Oct;4(5)","abstract":"This article provides an overview of sexual reproduction in the ascomycetes, a phylum of fungi that is named after the specialized sacs or \"asci\" that hold the sexual spores. They have therefore also been referred to as the Sac Fungi due to these characteristic structures that typically contain four to eight ascospores. Ascomycetes are morphologically diverse and include single-celled yeasts, filamentous fungi, and more complex cup fungi. The sexual cycles of many species, including those of the model yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe and the filamentous saprobes Neurospora crassa, Aspergillus nidulans, and Podospora anserina, have been examined in depth. In addition, sexual or parasexual cycles have been uncovered in important human pathogens such as Candida albicans and Aspergillus fumigatus, as well as in plant pathogens such as Fusarium graminearum and Cochliobolus heterostrophus. We summarize what is known about sexual fecundity in ascomycetes, examine how structural changes at the mating-type locus dictate sexual behavior, and discuss recent studies that reveal that pheromone signaling pathways can be repurposed to serve cellular roles unrelated to sex.","doi":"10.1128/microbiolspec.FUNK-0005-2016","authors":"Bennett RJ, Turgeon BG","authors_abbrev":"Bennett RJ et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-10-21","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-10-22 00:15:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR15819","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:33877","SPAC1F5.08c","HGNC:30701"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19404456","title":"Bundling, sliding, and pulling microtubules in cells and in silico.","citation":"HFSP J 2007 May;1(1):11-4","abstract":"Microtubules and other proteins self-organize into complex dynamic structures such as the mitotic spindle, which separates the chromosomes during cell division. Much is known about the individual molecular players involved in assembly and positioning of the mitotic spindle, but how they act together to generate the often unexpected behavior of the whole microtubule system is not understood. Two recent papers use a combination of experimental (imaging) and theoretical (computer simulation) methods to explore the formation of bipolar linear microtubule arrays in fission yeast and the oscillatory movement of the mitotic spindle in the nematode worm. In the simulation approach, the rules for the interactions of the components (microtubules and microtubule-associated proteins) are specified and the evolution of the system is followed, with the aim of identifying the minimal set of components that can mimic the real system. The work on fission yeast concludes that bipolar microtubule structures can arise from self-organization of microtubules through nucleators, bundlers, and sliders, without a requirement for a special microtubule-organizing center. The work on the worm embryo suggests that both the positive feedback that drives oscillations and the centering force that limits their amplitude may arise from microtubule pulling forces. The systems approach exemplified by these papers should stimulate new experiments aimed at discovering the principles of cellular organization.","doi":"10.2976/1.2740563/10.2976/1","authors":"Howard J, Tolić-Nørrelykke IM","authors_abbrev":"Howard J et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2009-05-01","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18184749","title":"The actomyosin ring recruits early secretory compartments to the division site in fission yeast.","citation":"Mol Biol Cell 2008 Mar;19(3):1125-38","abstract":"The ultimate goal of cytokinesis is to establish a membrane barrier between daughter cells. The fission yeast Schizosaccharomyces pombe utilizes an actomyosin-based division ring that is thought to provide physical force for the plasma membrane invagination. Ring constriction occurs concomitantly with the assembly of a division septum that is eventually cleaved. Membrane trafficking events such as targeting of secretory vesicles to the division site require a functional actomyosin ring suggesting that it serves as a spatial landmark. However, the extent of polarization of the secretion apparatus to the division site is presently unknown. We performed a survey of dynamics of several fluorophore-tagged proteins that served as markers for various compartments of the secretory pathway. These included markers for the endoplasmic reticulum, the COPII sites, and the early and late Golgi. The secretion machinery exhibited a marked polarization to the division site. Specifically, we observed an enrichment of the transitional endoplasmic reticulum (tER) accompanied by Golgi cisternae biogenesis. These processes required actomyosin ring assembly and the function of the EFC-domain protein Cdc15p. Cdc15p overexpression was sufficient to induce tER polarization in interphase. Thus, fission yeast polarizes its entire secretory machinery to the cell division site by utilizing molecular cues provided by the actomyosin ring.","authors":"Vjestica A, Tang XZ, Oliferenko S","authors_abbrev":"Vjestica A et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-01-11","publication_year":"2008","canto_session_key":"5ce1860d8c2a56ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-12-30 14:47:18","canto_approved_date":"2025-09-03 19:02:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-01 16:47:04","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.03","SPAC27F1.07","SPAC24B11.11c","SPAC1F5.04c","SPAC22F8.08","SPAC30.01c","SPBC1734.04","SPAP8A3.08","SPBC36B7.03","SPAC20G8.05c"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2023-12-30"},{"uniquename":"PMID:34080538","title":"Kinesin-6 Klp9 orchestrates spindle elongation by regulating microtubule sliding and growth.","citation":"Elife 2021 Jun 03;10","abstract":"Mitotic spindle function depends on the precise regulation of microtubule dynamics and microtubule sliding. Throughout mitosis, both processes have to be orchestrated to establish and maintain spindle stability. We show that during anaphase B spindle elongation in  Schizosaccharomyces pombe , the sliding motor Klp9 (kinesin-6) also promotes microtubule growth in vivo. In vitro, Klp9 can enhance and dampen microtubule growth, depending on the tubulin concentration. This indicates that the motor is able to promote and block tubulin subunit incorporation into the microtubule lattice in order to set a well-defined microtubule growth velocity. Moreover, Klp9 recruitment to spindle microtubules is dependent on its dephosphorylation mediated by XMAP215/Dis1, a microtubule polymerase, creating a link between the regulation of spindle length and spindle elongation velocity. Collectively, we unravel the mechanism of anaphase B, from Klp9 recruitment to the motors dual-function in regulating microtubule sliding and microtubule growth, allowing an inherent coordination of both processes.","doi":"10.7554/eLife.67489","authors":"Krüger LK, Gélin M, Ji L, Kikuti C, Houdusse A, Théry M, Blanchoin L, Tran PT","authors_abbrev":"Krüger LK et al.","pubmed_publication_date":"03 Jun 2021","pubmed_entrez_date":"2021-06-03","publication_year":"2021","canto_session_key":"420a5c4d2fd025ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-07-31 08:15:34","canto_approved_date":"2023-10-13 10:52:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-31 08:15:21","canto_added_date":"2021-06-05 00:15:04","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":26,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPCC895.07","SPBC15D4.01c","SPAC3A11.14c","SPCC736.14","SPAC18G6.15","SPAC3G9.12","SPAC25G10.07c","SPAC1782.09c","SPAC890.02c","SPBC12D12.01"],"gene_count":11,"ltp_gene_count":4,"approved_date":"2023-07-31"},{"uniquename":"PMID:12009298","title":"RTS1-an eukaryotic terminator of replication.","citation":"Int J Biochem Cell Biol 2002 Sep;34(9):1031-4","abstract":"Eukaryotic replication termination generally occurs randomly in the region between two active origins. However, termination, or pausing of the replication forks has been observed at specific loci. Recently, a site-specific terminator of replication named RTS1 was shown to play an important role in mating-type switching in Schizosaccharomyces pombe. Mating-type switching in S. pombe relies on an imprinting event that chemically modifies one strand of the DNA at the mating-type locus mat1. This imprint, that is formed only when mat1 is replicated in a specific direction, marks the DNA for a rearrangement leading to mating-type switching. The RTS1 element ensures that mat1 is replicated in the correct direction for imprinting and initiation of the subsequent mating-type switching event. This is the first replication terminator shown to play a role in cellular differentiation.","authors":"Vengrova S, Codlin S, Dalgaard JZ","authors_abbrev":"Vengrova S et al.","pubmed_publication_date":"Sep 2002","pubmed_entrez_date":"2002-05-16","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34810257","title":"Ccp1-Ndc80 switch at the N terminus of CENP-T regulates kinetochore assembly.","citation":"Proc Natl Acad Sci U S A 2021 Nov 30;118(48)","abstract":"Kinetochores, a protein complex assembled on centromeres, mediate chromosome segregation. In most eukaryotes, centromeres are epigenetically specified by the histone H3 variant CENP-A. CENP-T, an inner kinetochore protein, serves as a platform for the assembly of the outer kinetochore Ndc80 complex during mitosis. How CENP-T is regulated through the cell cycle remains unclear. Ccp1 (counteracter of CENP-A loading protein 1) associates with centromeres during interphase but delocalizes from centromeres during mitosis. Here, we demonstrated that Ccp1 directly interacts with CENP-T. CENP-T is important for the association of Ccp1 with centromeres, whereas CENP-T centromeric localization depends on Mis16, a homolog of human RbAp48/46. We identified a Ccp1-interaction motif (CIM) at the N terminus of CENP-T, which is adjacent to the Ndc80 receptor motif. The CIM domain is required for Ccp1 centromeric localization, and the CIM domain-deleted mutant phenocopies  ccp1 Δ. The CIM domain can be phosphorylated by CDK1 (cyclin-dependent kinase 1). Phosphorylation of CIM weakens its interaction with Ccp1. Consistent with this, Ccp1 dissociates from centromeres through all stages of the cell cycle in the phosphomimetic mutant of the CIM domain, whereas in the phospho-null mutant of the domain, Ccp1 associates with centromeres during mitosis. We further show that the phospho-null mutant disrupts the positioning of the Ndc80 complex during mitosis, resulting in chromosome missegregation. This work suggests that competitive exclusion between Ccp1 and Ndc80 at the N terminus of CENP-T via phosphorylation ensures precise kinetochore assembly during mitosis and uncovers a previously unrecognized mechanism underlying kinetochore assembly through the cell cycle.","doi":"10.1073/pnas.2104459118","authors":"Dong Q, Liu XL, Wang XH, Zhao Y, Chen YH, Li F","authors_abbrev":"Dong Q et al.","pubmed_publication_date":"30 Nov 2021","pubmed_entrez_date":"2021-11-23","publication_year":"2021","canto_session_key":"260925d9ac1a773d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Qianhua Dong","canto_first_approved_date":"2022-07-01 16:57:18","canto_approved_date":"2026-01-29 13:56:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-06-24 13:42:54","canto_added_date":"2022-01-16 01:15:04","annotation_curators":[{"name":"Qianhua Dong","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.13","SPAC17G8.15","SPBC11C11.03","SPCC1672.10","SPBC36B7.08c","SPBC1105.17","SPCC576.12c","SPBC11B10.09","SPBC2D10.16"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2022-07-01"},{"uniquename":"PMID:37831774","title":"Force redistribution in clathrin-mediated endocytosis revealed by coiled-coil force sensors.","citation":"Sci Adv 2023 Oct 13;9(41):eadi1535","abstract":"Forces are central to countless cellular processes, yet in vivo force measurement at the molecular scale remains difficult if not impossible. During clathrin-mediated endocytosis, forces produced by the actin cytoskeleton are transmitted to the plasma membrane by a multiprotein coat for membrane deformation. However, the magnitudes of these forces remain unknown. Here, we present new in vivo force sensors that induce protein condensation under force. We measured the forces on the fission yeast Huntingtin-Interacting Protein 1 Related (HIP1R) homolog End4p, a protein that links the membrane to the actin cytoskeleton. End4p is under ~19-piconewton force near the actin cytoskeleton, ~11 piconewtons near the clathrin lattice, and ~9 piconewtons near the plasma membrane. Our results demonstrate that forces are collected and redistributed across the endocytic machinery.","doi":"10.1126/sciadv.adi1535","authors":"Ren Y, Yang J, Fujita B, Jin H, Zhang Y, Berro J","authors_abbrev":"Ren Y et al.","pubmed_publication_date":"13 Oct 2023","pubmed_entrez_date":"2023-10-13","publication_year":"2023","canto_session_key":"2d7a5e210e702a6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Julien Berro","canto_first_approved_date":"2024-07-16 16:38:59","canto_approved_date":"2025-12-19 11:39:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-15 08:49:30","canto_added_date":"2023-10-13 23:25:04","annotation_curators":[{"name":"Julien Berro","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC162.07","SPAC688.11"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-07-16"},{"uniquename":"PMID:5591287","title":"The induction of replicating instabilities by mutagens in Schizosaccharomyces pombe.","citation":"Mutat Res 1967;4(6):753-63","abstract":"","authors":"Nasim A","authors_abbrev":"Nasim A","pubmed_publication_date":"1967","pubmed_entrez_date":"1967-11-01","publication_year":"1967","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPAB518","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28231281","title":"The intron in centromeric noncoding RNA facilitates RNAi-mediated formation of heterochromatin.","citation":"PLoS Genet 2017 Feb;13(2):e1006606","abstract":"In fission yeast, the formation of centromeric heterochromatin is induced through the RNA interference (RNAi)-mediated pathway. Some pre-mRNA splicing mutants (prp) exhibit defective formation of centromeric heterochromatin, suggesting that splicing factors play roles in the formation of heterochromatin, or alternatively that the defect is caused by impaired splicing of pre-mRNAs encoding RNAi factors. Herein, we demonstrate that the splicing factor spPrp16p is enriched at the centromere, and associates with Cid12p (a factor in the RNAi pathway) and the intron-containing dg ncRNA. Interestingly, removal of the dg intron, mutations of its splice sites, or replacement of the dg intron with an euchromatic intron significantly decreased H3K9 dimethylation. We also revealed that splicing of dg ncRNA is repressed in cells and its repression depends on the distance from the transcription start site to the intron. Inefficient splicing was also observed in other intron-containing centromeric ncRNAs, dh and antisense dg, and splicing of antisense dg ncRNA was repressed in the presence of the RNAi factors. Our results suggest that the introns retained in centromeric ncRNAs work as facilitators, co-operating with splicing factors assembled on the intron and serving as a platform for the recruitment of RNAi factors, in the formation of centromeric heterochromatin.","doi":"10.1371/journal.pgen.1006606","authors":"Mutazono M, Morita M, Tsukahara C, Chinen M, Nishioka S, Yumikake T, Dohke K, Sakamoto M, Ideue T, Nakayama JI, Ishii K, Tani T","authors_abbrev":"Mutazono M et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2017-02-24","publication_year":"2017","canto_session_key":"2df66d072b47bd3b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tokio Tani","canto_first_approved_date":"2017-04-11 17:05:53","canto_approved_date":"2022-03-10 10:42:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-01 05:50:10","canto_added_date":"2017-02-25 01:15:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":30,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tokio Tani","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1711.17","SPBC428.08c","SPCC1393.05","SPCC188.13c","SPSNRNA.04","SPCC663.12","SPCC1739.03","SPAC664.01c","SPCC736.11","SPBC582.04c","SPAC13G7.07","SPBC16D10.07c"],"gene_count":12,"ltp_gene_count":7,"approved_date":"2017-04-11"},{"uniquename":"PMID:12018481","title":"Solution structure determination of the two DNA-binding domains in the Schizosaccharomyces pombe Abp1 protein by a combination of dipolar coupling and diffusion anisotropy restraints.","citation":"J Biomol NMR 2002 Apr;22(4):333-47","abstract":"We have solved the solution structure of the N-terminal region of the fission yeast centromere protein, Abp1, bound to a 21-base pair DNA fragment bearing its recognition site (Mw = 30 kDa). Although the two DNA-binding domains in the Abpl protein were defined well by a conventional NOE-based NMR methodology, the overall structure of the Abpl protein was poorly defined, due to the lack of interdomain distance restraints. Therefore, we additionally used residual dipolar couplings measured in a weakly aligned state, and rotational diffusion anisotropies. Neither the NH residual dipolar couplings nor the backbone 15N T1/T2 data were sufficient to determine the overall structure of the Abpl protein, due to spectral overlap. We used a combination of these two orientational restraints (residual dipolar coupling and rotational diffusion anisotropy), which significantly improved the convergence of the overall structures. The range of the observed T1/T2 ratios was wider (20-50 for the secondary structure regions of Abp 1) than the previously reported data for several globular proteins, indicating that the overall shape of the Abp1.DNA complex is ellipsoid. This extended form would facilitate the recognition of the two separate sites in the relatively long DNA sequence by the DNA-binding domains of Apb1.","authors":"Kikuchi J, Iwahara J, Kigawa T, Murakami Y, Okazaki T, Yokoyama S","authors_abbrev":"Kikuchi J et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-05-23","publication_year":"2002","canto_session_key":"cb63948c27a5e35f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-14 21:43:53","canto_approved_date":"2023-02-15 10:20:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-14 21:43:46","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-14","pdb_entries":[{"pdb_id":"1iuf","gene_chains":[{"gene_uniquename":"SPBC1105.04c","chain":"A","position":"1-141"}],"title":"LOW RESOLUTION SOLUTION STRUCTURE OF THE TWO DNA-BINDING DOMAINS IN Schizosaccharomyces pombe ABP1 PROTEIN","entry_authors":"Kikuchi J,Iwahara J,Kigawa T,Murakami Y,Okazaki T,Yokoyama S,RIKEN Structural Genomics/Proteomics Initiative (RSGI)","entry_authors_abbrev":"Kikuchi J et al.","reference_uniquename":"PMID:12018481","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:28775286","title":"Elp3 and Dph3 of Schizosaccharomyces pombe mediate cellular stress responses through tRNA Lys  UUU  modifications.","citation":"Sci Rep 2017 Aug 03;7(1):7225","abstract":"Efficient protein synthesis in eukaryotes requires diphthamide modification of translation elongation factor eEF2 and wobble uridine modifications of tRNAs. In higher eukaryotes, these processes are important for preventing neurological and developmental defects and cancer. In this study, we used Schizosaccharomyces pombe as a model to analyse mutants defective in eEF2 modification (dph1Δ), in tRNA modifications (elp3Δ), or both (dph3Δ) for sensitivity to cytotoxic agents and thermal stress. The dph3Δ and elp3Δ mutants were sensitive to a range of drugs and had growth defects at low temperature. dph3Δ was epistatic with dph1Δ for sensitivity to hydroxyurea and methyl methanesulfonate, and with elp3Δ for methyl methanesulfonate and growth at 16 °C. The dph1Δ and dph3Δ deletions rescued growth defects of elp3Δ in response to thiabendazole and at 37 °C. Elevated tRNA Lys  UUU  levels suppressed the elp3Δ phenotypes and some of the dph3Δ phenotypes, indicating that lack of tRNA Lys  UUU  modifications were responsible. Furthermore, we found positive genetic interactions of elp3Δ and dph3Δ with sty1Δ and atf1Δ, indicating that Elp3/Dph3-dependent tRNA modifications are important for efficient biosynthesis of key factors required for accurate responses to cytotoxic stress conditions.","doi":"10.1038/s41598-017-07647-1","authors":"Villahermosa D, Fleck O","authors_abbrev":"Villahermosa D et al.","pubmed_publication_date":"03 Aug 2017","pubmed_entrez_date":"2017-08-05","publication_year":"2017","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-08-06 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPATRNALYS.02","SPAC8F11.02c","SPAC21E11.03c","SPAC24B11.06c","SPAC15E1.03","SPAC29A4.20","SPBC3B8.05"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:21572440","title":"Full-length transcriptome assembly from RNA-Seq data without a reference genome.","citation":"Nat Biotechnol 2011 May 15;29(7):644-52","abstract":"Massively parallel sequencing of cDNA has enabled deep and efficient probing of transcriptomes. Current approaches for transcript reconstruction from such data often rely on aligning reads to a reference genome, and are thus unsuitable for samples with a partial or missing reference genome. Here we present the Trinity method for de novo assembly of full-length transcripts and evaluate it on samples from fission yeast, mouse and whitefly, whose reference genome is not yet available. By efficiently constructing and analyzing sets of de Bruijn graphs, Trinity fully reconstructs a large fraction of transcripts, including alternatively spliced isoforms and transcripts from recently duplicated genes. Compared with other de novo transcriptome assemblers, Trinity recovers more full-length transcripts across a broad range of expression levels, with a sensitivity similar to methods that rely on genome alignments. Our approach provides a unified solution for transcriptome reconstruction in any sample, especially in the absence of a reference genome.","doi":"10.1038/nbt.1883","authors":"Grabherr MG, Haas BJ, Yassour M, Levin JZ, Thompson DA, Amit I, Adiconis X, Fan L, Raychowdhury R, Zeng Q, Chen Z, Mauceli E, Hacohen N, Gnirke A, Rhind N, di Palma F, Birren BW, Nusbaum C, Lindblad-Toh K, Friedman N, Regev A","authors_abbrev":"Grabherr MG et al.","pubmed_publication_date":"15 May 2011","pubmed_entrez_date":"2011-05-17","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9034168","title":"A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins.","citation":"FASEB J 1997 Jan;11(1):68-76","abstract":"Computer analysis of a conserved domain, BRCT, first described at the carboxyl terminus of the breast cancer protein BRCA1, a p53 binding protein (53BP1), and the yeast cell cycle checkpoint protein RAD9 revealed a large superfamily of domains that occur predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain consists of approximately 95 amino acid residues and occurs as a tandem repeat at the carboxyl terminus of numerous proteins, but has been observed also as a tandem repeat at the amino terminus or as a single copy. The BRCT superfamily presently includes approximately 40 nonorthologous proteins, namely, BRCA1, 53BP1, and RAD9; a protein family that consists of the fission yeast replication checkpoint protein Rad4, the oncoprotein ECT2, the DNA repair protein XRCC1, and yeast DNA polymerase subunit DPB11; DNA binding enzymes such as terminal deoxynucleotidyltransferases, deoxycytidyl transferase involved in DNA repair, and DNA-ligases III and IV; yeast multifunctional transcription factor RAP1; and several uncharacterized gene products. Another previously described domain that is shared by bacterial NAD-dependent DNA-ligases, the large subunits of eukaryotic replication factor C, and poly(ADP-ribose) polymerases appears to be a distinct version of the BRCT domain. The retinoblastoma protein (a universal tumor suppressor) and related proteins may contain a distant relative of the BRCT domain. Despite the functional diversity of all these proteins, participation in DNA damage-responsive checkpoints appears to be a unifying theme. Thus, the BRCT domain is likely to perform critical, yet uncharacterized, functions in the cell cycle control of organisms from bacteria to humans. The carboxyterminal BRCT domain of BRCA1 corresponds precisely to the recently identified minimal transcription activation domain of this protein, indicating one such function.","authors":"Bork P, Hofmann K, Bucher P, Neuwald AF, Altschul SF, Koonin EV","authors_abbrev":"Bork P et al.","pubmed_publication_date":"Jan 1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39036606","title":" Schizosaccharomyces pombe  as a predictor toxicity tool.","citation":"MethodsX 2024 Dec;13:102823","abstract":"The fission yeast  Schizosaccharomyces pombe  is frequently used as a genetically manipulable model system, offering valuable understandings into cellular mechanisms. In the present study, a comprehensive step-by-step methodology for the research of the action mechanisms and detoxification by efflux pumps is showed. The protocol involves the thawing and culture of yeast cells in liquid medium under controlled conditions to ensure exponential growth. After that, a dose-response assessment is carried out by culturing wild-type cells in liquid medium, followed by exposure to increasing concentrations of the toxic substances. Optical density measurements are taken spectrophotometrically after exposure, and the process is repeated at least three times for quantitative analysis. Subsequently, defective mutants are selected to explore specific mechanisms of action or detoxification by efflux pumps, with cultures prepared and treated similarly to the wild type. Optical density measurements are again taken after exposure for quantitative analysis. This methodology ensures robust and reproducible results for the research toxic substances effects on  S. pombe .- Schizosaccharomyces pombe  is an adequate tool to evaluate contaminants toxicity.-Dose-responses curves are obtained on wild type to evaluate toxicity mechanisms.-This methodology ensures robust and reproducible results for the research toxic substances effects on  S. pombe. ","doi":"10.1016/j.mex.2024.102823","authors":"Álvarez-Herrera C, Maisanaba S, Ruíz-Cabello ML, Repetto G","authors_abbrev":"Álvarez-Herrera C et al.","pubmed_publication_date":"Dec 2024","pubmed_entrez_date":"2024-07-22","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-07-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8041632","title":"SCR: novel human suppressors of cdc2/cdc13 mutants of Schizosaccharomyces pombe harbour motifs for RNA binding proteins.","citation":"Nucleic Acids Res 1994 Jul 11;22(13):2687-93","abstract":"By phenotypic complementation of the cdc2 and the cdc13 mutants of the fission yeast Schizosaccharomyces pombe, we have cloned two novel multicopy suppressors from a cDNA library of the human fibroblast. They encode homologous proteins containing two regions that are highly conserved among RNA binding proteins. We named them scr2 and scr3, the acronyms of the suppressor of cdc2 (cdc13) with RNA binding motif. They encode proteins of 403 (Scr2) and 407 (Scr3) amino acids. Western blot analysis showed that the amount of Cdc2 increased when either rat kidney fibroblasscr2 or scr3 was introduced into the cdc2-L7 and cdc13-117 mutant cells of S.pombe. No conspicuous alteration in the transcript level was detected as judged by Northern analysis. Considering that the cdc2+ suppresses the cdc13 mutant and vice versa, one of the possible interpretations of these result is that these genes suppress the mutants through the induction of the translation of Cdc2.","authors":"Kanaoka Y, Nojima H","authors_abbrev":"Kanaoka Y et al.","pubmed_publication_date":"11 Jul 1994","pubmed_entrez_date":"1994-07-11","publication_year":"1994","canto_session_key":"4205ad789bc3a808","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:12:10","canto_session_submitted_date":"2012-03-03 15:11:50","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:16135799","title":"Role of the Schizosaccharomyces pombe F-Box DNA helicase in processing recombination intermediates.","citation":"Mol Cell Biol 2005 Sep;25(18):8074-83","abstract":"In an effort to identify novel genes involved in recombination repair, we isolated fission yeast Schizosaccharomyces pombe mutants sensitive to methyl methanesulfonate (MMS) and a synthetic lethal with rad2. A gene that complements such mutations was isolated from the S. pombe genomic library, and subsequent analysis identified it as the fbh1 gene encoding the F-box DNA helicase, which is conserved in mammals but not conserved in Saccharomyces cerevisiae. An fbh1 deletion mutant is moderately sensitive to UV, MMS, and gamma rays. The rhp51 (RAD51 ortholog) mutation is epistatic to fbh1. fbh1 is essential for viability in stationary-phase cells and in the absence of either Srs2 or Rqh1 DNA helicase. In each case, lethality is suppressed by deletion of the recombination gene rhp57. These results suggested that fbh1 acts downstream of rhp51 and rhp57. Following UV irradiation or entry into the stationary phase, nuclear chromosomal domains of the fbh1Delta mutant shrank, and accumulation of some recombination intermediates was suggested by pulsed-field gel electrophoresis. Focus formation of Fbh1 protein was induced by treatment that damages DNA. Thus, the F-box DNA helicase appears to process toxic recombination intermediates, the formation of which is dependent on the function of Rhp51.","authors":"Morishita T, Furukawa F, Sakaguchi C, Toda T, Carr AM, Iwasaki H, Shinagawa H","authors_abbrev":"Morishita T et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-09-02","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4H3.05","SPAC3G6.06c","SPBC336.01","SPAC644.14c","SPAC20H4.07","SPAC2G11.12"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:10187772","title":"Transcriptional regulation of the Schizosaccharomyces pombe malic enzyme gene, mae2.","citation":"J Biol Chem 1999 Apr 09;274(15):9969-75","abstract":"The NAD-dependent malic enzyme from Schizosaccharomyces pombe catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2. Transcription of the S. pombe malic enzyme gene, mae2, was studied to elucidate the regulatory mechanisms involved in the expression of the gene. No evidence for substrate-induced expression of mae2 was observed in the presence of 0.2% L-malate. However, transcription of mae2 was induced when cells were grown in high concentrations of glucose or under anaerobic conditions. The increased levels of malic enzyme may provide additional pyruvate or assist in maintaining the redox potential under fermentative conditions. Deletion and mutation analyses of the 5'-flanking region of the mae2 gene revealed the presence of three novel negative cis-acting elements, URS1, URS2, and URS3, that seem to function cooperatively to repress transcription of the mae2 gene. URS1 and URS2 are also present in the promoter region of the S. pombe malate transporter gene, suggesting co-regulation of their expression. Furthermore, two positive cis-acting elements in the mae2 promoter, UAS1 and UAS2, show homology with the DNA recognition sites of the cAMP-dependent transcription factors ADR1, AP-2, and ATF (activating transcription factor)/CREB (cAMP response element binding).","authors":"Viljoen M, Volschenk H, Young RA, van Vuuren HJ","authors_abbrev":"Viljoen M et al.","pubmed_publication_date":"09 Apr 1999","pubmed_entrez_date":"1999-04-03","publication_year":"1999","canto_session_key":"85b5c71c5d520179","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-12 09:11:58","canto_approved_date":"2024-04-02 16:51:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-12 09:11:51","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC794.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-12"},{"uniquename":"EMBL:SPIUVI22R","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1594599","title":"The rad3+ gene of Schizosaccharomyces pombe is involved in multiple checkpoint functions and in DNA repair.","citation":"Proc Natl Acad Sci U S A 1992 Jun 01;89(11):4952-6","abstract":"A number of important molecular checkpoints are believed to control the orderly progression of cell cycle events. We have found that the radiation-sensitive Schizosaccharomyces pombe mutant rad3-136 is deficient in two molecular checkpoint functions. Unlike wild-type cells, the mutant cells are unable to arrest in the G2 phase of the cell cycle after DNA damage by gamma-irradiation and are also incapable of maintaining the dependence of mitosis upon the completion of DNA synthesis. An S. pombe genomic clone that complements the UV sensitivity of the rad3-136 mutant completely restores the missing checkpoint functions. The rad3+ gene is also likely to play a role in DNA repair.","authors":"Jimenez G, Yucel J, Rowley R, Subramani S","authors_abbrev":"Jimenez G et al.","pubmed_publication_date":"01 Jun 1992","pubmed_entrez_date":"1992-06-01","publication_year":"1992","canto_session_key":"38560610372534b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-17 16:17:22","canto_approved_date":"2026-06-09 19:02:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-03-08 13:50:24","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC20G8.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-03-17"},{"uniquename":"PMID:38346750","title":"Addition of α-1,3-glucan-binding domains to α-1,3-glucanase Agn1p from　 Schizosaccharomyces pombe enhances hydrolytic activity of insoluble α-1,3-glucan.","citation":"J Gen Appl Microbiol 2024 Feb 13;","abstract":"The glycoside hydrolase (GH) 71 α-1,3-glucanase (Agn1p) from Schizosaccharomyces pombe consists of an N-terminal signal sequence and a catalytic domain. Meanwhile, the GH87 α-1,3-glucanase (Agl-KA) from Bacillus circulans KA-304 consists of an N-terminal signal sequence, a first discoidin domain (DS1), a carbohydrate-binding module family 6 (CBM6), a threonine and proline repeat linker (TP), a second discoidin domain (DS2), an uncharacterized domain, and a catalytic domain. DS1, CBM6, and DS2 exhibit α-1,3-glucan binding activity. This study involved genetically fusing TP, DS1, CBM6, TP, and DS2 to the C-terminus of Agn1p, generating the fusion enzyme Agn1p-DCD. The fusion enzyme was then expressed in Escherichia coli and purified from the cell-free extract. Agn1p-DCD and Agn1p exhibited similar characteristics, such as optimal pH, optimal temperature, pH stability, and thermostability. Insoluble α-1,3-glucan (1%) hydrolyzing assay showed that Agn1p-DCD and Agn1p released approximately 7.6 and 5.0 mM of reducing sugars, respectively, after 48 h of reaction. Kinetic analysis and an α-1,3-glucan binding assay indicated that the addition of DS1, CBM6, and DS2 enhanced the affinity of Agn1p for α-1,3-glucan. Moreover, Agn1p-DCD contributed to enhancing the fungal growth inhibition activity when combined with a mixture of GH19 chitinase and GH16 β-1,3-glucanase.","doi":"10.2323/jgam.2024.02.001","authors":"Horaguchi Y, Yokomichi M, Takahashi M, Xu F, Konno H, Makabe K, Yano S","authors_abbrev":"Horaguchi Y et al.","pubmed_publication_date":"13 Feb 2024","pubmed_entrez_date":"2024-02-12","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-02-14 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36442092","title":"Mechanism of actin filament branch formation by Arp2/3 complex revealed by a high-resolution cryo-EM structureof the branch junction.","citation":"Proc Natl Acad Sci U S A 2022 Dec 06;119(49):e2206722119","abstract":"We reconstructed the structure of actin filament branch junctions formed by fission yeast Arp2/3 complex at 3.5 Å resolution from images collected by electron cryo-microscopy. During specimen preparation, all of the actin subunits and Arp3 hydrolyzed their bound adenosine triphosphate (ATP) and dissociated the γ-phosphate, but Arp2 retained the γ-phosphate. Binding tightly to the side of the mother filament and nucleating the daughter filament growing as a branch requires Arp2/3 complex to undergo a dramatic conformational change where two blocks of structure rotate relative to each other about 25° to align Arp2 and Arp3 as the first two subunits in the branch. During branch formation, Arp2/3 complex acquires more than 8,000 Å 2  of new buried surface, accounting for the stability of the branch. Inactive Arp2/3 complex binds only transiently to the side of an actin filament, because its conformation allows only a subset of the interactions found in the branch junction.","doi":"10.1073/pnas.2206722119","authors":"Chou SZ, Chatterjee M, Pollard TD","authors_abbrev":"Chou SZ et al.","pubmed_publication_date":"06 Dec 2022","pubmed_entrez_date":"2022-11-28","publication_year":"2022","canto_session_key":"648730947f0d1cfc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-11-29 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.03","SPAC17G8.04c","SPBC14C8.06","SPAC6F6.10c","SPAC11H11.06","SPBC1778.08c","SPAC6G9.07c"],"gene_count":7,"ltp_gene_count":7,"pdb_entries":[{"pdb_id":"8e9b","gene_chains":[{"gene_uniquename":"SPAC6F6.10c","chain":"D","position":"1-317"},{"gene_uniquename":"SPAC630.03","chain":"A","position":"1-427"},{"gene_uniquename":"SPBC14C8.06","chain":"C","position":"1-377"},{"gene_uniquename":"SPAC17G8.04c","chain":"G","position":"1-152"},{"gene_uniquename":"SPAC6G9.07c","chain":"F","position":"1-168"},{"gene_uniquename":"SPAC11H11.06","chain":"B","position":"1-390"},{"gene_uniquename":"SPBC1778.08c","chain":"E","position":"1-174"}],"title":"Cryo-EM structure of S. pombe Arp2/3 complex in the branch junction","entry_authors":"Chou SZ,Pollard TP","entry_authors_abbrev":"Chou SZ et al.","reference_uniquename":"PMID:36442092","experimental_method":"EM","resolution":"3.5"}]},{"uniquename":"PMID:26354768","title":"Suppression of Meiotic Recombination by CENP-B Homologs in Schizosaccharomyces pombe.","citation":"Genetics 2015 Nov;201(3):897-904","abstract":"Meiotic homologous recombination (HR) is not uniform across eukaryotic genomes, creating regions of HR hot- and coldspots. Previous study reveals that the Spo11 homolog Rec12 responsible for initiation of meiotic double-strand breaks in the fission yeast Schizosaccharomyces pombe is not targeted to Tf2 retrotransposons. However, whether Tf2s are HR coldspots is not known. Here, we show that the rates of HR across Tf2s are similar to a genome average but substantially increase in mutants deficient for the CENP-B homologs. Abp1, which is the most prominent of the CENP-B family members and acts as the primary determinant of HR suppression at Tf2s, is required to prevent gene conversion and maintain proper recombination exchange of homologous alleles flanking Tf2s. In addition, Abp1-mediated suppression of HR at Tf2s requires all three of its domains with distinct functions in transcriptional repression and higher-order genome organization. We demonstrate that HR suppression of Tf2s can be robustly maintained despite disruption to chromatin factors essential for transcriptional repression and nuclear organization of Tf2s. Intriguingly, we uncover a surprising cooperation between the histone methyltransferase Set1 responsible for histone H3 lysine 4 methylation and the nonhomologous end joining pathway in ensuring the suppression of HR at Tf2s. Our study identifies a molecular pathway involving functional cooperation between a transcription factor with epigenetic regulators and a DNA repair pathway to regulate meiotic recombination at interspersed repeats.","doi":"10.1534/genetics.115.179465","authors":"Johansen P, Cam HP","authors_abbrev":"Johansen P et al.","pubmed_publication_date":"Nov 2015","pubmed_entrez_date":"2015-09-11","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-09-13 00:18:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC543.03c","SPCC306.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:29232693","title":"Host factors that promote retrotransposon integration are similar in distantly related eukaryotes.","citation":"PLoS Genet 2017 Dec;13(12):e1006775","abstract":"Retroviruses and Long Terminal Repeat (LTR)-retrotransposons have distinct patterns of integration sites. The oncogenic potential of retrovirus-based vectors used in gene therapy is dependent on the selection of integration sites associated with promoters. The LTR-retrotransposon Tf1 of Schizosaccharomyces pombe is studied as a model for oncogenic retroviruses because it integrates into the promoters of stress response genes. Although integrases (INs) encoded by retroviruses and LTR-retrotransposons are responsible for catalyzing the insertion of cDNA into the host genome, it is thought that distinct host factors are required for the efficiency and specificity of integration. We tested this hypothesis with a genome-wide screen of host factors that promote Tf1 integration. By combining an assay for transposition with a genetic assay that measures cDNA recombination we could identify factors that contribute differentially to integration. We utilized this assay to test a collection of 3,004 S. pombe strains with single gene deletions. Using these screens and immunoblot measures of Tf1 proteins, we identified a total of 61 genes that promote integration. The candidate integration factors participate in a range of processes including nuclear transport, transcription, mRNA processing, vesicle transport, chromatin structure and DNA repair. Two candidates, Rhp18 and the NineTeen complex were tested in two-hybrid assays and were found to interact with Tf1 IN. Surprisingly, a number of pathways we identified were found previously to promote integration of the LTR-retrotransposons Ty1 and Ty3 in Saccharomyces cerevisiae, indicating the contribution of host factors to integration are common in distantly related organisms. The DNA repair factors are of particular interest because they may identify the pathways that repair the single stranded gaps flanking the sites of strand transfer following integration of LTR retroelements.","doi":"10.1371/journal.pgen.1006775","authors":"Rai SK, Sangesland M, Lee M, Esnault C, Cui Y, Chatterjee AG, Levin HL","authors_abbrev":"Rai SK et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-12-13","publication_year":"2017","canto_session_key":"60449d87b9094abf","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_session_submitted_date":"2018-02-04 15:04:41","canto_added_date":"2017-12-15 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23295325","title":"A single internal telomere tract ensures meiotic spindle formation.","citation":"EMBO Rep 2013 Mar 01;14(3):252-60","abstract":"Contact between telomeres and the fission yeast spindle pole body during meiotic prophase is crucial for subsequent spindle assembly, but the feature of telomeres that confers their ability to promote spindle formation remains mysterious. Here we show that while strains harbouring circular chromosomes devoid of telomere repeat tracts undergo aberrant meiosis with defective spindles, the insertion of a single internal telomere repeat stretch rescues the spindle defects. Moreover, the telomeric overhang-binding protein Pot1 is dispensable for rescue of spindle formation. Hence, an inherent feature of the double-strand telomeric region endows telomeres with the capacity to promote spindle formation.","doi":"10.1038/embor.2012.218","authors":"Tomita K, Bez C, Fennell A, Cooper JP","authors_abbrev":"Tomita K et al.","pubmed_publication_date":"01 Mar 2013","pubmed_entrez_date":"2013-01-09","publication_year":"2013","canto_session_key":"cacc931f418bb5da","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20814909","title":"Segmentation and tracking of cytoskeletal filaments using open active contours.","citation":"Cytoskeleton (Hoboken) 2010 Nov;67(11):693-705","abstract":"We use open active contours to quantify cytoskeletal structures imaged by fluorescence microscopy in two and three dimensions. We developed an interactive software tool for segmentation, tracking, and visualization of individual fibers. Open active contours are parametric curves that deform to minimize the sum of an external energy derived from the image and an internal bending and stretching energy. The external energy generates (i) forces that attract the contour toward the central bright line of a filament in the image, and (ii) forces that stretch the active contour toward the ends of bright ridges. Images of simulated semiflexible polymers with known bending and torsional rigidity are analyzed to validate the method. We apply our methods to quantify the conformations and dynamics of actin in two examples: actin filaments imaged by TIRF microscopy in vitro, and actin cables in fission yeast imaged by spinning disk confocal microscopy.","doi":"10.1002/cm.20481","authors":"Smith MB, Li H, Shen T, Huang X, Yusuf E, Vavylonis D","authors_abbrev":"Smith MB et al.","pubmed_publication_date":"Nov 2010","pubmed_entrez_date":"2010-09-04","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1367186","title":"Single chain antibody (SCA) encoding genes: one-step construction and expression in eukaryotic cells.","citation":"Biotechnology (N Y) 1991 Feb;9(2):165-9","abstract":"We report the expression, in eukaryotic cells, of a gene encoding a single chain antibody (SCA) and a rapid method for the construction of such genes. A SCA directed against the aromatic dye fluorescein was synthesized from a gene constructed by means of the simultaneous use of four PCR primers and templates of both light and heavy chain immunoglobulin cDNAs in the form of either plasmid clones or reverse transcribed hybridoma RNA. Two of the primers were partially complementary to one another and encoded the polypeptide linker which joins the immunoglobulin light and heavy chain variable domains of the SCA polypeptide. A functional, hapten-binding product was synthesized from the gene thus constructed in both E. coli and the fission yeast, Schizosaccharomyces pombe. Our results demonstrate that gene constructs encoding single chain antigen binding proteins can be synthesized very rapidly with only limited sequence information about the pertinent light and heavy chain immunoglobulin genes, and, that neither murine codon usage bias, Thermus aquaticus DNA polymerase infidelity, nor the eukaryotic cellular environment preclude the synthesis of functional single chain antigen binding proteins in non-lymphatic, non-murine eukaryotic cells.","authors":"Davis GT, Bedzyk WD, Voss EW, Jacobs TW","authors_abbrev":"Davis GT et al.","pubmed_publication_date":"Feb 1991","pubmed_entrez_date":"1991-02-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009915","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.111"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2534559","title":"Fission yeast cyclin: subcellular localisation and cell cycle regulation.","citation":"J Cell Sci Suppl 1989;12:9-19","abstract":"Entry into mitosis in the fission yeast Schizosaccharomyces pombe involves the interaction of a number of genes with the major cell cycle control gene, cdc2+. One of these, cdc13+, encodes a protein with homology to cyclin. By indirect immunofluorescence microscopy using antibodies to the appropriate bacterially-expressed protein, we have shown that both cdc13 and cdc2 are nuclear proteins in S. pombe. Both are localised to a nuclear domain distinct from that occupied by the DAPI-staining chromatin. The immunofluorescence signals of both proteins show a progressive increase during interphase but are undetectable at mitosis. Loss of cdc13 fluorescence at mitosis reflects the destruction of the protein. Thus, it behaves as a classic cyclin. This is not the case for cdc2, the level of which remains constant through the cell cycle. Cells carrying a disrupted copy of the cdc13+ gene fail to accumulate either cdc13 or cdc2 in the nucleus. Cells carrying a disrupted cdc2+ gene fail to accumulate cdc2 but reveal apparently normal levels of cdc13. cdc13 therefore appears to be required to localise cdc2 to the nucleus but not vice versa. The destruction of cdc13 at mitosis may allow cdc2 to redistribute to the cytoplasm.","authors":"Alfa CE, Booher R, Beach D, Hyams JS","authors_abbrev":"Alfa CE et al.","pubmed_publication_date":"1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_session_key":"643897cc05470b4b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-18 18:56:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-02-18 18:56:46","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPAC24H6.05","SPBC11B10.09","SPBC582.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-02-18"},{"uniquename":"PMID:28572185","title":"Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)-Based Quantitative Proteomics and Phosphoproteomics in Fission Yeast.","citation":"Cold Spring Harb Protoc 2017 Jun 01;2017(6):pdb.prot091686","abstract":"Modern mass spectrometry (MS)-based approaches are capable of identifying and quantifying thousands of proteins and phosphorylation events in a single biological experiment. Here we present a (phospho)proteomic workflow based on in-solution proteome digestion of samples labeled by stable isotope labeling by amino acids in cell culture (SILAC) and phosphopeptide enrichment using strong cation exchange (SCX) and TiO 2  chromatographies. These procedures are followed by high-accuracy MS measurement on an Orbitrap mass spectrometer and subsequent bioinformatic processing using MaxQuant software.","doi":"10.1101/pdb.prot091686","authors":"Carpy A, Koch A, Bicho CC, Borek WE, Hauf S, Sawin KE, Maček B","authors_abbrev":"Carpy A et al.","pubmed_publication_date":"01 Jun 2017","pubmed_entrez_date":"2017-06-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-06-04 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23661563","title":"All or nothing: protein complexes flip essentiality between distantly related eukaryotes.","citation":"Genome Biol Evol 2013;5(6):1049-59","abstract":"In the budding yeast Saccharomyces cerevisiae, the subunits of any given protein complex are either mostly essential or mostly nonessential, suggesting that essentiality is a property of molecular machines rather than individual components. There are exceptions to this rule, however, that is, nonessential genes in largely essential complexes and essential genes in largely nonessential complexes. Here, we provide explanations for these exceptions, showing that redundancy within complexes, as revealed by genetic interactions, can explain many of the former cases, whereas \"moonlighting,\" as revealed by membership of multiple complexes, can explain the latter. Surprisingly, we find that redundancy within complexes cannot usually be explained by gene duplication, suggesting alternate buffering mechanisms. In the distantly related Schizosaccharomyces pombe, we observe the same phenomenon of modular essentiality, suggesting that it may be a general feature of eukaryotes. Furthermore, we show that complexes flip essentiality in a cohesive fashion between the two species, that is, they tend to change from mostly essential to mostly nonessential, or vice versa, but not to mixed patterns. We show that these flips in essentiality can be explained by differing lifestyles of the two yeasts. Collectively, our results support a previously proposed model where proteins are essential because of their involvement in essential functional modules rather than because of specific topological features such as degree or centrality.","doi":"10.1093/gbe/evt074","authors":"Ryan CJ, Krogan NJ, Cunningham P, Cagney G","authors_abbrev":"Ryan CJ et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-05-11","publication_year":"2013","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1958212","title":"Cloning and sequencing of the gene encoding the large subunit of glutathione synthetase of Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 1991 Nov 27;181(1):430-6","abstract":"The gene for the large subunit of glutathione synthetase (EC 6.3.2.3) of Schizosaccharomyces pombe was cloned from a S. pombe genomic DNA library by complementation of cadmium hypersensitivity of a glutathione synthetase deficient mutant of S. pombe. A long open reading frame was found in the cloned DNA sequence. Amino acid sequence predicted from the long open reading frame coincided with amino acid sequences of peptides obtained by V8 protease digestion of the large subunit of the purified glutathione synthetase. The glutathione synthetase deficient mutant which harbored plasmids containing the glutathione synthetase large subunit gene exhibited glutathione synthetase activity higher than the activity in the wild type strain, though the plasmid did not contain the gene for the small subunit of the enzyme.","authors":"Mutoh N, Nakagawa CW, Ando S, Tanabe K, Hayashi Y","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"27 Nov 1991","pubmed_entrez_date":"1991-11-27","publication_year":"1991","canto_session_key":"c0ae8d0a9450e350","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-06-03 16:35:01","canto_approved_date":"2024-04-02 17:28:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-02 15:32:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-06-03"},{"uniquename":"PMID:17900736","title":"Accumulation of CdS nanoparticles by yeasts in a fed-batch bioprocess.","citation":"J Biotechnol 2007 Dec 01;132(4):481-6","abstract":"The yeasts Schizosaccharomyces pombe and Candida glabrata were successfully cultivated in a fed-batch process at cadmium levels up to 100 mg l(-1). S. pombe incorporated 20 mg C dg(-1) dry biomass within 24h. C. glabrata accumulated 8 mg C dg(-1) dry biomass in 24h. The higher Cd uptake from S. pombe cells correlate with the elevated glucose concentrations during and at the end of the cultivation. Analysis of the cells with energy-filtering transmission electron microscopy-element specific imaging (EFTEM-ESI) revealed that cadmium is not precipitated outside the cells or at the cell wall but evenly distributed inside the cell plasma. As Cd is highly toxic this indicates that Cd is immobilized by an intracellular detoxification mechanism. Size exclusion chromatography showed that Cd is associated to a protein fraction between 25 and 67 kDa which corresponds to the theoretical molecular weight of CdS nanoparticles of 35 kDa coated with phytochelatins. This structure has been proposed in literature.","authors":"Krumov N, Oder S, Perner-Nochta I, Angelov A, Posten C","authors_abbrev":"Krumov N et al.","pubmed_publication_date":"01 Dec 2007","pubmed_entrez_date":"2007-09-29","publication_year":"2007","canto_session_key":"2176bd3a1a176947","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:51:30","canto_session_submitted_date":"2012-02-27 11:04:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:30028833","title":"Exploration and stabilization of Ras1 mating zone: A mechanism with positive and negative feedbacks.","citation":"PLoS Comput Biol 2018 Jul;14(7):e1006317","abstract":"In mating fission yeast cells, sensing and response to extracellular pheromone concentrations occurs through an exploratory Cdc42 patch that stochastically samples the cell cortex before stabilizing towards a mating partner. Active Ras1 (Ras1-GTP), an upstream regulator of Cdc42, and Gap1, the GTPase-activating protein for Ras1, localize at the patch. We developed a reaction-diffusion model of Ras1 patch appearance and disappearance with a positive feedback by a Guanine nucleotide Exchange Factor (GEF) and Gap1 inhibition. The model is based on new estimates of Ras1-GDP, Ras1-GTP and Gap1 diffusion coefficients and rates of cytoplasmic exchange studied by FRAP. The model reproduces exploratory patch behavior and lack of Ras1 patch in cells lacking Gap1. Transition to a stable patch can occur by change of Gap1 rates constants or local increase of the positive feedback rate constants. The model predicts that the patch size and number of patches depend on the strength of positive and negative feedbacks. Measurements of Ras1 patch size and number in cells overexpressing the Ras1 GEF or Gap1 are consistent with the model.","doi":"10.1371/journal.pcbi.1006317","authors":"Khalili B, Merlini L, Vincenzetti V, Martin SG, Vavylonis D","authors_abbrev":"Khalili B et al.","pubmed_publication_date":"Jul 2018","pubmed_entrez_date":"2018-07-21","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-07-23 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27075443","title":"Yeast Gdt1 is a Golgi-localized calcium transporter required for stress-induced calcium signaling and protein glycosylation.","citation":"Sci Rep 2016 Apr 14;6:24282","abstract":"Calcium signaling depends on a tightly regulated set of pumps, exchangers, and channels that are responsible for controlling calcium fluxes between the different subcellular compartments of the eukaryotic cell. We have recently reported that two members of the highly-conserved UPF0016 family, human TMEM165 and budding yeast Gdt1p, are functionally related and might form a new group of Golgi-localized cation/Ca(2+) exchangers. Defects in the human protein TMEM165 are known to cause a subtype of Congenital Disorders of Glycosylation. Using an assay based on the heterologous expression of GDT1 in the bacterium Lactococcus lactis, we demonstrated the calcium transport activity of Gdt1p. We observed a Ca(2+) uptake activity in cells expressing GDT1, which was dependent on the external pH, indicating that Gdt1p may act as a Ca(2+)/H(+) antiporter. In yeast, we found that Gdt1p controls cellular calcium stores and plays a major role in the calcium response induced by osmotic shock when the Golgi calcium pump, Pmr1p, is absent. Importantly, we also discovered that, in the presence of a high concentration of external calcium, Gdt1p is required for glycosylation of carboxypeptidase Y and the glucanosyltransferase Gas1p. Finally we showed that glycosylation process is restored by providing more Mn(2+) to the cells.","doi":"10.1038/srep24282","authors":"Colinet AS, Sengottaiyan P, Deschamps A, Colsoul ML, Thines L, Demaegd D, Duchêne MC, Foulquier F, Hols P, Morsomme P","authors_abbrev":"Colinet AS et al.","pubmed_publication_date":"14 Apr 2016","pubmed_entrez_date":"2016-04-15","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G8.08c","SPAC186.05c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:22870388","title":"Quantitative single-molecule microscopy reveals that CENP-A(Cnp1) deposition occurs during G2 in fission yeast.","citation":"Open Biol 2012 Jul;2(7):120078","abstract":"The inheritance of the histone H3 variant CENP-A in nucleosomes at centromeres following DNA replication is mediated by an epigenetic mechanism. To understand the process of epigenetic inheritance, or propagation of histones and histone variants, as nucleosomes are disassembled and reassembled in living eukaryotic cells, we have explored the feasibility of exploiting photo-activated localization microscopy (PALM). PALM of single molecules in living cells has the potential to reveal new concepts in cell biology, providing insights into stochastic variation in cellular states. However, thus far, its use has been limited to studies in bacteria or to processes occurring near the surface of eukaryotic cells. With PALM, one literally observes and 'counts' individual molecules in cells one-by-one and this allows the recording of images with a resolution higher than that determined by the diffraction of light (the so-called super-resolution microscopy). Here, we investigate the use of different fluorophores and develop procedures to count the centromere-specific histone H3 variant CENP-A(Cnp1) with single-molecule sensitivity in fission yeast (Schizosaccharomyces pombe). The results obtained are validated by and compared with ChIP-seq analyses. Using this approach, CENP-A(Cnp1) levels at fission yeast (S. pombe) centromeres were followed as they change during the cell cycle. Our measurements show that CENP-A(Cnp1) is deposited solely during the G2 phase of the cell cycle.","doi":"10.1098/rsob.120078","authors":"Lando D, Endesfelder U, Berger H, Subramanian L, Dunne PD, McColl J, Klenerman D, Carr AM, Sauer M, Allshire RC, Heilemann M, Laue ED","authors_abbrev":"Lando D et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-08-08","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20388730","title":"Mannosylinositol phosphorylceramide is a major sphingolipid component and is required for proper localization of plasma-membrane proteins in Schizosaccharomyces pombe.","citation":"J Cell Sci 2010 May 01;123(Pt 9):1578-87","abstract":"In Saccharomyces cerevisiae, three classes of sphingolipids contain myo-inositol--inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC) and mannosyldiinositol phosphorylceramide [M(IP)(2)C]. No fission yeast equivalent of Ipt1p, the inositolphosphotransferase that synthesizes M(IP)(2)C from MIPC, has been found in the Schizosaccharomyces pombe genome. Analysis of the sphingolipid composition of wild-type cells confirmed that MIPC is the terminal and most abundant complex sphingolipid in S. pombe. Three proteins (Sur1p, Csg2p and Csh1p) have been shown to be involved in the synthesis of MIPC from IPC in S. cerevisiae. The S. pombe genome has three genes (SPAC2F3.01, SPCC4F11.04c and SPAC17G8.11c) that are homologues of SUR1, termed imt1(+), imt2(+) and imt3(+), respectively. To determine whether these genes function in MIPC synthesis in S. pombe, single and multiple gene disruptants were constructed. Single imt disruptants were found to be viable. MIPC was not detected and IPC levels were increased in the triple disruptant, indicating that the three SUR1 homologues are involved in the synthesis of MIPC. GFP-tagged Imt1p, Imt2p and Imt3p localized to Golgi apparatus membranes. The MIPC-deficient mutant exhibited pleiotropic phenotypes, including defects in cellular and vacuolar morphology, and in localization of ergosterols. MIPC seemed to be required for endocytosis of a plasma-membrane-localized amino acid transporter, because sorting of the transporter from the plasma membrane to the vacuole was severely impaired in the MIPC-deficient mutant grown under nitrogen-limiting conditions. These results suggest that MIPC has multiple functions not only in the maintenance of cell and vacuole morphology but also in vesicular trafficking in fission yeast.","doi":"10.1242/jcs.059139","authors":"Nakase M, Tani M, Morita T, Kitamoto HK, Kashiwazaki J, Nakamura T, Hosomi A, Tanaka N, Takegawa K","authors_abbrev":"Nakase M et al.","pubmed_publication_date":"01 May 2010","pubmed_entrez_date":"2010-04-15","publication_year":"2010","canto_session_key":"a1aa202992e46314","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-07-05 08:27:15","canto_approved_date":"2024-10-01 06:37:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-26 08:47:46","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F3.01","SPAC19G12.08","SPCC4F11.04c","SPAC17G8.11c","SPBC887.15c","SPBC359.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2024-07-05"},{"uniquename":"PMID:11459981","title":"Meiotic recombination and chromosome segregation in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 2001 Jul 17;98(15):8395-402","abstract":"In most organisms homologous recombination is vital for the proper segregation of chromosomes during meiosis, the formation of haploid sex cells from diploid precursors. This review compares meiotic recombination and chromosome segregation in the fission yeast Schizosaccharomyces pombe and the distantly related budding yeast Saccharomyces cerevisiae, two especially tractable microorganisms. Certain features, such as the occurrence of DNA breaks associated with recombination, appear similar, suggesting that these features may be common in eukaryotes. Other features, such as the role of these breaks and the ability of chromosomes to segregate faithfully in the absence of recombination, appear different, suggesting multiple solutions to the problems faced in meiosis.","authors":"Davis L, Smith GR","authors_abbrev":"Davis L et al.","pubmed_publication_date":"17 Jul 2001","pubmed_entrez_date":"2001-07-19","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:166019","title":"Genetic control of radiation sensitivity in Schizosaccharomyces pombe.","citation":"Genetics 1975 Apr;79(4):573-82","abstract":"Genetic analysis of a large number of radiation-sensitive mutants of S. pombe, isolated in different laboratories, showed that these isolates represent 22 non-allelic loci. The mutants were shown to fall into three distinct classes concerning response to UV and ionizing radiation, including two mutants which are primarily sensitive to ionizing radiation but not to UV. Single-gene mutants were crossed to obtain supersensitive double mutants. Such double mutants showed a marked increase in sensitivty to a variety of inactivating agents as compared to the parental strains. The isolation of three classes of radiation-sensitive mutants and the construction of double mutants implies the presence of multiple pathways in S. pombe for repair of radiation-induced damage. The bearing of these data on cellular repair mechanisms in eukaryotes is discussed.","authors":"Nasim A, Smith BP","authors_abbrev":"Nasim A et al.","pubmed_publication_date":"Apr 1975","pubmed_entrez_date":"1975-04-01","publication_year":"1975","canto_session_key":"2e6a836b3f4303b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-16 16:50:19","canto_approved_date":"2023-08-03 08:34:51","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-11-05 18:05:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":44,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_166019_phaf.tsv"}],"genes":["SPCC330.02","SPCC5E4.06","SPCC970.01","SPBC216.05","SPAC14C4.13","SPAC23C4.18c","SPAC1952.07","SPAC18B11.07c","SPAC1D4.12","SPAC3G6.06c","SPBC660.13c","SPBC649.03","SPAC664.07c","SPAC13G6.01c","SPAC2G11.12","SPAC30D11.10","SPCC338.17c","SPBC3E7.08c"],"gene_count":18,"ltp_gene_count":18,"approved_date":"2016-06-16"},{"uniquename":"PMID:28139976","title":"An aging-independent replicative lifespan in a symmetrically dividing eukaryote.","citation":"Elife 2017 Jan 31;6","abstract":"The replicative lifespan (RLS) of a cell-defined as the number of cell divisions before death-has informed our understanding of the mechanisms of cellular aging. However, little is known about aging and longevity in symmetrically dividing eukaryotic cells because most prior studies have used budding yeast for RLS studies. Here, we describe a multiplexed fission yeast lifespan micro-dissector (multFYLM) and an associated image processing pipeline for performing high-throughput and automated single-cell micro-dissection. Using the multFYLM, we observe continuous replication of hundreds of individual fission yeast cells for over seventy-five generations. Surprisingly, cells die without the classic hallmarks of cellular aging, such as progressive changes in size, doubling time, or sibling health. Genetic perturbations and drugs can extend the RLS via an aging-independent mechanism. Using a quantitative model to analyze these results, we conclude that fission yeast does not age and that cellular aging and replicative lifespan can be uncoupled in a eukaryotic cell.","doi":"10.7554/eLife.20340","authors":"Spivey EC, Jones SK, Rybarski JR, Saifuddin FA, Finkelstein IJ","authors_abbrev":"Spivey EC et al.","pubmed_publication_date":"31 Jan 2017","pubmed_entrez_date":"2017-02-01","publication_year":"2017","canto_session_key":"1546ab1e69ca08cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-02-28 15:46:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-02-28 15:46:34","canto_added_date":"2017-02-02 01:15:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPBC16D10.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-02-28"},{"uniquename":"PMID:20624975","title":"A non-ring-like form of the Dam1 complex modulates microtubule dynamics in fission yeast.","citation":"Proc Natl Acad Sci U S A 2010 Jul 27;107(30):13330-5","abstract":"The Dam1 complex is a kinetochore component that couples chromosomes to the dynamic ends of kinetochore microtubules (kMTs). Work in the budding yeast Saccharomyces cerevisiae has shown that the Dam1 complex forms a 16-unit ring encircling and tracking the tip of a MT in vitro, consistent with its cellular function as a coupler. Dam1 also forms smaller, nonring patches in vitro that track the dynamic ends of MTs. However, the identity of Dam1's functional form in vivo remains unknown. Here we report a comprehensive in vivo characterization of Dam1 in the fission yeast Schizosaccharomyces pombe. In addition to their dense localizations on kinetochores and spindle MTs during mitosis, we identify that Dam1 is also localized onto cytoplasmic MTs as discrete spots in interphase, providing the unique opportunity to analyze Dam1 oligomers at the single-particle resolution in live cells. Such analysis shows that each oligomer contains one to five copies of Dam1, and is able to \"switch-rail\" while moving along MTs, precluding the possibility of a 16-unit encircling structure. Dam1 patches track the plus ends of the shortening, but not the elongating, MTs and retard MT depolymerization. Together with Mal3, the EB1-like MT-interacting protein, cytoplasmic Dam1 plays an important role in maintaining proper cell shape. In mitosis, kinetochore-associated Dam1 appears to facilitate kMT depolymerization. Together, our findings suggest that patches, instead of rings, are the physiologically functional forms of Dam1 in pombe. Our findings help establish the benchmark parameters of the Dam1 coupler and elucidate the mechanism of its functions.","doi":"10.1073/pnas.1004887107","authors":"Gao Q, Courtheoux T, Gachet Y, Tournier S, He X","authors_abbrev":"Gao Q et al.","pubmed_publication_date":"27 Jul 2010","pubmed_entrez_date":"2010-07-14","publication_year":"2010","canto_session_key":"9754872522d7e5a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-08-22 21:18:12","canto_approved_date":"2021-04-06 18:29:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-27 07:41:59","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27.02c","SPAC1805.07c","SPAC18G6.15","SPAC589.08c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-08-22"},{"uniquename":"PMID:28528978","title":"Multimodal control of transcription factor Pap1 in Schizosaccharomyces pombe under nitrosative stress.","citation":"Biochem Biophys Res Commun 2017 Jul 15;489(1):42-47","abstract":"Schizosaccharomyces pombe Pap1, a bZIP transcription factor, is highly homologous to the mammalian c-Jun protein that belongs to the AP1 family of transcriptional regulators. The role of transcription factor Pap1 has been extensively studied under oxidative stress. Two cysteine residues in Pap1p namely, C278 and C501 form disulfide linkage under oxidative stress resulting in nuclear accumulation. We first time showed the involvement of Pap1 in the protection against nitrosative stress. In the present study we show that pap1 deletion makes growth of S. pombe sensitive to nitrosative stress. pap1 deletion also causes delayed recovery in terms of mitotic index under nitrosative stress. Our flow cytometry data shows that pap1 deletion causes slower recovery from the slowdown of DNA replication under nitrosative stress. This is the first report where we show that Pap1 transcription factor is localized in the nucleus under nitrosative stress. From our study it is evident that nuclear localization of Pap1 under nitrosative stress was not due to reactive oxygen species formation.","doi":"10.1016/j.bbrc.2017.05.100","authors":"Kar P, Biswas P, Ghosh S","authors_abbrev":"Kar P et al.","pubmed_publication_date":"15 Jul 2017","pubmed_entrez_date":"2017-05-23","publication_year":"2017","canto_session_key":"66f5ae4fde8d7440","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-05-24 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20062003","title":"Hairpin RNA induces secondary small interfering RNA synthesis and silencing in trans in fission yeast.","citation":"EMBO Rep 2010 Feb;11(2):112-8","abstract":"RNA interference (RNAi) is widespread in eukaryotes and regulates gene expression transcriptionally or post-transcriptionally. In fission yeast, RNAi is tightly coupled to template transcription and chromatin modifications that establish heterochromatin in cis. Exogenous double-stranded RNA (dsRNA) triggers seem to induce heterochromatin formation in trans only when certain silencing proteins are overexpressed. Here, we show that green fluorescent protein (GFP) hairpin dsRNA allows production of high levels of Argonaute-associated small interfering RNAs (siRNAs), which can induce heterochromatin formation at a remote locus. This silencing does not require any manipulation apart from hairpin expression. In cells expressing a ura4(+)-GFP fusion gene, production of GFP siRNAs causes the appearance of ura4 siRNAs from the target gene. Production of these secondary siRNAs depends on RNA-dependent RNA polymerase Rdp1 (RDRP(Rdp1)) function and other RNAi pathway components. This demonstrates that transitivity occurs in fission yeast and implies that RDRP(Rdp1) can synthesize RNA from targeted RNA templates in vivo, generating siRNAs not homologous to the hairpin.","doi":"10.1038/embor.2009.273","authors":"Simmer F, Buscaino A, Kos-Braun IC, Kagansky A, Boukaba A, Urano T, Kerr AR, Allshire RC","authors_abbrev":"Simmer F et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2010-01-12","publication_year":"2010","canto_session_key":"8e81367dbe1eb41c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-12-19 14:13:25","canto_approved_date":"2020-03-15 12:49:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-26 11:38:39","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPCC736.11","SPBC16D10.07c","SPAC18G6.02c","SPAC140.03","SPAC6F12.09","SPAC664.01c","SPBC800.03","SPCC188.13c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2019-12-19"},{"uniquename":"PMID:12868594","title":"In situ localization of cell wall alpha-1,3-glucan in the fission yeast Schizosaccharomyces pombe.","citation":"J Electron Microsc (Tokyo) 2003;52(2):237-42","abstract":"The yeast cell walls of the budding yeast Saccharomyces cerevisiae are well studied and the results show the existence of a framework composed of beta-1,3-glucan. It is reported that the cell wall of the fission yeast Schizosaccharomyces pombe has different components and our analysis by 13C-nuclear magnetic resonance (NMR) spectroscopy also showed there is alpha-1,3-glucan in its cell wall. To refine our understanding of the architecture of the yeast cell wall, we re-examined the cell wall glucans of S. pombe by NMR spectroscopy and prepared antibody against alpha-1,3-glucan, which is a characteristic component of this yeast. By the competitive enzyme-linked immunosorbent assay (ELISA) system, specificity of the antibody was restricted to alpha-1,3-glucan, which did not take a highly ordered structure. We analysed the localization of the cell wall glucans by immunoelectron microscopy. Transmission electron microscope (TEM) images showed that most of the alpha-1,3-glucan was along the cell membrane and appeared to enclose the cytoplasm, supporting previous reports that this glucan is synthesized on the cell membrane.","authors":"Sugawara T, Sato M, Takagi T, Kamasaki T, Ohno N, Osumi M","authors_abbrev":"Sugawara T et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-07-19","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2031714","title":"Two pathways in the biosynthesis of cadystins (gamma EC)nG in the cell-free system of the fission yeast.","citation":"Biochem Cell Biol 1991;69(2-3):115-21","abstract":"Small metal-binding peptides, cadystins, with the general structure of (gamma-Glu-Cys)n-Gly ((gamma EC)nG), were synthesized in a cell-free system of fission yeast to examine the in vivo synthetic pathway. The crude enzyme for cadystin synthesis was prepared by ammonium sulfate precipitation (75% saturation) from the 120,000 x g supernatant of the cell extract, and the excess salt in the enzyme fraction was removed by Sephadex gel filtration. Using this crude enzyme fraction, it was shown that there were two pathways for cadystin biosynthesis. One pathway is gamma-Glu-Cys (gamma EC) dipeptidyl transfer from both glutathione (gamma ECG) and cadystins to glutathione and cadystins. The other one is gamma EC polymerization from (gamma EC)n and glutathione to (gamma EC)n + i, followed by glycine addition with glutathione synthetase.","authors":"Hayashi Y, Nakagawa CW, Mutoh N, Isobe M, Goto T","authors_abbrev":"Hayashi Y et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-02-01","publication_year":"1991","canto_session_key":"9cf01076aeef20c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-11-14 14:08:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-08 21:03:32","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-11-08"},{"uniquename":"PMID:21775631","title":"The fission yeast pleckstrin homology domain protein Spo7 is essential for initiation of forespore membrane assembly and spore morphogenesis.","citation":"Mol Biol Cell 2011 Sep;22(18):3442-55","abstract":"Sporulation in fission yeast represents a unique mode of cell division in which a new cell is formed within the cytoplasm of a mother cell. This event is accompanied by formation of the forespore membrane (FSM), which becomes the plasma membrane of spores. At prophase II, the spindle pole body (SPB) forms an outer plaque, from which formation of the FSM is initiated. Several components of the SPB play an indispensable role in SPB modification, and therefore in sporulation. In this paper, we report the identification of a novel SPB component, Spo7, which has a pleckstrin homology (PH) domain. We found that Spo7 was essential for initiation of FSM assembly, but not for SPB modification. Spo7 directly bound to Meu14, a component of the leading edge of the FSM, and was essential for proper localization of Meu14. The PH domain of Spo7 had affinity for phosphatidylinositol 3-phosphate (PI3P). spo7 mutants lacking the PH domain showed aberrant spore morphology, similar to that of meu14 and phosphatidylinositol 3-kinase (pik3) mutants. Our study suggests that Spo7 coordinates formation of the leading edge and initiation of FSM assembly, thereby accomplishing accurate formation of the FSM.","doi":"10.1091/mbc.E11-02-0125","authors":"Nakamura-Kubo M, Hirata A, Shimoda C, Nakamura T","authors_abbrev":"Nakamura-Kubo M et al.","pubmed_publication_date":"Sep 2011","pubmed_entrez_date":"2011-07-22","publication_year":"2011","canto_session_key":"4794f2ac68f1b5ba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-06 14:29:34","canto_approved_date":"2022-02-07 20:35:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-20 05:51:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.06c","SPCC1183.12","SPAC6G9.04","SPBC32H8.11","SPBC1347.03","SPBC16C6.14"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-09-06"},{"uniquename":"PMID:12093372","title":"Fission yeast enters a joyful new era.","citation":"Genome Biol 2002;3(6):REPORTS4017","abstract":"A report on the Second International Fission Yeast Meeting, Kyoto, Japan, 25-30 March 2002.","authors":"Gómez EB, Bailis JM, Forsburg SL","authors_abbrev":"Gómez EB et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-07-03","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24475199","title":"Silencing motifs in the Clr2 protein from fission yeast, Schizosaccharomyces pombe.","citation":"PLoS One 2014;9(1):e86948","abstract":"The fission yeast, Schizosaccharomyces pombe, is a well-established model for heterochromatin formation, but the exact sequence of events for initiation remains to be elucidated. The essential factors involved include RNA transcribed from repeated sequences together with the methyltransferase Clr4. In addition, histone deacetylases, like Clr3, found in the SHREC complex are also necessary for transcriptional silencing. Clr2 is another crucial factor required for heterochromatin formation found in the SHREC complex. The function of Clr2 has been difficult to establish due to the lack of conserved domains or homology to proteins of known molecular function. Using a bioinformatics approach, three conserved motifs in Clr2 were identified, which contained amino acids important for transcriptional repression. Analysis of clr2 mutant strains revealed a major role for Clr2 in mating-type and rDNA silencing, and weaker effects on centromeric silencing. The effect on mating-type silencing showed variegation in several of the strains with mutated versions of Clr2 indicating an establishment or maintenance defect. Moreover, the critical amino acids in Clr2 were also necessary for transcriptional repression in a minimal system, by the tethering of Clr4 upstream of a reporter gene, inserted into the euchromatic part of the genome. Finally, in silico modeling suggested that the mutations in Clr2 cause disruption of secondary structures in the Clr2 protein. Identification of these critical amino acids in the protein provides a useful tool to explore the molecular mechanism behind the role of Clr2 in heterochromatin formation.","doi":"10.1371/journal.pone.0086948","authors":"Steinhauf D, Rodriguez A, Vlachakis D, Virgo G, Maksimov V, Kristell C, Olsson I, Linder T, Kossida S, Bongcam-Rudloff E, Bjerling P","authors_abbrev":"Steinhauf D et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-01-30","publication_year":"2014","canto_session_key":"ebd7df89af69aecb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pernilla Bjerling","canto_approved_date":"2014-03-20 15:29:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-03-16 19:12:47","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pernilla Bjerling","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-03-16"},{"uniquename":"PMID:33137119","title":"TOR Complex 2- independent mutations in the regulatory PIF pocket of Gad8AKT1/SGK1 define separate branches of the stress response mechanisms in fission yeast.","citation":"PLoS Genet 2020 Nov;16(11):e1009196","abstract":"The Target of rapamycin (TOR) protein kinase forms part of TOR complex 1 (TORC1) and TOR complex 2 (TORC2), two multi-subunit protein complexes that regulate growth, proliferation, survival and developmental processes by phosphorylation and activation of AGC-family kinases. In the fission yeast, Schizosaccharomyces pombe, TORC2 and its target, the AGC kinase Gad8 (an orthologue of human AKT or SGK1) are required for viability under stress conditions and for developmental processes in response to starvation cues. In this study, we describe the isolation of gad8 mutant alleles that bypass the requirement for TORC2 and reveal a separation of function of TORC2 and Gad8 under stress conditions. In particular, osmotic and nutritional stress responses appear to form a separate branch from genotoxic stress responses downstream of TORC2-Gad8. Interestingly, TORC2-independent mutations map into the regulatory PIF pocket of Gad8, a highly conserved motif in AGC kinases that regulates substrate binding in PDK1 (phosphoinositide dependent kinase-1) and kinase activity in several AGC kinases. Gad8 activation is thought to require a two-step mechanism, in which phosphorylation by TORC2 allows further phosphorylation and activation by Ksg1 (an orthologue of PDK1). We focus on the Gad8-K263C mutation and demonstrate that it renders the Gad8 kinase activity independent of TORC2 in vitro and independent of the phosphorylation sites of TORC2 in vivo. Molecular dynamics simulations of Gad8-K263C revealed abnormal high flexibility at T387, the phosphorylation site for Ksg1, suggesting a mechanism for the TORC2-independent Gad8 activity. Significantly, the K263 residue is highly conserved in the family of AGC-kinases, which may suggest a general way of keeping their activity in check when acting downstream of TOR complexes.","doi":"10.1371/journal.pgen.1009196","authors":"Pataki E, Simhaev L, Engel H, Cohen A, Kupiec M, Weisman R","authors_abbrev":"Pataki E et al.","pubmed_publication_date":"Nov 2020","pubmed_entrez_date":"2020-11-02","publication_year":"2020","canto_session_key":"1f7c9dd717c9f378","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronit Weisman","canto_first_approved_date":"2021-04-15 16:14:05","canto_approved_date":"2024-03-28 12:26:59","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-04-06 13:08:14","canto_added_date":"2020-11-04 01:15:05","annotation_curators":[{"name":"Ronit Weisman","community_curator":true,"annotation_count":36,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC24B10.07","SPCC1259.13","SPBC16G5.15c","SPBC30D10.10c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2021-04-15"},{"uniquename":"PMID:9843966","title":"Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs.","citation":"Proc Natl Acad Sci U S A 1998 Dec 08;95(25):14781-6","abstract":"We previously provided evidence that the protein encoded by the highly conserved skb1 gene is a putative regulator of Shk1, a p21(Cdc42/Rac)-activated kinase (PAK) homolog in the fission yeast Schizosaccharomyces pombe. skb1 null mutants are viable and competent for mating but less elongate than wild-type S. pombe cells, whereas cells that overexpress skb1 are hyperelongated. These phenotypes suggest a possible role for Skb1 as a mitotic inhibitor. Here we show genetic interactions of both skb1 and shk1 with genes encoding key mitotic regulators in S. pombe. Our results indicate that Skb1 negatively regulates mitosis by a mechanism that is independent of the Cdc2-activating phosphatase Cdc25 but that is at least partially dependent on Shk1 and the Cdc2 inhibitory kinase Wee1. We provide biochemical evidence for association of Skb1 and Shk1 with Cdc2 in S. pombe, suggesting that Skb1 and Shk1 inhibit mitosis through interaction with the Cdc2 complex, rather than by an indirect mechanism. These results provide evidence of a previously undescribed role for PAK-related protein kinases as mitotic inhibitors. We also describe the cloning of a human homolog of skb1, SKB1Hs, and show that it can functionally replace skb1 in S. pombe. Thus, the molecular functions of Skb1-related proteins have likely been substantially conserved through evolution.","authors":"Gilbreth M, Yang P, Bartholomeusz G, Pimental RA, Kansra S, Gadiraju R, Marcus S","authors_abbrev":"Gilbreth M et al.","pubmed_publication_date":"08 Dec 1998","pubmed_entrez_date":"1998-12-09","publication_year":"1998","canto_session_key":"4c718237e0521f89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-21 15:45:41","canto_approved_date":"2019-06-14 13:02:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-04 16:28:41","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.14c","SPBC11B10.09","SPAC24H6.05","SPCC18B5.03","SPBC16H5.11c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-12-21"},{"uniquename":"PMID:8689692","title":"Chromosomal inheritance of epigenetic states in fission yeast during mitosis and meiosis.","citation":"Cell 1996 Jul 12;86(1):95-101","abstract":"Inheritance of the active and inactive states of gene expression by individual cells is crucial for development. In fission yeast, mating-type region consists of three loci called mat1, mat2, and mat3. Transcriptionally silent mat2 and mat3 loci are separated by a 15 kb interval, designated the K-region, and serve as donors of information for transcriptionally active mat1 interconversion. In a strain carrying replacement of 7.5 kb of the K-region with the ura4 gene, we discovered that ura4 silencing and efficiency of mating-type switching were covariegated and were regulated by an epigenetic mechanism. Genetic analyses demonstrated that epigenetic states were remarkably stable not only in mitosis but also in meiosis and were linked to the mating-type region. This study indicates that different epigenetic states are heritable forms of chromatin organization at the mat region.","authors":"Grewal SI, Klar AJ","authors_abbrev":"Grewal SI et al.","pubmed_publication_date":"12 Jul 1996","pubmed_entrez_date":"1996-07-12","publication_year":"1996","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11792817","title":"MTOC formation during mitotic exit in fission yeast.","citation":"J Cell Sci 2001 Dec;114(Pt 24):4521-32","abstract":"Microtubules polymerise from nucleation templates containing gamma tubulin. These templates are generally concentrated in discrete structures called microtubule organising centres (MTOCs). In Schizosaccharomyces pombe, an equatorial MTOC (EMTOC) forms mid-way through anaphase B and then disassembles during the final stages of cell separation. We show that the EMTOC was generated by recruiting gamma tubulin to the equatorial F-actin ring before it constricted to cleave the cell in two during cytokinesis. The EMTOC was not a continuous ring. It had a variable structure ranging from a horseshoe to a number of short bars. EMTOC integrity depended upon the integrity of the F-actin but not the microtubule cytoskeleton. EMTOC assembly required the activity of both the septation-inducing network (SIN) that regulates the onset of cytokinesis and the anaphase-promoting complex. Activation of the SIN in interphase cells induced F-actin ring formation and contraction and the synthesis of the primary septum but did not promote EMTOC assembly. In contrast, overproduction of the polo-like kinase, Plo1, which also induced multiple rounds of septation in interphase cells, induced EMTOC formation. Thus, the network governing EMTOC formation shared many of the regulatory elements that control cytokinesis but was more complex and revealed an additional function for Plo1 during mitotic exit.","authors":"Heitz MJ, Petersen J, Valovin S, Hagan IM","authors_abbrev":"Heitz MJ et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2002-01-17","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000117","title":"Electronic Gene Ontology annotations created by ARBA machine learning models","abstract":"Association-Rule-Based Annotator (ARBA) predicts Gene Ontology (GO) terms among other types of functional annotation such as Protein Description (DE), Keywords (KW), Enzyme Commission numbers (EC), subcellular LOcation (LO), etc. For all annotation types, reviewed UniProtKB/Swiss-Prot records having manual annotations as reference data are used to perform the machine learning phase and generate prediction models. For GO terms, ARBA has an additional feature to augment reference data using the relations between GO terms in the GO graph. The data augmentation is based on adding more general annotations into records containing manual GO terms, which will result in richer reference data. The predicted GO terms are then propagated to all unreviewed UniProtKB/TrEMBL proteins that meet the conditions of ARBA models. GO annotations using this technique receive the evidence code Inferred from Electronic Annotation (IEA; ECO:0000501).","authors":"UniProt","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC211.04c","SPAC18G6.09c","SPAC926.07c","SPBC31F10.07","SPCC1020.04c","SPBC4C3.05c","SPCC757.12","SPCC330.07c","SPAC19A8.01c","SPBC1348.05","SPBC146.13c","SPAC1805.05","SPCC645.13","SPCC4G3.05c","SPCC757.11c","SPCC1906.01","SPBC15D4.09c","SPAC1486.09","SPAPB1A10.10c","SPBC1709.16c","SPAC23C4.15","SPBC26H8.07c","SPAC1F3.05","SPAC20G8.08c","SPAC16A10.03c","SPCC290.02","SPBC405.04c","SPAC1952.16","SPAC31G5.16c","SPBC3B9.07c","SPBC336.10c","SPAC2F7.03c","SPBC530.01","SPAC1565.02c","SPAC27E2.09","SPCC31H12.04c","SPAC750.01","SPBC947.05c","SPAC26H5.02c","SPCC613.01","SPAC26F1.01","SPBC1289.07c","SPAC16E8.13","SPCC16A11.17","SPCC794.11c","SPAC31G5.08","SPAC1B2.05","SPCC63.02c","SPCC126.07c","SPBC25H2.16c","SPCC16C4.13c","SPBC2D10.20","SPBP23A10.07","SPAC1F8.04c","SPCC74.09","SPCC18.12c","SPBC4.05","SPBC19F5.04","SPAC7D4.05","SPAC17G8.04c","SPAC2F7.02c","SPBC4.04c","SPAC57A10.04","SPBC25D12.03c","SPAC25H1.09","SPAC4G8.04","SPCC613.02","SPAPB17E12.05","SPCC1827.06c","SPAC26H5.10c","SPBC30D10.05c","SPAC24H6.03","SPBPB2B2.16c","SPBC12D12.04c","SPCC1682.02c","SPAC19D5.04","SPAPYUK71.03c","SPBC1703.04","SPCC162.07","SPBC16E9.11c","SPAC521.03"],"gene_count":81,"ltp_gene_count":0},{"uniquename":"PMID:24576188","title":"Oxidative stress response pathways: Fission yeast as archetype.","citation":"Crit Rev Microbiol 2015;41(4):520-35","abstract":"Schizosaccharomyces pombe is a popular model eukaryotic organism to study diverse aspects of mammalian biology, including responses to cellular stress triggered by redox imbalances within its compartments. The review considers the current knowledge on the signaling pathways that govern the transcriptional response of fission yeast cells to elevated levels of hydrogen peroxide. Particular attention is paid to the mechanisms that yeast cells employ to promote cell survival in conditions of intermediate and acute oxidative stress. The role of the Sty1/Spc1/Phh1 mitogen-activated protein kinase in regulating gene expression at multiple levels is discussed in detail.","doi":"10.3109/1040841X.2013.870968","authors":"Papadakis MA, Workman CT","authors_abbrev":"Papadakis MA et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2014-03-01","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37395447","title":"Hop2-Mnd1 and Swi5-Sfr1 stimulate Dmc1 filament assembly using distinct mechanisms.","citation":"Nucleic Acids Res 2023 Sep 08;51(16):8550-8562","abstract":"In meiosis, Dmc1 recombinase and the general recombinase Rad51 are responsible for pairing homologous chromosomes and exchanging strands. Fission yeast (Schizosaccharomyces pombe) Swi5-Sfr1 and Hop2-Mnd1 stimulate Dmc1-driven recombination, but the stimulation mechanism is unclear. Using single-molecule fluorescence resonance energy transfer (smFRET) and tethered particle motion (TPM) experiments, we showed that Hop2-Mnd1 and Swi5-Sfr1 individually enhance Dmc1 filament assembly on single-stranded DNA (ssDNA) and adding both proteins together allows further stimulation. FRET analysis showed that Hop2-Mnd1 enhances the binding rate of Dmc1 while Swi5-Sfr1 specifically reduces the dissociation rate during the nucleation, about 2-fold. In the presence of Hop2-Mnd1, the nucleation time of Dmc1 filaments shortens, and doubling the ss/double-stranded DNA (ss/dsDNA) junctions of DNA substrates reduces the nucleation times in half. Order of addition experiments confirmed that Hop2-Mnd1 binds on DNA to recruit and stimulate Dmc1 nucleation at the ss/dsDNA junction. Our studies directly support the molecular basis of how Hop2-Mnd1 and Swi5-Sfr1 act on different steps during the Dmc1 filament assembly. DNA binding of these accessory proteins and nucleation preferences of recombinases thus dictate how their regulation can take place.","doi":"10.1093/nar/gkad561","authors":"Lee W, Iwasaki H, Tsubouchi H, Li HW","authors_abbrev":"Lee W et al.","pubmed_publication_date":"08 Sep 2023","pubmed_entrez_date":"2023-07-03","publication_year":"2023","canto_session_key":"8ead86a4172a0058","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-07-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22730331","title":"Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions.","citation":"J Biol Chem 2012 Aug 24;287(35):29610-9","abstract":"Protein modification by SUMO and ubiquitin critically impacts genome stability via effectors that \"read\" their signals using SUMO interaction motifs or ubiquitin binding domains, respectively. A novel mixed SUMO and ubiquitin signal is generated by the SUMO-targeted ubiquitin ligase (STUbL), which ubiquitylates SUMO conjugates. Herein, we determine that the \"ubiquitin-selective\" segregase Cdc48-Ufd1-Npl4 also binds SUMO via a SUMO interaction motif in Ufd1 and can thus act as a selective receptor for STUbL targets. Indeed, we define key cooperative DNA repair functions for Cdc48-Ufd1-Npl4 and STUbL, thereby revealing a new signaling mechanism involving dual recruitment by SUMO and ubiquitin for Cdc48-Ufd1-Npl4 functions in maintaining genome stability.","doi":"10.1074/jbc.M112.379768","authors":"Nie M, Aslanian A, Prudden J, Heideker J, Vashisht AA, Wohlschlegel JA, Yates JR, Boddy MN","authors_abbrev":"Nie M et al.","pubmed_publication_date":"24 Aug 2012","pubmed_entrez_date":"2012-06-26","publication_year":"2012","canto_session_key":"fef47d2ff1397ae5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Michael Boddy","canto_first_approved_date":"2016-08-24 15:37:02","canto_approved_date":"2026-01-29 12:01:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-27 19:23:39","canto_added_date":"2013-01-03 02:47:35","annotation_curators":[{"name":"Michael Boddy","community_curator":true,"annotation_count":143,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":121,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP8B7.19","SPAP7G5.02c","SPAC15A10.07","SPBC577.08c","SPAC29E6.06c","SPAC5H10.03","SPCC1223.07c","SPAC3F10.13","SPAP8A3.09c","SPBC30D10.03c","SPBC1711.10c","SPAC17A2.05","SPAC222.09","SPAC694.02","SPBC1861.08c","SPAC4F8.12c","SPBC4F6.17c","SPBC1778.07","SPAC26F1.13c","SPAPB17E12.14c","SPBC23E6.02","SPBC16H5.10c","SPBC17D11.01","SPBC25D12.02c","SPCC188.09c","SPBC9B6.10","SPAC26F1.03","SPAC16C9.01c","SPAC13C5.04","SPAC1296.02","SPBC646.13","SPBC26H8.07c","SPBC713.07c","SPAC23G3.12c","SPBC31F10.12","SPBC365.06","SPCC18.18c","SPBP8B7.31","SPCC1840.05c","SPAC12G12.07c","SPBC12C2.04","SPCC1919.09","SPBC23G7.07c","SPAPB17E12.13","SPBC17D11.05","SPBP23A10.11c","SPAC24C9.12c","SPAC4C5.04","SPCC16C4.10","SPAC1805.16c","SPBC106.04","SPBC3E7.08c","SPBC4.03c","SPBC16A3.09c","SPAC23H4.10c","SPBC1604.09c","SPBC4F6.18c","SPCC16C4.09","SPBC725.08","SPBC530.04","SPAC1002.12c","SPAC144.12","SPBC1539.09c","SPAC144.05","SPCC1223.08c","SPCC63.14","SPAC30D11.13","SPBC3E7.01","SPCC1322.14c","SPCC1442.04c","SPACUNK4.16c","SPAC6G9.07c","SPAC15E1.03","SPBC660.07","SPBC16G5.01","SPBC16G5.11c","SPCC594.01","SPAC328.03","SPAC57A10.10c","SPAC1565.08","SPBC16H5.03c","SPCC576.10c","SPAC13F5.05","SPCC1259.13","SPBC25H2.05","SPBC4B4.09","SPCC1183.02","SPBC1711.12","SPCC330.09","SPBC2G2.12","SPAC17G8.04c","SPCC550.06c","SPCC622.15c","SPAC644.15","SPAC1142.02c","SPBC1198.14c","SPBC1703.14c","SPCC737.06c","SPAC10F6.06","SPAPB17E12.05","SPAC30D11.04c","SPBC3D6.06c","SPBC2G2.04c","SPCP31B10.05","SPAC3A11.10c","SPAC4A8.12c","SPAC1B1.03c","SPBP4H10.12","SPBC1105.01","SPCC1020.10","SPBC3D6.11c","SPAC17H9.13c","SPAC3G9.03","SPBC4C3.05c","SPBC19C7.06","SPBP35G2.07","SPCC1739.12","SPBC1105.02c","SPAC6G10.09","SPAC2C4.16c","SPBC342.02","SPBC4B4.07c","SPAC6F6.10c","SPBC3H7.15","SPAC630.03","SPAC6F12.13c","SPBC2F12.05c","SPAC25G10.01","SPBC1289.04c","SPBC1773.06c","SPBC4C3.07","SPAC23A1.14c","SPAC3H5.10","SPAC3F10.16c","SPBC428.03c","SPCC132.01c","SPCPB16A4.05c","SPCC1442.09","SPAC24B11.07c","SPAC4A8.16c","SPAC9.12c","SPAC1851.03","SPAC22H10.12c","SPBC21C3.13"],"gene_count":144,"ltp_gene_count":144,"approved_date":"2016-08-24"},{"uniquename":"PMID:36795330","title":"Heterologous Production of Calendic Acid Naturally Found in  Calendula officinalis  by Recombinant Fission Yeast.","citation":"J Agric Food Chem 2023 Mar 01;71(8):3842-3851","abstract":"Calendic acid (CA) is a conjugated fatty acid with anti-cancer properties that is widely present in seed oil of  Calendula officinalis . Using the co-expression of  C. officinalis  fatty acid conjugases (CoFADX-1 or CoFADX-2) and  Punica granatum  fatty acid desaturase (PgFAD2), we metabolically engineered the synthesis of CA in the yeast  Schizosaccharomyces pombe  without the need for linoleic acid (LA) supplementation. The highest CA titer and achieved accumulation were 4.4 mg/L and 3.7 mg/g of DCW in PgFAD2 + CoFADX-2 recombinant strain cultivated at 16 °C for 72 h, respectively. Further analyses revealed the accumulation of CA in free fatty acids (FFA) and downregulation of the  lcf1  gene encoding long-chain fatty acyl-CoA synthetase. The developed recombinant yeast system represents an important tool for the future identification of the essential components of the channeling machinery to produce CA as a high-value conjugated fatty acid at an industrial level.","doi":"10.1021/acs.jafc.2c08967","authors":"Garaiova M, Hua Q, Holic R","authors_abbrev":"Garaiova M et al.","pubmed_publication_date":"01 Mar 2023","pubmed_entrez_date":"2023-02-16","publication_year":"2023","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2023-02-17 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4419547","title":"The effect of mannose on the synthesis of the glycoprotein acid phosphatase in a mannose-deficient mutant of Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1974 Aug 07;362(1):13-6","abstract":"","authors":"Schmidt R, Jannsen S","authors_abbrev":"Schmidt R et al.","pubmed_publication_date":"07 Aug 1974","pubmed_entrez_date":"1974-08-07","publication_year":"1974","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38886153","title":"Ssu72 phosphatase deficiency leads to spindle crossing during the second meiotic division process.","citation":"Yi Chuan 2024 Jun 20;46(6):502-508","abstract":"Ssu72 is a component of the yeast cleavage/polyadenylation factor (CPF) complex, which catalyzes the dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II at S5-P and S7-P. It has been shown that Ssu72 phosphatase is involved in regulating chromosome cohesion during mitosis. To further clarify whether Ssu72 phosphatase affects chromosome separation during meiotic division in  Schizosaccharomyces pombe , we utilized green fluorescent protein (GFP) to label centromeres and red fluorescent protein to label microtubule protein Atb2. The entire meiotic chromosome separation process of  ssu72∆  cells was observed in real-time under fluorescence microscope. It was found that two spindles of  ssu72∆  cells crossed during the metaphase and anaphase of the second meiotic division, and this spindle crossing led to a new type of spore defect distribution pattern. The results of this study can provide important reference significance for studying the roles of phosphatase Ssu72 in higher organisms.","doi":"10.16288/j.yczz.24-047","authors":"Jing-Liang Y, Ling-Ling M, Yoshinori W","authors_abbrev":"Jing-Liang Y et al.","pubmed_publication_date":"20 Jun 2024","pubmed_entrez_date":"2024-06-17","publication_year":"2024","canto_session_key":"6c6b1ac4d74df5f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-10-05 12:31:01","canto_approved_date":"2024-10-05 12:31:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-09-26 09:42:11","canto_added_date":"2024-06-18 23:25:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-10-05"},{"uniquename":"PMID:11896182","title":"Microtubule organization in the green kingdom: chaos or self-order?","citation":"J Cell Sci 2002 Apr 01;115(Pt 7):1345-54","abstract":"Plant microtubule arrays differ fundamentally from their animal, fungal and protistan counterparts. These differences largely reflect the requirements of plant composite polymer cell walls and probably also relate to the acquisition of chloroplasts. Plant microtubules are usually dispersed and lack conspicuous organizing centres. The key to understanding this dispersed nature is the identification of proteins that interact with and regulate the spatial and dynamic properties of microtubules. Over the past decade, a number of these proteins have been uncovered, including numerous kinesin-related proteins and a 65 kDa class of structural microtubule-associated proteins that appear to be unique to plants. Mutational analysis has identified MOR1, a probable stabilizer of microtubules that is a homologue of the TOGp-XMAP215 class of high-molecular-weight microtubule-associated proteins, and a katanin p60 subunit homologue implicated in the severing of microtubules. The identification of these two proteins provides new insights into the mechanisms controlling microtubule assembly and dynamics, particularly in the dispersed cortical array found in highly polarized plant cells.","authors":"Wasteneys GO","authors_abbrev":"Wasteneys GO","pubmed_publication_date":"01 Apr 2002","pubmed_entrez_date":"2002-03-16","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30420521","title":"Shelterin and subtelomeric DNA sequences control nucleosome maintenance and genome stability.","citation":"EMBO Rep 2019 Jan;20(1)","abstract":"Telomeres and the shelterin complex cap and protect the ends of chromosomes. Telomeres are flanked by the subtelomeric sequences that have also been implicated in telomere regulation, although their role is not well defined. Here, we show that, in  Schizosaccharomyces pombe , the telomere-associated sequences (TAS) present on most subtelomeres are hyper-recombinogenic, have metastable nucleosomes, and unusual low levels of H3K9 methylation. Ccq1, a subunit of shelterin, protects TAS from nucleosome loss by recruiting the heterochromatic repressor complexes CLRC and SHREC, thereby linking nucleosome stability to gene silencing. Nucleosome instability at TAS is independent of telomeric repeats and can be transmitted to an intrachromosomal locus containing an ectopic TAS fragment, indicating that this is an intrinsic property of the underlying DNA sequence. When telomerase recruitment is compromised in cells lacking Ccq1, DNA sequences present in the TAS promote recombination between chromosomal ends, independent of nucleosome abundance, implying an active function of these sequences in telomere maintenance. We propose that Ccq1 and fragile subtelomeres co-evolved to regulate telomere plasticity by controlling nucleosome occupancy and genome stability.","doi":"10.15252/embr.201847181","authors":"van Emden TS, Forn M, Forné I, Sarkadi Z, Capella M, Martín Caballero L, Fischer-Burkart S, Brönner C, Simonetta M, Toczyski D, Halic M, Imhof A, Braun S","authors_abbrev":"van Emden TS et al.","pubmed_publication_date":"Jan 2019","pubmed_entrez_date":"2018-11-14","publication_year":"2019","canto_session_key":"e11600463e2f304a","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-06-22 16:23:44","canto_added_date":"2018-11-15 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30035712","title":"Gating mechanisms during actin filament elongation by formins.","citation":"Elife 2018 Jul 23;7","abstract":"Formins play an important role in the polymerization of unbranched actin filaments, and particular formins slow elongation by 5-95%. We studied the interactions between actin and the FH2 domains of formins Cdc12, Bni1 and mDia1 to understand the factors underlying their different rates of polymerization. All-atom molecular dynamics simulations revealed two factors that influence actin filament elongation and correlate with the rates of elongation. First, FH2 domains can sterically block the addition of new actin subunits. Second, FH2 domains flatten the helical twist of the terminal actin subunits, making the end less favorable for subunit addition. Coarse-grained simulations over longer time scales support these conclusions. The simulations show that filaments spend time in states that either allow or block elongation. The rate of elongation is a time-average of the degree to which the formin compromises subunit addition rather than the formin-actin complex literally being in 'open' or 'closed' states.","doi":"10.7554/eLife.37342","authors":"Aydin F, Courtemanche N, Pollard TD, Voth GA","authors_abbrev":"Aydin F et al.","pubmed_publication_date":"23 Jul 2018","pubmed_entrez_date":"2018-07-24","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-07-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8006074","title":"Analysis of the Schizosaccharomyces pombe cyclin puc1: evidence for a role in cell cycle exit.","citation":"J Cell Sci 1994 Mar;107 ( Pt 3):601-13","abstract":"The puc1+ gene, encoding a G1-type cyclin from the fission yeast Schizosaccharomyces pombe, was originally isolated by complementation in the budding yeast Saccharomyces cerevisiae. Here, we report the molecular characterization of this gene and analyse its role in S. pombe. We fail to identify any function of this cyclin at the mitotic G1/S transition in S. pombe, but demonstrate that it does function in exit from the mitotic cycle. Expression of the puc1+ gene is increased during nitrogen starvation, and puc1 affects the timing of sexual development in response to starvation. Overexpression of the puc1 protein blocks sexual development, and rescues pat1ts cells, which would otherwise undergo a lethal meiosis. We conclude that puc1 contributes to negative regulation of the timing of sexual development in fission yeast, and functions at the transition between cycling and non-cycling cells.","authors":"Forsburg SL, Nurse P","authors_abbrev":"Forsburg SL et al.","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_session_key":"a265654194a9e17a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-09 22:49:33","canto_approved_date":"2019-06-14 12:31:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-06-09 22:49:25","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC4E9.02","SPCC18B5.03","SPBC19C2.05","SPBC19F5.01c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-06-09"},{"uniquename":"PMID:19531030","title":"Production of heterologous proteins using the fission-yeast (Schizosaccharomyces pombe) expression system.","citation":"Biotechnol Appl Biochem 2009 Jun 22;53(Pt 4):227-35","abstract":"The fission yeast Schizosaccharomyces pombe is a particularly useful model for studying the function and regulation of genes from higher eukaryotes. The genome of Sc. pombe has been sequenced, and DNA microarray, proteome and transcriptome analyses have been carried out. Among the well-characterized yeast species, Sc. pombe is considered an attractive host for the production of heterologous proteins. Expression vectors for high-level expression in Sc. pombe have been developed and many foreign proteins have been successfully expressed. However, further improvements in the protein-expressing host systems are still required for the production of heterologous proteins involved in post-translational modification, metabolism and intracellular trafficking. This minireview focuses on recent advances in heterologous protein production by use of engineered fission-yeast strains.","doi":"10.1042/BA20090048","authors":"Takegawa K, Tohda H, Sasaki M, Idiris A, Ohashi T, Mukaiyama H, Giga-Hama Y, Kumagai H","authors_abbrev":"Takegawa K et al.","pubmed_publication_date":"22 Jun 2009","pubmed_entrez_date":"2009-06-18","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19942659","title":"Characterization of two different types of UDP-glucose/-galactose 4-epimerase involved in galactosylation in fission yeast.","citation":"Microbiology (Reading) 2010 Mar;156(Pt 3):708-718","abstract":"Schizosaccharomyces species are currently the only known organisms with two types of genes encoding UDP-glucose/-galactose 4-epimerase, uge1(+) and gal10(+). A strain deleted for uge1(+) exhibited a severe galactosylation defect and a decrease in activity and in UDP-galactose content when grown in glucose-rich medium (2 % glucose), indicating that Uge1p is a major UDP-glucose/-galactose 4-epimerase under these growth conditions. In contrast, gal10(+) was efficiently expressed and involved in galactosylation of cell-surface proteins in low-glucose medium (0.1 % glucose and 2 % glycerol), but not in galactose-containing medium. In a uge1Deltagal10Delta strain, the galactosylation defect was suppressed and UDP-galactose content restored to wild-type levels in galactose-containing medium. Disruption of gal7(+), encoding galactose-1-phosphate uridylyltransferase, in the uge1Deltagal10Delta strain reversed suppression of the galactosylation defect and reduced levels of UDP-galactose, indicating that galactose is transported from the medium to the cytosol and is converted into UDP-galactose via galactose 1-phosphate by Gal7p in Sch. pombe.","doi":"10.1099/mic.0.035279-0","authors":"Suzuki S, Matsuzawa T, Nukigi Y, Takegawa K, Tanaka N","authors_abbrev":"Suzuki S et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2009-11-28","publication_year":"2010","canto_session_key":"17a6a3be58a90b9c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-04-16 16:33:12","canto_approved_date":"2025-12-03 12:21:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-19 16:01:05","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.14c","SPBPB2B2.10c","SPBPB2B2.12c","HGNC:4116","SPCC1795.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2020-04-16"},{"uniquename":"PMID:35553986","canto_session_key":"380998dd37694dec","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-05-15 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24755092","title":"Cotranslational protein-RNA associations predict protein-protein interactions.","citation":"BMC Genomics 2014 Apr 22;15:298","abstract":"Most cellular proteins function as part of stable protein complexes. We recently showed that around 38% of proteins associate with mRNAs that encode interacting proteins, reflecting the cotranslational formation of the complex between the bait protein and the nascent peptides encoded by the interacting mRNAs. Here we hypothesise that these cotranslational protein-mRNA associations can be used to predict protein-protein interactions.\nWe found that the fission yeast Exo2 protein, which encodes an exonuclease of the XRN1 family, coimmunoprecipitates with the eti1 mRNA, which codes for a protein of unknown function and uninformative sequence. Based on this protein-mRNA association, we predicted that the Exo2 and Eti1 protein are part of the same complex, and confirmed this hypothesis by coimmunoprecipitation and colocalization of the proteins. Similarly, we show that the cotranslational interaction between the Sty1 MAP kinase and the cip2 mRNA, which encodes an RNA-binding protein, predicts a complex between Sty1 and Cip2.\nOur results demonstrate that cotranslational protein-mRNA associations can be used to identify new components of protein complexes.","doi":"10.1186/1471-2164-15-298","authors":"Duncan CD, Mata J","authors_abbrev":"Duncan CD et al.","pubmed_publication_date":"22 Apr 2014","pubmed_entrez_date":"2014-04-24","publication_year":"2014","canto_session_key":"6edf172f7a86963f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juan Mata","canto_first_approved_date":"2014-11-24 12:18:37","canto_approved_date":"2025-09-03 17:51:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-13 17:01:19","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Juan Mata","community_curator":true,"annotation_count":2,"orcid":"0000-0002-5514-3653","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.04c","SPAC12G12.09","SPBC19G7.10c","SPAC17A5.14","SPAC12G12.03","SPAC24B11.06c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2014-11-24"},{"uniquename":"PMID:27270696","title":"A Brief History of Schizosaccharomyces pombe Research: A Perspective Over the Past 70 Years.","citation":"Genetics 2016 Jun;203(2):621-9","abstract":"Since its humble start as a model organism in two European laboratories in the 1940s and 1950s, the fission yeast Schizosaccharomyces pombe has grown to become one of the best-studied eukaryotes today. This article outlines the way in which interest in S. pombe developed and spread from Europe to Japan, North America, and elsewhere from its beginnings up to the first International Meeting devoted to this yeast in 1999. We describe the expansion of S. pombe research during this period with an emphasis on many of the individual researchers involved and their interactions that resulted in the development of today's vibrant community.","doi":"10.1534/genetics.116.189407","authors":"Fantes PA, Hoffman CS","authors_abbrev":"Fantes PA et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-06-09","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-06-10 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9135148","title":"p56(chk1) protein kinase is required for the DNA replication checkpoint at 37 degrees C in fission yeast.","citation":"EMBO J 1997 Mar 17;16(6):1332-41","abstract":"Fission yeast p56(chk1) kinase is known to be involved in the DNA damage checkpoint but not to be required for cell cycle arrest following exposure to the DNA replication inhibitor hydroxyurea (HU). For this reason, p56(chk1) is considered not to be necessary for the DNA replication checkpoint which acts through the inhibitory phosphorylation of p34(cdc2) kinase activity. In a search for Schizosaccharomyces pombe mutants that abolish the S phase cell cycle arrest of a thermosensitive DNA polymerase delta strain at 37 degrees C, we isolated two chk1 alleles. These alleles are proficient for the DNA damage checkpoint, but induce mitotic catastrophe in several S phase thermosensitive mutants. We show that the mitotic catastrophe correlates with a decreased level of tyrosine phosphorylation of p34(cdc2). In addition, we found that the deletion of chk1 and the chk1 alleles abolish the cell cycle arrest and induce mitotic catastrophe in cells exposed to HU, if the cells are grown at 37 degrees C. These findings suggest that chk1 is important for the maintenance of the DNA replication checkpoint in S phase thermosensitive mutants and that the p56(chk1) kinase must possess a novel function that prevents premature activation of p34(cdc2) kinase under conditions of impaired DNA replication at 37 degrees C.","authors":"Francesconi S, Grenon M, Bouvier D, Baldacci G","authors_abbrev":"Francesconi S et al.","pubmed_publication_date":"17 Mar 1997","pubmed_entrez_date":"1997-03-17","publication_year":"1997","canto_session_key":"31a707ea44c981c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-08-17 15:33:53","canto_approved_date":"2021-01-06 17:27:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-03-17 16:15:29","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":102,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPAC1952.07","SPAC3H5.06c","SPBC336.04","SPBC11B10.09","SPAC20G8.01","SPAC20G4.04c","SPCC1259.13","SPAC8F11.07c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2018-08-17"},{"uniquename":"PMID:34928380","title":"Genome-wide chromosomal association of Upf1 is linked to Pol II transcription in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2022 Jan 11;50(1):350-367","abstract":"Although the RNA helicase Upf1 has hitherto been examined mostly in relation to its cytoplasmic role in nonsense mediated mRNA decay (NMD), here we report high-throughput ChIP data indicating genome-wide association of Upf1 with active genes in Schizosaccharomyces pombe. This association is RNase sensitive, correlates with Pol II transcription and mRNA expression levels. Changes in Pol II occupancy were detected in a Upf1 deficient (upf1Δ) strain, prevalently at genes showing a high Upf1 relative to Pol II association in wild-type. Additionally, an increased Ser2 Pol II signal was detected at all highly transcribed genes examined by ChIP-qPCR. Furthermore, upf1Δ cells are hypersensitive to the transcription elongation inhibitor 6-azauracil. A significant proportion of the genes associated with Upf1 in wild-type conditions are also mis-regulated in upf1Δ. These data envisage that by operating on the nascent transcript, Upf1 might influence Pol II phosphorylation and transcription.","doi":"10.1093/nar/gkab1249","authors":"De S, Edwards DM, Dwivedi V, Wang J, Varsally W, Dixon HL, Singh AK, Owuamalam PO, Wright MT, Summers RP, Hossain MN, Price EM, Wojewodzic MW, Falciani F, Hodges NJ, Saponaro M, Tanaka K, Azzalin CM, Baumann P, Hebenstreit D, Brogna S","authors_abbrev":"De S et al.","pubmed_publication_date":"11 Jan 2022","pubmed_entrez_date":"2021-12-20","publication_year":"2022","canto_session_key":"5b11cdbdf95534eb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-22 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2675898","title":"Regeneration and functional incorporation of bacteriorhodopsin in membranes of fission yeast but not in E. coli.","citation":"J Protein Chem 1989 Jun;8(3):345-6","abstract":"","authors":"Hildebrandt V","authors_abbrev":"Hildebrandt V","pubmed_publication_date":"Jun 1989","pubmed_entrez_date":"1989-06-01","publication_year":"1989","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9852950","title":"Vectors for the expression of tagged proteins in Schizosaccharomyces pombe.","citation":"Gene 1998 Oct 09;221(1):59-68","abstract":"A series of vectors is described which enables the episomal expression of proteins fused to different tag sequences in Schizosaccharomyces pombe. Proteins can be expressed with their amino termini fused to GFP/EGFP, three copies of the HA or Pk epitopes or a combined tag which contains two copies of the myc epitope and six histidine residues (MH). Fusion of the carboxyl terminus of a protein to a tag is possible with GFP/EGFP or Pk. Expression of the fusion proteins is controlled by the medium strength mutant version of the regulatable nmt1 promoter.","authors":"Craven RA, Griffiths DJ, Sheldrick KS, Randall RE, Hagan IM, Carr AM","authors_abbrev":"Craven RA et al.","pubmed_publication_date":"09 Oct 1998","pubmed_entrez_date":"1998-12-16","publication_year":"1998","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24425326","title":"An effective automated glucose sensor for fermentation monitoring and control.","citation":"World J Microbiol Biotechnol 1992 Jan;8(1):7-13","abstract":"An industrial glucose analyser was partnered to an automated injection system to evaluate glucose in the culture medium of a bioreactor. This sensor has been validated on continuous cultures ofSchizosaccharomyces pombe and continuous and fed-batch cultures ofSaccharomyces cerevisiae. In addition to the advantage of a more accurate process monitoring, the main interest of this sensor deals with the control of the substrate concentration to a prespecified reference signal. Several experiments have been carried out first to validate the sensor, then to control the process evolution.","doi":"10.1007/BF01200676","authors":"Queinnec I, Destruhaut C, Pourciel JB, Goma G","authors_abbrev":"Queinnec I et al.","pubmed_publication_date":"Jan 1992","pubmed_entrez_date":"2014-01-16","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 06:07:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22633956","title":"Taz1 enforces cell-cycle regulation of telomere synthesis.","citation":"Mol Cell 2012 Jun 29;46(6):797-808","abstract":"The dramatic telomerase-dependent overelongation of telomeres in cells lacking Taz1 (ortholog of human TRF1/TRF2) or Rap1 implicates these proteins in restraint of telomerase activity. However, the modes by which these proteins regulate telomerase remain mysterious. Here we show that the mechanisms underlying excessive telomerase activity differ markedly between taz1Δ and rap1Δ strains. Despite allowing elevated telomerase access, rap1Δ telomeres are processed and synthesized in a cell-cycle-constrained manner similar to that of wild-type cells. In contrast, taz1Δ telomeres are processed with little cell-cycle dependency and recruit telomerase over an abnormally wide range of cell-cycle stages. Furthermore, although taz1Δ telomeres experience transient attrition mediated by replication fork stalling, this is balanced not only by temporal expansion of the telomerase activity period, but also by markedly increased recruitment of telomerase and its accessory factor Est1, suggesting that stalled forks generate robust substrates for telomerase.","doi":"10.1016/j.molcel.2012.04.022","authors":"Dehé PM, Rog O, Ferreira MG, Greenwood J, Cooper JP","authors_abbrev":"Dehé PM et al.","pubmed_publication_date":"29 Jun 2012","pubmed_entrez_date":"2012-05-29","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20205354","title":"Mathematical modelling of eukaryotic DNA replication.","citation":"Chromosome Res 2010 Jan;18(1):147-61","abstract":"Eukaryotic DNA replication is a complex process. Replication starts at thousand origins that are activated at different times in S phase and terminates when converging replication forks meet. Potential origins are much more abundant than actually fire within a given S phase. The choice of replication origins and their time of activation is never exactly the same in any two cells. Individual origins show different efficiencies and different firing time probability distributions, conferring stochasticity to the DNA replication process. High-throughput microarray and sequencing techniques are providing increasingly huge datasets on the population-averaged spatiotemporal patterns of DNA replication in several organisms. On the other hand, single-molecule replication mapping techniques such as DNA combing provide unique information about cell-to-cell variability in DNA replication patterns. Mathematical modelling is required to fully comprehend the complexity of the chromosome replication process and to correctly interpret these data. Mathematical analysis and computer simulations have been recently used to model and interpret genome-wide replication data in the yeast Saccharomyces cerevisiae and Schizosaccharomyces pombe, in Xenopus egg extracts and in mammalian cells. These works reveal how stochasticity in origin usage confers robustness and reliability to the DNA replication process.","doi":"10.1007/s10577-009-9092-4","authors":"Hyrien O, Goldar A","authors_abbrev":"Hyrien O et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2010-03-06","publication_year":"2010","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9729425","title":"Trehalose-6P synthase is essential for trehalase activation triggered by glucose, nitrogen source or heat shock, but not by osmostress, in Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1998 Aug 24;1381(3):271-8","abstract":"Cells of Schizosaccharomyces pombe disrupted in the tps1+ gene, which encodes trehalose-6P synthase, were unable to increase trehalase activity in response to the addition of glucose or nitrogen source. Moreover, in contrast to normal cells, Deltatps1 cells did not increase trehalase activity by heat shock. Overexpression of tps1+ in cells devoid of trehalose-6P synthase restored the ability to increase trehalase after addition of nutrients or by heat shock. In glucose-repressed cells, which are normally refractory to the activation of trehalase by glucose, overexpression of tps1+ enabled the cells to increase trehalase activity upon addition of the sugar. Northern hybridisations were used to determine the level of mRNA for trehalase in normal and Deltatps1 cells. Transcription for trehalase was not significantly altered upon addition of glucose or nitrogen source, but increased markedly in heat-shocked cells even though trehalase activity remained unchanged in Deltatps1 cells. These findings provide evidence for a role of trehalose-6P synthase in the signalling pathway causing post-transcriptional activation of neutral trehalase induced by nutrients or heat shock. However, trehalase increased in Deltatps1 cells under hypertonic conditions suggesting the existence in Schiz. pombe of a distinct regulatory mechanism for enhancement of trehalase, specifically triggered by osmostress.","authors":"Cansado J, Vicente-Soler J, Soto T, Fernandez J, Gacto M","authors_abbrev":"Cansado J et al.","pubmed_publication_date":"24 Aug 1998","pubmed_entrez_date":"1998-09-05","publication_year":"1998","canto_session_key":"17c0501f20dc6e13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-19 15:05:31","canto_approved_date":"2024-12-03 11:56:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-03 16:04:18","canto_added_date":"2012-02-24 05:53:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.07","SPAC328.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-19"},{"uniquename":"PMID:26229103","title":"An antisense RNA-mediated mechanism eliminates a meiosis-specific copper-regulated transcript in mitotic cells.","citation":"J Biol Chem 2015 Sep 11;290(37):22622-37","abstract":"Sense and antisense transcripts produced from convergent gene pairs could interfere with the expression of either partner gene. In Schizosaccharomyces pombe, we found that the iss1(+) gene produces two transcript isoforms, including a long antisense mRNA that is complementary to the meiotic cum1(+) sense transcript, inhibiting cum1(+) expression in vegetative cells. Inhibition of cum1(+) transcription was not at the level of its initiation because fusion of the cum1(+) promoter to the lacZ gene showed that activation of the reporter gene occurs in response to low copper conditions. Further analysis showed that the transcription factor Cuf1 and conserved copper-signaling elements (CuSEs) are required for induction of cum1(+)-lacZ transcription under copper deficiency. Insertion of a multipartite polyadenylation signal immediately downstream of iss1(+) led to the exclusive production of a shorter iss1(+) mRNA isoform, thereby allowing accumulation of cum1(+) sense mRNA in copper-limited vegetative cells. This finding suggested that the long iss1(+) antisense mRNA could pair with cum1(+) sense mRNA, thereby producing double-stranded RNA molecules that could induce RNAi. We consistently found that mutant strains for RNAi (dcr1Δ, ago1Δ, rdp1Δ, and clr4Δ) are defective in selectively eliminating cum1(+) sense transcript in the G1 phase of the cell cycle. Taken together, these results describe the first example of a copper-regulated meiotic gene repressed by an antisense transcription mechanism in vegetative cells.","doi":"10.1074/jbc.M115.674556","authors":"Normant V, Beaudoin J, Labbé S","authors_abbrev":"Normant V et al.","pubmed_publication_date":"11 Sep 2015","pubmed_entrez_date":"2015-08-01","publication_year":"2015","canto_session_key":"388181eb2fa26607","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-02 00:19:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23177050","title":"Quantification and characterization of cell wall polysaccharides released by non-Saccharomyces yeast strains during alcoholic fermentation.","citation":"Int J Food Microbiol 2012 Nov 15;160(2):113-8","abstract":"In order to improve knowledge about the oenological characteristics of non-Saccharomyces yeast strains, and to reconsider their contribution to wine quality, we studied the release of polysaccharides by 13 non-Saccharomyces strains of different species (three wine yeasts, six grape yeasts, and three spoilage yeasts) during alcoholic fermentation in synthetic must. Three Saccharomyces cerevisiae strains were included for comparison. All of the non-Saccharomyces strains released polysaccharides into fermentation medium; the amount released depended on the yeast species, the number of cells formed and their physiological conditions. Normalizing the quantity of macromolecules released to the cell biomass revealed that most non-Saccharomyces strains produced a greater quantity of polysaccharides compared to S. cerevisiae strains after 7 and 14days of fermentation. This capacity was particularly expressed in the studied wine spoilage yeasts (Saccharomycodes ludwigii, Zygosaccharomyces bailii, and Brettanomyces bruxellensis). Chemical characterization of exocellular polysaccharides produced by non-Saccharomyces yeasts revealed them to essentially be mannoproteins with high mannose contents, ranging from 93% for S'codes. ludwigii to 73-74% for Pichia anomala and Starmerella bombicola. Protein contents varied from 9% for P. anomala to 29% for Z. bailii. These compositions were very similar to those of the S. cerevisiae strains, and to the chemical composition of the cell wall mannoproteins of different yeast species. The presence of galactose, in addition to mannose and glucose, in the exocellular polysaccharides released by Schizosaccharomyces pombe, confirmed the parietal nature of the polysaccharides released by non-Saccharomyces yeasts; only this species has a galactomannan located in the outer layer of the cell wall.","doi":"10.1016/j.ijfoodmicro.2012.10.007","authors":"Giovani G, Rosi I, Bertuccioli M","authors_abbrev":"Giovani G et al.","pubmed_publication_date":"15 Nov 2012","pubmed_entrez_date":"2012-11-27","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12682361","title":"The fission yeast TFIIB-related factor limits RNA polymerase III to a TATA-dependent pathway of TBP recruitment.","citation":"Nucleic Acids Res 2003 Apr 15;31(8):2108-16","abstract":"The RNA polymerase (pol) III-transcribed (e.g. tRNA and 5S rRNA) genes of traditionally studied organisms rely on gene-internal promoters that precisely position the initiation factor, TFIIIB, on the upstream promoter-less DNA. This is accomplished by the ability of the TFIIIB subunit, TFIIB-related factor (Brf1), to make stable protein-protein interactions with TATA-binding protein (TBP) and place it on the promoter-less upstream DNA. Unlike traditional model organisms, Schizosaccharomyces pombe tRNA and 5S rRNA genes contain upstream TATA promoters that are required to program functional pol III initiation complexes. In this study we demonstrate that S.pombe (Sp)Brf does not form stable interactions with TBP in the absence of DNA using approaches that do reveal stable association of TBP and S.cerevisiae (Sc)Brf1. Gel mobility analyses demonstrate that a TBP-TATA DNA complex can recruit SpBrf to a Pol III promoter. Consistent with this, overproduction of SpBrf in S.pombe increases the expression of a TATA-dependent, but not a TATA-less, suppressor tRNA gene. Since previous whole genome analysis also revealed TATA elements upstream of tRNA genes in Arabidopsis, this pathway may be more widespread than appreciated previously.","authors":"Huang Y, McGillicuddy E, Weindel M, Dong S, Maraia RJ","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"15 Apr 2003","pubmed_entrez_date":"2003-04-12","publication_year":"2003","canto_session_key":"89cf2d2967ce5748","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-05-24 18:33:55","canto_approved_date":"2021-01-02 05:27:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-01 11:37:06","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13F5.02c","SPBC13E7.10c","SPAC29E6.08","SPAC2G11.14"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-05-24"},{"uniquename":"PMID:27566474","title":"Culture medium optimization for osmotolerant yeasts by use of a parallel fermenter system and rapid microbiological testing.","citation":"J Microbiol Methods 2016 Nov;130:14-22","abstract":"In the present study, a culture medium for qualitative detection of osmotolerant yeasts, named OM, was developed. For the development, culture media with different concentrations of glucose, fructose, potassium chloride and glycerin were analyzed in a Biolumix™ test incubator. Selectivity for osmotolerant yeasts was guaranteed by a water activity (a w )-value of 0.91. The best results regarding fast growth of Zygosaccharomyces rouxii (WH 1002) were achieved in a culture medium consisting of 45% glucose, 5% fructose and 0.5% yeast extract and in a medium with 30% glucose, 10% glycerin, 5% potassium chloride and 0.5% yeast extract. Substances to stimulate yeast fermentation rates were analyzed in a RAMOS ®  parallel fermenter system, enabling online measurement of the carbon dioxide transfer rate (CTR) in shaking flasks. Significant increases of the CTR was achieved by adding especially 0.1-0.2% ammonium salts ((NH 4 ) 2 HPO 4 , (NH 4 ) 2 SO 4  or NH 4 NO 3 ), 0.5% meat peptone and 1% malt extract. Detection times and the CTR of 23 food-borne yeast strains of the genera Zygosaccharomyces, Torulaspora, Schizosaccharomyces, Candida and Wickerhamomyces were analyzed in OM bouillon in comparison to the selective culture media YEG50, MYG50 and DG18 in the parallel fermenter system. The OM culture medium enabled the detection of 10 2 CFU/g within a time period of 2-3days, depending on the analyzed yeast species. Compared with YEG50 and MYG50 the detection times could be reduced. As an example, W. anomalus (WH 1021) was detected after 124h in YEG50, 95.5h in MYG50 and 55h in OM bouillon. Compared to YEG50 the maximum CO 2  transfer rates for Z. rouxii (WH 1001), T. delbrueckii (DSM 70526), S. pombe (DSM 70576) and W. anomalus (WH 1016) increased by a factor ≥2.6. Furthermore, enrichment cultures of inoculated high-sugar products in OM culture medium were analyzed in the Biolumix™ system. The results proved that detection times of 3days for Z. rouxii and T. delbrueckii can be realized by using OM in combination with the automated test system even if low initial counts (10 1 CFU/g) are present in the products. In conclusion, the presented data suggest that the OM culture medium is appropriate for the enrichment of osmotolerant yeasts from high-sugar food products.","doi":"10.1016/j.mimet.2016.08.021","authors":"Pfannebecker J, Schiffer-Hetz C, Fröhlich J, Becker B","authors_abbrev":"Pfannebecker J et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-08-28","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-08-29 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27737912","title":"Atg20- and Atg24-family proteins promote organelle autophagy in fission yeast.","citation":"J Cell Sci 2016 Nov 15;129(22):4289-4304","abstract":"Autophagy cargos include not only soluble cytosolic materials but also bulky organelles, such as ER and mitochondria. In budding yeast, two proteins that contain the PX domain and the BAR domain, Atg20 and Atg24 (also known as Snx42 and Snx4, respectively) are required for organelle autophagy and contribute to general autophagy in a way that can be masked by compensatory mechanisms. It remains unclear why these proteins are important for organelle autophagy. Here, we show that in a distantly related fungal organism, the fission yeast Schizosaccharomyces pombe, autophagy of ER and mitochondria is induced by nitrogen starvation and is promoted by three Atg20- and Atg24-family proteins - Atg20, Atg24 and SPBC1711.11 (named here as Atg24b). These proteins localize at the pre-autophagosomal structure, or phagophore assembly site (PAS), during starvation. S. pombe Atg24 forms a homo-oligomer and acts redundantly with Atg20 and Atg24b, and the latter two proteins can form a hetero-oligomer. The organelle autophagy defect caused by the loss of these proteins is associated with a reduction of autophagosome size and a decrease in Atg8 accumulation at the PAS. These results provide new insights into the autophagic function of Atg20- and Atg24-family proteins.","authors":"Zhao D, Liu XM, Yu ZQ, Sun LL, Xiong X, Dong MQ, Du LL","authors_abbrev":"Zhao D et al.","pubmed_publication_date":"15 Nov 2016","pubmed_entrez_date":"2016-10-15","publication_year":"2016","canto_session_key":"27bd8acbaa46a888","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dan Zhao","canto_first_approved_date":"2018-04-17 13:50:36","canto_approved_date":"2023-10-02 01:53:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-17 05:24:02","canto_added_date":"2016-10-17 00:15:11","annotation_curators":[{"name":"Dan Zhao","community_curator":true,"annotation_count":37,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25A8.02","SPBC4B4.10c","SPAC7D4.04","SPAC9E9.14","SPAC10F6.11c","SPAC6F6.12","SPCC63.08c","SPBC1711.11","SPBC14F5.11c","SPAC140.01","SPAC7D4.15c","SPAC227.04","SPCC16A11.08","SPBC18H10.19","SPAC4F10.07c","SPAC6G9.11"],"gene_count":16,"ltp_gene_count":12,"approved_date":"2018-04-17"},{"uniquename":"EMBL:AU011790","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009477","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9730284","title":"The uracil permease of Schizosaccharomyces pombe: a representative of a family of 10 transmembrane helix transporter proteins of yeasts.","citation":"Yeast 1998 Aug;14(11):1051-9","abstract":"The uracil permease gene of Schizosaccharomyces pombe was cloned and sequenced. The deduced protein sequence shares strong similarities with five open reading frames from Saccharomyces cerevisiae, namely the uracil permease encoded by the FUR4 gene, the allantoin permease encoded by DAL4, a putative uridine permease (YBL042C) and two unknown ORFs YOR071c and YLR237w. A topological model retaining ten transmembrane helices, based on predictions and on experimental data established for the uracil permease of S. cerevisiae by Galan and coworkers (1996), is discussed for the four closest proteins of this family of transporters. The sequence of the uracil permease gene of S. pombe has been deposited in the EMBL data bank under Accession Number X98696.","authors":"de Montigny J, Straub ML, Wagner R, Bach ML, Chevallier MR","authors_abbrev":"de Montigny J et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-09-08","publication_year":"1998","canto_session_key":"5725e0afc9416f25","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-02-17 14:06:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-14 15:51:06","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1399.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-14"},{"uniquename":"PMID:19783542","title":"A Pom1 gradient is made to measure.","citation":"J Mol Cell Biol 2009 Dec;1(2):72-4","abstract":"In order for cell division to proceed, fission yeast must first attain critical cell size. The mechanism by which size is detected had not been identified until two recent studies showed that cells utilize an intracellular gradient of Pom1p kinase to measure cell length.","doi":"10.1093/jmcb/mjp020","authors":"Calvert ME","authors_abbrev":"Calvert ME","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-09-29","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22425159","title":"Transient structure associated with the spindle pole body directs meiotic microtubule reorganization in S. pombe.","citation":"Curr Biol 2012 Apr 10;22(7):562-74","abstract":"Vigorous chromosome movements driven by cytoskeletal assemblies are a widely conserved feature of sexual differentiation to facilitate meiotic recombination. In fission yeast, this process involves the dramatic conversion of arrays of cytoplasmic microtubules (MTs), generated from multiple MT organizing centers (MTOCs), into a single radial MT (rMT) array associated with the spindle pole body (SPB), the major MTOC during meiotic prophase. The rMT is then dissolved upon the onset of meiosis I when a bipolar spindle emerges to conduct chromosome segregation. Structural features and molecular mechanisms that govern these dynamic MT rearrangements are poorly understood.\nElectron tomography of the SPBs showed that the rMT emanates from a newly recognized amorphous structure, which we term the rMTOC. The rMTOC, which resides at the cytoplasmic side of the SPB, is highly enriched in γ-tubulin reminiscent of the pericentriolar material of higher eukaryotic centrosomes. Formation of the rMTOC depends on Hrs1/Mcp6, a meiosis-specific SPB component that is located at the rMTOC. At the onset of meiosis I, Hrs1/Mcp6 is subject to strict downregulation by both proteasome-dependent degradation and phosphorylation leading to complete inactivation of the rMTOC. This ensures rMT dissolution and bipolar spindle formation.\nOur study reveals the molecular basis for the transient generation of a novel MTOC, which triggers a program of MT rearrangement that is required for meiotic differentiation.","doi":"10.1016/j.cub.2012.02.042","authors":"Funaya C, Samarasinghe S, Pruggnaller S, Ohta M, Connolly Y, Müller J, Murakami H, Grallert A, Yamamoto M, Smith D, Antony C, Tanaka K","authors_abbrev":"Funaya C et al.","pubmed_publication_date":"10 Apr 2012","pubmed_entrez_date":"2012-03-20","publication_year":"2012","canto_session_key":"d7f3b64fc76f62d2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC947.12","SPBC20F10.06","SPAC3A11.05c","SPBC2G2.12","SPBC365.15"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:9675815","title":"Pombe: a gene-finding and exon-intron structure prediction system for fission yeast.","citation":"Yeast 1998 Jun 15;14(8):701-10","abstract":"A special program developed by the authors, called Pombe, identifies protein coding regions in the Schizosaccharomyces pombe genome. Linear discriminant analysis was applied to predict 5'-terminal, internal, 3'-terminal exons (coding-exon) and introns. The accuracy of the prediction was tested by cross verifications. The sensitivity, specificity and correlation coefficient for the internal exon prediction were 98.5%, 99.9% and 98.3% respectively at the nucleotide level. Open reading frames were studied and used to predict intron-less genes: 99.0% of such genes were identified with correct stopping sites. The gene structure was determined by dynamic programming and the prediction achieved 97.0% correlation coefficient at the nucleotide level. The program is available at http:(/)/clio.cshl.org/genefinder.","authors":"Chen T, Zhang MQ","authors_abbrev":"Chen T et al.","pubmed_publication_date":"15 Jun 1998","pubmed_entrez_date":"1998-07-24","publication_year":"1998","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15546125","title":"Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe.","citation":"Yeast 2004 Nov;21(15):1279-88","abstract":"Alpha-aminoadipate reductase (AAR), the signature enzyme for lysine biosynthesis in fungi, catalyses the conversion of alpha-aminoadipate to alpha-aminoadipate-semiadehyde in the presence of ATP and NADPH. In Saccharomyces cerevisiae and Candida albicans, the LYS2-encoded AAR is posttranslationally activated by CoA and the LYS5-encoded PPTase. The fission yeast Schizosaccharomyces pombe is evolutionarily highly diverged from S. cerevisiae and C. albicans. We report here several unusual activation characteristics of Sz. pombe Lys1p and Lys7p, isofunctional to Lys2p (AAR) and Lys5p (PPTase), respectively. Unlike the Lys2p from S. cerevisiae and C. albicans, the Sz. pombe Lys1p was active when expressed in E. coli and exhibited significant AAR activity without the addition of CoA or the Sz. pombe Lys7p intron free PPTase. Somewhat higher AAR activity was obtained with the addition of CoA and the Sz. pombe Lys7p PPTase. Substitution of G910A, S913T or S913A in the Sz. pombe Lys1p activation domain (IGGHSI) resulted in no AAR activity. Similarly, substitutions of several amino acid residues in the Sz. pombe Lys7p PPTase domain (G79A, R80K and P81A in Core 1; F93W, D94E, F95W and N96D in Core 1a; G124A, V125I and D126E in Core 2; K172R, E173D and K177R in Core 3) also resulted in no activation of Lys1p and no AAR activity. The Sz. pombe Lys1p amino acid sequence showed a high degree of similarity to other fungal Lys2p proteins; however, the Lys7p amino acid sequence showed much less similarity to other bacterial, fungal and animal PPTases representing several phylogenetic groups.","authors":"Guo S, Bhattacharjee JK","authors_abbrev":"Guo S et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-11-17","publication_year":"2004","canto_session_key":"d4b4d05fbf0e23a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-11-19 16:55:02","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-08 15:51:43","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.02c","SPAP7G5.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-10-08"},{"uniquename":"PMID:7885830","title":"Characterization of cDNA encoding mouse homolog of fission yeast dhp1+ gene: structural and functional conservation.","citation":"Nucleic Acids Res 1995 Feb 11;23(3):357-61","abstract":"The dhp1+ gene of Schizosaccharomyces pombe is a homolog of Saccharomyces cerevisiae HKE1/RAT1/TAP1 gene that is involved in RNA metabolism such as RNA trafficking and RNA synthesis. dhp1+ is also related to S. cerevisiae DST2 (SEP1) that encodes a DNA strand exchange protein required for sporulation and homologous recombination in S.cerevisiae. We isolated several clones of Dhm1, a mouse homolog of dhp1+, from mouse spermatocyte cDNA library and determined its nucleotide sequence. The Dhm1 gene consists of an open reading frame predicting a protein with 947 amino acids and molecular weight of 107,955. Northern blot analysis revealed that Dhm1 is transcribed at high level in testis, liver and kidney. The predicted product of Dhm1 (Dhm1p) has a significant homology with Dhp1p, Hke1p/Rat1p/Tap1p and Dst2p. In particular, Dhm1p, Dhp1p and Hke1p/Rat1p/Tap1p share strong similarity at the two regions of their N- and C-terminal parts. The Dhm1 gene on a multicopy plasmid rescued the temperature-sensitivity of dhp1ts and lethality of dhp1 null mutation, suggesting that Dhm1 is a mouse homolog of S.pombe dhp1+ and functions similarly in mouse as dhp1+.","authors":"Shobuike T, Sugano S, Yamashita T, Ikeda H","authors_abbrev":"Shobuike T et al.","pubmed_publication_date":"11 Feb 1995","pubmed_entrez_date":"1995-02-11","publication_year":"1995","canto_session_key":"725066fcbcdc288b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 14:45:05","canto_session_submitted_date":"2012-03-03 14:44:52","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.12c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:10747045","title":"The fission yeast git5 gene encodes a Gbeta subunit required for glucose-triggered adenylate cyclase activation.","citation":"Genetics 2000 Apr;154(4):1463-71","abstract":"Fission yeast adenylate cyclase is activated by the gpa2 Galpha subunit of a heterotrimeric guanine-nucleotide binding protein (G protein). We show that the git5 gene, also required for this activation, encodes a Gbeta subunit. In contrast to another study, we show that git5 is not a negative regulator of the gpa1 Galpha involved in the pheromone response pathway. While 43% identical to mammalian Gbeta's, the git5 protein lacks the amino-terminal coiled-coil found in other Gbeta subunits, yet the gene possesses some of the coding capacity for this structure 5' to its ORF. Although both gpa2 (Galpha) and git5 (Gbeta) are required for adenylate cyclase activation, only gpa2 is needed to maintain basal cAMP levels. Strains bearing a git5 disruption are derepressed for fbp1 transcription and sexual development even while growing in a glucose-rich environment, although fbp1 derepression is half that observed in gpa2 deletion strains. Multicopy gpa2 partially suppresses the loss of git5, while the converse is not true. These data suggest that Gbeta is required for activation of adenylate cyclase either by promoting the activation of Galpha or by independently activating adenylate cyclase subsequent to Galpha stimulation as seen in type II mammalian adenylate cyclase activation.","authors":"Landry S, Pettit MT, Apolinario E, Hoffman CS","authors_abbrev":"Landry S et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-04-04","publication_year":"2000","canto_session_key":"90c405d69ccaf60c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-19 08:35:13","canto_approved_date":"2022-06-06 06:36:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-19 08:35:05","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1753.02c","SPBC106.10","SPAC23H3.13c","SPBC32H8.07","SPBC21C3.20c","SPBC24C6.06","SPBC36.12c"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2017-09-19"},{"uniquename":"PMID:9524252","title":"Isolation of a novel heat shock protein 70-like gene, pss1+ of Schizosaccharomyces pombe homologous to hsp110/SSE subfamily.","citation":"Gene 1998 Mar 27;210(1):143-50","abstract":"A novel heat shock protein 70 (HSP70) gene, pss1+, of fission yeast, Schizosaccharomyces pombe (S. pombe), has been isolated as a multicopy suppressor of a synthetic lethal mutant of ras1+, which shows severe retardation of growth and aggregation phenotype when the ras1 gene function is absent. The pss1+ gene functionally complements the growth defect of the mutant. Sequence analysis revealed that pss1+ encodes an open reading frame (ORF) of 730amino acids that is homologous to the HSP70 family proteins. The Pss1 has high homology to the Saccharomyces cerevisiae (S. cerevisiae) heat shock protein Sse1p/Msi3p (43% identity) that belongs to the HSP110/SSE subfamily of HSP70. The consensus nucleotide sequence of the heat shock element (HSE) was found in the upstream region of pss1+ gene. The transcript level of pss1+ was moderately abundant during steady-state growth at 25 degrees C and increased a few-fold upon shifting to 42 degrees C. Furthermore, transcription of pss1+ increased in nitrogen-starved conditions. Disruption of the pss1+ gene confers a temperature-sensitive growth phenotype and unexpectedly causes the increase in thermotolerance in S. pombe.","authors":"Chung KS, Hoe KL, Kim KW, Yoo HS","authors_abbrev":"Chung KS et al.","pubmed_publication_date":"27 Mar 1998","pubmed_entrez_date":"1998-05-23","publication_year":"1998","canto_session_key":"abd6962adf48a2b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-09-25 10:50:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-25 10:50:02","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPAC110.03","SPAC110.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-09-25"},{"uniquename":"PMID:1934121","title":"Pheromone production and response in sterile mutants of fission yeast.","citation":"Curr Genet 1991 Jul;20(1-2):79-85","abstract":"Genetically heterothallic strains of various sterile mutants were assayed for residual production of the corresponding mating pheromone as well as responsiveness towards the opposite pheromone. No sexual activities were detected in ste11 strains (previously referred to as aff1 or steX, which we show are allelic), whilst the production of M factor was unaffected by ste1 to ste10 mutations. P factor production was still possible in class I ste mutants (ste5, ste6 and ste10), which also allow meiosis in diploid strains. With the exception of the leaky ste10-F23 mutant, no changes in cell morphology were induced by exposure to the opposite pheromone in the ste mutant strains.","authors":"Leupold U, Sipiczki M, Egel R","authors_abbrev":"Leupold U et al.","pubmed_publication_date":"Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_session_key":"033f786bc92907ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2013-02-01 17:00:14","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-01 16:57:40","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1D7.05","SPAC1D4.13","SPAC144.13c","SPBC32C12.02","SPCC1442.01","SPAC1565.04c","SPAC17H9.09c","SPAC23E2.03c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2013-02-01"},{"uniquename":"PMID:1737802","title":"A multicomponent protein of a fission yeast that promotes joint molecule formation from homologous DNAs.","citation":"J Biol Chem 1992 Feb 15;267(5):3514-22","abstract":"We developed a quantitative assay (\"homologous pairing gel assay\") adequate for the purification of the activity promoting the formation of joint molecules, an intermediate of homologous recombination (\"homologous pairing\"). With this assay, one can measure the extent of homologous pairing between a single-stranded DNA and a strand of 3H-labeled double-stranded DNA by crude enzyme preparations. Since the total activity did not significantly change during the sporulation process, we tried to purify the activity from a whole cell extract of mitotic cells of a fission yeast, (Schizosaccharomyces pombe). Through quantitative assaying of a single fraction or of mixed fractions, we obtained three fractions, all of which were required for the maximum level of the ATP-independent homologous pairing: Fractions 65, 100, and 30. In Fractions 100 and 30, polypeptides of approximately 100 and approximately 30 kDa (the 100- and 30-kDa polypeptides), respectively, were the sole detectable components. Fraction 65 contained a polypeptide of approximately 65 kDa (the 65-kDa polypeptide) as the major component and also small amounts of the 30- and 100-kDa polypeptides. Fraction 65 by itself promoted homologous pairing, but the reaction was saturated at a level of approximately 20% of the maximum level achieved with the recA protein. Even when added in excess, Fraction 30 or 100 alone did not promote detectable homologous pairing. A mixture of Fractions 65 and 100 at a rather strict optimum ratio only promoted homologous pairing, the level being 50-70% that with the recA protein, suggesting a stoichiometric complex of these polypeptides as the active form. Fraction 30 alone did not enhance the reaction with Fraction 65, but stimulated homologous pairing promoted by the optimum mixture of Fractions 65 and 100 to the maximum level achieved with the recA protein. Therefore, the homologous pairing-promoting protein from the fission yeast is likely to be a multicomponent protein.","authors":"Arai N, Kawasaki K, Shibata T","authors_abbrev":"Arai N et al.","pubmed_publication_date":"15 Feb 1992","pubmed_entrez_date":"1992-02-15","publication_year":"1992","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084829","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.17"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15249580","title":"A novel phosphatidylinositol(3,4,5)P3 pathway in fission yeast.","citation":"J Cell Biol 2004 Jul 19;166(2):205-11","abstract":"The mammalian tumor suppressor, phosphatase and tensin homologue deleted on chromosome 10 (PTEN), inhibits cell growth and survival by dephosphorylating phosphatidylinositol-(3,4,5)-trisphosphate (PI[3,4,5]P3). We have found a homologue of PTEN in the fission yeast, Schizosaccharomyces pombe (ptn1). This was an unexpected finding because yeast (S. pombe and Saccharomyces cerevisiae) lack the class I phosphoinositide 3-kinases that generate PI(3,4,5)P3 in higher eukaryotes. Indeed, PI(3,4,5)P3 has not been detected in yeast. Surprisingly, upon deletion of ptn1 in S. pombe, PI(3,4,5)P3 became detectable at levels comparable to those in mammalian cells, indicating that a pathway exists for synthesis of this lipid and that the S. pombe ptn1, like mammalian PTEN, suppresses PI(3,4,5)P3 levels. By examining various mutants, we show that synthesis of PI(3,4,5)P3 in S. pombe requires the class III phosphoinositide 3-kinase, vps34p, and the phosphatidylinositol-4-phosphate 5-kinase, its3p, but does not require the phosphatidylinositol-3-phosphate 5-kinase, fab1p. These studies suggest that a pathway for PI(3,4,5)P3 synthesis downstream of a class III phosphoinositide 3-kinase evolved before the appearance of class I phosphoinositide 3-kinases.","authors":"Mitra P, Zhang Y, Rameh LE, Ivshina MP, McCollum D, Nunnari JJ, Hendricks GM, Kerr ML, Field SJ, Cantley LC, Ross AH","authors_abbrev":"Mitra P et al.","pubmed_publication_date":"19 Jul 2004","pubmed_entrez_date":"2004-07-14","publication_year":"2004","canto_session_key":"0bf69081e6ca5d78","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-04-17 11:26:05","canto_approved_date":"2024-09-28 13:29:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-05 15:26:29","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC576.15c","SPBC609.02","SPAC19G12.14","SPAC458.05","SPAC11E3.11c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-04-17"},{"uniquename":"PMID:33232355","title":"Benzoic acid inhibits Coenzyme Q biosynthesis in Schizosaccharomyces pombe.","citation":"PLoS One 2020;15(11):e0242616","abstract":"Coenzyme Q (CoQ, ubiquinone) is an essential component of the electron transport system in aerobic organisms. Human type CoQ10, which has 10 units of isoprene in its quinone structure, is especially valuable as a food supplement. Therefore, studying the biosynthesis of CoQ10 is important not only for increasing metabolic knowledge, but also for improving biotechnological production. Herein, we show that Schizosaccharomyces pombe utilizes p-aminobenzoate (PABA) in addition to p-hydroxybenzoate (PHB) as a precursor for CoQ10 synthesis. We explored compounds that affect the synthesis of CoQ10 and found benzoic acid (Bz) at >5 μg/mL inhibited CoQ biosynthesis without accumulation of apparent CoQ intermediates. This inhibition was counteracted by incubation with a 10-fold lower amount of PABA or PHB. Overexpression of PHB-polyprenyl transferase encoded by ppt1 (coq2) also overcame the inhibition of CoQ biosynthesis by Bz. Inhibition by Bz was efficient in S. pombe and Schizosaccharomyces japonicus, but less so in Saccharomyces cerevisiae, Aureobasidium pullulans, and Escherichia coli. Bz also inhibited a S. pombe ppt1 (coq2) deletion strain expressing human COQ2, and this strain also utilized PABA as a precursor of CoQ10. Thus, Bz is likely to inhibit prenylation reactions involving PHB or PABA catalyzed by Coq2.","doi":"10.1371/journal.pone.0242616","authors":"Nishida I, Yanai R, Matsuo Y, Kaino T, Kawamukai M","authors_abbrev":"Nishida I et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-11-24","publication_year":"2020","canto_session_key":"e318eaedac1cc321","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_first_approved_date":"2021-01-13 21:56:32","canto_approved_date":"2021-01-13 21:56:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-10 04:08:20","canto_added_date":"2020-11-26 01:15:04","annotation_curators":[{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.18","SPAC1687.12c","SPAC56F8.04c","SPAC19G12.12"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2021-01-13"},{"uniquename":"EMBL:SPD254","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23754748","title":"Splicing functions and global dependency on fission yeast slu7 reveal diversity in spliceosome assembly.","citation":"Mol Cell Biol 2013 Aug;33(16):3125-36","abstract":"The multiple short introns in Schizosaccharomyces pombe genes with degenerate cis sequences and atypically positioned polypyrimidine tracts make an interesting model to investigate canonical and alternative roles for conserved splicing factors. Here we report functions and interactions of the S. pombe slu7(+) (spslu7(+)) gene product, known from Saccharomyces cerevisiae and human in vitro reactions to assemble into spliceosomes after the first catalytic reaction and to dictate 3' splice site choice during the second reaction. By using a missense mutant of this essential S. pombe factor, we detected a range of global splicing derangements that were validated in assays for the splicing status of diverse candidate introns. We ascribe widespread, intron-specific SpSlu7 functions and have deduced several features, including the branch nucleotide-to-3' splice site distance, intron length, and the impact of its A/U content at the 5' end on the intron's dependence on SpSlu7. The data imply dynamic substrate-splicing factor relationships in multiintron transcripts. Interestingly, the unexpected early splicing arrest in spslu7-2 revealed a role before catalysis. We detected a salt-stable association with U5 snRNP and observed genetic interactions with spprp1(+), a homolog of human U5-102k factor. These observations together point to an altered recruitment and dependence on SpSlu7, suggesting its role in facilitating transitions that promote catalysis, and highlight the diversity in spliceosome assembly.","doi":"10.1128/MCB.00007-13","authors":"Banerjee S, Khandelia P, Melangath G, Bashir S, Nagampalli V, Vijayraghavan U","authors_abbrev":"Banerjee S et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-06-12","publication_year":"2013","canto_session_key":"de8b67d975d050e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Geetha M","canto_first_approved_date":"2016-12-01 14:40:54","canto_approved_date":"2021-11-05 19:33:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-26 04:43:31","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Geetha M","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G7.11","SPSNRNA.06","SPBC146.07","SPAC17A5.02c","SPAC19B12.06c","SPAC15E1.08","SPAC8E11.02c","SPAC14C4.06c","SPBC1215.02c","SPBC428.16c","SPSNRNA.02","SPBC365.05c","SPSNRNA.05","SPBC6B1.07","SPCC16A11.05c"],"gene_count":15,"ltp_gene_count":7,"approved_date":"2016-12-01"},{"uniquename":"PMID:24831008","title":"The double zinc finger domain and adjacent accessory domain from the transcription factor loss of zinc sensing 1 (loz1) are necessary for DNA binding and zinc sensing.","citation":"J Biol Chem 2014 Jun 27;289(26):18087-96","abstract":"The Loz1 transcription factor from Schizosaccharomyces pombe plays an essential role in zinc homeostasis by repressing target gene expression in zinc-replete cells. To determine how Loz1 function is regulated by zinc, we employed a genetic screen to isolate mutants with impaired zinc-dependent gene expression and analyzed Loz1 protein truncations to map a minimal zinc-responsive domain. In the screen, we isolated 36 new loz1 alleles. 27 of these alleles contained mutations resulting in the truncation of the Loz1 protein. The remaining nine alleles contained point mutations leading to an amino acid substitution within a C-terminal double zinc finger domain. Further analysis of two of these substitutions revealed that they disrupted Loz1 DNA activity in vitro. By analyzing Loz1 protein truncations, we found that the last 96 amino acids of Loz1 was the smallest region that was able to confer partial zinc-dependent repression in vivo. This 96-amino acid region contains the double zinc finger domain and an accessory domain that enhances DNA binding. These results were further supported by the findings that MtfA, a transcription factor from Aspergillus nidulans that contains a related double zinc finger, is unable to complement loz1Δ, whereas a chimera of MtfA containing the Loz1 accessory domain is able to complement loz1Δ. Together, our studies indicate that the double zinc finger domain and adjacent accessory domain preceding zinc finger 1 are necessary for DNA binding and zinc-dependent repression.","doi":"10.1074/jbc.M114.551333","authors":"Ehrensberger KM, Corkins ME, Choi S, Bird AJ","authors_abbrev":"Ehrensberger KM et al.","pubmed_publication_date":"27 Jun 2014","pubmed_entrez_date":"2014-05-17","publication_year":"2014","canto_session_key":"bf037075feb20f28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Amanda Bird","canto_first_approved_date":"2020-02-18 13:55:25","canto_approved_date":"2023-09-12 09:36:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-12 20:57:51","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Amanda Bird","community_curator":true,"annotation_count":21,"orcid":"0000-0002-1846-7050","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.19c","SPBC16D10.06","SPAC5H10.06c","SPCC13B11.01"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2020-02-18"},{"uniquename":"PMID:28345120","title":"Fission Yeast srm1 is Involved in Stress Response and Cell Cycle.","citation":"Curr Microbiol 2017 Jun;74(6):725-731","abstract":"Polyamines are well-conserved, multifunctional polycations that contribute to a number of processes in the cells such as cell cycle, apoptosis, stress response, and gene expression. Therefore, polyamine levels should be kept under strict regulation by specific polyamine transporters and polyamine synthases. In this study, the aim is to experimentally characterize a predicted spermidine synthase gene srm1, which was identified upon sequence similarity, in fission yeast Schizosaccharomyces pombe. In an attempt to understand the role of this gene in cell cycle and stress response, deletion mutant of srm1 was generated and analyzed in terms of cell cycle regulation and environmental stress response. The results showed that srm1Δ cells had elongated cell size and were sensitive to osmotic stress, while they showed no sensitivity to DNA-damaging agents. To the best of our knowledge, this is the first experimental characterization of srm1 gene and its role in cell cycle progression and stress response.","doi":"10.1007/s00284-017-1241-y","authors":"Gevrekci AÖ","authors_abbrev":"Gevrekci AÖ","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2017-03-28","publication_year":"2017","canto_session_key":"1b864783d93dec1a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-29 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2364927","title":"A review of the CLIP system for the quantitative analysis of two-dimensional electrophoresis gels.","citation":"Electrophoresis 1990 May;11(5):415-9","abstract":"This paper reviews the CLIP image processing system for the complete analysis of two-dimensional electrophoresis images. The analysis problem for two-dimensional gel images can be broken down into three issues: segmentation of individual gel images, alignment and comparison of pairs of gel images, and information storage and retrieval. This paper describes these problems and reviews how the CLIP system handles each of them. Segmentation is the location and isolation of each protein spot on an individual gel image and also the extraction of individual spot data such as position, area and volume. There are three basic stages: background field correction, noise filtering, spot detection and information extraction. Alignment and comparison of gel images involves matching protein spots between two gels. This can be quite difficult because there is not a simple relationship which can transform one gel image onto another. The database issues concern storing all the information which has been obtained from the above operations such that retrieval of this information can be readily performed. The advantage of the CLIP system over others is speed of processing. CLIP series computers use one processor for every pixel of the camera image such that image processing algorithms run in parallel. The main disadvantage is in the cost of these machines. With the declining trend in the cost of parallel processors, these machines will become more and more viable alternatives. This papers reviews the algorithms for the analysis of two-dimensional gels. It is shown that CLIP is flexible enough to perform more than one type of algorithm for a particular operation.","authors":"Potter DJ","authors_abbrev":"Potter DJ","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-12-19 08:18:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7586030","title":"Molecular cloning of the meiosis-induced rec10 gene of Schizosaccharomyces pombe.","citation":"Curr Genet 1995 Apr;27(5):440-6","abstract":"The meiotic recombination gene rec10, which encodes a region-specific activator of recombination in Schizosaccharomyces pombe, has been cloned by genetic complementation and its nucleotide sequence determined. The rec10 gene was identified in a 5.6-kb cloned fragment by partial-deletion and insertion experiments. The nucleotide sequence of 3.5 kb of this clone revealed an open reading frame (ORF) encoding a 791 amino-acid polypeptide for the rec10 gene product. During meiosis, thermally induced in a temperature-sensitive pat1-114 mutant, the transcript of rec10 was induced to a maximal level at 2-3 h but was present at much lower levels before and after this time. The transient induction of the rec10 transcript and the rec10 mutant phenotype suggest that the rec10 gene product is involved primarily in the early steps of meiotic recombination localized to chromosome III in S. pombe.","authors":"Lin Y, Smith GR","authors_abbrev":"Lin Y et al.","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_session_key":"e685ee55dd3671fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-08-02 10:48:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-21 14:53:30","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-21"},{"uniquename":"PMID:38097609","title":"Ubiquitination-mediated Golgi-to-endosome sorting determines the toxin-antidote duality of fission yeast wtf meiotic drivers.","citation":"Nat Commun 2023 Dec 14;14(1):8334","abstract":"Killer meiotic drivers (KMDs) skew allele transmission in their favor by killing meiotic progeny not inheriting the driver allele. Despite their widespread presence in eukaryotes, the molecular mechanisms behind their selfish behavior are poorly understood. In several fission yeast species, single-gene KMDs belonging to the wtf gene family exert selfish killing by expressing a toxin and an antidote through alternative transcription initiation. Here we investigate how the toxin and antidote products of a wtf-family KMD gene can act antagonistically. Both the toxin and the antidote are multi-transmembrane proteins, differing only in their N-terminal cytosolic tails. We find that the antidote employs PY motifs (Leu/Pro-Pro-X-Tyr) in its N-terminal cytosolic tail to bind Rsp5/NEDD4 family ubiquitin ligases, which ubiquitinate the antidote. Mutating PY motifs or attaching a deubiquitinating enzyme transforms the antidote into a toxic protein. Ubiquitination promotes the transport of the antidote from the trans-Golgi network to the endosome, thereby preventing it from causing toxicity. A physical interaction between the antidote and the toxin enables the ubiquitinated antidote to translocate the toxin to the endosome and neutralize its toxicity. We propose that post-translational modification-mediated protein localization and/or activity changes may be a common mechanism governing the antagonistic duality of single-gene KMDs.","doi":"10.1038/s41467-023-44151-9","authors":"Zheng JX, Du TY, Shao GC, Ma ZH, Jiang ZD, Hu W, Suo F, He W, Dong MQ, Du LL","authors_abbrev":"Zheng JX et al.","pubmed_publication_date":"14 Dec 2023","pubmed_entrez_date":"2023-12-14","publication_year":"2023","canto_session_key":"423c5afa8f3e4209","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jin-Xin Zheng","canto_first_approved_date":"2025-01-07 16:26:01","canto_approved_date":"2025-01-07 16:26:01","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-12-27 04:40:54","canto_added_date":"2023-12-16 00:25:04","annotation_curators":[{"name":"Jin-Xin Zheng","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":6,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.15","SPCC663.17","SPCC285.07c","SPCC1281.08","SPCC736.05","SPCC1919.06c","SPCC1620.02","SPCC794.02","SPCC1906.04","SPCC162.04c","SPCC1183.10","SPCC970.11c","SPCC1450.08c","SPCC1906.03","SPCC548.03c","SPCC663.02"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2025-01-07"},{"uniquename":"PMID:25428765","title":"Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints.","citation":"J Biomol NMR 2015 Jan;61(1):55-64","abstract":"NMR structure determination of soluble proteins depends in large part on distance restraints derived from NOE. In this study, we examined the impact of paramagnetic relaxation enhancement (PRE)-derived distance restraints on protein structure determination. A high-resolution structure of the loop-rich soluble protein Sin1 could not be determined by conventional NOE-based procedures due to an insufficient number of NOE restraints. By using the 867 PRE-derived distance restraints obtained from the NOE-based structure determination procedure, a high-resolution structure of Sin1 could be successfully determined. The convergence and accuracy of the determined structure were improved by increasing the number of PRE-derived distance restraints. This study demonstrates that PRE-derived distance restraints are useful in the determination of a high-resolution structure of a soluble protein when the number of NOE constraints is insufficient.","doi":"10.1007/s10858-014-9882-7","authors":"Furuita K, Kataoka S, Sugiki T, Hattori Y, Kobayashi N, Ikegami T, Shiozaki K, Fujiwara T, Kojima C","authors_abbrev":"Furuita K et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-11-28","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-09-18 00:26:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPYUG7.02c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"2ruj","gene_chains":[{"gene_uniquename":"SPAPYUG7.02c","chain":"A","position":"247-400"}],"title":"Solution structure of MTSL spin-labeled Schizosaccharomyces pombe Sin1 CRIM domain","entry_authors":"Furuita K,Kataoka S,Sugiki T,Kobayashi N,Ikegami T,Shiozaki K,Fujiwara T,Kojima C","entry_authors_abbrev":"Furuita K et al.","reference_uniquename":"PMID:25428765","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:20085745","title":"Ubiquinol-binding site in the alternative oxidase: mutagenesis reveals features important for substrate binding and inhibition.","citation":"Biochim Biophys Acta 2010 Dec;1797(12):1933-9","abstract":"The alternative oxidase (AOX) is a non-protonmotive ubiquinol oxidase that is found in all plants, some fungi, green algae, bacteria and pathogenic protozoa. The lack of AOX in the mammalian host renders this protein an important potential therapeutic target in the treatment of pathogenic protozoan infections. Bioinformatic searches revealed that, within a putative ubiquinol-binding crevice in AOX, Gln242, Asn247, Tyr253, Ser256, His261 and Arg262 were highly conserved. To confirm that these amino-acid residues are important for ubiquinol-binding and hence activity substitution mutations were generated and characterised. Assessment of AOX activity in isolated Schizosaccharomyces pombe mitochondria revealed that mutation of either Gln242, Ser256, His261 and Arg262 resulted in >90% inhibition of antimycin A-insensitive respiration suggesting that hydroxyl, guanidino, imidazole groups, polar and charged residues in addition to the size of the amino-acid chain are important for ubiquinone-binding. Substitution of Asn247 with glutamine or Tyr253 with phenylalanine had little effect upon the respiratory rate indicating that these residues are not critical for AOX activity. However replacement of Tyr253 by alanine resulted in a 72% loss of activity suggesting that the benzoquinone group and not hydroxyl group is important for quinol binding. These results provide important new insights into the ubiquinol-binding site of the alternative oxidase, the identity of which maybe important for future rational drug design.","doi":"10.1016/j.bbabio.2010.01.013","authors":"Albury MS, Elliott C, Moore AL","authors_abbrev":"Albury MS et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-01-21","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11081738","title":"Microtubule-dependent nuclear positioning and nuclear-dependent septum positioning in the fission yeast Schizosaccharomyces [correction of Saccharomyces] pombe.","citation":"Biol Bull 2000 Oct;199(2):205-6","abstract":"","authors":"Tran PT, Doye V, Chang F, Inoué S","authors_abbrev":"Tran PT et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-11-18","publication_year":"2000","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28388440","title":"Genome and Epigenome Maintenance by Keeping Histone Turnover in Check.","citation":"Mol Cell 2017 Apr 06;66(1):3-4","abstract":"In this issue of Molecular Cell, Taneja et al. (2017) uncover a dual role for the conserved chromatin remodeler Fft3 in the maintenance of silent heterochromatin and the suppression of replication barriers at euchromatic loci through controlled histone turnover.","doi":"10.1016/j.molcel.2017.03.015","authors":"Fortuny A, Polo SE","authors_abbrev":"Fortuny A et al.","pubmed_publication_date":"06 Apr 2017","pubmed_entrez_date":"2017-04-08","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-04-09 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000096","title":"Automated transfer of experimentally-verified manual GO annotation data to close orthologs.","abstract":"Mouse Genome Database (MGD), The HUGO Gene Nomenclature Committee (HGNC), and Rat Genome Database (RGD) have extensive procedures in place, overseen by expert curation, to establish orthology relationships between their genes. The Experimentally based annotations annotated by each group (IDA, IMP IPI, IGI, and EXP) are used to provide annotations  to the respective mouse and rat orthologs, and given the ISO evidence code and an entry in the inferred_from field to indicate the orthologous entity. ","authors":"Mouse Genome Informatics scientific curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084826","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:3046932","title":"Sequence analysis of ARS elements in fission yeast.","citation":"EMBO J 1988 Jul;7(7):2203-9","abstract":"Chromosomal DNA of Schizosaccharomyces pombe contains sequences with properties analogous to ARS elements of Saccharomyces cerevisiae. Following Sau3A fragmentation of the S. pombe genome we have recovered a number of such fragments in an M13-based shuttle vector, suitable for subsequent sequence analysis. The complete nucleotide sequence has been obtained for eight ARS+ inserts derived from the Sau3A cloning and for the ARS present in pFL20 isolated previously by Losson and Lacroute (Cell, 32, 371-377, 1983). The Sau3A clones are single fragments between 0.8 and 1.8 kb. No ARS+ clones smaller than this were recovered even though the average size Sau3A fragment in S. pombe is approximately 200-300 bp. The sequence analysis revealed that all clones are AT-rich (69-75% A + T residues), and all contain a particularly AT-rich 11 bp core element represented by the consensus sequence 5' (A/T)PuTT-TATTTA(A/T) 3'. Deletion mapping indicates that the consensus in all cases is in the vicinity of a functional ARS domain. However precise excision of the consensus by in vitro mutagenesis has little effect on ARS activity as judged by the transformation assay. We argue that the association of the consensus with the ARS domain occurs too reproducibly to be explained by chance alone. We suggest that although it may not be essential for the extrachromosomal maintenance of plasmids in S. pombe, the consensus does have a function in situ in the chromosome and thus is always present as a cryptic sequence in the isolated ARS element.","authors":"Maundrell K, Hutchison A, Shall S","authors_abbrev":"Maundrell K et al.","pubmed_publication_date":"Jul 1988","pubmed_entrez_date":"1988-07-01","publication_year":"1988","canto_session_key":"08601cff9df4e95e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 14:40:06","canto_approved_date":"2019-01-07 14:40:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 14:39:59","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:19624755","title":"Deletion mutants of AP-1 adaptin subunits display distinct phenotypes in fission yeast.","citation":"Genes Cells 2009 Aug;14(8):1015-28","abstract":"Adaptins are subunits of the heterotetrameric (beta/mu/gamma/sigma) adaptor protein (AP) complexes that are involved in clathrin-mediated membrane trafficking. Here, we show that in Schizosaccharomyces pombe the deletion strains of each individual subunit of the AP-1 complex [Apl2 (beta), Apl4 (gamma), Apm1 (mu) and Aps1 (sigma)] caused distinct phenotypes on growth sensitivity to temperature or drugs. We also show that the Deltaapm1 and Deltaapl2 mutants displayed similar but more severe phenotypes than those of Deltaaps1 or Deltaapl4 mutants. Furthermore, the Deltaapl2Deltaaps1 and Deltaapl2Deltaapl4 double mutants displayed synthetic growth defects, whereas the Deltaaps1Deltaapl4 and Deltaapl2Deltaapm1 double mutants did not. In pull-down assay, Apm1 binds Apl2 even in the absence of Aps1 and Apl4, and Apl4 binds Aps1 even in the absence of Apm1 and Apl2. Consistently, the deletion of any subunit generally caused the disassociation of the heterotetrameric complex from endosomes, although some subunits weakly localized to endosomes. In addition, the deletion of individual subunits caused similar endosomal accumulation of v-SNARE synaptobrevin Syb1. Altogether, results suggest that the four subunits are all essential for the heterotetrameric complex formation and for the AP-1 function in exit transport from endosomes.","doi":"10.1111/j.1365-2443.2009.01327.x","authors":"Ma Y, Takeuchi M, Sugiura R, Sio SO, Kuno T","authors_abbrev":"Ma Y et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-07-24","publication_year":"2009","canto_session_key":"c6d09a7812ec9301","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-13 15:48:16","canto_approved_date":"2021-01-13 15:48:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-04 13:46:22","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":65,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.11","SPAP27G11.06c","SPBC947.02","SPAC6G9.11","SPCP1E11.06","SPAC144.18","SPBP16F5.07","SPAC22E12.09c","SPAC2G11.03c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2021-01-13"},{"uniquename":"PMID:19605557","title":"Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals.","citation":"Mol Biol Cell 2009 Sep;20(17):3974-84","abstract":"Glucosidase II (GII) plays a key role in glycoprotein biogenesis in the endoplasmic reticulum (ER). It is responsible for the sequential removal of the two innermost glucose residues from the glycan (Glc(3)Man(9)GlcNAc(2)) transferred to Asn residues in proteins. GII participates in the calnexin/calreticulin cycle; it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. GII is a heterodimer whose alpha subunit (GIIalpha) bears the glycosyl hydrolase active site, whereas its beta subunit (GIIbeta) role is controversial and has been reported to be involved in GIIalpha ER retention and folding. Here, we report that in the absence of GIIbeta, the catalytic subunit GIIalpha of the fission yeast Schizosaccharomyces pombe (an organism displaying a glycoprotein folding quality control mechanism similar to that occurring in mammalian cells) folds to an active conformation able to hydrolyze p-nitrophenyl alpha-d-glucopyranoside. However, the heterodimer is required to efficiently deglucosylate the physiological substrates Glc(2)Man(9)GlcNAc(2) (G2M9) and Glc(1)Man(9)GlcNAc(2) (G1M9). The interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta and mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement. We present evidence that also in mammalian cells GIIbeta modulates G2M9 and G1M9 trimming.","authors":"Stigliano ID, Caramelo JJ, Labriola CA, Parodi AJ, D'Alessio C","authors_abbrev":"Stigliano ID et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-07-17","publication_year":"2009","canto_session_key":"6b8ae0c3fd41751d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Cecilia D'Alessio","canto_first_approved_date":"2021-06-10 07:10:45","canto_approved_date":"2025-09-04 09:30:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-26 15:46:24","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Cecilia D'Alessio","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1002.03c","SPCC825.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-06-10"},{"uniquename":"PMID:16911511","title":"Physiological characterization and fed-batch production of an extracellular maltase of Schizosaccharomyces pombe CBS 356.","citation":"FEMS Yeast Res 2006 Sep;6(6):888-901","abstract":"The fission yeast Schizosaccharomyces pombe CBS 356 exhibits extracellular maltase activity. This activity may be of commercial interest as it exhibited a low pH optimum (3.5) and a high affinity for maltose (Km of 7.0+/-1.8 mM). N-terminal sequencing of the protein indicates that it is the product of the AGL1 gene. Regulation of this gene occurs via a derepression/repression mechanism. In sugar- or nitrogen-limited chemostat cultures, the specific rate of enzyme production (q(p)) was independent of the nature of the carbon source (i.e. glucose or maltose), but synthesis was partially repressed by high sugar concentrations. Furthermore, q(p) increased linearly with specific growth rate (mu) between 0.04 and 0.10 h(-1). The enzyme is easily mass-produced in aerobic glucose-limited fed-batch cultures, in which the specific growth rate is controlled to prevent alcoholic fermentation. In fed-batch cultures in which biomass concentrations of 83 g L(-1) were attained, the enzyme concentration reached 58,000 Units per liter culture supernatant. Extracellular maltase may be used as a dough additive in order to prevent mechanisms such as maltose-induced glucose efflux and maltose-hypersensitivity that occur in maltose-consuming Saccharomyces cerevisiae.","authors":"Jansen ML, Krook DJ, De Graaf K, van Dijken JP, Pronk JT, de Winde JH","authors_abbrev":"Jansen ML et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-08-17","publication_year":"2006","canto_session_key":"857068a897ef5024","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-10 21:38:44","canto_approved_date":"2024-06-13 19:31:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-10 11:01:11","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB24D3.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-10"},{"uniquename":"PMID:12537580","title":"RNAi hushes heterochromatin.","citation":"Genome Biol 2002;3(12):REVIEWS1035","abstract":"Repeated DNA elements and region-specific protein modifications combine within chromosomes to form a transcriptionally silent chromatin structure called heterochromatin. Recent work in the fission yeast Schizosaccharomyces pombe reveals that RNA is also an integral component of silent heterochromatin, providing a new perspective on how heterochromatin is organized and maintained in eukaryotic cells.","authors":"Bailis JM, Forsburg SL","authors_abbrev":"Bailis JM et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2003-01-23","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32697953","title":"Rapid and convenient biotransformation procedure for human drug metabolizing enzymes using permeabilized fission yeast cells.","citation":"Anal Biochem 2020 Oct 15;607:113704","abstract":"The development of convenient assays for the in vitro study of drug metabolizing enzymes (DMEs) such as cytochromes P450 (CYPs) and UDP-glucuronosyltransferases (UGTs) greatly facilitates metabolism studies of candidate drug compounds and other xenobiotics. We have developed and optimized an experimental approach that combines the advantages of recombinant expression in yeast with a microsomal-like biotransformation and thus allows for rapid and convenient enzymatic assays. Recombinant strains of the fission yeast Schizosaccharomyces pombe have previously been demonstrated to functionally express human CYPs and UGTs. Permeabilization of such cells with Triton X-100 results in the formation of enzyme bags, which can be used as biocatalysts. This protocol describes the preparation of such enzyme bags (3 h) and their application in enzyme activity assays (4 h) utilizing either pro-luminescent substrates and luminescence measurements or non-luminescent substrates and liquid chromatography coupled to mass spectrometry (LC-MS). Both applications provide practical tools for investigating CYP and UGT reactions in vitro without the need for additional sophisticated instrumentation or expertise.","doi":"10.1016/j.ab.2020.113704","authors":"Sharma S, Durairaj P, Bureik M","authors_abbrev":"Sharma S et al.","pubmed_publication_date":"15 Oct 2020","pubmed_entrez_date":"2020-07-23","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-07-24 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12738880","title":"TRAP230/ARC240 and TRAP240/ARC250 Mediator subunits are functionally conserved through evolution.","citation":"Proc Natl Acad Sci U S A 2003 May 27;100(11):6422-7","abstract":"In Saccharomyces cerevisiae Mediator, a subgroup of proteins (Srb8, Srb9, Srb10, and Srb11) form a module, which is involved in negative regulation of transcription. Homologues of Srb10 and Srb11 are found in some mammalian Mediator preparations, whereas no clear homologues have been reported for Srb8 and Srb9. Here, we identify a TRAP240/ARC250 homologue in Schizosaccharomyces pombe and demonstrate that this protein, spTrap240, is stably associated with a larger form of Mediator, which also contains conserved homologues of Srb8, Srb10, and Srb11. We find that spTrap240 and Sch. pombe Srb8 (spSrb8) regulate the same distinct subset of genes and have indistinguishable phenotypic characteristics. Importantly, Mediator containing the spSrb8/spTrap240/spSrb10/spSrb11 subunits is isolated only in free form, devoid of RNA polymerase II. In contrast, Mediator lacking this module associates with the polymerase. Our findings provide experimental evidence for recent suggestions that TRAP230/ARC240 and TRAP240/ARC250 may indeed be the Srb8 and Srb9 homologues of mammalian Mediator. Apparently Srb8/TRAP230/ARC240, Srb9/TRAP240/ARC250, Srb10, and Srb11 constitute a conserved Mediator submodule, which is involved in negative regulation of transcription in all eukaryotes.","authors":"Samuelsen CO, Baraznenok V, Khorosjutina O, Spahr H, Kieselbach T, Holmberg S, Gustafsson CM","authors_abbrev":"Samuelsen CO et al.","pubmed_publication_date":"27 May 2003","pubmed_entrez_date":"2003-05-10","publication_year":"2003","canto_session_key":"9162fb69e5c194af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-10-24 20:41:33","canto_approved_date":"2019-10-24 20:41:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-10-24 20:41:26","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23G3.01","SPBC28F2.12","SPAC23H4.17c","HGNC:22474","SPBC1861.02","SPBC31F10.03","SPBC947.04","SPBPB2B2.01","SPBC1198.02","SPCC1742.01","SPAC1F8.06","SPAC186.01","SPBPB7E8.01","SPACUNK4.10","SPAC2E1P3.05c","SPAPB24D3.07c","SPBC12D12.06","SPBC14F5.08","SPBC21.04","SPAC343.12","SPAC56F8.12","SPAC5D6.05","SPAC589.02c","SPBC31F10.04c","SPAC688.08"],"gene_count":24,"ltp_gene_count":10,"approved_date":"2019-10-24"},{"uniquename":"PMID:24118096","title":"Methionine sulphoxide reductases revisited: free methionine as a primary target of H₂O₂stress in auxotrophic fission yeast.","citation":"Mol Microbiol 2013 Dec;90(5):1113-24","abstract":"Amino acid methionine can suffer reversible oxidation to sulphoxide and further irreversible over-oxidation to methionine sulphone. As part of the cellular antioxidant scavenging activities are the methionine sulphoxide reductases (Msrs), with a reported role in methionine sulphoxide reduction, both free and in proteins. Three families of Msrs have been described, but the fission yeast genome only includes one representative for two of these families: MsrA/Mxr1 and MsrB/Mxr2. We have investigated their role in methionine reduction and H2 O2 sensitivity. We show here that MsrA/Mxr1 is able to reduce free oxidized methionine. Cells lacking each one of the genes are not significantly sensitive to different types of oxidative stresses, neither display altered life span. However, only when deletion of msrA/mxr1 is combined with deletion of met6, which confers methionine auxotrophy, the survival upon H2 O2 stress decreases by 100-fold. In fact, cells lacking only Met6, and which therefore require addition of methionine to the growth media, are extremely sensitive to H2 O2 stress. These and other evidences suggest that oxidation of free methionine is a primary target of peroxide toxicity in cells devoid of methionine biosynthetic capacity, and that an important role of Msrs is to recycle this oxidized free amino acid.","doi":"10.1111/mmi.12420","authors":"García-Santamarina S, Boronat S, Ayté J, Hidalgo E","authors_abbrev":"García-Santamarina S et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-10-15","publication_year":"2013","canto_session_key":"fea9b843c477c2cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elena Hidalgo","canto_first_approved_date":"2015-09-09 17:02:13","canto_approved_date":"2025-08-21 07:13:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-05-29 15:36:34","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Elena Hidalgo","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29E6.05c","SPAC4F10.20","SPBC216.04c","SPBC3F6.03","SPCC330.06c","SPAC22F3.10c","SPCC757.07c","SPBC577.08c","SPBC1773.02c","SPCC576.03c","SPBC56F2.11","SPAC13G7.06","SPBC36.04","SPAC24B11.06c","SPBC29B5.01","SPAC1783.07c","SPAC7D4.07c","SPBC32F12.03c"],"gene_count":18,"ltp_gene_count":9,"approved_date":"2015-09-09"},{"uniquename":"PMID:7177150","title":"Mutagenic action of structurally related alkene oxides on Schizosaccharomyces pombe: the influence, 'in vitro', of mouse-liver metabolizing system.","citation":"Mutat Res 1982 Dec;102(4):425-37","abstract":"A series of aliphatic epoxides were tested for their ability to induce forward mutations in the yeast Schizosaccharomyces pombe. For all the compounds under study, a linear dose-response relationship was found, and the ranking of the relative specific activity was: epichlorohydrin greater than ethylene oxide greater than glycidol greater than 1,2-epoxybutane greater than 1,1,1-trichloropropylene oxide greater than propylene oxide greater than 2,3-epoxybutane. The influence of the metabolic conversion of the epoxides by the mouse-liver S9 fraction was also investigated. In such conditions, except for the 2,3-epoxybutane, the genetic activity of epoxides seems to be reduced.","authors":"Migliore L, Rossi AM, Loprieno N","authors_abbrev":"Migliore L et al.","pubmed_publication_date":"Dec 1982","pubmed_entrez_date":"1982-12-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19164572","title":"Msc1 links dynamic Swi6/HP1 binding to cell fate determination.","citation":"Proc Natl Acad Sci U S A 2009 Jan 27;106(4):1163-8","abstract":"Eukaryotic genomes can be organized into distinct domains of heterochromatin or euchromatin. In the fission yeast Schizosaccharomyces pombe, assembly of heterochromatin at the silent mating-type region is critical for cell fate determination in the form of mating-type switching. Here, we report that the ubiquitin ligase, Msc1, is a critical factor required for proper cell fate determination in S. pombe. In the absence of Msc1, the in vivo mobility of Swi6 at heterochromatic foci is compromised, and centromere heterochromatin becomes hyperenriched with the heterochromatin binding protein Swi6/HP1. However, at the mating-type locus, Swi6 recruitment is defective in the absence of Msc1. Therefore, Msc1 links maintaining dynamic heterochromatin with proper heterochromatin assembly and cell fate determination. These findings have implications for understanding mechanisms of differentiation in other organisms.","doi":"10.1073/pnas.0811161106","authors":"Lawrence RJ, Volpe TA","authors_abbrev":"Lawrence RJ et al.","pubmed_publication_date":"27 Jan 2009","pubmed_entrez_date":"2009-01-24","publication_year":"2009","canto_session_key":"95569fb1c0b4c224","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-29 08:03:55","canto_approved_date":"2024-04-29 08:03:55","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-04-23 09:51:20","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":40,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c","SPCC622.16c","SPBC83.03c","SPAC23H4.12","SPBP35G2.10","SPAC18G6.02c","SPCC663.12","SPBC2D10.17","SPAC664.01c","SPBC800.03","SPBC428.08c","SPAC1B3.17","SPBC16D10.07c","SPAC6F12.09","SPCC1739.03","SPBC36.05c","SPBC11B10.10c","SPCC736.11","SPAC343.11c"],"gene_count":19,"ltp_gene_count":3,"approved_date":"2024-04-29"},{"uniquename":"PMID:12951513","title":"Isolation of suppressor mutants of phosphatidylinositol 3-phosphate 5-kinase deficient cells in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2003 Aug;67(8):1772-9","abstract":"The ste12+ gene of Schizosaccharomyces pombe codes for a phosphatidylinositol (PI) 3-phosphate 5'-kinase, which is required for efficient mating. Suppressor mutants for sterility of ste12Delta cells were screened for. Most of the mutant genes turned out to be recessive. Six genes were cloned and the open reading frames responsible for the suppressor activity were identified. They included genes coding for proteins with domains homologous to calcium transporters, casein kinase II, UBC13, AMSH, Vps23p, and Vps27p of Saccharomyces cerevisiae. Disruption of these genes resulted in suppression of the defects of the ste12Delta cells, including low mating efficiency and formation of large vacuoles. Since many of these gene products are homologous to the proteins involved in vesicle transport, sterility caused by inactivation of ste12 may be due to a disordered vesicle transport system.","authors":"Onishi M, Nakamura Y, Koga T, Takegawa K, Fukui Y","authors_abbrev":"Onishi M et al.","pubmed_publication_date":"Aug 2003","pubmed_entrez_date":"2003-09-03","publication_year":"2003","canto_session_key":"b7cd99483b431d7b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-02 11:19:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-02 11:19:12","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11E3.04c","SPBC3E7.01","SPAC19A8.05c","SPAC19B12.10","SPAC11H11.01","SPAC521.04c","SPBP35G2.05c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2014-07-02"},{"uniquename":"PMID:20129053","title":"The nuclear poly(A)-binding protein interacts with the exosome to promote synthesis of noncoding small nucleolar RNAs.","citation":"Mol Cell 2010 Jan 15;37(1):34-45","abstract":"Poly(A)-binding proteins (PABPs) are important to eukaryotic gene expression. In the nucleus, the PABP PABPN1 is thought to function in polyadenylation of pre-mRNAs. Deletion of fission yeast pab2, the homolog of mammalian PABPN1, results in transcripts with markedly longer poly(A) tails, but the nature of the hyperadenylated transcripts and the mechanism that leads to RNA hyperadenylation remain unclear. Here we report that Pab2 functions in the synthesis of noncoding RNAs, contrary to the notion that PABPs function exclusively on protein-coding mRNAs. Accordingly, the absence of Pab2 leads to the accumulation of polyadenylated small nucleolar RNAs (snoRNAs). Our findings suggest that Pab2 promotes poly(A) tail trimming from pre-snoRNAs by recruiting the nuclear exosome. This work unveils a function for the nuclear PABP in snoRNA synthesis and provides insights into exosome recruitment to polyadenylated RNAs.","doi":"10.1016/j.molcel.2009.12.019","authors":"Lemay JF, D'Amours A, Lemieux C, Lackner DH, St-Sauveur VG, Bähler J, Bachand F","authors_abbrev":"Lemay JF et al.","pubmed_publication_date":"15 Jan 2010","pubmed_entrez_date":"2010-02-05","publication_year":"2010","canto_session_key":"a8bdbe7f398d38ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-01-18 16:26:52","canto_approved_date":"2026-01-29 17:21:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-19 12:23:20","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":40,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.01","SPSNORNA.32","SPAC12G12.13c","SPSNORNA.25","SPSNORNA.46","SPSNORNA.34","SPAC4H3.10c","SPBC26H8.10","SPSNORNA.35","SPSNORNA.28","SPSNORNA.16","SPSNORNA.47","SPCC13B11.01","SPSNORNA.52","SPBC16E9.12c","SPSNORNA.37","SPSNORNA.40","SPSNORNA.50"],"gene_count":18,"ltp_gene_count":4,"approved_date":"2019-01-18"},{"uniquename":"PMID:40987243","title":"Metabolic control of cytokinesis by glucose cAMP-PKA signaling in fission yeast.","citation":"Microbiol Res 2025 Sep 19;302:128345","abstract":"Cytokinesis, the final step of cell division, must be precisely coordinated with the cellular metabolic status, yet the underlying regulatory mechanisms remain poorly understood. Here we show that in Schizosaccharomyces pombe, glucose signaling promotes cytokinesis via the evolutionarily conserved cAMP-PKA signaling pathway. Loss of the Pka1 catalytic subunit delays assembly and constriction of the contractile actomyosin ring (CAR), whereas constitutive PKA activation enhances CAR integrity and accelerates cytokinesis. Mechanistically, Pka1 downregulates the basal activity of the stress-activated MAPK Sty1 under glucose-rich conditions, thereby stabilizing the formin For3 and its nucleated actin cables, which collaborate to regulate CAR dynamics. Remarkably, cAMP-PKA signaling also facilitates cytokinesis through a parallel, actin cable-independent mechanism. Additionally, mitochondrial respiration contributes to cytokinesis in the presence of glucose through a PKA-independent pathway. These findings reveal a multilayered network that links carbon source metabolism to cytoskeletal organization and underscore the importance of tight PKA activity control for robust cell division.","doi":"10.1016/j.micres.2025.128345","authors":"Marín-Castillo A, León-Zaragoza S, Franco A, Vicente-Soler J, Núñez A, Soto T, Madrid M, Cansado J","authors_abbrev":"Marín-Castillo A et al.","pubmed_publication_date":"19 Sep 2025","pubmed_entrez_date":"2025-09-23","publication_year":"2025","canto_session_key":"29cbb921be4b4520","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-24 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16698922","title":"Hsk1 kinase is required for induction of meiotic dsDNA breaks without involving checkpoint kinases in fission yeast.","citation":"Proc Natl Acad Sci U S A 2006 May 23;103(21):8131-6","abstract":"Cdc7 kinase, conserved through evolution, is known to be essential for mitotic DNA replication. The role of Cdc7 in meiotic recombination was suggested in Saccharomyces cerevisiae, but its precise role has not been addressed. Here, we report that Hsk1, the Cdc7-related kinase in Schizosaccharomyces pombe, plays a crucial role during meiosis. In a hsk1 temperature-sensitive strain (hsk1-89), meiosis is arrested with one nucleus state before meiosis I in most of the cells and meiotic recombination frequency is reduced by one order of magnitude, whereas premeiotic DNA replication is delayed but is apparently completed. Strikingly, formation of meiotic dsDNA breaks (DSBs) are largely impaired in the mutant, and Hsk1 kinase activity is essential for these processes. Deletion of all three checkpoint kinases, namely Cds1, Chk1, and Mek1, does not restore DSB formation, meiosis, or Cdc2 activation, which is suppressed in hsk1-89, suggesting that these aberrations are not caused by known checkpoint pathways but that Hsk1 may regulate DSB formation and meiosis. Whereas transcriptional induction of some rec genes and horsetail movement are normal, chromatin remodeling at ade6-M26, a recombination hotspot, which is prerequisite for subsequent DSB formation at this locus, is not observed in hsk1-89. These results indicate unique and essential roles of Hsk1 kinase in the initiation of meiotic recombination and meiosis.","authors":"Ogino K, Hirota K, Matsumoto S, Takeda T, Ohta K, Arai K, Masai H","authors_abbrev":"Ogino K et al.","pubmed_publication_date":"23 May 2006","pubmed_entrez_date":"2006-05-16","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34349749","title":"Exomer Is Part of a Hub Where Polarized Secretion and Ionic Stress Connect.","citation":"Front Microbiol 2021;12:708354","abstract":"Plasma membrane and membranous organelles contribute to the physiology of the Eukaryotic cell by participating in vesicle trafficking and the maintenance of ion homeostasis. Exomer is a protein complex that facilitates vesicle transport from the  trans -Golgi network to the plasma membrane, and its absence leads to the retention of a set of selected cargoes in this organelle. However, this retention does not explain all phenotypes observed in exomer mutants. The  Schizosaccharomyces pombe  exomer is composed of Cfr1 and Bch1, and  cfr1Δ  and  bch1Δ  were sensitive to high concentrations of potassium salts but not sorbitol, which showed sensitivity to ionic but not osmotic stress. Additionally, the activity of the plasma membrane ATPase was higher in exomer mutants than in the wild-type, pointing to membrane hyperpolarization, which caused an increase in intracellular K +  content and mild sensitivity to Na + , Ca 2+ , and the aminoglycoside antibiotic hygromycin B. Moreover, in response to K +  shock, the intracellular Ca 2+  level of  cfr1Δ  cells increased significantly more than in the wild-type, likely due to the larger Ca 2+  spikes in the mutant. Microscopy analyses showed a defective endosomal morphology in the mutants. This was accompanied by an increase in the intracellular pools of the K +  exporting P-type ATPase Cta3 and the plasma membrane Transient Receptor Potential (TRP)-like Ca 2+  channel Pkd2, which were partially diverted from the  trans -Golgi network to the prevacuolar endosome. Despite this, most Cta3 and Pkd2 were delivered to the plasma membrane at the cell growing sites, showing that their transport from the  trans -Golgi network to the cell surface occurred in the absence of exomer. Nevertheless, shortly after gene expression in the presence of KCl, the polarized distribution of Cta3 and Pkd2 in the plasma membrane was disturbed in the mutants. Finally, the use of fluorescent probes suggested that the distribution and dynamics of association of some lipids to the plasma membrane in the presence of KCl were altered in the mutants. Thus, exomer participation in the response to K +  stress was multifaceted. These results supported the notion that exomer plays a general role in protein sorting at the  trans -Golgi network and in polarized secretion, which is not always related to a function as a selective cargo adaptor.","doi":"10.3389/fmicb.2021.708354","authors":"Moro S, Moscoso-Romero E, Poddar A, Mulet JM, Perez P, Chen Q, Valdivieso MH","authors_abbrev":"Moro S et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-08-05","publication_year":"2021","canto_session_key":"6464e04ca419e15b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-12-30 10:01:27","canto_approved_date":"2024-12-30 10:01:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-15 16:17:50","canto_added_date":"2021-08-07 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":90,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC794.11c","SPAC105.01c","SPCC1322.03","SPAC19A8.04","SPAC1F3.05","SPAC1F7.03","SPAC19G12.14","SPCC965.06","SPAPB2B4.04c","SPAC1639.02c","SPBC31E1.02c","SPBC651.11c","SPBP16F5.07","SPAC18B11.10","SPBC31F10.16","SPAC3F10.02c","SPAC6G9.12","SPAC6F6.01","SPCC663.14c","SPBC337.09","SPBC25H2.16c","SPAC630.14c","SPAC1F5.08c","SPBC839.06"],"gene_count":24,"ltp_gene_count":23,"approved_date":"2024-12-30"},{"uniquename":"PMID:27140925","title":"Molecular Genetic Tools and Techniques in Fission Yeast.","citation":"Cold Spring Harb Protoc 2016 May 02;2016(5)","abstract":"The molecular genetic tools used in fission yeast have generally been adapted from methods and approaches developed for use in the budding yeast, Saccharomyces cerevisiae Initially, the molecular genetics of Schizosaccharomyces pombe was developed to aid gene identification, but it is now applied extensively to the analysis of gene function and the manipulation of noncoding sequences that affect chromosome dynamics. Much current research using fission yeast thus relies on the basic processes of introducing DNA into the organism and the extraction of DNA for subsequent analysis. Targeted integration into specific genomic loci is often used to create site-specific mutants or changes to noncoding regulatory elements for subsequent phenotypic analysis. It is also regularly used to introduce additional sequences that generate tagged proteins or to create strains in which the levels of wild-type protein can be manipulated through transcriptional regulation and/or protein degradation. Here, we draw together a collection of core molecular genetic techniques that underpin much of modern research using S. pombe We summarize the most useful methods that are routinely used and provide guidance, learned from experience, for the successful application of these methods.","doi":"10.1101/pdb.top087601","authors":"Murray JM, Watson AT, Carr AM","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"02 May 2016","pubmed_entrez_date":"2016-05-04","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-05-05 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31053915","title":"Catechol O-methyltransferase homologs in Schizosaccharomyces pombe are response factors to alkaline and salt stress.","citation":"Appl Microbiol Biotechnol 2019 Jun;103(12):4881-4887","abstract":"How cells of the fission yeast Schizosaccharomyces pombe respond to alkaline stress is not well understood. Here, to elucidate the molecular mechanism underlying the alkaline stress response in S. pombe, we performed DNA microarray analysis. We found that a homolog of human catechol O-methyltransferase 2 (COMT2) is highly upregulated in S. pombe cells exposed to alkaline conditions. We designated the S. pombe homolog as cmt2 +  and also identified its paralog, cmt1 + , in the S. pombe genome. Reverse transcription PCR confirmed that both cmt1 +  and cmt2 +  are upregulated within 1 h of exposure to alkaline stress and downregulated within 30 min of returning to an acidic environment. Moreover, we verified that recombinant Cmt proteins exhibit catechol O-methyltransferase activity. To further characterize the expression of cmt1 +  and cmt2 + , we carried out an EGFP reporter assay using their promoter sequences, which showed that both genes respond not only to alkaline but also to salt stress. Collectively, our findings indicate that the cmt promoter might be an advantageous expression system for use in S. pombe under alkaline culture conditions.","doi":"10.1007/s00253-019-09858-0","authors":"Tominaga A, Higuchi Y, Mori H, Akai M, Suyama A, Yamada N, Takegawa K","authors_abbrev":"Tominaga A et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-05-05","publication_year":"2019","canto_session_key":"e9324976499786d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2019-05-17 12:44:16","canto_approved_date":"2024-01-03 16:50:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-17 07:23:06","canto_added_date":"2019-05-07 00:15:04","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.03","SPBPB21E7.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-05-17"},{"uniquename":"GO_REF:0000027","title":"BLAST search criteria for ISS assignment in PAMGO_GAT","abstract":"This GO reference describes the criteria used in assigning the evidence code of ISS via BLAST searches to annotate gene products from PAMGO_GAT. Standard BLASTP from NCBI was used (http://www.ncbi.nih.gov/blast) to query the non-redundant (NR) database. Hits are considered to be significant if the E-value is at or less than 10^-4. All other parameters are default according to http://www.ncbi.nih.gov/blast.","authors":"PAMGO_GAT curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25318672","title":"Increase in cellular triacylglycerol content and emergence of large ER-associated lipid droplets in the absence of CDP-DG synthase function.","citation":"Mol Biol Cell 2014 Dec 15;25(25):4083-95","abstract":"Excess fatty acids and sterols are stored as triacylglycerols and sterol esters in specialized cellular organelles, called lipid droplets. Understanding what determines the cellular amount of neutral lipids and their packaging into lipid droplets is of fundamental and applied interest. Using two species of fission yeast, we show that cycling cells deficient in the function of the ER-resident CDP-DG synthase Cds1 exhibit markedly increased triacylglycerol content and assemble large lipid droplets closely associated with the ER membranes. We demonstrate that these unusual structures recruit the triacylglycerol synthesis machinery and grow by expansion rather than by fusion. Our results suggest that interfering with the CDP-DG route of phosphatidic acid utilization rewires cellular metabolism to adopt a triacylglycerol-rich lifestyle reliant on the Kennedy pathway.","doi":"10.1091/mbc.E14-03-0832","authors":"He Y, Yam C, Pomraning K, Chin JS, Yew JY, Freitag M, Oliferenko S","authors_abbrev":"He Y et al.","pubmed_publication_date":"15 Dec 2014","pubmed_entrez_date":"2014-10-17","publication_year":"2014","canto_session_key":"0e38008c9ffaccbe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Snezhana Oliferenko","canto_first_approved_date":"2021-05-14 13:03:30","canto_approved_date":"2023-05-03 13:05:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-29 14:17:48","canto_added_date":"2014-10-18 00:15:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Snezhana Oliferenko","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC13A2.03","SPBC776.14","SPCC1235.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2021-05-14"},{"uniquename":"PMID:20162536","title":"Reagents for investigating MAPK signalling in model yeast species.","citation":"Yeast 2010 Jul;27(7):423-30","abstract":"Here we present a set of resources (bacterial expression plasmids and antibodies) for the interrogation of proteins involved in yeast MAPK signalling. We constructed bacterial protein expression plasmids for 25 proteins involved in MAPK signalling in budding yeast. From these constructs we expressed and purified proteins and generated rabbit polyclonal antibodies against 13 proteins in the pheromone MAPK pathway. We verified the specificity of the antibodies and employed them to follow pathway proteins in cells stimulated with pheromone. We show that these reagents can be used to detect pheromone-induced post-translational modifications and changes in the oligomeric state of pathway proteins. In addition to recognizing their target proteins in Saccharomyces cerevisiae, these antibodies allow the detection of predicted orthologues in the distant evolutionary relatives Kluyveromyces lactis and Schizosaccharomyces pombe. These antibodies are new tools for investigating MAPK signalling in model yeast species and may be useful for studying MAPK signalling in higher eukaryotes.","doi":"10.1002/yea.1758","authors":"Pincus D, Benjamin K, Burbulis I, Tsong AE, Resnekov O","authors_abbrev":"Pincus D et al.","pubmed_publication_date":"Jul 2010","pubmed_entrez_date":"2010-02-18","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42130072","title":"Enzyme structure and kinetics produce tRNA and nucleotide specificity of Schizosaccharomyces pombe CC- and A-adding enzymes.","citation":"Nucleic Acids Res 2026 May 05;54(9)","abstract":"Transfer RNAs (tRNAs) are transcribed and then processed through a series of post-transcriptional steps to produce mature forms that are charged with amino acids for translation. A CCA sequence is added at their 3' ends as the site of aminoacylation. Although a single enzyme typically adds the CCA tail without a nucleic acid template, Schizosaccharomyces pombe encodes two enzymes: CCA1 that adds the two cytosines and CCA2 that adds the adenosine. Here we explore how these two S. pombe enzymes evolved specificity to generate the 3' CCA tails. Enzymology (activity and kinetic assays) indicates distinct nucleotide addition specificity. CCA1 adds the sequential cytosines with a slower first addition followed by a quicker second addition. CCA2 then rapidly adds the terminal adenosine. Moreover, structural biology (crystal structures and molecular dynamics simulations) explains how the active site configuration and distances between active site and tRNA elbow binding residues of CCA1 and CCA2 restrict their tRNA substrate specificity. Together the data presented here describe how S. pombe CCA1 and CCA2 interrogate complete reaction complexes of tRNA and nucleotide substrates that arrange the particular components for active site catalysis and therefore specificity.","doi":"10.1093/nar/gkag475","authors":"Sikkema AP, Klemm BP, Perera L, Hall TMT","authors_abbrev":"Sikkema AP et al.","pubmed_publication_date":"05 May 2026","pubmed_entrez_date":"2026-05-14","publication_year":"2026","canto_session_key":"b4f5b4043e6f4421","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-05-14 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1093.04c","SPCC645.10"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"9ns3","gene_chains":[{"gene_uniquename":"SPAC1093.04c","chain":"A","position":"2-500"}],"title":"Structure of S. pombe CC-Adding Enzyme in complex with CTP","entry_authors":"Sikkema AP,Hall TMT","entry_authors_abbrev":"Sikkema AP et al.","reference_uniquename":"PMID:42130072","experimental_method":"X-ray","resolution":"2.05"},{"pdb_id":"9ns4","gene_chains":[{"gene_uniquename":"SPCC645.10","chain":"A","position":"1-484"}],"title":"Structure of S. pombe A-Adding Enzyme","entry_authors":"Sikkema AP,Hall TMT","entry_authors_abbrev":"Sikkema AP et al.","reference_uniquename":"PMID:42130072","experimental_method":"X-ray","resolution":"2.1"},{"pdb_id":"9ns2","gene_chains":[{"gene_uniquename":"SPAC1093.04c","chain":"A","position":"2-500"}],"title":"Structure of S. pombe CC-Adding Enzyme in complex with Pyrophosphate","entry_authors":"Sikkema AP,Hall TMT","entry_authors_abbrev":"Sikkema AP et al.","reference_uniquename":"PMID:42130072","experimental_method":"X-ray","resolution":"1.95"}]},{"uniquename":"PMID:18514516","title":"Rec25 and Rec27, novel linear-element components, link cohesin to meiotic DNA breakage and recombination.","citation":"Curr Biol 2008 Jun 03;18(11):849-54","abstract":"Meiosis is a specialized nuclear division by which sexually reproducing diploid organisms generate haploid gametes. Recombination between homologous chromosomes facilitates accurate meiotic chromosome segregation and is initiated by DNA double-strand breaks (DSBs) made by the conserved topoisomerase-like protein Spo11 (Rec12 in fission yeast), but DSBs are not evenly distributed across the genome. In Schizosaccharomyces pombe, proteinaceous structures known as linear elements (LinEs) are formed during meiotic prophase. The meiosis-specific cohesin subunits Rec8 and Rec11 are essential for DSB formation in some regions of the genome, as well as for formation of LinEs or the related synaptonemal complex (SC) in other eukaryotes. Proteins required for DSB formation decorate LinEs, and mutants lacking Rec10, a major component of LinEs, are completely defective for recombination. Although recombination may occur in the context of LinEs, it is not well understood how Rec10 is loaded onto chromosomes. We describe two novel components of LinEs in fission yeast, Rec25 and Rec27. Comparisons of rec25Delta, rec27Delta, and rec10Delta mutants suggest multiple pathways to load Rec10. In the major pathway, Rec10 is loaded, together with Rec25 and Rec27, in a Rec8-dependent manner with subsequent region-specific effects on recombination.","doi":"10.1016/j.cub.2008.05.025","authors":"Davis L, Rozalén AE, Moreno S, Smith GR, Martín-Castellanos C","authors_abbrev":"Davis L et al.","pubmed_publication_date":"03 Jun 2008","pubmed_entrez_date":"2008-06-03","publication_year":"2008","canto_session_key":"7169c40527631f2c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-07 14:38:51","canto_approved_date":"2021-04-22 16:16:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-08-07 14:38:46","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC577.05c","SPAC25G10.04c","SPBC29A10.14","SPAC17A5.18c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-08-07"},{"uniquename":"PMID:23271606","title":"Fission yeast TOR signaling is essential for the down-regulation of a hyperactivated stress-response MAP kinase under salt stress.","citation":"Mol Genet Genomics 2013 Feb;288(1-2):63-75","abstract":"TOR (target of rapamycin) signaling regulates cell growth and division in response to environmental stimuli such as the availability of nutrients and various forms of stress. The vegetative growth of fission yeast cells, unlike other eukaryotic cells, is not inhibited by treatment with rapamycin. We found that certain mutations including pmc1Δ (Ca(2+)-ATPase), cps9-193 (small GTPase, Ryh1) and cps1-12 (1,3-β-D-glucan synthase, Bgs1) confer a rapamycin-sensitive phenotype to cells under salt stress with potassium chloride (>0.5 M). Cytometric analysis revealed that the mutant cells were unable to enter the mitotic cell cycle when treated with the drug under salt stress. Gene cloning and overexpression experiments revealed that the sensitivity to rapamycin was suppressed by the ectopic expression of tyrosine phosphatases, Pyp1 and Pyp2, which are negative regulators of Spc1/Sty1 mitogen-activated protein kinase (MAPK). The level of tyrosine phosphorylation on Spc1 was higher and sustained substantially longer in these mutants than in the wild type under salt stress. The hyperphosphorylation was significantly suppressed by overexpression of pyp1 (+) with concomitant resumption of the mutant cells' growth. In fission yeast, TOR signaling has been thought to stimulate the stress-response pathway, because mutations of TORC2 components such as Tor1, Sin1 and Ste20 result in similar sensitive phenotypes to environmental stress. The present study, however, strongly suggests that TOR signaling is required for the down-regulation of a hyperactivated Spc1 for reentry into the mitotic cell cycle. This finding may shed light on our understanding of a new stress-responsive mechanism in TOR signaling in higher organisms.","doi":"10.1007/s00438-012-0731-7","authors":"Ishiguro J, Shibahara K, Ueda Y, Nakamura K","authors_abbrev":"Ishiguro J et al.","pubmed_publication_date":"Feb 2013","pubmed_entrez_date":"2012-12-29","publication_year":"2013","canto_session_key":"b1f440be3b3e4718","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC839.17c","SPBC19G7.05c","SPAC19D5.01","SPBC887.10","SPBC1A4.10c","SPBP4H10.04","SPCC24B10.07","SPAC4C5.02c","SPAC26F1.10c","SPBC1685.01"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:36230163","title":"Diversity of Volatile Aroma Compound Composition Produced by Non- Saccharomyces  Yeasts in the Early Phase of Grape Must Fermentation.","citation":"Foods 2022 Oct 05;11(19)","abstract":"There is a lack of studies evaluating the metabolic contribution of non- Saccharomyces  yeasts in early fermentation phases. This study aimed to investigate the volatile aroma profiles produced by various non- Saccharomyces  yeasts just before sequential inoculation with  Saccharomyces cerevisiae  to provide an insight into the particular effects they induce at this stage. The grape must of Malvazija istarska was inoculated with monocultures of  Torulaspora delbrueckii ,  Metschnikowia pulcherrima ,  Pichia kluyveri ,  Lachancea thermotolerans , and  Schizosaccharomyces pombe , alongside a  S. cerevisiae  control. Eighty volatile compounds were quantified via headspace solid-phase microextraction and gas chromatography-mass spectrometry, and the data were statistically elaborated. Volatile profiles of non- Saccharomyces  yeasts differed significantly from the  S. cerevisiae  control. Most treatments caused increases in linalool and β-damascenone, decreases in higher alcohols and fatty acids, and improved synthesis of odoriferous esters.  Torulaspora delbrueckii  and  M. pulcherrima  produced compounds not commonly found in  S. cerevisiae  fermented wines. Multivariate statistical analysis linked the investigated yeasts to specific, particularly abundant compounds. Future studies should explore to what degree these contributions persist after sequential inoculation with  S. cerevisiae  in diverse grape must matrices.","doi":"10.3390/foods11193088","authors":"Delač Salopek D, Horvat I, Hranilović A, Plavša T, Radeka S, Pasković I, Lukić I","authors_abbrev":"Delač Salopek D et al.","pubmed_publication_date":"05 Oct 2022","pubmed_entrez_date":"2022-10-14","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-10-16 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28469148","title":"Functional organization of protein determinants of meiotic DNA break hotspots.","citation":"Sci Rep 2017 May 03;7(1):1393","abstract":"During Schizosaccharomyces pombe meiotic prophase, homologous chromosomes are co-aligned by linear elements (LinEs) analogous to the axial elements of the synaptonemal complex (SC) in other organisms. LinE proteins also promote the formation of meiotic DNA double-strand breaks (DSBs), the precursors of cross-overs. Rec10 is required for essentially all DSBs and recombination, and three others (Rec25, Rec27, and Mug20) are protein determinants of DSB hotspots - they bind DSB hotspots with high specificity and are required for DSB formation there. These four LinE proteins co-localize in the nucleus in an interdependent way, suggesting they form a complex. We used random mutagenesis to uncover recombination-deficient missense mutants with novel properties. Some missense mutations changed essential residues conserved among Schizosaccharomyces species. DSB formation, gene conversion, and crossing-over were coordinately reduced in the mutants tested. Based on our mutant analysis, we revised the rec27 open reading frame: the new start codon is in the previously annotated first intron. Genetic and fluorescence-microscopy assays indicated that the Rec10 N- and C-terminal regions have complex interactions with Rec25. These mutants are a valuable resource to elucidate further how LinE proteins and the related SCs of other species regulate meiotic DSB formation to form crossovers crucial for meiosis.","doi":"10.1038/s41598-017-00742-3","authors":"Ma L, Fowler KR, Martín-Castellanos C, Smith GR","authors_abbrev":"Ma L et al.","pubmed_publication_date":"03 May 2017","pubmed_entrez_date":"2017-05-05","publication_year":"2017","canto_session_key":"dc43fea8ff20c487","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lijuan Ma","canto_first_approved_date":"2017-09-29 13:19:50","canto_approved_date":"2019-02-21 17:22:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-09-25 06:35:02","canto_added_date":"2017-05-06 00:15:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":42,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Lijuan Ma","community_curator":true,"annotation_count":42,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.04c","SPAC17A5.18c","SPBC36B7.06c","SPAC22G7.06c","SPBC577.05c","SPAC56F8.10","SPCC1322.13","SPCC777.09c","SPAC227.18"],"gene_count":9,"ltp_gene_count":4,"approved_date":"2017-09-29"},{"uniquename":"PMID:26368668","title":"Dynamics of an Active-Site Flap Contributes to Catalysis in a JAMM Family Metallo Deubiquitinase.","citation":"Biochemistry 2015 Oct 06;54(39):6038-51","abstract":"The endosome-associated deubiquitinase (DUB) AMSH is a member of the JAMM family of zinc-dependent metallo isopeptidases with high selectivity for Lys63-linked polyubiquitin chains, which play a key role in endosomal-lysosomal sorting of activated cell surface receptors. The catalytic domain of the enzyme features a flexible flap near the active site that opens and closes during its catalytic cycle. Structural analysis of its homologues, AMSH-LP (AMSH-like protein) and the fission yeast counterpart, Sst2, suggests that a conserved Phe residue in the flap may be critical for substrate binding and/or catalysis. To gain insight into the contribution of this flap in substrate recognition and catalysis, we generated mutants of Sst2 and characterized them using a combination of enzyme kinetics, X-ray crystallography, molecular dynamics simulations, and isothermal titration calorimetry (ITC). Our analysis shows that the Phe residue in the flap contributes key interactions during the rate-limiting step but not to substrate binding, since mutants of Phe403 exhibit a defect only in kcat but not in KM. Moreover, ITC studies show Phe403 mutants have similar KD for ubiquitin compared to the wild-type enzyme. The X-ray structures of both Phe403Ala and the Phe403Trp, in both the free and ubiquitin bound form, reveal no appreciable structural change that might impair substrate or alter product binding. We observed that the side chain of the Trp residue is oriented identically with respect to the isopeptide moiety of the substrate as the Phe residue in the wild-type enzyme, so the loss of activity seen in this mutant cannot be explained by the absence of a group with the ability to provide van der Waals interactions that facilitate the hyrdolysis of the Lys63-linked diubiquitin. Molecular dynamics simulations indicate that the flap in the Trp mutant is quite flexible, allowing almost free rotation of the indole side chain. Therefore, it is possible that these different dynamic properties of the flap in the Trp mutant, compared to the wild-type enzyme, manifest as a defect in interactions that facilitate the rate-limiting step. Consistent with this notion, the Trp mutant was able to cleave Lys48-linked and Lys11-linked diubiquitin better than the wild-type enzyme, indicating altered mobility and hence reduced selectivity.","doi":"10.1021/acs.biochem.5b00631","authors":"Bueno AN, Shrestha RK, Ronau JA, Babar A, Sheedlo MJ, Fuchs JE, Paul LN, Das C","authors_abbrev":"Bueno AN et al.","pubmed_publication_date":"06 Oct 2015","pubmed_entrez_date":"2015-09-15","publication_year":"2015","canto_session_key":"9baf78ee15c2e5b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-03-15 09:37:14","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-01-28 11:25:37","canto_added_date":"2015-09-16 00:19:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19B12.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-01-28"},{"uniquename":"PMID:26976145","title":"Microtubule dynamics decoded by the epigenetic state of centromeric chromatin.","citation":"Curr Genet 2016 Nov;62(4):691-695","abstract":"Cell division with accurate chromosome segregation is fundamental to cell survival of all organisms. The precise molecular mechanisms that ensure accurate chromosome segregation are still being discovered using a variety of experimental systems and approaches. Microtubule attachment to the kinetochore is a prerequisite for mitotic progression, failure of which activates the spindle assembly checkpoint (SAC). The dynamic tension generated by interaction of the centromere, kinetochore and microtubules is a key regulator of the SAC. Here, in the context of current literature we discuss our recent observation in fission yeast that epigenetic alterations in centromeric and pericentromeric chromatin can compensate for altered dynamics of kinetochore-microtubule attachment to permit escape from mitotic arrest. A role for the spatial configuration of the centromere to influence the finely tuned regulators of mitotic progression opens up new avenues for research.","authors":"George AA, Walworth NC","authors_abbrev":"George AA et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-03-16","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009839","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12419203","title":"Cell cycle: new functions for Cdc14 family phosphatases.","citation":"Curr Biol 2002 Oct 29;12(21):R733-5","abstract":"The Cdc14 phosphatase was identified by its requirement for mitotic exit in budding yeast. Cdc14 homologs exist throughout the eukaryotic kingdom, but it was unclear whether their function would also be conserved. Recent analyses in fission yeast, humans and now C. elegans suggest numerous other functions for this family of proteins.","authors":"Trautmann S, McCollum D","authors_abbrev":"Trautmann S et al.","pubmed_publication_date":"29 Oct 2002","pubmed_entrez_date":"2002-11-07","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12482946","title":"Dicer is required for chromosome segregation and gene silencing in fission yeast cells.","citation":"Proc Natl Acad Sci U S A 2002 Dec 24;99(26):16648-53","abstract":"RNA interference is a form of gene silencing in which the nuclease Dicer cleaves double-stranded RNA into small interfering RNAs. Here we report a role for Dicer in chromosome segregation of fission yeast. Deletion of the Dicer (dcr1+) gene caused slow growth, sensitivity to thiabendazole, lagging chromosomes during anaphase, and abrogated silencing of centromeric repeats. As Dicer in other species, Dcr1p degraded double-stranded RNA into approximately 23 nucleotide fragments in vitro, and dcr1Delta cells were partially rescued by expression of human Dicer, indicating evolutionarily conserved functions. Expression profiling demonstrated that dcr1+ was required for silencing of two genes containing a conserved motif.","authors":"Provost P, Silverstein RA, Dishart D, Walfridsson J, Djupedal I, Kniola B, Wright A, Samuelsson B, Radmark O, Ekwall K","authors_abbrev":"Provost P et al.","pubmed_publication_date":"24 Dec 2002","pubmed_entrez_date":"2002-12-17","publication_year":"2002","canto_session_key":"c72c3efc43c47d0d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2020-03-14 18:43:53","canto_approved_date":"2026-01-26 11:17:34","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-03-14 18:43:30","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c","SPNCRNA.231","SPBC3E7.02c","SPBC19C7.04c"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2020-03-14"},{"uniquename":"PMID:25194487","title":"Genetics advances in autosomal dominant focal epilepsies: focus on DEPDC5.","citation":"Prog Brain Res 2014;213:123-39","abstract":"Rare multiplex families with autosomal dominant focal epilepsies have been described with specific age-related and electroclinical syndromes: autosomal dominant nocturnal frontal lobe epilepsy (ADNFLE), familial temporal lobe epilepsy (FTLE), and familial focal epilepsy with variable foci (FFEVF). Molecular genetic advances in inherited focal epilepsies have pinpointed their genetic heterogeneity and the fact that they are mediated by different biological pathways: ion channel subunit genes have been linked to ADNFLE (CHRNA4, CHRNA2, CHRNB2, and KCNT1, encoding, respectively, the α4, α2, and β2 subunits of the neuronal nicotinic acetylcholine receptor, and a potassium channel subunit); neuronal secreted protein (LGI1-encoding epitempin) has been linked to autosomal dominant epilepsy with auditory features; and mTORC1-repressor DEPDC5 (DEP domain-containing protein 5) gene has recently been reported in a broad spectrum of inherited focal epilepsies (ADNFLE, FTLE, FFEVF). This chapter focuses on DEPDC5, a newly identified gene.","doi":"10.1016/B978-0-444-63326-2.00007-7","authors":"Baulac S","authors_abbrev":"Baulac S","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-09-08","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC26H8.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24531725","title":"Centromeric barrier disruption leads to mitotic defects in Schizosaccharomyces pombe.","citation":"G3 (Bethesda) 2014 Apr 16;4(4):633-42","abstract":"Centromeres are cis-acting chromosomal domains that direct kinetochore formation, enabling faithful chromosome segregation and preserving genome stability. The centromeres of most eukaryotic organisms are structurally complex, composed of nonoverlapping, structurally and functionally distinct chromatin subdomains, including the specialized core chromatin that underlies the kinetochore and pericentromeric heterochromatin. The genomic and epigenetic features that specify and preserve the adjacent chromatin subdomains critical to centromere identity are currently unknown. Here we demonstrate that chromatin barriers regulate this process in Schizosaccharomyces pombe. Reduced fitness and mitotic chromosome segregation defects occur in strains that carry exogenous DNA inserted at centromere 1 chromatin barriers. Abnormal phenotypes are accompanied by changes in the structural integrity of both the centromeric core chromatin domain, containing the conserved CENP-A(Cnp1) protein, and the flanking pericentric heterochromatin domain. Barrier mutant cells can revert to wild-type growth and centromere structure at a high frequency after the spontaneous excision of integrated exogenous DNA. Our results reveal a previously undemonstrated role for chromatin barriers in chromosome segregation and in the prevention of genome instability.","doi":"10.1534/g3.114.010397","authors":"Gaither TL, Merrett SL, Pun MJ, Scott KC","authors_abbrev":"Gaither TL et al.","pubmed_publication_date":"16 Apr 2014","pubmed_entrez_date":"2014-02-18","publication_year":"2014","canto_session_key":"f4d24384c0617a77","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:U80219","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30862564","title":"A comparative study of the proteome regulated by the Rpb4 and Rpb7 subunits of RNA polymerase II in fission yeast.","citation":"J Proteomics 2019 May 15;199:77-88","abstract":"RNA polymerase II is a conserved multi-subunit enzyme made up of twelve different subunits. Two of these subunits, Rpb4 and Rpb7, have been shown to perform functions in both transcription as well as outside of transcription in Saccharomyces cerevisiae. However, our knowledge about the roles of these subunits in Schizosaccharomyces pombe and higher eukaryotes is still limited. Moreover, both Rpb4 and Rpb7 are indispensable for viability of S. pombe and higher eukaryotes, in comparison to S. cerevisiae where deletion of only Rpb7 results in lethality. Therefore in this study, we used S. pombe strains expressing reduced levels of these subunits to determine their impact on the S. pombe proteome employing i-TRAQ based proteomics approach. Furthermore, proteomic profiling was carried out at two different time points to gain a temporal insight into the processes regulated by Rpb4 and Rpb7. The results showed that reduced levels of either Rpb4 or Rpb7 affected the expression of proteins involved in metabolism and ribosome biogenesis at both the time points. Our polysomal profiling experiments further revealed a role of these subunits in translation. Taken together, our results suggest a key role of Rpb4 and Rpb7 subunits in ribosome biogenesis and protein translation in S. pombe. SIGNIFICANCE: Rpb4 and Rpb7 subunits of RNA polymerase II are known for their diverse roles in regulating transcription, mRNA export, mRNA decay, stress response and translation in S. cerevisiae. However, their roles in other organisms are yet to be characterized in detail. Different lines of evidence also suggest that these subunits may function independently as well as a complex in budding yeast. Therefore, in the present study we employed a genome-wide quantitative proteomics-based approach to gain deeper insights into their cellular roles, and to examine if they regulate similar or different biological pathways in fission yeast. Our results provide evidence that they are both involved in primarily regulating metabolic pathways and ribosome biogenesis and also, play a role in protein translation in S. pombe.","doi":"10.1016/j.jprot.2019.03.007","authors":"Kumar D, Varshney S, Sengupta S, Sharma N","authors_abbrev":"Kumar D et al.","pubmed_publication_date":"15 May 2019","pubmed_entrez_date":"2019-03-14","publication_year":"2019","canto_session_key":"93c99c3ad75ffaf1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-07-09 23:32:13","canto_approved_date":"2019-07-09 23:32:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-07-02 03:26:14","canto_added_date":"2019-03-15 01:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.14c","SPACUNK4.06c","SPBC337.14"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2019-07-09"},{"uniquename":"PMID:10503008","title":"[RNA molecule directing the intracellular localization of the fission yeast meiotic regulator].","citation":"Tanpakushitsu Kakusan Koso 1999 Sep;44(12 Suppl):1732-40","abstract":"","authors":"Yamashita A, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-09-30","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39289458","title":"Characterization of Shy1, the Schizosaccharomyces pombe homolog of human SURF1.","citation":"Sci Rep 2024 Sep 17;14(1):21678","abstract":"Cytochrome c oxidase (complex IV) is the terminal enzyme in the mitochondrial respiratory chain. As a rare neurometabolic disorder caused by mutations in the human complex IV assembly factor SURF1, Leigh Syndrome (LS) is associated with complex IV deficiency. In this study, we comprehensively characterized Schizosaccharomyces pombe Shy1, the homolog of human SURF1. Bioinformatics analysis revealed that Shy1 contains a conserved SURF1 domain that links to the biogenesis of complex IV and shares high structural similarity with its homologs in Saccharomyces cerevisiae and humans. Our study showed that Shy1 is required for the expression of mtDNA-encoded genes and physically interacts with structural subunits and assembly factors of complex IV. Interestingly, Rip1, the subunit of ubiquinone-cytochrome c oxidoreductase or cytochrome bc 1  complex (complex III), can also co-immunoprecipitate with Shy1, suggesting Shy1 may be involved in the assembly of the mitochondrial respiratory chain supercomplexes. This conclusion is further corroborated by our BN-PAGE analysis. Unlike its homologs, deletion of shy1 does not critically disrupt respiratory chain assembly, indicating the presence of the compensatory mechanism(s) within S. pombe that ensure mitochondrial functionality. Collectively, our investigation elucidates that Shy1 plays a pivotal role in the sustainability of the regular function of mitochondria by participating in the assembly of complex IV in S. pombe.","doi":"10.1038/s41598-024-72681-9","authors":"Luo Y, Xu Y, Ahmad F, Feng G, Huang Y","authors_abbrev":"Luo Y et al.","pubmed_publication_date":"17 Sep 2024","pubmed_entrez_date":"2024-09-17","publication_year":"2024","canto_session_key":"224bb9b28b5395ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2024-09-28 07:48:42","canto_approved_date":"2024-10-08 13:52:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-09-27 12:21:14","canto_added_date":"2024-09-18 23:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMIT.10","SPMIT.05","SPMIT.08","SPMIT.01","SPBC26H8.14c","SPAC1B2.04","SPRRNA.01","SPBC119.06","SPCC338.10c","SPMIT.11","SPMIT.04","SPCC757.15","SPBC16H5.06","SPAC25B8.04c","SPRRNA.02","SPMIT.09","SPBC1604.25","SPBC1215.01","SPMIT.07"],"gene_count":19,"ltp_gene_count":8,"approved_date":"2024-09-28"},{"uniquename":"EMBL:AU011585","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3649292","title":"Nuclear pre-mRNA splicing in the fission yeast Schizosaccharomyces pombe strictly requires an intron-contained, conserved sequence element.","citation":"EMBO J 1987 Jun;6(6):1757-63","abstract":"It has recently been argued that pre-mRNA splicing in the fission yeast Schizosaccharomyces pombe may be more similar to splicing in metazoan species than in the budding yeast Saccharomyces cerevisiae. In this report we show that, contrary to this assumption, the conserved sequence element 5'-CTPu APy-3' found in all S. pombe introns 6-18 nucleotides upstream of the 3' splice site is, like the TACTAAC box in S. cerevisiae, indispensable for efficient splicing. The conserved adenine residue of this sequence is used for branch formation and point mutations introduced into the CTPuAPy sequence abolish splicing and seem not to result in the recruitment of cryptic branch sites. We also show that an S. cerevisiae intron is correctly excised in S. pombe whereby the TACTAAC box is used in branch formation.","authors":"Mertins P, Gallwitz D","authors_abbrev":"Mertins P et al.","pubmed_publication_date":"Jun 1987","pubmed_entrez_date":"1987-06-01","publication_year":"1987","canto_session_key":"db4d78a89e7f4ae9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 18:07:47","canto_approved_date":"2019-01-31 18:07:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 18:07:40","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:15040784","title":"Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex.","citation":"Biochem J 2004 May 15;380(Pt 1):1-17","abstract":"The assembly of a branched network of actin filaments provides the mechanical propulsion that drives a range of dynamic cellular processes, including cell motility. The Arp2/3 complex is a crucial component of such filament networks. Arp2/3 nucleates new actin filaments while bound to existing filaments, thus creating a branched network. In recent years, a number of proteins that activate the filament nucleation activity of Arp2/3 have been identified, most notably the WASP (Wiskott-Aldrich syndrome protein) family. WASP-family proteins activate the Arp2/3 complex, and consequently stimulate actin assembly, in response to extracellular signals. Structural studies have provided a significant refinement in our understanding of the molecular detail of how the Arp2/3 complex nucleates actin filaments. There has also been much progress towards an understanding of the complicated signalling processes that regulate WASP-family proteins. In addition, the use of gene disruption in a number of organisms has led to new insights into the specific functions of individual WASP-family members. The present review will discuss the Arp2/3 complex and its regulators, in particular the WASP-family proteins. Emphasis will be placed on recent developments in the field that have furthered our understanding of actin dynamics and cell motility.","authors":"Millard TH, Sharp SJ, Machesky LM","authors_abbrev":"Millard TH et al.","pubmed_publication_date":"15 May 2004","pubmed_entrez_date":"2004-03-26","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30600398","title":"Linking the organization of DNA replication with genome maintenance.","citation":"Curr Genet 2019 Jun;65(3):677-683","abstract":"The spatial and temporal organization of genome duplication, also referred to as the replication program, is defined by the distribution and the activities of the sites of replication initiation across the genome. Alterations to the replication profile are associated with cell fate changes during development and in pathologies, but the importance of undergoing S phase with distinct and specific programs remains largely unexplored. We have recently addressed this question, focusing on the interplay between the replication program and genome maintenance. In particular, we demonstrated that when cells encounter challenges to DNA synthesis, the organization of DNA replication drives the response to replication stress that is mediated by the ATR/Rad3 checkpoint pathway, thus shaping the pattern of genome instability along the chromosomes. In this review, we present the major findings of our study and discuss how they may bring new perspectives to our understanding of the biological importance of the replication program.","doi":"10.1007/s00294-018-0923-8","authors":"Singh B, Wu PJ","authors_abbrev":"Singh B et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-01-03","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-01-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25916703","title":"Microscopy techniques to examine DNA replication in fission yeast.","citation":"Methods Mol Biol 2015;1300:13-41","abstract":"Temporal and spatial visualization of replication proteins and associated structures within the narrow confines of a yeast nucleus is technically challenging. Choosing the appropriate method depends upon the parameters of the experiment, the nature of the molecules to be observed, and the hypothesis to be tested. In this chapter, we review three broad types of visualization: whole-cell fluorescence or immunofluorescence, which is useful for questions of timing and chromatin association; nuclear spreads, which provide greater resolution within the chromatin for co-localization and region-specific effects; and chromatin fibers, which allow observation of labeled proteins and newly synthesized DNA on a linear chromosome. We also suggest a mounting procedure for live fission yeast with fluorescent proteins. We discuss applications of these protocols and some considerations for choosing methods and fluorophores.","doi":"10.1007/978-1-4939-2596-4_2","authors":"Green MD, Sabatinos SA, Forsburg SL","authors_abbrev":"Green MD et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-04-29","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-04-30 00:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF14616","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6B12.16","YBR076W"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23764396","title":"Construction of the first compendium of chemical-genetic profiles in the fission yeast Schizosaccharomyces pombe and comparative compendium approach.","citation":"Biochem Biophys Res Commun 2013 Jul 12;436(4):613-8","abstract":"Genome-wide chemical genetic profiles in Saccharomyces cerevisiae since the budding yeast deletion library construction have been successfully used to reveal unknown mode-of-actions of drugs. Here, we introduce comparative approach to infer drug target proteins more accurately using two compendiums of chemical-genetic profiles from the budding yeast S. cerevisiae and the fission yeast Schizosaccharomyces pombe. For the first time, we established DNA-chip based growth defect measurement of genome-wide deletion strains of S. pombe, and then applied 47 drugs to the pooled heterozygous deletion strains to generate chemical-genetic profiles in S. pombe. In our approach, putative drug targets were inferred from strains hypersensitive to given drugs by analyzing S. pombe and S. cerevisiae compendiums. Notably, many evidences in the literature revealed that the inferred target genes of fungicide and bactericide identified by such comparative approach are in fact the direct targets. Furthermore, by filtering out the genes with no essentiality, the multi-drug sensitivity genes, and the genes with less eukaryotic conservation, we created a set of drug target gene candidates that are expected to be directly affected by a given drug in human cells. Our study demonstrated that it is highly beneficial to construct the multiple compendiums of chemical genetic profiles using many different species. The fission yeast chemical-genetic compendium is available at http://pombe.kaist.ac.kr/compendium.","doi":"10.1016/j.bbrc.2013.05.138","authors":"Han S, Lee M, Chang H, Nam M, Park HO, Kwak YS, Ha HJ, Kim D, Hwang SO, Hoe KL, Kim DU","authors_abbrev":"Han S et al.","pubmed_publication_date":"12 Jul 2013","pubmed_entrez_date":"2013-06-15","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF06645","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC887.22"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:14517336","title":"PIG-W is critical for inositol acylation but not for flipping of glycosylphosphatidylinositol-anchor.","citation":"Mol Biol Cell 2003 Oct;14(10):4285-95","abstract":"Many cell surface proteins are anchored to a membrane via a glycosylphosphatidylinositol (GPI), which is attached to the C termini in the endoplasmic reticulum. The inositol ring of phosphatidylinositol is acylated during biosynthesis of GPI. In mammalian cells, the acyl chain is added to glucosaminyl phosphatidylinositol at the third step in the GPI biosynthetic pathway and then is usually removed soon after the attachment of GPIs to proteins. The mechanisms and roles of the inositol acylation and deacylation have not been well clarified. Herein, we report derivation of human and Chinese hamster mutant cells defective in inositol acylation and the gene responsible, PIG-W. The surface expressions of GPI-anchored proteins on these mutant cells were greatly diminished, indicating the critical role of inositol acylation. PIG-W encodes a 504-amino acid protein expressed in the endoplasmic reticulum. PIG-W is most likely inositol acyltransferase itself because the tagged PIG-W affinity purified from transfected human cells had inositol acyltransferase activity and because both mutant cells were complemented with PIG-W homologs of Saccharomyces cerevisiae and Schizosaccharomyces pombe. The inositol acylation is not essential for the subsequent mannosylation, indicating that glucosaminyl phosphatidylinositol can flip from the cytoplasmic side to the luminal side of the endoplasmic reticulum.","authors":"Murakami Y, Siripanyapinyo U, Hong Y, Kang JY, Ishihara S, Nakakuma H, Maeda Y, Kinoshita T","authors_abbrev":"Murakami Y et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2003-10-01","publication_year":"2003","canto_session_key":"c994b0ce5d1a85b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-01-08 01:55:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-01-08 01:55:49","canto_added_date":"2012-02-24 05:50:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC144.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-01-08"},{"uniquename":"PMID:32195666","title":"An H3K9 methylation-dependent protein interaction regulates the non-enzymatic functions of a putative histone demethylase.","citation":"Elife 2020 Mar 20;9","abstract":"H3K9 methylation (H3K9me) specifies the establishment and maintenance of transcriptionally silent epigenetic states or heterochromatin. The enzymatic erasure of histone modifications is widely assumed to be the primary mechanism that reverses epigenetic silencing. Here, we reveal an inversion of this paradigm where a putative histone demethylase Epe1 in fission yeast, has a non-enzymatic function that opposes heterochromatin assembly. Mutations within the putative catalytic JmjC domain of Epe1 disrupt its interaction with Swi6 HP1  suggesting that this domain might have other functions besides enzymatic activity. The C-terminus of Epe1 directly interacts with Swi6 HP1 , and H3K9 methylation stimulates this protein-protein interaction in vitro and in vivo. Expressing the Epe1 C-terminus is sufficient to disrupt heterochromatin by outcompeting the histone deacetylase, Clr3 from sites of heterochromatin formation. Our results underscore how histone modifying proteins that resemble enzymes have non-catalytic functions that regulate the assembly of epigenetic complexes in cells.","doi":"10.7554/eLife.53155","authors":"Raiymbek G, An S, Khurana N, Gopinath S, Larkin A, Biswas S, Trievel RC, Cho US, Ragunathan K","authors_abbrev":"Raiymbek G et al.","pubmed_publication_date":"20 Mar 2020","pubmed_entrez_date":"2020-03-21","publication_year":"2020","canto_session_key":"51ba394d387e7ecd","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-03-22 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41632793","title":"Harnessing Metalloprotease Wss1 to Enhance Methanol Utilization.","citation":"ACS Synth Biol 2026 Feb 03;","abstract":"The research on synthetic methylotrophic bacteria for one-carbon (C1) feedstock assimilation has garnered substantial interest and is regarded as the forefront of biomanufacturing advancements. Nevertheless, the effective utilization of C1 feedstocks faces challenges due to inadequate tolerance toward C1 compounds. This study elucidates that the buildup of formaldehyde causes severe DNA-protein cross-linking (DPC), and thus hampers growth and methanol assimilation in  Escherichia coli . To tackle this issue, we exploited a metalloproteinase, SpWss1, from  Schizosaccharomyces pombe . By fine-overexpressing SpWss1 in the  E. coli  genome, we were able to alleviate DPC damage and enhance formaldehyde tolerance. Remarkably, the engineered strain displayed a 10-fold increase in the amount of methanol assimilated (142 mM) compared to that of the control strain lacking SpWss1 (14 mM). Moreover, through iterative substrate feeding of methanol and xylose in shake-flask experiments, the genetically modified strain exhibited improved consumption levels, reaching up to 309 mM (∼10 g/L), making it one of the highest methanol-consuming strains among all  E. coli  strains without adaptive evolution. Additionally, the modified strain significantly enhanced the sustainable production of valuable products, such as triacetic acid lactone and fatty acids, from methanol. Overall, our findings underscore the significant scientific and biotechnological importance of addressing DPC to optimize C1 assimilation, providing valuable insights for sustainable chemistry, engineering, and industrial biotechnology applications.","doi":"10.1021/acssynbio.5c00684","authors":"Chen Y, Zhu C, Sun W, Gonzalez R, Tan Z","authors_abbrev":"Chen Y et al.","pubmed_publication_date":"03 Feb 2026","pubmed_entrez_date":"2026-02-03","publication_year":"2026","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2026-02-05 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39126481","title":"Identifying Chromosome Movement Patterns During Meiosis Using ChroMo.","citation":"Methods Mol Biol 2024;2818:271-288","abstract":"During meiosis, transient associations between the nuclear envelope and telomeres transmit nuclear movements to chromosomes, enabling their pairing and recombination. Recent advances in the field of quantitative cell biology allow a large volume of information about the kinetics of these chromosome movements to be extracted and analyzed with the aim of identifying biologically relevant movement patterns. To this end, we have developed ChroMo, a freely available application for the unsupervised study of chromosome movements in fission yeast meiosis. ChroMo contains a set of time series algorithms to identify chromosome movement motifs that are not easily observable by direct human visualization and to establish causal relationships between phenotypes. In this chapter, we present a detailed protocol for the processing of raw live imaging data from fission yeast and its subsequent analysis in ChroMo.","doi":"10.1007/978-1-0716-3906-1_18","authors":"Pinto-Cruz J, Correas M, Mendoza-Madrigal R, León-Periñán D, Fernández-Álvarez A","authors_abbrev":"Pinto-Cruz J et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-08-10","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-08-10 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26107389","title":"Effect of Ethanol, Sulfur Dioxide and Glucose on the Growth of Wine Spoilage Yeasts Using Response Surface Methodology.","citation":"PLoS One 2015;10(6):e0128702","abstract":"Response surface methodology (RSM) was used to study the effect of three factors, sulfur dioxide, ethanol and glucose, on the growth of wine spoilage yeast species, Zygosaccharomyces bailii, Schizosaccharomyces pombe, Saccharomycodes ludwigii and Saccharomyces cerevisiae. Seventeen central composite rotatable design (CCRD) trials were designed for each test yeast using realistic concentrations of the factors (variables) in premium red wine. Polynomial regression equations were fitted to experimental data points, and the growth inhibitory conditions of these three variables were determined. The overall results showed Sa. ludwigii as the most resistant species growing under high ethanol/free sulfur dioxide concentrations, i.e., 15% (v/v)/20 mg L-1, 14% (v/v)/32 mg L-1 and 12.5% (v/v)/40 mg L-1, whereas other yeasts did not survive under the same levels of ethanol/free sulfur dioxide concentrations. The inhibitory effect of ethanol was primarily observed during longer incubation periods, compared with sulfur dioxide, which showed an immediate effect. In some CCRD trials, Sa. ludwigii and S. cerevisiae showed growth recovery after a short death period under the exposure of 20-32 mg L-1 sulfur dioxide in the presence of 11% (v/v) or more ethanol. However, Sc. pombe and Z. bailii did not show such growth recovery under similar conditions. Up to 10 g L-1 of glucose did not prevent cell death under the sulfur dioxide or ethanol stress. This observation demonstrates that the sugar levels commonly used in wine to sweeten the mouthfeel do not increase wine susceptibility to spoilage yeasts, contrary to the anecdotal evidence.","doi":"10.1371/journal.pone.0128702","authors":"Chandra M, Oro I, Ferreira-Dias S, Malfeito-Ferreira M","authors_abbrev":"Chandra M et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-06-25","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-06-26 00:20:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41474550","title":"Contrasting mutation patterns in haploid and diploid cells from two yeast species.","citation":"Genetics 2025 Dec 31;","abstract":"There is significant variation in the rate and spectrum of spontaneous mutations among taxa. How this variation is shaped by natural selection remains a subject of debate. The drift barrier hypothesis proposes that selection generally favors lower mutation rates due to the risk of deleterious mutations but acts less effectively against weak mutator alleles in smaller populations, allowing the mutation rate to increase due to genetic drift. Given this model, we propose that mutation rates may also be elevated in cell types that appear rarely in a population, where DNA replication and repair processes are subject to selection less often. We can begin to test this prediction in yeast species, some of which can be grown in either a haploid or diploid cell state. Existing data on the budding yeast Saccharomyces cerevisiae support this prediction, with a higher mutation rate observed in haploids, which is the rare cell type in natural populations. However, this pattern could also appear if haploidy is inherently mutagenic, regardless of the dominant cell type. To test these alternatives, we conducted a mutation accumulation experiment with haploid and diploid cells of the fission yeast Schizosaccharomyces pombe, in which diploidy is the rare cell type. In this species, we found a higher mutation rate in diploids, consistent with our prediction. In both species, the spectrum of mutations is also influenced by ploidy state. Our findings suggest that limits to selection on mutation may be evident as variation within species.","doi":"10.1093/genetics/iyaf282","authors":"Bao K, Gupte R, Braker N, Sharp NP","authors_abbrev":"Bao K et al.","pubmed_publication_date":"31 Dec 2025","pubmed_entrez_date":"2025-12-31","publication_year":"2025","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2026-01-01 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20923774","title":"Tay1 protein, a novel telomere binding factor from Yarrowia lipolytica.","citation":"J Biol Chem 2010 Dec 03;285(49):38078-92","abstract":"Inspection of the complete genome of the yeast Yarrowia lipolytica for the presence of genes encoding homologues of known telomere-binding proteins surprisingly revealed no counterparts of typical yeast Myb domain-containing telomeric factors including Rap1 or Taz1. Instead, we identified a gene, YALIOD10923g, encoding a protein containing two Myb domains, exhibiting a high degree of similarity to the Myb domain of human telomeric proteins TRF1 and TRF2 and homologous to an essential fission yeast protein Mug152 whose expression is elevated during meiosis. The protein, which we named Tay1p (telomere-associated in Yarrowia lipolytica 1), was purified for biochemical studies. Using a model Y. lipolytica telomere, we demonstrate that the protein preferentially binds to Y. lipolytica telomeric tracts. Tay1p binds along the telomeric tract as dimers and larger oligomers, and it is able to remodel the telomeric DNA into both looped structures and synaptic complexes of two model telomere DNAs. The ability of Tay1p to induce dimerization of telomeres in vitro goes in line with its oligomeric nature, where each oligomer can employ several Myb domains to form intermolecular telomere clusters. We also provide experimental evidence that Tay1p may be associated with Y. lipolytica telomeres in vivo. Together with its homologues from Schizosaccharomyces pombe and several basidiomycetous fungi (Sánchez-Alonso, P., and Guzman, P. (2008) Fungal Genet. Biol. 45, S54-S62), Tay1p constitutes a novel family of putative telomeric factors whose analysis may be instrumental in understanding the function and evolution of double-stranded DNA telomeric proteins.","doi":"10.1074/jbc.M110.127605","authors":"Kramara J, Willcox S, Gunisova S, Kinsky S, Nosek J, Griffith JD, Tomaska L","authors_abbrev":"Kramara J et al.","pubmed_publication_date":"03 Dec 2010","pubmed_entrez_date":"2010-10-07","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13G7.10","HGNC:11728","HGNC:11729"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15358115","title":"Differential expression and role of two dithiol glutaredoxins Grx1 and Grx2 in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2004 Sep 03;321(4):922-9","abstract":"Glutaredoxins are glutathione-specific thiol oxidoreductases. The regulation and the role of grx1(+) and grx2(+) genes encoding dithiol glutaredoxins were analyzed in Schizosaccharomyces pombe. When tested in the same genetic background including mating type, the grx1 null mutant became sensitive to hydrogen peroxide, whereas grx2 mutant became highly sensitive to paraquat, a superoxide generator. The grx1grx2 double mutant showed additive phenotype of each single mutant. The grx1(+) gene expression was induced by various stresses such as oxidants, salts, and heat, and increased in the stationary phase, whereas grx2(+) stayed constitutive. The induction was mediated via Spc1 MAP kinase path involving both Atf1 and Pap1 transcription factors. Sub-cellular fractionation as well as fluorescence microscopy revealed that Grx1 resides mainly in the cytosol, whereas Grx2 is in mitochondria. These results suggest distinct roles for Grx1 and Grx2 in S. pombe in mediating glutathione-dependent redox homeostasis.","authors":"Chung WH, Kim KD, Cho YJ, Roe JH","authors_abbrev":"Chung WH et al.","pubmed_publication_date":"03 Sep 2004","pubmed_entrez_date":"2004-09-11","publication_year":"2004","canto_session_key":"1c9816734b6da685","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-04 10:30:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 14:51:24","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15E1.09","SPAC1783.07c","SPAC4F10.20","SPBC29B5.01","SPAC24B11.06c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-11-05"},{"uniquename":"PMID:12111733","title":"Checking in on Cds1 (Chk2): A checkpoint kinase and tumor suppressor.","citation":"Bioessays 2002 Jun;24(6):502-11","abstract":"Together, DNA repair and checkpoint responses ensure the integrity of the genome. Coordination of cell cycle checkpoints and DNA repair are especially important following genotoxic radiation or chemotherapy, during which unusually high loads of DNA damage are sustained. In mammalian cells, the checkpoint kinase, Cds1 (also known as Chk2) is activated by ATM in response to DNA damage. The role of Cds1 as a checkpoint kinase depends on its ability to phosphorylate cell cycle regulators such p53, Cdc25 and Brca1. A role for Cds1 in repair is suggested by the finding that it interacts with the Holliday junction resolving activity Mus81. This review focuses on the many questions generated by recent progress in understanding the function and regulation of human Cds1.","authors":"McGowan CH","authors_abbrev":"McGowan CH","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-07-12","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:58:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10816254","title":"Cytokinesis in fission yeast: a myosin pas de deux.","citation":"Microsc Res Tech 2000 Apr 15;49(2):152-60","abstract":"Cytokinesis in the fission yeast, Schizosaccharomyces pombe consists of two distinct but overlapping events: the assembly and constriction of a cytokinetic actomyosin ring (CAR) and the formation of a cross wall or septum. These two processes must be spatially and temporally coordinated both with each other and with other cell cycle events, most notably spindle formation and anaphase chromosome segregation. In fission yeast, the CAR contains two unusual type II myosins, Myo2, encoded by the gene myo2(+), and Myp2, encoded by myp2(+). The relationship of these two proteins to each other and their relative contribution to CAR assembly and contraction is largely unknown. Here we review what is known about the role of each myosin in cytokinesis and present some new information concerning their regulation and possible physical interaction.","authors":"Mulvihill DP, Win TZ, Pack TP, Hyams JS","authors_abbrev":"Mulvihill DP et al.","pubmed_publication_date":"15 Apr 2000","pubmed_entrez_date":"2000-05-18","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28396503","title":"Correlation of Meiotic DSB Formation and Transcription Initiation Around Fission Yeast Recombination Hotspots.","citation":"Genetics 2017 Jun;206(2):801-809","abstract":"Meiotic homologous recombination, a critical event for ensuring faithful chromosome segregation and creating genetic diversity, is initiated by programmed DNA double-strand breaks (DSBs) formed at recombination hotspots. Meiotic DSB formation is likely to be influenced by other DNA-templated processes including transcription, but how DSB formation and transcription interact with each other has not been understood well. In this study, we used fission yeast to investigate a possible interplay of these two events. A group of hotspots in fission yeast are associated with sequences similar to the cyclic AMP response element and activated by the ATF/CREB family transcription factor dimer Atf1-Pcr1. We first focused on one of those hotspots,  ade6-3049 , and Atf1. Our results showed that multiple transcripts, shorter than the  ade6  full-length messenger RNA, emanate from a region surrounding the  ade6-3049  hotspot. Interestingly, we found that the previously known recombination-activation region of Atf1 is also a transactivation domain, whose deletion affected DSB formation and short transcript production at  ade6-3049  These results point to a possibility that the two events may be related to each other at  ade6-3049  In fact, comparison of published maps of meiotic transcripts and hotspots suggested that hotspots are very often located close to meiotically transcribed regions. These observations therefore propose that meiotic DSB formation in fission yeast may be connected to transcription of surrounding regions.","doi":"10.1534/genetics.116.197954","authors":"Yamada S, Okamura M, Oda A, Murakami H, Ohta K, Yamada T","authors_abbrev":"Yamada S et al.","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2017-04-12","publication_year":"2017","canto_session_key":"0251353dac864b0d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-04-13 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007975","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF049529","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33579693","title":"Monitoring  Schizosaccharomyces pombe  genome stress by visualizing end-binding protein Ku.","citation":"Biol Open 2021 Feb 15;10(2)","abstract":"Studies of genome stability have exploited visualization of fluorescently tagged proteins in live cells to characterize DNA damage, checkpoint, and repair responses. In this report, we describe a new tool for fission yeast, a tagged version of the end-binding protein Pku70 which is part of the KU protein complex. We compare Pku70 localization to other markers upon treatment to various genotoxins, and identify a unique pattern of distribution. Pku70 provides a new tool to define and characterize DNA lesions and the repair response.","doi":"10.1242/bio.054346","authors":"Jones CE, Forsburg SL","authors_abbrev":"Jones CE et al.","pubmed_publication_date":"15 Feb 2021","pubmed_entrez_date":"2021-02-13","publication_year":"2021","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-02-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20485745","title":"Toward one step analysis of cellular lipidomes using liquid chromatography coupled with mass spectrometry: application to Saccharomyces cerevisiae and Schizosaccharomyces pombe lipidomics.","citation":"Mol Biosyst 2010 Jun;6(6):1008-17","abstract":"Recent rapid growth of lipidomics is mainly attributed to technological advances in mass spectrometry. Development of soft ionization techniques, in combination with computational tools, has spurred subsequent development of various methods for lipid analysis. However, none of these existing approaches can cover major cellular lipids in a single run. Here we demonstrate that a single method of liquid chromatography coupled with mass spectrometry (LCMS) can be used for simultaneous profiling of major cellular lipids including glycerophospholipids (PLs), sphingolipids (SPLs), waxes, sterols (ST) and mono-, di- as well as triacylglycerides (MAG, DAG, TAG). We applied this approach to analyze these lipids in various organisms including Saccharomyces cerevisiae and Schizosaccharomyces pombe. While phospholipids and triacylglycerides of S. pombe mainly contain 18 : 1 fatty acyls, those of S. cerevisiae contain 16 : 1, 16 : 0 and 18 : 1 fatty acyls. S. cerevisiae and S. pombe contain distinct sphingolipid profiles. S. cerevisiae has abundant inositol phytoceramides (IPC), while S. pombe contains high levels of free phytoceramides as well as short chain phytoceramides (t18:1/20 : 0-B) and IPC (t18:1/20 : 0-B). In S. cerevisiae, our results demonstrated accumulation of ergosterol esters in tgl1Delta cells and accumulation of various TAG species in tgl3Delta cells, which are consistent with the function of the respective enzymes. Furthermore, we, for the first time, systematically characterized lipids in S. pombe and measured their dynamic changes in Deltaplh1Deltadga1 cells at different growth phases. We further discussed dynamic changes of phospholipids, sphingolipids and neutral lipids in the progress of programmed cell death in Deltaplh1Deltadga1 cells of S. pombe.","doi":"10.1039/b913353d","authors":"Shui G, Guan XL, Low CP, Chua GH, Goh JS, Yang H, Wenk MR","authors_abbrev":"Shui G et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-05-21","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9441849","title":"Identification of autonomously replicating sequence (ARS) elements in eukaryotic cells.","citation":"Methods 1997 Nov;13(3):221-33","abstract":"Autonomously replicating sequence (ARS) elements were first identified in the budding yeast Saccharomyces cerevisiae as chromosomal DNA fragments that promoted high frequency of transformation and extrachromosomal maintenance of plasmid DNA. These specific sequence elements were subsequently shown to function as origins of DNA replication. Detailed analysis of the structure and function of ARS elements has been limited largely to S. cerevisiae and more recently the fission yeast Schizosaccharomyces pombe. Characterization of ARS activity in other eukaryotes is far less complete. Here we describe the ARS assay developed in yeast and its application to the study of origin function in other eukaryotes. Other available methods for detecting autonomous replication in these systems are also presented.","authors":"Clyne RK, Kelly TJ","authors_abbrev":"Clyne RK et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-01-27","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16407840","title":"A functional analysis of PCNA-binding peptides derived from protein sequence, interaction screening and rational design.","citation":"Oncogene 2006 May 11;25(20):2850-9","abstract":"Proliferating cell nuclear antigen (PCNA) has no intrinsic enzymatic function, but functions as a sliding platform to mediate protein interactions with the DNA strand. Many proteins interact with PCNA through a small conserved motif with consensus QxxLxxFF. This work uses Schizosaccharomyces pombe and human cells to analyse the function of PCNA-binding peptides. Interacting peptides were identified using two-hybrid screening; one (pep102) binds directly to a physiologically relevant site on PCNA. The EGFP-pep102 overexpression phenotype is consistent with competitive blocking of PCNA-protein interactions. Various PCNA-binding peptides were all shown to inhibit PCNA function by competitive binding in both human and S. pombe cells as EGFP fusion proteins. The action of a p21(WAF1/Cip1)-derived peptide was complicated by the presence of additional functional domains and possible post-translational modification. The activity of pep102 was hampered by low expression in both model systems. The peptide derived from rational design (con1) was stable, highly active in inhibiting PCNA function both S. pombe and human cells and showed a high affinity for PCNA both in vitro and in vivo. These results validate the use of functional screening in yeast to identify peptide aptamers that are functional in mammalian cells; such aptamers provide excellent leads for small molecule antiproliferative therapies.","authors":"Warbrick E","authors_abbrev":"Warbrick E","pubmed_publication_date":"11 May 2006","pubmed_entrez_date":"2006-01-13","publication_year":"2006","canto_session_key":"6b4c4ebf89b9fe98","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-04-19 08:34:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-29 12:25:37","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.09"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2016-03-29"},{"uniquename":"PMID:40966507","title":"CRISPR-Cas9 targeting of G-Quadruplex DNA in ADH1 promoter highlights its role in transcriptome and metabolome regulation.","citation":"Nucleic Acids Res 2025 Sep 05;53(17)","abstract":"G-quadruplex (G4) structures are critical regulators of gene expression, yet the role of an individual G4 within its native chromatin remains underexplored, especially outside human systems. Here, we used CRISPR-Cas9 to introduce guanine-to-thymine mutations at a G4-forming motif within the adh1+ promoter in yeast Schizosaccharomyces pombe, creating two mutant strains: one with G4-only mutations and another with both G4 and TATA-box mutations. Chromatin immunoprecipitation using BG4 antibody confirmed reduced G4 enrichment in both mutants, validating G4 structure formation in the wild-type chromatin. Detailed characterizations demonstrated that the G4 mutations alter its dynamics without fully preventing its formation. These mutations significantly reduce adh1 transcript levels, with G4 TATA-box mutant causing the strongest transcriptional suppression. This indicates a positive regulatory role for the G4 structure in transcription. Furthermore, both mutants displayed altered transcriptomic profiles, particularly impacting the oxidoreductase pathway. Metabolomic analyses by mass spectrometry further highlighted substantial disruptions in NAD+/NADH metabolism, a key energy reservoir for metabolic regulation. These results highlight that tuning G4 dynamics, without abolishing the structure, can still profoundly affect gene expression and metabolism, unlike prior studies on the human MYC promoter that disrupted G4 formation. This represents the first such finding in yeast.","doi":"10.1093/nar/gkaf853","authors":"Obi I, Sengupta P, Sabouri N","authors_abbrev":"Obi I et al.","pubmed_publication_date":"05 Sep 2025","pubmed_entrez_date":"2025-09-18","publication_year":"2025","canto_session_key":"94fa8e0357057a3f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-18 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC12101","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9560390","title":"Sum1, a highly conserved WD-repeat protein, suppresses S-M checkpoint mutants and inhibits the osmotic stress cell cycle response in fission yeast.","citation":"Genetics 1998 Apr;148(4):1731-42","abstract":"The S-M checkpoint ensures that entry into mitosis is dependent on completion of DNA replication. In the fission yeast Schizosaccharomyces pombe, the SM checkpoint mutant cdc2-3w is thought to be defective in receiving the checkpoint signal. To isolate genes that function in the checkpoint pathway, we screened an S. pombe cDNA library for genes that, when overexpressed, could suppress the checkpoint defect of cdc2-3w. Using this approach, we have identified a novel gene, sum1+ (suppressor of uncontrolled mitosis). sum1+ encodes a highly conserved WD-transducin repeat protein with striking sequence similarity to the human transforming growth factor (TGF)-beta-receptor interacting protein TRIP-1 and to the translation initiation factor 3 subunit eIF3-p39, encoded by the TIF34 gene in Saccharomyces cerevisiae. S. pombe sum1+ is an essential gene, required for normal cell growth and division. In addition to restoring checkpoint control, overexpression of sum1+ inhibits the normal cell cycle response to osmotic stress. Furthermore, we demonstrate that inactivation of the stress-activated MAP kinase pathway, required for cell cycle stress response, restores the S-M checkpoint in cdc2-3w cells. These results suggest that Suml interacts with the stress-activated MAP kinase pathway and raise the possibility that environmental conditions may influence the checkpoint response in fission yeast.","authors":"Humphrey T, Enoch T","authors_abbrev":"Humphrey T et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-04-30","publication_year":"1998","canto_session_key":"9e9172c11d4beefc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-17 11:21:15","canto_approved_date":"2021-01-06 17:34:15","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-04 09:03:13","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC215.05","SPAC24B11.06c","SPAC26F1.10c","SPAC4D7.05"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-03-17"},{"uniquename":"PMID:3076289","title":"Cell cycle control genes in fission yeast and mammalian cells.","citation":"Trends Genet 1988 Oct;4(10):287-90","abstract":"","authors":"Lee M, Nurse P","authors_abbrev":"Lee M et al.","pubmed_publication_date":"Oct 1988","pubmed_entrez_date":"1988-10-01","publication_year":"1988","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21089507","title":"[Homologous chromosome pairing: another climax of meiosis].","citation":"Tanpakushitsu Kakusan Koso 2009 Mar;54(4 Suppl):547-51","abstract":"","authors":"Yamamoto A","authors_abbrev":"Yamamoto A","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2010-11-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2005825","title":"Molecular genetic analysis of fission yeast Schizosaccharomyces pombe.","citation":"Methods Enzymol 1991;194:795-823","abstract":"","authors":"Moreno S, Klar A, Nurse P","authors_abbrev":"Moreno S et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25002536","title":"A novel histone deacetylase complex in the control of transcription and genome stability.","citation":"Mol Cell Biol 2014 Sep 15;34(18):3500-14","abstract":"The acetylation state of histones, controlled by histone acetyltransferases (HATs) and deacetylases (HDACs), profoundly affects DNA transcription and repair by modulating chromatin accessibility to the cellular machinery. The Schizosaccharomyces pombe HDAC Clr6 (human HDAC1) binds to different sets of proteins that define functionally distinct complexes: I, I', and II. Here, we determine the composition, architecture, and functions of a new Clr6 HDAC complex, I'', delineated by the novel proteins Nts1, Mug165, and Png3. Deletion of nts1 causes increased sensitivity to genotoxins and deregulated expression of Tf2 elements, long noncoding RNA, and subtelomeric and stress-related genes. Similar, but more pervasive, phenotypes are observed upon Clr6 inactivation, supporting the designation of complex I'' as a mediator of a key subset of Clr6 functions. We also reveal that with the exception of Tf2 elements, the genome-wide loading sites and loci regulated by Clr6 I″ do not correlate. Instead, Nts1 loads at genes that are expressed in midmeiosis, following oxidative stress, or are periodically expressed. Collective data suggest that Clr6 I'' has (i) indirect effects on gene expression, conceivably by mediating higher-order chromatin organization of subtelomeres and Tf2 elements, and (ii) direct effects on the transcription of specific genes in response to certain cellular or environmental stimuli.","doi":"10.1128/MCB.00519-14","authors":"Zilio N, Codlin S, Vashisht AA, Bitton DA, Head SR, Wohlschlegel JA, Bähler J, Boddy MN","authors_abbrev":"Zilio N et al.","pubmed_publication_date":"15 Sep 2014","pubmed_entrez_date":"2014-07-09","publication_year":"2014","canto_session_key":"9c097ba571c89868","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nicola Zilio","canto_first_approved_date":"2015-06-09 08:31:27","canto_approved_date":"2024-04-04 17:39:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-21 09:59:49","canto_added_date":"2014-07-10 00:15:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Nicola Zilio","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.02","SPAC23G3.10c","SPBC12C2.10c","SPBC428.08c","SPBC16D10.01c","SPAC5D6.02c","SPCC1259.07","SPBC8D2.03c","SPBC83.08","SPCC1259.14c","SPAC1F7.05","SPCC645.04","SPBC23G7.12c","SPAC1F3.07c","SPCC5E4.06","SPBC28F2.11","SPCC24B10.19c","SPAC3A11.12c","SPBPB21E7.07","SPBC660.11","SPAC14C4.12c","SPBC651.10","SPAC8E11.02c","SPAC23G3.06","SPAC1565.08","SPBC16A3.15c","SPAC19G12.06c","SPBC3D6.02","SPCC14G10.03c","SPAC11E3.08c","SPBC1734.16c","SPBC1105.12","SPBC215.06c","SPBC1734.15","SPCC622.08c","SPCC550.05","SPAC31G5.13","SPAC6B12.15","SPBC20F10.04c","SPBC428.06c","SPBC16A3.08c","SPBC1D7.04","SPBC800.05c","SPBC106.13","SPAC1834.03c","SPBC16G5.15c","SPBC646.10c","SPCC622.09","SPAPB8E5.09","SPAC29A4.18","SPCC1682.13","SPCC576.10c","SPAC16A10.06c","SPAC17A2.13c","SPBC36.05c","SPCC1682.16","SPBC1709.11c","SPBC26H8.07c","SPAC16E8.12c","SPAC23H4.12"],"gene_count":60,"ltp_gene_count":59,"approved_date":"2015-06-09"},{"uniquename":"EMBL:AU007025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36562208","title":"A nuclear pore complex-associated regulation of SUMOylation in meiosis.","citation":"Genes Cells 2023 Mar;28(3):188-201","abstract":"The nuclear pore complex (NPC) provides a permeable barrier between the nucleoplasm and cytoplasm. In a subset of NPC constituents that regulate meiosis in the fission yeast Schizosaccharomyces pombe, we found that nucleoporin Nup132 (homolog of human Nup133) deficiency resulted in transient leakage of nuclear proteins during meiosis I, as observed in the nup132 gene-deleted mutant. The nuclear protein leakage accompanied the liberation of the small ubiquitin-like modifier (SUMO)-specific ubiquitin-like protease 1 (Ulp1) from the NPC. Ulp1 retention at the nuclear pore prevented nuclear protein leakage and restored normal meiosis in a mutant lacking Nup132. Furthermore, using mass spectrometry analysis, we identified DNA topoisomerase 2 (Top2) and RCC1-related protein (Pim1) as the target proteins for SUMOylation. SUMOylation levels of Top2 and Pim1 were altered in meiotic cells lacking Nup132. HyperSUMOylated Top2 increased the binding affinity at the centromeres of nup132 gene-deleted meiotic cells. The Top2-12KR sumoylation mutant was less localized to the centromeric regions. Our results suggest that SUMOylation of chromatin-binding proteins is regulated by the NPC-bound SUMO-specific protease and is important for the progression of meiosis.","doi":"10.1111/gtc.13003","authors":"Yang HJ, Asakawa H, Li FA, Haraguchi T, Shih HM, Hiraoka Y","authors_abbrev":"Yang HJ et al.","pubmed_publication_date":"Mar 2023","pubmed_entrez_date":"2022-12-23","publication_year":"2023","canto_session_key":"3e2392a0b8221682","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-12-24 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19G7.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34499173","title":"Visual detection of binary, ternary and quaternary protein interactions in fission yeast using a Pil1 co-tethering assay.","citation":"J Cell Sci 2021 Oct 01;134(19)","abstract":"Protein-protein interactions are vital for executing nearly all cellular processes. To facilitate the detection of protein-protein interactions in living cells of the fission yeast Schizosaccharomyces pombe, here we present an efficient and convenient method termed the Pil1 co-tethering assay. In its basic form, we tether a bait protein to mCherry-tagged Pil1, which forms cortical filamentary structures, and examine whether a GFP-tagged prey protein colocalizes with the bait. We demonstrate that this assay is capable of detecting pairwise protein-protein interactions of cytosolic proteins and nuclear proteins. Furthermore, we show that this assay can be used for detecting not only binary protein-protein interactions, but also ternary and quaternary protein-protein interactions. Using this assay, we systematically characterized the protein-protein interactions in the Atg1 complex and in the phosphatidylinositol 3-kinase (PtdIns3K) complexes and found that Atg38 is incorporated into the PtdIns3K complex I via an Atg38-Vps34 interaction. Our data show that this assay is a useful and versatile tool and should be added to the routine toolbox of fission yeast researchers. This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.258774","authors":"Yu ZQ, Liu XM, Zhao D, Xu DD, Du LL","authors_abbrev":"Yu ZQ et al.","pubmed_publication_date":"01 Oct 2021","pubmed_entrez_date":"2021-09-09","publication_year":"2021","canto_session_key":"3467ae430678df74","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li-Lin Du","canto_first_approved_date":"2021-10-25 15:47:17","canto_approved_date":"2021-11-01 17:08:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-10-21 08:53:33","canto_added_date":"2021-09-11 00:15:03","annotation_curators":[{"name":"Li-Lin Du","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":"interaction","file_name":"PMID_34499173_interactions.tab2.txt"}],"genes":["SPAC7D4.04","SPAC458.05","SPAC4F10.07c","SPAC20G8.10c","SPBC119.07","SPBC18H10.19","SPAC6G9.16c","SPCC63.08c","SPBC660.08","SPBP8B7.24c","SPCC1183.05c","SPAC10F6.11c","SPAC25A8.02","SPAC25H1.03","SPAC30D11.06c"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2021-10-25"},{"uniquename":"PMID:21406552","title":"RNAi genes pave their own way.","citation":"Genes Dev 2011 Mar 15;25(6):529-33","abstract":"Heterochromatin formation in fission yeast and the role of RNAi in this process have been intensively studied. So far, however, nothing is known about the regulation of expression of RNAi components during these events. Gullerova and colleagues (pp. 556-568) reveal an autoregulatory loop that regulates the expression of RNAi genes and centromeric heterochromatin formation during the cell cycle. Gene orientation plays a surprising role in this process.","doi":"10.1101/gad.2038611","authors":"Kamminga LM, Ketting RF","authors_abbrev":"Kamminga LM et al.","pubmed_publication_date":"15 Mar 2011","pubmed_entrez_date":"2011-03-17","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24972934","title":"Cross talk between NDR kinase pathways coordinates cytokinesis with cell separation in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2014 Aug;13(8):1104-12","abstract":"NDR (nuclear Dbf-2-related) kinases constitute key regulatory nodes in signaling networks that control multiple biological processes such as growth, proliferation, mitotic exit, morphogenesis, and apoptosis. Two NDR pathways called the septation initiation network (SIN) and the morphogenesis Orb6 network (MOR) exist in the fission yeast Schizosaccharomyces pombe. The SIN promotes cytokinesis, and the MOR drives cell separation at the end of cytokinesis and polarized growth during interphase. We showed previously that cross talk exists between these two pathways, with the SIN inhibiting the MOR during cytokinesis through phosphorylation of the MOR component Nak1 by the SIN Sid2 kinase. The reason for this inhibition remained uncertain. We show here that failure to inhibit MOR signaling during cytokinesis results in cell lysis at the site of septum formation. Time-lapse analysis revealed that MOR signaling during cytokinesis causes cells to prematurely initiate septum degradation/cell separation. The cell lysis phenotype is due to premature initiation of cell separation because it can be rescued by mutations in genes required for cell separation/septum degradation. We also shed further light on how the SIN inhibits the MOR. Sid2 phosphorylation of the MOR proteins Sog2 and Nak1 is required to prevent cell lysis during cytokinesis. Together, these results show that SIN inhibition of the MOR enforces proper temporal ordering of cytokinetic events.","doi":"10.1128/EC.00129-14","authors":"Gupta S, Govindaraghavan M, McCollum D","authors_abbrev":"Gupta S et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-06-29","publication_year":"2014","canto_session_key":"7999293403fb7249","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-04-22 11:01:54","canto_approved_date":"2025-04-22 11:01:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-22 11:01:17","canto_added_date":"2014-06-30 00:15:31","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":14,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17F3.02","SPBC887.09c","SPAPYUG7.03c","SPAC14C4.09","SPAC24B11.11c","SPBP19A11.04c","SPAC821.12","SPAC6G10.12c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2025-04-22"},{"uniquename":"PMID:3796591","title":"Site-specific mutagenesis of cdc2+, a cell cycle control gene of the fission yeast Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1986 Oct;6(10):3523-30","abstract":"The cdc2+ gene of Schizosaccharomyces pombe is homologous to the CDC28 gene of Saccharomyces cerevisiae. Both genes share limited homology with vertebrate protein kinases and have protein kinase activity. cdc2+ has been subjected to mutagenesis in vitro. A null allele of the gene, constructed by insertion of the S. cerevisiae LEU2 gene into a site within the gene, has a phenotype similar to that of many temperature-sensitive alleles of cdc2. Mutations within the predicted ATP-binding site and in a region which may be a site of phosphorylation result in loss of cdc2+ activity. A single substitution of Gly-146 to Asp-146 has been identified in cdc2-1w, a dominant activated allele of the gene. The four introns within the cdc2+ gene have been deleted. The resulting gene not only functions in fission yeast but also rescues cdc28(Ts) strains of S. cerevisiae, a property which is not shared by the genomic cdc2+ gene.","authors":"Booher R, Beach D","authors_abbrev":"Booher R et al.","pubmed_publication_date":"Oct 1986","pubmed_entrez_date":"1986-10-01","publication_year":"1986","canto_session_key":"fe602c464ab8a83c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-12 17:29:46","canto_approved_date":"2019-05-03 17:33:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-05-30 10:30:27","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-12-12"},{"uniquename":"EMBL:AB084837","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.25"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28733401","title":"Mating, Spore Dissection, and Selection of Diploid Cells in  Schizosaccharomyces japonicus .","citation":"Cold Spring Harb Protoc 2017 Dec 01;2017(12):pdb.prot091843","abstract":"Haploid yeast cells mate to form heterozygotes and subsequently undergo meiosis to form spores. This process can be used to produce gene combinations and variants that are useful for genetic analysis. For example, these spores can be used to generate double mutants or to measure genetic distances in a mutational analysis. Here, we describe mating and spore dissection procedures for  Schizosaccharomyces japonicus  cells. Although the overall procedures resemble those used in  Schizosaccharomyces pombe , some differences exist, including the use of EMM2 medium without nitrogen (EMM-N) for mating and the shorter incubation time of 16-20 h for  S. japonicus  cells. Furthermore, the  S. japonicus  zygotes produce eight spores and thus require an \"octad\" analysis.","doi":"10.1101/pdb.prot091843","authors":"Furuya K, Niki H","authors_abbrev":"Furuya K et al.","pubmed_publication_date":"01 Dec 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16233563","title":"Oxidative stress induction as a cause of Ba2+-dependent fungicidal action of UMP-derivative on the yeast Shizosaccharomyces pombe.","citation":"J Biosci Bioeng 2003;96(5):500-2","abstract":"A UMP-derivative, uridine 5'-hexadecylphosphate (UMPC16), exhibited a fungicidal action against various yeast strains including the fission yeast Schizosaccharomyces pombe in combination with Ba2+ ion. UMPC16 accelerated reactive oxygen species (ROS) generation in medium with Ba2+ ion in a dose- and time-dependent manner. Additional supplementation of Ca2+ ion into medium could suppress such a combined fungicidal action due to oxidative stress induction.","authors":"Tanaka T, Usuki Y","authors_abbrev":"Tanaka T et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2005-10-20","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB054299","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25633902","title":"Characterization and review of MTHFD1 deficiency: four new patients, cellular delineation and response to folic and folinic acid treatment.","citation":"J Inherit Metab Dis 2015 Sep;38(5):863-72","abstract":"In the folate cycle MTHFD1, encoded by MTHFD1, is a trifunctional enzyme containing 5,10-methylenetetrahydrofolate dehydrogenase, 5,10-methenyltetrahydrofolate cyclohydrolase and 10-formyltetrahydrofolate synthetase activity. To date, only one patient with MTHFD1 deficiency, presenting with hyperhomocysteinemia, megaloblastic anaemia, hemolytic uremic syndrome (HUS) and severe combined immunodeficiency, has been identified (Watkins et al J Med Genet 48:590-2, 2011). We now describe four additional patients from two different families. The second patient presented with hyperhomocysteinemia, megaloblastic anaemia, HUS, microangiopathy and retinopathy; all except the retinopathy resolved after treatment with hydroxocobalamin, betaine and folinic acid. The third patient developed megaloblastic anaemia, infection, autoimmune disease and moderate liver fibrosis but not hyperhomocysteinemia, and was successfully treated with a regime that included and was eventually reduced to folic acid. The other two, elder siblings of the third patient, died at 9 weeks of age with megaloblastic anaemia, infection and severe acidosis and had MTFHD1 deficiency diagnosed retrospectively. We identified a missense mutation (c.806C > T, p.Thr296Ile) and a splice site mutation (c.1674G > A) leading to exon skipping in the second patient, while the other three harboured a missense mutation (c.146C > T, p.Ser49Phe) and a premature stop mutation (c.673G > T, p.Glu225*), all of which were novel. Patient fibroblast studies revealed severely reduced methionine formation from [(14)C]-formate, which did not increase in cobalamin supplemented culture medium but was responsive to folic and folinic acid. These additional cases increase the clinical spectrum of this intriguing defect, provide in vitro evidence of disturbed methionine synthesis and substantiate the effectiveness of folic or folinic acid treatment.","doi":"10.1007/s10545-015-9810-3","authors":"Burda P, Kuster A, Hjalmarson O, Suormala T, Bürer C, Lutz S, Roussey G, Christa L, Asin-Cayuela J, Kollberg G, Andersson BA, Watkins D, Rosenblatt DS, Fowler B, Holme E, Froese DS, Baumgartner MR","authors_abbrev":"Burda P et al.","pubmed_publication_date":"Sep 2015","pubmed_entrez_date":"2015-01-31","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2G2.08","SPBC839.16"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:14333971","title":"METABOLISM OF D,1-MALIC ACID BY SCHIZOSACCHAROMYCES POMBE AND SCHIZOSACCHAROMYCES ACIDODEVORATUS.","citation":"Acta Microbiol Pol (1952) 1965;14:63-71","abstract":"","authors":"JAKUBOWSKA J, PIATKIEWICZ A","authors_abbrev":"JAKUBOWSKA J et al.","pubmed_publication_date":"1965","pubmed_entrez_date":"1965-01-01","publication_year":"1965","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1317550","title":"The swi4+ gene of Schizosaccharomyces pombe encodes a homologue of mismatch repair enzymes.","citation":"Nucleic Acids Res 1992 May 11;20(9):2271-8","abstract":"The swi4+ gene of Schizosaccharomyces pombe is involved in termination of copy-synthesis during mating-type switching. The gene was cloned by functional complementation of a swi4 mutant transformed with a genomic library. Determination of the nucleotide sequence revealed an open reading frame of 2979 nucleotides which is interrupted by a 68 bp long intron. The putative Swi4 protein shows homology to Duc-1 (human), Rep-3 (mouse), HexA (Streptococcus pneumoniae) and MutS (Salmonella typhimurium). The prokaryotic proteins are known as essential components involved in mismatch repair. A strain with a disrupted swi4+ gene was constructed and analysed with respect to the switching process. As in swi4 mutants duplications occur in the mating-type region of the swi4 (null) strain, reducing the efficiency of switching.","authors":"Fleck O, Michael H, Heim L","authors_abbrev":"Fleck O et al.","pubmed_publication_date":"11 May 1992","pubmed_entrez_date":"1992-05-11","publication_year":"1992","canto_session_key":"722b74f950617459","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-12-13 18:05:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-13 15:07:08","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8F11.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-13"},{"uniquename":"PMID:28206949","title":"Micromanaging checkpoint proteins.","citation":"Elife 2017 Feb 16;6","abstract":"The kinase Mps1, long known to be the 'boss' in mitotic checkpoint signaling, phosphorylates multiple proteins in the checkpoint signaling cascade.","doi":"10.7554/eLife.25001","authors":"Ciliberto A, Hauf S","authors_abbrev":"Ciliberto A et al.","pubmed_publication_date":"16 Feb 2017","pubmed_entrez_date":"2017-02-17","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-02-18 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF01764","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:28923","SPAC23C4.16c","HGNC:1165"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33804687","title":"Shake It Off: The Elimination of Erroneous Kinetochore-Microtubule Attachments and Chromosome Oscillation.","citation":"Int J Mol Sci 2021 Mar 20;22(6)","abstract":"Cell proliferation and sexual reproduction require the faithful segregation of chromosomes. Chromosome segregation is driven by the interaction of chromosomes with the spindle, and the attachment of chromosomes to the proper spindle poles is essential. Initial attachments are frequently erroneous due to the random nature of the attachment process; however, erroneous attachments are selectively eliminated. Proper attachment generates greater tension at the kinetochore than erroneous attachments, and it is thought that attachment selection is dependent on this tension. However, studies of meiotic chromosome segregation suggest that attachment elimination cannot be solely attributed to tension, and the precise mechanism of selective elimination of erroneous attachments remains unclear. During attachment elimination, chromosomes oscillate between the spindle poles. A recent study on meiotic chromosome segregation in fission yeast has suggested that attachment elimination is coupled to chromosome oscillation. In this review, the possible contribution of chromosome oscillation in the elimination of erroneous attachment is discussed in light of the recent finding.","doi":"10.3390/ijms22063174","authors":"Yamamoto A","authors_abbrev":"Yamamoto A","pubmed_publication_date":"20 Mar 2021","pubmed_entrez_date":"2021-04-03","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-04-07 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32222413","title":"\"Lessons from the extremes: Epigenetic and genetic regulation in point monocentromere and holocentromere establishment on artificial chromosomes\".","citation":"Exp Cell Res 2020 May 15;390(2):111974","abstract":"The formation of de novo centromeres on artificial chromosomes in humans (HACs) and fission yeast (SpYACs) has provided much insights to the epigenetic and genetic control on regional centromere establishment and maintenance. Similarly, the use of artificial chromosomes in point centromeric budding yeast Saccharomyces cerevisiae (ScYACs) and holocentric Caenorhabditis elegans (WACs) has revealed epigenetic regulation in the originally thought purely genetically-determined point centromeres and some centromeric DNA sequence features in holocentromeres, respectively. These relatively extreme and less characterized centromere organizations, on the endogenous chromosomes and artificial chromosomes, will be discussed and compared to the more well-studied regional centromere systems. This review will highlight some of the common epigenetic and genetic features in different centromere architectures, including the presence of the centromeric histone H3 variant, CENP-A or CenH3, centromeric and pericentric transcription, AT-richness and repetitiveness of centromeric DNA sequences.","doi":"10.1016/j.yexcr.2020.111974","authors":"Wong CYY, Ling YH, Mak JKH, Zhu J, Yuen KWY","authors_abbrev":"Wong CYY et al.","pubmed_publication_date":"15 May 2020","pubmed_entrez_date":"2020-03-31","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-04-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:144055","title":"Comparison of the properties of plasma membrane-bound and mitochondria-bound ATPases in the yeast Schizosaccharmoyces pombe.","citation":"Eur J Biochem 1977 Sep 15;79(1):319-28","abstract":"","authors":"Delhez J, Dufour JP, Thines D, Goffeau A","authors_abbrev":"Delhez J et al.","pubmed_publication_date":"15 Sep 1977","pubmed_entrez_date":"1977-09-15","publication_year":"1977","canto_session_key":"27433c1195df0566","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-23 18:09:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-23 18:08:56","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-23"},{"uniquename":"EMBL:AU013934","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24929437","title":"The translational landscape of fission-yeast meiosis and sporulation.","citation":"Nat Struct Mol Biol 2014 Jul;21(7):641-7","abstract":"Sexual development in Schizosaccharomyces pombe culminates in meiosis and sporulation. We used ribosome profiling to investigate the translational landscape of this process. We show that the translation efficiency of hundreds of genes is regulated in complex patterns, often correlating with changes in RNA levels. Ribosome-protected fragments show a three-nucleotide periodicity that identifies translated sequences and their reading frame. Using this property, we identified 46 new translated genes and found that 24% of noncoding RNAs are actively translated. We also detected 19 nested antisense genes, in which both DNA strands encode translated mRNAs. Finally, we identified 1,735 translated upstream open reading frames (ORFs) in leader sequences. In S. pombe, in contrast with Saccharomyces cerevisiae, sexual development is not accompanied by large increases in upstream ORF use, thus suggesting that this is an organism-specific adaptation, not a general feature of developmental processes.","doi":"10.1038/nsmb.2843","authors":"Duncan CD, Mata J","authors_abbrev":"Duncan CD et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-06-16","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC320.09","SPCC4G3.20","SPBC839.02","SPCC622.06c","SPCC417.03","SPAC3G6.07","SPBC27B12.10c","SPBC146.01","SPAC110.06","SPBC713.14c","SPAC1D4.08","SPAC823.17","SPCC622.03c","SPCC622.07","SPBC1685.17","SPCC162.07","SPAC22F3.04","SPCC1840.13","SPCC622.02","SPAC1A6.03c","SPBC15D4.08c","SPBC13G1.16","SPCC622.01c","SPCC794.15","SPAC959.11"],"gene_count":25,"ltp_gene_count":0},{"uniquename":"PMID:25031431","title":"Regulation of spindle pole body assembly and cytokinesis by the centrin-binding protein Sfi1 in fission yeast.","citation":"Mol Biol Cell 2014 Sep 15;25(18):2735-49","abstract":"Centrosomes play critical roles in the cell division cycle and ciliogenesis. Sfi1 is a centrin-binding protein conserved from yeast to humans. Budding yeast Sfi1 is essential for the initiation of spindle pole body (SPB; yeast centrosome) duplication. However, the recruitment and partitioning of Sfi1 to centrosomal structures have never been fully investigated in any organism, and the presumed importance of the conserved tryptophans in the internal repeats of Sfi1 remains untested. Here we report that in fission yeast, instead of doubling abruptly at the initiation of SPB duplication and remaining at a constant level thereafter, Sfi1 is gradually recruited to SPBs throughout the cell cycle. Like an sfi1Δ mutant, a Trp-to-Arg mutant (sfi1-M46) forms monopolar spindles and exhibits mitosis and cytokinesis defects. Sfi1-M46 protein associates preferentially with one of the two daughter SPBs during mitosis, resulting in a failure of new SPB assembly in the SPB receiving insufficient Sfi1. Although all five conserved tryptophans tested are involved in Sfi1 partitioning, the importance of the individual repeats in Sfi1 differs. In summary, our results reveal a link between the conserved tryptophans and Sfi1 partitioning and suggest a revision of the model for SPB assembly.","doi":"10.1091/mbc.E13-11-0699","authors":"Lee IJ, Wang N, Hu W, Schott K, Bähler J, Giddings TH, Pringle JR, Du LL, Wu JQ","authors_abbrev":"Lee IJ et al.","pubmed_publication_date":"15 Sep 2014","pubmed_entrez_date":"2014-07-18","publication_year":"2014","canto_session_key":"d1136231555649d1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-07-19 00:15:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20070859","title":"Fission yeast Vps1 and Atg8 contribute to oxidative stress resistance.","citation":"Genes Cells 2010 Mar;15(3):229-42","abstract":"Organisms have evolved diverse means to protect themselves from oxidative stress. To better understand the molecular mechanisms involved in oxidative stress resistance, we screened fission yeast mutants sensitive to paraquat, a reagent acting on the mitochondria to generate reactive oxygen species. Among the mutants we isolated, we focused on a mutant defective in the vps1(+) (vacuolar protein sorting 1) gene that encodes a dynamin-related protein family member. vps1Δ exhibited aberrant mitochondrial and vacuolar morphology on treatment with paraquat. vps1Δ was sensitive to osmotic stress, high concentrations of Ca(2+) and Fe(2+). Interestingly, the deletion of atg8(+), a gene essential for the autophagy pathway, exhibited strong genetic interactions with vps1Δ. The vps1Δatg8Δ double mutant was additively sensitive to oxidative stress, osmotic stress and Ca(2+). The deletion of vps1(+) rescued the bizarre vacuolar morphology shown by atg8Δ. Such genetic interactions were not observed with other atg mutants. Furthermore, the atg8-G116A mutant did not show abnormal vacuolar morphology while being sensitive to nitrogen starvation, an autophagy-related phenotype. Taken together, we conclude that atg8(+) regulates vacuolar functions independently of its role in autophagy. We propose that Vps1 and Atg8 cooperatively participate in vacuolar function, thereby contributing to oxidative stress resistance.","doi":"10.1111/j.1365-2443.2009.01376.x","authors":"Mikawa T, Kanoh J, Ishikawa F","authors_abbrev":"Mikawa T et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2010-01-15","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12C2.08","SPBC31E1.01c","SPAC767.01c","SPBP8B7.24c","SPAC19B12.08","SPBC6B1.05c","SPCC63.08c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:18337696","title":"Nitrogen depletion causes up-regulation of glutathione content and gamma-glutamyltranspeptidase in Schizosaccharomyces pombe.","citation":"J Microbiol 2008 Feb;46(1):70-4","abstract":"This work aims to elucidate the relationship between nitrogen depletion and Glutathione (GSH) level in Schizosaccharomyces pombe. The total GSH level was much higher in the Pap1-positive KP1 cells than in the Pap1-negative TP108-3C cells, suggesting that synthesis of GSH is dependent on Pap1. When the Pap1-positive KP1 cells were transferred to the nitrogen-depleted medium, total GSH level significantly increased up to 6 h and then slightly declined after 9 h. Elevation of the total GSH level was observed to be much less with the Pap1-negative cells. However, glucose deprivation was not able to enhance the GSH level in the KP1 cells. Activity of gamma-glutamyltranspeptidase (gamma-GT), an enzyme in the first step of GSH catabolism, also increased during nitrogen depletion. The total GSH level was more significantly enhanced in the KP1 cells overexpressing gamma-GT2 than gamma-GT1 during nitrogen starvation. Reactive oxygen species (ROS) levels were not changed during nitrogen starvation in both Pap1-positive and Pap1-negative cells. Collectively, nitrogen depletion causes up-regulation of GSH synthesis and gamma-GT in a Pap1-dependent manner.","doi":"10.1007/s12275-007-0244-y","authors":"Song SH, Lim CJ","authors_abbrev":"Song SH et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2008-03-14","publication_year":"2008","canto_session_key":"9d08f7029974925e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-10 15:03:12","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-10 15:03:02","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.09","SPAC1783.07c","SPAC56E4.06c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2014-12-10"},{"uniquename":"PMID:21502135","title":"Regulation and function of the fission yeast myosins.","citation":"J Cell Sci 2011 May 01;124(Pt 9):1383-90","abstract":"It is now quarter of a century since the actin cytoskeleton was first described in the fission yeast, Schizosaccharomyces pombe. Since then, a substantial body of research has been undertaken on this tractable model organism, extending our knowledge of the organisation and function of the actomyosin cytoskeleton in fission yeast and eukaryotes in general. Yeast represents one of the simplest eukaryotic model systems that has been characterised to date, and its genome encodes genes for homologues of the majority of actin regulators and actin-binding proteins found in metazoan cells. The ease with which diverse methodologies can be used, together with the small number of myosins, makes fission yeast an attractive model system for actomyosin research and provides the opportunity to fully understand the biochemical and functional characteristics of all myosins within a single cell type. In this Commentary, we examine the differences between the five S. pombe myosins, and focus on how these reflect the diversity of their functions. We go on to examine the role that the actin cytoskeleton plays in regulating the myosin motor activity and function, and finally explore how research in this simple unicellular organism is providing insights into the substantial impacts these motors can have on development and viability in multicellular higher-order eukaryotes.","doi":"10.1242/jcs.078527","authors":"East DA, Mulvihill DP","authors_abbrev":"East DA et al.","pubmed_publication_date":"01 May 2011","pubmed_entrez_date":"2011-04-20","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2349217","title":"Introduction of large linear minichromosomes into Schizosaccharomyces pombe by an improved transformation procedure.","citation":"Proc Natl Acad Sci U S A 1990 Jun;87(11):4043-7","abstract":"The efficiency of transformation of Schizosaccharomyces pombe has been increased 10- to 50-fold over previously reported methods. By using 1 microgram of plasmid, 7.0 x 10(5) transformants are regularly obtained. This increased transformation efficiency is mainly due to the inclusion of the cationic liposome-forming reagent Lipofectin in the protocol. Various parameters affecting transformation of Sc. pombe in the presence of Lipofectin have been examined. Lipofectin can also be used to increase transformation efficiency in Saccharomyces cerevisiae. It is also demonstrated that by using this improved transformation procedure, linear minichromosomes of greater than 500 kilobases can be introduced into Sc. pombe with relative ease. These minichromosomes can replicate as stable linear molecules upon reintroduction into Sc. pombe, demonstrating that Sc. pombe telomeres retain function when reintroduced as naked DNA. The ability of Sc. pombe to admit large DNA molecules indicates that it should be feasible to clone large DNA from other organisms in Sc. pombe.","authors":"Allshire RC","authors_abbrev":"Allshire RC","pubmed_publication_date":"Jun 1990","pubmed_entrez_date":"1990-06-01","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19150433","title":"Distinct requirements for the Rad32(Mre11) nuclease and Ctp1(CtIP) in the removal of covalently bound topoisomerase I and II from DNA.","citation":"Mol Cell 2009 Jan 16;33(1):117-23","abstract":"For a cancer cell to resist treatment with drugs that trap topoisomerases covalently on the DNA, the topoisomerase must be removed. In this study, we provide evidence that the Schizosaccharomyces pombe Rad32(Mre11) nuclease activity is involved in the removal of both Top2 from 5' DNA ends as well as Top1 from 3' ends in vivo. A ctp1(CtIP) deletion is defective for Top2 removal but overproficient for Top1 removal, suggesting that Ctp1(CtIP) plays distinct roles in removing topoisomerases from 5' and 3' DNA ends. Analysis of separation of function mutants suggests that MRN-dependent topoisomerase removal contributes significantly to resistance against topoisomerase-trapping drugs. This study has important implications for our understanding of the role of the MRN complex and CtIP in resistance of cells to a clinically important group of anticancer drugs.","doi":"10.1016/j.molcel.2008.11.021","authors":"Hartsuiker E, Neale MJ, Carr AM","authors_abbrev":"Hartsuiker E et al.","pubmed_publication_date":"16 Jan 2009","pubmed_entrez_date":"2009-01-20","publication_year":"2009","canto_session_key":"5b59bb193448a673","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-02-03 15:36:34","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-02-03 15:36:22","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":39,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPCC338.08","SPBC1703.14c","SPAC13C5.07","SPBC1A4.03c","SPBC543.03c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2017-02-03"},{"uniquename":"PMID:15640837","title":"Yeast polo-like kinases: functionally conserved multitask mitotic regulators.","citation":"Oncogene 2005 Jan 10;24(2):217-29","abstract":"The polo-like kinases (Plks) are a conserved subfamily of Ser/Thr protein kinases that play pivotal roles in regulating various cellular and biochemical events at multiple stages of M phase. Genetic and biochemical data revealed that both the budding yeast and the fission yeast polo kinase homologs (Cdc5 and Plo1, respectively) bear remarkable functional similarities with those in metazoan organisms, suggesting that the role of Plks is largely conserved throughout evolution. Thus, studies on Plks in genetically amenable lower eucaryotic organisms may yield valuable insights into the function of Plks in higher eucaryotic organisms. In this review, common properties and distinct functions of Cdc5 and Plo1 will be discussed and compared to properties and functions of Plks in higher eucaryotic organisms.","authors":"Lee KS, Park JE, Asano S, Park CJ","authors_abbrev":"Lee KS et al.","pubmed_publication_date":"10 Jan 2005","pubmed_entrez_date":"2005-01-11","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23154893","title":"Looping in on Ndc80 - how does a protein loop at the kinetochore control chromosome segregation?","citation":"Bioessays 2012 Dec;34(12):1070-7","abstract":"Segregation of chromosomes during mitosis requires the interaction of dynamic microtubules with the kinetochore, a large protein structure established on the centromere region of sister chromatids. The core microtubule-binding activity of the kinetochore resides in the KMN network, an outer kinetochore complex. As part of the KMN network, the Ndc80 complex, which is composed of Ndc80, Nuf2, Spc24, and Spc25, is able to bind directly to microtubules and has the ability to track with depolymerizing microtubules to produce chromosome movement. The Ndc80 complex binds directly to microtubules through a calponin homology domain and an unstructured tail in the N terminus of the Ndc80 protein. A recent flurry of papers has highlighted the importance of an internal loop region in Ndc80 in establishing end-on attachment to microtubules. Here I discuss these recent findings that suggest that the Ndc80 internal loop functions as a binding site for proteins required for kinetochore-microtubule interactions.","doi":"10.1002/bies.201200096","authors":"Nilsson J","authors_abbrev":"Nilsson J","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-11-17","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:47:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7622450","title":"Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes.","citation":"J Biol Chem 1995 Jul 14;270(28):16499-502","abstract":"Targeting of import substrate to nuclear pore complexes of permeabilized vertebrate cells was previously shown to require a protein complex composed of two subunits, termed karyopherin. Yeast contain a homologue of karyopherin alpha named Srp1p, which was initially identified as a genetic suppressor of mutations in a subunit of RNA polymerase I. To determine whether yeast contain a karyopherin complex that includes Srp1p as the karyopherin alpha homologue, we genetically replaced Srp1p with a Srp1-Protein A chimera. Cytosol from this strain contained a complex, composed of the chimera and a protein of 95 kDa, that was purified using affinity chromatography on IgG Sepharose. Microsequence analysis showed that the 95-kDa protein was identical with a yeast protein encoded by gene L8300.15 on chromosome XII. Sequence comparison revealed that the L8300.15 gene product is the closest structural homologue of vertebrate karyopherin beta. The yeast alpha and beta karyopherin subunits were expressed in Escherichia coli and were purified. When combined, they formed a heterodimeric complex and were active in targeting import substrate to nuclear envelopes of mammalian cells. We propose that all karyopherins function as alpha/beta heterodimers.","authors":"Enenkel C, Blobel G, Rexach M","authors_abbrev":"Enenkel C et al.","pubmed_publication_date":"14 Jul 1995","pubmed_entrez_date":"1995-07-14","publication_year":"1995","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC962.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24256285","title":"Role of Cdc42 dynamics in the control of fission yeast cell polarization.","citation":"Biochem Soc Trans 2013 Dec;41(6):1745-9","abstract":"Cell polarization is fundamental to many cellular processes, including cell differentiation, cell motility and cell fate determination. A key regulatory enzyme in the control of cell morphogenesis is the conserved Rho GTPase Cdc42, which breaks symmetry via self-amplifying positive-feedback mechanisms. Additional mechanisms of control, including competition between different sites of polarized cell growth and time-delayed negative feedback, define a cellular-level system that promotes Cdc42 oscillatory dynamics and modulates activated Cdc42 intracellular distribution.","doi":"10.1042/BST20130241","authors":"Das M, Verde F","authors_abbrev":"Das M et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_session_key":"e5e524ba2a0a7e0c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18540083","title":"Dikaryotic cell division of the fission yeast Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2008 Jun;72(6):1531-8","abstract":"Dikaryons, cells with two haploid nuclei contributed by the members of a mating pair, are part of the life cycle of many filamentous fungi, but the molecular mechanisms underlying the division of dikaryons are largely unknown. We found that the fission yeast Schizosaccharomyces pombe has a latent ability to divide as a dikaryon. Cells capable of restarting the mitotic cycle with two nuclei were prepared by transient inactivation of the septation initiation network. Close pairing of the two nuclei before mitosis was dependent on minus-end-directed kinesin Klp2p and was essential for propagation as a dikaryon. The two spindles extended in opposite directions, keeping their old spindle pole bodies at the prospective site of cell division until the mid-anaphase. The spindles then overlapped, exchanging the inner nuclei. Finally, twin mitosis was followed by a single cytokinesis, producing two daughter dikaryons carrying copies of the original pair of nuclei.","authors":"Okazaki K, Niwa O","authors_abbrev":"Okazaki K et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-06-10","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11134033","title":"Fission yeast homolog of murine Int-6 protein, encoded by mouse mammary tumor virus integration site, is associated with the conserved core subunits of eukaryotic translation initiation factor 3.","citation":"J Biol Chem 2001 Mar 30;276(13):10056-62","abstract":"The murine int-6 locus, identified as a frequent integration site of mouse mammary tumor viruses, encodes the 48-kDa eIF3e subunit of translation initiation factor eIF3. Previous studies indicated that the catalytically active core of budding yeast eIF3 consists of five subunits, all conserved in eukaryotes, but does not contain a protein closely related to eIF3e/Int-6. Whereas the budding yeast genome does not encode a protein closely related to murine Int-6, fission yeast does encode an Int-6 ortholog, designated here Int6. We found that fission yeast Int6/eIF3e is a cytoplasmic protein associated with 40 S ribosomes. FLAG epitope-tagged Tif35, a putative core eIF3g subunit, copurified with Int6 and all five orthologs of core eIF3 subunits. An int6 deletion (int6Delta) mutant was viable but grew slowly in minimal medium. This slow growth phenotype was accompanied by a reduction in the amount of polyribosomes engaged in translation and was complemented by expression of human Int-6 protein. These findings support the idea that human and Schizosaccharomyces pombe Int-6 homologs are involved in translation. Interestingly, haploid int6Delta cells showed unequal nuclear partitioning, possibly because of a defect in tubulin function, and diploid int6Delta cells formed abnormal spores. We propose that Int6 is not an essential subunit of eIF3 but might be involved in regulating the activity of eIF3 for translation of specific mRNAs in S. pombe.","authors":"Akiyoshi Y, Clayton J, Phan L, Yamamoto M, Hinnebusch AG, Watanabe Y, Asano K","authors_abbrev":"Akiyoshi Y et al.","pubmed_publication_date":"30 Mar 2001","pubmed_entrez_date":"2001-01-13","publication_year":"2001","canto_session_key":"c03bdfb180e8b701","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-10-31 21:58:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-31 19:45:00","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17D11.05","SPAC4D7.05","SPBC18H10.03","SPAC25G10.08","SPBC646.09c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-10-31"},{"uniquename":"PMID:15189983","title":"Suppressors of an adenylate cyclase deletion in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2004 Jun;3(3):610-9","abstract":"Schizosaccharomyces pombe utilizes two opposing signaling pathways to sense and respond to its nutritional environment. Glucose detection triggers a cyclic AMP signal to activate protein kinase A (PKA), while glucose or nitrogen starvation activates the Spc1/Sty1 stress-activated protein kinase (SAPK). One process controlled by these pathways is fbp1+ transcription, which is glucose repressed. In this study, we isolated strains carrying mutations that reduce high-level fbp1+ transcription conferred by the loss of adenylate cyclase (git2delta), including both wis1- (SAPK kinase) and spc1- (SAPK) mutants. While characterizing the git2delta suppressor strains, we found that the git2delta parental strains are KCl sensitive, though not osmotically sensitive. Of 102 git2delta suppressor strains, 17 strains display KCl-resistant growth and comprise a single linkage group, carrying mutations in the cgs1+ PKA regulatory subunit gene. Surprisingly, some of these mutants are mostly wild type for mating and stationary-phase viability, unlike the previously characterized cgs1-1 mutant, while showing a significant defect in fbp1-lacZ expression. Thus, certain cgs1- mutant alleles dramatically affect some PKA-regulated processes while having little effect on others. We demonstrate that the PKA and SAPK pathways regulate both cgs1+ and pka1+ transcription, providing a mechanism for cross talk between these two antagonistically acting pathways and feedback regulation of the PKA pathway. Finally, strains defective in both the PKA and SAPK pathways display transcriptional regulation of cgs1+ and pka1+, suggesting the presence of a third glucose-responsive signaling pathway.","authors":"Stiefel J, Wang L, Kelly DA, Janoo RT, Seitz J, Whitehall SK, Hoffman CS","authors_abbrev":"Stiefel J et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-06-11","publication_year":"2004","canto_session_key":"c3b8098ab8181f07","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-11-09 19:20:41","canto_approved_date":"2022-11-10 13:17:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-09 18:38:25","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC8C9.03","SPAC24B11.06c","SPBC19C7.03","SPBC1198.14c","SPBC106.10"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2022-11-09"},{"uniquename":"PMID:10769201","title":"The S. pombe orthologue of the S. cerevisiae mob1 gene is essential and functions in signalling the onset of septum formation.","citation":"J Cell Sci 2000 May;113 ( Pt 10):1695-704","abstract":"We have isolated the Schizosaccharomyces pombe orthologue of the Saccharomyces cerevisiae MOB1 gene in a screen designed to enrich for septation mutants. The gene is essential, and cells lacking it display a phenotype typical of septation signalling network mutants. mob1p is located on both spindle pole bodies throughout mitosis. In addition it is also co-localised with the medial ring later in mitosis, and flanks the septum as the medial ring contracts. We also demonstrate that mob1p can be precipitated from cells in a complex with the septation regulating kinase sid2p.","authors":"Salimova E, Sohrmann M, Fournier N, Simanis V","authors_abbrev":"Salimova E et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-04-19","publication_year":"2000","canto_session_key":"ec544fc38144a140","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-07-10 10:05:56","canto_approved_date":"2026-06-08 22:07:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-07-10 10:05:50","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":23,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPAC1565.06c","SPBC24C6.07","SPBC244.01c","SPAC24B11.11c","SPAC9G1.09","SPCC4B3.15","SPAC4F8.13c","SPBC12D12.01","SPBC1718.07c","SPBC21.06c","SPAC20G8.05c","SPCC1739.11c","SPCC645.05c","SPAC17G8.10c","SPAP8A3.08","SPAC222.10c","SPBC428.13c"],"gene_count":18,"ltp_gene_count":15,"approved_date":"2025-07-10"},{"uniquename":"PMID:8016079","title":"A small nuclear GTP-binding protein from tomato suppresses a Schizosaccharomyces pombe cell-cycle mutant.","citation":"Proc Natl Acad Sci U S A 1994 Jun 21;91(13):5863-7","abstract":"Ran is a 25-kDa Ras-related nuclear GTP-binding protein which is very highly conserved in humans, Saccharomyces cerevisiae, and Schizosaccharomyces pombe. Ran has been found to form a stable, noncovalent complex with the chromatin-associated protein RCC1, a negative regulator of mitosis. In Sch. pombe, a temperature-sensitive mutation in the RCC1 homolog encoded by the pim1 gene causes premature induction of mitosis, and this mutation can be suppressed by overexpression of the Ran homolog encoded by spi1. We report here the cloning of three Ran cDNAs from tomato. The Ran protein is very highly conserved among plants, animals, and fungi. In tomato, Ran mRNA is expressed in all tissues examined, even those with little or no cell division, indicating that Ran in plants may have functions other than just control of mitosis. We have found that the tomato Ran protein can direct a beta-glucuronidase reporter protein to the plant cell nucleus, confirming that Ran is a nuclear protein in plants. We show that the tomato Ran protein can suppress the Sch. pombe pim1 mutation, indicating that the tomato Ran protein and the Sch. pombe spi1 protein are functionally homologous.","authors":"Ach RA, Gruissem W","authors_abbrev":"Ach RA et al.","pubmed_publication_date":"21 Jun 1994","pubmed_entrez_date":"1994-06-21","publication_year":"1994","canto_session_key":"d4dc0fc42c0d6494","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-20 15:14:07","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-20 15:13:55","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC557.03c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-20"},{"uniquename":"PMID:31289327","title":"Telomere DNA length-dependent regulation of DNA replication timing at internal late replication origins.","citation":"Sci Rep 2019 Jul 09;9(1):9946","abstract":"DNA replication is initiated at replication origins on chromosomes at their scheduled time during S phase of the cell cycle. Replication timing control is highly conserved among eukaryotes but the underlying mechanisms are not fully understood. Recent studies have revealed that some telomere-binding proteins regulate replication timing at late-replicating origins throughout the genome. To investigate the molecular basis of this process, we analyzed the effects of excessive elongation of telomere DNA on replication timing by deleting telomere-associated shelterin proteins in Schizosaccharomyces pombe. We found that rap1∆ and poz1∆ cells showed abnormally accelerated replication at internal late origins but not at subtelomere regions. These defects were suppressed by removal of telomere DNA and by deletion of the telomere-binding protein Taz1. Furthermore, Sds21-a counter protein phosphatase against Dbf4-dependent kinase (DDK)-accumulated at elongated telomeres in a Taz1-dependent manner but was depleted at internal late origins, indicating that highly elongated telomeres sequester Sds21 at telomeres and perturb replication timing at internal regions. These results demonstrate that telomere DNA length is an important determinant of replication timing at internal regions of chromosomes in eukaryotes.","doi":"10.1038/s41598-019-46229-1","authors":"Hasegawa Y, Yamamoto M, Miyamori J, Kanoh J","authors_abbrev":"Hasegawa Y et al.","pubmed_publication_date":"09 Jul 2019","pubmed_entrez_date":"2019-07-11","publication_year":"2019","canto_session_key":"9f729989228125e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junko Kanoh","canto_first_approved_date":"2019-08-28 16:02:39","canto_approved_date":"2020-04-02 11:49:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-23 09:28:07","canto_added_date":"2019-07-12 00:15:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Junko Kanoh","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC31H12.05c","SPAC19G12.13c","SPAC6F6.17","SPBC1778.02","SPAC16A10.07c","SPBC29A3.14c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-08-28"},{"uniquename":"PMID:29294138","title":"Editor's Highlight: A Genome-wide Screening of Target Genes Against Silver Nanoparticles in Fission Yeast.","citation":"Toxicol Sci 2018 Jan 01;161(1):171-185","abstract":"To identify target genes against silver nanoparticles (AgNPs), we screened a genome-wide gene deletion library of 4843 fission yeast heterozygous mutants covering 96% of all protein encoding genes. A total of 33 targets were identified by a microarray and subsequent individual confirmation. The target pattern of AgNPs was more similar to those of AgNO3 and H2O2, followed by Cd and As. The toxic effect of AgNPs on fission yeast was attributed to the intracellular uptake of AgNPs, followed by the subsequent release of Ag+, leading to the generation of reactive oxygen species (ROS). Next, we focused on the top 10 sensitive targets for further studies. As described previously, 7 nonessential targets were associated with detoxification of ROS, because their heterozygous mutants showed elevated ROS levels. Three novel essential targets were related to folate metabolism or cellular component organization, resulting in cell cycle arrest and no induction in the transcriptional level of antioxidant enzymes such as Sod1 and Gpx1 when 1 of the 2 copies was deleted. Intriguingly, met9 played a key role in combating AgNP-induced ROS generation via NADPH production and was also conserved in a human cell line.","doi":"10.1093/toxsci/kfx208","authors":"Lee AR, Lee SJ, Lee M, Nam M, Lee S, Choi J, Lee HJ, Kim DU, Hoe KL","authors_abbrev":"Lee AR et al.","pubmed_publication_date":"01 Jan 2018","pubmed_entrez_date":"2018-01-03","publication_year":"2018","canto_session_key":"0ad02adeb90a8109","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-06-28 13:56:52","canto_approved_date":"2021-03-11 15:35:51","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-06-28 13:56:25","canto_added_date":"2018-01-04 01:15:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":81,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.10c","SPAC328.01c","SPAC3F10.02c","SPAC9G1.02","SPAC4D7.09","SPBC2F12.03c","SPBC887.12","SPAC56F8.10","SPBC106.02c","SPBC428.08c","SPAC1805.14","SPBC1709.05","SPCC4B3.08","SPBC887.10","SPCC16A11.14","SPBC30B4.03c","SPAC22F3.10c","SPBC2G5.06c","SPCC737.06c","SPBC36.06c","SPCC1827.07c","SPAC767.01c","SPAC3H1.10","SPAC3G9.12","SPBC29A3.03c","SPBC1604.12","SPAC9.02c","SPAC4G8.09","SPAC2F7.02c","SPAC1834.01","SPCC63.13","SPAC890.08","SPAC4H3.07c"],"gene_count":33,"ltp_gene_count":33,"approved_date":"2019-06-28"},{"uniquename":"PMID:967158","title":"The product of the ade1: gene in Schizosaccharomyces pombe: a bifunctional enzyme catalysing two distinct steps in purine biosynthesis.","citation":"Mol Gen Genet 1976 Sep 23;147(3):271-82","abstract":"The assignment of the known ade genes to steps in purine biosynthesis in Schizosaccharomyces pombe has been completed with the demonstration that an ade3 mutants lacks FGAR amidotransferase, ade1A mutants lack GAR synthetase and ade1B mutants lack AIR synthetase. A comparison of enzyme activity with map position for ade1 mutants shows that (1) complementing ade1A mutants lack GAR synthetase but posses wild type amounts of AIR synthetase, (2) complementing ade1B mutants lack AIR synthetase but posses variable amounts of GAR synthetase, (3) non-complementing mutants lack both activities. In wild type strains the two activities fractionate together throughout a hundred-fold purification. Hence the ade1 gene appears to code for a bifunctional enzyme catalysing two distinct steps in purine biosynthesis. The two activities are catalysed by two different regions of the polypeptide chain which can be altered independently by mutation. Gel filtration studies on partially purified enzymes from wild type and various complementing mutant strains, indicate that the bifunctional enzyme is a multimer consisting of between four and six sub-units of 40,000 daltons each. GAR synthetase activity is associated with both the monomeric and multimeric forms but AIR synthetase is only associated with the multimer. A comparison of enzyme levels between diploids and their original complementing haploid strains suggests that complementation is due to hybrid enzyme formation.","authors":"Fluri R, Coddington A, Flury U","authors_abbrev":"Fluri R et al.","pubmed_publication_date":"23 Sep 1976","pubmed_entrez_date":"1976-09-23","publication_year":"1976","canto_session_key":"3ca4ce72b9911abf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2012-12-21 15:18:54","canto_approved_date":"2024-04-04 11:18:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-11-19 16:45:19","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC405.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-21"},{"uniquename":"PMID:34251689","title":"Yesprit and Yeaseq: Applications for designing primers and browsing sequences for research using the four Schizosaccharomyces species.","citation":"Yeast 2021 Nov;38(11):583-591","abstract":"The polymerase chain reaction (PCR)-based gene targeting method, which can delete a specific gene or introduce tags, has been widely utilized to study gene function in fission yeast. One of the critical steps in this method is to design primers for amplifying DNA fragments of deletion or tagging modules and for checking the integration of those DNA fragments at designated loci. Although the primer design tool Pombe PCR Primer Program (PPPP) is available for Schizosaccharomyces pombe, there is no such publicly available application for the other three fission yeast species, S. cryophilus, S. japonicus, and S. octosporus. Likewise, no application enabling DNA/protein sequence retrieval for these three fission yeast species is available either. Therefore, access to such functionality would substantially assist in retrieval of gene sequences of interest and primer design in these fission yeast species. In this report, we describe two applications for fission yeast study: Yesprit and Yeaseq. Yesprit is a primer design tool for strain construction using the PCR-based method, and Yeaseq is a sequence viewer that can acquire the DNA/protein sequences of specific genes. Both tools can be run on the Windows, macOS, and Linux platforms. We believe that the Yesprit and Yeaseq will facilitate research using the four fission yeast species.","doi":"10.1002/yea.3660","authors":"Wang X, Xu R, Wang Y, Liu Z, Lou R, Sugiyama T","authors_abbrev":"Wang X et al.","pubmed_publication_date":"Nov 2021","pubmed_entrez_date":"2021-07-12","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-07-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18820678","title":"Stepwise chromatin remodelling by a cascade of transcription initiation of non-coding RNAs.","citation":"Nature 2008 Nov 06;456(7218):130-4","abstract":"Recent transcriptome analyses using high-density tiling arrays and data from large-scale analyses of full-length complementary DNA libraries by the FANTOM3 consortium demonstrate that many transcripts are non-coding RNAs (ncRNAs). These transcriptome analyses indicate that many of the non-coding regions, previously thought to be functionally inert, are actually transcriptionally active regions with various features. Furthermore, most relatively large ( approximately several kilobases) polyadenylated messenger RNA transcripts are transcribed from regions harbouring little coding potential. However, the function of such ncRNAs is mostly unknown and has been a matter of debate. Here we show that RNA polymerase II (RNAPII) transcription of ncRNAs is required for chromatin remodelling at the fission yeast Schizosaccharomyces pombe fbp1(+) locus during transcriptional activation. The chromatin at fbp1(+) is progressively converted to an open configuration, as several species of ncRNAs are transcribed through fbp1(+). This is coupled with the translocation of RNAPII through the region upstream of the eventual fbp1(+) transcriptional start site. Insertion of a transcription terminator into this upstream region abolishes both the cascade of transcription of ncRNAs and the progressive chromatin alteration. Our results demonstrate that transcription through the promoter region is required to make DNA sequences accessible to transcriptional activators and to RNAPII.","doi":"10.1038/nature07348","authors":"Hirota K, Miyoshi T, Kugou K, Hoffman CS, Shibata T, Ohta K","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"06 Nov 2008","pubmed_entrez_date":"2008-09-30","publication_year":"2008","canto_session_key":"ff9ebc8d76211732","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-31 23:19:53","canto_approved_date":"2024-01-31 23:19:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-29 15:51:28","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.1326","SPAC630.14c","SPNCRNA.1325","SPAC18B11.10","SPBC29B5.01","SPNCRNA.4604","SPAC6F12.02","SPBC1198.14c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2024-01-31"},{"uniquename":"PMID:3040264","title":"DNA topoisomerase II is required for condensation and separation of mitotic chromosomes in S. pombe.","citation":"Cell 1987 Sep 11;50(6):917-25","abstract":"We show that DNA topoisomerase II (topo II) is continuously required for mitotic chromosome changes in Schizosaccharomyces pombe. We constructed cold-sensitive (cs) or temperature-sensitive (ts) strains mutated in the genes coding for topo II (top2) and beta-tubulin (nda3). The ATP-dependent activity of the top2cs gene product is cs in vitro. The cloned top2cs gene sequence predicts an amino acid substitution. A cs top2-cs nda3 double mutant at 20 degrees C shows long, entangled chromosomes, which condense and separate upon the shift to permissive temperatures. If spindle formation is prevented at permissive temperatures, the chromosomes condense but do not separate. Thus topo II is required for final chromosome condensation; moreover, pulse-shift experiments show that topo II is required for chromatid disjuction. Experiments with ts top2-cs nda3 cells show that topo II is also required for chromosome separation in anaphase: inactivation of topo II and activation of beta-tubulin allow normal spindle formation but result in \"streaked\" chromosomes.","authors":"Uemura T, Ohkura H, Adachi Y, Morino K, Shiozaki K, Yanagida M","authors_abbrev":"Uemura T et al.","pubmed_publication_date":"11 Sep 1987","pubmed_entrez_date":"1987-09-11","publication_year":"1987","canto_session_key":"6e175411383ea731","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-11 19:54:26","canto_approved_date":"2023-05-03 16:47:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 14:11:21","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPBC1A4.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-10-11"},{"uniquename":"PMID:17261756","title":"Epigenetics and the estrogen receptor.","citation":"Ann N Y Acad Sci 2006 Nov;1089:73-87","abstract":"The position effect variegation in Drosophila and Schizosaccharomyces pombe, and higher-order chromatin structure regulation in yeast, is orchestrated by modifier genes of the Su(var) group, (e.g., histone deacetylases ([HDACs]), protein phosphatases) and enhancer E(Var) group (e.g., ATP [adenosine 5'-triphosphate]-dependent nucleosome remodeling proteins). Higher-order chromatin structure is regulated in part by covalent modification of the N-terminal histone tails of chromatin, and histone tails in turn serve as platforms for recruitment of signaling modules that include nonhistone proteins such as heterochromatin protein (HP1) and NuRD. Because the enzymes governing chromatin structure through covalent modifications of histones (acetylation, methylation, phosphorylation, ubiquitination) can also target nonhistone substrates, a mechanism is in place by which epigenetic regulatory processes can affect the function of these alternate substrates. The posttranslational modification of histones, through phosphorylation and acetylation at specific residues, alters chromatin structure in an orchestrated manner in response to specific signals and is considered the basis of a \"histone code.\" In an analogous manner, specific residues within transcription factors form a signaling module within the transcription factor to determine genetic target specificity and cellular fate. The architecture of these signaling cascades in transcription factors (SCITs) are poorly understood. The regulation of estrogen receptor (ERalpha) by enzymes that convey epigenetic signals is carefully orchestrated and is reviewed here.","authors":"Leader JE, Wang C, Popov VM, Fu M, Pestell RG","authors_abbrev":"Leader JE et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2007-01-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29133455","title":"How causal analysis can reveal autonomy in models of biological systems.","citation":"Philos Trans A Math Phys Eng Sci 2017 Dec 28;375(2109)","abstract":"Standard techniques for studying biological systems largely focus on their dynamical or, more recently, their informational properties, usually taking either a reductionist or holistic perspective. Yet, studying only individual system elements or the dynamics of the system as a whole disregards the organizational structure of the system-whether there are subsets of elements with joint causes or effects, and whether the system is strongly integrated or composed of several loosely interacting components. Integrated information theory offers a theoretical framework to (1) investigate the compositional cause-effect structure of a system and to (2) identify causal borders of highly integrated elements comprising local maxima of intrinsic cause-effect power. Here we apply this comprehensive causal analysis to a Boolean network model of the fission yeast ( Schizosaccharomyces pombe ) cell cycle. We demonstrate that this biological model features a non-trivial causal architecture, whose discovery may provide insights about the real cell cycle that could not be gained from holistic or reductionist approaches. We also show how some specific properties of this underlying causal architecture relate to the biological notion of autonomy. Ultimately, we suggest that analysing the causal organization of a system, including key features like intrinsic control and stable causal borders, should prove relevant for distinguishing life from non-life, and thus could also illuminate the origin of life problem.This article is part of the themed issue 'Reconceptualizing the origins of life'.","doi":"10.1098/rsta.2016.0358","authors":"Marshall W, Kim H, Walker SI, Tononi G, Albantakis L","authors_abbrev":"Marshall W et al.","pubmed_publication_date":"28 Dec 2017","pubmed_entrez_date":"2017-11-15","publication_year":"2017","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2017-11-16 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8843195","title":"The Atr and Atm protein kinases associate with different sites along meiotically pairing chromosomes.","citation":"Genes Dev 1996 Oct 01;10(19):2423-37","abstract":"A number of cell-cycle checkpoint genes have been shown to play important roles in meiosis. We have characterized the human and mouse counterpart of the Schizosaccharomyces pombe Rad3 protein, named Atr (for ataxia-telangiectasia- and rad3-related), and the protein that is mutated in ataxia-telangiectasia, Atm. We demonstrate that ATR mRNA and protein are expressed in human and mouse testis. More detailed analysis of specific cells in seminiferous tubules shows localization of Atr to the nuclei of cells in the process of meiosis I. Using immunoprecipitation and immunoblot analysis, we show that Atr and Atm proteins are approximately 300 and 350 kD relative molecular mass, respectively, and further demonstrate that both proteins have associated protein kinase activity. Further, we demonstrate that Atr and Atm interact directly with meiotic chromosomes and show complementary localization patterns on synapsing chromosomes. Atr is found at sites along unpaired or asynapsed chromosomal axes, whereas Atm is found along synapsed chromosomal axes. This is the first demonstration of a nuclear association of Atr and Atm proteins with meiotic chromosomes and suggests a direct role for these proteins in recognizing and responding to DNA strand interruptions that occur during meiotic recombination.","authors":"Keegan KS, Holtzman DA, Plug AW, Christenson ER, Brainerd EE, Flaggs G, Bentley NJ, Taylor EM, Meyn MS, Moss SB, Carr AM, Ashley T, Hoekstra MF","authors_abbrev":"Keegan KS et al.","pubmed_publication_date":"01 Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:11063679","title":"A fission yeast repression element cooperates with centromere-like sequences and defines a mat silent domain boundary.","citation":"Genetics 2000 Nov;156(3):983-94","abstract":"REII is a Schizosaccharomyces pombe repression element located at the centromere-proximal end of the mat silent domain. Here we show that inversion of REII enhances silencing on its centromere-proximal side while suppressing silencing on its centromere-distal side. Transplacement of REII to a position 2.5 kb from its native locus extends the region of stringent repression to the new REII site. These results suggest that REII defines a mat silent domain boundary by acting preferentially toward its centromere-distal side. To investigate cooperation between REII and a K-region sequence that shares homology with the centromeric dg dh repeats (cen2 homology), we targeted combinations of these elements to an ectopic site and monitored expression of an adjacent reporter gene. Centromeric dh-like sequences conferred low-level silencing on the adjacent reporter gene, and REII, which did not display silencing activity on its own, enhanced cen2 homology-mediated silencing. Cooperation was also apparent at the mat locus, where deletion of REII impaired repression stability. We propose that REII and the cen2 homology play different yet complementary roles in silencing establishment and inheritance at the mat locus.","authors":"Ayoub N, Goldshmidt I, Lyakhovetsky R, Cohen A","authors_abbrev":"Ayoub N et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-11-07","publication_year":"2000","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18794354","title":"Schizosaccharomyces pombe Ddb1 recruits substrate-specific adaptor proteins through a novel protein motif, the DDB-box.","citation":"Mol Cell Biol 2008 Nov;28(22):6746-56","abstract":"DDB1 was isolated as a UV-damaged DNA-binding protein, but recent studies established that it plays a role as a component of cullin 4A ubiquitin ligases. Cullin-RING complexes are the largest known ubiquitin ligase family, with hundreds of substrate-specific adaptor subunits and which are defined by characteristic motifs. A common motif for DDB1/cullin 4 ubiquitin ligases, a WDXR motif, was recently reported. Here, we show that Schizosaccharomyces pombe Ddb1 associates with several WD40 repeat proteins that share a novel protein motif designated the DDB-box, a motif essential for interaction with Ddb1 and independent of WD40 repeats, unlike the WDXR motif. We also show that ddb1(+) and the putative CSA homolog ckn1(+) are involved in transcription-coupled nucleotide excision repair and that the DDB-box is essential for the ckn1(+) function in vivo. These data indicate that the DDB-box is another common motif which defines adaptor proteins for DDB1/cullin 4 ubiquitin ligases.","doi":"10.1128/MCB.00757-08","authors":"Fukumoto Y, Dohmae N, Hanaoka F","authors_abbrev":"Fukumoto Y et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-09-17","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPCC736.15","SPCP25A2.02c","SPAC3A11.08","SPBC19C7.09c","HGNC:30002","SPBC609.03","SPAC24C9.12c","SPAC17H9.19c","SPBC577.09","SPAC17H9.10c","SPAC4A8.14","SPBC646.13","SPCC364.07","SPAC12G12.10","SPCC1739.13"],"gene_count":14,"ltp_gene_count":14},{"uniquename":"PMID:1398093","title":"Isolation and characterization of the Schizosaccharomyces pombe rad3 gene, involved in the DNA damage and DNA synthesis checkpoints.","citation":"Gene 1992 Sep 21;119(1):83-9","abstract":"We have cloned the Schizosaccharomyces pombe rad3 gene which is involved in G2 arrest following DNA damage, and in the dependence of mitosis on the completion of DNA replication. The gene was cloned by complementation of the sensitivity to UV light and gamma rays of the rad3-136 mutant with an Sz. pombe genomic library. Sublocalization of the complementing activity and sequencing of the clone identified an intronless 3210-bp open reading frame capable of encoding a 1070-amino acid protein with an M(r) of 121974. The rad3 gene is a new gene with no homologs in existing sequence databases. The gene is poorly expressed, with a codon bias index of -0.01. A disruption mutant affecting the coding region was only slightly more sensitive to UV light than the original rad3-136 mutant. The rad3 gene was mapped to NotI fragment C on chromosome II.","authors":"Seaton BL, Yucel J, Sunnerhagen P, Subramani S","authors_abbrev":"Seaton BL et al.","pubmed_publication_date":"21 Sep 1992","pubmed_entrez_date":"1992-09-21","publication_year":"1992","canto_session_key":"0bcb6b33a1bdb4ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-08-16 13:58:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-16 13:58:35","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"vw253@cam.ac.uk","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-08-16"},{"uniquename":"PMID:31956022","title":"Delineating the Rules for Structural Adaptation of Membrane-Associated Proteins to Evolutionary Changes in Membrane Lipidome.","citation":"Curr Biol 2020 Feb 03;30(3):367-380.e8","abstract":"Membrane function is fundamental to life. Each species explores membrane lipid diversity within a genetically predefined range of possibilities. How membrane lipid composition in turn defines the functional space available for evolution of membrane-centered processes remains largely unknown. We address this fundamental question using related fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. We show that, unlike S. pombe that generates membranes where both glycerophospholipid acyl tails are predominantly 16-18 carbons long, S. japonicus synthesizes unusual \"asymmetrical\" glycerophospholipids where the tails differ in length by 6-8 carbons. This results in stiffer bilayers with distinct lipid packing properties. Retroengineered S. pombe synthesizing the S.-japonicus-type phospholipids exhibits unfolded protein response and downregulates secretion. Importantly, our protein sequence comparisons and domain swap experiments support the hypothesis that transmembrane helices co-evolve with membranes, suggesting that, on the evolutionary scale, changes in membrane lipid composition may necessitate extensive adaptation of the membrane-associated proteome.","doi":"10.1016/j.cub.2019.11.043","authors":"Makarova M, Peter M, Balogh G, Glatz A, MacRae JI, Lopez Mora N, Booth P, Makeyev E, Vigh L, Oliferenko S","authors_abbrev":"Makarova M et al.","pubmed_publication_date":"03 Feb 2020","pubmed_entrez_date":"2020-01-21","publication_year":"2020","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:X68789","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22891259","title":"Fission yeast Ags1 confers the essential septum strength needed for safe gradual cell abscission.","citation":"J Cell Biol 2012 Aug 20;198(4):637-56","abstract":"Fungal cytokinesis requires the assembly of a dividing septum wall. In yeast, the septum has to be selectively digested during the critical cell separation process. Fission yeast cell wall α(1-3)glucan is essential, but nothing is known about its localization and function in the cell wall or about cooperation between the α- and β(1-3)glucan synthases Ags1 and Bgs for cell wall and septum assembly. Here, we generate a physiological Ags1-GFP variant and demonstrate a tight colocalization with Bgs1, suggesting a cooperation in the important early steps of septum construction. Moreover, we define the essential functions of α(1-3)glucan in septation and cell separation. We show that α(1-3)glucan is essential for both secondary septum formation and the primary septum structural strength needed to support the physical forces of the cell turgor pressure during cell separation. Consequently, the absence of Ags1 and therefore α(1-3)glucan generates a special and unique side-explosive cell separation due to an instantaneous primary septum tearing caused by the turgor pressure.","doi":"10.1083/jcb.201202015","authors":"Cortés JC, Sato M, Muñoz J, Moreno MB, Clemente-Ramos JA, Ramos M, Okada H, Osumi M, Durán A, Ribas JC","authors_abbrev":"Cortés JC et al.","pubmed_publication_date":"20 Aug 2012","pubmed_entrez_date":"2012-08-15","publication_year":"2012","canto_session_key":"5c6727a02c994591","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juan Carlos Ribas","canto_first_approved_date":"2018-11-08 14:22:25","canto_approved_date":"2026-01-31 14:22:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-04 09:50:34","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Juan Carlos Ribas","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.15c","SPBC19G7.05c","SPCC1281.01","SPBC21.06c","SPCC1919.10c","SPAC20G8.05c","SPAC24B11.11c","SPBC21B10.05c","SPBC32H8.12c","SPCC4B3.15","SPCC895.05","SPAC1F5.04c","SPCC1223.06","SPCC970.09","SPCC1739.11c","SPBC1604.20c"],"gene_count":16,"ltp_gene_count":12,"approved_date":"2018-11-08"},{"uniquename":"PMID:9535817","title":"Isolation and characterization of an invertase and its repressor genes from Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 1998 Apr 07;245(1):246-53","abstract":"PCR was used to isolate an invertase homolog gene from the fission yeast Schizosaccharomyces pombe. The cloned inv1(+) gene encodes a protein of 581 amino acids with 16 potential asparagine-linked glycosylation sites, and has 39% and 38% identity to the Schwanniomyces occidentalis and Saccharomyces cerevisiae SUC2 invertases. When the inv1(+) gene was disrupted, S. pombe strains lacked detectable invertase activity. This result showed that the inv1(+) gene encodes only one active invertase in S. pombe cells. The transcription of inv1(+) is repressed in the presence of glucose. The transcription of inv1(+) was not affected in cyr1Delta strain which lacks adenylate cyclase activity, unlike transcription of S. pombe fbp1(+) gene. We have identified an S. pombe gene (scr1(+)) that encodes a homolog of the Aspergillus nidulans CREA which is required for glucose repression of the glyconeogenic pathway. Although the deletion of scr1(+) did not influence the transcription of fbp1(+) gene, glucose repression of the inv1(+) gene was severely affected. These results showed that glucose repression of inv1(+) gene is dependent on scr1(+) gene, and S. pombe cAMP signalling pathway may not be essential for glucose repression of inv1(+) gene.","authors":"Tanaka N, Ohuchi N, Mukai Y, Osaka Y, Ohtani Y, Tabuchi M, Bhuiyan MS, Fukui H, Harashima S, Takegawa K","authors_abbrev":"Tanaka N et al.","pubmed_publication_date":"07 Apr 1998","pubmed_entrez_date":"1998-05-16","publication_year":"1998","canto_session_key":"7e0c631c21160a2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-03-17 13:21:41","canto_approved_date":"2023-10-29 17:35:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-17 13:21:35","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC1198.14c","SPBC1D7.02c","SPBC19C7.03","SPCC191.11"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2021-03-17"},{"uniquename":"PMID:17072895","title":"Proceedings of the 2006 European Fission Yeast Meeting. March 16-18, 2006. Hinxton, United Kingdom.","citation":"Yeast 2006 Oct 15;23(13):899-1043","abstract":"","authors":"","authors_abbrev":"","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23273429","title":"Nonequivalence observed for the 16-meric structure of a small heat shock protein, SpHsp16.0, from Schizosaccharomyces pombe.","citation":"Structure 2013 Feb 05;21(2):220-8","abstract":"Small heat shock proteins (sHsps) play a role in preventing the fatal aggregation of denatured proteins in the presence of stresses. The sHsps exist as monodisperse oligomers in their resting state. Because the hydrophobic N-terminal regions of sHsps are possible interaction sites for denatured proteins, the manner of assembly of the oligomer is critical for the activation and inactivation mechanisms. Here, we report the oligomer architecture of SpHsp16.0 from Schizosaccharomyces pombe determined with X-ray crystallography and small angle X-ray scattering. Both results indicate that eight dimers of SpHsp16.0 form an elongated sphere with 422 symmetry. The monomers show nonequivalence in the interaction with neighboring monomers and conformations of the N- and C-terminal regions. Variants for the N-terminal phenylalanine residues indicate that the oligomer formation ability is highly correlated with chaperone activity. Structural and biophysical results are discussed in terms of their possible relevance to the activation mechanism of SpHsp16.0.","doi":"10.1016/j.str.2012.11.015","authors":"Hanazono Y, Takeda K, Oka T, Abe T, Tomonari T, Akiyama N, Aikawa Y, Yohda M, Miki K","authors_abbrev":"Hanazono Y et al.","pubmed_publication_date":"05 Feb 2013","pubmed_entrez_date":"2013-01-01","publication_year":"2013","canto_session_key":"2e372e2cc60d9110","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-03 08:59:24","canto_approved_date":"2023-03-13 23:16:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-01 15:17:07","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-03","pdb_entries":[{"pdb_id":"3w1z","gene_chains":[{"gene_uniquename":"SPBC3E7.02c","chain":"A/B/C/D","position":"1-143"}],"title":"Heat shock protein 16.0 from Schizosaccharomyces pombe","entry_authors":"Hanazono Y,Takeda K,Akiyama N,Aikawa Y,Miki K","entry_authors_abbrev":"Hanazono Y et al.","reference_uniquename":"PMID:23273429","experimental_method":"X-ray","resolution":"2.401"}]},{"uniquename":"EMBL:AU010951","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16778077","title":"Histone modification-dependent and -independent pathways for recruitment of checkpoint protein Crb2 to double-strand breaks.","citation":"Genes Dev 2006 Jun 15;20(12):1583-96","abstract":"Cellular responses to DNA damage involve the relocalization of checkpoint proteins to DNA double-strand breaks (DSBs). The fission yeast checkpoint mediator protein Crb2, a homolog of mammalian 53BP1, forms ionizing radiation-induced nuclear foci (IRIF). The IRIF formation by Crb2 requires histone H2A C-terminal phosphorylation and H4-K20 methylation. However, the relevance of Crb2 relocalization is uncertain, because neither histone modification is required for a checkpoint response. Here we show that these histone modifications cooperate in the same Crb2 recruitment pathway, which also requires the Tudor and BRCT motifs in Crb2. In the absence of these histone modifications, an alternative recruitment pathway is sufficient for checkpoint activation and accumulation of Crb2 at a persistent DSB generated by HO endonuclease. This parallel pathway requires a cyclin-dependent kinase phosphorylation site in Crb2 that mediates an association with another BRCT protein Cut5 (the TopBP1 homolog), which also accumulates at HO-induced DSBs. We propose that such dual recruitment mechanisms may be a common feature of DNA damage checkpoint mediators.","authors":"Du LL, Nakamura TM, Russell P","authors_abbrev":"Du LL et al.","pubmed_publication_date":"15 Jun 2006","pubmed_entrez_date":"2006-06-17","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC342.05","SPCC622.08c","SPAC23C4.18c","SPAC19G12.06c","SPCC4B3.12"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:11527575","title":"A stochastic, molecular model of the fission yeast cell cycle: role of the nucleocytoplasmic ratio in cycle time regulation.","citation":"Biophys Chem 2001 Aug 30;92(1-2):1-15","abstract":"We propose a stochastic version of a recently published, deterministic model of the molecular mechanism regulating the mitotic cell cycle of fission yeast, Schizosaccharomyces pombe. Stochasticity is introduced in two ways: (i) by considering the known asymmetry of cell division, which produces daughter cells of slightly different sizes; and (ii) by assuming that the nuclear volumes of the two newborn cells may also differ. In this model, the accumulation of cyclins in the nucleus is proportional to the ratio of cytoplasmic to nuclear volumes. We have simulated the cell-cycle statistics of populations of wild-type cells and of wee1(-) mutant cells. Our results are consistent with well known experimental observations.","authors":"Sveiczer A, Tyson JJ, Novak B","authors_abbrev":"Sveiczer A et al.","pubmed_publication_date":"30 Aug 2001","pubmed_entrez_date":"2001-08-31","publication_year":"2001","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2492433","title":"Transport of L-lysine in the fission yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1989 Jan 30;978(2):203-8","abstract":"Systems of L-lysine transport in Schizosaccharomyces pombe are not constitutive, as at no phase of growth in a rich medium is lysine taken up. Transport activity appears only after preincubation of harvested cells with glucose or another suitable source of energy. If cycloheximide is added during this preincubation no transport systems are synthesized. After removal of glucose, the activity of the transport system decays with a half-time of 13 min. The transport of L-lysine into S. pombe cells from the stationary phase of growth preincubated for 60 min with 1% D-glucose is mediated by at least two systems, the high-affinity one with a Kt of 26 mumol/l and Jmax of 4.95 nmol/min per mg dry wt., the low-affinity one with a KT of 1.1 mmol/l and Jmax of 11.8 nmol/min per mg dry wt. The transport of lysine mediated by these two systems proceeds uphill. The high-affinity system has a pH optimum at 4.0-4.2, the accumulation ratio is highest at a cell density 2-5 mg dry wt. per ml and decreases with increasing lysine concentrations. Lysine accumulated by this system does not exit from cells. The only potent competitive inhibitors are L-arginine, L-histidine and D-lysine. The other amino acids tested do not behave as competitive inhibitors. Of the various metabolic inhibitors tested, the most potent were proton conductors and antimycin A.","authors":"Sychrová H, Horák J, Kotyk A","authors_abbrev":"Sychrová H et al.","pubmed_publication_date":"30 Jan 1989","pubmed_entrez_date":"1989-01-30","publication_year":"1989","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28282432","title":"Metabolic crosstalk between membrane and storage lipids facilitates heat stress management in Schizosaccharomyces pombe.","citation":"PLoS One 2017;12(3):e0173739","abstract":"Cell membranes actively participate in stress sensing and signalling. Here we present the first in-depth lipidomic analysis to characterize alterations in the fission yeast Schizosaccharomyces pombe in response to mild heat stress (HS). The lipidome was assessed by a simple one-step methanolic extraction. Genetic manipulations that altered triglyceride (TG) content in the absence or presence of HS gave rise to distinct lipidomic fingerprints for S. pombe. Cells unable to produce TG demonstrated long-lasting growth arrest and enhanced signalling lipid generation. Our results reveal that metabolic crosstalk between membrane and storage lipids facilitates homeostatic maintenance of the membrane physical/chemical state that resists negative effects on cell growth and viability in response to HS. We propose a novel stress adaptation mechanism in which heat-induced TG synthesis contributes to membrane rigidization by accommodating unsaturated fatty acids of structural lipids, enabling their replacement by newly synthesized saturated fatty acids.","doi":"10.1371/journal.pone.0173739","authors":"Péter M, Glatz A, Gudmann P, Gombos I, Török Z, Horváth I, Vígh L, Balogh G","authors_abbrev":"Péter M et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-03-11","publication_year":"2017","canto_session_key":"2c0c6b098c28ca92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-09-03 13:57:18","canto_approved_date":"2024-10-01 07:58:46","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-20 16:08:22","canto_added_date":"2017-03-12 01:15:14","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":9,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1235.15","SPBC776.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-09-03"},{"uniquename":"PMID:20512112","title":"Importance of polyadenylation in the selective elimination of meiotic mRNAs in growing S. pombe cells.","citation":"EMBO J 2010 Jul 07;29(13):2173-81","abstract":"A number of meiosis-specific mRNAs are initially weakly transcribed, but then selectively removed during fission yeast mitotic growth. These mRNAs harbour a region termed DSR (determinant of selective removal), which is recognized by the YTH family RNA-binding protein Mmi1p. Mmi1p directs the destruction of these mRNAs in collaboration with nuclear exosomes. However, detailed molecular mechanisms underlying this process of selective mRNA elimination have remained elusive. In this study, we demonstrate the critical role of polyadenylation in this process. Two-hybrid and genetic screens revealed potential interactions between Mmi1p and proteins involved in polyadenylation. Additional investigations showed that destruction of DSR-containing mRNAs by exosomes required polyadenylation by a canonical poly(A) polymerase. The recruitment of Pab2p, a poly(A)-binding protein, to the poly(A) tail was also necessary for mRNA destruction. In cells undergoing vegetative growth, Mmi1p localized with exosomes, Pab2p, and components of the polyadenylation complex in several patchy structures in the nucleoplasm. These patches may represent the sites for degradation of meiosis-specific mRNAs with untimely expression.","doi":"10.1038/emboj.2010.108","authors":"Yamanaka S, Yamashita A, Harigaya Y, Iwata R, Yamamoto M","authors_abbrev":"Yamanaka S et al.","pubmed_publication_date":"07 Jul 2010","pubmed_entrez_date":"2010-06-01","publication_year":"2010","canto_session_key":"69438ba591723417","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-25 19:10:20","canto_approved_date":"2026-01-30 14:33:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-26 17:43:17","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.04","SPAC1F3.01","SPCC736.12c","SPBC16E9.12c","SPBC26H8.10","SPAC644.16","SPNCRNA.103","SPAC12G12.13c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-02-25"},{"uniquename":"EMBL:AU012026","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10705982","title":"Purification and properties of pyridoxine oxidase from Aureobacterium luteolum and pyridoxal reductase from Schizosaccharomyces pombe.","citation":"Biofactors 2000;11(1-2):123-6","abstract":"","authors":"Yagi T, Ashiuchi M, Kaneda Y, Sano H","authors_abbrev":"Yagi T et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-03-08","publication_year":"2000","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9E9.11"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:41651413","title":"TORC2 Coordinates MBF-Dependent Transcription and Restrains Oxidative Stress Responses During DNA Replication Stress in Fission Yeast.","citation":"J Biol Chem 2026 Feb 04;:111242","abstract":"The Target of Rapamycin (TOR) kinase is a core component of two evolutionarily conserved complexes, TORC1 and TORC2, which regulate growth, metabolism, and stress responses. In Schizosaccharomyces pombe, TORC2 is dispensable for proliferation under optimal conditions but is essential for survival and adaptation to a variety of stress conditions, including DNA damage and replication stress. The MluI-binding factor (MBF) transcription complex regulates G1/S progression and the DNA replication stress response. Previously, we demonstrated that TORC2-Gad8 is required for the upregulation of MBF-dependent gene transcription in response to replication stress. Here, we show that in response to replication stress TORC2 is necessary for the accumulation of the initiating form of RNA polymerase II (Pol II) at MBF promoters. In contrast, the elongating form of Pol II aberrantly accumulates at MBF coding regions in TORC2-deficient cells under both induced and non-induced conditions, suggesting a defect in balancing Pol II initiation and elongation that leads to impaired MBF gene induction. Unexpectedly, TORC2-deficient cells also exhibit aberrant upregulation of stress-activated genes during replication stress, including a distinct subset of Pap1-dependent oxidative stress genes. Consistent with this, TORC2 mutant cells accumulate reactive oxygen species in response to replication stress. Together, our findings suggest that TORC2 is required to ensure proper upregulation of MBF-dependent gene transcription during replication stress, and to suppress inappropriate activation of oxidative stress response pathways.","doi":"10.1016/j.jbc.2026.111242","authors":"Cohen A, Mouzon A, Sprecher U, Kupiec M, Weisman R","authors_abbrev":"Cohen A et al.","pubmed_publication_date":"04 Feb 2026","pubmed_entrez_date":"2026-02-06","publication_year":"2026","canto_session_key":"e4b8c8d70f495dfb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-02-08 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9643541","title":"Schizosaccharomyces pombe isp4 encodes a transporter representing a novel family of oligopeptide transporters.","citation":"Mol Microbiol 1998 May;28(4):729-41","abstract":"We have recently cloned an oligopeptide transport gene from Candida albicans denoted OPT1. This gene showed significant sequence similarity to three open reading frames (ORFs) with no previously established function: isp4 from Schizosaccharomyces pombe and Saccharomyces cerevisiae YJL212C and YPR194C, identified during the genome project. The S. pombe gene isp4 was originally identified by Sato et al. as a gene that was upregulated through nitrogen starvation induction of meiosis. However, an isp4delta strain exhibited a wild-type phenotype with respect to sexual differentiation. We have found that the same isp4delta strain is deficient in tetrapeptide transport activity as measured by its resistance to toxic tetrapeptides, by its inability to accumulate a radiolabelled tetrapeptide and by the inability to use tetrapeptides as a sole source of an amino acid to satisfy an auxotrophic requirement. Similarly, we found that the ORF YPR194C from S. cerevisiae encodes an oligopeptide transporter. Sequence analyses as well as physiological evidence has led us to propose that the proteins encoded by isp4 and the genes identified from S. cerevisiae and C. albicans comprise a new group of transporters specific for small oligopeptides, which we have named the OPT family.","authors":"Lubkowitz MA, Barnes D, Breslav M, Burchfield A, Naider F, Becker JM","authors_abbrev":"Lubkowitz MA et al.","pubmed_publication_date":"May 1998","pubmed_entrez_date":"1998-06-27","publication_year":"1998","canto_session_key":"90e254b79d556ce0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-09-24 14:42:02","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-24 14:41:56","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-24"},{"uniquename":"PMID:6059030","title":"A remark to the origin of pure mutant clones observed after UV treatment of Schizosaccharomyces pombe.","citation":"Mutat Res 1967;4(4):514-6","abstract":"","authors":"Haefner K","authors_abbrev":"Haefner K","pubmed_publication_date":"1967","pubmed_entrez_date":"1967-07-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28648780","title":"The Histone Acetyltransferase Mst2 Protects Active Chromatin from Epigenetic Silencing by Acetylating the Ubiquitin Ligase Brl1.","citation":"Mol Cell 2017 Jul 20;67(2):294-307.e9","abstract":"Faithful propagation of functionally distinct chromatin states is crucial for maintaining cellular identity, and its breakdown can lead to diseases such as cancer. Whereas mechanisms that sustain repressed states have been intensely studied, regulatory circuits that protect active chromatin from inactivating signals are not well understood. Here we report a positive feedback loop that preserves the transcription-competent state of RNA polymerase II-transcribed genes. We found that Pdp3 recruits the histone acetyltransferase Mst2 to H3K36me3-marked chromatin. Thereby, Mst2 binds to all transcriptionally active regions genome-wide. Besides acetylating histone H3K14, Mst2 also acetylates Brl1, a component of the histone H2B ubiquitin ligase complex. Brl1 acetylation increases histone H2B ubiquitination, which positively feeds back on transcription and prevents ectopic heterochromatin assembly. Our work uncovers a molecular pathway that secures epigenome integrity and highlights the importance of opposing feedback loops for the partitioning of chromatin into transcriptionally active and inactive states.","doi":"10.1016/j.molcel.2017.05.026","authors":"Flury V, Georgescu PR, Iesmantavicius V, Shimada Y, Kuzdere T, Braun S, Bühler M","authors_abbrev":"Flury V et al.","pubmed_publication_date":"20 Jul 2017","pubmed_entrez_date":"2017-06-27","publication_year":"2017","canto_session_key":"2116f3ec933b2d67","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-09-29 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1919.15","SPCC736.11","SPCC188.13c","SPAC17G8.13c","SPAC664.03","SPAC29B12.02c","SPAC23D3.01","SPAC1952.05"],"gene_count":8,"ltp_gene_count":7},{"uniquename":"PMID:15623507","title":"PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol.","citation":"J Biol Chem 2005 Mar 11;280(10):9489-97","abstract":"Glycosylphosphatidylinositol (GPI) is a glycolipid that anchors many proteins to the eukaryotic cell surface. The biosynthetic pathway of GPI is mediated by sequential additions of sugars and other components to phosphatidylinositol. Four mannoses in the GPI are transferred from dolichol-phosphate-mannose (Dol-P-Man) and are linked through different glycosidic linkages. Therefore, four Dol-P-Man-dependent mannosyltransferases, GPI-MT-I, -MT-II, -MT-III, and -MT-IV for the first, second, third, and fourth mannoses, respectively, are required for generation of GPI. GPI-MT-I (PIG-M), GPI-MT-III (PIG-B), and GPI-MT-IV (SMP3) were previously reported, but GPI-MT-II remains to be identified. Here we report the cloning of PIG-V involved in transferring the second mannose in the GPI anchor. Human PIG-V encodes a 493-amino acid, endoplasmic reticulum (ER) resident protein with eight putative transmembrane regions. Saccharomyces cerevisiae protein encoded in open reading frame YBR004c, which we termed GPI18, has 25% amino acid identity to human PIG-V. Viability of the yeast gpi18 deletion mutant was restored by human PIG-V cDNA. PIG-V has two functionally important conserved regions facing the ER lumen. Taken together, we suggest that PIG-V is the second mannosyltransferase in GPI anchor biosynthesis.","authors":"Kang JY, Hong Y, Ashida H, Shishioh N, Murakami Y, Morita YS, Maeda Y, Kinoshita T","authors_abbrev":"Kang JY et al.","pubmed_publication_date":"11 Mar 2005","pubmed_entrez_date":"2004-12-30","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18B11.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24204302","title":"tRNA methyltransferase homolog gene TRMT10A mutation in young onset diabetes and primary microcephaly in humans.","citation":"PLoS Genet 2013 Oct;9(10):e1003888","abstract":"We describe a new syndrome of young onset diabetes, short stature and microcephaly with intellectual disability in a large consanguineous family with three affected children. Linkage analysis and whole exome sequencing were used to identify the causal nonsense mutation, which changed an arginine codon into a stop at position 127 of the tRNA methyltransferase homolog gene TRMT10A (also called RG9MTD2). TRMT10A mRNA and protein were absent in lymphoblasts from the affected siblings. TRMT10A is ubiquitously expressed but enriched in brain and pancreatic islets, consistent with the tissues affected in this syndrome. In situ hybridization studies showed that TRMT10A is expressed in human embryonic and fetal brain. TRMT10A is the mammalian ortholog of S. cerevisiae TRM10, previously shown to catalyze the methylation of guanine 9 (m(1)G9) in several tRNAs. Consistent with this putative function, in silico topology prediction indicated that TRMT10A has predominant nuclear localization, which we experimentally confirmed by immunofluorescence and confocal microscopy. TRMT10A localizes to the nucleolus of β- and non-β-cells, where tRNA modifications occur. TRMT10A silencing induces rat and human β-cell apoptosis. Taken together, we propose that TRMT10A deficiency negatively affects β-cell mass and the pool of neurons in the developing brain. This is the first study describing the impact of TRMT10A deficiency in mammals, highlighting a role in the pathogenesis of microcephaly and early onset diabetes. In light of the recent report that the type 2 diabetes candidate gene CDKAL1 is a tRNA methylthiotransferase, the findings in this family suggest broader relevance of tRNA methyltransferases in the pathogenesis of type 2 diabetes.","doi":"10.1371/journal.pgen.1003888","authors":"Igoillo-Esteve M, Genin A, Lambert N, Désir J, Pirson I, Abdulkarim B, Simonis N, Drielsma A, Marselli L, Marchetti P, Vanderhaeghen P, Eizirik DL, Wuyts W, Julier C, Chakera AJ, Ellard S, Hattersley AT, Abramowicz M, Cnop M","authors_abbrev":"Igoillo-Esteve M et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-11-09","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6B12.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11204772","title":"Sibling differences in cell death of the fission yeast, Schizosaccharomyces pombe, exposed to stress conditions.","citation":"Antonie Van Leeuwenhoek 2000 Aug;78(2):203-7","abstract":"","authors":"Miyata M, Miyata H, Johnson BF","authors_abbrev":"Miyata M et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2001-02-24","publication_year":"2000","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20876564","title":"Antagonistic roles of PP2A-Pab1 and Etd1 in the control of cytokinesis in fission yeast.","citation":"Genetics 2010 Dec;186(4):1261-70","abstract":"In Schizosaccharomyces pombe, Etd1 is a positive regulator of the septation initiation network (SIN), a conserved GTPase-regulated kinase cascade that triggers cytokinesis. Here we show that a mutation in the pab1 gene, which encodes the B-regulatory subunit of the protein phosphatase 2A (PP2A), suppresses mutations in the etd1 gene. Etd1 is required for the function of the GTPase Spg1, a key regulator of SIN signaling. Interestingly, the loss of Pab1 function restored the activity of Spg1 in Etd1-deficient cells. This result suggests that PP2A-Pab1-mediated dephosphorylation inhibits Spg1, thus antagonizing Etd1 function. The loss of pab1 function also rescues the lethality of mutants of other genes in the SIN cascade such as mob1, sid1, and cdc11. Two-hybrid assays indicate that Pab1 physically interacts with Mob1, Sid1, Sid2, and Cdc11, suggesting that the phosphatase 2A B-subunit is a component of the SIN complex. Together, our results indicate that PP2A-Pab1 plays a novel role in cytokinesis, regulating SIN activity at different levels. Pab1 is also required to activate polarized cell growth. Thus, PP2A-Pab1 may be involved in coordinating polar growth and cytokinesis.","doi":"10.1534/genetics.110.121368","authors":"Lahoz A, Alcaide-Gavilán M, Daga RR, Jimenez J","authors_abbrev":"Lahoz A et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-09-30","publication_year":"2010","canto_session_key":"85e293d86887ff6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-17 11:36:58","canto_approved_date":"2026-02-01 09:43:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-15 17:14:36","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":51,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.08","SPBC21.06c","SPBC24C6.07","SPCC1739.11c","SPBC11B10.09","SPAC1565.06c","SPAC16E8.09","SPAC20G8.05c","SPAC9G1.09","SPCC18B5.03","SPAC227.07c","SPAC6F6.08c","SPAC24B11.11c","SPBC428.13c"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2024-05-17"},{"uniquename":"PMID:11076964","title":"Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp.","citation":"J Cell Biol 2000 Nov 13;151(4):789-800","abstract":"Fission yeast myo1(+) encodes a myosin-I with all three tail homology domains (TH1, 2, 3) found in typical long-tailed myosin-Is. Myo1p tail also contains a COOH-terminal acidic region similar to the A-domain of WASp/Scar proteins and other fungal myosin-Is. Our analysis shows that Myo1p and Wsp1p, the fission yeast WASp-like protein, share functions and cooperate in controlling actin assembly. First, Myo1p localizes to cortical patches enriched at tips of growing cells and at sites of cell division. Myo1p patches partially colocalize with actin patches and are dependent on an intact actin cytoskeleton. Second, although deletion of myo1(+) is not lethal, Deltamyo1 cells have actin cytoskeletal defects, including loss of polarized cell growth, delocalized actin patches, and mating defects. Third, additional disruption of wsp1(+) is synthetically lethal, suggesting that these genes may share functions. In mapping the domains of Myo1p tail that share function with Wsp1p, we discovered that a Myo1p construct with just the head and TH1 domains is sufficient for cortical localization and to rescue all Deltamyo1 defects. However, it fails to rescue the Deltamyo1 Deltawsp1 lethality. Additional tail domains, TH2 and TH3, are required to complement the double mutant. Fourth, we show that a recombinant Myo1p tail binds to Arp2/3 complex and activates its actin nucleation activity.","authors":"Lee WL, Bezanilla M, Pollard TD","authors_abbrev":"Lee WL et al.","pubmed_publication_date":"13 Nov 2000","pubmed_entrez_date":"2000-11-15","publication_year":"2000","canto_session_key":"f9a2c4769a3f8ab9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-01-11 16:34:18","canto_approved_date":"2023-08-10 14:18:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-11 16:34:09","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":63,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.13c","SPNCRNA.1237","SPAC4F10.15c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2019-01-11"},{"uniquename":"PMID:33341559","title":"Effect of Saccharomyces cerevisiae and Schizosaccharomyces pombe strains on chemical composition and sensory quality of ciders made from Finnish apple cultivars.","citation":"Food Chem 2021 May 30;345:128833","abstract":"Composition of volatile compounds and concentrations of sugars and organic acids were studied in apple ciders produced with Saccharomyces cerevisiae and Schizosaccharomyces pombe yeasts using eleven different Finnish apple cultivars. Moreover, sensory quality of selected ciders was studied using check-all-that-apply test with untrained panelists. Seventy-seven volatile compounds were detected in the samples using HS-SPME-GC-MS. In general, the ciders had higher concentrations of higher alcohols, aldehydes, and acetals whereas the juices contained higher contents of C6-alcohols. Simultaneously, fermentation using S. pombe resulted in lower concentrations of malic acid, ethyl pentanoate, ethyl hexanoate, and volatile acids and higher concentrations of residual sugars compared to S. cerevisiae. Ciders made using S. cerevisiae were characterized as 'alcoholic' and 'yeasty' while S. pombe ciders were more frequently described as 'sweet', 'honey-like', and less rated as sour. Besides the strong effect by the yeasts, apple cultivars had significant effects on the compositional and sensorial properties of apple ciders.","doi":"10.1016/j.foodchem.2020.128833","authors":"He W, Liu S, Heponiemi P, Heinonen M, Marsol-Vall A, Ma X, Yang B, Laaksonen O","authors_abbrev":"He W et al.","pubmed_publication_date":"30 May 2021","pubmed_entrez_date":"2020-12-20","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-12-22 01:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9755169","title":"Cdc18 transcription and proteolysis couple S phase to passage through mitosis.","citation":"EMBO J 1998 Oct 01;17(19):5689-98","abstract":"In fission yeast, cdc18p plays a critical role in bringing about the onset of S phase. We show that cdc18p expression is subject to a complex sequence of cell cycle controls which ensure that cdc18p levels rise dramatically as cells exit mitosis, before the appearance of CDK activity in G1. We find that transcription of cdc18, together with the transcription of other cdc10p/res1p targets, is first initiated as cells enter mitosis and continues even in cells arrested in mitosis with highly condensed chromatin. However, cdc18p cannot accumulate during mitosis because it is targeted for proteolysis by mitotic cdc2p-protein kinase-mediated phosphorylation. On exit from mitosis, the cdc2p mitotic kinase activity falls, stabilizing cdc18p, which then rapidly accumulates. This combination of mitotic transcription and CDK-mediated proteolysis ensures that progression through mitosis simultaneously prepares cells for DNA replication. During S phase, cdc18 transcription is then switched off, preventing the re-initiation of DNA synthesis until the completion of the next round of mitosis.","authors":"Baum B, Nishitani H, Yanow S, Nurse P","authors_abbrev":"Baum B et al.","pubmed_publication_date":"01 Oct 1998","pubmed_entrez_date":"1998-10-02","publication_year":"1998","canto_session_key":"5ef3337d730491a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-05-04 08:29:52","canto_approved_date":"2024-04-13 07:28:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-04 15:49:23","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":13,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPAPB2B4.03","SPBC582.03","SPBC336.12c","SPBC725.16","SPAC17C9.01c","SPAC24H6.05","SPBC428.18","SPAC1F7.05","SPBC14C8.07c","SPBC11B10.09"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2018-05-04"},{"uniquename":"PMID:36250672","title":"Development of new tools to study membrane-anchored mammalian Atg8 proteins.","citation":"Autophagy 2023 May;19(5):1424-1443","abstract":"A:C autophagic membrane:cytosol; ALS amyotrophic lateral sclerosis; ATG4 autophagy related 4; Atg8 autophagy related 8; BafA1 bafilomycin A 1 ; BNIP3L/Nix BCL2 interacting protein 3 like; CALCOCO2/NDP52 calcium binding and coiled-coil domain 2; EBSS Earle's balanced salt solution; GABARAP GABA type A receptor-associated protein; GST glutathione S transferase; HKO hexa knockout; K d  dissociation constant; LIR LC3-interacting region; MAP1LC3/LC3 microtubule associated protein 1 light chain 3; NLS nuclear localization signal/sequence; PE phosphatidylethanolamine; SpHfl1  Schizosaccharomyces pombe organic solute transmembrane transporter; SQSTM1/p62 SQSTM1/p62; TARDBP/TDP-43 TAR DNA binding protein; TKO triple knockout.","doi":"10.1080/15548627.2022.2132040","authors":"Park SW, Jeon P, Yamasaki A, Lee HE, Choi H, Mun JY, Jun YW, Park JH, Lee SH, Lee SK, Lee YK, Song HK, Lazarou M, Cho DH, Komatsu M, Noda NN, Jang DJ, Lee JA","authors_abbrev":"Park SW et al.","pubmed_publication_date":"May 2023","pubmed_entrez_date":"2022-10-17","publication_year":"2023","canto_session_key":"546637ba34d5a2f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-02-19 06:04:39","canto_approved_date":"2023-02-19 06:04:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-19 06:04:32","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.06c","SPBP8B7.24c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2023-02-19","pdb_entries":[{"pdb_id":"7yo8","gene_chains":[{"gene_uniquename":"SPAC30D11.06c","chain":"A/A","position":"386-409"}],"title":"Crystal structure of fission yeast Hfl1 LIR fused to human GABARAPL2","entry_authors":"Yamasaki A,Noda NN","entry_authors_abbrev":"Yamasaki A et al.","reference_uniquename":"PMID:36250672","experimental_method":"X-ray","resolution":"1.805"}]},{"uniquename":"PMID:15933715","title":"Etd1p is a novel protein that links the SIN cascade with cytokinesis.","citation":"EMBO J 2005 Jul 06;24(13):2436-46","abstract":"In animal cells, cytokinesis occurs by constriction of an actomyosin ring. In fission yeast cells, ring constriction is triggered by the septum initiation network (SIN), an SPB-associated GTPase-regulated kinase cascade that coordinates exit from mitosis with cytokinesis. We have identified a novel protein, Etd1p, required to trigger actomyosin ring constriction in fission yeasts. This protein is localised at the cell tips during interphase. In mitosis, it relocates to the medial cortex region and, coincident with cytokinesis, it assembles into the actomyosin ring by association to Cdc15p. Relocation of Etd1p from the plasma membrane to the medial ring is triggered by SIN signalling and, reciprocally, relocation of the Sid2p-Mob1p kinase complex from the SPB to the division site, a late step in the execution of the SIN, requires Etd1p. These results suggest that Etd1p coordinates the mitotic activation of SIN with the initiation of actomyosin ring constriction. Etd1p peaks during cytokinesis and is degraded by the ubiquitin-dependent 26S-proteasome pathway at the end of septation, providing a mechanism to couple inactivation of SIN to completion of cytokinesis.","authors":"Daga RR, Lahoz A, Muñoz MJ, Moreno S, Jimenez J","authors_abbrev":"Daga RR et al.","pubmed_publication_date":"06 Jul 2005","pubmed_entrez_date":"2005-06-04","publication_year":"2005","canto_session_key":"3520ae1d8f10669a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-10-03 09:17:52","canto_approved_date":"2025-10-12 18:15:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-29 14:38:29","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPBC21.06c","SPBC428.13c","SPAC27F1.02c","SPAC20G8.05c","SPBC16G5.01","SPAC1006.08"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2022-10-03"},{"uniquename":"PMID:9514947","title":"The Byr2 kinase translocates to the plasma membrane in a Ras1-dependent manner.","citation":"Biochem Biophys Res Commun 1998 Mar 17;244(2):468-74","abstract":"The activation of mitogen-activated protein kinase cascades by the Ras GTPase is an evolutionarily conserved signal transduction mechanism. To better understand the interaction between Ras and its target kinase, we study the yeast Schizosaccharomyces pombe where the Ras1 GTPase activates the Byr2 kinase. Cell fractionation and immunofluorescence showed that Ras1 was localized to the plasma membrane and that Byr2 was in the cytoplasm. When Ras1 was overexpressed, Byr2 was translocated to the plasma membrane. Byr2 translocation was dependent on binding to Ras1 since Ras1-V12, an activated mutant of Ras1, caused more Byr2 translocation than Ras1, since Ras1-D38E, an effector domain mutant, did not cause Byr2 translocation, and since the Ras1-binding domain of Byr2 was necessary and sufficient to cause Byr2 translocation. The Byr2 protein was usually not uniform around the plasma membrane, but was frequently enriched at the cell ends and at the region of septal deposition. This uneven membrane localization depended upon regions of the Byr2 regulatory domain, in addition to those required for Ras1 binding, suggesting that these Byr2 domains participate in protein-protein interactions.","authors":"Bauman P, Cheng QC, Albright CF","authors_abbrev":"Bauman P et al.","pubmed_publication_date":"17 Mar 1998","pubmed_entrez_date":"1998-03-26","publication_year":"1998","canto_session_key":"67fc6a2ee3c6c565","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-18 15:44:08","canto_approved_date":"2026-04-10 20:09:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-09 08:31:45","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC1D7.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-04-18"},{"uniquename":"PMID:27789692","title":"WERAM: a database of writers, erasers and readers of histone acetylation and methylation in eukaryotes.","citation":"Nucleic Acids Res 2017 Jan 04;45(D1):D264-D270","abstract":"In this work, we developed a database WERAM (http://weram.biocuckoo.org/) for histone acetyltransferases, histone deacetylases, histone methyltransferases, histone demethylases and acetyl- or methyl-binding proteins, which catalyze, remove and recognize histone acetylation and methylation sites as 'writers', 'erasers' and 'readers', and synergistically determine the 'histone code'. From the scientific literature, we totally collected over 580 experimentally identified histone regulators from eight model organisms, including Homo sapiens, Mus musculus, Rattus norvegicus, Drosophila melanogaster, Caenorhabditis elegans, Arabidopsis thaliana, Schizosaccharomyces pombe and Saccharomyces cerevisiae We also collected ∼900 site-specific regulator-histone relations from the eight species. According to the experimental evidence, known histone regulators were classified into distinct families. To computationally detect more proteins in eukaryotes, we constructed hidden Markov model (HMM) profiles for histone regulator families. For families without HMM profiles, we also conducted orthologous searches. Totally, WERAM database contained more than 20 thousand non-redundant histone regulators from 148 eukaryotes. The detailed annotations and classification information of histone regulators were provided, together with site-specific histone substrates if available.","doi":"10.1093/nar/gkw1011","authors":"Xu Y, Zhang S, Lin S, Guo Y, Deng W, Zhang Y, Xue Y","authors_abbrev":"Xu Y et al.","pubmed_publication_date":"04 Jan 2017","pubmed_entrez_date":"2016-10-30","publication_year":"2017","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2016-10-31 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12646585","title":"Control of cell polarity in fission yeast by association of Orb6p kinase with the highly conserved protein methyltransferase Skb1p.","citation":"J Biol Chem 2003 Jul 04;278(27):25256-63","abstract":"In the fission yeast Schizosaccharomyces pombe, proper establishment and maintenance of cell polarity require Orb6p, a highly conserved serine/threonine kinase involved in regulating both cell morphogenesis and cell cycle control. Orb6p localizes to the cell tips during interphase and to the cell septum during mitosis. To investigate the mechanisms involved in Orb6p function, we conducted a two-hybrid screen to identify proteins that interact with Orb6p. Using this approach, we identified Skb1p, a highly conserved protein methyltransferase that has been implicated previously in cell cycle control, in the coordination of cell cycle progression with morphological changes, and in hyperosmotic stress response. We found that Skb1p associates with Orb6p in S. pombe cells and that the two proteins interact directly in vitro. Loss of Skb1p exacerbates the phenotype of orb6 mutants, suggesting that Skb1p and Orb6p functionally interact in S. pombe cells. Our results suggest that Skb1p affects the intracellular localization of Orb6p and that loss of Skb1p leads to a redistribution of the Orb6p kinase away from the cell tips. Furthermore, we found that Orb6p kinase activity is strongly increased following exposure to salt shock, suggesting that Orb6p has a role in cell response to hyperosmotic stress. Previous studies have shown that Skb1p interacts with the fission yeast p21-activated kinase homologue Pak1p/Shk1p to regulate cell polarity and cell cycle progression. Our findings identify Orb6p as an additional target for Skb1p and suggest a novel function for Skb1p in the control of cell polarity by regulating the subcellular localization of Orb6p.","authors":"Wiley DJ, Marcus S, D'urso G, Verde F","authors_abbrev":"Wiley DJ et al.","pubmed_publication_date":"04 Jul 2003","pubmed_entrez_date":"2003-03-21","publication_year":"2003","canto_session_key":"5e219fdc549363e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-08-17 16:17:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-08-17 16:17:37","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16H5.11c","SPCC970.04c","SPAC821.12"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-08-17"},{"uniquename":"PMID:20174682","title":"Meta-analysis of genome regulation and expression variability across hundreds of environmental and genetic perturbations in fission yeast.","citation":"Mol Biosyst 2010 Mar;6(3):543-52","abstract":"Genome-wide gene expression is re-programmed in response to external or internal factors such as environmental stress or genetic mutation, respectively, or as a function of endogenous processes such as cell proliferation or differentiation. Here we integrate expression profiling data that have been collected by our laboratory since 2001 and that interrogate more than 900 different experimental conditions. We take advantage of this large data set to rank all genes based on their variability in gene expression across the different conditions. The most variable genes were enriched for functions such as stress response, carbohydrate metabolism and trans-membrane transport, and these genes were underrepresented for introns and tended to be close to telomeres. We then compared how overall gene regulation and variability of gene expression across conditions is affected by environmental or genetic perturbations, and by endogenous programmes. Meiotic differentiation and environmental perturbations led to substantially greater gene expression variability and overall regulation than did genetic perturbations and the transcriptional programme accompanying cell proliferation. We also used the integrated data to identify gene regulation modules using two different clustering approaches. Two major clusters, containing growth- and metabolism-related genes on one hand and stress- and differentiation-related genes on the other, were reciprocally regulated across conditions. We discuss these findings with respect to other recent reports on the regulation and evolution of gene expression.","doi":"10.1039/b913876p","authors":"Pancaldi V, Schubert F, Bähler J","authors_abbrev":"Pancaldi V et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2010-02-23","publication_year":"2010","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8679693","title":"Cloning, sequencing and regulation of a cDNA encoding a small heat-shock protein from Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1996 Jun 07;1307(2):129-31","abstract":"We have isolated a Schizosaccharomyces pombe cDNA encoding a small heat-shock protein, designated Hsp9. The deduced amino acid sequence shares significant homology with the Saccharomyces cerevisiae Hsp12 gene product. Northern blot analysis identified a 600-base transcript which is expressed at a low level in S. pombe exponentially growing cells, but is strongly induced by heat-shock and upon entry into the stationary phase. An increase in the transcript level is also observed in response to glucose deprivation.","authors":"Orlandi I, Cavadini P, Popolo L, Vai M","authors_abbrev":"Orlandi I et al.","pubmed_publication_date":"07 Jun 1996","pubmed_entrez_date":"1996-06-07","publication_year":"1996","canto_session_key":"eb3706225c55307a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-05-07 07:21:36","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-01 12:05:40","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP8A3.04c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-01"},{"uniquename":"PMID:40132111","title":"A fission yeast CENP-B homologue Abp1 prevents RNAi-mediated heterochromatin formation at ribosomal DNA repeats.","citation":"Genetics 2025 Mar 25;","abstract":"In response to nutritional starvation, living cells sensitively regulate the production rates of molecules required for survival. Under glucose starvation, a facultative heterochromatinization of ribosomal DNA (rDNA) is considered to regulate ribosomal RNA (rRNA) production. However, the molecular mechanism is still unclear. Here, we report a novel function of CENP-B homologue Abp1 in forming facultative heterochromatin at rDNA repeats. We find that loss of Abp1 induces an ectopic nucleosome assembly at rDNA repeats. Interestingly, loss of Abp1 induces two mutually exclusive changes at rDNA repeats: an excess accumulation of methylation of histone H3 at lysine 9 (H3K9me), a hallmark of heterochromatin, and an active RNA polymerase II (RNAPII) transcription. This excess heterochromatin represses rRNA expression and requires RNAi machinery for its formation. Furthermore, we show that the excess heterochromatin does not affect cellular viability under glucose starvation but prevents the return to the proliferation cycle in recovering glucose-rich conditions. Since glucose starvation rapidly induces partial Abp1 disassociation from rDNA repeats, we propose that Abp1 regulates an activity of RNAPII transcription that is paradoxically required for RNAi-mediated heterochromatin formation and controls an appropriate level of heterochromatinization at rDNA repeats under glucose starvation.","doi":"10.1093/genetics/iyaf050","authors":"Tsunemine S, Mori M, Murakami Y","authors_abbrev":"Tsunemine S et al.","pubmed_publication_date":"25 Mar 2025","pubmed_entrez_date":"2025-03-25","publication_year":"2025","canto_session_key":"60b7aadea0b93d15","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Satoru Tsunemine","canto_first_approved_date":"2025-08-28 09:09:09","canto_approved_date":"2025-08-28 09:09:11","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-08-12 19:31:04","canto_added_date":"2025-03-26 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Satoru Tsunemine","community_curator":true,"annotation_count":58,"orcid":"0000-0001-5225-7156","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.09","SPBC146.03c","SPAC1834.04","SPBC8D2.04","SPCC306.03c","SPBC1105.04c","SPBC28F2.12","SPAC18G6.02c","SPBC428.08c","SPBC4C3.05c","SPAC23G3.01","SPCC736.11","SPCC188.13c","SPBC1105.11c","SPBC216.07c"],"gene_count":15,"ltp_gene_count":10,"approved_date":"2025-08-28"},{"uniquename":"EMBL:BK009173","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.1709"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18344406","title":"Schizosaccharomyces pombe Hst4 functions in DNA damage response by regulating histone H3 K56 acetylation.","citation":"Eukaryot Cell 2008 May;7(5):800-13","abstract":"The packaging of eukaryotic DNA into chromatin is likely to be crucial for the maintenance of genomic integrity. Histone acetylation and deacetylation, which alter chromatin accessibility, have been implicated in DNA damage tolerance. Here we show that Schizosaccharomyces pombe Hst4, a homolog of histone deacetylase Sir2, participates in S-phase-specific DNA damage tolerance. Hst4 was essential for the survival of cells exposed to the genotoxic agent methyl methanesulfonate (MMS) as well as for cells lacking components of the DNA damage checkpoint pathway. It was required for the deacetylation of histone H3 core domain residue lysine 56, since a strain with a point mutation of its catalytic domain was unable to deacetylate this residue in vivo. Hst4 regulated the acetylation of H3 K56 and was itself cell cycle regulated. We also show that MMS treatment resulted in increased acetylation of histone H3 lysine 56 in wild-type cells and hst4Delta mutants had constitutively elevated levels of histone H3 K56 acetylation. Interestingly, the level of expression of Hst4 decreased upon MMS treatment, suggesting that the cell regulates access to the site of DNA damage by changing the level of this protein. Furthermore, we find that the phenotypes of both K56Q and K56R mutants of histone H3 were similar to those of hst4Delta mutants, suggesting that proper regulation of histone acetylation is important for DNA integrity. We propose that Hst4 is a deacetylase involved in the restoration of chromatin structure following the S phase of cell cycle and DNA damage response.","doi":"10.1128/EC.00379-07","authors":"Haldar D, Kamakaka RT","authors_abbrev":"Haldar D et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-03-18","publication_year":"2008","canto_session_key":"ee41f2de8b73ee9b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-31 23:05:27","canto_approved_date":"2024-01-31 23:05:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-25 12:39:41","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":38,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC3E7.08c","SPBC16D10.07c","SPBC3D6.10","SPCC1259.13","SPAC694.06c","SPAPB24D3.04c","SPAC1556.01c","SPAC1834.04","SPAC1783.04c","SPAC3G6.06c","SPBC8D2.04","SPBC1105.11c","SPBC216.05","SPBC342.05"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2024-01-31"},{"uniquename":"PMID:893551","title":"Control of cell size and cycle time in Schizosaccharomyces pombe.","citation":"J Cell Sci 1977 Apr;24:51-67","abstract":"Steady-state and perturbed cells of Schizosaccharomyces pombe have been observed through several division cycles by time-lapse photomicrography. Perturbed cells were produced by the use of a conditional cell division cycle mutant in which nuclear division is reversibly blocked at high temperature. These experiments show that in both populations cell length at division and cell cycle duration are homeostatically controlled, probably by a primary size-control mechanism. Cycle time is indirectly controlled, as cells which have an extended cycle are on average larger at division, so that duaghters of such cells need to grow by a smaller amount and for a shorter period, before dividing again. In general, deviations from the mean are corrected within a single cycle, but in the case of very long cells the control breaks down because the cycle cannot be shortened by more than a quarter under the conditions used. These cells take more than one cycle to return to normal.","authors":"Fantes PA","authors_abbrev":"Fantes PA","pubmed_publication_date":"Apr 1977","pubmed_entrez_date":"1977-04-01","publication_year":"1977","canto_session_key":"dfdd67175f4b1f26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-07-20 12:14:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-07 10:12:47","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-07-07"},{"uniquename":"PMID:9710635","title":"A novel function of the DNA repair gene rhp6 in mating-type silencing by chromatin remodeling in fission yeast.","citation":"Mol Cell Biol 1998 Sep;18(9):5511-22","abstract":"Recent studies have indicated that the DNA replication machinery is coupled to silencing of mating-type loci in the budding yeast Saccharomyces cerevisiae, and a similar silencing mechanism may operate in the distantly related yeast Schizosaccharomyces pombe. Regarding gene regulation, an important function of DNA replication may be in coupling of faithful chromatin assembly to reestablishment of the parental states of gene expression in daughter cells. We have been interested in isolating mutants that are defective in this hypothesized coupling. An S. pombe mutant fortuitously isolated from a screen for temperature-sensitive growth and silencing phenotype exhibited a novel defect in silencing that was dependent on the switching competence of the mating-type loci, a property that differentiates this mutant from other silencing mutants of S. pombe as well as of S. cerevisiae. This unique mutant phenotype defined a locus which we named sng1 (for silencing not governed). Chromatin analysis revealed a switching-dependent unfolding of the donor loci mat2P and mat3M in the sng1(-) mutant, as indicated by increased accessibility to the in vivo-expressed Escherichia coli dam methylase. Unexpectedly, cloning and sequencing identified the gene as the previously isolated DNA repair gene rhp6. RAD6, an rhp6 homolog in S. cerevisiae, is required for postreplication DNA repair and ubiquitination of histones H2A and H2B. This study implicates the Rad6/rhp6 protein in gene regulation and, more importantly, suggests that a transient window of opportunity exists to ensure the remodeling of chromatin structure during chromosome replication and recombination. We propose that the effects of the sng1(-)/rhp6(-) mutation on silencing are indirect consequences of changes in chromatin structure.","authors":"Singh J, Goel V, Klar AJ","authors_abbrev":"Singh J et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-08-26","publication_year":"1998","canto_session_key":"1c94c9b00e24bffa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-04 07:59:06","canto_approved_date":"2024-04-02 15:15:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-02-24 10:12:13","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.07c","SPMTR.01","SPBC1711.01c","SPAC3H5.06c","SPAC664.01c","SPAC1142.03c","SPBC409.03","SPBC23G7.17c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2016-04-04"},{"uniquename":"PMID:24569939","title":"Crystal structure of the eukaryotic translation initiation factor 2A from Schizosaccharomyces pombe.","citation":"J Struct Funct Genomics 2014 Sep;15(3):125-30","abstract":"The eukaryotic translation initiation factor 2A (eIF2A) was identified as a factor that stimulates the binding of methionylated initiator tRNA (Met-tRNA i (Met) ) to the 40S ribosomal subunit, but its physiological role remains poorly defined. Recently, eIF2A was shown to be involved in unconventional translation initiation from CUG codons and in viral protein synthesis under stress conditions where eIF2 is inactivated. We determined the crystal structure of the WD-repeat domain of Schizosaccharomyces pombe eIF2A at 2.5 Å resolution. The structure adopts a novel nine-bladed β-propeller fold. In contrast to the usual β-propeller proteins, the central channel of the molecule has the narrower opening on the bottom of the protein and the wider opening on the top. Highly conserved residues are concentrated in the positively-charged top face, suggesting the importance of this face for interactions with nucleic acids or other initiation factors.","doi":"10.1007/s10969-014-9177-y","authors":"Kashiwagi K, Ito T, Yokoyama S","authors_abbrev":"Kashiwagi K et al.","pubmed_publication_date":"Sep 2014","pubmed_entrez_date":"2014-02-27","publication_year":"2014","canto_session_key":"edb353510ed2465c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-06 12:15:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-06 09:22:58","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4B4.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-06","pdb_entries":[{"pdb_id":"3wj9","gene_chains":[{"gene_uniquename":"SPBC4B4.04","chain":"A/B","position":"2-412"}],"title":"Crystal structure of the eukaryotic initiation factor","entry_authors":"Kashiwagi K,Ito T,Yokoyama S","entry_authors_abbrev":"Kashiwagi K et al.","reference_uniquename":"PMID:24569939","experimental_method":"X-ray","resolution":"2.506"}]},{"uniquename":"PMID:28904333","title":"The Ino80 complex mediates epigenetic centromere propagation via active removal of histone H3.","citation":"Nat Commun 2017 Sep 13;8(1):529","abstract":"The centromere is the chromosomal locus at which the kinetochore is assembled to direct chromosome segregation. The histone H3 variant, centromere protein A (CENP-A), is known to epigenetically mark active centromeres, but the mechanism by which CENP-A propagates at the centromere, replacing histone H3, remains poorly understood. Using fission yeast, here we show that the Ino80 adenosine triphosphate (ATP)-dependent chromatin-remodeling complex, which removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-A Cnp1  chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1 Hrp1 . CENP-A Cnp1  chromatin actively recruits the Ino80 complex to centromeres to elicit eviction of histone H3-containing nucleosomes. Artificial targeting of Ino80 subunits to a non-centromeric DNA sequence placed in a native centromere enhances the spreading of CENP-A Cnp1  chromatin into the non-centromeric DNA. Based on these results, we propose that CENP-A Cnp1  chromatin employs the Ino80 complex to mediate the replacement of histone H3 with CENP-A Cnp1 , and thereby reinforces itself.The histone variant CENP-A marks active centromeres and replaces H3 at centromeres through a poorly understood mechanism. Here, the authors provide evidence that the chromatin remodeller Ino80 promotes CENP-A chromatin assembly at the centromere in fission yeast.","doi":"10.1038/s41467-017-00704-3","authors":"Choi ES, Cheon Y, Kang K, Lee D","authors_abbrev":"Choi ES et al.","pubmed_publication_date":"13 Sep 2017","pubmed_entrez_date":"2017-09-15","publication_year":"2017","canto_session_key":"9c941de80b158052","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Daeyoup Lee","canto_first_approved_date":"2019-03-07 16:01:31","canto_approved_date":"2025-09-03 17:01:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-06 14:07:39","canto_added_date":"2017-09-16 00:15:15","annotation_curators":[{"name":"Daeyoup Lee","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":40,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.17","SPAC1783.05","SPAC6B12.05c","SPCC1259.04","SPBC1861.01c","SPBC11B10.10c","SPAC144.02","SPAPB1A10.02","SPAC222.04c","SPAC29B12.01","SPCC970.12","SPAC664.02c"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2019-03-07"},{"uniquename":"Pfam:PF10018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1105.06","HGNC:17903"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:14643434","title":"Regulation of alternative replication bypass pathways at stalled replication forks and its effects on genome stability: a yeast model.","citation":"Mutat Res 2003 Nov 27;532(1-2):137-55","abstract":"Replication-blocking lesions result in increased genomic instability by stalling replication forks. Eukaryotic cells appear to have evolved several surveillance and repair/bypass mechanisms to ensure that replication can be resumed at these stalled forks. In the yeast Saccharomyces cerevisiae, the helicases Srs2 and Sgs1 appear to play a role in controlling the processing and stabilization of stalled replication forks. These proteins appear to be tightly regulated throughout the cell cycle and play a direct role in DNA-damage checkpoints. This allows the cells to determine the best mechanism to reestablish replication at the stalled fork: by shuttling the lesion into the RAD6-dependent pathway that can lead to error-free or error-prone bypass; or by using homologous recombination. Under conditions where both the RAD6-dependent pathway and recombination are disabled, the cells can bypass the lesion using a novel damage avoidance mechanism that is controlled by Mgs1. Replication fork bypass processes appear to be highly conserved within eukaryotes, with homologs for SGS1 and MGS1 found in both Schizosaccharomyces pombe and mammalian cells.","authors":"Barbour L, Xiao W","authors_abbrev":"Barbour L et al.","pubmed_publication_date":"27 Nov 2003","pubmed_entrez_date":"2003-12-04","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19293830","title":"Force- and kinesin-8-dependent effects in the spatial regulation of fission yeast microtubule dynamics.","citation":"Mol Syst Biol 2009;5:250","abstract":"Microtubules (MTs) are central to the organisation of the eukaryotic intracellular space and are involved in the control of cell morphology. For these purposes, MT polymerisation dynamics are tightly regulated. Using automated image analysis software, we investigate the spatial dependence of MT dynamics in interphase fission yeast cells with unprecedented statistical accuracy. We find that MT catastrophe frequencies (switches from polymerisation to depolymerisation) strongly depend on intracellular position. We provide evidence that compressive forces generated by MTs growing against the cell pole locally reduce MT growth velocities and enhance catastrophe frequencies. Furthermore, we find evidence for an MT length-dependent increase in the catastrophe frequency that is mediated by kinesin-8 proteins (Klp5/6). Given the intrinsic susceptibility of MT dynamics to compressive forces and the widespread importance of kinesin-8 proteins, we propose that similar spatial regulation of MT dynamics plays a role in other cell types as well. In addition, our systematic and quantitative data should provide valuable input for (mathematical) models of MT organisation in living cells.","doi":"10.1038/msb.2009.5","authors":"Tischer C, Brunner D, Dogterom M","authors_abbrev":"Tischer C et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-03-19","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25372384","title":"The MluI cell cycle box (MCB) motifs, but not damage-responsive elements (DREs), are responsible for the transcriptional induction of the rhp51+ gene in response to DNA replication stress.","citation":"PLoS One 2014;9(11):e111936","abstract":"DNA replication stress induces the transcriptional activation of rhp51+, a fission yeast recA homolog required for repair of DNA double strand breaks. However, the mechanism by which DNA replication stress activates rhp51+ transcription is not understood. The promoter region of rhp51+ contains two damage-responsive elements (DREs) and two MluI cell cycle box (MCB) motifs. Using luciferase reporter assays, we examined the role of these elements in rhp51+ transcription. The full-length rhp51+ promoter and a promoter fragment containing MCB motifs only, but not a fragment containing DREs, mediated transcriptional activation upon DNA replication stress. Removal of the MCB motifs from the rhp51+ promoter abolished the induction of rhp51+ transcription by DNA replication stress. Consistent with a role for MCB motifs in rhp51+ transcription activation, deletion of the MBF (MCB-binding factor) co-repressors Nrm1 and Yox1 precluded rhp51+ transcriptional induction in response to DNA replication stress. Using cells deficient in checkpoint signaling molecules, we found that the Rad3-Cds1/Chk1 pathway partially mediated rhp51+ transcription in response to DNA replication stress, suggesting the involvement of unidentified checkpoint signaling pathways. Because MBF is critical for G1/S transcription, we examined how the cell cycle affected rhp51+ transcription. The transcription of rhp51+ and cdc18+, an MBF-dependent G1/S gene, peaked simultaneously in synchronized cdc25-22 cells. Furthermore, DNA replication stress maintained transcription of rhp51+ similarly to cdc18+. Collectively, these results suggest that MBF and its regulators mediate rhp51+ transcription in response to DNA replication stress, and underlie rhp51+ transcription at the G1/S transition.","doi":"10.1371/journal.pone.0111936","authors":"Sartagul W, Zhou X, Yamada Y, Ma N, Tanaka K, Furuyashiki T, Ma Y","authors_abbrev":"Sartagul W et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-11-06","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-11-07 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC1259.13"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:18357653","title":"Canavanine resistance and the mechanism of arginine uptake in the fission yeast Schizosaccharomyces pombe.","citation":"J Gen Microbiol 1984 Dec;130(12):3265-73","abstract":"The mechanism of resistance to the arginine analogue L-canavanine, and of arginine uptake, were examined in the fission yeast Schizosaccharomyces pombe. Two mutants with increased resistance to canavanine were analysed genetically: both were double mutants, and in each case one mutation conferred resistance to canavanine, while the other enhanced this resistance. Evidence is presented that can 1.1 strains are defective in one system for arginine uptake, which presumably prevents entry of canavanine into the cell. This system operates in the wild-type whether the nitrogen source supplied is ammonium or glutamate. Double mutants carrying can 1.1 and an arginine requirement are unable to grow on ammonium medium even when supplied with exogenous argine, while growth can occur on glutamate plus arginine. This suggested the existence of a second uptake system for arginine which is absent during growth on ammonium, and direct measurements of the rates of arginine uptake under various conditions confirmed this. Our observations closely parallel those made on the budding yeast Saccharomyces cerevisiae. The ability to select for or against function of the can 1 gene should facilitate certain types of genetical analysis in S.pombe.","authors":"Fantes PA, Creanor J","authors_abbrev":"Fantes PA et al.","pubmed_publication_date":"Dec 1984","pubmed_entrez_date":"1984-12-01","publication_year":"1984","canto_session_key":"8d0f7efa36ce277f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-04 19:03:00","canto_approved_date":"2022-07-11 16:26:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-18 10:54:33","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.09c","SPBC18H10.20c","SPBC725.14","SPBC18H10.16"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-07-04"},{"uniquename":"PMID:36705602","title":"Unraveling the kinetochore nanostructure in Schizosaccharomyces pombe using multi-color SMLM imaging.","citation":"J Cell Biol 2023 Apr 03;222(4)","abstract":"The key to ensuring proper chromosome segregation during mitosis is the kinetochore (KT), a tightly regulated multiprotein complex that links the centromeric chromatin to the spindle microtubules and as such leads the segregation process. Understanding its architecture, function, and regulation is therefore essential. However, due to its complexity and dynamics, only its individual subcomplexes could be studied in structural detail so far. In this study, we construct a nanometer-precise in situ map of the human-like regional KT of Schizosaccharomyces pombe using multi-color single-molecule localization microscopy. We measure each protein of interest (POI) in conjunction with two references, cnp1CENP-A at the centromere and sad1 at the spindle pole. This allows us to determine cell cycle and mitotic plane, and to visualize individual centromere regions separately. We determine protein distances within the complex using Bayesian inference, establish the stoichiometry of each POI and, consequently, build an in situ KT model with unprecedented precision, providing new insights into the architecture.","doi":"10.1083/jcb.202209096","authors":"Virant D, Vojnovic I, Winkelmeier J, Endesfelder M, Turkowyd B, Lando D, Endesfelder U","authors_abbrev":"Virant D et al.","pubmed_publication_date":"03 Apr 2023","pubmed_entrez_date":"2023-01-27","publication_year":"2023","canto_session_key":"b13cc9bdeed9433e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ulrike Endesfelder","canto_first_approved_date":"2023-06-28 14:36:31","canto_approved_date":"2023-06-28 15:11:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-28 14:36:21","canto_added_date":"2023-01-28 01:15:04","annotation_curators":[{"name":"Ulrike Endesfelder","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"file_curator_name":"Ulrike Endesfelder","file_curator_role":"community","annotation_file_curators":[{"name":"Ulrike Endesfelder","community_curator":true,"annotation_count":9,"orcid":"0000-0002-7801-6278","file_type":"quantitative_gene_expression","file_name":"PMID_36705602_Virant_quantitative_expression.txt"}],"genes":["SPBC800.13","SPCC1020.02","SPCC1235.07","SPBC11C11.03","SPAC1783.03","SPAC29E6.04","SPAC589.08c","SPCC188.04c","SPBC409.04c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2023-06-28"},{"uniquename":"PMID:8593691","title":"Expression and analysis of the green fluorescent protein gene in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1995 Nov;28(6):585-8","abstract":"This report demonstrates that the Aequorea victoria green fluorescence protein (gfp) gene product will fluoresce in the fission yeast Schizosaccharomyces pombe when expressed from an episomal expression vector. Fluorescence was readily detectable at both the colony and single cell level. Application of fluorescence-activated cell sorting (FACS) techniques showed that gfp-expressing cells could be detected when they were as rare as 1% of a total yeast population. Quantitative analysis of gfp-expressing cells constituting as little as 5% of a total population was possible. These observations establish the suitability of the gfp gene for use in S. pombe and, in combination with FACS, offers an experimental strategy for quantitative analysis of gene expression in yeast populations.","authors":"Atkins D, Izant JG","authors_abbrev":"Atkins D et al.","pubmed_publication_date":"Nov 1995","pubmed_entrez_date":"1995-11-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6962314","title":"Extrachromosomal inheritance of nalidixic acid resistance in the petite negative yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1982;187(1):96-100","abstract":"Spontaneous mutants resistant to nalidixic acid (NAL) were isolated from the petite negative yeast Schizosaccharomyces pombe (S. pombe). One of these mutants, resistant to 200 micrograms/ml NAL, nalr-Y13, was characterized both genetically and biochemically. The extrachromosomal inheritance of this mutation was demonstrated both by mitotic segregation and by mitotic haploidization analysis. In the wild-type, NAL at a concentration of 100 micrograms/ml almost completely inhibits incorporation of [14C]adenine in total DNA as well as in mitochondrial DNA. In the NAL-resistant mutant both total DNA synthesis and mitochondrial DNA synthesis were resistant to the drug. These results are discussed in view of previously published findings on the close interaction between the two DNA synthesizing systems in S. pombe.","authors":"Massardo DR, Del Giudice L, Manna F, Wolf K","authors_abbrev":"Massardo DR et al.","pubmed_publication_date":"1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15647790","title":"The sensitivity of yeast and yeast-like cells to new lysosomotropic agents.","citation":"Cell Mol Biol Lett 2004;9(4A):675-83","abstract":"The lysosomotropic action of the compounds DM-11 and DMAL-12s against Saccharomyces cerevisiae, Schizosaccharomyces pombe and Candida albicans is species- and pH-dependent. At pH 6.0, DMAL-12s is less effective against S. cerevisiae and S. pombe but more effective against C. albicans than DM-11. At pH 8.0, DMAL-12s strongly inhibits the growth of S. cerevisiae but has only a marginal effect on the resistant C. albicans. S. pombe did not grow at pH 8.0. As shown by quinacrine accumulation, DM-11 causes a general intracellular acidification in all three species, while with DMAL-12s, the acidification is marginal. Morphological changes caused by DMAL-12s in S. cerevisiae affect the cell interior but not surface structures, while S. pombe cells exhibit a thickened and wrinkled cell wall, shrunken protoplast and \"grainy\" plasma membrane. A large number of blisters resembling lipid droplets were observed inside S. cerevisiae and S. pombe vacuoles. The high susceptibility of S. pombe cells to the action of DM-11 and DMAL-12s contrasts with the low sensitivity of S. pombe H+-ATPase to the agents. In our C. albicans isolate, DMAL 12s did not have an effect on cell morphology and appeared to be unable to penetrate the cells, especially at pH 8.0.","authors":"Krasowska A, Chmielewska L, Adamski R, Luczyński J, Witek S, Sigler K","authors_abbrev":"Krasowska A et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2005-01-14","publication_year":"2004","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10749926","title":"A mutation in gamma-tubulin alters microtubule dynamics and organization and is synthetically lethal with the kinesin-like protein pkl1p.","citation":"Mol Biol Cell 2000 Apr;11(4):1225-39","abstract":"Mitotic segregation of chromosomes requires spindle pole functions for microtubule nucleation, minus end organization, and regulation of dynamics. gamma-Tubulin is essential for nucleation, and we now extend its role to these latter processes. We have characterized a mutation in gamma-tubulin that results in cold-sensitive mitotic arrest with an elongated bipolar spindle but impaired anaphase A. At 30 degrees C cytoplasmic microtubule arrays are abnormal and bundle into single larger arrays. Three-dimensional time-lapse video microscopy reveals that microtubule dynamics are altered. Localization of the mutant gamma-tubulin is like the wild-type protein. Prediction of gamma-tubulin structure indicates that non-alpha/beta-tubulin protein-protein interactions could be affected. The kinesin-like protein (klp) Pkl1p localizes to the spindle poles and spindle and is essential for viability of the gamma-tubulin mutant and in multicopy for normal cell morphology at 30 degrees C. Localization and function of Pkl1p in the mutant appear unaltered, consistent with a redundant function for this protein in wild type. Our data indicate a broader role for gamma-tubulin at spindle poles in regulating aspects of microtubule dynamics and organization. We propose that Pkl1p rescues an impaired function of gamma-tubulin that involves non-tubulin protein-protein interactions, presumably with a second motor, MAP, or MTOC component.","authors":"Paluh JL, Nogales E, Oakley BR, McDonald K, Pidoux AL, Cande WZ","authors_abbrev":"Paluh JL et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-04-06","publication_year":"2000","canto_session_key":"729f627c0beaa1b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-08-31 19:04:34","canto_approved_date":"2026-01-30 12:34:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-29 18:03:02","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPBC32F12.04","SPAC3A11.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-08-31"},{"uniquename":"PMID:21471007","title":"Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo.","citation":"Mol Biol Cell 2011 Jun 01;22(11):1810-23","abstract":"Glucosidase II (GII) sequentially removes the two innermost glucose residues from the glycan (Glc(3)Man(9)GlcNAc(2)) transferred to proteins. GII also participates in cycles involving the lectin/chaperones calnexin (CNX) and calreticulin (CRT) as it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase (UGGT). GII is a heterodimer in which the α subunit (GIIα) bears the active site, and the β subunit (GIIβ) modulates GIIα activity through its C-terminal mannose 6-phosphate receptor homologous (MRH) domain. Here we report that, as already described in cell-free assays, in live Schizosaccharomyces pombe cells a decrease in the number of mannoses in the glycan results in decreased GII activity. Contrary to previously reported cell-free experiments, however, no such effect was observed in vivo for UGGT. We propose that endoplasmic reticulum α-mannosidase-mediated N-glycan demannosylation of misfolded/slow-folding glycoproteins may favor their interaction with the lectin/chaperone CNX present in S. pombe by prolonging the half-lives of the monoglucosylated glycans (S. pombe lacks CRT). Moreover, we show that even N-glycans bearing five mannoses may interact in vivo with the GIIβ MRH domain and that the N-terminal GIIβ G2B domain is involved in the GIIα-GIIβ interaction. Finally, we report that protists that transfer glycans with low mannose content to proteins have nevertheless conserved the possibility of displaying relatively long-lived monoglucosylated glycans by expressing GIIβ MRH domains with a higher specificity for glycans with high mannose content.","doi":"10.1091/mbc.E11-01-0019","authors":"Stigliano ID, Alculumbre SG, Labriola CA, Parodi AJ, D'Alessio C","authors_abbrev":"Stigliano ID et al.","pubmed_publication_date":"01 Jun 2011","pubmed_entrez_date":"2011-04-08","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18371314","title":"The Cid1 poly(U) polymerase.","citation":"Biochim Biophys Acta 2008 Apr;1779(4):286-94","abstract":"The Schizosaccharomyces pombe cytoplasmic protein Cid1 acts as a poly(U) polymerase (PUP). Polyadenylated actin mRNA, a target of this activity, is uridylated upon arrest in S phase and is likely to be one of many such Cid1 targets. This RNA uridylation pathway appears to be conserved, as Cid1 orthologs in Arabidopsis thaliana, Caenorhabditis elegans and humans display PUP activity either in vitro or in Xenopus laevis oocytes. Here, we review the literature on Cid1, other PUPs and uridylation, a conserved and previously under-appreciated mechanism of RNA regulation.","doi":"10.1016/j.bbagrm.2008.03.003","authors":"Rissland OS, Norbury CJ","authors_abbrev":"Rissland OS et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-03-29","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17243098","title":"Human Raf-1 proteins associate with Rad24 and Cdc25 in cell-cycle checkpoint pathway of fission yeast, Schizosaccharomyces pombe.","citation":"J Cell Biochem 2007 May 15;101(2):488-97","abstract":"Raf-1 is a serine/threonine protein kinase that connects cell surface receptor signals to nuclear transcription factors. By screening Schizosaccharomyces pombe (S. pombe) cDNA library, we isolated Rad24, which is a 14-3-3 homolog that is important in the DNA damage checkpoint in S. pombe, as a Raf-1 interacting protein. The interaction found in yeast was confirmed by co-immunoprecipitation. Furthermore, Cdc25, which has been known to bind to Rad24, also associated with Raf-1 and was phosphorylated in vitro by catalytically active Raf-1. However, in the presence of Raf-1, an interaction between Rad24 and Cdc25 was inhibited in triple hybrid assay, indicating that Raf-1 inhibits the interaction between Rad24 and Cdc25. An in vitro competition assay showed that the binding of Cdc25 and of Rad24 to Raf-1 is mutually exclusive. Western blots of whole cell lysates probed with polyclonal antibodies specific for tyrosine-15-phosphorylated Cdc2 showed that overproduction of Rad24 led to the dephosphorylation of tyrosine residue on Cdc2, which is known to be activated through dephosphorylation by Cdc25 phosphatase. Unexpectedly, overexpression of catalytically inactive mutant protein of Raf-1, S624A, also caused tyrosine dephosphorylation of Cdc2. Thus, these data suggest that Raf-1 may interfere with the role of Rad24 by competing with Rad24 for binding to Cdc25 or a direct phosphorylation of Cdc25, bypassing the checkpoint pathway in DNA repair through Cdc25 activation.","authors":"Lee M, Yoo HS","authors_abbrev":"Lee M et al.","pubmed_publication_date":"15 May 2007","pubmed_entrez_date":"2007-01-24","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26523839","title":"Cell-based screens and phenomics with fission yeast.","citation":"Crit Rev Biochem Mol Biol 2016;51(2):86-95","abstract":"Next-generation sequencing approaches have considerably advanced our understanding of genome function and regulation. However, the knowledge of gene function and complex cellular processes remains a challenge and bottleneck in biological research. Phenomics is a rapidly emerging area, which seeks to rigorously characterize all phenotypes associated with genes or gene variants. Such high-throughput phenotyping under different conditions can be a potent approach toward gene function. The fission yeast Schizosaccharomyces pombe (S. pombe) is a proven eukaryotic model organism that is increasingly used for genomewide screens and phenomic assays. In this review, we highlight current large-scale, cell-based approaches used with S. pombe, including computational colony-growth measurements, genetic interaction screens, parallel profiling using barcodes, microscopy-based cell profiling, metabolomic methods and transposon mutagenesis. These diverse methods are starting to offer rich insights into the relationship between genotypes and phenotypes.","doi":"10.3109/10409238.2015.1103205","authors":"Rallis C, Bähler J","authors_abbrev":"Rallis C et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-11-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-04 01:19:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33522486","title":"Surprising phenotypic diversity of cancer-associated mutations of Gly 34 in the histone H3 tail.","citation":"Elife 2021 Feb 01;10","abstract":"Sequencing of cancer genomes has identified recurrent somatic mutations in histones, termed oncohistones, which are frequently poorly understood. Previously we showed that fission yeast expressing only the H3.3G34R mutant identified in aggressive pediatric glioma had reduced H3K36 trimethylation and acetylation, increased genomic instability and replicative stress, and defective homology-dependent DNA damage repair. Here we show that surprisingly distinct phenotypes result from G34V (also in glioma) and G34W (giant cell tumors of bone) mutations, differentially affecting H3K36 modifications, subtelomeric silencing, genomic stability; sensitivity to irradiation, alkylating agents, and hydroxyurea; and influencing DNA repair. In cancer, only 1 of 30 alleles encoding H3 is mutated. Whilst co-expression of wild-type H3 rescues most G34 mutant phenotypes, G34R causes dominant hydroxyurea sensitivity, homologous recombination defects, and dominant subtelomeric silencing. Together, these studies demonstrate the complexity associated with different substitutions at even a single residue in H3 and highlight the utility of genetically tractable systems for their analysis.","doi":"10.7554/eLife.65369","authors":"Lowe BR, Yadav RK, Henry RA, Schreiner P, Matsuda A, Fernandez AG, Finkelstein D, Campbell M, Kallappagoudar S, Jablonowski CM, Andrews AJ, Hiraoka Y, Partridge JF","authors_abbrev":"Lowe BR et al.","pubmed_publication_date":"01 Feb 2021","pubmed_entrez_date":"2021-02-01","publication_year":"2021","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-02-03 01:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24247430","title":"Phosphorylation of the TOR ATP binding domain by AGC kinase constitutes a novel mode of TOR inhibition.","citation":"J Cell Biol 2013 Nov 25;203(4):595-604","abstract":"TOR (target of rapamycin) signaling coordinates cell growth, metabolism, and cell division through tight control of signaling via two complexes, TORC1 and TORC2. Here, we show that fission yeast TOR kinases and mTOR are phosphorylated on an evolutionarily conserved residue of their ATP-binding domain. The Gad8 kinase (AKT homologue) phosphorylates fission yeast Tor1 at this threonine (T1972) to reduce activity. A T1972A mutation that blocked phosphorylation increased Tor1 activity and stress resistance. Nitrogen starvation of fission yeast inhibited TOR signaling to arrest cell cycle progression in G1 phase and promoted sexual differentiation. Starvation and a Gad8/T1972-dependent decrease in Tor1 (TORC2) activity was essential for efficient cell cycle arrest and differentiation. Experiments in human cell lines recapitulated these yeast observations, as mTOR was phosphorylated on T2173 in an AKT-dependent manner. In addition, a T2173A mutation increased mTOR activity. Thus, TOR kinase activity can be reduced through AGC kinase-controlled phosphorylation to generate physiologically significant changes in TOR signaling.","doi":"10.1083/jcb.201305103","authors":"Hálová L, Du W, Kirkham S, Smith DL, Petersen J","authors_abbrev":"Hálová L et al.","pubmed_publication_date":"25 Nov 2013","pubmed_entrez_date":"2013-11-20","publication_year":"2013","canto_session_key":"819935350ed7d37f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 16:28:32","canto_approved_date":"2024-03-28 12:30:02","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-02-23 10:51:34","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":66,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4C5.02c","SPCC4G3.08","SPBC216.07c","SPCC576.15c","SPCC24B10.07","SPBC30D10.10c","SPBC23E6.08","SPAC1851.04c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-10-31"},{"uniquename":"PMID:38252660","title":"Metabolic stress-induced long ncRNA transcription governs the formation of meiotic DNA breaks in the fission yeast fbp1 gene.","citation":"PLoS One 2024;19(1):e0294191","abstract":"Meiotic recombination is a pivotal process that ensures faithful chromosome segregation and contributes to the generation of genetic diversity in offspring, which is initiated by the formation of double-strand breaks (DSBs). The distribution of meiotic DSBs is not uniform and is clustered at hotspots, which can be affected by environmental conditions. Here, we show that non-coding RNA (ncRNA) transcription creates meiotic DSBs through local chromatin remodeling in the fission yeast fbp1 gene. The fbp1 gene is activated upon glucose starvation stress, in which a cascade of ncRNA-transcription in the fbp1 upstream region converts the chromatin configuration into an open structure, leading to the subsequent binding of transcription factors. We examined the distribution of meiotic DSBs around the fbp1 upstream region in the presence and absence of glucose and observed several new DSBs after chromatin conversion under glucose starvation conditions. Moreover, these DSBs disappeared when cis-elements required for ncRNA transcription were mutated. These results indicate that ncRNA transcription creates meiotic DSBs in response to stress conditions in the fbp1 upstream region. This study addressed part of a long-standing unresolved mechanism underlying meiotic recombination plasticity in response to environmental fluctuation.","doi":"10.1371/journal.pone.0294191","authors":"Tsuruta Y, Senmatsu S, Oe H, Hoffman CS, Hirota K","authors_abbrev":"Tsuruta Y et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-01-22","publication_year":"2024","canto_session_key":"b1a9a1757736198f","canto_annotation_status":"APPROVED","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_first_approved_date":"2024-04-22 14:47:23","canto_approved_date":"2024-04-22 14:47:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-21 23:50:13","canto_added_date":"2024-01-23 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC21E11.03c","SPBC29B5.01","SPBC1198.14c","SPAC3A12.14"],"gene_count":4,"ltp_gene_count":0,"approved_date":"2024-04-22"},{"uniquename":"PMID:18845326","title":"Omenn syndrome is associated with mutations in DNA ligase IV.","citation":"J Allergy Clin Immunol 2008 Dec;122(6):1219-20","abstract":"","doi":"10.1016/j.jaci.2008.08.031","authors":"Grunebaum E, Bates A, Roifman CM","authors_abbrev":"Grunebaum E et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-10-11","publication_year":"2008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1183.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1842341","title":"Pulling the string: cell cycle regulation during Drosophila development.","citation":"Semin Cell Biol 1991 Aug;2(4):223-31","abstract":"The extensive cell proliferation which accompanies the development of multicellular organisms is co-ordinated with other developmental events. Cell cycle progression during embryogenesis is therefore controlled according to developmental stage and developmental fate. In Drosophila, entry into S phase is a constitutive, unregulated event until late in development. Entry into mitosis, however, is the first control point used for differential regulation, and the transcriptionally controlled expression of string (the Drosophila homologue of Schizosaccharomyces pombe cdc25+) directs the precise patterns of the embryonic cell divisions after the onset of morphogenesis. In contrast to string, cyclin proteins are produced in excess and their rate of accumulation does not regulate the time of mitosis.","authors":"Lehner CF","authors_abbrev":"Lehner CF","pubmed_publication_date":"Aug 1991","pubmed_entrez_date":"1991-08-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1427071","title":"Fission yeast genes involved in coupling mitosis to completion of DNA replication.","citation":"Genes Dev 1992 Nov;6(11):2035-46","abstract":"We have isolated fission yeast mutants that enter mitosis when DNA replication is blocked with hydroxyurea. The mutants define eight linkage groups, three of which consist of alleles of the rad1, rad3, and rad17 genes. Recently, these fission yeast genes have been shown to be required for radiation-induced cell cycle arrest, as is the budding yeast RAD9 gene. The other five genes are called hus (hydroxyurea sensitive) 1-5. We propose that these genes participate in an intracellular signal transduction pathway that monitors the completion of DNA replication and transmits information to the mitotic control protein cdc2. Mutations that bypass the requirement for cdc25 (an activator of the mitotic regulator cdc2) also uncouple mitosis from DNA replication. However, mitosis is blocked by inhibitors of DNA replication in strains in which the cdc25 gene has been deleted, indicating that although cdc25 influences the coupling of mitosis to the completion of DNA replication, it is not essential for this control.","authors":"Enoch T, Carr AM, Nurse P","authors_abbrev":"Enoch T et al.","pubmed_publication_date":"Nov 1992","pubmed_entrez_date":"1992-11-01","publication_year":"1992","canto_session_key":"697b0dd703952f05","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-23 16:26:22","canto_approved_date":"2021-05-19 15:53:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-22 16:46:56","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":41,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC1952.07","SPAC20G4.04c","SPCC18B5.03","SPAC24H6.05","SPAC14C4.13","SPBC216.05","SPAC2G11.12","SPAC30D11.13"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2015-07-23"},{"uniquename":"PMID:29720710","title":"A novel role for ATR/Rad3 in G1 phase.","citation":"Sci Rep 2018 May 02;8(1):6880","abstract":"Checkpoint kinases are important in cellular surveillance pathways that help cells to cope with DNA damage and protect their genomes. In cycling cells, DNA replication is one of the most sensitive processes and therefore all organisms carefully regulate replication initiation and progression. The checkpoint kinase ATR plays important roles both in response to DNA damage and replication stress, and ATR inhibitors are currently in clinical trials for cancer treatment. Therefore, it is important to understand the roles of ATR in detail. Here we show that the fission yeast homologue Rad3 and the human ATR regulate events also in G1 phase in an unperturbed cell cycle. Rad3Δ mutants or human cells exposed to ATR inhibitor in G1 enter S phase prematurely, which results in increased DNA damage. Furthermore, ATR inhibition in a single G1 reduces clonogenic survival, demonstrating that long-term effects of ATR inhibition during G1 are deleterious for the cell. Interestingly, ATR inhibition through G1 and S phase reduces survival in an additive manner, strongly arguing that different functions of ATR are targeted in the different cell-cycle phases. We propose that potential effects of ATR inhibitors in G1 should be considered when designing future treatment protocols with such inhibitors.","doi":"10.1038/s41598-018-25238-6","authors":"Bøe CA, Håland TW, Boye E, Syljuåsen RG, Grallert B","authors_abbrev":"Bøe CA et al.","pubmed_publication_date":"02 May 2018","pubmed_entrez_date":"2018-05-04","publication_year":"2018","canto_session_key":"531dc8857cfaf2f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Beata Grallert","canto_first_approved_date":"2018-09-06 13:55:42","canto_approved_date":"2018-09-06 13:55:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-08-28 17:13:20","canto_added_date":"2018-05-05 00:15:03","annotation_curators":[{"name":"Beata Grallert","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-09-06"},{"uniquename":"EMBL:AU009594","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15470240","title":"Schizosaccharomyces pombe Pmr1p is essential for cell wall integrity and is required for polarized cell growth and cytokinesis.","citation":"Eukaryot Cell 2004 Oct;3(5):1124-35","abstract":"The cps5-138 fission yeast mutant shows an abnormal lemon-like morphology at 28 degrees C in minimal medium and a lethal thermosensitive phenotype at 37 degrees C. Cell growth is completely inhibited at 28 degrees C in a Ca2+-free medium, in which the wild type is capable of growing normally. Under these conditions, actin patches become randomly distributed throughout the cell, and defects in septum formation and subsequent cytokinesis appear. The mutant cell is hypersensitive to the cell wall-digesting enzymatic complex Novozym234 even under permissive conditions. The gene SPBC31E1.02c, which complements all the mutant phenotypes described above, was cloned and codes for the Ca2+-ATPase homologue Pmr1p. The gene is not essential under optimal growth conditions but is required under conditions of low Ca2+ (<0.1 mM) or high temperature (>35 degrees C). The green fluorescent protein-tagged Cps5 proteins, which are expressed under physiological conditions (an integrated single copy with its own promoter in the cps5Delta strain), display a localization pattern typical of endoplasmic reticulum proteins. Biochemical analyses show that 1,3-beta-D-glucan synthase activity in the mutant is decreased to nearly half that of the wild type and that the mutant cell wall contains no detectable galactomannan when the cells are exposed to a Ca2+-free medium. The mutant acid phosphatase has an increased electrophoretic mobility, suggesting that incomplete protein glycosylation takes place in the mutant cells. These results indicate that S. pombe Pmr1p is essential for the maintenance of cell wall integrity and cytokinesis, possibly by allowing protein glycosylation and the polarized actin distribution to take place normally. Disruption and complementation analyses suggest that Pmr1p shares its function with a vacuolar Ca2+-ATPase homologue, Pmc1p (SPAPB2B4.04c), to prevent lethal activation of calcineurin for cell growth.","authors":"Cortés JC, Katoh-Fukui R, Moto K, Ribas JC, Ishiguro J","authors_abbrev":"Cortés JC et al.","pubmed_publication_date":"Oct 2004","pubmed_entrez_date":"2004-10-08","publication_year":"2004","canto_session_key":"ce16e022a8aca226","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-02-24 14:19:38","canto_approved_date":"2022-08-30 07:06:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-24 14:19:29","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":49,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC7D4.06c","SPBC31E1.02c","SPAPB2B4.04c","SPBC19G7.05c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2014-02-24"},{"uniquename":"PMID:39383179","title":"Location of polyadenylation sites within 3' untranslated regions is linked to biological function in yeast.","citation":"Genetics 2024 Oct 09;","abstract":"Expression of a typical yeast gene results in ∼50 3' mRNA isoforms that are distinguished by the locations of poly(A) sites within the 3' untranslated regions (3' UTRs). The location of poly(A) sites with respect to the translational termination codon varies considerably among genes, but whether this has any functional significance is poorly understood. Using hierarchical clustering of 3' UTRs, we identify eight classes of S. cerevisiae genes based on their poly(A) site locations. Genes involved in related biological functions (GO categories) are uniquely over-represented in six of these classes. Similar analysis of S. pombe genes reveals three classes of 3' UTRs, all of which show over-representation of functionally related genes. Remarkably, S. cerevisiae and S. pombe homologs share related patterns of poly(A) site locations. These observations suggest that the location of poly(A) sites within 3' UTRs has biological significance.","doi":"10.1093/genetics/iyae163","authors":"Geisberg JV, Moqtaderi Z, Struh K","authors_abbrev":"Geisberg JV et al.","pubmed_publication_date":"09 Oct 2024","pubmed_entrez_date":"2024-10-09","publication_year":"2024","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2024-10-09 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9695831","title":"Discovering the poles in yeast.","citation":"Trends Cell Biol 1998 Apr;8(4):163-7","abstract":"How cells generate and orientate polarized growth is of fundamental importance to understanding cell morphogenesis. The budding yeast Saccharomyces cerevisiae and the distantly related fission yeast Schizosaccharomyces pombe have both been used for genetic analysis of cell morphogenesis. Generation and maintenance of their cell shape require the formation of polarized growth sites and the correct localization of these growth sites on the cell surface with respect to other cellular structures. In this review, the authors discuss and compare the mechanisms used by the two yeasts to achieve polarized growth.","authors":"Mata J, Nurse P","authors_abbrev":"Mata J et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-08-08","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33654827","title":"QUEEN-based Spatiotemporal ATP Imaging in Budding and Fission Yeast.","citation":"Bio Protoc 2019 Aug 05;9(15):e3320","abstract":"Yeasts have provided an exceptional model for studying metabolism and bioenergetics in eukaryotic cells. Among numerous metabolites, adenosine triphosphate (ATP) is a major metabolite that is essential for all living organisms. Therefore, a clearer understanding of ATP dynamics in living yeast cells is important for deciphering cellular energy metabolism. However, none of the methods currently available to measure ATP, including biochemical analyses and ATP indicators, have been suitable for close examinations of ATP concentrations in yeast cells at the single cell level. Using the recently developed ATP biosensor QUEEN, which is suitable for yeasts and bacteria, a protocol was described herein to visualize ATP concentrations in living budding and fission yeast cells. This simple method enables the easy and reliable examination of ATP dynamics in various yeast mutants, thereby providing novel molecular insights into cellular energy metabolism.","doi":"10.21769/BioProtoc.3320","authors":"Takaine M","authors_abbrev":"Takaine M","pubmed_publication_date":"05 Aug 2019","pubmed_entrez_date":"2021-03-03","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-03-05 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10938120","title":"Protein kinase A and mitogen-activated protein kinase pathways antagonistically regulate fission yeast fbp1 transcription by employing different modes of action at two upstream activation sites.","citation":"Mol Cell Biol 2000 Sep;20(17):6426-34","abstract":"A significant challenge to our understanding of eukaryotic transcriptional regulation is to determine how multiple signal transduction pathways converge on a single promoter to regulate transcription in divergent fashions. To study this, we have investigated the transcriptional regulation of the Schizosaccharomyces pombe fbp1 gene that is repressed by a cyclic AMP (cAMP)-dependent protein kinase A (PKA) pathway and is activated by a stress-activated mitogen-activated protein kinase (MAPK) pathway. In this study, we identified and characterized two cis-acting elements in the fbp1 promoter required for activation of fbp1 transcription. Upstream activation site 1 (UAS1), located approximately 900 bp from the transcriptional start site, resembles a cAMP response element (CRE) that is the binding site for the atf1-pcr1 heterodimeric transcriptional activator. Binding of this activator to UAS1 is positively regulated by the MAPK pathway and negatively regulated by PKA. UAS2, located approximately 250 bp from the transcriptional start site, resembles a Saccharomyces cerevisiae stress response element. UAS2 is bound by transcriptional activators and repressors regulated by both the PKA and MAPK pathways, although atf1 itself is not present in these complexes. Transcriptional regulation of fbp1 promoter constructs containing only UAS1 or UAS2 confirms that the PKA and MAPK regulation is targeted to both sites. We conclude that the PKA and MAPK signal transduction pathways regulate fbp1 transcription at UAS1 and UAS2, but that the antagonistic interactions between these pathways involve different mechanisms at each site.","authors":"Neely LA, Hoffman CS","authors_abbrev":"Neely LA et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-08-11","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40388360","title":"Site-to-site mutational dissection of fission yeast cohesin reveals its dynamics.","citation":"G3 (Bethesda) 2025 May 19;","abstract":"Cohesin is a heteropentameric protein complex that holds sister chromatids together from S phase to anaphase. Its two structural maintenance of chromosomes (SMC) subunits form a heterodimer, consisting of an ATPase head domain and a hinge domain connected by long coiled coils. Kleisin subunit associates with the head. Here, using Schizosaccharomyces pombe, we genetically dissected cohesin dynamics based on the relationship between the mutations causing temperature-sensitive and their suppressor mutations. First, we identified suppressor mutations that could rescue the lethality caused by cohesin ATPase mutations. Mutations in the DNA binding domain of cohesin loader Mis4, or in cell-cycle genes encoding MBF transcription factor complex or Wee1 kinase, rescued both Psm1 and Psm3 ATPase mutants. Then, we performed targeted mutagenesis in both ATPase domains for single-amino-acid substitutions, that can rescue the lethality of a kleisin ts mutant at restrictive temperature. Comparison of mutations obtained in Psm1 and Psm3 ATPase domains revealed that analogous mutations in the two ATPase domains were frequently observed. Last, suppressors of a coiled-coil mutation were mapped in coiled coils, indicating that proper folding of coiled coils is critical for cohesin functions. Suppressors of a hinge interface mutation frequently located at the other hinge interface, indicating that the two cohesin hinge interfaces work collaboratively in hinge-hinge interactions. Overall, genetic dissection of the relationship between cohesin lethal mutations and their suppressor mutations reflects cohesin dynamics in vivo.","doi":"10.1093/g3journal/jkaf111","authors":"Wei Q, Wang L, Zhang Y, Abulimiti S, Wang J, Xu X","authors_abbrev":"Wei Q et al.","pubmed_publication_date":"19 May 2025","pubmed_entrez_date":"2025-05-19","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-05-19 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16407326","title":"Evolutionary-conserved telomere-linked helicase genes of fission yeast are repressed by silencing factors, RNAi components and the telomere-binding protein Taz1.","citation":"Nucleic Acids Res 2006;34(1):78-88","abstract":"In Schizosaccharomyces pombe the RNAi machinery and proteins mediating heterochromatin formation regulate the transcription of non-coding centromeric repeats. These repeats share a high sequence similarity with telomere-linked helicase (tlh) genes, implying an ancestral relationship between the two types of elements and suggesting that transcription of the tlh genes might be regulated by the same factors as centromeric repeats. Indeed, we found that mutants lacking the histone methyltransferase Clr4, the Pcu4 cullin, Clr7 or Clr8, accumulate high levels of tlh forward and reverse transcripts. Mutations and conditions perturbing histone acetylation had similar effects further demonstrating that the tlh genes are normally repressed by heterochromatin. In contrast, mutations in the RNAi factors Dcr1, Ago1 or Rdp1 led only to a modest derepression of the tlh genes indicating an alternate pathway recruits heterochromatin components to telomeres. The telomere-binding protein Taz1 might be part of such a redundant pathway, tlh transcripts being present at low levels in Deltataz1 mutants and at higher levels in Deltataz1 Deltadcr1 double mutants. Surprisingly, the chromodomain protein Chp1, a component of the Ago1-containing RITS complex, contributes more to tlh repression than Ago1, indicating the repressive effects of Chp1 are partially independent of RITS. The tlh genes are found in the subtelomeric regions of several other fungi raising the intriguing possibility of conserved regulation and function.","authors":"Hansen KR, Ibarra PT, Thon G","authors_abbrev":"Hansen KR et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-01-13","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.07c","SPCC188.13c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9838130","title":"Analysis of the ntp1+ gene, encoding neutral trehalase in the fission yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1998 Nov 26;1443(1-2):225-9","abstract":"We have cloned and sequenced the ntp1+ gene that codes for neutral trehalase in the fission yeast Schizosaccharomyces pombe. The ntp1+ gene product (Ntp1p) showed a 45-55% identity with neutral trehalases from other yeasts at the amino acid sequence level. However, in clear contrast to other neutral yeast trehalases so far characterized (which show two cAMP phospho-sites), only one consensus site for cAMP-dependent protein phosphorylation was found in Ntp1p. Northern blot hybridization experiments demonstrated that the Wis-Phh1/Sty1 MAP kinase cascade regulates ntp1+ expression during osmostress.","authors":"Soto T, Fernández J, Dominguez A, Vicente-Soler J, Cansado J, Gacto M","authors_abbrev":"Soto T et al.","pubmed_publication_date":"26 Nov 1998","pubmed_entrez_date":"1998-12-05","publication_year":"1998","canto_session_key":"68e96f70cad39cef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-04 12:56:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 12:05:39","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-04"},{"uniquename":"PMID:17725619","title":"Protective role and regulation of Rad9 from the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 2007 Oct;275(2):270-7","abstract":"To assess novel cellular roles and regulation of Rad9 in the fission yeast Schizosaccharomyces pombe, the full-length rad9 gene was cloned into the shuttle vector pRS316, generating pYFRad9. The rad9 mRNA level was significantly increased in the S. pombe cells harboring the plasmid pYFRad9, suggesting that the cloned rad9 gene is functioning. The S. pombe cells harboring pYFRad9 showed higher survival in the minimal media containing nitric oxide (NO)-generating sodium nitroprusside (SNP, 20 muM) and no nitrogen than the vector control cells. SNP and nitrogen starvation notably enhanced the synthesis of beta-galactosidase from the rad9-lacZ fusion gene in the Pap1-positive cells but not in the Pap1-negative cells. The rad9 mRNA level, detected by semi-quantitative reverse transcriptase (RT)-PCR, was elevated in the Pap1-positive cells but not in the Pap1-negative cells by SNP and nitrogen starvation. It was also increased only in the Pap1-positive cells by diethylmaleate, which activates Pap1. Collectively, the results imply that Rad9 plays a protective role against nitrosative and nutritional stress and is positively regulated by NO and nitrogen starvation in a Pap1-dependent manner.","authors":"Kang MH, Park EH, Lim CJ","authors_abbrev":"Kang MH et al.","pubmed_publication_date":"Oct 2007","pubmed_entrez_date":"2007-08-30","publication_year":"2007","canto_session_key":"63096e9d8eb5a1fc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-10 14:29:51","canto_approved_date":"2019-10-13 15:45:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-10 14:29:40","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-12-10"},{"uniquename":"PANTHER:PTHR12296","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:24321","SPCC297.05","HGNC:29134","HGNC:29044","HGNC:26079"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16285853","title":"Cell-cycle control of gene expression in budding and fission yeast.","citation":"Annu Rev Genet 2005;39:69-94","abstract":"Cell-cycle control of transcription seems to be a universal feature of proliferating cells, although relatively little is known about its biological significance and conservation between organisms. The two distantly related yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe have provided valuable complementary insight into the regulation of periodic transcription as a function of the cell cycle. More recently, genome-wide studies of proliferating cells have identified hundreds of periodically expressed genes and underlying mechanisms of transcriptional control. This review discusses the regulation of three major transcriptional waves, which roughly coincide with three main cell-cycle transitions (initiation of DNA replication, entry into mitosis, and exit from mitosis). I also compare and contrast the transcriptional regulatory networks between the two yeasts and discuss the evolutionary conservation and possible roles for cell cycle-regulated transcription.","authors":"Bähler J","authors_abbrev":"Bähler J","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-11-16","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32583742","title":"Geometry of the nuclear envelope determines its flexural stiffness.","citation":"Mol Biol Cell 2020 Jul 21;31(16):1815-1821","abstract":"During closed mitosis in fission yeast, growing microtubules push onto the nuclear envelope to deform it, which results in fission into two daughter nuclei. The resistance of the envelope to bending, quantified by the flexural stiffness, helps determine the microtubule-dependent nuclear shape transformations. Computational models of envelope mechanics have assumed values of the flexural stiffness of the envelope based on simple scaling arguments. The validity of these estimates is in doubt, however, owing to the complex structure of the nuclear envelope. Here, we performed computational analysis of the bending of the nuclear envelope under applied force using a model that accounts for envelope geometry. Our calculations show that the effective bending modulus of the nuclear envelope is an order of magnitude larger than a single membrane and approximately five times greater than the nuclear lamina. This large bending modulus is in part due to the 45 nm separation between the two membranes, which supports larger bending moments in the structure. Further, the effective bending modulus is highly sensitive to the geometry of the nuclear envelope, ranging from twofold to an order magnitude larger than the corresponding single membrane. These results suggest that spatial variations in geometry and mechanical environment of the envelope may cause a spatial distribution of flexural stiffness in the same nucleus. Overall, our calculations support the possibility that the nuclear envelope may balance significant mechanical stresses in yeast and in cells from higher organisms.","doi":"10.1091/mbc.E20-02-0163","authors":"Agrawal A, Lele TP","authors_abbrev":"Agrawal A et al.","pubmed_publication_date":"21 Jul 2020","pubmed_entrez_date":"2020-06-26","publication_year":"2020","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2020-06-27 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7593289","title":"Interaction of cdc2 and rum1 regulates Start and S-phase in fission yeast.","citation":"J Cell Sci 1995 Oct;108 ( Pt 10):3285-94","abstract":"The p34cdc2 kinase is essential for progression past Start in the G1 phase of the fission yeast cell cycle, and also acts in G2 to promote mitotic entry. Whilst very little is known about the G1 function of cdc2, the rum1 gene has recently been shown to encode an important regulator of Start in fission yeast, and a model for rum1 function suggests that it inhibits p34cdc2 activity. Here we present genetic data suggesting that rum1 maintains p34cdc2 in a pre-Start G1 form, inhibiting its activity until the cell achieves the critical mass required for Start, and find that in the absence of rum1 p34cdc2 has increased Start activity in vivo. It is also known that mutation of cdc2, or overexpression of rum1, can disrupt the dependency of S-phase upon mitosis, resulting in an extra round of S-phase in the absence of mitosis. We show that cdc2 and rum1 interact in this process, and describe dominant cdc2 mutants causing multiple rounds of S-phase in the absence of mitosis. We suggest that interaction of rum1 and cdc2 regulates Start, and this interaction is important for the regulation of S-phase within the cell cycle.","authors":"Labib K, Moreno S, Nurse P","authors_abbrev":"Labib K et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_session_key":"5c6714c7f2a5126a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-01 09:40:15","canto_approved_date":"2020-07-24 15:08:48","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-03-27 13:50:54","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC336.12c","SPBC582.03","SPBC32F12.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-09-01"},{"uniquename":"PMID:10956666","title":"Rad22 protein, a rad52 homologue in Schizosaccharomyces pombe, binds to DNA double-strand breaks.","citation":"J Biol Chem 2000 Nov 10;275(45):35607-11","abstract":"DNA double-strand breaks can be introduced by exogenous agents or during normal cellular processes. Genes belonging to the RAD52 epistasis group are known to repair these breaks in budding yeast. Among these genes, RAD52 plays a central role in homologous recombination and DNA double-strand break repair. Despite its importance, its mechanism of action is not yet clear. It is known, however, that the human homologue of Rad52 is capable of binding to DNA ends in vitro. Herein, we show that Rad22 protein, a Rad52 homologue in the fission yeast Schizosaccharomyces pombe, can similarly bind to DNA ends at double-strand breaks. This end-binding ability was demonstrated in vitro by electron microscopy and by protection from exonuclease attack. We also showed that Rad22 specifically binds near double-strand break associated with mating type switching in vivo by chromatin immunoprecipitation analysis. This is the first evidence that a recombinational protein directly binds to DNA double-strand breaks in vivo.","authors":"Kim WJ, Lee S, Park MS, Jang YK, Kim JB, Park SD","authors_abbrev":"Kim WJ et al.","pubmed_publication_date":"10 Nov 2000","pubmed_entrez_date":"2000-08-25","publication_year":"2000","canto_session_key":"3ffea0888f88442d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-02 12:17:35","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-02 12:12:04","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-02"},{"uniquename":"EMBL:AU011783","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24846945","title":"[Subcellular fluorescence localization analysis of all SAGA subunits in fission yeast (Schizosaccharomyces pombe)].","citation":"Yi Chuan 2014 Feb;36(2):169-80","abstract":"SAGA(Spt-Ada-Gcn5 Acetyltransferase complex) is a multi-subunit and conservative transcription complex, which is composed of 19 subunits in fission yeast and regulates the transcription of 10% genes in vivo. Through constructing in situ integrated fluorescence strains, we analyzed subcellular fluorescence localization of all SAGA subunits. Microscopic data showed localization manners could be sorted by 4 types, suggesting that these SAGA subunits may have additional functions besides transcriptional regulation. Subunit Sgf73 is the bridge that connects deubiquitination module and other SAGA modules, lacking of sgf73+ not only significantly reduced nuclear fluorescence localization (NFL) of deubiq-uitination subunits Ubp8, Sgf11, Sus1, but also affected NFL of acetylation subunits Gcn5, Sgf29, Ngg1, and the core structure subunit Spt7.The impact indicates that Sgf73 is important to maintain enzymatic function and stabilization of SAGA. Moreover, deletion of sgf73+ also caused a cytokinesis defect, which is characterized by a multi-nucleus and multi-septum phenotype. Overexpressing ace2+ and mid2+ in Dsgf73, which are key genes involved in septum degradation, showed that ace2+ could not rescue the defect, and mid2+ could only partially compensate for the deficiency, suggesting that Sgf73 may play a role in other pathways that affect cytokinesis.","authors":"Zhou X, Zhou N, Yu Y, Lv H","authors_abbrev":"Zhou X et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2014-05-22","publication_year":"2014","canto_session_key":"ba39d5c137c5e4ad","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22085934","title":"The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex.","citation":"EMBO J 2012 Jan 18;31(2):279-90","abstract":"The Dcp1:Dcp2 decapping complex catalyses the removal of the mRNA 5' cap structure. Activator proteins, including Edc3 (enhancer of decapping 3), modulate its activity. Here, we solved the structure of the yeast Edc3 LSm domain in complex with a short helical leucine-rich motif (HLM) from Dcp2. The motif interacts with the monomeric Edc3 LSm domain in an unprecedented manner and recognizes a noncanonical binding surface. Based on the structure, we identified additional HLMs in the disordered C-terminal extension of Dcp2 that can interact with Edc3. Moreover, the LSm domain of the Edc3-related protein Scd6 competes with Edc3 for the interaction with these HLMs. We show that both Edc3 and Scd6 stimulate decapping in vitro, presumably by preventing the Dcp1:Dcp2 complex from adopting an inactive conformation. In addition, we show that the C-terminal HLMs in Dcp2 are necessary for the localization of the Dcp1:Dcp2 decapping complex to P-bodies in vivo. Unexpectedly, in contrast to yeast, in metazoans the HLM is found in Dcp1, suggesting that details underlying the regulation of mRNA decapping changed throughout evolution.","doi":"10.1038/emboj.2011.408","authors":"Fromm SA, Truffault V, Kamenz J, Braun JE, Hoffmann NA, Izaurralde E, Sprangers R","authors_abbrev":"Fromm SA et al.","pubmed_publication_date":"18 Jan 2012","pubmed_entrez_date":"2011-11-17","publication_year":"2012","canto_session_key":"8b91b02e39a87d36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-16 17:44:42","canto_approved_date":"2023-09-02 14:28:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-16 17:44:36","canto_added_date":"2012-06-12 03:08:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18E5.11c","SPBC3B9.21","SPBC800.09","SPAC19A8.12","SPAC18G6.09c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2023-02-16","pdb_entries":[{"pdb_id":"4a54","gene_chains":[{"gene_uniquename":"SPAC19A8.12","chain":"B","position":"242-291"},{"gene_uniquename":"SPBC18E5.11c","chain":"A","position":"1-94"}],"title":"Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6","entry_authors":"Fromm SA,Truffault V,Kamenz J,Braun JE,Hoffmann NA,Izaurralde E,Sprangers R","entry_authors_abbrev":"Fromm SA et al.","reference_uniquename":"PMID:22085934","experimental_method":"NMR","resolution":""},{"pdb_id":"4a53","gene_chains":[{"gene_uniquename":"SPBC18E5.11c","chain":"A","position":"1-121"}],"title":"Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6","entry_authors":"Fromm SA,Truffault V,Kamenz J,Braun JE,Hoffmann NA,Izaurralde E,Sprangers R","entry_authors_abbrev":"Fromm SA et al.","reference_uniquename":"PMID:22085934","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:31748520","title":"Chaperone-mediated ordered assembly of the SAGA and NuA4 transcription co-activator complexes in yeast.","citation":"Nat Commun 2019 Nov 20;10(1):5237","abstract":"Transcription initiation involves the coordinated activities of large multimeric complexes, but little is known about their biogenesis. Here we report several principles underlying the assembly and topological organization of the highly conserved SAGA and NuA4 co-activator complexes, which share the Tra1 subunit. We show that Tra1 contributes to the overall integrity of NuA4, whereas, within SAGA, it specifically controls the incorporation of the de-ubiquitination module (DUB), as part of an ordered assembly pathway. Biochemical and functional analyses reveal the mechanism by which Tra1 specifically interacts with either SAGA or NuA4. Finally, we demonstrate that Hsp90 and its cochaperone TTT promote Tra1 de novo incorporation into both complexes, indicating that Tra1, the sole pseudokinase of the PIKK family, shares a dedicated chaperone machinery with its cognate kinases. Overall, our work brings mechanistic insights into the assembly of transcriptional complexes and reveals the contribution of dedicated chaperones to this process.","doi":"10.1038/s41467-019-13243-w","authors":"Elías-Villalobos A, Toullec D, Faux C, Séveno M, Helmlinger D","authors_abbrev":"Elías-Villalobos A et al.","pubmed_publication_date":"20 Nov 2019","pubmed_entrez_date":"2019-11-22","publication_year":"2019","canto_session_key":"ddb5158a6caf4996","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dom Helmlinger","canto_first_approved_date":"2023-09-06 13:43:23","canto_approved_date":"2026-06-17 13:11:28","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-09-05 09:24:06","canto_added_date":"2019-12-13 14:36:57","annotation_curators":[{"name":"Dom Helmlinger","community_curator":true,"annotation_count":71,"orcid":"0000-0003-1501-0423","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.04c","SPCC965.07c","SPBC25H2.11c","SPAC1F5.11c","SPAC57A10.14","SPCC1795.08c","SPBC216.07c","SPAC977.12","SPBC21D10.10","SPAC4D7.10c","SPBC1604.17c","SPBC32H8.12c","SPAC458.03","SPAC637.12c","SPBC30D10.10c","SPBC887.18c","SPCC830.05c","SPAC1006.02","SPAC17G8.07","SPCC1884.01","SPCC569.05c","SPAC9G1.13c","SPCC622.13c","SPAC6F6.09","SPBC21B10.05c","SPAC23H4.12","SPBP16F5.03c","SPBC16A3.19","SPBP23A10.08","SPAC3G9.08","SPCC126.04c"],"gene_count":31,"ltp_gene_count":22,"approved_date":"2023-09-06"},{"uniquename":"PMID:9090842","title":"Functional characterization of Schizosaccharomyces pombe genes cloned in potassium transport defective yeast strains.","citation":"Folia Microbiol (Praha) 1996;41(1):105-6","abstract":"","authors":"Lichtenberg-Fraté H, Reid JD, Heyer M, Höfer M","authors_abbrev":"Lichtenberg-Fraté H et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"6e28338e69d9210a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-11-08 13:04:59","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-11-08 13:04:51","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3F10.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-11-08"},{"uniquename":"PMID:23103764","title":"Nucleosome positioning and transcription: fission yeast CHD remodellers make their move.","citation":"EMBO J 2012 Nov 28;31(23):4371-2","abstract":"Regularly positioned nucleosomes are a common feature of 5' ends of most eukaryotic genes. A series of three studies, Shim et al (2012) and Pointner et al (2012) in this issue of The EMBO Journal and Hennig et al (2012) in EMBO Reports, now show that in the fission yeast Schizosaccharomyces pombe this intragenic nucleosome positioning mostly requires two ATP-dependent remodellers of the CHD family, Hrp1 and Hrp3. Moreover, they suggest that Hrp1- and Hrp3-dependent nucleosome spacing contributes to the silencing of cryptic antisense transcription.","doi":"10.1038/emboj.2012.284","authors":"Touat-Todeschini L, Hiriart E, Verdel A","authors_abbrev":"Touat-Todeschini L et al.","pubmed_publication_date":"28 Nov 2012","pubmed_entrez_date":"2012-10-30","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19044021","title":"[Conserved telomeric-end structures among fission yeast and humans].","citation":"Tanpakushitsu Kakusan Koso 2008 Nov;53(14):1850-7","abstract":"","authors":"Miyoshi T, Ishikawa F","authors_abbrev":"Miyoshi T et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-12-03","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11470243","title":"Very-long-chain fatty acid-containing phospholipids accumulate in fatty acid synthase temperature-sensitive mutant strains of the fission yeast Schizosaccharomyces pombe fas2/lsd1.","citation":"Biochim Biophys Acta 2001 Jun 29;1532(3):223-33","abstract":"Fission yeast lsd1 strains show aberrant mitosis with a lsd phenotype, large and small daughter nuclei, and a very thick septum, the phenotypic expression being temperature-sensitive. The lsd1(+) gene is the homologue of the budding yeast FAS2 gene encoding the fatty acid synthase alpha-subunit as reported previously (S. Saitoh, K. Takahashi, K. Nabeshima, Y. Yamashita, Y. Nakaseko, A. Hirata, M. Yanagida, J. Cell Biol. 134 (1996) 949--961). In this paper, lsd1 is considered to represent fas2. Here, three fas2 strains were investigated and found to have missense point mutations at different sites in the gene encoding the alpha-subunit of fatty acid synthase. The mutation affected only slightly the enzymatic activities monitored in vitro. Unexpectedly, abnormal phospholipids, phosphatidylcholine and phosphatidylethanolamine, both of which contain a very-long-chain fatty acyl residue (1-melissoyl-2-oleolyl-sn-glycero-3-phosphocholine and 1-melissoyl-2-oleolyl-sn-glycero-3-phosphoethanolamine), accumulated in fas2 strains in a temperature-sensitive manner. Rescue of the fas2 strains by addition of palmitate to the medium at restrictive temperature was accompanied by disappearance of these abnormal phospholipids. Accumulation of these lipids in membranes may cause alteration of various cellular functions.","authors":"Yokoyama K, Saitoh S, Ishida M, Yamakawa Y, Nakamura K, Inoue K, Taguchi R, Tokumura A, Nishijima M, Yanagida M, Setaka M","authors_abbrev":"Yokoyama K et al.","pubmed_publication_date":"29 Jun 2001","pubmed_entrez_date":"2001-07-27","publication_year":"2001","canto_session_key":"d6acad95cdc1056","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-06-12 13:07:36","canto_approved_date":"2022-02-01 18:09:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-23 16:37:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-06-12"},{"uniquename":"PMID:6294466","title":"Construction of a Schizosaccharomyces pombe gene bank in a yeast bacterial shuttle vector and its use to isolate genes by complementation.","citation":"Mol Gen Genet 1982;187(2):326-9","abstract":"A gene bank of partial Sau3A restriction fragments of S. pombe DNA has been constructed in the plasmid vector, pDB248', which is capable of high frequency transformation of S. pombe. Procedures are described which enable plasmids to be recovered from S. pombe by their reintroduction into E. coli. These methods have been used to detect the S. pombe genes lys 1+, ade 6+ and his 2+ in the gene bank by complementation of mutant gene functions, and to physically isolate the lys 1+ gene.","authors":"Beach D, Piper M, Nurse P","authors_abbrev":"Beach D et al.","pubmed_publication_date":"1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8522609","title":"Fission yeast cell morphogenesis: identification of new genes and analysis of their role during the cell cycle.","citation":"J Cell Biol 1995 Dec;131(6 Pt 1):1529-38","abstract":"To identify new genes involved in the control of cell morphogenesis in the fission yeast Schizosaccharomyces pombe we have visually screened for temperature-sensitive mutants that show defects in cell morphology. We have isolated and characterized 64 mutants defining 19 independent genes, 10 of which have not been previously described. One class of mutants, defining 12 orb genes, become round and show a complete loss of cell polarity. A second class of mutants exhibits branched or bent morphologies. These mutants show defects in either selection of the growth site, defining two tea genes, or in the maintenance of growth direction, defining five ban genes. Immunofluorescence analysis of these morphological mutants shows defects in the organization of the microtubule and actin cytoskeleton. These defects include shortened, bundled, and asymmetrically localized microtubules and enlarged and mislocalized actin patches. Analysis of the mutant phenotypes has allowed us to order the genes into four groups according to their function during the cell cycle: genes required for the maintenance of cell polarity throughout the cell cycle; genes necessary only for the reestablishment of cell polarity after mitosis and not for maintaining cell polarity once it is established; genes essential for the transition from monopolar to bipolar growth and genes that severe as 'polarity markers'.","authors":"Verde F, Mata J, Nurse P","authors_abbrev":"Verde F et al.","pubmed_publication_date":"Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"b6b93831c9879682","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-02-21 14:29:40","canto_approved_date":"2022-12-13 10:38:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-12 15:26:02","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16C4.09","SPBC800.05c","SPCC1223.06","SPAC2E1P5.04c","SPBC1604.20c","SPBC1604.14c","SPAC17G8.14c","SPAC26F1.10c","SPBC17F3.02","SPCC1739.11c","SPAC821.12","SPAC17H9.09c","SPBC11B10.09","SPCC1840.02c"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2018-02-21"},{"uniquename":"PMID:23738021","title":"A genome-wide screening of potential target genes to enhance the antifungal activity of micafungin in Schizosaccharomyces pombe.","citation":"PLoS One 2013;8(5):e65904","abstract":"Micafungin is a non-reversible inhibitor of 1, 3-β-D-glucan synthase and interferes with fungal cell wall synthesis. Clinically, micafungin has been shown to be efficacious for the treatment of invasive candidiasis and invasive aspergillosis. However, considering its relatively restricted antifungal spectrum, combination therapy with micafungin plus other agents should be considered in critically ill patients. To identify potential therapeutic targets for syncretic drug combinations that potentiate micafungin action, we carried out a genome-wide screen for altered sensitivity to micafungin by using the model yeast Schizosaccharomyces pombe mutant library. We confirmed that 159 deletion strains in the library are micafungin sensitive and classified them into various functional categories, including cell wall biosynthesis, gene expression and chromatin remodeling, membrane trafficking, signaling transduction, ubiquitination, ergosterol biosynthetic process and a variety of other known functions or still unknown functions. On the other hand, we also investigated the growth inhibitory activities of some well-known drugs in combination with micafungin including antifungal drug amphotericin B, fluconazole and immunosuppressive drug FK506. We found that amphotericin B in combination with micafungin showed a more potent inhibitory activity against wild-type cells than that of micafungin alone, whereas fluconazole in combination with micafungin did not. Also, the immunosuppressive drug FK506 showed synergistic inhibitory effect with micafungin on the growth of wild-type cells, whereas it decreased the inhibitory effect of micafungin in Δpmk1 cells, a deletion mutant of the cell wall integrity mitogen-activated protein kinase (MAPK) Pmk1. Altogether, our findings provide useful information for new potential drug combinations in the treatment of fungal infections.","doi":"10.1371/journal.pone.0065904","authors":"Zhou X, Ma Y, Fang Y, gerile W, Jaiseng W, Yamada Y, Kuno T","authors_abbrev":"Zhou X et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-06-06","publication_year":"2013","canto_session_key":"6f23dfe41c518df8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-24 13:58:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-24 13:58:45","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":147,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_23738021_phaf.tsv"}],"genes":["SPCC1450.03","SPBC29A3.14c","SPAC3A12.10","SPAC13A11.01c","SPBC19G7.10c","SPAC227.01c","SPAC27E2.07","SPAC29A4.18","SPCC24B10.08c","SPBC21B10.03c","SPCC1322.03","SPCC18.06c","SPAC11G7.04","SPBC119.08","SPAC823.05c","SPBP4H10.04","SPAC630.14c","SPAC5D6.09c","SPCC645.07","SPCC970.07c","SPCC31H12.08c","SPAC17A5.04c","SPCC1020.08","SPAC3G9.08","SPAC1F5.08c","SPAC19G12.02c","SPBC1711.16","SPAC13C5.02","SPBC19C2.05","SPBC543.07","SPBC1105.04c","SPAC16.01","SPAC3H8.05c","SPAC17G8.11c","SPAC18B11.07c","SPAC23D3.09","SPBC336.01","SPCC364.03","SPAC3G6.01","SPAC17G8.14c","SPAC2G11.03c","SPAC15A10.03c","SPCC584.11c","SPCP1E11.04c","SPBC146.13c","SPBC800.04c","SPCC576.11","SPAC6G9.03c","SPBC21C3.19","SPCC16C4.20c","SPAC31G5.19","SPAC3A12.13c","SPBC1D7.04","SPAC3H5.10","SPBC23G7.08c","SPBC32F12.11","SPCC794.12c","SPBC21B10.13c","SPAC17H9.19c","SPAC31A2.02","SPAC8F11.10c","SPAC11G7.02","SPAC688.11","SPCC825.01","SPAC227.07c","SPBC16C6.04","SPAC17A5.14","SPAC644.14c","SPCC188.07","SPBP16F5.07","SPAC5D6.05","SPBC776.17","SPBP16F5.05c","SPAC22A12.07c","SPAC23A1.16c","SPAC22F8.02c"],"gene_count":76,"ltp_gene_count":2,"approved_date":"2014-07-24"},{"uniquename":"PMID:24823650","title":"RNA mimicry by the fap7 adenylate kinase in ribosome biogenesis.","citation":"PLoS Biol 2014 May;12(5):e1001860","abstract":"During biogenesis of the 40S and 60S ribosomal subunits, the pre-40S particles are exported to the cytoplasm prior to final cleavage of the 20S pre-rRNA to mature 18S rRNA. Amongst the factors involved in this maturation step, Fap7 is unusual, as it both interacts with ribosomal protein Rps14 and harbors adenylate kinase activity, a function not usually associated with ribonucleoprotein assembly. Human hFap7 also regulates Cajal body assembly and cell cycle progression via the p53-MDM2 pathway. This work presents the functional and structural characterization of the Fap7-Rps14 complex. We report that Fap7 association blocks the RNA binding surface of Rps14 and, conversely, Rps14 binding inhibits adenylate kinase activity of Fap7. In addition, the affinity of Fap7 for Rps14 is higher with bound ADP, whereas ATP hydrolysis dissociates the complex. These results suggest that Fap7 chaperones Rps14 assembly into pre-40S particles via RNA mimicry in an ATP-dependent manner. Incorporation of Rps14 by Fap7 leads to a structural rearrangement of the platform domain necessary for the pre-rRNA to acquire a cleavage competent conformation.","doi":"10.1371/journal.pbio.1001860","authors":"Loc'h J, Blaud M, Réty S, Lebaron S, Deschamps P, Bareille J, Jombart J, Robert-Paganin J, Delbos L, Chardon F, Zhang E, Charenton C, Tollervey D, Leulliot N","authors_abbrev":"Loc'h J et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2014-05-15","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3H5.05c","SPBC18H10.13","SPCC830.11c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:2020547","title":"Identification of a gene encoding the predicted ribosomal protein L7b divergently transcribed from POL1 in fission yeast Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1991 Mar 11;19(5):1099-104","abstract":"A 0.85 Kb RNA molecule is transcribed in the region upstream from the 5'-end of the S. pombe POL1 gene encoding the catalytic subunit of DNA polymerase alpha. The nucleotide sequence of the DNA region hybridizing with the 0.85 Kb transcript allowed us to identify an open reading frame coding for a predicted peptide which shows 50% identity with the rat ribosomal protein L7 and which is transcribed divergently from POL1. We have named this gene RPL7b because of the existence in S. pombe of a different sequence, named RPL7, which also codes for a putative protein showing homology with the rat ribosomal protein L7. The RPL7b gene includes a 291 bp-long intron containing the sequences necessary for intron excision and RNA splicing in S. pombe. The precise location of the intron was established by amplification and sequencing of a partial cDNA copy of the mRNA, whereas the initiation site of transcription was determined by reverse transcription of the 5' region of the mRNA. The 320 bp separating the starting methionine codons of RPL7b and POL1 genes should contain the signals necessary for their divergent transcription and regulation. The sequence 5'-AAGACAGTCACA-3', whose primary structure is homologous to a conserved block present in the 5'-untranscribed regions of other S. pombe genes of ribosomal proteins, is located about 50 bp upstream the transcription initiation site of RPL7b.","authors":"Damagnez V, de Recondo AM, Baldacci G","authors_abbrev":"Damagnez V et al.","pubmed_publication_date":"11 Mar 1991","pubmed_entrez_date":"1991-03-11","publication_year":"1991","canto_session_key":"facd733cc1d96a6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:32:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 17:17:35","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3H5.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-25"},{"uniquename":"PMID:18256544","title":"Unconventional effects of UVA radiation on cell cycle progression in S. pombe.","citation":"Cell Cycle 2008 Mar 01;7(5):611-22","abstract":"UVA radiation, the most abundant solar UV radiation reaching Earth's surface, induces oxidative stress through formation of reactive oxygen species (ROS) that can damage different cell components. Because of the broad spectrum of the possible targets of ROS, the cellular response to this radiation is complex. While extensive studies have allowed dissecting the effects of UVB, UVC and gamma radiations on cell cycle progression, few studies have dealt with the effect of UVA so far. Here we use Schizosaccharomyces pombe as a model organism to study biological effects of UVA radiation in living organisms. Through analysis of cell cycle progression in different mutant backgrounds we demonstrate that UVA delays cell cycle progression in G(2) cells in a dose dependent manner. However, despite Chk1 phosphorylation and in contrast to treatments with others genotoxic agents, this cell cycle delay is only partially dependent on DNA integrity checkpoint pathway. We also demonstrate that UVA irradiation of S phase cells slows down DNA replication in a checkpoint independent manner, activates Chk1 to prevent entry into abnormal mitosis and induces formation of Rad22 (homologue to human Rad52) foci. This indicates that DNA structure integrity is challenged. Furthermore, the cell cycle delay observed in checkpoint mutants exposed to UVA is not abolished when stress response pathway is inactivated or when down regulation of protein synthesis is prevented. In conclusion, fission yeast is a useful model to dissect the fundamental molecular mechanisms involved in UVA response that may contribute to skin cancer and aging.","authors":"Dardalhon D, Angelin AR, Baldacci G, Sage E, Francesconi S","authors_abbrev":"Dardalhon D et al.","pubmed_publication_date":"01 Mar 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2834104","title":"Primary structure of the ribosomal protein gene S6 from Schizosaccharomyces pombe.","citation":"Curr Genet 1988;13(1):57-63","abstract":"We have determined the nucleotide sequence of a ribosomal protein gene which codes for the ribosomal protein S6 (rps6). The sequence analysis revealed that the gene comprises 239 amino acids, giving rise to a basic protein with a molecular weight of 27,502 Da. The product of this gene is the equivalent of the ribosomal protein S10 from Saccharomyces cerevisiae. Northern analyses and S1 mapping of both the 5' and the 3' end of the transcripts of this gene show that it is transcribed into three distinct transcripts with different sizes and heterogeneous termini. In the DNA region flanking the coding sequence, several conserved elements are present that may be involved in the transcription initiation and termination.","authors":"Gross T, Nischt R, Gatermann K, Swida U, Käufer NF","authors_abbrev":"Gross T et al.","pubmed_publication_date":"1988","pubmed_entrez_date":"1988-01-01","publication_year":"1988","canto_session_key":"b46b284261275df3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-09-07 11:33:33","canto_approved_date":"2020-09-07 11:33:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-07 11:33:27","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13G6.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2020-09-07"},{"uniquename":"PMID:16864655","title":"Assembly of the cytokinetic contractile ring from a broad band of nodes in fission yeast.","citation":"J Cell Biol 2006 Jul 31;174(3):391-402","abstract":"We observed live fission yeast expressing pairs of functional fluorescent fusion proteins to test the popular model that the cytokinetic contractile ring assembles from a single myosin II progenitor or a Cdc12p-Cdc15p spot. Under our conditions, the anillin-like protein Mid1p establishes a broad band of small dots or nodes in the cortex near the nucleus. These nodes mature by the addition of conventional myosin II (Myo2p, Cdc4p, and Rlc1p), IQGAP (Rng2p), pombe Cdc15 homology protein (Cdc15p), and formin (Cdc12p). The nodes coalesce laterally into a compact ring when Cdc12p and profilin Cdc3p stimulate actin polymerization. We did not observe assembly of contractile rings by extension of a leading cable from a single spot or progenitor. Arp2/3 complex and its activators accumulate in patches near the contractile ring early in anaphase B, but are not concentrated in the contractile ring and are not required for assembly of the contractile ring. Their absence delays late steps in cytokinesis, including septum formation and cell separation.","authors":"Wu JQ, Sirotkin V, Kovar DR, Lord M, Beltzner CC, Kuhn JR, Pollard TD","authors_abbrev":"Wu JQ et al.","pubmed_publication_date":"31 Jul 2006","pubmed_entrez_date":"2006-07-26","publication_year":"2006","canto_session_key":"aaf219ab662cb08b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-01-11 16:34:44","canto_approved_date":"2024-04-05 15:11:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-11 16:34:36","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":46,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.03","SPAP8A3.08","SPCC645.05c","SPAC4F10.15c","SPAC1F5.04c","SPAC20G8.05c","SPAC4A8.15c","SPCC4B3.15","SPBC146.13c","SPAC926.03","SPAC4A8.05c","SPAC4F8.13c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2019-01-11"},{"uniquename":"PMID:23851719","title":"Spt6 prevents transcription-coupled loss of posttranslationally modified histone H3.","citation":"Sci Rep 2013;3:2186","abstract":"The tail of histone H3 is an ideal medium for storing epigenetic information because displacement of histone H3 is heavily restricted during transcription. To maintain the locus-specific modifications of histone H3, histone molecules should be retained locally at the original position through multiple rounds of transcription. Here, we found that fission yeast Spt6, a highly conserved RNA polymerase II-interacting histone H3-H4 chaperone, is essential for the maintenance of Lys-4 and Lys-9 methylation of histone H3 in euchromatin and heterochromatin, respectively. In euchromatin, loss of Lys-4 methylated histone H3 and deposition of newly synthesized Lys-56 acetylated histone H3 induced by Spt6 inactivation were coupled with transcription. While in heterochromatin, Spt6 prevents histone turnover and cryptic transcription in parallel with Clr3 histone deacetylase. We propose that Spt6 retains posttranslationally modified histone H3 during transcription to maintain epigenome integrity.","doi":"10.1038/srep02186","authors":"Kato H, Okazaki K, Iida T, Nakayama J, Murakami Y, Urano T","authors_abbrev":"Kato H et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-16","publication_year":"2013","canto_session_key":"89991a632fbaa28c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroaki Kato","canto_first_approved_date":"2016-02-09 11:08:45","canto_approved_date":"2022-03-18 14:10:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-01 15:48:04","canto_added_date":"2013-07-18 07:13:56","annotation_curators":[{"name":"Hiroaki Kato","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPBC428.08c","SPCC306.04c","SPAC1F7.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-02-09"},{"uniquename":"PMID:21289046","title":"On the connection between RNAi and heterochromatin at centromeres.","citation":"Cold Spring Harb Symp Quant Biol 2010;75:275-83","abstract":"RNA interference (RNAi) is a conserved silencing mechanism whereby double-strand RNA induces specific down-regulation of homologous sequences. In the fission yeast Schizosaccharomyces pombe, centromeric heterochromatin assembly is an RNAi-dependent process. Noncoding RNAs transcribed from pericentromeric repeat sequences are processed into short interfering RNAs (siRNAs) that direct the Argonaute-containing RNA-induced transcriptional silencing (RITS) effector complex to homologous nascent transcripts. RITS is required for H3K9 methylation by the histone methyltransferase (HMT) Clr4; conversely, H3K9 methylation can attract RITS to chromatin via binding of the chromodomain protein Chp1. This codependency has hampered dissection of the order of events and mechanisms of cross talk between the RNAi and chromatin modification machineries. To tackle this problem, we have developed systems that reconstitute heterochromatin at a euchromatic locus, using either hairpin triggers or DNA-tethered chromatin-modifying complexes. These systems reveal that RNAi is sufficient to promote heterochromatin assembly in cis and that direct recruitment of the HMT Clr4 can bypass the role of RNAi in heterochromatin assembly. We have also characterized a new pathway component, Stc1, that translates the RNAi signal into chromatin marks. We discuss the implications of these findings for our understanding of the mechanism and function of RNAi-directed heterochromatin assembly at centromeres.","doi":"10.1101/sqb.2010.75.024","authors":"Lejeune E, Bayne EH, Allshire RC","authors_abbrev":"Lejeune E et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2011-02-04","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7773104","title":"Glutamine synthetase/glutamate synthase ammonium-assimilating pathway in Schizosaccharomyces pombe.","citation":"Curr Microbiol 1995 Jun;30(6):367-72","abstract":"Kinetic parameters of glutamine synthetase (GS) and glutamate synthase (glutamine-oxoglutarate aminotransferase) (GOGAT) activities, including initial velocity, pH, and temperature optima, as well as Km values, were estimated in Schizosaccharomyces pombe crude cell-free extracts. Five glutamine auxotrophic mutants of S. pombe were isolated following MNNG treatment. These were designated gln1-1,2,3,4,5, and their growth could be repaired only by glutamine. Mutants gln1-1,2,3,4,5 were found to lack GS activity, but retained wild-type levels of NADP-glutamate dehydrogenase (GDH), NAD-GDH, and GOGAT. One further glutamine auxotrophic mutant, gln1-6, was isolated and found to lack both GS and GOGAT but retained wild-type levels of NADP-GDH and NAD-GDH activities. Fortuitously, this isolate was found to harbor an unlinked second mutation (designated gog1-1), which resulted in complete loss of GOGAT activity but retained wild-type GS activity. The growth phenotype of mutant gog1-1 (in the absence of the gln1-6 mutation) was found to be indistinguishable from the wild type on various nitrogen sources, including ammonium as a sole nitrogen source. Double-mutant strains containing gog1-1 and gdh1-1 or gdh2-1 (mutations that result specifically in the abolition of NADP-GDH activity) result in a complete lack of growth on ammonium as sole nitrogen source in contrast to gdh or gog mutants alone.","authors":"Perysinakis A, Kinghorn JR, Drainas C","authors_abbrev":"Perysinakis A et al.","pubmed_publication_date":"Jun 1995","pubmed_entrez_date":"1995-06-01","publication_year":"1995","canto_session_key":"1b1b8ae732261385","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-03-15 14:34:58","canto_approved_date":"2026-01-25 05:48:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-29 13:38:51","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H4.06","SPAPB1E7.07","SPCC622.12c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-03-15"},{"uniquename":"PMID:37881245","title":"A marker-free genome editing method in  S. pombe  using the  delitto perfetto  approach.","citation":"MicroPubl Biol 2023;2023","abstract":"The fission yeast, like budding yeast, offer an easy manipulation of their genome, despite their distinct biology. Most tools available in budding yeast are also available in fission yeast in versions taking into account the features of each organism. The  delitto perfetto  is a powerful approach, initially developed in  S. cerevisiae  , for  in vivo  site-directed mutagenesis. Here, we present an adaptation of the approach to  S. pombe  manipulation and demonstrate its applicability for a rapid, marker-free and efficient  in vivo  site-directed mutagenesis and N-terminal tagging of nonessential genes in fission yeast.","doi":"10.17912/micropub.biology.000997","authors":"Fréon K, Lambert SAE, Lobachev KS, Ait Saada A","authors_abbrev":"Fréon K et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-10-26","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-10-26 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2229195","title":"Continued DNA synthesis after a mitotic block in the double mutant cut1 cdc11 of the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1990 Jul;96 ( Pt 3):435-8","abstract":"DNA synthesis is normally dependent on a cell having previously gone through mitosis. Hirano et al. (1986), however, found that DNA synthesis continued at the restrictive temperature in the double mutant cut1 cdc11 of Schizosaccharomyces pombe even though mitosis was blocked in some of the cells. We have confirmed this result with bulk DNA assays of asynchronous cultures. Synchronous cultures of a diploid double mutant at the restrictive temperature showed two peaks of incorporation with an interval between them that was approximately the same as the doubling time in cell length. Flow cytometry showed that the cells had increased their DNA content from 4C (the diploid value) to about 16C after 7h. The cytological appearance at this time was mixed, with uninucleate, binucleate and dead cells, but fluorescence measurements on single cells indicated that about half the population had single nuclei with about the 16C value and had therefore gone through two rounds of DNA synthesis without mitosis.","authors":"Creanor J, Mitchison JM","authors_abbrev":"Creanor J et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_session_key":"21584b855b4b2af5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-04-08 15:09:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-05 15:46:46","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.04","SPCC1739.11c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-04-05"},{"uniquename":"PMID:29160296","title":"Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex.","citation":"Cell Res 2017 Dec;27(12):1503-1520","abstract":"Telomeric shelterin complex caps chromosome ends and plays a crucial role in telomere maintenance and protection. In the fission yeast Schizosaccharomyces pombe, shelterin is composed of telomeric single- and double-stranded DNA-binding protein subcomplexes Pot1-Tpz1 and Taz1-Rap1, which are bridged by their interacting protein Poz1. However, the structure of Poz1 and how Poz1 functions as an interaction hub in the shelterin complex remain unclear. Here we report the crystal structure of Poz1 in complex with Poz1-binding motifs of Tpz1 and Rap1. The crystal structure shows that Poz1 employs two different binding surfaces to interact with Tpz1 and Rap1. Unexpectedly, the structure also reveals that Poz1 adopts a dimeric conformation. Mutational analyses suggest that proper interactions between Tpz1, Poz1, and Rap1 in the shelterin core complex are required for telomere length homeostasis and heterochromatin structure maintenance at telomeres. Structural resemblance between Poz1 and the TRFH domains of other shelterin proteins in fission yeast and humans suggests a model for the evolution of shelterin proteins.","doi":"10.1038/cr.2017.145","authors":"Xue J, Chen H, Wu J, Takeuchi M, Inoue H, Liu Y, Sun H, Chen Y, Kanoh J, Lei M","authors_abbrev":"Xue J et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-11-22","publication_year":"2017","canto_session_key":"8eca88feb01d8e15","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-21 16:33:08","canto_approved_date":"2026-02-15 12:55:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-08-21 16:32:59","canto_added_date":"2017-11-23 01:15:14","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":53,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC212.11","SPAC6F6.16c","SPBCPT2R1.08c","SPCC188.07","SPAC19G12.13c","SPBC1778.02"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2024-08-21","pdb_entries":[{"pdb_id":"5xxf","gene_chains":[{"gene_uniquename":"SPAC19G12.13c","chain":"A/B","position":"2-247"},{"gene_uniquename":"SPAC6F6.16c","chain":"C/D","position":"478-508"}],"title":"Crystal structure of Poz1, Tpz1 and Rap1","entry_authors":"Xue J,Chen H,Wu J,Lei M","entry_authors_abbrev":"Xue J et al.","reference_uniquename":"PMID:29160296","experimental_method":"X-ray","resolution":"3.1"},{"pdb_id":"5xxe","gene_chains":[{"gene_uniquename":"SPAC19G12.13c","chain":"A/B","position":"2-249"},{"gene_uniquename":"SPAC6F6.16c","chain":"C/D","position":"477-508"}],"title":"Crystal structure of Poz1 and Tpz1","entry_authors":"Xue J,Chen H,Wu J,Lei M","entry_authors_abbrev":"Xue J et al.","reference_uniquename":"PMID:29160296","experimental_method":"X-ray","resolution":"2.5"}]},{"uniquename":"PMID:10577839","title":"DNA replication checkpoint control.","citation":"Front Biosci 1999 Dec 01;4:D841-8","abstract":"The eukaryotic cell cycle comprises two critical phases, DNA replication (S phase) and the subsequent distribution of an equivalent genome to each of two daughter cells at mitosis (M phase). A signal transduction cascade called the replication checkpoint has evolved to ensure that M phase does not occur prior to the completion of S phase. The mitotic regulators targeted by this checkpoint have recently been identified in the fission yeast Schizosaccharomyces pombe. As was the case for the DNA damage checkpoint, studies on the replication checkpoint in fission yeast promise to provide an excellent framework for analogous studies in mammalian cells.","authors":"Boddy MN, Russell P","authors_abbrev":"Boddy MN et al.","pubmed_publication_date":"01 Dec 1999","pubmed_entrez_date":"1999-11-30","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19416828","title":"Schizosaccharomyces pombe Rtf2 mediates site-specific replication termination by inhibiting replication restart.","citation":"Proc Natl Acad Sci U S A 2009 May 12;106(19):7927-32","abstract":"Here, we identify a phylogenetically conserved Schizosaccharomyces pombe factor, named Rtf2, as a key requirement for efficient replication termination at the site-specific replication barrier RTS1. We show that Rtf2, a proliferating cell nuclear antigen-interacting protein, promotes termination at RTS1 by preventing replication restart; in the absence of Rtf2, we observe the establishment of \"slow-moving\" Srs2-dependent replication forks. Analysis of the pmt3 (SUMO) and rtf2 mutants establishes that pmt3 causes a reduction in RTS1 barrier activity, that rtf2 and pmt3 are nonadditive, and that pmt3 (SUMO) partly suppresses the rtf2-dependent replication restart. Our results are consistent with a model in which Rtf2 stabilizes the replication fork stalled at RTS1 until completion of DNA synthesis by a converging replication fork initiated at a flanking origin.","doi":"10.1073/pnas.0812323106","authors":"Inagawa T, Yamada-Inagawa T, Eydmann T, Mian IS, Wang TS, Dalgaard JZ","authors_abbrev":"Inagawa T et al.","pubmed_publication_date":"12 May 2009","pubmed_entrez_date":"2009-05-07","publication_year":"2009","canto_session_key":"b6b9d534da028509","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-13 13:51:26","canto_approved_date":"2025-09-04 09:41:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-12 14:49:28","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":46,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPAC2G11.12","SPCC553.07c","SPAC1D4.09c","SPAC4H3.05","SPBC16A3.11","SPAC688.10","SPBC365.06"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-04-13"},{"uniquename":"PMID:15075270","title":"Cell division defects of Schizosaccharomyces pombe liz1- mutants are caused by defects in pantothenate uptake.","citation":"Eukaryot Cell 2004 Apr;3(2):406-12","abstract":"The liz1+ gene of the fission yeast Schizosaccharomyces pombe was previously identified by complementation of a mutation that causes abnormal mitosis when ribonucleotide reductase is inhibited. Liz1 has similarity to transport proteins from Saccharomyces cerevisiae, but the potential substrate and its connection to the cell division cycle remain elusive. We report here that liz1+ encodes a plasma membrane-localized active transport protein for the vitamin pantothenate, the precursor of coenzyme A (CoA). Liz1 is required for pantothenate uptake at low extracellular concentrations. A lack of pantothenate uptake results in three phenotypes: (i) slow growth, (ii) delayed septation, and (iii) aberrant mitosis in the presence of hydroxyurea (HU). All three phenotypes are suppressed by high extracellular concentrations of pantothenate, where pantothenate uptake occurs by passive diffusion. liz1Delta mutants are viable because they can synthesize pantothenate from uracil as an endogenous source. The use of uracil for both pantothenate biosynthesis and deoxyribonucleotide generation provides an explanation for the aberrant mitosis in the presence of HU. HU blocks ribonucleotide reductase, and we propose that the accumulation of ribonucleotides reduces uracil biosynthesis by feedback inhibition of aspartate transcarbamoylase. Thus, the addition of HU to liz1Delta mutants results in a shortage of pantothenate. Because liz1Delta mutants show striking similarities to mutants with defects in fatty acid biosynthesis, we propose that the shortage of pantothenate compromises fatty acid synthesis, resulting in slow growth and mitotic defects.","authors":"Stolz J, Caspari T, Carr AM, Sauer N","authors_abbrev":"Stolz J et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-04-13","publication_year":"2004","canto_session_key":"9a4ed1603d089abe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-03 12:49:29","canto_approved_date":"2021-01-05 17:00:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-12-13 15:17:01","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5H10.08c","SPBC2G2.01c","SPAC20G4.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-04-03"},{"uniquename":"PMID:26566110","title":"Sizing up to divide: mitotic cell-size control in fission yeast.","citation":"Annu Rev Cell Dev Biol 2015;31:11-29","abstract":"Schizosaccharomyces pombe is a good model to study cell-size control. These cells integrate size information into cell cycle controls at both the G1/S and G2/M transitions, although the primary control operates at the entry into mitosis. At G2/M there is both a size threshold, demonstrated by the fact that cells divide when they reach 14 μm in length, and also correction around this threshold, evident from the narrow distribution of sizes within a population. This latter property is referred to as size homeostasis. It has been argued that a population of cells accumulating mass in a linear fashion will have size homeostasis in the absence of size control, if cycle time is controlled by a fixed timer. Because fission yeast cells do not grow in a simple linear fashion, they require a size-sensing mechanism. However, current models do not fully describe all aspects of this control, especially the coordination of cell size with ploidy.","doi":"10.1146/annurev-cellbio-100814-125601","authors":"Wood E, Nurse P","authors_abbrev":"Wood E et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-11-14","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-11-15 01:19:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F7.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11113974","title":"Sequence analysis of two cosmids from Schizosaccharomyces pombe chromosome III.","citation":"Yeast 2000 Dec;16(16):1519-26","abstract":"We report the complete sequence of two cosmids, SPCC895 (38457 bp insert, EMBL Accession No. AL035247) and SPCC1322 (42068 bp insert, EMBL Accession No. AL035259), localized on chromosome III of the Schizosaccharomyces pombe genome. Fourteen Coding DNA sequences (CDSs) were identified in SPCC895 and 17 in SPCC1322. Two known genes were found in each cosmid: map2 and gms1 on SPCC895, encoding the mating type P-factor precursor and an UDP-galactose transporter, respectively, and bub1 and ade6 in SPCC1322, encoding a protein kinase and a phosphoribosylaminoimidazole carboxylase, respectively. The fission yeast K RNA gene has been localized to SPCC895. Three ribosomal proteins have been predicted among these two cosmids. Nine CDSs similar to known proteins were found on SPCC895, and seven on SPCC1322. They include putative genes for an uridylate kinase, a proteasome catalytic component, an ion transporter, a checkpoint protein, a translation initiation protein, a SNARE complex protein, a protein involved in cytoskeletal organization, a spindle pole body-associating protein, pre-mRNA splicing factor RNA helicase, a 3'-5' exonuclease for RNA 3' ss-tail, an UTP-glucose-1-phosphate uridylyltransferase, a leukotriene A(4) hydrolase, a member of the RanBP7-importin beta-Cse1p superfamily, a Ca(++)-calmodulin-dependent serine/threonine protein kinase and a prohibitin antiproliferative protein. One CDS is predicted to be an integral membrane protein. One CDS from SPCC895 is similar to a CDS of unknown function from Saccharomyces cerevisiae and three from SPCC1322 are similar to CDSs of unknown function from Candida albicans, S. cerevisiae and Sz. pombe, respectively. Finally, one CDS of SPCC895 and three of SPCC1322 correspond to orphan genes.","authors":"Lucas M, Gwillam R, Lepingle A, Lyne M, Rajandream MA, Rochet M, Wood V, Gaillardin C","authors_abbrev":"Lucas M et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-12-13","publication_year":"2000","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11581276","title":"Chromodomain protein Swi6-mediated role of DNA polymerase alpha in establishment of silencing in fission Yeast.","citation":"J Biol Chem 2001 Dec 21;276(51):47814-21","abstract":"Although DNA replication has been thought to play an important role in the silencing of mating type loci in Saccharomyces cerevisiae, recent studies indicate that silencing can be decoupled from replication. In Schizosaccharomyces pombe, mating type silencing is brought about by the trans-acting proteins, namely Swi6, Clr1-Clr4, and Rhp6, in cooperation with the cis-acting silencers. The latter contain an autonomous replication sequence, suggesting that DNA replication may be critical for silencing in S. pombe. To investigate the connection between DNA replication and silencing in S. pombe, we analyzed several temperature-sensitive mutants of DNA polymerase alpha. We find that one such mutant, swi7H4, exhibits silencing defects at mat, centromere, and telomere loci. This effect is independent of the checkpoint and replication defects of the mutant. Interestingly, the extent of the silencing defect in the swi7H4 mutant at the silent mat2 locus is further enhanced in absence of the cis-acting, centromere-proximal silencer. The chromodomain protein Swi6, which is required for silencing and is localized to mat and other heterochromatin loci, interacts with DNA polymerase alpha in vivo and in vitro in wild type cells. However, it does not interact with the mutant pol alpha and is delocalized away from the silent mat loci in the mutant. Our results demonstrate a role of DNA polymerase alpha in the establishment of silencing. We propose a recruitment model for the coupling of DNA replication with the establishment of silencing by the chromodomain protein Swi6, which may be applicable to higher eukaryotes.","authors":"Ahmed S, Saini S, Arora S, Singh J","authors_abbrev":"Ahmed S et al.","pubmed_publication_date":"21 Dec 2001","pubmed_entrez_date":"2001-10-03","publication_year":"2001","canto_session_key":"3b002d9e7447252b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-06-01 15:13:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-13 16:21:18","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC3H5.06c","SPAC664.01c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-02-13"},{"uniquename":"PMID:2785683","title":"Construction of a Not I restriction map of the fission yeast Schizosaccharomyces pombe genome.","citation":"Nucleic Acids Res 1989 Apr 11;17(7):2801-18","abstract":"Pulsed field gel electrophoresis and large DNA technology were used to construct a Not I restriction map of the entire genome of the fission yeast Schizosaccharomyces pombe. There are 14 detectable Not I sites in S. pombe 972h: 9 sites on chromosome I and 5 sites on chromosome II, while no Not I sites were found on chromosome III. The 17 fragments (including intact chromosome III) generated by Not I digestion were resolved by PFG electrophoresis. These fragments ranged in size from 4.5 kb to approximately 3.5 Mb. Various strategies were applied in determining, efficiently, the order of the fragments on the chromosomes. The genomic size measured by adding all the fragments together is about 14 Mb and the sizes of the three chromosomes are I, 5.7 Mb, II, 4.6 to 4.7 Mb, and III, 3.5 Mb. These are generally somewhat smaller than estimated previously.","authors":"Fan JB, Chikashige Y, Smith CL, Niwa O, Yanagida M, Cantor CR","authors_abbrev":"Fan JB et al.","pubmed_publication_date":"11 Apr 1989","pubmed_entrez_date":"1989-04-11","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11686295","title":"Conserved Wat1/Pop3 WD-repeat protein of fission yeast secures genome stability through microtubule integrity and may be involved in mRNA maturation.","citation":"J Cell Sci 2001 Aug;114(Pt 16):2911-20","abstract":"Accurate chromosome segregation is dependent upon the integrity of mitotic spindles, which pull each pair of sister chromatids towards opposite poles. In this study, we have characterised fission yeast pop3-5235, a diploidising mutant that is impaired in genome stability. Pop3 is the same as Wat1, a conserved protein containing 7 WD repeats. Pop3/Wat1 has also been isolated from a two-hybrid screen as a binding partner to Prp2, the large subunit of the essential splicing factor U2AF. In wat1 mutants, the cellular amount of alpha-tubulin is decreased to very low levels, which results in compromised microtubules and spindles, consequently leading to unequal chromosome separation. Further analysis shows that, in spite of the binding between Wat1 and Prp2, Wat1 may not be involved directly in splicing reactions per se. Instead, we find that Wat1 is required for the maintenance of alpha-tubulin mRNA levels; moreover, transcript levels of genes other than the alpha-tubulin gene are also equally decreased in this mutant. Wild-type Wat1, but not the mutant protein, forms a large complex in the cell with several other proteins, suggesting that Wat1 functions as a structural linker in the complex. The results suggest that Wat1 plays a role in mRNA maturation as a coupling protein between splicing and synthesis and/or stabilisation.","authors":"Ochotorena IL, Hirata D, Kominami K, Potashkin J, Sahin F, Wentz-Hunter K, Gould KL, Sato K, Yoshida Y, Vardy L, Toda T","authors_abbrev":"Ochotorena IL et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-11-01","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP8A3.06","SPBC1289.02c","SPBC146.07","SPBC21B10.05c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"EMBL:AU009860","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12898398","title":"Comparative genomics of yeast species: new insights into their biology.","citation":"Int Microbiol 2003 Sep;6(3):183-90","abstract":"The genomes of two hemiascomycetous yeasts (Saccharomyces cerevisiae and Candida albicans) and one archiascomycete (Schizosaccharomyces pombe) have been completely sequenced and the genes have been annotated. In addition, the genomes of 13 more Hemiascomycetes have been partially sequenced. The amount of data thus obtained provides information on the evolutionary relationships between yeast species. In addition, the differential genetic characteristics of the microorganisms explain a number of distinctive biological traits. Gene order conservation is observed between phylogenetically close species and is lost in distantly related species, probably due to rearrangements of short regions of DNA. However, gene function is much more conserved along evolution. Compared to S. cerevisiae and S. pombe, C. albicans has a larger number of specific genes, i.e., genes not found in other organisms, a fact that can account for the biological characteristics of this pathogenic dimorphic yeast which is able to colonize a large variety of environments.","authors":"Herrero E, de la Torre MA, Valentín E","authors_abbrev":"Herrero E et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-08-05","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16506099","title":"Genome-wide patterns of histone modifications in fission yeast.","citation":"Chromosome Res 2006;14(1):95-105","abstract":"We have used oligonucleotide tiling arrays to construct genome-wide high-resolution histone acetylation maps for fission yeast. The maps are corrected for nucleosome density and reveal surprisingly uniform patterns of modifications for five different histone acetylation sites. We found that histone acetylation and methylation patterns are generally polar, i.e. they change as a function of distance from the ATG codon. A typical fission yeast gene shows a distinct peak of histone acetylation around the ATG and gradually decreased acetylation levels in the coding region. The patterns are independent of gene length but dependent on the gene expression levels. H3K9Ac shows a stronger peak near the ATG and is more reduced in the coding regions of genes with high expression compared with genes with low expression levels. H4K16Ac is strongly reduced in coding regions of highly expressed genes. A second microarray platform was used to confirm the 5' to 3' polarity effects observed with tiling microarrays. By comparing coding region histone acetylation data in HDAC mutants and wild type, we found that hos2 affects primarily the 5' regions, sir2 and clr6 affect middle regions, and clr6 affects 3' regions. Thus, mechanisms involving different HDACs modulate histone acetylation levels to maintain a 5' to 3' polarity within the coding regions.","authors":"Sinha I, Wirén M, Ekwall K","authors_abbrev":"Sinha I et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-03-01","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39122693","title":"DEAD-box ATPase Dbp2 is the key enzyme in an mRNP assembly checkpoint at the 3'-end of genes and involved in the recycling of cleavage factors.","citation":"Nat Commun 2024 Aug 09;15(1):6829","abstract":"mRNA biogenesis in the eukaryotic nucleus is a highly complex process. The numerous RNA processing steps are tightly coordinated to ensure that only fully processed transcripts are released from chromatin for export from the nucleus. Here, we present the hypothesis that fission yeast Dbp2, a ribonucleoprotein complex (RNP) remodelling ATPase of the DEAD-box family, is the key enzyme in an RNP assembly checkpoint at the 3'-end of genes. We show that Dbp2 interacts with the cleavage and polyadenylation complex (CPAC) and localises to cleavage bodies, which are enriched for 3'-end processing factors and proteins involved in nuclear RNA surveillance. Upon loss of Dbp2, 3'-processed, polyadenylated RNAs accumulate on chromatin and in cleavage bodies, and CPAC components are depleted from the soluble pool. Under these conditions, cells display an increased likelihood to skip polyadenylation sites and a delayed transcription termination, suggesting that levels of free CPAC components are insufficient to maintain normal levels of 3'-end processing. Our data support a model in which Dbp2 is the active component of an mRNP remodelling checkpoint that licenses RNA export and is coupled to CPAC release.","doi":"10.1038/s41467-024-51035-z","authors":"Aydin E, Schreiner S, Böhme J, Keil B, Weber J, Žunar B, Glatter T, Kilchert C","authors_abbrev":"Aydin E et al.","pubmed_publication_date":"09 Aug 2024","pubmed_entrez_date":"2024-08-09","publication_year":"2024","canto_session_key":"70037dd3c2bd43be","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-06-22 16:16:31","canto_added_date":"2024-08-10 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24610629","title":"(1)H, (15)N and (13)C resonance assignments of the conserved region in the middle domain of S. pombe Sin1 protein.","citation":"Biomol NMR Assign 2015 Apr;9(1):89-92","abstract":"SAPK-interacting protein 1 (Sin1) is an important component of the target of rapamycin (TOR) complex 2 (TORC2). TOR is a serine/threonine-specific protein kinase and forms functionally distinct protein complexes referred to as TORC1 and TORC2. TORC2, conserved from yeast to humans, phosphorylates AGC-family protein kinases and has many cellular functions including the regulation of actin cytoskeleton. The Sin1 subunit of TORC2 is required for the binding of TORC2 to substrates, and the conserved region in the middle (CRIM) domain of Sin1 is important in the substrate recognition of TORC2. Here, we report on the (1)H, (13)C and (15)N resonance assignments of fission yeast Schizosaccharomyces pombe Sin1 (amino acids 247-400) (Sin1CRIM), which possesses the CRIM domain. These data contribute toward the structure determination of Sin1CRIM and an understanding of the interactions of Sin1CRIM with substrates of TORC2.","doi":"10.1007/s12104-014-9550-6","authors":"Kataoka S, Furuita K, Hattori Y, Kobayashi N, Ikegami T, Shiozaki K, Fujiwara T, Kojima C","authors_abbrev":"Kataoka S et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2014-03-11","publication_year":"2015","canto_session_key":"f46f5dc91cdd8b3e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-22 12:01:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-22 10:05:04","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPYUG7.02c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-05-22"},{"uniquename":"EMBL:AU006682","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2145514","title":"Novel potential mitotic motor protein encoded by the fission yeast cut7+ gene.","citation":"Nature 1990 Oct 11;347(6293):563-6","abstract":"The structure equivalent to higher eukaryotic centrosomes in fission yeast, the nuclear membrane-bound spindle pole body, is inactive during interphase. On transition from G2 to M phase of the cell cycle, the spindle pole body duplicates; the daughter pole bodies seed microtubules which interdigitate to form a short spindle that elongates to span the nucleus at metaphase. We have identified two loci which, when mutated, block spindle formation. The predicted product of one of these genes, cut7+, contains an amino-terminal domain similar to the kinesin heavy chain head domain, indicating that the cut7+ product could be a spindle motor. The cut7+ gene resembles the Aspergillus nidulans putative spindle motor gene bimC, both in terms of its organization with a homologous amino-terminal head and no obvious heptad repeats and in the morphology of the mutant phenotype. But we find no similarity between the carboxy termini of these genes, suggested that either the cut7+ gene represents a new class of kinesin genes and that fission yeast may in addition contain a bimC homologue, or that the carboxy termini of these mitotic kinesins are not evolutionarily conserved and that the cut7+ gene belongs to a subgroup of bimC-related kinesins.","authors":"Hagan I, Yanagida M","authors_abbrev":"Hagan I et al.","pubmed_publication_date":"11 Oct 1990","pubmed_entrez_date":"1990-10-11","publication_year":"1990","canto_session_key":"411c2c9c45290c9e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-02-28 11:59:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 16:42:24","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-25"},{"uniquename":"PMID:10341216","title":"Sto1p, a fission yeast protein similar to tubulin folding cofactor E, plays an essential role in mitotic microtubule assembly.","citation":"J Cell Sci 1999 Jun;112 ( Pt 12):1979-88","abstract":"The proper functioning of microtubules depends crucially on the availability of polymerizable alpha/beta tubulin dimers. Their production occurs concomitant with the folding of the tubulin polypeptides and is accomplished in part by proteins known as Cofactors A through E. In the fission yeast, Schizosaccharomyces pombe, this tubulin folding pathway is essential. We have taken advantage of the excellent cytology available in S. pombe to examine the phenotypic consequences of a deletion of sto1(+), a gene that encodes a protein similar to Cofactor E, which is required for the folding of alpha-tubulin. The interphase microtubule cytoskeleton in sto1-delta cells is severely disrupted, and as cells enter mitosis their spindles fail to form. After a transient arrest with condensed chromosomes, the cells exit mitosis and resume DNA synthesis, whereupon they septate abnormally and die. Overexpression of Spo1p is toxic to cells carrying a cold-sensitive allele of the alpha- but not the beta-tubulin gene, consistent with the suggestion that this protein plays a role like that of Cofactor E. Unlike its presumptive partner Cofactor D (Alp1p), however, Sto1p does not localize to microtubules but is found throughout the cell. Overexpression of Sto1p has no toxic effects in wild-type cells, suggesting that it is unable to disrupt alpha/beta tubulin dimers in vivo.","authors":"Grishchuk EL, McIntosh JR","authors_abbrev":"Grishchuk EL et al.","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-05-26","publication_year":"1999","canto_session_key":"32c932434e68709c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-03-15 09:37:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-07 15:53:09","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPAC22H10.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-07-07"},{"uniquename":"PMID:1313366","title":"Cloning and sequencing of arg3 and arg11 genes of Schizosaccharomyces pombe on a 10-kb DNA fragment. Heterologous expression and mitochondrial targeting of their translation products.","citation":"Eur J Biochem 1992 Apr 01;205(1):33-43","abstract":"The Schizosaccharomyces pombe arginine anabolic genes encoding ornithine carbamoyltransferase (arg3) and acetylglutamate kinase/acetylglutamyl-phosphate reductase (arg11) were cloned by functional complementation of S. pombe arg3 and arg11 mutant strains from S. pombe DNA genomic libraries. Restriction analysis and sequencing of the two clones showed that both genes are located on a common DNA fragment. The arg3 gene encodes a 327-amino-acid polypeptide presenting a strong identity to Saccharomyces cerevisiae and human ornithine carbamoyltransferases. The arg11 gene encodes a 884-amino-acid polypeptide. The acetylglutamate kinase and acetylglutamate-phosphate reductase domains have been defined by their identity with the S. cerevisiae ARG5,6 protein. The cloned arg11 gene from S. pombe does not complement an arg5,6 mutation in S. cerevisiae, nor does the ARG5,6 gene complement the S. pombe arg11- mutation. In contrast, both ornithine-carbamoyltransferase-encoding genes function in S. pombe. However, the S. pombe arg3 gene complements only weakly an arg3 S. cerevisiae strain, which is in agreement with the low level of expression of the S. pombe gene in S. cerevisiae. The subcellular localization of both ornithine carbamoyltransferases in the two yeasts indicates that, in contrast to the S. pombe enzyme, more than 95% of the S. cerevisiae enzyme remains in the S. pombe cytoplasm. The low expression of S. pombe ornithine carbamoyltransferases in S. cerevisiae did not allow its localization. The promoters of S. pombe arg3 and arg11 genes do not present striking similarities among themselves nor with the promoters of the equivalent genes of S. cerevisiae.","authors":"Van Huffel C, Dubois E, Messenguy F","authors_abbrev":"Van Huffel C et al.","pubmed_publication_date":"01 Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"7049256ffb8b397c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2012-11-21 16:22:01","canto_approved_date":"2026-03-09 16:01:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-21 16:20:55","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4G9.10","SPAC4G9.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-11-21"},{"uniquename":"PMID:64180","title":"[Comparison of the properties of mitochondrial and plasmic ATPases in the yeast Schizosaccharomyces pombe].","citation":"Arch Int Physiol Biochim 1976;84(3):602-3","abstract":"","authors":"Delhez J, Dufour JP, Goffeau A","authors_abbrev":"Delhez J et al.","pubmed_publication_date":"1976","pubmed_entrez_date":"1976-01-01","publication_year":"1976","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21652630","title":"Characterization of Mug33 reveals complementary roles for actin cable-dependent transport and exocyst regulators in fission yeast exocytosis.","citation":"J Cell Sci 2011 Jul 01;124(Pt 13):2187-99","abstract":"Although endocytosis and exocytosis have been extensively studied in budding yeast, there have been relatively few investigations of these complex processes in the fission yeast Schizosaccharomyces pombe. Here we identify and characterize fission yeast Mug33, a novel Tea1-interacting protein, and show that Mug33 is involved in exocytosis. Mug33 is a Sur7/PalI-family transmembrane protein that localizes to the plasma membrane at the cell tips and to cytoplasmic tubulovesicular elements (TVEs). A subset of Mug33 TVEs make long-range movements along actin cables, co-translocating with subunits of the exocyst complex. TVE movement depends on the type V myosin Myo52. Although mug33Δ mutants are viable, with only a mild cell-polarity phenotype, mug33Δ myo52Δ double mutants are synthetically lethal. Combining mug33 Δ with deletion of the formin For3 (for3Δ) leads to synthetic temperature-sensitive growth and strongly reduced levels of exocytosis. Interestingly, mutants in non-essential genes involved in exocyst function behave in a manner similar to mug33Δ when combined with myo52Δ and for3Δ. By contrast, combining mug33Δ with mutants in non-essential exocyst genes has only minor effects on growth. We propose that Mug33 contributes to exocyst function and that actin cable-dependent vesicle transport and exocyst function have complementary roles in promoting efficient exocytosis in fission yeast.","doi":"10.1242/jcs.084038","authors":"Snaith HA, Thompson J, Yates JR, Sawin KE","authors_abbrev":"Snaith HA et al.","pubmed_publication_date":"01 Jul 2011","pubmed_entrez_date":"2011-06-10","publication_year":"2011","canto_session_key":"dcd04bfe23f43146","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-01 14:53:24","canto_approved_date":"2026-06-23 04:33:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-01 14:52:53","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":60,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.05","SPBC215.05","SPAC9E9.09c","SPBC530.10c","SPAC24H6.07","SPCC306.08c","SPCC584.01c","SPAC13A11.01c","SPAC24C9.12c","SPAC57A7.04c","SPBC1734.11","SPCC18.18c","SPAC767.01c","SPCC576.08c","SPCP1E11.11","SPBC1539.09c","SPBC1711.06","SPBC21B10.05c","SPCC13B11.01","SPCC1739.13","SPAC56E4.04c","SPCC550.14","SPAC3C7.12","SPAC1B3.13","SPBC16H5.10c","SPAC2F7.05c","SPBC1A4.07c","SPAC1805.05","SPBC1A4.02c","SPAC16.02c","SPBC32H8.12c","SPAC6B12.12","SPBC21B10.10","SPAPB8E5.06c","SPBC3E7.02c","SPAC6G9.14","SPCC1840.02c","SPAPB17E12.13","SPBC776.11","SPAC23A1.10","SPAC1783.08c","SPAC3C7.11c","SPAC19B12.03","SPBC8D2.03c","SPAC13A11.02c","SPCC622.18","SPBC646.07c","SPCC576.10c","SPAC23C11.11","SPCC970.05","SPBC1A4.08c","SPAC17A5.15c","SPAC664.11","SPCC1795.11","SPBC1604.14c","SPCC1183.08c","SPAC15A10.16","SPCC1223.08c","SPAC3A12.10","SPAP7G5.05","SPAC20G8.06","SPAC22F8.09","SPAC140.02","SPBC1709.05","SPAC24H6.04","SPAC57A7.10c","SPAC10F6.01c","SPCC1739.10","SPAC4F8.12c","SPAC458.02c","SPAC23C4.08","SPCC417.07c","SPBP4H10.11c","SPAC688.11","SPAC1B3.05","SPBC839.13c","SPBC19G7.05c","SPAC1F8.07c","SPBC3B8.09","SPBC23E6.04c","SPAC12G12.04","SPAC664.08c","SPBC4F6.06","SPBC2D10.10c","SPAC1F7.05","SPCP31B10.07","SPBC24C6.04","SPAC1006.07","SPAC3C7.08c","SPAC31G5.03","SPAC17C9.03","SPBC14F5.05c","SPAC144.11","SPBC27.08c","SPAC23A1.11","SPBC2F12.07c","SPAC1687.22c","SPAP8A3.08","SPBC56F2.04","SPCC757.09c","SPAC1F7.13c","SPBC16C6.11","SPAC167.01","SPBC577.06c","SPBC16C6.13c","SPBC1604.20c","SPAC1556.07","SPBC18H10.12c","SPCC330.14c","SPAC821.11","SPAC13G7.02c","SPBC354.12","SPAC513.01c","SPAC1F12.07","SPCC576.11","SPAC26A3.04","SPAC637.05c","SPAC222.11","SPCC24B10.21","SPAC3H5.07","SPBC1711.13","SPBC17A3.04c","SPBPB2B2.12c","SPAPB8E5.02c","SPAC17A2.13c","SPAC1834.03c","SPAPB1E7.12","SPBC11C11.07","SPAC13F5.06c","SPBC1706.01","SPCC1906.01","SPAC31A2.14","SPAC6G9.09c","SPAC9.07c","SPAC2C4.16c","SPBC17G9.03c","SPCC736.15","SPBC651.01c","SPAC6G9.11","SPAC19G12.08","SPCP1E11.10","SPAC6G10.02c","SPAC521.05","SPAC17G6.13","SPAC926.04c","SPBC1815.01","SPBC25H2.16c","SPBC530.04","SPAC22A12.15c","SPAC23A1.06c","SPBC428.15","SPAC9G1.05","SPCC330.08","SPBC1711.05","SPBC3F6.04c","SPAC1687.06c","SPAC16E8.07c","SPAC1071.10c","SPBC839.15c","SPBPJ4664.04","SPCC1919.10c","SPBC31E1.06","SPCC417.08","SPBC32F12.11","SPCC794.09c","SPCC1223.06","SPAC26A3.07c","SPBC3B8.03","SPCC895.07","SPBC16H5.02","SPAC4D7.05","SPAC18G6.15","SPBC685.07c","SPBC2G5.05","SPBC4.07c","SPBC19F8.08","SPBC14F5.04c","SPAC29B12.04","SPAC1565.08","SPAC8E11.02c","SPAC926.09c","SPBC543.02c","SPAC25G10.08","SPAC6B12.15","SPAC20G8.09c","SPAC26A3.10","SPCC825.01","SPCPB16A4.05c","SPCC895.04c","SPAC110.04c","SPAC21E11.08","SPBP4H10.15","SPCC970.09","SPCC622.14","SPAC1527.03","SPCC1672.07","SPAC11G7.03","SPBC1703.07","SPBC23G7.12c","SPBC18H10.03","SPBP8B7.03c","SPBP35G2.07","SPCC962.03c","SPBC29A3.04","SPBC29A10.01","SPAC4A8.05c","SPAC24B11.06c","SPBC646.10c","SPAC9E9.03","SPAC20H4.01","SPAC1851.03","SPAC1420.03","SPCC1235.10c","SPBC106.20","SPAC26A3.09c","SPAC23C11.03","SPAC26F1.06","SPAC13G6.07c","SPAC17A5.03","SPAC30C2.04","SPBC405.07","SPAC3G9.03","SPBC16C6.06","SPBC83.08","SPBC56F2.02","SPBC1105.02c","SPBC13G1.10c","SPCC1322.11","SPBC106.06","SPCC1682.14","SPCC895.05","SPBC29A3.12","SPAC4H3.10c","SPBC29B5.03c","SPBC17G9.10","SPBC25H2.02"],"gene_count":236,"ltp_gene_count":12,"approved_date":"2017-02-01"},{"uniquename":"PMID:27185885","title":"G-rich telomeric and ribosomal DNA sequences from the fission yeast genome form stable G-quadruplex DNA structures in vitro and are unwound by the Pfh1 DNA helicase.","citation":"Nucleic Acids Res 2016 Jul 27;44(13):6213-31","abstract":"Certain guanine-rich sequences have an inherent propensity to form G-quadruplex (G4) structures. G4 structures are e.g. involved in telomere protection and gene regulation. However, they also constitute obstacles during replication if they remain unresolved. To overcome these threats to genome integrity, organisms harbor specialized G4 unwinding helicases. In Schizosaccharomyces pombe, one such candidate helicase is Pfh1, an evolutionarily conserved Pif1 homolog. Here, we addressed whether putative G4 sequences in S. pombe can adopt G4 structures and, if so, whether Pfh1 can resolve them. We tested two G4 sequences, derived from S. pombe ribosomal and telomeric DNA regions, and demonstrated that they form inter- and intramolecular G4 structures, respectively. Also, Pfh1 was enriched in vivo at the ribosomal G4 DNA and telomeric sites. The nuclear isoform of Pfh1 (nPfh1) unwound both types of structure, and although the G4-stabilizing compound Phen-DC3 significantly enhanced their stability, nPfh1 still resolved them efficiently. However, stable G4 structures significantly inhibited adenosine triphosphate hydrolysis by nPfh1. Because ribosomal and telomeric DNA contain putative G4 regions conserved from yeasts to humans, our studies support the important role of G4 structure formation in these regions and provide further evidence for a conserved role for Pif1 helicases in resolving G4 structures.","doi":"10.1093/nar/gkw349","authors":"Wallgren M, Mohammad JB, Yan KP, Pourbozorgi-Langroudi P, Ebrahimi M, Sabouri N","authors_abbrev":"Wallgren M et al.","pubmed_publication_date":"27 Jul 2016","pubmed_entrez_date":"2016-05-18","publication_year":"2016","canto_session_key":"fa1f8caf3177bc73","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-13 13:49:55","canto_approved_date":"2024-12-21 12:19:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-13 14:49:08","canto_added_date":"2016-05-19 00:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-08-13"},{"uniquename":"PMID:11004189","title":"Characterization of tpp1(+) as encoding a main trehalose-6P phosphatase in the fission yeast Schizosaccharomyces pombe.","citation":"J Bacteriol 2000 Oct;182(20):5880-4","abstract":"We have characterized an open reading frame of 2,454 bp on chromosome I of Schizosaccharomyces pombe as the gene encoding trehalose-6P phosphatase (tpp1(+)). Disruption of tpp1(+) caused in vivo accumulation of trehalose-6P upon heat shock and prevented cell growth at 37 to 40 degrees C. Accumulation of trehalose-6P in cells bearing a chromosomal disruption of the tpp1(+) gene and containing a plasmid with tpp1(+) under the control of the thiamine-repressible promotor correlated with tpp1(+) repression. The level of tpp1(+) mRNA rose upon heat shock, osmostress, or oxidative stress and was negatively controlled by cyclic AMP-dependent protein kinase activity. Expression of tpp1(+) during oxidative or osmotic stress, but not during heat shock, was under positive control by the wis1-sty1 (equivalent to phh1 and spc1) mitogen-activated protein kinase pathway. Analysis of Tpp1 protein levels suggests that the synthesis of trehalose-6P phosphatase may also be subjected to translational or posttranslational control.","authors":"Franco A, Soto T, Vicente-Soler J, Guillen PV, Cansado J, Gacto M","authors_abbrev":"Franco A et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-09-27","publication_year":"2000","canto_session_key":"74e71f74b286b84c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-29 13:29:13","canto_approved_date":"2024-12-03 12:01:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 10:15:43","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.15c","SPBC106.10","SPAC24B11.06c","SPAC1B9.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-04-29"},{"uniquename":"PMID:25825871","title":"Genetic interaction mapping reveals a role for the SWI/SNF nucleosome remodeler in spliceosome activation in fission yeast.","citation":"PLoS Genet 2015 Mar;11(3):e1005074","abstract":"Although numerous regulatory connections between pre-mRNA splicing and chromatin have been demonstrated, the precise mechanisms by which chromatin factors influence spliceosome assembly and/or catalysis remain unclear. To probe the genetic network of pre-mRNA splicing in the fission yeast Schizosaccharomyces pombe, we constructed an epistatic mini-array profile (E-MAP) and discovered many new connections between chromatin and splicing. Notably, the nucleosome remodeler SWI/SNF had strong genetic interactions with components of the U2 snRNP SF3 complex. Overexpression of SF3 components in ΔSWI/SNF cells led to inefficient splicing of many fission yeast introns, predominantly those with non-consensus splice sites. Deletion of SWI/SNF decreased recruitment of the splicing ATPase Prp2, suggesting that SWI/SNF promotes co-transcriptional spliceosome assembly prior to first step catalysis. Importantly, defects in SWI/SNF as well as SF3 overexpression each altered nucleosome occupancy along intron-containing genes, illustrating that the chromatin landscape both affects--and is affected by--co-transcriptional splicing.","doi":"10.1371/journal.pgen.1005074","authors":"Patrick KL, Ryan CJ, Xu J, Lipp JJ, Nissen KE, Roguev A, Shales M, Krogan NJ, Guthrie C","authors_abbrev":"Patrick KL et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-04-01","publication_year":"2015","canto_session_key":"513bd7e2876876a0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-04-02 00:18:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19381815","title":"High-throughput microfluidic system for monitoring diffusion-based monolayer yeast cell culture over long time periods.","citation":"Biomed Microdevices 2009 Oct;11(5):981-6","abstract":"We present a simple and high-throughput microfluidic system for diffusion-based monolayer yeast cell culture monitoring. Yeast cells are patterned into the micro-cavity array with a suitable height (4 μm) that keeps the cells fixed in monolayer during the cell division. Different sizes of cavities and different repeating times of injection were tested in order to realize as many single-cell/cavity as possible. Single-cell/cavity has been achieved in about 40% of 100 parallel cavities. As a demonstration, we apply this technology to investigate budding yeast and fission yeast cultures and show that it permits single-cell resolution over many cellular generations. Our results show that the technique provides an easy way to study the phenotype of single yeast cell cycle or cell-cell communication in high-throughput microfluidic system.","doi":"10.1007/s10544-009-9315-7","authors":"Luo C, Jiang L, Liang S, Ouyang Q, Ji H, Chen Y","authors_abbrev":"Luo C et al.","pubmed_publication_date":"Oct 2009","pubmed_entrez_date":"2009-04-22","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30794054","title":"An RNA aptamer to HP1/Swi6 facilitates heterochromatin formation at an ectopic locus in S.pombe.","citation":"RNA Biol 2019 Jun;16(6):742-753","abstract":"In the fission yeast Schizosaccharomyces pombe (S.pombe), heterochromatin domains are established and maintained by protein complexes that contain numerous RNA binding domains among their components. The fission yeast HP1 protein Swi6 is one such component and contains an unstructured RNA-binding hinge, which is important for the integrity and silencing of heterochromatin. In this study, we have used an RNA aptamer that likely binds to the Swi6 hinge with high affinity, as a tool to perturb the natural interactions mediated by this domain. When the hinge is blocked by the aptamer RNA, Swi6 appears to become less restricted to the pericentromeres and is enriched at specific euchromatic loci. This suggests a role for the Swi6 hinge, along with the chromoshadow domain (previously shown) in controlling the spread of heterochromatin in S.pombe. The study also highlights the potential of using a synthetic aptamer RNA as a tool to perturb nucleic acid - protein interaction in vivo with the objective of understanding the functional relevance of such an interaction.","doi":"10.1080/15476286.2019.1584026","authors":"Rani R, Yaseen AM, Malwade A, Sevilimedu A","authors_abbrev":"Rani R et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-02-23","publication_year":"2019","canto_session_key":"4710b4a242847ef4","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-02-24 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22907753","title":"Posttranscriptional regulation of cell-cell interaction protein-encoding transcripts by Zfs1p in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2012 Oct;32(20):4206-14","abstract":"Members of the tristetraprolin (TTP) family of CCCH tandem zinc finger proteins can bind directly to AU-rich elements in mRNAs and promote transcript deadenylation and decay. The yeast Schizosaccharomyces pombe expresses a single TTP family member, Zfs1p. In this study, we identified probable Zfs1p target mRNAs by comparing transcript levels in wild-type yeast and zfs1Δ mutants, using deep sequencing and microarray approaches. We also used direct RNA sequencing to determine polyadenylation site locations and to confirm the presence of potential Zfs1p target sequences within the target mRNA. These studies identified a set of transcripts containing potential Zfs1p binding sites that accumulated significantly in the zfs1Δ mutants; a subset of these transcripts decayed more slowly in the zfs1Δ mutants and bound directly to Zfs1p in coimmunoprecipitation assays. One apparent direct target encodes the transcription factor Cbf12p, which is known to increase cell-cell adhesion and flocculation when overexpressed. Studies of zfs1Δ cbf12Δ double mutants demonstrated that the increased flocculation seen in zfs1Δ mutants is due, at least in part, to a direct effect on the turnover of cbf12 mRNA. These data suggest that Zfs1p can both directly and indirectly regulate the levels of transcripts involved in cell-cell adhesion in this species.","authors":"Wells ML, Huang W, Li L, Gerrish KE, Fargo DC, Ozsolak F, Blackshear PJ","authors_abbrev":"Wells ML et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-22","publication_year":"2012","canto_session_key":"2d7543187cd20039","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-30 14:15:15","canto_approved_date":"2021-02-26 13:27:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-05 16:46:11","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC651.04","SPBP8B7.32","SPAC20G4.07c","SPAC890.03","SPBC725.07","SPAC869.01","SPAC227.03c","SPAP4C9.02","SPCC737.05","SPCC830.10","SPAC16C9.07","SPCC1235.03","SPBC27.02c","SPAC3C7.06c","SPAC3F10.12c","SPAC323.06c","SPAC688.10","SPCC24B10.18","SPAC821.08c","SPCC330.10","SPBPB8B6.06c","SPCC1235.01","SPCC1682.15","SPAC1F3.02c","SPCC1494.03","SPCC895.05","SPCC4B3.13","SPAC22F3.12c","SPAC3H5.09c","SPAC664.15","SPCC63.08c","SPBPB10D8.04c","SPBC19G7.08c","SPBC947.12","SPAC56F8.02","SPBC1703.14c","SPBPB10D8.06c","SPCC285.10c","SPCC1529.01","SPCC1742.01","SPAC10F6.05c","SPAC6B12.02c","SPAC19G12.16c","SPAC4H3.06","SPBC8E4.12c","SPAC167.01","SPAC23H4.17c","SPBC2G5.02c","SPAC23H3.04","SPBC887.18c","SPCC4B3.10c","SPAC27F1.08","SPAC8C9.16c","SPCC613.11c","SPBC649.03","SPAC1786.04","SPBC359.04c","SPBC19C7.02","SPBC1685.04","SPBC577.13","SPBC20F10.10","SPBP4G3.03","SPBPB8B6.04c","SPAC6G9.03c","SPBC577.11","SPCC1223.13","SPAC13G7.04c","SPAC22G7.08","SPAC31A2.12","SPBC56F2.15","SPAC4A8.14","SPBPB10D8.05c","SPAC1B3.15c","SPCC31H12.06","SPBC27.05","SPAC227.01c","SPCC1235.06","SPCC5E4.06","SPBC2F12.08c","SPBC3H7.14","SPCC18.07","SPAC959.10","SPCP25A2.02c","SPBC365.09c","SPBC1105.08","SPBC29A10.04","SPCC330.02","SPBC428.10","SPBC146.01","SPAC1834.08","SPAC3H1.09c","SPCC825.04c","SPCC1235.08c","SPAC5H10.12c","SPBC11B10.08","SPCC1322.14c","SPCC1739.06c","SPBC342.05","SPAC17H9.18c","SPCC4G3.05c","SPBC1718.07c","SPAC186.01","SPBC21B10.04c","SPBC3B9.21","SPBPB10D8.07c","SPCC622.03c","SPCC622.09","SPCC320.13c","SPAC3H5.08c","SPAC4G9.08c","SPAC16E8.11c","SPBPB10D8.01","SPBC29B5.02c","SPAC1039.02","SPAC343.06c","SPCC330.11","SPBC25B2.08","SPAC644.14c","SPBC16A3.19","SPAC4F8.10c","SPAC24H6.13","SPAC3C7.03c","SPAPYUK71.03c","SPAC1B3.11c","SPAC4C5.03","SPCC188.09c","SPAC589.03c","SPAC4D7.03","SPAC607.07c","SPAC869.05c","SPBC13A2.04c","SPBC30B4.07c","SPBC317.01","SPAC1002.11","SPCC736.04c","SPAC2G11.09","SPAC7D4.12c","SPBC1718.03","SPBC19C7.08c","SPAC19A8.16","SPAC17A2.14","SPBC1289.13c","SPCC1827.02c","SPAP27G11.13c","SPAC6G10.03c","SPCC645.13","SPBC1709.12","SPAC977.11","SPCC132.02","SPAC3F10.15c","SPCC63.10c","SPCC4B3.02c","SPAC23C11.10","SPAC22A12.03c","SPAC1834.09","SPAC27D7.11c","SPBC32F12.08c","SPBC336.03","SPAPB2B4.03","SPAC144.18","SPBC660.14","SPAC21E11.07","SPAC22A12.12c","SPBC20F10.03","SPCC1442.13c","SPBC9B6.09c","SPAC19G12.14","SPAC343.09","SPACUNK4.14","SPAPB24D3.09c","SPAC30D11.07","SPBC1539.04","SPAC1A6.03c","SPBC25H2.13c","SPAC1F8.06","SPBC29A3.17","SPBC336.08","SPCC553.04","SPAC23C11.13c","SPAC12B10.12c","SPBC17D11.01","SPCC16C4.11","SPBC1685.07c","SPAC30C2.08","SPAPB1E7.08c","SPAC1D4.05c"],"gene_count":186,"ltp_gene_count":8,"approved_date":"2017-06-30"},{"uniquename":"PMID:5660771","title":"Differential effects of caffeine in mutagen-treated Schizosaccharomyces pombe.","citation":"Mutat Res 1968;5(1):33-40","abstract":"","authors":"Clarke CH","authors_abbrev":"Clarke CH","pubmed_publication_date":"1968","pubmed_entrez_date":"1968-01-01","publication_year":"1968","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5847793","title":"Effect of 2-deoxyglucose on Schizosaccharomyces pombe.","citation":"J Bacteriol 1965 Oct;90(4):1032-5","abstract":"Megnet, Roland (Institut für Allgemeine Mikrobiologie der Universität, Bern, Switzerland). Effect of 2-deoxyglucose on Schizosaccharomyces pombe. J. Bacteriol. 90:1032-1035. 1965.-Cultivation of Schizosaccaromyces pombe in a medium containing 2-deoxyglucose (100 mug/ml) results in the death of the cells after an initial period of apparently normal growth. At higher deoxyglucose concentration (400 mug/ml), the cells die immediately after inoculation. Only growing cells are killed, and microscopic inspection of the cultures reveals cell-wall fragments of lysed cells. A mutant resistant to 2-deoxyglucose, which cannot use glucose as a carbon source, was found to be partially deficient in hexokinase. The data constitute evidence for the inhibition of some reaction(s) in the synthesis of cell-wall polysaccharides by metabolites of 2-deoxyglucose in this organism.","authors":"Megnet R","authors_abbrev":"Megnet R","pubmed_publication_date":"Oct 1965","pubmed_entrez_date":"1965-10-01","publication_year":"1965","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012425","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15625190","title":"Exonic splicing enhancers in fission yeast: functional conservation demonstrates an early evolutionary origin.","citation":"Genes Dev 2005 Jan 15;19(2):242-54","abstract":"Discrete sequence elements known as exonic splicing enhancers (ESEs) have been shown to influence both the efficiency of splicing and the profile of mature mRNAs in multicellular eukaryotes. While the existence of ESEs has not been demonstrated previously in unicellular eukaryotes, the factors known to recognize these elements and mediate their communication with the core splicing machinery are conserved and essential in the fission yeast Schizosaccharomyces pombe. Here, we provide evidence that ESE function is conserved through evolution by demonstrating that three exonic splicing enhancers derived from vertebrates (chicken ASLV, mouse IgM, and human cTNT) promote splicing of two distinct S. pombe pre-messenger RNAs (pre-mRNAs). Second, as in extracts from mammalian cells, ESE function in S. pombe is compromised by mutations and increased distance from the 3'-splice site. Third, three-hybrid analyses indicate that the essential SR (serine/arginine-rich) protein Srp2p, but not the dispensable Srp1p, binds specifically to both native and heterologous purine-rich elements; thus, Srp2p is the likely mediator of ESE function in fission yeast. Finally, we have identified five natural purine-rich elements from S. pombe that promote splicing of our reporter pre-mRNAs. Taken together, these results provide strong evidence that the genesis of ESE-mediated splicing occurred early in eukaryotic evolution.","authors":"Webb CJ, Romfo CM, van Heeckeren WJ, Wise JA","authors_abbrev":"Webb CJ et al.","pubmed_publication_date":"15 Jan 2005","pubmed_entrez_date":"2004-12-31","publication_year":"2005","canto_session_key":"adf4805a233dc936","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-11-07 14:56:08","canto_approved_date":"2023-03-02 07:56:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-27 12:55:01","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-07"},{"uniquename":"PMID:1956788","title":"Alignment of Sfi I sites with the Not I restriction map of Schizosaccharomyces pombe genome.","citation":"Nucleic Acids Res 1991 Nov 25;19(22):6289-94","abstract":"A Sfi I restriction map of the fission yeast Schizosaccharomyces pombe genome was aligned with the Not I restriction map. There are 16 Sfi I sites in the S. pombe genome. Three Sfi I sites are on chromosome III which is devoid of Not I sites. The sizes of the entire genome and individual chromosomes, calculated from the Sfi I fragment sizes, are consistent with that calculated from the Not I fragment sizes. The Sfi I map provides greater physical characterization of the S. pombe genome and further validates the use of S. pombe chromosomal DNA as size standard. These maps have allowed detection of polymorphism on all three chromosomes.","authors":"Fan JB, Grothues D, Smith CL","authors_abbrev":"Fan JB et al.","pubmed_publication_date":"25 Nov 1991","pubmed_entrez_date":"1991-11-25","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29997179","title":"Shelterin promotes tethering of late replication origins to telomeres for replication-timing control.","citation":"EMBO J 2018 Aug 01;37(15)","abstract":"DNA replication initiates at many discrete loci on eukaryotic chromosomes, and individual replication origins are regulated under a spatiotemporal program. However, the underlying mechanisms of this regulation remain largely unknown. In the fission yeast  Schizosaccharomyces pombe , the telomere-binding protein Taz1, ortholog of human TRF1/TRF2, regulates a subset of late replication origins by binding to the telomere-like sequence near the origins. Here, we showed using a  lacO /LacI-GFP system that Taz1-dependent late origins were predominantly localized at the nuclear periphery throughout interphase, and were localized adjacent to the telomeres in the G1/S phase. The peripheral localization that depended on the nuclear membrane protein Bqt4 was not necessary for telomeric association and replication-timing control of the replication origins. Interestingly, the shelterin components Rap1 and Poz1 were required for replication-timing control and telomeric association of Taz1-dependent late origins, and this requirement was bypassed by a minishelterin Tpz1-Taz1 fusion protein. Our results suggest that Taz1 suppresses replication initiation through shelterin-mediated telomeric association of the origins at the onset of S phase.","doi":"10.15252/embj.201898997","authors":"Ogawa S, Kido S, Handa T, Ogawa H, Asakawa H, Takahashi TS, Nakagawa T, Hiraoka Y, Masukata H","authors_abbrev":"Ogawa S et al.","pubmed_publication_date":"01 Aug 2018","pubmed_entrez_date":"2018-07-13","publication_year":"2018","canto_session_key":"b36db928e10b815f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-07-14 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.16c","SPAC19G12.13c","SPAC16A10.07c","SPBC1778.02"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:35861390","title":"Predicting and explaining the impact of genetic disruptions and interactions on organismal viability.","citation":"Bioinformatics 2022 Sep 02;38(17):4088-4099","abstract":"Existing computational models can predict single- and double-mutant fitness but they do have limitations. First, they are often tested via evaluation metrics that are inappropriate for imbalanced datasets. Second, all of them only predict a binary outcome (viable or not, and negatively interacting or not). Third, most are uninterpretable black box machine learning models.\nBudding yeast datasets were used to develop high-performance Multinomial Regression (MN) models capable of predicting the impact of single, double and triple genetic disruptions on viability. These models are interpretable and give realistic non-binary predictions and can predict negative genetic interactions (GIs) in triple-gene knockouts. They are based on a limited set of gene features and their predictions are influenced by the probability of target gene participating in molecular complexes or pathways. Furthermore, the MN models have utility in other organisms such as fission yeast, fruit flies and humans, with the single gene fitness MN model being able to distinguish essential genes necessary for cell-autonomous viability from those required for multicellular survival. Finally, our models exceed the performance of previous models, without sacrificing interpretability.\nAll code and processed datasets used to generate results and figures in this manuscript are available at our Github repository at https://github.com/KISRDevelopment/cell_viability_paper. The repository also contains a link to the GI prediction website that lets users search for GIs using the MN models.\nSupplementary data are available at Bioinformatics online.","doi":"10.1093/bioinformatics/btac519","authors":"Al-Anzi BF, Khajah M, Fakhraldeen SA","authors_abbrev":"Al-Anzi BF et al.","pubmed_publication_date":"02 Sep 2022","pubmed_entrez_date":"2022-07-21","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-07-23 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41453208","title":"Cnp1 N-terminal dynamics regulate L1 loop recognition by Mis15 to orchestrate kinetochore assembly in Schizosaccharomyces pombe.","citation":"J Mol Cell Biol 2025 Dec 26;","abstract":"Centromeres are defined by the histone H3 variant CENP-A, which serve as the foundation for kinetochore assembly and ensure faithful chromosome segregation. CENP-A nucleosomes possess distinctive dynamic features, including flexible DNA ends at the entry/exit sites and a mobile N-terminal region, which are properties proposed to facilitate kinetochore assembly, yet the underlying molecular mechanisms remain elusive. Here, we present cryo-electron microscopy structures of Cnp1, the Schizosaccharomyces pombe (S. pombe) ortholog of CENP-A, alone and in complex with Mis15, the fission yeast ortholog of CENP-N. By integrating structural, biochemical, and molecular dynamics analyses, we demonstrate that the N-terminal region of Cnp1 regulates both DNA-end breathing and the conformational mobility of the L1 loop, a critical structural element for Mis15 recognition. Either enhanced dynamics caused by N-terminal deletion or reduced dynamics from targeted residue substitution disrupt Mis15 binding in vitro and impair its centromeric localization in vivo, thereby compromising the earliest steps of constitutive centromere-associated network assembly. Our findings establish the Cnp1 N-terminus as a dynamic allosteric modulator of chromatin architecture and reveal an L1 loop modulation mechanism that links nucleosome flexibility to kinetochore specification and chromosome segregation fidelity in fission yeast.","doi":"10.1093/jmcb/mjaf056","authors":"Xiong Y, Jian Y, Zhang Y, Zhang M, Zhang X, Zhang K, Fu C, Tian T, Zang J","authors_abbrev":"Xiong Y et al.","pubmed_publication_date":"26 Dec 2025","pubmed_entrez_date":"2025-12-26","publication_year":"2025","canto_session_key":"13d662e258f81bd4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-28 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.08c","SPBC1105.17","SPBC8D2.03c","SPCC622.09"],"gene_count":4,"ltp_gene_count":4,"pdb_entries":[{"pdb_id":"9lrw","gene_chains":[{"gene_uniquename":"SPCC622.08c","chain":"C/G","position":"1-132"},{"gene_uniquename":"SPCC622.09","chain":"D/H","position":"1-126"},{"gene_uniquename":"SPBC8D2.03c","chain":"B/F","position":"1-103"},{"gene_uniquename":"SPBC1105.17","chain":"A/E","position":"1-120"}],"title":"Cryo-EM structure of Fission yeast centromeric nucleosome Class 2","entry_authors":"Xiong Y,Zang J","entry_authors_abbrev":"Xiong Y et al.","reference_uniquename":"PMID:41453208","experimental_method":"EM","resolution":"3.04"},{"pdb_id":"9lrv","gene_chains":[{"gene_uniquename":"SPCC622.08c","chain":"C/G","position":"1-132"},{"gene_uniquename":"SPCC622.09","chain":"D/H","position":"1-126"},{"gene_uniquename":"SPBC8D2.03c","chain":"B/F","position":"1-103"},{"gene_uniquename":"SPBC1105.17","chain":"A/E","position":"1-120"}],"title":"Cryo-EM structure of Fission yeast centromeric nucleosome Class 1","entry_authors":"Xiong Y,Zang J","entry_authors_abbrev":"Xiong Y et al.","reference_uniquename":"PMID:41453208","experimental_method":"EM","resolution":"2.99"}]},{"uniquename":"PMID:24794003","title":"Role of DNA replication in establishment and propagation of epigenetic states of chromatin.","citation":"Semin Cell Dev Biol 2014 Jun;30:131-43","abstract":"DNA replication is the fundamental process of duplication of the genetic information that is vital for survival of all living cells. The basic mechanistic steps of replication initiation, elongation and termination are conserved among bacteria, lower eukaryotes, like yeast and metazoans. However, the details of the mechanisms are different. Furthermore, there is a close coordination between chromatin assembly pathways and various components of replication machinery whereby DNA replication is coupled to \"chromatin replication\" during cell cycle. Thereby, various epigenetic modifications associated with different states of gene expression in differentiated cells and the related chromatin structures are faithfully propagated during the cell division through tight coupling with the DNA replication machinery. Several examples are found in lower eukaryotes like budding yeast and fission yeast with close parallels in metazoans.","doi":"10.1016/j.semcdb.2014.04.015","authors":"Singh J","authors_abbrev":"Singh J","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-05-06","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF105076","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8190062","title":"Molecular analysis of the dhp1+ gene of Schizosaccharomyces pombe: an essential gene that has homology to the DST2 and RAT1 genes of Saccharomyces cerevisiae.","citation":"Mol Gen Genet 1994 Apr;243(1):1-8","abstract":"The DST2 gene of Saccharomyces cerevisiae encodes a DNA strand exchange protein, STP beta, which is required for homologous recombination in both mitotic or meiotic cells. We have cloned a DST2-related gene from the fission yeast Schizosaccharomyces pombe and designated it dhp1+. The nucleotide sequence of dhp1+ revealed an open reading frame encoding a protein composed of 991 amino acids. The predicted amino acid sequence was significantly homologous to the S. cerevisiae STP beta, but lacked the carboxy-terminal sequence present in STP beta. Furthermore, dhp1+ shows greater homology to RAT1/HKE1, a gene which is involved in RNA trafficking and processing. Genetic experiments showed that dhp1+ on an S. cerevisiae expression vector could rescue both the defects of the S. cerevisiae DST2 disruptant, slow growth rate and a sporulation defect, and the lethality of the S. cerevisiae rat1ts mutation. This implies the functional similarity of dhp1+ to both DST2 and RAT1. However unlike DST2, dhp1+ is an essential gene for cell growth in S. pombe, suggesting that dhp1+ is not the true homologue of DST2 but rather of RAT1 in S. pombe. The possible roles of dhp1+ in recombination and cell growth in S. pombe are discussed.","authors":"Sugano S, Shobuike T, Takeda T, Sugino A, Ikeda H","authors_abbrev":"Sugano S et al.","pubmed_publication_date":"Apr 1994","pubmed_entrez_date":"1994-04-01","publication_year":"1994","canto_session_key":"cf188ade486f8613","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-06-30 23:50:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 23:40:48","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.07c","SPAC26A3.12c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-06-30"},{"uniquename":"PMID:11726496","title":"Crystal structure of the fission yeast mitochondrial Holliday junction resolvase Ydc2.","citation":"EMBO J 2001 Dec 03;20(23):6601-11","abstract":"Resolution of Holliday junctions into separate DNA duplexes requires enzymatic cleavage of an equivalent strand from each contributing duplex at or close to the point of strand exchange. Diverse Holliday junction-resolving enzymes have been identified in bacteria, bacteriophages, archaea and pox viruses, but the only eukaryotic examples identified so far are those from fungal mitochondria. We have now determined the crystal structure of Ydc2 (also known as SpCce1), a Holliday junction resolvase from the fission yeast Schizosaccharomyces pombe that is involved in the maintenance of mitochondrial DNA. This first structure of a eukaryotic Holliday junction resolvase confirms a distant evolutionary relationship to the bacterial RuvC family, but reveals structural features which are unique to the eukaryotic enzymes. Detailed analysis of the dimeric structure suggests mechanisms for junction isomerization and communication between the two active sites, and together with site-directed mutagenesis identifies residues involved in catalysis.","authors":"Ceschini S, Keeley A, McAlister MS, Oram M, Phelan J, Pearl LH, Tsaneva IR, Barrett TE","authors_abbrev":"Ceschini S et al.","pubmed_publication_date":"03 Dec 2001","pubmed_entrez_date":"2001-12-01","publication_year":"2001","canto_session_key":"7ab16ed95ce889ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-29 17:53:35","canto_approved_date":"2022-07-22 06:39:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-15 12:00:37","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-29","pdb_entries":[{"pdb_id":"1kcf","gene_chains":[{"gene_uniquename":"SPAC25G10.02","chain":"A/B","position":"1-258"}],"title":"Crystal Structure of the Yeast Mitochondrial Holliday Junction Resolvase, Ydc2","entry_authors":"Ceschini S,Keeley A,McAlister MSB,Oram M,Phelan J,Pearl LH,Tsaneva IR,Barrett TE","entry_authors_abbrev":"Ceschini S et al.","reference_uniquename":"PMID:11726496","experimental_method":"X-ray","resolution":"2.3"}]},{"uniquename":"PMID:36423630","title":"Chromatin localization of nucleophosmin organizes ribosome biogenesis.","citation":"Mol Cell 2022 Dec 01;82(23):4443-4457.e9","abstract":"Ribosome biogenesis takes place in the nucleolus, a nuclear membrane-less organelle. Although well studied, it remains unknown how nascent ribosomal subunits separate from the central chromatin compartment and move to the outer granular component, where maturation occurs. We find that the Schizosaccharomyces pombe nucleophosmin-like protein Fkbp39 localizes to rDNA sites encoding the 60S subunit rRNA, and this localization contributes to its specific association with nascent 60S subunits. Fkbp39 dissociates from chromatin to bind nascent 60S subunits, causing the latter to partition away from chromatin and from nascent 40S subunits through liquid-liquid phase separation. In vivo, Fkbp39 binding directs the translocation of nascent 60S subunits toward the nucleophosmin-rich granular component. This process increases the efficiency of 60S subunit assembly, facilitating the incorporation of 60S RNA domain III. Thus, chromatin localization determines the specificity of nucleophosmin in sorting nascent ribosomal subunits and coordinates their movement into specialized assembly compartments within the nucleolus.","doi":"10.1016/j.molcel.2022.10.033","authors":"Ugolini I, Bilokapic S, Ferrolino M, Teague J, Yan Y, Zhou X, Deshmukh A, White M, Kriwacki RW, Halic M","authors_abbrev":"Ugolini I et al.","pubmed_publication_date":"01 Dec 2022","pubmed_entrez_date":"2022-11-24","publication_year":"2022","canto_session_key":"d1339185f567b117","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-09 16:03:22","canto_approved_date":"2025-09-03 16:59:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-09 16:03:14","canto_added_date":"2022-11-26 01:15:20","annotation_curators":[{"name":"Valerie 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al.","reference_uniquename":"PMID:36423630","experimental_method":"EM","resolution":"3.1"},{"pdb_id":"8eug","gene_chains":[{"gene_uniquename":"SPBC29A3.04","chain":"G","position":"1-259"},{"gene_uniquename":"SPBC2F12.04","chain":"P","position":"1-187"},{"gene_uniquename":"SPBC685.07c","chain":"Z","position":"1-136"},{"gene_uniquename":"SPAC23A1.08c","chain":"g","position":"1-112"},{"gene_uniquename":"SPBC839.13c","chain":"O","position":"1-197"},{"gene_uniquename":"SPBC19F5.05c","chain":"n","position":"1-607"},{"gene_uniquename":"SPAC664.05","chain":"L","position":"1-208"},{"gene_uniquename":"SPBC4F6.13c","chain":"m","position":"1-740"},{"gene_uniquename":"SPCC576.11","chain":"N","position":"1-201"},{"gene_uniquename":"SPCC613.05c","chain":"h","position":"1-122"},{"gene_uniquename":"SPAC1805.13","chain":"M","position":"1-134"},{"gene_uniquename":"SPBC405.07","chain":"i","position":"1-99"},{"gene_uniquename":"SPCC1223.05c","chain":"j","position":"1-91"},{"gene_uniquename":"SPBC56F2.02","chain":"R","position":"1-193"},{"gene_uniquename":"SPCC663.04","chain":"8","position":"1-51"},{"gene_uniquename":"SPAC3G9.03","chain":"V","position":"1-139"},{"gene_uniquename":"SPAC3A12.10","chain":"S","position":"1-176"},{"gene_uniquename":"SPAC1F7.13c","chain":"A","position":"1-253"},{"gene_uniquename":"SPAC26A3.07c","chain":"J","position":"1-174"},{"gene_uniquename":"SPAC3H5.07","chain":"F","position":"1-250"},{"gene_uniquename":"SPCC5E4.07","chain":"a","position":"1-148"},{"gene_uniquename":"SPAC17A5.03","chain":"B","position":"1-388"},{"gene_uniquename":"SPAC3H5.12c","chain":"D","position":"1-294"},{"gene_uniquename":"SPBC29B5.03c","chain":"Y","position":"1-126"},{"gene_uniquename":"SPAC3H5.10","chain":"e","position":"1-127"},{"gene_uniquename":"SPCC622.18","chain":"E","position":"1-195"},{"gene_uniquename":"SPBC18E5.04","chain":"I","position":"1-221"},{"gene_uniquename":"SPAC11E3.15","chain":"U","position":"1-117"},{"gene_uniquename":"SPBC11C11.07","chain":"Q","position":"1-187"},{"gene_uniquename":"SPAC4G9.16c","chain":"H","position":"1-190"},{"gene_uniquename":"SPBC106.18","chain":"X","position":"1-141"},{"gene_uniquename":"SPAC22E12.13c","chain":"u","position":"1-192"},{"gene_uniquename":"SPBC776.01","chain":"b","position":"1-61"},{"gene_uniquename":"SPBC800.04c","chain":"K","position":"1-94"},{"gene_uniquename":"SPBC1711.06","chain":"C","position":"1-363"},{"gene_uniquename":"SPAC890.08","chain":"d","position":"1-113"},{"gene_uniquename":"SPAC890.04c","chain":"p","position":"1-440"},{"gene_uniquename":"SPCP31B10.08c","chain":"f","position":"1-108"},{"gene_uniquename":"SPBC577.02","chain":"k","position":"1-74"},{"gene_uniquename":"SPAC222.06","chain":"3","position":"1-302"},{"gene_uniquename":"SPAC15E1.03","chain":"o","position":"1-106"},{"gene_uniquename":"SPAC1250.05","chain":"c","position":"1-117"},{"gene_uniquename":"SPBC365.03c","chain":"T","position":"1-160"}],"title":"Ytm1 associated nascent 60S ribosome State 3","entry_authors":"Zhou X,Bilokapic S,Deshmukh AA,Halic M","entry_authors_abbrev":"Zhou X et al.","reference_uniquename":"PMID:36423630","experimental_method":"EM","resolution":"2.8"},{"pdb_id":"8esr","gene_chains":[{"gene_uniquename":"SPBC29A3.04","chain":"G","position":"1-259"},{"gene_uniquename":"SPAC17H9.05","chain":"J","position":"1-333"},{"gene_uniquename":"SPBC2F12.04","chain":"P","position":"1-187"},{"gene_uniquename":"SPBC685.07c","chain":"Z","position":"1-136"},{"gene_uniquename":"SPAC1687.11","chain":"w","position":"1-802"},{"gene_uniquename":"SPAC23A1.08c","chain":"g","position":"1-112"},{"gene_uniquename":"SPBC839.13c","chain":"O","position":"1-197"},{"gene_uniquename":"SPBC19F5.05c","chain":"n","position":"1-607"},{"gene_uniquename":"SPAC664.05","chain":"L","position":"1-208"},{"gene_uniquename":"SPBC4F6.13c","chain":"m","position":"1-740"},{"gene_uniquename":"SPBC26H8.08c","chain":"s","position":"1-470"},{"gene_uniquename":"SPCC576.11","chain":"N","position":"1-201"},{"gene_uniquename":"SPCC613.05c","chain":"h","position":"1-122"},{"gene_uniquename":"SPCC1827.05c","chain":"o","position":"1-276"},{"gene_uniquename":"SPAC1805.13","chain":"M","position":"1-134"},{"gene_uniquename":"SPBP8B7.20c","chain":"q","position":"1-608"},{"gene_uniquename":"SPBC887.03c","chain":"I","position":"1-747"},{"gene_uniquename":"SPCC1919.09","chain":"y","position":"1-244"},{"gene_uniquename":"SPBC405.07","chain":"i","position":"1-99"},{"gene_uniquename":"SPBC651.01c","chain":"b","position":"1-642"},{"gene_uniquename":"SPCC1223.05c","chain":"j","position":"1-91"},{"gene_uniquename":"SPBC56F2.02","chain":"R","position":"1-193"},{"gene_uniquename":"SPCC663.04","chain":"8","position":"1-51"},{"gene_uniquename":"SPAC3G9.03","chain":"V","position":"1-139"},{"gene_uniquename":"SPAC3A12.10","chain":"S","position":"1-176"},{"gene_uniquename":"SPAC664.06","chain":"t","position":"1-249"},{"gene_uniquename":"SPAC3H5.07","chain":"F","position":"1-250"},{"gene_uniquename":"SPCC5E4.07","chain":"a","position":"1-148"},{"gene_uniquename":"SPAC17A5.03","chain":"B","position":"1-388"},{"gene_uniquename":"SPBC29B5.03c","chain":"Y","position":"1-126"},{"gene_uniquename":"SPAC3H5.10","chain":"e","position":"1-127"},{"gene_uniquename":"SPCC622.18","chain":"E","position":"1-195"},{"gene_uniquename":"SPAC11E3.15","chain":"U","position":"1-117"},{"gene_uniquename":"SPAC1F7.02c","chain":"D","position":"1-578"},{"gene_uniquename":"SPBC11C11.07","chain":"Q","position":"1-187"},{"gene_uniquename":"SPAC4G9.16c","chain":"H","position":"1-190"},{"gene_uniquename":"SPBC106.18","chain":"X","position":"1-141"},{"gene_uniquename":"SPAC22E12.13c","chain":"u","position":"1-192"},{"gene_uniquename":"SPCC320.11c","chain":"l","position":"1-180"},{"gene_uniquename":"SPBC32H8.05","chain":"z","position":"1-117"},{"gene_uniquename":"SPBC800.06","chain":"A","position":"1-295"},{"gene_uniquename":"SPBC1711.06","chain":"C","position":"1-363"},{"gene_uniquename":"SPAC1142.04","chain":"7","position":"1-707"},{"gene_uniquename":"SPAC890.08","chain":"d","position":"1-113"},{"gene_uniquename":"SPAC890.04c","chain":"p","position":"1-440"},{"gene_uniquename":"SPCP31B10.08c","chain":"f","position":"1-108"},{"gene_uniquename":"SPBC577.02","chain":"k","position":"1-74"},{"gene_uniquename":"SPBC11G11.03","chain":"W","position":"1-241"},{"gene_uniquename":"SPAC8F11.04","chain":"K","position":"1-373"},{"gene_uniquename":"SPAC1250.05","chain":"c","position":"1-117"},{"gene_uniquename":"SPCP1E11.08","chain":"r","position":"1-260"},{"gene_uniquename":"SPBC365.03c","chain":"T","position":"1-160"},{"gene_uniquename":"SPBC1539.10","chain":"v","position":"1-209"}],"title":"Ytm1 associated nascent 60S ribosome (-fkbp39) State 2","entry_authors":"Zhou X,Bilokapic S,Deshmukh AA,Halic M","entry_authors_abbrev":"Zhou X et al.","reference_uniquename":"PMID:36423630","experimental_method":"EM","resolution":"3.2"}]},{"uniquename":"PMID:30943597","title":"Effect of Quinic Acid on the Growth of Some Wild Yeasts and Molds.","citation":"J Food Prot 1985 Apr;48(4):327-329","abstract":"The effect of quinic acid on growth of wild yeasts ( Hansenula anomala , Saccharomyces cerevisiae and Schizosaccharomyces pombe ) and molds ( Aspergillus amstelodami , Botrytis cinerea and Byssochlamys fulva ) was investigated. Quinic acid alone had no antifungal effect on the microbes tested. Generation time of the yeasts remained unaltered in the presence of up to 1% quinic acid, whereas growth of the molds was accelerated. No synergistic effect of quinic acid together with potassium sorbate or sodium benzoate was observed. Quinic acid was antagonistic to the antifungal effects of both potassium sorbate and sodium benzoate on molds. In co-use with sorbate and benzoate, quinic acid shortened the lag phase of the growth of molds. The inhibitory effect of 0.01 to 0.02% sodium benzoate was almost completely eliminated by adding 1% quinic acid.","doi":"10.4315/0362-028X-48.4.327","authors":"Kallio H, Ahtonen S, Sarimo SS","authors_abbrev":"Kallio H et al.","pubmed_publication_date":"Apr 1985","pubmed_entrez_date":"2019-04-05","publication_year":"1985","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-04-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8943016","title":"The highly conserved skb1 gene encodes a protein that interacts with Shk1, a fission yeast Ste20/PAK homolog.","citation":"Proc Natl Acad Sci U S A 1996 Nov 26;93(24):13802-7","abstract":"The Shk1 protein kinase, a homolog of Saccharomyces cerevisiae Ste20 and mammalian p21Cdc42/Rac-activated kinases, is an essential component of a Ras- and Cdc42-dependent signaling cascade required for cell viability, normal morphology, and mitogen-activated protein kinase-mediated sexual responses in the fission yeast, Schizosaccharomyces pombe. To identify S. pombe proteins that modulate or mediate Shk1 functions, we conducted a two-hybrid screen for Shk1-interacting proteins. One of the genes identified as a result of this screen was skb1. We show that Skb1 interacts with a region of the N-terminal regulatory domain of Shk1 distinct from that to which Cdc42 binds, and that Shk1, Cdc42, and Skb1 are able to form a ternary complex in vivo. S.pombe cells carrying an skb1 null mutation are less elongate in morphology than wild-type cells and exhibit a moderate growth defect. The morphology defect of the skb1 deletion mutant is suppressed by overexpression of Shk1. Overexpression of Skb1 causes wild-type S. pombe cells to become hyperelongated. Additional genetic analyses described herein suggest that Skb1 is a component of the morphology control branch of the Ras signaling cascade in S. pombe and that it positively modulates Shk1 function. Homologs of Skb1 are encoded by open reading frames in the genomes of S. cerevisiae and Caenorhabditis elegans and by an uncharacterized human cDNA sequence. Thus, skb1 may be the first well-characterized member of a highly conserved family of genes encoding potential p21Cdc42/Rac-activated kinase regulators.","authors":"Gilbreth M, Yang P, Wang D, Frost J, Polverino A, Cobb MH, Marcus S","authors_abbrev":"Gilbreth M et al.","pubmed_publication_date":"26 Nov 1996","pubmed_entrez_date":"1996-11-26","publication_year":"1996","canto_session_key":"56073e1995365bfd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-09 11:56:03","canto_approved_date":"2022-02-03 20:43:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-09 11:55:53","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16H5.11c","SPAC17H9.09c","SPBC1604.14c","SPBC1D7.05","SPAC16E8.09","SPCC613.12c","SPAC110.03","SPAC22H10.07","SPAC14C4.03"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2014-12-09"},{"uniquename":"PMID:36650956","title":"The proline-rich domain of fission yeast WASp (Wsp1p) interacts with actin filaments and inhibits actin polymerization.","citation":"FEBS Lett 2023 Mar;597(5):672-681","abstract":"Members of the Wiskott-Aldrich Syndrome protein (WASp) family activate Arp2/3 complex (actin-related proteins 2 and 3 complex) to form actin filament branches. The proline-rich domain (PRD) of WASp contributes to branching nucleation, and the PRD of budding yeast Las17 binds actin filaments [Urbanek AN et al. (2013) Curr Biol 23, 196-203]. Biochemical assays showed the recombinant PRD of fission yeast Schizosaccharomyces pombe Wsp1p binds actin filaments with micromolar affinity. Recombinant PRDs of both Wsp1p and Las17p slowed the elongation of actin filaments by Mg-ATP-actin monomers by half and slowed the spontaneous polymerization of Mg-ATP-actin monomers modestly. The affinity of PRDs of WASp-family proteins for actin filaments is high enough to contribute to the reported stimulation of actin filament branching by Arp2/3 complex.","doi":"10.1002/1873-3468.14571","authors":"Rosenbloom AD, Pollard TD","authors_abbrev":"Rosenbloom AD et al.","pubmed_publication_date":"Mar 2023","pubmed_entrez_date":"2023-01-18","publication_year":"2023","canto_session_key":"c99db296880f5c98","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-01-19 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26160178","title":"Dimerization Mediated by a Divergent Forkhead-associated Domain Is Essential for the DNA Damage and Spindle Functions of Fission Yeast Mdb1.","citation":"J Biol Chem 2015 Aug 21;290(34):21054-21066","abstract":"MDC1 is a key factor of DNA damage response in mammalian cells. It possesses two phospho-binding domains. In its C terminus, a tandem BRCA1 C-terminal domain binds phosphorylated histone H2AX, and in its N terminus, a forkhead-associated (FHA) domain mediates a phosphorylation-enhanced homodimerization. The FHA domain of the Drosophila homolog of MDC1, MU2, also forms a homodimer but utilizes a different dimer interface. The functional importance of the dimerization of MDC1 family proteins is uncertain. In the fission yeast Schizosaccharomyces pombe, a protein sharing homology with MDC1 in the tandem BRCA1 C-terminal domain, Mdb1, regulates DNA damage response and mitotic spindle functions. Here, we report the crystal structure of the N-terminal 91 amino acids of Mdb1. Despite a lack of obvious sequence conservation to the FHA domain of MDC1, this region of Mdb1 adopts an FHA-like fold and is therefore termed Mdb1-FHA. Unlike canonical FHA domains, Mdb1-FHA lacks all the conserved phospho-binding residues. It forms a stable homodimer through an interface distinct from those of MDC1 and MU2. Mdb1-FHA is important for the localization of Mdb1 to DNA damage sites and the spindle midzone, contributes to the roles of Mdb1 in cellular responses to genotoxins and an antimicrotubule drug, and promotes in vitro binding of Mdb1 to a phospho-H2A peptide. The defects caused by the loss of Mdb1-FHA can be rescued by fusion with either of two heterologous dimerization domains, suggesting that the main function of Mdb1-FHA is mediating dimerization. Our data support that FHA-mediated dimerization is conserved for MDC1 family proteins.","doi":"10.1074/jbc.M115.642538","authors":"Luo S, Xin X, Du LL, Ye K, Wei Y","authors_abbrev":"Luo S et al.","pubmed_publication_date":"21 Aug 2015","pubmed_entrez_date":"2015-07-11","publication_year":"2015","canto_session_key":"d471b5535e0570fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li-Lin Du","canto_first_approved_date":"2015-08-24 17:25:23","canto_approved_date":"2019-02-22 09:47:58","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-08-21 07:50:29","canto_added_date":"2015-07-11 00:21:14","annotation_curators":[{"name":"Li-Lin Du","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPACUNK4.14","SPCC622.08c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-08-24","pdb_entries":[{"pdb_id":"4s3h","gene_chains":[{"gene_uniquename":"SPACUNK4.14","chain":"A/B/C/D","position":"1-104"}],"title":"Crystal structure of S. pombe Mdb1 FHA domain","entry_authors":"Luo S,Ye K","entry_authors_abbrev":"Luo S et al.","reference_uniquename":"PMID:26160178","experimental_method":"X-ray","resolution":"2.701"}]},{"uniquename":"PMID:19308705","title":"The unnamed complex: what do we know about Smc5-Smc6?","citation":"Chromosome Res 2009;17(2):251-63","abstract":"The structural maintenance of chromosome (SMC) proteins constitute the cores of three protein complexes involved in chromosome metabolism; cohesin, condensin and the Smc5-Smc6 complex. While the roles of cohesin and condensin in sister chromatid cohesion and chromosome condensation respectively have been described, the cellular function of Smc5-Smc6 is as yet not understood, consequently the less descriptive name. The complex is involved in a variety of DNA repair pathways. It contains activities reminiscent of those described for cohesin and condensin, as well as several DNA helicases and endonucleases. It is required for sister chromatid recombination, and smc5-smc6 mutants suffer from the accumulation of unscheduled recombination intermediates. The complex contains a SUMO-ligase and potentially an ubiquitin-ligase; thus Smc5-Smc6 might presently have a dull name, but it seems destined to be recognized as a key player in the maintenance of chromosome stability. In this review we summarize our present understanding of this enigmatic protein complex.","doi":"10.1007/s10577-008-9016-8","authors":"De Piccoli G, Torres-Rosell J, Aragón L","authors_abbrev":"De Piccoli G et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-03-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25543137","title":"Dicer and Hsp104 function in a negative feedback loop to confer robustness to environmental stress.","citation":"Cell Rep 2015 Jan 06;10(1):47-61","abstract":"Epigenetic mechanisms can be influenced by environmental cues and thus evoke phenotypic variation. This plasticity can be advantageous for adaptation but also detrimental if not tightly controlled. Although having attracted considerable interest, it remains largely unknown if and how environmental cues such as temperature trigger epigenetic alterations. Using fission yeast, we demonstrate that environmentally induced discontinuous phenotypic variation is buffered by a negative feedback loop that involves the RNase Dicer and the protein disaggregase Hsp104. In the absence of Hsp104, Dicer accumulates in cytoplasmic inclusions and heterochromatin becomes unstable at elevated temperatures, an epigenetic state inherited for many cell divisions after the heat stress. Loss of Dicer leads to toxic aggregation of an exogenous prionogenic protein. Our results highlight the importance of feedback regulation in building epigenetic memory and uncover Hsp104 and Dicer as homeostatic controllers that buffer environmentally induced stochastic epigenetic variation and toxic aggregation of prionogenic proteins.","doi":"10.1016/j.celrep.2014.12.006","authors":"Oberti D, Biasini A, Kirschmann MA, Genoud C, Stunnenberg R, Shimada Y, Bühler M","authors_abbrev":"Oberti D et al.","pubmed_publication_date":"06 Jan 2015","pubmed_entrez_date":"2014-12-29","publication_year":"2015","canto_session_key":"739f6a8893d0f034","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Daniele Oberti","canto_first_approved_date":"2015-09-18 13:38:34","canto_approved_date":"2025-09-03 17:05:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-30 11:33:10","canto_added_date":"2014-12-31 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Daniele Oberti","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.08c","SPAC19A8.12","SPCC188.13c","SPAC57A7.04c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-09-18"},{"uniquename":"PMID:31618856","title":"Two XMAP215/TOG Microtubule Polymerases, Alp14 and Dis1, Play Non-Exchangeable, Distinct Roles in Microtubule Organisation in Fission Yeast.","citation":"Int J Mol Sci 2019 Oct 15;20(20)","abstract":"Proper bipolar spindle assembly underlies accurate chromosome segregation. A cohort of microtubule-associated proteins orchestrates spindle microtubule formation in a spatiotemporally coordinated manner. Among them, the conserved XMAP215/TOG family of microtubule polymerase plays a central role in spindle assembly. In fission yeast, two XMAP215/TOG members, Alp14 and Dis1, share essential roles in cell viability; however how these two proteins functionally collaborate remains undetermined. Here we show the functional interplay and specification of Alp14 and Dis1. Creation of new mutant alleles of  alp14 , which display temperature sensitivity in the absence of Dis1, enabled us to conduct detailed analyses of a double mutant. We have found that simultaneous inactivation of Alp14 and Dis1 results in early mitotic arrest with very short, fragile spindles. Intriguingly, these cells often undergo spindle collapse, leading to a lethal \"cut\" phenotype. By implementing an artificial targeting system, we have shown that Alp14 and Dis1 are not functionally exchangeable and as such are not merely redundant paralogues. Interestingly, while Alp14 promotes microtubule nucleation, Dis1 does not. Our results uncover that the intrinsic specification, not the spatial regulation, between Alp14 and Dis1 underlies the collaborative actions of these two XMAP215/TOG members in mitotic progression, spindle integrity and genome stability.","doi":"10.3390/ijms20205108","authors":"Yukawa M, Kawakami T, Pinder C, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"15 Oct 2019","pubmed_entrez_date":"2019-10-18","publication_year":"2019","canto_session_key":"ecfa7f1ddeb87155","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2019-10-28 18:23:26","canto_approved_date":"2022-07-11 17:43:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-25 07:32:19","canto_added_date":"2019-10-19 00:15:04","annotation_curators":[{"name":"Takashi Toda","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.14","SPCC895.07","SPBC365.15","SPBC409.04c","SPAC23C11.16"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2019-10-28"},{"uniquename":"PMID:1356078","title":"Thialysine-resistant mutants and uptake of lysine in Schizosaccharomyces pombe.","citation":"Curr Genet 1992 Apr;21(4-5):351-5","abstract":"Mutants defective in lysine transport were isolated and characterized. After UV-mutagenesis colonies resistant to thialysine, a toxic analogue of lysine, were isolated and L-lysine uptake into the mutant strains was analyzed. Among the thialysine-resistant strains a group of mutants was found, where the half-saturation constant, KT, of the high-affinity transport system for lysine was higher than in the wild-type, the high-affinity transport system for basic amino acids being specifically affected. This was confirmed by a complementation test in which all the thialysine-resistant strains with a higher KT for lysine uptake belonged to one complementation group. Kinetic and genetic analysis showed that our mutants were identical with can1-1 mutants, showing that a single high-affinity system for the transport of basic amino acids exists in S. pombe.","authors":"Sychrová H, Chevallier MR, Horák J, Kotyk A","authors_abbrev":"Sychrová H et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"d3097b2d0f95917f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2015-01-08 15:32:34","canto_approved_date":"2023-03-15 17:31:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-13 13:11:23","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC18H10.20c","SPBC18H10.16"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2015-01-08"},{"uniquename":"PMID:22918578","title":"Evolutionary diversification of eukaryotic DNA replication machinery.","citation":"Subcell Biochem 2012;62:19-35","abstract":"DNA replication research to date has focused on model organisms such as the vertebrate Xenopus laevis and the yeast species Saccharomyces cerevisiae and Schizosaccharomyces pombe. However, animals and fungi both belong to the Opisthokonta, one of about six eukaryotic phylogenetic 'supergroups', and therefore represent only a fraction of eukaryotic diversity. To explore evolutionary diversification of the eukaryotic DNA replication machinery a bioinformatic approach was used to investigate the presence or absence of yeast/animal replisome components in other eukaryotic taxa. A comparative genomic survey was undertaken of 59 DNA replication proteins in a diverse range of 36 eukaryotes from all six supergroups. Twenty-three proteins including Mcm2-7, Cdc45, RPA1, primase, some DNA polymerase subunits, RFC1-5, PCNA and Fen1 are present in all species examined. A further 20 proteins are present in all six eukaryotic supergroups, although not necessarily in every species: with the exception of RNase H2B and the fork protection complex component Timeless/Tof1, all of these are members of anciently derived paralogous families such as ORC, MCM, GINS or RPA. Together these form a set of 43 proteins that must have been present in the last common eukaryotic ancestor (LCEA). This minimal LCEA replisome is significantly more complex than the related replisome in Archaea, indicating evolutionary events including duplications of DNA replication genes in the LCEA lineage which parallel the early evolution of other complex eukaryotic cellular features.","doi":"10.1007/978-94-007-4572-8_2","authors":"Aves SJ, Liu Y, Richards TA","authors_abbrev":"Aves SJ et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-25","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25963819","title":"Nucleocytoplasmic transport in the midzone membrane domain controls yeast mitotic spindle disassembly.","citation":"J Cell Biol 2015 May 11;209(3):387-402","abstract":"During each cell cycle, the mitotic spindle is efficiently assembled to achieve chromosome segregation and then rapidly disassembled as cells enter cytokinesis. Although much has been learned about assembly, how spindles disassemble at the end of mitosis remains unclear. Here we demonstrate that nucleocytoplasmic transport at the membrane domain surrounding the mitotic spindle midzone, here named the midzone membrane domain (MMD), is essential for spindle disassembly in Schizosaccharomyces pombe cells. We show that, during anaphase B, Imp1-mediated transport of the AAA-ATPase Cdc48 protein at the MMD allows this disassembly factor to localize at the spindle midzone, thereby promoting spindle midzone dissolution. Our findings illustrate how a separate membrane compartment supports spindle disassembly in the closed mitosis of fission yeast.","doi":"10.1083/jcb.201412144","authors":"Lucena R, Dephoure N, Gygi SP, Kellogg DR, Tallada VA, Daga RR, Jimenez J","authors_abbrev":"Lucena R et al.","pubmed_publication_date":"11 May 2015","pubmed_entrez_date":"2015-05-13","publication_year":"2015","canto_session_key":"1d9460b2fe58c1c2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rafael Lucena","canto_first_approved_date":"2016-03-04 09:35:55","canto_approved_date":"2026-05-27 11:28:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-05-27 09:08:19","canto_added_date":"2015-05-14 00:19:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Rafael Lucena","community_curator":true,"annotation_count":93,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.08","SPAC1834.03c","SPBC9B6.08","SPBP8B7.06","SPCC1183.08c","SPCC18B5.01c","SPCC962.03c","SPAC12G12.03","SPAC26F1.03","SPAC8C9.04","SPAC17H9.04c","SPCC1682.10","SPBC16A3.08c","SPBC26H8.05c","SPBC582.07c","SPBC106.06","SPAC1F5.02","SPAC2F3.06c","SPAC890.08","SPCC285.13c","SPAC12G12.02","SPAC1D4.14","SPCC1840.02c","SPAC1071.08","SPBC3D6.02","SPAC3H5.12c","SPAC1565.08","SPBC646.10c","SPAC1805.04","SPBC1773.09c","SPAC24B11.06c","SPAC15A10.09c","SPBC19F5.05c","SPAC1420.03","SPBC365.03c","SPCC1682.16","SPBC215.06c","SPCC1827.03c","SPCC364.06","SPAPB1A10.09","SPAC11E3.15","SPAC1F7.02c","SPBP8B7.20c","SPBC428.04","SPCC794.07","SPCP25A2.03","SPAC13G7.02c","SPAC589.10c","SPBC36.05c","SPBC3B9.13c","SPBC2F12.13","SPCC417.08","SPCC1795.11","SPAC1782.09c","SPBC1685.15c","SPAC22G7.05","SPAC30D11.03","SPBC26H8.08c","SPBC56F2.02","SPAC1B1.03c","SPBC3E7.02c","SPCC18B5.07c","SPCC320.13c","SPBC29A3.16","SPBC839.04","SPBC17D11.05","SPAC20G4.08","SPBC1604.08c","SPAC222.12c","SPAC589.06c","SPBC216.01c","SPBC2G2.08","SPBC405.05","SPBP4H10.15","SPBC19C7.10","SPBC4C3.05c","SPCC965.05c","SPAC821.05","SPBC651.01c","SPCC13B11.01","SPCC825.01","SPAC3A11.12c","SPBC557.03c","SPCC895.05","SPBC13A2.04c","SPAC2F3.03c","SPAC30D11.04c","SPBC2G5.06c","SPBC776.15c","SPCP1E11.09c","SPBC30D10.13c"],"gene_count":91,"ltp_gene_count":91,"approved_date":"2016-03-04"},{"uniquename":"EMBL:AU012855","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10455235","title":"Schizosaccharomyces pombe homologue of glutathione peroxidase, which does not contain selenocysteine, is induced by several stresses and works as an antioxidant.","citation":"Yeast 1999 Aug;15(11):1125-32","abstract":"We have cloned a gene of Schizosaccharomyces pombe homologues to the glutathione peroxidase gene. The cloned gene, named gpx1(+), encoded a protein that was 158 amino acids in length and had a molecular mass of 18 kDa. The gpx1(+) gene is homologous with many glutathione peroxidase genes but the selenocysteine codon (UGA) position of mammalian genes is a cysteine codon (UGU) in S. pombe. gpx1(+) mRNA was induced by various stresses, including oxidative stress, osmostress and heat stress. These stresses activate the Wis1-Sty1/Spc1 MAP kinase cascade in S. pombe. Transcriptional factors Atf1 and Pap1 are under the control of this MAP kinase. In the disruption of the atf1(+) gene, gpx1(+) was not transcribed or induced. However, the expression of gpx1(+) was not affected by the disruption of the pap1(+) gene. These results indicated that gpx1(+) was under the control of transcription factor Atf1. Catalase can detoxicate H(2)O(2) in the same way as GPx and the disruptant of the catalase gene of S. pombe is hypersensitive to H(2)O(2). The catalase gene disruptant of S. pombe harbouring multicopy plasmid containing gpx1(+) restored the hypersensitivity to H(2)O(2) of the catalase gene disruptant. These results suggest that Gpx1 acts as a scavenger of H(2)O(2) in vivo.","authors":"Yamada K, Nakagawa CW, Mutoh N","authors_abbrev":"Yamada K et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-08-24","publication_year":"1999","canto_session_key":"32450f2b6ffd928f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-06 20:36:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-06 20:36:00","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPCC757.07c","SPAC1783.07c","SPBC32F12.03c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-01-06"},{"uniquename":"PMID:33176152","title":"Acute Heat Stress Leads to Reversible Aggregation of Nuclear Proteins into Nucleolar Rings in Fission Yeast.","citation":"Cell Rep 2020 Nov 10;33(6):108377","abstract":"Upon acute heat stress (HS), overall mRNA transcription, processing, and export are inhibited, leading to cell growth arrest. However, how cells turn off mRNA metabolism is not fully understood. Here, we show that acute HS results in the segregation and aggregation of multiple nuclear and nucleolar proteins into ring-like structures located at the nucleolar periphery (nucleolar rings [NuRs]). NuRs sequester essential factors required for nuclear mRNA metabolism and nuclear pore complex function, as well as cell-cycle regulators. When cells are switched back to growing temperatures, NuRs disaggregate, and their components relocate to their functional environments in an Hsf1- and Hsp104-dependent manner, and concomitantly with the reinitiation of cell growth. These findings highlight the contribution of reversible protein aggregation to the inhibition of overall RNA-related activities in the nucleus and its functional relevance in the maintenance of cellular homeostasis during acute HS.","doi":"10.1016/j.celrep.2020.108377","authors":"Gallardo P, Real-Calderón P, Flor-Parra I, Salas-Pino S, Daga RR","authors_abbrev":"Gallardo P et al.","pubmed_publication_date":"10 Nov 2020","pubmed_entrez_date":"2020-11-11","publication_year":"2020","canto_session_key":"96b76559a6d410c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silvia Salas-Pino","canto_first_approved_date":"2021-04-27 16:15:17","canto_approved_date":"2021-09-27 16:23:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-21 11:30:45","canto_added_date":"2020-11-13 01:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Silvia Salas-Pino","community_curator":true,"annotation_count":24,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC15D4.10c","SPBC16E9.12c","SPBP35G2.06c","SPAC1486.04c","SPCC320.13c","SPBC776.13","SPAC23C11.16","SPAC1782.09c","SPBC17G9.04c","SPBC1198.11c","SPAC13G7.02c","SPCC1739.13","SPAC2E12.02","SPBC582.03","SPAC644.12","SPBC16D10.08c","SPBC1921.03c","SPBC8D2.04","SPAC1805.04","SPCC162.08c","SPAC1006.03c","SPAC1F3.01"],"gene_count":22,"ltp_gene_count":22,"approved_date":"2021-04-27"},{"uniquename":"PMID:8628681","title":"The gamma subfamily of DNA polymerases: cloning of a developmentally regulated cDNA encoding Xenopus laevis mitochondrial DNA polymerase gamma.","citation":"Nucleic Acids Res 1996 Apr 15;24(8):1481-8","abstract":"We used the known sequence of the Saccharomyces cerevisiae DNA polymerase gamma to clone the genes or cDNAs encoding this enzyme in two other yeasts, Pychia pastoris and Schizosaccharomyces pombe, and one higher eukaryote, Xenopus laevis. To confirm the identity of the final X.laevis clone, two antisera raised against peptide sequences were shown to react with DNA polymerase gamma purified from X.laevis oocyte mitochondria. A developmentally regulated 4.6 kb mRNA is recognized on Northern blots of oocyte RNA using the X.laevis cDNA. Comparison of the four DNA polymerase gamma gene sequences revealed several highly conserved sequence blocks, comprising an N-terminal 3'-->5'exonuclease domain and a C-terminal polymerase active center interspersed with gamma-specific gene sequences. The consensus sequences for the DNA polymerase gamma exonuclease and polymerase domains show extensive sequence similarity to DNA polymerase I from Escherichia coli. Sequence conservation is greatest for residues located near the active centers of the exo and pol domains of the E.coli DNA polymerase I structure. The domain separating the exonuclease and polymerase active sites is larger in DNA polymerase gamma than in other members of family A (DNA polymerase I-like) polymerases. The S.cerevisiae DNA polymerase gamma is atypical in that it includes a 240 residue C-terminal extension that is not found in the other members of the DNA polymerase gamma family, or in other family A DNA polymerases.","authors":"Ye F, Carrodeguas JA, Bogenhagen DF","authors_abbrev":"Ye F et al.","pubmed_publication_date":"15 Apr 1996","pubmed_entrez_date":"1996-04-15","publication_year":"1996","canto_session_key":"be0d7574891b4e6b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 15:12:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 15:01:49","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.22"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-07-31"},{"uniquename":"PMID:19962315","title":"The F-BAR protein Syp1 negatively regulates WASp-Arp2/3 complex activity during endocytic patch formation.","citation":"Curr Biol 2009 Dec 15;19(23):1979-87","abstract":"Actin polymerization by Arp2/3 complex must be tightly regulated to promote clathrin-mediated endocytosis. Although many Arp2/3 complex activators have been identified, mechanisms for its negative regulation have remained more elusive. To address this, we analyzed the yeast arp2-7 allele, which is biochemically unique in causing unregulated actin assembly in vitro in the absence of Arp2/3 activators.\nWe examined endocytosis in arp2-7 mutants by live-cell imaging of Sla1-GFP, a coat marker, and Abp1-RFP, which marks the later actin phase of endocytosis. Sla1-GFP and Abp1-RFP lifetimes were accelerated in arp2-7 mutants, which is opposite to actin nucleation-impaired arp2 alleles or deletions of Arp2/3 activators. We performed a screen for multicopy suppressors of arp2-7 and identified SYP1, an FCHO1 homolog, which contains F-BAR and AP-2micro homology domains. Overexpression of SYP1 in arp2-7 cells slowed Sla1-GFP lifetimes closer to wild-type cells. Further, purified Syp1 directly inhibited Las17/WASp stimulation of Arp2/3 complex-mediated actin assembly in vitro. This activity was mapped to a fragment of Syp1 located between its F-BAR and AP-2micro homology domains and depends on sequences in Las17/WASp outside of the VCA domain.\nTogether, these data identify Syp1 as a novel negative regulator of WASp-Arp2/3 complex that helps choreograph the precise timing of actin assembly during endocytosis.","doi":"10.1016/j.cub.2009.10.062","authors":"Boettner DR, D'Agostino JL, Torres OT, Daugherty-Clarke K, Uygur A, Reider A, Wendland B, Lemmon SK, Goode BL","authors_abbrev":"Boettner DR et al.","pubmed_publication_date":"15 Dec 2009","pubmed_entrez_date":"2009-12-08","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-04-23 17:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38633868","title":"Generation and characterization of temperature-sensitive alleles encoding GPI anchored proteins Psu1 and Dfg502 in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2024;2024","abstract":"Glycosyl-phosphatidylinositol (GPI) anchored proteins are implicated in remodeling of the yeast cell wall during growth and division.  Schizosaccharomyces pombe  proteins, Psu1 , Dfg501 , and Dfg502 are predicted GPI anchored proteins with likely cell wall modifying activity. Here, we isolated and characterized null and temperature-sensitive alleles that will allow further analysis of the function of these proteins and  S. pombe  cell wall formation. Our data confirm that Psu1 is necessary for cell separation, maintaining proper cell shape, and viability. Additionally, we found that Dfg501 and Dfg502 share a redundant and essential function necessary for cell separation and viability.","doi":"10.17912/micropub.biology.001179","authors":"Tavafoghi B, Ren L, Gould KL, Willet AH","authors_abbrev":"Tavafoghi B et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-04-18","publication_year":"2024","canto_session_key":"8e996dc517973af5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2024-04-22 07:32:56","canto_approved_date":"2026-01-22 13:07:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-22 00:16:05","canto_added_date":"2024-04-18 23:25:05","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":8,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.06c","SPBC1198.07c","SPAC1002.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2024-04-22"},{"uniquename":"PMID:10428959","title":"Sin1: an evolutionarily conserved component of the eukaryotic SAPK pathway.","citation":"EMBO J 1999 Aug 02;18(15):4210-21","abstract":"The fission yeast Sty1/Spc1 mitogen-activated protein (MAP) kinase is a member of the eukaryotic stress-activated MAP kinase (SAPK) family. We have identified a protein, Sin1, that interacts with Sty1/Spc1 which is a member of a new evolutionarily conserved gene family. Cells lacking Sin1 display many, but not all, of the phenotypes of cells lacking the Sty1/Spc1 MAP kinase including sterility, multiple stress sensitivity and a cell-cycle delay. Sin1 is phosphorylated after stress but this is not Sty1/Spc1-dependent. Importantly, Sin1 is not required for activation of Sty1/Spc1 but is required for stress-dependent transcription via its substrate, Atf1. We find that in the absence of Sin1, Sty1/Spc1 appears to translocate to the nucleus but Atf1 is not fully phosphorylated and becomes unstable in response to environmental stress. Sin1 is also required for effective transcription via the AP-1 factor Pap1 but does not prevent its nuclear translocation. Remarkably chimaeric fusions of sin1 with chicken sin1 sequences rescue loss of sin1 function. We conclude that Sin1 is a novel component of the eukaryotic SAPK pathway.","authors":"Wilkinson MG, Pino TS, Tournier S, Buck V, Martin H, Christiansen J, Wilkinson DG, Millar JB","authors_abbrev":"Wilkinson MG et al.","pubmed_publication_date":"02 Aug 1999","pubmed_entrez_date":"1999-08-03","publication_year":"1999","canto_session_key":"47cceba0fa44ef05","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-06-10 07:33:31","canto_approved_date":"2025-09-02 20:32:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-25 18:26:09","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPBC215.05","SPAPYUG7.02c","SPBC29B5.01","SPBC3F6.03","SPAC24B11.06c","SPCC757.07c","SPAC19D5.01"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2021-06-10"},{"uniquename":"PMID:15576681","title":"Genetics of lagging strand DNA synthesis and maturation in fission yeast: suppression analysis links the Dna2-Cdc24 complex to DNA polymerase delta.","citation":"Nucleic Acids Res 2004;32(21):6367-77","abstract":"The Cdc24 protein is essential for the completion of chromosomal DNA replication in fission yeast. Although its precise role in this process is unclear, Cdc24 forms a complex with Dna2, a conserved endonuclease-helicase implicated in the removal of the RNA-DNA primer during Okazaki fragment processing. To gain further insights into Cdc24-Dna2 function, we screened for chromosomal suppressors of the temperature-sensitive cdc24-M38 allele and mapped the suppressing mutations into six complementation groups. Two of these mutations defined genes encoding the Pol3 and Cdc27 subunits of DNA polymerase delta. Sequence analysis revealed that all the suppressing mutations in Cdc27 resulted in truncation of the protein and loss of sequences that included the conserved C-terminal PCNA binding motif, previously shown to play an important role in maximizing enzyme processivity in vitro. Deletion of this motif is shown to be sufficient for suppression of both cdc24-M38 and dna2-C2, a temperature-sensitive allele of dna2(+), suggesting that disruption of the interaction between Cdc27 and PCNA renders the activity of the Cdc24-Dna2 complex dispensable.","authors":"Tanaka H, Ryu GH, Seo YS, MacNeill SA","authors_abbrev":"Tanaka H et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-12-04","publication_year":"2004","canto_session_key":"e976a54955ad43a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-13 14:39:02","canto_approved_date":"2026-01-29 16:33:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-31 16:43:47","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":56,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.02c","SPCC584.04","SPAC1834.01","SPAC8F11.07c","SPCC18B5.06","SPBC336.04","SPBC16D10.04c","SPBC887.14c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2017-01-13"},{"uniquename":"PMID:26366556","title":"Fission Yeast CSL Transcription Factors: Mapping Their Target Genes and Biological Roles.","citation":"PLoS One 2015;10(9):e0137820","abstract":"Cbf11 and Cbf12, the fission yeast CSL transcription factors, have been implicated in the regulation of cell-cycle progression, but no specific roles have been described and their target genes have been only partially mapped.\nUsing a combination of transcriptome profiling under various conditions and genome-wide analysis of CSL-DNA interactions, we identify genes regulated directly and indirectly by CSL proteins in fission yeast. We show that the expression of stress-response genes and genes that are expressed periodically during the cell cycle is deregulated upon genetic manipulation of cbf11 and/or cbf12. Accordingly, the coordination of mitosis and cytokinesis is perturbed in cells with genetically manipulated CSL protein levels, together with other specific defects in cell-cycle progression. Cbf11 activity is nutrient-dependent and Δcbf11-associated defects are mitigated by inactivation of the protein kinase A (Pka1) and stress-activated MAP kinase (Sty1p38) pathways. Furthermore, Cbf11 directly regulates a set of lipid metabolism genes and Δcbf11 cells feature a stark decrease in the number of storage lipid droplets.\nOur results provide a framework for a more detailed understanding of the role of CSL proteins in the regulation of cell-cycle progression in fission yeast.","doi":"10.1371/journal.pone.0137820","authors":"Převorovský M, Oravcová M, Tvarůžková J, Zach R, Folk P, Půta F, Bähler J","authors_abbrev":"Převorovský M et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-09-15","publication_year":"2015","canto_session_key":"7f8b3d85a47ad977","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Martin Převorovský","canto_first_approved_date":"2017-06-02 10:12:19","canto_approved_date":"2025-09-03 16:19:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-22 10:19:28","canto_added_date":"2015-09-16 00:19:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Martin Převorovský","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1450.16c","SPCC736.08","SPAC56E4.04c","SPAC22A12.06c","SPCC1281.06c","SPBC106.10","SPCC1223.13","SPBC18H10.02","SPBP4H10.11c","SPAC24B11.06c"],"gene_count":10,"ltp_gene_count":3,"approved_date":"2017-06-02"},{"uniquename":"PMID:15247218","title":"A cooperative role for Atf1 and Pap1 in the detoxification of the oxidative stress induced by glucose deprivation in Schizosaccharomyces pombe.","citation":"J Biol Chem 2004 Oct 01;279(40):41594-602","abstract":"In Schizosaccharomyces pombe, glucose concentrations below a certain threshold trigger the stress-activated protein kinase (SAPK) signal transduction pathway and promote increased transcription of Atf1-dependent genes coding for the general stress response. Removal of glucose specifically induces the nuclear accumulation of green fluorescent protein-labeled Pap1 (GFP-Pap1) and the expression of genes dependent on this transcription factor. In contrast, depletion of the nitrogen source triggers the SAPK pathway but does not activate Pap1-dependent gene transcription, indicating that carbon stress rather than growth arrest leads to an endogenous oxidative condition that favors nuclear accumulation of Pap1. The reductant agents glutathione or N-acetylcysteine suppress the nuclear accumulation of GFP-Pap1 induced by glucose deprivation without inhibiting the activation of the MAPK Sty1. In addition, cells expressing a mutant GFP-Pap1 unable to accumulate into the nucleus upon hydrogen peroxide-mediated oxidative stress failed to show this protein into the nucleus in the absence of glucose. These results support the concept of a concerted action between the SAPK pathway and the Pap1 transcription factor during glucose exhaustion by which glucose limitation induces activation of the SAPK pathway prior to the oxidative stress caused by glucose deprivation. The ensuing induction of Atf1-dependent genes (catalase) decreases the level of hydroperoxides allowing Pap1 nuclear accumulation and function. Congruent with this interpretation, glucose-depleted cells show higher adaptive response to exogenous oxidative stress than those maintained in the presence of glucose.","authors":"Madrid M, Soto T, Franco A, Paredes V, Vicente J, Hidalgo E, Gacto M, Cansado J","authors_abbrev":"Madrid M et al.","pubmed_publication_date":"01 Oct 2004","pubmed_entrez_date":"2004-07-13","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU013708","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20705581","title":"DNA replication origins, ORC/DNA interaction, and assembly of pre-replication complex in eukaryotes.","citation":"Acta Biochim Biophys Sin (Shanghai) 2010 Jul;42(7):433-9","abstract":"Chromosomal DNA replication in eukaryotic cells is highly complicated and sophisticatedly regulated. Owing to its large size, a typical eukaryotic genome contains hundreds to tens of thousands of initiation sites called DNA replication origins where DNA synthesis takes place. Multiple initiation sites remove the constraint of a genome size because only a certain amount of DNA can be replicated from a single origin in a limited time. The activation of these multiple origins must be coordinated so that each segment of chromosomal DNA is precisely duplicated only once per cell cycle. Although DNA replication is a vital process for cell growth and its mechanism is highly conserved, recent studies also reveal significant diversity in origin structure, assembly of pre-replication complex (pre-RC) and regulation of replication initiation along evolutionary lines. The DNA replication origins in the fission yeast Schizosaccharomyces pombe are found to contain a second essential element that is bound by Sap1 protein besides the essential origin recognition complex-binding site. Sap1 is recently demonstrated to be a novel replication initiation protein that plays an essential role in loading the initiation protein Cdc18 to origins and thus directly participates in pre-RC formation. In this review, we summarize the recent advance in understanding how DNA replication origins are organized, how pre-RC is assembled and how DNA replication is initiated and regulated in yeast and metazoans.","doi":"10.1093/abbs/gmq048","authors":"Sun J, Kong D","authors_abbrev":"Sun J et al.","pubmed_publication_date":"Jul 2010","pubmed_entrez_date":"2010-08-14","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21237269","title":"Fission yeast Schizosaccharomyces pombe as a new system for the investigation of corticosterone methyloxidase deficiency-causing mutations.","citation":"J Steroid Biochem Mol Biol 2011 Mar;124(1-2):31-7","abstract":"The aldosterone synthase, CYP11B2, catalyses the conversion of 11-deoxycorticosterone to aldosterone, a process that requires three steps: a hydroxylation at position 11β to form corticosterone, another one at position 18 to produce 18-hydroxycorticosterone, and, finally, an oxidation at position 18 to form aldosterone. Aldosterone synthase deficiency usually finds its expression in infancy as a life-threatening electrolyte imbalance, caused by mutations in the CYP11B2 gene. Therefore, in depth studies of mutations and their enzymatic activities will provide information for the diagnosis and management of hypoaldosteronism caused by CYP11B2 deficiencies. Here, we report the development of a fast and cheap whole-cell technology for the enzymatic characterisation of CYP11B2 mutations. The principle of the new system is the heterologous expression of the mutants of CYP11B2 in fission yeast (Schizosaccharomyces pombe) followed by steroid bioconversion assays for the enzymatic characterisation of the investigated mutants. The new system was validated and 10 known mutations of CYP11B2 have been investigated, two of them for the first time concerning their effect on the CYP11B2 three-step reaction. The results of the fission yeast system were in good agreement with the cell culture results presenting this new system as an alternative non radioactive method that can be applied for the enzymatic characterisation of CYP11B2 mutations.","doi":"10.1016/j.jsbmb.2011.01.002","authors":"Tin MK, Hakki T, Bernhardt R","authors_abbrev":"Tin MK et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-01-18","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36043331","title":"Fission yeast Ish1 and Les1 interact with each other in the lumen of the nuclear envelope.","citation":"Genes Cells 2022 Nov;27(11):643-656","abstract":"The nuclear envelope (NE) provides a permeable barrier that separates the eukaryotic genome from the cytoplasm. NE is a double membrane composed of inner and outer nuclear membranes. Ish1 is a stress-responsive NE protein in the fission yeast, Schizosaccharomyces pombe. Les1 is another NE protein that shares several similar domains with Ish1, but the relationship between them remains unknown. In this study, using fluorescence and electron microscopy, we found that most regions of these proteins were localized within the NE lumen. We also found that Ish1 interacted with Les1 via its C-terminal region in the NE lumen and that the NE localization of Ish1 depended on the C-terminal region of Les1. Ish1 and Les1 were co-localized at the NE in interphase cells, but when the nucleus divided at the end of mitosis (closed mitosis), they showed distinguishable localization at the midzone membrane domain. These results suggest the regulated interaction between Ish1 and Les1 in the NE lumen, although this interaction does not appear to be essential for cell survival.","doi":"10.1111/gtc.12981","authors":"Asakawa H, Hirano Y, Shindo T, Haraguchi T, Hiraoka Y","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"Nov 2022","pubmed_entrez_date":"2022-08-31","publication_year":"2022","canto_session_key":"0fe1144741ae8e33","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.05c","SPBC365.12c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:2178610","title":"Fission yeast cdc25 is a cell-cycle regulated protein.","citation":"Biochem Biophys Res Commun 1990 Feb 28;167(1):301-9","abstract":"Fission yeast cell division is initiated by the cdc2/cdc13-cyclin protein kinase which in its catalytically active state comprises the mitotic inducer. During interphase the cdc2/cyclin complex is assembled in an inactive state that requires cdc25+ gene function for M-phase activation. The cdc25+ product, a 76 kd phosphoprotein, is shown to oscillate in abundance during the cell cycle, reaching a peak at G2/M, and to be sensitive to nitrogen starvation. The level of cdc25 is subject to feedback regulation involving both cdc25 and cdc2.","authors":"Ducommun B, Draetta G, Young P, Beach D","authors_abbrev":"Ducommun B et al.","pubmed_publication_date":"28 Feb 1990","pubmed_entrez_date":"1990-02-28","publication_year":"1990","canto_session_key":"daa8d9bd0cad0945","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-06 13:48:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-05 18:14:01","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-03-05"},{"uniquename":"EMBL:Z29366","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12556522","title":"Defining the active site of Schizosaccharomyces pombe C-terminal domain phosphatase Fcp1.","citation":"J Biol Chem 2003 Apr 18;278(16):13627-32","abstract":"Fcp1 is an essential protein serine phosphatase that dephosphorylates the C-terminal domain (CTD) of RNA polymerase II. By testing the effects of serial N- and C-terminal deletions of the 723-amino acid Schizosaccharomyces pombe Fcp1, we defined a minimal phosphatase domain spanning amino acids 156-580. We employed site-directed mutagenesis (introducing 24 mutations at 14 conserved positions) to locate candidate catalytic residues. We found that alanine substitutions for Arg(223), Asp(258), Lys(280), Asp(297), and Asp(298) abrogated the phosphatase activity with either p-nitrophenyl phosphate or CTD-PO(4) as substrates. Structure-activity relationships were determined by introducing conservative substitutions at each essential position. Our results, together with previous mutational studies, highlight a constellation of seven amino acids (Asp(170), Asp(172), Arg(223), Asp(258), Lys(280), Asp(297), and Asp(298)) that are conserved in all Fcp1 orthologs and likely comprise the active site. Five of these residues (Asp(170), Asp(172), Lys(280), Asp(297), and Asp(298)) are conserved at the active site of T4 polynucleotide 3'-phosphatase, suggesting that Fcp1 and T4 phosphatase are structurally and mechanistically related members of the DXD phosphotransferase superfamily.","authors":"Hausmann S, Shuman S","authors_abbrev":"Hausmann S et al.","pubmed_publication_date":"18 Apr 2003","pubmed_entrez_date":"2003-01-31","publication_year":"2003","canto_session_key":"15ee54d35bd94b18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-19 17:03:51","canto_approved_date":"2023-03-17 07:15:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-19 17:03:44","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19B12.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-19"},{"uniquename":"PMID:6624143","title":"[Purification and isolation of the arom aggregates of Schizosaccharomyces pombe].","citation":"Z Allg Mikrobiol 1983;23(5):289-96","abstract":"The five enzymes that catalyzing steps two through six in the prechorismate polyaromatic amino acid biosynthetic pathway are physically associated and have been purified up to 400-fold from Schizosaccharomyces pombe. The native arom aggregate has a molecular weight of approx. 140,000-145,000 based on gel filtration, glycerol-density-gradient centrifugation, and polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. Similarities between the S. pombe arom aggregate and that of Neurospora crassa and Euglena gracilis are discussed.","authors":"Bode R, Kunze G","authors_abbrev":"Bode R et al.","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-01-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR002775","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YGR030C","SPAC1805.18","SPBP8B7.01c","HGNC:30361","HGNC:19909","HGNC:19949","YBR167C"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:24081329","title":"Poly(A) tail-mediated gene regulation by opposing roles of Nab2 and Pab2 nuclear poly(A)-binding proteins in pre-mRNA decay.","citation":"Mol Cell Biol 2013 Dec;33(23):4718-31","abstract":"The 3' end of most eukaryotic transcripts is decorated by poly(A)-binding proteins (PABPs), which influence the fate of mRNAs throughout gene expression. However, despite the fact that multiple PABPs coexist in the nuclei of most eukaryotes, how functional interplay between these nuclear PABPs controls gene expression remains unclear. By characterizing the ortholog of the Nab2/ZC3H14 zinc finger PABP in Schizosaccharomyces pombe, we show here that the two major fission yeast nuclear PABPs, Pab2 and Nab2, have opposing roles in posttranscriptional gene regulation. Notably, we find that Nab2 functions in gene-specific regulation in a manner opposite to that of Pab2. By studying the ribosomal-protein-coding gene rpl30-2, which is negatively regulated by Pab2 via a nuclear pre-mRNA decay pathway that depends on the nuclear exosome subunit Rrp6, we show that Nab2 promotes rpl30-2 expression by acting at the level of the unspliced pre-mRNA. Our data support a model in which Nab2 impedes Pab2/Rrp6-mediated decay by competing with Pab2 for polyadenylated transcripts in the nucleus. The opposing roles of Pab2 and Nab2 reveal that interplay between nuclear PABPs can influence gene regulation.","doi":"10.1128/MCB.00887-13","authors":"Grenier St-Sauveur V, Soucek S, Corbett AH, Bachand F","authors_abbrev":"Grenier St-Sauveur V et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-10-02","publication_year":"2013","canto_session_key":"d68db45202ee441d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"François Bachand","canto_first_approved_date":"2015-09-15 12:32:54","canto_approved_date":"2025-09-04 06:48:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-11 16:30:06","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"François Bachand","community_curator":true,"annotation_count":44,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":38,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.12c","SPBC16H5.10c","SPAC9.03c","SPAC4F8.12c","SPAC27D7.07c","SPAC1782.10c","SPAC2C4.03c","SPAC14C4.06c","SPAC16C9.06c","SPBC1289.11","SPBC3E7.14","SPBC146.07","SPBC4B4.09","SPAC607.03c","SPCC188.11","SPAC1250.05","SPBC6B1.07","SPBC2D10.10c","SPAC22F8.10c","SPAC22A12.09c","SPAC644.12","SPAPJ698.03c","SPSNORNA.35","SPBC651.01c","SPBP22H7.07","SPBC337.06c","SPBC20F10.01","SPBC646.10c","SPSNORNA.32","SPAC29E6.08","SPAC9G1.03c","SPAC27F1.09c","SPBP8B7.20c","SPBC13E7.01","SPAC6F12.16c","SPBC16E9.12c","SPBC31F10.11c","SPCC1183.07","SPAC26A3.08","SPAC29A4.04c","SPAC1F3.01","SPBC119.13c","SPBC19C2.14","SPAC1071.10c","SPAC29A4.08c","SPAC17H9.02","SPBC646.02","SPBC6B1.10","SPAC23G3.06","SPBC215.12","SPBC1861.08c","SPBC211.02c","SPBC776.08c"],"gene_count":53,"ltp_gene_count":49,"approved_date":"2015-09-15"},{"uniquename":"PMID:25347204","title":"Formation of [4Fe-4S] clusters in the mitochondrial iron-sulfur cluster assembly machinery.","citation":"J Am Chem Soc 2014 Nov 19;136(46):16240-50","abstract":"The generation of [4Fe-4S] clusters in mitochondria critically depends, in both yeast and human cells, on two A-type ISC proteins (in mammals named ISCA1 and ISCA2), which perform a nonredundant functional role forming in vivo a heterocomplex. The molecular function of ISCA1 and ISCA2 proteins, i.e., how these proteins help in generating [4Fe-4S] clusters, is still unknown. In this work we have structurally characterized the Fe/S cluster binding properties of human ISCA2 and investigated in vitro whether and how a [4Fe-4S] cluster is assembled when human ISCA1 and ISCA2 interact with the physiological [2Fe-2S](2+) cluster-donor human GRX5. We found that (i) ISCA2 binds either [2Fe-2S] or [4Fe-4S] cluster in a dimeric state, and (ii) two molecules of [2Fe-2S](2+) GRX5 donate their cluster to a heterodimeric ISCA1/ISCA2 complex. This complex acts as an \"assembler\" of [4Fe-4S] clusters; i.e., the two GRX5-donated [2Fe-2S](2+) clusters generate a [4Fe-4S](2+) cluster. The formation of the same [4Fe-4S](2+) cluster-bound heterodimeric species is also observed by having first one [2Fe-2S](2+) cluster transferred from GRX5 to each individual ISCA1 and ISCA2 proteins to form [2Fe-2S](2+) ISCA2 and [2Fe-2S](2+) ISCA1, and then mixing them together. These findings imply that such heterodimeric complex is the functional unit in mitochondria receiving [2Fe-2S] clusters from hGRX5 and assembling [4Fe-4S] clusters before their transfer to the final target apo proteins.","doi":"10.1021/ja507822j","authors":"Brancaccio D, Gallo A, Mikolajczyk M, Zovo K, Palumaa P, Novellino E, Piccioli M, Ciofi-Baffoni S, Banci L","authors_abbrev":"Brancaccio D et al.","pubmed_publication_date":"19 Nov 2014","pubmed_entrez_date":"2014-10-28","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC21E11.07","SPCC645.03c","SPBC3B9.17","SPAPB2B4.02"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:2446871","title":"The mitochondrial genome of the fission yeast, Schizosaccharomyces pombe. Sequence of the large-subunit ribosomal RNA gene, comparison of potential secondary structure in fungal mitochondrial large-subunit rRNAs and evolutionary considerations.","citation":"Eur J Biochem 1987 Dec 15;169(3):527-37","abstract":"The DNA sequence of the mitochondrial large subunit (LSU) rRNA gene of Schizosaccharomyces pombe has been determined. In the direction of transcription, this gene is located between the gene coding for subunit II of cytochrome oxidase and a cluster of three tRNA genes. Both the 5' and 3' ends of the LSU rRNA have been mapped precisely: whereas the 5' end can be assigned unambiguously to a single nucleotide position, multiple 3' ends occur within a run of eight U residues. Based on these results, the S. pombe LSU rRNA is between 2818 and 2826 nucleotides long. A sequence motif immediately upstream of the 5' end of the gene resembles that of the mitochondrial promoter motif of Saccharomyces cerevisiae; however, the sequence at the 3' end of the gene is not similar to any of the motifs implicated as processing signals in other mitochondrial systems. Unlike its counterparts in S. cerevisiae and Aspergillus nidulans, the mitochondrial LSU rRNA gene of S. pombe does not contain an intron. Comparison of potential secondary structure among the three fungal mitochondrial and Escherichia coli LSU rRNAs has defined a common secondary structure core, held together by long-range hydrogen-bonding interactions. A 5.8S-like structure is present within the 5'-terminal region of all three fungal mitochondrial LSU rRNAs; in contrast, no 4.5S-like structure is evident at the 3' end of these molecules. An evolutionary evaluation of highly conserved regions of a small set of LSU rRNA sequences suggests that S. pombe mitochondria diverged from a mitochondrial proto-fungal branch earlier than either A. nidulans or S. cerevisiae mitochondria. This result, considered in conjunction with the patterns of genome organization and codon usage in fungal mitochondria, points to a slower evolutionary clock speed in the mitochondrial genome of S. pombe.","authors":"Lang BF, Cedergren R, Gray MW","authors_abbrev":"Lang BF et al.","pubmed_publication_date":"15 Dec 1987","pubmed_entrez_date":"1987-12-15","publication_year":"1987","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32743131","title":"Fission yeast cell wall biosynthesis and cell integrity signalling.","citation":"Cell Surf 2018 Dec;4:1-9","abstract":"The cell wall is a structure external to the plasma membrane that is essential for the survival of the fungi. This polysaccharidic structure confers resistance to the cell internal turgor pressure and protection against mechanical injury. The fungal wall is also responsible for the shape of these organisms due to different structural polysaccharides, such as β-(1,3)-glucan, which form fibers and confer rigidity to the cell wall. These polysaccharides are not present in animal cells and therefore they constitute excellent targets for antifungal chemotherapies. Cell wall damage leads to the activation of MAPK signaling pathways, which respond to the damage by activating the repair of the wall and the maintenance of the cell integrity. Fission yeast  Schizosaccharomyces pombe  is a model organism for the study morphogenesis, cell wall, and how different inputs might regulate this structure. We present here a short overview of the fission yeast wall composition and provide information about the main biosynthetic activities that assemble this cell wall. Additionally, we comment the recent advances in the knowledge of the cell wall functions and discuss the role of the cell integrity MAPK signaling pathway in the regulation of fission yeast wall.","doi":"10.1016/j.tcsw.2018.10.001","authors":"Pérez P, Cortés JCG, Cansado J, Ribas JC","authors_abbrev":"Pérez P et al.","pubmed_publication_date":"Dec 2018","pubmed_entrez_date":"2020-08-04","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-08-06 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22640989","title":"Pds5 promotes cohesin acetylation and stable cohesin-chromosome interaction.","citation":"EMBO Rep 2012 Jun 29;13(7):645-52","abstract":"Pds5 and Wpl1 act as anti-establishment factors preventing sister-chromatid cohesion until counteracted in S-phase by the cohesin acetyl-transferase Eso1. However, Pds5 is also required to maintain sister-chromatid cohesion in G2. Here, we show that Pds5 is essential for cohesin acetylation by Eso1 and ensures the maintenance of cohesion by promoting a stable cohesin interaction with replicated chromosomes. The latter requires Eso1 only in the presence of Wapl, indicating that cohesin stabilization relies on Eso1 only to neutralize the anti-establishment activity. We suggest that Eso1 requires Pds5 to counteract anti-establishment. This allows both cohesion establishment and Pds5-dependent stable cohesin binding to chromosomes.","doi":"10.1038/embor.2012.72","authors":"Vaur S, Feytout A, Vazquez S, Javerzat JP","authors_abbrev":"Vaur S et al.","pubmed_publication_date":"29 Jun 2012","pubmed_entrez_date":"2012-05-30","publication_year":"2012","canto_session_key":"cbb77a46f2c34af0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:Y11376","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16278451","title":"Activation of AP-1-dependent transcription by a truncated translation initiation factor.","citation":"Eukaryot Cell 2005 Nov;4(11):1840-50","abstract":"Int6/eIF3e is a highly conserved subunit of eukaryotic translation initiation factor 3 (eIF3) that has also been reported to interact with subunits of the proteasome and the COP9 signalosome. Overexpression of full-length Int6 or a 13-kDa C-terminal fragment, Int6CT, in the fission yeast Schizosaccharomyces pombe causes multidrug resistance that requires the otherwise inessential AP-1 transcription factor Pap1. Here we show for the first time that Int6CT acts to increase the transcriptional activity of Pap1. Microarray hybridization data indicate that Int6CT overexpression resulted in the up-regulation of 67 genes; this expression profile closely matched that of cells overexpressing Pap1. Analysis of the upstream regulatory sequences of these genes showed that the majority contained AP-1 consensus binding sites. Partial defects in ubiquitin-dependent proteolysis have been suggested to confer Pap1-dependent multidrug resistance, but no such defect was seen on Int6CT overexpression. Indeed, none of the previously identified interactions of endogenous Int6 was required for the activation of Pap1 transcription described here. Moreover, Int6CT-induced activation of Pap1-responsive gene expression was independent of the ability of Pap1 to undergo a redox-regulated conformational change which mediates its relocalization to the nucleus and expression of oxidative stress response genes. Int6CT therefore activates Pap1-dependent transcription by a novel mechanism.","authors":"Jenkins CC, Mata J, Crane RF, Thomas B, Akoulitchev A, Bähler J, Norbury CJ","authors_abbrev":"Jenkins CC et al.","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-11-10","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC18H10.03","SPBC17D11.05","SPBC21H7.03c","SPAC4A8.16c","SPBC646.09c","SPAC25G10.08","SPAC637.07","SPCC1739.13","SPAC1783.07c"],"gene_count":9,"ltp_gene_count":8},{"uniquename":"PMID:9487130","title":"Regulation of telomere length by checkpoint genes in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1998 Mar;9(3):611-21","abstract":"We have studied telomere length in Schizosaccharomyces pombe strains carrying mutations affecting cell cycle checkpoints, DNA repair, and regulation of the Cdc2 protein kinase. Telomere shortening was found in rad1, rad3, rad17, and rad26 mutants. Telomere lengths in previously characterized rad1 mutants paralleled the replication checkpoint proficiency of those mutants. In contrast, rad9, chk1, hus1, and cds1 mutants had intact telomeres. No difference in telomere length was seen in mutants affected in the regulation of Cdc2, whereas some of the DNA repair mutants examined had slightly longer telomeres than did the wild type. Overexpression of the rad1(+) gene caused telomeres to elongate slightly. The kinetics of telomere shortening was monitored by following telomere length after disruption of the rad1(+) gene; the rate was approximately 1 nucleotide per generation. Wild-type telomere length could be restored by reintroduction of the wild-type rad1(+) gene. Expression of the Saccharomyces cerevisiae RCK1 protein kinase gene, which suppresses the radiation and hydroxyurea sensitivity of Sz. pombe checkpoint mutants, was able to attenuate telomere shortening in rad1 mutant cells and to increase telomere length in a wild-type background. The functional effects of telomere shortening in rad1 mutants were assayed by measuring loss of a linear and a circular minichromosome. A minor increase in loss rate was seen with the linear minichromosome, and an even smaller difference compared with wild-type was detected with the circular plasmid.","authors":"Dahlen M, Olsson T, Kanter-Smoler G, Ramne A, Sunnerhagen P","authors_abbrev":"Dahlen M et al.","pubmed_publication_date":"Mar 1998","pubmed_entrez_date":"1998-04-04","publication_year":"1998","canto_session_key":"c106524e4c73575e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-02-15 16:53:05","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-26 10:37:41","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.04c","SPBC3E7.08c","SPCC1259.13","SPAC1D4.12","SPAC14C4.13","SPCC18B5.03","SPCC18B5.11c","SPCC338.17c","SPAC664.07c","SPAC13G6.01c","SPAC9E9.08","SPBC216.05","SPBC11B10.09","SPAC1952.07"],"gene_count":14,"ltp_gene_count":12,"approved_date":"2014-08-26"},{"uniquename":"PMID:9197411","title":"Tolerance of low pH in Schizosaccharomyces pombe requires a functioning pub1 ubiquitin ligase.","citation":"Mol Gen Genet 1997 May 20;254(5):520-8","abstract":"A strain of Schizosaccharomyces pombe carrying a disrupted Na+/H+ antiporter gene (sod2::sup3-5), in addition to the common auxotrophic mutations, ade6-216, ura4-D18 and leu1-32, is highly sensitive to media adjusted to pH 6.9. Reversion analysis of this strain yielded a group of revertants capable of growth at pH 6.9. Two of the revertants elongated and failed to form colonies at pH 3.5. Genetic characterization of one of the pH-sensitive elongated strains, J227, showed the presence of two independently segregating mutations. One, pub1 (protein ubiquitin ligase 1), has recently been reported as an E3 protein ubiquitin ligase involved in cdc25 turnover. The second has been named elp3-1 (elongated at low pH). Genetic dissection of the original strain revealed that poor growth at high pH was due to the presence of the auxotrophic markers, suggesting a possible inhibitory effect of high pH on the function of permeases responsible for uptake of the necessary nutrients. Suppression of the high pH sensitivity required the presence of both the pub1-1 and elp3-1 mutations. While the pub1-1 mutation reduced the capacity of cells to tolerate relatively moderate concentrations of LiCl (3 mM) in liquid culture, it was capable of partially suppressing the extreme Li+ sensitivity caused by the sod2 disruption. Under these conditions, the growth of pub1-1 sod2::ura4 double mutant cells was improved over that of either pub1-1 or sod2::ura4 cells. The elp3-1 mutation had no effect on the Li+ tolerance in either wild-type or sod2::ura4 backgrounds. pub1-1 cells are elongated and incapable of colony formation at pH 3.5. In contrast, elp3-1 cells are elongated at pH 3.5 and pH 5.5 (the normal pH of minimal medium) but can form colonies under both conditions. J227 cells are significantly longer than either single mutant at pH 3.5 and do not form colonies but are visually similar to elp3-1 cells at pH 5.5. Complementation cloning in the J227 background yielded a genomic clone of pub1, allowing us to define the intron-exon structure of the gene. Sequences with high homology to the predicted amino acid sequence of pub1 have been identified in Saccharomyces cerevisiae (RSP5/NPI1), human (hRPF1), mouse (mNedd4), and rat (rNedd4). Based on the nature of our mutant selection, the pH-sensitive phenotype of the strains selected, and the known involvement of RSP5/ NPI1 in membrane permease turnover in S. cerevisiae, we hypothesize a role for pub1, either directly or indirectly, in regulating membrane transport processes. This is further supported by the broad range of effects that the pub1-1 mutation exerts on overall performance of cells at high and low external pH, and in the presence of toxic levels of Li+.","authors":"Saleki R, Jia Z, Karagiannis J, Young PG","authors_abbrev":"Saleki R et al.","pubmed_publication_date":"20 May 1997","pubmed_entrez_date":"1997-05-20","publication_year":"1997","canto_session_key":"f1d8eeb553561925","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-05 20:58:30","canto_approved_date":"2023-09-08 08:54:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-09-08 08:54:48","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11G7.02","SPAC29A4.20","SPAC977.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-10-05"},{"uniquename":"PMID:8914526","title":"Cloning of the cDNA and genomic clones for glutathione synthetase from Arabidopsis thaliana and complementation of a gsh2 mutant in fission yeast.","citation":"Plant Mol Biol 1996 Sep;31(6):1093-104","abstract":"Glutathione is essential for protecting plants from a range of environmental stresses, including heavy metals where it acts as a precursor for the synthesis of phytochelatins. A 1658 bp cDNA clone for glutathione synthetase (gsh2) was isolated from Arabidopsis thaliana plants that were actively synthesizing glutathione upon exposure to cadmium. The sequence of the clone revealed a protein with an estimated molecular mass of 53858 Da that was very similar to the protein from higher eukaryotes, was less similar to the gene from the fission yeast, Schizosaccharomyces pombe, and shared only a small region of similarity with the Escherichia coli protein. A 4.3 kb SstI fragment containing the genomic clone for glutathione synthetase was also isolated and sequenced. A comparison of the cDNA and genomic sequences revealed that the gene was composed of twelve exons. When the Arabidopsis cDNA cloned in a special shuttle vector was expressed in a S. pombe mutant deficient in glutathione synthetase activity, the plant cDNA was able to complement the yeast mutation. Glutathione synthetase activity was measurable in wild-type yeast cells, below detectable levels in the gsh2- mutant, and restored to substantial levels by the expression of the Arabidopsis cDNA. The S. pombe mutant expressing the plant cDNA had near wild type levels of total cellular thiols, 109Cd2+ binding activity, and cadmium resistance. Since the Arabidopsis cDNA was under control of a thiamine-repressible promoter, growth of the transformed yeast on thiamine-free medium increased expression of the cDNA resulting in increases in cadmium resistance.","authors":"Wang CL, Oliver DJ","authors_abbrev":"Wang CL et al.","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_session_key":"342b99a76cb8f1c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-21 13:16:39","canto_approved_date":"2022-02-25 05:38:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-02 15:51:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-21"},{"uniquename":"PMID:17510629","title":"A genome-wide role for CHD remodelling factors and Nap1 in nucleosome disassembly.","citation":"EMBO J 2007 Jun 20;26(12):2868-79","abstract":"Chromatin remodelling factors and histone chaperones were previously shown to cooperatively affect nucleosome assembly and disassembly processes in vitro. Here, we show that Schizosaccharomyces pombe CHD remodellers, the Hrp1 and Hrp3 paralogs physically interact with the histone chaperone Nap1. Genome-wide analysis of Hrp1, Hrp3 and Nap1 occupancy, combined with nucleosome density measurements revealed that the CHD factors and Nap1 colocalized in particular to promoter regions where they remove nucleosomes near the transcriptional start site. Hrp1 and Hrp3 also regulate nucleosome density in coding regions, where they have redundant roles to stimulate transcription. Previously, DNA replication-dependent and -independent nucleosome disassembly processes have been described. We found that nucleosome density increased in the hrp1 mutant in the absence of DNA replication. Finally, regions where nucleosome density increased in hrp1, hrp3 and nap1 mutants also showed nucleosome density and histone modification changes in HDAC and HAT mutants. Thus, this study revealed an important in vivo role for CHD remodellers and Nap1 in nucleosome disassembly at promoters and coding regions, which are linked to changes in histone acetylation.","authors":"Walfridsson J, Khorosjutina O, Matikainen P, Gustafsson CM, Ekwall K","authors_abbrev":"Walfridsson J et al.","pubmed_publication_date":"20 Jun 2007","pubmed_entrez_date":"2007-05-19","publication_year":"2007","canto_session_key":"ab232c941560cd80","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-05 23:15:24","canto_approved_date":"2025-12-14 14:47:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-05 23:14:28","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.08","SPAC4A8.16c","SPAC13G7.02c","SPCC1739.13","SPAC3G6.01","SPCC364.06","SPCC330.09","SPAC1783.05"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2023-07-05"},{"uniquename":"PMID:27664110","title":"Loss of Msp1p in Schizosaccharomyces pombe induces a ROS-dependent nuclear mutator phenotype that affects mitochondrial fission genes.","citation":"FEBS Lett 2016 Oct;590(20):3544-3558","abstract":"Mitochondria continually fuse and divide to dynamically adapt to changes in metabolism and stress. Mitochondrial dynamics are also required for mitochondrial DNA (mtDNA) integrity; however, the underlying reason is not known. In this study, we examined the link between mitochondrial fusion and mtDNA maintenance in Schizosaccharomyces pombe, which cannot survive without mtDNA, by screening for suppressors of the lethality induced by loss of the dynamin-related large GTPase Msp1p. Our findings reveal that inactivation of Msp1p induces a ROS-dependent nuclear mutator phenotype that affects mitochondrial fission genes involved in suppressing mitochondrial fragmentation and mtDNA depletion. This indicates that mitochondrial fusion is crucial for maintaining the integrity of both mitochondrial and nuclear genetic information. Furthermore, our study suggests that the primary roles of Msp1p are to organize mitochondrial membranes, thus making them competent for fusion, and maintain the integrity of mtDNA.","doi":"10.1002/1873-3468.12432","authors":"Delerue T, Khosrobakhsh F, Daloyau M, Emorine LJ, Dedieu A, Herbert CJ, Bonnefoy N, Arnauné-Pelloquin L, Belenguer P","authors_abbrev":"Delerue T et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-09-25","publication_year":"2016","canto_session_key":"e8e4518f9c7db116","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-10-16 16:28:49","canto_approved_date":"2019-10-18 13:13:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-10-16 16:28:42","canto_added_date":"2016-09-26 00:15:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.06","SPAC9G1.04","SPCC191.07","SPAC14C4.14","SPBC12C2.08","SPAC664.15","SPBC11G11.01","SPAC222.12c","SPAC8C9.06c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2019-10-16"},{"uniquename":"PMID:25398909","title":"Fission yeast Cactin restricts telomere transcription and elongation by controlling Rap1 levels.","citation":"EMBO J 2015 Jan 02;34(1):115-29","abstract":"The telomeric transcriptome comprises multiple long non-coding RNAs generated by transcription of linear chromosome ends. In a screening performed in Schizosaccharomyces pombe, we identified factors modulating the cellular levels of the telomeric transcriptome. Among these factors, Cay1 is the fission yeast member of the conserved family of Cactins, uncharacterized proteins crucial for cell growth and survival. In cay1∆ mutants, the cellular levels of the telomeric factor Rap1 are drastically diminished due to defects in rap1+ pre-mRNA splicing and Rap1 protein stability. cay1∆ cells accumulate histone H3 acetylated at lysine 9 at telomeres, which become transcriptionally desilenced, are over-elongated by telomerase and cause chromosomal aberrations in the cold. Overexpressing Rap1 in cay1+ deleted cells significantly reverts all telomeric defects. Additionally, cay1∆ mutants accumulate unprocessed Tf2 retrotransposon RNA through Rap1-independent mechanisms. Thus, Cay1 plays crucial roles in cells by ultimately harmonizing expression of transcripts originating from seemingly unrelated genomic loci.","doi":"10.15252/embj.201489559","authors":"Lorenzi LE, Bah A, Wischnewski H, Shchepachev V, Soneson C, Santagostino M, Azzalin CM","authors_abbrev":"Lorenzi LE et al.","pubmed_publication_date":"02 Jan 2015","pubmed_entrez_date":"2014-11-16","publication_year":"2015","canto_session_key":"3ccd13cb05a3f35a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-08-12 18:31:47","canto_approved_date":"2020-03-17 13:47:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-22 08:53:00","canto_added_date":"2014-11-17 01:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":59,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.13c","SPBC2D10.13","SPAC10F6.06","SPAC6F6.17","SPAC29E6.08","SPCC338.16","SPBP8B7.08c","SPAC23C11.10","SPBC2F12.12c","SPAC16A10.07c","SPBC1778.02","SPBC29A3.14c","SPAC26H5.06","SPBC2A9.02"],"gene_count":14,"ltp_gene_count":11,"approved_date":"2015-08-12"},{"uniquename":"PMID:30079490","title":"Mutations in WDR4 as a new cause of Galloway-Mowat syndrome.","citation":"Am J Med Genet A 2018 Nov;176(11):2460-2465","abstract":"Galloway-Mowat syndrome (GAMOS) is a phenotypically heterogeneous disorder characterized by neurodevelopmental defects combined with renal-glomerular disease, manifesting with proteinuria. To identify additional monogenic disease causes, we here performed whole exome sequencing (WES), linkage analysis, and homozygosity mapping in three affected siblings of an Indian family with GAMOS. Applying established criteria for variant filtering, we identify a novel homozygous splice site mutation in the gene WDR4 as the likely disease-causing mutation in this family. In line with previous reports, we observe growth deficiency, microcephaly, developmental delay, and intellectual disability as phenotypic features resulting from WDR4 mutations. However, the newly identified allele additionally gives rise to proteinuria and nephrotic syndrome, a phenotype that was never reported in patients with WDR4 mutations. Our data thus expand the phenotypic spectrum of WDR4 mutations by demonstrating that, depending on the specific mutated allele, a renal phenotype may be present. This finding suggests that GAMOS may occupy a phenotypic spectrum with other microcephalic diseases. Furthermore, WDR4 is an additional example of a gene that encodes a tRNA modifying enzyme and gives rise to GAMOS, if mutated. Our findings thereby support the recent observation that, like neurons, podocytes of the renal glomerulus are particularly vulnerable to cellular defects resulting from altered tRNA modifications.","doi":"10.1002/ajmg.a.40489","authors":"Braun DA, Shril S, Sinha A, Schneider R, Tan W, Ashraf S, Hermle T, Jobst-Schwan T, Widmeier E, Majmundar AJ, Daga A, Warejko JK, Nakayama M, Schapiro D, Chen J, Airik M, Rao J, Schmidt JM, Hoogstraten CA, Hugo H, Meena J, Lek M, Laricchia KM, Bagga A, Hildebrandt F","authors_abbrev":"Braun DA et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-08-07","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17385316","title":"[Cell phenotypes of a mutant in the gene encoding a Rad51 paralog in fission yeast].","citation":"Genetika 2007 Feb;43(2):183-8","abstract":"The discovery of three Rad51 paralogs in Saccharomyces cerevisiae (Rad55, Rad57, and Dmc1), four in Schizosaccharomyces pombe (Rhp55, Rhp57, Rlp 1, and Dmc 1), and six in human (Rad51 B, Rad51 C, Rad51 D, Xrcc2, Xrcc3, and Dmcl) indicate the functional diversity and specialization of RecA-like proteins in the line from the lower to higher organisms. This paper reports characterization of a number of mitotic and meiotic phenotypes of the cells mutant in rlpl gene, encoding a paralog of Rad5 1, in fission yeasts. No evident role of Rlp I protein in the repair of spontaneous lesions emerging during mating type switching was found. Rlpl does not interact physically with Dmcl. An elevated expression of rhp51 has a dominant negative effect on the cell survivability of rlpl mutant exposed to a DNA-damaging agent. We assume that Rlp 1 acts at the stages of recombination connected with disassembling of the nucleoprotein filament formed by Rhp51 protein.","authors":"Sultanova AN, Salakhova AF, Bashkirov VI, Khasanov FK","authors_abbrev":"Sultanova AN et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-03-28","publication_year":"2007","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18065650","title":"Fission yeast mitogen-activated protein kinase Sty1 interacts with translation factors.","citation":"Eukaryot Cell 2008 Feb;7(2):328-38","abstract":"Signaling by stress-activated mitogen-activated protein kinase (MAPK) pathways influences translation efficiency in mammalian cells and budding yeast. We have investigated the stress-activated MAPK from fission yeast, Sty1, and its downstream protein kinase, Mkp1/Srk1, for physically associated proteins using tandem affinity purification tagging. We find Sty1, but not Mkp1, to bind to the translation elongation factor eukaryotic elongation factor 2 (eEF2) and the translation initiation factor eukaryotic initiation factor 3a (eIF3a). The Sty1-eIF3a interaction is weakened under oxidative or hyperosmotic stress, whereas the Sty1-eEF2 interaction is stable. Nitrogen deprivation causes a transient strengthening of both the Sty1-eEF2 and the Sty1-Mkp1 interactions, overlapping with the time of maximal Sty1 activation. Analysis of polysome profiles from cells under oxidative stress, or after hyperosmotic shock or nitrogen deprivation, shows that translation in sty1 mutant cells recovers considerably less efficiently than that in the wild type. Cells lacking the Sty1-regulated transcription factor Atf1 are deficient in maintaining and recovering translational activity after hyperosmotic shock but not during oxidative stress or nitrogen starvation. In cells lacking Sty1, eIF3a levels are decreased, and phosphorylation of eIF3a is reduced. Taken together, our data point to a central role in translational adaptation for the stress-activated MAPK pathway in fission yeast similar to that in other investigated eukaryotes, with the exception that fission yeast MAPK-activated protein kinases seem not to be directly involved in this process.","authors":"Asp E, Nilsson D, Sunnerhagen P","authors_abbrev":"Asp E et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2007-12-11","publication_year":"2008","canto_session_key":"dba9909d81dd3740","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-11 16:21:50","canto_approved_date":"2020-03-14 15:12:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-11 16:21:39","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.08","SPAC513.01c","SPCP31B10.07","SPAC23A1.06c","SPBC29B5.01","SPBC17D11.05","SPCC417.08","SPAC24B11.06c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-10-11"},{"uniquename":"PMID:8423854","title":"DNA polymerase-alpha is essential for mating-type switching in fission yeast.","citation":"Nature 1993 Jan 21;361(6409):271-3","abstract":"In the fission yeast Schizosaccharomyces pombe, the double-stranded chromosomal break (DSB) at the mating-type locus (mat1) initiates recombination during mating-type switching. A constant DSB level is maintained throughout the cell-cycle. In the strand-segregation model for mating-type switching, it was postulated that if the DSB is generated during or soon after mat1 replication, one of the chromatids could be repaired and switched during replication in the next cell cycle, while the other chromatid inherits the break. Here we report a molecular characterization of swi7, one of the genes required for DSB formation. Surprisingly, a gene complementing the swi7 mutation maps to chromosome I and encodes S. pombe DNA polymerase-alpha. Disruption of this gene is lethal in both switching and non-switching strains, as expected. S. pombe DNA polymerase-alpha must therefore play a role in generating the DSB at mat1, suggesting that DSB formation is coupled with DNA replication.","authors":"Singh J, Klar AJ","authors_abbrev":"Singh J et al.","pubmed_publication_date":"21 Jan 1993","pubmed_entrez_date":"1993-01-21","publication_year":"1993","canto_session_key":"db135fedf50b8655","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-02 15:55:05","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-02 15:49:50","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-02"},{"uniquename":"PMID:9821290","title":"Stability and refractoriness of the high catalase activity in the oxidative-stress-resistant fission yeast Schizosaccharomyces pombe.","citation":"Folia Microbiol (Praha) 1998;43(4):369-72","abstract":"Effect of oxygen and metabolic substrates (glucose, ethanol) on the catalase activity of anaerobically grown Schizosaccharomyces pombe cells was assessed and compared with that of Saccharomyces cerevisiae in order to determine the catalase activity regulation in S. pombe. In contrast to S. cerevisiae, the total catalase activity of permeabilized S. pombe anaerobically grown cells is higher than that found in aerobically grown cells, is stable and constant under all circumstances (i.e. it is not induced by oxygen and/or substrates), and only a negligible part (3-5%) of it is contributed by de novo protein synthesis during aeration with or without substrates. The patent catalase activity of intact cells rises 2-fold during 6-h aeration without substrate and 7-8-fold in the presence of glucose or ethanol. The increase is not inhibited by cycloheximide and is thus not due to de novo catalase synthesis, but may reflect enhanced transport of catalase to the cell surface or a permeabilization of the plasma membrane during the aeration.","authors":"Sigler K, Gille G","authors_abbrev":"Sigler K et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-11-20","publication_year":"1998","canto_session_key":"a308a6e18ded196c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-11-24 12:50:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-24 12:50:38","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC757.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-11-24"},{"uniquename":"EMBL:AB084846","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.34"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15713014","title":"Potential application of a glucose-transport-deficient mutant of Schizosaccharomyces pombe for removing gluconic acid from grape must.","citation":"J Agric Food Chem 2005 Feb 23;53(4):1017-21","abstract":"Musts from rotten grapes typically contain high levels of gluconic acid, which can raise severe problems in winemaking processes. In this work, the ability of the glucose-transport-deficient mutant YGS-5 of Schizosaccharomyces pombe to completely or partly remove gluconic acid from a synthetic glucose-containing medium and the potential use of this yeast strain for the same purpose in musts and wines were examined. Surprisingly, the S. pombe YGS-5 strain successfully removed 93% of the initial gluconic acid (2.5 gL(-1)) and 80% of the initial malic acid (1.0 gL(-1)) within 30 h after inoculation. Also, the yeast strain produced no volatile compounds other than those obtained in fermentations conducted with the wine yeast Saccharomyces cerevisiae. S. pombe YGS-5 could thus be used to remove gluconic acid present in musts from rotten grapes. On the basis of these results, various ways of using S. pombe YGS-5 to treat musts containing gluconic acid in order to solve the problems due to the high gluconic acid concentrations in botrytized grape must are proposed.","authors":"Peinado RA, Moreno JJ, Medina M, Mauricio JC","authors_abbrev":"Peinado RA et al.","pubmed_publication_date":"23 Feb 2005","pubmed_entrez_date":"2005-02-17","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19799186","title":"Using Schizosaccharomyces pombe meiosis to analyze DNA recombination intermediates.","citation":"Methods Mol Biol 2009;557:235-52","abstract":"The fission yeast Schizosaccharomyces pombe has many biological characteristics that make it an ideal model organism for the study of meiosis. A nearly synchronous meiosis is one of the most important. Under certain environmental and genetic conditions, large cultures of S. pombe can be induced to undergo meiosis in a timely and predictable manner that allows for changes in the DNA to be observed and analyzed by gel electrophoresis. Initiation of meiotic recombination via programmed DNA double-strand breaks, the formation of joint molecule recombination intermediates, and the resolution of these intermediates into crossover DNA products can all be seen with consistent timing during the progression of a synchronous meiotic induction. The timing of recombination events, the genetic requirements for the formation and disappearance of recombination intermediates, and the analysis of the DNA structures of those intermediates allow a comparison of meiotic recombination in fission yeast with that in the only other species similarly studied, the budding yeast Saccharomyces cerevisiae.","doi":"10.1007/978-1-59745-527-5_15","authors":"Hyppa RW, Smith GR","authors_abbrev":"Hyppa RW et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-10-06","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34678589","title":"Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1.","citation":"DNA Repair (Amst) 2021 Dec;108:103232","abstract":"The cellular response to DNA damage (DDR) that causes replication collapse and/or DNA double strand breaks, is characterised by a massive change in the post-translational modifications (PTM) of hundreds of proteins involved in the detection and repair of DNA damage, and the communication of the state of damage to the cellular systems that regulate replication and cell division. A substantial proportion of these PTMs involve targeted phosphorylation, which among other effects, promotes the formation of multiprotein complexes through the specific binding of phosphorylated motifs on one protein, by specialised domains on other proteins. Understanding the nature of these phosphorylation mediated interactions allows definition of the pathways and networks that coordinate the DDR, and helps identify new targets for therapeutic intervention that may be of benefit in the treatment of cancer, where DDR plays a key role. In this review we summarise the present understanding of how phosphorylated motifs are recognised by BRCT domains, which occur in many DDR proteins. We particularly focus on TOPBP1 - a multi-BRCT domain scaffold protein with essential roles in replication and the repair and signalling of DNA damage.","doi":"10.1016/j.dnarep.2021.103232","authors":"Day M, Oliver AW, Pearl LH","authors_abbrev":"Day M et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-10-22","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.06c","SPACUNK4.14"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"7p0l","gene_chains":[{"gene_uniquename":"SPACUNK4.14","chain":"A/B","position":"384-581"},{"gene_uniquename":"SPAC19G12.06c","chain":"C/D","position":"125-131"}],"title":"Crystal structure of S.pombe Mdb1 BRCT domains in complex with a H2A phosphopeptide","entry_authors":"Day M,Oliver AW,Pearl LH","entry_authors_abbrev":"Day M et al.","reference_uniquename":"PMID:34678589","experimental_method":"X-ray","resolution":"1.97"},{"pdb_id":"7p0j","gene_chains":[{"gene_uniquename":"SPACUNK4.14","chain":"A","position":"384-581"}],"title":"Crystal structure of S.pombe Mdb1 BRCT domains","entry_authors":"Day M,Oliver AW,Pearl LH","entry_authors_abbrev":"Day M et al.","reference_uniquename":"PMID:34678589","experimental_method":"X-ray","resolution":"1.48"}]},{"uniquename":"PMID:1741305","title":"High efficiency transformation of Schizosaccharomyces pombe by electroporation.","citation":"Nucleic Acids Res 1992 Feb 11;20(3):621","abstract":"","authors":"Prentice HL","authors_abbrev":"Prentice HL","pubmed_publication_date":"11 Feb 1992","pubmed_entrez_date":"1992-02-11","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16068179","title":"Epistatic gene interactions in the control of division in fission yeast.","citation":"Nature 1979 May 31;279(5712):428-30","abstract":"THERE is currently much interest in the mechanism which controls the timing of cell division. Certain features of the control have been found to be common to a variety of eukaryotes. In particular, the importance of cell size as a parameter affecting cell cycle progress has been reported for mammalian cells(1,2) and for several single-celled eukaryotes(3-6). Another feature common to several systems is that growth conditions have a direct effect on the timing of division cycle events(7-9), and on cell size(9,10). In the fission yeast Schizosaccharomyces pombe, both cell size(6) and nutritional conditions(9) have been shown to affect cycle kinetics. The organism has been used extensively as a model eukaryotic system, largely because of the ease of measuring cell size and because division occurs by binary fission(11). More recently, its genetic tractability has led to the isolation of cell division cycle (cdc) mutants(12), and also of wee mutants altered in the control coordinating growth with the division cycle(13-15). The existence of such control mutants allows a more direct approach to the investigation of the molecular basis of division control, in contrast to the indirect methods used in other systems(4,16-18). wee mutants are so far unique to S. pombe. The most conspicuous property of wee mutants is their reduced cell size(13,14). Analysis of these mutants(15,19) and other evidence(9) has shown that control over cell division timing normally acts at entry to mitosis. As the function of a number of cdc genes is specifically required for mitosis(12), interactions between wee and cdc mutants which affect mitosis might be expected. I report here that the mitotic defect caused by a defective cdc25 allele is suppressed in wee mutants. Suppression by wee1 mutants is almost complete, while the wee2.1 mutation is a less effective suppressor. The significance of these findings for genetic models of the control of mitosis is considered.","authors":"Fantes P","authors_abbrev":"Fantes P","pubmed_publication_date":"31 May 1979","pubmed_entrez_date":"1979-05-31","publication_year":"1979","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10477296","title":"The Drosophila chiffon gene is required for chorion gene amplification, and is related to the yeast Dbf4 regulator of DNA replication and cell cycle.","citation":"Development 1999 Oct;126(19):4281-93","abstract":"The Drosophila chorion genes encode the major protein components of the chorion (eggshell) and are arranged in two clusters in the genome. To meet the demand for rapid chorion synthesis, Drosophila ovary follicle cells amplify the chorion gene clusters approximately 80-fold. Amplification proceeds through repeated firing of one or more DNA replication origins located near the center of each gene cluster. Hypomorphic mutant alleles of the chiffon gene cause thin, fragile chorions and female sterility, and were found to eliminate chorion gene amplification. Null alleles of chiffon had the additional phenotypes of rough eyes and thin thoracic bristles: phenotypes often associated with disruption of normal cell cycle. The chiffon locus was cloned by chromosomal walking from the nearby cactus locus. A 6.5 kb transcript was identified and confirmed to be chiffon by sequencing of mutant alleles and by phenotypic rescue with genomic transformation constructs. The protein predicted by translation of the 5.1 kb chiffon ORF contains two domains related to the S. cerevisiae Dbf4 regulator of DNA replication origin firing and cell cycle progression: a 44 residue domain designated CDDN1 (43% identical) and a 41 residue domain designated CDDN2 (12% identical). The CDDN domains were also found in the S. pombe homolog of Dbf4, Dfp1, as well as in the proteins predicted by translation of the Aspergillus nimO gene and specific human and mouse clones. The data suggest a family of eukaryotic proteins related to Dbf4 and involved in initiation of DNA replication.","authors":"Landis G, Tower J","authors_abbrev":"Landis G et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-09-08","publication_year":"1999","canto_session_key":"6ee34e1c86e378ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2012-03-22 19:52:27","canto_approved_date":"2025-11-21 15:42:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-03-03 17:59:00","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC550.13"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-22"},{"uniquename":"EMBL:AU012311","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.102"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:31877650","title":"Special Issue: Non-Conventional Yeasts: Genomics and Biotechnology.","citation":"Microorganisms 2019 Dec 20;8(1)","abstract":"Non-conventional yeasts, i.e., the vast biodiversity beyond already well-established model systems such as  Saccharomyces cerevisiae ,  Candida albicans  and  Schizosaccharomyces pombe  and a few others, are a huge and untapped resource of organisms. [...].","doi":"10.3390/microorganisms8010021","authors":"Wendland J","authors_abbrev":"Wendland J","pubmed_publication_date":"20 Dec 2019","pubmed_entrez_date":"2019-12-28","publication_year":"2019","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42137058","title":"Structural and mechanistic perspectives on Nse5/6 regulation of the Smc5/6 complex.","citation":"Front Mol Biosci 2026;13:1757821","abstract":"The Smc5/6 complex is a vital protector of eukaryotic genome stability, coordinating DNA repair, replication fork maintenance, recombination intermediate processing, and chromosome organization. Within this complex, the Nse5/6 heterodimer has recently emerged as a key factor influencing Smc5/6 dynamics, acting at the interface of structural control, enzymatic regulation, and chromatin recruitment. Structural studies from yeast to mammals show that Nse5/6 associate with the Smc5/6 head-neck region, restricting ATPase head engagement and stabilizing an inactive, chromatin-loading-ready state. Upon ATP binding and DNA interaction, conformational changes displace or reposition Nse5/6, facilitating Nse4-mediated head closure, DNA entrapment, and loop-modulating activity. Functional analyses across  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe , mammals, and plants indicate that Nse5/6 is essential for recruiting Smc5/6 to damaged or stalled replication forks, stabilizing chromatin association, and coordinating SUMO-dependent repair pathways. Loss of Nse5/6 leads to defects in replication stress tolerance, accumulation of recombination intermediates, impaired chromatin loading, and widespread genome instability. This review synthesizes emerging structural and functional insights into Nse5/6, emphasizing its conserved yet species-adapted mechanisms that regulate ATPase gating, DNA substrate selection, and chromatin recruitment. Collectively, these findings redefine Nse5/6 not as a peripheral structural factor but as a dynamic regulatory hub that orchestrates Smc5/6 activity in genome maintenance, development, and antiviral defense.","doi":"10.3389/fmolb.2026.1757821","authors":"Kim JH, Rao DR, Kim KD","authors_abbrev":"Kim JH et al.","pubmed_publication_date":"2026","pubmed_entrez_date":"2026-05-15","publication_year":"2026","canto_session_key":"a7de78848141a15e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-05-15 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36695178","title":"Diacylglycerol at the inner nuclear membrane fuels nuclear envelope expansion in closed mitosis.","citation":"J Cell Sci 2023 Feb 01;136(3)","abstract":"Nuclear envelope (NE) expansion must be controlled to maintain nuclear shape and function. The nuclear membrane expands massively during closed mitosis, enabling chromosome segregation within an intact NE. Phosphatidic acid (PA) and diacylglycerol (DG) can both serve as biosynthetic precursors for membrane lipid synthesis. How they are regulated in time and space and what the implications are of changes in their flux for mitotic fidelity are largely unknown. Using genetically encoded PA and DG probes, we show that DG is depleted from the inner nuclear membrane during mitosis in the fission yeast Schizosaccharomyces pombe, but PA does not accumulate, indicating that it is rerouted to membrane synthesis. We demonstrate that DG-to-PA conversion catalyzed by the diacylglycerol kinase Dgk1 (also known as Ptp4) and direct glycerophospholipid synthesis from DG by diacylglycerol cholinephosphotransferase/ethanolaminephosphotransferase Ept1 reinforce NE expansion. We conclude that DG consumption through both the de novo pathway and the Kennedy pathway fuels a spike in glycerophospholipid biosynthesis, controlling NE expansion and, ultimately, mitotic fidelity.","doi":"10.1242/jcs.260568","authors":"Foo S, Cazenave-Gassiot A, Wenk MR, Oliferenko S","authors_abbrev":"Foo S et al.","pubmed_publication_date":"01 Feb 2023","pubmed_entrez_date":"2023-01-25","publication_year":"2023","canto_session_key":"12398ff6230de6a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Snezhana Oliferenko","canto_first_approved_date":"2023-03-05 17:43:10","canto_approved_date":"2023-03-08 15:19:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-02 17:04:40","canto_added_date":"2023-01-26 01:15:04","annotation_curators":[{"name":"Snezhana Oliferenko","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.05","SPAC22A12.10","SPBC902.03","SPBC3B8.10c","SPAC1952.13"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2023-03-05"},{"uniquename":"PMID:11112691","title":"Two type V myosins with non-overlapping functions in the fission yeast Schizosaccharomyces pombe: Myo52 is concerned with growth polarity and cytokinesis, Myo51 is a component of the cytokinetic actin ring.","citation":"J Cell Sci 2001 Jan;114(Pt 1):69-79","abstract":"The fission yeast genome project has identified five myosin genes: one type I myosin, myo1(+), two type II myosins, myo2(+) and myp2(+), and two type V myosins, myo51(+) and myo52(+). Cells deleted for myo51(+) show normal morphology and growth rates whereas deletion of myo52(+) results in a partial loss of cell polarity, slow growth and cytokinetic defects. Combining both deletions in a single strain is phenotypically non-additive, myo52(delta) being epistatic to myo51(delta). Overproduction of Myo51 gives rise to elongated cells which fail to form functional septa whereas overproduction of Myo52 results in branched cells with aberrant septa that fail to cleave. Myo52 localises to the poles of growing cells but during cell division it relocalises to the cell equator as a bar that is bisected by the cytokinetic septum. Myo51 shows no obvious localisation during interphase but at cytokinesis it is associated with the contractile cytokinetic actin ring (CAR). Both myosins are dependent upon an intact actin cytoskeleton for localisation. Myo52 partially colocalises with the (alpha)-glucan synthase Mok1 at the cell tips and to a lesser extent at the septum. Mok1 is delocalised and upregulated in myo52(delta) and myo52(delta) cell walls are resistant to digestion by the cell wall degrading enzyme zymolyase. Thus myo52(+) appears to be involved in the local delivery or positioning of vesicles containing cell wall precursors at the cell tips and has a role in the maturation or cleavage of the septum. Myo51 has a non-essential role in cytokinesis as a component of the cytokinetic actin ring.","authors":"Win TZ, Gachet Y, Mulvihill DP, May KM, Hyams JS","authors_abbrev":"Win TZ et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2000-12-12","publication_year":"2001","canto_session_key":"43ecf1cd34feb2eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-11 13:20:08","canto_approved_date":"2025-09-03 13:32:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-11 13:20:01","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPBC32H8.12c","SPAC4A8.05c","SPBC146.13c","SPBC2D10.14c","SPCC1919.10c","SPCC1281.01"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2024-06-11"},{"uniquename":"PMID:20211136","title":"Stc1: a critical link between RNAi and chromatin modification required for heterochromatin integrity.","citation":"Cell 2010 Mar 05;140(5):666-77","abstract":"In fission yeast, RNAi directs heterochromatin formation at centromeres, telomeres, and the mating type locus. Noncoding RNAs transcribed from repeat elements generate siRNAs that are incorporated into the Argonaute-containing RITS complex and direct it to nascent homologous transcripts. This leads to recruitment of the CLRC complex, including the histone methyltransferase Clr4, promoting H3K9 methylation and heterochromatin formation. A key question is what mediates the recruitment of Clr4/CLRC to transcript-bound RITS. We have identified a LIM domain protein, Stc1, that is required for centromeric heterochromatin integrity. Our analyses show that Stc1 is specifically required to establish H3K9 methylation via RNAi, and interacts both with the RNAi effector Ago1, and with the chromatin-modifying CLRC complex. Moreover, tethering Stc1 to a euchromatic locus is sufficient to induce silencing and heterochromatin formation independently of RNAi. We conclude that Stc1 associates with RITS on centromeric transcripts and recruits CLRC, thereby coupling RNAi to chromatin modification.","doi":"10.1016/j.cell.2010.01.038","authors":"Bayne EH, White SA, Kagansky A, Bijos DA, Sanchez-Pulido L, Hoe KL, Kim DU, Park HO, Ponting CP, Rappsilber J, Allshire RC","authors_abbrev":"Bayne EH et al.","pubmed_publication_date":"05 Mar 2010","pubmed_entrez_date":"2010-03-10","publication_year":"2010","canto_session_key":"7cd37f3825c76d6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-11-04 15:25:48","canto_approved_date":"2024-04-01 15:41:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-03 16:10:49","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.07c","SPBC800.03","SPAC23G3.06","SPAC17H9.05","SPAC664.01c","SPBC1734.11","SPCC188.13c","SPAC1F12.07","SPCC736.11","SPBC83.03c","SPBP8B7.28c","SPAC6F12.09","SPAC18G6.02c","SPBC428.08c","SPAC3A11.08","SPBC12D12.08c","SPCC970.07c","SPCC613.12c","SPBC646.10c","SPCC11E10.08"],"gene_count":20,"ltp_gene_count":12,"approved_date":"2015-11-04"},{"uniquename":"PMID:31811632","title":"The Nuclear RNA Exosome and Its Cofactors.","citation":"Adv Exp Med Biol 2019;1203:113-132","abstract":"The RNA exosome is a highly conserved ribonuclease endowed with 3'-5' exonuclease and endonuclease activities. The multisubunit complex resides in both the nucleus and the cytoplasm, with varying compositions and activities between the two compartments. While the cytoplasmic exosome functions mostly in mRNA quality control pathways, the nuclear RNA exosome partakes in the 3'-end processing and complete decay of a wide variety of substrates, including virtually all types of noncoding (nc) RNAs. To handle these diverse tasks, the nuclear exosome engages with dedicated cofactors, some of which serve as activators by stimulating decay through oligoA addition and/or RNA helicase activities or, as adaptors, by recruiting RNA substrates through their RNA-binding capacities. Most nuclear exosome cofactors contain the essential RNA helicase Mtr4 (MTR4 in humans). However, apart from Mtr4, nuclear exosome cofactors have undergone significant evolutionary divergence. Here, we summarize biochemical and functional knowledge about the nuclear exosome and exemplify its cofactor variety by discussing the best understood model organisms-the budding yeast Saccharomyces cerevisiae, the fission yeast Schizosaccharomyces pombe, and human cells.","doi":"10.1007/978-3-030-31434-7_4","authors":"Schmid M, Jensen TH","authors_abbrev":"Schmid M et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-12-08","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17276908","title":"Cell division: mid-level management.","citation":"Curr Biol 2007 Feb 06;17(3):R93-5","abstract":"When a fission yeast cell divides, the anillin-like protein mid1p helps to position the contractile ring in the cell middle. Recent experiments from two groups have shown how the cell-polarity factor pom1p negatively regulates the distribution of mid1p.","authors":"Sawin KE","authors_abbrev":"Sawin KE","pubmed_publication_date":"06 Feb 2007","pubmed_entrez_date":"2007-02-06","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ577639","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.32"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17190594","title":"A molecular \"zipper\" for microtubules.","citation":"Cell 2006 Dec 29;127(7):1302-4","abstract":"The dynamics of the microtubule cytoskeleton are controlled by microtubule-associated proteins (MAPs). In this issue, show that Mal3p, the yeast EB1 homolog, belongs to a new class of MAPs that \"zipper\" up the seam of the microtubule lattice.","authors":"Kikkawa M, Metlagel Z","authors_abbrev":"Kikkawa M et al.","pubmed_publication_date":"29 Dec 2006","pubmed_entrez_date":"2006-12-28","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012484","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28944093","title":" Ypt4  and  lvs1  regulate vacuolar size and function in  Schizosaccharomyces pombe .","citation":"Cell Logist 2017;7(3):e1335270","abstract":"The yeast vacuole plays key roles in cellular stress responses. Here, we show that deletion of  lvs1 , the fission yeast homolog of the Chediak-Higashi Syndrome  CHS1 / LYST  gene, increases vacuolar size, similar to deletion of the Rab4 homolog  ypt4 . Overexpression of lvs1-YFP rescued vacuolar size in  ypt4Δ  cells, but ypt4-YFP did not rescue  lvs1Δ , suggesting that  lvs1  may act downstream of  ypt4 . Vacuoles were capable of hypotonic shock-induced fusion and recovery in both  ypt4Δ  and  lvs1Δ  cells, although recovery may be slightly delayed in  ypt4Δ . Endocytic and secretory trafficking were not affected, but  ypt4Δ  and  lvs1Δ  strains were sensitive to neutral pH and CaCl 2 , consistent with vacuolar dysfunction. In addition to changes in vacuolar size, deletion of  ypt4  also dramatically increased cell size, similar to  tor1  mutants. These results implicate  ypt4  and  lvs1  in maintenance of vacuolar size and suggest that  ypt4  may link vacuolar homeostasis to cell cycle progression.","doi":"10.1080/21592799.2017.1335270","authors":"Rains A, Bryant Y, Dorsett KA, Culver A, Egbaria J, Williams A, Barnes M, Lamere R, Rossi AR, Waldrep SC, Wilder C, Kliossis E, Styers ML","authors_abbrev":"Rains A et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-09-26","publication_year":"2017","canto_session_key":"00e0a3ede15887bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-09 18:35:27","canto_approved_date":"2022-08-29 16:02:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-09 18:35:20","canto_added_date":"2017-09-27 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.11c","SPBC28E12.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-11-09"},{"uniquename":"PMID:25533956","title":"Meikin is a conserved regulator of meiosis-I-specific kinetochore function.","citation":"Nature 2015 Jan 22;517(7535):466-71","abstract":"The kinetochore is the crucial apparatus regulating chromosome segregation in mitosis and meiosis. Particularly in meiosis I, unlike in mitosis, sister kinetochores are captured by microtubules emanating from the same spindle pole (mono-orientation) and centromeric cohesion mediated by cohesin is protected in the following anaphase. Although meiotic kinetochore factors have been identified only in budding and fission yeasts, these molecules and their functions are thought to have diverged earlier. Therefore, a conserved mechanism for meiotic kinetochore regulation remains elusive. Here we have identified in mouse a meiosis-specific kinetochore factor that we termed MEIKIN, which functions in meiosis I but not in meiosis II or mitosis. MEIKIN plays a crucial role in both mono-orientation and centromeric cohesion protection, partly by stabilizing the localization of the cohesin protector shugoshin. These functions are mediated mainly by the activity of Polo-like kinase PLK1, which is enriched to kinetochores in a MEIKIN-dependent manner. Our integrative analysis indicates that the long-awaited key regulator of meiotic kinetochore function is Meikin, which is conserved from yeasts to humans.","doi":"10.1038/nature14097","authors":"Kim J, Ishiguro K, Nambu A, Akiyoshi B, Yokobayashi S, Kagami A, Ishiguro T, Pendas AM, Takeda N, Sakakibara Y, Kitajima TS, Tanno Y, Sakuno T, Watanabe Y","authors_abbrev":"Kim J et al.","pubmed_publication_date":"22 Jan 2015","pubmed_entrez_date":"2014-12-24","publication_year":"2015","canto_session_key":"e13e49a2df6b7722","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2016-10-26 14:17:56","canto_approved_date":"2024-03-29 10:21:32","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-07-24 00:22:38","canto_added_date":"2015-02-14 01:15:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1753.03c","SPAC23C11.16","HGNC:51253","SPAC17A5.11","YHR014W","SPAC15E1.07c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2016-10-26"},{"uniquename":"PMID:9418887","title":"Activation of the kexin from Schizosaccharomyces pombe requires internal cleavage of its initially cleaved prosequence.","citation":"Mol Cell Biol 1998 Jan;18(1):400-8","abstract":"Members of the kexin family of processing enzymes are responsible for the cleavage of many proproteins during their transport through the secretory pathway. The enzymes themselves are made as inactive precursors, and we investigated the activation process by studying the maturation of Krp1, a kexin from the fission yeast Schizosaccharomyces pombe. Using a cell-free translation-translocation system prepared from Xenopus eggs, we found that Krp1 is made as a preproprotein that loses the presequence during translocation into the endoplasmic reticulum. The prosequence is also rapidly cleaved in a reaction that is autocatalytic and probably intramolecular and is inhibited by disruption of the P domain. Prosequence cleavage normally occurs at Arg-Tyr-Lys-Arg102/ (primary cleavage site) but can occur at Lys-Arg82 (internal cleavage site) and/or Trp-Arg99 when the basic residues are removed from the primary site. Cleavage of the prosequence is necessary but not sufficient for activation, and Krp1 is initially unable to process substrates presented in trans. Full activation is achieved after further incubation in the extract and is coincident with the addition of O-linked sugars. O glycosylation is not, however, essential for activity, and the crucial event appears to be cleavage of the initially cleaved prosequence at the internal site. Our results are consistent with a model in which the cleaved prosequence remains noncovalently associated with the catalytic domain and acts as an autoinhibitor of the enzyme. Inhibition is then relieved by a second (internal) cleavage of the inhibitory prosequence. Further support for this model is provided by our finding that overexpression of a Krp1 prosequence lacking a cleavable internal site dramatically reduced the growth rate of otherwise wild-type S. pombe cells, an effect that was not seen after overexpression of the normal, internally cleavable, prosequence or prosequences that lack the Lys-Arg102 residues.","authors":"Powner D, Davey J","authors_abbrev":"Powner D et al.","pubmed_publication_date":"Jan 1998","pubmed_entrez_date":"1998-01-07","publication_year":"1998","canto_session_key":"b6bfec3d1b81e412","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-12-11 19:42:07","canto_approved_date":"2024-08-13 15:07:47","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-12-11 19:42:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-12-11"},{"uniquename":"PMID:16079914","title":"Molecular analysis of kinetochore architecture in fission yeast.","citation":"EMBO J 2005 Aug 17;24(16):2919-30","abstract":"Kinetochore composition and structure are critical for understanding how kinetochores of different types perform similar functions in chromosome segregation. We used affinity purification to investigate the kinetochore composition and assembly in Schizosaccharomyces pombe. We identified a conserved DASH complex that functions to ensure precise chromosome segregation. Unlike DASH in budding yeast that is localized onto kinetochores throughout the cell cycle, SpDASH is localized onto kinetochores only in mitosis. We also identified two independent groups of kinetochore components, one of which, the Sim4 complex, contains several novel Fta proteins in addition to known kinetochore components. DASH is likely to be associated with the Sim4 complex via Dad1 protein. The other group, Ndc80-MIND-Spc7 complex, contains the conserved Ndc80 and MIND complexes and Spc7 protein. We propose that fission yeast kinetochore is comprised of at least two major structural motifs that are biochemically separable. Our results suggest a high degree of conservation between the kinetochores of budding yeast and fission yeast even though many individual protein subunits do not have a high degree of sequence similarity.","authors":"Liu X, McLeod I, Anderson S, Yates JR, He X","authors_abbrev":"Liu X et al.","pubmed_publication_date":"17 Aug 2005","pubmed_entrez_date":"2005-08-05","publication_year":"2005","canto_session_key":"7af2bdeca0a8d121","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-03-30 14:35:57","canto_approved_date":"2023-05-23 15:19:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-22 15:49:31","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC27F1.04c","SPAC1F8.06","SPBC11C11.03","SPAC16A10.05c","SPAC1805.07c","SPCC188.04c","SPBC336.08","SPAC8C9.17c","SPBP22H7.09c","SPAC4F10.12","SPCC417.02","SPBC409.04c","SPAC1687.20c","SPBC21.01","SPCC1393.04","SPCC1223.15c","SPBC18E5.03c","SPBC27.02c","SPCC1235.07","SPBC3B9.22c","SPAC1783.03","SPAC25B8.14","SPAC29E6.04","SPBP8B7.12c","SPBC32F12.08c","SPBC409.09c","SPCC1020.02","SPAC688.02c","SPAC14C4.16","SPAC11H11.05c","SPAC589.08c"],"gene_count":31,"ltp_gene_count":31,"approved_date":"2016-03-30"},{"uniquename":"EMBL:AU014142","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3002633","title":"Role of a ras homolog in the life cycle of Schizosaccharomyces pombe.","citation":"Cell 1986 Jan 31;44(2):329-36","abstract":"We have analyzed the function of the only ras homolog in S. pombe detectable by Southern blotting, ras1, which is homologous to mammalian ras genes and has been cloned. We have disrupted the ras1 gene and have replaced it with ras1Val17, which corresponds to a transforming variant of mammalian ras. Loss of ras1 activity by disruption results in the complete inability to mate. The cell body of a ras1- strain is extensively deformed, and a ras1-/ras1- diploid sporulates very poorly. Unlike RAS1 and RAS2 of S. cerevisiae, ras1 of S. pombe appears to have no effect on adenylate cyclase activity. This suggests that the target enzymes presumably modulated by ras proteins in signal transduction are not the same for all organisms.","authors":"Fukui Y, Kozasa T, Kaziro Y, Takeda T, Yamamoto M","authors_abbrev":"Fukui Y et al.","pubmed_publication_date":"31 Jan 1986","pubmed_entrez_date":"1986-01-31","publication_year":"1986","canto_session_key":"e6da612efb071dbe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-19 09:14:24","canto_approved_date":"2022-01-03 20:25:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 14:09:46","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-04-19"},{"uniquename":"PMID:12888508","title":"Double-stranded RNA-mediated gene silencing in fission yeast.","citation":"Nucleic Acids Res 2003 Aug 01;31(15):4481-9","abstract":"Double-stranded RNA (dsRNA) can specifically inhibit gene expression in a variety of organisms by invoking post-transcriptional degradation of homologous mRNA. Here we show that dsRNA-mediated gene regulation also occurs in the fission yeast Schizosaccharomyces pombe. We present evidence that: (i) reporter gene silencing is significantly enhanced when additional non-coding sense RNA is co-expressed with antisense RNA; (ii) expression of a panhandle RNA also silences target gene expression; (iii) expression of dsRNA is associated with siRNAs; (iv) a novel host-encoded factor which enhances antisense RNA gene silencing also enhances panhandle RNA-mediated gene inhibition. Both the exogenously introduced lacZ and c-myc genes are shown to be susceptible to dsRNA- mediated gene silencing in this model. Taken together, these data indicate that RNA-mediated gene silencing can occur through a RNAi-like mechanism in fission yeast.","authors":"Raponi M, Arndt GM","authors_abbrev":"Raponi M et al.","pubmed_publication_date":"01 Aug 2003","pubmed_entrez_date":"2003-07-31","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36018799","title":"Painters in chromatin: a unified quantitative framework to systematically characterize epigenome regulation and memory.","citation":"Nucleic Acids Res 2022 Sep 09;50(16):9083-9104","abstract":"In eukaryotes, many stable and heritable phenotypes arise from the same DNA sequence, owing to epigenetic regulatory mechanisms relying on the molecular cooperativity of 'reader-writer' enzymes. In this work, we focus on the fundamental, generic mechanisms behind the epigenome memory encoded by post-translational modifications of histone tails. Based on experimental knowledge, we introduce a unified modeling framework, the painter model, describing the mechanistic interplay between sequence-specific recruitment of chromatin regulators, chromatin-state-specific reader-writer processes and long-range spreading mechanisms. A systematic analysis of the model building blocks highlights the crucial impact of tridimensional chromatin organization and state-specific recruitment of enzymes on the stability of epigenomic domains and on gene expression. In particular, we show that enhanced 3D compaction of the genome and enzyme limitation facilitate the formation of ultra-stable, confined chromatin domains. The model also captures how chromatin state dynamics impact the intrinsic transcriptional properties of the region, slower kinetics leading to noisier expression. We finally apply our framework to analyze experimental data, from the propagation of γH2AX around DNA breaks in human cells to the maintenance of heterochromatin in fission yeast, illustrating how the painter model can be used to extract quantitative information on epigenomic molecular processes.","doi":"10.1093/nar/gkac702","authors":"Abdulla AZ, Vaillant C, Jost D","authors_abbrev":"Abdulla AZ et al.","pubmed_publication_date":"09 Sep 2022","pubmed_entrez_date":"2022-08-26","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-08-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23388459","title":"Kinesin-14 Pkl1 targets γ-tubulin for release from the γ-tubulin ring complex (γ-TuRC) ‬‬‬‬‬‬‬.","citation":"Cell Cycle 2013 Mar 01;12(5):842-8","abstract":"The γ-tubulin ring complex (γ-TuRC) is a key part of microtubule-organizing centers (MTOCs) that control microtubule polarity, organization and dynamics in eukaryotes. Understanding regulatory mechanisms of γ-TuRC function is of fundamental importance, as this complex is central to many cellular processes, including chromosome segregation, fertility, neural development, T-cell cytotoxicity and respiration. The fission yeast microtubule motor kinesin-14 Pkl1 regulates mitosis by binding to the γ-tubulin small complex (γ-TuSC), a subunit of γ-TuRC. Here we investigate the binding mechanism of Pkl1 to γ-TuSC and its functional consequences using genetics, biochemistry, peptide assays and cell biology approaches in vivo and in vitro. We identify two critical elements in the Tail domain of Pkl1 that mediate γ-TuSC binding and trigger release of γ-tubulin from γ-TuRC. Such action disrupts the MTOC and results in failed mitotic spindle assembly. This study is the first demonstration that a motor protein directly affects the structural composition of the γ-TuRC, and we provide details of this mechanism that may be of broad biological importance.","doi":"10.4161/cc.23822","authors":"Olmsted ZT, Riehlman TD, Branca CN, Colliver AG, Cruz LO, Paluh JL","authors_abbrev":"Olmsted ZT et al.","pubmed_publication_date":"01 Mar 2013","pubmed_entrez_date":"2013-02-08","publication_year":"2013","canto_session_key":"400bd40600ad347d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC365.15","SPBC428.20c","SPAC3A11.14c","SPAC25G10.07c","SPBC32F12.04"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"EMBL:X79705","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21224386","title":"Role of Swi6/HP1 self-association-mediated recruitment of Clr4/Suv39 in establishment and maintenance of heterochromatin in fission yeast.","citation":"J Biol Chem 2011 Mar 18;286(11):9308-20","abstract":"Swi6/HP1, an evolutionarily conserved protein, is critical for heterochromatin assembly in fission yeast and higher eukaryotes. In fission yeast, histone deacetylation by histone deacetylases is thought to be followed by H3-Lys-9 methylation by the histone methyltransferase Clr4/Suv39H1. H3-Lys-9-Me2 interacts with the chromodomain of Swi6/HP1. Swi6/HP1 is thought to act downstream of Clr4/Suv39, and further self-association of Swi6/HP1 is assumed to stabilize the heterochromatin structure. Here, we show that the self-association-defective mutant of Swi6 does not interact with Clr4. It not only fails to localize to heterochromatin loci but also interferes with heterochromatic localization of H3-Lys-9-Me2 (and thereby Clr4) and the endogenous Swi6 in a dominant negative manner. Thus, self-association of Swi6/HP1 helps in binding to and recruitment of Clr4 and thereby in establishment and maintenance of heterochromatin by a concerted rather than a sequential mechanism.","doi":"10.1074/jbc.M110.143198","authors":"Haldar S, Saini A, Nanda JS, Saini S, Singh J","authors_abbrev":"Haldar S et al.","pubmed_publication_date":"18 Mar 2011","pubmed_entrez_date":"2011-01-13","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c","SPAC664.01c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9658023","title":"A minisatellite sequence within the propeptide region of the vacuolar carboxypeptidase Y gene of Schizosaccharomyces pombe.","citation":"J Bacteriol 1998 Jul;180(14):3727-9","abstract":"We describe the presence of a minisatellite sequence that displays length polymorphisms in the fission yeast Schizosaccharomyces pombe. The minisatellite sequence was found to reside within the propeptide region of the vacuolar carboxypeptidase Y gene. The minisatellite sequence, which was found only at a single locus, was mitotically stable and displayed length polymorphisms between the two varieties of S. pombe (S. pombe var. pombe and S. pombe var. malidevorans). The minisatellite sequence, however, appeared to be species specific and was absent in other members of the Schizosaccharomyces genus. This report constitutes the first experimental demonstration of the presence of such sequences in yeasts.","authors":"Ingavale SS, Kaur R, Aggarwal P, Bachhawat AK","authors_abbrev":"Ingavale SS et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-07-11","publication_year":"1998","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31485231","title":"Effect of Ethanol-Derived Clove Leaf Extract on the Oxidative Stress Response in Yeast  Schizosaccharomyces pombe .","citation":"Int J Microbiol 2019;2019:2145378","abstract":"Compared to the widely explored antioxidant activity from the clove bud extract, less data are available regarding the potential pharmacological use of clove leaves. Our study aimed to explore the antioxidant activity of clove leaves extract in the cellular level. Thus, we used the yeast  Schizosaccharomyces pombe  as model organisms. Our data indicate that, following extract treatment (100 ppm), the viability of the stationary phase cells of  S. pombe  was higher than without extract and that of calorie restriction treatments. 100 ppm extract treatment also increased cell viability against H 2 O 2 -induced oxidative stress. Those data indicate that the extract could promote oxidative stress tolerance response in yeast cells, which occurred either during the stationary phase or due to exogenous exposure. Higher dose of extract (500 ppm) showed opposite effects, as cell viability was lower than that without treatment. Analysis toward the mitochondrial activity revealed that the extract did not induce mitochondrial activity unlike the calorie restriction treatment. Based on our data, clove leaf extract promotes oxidative stress tolerance response in the yeast  S. pombe , independent to that mitochondrial adaptive ROS signaling which commonly occurs in calorie restriction-induced oxidative stress tolerance response.","doi":"10.1155/2019/2145378","authors":"Fauzya AF, Astuti RI, Mubarik NR","authors_abbrev":"Fauzya AF et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-09-06","publication_year":"2019","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2019-09-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15640846","title":"The Plk3-Cdc25 circuit.","citation":"Oncogene 2005 Jan 10;24(2):299-305","abstract":"Polo-like kinases (Plks) are key regulators of the cell cycle, especially in the G2 phase and mitosis. They are incorporated into signaling networks that regulate many aspects of the cell cycle, including but not limited to centrosome maturation and separation, mitotic entry, chromosome segregation, mitotic exit, and cytokinesis. The Plks have well conserved 30-amino-acid elements, designated polo boxes (PBs), located in their carboxyl-termini, which with their flanking regions constitute a functional Polo-box domain (PBD). Members of the Plk family exist in a variety of organisms including Polo in Drosophila melanogaster; Cdc5 in Saccharomyces cerevisiae; Plo1 in Schizosaccharomyces pombe; Plx1 in Xenopus laevis; and Plk1, Snk/Plk2, Fnk/Prk/Plk3, and Sak in mammals. Polo, Cdc5, and Plo1 are essential for viability. The Plks can be separated into two groups according to their functions. The first group (Polo, Cdc5, plo1, Plx1, and Plk1) primarily performs mitotic functions, whereas the second group (Plk2 and Plk3) appears to have additional functions during the G1, S, and G2 phases of the cell cycle. Several contributions to this issue will discuss different aspects of Plk involvement in cell-cycle regulation. This review, therefore, will focus on the role of Plk3 in regulating Cdc25 phosphatase function and its effect on the cell cycle.","authors":"Myer DL, Bahassi el M, Stambrook PJ","authors_abbrev":"Myer DL et al.","pubmed_publication_date":"10 Jan 2005","pubmed_entrez_date":"2005-01-11","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17512398","title":"DegrAAAded into silence.","citation":"Cell 2007 May 18;129(4):651-3","abstract":"In fission yeast, RNA interference (RNAi)-dependent heterochromatin formation silences transgenes inserted at centromeres. In this issue, Bühler et al. (2007) demonstrate that the RNAi machinery directly targets transgene transcripts. Furthermore, they link transgene silencing to a protein complex resembling the TRAMP complex of budding yeast, which promotes transcript degradation via the exosome. Thus, RNAi-independent transcript degradation may also contribute to heterochromatin gene silencing.","authors":"Bayne EH, White SA, Allshire RC","authors_abbrev":"Bayne EH et al.","pubmed_publication_date":"18 May 2007","pubmed_entrez_date":"2007-05-22","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15811625","title":"Fission yeast mating-type switching: programmed damage and repair.","citation":"DNA Repair (Amst) 2005 May 02;4(5):525-36","abstract":"Mating-type switching in fission yeast follows similar rules as in budding yeast, but the underlying mechanisms are entirely different. Whilst the initiating double-strand cut in Saccharomyces cerevisiae requires recombinational repair for survival, the initial damage in Schizosaccharomyces pombe only affects a single strand, which can be sealed by gap repair in situ, whether or not it serves as an imprint for subsequent switching of mating type from an appropriate donor cassette. Recent papers have linked the transient stalling of a replication fork to the generation of a site-specific nick. This discontinuity then remains protected for a full cell cycle, until it interferes with replication in the next S-phase. It, thereby, represents a valuable model system to study the molecular safeguards to protect a replication fork at a predetermined hindrance to leading-strand extension. The versatility of this experimental system has increased further yet by the recent development of a conditional setup, where imprinting and switching can be repressed or derepressed in response to external stimuli.","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"02 May 2005","pubmed_entrez_date":"2005-04-07","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24841310","title":"piggyBac transposon-based insertional mutagenesis for the fission yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2014;1163:213-22","abstract":"Transposon-mediated insertional mutagenesis is a powerful tool for genetic screens. We have developed a piggyBac transposon-based mutagenesis system for the fission yeast Schizosaccharomyces pombe. Here, we describe in detail the procedure for inducing and selecting transpositions, and two protocols for identifying the transposon insertion sites, one using inverse PCR to identify the insertion sites in individual mutants, and the other using high-throughput sequencing to reveal the insertion sites in a mutant pool containing hundreds to thousands of mutants.","doi":"10.1007/978-1-4939-0799-1_16","authors":"Li J, Du LL","authors_abbrev":"Li J et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-05-21","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23873148","title":"A two-step mechanism for epigenetic specification of centromere identity and function.","citation":"Nat Cell Biol 2013 Sep;15(9):1056-66","abstract":"The basic determinant of chromosome inheritance, the centromere, is specified in many eukaryotes by an epigenetic mark. Using gene targeting in human cells and fission yeast, chromatin containing the centromere-specific histone H3 variant CENP-A is demonstrated to be the epigenetic mark that acts through a two-step mechanism to identify, maintain and propagate centromere function indefinitely. Initially, centromere position is replicated and maintained by chromatin assembled with the centromere-targeting domain (CATD) of CENP-A substituted into H3. Subsequently, nucleation of kinetochore assembly onto CATD-containing chromatin is shown to require either the amino- or carboxy-terminal tail of CENP-A for recruitment of inner kinetochore proteins, including stabilizing CENP-B binding to human centromeres or direct recruitment of CENP-C, respectively.","doi":"10.1038/ncb2805","authors":"Fachinetti D, Folco HD, Nechemia-Arbely Y, Valente LP, Nguyen K, Wong AJ, Zhu Q, Holland AJ, Desai A, Jansen LE, Cleveland DW","authors_abbrev":"Fachinetti D et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-07-23","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11683912","title":"Interaction of fission yeast ORC with essential adenine/thymine stretches in replication origins.","citation":"Genes Cells 2001 Oct;6(10):837-49","abstract":"Eukaryotic DNA replication is initiated from distinct regions on the chromosome. However, the mechanism for recognition of replication origins is not known for most eukaryotes. In fission yeast, replication origins are isolated as autonomously replicating sequences (ARSs). Multiple adenine/thymine clusters are essential for replication, but no short consensus sequences are found. In this paper, we examined the interaction of adenine/thymine clusters with the replication initiation factor ORC.\nThe SpOrc1 or SpOrc2 immunoprecipitates (IPs) containing at least four subunits of SpORC, interacted with the ars2004 fragment, which is derived from a predominant replication origin on the chromosome. SpORC-IPs preferentially interacted with two regions of the ars2004, which consist of consecutive adenines and AAAAT repeats and are essential for ARS activity. The nucleotide sequences required for the interaction with SpORC-IPs correspond closely to those necessary for in vivo ARS activity.\nOur results suggest that the SpORC interacts with adenine/thymine stretches, which have been shown to be the most important component in the fission yeast replication origin. The presence of multiple SpORC-binding sites, with certain sequence variations, is characteristic for the fission yeast replication origins.","authors":"Takahashi T, Masukata H","authors_abbrev":"Takahashi T et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-10-31","publication_year":"2001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP23A10.13","SPBC646.14c","SPBC29A10.15","SPBC685.09"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:24554432","title":"The Tea4-PP1 landmark promotes local growth by dual Cdc42 GEF recruitment and GAP exclusion.","citation":"J Cell Sci 2014 May 01;127(Pt 9):2005-16","abstract":"Cell polarization relies on small GTPases, such as Cdc42, which can break symmetry through self-organizing principles, and landmarks that define the axis of polarity. In fission yeast, microtubules deliver the Tea1-Tea4 complex to mark cell poles for growth, but how this complex activates Cdc42 is unknown. Here, we show that ectopic targeting of Tea4 to cell sides promotes the local activation of Cdc42 and cell growth. This activity requires that Tea4 binds the type I phosphatase (PP1) catalytic subunit Dis2 or Sds21, and ectopic targeting of either catalytic subunit is similarly instructive for growth. The Cdc42 guanine-nucleotide-exchange factor Gef1 and the GTPase-activating protein Rga4 are required for Tea4-PP1-dependent ectopic growth. Gef1 is recruited to ectopic Tea4 and Dis2 locations to promote Cdc42 activation. By contrast, Rga4 is locally excluded by Tea4, and its forced colocalization with Tea4 blocks ectopic growth, indicating that Rga4 must be present, but at sites distinct from Tea4. Thus, a Tea4-PP1 landmark promotes local Cdc42 activation and growth both through Cdc42 GEF recruitment and by creating a local trough in a Cdc42 GAP.","doi":"10.1242/jcs.142174","authors":"Kokkoris K, Gallo Castro D, Martin SG","authors_abbrev":"Kokkoris K et al.","pubmed_publication_date":"01 May 2014","pubmed_entrez_date":"2014-02-21","publication_year":"2014","canto_session_key":"ea5eb1c311e9f19d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2017-03-07 16:25:48","canto_approved_date":"2023-12-31 16:36:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-06 17:15:19","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G10.02c","SPBC1706.01","SPBC28E12.03","SPBC106.20","SPAC110.03","SPAC16E8.09","SPCC31H12.05c","SPBC776.02c","SPAC2F7.03c","SPCC1223.06","SPCC895.05","SPAC24H6.09"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2017-03-07"},{"uniquename":"PMID:8493107","title":"Algorithms and software tools for ordering clone libraries: application to the mapping of the genome of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1993 Apr 25;21(8):1965-74","abstract":"A complete set of software tools to aid the physical mapping of a genome has been developed and successfully applied to the genomic mapping of the fission yeast Schizosaccharomyces pombe. Two approaches were used for ordering single-copy hybridisation probes: one was based on the simulated annealing algorithm to order all probes, and another on inferring the minimum-spanning subset of the probes using a heuristic filtering procedure. Both algorithms produced almost identical maps, with minor differences in the order of repetitive probes and those having identical hybridisation patterns. A separate algorithm fitted the clones to the established probe order. Approaches for handling experimental noise and repetitive elements are discussed. In addition to these programs and the database management software, tools for visualizing and editing the data are described. The issues of combining the information from different libraries are addressed. Also, ways of handling multiple-copy probes and non-hybridisation data are discussed.","authors":"Mott R, Grigoriev A, Maier E, Hoheisel J, Lehrach H","authors_abbrev":"Mott R et al.","pubmed_publication_date":"25 Apr 1993","pubmed_entrez_date":"1993-04-25","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18385517","title":"Cds1 controls the release of Cdc14-like phosphatase Flp1 from the nucleolus to drive full activation of the checkpoint response to replication stress in fission yeast.","citation":"Mol Biol Cell 2008 Jun;19(6):2488-99","abstract":"The Cdc14p-like phosphatase Flp1p (also known as Clp1p) is regulated by cell cycle-dependent changes in its subcellular localization. Flp1p is restricted to the nucleolus and spindle pole body until prophase, when it is dispersed throughout the nucleus, mitotic spindle, and medial ring. Once released, Flp1p antagonizes Cdc2p/cyclin activity by reverting Cdc2p-phosphorylation sites on Cdc25p. On replication stress, ataxia-telangiectasia mutated/ATM/Rad3-related kinase Rad3p activates Cds1p, which phosphorylates key proteins ensuring the stability of stalled DNA replication forks. Here, we show that replication stress induces changes in the subcellular localization of Flp1p in a checkpoint-dependent manner. Active Cds1p checkpoint kinase is required to release Flp1p into the nucleus. Consistently, a Flp1p mutant (flp1-9A) lacking all potential Cds1p phosphorylation sites fails to relocate in response to replication blocks and, similarly to cells lacking flp1 (Deltaflp1), presents defects in checkpoint response to replication stress. Deltaflp1 cells accumulate reduced levels of a less active Cds1p kinase in hydroxyurea (HU), indicating that nuclear Flp1p regulates Cds1p full activation. Consistently, Deltaflp1 and flp1-9A have an increased percentage of Rad22p-recombination foci during HU treatment. Together, our data show that by releasing Flp1p into the nucleus Cds1p checkpoint kinase modulates its own full activation during replication stress.","authors":"Díaz-Cuervo H, Bueno A","authors_abbrev":"Díaz-Cuervo H et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-04","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC8E11.02c","SPAC1782.09c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:25552606","title":"Identification of new players in cell division, DNA damage response, and morphogenesis through construction of Schizosaccharomyces pombe deletion strains.","citation":"G3 (Bethesda) 2014 Dec 31;5(3):361-70","abstract":"Many fundamental biological processes are studied using the fission yeast, Schizosaccharomyces pombe. Here we report the construction of a set of 281 haploid gene deletion strains covering many previously uncharacterized genes. This collection of strains was tested for growth under a variety of different stress conditions. We identified new genes involved in DNA metabolism, completion of the cell cycle, and morphogenesis. This subset of nonessential gene deletions will add to the toolkits available for the study of biological processes in S. pombe.","doi":"10.1534/g3.114.015701","authors":"Chen JS, Beckley JR, McDonald NA, Ren L, Mangione M, Jang SJ, Elmore ZC, Rachfall N, Feoktistova A, Jones CM, Willet AH, Guillen R, Bitton DA, Bähler J, Jensen MA, Rhind N, Gould KL","authors_abbrev":"Chen JS et al.","pubmed_publication_date":"31 Dec 2014","pubmed_entrez_date":"2015-01-02","publication_year":"2014","canto_session_key":"6cf4da7b6ffd2aa6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-11-23 16:47:46","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-25 11:29:26","canto_added_date":"2015-01-03 01:17:06","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":264,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_25552606_phaf.tsv"}],"genes":["SPCC1442.08c","SPCC18.11c","SPCC1259.05c","SPBC16D10.06","SPCC1235.06","SPAC30D11.04c","SPAC607.02c","SPCC4B3.17","SPAC7D4.07c","SPCC970.06","SPBC15C4.01c","SPBC26H8.14c","SPAC458.05","SPCC1259.13","SPCC794.08","SPCC4B3.16","SPBC887.22","SPBC1683.05","SPBC83.10","SPBC25H2.18","SPCC1235.16","SPAC6B12.18","SPBC21B10.15","SPAC1B3.20","SPAC1002.15c","SPBC119.07","SPCC1259.16","SPBC19G7.08c","SPAC1B3.21","SPCC4B3.10c","SPCC290.04","SPAC4D7.14","SPBC28F2.07","SPBC651.10","SPAC19A8.08","SPBC19C7.03","SPBP16F5.04","SPAC16E8.09","SPAC20G4.09","SPAC1705.03c","SPAC16.03c","SPAC24B11.09","SPAC15A10.17","SPAC3H1.09c","SPBC13E7.11","SPBC25H2.16c","SPAC22F3.10c","SPAC10F6.01c","SPAC1486.10","SPCC1795.02c","SPBC11G11.05","SPBC1773.15","SPAC1F7.14c","SPCC1902.02","SPBC3E7.01","SPBC1718.01","SPBC19F8.08","SPBC1604.25","SPCC737.02c","SPAC19G12.05","SPCC825.02","SPAC17C9.02c","SPAC19G12.11","SPBC1604.04","SPBC3D6.08c","SPBC839.19","SPCC4F11.02","SPBC839.16","SPCC16C4.03","SPAC821.11","SPAC1F12.07","SPAC19G12.17","SPAC1783.04c","SPAC19B12.06c","SPCC4B3.20","SPBC3H7.15","SPCC1672.11c"],"gene_count":77,"ltp_gene_count":0,"approved_date":"2015-03-25"},{"uniquename":"PMID:38429687","title":"A clustering procedure for three-way RNA sequencing data using data transformations and matrix-variate Gaussian mixture models.","citation":"BMC Bioinformatics 2024 Mar 01;25(1):90","abstract":"RNA sequencing of time-course experiments results in three-way count data where the dimensions are the genes, the time points and the biological units. Clustering RNA-seq data allows to extract groups of co-expressed genes over time. After standardisation, the normalised counts of individual genes across time points and biological units have similar properties as compositional data. We propose the following procedure to suitably cluster three-way RNA-seq data: (1) pre-process the RNA-seq data by calculating the normalised expression profiles, (2) transform the data using the additive log ratio transform to map the composition in the D-part Aitchison simplex to a    D   -   1     -dimensional Euclidean vector, (3) cluster the transformed RNA-seq data using matrix-variate Gaussian mixture models and (4) assess the quality of the overall cluster solution and of individual clusters based on cluster separation in the transformed space using density-based silhouette information and on compactness of the cluster in the original space using cluster maps as a suitable visualisation. The proposed procedure is illustrated on RNA-seq data from fission yeast and results are also compared to an analogous two-way approach after flattening out the biological units.","doi":"10.1186/s12859-024-05717-6","authors":"Scharl T, Grün B","authors_abbrev":"Scharl T et al.","pubmed_publication_date":"01 Mar 2024","pubmed_entrez_date":"2024-03-01","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-03-03 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38181050","title":"The Cross-Regulation Between Set1, Clr4, and Lsd1/2 in Schizosaccharomyces pombe.","citation":"PLoS Genet 2024 Jan 05;20(1):e1011107","abstract":"Eukaryotic chromatin is organized into either silenced heterochromatin or relaxed euchromatin regions, which controls the accessibility of transcriptional machinery and thus regulates gene expression. In fission yeast, Schizosaccharomyces pombe, Set1 is the sole H3K4 methyltransferase and is mainly enriched at the promoters of actively transcribed genes. In contrast, Clr4 methyltransferase initiates H3K9 methylation, which has long been regarded as a hallmark of heterochromatic silencing. Lsd1 and Lsd2 are two highly conserved H3K4 and H3K9 demethylases. As these histone-modifying enzymes perform critical roles in maintaining histone methylation patterns and, consequently, gene expression profiles, cross-regulations among these enzymes are part of the complex regulatory networks. Thus, elucidating the mechanisms that govern their signaling and mutual regulations remains crucial. Here, we demonstrated that C-terminal truncation mutants, lsd1-ΔHMG and lsd2-ΔC, do not compromise the integrity of the Lsd1/2 complex but impair their chromatin-binding capacity at the promoter region of target genomic loci. We identified protein-protein interactions between Lsd1/2 and Raf2 or Swd2, which are the subunits of the Clr4 complex (CLRC) and Set1-associated complex (COMPASS), respectively. We showed that Clr4 and Set1 modulate the protein levels of Lsd1 and Lsd2 in opposite ways through the ubiquitin-proteasome-dependent pathway. During heat stress, the protein levels of Lsd1 and Lsd2 are upregulated in a Set1-dependent manner. The increase in protein levels is crucial for differential gene expression under stress conditions. Together, our results support a cross-regulatory model by which Set1 and Clr4 methyltransferases control the protein levels of Lsd1/2 demethylases to shape the dynamic chromatin landscape.","doi":"10.1371/journal.pgen.1011107","authors":"Liu H, Marayati BF, de la Cerda D, Lemezis BM, Gao J, Song Q, Chen M, Reid KZ","authors_abbrev":"Liu H et al.","pubmed_publication_date":"05 Jan 2024","pubmed_entrez_date":"2024-01-05","publication_year":"2024","canto_session_key":"3b1166bb2423f4aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ke Zhang Reid","canto_first_approved_date":"2024-05-09 07:03:02","canto_approved_date":"2024-06-21 16:25:08","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-05-06 18:30:39","canto_added_date":"2024-01-06 00:25:04","annotation_curators":[{"name":"Ke Zhang Reid","community_curator":true,"annotation_count":49,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.09","SPAC23E2.02","SPCC594.05c","SPCC970.07c","SPAC17G8.09","SPBC354.03","SPBC1105.11c","SPAC23H3.05c","SPBC13G1.08c","SPBC8D2.04","SPCC306.04c","SPAC30D11.08c","SPBC4.07c","SPCC1919.15","SPAC3A11.08","SPCC970.10c","SPBC18H10.06c","SPCC4G3.07c","SPBC146.09c","SPBC428.08c","SPCC613.12c","SPCC11E10.08","SPAC17H9.10c","SPCC18.11c","SPAC1834.04"],"gene_count":25,"ltp_gene_count":24,"approved_date":"2024-05-09"},{"uniquename":"PMID:8809017","title":"Localization of modified nucleotides in Schizosaccharomyces pombe spliceosomal small nuclear RNAs: modified nucleotides are clustered in functionally important regions.","citation":"RNA 1996 Sep;2(9):909-18","abstract":"The specific and dynamic RNA:RNA interactions between pre-mRNA and small nuclear RNAs (snRNAs), especially U2, U5, and U6 snRNAs, form the catalytic core and are at the heart of the spliceosome formation. The functionally important regions in the snRNAs correspond to the highly modified regions in snRNAs from human, rat, and plant cells. To better understand the importance of the modifications of snRNAs, we identified and localized the modified nucleotides in the five spliceosomal snRNAs of Schizosaccharomyces pombe cells. Twenty-two modified nucleotides, including base methylations, 2'-O-methylations, and pseudouridines, were found in the five spliceosomal snRNAs. The conservation of modified nucleotides between human and S. pombe snRNAs is striking. In addition, most of the modified nucleotides are in or around positions that form hydrogen bonds with the pre-mRNA or with other snRNAs. The results are consistent with the suggestion that modified nucleotides are clustered around functionally important regions of the spliceosomal snRNAs. These data provide the basis for further functional studies on posttranscriptional modifications in spliceosomal snRNAs.","authors":"Gu J, Patton JR, Shimba S, Reddy R","authors_abbrev":"Gu J et al.","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_session_key":"49b3aaa6f50dcd63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-27 12:55:47","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-27 12:55:36","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.01","SPSNRNA.05","SPSNRNA.06","SPSNRNA.02","SPSNRNA.04"],"gene_count":5,"ltp_gene_count":0,"approved_date":"2014-06-27"},{"uniquename":"PMID:7651414","title":"Two-step activation of meiosis by the mat1 locus in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1995 Sep;15(9):4964-70","abstract":"The mat1 locus is a key regulator of both conjugation and meiosis in the fission yeast Schizosaccharomyces pombe. Two alternative DNA segments of this locus, mat1-P and mat1-M, specify the haploid cell types (Plus and Minus). Each segment includes two genes: mat1-P includes mat1-Pc and mat1-Pm, while mat1-M includes mat1-Mc and mat1-Mm. The mat1-Pc and mat1-Mc genes are responsible for establishing the pheromone communication system that mediates conjugation between P and M cells, while all four mat1 genes are required for meiosis in diploid P/M cells. Our understanding of the initiation of meiosis is based largely on indirect observations, and a more precise investigation of these events was required to define the interaction between the mat1 genes. Here we resolve this issue using synthetic pheromones and P/M strains with mutations in either mat1-Pc or mat1-Mc. Our results suggest a model in which the mat1 locus plays two roles in controlling meiosis. In the first instance, the mat1-Pc and mat1-Mc functions are required to produce the mating pheromones and receptors that allow the generation of a pheromone signal. This signal is required to induce the expression of mat1-Pm and mat1-Mm. This appears to be the major pheromone-dependent step in controlling meiosis since ectopic expression of these genes allows meiosis in the absence of mat1-Pc and mat1-Mc. The mat1-Pm and mat1-Mm products complete the initiation of meiosis by activating transcription of the mei3 gene.","authors":"Willer M, Hoffmann L, Styrkársdóttir U, Egel R, Davey J, Nielsen O","authors_abbrev":"Willer M et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_session_key":"24e9f1d9ea02f952","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-12 14:13:40","canto_approved_date":"2026-04-08 07:32:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-05-04 15:44:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMTR.01","SPCC1795.06","SPMTR.02","SPBC119.04","SPBC23G7.17c","SPBC23G7.09","SPBPJ4664.03","SPAC513.03","SPAPB8E5.05","SPBC19C2.05"],"gene_count":10,"ltp_gene_count":5,"approved_date":"2018-10-12"},{"uniquename":"PMID:17122395","title":"Green tea polyphenols function as prooxidants to activate oxidative-stress-responsive transcription factors in yeasts.","citation":"Appl Environ Microbiol 2007 Jan;73(2):572-80","abstract":"Epigallocatechin gallate (EGCG) is the most abundant polyphenolic flavonoid in green tea. Catechin and its derivatives, including EGCG, are widely believed to function as antioxidants. Here we demonstrate that both EGCG and green tea extract (GTE) cause oxidative stress-related responses in the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe under weak alkaline conditions in terms of the activation of oxidative-stress-responsive transcription factors. GTE as well as EGCG induced the nuclear localization of Yap1 in S. cerevisiae, which was repressed by the addition of catalase but not by the addition of superoxide dismutase. The same phenomena were observed for the nucleocytoplasmic localization of Msn2 in S. cerevisiae and Pap1, a Yap1 homologue, in S. pombe. The formation of intramolecular disulfide bonds has been proposed to be crucial for the H(2)O(2)-induced nuclear localization of Yap1, and we verified the importance of cysteine residues of Yap1 in response to EGCG and GTE. Additionally, we show that EGCG and GTE produce H(2)O(2) in a weak alkaline medium. Finally, we conclude that tea polyphenols are able to act as prooxidants to cause a response to oxidative stress in yeasts under certain conditions.","authors":"Maeta K, Nomura W, Takatsume Y, Izawa S, Inoue Y","authors_abbrev":"Maeta K et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2006-11-24","publication_year":"2007","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD2668","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25526805","title":"Uncovering the role of Sgf73 in maintaining SAGA deubiquitinating module structure and activity.","citation":"J Mol Biol 2015 Apr 24;427(8):1765-78","abstract":"The SAGA (Spt-Ada-Gcn5 acetyltransferase) complex performs multiple functions in transcription activation including deubiquitinating histone H2B, which is mediated by a subcomplex called the deubiquitinating module (DUBm). The yeast DUBm comprises a catalytic subunit, Ubp8, and three additional subunits, Sgf11, Sus1 and Sgf73, all of which are required for DUBm activity. A portion of the non-globular Sgf73 subunit lies between the Ubp8 catalytic domain and the ZnF-UBP domain and has been proposed to contribute to deubiquitinating activity by maintaining the catalytic domain in an active conformation. We report structural and solution studies of the DUBm containing two different Sgf73 point mutations that disrupt deubiquitinating activity. We find that the Sgf73 mutations abrogate deubiquitinating activity by impacting the Ubp8 ubiquitin-binding fingers region and they have an unexpected effect on the overall folding and stability of the DUBm complex. Taken together, our data suggest a role for Sgf73 in maintaining both the organization and the ubiquitin-binding conformation of Ubp8, thereby contributing to overall DUBm activity.","doi":"10.1016/j.jmb.2014.12.004","authors":"Yan M, Wolberger C","authors_abbrev":"Yan M et al.","pubmed_publication_date":"24 Apr 2015","pubmed_entrez_date":"2014-12-21","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC126.04c","SPAC13A11.04c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:15466419","title":"Swi5 acts in meiotic DNA joint molecule formation in Schizosaccharomyces pombe.","citation":"Genetics 2004 Dec;168(4):1891-8","abstract":"Previously isolated Schizosaccharomyces pombe swi5 mutants are defective in mitotic mating-type switching and in repair of meiotic recombination-related DNA double-strand breaks. Here, we identify the swi5 gene, which encodes an 85-amino-acid polypeptide, similar to Sae3 of Saccharomyces cerevisiae, with an N-terminal predicted coiled-coil domain. A swi5 complete deletion mutant had normal mitotic growth rate but was hypersensitive to DNA-damaging agents and defective in mating-type switching. In meiosis, recombinant frequencies were reduced by a factor of approximately 10. The swi5 deletion strongly reduced the viable spore yields of mutants lacking Rhp55 or Rhp57, proteins thought to aid joint molecule formation. Furthermore, the swi5 deletion strongly suppressed the low viable spore yield of mutants lacking Mus81*Eme1, which resolves joint molecules such as Holliday junctions. These and previous results indicate that the small Swi5 polypeptide acts in a branched pathway of joint molecule formation to repair meiotic DNA breaks.","authors":"Ellermeier C, Schmidt H, Smith GR","authors_abbrev":"Ellermeier C et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-10-07","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC409.03","SPAC3C7.03c","SPCC4G3.05c","SPAPB1E7.06c"],"gene_count":4,"ltp_gene_count":3},{"uniquename":"PMID:30382337","title":"Mating-type switching by homology-directed recombinational repair: a matter of choice.","citation":"Curr Genet 2019 Apr;65(2):351-362","abstract":"In eukaryotes, all DNA transactions happen in the context of chromatin that often takes part in regulatory mechanisms. In particular, chromatin structure can regulate exchanges of DNA occurring through homologous recombination. Few systems have provided as detailed a view on this phenomenon as mating-type switching in yeast. Mating-type switching entails the choice of a template for the gene conversions of the expressed mating-type locus. In the fission yeast Schizosaccharomyces pombe, correct template choice requires two competing small recombination enhancers, SRE2 and SRE3, that function in the context of heterochromatin. These two enhancers act with the Swi2/Swi5 recombination accessory complex to initiate strand exchange in a cell-type-specific manner, from SRE2 in M cells and SRE3 in P cells. New research indicates that the Set1C complex, responsible for H3K4 methylation, and the Brl2 ubiquitin ligase, that catalyzes H2BK119 ubiquitylation, participate in the cell-type-specific selection of SRE2 or SRE3. Here, we review these findings, compare donor preference in S. pombe to the distantly related budding yeast Saccharomyces cerevisiae, and contrast the positive effects of heterochromatin on the donor selection process with other situations, where heterochromatin represses recombination.","doi":"10.1007/s00294-018-0900-2","authors":"Thon G, Maki T, Haber JE, Iwasaki H","authors_abbrev":"Thon G et al.","pubmed_publication_date":"Apr 2019","pubmed_entrez_date":"2018-11-02","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-03 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1896014","title":"Assignment of ten DNA repair genes from Schizosaccharomyces pombe to chromosomal NotI restriction fragments.","citation":"Mol Gen Genet 1991 Sep;228(3):470-2","abstract":"Ten DNA repair (rad) genes from the fission yeast, Schizosaccharomyces pombe were mapped to the 17 NotI fragments of the three chromosomes. Nine of the genes map to chromosome I, but there is no evidence for significant clustering.","authors":"Broughton BC, Barbet N, Murray J, Watts FZ, Koken MH, Lehmann AR, Carr AM","authors_abbrev":"Broughton BC et al.","pubmed_publication_date":"Sep 1991","pubmed_entrez_date":"1991-09-01","publication_year":"1991","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15601841","title":"Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the response to DNA damage.","citation":"Mol Cell Biol 2005 Jan;25(1):185-96","abstract":"The Schizosaccharomyces pombe SMC proteins Rad18 (Smc6) and Spr18 (Smc5) exist in a high-M(r) complex which also contains the non-SMC proteins Nse1, Nse2, Nse3, and Rad62. The Smc5-6 complex, which is essential for viability, is required for several aspects of DNA metabolism, including recombinational repair and maintenance of the DNA damage checkpoint. We have characterized Nse2 and show here that it is a SUMO ligase. Smc6 (Rad18) and Nse3, but not Smc5 (Spr18) or Nse1, are sumoylated in vitro in an Nse2-dependent manner, and Nse2 is itself autosumoylated, predominantly on the C-terminal part of the protein. Mutations of C195 and H197 in the Nse2 RING-finger-like motif abolish Nse2-dependent sumoylation. nse2.SA mutant cells, in which nse2.C195S-H197A is integrated as the sole copy of nse2, are viable, whereas the deletion of nse2 is lethal. Smc6 (Rad18) is sumoylated in vivo: the sumoylation level is increased upon exposure to DNA damage and is drastically reduced in the nse2.SA strain. Since nse2.SA cells are sensitive to DNA-damaging agents and to exposure to hydroxyurea, this implicates the Nse2-dependent sumoylation activity in DNA damage responses but not in the essential function of the Smc5-6 complex.","authors":"Andrews EA, Palecek J, Sergeant J, Taylor E, Lehmann AR, Watts FZ","authors_abbrev":"Andrews EA et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-12-17","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPCC5E4.06","SPAC16A10.06c","SPCC645.04"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PANTHER:PTHR43016:SF3","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3H1.02c","HGNC:17663"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38166399","title":"Fission yeast Wee1 is required for stable kinetochore-microtubule attachment.","citation":"Open Biol 2024 Jan;14(1):230379","abstract":"Wee1 is a cell cycle regulator that phosphorylates Cdk1/Cdc2 and inhibits G2/M transition. Loss of Wee1 in fission yeast results in an early onset of mitosis. Interestingly, we found that cells lacking Wee1 require the functional spindle checkpoint for their viability. Genetic analysis indicated that the requirement is not attributable to the early onset of mitosis. Live-cell imaging revealed that some kinetochores are not attached or bioriented in the  wee1  mutant. Furthermore, Mad2, a component of the spindle checkpoint known to recognize unattached kinetochores, accumulates in the vicinity of the spindle, representing activation of the spindle checkpoint in the mutant. It appears that the  wee1  mutant cannot maintain stable kinetochore-microtubule attachment, and relies on the delay imposed by the spindle checkpoint for establishing biorientation of kinetochores. This study revealed a role of Wee1 in ensuring accurate segregation of chromosomes during mitosis, and thus provided a basis for a new principle of cancer treatment with Wee1 inhibitors.","doi":"10.1098/rsob.230379","authors":"Takado M, Yamamoto TG, Chikashige Y, Matsumoto T","authors_abbrev":"Takado M et al.","pubmed_publication_date":"Jan 2024","pubmed_entrez_date":"2024-01-03","publication_year":"2024","canto_session_key":"cecb9f2b2616cb63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-11 16:31:46","canto_approved_date":"2026-01-26 21:20:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-04 08:57:43","canto_added_date":"2024-01-04 00:25:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC20F10.06","SPBC11B10.09","SPCC1322.12c","SPBC3D6.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2024-01-11"},{"uniquename":"PMID:41841625","title":"Tracking Mitotic Spindle Dynamics and Protein Localization in Fission Yeast With FYSKA, the Fission Yeast Spindle Kymograph Analyzer.","citation":"Cytoskeleton (Hoboken) 2026 Mar 17;","abstract":"Quantitative analysis of mitotic spindle dynamics requires accurate tracking despite challenges such as cell drift, spindle rotation, and fluctuating fluorescence signals. We developed the Fission Yeast Spindle Kymograph Analyzer (FYSKA), an automated software tool that tracks the spindle and constructs kymographs of spindle-associated proteins in Schizosaccharomyces pombe. FYSKA uses fluorescent spindle pole markers to achieve sub-pixel precision, applies error correction for transient signal loss, and maintains robustness under rotation or drift. Compared to semi-automated approaches, it generates kymographs with more consistent intensity profiles and improved capture of the spindle axis. Using FYSKA, we quantified spindle length fluctuations and examined localization patterns of the kinesin-5 motor Cut7 including asymmetric spindle pole recruitment in Cut11-7. These examples show how FYSKA enables automated, reproducible analysis of mitotic spindle organization and protein dynamics.","doi":"10.1002/cm.70109","authors":"Zhou B, Gergely ZR, Jones MH, Betterton MD","authors_abbrev":"Zhou B et al.","pubmed_publication_date":"17 Mar 2026","pubmed_entrez_date":"2026-03-17","publication_year":"2026","canto_session_key":"21d156245a93b0f0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-18 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27548313","title":"Transcription factors mediate condensin recruitment and global chromosomal organization in fission yeast.","citation":"Nat Genet 2016 Oct;48(10):1242-52","abstract":"It is becoming clear that structural-maintenance-of-chromosomes (SMC) complexes such as condensin and cohesin are involved in three-dimensional genome organization, yet their exact roles in functional organization remain unclear. We used chromatin interaction analysis by paired-end tag sequencing (ChIA-PET) to comprehensively identify genome-wide associations mediated by condensin and cohesin in fission yeast. We found that although cohesin and condensin often bind to the same loci, they direct different association networks and generate small and larger chromatin domains, respectively. Cohesin mediates associations between loci positioned within 100 kb of each other; condensin can drive longer-range associations. Moreover, condensin, but not cohesin, connects cell cycle-regulated genes bound by mitotic transcription factors. This study describes the different functions of condensin and cohesin in genome organization and how specific transcription factors function in condensin loading, cell cycle-dependent genome organization and mitotic chromosome organization to support faithful chromosome segregation.","doi":"10.1038/ng.3647","authors":"Kim KD, Tanizawa H, Iwasaki O, Noma K","authors_abbrev":"Kim KD et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-08-23","publication_year":"2016","canto_session_key":"3a5f16c5574b0a11","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-02-27 21:24:53","canto_approved_date":"2020-02-27 21:24:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-10 15:33:34","canto_added_date":"2016-08-25 00:15:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G10.12c","SPCC290.04","SPAC343.20","SPAC821.09","SPBP4H10.06c","SPBC1105.05"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2020-02-27"},{"uniquename":"PMID:31454903","title":"An Assay to Study Intra-Chromosomal Deletions in Yeast.","citation":"Methods Protoc 2019 Aug 26;2(3)","abstract":"An accurate DNA damage response pathway is critical for the repair of DNA double-strand breaks. Repair may occur by homologous recombination, of which many different sub-pathways have been identified. Some recombination pathways are conservative, meaning that the chromosome sequences are preserved, and others are non-conservative, leading to some alteration of the DNA sequence. We describe an in vivo genetic assay to study non-conservative intra-chromosomal deletions at regions of non-tandem direct repeats in  Schizosaccharomyces pombe . This assay can be used to study both spontaneous breaks arising during DNA replication and induced double-strand breaks created with the  S. cerevisiae  homothallic endonuclease ( HO ). The preliminary genetic validation of this assay shows that spontaneous breaks require  rad52 +   but not  rad51 +  , while induced breaks require both genes, in agreement with previous studies. This assay will be useful in the field of DNA damage repair for studying mechanisms of intra-chromosomal deletions.","doi":"10.3390/mps2030074","authors":"Lucas BE, McPherson MT, Hawk TM, Wilson LN, Kroh JM, Hickman KG, Fitzgerald SR, Disbennett WM, Rollins PD, Hylton HM, Baseer MA, Montgomery PN, Wu JQ, Petreaca RC","authors_abbrev":"Lucas BE et al.","pubmed_publication_date":"26 Aug 2019","pubmed_entrez_date":"2019-08-29","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-08-30 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000080","title":"Representation of plant development as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the development of a plant structure as a biological process. The underlying equivalence axiom template is \"'anatomical structure development' and 'results in development of' some P\", where P is a plant anatomical entity (PO:0025131).","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26006103","title":"Nitrosative stress induces a novel intra-S checkpoint pathway in Schizosaccharomyces pombe involving phosphorylation of Cdc2 by Wee1.","citation":"Free Radic Biol Med 2015 Sep;86:145-55","abstract":"Excess production of nitric oxide and reactive nitrogen intermediates causes nitrosative stress on cells. Schizosaccharomyces pombe was used as a model to study the cell cycle regulation under nitrosative stress response. We discovered a novel intra-S-phase checkpoint that is activated in S. pombe under nitrosative stress. The mechanism for this intra-S-phase checkpoint activation is distinctly different than previously reported for genotoxic stress in S. pombe by methyl methane sulfonate. Our flow cytometry data established the fact that Wee1 phosphorylates Cdc2 Tyr15 which leads to replication slowdown in the fission yeast under nitrosative stress. We checked the roles of Rad3, Rad17, Rad26, Swi1, Swi3, Cds1, and Chk1 under nitrosative stress but those were not involved in the activation of the DNA replication checkpoint. Rad24 was found to be involved in intra-S-phase checkpoint activation in S. pombe under nitrosative stress but that was independent of Cdc25.","doi":"10.1016/j.freeradbiomed.2015.05.021","authors":"Biswas P, Kar P, Ghosh S","authors_abbrev":"Biswas P et al.","pubmed_publication_date":"Sep 2015","pubmed_entrez_date":"2015-05-27","publication_year":"2015","canto_session_key":"8fc3df1608381305","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-05-28 00:19:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32579943","title":"The ASC-1 Complex Disassembles Collided Ribosomes.","citation":"Mol Cell 2020 Aug 20;79(4):603-614.e8","abstract":"Translating ribosomes that slow excessively incur collisions with trailing ribosomes. Persistent collisions are detected by ZNF598, a ubiquitin ligase that ubiquitinates sites on the ribosomal 40S subunit to initiate pathways of mRNA and protein quality control. The collided ribosome complex must be disassembled to initiate downstream quality control, but the mechanistic basis of disassembly is unclear. Here, we reconstitute the disassembly of a collided polysome in a mammalian cell-free system. The widely conserved ASC-1 complex (ASCC) containing the ASCC3 helicase disassembles the leading ribosome in an ATP-dependent reaction. Disassembly, but not ribosome association, requires 40S ubiquitination by ZNF598, but not GTP-dependent factors, including the Pelo-Hbs1L ribosome rescue complex. Trailing ribosomes can elongate once the roadblock has been removed and only become targets if they subsequently stall and incur collisions. These findings define the specific role of ASCC during ribosome-associated quality control and identify the molecular target of its activity.","doi":"10.1016/j.molcel.2020.06.006","authors":"Juszkiewicz S, Speldewinde SH, Wan L, Svejstrup JQ, Hegde RS","authors_abbrev":"Juszkiewicz S et al.","pubmed_publication_date":"20 Aug 2020","pubmed_entrez_date":"2020-06-25","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC15D4.13c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15577889","title":"Wee beasties.","citation":"Nature 2004 Dec 02;432(7017):557","abstract":"","authors":"Nurse P","authors_abbrev":"Nurse P","pubmed_publication_date":"02 Dec 2004","pubmed_entrez_date":"2004-12-04","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24013502","title":"Epe1 recruits BET family bromodomain protein Bdf2 to establish heterochromatin boundaries.","citation":"Genes Dev 2013 Sep 01;27(17):1886-902","abstract":"Heterochromatin spreading leads to the silencing of genes within its path, and boundary elements have evolved to constrain such spreading. In fission yeast, heterochromatin at centromeres I and III is flanked by inverted repeats termed IRCs, which are required for proper boundary functions. However, the mechanisms by which IRCs prevent heterochromatin spreading are unknown. Here, we identified Bdf2, which is homologous to the mammalian bromodomain and extraterminal (BET) family double bromodomain proteins involved in diverse types of cancers, as a factor required for proper boundary function at IRCs. Bdf2 is enriched at IRCs through its interaction with the boundary protein Epe1. The bromodomains of Bdf2 recognize acetylated histone H4 tails and antagonize Sir2-mediated deacetylation of histone H4K16. Furthermore, abolishing H4K16 acetylation (H4K16ac) with an H4K16R mutation promotes heterochromatin spreading, and mimicking H4K16ac by an H4K16Q mutation blocks heterochromatin spreading at IRCs. Our results thus illustrate a mechanism of establishing chromosome boundaries at specific sites through the recruitment of a factor that protects euchromatic histone modifications. They also reveal a previously unappreciated function of H4K16ac in cooperation with H3K9 methylation to regulate heterochromatin spreading.","doi":"10.1101/gad.221010.113","authors":"Wang J, Tadeo X, Hou H, Tu PG, Thompson J, Yates JR, Jia S","authors_abbrev":"Wang J et al.","pubmed_publication_date":"01 Sep 2013","pubmed_entrez_date":"2013-09-10","publication_year":"2013","canto_session_key":"72d734a43394b9a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Songtao Jia","canto_first_approved_date":"2015-04-28 13:24:14","canto_approved_date":"2025-04-11 14:03:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-19 02:32:42","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Songtao Jia","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1861.08c","SPAC3A12.13c","SPCC285.12","SPAC17A5.13","SPCC14G10.04","SPAC23C11.11","SPCC550.02c","SPAC1A6.02","SPCC4G3.18","SPAC4G9.08c","SPBC16G5.15c","SPAP8A3.06","SPBC428.08c","SPBC16E9.09c","SPAC2G11.11c","SPBC17G9.02c","SPAP4C9.02","SPAC11D3.02c","SPAC1093.05","SPAC1F3.01","SPCC1450.02","SPBC1711.17","SPAC27E2.03c","SPBC16D10.07c","SPCC11E10.07c","SPAC22A12.09c","SPCC1827.05c","SPAC4F8.12c","SPAP8A3.09c","SPBC23E6.02","SPBC4F6.06","SPAC23C4.19","SPCC1223.01","SPAC167.04","SPCC306.03c","SPAC1142.01","SPAC22G7.10","SPAC3G6.04","SPAC1071.01c","SPAC27E2.10c","SPBC1289.04c","SPAC9.03c","SPBC211.02c","SPBC800.03","SPBC15D4.14","SPBP23A10.07","SPAC1687.01","SPBP8B7.16c","SPCC364.04c","SPBC21H7.02","SPCC622.08c","SPCC622.09","SPAC1071.06","SPBC1A4.03c","SPBC12C2.06","SPBC2D10.04","SPCC14G10.02","SPCC1840.06","SPAC31A2.07c","SPAC8C9.15c","SPBC16H5.10c","SPCC63.14","SPCC330.13","SPAC20G4.08","SPAC23C4.15","SPAC4D7.04c","SPBC106.14c","SPBC31F10.11c","SPAC23H3.10","SPAP8A3.12c","SPAC1834.04","SPCC757.08","SPAC2E1P5.05","SPAC23G3.12c","SPBC1734.04","SPCC663.01c","SPAC1F3.06c","SPAC458.02c","SPAC17H9.12c","SPBC216.06c","SPBC13E7.10c","SPAC637.09","SPBC23E6.07c","SPBC2G5.02c","SPCC18.06c","SPAC26H5.09c","SPCC830.07c","SPAC24B11.11c","SPBC1289.07c","SPAC139.01c","SPAC6G10.05c","SPBC119.08","SPBC4C3.05c","SPBC646.13","SPAC6F6.17","SPBC11G11.05","SPCC16C4.09","SPCC338.13","SPAC11D3.04c","SPAC821.13c","SPCP31B10.06","SPBC146.03c","SPAC27F1.06c","SPAC5H10.03","SPAC1687.15","SPAC22E12.14c","SPAC23H4.09","SPAC2F3.03c","SPAC694.02","SPBC1604.14c","SPAC328.06","SPBC651.08c","SPBC1703.14c","SPBC18H10.04c","SPBC577.06c","SPBC646.02","SPCC645.08c","SPBC30D10.14","SPAC1250.01","SPBC11B10.10c","SPAC13F5.02c","SPAC1F5.10","SPAC25B8.12c","SPAC23C11.14","SPAC3C7.08c","SPCC1620.11","SPAC1002.04c","SPCC1753.01c","SPAC3A12.05c","SPCC622.16c","SPBC28F2.12","SPAC222.09","SPBC4B4.09","SPAC1F7.01c","SPAC31G5.11","SPBC582.09","SPBC947.02","SPAC631.02","SPCC1494.06c","SPAC12G12.07c","SPAC1071.02","SPAC12G12.05c","SPAC6F12.16c","SPBC106.20","SPCC132.01c","SPBC36B7.08c","SPAC12B10.01c","SPCC1682.02c","SPBC1289.03c","SPAC1834.03c","SPAC2G11.14","SPAC8C9.03","SPAC22E12.07","SPAC4F10.14c","SPBC26H8.03","SPAC32A11.04c","SPBC902.04","SPAC57A7.06","SPAPJ698.03c","SPBC1683.03c","SPAC1952.02","SPAC23G3.10c","SPAC30D11.03","SPBC29A10.04","SPBC713.02c","SPCC16C4.18c","SPAC21E11.06","SPAC683.02c","SPAC12G12.06c","SPAPB1A10.06c","SPBC15C4.05","SPAC23G3.09","SPCC18.05c","SPAC12G12.01c","SPAPJ696.02","SPBC4.04c","SPBC146.07","SPBC19F5.03","SPAC23G3.01","SPBC1826.01c","SPBC651.11c","SPCP25A2.03","SPCC4G3.07c","SPAC23H3.06","SPAC26A3.12c","SPAC1851.03","SPAC20H4.04","SPBC36.09","SPCC24B10.07","SPAC22F8.10c","SPCC1259.03","SPBC25H2.05","SPBC13E7.01","SPCC74.03c","SPCP1E11.06","SPAC607.03c","SPBC17D1.06","SPAC1687.22c","SPBC25H2.16c","SPBC2D10.11c","SPCC5E4.03c","SPAC1F7.02c","SPAC22F3.09c","SPAC17A5.14","SPCC188.11","SPAC3H1.12c"],"gene_count":206,"ltp_gene_count":8,"approved_date":"2015-04-28"},{"uniquename":"PMID:9374539","title":"Resistance to diverse drugs and ultraviolet light conferred by overexpression of a novel human 26 S proteasome subunit.","citation":"J Biol Chem 1997 Nov 28;272(48):30470-5","abstract":"We have investigated the usefulness of the fission yeast Schizosaccharomyces pombe as a model organism for the discovery of novel modes of drug resistance in human cells. In fission yeast, overexpression of the essential pad1(+) gene confers pleiotropic drug resistance through a pathway involving an AP-1 transcription factor encoded by pap1(+). We have identified POH1, a human pad1 homologue that can substitute fully for pad1(+) and induce AP-1-dependent drug resistance in fission yeast. POH1 also confers P-glycoprotein-independent resistance to taxol (paclitaxel), doxorubicin, 7-hydroxystaurosporine, and ultraviolet light when transiently overexpressed in mammalian cells. Poh1 is a previously unidentified component of the human 26 S proteasome, a multiprotein complex that degrades proteins targeted for destruction by the ubiquitin pathway. Hence, Poh1 is part of a conserved mechanism that determines cellular susceptibility to cytotoxic agents, perhaps by influencing the ubiquitin-dependent proteolysis of transcription factors.","authors":"Spataro V, Toda T, Craig R, Seeger M, Dubiel W, Harris AL, Norbury C","authors_abbrev":"Spataro V et al.","pubmed_publication_date":"28 Nov 1997","pubmed_entrez_date":"1997-12-31","publication_year":"1997","canto_session_key":"0a5874904c182164","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-03-20 12:00:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-03-20 12:00:36","canto_added_date":"2012-02-24 05:53:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-03-20"},{"uniquename":"PMID:7009322","title":"Intracellular population genetics: evidence for random drift of mitochondrial allele frequencies in Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Genetics 1980 Sep;96(1):237-62","abstract":"We report evidence for random drift of mitochondrial allele frequencies in zygote clones of Saccharomyces cerevisiae and Schizosaccharomyces pombe. Monofactorial and bifactorial crosses were done, using strains resistant or sensitive to erythromycin (alleles Er, Es), oligomycin (Or, Os), or diuron (Dr, Ds). The frequencies of resistant and sensitive cells (and thus the frequencies of the resistant and sensitive alleles) were determined for each of a number of clones of diploid cells arising from individual zygotes. Allele frequencies were extremely variable among these zygote clones; some clones were \"uniparental,\" with mitochondrial alleles from only one parent present. These observations suggest random drift of the allele frequencies in the population of mitochondrial genes within an individual zygote and its diploid progeny. Drift would cease when all the cells in a clone become homoplasmic, due to segregation of the mitochondrial genomes during vegetative cell divisions. To test this, we delayed cell division (and hence segregation) for varying times by starving zygotes in order to give drift more time to operate. As predicted, delaying cell division resulted in an increase in the variance of allele frequencies among the zygote clones and an increase in the proportion of uniparental zygote clones. The changes in form of the allele frequency distributions resembled those seen during random drift in finite Mendelian populations. In bifactorial crosses, genotypes as well as individual alleles were fixed or lost in some zygote clones. However, the mean recombination frequency for a large number of clones did not increase when cell division was delayed. Several possible molecular mechanisms for intracellular random drift are discussed.","authors":"Thrailkill KM, Birky CW","authors_abbrev":"Thrailkill KM et al.","pubmed_publication_date":"Sep 1980","pubmed_entrez_date":"1980-09-01","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23333317","title":"Removal of centrosomal PP1 by NIMA kinase unlocks the MPF feedback loop to promote mitotic commitment in S. pombe.","citation":"Curr Biol 2013 Feb 04;23(3):213-22","abstract":"Activation of the Cdk1/cyclin B complex, also known as mitosis-promoting factor (MPF), drives commitment to mitosis. Interphase MPF is inhibited through phosphorylation of Cdk1 by Wee1-related kinases. Because Cdc25 phosphatases remove this phosphate, Cdc25 activity is an essential part of the switch that drives cells into mitosis. The generation of a critical \"trigger\" of active MPF promotes a positive feedback loop that employs Polo kinase to boost Cdc25 activity and inhibit Wee1, thereby ensuring that mitotic commitment is a bistable switch. Mutations in the spindle pole body (SPB) component Cut12 suppress otherwise lethal deficiencies in Cdc25.\nCut12 harbors a bipartite protein phosphatase 1 (PP1) docking domain. Mutation of either element alone suppressed the temperature-dependent lethality of cdc25.22, whereas simultaneous ablation of both allowed cells to divide in the complete absence of Cdc25. Late G2 phase phosphorylation between the two elements by MPF and the NIMA kinase Fin1 blocked PP1(Dis2) recruitment, thereby promoting recruitment of Polo to Cut12 and the SPB and elevating global Polo kinase activity throughout the cell.\nPP1 recruitment to Cut12 sets a threshold for Polo's feedback-loop activity that locks the cell in interphase until Cdc25 pushes MPF activity through this barrier to initiate mitosis. We propose that events on the SPB (and, by inference, the centrosome) integrate inputs from diverse signaling networks to generate a coherent decision to divide that is appropriate for the particular environmental context of each cell. PP1 recruitment sets one or more critical thresholds for single or multiple local events within this switch.","doi":"10.1016/j.cub.2012.12.039","authors":"Grallert A, Chan KY, Alonso-Nuñez ML, Madrid M, Biswas A, Alvarez-Tabarés I, Connolly Y, Tanaka K, Robertson A, Ortiz JM, Smith DL, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"04 Feb 2013","pubmed_entrez_date":"2013-01-22","publication_year":"2013","canto_session_key":"acd1a2d2ddcf29cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2020-10-02 10:54:21","canto_approved_date":"2024-04-04 09:12:23","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-09-01 11:16:38","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":83,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPAC19E9.02","SPCC18B5.03","SPAC24H6.05","SPBC11B10.09","SPAC23C11.16","SPBC776.02c","SPBC649.05"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2020-10-02"},{"uniquename":"EMBL:SPUBL1","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22366461","title":"Brc1-dependent recovery from replication stress.","citation":"J Cell Sci 2012 Jun 01;125(Pt 11):2753-64","abstract":"BRCT-containing protein 1 (Brc1) is a multi-BRCT (BRCA1 carboxyl terminus) domain protein in Schizosaccharomyces pombe that is required for resistance to chronic replicative stress, but whether this reflects a repair or replication defect is unknown and the subject of this study. We show that brc1Δ cells are significantly delayed in recovery from replication pausing, though this does not activate a DNA damage checkpoint. DNA repair and recombination protein Rad52 is a homologous recombination protein that loads the Rad51 recombinase at resected double-stranded DNA (dsDNA) breaks and is also recruited to stalled replication forks, where it may stabilize structures through its strand annealing activity. Rad52 is required for the viability of brc1Δ cells, and brc1Δ cells accumulate Rad52 foci late in S phase that are potentiated by replication stress. However, these foci contain the single-stranded DNA (ssDNA) binding protein RPA, but not Rad51 or γH2A. Further, these foci are not associated with increased recombination between repeated sequences, or increased post-replication repair. Thus, these Rad52 foci do not represent sites of recombination. Following the initiation of DNA replication, the induction of these foci by replication stress is suppressed by defects in origin recognition complex (ORC) function, which is accompanied by loss of viability and severe mitotic defects. This suggests that cells lacking Brc1 undergo an ORC-dependent rescue of replication stress, presumably through the firing of dormant origins, and this generates RPA-coated ssDNA and recruits Rad52. However, as Rad51 is not recruited, and the checkpoint effector kinase Chk1 is not activated, these structures must not contain the unprotected primer ends found at sites of DNA damage that are required for recombination and checkpoint activation.","doi":"10.1242/jcs.103119","authors":"Bass KL, Murray JM, O'Connell MJ","authors_abbrev":"Bass KL et al.","pubmed_publication_date":"01 Jun 2012","pubmed_entrez_date":"2012-02-28","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4H3.05","SPCC5E4.06","SPAC30D11.10","SPAC644.14c","SPBC29A10.15","SPCC1259.13","SPBC582.05c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"EMBL:AU007158","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6754553","title":"Resistance of Schizosaccharomyces pombe to mechanical strain caused by mixing in continuous culture.","citation":"Folia Microbiol (Praha) 1982;27(5):363-4","abstract":"","authors":"Vraná D, Kalasová M","authors_abbrev":"Vraná D et al.","pubmed_publication_date":"1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31509190","title":"Modulation of fatty acid synthase by ATR checkpoint kinase Rad3.","citation":"J Mol Cell Biol 2019 Dec 19;11(12):1098-1100","abstract":"","doi":"10.1093/jmcb/mjz096","authors":"Qiu S, Liu S, Zaoti ZF, Wang X, Cai G","authors_abbrev":"Qiu S et al.","pubmed_publication_date":"19 Dec 2019","pubmed_entrez_date":"2019-09-12","publication_year":"2019","canto_session_key":"9d4969c256ad05d7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-07-19 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12930742","title":"Rho3p regulates cell separation by modulating exocyst function in Schizosaccharomyces pombe.","citation":"Genetics 2003 Aug;164(4):1323-31","abstract":"Cytokinesis is the final stage of the cell division cycle in which the mother cell is physically divided into two daughters. In recent years the fission yeast Schizosaccharomyces pombe has emerged as an attractive model organism for the study of cytokinesis, since it divides using an actomyosin ring whose constriction is coordinated with the centripetal deposition of new membranes and a division septum. The final step of cytokinesis in S. pombe requires the digestion of the primary septum to liberate two daughters. We have previously shown that the multiprotein exocyst complex is essential for this process. Here we report the isolation of rho3(+), encoding a Rho family GTPase, as a high-copy suppressor of an exocyst mutant, sec8-1. Overproduction of Rho3p also suppressed the temperature-sensitive growth phenotype observed in cells lacking Exo70p, another conserved component of the S. pombe exocyst complex. Cells deleted for rho3 arrest at higher growth temperatures with two or more nuclei and uncleaved division septa between pairs of nuclei. rho3Delta cells accumulate approximately 100-nm vesicle-like structures. These phenotypes are all similar to those observed in exocyst component mutants, consistent with a role for Rho3p in modulation of exocyst function. Taken together, our results suggest the possibility that S. pombe Rho3p regulates cell separation by modulation of exocyst function.","authors":"Wang H, Tang X, Balasubramanian MK","authors_abbrev":"Wang H et al.","pubmed_publication_date":"Aug 2003","pubmed_entrez_date":"2003-08-22","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC970.09","SPBC106.20","SPAC23C4.08"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:29149592","title":"Dynamics under the Telomeric Bridge.","citation":"Mol Cell 2017 Nov 16;68(4):643-644","abstract":"In this issue of Molecular Cell, Kim et al. (2017) have studied the structure and organization of the shelterin protein complex protecting telomeres in Schizosaccharomyces pombe and humans and discovered an allosteric structural transition that drives the formation of the shelterin complex and participates in telomere length regulation.","doi":"10.1016/j.molcel.2017.11.005","authors":"Pisano S, Gilson E, Giraud-Panis MJ","authors_abbrev":"Pisano S et al.","pubmed_publication_date":"16 Nov 2017","pubmed_entrez_date":"2017-11-18","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-11-19 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36951094","title":"Fission yeast Swi2 designates cell-type specific donor and stimulates Rad51-driven strand exchange for mating-type switching.","citation":"Nucleic Acids Res 2023 May 08;51(8):3869-3887","abstract":"A haploid of the fission yeast Schizosaccharomyces pombe expresses either the P or M mating-type, determined by the active, euchromatic, mat1 cassette. Mating-type is switched by Rad51-driven gene conversion of mat1 using a heterochromatic donor cassette, mat2-P or mat3-M. The Swi2-Swi5 complex, a mating-type switching factor, is central to this process by designating a preferred donor in a cell-type-specific manner. Swi2-Swi5 selectively enables one of two cis-acting recombination enhancers, SRE2 adjacent to mat2-P or SRE3 adjacent to mat3-M. Here, we identified two functionally important motifs in Swi2, a Swi6 (HP1 homolog)-binding site and two DNA-binding AT-hooks. Genetic analysis demonstrated that the AT-hooks were required for Swi2 localization at SRE3 to select the mat3-M donor in P cells, while the Swi6-binding site was required for Swi2 localization at SRE2 to select mat2-P in M cells. In addition, the Swi2-Swi5 complex promoted Rad51-driven strand exchange in vitro. Taken together, our results show how the Swi2-Swi5 complex would localize to recombination enhancers through a cell-type specific binding mechanism and stimulate Rad51-driven gene conversion at the localization site.","doi":"10.1093/nar/gkad204","authors":"Maki T, Thon G, Iwasaki H","authors_abbrev":"Maki T et al.","pubmed_publication_date":"08 May 2023","pubmed_entrez_date":"2023-03-23","publication_year":"2023","canto_session_key":"124f1f372bfd6615","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroshi Iwasaki","canto_first_approved_date":"2024-05-07 16:31:03","canto_approved_date":"2024-06-21 10:58:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-24 12:29:19","canto_added_date":"2023-03-24 01:15:05","annotation_curators":[{"name":"Hiroshi Iwasaki","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":29,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.03","SPAC664.01c","SPAC1142.03c","SPCC306.04c","SPAC15A10.03c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2024-05-07"},{"uniquename":"PMID:19143645","title":"TOR signalling regulates mitotic commitment through stress-activated MAPK and Polo kinase in response to nutrient stress.","citation":"Biochem Soc Trans 2009 Feb;37(Pt 1):273-7","abstract":"Cell growth and cell division are coupled to control cell size and this co-ordination is often modulated by the availability of nutrients. In many eukaryotes, TOR (target of rapamycin) signalling is involved in coupling nutrient sensing to cell growth and division controls. Nutrient stress inhibits TOR signalling to advance the timing of cell division and thus leads to continued cell division at reduced cell size. Most changes in the environment stimulate stress-activated MAPK (mitogen-activated protein kinase) signalling pathways. Several MAPKs also have a general role in the control of mitotic onset and cell division. In the present paper, I discuss the interplay between two major signalling pathways, the TOR and the stress MAPK signalling pathways, in controlling mitotic commitment, with the main focus being on fission yeast (Schizosaccharomyces pombe).","doi":"10.1042/BST0370273","authors":"Petersen J","authors_abbrev":"Petersen J","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2009-01-16","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU014250","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17565698","title":"Cdt1 degradation to prevent DNA re-replication: conserved and non-conserved pathways.","citation":"Cell Div 2007 Jun 12;2:18","abstract":"In eukaryotes, DNA replication is strictly regulated so that it occurs only once per cell cycle. The mechanisms that prevent excessive DNA replication are focused on preventing replication origins from being reused within the same cell cycle. This regulation involves the temporal separation of the formation of the pre-replicative complex (pre-RC) from the initiation of DNA replication. The replication licensing factors Cdt1 and Cdc6 recruit the presumptive replicative helicase, the Mcm2-7 complex, to replication origins in late M or G1 phase to form pre-RCs. In fission yeast and metazoa, the Cdt1 licensing factor is degraded at the start of S phase by ubiquitin-mediated proteolysis to prevent the reassembly of pre-RCs. In humans, two E3 complexes, CUL4-DDB1CDT2 and SCFSkp2, are redundantly required for Cdt1 degradation. The two E3 complexes use distinct mechanisms to target Cdt1 ubiquitination. Current data suggests that CUL4-DDB1CDT2-mediated degradation of Cdt1 is S-phase specific, while SCFSkp2-mediated Cdt1 degradation occurs throughout the cell cycle. The degradation of Cdt1 by the CUL4-DDB1CDT2 E3 complex is an evolutionarily ancient pathway that is active in fungi and metazoa. In contrast, SCFSkp2-mediated Cdt1 degradation appears to have arisen relatively recently. A role for Skp2 in Cdt1 degradation has only been demonstrated in humans, and the pathway is not conserved in yeast, invertebrates, or even among other vertebrates.","authors":"Kim Y, Kipreos ET","authors_abbrev":"Kim Y et al.","pubmed_publication_date":"12 Jun 2007","pubmed_entrez_date":"2007-06-15","publication_year":"2007","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33125111","title":"Loss of FZO1 gene results in changes of cell dynamics in fission yeast.","citation":"Int J Mol Med 2020 Dec;46(6):2194-2206","abstract":"Mitochondrial fission and fusion dynamics are critical cellular processes, and abnormalities in these processes are associated with severe human disorders, such as Beckwith‑Wiedemann syndrome, neurodegenerative diseases, Charcot‑Marie‑Tooth disease type 6, multiple symmetric lipomatosis and microcephaly. Fuzzy onions protein 1 (Fzo1p) regulates mitochondrial outer membrane fusion. In the present study, Schizosaccharomyces pombe (S. pombe) was used to explore the effect of FZO1 gene deletion on cell dynamics in mitosis. The mitochondrial morphology results showed that the mitochondria appeared to be fragmented and tubular in wild‑type cells; however, they were observed to accumulate in fzo1Δ cells. The FZO1 gene deletion was demonstrated to result in slow proliferation, sporogenesis defects, increased microtubule (MT) number and actin contraction defects in S. pombe. The FZO1 gene deletion also affected the rate of spindle elongation and phase time at the metaphase and anaphase, as well as spindle MT organization. Live‑cell imaging was performed on mutant strains to observe three distinct kinetochore behaviors (normal, lagging and mis‑segregation), as well as abnormal spindle breakage. The FZO1 gene deletion resulted in coenzyme and intermediate metabolite abnormalities as determined via metabolomics analysis. It was concluded that the loss of FZO1 gene resulted in deficiencies in mitochondrial dynamics, which may result in deficiencies in spindle maintenance, chromosome segregation, spindle breakage, actin contraction, and coenzyme and intermediate metabolite levels.","doi":"10.3892/ijmm.2020.4752","authors":"Yuan R, Ding X, Tan X, Hou Y","authors_abbrev":"Yuan R et al.","pubmed_publication_date":"Dec 2020","pubmed_entrez_date":"2020-10-30","publication_year":"2020","canto_session_key":"f8a1d3758cd90a28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-03-05 18:49:17","canto_approved_date":"2025-06-09 13:17:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-05 18:48:41","canto_added_date":"2020-11-01 01:15:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1706.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-03-05"},{"uniquename":"PMID:9599405","title":"Extracellular degradation of agonists as an adaptive mechanism.","citation":"Semin Cell Dev Biol 1998 Apr;9(2):111-8","abstract":"Many cellular responses are initiated by the binding of an extracellular ligand to receptors at the cell surface. The removal of these ligands, or agonists, would therefore be expected to contribute to the process by which cells recover from stimulation. While dilution in the extracellular medium reduces the concentration of most agonists, many cells have developed specific mechanisms for removing particular ligands. One of the more effective mechanisms is to degrade the extracellular agonist and here we review the production and action of the enzymes responsible for the degradation of a number of these agonists.","authors":"Ladds G, Hughes M, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-05-26","publication_year":"1998","canto_session_key":"4f75e98b55c64601","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-03-24 15:40:56","canto_approved_date":"2025-05-28 13:11:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-16 17:31:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.01","SPAC1296.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-03-24"},{"uniquename":"PMID:28821619","title":"Dsc E3 ligase localization to the Golgi requires the ATPase Cdc48 and cofactor Ufd1 for activation of sterol regulatory element-binding protein in fission yeast.","citation":"J Biol Chem 2017 Sep 29;292(39):16333-16350","abstract":"Sterol regulatory element-binding proteins (SREBPs) in the fission yeast  Schizosaccharomyces pombe  regulate lipid homeostasis and the hypoxic response under conditions of low sterol or oxygen availability. SREBPs are cleaved in the Golgi through the combined action of the Dsc E3 ligase complex, the rhomboid protease Rbd2, and the essential ATPases associated with diverse cellular activities (AAA + ) ATPase Cdc48. The soluble SREBP N-terminal transcription factor domain is then released into the cytosol to enter the nucleus and regulate gene expression. Previously, we reported that Cdc48 binding to Rbd2 is required for Rbd2-mediated SREBP cleavage. Here, using affinity chromatography and mass spectrometry experiments, we identified Cdc48-binding proteins in  S. pombe , generating a list of many previously unknown potential Cdc48-binding partners. We show that the established Cdc48 cofactor Ufd1 is required for SREBP cleavage but does not interact with the Cdc48-Rbd2 complex. Cdc48-Ufd1 is instead required at a step prior to Rbd2 function, during Golgi localization of the Dsc E3 ligase complex. Together, these findings demonstrate that two distinct Cdc48 complexes, Cdc48-Ufd1 and Cdc48-Rbd2, are required for SREBP activation and low-oxygen adaptation in  S. pombe .","doi":"10.1074/jbc.M117.802025","authors":"Burr R, Ribbens D, Raychaudhuri S, Stewart EV, Ho J, Espenshade PJ","authors_abbrev":"Burr R et al.","pubmed_publication_date":"29 Sep 2017","pubmed_entrez_date":"2017-08-20","publication_year":"2017","canto_session_key":"bea1c1e13005750d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2017-10-12 14:29:45","canto_approved_date":"2024-07-01 11:36:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-22 18:07:59","canto_added_date":"2017-08-21 00:15:15","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Peter Espenshade","community_curator":true,"annotation_count":140,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F3.15","SPAC25G10.05c","SPBC947.10","SPBC887.05c","SPBC29A10.08","SPCC285.11","SPAC1486.02c","SPBC106.03","SPAC1565.08","SPAC343.09","SPCC790.03","SPBC354.13","SPBC16A3.09c","SPBP4H10.07","SPCC1795.11","SPAC4F8.07c","SPAC4D7.11","SPAP32A8.03c","SPAC57A7.08","SPAC20H4.02","SPAC1B3.03c","SPAC18B11.03c","SPCC1020.01c","SPCC1442.07c","SPAC29A4.06c","SPBC17D11.02c","SPAC637.07","SPAC4A8.12c","SPBC1105.07c","SPBC216.03","SPAC19B12.11c","SPAC24C9.14","SPBC19C2.09","SPAC6G10.08","SPAC13G7.02c","SPBC365.06","SPBC21C3.11","SPAC2C4.15c","SPBC354.07c","SPCC4B3.01","SPBC15D4.11c","SPBC1711.10c","SPAC26A3.16","SPCC1827.04","SPCC306.08c","SPBC21B10.05c","SPBC3B9.15c","SPAC1A6.04c","SPCC1281.07c","SPBC354.05c","SPAC22E12.06c","SPAC343.12","SPAC17C9.11c","SPAC6B12.13","SPBC18H10.04c","SPCC4G3.12c","SPAC110.03","SPAC26H5.09c","SPAC2C4.17c"],"gene_count":59,"ltp_gene_count":57,"approved_date":"2017-10-12"},{"uniquename":"PMID:20098417","title":"DNA zip codes control an ancient mechanism for gene targeting to the nuclear periphery.","citation":"Nat Cell Biol 2010 Feb;12(2):111-8","abstract":"Many genes in Saccharomyces cerevisiae are recruited to the nuclear periphery after transcriptional activation. We have identified two gene recruitment sequences (GRS I and II) from the promoter of the INO1 gene that target the gene to the nuclear periphery. These GRSs function as DNA zip codes and are sufficient to target a nucleoplasmic locus to the nuclear periphery. Targeting requires components of the nuclear pore complex (NPC) and a GRS is sufficient to confer a physical interaction with the NPC. GRS I elements are enriched in promoters of genes that interact with the NPC, and genes that are induced by protein folding stress. Full transcriptional activation of INO1 and another GRS-containing gene requires GRS-mediated targeting of the promoter to the nuclear periphery. Finally, GRS I also functions as a DNA zip code in Schizosaccharomyces pombe, suggesting that this mechanism of targeting to the nuclear periphery has been conserved over approximately one billion years of evolution.","doi":"10.1038/ncb2011","authors":"Ahmed S, Brickner DG, Light WH, Cajigas I, McDonough M, Froyshteter AB, Volpe T, Brickner JH","authors_abbrev":"Ahmed S et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2010-01-26","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12424244","title":"Telomeric DNA ends are essential for the localization of Ku at telomeres in fission yeast.","citation":"J Biol Chem 2003 Jan 17;278(3):1924-31","abstract":"The Ku70-Ku80 heterodimer is a conserved protein complex essential for the non-homologous end-joining pathway. Ku proteins are also involved in telomere maintenance, although their precise roles remain to be elucidated. In fission yeast, pku70(+), the gene encoding the Ku70 homologue, has been reported. Here we report the identification and characterization of pku80(+), the gene encoding Ku80. Both pku70(+) and pku80(+) are essential for efficient non-homologous end-joining. We also found that the pku70 and pku80 mutants are sensitive to methyl methanesulfonate and hydroxyurea, suggesting their roles in the S phase. The pku80 mutant shows telomere shortening and tandem amplification of a subtelomeric sequence but no defects in the telomere position effect, as was previously reported for the pku70 mutant. By using the chromatin immunoprecipitation assay, we demonstrated that Pku70 and Pku80 physically interact with telomeric repeats and subtelomeric sequences. Interestingly, this telomere association of Pku proteins is independent of Taz1, a telomeric DNA-binding protein. We also showed that the Pku proteins do not associate with ectopically integrated telomeric repeats in the internal region of circular chromosomes. These results indicate that the physical end of DNA is necessary for the localization of Pku80 at telomeres.","authors":"Miyoshi T, Sadaie M, Kanoh J, Ishikawa F","authors_abbrev":"Miyoshi T et al.","pubmed_publication_date":"17 Jan 2003","pubmed_entrez_date":"2002-11-09","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC543.03c","SPCC126.02c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:39705284","title":"Proteomic and phosphoproteomic analyses reveal that TORC1 is reactivated by pheromone signaling during sexual reproduction in fission yeast.","citation":"PLoS Biol 2024 Dec 20;22(12):e3002963","abstract":"Starvation, which is associated with inactivation of the growth-promoting TOR complex 1 (TORC1), is a strong environmental signal for cell differentiation. In the fission yeast Schizosaccharomyces pombe, nitrogen starvation has distinct physiological consequences depending on the presence of mating partners. In their absence, cells enter quiescence, and TORC1 inactivation prolongs their life. In presence of compatible mates, TORC1 inactivation is essential for sexual differentiation. Gametes engage in paracrine pheromone signaling, grow towards each other, fuse to form the diploid zygote, and form resistant, haploid spore progenies. To understand the signaling changes in the proteome and phospho-proteome during sexual reproduction, we developed cell synchronization strategies and present (phospho-)proteomic data sets that dissect pheromone from starvation signals over the sexual differentiation and cell-cell fusion processes. Unexpectedly, these data sets reveal phosphorylation of ribosomal protein S6 during sexual development, which we establish requires TORC1 activity. We demonstrate that TORC1 is re-activated by pheromone signaling, in a manner that does not require autophagy. Mutants with low TORC1 re-activation exhibit compromised mating and poorly viable spores. Thus, while inactivated to initiate the mating process, TORC1 is reactivated by pheromone signaling in starved cells to support sexual reproduction.","doi":"10.1371/journal.pbio.3002963","authors":"Bérard M, Merlini L, Martin SG","authors_abbrev":"Bérard M et al.","pubmed_publication_date":"20 Dec 2024","pubmed_entrez_date":"2024-12-20","publication_year":"2024","canto_session_key":"5cba71fc62d1cc66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2025-04-22 10:49:53","canto_approved_date":"2025-04-22 10:49:53","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-01 16:41:14","canto_added_date":"2024-12-21 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":4,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":27,"orcid":"0000-0002-5317-2557","file_type":null,"file_name":null}],"file_curator_name":"Pascal Carme","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":3483,"orcid":"0009-0003-9059-1333","file_type":"protein_modification","file_name":"PMID_39705284_modifications.tsv"},{"name":"Pascal 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of Schizosaccharomyces pombe genes encoding the U1, U2, U3 and U4 snRNAs.","citation":"Gene 1989 Sep 30;81(2):227-35","abstract":"Schizosaccharomyces pombe contains a group of five relatively abundant small nuclear RNAs (snRNAs) which are immunoprecipitated by human autoimmune antibodies of Sm serotype. The S. pombe RNAs hybridise to probes specific for human U1, U2, U4, U5 and U6 and in each case are similar in size to the human species. A further group of snRNAs from S. pombe are precipitated by antibodies against U3 containing ribonucleoprotein; the most abundant of these species hybridises to a probe specific for human U3. We have cloned the genes encoding U1, U2, U3 and U4 from S. pombe, together with that encoding another abundant snRNA, previously designated SPU43. U2 and U4 are encoded by single-copy genes, while two genes encode U3. The latter are not clustered, since a chromosomal Southern transfer shows them to lie on different chromosomes.","authors":"Dandekar T, Tollervey D","authors_abbrev":"Dandekar T et al.","pubmed_publication_date":"30 Sep 1989","pubmed_entrez_date":"1989-09-30","publication_year":"1989","canto_session_key":"847bdd09379d5d36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-06-18 18:06:01","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-18 16:47:36","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.03","SPSNRNA.04","SPSNRNA.07","SPSNRNA.01","SPSNRNA.02"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-06-18"},{"uniquename":"PMID:8062838","title":"Three ARS elements contribute to the ura4 replication origin region in the fission yeast, Schizosaccharomyces pombe.","citation":"EMBO J 1994 Aug 01;13(15):3638-47","abstract":"The ura4 replication origin region, which is located near the ura4 gene on chromosome III of the fission yeast, Schizosaccharomyces pombe, contains multiple initiation sites. We have used 2D gel electrophoretic replicon mapping methods to study the distribution of these initiation sites, and have found that they are concentrated near three ARS elements (stretches of DNA which permit autonomous plasmid replication). To determine the roles of these ARS elements in the function of the ura4 origin region, we deleted either one or two of them from the chromosome and then assessed the consequences of the deletions by 2D gel electrophoresis. The results suggest that each of the three ARS elements is responsible for the initiation events in its vicinity and that the ARS elements interfere with each other in a hierarchical fashion. It is possible that the large initiation zones of animal cells are similarly composed of multiple mutually interfering origins.","authors":"Dubey DD, Zhu J, Carlson DL, Sharma K, Huberman JA","authors_abbrev":"Dubey DD et al.","pubmed_publication_date":"01 Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_session_key":"23ae9907624fcb02","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 14:59:59","canto_approved_date":"2019-01-07 14:59:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 14:59:53","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:19299465","title":"S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p.","citation":"J Cell Sci 2009 Apr 15;122(Pt 8):1163-73","abstract":"Batten disease is characterised by lysosomal dysfunction. The most common type of the disease is caused by mutations in the membrane protein CLN3, whose function is unknown. We show that the fission yeast orthologue Btn1p, previously implicated in vacuole function, is required for correct sorting of the vacuole hydrolase carboxypeptidase Y (Cpy1p). This is, in part, due to a defect in trafficking of Vps10p, the sorting receptor for Cpy1p, from the Golgi to the trans-Golgi network in btn1Delta cells. Our data also implicate btn1 in other Vps10-independent Cpy1-sorting pathways. Furthermore, btn1 affects the number, intracellular location and structure of Golgi compartments. We show that the prevacuole location of Btn1p is at the Golgi, because Btn1p colocalises predominantly with the Golgi marker Gms1p in compartments that are sensitive to Brefeldin A. Btn1p function might be linked to that of Vps34p, a phosphatidylinositol 3-kinase, because Btn1p acts as a multicopy suppressor of the severe Cpy1p vacuole protein-sorting defect of vps34Delta cells. Together, these results indicate an important role for Btn1p in the Golgi complex, which affects Golgi homeostasis and vacuole protein sorting. We propose a similar role for CLN3 in mammalian cells.","doi":"10.1242/jcs.038323","authors":"Codlin S, Mole SE","authors_abbrev":"Codlin S et al.","pubmed_publication_date":"15 Apr 2009","pubmed_entrez_date":"2009-03-21","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7399372","title":"Karyokinesis in growing and reverting protoplasts of Schizosaccharomyces pombe.","citation":"Folia Microbiol (Praha) 1980;25(3):219-27","abstract":"","authors":"Havelková M, Krípalová J","authors_abbrev":"Havelková M et al.","pubmed_publication_date":"1980","pubmed_entrez_date":"1980-01-01","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30072440","title":"Regulation of global translation during the cell cycle.","citation":"J Cell Sci 2018 Sep 03;131(17)","abstract":"It is generally accepted that global translation varies during the cell cycle and is low during mitosis. However, addressing this issue is challenging because it involves cell synchronization, which evokes stress responses that, in turn, affect translation rates. Here, we have used two approaches to measure global translation rates in different cell-cycle phases. First, synchrony in different cell-cycle phases was obtained involving the same stress, by using temperature-sensitive mutants. Second, translation and DNA content were measured by flow cytometry in exponentially growing, single cells. We found no major variation in global translation rates through the cell cycle in either fission yeast or mammalian cells. We also measured phosphorylation of eukaryotic initiation factor-2α, an event that is thought to downregulate global translation in mitosis. In contrast with the prevailing view, eIF2α phosphorylation correlated poorly with downregulation of global translation and ectopically induced eIF2α phosphorylation inhibited global translation only at high levels.","doi":"10.1242/jcs.220327","authors":"Stonyte V, Boye E, Grallert B","authors_abbrev":"Stonyte V et al.","pubmed_publication_date":"03 Sep 2018","pubmed_entrez_date":"2018-08-04","publication_year":"2018","canto_session_key":"ba7a09cb7674fda6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-10-05 12:49:43","canto_approved_date":"2018-10-05 12:49:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-09-06 14:25:19","canto_added_date":"2018-08-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G9.09c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2018-10-05"},{"uniquename":"PMID:20042603","title":"Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin.","citation":"J Biol Chem 2010 Feb 26;285(9):6835-47","abstract":"Toxoplasma gondii is a protozoan parasite belonging to the phylum Apicomplexa. Parasites in this phylum utilize a unique process of motility termed gliding, which is dependent on parasite actin filaments. Surprisingly, 98% of parasite actin is maintained as G-actin, suggesting that filaments are rapidly assembled and turned over. Little is known about the regulated disassembly of filaments in the Apicomplexa. In higher eukaryotes, the related actin depolymerizing factor (ADF) and cofilin proteins are essential regulators of actin filament turnover. ADF is one of the few actin-binding proteins conserved in apicomplexan parasites. In this study we examined the mechanism by which T. gondii ADF (TgADF) regulates actin filament turnover. Unlike other members of the ADF/cofilin (AC) family, apicomplexan ADFs lack key F-actin binding sites. Surprisingly, this promotes their enhanced disassembly of actin filaments. Restoration of the C-terminal F-actin binding site to TgADF stabilized its interaction with filaments but reduced its net filament disassembly activity. Analysis of severing activity revealed that TgADF is a weak severing protein, requiring much higher concentrations than typical AC proteins. Investigation of TgADF interaction with T. gondii actin (TgACT) revealed that TgADF disassembled short TgACT oligomers. Kinetic and steady-state polymerization assays demonstrated that TgADF has strong monomer-sequestering activity, inhibiting TgACT polymerization at very low concentrations. Collectively these data indicate that TgADF promoted the efficient turnover of actin filaments via weak severing of filaments and strong sequestering of monomers. This suggests a dual role for TgADF in maintaining high G-actin concentrations and effecting rapid filament turnover.","doi":"10.1074/jbc.M109.068155","authors":"Mehta S, Sibley LD","authors_abbrev":"Mehta S et al.","pubmed_publication_date":"26 Feb 2010","pubmed_entrez_date":"2010-01-01","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G4.06c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:12868054","title":"Characterization of vps33+, a gene required for vacuolar biogenesis and protein sorting in Schizosaccharomyces pombe.","citation":"Yeast 2003 Jul 30;20(10):845-55","abstract":"From the fission yeast Schizosaccharomyces pombe we have identified and deleted vps33, a gene encoding a homologue of VPS33, which is required for vacuolar biogenesis in S. cerevisiae cells. When the vps33(+) gene is disrupted, Sz. pombe strains are temperature-sensitive for growth and contain numerous small vesicular structures stained with FM4-64 in the cells. Deletion of the Sz. pombe vps33(+) gene results in pleiotropic phenotypes consistent with the absence of normal vacuoles, including missorting of vacuolar carboxypeptidase Y, various ion- and drug-sensitivities, and sporulation defects. These results are consistent with Vps33p being necessary for the morphogenesis of vacuoles and subsequent expression of vacuolar functions in Sz. pombe cells.","authors":"Iwaki T, Osawa F, Onishi M, Koga T, Fujita Y, Hosomi A, Tanaka N, Fukui Y, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"30 Jul 2003","pubmed_entrez_date":"2003-07-18","publication_year":"2003","canto_session_key":"bae1d88d8aeee742","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-03-17 19:25:43","canto_approved_date":"2022-11-19 19:28:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-17 19:16:28","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.09c","SPBC1703.15c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2020-03-17"},{"uniquename":"PMID:24589736","title":"Bidirectional motility of the fission yeast kinesin-5, Cut7.","citation":"Biochem Biophys Res Commun 2014 Mar 28;446(1):231-4","abstract":"Kinesin-5 is a homotetrameric motor with its motor domain at the N-terminus. Kinesin-5 crosslinks microtubules and functions in separating spindle poles during mitosis. In this study, the motile properties of Cut7, fission yeast kinesin-5, were examined for the first time. In in vitro motility assays, full-length Cut7 moved toward minus-end of microtubules, but the N-terminal half of Cut7 moved toward the opposite direction. Furthermore, additional truncated constructs lacking the N-terminal or C-terminal regions, but still contained the motor domain, did not switch the motile direction. These indicated that Cut7 was a bidirectional motor, and microtubule binding regions at the N-terminus and C-terminus were not involved in its directionality.","doi":"10.1016/j.bbrc.2014.02.106","authors":"Edamatsu M","authors_abbrev":"Edamatsu M","pubmed_publication_date":"28 Mar 2014","pubmed_entrez_date":"2014-03-05","publication_year":"2014","canto_session_key":"7dcf57548087f228","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25G10.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35164548","title":"Genome-Wide Characterization of SARS-CoV-2 Cytopathogenic Proteins in the Search of Antiviral Targets.","citation":"mBio 2021 Feb 22;13(1):e0016922","abstract":"Therapeutic inhibition of critical viral functions is important for curtailing coronavirus disease 2019 (COVID-19). We sought to identify antiviral targets through the genome-wide characterization of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) proteins that are crucial for viral pathogenesis and that cause harmful cytopathogenic effects. All 29 viral proteins were tested in a fission yeast cell-based system using inducible gene expression. Twelve proteins, including eight nonstructural proteins (NSP1, NSP3, NSP4, NSP5, NSP6, NSP13, NSP14, and NSP15) and four accessory proteins (ORF3a, ORF6, ORF7a, and ORF7b), were identified that altered cellular proliferation and integrity and induced cell death. Cell death correlated with the activation of cellular oxidative stress. Of the 12 proteins, ORF3a was chosen for further study in mammalian cells because it plays an important role in viral pathogenesis and its activities are linked to lung tissue damage and a cytokine storm. In human pulmonary and kidney epithelial cells, ORF3a induced cellular oxidative stress associated with apoptosis and necrosis and caused activation of proinflammatory response with production of the cytokines tumor necrosis factor alpha (TNF-α), interleukin-6 (IL-6), and IFN-β1, possibly through the activation of nuclear factor kappa B (NF-κB). To further characterize the mechanism, we tested a natural ORF3a Beta variant, Q57H, and a mutant with deletion of the highly conserved residue, ΔG188. Compared with wild-type ORF3a, the ΔG188 variant yielded more robust activation of cellular oxidative stress, cell death, and innate immune response. Since cellular oxidative stress and inflammation contribute to cell death and tissue damage linked to the severity of COVID-19, our findings suggest that ORF3a is a promising, novel therapeutic target against COVID-19.  IMPORTANCE  The ongoing COVID-19 pandemic caused by SARS-CoV-2 has claimed over 5.5 million lives with more than 300 million people infected worldwide. While vaccines are effective, the emergence of new viral variants could jeopardize vaccine protection. Treatment of COVID-19 by antiviral drugs provides an alternative to battle against the disease. The goal of this study was to identify viral therapeutic targets that can be used in antiviral drug discovery. Utilizing a genome-wide functional analysis in a fission yeast cell-based system, we identified 12 viral candidates, including ORF3a, which cause cellular oxidative stress, inflammation, apoptosis, and necrosis that contribute to cytopathogenicity and COVID-19. Our findings indicate that antiviral agents targeting ORF3a could have a great impact on COVID-19.","doi":"10.1128/mbio.00169-22","authors":"Zhang J, Li Q, Cruz Cosme RS, Gerzanich V, Tang Q, Simard JM, Zhao RY","authors_abbrev":"Zhang J et al.","pubmed_publication_date":"22 Feb 2021","pubmed_entrez_date":"2022-02-15","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-02-17 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20016281","title":"Int6 and Moe1 interact with Cdc48 to regulate ERAD and proper chromosome segregation.","citation":"Cell Cycle 2010 Jan 01;9(1):147-61","abstract":"Int6/eIF3e is implicated in tumorigenesis, but its molecular functions remain unclear. We have studied its fission yeast homolog Yin6, reporting that it regulates proteolysis by controlling the assembly/localization of proteasomes, and binds directly to another conserved protein, Moe1. In the present study, we isolated Cdc48 as a Moe1-binding protein from a yeast two-hybrid screen, and confirmed biochemically that they form a stable complex in fission yeast. Overexpressing Moe1 or Yin6 partially rescued phenotypes of cdc48 mutants; conversely, overexpressing Cdc48 partially rescued phenotypes of moe1 or yin6 mutants. Mutants defective in both Cdc48 and the Yin6-Moe1 complex showed growth defects that were far more severe than either alone. These double mutants were severely deficient in endoplasmic reticulum associated degradation (ERAD), as they were hypersensitive to accumulation of misfolded proteins. In addition, their chromosomes showed frequent defects in spindle attachment and segregation--these mitotic defects correlated with Ase1 and Bir1/survivin mislocalization. These results suggest that Cdc48, Yin6 and Moe1 act in the same protein complex to concertedly control ERAD and chromosome segregation. Many of these properties are evolutionarily conserved in humans, since human Cdc48 rescued the lethality of the yeast cdc48Delta mutant, and Int6 and Moe1/eIF3d bind Cdc48 in human cells.","authors":"Otero JH, Suo J, Gordon C, Chang EC","authors_abbrev":"Otero JH et al.","pubmed_publication_date":"01 Jan 2010","pubmed_entrez_date":"2009-12-18","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.08","SPAC637.07"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:39998228","title":"Fission yeast metabolome dynamics during phosphate starvation and replenishment.","citation":"mBio 2025 Feb 25;:e0024125","abstract":"","doi":"10.1128/mbio.00241-25","authors":"Sanchez AM, Kyaw AK, Violante SN, Garg A, Cross JR, Shuman S","authors_abbrev":"Sanchez AM et al.","pubmed_publication_date":"25 Feb 2025","pubmed_entrez_date":"2025-02-25","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-02-26 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18079700","title":"Cell-cycle regulation of cohesin stability along fission yeast chromosomes.","citation":"EMBO J 2008 Jan 09;27(1):111-21","abstract":"Sister chromatid cohesion is mediated by cohesin, but the process of cohesion establishment during S-phase is still enigmatic. In mammalian cells, cohesin binding to chromatin is dynamic in G1, but becomes stabilized during S-phase. Whether the regulation of cohesin stability is integral to the process of cohesion establishment is unknown. Here, we provide evidence that fission yeast cohesin also displays dynamic behavior. Cohesin association with G1 chromosomes requires continued activity of the cohesin loader Mis4/Ssl3, suggesting that repeated loading cycles maintain cohesin binding. Cohesin instability in G1 depends on wpl1, the fission yeast ortholog of mammalian Wapl, suggestive of a conserved mechanism that controls cohesin stability on chromosomes. wpl1 is nonessential, indicating that a change in wpl1-dependent cohesin dynamics is dispensable for cohesion establishment. Instead, we find that cohesin stability increases at the time of S-phase in a reaction that can be uncoupled from DNA replication. Hence, cohesin stabilization might be a pre-requisite for cohesion establishment rather than its consequence.","authors":"Bernard P, Schmidt CK, Vaur S, Dheur S, Drogat J, Genier S, Ekwall K, Uhlmann F, Javerzat JP","authors_abbrev":"Bernard P et al.","pubmed_publication_date":"09 Jan 2008","pubmed_entrez_date":"2007-12-15","publication_year":"2008","canto_session_key":"de87f5175641f7e9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasu Kakui","canto_first_approved_date":"2018-05-25 16:08:26","canto_approved_date":"2022-09-21 11:19:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-13 12:22:49","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yasu Kakui","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPCC338.17c","SPBC428.17c","SPAC1687.18c","SPBC16A3.11","SPBC29A10.14"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2018-05-25"},{"uniquename":"PMID:39256560","title":"Nitrogen signaling factor triggers a respiration-like gene expression program in fission yeast.","citation":"EMBO J 2024 Sep 10;","abstract":"Microbes have evolved intricate communication systems that enable individual cells of a population to send and receive signals in response to changes in their immediate environment. In the fission yeast Schizosaccharomyces pombe, the oxylipin nitrogen signaling factor (NSF) is part of such communication system, which functions to regulate the usage of different nitrogen sources. Yet, the pathways and mechanisms by which NSF acts are poorly understood. Here, we show that NSF physically interacts with the mitochondrial sulfide:quinone oxidoreductase Hmt2 and that it prompts a change from a fermentation- to a respiration-like gene expression program without any change in the carbon source. Our results suggest that NSF activity is not restricted to nitrogen metabolism alone and that it could function as a rheostat to prepare a population of S. pombe cells for an imminent shortage of their preferred nutrients.","doi":"10.1038/s44318-024-00224-z","authors":"Ohsawa S, Schwaiger M, Iesmantavicius V, Hashimoto R, Moriyama H, Matoba H, Hirai G, Sodeoka M, Hashimoto A, Matsuyama A, Yoshida M, Yashiroda Y, Bühler M","authors_abbrev":"Ohsawa S et al.","pubmed_publication_date":"10 Sep 2024","pubmed_entrez_date":"2024-09-10","publication_year":"2024","canto_session_key":"e8e9a85064af3936","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-09-11 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18394897","title":"RNA interference guides histone modification during the S phase of chromosomal replication.","citation":"Curr Biol 2008 Apr 08;18(7):490-5","abstract":"Heterochromatin is chromosomal material that remains condensed throughout the cell division cycle and silences genes nearby. It is found in almost all eukaryotes, and although discovered (in plants) almost 100 years ago, the mechanism by which heterochromatin is inherited has remained obscure. Heterochromatic silencing and histone H3 lysine-9 methylation (H3K9me2) depend, paradoxically, on heterochromatic transcription and RNA interference (RNAi).\nHere, we show that heterochromatin protein 1 in fission yeast (Swi6) is lost via phosphorylation of H3 serine 10 (H3S10) during mitosis, allowing heterochromatic transcripts to transiently accumulate in S phase. Rapid processing of these transcripts into small interfering RNA (siRNA) promotes restoration of H3K9me2 and Swi6 after replication when cohesin is recruited. We also show that RNAi in fission yeast is inhibited at high temperatures, providing a plausible mechanism for epigenetic phenomena that depend on replication and temperature, such as vernalization in plants and position effect variegation in animals.\nThese results explain how \"silent\" heterochromatin can be transcribed and lead to a model for epigenetic inheritance during replication.","doi":"10.1016/j.cub.2008.03.016","authors":"Kloc A, Zaratiegui M, Nora E, Martienssen R","authors_abbrev":"Kloc A et al.","pubmed_publication_date":"08 Apr 2008","pubmed_entrez_date":"2008-04-09","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31345733","title":"Distributing meiotic crossovers for optimal fertility and evolution.","citation":"DNA Repair (Amst) 2019 Sep;81:102648","abstract":"During meiosis, homologous chromosomes of a diploid cell are replicated and, without a second replication, are segregated during two nuclear divisions to produce four haploid cells (including discarded polar bodies in females of many species). Proper segregation of chromosomes at the first division requires in most species that homologous chromosomes be physically connected. Tension generated by connected chromosomes moving to opposite sides of the cell signals proper segregation. In the absence of the required connections, called crossovers, chromosomes often segregate randomly and produce aneuploid gametes and, thus, dead or disabled progeny. To be effective, crossovers must be properly distributed along chromosomes. Crossovers within or too near the centromere interfere with proper segregation; crossovers too near each other can ablate the required tension; and crossovers too concentrated in only one or a few regions would not re-assort most genetic characters important for evolution. Here, we discuss current knowledge of how the optimal distribution of crossovers is achieved in the fission yeast Schizosaccharomyces pombe, with reference to other well-studied species for comparison and illustration of the diversity of biology.","doi":"10.1016/j.dnarep.2019.102648","authors":"Nambiar M, Chuang YC, Smith GR","authors_abbrev":"Nambiar M et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-07-27","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-07-29 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37553386","title":"A conserved membrane curvature-generating protein is crucial for autophagosome formation in fission yeast.","citation":"Nat Commun 2023 Aug 08;14(1):4765","abstract":"Organelles are shaped by curvature-generating proteins, which include the reticulons and REEPs that are involved in forming the endoplasmic reticulum (ER). A conserved REEP subfamily differs from the ER-shaping REEPs in abundance and membrane topology and has unidentified functions. Here, we show that Rop1, the single member of this family in the fission yeast Schizosacharomyces pombe, is crucial for the macroautophagy of organelles and cytosolic proteins. Rop1 is needed for the formation of phagophores, cup-like structures consisting of two closely apposed membrane sheets that encapsulate cargo. It is recruited at early stages to phagophores and is required for their maturation into autophagosomes. Rop1 function relies on its ability to generate high membrane curvature and on its colocalization with the autophagy component Atg2 that is thought to reside at the phagophore rim. We propose that Rop1 facilitates the formation and growth of the double-membrane structure of the autophagosome.","doi":"10.1038/s41467-023-40530-4","authors":"Wang N, Shibata Y, Paulo JA, Gygi SP, Rapoport TA","authors_abbrev":"Wang N et al.","pubmed_publication_date":"08 Aug 2023","pubmed_entrez_date":"2023-08-08","publication_year":"2023","canto_session_key":"91fbedafa14f14da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tom Rapoport","canto_first_approved_date":"2024-04-09 13:50:59","canto_approved_date":"2025-06-16 16:56:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-25 18:09:12","canto_added_date":"2023-08-10 00:15:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":37,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Tom Rapoport","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31E1.01c","SPBC30D10.09c","SPBC31A8.01c","SPBC1709.05","SPBC16G5.05c","SPAC6B12.08","SPAC22H12.05c","SPCC830.08c","SPBP8B7.24c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2024-04-09"},{"uniquename":"PMID:16498703","title":"Yeast 14-3-3 proteins.","citation":"Yeast 2006 Feb;23(3):159-71","abstract":"14-3-3 proteins form a family of highly conserved proteins which are present in all eukaryotic organisms investigated, often in multiple isoforms, up to 13 in some plants. They interact with more than 200 different, mostly phosphorylated proteins. The molecular consequences of 14-3-3 binding are diverse: this binding may result in stabilization of the active or inactive phosphorylated form of the protein, to a conformational alteration leading to activation or inhibition, to a different subcellular localization, to the interaction with other proteins or to shielding of binding sites. The binding partners, and hence the 14-3-3 proteins, are involved in almost every cellular process and 14-3-3 proteins have been linked to several diseases, such as cancer, Alzheimer's disease, the neurological Miller-Dieker and spinocerebellar ataxia type 1 diseases and bovine spongiform encephalopathy (BSE). The yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe both have two genes encoding 14-3-3 proteins, BMH1 and BMH2 and rad24 and rad25, respectively. In these yeasts, 14-3-3 proteins are essential in most laboratory strains. As in higher eukaryotes, yeast 14-3-3 proteins bind to numerous proteins involved in a variety of cellular processes. Recent genome-wide studies on yeast strains with impaired 14-3-3 function support the participation of 14-3-3 proteins in numerous yeast cellular processes. Given the high evolutionary conservation of the 14-3-3 proteins, the experimental accessibility and relative simplicity of yeasts make them excellent model organisms for elucidating the function of the 14-3-3 protein family.","authors":"van Heusden GP, Steensma HY","authors_abbrev":"van Heusden GP et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-02-25","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28438891","title":"A second Wpl1 anti-cohesion pathway requires dephosphorylation of fission yeast kleisin Rad21 by PP4.","citation":"EMBO J 2017 May 15;36(10):1364-1378","abstract":"Cohesin mediates sister chromatid cohesion which is essential for chromosome segregation and repair. Sister chromatid cohesion requires an acetyl-transferase (Eso1 in fission yeast) counteracting Wpl1, promoting cohesin release from DNA We report here that Wpl1 anti-cohesion function includes an additional mechanism. A genetic screen uncovered that Protein Phosphatase 4 (PP4) mutants allowed cell survival in the complete absence of Eso1. PP4 co-immunoprecipitated Wpl1 and cohesin and Wpl1 triggered Rad21 de-phosphorylation in a PP4-dependent manner. Relevant residues were identified and mapped within the central domain of Rad21. Phospho-mimicking alleles dampened Wpl1 anti-cohesion activity, while alanine mutants were neutral indicating that Rad21 phosphorylation would shelter cohesin from Wpl1 unless erased by PP4. Experiments in post-replicative cells lacking Eso1 revealed two cohesin populations. Type 1 was released from DNA by Wpl1 in a PP4-independent manner. Type 2 cohesin, however, remained DNA-bound and lost its cohesiveness in a manner depending on Wpl1- and PP4-mediated Rad21 de-phosphorylation. These results reveal that Wpl1 antagonizes sister chromatid cohesion by a novel pathway regulated by the phosphorylation status of the cohesin kleisin subunit.","doi":"10.15252/embj.201696050","authors":"Birot A, Eguienta K, Vazquez S, Claverol S, Bonneu M, Ekwall K, Javerzat JP, Vaur S","authors_abbrev":"Birot A et al.","pubmed_publication_date":"15 May 2017","pubmed_entrez_date":"2017-04-26","publication_year":"2017","canto_session_key":"b2ae716b0ad7c3cb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jean-Paul Javerzat","canto_first_approved_date":"2017-11-01 16:03:40","canto_approved_date":"2022-09-21 11:42:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-04 09:41:21","canto_added_date":"2017-04-27 00:15:13","annotation_curators":[{"name":"Jean-Paul Javerzat","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.20","SPBC29A10.04","SPAC10F6.09c","SPAC31A2.05c","SPBC216.01c","SPBC26H8.05c","SPCC338.17c","SPBC428.17c","SPAC110.02","SPBC16A3.11"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2017-11-01"},{"uniquename":"PMID:8143803","title":"Homologous recombination in fission yeast: absence of crossover interference and synaptonemal complex.","citation":"Experientia 1994 Mar 15;50(3):295-306","abstract":"The study of homologous recombination in the fission yeast Schizosaccharomyces pombe has recently been extended to the cytological analysis of meiotic prophase. Unlike in most eukaryotes no tripartite SC structure is detectable, but linear elements resembling axial cores of other eukaryotes are retained. They may be indispensable for meiotic recombination and proper chromosome segregation in meiosis I. In addition fission yeast shows interesting features of chromosome organization in vegetative and meiotic cells: Centromeres and telomeres cluster and associate with the spindle pole body. The special properties of fission yeast meiosis correlate with the absence of crossover interference in meiotic recombination. These findings are discussed. In addition homologous recombination in fission yeast is reviewed briefly.","authors":"Kohli J, Bähler J","authors_abbrev":"Kohli J et al.","pubmed_publication_date":"15 Mar 1994","pubmed_entrez_date":"1994-03-15","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23770677","title":"In vitro contraction of cytokinetic ring depends on myosin II but not on actin dynamics.","citation":"Nat Cell Biol 2013 Jul;15(7):853-9","abstract":"Cytokinesis in many eukaryotes involves the contraction of an actomyosin-based contractile ring. However, the detailed mechanism of contractile ring contraction is not fully understood. Here, we establish an experimental system to study contraction of the ring to completion in vitro. We show that the contractile ring of permeabilized fission yeast cells undergoes rapid contraction in an ATP- and myosin-II-dependent manner in the absence of other cytoplasmic constituents. Surprisingly, neither actin polymerization nor its disassembly is required for contraction of the contractile ring, although addition of exogenous actin-crosslinking proteins blocks ring contraction. Using contractile rings generated from fission yeast cytokinesis mutants, we show that not all proteins required for assembly of the ring are required for its contraction in vitro. Our work provides the beginnings of the definition of a minimal contraction-competent cytokinetic ring apparatus.","doi":"10.1038/ncb2781","authors":"Mishra M, Kashiwazaki J, Takagi T, Srinivasan R, Huang Y, Balasubramanian MK, Mabuchi I","authors_abbrev":"Mishra M et al.","pubmed_publication_date":"Jul 2013","pubmed_entrez_date":"2013-06-18","publication_year":"2013","canto_session_key":"bfad67243d7e2d78","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-13 10:37:58","canto_approved_date":"2023-11-15 11:34:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-10 15:41:07","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC15A10.08","SPCC645.05c","SPAC27F1.02c","SPAC4A8.05c","SPCC613.04c","SPBC1778.06c","SPAP8A3.08"],"gene_count":8,"ltp_gene_count":2,"approved_date":"2020-12-13"},{"uniquename":"PMID:26238358","title":"RNAi and heterochromatin assembly.","citation":"Cold Spring Harb Perspect Biol 2015 Aug 03;7(8):a019323","abstract":"The involvement of RNA interference (RNAi) in heterochromatin formation has become clear largely through studies in the fission yeast Schizosaccharomyces pombe and plants like Arabidopsis thaliana. This article discusses how heterochromatic small interfering RNAs are produced and how the RNAi machinery participates in the formation and function of heterochromatin.","doi":"10.1101/cshperspect.a019323","authors":"Martienssen R, Moazed D","authors_abbrev":"Martienssen R et al.","pubmed_publication_date":"03 Aug 2015","pubmed_entrez_date":"2015-08-05","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-08-06 00:19:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22077425","title":"Schizosaccharomyces pombe, unlike Saccharomyces cerevisiae, may not directly regulate nuclear-cytoplasmic transport of spliced tRNAs in response to nutrient availability.","citation":"Biochem Cell Biol 2011 Dec;89(6):554-61","abstract":"Eukaryotic cells adapt to changes in nutrient levels by regulating key processes, such as gene transcription, ribosome biogenesis, and protein translation. Several studies have shown that nuclear export of tRNAs is also regulated in Saccharomyces cerevisiae and rat hepatoma H4IIE cells during nutrient stress. However, recent studies suggest that nutrient stress does not affect nuclear tRNA export in several mammalian cell lines, including rat hepatoma H4IIE. Furthermore, in contrast to previous studies, data reported more recently established that nuclear export of mature tRNAs derived from intron-containing pre-tRNAs, but not mature tRNAs made from intronless precursors, is affected by nutrient stress in several species of Saccharomyces, but not in the yeast Kluyveromyces lactis . Here, we provide evidence suggesting that Schizosaccharomyces pombe, like mammalian cells and K. lactis, but unlike Saccharomyces, do not directly regulate nuclear export of mature tRNAs made from intron-containing pre-tRNAs in response to nutrient stress. These studies collectively suggest that regulation of nuclear export of spliced tRNAs to the cytoplasm in response to nutrient availability may be limited to the genus Saccharomyces, which unlike other yeasts and higher eukaryotes produce energy for fermentative growth using respiration-independent pathways by downregulating the citric acid cycle and the electron transport chain.","doi":"10.1139/o11-061","authors":"Pierce JB, Mangroo D","authors_abbrev":"Pierce JB et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-11-15","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9475720","title":"Isolation of a Schizosaccharomyces pombe rad21ts mutant that is aberrant in chromosome segregation, microtubule function, DNA repair and sensitive to hydroxyurea: possible involvement of Rad21 in ubiquitin-mediated proteolysis.","citation":"Genetics 1998 Jan;148(1):49-57","abstract":"The fission yeast DNA repair gene rad21+ is essential for cell growth. To investigate the function essential for cell proliferation, we have isolated a temperature-sensitive mutant of the rad21+ gene. The mutant, rad21-K1, showed abnormal mitosis at the nonpermissive temperature. Some cells contained abnormal nuclear structures, such as condensed chromosomes with short spindles, or chromosomes stretched or unequally separated by elongating spindles. Other cells exhibited the displaced nucleus or a cut-like phenotype. Similar abnormalities were observed when the Rad21 protein was depleted from cells. We therefore concluded that Rad21 is essential for proper segregation of chromosomes. Moreover, the rad21-K1 mutant is sensitive not only to UV and gamma-ray irradiation but to thiabendazole and hydroxyurea, indicating that Rad21 plays important roles in microtubule function, DNA repair, and S phase function. The relation to the microtubule function was further confirmed by the fact that rad21+ genetically interacts with tubulin genes, nda2+ and nda3+. Finally, the growth of the rad21-K1 mutant was inhibited at the permissive temperature by introduction of another mutation in the cut9+ gene, coding for a component of the 20S cyclosome/anaphase promoting complex, which is involved in ubiquitin-mediated proteolysis. The results suggest that these diverse functions of Rad21 may be facilitated through ubiquitin-mediated proteolysis.","authors":"Tatebayashi K, Kato J, Ikeda H","authors_abbrev":"Tatebayashi K et al.","pubmed_publication_date":"Jan 1998","pubmed_entrez_date":"1998-02-25","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAC6F12.15c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:10102358","title":"Genetic interactions between Hsp90 and the Cdc2 mitotic machinery in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1999 Mar;261(2):242-50","abstract":"In Schizosaccharomyces pombe, wee1 encodes a tyrosine kinase that inhibits entry into mitosis by phophorylating Cdc2, the universal cyclin-dependent kinase (Cdk) that regulates the G2/M transition in all eukaryotic cells. A search for suppressors of the G2 arrest caused by overexpression of weel led to the isolation of a new allele of swo1 (named swo1-w1), the gene coding for chaperone Hsp90, which is required to stabilise Weel. The swo1-w1 allele carries a glycine to aspartic acid substitution at amino acid 155 that results in a partial loss of Hsp90 function. Cells bearing the swo1-w1 mutation in combination with the point mutation cdc2-33 or cdc2-M26 showed severe mitotic defects. Genetic interactions were not observed in combination with point mutations in other cdc genes, suggesting that Cdc2 specifically interacts with Hsp90. This synthetic lethal swo1-w1 cdc2-33 (or cdc2-M26) strain had normal levels of Cdc2 protein and histone H1 phosphorylation activity, indicating that Hsp90 is required to enable Cdc2 to interact with its mitotic substrates or regulators, rather than for its proper folding or stabilisation. In a wild-type background, swo1-w1 mutant cells were sensitive to temperature as well as to other stress agents, such as KCI, ethanol and formamide. Under these stressful growth conditions, the swo1-w1 cells displayed anaphase B arrest and aberrant septation patterns, indicating that a subset of proteins involved in mitosis and cytokinesis is highly dependent on chaperone Hsp90 for function.","authors":"Muñoz MJ, Jimenez J","authors_abbrev":"Muñoz MJ et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-04-02","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.04c","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:40700808","title":"Exploring the Cka1 kinase interactome: unveiling novel potential regulatory roles of CKII kinase in S. pombe.","citation":"Biochem Biophys Res Commun 2025 Jul 17;778:152382","abstract":"Casein kinase II (CKII) is a highly conserved, constitutively active serine/threonine kinase involved in regulation of diverse cellular processes. In the fission yeast Schizosaccharomyces pombe, Cka1 serves as a catalytic subunit of the CKII complex. To uncover novel Cka1 interactors and potential substrates, we employed RNase-free tandem affinity purification strategy coupled with mass spectrometry. This analysis revealed associations between Cka1 and components of the RSC chromatin remodeling and DNA packaging complexes, Pcs1/Mde4 complex, as well as proteins linked to snoRNA-containing ribonucleoproteins and spliceosomal machinery. Interestingly, in vitro kinase assays unveiled that Cka1 phosphorylates Pcs1 and Mde4, homologues of the Saccharomyces cerevisiae monopolin subunits. These findings suggest for the potential role of Cka1 kinase in regulating chromatin dynamics, pre-mRNA splicing, and mitotic division.","doi":"10.1016/j.bbrc.2025.152382","authors":"Jurcik J, Cipakova I, Karika LO, Bellova J, Kohutova L, Gregan J, Barath P, Cipak L","authors_abbrev":"Jurcik J et al.","pubmed_publication_date":"17 Jul 2025","pubmed_entrez_date":"2025-07-23","publication_year":"2025","canto_session_key":"f312ef954cdc89a3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-23 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C11.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33898463","title":"Tell the Difference Between Mitosis and Meiosis: Interplay Between Chromosomes, Cytoskeleton, and Cell Cycle Regulation.","citation":"Front Cell Dev Biol 2021;9:660322","abstract":"Meiosis is a specialized style of cell division conserved in eukaryotes, particularly designed for the production of gametes. A huge number of studies to date have demonstrated how chromosomes behave and how meiotic events are controlled. Yeast substantially contributed to the understanding of the molecular mechanisms of meiosis in the past decades. Recently, evidence began to accumulate to draw a perspective landscape showing that chromosomes and microtubules are mutually influenced: microtubules regulate chromosomes, whereas chromosomes also regulate microtubule behaviors. Here we focus on lessons from recent advancement in genetical and cytological studies of the fission yeast  Schizosaccharomyces pombe , revealing how chromosomes, cytoskeleton, and cell cycle progression are organized and particularly how these are differentiated in mitosis and meiosis. These studies illuminate that meiosis is strategically designed to fulfill two missions: faithful segregation of genetic materials and production of genetic diversity in descendants through elaboration by meiosis-specific factors in collaboration with general factors.","doi":"10.3389/fcell.2021.660322","authors":"Sato M, Kakui Y, Toya M","authors_abbrev":"Sato M et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-04-26","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-04-28 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26096785","title":"Chromosome domain architecture and dynamic organization of the fission yeast genome.","citation":"FEBS Lett 2015 Oct 07;589(20 Pt A):2975-86","abstract":"Advanced techniques including the chromosome conformation capture (3C) methodology and its derivatives are complementing microscopy approaches to study genome organization, and are revealing new details of three-dimensional (3D) genome architecture at increasing resolution. The fission yeast Schizosaccharomyces pombe (S. pombe) comprises a small genome featuring organizational elements of more complex eukaryotic systems, including conserved heterochromatin assembly machinery. Here we review key insights into genome organization revealed in this model system through a variety of techniques. We discuss the predominant role of Rabl-like configuration for interphase chromosome organization and the dynamic changes that occur during mitosis and meiosis. High resolution Hi-C studies have also revealed the presence of locally crumpled chromatin regions called \"globules\" along chromosome arms, and implicated a critical role for pericentromeric heterochromatin in imposing fundamental constraints on the genome to maintain chromosome territoriality and stability. These findings have shed new light on the connections between genome organization and function. It is likely that insights gained from the S. pombe system will also broadly apply to higher eukaryotes.","doi":"10.1016/j.febslet.2015.06.008","authors":"Mizuguchi T, Barrowman J, Grewal SI","authors_abbrev":"Mizuguchi T et al.","pubmed_publication_date":"07 Oct 2015","pubmed_entrez_date":"2015-06-23","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-06-24 00:20:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8618924","title":"Orp1, a member of the Cdc18/Cdc6 family of S-phase regulators, is homologous to a component of the origin recognition complex.","citation":"Proc Natl Acad Sci U S A 1995 Dec 19;92(26):12475-9","abstract":"cdc18+ of Schizosaccharomyces pombe is a periodically expressed gene that is required for entry into S phase and for the coordination of S phase with mitosis. cdc18+ is related to the Saccharomyces cerevisiae gene CDC6, which has also been implicated in the control of DNA replication. We have identified a new Sch. pombe gene, orp1+, that encodes an 80-kDa protein with amino acid sequence motifs conserved in the Cdc18 and Cdc6 proteins. Genetic analysis indicates that orp1+ is essential for viability. Germinating spores lacking the orp1+ gene are capable of undergoing one or more rounds of DNA replication but fail to progress further, arresting as long cells with a variety of deranged nuclear structures. Unlike cdc18+, orp1+ is expressed constitutively during the cell cycle. cdc18+, CDC6, and orp1+ belong to a family of related genes that also includes the gene ORC1, which encodes a subunit of the origin recognition complex (ORC) of S. cerevisiae. The products of this gene family share a 250-amino acid domain that is highly conserved in evolution and contains several characteristic motifs, including a consensus purine nucleotide-binding motif. Among the members of this gene family, orp1+ is most closely related to S. cerevisiae ORC1. Thus, the protein encoded by orp1+ may represent a component of an Sch. pombe ORC. The orp1+ gene is also closely related to an uncharacterized putative human homologue. It is likely that the members of the cdc18/CDC6 family play key roles in the regulation of DNA replication during the cell cycle of diverse species from archaebacteria to man.","authors":"Muzi-Falconi M, Kelly TJ","authors_abbrev":"Muzi-Falconi M et al.","pubmed_publication_date":"19 Dec 1995","pubmed_entrez_date":"1995-12-19","publication_year":"1995","canto_session_key":"f284fe43c381666f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-20 16:51:02","canto_approved_date":"2024-11-14 09:49:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-22 18:09:01","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-20"},{"uniquename":"PMID:22079013","title":"Crosstalk between NDR kinase pathways coordinates cell cycle dependent actin rearrangements.","citation":"Cell Div 2011 Nov 11;6:19","abstract":"Regulation of cytoskeletal remodeling is essential for cell cycle transitions. In fission yeast two NDR kinase signaling cascades, MOR and SIN, regulate the actin cytoskeleton to promote polarized growth during interphase and cytokinesis respectively. Our understanding of how these signaling pathways are coordinated to assist transition between the two cell-cycle stages is limited. Here, we review work from our laboratory, which reveals that cross talk between the SIN and MOR pathways is required for inhibition of interphase polarity programs during cytokinesis. Given the conservation of NDR kinase signaling pathways, our results may define general mechanisms by which these pathways are coordinated in higher organisms.","doi":"10.1186/1747-1028-6-19","authors":"Gupta S, McCollum D","authors_abbrev":"Gupta S et al.","pubmed_publication_date":"11 Nov 2011","pubmed_entrez_date":"2011-11-15","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37540145","title":"Completion of mitochondrial division requires the intermembrane space protein Mdi1/Atg44.","citation":"J Cell Biol 2023 Oct 02;222(10)","abstract":"Mitochondria are highly dynamic double membrane-bound organelles that maintain their shape in part through fission and fusion. Mitochondrial fission is performed by a dynamin-related protein, Dnm1 (Drp1 in humans), that constricts and divides the mitochondria in a GTP hydrolysis-dependent manner. However, it is unclear whether factors inside mitochondria help coordinate the process and if Dnm1/Drp1 activity is sufficient to complete the fission of both mitochondrial membranes. Here, we identify an intermembrane space protein required for mitochondrial fission in yeast, which we propose to name Mdi1 (also named Atg44). Loss of Mdi1 causes mitochondrial hyperfusion due to defects in fission, but not the lack of Dnm1 recruitment to mitochondria. Mdi1 is conserved in fungal species, and its homologs contain an amphipathic α-helix, mutations of which disrupt mitochondrial morphology. One model is that Mdi1 distorts mitochondrial membranes to enable Dnm1 to robustly complete fission. Our work reveals that Dnm1 cannot efficiently divide mitochondria without the coordinated function of Mdi1 inside mitochondria.","doi":"10.1083/jcb.202303147","authors":"Connor OM, Matta SK, Friedman JR","authors_abbrev":"Connor OM et al.","pubmed_publication_date":"02 Oct 2023","pubmed_entrez_date":"2023-08-04","publication_year":"2023","canto_session_key":"f9e73b547427ce13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jonathan Friedman","canto_first_approved_date":"2023-08-17 09:27:40","canto_approved_date":"2024-07-03 10:17:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-08-14 15:45:54","canto_added_date":"2023-08-08 09:52:58","annotation_curators":[{"name":"Jonathan Friedman","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.14c","SPBC12C2.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-08-17"},{"uniquename":"EMBL:AU009903","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35079912","title":"Identification and analysis of iron transporters from the fission yeast Schizosaccharomyces pombe.","citation":"Arch Microbiol 2022 Jan 26;204(2):152","abstract":"Iron is an essential trace metal ion required for all living organisms, and is taken up by iron transporters. Here, we identified and characterized three-candidate high-affinity (Fio1, Frp1 and Frp2) and two-candidate low-affinity iron transporters (Fet4 and Pdt1) from the fission yeast Schizosaccharomyces pombe. Protein sequence analyses revealed that Fio1 is a multicopper oxidase that contains three cupredoxin domains with eleven candidate iron-binding ligands, whereas Frp1 harbors a ferric reductase domain with three-candidate heme-binding ligands. Protein sequence analyses also revealed that Fet4 and Pdt1 are integral membrane proteins with 10 and 11 transmembrane regions, respectively. Deletion of fio1 and, to a lesser extent, frp1 impaired growth under iron-depleted conditions, whereas deletion of frp1 and, to a lesser extent, frp2 inhibited growth under iron-replete conditions. Deletion of fet4 and pdt1 did not affect the growth of cells under iron-depleted and iron-replete conditions. Deletion of fio1 or frp1 also increased the sensitivity of cells to other transition metals. The copper sensitivity of Δfio1 cells could be rescued by iron, suggesting that the addition of iron might decrease the uptake of potentially toxic copper in Δfio1 cells. The copper sensitivity of Δfio1 cells could also be rescued by deletion of frp1, suggesting that Fio1 and Frp1 may function together in iron and copper uptakes in S. pombe. Our results revealed that iron and copper uptake systems may be partially overlapped in S. pombe.","doi":"10.1007/s00203-021-02683-y","authors":"Ahmad F, Luo Y, Yin H, Zhang Y, Huang Y","authors_abbrev":"Ahmad F et al.","pubmed_publication_date":"26 Jan 2022","pubmed_entrez_date":"2022-01-26","publication_year":"2022","canto_session_key":"38d3a04a24fe3f3c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2022-04-26 07:43:52","canto_approved_date":"2022-04-26 07:43:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-31 08:54:23","canto_added_date":"2022-01-28 01:15:04","annotation_curators":[{"name":"Ying Huang","community_curator":true,"annotation_count":38,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1683.09c","SPBP26C9.03c","SPAC1783.07c","SPBC947.05c","SPAC1F7.08","SPAC27F1.08"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2022-04-26"},{"uniquename":"PMID:35507852","title":"Feeding broiler chicks with Schizosaccharomyces pombe-expressed phytase-containing diet improves growth performance, phosphorus digestibility, toe ash, and footpad lesions.","citation":"Anim Biosci 2022 Sep;35(9):1390-1399","abstract":"The objective of this study was to evaluate the effects of dietary supplementation of Schizosaccharomyces pombe (S. pombe) -expressed phytase on growth performance, apparent ileal digestibility, organ indexes, meat quality, toe ash, and footpad lesions score in broiler chicks.\nA total of 390 one-day-old broiler chicks were randomly assigned to 5 groups based on the initial body weight (42.15±0.17 g), there were 6 replicate cages per treatment and 13 birds (mixed sex) per cage. The experimental period was 45 days, including 4 periods (starter, days 1 to 10; grower, days 11 to 24; finisher 1, days 25 to 38; finisher 2, days 39 to 45). Dietary treatments were based on a corn-soybean meal-basal diet and supplemented with 500, 750, 1,000, and 1,500 FTU/kg S. pombe-expressed phytase. One phytase unit (FTU) was defined as the amount of enzyme that catalyzes the release of one micromole phosphate from phytate per minute at 37°C and pH 5.5.\nThe inclusion of increasing levels of phytase in the diet linearly increased the body weight gain during days 1 to 10 (p = 0.001), 25 to 38 (p = 0.016), 39 to 45 (p = 0.018), and 1 to 45 (p = 0.004), feed intake during days 25 to 38 (p = 0.032), feed conversion ratio during days 1 to 10 (p = 0.001), 39 to 45 (p = 0.038), and 1 to 45 (p = 0.012), carcass weight (p = 0.035), toe ash (p<0.001), and apparent ileal phosphorus digestibility (p = 0.049). However, the footpad lesions score (p = 0.040) decreased linearly with the increase in phytase levels in the diet.\nDietary supplementation of S. pombe-expressed phytase was beneficial to the growth performance, toe ash, apparent ileal phosphorus digestibility, and footpad lesions of broiler chicks in a dose-dependent manner.","doi":"10.5713/ab.21.0462","authors":"Dang X, Chun SG, Kim IH","authors_abbrev":"Dang X et al.","pubmed_publication_date":"Sep 2022","pubmed_entrez_date":"2022-05-04","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-05-07 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1001372","title":"Effect of heat on the viability of Schizosaccharomyces pombe 972h growing in synchronous cultures.","citation":"Exp Cell Res 1976 Dec;103(2):447-9","abstract":"","authors":"Bullock JG, Coakley WT","authors_abbrev":"Bullock JG et al.","pubmed_publication_date":"Dec 1976","pubmed_entrez_date":"1976-12-01","publication_year":"1976","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33106658","title":"Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion.","citation":"Nat Struct Mol Biol 2020 Dec;27(12):1185-1193","abstract":"The molecular function of Atg9, the sole transmembrane protein in the autophagosome-forming machinery, remains unknown. Atg9 colocalizes with Atg2 at the expanding edge of the isolation membrane (IM), where Atg2 receives phospholipids from the endoplasmic reticulum (ER). Here we report that yeast and human Atg9 are lipid scramblases that translocate phospholipids between outer and inner leaflets of liposomes in vitro. Cryo-EM of fission yeast Atg9 reveals a homotrimer, with two connected pores forming a path between the two membrane leaflets: one pore, located at a protomer, opens laterally to the cytoplasmic leaflet; the other, at the trimer center, traverses the membrane vertically. Mutation of residues lining the pores impaired IM expansion and autophagy activity in yeast and abolished Atg9's ability to transport phospholipids between liposome leaflets. These results suggest that phospholipids delivered by Atg2 are translocated from the cytoplasmic to the luminal leaflet by Atg9, thereby driving autophagosomal membrane expansion.","doi":"10.1038/s41594-020-00518-w","authors":"Matoba K, Kotani T, Tsutsumi A, Tsuji T, Mori T, Noshiro D, Sugita Y, Nomura N, Iwata S, Ohsumi Y, Fujimoto T, Nakatogawa H, Kikkawa M, Noda NN","authors_abbrev":"Matoba K et al.","pubmed_publication_date":"Dec 2020","pubmed_entrez_date":"2020-10-27","publication_year":"2020","canto_session_key":"4d7e0c232302b605","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-10-29 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC15D4.07c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"7d0i","gene_chains":[{"gene_uniquename":"SPBC15D4.07c","chain":"B/D/F/H/J/L","position":"1-702"}],"title":"Cryo-EM structure of Schizosaccharomyces pombe Atg9","entry_authors":"Matoba K,Tsutsumi A,Kikkawa M,Noda NN","entry_authors_abbrev":"Matoba K et al.","reference_uniquename":"PMID:33106658","experimental_method":"EM","resolution":"3.0"}]},{"uniquename":"PMID:8332516","title":"Comparison of Schizosaccharomyces pombe expression systems.","citation":"Nucleic Acids Res 1993 Jun 25;21(12):2955-6","abstract":"","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"25 Jun 1993","pubmed_entrez_date":"1993-06-25","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11432827","title":"Fission yeast ch-TOG/XMAP215 homologue Alp14 connects mitotic spindles with the kinetochore and is a component of the Mad2-dependent spindle checkpoint.","citation":"EMBO J 2001 Jul 02;20(13):3389-401","abstract":"The TOG/XMAP215-related proteins play a role in microtubule dynamics at its plus end. Fission yeast Alp14, a newly identified TOG/XMAP215 family protein, is essential for proper chromosome segregation in concert with a second homologue Dis1. We show that the alp14 mutant fails to progress towards normal bipolar spindle formation. Intriguingly, Alp14 itself is a component of the Mad2-dependent spindle checkpoint cascade, as upon addition of microtubule-destabilizing drugs the alp14 mutant is incapable of maintaining high H1 kinase activity, which results in securin destruction and premature chromosome separation. Live imaging of Alp14-green fluorescent protein shows that during mitosis, Alp14 is associated with the peripheral region of the kinetochores as well as with the spindle poles. This is supported by ChIP (chromatin immunoprecipitation) and overlapping localization with the kinetochore marker Mis6. An intact spindle is required for Alp14 localization to the kinetochore periphery, but not to the poles. These results indicate that the TOG/XMAP215 family may play a central role as a bridge between the kinetochores and the plus end of pole to chromosome microtubules.","authors":"Garcia MA, Vardy L, Koonrugsa N, Toda T","authors_abbrev":"Garcia MA et al.","pubmed_publication_date":"02 Jul 2001","pubmed_entrez_date":"2001-07-04","publication_year":"2001","canto_session_key":"1203df6a6f3957f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-08-24 20:08:07","canto_approved_date":"2025-05-27 14:06:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-16 17:37:31","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.14","SPCC895.07","SPBC800.05c","SPBC26H8.07c","SPBC20F10.06"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-08-24"},{"uniquename":"PMID:28986445","title":"Histone H3 Threonine 11 Phosphorylation Is Catalyzed Directly by the Meiosis-Specific Kinase Mek1 and Provides a Molecular Readout of Mek1 Activity  in Vivo .","citation":"Genetics 2017 Dec;207(4):1313-1333","abstract":" Saccharomyces cerevisiae  Mek1 is a CHK2/Rad53-family kinase that regulates meiotic recombination and progression upon its activation in response to DNA double-strand breaks (DSBs). The full catalog of direct Mek1 phosphorylation targets remains unknown. Here, we show that phosphorylation of histone H3 on threonine 11 (H3 T11ph) is induced by meiotic DSBs in  S. cerevisiae  and  Schizosaccharomyces pombe  Molecular genetic experiments in  S. cerevisiae  confirmed that Mek1 is required for H3 T11ph and revealed that phosphorylation is rapidly reversed when Mek1 kinase is no longer active. Reconstituting histone phosphorylation  in vitro  with recombinant proteins demonstrated that Mek1 directly catalyzes H3 T11 phosphorylation. Mutating H3 T11 to nonphosphorylatable residues conferred no detectable defects in otherwise unperturbed meiosis, although the mutations modestly reduced spore viability in certain strains where Rad51 is used for strand exchange in place of Dmc1. H3 T11ph is therefore mostly dispensable for Mek1 function. However, H3 T11ph provides an excellent marker of ongoing Mek1 kinase activity  in vivo  Anti-H3 T11ph chromatin immunoprecipitation followed by deep sequencing demonstrated that H3 T11ph was highly enriched at presumed sites of attachment of chromatin to chromosome axes, gave a more modest signal along chromatin loops, and was present at still lower levels immediately adjacent to DSB hotspots. These localization patterns closely tracked the distribution of Red1 and Hop1, axis proteins required for Mek1 activation. These findings provide insight into the spatial disposition of Mek1 kinase activity and the higher order organization of recombining meiotic chromosomes.","doi":"10.1534/genetics.117.300359","authors":"Kniewel R, Murakami H, Liu Y, Ito M, Ohta K, Hollingsworth NM, Keeney S","authors_abbrev":"Kniewel R et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-10-08","publication_year":"2017","canto_session_key":"fc92840c0d34336c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-10-09 00:15:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:39747188","title":"PhpC NF-Y  transcription factor infiltrates heterochromatin to generate cryptic intron-containing transcripts crucial for small RNA production.","citation":"Nat Commun 2025 Jan 02;16(1):268","abstract":"The assembly of repressive heterochromatin in eukaryotic genomes is crucial for silencing lineage-inappropriate genes and repetitive DNA elements. Paradoxically, transcription of repetitive elements within constitutive heterochromatin domains is required for RNA-based mechanisms, such as the RNAi pathway, to target heterochromatin assembly proteins. However, the mechanism by which heterochromatic repeats are transcribed has been unclear. Using fission yeast, we show that the conserved trimeric transcription factor (TF) PhpC NF-Y  complex can infiltrate constitutive heterochromatin via its histone-fold domains to transcribe repeat elements. PhpC NF-Y  collaborates with a Zn-finger containing TF to bind repeat promoter regions with CCAAT boxes. Mutating either the TFs or the CCAAT binding site disrupts the transcription of heterochromatic repeats. Although repeat elements are transcribed from both strands, PhpC NF-Y -dependent transcripts originate from only one strand. These TF-driven transcripts contain multiple cryptic introns which are required for the generation of small interfering RNAs (siRNAs) via a mechanism involving the spliceosome and RNAi machinery. Our analyses show that siRNA production by this TF-mediated transcription pathway is critical for heterochromatin nucleation at target repeat loci. This study reveals a mechanism by which heterochromatic repeats are transcribed, initiating their own silencing by triggering a primary cascade that produces siRNAs necessary for heterochromatin nucleation.","doi":"10.1038/s41467-024-55736-3","authors":"Srivastav MK, Folco HD, Nathanailidou P, Anil AT, Vijayakumari D, Jain S, Dhakshnamoorthy J, O'Neill M, Andresson T, Wheeler D, Grewal SIS","authors_abbrev":"Srivastav MK et al.","pubmed_publication_date":"02 Jan 2025","pubmed_entrez_date":"2025-01-02","publication_year":"2025","canto_session_key":"53e97b95347633ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Manjit Kumar Srivastav","canto_first_approved_date":"2025-07-02 09:25:04","canto_approved_date":"2025-08-13 19:07:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-11 14:07:44","canto_added_date":"2025-01-04 00:25:04","annotation_curators":[{"name":"Manjit Kumar Srivastav","community_curator":true,"annotation_count":44,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":48,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.08c","SPBC15D4.02","SPAC664.01c","SPCC970.07c","SPBC1105.14","SPAC31A2.11c","SPAC23C11.08","SPAPB1E7.14","SPBC725.11c","SPAC6B12.05c","SPAC1952.05","SPAC4A8.04","SPBC1683.10c","SPBC26H8.07c","SPCC1902.01","SPAC11E3.06","SPCC1235.14","SPCC1620.14c","SPBC29B5.01","SPAC23G3.04","SPAC1F3.07c","SPBC28F2.12","SPAC21E11.03c","SPBC428.08c","SPBC215.12","SPCC191.07","SPNCRNA.1165","SPAC1039.05c","SPNCRNA.1501","SPAC17G8.13c","SPBC1703.02","SPAC821.07c","SPBC4B4.03","SPCC1259.04","SPBC1734.15","SPAC32A11.03c","SPBC3B8.02","SPAC25G10.03","SPCC736.11","SPAC222.04c","SPNCRNA.5103","SPNCRNA.103","SPAPB1A11.04c","SPAC1250.01","SPAC144.02","SPAC29B12.01"],"gene_count":46,"ltp_gene_count":32,"approved_date":"2025-07-02"},{"uniquename":"PMID:3549158","title":"Buoyant density variation during the cell cycle in microorganisms.","citation":"Crit Rev Microbiol 1987;14(1):73-97","abstract":"The behavior of cell buoyant density during the cell cycle has been determined for a number of different cell types, including bacteria, yeast, and mammalian cells. Mean buoyant density was extremely constant and independent of cell age during the cell cycle of the bacterium Escherichia coli, the fission yeast Schizosaccharomyces cerevisiae, the protozoan Amoebae proteus, cells from suspension cell cultures of mouse lymphoma and myeloma, and Chinese hamster ovary cells. In all of these cases, the buoyant densities of these cells were very narrowly distributed, with coefficients of variation of 0.1 to 0.3%. In contrast, buoyant density was variable in cells with thick cell walls and high buoyant densities. Density varied markedly during the cell cycle of the budding yeast Schizosaccharomyces cerevisiae and of the bacterium Streptococcus faecium. The average buoyant densities of cells in exponentially growing cultures of E. coli or Schizosaccharomyces pombe were also independent of growth rate of the cultures. Experiments with E. coli have established that cell buoyant density is controlled by the osmoregulatory system. Although the regulatory mechanisms for this control are unknown, the results suggest that the same or similar mechanisms regulate buoyant density in all of the cells that do not have unduly heavy cell walls and, therefore, these regulatory mechanisms were either conserved during evolution or reflect the convergent evolution found for organic osmolytes.","authors":"Kubitschek HE","authors_abbrev":"Kubitschek HE","pubmed_publication_date":"1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9740128","title":"Intronic snoRNA biosynthesis in Saccharomyces cerevisiae depends on the lariat-debranching enzyme: intron length effects and activity of a precursor snoRNA.","citation":"RNA 1998 Sep;4(9):1096-110","abstract":"The eukaryotic small nucleolar RNAs (snoRNAs) are involved in processing of pre-rRNA and modification of rRNA nucleotides. Some snoRNAs are derived from mono- or polycistronic transcription units, whereas others are encoded in introns of protein genes. The present study addresses the role of the RNA lariat-debranching enzyme (Dbr1p) in the synthesis and function of intronic snoRNAs in the yeast Saccharomyces cerevisiae. Intronic snoRNA production was determined to depend on Dbr1p. Accumulation of mature intronic snoRNAs is reduced in a dbr1 mutant; instead, intronic snoRNAs are \"trapped\" within host intron lariats. Interestingly, the extent of intronic snoRNA accumulation in the form of lariats in dbr1 cells varied among different intronic snoRNAs. Intronic snoRNAs encoded within shorter introns, such as U24 and snR38, accumulate more unprocessed lariat precursors than those encoded within longer introns, e.g., U18 and snR39. This correlation was corroborated by experiments conducted with model intron:U24 snoRNA constructs. These results support a splicing-dependent exonucleolytic pathway for the biosynthesis of intronic snoRNAs. Curiously, U24 in a lariat may be functional in directing methylation of ribosomal RNA.","authors":"Ooi SL, Samarsky DA, Fournier MJ, Boeke JD","authors_abbrev":"Ooi SL et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-09-18","publication_year":"1998","canto_session_key":"8e48e2a479f3cdd6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-30 10:31:36","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-30 10:31:26","canto_added_date":"2016-09-21 00:21:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.02c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2016-09-30"},{"uniquename":"GO_REF:0000066","title":"Representation of transport of a chemical entity as molecular function in the Gene Ontology","abstract":"We have created a standard template for classes describing the transport of a chemical entity (ChEBI) as a molecular function. The underlying equivalence axiom template is \"GO:0005215 and 'transports or maintains localization of' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12786945","title":"Overlapping omt1+ and omt2+ genes are required for spore wall maturation in Schizosaccharomyces pombe.","citation":"Genes Cells 2003 Jun;8(6):547-58","abstract":"Overlapping genes that are transcribed from the same genomic regions are rare in eukaryotes and to date few detailed functional analyses have been reported.\nWe report here three novel overlapping transcripts that are specifically expressed during meiosis of Schizosaccharomyces pombe. They are denoted as omt1+, omt2+ and omt3+ after overlapping meiotic transcripts. omt1+ encodes a 12-kDa protein and omt2+ encodes a 11-kDa protein with homology to the bifunctional mammalian protein DCoH/PCBD. omt3+ does not have a significant open reading frame. The omt2+ transcript overlaps with both the omt1+ and omt3+ transcripts but the latter two transcripts do not overlap. omt1Delta and omt2Delta but not omt3Delta failed to form mature spore walls. The Omt1-GFP and Omt2-GFP fusion proteins localized to the outside and the inside of the spore walls, respectively. The sporulation-specific protein Meu10 and the spore wall components were abnormally localized in the spore walls of omt1Delta and omt2Delta.\nThe overlapping genes omt1+ and omt2+ express functional proteins that participate in spore wall maturation, indicating that gene overlap does not affect the physiological functions of the proteins encoded by these genes. Generation of overlapped RNA may be due to loose regulation of transcription termination during meiosis of S. pombe.","authors":"Kakihara Y, Nabeshima K, Hirata A, Nojima H","authors_abbrev":"Kakihara Y et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-06-06","publication_year":"2003","canto_session_key":"e930f865a30e2c82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-09-20 18:40:28","canto_approved_date":"2025-12-30 16:06:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-28 14:36:17","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.05c","SPBC32H8.11","SPCC1223.12c","SPAC27D7.04","SPNCRNA.130"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2014-09-20"},{"uniquename":"PMID:31073221","title":"Histone H2A insufficiency causes chromosomal segregation defects due to anaphase chromosome bridge formation at rDNA repeats in fission yeast.","citation":"Sci Rep 2019 May 09;9(1):7159","abstract":"The nucleosome, composed of DNA and a histone core, is the basic structural unit of chromatin. The fission yeast Schizosaccharomyces pombe has two genes of histone H2A, hta1 +  and hta2 + ; these genes encode two protein species of histone H2A (H2Aα and H2Aβ, respectively), which differ in three amino acid residues, and only hta2 +  is upregulated during meiosis. However, it is unknown whether S. pombe H2Aα and H2Aβ have functional differences. Therefore, in this study, we examined the possible functional differences between H2Aα and H2Aβ during meiosis in S. pombe. We found that deletion of hta2 + , but not hta1 + , causes defects in chromosome segregation and spore formation during meiosis. Meiotic defects in hta2 +  deletion cells were rescued by expressing additional copies of hta1 +  or by expressing hta1 +  from the hta2 promoter. This indicated that the defects were caused by insufficient amounts of histone H2A, and not by the amino acid residue differences between H2Aα and H2Aβ. Microscopic observation attributed the chromosome segregation defects to anaphase bridge formation in a chromosomal region at the repeats of ribosomal RNA genes (rDNA repeats). These results suggest that histone H2A insufficiency affects the chromatin structures of rDNA repeats, leading to chromosome missegregation in S. pombe.","doi":"10.1038/s41598-019-43633-5","authors":"Yamamoto TG, Ding DQ, Nagahama Y, Chikashige Y, Haraguchi T, Hiraoka Y","authors_abbrev":"Yamamoto TG et al.","pubmed_publication_date":"09 May 2019","pubmed_entrez_date":"2019-05-11","publication_year":"2019","canto_session_key":"01084161ef85ce6c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-05-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10749973","title":"The Schizosaccharomyces pombe protein Yab8p and a novel factor, Yip1p, share structural and functional similarity with the spinal muscular atrophy-associated proteins SMN and SIP1.","citation":"Hum Mol Genet 2000 Mar 22;9(5):663-74","abstract":"The motor neuron disease spinal muscular atrophy (SMA) is caused by reduced levels of functional survival of motor neurons (SMN) protein. Previous studies have shown that SMN binds to the SMN-interacting protein SIP1 and mediates the assembly of spliceosomal U snRNPs in the cytoplasm. In addition, a nuclear function for SMN in pre-mRNA splicing has recently been proposed. Here, we describe the analysis of the Schizo-saccharomyces pombe protein Yab8p and provide evidence that it is structurally and functionally related to SMN found in higher eukaryotes. We show that Yab8p interacts via its N-terminus with a novel protein termed Yip1p. Importantly, Yip1p exhibits homology to SIP1, and the mode of binding to Yab8p is remarkably similar to the SMN-SIP1 interaction. Hence, Yip1p is likely to be the homologue of SIP1 in S.pombe. Yab8p and Yip1p localize predominantly in the nucleus. Genetic studies demonstrate that Yab8p is essential for viability. Strikingly, suppression of YAB8 expression in a conditional knock-out strain causes nuclear accumulation of poly(A) mRNA and inhibition of splicing. These data identify Yab8p as a novel factor involved in splicing and suggest that Yab8p exerts a function similar or identical to the nuclear pool of SMN. Our studies provide a model system to study the cellular function of SMN in yeast, and should help in understanding the molecular events leading to SMA.","authors":"Hannus S, Bühler D, Romano M, Seraphin B, Fischer U","authors_abbrev":"Hannus S et al.","pubmed_publication_date":"22 Mar 2000","pubmed_entrez_date":"2000-04-06","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19B12.12c","SPAC2G11.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:689088","title":"Control of the timing of cell division in fission yeast. Cell size mutants reveal a second control pathway.","citation":"Exp Cell Res 1978 Sep;115(2):317-29","abstract":"","authors":"Fantes PA, Nurse P","authors_abbrev":"Fantes PA et al.","pubmed_publication_date":"Sep 1978","pubmed_entrez_date":"1978-09-01","publication_year":"1978","canto_session_key":"9a74e80e076097ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-07-20 12:10:12","canto_approved_date":"2019-06-14 12:53:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-20 12:09:05","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-07-20"},{"uniquename":"PMID:15226378","title":"Sister-chromatid cohesion mediated by the alternative RF-CCtf18/Dcc1/Ctf8, the helicase Chl1 and the polymerase-alpha-associated protein Ctf4 is essential for chromatid disjunction during meiosis II.","citation":"J Cell Sci 2004 Jul 15;117(Pt 16):3547-59","abstract":"Cohesion between sister chromatids mediated by a multisubunit complex called cohesin is established during DNA replication and is essential for the orderly segregation of chromatids during anaphase. In budding yeast, a specialized replication factor C called RF-C(Ctf18/Dcc1/Ctf8) and the DNA-polymerase-alpha-associated protein Ctf4 are required to maintain sister-chromatid cohesion in cells arrested for long periods in mitosis. We show here that CTF8, CTF4 and a helicase encoded by CHL1 are required for efficient sister chromatid cohesion in unperturbed mitotic cells, and provide evidence that Chl1 functions during S-phase. We also show that, in contrast to mitosis, RF-C(Ctf18/Dcc1/Cft8), Ctf4 and Chl1 are essential for chromosome segregation during meiosis and for the viability of meiotic products. Our finding that cells deleted for CTF8, CTF4 or CHL1 undergo massive meiosis II non-disjunction suggests that the second meiotic division is particularly sensitive to cohesion defects. Using a functional as well as a cytological assay, we demonstrate that CTF8, CHL1 and CTF4 are essential for cohesion between sister centromeres during meiosis but dispensable for cohesin's association with centromeric DNA. Our finding that mutants in fission yeast ctf18 and dcc1 have similar defects suggests that the involvement of the alternative RF-C(Ctf18/Dcc1/Ctf8) complex in sister chromatid cohesion might be highly conserved.","authors":"Petronczki M, Chwalla B, Siomos MF, Yokobayashi S, Helmhart W, Deutschbauer AM, Davis RW, Watanabe Y, Nasmyth K","authors_abbrev":"Petronczki M et al.","pubmed_publication_date":"15 Jul 2004","pubmed_entrez_date":"2004-07-01","publication_year":"2004","canto_session_key":"a5072a23ae384ac4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 15:55:43","canto_approved_date":"2024-06-28 10:21:02","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-01-27 17:07:26","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC902.02c","SPAC31A2.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-17"},{"uniquename":"PMID:21098641","title":"Regulation of cell cycle-specific gene expression in fission yeast by the Cdc14p-like phosphatase Clp1p.","citation":"J Cell Sci 2010 Dec 15;123(Pt 24):4374-81","abstract":"Regulated gene expression makes an important contribution to cell cycle control mechanisms. In fission yeast, a group of genes is coordinately expressed during a late stage of the cell cycle (M phase and cytokinesis) that is controlled by common cis-acting promoter motifs named pombe cell cycle boxes (PCBs), which are bound by a trans-acting transcription factor complex, PCB binding factor (PBF). PBF contains at least three transcription factors, a MADS box protein Mbx1p and two forkhead transcription factors, Sep1p and Fkh2p. Here we show that the fission yeast Cdc14p-like phosphatase Clp1p (Flp1p) controls M-G1 specific gene expression through PBF. Clp1p binds in vivo both to Mbx1p, a MADS box-like transcription factor, and to the promoters of genes transcribed at this cell cycle time. Because Clp1p dephosphorylates Mbx1p in vitro, and is required for Mbx1p cell cycle-specific dephosphorylation in vivo, our observations suggest that Clp1p controls cell cycle-specific gene expression through binding to and dephosphorylating Mbx1p.","doi":"10.1242/jcs.073056","authors":"Papadopoulou K, Chen JS, Mead E, Feoktistova A, Petit C, Agarwal M, Jamal M, Malik A, Spanos A, Sedgwick SG, Karagiannis J, Balasubramanian MK, Gould KL, McInerny CJ","authors_abbrev":"Papadopoulou K et al.","pubmed_publication_date":"15 Dec 2010","pubmed_entrez_date":"2010-11-25","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPBC16G5.15c","SPBC11B10.09","SPBC19G7.06","SPAC1782.09c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:16296344","title":"[Studies on HIV/AIDS using the fission yeast Schizosaccharomyces pombe].","citation":"Rinsho Byori 2005 Oct;53(10):950-6","abstract":"Human immunodeficiency virus (HIV) is a causative agent of acquired immunodeficiency syndrome (AIDS) and a member of Retrovirus family. The name of \"retrovirus\" is said to be derived from \"reverse-transcribing oncogenic virus.\" Living up to its name, retrovirus has contributed to oncology, especially in the field of cancer pathogenesis. Retrovirus research has led to discovery of a number of oncogenes as well. Since the discovery of HIV in 1983, however, retrovirus has also been considered as an important etiologic agent that could incapacitate the cells involved in immune responses. As of the end of 2004, the number of people living with HIV/AIDS is estimated to be as large as 40 million. Every year, nearly 5 million people are newly infected with HIV, and 3 million people die of AIDS in the world, mainly in Africa and southeastern and southern Asia. Despite extensive studies, detailed mechanisms of HIV pathogenesis are still unclear, and efforts are being made to clarify functions of various HIV proteins and identify the cellular factors that could interact with the HIV proteins. One of the HIV accessory proteins, Vpr, causes the host cell cycle arrest at G2 phase, which may play an important pathogenic role in AIDS induction. Exploiting the fission yeast Schizosaccharomyces pombe useful for cell cycle studies, I've been trying to elucidate the mechanism by which Vpr induces the G2 arrest as presented in this review.","authors":"Masuda M","authors_abbrev":"Masuda M","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-11-22","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6278416","title":"The 5S RNA genes of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1982 Jan 22;10(2):487-500","abstract":"The genomic arrangement and sequences of S. pombe 5S RNA genes are reported here. The 5S gene sequences appear to be dispersed within the genome, and are found independently of other rRNA genes. The sequences of two 5S genes examined show identical coding regions of 119 base pairs but have widely varying flanking sequences. A tRNAAsp gene is found in the 3' flanking region of one of the 5S genes. The tRNAAsp gene is faithfully transcribed in an X. laevis in vitro system, while the 5S genes are not transcribed in this system. The phylogenetic position of S. pombe is examined through comparison of 5S RNA sequences.","authors":"Mao J, Appel B, Schaack J, Sharp S, Yamada H, Söll D","authors_abbrev":"Mao J et al.","pubmed_publication_date":"22 Jan 1982","pubmed_entrez_date":"1982-01-22","publication_year":"1982","canto_session_key":"978e7f2b3ed1be95","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 22:00:37","canto_approved_date":"2018-12-22 22:00:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 22:00:29","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:27798241","title":"An acetyltransferase-independent function of Eso1 regulates centromere cohesion.","citation":"Mol Biol Cell 2016 Dec 15;27(25):4002-4010","abstract":"Eukaryotes contain three essential Structural Maintenance of Chromosomes (SMC) complexes: cohesin, condensin, and Smc5/6. Cohesin forms a ring-shaped structure that embraces sister chromatids to promote their cohesion. The cohesiveness of cohesin is promoted by acetylation of N-terminal lysines of the Smc3 subunit by the acetyltransferases Eco1 in Saccharomyces cerevisiae and the homologue, Eso1, in Schizosaccharomyces pombe. In both yeasts, these acetyltransferases are essential for cell viability. However, whereas nonacetylatable Smc3 mutants are lethal in S. cerevisiae, they are not in S. pombe We show that the lethality of a temperature-sensitive allele of eso1 (eso1-H17) is due to activation of the spindle assembly checkpoint (SAC) and is associated with premature centromere separation. The lack of cohesion at the centromeres does not correlate with Psm3 acetylation or cohesin levels at the centromeres, but is associated ith significantly reduced recruitment of the cohesin regulator Pds5. The SAC activation in this context is dependent on Smc5/6 function, which is required to remove cohesin from chromosome arms but not centromeres. The mitotic defects caused by Smc5/6 and Eso1 dysfunction are cosuppressed in double mutants. This identifies a novel function (or functions) for Eso1 and Smc5/6 at centromeres and extends the functional relationships between these SMC complexes.","authors":"Lin SJ, Tapia-Alveal C, Jabado OJ, Germain D, O'Connell MJ","authors_abbrev":"Lin SJ et al.","pubmed_publication_date":"15 Dec 2016","pubmed_entrez_date":"2016-11-01","publication_year":"2016","canto_session_key":"5103fb1b0cfbf1f3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-11-02 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPAC10F6.09c","SPCC5E4.06","SPBC16A3.11","SPCC1322.12c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:42014871","title":"Context-dependent activation and evolutionary buffering of a mating pheromone in fission yeast.","citation":"Commun Biol 2026 Apr 21;9(1)","abstract":"The evolution of mating signals drives reproductive isolation and speciation across diverse lineages. However, how short peptide pheromones, typically subject to strong structural constraints, achieve functional diversification remain unclear. In the fission yeast Schizosaccharomyces pombe, a previously established library of 153 single-amino acid variants of the mating pheromone M-factor was applied to large-scale competition assays under varied mating conditions. Mutations deleterious under standard conditions became advantageous at specific environmental pH levels, demonstrating context-dependent pheromone function activation. Synthetic peptide assays confirmed that certain substitutions act as environmental molecular switches. Comparative analysis with the closely related Schizosaccharomyces octosporus species further identified a permissive mutation that mitigates the effects of otherwise inactivating changes, enabling an evolutionary route without intermediate fitness loss. Our findings reveal how short peptide signals can evolve via environmentally contingent activation and compensatory interactions, offering a mechanistic framework for understanding the ecological and evolutionary dynamics of mating communication.","doi":"10.1038/s42003-026-10058-6","authors":"Seike T, Sakata N, Kotani H, Furusawa C","authors_abbrev":"Seike T et al.","pubmed_publication_date":"21 Apr 2026","pubmed_entrez_date":"2026-04-21","publication_year":"2026","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2026-04-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29900664","title":"Tschimganine and its derivatives extend the chronological life span of yeast via activation of the Sty1 pathway.","citation":"Genes Cells 2018 Jun 14;","abstract":"Most antiaging factors or life span extenders are associated with calorie restriction (CR). Very few of these factors function independently of, or additively with, CR. In this study, we focused on tschimganine, a compound that was reported to extend chronological life span (CLS). Although tschimganine led to the extension of CLS, it also inhibited yeast cell growth. We acquired a Schizosaccharomyces pombe mutant with a tolerance for tschimganine due to the gene crm1. The resulting Crm1 protein appears to export the stress-activated protein kinase Sty1 from the nucleus to the cytosol even under stressful conditions. Furthermore, we synthesized two derivative compounds of tschimganine, α-hibitakanine and β-hibitakanine; these derivatives did not inhibit cell growth, as seen with tschimganine. α-hibitakanine extended the CLS, not only in S. pombe but also in Saccharomyces cerevisiae, indicating the possibility that life span regulation by tschimganine derivative may be conserved across various yeast species. We found that the longevity induced by tschimganine was dependent on the Sty1 pathway. Based on our results, we propose that tschimganine and its derivatives extend CLS by activating the Sty1 pathway in fission yeast, and CR extends CLS via two distinct pathways, one Sty1-dependent and the other Sty1-independent. These findings provide the potential for creating an additive life span extension effect when combined with CR, as well as a better understanding of the mechanism of CLS.","doi":"10.1111/gtc.12604","authors":"Hibi T, Ohtsuka H, Shimasaki T, Inui S, Shibuya M, Tatsukawa H, Kanie K, Yamamoto Y, Aiba H","authors_abbrev":"Hibi T et al.","pubmed_publication_date":"14 Jun 2018","pubmed_entrez_date":"2018-06-15","publication_year":"2018","canto_session_key":"2b59f1de5a117ff3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-11-13 15:42:40","canto_approved_date":"2020-11-13 14:53:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-11-03 09:26:49","canto_added_date":"2018-06-16 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC757.07c","SPAC1805.17","SPBC409.07c","SPAC24B11.06c","SPBC215.05"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2018-11-13"},{"uniquename":"PMID:10921878","title":"Fission yeast Fizzy-related protein srw1p is a G(1)-specific promoter of mitotic cyclin B degradation.","citation":"EMBO J 2000 Aug 01;19(15):3968-77","abstract":"Downregulation of cyclin-dependent kinase (Cdk)-mitotic cyclin complexes is important during cell cycle progression and in G(1) arrested cells undergoing differentiation. srw1p, a member of the Fizzy-related protein family in fission yeast, is required for the degradation of cdc13p mitotic cyclin B during G(1) arrest. Here we show that srw1p is not required for the degradation of cdc13p during mitotic exit demonstrating that there are two systems operative at different stages of the cell cycle for cdc13p degradation, and that srw1p is phosphorylated by Cdk-cdc13p only becoming dephosphorylated during G(1) arrest. We propose that this phosphorylation targets srw1p for proteolysis and inhibits its activity to promote cdc13p turnover.","authors":"Yamaguchi S, Okayama H, Nurse P","authors_abbrev":"Yamaguchi S et al.","pubmed_publication_date":"01 Aug 2000","pubmed_entrez_date":"2000-08-02","publication_year":"2000","canto_session_key":"664a66149791e18c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-08-29 15:32:45","canto_approved_date":"2025-09-03 10:35:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-12 15:38:36","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC11E3.01c","SPBC582.03","SPAC144.13c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-08-29"},{"uniquename":"PMID:8625425","title":"pH sensitivity of Schizosaccharomyces pombe: effect on the cellular phenotype associated with lacZ gene expression.","citation":"Curr Genet 1996 Apr;29(5):457-61","abstract":"We report on a series of experiments in Schizosaccharomyces pombe to detect the blue-colour colony phenotype associated with expression of the Escherichia coli lacZ gene. Increasing the pH in solid minimal medium to optimize blue colony colour revealed a pH-sensitive phenotype in auxotrophic strains requiring uracil and leucine as external supplements. This phenotype was observed among common S. pombe stock strains, 5-fluoroorotic acid (5-FOA)selected strains, and random genetic segregants. Growth of prototrophic S. pombe strains 972 and 975 or the adenine auxotrophic strain NCYC 1860 were unaffected by an increase in external pH. Analysis of genetic segregants from three independent crosses indicated that a single auxotrophic marker (ura4- or leu1-32) was sufficient for yeast cell-growth inhibition when the medium pH was increased above 6.6. In contrast, growth of a Saccharomyces cerevisiae strain isogenic to AH22, requiring uracil, leucine and histidine, was unaffected by changes in the pH of the medium. These observations suggest that uptake of uracil and leucine into S. pombe cells is compromised by alterations in external pH. Our results have implications for detection of the lacZ gene-encoded bluecolour colony phenotype in S. pombe, which is optimized by growth in the presence of 5-bromo-4-chloro-3-indolyl- \"beta\"-D-galactoside (Xgal) at pH 7.0. We discuss the conditions under which this blue-colour phenotype can be routinely observed in S. pombe.","authors":"Arndt GM, Atkins D","authors_abbrev":"Arndt GM et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_session_key":"e09ae4029661cf1c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-09-27 11:01:04","canto_approved_date":"2024-07-15 11:55:32","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-09-27 11:00:57","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13","SPBC1A4.02c","SPCC330.05c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-09-27"},{"uniquename":"PMID:7565608","title":"Schizosaccharomyces pombe rds1, an adenine-repressible gene regulated by glucose, ammonium, phosphate, carbon dioxide and temperature.","citation":"Mol Gen Genet 1995 Aug 30;248(4):439-45","abstract":"We report the isolation and characterization of an adenine-repressible gene, rds1, in the fission yeast Schizosaccharomyces pombe. The transcript of rds1 is greatly increased in abundance when adenine auxotrophic strains are starved for adenine. rds1 is also derepressed when wild-type cells are starved for glucose, ammonium, or phosphate. In addition, derepression occurs when wild-type cells are exposed to a carbon dioxide atmosphere, when they are shifted to higher temperatures or when they enter stationary phase. The nucleotide sequence of the rds1 gene and the corresponding amino acid sequence of its protein share no obvious homologies with any other known gene or protein and we have not found a phenotype for rds1 disruption mutants. We speculate that expression of the rds1 gene is regulated by one or several components of the adenine nucleotide pool and that its gene product has a function in stress-related responses of the cell.","authors":"Ludin KM, Hilti N, Schweingruber ME","authors_abbrev":"Ludin KM et al.","pubmed_publication_date":"30 Aug 1995","pubmed_entrez_date":"1995-08-30","publication_year":"1995","canto_session_key":"07cc7abfbaa6d1b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-09 17:02:29","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-07-20 09:44:31","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13","SPAC4D7.08c","SPBC405.01","SPAC343.12","SPBC19C7.03"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2012-07-20"},{"uniquename":"PMID:18845253","title":"Cdk-counteracting phosphatases unlock mitotic exit.","citation":"Curr Opin Cell Biol 2008 Dec;20(6):661-8","abstract":"Entry into mitosis of the eukaryotic cell cycle is driven by rising cyclin-dependent kinase (Cdk) activity. During exit from mitosis, Cdk activity must again decline. Cdk downregulation by itself, however, is not able to guide mitotic exit, if not a phosphatase reverses mitotic Cdk phosphorylation events. In budding yeast, this role is played by the Cdc14 phosphatase. We are gaining an increasingly detailed picture of its regulation during anaphase, and of the way it orchestrates ordered progression through mitosis. Much less is known about protein dephosphorylation during mitotic exit in organisms other than budding yeast, but evidence is now mounting for crucial contributions of regulated phosphatases also in metazoan cells.","doi":"10.1016/j.ceb.2008.09.003","authors":"Queralt E, Uhlmann F","authors_abbrev":"Queralt E et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-10-11","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12519200","title":"Rga5p is a specific Rho1p GTPase-activating protein that regulates cell integrity in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2003 Jan;47(2):507-18","abstract":"Schizosaccharomyces pombe Rho1p regulates (1,3)beta-d-glucan synthesis and is required for cell integrity maintenance and actin cytoskeleton organization, but nothing is known about the regulation of this protein. At least nine different S. pombe genes code for proteins predicted to act as Rho GTPase-activating proteins (GAPs). The results shown in this paper demonstrate that the protein encoded by the gene named rga5+ is a GAP specific for Rho1p. rga5+ overexpression is lethal and causes morphological alterations similar to those reported for Rho1p inactivation. rga5+ deletion is not lethal and causes a mild general increase in cell wall biosynthesis and morphological alterations when cells are grown at 37 degrees C. Upon mild overexpression, Rga5p localizes to growth areas and possesses both in vivo and in vitro GAP activity specific for Rho1p. Overexpression of rho1+ in rga5Delta cells is lethal, with a morphological phenotype resembling that of the overexpression of the constitutively active allele rho1G15V. In addition (1,3)beta-d-glucan synthase activity, regulated by Rho1p, is increased in rga5Delta cells and decreased in rga5-overexpressing cells. Moreover, the increase in (1,3)beta-d-glucan synthase activity caused by rho1+ overexpression is considerably higher in rga5Delta than in wild-type cells. Genetic interactions suggest that Rga5p is also important for the regulation of the other known Rho1p effectors, Pck1p and Pck2p.","authors":"Calonge TM, Arellano M, Coll PM, Perez P","authors_abbrev":"Calonge TM et al.","pubmed_publication_date":"Jan 2003","pubmed_entrez_date":"2003-01-10","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.04","SPBC17F3.01c","SPAC17G8.14c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:5713811","title":"Analysis of the genetic instability induced by nitrous acid in Schizosaccharomyces pombe.","citation":"Genet Res 1968 Aug;12(1):45-54","abstract":"","authors":"Loprieno N, Abbondandolo A, Bonatti S, Guglielminetti R","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"Aug 1968","pubmed_entrez_date":"1968-08-01","publication_year":"1968","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36941121","title":"Metformin extends the chronological lifespan of fission yeast by altering energy metabolism and stress resistance capacity.","citation":"FEMS Yeast Res 2023 Jan 04;23","abstract":"The antiaging properties of metformin used for the treatment of type-2 diabetes mellitus have been studied extensively, but there is more to discover regarding underlying mechanisms. Here, we show that metformin significantly prolongs the chronological lifespan (CLS) of Schizosaccharomyces pombe through mechanisms similar to those observed in mammalian cells and other model organisms. While the presence of metformin in the medium caused an increase in carbohydrate consumption and ATP production, it reduced reactive oxygen species production and alleviate oxidative damage parameters such as lipid peroxidation and carbonylated proteins. We also tested whether the effect of metformin changed with the time it was added to the medium and observed that the lifespan-prolonging effect of metformin was related to the glucose concentration in the medium and did not prolong lifespan when added after glucose was completely depleted in the medium. On the other hand, cells inoculated in glucose-free medium containing metformin also showed extended lifespan suggesting that mechanisms other than that solely depend on glucose availability may be involved in extending the lifespan. These results suggest that metformin prolongs lifespan especially affecting energy metabolism and stress resistance capacity and that fission yeast can be effectively used when investigating the antiaging mechanisms of metformin.","doi":"10.1093/femsyr/foad018","authors":"Şeylan C, Tarhan Ç","authors_abbrev":"Şeylan C et al.","pubmed_publication_date":"04 Jan 2023","pubmed_entrez_date":"2023-03-20","publication_year":"2023","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2023-03-22 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25767875","title":"Fission yeast Scp3 potentially maintains microtubule orientation through bundling.","citation":"PLoS One 2015;10(3):e0120109","abstract":"Microtubules play important roles in organelle transport, the maintenance of cell polarity and chromosome segregation and generally form bundles during these processes. The fission yeast gene scp3+ was identified as a multicopy suppressor of the cps3-81 mutant, which is hypersensitive to isopropyl N-3-chlorophenylcarbamate (CIPC), a poison that induces abnormal multipolar spindle formation in higher eukaryotes. In this study, we investigated the function of Scp3 along with the effect of CIPC in the fission yeast Schizosaccharomyces pombe. Microscopic observation revealed that treatment with CIPC, cps3-81 mutation and scp3+ gene deletion disturbed the orientation of microtubules in interphase cells. Overexpression of scp3+ suppressed the abnormal orientation of microtubules by promoting bundling. Functional analysis suggested that Scp3 functions independently from Ase1, a protein largely required for the bundling of the mitotic spindle. A strain lacking the ase1+ gene was more sensitive to CIPC, with the drug affecting the integrity of the mitotic spindle, indicating that CIPC has a mitotic target that has a role redundant with Ase1. These results suggested that multiple systems are independently involved to ensure microtubule orientation by bundling in fission yeast.","doi":"10.1371/journal.pone.0120109","authors":"Ozaki K, Chikashige Y, Hiraoka Y, Matsumoto T","authors_abbrev":"Ozaki K et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-14","publication_year":"2015","canto_session_key":"7bfcc78d17ac6673","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-16 01:15:37","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3A11.02"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:8568898","title":"Structural analysis of mitochondrial DNA molecules from fungi and plants using moving pictures and pulsed-field gel electrophoresis.","citation":"J Mol Biol 1996 Feb 02;255(4):564-88","abstract":"The size and structure of mitochondrial DNA (mtDNA) molecules was investigated by conventional and pulsed-field gel electrophoresis (PFGE) and by analyzing moving pictures during electrophoresis of individual fluorescently labelled mtDNA molecules. Little or no mtDNA that migrated into the gel was found in circular form for fungi (Schizosaccharomyces pombe, Saccharomyces cerevisiae and Neurospora crassa) or plants (Brassica hirta, tobacco, voodoo lily and maize). Most mtDNA migrated as a smear of linear DNA sizes from about 50 to 100 or 250 kilobases (kb), depending on the species, irrespective of the size of the mitochondrial genome over a range of 0.06 to 570 kb. S. cerevisiae, B. hirta and tobacco also yielded a linear mtDNA fraction containing molecules > 1000 kb in size. About half the mtDNA remained in the well of the gel after PFGE. Moving pictures revealed that this well-bound (wb) mtDNA contained molecules larger than the genome size in linear form for all species (except N. crassa) and in multi-fibered, comet-like forms for most of the wb mtDNA of N. crassa and Sc. pombe. A minor amount of the wb mtDNA with visually interpretable structure was circular: circle sizes were both larger and smaller than the 80-kb genome of S. cerevisiae, larger than the 19-kb genome of Sc. pombe and smaller than the 208-kb and 570-kb genomes of B. hirta and maize, respectively. About 25 to 75% of the wb mtDNA from cultured tobacco cells was found in circles smaller than its genome size. Partial digestion of Sc. pombe mtDNA with restriction endonucleases that cleave once per genome revealed gel bands at about 38 kb and 19 kb with a smear of sizes between the bands and below the 19-kb band, suggesting a head-to-tail genomic concatemer as the most prominent form in extracted mtDNA. A pattern of bands with smears was also found for complete digests (with multiply cleaving enzymes) of mtDNA from Sc. pombe, S. cerevisiae and N. crassa, but bands without smears were found for digests of DNA from phage lambda and several plasmids.","authors":"Bendich AJ","authors_abbrev":"Bendich AJ","pubmed_publication_date":"02 Feb 1996","pubmed_entrez_date":"1996-02-02","publication_year":"1996","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23222840","title":"Centrosomal MPF triggers the mitotic and morphogenetic switches of fission yeast.","citation":"Nat Cell Biol 2013 Jan;15(1):88-95","abstract":"Activation of mitosis-promoting factor (MPF) drives mitotic commitment. In human cells active MPF appears first on centrosomes. We show that local activation of MPF on the equivalent organelle of fission yeast, the spindle pole body (SPB), promotes Polo kinase activity at the SPBs long before global MPF activation drives mitotic commitment. Artificially promoting MPF or Polo activity at various locations revealed that this local control of Plo1 activity on G2 phase SPBs dictates the timing of mitotic commitment. Cytokinesis of the rod-shaped fission yeast cell generates a naive, new, cell end. Growth is restricted to the experienced old end until a point in G2 phase called new end take off (NETO) when bipolar growth is triggered. NETO coincided with MPF activation of Plo1 on G2 phase SPBs (ref. 4). Both MPF and Polo activities were required for NETO and both induced NETO when ectopically activated at interphase SPBs. NETO promotion by MPF required polo. Thus, local MPF activation on G2 SPBs directs polo kinase to control at least two distinct and temporally separated, cell-cycle transitions at remote locations.","doi":"10.1038/ncb2633","authors":"Grallert A, Patel A, Tallada VA, Chan KY, Bagley S, Krapp A, Simanis V, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2012-12-11","publication_year":"2013","canto_session_key":"014aa031f039268b","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-05-27 09:01:11","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9115279","title":"Pch1(+), a second essential C-type cyclin gene in Schizosaccharomyces pombe.","citation":"J Biol Chem 1997 May 02;272(18):12100-6","abstract":"The Schizosaccharomyces pombe gene pch1(+) (pombe cyclin C homology) was isolated in a two-hybrid screen for proteins that interact with Cdc2. The cyclin box region of Pch1 protein shares greatest sequence identity with mammalian and Drosophila C-type cyclins ( approximately 33% identity). Pch1 is significantly less similar to Mcs2 (19% identity), a second member of the C-type cyclin family in S. pombe. Cdc2 co-precipitates with Pch1 in S. pombe cell lysates, although Cdc2 may not be the major catalytic partner of a Pch1 kinase in vivo. Purified Pch1-associated kinase phosphorylated myelin basic protein, histone H1, and a peptide corresponding to the carboxyl-terminal domain repeat of RNA polymerase II. The amount of pch1 mRNA does not oscillate during the cell cycle, as is the case for mRNA transcripts of other C-type cyclin genes. Deltapch1 cells are inviable, therefore S. pombe has two essential genes that encode members of the C-type cyclin family, pch1(+) and mcs2(+). The Deltapch1 mutation causes pleiotropic morphological defects and an associated growth deficiency, but loss of Pch1 activity does not result in a cdc cell cycle-arrest phenotype.","authors":"Furnari BA, Russell P, Leatherwood J","authors_abbrev":"Furnari BA et al.","pubmed_publication_date":"02 May 1997","pubmed_entrez_date":"1997-05-02","publication_year":"1997","canto_session_key":"bccb6092e76df671","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-07-07 13:52:03","canto_approved_date":"2021-04-16 15:37:22","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-28 16:10:42","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC32F12.06"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-07-07"},{"uniquename":"PMID:34133210","title":"Cdk1 phosphorylation of fission yeast paxillin inhibits its cytokinetic ring localization.","citation":"Mol Biol Cell 2021 Aug 15;32(17):1534-1544","abstract":"Divisions of the genetic material and cytoplasm are coordinated spatially and temporally to ensure genome integrity. This coordination is mediated in part by the major cell cycle regulator cyclin-dependent kinase (Cdk1). Cdk1 activity peaks during mitosis, but during mitotic exit/cytokinesis Cdk1 activity is reduced, and phosphorylation of its substrates is reversed by various phosphatases including Cdc14, PP1, PP2A, and PP2B. Cdk1 is known to phosphorylate several components of the actin- and myosin-based cytokinetic ring (CR) that mediates division of yeast and animal cells. Here we show that Cdk1 also phosphorylates the  Schizosaccharomyces pombe  CR component paxillin Pxl1. We determined that both the Cdc14 phosphatase Clp1 and the PP1 phosphatase Dis2 contribute to Pxl1 dephosphorylation at mitotic exit, but PP2B/calcineurin does not. Preventing Pxl1 phosphorylation by Cdk1 results in increased Pxl1 levels, precocious Pxl1 recruitment to the division site, and increased duration of CR constriction. In vitro Cdk1-mediated phosphorylation of Pxl1 inhibits its interaction with the F-BAR domain of the cytokinetic scaffold Cdc15, thereby disrupting a major mechanism of Pxl1 recruitment. Thus, Pxl1 is a novel substrate through which  S. pombe  Cdk1 and opposing phosphatases coordinate mitosis and cytokinesis.","doi":"10.1091/mbc.E20-12-0807","authors":"Mangione MC, Chen JS, Gould KL","authors_abbrev":"Mangione MC et al.","pubmed_publication_date":"15 Aug 2021","pubmed_entrez_date":"2021-06-16","publication_year":"2021","canto_session_key":"28333b01f58bc586","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"MariaSanta Mangione","canto_first_approved_date":"2021-07-14 07:34:14","canto_approved_date":"2021-09-10 20:22:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-07-07 17:03:59","canto_added_date":"2021-07-05 00:15:03","annotation_curators":[{"name":"MariaSanta Mangione","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPCC830.06","SPAC20G8.05c","SPBC4F6.12","SPAC1782.09c","SPBC776.02c","SPBC11B10.09"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2021-07-14"},{"uniquename":"PMID:2112089","title":"Structural and functional analysis of ypt2, an essential ras-related gene in the fission yeast Schizosaccharomyces pombe encoding a Sec4 protein homologue.","citation":"EMBO J 1990 Jun;9(6):1957-62","abstract":"Using the cloned Saccharomyces cerevisiae YPT1 gene as hybridization probe, a gene, designated ypt2, was isolated from the fission yeast Schizosaccharomyces pombe and found to encode a 200 amino acid long protein most closely related to the ypt branch of the ras superfamily. Disruption of the ypt2 gene is lethal. The bacterially produced ypt2 gene product is shown to bind GTP. A region of the ypt2 protein corresponding to but different from the 'effector region' of ras proteins is also different from that of ypt1 proteins of different species but identical to the 'effector loop' of the S.cerevisiae SEC4 gene product, a protein known to be required for vesicular protein transport. The S.pombe ypt2 gene under control of the S.cerevisiae GAL10 promoter is able to suppress the temperature-sensitive phenotype of a S. cerevisiae sec4 mutant, indicating a functional similarity of these GTP-binding proteins from the two very distantly related yeasts.","authors":"Haubruck H, Engelke U, Mertins P, Gallwitz D","authors_abbrev":"Haubruck H et al.","pubmed_publication_date":"Jun 1990","pubmed_entrez_date":"1990-06-01","publication_year":"1990","canto_session_key":"cc872132c252909e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-02-05 17:52:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-31 08:40:38","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-31"},{"uniquename":"PMID:16138082","title":"Mechanism of Lys48-linked polyubiquitin chain recognition by the Mud1 UBA domain.","citation":"EMBO J 2005 Sep 21;24(18):3178-89","abstract":"The ubiquitin-pathway associated (UBA) domain is a 40-residue polyubiquitin-binding motif. The Schizosaccharomyces pombe protein Mud1 is an ortholog of the Saccharomyces cerevisiae DNA-damage response protein Ddi1 and binds to K48-linked polyubiquitin through its UBA domain. We have solved the crystal structure of Mud1 UBA at 1.8 angstroms resolution, revealing a canonical three-helical UBA fold. We have probed the interactions of this domain using mutagenesis, surface plasmon resonance, NMR and analytical ultracentrifugation. We show that the ubiquitin-binding surface of Mud1 UBA extends beyond previously recognized motifs and can be functionally dissected into primary and secondary ubiquitin-binding sites. Mutation of Phe330 to alanine, a residue exposed between helices 2 and 3, significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyubiquitin, despite leaving the primary binding surface functionally intact. Moreover, K48-linked diubiquitin binds a single Mud1 UBA domain even in the presence of excess UBA. We therefore propose a mechanism for the recognition of K48-linked polyubiquitin chains by Mud1 in which diubiquitin units are specifically recognized by a single UBA domain.","authors":"Trempe JF, Brown NR, Lowe ED, Gordon C, Campbell ID, Noble ME, Endicott JA","authors_abbrev":"Trempe JF et al.","pubmed_publication_date":"21 Sep 2005","pubmed_entrez_date":"2005-09-03","publication_year":"2005","canto_session_key":"65ecf5af1bf30a8a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-28 13:05:53","canto_approved_date":"2023-02-28 13:05:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-15 12:19:20","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.08c","SPAC56F8.08"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2023-02-28","pdb_entries":[{"pdb_id":"1z96","gene_chains":[{"gene_uniquename":"SPAC56F8.08","chain":"A/B","position":"293-332"}],"title":"Crystal structure of the Mud1 UBA domain","entry_authors":"Trempe J-F,Brown NR,Lowe ED,Noble MEM,Gordon C,Campbell ID,Johnson LN,Endicott JA","entry_authors_abbrev":"Trempe J-F et al.","reference_uniquename":"PMID:16138082","experimental_method":"X-ray","resolution":"1.8"}]},{"uniquename":"PMID:24186369","title":"r-DNA plasmid from Schizosaccharomyces pombe: Cloning and use in yeast transformation.","citation":"Curr Genet 1982 Oct;6(1):31-8","abstract":"1. an extrachromosomal, extramitochondrial DNA circle of about 3 μm length, occurring in S. pombe, was cloned in pBR322 and a detailed restriction map of the cloned sequence constructed. 2. Hybridization of this DNA with the ribosomal DNA from S. cerevisiae revealed regions of homology which were mapped in the cloned S. pombe DNA. 3. A transformation system was developed using the URA3 gene of S. cerevisiae and the 3 μm molecule. It was shown that the r-DNA part of the hybrid plasmid promotes replication in S. pombe.","doi":"10.1007/BF00397639","authors":"Fournier P, Gaillardin C, de Louvencourt L, Heslot H, Lang BF, Kaudewitz F","authors_abbrev":"Fournier P et al.","pubmed_publication_date":"Oct 1982","pubmed_entrez_date":"2013-11-05","publication_year":"1982","canto_session_key":"ea2cd3fa5035d8b9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 20:16:20","canto_approved_date":"2019-01-31 20:16:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 20:16:08","canto_added_date":"2014-02-16 06:09:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:7857672","title":"Molecular cloning and characterization of a fission yeast gene responsible for supersensitivity to the spindle poison, isopropyl N-3-chlorophenyl carbamate.","citation":"Jpn J Genet 1994 Dec;69(6):671-8","abstract":"The cps3 gene of the fission yeast, Schizosaccharomyces pombe, was previously identified as a mutation conferring supersensitivity to the spindle poison, isopropyl N-3-chlorophenyl carbamate (CIPC). A 3.2 kb DNA fragment that complements the mutant phenotype was cloned from a S. pombe genomic library. The base sequence analysis showed that the fragment contains a maximum 1086 nucleotide open reading frame and that the putative product consists of 362 amino acids, having a molecular weight of 39.3 KDa. No significant homology of the potential product with known proteins could be found by database searches. A disruptant of the gene, produced by insertion of a ura4+ fragment was able to germinate, but not to undergo cell division, suggesting that the gene to be essential for the cell cycle progression. The disruption experiment suggests that the gene is an extragenic suppressor of cps3 mutation.","authors":"Ishiguro J, Uhara Y, Kawahara K","authors_abbrev":"Ishiguro J et al.","pubmed_publication_date":"Dec 1994","pubmed_entrez_date":"1994-12-01","publication_year":"1994","canto_session_key":"298ea235c069ec90","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2012-11-28 20:42:42","canto_approved_date":"2022-02-24 11:42:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-28 17:38:48","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A11.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-11-28"},{"uniquename":"PMID:15509783","title":"Kinetochore targeting of fission yeast Mad and Bub proteins is essential for spindle checkpoint function but not for all chromosome segregation roles of Bub1p.","citation":"Mol Cell Biol 2004 Nov;24(22):9786-801","abstract":"Several lines of evidence suggest that kinetochores are organizing centers for the spindle checkpoint response and the synthesis of a \"wait anaphase\" signal in cases of incomplete or improper kinetochore-microtubule attachment. Here we characterize Schizosaccharomyces pombe Bub3p and study the recruitment of spindle checkpoint components to kinetochores. We demonstrate by chromatin immunoprecipitation that they all interact with the central domain of centromeres, consistent with their role in monitoring kinetochore-microtubule interactions. Bub1p and Bub3p are dependent upon one another, but independent of the Mad proteins, for their kinetochore localization. We demonstrate a clear role for the highly conserved N-terminal domain of Bub1p in the robust targeting of Bub1p, Bub3p, and Mad3p to kinetochores and show that this is crucial for an efficient checkpoint response. Surprisingly, neither this domain nor kinetochore localization is required for other functions of Bub1p in chromosome segregation.","authors":"Vanoosthuyse V, Valsdottir R, Javerzat JP, Hardwick KG","authors_abbrev":"Vanoosthuyse V et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-29","publication_year":"2004","canto_session_key":"f9b779cdcdfe781f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-05-15 09:08:35","canto_approved_date":"2024-03-27 06:57:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-11 17:57:53","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.05c","SPAC23H3.08c","SPCC1322.12c","SPBC26H8.07c","SPCC1795.01c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-05-15"},{"uniquename":"PMID:12742165","title":"Never say never. The NIMA-related protein kinases in mitotic control.","citation":"Trends Cell Biol 2003 May;13(5):221-8","abstract":"Mitosis sees a massive reorganization of cellular architecture. The microtubule cytoskeleton is reorganized to form a bipolar spindle between duplicated microtubule organizing centers, the chromosomes are condensed, attached to the spindle at their kinetochores, and, through the action of multiple molecular motors, the chromosomes are segregated into two daughter cells. Mitosis also sees a substantial wave of protein phosphorylation, controlling signaling events that coordinate mitotic processes and ensure accurate chromosome segregation. The key switch for the onset of mitosis is the archetypal cyclin-dependent kinase, Cdc2. Under the direction of Cdc2 is an executive of protein serine/threonine kinases that fall into three families: the Polo kinases, Aurora kinases and the NIMA-related kinases (Nrk). The latter family has proven the most enigmatic in function, although recent advances from several sources are beginning to reveal a common functional theme.","authors":"O'Connell MJ, Krien MJ, Hunter T","authors_abbrev":"O'Connell MJ et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-05-14","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-11-26 01:19:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21880825","title":"Live cell imaging of yeast.","citation":"Cold Spring Harb Protoc 2011 Sep 01;2011(9)","abstract":"The development of cloning vectors for green fluorescent protein (GFP) and the simplicity of yeast reverse genetics allow straightforward labeling of yeast proteins in living cells. Budding and fission yeast are therefore attractive organisms in which to study dynamic cellular processes such as growth, cell division, and morphogenesis using live cell fluorescence microscopy. This article focuses on methods to culture, mount, and observe budding yeast cells using three-dimensional (3D) microscopy, but the methods are broadly applicable to other types of cells and other imaging techniques. The emphasis is on 3D imaging, because yeast cells are roughly spherical, and most organelles in yeast move in three dimensions. Three-dimensional imaging also makes it possible to apply image restoration methods (e.g., deconvolution) to obtain sharper images with better definition. This is important, because yeast cells are small (haploid Saccharomyces cerevisiae cells have a diameter of ~4-5 µm) relative to the resolution of even the best optical microscope (~0.25 µm).","doi":"10.1101/pdb.top065482","authors":"Rines DR, Thomann D, Dorn JF, Goodwin P, Sorger PK","authors_abbrev":"Rines DR et al.","pubmed_publication_date":"01 Sep 2011","pubmed_entrez_date":"2011-09-02","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24948612","title":"Serial number tagging reveals a prominent sequence preference of retrotransposon integration.","citation":"Nucleic Acids Res 2014 Jul;42(13):8449-60","abstract":"Transposable elements (TE) have both negative and positive impact on the biology of their host. As a result, a balance is struck between the host and the TE that relies on directing integration to specific genome territories. The extraordinary capacity of DNA sequencing can create ultra dense maps of integration that are being used to study the mechanisms that position integration. Unfortunately, the great increase in the numbers of insertion sites detected comes with the cost of not knowing which positions are rare targets and which sustain high numbers of insertions. To address this problem we developed the serial number system, a TE tagging method that measures the frequency of integration at single nucleotide positions. We sequenced 1 million insertions of retrotransposon Tf1 in the genome of Schizosaccharomyces pombe and obtained the first profile of integration with frequencies for each individual position. Integration levels at individual nucleotides varied over two orders of magnitude and revealed that sequence recognition plays a key role in positioning integration. The serial number system is a general method that can be applied to determine precise integration maps for retroviruses and gene therapy vectors.","doi":"10.1093/nar/gku534","authors":"Chatterjee AG, Esnault C, Guo Y, Hung S, McQueen PG, Levin HL","authors_abbrev":"Chatterjee AG et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-06-21","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11702950","title":"Phosphorylation of Mei2 and Ste11 by Pat1 kinase inhibits sexual differentiation via ubiquitin proteolysis and 14-3-3 protein in fission yeast.","citation":"Dev Cell 2001 Sep;1(3):389-99","abstract":"Fission yeast Pat1 kinase inhibits sexual differentiation by phosphorylating the meiotic inducer Mei2 and the transcription factor Ste11. Here, we show how Pat1 downregulates these proteins. Mei2 is degraded via a ubiquitin-proteasome pathway in a phosphorylation-dependent fashion. The E2 Ubc2 and the E3 Ubr1 are required for this proteolysis. In addition, Pat1 negatively regulates Ste11 via Rad24/14-3-3, thereby repressing mei2+ transcription. The Pat1 phosphorylation sites of Ste11 match the consensus recognition sequence for 14-3-3. Rad24 binds preferentially to phosphorylated Ste11, and this binding results in inhibition of the transcriptional activation capacity of Ste11. Overall, therefore, these results show that Pat1 coordinates concerted molecular mechanisms that govern the sexual differentiation developmental decision.","authors":"Kitamura K, Katayama S, Dhut S, Sato M, Watanabe Y, Yamamoto M, Toda T","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-11-13","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC19C7.02","SPAC8E11.02c","SPAC27D7.03c","SPBC32C12.02","SPBC337.08c","SPAC18B11.07c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:41064458","title":"The two coiled-coil domains of the fission yeast kinesin-6 Klp9 are required for motor tetramerization and spindle elongation.","citation":"MicroPubl Biol 2025;2025","abstract":"The fission yeast kinesin-6 Klp9 localizes to the spindle midzone at anaphase to produce sliding forces to elongate the bipolar spindle. In the absence of Klp9 , anaphase spindle elongation is attenuated by half its normal rate. Klp9 functions as a microtubule plus end-directed tetrameric motor. Tetramerization is the key to its microtubule sliding function, as tetramerization allows Klp9 to bind antiparallel microtubules at the midzone. The amino acid sequence of Klp9 indicates two alpha-helical coiled-coils domains CC1 and CC2, important for protein-protein interactions. We seeked the potential oligomerization states of Klp9 via its coiled-coils using AlphaFold3. AlphaFold predicted that CC1 can form dimers and together with CC2 can form tetramers. The different oligomeric states enabled precise experimental verifications. We measured Klp9 motor GFP intensity and anaphase spindle elongation rate for the full-length Klp9 , Klp9-deletion (Klp9Δ), and truncated Klp9 containing no coiled-coils, or only CC1, or both CC1 and CC2. The results indicate that: 1) GFP intensity increases with increasing oligomeric state, and 2) attenuated anaphase spindle velocity is restored only in the Klp9 truncation containing both CC1 and CC2. The experimental data are consistent with prediction, indicating that CC1 contributes to Klp9 dimerization, and that CC1 and CC2 together contribute to Klp9 tetramerization.","doi":"10.17912/micropub.biology.001829","authors":"Nguyen MT, Ji L, Tran PT","authors_abbrev":"Nguyen MT et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-10-09","publication_year":"2025","canto_session_key":"27b18d51126494b9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-09 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21389117","title":"Mes1 controls the meiosis I to meiosis II transition by distinctly regulating the anaphase-promoting complex/cyclosome coactivators Fzr1/Mfr1 and Slp1 in fission yeast.","citation":"Mol Biol Cell 2011 May;22(9):1486-94","abstract":"Meiosis is a specialized form of cell division generating haploid gametes and is dependent upon protein ubiquitylation by the anaphase-promoting complex/cyclosome (APC/C). Accurate control of the APC/C during meiosis is important in all eukaryotic cells and is in part regulated by the association of coactivators and inhibitors. We previously showed that the fission yeast meiosis-specific protein Mes1 binds to a coactivator and inhibits APC/C; however, regulation of the Mes1-mediated APC/C inhibition remains elusive. Here we show how Mes1 distinctively regulates different forms of the APC/C. We study all the coactivators present in the yeast genome and find that only Slp1/Cdc20 is essential for meiosis I progression. However, Fzr1/Mfr1 is a critical target for Mes1 inhibition because fzr1Δ completely rescues the defect on the meiosis II entry in mes1Δ cells. Furthermore, cell-free studies suggest that Mes1 behaves as a pseudosubstrate for Fzr1/Mfr1 but works as a competitive substrate for Slp1. Intriguingly, mutations in the D-box or KEN-box of Mes1 increase its recognition as a substrate by Fzr1, but not by Slp1. Thus Mes1 interacts with two coactivators in a different way to control the activity of the APC/C required for the meiosis I/meiosis II transition.","doi":"10.1091/mbc.E10-09-0774","authors":"Kimata Y, Kitamura K, Fenner N, Yamano H","authors_abbrev":"Kimata Y et al.","pubmed_publication_date":"May 2011","pubmed_entrez_date":"2011-03-11","publication_year":"2011","canto_session_key":"2e22c541f5e9e87c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-07 17:51:04","canto_approved_date":"2024-04-03 12:20:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-25 16:18:18","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":45,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5D6.08c","SPAC27E2.05","SPBC119.02","SPCC1259.15c","SPAC343.03","SPBC582.03","SPAC19G12.01c","SPBC14C8.01c","SPAC144.13c","SPCC1620.04c","SPBC2D10.20","SPAC13G6.08","SPBC1198.12","SPAC821.08c"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2017-02-07"},{"uniquename":"PMID:8662192","title":"The distance-dependence of the fission yeast ade6-M26 marker effect in two-factor crosses.","citation":"Curr Genet 1996 May;29(6):530-6","abstract":"Random spore analysis of crosses between a strain bearing the ade6-M26 hotspot mutation and strains bearing other ade6 mutations was performed. Recombinant prototroph frequencies increase with increasing distance from M26 for mutations both 5' and 3' of M26. Maximum prototroph frequencies are obtained for mutations lying more than 700 nucleotides downstream from M26. Similar results are obtained for crosses with the ade6-M375 control mutation, but the prototroph frequencies are lower. The factor of stimulation of recombination by M26 as compared to the M375 control (M26 marker effect) also displays distance-dependence. These results are discussed in the context of the mechanism of M26 recombination, as well as in relation to recombination initiation, hybrid DNA formation, and mismatch repair at ade6. Keywords Conversion middle dot M26 hotspot middle dot Recombination middle dot Schizosaccharomyces pombe","authors":"Zahn-Zabal M, Kohli J","authors_abbrev":"Zahn-Zabal M et al.","pubmed_publication_date":"May 1996","pubmed_entrez_date":"1996-05-01","publication_year":"1996","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20044953","title":"Aspartyl aminopeptidase of Schizosaccharomyces pombe has a molecular chaperone function.","citation":"BMB Rep 2009 Dec 31;42(12):812-6","abstract":"To screen chaperone proteins from Schizosaccharomyce pombe (S. pombe), we prepared recombinant citrate synthase of the fission yeast as a substrate of anti-aggregation assay. Purified recombinant citrate synthase showed citrate synthase activity and was suitable for the substrate of chaperone assay. Several heat stable proteins including aspartyl aminopeptidase (AAP) for candidates of chaperone were screened from the supernatant fraction of heat-treated crude extract of S. pombe. The purified AAP migrated as a single band of 47 kDa on SDS-polyacrylamide gel electrophoresis. The native size of AAP was estimated as 200 kDa by a HPLC gel permeation chromatography. This enzyme can remove the aspartyl residue at N-terminus of angiotensin I. In addition, AAP showed the heat stability and protected the aggregation of citrate synthase caused by thermal denaturation. This study showed that S. pombe AAP is a moonlight protein that has aspartyl aminopeptidase and chaperone activities.","authors":"Lee S, Kim JS, Yun CH, Chae HZ, Kim K","authors_abbrev":"Lee S et al.","pubmed_publication_date":"31 Dec 2009","pubmed_entrez_date":"2010-01-05","publication_year":"2009","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.02","SPAC6C3.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"GO_REF:0000033","title":"Annotation inferences using phylogenetic trees","abstract":"The Phylogenetic ANnotation using Gene Ontology (PAN-GO) method annotates evolutionary trees from the PANTHER database with GO terms describing molecular function, biological process and cellular component. The GO terms are manually selected by a curator and used to annotate ancestral genes in the phylogenetic tree using the evidence code IBA (Inferred from Biological Ancestor). All supporting annotations must be based on experimental data from the scientific literature. The PAN-GO annotations are fully traceable from the data in the 'with/from' column of the annotation, which provides the PANTHER node ID (PTN) from which the annotation is derived, as well as all descendants sequences that support the annotation of the ancestral node. ","authors":"Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul 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Regulation of Origin Firing by Mrc1 through Interaction with Hsk1 Kinase.","citation":"Mol Cell Biol 2017 Apr 01;37(7)","abstract":"Mrc1 is a conserved checkpoint mediator protein that transduces the replication stress signal to the downstream effector kinase. The loss of  mrc1  checkpoint activity results in the aberrant activation of late/dormant origins in the presence of hydroxyurea. Mrc1 was also suggested to regulate orders of early origin firing in a checkpoint-independent manner, but its mechanism was unknown. Here we identify HBS (Hsk1 bypass segment) on Mrc1. An Δ HBS  mutant does not activate late/dormant origin firing in the presence of hydroxyurea but causes the precocious and enhanced activation of weak early-firing origins during normal S-phase progression and bypasses the requirement for Hsk1 for growth. This may be caused by the disruption of intramolecular binding between HBS and NTHBS (N-terminal target of HBS). Hsk1 binds to Mrc1 through HBS and phosphorylates a segment adjacent to NTHBS, disrupting the intramolecular interaction. We propose that Mrc1 exerts a \"brake\" on initiation (through intramolecular interactions) and that this brake can be released (upon the loss of intramolecular interactions) by either the Hsk1-mediated phosphorylation of Mrc1 or the deletion of HBS (or a phosphomimic mutation of putative Hsk1 target serine/threonine), which can bypass the function of Hsk1 for growth. The brake mechanism may explain the checkpoint-independent regulation of early origin firing in fission yeast.","doi":"10.1128/MCB.00355-16","authors":"Matsumoto S, Kanoh Y, Shimmoto M, Hayano M, Ueda K, Fukatsu R, Kakusho N, Masai H","authors_abbrev":"Matsumoto S et al.","pubmed_publication_date":"01 Apr 2017","pubmed_entrez_date":"2017-01-11","publication_year":"2017","canto_session_key":"6afd178508832e2f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-01-12 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC694.06c","SPBC776.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:17207637","title":"Yeast apoptosis--from genes to pathways.","citation":"Semin Cancer Biol 2007 Apr;17(2):112-21","abstract":"Yeast are eukaryotic unicellular organisms that are easy to cultivate and offer a wide spectrum of genetic and cytological tools for research. Yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe have successfully been used as models for human cell division cycle. Stress conditions, cellular ageing, failed mating, certain mutations or heterologous expression of proapoptotic genes induce yeast cell death with the characteristic markers of apoptosis. Several crucial regulators of apoptosis are conserved between metazoans and yeast. This simple model organism offers the possibility to identify conserved and new components of the apoptotic machinery and to elucidate the regulatory pathways beyond.","authors":"Fröhlich KU, Fussi H, Ruckenstuhl C","authors_abbrev":"Fröhlich KU et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-01-09","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20066076","title":"Shaping fission yeast with microtubules.","citation":"Cold Spring Harb Perspect Biol 2009 Jul;1(1):a001347","abstract":"For cell morphogenesis, the cell must establish distinct spatial domains at specified locations at the cell surface. Here, we review the molecular mechanisms of cell polarity in the fission yeast Schizosaccharomyces pombe. These are simple rod-shaped cells that form cortical domains at cell tips for cell growth and at the cell middle for cytokinesis. In both cases, microtubule-based systems help to shape the cell by breaking symmetry, providing endogenous spatial cues to position these sites. The plus ends of dynamic microtubules deliver polarity factors to the cell tips, leading to local activation of the GTPase cdc42p and the actin assembly machinery. Microtubule bundles contribute to positioning the division plane through the nucleus and the cytokinesis factor mid1p. Recent advances illustrate how the spatial and temporal regulation of cell polarization integrates many elements, including historical landmarks, positive and negative controls, and competition between pathways.","doi":"10.1101/cshperspect.a001347","authors":"Chang F, Martin SG","authors_abbrev":"Chang F et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2010-01-13","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19587778","title":"The Schizosaccharomyces pombe checkpoint kinases Chk1 and Cds1 are important for cell survival in response to cisplatin.","citation":"PLoS One 2009 Jul 09;4(7):e6181","abstract":"DNA damage checkpoints insure that the integrity of genomic DNA is faithfully maintained throughout the eukaryotic cell cycle. In the presence of damaged DNA, checkpoints are triggered to delay cell cycle progression to allow for DNA repair. In fission yeast, the kinases Chk1 and Cds1 are major components of these DNA damage checkpoint pathways. Both Chk1 and Cds1 are important for viability in the presence of several DNA damaging agents. In this study we hypothesized that Chk1 and Cds1 play a vital role in fission yeast cells ability to survive exposure to the DNA damaging agent cisplatin. Cisplatin is a potent chemotherapeutic drug that interacts with DNA and causes both inter- and intra-strand DNA cross-links.\nHere, we demonstrated that treatment with cisplatin in fission yeast causes a Chk1-dependent DNA damage signal. chk1(-) cells were sensitive to cisplatin and Chk1 was phosphorylated in response to cisplatin treatment. We also showed that a Chk1-dependent DNA damage checkpoint pathway is activated in a dose-dependent fashion in cells challenged with cisplatin. Furthermore the Cds1 checkpoint kinase was also important for viability in cisplatin challenged cells. In cds1(-) cells, cisplatin treatment reduced cell viability and this phenotype was exacerbated in a chk1(-)/cds1(-) background.\nThus, we conclude that the concerted effort of both major checkpoint kinases in fission yeast, Chk1 and Cds1, protect cells from cisplatin induced DNA damage. These observations are significant because they suggest that various classes of inter-strand crosslinking agents may generate slightly different lesions as work by others did not observe loss of viability in cds1(-) cells treated with other crosslinking agents like nitrogen mustard.","doi":"10.1371/journal.pone.0006181","authors":"Paparatto D, Fletcher D, Piwowar K, Baldino K, Morel C, Dunaway S","authors_abbrev":"Paparatto D et al.","pubmed_publication_date":"09 Jul 2009","pubmed_entrez_date":"2009-07-10","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8056332","title":"The mating-type region of Schizosaccharomyces pombe contains an essential gene encoding a protein homologous to human modulators of HIV transactivation.","citation":"Gene 1994 Aug 05;145(2):205-10","abstract":"In Schizosaccharomyces pombe, an intrachromosomal crossover between the mating type (MT) expression locus and one of the silent donor cassettes is lethal due to the loss of the intervening L region. The region contains one essential gene, let1. This gene was cloned and sequenced. The deduced amino acid (aa) sequence of let1 shows extensive homologies with SUG1 from Saccharomyces cerevisiae. Significant homologies were also found with the human HIV transactivation modulators, MSS1 and TBP-1, as well as with subunit 4 of the mammalian 26 S protease. The data indicate that let1 is a member of a recently defined multigene family of ATPases.","authors":"Michael H, Schmidt H, Fleck O, Gutz H, Liedtke C, Lorentz A, Ostermann K","authors_abbrev":"Michael H et al.","pubmed_publication_date":"05 Aug 1994","pubmed_entrez_date":"1994-08-05","publication_year":"1994","canto_session_key":"ee6d36bd4958a47b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-06-12 18:19:48","canto_approved_date":"2024-06-12 18:19:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 17:03:14","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC23G7.12c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2024-06-12"},{"uniquename":"PMID:23478021","title":"Replication fork stability is essential for the maintenance of centromere integrity in the absence of heterochromatin.","citation":"Cell Rep 2013 Mar 28;3(3):638-45","abstract":"The centromere of many eukaryotes contains highly repetitive sequences marked by methylation of histone H3K9 by Clr4(KMT1). This recruits multiple heterochromatin proteins, including Swi6 and Chp1, to form a rigid centromere and ensure accurate chromosome segregation. In the absence of heterochromatin, cells show an increased rate of recombination in the centromere, as well as chromosome loss. These defects are severely aggravated by loss of replication fork stability. Thus, heterochromatin proteins and replication fork protection mechanisms work in concert to prevent abnormal recombination, preserve centromere integrity, and ensure faithful chromosome segregation.","doi":"10.1016/j.celrep.2013.02.007","authors":"Li PC, Petreaca RC, Jensen A, Yuan JP, Green MD, Forsburg SL","authors_abbrev":"Li PC et al.","pubmed_publication_date":"28 Mar 2013","pubmed_entrez_date":"2013-03-13","publication_year":"2013","canto_session_key":"c10e17dc5e141789","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.13c","SPCC18B5.11c","SPAC694.06c","SPAC664.01c","SPCC4G3.05c","SPAC18G6.02c","SPBC428.08c","SPAC644.14c"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:20214890","title":"A novel yeast cell-based screen identifies flavone as a tankyrase inhibitor.","citation":"Biochem Biophys Res Commun 2010 Apr 09;394(3):569-73","abstract":"The telomere-associated protein tankyrase 1 is a poly(ADP-ribose) polymerase and is considered to be a promising target for cancer therapy, especially for BRCA-associated cancers. However, an efficient assay system for inhibitor screening has not been established, mainly due to the difficulty of efficient preparation of the enzyme and its substrate. Here, we report a cell-based assay system for detecting inhibitory activity against tankyrase 1. We found that overexpression of the human tankyrase 1 gene causes a growth defect in the fission yeast Schizosaccharomyces pombe. Chemicals that restore the growth defect phenotype can be identified as potential tankyrase 1 inhibitors. We performed a high-throughput screen using this system, and identified flavone as a compound that restores the growth of yeast cells overexpressing tankyrase 1. Indeed, flavone inhibited poly(ADP-ribosyl)ation of proteins caused by overexpression of tankyrase 1 in yeast cells. This system allows rapid identification of inhibitory activity against tankyrase 1 and is amenable to high-throughput screening using robotics.","doi":"10.1016/j.bbrc.2010.03.021","authors":"Yashiroda Y, Okamoto R, Hatsugai K, Takemoto Y, Goshima N, Saito T, Hamamoto M, Sugimoto Y, Osada H, Seimiya H, Yoshida M","authors_abbrev":"Yashiroda Y et al.","pubmed_publication_date":"09 Apr 2010","pubmed_entrez_date":"2010-03-11","publication_year":"2010","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22464192","title":"Ribonucleotide reductase activity is coupled to DNA synthesis via proliferating cell nuclear antigen.","citation":"Curr Biol 2012 Apr 24;22(8):720-6","abstract":"Synthesis of deoxynucleoside triphosphates (dNTPs) is required for both DNA replication and DNA repair and is catalyzed by ribonucleotide reductases (RNR), which convert ribonucleotides to their deoxy forms [1, 2]. Maintaining the correct levels of dNTPs for DNA synthesis is important for minimizing the mutation rate [3-7], and this is achieved by tight regulation of RNR [2, 8, 9]. In fission yeast, RNR is regulated in part by a small protein inhibitor, Spd1, which is degraded in S phase and after DNA damage to allow upregulation of dNTP supply [10-12]. Spd1 degradation is mediated by the activity of the CRL4(Cdt2) ubiquitin ligase complex [5, 13, 14]. This has been reported to be dependent on modulation of Cdt2 levels, which are cell cycle regulated, peaking in S phase, and which also increase after DNA damage in a checkpoint-dependent manner [7, 13]. We show here that Cdt2 level fluctuations are not sufficient to regulate Spd1 proteolysis and that the key step in this event is the interaction of Spd1 with the polymerase processivity factor proliferating cell nuclear antigen (PCNA), complexed onto DNA. This mechanism thus provides a direct link between DNA synthesis and RNR regulation.","doi":"10.1016/j.cub.2012.02.070","authors":"Salguero I, Guarino E, Shepherd ME, Deegan TD, Havens CG, MacNeill SA, Walter JC, Kearsey SE","authors_abbrev":"Salguero I et al.","pubmed_publication_date":"24 Apr 2012","pubmed_entrez_date":"2012-04-03","publication_year":"2012","canto_session_key":"b2c7617cf382c042","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05","SPBC16D10.09","SPAC29B12.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11861754","title":"The COP9 signalosome: at the interface between signal transduction and ubiquitin-dependent proteolysis.","citation":"J Cell Sci 2002 Feb 01;115(Pt 3):467-73","abstract":"Recently the COP9 signalosome (CSN) has become a focus of interest for many researchers, because of its function at the interface between signal transduction and ubiquitin-dependent proteolysis. It is required for the proper progression of the cell cycle in Schizosaccharomyces pombe and is essential for development in plants and Drosophila. However, its function in mammalian cells remains obscure. Although the CSN shares structural similarities with the 26S proteasome lid complex (LID), its functions seem to be different from that of the LID. A variety of CSN-specific protein-protein interactions have been described in mammalian cells. However, it is currently unclear how many reflect true functions of the complex. Two activities associated with the CSN have been identified so far: a protein kinase and a deneddylase. The CSN-associated kinase phosphorylates transcription factors, which determines their stability towards the ubiquitin system. The associated deneddylase regulates the activity of specific SCF E3 ubiquitin ligases. The CSN thus appears to be a platform connecting signalling with proteolysis.","authors":"Bech-Otschir D, Seeger M, Dubiel W","authors_abbrev":"Bech-Otschir D et al.","pubmed_publication_date":"01 Feb 2002","pubmed_entrez_date":"2002-02-28","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4684596","title":"Effect of 2-deoxy-D-glucose on growth and cell walls of Schizosaccharomyces pombe 972h.","citation":"Arch Mikrobiol 1973;88(4):257-72","abstract":"","authors":"Poole RK, Lloyd D","authors_abbrev":"Poole RK et al.","pubmed_publication_date":"1973","pubmed_entrez_date":"1973-01-01","publication_year":"1973","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22778552","title":"Yeast and the AIDS virus: the odd couple.","citation":"J Biomed Biotechnol 2012;2012:549020","abstract":"Despite being simple eukaryotic organisms, the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe have been widely used as a model to study human pathologies and the replication of human, animal, and plant viruses, as well as the function of individual viral proteins. The complete genome of S. cerevisiae was the first of eukaryotic origin to be sequenced and contains about 6,000 genes. More than 75% of the genes have an assigned function, while more than 40% share conserved sequences with known or predicted human genes. This strong homology has allowed the function of human orthologs to be unveiled starting from the data obtained in yeast. RNA plant viruses were the first to be studied in yeast. In this paper, we focus on the use of the yeast model to study the function of the proteins of human immunodeficiency virus type 1 (HIV-1) and the search for its cellular partners. This human retrovirus is the cause of AIDS. The WHO estimates that there are 33.4 million people worldwide living with HIV/AIDS, with 2.7 million new HIV infections per year and 2.0 million annual deaths due to AIDS. Current therapy is able to control the disease but there is no permanent cure or a vaccine. By using yeast, it is possible to dissect the function of some HIV-1 proteins and discover new cellular factors common to this simple cell and humans that may become potential therapeutic targets, leading to a long-lasting treatment for AIDS.","doi":"10.1155/2012/549020","authors":"Andréola ML, Litvak S","authors_abbrev":"Andréola ML et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-07-11","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42212438","title":"Multiple ammonium transporters in fission yeast are coordinated by transcriptional and localization regulation in response to nitrogen starvation.","citation":"J Cell Sci 2026 May 29;","abstract":"Ammonium is a preferred nitrogen source for microorganisms. We investigated the regulation of ammonium transporters Amt1, Amt2, and Amt3 in the fission yeast Schizosaccharomyces pombe. Expression of the amt1+ gene increases under nitrogen starvation as well as in the TORC1-deficient mutant tor2-287, suggesting the negative regulation of amt1+ by TORC1. This regulation depends on the GATA transcription factor Gaf1, whose phosphorylation is regulated by Ppe1 and PP2A phosphatases. Ppe1 is required for the nuclear accumulation of Gaf1, partly contributing to the controlled expression of amt1+. On the other hand, PP2A phosphatase is essential for the amt1+ induction upon starvation, indicating distinct roles for Ppe1 and PP2A in Gaf1 regulation. Nitrogen starvation also promotes the plasma membrane translocation of Amt1 and Amt2 in a manner dependent on the Tsc-Rhb1 pathway. Intriguingly, the amt1▵ amt2▵ tsc▵ mutant is more sensitive to low-ammonium conditions than the amt1▵ amt2▵ amt3▵ triple mutant. Thus, there may be an unidentified ammonium transporter whose plasma membrane localization is also dependent on the Tsc-Rhb1 pathway.","doi":"10.1242/jcs.264532","authors":"Nakase Y, Lee NS, Wei ATC, Shibatani A, Yomogita T, Morozumi Y, Watanabe D, Takagi H, Shiozaki K","authors_abbrev":"Nakase Y et al.","pubmed_publication_date":"29 May 2026","pubmed_entrez_date":"2026-05-29","publication_year":"2026","canto_session_key":"842240c23ebd994b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-05-29 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1902.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25720772","title":"Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1.","citation":"Mol Cell Proteomics 2015 May;14(5):1275-87","abstract":"Complex phosphorylation-dependent signaling networks underlie the coordination of cellular growth and division. In the fission yeast Schizosaccharomyces pombe, the Dual specificity tyrosine-(Y)-phosphorylation regulated kinase (DYRK) family protein kinase Pom1 regulates cell cycle progression through the mitotic inducer Cdr2 and controls cell polarity through unknown targets. Here, we sought to determine the phosphorylation targets of Pom1 kinase activity by SILAC-based phosphoproteomics. We defined a set of high-confidence Pom1 targets that were enriched for cytoskeletal and cell growth functions. Cdr2 was the only cell cycle target of Pom1 kinase activity that we identified in cells. Mutation of Pom1-dependent phosphorylation sites in the C terminus of Cdr2 inhibited mitotic entry but did not impair Cdr2 localization. In addition, we found that Pom1 phosphorylated multiple substrates that function in polarized cell growth, including Tea4, Mod5, Pal1, the Rho GAP Rga7, and the Arf GEF Syt22. Purified Pom1 phosphorylated these cell polarity targets in vitro, confirming that they are direct substrates of Pom1 kinase activity and likely contribute to regulation of polarized growth by Pom1. Our study demonstrates that Pom1 acts in a linear pathway to control cell cycle progression while regulating a complex network of cell growth targets.","doi":"10.1074/mcp.M114.045245","authors":"Kettenbach AN, Deng L, Wu Y, Baldissard S, Adamo ME, Gerber SA, Moseley JB","authors_abbrev":"Kettenbach AN et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-02-28","publication_year":"2015","canto_session_key":"063efc493e59cfc2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-05-03 20:59:26","canto_approved_date":"2022-03-02 12:32:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-30 17:15:02","canto_added_date":"2015-03-01 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":49,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia 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,"SPCC1672.11c","SPAC17G6.16c","SPCC622.15c","SPAP14E8.02","SPAC823.03","SPAPB1E7.07","SPAC1782.11","SPBC12C2.05c","SPBC27B12.04c","SPBC25D12.05","SPAC23H4.15","SPAC3A12.11c","SPAC24H6.11c"],"gene_count":2120,"ltp_gene_count":11,"approved_date":"2017-05-03"},{"uniquename":"PMID:36951016","title":"The cell cycle and cell size influence the rates of global cellular translation and transcription in fission yeast.","citation":"EMBO J 2023 May 02;42(9):e113333","abstract":"How the production of biomass is controlled as cells increase in size and proceed through the cell cycle events is important for understanding the regulation of global cellular growth. This has been studied for decades but has not yielded consistent results, probably due to perturbations induced by the synchronisation methods used in most previous studies. To avoid this problem, we have developed a system to analyse unperturbed exponentially growing populations of fission yeast cells. We generated thousands of fixed single-cell measurements of cell size, cell cycle stage and the levels of global cellular translation and transcription. We show that translation scales with size, and additionally, increases at late S-phase/early G2 and early in mitosis and decreases later in mitosis, suggesting that cell cycle controls are also operative over global cellular translation. Transcription increases with both size and the amount of DNA, suggesting that the level of transcription of a cell may be the result of a dynamic equilibrium between the number of RNA polymerases associating and disassociating from DNA.","doi":"10.15252/embj.2022113333","authors":"Basier C, Nurse P","authors_abbrev":"Basier C et al.","pubmed_publication_date":"02 May 2023","pubmed_entrez_date":"2023-03-23","publication_year":"2023","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2023-03-24 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000111","title":"Gene Ontology annotations Inferred by Curator (IC) using at least one Inferred by Sequence Similarity (ISS) annotation to support the inference","abstract":"The Gene Ontology Consortium uses the IC (Inferred by Curator; ECO:0000305) evidence code when assignment of a GO term cannot be supported by direct experimental or sequence-based evidence, but can, based on a curator’s biological knowledge, be reasonably inferred from existing GO annotations to the same gene/gene product.  Use of the IC evidence code with GO_REF:0000111 indicates that a curator inferred the GO term based on at least one supporting annotation with an 'Inferred from Sequence Similarity' (ISS; ECO:0000250) evidence code.  Note that additional supporting annotations may be experimentally evidenced. When using GO_REF:0000111, the 'with/from' field must contain all GO identifiers used as supporting annotations.","authors":"TBD","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPATRNAALA.05","SPAC25B8.10","SPCC1259.04","SPCC550.12","SPBC3B9.06c","SPAC11D3.13","SPAC3G9.02","SPCTRNAARG.11","SPBTRNAPHE.03","SPBC1347.08c","SPCC622.13c","SPCTRNAASP.06","SPMITTRNAHIS.01","SPBC776.10c","SPAC1F7.06","SPAC732.01","SPBC19F5.03","SPBC36.05c","SPAC57A7.07c","SPMITTRNAVAL.01","SPBC16A3.13","SPBC13E7.05","SPCC16A11.09c","SPCC16A11.16c","SPCC962.01","SPBC1348.12","SPATRNACYS.03","SPAC11H11.04","SPAC24C9.09","SPAC31A2.09c","SPBC1105.11c","SPBTRNAGLY.08","SPBC1539.05","SPAC4G9.06c","SPCC1739.03","SPAC13G6.01c","SPBTRNAASP.05","SPAC19D5.11c","SPCC737.02c","SPAC17G8.03c","SPBTRNAASN.04","SPCC1259.10","SPBC27B12.01c","SPBC28F2.10c","SPBP16F5.02","SPBC1A4.03c","SPBTRNAILE.07","SPAC15E1.07c","SPAC27E2.01","SPBTRNAASN.01","SPCC18.13","SPAC630.10","SPAP8A3.11c","SPBC32H8.12c","SPAC222.07c","SPAC23A1.02c","SPMITTRNAASN.01","SPBC428.02c","SPAC17H9.17c","SPAC16E8.17c","SPAC823.12","SPBC1604.15","SPAC1002.13c","SPAC19D5.06c","SPAC24C9.06c","SPAC13G6.11c","SPAC227.16c","SPBC1921.07c","SPBC25H2.11c","SPAC3G9.16c","SPCC576.13","SPCC1450.10c","SPAC3G9.11c","SPBTRNALEU.08","SPBC17D1.04","SPBC25D12.04","SPBTRNAHIS.01","SPCC663.13c","SPAC11H11.05c","SPBTRNALEU.07","SPRRNA.26","SPCC550.10","SPAC4D7.10c","SPCC4G3.05c","SPAC2F3.13c","SPCC70.05c","SPAC23C4.14","SPBC18H10.06c","SPBC24C6.03","SPCC736.06","SPBP4H10.11c","SPCTRNAASN.06","SPCC790.02","SPAC22E12.19","SPBC56F2.03","SPAPB1E7.07","SPCC18.08","SPAC13F5.06c","SPAC24C9.16c","SPBC106.12c","SPBP23A10.08","SPMITTRNASER.02","SPAC6B12.04c","SPBTRNALEU.05","SPAC227.18","SPRRNA.13","SPAC1952.05","SPBC6B1.02","SPAC17A2.05","SPBC8E4.03","SPAC17G8.06c","SPCTRNAMET.07","SPAC13F5.03c","SPAC1565.01","SPMITTRNATHR.01","SPCTRNAVAL.12","SPBC19C7.08c","SPAC750.02c","SPBC1604.02c","SPBC19G7.19","SPCC285.17","SPBP4H10.12","SPAC23G3.04","SPBC3B9.12","SPAC17C9.06","SPBC557.04","SPAC25B8.02","SPAC8F11.03","SPBC16E9.09c","SPCC1235.13","SPATRNAPRO.03","SPATRNAASP.01","SPAC22F3.12c","SPAC227.08c","SPCC1393.02c","SPAC1783.01","SPBC16A3.06","SPATRNAVAL.01","SPCTRNAARG.09","SPAC4G8.08","SPAC17C9.01c","SPBC106.17c","SPCC1235.10c","SPBC6B1.12c","SPBC1677.03c","SPAP8A3.07c","SPBC1289.05c","SPRRNA.32","SPRRNA.50","SPAC1556.01c","SPAC10F6.17c","SPBC31F10.07","SPAC7D4.10","SPCC285.04","SPCP31B10.06","SPBC19C2.01","SPBTRNAHIS.02","SPBC4.02c","SPAC27F1.06c","SPCC1682.13","SPAC31G5.04","SPAC14C4.12c","SPATRNAILE.01","SPBC1711.10c","SPBC3B8.01c","SPCTRNATHR.10","SPAC12G12.10","SPCTRNATHR.08","SPCC895.03c","SPBC660.15","SPAC14C4.11","SPMITTRNAMET.02","SPBC16A3.10","SPBC21C3.02c","SPCC188.04c","SPAC6B12.12","SPBC887.17","SPCC338.13","SPBC577.04","SPCC1795.08c","SPBC13G1.11","SPATRNAPRO.02","SPAC21E11.04","SPBC16D10.02","SPCC1281.05","SPCTRNAARG.08","SPAC17G6.10","SPBTRNASER.06","SPAC222.12c","SPCC132.04c","SPBTRNAASN.02","SPAC6G10.05c","SPBC685.04c","SPAC15A10.06","SPCC24B10.05","SPMIT.10","SPRRNA.18","SPBTRNAGLY.04","SPMITTRNAASP.01","SPBC106.09","SPATRNAILE.03","SPBC543.10","SPMITTRNAPRO.01","SPCC364.05","SPAC11E3.08c","SPAC167.02","SPCC13B11.01","SPBTRNAALA.09","SPBC18H10.20c","SPCC11E10.04","SPAC1565.08","SPBTRNAILE.05","SPAC17A5.02c","SPCC962.05","SPCC1223.09","SPAC23G3.09","SPAC644.18c","SPMITTRNALYS.01","SPRRNA.16","SPAC26A3.12c","SPATRNALYS.02","SPAC20G4.03c","SPMIT.07","SPAC8C9.17c","SPAC343.05","SPBC776.18c","SPBC8D2.04","SPBC800.02","SPCTRNALYS.11","SPAC22G7.04","SPBTRNATRP.03","SPAC977.12","SPBC26H8.11c","SPBC1703.15c","SPAC23C11.09","SPBC1826.01c","SPRRNA.52","SPAC1093.02","SPAC15A10.02","SPBPB21E7.09","SPCC18B5.10c","SPAC1556.07","SPCC417.02","SPBTRNAGLN.04","SPBC15D4.09c","SPAC10F6.08c","SPAC29B12.06c","SPBC11G11.04","SPBC8D2.07c","SPCC1919.03c","SPCTRNAILE.09","SPBTRNALYS.09","SPAC25G10.07c","SPBC776.02c","SPBTRNAILE.06","SPAC186.03","SPBC1685.16","SPAC637.05c","SPCTRNAVAL.10","SPBTRNAALA.08","SPATRNAGLU.03","SPBC1198.10c","SPBC947.09","SPAC139.05","SPBC428.06c","SPATRNAMET.02","SPAC23C11.15","SPBTRNAALA.11","SPAC23C11.13c","SPCC1919.10c","SPCP1E11.02","SPATRNASER.04","SPAC821.13c","SPAC17A5.08","SPBP16F5.03c","SPMIT.04","SPCC645.05c","SPBC14C8.07c","SPAC4F8.07c","SPAC30C2.02","SPATRNALEU.01","SPAP11E10.02c","SPBC29A3.08","SPBC27.02c","SPBC1773.17c","SPAC2F7.07c","SPAC17H9.12c","SPCC613.10","SPAC19B12.03","SPAC31A2.15c","SPRRNA.35","SPCC63.10c","SPAC186.09","SPAC24H6.10c","SPCTRNASER.13","SPAC6B12.06c","SPAC732.02c","SPAC29A4.04c","SPATRNATHR.02","SPCC1223.15c","SPBC30B4.01c","SPAC26H5.13c","SPAC1D4.14","SPAC6G9.03c","SPBC409.09c","SPCC4B3.08","SPCC1450.02","SPAC22E12.11c","SPRRNA.30","SPAC8C9.03","SPAC1F7.09c","SPCC548.06c","SPAC26H5.07c","SPAC589.04","SPCTRNALYS.10","SPAC1556.02c","SPAC1002.04c","SPBTRNALEU.09","SPAC25B8.14","SPBTRNATRP.02","SPCC13B11.03c","SPCC1840.06","SPAC328.09","SPATRNAALA.06","SPBC27.06c","SPAC1071.06","SPBC1271.04c","SPAC1093.01","SPAC15A10.17","SPCC126.04c","SPAC23D3.09","SPBC27B12.13","SPBC16H5.06","SPBTRNAVAL.08","SPCC306.09c","SPBC10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"SPCC1259.07","SPAC16E8.02","SPCC18.01c","SPRRNA.28","SPAC343.15","SPCC5E4.05c","SPCC320.04c","SPAC3G9.04","SPCC757.03c","SPCTRNAVAL.11","SPBC11B10.03","SPAC23C4.13","SPCPB16A4.04c","SPAC3C7.01c","SPAC227.14","SPAC26F1.03","SPAC1F8.07c","SPRRNA.05","SPCTRNAGLN.05","SPATRNASER.02","SPBC577.12","SPBC1861.07","SPBC2F12.14c","SPBTRNASER.05","SPATRNALEU.04","SPBTRNAVAL.06","SPAC22H10.05c","SPATRNAILE.04","SPAC23H4.16c","SPAC24B11.08c","SPBC18A7.02c","SPCTRNASER.11","SPAC1687.03c","SPMIT.06","SPAC17D4.04","SPAC3G9.17","SPBC354.07c","SPAC12G12.04","SPAC767.01c","SPAC20G8.01","SPAC13A11.04c","SPAC30D11.05"],"gene_count":1068,"ltp_gene_count":0},{"uniquename":"PMID:17088292","title":"Diversity of tRNA genes in eukaryotes.","citation":"Nucleic Acids Res 2006;34(21):6137-46","abstract":"We compare the diversity of chromosomal-encoded transfer RNA (tRNA) genes from 11 eukaryotes as identified by tRNAScan-SE of their respective genomes. They include the budding and fission yeast, worm, fruit fly, fugu, chicken, dog, rat, mouse, chimp and human. The number of tRNA genes are between 170 and 570 and the number of tRNA isoacceptors range from 41 to 55. Unexpectedly, the number of tRNA genes having the same anticodon but different sequences elsewhere in the tRNA body (defined here as tRNA isodecoder genes) varies significantly (10-246). tRNA isodecoder genes allow up to 274 different tRNA species to be produced from 446 genes in humans, but only up to 51 from 275 genes in the budding yeast. The fraction of tRNA isodecoder genes among all tRNA genes increases across the phylogenetic spectrum. A large number of sequence differences in human tRNA isodecoder genes occurs in the internal promoter regions for RNA polymerase III. We also describe a systematic, ligation-based method to detect and quantify tRNA isodecoder molecules in human samples, and show differential expression of three tRNA isodecoders in six human tissues. The large number of tRNA isodecoder genes in eukaryotes suggests that tRNA function may be more diverse than previously appreciated.","authors":"Goodenbour JM, Pan T","authors_abbrev":"Goodenbour JM et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-11-08","publication_year":"2006","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4149272","title":"Oscillations of enzyme activities during the cell-cycle of a glucose-repressed fission-yeast Schizosaccharomyces pombe 972h-.","citation":"Biochem J 1973 Sep;136(1):195-207","abstract":"1. Increased specific activities of cytochrome c oxidase, catalase, succinate dehydrogenase, succinate-cytochrome c oxidoreductase, NADH-cytochrome c oxidoreductase and malate dehydrogenase were observed during glucose de-repression of Schizosaccharomyces pombe. 2. The cell-cycle of this organism was analysed by three different methods: (a) harvesting of cells at intervals from a synchronous culture, (b) separation of cells by rate-zonal centrifugation into different size classes and (c) separation of cells by isopycnic-zonal centrifugation into different density classes. 3. Measurement of enzyme activities during the cell-cycle showed that all the enzymes assayed [cytochrome c oxidase, catalase, acid p-nitrophenylphosphatase, NADH-dehydrogenase, NADH-cytochrome c oxidoreductase, NADPH-cytochrome c oxidoreductase, succinate dehydrogenase, malate dehydrogenase, isocitrate dehydrogenase (NADP) and fumarate hydratase] show periodic expression as ;peaks'. 4. Cytochrome c oxidase shows a single maximum at 0.67 of a cycle, whereas succinate dehydrogenase exhibits two maxima separated by 0.5 of a cell-cycle. 5. All other enzymes assayed showed two distinct maxima per cell-cycle; for catalase, malate dehydrogenase and NADPH-cytochrome c oxidoreductase there is the possibility of multiple fluctuations. 6. The single maximum of cytochrome c oxidase appears at a similar time in the cycle to one maximum of each of the other enzymes studied, except for NADH dehydrogenase. 7. These results are discussed with reference to previous observations on the expression of enzyme activities during the cell-cycle of yeasts.","authors":"Poole RK, Lloyd D","authors_abbrev":"Poole RK et al.","pubmed_publication_date":"Sep 1973","pubmed_entrez_date":"1973-09-01","publication_year":"1973","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000050","title":"Manual transfer of GO annotation data to genes by curator judgment of sequence model","abstract":"Transitive assignment of GO terms to a gene based on a curator's judgment of its match to a sequence model,such as a Pfam or InterPro entry, that has manually curated GO annotations, mappings to GO terms, or a description from which GO terms can be inferred. A statistical model of a sequence or group of sequences is used to make a prediction about the function of a protein or RNA. Annotations are created when a curator evaluates the results, using criteria that include excluding false positives and ensuring that the annotation is accurate for all matches. Statistical scores (such as e values and cutoff scores) and the functional specificity of the model may also be (but are not always) considered. Annotations resulting from the transfer of GO terms use the 'ISM' evidence code and include an accession for the model from which the annotation was projected in the 'with' field (column 8).","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC607.06c","SPCC645.06c","SPBC26H8.07c","SPRRNA.50","SPAC17G6.10","SPCTRNAGLY.10","SPATRNAVAL.01","SPCC63.13","SPAC4H3.01","SPBC17G9.12c","SPBTRNAARG.05","SPBC12D12.04c","SPATRNASER.04","SPBC30D10.15","SPBTRNATRP.02","SPAC11H11.03c","SPRRNA.52","SPAP32A8.03c","SPAC4A8.11c","SPRRNA.42","SPAPJ691.02","SPBC146.10","SPCTRNALYS.11","SPBC1348.08c","SPAC1002.13c","SPATRNAALA.01","SPBC18E5.01","SPCTRNAARG.11","SPMITTRNALYS.01","SPCC737.08","SPAPB2C8.01","SPMITTRNAVAL.01","SPBC1683.13c","SPAC5D6.04","SPAC227.19c","SPATRNAALA.05","SPMITTRNATYR.01","SPCTRNASER.09","SPBTRNAMET.06","SPRRNA.31","SPCTRNAHIS.04","SPAC1952.13","SPAC57A7.09","SPCTRNAPHE.04","SPATRNALYS.04","SPCC285.05","SPCC962.01","SPBC2G2.17c","SPBTRNATYR.04","SPBC25B2.03","SPAC22E12.19","SPBTRNAGLY.08","SPBC1289.15","SPAC11E3.05","SPCC1742.01","SPCTRNATHR.08","SPMITTRNASER.01","SPBTRNAGLY.04","SPAC11G7.02","SPRRNA.44","SPBTRNATHR.07","SPBC17D1.07c","SPCC736.13","SPBC1815.01","SPCC965.06","SPAC57A10.07","SPBTRNAASP.05","SPATRNAGLU.02","SPCC1795.08c","SPAPB15E9.01c","SPBC1105.12","SPBTRNAGLY.06","SPAC22A12.08c","SPBC19C7.06","SPATRNAALA.02","SPAC10F6.14c","SPRRNA.43","SPRRNA.17","SPAC12B10.16c","SPBPB21E7.07","SPATRNAALA.06","SPAC19A8.06","SPBC14F5.06","SPCTRNAGLU.10","SPBTRNAILE.06","SPMITTRNAILE.01","SPATRNAILE.03","SPCC306.02c","SPAC31G5.15","SPBTRNAPRO.07","SPRRNA.18","SPAC26A3.09c","SPCTRNATHR.09","SPATRNAPHE.02","SPBTRNAARG.07","SPCC553.12c","SPCTRNASER.11","SPBC18A7.01","SPAC26F1.01","SPBC947.04","SPAC1071.09c","SPRRNA.46","SPAC23C11.06c","SPBC17D11.03c","SPCTRNAGLN.05","SPCC297.05","SPBC1348.12","SPBC15C4.06c","SPAC17G8.14c","SPAC1039.07c","SPBC947.05c","SPCTRNAGLY.11","SPAC977.07c","SPAC1399.01c","SPCC285.09c","SPBP4H10.07","SPAC869.01","SPATRNAILE.04","SPRRNA.03","SPCC330.01c","SPCTRNAHIS.03","SPBTRNATRP.03","SPBC337.11","SPAC3F10.05c","SPBTRNAPRO.05","SPCC1919.11","SPCC330.11","SPAC1039.05c","SPRRNA.38","SPBP4H10.10","SPAC29E6.05c","SPBTRNAGLN.02","SPAC27D7.04","SPCC1827.03c","SPBTRNAILE.08","SPBC887.02","SPCC4B3.09c","SPCTRNAARG.08","SPAC1F5.09c","SPCC74.04","SPBC1706.03","SPAC2E1P5.02c","SPBTRNAILE.05","SPBTRNAARG.06","SPBTRNAALA.11","SPBTRNALYS.08","SPMITTRNALEU.02","SPRRNA.04","SPMITTRNALEU.01","SPCC18.01c","SPCTRNALEU.13","SPBC1105.17","SPBC21B10.08c","SPAC11D3.08c","SPATRNALEU.03","SPBC25B2.06c","SPCTRNAALA.12","SPATRNAARG.03","SPBTRNALEU.08","SPAC824.03c","SPBC21C3.03","SPCTRNAASN.06","SPMITTRNAASP.01","SPATRNAASP.01","SPBC1604.16c","SPBTRNALEU.07","SPCTRNAARG.09","SPCC1919.14c","SPATRNASER.01","SPCTRNAGLU.09","SPBC776.18c","SPATRNAILE.02","SPCTRNASER.13","SPCTRNAILE.09","SPBTRNAGLN.01","SPBC365.01","SPRRNA.10","SPCTRNAASN.05","SPBTRNAPRO.06","SPAC105.03c","SPAC14C4.04","SPCP31B10.02","SPCC550.04c","SPAC4A8.07c","SPRRNA.51","SPBC1271.01c","SPBC725.09c","SPAC1751.01c","SPATRNAILE.01","SPRRNA.37","SPATRNATHR.05","SPCC320.03","SPATRNATHR.04","SPAC750.01","SPCTRNASER.10","SPBTRNAMET.05","SPATRNACYS.03","SPAPB1A11.04c","SPRRNA.15","SPRRNA.49","SPAC11D3.04c","SPMITTRNATRP.01","SPMITTRNAMET.01","SPATRNACYS.01","SPAC26H5.11","SPRRNA.40","SPAC15A10.03c","SPAC3A12.03c","SPBC3H7.06c","SPAC186.01","SPCC794.04c","SPAC30.02c","SPAC23H3.10","SPCC1450.10c","SPCTRNAASP.06","SPRRNA.20","SPAC3H1.02c","SPRRNA.45","SPBC15C4.04c","SPATRNALEU.01","SPCTRNALYS.12","SPAC1F5.07c","SPAC1B9.02c","SPAC1039.01","SPBP22H7.05c","SPAC9.08c","SPBTRNATYR.03","SPBTRNALEU.09","SPATRNASER.02","SPBC23E6.05","SPAC3C7.05c","SPMITTRNACYS.01","SPMITTRNAGLU.01","SPAC13G6.10c","SPMIT.03","SPAC16A10.03c","SPATRNALEU.04","SPATRNAMET.01","SPCC31H12.06","SPCC584.13","SPCTRNALEU.12","SPAC30C2.06c","SPCTRNASER.07","SPBC1289.06c","SPAC29B12.13","SPAC821.05","SPBTRNAASN.01","SPBC359.04c","SPCC1259.01c","SPATRNAPRO.02","SPATRNAGLY.02","SPAC13C5.04","SPCC594.04c","SPBTRNAGLY.05","SPATRNALYS.02","SPBC3H7.14","SPAC27F1.05c","SPAC25B8.11","SPBTRNALEU.10","SPBC1703.06","SPAC3G6.03c","SPMITTRNAPRO.01","SPATRNALYS.05","SPCTRNAVAL.10","SPCC962.05","SPMITTRNAMET.02","SPBPB8B6.04c","SPAC167.05","SPRRNA.24","SPBC17G9.06c","SPCTRNAARG.10","SPAC589.09","SPAC3H1.11","SPATRNAGLU.01","SPATRNAGLU.03","SPBTRNAGLU.07","SPBTRNAASN.04","SPCC830.07c","SPBC1289.04c","SPBC1604.18c","SPBC428.07","SPAPB24D3.02c","SPRRNA.19","SPCC338.16","SPBC56F2.05c","SPCTRNAPRO.09","SPBC1271.07c","SPRRNA.06","SPAC19A8.05c","SPBTRNAGLY.07","SPBC28E12.06c","SPCTRNAMET.07","SPAC186.06","SPRRNA.35","SPBTRNAALA.09","SPMITTRNAHIS.01","SPATRNAALA.03","SPBC28F2.11","SPATRNAPRO.01","SPAC18G6.12c","SPRRNA.27","SPCC663.14c","SPAPB17E12.03","SPCTRNATHR.10","SPCTRNAGLN.06","SPATRNAALA.04","SPCTRNALEU.11","SPATRNAASP.02","SPBTRNAALA.07","SPATRNALEU.02","SPMITTRNAASN.01","SPATRNALYS.03","SPBC29A3.13","SPBC9B6.03","SPAC6F6.13c","SPCTRNAARG.13","SPAC11D3.03c","SPAC23A1.07","SPCTRNAVAL.09","SPBC16E9.11c","SPBC1348.09","SPAC31A2.10","SPRRNA.39","SPAC4G9.19","SPCTRNALYS.10","SPCC417.11c","SPAC1565.02c","SPBC25B2.10","SPBTRNASER.05","SPATRNALYS.01","SPBTRNAHIS.01","SPBTRNAVAL.05","SPCP31B10.06","SPCC1672.11c","SPBTRNAALA.08","SPBC651.11c","SPMITTRNAARG.02","SPCTRNAVAL.11","SPAC3H8.02","SPAPB1A10.07c","SPBTRNAALA.10","SPCTRNAARG.12","SPATRNASER.03","SPMITTRNAPHE.01","SPAC14C4.12c","SPCTRNASER.08","SPMITTRNATHR.01","SPMITTRNASER.02","SPAC16A10.01","SPRRNA.32","SPBC28E12.02","SPBC1718.02","SPAC977.14c","SPBC8E4.05c","SPAC16E8.09","SPATRNAVAL.04","SPBC13E7.02","SPBC365.13c","SPRRNA.41","SPBTRNAGLY.09","SPCTRNAASP.07","SPBC1711.05","SPRRNA.11","SPAC869.06c","SPAC144.08","SPCC18.04","SPAC23D3.01","SPAC1F7.11c","SPBTRNALYS.06","SPATRNATHR.02","SPCC970.03","SPCC757.05c","SPRRNA.48","SPATRNAPHE.01","SPAC7D4.12c","SPMITTRNAARG.01","SPBTRNATYR.02","SPBC16G5.17","SPBTRNAASP.04","SPBTRNAMET.04","SPRRNA.26","SPMITTRNAGLN.01","SPBC1773.03c","SPBTRNAGLY.03","SPBC530.11c","SPBC26H8.08c","SPATRNAPRO.03","SPAC1486.10","SPCC188.09c","SPBC2F12.07c","SPBC2G5.01","SPATRNAVAL.02","SPBC27B12.09c","SPBC8D2.04","SPAC2H10.01","SPCTRNAVAL.12","SPBTRNAVAL.06","SPRRNA.36","SPBTRNAGLU.08","SPAC26A3.10","SPAC16C9.01c","SPBTRNAGLN.04","SPAPB24D3.06c","SPAC12G12.01c","SPATRNAMET.02","SPBC16H5.14c","SPBTRNAGLU.05","SPAC25B8.01","SPATRNAVAL.03","SPATRNATHR.03","SPCC23B6.04c","SPCTRNAASP.05","SPAC144.05","SPBTRNATHR.06","SPAC1F3.04c","SPBC21D10.12","SPAC25H1.02","SPBC16H5.12c","SPBTRNAPHE.03","SPRRNA.34","SPBTRNALYS.07","SPBTRNAPRO.04","SPMITTRNAGLY.01","SPAC22A12.06c","SPBTRNALEU.06","SPAP11E10.02c","SPAC926.05c","SPRRNA.47","SPAC19A8.02","SPCC757.04","SPBC530.07c","SPBC106.03","SPAC890.05","SPCTRNAPHE.05","SPRRNA.16","SPBTRNALEU.05","SPBC15C4.02","SPMITTRNAALA.01","SPCTRNASER.12","SPAC637.03","SPATRNAARG.02","SPBC1683.09c","SPRRNA.12","SPCC1393.02c","SPBTRNAASN.02","SPCC584.03c","SPBC405.03c","SPBTRNAPRO.08","SPRRNA.30","SPBTRNAASN.03","SPRRNA.07","SPBC1347.02","SPAC19A8.01c","SPMITTRNAILE.02","SPBTRNAVAL.08","SPATRNAARG.01","SPAC20G8.04c","SPAC959.06c","SPBTRNAGLU.06","SPATRNAMET.03","SPRRNA.14","SPAC4H3.03c","SPBC3E7.11c","SPBC12C2.05c","SPCC417.12","SPCC24B10.07","SPBC839.04","SPRRNA.28","SPAC5H10.05c","SPBTRNALYS.09","SPRRNA.05","SPBC19C2.10","SPATRNATHR.01","SPCTRNAASP.08","SPAPB2B4.04c","SPRRNA.33","SPBTRNASER.06","SPAC17A5.12","SPATRNATRP.01","SPCC622.19","SPATRNAGLY.01","SPATRNATYR.01","SPATRNAGLU.04","SPAC29E6.01","SPCC1682.13","SPBTRNAGLN.03","SPAPYUK71.03c","SPBC8D2.16c","SPAC2E1P5.03","SPBC56F2.01","SPCC777.17c","SPCC191.05c","SPBTRNAHIS.02","SPCTRNAGLY.12","SPCC790.02","SPAC1F8.06","SPAC23E2.02","SPBC36B7.03","SPAC694.02","SPATRNACYS.02","SPAC56F8.02","SPMIT.02","SPAC57A10.09c","SPRRNA.29","SPBC16A3.02c","SPAC1F7.13c","SPBP23A10.13","SPCC1494.08c","SPBTRNAILE.07","SPAC694.04c","SPAC31A2.06","SPBPB21E7.01c","SPAC23A1.16c","SPBTRNAARG.04","SPBC8D2.03c","SPRRNA.13","SPBTRNAVAL.07"],"gene_count":517,"ltp_gene_count":0},{"uniquename":"PMID:6953418","title":"Extrachromosomal mutator inducing point mutations and deletions in mitochondrial genome of fission yeast.","citation":"Proc Natl Acad Sci U S A 1982 Apr;79(8):2618-22","abstract":"We report the isolation and characterization of a mutator mutant in the fission yeast Schizosaccharomyces pombe. This mutator is of extrachromosomal, very likely mitochondrial, inheritance and acts exclusively on mitochondrial mtDNA. It greatly enhances the frequency of spontaneous mitochondrial drug-resistance mutants compared to the wild type, but it is not obligatory for their occurrence. In contrast, mitochondrial respiratory deficient mutants can only be isolated from mutator strains. It could be shown that this mutator induces point mutations as well as deletions in the mitochondrial genome which lead to respiratory deficiency. This mutator might prove to have a novel function encoded by the mtDNA.","authors":"Seitz-Mayr G, Wolf K","authors_abbrev":"Seitz-Mayr G et al.","pubmed_publication_date":"Apr 1982","pubmed_entrez_date":"1982-04-01","publication_year":"1982","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30304922","title":"Mutation Analysis of Synthetic DNA Barcodes in a Fission Yeast Gene Deletion Library by Sanger Sequencing.","citation":"Genomics Inform 2018 Jun;16(2):22-29","abstract":"Incorporation of unique barcodes into fission yeast gene deletion collections has enabled the identification of gene functions by growth fitness analysis. For fine tuning, it is important to examine barcode sequences, because mutations arise during strain construction. Out of 8,708 barcodes (4,354 strains) covering 88.5% of all 4,919 open reading frames, 7,734 barcodes (88.8%) were validated as high-fidelity to be inserted at the correct positions by Sanger sequencing. Sequence examination of the 7,734 high-fidelity barcodes revealed that 1,039 barcodes (13.4%) deviated from the original design. In total, 1,284 mutations (mutation rate of 16.6%) exist within the 1,039 mutated barcodes, which is comparable to budding yeast (18%). When the type of mutation was considered, substitutions accounted for 845 mutations (10.9%), deletions accounted for 319 mutations (4.1%), and insertions accounted for 121 mutations (1.6%). Peculiarly, the frequency of substitutions (67.6%) was unexpectedly higher than in budding yeast (∼28%) and well above the predicted error of Sanger sequencing (∼2%), which might have arisen during the solid-phase oligonucleotide synthesis and PCR amplification of the barcodes during strain construction. When the mutation rate was analyzed by position within 20-mer barcodes using the 1,284 mutations from the 7,734 sequenced barcodes, there was no significant difference between up-tags and down-tags at a given position. The mutation frequency at a given position was similar at most positions, ranging from 0.4% (32/7,734) to 1.1% (82/7,734), except at position 1, which was highest (3.1%), as in budding yeast. Together, well-defined barcode sequences, combined with the next-generation sequencing platform, promise to make the fission yeast gene deletion library a powerful tool for understanding gene function.","doi":"10.5808/GI.2018.16.2.22","authors":"Lee M, Choi SJ, Han S, Nam M, Kim D, Kim DU, Hoe KL","authors_abbrev":"Lee M et al.","pubmed_publication_date":"Jun 2018","pubmed_entrez_date":"2018-10-12","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-10-13 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31064814","title":"Proximity-dependent biotinylation mediated by TurboID to identify protein-protein interaction networks in yeast.","citation":"J Cell Sci 2019 May 31;132(11)","abstract":"The use of proximity-dependent biotinylation assays coupled to mass spectrometry (PDB-MS) has changed the field of protein-protein interaction studies. However, despite the recurrent and successful use of BioID-based protein-protein interactions screening in mammalian cells, the implementation of PDB-MS in yeast has not been effective. Here, we report a simple and rapid approach in yeast to effectively screen for proximal and interacting proteins in their natural cellular environment by using TurboID, a recently described version of the BirA biotin ligase. Using the protein arginine methyltransferase Rmt3 and the RNA exosome subunits, Rrp6 and Dis3, the application of PDB-MS in yeast by using TurboID was able to recover protein-protein interactions previously identified using other biochemical approaches and provided new complementary information for a given protein bait. The development of a rapid and effective PDB assay that can systematically analyze protein-protein interactions in living yeast cells opens the way for large-scale proteomics studies in this powerful model organism.","doi":"10.1242/jcs.232249","authors":"Larochelle M, Bergeron D, Arcand B, Bachand F","authors_abbrev":"Larochelle M et al.","pubmed_publication_date":"31 May 2019","pubmed_entrez_date":"2019-05-09","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-07-02 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.10","SPAC20G8.01","SPAC29A4.02c","SPAC959.03c","SPAC1071.10c","SPAC458.07","SPBC1271.12","SPBC1703.07","SPBC1773.07c","SPBC18E5.11c","SPCC1223.07c","SPBC56F2.12","SPBC649.03","SPAC3H5.07","SPBC2G2.04c","SPAC631.01c","SPAC3A12.18","SPBC21H7.07c","SPBPJ4664.04","SPCPB16A4.05c","SPAC12G12.13c","SPBC18E5.06","SPAC1565.05","SPBC26H8.11c","SPCC74.03c","SPBC2G2.12","SPBC3E7.11c","SPBC365.13c","SPBC20F10.04c","SPBC16H5.02","SPAC1565.08","SPCC364.06","SPCC622.14","SPBC3B9.01","SPBC19F5.04","SPAC4A8.11c","SPBC18H10.04c","SPBC11G11.03","SPCC18B5.07c","SPBC28F2.07","SPAC1F7.05","SPBC21B10.03c","SPBC557.04","SPCC16C4.13c","SPAC2G11.07c","SPBC1D7.04","SPAC694.04c","SPAP32A8.02","SPAC16E8.06c","SPBC1271.04c","SPAPB1E7.07","SPBC19G7.15","SPBC354.10","SPBC839.16","SPAC589.10c","SPBC16H5.10c","SPAC17H9.02","SPAC630.14c","SPAC683.02c","SPCC63.14","SPAC22E12.17c","SPBC17D1.03c","SPCC737.06c","SPAC17A2.13c","SPBC16H5.12c","SPAP27G11.09c","SPAC1805.16c","SPBC2G5.03","SPCC1739.12","SPAP7G5.02c","SPAC343.10","SPCC622.12c","SPCC23B6.01c","SPBC1539.10","SPAP8A3.07c","SPBC1289.16c","SPBC9B6.10","SPBC16E9.16c","SPBC16G5.14c","SPAC521.03","SPAC3H8.02","SPBC409.05","SPBC26H8.08c","SPCPJ732.01","SPCC191.07","SPAC56F8.05c","SPBC17G9.09","SPBC8D2.10c","SPBC25H2.12c","SPAC10F6.01c","SPBC428.02c","SPAC23A1.17","SPBC405.01","SPAC1420.03","SPBC409.06","SPBC56F2.06","SPAC1687.15","SPAC140.02","SPBC25H2.05","SPBC215.09c","SPBC530.04","SPCC645.14c","SPAC17G8.14c","SPBC26H8.10","SPBC14F5.08","SPAC17A5.09c","SPBC3B8.09","SPAC24C9.11","SPBC16D10.07c","SPBC16G5.15c","SPCC188.06c","SPAC3F10.08c","SPAC7D4.07c","SPCC1795.11","SPAC23A1.12c","SPAC56E4.03","SPAC732.02c","SPAC9G1.10c","SPAC10F6.16","SPBC29A10.06c","SPCC24B10.21","SPCC4G3.18","SPAC25B8.12c","SPAC7D4.14c","SPBC25H2.02","SPCC1739.01","SPCC14G10.04","SPBC1A4.08c","SPAC2E1P5.05","SPCC584.04","SPCC584.11c","SPBC19G7.10c","SPAC1687.11","SPACUNK4.11c","SPBC660.16","SPAC32A11.04c","SPCC1442.09","SPBC776.17","SPBC1711.05","SPCC11E10.01","SPAC6F12.16c","SPAC23H3.09c","SPCC830.03","SPAC14C4.11","SPCC736.12c","SPBC12C2.06","SPBC1709.02c","SPAC13G6.09","SPAC25G10.09c","SPCC126.10","SPBC776.03","SPAC20G8.09c","SPBC365.11","SPBC13E7.10c","SPBP22H7.02c","SPBC36.04","SPCC757.07c","SPAC926.08c","SPAPJ760.02c","SPAC23C11.03","SPCC622.18","SPAC17H9.05","SPBC119.10","SPBC17D11.05","SPCC1739.07","SPBC18E5.07","SPAC23A1.03","SPAC664.08c","SPCC74.05","SPAC513.01c","SPAP8A3.04c","SPBC1105.02c","SPAC1783.07c","SPBC2D10.11c","SPAC10F6.13c","SPAC110.04c","SPCC16C4.07","SPBC56F2.08c","SPAC13D6.03c","SPAC9E9.03","SPBC409.07c","SPAC630.03","SPCC594.01","SPBC342.02","SPAC17A5.06","SPAC14C4.04","SPBC725.09c","SPAC17C9.03","SPAC1D4.02c","SPAC27D7.02c","SPBC354.12","SPAC2E1P3.04","SPCC24B10.08c","SPBC17D1.06","SPAC977.14c","SPBC25H2.15","SPAC26A3.15c","SPAC1F12.07","SPAC4F8.07c","SPCC825.01","SPCC550.15c","SPAPB1A10.13","SPCC576.08c","SPBC8D2.18c","SPCC1450.04","SPAC4F10.13c","SPAPJ696.01c","SPAC24C9.12c","SPBC8D2.06","SPAC1F3.01","SPAC23D3.07","SPBC336.14c","SPCC1442.08c","SPCC4G3.15c","SPCPB16A4.03c","SPBC16H5.08c","SPAC1687.22c","SPBC12C2.04","SPAC29A4.15","SPBC18H10.03","SPAC167.03c","SPAC890.05","SPAC4D7.05","SPAC27E2.03c","SPBC4.07c","SPCC1620.10","SPAC17G6.05c","SPAC23D3.06c","SPCC285.13c","SPBC577.15c","SPBC21H7.02","SPAC328.03","SPBC1A4.02c","SPBC947.13","SPAC22F3.10c","SPBC1773.10c","SPAC9.09","SPAC15A10.02","SPAC9E9.09c","SPAC343.05","SPBC215.05","SPAC1B9.02c","SPBC19F5.05c","SPCC1322.04","SPAC3G9.06","SPCC1753.01c","SPBC14F5.04c","SPCC18.14c","SPCP1E11.02","SPCC1393.06c","SPAC513.07","SPAC13G6.02c","SPCC1020.06c","SPBC337.10c","SPBC15D4.15","SPBC4C3.05c","SPBC1734.01c","SPBP4H10.05c","SPBC14F5.05c","SPAC26F1.13c","SPAC2F7.13c","SPAC31G5.13","SPAC824.09c","SPBC17G9.03c","SPBC19C7.06","SPAC15E1.04","SPAC3A11.13","SPBC660.13c","SPAC57A7.04c"],"gene_count":269,"ltp_gene_count":269},{"uniquename":"PMID:1770000","title":"The fission yeast gamma-tubulin is essential for mitosis and is localized at microtubule organizing centers.","citation":"J Cell Sci 1991 Aug;99 ( Pt 4):693-700","abstract":"gamma-Tubulin exists in fission yeast as the product of an essential gene, encoding a 446 amino acid protein that is 77.3% identical to Aspergillus nidulans gamma-tubulin. The gene disruption caused cell lethality, displaying condensed, undivided chromosomes with aberrant spindle structures. Anti-gamma-tubulin staining showed that gamma-tubulin is located, throughout the wild-type cell cycle, at the spindle pole bodies (SPBs), indicating that gamma-tubulin associates with interphase SPB in the absence of microtubules. In addition, anti-gamma-tubulin immunofluorescence staining revealed cytoplasmic, cell-equatorial putative MTOCs (microtubule organizing centers), which appear only during mitotic telophase and cytokinesis, and are located at the centers for the new cytoplasmic microtubule arrays of the two daughter cells. In the multiple-SPB mutant cut1-cdc11, anti-gamma-tubulin antibodies revealed many dots on the periphery of the nucleus. These results confirm that gamma-tubulin is an important member of the tubulin superfamily, suggest that it may be a universal component of MTOCs, and are consistent with a role for gamma-tubulin in controlling microtubule formation in vivo.","authors":"Horio T, Uzawa S, Jung MK, Oakley BR, Tanaka K, Yanagida M","authors_abbrev":"Horio T et al.","pubmed_publication_date":"Aug 1991","pubmed_entrez_date":"1991-08-01","publication_year":"1991","canto_session_key":"2ef712d4ff0feb1e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-09-15 11:57:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-23 14:02:54","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-23"},{"uniquename":"PMID:19758554","title":"Orchestrating twosome and foursome chromosome parties.","citation":"Dev Cell 2009 Sep;17(3):305-7","abstract":"The conserved centromere protein C (CENP-C) is indispensable for kinetochore function. Yet its mechanism of action has remained elusive. In this issue of Developmental Cell, Tanaka et al. report that the fission yeast homolog, Cnp3, acts as a linker protein that fulfills a variety of different roles in the bi- and mono-orientation of chromosomes during mitosis and meiosis I.","doi":"10.1016/j.devcel.2009.08.013","authors":"Kalitsis P, Choo KH","authors_abbrev":"Kalitsis P et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-09-18","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36794724","title":"Cellular responses to long-term phosphate starvation of fission yeast: Maf1 determines fate choice between quiescence and death associated with aberrant tRNA biogenesis.","citation":"Nucleic Acids Res 2023 Apr 24;51(7):3094-3115","abstract":"Inorganic phosphate is an essential nutrient acquired by cells from their environment. Here, we characterize the adaptative responses of fission yeast to chronic phosphate starvation, during which cells enter a state of quiescence, initially fully reversible upon replenishing phosphate after 2 days but resulting in gradual loss of viability during 4 weeks of starvation. Time-resolved analyses of changes in mRNA levels revealed a coherent transcriptional program in which phosphate dynamics and autophagy were upregulated, while the machineries for rRNA synthesis and ribosome assembly, and for tRNA synthesis and maturation, were downregulated in tandem with global repression of genes encoding ribosomal proteins and translation factors. Consistent with the transcriptome changes, proteome analysis highlighted global depletion of 102 ribosomal proteins. Concomitant with this ribosomal protein deficit, 28S and 18S rRNAs became vulnerable to site-specific cleavages that generated temporally stable rRNA fragments. The finding that Maf1, a repressor of RNA polymerase III transcription, was upregulated during phosphate starvation prompted a hypothesis that its activity might prolong lifespan of the quiescent cells by limiting production of tRNAs. Indeed, we found that deletion of maf1 results in precocious death of phosphate-starved cells via a distinctive starvation-induced pathway associated with tRNA overproduction and dysfunctional tRNA biogenesis.","doi":"10.1093/nar/gkad063","authors":"Garg A, Sanchez AM, Miele M, Schwer B, Shuman S","authors_abbrev":"Garg A et al.","pubmed_publication_date":"24 Apr 2023","pubmed_entrez_date":"2023-02-16","publication_year":"2023","canto_session_key":"2f3eb8594559cc00","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2023-09-01 16:12:12","canto_approved_date":"2024-05-16 13:31:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-08-21 22:56:32","canto_added_date":"2023-02-17 01:15:05","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":114,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBTRNAASN.02","SPCC645.02","SPAC24B11.05","SPAC2H10.01","SPATRNACYS.01","SPCTRNAPHE.04","SPATRNAPRO.02","SPBC577.13","SPBTRNATRP.03","SPCTRNAGLY.12","SPBTRNAASN.04","SPBC2F12.09c","SPBTRNATHR.06","SPNCRNA.1698","SPBC409.18","SPBTRNAGLY.09","SPCTRNATHR.10","SPAC4C5.01","SPCTRNAHIS.03","SPACUNK4.15","SPATRNAALA.06","SPAC16.05c","SPATRNAILE.01","SPBTRNATRP.02","SPBC21B10.04c","SPBC1271.09","SPAC806.04c","SPRRNA.24","SPRRNA.53","SPAC31G5.12c","SPCTRNAARG.10","SPBC4C3.12","SPAC1399.05c","SPBC17A3.03c","SPAC14C4.11","SPCC1393.13","SPBPB2B2.06c","SPAC7D4.05","SPAC1039.02","SPAC25B8.12c","SPBP35G2.12","SPCC1223.13","SPAC1783.07c","SPCC1672.06c","SPBC1703.13c","SPCC1393.08","SPBC530.11c","SPAC14C4.10c","SPATRNATHR.03","SPBC317.01","SPBTRNAMET.05","SPCTRNAASN.05","SPBC15D4.15","SPBTRNAGLN.02","SPATRNAVAL.01","SPAPB1E7.05","SPAC17G6.03","SPBC725.05c","SPBC1D7.02c","SPAC23D3.12","SPBC16E9.01c","SPBP4G3.02","SPAC25G10.03","SPAC3G6.03c","SPBC1778.03c","SPBC4.06","SPBC1652.01","SPATRNAARG.03","SPBC27B12.11c","SPBTRNAHIS.01","SPAC3H1.11","SPCC1322.14c","SPBTRNAGLY.04","SPBC14F5.13c","SPAC11E3.06","SPNCRNA.1712","SPAC644.05c","SPBC21H7.03c","SPBC713.07c","SPNCRNA.9001","SPAC11D3.11c","SPBC19C2.09","SPBTRNAPRO.07","SPAC13G7.10","SPBC2D10.06","SPCTRNAALA.12","SPAC823.14","SPCC830.10","SPBTRNAASN.01","SPRRNA.38","SPCC1020.07","SPBC1105.14","SPAC3A12.02","SPAC6G10.12c","SPAC56F8.16","SPATRNAPHE.01","SPAC6G9.05","SPATRNATHR.04","SPATRNAARG.01","SPBC8E4.01c","SPATRNAMET.02","SPATRNATYR.01","SPBTRNAMET.06","SPRRNA.05","SPAC6F12.02","SPAC2E12.02","SPBC30D10.03c","SPBC1683.01","SPBC1348.12"],"gene_count":109,"ltp_gene_count":73,"approved_date":"2023-09-01"},{"uniquename":"PMID:25378562","title":"Vsl1p cooperates with Fsv1p for vacuolar protein transport and homotypic fusion in Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 2015 Jan;161(Pt 1):89-98","abstract":"Members of the SNARE protein family participate in the docking-fusion step of several intracellular vesicular transport events. Saccharomyces cerevisiae Vam7p was identified as a SNARE protein that acts in vacuolar protein transport and membrane fusion. However, in Schizosaccharomyces pombe, there have been no reports regarding the counterpart of Vam7p. Here, we found that, although the SPCC594.06c gene has low similarity to Vam7p, the product of SPCC594.06c has a PX domain and SNARE motif like Vam7p, and thus we designated the gene Sch. pombe vsl1(+) (Vam7-like protein 1). The vsl1Δ cells showed no obvious defect in vacuolar protein transport. However, cells of the vsl1Δ mutant with a deletion of fsv1(+), which encodes another SNARE protein, displayed extreme defects in vacuolar protein transport and vacuolar morphology. Vsl1p was localized to the vacuolar membrane and prevacuolar compartment, and its PX domain was essential for proper localization. Expression of the fusion protein GFP-Vsl1p was able to suppress ZnCl2 sensitivity and the vacuolar protein sorting defect in the fsv1Δ cells. Moreover, GFP-Vsl1p was mislocalized in a pep12Δ mutant and in cells overexpressing fsv1(+). Importantly, overexpression of Sac. cerevisiae VAM7 could suppress the sensitivity to ZnCl2 of vsl1Δ cells and the vacuolar morphology defect of vsl1Δfsv1Δ cells in Sch. pombe. Taken together, these data suggest that Vsl1p and Fsv1p are required for vacuolar protein transport and membrane fusion, and they function cooperatively with Pep12p in the same membrane-trafficking step.","doi":"10.1099/mic.0.080481-0","authors":"Hosomi A, Higuchi Y, Yagi S, Takegawa K","authors_abbrev":"Hosomi A et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-11-08","publication_year":"2015","canto_session_key":"50574c5aacc2f341","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2017-09-16 14:13:39","canto_approved_date":"2023-02-03 15:10:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-23 06:58:19","canto_added_date":"2014-11-09 01:15:24","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.03c","SPBC3E7.01","SPAC458.05","SPCC594.06c","SPBC31E1.04","SPCC1795.03","SPAC19G12.10c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2017-09-16"},{"uniquename":"PMID:38830897","title":"Sororin is an evolutionary conserved antagonist of WAPL.","citation":"Nat Commun 2024 Jun 03;15(1):4729","abstract":"Cohesin mediates sister chromatid cohesion to enable chromosome segregation and DNA damage repair. To perform these functions, cohesin needs to be protected from WAPL, which otherwise releases cohesin from DNA. It has been proposed that cohesin is protected from WAPL by SORORIN. However, in vivo evidence for this antagonism is missing and SORORIN is only known to exist in vertebrates and insects. It is therefore unknown how important and widespread SORORIN's functions are. Here we report the identification of SORORIN orthologs in Schizosaccharomyces pombe (Sor1) and Arabidopsis thaliana (AtSORORIN). sor1Δ mutants display cohesion defects, which are partially alleviated by wpl1Δ. Atsororin mutant plants display dwarfism, tissue specific cohesion defects and chromosome mis-segregation. Furthermore, Atsororin mutant plants are sterile and separate sister chromatids prematurely at anaphase I. The somatic, but not the meiotic deficiencies can be alleviated by loss of WAPL. These results provide in vivo evidence for SORORIN antagonizing WAPL, reveal that SORORIN is present in organisms beyond the animal kingdom and indicate that it has acquired tissue specific functions in plants.","doi":"10.1038/s41467-024-49178-0","authors":"Prusén Mota I, Galova M, Schleiffer A, Nguyen TT, Kovacikova I, Farias Saad C, Litos G, Nishiyama T, Gregan J, Peters JM, Schlögelhofer P","authors_abbrev":"Prusén Mota I et al.","pubmed_publication_date":"03 Jun 2024","pubmed_entrez_date":"2024-06-03","publication_year":"2024","canto_session_key":"ecdb1fc29168829b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-11-12 12:08:12","canto_approved_date":"2024-11-17 15:16:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-12 11:54:38","canto_added_date":"2024-06-04 23:25:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPAC9E9.05","SPAC10F6.09c","SPBC16A3.11","SPAC110.02","SPBC428.17c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2024-11-12"},{"uniquename":"PMID:16950791","title":"Role of Hcn1 and its phosphorylation in fission yeast anaphase-promoting complex/cyclosome function.","citation":"J Biol Chem 2006 Oct 27;281(43):32284-93","abstract":"The anaphase-promoting complex/cyclosome (APC/C) is a conserved multisubunit ubiquitin ligase required for the degradation of key cell cycle regulators. The APC/C becomes active at the metaphase/anaphase transition and remains active during G(1) phase. One mechanism linked to activation of the APC/C is phosphorylation. Although many sites of mitotic phosphorylation have been identified in core components of the APC/C, the consequence of any individual phosphorylation event has not been elucidated in vivo. In this study, we show that Hcn1 is an essential core component of the fission yeast APC/C and is critical for maintaining complex integrity. Moreover, Hcn1 is a phosphoprotein in vivo. Phosphorylation of Hcn1 occurs at a single Cdk1 site in vitro and in vivo. Mutation of this site to alanine, but not aspartic acid, compromises APC/C function and leads to a specific defect in the completion of cell division.","authors":"Yoon HJ, Feoktistova A, Chen JS, Jennings JL, Link AJ, Gould KL","authors_abbrev":"Yoon HJ et al.","pubmed_publication_date":"27 Oct 2006","pubmed_entrez_date":"2006-09-05","publication_year":"2006","canto_session_key":"5897b3b8c236314e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-02-26 11:41:34","canto_approved_date":"2021-07-12 11:08:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-18 17:49:45","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.01c","SPBP23A10.04","SPBC1A4.01","SPAC27D7.05c","SPBC83.04","SPAC19G12.01c","SPBC11B10.09","SPAC23C11.12","SPAC6F12.15c","SPAC343.03","SPBC28E12.01c","SPAC6F12.14","SPBC106.09","SPAC6G10.12c","SPAC959.09c"],"gene_count":15,"ltp_gene_count":14,"approved_date":"2017-02-26"},{"uniquename":"PMID:1406591","title":"Mutations in the cdc10 start gene of Schizosaccharomyces pombe implicate the region of homology between cdc10 and SWI6 as important for p85cdc10 function.","citation":"Mol Gen Genet 1992 Sep;234(3):449-56","abstract":"The cdc10 gene of the fission yeast Schizosaccharomyces pombe is required for traverse of start and commitment to the mitotic cell division cycle rather than other fates. The product of the gene, p85cdc10, is a component of a factor that is thought to be involved in regulating the transcription of genes that are required for DNA synthesis. In order to define regions of the p85cdc10 protein that are important for its function a fine structure genetic map of the cdc10 gene was derived and the sequences of 13 cdc10ts mutants determined. The 13 mutants tested define eight alleles. Eleven of the mutants are located in the region that contains the two copies of the cdc10/SWI6 repeat motif, implicating it as important for p85cdc10 function.","authors":"Reymond A, Schmidt S, Simanis V","authors_abbrev":"Reymond A et al.","pubmed_publication_date":"Sep 1992","pubmed_entrez_date":"1992-09-01","publication_year":"1992","canto_session_key":"58d8ad0dec113279","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-11 17:05:23","canto_approved_date":"2026-01-29 16:55:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-19 23:40:43","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-01-11"},{"uniquename":"PMID:18727152","title":"The gap-filling sequence on the left arm of chromosome 2 in fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2008 Sep;25(9):673-9","abstract":"We report a gap-filling sequence between SPBPB21E7.09 (in contig c1348) and SPBPB10D8.01 (in contig pB10D8) on the left arm of chromosome 2 in the fission yeast, Schizosaccharomyces pombe. The sequence was determined from a BAC clone overlapping SPBPB21E7.01c (eno102) (in contig c1348) and SPBC1683.07 (mal1) (in contig pB10D8). The gap-filling sequence is 17,881 bp in length and contains five putative open reading frames, which were systematically named as SPBC460.01c, SPBC460.02c, SPBC460.03, SPBC460.04c and SPBC460.05. Their deduced amino acid sequences respectively include protein motifs corresponding to amino acid permease, glutathione S-transferase C-terminal domain, taurine catabolism dioxygenase TauD TfdA family and major facilitator superfamily, whereas their functions are unknown.","doi":"10.1002/yea.1613","authors":"Sasaki M, Idiris A, Tada A, Kumagai H, Giga-Hama Y, Tohda H","authors_abbrev":"Sasaki M et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-08-30","publication_year":"2008","canto_session_key":"79266661844338ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-09 15:30:41","canto_approved_date":"2019-01-09 15:30:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-09 15:30:34","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC460.05","SPBC460.03","SPBC460.02c","SPBC460.01c","SPBC460.04c"],"gene_count":5,"ltp_gene_count":0,"approved_date":"2019-01-09"},{"uniquename":"PMID:8781170","title":"Requirement of S. pombe exonuclease II, a homologue of S. cerevisiae Sep1, for normal mitotic growth and viability.","citation":"Curr Genet 1996 Sep;30(4):284-93","abstract":"Exonuclease II (ExoII) from Schizosaccharomyces pombe is a 5'-->3' single-stranded DNA exonuclease. We have cloned its gene, exo2, whose nucleotide sequence revealed that ExoII is a homologue of the multifunctional Saccharomyces cerevisiae Sep1 protein (also called Kem1, Xrn1, Rar5, Dst2). S. pombe exo2 null mutants were cold-sensitive for growth, had increased cell size at the restrictive temperature, were hypersensitive to the mitotic inhibitor thiabendazol and to caffeine, and died rapidly in stationary phase. Many of these phenotypes are similar to those of sep1 (kem1 or xrn1) mutants of S. cerevisiae. In contrast, the exo2 mutation had only a moderate effect on progression through meiosis and no significant effect on meiotic recombination. We discuss possible functions of the multifunctional ExoII protein.","authors":"Szankasi P, Smith GR","authors_abbrev":"Szankasi P et al.","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_session_key":"8cf9ec640280dda7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-23 14:13:00","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-23 14:12:54","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-23"},{"uniquename":"PMID:8939625","title":"The expression of recombinant proteins in yeasts.","citation":"Curr Opin Biotechnol 1996 Oct;7(5):517-24","abstract":"The methylotrophic yeasts Hansenula polymorpha and Pichia pastoris are rapidly becoming the systems of choice for the expression of recombinant proteins in yeast. However, the powerful genetic techniques available in Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe are still exploited to establish models to study medically important cell processes and screen for pharmacologically active compounds.","authors":"Sudbery PE","authors_abbrev":"Sudbery PE","pubmed_publication_date":"Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28945192","title":"Regulated Ire1-dependent mRNA decay requires no-go mRNA degradation to maintain endoplasmic reticulum homeostasis in  S. pombe .","citation":"Elife 2017 Sep 25;6","abstract":"The unfolded protein response (UPR) monitors and adjusts the protein folding capacity of the endoplasmic reticulum (ER). In  S. pombe , the ER membrane-resident kinase/endoribonuclease Ire1 utilizes a mechanism of selective degradation of ER-bound mRNAs (RIDD) to maintain homeostasis. We used a genetic screen to identify factors critical to the Ire1-mediated UPR and found several proteins, Dom34, Hbs1 and Ski complex subunits, previously implicated in ribosome rescue and mRNA no-go-decay (NGD). Ribosome profiling in ER-stressed cells lacking these factors revealed that Ire1-mediated cleavage of ER-associated mRNAs results in ribosome stalling and mRNA degradation. Stalled ribosomes iteratively served as a ruler to template precise, regularly spaced upstream mRNA cleavage events. This clear signature uncovered hundreds of novel target mRNAs. Our results reveal that the UPR in  S. pombe  executes RIDD in an intricate interplay between Ire1, translation, and the NGD pathway, and establish a critical role for NGD in maintaining ER homeostasis.","doi":"10.7554/eLife.29216","authors":"Guydosh NR, Kimmig P, Walter P, Green R","authors_abbrev":"Guydosh NR et al.","pubmed_publication_date":"25 Sep 2017","pubmed_entrez_date":"2017-09-26","publication_year":"2017","canto_session_key":"ac000fd52ebe2739","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rachel Green","canto_first_approved_date":"2017-10-31 16:01:51","canto_approved_date":"2023-11-15 19:20:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-13 14:21:28","canto_added_date":"2017-09-27 00:15:13","annotation_curators":[{"name":"Rachel Green","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":180,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_28945192_phaf.tsv"}],"genes":["SPCC1672.03c","SPCC417.07c","SPBC405.04c","SPBC3H7.05c","SPBC13E7.03c","SPAC13A11.01c","SPAC1142.08","SPCC364.03","SPBC16A3.08c","SPBC106.02c","SPBC16H5.04","SPBC651.10","SPBC8D2.12c","SPAC3C7.03c","SPCC613.06","SPAC14C4.08","SPBC13G1.02","SPCC1259.11c","SPCC16C4.06c","SPBC15D4.12c","SPCC285.04","SPCC1919.03c","SPAC3A11.04","SPBC691.05c","SPAC1805.15c","SPAC1952.05","SPAC15E1.09","SPAC140.02","SPAP8A3.03","SPBC354.08c","SPBC21C3.14c","SPAC4H3.07c","SPACUNK4.12c","SPAC1805.07c","SPBC418.01c","SPAP8A3.05","SPBPB21E7.01c","SPAC3G9.07c","SPAC2C4.06c","SPAC5D6.01","SPAP27G11.14c","SPAC17A5.18c","SPBC651.03c","SPAC19A8.02","SPBC1778.03c","SPAC17A5.14","SPAC17A2.02c","SPBC336.01","SPBC1734.12c","SPCC364.06","SPBC119.12","SPAC4G8.13c","SPAC13G6.14","SPBC24C6.04","SPBC25B2.01","SPBC947.02","SPCC1183.10","SPCC18B5.06","SPAC16E8.05c","SPCC4G3.02","SPBC1289.13c","SPAPB1E7.06c","SPBPB8B6.04c","SPBC530.05","SPAC31A2.02","SPBC342.01c","SPBC16E9.15","SPBC3H7.13","SPAC17A5.02c","SPCC330.02","SPCC70.06","SPAC2E1P5.03","SPBP8B7.31","SPBP4H10.09","SPBC3B8.03","SPBC1271.10c","SPAC13A11.04c","SPAC13C5.04","SPBPB2B2.14c","SPAC29B12.06c","SPCC24B10.08c","SPCC794.03","SPAC18B11.04","SPAC23G3.12c","SPBC32F12.02","SPAC17C9.07","SPCC594.04c","SPCC1450.09c","SPAC1D4.03c","SPAC22F8.02c","SPAPYUG7.02c","SPCC126.08c","SPBC19C2.13c","SPBP8B7.22","SPBC3E7.12c","SPCC1393.07c","SPCC31H12.05c","SPAC25H1.05","SPBC16G5.15c","SPBC31F10.13c","SPBC609.03","SPAC458.06","SPAC167.01","SPBC18E5.07","SPAC23H4.08","SPAC23H3.05c","SPCC4B3.08","SPAC4F10.04","SPCC11E10.08","SPBC4.05","SPAC1B1.04c","SPCC622.15c","SPAC664.01c","SPBC409.17c","SPAC17A2.06c","SPAC22F3.06c","SPAC13C5.02","SPCC126.01c","SPAC10F6.15","SPAC683.03","SPBC31A8.01c","SPBC1105.11c","SPBC29A10.06c","SPAC24H6.09","SPBC56F2.10c","SPBC216.01c","SPCC550.03c","SPAC2H10.01","SPAC630.04c","SPBC337.07c","SPCC548.05c","SPAC1782.05","SPAC589.10c","SPAC25B8.11","SPAC17A5.09c","SPAC9G1.12","SPAC2F7.06c","SPAC31A2.13c","SPCP1E11.02","SPAC57A10.14","SPAC24C9.14","SPBC12C2.02c","SPBC902.06","SPAC3C7.14c","SPAC1782.06c","SPAC6B12.05c","SPBC336.14c","SPBC1105.01","SPAC1A6.05c","SPCP31B10.05","SPBC18E5.11c","SPAC4F10.02","SPCC16C4.11","SPCC594.05c","SPBC16C6.02c","SPAC8C9.03","SPBC4F6.06","SPBC15C4.01c","SPAC328.01c","SPCC1494.10","SPBC15C4.05","SPBC3B8.07c","SPAC30D11.07","SPBC211.06","SPCC1020.06c","SPAC27E2.07","SPBC28F2.10c","SPAC15A10.05c","SPBC17D1.05","SPCC16C4.01","SPCC613.03","SPCC1840.02c","SPBC119.16c","SPBC1921.06c","SPAC1F7.08","SPBC17G9.10","SPAC343.10","SPAC959.04c","SPBC19C7.01","SPAC30D11.01c"],"gene_count":180,"ltp_gene_count":4,"approved_date":"2017-10-31"},{"uniquename":"PMID:7697346","title":"Meiosis. New roles for RNA in fission yeast.","citation":"Curr Biol 1995 Jan 01;5(1):4-6","abstract":"Recent investigations have revealed hitherto unsuspected roles for small, non-coding RNA molecules and regulated pre-mRNA splicing during meiosis in fission yeast.","authors":"MacNeill S, Fantes P","authors_abbrev":"MacNeill S et al.","pubmed_publication_date":"01 Jan 1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3870978","title":"On the nature and specificity of replicating instability in fission yeast.","citation":"Curr Genet 1985;10(4):291-6","abstract":"A strain of fission yeast carrying replicating instability (RI) will segregate mitotically three types of cells: unstable (still RI-carrying) cells, stable identical mutants and stable non-mutants. RI in fission yeast has previously been considered as a specific type of premutational lesion capable of (1) being replicated as such and (2) reverting at an appreciable rate to the normal state as well as changing into a stable mutation. In the present work genetic analysis of a previously studied RI-carrying strain showed this strain to be a diploid, most probably heterozygous for a recessive mutation. It was possible to construct other unstable heterozygous strains segregating predetermined mutants but not to induce RI by UV-irradiation of haploid cells. Thus evidence is presented against the premutational nature of RI in fission yeast.","authors":"Kurennaya ON, Devin AB","authors_abbrev":"Kurennaya ON et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37562570","title":"Phospholipid tail asymmetry allows cellular adaptation to anoxic environments.","citation":"J Biol Chem 2023 Sep;299(9):105134","abstract":"Membrane biophysical properties are critical to cell fitness and depend on unsaturated phospholipid acyl tails. These can only be produced in aerobic environments since eukaryotic desaturases require molecular oxygen. This raises the question of how cells maintain bilayer properties in anoxic environments. Using advanced microscopy, molecular dynamics simulations, and lipidomics by mass spectrometry we demonstrated the existence of an alternative pathway to regulate membrane fluidity that exploits phospholipid acyl tail length asymmetry, replacing unsaturated species in the membrane lipidome. We show that the fission yeast, Schizosaccharomyces japonicus, which can grow in aerobic and anaerobic conditions, is capable of utilizing this strategy, whereas its sister species, the well-known model organism Schizosaccharomyces pombe, cannot. The incorporation of asymmetric-tailed phospholipids might be a general adaptation to hypoxic environmental niches.","doi":"10.1016/j.jbc.2023.105134","authors":"Panconi L, Lorenz CD, May RC, Owen DM, Makarova M","authors_abbrev":"Panconi L et al.","pubmed_publication_date":"Sep 2023","pubmed_entrez_date":"2023-08-10","publication_year":"2023","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2023-08-12 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35171902","title":"The cAMP signaling pathway regulates Epe1 protein levels and heterochromatin assembly.","citation":"PLoS Genet 2022 Feb;18(2):e1010049","abstract":"The epigenetic landscape of a cell frequently changes in response to fluctuations in nutrient levels, but the mechanistic link is not well understood. In fission yeast, the JmjC domain protein Epe1 is critical for maintaining the heterochromatin landscape. While loss of Epe1 results in heterochromatin expansion, overexpression of Epe1 leads to defective heterochromatin. Through a genetic screen, we found that mutations in genes of the cAMP signaling pathway suppress the heterochromatin defects associated with Epe1 overexpression. We further demonstrated that the activation of Pka1, the downstream effector of cAMP signaling, is required for the efficient translation of epe1+ mRNA to maintain Epe1 overexpression. Moreover, inactivation of the cAMP-signaling pathway, either through genetic mutations or glucose deprivation, leads to the reduction of endogenous Epe1 and corresponding heterochromatin changes. These results reveal the mechanism by which the cAMP signaling pathway regulates heterochromatin landscape in fission yeast.","doi":"10.1371/journal.pgen.1010049","authors":"Bao K, Shan CM, Chen X, Raiymbek G, Monroe JG, Fang Y, Toda T, Koutmou KS, Ragunathan K, Lu C, Berchowitz LE, Jia S","authors_abbrev":"Bao K et al.","pubmed_publication_date":"Feb 2022","pubmed_entrez_date":"2022-02-16","publication_year":"2022","canto_session_key":"d99000225d887e1f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kehan Bao","canto_first_approved_date":"2022-02-28 15:54:08","canto_approved_date":"2024-04-12 17:40:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-02-26 17:20:10","canto_added_date":"2022-02-18 01:15:05","annotation_curators":[{"name":"Kehan Bao","community_curator":true,"annotation_count":39,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPAC8C9.03","SPBC32H8.07","SPAC23H3.13c","SPCC736.11","SPBC21C3.20c","SPCC1753.02c","SPCC285.09c","SPBC106.10","SPCC622.16c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2022-02-28"},{"uniquename":"PMID:39367033","title":"Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast Schizosaccharomyces pombe.","citation":"Sci Rep 2024 Oct 04;14(1):23105","abstract":"In eukaryotes, chromosomal DNA is equally distributed to daughter cells during mitosis, whereas the number of chromosomes is halved during meiosis. Despite considerable progress in understanding the molecular mechanisms that regulate mitosis, there is currently a lack of complete understanding of the molecular mechanisms regulating meiosis. Here, we took advantage of the fission yeast Schizosaccharomyces pombe, for which highly synchronous meiosis can be induced, and performed quantitative proteomics and phosphoproteomics analyses to track changes in protein expression and phosphorylation during meiotic divisions. We compared the proteomes and phosphoproteomes of exponentially growing mitotic cells with cells harvested around meiosis I, or meiosis II in strains bearing either the temperature-sensitive pat1-114 allele or conditional ATP analog-sensitive pat1-as2 allele of the Pat1 kinase. Comparing pat1-114 with pat1-as2 also allowed us to investigate the impact of elevated temperature (25 °C versus 34 °C) on meiosis, an issue that sexually reproducing organisms face due to climate change. Using TMTpro 18plex labeling and phosphopeptide enrichment strategies, we performed quantification of a total of 4673 proteins and 7172 phosphosites in S. pombe. We found that the protein level of 2680 proteins and the rate of phosphorylation of 4005 phosphosites significantly changed during progression of S. pombe cells through meiosis. The proteins exhibiting changes in expression and phosphorylation during meiotic divisions were represented mainly by those involved in the meiotic cell cycle, meiotic recombination, meiotic nuclear division, meiosis I, centromere clustering, microtubule cytoskeleton organization, ascospore formation, organonitrogen compound biosynthetic process, carboxylic acid metabolic process, gene expression, and ncRNA processing, among others. In summary, our findings provide global overview of changes in the levels and phosphorylation of proteins during progression of S. pombe cells through meiosis at normal and elevated temperatures, laying the groundwork for further elucidation of the functions and importance of specific proteins and their phosphorylation in regulating meiotic divisions in this yeast.","doi":"10.1038/s41598-024-74523-0","authors":"Sivakova B, Wagner A, Kretova M, Jakubikova J, Gregan J, Kratochwill K, Barath P, Cipak L","authors_abbrev":"Sivakova B et al.","pubmed_publication_date":"04 Oct 2024","pubmed_entrez_date":"2024-10-04","publication_year":"2024","canto_session_key":"7b511dd9f98b3b7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-11-01 17:30:35","canto_approved_date":"2025-01-31 11:45:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-10-31 14:08:35","canto_added_date":"2024-10-05 23:25:09","annotation_curators":[],"file_curator_name":"Pascal Carme","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":3226,"orcid":"0009-0003-9059-1333","file_type":"protein_modification","file_name":"PMID_39367033_modifications.tsv"},{"name":"Pascal 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13","SPAC2C4.12c","SPAC11D3.02c","SPBC11B10.09","SPAC23C4.07","SPAC4G9.03","SPAPB24D3.08c","SPAC1071.09c","SPBP8B7.31","SPBC9B6.08","SPBC13G1.04c","SPBC557.04","SPAC1399.01c","SPAC13C5.07","SPAC18B11.08c","SPBC354.05c","SPBC557.05","SPAC1F12.08","SPBC1685.14c","SPAC1002.14","SPBP8B7.11","SPAC17G8.06c","SPAC732.01","SPAC186.01","SPBP8B7.27","SPAC4G9.22","SPBC36.07","SPAC6F6.19","SPAC22F8.05","SPBC17D1.06","SPBC1711.16","SPBC29A3.06","SPAC23C11.03","SPCC1450.14c","SPAC630.03","SPCC1442.09","SPCC1393.07c","SPBC3B8.04c","SPCC645.03c","SPCC1840.09","SPCC132.03","SPAC1B9.02c","SPAC31G5.15","SPCC569.08c","SPBC27.03","SPBC887.18c","SPBC21.07c","SPCP1E11.05c","SPBC337.05c","SPAC4G8.08","SPAC343.17c","SPAC4F10.16c","SPCC736.15","SPBC543.02c","SPAC23D3.16","SPBC23G7.04c","SPAC6G10.08","SPAC8E11.02c","SPAC3G6.11","SPCC1183.01","SPCPB16A4.07","SPBC409.14c","SPBC21.01","SPAC23D3.04c","SPCC1281.06c","SPBC800.06","SPBC365.01","SPAC12B10.10","SPAC5H10.02c","SPBC15D4.07c","SPBCPT2R1.04c","SPCC1795.11","SPAC2C4.08","SPBC32H8.11","SPBC23G7.07c","SPAC16.04","SPAC18G6.03","SPAC1635.01","SPBC146.09c","SPAC4G9.20c","SPCC14G10.04","SPAC23H4.13c","SPCC550.15c","SPBC1289.07c","SPAC4G9.05","SPCC569.09","SPAC977.14c","SPAC22F3.06c","SPCC645.09","SPAC13G7.10","SPAC607.09c","SPBC1685.03"],"gene_count":2545,"ltp_gene_count":0,"approved_date":"2024-11-01"},{"uniquename":"PMID:10208430","title":"hRAD17, a structural homolog of the Schizosaccharomyces pombe RAD17 cell cycle checkpoint gene, stimulates p53 accumulation.","citation":"Oncogene 1999 Mar 04;18(9):1689-99","abstract":"The RAD17 gene product of S. Pombe is an essential component of the checkpoint control pathway which responds to both DNA damage and disruption of replication. We have identified a human cDNA that encodes a polypeptide which is structurally conserved with the S. Pombe Rad17 protein. The human gene, designated hRAD17, predicts an encoded protein of 590 amino acids and a molecular weight of 69 kD. Amino acid sequence alignment revealed that hRadl7 has 28.3% and 52.5% similarity with the S. Pombe Rad17 protein, and 21.8% identity and 45.8% similarity to the budding yeast cell cycle checkpoint protein, Rad 24. When introduced into the S. Pombe rad17 mutant, hRAD17 was able to partially revert its hydroxyurea and ionizing radiation hypersensitivity, but not its UV hypersensitivity. Permanent overexpression of the hRAD17 gene in human fibrosarcoma cells resulted in p53 activation and a significant reduction of S- and G2/M-phase cells accompanied by an accumulation of the G1-phase population, suggesting that hRAD17 may have a role in cell cycle checkpoint control. Immunostaining of HT-1080 cells transiently transfected with a hRAD17 construct confirmed the nuclear accumulation of p53, which mimics the induction caused by DNA damage. Using FISH analysis, we have mapped the hRAD17 locus to human chromosome 5q11.2.","authors":"Li L, Peterson CA, Kanter-Smoler G, Wei YF, Ramagli LS, Sunnerhagen P, Siciliano MJ, Legerski RJ","authors_abbrev":"Li L et al.","pubmed_publication_date":"04 Mar 1999","pubmed_entrez_date":"1999-04-20","publication_year":"1999","canto_session_key":"86d1a0fef7d5068c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 17:26:55","canto_session_submitted_date":"2012-03-03 17:26:35","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.13"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:28515324","title":"The diferric-tyrosyl radical cluster of ribonucleotide reductase and cytosolic iron-sulfur clusters have distinct and similar biogenesis requirements.","citation":"J Biol Chem 2017 Jul 07;292(27):11445-11451","abstract":"How each metalloprotein assembles the correct metal at the proper binding site presents challenges to the cell. The di-iron enzyme ribonucleotide reductase (RNR) uses a diferric-tyrosyl radical (Fe III  2 -Y • ) cofactor to initiate nucleotide reduction. Assembly of this cofactor requires O 2 , Fe II , and a reducing equivalent. Recent studies show that RNR cofactor biosynthesis shares the same source of iron, in the form of [2Fe-2S]-GSH 2  from the monothiol glutaredoxin Grx3/4, and the same electron source, in the form of the Dre2-Tah18 electron transfer chain, with the cytosolic iron-sulfur protein assembly (CIA) machinery required for maturation of [4Fe-4S] clusters in cytosolic and nuclear proteins. Here, we further investigated the interplay between the formation of the Fe III  2 -Y •  cofactor in RNR and the cellular iron-sulfur (Fe-S) protein biogenesis pathways by examining both the iron loading into the RNR β subunit and the RNR catalytic activity in yeast mutants depleted of individual components of the mitochondrial iron-sulfur cluster assembly (ISC) and the CIA machineries. We found that both iron loading and cofactor assembly in RNR are dependent on the ISC machinery. We also found that Dre2 is required for RNR cofactor formation but appears to be dispensable for iron loading. None of the CIA components downstream of Dre2 was required for RNR cofactor formation. Thus, the pathways for RNR and Fe-S cluster biogenesis bifurcate after the Dre2-Tah18 step. We conclude that RNR cofactor biogenesis requires the ISC machinery to mature the Grx3/4 and Dre2 Fe-S proteins, which then function in iron and electron delivery to RNR, respectively.","doi":"10.1074/jbc.M117.786178","authors":"Li H, Stümpfig M, Zhang C, An X, Stubbe J, Lill R, Huang M","authors_abbrev":"Li H et al.","pubmed_publication_date":"07 Jul 2017","pubmed_entrez_date":"2017-05-19","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC337.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16040243","title":"Two novel proteins, dos1 and dos2, interact with rik1 to regulate heterochromatic RNA interference and histone modification.","citation":"Curr Biol 2005 Aug 23;15(16):1448-57","abstract":"Chromosomal behavior during mitosis and meiosis depends in part on heterochromatic modifications such as histone H3 lysine-9 methylation (H3K9me). In fission yeast, the Heterochromatin Protein 1 homolog Swi6 recognizes H3K9me, silences transcription, and retains cohesin at pericentromeric repeats. Heterochromatin formation also depends on processing of transcripts derived from centromeric repeats by the RNAi machinery. The DDB1 homolog, Rik1, and histone methyltransferase, Clr4, act in a complex to promote H3K9me. However, the mechanism underlying this interaction is poorly understood.\nUsing a cytological screen, we have identified two novel genes, dos1(+) and dos2(+), which are required for localization of Swi6. Deletion of either of these genes results in mitotic and meiotic chromosome missegregation, defects in mitotic centromeric cohesion and meiotic telomere clustering, and loss of heterochromatic silencing. Dos1 is predominantly located in the nucleus in a Dos2-dependent manner and directly interacts with Rik1. Each of these genes is required for the association of H3K9me with centromeric repeats, as well as for the production of small interfering RNAs.\nDos1 and Dos2 are required for the formation of heterochromatin in fission yeast. We hypothesize that the physical interaction between Dos1 and Rik1 represents a role in regulating activity of the Rik1/Clr4 complex. Dos2 contributes to this role by regulating Dos1 localization. Our findings suggest a mechanism for recruitment of Clr4 in the RNAi-dependent heterochromatin pathway, in which Dos1 and Dos2 are essential.","authors":"Li F, Goto DB, Zaratiegui M, Tang X, Martienssen R, Cande WZ","authors_abbrev":"Li F et al.","pubmed_publication_date":"23 Aug 2005","pubmed_entrez_date":"2005-07-26","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC613.12c","SPCC970.07c","SPCC11E10.08"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11676924","title":"Telomere binding of the Rap1 protein is required for meiosis in fission yeast.","citation":"Curr Biol 2001 Oct 16;11(20):1618-23","abstract":"Telomeres are essential for chromosome integrity, protecting the ends of eukaryotic linear chromosomes during cell proliferation. Telomeres also function in meiosis; a characteristic clustering of telomeres beneath the nuclear membrane is observed during meiotic prophase in many organisms from yeasts to plants and humans, and the role of the telomeres in meiotic pairing and the recombination of homologous chromosomes has been demonstrated in the fission yeast Schizosaccharomyces pombe and in the budding yeast Saccharomyces cerevisiae. Here we report that S. pombe Rap1 is a telomeric protein essential for meiosis. While Rap1 is conserved in budding yeast and humans, schemes for telomere binding vary among species: human RAP1 binds to the telomere through interaction with the telomere binding protein TRF2; S. cerevisiae Rap1, however, binds telomeric DNA directly, and no orthologs of TRF proteins have been identified in this organism. In S. pombe, unlike in S. cerevisiae, an ortholog of human TRF has been identified. This ortholog, Taz1, binds directly to telomere repeats [18] and is necessary for telomere clustering in meiotic prophase. Our results demonstrate that S. pombe Rap1 binds to telomeres through interaction with Taz1, similar to human Rap1-TRF2, and that Taz1-mediated telomere localization of Rap1 is necessary for telomere clustering and for the successful completion of meiosis. Moreover, in taz1-disrupted cells, molecular fusion of Rap1 with the Taz1 DNA binding domain recovers telomere clustering and largely complements defects in meiosis, indicating that telomere localization of Rap1 is a key requirement for meiosis.","authors":"Chikashige Y, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"16 Oct 2001","pubmed_entrez_date":"2001-10-26","publication_year":"2001","canto_session_key":"1f8a9a6747848375","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-09 16:34:00","canto_approved_date":"2020-04-07 10:24:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-27 15:37:04","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.02","SPAC16A10.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-09"},{"uniquename":"PMID:5366939","title":"Mitochondrial DNA in the fission yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1969 Dec 16;195(2):579-81","abstract":"","authors":"Bostock CJ","authors_abbrev":"Bostock CJ","pubmed_publication_date":"16 Dec 1969","pubmed_entrez_date":"1969-12-16","publication_year":"1969","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20675407","title":"Combinatorial, site-specific requirement for heterochromatic silencing factors in the elimination of nucleosome-free regions.","citation":"Genes Dev 2010 Aug 15;24(16):1758-71","abstract":"High-resolution nucleosome occupancy maps of heterochromatic regions of wild-type and silencing-defective mutants of the fission yeast Schizosaccharomyces pombe revealed that heterochromatin induces the elimination of nucleosome-free regions (NFRs). NFRs associated with transcription initiation sites as well as those not associated with promoters are affected. We dissected the roles of the histone H3K9 methyltransferase Clr4 and the HP1 proteins Swi6 and Chp2, as well as the two catalytic activities of the SHREC histone deacetylase (HDAC)/ATPase effector complex. Strikingly, different DNA sites have distinct combinatorial requirements for these factors: Five classes of NFRs were identified that are eliminated by silencing factors through a mechanistic hierarchy governed by Clr4. The SHREC HDAC activity plays a major role in the elimination of class I-IV NFRs by antagonizing the action of RSC, a remodeling complex implicated in NFR formation. We propose that heterochromatin formation involves the deployment in several sequence-specific mechanisms to eliminate gaps between nucleosomes, thereby blocking access to the DNA.","doi":"10.1101/gad.1946410","authors":"Garcia JF, Dumesic PA, Hartley PD, El-Samad H, Madhani HD","authors_abbrev":"Garcia JF et al.","pubmed_publication_date":"15 Aug 2010","pubmed_entrez_date":"2010-08-03","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4B4.03","SPBC800.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:31987003","title":"Control of cellular organization and its coordination with the cell cycle.","citation":"Biosci Biotechnol Biochem 2020 May;84(5):869-875","abstract":"Cells organize themselves to maintain proper shape, structure, and size during growth and division for their cellular functions. However, how these cellular organizations coordinate with the cell cycle is not well understood. This review focuses on cell morphogenesis and size of the membrane-bound nucleus in the fission yeast  Schizosaccharomyces pombe . Growth polarity, an important factor for cell morphogenesis, in rod-shaped fission yeast is restricted to the cell tips and dynamically changes depending on the cell cycle stage. Furthermore, nuclear size in fission yeast is proportional to the cell size, resulting in a constant ratio between nuclear volume and cellular volume (N/C ratio). This review summarizes the signaling pathway(s) involved in growth polarity control and key factors involved in N/C ratio control and provides their roles in coordination between cell organization and the cell cycle.","doi":"10.1080/09168451.2020.1717926","authors":"Kume K","authors_abbrev":"Kume K","pubmed_publication_date":"May 2020","pubmed_entrez_date":"2020-01-29","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30601114","title":"RNA-binding proteins distinguish between similar sequence motifs to promote targeted deadenylation by Ccr4-Not.","citation":"Elife 2019 Jan 02;8","abstract":"The Ccr4-Not complex removes mRNA poly(A) tails to regulate eukaryotic mRNA stability and translation. RNA-binding proteins contribute to specificity by interacting with both Ccr4-Not and target mRNAs, but this is not fully understood. Here, we reconstitute accelerated and selective deadenylation of RNAs containing AU-rich elements (AREs) and Pumilio-response elements (PREs). We find that the fission yeast homologues of Tristetraprolin/TTP and Pumilio/Puf (Zfs1 and Puf3) interact with Ccr4-Not via multiple regions within low-complexity sequences, suggestive of a multipartite interface that extends beyond previously defined interactions. Using a two-color assay to simultaneously monitor poly(A) tail removal from different RNAs, we demonstrate that Puf3 can distinguish between RNAs of very similar sequence. Analysis of binding kinetics reveals that this is primarily due to differences in dissociation rate constants. Consequently, motif quality is a major determinant of mRNA stability for Puf3 targets in vivo and can be used for the prediction of mRNA targets.","doi":"10.7554/eLife.40670","authors":"Webster MW, Stowell JA, Passmore LA","authors_abbrev":"Webster MW et al.","pubmed_publication_date":"02 Jan 2019","pubmed_entrez_date":"2019-01-03","publication_year":"2019","canto_session_key":"1028f9ea656cb67b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lori Passmore","canto_first_approved_date":"2019-01-24 15:16:00","canto_approved_date":"2026-03-17 08:51:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-04 20:09:56","canto_added_date":"2019-01-04 01:15:04","annotation_curators":[{"name":"Lori Passmore","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.06","SPAC16C9.04c","SPAC57A7.04c","SPBC1718.07c","SPAC29B12.06c","SPAC1B3.05","SPAC1687.22c","SPCC4G3.15c","SPCC18.06c","SPCC31H12.08c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2019-01-24"},{"uniquename":"PMID:16922381","title":"[How does fission yeast cut8 regulate the nuclear localization of proteasome?].","citation":"Tanpakushitsu Kakusan Koso 2006 Aug;51(10 Suppl):1241-4","abstract":"","authors":"Takeda K, Yanagida M","authors_abbrev":"Takeda K et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-23","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22310068","title":"Identifying a static nonlinear structure in a biological system using noisy, sparse data.","citation":"J Theor Biol 2012 May 07;300:232-41","abstract":"When part of a biological system cannot be investigated directly by experimentation, we face the problem of structure identification: how can we construct a model for an unknown part of a mostly known system using measurements gathered from its input and output? This problem is especially difficult to solve when the measurements available are noisy and sparse, i.e. widely and unevenly spaced in time, as is common when measuring biological quantities at the cellular level. Here we present a procedure to identify a static nonlinearity embedded between two dynamical systems using noisy, sparse measurements. To reduce the level of error caused by measurement noise, we introduce the concept of weighted-sum predictability. If we make the input and output subsystems weighted-sum predictable and normalize the measurements to their weighted sum, we achieve better noise reduction than through normalizing to a loading control. We then interpolate the normalized measurements to obtain continuous input and output signals, with which we solve directly for the input-output characteristics of the unknown static nonlinearity. We demonstrate the effectiveness of this structure identification procedure by applying it to identify a model for ergosterol sensing by the proteins Sre1 and Scp1 in fission yeast. Simulations with this model produced outputs consistent with experimental observations. The techniques introduced here will provide researchers with a new tool by which biological systems can be identified and characterized.","doi":"10.1016/j.jtbi.2012.01.037","authors":"Porter JR, Burg JS, Espenshade PJ, Iglesias PA","authors_abbrev":"Porter JR et al.","pubmed_publication_date":"07 May 2012","pubmed_entrez_date":"2012-02-08","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15492511","title":"Checkpoint adaptation and recovery: back with Polo after the break.","citation":"Cell Cycle 2004 Nov;3(11):1383-6","abstract":"S. cerevisiae cells that are unable to repair a double strand break ultimately escape the DNA damage checkpoint arrest and enter mitosis. This process called 'adaptation' depends on functional Cdc5, a Polo-like kinase, and was long thought to be limited to single-cell organisms. However, the recent finding that Xenopus extracts can adapt to a long-lasting stall in DNA replication indicates that checkpoint adaptation does also occur in multicellular organisms. Interestingly, the Xenopus Polo-like kinase (Plx1) plays an important role in this adaptation. To add to this, data from our laboratory have shown that the human Polo-like kinase (Plk1) is also required for cell cycle reentry following a DNA damage-induced arrest. But here, Plk1 was shown to be required for bona-fide checkpoint recovery, rather than adaptation. That is, Plk1 is required to restart the cell cycle once all of the damage is repaired and checkpoint signaling is turned off. While the target of Plx1 during adaptation is a component of the checkpoint machinery (Claspin), the target of Plk1 during recovery turns out to be a mitotic regulator (Wee1). Here, we discuss some of the remarkable similarities and subtle differences in the molecular mechanisms that control checkpoint adaptation and recovery, and the role of Polo-like kinases therein.","authors":"van Vugt MA, Medema RH","authors_abbrev":"van Vugt MA et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-20","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35320724","title":"Cdc48 influence on separase levels is independent of mitosis and suggests translational sensitivity of separase.","citation":"Cell Rep 2022 Mar 22;38(12):110554","abstract":"Cdc48 (p97/VCP) is a AAA-ATPase that can extract ubiquitinated proteins from their binding partners and can cooperate with the proteasome for their degradation. A fission yeast cdc48 mutant (cdc48-353) shows low levels of the cohesin protease, separase, and pronounced chromosome segregation defects in mitosis. Separase initiates chromosome segregation when its binding partner securin is ubiquitinated and degraded. The low separase levels in the cdc48-353 mutant have been attributed to a failure to extract ubiquitinated securin from separase, resulting in co-degradation of separase along with securin. If true, Cdc48 would be important in mitosis. In contrast, we show here that low separase levels in the cdc48-353 mutant are independent of mitosis. Moreover, we find no evidence of enhanced separase degradation in the mutant. Instead, we suggest that the cdc48-353 mutant uncovers specific requirements for separase translation. Our results highlight a need to better understand how this key mitotic enzyme is synthesized.","doi":"10.1016/j.celrep.2022.110554","authors":"Vijayakumari D, Müller J, Hauf S","authors_abbrev":"Vijayakumari D et al.","pubmed_publication_date":"22 Mar 2022","pubmed_entrez_date":"2022-03-23","publication_year":"2022","canto_session_key":"28c85bd1757a57ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silke Hauf","canto_first_approved_date":"2022-03-28 12:39:29","canto_approved_date":"2026-02-06 15:49:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-19 07:53:35","canto_added_date":"2022-03-25 01:15:05","annotation_curators":[{"name":"Silke Hauf","community_curator":true,"annotation_count":51,"orcid":"0000-0001-5938-721X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.15c","SPBC36B7.05c","SPBC216.07c","SPBC839.17c","SPBC582.03","SPCC63.08c","SPBC646.09c","SPAC4A8.04","SPBC11C11.03","SPBC336.12c","SPAC1565.08","SPCC5E4.04","SPAC1006.01","SPBC14C8.01c","SPAC24C9.14","SPAC343.09","SPBC146.03c","SPBC21C3.11","SPBC1A4.03c","SPBC16A3.09c","SPAC25G10.07c","SPAC20H4.10"],"gene_count":22,"ltp_gene_count":11,"approved_date":"2022-03-28"},{"uniquename":"PMID:9450546","title":"A series of vectors to construct lacZ fusions for the study of gene expression in Schizosaccharomyces pombe.","citation":"FEBS Lett 1997 Dec 22;420(1):39-42","abstract":"We have constructed a series of plasmids to facilitate the fusion of promoters with or without coding regions of genes of Schizosaccharomyces pombe to the lacZ gene of Escherichia coli. These vectors carry a multiple cloning region in which fission yeast DNA may be inserted in three different reading frames with respect to the coding region of lacZ. The plasmids were constructed with the ura4+ or the his3+ marker of S. pombe. Functionality of the plasmids was tested measuring in parallel the expression of fructose 1,6-bisphosphatase and beta-galactosidase under the control of the fbp1+ promoter in different conditions.","authors":"Lafuente MJ, Petit T, Gancedo C","authors_abbrev":"Lafuente MJ et al.","pubmed_publication_date":"22 Dec 1997","pubmed_entrez_date":"1998-02-05","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33519754","title":"Modification of Transfer RNA Levels Affects Cyclin Aggregation and the Correct Duplication of Yeast Cells.","citation":"Front Microbiol 2020;11:607693","abstract":"Codon usage bias (the preferential use of certain synonymous codons (optimal) over others is found at the organism level (intergenomic) within specific genomes (intragenomic) and even in certain genes. Whether it is the result of genetic drift due to GC/AT content and/or natural selection is a topic of intense debate. Preferential codons are mostly found in genes encoding highly-expressed proteins, while lowly-expressed proteins usually contain a high proportion of rare (lowly-represented) codons. While optimal codons are decoded by highly expressed tRNAs, rare codons are usually decoded by lowly-represented tRNAs. Whether rare codons play a role in controlling the expression of lowly- or temporarily-expressed proteins is an open question. In this work we approached this question using two strategies, either by replacing rare glycine codons with optimal counterparts in the gene that encodes the cell cycle protein Cdc13, or by overexpression the tRNA   Gly   that decodes rare codons from the fission yeast,  Schizosaccharomyces pombe . While the replacement of synonymous codons severely affected cell growth, increasing tRNA levels affected the aggregation status of Cdc13 and cell division. These lead us to think that rare codons in lowly-expressed cyclin proteins are crucial for cell division, and that the overexpression of tRNA that decodes rare codons affects the expression of proteins containing these rare codons. These codons may be the result of the natural selection of codons in genes that encode lowly-expressed proteins.","doi":"10.3389/fmicb.2020.607693","authors":"Arias L, Martínez F, González D, Flores-Ríos R, Katz A, Tello M, Moreira S, Orellana O","authors_abbrev":"Arias L et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2021-02-01","publication_year":"2020","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2021-02-03 01:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084841","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.29"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21549339","title":"A mutation in the Golgi Qb-SNARE gene GOSR2 causes progressive myoclonus epilepsy with early ataxia.","citation":"Am J Hum Genet 2011 May 13;88(5):657-63","abstract":"The progressive myoclonus epilepsies (PMEs) are a group of predominantly recessive disorders that present with action myoclonus, tonic-clonic seizures, and progressive neurological decline. Many PMEs have similar clinical presentations yet are genetically heterogeneous, making accurate diagnosis difficult. A locus for PME was mapped in a consanguineous family with a single affected individual to chromosome 17q21. An identical-by-descent, homozygous mutation in GOSR2 (c.430G>T, p.Gly144Trp), a Golgi vesicle transport gene, was identified in this patient and in four apparently unrelated individuals. A comparison of the phenotypes in these patients defined a clinically distinct PME syndrome characterized by early-onset ataxia, action myoclonus by age 6, scoliosis, and mildly elevated serum creatine kinase. This p.Gly144Trp mutation is equivalent to a loss of function and results in failure of GOSR2 protein to localize to the cis-Golgi.","doi":"10.1016/j.ajhg.2011.04.011","authors":"Corbett MA, Schwake M, Bahlo M, Dibbens LM, Lin M, Gandolfo LC, Vears DF, O'Sullivan JD, Robertson T, Bayly MA, Gardner AE, Vlaar AM, Korenke GC, Bloem BR, de Coo IF, Verhagen JM, Lehesjoki AE, Gecz J, Berkovic SF","authors_abbrev":"Corbett MA et al.","pubmed_publication_date":"13 May 2011","pubmed_entrez_date":"2011-05-10","publication_year":"2011","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP14E8.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33179595","title":"Synergy between Wsp1 and Dip1 may initiate assembly of endocytic actin networks.","citation":"Elife 2020 Nov 12;9","abstract":"The actin filament nucleator Arp2/3 complex is activated at cortical sites in  Schizosaccharomyces pombe  to assemble branched actin networks that drive endocytosis. Arp2/3 complex activators Wsp1 and Dip1 are required for proper actin assembly at endocytic sites, but how they coordinately control Arp2/3-mediated actin assembly is unknown. Alone, Dip1 activates Arp2/3 complex without preexisting actin filaments to nucleate 'seed' filaments that activate Wsp1-bound Arp2/3 complex, thereby initiating branched actin network assembly. In contrast, because Wsp1 requires preexisting filaments to activate, it has been assumed to function exclusively in propagating actin networks by stimulating branching from preexisting filaments. Here we show that Wsp1 is important not only for propagation but also for initiation of endocytic actin networks. Using single molecule total internal reflection fluorescence microscopy we show that Wsp1 synergizes with Dip1 to co-activate Arp2/3 complex. Synergistic co-activation does not require preexisting actin filaments, explaining how Wsp1 contributes to actin network initiation in cells.","doi":"10.7554/eLife.60419","authors":"Balzer CJ, James ML, Narvaez-Ortiz HY, Helgeson LA, Sirotkin V, Nolen BJ","authors_abbrev":"Balzer CJ et al.","pubmed_publication_date":"12 Nov 2020","pubmed_entrez_date":"2020-11-12","publication_year":"2020","canto_session_key":"881818ae7e2c6d17","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-11-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.15c","SPBC24C6.10c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:10390529","title":"Terminator element mutations affect both the efficiency and position of RNA polymerase I termination in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1999 Jul 15;27(14):2883-8","abstract":"RNA polymerase I transcripts, purified from Schizosaccharomyces pombe cells, terminate at three sites that precede 'Sal box'-like termination element (TE) sequences. Essential features in these elements were investigated by the in vivo expression of targeted mutations. RNA analyses confirmed a functional significance for two of the elements (Boxes 1 and 3), but indicated that the third, less related, sequence (Box 2) does not function as a termination signal. The results further indicated that the most conserved residues in the two active TEs, as well as adjacent regions, are also most critical to function. Furthermore, some mutations in these elements or in immediately flanking sequences affect not only the efficiency of termination, but also alter the position of termination by as much as 35 nt. Since the element is able to influence the site of termination over a surprisingly long stretch of DNA sequence, these observations suggest that the TE does not act simply as a pause element by fixing the termination factor.","authors":"Shwed PS, Nazar RN","authors_abbrev":"Shwed PS et al.","pubmed_publication_date":"15 Jul 1999","pubmed_entrez_date":"1999-07-03","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29859088","title":"Using in vivo oxidation status of one- and two-component redox relays to determine H 2 O 2  levels linked to signaling and toxicity.","citation":"BMC Biol 2018 Jun 01;16(1):61","abstract":"","doi":"10.1186/s12915-018-0523-6","authors":"Domènech A, Ayté J, Antunes F, Hidalgo E","authors_abbrev":"Domènech A et al.","pubmed_publication_date":"01 Jun 2018","pubmed_entrez_date":"2018-06-03","publication_year":"2018","canto_session_key":"18d6d076b1c7c8b5","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-06-04 00:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC576.03c","SPAC1783.07c","SPAC7D4.07c","SPCC757.07c","SPBC577.08c"],"gene_count":5,"ltp_gene_count":4},{"uniquename":"PMID:21703453","title":"A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at the plasma membrane.","citation":"Cell 2011 Jun 24;145(7):1116-28","abstract":"Concentration gradients regulate many cell biological and developmental processes. In rod-shaped fission yeast cells, polar cortical gradients of the DYRK family kinase Pom1 couple cell length with mitotic commitment by inhibiting a mitotic inducer positioned at midcell. However, how Pom1 gradients are established is unknown. Here, we show that Tea4, which is normally deposited at cell tips by microtubules, is both necessary and, upon ectopic cortical localization, sufficient to recruit Pom1 to the cell cortex. Pom1 then moves laterally at the plasma membrane, which it binds through a basic region exhibiting direct lipid interaction. Pom1 autophosphorylates in this region to lower lipid affinity and promote membrane release. Tea4 triggers Pom1 plasma membrane association by promoting its dephosphorylation through the protein phosphatase 1 Dis2. We propose that local dephosphorylation induces Pom1 membrane association and nucleates a gradient shaped by the opposing actions of lateral diffusion and autophosphorylation-dependent membrane detachment.","doi":"10.1016/j.cell.2011.05.014","authors":"Hachet O, Berthelot-Grosjean M, Kokkoris K, Vincenzetti V, Moosbrugger J, Martin SG","authors_abbrev":"Hachet O et al.","pubmed_publication_date":"24 Jun 2011","pubmed_entrez_date":"2011-06-28","publication_year":"2011","canto_session_key":"46b68935ca658572","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2017-11-02 19:23:03","canto_approved_date":"2025-12-08 22:37:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-10 16:27:55","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":65,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPBC1706.01","SPBC776.02c","SPCC1223.06","SPAC2F7.03c","SPAC6G10.02c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-11-02"},{"uniquename":"PMID:17004072","title":"Chromosome segregation in fission yeast with mutations in the tubulin folding cofactor D.","citation":"Curr Genet 2006 Nov;50(5):281-94","abstract":"Faithful chromosome segregation requires the combined activities of the microtubule-based mitotic spindle and the multiple proteins that form mitotic kinetochores. Here, we show that the fission yeast mitotic mutant, tsm1-512, is an allele of the tubulin folding chaperone, cofactor D. Chromosome segregation in this and in an additional cofactor D mutant depends on growth conditions that are monitored specifically by the mitotic checkpoint proteins Mad1, 2, 3 and Bub3. The temperature-sensitive mutants we have used disrupt the function of cofactor D to different extents, but both strains form a mitotic spindle in which the poles separate in anaphase. However, chromosome segregation is often unequal, apparently due to a defect in kinetochore-microtubule interactions. Mutations in cofactor D render cells particularly sensitive to the expression levels of a CENP-B-like protein, Abp1p, which works as an allele-specific, high-copy suppressor of cofactor D. This and other genetic interactions between cofactor D mutants and specific kinetochore and spindle components suggest their critical role in establishing the normal kinetochore-microtubule interface.","authors":"Fedyanina OS, Mardanov PV, Tokareva EM, McIntosh JR, Grishchuk EL","authors_abbrev":"Fedyanina OS et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-09-28","publication_year":"2006","canto_session_key":"878405351e803458","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-12-29 14:54:25","canto_approved_date":"2026-01-29 20:43:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-02 15:36:24","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.04c","SPBC409.04c","SPCC736.14","SPBC20F10.06","SPAC22H10.10","SPBC11C11.04c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-12-29"},{"uniquename":"PMID:27474797","title":"Spatial control of translation repression and polarized growth by conserved NDR kinase Orb6 and RNA-binding protein Sts5.","citation":"Elife 2016 Jul 30;5","abstract":"RNA-binding proteins contribute to the formation of ribonucleoprotein (RNP) granules by phase transition, but regulatory mechanisms are not fully understood. Conserved fission yeast NDR (Nuclear Dbf2-Related) kinase Orb6 governs cell morphogenesis in part by spatially controlling Cdc42 GTPase. Here we describe a novel, independent function for Orb6 kinase in negatively regulating the recruitment of RNA-binding protein Sts5 into RNPs to promote polarized cell growth. We find that Orb6 kinase inhibits Sts5 recruitment into granules, its association with processing (P) bodies, and degradation of Sts5-bound mRNAs by promoting Sts5 interaction with 14-3-3 protein Rad24. Many Sts5-bound mRNAs encode essential factors for polarized cell growth, and Orb6 kinase spatially and temporally controls the extent of Sts5 granule formation. Disruption of this control system affects cell morphology and alters the pattern of polarized cell growth, revealing a role for Orb6 kinase in the spatial control of translational repression that enables normal cell morphogenesis.","doi":"10.7554/eLife.14216","authors":"Nuñez I, Rodriguez Pino M, Wiley DJ, Das ME, Chen C, Goshima T, Kume K, Hirata D, Toda T, Verde F","authors_abbrev":"Nuñez I et al.","pubmed_publication_date":"30 Jul 2016","pubmed_entrez_date":"2016-07-31","publication_year":"2016","canto_session_key":"c0a9c75bb30edb82","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-08-01 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1002.13c","SPBC336.03","SPBP19A11.04c","SPCC297.03","SPAC1834.06c","SPCC16C4.09","SPAC8E11.02c","SPAC821.12","SPBC17F3.02"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:12503848","title":"Cell-cycle responses to DNA damage in G2.","citation":"Int Rev Cytol 2003;222:99-140","abstract":"Cellular reproduction, at its basic level, is simply the passing of genetic information from a single parent cell into two daughter cells. As the cellular genome encodes all the information that defines a cell, it is crucial that the genome be accurately replicated. Furthermore, the duplicated genome must be properly segregated so that each daughter cell contains the exact same information as the parent cell. The processes by which this occurs is known as the cell cycle. The failure of either duplication or segregation of the genome can have disastrous consequences for an organism, including cancer and death. This article discusses what is known about checkpoints, the surveillance mechanisms that monitor both the fidelity and accuracy of DNA replication and segregation. Specifically, we will focus on the G2 checkpoint that is responsible for ensuring proper segregation of the duplicated genome into the daughter cells and how this checkpoint functions to arrest entry into mitosis in response to DNA damage.","authors":"Cuddihy AR, O'Connell MJ","authors_abbrev":"Cuddihy AR et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2002-12-31","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12871901","title":"The Schizosaccharomyces pombe cdt2(+) gene, a target of G1-S phase-specific transcription factor complex DSC1, is required for mitotic and premeiotic DNA replication.","citation":"Genetics 2003 Jul;164(3):881-93","abstract":"We have defined five sev genes by genetic analysis of Schizosaccharomyces pombe mutants, which are defective in both proliferation and sporulation. sev1(+)/cdt2(+) was transcribed during the G1-S phase of the mitotic cell cycle, as well as during the premeiotic S phase. The mitotic expression of cdt2(+) was regulated by the MCB-DSC1 system. A mutant of a component of DSC1 affected cdt2(+) expression in vivo, and a cdt2(+) promoter fragment containing MCB motifs bound DSC1 in vitro. Cdt2 protein also accumulated in S phase and localized to the nucleus. cdt2 null mutants grew slowly at 30 degrees and were unable to grow at 19 degrees. These cdt2 mutants were also medially sensitive to hydroxyurea, camptothecin, and 4-nitroquinoline-1-oxide and were synthetically lethal in combination with DNA replication checkpoint mutations. Flow cytometry analysis and pulsed-field gel electrophoresis revealed that S-phase progression was severely retarded in cdt2 mutants, especially at low temperatures. Under sporulation conditions, premeiotic DNA replication was impaired with meiosis I blocked. Furthermore, overexpression of suc22(+), a ribonucleotide reductase gene, fully complemented the sporulation defect of cdt2 mutants and alleviated their growth defect at 19 degrees. These observations suggest that cdt2(+) plays an important role in DNA replication in both the mitotic and the meiotic life cycles of fission yeast.","authors":"Yoshida SH, Al-Amodi H, Nakamura T, McInerny CJ, Shimoda C","authors_abbrev":"Yoshida SH et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-07-23","publication_year":"2003","canto_session_key":"495b692e25887eaf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-17 14:13:08","canto_approved_date":"2024-06-28 10:15:37","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-05-24 11:44:11","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPAC9E9.08","SPAC14C4.13","SPCC18B5.11c","SPAC24H6.05","SPAC17H9.19c","SPBC25D12.04","SPBC216.05","SPBC336.12c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2015-06-17"},{"uniquename":"PMID:21493688","title":"Cdt1 proteolysis is promoted by dual PIP degrons and is modulated by PCNA ubiquitylation.","citation":"Nucleic Acids Res 2011 Aug;39(14):5978-90","abstract":"Cdt1 plays a critical role in DNA replication regulation by controlling licensing. In Metazoa, Cdt1 is regulated by CRL4(Cdt2)-mediated ubiquitylation, which is triggered by DNA binding of proliferating cell nuclear antigen (PCNA). We show here that fission yeast Cdt1 interacts with PCNA in vivo and that DNA loading of PCNA is needed for Cdt1 proteolysis after DNA damage and in S phase. Activation of this pathway by ultraviolet (UV)-induced DNA damage requires upstream involvement of nucleotide excision repair or UVDE repair enzymes. Unexpectedly, two non-canonical PCNA-interacting peptide (PIP) motifs, which both have basic residues downstream, function redundantly in Cdt1 proteolysis. Finally, we show that poly-ubiquitylation of PCNA, which occurs after DNA damage, reduces Cdt1 proteolysis. This provides a mechanism for fine-tuning the activity of the CRL4(Cdt2) pathway towards Cdt1, allowing Cdt1 proteolysis to be more efficient in S phase than after DNA damage.","doi":"10.1093/nar/gkr222","authors":"Guarino E, Shepherd ME, Salguero I, Hua H, Deegan RS, Kearsey SE","authors_abbrev":"Guarino E et al.","pubmed_publication_date":"Aug 2011","pubmed_entrez_date":"2011-04-16","publication_year":"2011","canto_session_key":"7bd5662a92fe98d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-03-31 16:17:51","canto_approved_date":"2022-09-02 17:21:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-18 16:34:27","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":52,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.01","SPBC1734.06","SPBC428.18","SPBC16D10.09","SPAC664.07c","SPAC13G6.01c","SPAC17H9.19c","SPAC1952.07","SPAC14C4.13","SPBC23E6.07c","SPBC19C7.09c","SPBC3E7.08c","SPBC25H2.13c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2016-03-31"},{"uniquename":"PMID:18722173","title":"Chromosome fusions following telomere loss are mediated by single-strand annealing.","citation":"Mol Cell 2008 Aug 22;31(4):463-473","abstract":"Progressive telomere shortening eventually results in chromosome fusions and genome instability as the cell's ability to distinguish chromosome ends from DNA double-strand breaks is compromised. In fission yeast, such events frequently produce stable survivors with all circular chromosomes. To shed light on the repair pathways that mediate chromosome end fusions and generate circular chromosomes, we have examined a diverse array of DNA repair factors. We show that telomere attrition-induced chromosome fusions are dependent on the fission yeast homologs of Rad52, the ERCC1/XPF endonuclease, the single-stranded DNA-binding protein RPA, and the Srs2 and Werner/Bloom helicases, but not Ku and ligase 4. Consistent with a recombinational mechanism of single-strand annealing, cloned junctions map to four of five homology regions in subtelomeric DNA. A comparison with telomere uncapping caused by the absence of the double-stranded telomere-binding protein Taz1 demonstrates that the circumstances and cause of telomere dysfunction profoundly affect which DNA repair pathway is engaged.","doi":"10.1016/j.molcel.2008.05.028","authors":"Wang X, Baumann P","authors_abbrev":"Wang X et al.","pubmed_publication_date":"22 Aug 2008","pubmed_entrez_date":"2008-08-30","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPBC29A3.14c","SPAC26H5.06","SPCC1183.05c","SPAC2G11.12","SPAC4H3.05","SPCC330.01c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:27166749","title":"Paired arrangement of kinetochores together with microtubule pivoting and dynamics drive kinetochore capture in meiosis I.","citation":"Sci Rep 2016 May 11;6:25736","abstract":"Kinetochores are protein complexes on the chromosomes, whose function as linkers between spindle microtubules and chromosomes is crucial for proper cell division. The mechanisms that facilitate kinetochore capture by microtubules are still unclear. In the present study, we combine experiments and theory to explore the mechanisms of kinetochore capture at the onset of meiosis I in fission yeast. We show that kinetochores on homologous chromosomes move together, microtubules are dynamic and pivot around the spindle pole, and the average capture time is 3-4 minutes. Our theory describes paired kinetochores on homologous chromosomes as a single object, as well as angular movement of microtubules and their dynamics. For the experimentally measured parameters, the model reproduces the measured capture kinetics and shows that the paired configuration of kinetochores accelerates capture, whereas microtubule pivoting and dynamics have a smaller contribution. Kinetochore pairing may be a general feature that increases capture efficiency in meiotic cells.","doi":"10.1038/srep25736","authors":"Cojoc G, Florescu AM, Krull A, Klemm AH, Pavin N, Jülicher F, Tolić IM","authors_abbrev":"Cojoc G et al.","pubmed_publication_date":"11 May 2016","pubmed_entrez_date":"2016-05-12","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-05-13 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10219245","title":"Net1, a Sir2-associated nucleolar protein required for rDNA silencing and nucleolar integrity.","citation":"Cell 1999 Apr 16;97(2):245-56","abstract":"The Sir2 protein mediates gene silencing and repression of recombination at the rDNA repeats in budding yeast. Here we show that Sir2 executes these functions as a component of a nucleolar complex designated RENT (regulator of nucleolar silencing and telophase exit). Net1, a core subunit of this complex, preferentially cross-links to the rDNA repeats, but not to silent DNA regions near telomeres or to active genes, and tethers the RENT complex to rDNA. Net1 is furthermore required for rDNA silencing and nucleolar integrity. During interphase, Net1 and Sir2 colocalize to a subdomain within the nucleous, but at the end of mitosis a fraction of Sir2 leaves the nucleolus and disperses as foci throughout the nucleus, suggesting that the structure of rDNA silent chromatin changes during the cell cycle. Our findings suggest that a protein complex shown to regulate exit from mitosis is also involved in gene silencing.","authors":"Straight AF, Shou W, Dowd GJ, Turck CW, Deshaies RJ, Johnson AD, Moazed D","authors_abbrev":"Straight AF et al.","pubmed_publication_date":"16 Apr 1999","pubmed_entrez_date":"1999-04-29","publication_year":"1999","canto_session_key":"26c25b0f2bc424a4","canto_annotation_status":"APPROVED","canto_triage_status":"Wrong organism","canto_curator_role":"PomBase","canto_first_approved_date":"2026-06-24 15:39:46","canto_approved_date":"2026-06-24 15:39:46","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-06-24 15:38:38","canto_added_date":"2025-09-22 15:28:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC25D12.02c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2026-06-24"},{"uniquename":"PMID:22751018","title":"Structural basis for the activity of a cytoplasmic RNA terminal uridylyl transferase.","citation":"Nat Struct Mol Biol 2012 Aug;19(8):782-787","abstract":"Cytoplasmic terminal uridylyl transferases comprise a conserved family of enzymes that negatively regulate the stability or biological activity of a variety of eukaryotic RNAs, including mRNAs and tumor-suppressor let-7 microRNAs. Here we describe crystal structures of the Schizosaccharomyces pombe cytoplasmic terminal uridylyl transferase Cid1 in two apo conformers and bound to UTP. We demonstrate that a single histidine residue, conserved in mammalian Cid1 orthologs, is responsible for discrimination between UTP and ATP. We also describe a new high-affinity RNA substrate-binding mechanism of Cid1, which is essential for enzymatic activity and is mediated by three basic patches across the surface of the enzyme. Overall, our structures provide a basis for understanding the activity of Cid1 and a mechanism of UTP selectivity conserved in its human orthologs, suggesting potential implications for anticancer drug design.","doi":"10.1038/nsmb.2329","authors":"Yates LA, Fleurdépine S, Rissland OS, De Colibus L, Harlos K, Norbury CJ, Gilbert RJC","authors_abbrev":"Yates LA et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-07-04","publication_year":"2012","canto_session_key":"cd9cc6ef89d1846d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"vw253 cam.ac.uk","canto_first_approved_date":"2013-11-01 12:45:55","canto_approved_date":"2024-12-02 12:52:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-09 11:33:46","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"vw253 cam.ac.uk","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-11-01","pdb_entries":[{"pdb_id":"4e7x","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A/B/C/D","position":"1-405"}],"title":"Structural Basis for the Activity of a Cytoplasmic RNA Terminal U-transferase","entry_authors":"Yates LA,Fleurdepine S,Rissland OS,DeColibus L,Harlos K,Norbury CJ,Gilbert RJC","entry_authors_abbrev":"Yates LA et al.","reference_uniquename":"PMID:22751018","experimental_method":"X-ray","resolution":"3.2"},{"pdb_id":"4e8f","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A/B","position":"1-405"}],"title":"Structural Basis for the Activity of a Cytoplasmic RNA Terminal U-transferase","entry_authors":"Yates LA,Fleurdepine S,Rissland OS,DeColibus L,Harlos K,Norbury CJ,Gilbert RJC","entry_authors_abbrev":"Yates LA et al.","reference_uniquename":"PMID:22751018","experimental_method":"X-ray","resolution":"2.6"},{"pdb_id":"4e80","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A/B/C/D","position":"1-405"}],"title":"Structural Basis for the Activity of a Cytoplasmic RNA Terminal U-transferase","entry_authors":"Yates LA,Fleurdepine S,Rissland OS,DeColibus L,Harlos K,Norbury CJ,Gilbert RJC","entry_authors_abbrev":"Yates LA et al.","reference_uniquename":"PMID:22751018","experimental_method":"X-ray","resolution":"3.02"}]},{"uniquename":"PMID:19758441","title":"Dissecting the fission yeast regulatory network reveals phase-specific control elements of its cell cycle.","citation":"BMC Syst Biol 2009 Sep 16;3:93","abstract":"Fission yeast Schizosaccharomyces pombe and budding yeast Saccharomyces cerevisiae are among the original model organisms in the study of the cell-division cycle. Unlike budding yeast, no large-scale regulatory network has been constructed for fission yeast. It has only been partially characterized. As a result, important regulatory cascades in budding yeast have no known or complete counterpart in fission yeast.\nBy integrating genome-wide data from multiple time course cell cycle microarray experiments we reconstructed a gene regulatory network. Based on the network, we discovered in addition to previously known regulatory hubs in M phase, a new putative regulatory hub in the form of the HMG box transcription factor SPBC19G7.04. Further, we inferred periodic activities of several less known transcription factors over the course of the cell cycle, identified over 500 putative regulatory targets and detected many new phase-specific and conserved cis-regulatory motifs. In particular, we show that SPBC19G7.04 has highly significant periodic activity that peaks in early M phase, which is coordinated with the late G2 activity of the forkhead transcription factor fkh2. Finally, using an enhanced Bayesian algorithm to co-cluster the expression data, we obtained 31 clusters of co-regulated genes 1) which constitute regulatory modules from different phases of the cell cycle, 2) whose phase order is coherent across the 10 time course experiments, and 3) which lead to identification of phase-specific control elements at both the transcriptional and post-transcriptional levels in S. pombe. In particular, the ribosome biogenesis clusters expressed in G2 phase reveal new, highly conserved RNA motifs.\nUsing a systems-level analysis of the phase-specific nature of the S. pombe cell cycle gene regulation, we have provided new testable evidence for post-transcriptional regulation in the G2 phase of the fission yeast cell cycle. Based on this comprehensive gene regulatory network, we demonstrated how one can generate and investigate plausible hypotheses on fission yeast cell cycle regulation which can potentially be explored experimentally.","doi":"10.1186/1752-0509-3-93","authors":"Bushel PR, Heard NA, Gutman R, Liu L, Peddada SD, Pyne S","authors_abbrev":"Bushel PR et al.","pubmed_publication_date":"16 Sep 2009","pubmed_entrez_date":"2009-09-18","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14993272","title":"Lub1 participates in ubiquitin homeostasis and stress response via maintenance of cellular ubiquitin contents in fission yeast.","citation":"Mol Cell Biol 2004 Mar;24(6):2324-31","abstract":"Ubiquitin-dependent proteolysis plays a pivotal role in stress responses. To investigate the mechanisms of these cellular processes, we have been studying Schizosaccharomyces pombe mutants that have altered sensitivities to various stress conditions. Here, we showed that Lub1, a homologue of Ufd3p/Zzz4p/Doa1p in budding yeast, is involved in the regulation of ubiquitin contents. Disruption of the lub1+ gene resulted in monoubiquitin as well as multiubiquitin depletion without change in mRNA level and in hypersensitivity to various stress conditions. Consistently, overexpression of genes encoding ubiquitin suppressed the defects associated with lub1 mutation, indicating that the phenotypes of the lub1 mutants under stress conditions were due to cellular ubiquitin shortage at the posttranscriptional level. In addition, the lub1-deleted cells showed aberrant functions in ubiquitin/proteasome-dependent proteolysis, with accelerated degradation of ubiquitin. Also Cdc48, a stress-induced chaperon-like essential ATPase, was found to interact with Lub1, and this association might contribute to the stabilization of Lub1. Our results indicated that Lub1 is responsible for ubiquitin homeostasis at the protein level through a negative regulation of ubiquitin degradation.","authors":"Ogiso Y, Sugiura R, Kamo T, Yanagiya S, Lu Y, Okazaki K, Shuntoh H, Kuno T","authors_abbrev":"Ogiso Y et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-03-03","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.08","SPBC887.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:41790722","title":"Hypomorphic mutations in ura6 confer 5-FOA resistance in fission yeast.","citation":"PLoS One 2026;21(3):e0344121","abstract":"Genome integrity is essential for cellular survival and adaptation across diverse physiological states. The fission yeast Schizosaccharomyces pombe relies on conserved DNA repair pathways to maintain genome stability during proliferative growth and in the absence of cell division (quiescence/G0). Using 5-fluoroorotic acid (5-FOA) counter-selection, we examined spontaneous mutation accumulation in both conditions in a wild-type prototrophic strain. Unexpectedly, we identified in growing and quiescent cells a class of 5-FOA-resistant mutants that, unlike canonical ura4 or ura5 loss-of-function mutants, retain the ability to grow without uracil supplementation. Genetic analyses showed that this phenotype is stable and segregates as a single locus. Whole-genome sequencing of tetrads from independent crosses revealed multiple hypomorphic alleles of ura6, which encodes the essential uridylate kinase. These alleles, comprising non-synonymous substitutions and an in-frame duplication, cluster within conserved regions of the protein and likely reduce production of the toxic 5-FOA-derived metabolite while preserving sufficient uracil biosynthesis.","doi":"10.1371/journal.pone.0344121","authors":"Kowal C, Liu Y, Denis C, Arcangioli B, Francesconi S, Gangloff S","authors_abbrev":"Kowal C et al.","pubmed_publication_date":"2026","pubmed_entrez_date":"2026-03-06","publication_year":"2026","canto_session_key":"4071fc402f2ff531","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Serge Gangloff","canto_first_approved_date":"2026-06-17 08:50:57","canto_approved_date":"2026-06-17 08:50:57","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-06-10 09:47:11","canto_added_date":"2026-03-07 00:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":14,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Serge Gangloff","community_curator":true,"annotation_count":7,"orcid":"0000-0003-1333-6091","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2026-06-17"},{"uniquename":"PMID:32651564","title":"Efficient recovery of the RNA-bound proteome and protein-bound transcriptome using phase separation (OOPS).","citation":"Nat Protoc 2020 Aug;15(8):2568-2588","abstract":"RNA-protein interactions play a pivotal role in cell homeostasis and disease, but current approaches to study them require a considerable amount of starting material, favor the recovery of only a subset of RNA species or are complex and time-consuming. We recently developed orthogonal organic phase separation (OOPS): a quick, efficient and reproducible method to purify cross-linked RNA-protein adducts in an unbiased way. OOPS avoids molecular tagging or the capture of polyadenylated RNA. Instead, it is based on sampling the interface of a standard TRIzol extraction to enrich RNA-binding proteins (RBPs) and their cognate bound RNA. OOPS specificity is achieved by digesting the enriched interfaces with RNases or proteases to release the RBPs or protein-bound RNA, respectively. Here we present a step-by-step protocol to purify protein-RNA adducts, free protein and free RNA from the same sample. We further describe how OOPS can be applied in human cell lines, Arabidopsis thaliana, Schizosaccharomyces pombe and Escherichia coli and how it can be used to study RBP dynamics.","doi":"10.1038/s41596-020-0344-2","authors":"Villanueva E, Smith T, Queiroz RML, Monti M, Pizzinga M, Elzek M, Dezi V, Harvey RF, Ramakrishna M, Willis AE, Lilley KS","authors_abbrev":"Villanueva E et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-07-12","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-07-13 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20536828","title":"A screen for genes involved in respiration control and longevity in Schizosaccharomyces pombe.","citation":"Ann N Y Acad Sci 2010 Jun;1197:19-27","abstract":"We present results showing that glucose signaling has proaging effects in the yeast Schizosaccharomyces pombe. Deletion of the receptor that senses extracellular glucose (Git3) increases the life span of S. pombe, while constitutive activation of the Galpha subunit acting downstream of this receptor (Gpa2) shortens its life span. The latter mutant is also impaired for growth under respiration conditions. We have used this phenotype in a selection strategy to identify genes that when overexpressed can rescue the respiratory defect of constitutively active Galpha subunit mutants. Here, we report an extended version of the work we presented at the IABG meeting and the results of this screen. This strategy allowed us to isolate four genes: psp1(+)/moc1(+), cka1(+), adh1(+), and rpb10(+). Interestingly, the overexpression of these genes was also capable of increasing the chronological life span of wild-type yeast cells.","doi":"10.1111/j.1749-6632.2010.05198.x","authors":"Roux AE, Arseneault G, Chartrand P, Ferbeyre G, Rokeach LA","authors_abbrev":"Roux AE et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-06-12","publication_year":"2010","canto_session_key":"4b2746df9d755a7f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-25 22:14:15","canto_approved_date":"2024-03-18 16:20:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-25 22:14:06","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1753.02c","SPBC646.13","SPAC23C11.11","SPAC23H3.13c","SPCC13B11.01","SPAC1B3.12c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2014-06-25"},{"uniquename":"PMID:16143617","title":"Capture of extranuclear DNA at fission yeast double-strand breaks.","citation":"Genetics 2005 Dec;171(4):1535-48","abstract":"Proper repair of DNA double-strand breaks (DSBs) is necessary for the maintenance of genomic integrity. Here, a new simple assay was used to study extrachromosomal DSB repair in Schizosaccharomyces pombe. Strikingly, DSB repair was associated with the capture of fission yeast mitochondrial DNA (mtDNA) at high frequency. Capture of mtDNA fragments required the Lig4p/Pku70p nonhomologous end-joining (NHEJ) machinery and its frequency was highly increased in fission yeast cells grown to stationary phase. The fission yeast Mre11 complex Rad32p/Rad50p/Nbs1p was also required for efficient capture of mtDNA at DSBs, supporting a role for the complex in promoting intermolecular ligation. Competition assays further revealed that microsatellite DNA from higher eukaryotes was preferentially captured at yeast DSBs. Finally, cotransformation experiments indicated that, in NHEJ-deficient cells, capture of extranuclear DNA at DSBs was observed if homologies--as short as 8 bp--were present between DNA substrate and DSB ends. Hence, whether driven by NHEJ, microhomology-mediated end-joining, or homologous recombination, DNA capture associated with DSB repair is a mutagenic process threatening genomic stability.","authors":"Decottignies A","authors_abbrev":"Decottignies A","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-09-07","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23754627","title":"Non-mRNA 3' end formation: how the other half lives.","citation":"Wiley Interdiscip Rev RNA 2013;4(5):491-506","abstract":"The release of nascent RNA from transcribing RNA polymerase complexes is required for all further functions carried out by RNA molecules. The elements and processing machinery involved in 3' end formation therefore represent key determinants in the biogenesis and accumulation of cellular RNA. While these factors have been well-characterized for messenger RNA, recent work has elucidated analogous pathways for the 3' end formation of other important cellular RNA. Here, we discuss four specific cases of non-mRNA 3' end formation-metazoan small nuclear RNA, Saccharomyces cerevisiae small nuclear RNA, Schizosaccharomyces pombe telomerase RNA, and the mammalian MALAT1 large noncoding RNA-as models of alternative mechanisms to generate RNA 3' ends. Comparison of these disparate processing pathways reveals an emerging theme of evolutionary ingenuity. In some instances, evidence for the creation of a dedicated processing complex exists; while in others, components are utilized from the existing RNA processing machinery and modified to custom fit the unique needs of the RNA substrate. Regardless of the details of how non-mRNA 3' ends are formed, the lengths to which biological systems will go to release nascent transcripts from their DNA templates are fundamental for cell survival.","doi":"10.1002/wrna.1174","authors":"Peart N, Sataluri A, Baillat D, Wagner EJ","authors_abbrev":"Peart N et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-06-12","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37984574","title":"Designing Ubiquitin-like protease 1 (Ulp1) based nano biocatalysts: A promising technology for SUMO fusion proteins.","citation":"Int J Biol Macromol 2023 Nov 19;255:128258","abstract":"The SUMO proteases (Ulps), a group of cysteine proteases, are well known for their efficient ability to perform structure-based cleavage of SUMO tag from the protein of interest and generation of biotherapeutics with authentic N-terminus. However, the stability of Ulps has remained a challenge for the economical production of difficult-to-produce proteins in E. coli. Therefore, the present study aimed to establish the methodology for developing stable S. pombe Ulp1 preparation using different enzyme immobilization strategies. The whole-cell biocatalyst developed using the Pir1 anchor protein of Pichia cleaved the SUMO tag within 24 h of reaction incubation. The chemical immobilization using commercial epoxy and amino methacrylate beads significantly enhanced the operational reusability of SpUlp1 up to 24 cycles. Silica beads further improved the repetitive usage of the immobilized enzyme for 65 cycles. The SpUlp1 immobilization on laboratory-developed chitosan-coated iron oxide nanoparticles exhibited more than 90 % cleavage of SUMO tag from different substrates even after 100 consecutive reactions. Moreover, an effective SUMO tag removal was observed within 10 min of incubation. The operational stability of the immobilized enzyme was confirmed in a pH range of 5 to 13. The spherical nature of nanoparticles was confirmed by FESEM and TEM results. The successful chitosan coating and subsequent activation with glutaraldehyde were established via FT-IR. Furthermore, HRTEM, SAED, and XRD proved the crystalline nature of nanoparticles, while VSM confirmed the superparamagnetic behavior.","doi":"10.1016/j.ijbiomac.2023.128258","authors":"Babbal, Mohanty S, Khasa YP","authors_abbrev":"Babbal et al.","pubmed_publication_date":"19 Nov 2023","pubmed_entrez_date":"2023-11-20","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-11-22 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26852120","title":"Deubiquitination and the regulation of stress granule assembly.","citation":"Curr Genet 2016 Aug;62(3):503-6","abstract":"Stress granules (SGs) are evolutionarily conserved ribonucleoprotein (RNP) structures that form in response to a variety of environmental and cellular cues. The presence of these RNP granules has been linked to a number of human diseases, including neurodegenerative disorders like amyotrophic lateral sclerosis (ALS) and spinocerebellar ataxia type 2 (Li et al., J Cell Biol 201:361-372, 2013; Nonhoff et al., Mol Biol Cell 18:1385-1396, 2007). Understanding how the assembly of these granules is controlled could, therefore, suggest possible routes of therapy for patients afflicted with these conditions. Interestingly, several reports have identified a potential role for protein deubiquitination in the assembly of these RNP granules. In particular, recent work has found that a specific deubiquitinase enzyme, Ubp3, is required for efficient SG formation in S. cerevisiae (Nostramo et al., Mol Cell Biol 36:173-183, 2016). This same enzyme has been linked to SGs in other organisms, including humans and the fission yeast, Schizosaccharomyces pombe (Takahashi et al., Mol Cell Biol 33:815-829, 2013; Wang et al., RNA 18:694-703, 2012). At first glance, these observations suggest that a striking degree of conservation exists for a ubiquitin-based mechanism controlling SG assembly. However, the devil is truly in the details here, as the precise nature of the involvement of this deubiquitinating enzyme seems to vary in each organism. Here, we briefly review these differences and attempt to provide an overarching model for the role of ubiquitin in SG formation.","doi":"10.1007/s00294-016-0571-9","authors":"Nostramo R, Herman PK","authors_abbrev":"Nostramo R et al.","pubmed_publication_date":"Aug 2016","pubmed_entrez_date":"2016-02-08","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-02-09 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23940037","title":"The phosphatase Ptc7 induces coenzyme Q biosynthesis by activating the hydroxylase Coq7 in yeast.","citation":"J Biol Chem 2013 Sep 27;288(39):28126-37","abstract":"The study of the components of mitochondrial metabolism has potential benefits for health span and lifespan because the maintenance of efficient mitochondrial function and antioxidant capacity is associated with improved health and survival. In yeast, mitochondrial function requires the tight control of several metabolic processes such as coenzyme Q biosynthesis, assuring an appropriate energy supply and antioxidant functions. Many mitochondrial processes are regulated by phosphorylation cycles mediated by protein kinases and phosphatases. In this study, we determined that the mitochondrial phosphatase Ptc7p, a Ser/Thr phosphatase, was required to regulate coenzyme Q6 biosynthesis, which in turn activated aerobic metabolism and enhanced oxidative stress resistance. We showed that Ptc7p phosphatase specifically activated coenzyme Q6 biosynthesis through the dephosphorylation of the demethoxy-Q6 hydroxylase Coq7p. The current findings revealed that Ptc7p is a regulator of mitochondrial metabolism that is essential to maintain proper function of the mitochondria by regulating energy metabolism and oxidative stress resistance.","doi":"10.1074/jbc.M113.474494","authors":"Martín-Montalvo A, González-Mariscal I, Pomares-Viciana T, Padilla-López S, Ballesteros M, Vazquez-Fonseca L, Gandolfo P, Brautigan DL, Navas P, Santos-Ocaña C","authors_abbrev":"Martín-Montalvo A et al.","pubmed_publication_date":"27 Sep 2013","pubmed_entrez_date":"2013-08-14","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1556.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20682249","title":"Providing positional information with active transport on dynamic microtubules.","citation":"Biophys J 2010 Aug 04;99(3):726-35","abstract":"Microtubules (MTs) are dynamic protein polymers that change their length by switching between growing and shrinking states in a process termed dynamic instability. It has been suggested that the dynamic properties of MTs are central to the organization of the eukaryotic intracellular space, and that they are involved in the control of cell morphology, but the actual mechanisms are not well understood. Here, we present a theoretical analysis in which we explore the possibility that a system of dynamic MTs and MT end-tracking molecular motors is providing specific positional information inside cells. We compute the MT length distribution for the case of MT-length-dependent switching between growing and shrinking states, and analyze the accumulation of molecular motors at the tips of growing MTs. Using these results, we show that a transport system consisting of dynamic MTs and associated motor proteins can deliver cargo proteins preferentially to specific positions within the cell. Comparing our results with experimental data in the model organism fission yeast, we propose that the suggested mechanisms could play important roles in setting length scales during cellular morphogenesis.","doi":"10.1016/j.bpj.2010.05.026","authors":"Tischer C, Ten Wolde PR, Dogterom M","authors_abbrev":"Tischer C et al.","pubmed_publication_date":"04 Aug 2010","pubmed_entrez_date":"2010-08-05","publication_year":"2010","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10436025","title":"Fission yeast Pob1p, which is homologous to budding yeast Boi proteins and exhibits subcellular localization close to actin patches, is essential for cell elongation and separation.","citation":"Mol Biol Cell 1999 Aug;10(8):2745-57","abstract":"The fission yeast pob1 gene encodes a protein of 871 amino acids carrying an SH3 domain, a SAM domain, and a PH domain. Gene disruption and construction of a temperature-sensitive pob1 mutant indicated that pob1 is essential for cell growth. Loss of its function leads to quick cessation of cellular elongation. Pob1p is homologous to two functionally redundant Saccharomyces cerevisiae proteins, Boi1p and Boi2p, which are necessary for cell growth and relevant to bud formation. Overexpression of pob1 inhibits cell growth, causing the host cells to become round and swollen. In growing cells, Pob1p locates at cell tips during interphase and translocates near the division plane at cytokinesis. Thus, this protein exhibits intracellular dynamics similar to F-actin patches. However, Pob1p constitutes a layer, rather than patches, at growing cell tips. It generates two split discs flanking the septum at cytokinesis. The pob1-defective cells no longer elongate but swell gradually at the middle, eventually assuming a lemon-like morphology. Analysis using the pob1-ts allele revealed that Pob1p is also essential for cell separation. We speculate that Pob1p is located on growing plasma membrane, possibly through the function of actin patches, and may recruit proteins required for the synthesis of cell wall.","authors":"Toya M, Iino Y, Yamamoto M","authors_abbrev":"Toya M et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-08-06","publication_year":"1999","canto_session_key":"6286f8354d3d54ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-09 09:25:53","canto_approved_date":"2026-01-29 13:18:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-02-02 14:43:26","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC1D7.05","SPBC1289.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-06-09"},{"uniquename":"PMID:3198697","title":"The use of cell division cycle mutants to investigate the control of microtubule distribution in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1988 Mar;89 ( Pt 3):343-57","abstract":"We have characterized the changes in microtubule organization that occur through the cell division cycle of the fission yeast Schizosaccharomyces pombe by indirect immunofluorescence microscopy. During interphase, groups of cytoplasmic microtubules, independent of the spindle pole body (SPB), form an array extending between the cell tips. These microtubules are involved in positioning the nucleus at the cell equator and in the establishment of cell polarity. At mitosis, the interphase array disappears and is replaced by an intranuclear spindle extending between the now duplicated SPBs. Elongation of the spindle sees the appearance of astral microtubules emanating from the cytoplasmic face of the SPBs. These persist until the end of anaphase whereupon the spindle microtubules depolymerize and two microtubule organizing centres (MTOCs) at the cell equator re-establish the interphase array. We have used the unique properties of various cell division cycle mutants to investigate further the function of these different microtubule arrays and their temporal and positional control.","authors":"Hagan IM, Hyams JS","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"Mar 1988","pubmed_entrez_date":"1988-03-01","publication_year":"1988","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8449496","title":"Theoretical predictions and experimental observations of genomic mapping by anchoring random clones.","citation":"Genomics 1993 Feb;15(2):311-6","abstract":"Genome mapping by anchoring random clones has recently been the subject of intensive theoretical study. In this paper, differences between published predictions of properties of anchored groups of clones (\"contigs\") are analyzed and simplifications of the mathematical formulae describing these properties are presented. The theoretical predictions are compared with the experimental results from the physical mapping of the genome of Schizosaccharomyces pombe. Information about the number of genome sections with no anchored clone on them (\"oceans\") and the number of undetected overlaps between the contigs at a given stage of the experiment is required for the decision to change from the random strategy to that of a directed closure of gaps. We demonstrate that the expected number of oceans can be approximated by the number of groups of clones anchored by a single probe (\"singletons\"), as can the expected number of undetected overlaps between contigs by the number of contigs containing more than one anchor.","authors":"Grigoriev AV","authors_abbrev":"Grigoriev AV","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6092057","title":"The mitochondrial genome of the fission yeast Schizosaccharomyces pombe: highly homologous introns are inserted at the same position of the otherwise less conserved cox1 genes in Schizosaccharomyces pombe and Aspergillus nidulans.","citation":"EMBO J 1984 Sep;3(9):2129-36","abstract":"The DNA sequence of the second intron in the mitochondrial gene for subunit 1 of cytochrome oxidase (cox1), and the 3' part of the structural gene have been determined in Schizosaccharomyces pombe. Comparing the presumptive amino acid sequence of the 3' regions of the cox1 genes in fungi reveals similarly large evolutionary distances between Aspergillus nidulans, Saccharomyces cerevisiae and S. pombe. The comparison of exon sequences also reveals a stretch of only low homology and of general size variation among the fungal and mammalian genes, close to the 3' ends of the cox1 genes. The second intron in the cox1 gene of S. pombe contains an open reading frame, which is contiguous with the upstream exon and displays all characteristics common to class I introns. Three findings suggest a recent horizontal gene transfer of this intron from an Aspergillus type fungus to S. pombe. (i) The intron is inserted at exactly the same position of the cox1 gene, where an intron is also found in A. nidulans. (ii) Both introns contain the highest amino acid homology between the intronic unassigned reading frames of all fungi identified so far (70% identity over a stretch of 253 amino acids). However, in the most homologous region, a GC-rich sequence is inserted in the A. nidulans intron, flanked by two direct repeats of 5 bp. The 37-bp insert plus 5 bp of direct repeat amounts to an extra 42 bp in the A. nidulans intron. (iii) TGA codons are the preferred tryptophan codons compared with TGG in all mitochondrial protein coding sequences of fungi and mammalia.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Lang BF","authors_abbrev":"Lang BF","pubmed_publication_date":"Sep 1984","pubmed_entrez_date":"1984-09-01","publication_year":"1984","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR46423","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.06","HGNC:26151"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:39662831","title":"The putative polyamine transporter Shp2 facilitates phosphate export in an Xpr1-independent manner and contributes to high phosphate tolerance.","citation":"J Biol Chem 2024 Dec 09;:108056","abstract":"Phosphate (Pi) homeostasis at the cellular level is crucial, requiring coordinated Pi uptake, storage, and export. However, the regulatory mechanisms, particularly those governing Pi export, remain elusive, despite their relevance to human diseases like primary familial brain calcification. While Xpr1, conserved across eukaryotes, is the only known Pi exporter, the existence of additional Pi exporting factors is evident; however, these factors have been poorly characterized. Using the fission yeast Schizosaccharomyces pombe as a model, we have aimed to better understand cellular Pi homeostasis mechanisms. Previously, we showed three Pi regulators with SPX domains to be critical: Pqr1 (Pi uptake restrictor), Xpr1/Spx2, and the VTC complex (polyphosphate synthase). SPX domains bind to inositol pyrophosphate, modulating Pi regulator functions. The double mutant Δpqr1Δxpr1 hyper-accumulates Pi and undergoes cell death under high Pi conditions, indicating the necessity of both Pi uptake restriction and export. Notably, Δpqr1Δxpr1 exhibits residual Pi export activity independent of Xpr1, suggesting the presence of unidentified Pi exporters. To uncover these cryptic Pi exporters and regulators of Pi homeostasis, we conducted suppressor screening for high Pi hypersensitivity in Δpqr1Δxpr1. Among the eight suppressors identified, Shp2, a plasma-membrane protein, showed Pi export-facilitating activity in an Xpr1-independent manner, supporting cell proliferation at high Pi. The present results provide the first evidence for Pi export facilitator other than the established Xpr1, unprecedented in eukaryotes. As Shp2 is orthologous to the budding yeast Tpo1, a spermidine/polyamine transporter, a potential link between Pi homeostasis and polyamine metabolism can be speculated.","doi":"10.1016/j.jbc.2024.108056","authors":"Komamura T, Nishimura T, Ohta N, Takado M, Matsumoto T, Takeda K","authors_abbrev":"Komamura T et al.","pubmed_publication_date":"09 Dec 2024","pubmed_entrez_date":"2024-12-11","publication_year":"2024","canto_session_key":"140fc39c1d9e9588","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-12-13 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC530.15c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:15805471","title":"Ddb1 controls genome stability and meiosis in fission yeast.","citation":"Genes Dev 2005 Apr 01;19(7):853-62","abstract":"The human UV-damaged DNA-binding protein Ddb1 associates with cullin 4 ubiquitin ligases implicated in nucleotide excision repair (NER). These complexes also contain the signalosome (CSN), but NER-relevant ubiquitination targets have not yet been identified. We report that fission yeast Ddb1, Cullin 4 (Pcu4), and CSN subunits Csn1 and Csn2 are required for degradation of the ribonucleotide reductase (RNR) inhibitor protein Spd1. Ddb1-deficient cells have >20-fold increased spontaneous mutation rate. This is partly dependent on the error-prone translesion DNA polymerases. Spd1 deletion substantially reduced the mutation rate, suggesting that insufficient RNR activity accounts for approximately 50% of observed mutations. Epistasis analysis indicated that Ddb1 contributed to mutation avoidance and tolerance to DNA damage in a pathway distinct from NER. Finally, we show that Ddb1/Csn1/Cullin 4-mediated Spd1 degradation becomes essential when cells differentiate into meiosis. These results suggest that Ddb1, along with Cullin 4 and the signalosome, constitute a major pathway controlling genome stability, repair, and differentiation via RNR regulation.","authors":"Holmberg C, Fleck O, Hansen HA, Liu C, Slaaby R, Carr AM, Nielsen O","authors_abbrev":"Holmberg C et al.","pubmed_publication_date":"01 Apr 2005","pubmed_entrez_date":"2005-04-05","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4F6.15c","SPCC18B5.11c","SPCC1259.13","SPAC17H9.10c","SPBC19G7.01c","SPAC29B12.03","SPAC688.10","SPBC216.05","SPBC215.03c","SPAC3A11.08"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:15875007","title":"Cell biology: sterol sensor comes up for air.","citation":"Nature 2005 May 05;435(7038):37-8","abstract":"","authors":"Garza RM, Hampton RY","authors_abbrev":"Garza RM et al.","pubmed_publication_date":"05 May 2005","pubmed_entrez_date":"2005-05-06","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15941470","title":"Nuclear distribution and chromatin association of DNA polymerase alpha-primase is affected by TEV protease cleavage of Cdc23 (Mcm10) in fission yeast.","citation":"BMC Mol Biol 2005 Jun 07;6:13","abstract":"Cdc23/Mcm10 is required for the initiation and elongation steps of DNA replication but its biochemical function is unclear. Here, we probe its function using a novel approach in fission yeast, involving Cdc23 cleavage by the TEV protease.\nInsertion of a TEV protease cleavage site into Cdc23 allows in vivo removal of the C-terminal 170 aa of the protein by TEV protease induction, resulting in an S phase arrest. This C-terminal fragment of Cdc23 is not retained in the nucleus after cleavage, showing that it lacks a nuclear localization signal and ability to bind to chromatin. Using an in situ chromatin binding procedure we have determined how the S phase chromatin association of DNA polymerase alpha-primase and the GINS (Sld5-Psf1-Psf2-Psf3) complex is affected by Cdc23 inactivation. The chromatin binding and sub-nuclear distribution of DNA primase catalytic subunit (Spp1) is affected by Cdc23 cleavage and also by inactivation of Cdc23 using a degron allele, implying that DNA polymerase alpha-primase function is dependent on Cdc23. In contrast to the effect on Spp1, the chromatin association of the Psf2 subunit of the GINS complex is not affected by Cdc23 inactivation.\nAn important function of Cdc23 in the elongation step of DNA replication may be to assist in the docking of DNA polymerase alpha-primase to chromatin.","authors":"Yang X, Gregan J, Lindner K, Young H, Kearsey SE","authors_abbrev":"Yang X et al.","pubmed_publication_date":"07 Jun 2005","pubmed_entrez_date":"2005-06-09","publication_year":"2005","canto_session_key":"4488533ca5f8fdc3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-09 10:00:55","canto_approved_date":"2024-03-28 16:39:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-02-06 14:29:25","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6B12.10c","SPBC725.13c","SPBC1347.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-02-09"},{"uniquename":"PMID:8355807","title":"Fission yeast wee1 protein kinase is not required for DNA damage-dependent mitotic arrest.","citation":"Nature 1993 Aug 26;364(6440):824-7","abstract":"Checkpoints maintain the dependency relationships between discrete events in the cell cycle (for example, ensuring mitosis does not occur before DNA replication is complete). In Schizosaccharomyces pombe, mitotic checkpoints monitor DNA synthesis and the presence of DNA damage. The replication-dependent mitotic checkpoint prevents mitosis by inactivating p34cdc2 kinase. The mechanism by which the DNA damage checkpoint interacts with the mitotic machinery is distinct from that used by the replication checkpoint. The activity of p34cdc2 is controlled, in part, by the wee1 protein kinase, which inactivates cdc2 through phosphorylation at tyrosine-15 (ref. 7). Here we report normal mitotic arrest after DNA damage in S. pombe cells in which the wee1 gene is defective or missing. We suggest why these findings contradict a recent report which suggested that the wee1 gene product was required for DNA damage-dependent mitotic arrest.","authors":"Barbet NC, Carr AM","authors_abbrev":"Barbet NC et al.","pubmed_publication_date":"26 Aug 1993","pubmed_entrez_date":"1993-08-26","publication_year":"1993","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34666001","title":"Detection of surface forces by the cell-wall mechanosensor Wsc1 in yeast.","citation":"Dev Cell 2021 Oct 25;56(20):2856-2870.e7","abstract":"Surface receptors of animal cells, such as integrins, promote mechanosensation by forming clusters as signaling hubs that transduce tensile forces. Walled cells of plants and fungi also feature surface sensors, with long extracellular domains that are embedded in their cell walls (CWs) and are thought to detect injuries and promote repair. How these sensors probe surface forces remains unknown. By studying the conserved CW sensor Wsc1 in fission yeast, we uncovered the formation of micrometer-sized clusters at sites of force application onto the CW. Clusters assembled within minutes of CW compression, in dose dependence with mechanical stress and disassembled upon relaxation. Our data support that Wsc1 accumulates to sites of enhanced mechanical stress through reduced lateral diffusivity, mediated by the binding of its extracellular WSC domain to CW polysaccharides, independent of canonical polarity, trafficking, and downstream CW regulatory pathways. Wsc1 may represent an autonomous module to detect and transduce local surface forces onto the CW.","doi":"10.1016/j.devcel.2021.09.024","authors":"Neeli-Venkata R, Diaz CM, Celador R, Sanchez Y, Minc N","authors_abbrev":"Neeli-Venkata R et al.","pubmed_publication_date":"25 Oct 2021","pubmed_entrez_date":"2021-10-19","publication_year":"2021","canto_session_key":"8de8896718b55bd8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nicolas Minc","canto_first_approved_date":"2022-07-22 14:04:13","canto_approved_date":"2023-05-04 11:17:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-07-25 12:50:05","canto_added_date":"2021-10-23 00:15:07","annotation_curators":[{"name":"Nicolas Minc","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":41,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.12","SPCC645.07","SPAC1006.06","SPBC106.20","SPCC970.09","SPBC146.13c","SPCC1223.06","SPAC9G1.11c","SPAC2F7.03c","SPCC1183.11","SPCC1840.02c","SPAC4F10.15c","SPAC4F10.11","SPBC30B4.01c","SPAC11G7.01","SPAC688.11","SPBC1706.01","SPAC24B11.06c","SPAC18G6.15","SPCC1919.10c","SPCC895.05","SPAC17G8.14c","SPBC119.08","SPBC32F12.11"],"gene_count":24,"ltp_gene_count":23,"approved_date":"2022-07-22"},{"uniquename":"PMID:17304622","title":"Gene expressions and enzyme analyses in the Schizosaccharomyces pombe Deltapap1 transcription factor mutant exposed to Cd(2+).","citation":"J Basic Microbiol 2007 Feb;47(1):74-83","abstract":"The objective of this study was to investigate the role of the Pap1 transcription factor in response to long-term Cd(2+) stress. The Schizosaccharomyces pombe wild-type strain and the Deltapap1 mutant, treated with 0.5 mM CdSO(4), were used in antioxidant enzyme and gene expression experiments. The Deltapap1 mutant proved to be sensitive to Cd(2+) in the spot test assay, suggesting that the Pap1 transcription factor plays an important role in the response to Cd(2+) stress. The Cd(2+) uptake was the same in both strains. Determination of the superoxide level in the wild-type strain proved that superoxide was generated, suggesting that long-term Cd(2+) treatment could trigger oxidative stress. Furthermore, the Deltapap1 mutant displayed higher amounts of superoxide. These results were supported by the significantly lower amount of peroxide generated in the reaction catalyzed by superoxide dismutase (SOD). The Deltapap1 mutant had a significantly lower glutathione S-transferase specific activity than that of the wild-type strain during long-term Cd(2+) stress, caused by the lower GSH and sulfide assimilation. We have demonstrated that GST III activity was not induced by Cd(2+) stress in the Deltapap1 mutant. The overall low GST activity was not sufficient for the cell to eliminate Cd(2+) caused damage and could result in a Cd(2+)-sensitive phenotype of the Deltapap1 mutant. The RT-PCR and Northern blot experiments proved that gst2 was not induced either by short-term or by long-term Cd(2+) treatment. The SPCC965.06 (a putative K(+) ion channel subunit) gene expression increased, while the hmt1 (an ABC-type vacuolar transporter protein) expression decreased in both strains. No detectable alteration in the mRNA levels of, gpx1, hmt2, sod1, sod, and trx1 was observed. SOD enzyme analyses revealed that the absence of Pap1 protein could result in a lower SODs activity and affect the sulfate assimilation. This is the first report on the fact that the Pap1 transcription factor could play an important role in the cellular post-transcriptional/post-translational enzyme activity induction processes of SODs that occur in response to Cd(2+).","authors":"Takács K, Gazdag Z, Raspor P, Pesti M","authors_abbrev":"Takács K et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-02-17","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16142912","title":"Dissecting the domain structure of Cdc4p, a myosin essential light chain involved in Schizosaccharomyces pombe cytokinesis.","citation":"Biochemistry 2005 Sep 13;44(36):12136-48","abstract":"Cytokinesis is the process by which one cell divides into two. Key in the cytokinetic mechanism of Schizosaccharomyces pombe is the contractile ring myosin, which consists of two heavy chains (Myo2p), two essential light chains (Cdc4p), and two regulatory light chains (Rlc1p). Cdc4p is a dumbbell-shaped EF-hand protein composed of N- and C-terminal domains separated by a flexible linker. The properties of these two domains are of particular interest because each is hypothesized to have independent functions in binding different components of the cytokinesis machinery. To help define these properties, we used NMR spectroscopy to compare the structure, stability, and dynamics of the isolated N- and C-terminal domains with one another and with native Cdc4p. On the basis of invariant chemical shifts, the N-domain retains the same structure in isolation as in the context of the full-length Cdc4p, whereas the C-domain appears markedly perturbed. This perturbation results from intramolecular binding of the residual linker sequence at the N-terminus of the C-domain in a mode similar to that used by native Cdc4p to associate with target polypeptide sequences. NMR relaxation, thermal denaturation, and amide hydrogen exchange experiments also indicate that the C-domain is less stable and more dynamic than the N-domain, both in isolation and in the full-length protein. We hypothesize that these properties reflect a conformational plasticity of the C-domain, which may allow Cdc4p to interact with several regulatory or contractile ring proteins necessary for cytokinesis.","authors":"Escobar-Cabrera E, Venkatesan M, Desautels M, Hemmingsen SM, McIntosh LP","authors_abbrev":"Escobar-Cabrera E et al.","pubmed_publication_date":"13 Sep 2005","pubmed_entrez_date":"2005-09-07","publication_year":"2005","canto_session_key":"efbb9dec97a0e189","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-01-01 16:57:29","canto_approved_date":"2021-01-01 16:57:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-01 16:57:05","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP8A3.08"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2021-01-01"},{"uniquename":"PMID:10749974","title":"Characterization of the Schizosaccharomyces pombe orthologue of the human survival motor neuron (SMN) protein.","citation":"Hum Mol Genet 2000 Mar 22;9(5):675-84","abstract":"Childhood onset spinal muscular atrophy (SMA) is a common autosomal recessive disorder primarily characterized by the loss of lower alpha motor neurons. The underlying chromosomal defects causing SMA have been found in the survival motor neuron (SMN) gene. SMN has been shown previously to play a role in both snRNP biogenesis and mRNA processing, although direct evidence for the relationship between SMN and disease pathology has not been elucidated. SMN orthologues have been isolated in many species including Caenorhabditis elegans and Danio rerio. To study the function of SMN, we have identified and characterized the Schizosaccharomyces pombe orthologue of human SMN, smn1 (+). We have demonstrated that smn1 (+) is essential for viability in S.pombe and yeast expressing missense mutations in Smn1p, which mimic mutations in patients with Type I SMA, show significant mislocalization of the protein and a decrease in cell viability. Wild-type Smn1p is localized predominantly in the nucleus whereas yeast expressing Smn1p with missense mutations or deletions of specific domains of the protein accumulate cytoplasmic aggregates. Overexpression of Smn1p results in an increase in the growth rate of cells. Furthermore, mutations within two highly conserved protein interaction domains have a dominant-negative effect on growth, indicating that each domain is of functional significance in S.pombe. These dominant phenotypes can be suppressed by overexpression of murine Smn in the same cell. Given the structural and functional similarities between the protein in fission yeast and higher eukaryotes, S.pombe will be an ideal organism to study the role of SMN in RNA processing.","authors":"Owen N, Doe CL, Mellor J, Davies KE","authors_abbrev":"Owen N et al.","pubmed_publication_date":"22 Mar 2000","pubmed_entrez_date":"2000-04-06","publication_year":"2000","canto_session_key":"38681343ebb7c7fc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-01 16:56:38","canto_approved_date":"2022-02-08 08:48:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-01 16:56:29","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-01"},{"uniquename":"PMID:18553361","title":"Novel interactions of fission yeast kinesin 8 revealed through in vivo expression of truncation alleles.","citation":"Cell Motil Cytoskeleton 2008 Aug;65(8):626-40","abstract":"Fission yeast expresses two kinesin 8s, klp5+ and klp6+, which are important for diverse cellular functions: mitosis, meiosis, and the maintenance of normal cell morphology. During vegetative growth these motors display complex localization patterns, moving from the cytoplasm during interphase to the kinetochores in early mitosis, the interpolar spindle in anaphase B, and then back into the cytoplasm. We have expressed GFP-tagged alleles of domains from these motors, seeking the signals required for their localizations. The tail of Klp5p localized to the interphase nucleus, more specifically to telomeres. Addition of the neck re-directed this fragment to microtubules in the cytoplasm. Klp6-tail and the neck-tail domains of both motors localized at microtubule ends. Klp6-neck-tail localized to the spindle in early mitosis but to the pole-proximal ends of the spindle in anaphase B. The Klp5-motor and motor-neck localized to microtubules, often causing them to bundle. Over-expression of Klp6-motor or motor-neck resulted in shorter microtubules. These localization patterns were no different when constructs were expressed in strains lacking either or both of the endogenous, full-length proteins. Our results indicate that the localization signals for these kinesins are not derived from simple amino acid sequences but from complex interactions among multiple domains of each motor.","doi":"10.1002/cm.20289","authors":"West RR, McIntosh JR","authors_abbrev":"West RR et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-06-17","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21310294","title":"Cell cycle regulated gene expression in yeasts.","citation":"Adv Genet 2011;73:51-85","abstract":"The regulation of gene expression through the mitotic cell cycle, so that genes are transcribed at particular cell cycle times, is widespread among eukaryotes. In some cases, it appears to be important for control mechanisms, as deregulated expression results in uncontrolled cell divisions, which can cause cell death, disease, and malignancy. In this review, I describe the current understanding of such regulated gene expression in two established simple eukaryotic model organisms, the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe. In these two yeasts, the global pattern of cell cycle gene expression has been well described, and most of the transcription factors that control the various waves of gene expression, and how they are in turn themselves regulated, have been characterized. As related mechanisms occur in all other eukaryotes, including humans, yeasts offer an excellent paradigm to understand this important molecular process.","doi":"10.1016/B978-0-12-380860-8.00002-1","authors":"McInerny CJ","authors_abbrev":"McInerny CJ","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-02-12","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC04442","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000011","title":"Hidden Markov Models (TIGR)","abstract":"A Hidden Markov Model (HMM) is a statistical representation of patterns found in a data set. When using HMMs with proteins, the HMM is a statistical model of the patterns of the amino acids found in a multiple alignment of a set of proteins called the \"seed\". Seed proteins are chosen based on sequence similarity to each other. Seed members can be chosen with different levels of relationship to each other. They can be members of a superfamily (ex. ABC transporter, ATP-binding proteins), they can all share the same exact specific function (ex. biotin synthase) or they could share another type of relationship of intermediate specificity (ex. subfamily, domain). New proteins can be scored against the model generated from the seed according to how closely the patterns of amino acids in the new proteins match those in the seed. There are two scores assigned to the HMM which allow annotators to judge how well any new protein scores to the model. Proteins scoring above the \"trusted cutoff\" score can be assumed to be part of the group defined by the seed. Proteins scoring below the \"noise cutoff\" score can be assumed to NOT be a part of the group. Proteins scoring between the trusted and noise cutoffs may be part of the group but may not. One of the important features of HMMs is that they are built from a multiple alignment of protein sequences, not a pairwise alignment. This is significant, since shared similarity between many proteins is much more likely to indicate shared functional relationship than sequence similarity between just two proteins. The usefulness of an HMM is directly related to the amount of care that is taken in chosing the seed members, building a good multiple alignment of the seed members, assessing the level of specificity of the model, and choosing the cutoff scores correctly. In order to properly assess what functional relevance an above-trusted scoring HMM match has to a query, one must carefully determine what the functional scope of the HMM is. If the HMM models proteins that all share the same function then it is likely possible to assign a specific function to high-scoring match proteins based on the HMM. If the HMM models proteins that have a wide variety of functions, then it will not be possible to assign a specific function to the query based on the HMM match, however, depending on the nature of the HMM in question, it may be possible to assign a more general (family or subfamily level) function. In order to determine the functional scope of an HMM, one must carefully read the documentation associated with the HMM. The annotator must also consider whether the function attributed to the proteins in the HMM makes sense for the query based on what is known about the organism in which the query protein resides and in light of any other information that might be available about the query protein. After carefully considering all of these issues the annotator makes an annotation.","authors":"Michelle Gwinn, TIGR curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16963626","title":"A transcription factor cascade involving Fep1 and the CCAAT-binding factor Php4 regulates gene expression in response to iron deficiency in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2006 Nov;5(11):1866-81","abstract":"We have identified genes encoding candidate proteins involved in iron storage (pcl1+), the tricarboxylic acid cycle (sdh4+), and iron-sulfur cluster assembly (isa1+) that are negatively regulated in response to iron deprivation. Promoter deletion and site-directed mutagenesis permitted identification of a new cis-regulatory element in the promoter region of the pcl1+ gene. This cis-acting regulatory sequence containing the pentanucleotide sequence CCAAT is responsible for transcriptional repression of pcl1+ under low iron supply conditions. In Schizosaccharomyces pombe, the CCAAT-binding factor is a heteromeric DNA-binding complex that contains three subunits, designated Php2, Php3, and Php5. Inactivation of the php2+ locus negatively affects the transcriptional competency of pcl1+. A fourth subunit, designated Php4, is not essential for the transcriptional activation of target genes under basal and iron-replete conditions. We demonstrate that, in response to iron-limiting conditions, Php4 is required for down-regulation of pcl1+, sdh4+, and isa1+ mRNA levels. In vivo RNase protection studies reveal that the expression of php4+ is negatively regulated by iron and that this regulated expression requires a functional fep1+ gene. The results of these studies reveal that Fep1 represses php4+ expression in response to iron. In contrast, when iron is scarce, Fep1 becomes inactive and php4+ is expressed to act as a regulatory subunit of the CCAAT-binding factor that is required to block pcl1+, sdh4+, and isa1+ gene transcription.","authors":"Mercier A, Pelletier B, Labbé S","authors_abbrev":"Mercier A et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-09-12","publication_year":"2006","canto_session_key":"8b7a4bf27652b9d5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-05-24 08:15:03","canto_approved_date":"2024-04-03 12:39:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-24 08:14:57","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.16","YKL109W","SPAC23E2.01","SPBC725.11c","SPBC16E9.01c","SPBC3B8.02","SPAC23C11.08","SPAC1F7.08","SPBC1683.10c","SPCC645.03c","SPBC1718.07c"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2019-05-24"},{"uniquename":"PMID:10485849","title":"Fission yeast condensin complex: essential roles of non-SMC subunits for condensation and Cdc2 phosphorylation of Cut3/SMC4.","citation":"Genes Dev 1999 Sep 01;13(17):2271-83","abstract":"The condensin complex in frog extracts, containing two SMC (structural maintenance of chromosomes) and three non-SMC subunits, promotes mitotic chromosome condensation, and its supercoiling activity increases during mitosis by Cdc2 phosphorylation. Here, we report that fission yeast has the same five-member condensin complex, each of which is essential for mitotic condensation. The condensin complex was purified and the subunits were identified by microsequencing. Cnd1, Cnd2, and Cnd3, three non-SMC subunits showing a high degree of sequence conservation to frog subunits, are essential for viability, and their gene disruption leads to a phenotype indistinguishable from that observed in cut3-477 and cut14-208, known mutations in SMC4 and SMC2-like subunits. Condensin subunits tagged with GFP were observed to alter dramatically their localization during the cell cycle, enriched in the nucleus during mitosis, but cytoplasmic during other stages. This stage-specific alteration in localization requires mitosis-specific phosphorylation of the T19 Cdc2 site in Cut3. The T19 site is phosphorylated in vitro by Cdc2 kinase and shows the maximal phosphorylation in metaphase in vivo. Its alanine substitution mutant fails to suppress the temperature-sensitive phenotype of cut3-477, and shows deficiency in condensation, probably because Cut3 T19A remains cytoplasmic. Therefore, direct Cdc2 phosphorylation of fission yeast condensin may facilitate its nuclear accumulation during mitosis.","authors":"Sutani T, Yuasa T, Tomonaga T, Dohmae N, Takio K, Yanagida M","authors_abbrev":"Sutani T et al.","pubmed_publication_date":"01 Sep 1999","pubmed_entrez_date":"1999-09-15","publication_year":"1999","canto_session_key":"8d860f7ec28a89b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-03-14 10:15:52","canto_approved_date":"2026-01-29 15:01:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-08 10:23:35","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.13","SPBP4H10.06c","SPCC188.03","SPCC306.03c","SPBC146.03c","SPBC11B10.09","SPAC1805.17"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-03-14"},{"uniquename":"PMID:22927644","title":"Replication fork collapse and genome instability in a deoxycytidylate deaminase mutant.","citation":"Mol Cell Biol 2012 Nov;32(21):4445-54","abstract":"Ribonucleotide reductase (RNR) and deoxycytidylate deaminase (dCMP deaminase) are pivotal allosteric enzymes required to maintain adequate pools of deoxyribonucleoside triphosphates (dNTPs) for DNA synthesis and repair. Whereas RNR inhibition slows DNA replication and activates checkpoint responses, the effect of dCMP deaminase deficiency is largely unknown. Here, we report that deleting the Schizosaccharomyces pombe dcd1(+) dCMP deaminase gene (SPBC2G2.13c) increases dCTP ∼30-fold and decreases dTTP ∼4-fold. In contrast to the robust growth of a Saccharomyces cerevisiae dcd1Δ mutant, fission yeast dcd1Δ cells delay cell cycle progression in early S phase and are sensitive to multiple DNA-damaging agents, indicating impaired DNA replication and repair. DNA content profiling of dcd1Δ cells differs from an RNR-deficient mutant. Dcd1 deficiency activates genome integrity checkpoints enforced by Rad3 (ATR), Cds1 (Chk2), and Chk1 and creates critical requirements for proteins involved in recovery from replication fork collapse, including the γH2AX-binding protein Brc1 and Mus81 Holliday junction resolvase. These effects correlate with increased nuclear foci of the single-stranded DNA binding protein RPA and the homologous recombination repair protein Rad52. Moreover, Brc1 suppresses spontaneous mutagenesis in dcd1Δ cells. We propose that replication forks stall and collapse in dcd1Δ cells, burdening DNA damage and checkpoint responses to maintain genome integrity.","doi":"10.1128/MCB.01062-12","authors":"Sánchez A, Sharma S, Rozenzhak S, Roguev A, Krogan NJ, Chabes A, Russell P","authors_abbrev":"Sánchez A et al.","pubmed_publication_date":"Nov 2012","pubmed_entrez_date":"2012-08-29","publication_year":"2012","canto_session_key":"83b3cec202522e28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-08-29 09:02:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-08-09 15:17:57","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":41,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC644.14c","SPAC3G6.06c","SPBC582.05c","SPBC216.06c","SPCC4G3.05c","SPAC694.06c","SPAC1952.07","SPBC651.10","SPCC18B5.11c","SPBC216.05","SPCC338.08","SPCC23B6.05c","SPBC2G2.13c","SPAC17H9.10c"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2013-08-09"},{"uniquename":"PMID:21098295","title":"Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution.","citation":"Proc Natl Acad Sci U S A 2010 Dec 07;107(49):20992-7","abstract":"The structure of the 26S proteasome from Schizosaccharomyces pombe has been determined to a resolution of 9.1 Å by cryoelectron microscopy and single particle analysis. In addition, chemical cross-linking in conjunction with mass spectrometry has been used to identify numerous residue pairs in close proximity to each other, providing an array of spatial restraints. Taken together these data clarify the topology of the AAA-ATPase module in the 19S regulatory particle and its spatial relationship to the α-ring of the 20S core particle. Image classification and variance analysis reveal a belt of high \"activity\" surrounding the AAA-ATPase module which is tentatively assigned to the reversible association of proteasome interacting proteins and the conformational heterogeneity among the particles. An integrated model is presented which sheds light on the early steps of protein degradation by the 26S complex.","doi":"10.1073/pnas.1015530107","authors":"Bohn S, Beck F, Sakata E, Walzthoeni T, Beck M, Aebersold R, Förster F, Baumeister W, Nickell S","authors_abbrev":"Bohn S et al.","pubmed_publication_date":"07 Dec 2010","pubmed_entrez_date":"2010-11-25","publication_year":"2010","canto_session_key":"9384b5ffb973121c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-03-23 14:35:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-08-07 12:27:54","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC576.10c","SPAPB8E5.02c","SPAC23D3.07","SPAC31G5.13","SPCC1682.10","SPBC582.07c","SPBC646.16","SPAC31A2.04c","SPBC4C3.10c","SPAC22F8.06","SPAC3A11.12c","SPCC1442.06","SPBC106.16","SPAC23G3.11","SPBC16C6.07c","SPAC6G9.08","SPBC23G7.12c","SPAC13C5.01c","SPAC637.10c","SPBP19A11.03c","SPBC119.01","SPCC16A11.16c","SPCC63.12c","SPBC409.06","SPBC342.04","SPAC6G10.04c","SPCC1795.04c","SPAC4A8.13c","SPBC16G5.01","SPBC4.07c","SPBC17D11.07c","SPBC577.10","SPAC323.02c","SPAC607.05","SPAC1420.03","SPCC1682.16"],"gene_count":36,"ltp_gene_count":33,"approved_date":"2017-08-07"},{"uniquename":"EMBL:AU010786","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12546793","title":"Mitotic hyperphosphorylation of the fission yeast SIN scaffold protein cdc11p is regulated by the protein kinase cdc7p.","citation":"Curr Biol 2003 Jan 21;13(2):168-72","abstract":"The fission yeast septation initiation network (SIN) triggers the onset of septum formation and cytokinesis. SIN proteins signal from the spindle pole body (SPB), to which they bind in a cell cycle-dependent manner, via the scaffold proteins sid4p and cdc11p. cdc11p becomes hyperphosphorylated during anaphase, when the SIN is active. We have investigated the phosphorylation state of cdc11p during mitosis in various mutant backgrounds. We show that association of cdc11p with the spindle pole body is required for its phosphorylation and that ectopic activation of the SIN results in hyperphosphorylation of cdc11p. We demonstrate that mitotic hyperphosphorylation of cdc11p requires the activity of cdc7p and that its dephosphorylation at the end of mitosis requires PP2A-par1p. Furthermore, spindle checkpoint arrest prevents cdc11p hyperphosphorylation. Finally, we show that the septation inhibitor byr4p interacts preferentially with hypophosphorylated cdc11p. We conclude that cdc11p hyperphosphorylation correlates with activation of the SIN and that this may be mediated primarily by cdc7p in vivo.","authors":"Krapp A, Cano E, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"21 Jan 2003","pubmed_entrez_date":"2003-01-28","publication_year":"2003","canto_session_key":"a2468b284d810cf8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-12-09 20:59:49","canto_approved_date":"2025-02-28 09:04:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-12-06 11:54:07","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC428.13c","SPCC188.02","SPBC21.06c","SPAC6F6.08c","SPAC23C11.16","SPBC106.01","SPAC1565.06c","SPCC1739.11c","SPAC222.10c","SPBC26H8.07c","SPAC9G1.09","SPAC19E9.02","SPAC24B11.11c","SPAC1782.09c","SPBC244.01c"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2021-12-09"},{"uniquename":"PMID:9016645","title":"Molecular cloning and analysis of Schizosaccharomyces pombe Reb1p: sequence-specific recognition of two sites in the far upstream rDNA intergenic spacer.","citation":"Nucleic Acids Res 1997 Feb 15;25(4):904-10","abstract":"The coding sequences for a Schizosaccharomyces pombe sequence-specific DNA binding protein, Reb1p, have been cloned. The predicted S. pombe Reb1p is 24-29% identical to mouse TTF-1 (transcription termination factor-1) and Saccharomyces cerevisiae REB1 protein, both of which direct termination of RNA polymerase I catalyzed transcripts. The S.pombe Reb1 cDNA encodes a predicted polypeptide of 504 amino acids with a predicted molecular weight of 58.4 kDa. The S. pombe Reb1p is unusual in that the bipartite DNA binding motif identified originally in S.cerevisiae and Klyveromyces lactis REB1 proteins is uninterrupted and thus S.pombe Reb1p may contain the smallest natural REB1 homologous DNA binding domain. Its genomic coding sequences were shown to be interrupted by two introns. A recombinant histidine-tagged Reb1 protein bearing the rDNA binding domain has two homologous, sequence-specific binding sites in the S. pomber DNA intergenic spacer, located between 289 and 480 nt downstream of the end of the approximately 25S rRNA coding sequences. Each binding site is 13-14 bp downstream of two of the three proposed in vivo termination sites. The core of this 17 bp site, AGGTAAGGGTAATGCAC, is specifically protected by Reb1p in footprinting analysis.","authors":"Zhao A, Guo A, Liu Z, Pape L","authors_abbrev":"Zhao A et al.","pubmed_publication_date":"15 Feb 1997","pubmed_entrez_date":"1997-02-15","publication_year":"1997","canto_session_key":"f5fa68b24ab3f8be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-11 17:18:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 17:10:24","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1198.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-11"},{"uniquename":"PMID:7239444","title":"Only one aminopeptidase in Schizosaccharomyces pombe.","citation":"Hoppe Seylers Z Physiol Chem 1981 Apr;362(4):459-63","abstract":"","authors":"Atmanspacher D, Röhm KH","authors_abbrev":"Atmanspacher D et al.","pubmed_publication_date":"Apr 1981","pubmed_entrez_date":"1981-04-01","publication_year":"1981","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15208306","title":"Human Smp3p adds a fourth mannose to yeast and human glycosylphosphatidylinositol precursors in vivo.","citation":"J Biol Chem 2004 Aug 20;279(34):36083-92","abstract":"Yeast and human glycosylphosphatidylinositol (GPI) precursors differ in the extent to which a fourth mannose is present as a side branch of the third core mannose. A fourth mannose addition to GPIs has scarcely been detected in studies of mammalian GPI synthesis but is an essential step in the Saccharomyces cerevisiae pathway. We report that human SMP3 encodes a functional homolog of the yeast Smp3 GPI fourth mannosyl-transferase. Expression of hSMP3 in yeast complements growth and biochemical defects of smp3 mutants and permits in vivo mannosylation of trimannosyl (Man(3))-GPIs. Immunolocalization shows that hSmp3p resides in the endoplasmic reticulum in human cells. Northern analysis of mRNA from human tissues and cell lines indicates that hSMP3 is expressed in most tissues, with the highest levels in brain and colon, but its mRNA is nearly absent from cultured human cell lines. Correspondingly, increasing expression of hSMP3 in cultured HeLa cells causes abundant formation of three putative tetramannosyl (Man(4))-GPIs. Our data indicate that hSmp3p functions as a mannosyltransferase that adds a fourth mannose to certain Man(3)-GPIs during biosynthesis of the human GPI precursor, and suggest it may do so in a tissue-specific manner.","authors":"Taron BW, Colussi PA, Wiedman JM, Orlean P, Taron CH","authors_abbrev":"Taron BW et al.","pubmed_publication_date":"20 Aug 2004","pubmed_entrez_date":"2004-06-23","publication_year":"2004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1934126","title":"Common genes and pathways in the regulation of the mitotic and meiotic cell cycles of Schizosaccharomyces pombe.","citation":"Curr Genet 1991 Aug;20(3):199-204","abstract":"Cell division cycle mutants defective in G1, DNA replication or nuclear division were tested for sporulation at semi-restrictive temperatures. In cdc1-7, cdc5-120, cdc17-L16 and cdc18-46 no abnormalities were observed; cdc10-129, cdc20-M10, cdc21-M6B, cdc23-M36 and cdc24-M38 formed four-spored asci but with a low efficiency; cdc22-M45 was completely defective in meiosis, but could conjugate and formed zygotes with a single nucleus. Mutants defective in the mitotic initiation genes cdc2, cdc25 and cdc13 were blocked in meiosis II. None of the wee1-50, adh.nim1+ and win1+ alleles had any affect on sporulation, suggesting that their interactions with cdc25 and cdc2 are specific to mitosis. The meiotic function of cdc13 is TBZ-sensitive and probably exerted downstream of cdc2. Single mutants in cut1 or cut2 did not effect sporulation, whereas the double mutant cut1 cut2 formed two-spored asci. The results demonstrate that the cell division cycle and the meiotic developmental pathway share common genes and regulatory cascades.","authors":"Grallert B, Sipiczki M","authors_abbrev":"Grallert B et al.","pubmed_publication_date":"Aug 1991","pubmed_entrez_date":"1991-08-01","publication_year":"1991","canto_session_key":"774b7f1a9f489629","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-09 13:38:46","canto_approved_date":"2023-09-11 07:55:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-08 10:49:56","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.04","SPBC14C8.01c","SPBC1347.10","SPAC24H6.05","SPAC1F7.05","SPAC20G8.01","SPCC16A11.17","SPAC8F11.07c","SPBC14C8.07c","SPBC582.03","SPCC18B5.03","SPBC336.12c","SPBC11B10.09","SPBC25H2.13c","SPAC1006.09","SPAC644.12","SPAC27E2.05","SPAC644.06c"],"gene_count":18,"ltp_gene_count":18,"approved_date":"2015-06-09"},{"uniquename":"PMID:25483043","title":"Proteins involved in the degradation of cytoplasmic mRNA in the major eukaryotic model systems.","citation":"RNA Biol 2014;11(9):1122-36","abstract":"The process of mRNA decay and surveillance is considered to be one of the main posttranscriptional gene expression regulation platforms in eukaryotes. The degradation of stable, protein-coding transcripts is normally initiated by removal of the poly(A) tail followed by 5'-cap hydrolysis and degradation of the remaining mRNA body by Xrn1. Alternatively, the exosome complex degrades mRNA in the 3'>5'direction. The newly discovered uridinylation-dependent pathway, which is present in many different organisms, also seems to play a role in bulk mRNA degradation. Simultaneously, to avoid the synthesis of incorrect proteins, special cellular machinery is responsible for the removal of faulty transcripts via nonsense-mediated, no-go, non-stop or non-functional 18S rRNA decay. This review is focused on the major eukaryotic cytoplasmic mRNA degradation pathways showing many similarities and pointing out main differences between the main model-species: yeast, Drosophila, plants and mammals.","doi":"10.4161/rna.34406","authors":"Siwaszek A, Ukleja M, Dziembowski A","authors_abbrev":"Siwaszek A et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-12-09","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-12-25 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27462451","title":"The Chp1 chromodomain binds the H3K9me tail and the nucleosome core to assemble heterochromatin.","citation":"Cell Discov 2016;2:16004","abstract":"To maintain genome stability, cells pack large portions of their genome into silent chromatin or heterochromatin. Histone H3 lysine 9 methylation, a hallmark of heterochromatin, is recognized by conserved readers called chromodomains. But how chromodomains interact with their actual binding partner, the H3K9 methylated nucleosome, remains elusive. We have determined the structure of a nucleosome trimethylated at lysine 9 of histone H3 (H3K9me3 Nucleosome) in a complex with the chromodomain of Chp1, a protein required for RNA interference-dependent heterochromatin formation in fission yeast. The cryo-electron microscopy structure reveals that the chromodomain of Chp1 binds the histone H3 lysine 9 methylated tail and the core of the nucleosome, primarily histones H3 and H2B. Mutations in chromodomain of Chp1 loops, which interact with the nucleosome core, abolished this interaction in vitro. Moreover, fission yeast cells with Chp1 loop mutations have a defect in Chp1 recruitment and heterochromatin formation. This study reveals the structural basis for heterochromatic silencing and suggests that chromodomains could read histone code in the H3 tail and the nucleosome core, which would provide an additional layer of regulation.","doi":"10.1038/celldisc.2016.4","authors":"Zocco M, Marasovic M, Pisacane P, Bilokapic S, Halic M","authors_abbrev":"Zocco M et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-07-28","publication_year":"2016","canto_session_key":"a1b668e681ef3920","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-29 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1834.04","SPAC18G6.02c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9592143","title":"Single point mutations located outside the inter-monomer domains abolish trimerization of Schizosaccharomyces pombe PCNA.","citation":"Nucleic Acids Res 1998 Jun 01;26(11):2598-605","abstract":"We have generated proliferating cell nuclear antigen (PCNA) mutants by low fidelity PCR and screened for lethal mutations by testing for lack of complementation of a Schizosaccharomyces pombe strain disrupted for the pcn1 + gene. We thus identified eight lethal mutants out of the 50 cDNAs tested. Six were truncated in their C-terminal region due to the introduction of a stop codon within their coding sequences. Two were full-length with a single point mutation at amino acid 68 or 69. The two latter mutants were overexpressed in insect cells via a recombinant baculovirus and were purified. They were unable to stimulate DNA polymerase delta DNA replication activity on a poly(dA).oligo(dT) template. Cross-linking experiments showed that this was due to their inability to form trimers. Since these two mutations are adjacent and not located in a domain of the protein putatively involved in inter-monomer interactions, our results show that the beta-sheet betaF1 to which they belong must play an essential role in maintaining the 3-dimensional structure of S.pombe PCNA.","authors":"Piard K, Baldacci G, Tratner I","authors_abbrev":"Piard K et al.","pubmed_publication_date":"01 Jun 1998","pubmed_entrez_date":"1998-05-21","publication_year":"1998","canto_session_key":"03128c28f1e9a98a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-01-29 16:00:13","canto_approved_date":"2021-09-29 09:37:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-29 16:00:08","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-01-29"},{"uniquename":"PMID:41296594","title":" Schizosaccharomyces pombe  Telomerase RNA: Secondary Structure and Flexible-Scaffold Function.","citation":"Mol Cell Biol 2025 Nov 26;:1-18","abstract":"The telomerase RNA-protein enzyme is critical for most eukaryotes to complete genome copying by extending chromosome ends, thus solving the end-replication problem and postponing senescence. Despite the importance of the fission yeast  Schizosaccharomyces pombe  to biomedical research, very little is known about the structure of its 1212 nt telomerase RNA. We have determined the secondary structure of this large RNA, TER1, based on phylogenetics and bioinformatic modeling, as well as genetic and biochemical analyses. We find several conserved regions of the rapidly evolving TER1 RNA are important to maintain telomeres, based on testing truncation mutants  in vivo , whereas many other large regions are dispensable. This is similar to budding yeast telomerase RNA, and consistent with functioning as a flexible scaffold for the RNP. We tested if the essential three-way junction works from other locations in TER1, finding that it can, supporting that it is flexibly scaffolded. Furthermore, we find that a half-sized Mini-TER1 allele, built from the catalytic core and the three-way junction, reconstitutes catalytic activity with TERT  in vitro . Overall, we provide a secondary structure model for the large fission-yeast telomerase lncRNA, based on phylogenetics and molecular-genetic testing in cells, and insight into the RNP's physical and functional organization.","doi":"10.1080/10985549.2025.2571189","authors":"McMurdie K, Peeney AN, Mefford MA, Baumann P, Zappulla DC","authors_abbrev":"McMurdie K et al.","pubmed_publication_date":"26 Nov 2025","pubmed_entrez_date":"2025-11-26","publication_year":"2025","canto_session_key":"667860e9247746a8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-11-27 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26265144","title":"The long non-coding RNA world in yeasts.","citation":"Biochim Biophys Acta 2016 Jan;1859(1):147-54","abstract":"In recent years, it has become evident that eukaryotic genomes are pervasively transcribed and produce numerous non-coding transcripts, including long non-coding RNAs (lncRNAs). Although research of such genomic enigmas is in the early stages, a growing number of lncRNAs have been characterized and found to be principal actors in a variety of biological processes rather than merely representing transcriptional noise. Here, we review recent findings on lncRNAs in yeast systems. We especially focus on lncRNA-mediated cellular regulations to respond to environmental changes in the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe. This article is part of a Special Issue entitled: Clues to long noncoding RNA taxonomy1, edited by Dr. Tetsuro Hirose and Dr. Shinichi Nakagawa.","doi":"10.1016/j.bbagrm.2015.08.003","authors":"Yamashita A, Shichino Y, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2015-08-13","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-08-14 00:19:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15530393","title":"A programmed strand-specific and modified nick in S. pombe constitutes a novel type of chromosomal imprint.","citation":"Curr Biol 2004 Nov 09;14(21):1924-8","abstract":"The sexual locus mat1, in the fission yeast Schizosaccharomyces pombe, efficiently switches between the two mating types, P and M, by a process similar to gene conversion, using the silent mat2-P and mat3-M loci, respectively, as donors of the P and M genetic information . It has been proposed that an asymmetrically inherited, site- and strand-specific imprint at mat1 initiates the mating-type switching process . The molecular nature of the imprint is controversial; it was initially described as a double-strand break and then as a single-strand lesion or a strand-specific, alkali-labile modification . Here, we use E. coli DNA ligase in vitro to demonstrate that the imprint is a nick with no resection of nucleotides. By using ligation-mediated PCR, we show that the nick contains 3'OH and 5'OH unphosphorylated termini resistant to RNase treatments. This nonmutational mark on one of the DNA strands provides the first example of a novel type of imprint.","authors":"Kaykov A, Arcangioli B","authors_abbrev":"Kaykov A et al.","pubmed_publication_date":"09 Nov 2004","pubmed_entrez_date":"2004-11-09","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10462529","title":"Translational control of the cdc25 cell cycle phosphatase: a molecular mechanism coupling mitosis to cell growth.","citation":"J Cell Sci 1999 Sep;112 Pt 18:3137-46","abstract":"The eukaryotic translation initiation factor 4A (eIF4A) is an RNA helicase required for translation initiation of eukaryotic mRNAs. By engineering fission yeast mutants with diminished eIF4A activity, we have found that translation of cdc25 mRNAs (a dosage-dependent activator of mitosis in all eukaryotic cells) is particularly sensitive to limitations of protein synthesis mediated by limited eIF4A activity. Genetic and biochemical analysis indicated that a rate-limited translation initiation of cdc25 mRNAs, exerted throughout its unusual 5' untranslated leader, acts as a molecular sensor to ensure that a minimum cell mass (protein synthesis) is attained before mitosis occurs. The Cdc13 cyclin B is also among the limited pool of proteins whose translation is sensitive to reduced translation initiation activity. Interestingly, the 5' leader sequences of cdc25 and cdc13 mRNAs have conserved features which are unusual in other yeast mRNAs, suggesting that common mechanisms operate in the expression of these two key mitotic activators at the translational level.","authors":"Daga RR, Jimenez J","authors_abbrev":"Daga RR et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-08-27","publication_year":"1999","canto_session_key":"7cc0d044cd0fd080","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-06-26 14:11:41","canto_approved_date":"2024-04-03 10:53:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-05-18 21:58:33","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPCC18B5.03","SPAC24H6.05","SPAC1006.07","SPAC16E8.15"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-06-26"},{"uniquename":"PMID:41316862","title":"Deletion of Elongator Protein 1 (Elp1) relieves heterochromatin defects in a Pol II mutant of Schizosaccharomyces pombe.","citation":"Genetics 2025 Nov 29;","abstract":"Heterochromatin is a repressive epigenetic state that suppresses transcription and safeguards genomic integrity. However, the full mechanism of its regulation remains elusive. Here, we focus on a previously described RNA polymerase II (Pol II) variant called m203 in Schizosaccharomyces pombe, which has a single substitution mutation within the Rpb2 subunit of Pol II (rpb2-N44Y) that reduces RNAi-dependent heterochromatin at a pericentromeric reporter locus. Through CRISPR-Cas9 site-directed mutagenesis, we find that rpb2-N44Y is a gain-of-function mutation. Furthermore, the heterochromatin defects of the m203 variant require a subunit of the Elongator complex called Elongator Protein 1 (Elp1), a protein that canonically promotes mcm5s2U34 tRNA modifications. While the single knockout of Elp1 in the m203 strain majorly restored heterochromatin formation, single knockouts of the Elp3 or the Elp5 subunits of Elongator showed only modest effects. Furthermore, mcm5s2 U34 tRNA modifications are dispensable for Elp1-dependent heterochromatin. In contrast, the heterochromatin required core factors that are critical for heterochromatin formation, including protein mediators of the RNA interference (RNAi) pathway and H3K9 methylation. Overall, our study reveals two distinct Rpb2-centric pathways, via RNAi or Elp1, that can positively or negatively regulate heterochromatin, respectively. Furthermore, our findings reveal a chromatin function for Elp1 that does not rely on Elongator-dependent mcm5s2U34 tRNA modifications. This work expands our understanding of how Elp1 can influence chromatin biology.","doi":"10.1093/genetics/iyaf258","authors":"Nirmal MB, Pearce ME, Liu CT, Finkel JM, Darrow KS, Vo TV","authors_abbrev":"Nirmal MB et al.","pubmed_publication_date":"29 Nov 2025","pubmed_entrez_date":"2025-11-29","publication_year":"2025","canto_session_key":"a2f92528c1edab43","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tommy Vo","canto_first_approved_date":"2026-02-26 10:15:13","canto_approved_date":"2026-02-26 10:15:13","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-02-05 11:15:47","canto_added_date":"2025-11-30 00:25:10","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":41,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Tommy Vo","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23G3.01","SPAC20H4.03c","SPAC6F12.09","SPAPYUG7.04c","SPBC18E5.05c","SPCTRNALYS.11","SPBTRNALYS.06","SPCC736.11","SPBC36.07","SPCC188.13c","SPBC19C2.13c","SPAC29A4.20","SPAC1F3.01","SPBC428.08c"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2026-02-26"},{"uniquename":"PMID:24280780","title":"Crosstalk between the Tor and Gcn2 pathways in response to different stresses.","citation":"Cell Cycle 2014;13(3):453-61","abstract":"Regulating growth and the cell cycle in response to environmental fluctuations is important for all organisms in order to maintain viability. Two major pathways for translational regulation are found in higher eukaryotes: the Tor signaling pathway and those operating through the eIF2α kinases. Studies from several organisms indicate that the two pathways are interlinked, in that Tor complex 1 (TORC1) negatively regulates the Gcn2 kinase. Furthermore, inactivation of TORC1 may be required for activation of Gcn2 in response to stress. Here, we use the model organism Schizosaccharomyces pombe to investigate this crosstalk further. We find that the relationship is more complex than previously thought. First, in response to UV irradiation and oxidative stress, Gcn2 is fully activated in the presence of TORC1 signaling. Second, during amino-acid starvation, activation of Gcn2 is dependent on Tor2 activity, and Gcn2 is required for timely inactivation of the Tor pathway. Our data show that the crosstalk between the two pathways varies with the actual stress applied.","doi":"10.4161/cc.27270","authors":"Rødland GE, Tvegård T, Boye E, Grallert B","authors_abbrev":"Rødland GE et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2013-11-28","publication_year":"2014","canto_session_key":"ee30a8ecd45d8559","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC36B7.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23299958","title":"Finding the end: recruitment of telomerase to telomeres.","citation":"Nat Rev Mol Cell Biol 2013 Feb;14(2):69-82","abstract":"Telomeres, the ends of linear eukaryotic chromosomes, are characterized by the presence of multiple repeats of a short DNA sequence. This telomeric DNA is protected from illicit repair by telomere-associated proteins, which in mammals form the shelterin complex. Replicative polymerases are unable to synthesize DNA at the extreme ends of chromosomes, but in unicellular eukaryotes such as yeast and in mammalian germ cells and stem cells, telomere length is maintained by a ribonucleoprotein enzyme known as telomerase. Recent work has provided insights into the mechanisms of telomerase recruitment to telomeres, highlighting the contribution of telomere-associated proteins, including TPP1 in humans, Ccq1 in Schizosaccharomyces pombe and Cdc13 and Ku70-Ku80 in Saccharomyces cerevisiae.","doi":"10.1038/nrm3505","authors":"Nandakumar J, Cech TR","authors_abbrev":"Nandakumar J et al.","pubmed_publication_date":"Feb 2013","pubmed_entrez_date":"2013-01-10","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11791728","title":"Radicicol binding to Swo1/Hsp90 and inhibition of growth of specific temperature-sensitive cell cycle mutants of fission yeast.","citation":"Biosci Biotechnol Biochem 2001 Nov;65(11):2528-34","abstract":"A panel screening using cdc mutants of Schizosaccharomyces pombe identified radicicol as a potent growth inhibitor of certain mutants at the permissive temperature. The strains sensitive to radicicol were cdc7, cdc11, and cdc14, all of which are defective in early septum formation. Cytokinesis but not nuclear division of these mutants was inhibited by radicicol, but that of cells with the wild-type background was not. A biologically active derivative of radicicol with a biotin moiety at the C-11 position bound Swo1, an Hsp90 homologue in S. pombe. Increased Swo1 expression partially suppressed radicicol sensitivity of cdc14 and almost completely rescued morphological abnormalities in cdc14 and cdc7 cells induced by radicicol at the permissive temperature. On the other hand, the increased Swo1 expression did not restore septum formation at the nonpermissive temperature. These results suggest that Swo1, as a molecular chaperone, plays a role in stabilizing these temperature-sensitive proteins at the permissive temperature or in activating the cytokinesis signaling cascade.","authors":"Ki SW, Kasahara K, Kwon HJ, Ishigami K, Kitahara T, Beppu T, Yoshida M, Horinouchi S","authors_abbrev":"Ki SW et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2002-01-17","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.04c","SPBC24C6.07"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:30846209","title":"Spindle pole body movement is affected by glucose and ammonium chloride in fission yeast.","citation":"Biochem Biophys Res Commun 2019 Apr 16;511(4):820-825","abstract":"The complexity of chromatin dynamics is orchestrated by several active processes. In fission yeast, the centromeres are clustered around the spindle pole body (SPB) and oscillate in a microtubule- and adenosine triphosphate (ATP)-dependent manner. However, whether and how SPB oscillation are affected by different environmental conditions remain poorly understood. In this study, we quantitated movements of the SPB component, which colocalizes with the centromere in fission yeast. We found that SPB movement was significantly reduced at low glucose concentrations. Movement of the SPB was also affected by the presence of ammonium chloride. Power spectral analysis revealed that periodic movement of the SPB is disrupted by low glucose concentrations. Measurement of ATP levels in living cells by quantitative single-cell imaging suggests that ATP levels are not the only determinant of SPB movement. Our results provide novel insight into how SPB movement is regulated by cellular energy status and additional factors such as the medium nutritional composition.","doi":"10.1016/j.bbrc.2019.02.128","authors":"Ito H, Sugawara T, Shinkai S, Mizukawa S, Kondo A, Senda H, Sawai K, Ito K, Suzuki S, Takaine M, Yoshida S, Imamura H, Kitamura K, Namba T, Tate SI, Ueno M","authors_abbrev":"Ito H et al.","pubmed_publication_date":"16 Apr 2019","pubmed_entrez_date":"2019-03-09","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-03-10 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26365378","title":"ESCRTs Cooperate with a Selective Autophagy Receptor to Mediate Vacuolar Targeting of Soluble Cargos.","citation":"Mol Cell 2015 Sep 17;59(6):1035-42","abstract":"Autophagy transports cytosolic materials into lysosomes/vacuoles either in bulk or selectively. Selective autophagy requires cargo receptor proteins, which usually link cargos to the macroautophagy machinery composed of core autophagy-related (Atg) proteins. Here, we show that fission yeast Nbr1, a homolog of mammalian autophagy receptor NBR1, interacts with and facilitates the transport of two cytosolic hydrolases into vacuoles, in a way reminiscent of the budding yeast cytoplasm-to-vacuole targeting (Cvt) pathway, a prototype of selective autophagy. We term this pathway Nbr1-mediated vacuolar targeting (NVT). Surprisingly, unlike the Cvt pathway, the NVT pathway does not require core Atg proteins. Instead, it depends on the endosomal sorting complexes required for transport (ESCRTs). NVT components colocalize with ESCRTs at multivesicular bodies (MVBs) and rely on ubiquitination for their transport. Our findings demonstrate the ability of ESCRTs to mediate highly selective autophagy of soluble cargos, and suggest an unexpected mechanistic versatility of autophagy receptors.","doi":"10.1016/j.molcel.2015.07.034","authors":"Liu XM, Sun LL, Hu W, Ding YH, Dong MQ, Du LL","authors_abbrev":"Liu XM et al.","pubmed_publication_date":"17 Sep 2015","pubmed_entrez_date":"2015-09-15","publication_year":"2015","canto_session_key":"db8f8f5d2b131ec2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li-Lin Du","canto_first_approved_date":"2017-12-29 22:06:40","canto_approved_date":"2021-04-09 16:13:34","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-03-25 11:45:31","canto_added_date":"2015-09-16 00:19:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":40,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Li-Lin Du","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11G7.02","SPAC11E3.04c","SPAC4F10.07c","SPBC31E1.01c","SPBC15D4.07c","SPAC11H11.01","SPCC63.08c","SPAC7D4.04","SPAC19B12.10","SPBC4B4.10c","SPAC1805.15c","SPCC1322.05c","SPAC25A8.02","SPBP35G2.11c","SPAC4A8.04","SPBC1921.05","SPAC1006.01","SPAC19A8.05c"],"gene_count":18,"ltp_gene_count":16,"approved_date":"2017-12-29"},{"uniquename":"PMID:26223950","title":"Histone H4 acetylation required for chromatin decompaction during DNA replication.","citation":"Sci Rep 2015 Jul 30;5:12720","abstract":"Faithful DNA replication is a prerequisite for cell proliferation. Several cytological studies have shown that chromosome structures alter in the S-phase of the cell cycle. However, the molecular mechanisms behind the alteration of chromosome structures associated with DNA replication have not been elucidated. Here, we investigated chromatin structures and acetylation of specific histone residues during DNA replication using the meiotic nucleus of the fission yeast Schizosaccharomyces pombe. The S. pombe meiotic nucleus provides a unique opportunity for measuring the levels of compaction of chromatin along the chromosome in a defined orientation. By direct measurement of chromatin compaction in living cells, we demonstrated that decompaction of chromatin occurs during meiotic DNA replication. This chromatin decompaction was suppressed by depletion of histone acetyltransferase Mst1 or by arginine substitution of specific lysine residues (K8 and K12) of histone H4. These results suggest that acetylation of histone H4 residues K8 and K12 plays a critical role in loosening chromatin structures during DNA replication.","doi":"10.1038/srep12720","authors":"Ruan K, Yamamoto TG, Asakawa H, Chikashige Y, Kimura H, Masukata H, Haraguchi T, Hiraoka Y","authors_abbrev":"Ruan K et al.","pubmed_publication_date":"30 Jul 2015","pubmed_entrez_date":"2015-07-31","publication_year":"2015","canto_session_key":"1fdf0eb67b32f997","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-02 00:19:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25918164","title":"Endoplasmic Reticulum Exit of Golgi-resident Defective for SREBP Cleavage (Dsc) E3 Ligase Complex Requires Its Activity.","citation":"J Biol Chem 2015 Jun 05;290(23):14430-40","abstract":"Layers of quality control ensure proper protein folding and complex formation prior to exit from the endoplasmic reticulum. The fission yeast Dsc E3 ligase is a Golgi-localized complex required for sterol regulatory element-binding protein (SREBP) transcription factor activation that shows architectural similarity to endoplasmic reticulum-associated degradation E3 ligases. The Dsc E3 ligase consists of five integral membrane proteins (Dsc1-Dsc5) and functionally interacts with the conserved AAA-ATPase Cdc48. Utilizing an in vitro ubiquitination assay, we demonstrated that Dsc1 has ubiquitin E3 ligase activity that requires the E2 ubiquitin-conjugating enzyme Ubc4. Mutations that specifically block Dsc1-Ubc4 interaction prevent SREBP cleavage, indicating that SREBP activation requires Dsc E3 ligase activity. Surprisingly, Golgi localization of the Dsc E3 ligase complex also requires Dsc1 E3 ligase activity. Analysis of Dsc E3 ligase complex formation, glycosylation, and localization indicated that Dsc1 E3 ligase activity is specifically required for endoplasmic reticulum exit of the complex. These results define enzyme activity-dependent sorting as an autoregulatory mechanism for protein trafficking.","doi":"10.1074/jbc.M114.630863","authors":"Raychaudhuri S, Espenshade PJ","authors_abbrev":"Raychaudhuri S et al.","pubmed_publication_date":"05 Jun 2015","pubmed_entrez_date":"2015-04-29","publication_year":"2015","canto_session_key":"8f019ff3f6b166f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2018-02-14 12:02:08","canto_approved_date":"2022-01-17 14:30:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-20 20:54:56","canto_added_date":"2015-04-30 00:19:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Peter Espenshade","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC285.11","SPBC31F10.06c","SPAC4D7.11","SPBC119.02","SPAC1486.02c","SPBC19C2.09","SPAC20H4.02","SPBC1734.04","SPBC1604.21c","SPBC947.10"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2018-02-14"},{"uniquename":"PMID:8763147","title":"Changes in cell wall composition of deformed ras1- cells of Schizosaccharomyces pombe.","citation":"Folia Microbiol (Praha) 1995;40(5):519-27","abstract":"Disruption of the Schizosaccharomyces pombe ras1 gene results in a morphological transformation to large spheres, in contrast to wild-type cells which grow as rods. Chemical analysis of isolated cell walls showed no significant changes in saccharide content but an increase in protein and phosphate contents in ras1- walls relative to parent walls. Polymers tightly bound to the cell wall were solubilized by SDS treatment. Several compounds with molar mass ranging from 22 to 130 kDa and more were resolved by gel filtration and SDS-PAGE. Among low-molar-mass species, a component moving as a band at 31 kDa was conspicuous in ras1- cell walls. It was solubilized by heating in Tris-HCl buffer and shown to have a beta-1,3-glucanase activity against laminarin. The level of the enzyme was by 30% higher in the ras1- cell wall than in the wild-type cell wall. This enzyme may participate in the remodelling of the rigid glucan network and account (at least partially) for the aberrant cell shape. The ras1- cell wall contained a high level of charged polymers, especially phosphoproteins, raising the appealing possibility that ras1- is involved in a putative kinase cascade required to sense and respond to external stimuli destined for the cell wall. Although the present study shows that ras1 loss of function and altered cell wall composition are closely linked defects, it has still to be shown that the ras1 protein is directly involved in alterations found in the mutant cell walls.","authors":"Harmouch N, Pichová A, Coulon J, Streiblová E, Bonaly R","authors_abbrev":"Harmouch N et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_session_key":"deeff8479cc279d8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-05-14 08:39:55","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-14 08:39:49","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-05-14"},{"uniquename":"EMBL:AJ007736","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.25"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12359080","title":"Characterization of recombinant YakC of Schizosaccharomyces pombe showing YakC defines a new family of aldo-keto reductases.","citation":"J Biochem 2002 Oct;132(4):635-41","abstract":"The yakC gene in Schizosaccharomyces pombe, which encodes yakC protein (YakC), a potential member of an aldo-keto reductase (AKR) family, was cloned and expressed in Escherichia coli cells. The recombinant YakC purified to homogeneity catalyzed the reduction of 2-nitrobenzaldehyde (k(cat), 44.1 s(-1), K(m), 0.185 +/- 0.018 mM), 2-phthalaldehyde (19.8, 0.333 +/- 0.032), and pyridine-2-aldehyde (7.64, 0.302 +/- 0.028). Neither pyridoxal nor other compounds examined acted as substrates. NADPH, but not NADH, was a hydrogen donor. The enzyme is a monomer with a molecular weight of 38,900 +/- 6,600 (SDS-PAGE). The amino acid sequence deduced from yakC showed the highest (34%) identity with that of pyridoxal reductase (AKR8A1) among the identified AKRs. Twenty-one function-unknown proteins showed 40% or higher identity to the deduced amino acid sequence: DR2261 protein of Deionococcus radiodurans showed the highest (50%) identity. The predicted secondary structure of YakC is similar to that of human aldose reductase, a representative AKR. The results establish YakC as the first member of a new AKR family, AKR13. The yeast cells contained enzyme(s) other than YakC and pyridoxal reductase with the ability to reduce 2-nitrobenzaldehyde: total (100%) activity in the crude extract consisted of about 23% YakC, about 44% pyridoxal reductase, and about 33% other enzyme(s).","authors":"Morita T, Huruta T, Ashiuchi M, Yagi T","authors_abbrev":"Morita T et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-10-03","publication_year":"2002","canto_session_key":"2518c35b5c2da685","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-06 14:54:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 21:52:02","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:38295128","title":"A connection between the ribosome and two S. pombe tRNA modification mutants subject to rapid tRNA decay.","citation":"PLoS Genet 2024 Jan 31;20(1):e1011146","abstract":"tRNA modifications are crucial in all organisms to ensure tRNA folding and stability, and accurate translation. In both the yeast Saccharomyces cerevisiae and the evolutionarily distant yeast Schizosaccharomyces pombe, mutants lacking certain tRNA body modifications (outside the anticodon loop) are temperature sensitive due to rapid tRNA decay (RTD) of a subset of hypomodified tRNAs. Here we show that for each of two S. pombe mutants subject to RTD, mutations in ribosomal protein genes suppress the temperature sensitivity without altering tRNA levels. Prior work showed that S. pombe trm8Δ mutants, lacking 7-methylguanosine, were temperature sensitive due to RTD, and that one class of suppressors had mutations in the general amino acid control (GAAC) pathway, which was activated concomitant with RTD, resulting in further tRNA loss. We now find that another class of S. pombe trm8Δ suppressors have mutations in rpl genes, encoding 60S subunit proteins, and that suppression occurs with minimal restoration of tRNA levels and reduced GAAC activation. Furthermore, trm8Δ suppression extends to other mutations in the large or small ribosomal subunit. We also find that S. pombe tan1Δ mutants, lacking 4-acetylcytidine, are temperature sensitive due to RTD, that one class of suppressors have rpl mutations, associated with minimal restoration of tRNA levels, and that suppression extends to other rpl and rps mutations. However, although S. pombe tan1Δ temperature sensitivity is associated with some GAAC activation, suppression by an rpl mutation only modestly inhibits GAAC activation. We propose a model in which ribosomal protein mutations result in reduced ribosome concentrations, leading to both reduced ribosome collisions and a reduced requirement for tRNA, with these effects having different relative importance in trm8Δ and tan1Δ mutants. This model is consistent with our results in S. cerevisiae trm8Δ trm4Δ mutants, known to undergo RTD, fueling speculation that this model applies across eukaryotes.","doi":"10.1371/journal.pgen.1011146","authors":"De Zoysa T, Hauke AC, Iyer NR, Marcus E, Ostrowski SM, Stegemann F, Ermolenko DN, Fay JC, Phizicky EM","authors_abbrev":"De Zoysa T et al.","pubmed_publication_date":"31 Jan 2024","pubmed_entrez_date":"2024-01-31","publication_year":"2024","canto_session_key":"36502c2f15fe4801","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Eric Phizicky","canto_first_approved_date":"2025-01-01 10:15:03","canto_approved_date":"2026-06-09 08:01:10","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-12-27 12:58:27","canto_added_date":"2024-02-01 00:25:05","annotation_curators":[{"name":"Eric Phizicky","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":91,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17G9.10","SPBC25H2.10c","SPAC521.05","SPBC11C11.09c","SPATRNALEU.03","SPBC1105.02c","SPAC1783.08c","SPAC26A3.12c","SPCPB16A4.04c","SPCC31H12.04c","SPAC17A5.14","SPBC26H8.08c","SPBC2F12.04","SPAC9G1.03c","SPBC36B7.09","SPAC26A3.07c","SPCC5E4.07","SPAC25G10.06","SPBC839.13c","SPAC23C11.02c","SPAC20G8.09c"],"gene_count":21,"ltp_gene_count":14,"approved_date":"2025-01-01"},{"uniquename":"PMID:28903048","title":"Set2 Methyltransferase Facilitates DNA Replication and Promotes Genotoxic Stress Responses through MBF-Dependent Transcription.","citation":"Cell Rep 2017 Sep 12;20(11):2693-2705","abstract":"Chromatin modification through histone H3 lysine 36 methylation by the SETD2 tumor suppressor plays a key role in maintaining genome stability. Here, we describe a role for Set2-dependent H3K36 methylation in facilitating DNA replication and the transcriptional responses to both replication stress and DNA damage through promoting MluI cell-cycle box (MCB) binding factor (MBF)-complex-dependent transcription in fission yeast. Set2 loss leads to reduced MBF-dependent ribonucleotide reductase (RNR) expression, reduced deoxyribonucleoside triphosphate (dNTP) synthesis, altered replication origin firing, and a checkpoint-dependent S-phase delay. Accordingly, prolonged S phase in the absence of Set2 is suppressed by increasing dNTP synthesis. Furthermore, H3K36 is di- and tri-methylated at these MBF gene promoters, and Set2 loss leads to reduced MBF binding and transcription in response to genotoxic stress. Together, these findings provide new insights into how H3K36 methylation facilitates DNA replication and promotes genotoxic stress responses in fission yeast.","doi":"10.1016/j.celrep.2017.08.058","authors":"Pai CC, Kishkevich A, Deegan RS, Keszthelyi A, Folkes L, Kearsey SE, De León N, Soriano I, de Bruin RAM, Carr AM, Humphrey TC","authors_abbrev":"Pai CC et al.","pubmed_publication_date":"12 Sep 2017","pubmed_entrez_date":"2017-09-14","publication_year":"2017","canto_session_key":"ec2b429a49be3976","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-02-21 12:14:54","canto_approved_date":"2022-07-10 07:36:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-13 14:31:01","canto_added_date":"2017-09-15 00:15:15","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":55,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.16","SPAC29B12.02c","SPBC428.18","SPCC18B5.11c","SPAC29B12.03","SPAC13D6.02c","SPBC16A3.07c","SPBC216.05","SPCC24B10.09","SPAC1F7.05","SPBC14C8.07c","SPAP14E8.02","SPBC21B10.13c","SPCC1259.13"],"gene_count":14,"ltp_gene_count":7,"approved_date":"2018-02-21"},{"uniquename":"PMID:19074598","title":"Functional differentiation of tbf1 orthologues in fission and budding yeasts.","citation":"Eukaryot Cell 2009 Feb;8(2):207-16","abstract":"In Saccharomyces cerevisiae, TBF1, an essential gene, influences telomere function but also has other roles in the global regulation of transcription. We have identified a new member of the tbf1 gene family in the mammalian pathogen Pneumocystis carinii. We demonstrate by transspecies complementation that its ectopic expression can provide the essential functions of Schizosaccharomyces pombe tbf1 but that there is no rescue between fission and budding yeast orthologues. Our findings indicate that an essential function of this family of proteins has diverged in the budding and fission yeasts and suggest that effects on telomere length or structure are not the primary cause of inviability in S. pombe tbf1 null strains.","doi":"10.1128/EC.00174-08","authors":"Cockell MM, Lo Presti L, Cerutti L, Cano Del Rosario E, Hauser PM, Simanis V","authors_abbrev":"Cockell MM et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-12-17","publication_year":"2009","canto_session_key":"92e15acd416a326e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-09-13 09:06:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-08 13:19:11","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-05-08"},{"uniquename":"PMID:11856374","title":"Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro.","citation":"Genes Cells 2002 Jan;7(1):59-73","abstract":"CIA, an interactor of the CCG1 histone acetyltransferase subunit of TFIID, was identified as a human histone chaperone. The Saccharomyces cerevisiae orthologue ASF1, when it was over-expressed, was reported to cause de-repression of silent loci; however, the involvement of Asf1p in the alteration of nucleosomal structures remained unknown. Curiously, there is a polyanionic stretch, a structural motif characteristic of histone chaperones, in S. cerevisiae Asf1p, but not in human CIA. We investigated how CIA/Asf1p utilizes its domain(s) for the alteration of nucleosomal structure.\nTo characterize the relationships between the domain structures and nuclear functions of CIA, we isolated the gene for the CIA counterpart in Schizosaccharomyces pombe, designated cia1+, whose putative product contains a polyanionic stretch. Gene disruption of cia1+ was lethal, which is the distinct phenotype of viable S. cerevisiae asf1. The cia1- lethality was rescued by the introduction of S. cerevisiae ASF1, but not by the introduction of human CIA cDNA. To our surprise, the construct that produces Asf1p, lacking the polyanionic stretch, is capable of rescuing the lethality caused by the cia1+ deletion, while the highly conserved N-terminal region of Asf1p is essential for the complementation of cia1- growth defects. The polyanionic stretch-deleted Asf1p is sufficient both for interaction with histones H3/H4 and for nucleosome assembly in vitro, as well as for telomeric de-repression in vivo.\nThese findings suggest that the areas responsible for both the conserved and species-specific functions of CIA/cia1/Asf1p are within their highly conserved regions and that the yeast-specific polyanionic stretch of cia1/Asf1p is not necessary for viability, histone binding, nucleosome assembly, or anti-silencing.","authors":"Umehara T, Chimura T, Ichikawa N, Horikoshi M","authors_abbrev":"Umehara T et al.","pubmed_publication_date":"Jan 2002","pubmed_entrez_date":"2002-02-22","publication_year":"2002","canto_session_key":"10569b018029d625","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-12 14:15:23","canto_approved_date":"2024-06-12 14:15:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 14:15:14","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC663.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-06-12"},{"uniquename":"PMID:19098712","title":"Rng3, a member of the UCS family of myosin co-chaperones, associates with myosin heavy chains cotranslationally.","citation":"EMBO Rep 2009 Feb;10(2):186-91","abstract":"The production of functional myosin heavy chains in many eukaryotic organisms requires the function of proteins containing UCS domains (UNC-45/CRO1/She4), which bind to the myosin head domain and stimulate its folding. UCS proteins are essential for myosin-related functions such as muscle formation, RNA localization and cytokinesis. Here, we show that the Schizosaccharomyces pombe UCS protein Rng3 associates with polysomes, suggesting that UCS proteins might assist myosin folding cotranslationally. To identify Rng3 cotranslational targets systematically, we purified Rng3-associated RNAs and used DNA microarrays to identify the transcripts. Rng3 copurified with only seven transcripts (around 0.1% of S. pombe genes), including all five messenger RNAs encoding myosin heavy chains. These results suggest that every myosin heavy chain in S. pombe is a cotranslational target of Rng3. Furthermore, our data suggest that microarray-based approaches allow the genome-wide identification of cotranslational chaperone targets, and thus pave the way for the dissection of translation-linked chaperone networks.","doi":"10.1038/embor.2008.228","authors":"Amorim MJ, Mata J","authors_abbrev":"Amorim MJ et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-12-23","publication_year":"2009","canto_session_key":"9dc149b26033fc0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-04-23 21:34:52","canto_approved_date":"2023-09-26 07:33:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-16 10:23:57","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.13c","SPCC645.05c","SPBC2D10.14c","SPAC4A8.05c","SPCC1919.10c","SPCC613.04c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-04-23"},{"uniquename":"PMID:9564789","title":"Natural organic compounds that affect to microtubule functions.","citation":"Yakugaku Zasshi 1998 Apr;118(4):112-26","abstract":"Microtubules (MT), composed of a protein tubulin (TN) alpha,beta-heterodimer with concomitant other proteins, microtubule associated proteins (MAPs and tau), are known to be the main component of spindles in a mitotic apparatus of eucaryotic cells, and are also involved in many other basic and essential cell functions. There are a number of natural and synthetic compounds that interfere with MT function to cause the mitotic arrest of eucaryotic cells. Such antimitotic agents show a broad biological activity, and can be used for medicinal and agrochemical purposes. On the other hand, they are also important as the biochemical tools for understanding the dynamics of MT network. Most of such antimitotic agents, with a few exceptions, bind to beta-TN. Among them, colchicine (CLC), vinblastine (VLB) and taxol have been of major importance in biochemical studies of MT and in studies of their intracellular functions. The former two both inhibit MT assembly but their binding sites on beta-TN are different; CLC-site and VLB-site, and many MT inhibitors bind to either sites. Taxol bind to TN at a site other than CLC-site and VLB-site, and promote MT assembly. We have worked on a variety of antimitotic agents that bind to CLC, VLB or taxol-site, in discoveries, structures, biological actions and/or interactions with TN. In this paper, I summarized the results of our studies on VLB-site ligands; (1) rhizoxin (RZX), isolated as a phytotoxin produced by a plant pathogenic fungus, and its related compounds, (2) derivatives of ansamitocin P-3 (ASMP3) (maytansinoid: MAY), isolated as a cytotoxic metabolite of an Actinomycete, (3) phomopsin A (PMSA), isolated as a mycotoxin produced by a plant parasitic fungus, (4) dolastatin 10 (DLS10), isolated as a cytotoxic metabolite of a see animal, (5) ustiloxins (USL) A-F, isolated as a mycotoxin produced by a plant pathogenic fungus, (6) arenastation A (ARSA), isolated as a cytotoxic metabolite of a sponge, and its synthetic analogs. From our studies on interactions of these VLB-site ligands with TN, we showed that the presence of a distinct RZX/MAY-binding site which only partially overlap with VLB-site, and that PMSA, DLS10, USLs and ARSA bind to the RZX/MAY site. RZX, ASMP3 and ARSA inhibit the growth of a variety of fungi, including Aspergillus nidulans. In order to obtain information as to the drug-TN interaction at the RZX/MAY site, RZX-resistant beta-TN gene mutants were isolated from RZX-sensitive wild-type A. nidulans. In all the beta-TN gene mutants, single amino acid (100th) alteration, asparagine-to-isoleucine, was observed. Sequence displacement experiments confirmed that this alteration conferred resistance to RZX and ASMP3, and also to ARSA. This resistance mechanism was further verified with yeasts Schizosaccharomyces pombe and Saccharomyces serevisiae. All the natural ligands mentioned above show potent cytotoxicity against human and murine tumor cells, but VLB, PMSA, DLS10 and USLA are inactive to both RZX-sensitive and -resistant fungal strains.","authors":"Iwasaki S","authors_abbrev":"Iwasaki S","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-06-20","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35416247","title":"Tschimganine has different targets for chronological lifespan extension and growth inhibition in fission yeast.","citation":"Biosci Biotechnol Biochem 2022 May 24;86(6):775-779","abstract":"Tschimganine inhibits growth and extends the chronological lifespan in Schizosaccharomyces pombe. We synthesized a Tschimganine analog, Mochimganine, which extends the lifespan similar to Tschimganine but exhibits a significantly weaker growth inhibition effect. Based on the comparative analysis of these compounds, we propose that Tschimganine has at least 2 targets: one extends the lifespan and the other inhibits growth.","doi":"10.1093/bbb/zbac051","authors":"Ohtsuka H, Matsumoto T, Mochida T, Shimasaki T, Shibuya M, Yamamoto Y, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"24 May 2022","pubmed_entrez_date":"2022-04-13","publication_year":"2022","canto_session_key":"96d9bd593bfd06c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2022-07-13 10:24:22","canto_approved_date":"2022-08-02 15:11:56","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-07-04 23:43:40","canto_added_date":"2022-04-15 00:15:05","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":8,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":2,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16E9.16c","SPCC757.07c","SPBC4F6.17c","SPBC2F12.17","SPBP23A10.16","SPBC725.10","SPCC576.03c","SPCC1235.14","SPCPB1C11.01"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2022-07-13"},{"uniquename":"PMID:14625383","title":"Individual microtubule dynamics contribute to the function of mitotic and cytoplasmic arrays in fission yeast.","citation":"J Cell Sci 2003 Dec 15;116(Pt 24):4891-903","abstract":"Schizosaccharomyces pombe is an excellent organism for studying microtubule dynamics owing to the presence of well-defined microtubule arrays that undergo dramatic rearrangements during various stages of the cell cycle. Using sensitive time-lapse video microscopy and kymographic analysis, we have determined the polymerization/depolymerization kinetics of individual microtubules within these arrays throughout the fission yeast cell cycle. Interphase bundles are composed of 4-7 microtubules that act autonomously, demonstrating that individual microtubules are responsible for mediating the functions ascribed to these arrays. The nucleation and growth of cytoplasmic microtubules is inhibited upon cellular transition into mitosis, leading to their gradual disappearance. At the onset of mitosis, microtubules form on the nuclear face of the spindle pole body and exhibit dramatically increased dynamics. The presence of these intra-nuclear astral microtubules (INA) is reminiscent of spindle assembly and the search and chromosome capture mechanism observed in metazoan cells. Consistent with other in vivo studies, we do not observe microtubule flux in the anaphase B spindle. Finally, the depolymerization of individual microtubules alternates between each half-spindle, resulting in spindle collapse during telophase. On the basis of these observations, we conclude that microtubules in these diverse cytoskeletal arrays have autonomous behaviors that are an essential component of any model describing cell-cycle-dependent changes in the behavior and function of microtubule arrays.","authors":"Sagolla MJ, Uzawa S, Cande WZ","authors_abbrev":"Sagolla MJ et al.","pubmed_publication_date":"15 Dec 2003","pubmed_entrez_date":"2003-11-20","publication_year":"2003","canto_session_key":"87e4a7babbfc2437","canto_annotation_status":"APPROVED","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_first_approved_date":"2022-06-13 11:44:03","canto_approved_date":"2022-06-13 11:44:03","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-06-13 11:43:56","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2022-06-13"},{"uniquename":"PMID:5073988","title":"Relation between repair mechanisms and induced mitotic recombination after UV irradiation, in the yeast Schizosaccharomyces pombe. Effects of caffeine.","citation":"Mol Gen Genet 1972;117(2):153-66","abstract":"","authors":"Fabre F","authors_abbrev":"Fabre F","pubmed_publication_date":"1972","pubmed_entrez_date":"1972-01-01","publication_year":"1972","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38895340","title":"CLCC1 promotes hepatic neutral lipid flux and nuclear pore complex assembly.","citation":"bioRxiv 2024 Jun 08;","abstract":"Imbalances in lipid storage and secretion lead to the accumulation of hepatocyte lipid droplets (LDs) (i.e., hepatic steatosis). Our understanding of the mechanisms that govern the channeling of hepatocyte neutral lipids towards cytosolic LDs or secreted lipoproteins remains incomplete. Here, we performed a series of CRISPR-Cas9 screens under different metabolic states to uncover mechanisms of hepatic neutral lipid flux. Clustering of chemical-genetic interactions identified CLIC-like chloride channel 1 (CLCC1) as a critical regulator of neutral lipid storage and secretion. Loss of CLCC1 resulted in the buildup of large LDs in hepatoma cells and knockout in mice caused liver steatosis. Remarkably, the LDs are in the lumen of the ER and exhibit properties of lipoproteins, indicating a profound shift in neutral lipid flux. Finally, remote homology searches identified a domain in CLCC1 that is homologous to yeast Brl1p and Brr6p, factors that promote the fusion of the inner and outer nuclear envelopes during nuclear pore complex assembly. Loss of CLCC1 lead to extensive nuclear membrane herniations, consistent with impaired nuclear pore complex assembly. Thus, we identify CLCC1 as the human Brl1p/Brr6p homolog and propose that CLCC1-mediated membrane remodeling promotes hepatic neutral lipid flux and nuclear pore complex assembly.","doi":"10.1101/2024.06.07.597858","authors":"Mathiowetz AJ, Meymand ES, Deol KK, Parlakgül G, Lange M, Pang SP, Roberts MA, Torres EF, Jorgens DM, Zalpuri R, Kang M, Boone C, Zhang Y, Morgens DW, Tso E, Zhou Y, Talukdar S, Levine TP, Ku G, Arruda AP, Olzmann JA","authors_abbrev":"Mathiowetz AJ et al.","pubmed_publication_date":"08 Jun 2024","pubmed_entrez_date":"2024-06-19","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8F11.06","HGNC:29675"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12972571","title":"Fission yeast Cdc23/Mcm10 functions after pre-replicative complex formation to promote Cdc45 chromatin binding.","citation":"Mol Biol Cell 2003 Sep;14(9):3876-87","abstract":"Using a cytological assay to monitor the successive chromatin association of replication proteins leading to replication initiation, we have investigated the function of fission yeast Cdc23/Mcm10 in DNA replication. Inactivation of Cdc23 before replication initiation using tight degron mutations has no effect on Mcm2 chromatin association, and thus pre-replicative complex (pre-RC) formation, although Cdc45 chromatin binding is blocked. Inactivating Cdc23 during an S phase block after Cdc45 has bound causes a small reduction in Cdc45 chromatin binding, and replication does not terminate in the absence of Mcm10 function. These observations show that Cdc23/Mcm10 function is conserved between fission yeast and Xenopus, where in vitro analysis has indicated a similar requirement for Cdc45 binding, but apparently not compared with Saccharomyces cerevisiae, where Mcm10 is needed for Mcm2 chromatin binding. However, unlike the situation in Xenopus, where Mcm10 chromatin binding is dependent on Mcm2-7, we show that the fission yeast protein is bound to chromatin throughout the cell cycle in growing cells, and only displaced from chromatin during quiescence. On return to growth, Cdc23 chromatin binding is rapidly reestablished independently from pre-RC formation, suggesting that chromatin association of Cdc23 provides a link between proliferation and competence to execute DNA replication.","authors":"Gregan J, Lindner K, Brimage L, Franklin R, Namdar M, Hart EA, Aves SJ, Kearsey SE","authors_abbrev":"Gregan J et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-09-16","publication_year":"2003","canto_session_key":"37237b530ab38bc9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-11-20 16:32:59","canto_approved_date":"2024-08-13 16:02:32","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-09-15 10:20:23","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17D4.02","SPBC25D12.03c","SPBC4.04c","SPBC336.12c","SPBC582.03","SPBC1347.10","SPBC776.12c","SPCC16A11.17"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2015-11-20"},{"uniquename":"PMID:1620099","title":"The switching gene swi6 affects recombination and gene expression in the mating-type region of Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1992 Jun;233(3):436-42","abstract":"The products of 11 switching (swi) genes are required for efficient mating-type (MT) switching in homothallic (h90) strains of Schizosaccharomyces pombe. The MT region of h90 comprises three cassette genes: the expression site mat1:1 and two silent loci, mat2:2 and mat3:3. Besides reducing MT switching, the swi6 mutation leads to deletions in the MT region caused by intrachromosomal cross-overs between two paired cassettes. These deletions only arise if DNA double-strand breaks are present at mat1:1, which initiate MT switching. Furthermore, swi6 allows meiotic recombination in the K region, a region of 16 kb between mat2:2 and mat3:3; in wild-type strains no recombination occurs in K. swi6 also allows the simultaneous expression of two different cassettes in the same haploid cell. Thus swi6 may have an influence on the general chromatin structure in the MT region.","authors":"Lorentz A, Heim L, Schmidt H","authors_abbrev":"Lorentz A et al.","pubmed_publication_date":"Jun 1992","pubmed_entrez_date":"1992-06-01","publication_year":"1992","canto_session_key":"02f271a61155c4f5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-12-21 16:02:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-10 16:25:21","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPBC30D10.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-09-10"},{"uniquename":"PMID:11452021","title":"Involvement of Schizosaccharomyces pombe Srs2 in cellular responses to DNA damage.","citation":"Nucleic Acids Res 2001 Jul 15;29(14):2963-72","abstract":"In the budding yeast Saccharomyces cerevisiae the Srs2/RadH DNA helicase promotes survival after ultraviolet (UV) irradiation, and has been implicated in DNA repair, recombination and checkpoint signalling following DNA damage. A second helicase, Sgs1, is the S.cerevisiae homologue of the human BLM and WRN proteins, which are defective in cancer predisposition and/or premature ageing syndromes. Saccharomyces cerevisiae cells lacking both Srs2 and Sgs1 exhibit a severe growth defect. We have identified an Srs2 orthologue in the fission yeast Schizosaccharomyces pombe, and have investigated its role in responses to UV irradiation and inhibition of DNA replication. Deletion of fission yeast srs2 caused spontaneous hyper-recombination and UV sensitivity, and simultaneous deletion of the SGS1 homologue rqh1 caused a severe growth defect reminiscent of that seen in the equivalent S.cerevisiae mutant. However, unlike in budding yeast, inactivation of the homologous recombination pathway did not suppress this growth defect. Indeed, the homologous recombination pathway was required for maintenance of normal fission yeast viability in the absence of Srs2, and loss of homologous recombination and loss of Srs2 contributed additively to UV sensitivity. We conclude that Srs2 plays related, but not identical, roles in the two yeast species.","authors":"Wang SW, Goodwin A, Hickson ID, Norbury CJ","authors_abbrev":"Wang SW et al.","pubmed_publication_date":"15 Jul 2001","pubmed_entrez_date":"2001-07-14","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC4H3.05","SPAC2G11.12","SPAC30D11.10","SPAC15A10.03c","SPBC3E7.08c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:12850446","title":"Cytokinesis in fission yeast: a story of rings, rafts and walls.","citation":"Trends Genet 2003 Jul;19(7):403-8","abstract":"","authors":"Rajagopalan S, Wachtler V, Balasubramanian M","authors_abbrev":"Rajagopalan S et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-07-10","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26459557","title":"The right place at the right time: chaperoning core histone variants.","citation":"EMBO Rep 2015 Nov;16(11):1454-66","abstract":"Histone proteins dynamically regulate chromatin structure and epigenetic signaling to maintain cell homeostasis. These processes require controlled spatial and temporal deposition and eviction of histones by their dedicated chaperones. With the evolution of histone variants, a network of functionally specific histone chaperones has emerged. Molecular details of the determinants of chaperone specificity for different histone variants are only slowly being resolved. A complete understanding of these processes is essential to shed light on the genuine biological roles of histone variants, their chaperones, and their impact on chromatin dynamics.","doi":"10.15252/embr.201540840","authors":"Mattiroli F, D'Arcy S, Luger K","authors_abbrev":"Mattiroli F et al.","pubmed_publication_date":"Nov 2015","pubmed_entrez_date":"2015-10-14","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-06-30 14:45:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26254921","title":"Elutriation for Cell Cycle Synchronization in Fission Yeast.","citation":"Methods Mol Biol 2016;1342:149-55","abstract":"Cell synchronization is a powerful technique for studying the eukaryotic cell cycle events precisely. The fission yeast is a rod-shaped cell whose growth is coordinated with the cell cycle. Monitoring the cellular growth of fission yeast is a relatively simple way to measure the cell cycle stage of a cell. Here, we describe a detailed method of unperturbed cell synchronization, named centrifugal elutriation, for fission yeast.","doi":"10.1007/978-1-4939-2957-3_7","authors":"Kume K","authors_abbrev":"Kume K","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-08-10","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-08-11 00:20:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24255738","title":"Phosphorelay-dependent and -independent regulation of MAPKKK by the Mcs4 response regulator in fission yeast.","citation":"Commun Integr Biol 2013 Sep 01;6(5):e25020","abstract":"In a \"two-component system,\" extracellular stimuli are transmitted by the transfer of a phosphoryl group from a sensor histidine kinase to a response regulator (RR), a mechanism referred to as phosphorelay. In the fission yeast Schizosaccharomyces pombe, peroxide stress signals are transmitted by phosphorelay to the Mcs4 RR, which activates the Spc1 MAP kinase (MAPK) cascade. We previously demonstrated that a glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) physically interacts with Mcs4 and promotes phosphorelay signaling to Mcs4. Independently of the phosphorelay mechanism, Mcs4 also plays a critical role in osmostress signaling, as a part of the stable ternary complex with the Wis4 and Win1 MAPK kinase kinases (MAPKKKs). Interestingly, GAPDH dissociates from Mcs4 upon osmostress, while oxidative stress promotes their association. The Mcs4 RR may serve as a switching hub that mediates activation of the Wis4-Win1 MAPKKK heteromer in response to different forms of stress.","doi":"10.4161/cib.25020","authors":"Morigasaki S, Shiozaki K","authors_abbrev":"Morigasaki S et al.","pubmed_publication_date":"01 Sep 2013","pubmed_entrez_date":"2013-11-21","publication_year":"2013","canto_session_key":"19e705d0ee416663","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaz Shiozaki","canto_approved_date":"2017-08-04 10:09:32","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-03-11 07:18:24","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kaz Shiozaki","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.09","SPBC887.10","SPAC9G1.02","SPBC409.07c","SPBC32F12.11","SPBC725.02"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2014-03-11"},{"uniquename":"PMID:8824588","title":"The Atf1 transcription factor is a target for the Sty1 stress-activated MAP kinase pathway in fission yeast.","citation":"Genes Dev 1996 Sep 15;10(18):2289-301","abstract":"The atf1+ gene of Schizosaccharomyces pombe encodes a bZIP transcription factor with strong homology to the mammalian factor ATF-2. ATF-2 is regulated through phosphorylation in mammalian cells by the stress-activated mitogen-activated protein (MAP) kinases SAPK/JNK and p38. We show here that the fission yeast Atf1 factor is also regulated by a stress-activated kinase, Sty1. The Sty1 kinase is stimulated by a variety of different stress conditions including osmotic and oxidative stress and heat shock. Deletion of the atf1+ gene results in many, but not all, of the phenotypes associated with loss of Sty1, including sensitivity to environmental stress and inability to undergo sexual conjugation. Furthermore, we identify a number of target genes that are induced rapidly in a manner dependent upon both the Sty1 kinase and the Atf1 transcription factor. These genes include gpd1+, which is important for the response of cells to osmotic stress, the catalase gene lambda important for cells to combat oxidative stress, and pyp2+, which encodes a tyrosine-specific MAP kinase phosphatase. Induction of Pyp2 by Atf1 is direct in that it does not require de novo protein synthesis and results in a negative feedback loop that serves to control signaling through the Sty1/Wis1 pathway. We show that Atf1 associates stably and is phosphorylated by the Sty1 kinase in vitro. Taken together, these results indicate that the interaction between AM and Sty1 is direct. These findings highlight a remarkable level of conservation in transcriptional control by stress-activated MAP kinase pathways between fission yeast and mammalian cells.","authors":"Wilkinson MG, Samuels M, Takeda T, Toone WM, Shieh JC, Toda T, Millar JB, Jones N","authors_abbrev":"Wilkinson MG et al.","pubmed_publication_date":"15 Sep 1996","pubmed_entrez_date":"1996-09-15","publication_year":"1996","canto_session_key":"87061c0c995c08bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-27 16:20:30","canto_approved_date":"2020-12-18 16:05:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-07 18:24:54","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC757.07c","SPBC19C2.05","SPAC24H6.05","SPBC29B5.01","SPAC19D5.01","SPBC409.07c","SPBC215.05","SPAC24B11.06c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2017-10-27"},{"uniquename":"PMID:18252797","title":"Homoeostasis between the GTPase Spg1p and its GAP in the regulation of cytokinesis in S. pombe.","citation":"J Cell Sci 2008 Mar 01;121(Pt 5):601-8","abstract":"Cytokinesis in Schizosaccharomyces pombe begins at mitotic entry, when the site of division is defined by formation of the contractile acto-myosin ring (CAR) at the cell cortex. Contraction of the CAR and formation of the division septum are triggered at the end of mitosis by septation initiation network (SIN) proteins associated with the spindle pole body (SPB). SIN signalling requires activation of the GTPase Spg1p, which is regulated by the bipartite GTPase-activating protein (GAP) Byr4p-Cdc16p. We show that, for Spg1p to associate with the SPB, it must be bound to its GAP or to its mitotic effector, the protein kinase Cdc7p. Analysis of the GAP proteins reveals that the steady-state level of Byr4p reflects that of Spg1p. Furthermore, if the interaction of Byr4p with Spg1p is compromised, the level of Byr4p decreases dramatically. The adaptation of the level of Byr4p to that of Spg1p requires the presence of Cdc16p and is mediated by proteasome-dependent destruction. It requires neither association with the SPB nor an active SIN. We propose a mechanism that limits the amount of the Byr4p-Cdc16p GAP to the amount required to inhibit Spg1p signalling.","doi":"10.1242/jcs.022772","authors":"Krapp A, Collin P, Cano Del Rosario E, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"01 Mar 2008","pubmed_entrez_date":"2008-02-07","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.06c","SPAC222.10c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9490630","title":"Mutations in the bimC box of Cut7 indicate divergence of regulation within the bimC family of kinesin related proteins.","citation":"J Cell Sci 1998 Apr;111 ( Pt 7):853-65","abstract":"Members of the bimC family of kinesin related proteins (KRPs) play vital roles in the formation and function of the mitotic spindle. Although they share little amino acid homology outside the highly conserved microtubule motor domain, several family members do contain a 'bimC box', a sequence motif around a p34(cdc2) consensus phosphorylation site in their carboxy-terminal 'tail' region. One family member, Eg5, requires phosphorylation at this site for association with the mitotic spindle. We show that mutations in the Schizosaccharomyces pombe cut7+ gene that change the bimC box p34(cdc2) consensus phosphorylation site at position 1,011 and a neighbouring MAP kinase consensus phosphorylation site at position 1,020 to non-phosphorylatable residues did not affect the ability of S. pombe cut7 genes to complement temperature sensitive cut7 mutants. Phosphorylation site mutants expressed as fusions to green fluorescent protein associated with the mitotic spindle with a localisation indistinguishable from similarly expressed wild-type Cut7. Cells in which cut7.T1011A replaced the genomic copy of cut7+ were viable and formed normal spindles. Deletion of the entire carboxy-terminal tail region did not affect the ability of Cut7 to associate with the mitotic spindle but did inhibit normal spindle formation. Thus, unlike Eg5, neither the p34(cdc2) consensus phosphorylation site in the bimC box nor the entire tail region of Cut7 are required for association with the mitotic spindle.","authors":"Drummond DR, Hagan IM","authors_abbrev":"Drummond DR et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-05-20","publication_year":"1998","canto_session_key":"8505764defef1039","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-26 12:29:26","canto_approved_date":"2024-03-28 17:53:35","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-08-07 10:11:41","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-03-26"},{"uniquename":"PMID:40388338","title":"Analysis of the Expression and Complexes Assembly of the Mitochondrial Respiratory Chain Proteins in the Fission Yeast Schizosaccharomyces pombe.","citation":"J Vis Exp 2025 May 02;(219)","abstract":"The mitochondrial respiratory chain is crucial for cellular energy metabolism, serving as the core of oxidative phosphorylation. The mitochondrial respiratory chain comprises five enzyme complexes and their interacting supercomplexes. Analysis of the expression and complexes assembly of these proteins is vital to understanding mitochondrial function. This can be studied by combining biochemical and genetic methods in an excellent model organism fission yeast Schizosaccharomyces pombe (S. pombe), which provides a compensatory system to budding yeast for studies of mitochondrial biology. Here, we present a detailed protocol for the isolation of S. pombe mitochondria and analysis of expression levels and complexes assembly of the mitochondrial respiratory proteins by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and blue native-PAGE (BN-PAGE). Briefly, mitochondria from the wild-type and gene mutants are purified, and then their complexes are solubilized and subjected to SDS-PAGE/BN-PAGE and immunoblotting. This method enables the characterization of a gene's novel function in the mitochondrial respiratory chain.","doi":"10.3791/68336","authors":"Lu G, Shang J, Feng G","authors_abbrev":"Lu G et al.","pubmed_publication_date":"02 May 2025","pubmed_entrez_date":"2025-05-19","publication_year":"2025","canto_session_key":"662e660c0ed086d9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-05-19 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11278870","title":"The fission yeast copper-sensing transcription factor Cuf1 regulates the copper transporter gene expression through an Ace1/Amt1-like recognition sequence.","citation":"J Biol Chem 2001 May 04;276(18):15472-80","abstract":"Transcriptional regulation of genes encoding critical components of copper transport is essential for copper homeostasis and growth in yeast. Analysis of regulatory regions in the promoter of the ctr4(+) copper transporter gene in fission yeast Schizosaccharomyces pombe reveals the identity of a conserved copper-signaling element (CuSE), which is recognized by the transcription factor Cuf1. We demonstrate that CuSE is necessary for transcriptional activation in response to copper deprivation conditions. Interestingly, the CuSE element bears a strong sequence similarity to the recognition site, denoted MRE (metal regulatory element), which is recognized by a distinct class of copper sensors required for copper detoxification, including Ace1 from Saccharomyces cerevisiae and Amt1 from Candida glabrata. When a consensus MRE from S. cerevisiae is introduced into S. pombe, transcription is induced by copper deprivation in a Cuf1-dependent manner, similar to regulation by Mac1, the nuclear sensor for regulating the expression of genes encoding components involved in copper transport in S. cerevisiae. UV-cross-linking experiments show that the Cuf1 protein directly binds the CuSE. These results demonstrate that the Cuf1 nutritional copper-sensing factor possesses a module that functions similarly to domains found in the Ace1/Amt1 class of metalloregulatory factors, which allows the protein to act through a closely related MRE-like sequence to regulate copper transport gene expression in S. pombe.","authors":"Beaudoin J, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"04 May 2001","pubmed_entrez_date":"2001-03-30","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1538784","title":"Kinesin-related cut7 protein associates with mitotic and meiotic spindles in fission yeast.","citation":"Nature 1992 Mar 05;356(6364):74-6","abstract":"Several mitotic and meiotic gene products are related to the microtubule motor kinesin, providing insight into the molecular basis of the complex motile events responsible for spindle formation and function. Of these genes, three have been shown to affect spindle structure when mutated. The most severe phenotype is seen in Aspergillus nidulans bimC and Schizosaccharomyces pombe cut7 mutants. In both fungi the intranuclear spindle is bipolar, with microtubules that emanate from spindle pole bodies at either pole, interdigitating in a central overlap zone. In bimC and cut7 mutants, microtubule interdigitation does not appear to take place, instead two unconnected half spindles form and chromosome separation fails. Here we report that cut7 protein concentrates on or near the spindle pole bodies throughout mitotic and meiotic nuclear division and associates with mitotic spindle microtubules in a stage-specific manner, associating with the mid-anaphase B midzone. In cut7ts mutants, spindle pole bodies stain but mitotic microtubules do not.","authors":"Hagan I, Yanagida M","authors_abbrev":"Hagan I et al.","pubmed_publication_date":"05 Mar 1992","pubmed_entrez_date":"1992-03-05","publication_year":"1992","canto_session_key":"d05448f3a0821419","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-02-28 12:15:14","canto_approved_date":"2023-01-26 10:30:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-18 17:13:29","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-02-28"},{"uniquename":"PMID:28751212","title":"Identification of three signaling molecules required for calcineurin-dependent monopolar growth induced by the DNA replication checkpoint in fission yeast.","citation":"Biochem Biophys Res Commun 2017 Sep 30;491(4):883-889","abstract":"Cell polarity is coordinately regulated with the cell cycle. Growth polarity of the fission yeast Schizosaccharomyces pombe transits from monopolar to bipolar during G2 phase, termed NETO (new end take off). Upon perturbation of DNA replication, the checkpoint kinase Cds1/CHK2 induces NETO delay through activation of Ca 2+ /calmodulin-dependent protein phosphatase calcineurin (CN). CN in turn regulates its downstream targets including the microtubule (MT) plus-end tracking CLIP170 homologue Tip1 and the Casein kinase 1γ Cki3. However, whether and which Ca 2+  signaling molecules are involved in the NETO delay remains elusive. Here we show that 3 genes (trp1322, vcx1 and SPAC6c3.06c encoding TRP channel, antiporter and P-type ATPase, respectively) play vital roles in the NETO delay. Upon perturbation of DNA replication, these 3 genes are required for not only the NETO delay but also for the maintenance of cell viability. Trp1322 and Vcx1 act downstream of Cds1 and upstream of CN for the NETO delay, whereas SPAC6c3.06c acts downstream of CN. Consistently, Trp1322 and Vcx1, but not SPAC6c3.06c, are essential for activation of CN. Interestingly, we have found that elevated extracellular Ca 2+  per se induces a NETO delay, which depends on CN and its downstream target genes. These findings imply that Ca 2+ -CN signaling plays a central role in cell polarity control by checkpoint activation.","doi":"10.1016/j.bbrc.2017.07.129","authors":"Kume K, Hashimoto T, Suzuki M, Mizunuma M, Toda T, Hirata D","authors_abbrev":"Kume K et al.","pubmed_publication_date":"30 Sep 2017","pubmed_entrez_date":"2017-07-29","publication_year":"2017","canto_session_key":"33d3cd2178fc2bdc","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-07-30 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40859013","title":"RNase III cleavage sites spread across splice junctions enforce sequential snoRNA processing.","citation":"EMBO Rep 2025 Aug 26;","abstract":"Small nucleolar RNAs (snoRNAs) are a class of eukaryotic non-coding RNA molecules whose precursor transcripts are capped and polyadenylated. However, these end modifications are detrimental to snoRNA function and must be removed, a process typically involving excision from introns and/or endonucleolytic cleavage. For RNA precursors that host multiple snoRNAs, the sequence of maturation events is potentially important, but not well understood. Here, we report a new mode of maturation concerning snoRNA pairs that are co-hosted in the intron and the adjacent 3' exon of a precursor transcript. For a snoRNA pair with this arrangement in Schizosaccharomyces pombe, we found that the sequence surrounding an exon-exon junction within their precursor transcript folds into a hairpin after splicing of the intron. This hairpin recruits the RNase III ortholog Pac1, which participates in the maturation of the downstream snoRNA by cleaving the precursor. Our findings suggest that conditional RNase III cleavage signals hidden in an exon-exon junction evolved to enforce sequential snoRNA processing. Sequence analysis suggests that this mechanism is conserved in animals and plants.","doi":"10.1038/s44319-025-00553-y","authors":"Migeot V, Mary Y, Fafard-Couture E, Lombard P, Bachand F, Scott MS, Yague-Sanz C","authors_abbrev":"Migeot V et al.","pubmed_publication_date":"26 Aug 2025","pubmed_entrez_date":"2025-08-26","publication_year":"2025","canto_session_key":"7d8029d6f159353e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-08-27 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC119.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35028663","title":"Dynamic configurations of meiotic DNA-break hotspot determinant proteins.","citation":"J Cell Sci 2022 Feb 01;135(3)","abstract":"Appropriate DNA double-strand break (DSB) and crossover distributions are required for proper meiotic chromosome segregation. Schizosaccharomyces pombe linear element proteins (LinEs) determine DSB hotspots; LinE-bound hotspots form three-dimensional clusters over ∼200 kb chromosomal regions. Here, we investigated LinE configurations and distributions in live cells using super-resolution fluorescence microscopy. We found LinEs form two chromosomal structures, dot-like and linear structures, in both zygotic and azygotic meiosis. Dot-like LinE structures appeared around the time of meiotic DNA replication, underwent dotty-to-linear-to-dotty configurational transitions and disassembled before the first meiotic division. DSB formation and repair did not detectably influence LinE structure formation but failure of DSB formation delayed disassembly. Recombination-deficient LinE missense mutants formed dot-like, but not linear, LinE structures. Our quantitative study reveals a transient form of LinE structures and suggests a novel role for LinE proteins in regulating meiotic events, such as DSB repair. We discuss the relationship of LinEs and the synaptonemal complex in other species. This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.259061","authors":"Chuang YC, Smith GR","authors_abbrev":"Chuang YC et al.","pubmed_publication_date":"01 Feb 2022","pubmed_entrez_date":"2022-01-14","publication_year":"2022","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-01-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25803873","title":"Calnexin is essential for survival under nitrogen starvation and stationary phase in Schizosaccharomyces pombe.","citation":"PLoS One 2015;10(3):e0121059","abstract":"Cell fate is determined by the balance of conserved molecular mechanisms regulating death (apoptosis) and survival (autophagy). Autophagy is a process by which cells recycle their organelles and macromolecules through degradation within the vacuole in yeast and plants, and lysosome in metazoa. In the yeast Schizosaccharomyces pombe, autophagy is strongly induced under nitrogen starvation and in aging cells. Previously, we demonstrated that calnexin (Cnx1p), a highly conserved transmembrane chaperone of the endoplasmic reticulum (ER), regulates apoptosis under ER stress or inositol starvation. Moreover, we showed that in stationary phase, Cnx1p is cleaved into two moieties, L_Cnx1p and S_Cnx1p. Here, we show that the processing of Cnx1p is regulated by autophagy, induced by nitrogen starvation or cell aging. The cleavage of Cnx1p involves two vacuolar proteases: Isp6, which is essential for autophagy, and its paralogue Psp3. Blocking autophagy through the knockout of autophagy-related genes (atg) results in inhibition of both, the cleavage and the trafficking of Cnx1p from the ER to the vacuole. We demonstrate that Cnx1p is required for cell survival under nitrogen-starvation and in chronological aging cultures. The death of the mini_cnx1 mutant (overlapping S_cnx1p) cells is accompanied by accumulation of high levels of reactive-oxygen species (ROS), a slowdown in endocytosis and severe cell-wall defects. Moreover, mutant cells expressing only S_Cnx1p showed cell wall defects. Co-expressing mutant overlapping the L_Cnx1p and S_Cnx1p cleavage products reverses the death, ROS phenotype and cell wall defect to wild-type levels. As it is involved in both apoptosis and autophagy, Cnx1p could be a nexus for the crosstalk between these pro-death and pro-survival mechanisms. Ours, and observations in mammalian systems, suggest that the multiple roles of calnexin depend on its sub-cellular localization and on its cleavage. The use of S. pombe should assist in further shedding light on the multiple roles of calnexin.","doi":"10.1371/journal.pone.0121059","authors":"Núñez A, Dulude D, Jbel M, Rokeach LA","authors_abbrev":"Núñez A et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-25","publication_year":"2015","canto_session_key":"0003e68d3973e436","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-13 11:35:30","canto_approved_date":"2025-05-27 09:53:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-13 11:35:23","canto_added_date":"2015-03-26 01:15:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":48,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.10c","SPAC1006.01","SPAC1296.03c","SPAC26A3.01","SPCC1259.10","SPBC354.02c","SPAC3H1.05","SPBC18A7.01","SPCC63.08c","SPBC16G5.09","SPAC3C7.11c","SPAC22E12.14c","SPAC19G12.10c","SPAC24B11.06c","SPAC20G8.10c","SPBC15D4.07c","SPCC1795.09","SPACUNK4.08","SPBP8B7.24c","SPAC4A8.04"],"gene_count":20,"ltp_gene_count":20,"approved_date":"2018-02-13"},{"uniquename":"PMID:19597311","title":"Nanoscopic morphological changes in yeast cell surfaces caused by oxidative stress: an atomic force microscopic study.","citation":"J Microbiol Biotechnol 2009 Jun;19(6):547-55","abstract":"Nanoscopic changes in the cell surface morphology of the yeasts Saccharomyces cerevisiae (strain NCYC 1681) and Schizosaccharomyces pombe (strain DVPB 1354), due to their exposure to varying concentrations of hydrogen peroxide (oxidative stress), were investigated using an atomic force microscope (AFM). Increasing hydrogen peroxide concentration led to a decrease in cell viabilities and mean cell volumes, and an increase in the surface roughness of the yeasts. In addition, AFM studies revealed that oxidative stress caused cell compression in both S. cerevisiae and Schiz. pombe cells and an increase in the number of aged yeasts. These results confirmed the importance and usefulness of AFM in investigating the morphology of stressed microbial cells at the nanoscale. The results also provided novel information on the relative oxidative stress tolerance of S. cerevisiae and Schiz. pombe.","authors":"Canetta E, Walker GM, Adya AK","authors_abbrev":"Canetta E et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-07-15","publication_year":"2009","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8367312","title":"The primary sequence of the Schizosaccharomyces pombe protein homologous to S.cerevisiae ribosomal protein L2.","citation":"Nucleic Acids Res 1993 Aug 11;21(16):3900","abstract":"","authors":"Presutti C, Villa T, Bozzoni I","authors_abbrev":"Presutti C et al.","pubmed_publication_date":"11 Aug 1993","pubmed_entrez_date":"1993-08-11","publication_year":"1993","canto_session_key":"f0fe51d86bee99ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-04-14 19:15:35","canto_approved_date":"2019-04-14 19:15:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-04-14 19:15:28","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC839.04","SPAC1F7.13c","SPBC2F12.07c"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2019-04-14"},{"uniquename":"PMID:9649516","title":"Fission yeast cdc24(+) encodes a novel replication factor required for chromosome integrity.","citation":"Genetics 1998 Jul;149(3):1221-33","abstract":"A mutation within the Schizosaccharomyces pombe cdc24(+) gene was identified previously in a screen for cell division cycle mutants and the cdc24(+) gene was determined to be essential for S phase in this yeast. We have isolated the cdc24(+) gene by complementation of a new temperature-sensitive allele of the gene, cdc24-G1. The DNA sequence predicts the presence of an open reading frame punctuated by six introns which encodes a pioneer protein of 58 kD. A cdc24 null mutant was generated by homologous recombination. Haploid cells lacking cdc24(+) are inviable, indicating that cdc24(+) is an essential gene. The transcript of cdc24(+) is present at constant levels throughout the cell cycle. Cells lacking cdc24(+) function show a checkpoint-dependent arrest with a 2N DNA content, indicating a block late in S phase. Arrest is accompanied by a rapid loss of viability and chromosome breakage. An S. pombe homolog of the replicative DNA helicase DNA2 of S. cerevisiae suppresses cdc24. These results suggest that Cdc24p plays a role in the progression of normal DNA replication and is required to maintain genomic integrity.","authors":"Gould KL, Burns CG, Feoktistova A, Hu CP, Pasion SG, Forsburg SL","authors_abbrev":"Gould KL et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-07-03","publication_year":"1998","canto_session_key":"c9a5bcda9f0382fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-01 12:03:18","canto_approved_date":"2026-01-29 16:31:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-22 11:38:40","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8F11.07c","SPBC16D10.04c","SPAC1952.07"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-06-01"},{"uniquename":"PMID:38448439","title":"Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex.","citation":"Nat Commun 2024 Mar 06;15(1):2059","abstract":"Arp2/3 complex nucleates branched actin filaments for cell and organelle movements. Here we report a 2.7 Å resolution cryo-EM structure of the mature branch junction formed by S. pombe Arp2/3 complex that provides details about interactions with both mother and daughter filaments. We determine a second structure at 3.2 Å resolution with the phosphate analog BeF x  bound with ADP to Arp3 and ATP bound to Arp2. In this ADP-BeF x  transition state the outer domain of Arp3 is rotated 2° toward the mother filament compared with the ADP state and makes slightly broader contacts with actin in both the mother and daughter filaments. Thus, dissociation of P i  from the ADP-P i  transition state reduces the interactions of Arp2/3 complex with the actin filaments and may contribute to the lower mechanical stability of mature branch junctions with ADP bound to the Arps. Our structures also reveal that the mother filament in contact with Arp2/3 complex is slightly bent and twisted, consistent with the preference of Arp2/3 complex binding curved actin filaments. The small degree of twisting constrains models of actin filament mechanics.","doi":"10.1038/s41467-024-46179-x","authors":"Chavali SS, Chou SZ, Cao W, Pollard TD, De La Cruz EM, Sindelar CV","authors_abbrev":"Chavali SS et al.","pubmed_publication_date":"06 Mar 2024","pubmed_entrez_date":"2024-03-06","publication_year":"2024","canto_session_key":"af89930c3f9430a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-15 06:56:36","canto_approved_date":"2024-06-15 06:56:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-15 06:56:27","canto_added_date":"2024-03-09 00:25:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.07c","SPAC630.03","SPAC17G8.04c","SPBC1778.08c","SPAC11H11.06","SPAC6F6.10c","SPBC14C8.06"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2024-06-15","pdb_entries":[{"pdb_id":"8uxw","gene_chains":[{"gene_uniquename":"SPAC6F6.10c","chain":"D","position":"1-317"},{"gene_uniquename":"SPAC630.03","chain":"A","position":"1-427"},{"gene_uniquename":"SPBC14C8.06","chain":"C","position":"1-377"},{"gene_uniquename":"SPAC17G8.04c","chain":"G","position":"1-152"},{"gene_uniquename":"SPAC6G9.07c","chain":"F","position":"1-168"},{"gene_uniquename":"SPAC11H11.06","chain":"B","position":"1-390"},{"gene_uniquename":"SPBC1778.08c","chain":"E","position":"1-174"}],"title":"Arp2/3 branch junction complex, ADP state","entry_authors":"Chavali SS,Chou SZ,Sindelar CV","entry_authors_abbrev":"Chavali SS et al.","reference_uniquename":"PMID:38448439","experimental_method":"EM","resolution":"2.7"},{"pdb_id":"8uxx","gene_chains":[{"gene_uniquename":"SPAC6F6.10c","chain":"D","position":"1-317"},{"gene_uniquename":"SPAC630.03","chain":"A","position":"1-427"},{"gene_uniquename":"SPBC14C8.06","chain":"C","position":"1-377"},{"gene_uniquename":"SPAC17G8.04c","chain":"G","position":"1-152"},{"gene_uniquename":"SPAC6G9.07c","chain":"F","position":"1-168"},{"gene_uniquename":"SPAC11H11.06","chain":"B","position":"1-390"},{"gene_uniquename":"SPBC1778.08c","chain":"E","position":"1-174"}],"title":"Arp2/3 branch junction complex, BeFx state","entry_authors":"Chavali SS,Chou SZ,Sindelar CV","entry_authors_abbrev":"Chavali SS et al.","reference_uniquename":"PMID:38448439","experimental_method":"EM","resolution":"3.2"}]},{"uniquename":"PMID:14594458","title":"PCAS--a precomputed proteome annotation database resource.","citation":"BMC Genomics 2003 Nov 01;4(1):42","abstract":"Many model proteomes or \"complete\" sets of proteins of given organisms are now publicly available. Much effort has been invested in computational annotation of those \"draft\" proteomes. Motif or domain based algorithms play a pivotal role in functional classification of proteins. Employing most available computational algorithms, mainly motif or domain recognition algorithms, we set up to develop an online proteome annotation system with integrated proteome annotation data to complement existing resources.\nWe report here the development of PCAS (ProteinCentric Annotation System) as an online resource of pre-computed proteome annotation data. We applied most available motif or domain databases and their analysis methods, including hmmpfam search of HMMs in Pfam, SMART and TIGRFAM, RPS-PSIBLAST search of PSSMs in CDD, pfscan of PROSITE patterns and profiles, as well as PSI-BLAST search of SUPERFAMILY PSSMs. In addition, signal peptide and TM are predicted using SignalP and TMHMM respectively. We mapped SUPERFAMILY and COGs to InterPro, so the motif or domain databases are integrated through InterPro. PCAS displays table summaries of pre-computed data and a graphical presentation of motifs or domains relative to the protein. As of now, PCAS contains human IPI, mouse IPI, and rat IPI, A. thaliana, C. elegans, D. melanogaster, S. cerevisiae, and S. pombe proteome.PCAS is available at http://pak.cbi.pku.edu.cn/proteome/gca.php\nPCAS gives better annotation coverage for model proteomes by employing a wider collection of available algorithms. Besides presenting the most confident annotation data, PCAS also allows customized query so users can inspect statistically less significant boundary information as well. Therefore, besides providing general annotation information, PCAS could be used as a discovery platform. We plan to update PCAS twice a year. We will upgrade PCAS when new proteome annotation algorithms identified.","authors":"Zhang Y, Yin Y, Chen Y, Gao G, Yu P, Luo J, Jiang Y","authors_abbrev":"Zhang Y et al.","pubmed_publication_date":"01 Nov 2003","pubmed_entrez_date":"2003-11-05","publication_year":"2003","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12186944","title":"Cytokinetic actomyosin ring formation and septation in fission yeast are dependent on the full recruitment of the polo-like kinase Plo1 to the spindle pole body and a functional spindle assembly checkpoint.","citation":"J Cell Sci 2002 Sep 15;115(Pt 18):3575-86","abstract":"In dividing cells, the assembly and contraction of the cytokinetic actomyosin ring (CAR) is precisely coordinated with spindle formation and chromosome segregation. Despite having a cell wall, the fission yeast Schizosaccharomyces pombe forms a CAR reminiscent of the structure responsible for the cleavage of cells with flexible boundaries. We used the myo2-gc fission yeast strain in which the chromosomal copy of the type II myosin gene, myo2(+), is fused to the gene encoding green fluorescent protein (GFP) to investigate the dynamics of Myo2 recruitment to the cytokinetic actomyosin ring in living cells. Analysis of CAR formation in relation to spindle pole body (SPB) and centromere separation enabled us to pinpoint the timing of Myo2 recruitment into a stable CAR structure to the onset of anaphase A. Depolymerisation of actin with latrunculin B did not affect the timing of Myo2 accumulation at the cell equator (although Myo2 no longer formed a ring), whereas depolymerisation of microtubules with either thiabendazole (TBZ) or methyl 2-benzimidazolecarbamate (MBC) resulted in a delay of up to 90 minutes in CAR formation. Microtubule depolymerisation also delayed the localisation of other CAR components such as actin and Mid1/Dmf1. The delay of cytokinesis in response to loss of microtubule integrity was abolished in cells lacking the spindle assembly checkpoint protein Mad2 or containing non-functional Cdc16, a component of the fission yeast septation initiation network (SIN). The delay was also abolished in cells lacking Zfs1, a component of the previously described S. pombe cytokinesis checkpoint. Recruitment of the polo-related kinase, Plo1, a key regulator of CAR formation, to the SPBs was substantially reduced in TBZ in a Mad2-dependent manner. Loading of Cdc7, a component of the SIN and downstream of Plo1 in the cytokinesis pathway, onto the the SPBs was also delayed in TBZ to the same extent as CAR formation. We conclude that CAR formation is subject to regulation by the spindle assembly checkpoint via the loading of Plo1 onto the SPBs and the consequent activation of the SIN.","authors":"Mulvihill DP, Hyams JS","authors_abbrev":"Mulvihill DP et al.","pubmed_publication_date":"15 Sep 2002","pubmed_entrez_date":"2002-08-21","publication_year":"2002","canto_session_key":"279efabf0d924bdf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-20 16:24:25","canto_approved_date":"2020-07-21 05:04:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-22 14:11:41","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPCC4B3.15","SPBC20F10.06","SPAC23C11.16","SPCC645.05c","SPBC1718.07c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-11-20"},{"uniquename":"PMID:28679702","title":"Selecting  Schizosaccharomyces pombe  Diploids.","citation":"Cold Spring Harb Protoc 2017 Jul 05;2017(7):pdb.prot091702","abstract":"Here we describe procedures for the selection of diploid  Schizosaccharomyces pombe  ade6-M210/ade6-M216  heteroallelic complementation is widely used to select for Ade +  diploids. Such diploids will readily sporulate when starved of nitrogen. For some investigations, stable diploids are preferable (e.g., for genetic complementation tests), and in these cases mating an  h -   strain with an  h 90  mat2-Pi-102  strain can be used to prevent sporulation. When  ade6-M210/ade6-M216  mutations impact on, or show synthetic interactions with, the gene of interest, two different auxotrophic markers can be used to select complementation.","doi":"10.1101/pdb.prot091702","authors":"Ekwall K, Thon G","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"05 Jul 2017","pubmed_entrez_date":"2017-07-07","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-08 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18036347","title":"Mutations of the SM protein Sly1 resulting in bypass of GTPase requirement in vesicular transport are confined to a short helical region.","citation":"FEBS Lett 2007 Dec 11;581(29):5698-702","abstract":"Ypt/Rab GTPases and Sec1/Munc18 (SM) proteins are key components of the membrane fusion machinery. Here, we describe new mutants of the yeast SM protein Sly1 that specifically bypass the need for GTPases Ypt1 and Ypt6 in vesicular transport. All sequence alterations are confined to a short alpha-helix (alpha-20), which is conserved in fungal Sly1 proteins and, when deleted, results in GTPase suppression. Whereas Sly1p of the evolutionarily distant fission yeast Schizosaccharomyces pombe can functionally replace Sly1p in Sacchromyces cerevisiae, mammalian homologues cannot. This indicates that alpha-20 in fungal Sly1p plays an important role in mediating Ypt/Rab-regulated Sly1p function in membrane fusion.","authors":"Li Y, Schmitt HD, Gallwitz D, Peng RW","authors_abbrev":"Li Y et al.","pubmed_publication_date":"11 Dec 2007","pubmed_entrez_date":"2007-11-27","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23091701","title":"Impaired coenzyme A synthesis in fission yeast causes defective mitosis, quiescence-exit failure, histone hypoacetylation and fragile DNA.","citation":"Open Biol 2012 Sep;2(9):120117","abstract":"Biosynthesis of coenzyme A (CoA) requires a five-step process using pantothenate and cysteine in the fission yeast Schizosaccharomyces pombe. CoA contains a thiol (SH) group, which reacts with carboxylic acid to form thioesters, giving rise to acyl-activated CoAs such as acetyl-CoA. Acetyl-CoA is essential for energy metabolism and protein acetylation, and, in higher eukaryotes, for the production of neurotransmitters. We isolated a novel S. pombe temperature-sensitive strain ppc1-537 mutated in the catalytic region of phosphopantothenoylcysteine synthetase (designated Ppc1), which is essential for CoA synthesis. The mutant becomes auxotrophic to pantothenate at permissive temperature, displaying greatly decreased levels of CoA, acetyl-CoA and histone acetylation. Moreover, ppc1-537 mutant cells failed to restore proliferation from quiescence. Ppc1 is thus the product of a super-housekeeping gene. The ppc1-537 mutant showed combined synthetic lethal defects with five of six histone deacetylase mutants, whereas sir2 deletion exceptionally rescued the ppc1-537 phenotype. In synchronous cultures, ppc1-537 cells can proceed to the S phase, but lose viability during mitosis failing in sister centromere/kinetochore segregation and nuclear division. Additionally, double-strand break repair is defective in the ppc1-537 mutant, producing fragile broken DNA, probably owing to diminished histone acetylation. The CoA-supported metabolism thus controls the state of chromosome DNA.","doi":"10.1098/rsob.120117","authors":"Nakamura T, Pluskal T, Nakaseko Y, Yanagida M","authors_abbrev":"Nakamura T et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-10-24","publication_year":"2012","canto_session_key":"e6290ba95085143d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomas Pluskal","canto_first_approved_date":"2015-08-17 16:02:53","canto_approved_date":"2026-04-05 07:14:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-21 11:57:41","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tomas Pluskal","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.10","SPAC139.06","SPBC36.05c","SPBC16D10.07c","SPAC3G9.07c","SPBC4B4.01c","SPBC409.04c","SPCC132.02","SPAC1783.04c","SPCC191.02c","SPAC1687.20c","SPBC800.03","SPAC637.12c","SPCC4B3.18"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2015-08-17"},{"uniquename":"PMID:36959220","title":"The K/HDEL receptor does not recycle but instead acts as a Golgi-gatekeeper.","citation":"Nat Commun 2023 Mar 23;14(1):1612","abstract":"Accurately measuring the ability of the K/HDEL receptor (ERD2) to retain the ER cargo Amy-HDEL has questioned earlier results on which the popular receptor recycling model is based upon. Here we demonstrate that ERD2 Golgi-retention, rather than fast ER export supports its function. Ligand-induced ERD2 redistribution is only observed when the C-terminus is masked or mutated, compromising the signal that prevents Golgi-to-ER transport of the receptor. Forcing COPI mediated retrograde transport destroys receptor function, but introducing ER-to-Golgi export or cis-Golgi retention signals re-activate ERD2 when its endogenous Golgi-retention signal is masked or deleted. We propose that ERD2 remains fixed as a Golgi gatekeeper, capturing K/HDEL proteins when they arrive and releasing them again into a subdomain for retrograde transport back to the ER. An in vivo ligand:receptor ratio far greater than 100 to 1 strongly supports this model, and the underlying mechanism appears to be extremely conserved across kingdoms.","doi":"10.1038/s41467-023-37056-0","authors":"Alvim JC, Bolt RM, An J, Kamisugi Y, Cuming A, Silva-Alvim FAL, Concha JO, daSilva LLP, Hu M, Hirsz D, Denecke J","authors_abbrev":"Alvim JC et al.","pubmed_publication_date":"23 Mar 2023","pubmed_entrez_date":"2023-03-24","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP8B7.22"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32502403","title":"Selective Nuclear Pore Complex Removal Drives Nuclear Envelope Division in Fission Yeast.","citation":"Curr Biol 2020 Aug 17;30(16):3212-3222.e2","abstract":"An important question in cell biology is how cellular organelles partition during cell division. In organisms undergoing closed mitosis, the elongation of an intranuclear spindle drives nuclear division, generating two identically sized nuclei [1, 2]. However, how the site of nuclear division is determined and the underlying mechanism driving nuclear envelope (NE) fission remain largely unknown. Here, using the fission yeast, we show that the microtubule bundler Ase1/PRC1 at the spindle midzone is required for the local concentration of nuclear pore complexes (NPCs) in the region of the NE in contact with the central spindle. As the spindle elongates during anaphase B, components of these NPCs are sequentially eliminated, and this is accompanied by the local remodeling of the NE. These two events lead to the eventual removal of NPCs and nuclear division. In the absence of importin α, NPCs remain stable in this region and no event of NE remodeling is observed. Consequently, cells fail to undergo nuclear division. Thus, our results highlight a new role of the central spindle as a spatial cue that determines the site of nuclear division and point to NPC removal as the triggering event.","doi":"10.1016/j.cub.2020.05.066","authors":"Expósito-Serrano M, Sánchez-Molina A, Gallardo P, Salas-Pino S, Daga RR","authors_abbrev":"Expósito-Serrano M et al.","pubmed_publication_date":"17 Aug 2020","pubmed_entrez_date":"2020-06-06","publication_year":"2020","canto_session_key":"490a9063fbc7021a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rafael Daga","canto_first_approved_date":"2020-12-10 11:57:21","canto_approved_date":"2022-05-01 19:13:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-02 15:45:55","canto_added_date":"2020-06-07 00:15:06","annotation_curators":[{"name":"Rafael Daga","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.08c","SPCC285.13c","SPCC18B5.07c","SPBC365.12c","SPBC800.05c","SPAPB1A10.09","SPAC18G6.10","SPAC1805.04","SPBC428.04","SPCC162.08c","SPBC31A8.01c","SPCC830.08c","SPAC30D11.04c","SPAC1786.03","SPAC1486.04c","SPBC428.01c"],"gene_count":16,"ltp_gene_count":10,"approved_date":"2020-12-10"},{"uniquename":"EMBL:AY034032","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30836700","title":"Quantifying Tubulin Concentration and Microtubule Number Throughout the Fission Yeast Cell Cycle.","citation":"Biomolecules 2019 Mar 04;9(3)","abstract":"The fission yeast  Schizosaccharomyces  pombe  serves as a good genetic model organism for the molecular dissection of the microtubule (MT) cytoskeleton. However, analysis of the number and distribution of individual MTs throughout the cell cycle, particularly during mitosis, in living cells is still lacking, making quantitative modelling imprecise. We use quantitative fluorescent imaging and analysis to measure the changes in tubulin concentration and MT number and distribution throughout the cell cycle at a single MT resolution in living cells. In the wild-type cell, both mother and daughter spindle pole body (SPB) nucleate a maximum of 23 ± 6 MTs at the onset of mitosis, which decreases to a minimum of 4 ± 1 MTs at spindle break down. Interphase MT bundles, astral MT bundles, and the post anaphase array (PAA) microtubules are composed primarily of 1 ± 1 individual MT along their lengths. We measure the cellular concentration of αβ-tubulin subunits to be ~5 µM throughout the cell cycle, of which one-third is in polymer form during interphase and one-quarter is in polymer form during mitosis. This analysis provides a definitive characterization of αβ-tubulin concentration and MT number and distribution in fission yeast and establishes a foundation for future quantitative comparison of mutants defective in MTs.","doi":"10.3390/biom9030086","authors":"Loiodice I, Janson ME, Tavormina P, Schaub S, Bhatt D, Cochran R, Czupryna J, Fu C, Tran PT","authors_abbrev":"Loiodice I et al.","pubmed_publication_date":"04 Mar 2019","pubmed_entrez_date":"2019-03-07","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-03-08 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR011990","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1687.18c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23828040","title":"Involvement of Schizosaccharomyces pombe rrp1+ and rrp2+ in the Srs2- and Swi5/Sfr1-dependent pathway in response to DNA damage and replication inhibition.","citation":"Nucleic Acids Res 2013 Sep;41(17):8196-209","abstract":"Previously we identified Rrp1 and Rrp2 as two proteins required for the Sfr1/Swi5-dependent branch of homologous recombination (HR) in Schizosaccharomyces pombe. Here we use a yeast two-hybrid approach to demonstrate that Rrp1 and Rrp2 can interact with each other and with Swi5, an HR mediator protein. Rrp1 and Rrp2 form co-localizing methyl methanesulphonate-induced foci in nuclei, further suggesting they function as a complex. To place the Rrp1/2 proteins more accurately within HR sub-pathways, we carried out extensive epistasis analysis between mutants defining Rrp1/2, Rad51 (recombinase), Swi5 and Rad57 (HR-mediators) plus the anti-recombinogenic helicases Srs2 and Rqh1. We confirm that Rrp1 and Rrp2 act together with Srs2 and Swi5 and independently of Rad57 and show that Rqh1 also acts independently of Rrp1/2. Mutants devoid of Srs2 are characterized by elevated recombination frequency with a concomitant increase in the percentage of conversion-type recombinants. Strains devoid of Rrp1 or Rrp2 did not show a change in HR frequency, but the number of conversion-type recombinants was increased, suggesting a possible function for Rrp1/2 with Srs2 in counteracting Rad51 activity. Our data allow us to propose a model placing Rrp1 and Rrp2 functioning together with Swi5 and Srs2 in a synthesis-dependent strand annealing HR repair pathway.","doi":"10.1093/nar/gkt564","authors":"Dziadkowiec D, Kramarz K, Kanik K, Wisniewski P, Carr AM","authors_abbrev":"Dziadkowiec D et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-07-06","publication_year":"2013","canto_session_key":"94e8d96f739efc51","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4H3.05","SPBC409.03","SPAC2G11.12","SPBC28F2.07","SPBC23E6.02","SPAC17A2.12","SPAC20H4.07","SPAC644.14c","SPBC365.06"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"InterPro:IPR018808","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4C3.06","HGNC:25180","HGNC:25412","HGNC:29002"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28082423","title":"Facile manipulation of protein localization in fission yeast through binding of GFP-binding protein to GFP.","citation":"J Cell Sci 2017 Mar 01;130(5):1003-1015","abstract":"GFP-binding protein (or GBP) has been recently developed in various systems and organisms as an efficient tool to purify GFP-fusion proteins. Due to the high affinity between GBP and GFP or GFP variants, this GBP-based approach is also ideally suited to alter the localization of functional proteins in live cells. In order to facilitate the wide use of the GBP-targeting approach in the fission yeast  Schizosaccharomyces pombe , we developed a set of pFA6a-, pJK148- and pUC119-based vectors containing GBP- or GBP-mCherry-coding sequences and variants of inducible  nmt1  or constitutive  adh1  promoters that result in different levels of expression. The GBP or GBP-mCherry fragments can serve as cassettes for N- or C-terminal genomic tagging of genes of interest. We illustrated the application of these vectors in the construction of yeast strains with Dma1 or Cdc7 tagged with GBP-mCherry and efficient targeting of Dma1- or Cdc7-GBP-mCherry to the spindle pole body by Sid4-GFP. This series of vectors should help to facilitate the application of the GBP-targeting approach in manipulating protein localization and the analysis of gene function in fission yeast, at the level of single genes, as well as at a systematic scale.","doi":"10.1242/jcs.198457","authors":"Chen YH, Wang GY, Hao HC, Chao CJ, Wang Y, Jin QW","authors_abbrev":"Chen YH et al.","pubmed_publication_date":"01 Mar 2017","pubmed_entrez_date":"2017-01-14","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-01-15 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20579106","title":"An oleate-stimulated, phosphatidylinositol 4,5-bisphosphate-independent phospholipase D in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2010 Sep;10(6):717-26","abstract":"Phospholipase D1 (PLD1) is an important enzyme involved in lipid-mediated signal transduction and membrane dynamics in eukaryotes. PLD1 preferentially hydrolyzes phosphatidylcholine to phosphatidic acid. This potent second messenger is involved in cytoskeletal reorganization, secretion, and membrane trafficking in eukaryotic cells. In Saccharomyces cerevisiae, PLD1 is involved in polarized growth and morphogenesis during pheromone response and sporulation. The presence of a PLD activity in Schizosaccharomyces pombe is demonstrated. PLD activity was able to hydrolyze a fluorescently labeled analog of phosphatidylcholine and was capable of performing the transphosphatidylation reaction characteristic of PLDs. Schizosaccharomyces pombe PLD activity was unaffected by phosphatidylinositol 4,5 bisphosphate (PIP(2)), but was slightly stimulated by oleate. PLD activity was shown to increase when the S. pombe cells underwent mating and sporulation. Here, we also report the molecular cloning of the first phospholipase D isoform from an S. pombe genomic DNA library (EMBL accession no. FN547388). Comparisons of three divergent yeasts, S. pombe, S. cerevisiae, and Candida albicans, with respect to the PLD enzymes revealed differences in regulation by oleate and PIP(2). Even with high homology in the protein sequences between the PLD1 enzymes of S. cerevisiae, C. albicans, and S. pombe, there was variation with the effects of the regulators.","doi":"10.1111/j.1567-1364.2010.00646.x","authors":"Harkins AL, Yuan G, London SD, Dolan JW","authors_abbrev":"Harkins AL et al.","pubmed_publication_date":"Sep 2010","pubmed_entrez_date":"2010-06-29","publication_year":"2010","canto_session_key":"270530574181e6be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:53:18","canto_session_submitted_date":"2012-02-27 11:05:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F7.16c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-02-27"},{"uniquename":"PMID:19001087","title":"Checkpoint-dependent regulation of origin firing and replication fork movement in response to DNA damage in fission yeast.","citation":"Mol Cell Biol 2009 Jan;29(2):602-11","abstract":"To elucidate the checkpoint mechanism responsible for slowing passage through S phase when fission yeast cells are treated with the DNA-damaging agent methyl methanesulfonate (MMS), we carried out two-dimensional gel analyses of replication intermediates in cells synchronized by cdc10 block (in G(1)) followed by release into synchronous S phase. The results indicated that under these conditions early-firing centromeric origins were partially delayed but late-firing telomeric origins were not delayed. Replication intermediates persisted in MMS-treated cells, suggesting that replication fork movement was inhibited. These effects were dependent on the Cds1 checkpoint kinase and were abolished in cells overexpressing the Cdc25 phosphatase, suggesting a role for the Cdc2 cyclin-dependent kinase. We conclude that both partial inhibition of the firing of a subset of origins and inhibition of replication fork movement contribute to the slowing of S phase in MMS-treated fission yeast cells.","doi":"10.1128/MCB.01319-08","authors":"Kumar S, Huberman JA","authors_abbrev":"Kumar S et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2008-11-13","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23038266","title":"The ubiquitin-associated (UBA) 1 domain of Schizosaccharomyces pombe Rhp23 is essential for the recognition of ubiquitin-proteasome system substrates both in vitro and in vivo.","citation":"J Biol Chem 2012 Dec 07;287(50):42344-51","abstract":"The ubiquitin-proteasome system is essential for maintaining a functional cell. Not only does it remove incorrectly folded proteins, it also regulates protein levels to ensure their appropriate spatial and temporal distribution. Proteins marked for degradation by the addition of Lys(48)-linked ubiquitin (Ub) chains are recognized by shuttle factors and transported to the 26 S proteasome. One of these shuttle factors, Schizosaccharomyces pombe Rhp23, has an unusual domain architecture. It comprises an N-terminal ubiquitin-like domain that can recognize the proteasome followed by two ubiquitin-associated (UBA) domains, termed UBA1 and UBA2, which can bind Ub. This architecture is conserved up to humans, suggesting that both domains are important for Rhp23 function. Such an extent of conservation raises the question as to why, in contrast to all other shuttle proteins, does Rhp23 require two UBA domains? We performed in vitro Ub binding assays using domain swap chimeric proteins and mutated domains in isolation as well as in the context of the full-length protein to reveal that the Ub binding properties of the UBA domains are context-dependent. In vivo, the internal Rhp23 UBA1 domain provides sufficient Ub recognition for the protein to function without UBA2.","doi":"10.1074/jbc.M112.419838","authors":"Medina B, Paraskevopoulos K, Boehringer J, Sznajder A, Robertson M, Endicott J, Gordon C","authors_abbrev":"Medina B et al.","pubmed_publication_date":"07 Dec 2012","pubmed_entrez_date":"2012-10-06","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC126.03","SPBC2D10.12","SPBC337.08c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:30355803","title":"Greatwall kinase at a glance.","citation":"J Cell Sci 2018 Oct 24;131(20)","abstract":"Mitosis is controlled by a subtle balance between kinase and phosphatase activities that involve the master mitotic kinase cyclin-B-Cdk1 and its antagonizing protein phosphatase 2A-B55 (PP2A-B55). Importantly, the Greatwall (Gwl; known as Mastl in mammals, Rim15 in budding yeast and Ppk18 in fission yeast) kinase pathway regulates PP2A-B55 activity by phosphorylating two proteins, cAMP-regulated phosphoprotein 19 (Arpp19) and α-endosulfine (ENSA). This phosphorylation turns these proteins into potent inhibitors of PP2A-B55, thereby promoting a correct timing and progression of mitosis. In this Cell Science at a Glance article and the accompanying poster, we discuss how Gwl is regulated in space and time, and how the Gwl-Arpp19-ENSA-PP2A-B55 pathway plays an essential role in the control of M and S phases from yeast to human. We also summarize how Gwl modulates oncogenic properties of cells and how nutrient deprivation influences Gwl activity.","doi":"10.1242/jcs.222364","authors":"Castro A, Lorca T","authors_abbrev":"Castro A et al.","pubmed_publication_date":"24 Oct 2018","pubmed_entrez_date":"2018-10-26","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-10-27 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF10427","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC83.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:14625382","title":"Wee1-dependent mechanisms required for coordination of cell growth and cell division.","citation":"J Cell Sci 2003 Dec 15;116(Pt 24):4883-90","abstract":"Wee1-related kinases function in a highly conserved mechanism that controls the timing of entry into mitosis. Loss of Wee1 function causes fission yeast and budding yeast cells to enter mitosis before sufficient growth has occurred, leading to formation of daughter cells that are smaller than normal. Early work in fission yeast suggested that Wee1 is part of a cell-size checkpoint that prevents entry into mitosis before cells have reached a critical size. Recent experiments in fission yeast and budding yeast have provided new support for this idea. In addition, studies in budding yeast have revealed the existence of highly intricate signaling networks that are required for regulation of Swe1, the budding yeast homolog of Wee1. Further understanding of these signaling networks may provide important clues to how cell growth and cell division are coordinated.","authors":"Kellogg DR","authors_abbrev":"Kellogg DR","pubmed_publication_date":"15 Dec 2003","pubmed_entrez_date":"2003-11-20","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR12791","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.13","SPAC31A2.13c","HGNC:14562","HGNC:19348"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:11331883","title":"Fission yeast Bub1 is essential in setting up the meiotic pattern of chromosome segregation.","citation":"Nat Cell Biol 2001 May;3(5):522-6","abstract":"In meiosis, sister-chromatids move to the same spindle pole during the first division (MI) and to opposite poles during the second division (MII). This requires that MI sister kinetochores are co-orientated and form an apparent single functional unit that only interacts with microtubules from one pole, and that sister-chromatids remain associated through their centromeres until anaphase II. Here we investigate the function of Bub1 and Mad2, which are components of the mitotic-spindle checkpoint, on chromosome segregation during meiosis. Both proteins are required to prevent the occurrence of non-disjunction events in MI, which is consistent with recent findings that components of the mitotic-spindle checkpoint also operate during meiosis. However, Bub1 has several functions that are not shared with Mad2. When the bub1 gene is deleted, sister chromatids often move to opposite spindle poles during MI, indicating that sister kinetochores are disunited. Furthermore, the cohesin Rec8 is never retained at centromeres at anaphase I and sister-chromatid cohesion is lost. Our results show that Bub1, besides its functions in monitoring chromosome attachment, is essential for two other significant aspects of MI - unification of sister kinetochores and retention of centromeric cohesion.","authors":"Bernard P, Maure JF, Javerzat JP","authors_abbrev":"Bernard P et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-02","publication_year":"2001","canto_session_key":"f507eb8aa144ccde","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-03-03 07:49:17","canto_approved_date":"2024-04-24 16:06:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-25 13:11:25","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.12c","SPBC29A10.14","SPBC20F10.06"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2021-03-03"},{"uniquename":"GO_REF:0000087","title":"Representation of protein localization and establishment of protein localization as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the protein localization and establishment of protein localization to a cellular component as a biological process. The underlying equivalence axiom templates are \"GO:0008104 and 'has_target_end_location' some C\" (protein localization) and \"GO:0045184 and 'has_target_end_location' some C\" (establishment of protein localization), where C is cellular component.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17248917","title":"Maximum likelihood estimation of linkage and interference from tetrad data.","citation":"Genetics 1979 May;92(1):231-45","abstract":"Maximum likelihood equations have been derived for estimation of map distance and interference from two-point and ranked tetrad data. The estimators have been applied to data from Saccharomyces cerevisiae and Schizosaccharomyces pombe. S. cerevisiae consistently shows quite strong interference over the mapped genome. In striking contrast, S. pombe consistently shows much weaker interference and many crosses exhibit negative interference. In neither species was there a conspicuous tendency for intervals spanning a centromere to show less interference than those that did not. Since the amount of recombination per microgram of DNA in the two species is similar, the difference in interference characteristics seems to be a reflection of some fundamental difference in the recombination process of the two species.","authors":"Snow R","authors_abbrev":"Snow R","pubmed_publication_date":"May 1979","pubmed_entrez_date":"1979-05-01","publication_year":"1979","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12727894","title":"Monopolar spindle attachment of sister chromatids is ensured by two distinct mechanisms at the first meiotic division in fission yeast.","citation":"EMBO J 2003 May 01;22(9):2284-96","abstract":"At meiosis I, sister chromatids attach to the same spindle pole (i.e. monopolar attachment). Mechanisms establishing monopolar attachment remain largely unknown. In the fission yeast Schizosaccharomyces pombe, monopolar attachment is established in haploid cells, indicating that homologous chromosomes are dispensable for its establishment. This monopolar attachment requires both mating pheromone signaling and inactivation of Pat1 kinase (a key negative regulator of meiosis). It also requires the meiotic cohesin factor Rec8 but not the recombination factor Rec12. In contrast, in diploid cells, monopolar attachment is established by Pat1 inactivation alone, and does not require mating pheromone signaling. Furthermore, monopolar attachment requires Rec12 in addition to Rec8. These results indicate that monopolar attachment of sister chromatids can be established by two distinct mechanisms in S.pombe, one that is pheromone dependent and recombination independent, and a second that is pheromone independent and recombination dependent. We propose that co-operation of these two mechanisms generates the high fidelity of monopolar attachment.","authors":"Yamamoto A, Hiraoka Y","authors_abbrev":"Yamamoto A et al.","pubmed_publication_date":"01 May 2003","pubmed_entrez_date":"2003-05-03","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPAC17A5.11","SPBC29A10.14"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU009583","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000034","title":"Phenoscape Skeletal Anatomy Jamboree","abstract":"Skeletal cell terms and relationships were added and revised at the Skeletal Anatomy Jamboree held by Phenoscape (NSF grant BDI-0641025) and hosted by the National Evolutionary Synthesis Center (NESCent), April 9-10, 2010.","authors":"Brian K. Hall (Dalhousie University), Matthew Vickaryous (Ontario Veterinary College, University of Guelph), David Blackburn, University of Kansas; Wasila Dahdul, University of South Dakota and NESCent; Alexander Diehl, Mouse Genome Informatics (MGI); Melissa Haendel, Oregon Health Sciences University; John G. Lundberg, Department of Ichthyology, Academy of Natural Sciences, Philadelphia; Paula Mabee, Department of Biology, University of South Dakota; Martin Ringwald, Mouse Genome Informatics (MGI); Erik Segerdell, Oregon Health Sciences University; Ceri Van Slyke, Zebrafish Information Network (ZFIN); Monte Westerfield, Zebrafish Information Network (ZFIN) and Institute of Neuroscience, University of Oregon.","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19948484","title":"Membrane proteins Bqt3 and -4 anchor telomeres to the nuclear envelope to ensure chromosomal bouquet formation.","citation":"J Cell Biol 2009 Nov 02;187(3):413-27","abstract":"In many organisms, telomeres cluster to form a bouquet arrangement of chromosomes during meiotic prophase. Previously, we reported that two meiotic proteins, Bqt1 and -2, are required for tethering telomeres to the spindle pole body (SPB) during meiotic prophase in fission yeast. This study has further identified two novel, ubiquitously expressed inner nuclear membrane (INM) proteins, Bqt3 and -4, which are required for bouquet formation. We found that in the absence of Bqt4, telomeres failed to associate with the nuclear membranes in vegetative cells and consequently failed to cluster to the SPB in meiotic prophase. In the absence of Bqt3, Bqt4 protein was degraded during meiosis, leading to a phenotype similar to that of the bqt4-null mutant. Collectively, these results show that Bqt4 anchors telomeres to the INM and that Bqt3 protects Bqt4 from protein degradation. Interestingly, the functional integrity of telomeres is maintained even when they are separated from the nuclear envelope in vegetative cells.","doi":"10.1083/jcb.200902122","authors":"Chikashige Y, Yamane M, Okamasa K, Tsutsumi C, Kojidani T, Sato M, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"02 Nov 2009","pubmed_entrez_date":"2009-12-02","publication_year":"2009","canto_session_key":"10192b215ce8c3bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-02 16:26:42","canto_approved_date":"2025-05-27 13:44:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-26 03:38:28","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC594.07c","SPBC12D12.01","SPBC1778.02","SPAC1002.06c","SPBC19C7.10"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2019-01-02"},{"uniquename":"PMID:8619315","title":"Gcs1, a gene encoding gamma-glutamylcysteine synthetase in the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 1995 Sep 30;11(12):1171-7","abstract":"By complementation of a mutant resistant to N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) we have identified the gcs1 gene, encoding a putative gamma-glutamylcysteine synthetase. The gene is possibly interrupted by two introns and has 49% identical and 80% similar amino acids compared with the homologous protein from rat. In comparison with the Saccharomyces cerevisiae homologue it possesses 41% identical and 74% similar amino acids.","authors":"Coblenz A, Wolf K","authors_abbrev":"Coblenz A et al.","pubmed_publication_date":"30 Sep 1995","pubmed_entrez_date":"1995-09-30","publication_year":"1995","canto_session_key":"97baf400b5574051","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-06-20 17:02:59","canto_session_submitted_date":"2012-06-01 12:26:15","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F3.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-06-01"},{"uniquename":"PMID:26542710","title":"Identification and characterization of Csh3 as an SH3 protein that interacts with fission yeast Cap1.","citation":"FEMS Yeast Res 2015 Dec;15(8)","abstract":"Schizosaccharomyces pombe Cap1 has been identified as the (adenylyl) cyclase-associated protein. Cap1 was able to bind Cap1 itself and actin. Cap1 localized at the growing tip, and this localization was dependent on the Cap1 P2 region. In a two-hybrid screening using cap1 as bait, we isolated csh3, which encodes a protein of 296 amino acids with an SH3 domain and a proline/glutamine-rich region. The binding of Csh3 and Cap1 was confirmed by in vivo pull down assays. Cooperative functions of Csh3 and Cap1 were observed. Deletion of both csh3 and cap1 resulted in heightened sensitivity to CaCl2, while disruption of either gene alone did not have any effect in this regard. In addition, over-expression of csh3 or cap1 alone did not affect cell growth, while over-expression of both genes resulted in growth retardation. Finally, while Csh3-GFP localized to the cytoplasm in wild-type cells, its localization was altered in cap1Δ cells, suggesting that the interaction between Csh3 and Cap1 controls the cellular localization of Csh3. These results demonstrate that Cap1 in Schizo. pombe is a multifunctional protein that functions through interaction with Cap1 itself and other proteins including adenylyl cyclase, actin and Csh3.","doi":"10.1093/femsyr/fov097","authors":"Yamamoto T, Kobayashi-Ooka Y, Zhou GL, Kawamukai M","authors_abbrev":"Yamamoto T et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-11-07","publication_year":"2015","canto_session_key":"8696d1390e6352bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_first_approved_date":"2017-05-17 22:47:12","canto_approved_date":"2025-12-11 13:04:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-30 02:04:25","canto_added_date":"2015-11-08 01:19:14","annotation_curators":[{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC306.09c","SPBC119.05c","SPBC11C11.09c","SPBC32H8.12c","SPAC20G4.06c","SPCC794.09c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-05-17"},{"uniquename":"PMID:8507210","title":"Processing of the small GTP-binding protein SpYPT1p in Schizosaccharomyces pombe and in mammalian COS cells.","citation":"Biochem Biophys Res Commun 1993 May 14;192(3):983-90","abstract":"SpYPT1p belongs to a family of ras-like GTP-binding proteins which is believed to be involved in the regulation of intracellular vesicular trafficking. We have analyzed the processing of this protein in its natural environment, the fission yeast Schizosaccharomyces pombe, and when expressed in transfected mammalian COS cells. In COS cells SpYPT1p exists in two forms: a cytosolic 24 kDa protein which represents the unprocessed precursor form and a prenylated 23.5 kDa protein which is equally distributed between membranes and cytosol. In contrast, in S.pombe we have been unable to detect any prenylation of the protein, despite the presence of a potential C-terminal CysCys prenylation site. In addition a 23.5 kDa form was localized exclusively in the cytosol and a third membrane-bound 23 kDa form was also detected. Pulse-chase experiments revealed that in S.pombe SpYPT1p is co-translationally or immediately after translation converted to the 23.5 kDa form which is then rapidly processed to the 23 kDa membrane bound form. We have been unable to detect any significant soluble pool of the protein.","authors":"Giannakouros T, Newman CM, Armstrong J, Magee AI","authors_abbrev":"Giannakouros T et al.","pubmed_publication_date":"14 May 1993","pubmed_entrez_date":"1993-05-14","publication_year":"1993","canto_session_key":"aa3315efdb95d115","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-05-21 12:15:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-17 07:23:12","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-05-17"},{"uniquename":"PMID:22631437","title":"Genome-scale metabolic model of the fission yeast Schizosaccharomyces pombe and the reconciliation of in silico/in vivo mutant growth.","citation":"BMC Syst Biol 2012 Jul 05;6:49","abstract":"Over the last decade, the genome-scale metabolic models have been playing increasingly important roles in elucidating metabolic characteristics of biological systems for a wide range of applications including, but not limited to, system-wide identification of drug targets and production of high value biochemical compounds. However, these genome-scale metabolic models must be able to first predict known in vivo phenotypes before it is applied towards these applications with high confidence. One benchmark for measuring the in silico capability in predicting in vivo phenotypes is the use of single-gene mutant libraries to measure the accuracy of knockout simulations in predicting mutant growth phenotypes.\nHere we employed a systematic and iterative process, designated as Reconciling In silico/in vivo mutaNt Growth (RING), to settle discrepancies between in silico prediction and in vivo observations to a newly reconstructed genome-scale metabolic model of the fission yeast, Schizosaccharomyces pombe, SpoMBEL1693. The predictive capabilities of the genome-scale metabolic model in predicting single-gene mutant growth phenotypes were measured against the single-gene mutant library of S. pombe. The use of RING resulted in improving the overall predictive capability of SpoMBEL1693 by 21.5%, from 61.2% to 82.7% (92.5% of the negative predictions matched the observed growth phenotype and 79.7% the positive predictions matched the observed growth phenotype).\nThis study presents validation and refinement of a newly reconstructed metabolic model of the yeast S. pombe, through improving the metabolic model's predictive capabilities by reconciling the in silico predicted growth phenotypes of single-gene knockout mutants, with experimental in vivo growth data.","doi":"10.1186/1752-0509-6-49","authors":"Sohn SB, Kim TY, Lee JH, Lee SY","authors_abbrev":"Sohn SB et al.","pubmed_publication_date":"05 Jul 2012","pubmed_entrez_date":"2012-05-29","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34019809","title":"Molecular mechanism of N-terminal acetylation by the ternary NatC complex.","citation":"Structure 2021 Oct 07;29(10):1094-1104.e4","abstract":"Protein N-terminal acetylation is predominantly a ribosome-associated modification, with NatA-E serving as the major enzymes. NatC is the most unusual of these enzymes, containing one Naa30 catalytic subunit and two auxiliary subunits, Naa35 and Naa38; and substrate selectivity profile that overlaps with NatE. Here, we report the cryoelectron microscopy structure of S. pombe NatC with a NatE/C-type bisubstrate analog and inositol hexaphosphate (IP 6 ), and associated biochemistry studies. We find that the presence of three subunits is a prerequisite for normal NatC acetylation activity in yeast and that IP 6  binds tightly to NatC to stabilize the complex. We also describe the molecular basis for IP 6 -mediated NatC complex stabilization and the overlapping yet distinct substrate profiles of NatC and NatE.","doi":"10.1016/j.str.2021.05.003","authors":"Deng S, Gottlieb L, Pan B, Supplee J, Wei X, Petersson EJ, Marmorstein R","authors_abbrev":"Deng S et al.","pubmed_publication_date":"07 Oct 2021","pubmed_entrez_date":"2021-05-21","publication_year":"2021","canto_session_key":"5342aa989c2f1d8a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-09-14 09:01:27","canto_approved_date":"2022-02-07 20:37:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-05 18:04:23","canto_added_date":"2021-05-23 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC947.03c","SPBC15D4.06","SPBC1861.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2021-09-14","pdb_entries":[{"pdb_id":"7l1k","gene_chains":[{"gene_uniquename":"SPBC947.03c","chain":"C","position":"1-72"},{"gene_uniquename":"SPBC15D4.06","chain":"A","position":"1-150"},{"gene_uniquename":"SPBC1861.03","chain":"B","position":"1-708"}],"title":"Cryo-EM structure of S. Pombe NatC complex with a Bisubstrate inhibitor and inositol hexaphosphate","entry_authors":"Deng S,Marmorstein R","entry_authors_abbrev":"Deng S et al.","reference_uniquename":"PMID:34019809","experimental_method":"EM","resolution":"3.16"}]},{"uniquename":"PMID:32168916","title":"Human Cancer-Associated Mutations of SF3B1 Lead to a Splicing Modification of Its Own RNA.","citation":"Cancers (Basel) 2020 Mar 11;12(3)","abstract":"Deregulation of pre-mRNA splicing is observed in many cancers and hematological malignancies. Genes encoding splicing factors are frequently mutated in myelodysplastic syndromes, in which  SF3B1  mutations are the most frequent. SF3B1 is an essential component of the U2 small nuclear ribonucleoprotein particle that interacts with branch point sequences close to the 3' splice site during pre-mRNA splicing.  SF3B1  mutations mostly lead to substitutions at restricted sites in the highly conserved HEAT domain, causing a modification of its function. We found that SF3B1 was aberrantly spliced in various neoplasms carrying an  SF3B1  mutation, by exploring publicly available RNA sequencing raw data. We aimed to characterize this novel SF3B1 transcript, which is expected to encode a protein with an insertion of eight amino acids in the H3 repeat of the HEAT domain. We investigated the splicing proficiency of this SF3B1 protein isoform, in association with the most frequent mutation (K700E), through functional complementation assays in two myeloid cell lines stably expressing distinct SF3B1 variants. The yeast  Schizosaccharomyces  pombe  was also used as an alternative model. Insertion of these eight amino acids in wild-type or mutant SF3B1 (K700E) abolished SF3B1 essential function, highlighting the crucial role of the H3 repeat in the splicing function of SF3B1.","doi":"10.3390/cancers12030652","authors":"Bergot T, Lippert E, Douet-Guilbert N, Commet S, Corcos L, Bernard DG","authors_abbrev":"Bergot T et al.","pubmed_publication_date":"11 Mar 2020","pubmed_entrez_date":"2020-03-15","publication_year":"2020","canto_session_key":"79cfb1652794d9bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-07-10 07:33:54","canto_approved_date":"2024-02-23 17:39:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-25 12:51:25","canto_added_date":"2020-03-16 01:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.06","SPBC26H8.07c","SPAC27F1.09c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2021-07-10"},{"uniquename":"PMID:34255844","title":"The cooperative assembly of shelterin bridge provides a kinetic gateway that controls telomere length homeostasis.","citation":"Nucleic Acids Res 2021 Aug 20;49(14):8110-8119","abstract":"Shelterin is a six-protein complex that coats chromosome ends to ensure their proper protection and maintenance. Similar to the human shelterin, fission yeast shelterin is composed of telomeric double- and single-stranded DNA-binding proteins, Taz1 and Pot1, respectively, bridged by Rap1, Poz1 and Tpz1. The assembly of the proteinaceous Tpz1-Poz1-Rap1 complex occurs cooperatively and disruption of this shelterin bridge leads to unregulated telomere elongation. However, how this biophysical property of bridge assembly is integrated into shelterin function is not known. Here, utilizing synthetic bridges with a range of binding properties, we find that synthetic shelterin bridge lacking cooperativity requires a linker pair that matches the native bridge in complex lifespan but has dramatically higher affinity. We find that cooperative assembly confers kinetic properties on the shelterin bridge allowing disassembly to function as a molecular timer, regulating the duration of the telomere open state, and consequently telomere lengthening to achieve a defined species-specific length range.","doi":"10.1093/nar/gkab550","authors":"Liu J, Hu X, Bao K, Kim JK, Zhang C, Jia S, Qiao F","authors_abbrev":"Liu J et al.","pubmed_publication_date":"20 Aug 2021","pubmed_entrez_date":"2021-07-13","publication_year":"2021","canto_session_key":"708b18da700d87e9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Feng Qiao","canto_first_approved_date":"2021-08-05 13:03:44","canto_approved_date":"2024-04-03 11:36:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-07-24 03:12:56","canto_added_date":"2021-07-15 00:15:03","annotation_curators":[{"name":"Feng Qiao","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.13c","SPBC428.08c","SPAC16A10.07c","SPAC26H5.06","SPCC188.07","SPBC1778.02","SPAC6F6.16c"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2021-08-05"},{"uniquename":"PMID:23861491","title":"Lariat sequencing in a unicellular yeast identifies regulated alternative splicing of exons that are evolutionarily conserved with humans.","citation":"Proc Natl Acad Sci U S A 2013 Jul 30;110(31):12762-7","abstract":"Alternative splicing is a potent regulator of gene expression that vastly increases proteomic diversity in multicellular eukaryotes and is associated with organismal complexity. Although alternative splicing is widespread in vertebrates, little is known about the evolutionary origins of this process, in part because of the absence of phylogenetically conserved events that cross major eukaryotic clades. Here we describe a lariat-sequencing approach, which offers high sensitivity for detecting splicing events, and its application to the unicellular fungus, Schizosaccharomyces pombe, an organism that shares many of the hallmarks of alternative splicing in mammalian systems but for which no previous examples of exon-skipping had been demonstrated. Over 200 previously unannotated splicing events were identified, including examples of regulated alternative splicing. Remarkably, an evolutionary analysis of four of the exons identified here as subject to skipping in S. pombe reveals high sequence conservation and perfect length conservation with their homologs in scores of plants, animals, and fungi. Moreover, alternative splicing of two of these exons have been documented in multiple vertebrate organisms, making these the first demonstrations of identical alternative-splicing patterns in species that are separated by over 1 billion y of evolution.","doi":"10.1073/pnas.1218353110","authors":"Awan AR, Manfredo A, Pleiss JA","authors_abbrev":"Awan AR et al.","pubmed_publication_date":"30 Jul 2013","pubmed_entrez_date":"2013-07-18","publication_year":"2013","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27712582","title":"Spotsizer: High-throughput quantitative analysis of microbial growth.","citation":"Biotechniques 2016 Oct 01;61(4):191-201","abstract":"Microbial colony growth can serve as a useful readout in assays for studying complex genetic interactions or the effects of chemical compounds. Although computational tools for acquiring quantitative measurements of microbial colonies have been developed, their utility can be compromised by inflexible input image requirements, non-trivial installation procedures, or complicated operation. Here, we present the Spotsizer software tool for automated colony size measurements in images of robotically arrayed microbial colonies. Spotsizer features a convenient graphical user interface (GUI), has both single-image and batch-processing capabilities, and works with multiple input image formats and different colony grid types. We demonstrate how Spotsizer can be used for high-throughput quantitative analysis of fission yeast growth. The user-friendly Spotsizer tool provides rapid, accurate, and robust quantitative analyses of microbial growth in a high-throughput format. Spotsizer is freely available at https://data.csiro.au/dap/landingpage?pid=csiro:15330 under a proprietary CSIRO license.","doi":"10.2144/000114459","authors":"Bischof L, Převorovský M, Rallis C, Jeffares DC, Arzhaeva Y, Bähler J","authors_abbrev":"Bischof L et al.","pubmed_publication_date":"01 Oct 2016","pubmed_entrez_date":"2016-10-08","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-10-09 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29697047","title":"Rev7 and 53BP1/Crb2 prevent RecQ helicase-dependent hyper-resection of DNA double-strand breaks.","citation":"Elife 2018 Apr 26;7","abstract":"Poly(ADP ribose) polymerase inhibitors (PARPi) target cancer cells deficient in homology-directed repair of DNA double-strand breaks (DSBs). In preclinical models, PARPi resistance is tied to altered nucleolytic processing (resection) at the 5' ends of a DSB. For example, loss of either 53BP1 or Rev7/MAD2L2/FANCV derepresses resection to drive PARPi resistance, although the mechanisms are poorly understood. Long-range resection can be catalyzed by two machineries: the exonuclease Exo1, or the combination of a RecQ helicase and Dna2. Here, we develop a single-cell microscopy assay that allows the distinct phases and machineries of resection to be interrogated simultaneously in living  S. pombe  cells. Using this assay, we find that the 53BP1 orthologue and Rev7 specifically repress long-range resection through the RecQ helicase-dependent pathway, thereby preventing hyper-resection. These results suggest that 'rewiring' of BRCA1-deficient cells to employ an Exo1-independent hyper-resection pathway is a driver of PARPi resistance.","doi":"10.7554/eLife.33402","authors":"Leland BA, Chen AC, Zhao AY, Wharton RC, King MC","authors_abbrev":"Leland BA et al.","pubmed_publication_date":"26 Apr 2018","pubmed_entrez_date":"2018-04-27","publication_year":"2018","canto_session_key":"b9ee517cdefb5f7c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Megan King","canto_first_approved_date":"2026-03-26 09:04:25","canto_approved_date":"2026-03-26 09:04:25","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-03-25 08:25:29","canto_added_date":"2018-04-28 00:15:04","annotation_curators":[{"name":"Megan King","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":6,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.05","SPAC688.10","SPAC2G11.12","SPBC342.05","SPBC12D12.09","SPBC543.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2026-03-26"},{"uniquename":"EMBL:AU010730","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.82"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11780129","title":"Recruitment of cohesin to heterochromatic regions by Swi6/HP1 in fission yeast.","citation":"Nat Cell Biol 2002 Jan;4(1):89-93","abstract":"Fission yeast centromeres, like those of higher eukaryotes, are composed of repeated DNA structures and associated heterochromatin protein complexes, that have a critical function in the faithful segregation of chromosomes during cell division. Cohesin protein complexes, which are essential for sister-chromatid cohesion and proper chromosome segregation, are enriched at centromeric repeats. We have identified a functional and physical link between heterochromatin and cohesin. We find that the preferential localization of cohesins at the centromeric repeats is dependent on Swi6, a conserved heterochromatin protein that is required for proper kinetochore function. Cohesin is also enriched at the mating-type heterochromatic region in a manner that depends on Swi6 and is required to preserve the genomic integrity of this locus. We provide evidence that a cohesin subunit Psc3 interacts with Swi6 and its mouse homologue HP1. These data define a conserved function of Swi6/HP1 in recruitment of cohesin to heterochromatic regions, promoting the proper segregation of chromosomes.","authors":"Nonaka N, Kitajima T, Yokobayashi S, Xiao G, Yamamoto M, Grewal SI, Watanabe Y","authors_abbrev":"Nonaka N et al.","pubmed_publication_date":"Jan 2002","pubmed_entrez_date":"2002-01-10","publication_year":"2002","canto_session_key":"8ddb4e6192c755eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-04-12 16:44:20","canto_approved_date":"2026-01-30 14:26:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-13 07:29:33","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.20c","SPCC338.17c","SPAC17H9.20","SPBC29A10.04","SPCC11E10.08","SPAC664.01c","SPAC3G6.06c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2024-04-12"},{"uniquename":"PMID:34352089","title":"Co-transcriptional RNA cleavage by Drosha homolog Pac1 triggers transcription termination in fission yeast.","citation":"Nucleic Acids Res 2021 Sep 07;49(15):8610-8624","abstract":"Transcription termination of protein-coding genes in eukaryotic cells usually relies on a tight coordination between the cleavage and polyadenylation of the pre-mRNA, and 5'-3' degradation of the downstream nascent transcript. Here we investigated the contribution of the essential fission yeast endonuclease Pac1, a homolog of human Drosha that cleaves hairpin RNA structures, in triggering polyadenylation-independent transcription termination. Using ChIP-sequencing in Pac1-deficient cells, we found that Pac1 triggers transcription termination at snRNA and snoRNA genes as well as at specific protein-coding genes. Notably, we found that Pac1-dependent premature termination occurred at two genes encoding conserved transmembrane transporters whose expression were strongly repressed by Pac1. Analysis by genome editing indicated that a stem-loop structure in the nascent transcript directs Pac1-mediated cleavage and that the regions upstream and downstream of the Pac1 cleavage site in the targeted mRNAs were stabilized by mutation of nuclear 3'-5' and 5'-3' exonucleases, respectively. Our findings unveil a premature transcription termination pathway that uncouples co-transcriptional RNA cleavage from polyadenylation, triggering rapid nuclear RNA degradation.","doi":"10.1093/nar/gkab654","authors":"Yague-Sanz C, Duval M, Larochelle M, Bachand F","authors_abbrev":"Yague-Sanz C et al.","pubmed_publication_date":"07 Sep 2021","pubmed_entrez_date":"2021-08-05","publication_year":"2021","canto_session_key":"f5403fffd3ecaf81","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"François Bachand","canto_first_approved_date":"2021-11-07 20:02:07","canto_approved_date":"2024-03-29 12:45:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-10-28 10:40:25","canto_added_date":"2021-08-07 00:15:03","annotation_curators":[{"name":"François Bachand","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.03","SPBC530.02","SPBC119.11c","SPSNORNA.21","SPSNORNA.54","SPSNRNA.01","SPSNRNA.02","SPSNRNA.04","SPSNRNA.05","SPAC11D3.05","SPAC26A3.12c","SPSNORNA.33","SPSNRNA.07"],"gene_count":13,"ltp_gene_count":4,"approved_date":"2021-11-07"},{"uniquename":"PMID:30110807","title":"Active bundles of polar and bipolar filaments.","citation":"Phys Rev E 2018 Jul;98(1-1):012413","abstract":"Bundles of actin filaments and molecular motors of the myosin family are a common subcellular organizational motif. Typically, such bundles are under contractile stress resulting from interactions between the filaments and the motors. This holds in particular for contractile rings that appear in the late stages of cell division in animal cells and that cleave the mother into two daughter cells. It was recently shown that myosin organizes into regularly spaced clusters along rings in mammalian cells, whereas myosin clusters in fission yeast travel along the perimeter of actomyosin rings [Wollrab et al., Nat. Commun. 7, 11860 (2016)2041-172310.1038/ncomms11860]. A mechanism based on the association of the structurally polar actin filaments into bipolar structures was shown to provide a common explanation for both observations. Here, we analyze the dynamics of this mechanism in detail. We find a rich phase diagram depending on the actomyosin interaction strength and the stability of the bipolar structures. The system can notably organize into traveling waves. Furthermore, we identify the nature of the bifurcations connecting the various patterns as parameters are changed. Finally, we report experimental patterns observed in cytokinetic rings in fission yeast and link them to solutions of our dynamic equations. Our analysis highlights the possible role played by local polarity sorting of actin filaments for the dynamics and functionality of actomyosin networks.","doi":"10.1103/PhysRevE.98.012413","authors":"Kreten FH, Hoffmann C, Riveline D, Kruse K","authors_abbrev":"Kreten FH et al.","pubmed_publication_date":"Jul 2018","pubmed_entrez_date":"2018-08-17","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-08-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29514920","title":"Cell size-dependent regulation of Wee1 localization by Cdr2 cortical nodes.","citation":"J Cell Biol 2018 May 07;217(5):1589-1599","abstract":"Cell size control requires mechanisms that link cell growth with Cdk1 activity. In fission yeast, the protein kinase Cdr2 forms cortical nodes that include the Cdk1 inhibitor Wee1 along with the Wee1-inhibitory kinase Cdr1. We investigated how nodes inhibit Wee1 during cell growth. Biochemical fractionation revealed that Cdr2 nodes were megadalton structures enriched for activated Cdr2, which increases in level during interphase growth. In live-cell total internal reflection fluorescence microscopy videos, Cdr2 and Cdr1 remained constant at nodes over time, but Wee1 localized to nodes in short bursts. Recruitment of Wee1 to nodes required Cdr2 kinase activity and the noncatalytic N terminus of Wee1. Bursts of Wee1 localization to nodes increased 20-fold as cells doubled in size throughout G2. Size-dependent signaling was caused in part by the Cdr2 inhibitor Pom1, which suppressed Wee1 node bursts in small cells. Thus, increasing Cdr2 activity during cell growth promotes Wee1 localization to nodes, where inhibitory phosphorylation of Wee1 by Cdr1 and Cdr2 kinases promotes mitotic entry.","doi":"10.1083/jcb.201709171","authors":"Allard CAH, Opalko HE, Liu KW, Medoh U, Moseley JB","authors_abbrev":"Allard CAH et al.","pubmed_publication_date":"07 May 2018","pubmed_entrez_date":"2018-03-09","publication_year":"2018","canto_session_key":"13625faa87e9dab3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Corey Allard","canto_first_approved_date":"2018-07-03 10:41:23","canto_approved_date":"2025-09-03 13:12:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-27 14:39:14","canto_added_date":"2018-03-10 01:15:04","annotation_curators":[{"name":"Corey Allard","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.03c","SPCC18B5.03","SPAC644.06c","SPAC57A10.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-07-03"},{"uniquename":"PMID:11950927","title":"The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with the inner centromere protein Pic1 and mediates chromosome segregation and cytokinesis.","citation":"Mol Biol Cell 2002 Apr;13(4):1132-43","abstract":"The chromosomal passenger proteins aurora-B, survivin, and inner centromere protein (INCENP) have been implicated in coordinating chromosome segregation with cell division. This work describes the interplay between aurora, survivin, and INCENP orthologs in the fission yeast Schizosaccharomyces pombe and defines their roles in regulating chromosome segregation and cytokinesis. We describe the cloning and characterization of the aurora-related kinase gene ark1(+), demonstrating that it is an essential gene required for sister chromatid segregation. Cells lacking Ark1p exhibit the cut phenotype, DNA fragmentation, and other defects in chromosome segregation. Overexpression of a kinase-defective version of Ark1, Ark1-K147R, inhibits cytokinesis, with cells exhibiting an elongated, multiseptate phenotype. Ark1p interacts physically and/or genetically with the survivin and INCENP orthologs Bir1p and Pic1p. We identified Pic1p in a two-hybrid screen for Ark1-K147R interacting partners and went on to map domains in both proteins that mediate their binding. Pic1p residues 925-972 are necessary and sufficient for Ark1p binding, which occurs through the kinase domain. As with Ark1-K147R, overexpression of Ark1p-binding fragments of Pic1p leads to multiseptate phenotypes. We also provide evidence that the dominant-negative effect of Ark1-K147R requires Pic1p binding, indicating that the formation of Ark1p-Pic1p complexes is required for the execution of cytokinesis.","authors":"Leverson JD, Huang HK, Forsburg SL, Hunter T","authors_abbrev":"Leverson JD et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-16","publication_year":"2002","canto_session_key":"b7c7becd0bc7a254","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-06-30 18:15:19","canto_approved_date":"2025-09-03 16:23:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-30 18:11:18","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.15","SPCC962.02c","SPCC320.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-06-30"},{"uniquename":"PMID:11952834","title":"Tropomyosin is required for the cell fusion process during conjugation in fission yeast.","citation":"Genes Cells 2002 Apr;7(4):375-84","abstract":"Tropomyosin is an actin-binding protein, which is thought to stabilize actin filaments and influence many aspects of F-actin. In fission yeast, the cdc8 gene encodes tropomyosin, and the gene product Cdc8p is known to be essential for the formation of the F-actin contractile ring and hence for cytokinesis in the mitotic cell cycle.\nWe isolated fission yeast mutants that were defective in cell fusion during conjugation. One of them turned out to carry a point mutation in cdc8. We found that the original temperature-sensitive cdc8 mutant frequently failed to undergo cell fusion when mated at a semi-permissive temperature. Additional cdc8 mutants isolated by targeted mutagenesis also showed defects in both cell fusion and cytokinesis. A decrease in the amount of intracellular Cdc8p also affected both, but cell growth was more severely blocked than cell fusion in this case. Immunostaining revealed that Cdc8p was localized as a spot at the cell-to-cell attachment site during conjugation, without overlapping with F-actin patches.\nTropomyosin Cdc8p is indispensable for cell fusion during conjugation in fission yeast. However, cell fusion appears to require fewer tropomyosin molecules than cytokinesis. We speculate that tropomyosin may organize a small F-actin-containing organelle at the cell-to-cell contact site in each mating cell, which plays a key role in cell fusion.","authors":"Kurahashi H, Imai Y, Yamamoto M","authors_abbrev":"Kurahashi H et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-16","publication_year":"2002","canto_session_key":"6550c24d9d5e0527","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-09 21:00:25","canto_approved_date":"2026-01-01 16:12:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-07 13:31:41","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.02c","SPAC27F1.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-03-09"},{"uniquename":"EMBL:AU007971","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10679013","title":"The puc1 cyclin regulates the G1 phase of the fission yeast cell cycle in response to cell size.","citation":"Mol Biol Cell 2000 Feb;11(2):543-54","abstract":"Eukaryotic cells coordinate cell size with cell division by regulating the length of the G1 and G2 phases of the cell cycle. In fission yeast, the length of the G1 phase depends on a precise balance between levels of positive (cig1, cig2, puc1, and cdc13 cyclins) and negative (rum1 and ste9-APC) regulators of cdc2. Early in G1, cyclin proteolysis and rum1 inhibition keep the cdc2/cyclin complexes inactive. At the end of G1, the balance is reversed and cdc2/cyclin activity down-regulates both rum1 and the cyclin-degrading activity of the APC. Here we present data showing that the puc1 cyclin, a close relative of the Cln cyclins in budding yeast, plays an important role in regulating the length of G1. Fission yeast cells lacking cig1 and cig2 have a cell cycle distribution similar to that of wild-type cells, with a short G1 and a long G2. However, when the puc1(+) gene is deleted in this genetic background, the length of G1 is extended and these cells undergo S phase with a greater cell size than wild-type cells. This G1 delay is completely abolished in cells lacking rum1. Cdc2/puc1 function may be important to down-regulate the rum1 Cdk inhibitor at the end of G1.","authors":"Martín-Castellanos C, Blanco MA, de Prada JM, Moreno S","authors_abbrev":"Martín-Castellanos C et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-02-26","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.09","SPCC4E9.02","SPBC19F5.01c","SPBC11B10.09","SPAPB2B4.03"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:28087710","title":"Targeting Argonaute to chromatin.","citation":"Genes Dev 2016 Dec 15;30(24):2649-2650","abstract":"In many eukaryotes, siRNAs bound to Argonaute proteins guide chromatin-modifying enzymes to complementary loci, resulting in transcriptional gene silencing. Multiple lines of evidence indicate that siRNAs base-pair with longer RNAs produced at target loci, but the possibility that siRNAs base-pair directly with DNA remains an attractive hypothesis. In a recent study, Shimada et al. (pp. 2571-2580) conducted experiments that address these alternative hypotheses, yielding additional evidence that fission yeast siRNA-Argonaute silencing complexes are recruited to target loci exclusively via interactions with nascent transcripts.","doi":"10.1101/gad.294900.116","authors":"Wendte JM, Pikaard CS","authors_abbrev":"Wendte JM et al.","pubmed_publication_date":"15 Dec 2016","pubmed_entrez_date":"2017-01-15","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-01-16 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1937013","title":"Identification of two cell-cycle-controlling cdc2 gene homologs in Arabidopsis thaliana.","citation":"Gene 1991 Sep 15;105(2):159-65","abstract":"The cdc2 gene product (p34cdc2) has been thought to play a central role in control of the mitotic cell cycle of yeasts and animals. To approach an understanding of the cell-cycle-control system in higher plants, we isolated, from an Arabidopsis thaliana cDNA library, two clones (CDC2a and CDC2b) similar to the Schizosaccharomyces pombe cdc2 gene. Genomic Southern-blot analysis with the CDC2a and CDC2b cDNA probes suggested that the A. thaliana genome contains several additional cdc2-like genes, which together with the CDC2a and CDC2b genes may constitute a CDC2 gene family. The CDC2a cDNA expressed in Sc. pombe corrected the elongated morphology, caused by the temperature-sensitive cdc2-33 mutation, to the normal shapes, indicating that the A. thaliana CDC2a gene product resembles Sc. pombe p34cdc2 functionally as well as structurally. These results support the view that the cell cycle of higher plants is controlled by an analogue of a p34cdc2-centered regulatory system like that of yeasts and animals.","authors":"Hirayama T, Imajuku Y, Anai T, Matsui M, Oka A","authors_abbrev":"Hirayama T et al.","pubmed_publication_date":"15 Sep 1991","pubmed_entrez_date":"1991-09-15","publication_year":"1991","canto_session_key":"7bef6308897f9544","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 12:32:17","canto_session_submitted_date":"2012-03-03 12:31:59","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:37625737","title":"Strategies for rapid production of crystallization quality coatomer WD40 domains.","citation":"Protein Expr Purif 2023 Dec;212:106358","abstract":"The vesicular secretion of soluble cargo proteins from the endoplasmic reticulum (ER) is accompanied by the export of ER-resident membrane proteins that are co-packaged in secretory vesicles. The cytosolic coatomer protein complex I (COPI) utilizes the N-terminal WD40 domains of α-COPI and β'-COPI subunits to bind these membrane protein \"clients\" for ER retrieval. These \"αWD40\" and \"β'WD40\" domains are structural homologs that demonstrate distinct selectivity for client proteins. However, elucidation of the atomic-level principles of coatomer-client interactions has been challenging due to the tendency of αWD40 domain to undergo aggregation during expression and purification. Here we describe a rapid recombinant production strategy from E. coli, which substantially enhances the quality of the purified αWD40 domain. The αWD40 purification and crystallization are completed within one day, which minimizes aggregation losses and yields a 1.9 Å resolution crystal structure. We demonstrate the versatility of this strategy by applying it to purify the β'WD40 domain, which yields crystal structures in the 1.2-1.3 Å resolution range. As an alternate recombinant production system, we develop a cost-effective strategy for αWD40 production in human Expi293 cells. Finally, we suggest a roadmap to simplify these protocols further, which is of significance for the production of WD40 mutants prone to rapid aggregation. The WD40 production strategies presented here are likely to have broad applications because the WD40 domain represents one of the largest families of biomolecular interaction modules in the eukaryotic proteome and is critical for trafficking of host as well as viral proteins such as the SARS-CoV-2 spike protein.","doi":"10.1016/j.pep.2023.106358","authors":"Dey D, Hasan SS","authors_abbrev":"Dey D et al.","pubmed_publication_date":"Dec 2023","pubmed_entrez_date":"2023-08-25","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBPJ4664.04"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"8evl","gene_chains":[{"gene_uniquename":"SPBPJ4664.04","chain":"A/B/C","position":"1-327"}],"title":"Crystal structure of alpha-COPI N-terminal WD40 domain","entry_authors":"Dey D,Hasan SS","entry_authors_abbrev":"Dey D et al.","reference_uniquename":"PMID:37625737","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:11041002","title":"[Chromosomal localization of rpb9+ and tfa1+ genes, coding for components of the mRNA synthesis apparatus of Schizosaccharomyces pombe].","citation":"Bioorg Khim 2000 Aug;26(8):623-30","abstract":"Using DNA hybridization on cosmid filters of high density, we established chromosomal localization of the rpb9+ gene encoding one of the specific subunits of RNA polymerase II of Schizosaccharomyces pombe and thus filled in the last gap in the mapping of the genes encoding components of RNA polymerase II of the fission yeast. The primary structure of three extended regions of the Sz. pombe chromosome I was elucidated and, as a result, genes neighboring on rpb9+ were identified. One of them proved to be the tfa1+ gene, encoding the large (alpha) subunit of the general factor of transcription initiation TFIIE.","authors":"Shpakovskiĭ GV, Baranova GM","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2000-10-21","publication_year":"2000","canto_session_key":"1e9fcb0d5b44459b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 21:10:48","canto_approved_date":"2018-12-22 21:10:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 21:10:42","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"EMBL:SPAB538","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18203864","title":"Response of Schizosaccharomyces pombe to zinc deficiency.","citation":"Eukaryot Cell 2008 Mar;7(3):454-64","abstract":"A component of the cellular response to zinc deficiency operates via control of transcript abundance. Therefore, microarray analysis was employed to identify Schizosaccharomyces pombe genes whose mRNA levels are regulated by intracellular zinc status. A set of 57 genes whose mRNA levels were substantially reduced in response to zinc deficiency was identified, while the mRNA levels of 63 genes were increased by this condition. In order to investigate the mechanisms that control these responses, a genetic screen was employed to identify mutants with defective zinc-responsive gene expression. Two strains (II-1 and V7) that were identified by this screen harbor mutations that are linked to zrt1+, which encodes a putative Zrt/IRT-like protein (ZIP) zinc uptake transporter. Importantly, zrt1+ mRNA levels are increased in response to zinc deprivation, and cells lacking functional Zrt1 are highly impaired in their ability to proliferate at limiting zinc concentrations. Furthermore, zrt1 null cells were found to have severely reduced zinc contents, indicating that Zrt1 functions as a key regulator of intracellular zinc levels in fission yeast. The deletion of fet4+, another zinc-responsive gene encoding a putative metal ion transporter, exacerbated the phenotypes associated with the loss of Zrt1, suggesting that Fet4 also plays a role in zinc uptake under limiting conditions.","doi":"10.1128/EC.00408-07","authors":"Dainty SJ, Kennedy CA, Watt S, Bähler J, Whitehall SK","authors_abbrev":"Dainty SJ et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-01-22","publication_year":"2008","canto_session_key":"60100461d789b19f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2022-02-02 15:47:55","canto_approved_date":"2024-10-14 10:39:22","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2022-02-02 15:47:49","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.03","SPBC1348.06c","SPBC16D10.06","SPAC5H10.06c","SPBP26C9.03c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2022-02-02"},{"uniquename":"PMID:29789819","title":"Exploring the cellular uptake and localisation of phosphorescent rhenium fac-tricarbonyl metallosurfactants as a function of lipophilicity.","citation":"Dalton Trans 2018 Oct 16;47(40):14241-14253","abstract":"A systematic study of the cellular uptake of emissive complexes as a function of their lipophilicity is presented. Here a series of amphiphilic rhenium fac-tricarbonyl bisimine complexes bearing axial substituted imidazole or thiazole ligands, [Re(bpy)(CO)3(ImCnHm)]+ {n = 1 m = 3 (1+), n = 4 m = 9 (2+), n = 8 m = 17 (3+), n = 12 m = 25 (4+), n = 16 m = 33 (5+), n = 2 m = 3 (6+); bpy = 2,2'-bipyridine, Im = imidazole} and [Re(bpy)(CO)3(L)]+ {L = 1-mesitylimidazole, ImMes (7+), 4,5-dimethylthiazole, dmt (8+) and 4-methyl-5-thiazole-ethanol, mte (9+)} is reported. The X-ray crystal structures of 2+, 8+ and 9+ confirm the geometry and expected distribution of ligands and indicated that the plane of the imidazole/thiazole ring is approximately parallel to the long axis of the bipy ligand. Luminescence studies revealed excellent properties for their use in cell imaging with visible excitation and broad emission profiles. Their uptake in two distinct species has been examined by fluorescence imaging of the diplomonad fish parasite Spironucleus vortens (S. vortens) and rod-shaped yeast Schizosaccharomyces pombe (Schiz. pombe) as a function of their lipophilicity. The uptake of the complexes was highest for the more lipophilic 2+-5+ in both S. vortens and Schiz. pombe in which the long alkyl chain aids in crossing bilipid membranes. However, the increased lipophilicity of longer chains also resulted in greater toxicity. Localisation over the whole cell varied with differing alkyl chain lengths with complex 2+ preferentially locating to the nucleus of S. vortens, 3+ showing enhanced nuclear partitioning in Schiz. pombe, and 4+ for the remaining cell wall bound in the case of S. vortens. Interestingly, complexes of intermediate lipophilicity such as 7+ and 8+ showed reasonable uptake, proved to be non-toxic, and were capable of crossing exterior cell walls and localising in the organelles of the cells.","doi":"10.1039/c8dt00669e","authors":"Hallett AJ, Placet E, Prieux R, McCafferty D, Platts JA, Lloyd D, Isaacs M, Hayes AJ, Coles SJ, Pitak MB, Marchant S, Marriott SN, Allemann RK, Dervisi A, Fallis IA","authors_abbrev":"Hallett AJ et al.","pubmed_publication_date":"16 Oct 2018","pubmed_entrez_date":"2018-05-24","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-05-25 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:893531","title":"Effects of heat shock and cycloheximide on growth and division of the fission yeast, Schizosaccharomyces pombe. With an Appendix. Estimation of division delay for S. pombe from cell plate index curves.","citation":"J Cell Sci 1977 Feb;23:1-23","abstract":"","authors":"Polanshek MM","authors_abbrev":"Polanshek MM","pubmed_publication_date":"Feb 1977","pubmed_entrez_date":"1977-02-01","publication_year":"1977","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9108295","title":"The Schizosaccharomyces pombe cdc6 gene encodes the catalytic subunit of DNA polymerase delta.","citation":"Mol Gen Genet 1997 Mar 18;254(1):93-7","abstract":"The cdc6 mutants of Schizosaccharomyces pombe have been classified as being defective in progression through the G2 phase of the cell cycle. We cloned an S. pombe gene that could complement the temperature-sensitive growth of the cdc6-23 mutant. Unexpectedly, the cloned gene was allelic to pol3, which encodes the catalytic subunit of DNA polymerase delta. Integration mapping confirmed that ccd6 and pol3 are identical. The cdc6-23 mutant carries one amino acid substitution in the conserved N3 region of Pol3.","authors":"Iino Y, Yamamoto M","authors_abbrev":"Iino Y et al.","pubmed_publication_date":"18 Mar 1997","pubmed_entrez_date":"1997-03-18","publication_year":"1997","canto_session_key":"534081bf9d15560a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-12-18 15:24:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-25 11:07:38","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC336.12c","SPBC336.04"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-11-25"},{"uniquename":"PMID:12134075","title":"A fourth component of the fission yeast gamma-tubulin complex, Alp16, is required for cytoplasmic microtubule integrity and becomes indispensable when gamma-tubulin function is compromised.","citation":"Mol Biol Cell 2002 Jul;13(7):2360-73","abstract":"gamma-Tubulin functions as a multiprotein complex, called the gamma-tubulin complex (gamma-TuC), and composes the microtubule organizing center (MTOC). Fission yeast Alp4 and Alp6 are homologues of two conserved gamma-TuC proteins, hGCP2 and hGCP3, respectively. We isolated a novel gene, alp16(+), as a multicopy suppressor of temperature-sensitive alp6-719 mutants. alp16(+) encodes a 759-amino-acid protein with two conserved regions found in all other members of gamma-TuC components. In addition, Alp16 contains an additional motif, which shows homology to hGCP6/Xgrip210. Gene disruption shows that alp16(+) is not essential for cell viability. However, alp16 deletion displays abnormally long cytoplasmic microtubules, which curve around the cell tip. Furthermore, alp16-deleted mutants are hypersensitive to microtubule-depolymerizing drugs and synthetically lethal with either temperature-sensitive alp4-225, alp4-1891, or alp6-719 mutants. Overproduction of Alp16 is lethal, with defective phenotypes very similar to loss of Alp4 or Alp6. Alp16 localizes to the spindle pole body throughout the cell cycle and to the equatorial MTOC at postanaphase. Alp16 coimmunoprecipitates with gamma-tubulin and cosediments with the gamma-TuC in a large complex (>20 S). Alp16 is, however, not required for the formation of this large complex. We discuss evolutional conservation and divergence of structure and function of the gamma-TuC between yeast and higher eukaryotes.","authors":"Fujita A, Vardy L, Garcia MA, Toda T","authors_abbrev":"Fujita A et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-07-23","publication_year":"2002","canto_session_key":"358b3c6cea85e681","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-23 18:19:30","canto_approved_date":"2022-07-21 08:14:36","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2015-04-23 12:44:10","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["HGNC:18127","SPBC365.15","SPBC32F12.04","SPBC428.20c","SPCC4G3.19"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-01-23"},{"uniquename":"PMID:1177967","title":"On homo- and heterothallism in Schizosaccharomyces pombe.","citation":"Mycologia 1975;67(4):748-59","abstract":"","authors":"Gutz H, Doe FJ","authors_abbrev":"Gutz H et al.","pubmed_publication_date":"1975","pubmed_entrez_date":"1975-07-01","publication_year":"1975","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29021344","title":"A microtubule polymerase cooperates with the kinesin-6 motor and a microtubule cross-linker to promote bipolar spindle assembly in the absence of kinesin-5 and kinesin-14 in fission yeast.","citation":"Mol Biol Cell 2017 Dec 01;28(25):3647-3659","abstract":"Accurate chromosome segregation relies on the bipolar mitotic spindle. In many eukaryotes, spindle formation is driven by the plus-end-directed motor kinesin-5 that generates outward force to establish spindle bipolarity. Its inhibition leads to the emergence of monopolar spindles with mitotic arrest. Intriguingly, simultaneous inactivation of the minus-end-directed motor kinesin-14 restores spindle bipolarity in many systems. Here we show that in fission yeast, three independent pathways contribute to spindle bipolarity in the absence of kinesin-5/Cut7 and kinesin-14/Pkl1. One is kinesin-6/Klp9 that engages with spindle elongation once short bipolar spindles assemble. Klp9 also ensures the medial positioning of anaphase spindles to prevent unequal chromosome segregation. Another is the Alp7/TACC-Alp14/TOG microtubule polymerase complex. Temperature-sensitive  alp7cut7pkl1  mutants are arrested with either monopolar or very short spindles. Forced targeting of Alp14 to the spindle pole body is sufficient to render  alp7cut7pkl1  triply deleted cells viable and promote spindle assembly, indicating that Alp14-mediated microtubule polymerization from the nuclear face of the spindle pole body could generate outward force in place of Cut7 during early mitosis. The third pathway involves the Ase1/PRC1 microtubule cross-linker that stabilizes antiparallel microtubules. Our study, therefore, unveils multifaceted interplay among kinesin-dependent and -independent pathways leading to mitotic bipolar spindle assembly.","doi":"10.1091/mbc.E17-08-0497","authors":"Yukawa M, Kawakami T, Okazaki M, Kume K, Tang NH, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"01 Dec 2017","pubmed_entrez_date":"2017-10-13","publication_year":"2017","canto_session_key":"17cceecf86230427","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2018-02-02 14:49:50","canto_approved_date":"2024-04-03 16:08:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-01 07:40:37","canto_added_date":"2017-10-17 00:15:30","annotation_curators":[{"name":"Takashi Toda","community_curator":true,"annotation_count":40,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.04c","SPAC3A11.14c","SPAPB1A10.09","SPAC4D7.07c","SPCC736.14","SPBC13E7.06","SPCC895.07","SPAC890.02c","SPBC15D4.01c","SPBC2G2.14","SPCC1322.12c","SPAC25G10.07c","SPBC20F10.06"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2018-02-02"},{"uniquename":"GO_REF:0000074","title":"Representation of export of a chemical as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the export of a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom template is \"GO:0006810 and 'exports' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21811607","title":"Transient receptor potential (TRP) and Cch1-Yam8 channels play key roles in the regulation of cytoplasmic Ca2+ in fission yeast.","citation":"PLoS One 2011;6(7):e22421","abstract":"The regulation of cytoplasmic Ca(2+) is crucial for various cellular processes. Here, we examined the cytoplasmic Ca(2+) levels in living fission yeast cells by a highly sensitive bioluminescence resonance energy transfer-based assay using GFP-aequorin fusion protein linked by 19 amino acid. We monitored the cytoplasmic Ca(2+) level and its change caused by extracellular stimulants such as CaCl(2) or NaCl plus FK506 (calcineurin inhibitor). We found that the extracellularly added Ca(2+) caused a dose-dependent increase in the cytoplasmic Ca(2+) level and resulted in a burst-like peak. The overexpression of two transient receptor potential (TRP) channel homologues, Trp1322 or Pkd2, markedly enhanced this response. Interestingly, the burst-like peak upon TRP overexpression was completely abolished by gene deletion of calcineurin and was dramatically decreased by gene deletion of Prz1, a downstream transcription factor activated by calcineurin. Furthermore, 1 hour treatment with FK506 failed to suppress the burst-like peak. These results suggest that the burst-like Ca(2+) peak is dependent on the transcriptional activity of Prz1, but not on the direct TRP dephosphorylation. We also found that extracellularly added NaCl plus FK506 caused a synergistic cytosolic Ca(2+) increase that is dependent on the inhibition of calcineurin activity, but not on the inhibition of Prz1. The synergistic Ca(2+) increase is abolished by the addition of the Ca(2+) chelator BAPTA into the media, and is also abolished by deletion of the gene encoding a subunit of the Cch1-Yam8 Ca(2+) channel complex, indicating that the synergistic increase is caused by the Ca(2+) influx from the extracellular medium via the Cch1-Yam8 complex. Furthermore, deletion of Pmk1 MAPK abolished the Ca(2+) influx, and overexpression of the constitutively active Pek1 MAPKK enhanced the influx. These results suggest that Pmk1 MAPK and calcineurin positively and negatively regulate the Cch1-Yam8 complex, respectively, via modulating the balance between phosphorylation and dyphosphorylation state.","doi":"10.1371/journal.pone.0022421","authors":"Ma Y, Sugiura R, Koike A, Ebina H, Sio SO, Kuno T","authors_abbrev":"Ma Y et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-08-04","publication_year":"2011","canto_session_key":"ab447353ab14b3a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-14 06:04:49","canto_approved_date":"2026-03-26 22:38:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-23 10:58:22","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPAC1F7.03","SPAC1F5.08c","SPBC543.07","SPBC31E1.02c","SPAC3A12.14","SPCC663.14c","SPCC1322.03","SPAC4G8.13c","SPAC1F3.02c","SPAC6F6.01","SPBC119.08"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2017-07-14"},{"uniquename":"PMID:15647375","title":"The roles of fission yeast ase1 in mitotic cell division, meiotic nuclear oscillation, and cytokinesis checkpoint signaling.","citation":"Mol Biol Cell 2005 Mar;16(3):1378-95","abstract":"The Ase1/Prc1 proteins constitute a conserved microtubule-associated protein family that is implicated in central spindle formation and cytokinesis. Here we characterize a role for fission yeast Ase1. Ase1 localizes to microtubule overlapping zones and displays dynamic alterations of localization during the cell cycle. In particular, its spindle localization during metaphase is reduced substantially, followed by robust appearance at the spindle midzone in anaphase. ase1 deletions are viable but defective in nuclear and septum positioning and completion of cytokinesis, which leads to diploidization and chromosome loss. Time-lapse imaging shows that elongating spindles collapse abruptly in the middle of anaphase B. Either absence or overproduction of Ase1 results in profound defects on microtubule bundling in an opposed manner, indicating that Ase1 is a dose-dependent microtubule-bundling factor. In contrast microtubule nucleating activities are not noticeably compromised in ase1 mutants. During meiosis astral microtubules are not bundled and oscillatory nuclear movement is impaired significantly. The Aurora kinase does not correctly localize to central spindles in the absence of Ase1. Finally Ase1 acts as a regulatory component in the cytokinesis checkpoint that operates to inhibit nuclear division when the cytokinesis apparatus is perturbed. Ase1, therefore, couples anaphase completion with cytokinesis upon cell division.","authors":"Yamashita A, Sato M, Fujita A, Yamamoto M, Toda T","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-01-14","publication_year":"2005","canto_session_key":"1d66b48c0e2f2f2b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-02-10 09:19:01","canto_approved_date":"2024-05-02 05:54:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-26 15:00:09","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPBC26H8.07c","SPBC21.06c","SPCC320.13c","SPBC19G7.05c","SPAP8A3.08","SPAC4A8.15c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2016-02-10"},{"uniquename":"PMID:34910346","title":"Histone variant H2A.Z plays multiple roles in the maintenance of heterochromatin integrity.","citation":"Genes Cells 2022 Feb;27(2):93-112","abstract":"H2A.Z, an evolutionally well-conserved histone H2A variant, is involved in many biological processes. Although the function of H2A.Z in euchromatic gene regulation is well known, its function and deposition mechanism in heterochromatin are still unclear. Here, we report that H2A.Z plays multiple roles in fission yeast heterochromatin. While a small amount of H2A.Z localizes at pericentromeric heterochromatin, loss of methylation of histone H3 at Lys9 (H3K9me) induces the accumulation of H2A.Z, which is dependent on the H2A.Z loader, SWR complex. The accumulated H2A.Z suppresses heterochromatic non-coding RNA transcription. This transcriptional repression activity requires the N-terminal tail of H2A.Z, which is involved in the regulation of euchromatic gene transcription. RNAi-defective cells, in which a substantial amount of H3K9me is retained by RNAi-independent heterochromatin assembly, also accumulate H2A.Z at heterochromatin, and the additional loss of H2A.Z in these cells triggers a further decrease in H3K9me. Our results suggest that H2A.Z facilitates RNAi-independent heterochromatin assembly by antagonizing the demethylation activity of Epe1, an eraser of H3K9me. Furthermore, H2A.Z suppresses Epe1-mediated transcriptional activation, which is required for subtelomeric gene repression. Our results provide novel evidence that H2A.Z plays diverse roles in chromatin silencing.","doi":"10.1111/gtc.12911","authors":"Tsukii K, Takahata S, Murakami Y","authors_abbrev":"Tsukii K et al.","pubmed_publication_date":"Feb 2022","pubmed_entrez_date":"2021-12-15","publication_year":"2022","canto_session_key":"f4ccd02b3cf4f24a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-17 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1983087","title":"Biological activity of the mammalian RAP genes in yeast.","citation":"Cell Regul 1990 Sep;1(10):763-9","abstract":"We have screened expression libraries for mammalian cDNAs capable of suppressing defects in ras1- Schizosaccharomyces pombe. Both the RAP1A and RAP1B genes were identified in this manner. They suppress defects in cell morphology and sporulation, although not conjugation. In contrast, RAP genes do not suppress phenotypes in the yeast Saccharomyces cerevisiae that are deficient in RAS. Indeed, expression of RAP1A appears to antagonize the activated S. cerevisiae RAS2val19 gene. These results indicate that RAP proteins can interact with RAS targets, sometimes productively, sometimes nonproductively.","authors":"Xu HP, Wang Y, Riggs M, Rodgers L, Wigler M","authors_abbrev":"Xu HP et al.","pubmed_publication_date":"Sep 1990","pubmed_entrez_date":"1990-09-01","publication_year":"1990","canto_session_key":"8cd49ea131e995f2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 12:37:50","canto_session_submitted_date":"2012-03-03 12:37:27","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:1896023","title":"A quantitative assay to measure chromosome stability in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1991 Sep;229(1):77-80","abstract":"The fidelity of mitotic chromosome transmission in Schizosaccharomyces pombe was estimated quantitatively by using cycloheximide resistance as a means to select cells that had undergone chromosome loss or nondisjunction. We aimed to investigate the connection between recombination and mitotic chromosome stability. A number of mutants defective in mitotic recombination such as cdc17-L16, rec59-72, and rec50-25 were tested and in these an approximately ten fold elevation of mitotic haploidization rate was found compared with controls. Our data suggest that recombination is important in controlling the maintenance of chromosomes during mitosis.","authors":"Bodi Z, Gysler-Junker A, Kohli J","authors_abbrev":"Bodi Z et al.","pubmed_publication_date":"Sep 1991","pubmed_entrez_date":"1991-09-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37239918","title":"Identification of New FG-Repeat Nucleoporins with Amyloid Properties.","citation":"Int J Mol Sci 2023 May 10;24(10)","abstract":"Amyloids are fibrillar protein aggregates with a cross-β structure. More than two hundred different proteins with amyloid or amyloid-like properties are already known. Functional amyloids with conservative amyloidogenic regions were found in different organisms. Protein aggregation appears to be beneficial for the organism in these cases. Therefore, this property might be conservative for orthologous proteins. The amyloid aggregates of the CPEB protein were suggested to play an important role in the long-term memory formation in  Aplysia californica ,  Drosophila melanogaster , and  Mus musculus . Moreover, the FXR1 protein demonstrates amyloid properties among the Vertebrates. A few nucleoporins (e.g., yeast Nup49, Nup100, Nup116, and human Nup153 and Nup58), are supposed or proved to form amyloid fibrils. In this study, we performed wide-scale bioinformatic analysis of nucleoporins with FG-repeats (phenylalanine-glycine repeats). We demonstrated that most of the barrier nucleoporins possess potential amyloidogenic properties. Furthermore, the aggregation-prone properties of several Nsp1 and Nup100 orthologs in bacteria and yeast cells were analyzed. Only two new nucleoporins,  Drosophila melanogaster  Nup98 and  Schizosaccharomyces pombe  Nup98, aggregated in different experiments. At the same time,  Taeniopygia guttata  Nup58 only formed amyloids in bacterial cells. These results rather contradict the hypothesis about the functional aggregation of nucleoporins.","doi":"10.3390/ijms24108571","authors":"Danilov LG, Sukhanova XV, Rogoza TM, Antonova EY, Trubitsina NP, Zhouravleva GA, Bondarev SA","authors_abbrev":"Danilov LG et al.","pubmed_publication_date":"10 May 2023","pubmed_entrez_date":"2023-05-27","publication_year":"2023","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2023-05-28 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23536430","title":"The VPS35 gene and Parkinson's disease.","citation":"Mov Disord 2013 May;28(5):569-75","abstract":"Parkinson's disease (PD), the second most common age-related neurodegenerative disease, is characterized by loss of dopaminergic and nondopaminergic neurons, leading to a variety of motor and nonmotor symptoms. In addition to environmental factors, genetic predisposition and specific gene mutations have been shown to play an important role in the pathogenesis of this disorder. Recently, the identification of the vacuolar protein sorting 35 homolog gene (VPS35), linked to autosomal dominant late-onset PD, has provided new clues to the pathogenesis of PD. Here we discuss the VPS35 gene, its protein function, and various pathways involved in Wnt/β-catenin signaling and in the role of DMT1 mediating the uptake of iron and iron translocation from endosomes to the cytoplasm. Further understanding of these mechanisms will undoubtedly provide new insights into the pathogenic mechanisms of PD and may lead to prevention and better treatment of the disorder.","doi":"10.1002/mds.25430","authors":"Deng H, Gao K, Jankovic J","authors_abbrev":"Deng H et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-03-29","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC777.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1819510","title":"New elements in the mitotic control of the fission yeast Schizosaccharomyces pombe.","citation":"Cold Spring Harb Symp Quant Biol 1991;56:605-11","abstract":"The p107wee1 protein kinase plays a central role in regulating the cell cycle of fission yeast. It mediates transmission of signal(s) related to the nutritional status of the cell to the p34cdc2 protein kinase, which is an active component of the MPF complex driving cells into mitosis. p107wee1 is itself subject to control by the products of other genes such as nim1+/cdr1+, win1+, and perhaps wis1+ and other wis+ genes. At present, the relationships between these genes and their possible roles in the mitotic control are unclear and must await further analysis (Fig. 5). It is likely that some of the gene products are concerned with the sensing and/or transmission of nutritional signals. p107wee1 negatively regulates the activity of p34cdc2, probably by direct tyrosine phosphorylation, and also appears to regulate the activities of the cdc1+ and cdc27+ gene products. The effects of nitrogen starvation and of wee1 mutations on conditional lethal mutations at the cdc1, cdc2, and cdc27 loci, taken together, support the largely speculative model shown in Figure 5. During the normal cycle, the balance between phosphorylated and dephosphorylated p34cdc2 changes such that at the appropriate time, p34cdc2 is activated and the cell enters mitosis. We suggest that the cdc1+ and cdc27+ products may be regulated in a similar way. Such a mechanism would ensure coordinated activation of these and perhaps other proteins required for the G2/M transition. There are, of course, many uncertainties, and these must await elucidation by biochemical and genetic analysis.","authors":"Fantes PA, Warbrick E, Hughes DA, MacNeill SA","authors_abbrev":"Fantes PA et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31883795","title":"Positioning Heterochromatin at the Nuclear Periphery Suppresses Histone Turnover to Promote Epigenetic Inheritance.","citation":"Cell 2020 Jan 09;180(1):150-164.e15","abstract":"In eukaryotes, heterochromatin is generally located at the nuclear periphery. This study investigates the biological significance of perinuclear positioning for heterochromatin maintenance and gene silencing. We identify the nuclear rim protein Amo1 NUPL2  as a factor required for the propagation of heterochromatin at endogenous and ectopic sites in the fission yeast genome. Amo1 associates with the Rix1 PELP1 -containing RNA processing complex RIXC and with the histone chaperone complex FACT. RIXC, which binds to heterochromatin protein Swi6 HP1  across silenced chromosomal domains and to surrounding boundary elements, connects heterochromatin with Amo1 at the nuclear periphery. In turn, the Amo1-enriched subdomain is critical for Swi6 association with FACT that precludes histone turnover to promote gene silencing and preserve epigenetic stability of heterochromatin. In addition to uncovering conserved factors required for perinuclear positioning of heterochromatin, these analyses elucidate a mechanism by which a peripheral subdomain enforces stable gene repression and maintains heterochromatin in a heritable manner.","doi":"10.1016/j.cell.2019.12.004","authors":"Holla S, Dhakshnamoorthy J, Folco HD, Balachandran V, Xiao H, Sun LL, Wheeler D, Zofall M, Grewal SIS","authors_abbrev":"Holla S et al.","pubmed_publication_date":"09 Jan 2020","pubmed_entrez_date":"2019-12-30","publication_year":"2020","canto_session_key":"69a310e75d21c964","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sahana Holla","canto_first_approved_date":"2025-03-03 09:52:26","canto_approved_date":"2025-03-03 09:52:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-02-21 10:35:21","canto_added_date":"2020-01-17 12:14:11","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":83,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Sahana Holla","community_curator":true,"annotation_count":100,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H1.01c","SPBC28F2.02","SPCC736.11","SPBC609.05","SPAPB1E7.03","SPBC1861.02","SPAC29B12.01","SPBC1D7.04","SPCC1902.02","SPBC660.13c","SPAC26A3.12c","SPBP8B7.20c","SPAC23C4.15","SPBC713.10","SPAC16.02c","SPBP8B7.19","SPAC2F3.04c","SPAC1834.03c","SPAC1250.01","SPBC1A4.03c","SPAC17A2.13c","SPAC4G9.08c","SPAC1B3.05","SPCC18B5.07c","SPBC646.10c","SPCP1E11.11","SPAC16E8.06c","SPBC660.11","SPBP22H7.02c","SPBP23A10.13","SPBC1734.15","SPBC16A3.05c","SPBC1778.02","SPAC1486.05","SPCC18.06c","SPBC1105.17","SPAC1834.04","SPBC14F5.03c","SPBC1289.07c","SPAC19G12.06c","SPCC18.07","SPCC330.13","SPAC16E8.01","SPCC290.02","SPCC31H12.08c","SPCC622.09","SPCC162.08c","SPAPB8E5.09","SPCC1682.04","SPCC4G3.15c","SPAC9.09","SPAC1687.01","SPAP8A3.09c","SPBC557.03c","SPCC1902.01","SPBC31F10.14c","SPBC16C6.12c","SPCC830.03","SPAC29B12.06c","SPAC31G5.19","SPBC31E1.05","SPAC694.06c","SPAC664.01c","SPAC13G7.08c","SPCC622.08c","SPAC15A10.15","SPAC29B12.02c","SPBC2G5.07c","SPAC227.02c","SPCC622.16c","SPAC3C7.08c","SPMTR.01","SPBC365.10","SPAC57A7.04c","SPBC16E9.12c","SPBC651.08c","SPCC1393.06c","SPCC4G3.18","SPAC1783.05","SPAC23C11.11","SPAC23G3.06","SPBC83.08","SPAC19E9.01c","SPAC23H4.12","SPAC30D11.04c","SPAC144.06","SPCC736.12c","SPBC28F2.11","SPBC15D4.10c","SPBC428.08c","SPCC285.13c","SPAC18G6.10","SPBC19C7.10","SPBC11B10.10c","SPBC16C6.10","SPBP35G2.10","SPCC1753.01c","SPAC4H3.11c","SPCC1672.02c","SPCC188.07","SPAC1556.01c","SPAC14C4.05c","SPAC20G8.06","SPBC13A2.02","SPAC23D3.06c"],"gene_count":105,"ltp_gene_count":102,"approved_date":"2025-03-03"},{"uniquename":"PMID:19352039","title":"Identification of Ecl family genes that extend chronological lifespan in fission yeast.","citation":"Biosci Biotechnol Biochem 2009 Apr 23;73(4):885-9","abstract":"In fission yeast, we identified two genes, named ecl2+ and ecl3+, that are paralogous to ecl1+, which extends the chronological lifespan. Both ecl2+ and ecl3+ extend the chronological lifespan when overexpressed as ecl1+. ecl2+ and ecl3+ encode 84- and 89-amino acid polypeptides respectively that are not annotated in the current database. The Ecl2 protein is localized mainly in the nucleus, as Ecl1. These results suggest that ecl1+, ecl2+, and ecl3+ have overlapping functions in the regulation of chronological lifespan.","authors":"Ohtsuka H, Ogawa Y, Mizuno H, Mita S, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"23 Apr 2009","pubmed_entrez_date":"2009-04-09","publication_year":"2009","canto_session_key":"4e5bbb90328509e9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_approved_date":"2015-03-31 16:25:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-31 16:25:46","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.16c","SPCC70.12c","SPBC8E4.12c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-03-31"},{"uniquename":"PMID:11723232","title":"Anticancer agent E7070 inhibits amino acid and uracil transport in fission yeast.","citation":"Mol Pharmacol 2001 Dec;60(6):1254-9","abstract":"E7070 is a novel sulfonamide anticancer agent that inhibits cell cycle progression in G1 in mammalian cells, but its action targets are not known. We recently employed the genetically amenable fission yeast Schizosaccharomyces pombe as a model organism to search for its targets. Here, we show that E7070 inhibits imports of amino acid and uracil into S. pombe cells. Unlike their prototrophic counterparts, leucine- and uracil-auxotrophic strains are sensitive to E7070 and are unable to proliferate with a delayed G1-S transition in low-glucose yeast extract-polypeptone medium containing this drug because this chemical markedly inhibits the uptake of leucine and uracil in low glucose medium. Furthermore, addition of leucine or uracil to the culture medium or overexpression of genes encoding an amino acid or uracil transporter suppresses the E7070-imposed growth inhibition of these auxotrophic strains. Thus, some of the molecular targets for E7070 action in S. pombe are likely to be leucine and uracil transporters.","authors":"Tsukahara K, Watanabe T, Hata-Sugi N, Yoshimatsu K, Okayama H, Nagasu T","authors_abbrev":"Tsukahara K et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-11-28","publication_year":"2001","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013406","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32047038","title":"Basis for metabolite-dependent Cullin-RING ligase deneddylation by the COP9 signalosome.","citation":"Proc Natl Acad Sci U S A 2020 Feb 25;117(8):4117-4124","abstract":"The Cullin-RING ligases (CRLs) are the largest family of ubiquitin E3s activated by neddylation and regulated by the deneddylase COP9 signalosome (CSN). The inositol polyphosphate metabolites promote the formation of CRL-CSN complexes, but with unclear mechanism of action. Here, we provide structural and genetic evidence supporting inositol hexakisphosphate (IP 6 ) as a general CSN cofactor recruiting CRLs. We determined the crystal structure of IP 6  in complex with CSN subunit 2 (CSN2), based on which we identified the IP 6 -corresponding electron density in the cryoelectron microscopy map of a CRL4A-CSN complex. IP 6  binds to a cognate pocket formed by conserved lysine residues from CSN2 and Rbx1/Roc1, thereby strengthening CRL-CSN interactions to dislodge the E2 CDC34/UBE2R from CRL and to promote CRL deneddylation. IP 6  binding-deficient  Csn2   K70E/K70E   knockin mice are embryonic lethal. The same mutation disabled  Schizosaccharomyces pombe  Csn2 from rescuing UV-hypersensitivity of  csn2 -null yeast. These data suggest that CRL transition from the E2-bound active state to the CSN-bound sequestered state is critically assisted by an interfacial IP 6  small molecule, whose metabolism may be coupled to CRL-CSN complex dynamics.","doi":"10.1073/pnas.1911998117","authors":"Lin H, Zhang X, Liu L, Fu Q, Zang C, Ding Y, Su Y, Xu Z, He S, Yang X, Wei X, Mao H, Cui Y, Wei Y, Zhou C, Du L, Huang N, Zheng N, Wang T, Rao F","authors_abbrev":"Lin H et al.","pubmed_publication_date":"25 Feb 2020","pubmed_entrez_date":"2020-02-13","publication_year":"2020","canto_session_key":"1f2b998f7febc360","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-09-28 15:45:08","canto_approved_date":"2020-09-28 15:45:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-28 15:44:49","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H4.18c","SPCC4B3.10c","SPAC17G6.12","SPAPB17E12.04c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2020-09-28"},{"uniquename":"PMID:26729913","title":"BioGRID: A Resource for Studying Biological Interactions in Yeast.","citation":"Cold Spring Harb Protoc 2016 Jan 04;2016(1):pdb.top080754","abstract":"The Biological General Repository for Interaction Datasets (BioGRID) is a freely available public database that provides the biological and biomedical research communities with curated protein and genetic interaction data. Structured experimental evidence codes, an intuitive search interface, and visualization tools enable the discovery of individual gene, protein, or biological network function. BioGRID houses interaction data for the major model organism species--including yeast, nematode, fly, zebrafish, mouse, and human--with particular emphasis on the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe as pioneer eukaryotic models for network biology. BioGRID has achieved comprehensive curation coverage of the entire literature for these two major yeast models, which is actively maintained through monthly curation updates. As of September 2015, BioGRID houses approximately 335,400 biological interactions for budding yeast and approximately 67,800 interactions for fission yeast. BioGRID also supports an integrated posttranslational modification (PTM) viewer that incorporates more than 20,100 yeast phosphorylation sites curated through its sister database, the PhosphoGRID.","doi":"10.1101/pdb.top080754","authors":"Oughtred R, Chatr-aryamontri A, Breitkreutz BJ, Chang CS, Rust JM, Theesfeld CL, Heinicke S, Breitkreutz A, Chen D, Hirschman J, Kolas N, Livstone MS, Nixon J, O'Donnell L, Ramage L, Winter A, Reguly T, Sellam A, Stark C, Boucher L, Dolinski K, Tyers M","authors_abbrev":"Oughtred R et al.","pubmed_publication_date":"04 Jan 2016","pubmed_entrez_date":"2016-01-06","publication_year":"2016","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2016-01-07 01:19:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22349564","title":"Schizosaccharomyces pombe homologs of the Saccharomyces cerevisiae mitochondrial proteins Cbp6 and Mss51 function at a post-translational step of respiratory complex biogenesis.","citation":"Mitochondrion 2012 May;12(3):381-90","abstract":"Complexes III and IV of the mitochondrial respiratory chain contain a few key subunits encoded by the mitochondrial genome. In Saccharomyces cerevisiae, fifteen mRNA-specific translational activators control mitochondrial translation, of which five are conserved in Schizosaccharomyces pombe. These include homologs of Cbp3, Cbp6 and Mss51 that participate in translation and the post-translational steps leading to the assembly of respiratory complexes III and IV. In this study we show that in contrast to budding yeast, Cbp3, Cbp6 and Mss51 from S. pombe are not required for the translation of mitochondrial mRNAs, but fulfill post-translational functions, thus probably accounting for their conservation.","doi":"10.1016/j.mito.2012.02.002","authors":"Kühl I, Fox TD, Bonnefoy N","authors_abbrev":"Kühl I et al.","pubmed_publication_date":"May 2012","pubmed_entrez_date":"2012-02-22","publication_year":"2012","canto_session_key":"847e79ae2982da4f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-28 12:03:18","canto_approved_date":"2021-01-28 12:03:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-27 11:49:26","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":42,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.04c","SPCC4B3.17","SPMIT.01","SPMIT.11","SPMIT.04","SPCC11E10.04","SPBC947.14c","SPMIT.05","SPAC8C9.06c"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2021-01-28"},{"uniquename":"PMID:10392445","title":"Eleven novel sep genes of Schizosaccharomyces pombe required for efficient cell separation and sexual differentiation.","citation":"Yeast 1999 Jun 15;15(8):669-86","abstract":"Genetic analysis of 20 sterile mutants prone to form hyphae revealed 11 novel ste genes (sep6 to sep16) of Schizosaccharomyces pombe. None of the mutants was completely mycelial. Most mutants formed branching hyphae and showed normal septation. Aberrant septal structures and actin distribution were seen only at 36 degrees C. sep9-307, sep14-576 and sep15-598 showed genetic interactions with sep1-1, a mutation in a forkhead transcription factor homologue. Additional genetic interactions were detected between sep6-194, sep15-598 and cdc16-116, a mutant allele of an anaphase modulator of p34cdc2. sep9-307 and sep15-598 caused dikaryosis in wee1- background. In mating and sporulation tests, sep6-, sep7-, sep9-, sep10-, sep11- and sep15- proved to be defective in conjugation only, whereas sep8-, sep13- and sep16- were also defective in meiosis-sporulation. sep12- and sep14- were only partially sterile. All mutants could produce M-factor but sep8-, sep11-, sep15- and sep16- were defective in P-factor production. The mutations in sep8, sep11 and sep16 suppressed the pat1-114-driven meiosis. All mutants were sensitive to the presence of higher concentrations of chloride in the medium and to short heat shocks. The diversity of the mutant phenotypes and the pleiotropic effects of the mutations suggest that these sep genes might act in, or interact with, a multiple overlapping network of regulatory modules.","authors":"Grallert A, Grallert B, Zilahi E, Szilagyi Z, Sipiczki M","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"15 Jun 1999","pubmed_entrez_date":"1999-07-07","publication_year":"1999","canto_session_key":"a02efb01ac764f2e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-06-25 14:47:57","canto_approved_date":"2026-01-29 17:48:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-25 14:47:42","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":81,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPCC18B5.03","SPBC14C8.17c","SPBC4C3.12","SPCP31B10.03c","SPBC21.04","SPBC19C2.05","SPAC5D6.05"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2020-06-25"},{"uniquename":"PMID:31217286","title":"Increasing ergosterol levels delays formin-dependent assembly of F-actin cables and disrupts division plane positioning in fission yeast.","citation":"J Cell Sci 2019 Jul 01;132(13)","abstract":"In most eukaryotes, cytokinesis is mediated by the constriction of a contractile acto-myosin ring (CR), which promotes the ingression of the cleavage furrow. Many components of the CR interact with plasma membrane lipids suggesting that lipids may regulate CR assembly and function. Although there is clear evidence that phosphoinositides play an important role in cytokinesis, much less is known about the role of sterols in this process. Here, we studied how sterols influence division plane positioning and CR assembly in fission yeast. We show that increasing ergosterol levels in the plasma membrane blocks the assembly of F-actin cables from cytokinetic precursor nodes, preventing their compaction into a ring. Abnormal F-actin cables form after a delay, leading to randomly placed septa. Since the formin Cdc12 was detected on cytokinetic precursors and the phenotype can be partially rescued by inhibiting the Arp2/3 complex, which competes with formins for F-actin nucleation, we propose that ergosterol may inhibit formin dependent assembly of F-actin cables from cytokinetic precursors.","doi":"10.1242/jcs.227447","authors":"Arbizzani F, Rincon SA, Paoletti A","authors_abbrev":"Arbizzani F et al.","pubmed_publication_date":"01 Jul 2019","pubmed_entrez_date":"2019-06-21","publication_year":"2019","canto_session_key":"eabcf681d0ea9788","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-25 13:31:00","canto_approved_date":"2024-05-03 12:57:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-02 15:10:43","canto_added_date":"2019-06-22 00:15:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":20,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.13c","SPAC1F5.04c","SPBC16E9.05","SPBC1A4.05","SPCC4B3.15","SPAC20G8.05c","SPBC146.13c","SPAC630.08c"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2024-03-25"},{"uniquename":"PMID:6696747","title":"A study of the maloalcoholic fermentation pathway in Schizosaccharomyces pombe.","citation":"Biochem J 1984 Jan 15;217(2):585-8","abstract":"The pathway of the maloalcoholic fermentation in Schizosaccharomyces pombe was investigated by a 1H-, 2H- and 13C-n.m.r.-spectroscopic study of hydrogen and deuterium distribution on the ethanol produced by S. pombe from L-malic acid in 2H2O and from L-[2-2H]malic acid. Our findings rule out a double-decarboxylation mechanism and agree with a pathway that involves acetaldehyde as intermediate.","authors":"Maconi E, Manachini PL, Aragozzini F, Gennari C, Ricca GS","authors_abbrev":"Maconi E et al.","pubmed_publication_date":"15 Jan 1984","pubmed_entrez_date":"1984-01-15","publication_year":"1984","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19228417","title":"MCM-GINS and MCM-MCM interactions in vivo visualised by bimolecular fluorescence complementation in fission yeast.","citation":"BMC Cell Biol 2009 Feb 19;10:12","abstract":"Each of the three individual components of the CMG complex (Cdc45, MCM and GINS) is essential for chromosomal DNA replication in eukaryotic cells, both for the initiation of replication at origins and also for normal replication fork progression. The MCM complex is a DNA helicase that most likely functions as the catalytic core of the replicative helicase, unwinding the parental duplex DNA ahead of the moving replication fork, whereas Cdc45 and the GINS complex are believed to act as accessory factors for MCM.\nTo investigate interactions between components of the CMG complex, we have used bimolecular fluorescence complementation (BiFC) in the fission yeast Schizosaccharomyces pombe for the first time, to analyse protein-protein interactions between GINS and MCM subunits expressed from their native chromosomal loci. We demonstrate interactions between GINS and MCM in the nuclei of exponentially-growing fission yeast cells and on chromatin in binucleate S-phase cells. In addition we present evidence of MCM-MCM interactions in diploid fission yeast cells. As with GINS-MCM interactions, MCM-MCM interactions also occur on chromatin in S-phase cells.\nBimolecular fluorescence complementation can be used in fission yeast to visualise interactions between two of the three components of the CMG complex, offering the prospect that this technique could in the future be used to allow studies on replication protein dynamics in living S. pombe cells.","doi":"10.1186/1471-2121-10-12","authors":"Akman G, MacNeill SA","authors_abbrev":"Akman G et al.","pubmed_publication_date":"19 Feb 2009","pubmed_entrez_date":"2009-02-21","publication_year":"2009","canto_session_key":"6c38cddc05bafae9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-11-07 16:29:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-07 16:28:10","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.09","SPCC16A11.17"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-07"},{"uniquename":"PMID:21931816","title":"Global gene expression analysis of fission yeast mutants impaired in Ser-2 phosphorylation of the RNA pol II carboxy terminal domain.","citation":"PLoS One 2011;6(9):e24694","abstract":"In Schizosaccharomyces pombe the nuclear-localized Lsk1p-Lsc1p cyclin dependent kinase complex promotes Ser-2 phosphorylation of the heptad repeats found within the RNA pol II carboxy terminal domain (CTD). Here, we first provide evidence supporting the existence of a third previously uncharacterized Ser-2 CTD kinase subunit, Lsg1p. As expected for a component of the complex, Lsg1p localizes to the nucleus, promotes Ser-2 phosphorylation of the CTD, and physically interacts with both Lsk1p and Lsc1p in vivo. Interestingly, we also demonstrate that lsg1Δ mutants--just like lsk1Δ and lsc1Δ strains--are compromised in their ability to faithfully and reliably complete cytokinesis. Next, to address whether kinase mediated alterations in CTD phosphorylation might selectively alter the expression of genes with roles in cytokinesis and/or the cytoskeleton, global gene expression profiles were analyzed. Mutants impaired in Ser-2 phosphorylation display little change with respect to the level of transcription of most genes. However, genes affecting cytokinesis--including the actin interacting protein gene, aip1--as well as genes with roles in meiosis, are included in a small subset that are differentially regulated. Significantly, genetic analysis of lsk1Δ aip1Δ double mutants is consistent with Lsk1p and Aip1p acting in a linear pathway with respect to the regulation of cytokinesis.","doi":"10.1371/journal.pone.0024694","authors":"Saberianfar R, Cunningham-Dunlop S, Karagiannis J","authors_abbrev":"Saberianfar R et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-09-21","publication_year":"2011","canto_session_key":"238851c4baaed103","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-08-16 15:54:56","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-21 17:23:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPBC649.05","SPAC2F3.15","SPAC9G1.05","SPAC3G9.01","SPCC4B3.08","SPAC1782.09c","SPAC6F6.08c"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2014-11-21"},{"uniquename":"PMID:14561399","title":"Centromere silencing and function in fission yeast is governed by the amino terminus of histone H3.","citation":"Curr Biol 2003 Oct 14;13(20):1748-57","abstract":"Centromeric domains often consist of repetitive elements that are assembled in specialized chromatin, characterized by hypoacetylation of histones H3 and H4 and methylation of lysine 9 of histone H3 (K9-MeH3). Perturbation of this underacetylated state by transient treatment with histone deacetylase inhibitors leads to defective centromere function, correlating with delocalization of the heterochromatin protein Swi6/HP1. Likewise, deletion of the K9-MeH3 methyltransferase Clr4/Suvar39 causes defective chromosome segregation. Here, we create fission yeast strains retaining one histone H3 and H4 gene; the creation of these strains allows mutation of specific N-terminal tail residues and their role in centromeric silencing and chromosome stability to be investigated.\nReduction of H3/H4 gene dosage to one-third does not affect cell viability or heterochromatin formation. Mutation of lysines 9 or 14 or serine 10 within the amino terminus of histone H3 impairs centromere function, leading to defective chromosome segregation and Swi6 delocalization. Surprisingly, silent centromeric chromatin does not require the conserved lysine 8 and 16 residues of histone H4.\nTo date, mutation of conserved N-terminal residues in endogenous histone genes has only been performed in budding yeast, which lacks the Clr4/Suvar39 histone methyltransferase and Swi6/HP1. We demonstrate the importance of conserved residues within the histone H3 N terminus for the maintenance of centromeric heterochromatin in fission yeast. In sharp contrast, mutation of two conserved lysines within the histone H4 tail has no impact on the integrity of centromeric heterochromatin. Our data highlight the striking divergence between the histone tail requirements for the fission yeast and budding yeast silencing pathways.","authors":"Mellone BG, Ball L, Suka N, Grunstein MR, Partridge JF, Allshire RC","authors_abbrev":"Mellone BG et al.","pubmed_publication_date":"14 Oct 2003","pubmed_entrez_date":"2003-10-17","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC1834.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10409743","title":"A fission yeast gene, him1(+)/dfp1(+), encoding a regulatory subunit for Hsk1 kinase, plays essential roles in S-phase initiation as well as in S-phase checkpoint control and recovery from DNA damage.","citation":"Mol Cell Biol 1999 Aug;19(8):5535-47","abstract":"Saccharomyces cerevisiae CDC7 encodes a serine/threonine kinase required for G(1)/S transition, and its related kinases are present in fission yeast as well as in higher eukaryotes, including humans. Kinase activity of Cdc7 protein depends on the regulatory subunit, Dbf4, which also interacts with replication origins. We have identified him1(+) from two-hybrid screening with Hsk1, a fission yeast homologue of Cdc7 kinase, and showed that it encodes a regulatory subunit of Hsk1. Him1, identical to Dfp1, previously identified as an associated molecule of Hsk1, binds to Hsk1 and stimulates its kinase activity, which phosphorylates both catalytic and regulatory subunits as well as recombinant MCM2 protein in vitro. him1(+) is essential for DNA replication in fission yeast cells, and its transcription is cell cycle regulated, increasing at middle M to late G(1). The protein level is low at START in G(1), increases at the G(1)/S boundary, and is maintained at a high level throughout S phase. Him1 protein is hyperphosphorylated at G(1)/S through S during the cell cycle as well as in response to early S-phase arrest induced by nucleotide deprivation. Deletion of one of the motifs conserved in regulatory subunits for Cdc7-related kinases as well as alanine substitution of three serine and threonine residues present in the same motif resulted in a defect in checkpoint regulation normally induced by hydroxyurea treatment. The alanine mutant also showed growth retardation after UV irradiation and the addition of methylmethane sulfonate. In keeping with this result, a database search indicates that him1(+) is identical to rad35(+). Our results reveal a novel function of the Cdc7/Dbf4-related kinase complex in S-phase checkpoint control as well as in growth recovery from DNA damage in addition to its predicted essential function in S-phase initiation.","authors":"Takeda T, Ogino K, Matsui E, Cho MK, Kumagai H, Miyake T, Arai K, Masai H","authors_abbrev":"Takeda T et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-07-20","publication_year":"1999","canto_session_key":"982304b134332abd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-10 14:43:28","canto_approved_date":"2022-01-04 09:56:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-15 18:29:50","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":27,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC550.13","SPCC1259.13","SPBC776.12c","SPBC4.04c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2015-06-10"},{"uniquename":"PMID:28867658","title":"Identification and characterization of a potent and biologically-active PDE4/7 inhibitor via fission yeast-based assays.","citation":"Cell Signal 2017 Dec;40:73-80","abstract":"We previously constructed a collection of fission yeast strains that express various mammalian cyclic nucleotide phosphodiesterases (PDEs) and developed a cell-based high throughput screen (HTS) for small molecule PDE inhibitors. Here we describe a compound, BC54, that is a selective inhibitor of enzymes from the cAMP-specific PDE4 and PDE7 families. Consistent with the biological effect of other PDE4 and PDE7 inhibitors, BC54 displays potent anti-inflammatory properties and is superior to a combination of rolipram (a PDE4 inhibitor) and BRL50481 (a PDE7A inhibitor) for inducing apoptosis in chronic lymphocytic leukemia (CLL) cells. We further exploited PKA-regulated growth phenotypes in fission yeast to isolate two mutant alleles of the human PDE4B2 gene that encode enzymes possessing single amino acid changes that confer partial resistance to BC54. We confirm this resistance to both BC54 and rolipram via yeast-based assays and, for PDE4B2 T407A , in vitro enzyme assays. Thus, we are able to use this system for both chemical screens to identify biologically-active PDE inhibitors and molecular genetic studies to characterize the interaction of these molecules with their target enzymes. Based on its potency, selectivity, and effectiveness in cell culture, BC54 should be a useful tool to study biological processes regulated by PDE4 and PDE7 enzymes.","doi":"10.1016/j.cellsig.2017.08.011","authors":"de Medeiros AS, Wyman AR, Alaamery MA, Allain C, Ivey FD, Wang L, Le H, Morken JP, Habara A, Le C, Cui S, Lerner A, Hoffman CS","authors_abbrev":"de Medeiros AS et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-09-05","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-09-06 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31597679","title":"Phosphoregulation of tropomyosin is crucial for actin cable turnover and division site placement.","citation":"J Cell Biol 2019 Nov 04;218(11):3548-3559","abstract":"Tropomyosin is a coiled-coil actin binding protein key to the stability of actin filaments. In muscle cells, tropomyosin is subject to calcium regulation, but its regulation in nonmuscle cells is not understood. Here, we provide evidence that the fission yeast tropomyosin, Cdc8, is regulated by phosphorylation of a serine residue. Failure of phosphorylation leads to an increased number and stability of actin cables and causes misplacement of the division site in certain genetic backgrounds. Phosphorylation of Cdc8 weakens its interaction with actin filaments. Furthermore, we show through in vitro reconstitution that phosphorylation-mediated release of Cdc8 from actin filaments facilitates access of the actin-severing protein Adf1 and subsequent filament disassembly. These studies establish that phosphorylation may be a key mode of regulation of nonmuscle tropomyosins, which in fission yeast controls actin filament stability and division site placement.","doi":"10.1083/jcb.201809089","authors":"Palani S, Köster DV, Hatano T, Kamnev A, Kanamaru T, Brooker HR, Hernandez-Fernaud JR, Jones AME, Millar JBA, Mulvihill DP, Balasubramanian MK","authors_abbrev":"Palani S et al.","pubmed_publication_date":"04 Nov 2019","pubmed_entrez_date":"2019-10-11","publication_year":"2019","canto_session_key":"cc4e9d3426a0ea9d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-10-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24680781","title":"Identification of Tf1 integration events in S. pombe under nonselective conditions.","citation":"Gene 2014 Jun 01;542(2):221-31","abstract":"Integration of retroviral elements into the host genome is a phenomena observed among many classes of retroviruses. Much information concerning the integration of retroviral elements has been documented based on in vitro analysis or expression of selectable markers. To identify possible Tf1 integration events within silent regions of the Schizosaccharomyces pombe genome, we focused on performing an in vivo genome-wide analysis of Tf1 integration events from the nonselective phase of the retrotransposition assay. We analyzed 1000 individual colonies streaked from four independent Tf1 transposed patches under nonselection conditions. Our analysis detected a population of G418(S)/neo(+) Tf1 integration events that would have been overlooked during the selective phase of the assay. Further RNA analysis from the G418(S)/neo(+) clones revealed 50% of clones expressing the neo selectable marker. Our data reveals Tf1's ability to insert within silent regions of S. pombe's genome.","doi":"10.1016/j.gene.2014.03.030","authors":"Cherry KE, Hearn WE, Seshie OY, Singleton TL","authors_abbrev":"Cherry KE et al.","pubmed_publication_date":"01 Jun 2014","pubmed_entrez_date":"2014-04-01","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39333464","title":"Uridylation regulates mRNA decay directionality in fission yeast.","citation":"Nat Commun 2024 Sep 27;15(1):8359","abstract":"Cytoplasmic mRNA decay is effected by exonucleolytic degradation in either the 5' to 3' or 3' to 5' direction. Pervasive terminal uridylation is implicated in mRNA degradation, however, its functional relevance for bulk mRNA turnover remains poorly understood. In this study, we employ genome-wide 3'-RACE (gw3'-RACE) in the model system fission yeast to elucidate the role of uridylation in mRNA turnover. We observe widespread uridylation of shortened poly(A) tails, promoting efficient 5' to 3' mRNA decay and ensuring timely and controlled mRNA degradation. Inhibition of this uridylation process leads to excessive deadenylation and enhanced 3' to 5' mRNA decay accompanied by oligouridylation. Strikingly we found that uridylation of poly(A) tails and oligouridylation of non-polyadenylated substrates are catalysed by different terminal uridyltransferases Cid1 and Cid16 respectively. Our study sheds new light on the intricate regulatory mechanisms underlying bulk mRNA turnover, demonstrating the role of uridylation in modulating mRNA decay pathways.","doi":"10.1038/s41467-024-50824-w","authors":"Grochowski M, Lipińska-Zubrycka L, Townsend S, Golisz-Mocydlarz A, Zakrzewska-Płaczek M, Brzyżek G, Jurković B, Świeżewski S, Ralser M, Małecki M","authors_abbrev":"Grochowski M et al.","pubmed_publication_date":"27 Sep 2024","pubmed_entrez_date":"2024-09-27","publication_year":"2024","canto_session_key":"ff80aaf19b5e7f04","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Michal Malecki","canto_first_approved_date":"2024-12-06 12:35:49","canto_approved_date":"2024-12-24 13:05:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-06 11:06:14","canto_added_date":"2024-09-28 23:25:06","annotation_curators":[{"name":"Michal Malecki","community_curator":true,"annotation_count":5,"orcid":"0000-0002-1525-5036","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":36,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.09c","SPAC17H9.01","SPCC550.03c","SPBC3D6.08c","SPAC17A5.14","SPAC19D5.03","SPAC2C4.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2024-12-06"},{"uniquename":"EMBL:AU009021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11263963","title":"Rkp1/Cpc2, a fission yeast RACK1 homolog, is involved in actin cytoskeleton organization through protein kinase C, Pck2, signaling.","citation":"Biochem Biophys Res Commun 2001 Mar 23;282(1):10-5","abstract":"The Rkp1/Cpc2, a fission yeast RACK1 homolog, interacted with Pck2, one of the known PKC homologs, in vivo and in vitro. The rkp1-deletion mutants (Deltarkp1) are elongated and the pck2-deletion mutant (Deltapck2) showed abnormal morphology. The double-deletion mutant (Deltarkp1Deltapck2) showed more aberrant cell shapes and was sensitive to high salt concentration. Both Deltarkp1 and Deltapck2 cells were sensitive to latrunculin B (Lat B) which inhibits actin polymerization. The cells expressing the human RACK1 homolog complemented the latrunculin B sensitivity of Deltarkp1 indicating that human RACK1 is a functional homolog of Rkp1/Cpc2. We propose that Rkp1/Cpc2 may function as a receptor for Pck2 in the regulation of actin cytoskeleton organization during cell wall synthesis and morphogenesis of Schizosaccharomyces pombe.","authors":"Won M, Park SK, Hoe KL, Jang YJ, Chung KS, Kim DU, Kim HB, Yoo HS","authors_abbrev":"Won M et al.","pubmed_publication_date":"23 Mar 2001","pubmed_entrez_date":"2001-03-27","publication_year":"2001","canto_session_key":"66bd776c94a56c16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-23 09:20:06","canto_approved_date":"2025-12-09 18:48:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-16 10:26:27","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":19,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.04c","SPAC6B12.15"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-04-23"},{"uniquename":"InterPro:IPR005579","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1556.05c","HGNC:28359"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19217404","title":"Fission yeast Scm3: A CENP-A receptor required for integrity of subkinetochore chromatin.","citation":"Mol Cell 2009 Feb 13;33(3):299-311","abstract":"The mechanisms ensuring specific incorporation of CENP-A at centromeres are poorly understood. Mis16 and Mis18 are required for CENP-A localization at centromeres and form a complex that is conserved from fission yeast to human. Fission yeast sim1 mutants that alleviate kinetochore domain silencing are defective in Scm3(Sp), the ortholog of budding yeast Scm3(Sc). Scm3(Sp) depends on Mis16/18 for its centromere localization and like them is recruited to centromeres in late anaphase. Importantly, Scm3(Sp) coaffinity purifies with CENP-A(Cnp1) and associates with CENP-A(Cnp1) in vitro, yet localizes independently of intact CENP-A(Cnp1) chromatin and is differentially released from chromatin. While Scm3(Sc) has been proposed to form a unique hexameric nucleosome with CENP-A(Cse4) and histone H4 at budding yeast point centromeres, we favor a model in which Scm3(Sp) acts as a CENP-A(Cnp1) receptor/assembly factor, cooperating with Mis16 and Mis18 to receive CENP-A(Cnp1) from the Sim3 escort and mediate assembly of CENP-A(Cnp1) into subkinetochore chromatin.","doi":"10.1016/j.molcel.2009.01.019","authors":"Pidoux AL, Choi ES, Abbott JK, Liu X, Kagansky A, Castillo AG, Hamilton GL, Richardson W, Rappsilber J, He X, Allshire RC","authors_abbrev":"Pidoux AL et al.","pubmed_publication_date":"13 Feb 2009","pubmed_entrez_date":"2009-02-17","publication_year":"2009","canto_session_key":"b7b22ba04350037e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-02-01 21:35:13","canto_approved_date":"2026-03-23 14:38:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-01 16:35:57","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":35,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18E5.03c","SPAPB1A10.02","SPBC1105.17","SPCC970.12","SPCC1672.10","SPAC1687.20c","SPBC577.15c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2019-02-01"},{"uniquename":"PMID:11929209","title":"The DNA damage response in filamentous fungi.","citation":"Fungal Genet Biol 2002 Apr;35(3):183-95","abstract":"The mechanisms used by fungal cells to repair DNA damage have been subjects of intensive investigation for almost 50 years. As a result, the model yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae have led the way in yielding critical insights into the nature of the DNA damage response. At the same time, largely through the efforts of Etta Kafer, Hirokazu Inoue, and colleagues, a substantial collection of Aspergillus nidulans and Neurospora crassa DNA repair mutants has been identified and characterized in detail. As the analysis of these mutants continues and increasing amounts of annotated genome sequence become available, it is becoming readily apparent that the DNA damage response of filamentous fungi possesses several features that distinguish it from the model yeasts. These features are emphasized in this review, which describes the genes, regulatory networks, and processes that compose the fungal DNA damage response. Further characterization of this response will likely yield general insights that are applicable to animals and plants. Moreover, it may also become evident that the DNA damage response can be manipulated to control fungal growth.","authors":"Goldman GH, McGuire SL, Harris SD","authors_abbrev":"Goldman GH et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-04","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009197","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16921581","title":"Recombineering reagents for improved inducible expression and selection marker re-use in Schizosaccharomyces pombe.","citation":"Yeast 2006 Aug;23(11):813-23","abstract":"The fission yeast Schizosaccharomyces pombe is an excellent model organism for cell biology. However, its genetic toolbox is less developed than that of Saccharomyces cerevisiae. In the first part of this study we describe an improved inducible expression vector based on tetracycline regulation of the CaMV35S promoter, which is also capable of chromosomal integration and therefore works in minimal and in rich media. We found that anhydrotetracycline is a superior ligand for induction. Maximum expression levels were observed after 12 h in minimal media (EMM) and after 9 h in rich media (YES), which is faster than the nmt1 promoter system. The system was combined with a convenient recombineering-based subcloning strategy for ease of cloning. In the second part we present four template plasmids, pSVEM-bsd, pSVEM-nat, pSVEM-kan and pSVEM-hph, which harbour four recyclable disruption cassettes based on the Cre recombinase lox71/66 strategy for use in PCR targeting methods. Cre-mediated excision leaves a non-functional mutant lox site in the genome, allowing the reiterative usage of these cassettes for multiple targetings. These cassettes are also configured with dual eukaryotic/prokaryotic promoters so that they can be used for recombineering in E. coli. Amongst other purposes, this permits the rapid and convenient creation of targeting constructs with much longer homology arms for difficult and complex targetings in the Sz. pombe genome.","authors":"Erler A, Maresca M, Fu J, Stewart AF","authors_abbrev":"Erler A et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-22","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33427950","title":"Checkpoint functions of RecQ helicases at perturbed DNA replication fork.","citation":"Curr Genet 2021 Jun;67(3):369-382","abstract":"DNA replication checkpoint is a cell signaling pathway that is activated in response to perturbed replication. Although it is crucial for maintaining genomic integrity and cell survival, the exact mechanism of the checkpoint signaling remains to be understood. Emerging evidence has shown that RecQ helicases, a large family of helicases that are conserved from bacteria to yeasts and humans, contribute to the replication checkpoint as sensors, adaptors, or regulation targets. Here, we highlight the multiple functions of RecQ helicases in the replication checkpoint in four model organisms and present additional evidence that fission yeast RecQ helicase Rqh1 may participate in the replication checkpoint as a sensor.","doi":"10.1007/s00294-020-01147-y","authors":"Ahamad N, Khan S, Mahdi ATA, Xu YJ","authors_abbrev":"Ahamad N et al.","pubmed_publication_date":"Jun 2021","pubmed_entrez_date":"2021-01-11","publication_year":"2021","canto_session_key":"bb0b2618db1e0e56","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-01-13 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC1259.13","SPBC216.05","SPAC2G11.12"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"EMBL:Z32838","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33320707","title":"Fission yeast cell cycle mutants and the logic of eukaryotic cell cycle control.","citation":"Mol Biol Cell 2020 Dec 15;31(26):2871-2873","abstract":"Cell cycle mutants in the budding and fission yeasts have played critical roles in working out how the eukaryotic cell cycle operates and is controlled. The starting point was Lee Hartwell's 1970s landmark papers describing the first cell division cycle (CDC) mutants in budding yeast. These mutants were blocked at different cell cycle stages and so were unable to complete the cell cycle, thus defining genes necessary for successful cell division. Inspired by Hartwell's work, I isolated CDC mutants in the very distantly related fission yeast. This started a program of searches for mutants in fission yeast that revealed a range of phenotypes informative about eukaryotic cell cycle control. These included mutants defining genes that were rate-limiting for the onset of mitosis and of the S-phase, that were responsible for there being only one S-phase in each cell cycle, and that ensured that mitosis only took place when S-phase was properly completed. This is a brief account of the discovery of these mutants and how they led to the identification of cyclin-dependent kinases as core to these cell cycle controls.","doi":"10.1091/mbc.E20-10-0623","authors":"Nurse P","authors_abbrev":"Nurse P","pubmed_publication_date":"15 Dec 2020","pubmed_entrez_date":"2020-12-15","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-12-17 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12456722","title":"Mob2p interacts with the protein kinase Orb6p to promote coordination of cell polarity with cell cycle progression.","citation":"J Cell Sci 2003 Jan 01;116(Pt 1):125-35","abstract":"The molecular mechanisms that temporally and spatially coordinate cell morphogenesis with the cell cycle remain poorly understood. Here we describe the characterization of fission yeast Mob2p, a novel protein required for regulating cell polarity and cell cycle control. Deletion of mob2 is lethal and causes cells to become spherical, with depolarized actin and microtubule cytoskeletons. A decrease in Mob2p protein level results in a defect in the activation of bipolar growth. This phenotype is identical to that of mutants defective in the orb6 protein kinase gene, and we find that Mob2p physically interacts with Orb6p. In addition, overexpression of Mob2p, like that of Orb6p, results in a delay in the onset of mitosis. Mob2p localizes to the cell periphery and cytoplasm throughout the cell cycle and to the division site during late anaphase and telophase. Mob2p is unable to localize to the cell middle in mutants defective in actomyosin ring and septum formation. Our results suggest that Mob2p, along with Orb6p, is required for coordinating polarized cell growth during interphase with the onset of mitosis.","authors":"Hou MC, Wiley DJ, Verde F, McCollum D","authors_abbrev":"Hou MC et al.","pubmed_publication_date":"01 Jan 2003","pubmed_entrez_date":"2002-11-29","publication_year":"2003","canto_session_key":"e254a152e54d321b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-17 14:53:16","canto_approved_date":"2020-03-15 15:08:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-17 14:53:07","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPCC970.04c","SPAC821.12","SPAC24B11.11c","SPAC4A8.15c","SPBC21.06c","SPCC18B5.03"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-08-17"},{"uniquename":"PMID:24806966","title":"The extent of error-prone replication restart by homologous recombination is controlled by Exo1 and checkpoint proteins.","citation":"J Cell Sci 2014 Jul 01;127(Pt 13):2983-94","abstract":"Genetic instability, a hallmark of cancer, can occur when the replication machinery encounters a barrier. The intra-S-phase checkpoint maintains stalled replication forks in a replication-competent configuration by phosphorylating replisome components and DNA repair proteins to prevent forks from catastrophically collapsing. Here, we report a novel function of the core Schizosaccharomyces pombe checkpoint sensor kinase, Rad3 (an ATR orthologue), that is independent of Chk1 and Cds1 (a CHK2 orthologue); Rad3(ATR) regulates the association of recombination factors with collapsed forks, thus limiting their genetic instability. We further reveal antagonistic roles for Rad3(ATR) and the 9-1-1 clamp - Rad3(ATR) restrains MRN- and Exo1-dependent resection, whereas the 9-1-1 complex promotes Exo1 activity. Interestingly, the MRN complex, but not its nuclease activity, promotes resection and the subsequent association of recombination factors at collapsed forks. The biological significance of this regulation is revealed by the observation that Rad3(ATR) prevents Exo1-dependent genome instability upstream of a collapsed fork without affecting the efficiency of recombination-mediated replication restart. We propose that the interplay between Rad3(ATR) and the 9-1-1 clamp functions to fine-tune the balance between the need for the recovery of replication through recombination and the risk of increased genome instability.","doi":"10.1242/jcs.152678","authors":"Tsang E, Miyabe I, Iraqui I, Zheng J, Lambert SA, Carr AM","authors_abbrev":"Tsang E et al.","pubmed_publication_date":"01 Jul 2014","pubmed_entrez_date":"2014-05-09","publication_year":"2014","canto_session_key":"7868e50c2d161b23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tony Carr","canto_first_approved_date":"2015-01-08 10:27:39","canto_approved_date":"2020-06-29 15:26:57","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-01-06 16:55:13","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Tony Carr","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPAC13C5.07","SPAC14C4.13","SPBC216.05","SPCC1259.13","SPBC29A10.05","SPAC664.07c","SPCC18B5.11c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-01-08"},{"uniquename":"EMBL:AU007498","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18061564","title":"Stabilization of overlapping microtubules by fission yeast CLASP.","citation":"Dev Cell 2007 Dec;13(6):812-27","abstract":"Many microtubule (MT) structures contain dynamic MTs that are bundled and stabilized in overlapping arrays. CLASPs are conserved MT-binding proteins implicated in the regulation of MT plus ends. Here, we show that the Schizosaccharomyces pombe CLASP, cls1p/peg1p, mediates the stabilization of overlapping MTs within the mitotic spindle and interphase bundles. cls1p localizes to these regions but not to interphase MT plus ends. Inactivation of cls1p leads to the rapid depolymerization of spindle midzone MTs. cls1p also stabilizes a subset of MTs within interphase bundles. cls1p prevents disassembly of the entire microtubule, while still allowing for plus-end growth. It has no measurable effects on MT nucleation, polymerization, catastrophe, or bundling. A direct interaction with ase1p (PRC1/MAP65) targets cls1p to regions of antiparallel MT overlap. These findings show how a MT-stabilizing factor attached to specific sites on MTs can help to generate MT structures that have both dynamic and stable components.","authors":"Bratman SV, Chang F","authors_abbrev":"Bratman SV et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-12-07","publication_year":"2007","canto_session_key":"4de0124e8c719689","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-23 10:59:14","canto_approved_date":"2024-07-02 13:09:43","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-11-14 18:52:56","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPCC417.07c","SPAC3G9.12"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-11-23"},{"uniquename":"PMID:10504305","title":"Schizosaccharomyces pombe protein kinase C homologues, pck1p and pck2p, are targets of rho1p and rho2p and differentially regulate cell integrity.","citation":"J Cell Sci 1999 Oct;112 ( Pt 20):3569-78","abstract":"Schizosaccharomyces pombe rho1(+) is required for maintenance of cell integrity and polarization of the actin cytoskeleton. However, no other effector besides the (1,3)beta-D-glucan synthase enzyme has been identified in S. pombe. We have further investigated if rho1(+ )signalling could be also mediated by the two protein kinase C homologues, pck1p and pck2p. We show in this study that both kinases interact with rho1p and rho2p only when bound to GTP, as most GTPase effectors do. Interestingly, the interaction was mapped in a different part of the proteins than in Saccharomyces cerevisiae Pkc1p. Thus, active rho1p binds to the amino-terminal region of the pcks where two HR1 motifs are located, and binding to the GTPase dramatically stabilizes the kinases. Detailed biochemical analysis suggests that pck2p is more important in the regulation of the enzyme (1-3)beta-D-glucan synthase. Thus, overexpression of pck2(+), but not pck1(+), caused a general increase in cell wall biosynthesis, mainly in beta-glucan, and (1-3)beta-D-glucan synthase activity was considerably augmented. When this activity was separated into soluble and membrane fractions and reconstituted, the increase caused by pck2(+) overexpression was exclusively detected in the membrane component. We also show that both protein kinase C homologues are required for the maintenance of cell integrity. pck1delta and pck2delta strains present a number of defects related to the cell wall, indicating that this structure might be co-ordinately regulated by both kinases. In addition, pck2p, but not pck1p, seems to be involved in keeping cell polarity. Genetic evidence indicates that both pck1(+) and pck2(+) interact with cps1(+) and gls2(+), two genes similar to S. cerevisiae FKS1 and FKS2 that encode membrane subunits of the (1-3)beta-D-glucan synthase. pck1(+ )also showed a genetic interaction with ras1(+) and ral1(+) suggesting the existence of a functional link between both signalling pathways.","authors":"Arellano M, Valdivieso MH, Calonge TM, Coll PM, Duran A, Perez P","authors_abbrev":"Arellano M et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-10-03","publication_year":"1999","canto_session_key":"e0e85df0e0e16a77","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-07-31 15:10:12","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-05-17 11:06:04","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":54,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.14c","SPAC1F7.04","SPAC16.01","SPAC110.03","SPAC17H9.09c","SPBC19G7.05c","SPAC1002.03c","SPAC16E8.09","SPBC12D12.04c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2013-05-17"},{"uniquename":"PMID:16595622","title":"Rqh1 blocks recombination between sister chromatids during double strand break repair, independent of its helicase activity.","citation":"Proc Natl Acad Sci U S A 2006 Apr 11;103(15):5875-80","abstract":"Many questions remain about the process of DNA double strand break (DSB) repair by homologous recombination (HR), particularly concerning the exact function played by individual proteins and the details of specific steps in this process. Some recent studies have shown that RecQ DNA helicases have a function in HR. We studied the role of the RecQ helicase Rqh1 with HR proteins in the repair of a DSB created at a unique site within the Schizosaccharomyces pombe genome. We found that DSBs in rqh1(+) cells, are predominantly repaired by interchromosomal gene conversion, with HR between sister chromatids [sister-chromatid conversion (SCC)], occurring less frequently. In Deltarqh1 cells, repair by SCC is favored, and gene conversion rates slow significantly. When we limited the potential for SCC in Deltarqh1 cells by reducing the length of the G2 phase of the cell cycle, DSB repair continued to be predominated by SCC, whereas it was essentially eliminated in wild-type cells. These data indicate that Rqh1 acts to regulate DSB repair by blocking SCC. Interestingly, we found that this role for Rqh1 is independent of its helicase activity. In the course of these studies, we also found nonhomologous end joining to be largely faithful in S. pombe, contrary to current belief. These findings provide insight into the regulation of DSB repair by RecQ helicases.","authors":"Hope JC, Mense SM, Jalakas M, Mitsumoto J, Freyer GA","authors_abbrev":"Hope JC et al.","pubmed_publication_date":"11 Apr 2006","pubmed_entrez_date":"2006-04-06","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21984208","title":"Crystal structures of aprataxin ortholog Hnt3 reveal the mechanism for reversal of 5'-adenylated DNA.","citation":"Nat Struct Mol Biol 2011 Oct 09;18(11):1297-9","abstract":"Aprataxin is a DNA deadenylase that resolves DNA 5'-AMP termini and reverses abortive DNA ligation. The crystal structures of Schizosaccharomyces pombe aprataxin Hnt3 in its apo form and in complex to dsDNA and dsDNA-AMP reveal how Hnt3 recognizes and processes 5'-adenylated DNA in a structure-specific manner. The bound DNA adopts a 5'-flap conformation that facilitates 5'-AMP access to the active site, where AMP cleavage occurs by a canonical catalytic mechanism.","doi":"10.1038/nsmb.2145","authors":"Gong Y, Zhu D, Ding J, Dou CN, Ren X, Gu L, Jiang T, Wang DC","authors_abbrev":"Gong Y et al.","pubmed_publication_date":"09 Oct 2011","pubmed_entrez_date":"2011-10-11","publication_year":"2011","canto_session_key":"604021fe9263133e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2012-12-06 13:41:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-06 13:41:39","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-06","pdb_entries":[{"pdb_id":"3spl","gene_chains":[{"gene_uniquename":"SPCC18.09c","chain":"A/B/C/D","position":"33-232"}],"title":"Crystal structure of aprataxin ortholog Hnt3 in complex with DNA and AMP","entry_authors":"Gong Y,Zhu D,Ding J,Dou C,Ren X,Jiang T,Wang D","entry_authors_abbrev":"Gong Y et al.","reference_uniquename":"PMID:21984208","experimental_method":"X-ray","resolution":"2.101"},{"pdb_id":"3spd","gene_chains":[{"gene_uniquename":"SPCC18.09c","chain":"A/B/C/D","position":"33-232"}],"title":"Crystal structure of aprataxin ortholog Hnt3 in complex with DNA","entry_authors":"Gong Y,Zhu D,Ding J,Dou C,Ren X,Jiang T,Wang D","entry_authors_abbrev":"Gong Y et al.","reference_uniquename":"PMID:21984208","experimental_method":"X-ray","resolution":"1.912"},{"pdb_id":"3sp4","gene_chains":[{"gene_uniquename":"SPCC18.09c","chain":"A/B","position":"33-232"}],"title":"Crystal structure of aprataxin ortholog Hnt3 from Schizosaccharomyces pombe","entry_authors":"Gong Y,Zhu D,Ding J,Dou C,Ren X,Jiang T,Wang D","entry_authors_abbrev":"Gong Y et al.","reference_uniquename":"PMID:21984208","experimental_method":"X-ray","resolution":"1.8"}]},{"uniquename":"PMID:10914027","title":"Exploiting the utility of yeast in the context of programmed cell death.","citation":"Methods Enzymol 2000;322:297-322","abstract":"Many researchers have explored the extent to which yeast can be used to dissect the mechanisms of programmed cell death in higher cells. Yeast has been used as a system to analyze protein-protein interactions and structure-function relationships, and as a cloning tool to identify novel higher eukaryote regulators of apoptosis. In addition, classic genetic strategies in yeast have been used to analyze the mechanisms of action of core pathway members. The purpose of this chapter is to describe the strategies pursued and act as a source for the technical details necessary to exploit the yeast Saccharomyces cerevisiae and Schizosaccharomyces pombe in the context of programmed cell death.","authors":"Torgler CN, Brown R, Meldrum E","authors_abbrev":"Torgler CN et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-07-29","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15827087","title":"End4/Sla2 is involved in establishment of a new growth zone in Schizosaccharomyces pombe.","citation":"J Cell Sci 2005 May 01;118(Pt 9):1843-50","abstract":"The rod-shaped Schizosaccharomyces pombe cell grows in a polarized fashion from opposing ends. Correct positioning of the growth zones is directed by the polarity marker Tea1 located at the cell ends where actin patches accumulate and cell growth takes place. We show that the S. pombe homologue of Saccharomyces cerevisiae SLA2, a protein involved in cortical actin organization and endocytosis, provides a link between the polarity marker and the growth machinery. In wild-type fission yeast cells, this homologue End4/Sla2 is enriched at cell ends during interphase and localizes to a medial ring at cell division, mirroring the actin localization pattern throughout the cell cycle. Proper localization relies on membrane trafficking and is independent of both the actin and microtubule cytoskeletons. End4/Sla2 is required for the establishment of new polarised growth zones, and deletion of its C-terminal talin-like domain prevents the establishment of a new growth zone after cell fission. We propose that End4/Sla2 acts downstream of the polarity marker Tea1 and is implicated in the recruitment of the actin cytoskeleton to bring about polarised cell growth.","authors":"Castagnetti S, Behrens R, Nurse P","authors_abbrev":"Castagnetti S et al.","pubmed_publication_date":"01 May 2005","pubmed_entrez_date":"2005-04-14","publication_year":"2005","canto_session_key":"eab9a81ad211e62f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-01-12 15:03:31","canto_approved_date":"2024-07-16 13:06:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-03 16:30:03","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":27,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPAC688.11","SPCC1223.06"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-01-12"},{"uniquename":"PMID:18355038","title":"Deciphering the mechanism of thermodynamic accommodation of telomeric oligonucleotide sequences by the Schizosaccharomyces pombe protection of telomeres 1 (Pot1pN) protein.","citation":"Biochemistry 2008 Apr 15;47(15):4345-4358","abstract":"Linear chromosomes terminate in specialized nucleoprotein structures called telomeres, which are required for genomic stability and cellular proliferation. Telomeres end in an unusual 3' single-strand overhang that requires a special capping mechanism to prevent inappropriate recognition by the DNA damage machinery. In Schizosaccharomyces pombe, this protective function is mediated by the Pot1 protein, which binds specifically and with high affinity to telomeric ssDNA. We have characterized the thermodynamics and accommodation of both cognate and noncognate telomeric single-stranded DNA (ssDNA) sequences by Pot1pN, an autonomous ssDNA-binding domain (residues 1-187) found in full-length S. pombe Pot1. Direct calorimetric measurements of cognate telomeric ssDNA binding to Pot1pN show favorable enthalpy, unfavorable entropy, and a negative heat-capacity change. Thermodynamic analysis of the binding of noncognate telomeric ssDNA to Pot1pN resulted in unexpected changes in free energy, enthalpy, and entropy. Chemical-shift perturbation and structural analysis of these bound noncognate sequences show that these thermodynamic changes result from the structural rearrangement of both Pot1pN and the bound oligonucleotide. These data suggest that the ssDNA-binding interface is highly dynamic and, in addition to the conformation observed in the crystal structure of the Pot1pN/d(GGTTAC) complex, capable of adopting alternative thermodynamically equivalent conformations.","doi":"10.1021/bi701778x","authors":"Croy JE, Fast JL, Grimm NE, Wuttke DS","authors_abbrev":"Croy JE et al.","pubmed_publication_date":"15 Apr 2008","pubmed_entrez_date":"2008-03-22","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25041276","title":"Mechanosensitive channels Msy1 and Msy2 are required for maintaining organelle integrity upon hypoosmotic shock in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2014 Sep;14(6):992-4","abstract":"The mechanosensitive channels, Mys1 and Msy2, in fission yeast are localized in the endoplasmic reticulum membrane and control cytoplasmic Ca(2+) levels in the hypoosmotic response. We here investigated changes in organellar structures with hypoosmotic shock using transmission electron microscopy. While msy1(-) and msy2(-) single mutant cells developed a number of swollen vacuoles following hypoosmotic shock, similar to wild-type cells, msy1(-) msy2(-) double mutant cells only had two abnormally large vacuoles and cracks between the inner and outer nuclear membranes. These results suggest that Msy1 and Msy2 may be involved in maintaining vacuole integrity and protecting the nuclear envelope upon hypoosmotic shock and also that these two channels are functionally complementary.","doi":"10.1111/1567-1364.12181","authors":"Nakayama Y, Hirata A, Iida H","authors_abbrev":"Nakayama Y et al.","pubmed_publication_date":"Sep 2014","pubmed_entrez_date":"2014-07-22","publication_year":"2014","canto_session_key":"9a3272bd6224c6c7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-07-23 00:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1183.11","SPAC2C4.17c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:19422421","title":"Interactions between Swi1-Swi3, Mrc1 and S phase kinase, Hsk1 may regulate cellular responses to stalled replication forks in fission yeast.","citation":"Genes Cells 2009 Jun;14(6):669-82","abstract":"The Swi1-Swi3 replication fork protection complex and Mrc1 protein are required for stabilization of stalled replication forks in fission yeast. Hsk1 kinase also plays roles in checkpoint responses elicited by arrested replication forks. We show that both Swi1 and Swi3, the abundance of which are interdependent, are required for chromatin association of Mrc1. Co-immunoprecipitation experiments show the interactions of Swi1-Swi3, Mrc1 and Hsk1. Mrc1 interacts with Swi3 and Hsk1 proteins through its central segment (378-879) containing a SQ/TQ cluster, and this segment is sufficient for checkpoint reaction. The SQ/TQ cluster segment (536-673) is essential but not sufficient for the interactions and for resistance to replication inhibitor hydroxyurea. Mrc1 protein level is increased in hsk1-89 cells due to apparent stabilization, and we have identified a potential phosphodegron sequence. These results suggest that interactions of the Swi1-Swi3 complex and Hsk1 kinase with Mrc1 may play a role in cellular responses to stalled replication forks in fission yeast.","doi":"10.1111/j.1365-2443.2009.01300.x","authors":"Shimmoto M, Matsumoto S, Odagiri Y, Noguchi E, Russell P, Masai H","authors_abbrev":"Shimmoto M et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-05-09","publication_year":"2009","canto_session_key":"21220c7b23915d21","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-05-14 13:00:08","canto_approved_date":"2022-11-26 09:48:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-14 13:00:02","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":41,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":72,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_19422421_phaf.tsv"}],"genes":["SPBC776.12c","SPAC694.06c","SPBC30D10.04","SPBC216.06c","SPCC550.13"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-05-14"},{"uniquename":"PMID:35300005","title":"Canavanine resistance mutation  can1-1  in  Schizosaccharomyces pombe  is a missense mutation in the ubiquitin ligase adaptor gene  any1 .","citation":"MicroPubl Biol 2022;2022","abstract":"In  Schizosaccharomyces pombe , the  can1-1  mutation confers resistance to the toxic arginine analog canavanine. This mutation has been assumed to disrupt a gene encoding an arginine transporter. In PomBase, the gene  SPBC18H10.16  is currently designated  can1 . Here, we sequenced the genomes of three  can1-1  strains. No mutations were found in  SPBC18H10.16 . Instead, these strains harbor an R175C mutation in the gene  any1  ( SPBC18H10.20c ).  any1  encodes an α-arrestin that acts as a ubiquitin ligase adaptor to downregulate plasma membrane amino acid transporters. Our findings indicate that  can1-1  is not a loss-of-function mutation in an amino acid transporter gene, but a possible gain-of-function mutation in a gene encoding a negative regulator of amino acid transporters.","doi":"10.17912/micropub.biology.000538","authors":"Yang YS, Ning SK, Lyu XH, Suo F, Jia GS, Li W, Du LL","authors_abbrev":"Yang YS et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-03-18","publication_year":"2022","canto_session_key":"21fef5a562927ba9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li-Lin Du","canto_first_approved_date":"2022-03-25 09:01:37","canto_approved_date":"2022-03-31 12:34:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-24 00:15:22","canto_added_date":"2022-03-20 01:15:03","annotation_curators":[{"name":"Li-Lin Du","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18H10.20c","SPBC18H10.16"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2022-03-25"},{"uniquename":"PMID:7683759","title":"Analysis of DNA repair pathways of Schizosaccharomyces pombe by means of swi-rad double mutants.","citation":"Mutat Res 1993 Jun;294(1):59-67","abstract":"In Schizosaccharomyces pombe 11 different switching genes (swi1 to swi10 and rad22) are known which are involved in mating-type (MT) switching. Mutations in swi5, swi9, swi10 and rad22 also cause an increased radiation sensitivity. We tested whether the survival of these mutants after UV irradiation is influenced by caffeine. We included rad1 and rad13 mutants in our experiments which do not affect MT switching. Several double and triple mutants were constructed. We were able to assign the switching genes to different repair pathways: swi9 and swi10 are involved in excision repair, rad22 has a function in recombination repair, while swi5 appears to be involved in a hitherto unknown pathway. This 'swi5 pathway' is stimulated (!) by caffeine. Previously it was found that the swi5 mutation also reduces meiotic recombination. As to rad genes, we found a few inconsistencies with previous reports in the literature.","authors":"Schlake C, Ostermann K, Schmidt H, Gutz H","authors_abbrev":"Schlake C et al.","pubmed_publication_date":"Jun 1993","pubmed_entrez_date":"1993-06-01","publication_year":"1993","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36358328","title":"Crystal Structure of  Schizosaccharomyces pombe  Rho1 Reveals Its Evolutionary Relationship with Other Rho GTPases.","citation":"Biology (Basel) 2022 Nov 07;11(11)","abstract":"The Rho protein, a homolog of Ras, is a member of the Ras superfamily of small GTPases. Rho family proteins are involved in cytoskeletal organization, cell mobility, and polarity, and are implicated in cancer morphogenesis. Although Rho homologs from higher-order mammalian organisms are well studied, there are few studies examining Rho proteins in lower-level single-celled organisms. Here, we report on the crystal structure of Rho1 from  Schizosaccharomyces pombe  ( Sp Rho1) in complex with GDP in the presence of Mg 2+  at a 2.78 Å resolution. The overall structure is similar to that of known Rho homologs, including human RhoA, human RhoC, and  Aspergillus fumigatus  Rho1 ( Af Rho1), with some exceptions. We observed subtle differences at the Switch I and II regions, in β2 and β3, and in the Rho insert domain and loop from Phe107 to Pro112. Our analysis suggests that  Sp Rho is evolutionarily closer to  Hs RhoC than  Hs RhoA, as previously believed.","doi":"10.3390/biology11111627","authors":"Huang Q, Xie J, Seetharaman J","authors_abbrev":"Huang Q et al.","pubmed_publication_date":"07 Nov 2022","pubmed_entrez_date":"2022-11-11","publication_year":"2022","canto_session_key":"e4dc3975c8064de7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-11 17:38:02","canto_approved_date":"2023-03-11 17:38:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-11 17:37:55","canto_added_date":"2022-11-16 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-03-11","pdb_entries":[{"pdb_id":"8etd","gene_chains":[{"gene_uniquename":"SPAC1F7.04","chain":"A/B","position":"1-202"}],"title":"Crystal Structure of Schizosaccharomyces pombe Rho1","entry_authors":"Huang Q,Xie J,Seetharaman J","entry_authors_abbrev":"Huang Q et al.","reference_uniquename":"PMID:36358328","experimental_method":"X-ray","resolution":"2.78"}]},{"uniquename":"PMID:21386895","title":"Cell-cycle analysis of fission yeast cells by flow cytometry.","citation":"PLoS One 2011 Feb 28;6(2):e17175","abstract":"The cell cycle of the fission yeast, Schizosaccharomyces pombe, does not easily lend itself to analysis by flow cytometry, mainly because cells in G(1) and G(2) phase contain the same amount of DNA. This occurs because fission yeast cells under standard growth conditions do not complete cytokinesis until after G(1) phase. We have devised a flow cytometric method exploiting the fact that cells in G(1) phase contain two nuclei, whereas cells in G(2) are mononuclear. Measurements of the width as well as the total area of the DNA-associated fluorescence signal allows the discrimination between cells in G(1) and in G(2) phase and the cell-cycle progression of fission yeast can be followed in detail by flow cytometry. Furthermore, we show how this method can be used to monitor the timing of cell entry into anaphase. Fission yeast cells tend to form multimers, which represents another problem of flow cytometry-based cell-cycle analysis. Here we present a method employing light-scatter measurements to enable the exclusion of cell doublets, thereby further improving the analysis of fission yeast cells by flow cytometry.","doi":"10.1371/journal.pone.0017175","authors":"Knutsen JH, Rein ID, Rothe C, Stokke T, Grallert B, Boye E","authors_abbrev":"Knutsen JH et al.","pubmed_publication_date":"28 Feb 2011","pubmed_entrez_date":"2011-03-10","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11983163","title":"Only connect: linking meiotic DNA replication to chromosome dynamics.","citation":"Mol Cell 2002 Apr;9(4):703-11","abstract":"The process of meiosis reduces a diploid cell to four haploid gametes and is accompanied by extensive recombination. Thus, chromosome dynamics in meiosis are significantly different than in mitotic cells. This review analyzes unique features of meiotic DNA replication and describes how it affects subsequent recombination and chromosome segregation.","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-05-02","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1680238","title":"The Florey Lecture, 1990. How is the cell division cycle regulated?","citation":"Philos Trans R Soc Lond B Biol Sci 1991 Jun 29;332(1264):271-6","abstract":"It is argued in this lecture that in most eukaryotic cells onset of mitosis is coupled to attainment of a critical cell mass and to completion of the previous S-phase. In fission yeast these controls operate through a regulatory gene network that activates the p34cdc2 protein kinase at mitosis. This is brought about by dephosphorylation of a tyrosine residue located in the ATP binding site of the kinase. The p34cdc2 protein kinase is also important for regulating the onset of mitosis in vertebrate cells suggesting that there is a universal control regulating mitosis in all eukaryotic cells.","authors":"Nurse P","authors_abbrev":"Nurse P","pubmed_publication_date":"29 Jun 1991","pubmed_entrez_date":"1991-06-29","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1291242","title":"Identification and characterization of a complex chromosomal replication origin in Schizosaccharomyces pombe.","citation":"Chromosoma 1992;102(1 Suppl):S7-16","abstract":"In the budding yeast, S. cerevisiae, two-dimensional (2D) gel electrophoresis techniques permit mapping of DNA replication origins to short stretches of DNA (+/- 300 bp). In contrast, in mammalian cells and Drosophila, 2D gel techniques do not permit precise origin localization; the results have been interpreted to suggest that replication initiates in broad zones (several kbp or more). However, alternative techniques (replication timing, nascent strand polarity analysis, nascent strand size analysis) suggest that mammalian origins can be mapped to short DNA stretches, just like S. cerevisiae origins. Because the fission yeast, Schizosaccharomyces pombe, resembles higher organisms in several ways to a greater extent than does S. cerevisiae, we thought that S. pombe replication origins might prove to resemble--and thus be helpful models for--animal cell origins. An attempt to test this possibility using 2D gel techniques resulted in identification of a replication origin near the ura4 gene on chromosome III of S. pombe. The 2D gel patterns produced by this S. pombe origin indeed resemble the patterns produced by animal cell origins and show that the S. pombe origin cannot be precisely located. The data suggest an initiation zone of 3-5 kbp. Some aspects of the 2D gel patterns detected at the S. pombe origin cannot be explained by the rationale of initiation in broad zones, suggesting that future biochemical and genetic studies of this complex origin are likely to provide information useful in helping to understand the apparent conflict between the 2D gel mapping techniques and other mapping techniques at animal cell origins.","authors":"Zhu J, Brun C, Kurooka H, Yanagida M, Huberman JA","authors_abbrev":"Zhu J et al.","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25492408","title":"Meiotic nuclear movements in fission yeast are regulated by the transcription factor Mei4 downstream of a Cds1-dependent replication checkpoint pathway.","citation":"Genes Cells 2015 Mar;20(3):160-72","abstract":"In meiosis, the fission yeast nucleus displays an elongated morphology, moving back and forth within the cell; these nuclear movements continue for approximately 2 h before meiotic nuclear divisions. Meiotic DNA replication occurs in an early phase of the nuclear movements and is followed by meiotic prophase. Here we report that in mutants deficient in meiotic DNA replication, the duration of nuclear movements is strikingly prolonged to four to 5 h. We found that this prolongation was caused by the Cds1-dependent replication checkpoint, which represses expression of the mei4(+) gene encoding a meiosis-specific transcription factor. In the absence of Mei4, nuclear movements persisted for more than 8 h. In contrast, overproduction of Mei4 accelerated termination of nuclear movements to approximately 30 min. These results show that Mei4 is involved in the termination of nuclear movements and that Mei4-mediated regulatory pathways link a DNA replication checkpoint to the termination of nuclear movements.","doi":"10.1111/gtc.12207","authors":"Ruan K, Yamamoto TG, Asakawa H, Chikashige Y, Masukata H, Haraguchi T, Hiraoka Y","authors_abbrev":"Ruan K et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2014-12-11","publication_year":"2015","canto_session_key":"915dd27f11d0b65d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasushi Hiraoka","canto_first_approved_date":"2017-11-02 19:31:39","canto_approved_date":"2024-04-02 17:04:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-09 12:15:57","canto_added_date":"2014-12-12 01:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Yasushi Hiraoka","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC1F7.05","SPAC17H9.10c","SPBC660.14","SPCC18B5.03","SPBC32H8.11","SPBC215.03c","SPAC24H6.05"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-11-02"},{"uniquename":"PMID:19518131","title":"Nonadditivity in the recognition of single-stranded DNA by the schizosaccharomyces pombe protection of telomeres 1 DNA-binding domain, Pot1-DBD.","citation":"Biochemistry 2009 Jul 28;48(29):6864-75","abstract":"The Schizosaccharomyces pombe protection of telomeres 1 (SpPot1) protein recognizes the 3' single-stranded ends of telomeres and provides essential protective and regulatory functions. The ssDNA-binding activity of SpPot1 is conferred by its ssDNA-binding domain, Pot1-DBD (residues 1-389), which can be further separated into two distinct domains, Pot1pN (residues 1-187) and Pot1pC (residues 188-389). Here we show that Pot1pC, like Pot1pN, can function independently of Pot1-DBD and binds specifically to a minimal nonameric oligonucleotide, d(GGTTACGGT), with a K(D) of 400 +/- 70 nM (specifically recognized nucleotides in bold). NMR chemical shift perturbation analysis indicates that the overall structures of the isolated Pot1pN and Pot1pC domains remain intact in Pot1-DBD. Furthermore, alanine scanning reveals modest differences in the ssDNA-binding contacts provided by isolated Pot1pN and within Pot1-DBD. Although the global character of both Pot1pN and Pot1pC is maintained in Pot1-DBD, chemical shift perturbation analysis highlights localized structural differences within the G1/G2 and T3/T4 binding pockets of Pot1pN in Pot1-DBD, which correlate with its distinct ssDNA-binding activity. Furthermore, we find evidence for a putative interdomain interface on Pot1pN that mediates interactions with Pot1pC that ultimately result in the altered ssDNA-binding activity of Pot1-DBD. Together, these data provide insight into the mechanisms underlying the activity and regulation of SpPot1 at the telomere.","doi":"10.1021/bi900307x","authors":"Croy JE, Altschuler SE, Grimm NE, Wuttke DS","authors_abbrev":"Croy JE et al.","pubmed_publication_date":"28 Jul 2009","pubmed_entrez_date":"2009-06-13","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:V01360","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPATRNAMET.01","SPATRNASER.01"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:20609363","title":"Pac1 endonuclease and Dhp1p 5'-->3' exonuclease are required for U3 snoRNA termination in Schizosaccharomyces pombe.","citation":"FEBS Lett 2010 Aug 04;584(15):3436-41","abstract":"Maturation of some snoRNAs is dependent on RNase III-like endonuclease-mediated transcript cleavage, which serves as an entry for the nuclear exosome complex that trims the transcript at the 3'-end. Sequence deletions suggest this cleavage in the U3 snoRNA transcripts of Schizosaccharomyces pombe can induce transcript termination. Using mutational analyses, we demonstrate that the degree of cleavage correlates closely with both RNA maturation and transcript termination. We also show that the RNase III-like endonuclease, Pac1, and the nuclear 5'-exonuclease, Dhp1p, are essential for RNA production and transcript termination, supporting a \"reversed torpedoes\" model in which the endonuclease cut allows 5'- and 3'-exonuclease activities access to the transcript, leading simultaneously to transcript termination in one direction and RNA maturation in the other.","doi":"10.1016/j.febslet.2010.06.042","authors":"Nabavi S, Nazar RN","authors_abbrev":"Nabavi S et al.","pubmed_publication_date":"04 Aug 2010","pubmed_entrez_date":"2010-07-09","publication_year":"2010","canto_session_key":"793b59b0cfa3190c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-19 11:30:41","canto_approved_date":"2023-07-05 12:32:22","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-08-19 11:17:26","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.03","SPSNRNA.07","SPAC26A3.12c","SPBC119.11c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2014-08-19"},{"uniquename":"PMID:42291817","title":"Nanobody-based analysis of RhoGTPase stress response in  Schizosaccharomyces pombe : Role of  mtl 2.","citation":"Biotechnol Rep (Amst) 2026 Sep;51:e00963","abstract":" Schizosaccharomyces pombe  ( S.pombe ), commonly referred to as fission yeast, is a widely utilised model organism for studying cellular responses to stress. The stress response mechanisms are largely conserved, offering insights into similar processes in higher eukaryotes, including humans.We have developed an in vivo nanobody-library screening platform in Δ mtl 2 fission yeast subjected to lethal caspofungin stress, enabling the direct selection of nanobodies that improve survival. Through this method, we isolate a nanobody (Clone-C) that binds to and regulates the Rho1 GEF (Guanine nucleotide Exchange factor) Rgf1, enhancing cell survival and uncovering a hitherto unreported Mtl2-Rgf1-Rho1GTPase regulatory axis in the cell-wall stress response. This nanobody-based fluorescence-readout method offers a versatile tool for gene identification and antifungal target/ADC screening under certain stress conditions.","doi":"10.1016/j.btre.2026.e00963","authors":"Rasheed N, Ali X, Ali T, Muhammad F, Rasheed MA","authors_abbrev":"Rasheed N et al.","pubmed_publication_date":"Sep 2026","pubmed_entrez_date":"2026-06-15","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-15 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10504341","title":"The C-terminal domain of the Cdc2 inhibitory kinase Myt1 interacts with Cdc2 complexes and is required for inhibition of G(2)/M progression.","citation":"J Cell Sci 1999 Oct;112 ( Pt 19):3361-71","abstract":"Activation of Cdc2, is the universal event controlling the onset of mitosis. In higher eukaryotes, Cdc2 activity is in part regulated by inhibitory phosphorylation of Thr14 and Tyr15, catalyzed by Wee1 and Myt1, which prevents catastrophic premature entry into mitosis. In this study we defined the function of Myt1 by overexpression studies in both S. pombe and a human osteosarcoma cell line. Similar to Wee1, overexpression of human Myt1 prevented entry into mitosis in both cell types; however, Myt1 catalytic activity was not essential for the cell cycle delay observed with human cells. Myt1 expression was restricted to proliferating cells. Furthermore, we detected no major decline in Myt1 protein abundance prior to the entry into mitosis, which coincides with the loss of Myt1 activity. We localized mitotic phosphoepitopes, recognized by the monoclonal antibody MPM-2, to the C-terminal domain of Myt1. The mitotic peptidyl-prolyl isomerase, Pin1, was able to associate with this domain in a phosphorylation-dependent manner. Truncation of the C-terminal domain of Myt1 prevented its ability to induce G(2)/M phase arrest in overexpression studies in human cells and dramatically reduced its ability to phosphorylate Cdc2 in vitro. We demonstrate that the C-terminal domain of Myt1 was required for recruitment of Cdc2, and we infer that this domain lies in the cytoplasm because it can interact with and is phosphorylated by Cdc2. In conclusion, we propose that Myt1 can negatively regulate Cdc2/cyclin B1 and inhibit G(2)/M progression by two means, both of which require the C-terminal domain; first, Myt1 can bind and sequester Cdc2/cyclin B1 in the cytoplasm preventing entry into the nucleus, and, second, it can phosphorylate associated Cdc2/cyclin B1 at Thr14 and Tyr15 thus inhibiting its catalytic activity.","authors":"Wells NJ, Watanabe N, Tokusumi T, Jiang W, Verdecia MA, Hunter T","authors_abbrev":"Wells NJ et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-10-03","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF07989","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC417.07c","HGNC:15580","HGNC:18672"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22523368","title":"The monothiol glutaredoxin Grx4 exerts an iron-dependent inhibitory effect on Php4 function.","citation":"Eukaryot Cell 2012 Jun;11(6):806-19","abstract":"When iron is scarce, Schizosaccharomyces pombe cells repress transcription of several genes that encode iron-using proteins. Php4 mediates this transcriptional control by specifically interacting with the CCAAT-binding core complex that is composed of Php2, Php3, and Php5. In contrast, when there is sufficient iron, Php4 is inactivated, thus allowing the transcription of many genes that encode iron-requiring proteins. Analysis by bimolecular fluorescence complementation and two-hybrid assays showed that Php4 and the monothiol glutaredoxin Grx4 physically interact with each other. Deletion mapping analysis revealed that the glutaredoxin (GRX) domain of Grx4 associates with Php4 in an iron-dependent manner. Site-directed mutagenesis identified the Cys172 of Grx4 as being required for this iron-dependent association. Subsequent analysis showed that, although the thioredoxin (TRX) domain of Grx4 interacts strongly with Php4, this interaction is insensitive to iron. Fine mapping analysis revealed that the Cys35 of Grx4 is necessary for the association between the TRX domain and Php4. Taken together, the results revealed that whereas the TRX domain interacts constitutively with Php4, the GRX domain-Php4 association is both modulated by iron and required for the inhibition of Php4 activity in response to iron repletion.","doi":"10.1128/EC.00060-12","authors":"Vachon P, Mercier A, Jbel M, Labbé S","authors_abbrev":"Vachon P et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2012-04-24","publication_year":"2012","canto_session_key":"b768efa38471ed4b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC26H8.06","SPBC16E9.01c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12426374","title":"Spindle-kinetochore attachment requires the combined action of Kin I-like Klp5/6 and Alp14/Dis1-MAPs in fission yeast.","citation":"EMBO J 2002 Nov 15;21(22):6015-24","abstract":"Fission yeast Klp5 and Klp6 belong to the microtubule-destabilizing Kin I family. In klp5 mutants, spindle checkpoint proteins Mad2 and Bub1 are recruited to mitotic kinetochores for a prolonged duration, indicating that these kinetochores are unattached. Further analysis shows that there are kinetochores to which only Bub1, but not Mad2, localizes. These kinetochores are likely to have been captured, yet lack tension. Thus Klp5 and Klp6 play a role in a spindle- kinetochore interaction at dual steps, capture and generation of tension. The TOG/XMAP215 family, Alp14 and Dis1 are known to stabilize microtubules and be required for the bivalent attachment of the kinetochore to the spindle. Despite apparent opposing activities towards microtubule stability, Klp5/Klp6 and Alp14/Dis1 share an essential function, as either dis1klp or alp14klp mutants are synthetically lethal, like alp14dis1. Defective phenotypes are similar to each other, characteristic of attachment defects and chromosome mis-segregation. Furthermore Alp14 is of significance for kinetochore localization of Klp5. We propose that Klp5/Klp6 and Alp14/Dis1 play a collaborative role in bipolar spindle formation during prometaphase through producing spindle dynamism.","authors":"Garcia MA, Koonrugsa N, Toda T","authors_abbrev":"Garcia MA et al.","pubmed_publication_date":"15 Nov 2002","pubmed_entrez_date":"2002-11-12","publication_year":"2002","canto_session_key":"266a57bb225cd9a6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-04-23 18:09:46","canto_approved_date":"2023-06-15 15:43:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-07 14:25:09","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPCC338.17c","SPCC1322.12c","SPCC736.14","SPCC320.13c","SPCC895.07","SPBC1685.15c","SPBC2F12.13"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2018-04-23"},{"uniquename":"PMID:12507760","title":"Ratiometric fluorescence measurements of membrane potential generated by yeast plasma membrane H(+)-ATPase reconstituted into vesicles.","citation":"Biochim Biophys Acta 2003 Jan 10;1609(1):71-9","abstract":"Potential-sensitive fluorescent probes oxonol V and oxonol VI were employed for monitoring membrane potential (Delta(psi)) generated by the Schizosaccharomyces pombe plasma membrane H(+)-ATPase reconstituted into vesicles. Oxonol VI was used for quantitative measurements of the Delta(psi) because its response to membrane potential changes can be easily calibrated, which is not possible with oxonol V. However, oxonol V has a superior sensitivity to Delta(psi) at very low concentration of reconstituted vesicles, and thus it is useful for testing quality of the reconstitution. Oxonol VI was found to be a good emission-ratiometric probe. We have shown that the reconstituted H(+)-ATPase generates Delta(psi) of about 160 mV on the vesicle membrane. The generated Delta(psi) was stable at least over tens of minutes. An influence of the H(+) membrane permeability on the Delta(psi) buildup was demonstrated by manipulating the H(+) permeability with the protonophore CCCP. Ratiometric measurements with oxonol VI thus offer a promising tool for studying processes accompanying the yeast plasma membrane H(+)-ATPase-mediated Delta(psi) buildup.","authors":"Holoubek A, Vecer J, Opekarová M, Sigler K","authors_abbrev":"Holoubek A et al.","pubmed_publication_date":"10 Jan 2003","pubmed_entrez_date":"2003-01-01","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19272449","title":"Comprehensive proteomic analysis of Schizosaccharomyces pombe by two-dimensional HPLC-tandem mass spectrometry.","citation":"Methods 2009 Jul;48(3):311-9","abstract":"We describe a detailed and widely applicable method for comprehensive proteomic profiling of the fission yeast Schizosaccharomyces pombe by 2-dimensional high performance liquid chromatography-electrospray ionization-tandem mass spectrometry that demonstrates high sensitivity and robust operation. Steps ranging from the preparation of total proteins, digestion of proteins to peptides, and separation of peptides by two-dimensional (1. strong cation exchange and 2. reversed-phase) high performance liquid chromatography followed by tandem mass spectrometry and data processing have been optimized for our instrumentation platform. Using this technology, we identify ca. 3400 proteins per sample and have identified an estimated 4600 proteins in vegetative cells (equal to ca. 90% of the predicted S. pombe proteome) at a false discovery rate of 0.02. Considering the fact that approximately 500 genes are strongly induced during sexual differentiation, and sexual differentiation was not included in our experiments, the proteomic profiling technique affords what should be virtually complete coverage of the vegetative S. pombe proteome. In addition, these methods are widely applicable, having been used for proteomic profiling of several other organisms.","doi":"10.1016/j.ymeth.2009.02.023","authors":"Brill LM, Motamedchaboki K, Wu S, Wolf DA","authors_abbrev":"Brill LM et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-03-11","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32366382","title":"Spt5 Phosphorylation and the Rtf1 Plus3 Domain Promote Rtf1 Function through Distinct Mechanisms.","citation":"Mol Cell Biol 2020 Jul 14;40(15)","abstract":"Rtf1 is a conserved RNA polymerase II (RNAPII) elongation factor that promotes cotranscriptional histone modification, RNAPII transcript elongation, and mRNA processing. Rtf1 function requires the phosphorylation of Spt5, an essential RNAPII processivity factor. Spt5 is phosphorylated within its C-terminal domain (CTD) by cyclin-dependent kinase 9 (Cdk9), the catalytic component of positive transcription elongation factor b (P-TEFb). Rtf1 recognizes phosphorylated Spt5 (pSpt5) through its Plus3 domain. Since Spt5 is a unique target of Cdk9 and Rtf1 is the only known pSpt5-binding factor, the Plus3/pSpt5 interaction is thought to be a key Cdk9-dependent event regulating RNAPII elongation. Here, we dissect Rtf1 regulation by pSpt5 in the fission yeast  Schizosaccharomyces pombe  We demonstrate that the Plus3 domain of Rtf1 (Prf1 in  S. pombe ) and pSpt5 are functionally distinct and that they act in parallel to promote Prf1 function. This alternate Plus3 domain function involves an interface that overlaps the pSpt5-binding site and that can interact with single-stranded nucleic acid or with the polymerase-associated factor (PAF) complex  in vitro  We further show that the C-terminal region of Prf1, which also interacts with PAF, has a similar parallel function with pSpt5. Our results elucidate unexpected complexity underlying Cdk9-dependent pathways that regulate transcription elongation.","doi":"10.1128/MCB.00150-20","authors":"Chen JJ, Mbogning J, Hancock MA, Majdpour D, Madhok M, Nassour H, Dallagnol JC, Pagé V, Chatenet D, Tanny JC","authors_abbrev":"Chen JJ et al.","pubmed_publication_date":"14 Jul 2020","pubmed_entrez_date":"2020-05-06","publication_year":"2020","canto_session_key":"8481a1a5bf90b23e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jennifer Chen","canto_first_approved_date":"2020-06-11 15:36:14","canto_approved_date":"2026-06-18 09:48:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-05-22 13:02:27","canto_added_date":"2020-05-07 00:15:04","annotation_curators":[{"name":"Jennifer Chen","community_curator":true,"annotation_count":71,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC13E7.08c","SPAC22F8.07c","SPBC32H8.10","SPBC651.09c","SPAC27D7.14c","SPAC664.03","SPAC23C4.19"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2020-06-11"},{"uniquename":"PMID:18548657","title":"Preparation and performance of immobilized yeast cells in columns containing no inert carrier.","citation":"Biotechnol Bioeng 1983 Feb;25(2):363-75","abstract":"Schizosaccharomyces pombe was cultivated in a medium of glucose (10 g/L) malt extract (3 g/L), yeast extract (3 g/L), and bactopeptone (5 g/L) to form flocs. More than 95% of the cell population were flocculated. Variation in glucose concentration (from 10 to 100 g/L) did not affect flocculation. Yeast extract helped induce flocculation. Application of the immobilized yeast for the continuous production of ethanol was tested in a column reactor. Soft yeast flocs (50-200 mesh) underwent morphological changes to heavy particles (0.1-0.3 cm diameter) after continuously being fed with fresh substrates in the column. Productivity as high as 87 g EtOH L(-1) h(-1) was obtained when a 150 g/L glucose medium was fed. The performance of this yeast reactor was stable over a two-month period. The ethanol yield was 97% of the theoretical maximum based upon glucose consumed.","authors":"Hsiao HY, Chiang LC, Yang CM, Chen LF, Tsao GT","authors_abbrev":"Hsiao HY et al.","pubmed_publication_date":"Feb 1983","pubmed_entrez_date":"1983-02-01","publication_year":"1983","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8855663","title":"A quantitative model for the cdc2 control of S phase and mitosis in fission yeast.","citation":"Trends Genet 1996 Sep;12(9):345-50","abstract":"In this article we consider the role of the cyclin-dependent protein kinase cdc2 in regulating progression through the fission yeast cell cycle. The onset of mitosis is governed by cdc2 in partnership with the B-type cyclin, cdc13. Recent evidence shows that the cdc2-cdc13 complex can also control the onset of S phase and, in addition, ensures that there is only one S phase per cell cycle. This leads us to propose a novel quantitative model in which different levels of cdc2 activity regulate cell-cycle progression: S phase is initiated when protein kinase activity increases from a very low to a moderate level; maintenance of this moderate level prevents re-initiation of S phase, and a further increase of activity to a high level initiates mitosis. Inactivation of the kinase activity at the end of mitosis resets the cell for a new cell cycle.","authors":"Stern B, Nurse P","authors_abbrev":"Stern B et al.","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24147005","title":"The coordination of cell growth during fission yeast mating requires Ras1-GTP hydrolysis.","citation":"PLoS One 2013;8(10):e77487","abstract":"The spatial and temporal control of polarity is fundamental to the survival of all organisms. Cells define their polarity using highly conserved mechanisms that frequently rely upon the action of small GTPases, such as Ras and Cdc42. Schizosaccharomyces pombe is an ideal system with which to study the control of cell polarity since it grows from defined tips using Cdc42-mediated actin remodeling. Here we have investigated the importance of Ras1-GTPase activity for the coordination of polarized cell growth during fission yeast mating. Following pheromone stimulation, Ras1 regulates both a MAPK cascade and the activity of Cdc42 to enable uni-directional cell growth towards a potential mating partner. Like all GTPases, when bound to GTP, Ras1 adopts an active conformation returning to an inactive state upon GTP-hydrolysis, a process accelerated through interaction with negative regulators such as GAPs. Here we show that, at low levels of pheromone stimulation, loss of negative regulation of Ras1 increases signal transduction via the MAPK cascade. However, at the higher concentrations observed during mating, hyperactive Ras1 mutations promote cell death. We demonstrate that these cells die due to their failure to coordinate active Cdc42 into a single growth zone resulting in disorganized actin deposition and unsustainable elongation from multiple tips. These results provide a striking demonstration that the deactivation stage of Ras signaling is fundamentally important in modulating cell polarity.","doi":"10.1371/journal.pone.0077487","authors":"Weston C, Bond M, Croft W, Ladds G","authors_abbrev":"Weston C et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-10-23","publication_year":"2013","canto_session_key":"51afeaedc270a24c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-05-10 12:28:07","canto_approved_date":"2022-01-03 19:40:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-10 12:28:00","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":43,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.12c","SPBC1D7.05","SPAC17H9.09c","SPBC1289.04c","SPAC110.03","SPAC1296.03c","SPBC28E12.03","SPAC11H11.04","SPAC16E8.09"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2018-05-10"},{"uniquename":"PMID:15163365","title":"Modelling the fission yeast cell cycle.","citation":"Brief Funct Genomic Proteomic 2004 Feb;2(4):298-307","abstract":"The molecular networks regulating basic physiological processes in a cell can be converted into mathematical equations (eg differential equations) and solved by a computer. The division cycle of eukaryotic cells is an important example of such a control system, and fission yeast is an excellent test organism for the computational modelling approach. The mathematical model is tested by simulating wild-type cells and many known cell cycle mutants. This paper describes an example where this approach is useful in understanding multiple rounds of DNA synthesis (endoreplication) in fission yeast cells that lack the main (B-type) mitotic cyclin, Cdc13. It is proposed that the key physiological variable driving progression through the cell cycle during balanced growth and division is the mass/DNA ratio, rather than the mass/nucleus ratio.","authors":"Sveiczer A, Tyson JJ, Novak B","authors_abbrev":"Sveiczer A et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2004-05-28","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24874881","title":"The proper splicing of RNAi factors is critical for pericentric heterochromatin assembly in fission yeast.","citation":"PLoS Genet 2014;10(5):e1004334","abstract":"Heterochromatin preferentially assembles at repetitive DNA elements, playing roles in transcriptional silencing, recombination suppression, and chromosome segregation. The RNAi machinery is required for heterochromatin assembly in a diverse range of organisms. In fission yeast, RNA splicing factors are also required for pericentric heterochromatin assembly, and a prevailing model is that splicing factors provide a platform for siRNA generation independently of their splicing activity. Here, by screening the fission yeast deletion library, we discovered four novel splicing factors that are required for pericentric heterochromatin assembly. Sequencing total cellular RNAs from the strongest of these mutants, cwf14Δ, showed intron retention in mRNAs of several RNAi factors. Moreover, introducing cDNA versions of RNAi factors significantly restored pericentric heterochromatin in splicing mutants. We also found that mutations of splicing factors resulted in defective telomeric heterochromatin assembly and mis-splicing the mRNA of shelterin component Tpz1, and that replacement of tpz1+ with its cDNA partially rescued heterochromatin defects at telomeres in splicing mutants. Thus, proper splicing of RNAi and shelterin factors contributes to heterochromatin assembly at pericentric regions and telomeres.","doi":"10.1371/journal.pgen.1004334","authors":"Kallgren SP, Andrews S, Tadeo X, Hou H, Moresco JJ, Tu PG, Yates JR, Nagy PL, Jia S","authors_abbrev":"Kallgren SP et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-05-31","publication_year":"2014","canto_session_key":"7d550a48ebee17b7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC10F6.02c","SPBC31F10.11c","SPAC1F3.09","SPBC16H5.10c","SPAC1834.04","SPAC644.12","SPBC16H5.05c","SPBC11G11.06c","SPBC646.02","SPBC21C3.05","SPBC3E7.13c","SPAC20H4.06c","SPCP1E11.07c","SPBC18H10.10c","SPCC550.02c","SPAC4F8.12c","SPAC57A7.04c","SPAC57A10.03","SPBC36.09","SPCC188.11","SPBC28F2.04c","SPBC28F2.03","SPAC13G7.07","SPAC20G8.06","SPAC21E11.05c","SPBC13E7.02","SPAC29A4.08c","SPBC32F12.05c","SPBC3E7.14","SPBP22H7.07","SPBC660.11","SPBC6B1.10","SPCC622.09","SPBC530.14c","SPCP1E11.11","SPBC24C6.11","SPBC215.12","SPAC2C4.03c","SPBC13E7.01","SPAC4A8.09c","SPAC19G12.07c","SPAC26A3.08","SPBC365.05c","SPCC1393.05","SPBC337.06c","SPBC146.05c","SPBC1861.08c","SPAC6G10.10c","SPBC1289.11","SPBC19C2.14","SPAC1486.03c","SPAC31G5.18c","SPAC9.03c","SPBC211.02c","SPAC20H4.09","SPAC3A12.11c","SPCC1620.10","SPBC4B4.05","SPBC3B9.02c","SPAC30D11.09","SPCC736.11"],"gene_count":61,"ltp_gene_count":61},{"uniquename":"PMID:18397994","title":"Slk1 is a meiosis-specific Sid2-related kinase that coordinates meiotic nuclear division with growth of the forespore membrane.","citation":"J Cell Sci 2008 May 01;121(Pt 9):1383-92","abstract":"Septation and spore formation in fission yeast are compartmentalization processes that occur during the mitotic and meiotic cycles, and that are regulated by the septation initiation network (SIN). In mitosis, activation of Sid2 protein kinase transduces the signal from the spindle pole body (SPB) to the middle of the cell in order to promote the constriction of the actomyosin ring. Concomitant with ring contraction, membrane vesicles are added at the cleavage site to enable the necessary expansion of the cell membrane. In meiosis, the forespore membrane is synthesized from the outer layers of the SPB by vesicle fusion. This membrane grows and eventually engulfs each of the four haploid nuclei. The molecular mechanism that connects the SIN pathway with synthesis of the forespore membrane is poorly understood. Here, we describe a meiosis-specific Sid2-like kinase (Slk1), which is important for the coordination of the growth of the forespore membrane with the meiotic nuclear divisions. Slk1 and Sid2 are required for forespore membrane biosynthesis and seem to be the final output of the SIN pathway in meiosis.","doi":"10.1242/jcs.023812","authors":"Pérez-Hidalgo L, Rozalén AE, Martín-Castellanos C, Moreno S","authors_abbrev":"Pérez-Hidalgo L et al.","pubmed_publication_date":"01 May 2008","pubmed_entrez_date":"2008-04-10","publication_year":"2008","canto_session_key":"fe12cd716f83c472","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-15 14:25:22","canto_approved_date":"2024-08-15 14:25:22","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-15 14:25:15","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":16,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPCC417.06c","SPAC24B11.11c","SPAC607.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-08-15"},{"uniquename":"EMBL:AU011629","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17981703","title":"Involvement of Dcr1 in post-transcriptional regulation of gene expression in Schizosaccharomyces pombe.","citation":"Front Biosci 2008 Jan 01;13:2203-15","abstract":"The ribonuclease III Dicer (Dcr1) has been shown to be required for chromosome segregation and gene silencing in Schizosaccharomyces pombe. These effects are thought to be transcriptional, mediated by formation and maintenance of heterochromatin, and guided by small RNAs derived from Dcr1 along a process known as RNA interference. In order to get further insights into the gene regulatory role of Dcr1, we performed comparative analyses of dcr1 knockout and wild-type fission yeast strains. Analysis of part of the soluble proteomes identified eight cellular proteins whose expression is under Dcr1 control, three of which are integral constituents of the glycolysis pathway. Further correlations with their respective mRNA transcript levels are compatible with the existence of a post-transcriptional gene regulatory mechanism involving Dcr1 or a Dcr1 complex. Experiments designed to identify components of Dcr1 complexes unveiled two novel Dcr1 interactors, namely the zinc finger protein Byr3 and the ribosomal protein L12. Consistently enriched in Dcr1 immune complexes, Byr3 and L12 may link Dcr1 to the transcriptional and translational machineries, respectively, and contribute to post-transcriptional gene regulation in fission yeast.","authors":"Gobeil LA, Plante P, Rohani M, Ouellette M, Provost P","authors_abbrev":"Gobeil LA et al.","pubmed_publication_date":"01 Jan 2008","pubmed_entrez_date":"2007-11-06","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.13c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:30049830","title":"Huntingtin-interacting protein 1 (HIP1) regulates arthritis severity and synovial fibroblast invasiveness by altering PDGFR and Rac1 signalling.","citation":"Ann Rheum Dis 2018 Nov;77(11):1627-1635","abstract":"While new treatments for rheumatoid arthritis (RA) have markedly improved disease control by targeting immune/inflammatory pathways, current treatments rarely induce remission, underscoring the need for therapies that target other aspects of the disease. Little is known about the regulation of disease severity and joint damage, which are major predictors of disease outcome, and might be better or complementary targets for therapy. In this study, we aimed to discover and characterise a new arthritis severity gene.\nAn unbiased and phenotype-driven strategy including studies of unique congenic rat strains was used to identify new arthritis severity and joint damage genes. Fibroblast-like synoviocytes (FLS) from rats and patients with RA expressing or not Huntingtin-interacting protein 1 (HIP1) were studied for invasiveness, morphology and cell signalling. HIP1 knockout mice were used in in vivo confirmatory studies. Paired t-test was used.\nDNA sequencing and subcongenic strains studied in pristane-induced arthritis identified a new amino acid changing functional variant in HIP1. HIP1 was required for the increased invasiveness of FLS from arthritic rats and from patients with RA. Knocking down HIP1 expression reduced receptor tyrosine kinase-mediated responses in RA FLS, including RAC1 activation, affecting actin cytoskeleton and cell morphology and interfering with the formation of lamellipodia, consistent with reduced invasiveness. HIP1 knockout mice were protected in KRN serum-induced arthritis and developed milder disease.\nHIP1 is a new arthritis severity gene and a potential novel prognostic biomarker and target for therapy in RA.","doi":"10.1136/annrheumdis-2018-213498","authors":"Laragione T, Brenner M, Lahiri A, Gao E, Harris C, Gulko PS","authors_abbrev":"Laragione T et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-07-28","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC688.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15911983","title":"Genetic manipulation of yeast to identify genes involved in regulation of chemosensitivity.","citation":"Methods Mol Med 2005;111:241-55","abstract":"Fission and budding yeast have been regarded as valuable tools for studying several cellular processes in eukaryotic cells and have been exploited as model systems for the identification of determinants of chemosensitivity. Indeed, yeast mutants of DNA repair and cell cycle checkpoint pathways exhibit increased sensitivity to selected antitumor drugs, thereby allowing us to establish the role of specific genes in drug response. The basic cellular functions of simple eukaryotic organisms and mammalian cells are conserved. Thus, the features of yeast, such as a small genome, a fast growth rate, and a peculiar life cycle, which allows easy genetic manipulation, can provide advantages in the identification of determinants of chemosensitivity. Here we focus on methods developed in fission yeast with particular reference to gene disruption, transformation, and mutagenesis approaches. These methods could be useful in an attempt to develop target-specific therapeutic strategies.","authors":"Beretta GL, Perego P","authors_abbrev":"Beretta GL et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-05-25","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF196291","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40668054","title":"Palmitoylation of the fission yeast protein Isp3 is essential for formation of the outermost layer of the spore wall.","citation":"Biosci Biotechnol Biochem 2025 Jul 16;","abstract":"Fission yeast spores possess strong resistance to environmental stresses, largely due to the outermost proteinaceous \"Isp3 layer\", which comprises Isp3 protein. Isp3 is palmitoylated and its localization to the spore periphery is impaired in mutants lacking palmitoyltransferase; however, the precise role of Isp3 palmitoylation remains unclear. Here, we found that Isp3-GFP was expressed at wild-type levels in forming spores in mug142∆ cells lacking the palmitoyltransferase catalytic unit; thus, lack of palmitoylation did not reduce Isp3 protein stability. Next, we identified cysteine 7 as the key palmitoylation site essential for Isp3 localization to the spore periphery. Electron microscopy revealed that the Isp3 fibrillar layer was absent in both mug142Δ and isp3-C7S spores. Additionally, the isp3-C7S spores displayed increased sensitivity to alcohol stress, similar to isp3∆ spores. Collectively, these results demonstrate that palmitoylation of Isp3 is essential for relocation of Isp3 to the spore surface and assembly of the Isp3 layer.","doi":"10.1093/bbb/zbaf104","authors":"Sakai T, Minomo N, Sakaguchi T, Tahara YO, Miyata M, Nakamura T","authors_abbrev":"Sakai T et al.","pubmed_publication_date":"16 Jul 2025","pubmed_entrez_date":"2025-07-16","publication_year":"2025","canto_session_key":"2ba627fdbad68ff9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-16 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25203555","title":"Fission yeast Pxd1 promotes proper DNA repair by activating Rad16XPF and inhibiting Dna2.","citation":"PLoS Biol 2014 Sep;12(9):e1001946","abstract":"Structure-specific nucleases play crucial roles in many DNA repair pathways. They must be precisely controlled to ensure optimal repair outcomes; however, mechanisms of their regulation are not fully understood. Here, we report a fission yeast protein, Pxd1, that binds to and regulates two structure-specific nucleases: Rad16XPF-Swi10ERCC1 and Dna2-Cdc24. Strikingly, Pxd1 influences the activities of these two nucleases in opposite ways: It activates the 3' endonuclease activity of Rad16-Swi10 but inhibits the RPA-mediated activation of the 5' endonuclease activity of Dna2. Pxd1 is required for Rad16-Swi10 to function in single-strand annealing, mating-type switching, and the removal of Top1-DNA adducts. Meanwhile, Pxd1 attenuates DNA end resection mediated by the Rqh1-Dna2 pathway. Disabling the Dna2-inhibitory activity of Pxd1 results in enhanced use of a break-distal repeat sequence in single-strand annealing and a greater loss of genetic information. We propose that Pxd1 promotes proper DNA repair by differentially regulating two structure-specific nucleases.","doi":"10.1371/journal.pbio.1001946","authors":"Zhang JM, Liu XM, Ding YH, Xiong LY, Ren JY, Zhou ZX, Wang HT, Zhang MJ, Yu Y, Dong MQ, Du LL","authors_abbrev":"Zhang JM et al.","pubmed_publication_date":"Sep 2014","pubmed_entrez_date":"2014-09-10","publication_year":"2014","canto_session_key":"ad3cea5e630841a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jia-Min Zhang","canto_first_approved_date":"2018-01-12 15:58:03","canto_approved_date":"2023-12-29 09:41:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-30 09:53:22","canto_added_date":"2014-09-11 00:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":53,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jia-Min Zhang","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.02","SPBC16D10.04c","SPBC4F6.15c","SPAC8F11.07c","SPCC1259.13","SPBC29A10.05","SPCC970.01","SPBC649.03","SPBC887.14c","SPBC1703.14c","SPCP31B10.05","SPBC409.16c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2018-01-12"},{"uniquename":"PMID:30840879","title":"The F-BAR Domain of Rga7 Relies on a Cooperative Mechanism of Membrane Binding with a Partner Protein during Fission Yeast Cytokinesis.","citation":"Cell Rep 2019 Mar 05;26(10):2540-2548.e4","abstract":"F-BAR proteins bind the plasma membrane (PM) to scaffold and organize the actin cytoskeleton. To understand how F-BAR proteins achieve their PM association, we studied the localization of a Schizosaccharomyces pombe F-BAR protein Rga7, which requires the coiled-coil protein Rng10 for targeting to the division site during cytokinesis. We find that the Rga7 F-BAR domain directly binds a motif in Rng10 simultaneously with the PM, and that an adjacent Rng10 motif independently binds the PM. Together, these multivalent interactions significantly enhance Rga7 F-BAR avidity for membranes at physiological protein concentrations, ensuring the division site localization of Rga7. Moreover, the requirement for the F-BAR domain in Rga7 localization and function in cytokinesis is bypassed by tethering an Rga7 construct lacking its F-BAR to Rng10, indicating that at least some F-BAR domains are necessary but not sufficient for PM targeting and are stably localized to specific cortical positions through adaptor proteins.","doi":"10.1016/j.celrep.2019.01.112","authors":"Liu Y, McDonald NA, Naegele SM, Gould KL, Wu JQ","authors_abbrev":"Liu Y et al.","pubmed_publication_date":"05 Mar 2019","pubmed_entrez_date":"2019-03-07","publication_year":"2019","canto_session_key":"95c831769f7efdd6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yajun Liu","canto_first_approved_date":"2019-07-03 06:30:25","canto_approved_date":"2024-04-02 14:07:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-24 21:03:30","canto_added_date":"2019-03-08 01:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yajun Liu","community_curator":true,"annotation_count":32,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.07c","SPBC23G7.08c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-07-03"},{"uniquename":"PMID:19520858","title":"Degradation of sterol regulatory element-binding protein precursor requires the endoplasmic reticulum-associated degradation components Ubc7 and Hrd1 in fission yeast.","citation":"J Biol Chem 2009 Jul 31;284(31):20512-21","abstract":"Sre1, the fission yeast sterol regulatory element-binding protein (SREBP), is an endoplasmic reticulum (ER) membrane-bound transcription factor that is a principal regulator of hypoxic gene expression. Under low oxygen, Sre1 is cleaved from its inactive ER precursor form to generate an active nuclear transcription factor that up-regulates genes required for low oxygen growth. To maintain a constant supply of Sre1, Sre1 precursor synthesis must be regulated to replenish Sre1 precursor lost to proteolytic cleavage under low oxygen. In this study, we investigated the mechanisms controlling Sre1 precursor levels. We found that positive feedback regulation at the sre1(+) promoter increases the synthesis of the Sre1 precursor under low oxygen and that this regulation is required for maximal Sre1 activation and target gene expression. We also demonstrate that the Sre1 precursor is rapidly degraded by the proteasome in the absence of its binding partner Scp1, which is required for oxygen-regulated Sre1 cleavage. Degradation of Sre1 in the absence of Scp1 requires the ER-associated degradation (ERAD) components Ubc7, an E2 ubiquitin conjugating enzyme, and Hrd1, an E3 ubiquitin ligase. We conclude that positive feedback regulation to up-regulate Sre1 precursor synthesis under low oxygen is essential for Sre1 function and propose that excess Sre1 precursor is removed by ERAD to ensure complex formation between Sre1 and its binding partner Scp1. Thus, Sre1 is a new example of an endogenous ERAD substrate, establishing fission yeast as an organism for the study of this important degradative pathway.","doi":"10.1074/jbc.M109.002436","authors":"Hughes BT, Nwosu CC, Espenshade PJ","authors_abbrev":"Hughes BT et al.","pubmed_publication_date":"31 Jul 2009","pubmed_entrez_date":"2009-06-13","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP16F5.04","SPBC19C2.09","SPBC17D11.02c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU007729","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24186364","title":"Organisation of the complex locus trp1 in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1982 Oct;6(1):13-8","abstract":"65 trp1(-) alleles of Schizosaccharomyces pombe have been analysed for their interallelic complementation pattern, suppressibility by nonsense suppressors and position of the corresponding mutation site on an intragenic map of the trp1 locus. In addition to the three complementation classes previously described (Schweingruher and Dietrich 1973) as defective in phosphoribosylanthranilate isomerase (trp1A), indole glycerolphosphate synthetase (trp1B) and anthranilate synthetase (trp1C), two new complementation classes, trp1BC and trp1ABC, were found. The former is represented by a single allele which can only complement trp1A mutants. The latter is represented by six alleles which fail to complement tester mutants of the trp1A, trp1B or trp1C class. Classes trp1A, trp1B and trp1C correspond to mutations in three nonoverlapping regions mapping in the order trp1A, trp1B and trp1C All the alleles of the trp1BC and trp1ABC classes correspond to mutations in the trp1C region. Nonsense alleles of the opal (UGA) or ochre (UAA) type were found in the trp1A (2 alleles out of 17) and trp1ABC (5 alleles out of 6) classes only. These data indicate that the trp1 locus is transcribed as a single messenger RNA with transcription starting from the trp1C region. This messenger is probably translated in a single, multifunctional polypeptide, or at most in two polypeptides coded for by the trp1B-trp1C and by the trp1A regions. In addition, the polar effect of nonsense mutations in the trp1C region is cancelled by rare spontaneous mutations occuring at or very near the trp1 locus, which may act by creating an internal single for the initiation of transcription and/or translation.","doi":"10.1007/BF00397634","authors":"Thuriaux P, Heyer WD, Strauss A","authors_abbrev":"Thuriaux P et al.","pubmed_publication_date":"Oct 1982","pubmed_entrez_date":"2013-11-05","publication_year":"1982","canto_session_key":"17515695aa71e3b3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-04-17 16:22:24","canto_approved_date":"2024-12-07 15:46:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-17 16:14:02","canto_added_date":"2014-02-16 06:09:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1539.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-17"},{"uniquename":"PMID:23221705","title":"Core histone charge and linker histone H1 effects on the chromatin structure of Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2012;76(12):2261-6","abstract":"Histones are highly conserved proteins among eukaryotes. However, yeast histones are more divergent in their sequences. In particular, the histone tail regions of the fission yeast, Schizosaccharomyces pombe, have fewer lysine residues, making their charges less positive than those of higher eukaryotes. In addition, the S. pombe chromatin lacks linker histones. How these factors affected yeast chromatin folding was analysed by biochemical reconstitution in combination with atomic force microscopy. Reconstitution of a nucleosome array showed that S. pombe chromatin has a more open structure similar to reconstituted human acetylated chromatin. The S. pombe nucleosomal array formed thinner fibers than those of the human nucleosomal array in the presence of mammalian linker histone H1. Such S. pombe fibers were more comparable to human acetylated fibers. These findings suggest that the core histone charges would determine the intrinsic characteristics of S. pombe chromatin and affect inter-nucleosomal interactions.","authors":"Prieto E, Hizume K, Kobori T, Yoshimura SH, Takeyasu K","authors_abbrev":"Prieto E et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-12-11","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1318242","title":"Synthesis and degradation of polyphosphate in the fission yeast Schizosaccharomyces pombe: mutations in phosphatase genes do not affect polyphosphate metabolism.","citation":"FEMS Microbiol Lett 1992 Apr 15;71(2):151-6","abstract":"The fission yeast Schizosaccharomyces pombe was found to accumulate large amounts of polyphosphate, particularly when grown on arginine as the nitrogen source. Upon transfer to a medium without phosphate, polyphosphate was degraded and served as an endogenous phosphate reserve. When phosphate was added again after a prolonged period of phosphate starvation, fission yeast cells synthesized more polyphosphate than they had contained before starvation, a phenomenon known as over-compensation. Strains carrying mutated structural genes for three different phosphatases, pho1, pho2 or pho3, degraded polyphosphate at the same rate as the wild-type strain during phosphate starvation and showed the same type of over-compensation when phosphate was added again.","authors":"Müller J, Westenberg B, Boller T, Wiemken A","authors_abbrev":"Müller J et al.","pubmed_publication_date":"15 Apr 1992","pubmed_entrez_date":"1992-04-15","publication_year":"1992","canto_session_key":"d1b3ad6fc7c623d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-28 10:42:28","canto_approved_date":"2019-11-28 10:42:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-15 15:37:31","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPBC15D4.15"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-11-28"},{"uniquename":"PMID:23471351","title":"Stress induces remodelling of yeast interaction and co-expression networks.","citation":"Mol Biosyst 2013 Jul;9(7):1697-707","abstract":"Network analysis provides a powerful framework for the interpretation of genome-wide data. While static network approaches have proved fruitful, there is increasing interest in the insights gained from the analysis of cellular networks under different conditions. In this work, we study the effect of stress on cellular networks in fission yeast. Stress elicits a sophisticated and large scale cellular response, involving a shift of resources from cell growth and metabolism towards protection and maintenance. Previous work has suggested that these changes can be appreciated at the network level. In this paper, we study two types of cellular networks: gene co-regulation networks and weighted protein interaction networks. We show that in response to oxidative stress, the co-regulation networks re-organize towards a more modularised structure: while sets of genes become more tightly co-regulated, co-regulation between these modules is decreased. This shift translates into longer average shortest path length, increased transitivity, and decreased modular overlap in these networks. We also find a similar change in structure in the weighted protein interaction network in response to both oxidative stress and nitrogen starvation, confirming and extending previous findings. These changes in network structure could represent an increase in network robustness and/or the emergence of more specialised functional modules. Additionally, we find stress induces tighter co-regulation of non-coding RNAs, decreased functional importance of splicing factors, as well as changes in the centrality of genes involved in chromatin organization, cytoskeleton organization, cell division, and protein turnover.","doi":"10.1039/c3mb25548d","authors":"Lehtinen S, Marsellach FX, Codlin S, Schmidt A, Clément-Ziza M, Beyer A, Bähler J, Orengo C, Pancaldi V","authors_abbrev":"Lehtinen S et al.","pubmed_publication_date":"Jul 2013","pubmed_entrez_date":"2013-03-09","publication_year":"2013","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21441097","title":"TRFolder: computational prediction of novel telomerase RNA structures in yeast genomes.","citation":"Int J Bioinform Res Appl 2011;7(1):63-81","abstract":"The identification of Telomerase RNAs (TRs) has been difficult owing to their rapid evolutionary divergence. The common core structure found in all known TRs contains a pseudoknot and a triple helix, which are beyond the capability of existing RNA-structure-profiling techniques. We describe a novel approach to predict the structure of key TR features and to aid the identification of TRs in genomes, using a program we developed, TRFolder. We applied our method to confirm and improve previously studied core structures from Saccharomyces and Kluyveromyces TRs. We made novel structural predictions of core elements of the TRs from Schizosaccharomyces pombe, Candida albicans, and several other yeast species.","authors":"Guo L, Zhang D, Wang Y, Malmberg RL, McEachern M, Cai L","authors_abbrev":"Guo L et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-03-29","publication_year":"2011","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR15346","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:2712","SPCC11E10.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16370357","title":"[Mechanism of chromosome segregation in meiosis].","citation":"Seikagaku 2005 Nov;77(11):1396-404","abstract":"","authors":"Sakuno T, Watanabe Y","authors_abbrev":"Sakuno T et al.","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-12-24","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9524127","title":"Hus1p, a conserved fission yeast checkpoint protein, interacts with Rad1p and is phosphorylated in response to DNA damage.","citation":"EMBO J 1998 Apr 01;17(7):2055-66","abstract":"The hus1+ gene is one of six fission yeast genes, termed the checkpoint rad genes, which are essential for both the S-M and DNA damage checkpoints. Classical genetics suggests that these genes are required for activation of the PI-3 kinase-related (PIK-R) protein, Rad3p. Using a dominant negative allele of hus1+, we have demonstrated a genetic interaction between hus1+ and another checkpoint rad gene, rad1+. Hus1p and Rad1p form a stable complex in wild-type fission yeast, and the formation of this complex is dependent on a third checkpoint rad gene, rad9+, suggesting that these three proteins may exist in a discrete complex in the absence of checkpoint activation. Hus1p is phosphorylated in response to DNA damage, and this requires rad3+ and each of the other checkpoint rad genes. Although there is no gene related to hus1+ in the Saccharomyces cerevisiae genome, we have identified closely related mouse and human genes, suggesting that aspects of the checkpoint control mechanism are conserved between fission yeast and higher eukaryotes.","authors":"Kostrub CF, Knudsen K, Subramani S, Enoch T","authors_abbrev":"Kostrub CF et al.","pubmed_publication_date":"01 Apr 1998","pubmed_entrez_date":"1998-06-06","publication_year":"1998","canto_session_key":"08cc3df57adda022","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-04-30 10:26:12","canto_approved_date":"2023-07-10 17:01:03","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2019-04-30 10:26:05","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPBC216.05","SPAC14C4.13","SPCC18B5.11c","SPAC664.07c","SPAC20G4.04c","SPCC18B5.03","SPCC1259.13","SPBC11B10.09","SPAC9E9.08"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2019-04-30"},{"uniquename":"PMID:36095070","title":"The hallmark domain of the oldest autophagy receptor family is a cargo-binding module.","citation":"Autophagy 2023 Apr;19(4):1359-1360","abstract":"In selective macroautophagy/autophagy, autophagy receptors are key molecules that determine cargo specificity. Most known autophagy receptors only exist in some but not all eukaryotic lineages. The exception is Nbr1 proteins, which are conserved across eukaryotes. The four-tryptophan (FW) domain is the hallmark of Nbr1 proteins, but its function has been unknown. Our recent study found that the FW domain in the Nbr1 protein of the filamentous fungus  Chaetomium thermophilum  binds the α-mannosidase Ams1, a known selective autophagy cargo in budding yeast and fission yeast. Furthermore, we showed that when  C. thermophilum  Nbr1 and Ams1 are expressed heterologously in fission yeast, FW domain-mediated binding can promote autophagic delivery of Ams1 into vacuoles. We solved the structure of the FW-Ams1 complex and revealed the structural mechanism underlying Ams1 recognition by the FW domain. The  N -terminal di-glycine peptide of Ams1 fits into a conserved pocket of the FW domain. We propose that this cargo-binding mechanism may also be employed by Nbr1 proteins in other eukaryotes.","doi":"10.1080/15548627.2022.2123636","authors":"Pan ZQ, Ye K, Du LL","authors_abbrev":"Pan ZQ et al.","pubmed_publication_date":"Apr 2023","pubmed_entrez_date":"2022-09-12","publication_year":"2023","canto_session_key":"07946c4126864269","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-15 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP35G2.11c","SPAC513.05"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:21348937","title":"Biodiversity in sulfur metabolism in hemiascomycetous yeasts.","citation":"FEMS Yeast Res 2011 Jun;11(4):366-78","abstract":"The evolution of the metabolism of sulfur compounds among yeast species was investigated. Differences between species were observed in the cysteine biosynthesis pathway. Most yeast species possess two pathways leading to cysteine production, the transsulfuration pathway and the O-acetyl-serine (OAS) pathway, with the exception of Saccharomyces cerevisiae and Candida glabrata, which only display the transsulfuration pathway, and Schizosaccharomyces pombe, which only have the OAS pathway. An examination of the components of the regulatory network in the different species shows that it is conserved in all the species analyzed, as its central component Met4p was shown to keep its functional domains and its partners were present. The analysis of the presence of genes involved in the catabolic pathway shows that it is evolutionarily conserved in the sulfur metabolism and leads us to propose a role for two gene families which appeared to be highly conserved. This survey has provided ways to understand the diversity of sulfur metabolism products among yeast species through the reconstruction of these pathways. This diversity could account for the difference in metabolic potentialities of the species with a biotechnological interest.","doi":"10.1111/j.1567-1364.2011.00725.x","authors":"Hébert A, Casaregola S, Beckerich JM","authors_abbrev":"Hébert A et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-02-26","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23832353","title":"The fission yeast php2 mutant displays a lengthened chronological lifespan.","citation":"Biosci Biotechnol Biochem 2013;77(7):1548-55","abstract":"The Schizosaccharomyces pombe php2(+) gene encodes a subunit of the CCAAT-binding factor complex. We found that disruption of the php2(+) gene extended the chronological lifespan of the fission yeast. Moreover, the lifespan of the Δphp2 mutant was barely extended under calorie restricted (CR) conditions. Many other phenotypes of the Δphp2 mutant resembled those of wild-type cells grown under CR conditions, suggesting that the Δphp2 mutant might undergo CR. The mutant also showed low respiratory activity concomitant with decreased expression of the cyc1(+) and rip1(+) genes, both of which are involved in mitochondrial electron transport. On the basis of a chromatin immunoprecipitation assay, we determined that Php2 binds to a DNA region upstream of cyc1(+) and rip1(+) in S. pombe. Here we discuss the possible mechanisms by which the chronological lifespan of Δphp2 mutant is extended.","authors":"Takuma K, Ohtsuka H, Azuma K, Murakami H, Aiba H","authors_abbrev":"Takuma K et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-09","publication_year":"2013","canto_session_key":"c0ce05a74db23f8e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_approved_date":"2016-07-11 12:58:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-07-04 09:00:55","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B8.02","SPBC16H5.06","SPBC725.11c","SPCC191.07","SPAC23C11.08","SPBC337.15c","SPAC24B11.06c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2016-07-04"},{"uniquename":"PMID:18769921","title":"Genetic analysis reveals different roles of Schizosaccharomyces pombe sfr1/dds20 in meiotic and mitotic DNA recombination and repair.","citation":"Curr Genet 2008 Oct;54(4):197-211","abstract":"DNA double-strand break (DSB) repair mediated by the Rad51 pathway of homologous recombination is conserved in eukaryotes. In yeast, Rad51 paralogs, Saccharomyces cerevisiae Rad55-Rad57 and Schizosaccharomyces pombe Rhp55-Rhp57, are mediators of Rad51 nucleoprotein formation. The recently discovered S. pombe Sfr1/Dds20 protein has been shown to interact with Rad51 and to operate in the Rad51-dependent DSB repair pathway in parallel to the paralog-mediated pathway. Here we show that Sfr1 is a nuclear protein and acts downstream of Rad50 in DSB processing. sfr1Delta is epistatic to rad18 (-) and rad60 (-), and Sfr1 is a high-copy suppressor of the replication and repair defects of a rad60 mutant. Sfr1 functions in a Cds1-independent UV damage tolerance mechanism. In contrast to mitotic recombination, meiotic recombination is significantly reduced in sfr1Delta strains. Our data indicate that Sfr1 acts in DSB repair mainly outside of S-phase, and is required for wild-type levels of meiotic recombination. We suggest that Sfr1 acts early in recombination and has a specific role in Rad51 filament assembly, distinct from that of the Rad51 paralogs.","doi":"10.1007/s00294-008-0212-z","authors":"Khasanov FK, Salakhova AF, Khasanova OS, Grishchuk AL, Chepurnaja OV, Korolev VG, Kohli J, Bashkirov VI","authors_abbrev":"Khasanov FK et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-09-05","publication_year":"2008","canto_session_key":"c92c4fac293808ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-09-29 14:46:57","canto_approved_date":"2025-09-04 09:48:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-29 14:46:48","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":56,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.06","SPBC3E7.08c","SPBC1921.02","SPBC28F2.07","SPCC18B5.11c","SPAC644.14c","SPAC2G11.12","SPBC19C7.09c","SPAC15A10.03c","SPAC1556.01c","SPAC3C7.03c","SPAC4H3.05"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2016-09-29"},{"uniquename":"PMID:9370289","title":"The human RAE1 gene is a functional homologue of Schizosaccharomyces pombe rae1 gene involved in nuclear export of Poly(A)+ RNA.","citation":"Gene 1997 Oct 01;198(1-2):251-8","abstract":"A Schizosaccharomyces pombe temperature-sensitive mutant, rae1-1, was previously identified by us as being defective in nuclear export of Poly(A)+ RNA when grown at restrictive temperature. Here, we report the isolation of the human homologue of the S. pombe rae1 gene. The RAE1 genes are highly conserved in evolution in both structure and function. The human RAE1 cDNA, when expressed from the CMV-promoter, can suppress partially the temperature sensitivity of the rae1-1 mutant. This is also reflected by increased Poly(A)+ RNA export at a restrictive temperature. An epitope tagged human Rae1p localizes to both the nucleus and the cytoplasm in transiently transfected HeLa cells. We discuss the potential role of Rae1p in nuclear cytoplasmic trafficking in yeast and higher eukaryotic cells.","authors":"Bharathi A, Ghosh A, Whalen WA, Yoon JH, Pu R, Dasso M, Dhar R","authors_abbrev":"Bharathi A et al.","pubmed_publication_date":"01 Oct 1997","pubmed_entrez_date":"1997-11-25","publication_year":"1997","canto_session_key":"9382823f7e3a2d55","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 16:37:58","canto_session_submitted_date":"2012-03-03 16:24:06","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.05c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:10611485","title":"The tRNA N2,N2-dimethylguanosine-26 methyltransferase encoded by gene trm1 increases efficiency of suppression of an ochre codon in Schizosaccharomyces pombe.","citation":"FEBS Lett 1999 Dec 24;464(1-2):67-70","abstract":"In the majority of eukaryotic tRNAs, the guanosine at position 26 is modified by a dimethyl group, but so far a function of this modification has not been detected. We isolated the Schizosaccharomyces pombe gene, trm1, encoding the tRNA N2, N2-dimethylguanosine-26 methyltransferase. Strains having the gene deleted completely lack N2,N2-dimethylguanosine. In strains carrying the weak ochre tRNA suppressor sup3-i, deletion of trm1 abolishes suppression indicating that the trm1 deletion acts as an antisuppressor mutation. The result suggests that in vivo N2, N2-dimethylguanosine-26 increases the capacity of the sup3-i serine tRNA to translate the UAA (ochre) codon.","authors":"Niederberger C, Gräub R, Costa A, Desgrès J, Schweingruber ME","authors_abbrev":"Niederberger C et al.","pubmed_publication_date":"24 Dec 1999","pubmed_entrez_date":"1999-12-28","publication_year":"1999","canto_session_key":"0665360651ed660b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-02 17:14:20","canto_approved_date":"2025-02-05 08:15:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-30 10:23:28","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25D12.05","SPATRNASER.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-06-02"},{"uniquename":"PMID:7565614","title":"A fission yeast gene mapping close to suc1 encodes a protein containing two bromodomains.","citation":"Mol Gen Genet 1995 Aug 30;248(4):491-8","abstract":"A novel gene, brd1, has been cloned from the fission yeast Schizosaccharomyces pombe. The predicted brd1 product contains two copies of an imperfect repeat of 96 amino acid residues in its N-terminal half. These each include a region with high homology to the bromodomains found in transcriptional activator proteins from a diversity of eukaryotes. An in vivo deletion of the complete brd1 open reading frame is not lethal but cells exhibit thermosensitivity, with reductions in both cell growth and stationary phase survival at 36 degrees C. brd1 maps adjacent to the gene suc1, but is expressed separately to give a low abundance 2.1 kb mRNA.","authors":"Aves SJ, Hindley J, Phear GA, Tongue N","authors_abbrev":"Aves SJ et al.","pubmed_publication_date":"30 Aug 1995","pubmed_entrez_date":"1995-08-30","publication_year":"1995","canto_session_key":"7940d5d489db05dd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-04-02 17:05:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-02 17:05:10","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-02"},{"uniquename":"PMID:19502729","title":"Glutamyl tRNA synthetases and glutamic acid induce sexual differentiation of Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2009 Jun;73(6):1339-47","abstract":"The moc3 gene was screened out as an inducer of sexual differentiation in fission yeast Schizosaccharomyces pombe. We isolated a novel gene, named ers2, encoding mitochondrial glutamyl tRNA synthetase (mGluRS) as a Moc3 interacting element by the yeast two-hybrid system. Cytoplasmic glutamyl tRNA synthetase (cGluRS) also interacted with Moc3 in a yeast two-hybrid system. Disruption of ers1 (cGluRS) and of ers2 (mGluRS) indicated that these genes are both essential for the cell growth of S. pombe. We found that ers2 severely affected cell growth and decreased viability, but induced sexual differentiation of S. pombe when it was over-expressed. Over-expression of ers1 also stimulated sexual differentiation in S. pombe. These observations led us to test the effects of various amino acids on sexual differentiation. We found that glutamic acid, as well as other specific amino acids, such as tryptophan, methionine, and threonine, efficiently induced sexual differentiation in S. pombe. Our findings suggest a new regulatory mechanism where GluRSs and glutamic acid are involved in sexual differentiation in S. pombe.","authors":"Paul SK, Goldar MM, Yakura M, Oowatari Y, Kawamukai M","authors_abbrev":"Paul SK et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-06-09","publication_year":"2009","canto_session_key":"179d07b1db7b4432","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-30 23:19:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-09 15:18:24","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.07c","SPAPB1A10.11c","SPAC17A5.15c","SPAC26F1.13c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2013-10-09"},{"uniquename":"PMID:26263625","title":"[Hybrid Sterility of the Yeast Schizosaccharomyces pombe: Genetic Genus and Many Species in statu nascendi?].","citation":"Mikrobiologiia 2015;84(2):192-203","abstract":"A phenomenon of ascospore death was observed in a number of Schizosaccharomyces pombe interstrain hybrids. Meiotic recombination of the control parental auxotrophic markers was, however, observed in a random ascospore analysis. Genetic and molecular biological data indicated existence of at least geographical divergence of the genomes in Sch. pombe populations. Classification of the genus, species, and varieties of these yeasts is discussed.","authors":"Naumov GI, Kondratieva VI, Naumova ES","authors_abbrev":"Naumov GI et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-08-13","publication_year":"2015","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2015-08-14 00:19:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21823226","title":"RITS-connecting transcription, RNA interference, and heterochromatin assembly in fission yeast.","citation":"Wiley Interdiscip Rev RNA 2011;2(5):632-46","abstract":"In recent years, a bevy of evidence has been unearthed indicating that 'silent' heterochromatin is not as transcriptionally inert as once thought. In the unicellular yeast Schizosaccharomyces pombe, the processing of transcripts derived from centromeric repeats into homologous short interfering RNA (siRNA) is essential for the formation of centromeric heterochromatin. Deletion of genes required for siRNA biogenesis showed that core components of the canonical RNA interference (RNAi) pathway are essential for centromeric heterochromatin assembly as well as for centromere function. Subsequent purification of the RNA-induced initiation of transcriptional gene silencing (RITS) complex provided the critical link between siRNAs and heterochromatin assembly, with RITS acting as a physical bridge between noncoding RNA scaffolds and chromatin. Here, we review current understanding of how RITS promotes heterochromatin formation and how it participates in transcription-coupled silencing. WIREs RNA 2011 2 632-646 DOI: 10.1002/wrna.80 For further resources related to this article, please visit the WIREs website.","doi":"10.1002/wrna.80","authors":"Creamer KM, Partridge JF","authors_abbrev":"Creamer KM et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-08-09","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9717576","title":"Deleterious effects of androstenedione on growth and cell morphology of Schizosaccharomyces pombe.","citation":"Antonie Van Leeuwenhoek 1998 Feb;73(2):189-94","abstract":"Androgens (androstenedione and testosterone) belong to the most important compounds in human steroidogenesis. The 17 beta-hydroxysteroid dehydrogenase responsible for interconversion of the oxygenic group on C-17 of androgens ring is involved in steroid hormone synthesis. The fission yeast Schizosaccharomyces pombe 972 h- was found to contain constitutive 17 beta-hydroxysteroid dehydrogenase that was able to reduce androstenedione to testosterone and oxidize testosterone to androstenedione. The reductive pathway was found to be predominant while the oxidative one was carried out with much lower activity. Exogenous androstenedione, contrary to testosterone, inhibited S. pombe growth and stimulated the formation of aberrant swollen cells with slighter cell wall sensitivity to the action of the lytic enzyme Novozym. It is postulated that the 17 beta-hydroxysteroid dehydrogenase prevents the deleterious effects of androstenedione on the morphology and growth of the yeast's cells by androstedione reduction to testosterone.","authors":"Długoński J, Wilmańska D","authors_abbrev":"Długoński J et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-08-26","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2908246","title":"Cloning and sequencing of the cyclin-related cdc13+ gene and a cytological study of its role in fission yeast mitosis.","citation":"J Cell Sci 1988 Dec;91 ( Pt 4):587-95","abstract":"We have cloned and sequenced the cdc13+ gene from fission yeast. When a major part of the cdc13+ gene is deleted from the chromosome, cells arrest in interphase, but partial loss of gene activity leads to cells containing condensed chromosomes, aberrant septa and a microtubular cytoskeleton with characteristics of both G2 and M. Expression of this phenotype is influenced by the nutritional status of the cell. Our results suggest that the cdc13+ gene function is required for the control of the G2 to M transition. It appears to play a role in regulating the separate pathways of events involved in the physical process of mitosis, for example in the reorganization of the cytoskeleton on transition from G2 to mitosis. The cdc13+ gene function interacts closely with both the yeast and human homologues of cdc2+, suggesting that mammalian cells may contain a cdc13+ homologue. The gene encodes a putative polypeptide of 482 amino acids, and a central region of 176 amino acids of this polypeptide is 50% identical with sea urchin cyclin. Therefore, the cdc13+ protein is cyclin related and could act as a regulator or substrate of the p34cdc2 protein kinase, which initiates mitosis.","authors":"Hagan I, Hayles J, Nurse P","authors_abbrev":"Hagan I et al.","pubmed_publication_date":"Dec 1988","pubmed_entrez_date":"1988-12-01","publication_year":"1988","canto_session_key":"9e29d45d34f5263a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-04-06 13:27:50","canto_approved_date":"2025-09-03 13:18:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-05 17:13:10","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":5,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-04-06"},{"uniquename":"PMID:9199286","title":"Mkh1, a MEK kinase required for cell wall integrity and proper response to osmotic and temperature stress in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1997 Jul;17(7):3508-19","abstract":"We have identified a Schizosaccharomyces pombe gene, mkh1, that encodes a MEK kinase (MEKK) homolog. The coding region of mkh1 is contained within a single exon encoding a 1,116-amino-acid protein. The putative catalytic domain of Mkh1 is 54% identical to the catalytic domain of S. cerevisiae Bck1, the most closely related protein. Deletion of mkh1 did not significantly affect cell growth or division under standard conditions. However, mkh1delta cell growth was inhibited by high KCl or NaCl concentrations. mkh1delta cells required a longer time to reenter the cell cycle after prolonged stationary-phase arrest. Also, mkh1delta cells exhibited a round cell shape, while overexpression of Mkh1 resulted in an elongated cell shape. mkh1delta cells exhibited a more dramatic phenotype when grown in nutrient-limiting conditions at high temperature or in hyperosmotic medium. In such conditions, completion of cytokinesis was inhibited, resulting in the growth of pseudohyphal filaments with multiple septa and nuclei. Also, mkh1delta cells were hypersensitive to beta-glucanase treatment. Together these results suggest that Mkh1 regulates cell morphology, cell wall integrity, salt resistance, cell cycle reentry from stationary-phase arrest, and filamentous growth in response to stress. These phenotypes are essentially identical to those exhibited by cells lacking Pmk1/Spm1, a recently identified mitogen-activated protein kinase. Our evidence suggests that Pmk1/Spm1 acts downstream from Mkh1 in a common pathway. Our results also suggest that Mkh1 and Pck2 act independently to maintain cell wall integrity, cell morphology, and salt resistance but act in opposition to regulate filamentous growth.","authors":"Sengar AS, Markley NA, Marini NJ, Young D","authors_abbrev":"Sengar AS et al.","pubmed_publication_date":"Jul 1997","pubmed_entrez_date":"1997-07-01","publication_year":"1997","canto_session_key":"2cf3451aa9ef777f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-02-09 18:34:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-14 10:01:23","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.02c","SPBC409.07c","SPBC12D12.04c","SPAC17G8.14c","SPAC24B11.06c","SPBC119.08"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-05-14"},{"uniquename":"PMID:21324894","title":"Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast.","citation":"J Biol Chem 2011 Apr 15;286(15):13775-90","abstract":"Eukaryotic cells monitor and maintain protein quality through a set of protein quality control (PQC) systems whose role is to minimize the harmful effects of the accumulation of aberrant proteins. Although these PQC systems have been extensively studied in the cytoplasm, nuclear PQC systems are not well understood. The present work shows the existence of a nuclear PQC system mediated by the ubiquitin-proteasome system in the fission yeast Schizosaccharomyces pombe. Asf1-30, a mutant form of the histone chaperone Asf1, was used as a model substrate for the study of the nuclear PQC. A temperature-sensitive Asf1-30 protein localized to the nucleus was selectively degraded by the ubiquitin-proteasome system. The Asf1-30 mutant protein was highly ubiquitinated at higher temperatures, and it remained stable in an mts2-1 mutant, which lacks proteasome activity. The E2 enzyme Ubc4 was identified among 11 candidate proteins as the ubiquitin-conjugating enzyme in this system, and San1 was selected among 100 candidates as the ubiquitin ligase (E3) targeting Asf1-30 for degradation. San1, but not other nuclear E3s, showed specificity for the mutant nuclear Asf1-30, but did not show activity against wild-type Asf1. These data clearly showed that the aberrant nuclear protein was degraded by a defined set of E1-E2-E3 enzymes through the ubiquitin-proteasome system. The data also show, for the first time, the presence of a nuclear PQC system in fission yeast.","doi":"10.1074/jbc.M110.169953","authors":"Matsuo Y, Kishimoto H, Tanae K, Kitamura K, Katayama S, Kawamukai M","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"15 Apr 2011","pubmed_entrez_date":"2011-02-18","publication_year":"2011","canto_session_key":"0d6e46fca4be8cc5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-08 20:33:38","canto_approved_date":"2026-01-31 12:06:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-09 16:23:36","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":45,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2A9.04c","SPBC1105.17","SPCC663.05c","SPBC17D11.02c","SPBC119.02","SPBC4.07c","SPBC409.04c","SPBC557.03c","SPBC14F5.07"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-12-08"},{"uniquename":"PMID:22561346","title":"CENP-T proteins are conserved centromere receptors of the Ndc80 complex.","citation":"Nat Cell Biol 2012 May 06;14(6):604-13","abstract":"Centromeres direct the assembly of kinetochores, microtubule-attachment sites that allow chromosome segregation on the mitotic spindle. Fundamental differences in size and organization between evolutionarily distant eukaryotic centromeres have in many cases obscured general principles of their function. Here we demonstrate that centromere-binding proteins are highly conserved between budding yeast and humans. We identify the histone-fold protein Cnn1(CENP-T) as a direct centromere receptor of the microtubule-binding Ndc80 complex. The amino terminus of Cnn1 contains a conserved peptide motif that mediates stoichiometric binding to the Spc24-25 domain of the Ndc80 complex. Consistent with the critical role of this interaction, artificial tethering of the Ndc80 complex through Cnn1 allows mini-chromosomes to segregate in the absence of a natural centromere. Our results reveal the molecular function of CENP-T proteins and demonstrate how the Ndc80 complex is anchored to centromeres in a manner that couples chromosome movement to spindle dynamics.","doi":"10.1038/ncb2493","authors":"Schleiffer A, Maier M, Litos G, Lampert F, Hornung P, Mechtler K, Westermann S","authors_abbrev":"Schleiffer A et al.","pubmed_publication_date":"06 May 2012","pubmed_entrez_date":"2012-05-08","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC18E5.03c","SPBC800.13","YFR046C","YPR046W","YJR135C","YDR374W-A","YGR179C","HGNC:32933","SPCC1235.07","SPBC21.01","SPCC1393.04","SPBP8B7.12c","SPAC4F10.12","SPAC1783.03","SPAC17G8.15","YDR383C","YBR211C","YPL018W","YBR107C","HGNC:21488","HGNC:29479","HGNC:21348"],"gene_count":9,"ltp_gene_count":0},{"uniquename":"PMID:18225957","title":"Nuc2p, a subunit of the anaphase-promoting complex, inhibits septation initiation network following cytokinesis in fission yeast.","citation":"PLoS Genet 2008 Jan;4(1):e17","abstract":"In most cell types, mitosis and cytokinesis are tightly coupled such that cytokinesis occurs only once per cell cycle. The fission yeast Schizosaccharomyces pombe divides using an actomyosin-based contractile ring and is an attractive model for the study of the links between mitosis and cytokinesis. In fission yeast, the anaphase-promoting complex/cyclosome (APC/C) and the septation initiation network (SIN), a spindle pole body (SPB)-associated GTPase-driven signaling cascade, function sequentially to ensure proper coordination of mitosis and cytokinesis. Here, we find a novel interplay between the tetratricopeptide repeat (TPR) domain-containing subunit of the APC/C, Nuc2p, and the SIN, that appears to not involve other subunits of the APC/C. Overproduction of Nuc2p led to an increase in the presence of multinucleated cells, which correlated with a defect in actomyosin ring maintenance and localization of the SIN component protein kinases Cdc7p and Sid1p to the SPBs, indicative of defective SIN signaling. Conversely, loss of Nuc2p function led to increased SIN signaling, characterized by the persistent localization of Cdc7p and Sid1p on SPBs and assembly of multiple actomyosin rings and division septa. Nuc2p appears to function independently of the checkpoint with FHA and ring finger (CHFR)-related protein Dma1p, a known inhibitor of the SIN in fission yeast. Genetic and biochemical analyses established that Nuc2p might influence the nucleotide state of Spg1p GTPase, a key regulator of the SIN. We propose that Nuc2p, by inhibiting the SIN after cell division, prevents further deleterious cytokinetic events, thereby contributing to genome stability.","doi":"10.1371/journal.pgen.0040017","authors":"Chew TG, Balasubramanian MK","authors_abbrev":"Chew TG et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2008-01-30","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.06c","SPAC17C9.01c","SPAC17G8.10c","SPBC21.06c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:21826257","title":"Contribution of Alanine-76 and Serine Phosphorylation in α-Synuclein Membrane Association and Aggregation in Yeasts.","citation":"Parkinsons Dis 2011;2011:392180","abstract":"In Parkinson's disease (PD), misfolded and aggregated α-synuclein protein accumulates in degenerating midbrain dopaminergic neurons. The amino acid alanine-76 in α-synuclein and phosphorylation at serine-87 and serine-129 are thought to regulate its aggregation and toxicity. However, their exact contributions to α-synuclein membrane association are less clear. We found that α-synuclein is indeed phosphorylated in fission yeast and budding yeast, the two models that we employed for assessing α-synuclein aggregation and membrane association properties, respectively. Surprisingly, blocking serine phosphorylation (S87A, S129A, and S87A/S129A) or mimicking it (S87D, S129D) altered α-synuclein aggregation in fission yeast. Either blocking or mimicking this phosphorylation increased endomembrane association in fission yeast, but only mimicking it decreased plasma membrane association in budding yeast. Polar substitution mutations of alanine-76 (A76E and A76R) decreased α-synuclein membrane association in budding yeast and decreased aggregation in fission yeast. These yeast studies extend our understanding of serine phosphorylation and alanine-76 contributions to α-synuclein aggregation and are the first to detail their impact on α-synuclein's plasma membrane and endomembrane association.","doi":"10.4061/2011/392180","authors":"Fiske M, Valtierra S, Solvang K, Zorniak M, White M, Herrera S, Konnikova A, Brezinsky R, Debburman S","authors_abbrev":"Fiske M et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-08-10","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39413787","title":"Kinesin-5/Cut7 C-terminal tail phosphorylation is essential for microtubule sliding force and bipolar mitotic spindle assembly.","citation":"Curr Biol 2024 Oct 15;","abstract":"Kinesin-5 motors play an essential role during mitotic spindle assembly in many organisms 1  ,  2  ,  3  ,  4  ,  5  ,  6  ,  7  ,  8  ,  9  ,  10  ,  11 : they crosslink antiparallel spindle microtubules, step toward plus ends, and slide the microtubules apart. 12  ,  13  ,  14  ,  15  ,  16  ,  17  This activity separates the spindle poles and chromosomes. Kinesin-5s are not only plus-end-directed but can walk or be carried toward MT minus ends, 18  ,  19  ,  20  ,  21  ,  22  ,  23  ,  24  ,  25  ,  26  ,  27  ,  28  ,  29  ,  30  ,  31  ,  32  ,  33  ,  34  where they show enhanced localization. 3  ,  5  ,  7  ,  27  ,  29  ,  32  The kinesin-5 C-terminal tail interacts with and regulates the motor, affecting structure, motility, and sliding force of purified kinesin-5 35  ,  36  ,  37  along with motility and spindle assembly in cells. 27  ,  38  ,  39  The tail contains phosphorylation sites, particularly in the conserved BimC box. 6  ,  7  ,  40  ,  41  ,  42  ,  43  ,  44  Nine mitotic tail phosphorylation sites were identified in the kinesin-5 motor of the fission yeast Schizosaccharomyces pombe, 45  ,  46  ,  47  ,  48  suggesting that multi-site phosphorylation may regulate kinesin-5s. Here, we show that mutating all nine sites to either alanine or glutamate causes temperature-sensitive lethality due to a failure of bipolar spindle assembly. We characterize kinesin-5 localization and sliding force in the spindle based on Cut7-dependent microtubule minus-end protrusions in cells lacking kinesin-14 motors. 39  ,  49  ,  50  ,  51  ,  52  Imaging and computational modeling show that Cut7p simultaneously moves toward the minus ends of protrusion MTs and the plus ends of spindle midzone MTs. Phosphorylation mutants show dramatic decreases in protrusions and sliding force. Comparison to a model of force to create protrusions suggests that tail truncation and phosphorylation mutants decrease Cut7p sliding force similarly to tail-truncated human Eg5. 36  Our results show that C-terminal tail phosphorylation is required for kinesin-5/Cut7 sliding force and bipolar spindle assembly in fission yeast.","doi":"10.1016/j.cub.2024.08.035","authors":"Jones MH, Gergely ZR, Steckhahn D, Zhou B, Betterton MD","authors_abbrev":"Jones MH et al.","pubmed_publication_date":"15 Oct 2024","pubmed_entrez_date":"2024-10-16","publication_year":"2024","canto_session_key":"be405bbd6ebccf13","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-10-17 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17515930","title":"Rad3-dependent phosphorylation of the checkpoint clamp regulates repair-pathway choice.","citation":"Nat Cell Biol 2007 Jun;9(6):691-7","abstract":"When replication forks collapse, Rad3 phosphorylates the checkpoint-clamp protein Rad9 in a manner that depends on Thr 225, a residue within the PCNA-like domain. The physiological function of Thr 225-dependent Rad9 phosphorylation, however, remains elusive. Here, we show that Thr 225-dependent Rad9 phosphorylation by Rad3 regulates DNA repair pathways. A rad9(T225C) mutant induces a translesion synthesis (TLS)-dependent high spontaneous mutation rate and a hyper-recombination phenotype. Consistent with this, Rad9 coprecipitates with the post-replication repair protein Mms2. This interaction is dependent on Rad9 Thr 225 and is enhanced by DNA damage. Genetic analyses indicate that Thr 225-dependent Rad9 phosphorylation prevents inappropriate Rhp51-dependent recombination, potentially by redirecting the repair through a Pli1-mediated sumoylation pathway into the error-free branch of the Rhp6 repair pathway. Our findings reveal a new mechanism by which phosphorylation of Rad9 at Thr 225 regulates the choice of repair pathways for maintaining genomic integrity during the cell cycle.","authors":"Kai M, Furuya K, Paderi F, Carr AM, Wang TS","authors_abbrev":"Kai M et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-05-23","publication_year":"2007","canto_session_key":"bfee12214ebdf8f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-09 13:49:39","canto_approved_date":"2021-12-29 21:58:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-23 10:55:19","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC688.10","SPAC664.07c","SPBC1734.06","SPAC4H3.05","SPCC338.05c","SPAC644.14c","SPBC336.01","SPBC16A3.11","SPAC1687.05","SPAC3C7.03c","SPBC16D10.09","SPCC553.07c"],"gene_count":13,"ltp_gene_count":11,"approved_date":"2018-04-09"},{"uniquename":"PMID:17531813","title":"Cdc18 enforces long-term maintenance of the S phase checkpoint by anchoring the Rad3-Rad26 complex to chromatin.","citation":"Mol Cell 2007 May 25;26(4):553-63","abstract":"DNA replication is initiated by recruitment of Cdc18 to origins. During S phase, CDK-dependent destruction of Cdc18 occurs. We show that when DNA replication stalls, Cdc18 persists in a chromatin-bound complex including the checkpoint kinases Rad3 and Rad26. Rad26 directly binds Cdc18 and is required for Rad3 recruitment to chromatin. Depletion of Cdc18 when DNA replication is stalled leads to release of Rad3 and Rad26 from chromatin and entry into an aberrant mitosis even though replication intermediates can still be detected. These findings indicate that Cdc18 plays a pivotal role in checkpoint maintenance by anchoring the Rad3-Rad26 complex to chromatin. Cdc18 persistence during DNA-replication arrest requires the S phase checkpoint that inhibits the S phase CDK. We propose that S phase arrest activates the S phase checkpoint blocking mitosis onset and inhibiting Cdc18 degradation, and that the stabilized Cdc18, in turn, anchors Rad3 to chromatin to ensure long-term checkpoint maintenance.","authors":"Hermand D, Nurse P","authors_abbrev":"Hermand D et al.","pubmed_publication_date":"25 May 2007","pubmed_entrez_date":"2007-05-29","publication_year":"2007","canto_session_key":"c396e950a0cdf1ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-12-05 15:38:04","canto_approved_date":"2026-06-26 08:18:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-11-10 11:44:43","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":24,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.08","SPCC18B5.11c","SPBC14C8.07c","SPBC1718.01","SPBC216.05","SPAPB2B4.03","SPBC582.03","SPBC428.18","SPAC24H6.05","SPBC11B10.09","SPAC4D7.03"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2017-12-05"},{"uniquename":"PMID:12840005","title":"Complex mechanism of site-specific DNA replication termination in fission yeast.","citation":"EMBO J 2003 Jul 01;22(13):3431-40","abstract":"A site-specific replication terminator, RTS1, is present at the Schizosaccharomyces pombe mating-type locus mat1. RTS1 regulates the direction of replication at mat1, optimizing mating-type switching that occurs as a replication-coupled recombination event. Here we show that RTS1 contains two cis-acting sequences that cooperate for efficient replication termination. First, a sequence of approximately 450 bp containing four repeated 55 bp motifs is essential for function. Secondly, a purine-rich sequence of approximately 60 bp without intrinsic activity, located proximal to the repeats, acts cooperatively to increase barrier activity 4-fold. Our data suggest that the trans-acting factors rtf1p and rtf2p act through the repeated motifs and the purine-rich element, respectively. Thus, efficient site-specific replication termination at RTS1 occurs by a complex mechanism involving several cis-acting sequences and trans-acting factors. Interestingly, RTS1 displays similarities to mammalian rDNA replication barriers.","authors":"Codlin S, Dalgaard JZ","authors_abbrev":"Codlin S et al.","pubmed_publication_date":"01 Jul 2003","pubmed_entrez_date":"2003-07-04","publication_year":"2003","canto_session_key":"c8e6356a39f3ee63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-12 14:19:26","canto_approved_date":"2024-04-09 09:57:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-12 14:19:13","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.06c","SPAC22F8.07c","SPBC30D10.04","SPAC1D4.09c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-04-12"},{"uniquename":"PANTHER:PTHR13396","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:18537","HGNC:17592","SPAC328.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24312672","title":"A quality control mechanism linking meiotic success to release of ascospores.","citation":"PLoS One 2013;8(12):e82758","abstract":"Eukaryotic organisms employ a variety of mechanisms during meiosis to assess and ensure the quality of their gametes. Defects or delays in successful meiotic recombination activate conserved mechanisms to delay the meiotic divisions, but many multicellular eukaryotes also induce cell death programs to eliminate gametes deemed to have failed during meiosis. It is generally thought that yeasts lack such mechanisms. Here, we show that in the fission yeast Schizosaccharomyces pombe, defects in meiotic recombination lead to the activation of a checkpoint that is linked to ascus wall endolysis--the process by which spores are released in response to nutritional cues for subsequent germination. Defects in meiotic recombination are sensed as unrepaired DNA damage through the canonical ATM and ATR DNA damage response kinases, and this information is communicated to the machinery that stimulates ascus wall breakdown. Viability of spores that undergo endolysis spontaneously is significantly higher than that seen upon chemical endolysis, demonstrating that this checkpoint contributes to a selective mechanism for the germination of high quality progeny. These results provide the first evidence for the existence of a checkpoint linking germination to meiosis and suggest that analysis solely based on artificial, enzymatic endolysis bypasses an important quality control mechanism in this organism and potentially other ascomycota, which are models widely used to study meiosis.","doi":"10.1371/journal.pone.0082758","authors":"Guo H, King MC","authors_abbrev":"Guo H et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-12-07","publication_year":"2013","canto_session_key":"fc977dd225947500","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4G3.05c","SPAC17A5.11","SPCC23B6.03c","SPBC216.05","SPAC3A11.05c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:22495024","title":"Processing peptidases in mitochondria and chloroplasts.","citation":"Biochim Biophys Acta 2013 Feb;1833(2):360-70","abstract":"Most of the mitochondrial and chloroplastic proteins are nuclear encoded and synthesized in the cytosol as precursor proteins with N-terminal extensions called targeting peptides. Targeting peptides function as organellar import signals, they are recognized by the import receptors and route precursors through the protein translocons across the organellar membranes. After the fulfilled function, targeting peptides are proteolytically cleaved off inside the organelles by different processing peptidases. The processing of mitochondrial precursors is catalyzed in the matrix by the Mitochondrial Processing Peptidase, MPP, the Mitochondrial Intermediate Peptidase, MIP (recently called Octapeptidyl aminopeptidase 1, Oct1) and the Intermediate cleaving peptidase of 55kDa, Icp55. Furthermore, different inner membrane peptidases (Inner Membrane Proteases, IMPs, Atp23, rhomboids and AAA proteases) catalyze additional processing functions, resulting in intra-mitochondrial sorting of proteins, the targeting to the intermembrane space or in the assembly of proteins into inner membrane complexes. Chloroplast targeting peptides are cleaved off in the stroma by the Stromal Processing Peptidase, SPP. If the protein is further translocated to the thylakoid lumen, an additional thylakoid-transfer sequence is removed by the Thylakoidal Processing Peptidase, TPP. Proper function of the D1 protein of Photosystem II reaction center requires its C-terminal processing by Carboxy-terminal processing protease, CtpA. Both in mitochondria and in chloroplasts, the cleaved targeting peptides are finally degraded by the Presequence Protease, PreP. The organellar proteases involved in precursor processing and targeting peptide degradation constitute themselves a quality control system ensuring the correct maturation and localization of proteins as well as assembly of protein complexes, contributing to sustenance of organelle functions. Dysfunctions of several mitochondrial processing proteases have been shown to be associated with human diseases. This article is part of a Special Issue entitled: Protein Import and Quality Control in Mitochondria and Plastids.","doi":"10.1016/j.bbamcr.2012.03.012","authors":"Teixeira PF, Glaser E","authors_abbrev":"Teixeira PF et al.","pubmed_publication_date":"Feb 2013","pubmed_entrez_date":"2012-04-13","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC12B10.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37956308","title":"Topoisomerase 1 facilitates nucleosome reassembly at stress genes during recovery.","citation":"Nucleic Acids Res 2023 Dec 11;51(22):12161-12173","abstract":"Chromatin remodeling is essential to allow full development of alternative gene expression programs in response to environmental changes. In fission yeast, oxidative stress triggers massive transcriptional changes including the activation of hundreds of genes, with the participation of histone modifying complexes and chromatin remodelers. DNA transcription is associated to alterations in DNA topology, and DNA topoisomerases facilitate elongation along gene bodies. Here, we test whether the DNA topoisomerase Top1 participates in the RNA polymerase II-dependent activation of the cellular response to oxidative stress. Cells lacking Top1 are resistant to H2O2 stress. The transcriptome of Δtop1 strain was not greatly affected in the absence of stress, but activation of the anti-stress gene expression program was more sustained than in wild-type cells. Top1 associated to stress open reading frames. While the nucleosomes of stress genes are partially and transiently evicted during stress, the chromatin configuration remains open for longer times in cells lacking Top1, facilitating RNA polymerase II progression. We propose that, by removing DNA tension arising from transcription, Top1 facilitates nucleosome reassembly and works in synergy with the chromatin remodeler Hrp1 as opposing forces to transcription and to Snf22 / Hrp3 opening remodelers.","doi":"10.1093/nar/gkad1066","authors":"Vega M, Barrios R, Fraile R, de Castro Cogle K, Castillo D, Anglada R, Casals F, Ayté J, Lowy-Gallego E, Hidalgo E","authors_abbrev":"Vega M et al.","pubmed_publication_date":"11 Dec 2023","pubmed_entrez_date":"2023-11-13","publication_year":"2023","canto_session_key":"a64204abb2ff60b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Montserrat Vega","canto_first_approved_date":"2025-01-01 10:03:43","canto_approved_date":"2025-09-04 12:46:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-30 09:16:36","canto_added_date":"2023-11-14 00:25:04","annotation_curators":[{"name":"Montserrat Vega","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1703.14c","SPCC1620.14c","SPAC1783.05","SPAC3G6.01","SPCC1442.10c","SPCC757.07c","SPBC106.02c","SPAP8A3.04c","SPBC29B5.01"],"gene_count":9,"ltp_gene_count":4,"approved_date":"2025-01-01"},{"uniquename":"PMID:34279742","title":"Ancestry analysis indicates two different sets of essential genes in eukaryotic model species.","citation":"Funct Integr Genomics 2021 Jul;21(3-4):523-531","abstract":"Essential genes are so-called because they are crucial for organism perpetuation. Those genes are usually related to essential functions to cellular metabolism or multicellular homeostasis. Deleterious alterations on essential genes produce a spectrum of phenotypes in multicellular organisms. The effects range from the impairment of the fertilization process, disruption of fetal development, to loss of reproductive capacity. Essential genes are described as more evolutionarily conserved than non-essential genes. However, there is no consensus about the relationship between gene essentiality and gene age. Here, we identified essential genes in five model eukaryotic species (Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melanogaster, Caenorhabditis elegans, and Mus musculus) and estimate their evolutionary ancestry and their network properties. We observed that essential genes, on average, are older than other genes in all species investigated. The relationship of network properties and gene essentiality convey with previous findings, showing essential genes as important nodes in biological networks. As expected, we also observed that essential orthologs shared by the five species evaluated here are old. However, all the species evaluated here have a specific set of young essential genes not shared among them. Additionally, these two groups of essential genes are involved with distinct biological functions, suggesting two sets of essential genes: (i) a set of old essential genes common to all the evaluated species, regulating basic cellular functions, and (ii) a set of young essential genes exclusive to each species, which perform specific essential functions in each species.","doi":"10.1007/s10142-021-00794-9","authors":"de Souza ID, Reis CF, Morais DAA, Fernandes VGS, Cavalcante JVF, Dalmolin RJS","authors_abbrev":"de Souza ID et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-07-19","publication_year":"2021","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-07-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8462844","title":"Marker effects of G to C transversions on intragenic recombination and mismatch repair in Schizosaccharomyces pombe.","citation":"Genetics 1993 Apr;133(4):825-35","abstract":"G to C transversion mutations show very strong allele-specific marker effects on the frequency of wild-type recombinants in intragenic two-factor crosses. Here we present a detailed study of the marker effect of one representative, the ade6-M387 mutation of Schizosaccharomyces pombe. Crosses of M387 with other mutations at varying distance reveal highly increased prototroph frequencies in comparison with the C to T transition mutation ade6-51 (control without any known marker effect) located four nucleotides from M387. The marker effect of M387 is strongest (> 40-fold) for crosses with mutations less than 15 nucleotides from M387. It decreases to an intermediate level (5-10-fold) in crosses with mutations located 25-150 base pairs from M387/51 and is very low in crosses with mutations beyond 200 base pairs. On the basis of these results and the quantitation of the low efficiency of C/C mismatch repair presented in the accompanying publication we propose the existence of at least two different types of mechanisms for base mismatch repair in fission yeast. The major system is suggested to recognize all base mismatches except C/C with high efficiency and to generate long excision tracts (approximately 100 nucleotides unidirectionally). The minor system is proposed to recognize all base mismatches including C/C with low and variable efficiency and to have short excision tracts (approximately 10 nucleotides unidirectionally). We estimate from the M387 marker effect that the minor system accounts for approximately 1-8% repair of non-C/C mismatches (depending on the nature of the mutation) in fission yeast meiosis.","authors":"Schär P, Kohli J","authors_abbrev":"Schär P et al.","pubmed_publication_date":"Apr 1993","pubmed_entrez_date":"1993-04-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17059860","title":"De novo cholesterol synthesis at the crossroads of adaptive response to extracellular stress through SREBP.","citation":"Biochimie 2007 Feb;89(2):260-4","abstract":"Cell sterol supply is subjected to tight negative feedback regulation through the SREBP pathway. Upon cholesterol depletion, SREBP transcription factors become activated by cleavage of a membrane bound precursor form, which stimulates the expression of the genes encoding proteins of the cholesterol synthesis pathway. In this paper, we discuss two situations of extracellular stress (hypoxia and heat shock) in which the cholesterol synthesis pathway and SREBPs are directly impacted to generate an adaptive response to cell damage. On one hand, the lack of oxygen in fission yeast Saccharomyces pombe induces a drop in cholesterol synthesis which in turn activates SREBP-mediated transcription. The presence of genes involved in the anaerobic growth program among SREBP target genes in fission yeast, indicates that SREBP behaves as an oxygen sensor, required for adaptive growth in low oxygen. On the other hand, upon heat shock in mammalian cells, SREBP-responsive heat shock proteins have been characterized, which were able to upregulate sterol synthesis by targeting the activity of HMG-CoA reductase, the rate limiting enzyme in this pathway. Although not yet proven, high rates of sterol synthesis can be viewed as an adaptive response to correct structural membrane damage and bilayer fluidification induced by thermal stress. Together these situations illustrate how the highly regulated SREBP pathway for the control of sterol synthesis can be used to achieve cell adaptive responses to extracellular stresses.","authors":"Robichon C, Dugail I","authors_abbrev":"Robichon C et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2006-10-25","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010093","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2157626","title":"Isolation and characterization of mutants constitutive for expression of the fbp1 gene of Schizosaccharomyces pombe.","citation":"Genetics 1990 Apr;124(4):807-16","abstract":"Transcription of the fbp1 gene of Schizosaccharomyces pombe, encoding fructose-1,6-bisphosphatase, is glucose repressible. We have constructed two hybrid genes, containing the fbp1 promoter, that allow selection for mutations that alter transcriptional regulation of fbp1. Strains carrying fbp1-ura4 and fbp1-lacZ fusions are phenotypically Ura-, resistant to 5-fluoro-orotic acid, and express a low level of beta-galactosidase activity when grown under repressing conditions (8% glucose). By selecting for Ura+ strains grown under repressing conditions, we have isolated 187 independent mutants that constitutively express the fbp1-ura4 fusion. These mutants identify ten complementation groups that represent ten unlinked git (glucose insensitive transcription) genes. The git gene products are required in trans for glucose repression of expression from the fbp1 promoter since these mutations also alter expression of the fbp1-lacZ fusion. We have shown that transcription of the wild type fbp1 gene in most git mutants is elevated to a level consistent with the increased expression of the fbp1-lacZ hybrid gene. Mutations in some git genes confer additional phenotypes such as slow growth, temperature-sensitive lethality and reduced spore viability. Therefore, some of these genes are likely to encode factors that are of general importance for S. pombe transcription.","authors":"Hoffman CS, Winston F","authors_abbrev":"Hoffman CS et al.","pubmed_publication_date":"Apr 1990","pubmed_entrez_date":"1990-04-01","publication_year":"1990","canto_session_key":"beb013202ef91cd2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-12-21 03:07:46","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-02-16 22:39:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.14c","SPAC926.04c","SPBC19C7.03","SPBC32H8.07","SPBC106.10","SPBC36.12c","SPBC21C3.20c","SPAC23H3.13c","SPBC9B6.08","SPCC1753.02c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2012-02-16"},{"uniquename":"PMID:3684587","title":"Sequence of the cDNA for one acidic ribosomal protein of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1987 Nov 11;15(21):9089","abstract":"","authors":"Beltrame M, Bianchi ME","authors_abbrev":"Beltrame M et al.","pubmed_publication_date":"11 Nov 1987","pubmed_entrez_date":"1987-11-11","publication_year":"1987","canto_session_key":"93d7e812efdb51f5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 14:50:48","canto_approved_date":"2019-01-07 14:50:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 14:50:42","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:30602528","title":"Glucose starvation triggers filamentous septin assemblies in an  S. pombe  septin-2 deletion mutant.","citation":"Biol Open 2019 Jan 02;8(1)","abstract":"Using correlative light and electron microscopy (CLEM), we studied the intracellular organization by of glucose-starved fission yeast cells ( Schizosaccharomyces pombe ) with regards to the localization of septin proteins throughout the cytoplasm. Thereby, we found that for cells carrying a deletion of the gene encoding septin-2 (spn2Δ), starvation causes a GFP-tagged version of septin-3 (spn3-GFP) and family members, to assemble into a single, prominent filamentous structure. It was previously shown that during exponential growth, spn2Δ cells form septin-3 polymers. However, the polymers we observed during exponential growth are different from the spn3p-GFP structure we observed in starved cells. Using CLEM, in combination with anti-GFP immunolabeling on plastic-sections, we could assign spn3p-GFP to the filaments we have found in EM pictures. Besides septin-3, these filamentous assemblies most likely also contain septin-1 as an RFP-tagged version of this protein forms a very similar structure in starved spn2Δ cells. Our data correlate phase-contrast and fluorescence microscopy with electron micrographs of plastic-embedded cells, and further on with detailed views of tomographic 3D reconstructions. Cryo-electron microscopy of spn2Δ cells in vitrified sections revealed a very distinct overall morphology of the spn3p-GFP assembly. The fine-structured, regular density pattern suggests the presence of assembled septin-3 filaments that are clearly different from F-actin bundles. Furthermore, we found that starvation causes substantial mitochondria fission, together with massive decoration of their outer membrane by ribosomes.","doi":"10.1242/bio.037622","authors":"Liu M, Heimlicher MB, Bächler M, Ibeneche-Nnewihe CC, Florin EL, Brunner D, Hoenger A","authors_abbrev":"Liu M et al.","pubmed_publication_date":"02 Jan 2019","pubmed_entrez_date":"2019-01-04","publication_year":"2019","canto_session_key":"5f9a8c2e3ed611f2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-01-05 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000118","title":"TreeGrafter-generated GO annotations","abstract":"TreeGrafter is a software tool for annotating protein sequences using pre-annotated PANTHER phylogenetic trees. TreeGrafter takes an input query protein sequence, finds the best matching homologous family, and then grafts it to the best location in the tree. It then annotates the query sequence by propagating annotations from the appropriate ancestral node(s) in the reference tree, which were manually annotated using the PAN-GO method (see GOREF_0000033). This method is integrated into InterProScan, which produces annotations to millions of genes across tens of thousands of organisms.","authors":"Haiming Tang, Dustin Ebert, Matthias Blum, Robert Finn, Paul Thomas ","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9528784","title":"The Schizosaccharomyces pombe mei4+ gene encodes a meiosis-specific transcription factor containing a forkhead DNA-binding domain.","citation":"Mol Cell Biol 1998 Apr;18(4):2118-29","abstract":"The mei4+ gene of the fission yeast Schizosaccharomyces pombe was cloned by functional complementation. The mei4 disruptant failed to complete meiosis-I but could proliferate normally. mei4+ was transcribed only in meiosis-proficient diploid cells after premeiotic DNA replication. The mei4+ open reading frame encodes a 57-kDa serine-rich protein comprised of 517 amino acids with a forkhead/HNF3 DNA-binding domain in the amino-terminal region. Transcription of spo6+, a gene required for sporulation, was dependent on the mei4+ function. Two copies of the GTAAAYA consensus sequence, proposed as the binding site for human forkhead proteins, were found in the promoter region of spo6+. A gel mobility shift assay demonstrated the sequence-dependent binding of the GST-Mei4 forkhead domain fusion protein to DNA fragments with one of the consensus elements. Deletion of this consensus element from the spo6 promoter abolished the transcription of spo6+ and resulted in a sporulation deficiency. One-hybrid assay of Mei4 which was fused to the Gal4 DNA-binding domain localized the transcriptional activation domain in the C-terminal 140 amino acids of Mei4. These results indicate that Mei4 functions as a meiosis-specific transcription factor of S. pombe.","authors":"Horie S, Watanabe Y, Tanaka K, Nishiwaki S, Fujioka H, Abe H, Yamamoto M, Shimoda C","authors_abbrev":"Horie S et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-04-07","publication_year":"1998","canto_session_key":"07dd8e6bdc30211a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-04 11:31:33","canto_approved_date":"2023-06-20 09:10:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-05 10:52:46","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5D6.08c","SPBC32H8.11","SPMTR.02","SPBC1778.04"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2016-09-04"},{"uniquename":"PMID:8692811","title":"Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors.","citation":"Proc Natl Acad Sci U S A 1996 Jun 25;93(13):6308-13","abstract":"A large family of isoquinoline sulfonamide compounds inhibits protein kinases by competing with adenosine triphosphates(ATP), yet interferes little with the activity of other ATP-using enzymes such as ATPases and adenylate cyclases. One such compound, N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide (CK17), is selective for casein kinase-1 isolated from a variety of sources. Here we report the crystal structure of the catalytic domain of Schizosaccharomyces pombe casein kinase-1 complexed with CK17, refined to a crystallographic R-factor of 17.8% at 2.5 angstrom resolution. The structure provides new insights into the mechanism of the ATP-competing inhibition and the origin of their selectivity toward different protein kinases. Selectivity for protein kinases versus other enzymes is achieved by hydrophobic contacts and the hydrogen bond with isoquinoline ring. We propose that the hydrogen bond involving the ring nitrogen-2 atom of the isoquinoline must be preserved, but that the ring can flip depending on the chemical substituents at ring positions 5 and 8. Selectivity for individual members of the protein kinase family is achieved primarily by interactions with these substituents.","authors":"Xu RM, Carmel G, Kuret J, Cheng X","authors_abbrev":"Xu RM et al.","pubmed_publication_date":"25 Jun 1996","pubmed_entrez_date":"1996-06-25","publication_year":"1996","canto_session_key":"548cabd71c9a6463","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-30 19:16:54","canto_approved_date":"2020-01-17 19:44:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-30 19:16:43","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-30","pdb_entries":[{"pdb_id":"2csn","gene_chains":[{"gene_uniquename":"SPBC1347.06c","chain":"A","position":"2-298"}],"title":"BINARY COMPLEX OF CASEIN KINASE-1 WITH CKI7","entry_authors":"Xu R-M,Cheng X","entry_authors_abbrev":"Xu R-M et al.","reference_uniquename":"PMID:8692811","experimental_method":"X-ray","resolution":"2.5"}]},{"uniquename":"PMID:17466618","title":"A two-way street: LSD1 regulates chromatin boundary formation in S. pombe and Drosophila.","citation":"Mol Cell 2007 Apr 27;26(2):160-2","abstract":"Two recent studies in Molecular Cell (Lan et al., 2007; Rudolph et al., 2007) implicate histone demethylation by LSD1 in the regulation of boundaries between silenced and active chromatin domains in both fission yeast and flies, but by distinct mechanisms.","authors":"Chosed R, Dent SY","authors_abbrev":"Chosed R et al.","pubmed_publication_date":"27 Apr 2007","pubmed_entrez_date":"2007-05-01","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733413","title":"Live Cell Imaging of the  Schizosaccharomyces pombe  Sexual Life Cycle.","citation":"Cold Spring Harb Protoc 2017 Oct 03;2017(10):pdb.prot090225","abstract":"The fission yeast  Schizosaccharomyces pombe  is an invaluable model system for studying the principles that drive sexual differentiation and the meiotic cell division cycle. We describe a simple protocol for microscopic observation of the entire sexual life cycle that can be adapted to focus on specific stages of sexual differentiation. After growth to exponential phase in a nitrogen-rich medium, cell cultures are switched to a nitrogen-deprived medium until the population is enriched for the specific stage of the sexual lifecycle to be studied. Cells are then mounted in easily constructed customized agarose pad chambers for imaging.","doi":"10.1101/pdb.prot090225","authors":"Merlini L, Vjestica A, Dudin O, Bendezú F, Martin SG","authors_abbrev":"Merlini L et al.","pubmed_publication_date":"03 Oct 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1829424","title":"Characterization of a Schizosaccharomyces pombe morphological mutant altered in the galactomannan content.","citation":"FEMS Microbiol Lett 1991 Apr 15;63(2-3):263-7","abstract":"In a search for Schizosaccharomyces pombe mutants resistant to the antifungal agent papulacandin B, a morphological mutant was isolated. The mutant is round shaped in contrast to the rod shaped parental strain. This morphological defect segregated as a recessive Mendelian character and was not observed in other papulacandin B resistant mutants belonging to the same complementation group. The mutation mapped in the right arm of S. pombe chromosome III very close to pap1 marker. Mutant cell walls were more susceptible to alkali extraction and Novozyme degradation than those from the wild-type. A specific reduction in the cell wall galactomannan fraction was the only significant difference detected as compared to the wild-type strain. Levels of beta (1,3)-glucan and mannan synthases as well as other enzymic periplasmic mannoproteins were very similar in wild type and mutant strains.","authors":"Ribas JC, Roncero C, Rico H, Durán A","authors_abbrev":"Ribas JC et al.","pubmed_publication_date":"15 Apr 1991","pubmed_entrez_date":"1991-04-15","publication_year":"1991","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24487582","title":"Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells.","citation":"Nat Methods 2014 Mar;11(3):319-24","abstract":"Mass spectrometry (MS)-based proteomics typically employs multistep sample-preparation workflows that are subject to sample contamination and loss. We report an in-StageTip method for performing sample processing, from cell lysis through elution of purified peptides, in a single, enclosed volume. This robust and scalable method largely eliminates contamination or loss. Peptides can be eluted in several fractions or in one step for single-run proteome analysis. In one day, we obtained the largest proteome coverage to date for budding and fission yeast, and found that protein copy numbers in these cells were highly correlated (R(2) = 0.78). Applying the in-StageTip method to quadruplicate measurements of a human cell line, we obtained copy-number estimates for 9,667 human proteins and observed excellent quantitative reproducibility between replicates (R(2) = 0.97). The in-StageTip method is straightforward and generally applicable in biological or clinical applications.","doi":"10.1038/nmeth.2834","authors":"Kulak NA, Pichler G, Paron I, Nagaraj N, Mann M","authors_abbrev":"Kulak NA et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-02-04","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32710633","title":"Gcn2 eIF2α kinase mediates combinatorial translational regulation through nucleotide motifs and uORFs in target mRNAs.","citation":"Nucleic Acids Res 2020 Sep 18;48(16):8977-8992","abstract":"The protein kinase Gcn2 is a central transducer of nutritional stress signaling important for stress adaptation by normal cells and the survival of cancer cells. In response to nutrient deprivation, Gcn2 phosphorylates eIF2α, thereby repressing general translation while enhancing translation of specific mRNAs with upstream ORFs (uORFs) situated in their 5'-leader regions. Here we performed genome-wide measurements of mRNA translation during histidine starvation in fission yeast Schizosaccharomyces pombe. Polysome analyses were combined with microarray measurements to identify gene transcripts whose translation was up-regulated in response to the stress in a Gcn2-dependent manner. We determined that translation is reprogrammed to enhance RNA metabolism and chromatin regulation and repress ribosome synthesis. Interestingly, translation of intron-containing mRNAs was up-regulated. The products of the regulated genes include additional eIF2α kinase Hri2 amplifying the stress signaling and Gcn5 histone acetyl transferase and transcription factors, together altering genome-wide transcription. Unique dipeptide-coding uORFs and nucleotide motifs, such as '5'-UGA(C/G)GG-3', are found in 5' leader regions of regulated genes and shown to be responsible for translational control.","doi":"10.1093/nar/gkaa608","authors":"Chikashige Y, Kato H, Thornton M, Pepper W, Hilgers M, Cecil A, Asano I, Yamada H, Mori C, Brunkow C, Moravek C, Urano T, Singh CR, Asano K","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"18 Sep 2020","pubmed_entrez_date":"2020-07-26","publication_year":"2020","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2020-07-29 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35618649","title":"Absence of the Rpb9 subunit of RNA polymerase II reduces the chronological life span in fission yeast.","citation":"J Basic Microbiol 2022 Aug;62(8):900-910","abstract":"Fission yeast RNA polymerase II consists of 12 subunits, Rpb1-Rpb12. Among these subunits, Rpb9 is the only subunit whose absence does not cause lethality under optimum growth conditions in fission yeast. However, an rpb9 null fission yeast mutant exhibits a slow-growth phenotype under optimum growth conditions and a defect in survival under environmental and genotoxic stress conditions. To further gain an understanding of its physiological roles, in the present study we have elucidated the role of the Rpb9 subunit in chronological aging using fission yeast as the model organism. Our results provide evidence that the absence of Rpb9 reduces the chronological life span in fission yeast. Our data further shows that lack of Rpb9 in fission yeast causes oxidative stress sensitivity and accumulation of reactive oxygen species during the stationary phase. Our domain mapping experiments have demonstrated that the Rpb9 region encompassing its amino-terminal zinc finger domain and the central linker region is important for the role of Rpb9 in chronological aging. Finally, we also show that expression of the budding yeast or human Rpb9 ortholog can functionally complement the reduced chronological life span phenotype of the fission yeast rpb9 deletion mutant. Taken together, our study has identified a new role of the Rpb9 subunit in chronological aging.","doi":"10.1002/jobm.202200036","authors":"Bhardwaj V, Sharma N","authors_abbrev":"Bhardwaj V et al.","pubmed_publication_date":"Aug 2022","pubmed_entrez_date":"2022-05-26","publication_year":"2022","canto_session_key":"f39eb1ef9c07924e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-08-25 10:06:04","canto_approved_date":"2022-08-25 10:06:04","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-07-06 07:46:49","canto_added_date":"2022-05-29 00:15:04","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":6,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPYUG7.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-08-25"},{"uniquename":"PMID:28162953","title":"Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex.","citation":"Structure 2017 Mar 07;25(3):434-445","abstract":"The membrane ring that equatorially circumscribes the nuclear pore complex (NPC) in the perinuclear lumen of the nuclear envelope is composed largely of Pom152 in yeast and its ortholog Nup210 (or Gp210) in vertebrates. Here, we have used a combination of negative-stain electron microscopy, nuclear magnetic resonance, and small-angle X-ray scattering methods to determine an integrative structure of the ∼120 kDa luminal domain of Pom152. Our structural analysis reveals that the luminal domain is formed by a flexible string-of-pearls arrangement of nine repetitive cadherin-like Ig-like domains, indicating an evolutionary connection between NPCs and the cell adhesion machinery. The 16 copies of Pom152 known to be present in the yeast NPC are long enough to form the observed membrane ring, suggesting how interactions between Pom152 molecules help establish and maintain the NPC architecture.","doi":"10.1016/j.str.2017.01.006","authors":"Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J","authors_abbrev":"Upla P et al.","pubmed_publication_date":"07 Mar 2017","pubmed_entrez_date":"2017-02-07","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.07","HGNC:30052"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38306987","title":"Understanding cytokinesis interaction by interaction.","citation":"Structure 2024 Feb 01;32(2):120-121","abstract":"In this issue of Structure, Hall et al. 1  investigate the binding modes of anillin-like Mid1. During cytokinesis, Mid1 connects the contractile ring to the plasma membrane. Using computer simulations, the authors demonstrated how this connection is established via the L3 loop of the C2 domain.","doi":"10.1016/j.str.2024.01.001","authors":"Larsen AH","authors_abbrev":"Larsen AH","pubmed_publication_date":"01 Feb 2024","pubmed_entrez_date":"2024-02-02","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-02-06 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010392","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11128980","title":"New concepts in fission yeast morphogenesis.","citation":"Philos Trans R Soc Lond B Biol Sci 2000 Jul 29;355(1399):873-7","abstract":"The ability to generate spatial form is a fundamental characteristic of all living organisms, which has been much studied by successive generations of developmental biologists. In recent years increasing numbers of cell biologists have turned their attention to the mechanisms by which cells generate their spatial form. These include the mechanisms that position components in different places within the cell, that specify the position of these components, and that generate the overall shape of these components. These problems are entirely analogous to those studied by developmental biologists, although usually at the level of the whole organism, organ or tissue. Because the organization of all cells is basically similar, it is possible that the concepts and the underlying molecular mechanisms of cell morphogenesis may be highly conserved. In this article we consider the generation of spatial form within the fission yeast cell, focusing on emerging new concepts, which may be applicable to the morphogenesis of other cells.","authors":"Brunner D, Nurse P","authors_abbrev":"Brunner D et al.","pubmed_publication_date":"29 Jul 2000","pubmed_entrez_date":"2000-12-29","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21441914","title":"ABC ATPase signature helices in Rad50 link nucleotide state to Mre11 interface for DNA repair.","citation":"Nat Struct Mol Biol 2011 Apr;18(4):423-31","abstract":"The Rad50 ABC-ATPase complex with Mre11 nuclease is essential for dsDNA break repair, telomere maintenance and ataxia telangiectasia-mutated kinase checkpoint signaling. How Rad50 affects Mre11 functions and how ABC-ATPases communicate nucleotide binding and ligand states across long distances and among protein partners are questions that have remained obscure. Here, structures of Mre11-Rad50 complexes define the Mre11 2-helix Rad50 binding domain (RBD) that forms a four-helix interface with Rad50 coiled coils adjoining the ATPase core. Newly identified effector and basic-switch helix motifs extend the ABC-ATPase signature motif to link ATP-driven Rad50 movements to coiled coils binding Mre11, implying an ~30-Å pull on the linker to the nuclease domain. Both RBD and basic-switch mutations cause clastogen sensitivity. Our new results characterize flexible ATP-dependent Mre11 regulation, defects in cancer-linked RBD mutations, conserved superfamily basic switches and motifs effecting ATP-driven conformational change, and they provide a unified comprehension of ABC-ATPase activities.","doi":"10.1038/nsmb.2038","authors":"Williams GJ, Williams RS, Williams JS, Moncalian G, Arvai AS, Limbo O, Guenther G, SilDas S, Hammel M, Russell P, Tainer JA","authors_abbrev":"Williams GJ et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2011-03-29","publication_year":"2011","canto_session_key":"7744c021aa35dd69","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-03-27 12:33:09","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-03-27 12:33:03","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":65,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.05","SPAC1556.01c","SPAC13C5.07","SPBC6B1.09c","SPBC543.03c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-03-27"},{"uniquename":"PMID:36799444","title":"Inner nuclear membrane proteins Lem2 and Bqt4 interact with different lipid synthesis enzymes in fission yeast.","citation":"J Biochem 2023 Jun 30;174(1):33-46","abstract":"The nuclear envelope (NE) is a double-membrane structure consisting of inner and outer membranes that spatially separate the nucleus from the cytoplasm, and its function is critical for cellular functions such as genome maintenance. In the fission yeast, Schizosaccharomyces pombe, the inner nuclear membrane proteins, Lem2 and Bqt4, play pivotal roles in maintaining the NE structure. We previously found that the double deletion of lem2+ and bqt4+ causes a synthetic lethal defect associated with severe NE rupture, and overexpression of Elo2, a solo very-long-chain fatty acid elongase, suppresses this defect by restoring the NE. However, the molecular basis of this restoration remains elusive. To address this, we identified Lem2- and Bqt4-binding proteins via immunoprecipitation and mass spectrometry in this study. Forty-five and 23 proteins were identified as Lem2- and Bqt4-binding proteins, respectively. Although these binding proteins partially overlapped, Lem2 and Bqt4 interacted with different types of lipid metabolic enzymes: Cho2, Ole1 and Erg11 for Lem2 and Cwh43 for Bqt4. These enzymes are known to be involved in various lipid synthesis processes, suggesting that Lem2 and Bqt4 may contribute to the regulation of lipid synthesis by binding to these enzymes.","doi":"10.1093/jb/mvad017","authors":"Hirano Y, Kinugasa Y, Kubota Y, Obuse C, Haraguchi T, Hiraoka Y","authors_abbrev":"Hirano Y et al.","pubmed_publication_date":"30 Jun 2023","pubmed_entrez_date":"2023-02-17","publication_year":"2023","canto_session_key":"705d6edbff5f2b70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Hirano","canto_first_approved_date":"2023-06-08 11:35:02","canto_approved_date":"2023-06-09 15:18:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-03 06:02:23","canto_added_date":"2023-02-18 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yasuhiro Hirano","community_curator":true,"annotation_count":72,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1709.05","SPBC2G5.01","SPBC16H5.02","SPAC18G6.05c","SPCC18.14c","SPAC13A11.02c","SPBC19C7.10","SPBC146.14c","SPAC926.09c","SPBC18H10.12c","SPBC839.08c","SPBC1105.02c","SPCC1840.03","SPAC1071.10c","SPBC17A3.05c","SPBC1271.02","SPBC8E4.01c","SPAC11D3.14c","SPAC1834.05","SPBP19A11.03c","SPBC18H10.03","SPBC26H8.03","SPAC13G6.02c","SPAC23C11.11","SPAC589.12","SPBC1604.08c","SPAC22G7.06c","SPBC646.07c","SPAC22A12.15c","SPBC1A4.08c","SPCC594.07c","SPBC14F5.03c","SPAC664.05","SPCC18B5.01c","SPBC4.07c","SPCC338.15","SPCC1795.11","SPCC162.09c","SPAC14C4.14","SPAC17A2.13c","SPAC926.04c","SPBC1685.14c","SPBP8B7.03c","SPCC962.03c","SPBC29A3.04","SPCC550.11","SPAC8E11.02c","SPCC417.08","SPAC1B1.03c","SPCC13B11.01","SPAC19A8.04","SPCC584.01c","SPCC1281.06c","SPAC18G6.10","SPCC622.18","SPBC1703.13c","SPBC18H10.02","SPBC1921.05","SPAC513.01c","SPCC1322.14c","SPAC1F8.07c","SPAC27F1.07","SPAC23A1.10"],"gene_count":63,"ltp_gene_count":62,"approved_date":"2023-06-08"},{"uniquename":"PMID:3084798","title":"The cloning and characterization of a RAS gene from Schizosaccharomyces pombe.","citation":"J Mol Evol 1986;23(1):41-51","abstract":"We have cloned and determined the complete nucleotide sequence of a RAS gene from the yeast Schizosaccharomyces pombe (SP-RAS). The putative RAS protein of 214 amino acids is encoded by two noncontiguous reading frames separated by an intron of 86 bp. The SP-RAS gene product shares extensive homology with the proteins of the Saccharomyces cerevisiae (SC), Dictyostelium, Drosophila, and human RAS genes in its N-terminal region but not in its C-terminal region. The extended C-terminal regions found in the SC-RAS genes have no counterpart in the SP-RAS gene. Thus the RAS genes of these two yeasts are structurally quite distinct. The SP-RAS sequence was expressed in vivo.","authors":"Nadin-Davis SA, Yang RC, Narang SA, Nasim A","authors_abbrev":"Nadin-Davis SA et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_session_key":"748caea752cefd89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-02 13:46:04","canto_approved_date":"2019-01-02 13:46:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 22:19:36","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-02"},{"uniquename":"PMID:24879348","title":"A protective role of methionine-R-sulfoxide reductase against cadmium in Schizosaccharomyces pombe.","citation":"J Microbiol 2014 Nov;52(11):976-81","abstract":"The Schizosaccharomyces pombe cells harboring the methionine- R-sulfoxide reductase (MsrB)-overexpressing recombinant plasmid pFMetSO exhibited better growth than vector control cells, when shifted into fresh medium containing cadmium chloride (abbreviated as Cd). Although both groups of cells contained enhanced reactive oxygen species (ROS) and nitric oxide (NO) levels in the presence of Cd, ROS and NO levels were significantly lower in the S. pombe cells harboring pFMetSO than in vector control cells. Conversely, the S. pombe cells harboring pFMetSO possessed higher total glutathione (GSH) levels and a greater reduced/oxidized GSH ratio than vector control cells under the same conditions.","doi":"10.1007/s12275-014-3512-7","authors":"Lim CJ, Jo H, Kim K","authors_abbrev":"Lim CJ et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-06-01","publication_year":"2014","canto_session_key":"9dfc76eb8e658bb4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-06-25 22:32:37","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-12 09:10:45","canto_added_date":"2014-06-06 13:10:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-12"},{"uniquename":"PMID:2381421","title":"Effects of seven different mutations in the pho1 gene on enzymatic activity, glycosylation and secretion of acid phosphatase in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1990 May;221(3):403-10","abstract":"Structural gene mutants of the cell-surface glycoprotein acid phosphatase of Schizosaccharomyces pombe were analysed to define structural determinants that are responsible for enzymatic activity, N-glycosylation and secretion. All seven defined mutations cause a single amino acid substitution in the mature acid phosphatase protein and destroy the enzymatic activity. The mutational lesions are distributed throughout the pho1 gene. A ser to phe substitution at position 349 abolishes enzymatic activity only and does not affect glycosylation and secretion. Two mutations create a new N-glycosylation site by substitution of pro at position 56 by phe and ser, respectively. This new site is apparently used in the mutants. Their core-glycosylated acid phosphatase is slightly larger than that of the wild type. Overglycosylation seems not to affect secretion. Four different mutations (a gly to asp substitution at position 281 and ser to phe substitutions at positions 150, 271 and 277) cause intracellular accumulation of enzymatically inactive core-glycosylated acid phosphatase precursor. These mutational lesions apparently block transport of acid phosphatase from the endoplasmic reticulum to the Golgi apparatus.","authors":"Schwaninger R, Dumermuth E, Schweingruber ME","authors_abbrev":"Schwaninger R et al.","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_session_key":"bfb811af6b3b85e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-15 14:14:16","canto_approved_date":"2021-10-19 14:51:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-06-07 09:43:30","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-11-15"},{"uniquename":"PMID:35406650","title":"Fission Yeast Autophagy Machinery.","citation":"Cells 2022 Mar 24;11(7)","abstract":"Autophagy is a conserved process that delivers cytoplasmic components to the vacuole/lysosome. It plays important roles in maintaining cellular homeostasis and conferring stress resistance. In the fission yeast  Schizosaccharomyces pombe , autophagy is important for cell survival under nutrient depletion and ER stress conditions. Experimental analyses of fission yeast autophagy machinery in the last 10 years have unveiled both similarities and differences in autophagosome biogenesis mechanisms between fission yeast and other model eukaryotes for autophagy research, in particular, the budding yeast  Saccharomyces cerevisiae . More recently, selective autophagy pathways that deliver hydrolytic enzymes, the ER, and mitochondria to the vacuole have been discovered in fission yeast, yielding novel insights into how cargo selectivity can be achieved in autophagy. Here, we review the progress made in understanding the autophagy machinery in fission yeast.","doi":"10.3390/cells11071086","authors":"Xu DD, Du LL","authors_abbrev":"Xu DD et al.","pubmed_publication_date":"24 Mar 2022","pubmed_entrez_date":"2022-04-12","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-04-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40346880","title":"Mechanical Coupling With the Nuclear Envelope Shapes the Schizosaccharomyces pombe Mitotic Spindle.","citation":"Cytoskeleton (Hoboken) 2025 May 10;","abstract":"The fission yeast Schizosaccharomyces pombe divides via closed mitosis, meaning that spindle elongation and chromosome segregation transpire entirely within the closed nuclear envelope. Both the spindle and nuclear envelope must undergo shape changes and exert varying forces on each other during this process. Previous work has demonstrated that nuclear envelope expansion (Yam, He, Zhang, Chiam, & Oliferenko, 2011; Mori & Oliferenko, 2020) and spindle pole body (SPB) embedding in the nuclear envelope are required for normal S. pombe mitosis, and mechanical modeling has described potential contributions of the spindle to nuclear morphology (Fang et al., 2020; Zhu et al., 2016). However, it is not yet fully clear how and to what extent the nuclear envelope and mitotic spindle each directly shape each other during closed mitosis. Here, we investigate this relationship by observing the behaviors of spindles and nuclei in live mitotic fission yeast following laser ablation. First, we characterize these dynamics in mitotic S. pombe nuclei with increased envelope tension, finding that nuclear envelope tension can both bend the spindle and slow elongation. Next, we directly probe the mechanical connection between spindles and nuclear envelopes by ablating each structure. We demonstrate that envelope tension can be relieved by severing spindles and that spindle compression can be relieved by rupturing the envelope. We interpret our experimental data via two quantitative models that demonstrate that fission yeast spindles and nuclear envelopes are a mechanical pair that can each shape the other's morphology.","doi":"10.1002/cm.22035","authors":"Begley MA, Mahoney T, Medina CP, Zareiesfandabadi P, Rapp MB, Tirfe M, LeBlanc SJ, Betterton MD, Elting MW","authors_abbrev":"Begley MA et al.","pubmed_publication_date":"10 May 2025","pubmed_entrez_date":"2025-05-10","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-05-11 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15780661","title":"Efficient conversion of 11-deoxycortisol to cortisol (hydrocortisone) by recombinant fission yeast Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2005 Apr;5(6-7):621-5","abstract":"Genetically engineered microorganisms are being increasingly used for the industrial production of complicated chemical compounds such as steroids; however, there have been few reports on the use of the fission yeast Schizosaccharomyces pombe for this purpose. We previously have demonstrated that this yeast is a unique host for recombinant expression of human CYP11B2 (aldosterone synthase), and here we report the functional production of human CYP11B1 (steroid 11beta-hydroxylase) in S. pombe using our new integration vector pCAD1. In the human adrenal, the mitochondrial cytochrome P450 enzyme CYP11B1 catalyses the conversion of 11-deoxycortisol to cortisol, a key reaction in cortisol biosynthesis that in addition is of fundamental interest for the technical synthesis of glucocorticoids. We observed that the endogenous mitochondrial electron transport system detected previously by us is capable of supplying this enzyme with the reducing equivalents necessary for steroid hydroxylation activity. Under optimised cultivation conditions the transformed yeasts show in vivo the inducible ability to efficiently and reliably convert deoxycortisol to cortisol at an average rate of 201 microM d(-1) over a period of 72h, the highest value published to date for this biotransformation.","authors":"Drăgan CA, Zearo S, Hannemann F, Bernhardt R, Bureik M","authors_abbrev":"Drăgan CA et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-03-23","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27738016","title":"RNA interference is essential for cellular quiescence.","citation":"Science 2016 Nov 11;354(6313)","abstract":"Quiescent cells play a predominant role in most organisms. Here we identify RNA interference (RNAi) as a major requirement for quiescence (G 0  phase of the cell cycle) in Schizosaccharomyces pombe RNAi mutants lose viability at G 0  entry and are unable to maintain long-term quiescence. We identified suppressors of G 0  defects in cells lacking Dicer (dcr1Δ), which mapped to genes involved in chromosome segregation, RNA polymerase-associated factors, and heterochromatin formation. We propose a model in which RNAi promotes the release of RNA polymerase in cycling and quiescent cells: (i) RNA polymerase II release mediates heterochromatin formation at centromeres, allowing proper chromosome segregation during mitotic growth and G 0  entry, and (ii) RNA polymerase I release prevents heterochromatin formation at ribosomal DNA during quiescence maintenance. Our model may account for the codependency of RNAi and histone H3 lysine 9 methylation throughout eukaryotic evolution.","authors":"Roche B, Arcangioli B, Martienssen RA","authors_abbrev":"Roche B et al.","pubmed_publication_date":"11 Nov 2016","pubmed_entrez_date":"2016-10-15","publication_year":"2016","canto_session_key":"93e1b181a0463890","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Benjamin Roche","canto_first_approved_date":"2021-02-11 16:02:43","canto_approved_date":"2026-06-26 08:40:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-09-25 05:54:36","canto_added_date":"2016-10-17 00:15:11","annotation_curators":[{"name":"Benjamin Roche","community_curator":true,"annotation_count":190,"orcid":"0000-0003-3912-6340","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4C3.05c","SPAC30D11.10","SPBC1198.11c","SPAC664.01c","SPCC11E10.08","SPCC970.07c","SPBC1105.11c","SPCC188.13c","SPCC736.11","SPCP31B10.03c","SPAC29E6.08","SPCC1259.03","SPBC428.08c","SPAC644.14c","SPAC17G8.13c","SPBC11C11.03","SPAC6F12.09","SPAC1834.04","SPBC16C6.10","SPBC2F12.13","SPBC8D2.04"],"gene_count":21,"ltp_gene_count":19,"approved_date":"2021-02-11"},{"uniquename":"PMID:17504808","title":"The Clr4 methyltransferase determines the subnuclear localization of the mating-type region in fission yeast.","citation":"J Cell Sci 2007 Jun 01;120(Pt 11):1935-43","abstract":"The genome has a non-random spatial distribution in the cell nucleus. In Schizosaccharomyces pombe, it has been shown that the centromeres, telomeres and the mating-type region localize to the nuclear membrane (NM), the former by attaching to the spindle pole body (SPB). In addition, reporter genes inserted into these areas are transcriptionally repressed because of the formation of specialized chromatin structures. Performing live cell analysis we found that in a wild-type strain the mating-type region was positioned in the proximity of the SPB, the location where the pericentromeric heterochromatin is also found. In a strain lacking the histone methyltransferase Clr4, crucial for the formation of heterochromatin, the mating-type region had a random localization in the nucleus. Moreover, in a strain in which the two boundary elements IR-L and IR-R had been deleted, the mating-type region was displaced from its position at the proximity of the SPB, but remained in the vicinity of the NM. Moreover, in all investigated strains with silencing deficiencies the distance between the mating-type region and the SPB increased. This result indicates a correlation between transcriptional derepression and displacement of the region. Two different models of how the mating-type chromatin is organized in the nucleus are discussed.","authors":"Alfredsson-Timmins J, Henningson F, Bjerling P","authors_abbrev":"Alfredsson-Timmins J et al.","pubmed_publication_date":"01 Jun 2007","pubmed_entrez_date":"2007-05-17","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38899956","title":"Gut mycobiome alterations in obesity in geographically different regions.","citation":"Gut Microbes 2024;16(1):2367297","abstract":"The gut fungi play important roles in human health and are involved in energy metabolism. This study aimed to examine gut mycobiome composition in obese subjects in two geographically different regions in China and to identify specific gut fungi associated with obesity. A total of 217 subjects from two regions with different urbanization levels [Hong Kong (HK): obese,  n  = 59; lean,  n  = 59; Kunming (KM): obese,  n  = 50; lean,  n  = 49. Mean body mass index (BMI) for obesity = 33.7] were recruited. We performed deep shotgun metagenomic sequencing on fecal samples to compare gut mycobiome composition and trophic functions in lean and obese subjects across these two regions. The gut mycobiome of obese subjects in both HK and KM were altered compared to those of lean subjects, characterized by a decrease in the relative abundance of  Nakaseomyces ,  Schizosaccharomyces pombe ,  Candida dubliniensis  and an increase in the abundance of  Lanchanceathermotolerans ,  Saccharomyces paradox ,  Parastagonospora nodorum  and  Myceliophthorathermophila . Reduced fungal - bacterial and fungal - fungal correlations as well as increased negative fungal-bacterial correlations were observed in the gut of obese subjects. Furthermore, the anti-obesity effect of fungus  S. pombe  was further validated using a mouse model. Supplementing high-fat diet-induced obese mice with the fungus for 12 weeks led to a significant reduction in body weight gain ( p  < 0.001), and an improvement in lipid and glucose metabolism compared to mice without intervention. In conclusion, the gut mycobiome composition and functionalities of obese subjects were altered. These data shed light on the potential of utilizing fungus-based therapeutics for the treatment of obesity.  S. pombe  may serve as a potential fungal probiotic in the prevention of diet-induced obesity and future human trials are needed.","doi":"10.1080/19490976.2024.2367297","authors":"Zhan H, Wan Y, Sun Y, Xu Z, Zhang F, Yang K, Zhu W, Cheung CP, Tang W, Ng EK, Wong SK, Yeoh YK, Kl Chan F, Miao Y, Zuo T, Zeng Z, Ng SC","authors_abbrev":"Zhan H et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-06-20","publication_year":"2024","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2024-06-20 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21297349","title":"Bfr1p is responsible for tributyltin resistance in Schizosaccharomyces pombe.","citation":"J Toxicol Sci 2011 Jan;36(1):117-20","abstract":"ATP-binding cassette (ABC) transporter plays an important role for resistance against xenobiotics. There are eleven ABC transporter genes in the genome of fission yeast Schizosaccharomyces pombe. We examined the role of ABC transporter against the toxicity of tributyltin chloride (TBT), a widespread environmental pollutant, in cell growth. Among individual ABC transporter mutants, the growth of a mutant deficient in Bfr1p, a plasma membrane-embedded transporter, was extremely sensitive to TBT. The lethal TBT concentration inducing 50% of cell death (LC(50)) was 25 µM for the parent strain and 10.2 µM for the bfr1∆ mutant. Thus, Bfr1p was responsible for TBT resistance in S. pombe.","authors":"Akiyama K, Iwaki T, Sugimoto N, Chardwiriyapreecha S, Kawano M, Nishimoto S, Sugahara T, Sekito T, Kakinuma Y","authors_abbrev":"Akiyama K et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2011-02-08","publication_year":"2011","canto_session_key":"4fc06348b3433ce3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-29 08:30:04","canto_approved_date":"2022-06-22 13:55:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-29 08:29:57","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.01c","SPCC663.03","SPBC9B6.09c","SPBC359.05","SPAC15A10.01","SPAC3F10.11c","SPAPB24D3.09c","SPBC25B2.02c","SPAC30.04c","SPAC9E9.12c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2014-08-29"},{"uniquename":"PMID:7019207","title":"An homologous in vitro assay for yeast nonsense suppressors.","citation":"J Biol Chem 1981 Jul 25;256(14):7298-304","abstract":"A cell-free translation system, from the yeast Saccharomyces cerevisiae, has been used to develop an in vitro assay for yeast UGA, ochre and amber suppressors. Amber suppression was assayed by read-through of the brome mosaic virus coat protein cistron UAG terminator. UGA suppression was assayed by read-through of the rabbit beta-globin UGA terminator and ochre suppression by read-through of the rabbit alpha-globin mRNA UAA terminator. Ochre suppression was increased 3-fold when the globin mRNA was heat denatured prior to translation; this was due to an increase in the synthesis of alpha-globin relative to beta-globin. Amber suppression was more efficient in vitro (46%) than ochre suppression (14%). UGA suppression was also highly efficient in vitro, reaching almost 100% using a purified UGA suppressor tRNA from Schizosaccharomyces pombe. Unfractionated yeast tRNA, from a sup+ strain, contained a tRNA species able to suppress UGA termination codons in vitro, but no tRNA species able to suppress either UAA or UAG was found. This homologous in vitro assay for yeast nonsense suppressors will allow, for the first time, an approach to the biochemical analysis of yeast mutants that modify the efficiency of nonsense suppression in vivo.","authors":"Tuite MF, Cox BS, McLaughlin CS","authors_abbrev":"Tuite MF et al.","pubmed_publication_date":"25 Jul 1981","pubmed_entrez_date":"1981-07-25","publication_year":"1981","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28054200","title":"The functions of the multi-tasking Pfh1 Pif1  helicase.","citation":"Curr Genet 2017 Aug;63(4):621-626","abstract":"Approximately, 1% of the genes in eukaryotic genomes encode for helicases, which make the number of helicases expressed in the cell considerably high. Helicases are motor proteins that participate in many central aspects of the nuclear and mitochondrial genomes, and based on their helicase motif conservation, they are divided into different helicase families. The Pif1 family of helicases is an evolutionarily conserved helicase family that is associated with familial breast cancer in humans. The Schizosaccharomyces pombe Pfh1 helicase belongs to the Pif1 helicase family and is a multi-tasking helicase that is important for replication fork progression through natural fork barriers, for G-quadruplex unwinding, and for Okazaki fragment maturation, and these activities are potentially shared by the human Pif1 helicase. This review discusses the known functions of the Pfh1 helicase, the study of which has led to a better understanding of nucleic acid metabolism in eukaryotes.","doi":"10.1007/s00294-016-0675-2","authors":"Sabouri N","authors_abbrev":"Sabouri N","pubmed_publication_date":"Aug 2017","pubmed_entrez_date":"2017-01-06","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-01-07 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC887.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10747044","title":"A recombination repair gene of Schizosaccharomyces pombe, rhp57, is a functional homolog of the Saccharomyces cerevisiae RAD57 gene and is phylogenetically related to the human XRCC3 gene.","citation":"Genetics 2000 Apr;154(4):1451-61","abstract":"To identify Schizosaccharomyces pombe genes involved in recombination repair, we identified seven mutants that were hypersensitive to both methyl methanesulfonate (MMS) and gamma-rays and that contained mutations that caused synthetic lethality when combined with a rad2 mutation. One of the mutants was used to clone the corresponding gene from a genomic library by complementation of the MMS-sensitive phenotype. The gene obtained encodes a protein of 354 amino acids whose sequence is 32% identical to that of the Rad57 protein of Saccharomyces cerevisiae. An rhp57 (RAD57 homolog of S. pombe) deletion strain was more sensitive to MMS, UV, and gamma-rays than the wild-type strain and showed a reduction in the frequency of mitotic homologous recombination. The MMS sensitivity was more severe at lower temperature and was suppressed by the presence of a multicopy plasmid bearing the rhp51 gene. An rhp51 rhp57 double mutant was as sensitive to UV and gamma-rays as an rhp51 single mutant, indicating that rhp51 function is epistatic to that of rhp57. These characteristics of the rhp57 mutants are very similar to those of S. cerevisiae rad57 mutants. Phylogenetic analysis suggests that Rhp57 and Rad57 are evolutionarily closest to human Xrcc3 of the RecA/Rad51 family of proteins.","authors":"Tsutsui Y, Morishita T, Iwasaki H, Toh H, Shinagawa H","authors_abbrev":"Tsutsui Y et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-04-04","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20H4.07","SPAC3G6.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8082193","title":"The ade4 gene of Schizosaccharomyces pombe: cloning, sequence and regulation.","citation":"Curr Genet 1994 May;25(5):465-8","abstract":"We report the isolation and sequence of the Schizosaccharomyces pombe ade4 gene which encodes the glutamine phosphoribosylpyrophosphate amidotransferase, the first enzyme of the purine nucleotide de-novo biosynthetic pathway. The enzyme contains 533 amino acids and its sequence exhibits homologies to the corresponding enzymes of Saccharomyces cerevisiae, Escherichia coli, Bacillus subtilis, chicken, rat, and human. In contrast to the situation in S. cerevisiae, adenine does not repress ade4 expression at the mRNA level and also other nutritional signals seem not to affect its expression.","authors":"Ludin KM, Hilti N, Schweingruber ME","authors_abbrev":"Ludin KM et al.","pubmed_publication_date":"May 1994","pubmed_entrez_date":"1994-05-01","publication_year":"1994","canto_session_key":"3f673f9d9e5ca973","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-05-21 12:06:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-20 07:58:16","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4D7.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-05-20"},{"uniquename":"PMID:12967011","title":"Enhancing ethanol tolerance of a self-flocculating fusant of Schizosaccharomyces pombe and Saccharomyces cerevisiae by Mg2+ via reduction in plasma membrane permeability.","citation":"Biotechnol Lett 2003 Jul;25(14):1191-4","abstract":"Mg2+ at 3.5 mM increased the tolerance of a self-flocculating fusant of Schizosaccharomyces pombe and Saccharomyces cerevisiae to ethanol. After 9 h of exposure to 20% (v/v) ethanol at 30 degrees C, all cells died whereas over 50% remained viable for the cells grown with Mg2+. The effect of Mg2+ is closely related to its ability to decrease plasma membrane permeability of cells subjected to ethanol stress.","authors":"Hu CK, Bai FW, An LJ","authors_abbrev":"Hu CK et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-09-12","publication_year":"2003","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1100491","title":"The isolation of protoplasts of the fission yeast Schizosaccharomyces by Trichoderma viride and snail enzymes.","citation":"Folia Microbiol (Praha) 1975;20(4):273-6","abstract":"The formation of protoplasts of the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces versatilis after the combined application of snail enzymes and Trichoderma viride enzymes in an osmotic stabilizer (0.4M KCl, pH 5.5) was studied by light and electron microscopy. The effect of the enzymes used leads during 30 min to the formation of 100% protoplast population. Using electron microscopy no original walls or wall remnants were detected in the suspension of protoplasts. Protoplasts are viable and in liquid nutrient medium they regenerate cell walls and revert into normal cells. Such a protoplast population may be useful for biochemical study of protoplast metabolism by quantitative methods as well as for the chemical study of regenerating cell walls.","authors":"Kopecká M","authors_abbrev":"Kopecká M","pubmed_publication_date":"1975","pubmed_entrez_date":"1975-01-01","publication_year":"1975","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10559981","title":"A Rad3-Rad26 complex responds to DNA damage independently of other checkpoint proteins.","citation":"Nat Cell Biol 1999 Nov;1(7):393-8","abstract":"The conserved PIK-related kinase Rad3 is required for all DNA-integrity-checkpoint responses in fission yeast. Here we report a stable association between Rad3 and Rad26 in soluble protein extracts. Rad26 shows Rad3-dependent phosphorylation after DNA damage. Unlike phosphorylation of Hus1, Crb2/Rhp9, Cds1 and Chk1, phosphorylation of Rad26 does not require other known checkpoint proteins. Rad26 phosphorylation is the first biochemical marker of Rad3 function, indicating that Rad3-related checkpoint kinases may have a direct role in DNA-damage recognition.","authors":"Edwards RJ, Bentley NJ, Carr AM","authors_abbrev":"Edwards RJ et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-11-24","publication_year":"1999","canto_session_key":"eac4af49b1a4ec47","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-11-13 11:04:00","canto_approved_date":"2024-02-28 09:59:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-22 14:39:46","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":31,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC664.07c","SPCC1259.13","SPAC3H5.06c","SPCC16A11.17","SPAC9E9.08","SPBC336.04","SPAC20G8.01","SPBC336.12c","SPAC1952.07","SPAC14C4.13","SPAC20G4.04c","SPBC25H2.13c","SPBC216.05"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2018-11-13"},{"uniquename":"PMID:27916534","title":"Critical role of the proton-dependent oligopeptide transporter (POT) in the cellular uptake of the peptidyl nucleoside antibiotic, blasticidin S.","citation":"Biochim Biophys Acta Mol Cell Res 2017 Feb;1864(2):393-398","abstract":"Blasticidin S (BlaS) interferes in the cell growth of both eukaryotes and prokaryotes. Its mode of action as a protein synthesis inhibitor has been investigated extensively. However, the mechanism of BlaS transport into the target cells is not understood well. Here, we show that Ptr2, a member of the proton-dependent oligopeptide transporter (POT) family, is responsible for the uptake of BlaS in yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae. Notably, some mutants of Ptr2 that are dysfunctional in dipeptide uptake were still competent to transport BlaS. Mouse-derived oligopeptide transporter PepT1 conferred BlaS sensitivity in the S. cerevisiae ptr2∆ mutant. Furthermore, bacterial POT family proteins also potentiated the BlaS sensitivity of E. coli. The role of the POT family oligopeptide transporters in the uptake of BlaS is conserved across species from bacteria to mammals.","doi":"10.1016/j.bbamcr.2016.11.030","authors":"Kitamura K, Kinsui EZ, Abe F","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-12-06","publication_year":"2017","canto_session_key":"8005a381ec1cadfd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-12-07 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC13A2.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9548938","title":"Location of subunit-subunit contact sites on RNA polymerase II subunit 3 from the fission yeast Schizosaccharomyces pombe.","citation":"Biochemistry 1998 Apr 21;37(16):5542-8","abstract":"RNA polymerase II from the fission yeast Schizosaccharomyces pombe consists of 10 putative subunits. Subunit 3 (Rpb3) is a homologue of prokaryotic alpha subunit, which plays a key role in the assembly of core enzyme subunits. Previously we indicated that Rpb3 also plays an essential role in subunit assembly because it interacts with at least four subunits, two large subunits (Rpb1 and Rpb2) and two medium-sized subunits (Rpb3 and Rpb5) (1), and it constitutes a core subassembly consisting of Rpb2, Rpb3, and Rpb11 (2). Using a synthetic mixture of equimolar amounts of individual subunits, which were all purified from cDNA-expressed Escherichia coli, we found here that Rpb3 also interacts with Rpb11, another alpha homologue. By making a set of Rpb3 deletion derivatives, we carried out mapping of the Rpb5- and Rpb11-contact sites on Rpb3. By far-Western blot and GST pull-down assays, we found that the amino acid sequence between residues 105-263 of Rpb3 is involved in binding Rpb5, and the sequence between residues 105-297 is required for binding Rpb11. Although the Rpb5- and Rpb11-contact sites on Rpb3 overlap each other, both subunits are able to associate with Rpb3 simultaneously. The binding of Rpb5 stabilizes the Rpb3-Rpb11 heterodimer.","authors":"Yasui K, Ishiguro A, Ishihama A","authors_abbrev":"Yasui K et al.","pubmed_publication_date":"21 Apr 1998","pubmed_entrez_date":"1998-05-16","publication_year":"1998","canto_session_key":"1efd7df65c853c1a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-26 23:18:05","canto_approved_date":"2020-11-26 23:18:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-26 23:17:58","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1020.04c","SPAC23C4.15","SPAC1B3.12c","SPAC3A12.07","SPBC14C8.12","SPCC1442.10c","SPBC19C2.03"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2020-11-26"},{"uniquename":"PMID:1846086","title":"S. pombe gene sds22+ essential for a midmitotic transition encodes a leucine-rich repeat protein that positively modulates protein phosphatase-1.","citation":"Cell 1991 Jan 11;64(1):149-57","abstract":"The fission yeast dis2+ gene encodes one of the two type 1 protein phosphatases (PP1) in this organism. Its semidominant mutant dis2-11 is defective in mitosis. Here we report the characterization of a high dosage suppressor, sds22+, that complements dis2-11. Sequencing of the cloned sds22+ gene predicts a novel 30 kd protein, which consists almost entirely of leucine-rich 22 amino acid repeats and is enriched in the insoluble nuclear fraction. sds22+ is an essential gene required for the mitotic metaphase/anaphase transition; gene disruption causes cell cycle arrest at midmitosis. Unexpectedly, the sds22+ gene becomes dispensable upon high dosage of the PP1 genes. The sds22+ product appears to facilitate PP1-dependent dephosphorylation, but does not substitute PP1. We propose that the sds22+ protein forms a repeating helical rod that is capable of enhancing a PP1-dependent dephosphorylation activity that is essential in midmitosis.","authors":"Ohkura H, Yanagida M","authors_abbrev":"Ohkura H et al.","pubmed_publication_date":"11 Jan 1991","pubmed_entrez_date":"1991-01-11","publication_year":"1991","canto_session_key":"c93df2f114eaee6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-11-07 15:14:17","canto_approved_date":"2020-03-20 17:18:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-27 09:08:36","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC31H12.05c","SPAC4A8.12c","SPBC646.13","SPBC776.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-11-07"},{"uniquename":"PMID:32840771","title":"Analysis of DNA Double-Strand Break End Resection and Single-Strand Annealing in S. pombe.","citation":"Methods Mol Biol 2021;2153:47-57","abstract":"DNA double-strand break (DSB) end resection is an essential step for homologous recombination. It generates 3' single-stranded DNA needed for the loading of the strand exchange proteins and DNA damage checkpoint proteins. To study the mechanism of end resection in fission yeast, we apply a robust, quantitative and inducible assay. Resection is followed at a single per genome DSB synchronously generated by the tet-inducible I-PpoI endonuclease. An additional assay to follow resection involves recombination between two direct repeats by single-strand annealing (SSA), since SSA requires extensive resection to expose two single-strand repeats for annealing. The kinetics of resection and SSA repair are then measured using Southern blots.","doi":"10.1007/978-1-0716-0644-5_4","authors":"Yan Z, Kumar S, Ira G","authors_abbrev":"Yan Z et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2020-08-26","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-08-27 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15184401","title":"Myosin-II reorganization during mitosis is controlled temporally by its dephosphorylation and spatially by Mid1 in fission yeast.","citation":"J Cell Biol 2004 Jun 07;165(5):685-95","abstract":"Cytokinesis in many eukaryotes requires an actomyosin contractile ring. Here, we show that in fission yeast the myosin-II heavy chain Myo2 initially accumulates at the division site via its COOH-terminal 134 amino acids independently of F-actin. The COOH-terminal region can access to the division site at early G2, whereas intact Myo2 does so at early mitosis. Ser1444 in the Myo2 COOH-terminal region is a phosphorylation site that is dephosphorylated during early mitosis. Myo2 S1444A prematurely accumulates at the future division site and promotes formation of an F-actin ring even during interphase. The accumulation of Myo2 requires the anillin homologue Mid1 that functions in proper ring placement. Myo2 interacts with Mid1 in cell lysates, and this interaction is inhibited by an S1444D mutation in Myo2. Our results suggest that dephosphorylation of Myo2 liberates the COOH-terminal region from an intramolecular inhibition. Subsequently, dephosphorylated Myo2 is anchored by Mid1 at the medial cortex and promotes the ring assembly in cooperation with F-actin.","authors":"Motegi F, Mishra M, Balasubramanian MK, Mabuchi I","authors_abbrev":"Motegi F et al.","pubmed_publication_date":"07 Jun 2004","pubmed_entrez_date":"2004-06-09","publication_year":"2004","canto_session_key":"7e2a2611a978753c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-01-07 13:26:42","canto_approved_date":"2026-02-14 08:21:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-14 21:43:03","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPCC4B3.15","SPCC645.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-01-07"},{"uniquename":"PMID:10198290","title":"Mitotic control in the absence of cdc25 mitotic inducer in fission yeast.","citation":"J Cell Sci 1999 Apr;112 ( Pt 7):1085-92","abstract":"Fission yeast cells tolerate the total absence of the cdc25 mitotic inducer in two cases, either in cdc2-3w or in wee1 genetic backgrounds. In the cdc2-3w cdc25Delta double mutant, the rate-limiting step leading to mitosis is reaching a critical size. However, the size control of this mutant operates in late G2, which is different from wild-type (WT) cells. This fact suggests that in WT the rate-limiting molecular process during the G2 timer is the Tyr15 dephosphorylation of cdc2, for which the cdc25 phosphatase (together with its back-up, pyp3) is dependent. In the wee1-50 cdc25Delta mutant, the population splits into different clusters, all lacking mitotic size control. This strain maintains size homeostasis by a novel method, which is random movement of the cells from one cluster to another in the successive generations. These cells should normally have a 'minimal cycle', a 'timer' with short G1 and G2 phases. However, very often the cells abort mitosis, possibly at an early event and return back to early G2, thus lengthening their cycles. The inability of these cells to start anaphase might be caused by the absence of the main mitotic regulators (wee1 and cdc25) and the improper regulation of their back-up copies (mik1 and pyp3, respectively).","authors":"Sveiczer A, Novak B, Mitchison JM","authors_abbrev":"Sveiczer A et al.","pubmed_publication_date":"Apr 1999","pubmed_entrez_date":"1999-04-13","publication_year":"1999","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30014536","title":"Distinct modes of stress granule assembly mediated by the KH-type RNA-binding protein Rnc1.","citation":"Genes Cells 2018 Sep;23(9):778-785","abstract":"We have previously identified the KH-type RNA-binding protein Rnc1 as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. Rnc1 localization in response to stress has not been elucidated thus far. Here, we report the dual roles of Rnc1 in assembly of stress granules (SGs), nonmembranous cytoplasmic foci composed of messenger ribonucleoproteins. Rnc1 can localize to poly(A)-binding protein (Pabp)-positive SGs upon various stress stimuli, including heat shock (HS) and arsenite treatment. Furthermore, Rnc1 deletion results in decreased SGs, indicating that Rnc1 is a new component and a regulator of SGs. Notably, Rnc1 translocates to the dot-like structures faster than Pabp, and this stress-induced Rnc1 translocation does not require its RNA-binding ability, as the Rnc1 KH  1,2,3  GD  mutant protein with impaired RNA-binding activity forms dots rather more efficiently than the wild-type Rnc1 upon HS. Interestingly, in the absence of stress, Rnc1 overproduction induced massive aggregation of Pabp-positive SGs and eIF2α phosphorylation. In clear contrast, overproduction of the Rnc1 KH  1,2,3  GD  mutant failed to induce Pabp aggregation and eIF2α phosphorylation, indicating that Rnc1 overproduction-induced SG assembly requires Rnc1 RNA-binding activity. Collectively, Rnc1 regulates SG assembly, dependently or independently of its RNA-binding activity.","doi":"10.1111/gtc.12624","authors":"Satoh R, Hara N, Kawasaki A, Takasaki T, Sugiura R","authors_abbrev":"Satoh R et al.","pubmed_publication_date":"Sep 2018","pubmed_entrez_date":"2018-07-18","publication_year":"2018","canto_session_key":"8336c866d1b076fc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-07-19 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27402898","title":"Relative contributions of the structural and catalytic roles of Rrp6 in exosomal degradation of individual mRNAs.","citation":"RNA 2016 Sep;22(9):1311-9","abstract":"The RNA exosome is a conserved complex for RNA degradation with two ribonucleolytic subunits, Dis3 and Rrp6. Rrp6 is a 3'-5' exonuclease, but it also has a structural role in helping target RNAs to the Dis3 activity. The relative importance of the exonuclease activity and the targeting activity probably differs between different RNA substrates, but this is poorly understood. To understand the relative contributions of the exonuclease and the targeting activities to the degradation of individual RNA substrates in Schizosaccharomyces pombe, we compared RNA levels in an rrp6 null mutant to those in an rrp6 point mutant specifically defective in exonuclease activity. A wide range of effects was found, with some RNAs dependent mainly on the structural role of Rrp6 (\"protein-dependent\" targets), other RNAs dependent mainly on the catalytic role (\"activity-dependent\" targets), and some RNAs dependent on both. Some protein-dependent RNAs contained motifs targeted via the RNA-binding protein Mmi1, while others contained a motif possibly involved in response to iron. In these and other cases Rrp6 may act as a structural adapter to target specific RNAs to the exosome by interacting with sequence-specific RNA-binding proteins.","doi":"10.1261/rna.051490.115","authors":"Mukherjee K, Gardin J, Futcher B, Leatherwood J","authors_abbrev":"Mukherjee K et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-07-13","publication_year":"2016","canto_session_key":"2c54ac63dbe06059","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-14 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F3.01","SPBC26H8.10","SPCC736.12c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:9191271","title":"Isolation of yeast mutants hypersensitive to mating pheromones.","citation":"Biochem Soc Trans 1997 May;25(2):227S","abstract":"","authors":"Davis K, Davey J","authors_abbrev":"Davis K et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"bb15399f563a39a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-04-29 10:33:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-04-27 16:13:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPAC513.03","SPBPJ4664.03","SPMTR.02","SPAPB8E5.05"],"gene_count":5,"ltp_gene_count":0,"approved_date":"2012-04-27"},{"uniquename":"PMID:15948957","title":"Protein O-mannosylation is crucial for cell wall integrity, septation and viability in fission yeast.","citation":"Mol Microbiol 2005 Jul;57(1):156-70","abstract":"Protein O-mannosyltransferases (PMTs) initiate the assembly of O-mannosyl glycans, which are of fundamental importance in eukaryotes. The PMT family, which is classified into PMT1, PMT2 and PMT4 subfamilies, is evolutionarily conserved. Despite the fact that PMTs are crucial for viability of baker's yeast as well as of mouse, recent studies suggested that there are significant differences in the organization and properties of the O-mannosylation machinery between yeasts and mammals. In this study we identified and characterized the PMT family of the archaeascomycete Schizosaccharomyces pombe. Unlike Saccharomyces cerevisiae where the PMT family is highly redundant, in S. pombe only one member of each PMT subfamily is present, namely, oma1+ (protein O-mannosyltransferase), oma2+ and oma4+. They all act as protein O-mannosyltransferases in vivo. oma1+ and oma2+ form heteromeric protein complexes and recognize different protein substrates compared to oma4+, suggesting that similar principles underlie mannosyltransfer reaction in S. pombe and budding yeast. Deletion of oma2+, as well as simultaneous deletion of oma1+ and oma4+ is lethal. Characterization of the viable S. pombe oma1Delta and oma4Delta single mutants showed that a lack of O-mannosylation results in abnormal cell wall and septum formation, thereby severely affecting cell morphology and cell-cell separation.","authors":"Willer T, Brandl M, Sipiczki M, Strahl S","authors_abbrev":"Willer T et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-06-14","publication_year":"2005","canto_session_key":"4bb09fd73c930f7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-01-05 14:25:11","canto_approved_date":"2024-07-22 08:37:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-30 20:36:49","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAPB1E7.09","SPAC22A12.07c","SPBC30B4.01c","SPBC16C6.09"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-01-05"},{"uniquename":"PMID:12808110","title":"Schizosaccharomyces pombe checkpoint response to DNA interstrand cross-links.","citation":"Mol Cell Biol 2003 Jul;23(13):4728-37","abstract":"Drugs that produce covalent interstrand cross-links (ICLs) in DNA remain central to the treatment of cancer, but the cell cycle checkpoints activated by ICLs have received little attention. We have used the fission yeast, Schizosaccharomyces pombe, to elucidate the checkpoint responses to the ICL-inducing anticancer drugs nitrogen mustard and mitomycin C. First we confirmed that the repair pathways acting on ICLs in this yeast are similar to those in the main organisms studied to date (Escherichia coli, budding yeast, and mammalian cells), principally nucleotide excision repair and homologous recombination. We also identified and disrupted the S. pombe homologue of the Saccharomyces cerevisiae SNM1/PSO2 ICL repair gene and found that this activity is required for normal resistance to cross-linking agents, but not other forms of DNA damage. Survival and biochemical analysis indicated a key role for the \"checkpoint Rad\" family acting through the chk1-dependent DNA damage checkpoint in the ICL response. Rhp9-dependent phosphorylation of Chk1 correlates with G(2) arrest following ICL induction. In cells able to bypass the G(2) block, a second-cycle (S-phase) arrest was observed. Only a transient activation of the Cds1 DNA replication checkpoint factor occurs following ICL formation in wild-type cells, but this is increased and persists in G(2) arrest-deficient mutants. This likely reflects the fraction of cells escaping the G(2) damage checkpoint and arresting in the subsequent S phase due to ICL replication blocks. Disruption of cds1 confers increased resistance to ICLs, suggesting that this second-cycle S-phase arrest might be a lethal event.","authors":"Lambert S, Mason SJ, Barber LJ, Hartley JA, Pearce JA, Carr AM, McHugh PJ","authors_abbrev":"Lambert S et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-06-17","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPCC18B5.11c","SPAC22A12.01c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:39449363","title":"Epigenome Mapping in Quiescent Cells Reveals a Key Role for H3K4me3 in Regulation of RNA Polymerase II Activity.","citation":"Epigenomes 2024 Oct 22;8(4)","abstract":"(1) Background: Quiescent cells are those that have stopped dividing and show strongly reduced levels of gene expression during dormancy. In response to appropriate signals, the cells can wake up and start growing again. Many histone modifications are regulated in quiescence, but their exact functions remain to be determined. (2) Methods: Here, we map the different histone modifications, H3K4me3, H3K9ac, H3K9me2, and H3K9me3, and the histone variant H2A.Z, comparing vegetative and quiescent fission yeast ( S. pombe ) cells. We also map histone H3 as a control and RNA polymerase II (phosphorylated at S2 and S5) to enable comparisons of their occupancies within genes. We use ChIP-seq methodology and several different bioinformatics tools. (3) Results: The histone modification mapping data show that H3K4me3 changes stand out as being the most significant. Changes in occupancy of histone variant H2A.Z were also significant, consistent with earlier studies. Regarding gene expression changes in quiescence, we found that changes in mRNA levels were associated with changes in occupancy of RNA polymerase II (S2 and S5). Analysis of quiescence genes showed that increased H3K4me3 levels and RNA polymerase II occupancy were super-significant in a small set of core quiescence genes that are continuously upregulated during dormancy. We demonstrate that several of these genes were require Set1C/COMPASS activity for their strong induction during quiescence. (4) Conclusions: Our results imply that regulation of gene expression in quiescent cells involves epigenome changes with a key role for H3K4me3 in regulation of RNA polymerase II activity, and that different gene activation mechanisms control early and core quiescence genes. Thus, our data give further insights into important epigenome changes in quiescence using fission yeast as an experimental model.","doi":"10.3390/epigenomes8040039","authors":"Zeng S, Ekwall K","authors_abbrev":"Zeng S et al.","pubmed_publication_date":"22 Oct 2024","pubmed_entrez_date":"2024-10-25","publication_year":"2024","canto_session_key":"845771114135aa81","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-10-25 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18684775","title":"A genome-wide screen of genes involved in cadmium tolerance in Schizosaccharomyces pombe.","citation":"Toxicol Sci 2008 Nov;106(1):124-39","abstract":"Cadmium is a worldwide environmental toxicant responsible for a range of human diseases including cancer. Cellular injury from cadmium is minimized by stress-responsive detoxification mechanisms. We explored the genetic requirements for cadmium tolerance by individually screening mutants from the fission yeast (Schizosaccharomyces pombe) haploid deletion collection for inhibited growth on agar growth media containing cadmium. Cadmium-sensitive mutants were further tested for sensitivity to oxidative stress (hydrogen peroxide) and osmotic stress (potassium chloride). Of 2649 mutants screened, 237 were sensitive to cadmium, of which 168 were cadmium specific. Most were previously unknown to be involved in cadmium tolerance. The 237 genes represent a number of pathways including sulfate assimilation, phytochelatin synthesis and transport, ubiquinone (Coenzyme Q10) biosynthesis, stress signaling, cell wall biosynthesis and cell morphology, gene expression and chromatin remodeling, vacuole function, and intracellular transport of macromolecules. The ubiquinone biosynthesis mutants are acutely sensitive to cadmium but only mildly sensitive to hydrogen peroxide, indicating that Coenzyme Q10 plays a larger role in cadmium tolerance than just as an antioxidant. These and several other mutants turn yellow when exposed to cadmium, suggesting cadmium sulfide accumulation. This phenotype can potentially be used as a biomarker for cadmium. There is remarkably little overlap with a comparable screen of the Saccharomyces cerevisiae haploid deletion collection, indicating that the two distantly related yeasts utilize significantly different strategies for coping with cadmium stress. These strategies and their relation to cadmium detoxification in humans are discussed.","doi":"10.1093/toxsci/kfn153","authors":"Kennedy PJ, Vashisht AA, Hoe KL, Kim DU, Park HO, Hayles J, Russell P","authors_abbrev":"Kennedy PJ et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-08-08","publication_year":"2008","canto_session_key":"eba4e446aec8427a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-09-24 14:11:58","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-24 14:11:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":337,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_18684775_phaf.tsv"}],"genes":["SPBC3B8.10c","SPCC1827.03c","SPAC4A8.03c","SPAC24B11.12c","SPBC32H8.07","SPBC119.16c","SPAC688.04c","SPAC521.03","SPAC12G12.15","SPCC584.01c","SPBP8B7.23","SPBC19G7.18c","SPCC16C4.10","SPBPB2B2.19c","SPAC186.02c","SPCC737.09c","SPAC17A2.02c","SPCC1494.10","SPBC685.03","SPBC1703.14c","SPCC594.06c","SPAC19B12.10","SPBC20F10.05","SPCC11E10.08","SPCC794.03","SPAC2F3.15","SPAC17A2.09c","SPAC630.06c","SPAC3G6.01","SPCC13B11.01","SPCC1020.11c","SPAC3C7.04","SPBC530.04","SPBC1685.15c","SPCC126.04c","SPBC800.09","SPBC119.12","SPCC965.06","SPCC162.06c","SPCC162.02c","SPBC1198.08","SPAC23C11.14","SPAC19G12.08","SPAC11G7.02","SPBC1921.07c","SPBC902.03","SPAC631.02","SPBC359.03c","SPBC215.01","SPAC30C2.02","SPAC977.08","SPAC25A8.01c","SPBC4F6.06","SPAC11E3.05","SPAC27D7.08c","SPBC1348.07","SPAC27F1.08","SPBC8D2.19","SPBC2G5.06c","SPAC22F3.10c","SPBC28F2.10c","SPBC1A4.04","SPAC19D5.02c","SPCC777.03c","SPBC31E1.02c","SPBC12D12.07c","SPCC594.05c","SPBC21B10.06c","SPBC409.16c","SPCC550.03c","SPAC8C9.03","SPBC691.03c","SPBC30B4.03c","SPBC2G5.03","SPBC6B1.06c","SPAC1783.02c","SPCC188.02","SPBC582.08","SPBC14F5.13c","SPAC4F8.08","SPBC337.15c","SPCC1450.06c","SPBC21B10.13c","SPBC106.01","SPCC895.07","SPBC530.03c","SPAC22F3.13","SPAC513.04","SPBC19G7.03c","SPAC20H4.09","SPAC589.08c","SPAC806.04c","SPCC1682.11c","SPCC1442.04c","SPBC651.10","SPAP14E8.04","SPAC17C9.13c","SPBC1861.03","SPBC530.08","SPAC3F10.07c","SPCC63.02c","SPAC6F12.09","SPCC1281.03c","SPAC29B12.05c","SPAC4G9.20c","SPAC16C9.05","SPAC25G10.03","SPAC12B10.03","SPBC146.13c","SPBC27B12.06","SPAC22F3.09c","SPCC188.09c","SPCC794.11c","SPBC13G1.08c","SPAC22H10.13","SPCC162.05","SPAC31A2.11c","SPBC25H2.09","SPBC21D10.07","SPBC609.05","SPAC6G10.06","SPBC577.11","SPAC4G9.14","SPBC1198.11c","SPBC887.10","SPCC16C4.20c","SPBC27.08c","SPBC3H7.09","SPAPJ696.01c","SPCC1840.09","SPAC1783.07c","SPCC13B11.04c","SPCC126.10","SPCC1442.16c","SPAC4F10.04","SPAC821.05","SPBC317.01","SPAC23D3.09","SPBC3H7.11","SPBC336.03","SPAC977.14c","SPAC664.02c","SPAC767.01c","SPBC30B4.04c","SPAC4D7.06c","SPCC4G3.04c","SPCC18.06c","SPAC9G1.02","SPBC725.04","SPBC800.03","SPCC1393.03","SPAC20H4.02","SPBC947.03c","SPAC30.02c","SPCC16C4.11","SPAC12G12.12","SPAC13G7.06","SPAC6B12.12","SPBC36.04","SPBC24C6.05","SPBC1706.01","SPAC31G5.18c","SPAC1002.15c","SPAC823.10c","SPAC144.03","SPCC16C4.04","SPAC1952.05","SPAC29A4.20","SPCC417.02","SPAC1071.02","SPAC21E11.03c","SPAC22F8.11","SPAC1805.07c","SPBC1539.08","SPBC530.01","SPAC1002.03c","SPBC337.03","SPBC2G2.14","SPCC613.02","SPAC1039.08","SPAC24B11.06c","SPBC713.05","SPCC1259.10","SPAC26H5.05","SPAC17G8.07","SPAC13C5.04","SPAC3H1.10","SPCC16A11.07","SPCP1E11.04c","SPAC25B8.05","SPAC630.13c","SPBC27.02c","SPAC16A10.05c","SPAC23H4.07c","SPCC4B3.15","SPBC8D2.18c","SPAC14C4.06c","SPAC26A3.10","SPBC543.05c","SPCC1393.02c","SPBC83.18c","SPBC12C2.03c","SPAC17H9.08","SPAC17A2.11","SPAC1782.11","SPBC1711.04","SPAC9.02c","SPBC119.03","SPAC1071.11","SPBC19F8.06c","SPBPB10D8.01","SPCC11E10.07c","SPCC338.14","SPAC17A2.14","SPAPB1A10.12c","SPAC1782.05","SPBC4.06","SPAC17A5.16","SPBC3B8.02","SPAC15E1.06","SPCC24B10.20","SPBC409.15","SPBC336.15","SPCC1739.06c","SPAC6B12.05c","SPCC553.01c","SPAC56F8.04c","SPBC800.05c","SPCC584.02","SPBC3E7.10","SPAC6G9.05","SPBC3H7.12","SPBC12C2.09c","SPAPYUK71.03c","SPAC1687.12c","SPBC1105.10","SPBC342.03","SPCC1919.04"],"gene_count":238,"ltp_gene_count":1,"approved_date":"2013-09-24"},{"uniquename":"PMID:8765231","title":"Phosphoglycerate mutase from Schizosaccharomyces pombe: development of an expression system and characterisation of three histidine mutants of the enzyme.","citation":"Biochim Biophys Acta 1996 Aug 15;1296(1):69-75","abstract":"The small, monomeric, phosphoglycerate mutase (PGAM) from Schizosaccharomyces pombe has been overexpressed in a strain of Saccharomyces cerevisiae in which the gene encoding PGAM has been deleted, with a yield of purified enzyme of 10-15 mg per litre cell culture. Three mutants in which histidine residues in S. pombe PGAM have been substituted by glutamine have been purified and characterised. Two mutants (H151Q and H196Q) have kinetic and structural properties very similar to wild-type enzyme, consistent with the proposed location of these (non-conserved) histidines on the surface of the enzyme. The third mutant (H163Q) involving a histidine thought to be part of the active site has greatly reduced mutase and phosphatase activities. Mass spectrometry shows that the phosphorylated form of the H163Q is several 100-times more stable towards hydrolysis than the phosphorylated form of wild-type enzyme. The H163Q mutant appears to be structurally quite distinct from wild-type enzyme. 600 MHz 1D proton NMR spectra of good quality have been obtained for wild-type enzyme and the H151Q and H196Q mutants.","authors":"Nairn J, Price NC, Kelly SM, Rigden D, Fothergill-Gilmore LA, Krell T","authors_abbrev":"Nairn J et al.","pubmed_publication_date":"15 Aug 1996","pubmed_entrez_date":"1996-08-15","publication_year":"1996","canto_session_key":"258041a63b9b8e88","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-13 12:10:53","canto_approved_date":"2024-11-05 12:30:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-11 14:09:58","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26F1.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-13"},{"uniquename":"PMID:9878752","title":"Overview of N- and O-linked oligosaccharide structures found in various yeast species.","citation":"Biochim Biophys Acta 1999 Jan 06;1426(2):227-37","abstract":"Yeast and most higher eukaryotes utilize an evolutionarily conserved N-linked oligosaccharide biosynthetic pathway that involves the formation of a Glc3Man9GlcNAc2-PP-dolichol lipid-linked precursor, the glycan portion of which is co-translationally transferred in the endoplasmic reticulum (ER) to suitable Asn residues on nascent polypeptides. Subsequently, ER processing glycohydrolases remove the three glucoses and, with the exception of Schizosaccharomyces pombe, a single, specific mannose residue. Processing sugar transferases in the Golgi lead to the formation of core-sized structures (Hex<15GlcNac2) as well as cores with an extended poly-alpha1,6-Man 'backbone' that is derivatized with various carbohydrate side chains in a species-specific manner (Hex50-200GlnNAc2). In some cases these are short alpha1,2-linked Man chains with (Saccharomyces cerevisiae) or without (Pichia pastoris) alpha1,3-Man caps, while in other yeast (S. pombe), the side chains are alpha1,2-linked Gal, some of which are capped with beta-1,3-linked pyruvylated Gal residues. Charged groups are also found in S. cerevisiae and P. pastoris N-glycans in the form of mannose phosphate diesters. Some pathogenic yeast (Candida albicans) add poly-beta1,2-Man extension through a phosphate diester to their N-glycans, which appears involved in virulence. O-Linked glycan synthesis in yeast, unlike in animal cells where it is initiated in the Golgi using nucleotide sugars, begins in the ER by addition of a single mannose from Man-P-dolichol to selected Ser/Thr residues in newly made proteins. Once transported to the Golgi, sugar transferases add one (C. albicans) or more (P. pastoris) alpha1,2-linked mannose that may be capped with one or two alpha1,3-linked mannoses (S. cerevisiae). S. pombe is somewhat unique in that it synthesizes a family of mixed O-glycans with additional alpha1,2-linked Man and alpha1,2- and 1, 3-linked Gal residues.","authors":"Gemmill TR, Trimble RB","authors_abbrev":"Gemmill TR et al.","pubmed_publication_date":"06 Jan 1999","pubmed_entrez_date":"1999-01-08","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000105","title":"Gene Ontology annotation of transfer RNAs based on tRNAscan-SE analysis of the Drosophila melanogaster genome (2002).","abstract":"Gene Ontology annotation based on predicted cytoplasmic tRNAs using tRNAscan-SE analysis (doi: 10.1093/nar/25.5.0955) of the Drosophila melanogaster genome (2002). Annotations have been reviewed by FlyBase (2015) and found to be consistent when compared with the most recent tRNAscan-SE analysis of the genome (http://gtrnadb.ucsc.edu/genomes/eukaryota/Dmela6/).","authors":"FlyBase","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22896789","title":"Ensuring the faithful execution of cytokinesis in Schizosaccharomyces pombe.","citation":"Commun Integr Biol 2012 May 01;5(3):265-71","abstract":"Eukaryotic cells ensure error-free progress through the cell cycle by monitoring (1) the completion of cell cycle events, (2) damage to critical cellular components, or (3) structural changes such as the attachment of kinetochores to the mitotic spindle. In the presence of damage, or in the face of a reduced capacity to complete essential events, cells are capable of delaying the cell cycle so that damage can be repaired, or previous cell cycle phases can proceed to completion. Although such \"checkpoints\" have been extensively studied in many organisms-and much is understood with respect to the monitoring of DNA replication and DNA damage-little is known with regards to mechanisms that might monitor the completion of cytokinesis. In this review I summarize recent work from the fission yeast, Schizosaccharomyces pombe, describing the existence of regulatory modules that aid in ensuring the faithful and reliable execution of cytokinesis. Together, these modules promote the maintenance of a \"cytokinesis-competent\" state characterized by delayed progression into mitosis and the continuous repair and/or re-establishment of the acto-myosin ring. In this way, fission yeast cells are able to increase the likelihood of successful cell division prior to committing to a subsequent cell cycle. The recent demonstration of conservation between S. pombe components of these modules, and human proteins with defined roles in preventing cell division failure, suggest that the lessons learned in S. pombe may be applicable to other eukaryotes.","doi":"10.4161/cib.19860","authors":"Karagiannis J","authors_abbrev":"Karagiannis J","pubmed_publication_date":"01 May 2012","pubmed_entrez_date":"2012-08-17","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:Z14055","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006642","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40287791","title":"Screening and application of unstable genetically resistant strains in fission yeast.","citation":"Yi Chuan 2025 May;47(5):589-599","abstract":"Reversible alterations at DNA sequence or epigenetic levels can result in phenotypes that are unstably inherited. The reversibility of these inheritable changes might be uniquely beneficial for adaption to possible fluctuations in environment. However, unstable changes are always ignored for the genetic instability in traditional studies, especially in the cause of drug resistance. In this study, we conduct a specific genetic screen in fission yeast using rapamycin (+caffeine) and obtain 173 resistant isolates. In contrast to the common strategy of isolating stable genetic mutants, we passage the cell culture with rapamycin resistance on drug free condition and test the resistance of offspring every five days, and obtain 14 strains that exhibit unstable resistance to rapamycin (the drug resistance is lost randomly among the cell progenies without drug selection pressure). Further studies show that the unstable genetic resistance of some strains is regulated by reversible DNA sequence alterationat the  ssp1  gene locus. This study provides new insights and relevant scientific basis for the regulatory mechanism of unstable drug resistance in the process of rapamycin as a clinical anti-tumor drug, and a new possible target for solving the problem of drug resistance.","doi":"10.16288/j.yczz.24-266","authors":"Dan LF, Chu YW, Wang XR, He XW","authors_abbrev":"Dan LF et al.","pubmed_publication_date":"May 2025","pubmed_entrez_date":"2025-04-27","publication_year":"2025","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2025-04-27 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32548620","title":"Inverted meiosis: an alternative way of chromosome segregation for reproduction.","citation":"Acta Biochim Biophys Sin (Shanghai) 2020 Jul 10;52(7):702-707","abstract":"Canonical meiosis is characterized by two sequential rounds of nuclear divisions following one round of DNA replication-reductional segregation of homologous chromosomes during the first division and equational segregation of sister chromatids during the second division. Meiosis in an inverted order of two nuclear divisions-inverted meiosis has been observed in several species with holocentromeres as an adaptive strategy to overcome the obstacle in executing a canonical meiosis due to the holocentric chromosome structure. Recent findings of co-existence of inverted and canonical meiosis in two monocentric organisms, human and fission yeast, suggested that inverted meiosis could be common and also lead to the puzzle regarding the mechanistic feasibility for executing two meiosis programs simultaneously. Here, we discuss apparent conflicts for concurrent canonical meiosis and inverted meiosis. Furthermore, we attempt to provide a working model that may be compatible for both forms of meiosis.","doi":"10.1093/abbs/gmaa054","authors":"Li W, He X","authors_abbrev":"Li W et al.","pubmed_publication_date":"10 Jul 2020","pubmed_entrez_date":"2020-06-18","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-06-19 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16118282","title":"Effects of the tumor inhibitory triterpenoid avicin G on cell integrity, cytokinesis, and protein ubiquitination in fission yeast.","citation":"Proc Natl Acad Sci U S A 2005 Sep 06;102(36):12771-6","abstract":"Avicins comprise a class of triterpenoid compounds that exhibit tumor inhibitory activity. Here we show that avicin G is inhibitory to growth of the fission yeast Schizosaccharomyces pombe. S. pombe cells treated with a lethal concentration of avicin G (20 microM) exhibited a shrunken morphology, indicating that avicin G adversely affects cell integrity. Cells treated with a sublethal concentration of avicin G (6.5 microM) exhibited a strong cytokinesis-defective phenotype (multiseptated cells), as well as cell morphology defects. These phenotypes bear resemblance to those resulting from loss of Rho1 GTPase function in S. pombe. Indeed, Rho1-deficient S. pombe cells were strongly hypersensitive to avicin G, suggesting that the compound may perturb Rho1-dependent processes. Consistent with previously observed effects in human Jurkat T cells, avicin G treatment resulted in hyperaccumulation of ubiquitinated proteins in S. pombe cells. Interestingly, proteasome-defective S. pombe mutants were not markedly hypersensitive to avicin G, whereas an anaphase-promoting complex (mitotic ubiquitin ligase) mutant exhibited avicin G resistance, suggesting that the increase in levels of ubiquitinated proteins resulting from avicin G treatment may be due to increased protein ubiquitination, rather than inhibition of 26S proteasome activity. Mutants defective in the cAMP/PKA pathway also exhibited resistance to avicin G. Our results suggest that S. pombe will be a useful model organism for elucidating molecular targets of avicin G and serve as a guide to clinical application where dysfunctional aspects of Rho and/or ubiquitination function have been demonstrated as in cancer, fibrosis, and inflammation.","authors":"Gutterman JU, Lai HT, Yang P, Haridas V, Gaikwad A, Marcus S","authors_abbrev":"Gutterman JU et al.","pubmed_publication_date":"06 Sep 2005","pubmed_entrez_date":"2005-08-25","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12198172","title":"The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases.","citation":"EMBO J 2002 Sep 02;21(17):4699-708","abstract":"We recently demonstrated that the major decapping activity in mammalian cells involves DcpS, a scavenger pyrophosphatase that hydrolyzes the residual cap structure following 3' to 5' decay of an mRNA. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. We purified DcpS from mammalian cells and identified the cDNA encoding a novel 40 kDa protein possessing DcpS activity. Consistent with purified DcpS, the recombinant protein specifically hydrolyzed methylated cap analog but did not hydrolyze unmethylated cap analog nor did it function on intact capped RNA. Sequence alignments of DcpS from different organisms revealed the presence of a conserved hexapeptide, containing a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues. Mutagenesis analysis revealed that the central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.","authors":"Liu H, Rodgers ND, Jiao X, Kiledjian M","authors_abbrev":"Liu H et al.","pubmed_publication_date":"02 Sep 2002","pubmed_entrez_date":"2002-08-29","publication_year":"2002","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.20"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12756240","title":"Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart.","citation":"J Biol Chem 2003 Aug 08;278(32):29719-27","abstract":"The results of in vivo and in organellar experiments indicate that the Hsp70 Ssq1 and the J-protein Jac1 function together to assist in the biogenesis of iron-sulfur (Fe/S) centers in the mitochondrial matrix. Here we present biochemical evidence supporting this idea. Isu, the proposed scaffold on which Fe/S centers are assembled, is a substrate for both Jac1 and Ssq1. Jac1 and Isu1 cooperatively stimulate the ATPase activity of Ssq1. In addition, Jac1 facilitates the interaction of Ssq1 with Isu1 in the presence of ATP. These findings are consistent with the role in Fe/S biogenesis previously proposed for the bacterial Hsp70 Hsc66 and J-protein Hsc20 that interact with the bacterial Isu homologue IscU. However, unlike the bacterial Hsp70, we found that Ssq1 has a high affinity for nucleotide, and shares a nucleotide exchange factor, Mge1, with a second mitochondrial Hsp70, Ssc1. Thus, whereas the bacterial and mitochondrial chaperone systems share critical features, they possess significant biochemical differences as well.","authors":"Dutkiewicz R, Schilke B, Knieszner H, Walter W, Craig EA, Marszalek J","authors_abbrev":"Dutkiewicz R et al.","pubmed_publication_date":"08 Aug 2003","pubmed_entrez_date":"2003-05-21","publication_year":"2003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3B9.19"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38499788","title":"TOR regulates variability of protein synthesis rates.","citation":"EMBO J 2024 Mar 18;","abstract":"Cellular processes are subject to inherent variability, but the extent to which cells can regulate this variability has received little investigation. Here, we explore the characteristics of the rate of cellular protein synthesis in single cells of the eukaryote fission yeast. Strikingly, this rate is highly variable despite protein synthesis being dependent on hundreds of reactions which might be expected to average out at the overall cellular level. The rate is variable over short time scales, and exhibits homoeostatic behaviour at the population level. Cells can regulate the level of variability through processes involving the TOR pathway, suggesting there is an optimal level of variability conferring a selective advantage. While this could be an example of bet-hedging, but we propose an alternative explanation: regulated 'loose' control of complex processes of overall cellular metabolism such as protein synthesis, may lead to this variability. This could ensure cells are fluid in control and agile in response to changing conditions, and may constitute a novel organisational principle of complex metabolic cellular systems.","doi":"10.1038/s44318-024-00075-8","authors":"Basier C, Nurse P","authors_abbrev":"Basier C et al.","pubmed_publication_date":"18 Mar 2024","pubmed_entrez_date":"2024-03-19","publication_year":"2024","canto_session_key":"fd365a2697a73307","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-20 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12531030","title":"Two budding yeast RAD4 homologs in fission yeast play different roles in the repair of UV-induced DNA damage.","citation":"DNA Repair (Amst) 2002 Oct 01;1(10):833-45","abstract":"We have identified two fission yeast homologs of budding yeast Rad4 and human xeroderma pigmentosum complementation group C (XP-C) correcting protein, designated Rhp4A and Rhp4B. Here we show that the rhp4 genes encode NER factors that are required for UV-induced DNA damage repair in fission yeast. The rhp4A-deficient cells but not the rhp4B-deficient cells are sensitive to UV irradiation. However, the disruption of both rhp4A and rhp4B resulted in UV sensitivity that was greater than that of the rhp4A-deficient cells, revealing that Rhp4B plays a role in DNA repair on its own. Fission yeast has two pathways to repair photolesions on DNA, namely, nucleotide excision repair (NER) and UV-damaged DNA endonuclease-dependent excision repair (UVER). Studies with the NER-deficient rad13 and the UVER-deficient (Delta)uvde mutants showed the two rhp4 genes are involved in NER and not UVER. Assessment of the ability of the various mutants to remove cyclobutane pyrimidine dimers (CPDs) from the rbp2 gene locus indicated that Rhp4A is involved in the preferential repair of lesions on the transcribed DNA strand and plays the major role in fission yeast NER. Rhp4B in contrast acts as an accessory protein in non-transcribed strand (NTS) repair.","authors":"Fukumoto Y, Hiyama H, Yokoi M, Nakaseko Y, Yanagida M, Hanaoka F","authors_abbrev":"Fukumoto Y et al.","pubmed_publication_date":"01 Oct 2002","pubmed_entrez_date":"2003-01-18","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2D10.12","SPBC19C7.09c","SPCC4G3.10c","SPAC12B10.12c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:28774892","title":"Dialogue between centrosomal entrance and exit scaffold pathways regulates mitotic commitment.","citation":"J Cell Biol 2017 Sep 04;216(9):2795-2812","abstract":"The fission yeast scaffold molecule Sid4 anchors the septum initiation network to the spindle pole body (SPB, centrosome equivalent) to control mitotic exit events. A second SPB-associated scaffold, Cut12, promotes SPB-associated Cdk1-cyclin B to drive mitotic commitment. Signals emanating from each scaffold have been assumed to operate independently to promote two distinct outcomes. We now find that signals from Sid4 contribute to the Cut12 mitotic commitment switch. Specifically, phosphorylation of Sid4 by NIMA Fin1  reduces Sid4 affinity for its SPB anchor, Ppc89, while also enhancing Sid4's affinity for casein kinase 1δ (CK1δ). The resulting phosphorylation of Sid4 by the newly docked CK1δ recruits Chk2 Cds1  to Sid4. Chk2 Cds1  then expels the Cdk1-cyclin B antagonistic phosphatase Flp1/Clp1 from the SPB. Flp1/Clp1 departure can then support mitotic commitment when Cdk1-cyclin B activation at the SPB is compromised by reduction of Cut12 function. Such integration of signals emanating from neighboring scaffolds shows how centrosomes/SPBs can integrate inputs from multiple pathways to control cell fate.","doi":"10.1083/jcb.201702172","authors":"Chan KY, Alonso-Nuñez M, Grallert A, Tanaka K, Connolly Y, Smith DL, Hagan IM","authors_abbrev":"Chan KY et al.","pubmed_publication_date":"04 Sep 2017","pubmed_entrez_date":"2017-08-05","publication_year":"2017","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-08-06 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC694.06c","SPAC19E9.02","SPAC23C4.12","SPBC3H7.15","SPBC244.01c","SPBC649.05","SPAC4H3.11c","SPCC18B5.11c"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:17449867","title":"Interaction of Epe1 with the heterochromatin assembly pathway in Schizosaccharomyces pombe.","citation":"Genetics 2007 Apr;175(4):1549-60","abstract":"Epe1 is a JmjC domain protein that antagonizes heterochromatization in Schizosaccharomyces pombe. Related JmjC domain proteins catalyze a histone demethylation reaction that depends on Fe(II) and alpha-ketoglutarate. However, no detectable demethylase activity is associated with Epe1, and its JmjC domain lacks conservation of Fe(II)-binding residues. We report that Swi6 recruits Epe1 to heterochromatin and that overexpression of epe1+, like mutations in silencing genes or overexpression of swi6+, upregulates expression of certain genes. A significant overlap was observed between the lists of genes that are upregulated by overexpression of epe1+ and those that are upregulated by mutations in histone deacetylase genes. However, most of the common genes are not regulated by Clr4 histone methyltransferase. This suggests that Epe1 interacts with the heterochromatin assembly pathway at the stage of histone deacetylation. Mutational inactivation of Epe1 downregulates approximately 12% of S. pombe genes, and the list of these genes overlaps significantly with the lists of genes that are upregulated by mutations in silencing genes and genes that are hyperacetylated at their promoter regions in clr6-1 mutants. We propose that an interplay between the repressive HDACs activity and Epe1 helps to regulate gene expression in S. pombe.","authors":"Isaac S, Walfridsson J, Zohar T, Lazar D, Kahan T, Ekwall K, Cohen A","authors_abbrev":"Isaac S et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-04-24","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.16c","SPAC664.01c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:39378339","title":"Arrayed CRISPRi library to suppress genes required for Schizosaccharomyces pombe viability.","citation":"J Cell Biol 2025 Jan 06;224(1)","abstract":"The fission yeast, Schizosaccharomyces pombe, is an excellent eukaryote model organism for studying essential biological processes. Its genome contains ∼1,200 genes essential for cell viability, most of which are evolutionarily conserved. To study these essential genes, resources enabling conditional perturbation of target genes are required. Here, we constructed comprehensive arrayed libraries of plasmids and strains to knock down essential genes in S. pombe using dCas9-mediated CRISPRi. These libraries cover ∼98% of all essential genes in fission yeast. We estimate that in ∼60% of these strains, transcription of a target gene was repressed so efficiently that cell proliferation was significantly inhibited. To demonstrate the usefulness of these libraries, we performed metabolic analyses with knockdown strains and revealed flexible interaction among metabolic pathways. Libraries established in this study enable comprehensive functional analyses of essential genes in S. pombe and will facilitate the understanding of essential biological processes in eukaryotes.","doi":"10.1083/jcb.202404085","authors":"Ishikawa K, Soejima S, Nishimura T, Saitoh S","authors_abbrev":"Ishikawa K et al.","pubmed_publication_date":"06 Jan 2025","pubmed_entrez_date":"2024-10-08","publication_year":"2025","canto_session_key":"18a1ffa071403375","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-08-14 20:48:00","canto_approved_date":"2026-03-25 11:36:24","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-08-12 19:12:07","canto_added_date":"2024-10-08 23:25:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.20c","SPBC19C2.07","SPCC553.02","SPAC4A8.11c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2025-08-14"},{"uniquename":"PMID:33153481","title":"Fission yeast condensin contributes to interphase chromatin organization and prevents transcription-coupled DNA damage.","citation":"Genome Biol 2020 Nov 05;21(1):272","abstract":"Structural maintenance of chromosomes (SMC) complexes are central organizers of chromatin architecture throughout the cell cycle. The SMC family member condensin is best known for establishing long-range chromatin interactions in mitosis. These compact chromatin and create mechanically stable chromosomes. How condensin contributes to chromatin organization in interphase is less well understood.\nHere, we use efficient conditional depletion of fission yeast condensin to determine its contribution to interphase chromatin organization. We deplete condensin in G2-arrested cells to preempt confounding effects from cell cycle progression without condensin. Genome-wide chromatin interaction mapping, using Hi-C, reveals condensin-mediated chromatin interactions in interphase that are qualitatively similar to those observed in mitosis, but quantitatively far less prevalent. Despite their low abundance, chromatin mobility tracking shows that condensin markedly confines interphase chromatin movements. Without condensin, chromatin behaves as an unconstrained Rouse polymer with excluded volume, while condensin constrains its mobility. Unexpectedly, we find that condensin is required during interphase to prevent ongoing transcription from eliciting a DNA damage response.\nIn addition to establishing mitotic chromosome architecture, condensin-mediated long-range chromatin interactions contribute to shaping chromatin organization in interphase. The resulting structure confines chromatin mobility and protects the genome from transcription-induced DNA damage. This adds to the important roles of condensin in maintaining chromosome stability.","doi":"10.1186/s13059-020-02183-0","authors":"Kakui Y, Barrington C, Barry DJ, Gerguri T, Fu X, Bates PA, Khatri BS, Uhlmann F","authors_abbrev":"Kakui Y et al.","pubmed_publication_date":"05 Nov 2020","pubmed_entrez_date":"2020-11-06","publication_year":"2020","canto_session_key":"ba8221c44a2afd95","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasutaka Kakui","canto_first_approved_date":"2020-11-18 15:28:34","canto_approved_date":"2026-01-19 10:19:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-15 14:05:34","canto_added_date":"2020-11-11 01:15:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Yasutaka Kakui","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-11-18"},{"uniquename":"PMID:2666172","title":"Substrate structural requirements of Schizosaccharomyces pombe RNase P.","citation":"FEBS Lett 1989 Jul 17;251(1-2):84-8","abstract":"RNase P from Schizosaccharomyces pombe has been purified over 2000-fold. The apparent Km for two S. pombe tRNA precursors derived from the supS1 and sup3-e tRNA(Ser) genes is 20 nM; the apparent Vmax is 2.5 nM/min (supS1) and 1.1 nM/min (sup3-e). Processing studies with precursors of other mutants show that the structures of the acceptor stem and anticodon/intron loop of tRNA are crucial for S. pombe RNase P action.","authors":"Drainas D, Zimmerly S, Willis I, Söll D","authors_abbrev":"Drainas D et al.","pubmed_publication_date":"17 Jul 1989","pubmed_entrez_date":"1989-07-17","publication_year":"1989","canto_session_key":"782f093d22870ff5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 13:55:16","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-20 13:54:48","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.128"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:23101633","title":"Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells.","citation":"Cell 2012 Oct 26;151(3):671-83","abstract":"Data on absolute molecule numbers will empower the modeling, understanding, and comparison of cellular functions and biological systems. We quantified transcriptomes and proteomes in fission yeast during cellular proliferation and quiescence. This rich resource provides the first comprehensive reference for all RNA and most protein concentrations in a eukaryote under two key physiological conditions. The integrated data set supports quantitative biology and affords unique insights into cell regulation. Although mRNAs are typically expressed in a narrow range above 1 copy/cell, most long, noncoding RNAs, except for a distinct subset, are tightly repressed below 1 copy/cell. Cell-cycle-regulated transcription tunes mRNA numbers to phase-specific requirements but can also bring about more switch-like expression. Proteins greatly exceed mRNAs in abundance and dynamic range, and concentrations are regulated to functional demands. Upon transition to quiescence, the proteome changes substantially, but, in stark contrast to mRNAs, proteins do not uniformly decrease but scale with cell volume.","doi":"10.1016/j.cell.2012.09.019","authors":"Marguerat S, Schmidt A, Codlin S, Chen W, Aebersold R, Bähler J","authors_abbrev":"Marguerat S et al.","pubmed_publication_date":"26 Oct 2012","pubmed_entrez_date":"2012-10-30","publication_year":"2012","canto_session_key":"181fb7601c13bfc2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-11-01 16:38:51","canto_approved_date":"2017-11-01 16:38:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-31 17:58:11","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"file_curator_name":"Samuel Marguerat","file_curator_role":"community","annotation_file_curators":[{"name":"Samuel Marguerat","community_curator":true,"annotation_count":3400,"orcid":"0000-0002-2402-3165","file_type":"quantitative_gene_expression","file_name":"PMID_16224022_Marguerat_protein_proliferation_quantitative_expression.txt"},{"name":"Samuel Marguerat","community_curator":true,"annotation_count":2722,"orcid":"0000-0002-2402-3165","file_type":"quantitative_gene_expression","file_name":"PMID_16224022_Marguerat_protein_quiescence_quantitative_expression.txt"},{"name":"Samuel Marguerat","community_curator":true,"annotation_count":6892,"orcid":"0000-0002-2402-3165","file_type":"quantitative_gene_expression","file_name":"PMID_16224022_Marguerat_RNA_proliferation_quantitative_expression.txt"},{"name":"Samuel 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of the structural genes encoding M-factor in the fission yeast Schizosaccharomyces pombe: identification of a third gene, mfm3.","citation":"Mol Cell Biol 1994 Jun;14(6):3895-905","abstract":"We previously identified two genes, mfm1 and mfm2, with the potential to encode the M-factor mating pheromone of the fission yeast Schizosaccharomyces pombe (J. Davey, EMBO J. 11:951-960, 1992), but further analysis revealed that a mutant strain lacking both genes still produced active M-factor. Here we describe the isolation and characterization of a third M-factor gene, mfm3. A mutant lacking all three genes fails to produce M-factor, indicating that all functional M-factor genes now have been identified. The triple mutant exhibits an absolute mating defect in M cells, a defect that is not rescued by addition of exogenous M-factor. A mutational analysis reveals that all three mfm genes contribute to the production of M-factor. Their transcription is limited to M cells and requires the mat1-Mc and ste11 gene products. Each gene is induced when the cells are starved of nitrogen and further induced by a pheromone signal. Additionally, the signal transduction machinery associated with the pheromone response is required for transcription of the mfm genes in both stimulated and unstimulated cells.","authors":"Kjaerulff S, Davey J, Nielsen O","authors_abbrev":"Kjaerulff S et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_session_key":"4cf5f407a9f3d7f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-11 21:18:01","canto_approved_date":"2026-04-08 07:19:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-03-12 13:27:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":52,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.03","SPAC31G5.09c","SPCC1795.06","SPAC17H9.09c","SPBC23G7.09","SPBC24C6.06","SPBC1D7.05","SPAC1D4.13","SPAPB8E5.05","SPAC513.03","SPBC32C12.02","SPMTR.01"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2018-06-11"},{"uniquename":"PMID:5020213","title":"The microbiological assay of total and free inositol with Schizosaccharomyces pombe.","citation":"Analyst 1972 Jan;97(150):74-6","abstract":"","authors":"Barton-Wright EC","authors_abbrev":"Barton-Wright EC","pubmed_publication_date":"Jan 1972","pubmed_entrez_date":"1972-01-01","publication_year":"1972","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41203586","title":"Identification of an ERGIC-Like Compartment in Fission Yeast: Emp43 Functions as a Lectin-Like Cargo Receptor for Glycosylated Proteins.","citation":"Mol Microbiol 2025 Nov 07;","abstract":"The endoplasmic reticulum-Golgi intermediate compartment (ERGIC) plays a crucial role in the secretory pathway; however, its existence and function in lower eukaryotes remain largely unexamined. In this study, we identified Emp43 (SPBC4F6.05c) of Schizosaccharomyces pombe, an orthologue of human (Homo sapiens) ERGIC-53, and demonstrated its localization to an ERGIC-like compartment. The localization of Emp43 depended on its C-terminal KYL motif and oligomerization through the CC1 domain. Deletion of S. pombe emp43 +  resulted in significant sensitivity to MgCl 2  and FK506, along with defects in septum integrity, indicating a role in cell wall maintenance. Further analysis identified Ssp120 of S. pombe, an orthologue of human MCFD2, as a functional partner of Emp43. Yeast two-hybrid assays confirmed a strong interaction between Emp43 and Ssp120, and both proteins co-localized within an ERGIC-like compartment. Additionally, we identified Meu17 of S. pombe, a glucan-α-1,4-glucosidase homolog, as a potential ligand for Emp43. Overexpression of Meu17 rescued MgCl 2  sensitivity in both emp43Δ and ssp120Δ strains, while mutations in its N-linked glycosylation sites (N383, N409) or its predicted active site (D203) disrupted its septum localization and functional rescue capability. Our findings indicate that Emp43 forms a complex with Ssp120 to facilitate the transport of glycosylated proteins, such as Meu17, within an ERGIC-like compartment in fission yeast S. pombe. This study provides the first evidence of an ERGIC-like structure in S. pombe and highlights the conserved nature of ERGIC-associated mechanisms across eukaryotes.","doi":"10.1111/mmi.70033","authors":"Imamura I, Kawaguchi S, Suzuki S, Kamiya Y, Ohnishi Y, Ueda J, Nashiki K, Takegawa K, Tabuchi M, Tanaka N","authors_abbrev":"Imamura I et al.","pubmed_publication_date":"07 Nov 2025","pubmed_entrez_date":"2025-11-07","publication_year":"2025","canto_session_key":"10bfbfdfd68196fc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2026-04-07 08:33:40","canto_approved_date":"2026-05-06 08:20:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-03-03 21:11:53","canto_added_date":"2025-11-10 00:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":86,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC613.03","SPAC23A1.12c","SPBC11C11.02","SPBC1604.12","SPAC23H4.06","SPBC4F6.05c","SPBP4H10.04","SPBP8B7.06","SPBC14C8.05c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2026-04-07"},{"uniquename":"PMID:8089179","title":"Human gamma-tubulin functions in fission yeast.","citation":"J Cell Biol 1994 Sep;126(6):1465-73","abstract":"gamma-Tubulin is a phylogenetically conserved component of microtubule-organizing centers that is essential for viability and microtubule function. To examine the functional conservation of gamma-tubulin, we have tested the ability of human gamma-tubulin to function in the fission yeast Schizosaccharomyces pombe. We have found that expression of a human gamma-tubulin cDNA restores viability and a near-normal growth rate to cells of S. pombe lacking endogenous gamma-tubulin. Immunofluorescence microscopy showed that these cells contained normal mitotic spindles and interphase microtubule arrays, and that human gamma-tubulin, like S. pombe gamma-tubulin, localized to spindle pole bodies, the fungal microtubule-organizing centers. These results demonstrate that human gamma-tubulin functions in fission yeast, and they suggest that in spite of the great morphological differences between the microtubule-organizing centers of humans and fission yeasts, gamma-tubulin is likely to perform the same tasks in both. They suggest, moreover, that the proteins that interact with gamma-tubulin, including, most obviously, microtubule-organizing center proteins, must also be conserved. We have also found that a fivefold overexpression of S. pombe gamma-tubulin causes no reduction in growth rates or alteration of microtubule organization. We hypothesize that the excess gamma-tubulin is maintained in the cytoplasm in a form incapable of nucleating microtubule assembly. Finally, we have found that expression of human gamma-tubulin or overexpression of S. pombe gamma-tubulin causes no significant alteration of resistance to the antimicrotubule agents benomyl, thiabendazole and nocodazole.","authors":"Horio T, Oakley BR","authors_abbrev":"Horio T et al.","pubmed_publication_date":"Sep 1994","pubmed_entrez_date":"1994-09-01","publication_year":"1994","canto_session_key":"ef3d2810e01d19cb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:25:07","canto_session_submitted_date":"2012-03-03 15:24:53","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.04"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:27343268","title":"Determination of the Frequency of Minichromosome Loss to Assess Chromosome Stability in Fission Yeast.","citation":"Cold Spring Harb Protoc 2018 Mar 01;2018(3)","abstract":"Quantitative assessment of chromosome stability in specific genetic backgrounds or under conditions of environmental stress can be addressed by direct cytological examination of chromosome transmission errors (using live or fixed imaging); however, in many cases, this is impractical, particularly when the rate of loss is low. Model chromosomes that allow simple and convenient assessment of chromosome stability are therefore useful. Ch16 is a 530-kb minichromosome constructed by the deletion of large portions of chromosome 3 termini. Ch16 carries the  ade6-M216  allele, which interallelically complements the  ade6-M210  mutation. Hence, Ade +  is an indication of the presence of Ch16, and Ade -  indicates its loss. Ade +  and Ade -  are phenotypically discernible as white and red colonies, respectively, on media containing limiting amounts of adenine. When a single cell bearing Ch16 divides on a plate to give rise to two daughter cells, one of which has lost Ch16, it will result in the formation of a half-sectored colony (half of the colony is red and the other half is white). The frequency of half-sectored colonies provides an accurate estimate of mitotic minichromosome loss per cell division. This protocol describes a method to determine half-sectored colony frequency and potential problems associated with the method.","doi":"10.1101/pdb.prot091991","authors":"Niwa O","authors_abbrev":"Niwa O","pubmed_publication_date":"01 Mar 2018","pubmed_entrez_date":"2016-06-26","publication_year":"2018","canto_session_key":"0596d61423e232f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-06-29 14:46:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-06-29 14:46:16","canto_added_date":"2016-06-29 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2016-06-29"},{"uniquename":"PMID:23468430","title":"Intronic sequence elements impede exon ligation and trigger a discard pathway that yields functional telomerase RNA in fission yeast.","citation":"Genes Dev 2013 Mar 15;27(6):627-38","abstract":"The fission yeast telomerase RNA (TER1) precursor harbors an intron immediately downstream from its mature 3' end. Unlike most introns, which are removed from precursor RNAs by the spliceosome in two sequential but tightly coupled transesterification reactions, TER1 only undergoes the first cleavage reaction during telomerase RNA maturation. The mechanism underlying spliceosome-mediated 3' end processing has remained unclear. We now demonstrate that a strong branch site (BS), a long distance to the 3' splice site (3' SS), and a weak polypyrimidine (Py) tract act synergistically to attenuate the transition from the first to the second step of splicing. The observation that a strong BS antagonizes the second step of splicing in the context of TER1 suggests that the BS-U2 snRNA interaction is disrupted after the first step and thus much earlier than previously thought. The slow transition from first to second step triggers the Prp22 DExD/H-box helicase-dependent rejection of the cleaved products and Prp43-dependent \"discard\" of the splicing intermediates. Our findings explain how the spliceosome can function in 3' end processing and provide new insights into the mechanism of splicing.","doi":"10.1101/gad.212738.112","authors":"Kannan R, Hartnett S, Voelker RB, Berglund JA, Staley JP, Baumann P","authors_abbrev":"Kannan R et al.","pubmed_publication_date":"15 Mar 2013","pubmed_entrez_date":"2013-03-08","publication_year":"2013","canto_session_key":"81a17ee0dd146a18","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35231427","title":"Physical properties of the cytoplasm modulate the rates of microtubule polymerization and depolymerization.","citation":"Dev Cell 2022 Feb 28;57(4):466-479.e6","abstract":"The cytoplasm is a crowded, visco-elastic environment whose physical properties change according to physiological or developmental states. How the physical properties of the cytoplasm impact cellular functions in vivo remains poorly understood. Here, we probe the effects of cytoplasmic concentration on microtubules by applying osmotic shifts to fission yeast, moss, and mammalian cells. We show that the rates of both microtubule polymerization and depolymerization scale linearly and inversely with cytoplasmic concentration; an increase in cytoplasmic concentration decreases the rates of microtubule polymerization and depolymerization proportionally, whereas a decrease in cytoplasmic concentration leads to the opposite. Numerous lines of evidence indicate that these effects are due to changes in cytoplasmic viscosity rather than cellular stress responses or macromolecular crowding per se. We reconstituted these effects on microtubules in vitro by tuning viscosity. Our findings indicate that, even in normal conditions, the viscosity of the cytoplasm modulates the reactions that underlie microtubule dynamic behaviors.","doi":"10.1016/j.devcel.2022.02.001","authors":"Molines AT, Lemière J, Gazzola M, Steinmark IE, Edrington CH, Hsu CT, Real-Calderon P, Suhling K, Goshima G, Holt LJ, Thery M, Brouhard GJ, Chang F","authors_abbrev":"Molines AT et al.","pubmed_publication_date":"28 Feb 2022","pubmed_entrez_date":"2022-03-01","publication_year":"2022","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2022-03-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23886939","title":"Functional replacement of fission yeast γ-tubulin small complex proteins Alp4 and Alp6 by human GCP2 and GCP3.","citation":"J Cell Sci 2013 Oct 01;126(Pt 19):4406-13","abstract":"Microtubule-organizing centers such as the γ-tubulin ring complex (γ-TuRC) act as a template for polarized growth and regulation of microtubules that are essential for diverse cellular structures and processes in eukaryotes. New structural models of the budding yeast γ-tubulin small complex (γ-TuSC) of the γ-TuRC combined with functional studies done in multiple eukaryotes are revealing the first mechanistic clues into control of microtubule nucleation and organization. Cross-species studies of human and budding yeast γ-TuSC proteins in fission yeast revealed conserved and divergent structural and functional features of the γ-TuSC. We show genetically that GCP3/Spc98 function is fully conserved with Alp6 across species but that functional differences exist between GCP2/Spc97 and Alp4. By further analysis of human γ-TuSC proteins, we found that GCP3 assembles normally into the >2000 kDa fission yeast γ-TuRC and that the GCP3 gene replaces fission yeast alp6. Interestingly, human GCP2 replaces the essential alp4 gene but is unable to rescue a normally recessive G1 defect of the alp4-1891 allele that results in loss of γ-TuRC from poles in subsequent cell cycles. Biochemically, GCP2 incorporation into fission yeast γ-TuRC is limited in the presence of Alp4; instead, the bulk of GCP2 fractionates as smaller complexes. By generating a functional Alp4-GCP2 chimeric protein we determined that the GCP2 N-terminal domain limits its ability to fully displace or compete with Alp4 during γ-TuRC assembly. Our findings have broad importance for understanding the essential domains of γ-TuSC proteins in the γ-TuRC mechanism.","doi":"10.1242/jcs.128173","authors":"Riehlman TD, Olmsted ZT, Branca CN, Winnie AM, Seo L, Cruz LO, Paluh JL","authors_abbrev":"Riehlman TD et al.","pubmed_publication_date":"01 Oct 2013","pubmed_entrez_date":"2013-07-27","publication_year":"2013","canto_session_key":"ed40a927a6bbe61b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC365.15","SPBC428.20c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8673016","title":"Evidences for possible involvement of Rhp51 protein in mitotic events including chromosome segregation.","citation":"Biochem Mol Biol Int 1995 Oct;37(2):329-37","abstract":"To understand the role of the Rhp51 protein in Schizosaccharomyces pombe, we examined the phenotypes of the null mutant for the rhp51+ gene. Unlike Saccharomyces cerevisiae rad51 mutants, S. pombe rhp51 mutants (rhp51delta cells) displayed slow growth and heterogeneity in cell size, indicating perturbation of the cell cycle. Furthermore, many aberrant nuclear structures found in 4',6'-diamidino-2-phenylindole (DAPI)-stained rhp51delta cells and the caffeine hypersensitivity of the mutant cells suggested an involvement of the Rhp51 protein in normal chromosome segregation. These data suggested that the Rhp51 proteins were required for normal cell growth as well as a DNA repair pathway. Moreover, rhp51delta mutants showed a considerable sensitivity to ultraviolet (UV) light-irradiation as well as methyl methanesulfonate (MMS) treatment, indicating that the Rhp51 proteins are involved in both the active excision mechanism of UV-induced DNA damage and recombinational repair in S. pombe. Taken together, we suggest that the role(s) of the Rhp51 protein in S. pombe may be different from those of Rad51 in S. cerevisiae.","authors":"Jang YK, Jin YH, Shim YS, Kim MJ, Yoo EJ, Seong RH, Hong SH, Park SD","authors_abbrev":"Jang YK et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9390410","title":"Backbone assignment of double labelled 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe.","citation":"J Biomol NMR 1997 Oct;10(3):309-10","abstract":"","authors":"Uhrínová S, Uhrín D, Nairn J, Price NC, Fothergill-Gilmore LA, Barlow PN","authors_abbrev":"Uhrínová S et al.","pubmed_publication_date":"Oct 1997","pubmed_entrez_date":"1997-12-09","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12697061","title":"Fission yeast Rad26 responds to DNA damage independently of Rad3.","citation":"BMC Genet 2003 Apr 03;4:6","abstract":"The Rad26/Rad3 complex in fission yeast detects genotoxic insults and initiates the cell cycle arrest and recovery activities of the DNA damage checkpoint. To investigate how the Rad26/Rad3 complex performs these functions, we constructed and characterized Rad26-GFP.\nRad26-GFP localized to approximately six nuclear dots in cycling cells. Following treatment with a DNA damaging agent, Rad26-GFP localization changed. Damaged cells contained one or two bright Rad26-GFP spots, in addition to smaller, more numerous Rad26-GFP speckles. Genetic analyses demonstrated that these Rad26-GFP patterns (dots, spots and speckles) were unaffected by null mutations in other DNA damage checkpoint genes, including rad3+. Data obtained with our Rad26.T12-GFP fusion protein correlate spots with cell cycle arrest activities and speckles with DNA repair activities. In addition, physiological experiments demonstrated that rad26Delta and rad3Delta alleles confer sensitivity to a microtubule-depolymerizing drug.\nWe have discovered three distinct Rad26-GFP cellular structures. Formation of these structures did not require other checkpoint proteins. These data demonstrate that Rad26 can respond to genotoxic insult in the absence of Rad3 and the other checkpoint Rad proteins.","authors":"Wolkow TD, Enoch T","authors_abbrev":"Wolkow TD et al.","pubmed_publication_date":"03 Apr 2003","pubmed_entrez_date":"2003-04-17","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9E9.08"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:554533","title":"Temperature sensitivity of flocculation induction, conjugation and sporulation in fission yeast.","citation":"Antonie Van Leeuwenhoek 1979;45(3):391-400","abstract":"Homothallic cultures of Schizosaccharomyces pombe, anaerobically grown to stationary phase in broth at 32 degrees C, were induced by aeration to flocculate. Flocculation was followed by copulation, conjugation, zygote formation, meiosis and sporulation. Cultures grown to stationary phase at 32 degrees C and then aerated at 37 degrees C did not sporulate. Grown to stationary phase at 37 degrees C, cultures were not immediately inducible when aerated at 32 degrees C. To identify which events in the developmental sequence were thermosensitive, we grew and induced cultures at 32 degrees C and then shifted them at various times to 37 degrees C. We observed the following events to be thermosensitive: development of respiratory sufficiency, readiness (inducibility of a culture within 1 h), flocculation induction, copulation, conjugation and early sporulation (including meiosis). Respiration, flocculation and spore maturation were thermoresistant. Conjugation-induced lysis and postdevelopmental deflocculation were enhanced at 37 degrees C.","authors":"Calleja GB, Johnson BF","authors_abbrev":"Calleja GB et al.","pubmed_publication_date":"1979","pubmed_entrez_date":"1979-01-01","publication_year":"1979","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26527280","title":"Robust Ordering of Anaphase Events by Adaptive Thresholds and Competing Degradation Pathways.","citation":"Mol Cell 2015 Nov 05;60(3):446-59","abstract":"The splitting of chromosomes in anaphase and their delivery into the daughter cells needs to be accurately executed to maintain genome stability. Chromosome splitting requires the degradation of securin, whereas the distribution of the chromosomes into the daughter cells requires the degradation of cyclin B. We show that cells encounter and tolerate variations in the abundance of securin or cyclin B. This makes the concurrent onset of securin and cyclin B degradation insufficient to guarantee that early anaphase events occur in the correct order. We uncover that the timing of chromosome splitting is not determined by reaching a fixed securin level, but that this level adapts to the securin degradation kinetics. In conjunction with securin and cyclin B competing for degradation during anaphase, this provides robustness to the temporal order of anaphase events. Our work reveals how parallel cell-cycle pathways can be temporally coordinated despite variability in protein concentrations.","doi":"10.1016/j.molcel.2015.09.022","authors":"Kamenz J, Mihaljev T, Kubis A, Legewie S, Hauf S","authors_abbrev":"Kamenz J et al.","pubmed_publication_date":"05 Nov 2015","pubmed_entrez_date":"2015-11-04","publication_year":"2015","canto_session_key":"f8b9e68a8b938c8d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silke Hauf","canto_first_approved_date":"2020-06-16 14:13:15","canto_approved_date":"2026-06-26 11:19:58","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-06-14 18:55:41","canto_added_date":"2016-02-14 01:15:14","annotation_curators":[{"name":"Silke Hauf","community_curator":true,"annotation_count":17,"orcid":"0000-0001-5938-721X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":"quantitative_gene_expression","file_name":"PMID_26527280_Kamenz_protein_quantitative_expression.txt"}],"genes":["SPAC23C11.16","SPAC24H6.05","SPCC338.17c","SPCC5E4.04","SPAC6F12.15c","SPAC637.10c","SPBC11B10.09","SPBC20F10.06","SPAC144.13c","SPAC821.08c","SPBC582.03","SPBC14C8.01c","SPAC17C9.13c","SPAC31G5.13"],"gene_count":14,"ltp_gene_count":7,"approved_date":"2020-06-16"},{"uniquename":"PMID:24006493","title":"Mzt1/Tam4, a fission yeast MOZART1 homologue, is an essential component of the γ-tubulin complex and directly interacts with GCP3(Alp6).","citation":"Mol Biol Cell 2013 Nov;24(21):3337-49","abstract":"In humans, MOZART1 plays an essential role in mitotic spindle formation as a component of the γ-tubulin ring complex. We report that the fission yeast homologue of MOZART1, Mzt1/Tam4, is located at microtubule-organizing centers (MTOCs) and coimmunoprecipitates with γ-tubulin Gtb1 from cell extracts. We show that mzt1/tam4 is an essential gene in fission yeast, encoding a 64-amino acid peptide, depletion of which leads to aberrant microtubule structure, including malformed mitotic spindles and impaired interphase microtubule array. Mzt1/Tam4 depletion also causes cytokinesis defects, suggesting a role of the γ-tubulin complex in the regulation of cytokinesis. Yeast two-hybrid analysis shows that Mzt1/Tam4 forms a complex with Alp6, a fission yeast homologue of γ-tubulin complex protein 3 (GCP3). Biophysical methods demonstrate that there is a direct interaction between recombinant Mzt1/Tam4 and the N-terminal region of GCP3(Alp6). Together our results suggest that Mzt1/Tam4 contributes to the MTOC function through regulation of GCP3(Alp6).","doi":"10.1091/mbc.E13-05-0253","authors":"Dhani DK, Goult BT, George GM, Rogerson DT, Bitton DA, Miller CJ, Schwabe JW, Tanaka K","authors_abbrev":"Dhani DK et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-09-06","publication_year":"2013","canto_session_key":"7b2ad53e7a1727a2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kayoko Tanaka","canto_first_approved_date":"2015-04-04 07:05:42","canto_approved_date":"2022-08-30 08:39:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-22 10:34:26","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Kayako Tanaka","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Kayoko Tanaka","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":3,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.20c","SPAC9G1.15c","SPBC365.15","SPBC32F12.04"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-04-04"},{"uniquename":"PMID:15157885","title":"Choosing and using Schizosaccharomyces pombe plasmids.","citation":"Methods 2004 Jul;33(3):189-98","abstract":"A wide range of plasmids has been developed for molecular studies in the fission yeast Schizosaccharomyces pombe. This includes general purpose episomes, expression vectors, epitope tagging plasmids, and integration vectors. This review describes the typical features of S. pombe vectors, including replication origins, positive and negative selection markers, and constitutive and inducible promoter systems. We will also discuss vectors with epitope tags and how these can be used to modify episomal or endogenous gene sequences. Considerations for choosing and using a plasmid are presented and specialized methods are described.","authors":"Siam R, Dolan WP, Forsburg SL","authors_abbrev":"Siam R et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8315659","title":"A fungal phylogeny based upon orotidine 5'-monophosphate decarboxylase.","citation":"J Mol Evol 1993 Apr;36(4):389-95","abstract":"Orotidine 5'-monophosphate decarboxylase protein sequences from 14 fungi, 1 slime mold, 2 mammals, and 3 bacteria are compared and aligned and shown to be homologous. Based on the optimal alignment of the fungal sequences, a phylogenetic tree is derived. Within the fungi, the fission yeast Schizosaccharomyces pombe shows a closer relationship to both basidiomycetes and phycomycetes than it does to orthodox ascomycetes (plectomycetes, pyrenomycetes, and budding yeasts). Intron conservation shows a close relationship between phycomycetes and basidiomycetes. The imperfect fungi Trichoderma and Cephalosporium are shown to be closely related to Neurospora. The predicted origin of the group of budding yeasts is dependent on the analytical method used.","authors":"Radford A","authors_abbrev":"Radford A","pubmed_publication_date":"Apr 1993","pubmed_entrez_date":"1993-04-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9301025","title":"Mapping of ure1, ure2 and ure3 markers in fission yeast.","citation":"Yeast 1997 Sep 30;13(12):1195-7","abstract":"The following urease genes of the fission yeast Schizosaccharomyces pombe have been mapped by induced haploidization and tetrad analysis--ure1: chromosome are III-L; ure2 and ure3: chromosome are I-R. The previously determined tps19-rad1 interval (11-12 cM) has been increased to 18 cM. A convenient medium for rapidly scoring the ure gene markers of fission yeast was developed.","authors":"Lubbers MW, Thornton RJ, Honey NK","authors_abbrev":"Lubbers MW et al.","pubmed_publication_date":"30 Sep 1997","pubmed_entrez_date":"1997-09-25","publication_year":"1997","canto_session_key":"30e1bdcc27bfaabd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"antonia lock","canto_approved_date":"2017-06-30 11:16:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-06-30 11:14:25","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"antonia lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22G7.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-06-30"},{"uniquename":"PMID:17114925","title":"A cullin E3 ubiquitin ligase complex associates with Rik1 and the Clr4 histone H3-K9 methyltransferase and is required for RNAi-mediated heterochromatin formation.","citation":"RNA Biol 2005;2(3):106-11","abstract":"The assembly of heterochromatin in fission yeast and metazoans requires histone H3-lysine 9 (-K9) methylation by the conserved Clr4/Suv39h methyltransferase. In fission yeast, H3-K9 methylation requires components of the RNAi machinery and is initiated by the RNA-Induced Transcriptional Silencing (RITS) complex. Here we report the purification of a novel complex that associates with the Clr4 methyltransferase, termed the CLRC (CLr4-Rik1-Cul4) complex. By affinity purification of the Clr4-associated protein Rik1, we show that, in addition to Clr4, Rik1 is associated with the fission yeast E3 ubiquitin ligase Cullin4 (Cul4, encoded by cul4(+)), the ubiquitin-like protein, Ned8, and two previously uncharacterized proteins, designated Cmc1 and Cmc2. In addition, the complex contains substochiometric amounts of histones H2B and H4, and the 14-3-3 protein, Rad24. Deletion of cul4(+), cmc1(+), cmc2(+) and rad24(+) results in a complete loss of silencing of a ura4(+) reporter gene inserted within centromeric DNA repeats or the silent mating type locus. Each of the above deletions also results in accumulation of noncoding RNAs transcribed from centromeric repeats and telomeric DNA regions, and a corresponding loss of small RNAs that are homologous to centromeric repeats, suggesting a defect in the processing of noncoding RNA to small RNA. Based on these results, we propose that the components of the Clr4-Rik1-Cul4 complex act concertedly at an early step in heterochromatin formation.","authors":"Hong EJ, Villén J, Gerace EL, Gygi SP, Moazed D","authors_abbrev":"Hong EJ et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2006-11-23","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC613.12c","SPAC3A11.08","SPCC970.07c","SPAC1834.03c","SPCC622.09","SPAC23H4.18c","SPBC428.08c","SPCC11E10.08","SPBC12D12.08c","SPAC8E11.02c"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:8443406","title":"Functional homology of protein kinases required for sexual differentiation in Schizosaccharomyces pombe and Saccharomyces cerevisiae suggests a conserved signal transduction module in eukaryotic organisms.","citation":"Mol Biol Cell 1993 Jan;4(1):107-20","abstract":"We present genetic evidence that three presumptive protein kinases of Schizosaccharomyces pombe, byr2, byr1, and spk1 that are structurally related to protein kinases of Saccharomyces cerevisiae, STE11, STE7, and FUS3, respectively, are also functionally related. In some cases, introduction of the heterologous protein kinase into a mutant was sufficient for complementation. In other cases (as in a ste11- mutant of S. cerevisiae), expression of two S. pombe protein kinases (byr2 and byr1) was required to observe complementation, suggesting that byr2 and byr1 act cooperatively. Complementation in S. pombe mutants is observed as restoration of sporulation and conjugation and in S. cerevisiae as restoration of conjugation, pheromone-induced cell cycle arrest, and pheromone-induced transcription of the FUS1 gene. We also show that the S. pombe kinases bear a similar relationship to the mating pheromone receptor apparatus as do their S. cerevisiae counterparts. Our results indicate that pheromone-induced signal transduction employs a conserved set of kinases in these two evolutionarily distant yeasts despite an apparently significant difference in function of the heterotrimeric G proteins. We suggest that the STE11/byr2, STE7/byr1, and FUS3/spk1 kinases comprise a signal transduction module that may be conserved in higher eukaryotes. Consistent with this hypothesis, we show that a mammalian mitogen-activated protein (MAP) kinase, ERK2, can partially replace spk1 function in S. pombe.","authors":"Neiman AM, Stevenson BJ, Xu HP, Sprague GF, Herskowitz I, Wigler M, Marcus S","authors_abbrev":"Neiman AM et al.","pubmed_publication_date":"Jan 1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_session_key":"986cd0e5341a9fe8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-14 22:00:25","canto_approved_date":"2025-12-12 18:49:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-05 22:32:42","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.09c","SPAC17H9.09c","SPBC1D7.05","SPBC24C6.06","SPAC1D4.13"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-06-14"},{"uniquename":"PMID:19959363","title":"Cytokinesis and the contractile ring in fission yeast: towards a systems-level understanding.","citation":"Trends Microbiol 2010 Jan;18(1):38-45","abstract":"Cytokinesis, the final stage of the cell division cycle, requires the proper placement, assembly and contraction of an actomyosin-based contractile ring. Conserved sets of cytokinesis proteins and pathways have now been identified and characterized functionally. Additionally, fluorescent protein fusion technology enables quantitative high-resolution imaging of protein dynamics in living cells. For these reasons, the study of cytokinesis is now ripe for quantitative, systems-level approaches. Here, we review our current understanding of the molecular mechanisms of contractile ring dynamics in the model organism Schizosaccharomyces pombe (fission yeast), focusing on recent examples that illustrate a synergistic integration of quantitative experimental data with computational modeling. A picture of a highly dynamic and integrated system consisting of overlapping networks is beginning to emerge, the detailed nature of which remains to be elucidated.","doi":"10.1016/j.tim.2009.10.002","authors":"Bathe M, Chang F","authors_abbrev":"Bathe M et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-12-05","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21642440","title":"Actin filament bundling by fimbrin is important for endocytosis, cytokinesis, and polarization in fission yeast.","citation":"J Biol Chem 2011 Jul 29;286(30):26964-77","abstract":"Through the coordinated action of diverse actin-binding proteins, cells simultaneously assemble actin filaments with distinct architectures and dynamics to drive different processes. Actin filament cross-linking proteins organize filaments into higher order networks, although the requirement of cross-linking activity in cells has largely been assumed rather than directly tested. Fission yeast Schizosaccharomyces pombe assembles actin into three discrete structures: endocytic actin patches, polarizing actin cables, and the cytokinetic contractile ring. The fission yeast filament cross-linker fimbrin Fim1 primarily localizes to Arp2/3 complex-nucleated branched filaments of the actin patch and by a lesser amount to bundles of linear antiparallel filaments in the contractile ring. It is unclear whether Fim1 associates with bundles of parallel filaments in actin cables. We previously discovered that a principal role of Fim1 is to control localization of tropomyosin Cdc8, thereby facilitating cofilin-mediated filament turnover. Therefore, we hypothesized that the bundling ability of Fim1 is dispensable for actin patches but is important for the contractile ring and possibly actin cables. By directly visualizing actin filament assembly using total internal reflection fluorescence microscopy, we determined that Fim1 bundles filaments in both parallel and antiparallel orientations and efficiently bundles Arp2/3 complex-branched filaments in the absence but not the presence of actin capping protein. Examination of cells exclusively expressing a truncated version of Fim1 that can bind but not bundle actin filaments revealed that bundling activity of Fim1 is in fact important for all three actin structures. Therefore, fimbrin Fim1 has diverse roles as both a filament \"gatekeeper\" and as a filament cross-linker.","doi":"10.1074/jbc.M111.239004","authors":"Skau CT, Courson DS, Bestul AJ, Winkelman JD, Rock RS, Sirotkin V, Kovar DR","authors_abbrev":"Skau CT et al.","pubmed_publication_date":"29 Jul 2011","pubmed_entrez_date":"2011-06-07","publication_year":"2011","canto_session_key":"4290cb5e2c94dfb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-07 16:09:52","canto_approved_date":"2023-03-23 14:15:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-07 16:09:41","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.06c","SPAC6F6.10c","SPBC1778.06c","SPCC1919.10c","SPAC17G8.04c","SPBC1778.08c","SPAC12B10.07","SPAC15A10.08","SPAC6G9.07c","SPAC27F1.02c","SPBC14C8.06","SPAC11H11.06","SPAC630.03","SPAC631.01c"],"gene_count":14,"ltp_gene_count":9,"approved_date":"2017-07-07"},{"uniquename":"PMID:5159831","title":"Synchronization of cell divisions in the fission yeast, Schizosaccharomyces pombe, using heat shocks.","citation":"C R Trav Lab Carlsberg 1971;38(18):351-68","abstract":"","authors":"Kramhoft B, Zeuthen E","authors_abbrev":"Kramhoft B et al.","pubmed_publication_date":"1971","pubmed_entrez_date":"1971-01-01","publication_year":"1971","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37805140","title":"Crosstalk between the tRNA methyltransferase Trm1 and RNA chaperone La influences eukaryotic tRNA maturation.","citation":"J Biol Chem 2023 Nov;299(11):105326","abstract":"tRNAs undergo an extensive maturation process involving posttranscriptional modifications often associated with tRNA structural stability and promoting the native fold. Impaired posttranscriptional modification has been linked to human disease, likely through defects in translation, mitochondrial function, and increased susceptibility to degradation by various tRNA decay pathways. More recently, evidence has emerged that bacterial tRNA modification enzymes can act as tRNA chaperones to guide tRNA folding in a manner independent from catalytic activity. Here, we provide evidence that the fission yeast tRNA methyltransferase Trm1, which dimethylates nuclear- and mitochondrial-encoded tRNAs at G26, can also promote tRNA functionality in the absence of catalysis. We show that WT and catalytic-dead Trm1 are active in an in vivo tRNA-mediated suppression assay and possess RNA strand annealing and dissociation activity in vitro, similar to previously characterized RNA chaperones. Trm1 and the RNA chaperone La have previously been proposed to function synergistically in promoting tRNA maturation, yet we surprisingly demonstrate that La binding to nascent pre-tRNAs decreases Trm1 tRNA dimethylation in vivo and in vitro. Collectively, these results support the hypothesis for tRNA modification enzymes that combine catalytic and noncatalytic activities to promote tRNA maturation, as well as expand our understanding of how La function can influence tRNA modification.","doi":"10.1016/j.jbc.2023.105326","authors":"Porat J, Vakiloroayaei A, Remnant BM, Talebi M, Cargill T, Bayfield MA","authors_abbrev":"Porat J et al.","pubmed_publication_date":"Nov 2023","pubmed_entrez_date":"2023-10-07","publication_year":"2023","canto_session_key":"269782b0ebb602b9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jennifer Porat","canto_first_approved_date":"2023-11-10 12:11:02","canto_approved_date":"2025-05-20 12:30:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-13 15:53:08","canto_added_date":"2023-10-08 23:25:04","annotation_curators":[{"name":"Jennifer Porat","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBTRNALEU.09","SPAC31G5.12c","SPCTRNALEU.11","SPBTRNALEU.08","SPBC25D12.05","SPATRNASER.03","SPCTRNASER.11","SPATRNALEU.04","SPBTRNALEU.10","SPAC57A10.10c"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2023-11-10"},{"uniquename":"EMBL:SPC09468","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008190","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30471998","title":"Dip1 Co-opts Features of Branching Nucleation to Create Linear Actin Filaments that Activate WASP-Bound Arp2/3 Complex.","citation":"Curr Biol 2018 Dec 03;28(23):3886-3891.e4","abstract":"When activated by Wiskott-Aldrich syndrome proteins (WASP), Arp2/3 complex nucleates branched actin filaments important for processes like cellular motility and endocytosis [1]. WASP-mediated activation of Arp2/3 complex requires a preformed actin filament, ensuring that activation by WASP creates branched instead of linear filaments. However, this biochemical requirement also means that assembly of branched actin networks must be primed with an initial seed filament [2-4]. We recently described a class of activators called WISH/DIP/SPIN90 (WDS) proteins, which, unlike WASP, activate Arp2/3 complex without a preformed filament [4]. Although this property may allow WDS proteins to serve as seed filament generators, it is unknown whether actin filaments nucleated by WDS-activated Arp2/3 complex can activate WASP-bound Arp2/3 complex. Further, despite their potential importance as branched actin network initiators, little is known about how WDS proteins turn on Arp2/3 complex. Here, we use two-color single-molecule total internal reflection fluorescence (TIRF) microscopy to show that Dip1, the S. pombe WDS protein [5], co-opts features of branching nucleation to activate Arp2/3 complex. Specifically, it activates Arp2/3 complex to nucleate linear filaments analogous to the branch created by WASP-mediated activation. The barbed ends of Dip1-Arp2/3 nucleated filaments are free to elongate, and their pointed ends remain anchored to Dip1-bound Arp2/3 complex. The linear filaments nucleated by Dip1-bound Arp2/3 complex activate WASP-bound Arp2/3 complex as potently as spontaneously nucleated or branched actin filaments. These observations provide important insights into the regulation of Arp2/3 complex by its activators and the molecular basis for initiation of branched actin networks.","doi":"10.1016/j.cub.2018.10.045","authors":"Balzer CJ, Wagner AR, Helgeson LA, Nolen BJ","authors_abbrev":"Balzer CJ et al.","pubmed_publication_date":"03 Dec 2018","pubmed_entrez_date":"2018-11-26","publication_year":"2018","canto_session_key":"5aa10f6490885b2e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Connor Balzer","canto_first_approved_date":"2018-12-12 16:45:37","canto_approved_date":"2022-09-21 18:46:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-05 18:04:35","canto_added_date":"2018-11-27 01:15:04","annotation_curators":[{"name":"Connor Balzer","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC24C6.10c","SPAC4F10.15c","SPAC630.03","SPAC11H11.06"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-12-12"},{"uniquename":"PMID:19795185","title":"Nitric oxide as a signaling molecule in the fission yeast Schizosaccharomyces pombe.","citation":"Protoplasma 2009 Dec;238(1-4):59-66","abstract":"Nitric oxide synthases (NOS) catalyze the synthesis of ubiquitous signaling molecule nitric oxide (NO) which controls numerous biological processes. Using a spectrofluorometric NOS assay, we have measured the rate of total NO production in the crude cell extracts of Schizosaccharomyces pombe. NO production was reduced in the absence of NOS cofactors calmodulin and tetrahydrobiopterin, and a competitive NOS inhibitor NG-nitro-L-arginine methyl ester (L-NAME) was able to cause a statistically significant inhibition on the rate of total NO production. These results, for the first time, provide evidence that an enzyme with a NOS-like activity may be present in the fission yeast. In order to assess the possible regulatory roles of NO as a signaling molecule in this yeast, using the differential display technique, we screened for NO-responsive genes whose expression decreased upon exposure to L-NAME and increased in response to an NO donor, sodium nitroprusside treatment. Differential expression patterns of byr1, pek1, sid1, and wis1 genes were confirmed by quantitative real-time PCR. The physiological experiments performed based on the functions and molecular interactions of these genes have pointed to the possibility that NO production might be required for sporulation in S. pombe. Taken together, these findings suggest that NO may function as a signaling molecule which can induce both transcriptional and physiological changes in the fission yeast. Hence, these data also imply that S. pombe can be used as a model system for investigating the mechanisms underlying NO-related complex signaling pathways.","doi":"10.1007/s00709-009-0074-3","authors":"Kig C, Temizkan G","authors_abbrev":"Kig C et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-10-02","publication_year":"2009","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18601187","title":"Selective separation of microorganisms by lectins: yeast and concanavalin A as a model system.","citation":"Biotechnol Bioeng 1992 Oct 05;40(7):835-43","abstract":"Specific aggregation and separation of microorganisms was investigated using yeasts and concanavalin A as a model system. Cells of Saccharomyces cerevisiae were specifically aggregated and so separated from those of Schizosaccharomyces pombe. Optimum aggregation with over 99% of cells aggregated was achieved by adjustment to pH value and applied agitation. Dimeric lectin structure caused a far higher degree of aggregation than did tetrameric. Degree of aggregation was also strongly influenced by the ratio of lectin/cell concentrations, optimum aggregation occurring in the middle range of ratios. A high ratio of lectin to cells inhibited aggregation, occupation of most of the available receptors preventing intercellular bonding by divalent lectins. Detachment and reuse of concanavalin A was demonstrated using switching from moderate to low pH value. Potential uses for species-specific-separation of microorganisms are discussed.","authors":"Stratford M, Bond CJ","authors_abbrev":"Stratford M et al.","pubmed_publication_date":"05 Oct 1992","pubmed_entrez_date":"1992-10-05","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39156640","title":"Fission yeast Bgs1 glucan synthase participates in the control of growth polarity and membrane traffic.","citation":"iScience 2024 Aug 16;27(8):110477","abstract":"Rod-shaped fission yeast grows through cell wall expansion at poles and septum, synthesized by essential glucan synthases. Bgs1 synthesizes the linear β(1,3)glucan of primary septum at cytokinesis. Linear β(1,3)glucan is also present in the wall poles, suggesting additional Bgs1 roles in growth polarity. Our study reveals an essential collaboration between Bgs1 and Tea1-Tea4, but not other polarity factors, in controlling growth polarity. Simultaneous absence of Bgs1 function and Tea1-Tea4 causes complete loss of growth polarity, spread of other glucan synthases, and spherical cell formation, indicating this defect is specifically due to linear β(1,3)glucan absence. Furthermore, linear β(1,3)glucan absence induces actin patches delocalization and sterols spread, which are ultimately responsible for the growth polarity loss without Tea1-Tea4. This suggests strong similarities in Bgs1 functions controlling actin structures during cytokinesis and polarized growth. Collectively, our findings unveil that cell wall β(1,3)glucan regulates polarized growth, like the equivalent extracellular matrix in neuronal cells.","doi":"10.1016/j.isci.2024.110477","authors":"Ramos M, Martín-García R, Curto MÁ, Gómez-Delgado L, Moreno MB, Sato M, Portales E, Osumi M, Rincón SA, Pérez P, Ribas JC, Cortés JCG","authors_abbrev":"Ramos M et al.","pubmed_publication_date":"16 Aug 2024","pubmed_entrez_date":"2024-08-19","publication_year":"2024","canto_session_key":"dc8ce5293f6f8c29","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juan Carlos García Cortés","canto_first_approved_date":"2025-03-03 12:34:11","canto_approved_date":"2025-12-29 11:52:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-02-28 10:58:10","canto_added_date":"2024-08-19 23:25:04","annotation_curators":[{"name":"Juan Carlos García Cortés","community_curator":true,"annotation_count":4,"orcid":"0000-0002-2395-6668","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":51,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.02c","SPCC1840.02c","SPBC1706.01","SPBC19G7.05c","SPAC2F7.03c","SPBC32H8.12c","SPAC110.03","SPAC688.11","SPCC1223.06","SPBC1604.20c","SPCC1281.01","SPAC4F10.15c","SPAC19G12.10c","SPAC18G6.15"],"gene_count":14,"ltp_gene_count":10,"approved_date":"2025-03-03"},{"uniquename":"EMBL:AU013013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3011744","title":"Metabolism of the phospholipid precursor inositol and its relationship to growth and viability in the natural auxotroph Schizosaccharomyces pombe.","citation":"J Bacteriol 1986 Jun;166(3):779-86","abstract":"Phospholipid metabolism in the fission yeast Schizosaccharomyces pombe was examined. Three enzymes of phospholipid biosynthesis, cytidine diphosphate diacylglycerol synthase (CDP-DG), phosphatidylinositol (PI) synthase, and phosphatidylserine (PS) synthase, were characterized in extracts of S. pombe cells. Contrary to an earlier report, we were able to demonstrate that CDP-DG served as a precursor for PI and PS biosynthesis in S. pombe. S. pombe is naturally auxotrophic for the phospholipid precursor inositol. We found that S. pombe was much more resistant to loss of viability during inositol starvation than artificially generated inositol auxotrophs of Saccharomyces cerevisiae. The phospholipid composition of S. pombe cells grown in inositol-rich medium (50 microM) was similar to that of S. cerevisiae cells grown under similar conditions. However, growth of S. pombe at low inositol concentrations (below 30 microM) affected the ratio of the anionic phospholipids PI and PS, while the relative proportions of other glycerophospholipids remained unchanged. During inositol starvation, the rate of PI synthesis decreased rapidly, and there was a concomitant increase in the rate of PS synthesis. Phosphatidic acid and CDP-DG, which are precursors to these phospholipids, also increased when PI synthesis was blocked by lack of exogenous inositol. The major product of turnover of inositol-containing phospholipids in S. pombe was found to be free inositol, which accumulated in the medium and could be reused by the cell.","authors":"Fernandez S, Homann MJ, Henry SA, Carman GM","authors_abbrev":"Fernandez S et al.","pubmed_publication_date":"Jun 1986","pubmed_entrez_date":"1986-06-01","publication_year":"1986","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC26H8.11c","SPAC6G10.03c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:30718387","title":"Dynamics of DNA replication in a eukaryotic cell.","citation":"Proc Natl Acad Sci U S A 2019 Mar 12;116(11):4973-4982","abstract":"Each genomic locus in a eukaryotic cell has a distinct average time of replication during S phase that depends on the spatial and temporal pattern of replication initiation events. Replication timing can affect genomic integrity because late replication is associated with an increased mutation rate. For most eukaryotes, the features of the genome that specify the location and timing of initiation events are unknown. To investigate these features for the fission yeast,  Schizosaccharomyces pombe , we developed an integrative model to analyze large single-molecule and global genomic datasets. The model provides an accurate description of the complex dynamics of  S. pombe  DNA replication at high resolution. We present evidence that there are many more potential initiation sites in the  S. pombe  genome than previously identified and that the distribution of these sites is primarily determined by two factors: the sequence preferences of the origin recognition complex (ORC), and the interference of transcription with the assembly or stability of prereplication complexes (pre-RCs). We suggest that in addition to directly interfering with initiation, transcription has driven the evolution of the binding properties of ORC in  S. pombe  and other eukaryotic species to target pre-RC assembly to regions of the genome that are less likely to be transcribed.","doi":"10.1073/pnas.1818680116","authors":"Kelly T, Callegari AJ","authors_abbrev":"Kelly T et al.","pubmed_publication_date":"12 Mar 2019","pubmed_entrez_date":"2019-02-06","publication_year":"2019","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2019-02-07 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31282894","title":"Examination of Mitotic and Meiotic Fission Yeast Nuclear Dynamics by Fluorescence Live-cell Microscopy.","citation":"J Vis Exp 2019 Jun 24;(148)","abstract":"Live-cell imaging is a microscopy technique used to examine cell and protein dynamics in living cells. This imaging method is not toxic, generally does not interfere with cell physiology, and requires minimal experimental handling. The low levels of technical interference enable researchers to study cells across multiple cycles of mitosis and to observe meiosis from beginning to end. Using fluorescent tags such as Green Fluorescent Protein (GFP) and Red Fluorescent Protein (RFP), researchers can analyze different factors whose functions are important for processes like transcription, DNA replication, cohesion, and segregation. Coupled with data analysis using Fiji (a free, optimized ImageJ version), live-cell imaging offers various ways of assessing protein movement, localization, stability, and timing, as well as nuclear dynamics and chromosome segregation. However, as is the case with other microscopy methods, live-cell imaging is limited by the intrinsic properties of light, which put a limit to the resolution power at high magnifications, and is also sensitive to photobleaching or phototoxicity at high wavelength frequencies. However, with some care, investigators can bypass these physical limitations by carefully choosing the right conditions, strains, and fluorescent markers to allow for the appropriate visualization of mitotic and meiotic events.","doi":"10.3791/59822","authors":"Escorcia W, Shen KF, Yuan JP, Forsburg SL","authors_abbrev":"Escorcia W et al.","pubmed_publication_date":"24 Jun 2019","pubmed_entrez_date":"2019-07-09","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-07-11 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35293864","title":"Microtubule rescue at midzone edges promotes overlap stability and prevents spindle collapse during anaphase B.","citation":"Elife 2022 Mar 16;11","abstract":"During anaphase B, molecular motors slide interpolar microtubules to elongate the mitotic spindle, contributing to the separation of chromosomes. However, sliding of antiparallel microtubules reduces their overlap, which may lead to spindle breakage, unless microtubules grow to compensate sliding. How sliding and growth are coordinated is still poorly understood. In this study, we have used the fission yeast  S. pombe  to measure microtubule dynamics during anaphase B. We report that the coordination of microtubule growth and sliding relies on promoting rescues at the midzone edges. This makes microtubules stable from pole to midzone, while their distal parts including the plus ends alternate between assembly and disassembly. Consequently, the midzone keeps a constant length throughout anaphase, enabling sustained sliding without the need for a precise regulation of microtubule growth speed. Additionally, we found that in  S. pombe , which undergoes closed mitosis, microtubule growth speed decreases when the nuclear membrane wraps around the spindle midzone.","doi":"10.7554/eLife.72630","authors":"Lera-Ramirez M, Nédélec FJ, Tran PT","authors_abbrev":"Lera-Ramirez M et al.","pubmed_publication_date":"16 Mar 2022","pubmed_entrez_date":"2022-03-16","publication_year":"2022","canto_session_key":"baddf4c6b54fd68c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-05-17 12:20:59","canto_approved_date":"2022-05-17 12:24:32","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-04-14 10:12:50","canto_added_date":"2022-03-18 01:15:04","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPAC3G9.12","SPCC320.13c","SPBC2F12.13","SPAC18G6.15","SPBC15D4.01c","SPBC1685.15c","SPAC23C4.05c","SPBC3B8.10c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2022-05-17"},{"uniquename":"PMID:24741789","title":"Rad51 overexpression and resistance to genotoxic agents. A study in the fission yeast Schizosaccharomyces pombe.","citation":"Rev Med Chir Soc Med Nat Iasi 2014;118(1):133-40","abstract":"Many cancer cell lines have been found to overexpress the recombinase Rad51. The overexpression is associated with increased invasive potential and resistance to DNA-damaging therapeutic agents. This has been attributed to an increased capacity of cells overexpressing Rad51 to repair DNA lesions or to a genetic stabilization of the genome.\nAs the explanations are somewhat controversial, we attempted to reproduce overexpression in the unicellular eukaryote Schizosaccharomyces pombe to have a simpler tool to study the problem of Rad51 overexpression and its induced resistance to DNA-damaging agents.\nWe used the nmt1 promoter inserted upstream of rad51 gene to induce its overexpression and studied the phenotype of the transformed strain, especially its sensitivity to camptothecin and hydroxyurea.\nWe found that overexpression induced sensitivity to the two drugs even when it was associated with the deletion of a recombination mediator rad22/rad52 gene. However, when overexpression was associated with the deletion of the helicase-encoding fbh1 gene, the sensitivity to camptothecin was diminished.","authors":"Stanescu RS, Bordeianu G, Stoica B, Ungureanu D, Rusu M, Petrescu-Danila E","authors_abbrev":"Stanescu RS et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-04-19","publication_year":"2014","canto_session_key":"4886b6d59cafa045","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-30 15:25:19","canto_approved_date":"2022-05-11 17:05:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-30 15:25:13","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPBC336.01","SPAC644.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-10-30"},{"uniquename":"PMID:18556189","title":"Cloning and overexpression of a maltase gene from Schizosaccharomyces pombe in Escherichia coli and characterization of the recombinant maltase.","citation":"Mycol Res 2008 Aug;112(Pt 8):983-9","abstract":"The Schizosaccharomyces pombe maltase structural gene (SPMAL1(+)) was amplified from genomic DNA of S. pombe by PCR. An open reading frame of 1740bp, encoding a putative 579 amino-acid protein with a calculated molecular mass of 67.7kDa was characterized in the genomic DNA insert of plasmid pQE30. The specific maltase activity in the induced transformants was 21 times higher than that in wild-type. However, the estimated molecular mass of the purified recombinant maltase was 44.3kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The optimal temperature and pH of the purified recombinant maltase were 40 degrees C and 6, respectively. The recombinant maltase was weakly activated by Mg(2+), Ca(2+), Na(+), and Ba(2+), but was strongly inhibited by Hg(2+), Ag(+) and Cu(2+), EDTA, and PMSF. The purified maltase could actively hydrolyse rho-nitrophenyl glucoside (PNPG), maltose, dextrin, and soluble starch. The results demonstrate that maltase from S. pombe was different from that from other yeasts, and might be usefully exploited in the future by the biotechnology industry or lead to the development of new molecular genetic tools.","doi":"10.1016/j.mycres.2008.01.024","authors":"Chi Z, Ni X, Yao S","authors_abbrev":"Chi Z et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-06-17","publication_year":"2008","canto_session_key":"a87bcb91d6476796","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-11-26 11:47:40","canto_approved_date":"2024-06-13 19:26:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-26 11:44:15","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1683.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-11-26"},{"uniquename":"PMID:9490488","title":"Mitotic arrest: Mad2 prevents sleepy from waking up the APC.","citation":"Science 1998 Feb 13;279(5353):999-1000","abstract":"","authors":"Elledge SJ","authors_abbrev":"Elledge SJ","pubmed_publication_date":"13 Feb 1998","pubmed_entrez_date":"1998-03-07","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12005197","title":"Abnormal formation of the glucan network from regenerating protoplasts in Schizosaccharomyces pombe cps8 actin point mutant.","citation":"J Electron Microsc (Tokyo) 2000;49(4):569-78","abstract":"To study the close relationship between the actin cytoskeleton and cell wall formation, the process of cell wall formation in reverting protoplasts of the fission yeast, Schizosaccharomyces pombe, cps8 actin point mutant was investigated by ultra-high-resolution low-voltage scanning electron microscopy (UHR-LVSEM) and transmission electron microscopy (TEM). The protoplast of the cps8 mutant began to form a glucan network in a unipolar manner and to secrete alpha-galactomannan. The site of cell wall formation grew in a cylindrical shape in the wild-type protoplast. The alpha-galactomannan did not fill in the intrafibrillar spaces completely, however, and the fibrils were exposed on the cell surface. UHR-LVSEM images indicated that the glucan fibrils were thin and rope-shaped, forming a looser network than the wild-type. TEM images indicated the finest fibrils were approximately 1.5 nm in diameter, the same diameter as the wild-type. These results suggest that the cps8 mutant was insufficient in developing cross-linkage with the glucan fibrils up to the wide ribbon shape as found in the wild-type [Osumi M et al. (1989) J. Electron Microsc. 38: 457-468; Osumi M (1998) Micron 29: 207-233]. These findings appear to indicate that the actin cytoskeleton controls formation of the glucan network and secretion of beta-1,6-glucan, and confirm the close relationship of the actin cytoskeleton and glucan formation.","authors":"Konomi M, Ishiguro J, Osumi M","authors_abbrev":"Konomi M et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2002-05-15","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25768528","title":"Aggregation-fragmentation model of robust concentration gradient formation.","citation":"Phys Rev E Stat Nonlin Soft Matter Phys 2015 Feb;91(2):022704","abstract":"Concentration gradients of signaling molecules are essential for patterning during development and they have been observed in both unicellular and multicellular systems. In subcellular systems, clustering of the signaling molecule has been observed. We develop a theoretical model of cluster-mediated concentration gradient formation based on the Becker-Döring equations of aggregation-fragmentation processes. We show that such a mechanism produces robust concentration gradients on realistic time and spatial scales so long as the process of clustering does not significantly stabilize the signaling molecule. Finally, we demonstrate that such a model is applicable to the pom1p subcellular gradient in fission yeast.","authors":"Saunders TE","authors_abbrev":"Saunders TE","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2015-03-14","publication_year":"2015","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2015-03-16 01:15:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008148","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:151099","title":"Solubilization by lysolecithin and purification of the plasma membrane ATPase of the yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1978 Oct 10;253(19):7026-32","abstract":"Purified plasma membranes of Schizosaccharomyces pombe were obtained by precipitation at pH 5.2 of a crude particulate fraction, followed by differential centrifugations and isopycnic centrifugation in a discontinuous sucrose gradient. The specific activity of the Mg2+-requiring plasma membrane ATPase activity (EC 3.6.1.3) was enriched from 0.3 mumol min-1 x mg-1 of protein in the homogenate to 26 in the purified membranes. The optimal conditions for solubilization of the ATPase activity by lysolecithin were found to be: 2 mg/ml of lysolecithin, a lysolecithin to protein ratio of 8 at pH 7.5, and 15 degrees C in the presence of 1 mM ATP and 1 mM ethylenediaminetetraacetic acid. A 6- to 7-fold purification of the solubilized ATPase activity was obtained by centrifugation of the lysolecithin extract in sucrose gradient. Part of the ATPase activity which was inactivated during the centrifugation in the sucrose gradient could be restored by addition of a micellar solution of 50 microgram of lysolecithin/ml during the assay. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate of the purified enzyme showed only one band of Mr = 105,000 stained with Coomassie blue. Another ATPase component of apparent molecular weight lower than 10,000 was stained by periodic Schiff reagent but not colored by Coomassie blue. The purified enzyme was 85% inhibited by 50 micrometer N,N'-dicyclohexylcarbodiimide and 94% inhibited by 53 microgram of Dio-9/ml.","authors":"Dufour JP, Goffeau A","authors_abbrev":"Dufour JP et al.","pubmed_publication_date":"10 Oct 1978","pubmed_entrez_date":"1978-10-10","publication_year":"1978","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31152193","title":"Spindle assembly without spindle pole body insertion into the nuclear envelope in fission yeast meiosis.","citation":"Chromosoma 2019 Sep;128(3):267-277","abstract":"Centrosomes represent the major microtubule organizing center (MTOC) in eukaryotic cells and are responsible for nucleation of the spindle, the vehicle of chromosome segregation. In human female meiosis, however, spindle assembly occurs in the absence of centrosomes or other MTOCs and microtubules are nucleated around chromosomes. In yeast, spindle formation in mitosis and meiosis depends on the activity of spindle pole bodies (SPBs), the functional equivalents of centrosomes; thus, SPBs and centrosomes use similar machineries to assemble spindles. Here, we develop a system to explore the molecular mechanisms supporting acentrosomal spindle formation using fission yeast meiosis as a model scenario. We achieve this situation by removing access of the SPBs to the nucleus after their duplication. Under these conditions, we observe self-assembly-based spindle formation in the nuclear environment, conferring an ability to segregate chromosomes independently of the SPBs. Our results open the possibility to utilize the experimental advantages of fission yeast for insights into the molecular basis of acentrosomal spindle formation in meiosis.","doi":"10.1007/s00412-019-00710-y","authors":"Pineda-Santaella A, Fernández-Álvarez A","authors_abbrev":"Pineda-Santaella A et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-06-02","publication_year":"2019","canto_session_key":"12aa59986caea550","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-06-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33176147","title":"DNA Binding by the Mis4 Scc2  Loader Promotes Topological DNA Entrapment by the Cohesin Ring.","citation":"Cell Rep 2020 Nov 10;33(6):108357","abstract":"Cohesin, a critical mediator of genome organization including sister chromatid cohesion, is a ring-shaped multi-subunit ATPase that topologically embraces DNA. Its loading and function on chromosomes require the Scc2-Scc4 loader. Using biochemical reconstitution, we show here that the ability of the loader to bind DNA plays a critical role in promoting cohesin loading. Two distinct sites within the Mis4 Scc2  subunit are found to cooperatively bind DNA. Mis4 Scc2  initially forms a tertiary complex with cohesin on DNA and promotes subsequent topological DNA entrapment by cohesin through its DNA binding activity, a process that requires an additional DNA binding surface provided by Psm3 Smc3 , the ATPase domain of cohesin. Furthermore, we show that mutations in the two DNA binding sites of Mis4 impair the chromosomal loading of cohesin. These observations demonstrate the physiological importance of DNA binding by the loader and provide mechanistic insights into the process of topological cohesin loading.","doi":"10.1016/j.celrep.2020.108357","authors":"Kurokawa Y, Murayama Y","authors_abbrev":"Kurokawa Y et al.","pubmed_publication_date":"10 Nov 2020","pubmed_entrez_date":"2020-11-11","publication_year":"2020","canto_session_key":"84f0f5ee8d42bdac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-10 13:34:48","canto_approved_date":"2024-04-03 15:31:53","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-12-03 17:52:38","canto_added_date":"2020-11-13 01:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAC10F6.09c","SPAC1687.18c","SPAC31A2.05c","SPBC29A10.04","SPAC17H9.20"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2020-12-10"},{"uniquename":"PMID:26910977","title":"[Comparing Cell Toxicity of Schizosaccharomyces pombe Exposure to Airborne PM2.5 from Beijing and Inert Particle SiO2].","citation":"Huan Jing Ke Xue 2015 Nov;36(11):3943-51","abstract":"To figure out the main factor of PM2.5 toxicity to cell, this study compared the cell toxicity of Schizosaccharomyces pombe (S. pombe), a model organism, exposed to inert ultrafine SiO2 particles, a model particle, and airborne PM2.5 collected from campus of Peking University Beijing China. Using ultraviolet spectrophotometry to measure cell proliferation ratio, and environmental scanning microscope to observe the particle adhesion on the cell surface, and detecting cellular ROS generation with DHE fluorescent dye chromogenic method, and using single cell gel electrophoresis to test cell DNA damage, the experiment results indicated that the ultrafine SiO2 particles (< 60 nm) could inhibit the cell proliferation of S. pombe, mainly through adsorbing onto the cell surface to change the permeability of the cell wall; but it could not induce cells to generate ROS to cause the oxidative damage. PM2.5, the average particle size of which was larger than that of SiO2 particles, could cause oxidative damages to cells mainly by inducing cells to generate ROS, and damage DNA simultaneously. It might illustrate that there was no direct relationship between the toxicity of PM2.5 and its physical properties such as the particle size.","authors":"Liu MJ, Huang Y, Wen H, Qiu GY","authors_abbrev":"Liu MJ et al.","pubmed_publication_date":"Nov 2015","pubmed_entrez_date":"2016-02-26","publication_year":"2015","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2016-02-28 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24095277","title":"Argonaute and Triman generate dicer-independent priRNAs and mature siRNAs to initiate heterochromatin formation.","citation":"Mol Cell 2013 Oct 24;52(2):173-83","abstract":"RNAi is a conserved mechanism in which small RNAs induce silencing of complementary targets. We have previously identified priRNAs, a class of Dicer-independent small RNAs in fission yeast. The mechanism by which Dicer-independent small RNAs are generated is not well understood in any species. Here we reconstitute the final steps of priRNA and siRNA biogenesis in vitro. We identify the 3'-5' exonuclease Triman and demonstrate that Argonaute, loaded with longer RNA precursors, recruits Triman to generate mature priRNAs and siRNAs. We show that priRNA and siRNA trimming is required for de novo assembly of heterochromatin at centromeric repeats and the mat locus and for maintenance of heterochromatin at developmental genes. Furthermore, in rrp6Δ cells RNAi targets diverse genes in a Triman-dependent way, indicating that the exosome protects the genome from spurious RNAi. Our results suggest that Argonaute association with RNA degradation products generates priRNAs and triggers RNAi in a process of transcriptome surveillance.","doi":"10.1016/j.molcel.2013.08.046","authors":"Marasovic M, Zocco M, Halic M","authors_abbrev":"Marasovic M et al.","pubmed_publication_date":"24 Oct 2013","pubmed_entrez_date":"2013-10-08","publication_year":"2013","canto_session_key":"bdc3c1cc3b2e49bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-25 20:07:08","canto_approved_date":"2025-11-12 11:13:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-16 14:02:55","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.11","SPCC188.13c","SPAC8C9.04","SPBC23G7.06c","SPBC29A10.09c","SPAC1F3.01","SPCC18.06c","SPBC428.08c","SPBC216.02","SPAC13G7.07","SPBC83.03c","SPBPB10D8.04c","SPAC18G6.02c","SPBC32H8.11","SPBC23G7.12c","SPAC140.03"],"gene_count":16,"ltp_gene_count":10,"approved_date":"2017-09-25"},{"uniquename":"PMID:1479919","title":"Manipulation of large minichromosomes in Schizosaccharomyces pombe with liposome-enhanced transformation.","citation":"Methods Enzymol 1992;216:614-31","abstract":"","authors":"Allshire RC","authors_abbrev":"Allshire RC","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11920679","title":"DNA mismatch repair and mutation avoidance pathways.","citation":"J Cell Physiol 2002 Apr;191(1):28-41","abstract":"Unpaired and mispaired bases in DNA can arise by replication errors, spontaneous or induced base modifications, and during recombination. The major pathway for correction of mismatches arising during replication is the MutHLS pathway of Escherichia coli and related pathways in other organisms. MutS initiates repair by binding to the mismatch, and activates together with MutL the MutH endonuclease, which incises at hemimethylated dam sites and thereby mediates strand discrimination. Multiple MutS and MutL homologues exist in eukaryotes, which play different roles in the mismatch repair (MMR) pathway or in recombination. No MutH homologues have been identified in eukaryotes, suggesting that strand discrimination is different to E. coli. Repair can be initiated by the heterodimers MSH2-MSH6 (MutSalpha) and MSH2-MSH3 (MutSbeta). Interestingly, MSH3 (and thus MutSbeta) is missing in some genomes, as for example in Drosophila, or is present as in Schizosaccharomyces pombe but appears to play no role in MMR. MLH1-PMS1 (MutLalpha) is the major MutL homologous heterodimer. Again some, but not all, eukaryotes have additional MutL homologues, which all form a heterodimer with MLH1 and which play a minor role in MMR. Additional factors with a possible function in eukaryotic MMR are PCNA, EXO1, and the DNA polymerases delta and epsilon. MMR-independent pathways or factors that can process some types of mismatches in DNA are nucleotide-excision repair (NER), some base excision repair (BER) glycosylases, and the flap endonuclease FEN-1. A pathway has been identified in Saccharomyces cerevisiae and human that corrects loops with about 16 to several hundreds of unpaired nucleotides. Such large loops cannot be processed by MMR.","authors":"Marti TM, Kunz C, Fleck O","authors_abbrev":"Marti TM et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-03-29","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20061379","title":"Hydrogen peroxide-sensitive cysteines in the Sty1 MAPK regulate the transcriptional response to oxidative stress.","citation":"J Biol Chem 2010 Mar 05;285(10):7505-16","abstract":"MAPK are activated by and orchestrate responses to multiple, diverse stimuli. Although these responses involve the increased phosphorylation of substrate effector proteins, e.g. transcription factors, the mechanisms by which responses are tailored to particular stimuli are unclear. In the fission yeast Schizosaccharomyces pombe, the Sty1 MAPK is crucial for changes in gene expression that allow adaptation to many forms of environmental stress. Here, we have identified two cysteine residues in Sty1, Cys-153 and Cys-158, that are important for hydrogen peroxide-induced gene expression and oxidative stress resistance but not for other functions of Sty1. Many Sty1-dependent changes in gene expression are mediated by the Atf1 transcription factor. In response to stress, Sty1 increases Atf1 levels by (i) promoting increases in atf1 mRNA and by (ii) directly phosphorylating and stabilizing Atf1 protein. Although dispensable for phosphorylation and stabilization of Atf1 protein, we find that both Cys-153 and Cys-158 are required for increases in atf1 mRNA levels and Atf1-dependent gene expression in response to hydrogen peroxide but not osmotic stress. Indeed, our data indicate that oxidation of Sty1, by formation of a disulfide bond between Cys-153 and Cys-158, is important for maintaining atf1 mRNA stability at high concentrations of hydrogen peroxide. Together, these data reveal that redox regulation of cysteine thiols in Sty1 is involved in a stress-specific mechanism regulating transcriptional responses to oxidative stress. Intriguingly, the conservation of these cysteine residues in other MAPK raises the possibility that similar mechanisms may ensure appropriate responses to hydrogen peroxide in other eukaryotes.","doi":"10.1074/jbc.M109.040840","authors":"Day AM, Veal EA","authors_abbrev":"Day AM et al.","pubmed_publication_date":"05 Mar 2010","pubmed_entrez_date":"2010-01-12","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC29B5.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:10397757","title":"Isolated mammalian and Schizosaccharomyces pombe ran-binding domains rescue S. pombe sbp1 (RanBP1) genomic mutants.","citation":"Mol Biol Cell 1999 Jul;10(7):2175-90","abstract":"Mammalian Ran-binding protein-1 (RanBP1) and its fission yeast homologue, sbp1p, are cytosolic proteins that interact with the GTP-charged form of Ran GTPase through a conserved Ran-binding domain (RBD). In vitro, this interaction can accelerate the Ran GTPase-activating protein-mediated hydrolysis of GTP on Ran and the turnover of nuclear import and export complexes. To analyze RanBP1 function in vivo, we expressed exogenous RanBP1, sbp1p, and the RBD of each in mammalian cells, in wild-type fission yeast, and in yeast whose endogenous sbp1 gene was disrupted. Mammalian cells and wild-type yeast expressing moderate levels of each protein were viable and displayed normal nuclear protein import. sbp1(-) yeast were inviable but could be rescued by all four exogenous proteins. Two RBDs of the mammalian nucleoporin RanBP2 also rescued sbp1(-) yeast. In mammalian cells, wild-type yeast, and rescued mutant yeast, exogenous full-length RanBP1 and sbp1p localized predominantly to the cytosol, whereas exogenous RBDs localized predominantly to the cell nucleus. These results suggest that only the RBD of sbp1p is required for its function in fission yeast, and that this function may not require confinement of the RBD to the cytosol. The results also indicate that the polar amino-terminal portion of sbp1p mediates cytosolic localization of the protein in both yeast and mammalian cells.","authors":"Novoa I, Rush MG, D'Eustachio P","authors_abbrev":"Novoa I et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-09","publication_year":"1999","canto_session_key":"65859fd450d0beb4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-10-21 14:59:55","canto_approved_date":"2022-02-24 11:16:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-20 15:42:37","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1773.07c","SPAC1687.11"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-10-21"},{"uniquename":"PMID:3546317","title":"Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.","citation":"J Biol Chem 1987 Mar 15;262(8):3754-61","abstract":"A three-dimensional model of yeast alcohol dehydrogenase, based on the homologous horse liver enzyme, was used to compare the substrate binding pockets of the three isozymes (I, II, and III) from Saccharomyces cerevisiae and the enzyme from Schizosaccharomyces pombe. Isozyme I and the S. pombe enzyme have methionine at position 294 (numbered as in the liver enzyme, corresponding to 270 in yeast), whereas isozymes II and III have leucine. Otherwise the active sites of the S. cerevisiae enzymes are the same. All four wild-type enzymes were produced from the cloned genes. In addition, oligonucleotide-directed mutagenesis was used to change Met-294 in alcohol dehydrogenase I to leucine. The mechanisms for all five enzymes were predominantly ordered with ethanol (but partially random with butanol) at pH 7.3 and 30 degrees C. The wild-type alcohol dehydrogenases and the leucine mutant had similar kinetic constants, except that isozyme II had 10-20-fold smaller Michaelis and inhibition constants for ethanol. Thus, residue 294 is not responsible for this difference. Apparently, substitutions outside of the substrate binding pocket indirectly affect the interactions of the alcohol dehydrogenases with ethanol. Nevertheless, the substitution of methionine with leucine in the substrate binding site of alcohol dehydrogenase I produced a 7-10-fold increase in reactivity (V/Km) with butanol, pentanol, and hexanol. The higher activity is due to tighter binding of the longer chain alcohols and to more rapid hydrogen transfer.","authors":"Ganzhorn AJ, Green DW, Hershey AD, Gould RM, Plapp BV","authors_abbrev":"Ganzhorn AJ et al.","pubmed_publication_date":"15 Mar 1987","pubmed_entrez_date":"1987-03-15","publication_year":"1987","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC13B11.01"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:18783176","title":"Respiratory oscillations in yeasts.","citation":"Adv Exp Med Biol 2008;641:118-40","abstract":"Respiratory oscillations in yeasts have been studied in three time domains with periods of (a) about a minute, (b) about 40 min, and (c) about a day. Reactive responses (damped oscillations), rhythms and temperature-compensated clocks have been described for (b) and (c), but a timekeeping clock has not yet been shown for (a). Synchronous populations reveal the time-structure that can only otherwise be studied in single organisms; this is because time-averaging through an asynchronous population conceals its fine structure. Early studies with synchronous cultures made by size selection methods indicated ultradian-clock driven oscillations in respiration, pools of adenylates, total protein, RNA synthesis and many enzyme activities (tau = 40 min in Schizosaccharomyces pombe, 30 min in Candida utilis), and more recently in self-synchronised continuous cultures of Saccharomyces cerevisiae (tau = 48 min). Most detailed understanding comes from the latter system, where continuous, noninvasive real-time monitoring (of 02 uptake, CO2 production, and NAD(P)H redox state) is combined with frequent discrete time samples (for other redox components, including H2S, GSH and cytochromes, metabolites, and mRNA levels). A redox switch lies at the heart of this ultradian clock and a plethora of outputs is optimized to a time-base that is genetically-determined and differs in different organisms. It is suggested that the entire temporal landscape of all eukaryotic organisms and the cells of higher plants and animals is constructed on this basis. A time frame for the coordination and coherence of all intracellular processes and the construction and assembly of cellular structures is provided by the ultradian clock The circadian clock matches these functions to the daily cycle of the external environment.","authors":"Lloyd D","authors_abbrev":"Lloyd D","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-09-12","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3892482","title":"Evaluation of heterologous ARS activity in S. cerevisiae using cloned DNA from S. pombe.","citation":"Nucleic Acids Res 1985 May 24;13(10):3711-22","abstract":"Cloned segments of Schizosaccharomyces pombe genomic DNA were screened for ARS activity in the native host, S. pombe, using high frequency transformation, phenotypic instability and extrachromosomal maintenance of unrearranged plasmid sequences as criteria for ARS function. This analysis revealed 12 ARS elements in a total of 230 kb of chromosomal DNA, indicating an average frequency of one ARS every 19 kb of genomic DNA. We then used these clones to assess the reliability of the S. cerevisiae assay for detecting ARS elements in heterologous DNA. The results show that not only does the S. cerevisiae assay fail to detect a large proportion of true ARS elements but it also wrongly identifies a significant proportion of clones which did not display ARS activity in the native host. We would therefore recommend restraint when extrapolating from observed ARS function of heterologous DNA in S. cerevisiae to a presumed analogous role in the original host.","authors":"Maundrell K, Wright AP, Piper M, Shall S","authors_abbrev":"Maundrell K et al.","pubmed_publication_date":"24 May 1985","pubmed_entrez_date":"1985-05-24","publication_year":"1985","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31399036","title":"Quantitative principles of cis-translational control by general mRNA sequence features in eukaryotes.","citation":"Genome Biol 2019 Aug 09;20(1):162","abstract":"General translational cis-elements are present in the mRNAs of all genes and affect the recruitment, assembly, and progress of preinitiation complexes and the ribosome under many physiological states. These elements include mRNA folding, upstream open reading frames, specific nucleotides flanking the initiating AUG codon, protein coding sequence length, and codon usage. The quantitative contributions of these sequence features and how and why they coordinate to control translation rates are not well understood.\nHere, we show that these sequence features specify 42-81% of the variance in translation rates in Saccharomyces cerevisiae, Schizosaccharomyces pombe, Arabidopsis thaliana, Mus musculus, and Homo sapiens. We establish that control by RNA secondary structure is chiefly mediated by highly folded 25-60 nucleotide segments within mRNA 5' regions, that changes in tri-nucleotide frequencies between highly and poorly translated 5' regions are correlated between all species, and that control by distinct biochemical processes is extensively correlated as is regulation by a single process acting in different parts of the same mRNA.\nOur work shows that general features control a much larger fraction of the variance in translation rates than previously realized. We provide a more detailed and accurate understanding of the aspects of RNA structure that directs translation in diverse eukaryotes. In addition, we note that the strongly correlated regulation between and within cis-control features will cause more even densities of translational complexes along each mRNA and therefore more efficient use of the translation machinery by the cell.","doi":"10.1186/s13059-019-1761-9","authors":"Li JJ, Chew GL, Biggin MD","authors_abbrev":"Li JJ et al.","pubmed_publication_date":"09 Aug 2019","pubmed_entrez_date":"2019-08-11","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-08-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27274088","title":"Proximity-dependent biotin labelling in yeast using the engineered ascorbate peroxidase APEX2.","citation":"Biochem J 2016 Aug 15;473(16):2463-9","abstract":"The engineered ascorbate peroxidase (APEX2) has been effectively employed in mammalian cells to identify protein-protein interactions. APEX2 fused to a protein of interest covalently tags nearby proteins with biotin-phenol (BP) when H2O2 is added to the cell culture medium. Subsequent affinity purification of biotinylated proteins allows for identification by MS. BP labelling occurs in 1 min, providing temporal control of labelling. The APEX2 tool enables proteomic mapping of subcellular compartments as well as identification of dynamic protein complexes, and has emerged as a new methodology for proteomic analysis. Despite these advantages, a related APEX2 approach has not been developed for yeast. Here we report methods to enable APEX2-mediated biotin labelling in yeast. Our work demonstrated that high osmolarity and disruption of cell wall integrity permits live-cell biotin labelling in Schizosaccharomyces pombe and Saccharomyces cerevisiae respectively. Under these conditions, APEX2 permitted targeted and proximity-dependent labelling of proteins. The methods described herein set the stage for large-scale proteomic studies in yeast. With modifications, the method is also expected to be effective in other organisms with cell walls, such as bacteria and plants.","doi":"10.1042/BCJ20160106","authors":"Hwang J, Espenshade PJ","authors_abbrev":"Hwang J et al.","pubmed_publication_date":"15 Aug 2016","pubmed_entrez_date":"2016-06-09","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-06-10 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC285.11","SPAC1565.08"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:3071741","title":"Isolation and characterization of Schizosaccharomyces pombe mutants phenotypically similar to ras1-.","citation":"Mol Gen Genet 1988 Dec;215(1):26-31","abstract":"We isolated mutants of Schizosaccharomyces pombe which have deformed cell morphology, are deficient in conjugation and poor in sporulation. This phenotype is characteristic of the ras1 defective mutant previously identified. Tests of the mutants for allelism using cell fusion showed that they define five complementation groups, one of which is ras1 itself. The others are named ral1 through ral4 (ras like). Mutants in ral3 or ral4 conjugate at a very low frequency, while the others apparently do not conjugate at all. Plasmid clones complementing ral1, ral2 or ral3, which apparently carry the respective gene, were isolated from S. pombe genomic libraries. Multiple copies of either the ral2 or the ral3 gene could partially restore mating ability in ral1- strains. Multiple copies of the ras1 gene could partially restore mating ability in ral1- and ral2- strains. These results suggest that the ral1, ral2 and ras1 genes may function in a common pathway in that order. The ral3 gene may influence this pathway. Analysis of these gene products will aid identification of factors which interact with Ras proteins.","authors":"Fukui Y, Yamamoto M","authors_abbrev":"Fukui Y et al.","pubmed_publication_date":"Dec 1988","pubmed_entrez_date":"1988-12-01","publication_year":"1988","canto_session_key":"423a987e520829e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-03-04 16:09:01","canto_approved_date":"2021-10-15 12:26:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-26 13:26:47","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22H10.07","SPAC17H9.09c","SPBC21.05c","SPAC16E8.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2013-03-04"},{"uniquename":"PMID:25410910","title":"Casein kinase 2 inhibits HomolD-directed transcription by Rrn7 in Schizosaccharomyces pombe.","citation":"FEBS J 2015 Feb;282(3):491-503","abstract":"In Schizosaccharomyces pombe, ribosomal protein gene (RPG) promoters contain a TATA analogue element called the HomolD box. The HomolD-binding protein Rrn7 forms a complex with the RNA polymerase II machinery. Despite the importance of ribosome biogenesis to cell survival, the mechanisms involved in the regulation of transcription of eukaryotic RPGs are unknown. In this study, we identified Rrn7 as a new substrate of the pleiotropic casein kinase 2 (CK2), which is a regulator of basal transcription. Recombinant Rrn7 from S. pombe, which is often used as a model organism for studying eukaryotic transcription, interacted with CK2 in vitro and in vivo. Furthermore, CK2-mediated phosphorylation of Rrn7 inhibited its HomolD-directed transcriptional activity and ability to bind to an oligonucleotide containing a HomolD box in vitro. Mutation of Rrn7 at Thr67 abolished these effects, indicating that this residue is a critical CK2 phosphorylation site. Finally, Rrn7 interacted with the regulatory subunit of CK2 in vivo, inhibition of CK2 in vivo potentiated ribosomal protein gene transcription, and chromatin immunoprecipitation analyses identified that the catalytic subunit of CK2 was associated with the rpk5 gene promoter in S. pombe. Taken together, these data suggest that CK2 inhibits ribosomal protein gene transcription in S. pombe via phosphorylation of Rrn7 at Thr67.","doi":"10.1111/febs.13157","authors":"Moreira-Ramos S, Rojas DA, Montes M, Urbina F, Miralles VJ, Maldonado E","authors_abbrev":"Moreira-Ramos S et al.","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2014-11-21","publication_year":"2015","canto_session_key":"af81fc769ebaf5b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-12 16:09:45","canto_approved_date":"2020-02-28 17:55:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-15 10:11:30","canto_added_date":"2014-11-22 01:16:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.09c","SPAC1851.03","SPAC23C11.11"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-10-12"},{"uniquename":"PMID:28108582","title":"Identification of a novel protein kinase that affects the chronological lifespan in fission yeast.","citation":"FEMS Microbiol Lett 2017 Jan;364(2)","abstract":"Chronological lifespan is defined by how long a cell can survive in a non-dividing state. In yeast, it is measured by viability after entry into the stationary phase. To understand the regulatory mechanisms of chronological lifespan in Schizosaccharomyces pombe, it is necessary to identify and characterize novel factors involved in the regulation of chronological lifespan. To this end, we have screened for a long-lived mutant and identified that novel gene nnk1 +  that encodes an essential protein kinase is the determinant of chronological lifespan. We showed that the expression of major glucose transporter gene, ght5 + , is decreased in the isolated nnk1-35 mutant, suggesting that Nnk1 protein is involved in the regulation of ght5 +  The consumption of glucose in the growth medium after saturated growth was lower in the nnk1-35 mutant than that in wild-type cell. The isolated ght5 deletion mutant showed long-lived phenotype. Based on these results, we propose that Nnk1 regulates chronological lifespan through the regulation of ght5 +  Nnk1 might coordinate glucose availability and lifespan in fission yeast.","doi":"10.1093/femsle/fnw257","authors":"Kurauchi T, Hashizume A, Imai Y, Hayashi K, Tsubouchi S, Ihara K, Ohtsuka H, Aiba H","authors_abbrev":"Kurauchi T et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2017-01-22","publication_year":"2017","canto_session_key":"e4f5c700a6334e7e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_first_approved_date":"2019-11-23 15:13:51","canto_approved_date":"2020-03-15 15:12:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-22 03:38:36","canto_added_date":"2017-01-23 01:15:11","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":1,"orcid":"0000-0002-7775-0446","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC70.05c","SPCC1235.14"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-11-23"},{"uniquename":"PMID:15116432","title":"Identification of genes encoding putative nucleoporins and transport factors in the fission yeast Schizosaccharomyces pombe: a deletion analysis.","citation":"Yeast 2004 Apr 30;21(6):495-509","abstract":"In a systematic approach to study genes that are related to nucleocytoplasmic trafficking in the fission yeast Schizosaccharomyces pombe, the open reading frames (ORFs) of 26 putative nucleoporins and transport factors were deleted. Here we report the initial characterization of these deletion mutants. Of the 26 putative genes deleted, 14 were found to be essential for viability. Null mutations of essential genes resulted in failure to either complete one round or to sustain cell division. Four of the 14 essential genes, SPBC582.11c, SPBC17G9.04c, SPBC3B9.16c and SPCC162.08c, encode putative nucleoporins and a myosin-like protein with homologues NUP84, NUP85, NUP120 and MLP1, respectively, that are not required for viability in Saccharomyces cerevisiae, suggesting that their gene products perform critical functions in Sz. pombe. On the basis of combined drug sensitivity assays and genetic analysis we have identified five non-essential null mutants that were hypersensitive to the microtubule depolymerizing drug thiabendazole (TBZ) and exhibited a cut phenotype upon TBZ treatment, suggesting possible involvement in microtubule function. Three of the corresponding ORFs, SPCC18B5.07c, nup40 and SPAC1805.04, encode putative nucleoporins with low similarity to the S. cerevisiae nucleoporins NUP2p, NUP53p and NUP133p, respectively. Further genetic analysis revealed that one of the nucleoporin genes, nup40, and another gene, SPCC1322.06, encoding a putative importin-beta/Cse1p superfamily protein may have a spindle checkpoint function.","authors":"Chen XQ, Du X, Liu J, Balasubramanian MK, Balasundaram D","authors_abbrev":"Chen XQ et al.","pubmed_publication_date":"30 Apr 2004","pubmed_entrez_date":"2004-04-30","publication_year":"2004","canto_session_key":"d2b55761573bd2da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-03-24 11:11:28","canto_approved_date":"2022-02-07 17:07:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-19 13:54:55","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":115,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2C4.11c","SPAC15F9.02","SPBC19G7.15","SPBC428.01c","SPAC22G7.02","SPAC22H10.03c","SPBC14F5.03c","SPCC4B3.07","SPBC30B4.05","SPCC1840.03","SPAC26A3.15c","SPAC1805.04","SPBC1604.08c","SPAC2F3.06c","SPBC28F2.02","SPAC23D3.06c","SPAC19E9.01c","SPBC3B9.16c","SPAC1B1.03c","SPCC1322.06","SPCC18B5.07c","SPBC17G9.04c","SPAC22G7.09c","SPCC162.08c","SPCC290.03c","SPAC1486.05"],"gene_count":26,"ltp_gene_count":26,"approved_date":"2015-03-24"},{"uniquename":"EMBL:BI542460","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11698194","title":"The role of the yeast spindle pole body and the mammalian centrosome in regulating late mitotic events.","citation":"Curr Opin Cell Biol 2001 Dec;13(6):762-9","abstract":"Centrosomes of vertebrate cells and spindle pole bodies (SPBs) of fungi were first recognized through their ability to organize microtubules. Recent studies suggest that centrosomes and SPBs also have a function in the regulation of cell cycle progression, in particular in controlling late mitotic events. Regulators of mitotic exit and cytokinesis are associated with the SPB of budding and fission yeast. Elucidation of the molecular roles played by these regulators is helping to clarify the function of the SPB in controlling progression though mitosis.","authors":"Pereira G, Schiebel E","authors_abbrev":"Pereira G et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-11-08","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21755449","title":"Synchronization of yeast.","citation":"Methods Mol Biol 2011;761:173-200","abstract":"The budding yeast Saccharomyces cerevisiae and fission yeast Schizosaccharomyces pombe are amongst the simplest and most powerful model systems for studying the genetics of cell cycle control. Because yeast grows very rapidly in simple and economical media, large numbers of cells can easily be obtained for genetic, molecular, and biochemical studies of the cell cycle. The use of synchronized cultures greatly aids in the ease and interpretation of cell cycle studies. In principle, there are two general methods for obtaining synchronized yeast populations. Block and release methods can be used to induce cell cycle synchrony. Alternatively, centrifugal elutriation can be used to select synchronous populations. Because each method has innate advantages and disadvantages, the use of multiple approaches helps in generalizing results. An overview of the most commonly used methods to generate synchronized yeast cultures is presented along with working Notes, a section that includes practical comments, experimental considerations and observations, and hints regarding the pros and cons innate to each approach.","doi":"10.1007/978-1-61779-182-6_12","authors":"Manukyan A, Abraham L, Dungrawala H, Schneider BL","authors_abbrev":"Manukyan A et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-07-15","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14731390","title":"Indecent exposure: when telomeres become uncapped.","citation":"Mol Cell 2004 Jan 16;13(1):7-18","abstract":"The protective \"cap\" that assembles at chromosome ends recruits and controls an intricate network of biochemical activities, each one critical for telomere structure and the maintenance of genomic stability. Recent studies have uncovered the components of telomere caps and have started to define the pathways that lead from telomere dysfunction to chromosomal catastrophe.","authors":"Ferreira MG, Miller KM, Cooper JP","authors_abbrev":"Ferreira MG et al.","pubmed_publication_date":"16 Jan 2004","pubmed_entrez_date":"2004-01-21","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14654686","title":"Functional significance of intermediate cleavages in the 3'ETS of the pre-rRNA from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2003 Dec 15;31(24):7110-6","abstract":"Pathways for the maturation of ribosomal RNAs are complex with numerous intermediate cleavage sites that are not always conserved closely in the course of evolution. Both in eukaryotes and bacteria genetic analyses and in vitro studies have strongly implicated RNase III-like enzymes in the processing of rRNA precursors. In Schizosacharomyces pombe, for example, the RNase III-like Pac1 nuclease has been shown to cleave the free 3'ETS at two known intermediate sites but, in the presence of RAC protein, the same RNA also is cleaved at the 3'-end of the 25 S rRNA sequence. In this study normal and mutant 3'ETS sequences were digested with the Pac1 enzyme to further evaluate its role in rRNA processing. Accurate cleavage at the known intermediate processing sites was dependent on the integrity of the helical structure at these sites as well as a more distal upper stem region in the conserved extended hairpin structure of the 3'ETS. The cleavage of mutant 3'ETS sequences also generally correlated with the known effects of these mutations on rRNA production, in vivo. One mutant, however, was efficiently processed in vivo but was not a substrate for the Pac1 nuclease, in vitro. In contrast, in the presence of RAC protein, the same RNA remained susceptible to Pac1 nuclease cleavage at the 3'-end of the 25 rRNA sequence, indicating that the removal of the 3'ETS does not require cleavage at the intermediate sites. These results suggest that basic maturation pathways may be less complex than previously reported raising similar questions about other intermediate processing sites, which have been identified by analyses of termini, and/or processing, in vitro.","authors":"Ivakine E, Spasov K, Frendewey D, Nazar RN","authors_abbrev":"Ivakine E et al.","pubmed_publication_date":"15 Dec 2003","pubmed_entrez_date":"2003-12-05","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22647846","title":"A dominant role for meiosis-specific 3' RNA processing in controlling expression of a fission yeast cyclin gene.","citation":"RNA 2012 Jul;18(7):1408-20","abstract":"Meiotic gene regulation provides a rich source of insight into mechanisms of temporal control during development. We previously reported that accumulation of many meiotic mRNAs in fission yeast is governed by changes in 3' RNA processing and elucidated the molecular basis of this regulatory mechanism for an early meiotic gene. Here, we report that cleavage/polyadenylation is also the nexus of negative control for middle meiotic genes. Parallel profiles of splicing and polyadenylation are observed over a meiotic time course for both rem1 and spo4 but not for a constitutive control gene. Nevertheless, polyadenylation of rem1 transcripts is restricted to meiosis by a splicing-independent mechanism. Through systematic sequence substitutions, we identified a negative control region (NCR) located upstream of the rem1 transcription start site and found that it is required to block 3' RNA processing in proliferating cells. Ablation of the NCR relieves inhibition regardless of whether the intron is present, absent, or carries splice site mutations. Consistent with the previous report of a polypeptide encoded by the first exon of rem1, we discovered a second 3' processing site just downstream from the 5' splice site. Polyadenylation within the intron is activated concurrent with the downstream site during meiosis, is controlled by the NCR, and is enhanced when splicing is blocked via 5' junction or branch point mutations. Taken together, these data suggest a novel regulatory mechanism in which a 5' element modulates the dynamic interplay between splicing and polyadenylation.","doi":"10.1261/rna.033423.112","authors":"Potter K, Cremona N, Sunder S, Wise JA","authors_abbrev":"Potter K et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-06-01","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30503780","title":"The Inner Nuclear Membrane Protein Bqt4 in Fission Yeast Contains a DNA-Binding Domain Essential for Telomere Association with the Nuclear Envelope.","citation":"Structure 2019 Feb 05;27(2):335-343.e3","abstract":"Telomeres, the protective caps at the end of the chromosomes, are often associated with the nuclear envelope (NE). Telomere positioning to the NE is dynamically regulated during mitosis and meiosis. One inner nuclear membrane protein, Bqt4, in Schizosaccharomyces pombe plays essential roles in connecting telomeres to the NE. However, the structural basis of Bqt4 in mediating telomere-NE association is not clear. Here, we report the crystal structure of the N-terminal domain of Bqt4. The N-terminal domain of Bqt4 structurally resembles the APSES-family DNA-binding domain and has a moderate double-stranded DNA-binding activity. Disruption of Bqt4-DNA interaction results in telomere detachment from the NE. These data suggest that the DNA-binding activity of Bqt4 may function to prime the chromosome onto the NE and promote telomere-NE association.","doi":"10.1016/j.str.2018.10.010","authors":"Hu C, Inoue H, Sun W, Takeshita Y, Huang Y, Xu Y, Kanoh J, Chen Y","authors_abbrev":"Hu C et al.","pubmed_publication_date":"05 Feb 2019","pubmed_entrez_date":"2018-12-04","publication_year":"2019","canto_session_key":"5ec20d07d1c694d3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yong Chen","canto_first_approved_date":"2019-01-02 17:24:23","canto_approved_date":"2023-05-15 12:45:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-20 05:18:52","canto_added_date":"2018-12-08 01:15:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yong Chen","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.10","SPBC19C7.10","SPBC1778.02","SPBC12D12.01"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2019-01-02","pdb_entries":[{"pdb_id":"5ybx","gene_chains":[{"gene_uniquename":"SPBC19C7.10","chain":"A","position":"2-140"}],"title":"Crystal structure of the N-terminal domain of Bqt4 in S.pombe","entry_authors":"Hu C,Chen Y","entry_authors_abbrev":"Hu C et al.","reference_uniquename":"PMID:30503780","experimental_method":"X-ray","resolution":"2.501"}]},{"uniquename":"PMID:9372936","title":"Npp106p, a Schizosaccharomyces pombe nucleoporin similar to Saccharomyces cerevisiae Nic96p, functionally interacts with Rae1p in mRNA export.","citation":"Mol Cell Biol 1997 Dec;17(12):7047-60","abstract":"To identify components of the mRNA export machinery in Schizosaccharomyces pombe, a screen was developed to identify mutations that were synthetically lethal with the conditional mRNA export allele rae1-167. Mutations defining three complementation groups were isolated, and here we report the characterization of npp106 (for nuclear pore protein of 106 kDa). This gene encodes a predicted protein that has significant similarity to the Nic96p nucleoporin of Saccharomyces cerevisiae. Consistent with Npp106p being a nucleoporin, a functional green fluorescent protein (GFP)-tagged Npp106p localized to the nuclear periphery. In contrast to NIC96, the npp106 gene is not essential. Moreover, a delta npp106 mutant did not show cytoplasmic mislocalization of a simian virus 40 nuclear localization signal-GFP-LacZ reporter protein, and a fraction of cells had accumulation of poly(A)+ RNA in the nucleus. A consequence of the synthetic lethality between rae1-167 and npp106-1 was the accumulation of poly(A)+ RNA in the nucleus when cells were grown under synthetic lethal conditions. In addition to npp106-1, which is a nonsense mutation that truncates the protein at amino acid 292, the delta npp106 mutation was synthetically lethal with rae1-167, suggesting that the synthetic lethality is a consequence of the loss of a function of npp106. We further demonstrate that a region between amino acids 74 and 348 of Npp106p is required for complementation of the synthetic lethality. These results uncover a potential direct or indirect involvement of Npp106p in mRNA export.","authors":"Yoon JH, Whalen WA, Bharathi A, Shen R, Dhar R","authors_abbrev":"Yoon JH et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1997-12-31","publication_year":"1997","canto_session_key":"3aad414b8b97983b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-12-21 15:59:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-04 16:33:06","canto_added_date":"2012-02-24 05:53:34","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.05c","SPCC1739.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-09-04"},{"uniquename":"Pfam:PF11326","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC227.17c","HGNC:27012"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11119724","title":"Regulation of Wee1 kinase in response to protein synthesis inhibition.","citation":"FEBS Lett 2000 Dec 15;486(3):305-9","abstract":"To investigate the mechanism coupling growth (protein synthesis) with cell division, we examined the relationship between the tyrosine kinase Wee1 that inhibits Cdc2-Cdc13 mitosis-inducing kinase by phosphorylating it, and protein synthesis inhibition in fission yeast. The wee1-50 mutant showed supersensitivity to protein synthesis inhibitor, cycloheximide. Wee1 was essential for the G(2) delay upon a partial inhibition of protein synthesis. Indeed, the protein synthesis inhibition caused an increase in the Wee1 protein by the Sty1/Spc1 MAPK-dependent transcriptional and the Sty1/Spc1 MAPK-independent post-transcriptional regulations. Further, the results indicated that the post-transcriptional regulation is important for the G(2) delay.","authors":"Suda M, Yamada S, Toda T, Miyakawa T, Hirata D","authors_abbrev":"Suda M et al.","pubmed_publication_date":"15 Dec 2000","pubmed_entrez_date":"2000-12-20","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9312055","title":"Fission yeast Cut2 required for anaphase has two destruction boxes.","citation":"EMBO J 1997 Oct 01;16(19):5977-87","abstract":"The fission yeast Schizosaccharomyces pombe cut2(+) gene is essential for sister chromatid separation. Cut2 protein, which locates in the interphase nucleus and along the metaphase spindle, disappears in anaphase with the same timing as mitotic cyclin destruction. This proteolysis depends on the APC (Anaphase-Promoting Complex)-cyclosome which contains ubiquitin ligase activity. The N-terminus of Cut2 contains two stretches similar to the mitotic cyclin destruction box. We show that both sequences (33RAPLGSTKQ and 52RTVLGGKST) serve as destruction boxes and are required for in vitro polyubiquitination and proteolysis. Cut2 with doubly mutated destruction boxes inhibits anaphase, whereas Cut2 with singly mutated boxes can suppress cut2 mutations. Strong expression of the N-terminal 73 residues containing the destruction boxes leads to the accumulation of endogenous cyclin and Cut2, and arrests cells in metaphase, whereas the same fragment with the mutated boxes does not. Cut2 proteolysis occurs in vitro using Xenopus mitotic extracts in the presence of functional destruction boxes. Furthermore, Cut2 is polyubiquitinated in an in vitro system using HeLa extracts, and this polyubiquitination requires the destruction boxes.","authors":"Funabiki H, Yamano H, Nagao K, Tanaka H, Yasuda H, Hunt T, Yanagida M","authors_abbrev":"Funabiki H et al.","pubmed_publication_date":"01 Oct 1997","pubmed_entrez_date":"1997-10-06","publication_year":"1997","canto_session_key":"e01b2f3ba979a8d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-02-19 07:18:52","canto_approved_date":"2023-02-03 15:40:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-02 16:29:55","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.01c","SPBC11B10.09","SPBC582.03","SPBC336.12c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2017-02-19"},{"uniquename":"PMID:34849813","title":"Defining the consequences of endogenous genetic variation within a novel family of Schizosaccharomyces pombe heterochromatin nucleating sequences.","citation":"G3 (Bethesda) 2021 Aug 07;11(8)","abstract":"Centromeres are essential for genetic inheritance-they prevent aneuploidy by providing a physical link between DNA and chromosome segregation machinery. In many organisms, centromeres form at sites of repetitive DNAs that help establish the chromatin architecture required for centromere function. These repeats are often rapidly evolving and subject to homogenization, which causes the expansion of novel repeats and sequence turnover. Thus, centromere sequence varies between individuals and across species. This variation can affect centromere function. We utilized Schizosaccharomyces pombe to assess the relationship between centromere sequence and chromatin structure and determine how sensitive this relationship is to genetic variation. In S. pombe, nucleating sequences within centromere repeats recruit heterochromatin via multiple mechanisms, which include RNA-interference (RNAi) . Heterochromatin, in turn, contributes to centromere function through its participation in three essential processes; establishment of a kinetochore, cohesion of sister chromatids, and suppression of recombination. Here, we show that a centromere element containing RevCen, a target of the RNAi pathway, establishes heterochromatin and gene silencing when relocated to a chromosome arm. Within this RevCen-containing element (RCE), a highly conserved domain is necessary for full heterochromatin nucleation but cannot establish heterochromatin independently. We characterize the 10 unique RCEs in the S. pombe centromere assembly, which range from 60% to 99.6% identical, and show that all are sufficient to establish heterochromatin. These data affirm the importance of centromere repeats in establishing heterochromatin and suggest there is flexibility within the sequences that mediate this process. Such flexibility may preserve centromere function despite the rapid evolution of centromere repeats.","doi":"10.1093/g3journal/jkab185","authors":"Joshi A, Musicante MJ, Wheeler BS","authors_abbrev":"Joshi A et al.","pubmed_publication_date":"07 Aug 2021","pubmed_entrez_date":"2021-12-01","publication_year":"2021","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2021-12-03 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10882124","title":"Meiotic DNA breaks associated with recombination in S. pombe.","citation":"Mol Cell 2000 May;5(5):883-8","abstract":"In the fission yeast Schizosaccharomyces pombe, we have detected prominent DNA breaks that appeared shortly after premeiotic DNA replication. These breaks, like meiotic recombination, required the products of the six rec genes tested. Prominent breaks were detected at widely separated sites, about 100-300 kb apart, equivalent to about 50-150 sites per genome or approximately the number of meiotic recombination events. Certain features of these breaks are similar to those in the distantly related yeast Saccharomyces cerevisiae, the only other organism in which meiotic DNA breaks have been reported. Other features, however, appear to be different. These results suggest that, although DNA breaks may be a general feature of meiotic recombination, the breaks in S. pombe may play a role different from those in S. cerevisiae.","authors":"Cervantes MD, Farah JA, Smith GR","authors_abbrev":"Cervantes MD et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-07-06","publication_year":"2000","canto_session_key":"3ddfb9b68e90878e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-09-15 14:45:08","canto_approved_date":"2020-09-15 14:45:08","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-09-15 14:45:02","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPAC25G10.04c","SPCC1753.03c","SPAC17A5.11","SPBC32F12.02","SPBC21B10.12"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2020-09-15"},{"uniquename":"PMID:9287302","title":"Isolation, expression, and regulation of the pgr1(+) gene encoding glutathione reductase absolutely required for the growth of Schizosaccharomyces pombe.","citation":"J Biol Chem 1997 Sep 12;272(37):23042-9","abstract":"The pgr1(+) gene encoding glutathione reductase (GR, EC 1.6.4.2) was isolated from Schizosaccharomyces pombe using a polymerase chain reaction fragment as a probe. The gene consists of two exons and an intron of 55 nucleotides, encoding a polypeptide of 465 amino acids (50,238 Da) with conserved residues characteristic of GR. The transcriptional start site was localized at 239 nucleotides upstream from the ATG initiation codon. The level of transcript as well as the GR enzyme activity increased more than 11-fold when the cloned pgr1(+) gene was expressed on a multicopy plasmid. This overexpression conferred on S. pombe cells more resistance against menadione, a redox cycling agent, but not against H2O2. The level of pgr1(+) transcripts increased by treatment with oxidants such as menadione, cumene hydroperoxide, and diamide. It also increased by treatment with high osmolarity, heat shock, or at the stationary growth phase. The deletion of the pap1(+) gene encoding an AP-1 homolog in S. pombe caused reduction in the pgr1(+) gene expression. Furthermore, Deltapap1 cells lost the inducibility of pgr1(+) gene expression by the above stresses, implying that Pap1 is involved in general stress-inducible gene expression. When the pgr1(+) gene was disrupted, the haploid spores were not viable. Repression of nmt1 promoter-driven pgr1(+) expression by thiamine caused cessation of growth, which was rescued by the episomal pgr1(+) gene. These results indicate that GR activity, which efficiently reduces GSSG, is essentially required for the growth of S. pombe, unlike in Saccharomyces cerevisiae or Escherichia coli.","authors":"Lee J, Dawes IW, Roe JH","authors_abbrev":"Lee J et al.","pubmed_publication_date":"12 Sep 1997","pubmed_entrez_date":"1997-09-12","publication_year":"1997","canto_session_key":"efdf248e3a0f9c6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-03-20 22:15:27","canto_approved_date":"2025-04-12 11:17:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-25 14:09:06","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPBC17A3.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-03-20"},{"uniquename":"PMID:22833559","title":"Regulation of SREBP during hypoxia requires Ofd1-mediated control of both DNA binding and degradation.","citation":"Mol Biol Cell 2012 Sep;23(18):3764-74","abstract":"Cells adapt to changes in ambient oxygen by changing their gene expression patterns. In fission yeast, the sterol regulatory element-binding protein Sre1 is proteolytically cleaved under low oxygen, and its N-terminal segment (Sre1N) serves as a hypoxic transcription factor. When oxygen is present, the prolyl hydroxylase Ofd1 down-regulates Sre1N activity in two ways: first, by inhibiting its binding to DNA, and second, by accelerating its degradation. Here we use a mathematical model to assess what each of these two regulatory functions contributes to the hypoxic response of the cell. By disabling individual regulatory functions in the model, which would be difficult in vivo, we found that the Ofd1 function of inhibiting Sre1N binding to DNA is essential for oxygen-dependent Sre1N regulation. The other Ofd1 function of accelerating Sre1N degradation is necessary for the yeast to quickly turn off its hypoxic response when oxygen is restored. In addition, the model predicts that increased Ofd1 production at low oxygen plays an important role in the hypoxic response, and the model indicates that the Ofd1 binding partner Nro1 tunes the response to oxygen. This model quantifies our understanding of a novel oxygen-sensing mechanism that is widely conserved.","doi":"10.1091/mbc.E12-06-0451","authors":"Porter JR, Lee CY, Espenshade PJ, Iglesias PA","authors_abbrev":"Porter JR et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-07-27","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18157149","title":"Identification and characterization of the Schizosaccharomyces pombe TER1 telomerase RNA.","citation":"Nat Struct Mol Biol 2008 Jan;15(1):34-42","abstract":"Although the catalytic subunit of the Schizosaccharomyces pombe telomerase holoenzyme was identified over ten years ago, the unusual heterogeneity of its telomeric DNA made it difficult to identify its RNA component. We used a new two-step immunoprecipitation and reverse transcription-PCR technique to identify the S. pombe telomerase RNA, which we call TER1. TER1 RNA was 1,213 nucleotides long, similar in size to the Saccharomyces cerevisiae telomerase RNA, TLC1. TER1 RNA associated in vivo with the two known subunits of the S. pombe telomerase holoenzyme, Est1p and Trt1p, and neither association was dependent on the other holoenzyme component. We present a model to explain how telomerase introduces heterogeneity into S. pombe telomeres. The technique used here to identify TER1 should be generally applicable to other model organisms.","authors":"Webb CJ, Zakian VA","authors_abbrev":"Webb CJ et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-12-25","publication_year":"2008","canto_session_key":"0205e2ea9f154b73","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-08 16:02:13","canto_approved_date":"2024-04-03 12:35:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-08 16:01:54","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.13","SPNCRNA.214","SPBC29A3.14c","SPBC543.03c","SPCC126.02c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2015-10-08"},{"uniquename":"PMID:6700607","title":"The effect of spermine on spontaneous and UV-induced mutations in Schizosaccharomyces pombe.","citation":"Mutat Res 1984 Feb;125(2):205-11","abstract":"The effect of different concentrations of spermine on spontaneous and UV-induced mutation in the adenine forward mutation system of Schizosaccharomyces pombe was investigated. The effect of spermine on spontaneous mutation was studied in 5 mutator strains (mut 1-4, mut 1-23, mut 2-9, mut 2-20 and mut 3-21) and on UV-induced mutation in a pigmented adenine-requiring strain and its radiation-sensitive derivative (rad 13). The effect of spermine exposure on mutation induction before and after UV irradiation was also investigated. Spermine increased spontaneous forward mutation in the mut 1-4 strain by 47%, and enhanced UV-induced forward mutation 2-fold in the rad 13 and normal pigmented strains. No antimutagenic effect of spermine was seen in any of the strains tested. This is in marked contrast to the antimutagenic effect of spermine observed with bacteria.","authors":"Prendergast JA, Kamra OP, Nasim A","authors_abbrev":"Prendergast JA et al.","pubmed_publication_date":"Feb 1984","pubmed_entrez_date":"1984-02-01","publication_year":"1984","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23117617","title":"Chromosomally-retained RNA mediates homologous pairing.","citation":"Nucleus 2012;3(6):516-9","abstract":"Pairing and recombination of homologous chromosomes are essential for ensuring correct segregation of chromosomes in meiosis. In S. pombe, chromosomes are first bundled at the telomeres (forming a telomere bouquet) and then aligned by oscillatory movement of the elongated \"horsetail\" nucleus. Telomere clustering and subsequent chromosome alignment promote pairing of homologous chromosomes. However, this telomere-bundled alignment of chromosomes cannot be responsible for the specificity of chromosome pairing. Thus, there must be some mechanism to facilitate recognition of homologous partners after telomere clustering. Recent studies in S. pombe have shown that RNA transcripts retained on the chromosome, or RNA bodies, may play a role in recognition of homologous chromosomes for pairing. Acting as fiducial markers of homologous loci they would abrogate the need for direct DNA sequence homology searching.","doi":"10.4161/nucl.22732","authors":"Ding DQ, Haraguchi T, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-11-03","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22965128","title":"The THO complex cooperates with the nuclear RNA surveillance machinery to control small nucleolar RNA expression.","citation":"Nucleic Acids Res 2012 Nov 01;40(20):10240-53","abstract":"THO is a multi-protein complex that promotes coupling between transcription and mRNA processing. In contrast to its role in mRNA biogenesis, we show here that the fission yeast THO complex negatively controls the expression of non-coding small nucleolar (sno) RNAs. Accordingly, the deletion of genes encoding subunits of the evolutionarily conserved THO complex results in increased levels of mature snoRNAs. We also show physical and functional connections between THO and components of the TRAMP polyadenylation complex, whose loss of function also results in snoRNA accumulation. Consistent with a role in snoRNA expression, we demonstrate that THO and TRAMP complexes are recruited to snoRNA genes, and that a functional THO complex is required to maintain TRAMP occupancy at sites of snoRNA transcription. Our findings suggest that THO promotes exosome-mediated degradation of snoRNA precursors by ensuring the presence of the TRAMP complex at snoRNA genes. This study unveils an unexpected role for THO in the control of snoRNA expression and provides a new link between transcription and nuclear RNA decay.","doi":"10.1093/nar/gks838","authors":"Larochelle M, Lemay JF, Bachand F","authors_abbrev":"Larochelle M et al.","pubmed_publication_date":"01 Nov 2012","pubmed_entrez_date":"2012-09-12","publication_year":"2012","canto_session_key":"ef68152fe75e2835","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC577.04","SPAC6F12.16c","SPAC12G12.13c","SPCC24B10.11c","SPBC16E9.12c","SPAC1D4.14","SPBP35G2.08c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:8579247","title":"Three-dimensional structure of tubular networks, presumably Golgi in nature, in various yeast strains: a comparative study.","citation":"Anat Rec 1995 Nov;243(3):283-93","abstract":"In the yeast Saccharomyces cerevisiae, the Golgi apparatus consists of discrete units distributed throughout the cytoplasm. When such units are examined in three dimensions, in relatively thick sections prepared for the electron microscope, they usually appear as small tubular networks with a stained material accumulating in dilations located at the junctions of membranous tubules. To see whether such tubular networks are observed in other yeast species, the three-dimensional structure of organelles in eight additional yeast strains, endowed with diverse biological properties, are examined.\nYeast strains were grown at 24 degrees C in YPD medium (2% Bactopeptone, 1% Bactoyeast extract, and 2% glucose). Cells that were examined by electron microscopy came from exponentially growing cultures grown in a shaking water bath and maintained at a OD 600 (optical density at 600 nm) of 0.5. Cells were fixed in a fixative containing 2% glutaraldehyde in 0.1 M cacodylate buffer pH 7.4 and 0.8 M sorbitol. They were then treated for 15 min in 1% sodium metaperiodate and postfixed for 1 hr in potassium ferrocyanide-osmic acid. They were preembedded in agarose prior to dehydration and finally embedded in Epon. In these conditions, the preservation of cell organelles was improved and the cytoplasmic retraction from the cell wall was minimized. Photographs of sections tilted at +/- 15 degrees from the 0 degrees position of the goniometric stage were used to prepare stereopairs from which the three-dimensional configuration of the organelles was visualized.\nIn all yeast strains, tubular networks appeared as separate elements or units disperse throughout the cytoplasm. Each unit consisted of anastomosed membranous tubules. In some strains such as Saccharomyces cerevisiae, Zygosaccharomyces rouxii, or Saccharomyces pombe, such units appeared mainly as polygonal networks of intensely stained membranous tubules. Along these networks, distensions filled with stained material were similar in size to nearby secretory granules, suggesting that the latter formed by fragmentation of the tubular networks. In Hansenula polymorpha, Pichia pastoris, and Debaryomyces hansenii, networks of anastomosed tubules were closely superposed to each other and formed parallel arrays reminiscent of the stacks of Golgi saccules seen in mammalian cells. However, in contrast to what is usually found in the latter, the layers making up the parallel arrays in yeasts, were clearly continuous to each other. In other strains, i.e., Kluyveromyces lactis, Candida albicans, and Candida parapsilosis, the situation was intermediate and their cytoplasm contained only arrays of small size with two or at most three superposed layers of membranous tubules. Small vesicles in the 30-50 nm range were rarely encountered in most yeast strains.\nIt is therefore concluded that tubular networks, presumably Golgi in nature, are present in all yeasts examined so far. Yet, in some strains, these tubular networks may be arranged in parallel arrays or stacks.","authors":"Rambourg A, Clermont Y, Ovtracht L, Képès F","authors_abbrev":"Rambourg A et al.","pubmed_publication_date":"Nov 1995","pubmed_entrez_date":"1995-11-01","publication_year":"1995","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7764687","title":"High-level expression of human lipocortin I in the fission yeast Schizosaccharomyces pombe using a novel expression vector.","citation":"Biotechnology (N Y) 1994 Apr;12(4):400-4","abstract":"We have developed a novel expression system that allows the fission yeast, Schizosaccharomyces pombe, to be used for the efficient overproduction of heterologous proteins. As an example of the utility of this system, human lipocortin I was expressed to 50 percent of soluble protein, and 150 mg of highly purified material was obtained from 10 grams of wet cell paste. Expression of lipocortin I was driven by the human cytomegalovirus (hCMV) promoter in a vector that also contains a neomycin resistance gene (neo) under the control of the SV40 early promoter, permitting selection for increasing copy-number with increasing concentrations of the antibiotic G418. The purified protein was equivalent to its native counterpart with respect to antigenicity and biochemical properties such as phospholipase A2 inhibition, actin binding and N-terminal acetylation. We have also used this system to produce comparable amounts of other proteins including rat arginase, rat NDP-kinase and human interleukin-6.","authors":"Giga-Hama Y, Tohda H, Okada H, Owada MK, Okayama H, Kumagai H","authors_abbrev":"Giga-Hama Y et al.","pubmed_publication_date":"Apr 1994","pubmed_entrez_date":"1994-04-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40562936","title":"Spatiotemporal orchestration of mitosis by cyclin-dependent kinase.","citation":"Nature 2025 Jun 25;","abstract":"Mitotic onset is a critical transition for eukaryotic cell proliferation. The commonly held view of mitotic control is that the master regulator, cyclin-dependent kinase (CDK), is first activated in the cytoplasm, at the centrosome, initiating mitosis 1-3 . Bistability in CDK activation ensures that the transition is irreversible, but how this unfolds in a spatially compartmentalized cell is unknown 4-8 . Here, using fission yeast, we show that CDK is first activated in the nucleus, and that the bistable responses differ markedly between the nucleus and the cytoplasm, with a stronger response in the nucleus driving mitotic signal propagation from there to the cytoplasm. Abolishing cyclin-CDK localization to the centrosome led to activation occurring only in the nucleus, spatially uncoupling the nucleus and cytoplasm mitotically, suggesting that centrosomal cyclin-CDK acts as a 'signal relayer'. We propose that the key mitotic regulatory system operates in the nucleus in proximity to DNA, which enables incomplete DNA replication and DNA damage to be effectively monitored to preserve genome integrity and to integrate ploidy within the CDK control network. This spatiotemporal regulatory framework establishes core principles for control of the onset of mitosis and highlights that the CDK control system operates within distinct regulatory domains in the nucleus and cytoplasm.","doi":"10.1038/s41586-025-09172-y","authors":"Kapadia N, Nurse P","authors_abbrev":"Kapadia N et al.","pubmed_publication_date":"25 Jun 2025","pubmed_entrez_date":"2025-06-25","publication_year":"2025","canto_session_key":"6690219b542677d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-06-26 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22426535","title":"The DNA helicase Pfh1 promotes fork merging at replication termination sites to ensure genome stability.","citation":"Genes Dev 2012 Mar 15;26(6):594-602","abstract":"Bidirectionally moving DNA replication forks merge at termination sites composed of accidental or programmed DNA-protein barriers. If merging fails, then regions of unreplicated DNA can result in the breakage of DNA during mitosis, which in turn can give rise to genome instability. Despite its importance, little is known about the mechanisms that promote the final stages of fork merging in eukaryotes. Here we show that the Pif1 family DNA helicase Pfh1 plays a dual role in promoting replication fork termination. First, it facilitates replication past DNA-protein barriers, and second, it promotes the merging of replication forks. A failure of these processes in Pfh1-deficient cells results in aberrant chromosome segregation and heightened genome instability.","doi":"10.1101/gad.184663.111","authors":"Steinacher R, Osman F, Dalgaard JZ, Lorenz A, Whitby MC","authors_abbrev":"Steinacher R et al.","pubmed_publication_date":"15 Mar 2012","pubmed_entrez_date":"2012-03-20","publication_year":"2012","canto_session_key":"8a79079584833765","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPBC887.14c","SPAC644.14c","SPCC4G3.05c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:9421507","title":"Identification and characterization of srp1, a gene of fission yeast encoding a RNA binding domain and a RS domain typical of SR splicing factors.","citation":"Nucleic Acids Res 1998 Jan 15;26(2):505-11","abstract":"The SR protein family is involved in constitutive and regulated pre-mRNA splicing and has been found to be evolutionarily conserved in metazoan organisms. In contrast, the genome of the unicellular yeast Saccharomyces cerevisiae does not contain genes encoding typical SR proteins. The mammalian SR proteins consist of one or two characteristic RNA binding domains (RBD), containing the signature sequences RDAEDA and SWQDLKD respectively, and a RS (arginine/serine-rich) domain which gave the family its name. We have now cloned from the fission yeast Schizosaccharomyces pombe the gene srp1. This gene is the first yeast gene encoding a protein with typical features of mammalian SR protein family members. The gene is not essential for growth. We show that overexpression of the RNA binding domain inhibits pre-mRNA splicing and that the highly conserved sequence RDAEDA in the RBD is involved. Overexpression of Srp1 containing mutations in the RS domain also inhibits pre-mRNA splicing activity. Furthermore, we show that overexpression of Srp1 and overexpression of the mammalian SR splicing factor ASF/SF2 suppress the pre-mRNA splicing defect of the temperature-sensitive prp4-73 allele. prp4 encodes a protein kinase involved in pre-mRNA splicing. These findings are consistent with the notion that Srp1 plays a role in the splicing process.","authors":"Gross T, Richert K, Mierke C, Lützelberger M, Käufer NF","authors_abbrev":"Gross T et al.","pubmed_publication_date":"15 Jan 1998","pubmed_entrez_date":"1998-02-28","publication_year":"1998","canto_session_key":"ed8cb0c6b8c64aff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-30 13:35:22","canto_approved_date":"2026-01-31 14:44:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-30 13:35:08","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.08","SPCC777.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-30"},{"uniquename":"PMID:15811919","title":"Transcription and RNA-processing in fission yeast mitochondria.","citation":"RNA 2005 May;11(5):785-95","abstract":"We systematically examined transcription and RNA-processing in mitochondria of the petite-negative fission yeast Schizosaccharomyces pombe. Two presumptive transcription initiation sites at opposite positions on the circular-mapping mtDNA were confirmed by in vitro capping of primary transcripts with guanylyl-transferase. The major promoter (Pma) is located adjacent to the 5'-end of the rnl gene, and a second, minor promoter (Pmi) upstream from cox3. The primary 5'-termini of the mature rnl and cox3 transcripts remain unmodified. A third predicted accessory transcription initiation site is within the group IIA1 intron of the cob gene (cobI1). The consensus promoter motif of S. pombe closely resembles the nonanucleotide promoter motifs of various yeast mtDNAs. We further characterized all mRNAs and the two ribosomal RNAs by Northern hybridization, and precisely mapped their 5'- and 3'-ends. The mRNAs have leader sequences with a length of 38 up to 220 nt and, in most instances, are created by removal of tRNAs from large precursor RNAs. Like cox2 and rnl, cox1 and cox3 are not separated by tRNA genes; instead, transcription initiation from the promoters upstream from rnl and cox3 compensates for the lack of tRNA-mediated 5'-processing. The 3'-termini of mRNAs and of SSU rRNA are processed at distinct, C-rich motifs that are located at a variable distance (1-15 nt) downstream from mRNA and SSU-rRNA coding regions. The accuracy of RNA-processing at these sites is sequence-dependent. Similar 3'-RNA-processing motifs are present in species of the genus Schizosaccharomyces, but not in budding yeasts that have functionally analogous A+T-rich dodecamer processing signals.","authors":"Schäfer B, Hansen M, Lang BF","authors_abbrev":"Schäfer B et al.","pubmed_publication_date":"May 2005","pubmed_entrez_date":"2005-04-07","publication_year":"2005","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9871115","title":"Schizosaccharomyces pombe exo1 is involved in the same mismatch repair pathway as msh2 and pms1.","citation":"Curr Genet 1998 Dec;34(5):343-50","abstract":"Besides the MutLS-like system, Schizosaccharomyces pombe has an additional pathway of mismatch repair. This minor pathway, producing short excision tracts, repairs C/C and, with lower efficiency, other mismatches also. We investigated the involvement of the exo1+, msh2+ and pms1+ genes in the two pathways. The exo1+ gene encodes a 5' to 3' exonuclease, while msh2+ and pms1+ are homologs of Escherichia coli mutS and mutL, respectively. Intragenic two-factor crosses showed that exo1+, msh2+ and pms1+ are involved in the major, but not in the C/C-correcting, pathway. Post-meiotic segregation frequencies and mitotic mutation rates in single and double mutants supported this finding. Furthermore, msh2 delta was epistatic over exo1 delta, and the ExoI enzyme is likely to be redundant with other exonucleases.","authors":"Rudolph C, Fleck O, Kohli J","authors_abbrev":"Rudolph C et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1998-12-31","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.05","SPBC19G7.01c","SPAC19G12.02c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:16111936","title":"Meiosis: organizing microtubule organizers.","citation":"Curr Biol 2005 Aug 23;15(16):R633-5","abstract":"During meiosis in fission yeast, the zygote nucleus undergoes microtubule-driven oscillatory movements that ultimately serve to promote genetic recombination. An essential component of this is a meiosis-specific consolidation of microtubule-organizing activity to the the spindle pole body, driven by the novel coiled-coil protein mcp6/hrs1p.","authors":"Sawin KE","authors_abbrev":"Sawin KE","pubmed_publication_date":"23 Aug 2005","pubmed_entrez_date":"2005-08-23","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10462482","title":"Cloning and characterization of psu1(+), a new essential fission yeast gene involved in cell wall synthesis.","citation":"Biochem Biophys Res Commun 1999 Aug 27;262(2):368-74","abstract":"We have isolated a new gene, psu1(+), from the fission yeast Schizosaccharomyces pombe. The predicted amino acid sequences shows that this protein has striking homology to the SUN family of the budding yeast, hence designated Psu1 (S. pombe homologue of the SUN family). Disruption of the psu1(+) gene revealed that it is essential for growth, and the null phenotype showed the swelling of cells followed by eventual lysis. We introduced psu1(+) gene in the disruptant strain and repressed it giving resistance to 1, 3-beta-glucanase digestion. Our results suggest that Psu1 plays an essential role in cell wall synthesis in S. pombe.","authors":"Omi K, Sonoda H, Nagata K, Sugita K","authors_abbrev":"Omi K et al.","pubmed_publication_date":"27 Aug 1999","pubmed_entrez_date":"1999-08-27","publication_year":"1999","canto_session_key":"4c41745717a03c78","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-02 08:31:32","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-02 08:31:24","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1002.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-02"},{"uniquename":"PMID:41684683","title":"The  Schizosaccharomyces pombe  Glycosyltransferase Gmh5 is a Functional Homologue of the α-1,6-Mannosyltransferase Mnn10 Crucial for N-Glycan Processing.","citation":"Food Technol Biotechnol 2026;64(1):39-52","abstract":"This study provides the first functional characterization of Gmh5p as a mannosyltransferase of the GT34 family and demonstrates its role in N-glycan biosynthesis. Our findings expand the current understanding of the diversity and specificity of glycosyltransferases in eukaryotes and highlight their importance in cell wall biology.","doi":"10.17113/ftb.64.01.26.9195","authors":"Lommel M, Hutzler F, Siukstaite L, Wild K, Grbavac A, Sinning I, Strahl S","authors_abbrev":"Lommel M et al.","pubmed_publication_date":"2026","pubmed_entrez_date":"2026-02-13","publication_year":"2026","canto_session_key":"ed2010bd25c1286c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-02-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1E7.09","SPAC32A11.03c","SPBC16C6.09","SPAC637.06","SPCC1906.01","SPAP14E8.04"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:739977","title":"Contribution of a caffeine-sensitive recombinational repair pathway to survival and mutagenesis in UV-irradiated Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1978 Nov 16;167(1):43-9","abstract":"","authors":"Gentner NE, Werner MM, Hannan MA, Nasim A","authors_abbrev":"Gentner NE et al.","pubmed_publication_date":"16 Nov 1978","pubmed_entrez_date":"1978-11-16","publication_year":"1978","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26908286","title":"Copper(I) stabilization by cysteine/tryptophan motif in the extracellular domain of Ctr4.","citation":"J Inorg Biochem 2016 Jun;159:45-9","abstract":"Copper transporter Ctr4 of fission yeast has a quasi-palindromic sequence rich in cysteine and aromatic amino acid residues, CX4YWNWYX4C (where X represents any amino acid), in the N-terminal extracellular domain. A 24-mer peptide comprising this sequence is bound to Cu(I) through the cysteine thiolate coordination. Luminescence, UV absorption and resonance Raman spectra of the Cu(I)-peptide complex show that at least one of the two tryptophan side chains is located in close proximity to the thiolate-Cu(I) center and interacts with the Cu(I) ion via π-electrons of the indole ring. Although the thiolates and Cu(I) are oxidized to disulfide and Cu(II), respectively, only very slowly in air-saturated solutions, replacements of the tryptophan residues to phenylalanine significantly accelerate the oxidation reactions. The results obtained indicate that the interaction between Cu(I) and tryptophan via π-electrons plays a significant role in protecting the thiolate-Cu(I) center against the oxidation. The cysteine- and tryptophan-rich quasi-palindromic sequence may be a metal binding motif that stabilizes Cu(I) in the oxidizing extracellular environment.","doi":"10.1016/j.jinorgbio.2016.02.004","authors":"Okada M, Miura T","authors_abbrev":"Okada M et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-02-25","publication_year":"2016","canto_session_key":"80654dbf35d8f4cd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-28 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19696784","title":"Nucleocytoplasmic transport of Alp7/TACC organizes spatiotemporal microtubule formation in fission yeast.","citation":"EMBO Rep 2009 Oct;10(10):1161-7","abstract":"Ran GTPase activates several target molecules to induce microtubule formation around the chromosomes and centrosomes. In fission yeast, in which the nuclear envelope does not break down during mitosis, Ran targets the centrosomal transforming acidic coiled-coil (TACC) protein Alp7 for spindle formation. Alp7 accumulates in the nucleus only during mitosis, although its underlying mechanism remains elusive. Here, we investigate the behaviour of Alp7 and its binding partner, Alp14/TOG, throughout the cell cycle. Interestingly, Alp7 enters the nucleus during interphase but is subsequently exported to the cytoplasm by the Exportin-dependent nuclear export machinery. The continuous nuclear export of Alp7 during interphase is essential for maintaining the array-like cytoplasmic microtubule structure. The mitosis-specific nuclear accumulation of Alp7 seems to be under the control of cyclin-dependent kinase (CDK). These results indicate that the spatiotemporal regulation of microtubule formation is established by the Alp7/TACC-Alp14/TOG complex through the coordinated interplay of Ran and CDK.","doi":"10.1038/embor.2009.158","authors":"Sato M, Okada N, Kakui Y, Yamamoto M, Yoshida M, Toda T","authors_abbrev":"Sato M et al.","pubmed_publication_date":"Oct 2009","pubmed_entrez_date":"2009-08-22","publication_year":"2009","canto_session_key":"480394fd534ef4bd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-04-23 18:08:08","canto_approved_date":"2022-02-07 14:59:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-07 17:03:34","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC895.07","SPBC11B10.09","SPAC890.02c","SPAC1805.17","SPBC582.03"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2018-04-23"},{"uniquename":"PMID:17901865","title":"Fission yeast goes synthetic.","citation":"Nat Methods 2007 Oct;4(10):777-8","abstract":"","authors":"Nielsen O","authors_abbrev":"Nielsen O","pubmed_publication_date":"Oct 2007","pubmed_entrez_date":"2007-09-29","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29290562","title":"Cell Size and Growth Rate Are Modulated by TORC2-Dependent Signals.","citation":"Curr Biol 2018 Jan 22;28(2):196-210.e4","abstract":"The size of all cells, from bacteria to vertebrates, is proportional to the growth rate set by nutrient availability, but the underlying mechanisms are unknown. Here, we show that nutrients modulate cell size and growth rate via the TORC2 signaling network in budding yeast. An important function of the TORC2 network is to modulate synthesis of ceramide lipids, which play roles in signaling. TORC2-dependent control of ceramide signaling strongly influences both cell size and growth rate. Thus, cells that cannot make ceramides fail to modulate their growth rate or size in response to changes in nutrients. PP2A associated with the Rts1 regulatory subunit (PP2A Rts1 ) is embedded in a feedback loop that controls TORC2 signaling and helps set the level of TORC2 signaling to match nutrient availability. Together, the data suggest a model in which growth rate and cell size are mechanistically linked by ceramide-dependent signals arising from the TORC2 network.","doi":"10.1016/j.cub.2017.11.069","authors":"Lucena R, Alcaide-Gavilán M, Schubert K, He M, Domnauer MG, Marquer C, Klose C, Surma MA, Kellogg DR","authors_abbrev":"Lucena R et al.","pubmed_publication_date":"22 Jan 2018","pubmed_entrez_date":"2018-01-02","publication_year":"2018","canto_session_key":"cd319883c8c39b90","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-10-24 10:59:24","canto_approved_date":"2019-10-24 10:59:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-10-09 20:24:56","canto_added_date":"2019-10-09 20:22:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-10-24"},{"uniquename":"PMID:38269097","title":"Rapamycin-sensitive mechanisms confine the growth of fission yeast below the temperatures detrimental to cell physiology.","citation":"iScience 2024 Jan 19;27(1):108777","abstract":"Cells cease to proliferate above their growth-permissible temperatures, a ubiquitous phenomenon generally attributed to heat damage to cellular macromolecules. We here report that, in the presence of rapamycin, a potent inhibitor of Target of Rapamycin Complex 1 (TORC1), the fission yeast  Schizosaccharomyces pombe  can proliferate at high temperatures that usually arrest its growth. Consistently, mutations to the TORC1 subunit RAPTOR/Mip1 and the TORC1 substrate Sck1 significantly improve cellular heat resistance, suggesting that TORC1 restricts fission yeast growth at high temperatures. Aiming for a more comprehensive understanding of the negative regulation of high-temperature growth, we conducted genome-wide screens, which identified additional factors that suppress cell proliferation at high temperatures. Among them is Mks1, which is phosphorylated in a TORC1-dependent manner, forms a complex with the 14-3-3 protein Rad24, and suppresses the high-temperature growth independently of Sck1. Our study has uncovered unexpected mechanisms of growth restraint even below the temperatures deleterious to cell physiology.","doi":"10.1016/j.isci.2023.108777","authors":"Morozumi Y, Mahayot F, Nakase Y, Soong JX, Yamawaki S, Sofyantoro F, Imabata Y, Oda AH, Tamura M, Kofuji S, Akikusa Y, Shibatani A, Ohta K, Shiozaki K","authors_abbrev":"Morozumi Y et al.","pubmed_publication_date":"19 Jan 2024","pubmed_entrez_date":"2024-01-25","publication_year":"2024","canto_session_key":"9dba3a4623d24c82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yuichi Morozumi","canto_first_approved_date":"2024-04-18 09:45:59","canto_approved_date":"2026-01-23 10:30:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-26 06:53:36","canto_added_date":"2024-01-26 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":169,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Yuichi Morozumi","community_curator":true,"annotation_count":132,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC57A7.11","SPAC1F8.07c","SPBC216.07c","SPBC839.15c","SPAC1A6.04c","SPAC144.03","SPBC17D1.05","SPBC1105.05","SPAC26F1.06","SPAC25H1.07","SPAC23A1.10","SPBC685.06","SPAC6G9.09c","SPBC17G9.05","SPBC577.02","SPBC21C3.13","SPAC821.09","SPAC3G9.03","SPAC11H11.06","SPAPB1E7.04c","SPBC1685.10","SPBC18E5.06","SPCC1840.02c","SPBC4.07c","SPCC23B6.04c","SPAPB17E12.13","SPBC32F12.11","SPCC4G3.08","SPAC3F10.04","SPCC1223.05c","SPAC1F8.03c","SPAC664.11","SPAC17H9.04c","SPAC8C9.08","SPAC17A5.03","SPCC24B10.09","SPAPB8E5.02c","SPBC1685.02c","SPAC694.05c","SPBC2F12.04","SPBC1703.13c","SPAC31G5.03","SPCC18.14c","SPAC589.06c","SPBC215.09c","SPBC17G9.10","SPAC1142.04","SPBC1539.09c","SPCC1281.01","SPBC3E7.02c","SPAC26F1.07","SPCC18.01c","SPAC22G7.06c","SPAC589.10c","SPBC365.03c","SPAC30D11.12","SPAC3H1.07","SPCC1739.13","SPBC21C3.08c","SPAC19G12.16c","SPAC24H6.04","SPBC3D6.15","SPBP4H10.13","SPCC962.04","SPAC6G9.02c","SPAC17A2.13c","SPBC16C6.09","SPAC22A12.15c","SPCC162.07","SPAPB15E9.01c","SPBC3D6.02","SPAC513.01c","SPCC1259.01c","SPAC6F6.07c","SPAC27D7.06","SPAC1B9.02c","SPBC1815.01","SPAC20G4.06c","SPAC31G5.12c","SPAC3H5.09c","SPAC664.05","SPCC1919.02","SPBC56F2.09c","SPBC1734.01c","SPAC18G6.14c","SPAC1F7.13c","SPAC19B12.03","SPAC57A7.04c","SPBC83.17","SPAP27G11.13c","SPAC23H4.09","SPCC965.04c","SPCC63.14","SPBC685.07c","SPCC794.12c","SPBC839.16","SPAC22E12.14c","SPAC17D4.04","SPBC4F6.09","SPCC622.18","SPBC776.01","SPCC663.04","SPBC23G7.15c","SPCC1281.06c","SPBC19C2.07","SPAPJ698.02c","SPAC1420.01c","SPAPB18E9.05c","SPCC576.08c","SPAC30.04c","SPBC4F6.14","SPAPB8E5.06c","SPAC1F7.08","SPAC22F8.09","SPAC8E11.02c","SPBC11C11.09c","SPACUNK4.07c","SPBC3B9.13c","SPAC19G12.10c","SPAC57A7.06","SPAC926.04c","SPCPB16A4.03c","SPCC330.14c","SPBC839.17c","SPBP23A10.08","SPAC1039.02","SPAC4F10.07c","SPBC29A3.04","SPAC323.05c","SPAC890.08","SPAPB8E5.03","SPMIT.10","SPCC417.08","SPCC1450.04","SPBC18H10.13","SPAC1071.10c","SPAC19A8.04","SPBC21H7.04","SPMIT.03","SPAPB1E7.12","SPAC3C7.11c"],"gene_count":142,"ltp_gene_count":111,"approved_date":"2024-04-18"},{"uniquename":"PMID:12742059","title":"A complete inventory of fungal kinesins in representative filamentous ascomycetes.","citation":"Fungal Genet Biol 2003 Jun;39(1):1-15","abstract":"Complete inventories of kinesins from three pathogenic filamentous ascomycetes, Botryotinia fuckeliana, Cochliobolus heterostrophus, and Gibberella moniliformis, are described. These protein sequences were compared with those of the filamentous saprophyte, Neurospora crassa and the two yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Data mining and phylogenetic analysis of the motor domain yielded a constant set of 10 kinesins in the filamentous fungal species, compared with a smaller set in S. cerevisiae and S. pombe. The filamentous fungal kinesins fell into nine subfamilies when compared with well-characterized kinesins from other eukaryotes. A few putative kinesins (one in B. fuckeliana and two in C. heterostrophus) could not be defined as functional, due to unorthodox organization and lack of experimental data. The broad representation of filamentous fungal kinesins across most of the known subfamilies and the ease of gene manipulation make fungi ideal models for functional and evolutionary investigation of these proteins.","authors":"Schoch CL, Aist JR, Yoder OC, Gillian Turgeon B","authors_abbrev":"Schoch CL et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-05-14","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010557","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36138017","title":"Ubiquitination of CLIP-170 family protein restrains polarized growth upon DNA replication stress.","citation":"Nat Commun 2022 Sep 22;13(1):5565","abstract":"Microtubules play a crucial role during the establishment and maintenance of cell polarity. In fission yeast cells, the microtubule plus-end tracking proteins (+TIPs) (including the CLIP-170 homologue Tip1) regulate microtubule dynamics and also transport polarity factors to the cell cortex. Here, we show that the E3 ubiquitin ligase Dma1 plays an unexpected role in controlling polarized growth through ubiquitinating Tip1. Dma1 colocalizes with Tip1 to cortical sites at cell ends, and is required for ubiquitination of Tip1. Although the absence of dma1 +  does not cause apparent polar growth defects in vegetatively growing cells, Dma1-mediated Tip1 ubiquitination is required to restrain polar growth upon DNA replication stress. This mechanism is distinct from the previously recognized calcineurin-dependent inhibition of polarized growth. In this work, we establish a link between Dma1-mediated Tip1 ubiquitination and DNA replication or DNA damage checkpoint-dependent inhibition of polarized growth in fission yeast.","doi":"10.1038/s41467-022-33311-y","authors":"Wang X, Zheng F, Yi YY, Wang GY, Hong LX, McCollum D, Fu C, Wang Y, Jin QW","authors_abbrev":"Wang X et al.","pubmed_publication_date":"22 Sep 2022","pubmed_entrez_date":"2022-09-22","publication_year":"2022","canto_session_key":"cd0646514a96db42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xi Wang","canto_first_approved_date":"2023-01-20 14:30:02","canto_approved_date":"2025-09-03 13:19:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-01-12 03:10:17","canto_added_date":"2022-09-25 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Xi Wang","community_curator":true,"annotation_count":14,"orcid":"0000-0003-3894-5440","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.12","SPBC1706.01","SPAC3H5.06c","SPAC17G8.10c","SPBP4H10.04"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2023-01-20"},{"uniquename":"PMID:29809148","title":"Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore.","citation":"Elife 2018 May 29;7","abstract":"Non-centrosomal microtubule organizing centers (MTOCs) are important for microtubule organization in many cell types. In fission yeast  Schizosaccharomyces pombe , the protein Mto1, together with partner protein Mto2 (Mto1/2 complex), recruits the γ-tubulin complex to multiple non-centrosomal MTOCs, including the nuclear envelope (NE). Here, we develop a comparative-interactome mass spectrometry approach to determine how Mto1 localizes to the NE. Surprisingly, we find that Mto1, a constitutively cytoplasmic protein, docks at nuclear pore complexes (NPCs), via interaction with exportin Crm1 and cytoplasmic FG-nucleoporin Nup146. Although Mto1 is not a nuclear export cargo, it binds Crm1 via a nuclear export signal-like sequence, and docking requires both Ran in the GTP-bound state and Nup146 FG repeats. In addition to determining the mechanism of MTOC formation at the NE, our results reveal a novel role for Crm1 and the nuclear export machinery in the stable docking of a cytoplasmic protein complex at NPCs.","doi":"10.7554/eLife.33465","authors":"Bao XX, Spanos C, Kojidani T, Lynch EM, Rappsilber J, Hiraoka Y, Haraguchi T, Sawin KE","authors_abbrev":"Bao XX et al.","pubmed_publication_date":"29 May 2018","pubmed_entrez_date":"2018-05-30","publication_year":"2018","canto_session_key":"d5613a72593b9597","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-05-31 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22718908","title":"DNA polymerization-independent functions of DNA polymerase epsilon in assembly and progression of the replisome in fission yeast.","citation":"Mol Biol Cell 2012 Aug;23(16):3240-53","abstract":"DNA polymerase epsilon (Pol ε) synthesizes the leading strands, following the CMG (Cdc45, Mcm2-7, and GINS [Go-Ichi-Nii-San]) helicase that translocates on the leading-strand template at eukaryotic replication forks. Although Pol ε is essential for the viability of fission and budding yeasts, the N-terminal polymerase domain of the catalytic subunit, Cdc20/Pol2, is dispensable for viability, leaving the following question: what is the essential role(s) of Pol ε? In this study, we investigated the essential roles of Pol ε using a temperature-sensitive mutant and a recently developed protein-depletion (off-aid) system in fission yeast. In cdc20-ct1 cells carrying mutations in the C-terminal domain of Cdc20, the CMG components, RPA, Pol α, and Pol δ were loaded onto replication origins, but Cdc45 did not translocate from the origins, suggesting that Pol ε is required for CMG helicase progression. In contrast, depletion of Cdc20 abolished the loading of GINS and Cdc45 onto origins, indicating that Pol ε is essential for assembly of the CMG complex. These results demonstrate that Pol ε plays essential roles in both the assembly and progression of CMG helicase.","doi":"10.1091/mbc.E12-05-0339","authors":"Handa T, Kanke M, Takahashi TS, Nakagawa T, Masukata H","authors_abbrev":"Handa T et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-06-22","publication_year":"2012","canto_session_key":"a3ce872c46b27485","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-12-18 15:02:04","canto_approved_date":"2026-06-09 14:31:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-18 15:01:54","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":99,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25D12.03c","SPAC23C4.18c","SPAC3H5.06c","SPAC6B12.11","SPBP8B7.14c","SPBC17D11.06","SPBC25H2.13c","SPBC211.04c","SPBC16D10.09","SPBC4.04c","SPCC16C4.22","SPBC1347.10","SPBC336.04","SPCC16A11.17","SPBP23A10.09","SPAC1B2.05","SPBP4H10.21c","SPCC1753.01c","SPAC24H6.06","SPAC17D4.02","SPBC725.13c","SPAC227.16c","SPBC3D6.09"],"gene_count":23,"ltp_gene_count":18,"approved_date":"2018-12-18"},{"uniquename":"PMID:24948786","title":"Histone H2B ubiquitination promotes the function of the anaphase-promoting complex/cyclosome in Schizosaccharomyces pombe.","citation":"G3 (Bethesda) 2014 Jun 19;4(8):1529-38","abstract":"Ubiquitination and deubiquitination of proteins are reciprocal events involved in many cellular processes, including the cell cycle. During mitosis, the metaphase to anaphase transition is regulated by the ubiquitin ligase activity of the anaphase-promoting complex/cyclosome (APC/C). Although the E3 ubiquitin ligase function of the APC/C has been well characterized, it is not clear whether deubiquitinating enzymes (DUBs) play a role in reversing APC/C substrate ubiquitination. Here we performed a genetic screen to determine what DUB, if any, antagonizes the function of the APC/C in the fission yeast Schizosaccharomyces pombe. We found that deletion of ubp8, encoding the Spt-Ada-Gcn5-Acetyl transferase (SAGA) complex associated DUB, suppressed temperature-sensitive phenotypes of APC/C mutants cut9-665, lid1-6, cut4-533, and slp1-362. Our analysis revealed that Ubp8 antagonizes APC/C function in a mechanism independent of the spindle assembly checkpoint and proteasome activity. Notably, suppression of APC/C mutants was linked to loss of Ubp8 catalytic activity and required histone H2B ubiquitination. On the basis of these data, we conclude that Ubp8 antagonizes APC/C function indirectly by modulating H2B ubiquitination status.","doi":"10.1534/g3.114.012625","authors":"Elmore ZC, Beckley JR, Chen JS, Gould KL","authors_abbrev":"Elmore ZC et al.","pubmed_publication_date":"19 Jun 2014","pubmed_entrez_date":"2014-06-21","publication_year":"2014","canto_session_key":"c461bdb0e3a386a5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.08c","SPBC6B1.06c","SPAC31G5.13","SPAC6F12.15c","SPBC106.09","SPCC1919.15","SPAC57A10.14","SPBC6B1.12c","SPCC126.04c","SPBC14C8.17c","SPAC22F8.12c","SPAC19G12.01c","SPCC622.09","SPAC13A11.04c"],"gene_count":14,"ltp_gene_count":14},{"uniquename":"EMBL:AU011703","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6370683","title":"The Schizosaccharomyces pombe sup3-i suppressor recognizes ochre, but not amber codons in vitro and in vivo.","citation":"EMBO J 1984 Feb;3(2):423-8","abstract":"The inefficient suppressor sup3-i of the fission yeast Schizosaccharomyces pombe is an ochre suppressor. Sup3-i was derived from the efficient serine inserting UGA suppressor sup3-e. The cloning and sequencing of the sup3-i gene indicate that the suppressor is different from the parent sup3-e by a C----T substitution in the sequence coding for the middle position of the anticodon. In vitro translation assays supplemented with purified sup3-i tRNA and programmed with Xenopus globin mRNAs lead to the accumulation of a readthrough product in response to UAA termination signals, but not in response to UGA termination codons. Transformation of Saccharomyces cerevisiae nonsense mutant strains with plasmid DNA carrying the S. pombe sup3-i gene, led to ochre, but not amber or UGA suppression in vivo.","authors":"Hottinger H, Stadelmann B, Pearson D, Frendewey D, Kohli J, Söll D","authors_abbrev":"Hottinger H et al.","pubmed_publication_date":"Feb 1984","pubmed_entrez_date":"1984-02-01","publication_year":"1984","canto_session_key":"36263e61e363c966","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-30 10:22:43","canto_approved_date":"2021-11-05 19:35:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-30 10:22:36","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPATRNASER.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-30"},{"uniquename":"PMID:34085220","title":"Highly Synchronous Mitotic Progression in Schizosaccharomyces pombe Upon Relief of Transient Cdc2-asM17 Inhibition.","citation":"Methods Mol Biol 2021;2329:123-142","abstract":"Synchronized progression of a cell population through the cell division cycle supports the biochemical and functional dissection of cell cycle controls and execution. The concerted behaviour of the population reflects the attributes of each cell within that population. The reversible imposition of a block to cell cycle progression at the G2-M boundary through transient inactivation of the Cdk1-Cyclin B activating phosphatase, Cdc25, with the temperature sensitive cdc25-22 mutant, has been widely used to study fission yeast mitosis and DNA replication. However, the biology of the compromised Cdc25-22 phosphatase generates significant division abnormalities upon release from mitotic arrest. We show how reversible inhibition of Cdc2-asM17, with the ATP analog 3-BrB-PP1, generates higher levels of synchrony with timing and morphology much more reminiscent of a normal division. We also describe a version of the H1 kinase assay of Cdk1-Cyclin B activity that is widely used to monitor mitotic progression which does not require radiolabeled ATP.","doi":"10.1007/978-1-0716-1538-6_10","authors":"Singh P, Halova L, Hagan IM","authors_abbrev":"Singh P et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-06-04","publication_year":"2021","canto_session_key":"40b76fa6de8bc15d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-06 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:24353754","title":"PombeX: robust cell segmentation for fission yeast transillumination images.","citation":"PLoS One 2013;8(12):e81434","abstract":"Schizosaccharomyces pombe shares many genes and proteins with humans and is a good model for chromosome behavior and DNA dynamics, which can be analyzed by visualizing the behavior of fluorescently tagged proteins in vivo. Performing a genome-wide screen for changes in such proteins requires developing methods that automate analysis of a large amount of images, the first step of which requires robust segmentation of the cell. We developed a segmentation system, PombeX, that can segment cells from transmitted illumination images with focus gradient and varying contrast. Corrections for focus gradient are applied to the image to aid in accurate detection of cell membrane and cytoplasm pixels, which is used to generate initial contours for cells. Gradient vector flow snake evolution is used to obtain the final cell contours. Finally, a machine learning-based validation of cell contours removes most incorrect or spurious contours. Quantitative evaluations show overall good segmentation performance on a large set of images, regardless of differences in image quality, lighting condition, focus condition and phenotypic profile. Comparisons with recent related methods for yeast cells show that PombeX outperforms current methods, both in terms of segmentation accuracy and computational speed.","doi":"10.1371/journal.pone.0081434","authors":"Peng JY, Chen YJ, Green MD, Sabatinos SA, Forsburg SL, Hsu CN","authors_abbrev":"Peng JY et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-12-20","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-01-15 18:44:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10996309","title":"Schizosaccharomyces pombe Rad9 contains a BH3-like region and interacts with the anti-apoptotic protein Bcl-2.","citation":"FEBS Lett 2000 Sep 15;481(2):122-6","abstract":"Here we report that the Schizosaccharomyces pombe Rad9 (SpRad9) protein contains a group of amino acids with similarity to the Bcl-2 homology 3 death domain, which is required for SpRad9 interaction with human Bcl-2 and apoptosis induction in human cells. Overexpression of Bcl-2 in S. pombe inhibits cell growth independently of rad9, but enhances resistance of rad9-null cells to methyl methanesulfonate, ultraviolet and ionizing radiation. These observations suggest that SpRad9 may represent the first member of the Bcl-2 protein family identified in yeast, though the cell death pathways in S. pombe may differ from those found in mammals.","authors":"Komatsu K, Hopkins KM, Lieberman HB, Wang H","authors_abbrev":"Komatsu K et al.","pubmed_publication_date":"15 Sep 2000","pubmed_entrez_date":"2000-09-21","publication_year":"2000","canto_session_key":"422cbe6fb6bdb6bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-29 16:04:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-26 13:34:04","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-26"},{"uniquename":"PMID:15117754","title":"Identification of DNA regulatory motifs using Bayesian variable selection.","citation":"Bioinformatics 2004 Nov 01;20(16):2553-61","abstract":"Understanding the mechanisms that determine gene expression regulation is an important and challenging problem. A common approach consists of identifying DNA-binding sites from a collection of co-regulated genes and their nearby non-coding DNA sequences. Here, we consider a regression model that linearly relates gene expression levels to a sequence matching score of nucleotide patterns. We use Bayesian models and stochastic search techniques to select transcription factor binding site candidates, as an alternative to stepwise regression procedures used by other investigators.\nWe demonstrate through simulated data the improved performance of the Bayesian variable selection method compared to the stepwise procedure. We then analyze and discuss the results from experiments involving well-studied pathways of Saccharomyces cerevisiae and Schizosaccharomyces pombe. We identify regulatory motifs known to be related to the experimental conditions considered. Some of our selected motifs are also in agreement with recent findings by other researchers. In addition, our results include novel motifs that constitute promising sets for further assessment.\nThe Matlab code for implementing the Bayesian variable selection method may be obtained from the corresponding author.","authors":"Tadesse MG, Vannucci M, Liò P","authors_abbrev":"Tadesse MG et al.","pubmed_publication_date":"01 Nov 2004","pubmed_entrez_date":"2004-05-01","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14522690","title":"Traditional non-alcoholic beverage, Togwa, in East Africa, produced from maize flour and germinated finger millet.","citation":"Int J Food Sci Nutr 2003 Nov;54(6):447-55","abstract":"The traditional non-alcoholic beverage in East Africa, togwa, produced from the flour of maize and germinated finger millet (finger millet malt), was investigated. The preparation techniques of togwa observed in the rural villages of East Africa are described, and the temperature and pH profile of togwa during its manufacture are also shown. Maize and finger millet malt should be the source of starch and amylase, respectively. Maize flour slurry was heated once with stirring up to around 80 degrees C and cooled to about 50 degrees C, and then finger millet malt flour was added to the warm porridge paste and kept at about 50 degrees C for 20 min. The consistency of the paste was suddenly reduced by addition of finger millet malt flour and the gel paste changed to viscous liquid, which was kept in a container and incubated at ambient temperature for 15 h. After incubation it became sweet and was ready to drink without removal of any insoluble materials. Changes in the concentration of glucose and lactic acid of togwa during its maturation period were measured using portable devices until 70 h incubation at the rural village of Tanzania in a dry season. Glucose level increased with incubation and reached the threshold value of sweetness; 24 h incubation later, the lactate level increased and pH decreased. The preparation techniques of a traditional alcoholic beverage, pombe, were also investigated in the same rural locality, and the differences and characteristics of both traditional beverages are discussed.","authors":"Kitabatake N, Gimbi DM, Oi Y","authors_abbrev":"Kitabatake N et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-10-03","publication_year":"2003","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23521895","title":"Chemical genetic screen in fission yeast reveals roles for vacuolar acidification, mitochondrial fission, and cellular GMP levels in lifespan extension.","citation":"Aging Cell 2013 Aug;12(4):574-83","abstract":"The discovery that genetic mutations in several cellular pathways can increase lifespan has lent support to the notion that pharmacological inhibition of aging pathways can be used to extend lifespan and to slow the onset of age-related diseases. However, so far, only few compounds with such activities have been described. Here, we have conducted a chemical genetic screen for compounds that cause the extension of chronological lifespan of Schizosaccharomyces pombe. We have characterized eight natural products with such activities, which has allowed us to uncover so far unknown anti-aging pathways in S. pombe. The ionophores monensin and nigericin extended lifespan by affecting vacuolar acidification, and this effect depended on the presence of the vacuolar ATPase (V-ATPase) subunits Vma1 and Vma3. Furthermore, prostaglandin J₂ displayed anti-aging properties due to the inhibition of mitochondrial fission, and its effect on longevity required the mitochondrial fission protein Dnm1 as well as the G-protein-coupled glucose receptor Git3. Also, two compounds that inhibit guanosine monophosphate (GMP) synthesis, mycophenolic acid (MPA) and acivicin, caused lifespan extension, indicating that an imbalance in guanine nucleotide levels impinges upon longevity. We furthermore have identified diindolylmethane (DIM), tschimganine, and the compound mixture mangosteen as inhibiting aging. Taken together, these results reveal unanticipated anti-aging activities for several phytochemicals and open up opportunities for the development of novel anti-aging therapies.","doi":"10.1111/acel.12077","authors":"Stephan J, Franke J, Ehrenhofer-Murray AE","authors_abbrev":"Stephan J et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-03-26","publication_year":"2013","canto_session_key":"13f28eac0268b48b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-22 15:26:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-22 15:25:58","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC343.05","SPAC22E12.14c","SPBC25B2.02c","SPBC1718.06","SPBC12C2.08","SPAC1B3.14","SPCC1753.02c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2014-10-22"},{"uniquename":"EMBL:SPEIF4E","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11696322","title":"Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division.","citation":"Curr Biol 2001 Oct 30;11(21):1656-65","abstract":"Both symmetric and asymmetric cell divisions are required for the generation of appropriate cell lineages during development. Wild-type Schizosaccharomyces pombe cells divide in a symmetric fashion to produce two similar rod-shaped daughter cells. Formins are proteins with conserved roles in cell polarity, cytokinesis, and the regulation of actin and microtubule cytoskeletons.\nHere, we identify and characterize a new S. pombe formin, for3p. for3 Delta mutant cells divide in an asymmetric manner; a mother cell divides medially to produce one daughter cell that develops into a monopolar cell and one daughter that develops into a bipolar cell. Both daughter cells recapitulate similar asymmetric lineages themselves. Inheritance of the bipolar pattern correlates with inheritance of the recent birth scar, not with asymmetry in the spindle pole bodies. for3 Delta mutants lack interphase actin cables and have delocalized actin patch and myo52p (type V myosin) distributions. for3 Delta cells have normal microtubule dynamics and cortical interactions but have defects in microtubule organization and increased numbers of microtubule bundles. for3p-GFP is localized at both cell tips in an actin-dependent manner and at the cell division site.\nfor3p is a cell polarity factor required for interphase actin cable formation and microtubule organization. The for3 Delta phenotype suggests that cells are able to grow in a polarized manner even in the absence of functional actin cables and polarized distribution of actin patches. for3p and possibly actin cables are part of a regulatory network that ensures that cell divisions are symmetric.","authors":"Feierbach B, Chang F","authors_abbrev":"Feierbach B et al.","pubmed_publication_date":"30 Oct 2001","pubmed_entrez_date":"2001-11-07","publication_year":"2001","canto_session_key":"11b0f6081ab49c11","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-22 11:42:14","canto_approved_date":"2026-04-20 11:55:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-18 06:38:54","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPCC895.05"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-10-22"},{"uniquename":"EMBL:AF027823","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33775846","title":"Simplification of nutritional conditions in transformation procedures for genome editing with the CRISPR/Cas9 system for fission yeast.","citation":"Gene 2021 Jun 05;784:145595","abstract":"CRISPR/Cas9 is a powerful tool for genome editing. Several studies have been conducted to take the benefit of the versatile tool in the fission yeast Schizosaccharomyces pombe. However, the protocols for the CRISPR/Cas9 system proposed in previous studies are complicated in culture conditions compared to traditional genome editing methods. In this study, we introduced vectors for expression of sgRNA as well as Cas9, which employ natMX6 and bsdMX6 dominant selection markers. Using these materials, we examined nutritional conditions of cell cultures and found that nitrogen depletion introduced in previous methods does not affect the efficiency of genome editing. We found that bsdMX6-based plasmids enable us to skip any recovery steps before plating onto medium containing blasticidin S, unlike other antibiotic resistance selection markers. We thus propose easier transformation procedures with natMX6 and particularly bsdMX6 markers. We also simulate prescreening of mutants by genotyping with DNA endonucleases or proofreading PCR instead of relying on existing knowledge of mutant phenotypes. These materials and methods assist easy construction of S. pombe strains using CRISPR/Cas9, thereby accelerating seamless introduction of CRISPR/Cas9 to S. pombe researchers.","doi":"10.1016/j.gene.2021.145595","authors":"Li S, Toya M, Sato M","authors_abbrev":"Li S et al.","pubmed_publication_date":"05 Jun 2021","pubmed_entrez_date":"2021-03-29","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-03-31 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29720420","title":"The contribution of non-essential  Schizosaccharomyces pombe  genes to fitness in response to altered nutrient supply and target of rapamycin activity.","citation":"Open Biol 2018 May;8(5)","abstract":"Nutrient fluctuations in the cellular environment promote changes in cell metabolism and growth to adapt cell proliferation accordingly. The target of rapamycin (TOR) signalling network plays a key role in the coordination of growth and cell proliferation with the nutrient environment and, importantly, nutrient limitation reduces TOR complex 1 (TORC1) signalling. We have performed global quantitative fitness profiling of the collection of  Schizosaccharomyces pombe  strains from which non-essential genes have been deleted. We identified genes that regulate fitness when cells are grown in a nutrient-rich environment compared with minimal environments, with varying nitrogen sources including ammonium, glutamate and proline. In addition, we have performed the first global screen for genes that regulate fitness when both TORC1 and TORC2 signalling is reduced by Torin1. Analysis of genes whose deletions altered fitness when nutrients were limited, or when TOR signalling was compromised, identified a large number of genes that regulate transmembrane transport, transcription and chromatin organization/regulation and vesicle-mediated transport. The ability to tolerate reduced TOR signalling placed demands upon a large number of biological processes including autophagy, mRNA metabolic processing and nucleocytoplasmic transport. Importantly, novel biological processes and all processes known to be regulated by TOR were identified in our screens. In addition, deletion of 62 genes conserved in humans gave rise to strong sensitivity or resistance to Torin1, and 29 of these 62 genes have novel links to TOR signalling. The identification of chromatin and transcriptional regulation, nutritional uptake and transport pathways in this powerful genetic model now paves the way for a molecular understanding of how cells adapt to the chronic and acute fluctuations in nutrient supply that all eukaryotes experience at some stage, and which is a key feature of cancer cells within solid tumours.","doi":"10.1098/rsob.180015","authors":"Lie S, Banks P, Lawless C, Lydall D, Petersen J","authors_abbrev":"Lie S et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-05-04","publication_year":"2018","canto_session_key":"d86927c452a015b5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-05-05 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26251183","title":"POLE mutations in families predisposed to cutaneous melanoma.","citation":"Fam Cancer 2015 Dec;14(4):621-8","abstract":"Germline mutations in the exonuclease domain of POLE have been shown to predispose to colorectal cancers and adenomas. POLE is an enzyme involved in DNA repair and chromosomal DNA replication. In order to assess whether such mutations might also predispose to cutaneous melanoma, we interrogated whole-genome and exome data from probands of 34 melanoma families lacking pathogenic mutations in known high penetrance melanoma susceptibility genes: CDKN2A, CDK4, BAP1, TERT, POT1, ACD and TERF2IP. We found a novel germline mutation, POLE p.(Trp347Cys), in a 7-case cutaneous melanoma family. Functional assays in S. pombe showed that this mutation led to an increased DNA mutation rate comparable to that seen with a Pol ε mutant with no exonuclease activity. We then performed targeted sequencing of POLE in 1243 cutaneous melanoma cases and found that a further ten probands had novel or rare variants in the exonuclease domain of POLE. Although this frequency is not significantly higher than that in unselected Caucasian controls, we observed multiple cancer types in the melanoma families, suggesting that some germline POLE mutations may predispose to a broad spectrum of cancers, including melanoma. In addition, we found the first mutation outside the exonuclease domain, p.(Gln520Arg), in a family with an extensive history of colorectal cancer.","doi":"10.1007/s10689-015-9826-8","authors":"Aoude LG, Heitzer E, Johansson P, Gartside M, Wadt K, Pritchard AL, Palmer JM, Symmons J, Gerdes AM, Montgomery GW, Martin NG, Tomlinson I, Kearsey S, Hayward NK","authors_abbrev":"Aoude LG et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-08-08","publication_year":"2015","canto_session_key":"dcd4b5994e8b85ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-10-08 15:38:26","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-08-25 11:52:58","canto_added_date":"2015-08-09 00:19:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-08-25"},{"uniquename":"PMID:23035257","title":"Targeting mitochondrial transcription in fission yeast with ETB, an inhibitor of HSP60, the chaperone that binds to the mitochondrial transcription factor Mtf1.","citation":"Genes Cells 2012 Feb;17(2):122-31","abstract":"Mtf1 has been characterized as a mitochondrial transcription factor and is shown to regulat mitochondrial transcription. Mtf1 has an additional function as a transcription factor for the nuclear gene srk1 in fission yeast. Hsp60 has been linked to a variety of important cellular functions such as apoptosis and the immune response. It functions mainly as a molecular chaperone that assists correct protein folding in the mitochondrion. Epolactaene tertiary butyl ester(ETB) is an inhibitor of human Hsp60 that can inhibit Hsp60 chaperone activity. In this study,we report that in fission yeast, Mtf1 binds to Hsp60 in vivo and in vitro, ETB inhibits the binding of Mtf1 and Hsp60, and inhibits mitochondrial transcription but not nuclear transcription of srk1. We propose that Hsp60 may act as a molecular chaperone that folds mitochondrial Mtf1 into a functional form and that ETB inhibits this Hsp60 chaperone activity by disrupting Mtf1 binding to Hsp60 and thus inhibits mitochondrial transcription in fission yeast.","authors":"Sun W, Wang L, Jiang H, Chen D, Murchie AI","authors_abbrev":"Sun W et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2012-10-05","publication_year":"2012","canto_session_key":"f9396b475a851162","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-12-13 16:53:24","canto_approved_date":"2024-12-14 19:38:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-13 16:53:13","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC794.09c","SPAC12G12.04","SPAC1002.08c","SPBC1711.06"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-12-13"},{"uniquename":"PMID:9106659","title":"The meiotic recombination hot spot created by the single-base substitution ade6-M26 results in remodeling of chromatin structure in fission yeast.","citation":"Genes Dev 1997 Apr 01;11(7):876-86","abstract":"The G -->T transversion mutation, ade6-M26, creates the heptanucleotide sequence ATGACTG, which lies close to the 5' end of the open reading frame of the ade6 gene in Schizosaccharomyces pombe. The mutation generates a meiosis-specific recombination hot spot and a binding site for the Mts1/Mts2 protein. We examined the chromatin structure at the ade6 locus in the M26 strain and compared it to that of the wild-type and hot spot-negative control M375. Micrococcal nuclease (MNase) digestion and indirect end-labeling methods were applied. In the M26 strain, we detected a new MNase-hypersensitive site at the position of the M26 mutation and no longer observed the phasing of nucleosomes seen in the wild-type and the M375 strains. Quantitative comparison of MNase sensitivity of the chromatin in premeiotic and meiotic cultures revealed a small meiotic induction of MNase hypersensitivity in the ade6 promoter region of the wild-type and M375 strains. The meiotic induction of MNase hypersensitivity was enhanced significantly in the ade6 promoter region of the M26 strain and also occurred at the M26 mutation site. The formation of the MNase-sensitive region around the heptamer sequence was abolished by the introduction of single-nucleotide substitutions in the heptamer sequence, which also abolish hot spot activity and binding of Mts1/Mts2. These data suggest that Mts1/Mts2 binding to the heptamer sequence results in a chromatin structure suitable for the recruitment of a meiosis-specific recombination function or functions.","authors":"Mizuno K, Emura Y, Baur M, Kohli J, Ohta K, Shibata T","authors_abbrev":"Mizuno K et al.","pubmed_publication_date":"01 Apr 1997","pubmed_entrez_date":"1997-04-01","publication_year":"1997","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8082176","title":"A mitochondrial group-I intron in fission yeast encodes a maturase and is mobile in crosses.","citation":"Curr Genet 1994 Apr;25(4):336-41","abstract":"The open reading frame in the first intron of the mitochondrial gene encoding subunit I of cytochrome c oxidase encodes a maturase and stimulates homologous recombination in Escherichia coli. In this paper, we demonstrate that this intron is mobile in crosses, indicating that it also encodes an endonuclease. This is the first report on an intron which possesses mobility and acts as a maturase.","authors":"Schäfer B, Wilde B, Massardo DR, Manna F, Del Giudice L, Wolf K","authors_abbrev":"Schäfer B et al.","pubmed_publication_date":"Apr 1994","pubmed_entrez_date":"1994-04-01","publication_year":"1994","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16624923","title":"Fission yeast Num1p is a cortical factor anchoring dynein and is essential for the horse-tail nuclear movement during meiotic prophase.","citation":"Genetics 2006 Jul;173(3):1187-96","abstract":"During meiotic prophase in the fission yeast Schizosaccharomyces pombe, the nucleus oscillates between the two ends of a cell. This oscillatory nuclear movement is important to promote accurate pairing of homologous chromosomes and requires cytoplasmic dynein. Dynein accumulates at the points where microtubule plus ends contact the cell cortex and generate a force to drive nuclear oscillation. However, it remains poorly understood how dynein associates with the cell cortex. Here we show that S. pombe Num1p functions as a cortical-anchoring factor for dynein. Num1p is expressed in a meiosis-specific manner and localized to the cell cortex through its C-terminal PH domain. The num1 deletion mutant shows microtubule dynamics comparable to that in the wild type. However, it lacks cortical accumulation of dynein and is defective in the nuclear oscillation as is the case for the dynein mutant. We also show that Num1p can recruit dynein independently of the CLIP-170 homolog Tip1p.","authors":"Yamashita A, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-04-21","publication_year":"2006","canto_session_key":"8725231a57c6eeb3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-23 10:51:18","canto_approved_date":"2022-07-28 15:26:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-19 15:01:26","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPAC27D7.13c","SPBC216.02","SPAC3C7.12"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-11-23"},{"uniquename":"PMID:34289255","title":"Corrections: Fission Yeast Schizosaccharomyces pombe: A Unicellular \"Micromammal\" Model Organism Aditi Vyas, Anna V. Freitas, Zachary A. Ralston, and Zhaohua Tang.","citation":"Curr Protoc 2021 Jul;1(7):e225","abstract":"","doi":"10.1002/cpz1.225","authors":"Vyas A, Freitas AV, Ralston ZA, Tang Z","authors_abbrev":"Vyas A et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-07-21","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-07-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10731689","title":"Role of Atf1 and Pap1 in the induction of the catalase gene of fission yeast schizosaccharomyces pombe.","citation":"J Biochem 2000 Feb;127(2):233-8","abstract":"We examined the induction of the catalase gene (ctt1(+)) of fission yeast Schizosaccharomyces pombe in response to several stresses by using mutants of transcription factors (Atf1 and Pap1) and a series of deletion mutants of the ctt1(+) promoter region. A transcription factor, Atf1, and its binding site are necessary for the induction of ctt1(+) by osmotic stress, UV irradiation, and heat shock. Induction by menadione treatment, which produces superoxide anion, required element A, the region from -111 to -90 (numbered with the transcription start site as +1). The factor responsible for the induction of the gene by oxidative stress via element A was identified as the transcription factor Pap1. We also found that Atf1 is activated by menadione treatment in pap1 mutant cells, although it is not activated by menadione treatment in pap1(+) cells. The activity of catalase is not increased in pap1 cells by several stresses, despite mRNA induction, suggesting that Pap1 plays some role in the expression of catalase activity.","authors":"Nakagawa CW, Yamada K, Mutoh N","authors_abbrev":"Nakagawa CW et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-03-25","publication_year":"2000","canto_session_key":"e10a225101cf987c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-25 15:19:26","canto_approved_date":"2020-01-06 16:06:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-07-24 16:03:45","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPCC757.07c","SPAC1783.07c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2017-07-25"},{"uniquename":"PMID:28301289","title":"Genome-wide characterization of Mediator recruitment, function, and regulation.","citation":"Transcription 2017 May 27;8(3):169-174","abstract":"Mediator is a conserved and essential coactivator complex broadly required for RNA polymerase II (RNAPII) transcription. Recent genome-wide studies of Mediator binding in budding yeast have revealed new insights into the functions of this critical complex and raised new questions about its role in the regulation of gene expression.","doi":"10.1080/21541264.2017.1291082","authors":"Grünberg S, Zentner GE","authors_abbrev":"Grünberg S et al.","pubmed_publication_date":"27 May 2017","pubmed_entrez_date":"2017-03-17","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-02-09 01:15:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21215368","title":"The Cul4-Ddb1(Cdt)² ubiquitin ligase inhibits invasion of a boundary-associated antisilencing factor into heterochromatin.","citation":"Cell 2011 Jan 07;144(1):41-54","abstract":"Partitioning of chromosomes into euchromatic and heterochromatic domains requires mechanisms that specify boundaries. The S. pombe JmjC family protein Epe1 prevents the ectopic spread of heterochromatin and is itself concentrated at boundaries. Paradoxically, Epe1 is recruited to heterochromatin by HP1 silencing factors that are distributed throughout heterochromatin. We demonstrate here that the selective enrichment of Epe1 at boundaries requires its regulation by the conserved Cul4-Ddb1(Cdt)² ubiquitin ligase, which directly recognizes Epe1 and promotes its polyubiquitylation and degradation. Strikingly, in cells lacking the ligase, Epe1 persists in the body of heterochromatin thereby inducing a defect in gene silencing. Epe1 is the sole target of the Cul4-Ddb1(Cdt)² complex whose destruction is necessary for the preservation of heterochromatin. This mechanism acts parallel with phosphorylation of HP1/Swi6 by CK2 to restrict Epe1. We conclude that the ubiquitin-dependent sculpting of the chromosomal distribution of an antisilencing factor is critical for heterochromatin boundaries to form correctly.","doi":"10.1016/j.cell.2010.11.051","authors":"Braun S, Garcia JF, Rowley M, Rougemaille M, Shankar S, Madhani HD","authors_abbrev":"Braun S et al.","pubmed_publication_date":"07 Jan 2011","pubmed_entrez_date":"2011-01-11","publication_year":"2011","canto_session_key":"3f965e2cb9468a50","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-07-02 15:05:52","canto_approved_date":"2025-07-02 15:05:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-07-02 15:05:47","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":102,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC215.06c","SPCC11E10.08","SPAC23D3.01","SPCC18B5.03","SPCC417.07c","SPAC8C9.17c","SPBC651.10","SPAC664.01c","SPBCPT2R1.07c","SPAC29B12.03","SPAC19A8.10","SPBC216.06c","SPCC622.16c","SPAC17H9.19c","SPBC32H8.11","SPBC2D10.17","SPAC1687.05","SPBC4B4.03","SPAC17H9.10c","SPAC1851.03","SPCC895.07"],"gene_count":21,"ltp_gene_count":18,"approved_date":"2025-07-02"},{"uniquename":"PMID:8088515","title":"An analysis of interference in the fission yeast Schizosaccharomyces pombe.","citation":"Genetics 1994 Jul;137(3):701-7","abstract":"The evaluation of three-point crosses at the tetrad and random spore level leads to the conclusion that both chiasma and chromatid interference are absent in the fission yeast Schizosaccharomyces pombe.","authors":"Munz P","authors_abbrev":"Munz P","pubmed_publication_date":"Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8001176","title":"Mapping of additional markers in fission yeast, especially fus1 and three mfm genes.","citation":"Curr Genet 1994 Aug;26(2):187-9","abstract":"The following genes of the fission yeast Schizosaccharomyces pombe have been mapped by tetrad analysis--chromosome arm I-L: mfm2, rad24, rad25; I-R: abc1, fus1, mfm1; II-L: mfm3; II-R: mam1, rad13. A hot-spot of meiotic recombination although not quite so active as suggested by previous maps, may be located between rad25 and aro5 on I-L.","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3142867","title":"Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of Schizosaccharomyces pombe.","citation":"J Bacteriol 1988 Dec;170(12):5968-70","abstract":"The alpha-aminoadipate (AA) pathway for the biosynthesis of lysine was investigated in the wild type and in lysine auxotrophs of the fission yeast Schizosaccharomyces pombe. Of the eight enzyme activities of the AA pathway that have been examined so far, six were present in the extract of wild-type S. pombe cells. Growth response to AA and accumulation studies indicated that three lysine auxotrophs, the lys2-97, lys4-95, and lys8-1 strains, were blocked before the AA step and that four lysine auxotrophs, the lys1-131, lys3-37, lys6-3, and lys7-2 strains, were blocked after the AA step. Among the mutants investigated, the lys2-97 mutant exhibited an enzyme lesion at the cis-homoaconitate hydratase step, the lys1-131 and lys7-2 mutants exhibited lesions at the AA reductase step, and lys3-37 exhibited a lesion at the saccharopine dehydrogenase step. These results demonstrated the basic similarity of the AA pathway in S. pombe and Saccharomyces cerevisiae.","authors":"Ye ZH, Bhattacharjee JK","authors_abbrev":"Ye ZH et al.","pubmed_publication_date":"Dec 1988","pubmed_entrez_date":"1988-12-01","publication_year":"1988","canto_session_key":"bf64e763d446eedd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-06-30 10:45:45","canto_approved_date":"2026-03-09 15:57:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 14:36:58","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC343.16","SPAC227.18","SPAP7G5.04c","SPAC17C9.02c","SPBC1105.02c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-06-30"},{"uniquename":"PMID:26787842","title":"Scaffold Protein Ahk1, Which Associates with Hkr1, Sho1, Ste11, and Pbs2, Inhibits Cross Talk Signaling from the Hkr1 Osmosensor to the Kss1 Mitogen-Activated Protein Kinase.","citation":"Mol Cell Biol 2016 Jan 19;36(7):1109-23","abstract":"In the budding yeast Saccharomyces cerevisiae, osmostress activates the Hog1 mitogen-activated protein kinase (MAPK), which regulates diverse osmoadaptive responses. Hkr1 is a large, highly glycosylated, single-path transmembrane protein that is a putative osmosensor in one of the Hog1 upstream pathways termed the HKR1 subbranch. The extracellular region of Hkr1 contains both a positive and a negative regulatory domain. However, the function of the cytoplasmic domain of Hkr1 (Hkr1-cyto) is unknown. Here, using a mass spectrometric method, we identified a protein, termed Ahk1 (Associated with Hkr1), that binds to Hkr1-cyto. Deletion of the AHK1 gene (in the absence of other Hog1 upstream branches) only partially inhibited osmostress-induced Hog1 activation. In contrast, Hog1 could not be activated by constitutively active mutants of the Hog1 pathway signaling molecules Opy2 or Ste50 in ahk1Δ cells, whereas robust Hog1 activation occurred in AHK1(+) cells. In addition to Hkr1-cyto binding, Ahk1 also bound to other signaling molecules in the HKR1 subbranch, including Sho1, Ste11, and Pbs2. Although osmotic stimulation of Hkr1 does not activate the Kss1 MAPK, deletion of AHK1 allowed Hkr1 to activate Kss1 by cross talk. Thus, Ahk1 is a scaffold protein in the HKR1 subbranch and prevents incorrect signal flow from Hkr1 to Kss1.","doi":"10.1128/MCB.01017-15","authors":"Nishimura A, Yamamoto K, Oyama M, Kozuka-Hata H, Saito H, Tatebayashi K","authors_abbrev":"Nishimura A et al.","pubmed_publication_date":"19 Jan 2016","pubmed_entrez_date":"2016-01-21","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC7D4.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24358832","title":"Identification of two telomere-proximal fission yeast DNA replication origins constrained by nearby cis-acting sequences to replicate in late S phase.","citation":"F1000Res 2012;1:58","abstract":"Telomeres of the fission yeast,  Schizosaccharomyces pombe, are known to replicate in late S phase, but the reasons for this late replication are not fully understood. We have identified two closely-spaced DNA replication origins, 5.5 to 8 kb upstream from the telomere itself. These are the most telomere-proximal of all the replication origins in the fission yeast genome. When located by themselves in circular plasmids, these origins fired in early S phase, but if flanking sequences closer to the telomere were included in the circular plasmid, then replication was restrained to late S phase - except in cells lacking the replication-checkpoint kinase, Cds1. We conclude that checkpoint-dependent late replication of telomere-associated sequences is dependent on nearby cis-acting sequences, not on proximity to the physical end of a linear chromosome.","doi":"10.12688/f1000research.1-58.v1","authors":"Chaudari A, Huberman JA","authors_abbrev":"Chaudari A et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2013-12-24","publication_year":"2012","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:48:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12779461","title":"Mathematical model of the cell division cycle of fission yeast.","citation":"Chaos 2001 Mar;11(1):277-286","abstract":"Much is known about the genes and proteins controlling the cell cycle of fission yeast. Can these molecular components be spun together into a consistent mechanism that accounts for the observed behavior of growth and division in fission yeast cells? To answer this question, we propose a mechanism for the control system, convert it into a set of 14 differential and algebraic equations, study these equations by numerical simulation and bifurcation theory, and compare our results to the physiology of wild-type and mutant cells. In wild-type cells, progress through the cell cycle (G1-->S-->G2-->M) is related to cyclic progression around a hysteresis loop, driven by cell growth and chromosome alignment on the metaphase plate. However, the control system operates much differently in double-mutant cells, wee1(-) cdc25Delta, which are defective in progress through the latter half of the cell cycle (G2 and M phases). These cells exhibit \"quantized\" cycles (interdivision times clustering around 90, 160, and 230 min). We show that these quantized cycles are associated with a supercritical Hopf bifurcation in the mechanism, when the wee1 and cdc25 genes are disabled. (c) 2001 American Institute of Physics.","authors":"Novak B, Pataki Z, Ciliberto A, Tyson JJ","authors_abbrev":"Novak B et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2003-06-05","publication_year":"2001","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15579205","title":"Mapping and mutation of the conserved DNA polymerase interaction motif (DPIM) located in the C-terminal domain of fission yeast DNA polymerase delta subunit Cdc27.","citation":"BMC Mol Biol 2004 Dec 03;5(1):21","abstract":"DNA polymerases alpha and delta play essential roles in the replication of chromosomal DNA in eukaryotic cells. DNA polymerase alpha (Pol alpha)-primase is required to prime synthesis of the leading strand and each Okazaki fragment on the lagging strand, whereas DNA polymerase delta (Pol delta) is required for the elongation stages of replication, a function it appears capable of performing on both leading and lagging strands, at least in the absence of DNA polymerase epsilon (Pol epsilon).\nHere it is shown that the catalytic subunit of Pol alpha, Pol1, interacts with Cdc27, one of three non-catalytic subunits of fission yeast Pol delta, both in vivo and in vitro. Pol1 interacts with the C-terminal domain of Cdc27, at a site distinct from the previously identified binding sites for Cdc1 and PCNA. Comparative protein sequence analysis identifies a protein sequence motif, called the DNA polymerase interaction motif (DPIM), in Cdc27 orthologues from a wide variety of eukaryotic species, including mammals. Mutational analysis shows that the DPIM in fission yeast Cdc27 is not required for effective DNA replication, repair or checkpoint function.\nA short protein sequence motif (DPIM) has been identified as mediating Pol alpha-Pol delta interactions in fission yeast. Despite being conserved across species, mutational analysis indicates the DPIM does not play an essential role in vivo, suggesting that interaction between the two polymerases is also non-essential.","authors":"Gray FC, Pohler JR, Warbrick E, MacNeill SA","authors_abbrev":"Gray FC et al.","pubmed_publication_date":"03 Dec 2004","pubmed_entrez_date":"2004-12-08","publication_year":"2004","canto_session_key":"3039c7ffca6fc091","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-02-12 16:47:24","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-12 16:46:57","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":48,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_15579205_phaf.tsv"}],"genes":["SPBC1734.02c","SPAC27E2.05","SPAC3H5.06c","SPBC16D10.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-02-12"},{"uniquename":"PMID:16931337","title":"An isoquinolinium derivative selectively inhibits MAPK Spc1 of the stress-activated MAPK cascade of Schizosaccharomyces pombe.","citation":"Chem Biol 2006 Aug;13(8):881-9","abstract":"We have extended the search for selective inhibitors of the kinases of MAPK cascades by screening a derivative library of one of the isoquinoline rings of the protoberberine backbone. HWY 5069 inhibited the proliferation of wild-type and all mutants of Schizosaccharomyces pombe examined, except spc1Delta, at a minimal inhibitory concentration (MIC) of 3.76 microM. HWY 5069 also completely inhibited Spc1 kinase activity in vitro with an IC(50) of 16.4 microM as a competitive inhibitor of substrate binding. It was highly selective for Spc1 and did not affect the activity of other kinases in the MAPK cascades of fission yeast and mammals, including functional homologs of Spc1.","authors":"Kim HJ, Park JE, Jin S, Kim JH, Song K","authors_abbrev":"Kim HJ et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-26","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25844024","title":"A microfluidic device for the hydrodynamic immobilisation of living fission yeast cells for super-resolution imaging.","citation":"Sens Actuators B Chem 2014 Mar 01;192:36-41","abstract":"We describe a microfluidic device designed specifically for the reversible immobilisation of  Schizosaccharomyces pombe  (Fission Yeast) cells to facilitate live cell super-resolution microscopy. Photo-Activation Localisation Microscopy (PALM) is used to create detailed super-resolution images within living cells with a modal accuracy of >25 nm in the lateral dimensions. The novel flow design captures and holds cells in a well-defined array with minimal effect on the normal growth kinetics. Cells are held over several hours and can continue to grow and divide within the device during fluorescence imaging.","authors":"Bell L, Seshia A, Lando D, Laue E, Palayret M, Lee SF, Klenerman D","authors_abbrev":"Bell L et al.","pubmed_publication_date":"01 Mar 2014","pubmed_entrez_date":"2015-04-07","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-04-08 00:19:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17473877","title":"SIN-fully silent: HDAC complexes in fission yeast.","citation":"Nat Struct Mol Biol 2007 May;14(5):358-9","abstract":"","authors":"Roguev A, Krogan NJ","authors_abbrev":"Roguev A et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-05-03","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15173168","title":"Cds1 phosphorylation by Rad3-Rad26 kinase is mediated by forkhead-associated domain interaction with Mrc1.","citation":"J Biol Chem 2004 Jul 30;279(31):32079-86","abstract":"The protein kinase Cds1 is an effector of the replication checkpoint in the fission yeast Schizosaccharomyces pombe. Cds1 is required to stabilize stalled replication forks, and it helps to prevent the onset of mitosis until the genome is fully replicated. Mrc1 (mediator of the replication checkpoint-1) and Rad3-Rad26 kinase are required for Cds1 activation, but exactly how Mrc1 mediates Cds1 activation is unknown. Here we show that Mrc1 is required for the initial threonine 11 phosphorylation of Cds1 by Rad3-Rad26. Mrc1 specifically interacts with the forkhead-associated (FHA) domain of Cds1 in yeast two-hybrid assays. Mutations in the FHA domain that abolish this interaction also eliminate Thr-11 phosphorylation of Cds1. Weak Thr-11 phosphorylation of a \"kinase-dead\" mutant of Cds1 is rescued by co-expression of wild type Cds1. The requirement for Mrc1 in the replication checkpoint can be partially eliminated by expression of a Rad26-Cds1 fusion protein. These findings suggest that recognition of Mrc1 by the FHA domain of Cds1 serves to recruit Cds1 to Rad3-Rad26. This interaction mediates the initial Thr-11 phosphorylation of Cds1 by Rad3-Rad26 with subsequent intermolecular phosphorylation events leading to full activation of Cds1.","authors":"Tanaka K, Russell P","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"30 Jul 2004","pubmed_entrez_date":"2004-06-03","publication_year":"2004","canto_session_key":"9846a03793b7b22e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-04-11 13:39:41","canto_approved_date":"2025-09-04 11:59:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-11 13:39:32","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":33,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC9E9.08","SPAC694.06c","SPAPB2B4.03","SPCC18B5.11c","SPBC216.05"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-04-11"},{"uniquename":"PMID:10022828","title":"Evidence for F-actin-dependent and -independent mechanisms involved in assembly and stability of the medial actomyosin ring in fission yeast.","citation":"EMBO J 1999 Feb 15;18(4):854-62","abstract":"Cell division in a number of eukaryotes, including the fission yeast Schizosaccharomyces pombe, is achieved through a medially placed actomyosin-based contractile ring. Although several components of the actomyosin ring have been identified, the mechanisms regulating ring assembly are still not understood. Here, we show by biochemical and mutational studies that the S.pombe actomyosin ring component Cdc4p is a light chain associated with Myo2p, a myosin II heavy chain. Localization of Myo2p to the medial ring depended on Cdc4p function, whereas localization of Cdc4p at the division site was independent of Myo2p. Interestingly, the actin-binding and motor domains of Myo2p are not required for its accumulation at the division site although the motor activity of Myo2p is essential for assembly of a normal actomyosin ring. The initial assembly of Myo2p and Cdc4p at the division site requires a functional F-actin cytoskeleton. Once established, however, F-actin is not required for the maintenance of Cdc4p and Myo2p medial rings, suggesting that the attachment of Cdc4p and Myo2p to the division site involves proteins other than actin itself.","authors":"Naqvi NI, Eng K, Gould KL, Balasubramanian MK","authors_abbrev":"Naqvi NI et al.","pubmed_publication_date":"15 Feb 1999","pubmed_entrez_date":"1999-02-18","publication_year":"1999","canto_session_key":"6d218019d6c51a94","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-25 15:35:23","canto_approved_date":"2025-09-04 11:00:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-25 15:35:17","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAP8A3.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-01-25"},{"uniquename":"PMID:26658609","title":"The alternate AP-1 adaptor subunit Apm2 interacts with the Mil1 regulatory protein and confers differential cargo sorting.","citation":"Mol Biol Cell 2016 Feb 01;27(3):588-98","abstract":"Heterotetrameric adaptor protein complexes are important mediators of cargo protein sorting in clathrin-coated vesicles. The cell type-specific expression of alternate μ chains creates distinct forms of AP-1 with altered cargo sorting, but how these subunits confer differential function is unclear. Whereas some studies suggest the μ subunits specify localization to different cellular compartments, others find that the two forms of AP-1 are present in the same vesicle but recognize different cargo. Yeast have two forms of AP-1, which differ only in the μ chain. Here we show that the variant μ chain Apm2 confers distinct cargo-sorting functions. Loss of Apm2, but not of Apm1, increases cell surface levels of the v-SNARE Snc1. However, Apm2 is unable to replace Apm1 in sorting Chs3, which requires a dileucine motif recognized by the γ/σ subunits common to both complexes. Apm2 and Apm1 colocalize at Golgi/early endosomes, suggesting that they do not associate with distinct compartments. We identified a novel, conserved regulatory protein that is required for Apm2-dependent sorting events. Mil1 is a predicted lipase that binds Apm2 but not Apm1 and contributes to its membrane recruitment. Interactions with specific regulatory factors may provide a general mechanism to diversify the functional repertoire of clathrin adaptor complexes.","doi":"10.1091/mbc.E15-09-0621","authors":"Whitfield ST, Burston HE, Bean BD, Raghuram N, Maldonado-Báez L, Davey M, Wendland B, Conibear E","authors_abbrev":"Whitfield ST et al.","pubmed_publication_date":"01 Feb 2016","pubmed_entrez_date":"2015-12-15","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC607.08c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU006894","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF195027","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000084","title":"Representation of plant structural organization as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the structural organization of a plant structure as a biological process. The underlying equivalence axiom template is \"'anatomical structure arrangement' and 'results in structural organization of' some P\", where P is a plant anatomical entity (PO:0025131).","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29754461","title":"Computational modeling highlights the role of the disordered Formin Homology 1 domain in profilin-actin transfer.","citation":"FEBS Lett 2018 Jun;592(11):1804-1816","abstract":"Formins accelerate actin polymerization, assumed to occur through flexible Formin Homology 1 (FH1) domain-mediated transfer of profilin-actin to the barbed end. To study FH1 properties and address sequence effects, including varying length/distribution of profilin-binding proline-rich motifs, we performed all-atom simulations of a set of representative FH1 domains of formins: mouse mDia1 and mDia2, budding yeast Bni1 and Bnr1, and fission yeast Cdc12, For3, and Fus1. We find FH1 has flexible regions between high-propensity polyproline helix regions. A coarse-grained model retaining sequence specificity, assuming rigid polyproline segments, describes their size. Multiple bound profilins or profilin-actin complexes expand mDia1-FH1, which may be important in cells. Simulations of the barbed end bound to Bni1-FH1-FH2 dimer show that the leading FH1 can better transfer profilin or profilin-actin, with decreasing probability as the distance from FH2 increases.","doi":"10.1002/1873-3468.13088","authors":"Horan BG, Zerze GH, Kim YC, Vavylonis D, Mittal J","authors_abbrev":"Horan BG et al.","pubmed_publication_date":"Jun 2018","pubmed_entrez_date":"2018-05-14","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-05-15 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7262540","title":"Regulatory genes controlling mitosis in the fission yeast Schizosaccharomyces pombe.","citation":"Genetics 1980 Nov;96(3):627-37","abstract":"Fifty-two wee mutants that undergo mitosis and cell division at a reduced size compared with wild type have been genetically analyzed. The mutants define two genes, wee1 and cdc2, which control the timing of mitosis. Fifty-one of the mutants map at the wee1 locus, which is unlinked to any known cdc gene. One of the wee1 alleles has been shown to be nonsense suppressible. The 52nd were mutant maps within cdc2. Previously, only temperature-sensitive mutants that become blocked at mitosis have been found at the cdc2 locus. The simplest interpretation of these observations is that wee1+ codes for a negative element or inhibitor, and cdc2+ codes for a positive element or activator in the mitotic control. The gene dosage of wee1+ plays some role in determining the timing of mitosis, but the gene dosage of cdc2+ has little effect. However, some aspect of the cdc2 gene product activity is important for determining when mitosis takes place. The possible roles of wee1 and cdc2 in the mitotic control are discussed, with particular reference to the part they may play in the monitoring of cell growth rate, both of which influence the timing of mitosis.","authors":"Nurse P, Thuriaux P","authors_abbrev":"Nurse P et al.","pubmed_publication_date":"Nov 1980","pubmed_entrez_date":"1980-11-01","publication_year":"1980","canto_session_key":"91da8e4c4e7b6d48","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-01-12 16:04:34","canto_approved_date":"2026-01-19 10:18:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-27 15:15:51","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":30,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC11B10.09","SPATRNASER.03","SPCC1322.13"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-01-12"},{"uniquename":"PMID:6353183","title":"[Characteristics of the segregation of a new remote hybrid compared to an earlier remote hybrid obtained from crossing Saccharomyces cerevisiae with Schizosaccharomyces pombe].","citation":"Mikrobiologiia 1983;52(3):512-4","abstract":"The variability of two remote hybrids between Saccharomyces cerevisiae and Schizosaccharomyces pombe was compared in the course of their vegetative splitting. Hybrid 69 was obtained upon fusion of germinating spores, hybrid 92 was produced by copulation of vegetative cells. The variability of hybrid 92 was more diverse in terms of the size and shape of its cells; moreover, the hybrid yielded adenine-dependent haploid cells typical of S. cerevisiae with red colonies as well as dividing cells very similar to S. pombe with cross septa. Hybrid 69 did not produce such cultures.","authors":"Kosikov KV","authors_abbrev":"Kosikov KV","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-05-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19152795","title":"Damage recognition by UV damage endonuclease from Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2009 May 01;8(5):600-11","abstract":"UV damage endonuclease (UVDE) from Schizosaccharomyces pombe initiates repair of UV lesions and abasic sites by nicking the DNA 5' to the damaged site. In this paper we show that in addition UVDE incises DNA containing a single-strand nick or gap, but that the enzymatic activity on these substrates as well as on abasic sites strongly depends on the presence of a neighbouring pyrimidine residue. This indicates that, although UVDE may have been derived from an ancestral AP endonuclease its major substrate is a UV lesion and not an AP site. We propose that UVDE rotates two nucleotides into a pocket of the protein in order to bring the scissile bond close to the active site and that purine bases are excluded from this pocket. We also show that in the DNA complex residue Tyr-358 of UVDE penetrates the DNA helix causing unstacking of two residues opposite the lesion, thereby stabilizing the protein-DNA interaction, most likely by promoting bending of the DNA. In the absence of Tyr-358 the enzyme exhibits an increased catalytic activity on UV-induced lesions, but only at a lower pH of 6.5. At physiological conditions (pH 7.5) the mutant protein completely looses its catalytic activity although it can still bind to the DNA. We propose that in addition to stabilizing the bend in the DNA the hydrophobic side chain of Tyr-358 shields the active site from exposure to the solvent.","doi":"10.1016/j.dnarep.2008.12.004","authors":"Paspaleva K, Moolenaar GF, Goosen N","authors_abbrev":"Paspaleva K et al.","pubmed_publication_date":"01 May 2009","pubmed_entrez_date":"2009-01-21","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15911625","title":"Functional homology among human and fission yeast Cdc14 phosphatases.","citation":"J Biol Chem 2005 Aug 12;280(32):29144-50","abstract":"Budding and fission yeast Cdc14 homologues, a conserved family of serine-threonine phosphatases, play a role in the inactivation of mitotic cyclin-dependent kinases (CDKs) by molecularly distinct mechanisms. Saccharomyces cerevisiae Cdc14 protein phosphatase inactivates CDKs by promoting mitotic cyclin degradation and the accumulation of a CDK inhibitor to allow budding yeast cells to exit from mitosis. Schizosaccharomyces pombe Flp1 phosphatase down-regulates CDK/cyclin activity, controlling the degradation of the Cdc25 tyrosine phosphatase for fission yeast cells to undergo cytokinesis. In the present work, we show that human Cdc14 homologues (hCdc14A and hCdc14B) rescued flp1-deficient fission yeast strains, indicating functional homology. We also show that hCdc14A and B interacted in vivo with S. pombe Cdc25 and that hCdc14A dephosphorylated this mitotic inducer both in vitro and in vivo. Our results support a Cdc14 conserved inhibitory mechanism acting on S. pombe Cdc25 protein and suggest that human cells may regulate Cdc25 in a similar manner to inactivate Cdk1-mitotic cyclin complexes.","authors":"Vázquez-Novelle MD, Esteban V, Bueno A, Sacristán MP","authors_abbrev":"Vázquez-Novelle MD et al.","pubmed_publication_date":"12 Aug 2005","pubmed_entrez_date":"2005-05-25","publication_year":"2005","canto_session_key":"af6415e445f68d42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-23 18:15:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-23 18:15:47","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC24H6.05","SPAC1782.09c","SPBC582.03"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2015-01-23"},{"uniquename":"PMID:33812868","title":"Histone transcription regulator Slm9 is required for cytoophidium biogenesis.","citation":"Exp Cell Res 2021 Jun 01;403(1):112582","abstract":"The cytoophidium, a subcellular structure composed of CTP synthase, can be observed during the division of Schizosaccharomyces pombe. Cytoophidium formation changes periodically with the cell cycle of yeast cells. Here, we find that histone chaperone Slm9 is required for the integrity of cytoophidia in fission yeast. When the slm9 gene is knocked out, we observe that morphological characteristics, the abundance of cytoophidia and the division of the yeast cells are significantly affected. Fragmented cytoophidia occur in slm9 mutant cells, a phenomenon rarely observed in wild-type cells. Our study reveals a potential link between a chromosomal regulatory factor and cytoophidium biogenesis.","doi":"10.1016/j.yexcr.2021.112582","authors":"Feng HC, Andreadis C, Liu JL","authors_abbrev":"Feng HC et al.","pubmed_publication_date":"01 Jun 2021","pubmed_entrez_date":"2021-04-04","publication_year":"2021","canto_session_key":"bcd9e2d1858d75e5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-04-07 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC15D4.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37237082","title":"Fission yeast Srr1 and Skb1 promote isochromosome formation at the centromere.","citation":"Commun Biol 2023 May 26;6(1):551","abstract":"Rad51 maintains genome integrity, whereas Rad52 causes non-canonical homologous recombination leading to gross chromosomal rearrangements (GCRs). Here we find that fission yeast Srr1/Ber1 and Skb1/PRMT5 promote GCRs at centromeres. Genetic and physical analyses show that srr1 and skb1 mutations reduce isochromosome formation mediated by centromere inverted repeats. srr1 increases DNA damage sensitivity in rad51 cells but does not abolish checkpoint response, suggesting that Srr1 promotes Rad51-independent DNA repair. srr1 and rad52 additively, while skb1 and rad52 epistatically reduce GCRs. Unlike srr1 or rad52, skb1 does not increase damage sensitivity. Skb1 regulates cell morphology and cell cycle with Slf1 and Pom1, respectively, but neither Slf1 nor Pom1 causes GCRs. Mutating conserved residues in the arginine methyltransferase domain of Skb1 greatly reduces GCRs. These results suggest that, through arginine methylation, Skb1 forms aberrant DNA structures leading to Rad52-dependent GCRs. This study has uncovered roles for Srr1 and Skb1 in GCRs at centromeres.","doi":"10.1038/s42003-023-04925-9","authors":"Mongia P, Toyofuku N, Pan Z, Xu R, Kinoshita Y, Oki K, Takahashi H, Ogura Y, Hayashi T, Nakagawa T","authors_abbrev":"Mongia P et al.","pubmed_publication_date":"26 May 2023","pubmed_entrez_date":"2023-05-26","publication_year":"2023","canto_session_key":"83235993b938b667","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takuro Nakagawa","canto_first_approved_date":"2023-06-19 13:06:34","canto_approved_date":"2025-08-20 12:29:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-10 05:43:32","canto_added_date":"2023-05-28 00:15:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Takuro Nakagawa","community_curator":true,"annotation_count":34,"orcid":"0000-0003-3455-8224","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPBC16H5.11c","SPAC30D11.10","SPBC14C8.13","SPAC821.03c","SPAC2F7.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2023-06-19"},{"uniquename":"PMID:9684351","title":"The ultrastructure of yeast: cell wall structure and formation.","citation":"Micron 1998;29(2-3):207-33","abstract":"Yeasts are unicellular eukaryotes, and are used widely as a model system in basic and applied fields of life science, medicine, and biotechnology. The ultrastructure of yeast cells was first studied in 1957 and the techniques used have advanced greatly in the 40 years since then; an overview of these methods is first presented in this review. The ultrastructure of budding and dimorphic yeast cells observed with a scanning electron microscope (SEM) and a transmission electron microscope (TEM) after thin sectioning and freeze-etching are then described, followed by discussion of the regeneration of the cell wall of Candida albicans protoplasts detected by cryosectioning. C. albicans protoplasts are regenerated to synthesize microfibrils on their surface. They are aggregated into thicker bundles which are intermeshed, forming a wide-meshed network of long fibrils. These microfibrillar structures are chains of beta-1,3-glucan which are broken down after treatment with beta-1,3-glucanase. Morphologically identical microfibrils are synthesized in vitro by a cell-free system in which the active cell membrane fraction as a source of beta-1,3-glucan synthetase and UDP glucose as the sole substrate are used. The diameter of an elemental fibril of beta-glucan is estimated to be 2.8 nm from the pattern of autocorrelation of the image obtained by computer processing. In contrast, in the presence of aculeacin A the formation of normal fibrillar nets or bundles is significantly inhibited, resulting in the occurrence of short fibrils. These electron microscopic data suggest that aculeacin A inhibits not only the synthesis of beta-1,3-glucan but the aggregation of microfibrils of this polysaccharide, allowing formation of the crystalline structure. On the basis of the cumulative data obtained from the electron microscopic studies, we are led to the assumption that de novo synthesized beta-glucan chains might initially form fine particles which are then transformed into thin fibrils with single to multiple strands which appear to be oriented parallel to each other so that they develop into fibrillar structures. This process of assembly of beta-glucan molecules leads to the development of a fibrous network within the regenerating Candida cell wall. Third, the mechanism of cell wall formation is shown by low-voltage (LV) SEM and TEM, using various techniques and computer graphics, of the regeneration system of Schizosaccharomyces pombe protoplasts: after 10 min of regeneration, the protoplasts begin to grow fibrillar substances of a beta-glucan nature, and a fibrillar network covers the surface of all protoplasts. The network is originally formed as fine particles on the protoplast surface and these are subsequently lengthened to microfibrils 2 nm thick. The microfibrils twist around each other and develop into 8 nm thick fibrils forming flat bundles 16 nm thick. Interfibrillar spaces are gradually filled with amorphous particles of an alpha-galactomannan nature and, finally, the complete cell wall is formed after 12 h. Treatment of reverting protoplasts with RuO4 provided clear TEM images of glucan fibrils with high electron density. The relationship between cell wall regeneration and intracellular organelles was examined by using serial thin sections stained with PATAg and computer-aided three-dimensional reconstruction. The secretory vesicles in a protoplast had increased markedly by 1.4, 3.4, and 5.8 times at 1.5, 3.0, and 5 h, respectively. Three-dimensional analysis indicates that Golgi apparatuses are located close together in the nucleus of the protoplast and are dispersed into the cytoplasm during the progress of cell wall formation.","authors":"Osumi M","authors_abbrev":"Osumi M","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-07-31","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16080597","title":"[The dds20+ gene controls a novel Rad51Sp-dependent pathway of recombinational repair in Schizosaccharomyces pombe].","citation":"Genetika 2005 Jun;41(6):736-45","abstract":"Repair of DNA double-strand break (DSB) is an evolutionary conserved Rad51-mediated mechanism. In yeasts, Rad51 paralogs, Saccharomyces cerevisiae Rad55-Rad57 and Schizosaccharomyces pombe Rhp55-Rhp57 are mediators of the nucleoprotein RadS1 filament formation. As shown in this work, a novel RAD51Sp-dependent pathway of DSB repair acts in S. pombe parallel to the pathway mediated by Rad51 paralogs. A new gene dds20+ that controls this pathway was identified. The overexpression of dds20+ partially suppresses defects of mutant rhp55delta in DNA repair. Cells of dds20delta manifest hypersensitivity to a variety of genotoxins. Epistatic analysis revealed that dds20+ is a gene of the recombinational repair group. The role of Dds20 in repair of spontaneous damages occurring in the process of replication and mating-type switching remains unclear. The results obtained suggest that Dds20 has functions beyond the mitotic S phase. The Dds20 protein physically interacts with Rhp51 (Rad51Sp). Dds20 is assumed to operate at early recombinational stages and to play a specific role in the Rad51 protein filament assembly differing from that of Rad51 paralogs.","authors":"Salakhova AF, Savchenko GV, Khasanov FK, Chepurnaia OV, Korolev VG, Bashkirov VI","authors_abbrev":"Salakhova AF et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-08-06","publication_year":"2005","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.03c","SPAC644.14c","SPBC28F2.07"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:27151298","title":"Orderly progression through S-phase requires dynamic ubiquitylation and deubiquitylation of PCNA.","citation":"Sci Rep 2016 May 06;6:25513","abstract":"Proliferating-cell nuclear antigen (PCNA) is a DNA sliding clamp with an essential function in DNA replication and a key role in tolerance to DNA damage by ensuring the bypass of lesions. In eukaryotes, DNA damage tolerance is regulated by ubiquitylation of lysine 164 of PCNA through a well-known control mechanism; however, the regulation of PCNA deubiquitylation remains poorly understood. Our work is a systematic and functional study on PCNA deubiquitylating enzymes (DUBs) in Schizosaccharomyces pombe. Our study reveals that the deubiquitylation of PCNA in fission yeast cells is a complex process that requires several ubiquitin proteases dedicated to the deubiquitylation of a specific subnuclear fraction of mono- and di-ubiquitylated PCNA or a particular type of poly-ubiquitylated PCNA and that there is little redundancy among these enzymes. To understand how DUB activity regulates the oscillatory pattern of ubiquitylated PCNA in fission yeast, we assembled multiple DUB mutants and found that a quadruple mutation of ubp2(+), ubp12(+), ubp15(+), and ubp16(+) leads to the stable accumulation of mono-, di-, and poly-ubiquitylated forms of PCNA, increases S-phase duration, and sensitizes cells to DNA damage. Our data suggest that the dynamic ubiquitylation and deubiquitylation of PCNA occurs during S-phase to ensure processive DNA replication.","doi":"10.1038/srep25513","authors":"Álvarez V, Viñas L, Gallego-Sánchez A, Andrés S, Sacristán MP, Bueno A","authors_abbrev":"Álvarez V et al.","pubmed_publication_date":"06 May 2016","pubmed_entrez_date":"2016-05-07","publication_year":"2016","canto_session_key":"d91d901cb0a83596","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Vanesa Álvarez","canto_first_approved_date":"2018-03-24 18:27:30","canto_approved_date":"2023-12-30 10:43:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-15 17:45:07","canto_added_date":"2016-05-08 00:15:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":100,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Vanesa Álvarez","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC328.06","SPBC1734.06","SPAC13G6.01c","SPBC713.02c","SPCC1682.12c","SPAC11E3.04c","SPBC16D10.09","SPCC1494.05c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-03-24"},{"uniquename":"PMID:10491317","title":"Deletion of the sep1(+) forkhead transcription factor homologue is not lethal but causes hyphal growth in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 1999 Sep 24;263(2):465-74","abstract":"sep1(+), the Schizosaccharomyces pombe homologue of the forkhead/HNF-3 transcription factors, plays a role in the cell separation at the end of mitosis. Its inactivation by interruption of the coding region is not lethal but renders the sister cells unable to separate and causes hyphal growth. The persistence of unsplit septa indirectly interferes with the establishment of new cell polarity by preventing cell growth at cell tips. Temporal changes in the transcription of sep1(+) correlate with the cell cycle progression showing maximal expression at the peak of cell plate index in synchronized cultures. The constitutive overexpression of sep1(+) has no discernible effect on the morphology and physiology of the cells.","authors":"Ribár B, Grallert A, Oláh E, Szállási Z","authors_abbrev":"Ribár B et al.","pubmed_publication_date":"24 Sep 1999","pubmed_entrez_date":"1999-09-24","publication_year":"1999","canto_session_key":"1a18e5aaed41d660","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-09-07 17:07:04","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-02 08:29:00","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.05c","SPCC1223.06","SPBC4C3.12","SPAC5D6.05","SPBC16G5.15c"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2014-07-02"},{"uniquename":"PMID:42136729","title":"Cmp7-dependent recruitment of Alx1 to a mitotic nuclear envelope hole in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2026;2026","abstract":" The nuclear envelope maintains nucleocytoplasmic compartmentalization. Divergent strategies exist to accommodate the nuclear envelope during mitotic chromatin segregation. While the endosomal sorting complexes required for transport (ESCRT) machinery drives nuclear envelope remodeling during this process, recent work in  Schizosaccharomyces japonicus  suggests an ESCRT-independent pathway promoting nucleocytoplasmic compartmentalization mediated by Alx1 . We investigate if this ESCRT-independent pathway is conserved in  Schizosaccharomyces pombe.  We find Alx1-GFP is recruited to a mitotic nuclear envelope hole in  S. pombe  , but that recruitment depends on the ESCRT machinery. Our data suggest diverse strategies of mitotic nuclear envelope remodeling necessitate varying strategies of promoting nucleocytoplasmic compartmentalization.","doi":"10.17912/micropub.biology.002122","authors":"Genereux KD, Walker ON, Benders SO, Le TT, Ader NR","authors_abbrev":"Genereux KD et al.","pubmed_publication_date":"2026","pubmed_entrez_date":"2026-05-15","publication_year":"2026","canto_session_key":"137811198721bd9f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juni Zugish","canto_first_approved_date":"2026-06-13 19:54:46","canto_approved_date":"2026-06-13 19:54:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-06-02 15:31:04","canto_added_date":"2026-05-15 23:25:04","annotation_curators":[{"name":"Juni Zugish","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.18c","SPAC2G11.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2026-06-13"},{"uniquename":"PMID:10825192","title":"Mechanism of caffeine-induced checkpoint override in fission yeast.","citation":"Mol Cell Biol 2000 Jun;20(12):4288-94","abstract":"Mitotic checkpoints restrain the onset of mitosis (M) when DNA is incompletely replicated or damaged. These checkpoints are conserved between the fission yeast Schizosaccharomyces pombe and mammals. In both types of organisms, the methylxanthine caffeine overrides the synthesis (S)-M checkpoint that couples mitosis to completion of DNA S phase. The molecular target of caffeine was sought in fission yeast. Caffeine prevented activation of Cds1 and phosphorylation of Chk1, two protein kinases that enforce the S-M checkpoint triggered by hydroxyurea. Caffeine did not inhibit these kinases in vitro but did inhibit Rad3, a kinase that regulates Cds1 and Chk1. In accordance with this finding, caffeine also overrode the G(2)-M DNA damage checkpoint that requires Rad3 function. Rad3 coprecipitated with Cds1 expressed at endogenous amounts, a finding that supports the hypothesis that Rad3 is involved in direct activation of Cds1.","authors":"Moser BA, Brondello JM, Baber-Furnari B, Russell P","authors_abbrev":"Moser BA et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-05-29","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05","SPCC1259.13","SPCC18B5.11c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23832177","title":"Histone deacetylases govern heterochromatin in every phase.","citation":"EMBO J 2013 Aug 28;32(17):2301-3","abstract":"EMBO J 32 17, 2321–2325 doi:; DOI: 10.1038/emboj.2013.143; published online June 14 2013 Deacetylation of histone tails has been shown to play a role during heterochromatin formation, but the precise mechanism of action has not been understood. Complementary results presented in two recent articles in  The EMBO Journal  (Alper et al, 2013; Buscaino et al, 2013) together reveal how histone deacetylases (HDACs) affect the various phases of heterochromatin formation: establishment, maintenance and spreading.","doi":"10.1038/emboj.2013.154","authors":"Murakami Y","authors_abbrev":"Murakami Y","pubmed_publication_date":"28 Aug 2013","pubmed_entrez_date":"2013-07-09","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11689699","title":"Site-specific DNA binding of the Schizosaccharomyces pombe origin recognition complex is determined by the Orc4 subunit.","citation":"Mol Cell Biol 2001 Dec;21(23):8095-103","abstract":"The mechanism by which origin recognition complexes (ORCs) identify replication origins was investigated using purified Orc proteins from Schizosaccharomyces pombe. Orc4p alone bound tightly and specifically to several sites within S. pombe replication origins that are genetically required for origin activity. These sites consisted of clusters of A or T residues on one strand but were devoid of either alternating A and T residues or GC-rich sequences. Addition of a complex consisting of Orc1, -2, -3, -5, and -6 proteins (ORC-5) altered neither Orc4p binding to origin DNA nor Orc4p protection of specific sequences. ORC-5 alone bound weakly and nonspecifically to DNA; strong binding required the presence of Orc4p. Under these conditions, all six subunits remained bound to chromatin isolated from each phase of the cell division cycle. These results reveal that the S. pombe ORC binds to multiple, specific sites within replication origins and that site selection, at least in vitro, is determined solely by the Orc4p subunit.","authors":"Kong D, DePamphilis ML","authors_abbrev":"Kong D et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-11-02","publication_year":"2001","canto_session_key":"2620118452a4fb4c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-07-06 12:34:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-12-20 17:06:25","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.13","SPBC2A9.12","SPBC646.14c","SPBC685.09","SPBC29A10.15","SPAC3H1.01c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2013-12-20"},{"uniquename":"PMID:38376141","title":"Disordered regions and folded modules in CAF-1 promote histone deposition in  Schizosaccharomyces pombe .","citation":"Elife 2024 Feb 20;12","abstract":"Genome and epigenome integrity in eukaryotes depends on the proper coupling of histone deposition with DNA synthesis. This process relies on the evolutionary conserved histone chaperone CAF-1 for which the links between structure and functions are still a puzzle. While studies of the  Saccharomyces cerevisiae  CAF-1 complex enabled to propose a model for the histone deposition mechanism, we still lack a framework to demonstrate its generality and in particular, how its interaction with the polymerase accessory factor PCNA is operating. Here, we reconstituted a complete  Sp CAF-1 from fission yeast. We characterized its dynamic structure using NMR, SAXS and molecular modeling together with in vitro and in vivo functional studies on rationally designed interaction mutants. Importantly, we identify the unfolded nature of the acidic domain which folds up when binding to histones. We also show how the long KER helix mediates DNA binding and stimulates  Sp CAF-1 association with PCNA. Our study highlights how the organization of CAF-1 comprising both disordered regions and folded modules enables the dynamics of multiple interactions to promote synthesis-coupled histone deposition essential for its DNA replication, heterochromatin maintenance, and genome stability functions.","doi":"10.7554/eLife.91461","authors":"Ouasti F, Audin M, Fréon K, Quivy JP, Tachekort M, Cesard E, Thureau A, Ropars V, Fernández Varela P, Moal G, Soumana-Amadou I, Uryga A, Legrand P, Andreani J, Guerois R, Almouzni G, Lambert S, Ochsenbein F","authors_abbrev":"Ouasti F et al.","pubmed_publication_date":"20 Feb 2024","pubmed_entrez_date":"2024-02-20","publication_year":"2024","canto_session_key":"da7b4175a523a7e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Lambert","canto_first_approved_date":"2024-08-02 09:37:37","canto_approved_date":"2026-06-26 08:33:55","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-10 10:28:45","canto_added_date":"2024-02-21 00:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":11,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Sarah Lambert","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.11c","SPBC8D2.03c","SPBC16D10.09","SPBC31F10.13c","SPAC1834.03c","SPBC29A10.03c","SPBC8D2.04","SPAC1834.04","SPAC26H5.03","SPAC25H1.06","SPBC1105.12"],"gene_count":11,"ltp_gene_count":4,"approved_date":"2024-08-02"},{"uniquename":"PMID:10931354","title":"A temperature-sensitive Krp1 allows in vivo characterization of kexin activation.","citation":"Mol Microbiol 2000 Aug;37(3):606-18","abstract":"Members of the kexin family of processing enzymes are responsible for the cleavage of many proproteins during their transport through the secretory pathway. The enzymes are themselves made as inactive precursors and we have investigated the activation of Krp1, a kexin from the fission yeast Schizosaccharomyces pombe. As Krp1 is essential for cell growth, we have used a krp1ts strain to investigate the role of the prosequence in the activation process. Mutations that reduce either the efficiency with which the prosequence is released or the rate at which the released prosegment is subsequently cleaved at an internal site are less active when assayed in vivo. We also show that prosegments lacking an internal dibasic motif can act as autoinhibitors and prevent activation of the catalytic fragment. Krp1 constructs containing prosequences based on these inhibitors do not become active in vitro. Surprisingly, the same constructs do become active in the intact cell and appear to suggest that alternative activation processes can be used by these enzymes.","authors":"Ladds G, Davis K, Powner D, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2000-08-10","publication_year":"2000","canto_session_key":"eb07f91aa716d2b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-08-05 14:08:22","canto_approved_date":"2025-06-17 07:13:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-27 07:40:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-08-05"},{"uniquename":"PMID:28733393","title":"Microscopic Observation of Living Cells Stained with Fluorescent Probes.","citation":"Cold Spring Harb Protoc 2017 Oct 03;2017(10):pdb.prot079848","abstract":"Fluorescence imaging of living cells provides a unique opportunity to follow dynamic behavior of specific molecules under physiological conditions. In the fission yeast  Schizosaccharomyces pombe , expression of a target protein genetically fused with a fluorescent protein such as the jellyfish green fluorescent protein (GFP) is widely used. In addition, fluorescent chemical reagents are also used to stain specific molecules (e.g., Hoechst 33324 to stain DNA). Specimens of  S. pombe  cells for live cell imaging are prepared by either of two methods: sandwiching the cells between glass coverslips and by mounting the cells on a glass-bottom culture dish. For time-lapse observation, it is necessary to immobilize fission yeast cells on the glass surface of the glass-bottom dish because they are nonadherent and tend to move easily as a result of stage movement, convection flow of culture medium, and the contact and pushing of neighboring cells during cell growth. Either concanavalin A or soybean lectin, which bind to  S. pombe  cell walls, can be used for immobilization. Considerations for sample preparations and observation conditions are described.","doi":"10.1101/pdb.prot079848","authors":"Asakawa H, Ding DQ, Haraguchi T, Hiraoka Y","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"03 Oct 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10716938","title":"Fission yeast switches mating type by a replication-recombination coupled process.","citation":"EMBO J 2000 Mar 15;19(6):1389-96","abstract":"Fission yeast exhibits a homothallic life cycle, in which the mating type of the cell mitotically alternates in a highly regulated fashion. Pedigree analysis of dividing cells has shown that only one of the two sister cells switches mating type. It was shown recently that a site- and strand-specific DNA modification at the mat1 locus precedes mating-type switching. By tracking the fate of mat1 DNA throughout the cell cycle with a PCR assay, we identified a novel DNA intermediate of mating-type switching in S-phase. The time and rate of appearance and disappearance of this DNA intermediate are consistent with a model in which mating-type switching occurs through a replication-recombination coupled pathway. Such a process provides experimental evidence in support of a copy choice recombination model in Schizosaccharomyces pombe mating-type switching and is reminiscent of the sister chromatid recombination used to complete replication in the presence of certain types of DNA damage.","authors":"Arcangioli B, de Lahondès R","authors_abbrev":"Arcangioli B et al.","pubmed_publication_date":"15 Mar 2000","pubmed_entrez_date":"2000-03-16","publication_year":"2000","canto_session_key":"e9134c235c0d1bad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-06-07 16:22:45","canto_approved_date":"2023-03-15 17:37:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-07 16:21:46","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8F11.03","SPBC4F6.15c","SPAC3H5.06c","SPBC216.06c","SPBC409.03","SPAC1142.03c","SPAC664.01c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-06-07"},{"uniquename":"PMID:28586299","title":"Inter-Fork Strand Annealing causes genomic deletions during the termination of DNA replication.","citation":"Elife 2017 Jun 06;6","abstract":"Problems that arise during DNA replication can drive genomic alterations that are instrumental in the development of cancers and many human genetic disorders. Replication fork barriers are a commonly encountered problem, which can cause fork collapse and act as hotspots for replication termination. Collapsed forks can be rescued by homologous recombination, which restarts replication. However, replication restart is relatively slow and, therefore, replication termination may frequently occur by an active fork converging on a collapsed fork. We find that this type of non-canonical fork convergence in fission yeast is prone to trigger deletions between repetitive DNA sequences via a mechanism we call Inter-Fork Strand Annealing (IFSA) that depends on the recombination proteins Rad52, Exo1 and Mus81, and is countered by the FANCM-related DNA helicase Fml1. Based on our findings, we propose that IFSA is a potential threat to genomic stability in eukaryotes.","doi":"10.7554/eLife.25490","authors":"Morrow CA, Nguyen MO, Fower A, Wong IN, Osman F, Bryer C, Whitby MC","authors_abbrev":"Morrow CA et al.","pubmed_publication_date":"06 Jun 2017","pubmed_entrez_date":"2017-06-07","publication_year":"2017","canto_session_key":"f988eca9cbf13b9a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Matthew Whitby","canto_first_approved_date":"2019-06-06 14:13:09","canto_approved_date":"2019-06-12 10:11:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-06-04 07:59:01","canto_added_date":"2017-06-08 00:15:19","annotation_curators":[{"name":"Matthew Whitby","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9.05","SPAC30D11.10","SPCC4G3.05c","SPAC644.14c","SPBC29A10.05"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-06-06"},{"uniquename":"PMID:22307589","title":"Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach.","citation":"Proc Natl Acad Sci U S A 2012 Jan 31;109(5):1380-7","abstract":"The 26S proteasome is at the executive end of the ubiquitin-proteasome pathway for the controlled degradation of intracellular proteins. While the structure of its 20S core particle (CP) has been determined by X-ray crystallography, the structure of the 19S regulatory particle (RP), which recruits substrates, unfolds them, and translocates them to the CP for degradation, has remained elusive. Here, we describe the molecular architecture of the 26S holocomplex determined by an integrative approach based on data from cryoelectron microscopy, X-ray crystallography, residue-specific chemical cross-linking, and several proteomics techniques. The \"lid\" of the RP (consisting of Rpn3/5/6/7/8/9/11/12) is organized in a modular fashion. Rpn3/5/6/7/9/12 form a horseshoe-shaped heterohexamer, which connects to the CP and roofs the AAA-ATPase module, positioning the Rpn8/Rpn11 heterodimer close to its mouth. Rpn2 is rigid, supporting the lid, while Rpn1 is conformationally variable, positioned at the periphery of the ATPase ring. The ubiquitin receptors Rpn10 and Rpn13 are located in the distal part of the RP, indicating that they were recruited to the complex late in its evolution. The modular structure of the 26S proteasome provides insights into the sequence of events prior to the degradation of ubiquitylated substrates.","doi":"10.1073/pnas.1120559109","authors":"Lasker K, Förster F, Bohn S, Walzthoeni T, Villa E, Unverdorben P, Beck F, Aebersold R, Sali A, Baumeister W","authors_abbrev":"Lasker K et al.","pubmed_publication_date":"31 Jan 2012","pubmed_entrez_date":"2012-02-07","publication_year":"2012","canto_session_key":"c06b67e8d6ba5598","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-30 12:34:35","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-30 12:34:29","canto_added_date":"2016-09-21 00:19:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC106.16","SPBC646.16","SPCC1795.04c","SPBC582.07c","SPCC1442.06","SPBC119.01","SPCC576.10c","SPAC23G3.11","SPAC31G5.13","SPAC3A11.12c","SPBC4.07c","SPAC13C5.01c","SPCC1682.16","SPBC17D11.07c","SPAC6G10.04c","SPAC637.10c","SPBC16C6.07c","SPBC23G7.12c"],"gene_count":18,"ltp_gene_count":18,"approved_date":"2016-09-30"},{"uniquename":"PMID:11821054","title":"A DMSO-sensitive conditional mutant of the fission yeast orthologue of the Saccharomyces cerevisiae SEC13 gene is defective in septation.","citation":"FEBS Lett 2002 Jan 30;511(1-3):85-9","abstract":"Dissection of complex processes using model organisms such as yeasts relies heavily upon the use of conditional mutants. We have generated a collection of fission yeast mutants sensitive to dimethylsulphoxide (DMSO). Among these we have found a mutant in the Schizosaccharomyces pombe orthologue of the Saccharomyces cerevisiae SEC13 gene, which fails to cleave the division septum. Generation of a null allele demonstrates that the S. pombe sec13 gene is essential.","authors":"Poloni D, Simanis V","authors_abbrev":"Poloni D et al.","pubmed_publication_date":"30 Jan 2002","pubmed_entrez_date":"2002-02-01","publication_year":"2002","canto_session_key":"64694dedd55e6de2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-05-29 12:54:41","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-29 12:54:34","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.05c","SPBC215.15"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-05-29"},{"uniquename":"PMID:17724118","title":"Three-dimensional arrangement of F-actin in the contractile ring of fission yeast.","citation":"J Cell Biol 2007 Aug 27;178(5):765-71","abstract":"The contractile ring, which is required for cytokinesis in animal and yeast cells, consists mainly of actin filaments. Here, we investigate the directionality of the filaments in fission yeast using myosin S1 decoration and electron microscopy. The contractile ring is composed of around 1,000 to 2,000 filaments each around 0.6 mum in length. During the early stages of cytokinesis, the ring consists of two semicircular populations of parallel filaments of opposite directionality. At later stages, before contraction, the ring filaments show mixed directionality. We consider that the ring is initially assembled from a single site in the division plane and that filaments subsequently rearrange before contraction initiates.","authors":"Kamasaki T, Osumi M, Mabuchi I","authors_abbrev":"Kamasaki T et al.","pubmed_publication_date":"27 Aug 2007","pubmed_entrez_date":"2007-08-29","publication_year":"2007","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8536311","title":"Schizosaccharomyces pombe pac2+ controls the onset of sexual development via a pathway independent of the cAMP cascade.","citation":"Curr Genet 1995 Jun;28(1):32-8","abstract":"The Schizosaccharomyces pombe pac2 gene encodes a protein of 235 amino acids not similar to any protein of known function. Cells over-expressing pac2 were poor in mating and sporulation. Expression of ste11, which encodes a key transcription factor for sexual development, was not inducible by nitrogen starvation in these cells. Cells defective in pac2 could express ste11 and enter sexual development under incomplete starvation conditions. Although expression of ste11 is regulated primarily by the cAMP cascade, genetic analysis indicated that this cascade and pac2 can partially compensate for each other in the regulation of sexual development, and that neither of them is epistatic over the other. Thus, Pac2 appears to control ste11 expression via a signaling pathway independent of the cAMP cascade.","authors":"Kunitomo H, Sugimoto A, Wilkinson CR, Yamamoto M","authors_abbrev":"Kunitomo H et al.","pubmed_publication_date":"Jun 1995","pubmed_entrez_date":"1995-06-01","publication_year":"1995","canto_session_key":"e25a10ee7a1d5416","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-09-25 12:30:22","canto_approved_date":"2019-06-14 08:53:27","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-25 12:30:14","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPBC32C12.02","SPCC285.09c","SPBC106.10","SPAC31G5.11"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-09-25"},{"uniquename":"EMBL:AU011358","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2402440","title":"Nuclear pre-mRNA introns: analysis and comparison of intron sequences from Tetrahymena thermophila and other eukaryotes.","citation":"Nucleic Acids Res 1990 Sep 11;18(17):5133-41","abstract":"We have sequenced 14 introns from the ciliate Tetrahymena thermophila and include these in an analysis of the 27 intron sequences available from seven T. thermophila protein-encoding genes. Consensus 5' and 3' splice junctions were determined and found to resemble the junctions of other nuclear pre-mRNA introns. Unique features are noted and discussed. Overall the introns have a mean A + T content of 85% (21% higher than neighbouring exons) with smaller introns tending towards a higher A + T content. Approximately half of the introns are less than 100 bp. Introns from other organisms (approximately 30 of each) were also examined. The introns of Dictyostelium discoideum, Caenorhabditis elegans and Drosophila melanogaster, like those of T. thermophila, have a much higher mean A + T content than their neighbouring exons (greater than 20%). Introns from plants, Neurospora crassa and Schizosaccharomyces pombe also have a significantly higher A + T content (10%-20%). Since a high A + T content is required for intron splicing in plants (58), the elevated A + T content in the introns of these other organisms may also be functionally significant. The introns of yeast (Saccharomyces cerevisiae) and mammals (humans) appear to lack this trait and thus in some aspects may be atypical. The polypyrimidine tract, so distinctive of vertebrate introns, is not a trait of the introns in the non-vertebrate organisms examined in this study.","authors":"Csank C, Taylor FM, Martindale DW","authors_abbrev":"Csank C et al.","pubmed_publication_date":"11 Sep 1990","pubmed_entrez_date":"1990-09-11","publication_year":"1990","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42150082","title":"Regulation of Pfh1 helicase activity by nucleic acid interactions and mitochondrial SSB.","citation":"Proc Natl Acad Sci U S A 2026 May 26;123(21):e2602528123","abstract":"Pif1-family helicases are essential for proper nuclear and mitochondrial genome maintenance, yet the regulation of their activities remains incompletely understood. Here, we use single-molecule manipulation and visualization techniques to dissect the real-time mechanochemical behavior of Pfh1, the sole Pif1-family helicase in  Schizosaccharomyces pombe.  We systematically varied force, ATP concentration, fork composition, and the single-stranded DNA-binding protein spRim1, to quantify the unwinding and single-stranded DNA translocation properties of Pfh1. We find that Pfh1 operates through unwinding-rewinding cycles during which coordinated interactions with both DNA strands at the fork optimize ATP utilization. Contacts with the translocating strand modulate ATP affinity, while interactions with the displaced strand control maximum unwinding velocity. Binding of spRim1 to the displaced strand disrupts the latter interactions, increasing the unwinding velocity. Stable interactions of the helicase with both strands at the fork may limit unwinding processivity to ~20 bp, eventually triggering transition to rewinding. Rewinding proceeds through an ATP-dependent process that is incompatible with strand switching, in which ATP turnover modulates DNA contacts and rewinding rate. Binding of spRim1 to the displaced strand further accelerates rewinding, possibly by competing with helicase-DNA interactions, and facilitates recovery of the active unwinding conformation once the fork has rewound. Together, these findings suggest that Pfh1 balances unwinding and rewinding through coordinated ATP-dependent strand interactions, providing insight into how Pif1-family helicases are controlled at replication forks.","doi":"10.1073/pnas.2602528123","authors":"Ortiz-Rodríguez M, Singh SP, Cao-García FJ, Galletto R, Ibarra B","authors_abbrev":"Ortiz-Rodríguez M et al.","pubmed_publication_date":"26 May 2026","pubmed_entrez_date":"2026-05-18","publication_year":"2026","canto_session_key":"392e3f3c3432b077","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-05-18 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1538696","title":"Molecular cloning and sequence analysis of cdc27+ required for the G2-M transition in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1992 Feb;231(3):401-10","abstract":"The cell division cycle gene cdc27+ of the fission yeast Schizosaccharomyces pombe is required for the transition from G2 into mitosis. Genetic and physiological experiments suggest a close relationship between cdc27+ and the cdc2+ gene, a key regulator of mitosis in yeast and also in higher eukaryotic cells. We isolated the cdc27+ gene by complementation of a temperature-sensitive cdc27 mutant. The DNA sequence of this gene predicts a 1116 nucleotide open reading frame split by five short introns, ranging in size from 49 to 74 nucleotides. Analysis of cDNA clones confirmed the structure of the gene. The deduced cdc27+ gene product consists of 372 amino acids with a predicted Mr of 43 kDa. No homology of the predicted protein with known proteins could be found, thus the cdc27+ gene encodes a novel function required for the G2-M transition. Northern analysis revealed two mRNAs of 1.4 and 2.2 kb transcribed from this gene, the smaller transcript being approximately tenfold more abundant than the larger. The level of cdc27+ mRNAs remained constant through the cell cycle indicating that the time of action of the cdc27+ gene, which is known to be regulated by elements of the mitotic control, is not determined by periodic accumulation of its transcripts.","authors":"Hughes DA, MacNeill SA, Fantes PA","authors_abbrev":"Hughes DA et al.","pubmed_publication_date":"Feb 1992","pubmed_entrez_date":"1992-02-01","publication_year":"1992","canto_session_key":"ed3d63f2a1ec6250","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-20 16:46:40","canto_approved_date":"2021-01-22 14:51:53","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-04-25 14:44:15","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-20"},{"uniquename":"PMID:8119981","title":"Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression.","citation":"J Biol Chem 1994 Mar 04;269(9):6320-4","abstract":"The molecular action of leptomycin B (LMB), an agent inducing arrest of the eukaryotic cell cycle at G1 and G2 phases, was investigated by analyzing an LMB resistance gene of Schizosaccharomyces pombe. A genomic library of an LMB-resistant mutant was screened for LMB resistance, and a DNA fragment containing an open reading frame (ORF) of 1078 amino acids was cloned on a multicopy vector. The plasmid was found to confer drug resistance specifically to LMB. Nucleotide sequencing revealed that the ORF was a mutant gene for the essential nuclear protein crm1, which had been reported to complement a cold-sensitive mutation causing deformed nuclear morphology. The gene product named crm1-N1 had two amino acid replacements (Gly-503 to Asp and Met-546 to Ile). Two allelic mutants of crm1 (crm1-809 and crm1-119) were found to be hypersensitive and resistant, respectively, to LMB. Nuclear morphology of the cold-sensitive crm1-809 mutant at the restrictive temperature was almost the same as that of the wild-type cells treated with LMB. Furthermore, a low concentration of LMB induced the intracellular accumulation of a 25-kDa protein in the wild-type cells, which was immunologically identical to the protein accumulating in the crm1-809 mutant cells. These results strongly suggest that LMB primarily inhibits the function of the crm1 gene which is required for maintaining higher order chromosome structures, correct gene expression, and cell growth in the fission yeast.","authors":"Nishi K, Yoshida M, Fujiwara D, Nishikawa M, Horinouchi S, Beppu T","authors_abbrev":"Nishi K et al.","pubmed_publication_date":"04 Mar 1994","pubmed_entrez_date":"1994-03-04","publication_year":"1994","canto_session_key":"f907219df93ff77f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-12 06:09:41","canto_approved_date":"2020-06-19 13:08:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-22 06:48:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.14c","SPAC1805.17","SPCC663.03"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2014-08-12"},{"uniquename":"EMBL:AU010285","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008495","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38616173","title":"Low-Molecular Weight Compounds that Extend the Chronological Lifespan of Yeasts, Saccharomyces cerevisiae, and Schizosaccharomyces pombe.","citation":"Adv Biol (Weinh) 2024 Apr 14;:e2400138","abstract":"Yeast is an excellent model organism for research for regulating aging and lifespan, and the studies have made many contributions to date, including identifying various factors and signaling pathways related to aging and lifespan. More than 20 years have passed since molecular biological perspectives are adopted in this research field, and intracellular factors and signal pathways that control aging and lifespan have evolutionarily conserved from yeast to mammals. Furthermore, these findings have been applied to control the aging and lifespan of various model organisms by adjustment of the nutritional environment, genetic manipulation, and drug treatment using low-molecular weight compounds. Among these, drug treatment is easier than the other methods, and research into drugs that regulate aging and lifespan is consequently expected to become more active. Chronological lifespan, a definition of yeast lifespan, refers to the survival period of a cell population under nondividing conditions. Herein, low-molecular weight compounds are summarized that extend the chronological lifespan of Saccharomyces cerevisiae and Schizosaccharomyces pombe, along with their intracellular functions. The low-molecular weight compounds are also discussed that extend the lifespan of other model organisms. Compounds that have so far only been studied in yeast may soon extend lifespan in other organisms.","doi":"10.1002/adbi.202400138","authors":"Ohtsuka H, Shimasaki T, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"14 Apr 2024","pubmed_entrez_date":"2024-04-14","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-04-15 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19447181","title":"Ab initio reconstruction of helical samples with heterogeneity, disorder and coexisting symmetries.","citation":"J Struct Biol 2009 Aug;167(2):97-105","abstract":"We describe modifications of the single particle helical reconstruction approach devised for the analysis of a sample that could not be processed with existing methods due to its variable and short range helical order. The added steps of reference-free two-dimensional image classification and alignment, and automated microtubule removal from images, have particular application to proteins or protein complexes that assemble around microtubules. The method was successfully applied to the Dam1 complex, an essential component of the yeast kinetochore that couples replicated chromosomes to spindle microtubules during mitosis. Because of its novel mode of binding, which does not involve a footprint on the microtubule lattice, new steps to deal with the disorder and heterogeneity of the Dam1 complex assembly were required to gain structural information about this complex both routinely and efficiently.","doi":"10.1016/j.jsb.2009.05.002","authors":"Ramey VH, Wang HW, Nogales E","authors_abbrev":"Ramey VH et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-05-19","publication_year":"2009","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17622533","title":"Six new amino acid-auxotrophic markers for targeted gene integration and disruption in fission yeast.","citation":"Curr Genet 2007 Aug;52(2):97-105","abstract":"Fission yeast Schizosaccharomyces pombe is amenable to genetics and is an excellent model system for studying eukaryotic cell biology. However, auxotrophic markers that can be used for both targeted gene integration and disruption are very limited. Here we performed a forward genetic screen in an effort to develop a new set of selectable markers for use in this yeast. Mutants that were auxotrophic for arginine, asparagine, cysteine, lysine, methionine and phenylalanine were isolated. Six genes were analyzed in detail and the mutations in the genes were identified. Among these six are three new genes: asn1 (+), cys2 (+) and pha2 (+) were required for biosynthesis of asparagine, cysteine and phenylalanine, respectively. New alleles of arg1 (+), lys3 (+) and met6 (+) were also identified. All of these genes proved to be suitable as selectable markers for targeted gene integration and disruption. We also showed that in Schizosaccharomyces pombe there are two apparent homologues of Saccharomyces cerevisiae MET2: the previously known met6 (+), and SPBC106.17c (named cys2 (+)). The cys2 mutation required cysteine rather than methionine. These new tools, specifically, new selectable markers, will be useful in further genetic and biological studies in fission yeast.","authors":"Ma Y, Sugiura R, Saito M, Koike A, Sio SO, Fujita Y, Takegawa K, Kuno T","authors_abbrev":"Ma Y et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-07-12","publication_year":"2007","canto_session_key":"95b10aba61b7beed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-07 09:48:17","canto_approved_date":"2026-03-09 15:55:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-06 12:12:57","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.10","SPBC56F2.11","SPBC27.08c","SPAC10F6.01c","SPBC106.17c","SPCC777.09c","SPAC13G7.06","SPBC1105.02c","SPAC227.18","SPAC31G5.04","SPAC343.16","SPBC119.10","SPBC30D10.16"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2016-02-07"},{"uniquename":"PMID:19136623","title":"Phosphorylation of Swi6/HP1 regulates transcriptional gene silencing at heterochromatin.","citation":"Genes Dev 2009 Jan 01;23(1):18-23","abstract":"Heterochromatin protein 1 (HP1) recruits various effectors to heterochromatin for multiple functions, but its regulation is unclear. In fission yeast, a HP1 homolog Swi6 recruits SHREC, Epe1, and cohesin, which are involved in transcriptional gene silencing (TGS), transcriptional activation, and sister chromatid cohesion, respectively. We found that casein kinase II (CK2) phosphorylated Swi6. Loss of CK2-dependent Swi6 phosphorylation alleviated heterochromatic TGS without affecting heterochromatin structure. This was due to the inhibited recruitment of SHREC to heterochromatin, accompanied by an increase in Epe1. Interestingly, loss of phosphorylation did not affect cohesion. These results indicate that CK2-dependent Swi6 phosphorylation specifically controls TGS in heterochromatin.","doi":"10.1101/gad.1708009","authors":"Shimada A, Dohke K, Sadaie M, Shinmyozu K, Nakayama J, Urano T, Murakami Y","authors_abbrev":"Shimada A et al.","pubmed_publication_date":"01 Jan 2009","pubmed_entrez_date":"2009-01-13","publication_year":"2009","canto_session_key":"9f1403044bcde8c5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-07-02 16:39:01","canto_approved_date":"2024-07-03 15:34:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-02 16:38:32","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":42,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPBC29B5.01","SPBC800.03","SPAC664.01c","SPAC23C11.11","SPBP35G2.10","SPBC16C6.10","SPAC1851.03","SPCC188.13c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2024-07-02"},{"uniquename":"EMBL:AU006507","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29440310","title":"Asp1 Bifunctional Activity Modulates Spindle Function via Controlling Cellular Inositol Pyrophosphate Levels in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2018 May 01;38(9)","abstract":"The generation of two daughter cells with the same genetic information requires error-free chromosome segregation during mitosis. Chromosome transmission fidelity is dependent on spindle structure/function, which requires Asp1 in the fission yeast  Schizosaccharomyces pombe  Asp1 belongs to the diphosphoinositol pentakisphosphate kinase (PPIP5K)/Vip1 family which generates high-energy inositol pyrophosphate (IPP) molecules. Here, we show that Asp1 is a bifunctional enzyme  in vivo : Asp1 kinase generates specific IPPs which are the substrates of the Asp1 pyrophosphatase. Intracellular levels of these IPPs directly correlate with microtubule stability: pyrophosphatase loss-of-function mutants raised Asp1-made IPP levels 2-fold, thus increasing microtubule stability, while overexpression of the pyrophosphatase decreased microtubule stability. Absence of Asp1-generated IPPs resulted in an aberrant, increased spindle association of the  S. pombe  kinesin-5 family member Cut7, which led to spindle collapse. Thus, chromosome transmission is controlled via intracellular IPP levels. Intriguingly, identification of the mitochondrion-associated Met10 protein as the first pyrophosphatase inhibitor revealed that IPPs also regulate mitochondrial distribution.","doi":"10.1128/MCB.00047-18","authors":"Pascual-Ortiz M, Saiardi A, Walla E, Jakopec V, Künzel NA, Span I, Vangala A, Fleig U","authors_abbrev":"Pascual-Ortiz M et al.","pubmed_publication_date":"01 May 2018","pubmed_entrez_date":"2018-02-15","publication_year":"2018","canto_session_key":"a285c6590adb104d","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-02-28 22:13:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC584.01c","SPAC23H3.08c","SPCC1672.06c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:31768988","title":"Strategies for Generating RNA Exosome Complexes from Recombinant Expression Hosts.","citation":"Methods Mol Biol 2020;2062:417-425","abstract":"The eukaryotic RNA exosome is a conserved and ubiquitous multiprotein complex that possesses multiple RNase activities and is involved in a diverse array of RNA degradation and processing events. While much of our current understanding of RNA exosome function has been elucidated using genetics and cell biology based studies of protein functions, in particular in S. cerevisiae, many important contributions in the field have been enabled through use of in vitro reconstituted complexes. Here, we present an overview of our approach to purify exosome components from recombinant sources and reconstitute them into functional complexes. Three chapters following this overview provide detailed protocols for reconstituting exosome complexes from S. cerevisiae, S. pombe, and H. sapiens. We additionally provide insight on some of the drawbacks of these methods and highlight several important discoveries that have been achieved using reconstituted complexes.","doi":"10.1007/978-1-4939-9822-7_20","authors":"Weick EM, Zinder JC, Lima CD","authors_abbrev":"Weick EM et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2019-11-27","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-11-28 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32023460","title":"Plasma Membrane Furrows Control Plasticity of ER-PM Contacts.","citation":"Cell Rep 2020 Feb 04;30(5):1434-1446.e7","abstract":"The plasma membrane (PM) forms extensive close junctions with the cortical endoplasmic reticulum (cER) in many cell types, ranging from yeast to mammals. How cells modulate structural plasticity of ER-PM contacts to accommodate space-demanding cortical events is largely unknown. Here, we report a role for eisosome-driven PM furrows in regulating ER-PM contact plasticity in fission yeast. We demonstrate that eisosome-coated PM invaginations function to stabilize local ER-PM contacts and attenuate cER remodeling dynamics through electrostatic Scs2-Pil1 interactions. We also identify divergent roles of ER-shaping proteins in controlling cER remodeling capacity and ER-PM contact plasticity. Furthermore, we show that eisosome organization is responsive to PM tension variations during active PM remodeling, which may enable adaptive control of ER-PM contact plasticity to potentially coordinate with space-demanding PM events. We thus propose a cellular strategy of modulating membrane contact plasticity by deploying sensory elements at contact sites.","doi":"10.1016/j.celrep.2019.12.098","authors":"Ng AQE, Ng AYE, Zhang D","authors_abbrev":"Ng AQE et al.","pubmed_publication_date":"04 Feb 2020","pubmed_entrez_date":"2020-02-06","publication_year":"2020","canto_session_key":"c605477efc21b69a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dan Zhang","canto_first_approved_date":"2020-03-19 13:01:50","canto_approved_date":"2026-04-22 15:38:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-23 10:24:25","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"Dan Zhang","community_curator":true,"annotation_count":24,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":4,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.10c","SPBC16G5.05c","SPAC17C9.12","SPCC830.08c","SPBC31A8.01c","SPCC736.15","SPAC1A6.07","SPAC222.14c","SPAC24B11.06c","SPBC1685.13","SPBC1539.04"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2020-03-19"},{"uniquename":"PMID:16962997","title":"Cerulenin-mediated apoptosis is involved in adenine metabolic pathway.","citation":"Biochem Biophys Res Commun 2006 Oct 27;349(3):1025-31","abstract":"Cerulenin, a fatty acid synthase (FAS) inhibitor, induces apoptosis of variety of tumor cells. To elucidate mode of action by cerulenin, we employed the proteomics approach using Schizosaccharomyces pombe. The differential protein expression profile of S. pombe revealed that cerulenin modulated the expressions of proteins involved in stresses and metabolism, including both ade10 and adk1 proteins. The nutrient supplementation assay demonstrated that cerulenin affected enzymatic steps transferring a phosphoribosyl group. This result suggests that cerulenin accumulates AMP and p-ribosyl-s-amino-imidazole carboxamide (AICAR) and reduces other necessary nucleotides, which induces feedback inhibition of enzymes and the transcriptional regulation of related genes in de novo and salvage adenine metabolic pathway. Furthermore, the deregulation of adenine nucleotide synthesis may interfere ribonucleotide reductase and cause defects in cell cycle progression and chromosome segregation. In conclusion, cerulenin induces apoptosis through deregulation of adenine nucleotide biosynthesis resulting in nuclear division defects in S. pombe.","authors":"Chung KS, Sun NK, Lee SH, Lee HJ, Choi SJ, Kim SK, Song JH, Jang YJ, Song KB, Yoo HS, Simon J, Won M","authors_abbrev":"Chung KS et al.","pubmed_publication_date":"27 Oct 2006","pubmed_entrez_date":"2006-09-12","publication_year":"2006","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34050143","title":"A single m 6 A modification in U6 snRNA diversifies exon sequence at the 5' splice site.","citation":"Nat Commun 2021 May 28;12(1):3244","abstract":"N 6 -methyladenosine (m 6 A) is a modification that plays pivotal roles in RNA metabolism and function, although its functions in spliceosomal U6 snRNA remain unknown. To elucidate its role, we conduct a large-scale transcriptome analysis of a Schizosaccharomyces pombe strain lacking this modification and found a global change of pre-mRNA splicing. The most significantly impacted introns are enriched for adenosine at the fourth position pairing the m 6 A in U6 snRNA, and exon sequences weakly recognized by U5 snRNA. This suggests cooperative recognition of 5' splice site by U6 and U5 snRNPs, and also a role of m 6 A facilitating efficient recognition of the splice sites weakly interacting with U5 snRNA, indicating that U6 snRNA m 6 A relaxes the 5' exon constraint and allows protein sequence diversity along with explosively increasing number of introns over the course of eukaryotic evolution.","doi":"10.1038/s41467-021-23457-6","authors":"Ishigami Y, Ohira T, Isokawa Y, Suzuki Y, Suzuki T","authors_abbrev":"Ishigami Y et al.","pubmed_publication_date":"28 May 2021","pubmed_entrez_date":"2021-05-29","publication_year":"2021","canto_session_key":"f319c30cc415bc60","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-31 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9561743","title":"Growth phase-dependent active transport of pyridoxine in a fission yeast, Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 1998 Apr 01;161(1):145-50","abstract":"Schizosaccharomyces pombe showed maximum pyridoxine uptake activity around 10 h after starting cultivation. High concentrations of thiamine and pyridoxine in the medium did not affect the activity or the time but changed intracellular levels of vitamin B6 compounds. Pyridoxine was taken up by a saturable mechanism with two kinds of affinity (K(m) 22.4 microM and 118 microM). The uptake depended on the energy produced anaerobically with an optimum pH of 4.5. The uptake was completely inhibited by amiloride, sodium azide or 2,4-dinitrophenol. The uptake system of the fission yeast was different in various respects from that of a budding yeast.","authors":"Yagi T, Tanouchi A, Hiraoka Y","authors_abbrev":"Yagi T et al.","pubmed_publication_date":"01 Apr 1998","pubmed_entrez_date":"1998-04-30","publication_year":"1998","canto_session_key":"efa69c18447faeb6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-03 15:35:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-10-29 08:50:52","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-10-29"},{"uniquename":"PMID:9666312","title":"Purification and kinetic characterization of hexokinase and glucose-6-phosphate dehydrogenase from Schizosaccharomyces pombe.","citation":"Biochem Cell Biol 1998;76(1):107-13","abstract":"Hexokinase and D-glucose-6-phosphate dehydrogenase (G6PDH) from Schizosaccharomyces pmbe have been purified 250-fold by an identical three-step. Both enzymes are dimeric with a molecular mass of 88 kDa for the kinase and 112 kDa for the dehydrogenase. Steady-state kinetic studies were performed on hexokinase and G6PDH, which form the glucose phosphate branch of the oxidative pentose phosphate pathway of S. pombe (fission yeast). Hexokinase promotes Mg(2+)-activated phosphorylation of D-glucose by the equilibrium random Bi Bi mechanism with formation of the abortive enzyme-ADP-glucose complex. ADP inhibits the kinase competitively versus ATP and noncompetitively versus D-glucose. The Mg2+ activation of hexokinase is associated with an increase in the maximal velocity by its interaction with the ternary complex to facilitate the transfer of the phosphoryl group. G6PDH catalyzes NADP(+)-linked oxidation of D-glucose-6-phosphate by the ordered Bi Bi mechanism with NADP+ as the leading reactant. High NADP+ concentration inhibits the dehydrogenase by forming the dead-end ternary complex. In addition, G6PDH is also subjected to product inhibition by NADPH and noncompetitive inhibition by A(G)TP. Thus, the oxidative pentose phosphate pathway in S. pombe may be regulated via inhibition of hexokinase by ADP in conjunction with inhibition of G6PDH by NADPH and ATP.","authors":"Tsai CS, Chen Q","authors_abbrev":"Tsai CS et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-07-17","publication_year":"1998","canto_session_key":"e48ed9a906a89d37","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-15 17:09:32","canto_approved_date":"2018-12-15 17:09:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-15 17:09:25","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.04"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2018-12-15"},{"uniquename":"PMID:16115814","title":"Pas1, a G1 cyclin, regulates amino acid uptake and rescues a delay in G1 arrest in Tsc1 and Tsc2 mutants in Schizosaccharomyces pombe.","citation":"Hum Mol Genet 2005 Oct 01;14(19):2851-8","abstract":"Tuberous sclerosis complex is a tumor suppressor syndrome caused by mutations in either the TSC1 or the TSC2 gene. Previous studies have shown that deletion of the TSC1 or TSC2 ortholog in Schizosaccharomyces pombe results in an amino acid uptake defect, with conditional lethality. We identified a G1 cyclin, pas1+, as a high-copy suppressor of this defect in Deltatsc1. Disruption of pas1+ causes defects in arginine and leucine uptake that are remarkably similar to Deltatsc1 and Deltatsc2, whereas Deltapas1Deltatsc1 and Deltapas1Deltatsc2 double mutants have more severe amino acid uptake defects. In a second screen, we identified a novel G63D/S165 N mutant of the small GTPase Rhb1, the target of the Tsc1/Tsc2 protein complex. The Rhb1 mutant suppresses amino acid uptake in Deltatsc1 yeast, but not in Deltapas1 yeast. Hence, Pas1 does not regulate amino acid uptake through Rhb1. To determine whether Pas1 links nutrient availability to cell cycle progression downstream of the Tsc1/Tsc2 complex, we examined the kinetics of G1 arrest in single and double mutant strains. After nitrogen starvation, Deltatsc1 and Deltatsc2 yeast had a delay in G1 arrest when compared with wild-type, which was rescued by deletion of pas1+. In summary, we identified the G1 cyclin, Pas1, as a novel regulator of amino acid uptake. Our data support a model in which Pas1 inhibits G1 arrest downstream of Tsc1 and Tsc2, linking nutrient uptake and cell cycle progression in yeast.","authors":"van Slegtenhorst M, Mustafa A, Henske EP","authors_abbrev":"van Slegtenhorst M et al.","pubmed_publication_date":"01 Oct 2005","pubmed_entrez_date":"2005-08-24","publication_year":"2005","canto_session_key":"2697c460cee0ce6a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-07 17:50:02","canto_approved_date":"2024-07-15 11:44:56","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-01-12 17:55:57","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":46,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.13","SPAC1039.09","SPAC869.10c","SPAC630.13c","SPBC1A4.02c","SPBC428.16c","SPBC29A3.02c","SPAC19E9.03","SPCC330.05c","SPCC1322.13","SPAP7G5.06"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2017-03-07"},{"uniquename":"PMID:26697368","title":"Genome wide transcription profiling reveals a major role for the transcription factor Atf1 in regulation of cell division in Schizosaccharomyces pombe.","citation":"Genom Data 2015 Dec;6:184-7","abstract":"The mechanism underlying stringently controlled sequence of events in the eukaryotic cell cycle involves periodic transcription of a number of genes encoding important regulators of cell cycle, growth, proliferation and apoptosis. Deregulated activities of transcription factors that contribute to this programmed gene expression, are associated with many diseases including cancer. A detailed mechanistic understanding of the transcriptional control associated with cell division is, therefore, important. We have reported earlier that the transcription factor Atf1 in Schizosaccharomyces pombe can regulate G2-M transition by directly controlling the expression of the mitotic cyclin Cdc13 (1).To gain a better understanding of the role of Atf1 in cell cycle, we performed a microarray based identification of cell cycle related targets of Atf1. The microarray data are available at NCBI's Gene Expression Omnibus (GEO) Series (accession number GSE71820). Here we report the annotation of the genes whose expression get altered by Atf1 overexpression and also provide details related to sample processing and statistical analysis of our microarray data.","doi":"10.1016/j.gdata.2015.09.014","authors":"Bandyopadhyay S, Sundaram G","authors_abbrev":"Bandyopadhyay S et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-12-24","publication_year":"2015","canto_session_key":"7d087bec74eeb3b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Geetanjali Sundaram","canto_approved_date":"2017-01-31 14:10:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-02-29 09:57:59","canto_added_date":"2015-12-25 01:19:07","annotation_curators":[{"name":"Geetanjali Sundaram","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-02-29"},{"uniquename":"EMBL:AU010643","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9024682","title":"A centromere DNA-binding protein from fission yeast affects chromosome segregation and has homology to human CENP-B.","citation":"J Cell Biol 1997 Feb 10;136(3):487-500","abstract":"Genetic and biochemical strategies have been used to identify Schizosaccharomyces pombe proteins with roles in centromere function. One protein, identified by both approaches, shows significant homology to the human centromere DNA-binding protein, CENP-B, and is identical to Abp1p (autonomously replicating sequence-binding protein 1) (Murakami, Y., J.A. Huberman, and J. Hurwitz. 1996. Proc. Natl. Acad. Sci. USA. 93:502-507). Abp1p binds in vitro specifically to at least three sites in centromeric central core DNA of S. pombe chromosome II (cc2). Overexpression of abp1 affects mitotic chromosome stability in S. pombe. Although inactivation of the abp1 gene is not lethal, the abp1 null strain displays marked mitotic chromosome instability and a pronounced meiotic defect. The identification of a CENP-B-related centromere DNA-binding protein in S. pombe strongly supports the hypothesis that fission yeast centromeres are structurally and functionally related to the centromeres of higher eukaryotes.","authors":"Halverson D, Baum M, Stryker J, Carbon J, Clarke L","authors_abbrev":"Halverson D et al.","pubmed_publication_date":"10 Feb 1997","pubmed_entrez_date":"1997-02-10","publication_year":"1997","canto_session_key":"6913a3b5e8aa3c2b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-31 17:54:56","canto_approved_date":"2024-06-28 11:06:23","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-08-31 17:54:51","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-31"},{"uniquename":"PMID:23678980","title":"Hydrophilic material for the selective enrichment of 5-hydroxymethylcytosine and its liquid chromatography-tandem mass spectrometry detection.","citation":"Anal Chem 2013 Jun 18;85(12):6129-35","abstract":"5-Methylcytosine (5-mC), an important epigenetic modification involved in development, can be converted enzymatically to 5-hydroxymethylcytosine (5-hmC). 5-hmC is considered an intermediate of active DNA cytosine demethylation and makes itself serve as an epigenetic mark. 5-hmC content in most mammalian cells is low and the quantification of 5-hmC by liquid chromatography-mass spectrometry (LC-MS) frequently suffers from ion suppression by the presence of unmodified nucleosides. To circumvent this problem, we developed a method to selectively transfer a glucosyl group to the hydroxymethyl moiety of 5-hmC and form a more hydrophilic residue (β-glucosyl-5-hydroxymethyl-2'-deoxycytidine, 5-gmdC) by using T4 β-glucosyltransferase. The more hydrophilic 5-gmdC can be selectively enriched by using NH2-silica via hydrophilic interaction prior to liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis, which eliminates the ion suppression and significantly improves the detection sensitivity and accuracy. Using this method, we successfully quantified 5-hmC content in genomic DNA of three human cell lines and seven yeast strains. To the best of our knowledge, this is the first report about the existence of 5-hmC in the model organism of yeast. In addition, the contents of 5-hmC in two yeast strains of Schizosaccharomyces pombe are even higher than those of 5-mC, indicating that 5-hmC may play important roles on the physiological functions of yeast.","doi":"10.1021/ac4010869","authors":"Tang Y, Chu JM, Huang W, Xiong J, Xing XW, Zhou X, Feng YQ, Yuan BF","authors_abbrev":"Tang Y et al.","pubmed_publication_date":"18 Jun 2013","pubmed_entrez_date":"2013-05-18","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31974447","title":"Formation of S. pombe Erh1 homodimer mediates gametogenic gene silencing and meiosis progression.","citation":"Sci Rep 2020 Jan 23;10(1):1034","abstract":"Timely and accurate expression of the genetic information relies on the integration of environmental cues and the activation of regulatory networks involving transcriptional and post-transcriptional mechanisms. In fission yeast, meiosis-specific transcripts are selectively targeted for degradation during mitosis by the EMC complex, composed of Erh1, the ortholog of human ERH, and the YTH family RNA-binding protein Mmi1. Here, we present the crystal structure of Erh1 and show that it assembles as a homodimer. Mutations of amino acid residues to disrupt Erh1 homodimer formation result in loss-of-function phenotypes, similar to erh1∆ cells: expression of meiotic genes is derepressed in mitotic cells and meiosis progression is severely compromised. Interestingly, formation of Erh1 homodimer is dispensable for interaction with Mmi1, suggesting that only fully assembled EMC complexes consisting of two Mmi1 molecules bridged by an Erh1 dimer are functionally competent. We also show that Erh1 does not contribute to Mmi1-dependent down-regulation of the meiosis regulator Mei2, supporting the notion that Mmi1 performs additional functions beyond EMC. Overall, our results provide a structural basis for the assembly of the EMC complex and highlight its biological relevance in gametogenic gene silencing and meiosis progression.","doi":"10.1038/s41598-020-57872-4","authors":"Hazra D, Andrić V, Palancade B, Rougemaille M, Graille M","authors_abbrev":"Hazra D et al.","pubmed_publication_date":"23 Jan 2020","pubmed_entrez_date":"2020-01-25","publication_year":"2020","canto_session_key":"e3df150646d26fce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mathieu Rougemaille","canto_first_approved_date":"2021-01-21 16:17:13","canto_approved_date":"2021-01-21 16:17:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-01-15 15:41:32","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"Mathieu Rougemaille","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPNCRNA.103","SPCC736.12c","SPAC19G12.17","SPBC32H8.11","SPAC27D7.13c"],"gene_count":6,"ltp_gene_count":1,"approved_date":"2021-01-21","pdb_entries":[{"pdb_id":"6s2w","gene_chains":[{"gene_uniquename":"SPAC19G12.17","chain":"A/B/C","position":"1-104"}],"title":"Structure of S. pombe Erh1, a protein important for meiotic mRNA decay in mitosis and meiosis progression.","entry_authors":"Hazra D,Graille M","entry_authors_abbrev":"Hazra D et al.","reference_uniquename":"PMID:31974447","experimental_method":"X-ray","resolution":"1.95"}]},{"uniquename":"PMID:27825453","title":"Cytokinesis: Going Super-Resolution in Live Cells.","citation":"Curr Biol 2016 Nov 07;26(21):R1150-R1152","abstract":"Super-resolution fluorescence microscopy has emerged as a powerful tool for studying molecular organization, but mostly in fixed cells. New work using high-speed fluorescence photoactivation localization microscopy now reveals the organization of cytokinesis nodes and contractile rings in live fission yeast cells.","doi":"10.1016/j.cub.2016.09.026","authors":"Liu Y, Wu JQ","authors_abbrev":"Liu Y et al.","pubmed_publication_date":"07 Nov 2016","pubmed_entrez_date":"2016-11-10","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-11-10 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084865","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.53"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10996255","title":"Members of the Arabidopsis 14-3-3 gene family trans-complement two types of defects in fission yeast.","citation":"Plant Sci 2000 Sep 08;158(1-2):155-161","abstract":"14-3-3 proteins are highly conserved among eukaryotes and perform diverse biochemical activities. We isolated five types of Arabidopsis 14-3-3 cDNAs in a screen for clones that could block ectopic meiosis driven by the pat1 mutation in fission yeast. Overexpression of fission yeast rad24, which encodes a 14-3-3 protein, also suppressed pat1. All Arabidopsis clones isolated could rescue the deformed morphology and elevated UV sensitivity of the rad24 mutant. Thus, it appears that Arabidopsis 14-3-3 proteins can generally substitute for their fission yeast counterpart in function. Expression of an Arabidopsis 14-3-3 clone, GF14µ, was shown to be rather ubiquitous among plant organs.","authors":"Kuromori T, Yamamoto M","authors_abbrev":"Kuromori T et al.","pubmed_publication_date":"08 Sep 2000","pubmed_entrez_date":"2000-09-21","publication_year":"2000","canto_session_key":"c834fc2c5d8eb058","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-13 13:24:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-13 13:24:22","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPBC19C2.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-10-13"},{"uniquename":"PMID:29319508","title":"Genes Controlling 2-deoxyglucose Induced Lysis and Formation of Reactive Oxygen Species in Schizosaccharomyces pombe.","citation":"Pol J Microbiol 2017 Sep 27;66(3):393-396","abstract":"Schizosaccharomyces pombe cells of strains each carrying a deletion of one of the genes snf5, ypa1, pho7 and pas1 and of a strain overexpressing gene odr1, have been previously shown to grow in presence of the toxic glucose analogue 2-deoxyglucose (2-DG). Here we report that these genes control 2-DG induced lysis and are, with the exception of odr1, also involved in control of formation of reactive oxygen species (ROS) upon exposure of cells to H2O2. Lysis of deletion strains, but not of strain overexpressing odr1, is dependent on glucose concentration of the medium whereas ROS formation is glucose independent.","doi":"10.5604/01.3001.0010.4877","authors":"Vishwanatha A, D'Souza CJM, Schweingruber ME","authors_abbrev":"Vishwanatha A et al.","pubmed_publication_date":"27 Sep 2017","pubmed_entrez_date":"2018-01-11","publication_year":"2017","canto_session_key":"b466cec3cdc7c5c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Akshay Vishwanatha","canto_first_approved_date":"2018-03-01 14:17:59","canto_approved_date":"2018-03-01 14:17:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-22 13:43:33","canto_added_date":"2018-01-12 01:15:45","annotation_curators":[{"name":"Akshay Vishwanatha","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19E9.03","SPAC2F7.08c","SPAC4F10.04","SPBC215.10","SPBC27B12.11c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-03-01"},{"uniquename":"PMID:34202872","title":"Single-Agent and Fixed-Dose Combination HIV-1 Protease Inhibitor Drugs in Fission Yeast ( Schizosaccharomyces pombe ).","citation":"Pathogens 2021 Jun 24;10(7)","abstract":"Successful combination antiretroviral therapies (cART) eliminate active replicating HIV-1, slow down disease progression, and prolong lives. However, cART effectiveness could be compromised by the emergence of viral multidrug resistance, suggesting the need for new drug discoveries. The objective of this study was to further demonstrate the utility of the fission yeast cell-based systems that we developed previously for the discovery and testing of HIV protease (PR) inhibitors (PIs) against wild-type or multi-PI drug resistant  M11 PR that we isolated from an infected individual. All thirteen FDA-approved single-agent and fixed-dose combination HIV PI drugs were tested. The effect of these drugs on HIV PR activities was tested in pure compounds or formulation drugs. All FDA-approved PI drugs, except for a prodrug FPV, were able to suppress the wild-type PR-induced cellular and enzymatic activities. Relative drug potencies measured by EC 50  in fission yeast were discussed in comparison with those measured in human cells. In contrast, none of the FDA-approved drugs suppressed the multi-PI drug resistant  M11 PR activities. Results of this study show that fission yeast is a reliable cell-based system for the discovery and testing of HIV PIs and further demonstrate the need for new PI drugs against viral multi-PI resistance.","doi":"10.3390/pathogens10070804","authors":"Zhang J, Vernon K, Li Q, Benko Z, Amoroso A, Nasr M, Zhao RY","authors_abbrev":"Zhang J et al.","pubmed_publication_date":"24 Jun 2021","pubmed_entrez_date":"2021-07-02","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-07-04 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR12844","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:19700","HGNC:21574","HGNC:21204","SPBC1289.04c","HGNC:19701","HGNC:23034"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11294907","title":"Roles of a fimbrin and an alpha-actinin-like protein in fission yeast cell polarization and cytokinesis.","citation":"Mol Biol Cell 2001 Apr;12(4):1061-77","abstract":"Eukaryotic cells contain many actin-interacting proteins, including the alpha-actinins and the fimbrins, both of which have actin cross-linking activity in vitro. We report here the identification and characterization of both an alpha-actinin-like protein (Ain1p) and a fimbrin (Fim1p) in the fission yeast Schizosaccharomyces pombe. Ain1p localizes to the actomyosin-containing medial ring in an F-actin-dependent manner, and the Ain1p ring contracts during cytokinesis. ain1 deletion cells have no obvious defects under normal growth conditions but display severe cytokinesis defects, associated with defects in medial-ring and septum formation, under certain stress conditions. Overexpression of Ain1p also causes cytokinesis defects, and the ain1 deletion shows synthetic effects with other mutations known to affect medial-ring positioning and/or organization. Fim1p localizes both to the cortical actin patches and to the medial ring in an F-actin-dependent manner, and several lines of evidence suggest that Fim1p is involved in polarization of the actin cytoskeleton. Although a fim1 deletion strain has no detectable defect in cytokinesis, overexpression of Fim1p causes a lethal cytokinesis defect associated with a failure to form the medial ring and concentrate actin patches at the cell middle. Moreover, an ain1 fim1 double mutant has a synthetical-lethal defect in medial-ring assembly and cell division. Thus, Ain1p and Fim1p appear to have an overlapping and essential function in fission yeast cytokinesis. In addition, protein-localization and mutant-phenotype data suggest that Fim1p, but not Ain1p, plays important roles in mating and in spore formation.","authors":"Wu JQ, Bähler J, Pringle JR","authors_abbrev":"Wu JQ et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-04-11","publication_year":"2001","canto_session_key":"dd81766bd2cc050a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-06-09 15:42:56","canto_approved_date":"2026-06-17 12:47:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-06-09 15:42:50","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":67,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.03","SPAC15A10.08","SPCC4B3.15","SPAC4F8.13c","SPBC1778.06c","SPCC645.05c","SPBC32H8.12c","SPAC4A8.15c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-06-09"},{"uniquename":"PMID:24286828","title":"Entrapment of chromosomes by condensin rings prevents their breakage during cytokinesis.","citation":"Dev Cell 2013 Nov 25;27(4):469-78","abstract":"Successful segregation of chromosomes during mitosis and meiosis depends on the action of the ring-shaped condensin complex, but how condensin ensures the complete disjunction of sister chromatids is unknown. We show that the failure to segregate chromosome arms, which results from condensin release from chromosomes by proteolytic cleavage of its ring structure, leads to a DNA damage checkpoint-dependent cell-cycle arrest. Checkpoint activation is triggered by the formation of chromosome breaks during cytokinesis, which proceeds with normal timing despite the presence of lagging chromosome arms. Remarkably, enforcing condensin ring reclosure by chemically induced dimerization just before entry into anaphase is sufficient to restore chromosome arm segregation. We suggest that topological entrapment of chromosome arms by condensin rings ensures their clearance from the cleavage plane and thereby avoids their breakage during cytokinesis.","doi":"10.1016/j.devcel.2013.10.018","authors":"Cuylen S, Metz J, Hruby A, Haering CH","authors_abbrev":"Cuylen S et al.","pubmed_publication_date":"25 Nov 2013","pubmed_entrez_date":"2013-11-30","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20655467","title":"Crossover invariance determined by partner choice for meiotic DNA break repair.","citation":"Cell 2010 Jul 23;142(2):243-55","abstract":"Crossovers between meiotic homologs are crucial for their proper segregation, and crossover number and position are carefully controlled. Crossover homeostasis in budding yeast maintains crossovers at the expense of noncrossovers when double-strand DNA break (DSB) frequency is reduced. The mechanism of maintaining constant crossover levels in other species has been unknown. Here we investigate in fission yeast a different aspect of crossover control--the near invariance of crossover frequency per kb of DNA despite large variations in DSB intensity across the genome. Crossover invariance involves the choice of sister chromatid versus homolog for DSB repair. At strong DSB hotspots, intersister repair outnumbers interhomolog repair approximately 3:1, but our genetic and physical data indicate the converse in DSB-cold regions. This unanticipated mechanism of crossover control may operate in many species and explain, for example, the large excess of DSBs over crossovers and the repair of DSBs on unpaired chromosomes in diverse species.","doi":"10.1016/j.cell.2010.05.041","authors":"Hyppa RW, Smith GR","authors_abbrev":"Hyppa RW et al.","pubmed_publication_date":"23 Jul 2010","pubmed_entrez_date":"2010-07-27","publication_year":"2010","canto_session_key":"dcd57b242720f786","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC409.03","SPAC8E11.03c","SPAC20H4.07","SPCC4G3.05c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:25619765","title":"The CENP-A N-tail confers epigenetic stability to centromeres via the CENP-T branch of the CCAN in fission yeast.","citation":"Curr Biol 2015 Feb 02;25(3):348-356","abstract":"In most eukaryotes, centromeres are defined epigenetically by presence of the histone H3 variant CENP-A [1-3]. CENP-A-containing chromatin recruits the constitutive centromere-associated network (CCAN) of proteins, which in turn directs assembly of the outer kinetochore to form microtubule attachments and ensure chromosome segregation fidelity [4-6]. Whereas the mechanisms that load CENP-A at centromeres are being elucidated, the functions of its divergent N-terminal tail remain enigmatic [7-12]. Here, we employ the well-studied fission yeast centromere [13-16] to investigate the function of the CENP-A (Cnp1) N-tail. We show that alteration of the N-tail does not affect Cnp1 loading at centromeres, outer kinetochore formation, or spindle checkpoint signaling but nevertheless elevates chromosome loss. N-tail mutants exhibited synthetic lethality with an altered centromeric DNA sequence, with rare survivors harboring chromosomal fusions in which the altered centromere was epigenetically inactivated. Elevated centromere inactivation was also observed for N-tail mutants with unaltered centromeric DNA sequences. N-tail mutants specifically reduced localization of the CCAN proteins Cnp20/CENP-T and Mis6/CENP-I, but not Cnp3/CENP-C. Overexpression of Cnp20/CENP-T suppressed defects in an N-tail mutant, suggesting a link between reduced CENP-T recruitment and the observed centromere inactivation phenotype. Thus, the Cnp1 N-tail promotes epigenetic stability of centromeres in fission yeast, at least in part via recruitment of the CENP-T branch of the CCAN.","doi":"10.1016/j.cub.2014.11.060","authors":"Folco HD, Campbell CS, May KM, Espinoza CA, Oegema K, Hardwick KG, Grewal SIS, Desai A","authors_abbrev":"Folco HD et al.","pubmed_publication_date":"02 Feb 2015","pubmed_entrez_date":"2015-01-27","publication_year":"2015","canto_session_key":"41cf39ea6dc64d5a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hernan Diego Folco","canto_first_approved_date":"2016-01-20 16:23:49","canto_approved_date":"2026-06-21 13:56:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-30 17:19:28","canto_added_date":"2015-01-28 01:15:43","annotation_curators":[{"name":"Arshad Desai","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Hernan Diego Folco","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.20c","SPBC800.13","SPBC428.08c","SPBC1105.17","SPAPB1A10.02","SPBC11C11.03","SPBC1861.01c","SPAC10F6.09c"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2016-01-20"},{"uniquename":"PMID:21437270","title":"The FUN30 chromatin remodeler, Fft3, protects centromeric and subtelomeric domains from euchromatin formation.","citation":"PLoS Genet 2011 Mar;7(3):e1001334","abstract":"The chromosomes of eukaryotes are organized into structurally and functionally discrete domains. This implies the presence of insulator elements that separate adjacent domains, allowing them to maintain different chromatin structures. We show that the Fun30 chromatin remodeler, Fft3, is essential for maintaining a proper chromatin structure at centromeres and subtelomeres. Fft3 is localized to insulator elements and inhibits euchromatin assembly in silent chromatin domains. In its absence, euchromatic histone modifications and histone variants invade centromeres and subtelomeres, causing a mis-regulation of gene expression and severe chromosome segregation defects. Our data strongly suggest that Fft3 controls the identity of chromatin domains by protecting these regions from euchromatin assembly.","doi":"10.1371/journal.pgen.1001334","authors":"Strålfors A, Walfridsson J, Bhuiyan H, Ekwall K","authors_abbrev":"Strålfors A et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-03-26","publication_year":"2011","canto_session_key":"edf1fcf16969393b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-03-23 14:40:26","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-02-15 16:16:54","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25A8.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-02-15"},{"uniquename":"PMID:1868574","title":"Thiamine in Schizosaccharomyces pombe: dephosphorylation, intracellular pool, biosynthesis and transport.","citation":"Curr Genet 1991 Apr;19(4):249-54","abstract":"We have investigated the thiamine metabolism in Schizosaccharomyces pombe and shown that: (1) Thiamine-repressible acid phosphate, coded for by the gene pho4, dephosphorylates thiamine phosphates indicating that the enzyme acts as a thiamine phosphate phosphatase. (2) In vivo synthesized thiamine is present intracellularly mainly as thiamine diphosphate. Starving cells for glucose decreases the intracellular thiamine pool. (3) The genes thi2, thi3 and thi4 control thiamine biosynthesis and probably code for thiamine biosynthetic enzymes. Thi3, which is involved in the synthesis of the pyrimidine moiety of the thiamine molecule, is allelic to the thiamine repressible gene nmt1. (4) Thiamine uptake is a thiamine regulated process, probably occurs by active transport and is controlled by the gene ptr1.","authors":"Schweingruber AM, Dlugonski J, Edenharter E, Schweingruber ME","authors_abbrev":"Schweingruber AM et al.","pubmed_publication_date":"Apr 1991","pubmed_entrez_date":"1991-04-01","publication_year":"1991","canto_session_key":"c2a58169d7d0b7d3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-03-12 16:36:43","canto_approved_date":"2023-01-26 17:36:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 16:36:37","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.02","SPBC26H8.01","SPBC428.03c","SPAC19D5.04","SPAC23H4.10c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2015-03-12"},{"uniquename":"PMID:22438582","title":"Spindle pole body components are reorganized during fission yeast meiosis.","citation":"Mol Biol Cell 2012 May;23(10):1799-811","abstract":"During meiosis, the centrosome/spindle pole body (SPB) must be regulated in a manner distinct from that of mitosis to achieve a specialized cell division that will produce gametes. In this paper, we demonstrate that several SPB components are localized to SPBs in a meiosis-specific manner in the fission yeast Schizosaccharomyces pombe. SPB components, such as Cut12, Pcp1, and Spo15, which stay on the SPB during the mitotic cell cycle, disassociate from the SPB during meiotic prophase and then return to the SPB immediately before the onset of meiosis I. Interestingly, the polo kinase Plo1, which normally localizes to the SPB during mitosis, is excluded from them in meiotic prophase, when meiosis-specific, horse-tail nuclear movement occurs. We found that exclusion of Plo1 during this period was essential to properly remodel SPBs, because artificial targeting of Plo1 to SPBs resulted in an overduplication of SPBs. We also found that the centrin Cdc31 was required for meiotic SPB remodeling. Thus Plo1 and a centrin play central roles in the meiotic SPB remodeling, which is essential for generating the proper number of meiotic SPBs and, thereby provide unique characteristics to meiotic divisions.","doi":"10.1091/mbc.E11-11-0951","authors":"Ohta M, Sato M, Yamamoto M","authors_abbrev":"Ohta M et al.","pubmed_publication_date":"May 2012","pubmed_entrez_date":"2012-03-23","publication_year":"2012","canto_session_key":"5524d2f4237ade3e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2020-02-29 14:59:35","canto_approved_date":"2024-03-26 16:27:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-20 01:26:57","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Masamitsu Sato","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC23C11.16","SPBC12D12.01","SPCC1682.04","SPAC6G9.06c","SPBC649.05","SPBC8D2.05c","SPBC11B10.09","SPAC1F3.06c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2020-02-29"},{"uniquename":"PMID:9115433","title":"Centromeres, checkpoints and chromatid cohesion.","citation":"Curr Opin Genet Dev 1997 Apr;7(2):264-73","abstract":"An emerging view is that the formation of active centromeres is modulated in an epigenetic manner reflecting the association of centromeres with heterochromatin. Support for this comes from studies on fission yeast centromeres, the properties of human neocentromeres and dicentric chromosomes, and analyses of Drosophila minichromosome deletion derivatives. A link has been established between tension across kinetochores and the phosphorylation status of kinetochore components. Vertebrate homologues of yeast MAD2 have recently been isolated and localized to kinetochores, indicating that components of the spindle integrity checkpoint are conserved. The linkage between sister chromatids is only dissolved at anaphase during mitotic and meiotic divisions. Phenotypic and localization data combined with their pattern of rapid degradation at anaphase have implicated several yeast and Drosophila proteins in aspects of sister chromatid cohesion.","authors":"Allshire RC","authors_abbrev":"Allshire RC","pubmed_publication_date":"Apr 1997","pubmed_entrez_date":"1997-04-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19475389","title":"Visualization of fluorescence-tagged proteins in fission yeast: the analysis of mitotic spindle dynamics using GFP-tubulin under the native promoter.","citation":"Methods Mol Biol 2009;545:185-203","abstract":"Mitotic spindle microtubules pull chromosomes toward each pole to generate two daughter cells. Proper spindle formation and function are required to prevent tumorigenesis and cell death. The fission yeast Schizosaccharomyces pombe has been widely used as a model organism to understand the molecular mechanism of mitosis due to its convenience in genetics, molecular biology, and cell biology. The development of fluorescent protein systems and microscopy enables us to investigate the \"true\" behavior of proteins in living fission yeast cells using a strain with a fluorescence-tagged gene under its native promoter. In this way the level of expression of tagged protein is similar to the level of wild-type nontagged protein. In this chapter we illustrate standard methods to generate strains expressing fluorescently tagged proteins and to observe them under the microscope. Specifically, we introduce a GFP-tubulin strain to analyze the dynamic behavior of spindle microtubules. Observation of GFP-tubulin under its native promoter has illuminated the process of kinetochore-microtubule attachment process in fission yeast.","doi":"10.1007/978-1-60327-993-2_11","authors":"Sato M, Toya M, Toda T","authors_abbrev":"Sato M et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-05-29","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33504776","title":"Complete sequences of Schizosaccharomyces pombe subtelomeres reveal multiple patterns of genome variation.","citation":"Nat Commun 2021 Jan 27;12(1):611","abstract":"Genome sequences have been determined for many model organisms; however, repetitive regions such as centromeres, telomeres, and subtelomeres have not yet been sequenced completely. Here, we report the complete sequences of subtelomeric homologous (SH) regions of the fission yeast Schizosaccharomyces pombe. We overcame technical difficulties to obtain subtelomeric repetitive sequences by constructing strains that possess single SH regions of a standard laboratory strain. In addition, some natural isolates of S. pombe were analyzed using previous sequencing data. Whole sequences of SH regions revealed that each SH region consists of two distinct parts with mosaics of multiple common segments or blocks showing high variation among subtelomeres and strains. Subtelomere regions show relatively high frequency of nucleotide variations among strains compared with the other chromosomal regions. Furthermore, we identified subtelomeric RecQ-type helicase genes, tlh3 and tlh4, which add to the already known tlh1 and tlh2, and found that the tlh1-4 genes show high sequence variation with missense mutations, insertions, and deletions but no severe effects on their RNA expression. Our results indicate that SH sequences are highly polymorphic and hot spots for genome variation. These features of subtelomeres may have contributed to genome diversity and, conversely, various diseases.","doi":"10.1038/s41467-020-20595-1","authors":"Oizumi Y, Kaji T, Tashiro S, Takeshita Y, Date Y, Kanoh J","authors_abbrev":"Oizumi Y et al.","pubmed_publication_date":"27 Jan 2021","pubmed_entrez_date":"2021-01-28","publication_year":"2021","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2021-01-30 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16980382","title":"Genetic evidence for phospholipid-mediated regulation of the Rab GDP-dissociation inhibitor in fission yeast.","citation":"Genetics 2006 Nov;174(3):1259-71","abstract":"We have previously identified mutant alleles of genes encoding two Rab proteins, Ypt3 and Ryh1, through a genetic screen using the immunosuppressant drug FK506 in fission yeast. In the same screen, we isolated gdi1-i11, a mutant allele of the essential gdi1+ gene encoding Rab GDP-dissociation inhibitor. In gdi1-i11, a conserved Gly267 was substituted by Asp. The Gdi1G267D protein failed to extract Rabs from membrane and Rabs were depleted from the cytosolic fraction in the gdi1-i11 mutant cells. Consistently, the Gdi1G267D protein was found mostly in the membrane fraction, whereas wild-type Gdi1 was found in both the cytosolic and the membrane fraction. Notably, overexpression of spo20+, encoding a phosphatidylcholine/phosphatidylinositol transfer protein, rescued gdi1-i11 mutation, but not ypt3-i5 or ryh1-i6. The gdi1-i11 and spo20-KC104 mutations are synthetically lethal, and the wild-type Gdi1 failed to extract Rabs from the membrane in the spo20-KC104 mutant. The phosphatidylinositol-transfer activity of Spo20 is dispensable for the suppression of the gdi1-i11 mutation, suggesting that the phosphatidylcholine-transfer activity is important for the suppression. Furthermore, knockout of the pct1+ gene encoding a choline phosphate cytidyltransferase rescued the gdi1-i11 mutation. Together, our findings suggest that Spo20 modulates Gdi1 function via regulation of phospholipid metabolism of the membranes.","authors":"Ma Y, Kuno T, Kita A, Nabata T, Uno S, Sugiura R","authors_abbrev":"Ma Y et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-09-19","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4C5.02c","SPAC3H8.10","SPAC644.04","SPAC18G6.03","SPAC9E9.07c","SPBP4H10.04","SPAC22H10.12c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:16926515","title":"A rapid method for protein extraction from fission yeast.","citation":"Biosci Biotechnol Biochem 2006 Aug;70(8):1992-4","abstract":"Researchers working with fission yeast conduct protein extraction widely and frequently, but this includes the handling of glass beads, and hence is laborious and cumbersome, especially when dealing with a large number of samples. Here we describe a rapid and reliable method for preparing protein extract from fission yeast, one which is applicable to routine western blotting.","authors":"Matsuo Y, Asakawa K, Toda T, Katayama S","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-24","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22526418","title":"Meiotic actin rings are essential for proper sporulation in fission yeast.","citation":"J Cell Sci 2012 Mar 15;125(Pt 6):1429-39","abstract":"Sporulation is a unique form of cytokinesis that occurs following meiosis II in many yeasts, during which four daughter cells (spores) are generated within a single mother cell. Here we characterize the role of F-actin in the process of sporulation in the fission yeast Schizosaccharomyces pombe. As shown previously, we find that F-actin assembles into four ring structures per ascus, referred to as the meiotic actin ring (MeiAR). The actin nucleators Arp2/3 and formin For3 assemble into ring structures that overlap with Meu14, a protein known to assemble into the so-called leading edge, a ring structure that is known to guide forespore membrane assembly. Interestingly, F-actin makes rings that occupy a larger region behind the leading edge ring. Time-lapse microscopy showed that the MeiAR assembles near the spindle pole bodies and undergoes an expansion in diameter during the early stages of meiosis II, followed by closure in later stages of meiosis II. MeiAR closure completes the process of forespore membrane assembly. Loss of the MeiAR leads to excessive assembly of forespore membranes with a deformed appearance. The rate of closure of the MeiAR is dictated by the function of the septation initiation network (SIN). We conclude that the MeiAR ensures proper targeting of the membrane biogenesis machinery to the leading edge, thereby ensuring the formation of spherical spores.","doi":"10.1242/jcs.091561","authors":"Yan H, Balasubramanian MK","authors_abbrev":"Yan H et al.","pubmed_publication_date":"15 Mar 2012","pubmed_entrez_date":"2012-04-25","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26891792","title":"Calcium modulation of doxorubicin cytotoxicity in yeast and human cells.","citation":"Genes Cells 2016 Mar;21(3):226-40","abstract":"Doxorubicin is a widely used chemotherapeutic agent, but its utility is limited by cellular resistance and off-target effects. To understand the molecular mechanisms regulating chemotherapeutic responses to doxorubicin, we previously carried out a genomewide search of doxorubicin-resistance genes in Schizosaccharomyces pombe fission yeast and showed that these genes are organized into networks that counteract doxorubicin cytotoxicity. Here, we describe the identification of a subgroup of doxorubicin-resistance genes that, when disrupted, leads to reduced tolerance to exogenous calcium. Unexpectedly, we observed a suppressive effect of calcium on doxorubicin cytotoxicity, where concurrent calcium and doxorubicin treatment resulted in significantly higher cell survival compared with cells treated with doxorubicin alone. Conversely, inhibitors of voltage-gated calcium channels enhanced doxorubicin cytotoxicity in the mutants. Consistent with these observations in fission yeast, calcium also suppressed doxorubicin cytotoxicity in human breast cancer cells. Further epistasis analyses in yeast showed that this suppression of doxorubicin toxicity by calcium was synergistically dependent on Rav1 and Vph2, two regulators of vacuolar-ATPase assembly; this suggests potential modulation of the calcium-doxorubicin interaction by fluctuating proton concentrations within the cellular environment. Thus, the modulatory effects of drugs or diet on calcium concentrations should be considered in doxorubicin treatment regimes.","doi":"10.1111/gtc.12346","authors":"Nguyen TT, Lim YJ, Fan MH, Jackson RA, Lim KK, Ang WH, Ban KH, Chen ES","authors_abbrev":"Nguyen TT et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2016-02-20","publication_year":"2016","canto_session_key":"a3d4e7143693a96d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-06-21 14:43:15","canto_approved_date":"2023-06-21 14:43:15","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-06-21 14:43:07","canto_added_date":"2016-02-21 01:15:13","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":43,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.15c","SPBC4F6.10","SPBC2D10.13","SPBC21B10.13c","SPAC10F6.08c","SPAC644.14c","SPAC1805.07c","SPBC19G7.10c","SPBC16A3.07c","SPBC2F12.12c","SPBC16H5.13","SPBC18H10.02","SPAC8E11.02c","SPAC31G5.19","SPAC513.03","SPCC777.13","SPCC16C4.20c","SPCC757.10","SPAC1B2.04","SPBC1105.10","SPAC630.14c","SPBC28F2.10c","SPAC1952.05","SPCC24B10.08c","SPCC417.02","SPAC13C5.07","SPCC18.06c","SPAC23D3.09","SPBC32F12.08c"],"gene_count":29,"ltp_gene_count":29,"approved_date":"2023-06-21"},{"uniquename":"PMID:12796296","title":"Scw1p antagonizes the septation initiation network to regulate septum formation and cell separation in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2003 Jun;2(3):510-20","abstract":"Cytokinesis in the fission yeast Schizosaccharomyces pombe is regulated by a signaling pathway termed the septation initiation network (SIN). The SIN is essential for initiation of actomyosin ring constriction and septum formation. In a screen to search for mutations that can rescue the sid2-250 SIN mutant, we obtained scw1-18. Both the scw1-18 mutant and the scw1 deletion mutant (scw1Delta mutant), have defects in cell separation. Both the scw1-18 and scw1Delta mutations rescue the growth defects of not just the sid2-250 mutant but also the other temperature-sensitive SIN mutants. Other cytokinesis mutants, such as those defective for actomyosin ring formation, are not rescued by scw1Delta. scw1Delta does not seem to rescue the SIN by restoring SIN signaling defects. However, scw1Delta may function downstream of the SIN to promote septum formation, since scw1Delta can rescue the septum formation defects of the cps1-191beta-1,3-glucan synthase mutant, which is required for synthesis of the primary septum.","authors":"Jin QW, McCollum D","authors_abbrev":"Jin QW et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-06-11","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9G1.09","SPCC1739.11c","SPAC1565.06c","SPBC26H8.07c","SPBC244.01c","SPBC21.06c","SPCC16C4.07","SPBC24C6.07","SPBC19G7.05c","SPAC24B11.11c","SPBC428.13c"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:11337588","title":"Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.","citation":"Science 2001 May 18;292(5520):1382-5","abstract":"SCF ubiquitin ligases control various processes by marking regulatory proteins for ubiquitin-dependent proteolysis. To illuminate how SCF complexes are regulated, we sought proteins that interact with the human SCF component CUL1. The COP9 signalosome (CSN), a suppressor of plant photomorphogenesis, associated with multiple cullins and promoted cleavage of the ubiquitin-like protein NEDD8 from Schizosaccharomyces pombe CUL1 in vivo and in vitro. Multiple NEDD8-modified proteins uniquely accumulated in CSN-deficient S. pombe cells. We propose that the broad spectrum of activities previously attributed to CSN subunits--including repression of photomorphogenesis, activation of JUN, and activation of p27 nuclear export--underscores the importance of dynamic cycles of NEDD8 attachment and removal in biological regulation.","authors":"Lyapina S, Cope G, Shevchenko A, Serino G, Tsuge T, Zhou C, Wolf DA, Wei N, Shevchenko A, Deshaies RJ","authors_abbrev":"Lyapina S et al.","pubmed_publication_date":"18 May 2001","pubmed_entrez_date":"2001-05-05","publication_year":"2001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G6.12","SPBC409.05","SPBC337.08c","SPAC23H4.18c","SPAPB17E12.04c","SPBC215.03c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:23089178","title":"Sim3 shares some common roles with the histone chaperone Asf1 in fission yeast.","citation":"FEBS Lett 2012 Nov 30;586(23):4190-6","abstract":"An H3/H4 histone chaperone, Asf1, plays an essential role in maintaining genomic stability in many species, including fission yeast. Here, we showed that overexpression of a CENP-A chaperone Sim3 suppressed the temperature sensitive phenotype of asf1-33 and asf1-30 mutants and the defect in chromatin structure, and prevented the accumulation of DNA damage in asf1-33 mutants at high temperatures. Furthermore, asf1-33 and Δsim3 were synthetic lethal. Consistent with this, shutdown of sim3 expression in asf1-33 Δsim3 double mutants that contained extragenic sim3 resulted in growth retardation. In addition, the Δsim3 mutant displayed sensitivity to thiabendazol and hydroxyurea, which suggests that Sim3 plays a general role in maintaining chromatin structure. Our results suggest a possibility that Sim3 functions as a histone chaperone.","doi":"10.1016/j.febslet.2012.10.020","authors":"Tanae K, Horiuchi T, Yamakawa T, Matsuo Y, Kawamukai M","authors_abbrev":"Tanae K et al.","pubmed_publication_date":"30 Nov 2012","pubmed_entrez_date":"2012-10-24","publication_year":"2012","canto_session_key":"fff7bcd8f346ff56","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai ","canto_first_approved_date":"2015-08-17 16:21:15","canto_approved_date":"2024-01-17 20:21:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-12 01:00:33","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Makoto Kawamukai ","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC663.05c","SPBC577.15c","SPBC1105.17"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-08-17"},{"uniquename":"PMID:9439701","title":"Identification of preussin as a selective inhibitor for cell growth of the fission yeast ts mutants defective in Cdc2-regulatory genes.","citation":"J Antibiot (Tokyo) 1997 Mar;50(3):267-9","abstract":"","authors":"Kasahara K, Yoshida M, Eishima J, Takesako K, Beppu T, Horinouchi S","authors_abbrev":"Kasahara K et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10526174","title":"Functional complementation of the Schizosaccharomyces pombe wis1 mutant by Arabidopsis MEK1 and non-catalytic enhancement by CTR1.","citation":"FEBS Lett 1999 Oct 15;459(3):405-10","abstract":"Arabidopsis thaliana MEK1 encodes a MAPKK homolog whose role in plants is currently unknown. High (but not low) expression of MEK1 rescued the Deltawis1 (MAPKK) mutant of the Schizosaccharomyces pombe Win1/Wis4-Wis1-Sty1 stress-activated MAPK pathway. Rescue was dependent upon upstream and downstream components of the pathway, suggesting that MEK1 might function in a homologous MAPK pathway in plants. When MEK1 was expressed at a low level, rescue of Deltawis1 was achieved by co-expressing Arabidopsis CTR1 (a putative MAPKK kinase (MAPKKK)). CTR1 constructs alone did not rescue the pathway, indicating that CTR1 augmented MEK1 function. Further data indicated that this enhancement was not due to CTR1 kinase activity.","authors":"Pan Z, Chang C","authors_abbrev":"Pan Z et al.","pubmed_publication_date":"15 Oct 1999","pubmed_entrez_date":"1999-10-20","publication_year":"1999","canto_session_key":"80a615a94d19aeac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-06-30 09:16:46","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 09:12:32","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-30"},{"uniquename":"PMID:15774029","title":"Comparative context analysis of codon pairs on an ORFeome scale.","citation":"Genome Biol 2005;6(3):R28","abstract":"Codon context is an important feature of gene primary structure that modulates mRNA decoding accuracy. We have developed an analytical software package and a graphical interface for comparative codon context analysis of all the open reading frames in a genome (the ORFeome). Using the complete ORFeome sequences of Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida albicans and Escherichia coli, we show that this methodology permits large-scale codon context comparisons and provides new insight on the rules that govern the evolution of codon-pair context.","authors":"Moura G, Pinheiro M, Silva R, Miranda I, Afreixo V, Dias G, Freitas A, Oliveira JL, Santos MA","authors_abbrev":"Moura G et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-03-19","publication_year":"2005","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29079657","title":"TORC1 and TORC2 converge to regulate the SAGA co-activator in response to nutrient availability.","citation":"EMBO Rep 2017 Dec;18(12):2197-2218","abstract":"Gene expression regulation is essential for cells to adapt to changes in their environment. Co-activator complexes have well-established roles in transcriptional regulation, but less is known about how they sense and respond to signaling cues. We have previously shown that, in fission yeast, one such co-activator, the SAGA complex, controls gene expression and the switch from proliferation to differentiation in response to nutrient availability. Here, using a combination of genetic, biochemical, and proteomic approaches, we show that SAGA responds to nutrients through the differential phosphorylation of its Taf12 component, downstream of both the TORC1 and TORC2 pathways. Taf12 phosphorylation increases early upon starvation and is controlled by the opposing activities of the PP2A phosphatase, which is activated by TORC1, and the TORC2-activated Gad8 AKT  kinase. Mutational analyses suggest that Taf12 phosphorylation prevents cells from committing to differentiation until starvation reaches a critical level. Overall, our work reveals that SAGA is a direct target of nutrient-sensing pathways and has uncovered a mechanism by which TORC1 and TORC2 converge to control gene expression and cell fate decisions.","doi":"10.15252/embr.201744942","authors":"Laboucarié T, Detilleux D, Rodriguez-Mias RA, Faux C, Romeo Y, Franz-Wachtel M, Krug K, Maček B, Villén J, Petersen J, Helmlinger D","authors_abbrev":"Laboucarié T et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-10-29","publication_year":"2017","canto_session_key":"5bef3e6a63b5bcf4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dominique Helmlinger","canto_first_approved_date":"2019-04-04 22:31:36","canto_approved_date":"2026-04-24 06:44:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-07 15:52:33","canto_added_date":"2017-10-30 01:15:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":107,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Dominique Helmlinger","community_curator":true,"annotation_count":89,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB18E9.02c","SPAC13A11.04c","SPAC2G11.14","SPBC428.16c","SPAC4D7.10c","SPCC5E4.03c","SPCC16C4.18c","SPAC57A10.14","SPAC1952.05","SPBC6B1.12c","SPBC28F2.10c","SPBC1921.07c","SPCC61.02","SPAC823.06","SPAC22F3.13","SPCC188.02","SPBP16F5.03c","SPAC15A10.02","SPAC12G12.05c","SPAC630.13c","SPBC25H2.11c","SPCC63.05","SPBC21H7.02","SPBC30D10.10c","SPBC16H5.07c","SPAC27D7.03c","SPAC23G3.09","SPAC13F5.02c","SPAC24B11.06c","SPBC887.18c","SPBC15D4.14","SPBC14C8.17c","SPCC74.03c","SPAC10F6.16","SPAC227.07c","SPCC126.04c","SPCC24B10.08c","SPBC32C12.02","SPAC1002.04c","SPBC216.07c","SPAC3A12.05c","SPCC24B10.07","SPCC1259.06","SPCC285.09c","SPCC1494.02c"],"gene_count":45,"ltp_gene_count":43,"approved_date":"2019-04-04"},{"uniquename":"PMID:41101310","title":"Mitochondrial function regulates cell growth kinetics to maintain mitochondrial homeostasis.","citation":"Curr Biol 2025 Oct 15;","abstract":"Mitochondria are not produced de novo in newly divided daughter cells but are inherited from the mother cell during mitosis. While mitochondrial homeostasis is crucial for living cells, the feedback responses that maintain mitochondrial volume across generations of dividing cells remain elusive. Here, using a microfluidic yeast \"mother machine,\" we tracked several generations of fission yeast cells and observed that cell size and mitochondrial volume grew exponentially during the cell cycle. We discovered that while mitochondrial homeostasis relied on the \"sizer\" mechanism of cell size maintenance, mitochondrial function was a critical determinant of the timing of cell division; cells born with lower-than-average amounts of mitochondria grew slower and thus added more mitochondria before they divided. Thus, mitochondrial addition during the cell cycle was tailored to the volume of mitochondria at birth, such that all cells ultimately contained the same mitochondrial volume at cell division. Quantitative modeling and experiments with mitochondrial DNA-deficient rho0 cells additionally revealed that mitochondrial function was essential for driving the exponential growth of cells. Altogether, we demonstrate a central role for mitochondrial activity in dictating cellular growth rates and ensuring mitochondrial volume homeostasis.","doi":"10.1016/j.cub.2025.09.046","authors":"Chacko LA, Nakaoka H, Morris RG, Marshall WF, Ananthanarayanan V","authors_abbrev":"Chacko LA et al.","pubmed_publication_date":"15 Oct 2025","pubmed_entrez_date":"2025-10-16","publication_year":"2025","canto_session_key":"1cc6b425cd069677","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-17 23:25:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9023122","title":"PCR-mediated direct gene disruption in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1997 Mar 01;25(5):1080-1","abstract":"We have examined the feasibility and efficiency of PCR-mediated direct gene disruptions in the fission yeast Schizosaccharomyces pombe. In the present study, the S.pombe ura4+ gene was amplified by PCR with oligonucleotides that had short flanking regions ( approximately 40 bp) to the target gene. Using this purified PCR product we were able to disrupt genes in an S. pombe strain bearing aura4 deletion, with an efficiency ranging between 1 and 3% among selected transformants. The results indicated that despite S.pombe's preference for non-homologous or illegitimate recombination, even very short stretches of homologous regions could be used to target genes at a defined frequency in this organism. The successful disruption of four independent genes (sts1+, gcs1+, gsh2+and hmt1+) by this method further demonstrates that, despite the relatively low efficiency, the method is very feasible, and it's simplicity, especially when coupled to phenotype-based screening, should greatly facilitate disruption of genes in S.pombe.","authors":"Kaur R, Ingavale SS, Bachhawat AK","authors_abbrev":"Kaur R et al.","pubmed_publication_date":"01 Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36750367","title":"Aberrant association of chromatin with nuclear periphery induced by Rif1 leads to mitotic defect.","citation":"Life Sci Alliance 2023 Apr;6(4)","abstract":"The architecture and nuclear location of chromosomes affect chromatin events. Rif1, a crucial regulator of replication timing, recognizes G-quadruplex and inhibits origin firing over the 50-100-kb segment in fission yeast,  Schizosaccharomyces pombe , leading us to postulate that Rif1 may generate chromatin higher order structures inhibitory for initiation. However, the effects of Rif1 on chromatin localization in nuclei have not been known. We show here that Rif1 overexpression causes growth inhibition and eventually, cell death in fission yeast. Chromatin-binding activity of Rif1, but not recruitment of phosphatase PP1, is required for growth inhibition. Overexpression of a PP1-binding site mutant of Rif1 does not delay the S-phase, but still causes cell death, indicating that cell death is caused not by S-phase problems but by issues in other phases of the cell cycle, most likely the M-phase. Indeed, Rif1 overexpression generates cells with unequally segregated chromosomes. Rif1 overexpression relocates chromatin near nuclear periphery in a manner dependent on its chromatin-binding ability, and this correlates with growth inhibition. Thus, coordinated progression of S- and M-phases may require regulated Rif1-mediated chromatin association with the nuclear periphery.","doi":"10.26508/lsa.202201603","authors":"Kanoh Y, Ueno M, Hayano M, Kudo S, Masai H","authors_abbrev":"Kanoh Y et al.","pubmed_publication_date":"Apr 2023","pubmed_entrez_date":"2023-02-07","publication_year":"2023","canto_session_key":"d7b4b1693697f1fb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-02-09 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7748486","title":"Schizosaccharomyces pombe: a model for molecular studies of eukaryotic genes.","citation":"DNA Cell Biol 1995 May;14(5):359-71","abstract":"Several features of the fission yeast Schizosaccharomyces pombe make it exceptionally well suited for the study of eukaryotic genes. It is a relatively simple eukaryote that can be readily grown and manipulated in the laboratory, using a variety of highly developed and sophisticated methodologies. Schizosaccharomyces pombe cells share many molecular, genetic, and biochemical features with cells from multicellular organisms, making it a particularly useful model to study the structure, function, and regulation of genes from more complex species. For examples, this yeast divides by binary fission, has many genes that contain introns, is capable of using mammalian gene promoters and polyadenylation signals, and has been used to clone mammalian genes by functional complementation of mutants. We present a summary of the biology of S. pombe, useful features that make it amenable to laboratory studies, and molecular techniques available to manipulate the genome of this organism as well as other eukaryotic genes within the fission yeast cellular environment.","authors":"Zhao Y, Lieberman HB","authors_abbrev":"Zhao Y et al.","pubmed_publication_date":"May 1995","pubmed_entrez_date":"1995-05-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22064471","title":"Physical breakdown of the nuclear envelope is not necessary for breaking its barrier function.","citation":"Nucleus 2011;2(6):523-6","abstract":"During mitosis in higher eukaryotic cells, nuclear envelope breakdown (NEBD) occurs and leads to the disassembly of the nuclear membrane and nuclear pore complexes (NPC). This brings about a mixing of nuclear and cytoplasmic macromolecules (open mitosis). On the other hand, in many fungi, mitosis occurs without NEBD (closed mitosis). In a recent study, we reported a novel phenomenon in a closed mitosis organism, Schizosaccharomyces pombe: mixing of nuclear and cytoplasmic proteins occurred in meiosis without breakdown of the nuclear membrane or disassembly of nuclear pore complexes. We designated this event virtual nuclear envelope breakdown (V-NEBD). The key event in V-NEBD is nuclear translocation of Rna1, a RanGAP1 homologue in S. pombe. This leads to collapse of the Ran-GTP gradient across the nuclear envelope (NE) and occurs coincidently with V-NEBD. Thus, the barrier function of the NE can be abated without its physical breakdown through modulation of the Ran-GTP gradient.","doi":"10.4161/nucl.2.6.16117","authors":"Asakawa H, Hiraoka Y, Haraguchi T","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-11-09","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12419233","title":"Increased recombination intermediates and homologous integration hot spots at DNA replication origins.","citation":"Mol Cell 2002 Oct;10(4):907-16","abstract":"We have studied the relationship between DNA replication and recombination in Schizosaccharomyces pombe using two-dimensional gel electrophoresis and functional analysis. Our results indicate that the activation of replication origins (ORIs) during the mitotic cell cycle is associated with the generation of joint DNA molecules between sister chromatids. The frequency of integration by homologous recombination was up to 50-fold higher than the genomic average within a narrow window overlapping the ars1 replication initiation site. The S. pombe rad22Delta, rhp51Delta, and rhp54Delta mutants, deficient in mitotic recombination, activate ORIs very inefficiently and accumulate abnormal replication intermediates. These results focus on the general link between replication and recombination previously found in several systems and suggest a role for recombination in the initiation of eukaryotic DNA replication.","authors":"Segurado M, Gómez M, Antequera F","authors_abbrev":"Segurado M et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-11-07","publication_year":"2002","canto_session_key":"11c3ac215c375cc3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-08-21 09:03:45","canto_approved_date":"2024-08-21 09:03:45","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-21 09:03:39","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPAC15A10.03c","SPAC644.14c"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2024-08-21"},{"uniquename":"PMID:21377093","title":"Cell cycle: who turns the crank?","citation":"Curr Biol 2011 Mar 08;21(5):R185-7","abstract":"The oscillating activity of a single CDK-cyclin fusion protein can drive the orderly progression of yeast cells through DNA replication, mitosis and cell division.","doi":"10.1016/j.cub.2011.01.042","authors":"Tyson JJ, Novak B","authors_abbrev":"Tyson JJ et al.","pubmed_publication_date":"08 Mar 2011","pubmed_entrez_date":"2011-03-08","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21295003","title":"A chemical compound for controlled expression of nmt1-driven gene in the fission yeast Schizosaccharomyces pombe.","citation":"Anal Biochem 2011 May 15;412(2):159-64","abstract":"The fission yeast Schizosaccharomyces pombe is a useful model organism for studying a variety of eukaryotic cellular events such as the cell cycle control mechanisms. For inducible expression of exogenous genes in S. pombe, vectors carrying the nmt1 (no message in thiamine 1) promoter are most commonly used. Although nmt1 is a potent promoter, its transcription activity is drastically repressed in the presence of a low concentration of thiamine. Therefore, a combination of thiamine and nmt1 promoter is convenient for regulating gene expression in an all-or-none fashion. However, it has been difficult to adjust the nmt1 promoter activity in a controlled manner. Here we describe a chemical compound, designated as YAM2, whose repressive activity on the nmt1 promoter has a wider linear range than thiamine. Expression of exogenous proteins, such as human immunodeficiency virus type 1 Vpr and jellyfish green fluorescent protein, driven by the nmt1 promoter is gradually repressed by YAM2 in a dose-dependent manner. YAM2 does not exhibit a detectable level of cytotoxicity at a concentration required to fully repress the nmt1 promoter. The compound may serve as a useful tool for controlled expression of the nmt1-driven gene in S. pombe.","doi":"10.1016/j.ab.2011.01.039","authors":"Nakamura Y, Arai A, Takebe Y, Masuda M","authors_abbrev":"Nakamura Y et al.","pubmed_publication_date":"15 May 2011","pubmed_entrez_date":"2011-02-08","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23193295","title":"Transposon integration enhances expression of stress response genes.","citation":"Nucleic Acids Res 2013 Jan;41(2):775-89","abstract":"Transposable elements possess specific patterns of integration. The biological impact of these integration profiles is not well understood. Tf1, a long-terminal repeat retrotransposon in Schizosaccharomyces pombe, integrates into promoters with a preference for the promoters of stress response genes. To determine the biological significance of Tf1 integration, we took advantage of saturated maps of insertion activity and studied how integration at hot spots affected the expression of the adjacent genes. Our study revealed that Tf1 integration did not reduce gene expression. Importantly, the insertions activated the expression of 6 of 32 genes tested. We found that Tf1 increased gene expression by inserting enhancer activity. Interestingly, the enhancer activity of Tf1 could be limited by Abp1, a host surveillance factor that sequesters transposon sequences into structures containing histone deacetylases. We found the Tf1 promoter was activated by heat treatment and, remarkably, only genes that themselves were induced by heat could be activated by Tf1 integration, suggesting a synergy of Tf1 enhancer sequence with the stress response elements of target promoters. We propose that the integration preference of Tf1 for the promoters of stress response genes and the ability of Tf1 to enhance the expression of these genes co-evolved to promote the survival of cells under stress.","doi":"10.1093/nar/gks1185","authors":"Feng G, Leem YE, Levin HL","authors_abbrev":"Feng G et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2012-11-30","publication_year":"2013","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-12-03 14:05:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32554481","title":"Communication between Cyclin-dependent kinase Cdc2 and the Wis1-Spc1 MAPK pathway determines mitotic timing in  Schizosaccharomyces pombe .","citation":"Biol Open 2020 Jul 21;9(7)","abstract":"Checkpoint activation and gene expression modulation represent key determinants of cellular survival in adverse conditions. The former is regulated by cyclin-dependent kinases (CDKs) while the latter can be controlled by mitogen-activated protein kinases (MAPKs). Association between cell-cycle progression and MAPK-dependent gene expression exists in cells growing in optimal environments. While MAPK-mediated regulation of the cell cycle is well characterised, the reciprocal influence of mitotic CDK on stress response is not well studied. We present evidence that CDK activity can regulate the extent of MAPK activation in  Schizosaccharomyces pombe  cells. We show that increasing or decreasing mitotic CDK (Cdc2) activity in  S. pombe  cells can affect the activation of stress responsive MAPK (Spc1) even in the absence of stress stimuli. Our results indicate that the strong correlation between Cdc2 activity and Spc1 MAPK-activity in  S. pombe  is important in regulating mitotic timing.This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/bio.053322","authors":"Ghosal A, Sarkar P, Sundaram G","authors_abbrev":"Ghosal A et al.","pubmed_publication_date":"21 Jul 2020","pubmed_entrez_date":"2020-06-20","publication_year":"2020","canto_session_key":"90c1475c7b7285bc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-06-21 00:15:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC887.22","SPBC409.07c","SPBC11B10.09","SPAC8E11.02c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:26486373","title":"Cellular economy in fission yeast cells continuously cultured with limited nitrogen resources.","citation":"Sci Rep 2015 Oct 21;5:15617","abstract":"In ribosome biogenesis, a large fraction of ribosomes is used for producing ribosomal proteins themselves. Here, we applied simulation and experimentation to determine what fraction of ribosomes should be allocated for the synthesis of ribosomal proteins to optimize cellular economy for growth. We define the \"r-fraction\" as the fraction of mRNA of the ribosomal protein genes out of the total mRNA, and we simulated the effect of the r-fraction on the number of ribosomes. We then empirically measured the amount of protein and RNA in fission yeast cells cultured with high and low nitrogen sources. In the cells cultured with a low nitrogen source, the r-fraction decreased from 0.46 to 0.42 with a 40% reduction of rRNA, but the reduction of the total protein was smaller at 30%. These results indicate that the r-fraction is internally controlled to optimize the efficiency of protein synthesis at a limited cellular cost.","doi":"10.1038/srep15617","authors":"Chikashige Y, Arakawa S, Leibnitz K, Tsutsumi C, Mori C, Osakada H, Murata M, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"21 Oct 2015","pubmed_entrez_date":"2015-10-22","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-10-23 00:19:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27320927","title":"Rif1 Regulates the Fate of DNA Entanglements during Mitosis.","citation":"Cell Rep 2016 Jun 28;16(1):148-160","abstract":"Clearance of entangled DNA from the anaphase mid-region must accurately proceed in order for chromosomes to segregate with high fidelity. Loss of Taz1 (fission yeast ortholog of human TRF1/TRF2) leads to stalled telomeric replication forks that trigger telomeric entanglements; the resolution of these entanglements fails at ≤20°C. Here, we investigate these entanglements and their promotion by the conserved replication/repair protein Rif1. Rif1 plays no role in taz1Δ fork stalling. Rather, Rif1 localizes to the anaphase mid-region and regulates the resolution of persisting DNA structures. This anaphase role for Rif1 is genetically separate from the role of Rif1 in S/G2, though both roles require binding to PP1 phosphatase, implying spatially and temporally distinct Rif1-regulated phosphatase substrates. Rif1 thus acts as a double-edged sword. Although it inhibits the resolution of taz1Δ telomere entanglements, it promotes the resolution of non-telomeric ultrafine anaphase bridges at ≤20°C. We suggest a unifying model for Rif1's seemingly diverse roles in chromosome segregation in eukaryotes.","doi":"10.1016/j.celrep.2016.05.077","authors":"Zaaijer S, Shaikh N, Nageshan RK, Cooper JP","authors_abbrev":"Zaaijer S et al.","pubmed_publication_date":"28 Jun 2016","pubmed_entrez_date":"2016-06-21","publication_year":"2016","canto_session_key":"dc3c25bebb39928d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-06-22 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.17","SPAC16A10.07c","SPBC776.12c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:41111104","title":"Monitoring Local Chromatin Dynamics Regulated by SMC Complexes in Fission Yeast.","citation":"Methods Mol Biol 2026;2991:83-91","abstract":"Structural maintenance of chromosomes (SMC) complexes organize genome architecture throughout the cell cycle. Condensin, a member of the SMC complex family, engages chromatin loci by embracing chromatin within its ring and constrains the dynamics of chromatin fiber to shape mitotic chromosomes. To understand how condensin constrains chromatin dynamics, it is crucial to monitor the mobility of chromatin fiber with high temporal and spatial resolution. Here, I describe a step-by-step protocol to record the dynamics of chromatin locus visualized using the LacO/LacI system in fission yeast, followed by the determination of its physical properties. This method is applicable not only for monitoring the dynamics of chromatin fiber but also for tracking various types of particles in living cells.","doi":"10.1007/978-1-0716-5005-9_5","authors":"Kakui Y","authors_abbrev":"Kakui Y","pubmed_publication_date":"2026","pubmed_entrez_date":"2025-10-19","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-10-20 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12604790","title":"The Cdc23 (Mcm10) protein is required for the phosphorylation of minichromosome maintenance complex by the Dfp1-Hsk1 kinase.","citation":"Proc Natl Acad Sci U S A 2003 Mar 04;100(5):2334-9","abstract":"Previous studies in Saccharomyces cerevisiae have defined an essential role for the Dbf4-Cdc7 kinase complex in the initiation of DNA replication presumably by phosphorylation of target proteins, such as the minichromosome maintenance (Mcm) complex. We have examined the phosphorylation of the Mcm complex by the Dfp1-Hsk1 kinase, the Schizosaccharomyces pombe homologue of Dbf4-Cdc7. In vitro, the purified Dfp1-Hsk1 kinase efficiently phosphorylated Mcm2p. In contrast, Mcm2p, present in the six-subunit Mcm complex, was a poor substrate of this kinase and required Cdc23p (homologue of Mcm10p) for efficient phosphorylation. In the presence of Cdc23p, Dfp1-Hsk1 phosphorylated the Mcm2p and Mcm4p subunits of the Mcm complex. Cdc23p interacted with both the Mcm complex and Dfp1-Hsk1 by selectively binding to the Mcm467 subunits and Dfp1p, respectively. The N terminus of Cdc23p was found to interact directly with Dfp1-Hsk1 and was essential for phosphorylation of the Mcm complex. Truncated derivatives of Cdc23p that complemented the temperature-sensitive phenotype of cdc23 mutant cells also stimulated the phosphorylation of Mcm complex, implying that this activity might be a critical role of Cdc23p in vivo. These results suggest that Cdc23p participates in the activation of prereplicative complex by recruiting the Dfp1-Hsk1 kinase and stimulating the phosphorylation of the Mcm complex.","authors":"Lee JK, Seo YS, Hurwitz J","authors_abbrev":"Lee JK et al.","pubmed_publication_date":"04 Mar 2003","pubmed_entrez_date":"2003-02-27","publication_year":"2003","canto_session_key":"a67f3e355eafcf32","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-06-01 18:50:09","canto_approved_date":"2021-11-02 13:35:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-03 13:47:46","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":39,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.10","SPBC776.12c","SPCC1682.02c","SPBC14C8.07c","SPCC16A11.17","SPBC4.04c","SPBC428.18","SPBP23A10.13","SPCC550.13"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2018-06-01"},{"uniquename":"PMID:37002018","title":"Mechanistic insights into Schizosaccharomyces pombe GT-A family protein Pvg3 in the biosynthesis of pyruvylated β1,3-galactose of N-linked oligosaccharides.","citation":"J Biosci Bioeng 2023 Jun;135(6):423-432","abstract":"N-linked oligosaccharides in the fission yeast Schizosaccharomyces pombe contain large amounts of d-galactose (Gal), which mainly comprises α1,2- and α1,3-linked Gal except for pyruvylated β1,3-linked Gal (PvGalβ) at the non-reducing end. The PvGalβ unit of N-glycans is important for regulating nonsexual flocculation and invasive growth, but the mechanistic basis for β-galactosylation in fission yeast is poorly understood. To gain insight into this mechanism, we have characterized three genes previously identified to be involved in PvGalβ biosynthesis (pvg2, pvg3, and pvg5), with a focus on pvg3, which is predicted to contain a domain conserved in galactosyltransferase family 31 (GT31) proteins. Fluorescent microscopy revealed that Pvg3 is stably localized at the Golgi membrane, regardless of the presence of pvg2 +  or pvg5 + , suggesting that Pvg2 and Pvg5 are essential for the function of Pvg3 as a β1,3-galactosyltransferase, and not for its localization to the Golgi. Mutation of the GT31 family DXD motif and GT-A fold in Pvg3 resulted in loss of catalytic activity in vivo, supporting the idea that Pvg3 is a GT-A type β1,3-galactosyltransferase. Docking simulations further indicated that Pvg3 can recognize donor and acceptor substrates suitable for β-(1→3) bond formation. Yeast two-hybrid assay showed that Pvg5 physically interacts with Pvg3 and the pyruvyltransferase Pvg1. Collectively, these results provide insight into β-galactosylation catalyzed by Pvg3 and the supporting role of Pvg5 in PvGalβ biosynthesis.","doi":"10.1016/j.jbiosc.2023.03.002","authors":"Fukunaga T, Watanabe M, Nakamichi Y, Morita T, Higuchi Y, Maekawa H, Takegawa K","authors_abbrev":"Fukunaga T et al.","pubmed_publication_date":"Jun 2023","pubmed_entrez_date":"2023-03-31","publication_year":"2023","canto_session_key":"a1b70808fdad4f17","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-04-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD272","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11820777","title":"Isolation and characterization of a novel F-box protein Pof10 in fission yeast.","citation":"Biochem Biophys Res Commun 2002 Feb 08;290(5):1399-407","abstract":"The SCF complex is a type of ubiquitin-protein ligase (E3) that consists of invariable components, including Skp1, Cdc53/Cul1, and Rbx1, as well as variable components known as F-box proteins. Using a yeast two-hybrid system, we isolated six proteins that interact with Schizosaccharomyces pombe Skp1. Among them, Pof10 is a novel F-box protein consisting of 662 amino acids, harboring the F-box domain required for the binding to Skp1 and followed by four WD40 repeats. Overexpression of Pof10 in fission yeast resulted in loss of viability with marked morphological changes that are similar to those in pop1 mutant yeast. Coexpression of Skp1 with Pof10 prevented the lethality, suggesting that the lethality from Pof10 overexpression results from the sequestration of Skp1 from other F-box proteins including Pop1. Whereas most F-box proteins show rapid turnover, Pof10 has a remarkably long half-life in vivo and has been shown to be localized predominantly in cytoplasm. These results suggest that the stable F-box protein Pof10 might target abundant cytoplasmic proteins for degradation in fission yeast.","authors":"Ikebe C, Kominami K, Toda T, Nakayama K","authors_abbrev":"Ikebe C et al.","pubmed_publication_date":"08 Feb 2002","pubmed_entrez_date":"2002-02-01","publication_year":"2002","canto_session_key":"52e15d3990f414f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-20 15:14:02","canto_approved_date":"2022-02-01 22:57:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-20 15:13:54","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.02c","SPAC57A10.05c","SPBC409.05","SPBC365.06","SPBC1703.06","SPBC36.07","SPAPYUG7.02c","SPBC1539.01c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-05-20"},{"uniquename":"PMID:9689051","title":"Identification of a putative alpha-glucan synthase essential for cell wall construction and morphogenesis in fission yeast.","citation":"Proc Natl Acad Sci U S A 1998 Aug 04;95(16):9161-6","abstract":"The cell wall protects fungi against lysis and determines their cell shape. Alpha-glucan is a major carbohydrate component of the fungal cell wall, but its function is unknown and its synthase has remained elusive. Here, we describe a fission yeast gene, ags1(+), which encodes a putative alpha-glucan synthase. In contrast to the structure of other carbohydrate polymer synthases, the predicted Ags1 protein consists of two probable catalytic domains for alpha-glucan assembly, namely an intracellular domain for alpha-glucan synthesis and an extracellular domain speculated to cross-link or remodel alpha-glucan. In addition, the predicted Ags1 protein contains a multipass transmembrane domain that might contribute to transport of alpha-glucan across the membrane. Loss of Ags1p function in a temperature-sensitive mutant results in cell lysis, whereas mutant cells grown at the semipermissive temperature contain decreased levels of cell wall alpha-glucan and fail to maintain rod shapes, causing rounding of the cells. These findings demonstrate that alpha-glucan is essential for fission yeast morphogenesis.","authors":"Hochstenbach F, Klis FM, van den Ende H, van Donselaar E, Peters PJ, Klausner RD","authors_abbrev":"Hochstenbach F et al.","pubmed_publication_date":"04 Aug 1998","pubmed_entrez_date":"1998-08-05","publication_year":"1998","canto_session_key":"79910200d838ab70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-09-10 16:31:48","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-10 16:31:41","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1281.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-10"},{"uniquename":"PMID:1644270","title":"Nuclear mutations in the petite-negative yeast Schizosaccharomyces pombe allow growth of cells lacking mitochondrial DNA.","citation":"Genetics 1992 Jun;131(2):255-60","abstract":"The fission yeast Schizosaccharomyces pombe has never been found to give rise to viable cells totally lacking mitochondrial DNA (rho(o)). This paper describes the isolation of rho(o) strains of S. pombe by very long term incubation of cells in liquid medium containing glucose, potassium acetate and ethidium bromide. Once isolated, the rho(o) strains did not require potassium acetate or any other novel growth factors. These nonrespiring strains contained no mitochondrial DNA (mtDNA) detectable either by gel-blot hybridization using as probe a clone containing the entire S. pombe mtDNA, or by 1',6-diamidino-2-phenylindole staining of whole cells. Induction of rho(o) derivatives of standard laboratory strains was not reproducible from culture to culture. The cause of this irreproducibility appears to be that growth of the rho(o) strains of S. pombe depended on nuclear mutations that occurred in some, but not all, of the initial cultures. Two independent rho(o) isolates contained mutations in unlinked genes, termed ptp1-1 and ptp2-1. These mutations allowed reproducible ethidium bromide induction of viable rho(o) strains. No other phenotypes were associated with ptp mutations in rho+ strains.","authors":"Haffter P, Fox TD","authors_abbrev":"Haffter P et al.","pubmed_publication_date":"Jun 1992","pubmed_entrez_date":"1992-06-01","publication_year":"1992","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23314747","title":"Myb-domain protein Teb1 controls histone levels and centromere assembly in fission yeast.","citation":"EMBO J 2013 Feb 06;32(3):450-60","abstract":"The TTAGGG motif is common to two seemingly unrelated dimensions of chromatin function-the vertebrate telomere repeat and the promoter regions of many Schizosaccharomyces pombe genes, including all of those encoding canonical histones. The essential S. pombe protein Teb1 contains two Myb-like DNA binding domains related to those found in telomere proteins and binds the human telomere repeat sequence TTAGGG. Here, we analyse Teb1 binding throughout the genome and the consequences of reduced Teb1 function. Chromatin immunoprecipitation (ChIP)-on-chip analysis reveals robust Teb1 binding at many promoters, notably including all of those controlling canonical histone gene expression. A hypomorphic allele, teb1-1, confers reduced binding and reduced levels of histone transcripts. Prompted by previously suggested connections between histone expression and centromere identity, we examined localization of the centromeric histone H3 variant Cnp1 and found reduced centromeric binding along with reduced centromeric silencing. These data identify Teb1 as a master regulator of histone levels and centromere identity.","doi":"10.1038/emboj.2012.339","authors":"Valente LP, Dehé PM, Klutstein M, Aligianni S, Watt S, Bähler J, Cooper JP","authors_abbrev":"Valente LP et al.","pubmed_publication_date":"06 Feb 2013","pubmed_entrez_date":"2013-01-15","publication_year":"2013","canto_session_key":"1dfcad20e9ecff36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nadeem Shaikh","canto_first_approved_date":"2018-03-01 14:02:24","canto_approved_date":"2023-12-31 11:22:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-01 12:40:55","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Nadeem Shaikh","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.02","SPAC13G7.10","SPBC800.13","SPAC1834.04","SPBC1105.11c","SPBC8D2.04","SPAC1687.20c","SPCC290.04","SPBC11B10.10c","SPBC1105.17","SPAC4A8.04"],"gene_count":11,"ltp_gene_count":2,"approved_date":"2018-03-01"},{"uniquename":"EMBL:AU009400","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21655279","title":"The essential functions of NEDD8 are mediated via distinct surface regions, and not by polyneddylation in Schizosaccharomyces pombe.","citation":"PLoS One 2011;6(5):e20089","abstract":"The ubiquitin-like protein NEDD8 is highly conserved in eukaryotes, from man to Schizosaccharomyces pombe. NEDD8 conjugation to cullin proteins is a prerequisite for cullin based E3 ubiquitin ligase activity, and essential for S. pombe viability. Here, we have performed alanine scanning mutagenesis of all conserved surface residues and show that the majority of essential residues were located around the hydrophobic patch and the C-terminus. However, we further identified essential residues not previously reported to be involved in ubiquitin ligase regulation that importantly do not prevent Ned8p conjugation. We also find that mutation of all conserved lysine residues in Ned8p, did not affect yeast viability, suggesting that mono-neddylation is sufficient for yeast viability under most conditions.","doi":"10.1371/journal.pone.0020089","authors":"Girdwood D, Xirodimas DP, Gordon C","authors_abbrev":"Girdwood D et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-06-10","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17579515","title":"The spindle pole bodies facilitate nuclear envelope division during closed mitosis in fission yeast.","citation":"PLoS Biol 2007 Jul;5(7):e170","abstract":"Many organisms divide chromosomes within the confines of the nuclear envelope (NE) in a process known as closed mitosis. Thus, they must ensure coordination between segregation of the genetic material and division of the NE itself. Although many years of work have led to a reasonably clear understanding of mitotic spindle function in chromosome segregation, the NE division mechanism remains obscure. Here, we show that fission yeast cells overexpressing the transforming acid coiled coil (TACC)-related protein, Mia1p/Alp7p, failed to separate the spindle pole bodies (SPBs) at the onset of mitosis, but could assemble acentrosomal bipolar and antiparallel spindle structures. Most of these cells arrested in anaphase with fully extended spindles and nonsegregated chromosomes. Spindle poles that lacked the SPBs did not lead the division of the NE during spindle elongation, but deformed it, trapping the chromosomes within. When the SPBs were severed by laser microsurgery in wild-type cells, we observed analogous deformations of the NE by elongating spindle remnants, resulting in NE division failure. Analysis of dis1Delta cells that elongate spindles despite unattached kinetochores indicated that the SPBs were required for maintaining nuclear shape at anaphase onset. Strikingly, when the NE was disassembled by utilizing a temperature-sensitive allele of the Ran GEF, Pim1p, the abnormal spindles induced by Mia1p overexpression were capable of segregating sister chromatids to daughter cells, suggesting that the failure to divide the NE prevents chromosome partitioning. Our results imply that the SPBs preclude deformation of the NE during spindle elongation and thus serve as specialized structures enabling nuclear division during closed mitosis in fission yeast.","authors":"Zheng L, Schwartz C, Magidson V, Khodjakov A, Oliferenko S","authors_abbrev":"Zheng L et al.","pubmed_publication_date":"Jul 2007","pubmed_entrez_date":"2007-06-21","publication_year":"2007","canto_session_key":"8b6f74049ec3405d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-02-09 12:35:34","canto_approved_date":"2025-12-23 12:38:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-23 21:27:23","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPAC890.02c","SPBC557.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-02-09"},{"uniquename":"EMBL:SPD252","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8467507","title":"Yeast cells can enter a quiescent state through G1, S, G2, or M phase of the cell cycle.","citation":"Cancer Res 1993 Apr 15;53(8):1867-70","abstract":"We have examined the ability of the yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae to enter a quiescent state through G1, S, G2, or M phase of the cell cycle. We monitored entry to a quiescent state by measuring two well known properties of quiescent cells, i.e., long-term viability and a dramatic increase in resistance to thermal heat shock relative to cycling cells. For this purpose, we made use of yeast cell division cycle (cdc) mutants with which we could arrest most of the cells in culture at specific points in the cell cycle. We find that these eukaryotes can enter a reversible quiescent state at any of the points in the cell cycle we examined if the cells are exposed to starvation conditions (starvation normally signals cells to leave the cell cycle). These findings indicate that mechanisms involved in entry to and exit from a quiescent state can operate not only in G1 phase (leading to G0 arrested cells) but can also operate in S, G2, and M phases of the cell cycle. These findings may be important for clinical oncology in cases where tumor cells escape the cytotoxic effects of chemotherapeutic agents. It may be that escape from the effect of these drugs is due to tumor cells entering quiescent states at points in the cell cycle other than G1 phase. Perhaps different chemotherapeutic strategies may be required to kill tumor cells reentering the cell cycle from other than G1.","authors":"Wei W, Nurse P, Broek D","authors_abbrev":"Wei W et al.","pubmed_publication_date":"15 Apr 1993","pubmed_entrez_date":"1993-04-15","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013381","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28148852","title":"Small-Scale Immunoprecipitation from Fission Yeast Cell Extracts.","citation":"Cold Spring Harb Protoc 2017 Feb 01;2017(2)","abstract":"We describe procedures for the immunoprecipitation (IP) of a molecule of interest from cell extracts under native or denaturing conditions. The methods are equally effective with antibodies that directly recognize the molecule of interest and those that recognize a generic peptide \"epitope tag\" that has been fused to sequences encoding the gene of interest. The diverse chemistry of intermolecular interactions and enzymatic activities means that a range of different buffer conditions must be assessed empirically to identify optimal conditions for the study of a specific target/complex in a particular assay. We describe three buffers that can serve as starting points for this empirical testing and discuss modifications that are commonly used in the optimization of assays based on immunoprecipitation.","doi":"10.1101/pdb.prot091587","authors":"Grallert A, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"01 Feb 2017","pubmed_entrez_date":"2017-02-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-02-04 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7862522","title":"The fission yeast gene pmt1+ encodes a DNA methyltransferase homologue.","citation":"Nucleic Acids Res 1995 Jan 25;23(2):203-10","abstract":"DNA methylation of cytosine residues is a widespread phenomenon and has been implicated in a number of biological processes in both prokaryotes and eukaryotes. This methylation occurs at the 5-position of cytosine and is catalyzed by a distinct family of conserved enzymes, the cytosine-5 methyltransferases (m5C-MTases). We have cloned a fission yeast gene pmt1+ (pombe methyltransferase) which encodes a protein that shares significant homology with both prokaryotic and eukaryotic m5C-MTases. All 10 conserved domains found in these enzymes are present in the pmt1 protein. This is the first m5C-MTase homologue cloned from a fungal species. Its presence is surprising, given the inability to detect DNA methylation in yeasts. Haploid cells lacking the pmt1+ gene are viable, indicating that pmt1+ is not an essential gene. Purified, bacterially produced pmt1 protein does not possess obvious methyltransferase activity in vitro. Thus the biological significance of the m5C-MTase homologue in fission yeast is currently unclear.","authors":"Wilkinson CR, Bartlett R, Nurse P, Bird AP","authors_abbrev":"Wilkinson CR et al.","pubmed_publication_date":"25 Jan 1995","pubmed_entrez_date":"1995-01-25","publication_year":"1995","canto_session_key":"c57f22a897472fa7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-25 11:04:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-13 03:04:33","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-13"},{"uniquename":"PMID:17332744","title":"Recruitment of P-TEFb (Cdk9-Pch1) to chromatin by the cap-methyl transferase Pcm1 in fission yeast.","citation":"EMBO J 2007 Mar 21;26(6):1552-9","abstract":"Capping of nascent pre-mRNAs is thought to be a prerequisite for productive elongation and associated serine 2 phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (PolII). The mechanism mediating this link is unknown, but is likely to include the capping machinery and P-TEPb. We report that the fission yeast P-TEFb (Cdk9-Pch1) forms a complex with the cap-methyltransferase Pcm1 and these proteins colocalise on chromatin. Ablation of Cdk9 function through chemical genetics causes growth arrest and abolishes serine 2 phosphorylation on the PolII CTD. Strikingly, depletion of Pcm1 also leads to a dramatic decrease of phospho-serine 2. Chromatin immunoprecipitations show a severe decrease of chromatin-bound Cdk9-Pch1 when Pcm1 is depleted. On the contrary, Cdk9 is not required for association of Pcm1 with chromatin. Furthermore, compromising Cdk9 activity leads to a promoter-proximal PolII stalling and sensitivity to 6-azauracil, reflecting elongation defects. The in vivo data presented here strongly support the existence of a molecular mechanism where the cap-methyltransferase recruits P-TEFb to chromatin, thereby ensuring that only properly capped transcripts are elongated.","authors":"Guiguen A, Soutourina J, Dewez M, Tafforeau L, Dieu M, Raes M, Vandenhaute J, Werner M, Hermand D","authors_abbrev":"Guiguen A et al.","pubmed_publication_date":"21 Mar 2007","pubmed_entrez_date":"2007-03-03","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5123876","title":"The substrate specificity of purine phosphoribosyltransferases in Schizosaccharomyces pombe.","citation":"Biochem J 1971 May;122(4):415-20","abstract":"1. The activities of the purine phosphoribosyltransferases (EC 2.4.2.7 and 2.4.2.8) in purine-analogue-resistant mutants of Schizosaccharomyces pombe were checked. An 8-azathioxanthine-resistant mutant lacked hypoxanthine phosphoribosyltransferase, xanthine phosphoribosyltransferase and guanine phosphoribosyltransferase activities (EC 2.4.2.8) and appeared to carry a single mutation. Two 2,6-diaminopurine-resistant mutants retained these activities but lacked adenine phosphoribosyltransferase activity (EC 2.4.2.7). This evidence, together with data on purification and heat-inactivation patterns of phosphoribosyltransferase activities towards the various purines, strongly suggests that there are two phosphoribosyltransferase enzymes for purine bases in Schiz. pombe, one active with adenine, the other with hypoxanthine, xanthine and guanine. 2. Neither growth-medium supplements of purines nor mutations on genes involved in the pathway for new biosynthesis of purine have any influence on the amount of hypoxanthine-xanthine-guanine phosphoribosyltransferase produced by this organism.","authors":"De Groodt A, Whitehead EP, Heslot H, Poirier L","authors_abbrev":"De Groodt A et al.","pubmed_publication_date":"May 1971","pubmed_entrez_date":"1971-05-01","publication_year":"1971","canto_session_key":"bc7de8f19d71ae77","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-12 09:15:10","canto_approved_date":"2018-06-12 13:39:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-11 22:45:50","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.13c","SPAC23A1.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-12"},{"uniquename":"PMID:9794810","title":"Inositol hexakisphosphate in Schizosaccharomyces pombe: synthesis from Ins(1,4,5)P3 and osmotic regulation.","citation":"Biochem J 1998 Nov 01;335 ( Pt 3)(Pt 3):671-9","abstract":"Schizosaccharomyces pombe extracts synthesize InsP6 (myo-inositol hexaphosphate) from Ins(1,4,5)P3 plus ATP. An S. pombe soluble fraction converts Ins(1,4,5)P3 into Ins(1,4,5,6)P4 and Ins(1,3,4, 5)P4, in a constant ratio of approximately 5:1, and thence to Ins(1, 3,4,5,6)P5 and InsP6. We have purified a soluble Mg2+-dependent kinase of molecular mass approximately 41 kDa that makes Ins(1,4,5, 6)P4 and Ins(1,3,4,5)P4 in the same ratio and also converts Ins(1,4, 5,6)P4 or Ins(1,3,4,5)P4 into Ins(1,3,4,5,6)P5 and InsP6. Of InsP3 isomers other than Ins(1,4,5)P3, only the non-biological molecule Ins(1,4,6)P3 potently 'competed' with all steps in conversion of Ins(1,4,5)P3 into InsP6. Examination of molecular graphics representations allowed us to draw tentative conclusions about the environment needed for an hydroxyl group to be phosphorylated by this kinase and to predict successfully that the purified kinase would phosphorylate the 5-hydroxyl of Ins(1,4,6)P3. S. pombe that have been cultured with [3H]inositol contains a variety of 3H-labelled inositol polyphosphates, with Ins(1,4,5)P3 and InsP6 the most prominent, and the InsP6 concentration quickly increases in hyper-osmotically stressed S. pombe. This yeast therefore contains InsP6 and Ins(1,4,5)P3 as normal constituents, makes more InsP6 when hyper-osmotically stressed and contains a versatile inositol polyphosphate kinase that synthesizes InsP6 from Ins(1,4,5)P3.","authors":"Ongusaha PP, Hughes PJ, Davey J, Michell RH","authors_abbrev":"Ongusaha PP et al.","pubmed_publication_date":"01 Nov 1998","pubmed_entrez_date":"1998-10-31","publication_year":"1998","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41032120","title":"Transcriptome changes of fission yeast cells exposed to fumonisin B1 or co-cultured with Fusarium verticillioides.","citation":"Appl Microbiol Biotechnol 2025 Oct 01;109(1):211","abstract":"Fusarium verticillioides poses a high food safety risk worldwide due to its mycotoxin production. Successful control of Fusaria may rely on promising biocontrol agents, including yeasts. Although the fission yeast Schizosaccharomyces pombe tolerated Fusarium mycotoxins well, including zearalenone, T2, deoxynivalenol, and fumonisins (FUMs), it did not significantly inhibit the growth of F. verticillioides. Meanwhile fumonisin B1 (FB1) supplementation did not decrease S. pombe cell density in submerged liquid cultures, the colony-forming capability of the yeast was reduced. RNA sequencing showed that S. pombe genes involved in cell adhesion and flocculation were downregulated after FB1 exposure. In addition, the expression of several hydrolase genes was also altered. In co-cultures with F. verticillioides, genes encoding oxidoreductases and hydrolases and those linked to purine nucleotide metabolisms were downregulated, while the expression of genes involved in membrane and transport processes was increased. The expression of several F. verticillioides genes also changed after co-cultivation. Oxidoreductase, transmembrane transport, and purine metabolism genes were upregulated under co-culturing; meanwhile, hydrolase genes, together with carbon metabolism and polysaccharide catabolism genes, were downregulated. Co-cultivation also decreased fumonisin production via the downregulation of genes FUM19, FUM21, and FvATFA encoding the fumonisin transporter, a local Zn(II)2Cys6-type transcriptional regulator and an important global regulator bZIP-type transcription factor, respectively. Although further experiments should clarify the mechanism of the fission yeast-elicited inhibition of fumonisin production, these results may pave the way for the development and implementation of novel, innovative approaches to control mycotoxin production by F. verticillioides in the feed and food chain. KEY POINTS: • 0.5 ppm FB1 reduced the colony-forming ability of S. pombe and caused transcriptional changes. • Expression of transport and hydrolase genes changed in yeast during co-cultivation with mold. • Two FUM cluster genes and FvATFA were downregulated in Fusarium co-cultured with S. pombe.","doi":"10.1007/s00253-025-13601-3","authors":"Papp LA, Acs-Szabo L, Kovács S, Adácsi C, Batta G, Pusztahelyi T, Pócsi I, Miklós I","authors_abbrev":"Papp LA et al.","pubmed_publication_date":"01 Oct 2025","pubmed_entrez_date":"2025-10-01","publication_year":"2025","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2025-10-01 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22521786","title":"Phosphodependent recruitment of Bub1 and Bub3 to Spc7/KNL1 by Mph1 kinase maintains the spindle checkpoint.","citation":"Curr Biol 2012 May 22;22(10):891-9","abstract":"The spindle assembly checkpoint (SAC) is the major surveillance system that ensures that sister chromatids do not separate until all chromosomes are correctly bioriented during mitosis. Components of the checkpoint include Mad1, Mad2, Mad3 (BubR1), Bub3, and the kinases Bub1, Mph1 (Mps1), and Aurora B. Checkpoint proteins are recruited to kinetochores when individual kinetochores are not bound to spindle microtubules or not under tension. Kinetochore association of Mad2 causes it to undergo a conformational change, which promotes its association to Mad3 and Cdc20 to form the mitotic checkpoint complex (MCC). The MCC inhibits the anaphase-promoting complex/cyclosome (APC/C) until the checkpoint is satisfied. SAC silencing derepresses Cdc20-APC/C activity. This triggers the polyubiquitination of securin and cyclin, which promotes the dissolution of sister chromatid cohesion and mitotic progression. We, and others, recently showed that association of PP1 to the Spc7/Spc105/KNL1 family of kinetochore proteins is necessary to stabilize microtubule-kinetochore attachments and silence the SAC. We now report that phosphorylation of the conserved MELT motifs in Spc7 by Mph1 (Mps1) recruits Bub1 and Bub3 to the kinetochore and that this is required to maintain the SAC signal.","doi":"10.1016/j.cub.2012.03.051","authors":"Shepperd LA, Meadows JC, Sochaj AM, Lancaster TC, Zou J, Buttrick GJ, Rappsilber J, Hardwick KG, Millar JB","authors_abbrev":"Shepperd LA et al.","pubmed_publication_date":"22 May 2012","pubmed_entrez_date":"2012-04-24","publication_year":"2012","canto_session_key":"0c53b7a36b2fe15f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-01-15 06:58:41","canto_approved_date":"2026-01-31 15:47:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-04 23:50:37","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":61,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.01","SPBC582.03","SPAC23H3.08c","SPCC1020.02","SPBC26H8.07c","SPCC1322.12c","SPCC1795.01c","SPBC776.02c","SPCC736.14","SPCC320.13c","SPBC20F10.06","SPBC106.01","SPAC589.08c","SPBC2F12.13","SPBC3D6.04c"],"gene_count":15,"ltp_gene_count":10,"approved_date":"2018-01-15"},{"uniquename":"PMID:21531205","title":"Multi-domain CGFS-type glutaredoxin Grx4 regulates iron homeostasis via direct interaction with a repressor Fep1 in fission yeast.","citation":"Biochem Biophys Res Commun 2011 May 20;408(4):609-14","abstract":"The fission yeast Schizosaccharomyces pombe contains two CGFS-type monothiol glutaredoxins, Grx4 and Grx5, which are localized primarily in the nucleus and mitochondria, respectively. We observed involvement of Grx4 in regulating iron-responsive gene expression, which is modulated by a repressor Fep1. Lack of Grx4 caused defects not only in growth but also in the expression of both iron-uptake and iron-utilizing genes regardless of iron availability. In order to unravel how Grx4 is involved in Fep1-mediated regulation, interaction between them was investigated. Co-immunoprecipitation and bimolecular fluorescence complementation (BiFC) revealed that Grx4 physically interacts with Fep1 in vivo. BiFC revealed localized nuclear dots produced by interaction of Grx4 with Fep1. Mutation of cysteine-172 in the CGFS motif to serine (C172S) produced effects similarly observed under Grx4 depletion, such as the loss of iron-dependent gene regulation and the absence of nuclear dots in BiFC analysis. These results suggest that the ability of Grx4 to bind iron, most likely Fe-S cofactor, could be critical in interacting with and modulating the activity of Fep1.","doi":"10.1016/j.bbrc.2011.04.069","authors":"Kim KD, Kim HJ, Lee KC, Roe JH","authors_abbrev":"Kim KD et al.","pubmed_publication_date":"20 May 2011","pubmed_entrez_date":"2011-05-03","publication_year":"2011","canto_session_key":"57ee19731b127383","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-27 12:19:25","canto_approved_date":"2022-07-22 06:43:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-27 12:19:17","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23E2.01","SPAC1F7.08","SPBC26H8.06","SPBC1683.10c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2014-10-27"},{"uniquename":"PMID:10234787","title":"Schizosaccharomyces pombe stt3+ is a functional homologue of Saccharomyces cerevisiae STT3 which regulates oligosaccharyltransferase activity.","citation":"Yeast 1999 Apr;15(6):497-505","abstract":"The Saccharomyces cerevisiae STT3 (ScSTT3) gene encodes a protein which is involved in protein glycosylation via the regulation of oligosaccharyltransferase activity. We have cloned and isolated the Schizosaccharomyces pombe STT3 homologous gene (Spstt3+). The Spstt3+ gene encodes a protein consisting of 749 amino acid residues which has significant homology with ScStt3p and the mouse Stt3p-homologue Itm1p. Disruption of the Spstt3+ gene shows that this gene is essential for growth. Like Itm1, Spstt3+ partially suppressed the temperature sensitivity of the stt3-1 mutation of S. cerevisiae, indicating that Spstt3+ is a functional and structural homologue of the ScSTT3 gene.","authors":"Yoshida S, Matsuura A, Merregaert J, Anraku Y","authors_abbrev":"Yoshida S et al.","pubmed_publication_date":"Apr 1999","pubmed_entrez_date":"1999-05-11","publication_year":"1999","canto_session_key":"6f20bc995fe43cbd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-07-12 13:14:02","canto_session_submitted_date":"2012-07-12 10:06:04","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1271.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-07-12"},{"uniquename":"PMID:27587785","title":"Analysis of the Schizosaccharomyces pombe Cell Cycle.","citation":"Cold Spring Harb Protoc 2016 Sep 01;2016(9)","abstract":"Schizosaccharomyces pombe cells are rod shaped, and they grow by tip elongation. Growth ceases during mitosis and cell division; therefore, the length of a septated cell is a direct measure of the timing of mitotic commitment, and the length of a wild-type cell is an indicator of its position in the cell cycle. A large number of documented stage-specific changes can be used as landmarks to characterize cell cycle progression under specific experimental conditions. Conditional mutations can permanently or transiently block the cell cycle at almost any stage. Large, synchronously dividing cell populations, essential for the biochemical analysis of cell cycle events, can be generated by induction synchrony (arrest-release of a cell cycle mutant) or selection synchrony (centrifugal elutriation or lactose-gradient centrifugation). Schizosaccharomyces pombe cell cycle studies routinely combine particular markers, mutants, and synchronization procedures to manipulate the cycle. We describe these techniques and list key landmarks in the fission yeast mitotic cell division cycle.","doi":"10.1101/pdb.top082800","authors":"Hagan IM, Grallert A, Simanis V","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"01 Sep 2016","pubmed_entrez_date":"2016-09-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-09-04 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27363521","title":"Still and rotating myosin clusters determine cytokinetic ring constriction.","citation":"Nat Commun 2016 Jul 01;7:11860","abstract":"The cytokinetic ring is essential for separating daughter cells during division. It consists of actin filaments and myosin motors that are generally assumed to organize as sarcomeres similar to skeletal muscles. However, direct evidence is lacking. Here we show that the internal organization and dynamics of rings are different from sarcomeres and distinct in different cell types. Using micro-cavities to orient rings in single focal planes, we find in mammalian cells a transition from a homogeneous distribution to a periodic pattern of myosin clusters at the onset of constriction. In contrast, in fission yeast, myosin clusters rotate prior to and during constriction. Theoretical analysis indicates that both patterns result from acto-myosin self-organization and reveals differences in the respective stresses. These findings suggest distinct functional roles for rings: contraction in mammalian cells and transport in fission yeast. Thus self-organization under different conditions may be a generic feature for regulating morphogenesis in vivo.","doi":"10.1038/ncomms11860","authors":"Wollrab V, Thiagarajan R, Wald A, Kruse K, Riveline D","authors_abbrev":"Wollrab V et al.","pubmed_publication_date":"01 Jul 2016","pubmed_entrez_date":"2016-07-02","publication_year":"2016","canto_session_key":"d80c0723750b689b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-03 00:16:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25838386","title":"Epigenetics. Restricted epigenetic inheritance of H3K9 methylation.","citation":"Science 2015 Apr 03;348(6230):132-5","abstract":"Posttranslational histone modifications are believed to allow the epigenetic transmission of distinct chromatin states, independently of associated DNA sequences. Histone H3 lysine 9 (H3K9) methylation is essential for heterochromatin formation; however, a demonstration of its epigenetic heritability is lacking. Fission yeast has a single H3K9 methyltransferase, Clr4, that directs all H3K9 methylation and heterochromatin. Using releasable tethered Clr4 reveals that an active process rapidly erases H3K9 methylation from tethering sites in wild-type cells. However, inactivation of the putative histone demethylase Epe1 allows H3K9 methylation and silent chromatin maintenance at the tethering site through many mitotic divisions, and transgenerationally through meiosis, after release of tethered Clr4. Thus, H3K9 methylation is a heritable epigenetic mark whose transmission is usually countered by its active removal, which prevents the unauthorized inheritance of heterochromatin.","doi":"10.1126/science.1260638","authors":"Audergon PN, Catania S, Kagansky A, Tong P, Shukla M, Pidoux AL, Allshire RC","authors_abbrev":"Audergon PN et al.","pubmed_publication_date":"03 Apr 2015","pubmed_entrez_date":"2015-04-04","publication_year":"2015","canto_session_key":"27553d3352ec591e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-06-28 12:33:35","canto_approved_date":"2025-12-19 15:44:30","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-06-27 13:00:32","canto_added_date":"2015-04-05 00:19:07","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":10,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25H1.02","SPAC23E2.02","SPAC1002.05c","SPAC343.11c","SPCC622.16c","SPBP19A11.06","SPBC146.09c","SPCC622.19"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2024-06-28"},{"uniquename":"PMID:7845361","title":"Ethanol-hypersensitive and ethanol-dependent cdc- mutants in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1994 Oct 17;245(1):86-95","abstract":"Ethanol-hypersensitive strains (ets mutants), unable to grow on media containing 6% ethanol, were isolated from a sample of mutagenized Schizosaccharomyces pombe wild-type cells. Genetic analysis of these ets strains demonstrated that the ets phenotype is associated with mutations in a large set of genes, including cell division cycle (cdc) genes, largely non-overlapping with the set represented by the temperature conditional method; accordingly, we isolated some ets non-ts cdc- mutants, which may identify novel essential genes required for regulation of the S. pombe cell cycle. Conversely, seven well characterized ts cdc- mutants were tested for their ethanol sensitivity; among them, cdc1-7 and cdc13-117 exhibited a tight ets phenotype. Ethanol sensitivity was also tested in strains bearing different alleles of the cdc2 gene, and we found that some of them were ets, but others were non-ets; thus, ethanol hypersensitivity is an allele-specific phenotype. Based on the single base changes found in each particular allele of the cdc2 gene, it is shown that a single amino acid substitution in the p34cdc2 gene product can produce this ets phenotype, and that ethanol hypersensitivity is probably due to the influence of this alcohol on the secondary and/or tertiary structure of the target protein. Ethanol-dependent (etd) mutants were also identified as mutants that can only be propagated on ethanol-containing media. This novel type of conditional phenotype also covers many unrelated genes. One of these etd mutants, etd1-1, was further characterized because of the lethal cdc- phenotype of the mutant cells under restrictive conditions (absence of ethanol). The isolation of extragenic suppressors of etd1-1, and the complementation cloning of a DNA fragment encompassing the etd1+ wild-type gene (or an extragenic multicopy suppressor) demonstrate that current genetic techniques may be applied to mutants isolated by using ethanol as a selective agent.","authors":"Jimenez J, Oballe J","authors_abbrev":"Jimenez J et al.","pubmed_publication_date":"17 Oct 1994","pubmed_entrez_date":"1994-10-17","publication_year":"1994","canto_session_key":"cde455cb3433cedb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-12-13 21:22:09","canto_approved_date":"2021-10-15 12:55:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-02-19 11:36:27","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC227.07c","SPAC1006.08","SPAC27E2.05","SPBC582.03","SPBC11B10.09"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-12-13"},{"uniquename":"PMID:33432131","title":"Experimental evolution of adaptive divergence under varying degrees of gene flow.","citation":"Nat Ecol Evol 2021 Mar;5(3):338-349","abstract":"Adaptive divergence is the key evolutionary process generating biodiversity by means of natural selection. Yet, the conditions under which it can arise in the presence of gene flow remain contentious. To address this question, we subjected 132 sexually reproducing fission yeast populations, sourced from two independent genetic backgrounds, to disruptive ecological selection and manipulated the level of migration between environments. Contrary to theoretical expectations, adaptive divergence was most pronounced when migration was either absent (allopatry) or maximal (sympatry), but was much reduced at intermediate rates (parapatry and local mating). This effect was apparent across central life-history components (survival, asexual growth and mating) but differed in magnitude between ancestral genetic backgrounds. The evolution of some fitness components was constrained by pervasive negative correlations (trade-off between asexual growth and mating), while others changed direction under the influence of migration (for example, survival and mating). In allopatry, adaptive divergence was mainly conferred by standing genetic variation and resulted in ecological specialization. In sympatry, divergence was mainly mediated by novel mutations enriched in a subset of genes and was characterized by the repeated emergence of two strategies: an ecological generalist and an asexual growth specialist. Multiple loci showed consistent evidence for antagonistic pleiotropy across migration treatments providing a conceptual link between adaptation and divergence. This evolve-and-resequence experiment shows that rapid ecological differentiation can arise even under high rates of gene flow. It further highlights that adaptive trajectories are governed by complex interactions of gene flow, ancestral variation and genetic correlations.","doi":"10.1038/s41559-020-01363-2","authors":"Tusso S, Nieuwenhuis BPS, Weissensteiner B, Immler S, Wolf JBW","authors_abbrev":"Tusso S et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2021-01-12","publication_year":"2021","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-01-14 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21979813","title":"Acetylation regulates monopolar attachment at multiple levels during meiosis I in fission yeast.","citation":"EMBO Rep 2011 Oct 28;12(11):1189-95","abstract":"In fission yeast, meiotic mono-orientation of sister kinetochores is established by cohesion at the core centromere, which is established by a meiotic cohesin complex and the kinetochore protein Moa1. The cohesin subunit Psm3 is acetylated by Eso1 and deacetylated by Clr6. We show that in meiosis, Eso1 is required for establishing core centromere cohesion during S phase, whereas Moa1 is required for maintaining this cohesion after S phase. The clr6-1 mutation suppresses the mono-orientation defect of moa1Δ cells, although the Clr6 target for this suppression is not Psm3. Thus, several acetylations are crucial for establishing and maintaining core centromere cohesion.","doi":"10.1038/embor.2011.188","authors":"Kagami A, Sakuno T, Yamagishi Y, Ishiguro T, Tsukahara T, Shirahige K, Tanaka K, Watanabe Y","authors_abbrev":"Kagami A et al.","pubmed_publication_date":"28 Oct 2011","pubmed_entrez_date":"2011-10-08","publication_year":"2011","canto_session_key":"f07cbe80a4008b28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2018-03-28 15:17:27","canto_approved_date":"2024-07-12 08:00:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-02 16:19:49","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.05c","SPAC10F6.09c","SPAC3G9.07c","SPAC15E1.07c","SPBC16A3.11","SPBC428.17c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-03-28"},{"uniquename":"PMID:26843489","title":"Mutations in EXOSC2 are associated with a novel syndrome characterised by retinitis pigmentosa, progressive hearing loss, premature ageing, short stature, mild intellectual disability and distinctive gestalt.","citation":"J Med Genet 2016 Jun;53(6):419-25","abstract":"Retinitis pigmentosa in combination with hearing loss can be a feature of different Mendelian disorders. We describe a novel syndrome caused by biallelic mutations in the 'exosome component 2' (EXOSC2) gene.\nClinical ascertainment of three similar affected patients followed by whole exome sequencing.\nThree individuals from two unrelated German families presented with a novel Mendelian disorder encompassing childhood myopia, early onset retinitis pigmentosa, progressive sensorineural hearing loss, hypothyroidism, short stature, brachydactyly, recognisable facial gestalt, premature ageing and mild intellectual disability. Whole exome sequencing revealed homozygous or compound heterozygous missense variants in the EXOSC2 gene in all three patients. EXOSC2 encodes the 'ribosomal RNA-processing protein 4' (RRP4)-one of the core components of the RNA exosome. The RNA exosome is a multiprotein complex that plays key roles in RNA processing and degradation. Intriguingly, the EXOSC2-associated phenotype shows only minimal overlap with the previously reported diseases associated with mutations in the RNA exosome core component genes EXOSC3 and EXOSC8.\nWe report a novel condition that is probably caused by altered RNA exosome function and expands the spectrum of clinical consequences of impaired RNA metabolism.","doi":"10.1136/jmedgenet-2015-103511","authors":"Di Donato N, Neuhann T, Kahlert AK, Klink B, Hackmann K, Neuhann I, Novotna B, Schallner J, Krause C, Glass IA, Parnell SE, Benet-Pages A, Nissen AM, Berger W, Altmüller J, Thiele H, Weber BH, Schrock E, Dobyns WB, Bier A, Rump A","authors_abbrev":"Di Donato N et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-02-05","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F7.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9552386","title":"Tyrosine kinases wee1 and mik1 as effectors of DNA replication checkpoint control.","citation":"Prog Cell Cycle Res 1996;2:91-7","abstract":"Cell cycle studies have revealed mechanisms that prevent cell division if DNA fails to be completely replicated or sustains damage. Here we focus on the evidence from yeast genetics that the wee1 and mik1 tyrosine kinases cooperate in the inhibitory phosphorylation of cdc2p, and the possibility that these kinases function in pathways that ensure the integrity of the genome prior to cell division. We also review the progress in cloning and analysing wee1-like tyrosine kinases from higher eukaryotes, and the evidence for and against their functioning in ensuring DNA replication prior to mitosis. Finally, we discuss the genes involved in these feedback controls and suggest that wee1p and mik1p might be the ultimate effectors that prevent mitosis when a checkpoint is triggered.","authors":"Tourret J, McKeon F","authors_abbrev":"Tourret J et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27382173","title":"Generalized nucleation and looping model for epigenetic memory of histone modifications.","citation":"Proc Natl Acad Sci U S A 2016 Jul 19;113(29):E4180-9","abstract":"Histone modifications can redistribute along the genome in a sequence-independent manner, giving rise to chromatin position effects and epigenetic memory. The underlying mechanisms shape the endogenous chromatin landscape and determine its response to ectopically targeted histone modifiers. Here, we simulate linear and looping-driven spreading of histone modifications and compare both models to recent experiments on histone methylation in fission yeast. We find that a generalized nucleation-and-looping mechanism describes key observations on engineered and endogenous methylation domains including intrinsic spatial confinement, independent regulation of domain size and memory, variegation in the absence of antagonists, and coexistence of short- and long-term memory at loci with weak and strong constitutive nucleation. These findings support a straightforward relationship between the biochemical properties of chromatin modifiers and the spatiotemporal modification pattern. The proposed mechanism gives rise to a phase diagram for cellular memory that may be generally applicable to explain epigenetic phenomena across different species.","doi":"10.1073/pnas.1605862113","authors":"Erdel F, Greene EC","authors_abbrev":"Erdel F et al.","pubmed_publication_date":"19 Jul 2016","pubmed_entrez_date":"2016-07-07","publication_year":"2016","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-08 00:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28065318","title":"In vitro reactivation of the cytokinetic contractile ring of fission yeast cells.","citation":"Methods Cell Biol 2017;137:387-394","abstract":"Cytokinesis is a process by which a mother cell is divided into two daughter cells after chromosome segregation. In both animal and fungal cells, cytokinesis is carried out by the constriction of the contractile ring made up of actin, myosin-II, and other conserved proteins. Detailed genetic and cell biological analysis of cytokinesis has led to the identification of various genes involved in the process of cytokinesis including the cytological description of the process. However, detailed biochemical analysis of the process is lacking. Critical questions that aim to understand aspects, such as the organization of actin and myosin in the contractile ring, the architecture of the ring, and the molecular process of ring contraction, remain unanswered. We have developed a method to address these aspects of cytokinesis. Using the fission yeast Schizosaccharomyces pombe, we present a method whereby cell-ghosts containing functional contractile rings can be isolated and used to perform various biochemical analysis as well as detailed electron microscopy studies.","doi":"10.1016/bs.mcb.2016.03.037","authors":"Mabuchi I, Kashiwazaki J, Mishra M","authors_abbrev":"Mabuchi I et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-01-10","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-01-11 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8654751","title":"Isolation of the plc1 gene from the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1995 Nov;23(4):566S","abstract":"","authors":"Slaaby R, Davey J","authors_abbrev":"Slaaby R et al.","pubmed_publication_date":"Nov 1995","pubmed_entrez_date":"1995-11-01","publication_year":"1995","canto_session_key":"401082b41eab153","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:45:11","canto_session_submitted_date":"2012-02-27 11:06:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:25432776","title":"Natural genetic variation impacts expression levels of coding, non-coding, and antisense transcripts in fission yeast.","citation":"Mol Syst Biol 2014 Nov 28;10(11):764","abstract":"Our current understanding of how natural genetic variation affects gene expression beyond well-annotated coding genes is still limited. The use of deep sequencing technologies for the study of expression quantitative trait loci (eQTLs) has the potential to close this gap. Here, we generated the first recombinant strain library for fission yeast and conducted an RNA-seq-based QTL study of the coding, non-coding, and antisense transcriptomes. We show that the frequency of distal effects (trans-eQTLs) greatly exceeds the number of local effects (cis-eQTLs) and that non-coding RNAs are as likely to be affected by eQTLs as protein-coding RNAs. We identified a genetic variation of swc5 that modifies the levels of 871 RNAs, with effects on both sense and antisense transcription, and show that this effect most likely goes through a compromised deposition of the histone variant H2A.Z. The strains, methods, and datasets generated here provide a rich resource for future studies.","doi":"10.15252/msb.20145123","authors":"Clément-Ziza M, Marsellach FX, Codlin S, Papadakis MA, Reinhardt S, Rodríguez-López M, Martin S, Marguerat S, Schmidt A, Lee E, Workman CT, Bähler J, Beyer A","authors_abbrev":"Clément-Ziza M et al.","pubmed_publication_date":"28 Nov 2014","pubmed_entrez_date":"2014-11-30","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-12-01 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15515904","title":"[Effect of radiofrequency of electromagnetic radiation on yeast sensitivity to fungicide antibiotics].","citation":"Mikrobiol Z 2004;66(4):69-77","abstract":"Saccharomyces cerevisiae UCM Y-517, Candida utilis UCM Y-961 and Schizosaccharomyces pombe UCM Y-94T have been studied for their sensitivity to fungicide antibiotics under the effect of electromagnetic radiation (40.68 MHz, 15 and 30 W). Yeast sensitivity to nystatin, amphotericin B, klotrimazol, itrakonazol, flukonazol as well as the effects arising as a result of the effect of radiofrequency radiation are characterized by species specificity. Irradiation did not exert statistically reliable effect on S. cerevisiae and S. pombe sensitivity to fungicide antibiotics. The increase of resistance of C. utilis to antibiotics (growth delay zones were absent in 70-90% of experiments) in the case of preliminary irradiation of this strain was stated. Separate preliminary irradiation of antibiotics did not result in the change of their antifungal activity. The arising effects were noticed to depend on the radiation power. Possible reasons of species specificity in sensing electromagnetic radiation are considered.","authors":"Voĭchuk SI, Gromozova EN","authors_abbrev":"Voĭchuk SI et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-11-02","publication_year":"2004","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17986764","title":"Accelerated chronological aging of a mutant fission yeast deficient in both glutathione and superoxide dismutase having cu and zn as cofactors and its enhancement by sir2 deficiency.","citation":"Biosci Biotechnol Biochem 2007 Nov;71(11):2841-4","abstract":"A mutant of Schizosaccharomyces pombe deficient in both superoxide dismutase with copper and zinc as cofactors and glutathione was hypersensitive to menadione, which intracellularly generates superoxide radicals, and showed short chronological lifespan with more oxidation of proteins. Disruption of the sir2 gene in the double mutant enhanced the short chronological lifespan without more enhanced protein oxidation.","authors":"Mutoh N, Kitajima S","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-11-08","publication_year":"2007","canto_session_key":"1636fd7c26646589","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-02 16:00:16","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-02 10:31:43","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.10c","SPBC16D10.07c","SPAC821.10c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-10-02"},{"uniquename":"PMID:31004207","title":"The impacts of Schizosaccharomyces on winemaking.","citation":"Appl Microbiol Biotechnol 2019 Jun;103(11):4291-4312","abstract":"In the past century, yeasts from the genus Saccharomyces represented the only option in fermentation industries, such as winemaking, to produce wine, beer, and other fermented products. However, other genera are currently emerging to solve challenges in modern enology. Schizosaccharomyces pombe is showing promising results in solving specific challenges in northern, cool viticulture regions with highly acidic wines by deacidifying these wines through its malic acid metabolism. In addition, this microorganism is considered beneficial in warm growing regions with challenges such as the control of wine food safety problems such as the presence of biogenic amines, ochratoxin A, or ethyl carbamate. Indeed, the genus Schizosaccharomyces positively influences other important wine quality parameters, such as color and polysaccharide content. However, the main challenge of using this genus remains the selection of proper strains that alleviate problems such as the production of high acetate concentrations. Industries other than wine production such as ginger fermentation, apple wine, Kei-apple fermentation, plum wine, sparkling wine, and bilberry fermentation industries have also started to study Schizosaccharomyces species as an alternative tool for solving specific related problems. The review discusses the influence of Schizosaccharomyces on different fermentation quality parameters and its main applications in different industries.","doi":"10.1007/s00253-019-09827-7","authors":"Benito S","authors_abbrev":"Benito S","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-04-21","publication_year":"2019","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2019-04-22 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36064597","title":"Histone deacetylation primes self-propagation of heterochromatin domains to promote epigenetic inheritance.","citation":"Nat Struct Mol Biol 2022 Sep;29(9):898-909","abstract":"Heterochromatin assembly, involving histone H3 lysine-9 methylation (H3K9me), is nucleated at specific genomic sites but can self-propagate across extended domains and, indeed, generations. Self-propagation requires Clr4/Suv39h methyltransferase recruitment by pre-existing H3K9 tri-methylation (H3K9me3) to perpetuate H3K9me deposition and is dramatically affected by chromatin context. However, the mechanism priming self-propagation of heterochromatin remains undefined. We show that robust chromatin association of fission yeast class II histone deacetylase Clr3 is necessary and sufficient to support heterochromatin propagation in different chromosomal contexts. Efficient targeting of Clr3, which suppresses histone turnover and maintains H3K9me3, enables self-propagation of an ectopic heterochromatin domain via the Clr4/Suv39h read-write mechanism requiring methylated histones. The deacetylase activity of Clr3 is necessary and, when inactivated, heterochromatin propagation can be recapitulated by removing two major histone acetyltransferases. Our results show that histone deacetylation, a conserved heterochromatin feature, preserves H3K9me3 that transmits epigenetic memory for stable propagation of silenced chromatin domains through multiple generations.","doi":"10.1038/s41594-022-00830-7","authors":"Zofall M, Sandhu R, Holla S, Wheeler D, Grewal SIS","authors_abbrev":"Zofall M et al.","pubmed_publication_date":"Sep 2022","pubmed_entrez_date":"2022-09-05","publication_year":"2022","canto_session_key":"f4ac1c05af48834b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-08 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15800064","title":"Mto2p, a novel fission yeast protein required for cytoplasmic microtubule organization and anchoring of the cytokinetic actin ring.","citation":"Mol Biol Cell 2005 Jun;16(6):3052-63","abstract":"Microtubules regulate diverse cellular processes, including chromosome segregation, nuclear positioning, and cytokinesis. In many organisms, microtubule nucleation requires gamma-tubulin and associated proteins present at specific microtubule organizing centers (MTOCs). In fission yeast, interphase cytoplasmic microtubules originate from poorly characterized interphase MTOCs and spindle pole body (SPB), and during late anaphase from the equatorial MTOC (EMTOC). It has been previously shown that Mto1p (Mbo1p/Mod20p) function is important for the organization/nucleation of all cytoplasmic microtubules. Here, we show that Mto2p, a novel protein, interacts with Mto1p and is important for establishing a normal interphase cytoplasmic microtubule array. In addition, mto2Delta cells fail to establish a stable EMTOC and localize gamma-tubulin complex members to this medial structure. As predicted from these functions, Mto2p localizes to microtubules, the SPB, and the EMTOC in an Mto1p-dependent manner. mto2Delta cells fail to anchor the cytokinetic actin ring in the medial region of the cell and under conditions that mildly perturb actin structures, these rings unravel in mto2Delta cells. Our results suggest that the Mto2p and the EMTOC are critical for anchoring the cytokinetic actin ring to the medial region of the cell and for proper coordination of mitosis with cytokinesis.","authors":"Venkatram S, Jennings JL, Link A, Gould KL","authors_abbrev":"Venkatram S et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-04-01","publication_year":"2005","canto_session_key":"3fce956824b89a65","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-28 10:30:37","canto_approved_date":"2023-05-16 13:54:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-23 11:30:06","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPBC211.06","SPBC365.15","SPBC428.20c","SPCC4G3.19","SPBC902.06","SPCC417.07c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2016-09-28"},{"uniquename":"EMBL:AU011183","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36692369","title":"Acetylation of fission yeast tropomyosin does not promote differential association with cognate formins.","citation":"Cytoskeleton (Hoboken) 2023 Mar;80(3-4):77-92","abstract":"It was proposed from cellular studies that S. pombe tropomyosin Cdc8 (Tpm) segregates into two populations due to the presence or absence of an amino-terminal acetylation that specifies which formin-mediated F-actin networks it binds, but with no supporting biochemistry. To address this mechanism in vitro, we developed methods for S. pombe actin expression in Sf9 cells. We then employed 3-color TIRF microscopy using all recombinant S. pombe proteins to probe in vitro multicomponent mechanisms involving actin, acetylated and unacetylated Tpm, formins, and myosins. Acetyl-Tpm exhibits tight binding to actin in contrast to weaker binding by unacetylated Tpm. In disagreement with the differential recruitment model, Tpm showed no preferential binding to filaments assembled by the FH1-FH2-domains of two S. pombe formins, nor did Tpm binding have any bias towards the growing formin-bound actin filament barbed end. Although our in vitro findings do not support a direct formin-tropomyosin interaction, it is possible that formins bias differential tropomyosin isoform recruitment through undiscovered mechanisms. Importantly, despite a 12% sequence divergence between skeletal and S. pombe actin, S. pombe myosins Myo2 and Myo51 exhibited similar motile behavior with these two actins, validating key prior findings with these myosins that used skeletal actin.","doi":"10.1002/cm.21745","authors":"Tang Q, Pollard LW, Homa KE, Kovar DR, Trybus KM","authors_abbrev":"Tang Q et al.","pubmed_publication_date":"Mar 2023","pubmed_entrez_date":"2023-01-24","publication_year":"2023","canto_session_key":"13a50729dc0000d7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-01-25 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2325639","title":"Functional analysis of a centromere from fission yeast: a role for centromere-specific repeated DNA sequences.","citation":"Mol Cell Biol 1990 May;10(5):1863-72","abstract":"A circular minichromosome carrying functional centromere sequences (cen2) from Schizosaccharomyces pombe chromosome II behaves as a stable, independent genetic linkage group in S. pombe. The cen2 region was found to be organized into four large tandemly repeated sequence units which span over 80 kilobase pairs (kb) of untranscribed DNA. Two of these units occurred in a 31-kb inverted repeat that flanked a 7-kb central core of nonhomology. The inverted repeat region had centromere function, but neither the central core alone nor one arm of the inverted repeat was functional. Deletion of a portion of the repeated sequences that flank the central core had no effect on mitotic segregation functions or on meiotic segregation of a minichromosome to two of the four haploid progeny, but drastically impaired centromere-mediated maintenance of sister chromatid attachment in meiosis I. This requirement for centromere-specific repeated sequences could not be satisfied by introduction of random DNA sequences. These observations suggest a function for the heterochromatic repeated DNA sequences found in the centromere regions of higher eucaryotes.","authors":"Clarke L, Baum MP","authors_abbrev":"Clarke L et al.","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_session_key":"83e7040886880e40","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 18:05:08","canto_approved_date":"2019-01-31 18:05:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 17:33:38","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:8299169","title":"Cloning and manipulation of the Schizosaccharomyces pombe his7+ gene as a new selectable marker for molecular genetic studies.","citation":"Curr Genet 1993 Dec;24(6):491-5","abstract":"We have cloned the his7+ gene of the fission yeast Schizosaccharomyces pombe by complementation of the recessive mutant allele his7-366. The his7+ gene is able to complement a mutation of the Escherichia coli hisI gene, suggesting that his7+ encodes a phosphoribosyl-AMP cyclohydrase. Subcloning experiments localize the gene to a 1.9-kb XbaI-BglII fragment. We describe the construction of plasmids to facilitate the use of his7+ as a selectable marker in S. pombe studies. Plasmid pEA2 carries his7+ cloned into the pUC18 polylinker. From either pEA2 or the original his7+ clone, pMN1, fragments carrying his7+ can be isolated using a variety of restriction enzymes for the construction of gene disruptions. Plasmid pEA500 is a cloning vector that carries his7+ and ars1, yet retains the ability to use the blue/white color screen to identify recombinants.","authors":"Apolinario E, Nocero M, Jin M, Hoffman CS","authors_abbrev":"Apolinario E et al.","pubmed_publication_date":"Dec 1993","pubmed_entrez_date":"1993-12-01","publication_year":"1993","canto_session_key":"3058c7d21384f30e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-04-23 07:47:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-04-19 15:26:00","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-04-19"},{"uniquename":"PMID:8573790","title":"Drosophila Wee1 kinase rescues fission yeast from mitotic catastrophe and phosphorylates Drosophila Cdc2 in vitro.","citation":"Mol Biol Cell 1995 Oct;6(10):1333-47","abstract":"Cdc2 kinase activity is required for triggering entry into mitosis in all known eukaryotes. Elaborate mechanisms have evolved for regulating Cdc2 activity so that mitosis occurs in a timely manner, when preparations for its execution are complete. In Schizosaccharomyces pombe, Wee1 and a related Mik1 kinase are Cdc2-inhibitory kinases that are required for preventing premature activation of the mitotic program. To identify Cdc2-inhibitory kinases in Drosophila, we screened for cDNA clones that rescue S. pombe wee1- mik1- mutants from lethal mitotic catastrophe. One of the genes identified in this screen, Drosophila wee1 (Dwee1), encodes a new Wee1 homologue. Dwee1 kinase is closely related to human and Xenopus Wee1 homologues, and can inhibit Cdc2 activity by phosphorylating a critical tyrosine residue. Dwee1 mRNA is maternally provided to embryos, and is zygotically expressed during the postblastoderm divisions of embryogenesis. Expression remains high in the proliferating cells of the central nervous system well after cells in the rest of the embryo have ceased dividing. The loss of zygotically expressed Dwee1 does not lead to mitotic catastrophe during postblastoderm cycles 14 to 16. This result may indicate that maternally provided Dwee1 is sufficient for regulating Cdc2 during embryogenesis, or it may reflect the presence of a redundant Cdc2 inhibitory kinase, as in fission yeast.","authors":"Campbell SD, Sprenger F, Edgar BA, O'Farrell PH","authors_abbrev":"Campbell SD et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_session_key":"4d2ab5750dd744f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:55:22","canto_session_submitted_date":"2012-03-03 15:53:48","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.14","SPCC18B5.03"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:27825338","title":"Sequential and counter-selectable cassettes for fission yeast.","citation":"BMC Biotechnol 2016 Nov 08;16(1):76","abstract":"Fission yeast is one of the most commonly used model organisms for studying genetics. For selection of desirable genotypes, antibiotic resistance cassettes are widely integrated into the genome near genes of interest. In yeasts, this is achieved by PCR amplification of the cassette flanked by short homology sequences, which can be incorporated by homology directed repair. However, the currently available cassettes all share the same tef promoter and terminator sequences. It can therefore be challenging to perform multiple genetic modifications by PCR-based targeting, as existing resistance cassettes in strains can be favored for recombination due to shared homology between the cassettes.\nHere we have generated new selection cassettes that do not recombine with those traditionally used. We achieved this by swapping the tef promoter and terminator sequences in the established antibiotic resistance MX6 cassette series for alternative promoters and/or terminators. The newly created selection cassettes did not recombine with the tef-containing MX6 cassettes already present in the genome, allowing for sequential gene targeting using the PCR-based method. In addition, we have generated a series of plasmids to facilitate the C-terminal tagging of genes with desired epitopes. We also utilized the anti-selection gene HSV-TK, which results in cell death in strains grown on the drug 5-Fluoro-2'-deoxyuridine (FdU, Floxuridin or FUDR). By fusing an antibiotic resistance gene to HSV-TK, we were able to select on the relevant antibiotic as well as counter-select on FdU media to confirm the desired genomic modification had been made. We noted that the efficiency of the counter selection by FdU was enhanced by treatment with hydroxyurea. However, a number of DNA replication checkpoint and homologous recombination mutants, including rad3∆, cds1∆, rad54∆ and rad55∆, exhibited sensitivity to FdU even though those strains did not carry the HSV-TK gene. To remove counter-selectable markers, we introduced the Cre-loxP irreversible recombination method. Finally, utilizing the negative selectable markers, we showed efficient induction of point mutations in an endogenous gene by a two-step transformation method.\nThe plasmid constructs and techniques described here are invaluable tools for sequential gene targeting and will simplify construction of fission yeast strains required for study.","authors":"Amelina H, Moiseeva V, Collopy LC, Pearson SR, Armstrong CA, Tomita K","authors_abbrev":"Amelina H et al.","pubmed_publication_date":"08 Nov 2016","pubmed_entrez_date":"2016-11-10","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-10 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27084937","title":"Transcription facilitates sister chromatid cohesion on chromosomal arms.","citation":"Nucleic Acids Res 2016 Aug 19;44(14):6676-92","abstract":"Cohesin is a multi-subunit protein complex essential for sister chromatid cohesion, gene expression and DNA damage repair. Although structurally well studied, the underlying determinant of cohesion establishment on chromosomal arms remains enigmatic. Here, we show two populations of functionally distinct cohesin on chromosomal arms using a combination of genomics and single-locus specific DNA-FISH analysis. Chromatin bound cohesin at the loading sites co-localizes with Pds5 and Eso1 resulting in stable cohesion. In contrast, cohesin independent of its loader is unable to maintain cohesion and associates with chromatin in a dynamic manner. Cohesive sites coincide with highly expressed genes and transcription inhibition leads to destabilization of cohesin on chromatin. Furthermore, induction of transcription results in de novo recruitment of cohesive cohesin. Our data suggest that transcription facilitates cohesin loading onto chromosomal arms and is a key determinant of cohesive sites in fission yeast.","doi":"10.1093/nar/gkw252","authors":"Bhardwaj S, Schlackow M, Rabajdova M, Gullerova M","authors_abbrev":"Bhardwaj S et al.","pubmed_publication_date":"19 Aug 2016","pubmed_entrez_date":"2016-04-17","publication_year":"2016","canto_session_key":"a8c8ca0b894c2c57","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-04-18 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC00001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23840894","title":"Sip1, an AP-1 accessory protein in fission yeast, is required for localization of Rho3 GTPase.","citation":"PLoS One 2013;8(7):e68488","abstract":"Rho family GTPases act as molecular switches to regulate a range of physiological functions, including the regulation of the actin-based cytoskeleton, membrane trafficking, cell morphology, nuclear gene expression, and cell growth. Rho function is regulated by its ability to bind GTP and by its localization. We previously demonstrated functional and physical interactions between Rho3 and the clathrin-associated adaptor protein-1 (AP-1) complex, which revealed a role of Rho3 in regulating Golgi/endosomal trafficking in fission yeast. Sip1, a conserved AP-1 accessory protein, recruits the AP-1 complex to the Golgi/endosomes through physical interaction. In this study, we showed that Sip1 is required for Rho3 localization. First, overexpression of rho3⁺ suppressed defective membrane trafficking associated with sip1-i4 mutant cells, including defects in vacuolar fusion, Golgi/endosomal trafficking and secretion. Notably, Sip1 interacted with Rho3, and GFP-Rho3, similar to Apm1-GFP, did not properly localize to the Golgi/endosomes in sip1-i4 mutant cells at 27°C. Interestingly, the C-terminal region of Sip1 is required for its localization to the Golgi/endosomes, because Sip1-i4-GFP protein failed to properly localize to Golgi/endosomes, whereas the fluorescence of Sip1ΔN mutant protein co-localized with that of FM4-64. Consistently, in the sip1-i4 mutant cells, which lack the C-terminal region of Sip1, binding between Apm1 and Rho3 was greatly impaired, presumably due to mislocalization of these proteins in the sip1-i4 mutant cells. Furthermore, the interaction between Apm1 and Rho3 as well as Rho3 localization to the Golgi/endosomes were significantly rescued in sip1-i4 mutant cells by the expression of Sip1ΔN. Taken together, these results suggest that Sip1 recruits Rho3 to the Golgi/endosomes through physical interaction and enhances the formation of the Golgi/endosome AP-1/Rho3 complex, thereby promoting crosstalk between AP-1 and Rho3 in the regulation of Golgi/endosomal trafficking in fission yeast.","doi":"10.1371/journal.pone.0068488","authors":"Yu Y, Li C, Kita A, Katayama Y, Kubouchi K, Udo M, Imanaka Y, Ueda S, Masuko T, Sugiura R","authors_abbrev":"Yu Y et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-11","publication_year":"2013","canto_session_key":"e39329bc7507259d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP27G11.06c","SPBP16F5.07","SPAC23C4.08","SPBC27B12.08","SPBC947.02","SPCP1E11.06"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:27327046","title":"Use of a fluoride channel as a new selection marker for fission yeast plasmids and application to fast genome editing with CRISPR/Cas9.","citation":"Yeast 2016 Oct;33(10):549-557","abstract":"Fission yeast is a powerful model organism that has provided insights into important cellular processes thanks to the ease of its genome editing by homologous recombination. However, creation of strains with a large number of targeted mutations or containing plasmids has been challenging because only a very small number of selection markers is available in Schizosaccharomyces pombe. In this paper, we identify two fission yeast fluoride exporter channels (Fex1p and Fex2p) and describe the development of a new strategy using Fex1p as a selection marker for transformants in rich media supplemented with fluoride. To our knowledge this is the first positive selection marker identified in S. pombe that does not use auxotrophy or drug resistance and that can be used for plasmids transformation or genomic integration in rich media. We illustrate the application of our new marker by significantly accelerating the protocol for genome edition using CRISPR/Cas9 in S. pombe. Copyright © 2016 John Wiley & Sons, Ltd.","doi":"10.1002/yea.3178","authors":"Fernandez R, Berro J","authors_abbrev":"Fernandez R et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-06-22","publication_year":"2016","canto_session_key":"8bbf965b2fdf46b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Julien Berro","canto_first_approved_date":"2017-11-14 16:27:11","canto_approved_date":"2025-09-03 15:14:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-19 16:14:07","canto_added_date":"2016-06-23 00:15:14","annotation_curators":[{"name":"Julien Berro","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.11","SPBPB8B6.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-11-14"},{"uniquename":"PMID:21307597","title":"Ecl1, a regulator of the chronological lifespan of Schizosaccharomyces pombe, is induced upon nitrogen starvation.","citation":"Biosci Biotechnol Biochem 2011;75(2):279-83","abstract":"In fission yeast, ecl1(+) was identified as a novel factor that extends chronological lifespan when overexpressed. Ecl1 is a small protein consisting of 80 amino acids localized mainly in the nucleus. However, the mechanism by which it affects chronological lifespan has not been elucidated clearly. Here we analyzed the expression profile of Ecl1, especially as to cell cycle and growth phase, and found that it is induced upon nitrogen starvation. Then we analyzed the relevance of factors, Atf1, Ste11, and Tor1, which are known to be involved in the signaling of nitrogen starvation. Though the nitrogen starvation-induced expression of Ecl1 did not change in the atf1Δ mutant, induction in both the ste11Δ mutant and the tor1Δ mutant showed a delay. Based on these observations, the regulation of Ecl1 is discussed.","authors":"Miwa Y, Ohtsuka H, Naito C, Murakami H, Aiba H","authors_abbrev":"Miwa Y et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-02-11","publication_year":"2011","canto_session_key":"88385193e3836bbf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-03-31 16:41:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-31 16:41:40","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC70.12c","SPBC29B5.01","SPBC30D10.10c","SPBC32C12.02"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-03-31"},{"uniquename":"PMID:18388974","title":"Cloning of the ATP sulphurylase gene of Schizosaccharomyces pombe by functional complementation.","citation":"Can J Microbiol 2008 Jan;54(1):71-4","abstract":"The ATP sulphurylase gene of Schizosaccharomyces pombe has been cloned by complementation of cysteine auxotrophy of a selenate-resistant mutant, which supposedly had a defect in ATP sulphurylase. A sulphate nonutilizing (cysteine auxotrophic) and selenate-resistant mutant of S. pombe was transformed with a wild-type S. pombe genomic library and sulphate-utilizing clones were isolated. The open reading frame encoding the ATP sulphurylase enzyme was found to be responsible for the restoration of sulphate assimilation. Transformants became as sensitive for selenate as the wild-type strain and produced a comparable amount of ATP sulphurylase as the prototrophic strains. The cloned ATP sulphurylase gene (sua1) proved to be an efficient selection marker in an ARS vector, when different isogenic or nonisogenic S. pombe selenate-resistant mutants were used as cloning hosts. Complementation of sua1- mutations by sua1-bearing multicopy vectors functions as a useful dual positive and negative selection marker. The cloned sua1 gene also complemented the met3 (ATP sulphurylase deficient) mutation in Saccharomyces cerevisiae.","doi":"10.1139/w07-111","authors":"Simonics T, Maráz A","authors_abbrev":"Simonics T et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2008-04-05","publication_year":"2008","canto_session_key":"6c5dc6a27e03eeb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-30 23:20:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-30 23:16:43","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-30"},{"uniquename":"PMID:19054127","title":"Identification and characterization of a gene required for alpha1,2-mannose extension in the O-linked glycan synthesis pathway in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2009 Feb;9(1):115-25","abstract":"The KTRalpha1,2-mannosyltransferase gene family of Saccharomyces cerevisiae is responsible not only for outer-chain modifications of N-linked oligosaccharides but also for elongation of O-linked mannose residues. To identify genes involved in the elongation step of O-linked oligosaccharide chains in Schizosaccharomyces pombe, we characterized six genes, omh1(+)-omh6(+), that share significant sequence similarity to the S. cerevisiae KTR family. Six deletion strains were constructed, each carrying a single disrupted omh allele. All strains were viable, indicating that none of the omh genes was essential. Heterologous expression of a chitinase from S. cerevisiae in the omh mutants revealed that O-glycosylation of chitinase had decreased in omh1Delta cells, but not in the other mutants, indicating that the other omh genes do not appear to be required for O-glycan synthesis. Addition of the second alpha1,2-linked mannose residue was blocked in omh1Delta cells. An Omh1-GFP fusion protein was found to be localized in the Golgi apparatus. These results indicate that Omh1p plays a major role in extending alpha1,2-linked mannose in the O-glycan pathway in S. pombe.","doi":"10.1111/j.1567-1364.2008.00458.x","authors":"Ikeda Y, Ohashi T, Tanaka N, Takegawa K","authors_abbrev":"Ikeda Y et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-12-05","publication_year":"2009","canto_session_key":"4bd674ce652a4adc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-05-26 16:48:55","canto_approved_date":"2024-06-19 15:17:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-19 12:44:13","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1773.08c","SPAC959.04c","SPBC16H5.09c","SPCC777.07","SPBC19C7.12c","SPBC32H8.08c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-05-26"},{"uniquename":"EMBL:AU010014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.95","SPNCRNA.84"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8324197","title":"Dielectric energy of orientation in dead and living cells of Schizosaccharomyces pombe. Fitting of experimental results to a theoretical model.","citation":"Biophys J 1993 May;64(5):1626-31","abstract":"Using the experimental data obtained with killed cells of Schizosaccharomyces pombe (1), we have formulated a theoretical model that is able to predict cell orientation for microorganisms with ellipsoidal or cylindrical shapes as a function of the frequency of the electric field and of the conductivity of the external medium. In this model, comparison of the difference in potential energy for both orientations parallel-perpendicular with the thermal agitation energy allows one to interpret the intervals where these orientations occur. The model implies that the conductivity of the cytoplasm is slightly higher than that of the external medium. This assumption is easy to understand taking into account that not all the intracytoplasmic material is released to the exterior during cell death.","authors":"Asencor FJ, Santamaría C, Iglesias FJ, Domínguez A","authors_abbrev":"Asencor FJ et al.","pubmed_publication_date":"May 1993","pubmed_entrez_date":"1993-05-01","publication_year":"1993","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7698661","title":"Cloning and sequence analysis of an ERG24 homolog from Schizosaccharomyces pombe.","citation":"Gene 1995 Mar 21;155(1):139-40","abstract":"The Schizosaccharomyces pombe (Sp) erg24 cDNA, encoding C-14 sterol reductase (erg24p), has been cloned and sequenced. The nucleotide sequence of Sp erg24 contains an open reading frame encoding a 424-amino-acid protein. The deduced aa sequence of Sp erg24 shows significant homology with Saccharomyces cerevisiae (Sc) Erg24p, as well as with other members of a larger gene family that includes yeast C-24(28) sterol reductase (Erg4p) and a vertebrate inner nuclear membrane protein, the lamin B receptor (LBR).","authors":"Smith S","authors_abbrev":"Smith S","pubmed_publication_date":"21 Mar 1995","pubmed_entrez_date":"1995-03-21","publication_year":"1995","canto_session_key":"561f1accb0f396da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:33:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 21:19:14","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16G5.18"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-25"},{"uniquename":"PMID:1574925","title":"Architectural features of pre-mRNA introns in the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 1992 Mar;8(3):171-82","abstract":"The architectural features of 73 introns found in 36 genes of the fission yeast Schizosaccharomyces pombe have been compiled and tabulated. The introns from S. pombe can be grouped into two size classes. Intron features are discussed in comparison to intron features of Saccharomyces cerevisiae and other eukaryotes. The results indicate that S. pombe displays quite different architectural features than the budding yeast S. cerevisiae. However, particularly in the 3' region, S. pombe introns also appear to differ from mammalian introns.","authors":"Prabhala G, Rosenberg GH, Käufer NF","authors_abbrev":"Prabhala G et al.","pubmed_publication_date":"Mar 1992","pubmed_entrez_date":"1992-03-01","publication_year":"1992","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24786825","title":"Application of a phosphite dehydrogenase gene as a novel dominant selection marker for yeasts.","citation":"J Biotechnol 2014 Jul 20;182-183:68-73","abstract":"The use of antibiotic resistance markers in the commercial application of genetically modified microorganisms is limited due to restrictions on the release of antibiotics and their resistance genes to the environment. To avoid contamination by other microorganisms, the development of a dominant selection marker with low environmental risks is still needed. Here we demonstrated a new selection system for Schizosaccharomyces pombe and Saccharomyces cerevisiae using a bacterial phosphite dehydrogenase gene (ptxD). A Sz. pombe transformant carrying ptxD under a strong promoter or on a multicopy plasmid grew on a minimal medium containing phosphite (Pt) as a sole source of phosphorus. To adapt this system to S. cerevisiae strains, codon optimization of ptxD was necessary. The codon-optimized ptxD system appeared effective in not only laboratorial but also industrial S. cerevisiae strains that are diploid or polyploid. Since Pt is a safe and inexpensive chemical, ptxD could be used as a novel dominant selection marker applicable on an industrial scale.","doi":"10.1016/j.jbiotec.2014.04.012","authors":"Kanda K, Ishida T, Hirota R, Ono S, Motomura K, Ikeda T, Kitamura K, Kuroda A","authors_abbrev":"Kanda K et al.","pubmed_publication_date":"20 Jul 2014","pubmed_entrez_date":"2014-05-03","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012213","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25352303","title":"Genome organization: 3D genome architecture--of loops and globules.","citation":"Nat Rev Genet 2014 Dec;15(12):780","abstract":"","doi":"10.1038/nrg3858","authors":"Koch L","authors_abbrev":"Koch L","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-10-30","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-01-14 01:15:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009320","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34036246","title":"Distinct spatiotemporal distribution of Hsp90 under high-heat and mild-heat stress conditions in fission yeast.","citation":"MicroPubl Biol 2021 May 04;2021","abstract":"The molecular chaperone Hsp90 is highly conserved from bacteria to mammals. In fission yeast, Hsp90 is essential in many cellular processes and its expression is known to be increased by heat stress (HS). Here, we describe the distinct spatiotemporal distribution of Hsp90 under high-heat stress (HHS: 45˚C) and mild-heat stress (MHS: 37˚C). Hsp90 is largely distributed in the cytoplasm under non-stressed conditions (27˚C). Under HHS, Hsp90 forms several cytoplasmic granules within 5 minutes, then the granules disappear within 60 minutes. Under MHS, Hsp90 forms fewer granules than under HHS within 5 minutes and strikingly the granules persist and grow in size. In addition, nuclear enrichment of Hsp90 was observed after 60 minutes under both HS conditions. Our data suggest that assembly/disassembly of Hsp90 granules is differentially regulated by temperatures.","doi":"10.17912/micropub.biology.000388","authors":"Takasaki T, Tomimoto N, Ikehata T, Satoh R, Sugiura R","authors_abbrev":"Takasaki T et al.","pubmed_publication_date":"04 May 2021","pubmed_entrez_date":"2021-05-26","publication_year":"2021","canto_session_key":"8445df55799b685c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10856773","title":"Simple detection method for distinguishing dead and living yeast colonies.","citation":"J Microbiol Methods 2000 Jun;41(1):19-21","abstract":"A rapid and simple assay was developed for detection of yeast colonies containing dying or dead cells. Methylene blue, phloxin B, rose bengal and trypan blue at concentrations of 5-10 micromol l(-1) were shown to stain non-viable cells in colonies of Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida albicans and Filobasidium capsuligenum without staining or affecting the viability of living cells of the colonies.","authors":"Kucsera J, Yarita K, Takeo K","authors_abbrev":"Kucsera J et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-06-17","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33245560","title":"Construction and characterization of a zinc-inducible gene expression vector in fission yeast.","citation":"Yeast 2021 Apr;38(4):251-261","abstract":"Gene expression vectors are useful and important tools that are commonly used in a variety of experiments, including expression of foreign genes, functional analysis of genes of interest and complementation experiments. In this study, a hybrid promoter, combining the adh1 +  upstream activating sequence (UAS) of fission yeast and the GAL10 core promoter of budding yeast, was constructed to enable high level expression depending on the presence of zinc in culture medium for fission yeast. When the hybrid promoter was cloned on the multicopy plasmid, it was fully induced and repressed within 10 h in the presence and absence of zinc, respectively. The kinetics of induction and reduction were similar to those of the endogenous adh1 +  mRNA. In contrast, native adh1 +  promoter lost its tight repression in zinc-depleted condition when it was cloned on the plasmid. Because adh1 +  UAS-specific transcription factors have not yet been identified, we identified UAS elements involved in zinc sensing by characterizing this hybrid promoter. We also found that the expression level increased by the TATA box mutation, GATAA, in the presence of zinc.","doi":"10.1002/yea.3539","authors":"Takahata S, Asanuma T, Mori M, Murakami Y","authors_abbrev":"Takahata S et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2020-11-27","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-11-29 01:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBPB2B2.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20655916","title":"TERRA biogenesis, turnover and implications for function.","citation":"FEBS Lett 2010 Sep 10;584(17):3812-8","abstract":"Telomeres are heterochromatic structures at the ends of eukaryotic chromosomes. As other heterochromatin regions, telomeres are transcribed, from the subtelomeric region towards chromosome ends into the long non-coding RNA TERRA. Telomere transcription is a widespread phenomenon as it has been observed in species belonging to several kingdoms of the eukaryotic domain. TERRA is part of telomeric heterochromatin in addition to being present in the nucleoplasm. Here, we review the current knowledge of TERRA structure, biogenesis and turnover. In addition, we discuss presumed roles of this RNA during replication of telomeric DNA, heterochromatin formation and the regulation of telomerase.","doi":"10.1016/j.febslet.2010.07.032","authors":"Feuerhahn S, Iglesias N, Panza A, Porro A, Lingner J","authors_abbrev":"Feuerhahn S et al.","pubmed_publication_date":"10 Sep 2010","pubmed_entrez_date":"2010-07-27","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-11-10 16:51:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26358720","title":"Single-Nucleotide-Specific Targeting of the Tf1 Retrotransposon Promoted by the DNA-Binding Protein Sap1 of Schizosaccharomyces pombe.","citation":"Genetics 2015 Nov;201(3):905-24","abstract":"Transposable elements (TEs) constitute a substantial fraction of the eukaryotic genome and, as a result, have a complex relationship with their host that is both adversarial and dependent. To minimize damage to cellular genes, TEs possess mechanisms that target integration to sequences of low importance. However, the retrotransposon Tf1 of Schizosaccharomyces pombe integrates with a surprising bias for promoter sequences of stress-response genes. The clustering of integration in specific promoters suggests that Tf1 possesses a targeting mechanism that is important for evolutionary adaptation to changes in environment. We report here that Sap1, an essential DNA-binding protein, plays an important role in Tf1 integration. A mutation in Sap1 resulted in a 10-fold drop in Tf1 transposition, and measures of transposon intermediates support the argument that the defect occurred in the process of integration. Published ChIP-Seq data on Sap1 binding combined with high-density maps of Tf1 integration that measure independent insertions at single-nucleotide positions show that 73.4% of all integration occurs at genomic sequences bound by Sap1. This represents high selectivity because Sap1 binds just 6.8% of the genome. A genome-wide analysis of promoter sequences revealed that Sap1 binding and amounts of integration correlate strongly. More important, an alignment of the DNA-binding motif of Sap1 revealed integration clustered on both sides of the motif and showed high levels specifically at positions +19 and -9. These data indicate that Sap1 contributes to the efficiency and position of Tf1 integration.","doi":"10.1534/genetics.115.181602","authors":"Hickey A, Esnault C, Majumdar A, Chatterjee AG, Iben JR, McQueen PG, Yang AX, Mizuguchi T, Grewal SI, Levin HL","authors_abbrev":"Hickey A et al.","pubmed_publication_date":"Nov 2015","pubmed_entrez_date":"2015-09-12","publication_year":"2015","canto_session_key":"48962b9e331018c2","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-09-13 00:18:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1672.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16278931","title":"Activation of S phase checkpoint by cigarette smoke extract in Schizosaccharomyces pombe.","citation":"Yeast 2005 Nov;22(15):1223-38","abstract":"Cigarette smoke has long been recognized as a major environmental pollutant that can cause significant damage to the cellular macromolecules. Although much is known about the types of damage, little is known about the cellular responses to the stress caused by cigarette smoke. We have used the fission yeast Schizosaccharomyces pombe to elucidate the overall cellular responses towards cigarette smoke. Here, we demonstrate that fission yeast cells exposed to aqueous extract of cigarette smoke exhibit cell cycle arrest and cell death in a dose-dependent manner. Cigarette smoke treatment also results in accumulation of reactive oxygen species, unusual nuclear morphology and altered cellular structure. Our data further establish activation of the S phase checkpoint in cigarette smoke-exposed Sz. pombe cells. The checkpoint proteins Rad3, Rad26, Rad17, Rad1, Hus1 and Cds1 play key roles in this process, as evidenced by cell survival and biochemical analysis, although another checkpoint protein, Rad9, seems to be less required. Our results also suggest involvement of the stress-activated protein kinase Spc1/Sty1 and the bZIP transcription factors Atf1 and Pap1 in the cellular response towards cigarette smoke extract. These findings indicate activation of the critical S phase checkpoint and cell cycle arrest in Sz. pombe following CSE assault.","authors":"Chaudhuri SP, Sundaram G, Bhattacharya A, Ray P, Ray A, Chatterjee IB, Chattopadhyay D","authors_abbrev":"Chaudhuri SP et al.","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-11-10","publication_year":"2005","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15701794","title":"Amiloride uptake and toxicity in fission yeast are caused by the pyridoxine transporter encoded by bsu1+ (car1+).","citation":"Eukaryot Cell 2005 Feb;4(2):319-26","abstract":"Amiloride, a diuretic drug that acts by inhibition of various sodium transporters, is toxic to the fission yeast Schizosaccharomyces pombe. Previous work has established that amiloride sensitivity is caused by expression of car1+, which encodes a protein with similarity to plasma membrane drug/proton antiporters from the multidrug resistance family. Here we isolated car1+ by complementation of Saccharomyces cerevisiae mutants that are deficient in pyridoxine biosynthesis and uptake. Our data show that Car1p represents a new high-affinity, plasma membrane-localized import carrier for pyridoxine, pyridoxal, and pyridoxamine. We therefore propose the gene name bsu1+ (for vitamin B6 uptake) to replace car1+. Bsu1p displays an acidic pH optimum and is inhibited by various protonophores, demonstrating that the protein works as a proton symporter. The expression of bsu1+ is associated with amiloride sensitivity and pyridoxine uptake in both S. cerevisiae and S. pombe cells. Moreover, amiloride acts as a competitor of pyridoxine uptake, demonstrating that both compounds are substrates of Bsu1p. Taken together, our data show that S. pombe and S. cerevisiae possess unrelated plasma membrane pyridoxine transporters. The S. pombe protein may be structurally related to the unknown human pyridoxine transporter, which is also inhibited by amiloride.","authors":"Stolz J, Wöhrmann HJ, Vogl C","authors_abbrev":"Stolz J et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2005-02-11","publication_year":"2005","canto_session_key":"f290368a6acf0d54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-06-12 09:19:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-12 09:19:46","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29B12.04","SPAC17A2.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-12"},{"uniquename":"PMID:24711392","title":"SUMOylation regulates telomere length by targeting the shelterin subunit Tpz1(Tpp1) to modulate shelterin-Stn1 interaction in fission yeast.","citation":"Proc Natl Acad Sci U S A 2014 Apr 22;111(16):5950-5","abstract":"Telomeres protect DNA ends of linear eukaryotic chromosomes from degradation and fusion, and ensure complete replication of the terminal DNA through recruitment of telomerase. The regulation of telomerase is a critical area of telomere research and includes cis regulation by the shelterin complex in mammals and fission yeast. We have identified a key component of this regulatory pathway as the SUMOylation [the covalent attachment of a small ubiquitin-like modifier (SUMO) to target proteins] of a shelterin subunit in fission yeast. SUMOylation is known to be involved in the negative regulation of telomere extension by telomerase; however, how SUMOylation limits the action of telomerase was unknown until now. We show that SUMOylation of the shelterin subunit TPP1 homolog in Schizosaccharomyces pombe (Tpz1) on lysine 242 is important for telomere length homeostasis. Furthermore, we establish that Tpz1 SUMOylation prevents telomerase accumulation at telomeres by promoting recruitment of Stn1-Ten1 to telomeres. Our findings provide major mechanistic insights into how the SUMOylation pathway collaborates with shelterin and Stn1-Ten1 complexes to regulate telomere length.","doi":"10.1073/pnas.1401359111","authors":"Miyagawa K, Low RS, Santosa V, Tsuji H, Moser BA, Fujisawa S, Harland JL, Raguimova ON, Go A, Ueno M, Matsuyama A, Yoshida M, Nakamura TM, Tanaka K","authors_abbrev":"Miyagawa K et al.","pubmed_publication_date":"22 Apr 2014","pubmed_entrez_date":"2014-04-09","publication_year":"2014","canto_session_key":"e24fc3af1e6b6716","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06","SPAC19G12.13c","SPBC409.12c","SPAC6F6.16c","SPCC188.07","SPBC365.06"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:11452028","title":"Expression of hsp16 in response to nucleotide depletion is regulated via the spc1 MAPK pathway in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2001 Jul 15;29(14):3030-40","abstract":"A universal response to elevated temperature and other forms of physiological stress is the induction of heat shock proteins (HSPs). Hsp16 in Schizosaccharomyces pombe encodes a polypeptide of predicted molecular weight 16 kDa that belongs to the HSP20/alpha-crystallin family whose members range in size from 12 to 43 kDa. Heat shock treatment increases expression of the hsp16 gene by 64-fold in wild-type cells and 141-fold in cdc22-M45 (ribonucleotide reductase) mutant cells. Hsp16 expression is mediated by the spc1 MAPK signaling pathway through the transcription factor atf1 and in addition through the HSF pathway. Nucleotide depletion or DNA damage as occurs in cdc22-M45 mutant cells, or during hydroxyurea or camptothecin treatment, is sufficient to activate hsp16 expression through atf1. Our findings suggest a novel role for small HSPs in the stress response following nucleotide depletion and DNA damage. This extends the types of damage that are sensed by the spc1 MAPK pathway via atf1.","authors":"Taricani L, Feilotter HE, Weaver C, Young PG","authors_abbrev":"Taricani L et al.","pubmed_publication_date":"15 Jul 2001","pubmed_entrez_date":"2001-07-14","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19A8.10","SPBC3E7.02c","SPBC1289.15","SPBC365.06","SPBC1734.06","SPAC630.14c","SPAC513.01c","SPCC417.08","SPCP31B10.06"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:28352647","title":"Single-step Marker Switching in  Schizosaccharomyces pombe  Using a Lithium Acetate Transformation Protocol.","citation":"Bio Protoc 2016 Dec 20;6(24)","abstract":"The ability to utilize different selectable markers for tagging or mutating multiple genes in  Schizosaccharomyces pombe  is hampered by the historical use of only two selectable markers,  ura4 +   and  kanMX6 ; the latter conferring resistance to the antibiotic G418 (geneticin). More markers have been described recently, but introducing these into yeast cells often requires strain construction from scratch. To overcome this problem we and other groups have created transformation cassettes with flanking homologies to  ura4  +  and  kanMX6  which enable an efficient and time-saving way to exchange markers in existing mutated or tagged fission yeast strains. Here, we present a protocol for single-step marker switching by lithium acetate transformation in fission yeast,  Schizosaccharomyces pombe . In the following we describe how to swap the  ura4 +   marker to a  kanMX6, natMX4,  or  hphMX4  marker, which provide resistance against the antibiotics G418, nourseothricin (clonNAT) or hygromycin B, respectively. We also detail how to exchange any of the  MX  markers for nutritional markers, such as  arg3 + , his3 + , leu1 +   and  ura4 +   .","doi":"10.21769/BioProtoc.2075","authors":"Brown SD, Lorenz A","authors_abbrev":"Brown SD et al.","pubmed_publication_date":"20 Dec 2016","pubmed_entrez_date":"2017-03-30","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-03-31 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:79390","title":"Solubilization and purification of the plasma membrane ATPase from Schizosaccharomyces pombe [proceedings].","citation":"Arch Int Physiol Biochim 1977 Dec;85(5):974-5","abstract":"","authors":"Dufour JP, Goffeau A","authors_abbrev":"Dufour JP et al.","pubmed_publication_date":"Dec 1977","pubmed_entrez_date":"1977-12-01","publication_year":"1977","canto_session_key":"cbf85e47e36b4774","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-23 17:58:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-23 17:57:59","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-23"},{"uniquename":"PMID:39333500","title":"Cdc42 mobility and membrane flows regulate fission yeast cell shape and survival.","citation":"Nat Commun 2024 Sep 27;15(1):8363","abstract":"Polarized exocytosis induced by local Cdc42 GTPase activity results in membrane flows that deplete low-mobility membrane-associated proteins. A reaction-diffusion particle model comprising Cdc42 positive feedback activation, hydrolysis by GTPase-activating proteins (GAPs), and flow-induced displacement by exo/endocytosis shows that flow-induced depletion of low mobility GAPs promotes polarization. We modified Cdc42 mobility in Schizosaccharomyces pombe by replacing its prenylation site with 1, 2 or 3 repeats of the Rit C-terminal membrane-binding domain (ritC), yielding alleles with progressively lower mobility and increased flow-coupling. While Cdc42-1ritC cells are viable and polarized, Cdc42-2ritC polarize poorly and Cdc42-3ritC are inviable, in agreement with model's predictions. Deletion of Cdc42 GAPs restores viability to Cdc42-3ritC cells, verifying the model's prediction that GAP deletion increases Cdc42 activity at the expense of polarization. Our work demonstrates how membrane flows are an integral part of Cdc42-driven pattern formation and require Cdc42-GTP to turn over faster than the surface on which it forms.","doi":"10.1038/s41467-024-52655-1","authors":"Rutkowski DM, Vincenzetti V, Vavylonis D, Martin SG","authors_abbrev":"Rutkowski DM et al.","pubmed_publication_date":"27 Sep 2024","pubmed_entrez_date":"2024-09-27","publication_year":"2024","canto_session_key":"a50d887380e58042","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2024-10-16 12:02:06","canto_approved_date":"2026-05-13 05:43:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-10-02 16:08:43","canto_added_date":"2024-09-28 23:25:06","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":9,"orcid":"0000-0002-5317-2557","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29A4.11","SPAC110.03","SPBC354.13","SPBC28E12.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-10-16"},{"uniquename":"PMID:24387855","title":"Modified COLD-PCR for detection of minor microorganisms in wine samples during the fermentation.","citation":"Food Microbiol 2014 May;39:74-80","abstract":"The detection of low-abundant microorganism is difficult when in a sample in which a specific microorganism represents an overwhelming majority using polymerase chain reaction (PCR)-based methods. A modified CO-amplification at Lower Denaturation temperature PCR (mCOLD-PCR) method was developed to detect low-abundant microorganisms using a double-strand RNA probe to inhibit the amplification of the sequence of a major microorganism. Combining the mCOLD-PCR and downstream application (e.g., denaturing gradient gel electrophoresis (DGGE) and next-generation sequencing (NGS)), low-abundant microorganisms were detected more efficiently, even when a specific microorganism represents an overwhelming majority of the sample. We demonstrated that mCOLD-PCR-DGGE enabled us to detect Schizosaccharomyces pombe in a model sample coexisting with 10,000 times as many Saccharomyces cerevisiae. When mCOLD-PCR-DGGE was applied in the microbiota analysis of a fermenting white wine, Candida sp. and Cladosporium sp., which were not detected by conventional PCR, were detected. According to the NGS analysis after mCOLD-PCR of a fermenting red wine, the detection ratio of Saccharomyces was decreased dramatically, and the detection ratios of other microorganisms and the numbers of genera detected were increased compared with the conventional PCR. Thus, the application of mCOLD-PCR will reveal comprehensive microbiota of fermented foods, beverages, and so on.","doi":"10.1016/j.fm.2013.11.009","authors":"Takahashi M, Masaki K, Mizuno A, Goto-Yamamoto N","authors_abbrev":"Takahashi M et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2014-01-07","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17971862","title":"An RNA polymerase III-dependent heterochromatin barrier at fission yeast centromere 1.","citation":"PLoS One 2007 Oct 31;2(10):e1099","abstract":"Heterochromatin formation involves the nucleation and spreading of structural and epigenetic features along the chromatin fiber. Chromatin barriers and associated proteins counteract the spreading of heterochromatin, thereby restricting it to specific regions of the genome. We have performed gene expression studies and chromatin immunoprecipitation on strains in which native centromere sequences have been mutated to study the mechanism by which a tRNA(Alanine) gene barrier (cen1 tDNA(Ala)) blocks the spread of pericentromeric heterochromatin at the centromere of chromosome 1 (cen1) in the fission yeast, Schizosaccharomyces pombe. Within the centromere, barrier activity is a general property of tDNAs and, unlike previously characterized barriers, requires the association of both transcription factor IIIC and RNA Polymerase III. Although the cen1 tDNA(Ala) gene is actively transcribed, barrier activity is independent of transcriptional orientation. These findings provide experimental evidence for the involvement of a fully assembled RNA polymerase III transcription complex in defining independent structural and functional domains at a eukaryotic centromere.","authors":"Scott KC, White CV, Willard HF","authors_abbrev":"Scott KC et al.","pubmed_publication_date":"31 Oct 2007","pubmed_entrez_date":"2007-11-01","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16914721","title":"Upf1, an RNA helicase required for nonsense-mediated mRNA decay, modulates the transcriptional response to oxidative stress in fission yeast.","citation":"Mol Cell Biol 2006 Sep;26(17):6347-56","abstract":"In the fission yeast Schizosaccharomyces pombe, oxidative stress triggers the activation of the Spc1/Sty1 mitogen-activated protein kinase, which in turn phosphorylates the Atf1/Pcr1 heterodimeric transcription factor to effect global changes in the patterns of gene expression. This transcriptional response is also controlled by Csx1, an RNA-binding protein that directly associates with and stabilizes atf1(+) mRNA. Here we report the surprising observation that this response also requires Upf1, a component of the nonsense-mediated mRNA decay (NMD) system. Accordingly, upf1Delta and csx1Delta strains are similarly sensitive to oxidative stress, and the effects of the mutations are not additive, suggesting that Upf1 and Csx1 work in the same pathway to stabilize atf1(+) mRNA during oxidative stress. Consistent with these observations, whole-genome expression profiling studies have shown that Upf1 controls the expression of more than 100 genes that are transcriptionally induced in response to oxidative stress, the large majority of which are also controlled by Atf1 and Csx1. The unexpected connection between an NMD factor and the oxidative stress response in fission yeast may provide important new clues about the physiological function of NMD in other species.","authors":"Rodríguez-Gabriel MA, Watt S, Bähler J, Russell P","authors_abbrev":"Rodríguez-Gabriel MA et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-08-18","publication_year":"2006","canto_session_key":"9a6cbb66c43cb971","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-22 15:31:01","canto_approved_date":"2025-09-02 17:31:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-03 12:16:53","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":59,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16C9.06c","SPAC1039.02","SPAC19A8.08","SPBC29B5.01","SPBC21C3.16c","SPAC139.04c","SPCC663.07c","SPBC18E5.14c","SPCC757.07c","SPBC1683.07","SPBC8E4.01c","SPAC27D7.11c","SPAC25H1.03","SPBC21C3.19","SPBC1347.07","SPCC622.17","SPBC1861.02","SPAPB24D3.07c","SPAC11D3.01c","SPAC11G7.05c","SPAC17A2.09c","SPAC23D3.12","SPAC750.08c","SPCC794.12c","SPCC18B5.02c","SPBC3E7.06c","SPAC1687.16c","SPBC32F12.03c","SPAC56F8.14c","SPAC922.04","SPBC23G7.10c","SPNCRNA.9001","SPBC1773.14","SPAC21E11.03c","SPAC27D7.09c","SPCC1884.02","SPBC23G7.12c","SPBC660.15","SPBP8B7.12c","SPBPB2B2.06c","SPCC1281.07c","SPAP8A3.04c","SPBC887.17","SPCC965.05c","SPAC343.12","SPBC16A3.18","SPAC922.03","SPCC794.03","SPAC12G12.03","SPAC212.09c","SPBC409.04c","SPAC24B11.06c"],"gene_count":52,"ltp_gene_count":6,"approved_date":"2015-12-22"},{"uniquename":"PMID:16921551","title":"Increased TCA cycle activity and reduced oxygen consumption during cytochrome P450-dependent biotransformation in fission yeast.","citation":"Yeast 2006 Aug;23(11):779-94","abstract":"Cytochrome P450s are haem-containing monooxygenases that catalyse a variety of oxidations utilizing a large substrate spectrum and are therefore of interest for biotechnological applications. We expressed human CYP21 in fission yeast Schizosaccharomyces pombe as a eukaryotic model for P450-dependent whole-cell biotransformation. The resulting strain displayed strong steroid hydroxylase activity that was accompanied by contrary effects on respiration and non-respiratory oxygen consumption, which combined to a significant decline in total oxygen consumption of the cells. While production of ROS (reactive oxygen species) decreased, the TCA cycle activity increased, as was shown by metabolic flux (METAFoR) analysis. Pentose phosphate pathway (PPP) activity was found to be negligible, regardless of growth phase, CYP21 expression or biocatalytic activity, indicating that NADPH levels in Sz. pombe are sufficiently high to support an exogenous P450 without adaptations of central carbon metabolism. We conclude from these data that neither oxygen supply nor NADPH availability are limiting factors in P450-dependent biocatalysis in Sz. pombe.","authors":"Dragan CA, Blank LM, Bureik M","authors_abbrev":"Dragan CA et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-22","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26499799","title":"Probing the Mec1ATR Checkpoint Activation Mechanism with Small Peptides.","citation":"J Biol Chem 2016 Jan 01;291(1):393-401","abstract":"Yeast Mec1, the ortholog of human ATR, is the apical protein kinase that initiates the cell cycle checkpoint in response to DNA damage and replication stress. The basal activity of Mec1 kinase is activated by cell cycle phase-specific activators. Three distinct activators stimulate Mec1 kinase using an intrinsically disordered domain of the protein. These are the Ddc1 subunit of the 9-1-1 checkpoint clamp (ortholog of human and Schizosaccharomyces pombe Rad9), the replication initiator Dpb11 (ortholog of human TopBP1 and S. pombe Cut5), and the multifunctional nuclease/helicase Dna2. Here, we use small peptides to determine the requirements for Mec1 activation. For Ddc1, we identify two essential aromatic amino acids in a hydrophobic environment that when fused together are proficient activators. Using this increased insight, we have been able to identify homologous motifs in S. pombe Rad9 that can activate Mec1. Furthermore, we show that a 9-amino acid Dna2-based peptide is sufficient for Mec1 activation. Studies with mutant activators suggest that binding of an activator to Mec1 is a two-step process, the first step involving the obligatory binding of essential aromatic amino acids to Mec1, followed by an enhancement in binding energy through interactions with neighboring sequences.","doi":"10.1074/jbc.M115.687145","authors":"Wanrooij PH, Tannous E, Kumar S, Navadgi-Patil VM, Burgers PM","authors_abbrev":"Wanrooij PH et al.","pubmed_publication_date":"01 Jan 2016","pubmed_entrez_date":"2015-10-27","publication_year":"2016","canto_session_key":"1a738af2bae8f80d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-04-05 08:59:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-04-05 08:59:26","canto_added_date":"2015-10-28 01:19:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-04-05"},{"uniquename":"PMID:18199682","title":"Cation diffusion facilitator Cis4 is implicated in Golgi membrane trafficking via regulating zinc homeostasis in fission yeast.","citation":"Mol Biol Cell 2008 Apr;19(4):1295-303","abstract":"We screened for mutations that confer sensitivities to the calcineurin inhibitor FK506 and to a high concentration of MgCl(2) and isolated the cis4-1 mutant, an allele of the gene encoding a cation diffusion facilitator (CDF) protein that is structurally related to zinc transporters. Consistently, the addition of extracellular Zn(2+) suppressed the phenotypes of the cis4 mutant cells. The cis4 mutants and the mutant cells of another CDF-encoding gene SPBC16E9.14c (we named zrg17(+)) shared common and nonadditive zinc-suppressible phenotypes, and Cis4 and Zrg17 physically interacted. Cis4 localized at the cis-Golgi, suggesting that Cis4 is responsible for Zn(2+) uptake to the cis-Golgi. The cis4 mutant cells showed phenotypes such as weak cell wall and decreased acid phosphatase secretion that are thought to be resulting from impaired membrane trafficking. In addition, the cis4 deletion cells showed synthetic growth defects with all the four membrane-trafficking mutants tested, namely ypt3-i5, ryh1-i6, gdi1-i11, and apm1-1. Interestingly, the addition of extracellular Zn(2+) significantly suppressed the phenotypes of the ypt3-i5 and apm1-1 mutant cells. These results suggest that Cis4 forms a heteromeric functional complex with Zrg17 and that Cis4 is implicated in Golgi membrane trafficking through the regulation of zinc homeostasis in fission yeast.","authors":"Fang Y, Sugiura R, Ma Y, Yada-Matsushima T, Umeno H, Kuno T","authors_abbrev":"Fang Y et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-01-18","publication_year":"2008","canto_session_key":"758942e0a4ac0491","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17D4.03c","SPAC18G6.03","SPBC16E9.14c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11408483","title":"Binding and repair of mismatched DNA mediated by Rhp14, the fission yeast homologue of human XPA.","citation":"J Biol Chem 2001 Aug 17;276(33):30766-72","abstract":"Rhp14 of Schizosaccharomyces pombe is homologous to human XPA and Saccharomyces cerevisiae Rad14, which act in nucleotide excision repair of DNA damages induced by ultraviolet light and chemical agents. Cells with disrupted rhp14 were highly sensitive to ultraviolet light, and epistasis analysis with swi10 (nucleotide excision repair) and rad2 (Uve1-dependent ultraviolet light damage repair pathway) revealed that Rhp14 is an important component of nucleotide excision repair for ultraviolet light-induced damages. Moreover, defective rhp14 caused instability of a GT repeat, similar to swi10 and synergistically with msh2 and exo1. Recombinant Rhp14 with an N-terminal hexahistidine tag was purified from Escherichia coli. Complementation studies with a rhp14 mutant demonstrated that the tagged Rhp14 is functional in repair of ultraviolet radiation-induced damages and in mitotic mutation avoidance. In bandshift assays, Rhp14 showed a preference to substrates with mismatched and unpaired nucleotides. Similarly, XPA bound more efficiently to C/C, A/C, and T/C mismatches than to homoduplex DNA. Our data show that mismatches and loops in DNA are substrates of nucleotide excision repair. Rhp14 is likely part of the recognition complex but alone is not sufficient for the high discrimination of nucleotide excision repair for modified DNA.","authors":"Hohl M, Christensen O, Kunz C, Naegeli H, Fleck O","authors_abbrev":"Hohl M et al.","pubmed_publication_date":"17 Aug 2001","pubmed_entrez_date":"2001-06-16","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC649.03","SPBC4F6.15c","SPAC3G6.06c"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:28117401","title":"Transient structural variations have strong effects on quantitative traits and reproductive isolation in fission yeast.","citation":"Nat Commun 2017 Jan 24;8:14061","abstract":"Large structural variations (SVs) within genomes are more challenging to identify than smaller genetic variants but may substantially contribute to phenotypic diversity and evolution. We analyse the effects of SVs on gene expression, quantitative traits and intrinsic reproductive isolation in the yeast Schizosaccharomyces pombe. We establish a high-quality curated catalogue of SVs in the genomes of a worldwide library of S. pombe strains, including duplications, deletions, inversions and translocations. We show that copy number variants (CNVs) show a variety of genetic signals consistent with rapid turnover. These transient CNVs produce stoichiometric effects on gene expression both within and outside the duplicated regions. CNVs make substantial contributions to quantitative traits, most notably intracellular amino acid concentrations, growth under stress and sugar utilization in winemaking, whereas rearrangements are strongly associated with reproductive isolation. Collectively, these findings have broad implications for evolution and for our understanding of quantitative traits including complex human diseases.","doi":"10.1038/ncomms14061","authors":"Jeffares DC, Jolly C, Hoti M, Speed D, Shaw L, Rallis C, Balloux F, Dessimoz C, Bähler J, Sedlazeck FJ","authors_abbrev":"Jeffares DC et al.","pubmed_publication_date":"24 Jan 2017","pubmed_entrez_date":"2017-01-25","publication_year":"2017","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2017-01-26 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23820557","title":"Secretory production of ricinoleic acid in fission yeast Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2013 Oct;97(19):8663-71","abstract":"We have succeeded to produce a high content of ricinoleic acid (RA), a hydroxylated fatty acid with great values as a petrochemical replacement, in fission yeast Schizosaccharomyces pombe by introducing Claviceps purpurea oleate Δ12-hydroxylase gene (CpFAH12). Although the production was toxic to S. pombe cells, we solved the problem by identifying plg7, encoding phospholipase A2, as a multicopy suppressor. Characterization of the RA-tolerant strains suggested that the removal of RA moieties from phospholipids would be the suppression mechanism by plg7. In this study, we extended our analysis and report our new discovery that the overexpression of plg7 enabled cells to secrete free RA into culture media. When the FAH12 integrant in the absence of the overexpressed plg7 was grown at 20 °C for 11 days, the amount of intracellular RA reached 200.1 μg/ml of culture and only 69.3 μg/ml of RA was detected in culture media. On the other hand, the FAH12 integrant harboring the plg7 multicopy plasmid secreted RA in the media (184.5 μg/ml) without decreasing the amount in the cells, i.e., a significantly higher total secretion and a lead to making RA by its secretory production in S. pombe.","doi":"10.1007/s00253-013-5060-1","authors":"Yazawa H, Kumagai H, Uemura H","authors_abbrev":"Yazawa H et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-07-04","publication_year":"2013","canto_session_key":"9b92d291d7690673","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-05-17 14:20:32","canto_approved_date":"2019-05-17 14:20:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-17 14:20:16","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC106.11c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-05-17"},{"uniquename":"PMID:14673172","title":"Transcription termination factor reb1p causes two replication fork barriers at its cognate sites in fission yeast ribosomal DNA in vivo.","citation":"Mol Cell Biol 2004 Jan;24(1):398-406","abstract":"Polar replication fork barriers (RFBs) near the 3' end of the rRNA transcriptional unit are a conserved feature of ribosomal DNA (rDNA) replication in eukaryotes. In the mouse, in vivo studies indicate that the cis-acting Sal boxes required for rRNA transcription termination are also involved in replication fork blockage. On the contrary, in the budding yeast Saccharomyces cerevisiae, the rRNA transcription termination factors are not required for RFBs. Here we characterized the rDNA RFBs in the fission yeast Schizosaccharomyces pombe. S. pombe rDNA contains three closely spaced polar replication barriers named RFB1, RFB2, and RFB3 in the 3' to 5' order. The transcription termination protein reb1 and its two binding sites, present at the 3' end of the coding region, were required for fork arrest at RFB2 and RFB3 in vivo. On the other hand, fork arrest at the strongest RFB1 barrier was independent of the above transcription termination factors. Therefore, RFB2 and RFB3 resemble the barriers present in the mouse rDNA, whereas RFB1 is similar to the budding yeast RFBs. These results suggest that during evolution, cis- and trans-acting factors required for rRNA transcription termination became involved in replication fork blockage also. S. pombe is suggested to be a transitional species in which both mechanisms coexist.","authors":"Sánchez-Gorostiaga A, López-Estraño C, Krimer DB, Schvartzman JB, Hernández P","authors_abbrev":"Sánchez-Gorostiaga A et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2003-12-16","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1198.11c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:12761200","title":"Characterization of novel acetyltransferases found in budding and fission yeasts that detoxify a proline analogue, azetidine-2-carboxylic acid.","citation":"J Biochem 2003 Jan;133(1):67-74","abstract":"We recently found that budding yeast Saccharomyces cerevisiae sigma1278b, but not genome project strain S288C, has a gene conferring resistance to L-azetidine-2-carboxylic acid (AZC), a toxic four-membered ring analogue of L-proline. Also, the gene, designated as MPR1, encodes a novel acetyltransferase that detoxifies AZC via acetylation. We now report the results of subsequent work. On a homology search with MPR1, we detected a gene in fission yeast Schizosaccharomyces pombe. This gene, designated as ppr1(+) (pombe MPR1), is responsible for the AZC-resistance of S. pombe as judged from the results of gene disruption and overexpression experiments. Escherichia coli cells expressing ppr1(+), like ones expressing MPR1, were resistant to AZC and produced an AZC acetyltransferase. We further found that the enzymes encoded by MPR1 and ppr1(+) were homodimers, and catalyzed the acetylation of AZC but not any other L-proline-related compounds. Ppr1p was more thermostable than Mpr1p, although Ppr1p had a lower optimum temperature than Mpr1p. The higher AZC acetylation activity of Mpr1p, in comparison to that of Ppr1p, was attributed to the larger k(cat)/K(m) value for acetyl-CoA of Mpr1p than that of Ppr1p.","authors":"Nomura M, Nakamori S, Takagi H","authors_abbrev":"Nomura M et al.","pubmed_publication_date":"Jan 2003","pubmed_entrez_date":"2003-05-23","publication_year":"2003","canto_session_key":"3988f705e0240ebe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-07-02 08:30:26","canto_approved_date":"2019-05-04 10:27:39","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-02 08:30:20","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC21E11.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-02"},{"uniquename":"PMID:23422000","title":"Regulatory motifs in Chk1.","citation":"Cell Cycle 2013 Mar 15;12(6):916-22","abstract":"Chk1 is the effector kinase of the G 2 DNA damage checkpoint. Chk1 homologs possess a highly conserved N-terminal kinase domain and a less conserved C-terminal regulatory domain. In response to DNA damage, Chk1 is recruited to mediator proteins assembled at lesions on replication protein A (RPA)-coated single-stranded DNA (ssDNA). Chk1 is then activated by phosphorylation on S345 in the C-terminal regulatory domain by the PI3 kinase-related kinases ATM and ATR to enforce a G 2 cell cycle arrest to allow time for DNA repair. Models have emerged in which this C-terminal phosphorylation relieves auto-inhibitory regulation of the kinase domain by the regulatory domain. However, experiments in fission yeast have shown that deletion of this putative auto-inhibitory domain actually inactivates Chk1 function. We show here that Chk1 homologs possess a kinase-associated 1 (KA1) domain that possesses residues previously implicated in Chk1 auto-inhibition. In addition, all Chk1 homologs have a small and highly conserved C-terminal extension (CTE domain). In fission yeast, both of these motifs are essential for Chk1 activation through interaction with the mediator protein Crb2, the homolog of human 53BP1. Thus, through different intra- and intermolecular interactions, these motifs explain why the regulatory domain exerts both positive and negative control over Chk1 activation. Such motifs may provide alternative targets to the ATP-binding pocket on which to dock Chk1 inhibitors as anticancer therapeutics.","doi":"10.4161/cc.23881","authors":"Caparelli ML, O'Connell MJ","authors_abbrev":"Caparelli ML et al.","pubmed_publication_date":"15 Mar 2013","pubmed_entrez_date":"2013-02-21","publication_year":"2013","canto_session_key":"94dcf9a5e6dce38f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC342.05","SPCC1259.13"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11882285","title":"Requirement of chromatid cohesion proteins rad21/scc1 and mis4/scc2 for normal spindle-kinetochore interaction in fission yeast.","citation":"Curr Biol 2002 Mar 05;12(5):347-58","abstract":"Proteins conserved from yeast to human hold two sister chromatids together. The failure to form cohesion in the S phase results in premature separation of chromatids in G2/M. Mitotic kinetochores free from microtubules or the lack of tension are known to activate spindle checkpoint.\nThe loss of chromatid cohesion in fission yeast mutants (mis4-242 and rad21-K1) leads to the activation of Mad2- and Bub1-dependent checkpoint, possibly due to a diminished microtubule-kinetochore interaction. Bub1, a checkpoint kinase, localizes briefly at early mitotic kinetochores in wild-type, whereas the cohesion mutation greatly increases the duration of kinetochore localization. Bub1 is bound to the central centromere region of mitotic cells. These cohesion mutants are hypersensitive to a tubulin poison and are synthetic lethal with dis1 and bir1/cut17, which are defective in microtubule-kinetochore interaction. The formation of specialized centromere chromatin containing CENP-A does not require cohesion. Dominant-negative noncleavable Rad21 fails to activate checkpoint but blocks sister chromatid separation and full spindle elongation in anaphase.\nMis4 and Rad21 (budding yeast Scc2 and Scc1 homologs, respectively) act in establishing the normal spindle-kinetochore interaction in early mitosis and inhibit sister chromatid separation until the cleavage of Rad21 in anaphase. Checkpoint directly or indirectly monitors the states of cohesion in early mitosis. Full spindle extension occurs with unequal nuclear division in cohesion mutants in the absence of Mad2.","authors":"Toyoda Y, Furuya K, Goshima G, Nagao K, Takahashi K, Yanagida M","authors_abbrev":"Toyoda Y et al.","pubmed_publication_date":"05 Mar 2002","pubmed_entrez_date":"2002-03-08","publication_year":"2002","canto_session_key":"9dc7446c41f69cf6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-05-02 16:23:14","canto_approved_date":"2025-09-03 10:16:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-02 16:12:52","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC962.02c","SPCC338.17c","SPBC20F10.06","SPAC31A2.05c","SPCC1322.12c","SPBC14C8.01c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2018-05-02"},{"uniquename":"PMID:17190604","title":"The Schizosaccharomyces pombe EB1 homolog Mal3p binds and stabilizes the microtubule lattice seam.","citation":"Cell 2006 Dec 29;127(7):1415-24","abstract":"End binding 1 (EB1) proteins are highly conserved regulators of microtubule dynamics. Using electron microscopy (EM) and high-resolution surface shadowing we have studied the microtubule-binding properties of the fission yeast EB1 homolog Mal3p. This allowed for a direct visualization of Mal3p bound on the surface of microtubules. Mal3p particles usually formed a single line on each microtubule along just one of the multiple grooves that are formed by adjacent protofilaments. We provide structural data showing that the alignment of Mal3p molecules coincides with the microtubule lattice seam as well as data suggesting that Mal3p not only binds but also stabilizes this seam. Accordingly, Mal3p stabilizes microtubules through a specific interaction with what is potentially the weakest part of the microtubule in a way not previously demonstrated. Our findings further suggest that microtubules exhibit two distinct reaction platforms on their surface that can independently interact with target structures such as microtubule-associated proteins, motors, kinetochores, or membranes.","authors":"Sandblad L, Busch KE, Tittmann P, Gross H, Brunner D, Hoenger A","authors_abbrev":"Sandblad L et al.","pubmed_publication_date":"29 Dec 2006","pubmed_entrez_date":"2006-12-28","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPBC800.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:19160458","title":"Improved tools for efficient mapping of fission yeast genes: identification of microtubule nucleation modifier mod22-1 as an allele of chromatin- remodelling factor gene swr1.","citation":"Yeast 2008 Dec;25(12):913-25","abstract":"Fission yeast genes identified in genetic screens are usually cloned by transformation of mutants with plasmid libraries. However, for some genes this can be difficult, and positional cloning approaches are required. The mutation swi5-39 reduces recombination frequency in homozygous crosses and has been used as a tool in mapping gene position (Schmidt, 1993). However, strain construction in swi5-39-based mapping is significantly more laborious than is desirable. Here we describe a set of strains designed to make swi5-based mapping more efficient and more powerful. The first improvement is the use of a swi5Delta strain marked with kanamycin (G418) resistance, which greatly facilitates identification of swi5 mutants. The second improvement, which follows directly from the first, is the introduction of a large number of auxotrophic markers into mapping strains, increasing the likelihood of finding close linkage between a marker and the mutation of interest. We combine these new mapping strains with a rec12Delta-based approach for initial mapping of a mutation to an individual chromosome. Together, the two methods allow an approximate determination of map position in only a small number of crosses. We used these to determine that mod22-1, a modifier of microtubule nucleation phenotypes, encodes a truncation allele of Swr1, a chromatin-remodelling factor involved in nucleosomal deposition of H2A.Z histone variant Pht1. Expression microarray analysis of mod22-1, swr1Delta and pht1Delta cells suggests that the modifier phenotype of mod22-1 mutants may be due to small changes in expression of one or more genes involved in tubulin function.","doi":"10.1002/yea.1639","authors":"Anders A, Watt S, Bähler J, Sawin KE","authors_abbrev":"Anders A et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2009-01-23","publication_year":"2008","canto_session_key":"f02a981bd70740a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-03-19 11:22:57","canto_approved_date":"2022-11-21 11:21:36","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-03-19 11:22:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.13c","SPAC11E3.01c","SPBC211.06","SPBC11B10.10c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2014-03-19"},{"uniquename":"PMID:15689108","title":"Ferrichrome in Schizosaccharomyces pombe--an iron transport and iron storage compound.","citation":"Biometals 2004 Dec;17(6):647-54","abstract":"Schizosaccharomyces pombe has been assumed not to produce siderophores. Nevertheless, the genomic sequence of this fission yeast revealed the presence of siderophore biosynthetic genes for hydroxamates. Applying a bioassay based on an Aspergillus nidulans strain deficient in siderophore biosynthesis, and using reversed-phase HPLC and mass spectrometry analysis, we demonstrate that S. pombe excretes and accumulates intracellularly the hydroxamate-type siderophore ferrichrome. Under iron-limiting conditions, the cellular ferrichrome pool was present in the desferri-form, while under iron-richconditions, in the ferri-form. In contrast to S. pombe, hydroxamate-type siderophores could not be detected intwo other yeast species, Saccharomyces cerevisiae and Candida albicans.","authors":"Schrettl M, Winkelmann G, Haas H","authors_abbrev":"Schrettl M et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2005-02-04","publication_year":"2004","canto_session_key":"a9805b74391d294c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-06-05 08:23:28","canto_approved_date":"2019-06-05 08:23:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-06-05 08:23:21","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC23G3.03","SPAC23G3.02c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2019-06-05"},{"uniquename":"PMID:2840284","title":"The S.pombe mei2 gene encoding a crucial molecule for commitment to meiosis is under the regulation of cAMP.","citation":"EMBO J 1988 Mar;7(3):761-7","abstract":"The complete nucleotide sequence of the mei2 gene of Schizosaccharomyces pombe, which is essential for initiation of meiosis, is presented and four transcriptional start sites assigned. Transcription of mei2 and other genes involved in life cycle control of S. pombe, which is inducible by nitrogen starvation, is inhibited by addition of cAMP, suggesting that cAMP can mediate the signal of nitrogen supply in S.pombe. mei2 is the furthest downstream among target genes regulated by cAMP and genetic or physiological factors so far shown to block uncontrolled meiosis in S.pombe, which is provoked by inactivation of the part1 gene product, are either mutations at the mei2 locus or inhibitors of its expression. Cooperation of two regulatory pathways, one leading to the inactivation of pat1 activity and the other to the supply of the mei2 product, appears to commit cells to meiosis in S.pombe.","authors":"Watanabe Y, Lino Y, Furuhata K, Shimoda C, Yamamoto M","authors_abbrev":"Watanabe Y et al.","pubmed_publication_date":"Mar 1988","pubmed_entrez_date":"1988-03-01","publication_year":"1988","canto_session_key":"e2075e32cd765cb6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-30 16:08:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-02 13:54:45","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPBC119.04","SPBC119.11c","SPBC19C2.05"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2014-05-02"},{"uniquename":"PMID:30649994","title":"A conserved mechanism for mitochondria-dependent dynein anchoring.","citation":"Mol Biol Cell 2019 Mar 01;30(5):691-702","abstract":"Mitochondrial anchors have functions that extend beyond simply positioning mitochondria. In budding yeast, mitochondria drive the assembly of the mitochondrial anchor protein Num1 into clusters, which serve to anchor mitochondria as well as dynein to the cell cortex. Here, we explore a conserved role for mitochondria in dynein anchoring by examining the tethering functions of the evolutionarily distant Schizosaccharomyces pombe Num1 homologue. In addition to its function in dynein anchoring, we find that S. pombe Num1, also known as Mcp5, interacts with and tethers mitochondria to the plasma membrane in S. pombe and Saccharomyces cerevisiae. Thus, the mitochondria and plasma membrane-binding domains of the Num1 homologues, as well as the membrane features these domains recognize, are conserved. In S. pombe, we find that mitochondria impact the assembly and cellular distribution of Num1 clusters and that Num1 clusters actively engaged in mitochondrial tethering serve as cortical attachment sites for dynein. Thus, mitochondria play a critical and conserved role in the formation and distribution of dynein-anchoring sites at the cell cortex and, as a consequence, impact dynein function. These findings shed light on an ancient mechanism of mitochondria-dependent dynein anchoring that is conserved over more than 450 million years of evolution, raising the intriguing possibility that the role mitochondria play in dynein anchoring and function extends beyond yeast to higher eukaryotes.","doi":"10.1091/mbc.E18-07-0466","authors":"Kraft LM, Lackner LL","authors_abbrev":"Kraft LM et al.","pubmed_publication_date":"01 Mar 2019","pubmed_entrez_date":"2019-01-17","publication_year":"2019","canto_session_key":"bb94978e6c7b86d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Laura Lackner","canto_first_approved_date":"2019-06-05 08:15:11","canto_approved_date":"2026-02-25 17:51:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-20 21:05:48","canto_added_date":"2019-01-18 01:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Laura Lackner","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.08","SPBC25B2.07c","SPBC216.02","SPAC1093.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-06-05"},{"uniquename":"PMID:26255844","title":"Tethering of SCF(Dia2) to the Replisome Promotes Efficient Ubiquitylation and Disassembly of the CMG Helicase.","citation":"Curr Biol 2015 Aug 31;25(17):2254-9","abstract":"Disassembly of the Cdc45-MCM-GINS (CMG) DNA helicase, which unwinds the parental DNA duplex at eukaryotic replication forks, is the key regulated step during replication termination but is poorly understood. In budding yeast, the F-box protein Dia2 drives ubiquitylation of the CMG helicase at the end of replication, leading to a disassembly pathway that requires the Cdc48 segregase. The substrate-binding domain of Dia2 comprises leucine-rich repeats, but Dia2 also has a TPR domain at its amino terminus that interacts with the Ctf4 and Mrc1 subunits of the replisome progression complex, which assembles around the CMG helicase at replication forks. Previous studies suggested two disparate roles for the TPR domain of Dia2, either mediating replisome-specific degradation of Mrc1 and Ctf4 or else tethering SCF(Dia2) (SCF [Skp1/cullin/F-box protein]) to the replisome to increase its local concentration at replication forks. Here, we show that SCF(Dia2) does not mediate replisome-specific degradation of Mrc1 and Ctf4, either during normal S phase or in response to replication stress. Instead, the tethering of SCF(Dia2) to the replisome progression complex increases the efficiency of ubiquitylation of the Mcm7 subunit of CMG, both in vitro and in vivo. Correspondingly, loss of tethering reduces the efficiency of CMG disassembly in vivo and is synthetic lethal in combination with a disassembly-defective allele of CDC48. Residual ubiquitylation of Mcm7 in dia2-ΔTPR cells is still CMG specific, highlighting the complex regulation of the final stages of chromosome replication, about which much still remains to be learned.","doi":"10.1016/j.cub.2015.07.012","authors":"Maculins T, Nkosi PJ, Nishikawa H, Labib K","authors_abbrev":"Maculins T et al.","pubmed_publication_date":"31 Aug 2015","pubmed_entrez_date":"2015-08-11","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1E7.02c","SPCC338.16"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:41090244","title":"Decreased Mitochondrial Translation Suppresses 3,3'-Diindolylmethane-Induced Reactive Oxygen Species Generation in Schizosaccharomyces Pombe.","citation":"Genes Cells 2025 Nov;30(6):e70056","abstract":"Broccoli-derived 3,3'-diindolylmethane (DIM) exhibits anticancer effects. The compound also inhibits the growth of fission yeast cells. Reduction of mitochondrial translation alleviates the growth defects caused by DIM in fission yeast; however, the underlying molecular mechanisms remain unclear. In this study, we show that DIM-induced reactive oxygen species (ROS) colocalized with mitochondria. Deletion of tsf1 + , which leads to reduced mitochondrial translation, suppressed this colocalization. Deletions of stress response genes, such as sty1 + , pap1 + , and atf1 + , increased DIM sensitivity. Growth defects in the wild-type and sty1, pap1, and atf1 disruptants in the presence of DIM were suppressed by the ROS scavenger N-acetylcysteine. Moreover, the ROS scavenger Sod1, which is suggested to function in the mitochondrial intermembrane space and cytoplasm, was important for survival in the presence of DIM. Collectively, the study results suggest that DIM increases ROS levels in mitochondria and suppression of ROS increase in mitochondria via inhibition of mitochondrial translation is the mechanism by which DIM-induced growth defects in wild-type cells are suppressed. Overall, the study highlights the potential use of DIM as an anticancer drug to increase ROS generation in mitochondria in cancer cells.","doi":"10.1111/gtc.70056","authors":"Wang K, Osawa H, Nagai H, Ueno M","authors_abbrev":"Wang K et al.","pubmed_publication_date":"Nov 2025","pubmed_entrez_date":"2025-10-15","publication_year":"2025","canto_session_key":"acf7d5e31dcc1495","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-15 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22586919","title":"Construction of the industrial ethanol-producing strain of Saccharomyces cerevisiae able to ferment cellobiose and melibiose.","citation":"Prikl Biokhim Mikrobiol 2012;48(2):243-8","abstract":"The gene mel1, encoding alpha-galactosidase in Schizosaccharomyces pombe, and the gene bgl2, encoding and beta-glucosidase in Trichoderma reesei, were isolated and co-expressed in the industrial ethanol-producing strain of Saccharomyces cerevisiae. The resulting strains were able to grow on cellobiose and melibiose through simultaneous production of sufficient extracellular alpha-galactosidase and beta-glucosidase activity. Under aerobic conditions, the growth rate of the recombinant strain GC 1 co-expressing 2 genes could achieve 0.29 OD600 h(-1) and a biomass yield up to 7.8 g l(-1) dry cell weight on medium containing 10.0 g l(-1) cellobiose and 10.0 g l(-1) melibiose as sole carbohydrate source. Meanwhile, the new strain of S. cerevisiae CG 1 demonstrated the ability to directly produce ethanol from microcrystalline cellulose during simultaneous saccharification and fermentation process. Approximately 36.5 g l(-1) ethanol was produced from 100 g of cellulose supplied with 5 g l(-1) melibose within 60 h. The yield (g of ethanol produced/g of carbohydrate consumed) was 0.44 g/g, which corresponds to 88.0% of the theoretical yield.","authors":"Zhang L, Guo ZP, Ding ZY, Wang ZX, Shi GY","authors_abbrev":"Zhang L et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-05-17","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000104","title":"Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features.","abstract":"GO terms are manually assigned to each rule in UniRule. These rules are prepared manually by UniProt curators based on the annotations present in reviewed UniProtKB/Swiss-Prot records that share sequence features, sequence similarity and taxonomy. The assigned GO terms are then transferred to all unreviewed UniProtKB/TrEMBL proteins that meet the conditions given in the UniRule rule. GO annotations using this technique receive the evidence code Inferred from Electronic Annotation (IEA; ECO:0000501). These annotations are updated regularly by UniProt and are available for download on both the GO and GOA EBI ftp sites. To report an annotation error or inconsistency, or for further information, please contact the UniProt Automated Annotation team at automated_annotation@ebi.ac.uk. UniRule is a collaboration between the European Bioinformatics Institute (EMBL-EBI), the Swiss Institute of Bioinformatics (SIB), and the Protein Information Resource at Georgetown University (PIR). For further information, please see UniProt: a hub for protein information Nucleic Acids Res. 2015, 43, D204, doi: 10.1093/nar/gku989 or www.uniprot.org.","authors":"UniProt curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1271.14","SPBC2F12.14c","SPBC29A10.01","SPAC16C9.02c","SPBC336.14c","SPBC1198.02","SPAC821.05","SPAC1834.02","SPAC1F3.04c","SPBC887.14c","SPAC4A8.16c","SPAC3A12.13c","SPAC23C11.09","SPAC25G10.08","SPAC1751.03","SPBC19F5.05c","SPAC1687.11","SPCC1620.08","SPBC887.01","SPAC144.03","SPBC146.12","SPBC4F6.13c","SPAC222.14c","SPBC17D11.05","SPAC20H4.05c","SPAC4G9.03","SPAC27E2.03c","SPAC25B8.03","SPBC1683.02","SPBC16E9.18","SPAC57A10.14","SPBC6B1.12c","SPBC337.10c","SPCC830.10","SPBP35G2.09","SPBC14C8.03","SPBC18H10.03","SPAC22H10.05c","SPCC4G3.04c","SPBC4C3.07","SPAC56F8.04c","SPAC3G6.06c","SPAC1687.12c","SPBC16G5.02c","SPBC646.09c","SPAC4D7.05","SPAC31G5.15","SPCC1235.16","SPAC8F11.09c","SPAC1296.06","SPAC4G9.15"],"gene_count":51,"ltp_gene_count":0},{"uniquename":"PMID:21658004","title":"Altering the stability of the Cdc8 overlap region modulates the ability of this tropomyosin to bind co-operatively to actin and regulate myosin.","citation":"Biochem J 2011 Sep 01;438(2):265-73","abstract":"Tm (tropomyosin) is an evolutionarily conserved α-helical coiled-coil protein, dimers of which form end-to-end polymers capable of associating with and stabilizing actin filaments, and regulating myosin function. The fission yeast Schizosaccharomyces pombe possesses a single essential Tm, Cdc8, which can be acetylated on its N-terminal methionine residue to increase its affinity for actin and enhance its ability to regulate myosin function. We have designed and generated a number of novel Cdc8 mutant proteins with N-terminal substitutions to explore how stability of the Cdc8 overlap region affects the regulatory function of this Tm. By correlating the stability of each protein, its propensity to form stable polymers, its ability to associate with actin and to regulate myosin, we have shown that the stability of the N-terminal of the Cdc8 α-helix is crucial for Tm function. In addition we have identified a novel Cdc8 mutant with increased N-terminal stability, dimers of which are capable of forming Tm polymers significantly longer than the wild-type protein. This protein had a reduced affinity for actin with respect to wild-type, and was unable to regulate actomyosin interactions. The results of the present paper are consistent with acetylation providing a mechanism for modulating the formation and stability of Cdc8 polymers within the fission yeast cell. The data also provide evidence for a mechanism in which Tm dimers form end-to-end polymers on the actin filament, consistent with a co-operative model for Tm binding to actin.","doi":"10.1042/BJ20101316","authors":"East DA, Sousa D, Martin SR, Edwards TA, Lehman W, Mulvihill DP","authors_abbrev":"East DA et al.","pubmed_publication_date":"01 Sep 2011","pubmed_entrez_date":"2011-06-11","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27F1.02c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:21244825","title":"Precision of sensing cell length via concentration gradients.","citation":"Biophys J 2011 Jan 19;100(2):294-303","abstract":"Unicellular organisms are typically found to have a characteristic cell size. To achieve a homeostatic distribution of cell sizes over many generations requires that cell length is actively sensed and regulated. However, the mechanisms by which cell size is controlled remain poorly understood. Recent experiments in fission yeast have shown that cell length is controlled in part by polar gradients of the protein Pom1 together with localized measurement of concentration at midcell. Dilution as the cell grows leads to a reduction in the midcell protein concentration, which lifts a block on mitosis. Here we analyze the precision of this mechanism for length sensing in the presence of inevitable intrinsic noise in the processes leading to formation and measurement of this gradient. We find that the use of concentration gradients allows for more robust length sensing than a comparable spatially uniform system, and allows for reliable length determination even if the average protein concentration throughout the cell remains constant as the cell grows. Optimal values for the gradient decay length and receptor dissociation constant emerge from maximizing sensitivity while minimizing the impact of density fluctuations.","doi":"10.1016/j.bpj.2010.11.046","authors":"Tostevin F","authors_abbrev":"Tostevin F","pubmed_publication_date":"19 Jan 2011","pubmed_entrez_date":"2011-01-20","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15990877","title":"Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p for mRNA export in fission yeast.","citation":"EMBO J 2005 Jul 20;24(14):2512-23","abstract":"The breast cancer tumor suppressor BRCA2-interacting protein, DSS1, and its homologs are critical for DNA recombination in eukaryotic cells. We found that Dss1p, along with Mlo3p and Uap56p, Schizosaccharomyces pombe homologs of two messenger RNA (mRNA) export factors of the NXF-NXT pathway, is required for mRNA export in S. pombe. Previously, we showed that the nuclear pore-associated Rae1p is an essential mRNA export factor in S. pombe. Here, we show that Dss1p and Uap56p function by linking mRNA adapter Mlo3p to Rae1p for targeting mRNA-protein complex (mRNP) to the proteins of the nuclear pore complex (NPC). Dss1p preferentially recruits to genes in vivo and interacts with -FG (phenylalanine glycine) nucleoporins in vivo and in vitro. Thus, Dss1p may function at multiple steps of mRNA export, from mRNP biogenesis to their targeting and translocation through the NPC.","authors":"Thakurta AG, Gopal G, Yoon JH, Kozak L, Dhar R","authors_abbrev":"Thakurta AG et al.","pubmed_publication_date":"20 Jul 2005","pubmed_entrez_date":"2005-07-02","publication_year":"2005","canto_session_key":"f05818ede1e13eae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-04-15 11:27:43","canto_approved_date":"2024-01-16 15:18:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-11 15:31:46","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.05c","SPAC23D3.06c","SPAC3G6.02","SPBC1D7.04","SPAC17G6.14c","SPAC3C7.08c","SPBC1921.03c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-04-15"},{"uniquename":"Pfam:CL0020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4B3.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38824495","title":"New wheat straw fermentation feed: recombinant  Schizosaccharomyces pombe  efficient degradation of lignocellulose and increase feed protein.","citation":"Prep Biochem Biotechnol 2024 Jun 02;:1-9","abstract":"Wheat straw contains a high amount of lignin, hindering the action of cellulase and hemicellulase enzymes, leading to difficulties in nutrient absorption by animals from straw feed. However, currently, the biological treatment of straw relies primarily on fungal degradation and cannot be directly utilized for the preparation of livestock feed. This study focuses on enzymatic co-fermentation of wheat straw to produce high-protein, low-cellulose biological feed, integrating lignin degradation with feed manufacturing, thereby simplifying the feed production process. After the optimization using Box-Behnken Design for the feed formulation, with a glucose oxidase addition of 2.46%, laccase addition of 3.4%, and malonic acid addition of 0.6%, the wheat straw feed prepared in this experiment exhibited a true protein content of 9.35%. This represented a fourfold increase compared to the non-fermented state, and the lignocellulose degradation rate of wheat straw reached 45.42%. These results not only highlight the substantial enhancement in protein content but also underscore the significant advancement in lignocellulose breakdown. This formulation significantly enhanced the palatability and nutritional value of the straw feed, contributing to the industrial development of straw feed.","doi":"10.1080/10826068.2024.2353637","authors":"Chen X, Liang X, Shi N, He L, Ma Y, Zhu D, Ni Z, Chen H","authors_abbrev":"Chen X et al.","pubmed_publication_date":"02 Jun 2024","pubmed_entrez_date":"2024-06-02","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-06-02 23:25:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12684507","title":"A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis.","citation":"J Biol Chem 2003 Jun 20;278(25):22498-505","abstract":"Deficiency of GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (hALG2), is the cause of a new type of congenital disorders of glycosylation (CDG) designated CDG-Ii. The patient presented normal at birth but developed in the 1st year of life a multisystemic disorder with mental retardation, seizures, coloboma of the iris, hypomyelination, hepatomegaly, and coagulation abnormalities. An accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol was observed in skin fibroblasts of the patient. Incubation of patient fibroblast extracts with Man1GlcNAc2-PP-dolichol and GDP-mannose revealed a severely reduced activity of the mannosyltransferase elongating Man1GlcNAc2-PP dolichol. Because the Saccharomyces cerevisiae mutant alg2-1 was known to accumulate the same shortened dolichol-linked oligosaccharides as the patient, the yeast ALG2 sequence was used to identify the human ortholog. Genetic analysis revealed that the patient was heterozygous for a single nucleotide deletion and a single nucleotide substitution in the human ortholog of yeast ALG2. Expression of wild type but not of mutant hALG2 cDNA restored the mannosyltransferase activity and the biosynthesis of dolichol-linked oligosaccharides both in patient fibroblasts and in the alg2-1 yeast cells. hALG2 was shown to act as an alpha1,3-mannosyltransferase. The resulting Manalpha1,3-ManGlcNAc2-PP dolichol is further elongated by a yet unknown alpha1,6-mannosyltransferase.","authors":"Thiel C, Schwarz M, Peng J, Grzmil M, Hasilik M, Braulke T, Kohlschütter A, von Figura K, Lehle L, Körner C","authors_abbrev":"Thiel C et al.","pubmed_publication_date":"20 Jun 2003","pubmed_entrez_date":"2003-04-10","publication_year":"2003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:5924278","title":"Induction of mitotic segregation with p-fluorophenylalanine in Schizosaccharomyces pombe.","citation":"J Bacteriol 1966 Nov;92(5):1567-8","abstract":"","authors":"Gutz H","authors_abbrev":"Gutz H","pubmed_publication_date":"Nov 1966","pubmed_entrez_date":"1966-11-01","publication_year":"1966","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25883047","title":"Genetic and structural analysis of the essential fission yeast RNA polymerase II CTD phosphatase Fcp1.","citation":"RNA 2015 Jun;21(6):1135-46","abstract":"Protein phosphatases regulate mRNA synthesis and processing by remodeling the carboxy-terminal domain (CTD) of RNA polymerase II (Pol2) to dynamically inscribe a Pol2 CTD code. Fission yeast Fcp1 (SpFcp1) is an essential 723-amino acid CTD phosphatase that preferentially hydrolyzes Ser2-PO4 of the YS(2)PTSPS repeat. The SpFcp1 catalytic domain (aa 140-580) is composed of a DxDxT acyl-phosphatase module (FCPH) and a BRCT module. Here we conducted a genetic analysis of SpFcp1, which shows that (i) phosphatase catalytic activity is required for vegetative growth of fission yeast; (ii) the flanking amino-terminal domain (aa 1-139) and its putative metal-binding motif C(99)H(101)Cys(109)C(112) are essential; (iii) the carboxy-terminal domain (aa 581-723) is dispensable; (iv) a structurally disordered internal segment of the FCPH domain (aa 330-393) is dispensable; (v) lethal SpFcp1 mutations R271A and R299A are rescued by shortening the Pol2 CTD repeat array; and (vi) CTD Ser2-PO4 is not the only essential target of SpFcp1 in vivo. Recent studies highlight a second CTD code involving threonine phosphorylation of a repeat motif in transcription elongation factor Spt5. We find that Fcp1 can dephosphorylate Thr1-PO4 of the fission yeast Spt5 CTD nonamer repeat T(1)PAWNSGSK. We identify Arg271 as a governor of Pol2 versus Spt5 CTD substrate preference. Our findings implicate Fcp1 as a versatile sculptor of both the Pol2 and Spt5 CTD codes. Finally, we report a new 1.45 Å crystal structure of SpFcp1 with Mg(2+) and AlF3 that mimics an associative phosphorane transition state of the enzyme-aspartyl-phosphate hydrolysis reaction.","doi":"10.1261/rna.050286.115","authors":"Schwer B, Ghosh A, Sanchez AM, Lima CD, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-04-18","publication_year":"2015","canto_session_key":"2bbc4c52646dd9ef","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-04-19 00:19:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.19","SPBC25H2.13c","SPAC3G9.04","SPBC28F2.12","SPAC19B12.05c"],"gene_count":5,"ltp_gene_count":5,"pdb_entries":[{"pdb_id":"4xpz","gene_chains":[{"gene_uniquename":"SPAC19B12.05c","chain":"A","position":"149-580"}],"title":"Structure of fission yeast RNA polymerase II CTD phosphatase Fcp1-R271A bound to aluminum fluoride","entry_authors":"Ghosh A,Lima CD","entry_authors_abbrev":"Ghosh A et al.","reference_uniquename":"PMID:25883047","experimental_method":"X-ray","resolution":"1.45"},{"pdb_id":"4xq0","gene_chains":[{"gene_uniquename":"SPAC19B12.05c","chain":"A","position":"149-580"}],"title":"Structure of fission yeast RNA polymerase II CTD phosphatase Fcp1-R271A bound to beryllium fluoride","entry_authors":"Ghosh A,Lima CD","entry_authors_abbrev":"Ghosh A et al.","reference_uniquename":"PMID:25883047","experimental_method":"X-ray","resolution":"1.85"}]},{"uniquename":"PMID:2065367","title":"Characterization of a novel open reading frame, urf a, in the mitochondrial genome of fission yeast: correlation of urf a mutations with a mitochondrial mutator phenotype and a possible role of frameshifting in urf a expression.","citation":"Curr Genet 1991 Feb;19(2):95-102","abstract":"Between the genes for tRNA(gin) and tRNA(ile) an open reading frame of 227 amino acids has been identified which is unique among known mitochondrial genomes and which has been termed urf a (Lang et al. 1983; Kornrumpf et al. 1984). It uses the \"mitochondrial\" genetic code, i.e., it contains a TGA codon, whereas all other protein-encoding genes, and all but one intronic open reading frame, use the \"standard\" genetic code (UGG for tryptophan). A previous paper has demonstrated that \"mutator\" strains show an increased formation of mitochondrial drug-resistant and respiration-deficient mutants (including deletions). In this paper we show that the mutator activity is correlated with mutations in urf a. A detailed analysis of one urf a mutant is presented (anar-6), where the deletion of an A residue leads to a frameshift mutation and consequently to premature termination of the putative protein. The phenotype of colonies originating from a single mutant clone varies from no growth up to full growth on non-fermentable substrate. This phenomenon of phenotypic segregation can be explained by the ability of the cell to perform translational frameshifting. A detailed analysis of the DNA sequence and the putative urf a protein will be presented and a possible function of the protein will be discussed.","authors":"Zimmer M, Krabusch M, Wolf K","authors_abbrev":"Zimmer M et al.","pubmed_publication_date":"Feb 1991","pubmed_entrez_date":"1991-02-01","publication_year":"1991","canto_session_key":"03a090dd69543b04","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-11-20 14:04:33","canto_approved_date":"2024-04-04 14:42:36","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-11-20 14:04:29","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMIT.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-20"},{"uniquename":"PMID:28060464","title":"RNA polymerase II components and Rrn7 form a preinitiation complex on the HomolD box to promote ribosomal protein gene expression in Schizosaccharomyces pombe.","citation":"FEBS J 2017 Feb;284(4):615-633","abstract":"In Schizosaccharomyces pombe, ribosomal protein gene (RPG) promoters contain a TATA box analog, the HomolD box, which is bound by the Rrn7 protein. Despite the importance of ribosome biogenesis for cell survival, the mechanisms underlying RPG transcription remain unknown. In this study, we found that components of the RNA polymerase II (RNAPII) system, consisting of the initiation or general transcription factors (GTFs) TFIIA, IIB, IIE, TATA-binding protein (TBP) and the RNAPII holoenzyme, interacted directly with Rrn7 in vitro, and were able to form a preinitiation complex (PIC) on the HomolD box. PIC complex formation follows an ordered pathway on these promoters. The GTFs and RNAPII can also be cross-linked to HomolD-containing promoters in vivo. In an in vitro reconstituted transcription system, RNAPII components and Rrn7 were necessary for HomolD-directed transcription. The Mediator complex was required for basal transcription from those promoters in whole cell extract (WCE). The Med17 subunit of Mediator also can be cross-linked to the promoter region of HomolD-containing promoters in vivo, suggesting the presence of the Mediator complex on HomolD box-containing promoters. Together, these data show that components of the RNAPII machinery and Rrn7 participate in the PIC assembly on the HomolD box, thereby directing RPG transcription.","doi":"10.1111/febs.14006","authors":"Montes M, Moreira-Ramos S, Rojas DA, Urbina F, Käufer NF, Maldonado E","authors_abbrev":"Montes M et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2017-01-07","publication_year":"2017","canto_session_key":"e1330013c3f979e7","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-06-15 07:39:11","canto_added_date":"2017-01-08 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29E6.08","SPAC16E8.16","SPBC336.09c","SPAC458.07","SPCC553.11c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:11121507","title":"Yeast mutants as a model system for identification of determinants of chemosensitivity.","citation":"Pharmacol Rev 2000 Dec;52(4):477-92","abstract":"The fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae have become valuable tools for the study of basic cellular functions of eukaryotic cells, including DNA repair mechanisms and cell cycle control. Since the major signaling pathways and cellular processes involved in cellular response to cytotoxic agents are conserved between yeasts and mammalian cells, these simple eukaryotic systems could be excellent models for the identification of molecular/cellular mechanisms of sensitivity to antitumor drugs. We describe relevant biological features of yeast cells and potential applications derived by their genetic manipulation. In particular, we have outlined the role of genes involved in repair processes and in checkpoint control, with specific reference to genes regulating radiation-sensitivity. Specific examples are provided concerning the use of both yeasts in understanding the mechanism of action of platinum compounds and topoisomerase inhibitors. The availability of the genomic sequence of these organisms as well as of new technologies (microarrays, proteomics) is expected to allow the identification of potential drug targets, since the drug discovery process is moving toward a genomic orientation. Among eukaryotic organisms, yeasts are suitable for easy genetic manipulations, and specific genetic alterations are exploitable for assessing the effects of chemotherapeutic agents with different mechanism of action. Although still at an early stage, this fast-moving field shows promise as a novel and potentially useful method for development of target-specific therapeutic approaches.","authors":"Perego P, Jimenez GS, Gatti L, Howell SB, Zunino F","authors_abbrev":"Perego P et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-12-21","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23263988","title":"Quantitative analysis of chromosome condensation in fission yeast.","citation":"Mol Cell Biol 2013 Mar;33(5):984-98","abstract":"Chromosomes undergo extensive conformational rearrangements in preparation for their segregation during cell divisions. Insights into the molecular mechanisms behind this still poorly understood condensation process require the development of new approaches to quantitatively assess chromosome formation in vivo. In this study, we present a live-cell microscopy-based chromosome condensation assay in the fission yeast Schizosaccharomyces pombe. By automatically tracking the three-dimensional distance changes between fluorescently marked chromosome loci at high temporal and spatial resolution, we analyze chromosome condensation during mitosis and meiosis and deduct defined parameters to describe condensation dynamics. We demonstrate that this method can determine the contributions of condensin, topoisomerase II, and Aurora kinase to mitotic chromosome condensation. We furthermore show that the assay can identify proteins required for mitotic chromosome formation de novo by isolating mutants in condensin, DNA polymerase ε, and F-box DNA helicase I that are specifically defective in pro-/metaphase condensation. Thus, the chromosome condensation assay provides a direct and sensitive system for the discovery and characterization of components of the chromosome condensation machinery in a genetically tractable eukaryote.","doi":"10.1128/MCB.01400-12","authors":"Petrova B, Dehler S, Kruitwagen T, Hériché JK, Miura K, Haering CH","authors_abbrev":"Petrova B et al.","pubmed_publication_date":"Mar 2013","pubmed_entrez_date":"2012-12-25","publication_year":"2013","canto_session_key":"4e1a549f9ec3252a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-04-19 15:32:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-04 14:00:23","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPCC306.03c","SPBP4H10.06c","SPCC188.03","SPCC320.13c","SPBC1A4.03c","SPBC336.01","SPBC146.03c","SPBC776.13"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2014-04-04"},{"uniquename":"PMID:38674622","title":"Yeast Diversity in Honey and Pollen Samples from Stingless Bees in the State of Bahia, Brazil: Use of the MALDI-TOF MS/Genbank Proteomic Technique.","citation":"Microorganisms 2024 Mar 28;12(4)","abstract":"(1) Background: The identification of microorganisms includes traditional biochemical methods, molecular biology methods evaluating the conserved regions of rRNA, and the molecular biology of proteins (proteomics), such as MALDI-TOF MS mass spectrometry. This work aimed to identify the biodiversity of yeasts associated with stingless bee species' honey and pollen,  Melipona scutellaris ,  Nannotrigona testaceicornes , and  Tetragonisca angustula , from the region of São Gonçalo dos Campos-Bahia (BA) state, Brazil. (2) Methods: Cellular proteins were extracted from 2837 microbial isolates (pollen and honey) and identified via MALDI-TOF MS. The identified yeast species were also compared to the mass spectra of taxonomically well-characterized reference strains, available from the National Center of Biotechnology Information (NCBI) database. (3) Results: Nine yeast species were identified:  Candida maltosa ,  Candida norvegica ,  Kazachstania telluris ,  Schizosaccharomyces pombe ,  Scheffersomyces insectosus ,  Meyerozyma guilliermondii ,  Brettanomyces bruxellensis ,  Kazachstania exigua , and  Starmerella lactis-condensi. Nannotrigona testaceicornes  pollen had the highest number of yeast colonies. The yeasts  Brettanomyces bruxellensis  and  Kazachstania telluris  showed high populations in the samples of  Nannotrigona testaceicornes  and  Melipona scutellaris , respectively. This work shows that there is some sharing of the same species of yeast between honey and pollen from the same beehive. (4) Conclusions: A total of 71.84% of the identified species present a high level of confidence at the species level. Eight yeast species ( Candida maltosa ,  Candida norvegica ,  Kazachstania telluris ,  Schizosaccharomyces pombe ,  Scheffersomyces insectosus ,  Meyerozyma guilliermondii ,  Kazachstania exigua , and  Starmerella lactis-condensi ) were found for the first time in the samples that the authors inspected. This contributes to the construction of new knowledge about the diversity of yeasts associated with stingless bee products, as well as to the possibility of the biotechnological application of some yeast species.","doi":"10.3390/microorganisms12040678","authors":"da Silva RNA, Magalhães-Guedes KT, de Oliveira Alves RM, Souza AC, Schwan RF, Umsza-Guez MA","authors_abbrev":"da Silva RNA et al.","pubmed_publication_date":"28 Mar 2024","pubmed_entrez_date":"2024-04-27","publication_year":"2024","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2024-04-27 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26518661","title":"The Paf1 complex factors Leo1 and Paf1 promote local histone turnover to modulate chromatin states in fission yeast.","citation":"EMBO Rep 2015 Dec;16(12):1673-87","abstract":"The maintenance of open and repressed chromatin states is crucial for the regulation of gene expression. To study the genes involved in maintaining chromatin states, we generated a random mutant library in Schizosaccharomyces pombe and monitored the silencing of reporter genes inserted into the euchromatic region adjacent to the heterochromatic mating type locus. We show that Leo1-Paf1 [a subcomplex of the RNA polymerase II-associated factor 1 complex (Paf1C)] is required to prevent the spreading of heterochromatin into euchromatin by mapping the heterochromatin mark H3K9me2 using high-resolution genomewide ChIP (ChIP-exo). Loss of Leo1-Paf1 increases heterochromatin stability at several facultative heterochromatin loci in an RNAi-independent manner. Instead, deletion of Leo1 decreases nucleosome turnover, leading to heterochromatin stabilization. Our data reveal that Leo1-Paf1 promotes chromatin state fluctuations by enhancing histone turnover.","doi":"10.15252/embr.201541214","authors":"Sadeghi L, Prasad P, Ekwall K, Cohen A, Svensson JP","authors_abbrev":"Sadeghi L et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-11-01","publication_year":"2015","canto_session_key":"6e89c33ec1a6bb2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-07-31 11:00:06","canto_approved_date":"2025-09-03 17:55:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-25 13:38:38","canto_added_date":"2015-11-02 01:19:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":84,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.11c","SPAPB1A10.02","SPBC800.03","SPAC1F3.01","SPBC609.05","SPAC12G12.13c","SPAC27D7.14c","SPCC1322.12c","SPAC17H9.10c","SPBC24C6.09c","SPAC27D7.13c","SPBC32H8.11","SPCC736.11","SPAC139.06","SPAC29B12.03","SPAC13A11.03","SPAC664.01c","SPAC17G8.13c","SPAC1556.01c","SPBC17G9.02c","SPCC70.09c","SPAC19A8.10","SPAC23H3.14","SPBC13E7.08c","SPCC622.09","SPAC22F3.09c","SPAC664.03","SPCC622.16c","SPAC4H3.10c","SPAC22F8.12c","SPCC306.04c"],"gene_count":31,"ltp_gene_count":20,"approved_date":"2019-07-31"},{"uniquename":"GO_REF:0000022","title":"Improving the representation of immunology in the biological process Ontology","abstract":"GO terms describing processes, functions, and cellular components related to the immune system have existed in the GO from its beginning and been used extensively in the annotation of gene products. However, particularly in the biological process ontology, the initial set of terms relating to immunology failed to cover the breadth of known immunological processes, and in many cases diverged from current usage and understanding in their names, definitions, and ontological placement. As part of a larger effort to improve the representation of immunology in the GO, a GO Content Meeting was held November 15-16, 2005, at The Institute for Genomic Research, to discuss improvements to representation of immunology in the biological process ontology of the GO. As a result of the meeting, a number of high level terms for immunological processes were created, an overall structure for immunologically related terms was established, and certain existing terms were renamed or redefined as well to bring them in line with current usage.","authors":"Alison Deckhut Augustine (1), Alan Collmer (2), Judith A. Blake (3, 4), Candace W. Collmer (2, 3), Shane C. Burgess (5), Lindsay Grey Cowell (6), Jennifer I. Clark (3, 7), Bernard de Bono (7), Russell T. Collins (8), Alexander D. Diehl (3, 4), Michelle Gwinn Giglio (3, 9), Jamie A. Lee (10), Linda Hannick (3, 9), Jane Lomax (3, 7), Midori A. Harris (3, 7), Christopher J. Mungall (3, 11), David P. Hill (3, 4), Richard H. Scheuermann (10), Amelia Ireland (3, 7), Alessandro Sette (12) (1. NIAID, 2. Cornell University, 3. The GO Consortium, 4. Mouse Genome Informatics, 5. Mississippi State University, 6. Duke University, 7. EMBL-EBI, 8. University of Cambridge, 9. The Institute for Genomic Research, 10. U.T. Southwestern Medical Center, 11. HHMI, 12. La Jolla Institute for Allergy and Immunology)","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10756733","title":"[Inositol is necessary to sexual differentiation in Schizosaccharomyces pombe].","citation":"Rev Med Chir Soc Med Nat Iasi 1997;101(1-2):87-91","abstract":"Sexual differentiation in fission yeast Schizosaccharomyces pombe was found to be dependent on the glucose and inositol contents of culture media. Certain combinations in the amounts of these two compounds suppressed mating and sporulation, while maintaining normal viability. Inositol was found to be required for mating and sporulation in both nitrogen-rich and nitrogen-poor media (the lack of nitrogen is most well-known factor that induces the sexual differentiation). The experiments were performed using the wild-type strains and standard media. Mutants carrying the pat1-114 temperature-sensitive allele circumvented the need for inositol at the restrictive temperature.","authors":"Poiţelea M, Rusu M","authors_abbrev":"Poiţelea M et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11054821","title":"Analysis of 114 kb of DNA sequence from fission yeast chromosome 2 immediately centromere-distal to his5.","citation":"Yeast 2000 Nov;16(15):1405-11","abstract":"One hundred and fourteen kilobase pairs (kb) of contiguous genomic sequence have been determined immediately distal to the his5 genetic marker located about 0.9 Mb from the centromere on the long arm of Schizosaccharomyces pombe chromosome 2. The sequence is contained in overlapping cosmid clones c16H5, c12D12, c24C6 and c19G7, of which 20 kb are identical to previously reported sequence from clone c21H7. The remaining 93 781 bp of sequence contains 10 known genes (cdc14, cdm1, cps1, gpa1, msh2, pck2, rip1, rps30-2, sad1 and ubl1), 32 open reading frames (ORFs) capable of coding for proteins of at least 100 amino acid residues in length, one 5S rRNA gene, one tRNA(Pro) gene, one lone Tf1-type long terminal repeat (LTR) and one lone Tf2-type LTR. There is a density of one protein-coding gene per 2.2 kb and 22 of the 42 ORFs (52%) incorporate one or more introns. Twenty-one of the novel ORFs show sequence similarities which suggest functions of their products, including a cyclin C, a MADS box transcription factor, mad2-like protein, telomere binding protein, topoisomerase II-associated protein, ATP-dependent DEAH box RNA helicase, G10 protein, ubiquitin-activating e1-like enzyme, nucleoporin, prolyl-tRNA synthetase, peptidylprolyl isomerase, delta-1-pyrroline-5-carboxylate dehydrogenase, protein transport protein, coatomer epsilon, TCP-1 chaperonin, beta-subunit of 6-phosphofructokinase, aminodeoxychorismate lyase, a phosphate transport protein and a thioredoxin.","authors":"Xiang Z, Moore K, Wood V, Rajandream MA, Barrell BG, Skelton J, Churcher CM, Lyne MH, Devlin K, Gwilliam R, Rutherford KM, Aves SJ","authors_abbrev":"Xiang Z et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-10-31","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32636306","title":"Aurora A regulation by reversible cysteine oxidation reveals evolutionarily conserved redox control of Ser/Thr protein kinase activity.","citation":"Sci Signal 2020 Jul 07;13(639)","abstract":"Reactive oxygen species (ROS) are physiological mediators of cellular signaling and play potentially damaging roles in human diseases. In this study, we found that the catalytic activity of the Ser/Thr kinase Aurora A was inhibited by the oxidation of a conserved cysteine residue (Cys 290 ) that lies adjacent to Thr 288 , a critical phosphorylation site in the activation segment. Cys is present at the equivalent position in ~100 human Ser/Thr kinases, a residue that we found was important not only for the activity of human Aurora A but also for that of fission yeast MAPK-activated kinase (Srk1) and PKA (Pka1). Moreover, the presence of this conserved Cys predicted biochemical redox sensitivity among a cohort of human CAMK, AGC, and AGC-like kinases. Thus, we predict that redox modulation of the conserved Cys 290  of Aurora A may be an underappreciated regulatory mechanism that is widespread in eukaryotic Ser/Thr kinases. Given the key biological roles of these enzymes, these findings have implications for understanding physiological and pathological responses to ROS and highlight the importance of protein kinase regulation through multivalent modification of the activation segment.","doi":"10.1126/scisignal.aax2713","authors":"Byrne DP, Shrestha S, Galler M, Cao M, Daly LA, Campbell AE, Eyers CE, Veal EA, Kannan N, Eyers PA","authors_abbrev":"Byrne DP et al.","pubmed_publication_date":"07 Jul 2020","pubmed_entrez_date":"2020-07-09","publication_year":"2020","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-07-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29689193","title":"Mechanosensation Dynamically Coordinates Polar Growth and Cell Wall Assembly to Promote Cell Survival.","citation":"Dev Cell 2018 Apr 23;45(2):170-182.e7","abstract":"How growing cells cope with size expansion while ensuring mechanical integrity is not known. In walled cells, such as those of microbes and plants, growth and viability are both supported by a thin and rigid encasing cell wall (CW). We deciphered the dynamic mechanisms controlling wall surface assembly during cell growth, using a sub-resolution microscopy approach to monitor CW thickness in live rod-shaped fission yeast cells. We found that polar cell growth yielded wall thinning and that thickness negatively influenced growth. Thickness at growing tips exhibited a fluctuating behavior with thickening phases followed by thinning phases, indicative of a delayed feedback promoting thickness homeostasis. This feedback was mediated by mechanosensing through the CW integrity pathway, which probes strain in the wall to adjust synthase localization and activity to surface growth. Mutants defective in thickness homeostasis lysed by rupturing the wall, demonstrating its pivotal role for walled cell survival.","doi":"10.1016/j.devcel.2018.03.022","authors":"Davì V, Tanimoto H, Ershov D, Haupt A, De Belly H, Le Borgne R, Couturier E, Boudaoud A, Minc N","authors_abbrev":"Davì V et al.","pubmed_publication_date":"23 Apr 2018","pubmed_entrez_date":"2018-04-25","publication_year":"2018","canto_session_key":"e677bdbfedf4a422","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nicolas Minc","canto_first_approved_date":"2018-11-08 15:53:01","canto_approved_date":"2020-01-17 12:15:35","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-11-06 10:42:48","canto_added_date":"2018-04-26 00:15:04","annotation_curators":[{"name":"Nicolas Minc","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.08","SPBC12D12.04c","SPCC645.07","SPBC30B4.01c","SPCC1840.02c","SPAC821.12","SPAC1F7.04","SPCC1223.06"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2018-11-08"},{"uniquename":"GO_REF:0000041","title":"Gene Ontology annotation based on UniPathway vocabulary mapping. ","abstract":"Transitive assignment of GO terms based on the UniPathway pathway vocabulary. UniPathway is a manually curated resource of enzyme-catalyzed and spontaneous chemical reactions. It provides a hierarchical representation of metabolic pathways. Descriptions of the pathway(s) that a particular protein is involved in are included in UniProtKB records.<br>UniPathway data are cross-linked to existing pathway resources such as KEGG and MetaCyc. Further information on the UniPathway resource is available at http://www.unipathway.org/obiwarehouse/unipathway.<br>When a UniPathway pathway describes a concept that is within the scope of the Gene Ontology, it is investigated to determine whether it is appropriate to map the term to an equivalent term in GO. The mapping between UniPathway terms and GO terms is carried out manually. Definitions and hierarchies of the terms in the two resources are compared and the mapping generated will reflect the most correct correspondence. The translation table between GO terms and UniPathway pathways is maintained by the UniPathway team and is available at http://www.grenoble.prabi.fr/dev/obiwarehouse/download/unipathway/public/unipathway2go.tsv.","authors":"UniProt-GOA","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC106.04","SPAC24C9.12c","SPBP8B7.18c","SPCC1223.02","SPCC18B5.05c","SPAC1002.17c","SPCC1223.03c","SPCC965.14c","SPBP8B7.17c","SPAC1B3.01c","SPBC16G5.02c","SPCC162.11c","SPAC22G7.06c","SPAC227.14","SPBC725.15","SPBC1711.04","SPAC23H4.10c","SPAC1399.04c","SPBP8B7.29","SPAC10F6.03c","SPAC18G6.04c","SPBC460.04c","SPBC19G7.02","SPBC21C3.08c","SPCC338.14","SPAC9E9.11","SPAC16.03c","SPAC15E1.04"],"gene_count":28,"ltp_gene_count":0},{"uniquename":"PMID:16262699","title":"Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans.","citation":"FEBS J 2005 Nov;272(21):5606-22","abstract":"The isoprenoid chain of ubiquinone (Q) is determined by trans-polyprenyl diphosphate synthase in micro-organisms and presumably in mammals. Because mice and humans produce Q9 and Q10, they are expected to possess solanesyl and decaprenyl diphosphate synthases as the determining enzyme for a type of ubiquinone. Here we show that murine and human solanesyl and decaprenyl diphosphate synthases are heterotetramers composed of newly characterized hDPS1 (mSPS1) and hDLP1 (mDLP1), which have been identified as orthologs of Schizosaccharomyces pombe Dps1 and Dlp1, respectively. Whereas hDPS1 or mSPS1 can complement the S. pombe dps1 disruptant, neither hDLP1 nor mDLP1 could complement the S. pombe dLp1 disruptant. Thus, only hDPS1 and mSPS1 are functional orthologs of SpDps1. Escherichia coli was engineered to express murine and human SpDps1 and/or SpDlp1 homologs and their ubiquinone types were determined. Whereas transformants expressing a single component produced only Q8 of E. coli origin, double transformants expressing mSPS1 and mDLP1 or hDPS1 and hDLP1 produced Q9 or Q10, respectively, and an in vitro activity of solanesyl or decaprenyl diphosphate synthase was verified. The complex size of the human and murine long-chain trans-prenyl diphosphate synthases, as estimated by gel-filtration chromatography, indicates that they consist of heterotetramers. Expression in E. coli of heterologous combinations, namely, mSPS1 and hDLP1 or hDPS1 and mDLP1, generated both Q9 and Q10, indicating both components are involved in determining the ubiquinone side chain. Thus, we identified the components of the enzymes that determine the side chain of ubiquinone in mammals and they resembles the S. pombe, but not plant or Saccharomyces cerevisiae, type of enzyme.","authors":"Saiki R, Nagata A, Kainou T, Matsuda H, Kawamukai M","authors_abbrev":"Saiki R et al.","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-11-03","publication_year":"2005","canto_session_key":"ef9f171b6b2903ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-21 16:47:20","canto_approved_date":"2025-01-20 22:52:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-21 16:47:13","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.01","SPAC19G12.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-10-21"},{"uniquename":"PMID:24607700","title":"Revisiting the neuropathogenesis of Zellweger syndrome.","citation":"Neurochem Int 2014 Apr;69:1-8","abstract":"Zellweger syndrome (ZS) is a neonatal-lethal genetic disease that affects all tissues, and features neuropathology that involves primary developmental defects as well as neurodegeneration. Neuropathological changes include abnormal neuronal migration affecting the cerebral hemispheres, cerebellum and inferior olivary complex, abnormal Purkinje cell arborisation, demyelination and post-developmental neuronal degeneration. ZS is caused by mutations in peroxisome biogenesis, or PEX, genes which lead to defective peroxisome biogenesis and the resultant loss of peroxisomal metabolic function. The molecular and cellular bases of ZS neuropathology are still not completely understood. Attempts to explain the neuropathogenesis have implicated peroxisomal metabolic dysfunction, and more specifically the loss of peroxisomal products, such as plasmalogens and docosahexaenoic, and the accumulation of peroxisomal substrates, such as very-long-chain-fatty acids. In this review, consideration is also given to recent findings that implicate other candidate pathogenetic factors, such as mitochondrial dysfunction, oxidative stress, protein misfolding, aberrant cell signalling, and inflammation - factors that have also been identified as important in the pathogenesis of other neurological diseases.","doi":"10.1016/j.neuint.2014.02.007","authors":"Crane DI","authors_abbrev":"Crane DI","pubmed_publication_date":"Apr 2014","pubmed_entrez_date":"2014-03-11","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC553.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:36257942","title":"Proteome effects of genome-wide single gene perturbations.","citation":"Nat Commun 2022 Oct 18;13(1):6153","abstract":"Protein abundance is controlled at the transcriptional, translational and post-translational levels, and its regulatory principles are starting to emerge. Investigating these principles requires large-scale proteomics data and cannot just be done with transcriptional outcomes that are commonly used as a proxy for protein abundance. Here, we determine proteome changes resulting from the individual knockout of 3308 nonessential genes in the yeast Schizosaccharomyces pombe. We use similarity clustering of global proteome changes to infer gene functionality that can be extended to other species, such as humans or baker's yeast. Furthermore, we analyze a selected set of deletion mutants by paired transcriptome and proteome measurements and show that upregulation of proteins under stable transcript expression utilizes optimal codons.","doi":"10.1038/s41467-022-33814-8","authors":"Öztürk M, Freiwald A, Cartano J, Schmitt R, Dejung M, Luck K, Al-Sady B, Braun S, Levin M, Butter F","authors_abbrev":"Öztürk M et al.","pubmed_publication_date":"18 Oct 2022","pubmed_entrez_date":"2022-10-18","publication_year":"2022","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2022-10-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36408920","title":"UniProt: the Universal Protein Knowledgebase in 2023.","citation":"Nucleic Acids Res 2023 Jan 06;51(D1):D523-D531","abstract":"The aim of the UniProt Knowledgebase is to provide users with a comprehensive, high-quality and freely accessible set of protein sequences annotated with functional information. In this publication we describe enhancements made to our data processing pipeline and to our website to adapt to an ever-increasing information content. The number of sequences in UniProtKB has risen to over 227 million and we are working towards including a reference proteome for each taxonomic group. We continue to extract detailed annotations from the literature to update or create reviewed entries, while unreviewed entries are supplemented with annotations provided by automated systems using a variety of machine-learning techniques. In addition, the scientific community continues their contributions of publications and annotations to UniProt entries of their interest. Finally, we describe our new website (https://www.uniprot.org/), designed to enhance our users' experience and make our data easily accessible to the research community. This interface includes access to AlphaFold structures for more than 85% of all entries as well as improved visualisations for subcellular localisation of proteins.","doi":"10.1093/nar/gkac1052","authors":"UniProt Consortium","authors_abbrev":"UniProt Consortium","pubmed_publication_date":"06 Jan 2023","pubmed_entrez_date":"2022-11-21","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.10c","SPAC212.08c","SPBC16A3.14","SPAC4A8.08c","SPCC1322.10","SPBC354.15","SPBC947.10","SPAC19G12.16c","SPAC2E1P3.05c","SPBC725.01","SPBC543.07","SPBC947.05c","SPAC1296.02","SPAC4F8.05c","SPCC970.01","SPAC3C7.11c","SPBC543.08","SPBC25H2.18","SPAC13G6.03","SPBC1348.10c","SPAPB15E9.01c","SPAC11G7.03","SPAC13G6.06c","SPBC4F6.18c","SPCC622.09","SPBC21C3.18","SPAC2G11.13","SPBC776.07","SPAC26H5.12","SPCC306.08c","SPAC1039.07c","SPBC31A8.01c","SPBC56F2.12","SPAC15A10.01","SPAC14C4.09","SPAC3G9.13c","SPBC1289.09","SPBC16G5.09","SPAC821.10c","SPAC139.04c","SPAC8C9.06c","SPBC2G2.12","SPAC1B3.10c","SPAC12B10.11","SPCC1919.12c","SPCC757.05c","SPBC13G1.05","SPBC1347.13c","SPBC2D10.08c","SPCC1322.03","SPBP23A10.11c","SPAC23H4.04","SPAC26F1.04c","SPCC18.01c","SPBC16G5.06","SPAPB1E7.04c","SPBC211.01","SPAC27E2.11c","SPAC19G12.11","SPBC1E8.05","SPBC1105.08","SPBPB2B2.06c","SPBC24C6.13","SPAC16A10.04","SPBC4B4.11","SPBC16A3.03c","SPBC16E9.07","SPBC337.15c","SPBC1289.16c","SPCC1235.14","SPAC30.04c","SPCC330.12c","SPAC19E9.01c","SPCC1672.09","SPBC713.07c","SPAC23H4.05c","SPBC9B6.04c","SPAC13G7.04c","SPAP27G11.02","SPAC977.07c","SPBC713.14c","SPBC2G5.01","SPCC1020.05","SPBC1734.13","SPCC794.07","SPCC622.08c","SPCC16A11.06c","SPAC6B12.06c","SPCC16C4.13c","SPBC1289.15","SPCC24B10.17","SPAC11D3.10","SPAC23H4.03c","SPAC144.04c","SPCC306.11","SPAC1F8.01","SPAC23A1.14c","SPAC16.03c","SPAC13G6.02c","SPBP4H10.10","SPBC16E9.09c","SPCC1259.02c","SPBC1677.03c","SPBC4F6.05c","SPCC11E10.01","SPAC21E11.08","SPBC3B9.19","SPAC24C9.06c","SPBC947.15c","SPBC2G2.04c","SPBC21C3.04c","SPCC737.09c","SPBC16A3.16","SPAC3H8.05c","SPAC23G3.02c","SPAC17G8.13c","SPBC21D10.07","SPBC215.14c","SPAC1399.06","SPAC3H1.04c","SPCC777.17c","SPBP4H10.15","SPAC23D3.17","SPCC24B10.05","SPBC1683.09c","SPAC3A12.19","SPBC1703.02","SPCC1259.09c","SPAC27E2.09","SPBP23A10.17","SPAC1B3.11c","SPAC1F5.06","SPAC1039.06","SPAC6B12.04c","SPAC19G12.10c","SPAC12G12.04","SPCC1259.10","SPAC167.09","SPBC887.13c","SPBC16H5.06","SPAC3A11.10c","SPAC186.03","SPBC3F6.03","SPAC22A12.15c","SPBC17A3.07","SPBC713.03","SPAC2F3.09","SPBC18E5.13","SPAC4G8.12c","SPAC144.10c","SPBC1921.06c","SPAC644.17c","SPBC25B2.02c","SPAC3A12.17c","SPBC1718.06","SPAC4G9.17c","SPAC22H12.04c","SPAC27F1.10","SPAC23D3.14c","SPCC1442.15c","SPAC25B8.18","SPBC15D4.04","SPAC24B11.11c","SPAC6C3.04","SPBC11B10.01","SPBC2F12.10","SPBC16A3.13","SPAC1782.12c","SPAC3F10.11c","SPAC23H3.09c","SPBC337.07c","SPBC342.03","SPAC11D3.09","SPAC7D4.07c","SPAC1F12.07","SPAC17A5.08","SPCC4B3.09c","SPCC663.14c","SPCC4G3.06c","SPAC17A2.11","SPAPB1A10.12c","SPBC1539.04","SPAC56F8.06c","SPAC27F1.05c","SPCC61.05","SPAPB1A10.10c","SPBC776.05","SPCC569.02c","SPAC20G8.02","SPBC36.04","SPBC1198.06c","SPAP8A3.03","SPAC23A1.04c","SPAC56E4.06c","SPAC1486.06","SPBC11B10.04c","SPBC146.10","SPBC3E7.05c","SPBC26H8.01","SPAC630.12","SPAC23C4.08","SPCC1322.01","SPBC106.02c","SPAC16.01","SPBC27B12.06","SPCC1235.13","SPBC902.03","SPBP19A11.02c","SPCC736.06","SPAC17G8.06c","SPAPB1E7.09","SPCC18B5.01c","SPCC4G3.04c","SPAC19G12.06c","SPAC18B11.05","SPAC664.09","SPCC16C4.11","SPBC3H7.03c","SPAP11E10.02c","SPAC25H1.09","SPBC405.04c","SPBC428.16c","SPAC1F8.06","SPAPB8E5.04c","SPAP7G5.06","SPBC1773.03c","SPAC922.03","SPBC1289.06c","SPAC22F8.02c","SPAC1834.05","SPCP31B10.02","SPCC1795.06","SPBP23A10.03c","SPCC645.09","SPAC821.09","SPACUNK4.08","SPBC839.11c","SPBC776.12c","SPBC14C8.15","SPBP4H10.05c","SPCC417.11c","SPCP20C8.02c","SPBC3B8.01c","SPBC2G2.17c","SPAC57A7.09","SPCC338.15","SPAC26H5.08c","SPBP26C9.03c","SPAC1486.08","SPAPB1A10.11c","SPBC29A3.15c","SPBC16C6.08c","SPCC4G3.08","SPAC664.11","SPBC14C8.05c","SPAC29B12.10c","SPCC736.03c","SPAC977.05c","SPBC26H8.16","SPBPB2B2.15","SPCC306.06c","SPAC186.01","SPBC25H2.08c","SPAC16E8.10c","SPBC21B10.06c","SPAC22F3.06c","SPAC4A8.11c","SPAC1786.02","SPBC4B4.08","SPBC9B6.06","SPBC30B4.01c","SPAC27E2.06c","SPBC4F6.17c","SPBC8D2.17","SPBC16E9.18","SPBC2G5.06c","SPAC1039.02","SPCC74.06","SPBC902.05c","SPBC21C3.03","SPBC685.03","SPAP14E8.04","SPAC1F7.05","SPBC15C4.04c","SPAC1006.05c","SPBC1711.09c","SPAP7G5.03","SPBC1539.08","SPBC839.15c","SPCC1840.12","SPCC1183.04c","SPBC19G7.07c","SPAC1486.07c","SPAC750.07c","SPBC428.11","SPBC11B10.07c","SPAC13C5.06c","SPBC119.18","SPBC26H8.05c","SPAC27D7.06","SPAC17A2.10c","SPCC4B3.03c","SPAC12B10.05","SPAC23A1.18c","SPBC16A3.12c","SPCC1840.08c","SPCC1919.02","SPAC17H9.14c","SPAC8C9.14","SPBC1105.03c","SPBC106.17c","SPCC18.08","SPCC4F11.04c","SPAC25H1.07","SPBC839.06","SPAC959.05c","SPAC24C9.10c","SPAC1783.07c","SPAC1002.09c","SPAC1486.11","SPAC22H12.05c","SPAC922.04","SPAPB2C8.01","SPBC1711.12","SPAC56F8.02","SPAC1952.11c","SPAC21E11.07","SPAC19D5.07","SPBC13E7.04","SPBC13G1.11","SPAC343.02","SPAC31G5.14","SPBC20F10.07","SPAC4G9.09c","SPAC824.08","SPBC18E5.10","SPCC548.06c","SPAC19D5.02c","SPBC14C8.10","SPAC10F6.13c",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regulation of heterochromatin inheritance by Dpb3-Dpb4 complex.","citation":"Proc Natl Acad Sci U S A 2017 Nov 21;114(47):12524-12529","abstract":"During DNA replication, chromatin is disrupted ahead of the replication fork, and epigenetic information must be restored behind the fork. How epigenetic marks are inherited through DNA replication remains poorly understood. Histone H3 lysine 9 (H3K9) methylation and histone hypoacetylation are conserved hallmarks of heterochromatin. We previously showed that the inheritance of H3K9 methylation during DNA replication depends on the catalytic subunit of DNA polymerase epsilon, Cdc20. Here we show that the histone-fold subunit of Pol epsilon, Dpb4, interacts an uncharacterized small histone-fold protein, SPCC16C4.22, to form a heterodimer in fission yeast. We demonstrate that SPCC16C4.22 is nonessential for viability and corresponds to the true ortholog of Dpb3. We further show that the Dpb3-Dpb4 dimer associates with histone deacetylases, chromatin remodelers, and histones and plays a crucial role in the inheritance of histone hypoacetylation in heterochromatin. We solve the 1.9-Å crystal structure of Dpb3-Dpb4 and reveal that they form the H2A-H2B-like dimer. Disruption of Dpb3-Dpb4 dimerization results in loss of heterochromatin silencing. Our findings reveal a link between histone deacetylation and H3K9 methylation and suggest a mechanism for how two processes are coordinated during replication. We propose that the Dpb3-Dpb4 heterodimer together with Cdc20 serves as a platform for the recruitment of chromatin modifiers and remodelers that mediate heterochromatin assembly during DNA replication, and ensure the faithful inheritance of epigenetic marks in heterochromatin.","doi":"10.1073/pnas.1712961114","authors":"He H, Li Y, Dong Q, Chang AY, Gao F, Chi Z, Su M, Zhang F, Ban H, Martienssen R, Chen YH, Li F","authors_abbrev":"He H et al.","pubmed_publication_date":"21 Nov 2017","pubmed_entrez_date":"2017-11-08","publication_year":"2017","canto_session_key":"5c114aae15de6314","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Fei Li","canto_first_approved_date":"2017-12-04 14:23:37","canto_approved_date":"2025-10-16 08:11:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-21 21:06:28","canto_added_date":"2017-11-09 01:15:46","annotation_curators":[{"name":"Fei Li","community_curator":true,"annotation_count":27,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.05","SPCC16C4.22","SPBC16D10.07c","SPBC25H2.13c","SPBC3D6.09","SPBC36.05c","SPAC664.01c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2017-12-04","pdb_entries":[{"pdb_id":"5y27","gene_chains":[{"gene_uniquename":"SPCC16C4.22","chain":"B","position":"1-87"},{"gene_uniquename":"SPBC3D6.09","chain":"A","position":"2-210"}],"title":"Crystal structure of Se-Met Dpb4-Dpb3","entry_authors":"Li Y,Gao F,Su M,Zhang FB,Chen YH","entry_authors_abbrev":"Li Y et al.","reference_uniquename":"PMID:29109278","experimental_method":"X-ray","resolution":"1.9"},{"pdb_id":"5y26","gene_chains":[{"gene_uniquename":"SPCC16C4.22","chain":"B","position":"1-87"},{"gene_uniquename":"SPBC3D6.09","chain":"A","position":"2-210"}],"title":"Crystal structure of native Dpb4-Dpb3","entry_authors":"Chen YH,Li Y,Gao F","entry_authors_abbrev":"Chen YH et al.","reference_uniquename":"PMID:29109278","experimental_method":"X-ray","resolution":"2.003"}]},{"uniquename":"PMID:29844133","title":"Loss of Elongation-Like Factor 1 Spontaneously Induces Diverse, RNase H-Related Suppressor Mutations in  Schizosaccharomyces pombe .","citation":"Genetics 2018 Aug;209(4):967-981","abstract":"A healthy individual may carry a detrimental genetic trait that is masked by another genetic mutation. Such suppressive genetic interactions, in which a mutant allele either partially or completely restores the fitness defect of a particular mutant, tend to occur between genes that have a confined functional connection. Here we investigate a self-recovery phenotype in  Schizosaccharomyces pombe , mediated by suppressive genetic interactions that can be amplified during cell culture. Cells without Elf1, an AAA+ family ATPase, have severe growth defects initially, but quickly recover growth rates near to those of wild-type strains by acquiring suppressor mutations.  elf1Δ  cells accumulate RNAs within the nucleus and display effects of genome instability such as sensitivity to DNA damage, increased incidence of lagging chromosomes, and mini-chromosome loss. Notably, the rate of phenotypic recovery was further enhanced in  elf1Δ  cells when RNase H activities were abolished and significantly reduced upon overexpression of RNase H1, suggesting that loss of Elf1-related genome instability can be resolved by RNase H activities, likely through eliminating the potentially mutagenic DNA-RNA hybrids caused by RNA nuclear accumulation. Using whole genome sequencing, we mapped a few consistent suppressors of  elf1Δ  including mutated Cue2, Rpl2702, and SPBPJ4664.02, suggesting previously unknown functional connections between Elf1 and these proteins. Our findings describe a mechanism by which cells bearing mutations that cause fitness defects and genome instability may accelerate the fitness recovery of their population through quickly acquiring suppressors. We propose that this mechanism may be universally applicable to all microorganisms in large-population cultures.","doi":"10.1534/genetics.118.301055","authors":"Marayati BF, Drayton AL, Tucker JF, Huckabee RH, Anderson AM, Pease JB, Zeyl CW, Zhang K","authors_abbrev":"Marayati BF et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-05-31","publication_year":"2018","canto_session_key":"b2192f51379c99f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ke Zhang","canto_first_approved_date":"2018-07-18 11:33:38","canto_approved_date":"2022-09-02 17:01:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-05 18:34:57","canto_added_date":"2018-06-01 00:15:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"B Fadi Marayati","community_curator":true,"annotation_count":20,"orcid":null,"file_type":null,"file_name":null},{"name":"Ke Zhang","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.06c","SPBC36.05c","SPCC1235.03","SPAC3C7.08c","SPAC4G9.02","SPBC1D7.04","SPAC1F3.01","SPCC74.05"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-07-18"},{"uniquename":"PMID:12741836","title":"Iron-sulfur cluster biosynthesis. A comparative kinetic analysis of native and Cys-substituted ISA-mediated [2Fe-2S]2+ cluster transfer to an apoferredoxin target.","citation":"Biochemistry 2003 May 20;42(19):5784-91","abstract":"ISA type proteins mediate cluster transfer to apoprotein targets. Rate constants have been determined for cluster transfer from Schizosaccharomyces pombe ISA to apo Fd. Substitution of the cysteine residues of ISA produced derivative proteins (C72A, C136A, and C138A) that were found to be at least as active in cluster transfer reactions as the native form at 25 degrees C (k(2) approximately 170 M(-1) min(-1) for native, k(2) approximately 169 M(-1) min(-1) for C72A, k(2) approximately 206 M(-1) min(-1) for C136A, and k(2) approximately 242 M(-1) min(-1) for C138A), although the yield of cluster transfer was found to be lower as a consequence of the enhanced lability of clusters in the derivative proteins. Minor variations in rate constant for the ISA Cys derivatives do not reflect any change in the affinity of binding to the apo Fd since k(2) was found to be independent of the concentration of apo Fd over the range of 1-25 microM. The pH dependence of cluster transfer rates was found to be similar for native and C136A ISA, with an observed pK(a) of 7.8 determined from the pH profiles for cluster transfer activity of each protein. The temperature dependence of the rate constant defining the cluster transfer reaction for the wild type versus this C136A ISA derivative is distinct (DeltaH* approximately 6.3 kcal mol(-1) and DeltaS* approximately -27.3 cal K(-1) mol(-1) for native and DeltaH* approximately 2.7 kcal mol(-1) and DeltaS* approximately -38.9 cal K(-1) mol(-1) for C136A ISA). Instability of the protein-bound cluster precluded a comparison with data from pH and temperature dependencies for the two other Cys derivatives. Experiments to determine the dependence of reaction rate constants on viscosity indicate cluster transfer is rate-limiting. A comparison of cross-species rate constants for cluster transfer to apo Fd targets from Homo sapiens and S. pombe demonstrated that the identity of the Fd is less critical for promoting cluster transfer from Sp ISA (at 25 degrees C, k(2) approximately 170 M(-1) min(-1) for Sp Fd and k(2) approximately 169 M(-1) min(-1) for Hs Fd). This contrasts with an earlier observation for ISU-mediated cluster assembly [Wu, S., et al. (2002) Biochemistry 41, 8876-8885], where the rates differed for Hs and Sp target Fd's, suggesting distinct binding sites for binding of holo ISA and ISU to apo Fd.","authors":"Wu SP, Cowan JA","authors_abbrev":"Wu SP et al.","pubmed_publication_date":"20 May 2003","pubmed_entrez_date":"2003-05-14","publication_year":"2003","canto_session_key":"07db7eb42e9a3d64","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-09 14:21:48","canto_approved_date":"2023-06-20 13:18:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-19 14:55:33","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.03c","SPAC22E12.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-04-09"},{"uniquename":"PMID:16028519","title":"[Characterization of Schizosaccharomyces hominis].","citation":"Zh Mikrobiol Epidemiol Immunobiol 2005;(3):74-5","abstract":"The cultural, morphological, physiological and biological characteristics of Schizosaccharomyces hominis, Benedek strain BKM Y-650 were under study. This name is regarded as synonymous to Schizosaccharomyces pombe Lindner.","authors":"Golubev VI, Golubeva EV","authors_abbrev":"Golubev VI et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-07-21","publication_year":"2005","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26507459","title":"Mitochondrial superoxide dismutase deficiency accelerates chronological aging in the fission yeast Schizosaccharomyces pombe.","citation":"Cell Biol Int 2016 Jan;40(1):100-6","abstract":"A mitochondrial superoxide dismutase (SOD2) is the first line of antioxidant defense against mitochondrial superoxide. Even though the involvement of SOD2 in lifespan has been studied extensively in several organisms, characterization of the aging process has not been performed for the sod2 mutant (sod2Δ) of a prominent model Schizosaccharomyces pombe. In this study, we measured the chronological lifespan of sod2Δ cells by their ability to survive in long-term culture. SOD2 deficiency drastically decreased cell viability in the stationary phase. The mutation frequency of nuclear DNA in sod2Δ was elevated in the stationary phase, and cellular proteins and nuclear DNA were extensively degraded, concurrent with cell death. The sod2 gene in wild-type cells could be induced by an increase in endogenous oxidative stresses, after which, SOD2 activity was substantially elevated during the stationary phase. Culture in a lower glucose concentration (calorie restriction) prominently extended the sod2Δ lifespan. Therefore, S. pombe SOD2 plays a critical role in longevity through its upregulation in the non-dividing phase.","doi":"10.1002/cbin.10556","authors":"Ogata T, Senoo T, Kawano S, Ikeda S","authors_abbrev":"Ogata T et al.","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2015-10-29","publication_year":"2016","canto_session_key":"231811fcb0eb9556","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-26 16:54:07","canto_approved_date":"2020-03-15 15:11:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-26 16:33:07","canto_added_date":"2015-10-30 01:19:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1486.01","SPAC821.10c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2016-10-26"},{"uniquename":"PMID:31223645","title":"Reciprocal regulation of TORC signaling and tRNA modifications by Elongator enforces nutrient-dependent cell fate.","citation":"Sci Adv 2019 Jun;5(6):eaav0184","abstract":"Nutrient availability has a profound impact on cell fate. Upon nitrogen starvation, wild-type fission yeast cells uncouple cell growth from cell division to generate small, round-shaped cells that are competent for sexual differentiation. The TORC1 (TOR complex 1) and TORC2 complexes exert opposite controls on cell growth and cell differentiation, but little is known about how their activity is coordinated. We show that transfer RNA (tRNA) modifications by Elongator are critical for this regulation by promoting the translation of both key components of TORC2 and repressors of TORC1. We further identified the TORC2 pathway as an activator of Elongator by down-regulating a Gsk3 (glycogen synthase kinase 3)-dependent inhibitory phosphorylation of Elongator. Therefore, a feedback control is operating between TOR complex (TORC) signaling and tRNA modification by Elongator to enforce the advancement of mitosis that precedes cell differentiation.","doi":"10.1126/sciadv.aav0184","authors":"Candiracci J, Migeot V, Chionh YH, Bauer F, Brochier T, Russell B, Shiozaki K, Dedon P, Hermand D","authors_abbrev":"Candiracci J et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-06-22","publication_year":"2019","canto_session_key":"28d42787d68c1d02","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-06-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPAB4296","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8187760","title":"Genetic analysis of cell morphogenesis in fission yeast--a role for casein kinase II in the establishment of polarized growth.","citation":"EMBO J 1994 May 01;13(9):2066-74","abstract":"We have initiated a study to identify genes regulating cell morphogenesis in the fission yeast Schizosaccharomyces pombe. Five genes have been identified, orb1-orb5, whose mutation gives rise to spherical cells, indicative of an inability to polarize growth. Two further genes have been identified, tea1 and ban1, whose mutant alleles have disturbed patterns of tip growth, leading to T-shaped and curved cells. In fission yeast, sites of cell wall deposition are defined by actin localization, with actin distributions and therefore growth patterns undergoing cell cycle stage-specific reorganization. Studies of double mutants constructed between orb5-19 and various cdc mutants blocked before and after cell division show that orb5 is required for the re-establishment of polar growth following cytokinesis. This indicates that the mutant allele orb5-19 is defective in the reinitiation of polarized growth, even though actin reorganization to the cell tips occurs normally. orb5 encodes a fission yeast homologue of casein kinase II alpha. We propose that this kinase plays a role in the translation of cell polarity into polarized growth, but not in the establishment of polarity itself.","authors":"Snell V, Nurse P","authors_abbrev":"Snell V et al.","pubmed_publication_date":"01 May 1994","pubmed_entrez_date":"1994-05-01","publication_year":"1994","canto_session_key":"191643d2928456ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-09-28 04:06:47","canto_approved_date":"2026-01-31 11:42:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-04 16:55:27","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPCC16C4.09","SPCC1739.11c","SPCC1223.06","SPBC17F3.02","SPAC16E8.09","SPBC1604.14c","SPAC23C11.11","SPBC11B10.09","SPAC24H6.05"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2016-09-28"},{"uniquename":"PMID:16325576","title":"The kinetochore protein Moa1 enables cohesion-mediated monopolar attachment at meiosis I.","citation":"Cell 2005 Dec 02;123(5):803-17","abstract":"Meiosis resembles mitosis but employs a unique \"reductional\" nuclear division to allow the production of haploid gametes from diploid cells. The crucial ploidy reduction step requires that sister kinetochores attach to microtubules emanating from the same spindle pole, achieving \"monopolar attachment,\" which ensures that maternal and paternal chromosomes are segregated. Here we screened for factors required to establish monopolar attachment in fission yeast and identified a novel protein, Moa1. Moa1 is meiosis specific and localizes exclusively to the central core of the centromere, a region that binds meiotic Rec8-containing cohesin complexes but not mitotic Rad21/Scc1-containing complexes. Enforced cleavage of Rec8 in the central core region led to the disruption of monopolar attachment, as in moa1Delta cells, without diminishing Moa1 localization. Moa1 physically interacts with Rec8, implying that Moa1 functions only through Rec8, presumably to facilitate central core cohesion. These results prove that monoorientation of kinetochores is established in a cohesion-mediated manner.","authors":"Yokobayashi S, Watanabe Y","authors_abbrev":"Yokobayashi S et al.","pubmed_publication_date":"02 Dec 2005","pubmed_entrez_date":"2005-12-06","publication_year":"2005","canto_session_key":"db9b5a7b5f36c25c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-05-15 19:18:05","canto_approved_date":"2023-09-28 19:09:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-19 17:12:12","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.03c","SPBC29A10.14","SPAC110.02","SPAC19D5.11c","SPAC31A2.15c","SPAC17A5.11","SPAC15E1.07c","SPBC1861.01c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2021-05-15"},{"uniquename":"PMID:9868371","title":"Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals.","citation":"Trends Biochem Sci 1998 Dec;23(12):481-5","abstract":"MAP-kinase signaling pathways are activated by multiple extracellular stimuli. The specificity of activation and function of MAP-kinase signaling modules is determined, in part, by scaffold proteins that create multienzyme complexes. In Saccharomyces cerevisiae, two MAP-kinase-scaffold proteins have been identified. Recent studies of mammalian cells have also led to the identification of putative scaffold proteins. These scaffold proteins appear to facilitate MAP-kinase activation, in response to specific physiological stimuli, and to insulate the bound MAP-kinase module against activation by irrelevant stimuli. Scaffold proteins are therefore critical components of MAP-kinase modules and ensure signaling specificity.","authors":"Whitmarsh AJ, Davis RJ","authors_abbrev":"Whitmarsh AJ et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1998-12-30","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8918880","title":"20S cyclosome complex formation and proteolytic activity inhibited by the cAMP/PKA pathway.","citation":"Nature 1996 Nov 21;384(6606):276-9","abstract":"The 20S cyclosome complex (also known as the anaphase-promoting complex) has ubiquitin ligase activity and is required for mitotic cyclin destruction and sister chromatid separation. The formation and activation of the 20S cyclosome complex is regulated by an unknown mechanism. Here we show that Cut4 (ref. 6) is an essential component of the cyclosome in fission yeast. Cut4 shares sequence similarity with BimE, a protein that regulates mitosis in Aspergillus nidulans. Mutations in cut4 result in hypersensitivity to cyclic AMP and to stress-inducing heavy metals, inhibition of the onset of anaphase, disruption of the 20S complex, and inhibition of mitotic cyclin ubiquitination. These phenotypes are fully suppressed by cAMP phosphodiesterase and the protein kinase A (PKA) regulatory subunit and weakly suppressed by Sti1 (an activator of the Hsp70 and Hsp90 chaperones). Suppression correlates with the amount of 20S complex, indicating that cyclosome formation and activation is inhibited by the cAMP/PKA pathway.","authors":"Yamashita YM, Nakaseko Y, Samejima I, Kumada K, Yamada H, Michaelson D, Yanagida M","authors_abbrev":"Yamashita YM et al.","pubmed_publication_date":"21 Nov 1996","pubmed_entrez_date":"1996-11-21","publication_year":"1996","canto_session_key":"60cfb81b2cb37543","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-21 14:35:59","canto_approved_date":"2026-01-29 12:09:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-13 13:53:49","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPAC6F12.15c","SPBC106.09","SPCC285.09c","SPAC8C9.03","SPCC645.14c","SPAC17C9.01c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2016-09-21"},{"uniquename":"PMID:9367977","title":"The control of septum formation in fission yeast.","citation":"Genes Dev 1997 Nov 15;11(22):2939-51","abstract":"","authors":"Gould KL, Simanis V","authors_abbrev":"Gould KL et al.","pubmed_publication_date":"15 Nov 1997","pubmed_entrez_date":"1997-12-31","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU014441","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19864459","title":"Roles of formin nodes and myosin motor activity in Mid1p-dependent contractile-ring assembly during fission yeast cytokinesis.","citation":"Mol Biol Cell 2009 Dec;20(24):5195-210","abstract":"Two prevailing models have emerged to explain the mechanism of contractile-ring assembly during cytokinesis in the fission yeast Schizosaccharomyces pombe: the spot/leading cable model and the search, capture, pull, and release (SCPR) model. We tested some of the basic assumptions of the two models. Monte Carlo simulations of the SCPR model require that the formin Cdc12p is present in >30 nodes from which actin filaments are nucleated and captured by myosin-II in neighboring nodes. The force produced by myosin motors pulls the nodes together to form a compact contractile ring. Live microscopy of cells expressing Cdc12p fluorescent fusion proteins shows for the first time that Cdc12p localizes to a broad band of 30-50 dynamic nodes, where actin filaments are nucleated in random directions. The proposed progenitor spot, essential for the spot/leading cable model, usually disappears without nucleating actin filaments. alpha-Actinin ain1 deletion cells form a normal contractile ring through nodes in the absence of the spot. Myosin motor activity is required to condense the nodes into a contractile ring, based on slower or absent node condensation in myo2-E1 and UCS rng3-65 mutants. Taken together, these data provide strong support for the SCPR model of contractile-ring formation in cytokinesis.","authors":"Coffman VC, Nile AH, Lee IJ, Liu H, Wu JQ","authors_abbrev":"Coffman VC et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-10-30","publication_year":"2009","canto_session_key":"0605d16350ff45c7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30583377","title":"Antioxidant and antimicrobial properties of randomly methylated β cyclodextrin - captured essential oils.","citation":"Food Chem 2019 Apr 25;278:305-313","abstract":"Free essential oils and their active components have a low physiochemical stability and low aqueous solubility which limit their applications as food preservatives and in packaging industry. The aim of this study was to characterize the physicochemical properties, antioxidant activities and antimicrobial activity of randomly methylated β cyclodextrin (RAMEB) encapsulated thyme oil, lemon balm oil, lavender oil, peppermint oil and their active components that include thymol, citral, linalool, menthol and borneol. Inclusion complex formation of essential oils (EOs) and RAMEB were evaluated by several methods. Antioxidant capacities of RAMEB-EOs/components were reported to be more stable than free EOs/components (P < 0.05). Rapid SYBR green I/propidium iodide live/dead microbial cellular discrimination assay for Schizosaccharomyces pombe, Escherichia coli and Staphylococcus aureus showed similar results when compared with flow cytometry analysis (P < 0.01) suggesting that our novel microplate fluorescence method could be applied for the fast live/dead microbial discrimination in antimicrobial assays.","doi":"10.1016/j.foodchem.2018.11.047","authors":"Das S, Gazdag Z, Szente L, Meggyes M, Horváth G, Lemli B, Kunsági-Máté S, Kuzma M, Kőszegi T","authors_abbrev":"Das S et al.","pubmed_publication_date":"25 Apr 2019","pubmed_entrez_date":"2018-12-26","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-12-27 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013689","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15483052","title":"BAF53/Arp4 homolog Alp5 in fission yeast is required for histone H4 acetylation, kinetochore-spindle attachment, and gene silencing at centromere.","citation":"Mol Biol Cell 2005 Jan;16(1):316-27","abstract":"Nuclear actin-related proteins play vital roles in transcriptional regulation; however, their biological roles remain elusive. Here, we characterize Alp5, fission yeast homolog of Arp4/BAF53. The temperature-sensitive mutant alp5-1134 contains a single amino acid substitution in the conserved C-terminal domain (S402N) and displays mitotic phenotypes, including chromosome condensation and missegregation. Alp5 forms a complex with Mst1-HAT (histone acetyltransferase). Consistently, inhibition of histone deacetylases (HDACs), by either addition of a specific inhibitor or a mutation in HDAC-encoding clr6+ gene, rescues alp5-1134. Immunoblotting with specific antibodies against acetylated histones shows that Alp5 is required for histone H4 acetylation at lysines 5, 8, and 12, but not histone H3 lysines 9 or 14, and furthermore Clr6 plays an opposing role. Mitotic arrest is ascribable to activation of the Mad2/Bub1 spindle checkpoint, in which both proteins localize to the mitotic kinetochores in alp5-1134. Intriguingly, alp5-1134 displays transcriptional desilencing at the core centromere without altering the overall chromatin structure, which also is suppressed by a simultaneous mutation in clr6+. This result shows that Alp5 is essential for histone H4 acetylation, and its crucial role lies in the establishment of bipolar attachment of the kinetochore to the spindle and transcriptional silencing at the centromere.","authors":"Minoda A, Saitoh S, Takahashi K, Toda T","authors_abbrev":"Minoda A et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-10-16","publication_year":"2005","canto_session_key":"3ddc3ca948411f8e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-04 10:17:13","canto_approved_date":"2022-02-11 15:40:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-27 18:41:10","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.17","SPBC3D6.04c","SPAC637.12c","SPAC23H3.08c","SPCC1322.12c","SPBC36.05c","SPCC1795.01c","SPBC582.03","SPBC20F10.06","SPAC27F1.04c","SPBP23A10.08","SPAC1687.20c","SPAC3G9.07c"],"gene_count":13,"ltp_gene_count":9,"approved_date":"2015-11-04"},{"uniquename":"PMID:27687866","title":"Genetic controls of DNA damage avoidance in response to acetaldehyde in fission yeast.","citation":"Cell Cycle 2017 Jan 02;16(1):45-58","abstract":"Acetaldehyde, a primary metabolite of alcohol, forms DNA adducts and disrupts the DNA replication process, causing genomic instability, a hallmark of cancer. Indeed, chronic alcohol consumption accounts for approximately 3.6% of all cancers worldwide. However, how the adducts are prevented and repaired after acetaldehyde exposure is not well understood. In this report, we used the fission yeast Schizosaccharomyces pombe as a model organism to comprehensively understand the genetic controls of DNA damage avoidance in response to acetaldehyde. We demonstrate that Atd1 functions as a major acetaldehyde detoxification enzyme that prevents accumulation of Rad52-DNA repair foci, while Atd2 and Atd3 have minor roles in acetaldehyde detoxification. We found that acetaldehyde causes DNA damage at the replication fork and activates the cell cycle checkpoint to coordinate cell cycle arrest with DNA repair. Our investigation suggests that acetaldehyde-mediated DNA adducts include interstrand-crosslinks and DNA-protein crosslinks. We also demonstrate that acetaldehyde activates multiple DNA repair pathways. Nucleotide excision repair and homologous recombination, which are both epistatically linked to the Fanconi anemia pathway, have major roles in acetaldehyde tolerance, while base excision repair and translesion synthesis also contribute to the prevention of acetaldehyde-dependent genomic instability. We also show the involvement of Wss1-related metalloproteases, Wss1 and Wss2, in acetaldehyde tolerance. These results indicate that acetaldehyde causes cellular stresses that require cells to coordinate multiple cellular processes in order to prevent genomic instability. Considering that acetaldehyde is a human carcinogen, our genetic studies serve as a guiding investigation into the mechanisms of acetaldehyde-dependent genomic instability and carcinogenesis.","doi":"10.1080/15384101.2016.1237326","authors":"Noguchi C, Grothusen G, Anandarajan V, Martínez-Lage García M, Terlecky D, Corzo K, Tanaka K, Nakagawa H, Noguchi E","authors_abbrev":"Noguchi C et al.","pubmed_publication_date":"02 Jan 2017","pubmed_entrez_date":"2016-10-01","publication_year":"2017","canto_session_key":"80aa26a88a0428ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Eishi Noguchi","canto_approved_date":"2016-11-10 15:35:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-10-27 16:56:28","canto_added_date":"2016-10-02 00:15:10","annotation_curators":[{"name":"Eishi Noguchi","community_curator":true,"annotation_count":46,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":72,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.01","SPAC9E9.09c","SPCC1442.07c","SPAC30D11.07","SPAC688.10","SPAC9.05","SPAC521.02","SPAC30D11.10","SPBC4F6.15c","SPAC922.07c","SPBC216.05","SPBC16A3.11","SPBC3D6.10","SPBC216.06c","SPAC688.06c","SPAC9E9.08","SPCC550.10","SPAC22A12.01c","SPBC146.06c","SPAC3G6.11","SPCC553.07c","SPAC644.14c"],"gene_count":22,"ltp_gene_count":22,"approved_date":"2016-10-27"},{"uniquename":"EMBL:U92792","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29032152","title":"Structure function characterization of the ELL Associated Factor (EAF) from Schizosaccharomyces pombe.","citation":"Gene 2018 Jan 30;641:117-128","abstract":"EAF (ELL Associated Factor) proteins interact with the transcription elongation factor, ELL (Eleven nineteen Lysine rich Leukemia) and enhance its ability to stimulate RNA polymerase II-mediated transcriptional elongation in vitro. Schizosaccharomyces pombe contains a single homolog of EAF (SpEAF), which is not essential for survival of S. pombe in contrast to its essential higher eukaryotic homologs. The physiological role of SpEAF is not well understood. In this study, we show that S. pombe EAF is important in regulating growth of S. pombe cells during normal growth conditions. Moreover, SpEAF is also essential for survival under conditions of DNA damage, while its deletion does not affect growth under environmental stress conditions. Our in vivo structure-function studies further demonstrate that while both the amino and carboxyl terminal domains of SpEAF possess the potential to activate transcription, only the amino terminal domain of SpEAF is involved in interaction with the S. pombe ELL protein. The carboxyl-terminus of SpEAF is required for rescue of the growth defect under normal and DNA damaging conditions that is associated with the absence of SpEAF. Using bioinformatics and circular dichroism spectroscopy, we show that the carboxyl-terminus of SpEAF has a disordered conformation. Furthermore, addition of trifluoroethanol triggered its transition from a disordered to α-helical conformation. Taken together, the results presented here identify novel structural and functional features of SpEAF protein, providing insights into how EAF proteins may enforce transcriptional control of gene expression.","doi":"10.1016/j.gene.2017.10.031","authors":"Dabas P, Sweta K, Ekka M, Sharma N","authors_abbrev":"Dabas P et al.","pubmed_publication_date":"30 Jan 2018","pubmed_entrez_date":"2017-10-17","publication_year":"2018","canto_session_key":"92e8195e77f492c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Preeti Dabas","canto_first_approved_date":"2018-11-02 17:29:18","canto_approved_date":"2025-09-03 17:22:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-25 14:52:31","canto_added_date":"2017-10-18 00:15:28","annotation_curators":[{"name":"Preeti Dabas","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.10c","SPBP23A10.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-11-02"},{"uniquename":"PMID:12193643","title":"Molecular biology. RNAi and heterochromatin--a hushed-up affair.","citation":"Science 2002 Sep 13;297(5588):1818-9","abstract":"","authors":"Allshire R","authors_abbrev":"Allshire R","pubmed_publication_date":"13 Sep 2002","pubmed_entrez_date":"2002-08-24","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22202177","title":"CYP105A1 mediated 3-hydroxylation of glimepiride and glibenclamide using a recombinant Bacillus megaterium whole-cell catalyst.","citation":"J Biotechnol 2012 Feb 10;157(3):405-12","abstract":"CYP105A1 from Streptomyces griseolus belongs to a widespread family of soluble prokaryotic cytochromes P450. For in vitro studies we established an electron transfer system, consisting of the ferredoxin Etp1(fd) and the ferredoxin reductase Arh1 from the fission yeast Schizosaccharomyces pombe. We investigated the metabolism of glibenclamide and glimepiride, hypoglycemic drugs of sulfonylurea type, and determined corresponding in vitro kinetic parameters. The resulting 3-cyclohexyl-hydroxylation activity towards glibenclamide and glimepiride was demonstrated by NMR analysis. Furthermore, the main product of glibenclamide, cis-3-hydroxy-glibenclamide is identical with the phase-1-metabolite of this drug in human. The orientation of glimepiride and glibenclamide in the active site of the enzyme is shown by a computational docking model. For high scale production of sulfonylurea derivatives, we designed whole-cell biocatalysts based on Bacillus megaterium MS941. Surprisingly, the system expressing only CYP105A1 showed a similar activity towards hydroxylation of glimepiride and glibenclamide compared to the system expressing additionally the redox partners, Arh1 and Etp1(fd)(516-618), indicating that the host strain provides a functional endogenous electron transfer system.","doi":"10.1016/j.jbiotec.2011.12.006","authors":"Kleser M, Hannemann F, Hutter M, Zapp J, Bernhardt R","authors_abbrev":"Kleser M et al.","pubmed_publication_date":"10 Feb 2012","pubmed_entrez_date":"2011-12-29","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34239122","title":"Membrane perturbation by lipidated Atg8 underlies autophagosome biogenesis.","citation":"Nat Struct Mol Biol 2021 Jul;28(7):583-593","abstract":"Autophagosome biogenesis is an essential feature of autophagy. Lipidation of Atg8 plays a critical role in this process. Previous in vitro studies identified membrane tethering and hemi-fusion/fusion activities of Atg8, yet definitive roles in autophagosome biogenesis remained controversial. Here, we studied the effect of Atg8 lipidation on membrane structure. Lipidation of Saccharomyces cerevisiae Atg8 on nonspherical giant vesicles induced dramatic vesicle deformation into a sphere with an out-bud. Solution NMR spectroscopy of Atg8 lipidated on nanodiscs identified two aromatic membrane-facing residues that mediate membrane-area expansion and fragmentation of giant vesicles in vitro. These residues also contribute to the in vivo maintenance of fragmented vacuolar morphology under stress in fission yeast, a moonlighting function of Atg8. Furthermore, these aromatic residues are crucial for the formation of a sufficient number of autophagosomes and regulate autophagosome size. Together, these data demonstrate that Atg8 can cause membrane perturbations that underlie efficient autophagosome biogenesis.","doi":"10.1038/s41594-021-00614-5","authors":"Maruyama T, Alam JM, Fukuda T, Kageyama S, Kirisako H, Ishii Y, Shimada I, Ohsumi Y, Komatsu M, Kanki T, Nakatogawa H, Noda NN","authors_abbrev":"Maruyama T et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-07-09","publication_year":"2021","canto_session_key":"26e948329e3e06ac","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-07-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28229207","title":"Engineering rTCA pathway and C4-dicarboxylate transporter for L-malic acid production.","citation":"Appl Microbiol Biotechnol 2017 May;101(10):4041-4052","abstract":"L-Malic acid is an important component of a vast array of food additives, antioxidants, disincrustants, pharmaceuticals, and cosmetics. Here, we presented a pathway optimization strategy and a transporter modification approach to reconstruct the L-malic acid biosynthesis pathway and transport system, respectively. First, pyruvate carboxylase (pyc) and malate dehydrogenase (mdh) from Aspergillus flavus and Rhizopus oryzae were combinatorially overexpressed to construct the reductive tricarboxylic acid (rTCA) pathway for L-malic acid biosynthesis. Second, the L-malic acid transporter (Spmae) from Schizosaccharomyces pombe was engineered by removing the ubiquitination motification to enhance the L-malic acid efflux system. Finally, the L-malic acid pathway was optimized by controlling gene expression levels, and the final L-malic acid concentration, yield, and productivity were up to 30.25 g L -1 , 0.30 g g -1 , and 0.32 g L -1  h -1  in the resulting strain W4209 with CaCO 3  as a neutralizing agent, respectively. In addition, these corresponding parameters of pyruvic acid remained at 30.75 g L -1 , 0.31 g g -1 , and 0.32 g L -1  h -1 , respectively. The metabolic engineering strategy used here will be useful for efficient production of L-malic acid and other chemicals.","doi":"10.1007/s00253-017-8141-8","authors":"Chen X, Wang Y, Dong X, Hu G, Liu L","authors_abbrev":"Chen X et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2017-02-24","publication_year":"2017","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2017-02-25 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8082169","title":"Complete absence of mitochondrial DNA in the petite-negative yeast Schizosaccharomyces pombe leads to resistance towards the alkaloid lycorine.","citation":"Curr Genet 1994 Jan;25(1):80-3","abstract":"The petite-positive yeast Saccharomyces cerevisiae can be efficiently and completely converted to respiratory-deficient cytoplasmic petite mutants by intercalating drugs. Rho0 petites from Schizosaccharomyces pombe could only be obtained in strains carrying a nuclear mutation. In this paper we report the efficient isolation of rho0 mutants in a Sch. pombe strain containing a mitochondrial mutator mutation. We also show that the alkaloid lycorine is able to differentiate between cells containing defective mitochondrial DNA (mit-) and those lacking mitochondrial DNA completely (rho0). Rho0 cells are resistant to the alkaloid whereas mit- and wild-type cells show the same sensitivity.","authors":"Massardo DR, Manna F, Schäfer B, Wolf K, Del Giudice L","authors_abbrev":"Massardo DR et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17032641","title":"Global roles of Ste11p, cell type, and pheromone in the control of gene expression during early sexual differentiation in fission yeast.","citation":"Proc Natl Acad Sci U S A 2006 Oct 17;103(42):15517-22","abstract":"Fission yeast cells belong to one of two specialized cell types, M or P. Specific environmental conditions trigger sexual differentiation, which leads to an internal program starting with pheromone signaling between M and P cells, followed by mating, meiosis, and sporulation. The initial steps of this process are controlled by Ste11p, a master transcriptional regulator that activates the expression of cell type-specific genes (only expressed in either M or P cells) as well as genes expressed in both M and P cells. Pheromone signaling is activated by Ste11p-dependent transcription and, in turn, enhances some of this transcription in a positive feedback. To obtain a genomewide view of Ste11p target genes, their cell-type specificity, and their dependence on pheromone, we used DNA microarrays along with different genetic and environmental manipulations of fission yeast cells. We identified 78 Ste11p-dependent genes, 12 and 4 of which are only expressed in M and P cells, respectively. These genes show differing grades of pheromone dependencies for Ste11p-activated transcription, ranging from complete independence to complete dependence on pheromone. We systematically deleted all novel cell type-specific genes and characterized their phenotype during sexual differentiation. A comparison with a similar data set from the distantly related budding yeast reveals striking conservation in both number and types of the proteins that define cell types. Given the divergent mechanisms regulating cell type-specific gene expression, our results highlight the plasticity of regulatory circuits, which evolve to allow adaptation to changing environments and lifestyles.","authors":"Mata J, Bähler J","authors_abbrev":"Mata J et al.","pubmed_publication_date":"17 Oct 2006","pubmed_entrez_date":"2006-10-13","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32C12.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15827614","title":"Mismatch dependent uracil/thymine-DNA glycosylases excise exocyclic hydroxyethano and hydroxypropano cytosine adducts.","citation":"Acta Biochim Pol 2005;52(1):149-65","abstract":"Exocyclic adducts of DNA bases, such as etheno- and hydroxyalkano- ones, are generated by a variety of bifunctional agents, including endogenously formed products of lipid peroxidation. In this work we selectively modified cytosines in the 5'-d(TTT TTT CTT TTT CTT TTT CTT TTT T)-3' oligonucleotide using: chloroacetaldehyde to obtain 3,N(4)-alpha-hydroxyethano- (HEC) and 3,N(4)-etheno- (epsilonC), acrolein to obtain 3,N(4)-alpha-hydroxypropano- (HPC) and crotonaldehyde to obtain 3,N(4)-alpha-hydroxy-gamma-methylpropano- (mHPC) adducts of cytosine. The studied adducts are alkali-labile which results in oligonucleotide strain breaks at the sites of modification upon strong base treatment. The oligonucleotides carrying adducted cytosines were studied as substrates of Escherichia coli Mug, human TDG and fission yeast Thp1p glycosylases. All the adducts studied are excised by bacterial Mug although with various efficiency: epsilonC >HEC >HPC >mHPC. The yeast enzyme excises efficiently epsilonC>HEC>HPC, whereas the human enzyme excises only epsilonC. The pH-dependence curves of excision of eC, HEC and HPC by Mug are bell shaped and the most efficient excision of adducts occurs within the pH range of 8.6-9.6. The observed increase of excision of HEC and HPC above pH 7.2 can be explained by deprotonation of these adducts, which are high pK(a) compounds and exist in a protonated form at neutrality. On the other hand, since epsilonC is in a neutral form in the pH range studied, we postulate an involvement of an additional catalytic factor. We hypothesize that the enzyme structure undergoes a pH-induced rearrangement allowing the participation of Lys68 of Mug in catalysis via a hydrogen bond interaction of its epsilon-amino group with N(4) of the cytosine exocyclic adducts.","authors":"Borys-Brzywczy E, Arczewska KD, Saparbaev M, Hardeland U, Schär P, Kuśmierek JT","authors_abbrev":"Borys-Brzywczy E et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-04-14","publication_year":"2005","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18177669","title":"Mim1 functions in an oligomeric form to facilitate the integration of Tom20 into the mitochondrial outer membrane.","citation":"J Mol Biol 2008 Feb 22;376(3):671-80","abstract":"The translocase of the outer mitochondrial membrane (TOM) complex is the general entry site into the organelle for newly synthesized proteins. Despite its central role in the biogenesis of mitochondria, the assembly process of this complex is not completely understood. Mim1 (mitochondrial import protein 1) is a mitochondrial outer membrane protein with an undefined role in the assembly of the TOM complex. The protein is composed of an N-terminal cytosolic domain, a central putative transmembrane segment (TMS) and a C-terminal domain facing the intermembrane space. Here we show that Mim1 is required for the integration of the import receptor Tom20 into the outer membrane. We further investigated what the structural characteristics allowing Mim1 to fulfil its function are. The N- and C-terminal domains of Mim1 are crucial neither for the function of the protein nor for its biogenesis. Thus, the TMS of Mim1 is the minimal functional domain of the protein. We show that Mim1 forms homo-oligomeric structures via its TMS, which contains two helix-dimerization GXXXG motifs. Mim1 with mutated GXXXG motifs did not form oligomeric structures and was inactive. With all these data taken together, we propose that the homo-oligomerization of Mim1 allows it to fulfil its function in promoting the integration of Tom20 into the mitochondrial outer membrane.","doi":"10.1016/j.jmb.2007.12.006","authors":"Popov-Celeketić J, Waizenegger T, Rapaport D","authors_abbrev":"Popov-Celeketić J et al.","pubmed_publication_date":"22 Feb 2008","pubmed_entrez_date":"2008-01-08","publication_year":"2008","canto_session_key":"b692d74e29d5a836","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-04-18 17:08:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-18 17:08:15","canto_added_date":"2016-04-18 17:07:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC713.08"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2016-04-18"},{"uniquename":"PMID:15062098","title":"Sid4p-Cdc11p assembles the septation initiation network and its regulators at the S. pombe SPB.","citation":"Curr Biol 2004 Apr 06;14(7):579-84","abstract":"The Schizosaccharomyces pombe septation initiation network (SIN) triggers actomyosin ring constriction, septation, and cell division. It is organized at the spindle pole body (SPB) by the scaffold proteins Sid4p and Cdc11p. Here, we dissect the contributions of Sid4p and Cdc11p in anchoring SIN components and SIN regulators to the SPB. We find that Sid4p interacts with the SIN activator, Plo1p, in addition to Cdc11p and Dma1p. While the C terminus of Cdc11p is involved in binding Sid4p, its N-terminal half is involved in a wide variety of direct protein-protein interactions, including those with Spg1p, Sid2p, Cdc16p, and Cdk1p-Cdc13p. Given that the localizations of the remaining SIN components depend on Spg1p or Cdc16p, these data allow us to build a comprehensive model of SIN component organization at the SPB. FRAP experiments indicate that Sid4p and Cdc11p are stable SPB components, whereas signaling components of the SIN are dynamically associated with these structures. Our results suggest that the Sid4p-Cdc11p complex organizes a signaling hub on the SPB and that this hub coordinates cell and nuclear division.","authors":"Morrell JL, Tomlin GC, Rajagopalan S, Venkatram S, Feoktistova AS, Tasto JJ, Mehta S, Jennings JL, Link A, Balasubramanian MK, Gould KL","authors_abbrev":"Morrell JL et al.","pubmed_publication_date":"06 Apr 2004","pubmed_entrez_date":"2004-04-06","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.06c","SPCC1739.11c","SPBC428.13c","SPBC11B10.09","SPBC582.03","SPAC6F6.08c","SPAC23C11.16","SPBC244.01c","SPAC24B11.11c"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:11003674","title":"Nuclear import of the retrotransposon Tf1 is governed by a nuclear localization signal that possesses a unique requirement for the FXFG nuclear pore factor Nup124p.","citation":"Mol Cell Biol 2000 Oct;20(20):7798-812","abstract":"Retroviruses, such as human immunodeficiency virus, that infect nondividing cells generate integration precursors that must cross the nuclear envelope to reach the host genome. As a model for retroviruses, we investigated the nuclear entry of Tf1, a long-terminal-repeat-containing retrotransposon of the fission yeast Schizosaccharomyces pombe. Because the nuclear envelope of yeasts remains intact throughout the cell cycle, components of Tf1 must be transported through the envelope before integration can occur. The nuclear localization of the Gag protein of Tf1 is different from that of other proteins tested in that it has a specific requirement for the FXFG nuclear pore factor, Nup124p. Using extensive mutagenesis, we found that Gag contained three nuclear localization signals (NLSs) which, when included individually in a heterologous protein, were sufficient to direct nuclear import. In the context of the intact transposon, mutations in the NLS that mapped to the first 10 amino acid residues of Gag significantly impaired Tf1 retrotransposition and abolished nuclear localization of Gag. Interestingly, this NLS activity in the heterologous protein was specifically dependent upon the presence of Nup124p. Deletion analysis of heterologous proteins revealed the surprising result that the residues in Gag with the NLS activity were independent from the residues that conveyed the requirement for Nup124p. In fact, a fragment of Gag that lacked NLS activity, residues 10 to 30, when fused to a heterologous protein, was sufficient to cause the classical NLS of simian virus 40 to require Nup124p for nuclear import. Within the context of the current understanding of nuclear import, these results represent the novel case of a short amino acid sequence that specifies the need for a particular nuclear pore complex protein.","authors":"Dang VD, Levin HL","authors_abbrev":"Dang VD et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-09-26","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24637325","title":"Cytokinetic nodes in fission yeast arise from two distinct types of nodes that merge during interphase.","citation":"J Cell Biol 2014 Mar 17;204(6):977-88","abstract":"We investigated the assembly of cortical nodes that generate the cytokinetic contractile ring in fission yeast. Observations of cells expressing fluorescent fusion proteins revealed two types of interphase nodes. Type 1 nodes containing kinase Cdr1p, kinase Cdr2p, and anillin Mid1p form in the cortex around the nucleus early in G2. Type 2 nodes with protein Blt1p, guanosine triphosphate exchange factor Gef2p, and kinesin Klp8p emerge from contractile ring remnants. Quantitative measurements and computer simulations showed that these two types of nodes come together by a diffuse-and-capture mechanism: type 2 nodes diffuse to the equator and are captured by stationary type 1 nodes. During mitosis, cytokinetic nodes with Mid1p and all of the type 2 node markers incorporate into the contractile ring, whereas type 1 nodes with Cdr1p and Cdr2p follow the separating nuclei before dispersing into the cytoplasm, dependent on septation initiation network signaling. The two types of interphase nodes follow parallel branches of the pathway to prepare nodes for cytokinesis.","doi":"10.1083/jcb.201307174","authors":"Akamatsu M, Berro J, Pu KM, Tebbs IR, Pollard TD","authors_abbrev":"Akamatsu M et al.","pubmed_publication_date":"17 Mar 2014","pubmed_entrez_date":"2014-03-19","publication_year":"2014","canto_session_key":"78d823a63014594c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15979194","title":"RNA interference and heterochromatin in the fission yeast Schizosaccharomyces pombe.","citation":"Trends Genet 2005 Aug;21(8):450-6","abstract":"Fission yeast is a useful model for RNA interference because it has single-copy genes for components of the RNAi pathway such as argonaute, dicer and RNA-dependent RNA polymerase (RdRP). Functions for RNAi revealed in S. pombe, such as heterochromatic silencing and chromosome segregation, are likely to be ancient because they are shared with some other eukaryotes. The underlying mechanisms are being rapidly unraveled.","authors":"Martienssen RA, Zaratiegui M, Goto DB","authors_abbrev":"Martienssen RA et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-06-28","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39945308","title":"Characterization of the Swi6/HP1 binding motif in its partner protein reveals the basis for the functional divergence of the HP1 family proteins in fission yeast.","citation":"FASEB J 2025 Feb 28;39(4):e70387","abstract":"The heterochromatin protein 1 (HP1) family recognizes lysine 9-methylated histone H3 (H3K9me) and recruits other transacting factors to establish higher order chromatin structures. In the fission yeast Schizosaccharomyces pombe (S. pombe), two HP1 family proteins, Swi6 and Chp2, play distinct roles in recruiting transacting factors: Swi6 primarily recruits Epe1, a Jumonji C domain-containing protein involved in histone H3K9 demethylation, whereas Chp2 recruits Mit1, a component of the Snf2/Hdac Repressive Complex. However, detailed mechanisms of how multiple HP1 family proteins and their respective interactors work cooperatively or exclusively to form higher order chromatin structures remain elusive. In this study, we investigated the interactions between Swi6 and Epe1. We found that Swi6 interacts with Epe1 through its chromoshadow domain, and identified a unique motif, named the FVI motif, in Epe1 involved in this interaction through detailed mapping of the region. Enhanced green fluorescent protein (EGFP) tethering assays showed that the FVI motif is sufficient to recruit ectopically expressed EGFP to heterochromatic regions, and mutational analyses revealed that conserved hydrophobic residues in this motif are essential for proper targeting. Structural simulations further supported the importance of these residues in Swi6 binding. Interestingly, Mit1 containing the Epe1 FVI motif was recruited to the heterochromatic regions by Swi6 but not by Chp2. Cells expressing mutant Mit1 maintained heterochromatic silencing even in chp2∆ cells, suggesting that Chp2 is not required for heterochromatin formation when Mit1 is recruited by Swi6. These findings highlight distinct HP1-binding motifs in interactors, contributing to functional divergence among HP1 family proteins.","doi":"10.1096/fj.202402264RR","authors":"Oya T, Tanaka M, Hayashi A, Yoshimura Y, Nakamura R, Arita K, Murakami Y, Nakayama JI","authors_abbrev":"Oya T et al.","pubmed_publication_date":"28 Feb 2025","pubmed_entrez_date":"2025-02-13","publication_year":"2025","canto_session_key":"855fbb0238fc409f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-ichi Nakayama","canto_first_approved_date":"2025-04-10 07:44:27","canto_approved_date":"2025-04-10 07:44:27","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-03-26 08:25:37","canto_added_date":"2025-02-14 00:25:05","annotation_curators":[{"name":"Jun-ichi Nakayama","community_curator":true,"annotation_count":11,"orcid":"0000-0002-5597-8239","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":9,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16C6.10","SPBC428.08c","SPAC664.01c","SPCC330.05c","SPBP35G2.10","SPAC1142.03c","SPCC622.16c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2025-04-10"},{"uniquename":"PMID:7953533","title":"A molecular evolutionary framework for eukaryotic model organisms.","citation":"Curr Biol 1994 Jul 01;4(7):596-603","abstract":"Implicit in the characterization of a model organism is the hope that insights into its biology can be extended to other species. For this hope to be fulfilled, the phylogenetic position of the model organism within a larger evolutionary framework must be known. We focus here on major model organisms of developmental genetics and cell biology. We first consider the positions of the nematode Caenorhabditis elegans and the arthropod Drosophila melanogaster within a phylogeny of the major advanced metazoan groups. Then we consider the evolutionary relationships between fungi (represented by Saccharomyces cerevisiae and Schizosaccharomyces pombe), plants, and animals.\nWe show, by a direct comparison with small subunit ribosomal RNA (18 S rRNA), that RNA polymerase II is an appropriate molecule for addressing the phylogenetic branchings in the early evolution of eukaryotes. The results from the analyses of newly determined and previously published sequences of the two largest subunits of RNA polymerase II suggest the following. Firstly, that plants and animals share a last common ancestor that excludes fungi, the lineage of which originated earlier. Secondly, that the lineage leading to the nematode Caenorhabditis elegans diverged earlier from the Metazoa than the lineages of arthropods, deuterostomes, annelids and molluscs. Finally, that deuterostomes arose from within protostomes.\nRNA polymerase II is well-suited for the elucidation of the evolutionary relationships among eukaryotes. We emphasize the implications of our results for other biological disciplines in addition to molecular evolution, as a phylogenetic framework allows predictions and inferences to be made about the existence of fundamental biological mechanisms elucidated in model organisms.","authors":"Sidow A, Thomas WK","authors_abbrev":"Sidow A et al.","pubmed_publication_date":"01 Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12832769","title":"Expression, purification and preliminary X-ray analysis of the BRCT domain from Rhp9/Crb2.","citation":"Acta Crystallogr D Biol Crystallogr 2003 Jul;59(Pt 7):1230-3","abstract":"The BRCT domain from Rhp9 (a Schizosaccharomyces pombe DNA-damage checkpoint protein) has been expressed, purified and crystallized. Overexpression in bacterial cells was achieved by minimizing aeration during host cell growth. A robotic screen was used to determine the solubility parameters; concentration of the protein was achieved by exploiting this information. Single crystals suitable for X-ray analysis were obtained in two forms by vapour diffusion (trigonal, unit-cell parameters a = b = 228.04, c = 70.42 A, and tetragonal, P4/m Laue group symmetry, unit-cell parameters a = b = 72.3, c = 91.1 A).","authors":"Hinks JA, Roe M, Ho JC, Watts FZ, Phelan J, McAllister M, Pearl LH","authors_abbrev":"Hinks JA et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-07-02","publication_year":"2003","canto_session_key":"717f8411adb629b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-08 09:58:57","canto_approved_date":"2019-11-08 09:58:58","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-08 09:58:52","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC342.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-11-08"},{"uniquename":"PMID:27855785","title":"Sec24 phosphorylation regulates autophagosome abundance during nutrient deprivation.","citation":"Elife 2016 Nov 18;5","abstract":"Endoplasmic Reticulum (ER)-derived COPII coated vesicles constitutively transport secretory cargo to the Golgi. However, during starvation-induced stress, COPII vesicles have been implicated as a membrane source for autophagosomes, distinct organelles that engulf cellular components for degradation by macroautophagy (hereafter called autophagy). How cells regulate core trafficking machinery to fulfill dramatically different cellular roles in response to environmental cues is unknown. Here we show that phosphorylation of conserved amino acids on the membrane-distal surface of the  Saccharomyces cerevisiae  COPII cargo adaptor, Sec24, reprograms COPII vesicles for autophagy. We also show casein kinase 1 (Hrr25) is a key kinase that phosphorylates this regulatory surface. During autophagy, Sec24 phosphorylation regulates autophagosome number and its interaction with the C-terminus of Atg9, a component of the autophagy machinery required for autophagosome initiation. We propose that the acute need to produce autophagosomes during starvation drives the interaction of Sec24 with Atg9 to increase autophagosome abundance.","doi":"10.7554/eLife.21167","authors":"Davis S, Wang J, Zhu M, Stahmer K, Lakshminarayan R, Ghassemian M, Jiang Y, Miller EA, Ferro-Novick S","authors_abbrev":"Davis S et al.","pubmed_publication_date":"18 Nov 2016","pubmed_entrez_date":"2016-11-19","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F8.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:39057340","title":"The Mechanosensitive Pkd2 Channel Modulates the Recruitment of Myosin II and Actin to the Cytokinetic Contractile Ring.","citation":"J Fungi (Basel) 2024 Jun 28;10(7)","abstract":"Cytokinesis, the last step in cell division, separates daughter cells through mechanical force. This is often through the force produced by an actomyosin contractile ring. In fission yeast cells, the ring helps recruit a mechanosensitive ion channel, Pkd2, to the cleavage furrow, whose activation by membrane tension promotes calcium influx and daughter cell separation. However, it is unclear how the activities of Pkd2 may affect the actomyosin ring. Here, through both microscopic and genetic analyses of a hypomorphic  pkd2  mutant, we examined the potential role of this essential gene in assembling the contractile ring. The  pkd2-81KD  mutation significantly increased the counts of the type II myosin heavy chain Myo2 (+18%), its regulatory light chain Rlc1 (+37%) and actin (+100%) molecules in the ring, compared to the wild type. Consistent with a regulatory role of Pkd2 in the ring assembly, we identified a strong negative genetic interaction between  pkd2-81KD  and the temperature-sensitive mutant  myo2-E1 . The  pkd2-81KD myo2-E1  cells often failed to assemble a complete contractile ring. We conclude that Pkd2 modulates the recruitment of type II myosin and actin to the contractile ring, suggesting a novel calcium-dependent mechanism regulating the actin cytoskeletal structures during cytokinesis.","doi":"10.3390/jof10070455","authors":"Chowdhury P, Sinha D, Poddar A, Chetluru M, Chen Q","authors_abbrev":"Chowdhury P et al.","pubmed_publication_date":"28 Jun 2024","pubmed_entrez_date":"2024-07-26","publication_year":"2024","canto_session_key":"b3d2056aaedad536","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-07-26 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21098141","title":"Cellular stress induces cytoplasmic RNA granules in fission yeast.","citation":"RNA 2011 Jan;17(1):120-33","abstract":"Severe stress causes plant and animal cells to form large cytoplasmic granules containing RNA and proteins. Here, we demonstrate the existence of stress-induced cytoplasmic RNA granules in Schizosaccharomyces pombe. Homologs to several known protein components of mammalian processing bodies and stress granules are found in fission yeast RNA granules. In contrast to mammalian cells, poly(A)-binding protein (Pabp) colocalizes in stress-induced granules with decapping protein. After glucose deprivation, protein kinase A (PKA) is required for accumulation of Pabp-positive granules and translational down-regulation. This is the first demonstration of a role for PKA in RNA granule formation. In mammals, the translation initiation protein eIF2α is a key regulator of formation of granules containing poly(A)-binding protein. In S. pombe, nonphosphorylatable eIF2α does not block but delays granule formation and subsequent clearance after exposure to hyperosmosis. At least two separate pathways in S. pombe appear to regulate stress-induced granules: pka1 mutants are fully proficient to form granules after hyperosmotic shock; conversely, eIF2α does not affect granule formation in glucose starvation. Further, we demonstrate a Pka1-dependent link between calcium perturbation and RNA granules, which has not been described earlier in any organism.","doi":"10.1261/rna.2268111","authors":"Nilsson D, Sunnerhagen P","authors_abbrev":"Nilsson D et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-11-25","publication_year":"2011","canto_session_key":"4aeea6750a0a5a58","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Per Sunnerhagen","canto_first_approved_date":"2015-11-05 15:46:42","canto_approved_date":"2025-09-04 12:10:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-19 08:05:18","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Per Sunnerhagen","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.04c","SPAC24B11.06c","SPBC17D11.05","SPBC16D10.08c","SPAC17C9.03","SPBC106.10","SPBC36B7.09","SPAC3G9.09c","SPAC17A2.09c","SPAC19A8.12"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2015-11-05"},{"uniquename":"PMID:10898975","title":"Dynamics of interphase microtubules in Schizosaccharomyces pombe.","citation":"Curr Biol 2000 Jun 29;10(13):766-75","abstract":"Microtubules in interphase Schizosaccharomyces pombe are essential for maintaining the linear growth habit of these cells. The dynamics of assembly and disassembly of these microtubules are so far uncharacterised.\nLive cell confocal imaging of alpha1 tubulin tagged with enhanced green fluorescent protein revealed longitudinally oriented, dynamically unstable interphase microtubule assemblies (IMAs). The IMAs were uniformly bright along their length apart from a zone of approximately doubly intense fluorescence commonly present close to their centres. The ends of each IMA switched from growth ( approximately 3.0 microm/min) to shrinkage ( approximately 4.5 microm/min) at 1.0 events per minute and from shrinkage to growth at 1.9 events per minute, and the two ends were equivalently dynamic, suggesting equivalent structure. We accordingly propose a symmetrical model for microtubule packing within the IMAs, in which microtubules are plus ends out and overlap close to the equator of the cell. IMAs may contain multiple copies of this motif; if so, then within each IMA end, the microtubule ends must synchronise catastrophe and rescue. When both ends of an IMA lodge in the hemispherical cell ends, the IMAs start to bend under compression and their overall growth rate is inhibited about twofold. Similar microtubule dynamics were observed in cells ranging in size from half to twice normal length. Patterned photobleaching indicated no detectable treadmilling or microtubule sliding during interphase.\nThe consequence of the mechanisms described is continuous recruitment of microtubule ends to the ends of growing cells, supporting microtubule-based transport into the cell ends and qualitatively accounting for the essential role for microtubules in directing linear cell growth in S. pombe.","authors":"Drummond DR, Cross RA","authors_abbrev":"Drummond DR et al.","pubmed_publication_date":"29 Jun 2000","pubmed_entrez_date":"2000-07-19","publication_year":"2000","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31766775","title":" Schizosaccharomyces pombe  can Reduce Acetic Acid Produced by  Baijiu  Spontaneous Fermentation Microbiota.","citation":"Microorganisms 2019 Nov 22;7(12)","abstract":"The spontaneous fermentation of alcoholic beverage is a bioprocess donated by microbiota with complex stress environments. Among various microbes, non- Saccharomyces  yeasts have high stress tolerance and significantly affect the taste and quality of products in process. Although many researchers have focused on the influence of acid stress, the mechanism of non- Saccharomyces  yeasts to tolerant stress remains unclear in microbiota. To bridge the gap, we constructed in situ and in vitro studies to explore the reduction pathway of acetic acid in non- Saccharomyces  yeasts. In this study, we found  Schizosaccharomyces pombe  has special capacities to resist 10 g/L acetic acid in laboratory cultures and decrease the average concentration of acetic acid from 9.62 to 6.55 g/kg fermented grains in Chinese Maotai-flavor liquor ( Baijiu ) production. Moreover,  Schi. pombe  promoted metabolic level of mevalonate pathway (high expressions of gene  ACCAT1 ,  HMGCS1,  and  HMGCR1 ) to degrade a high concentration of acetic acid. Meanwhile,  Schi. pombe  also improved the concentration of mevalonic acid that is the precursor of terpenes to enhance the taste and quality of  Baijiu . Overall, the synchronicity of reduction and generation in  Schi. pombe  advances the current knowledge to guide more suitable strategies for mechanism studies of non- Saccharomyces  yeasts in fermented industries of alcoholic beverages.","doi":"10.3390/microorganisms7120606","authors":"Song Z, Du H, Zhang M, Nie Y, Xu Y","authors_abbrev":"Song Z et al.","pubmed_publication_date":"22 Nov 2019","pubmed_entrez_date":"2019-11-27","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-11-28 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36537249","title":"The fission yeast kinetochore complex Mhf1-Mhf2 regulates the spindle assembly checkpoint and faithful chromosome segregation.","citation":"J Cell Sci 2023 Jan 15;136(2)","abstract":"The outer kinetochore serves as a platform for the initiation of the spindle assembly checkpoint (SAC) and for mediating kinetochore-microtubule attachments. How the inner kinetochore subcomplex CENP-S-CENP-X is involved in regulating the SAC and kinetochore-microtubule attachments has not been well characterized. Using live-cell microscopy and yeast genetics, we found that Mhf1-Mhf2, the CENP-S-CENP-X counterpart in the fission yeast Schizosaccharomyces pombe, plays crucial roles in promoting the SAC and regulating chromosome segregation. The absence of Mhf2 attenuates the SAC, impairs the kinetochore localization of most of the components in the constitutive centromere-associated network (CCAN), and alters the localization of the kinase Ark1 (yeast homolog of Aurora B) to the kinetochore. Hence, our findings constitute a model in which Mhf1-Mhf2 ensures faithful chromosome segregation by regulating the accurate organization of the CCAN complex, which is required for promoting SAC signaling and for regulating kinetochore-microtubule attachments. This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.260124","authors":"Jian Y, Nie L, Liu S, Jiang Y, Dou Z, Liu X, Yao X, Fu C","authors_abbrev":"Jian Y et al.","pubmed_publication_date":"15 Jan 2023","pubmed_entrez_date":"2022-12-20","publication_year":"2023","canto_session_key":"3e04cbe2621b6a70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yanze Jian","canto_first_approved_date":"2023-04-08 16:10:46","canto_approved_date":"2026-03-12 12:04:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-04-13 14:25:48","canto_added_date":"2022-12-21 01:15:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yanze Jian","community_curator":true,"annotation_count":21,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.13","SPBP22H7.09c","SPCC1235.07","SPBC2D10.16","SPBC409.04c","SPCC1322.12c","SPCC1020.02","SPBC1861.01c","SPBP8B7.12c","SPAC25B8.14","SPBC18E5.03c","SPAC4F10.12","SPBC20F10.06","SPAC1783.03","SPCC576.12c","SPBC11C11.03"],"gene_count":16,"ltp_gene_count":3,"approved_date":"2023-04-08"},{"uniquename":"PMID:25825514","title":"To avoid a mating mishap, yeast focus and communicate.","citation":"J Cell Biol 2015 Mar 30;208(7):867-8","abstract":"During mating, yeast cells must perforate their rigid cell walls at the right place to allow cell-cell fusion. In this issue, Dudin et al. (2015; J. Cell Biol. http://dx.doi.org/jcb.201411124) image mating fission yeast cells with unprecedented spatiotemporal resolution. The authors find that when mating cells come into contact, they form aster-like actin structures that direct cell wall remodeling precisely to the point of contact.","doi":"10.1083/jcb.201502095","authors":"McClure AW, Lew DJ","authors_abbrev":"McClure AW et al.","pubmed_publication_date":"30 Mar 2015","pubmed_entrez_date":"2015-04-01","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-04-02 00:18:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20127475","title":"Generation of expression vectors for high-throughput functional analysis of target genes in Schizosaccharomyces pombe.","citation":"J Microbiol 2009 Dec;47(6):789-95","abstract":"An immediate challenge in the post-genomic era is to assign a biological functions to proteins unraveled by genome analysis. This report is based on studies conducted using Schizosaccharomyces pombe, a simple model organism, and presents various vector systems as tools for high-throughput functional analysis of human genes. We constructed S. pombe expression vectors for efficient cloning of genes via the Gateway system. We modified the pREP and pSLF series vectors, which are widely used for gene expression in S. pombe. The vectors constructed have a uniform backbone of S. pombe autonomously replicating sequence (ARS) elements with different selective markers, namely, urw4 (+) and Saccharomyces cerevisiae LEU2 complementing leul. These vectors contain 3 different strengths of the inducible promoter nmtl, which affect the expression levels of the cloned open reading frames (ORFs). Further, target proteins can be fused with an N-terminal or C-terminal tag such as triple hemagglutinin (3x HA), enhanced green fluorescent protein (EGFP), or Discosoma red fluorescent protein (DsRed). We tested the feasibility of the constructed vectors by using 3 human genes, namely, RAB18, SCC-112, and PTEN. Proper expression of tagged RAB18 was confirmed by western blot analysis. Further, localization of RAB18, SCC112, and PTEN was demonstrated. The constructed vectors can be utilized for high-throughput functional analysis of heterologous genes.","doi":"10.1007/s12275-009-0010-4","authors":"Ahn J, Choi CH, Kang CM, Kim CH, Park HM, Song KB, Hoe KL, Won M, Chung KS","authors_abbrev":"Ahn J et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2010-02-04","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2569363","title":"The fission yeast cdc2/cdc13/suc1 protein kinase: regulation of catalytic activity and nuclear localization.","citation":"Cell 1989 Aug 11;58(3):485-97","abstract":"The products of the cdc13+ and cdc2+ genes form a stable complex that displays protein kinase activity in vitro. p63cdc13 is a substrate of p34cdc2, the catalytic subunit of the kinase. The histone H1 kinase activity of cdc2 oscillates during the cell cycle. Activation of the preformed cdc2/cdc13 complex at the G2/M transition requires cdc25+ gene function. Post-metaphase inactivation of the kinase is associated with loss of cdc13, which shares sequence homology with mitotic cyclins and, in common with these proteins, is degraded at each cell division. cdc13 and cdc2 co-localize in the cell nucleus. cdc2 is not degraded during mitosis, but in the absence of cdc13 it is not localized in the nucleus. These observations suggest that the cdc13+-encoded cyclin acts to regulate both the catalytic properties and the localization of the protein kinase of which it is a subunit.","authors":"Booher RN, Alfa CE, Hyams JS, Beach DH","authors_abbrev":"Booher RN et al.","pubmed_publication_date":"11 Aug 1989","pubmed_entrez_date":"1989-08-11","publication_year":"1989","canto_session_key":"8855a2414459b824","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-13 10:47:51","canto_approved_date":"2023-05-04 12:39:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-19 14:32:04","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC1734.14c","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-11-13"},{"uniquename":"PMID:7254221","title":"Spontaneous and UV-induced recombination in radiation-sensitive mutants of Schizosaccharomyces pombe.","citation":"Mutat Res 1981 Mar;81(1):37-48","abstract":"The rad alleles of 18 unlinked genes of S. pombe were tested for their level of spontaneous meiotic, spontaneous mitotic and UV-induced mitotic recombination in the ade7-50 x ade7-152 interval. The effects of these rad alleles on meiosis and cell morphology were also studied. None of these mutants showed a clear-cut reduction of spontaneous recombination rates, no matter whether they had lost or retained a caffeine-sensitive repair of UV-induced lesions, which has previously been interpreted as a recombinational pathway of DNA repair (Fabre, 1972a; Gentner, 1977; Gentner et al., 1978). rad1-1 was the only mutant with a reduced frequency of UV-induced recombination. Some mutants displayed an increased frequency of mitotic recombination, either spontaneously (rad 15-P, rad 21-45), UV-induced (rad8-190) or both (rad2-44). Previous hypothesis on the contribution of recombination to DNA repair in S. pombe are reconsidered in the light of these data.","authors":"Grossenbacher-Grunder AM, Thuriaux P","authors_abbrev":"Grossenbacher-Grunder AM et al.","pubmed_publication_date":"Mar 1981","pubmed_entrez_date":"1981-03-01","publication_year":"1981","canto_session_key":"c16d1f65344ac5bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-05 16:44:37","canto_approved_date":"2023-08-03 08:36:01","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2016-01-05 16:44:29","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.01","SPAC14C4.13","SPCC5E4.06","SPAC1D4.12","SPCC338.17c","SPAC3G6.06c","SPAC1952.07","SPAC30D11.10","SPBC216.05","SPAC664.07c","SPAC23C4.18c","SPBC3E7.08c","SPAC13G6.01c","SPAC18B11.07c"],"gene_count":14,"ltp_gene_count":6,"approved_date":"2016-01-05"},{"uniquename":"PMID:38525852","title":"Recent Advances on Small-Molecule Inhibitors of Lipocalin-like Proteins.","citation":"J Med Chem 2024 Apr 11;67(7):5144-5167","abstract":"Lipid transfer proteins (LTPs) are crucial players in nonvesicular lipid trafficking. LTPs sharing a lipocalin lipid transfer domain (lipocalin-like proteins) have a wide range of biological functions, such as regulating immune responses and cell proliferation, differentiation, and death as well as participating in the pathogenesis of inflammatory, metabolic, and neurological disorders and cancer. Therefore, the development of small-molecule inhibitors targeting these LTPs is important and has potential clinical applications. Herein, we summarize the structure and function of lipocalin-like proteins, mainly including retinol-binding proteins, lipocalins, and fatty acid-binding proteins and discuss the recent advances on small-molecule inhibitors for these protein families and their applications in disease treatment. The findings of our Perspective can provide guidance for the development of inhibitors of these LTPs and highlight the challenges that might be faced during the procedures.","doi":"10.1021/acs.jmedchem.4c00086","authors":"Chen S, Pan Z, Liu M, Guo L, Jiang X, He G","authors_abbrev":"Chen S et al.","pubmed_publication_date":"11 Apr 2024","pubmed_entrez_date":"2024-03-25","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC36B7.02","SPCC584.11c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:17248549","title":"Site Specific Induction of Gene Conversion in SCHIZOSACCHAROMYCES POMBE.","citation":"Genetics 1971 Nov;69(3):317-37","abstract":"","authors":"Gutz H","authors_abbrev":"Gutz H","pubmed_publication_date":"Nov 1971","pubmed_entrez_date":"1971-11-01","publication_year":"1971","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29681468","title":"Discrimination against RNA Backbones by a ssDNA Binding Protein.","citation":"Structure 2018 May 01;26(5):722-733.e2","abstract":"Pot1 is the shelterin component responsible for the protection of the single-stranded DNA (ssDNA) overhang at telomeres in nearly all eukaryotic organisms. The C-terminal domain of the DNA-binding domain, Pot1pC, exhibits non-specific ssDNA recognition, achieved through thermodynamically equivalent alternative binding conformations. Given this flexibility, it is unclear how specificity for ssDNA over RNA, an activity required for biological function, is achieved. Examination of the ribose-position specificity of Pot1pC shows that ssDNA specificity is additive but not uniformly distributed across the ligand. High-resolution structures of several Pot1pC complexes with RNA-DNA chimeric ligands reveal Pot1pC discriminates against RNA by utilizing non-compensatory binding modes that feature significant rearrangement of the binding interface. These alternative conformations, accessed through both ligand and protein flexibility, recover much, but not all, of the binding energy, leading to the observed reduction in affinities. These findings suggest that intermolecular interfaces are remarkably sophisticated in their tuning of specificity toward flexible ligands.","doi":"10.1016/j.str.2018.03.016","authors":"Lloyd NR, Wuttke DS","authors_abbrev":"Lloyd NR et al.","pubmed_publication_date":"01 May 2018","pubmed_entrez_date":"2018-04-24","publication_year":"2018","canto_session_key":"b9c34809dff1903d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-02-24 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"5uso","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"199-337"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssRNA/ssDNA chimera (GGTTACrGrGrU)","entry_authors":"Lloyd NR,Wuttke DS","entry_authors_abbrev":"Lloyd NR et al.","reference_uniquename":"PMID:29681468","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"5usn","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"199-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssRNA/ssDNA chimera (rGrGrUTACGGT)","entry_authors":"Lloyd NR,Wuttke DS","entry_authors_abbrev":"Lloyd NR et al.","reference_uniquename":"PMID:29681468","experimental_method":"X-ray","resolution":"1.9"},{"pdb_id":"5usb","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"199-337"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssRNA/ssDNA chimera (rGGTTACGGT)","entry_authors":"Lloyd NR,Wuttke DS","entry_authors_abbrev":"Lloyd NR et al.","reference_uniquename":"PMID:29681468","experimental_method":"X-ray","resolution":"1.615"}]},{"uniquename":"PMID:7642145","title":"Isolation and characterization of SpTRK, a gene from Schizosaccharomyces pombe predicted to encode a K+ transporter protein.","citation":"Gene 1995 Aug 08;161(1):97-101","abstract":"A novel gene, SpTRK, has been isolated from DNA of the fission yeast Schizosaccharomyces pombe (Sp) by hybridization to an oligodeoxyribonucleotide (oligo) probe designed from a sequence fully conserved between the potassium transporter genes TRK1 and TRK2 of Saccharomyces cerevisiae (Sc). SpTRK is a single-copy gene located on Sp chromosome I. Nucleotide sequence analysis of the cloned gene identified an open reading frame (ORF) with coding capacity for a protein of 833 amino acids (aa). The predicted SpTRK aa sequence showed a high level of conservation relative to the potassium transporters of Sc and Saccharomyces uvarum (Su), particularly within their transmembrane (TM) domains and in aa required for their ion transport functions. A single SpTRK transcript of about 2.7 kb is expressed at high levels in exponentially growing Sp cells, but it is downregulated in cells from stationary cultures.","authors":"Soldatenkov VA, Velasco JA, Avila MA, Dritschilo A, Notario V","authors_abbrev":"Soldatenkov VA et al.","pubmed_publication_date":"08 Aug 1995","pubmed_entrez_date":"1995-08-08","publication_year":"1995","canto_session_key":"1bf84fcc64ed9c24","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:43:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 21:30:56","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3F10.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-25"},{"uniquename":"PMID:31989521","title":"Pulsed-Field Gel Electrophoresis for Detecting Chromosomal DNA Breakage in Fission Yeast.","citation":"Methods Mol Biol 2020;2119:135-143","abstract":"DNA-strand breaks influence structure and function of chromosomes in diverse ways, and it is essential to analyze the lesions to understand behaviors of genetic information. For researchers in a wide array of fields including recombination, repair, and DNA damage response, efficient and easy detection of DNA breaks is of paramount importance. Among several procedures suitable for this purpose, a method to directly observe broken chromosomes by pulsed-field gel electrophoresis, using the fission yeast Schizosaccharomyces pombe as a model organism, is described in this chapter. Because S. pombe chromosomes are megabase-size, careful attention should be paid to maintain DNA as intact as possible. The protocol includes induction of DNA breaks, preparation of chromosomes, and separation of chromosomal DNA by PFGE. This procedure can be applicable to other species as well as other experiments handling large-size DNA molecules.","doi":"10.1007/978-1-0716-0323-9_12","authors":"Yamada T, Murakami H, Ohta K","authors_abbrev":"Yamada T et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-01-29","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30408892","title":"Fungal responses to reactive oxygen species.","citation":"Med Mycol 2006 Sep 01;44(Supplement_1):S101-S107","abstract":"Reactive oxygen species (ROS) such as hydrogen peroxide, produced externally or during normal metabolism, can damage different cell components and usually trigger a counteracting antioxidant response. The fact that animals and humans utilize ROS and related nitrogen reactive species to prevent fungal infection has generated great interest in defining the components of the antioxidant response and studying their role as virulence determinants in fungi. Here we review the role of specific enzyme and non-enzyme mediated antioxidant mechanisms in virulence, as well as the signal transduction mechanisms that fungal cells use to perceive high ROS levels and induce gene expression. We focus on Schizosaccharomyces pombe antioxidant responses, which involve a prokaryotic-type multistep phosphorelay coupled to a stress-response MAP kinase pathway and an AP-1 type transcription factor, in relation to homologous mechanisms in Aspergillus nidulans and the human pathogen A. fumigatus. Compared to S. pombe and other unicellular fungi, filamentous fungi have additional mechanisms to handle ROS, such as the presence of a larger number of phosphorelay sensor kinases, antioxidant enzymes and secondary metabolites with antioxidant functions. In addition, filamentous fungi have enzymes like the NADPH oxidases, which regulate multicellular development through ROS production and therefore, offer a unique opportunity to study the interplay between ROS production, perception and detoxification, and the role of these processes in cell differentiation and pathogenesis.","doi":"10.1080/13693780600900080","authors":"Aguirre J, Hansberg W, Navarro R","authors_abbrev":"Aguirre J et al.","pubmed_publication_date":"01 Sep 2006","pubmed_entrez_date":"2018-11-10","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-12 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17246436","title":"The Ade6-M26 Mutation of Schizosaccharomyces Pombe Increases the Frequency of Crossing over.","citation":"Genetics 1988 Jul;119(3):507-15","abstract":"The ade6-M26 mutation of Schizosaccharomyces pombe increases conversion frequency in comparison with the nearby mutation ade6-M375. In order to investigate the effect of ade6-M26 on crossover frequency, heteroallelic ade6 duplications were constructed by integration of plasmids carrying the marker gene ura4. One ade6 gene carries either of the mutations M26 or M375 while the other ade6 copy carries the L469 mutation in both duplications. The duplication with ade6-M26 yields Ade(+) recombinants at significantly higher frequencies in meiosis, but not in mitosis. Tetrad analysis and physical characterization of spore clones from recombination tetrads demonstrate that conversions, unequal crossovers and intrachromatid exchanges occur at higher frequencies but with unaltered proportions among them. The conversion events show a pronounced bias when M26 is involved: they take place preferentially at the M26 allele. Thus the ade6-M26 mutation not only enhances conversion frequency as demonstrated before, but also crossover frequency. It displays the properties expected for a preferred site of initiation of general meiotic recombination. The duplications also yielded new information on ectopic recombination in S. pombe: ectopic crossovers occur in the duplications at much higher frequency than among naturally dispersed homologous sequences.","authors":"Schuchert P, Kohli J","authors_abbrev":"Schuchert P et al.","pubmed_publication_date":"Jul 1988","pubmed_entrez_date":"1988-07-01","publication_year":"1988","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33139498","title":"Lysing Yeast Cells with Glass Beads for Immunoprecipitation.","citation":"Cold Spring Harb Protoc 2020 Nov 02;2020(11)","abstract":"Yeast cells display cell walls that must first be broken before the addition of detergents for lysis. This method describes the use of glass beads in combination with a mechanical bead beater to disrupt cell walls of both  Saccharomyces cerevisiae  or  Schizosaccharomyces pombe  directly in a nonionic detergent Lysis buffer containing 0.1% Nonidet P-40. Alternatively, this protocol can be applied for the lysis of yeast cells in Lysis buffer without detergent; upon completion of the bead beating, Triton X-100 is added to complete lysis. Yeast cells are cultured and collected while in log phase before being washed once and mixed together with glass beads in a tube. The applied shaking process facilitates disruption of the cell walls, upon which separation of yeast and glass beads is accomplished by forcing lysed cells through a hole created in the bottom of the tube during the centrifugation process. An alternative bead-beating protocol details the use of Lysis Buffer 2, which does not contain detergents and calls for the addition of Triton X-100 after cell lysis in the presence of glass beads. Use of Lysis Buffer 2 without detergent may avoid bubble and foam formation during the bead-beating process that could potentially denature proteins.","doi":"10.1101/pdb.prot098590","authors":"DeCaprio J, Kohl TO","authors_abbrev":"DeCaprio J et al.","pubmed_publication_date":"02 Nov 2020","pubmed_entrez_date":"2020-11-03","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-11-05 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11583612","title":"Common themes in mechanisms of gene silencing.","citation":"Mol Cell 2001 Sep;8(3):489-98","abstract":"The assembly of DNA into regions of inaccessible chromatin, called silent chromatin, is involved in the regulation of gene expression and maintenance of chromosome stability in eukaryotes. Recent studies on Sir2-containing silencing complexes in budding yeast and HP1- and Swi6-containing silencing complexes in metazoans and fission yeast suggest a common mechanism for the assembly of these domains, which involves the physical coupling of histone modifying enzymes to histone binding proteins.","authors":"Moazed D","authors_abbrev":"Moazed D","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-10-05","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27146110","title":"Kinesin-8 effects on mitotic microtubule dynamics contribute to spindle function in fission yeast.","citation":"Mol Biol Cell 2016 Nov 07;27(22):3490-3514","abstract":"Kinesin-8 motor proteins destabilize microtubules. Their absence during cell division is associated with disorganized mitotic chromosome movements and chromosome loss. Despite recent work studying effects of kinesin-8s on microtubule dynamics, it remains unclear whether the kinesin-8 mitotic phenotypes are consequences of their effect on microtubule dynamics, their well-established motor activity, or additional, unknown functions. To better understand the role of kinesin-8 proteins in mitosis, we studied the effects of deletion of the fission yeast kinesin-8 proteins Klp5 and Klp6 on chromosome movements and spindle length dynamics. Aberrant microtubule-driven kinetochore pushing movements and tripolar mitotic spindles occurred in cells lacking Klp5 but not Klp6. Kinesin-8-deletion strains showed large fluctuations in metaphase spindle length, suggesting a disruption of spindle length stabilization. Comparison of our results from light microscopy with a mathematical model suggests that kinesin-8-induced effects on microtubule dynamics, kinetochore attachment stability, and sliding force in the spindle can explain the aberrant chromosome movements and spindle length fluctuations seen.","authors":"Gergely ZR, Crapo A, Hough LE, McIntosh JR, Betterton MD","authors_abbrev":"Gergely ZR et al.","pubmed_publication_date":"07 Nov 2016","pubmed_entrez_date":"2016-05-06","publication_year":"2016","canto_session_key":"ffbebba84aad52e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Meredith Betterton","canto_first_approved_date":"2018-03-26 13:52:06","canto_approved_date":"2024-05-16 13:16:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-05-18 17:25:30","canto_added_date":"2016-05-07 00:15:14","annotation_curators":[{"name":"Meredith Betterton","community_curator":true,"annotation_count":40,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.13","SPBC1685.15c","SPBC26H8.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-03-26"},{"uniquename":"PMID:22916195","title":"Identifying the hotspots on the top faces of WD40-repeat proteins from their primary sequences by β-bulges and DHSW tetrads.","citation":"PLoS One 2012;7(8):e43005","abstract":"The analysis of 36 available crystal structures of WD40 repeat proteins reveals widespread existence of a beta-bulge formed at the beginning of strand a and the end of strand b, termed as WD(b-a) bulge: among a total of 259 WD40 blades, there are 243 such β-bulges. The R(1) positions in these WD(b-a) bulges have fair distributions of Arg, His, Ile, Leu, Lys, Met, Phe, Trp, Tyr and Val residues. These residues protrude on the top face of the WD40 proteins and can serve as hotspots for protein-protein interactions. An analysis of 29 protein complexes formed by 17 WD proteins reveals that these R(1) residues, along with two other residues (R(1)-2 and D-1), are indeed widely involved in protein-protein interactions. Interestingly, these WD(b-a) bulges can be easily identified by the 4-amino acid sequences of (V, L, I), R(1), R(2), (V, L, I), along with some other significant amino acids. Thus, the hotspots of WD40 proteins on the top face can be readily predicted based on the primary sequences of the proteins. The literature-reported mutagenesis studies for Met30, MDV1, Tup11, COP1 and SPA1, which crystal structures are not available, can be readily understood based on the feature-based method. Applying the method, the twelve potential hotspots on the top face of Tup11 from S. japonicas have been identified. Our ITC measurements confirm seven of them, Tyr382, Arg284, Tyr426, Tyr508, Leu559, Lys575 and Ile601, are essential for recognizing Fep1. The ITC measurements further convinced that the feature-based method provides accurate prediction of hotspots on the top face.","doi":"10.1371/journal.pone.0043005","authors":"Wu XH, Wang Y, Zhuo Z, Jiang F, Wu YD","authors_abbrev":"Wu XH et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-24","publication_year":"2012","canto_triage_status":"Structure","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16135800","title":"The F-Box DNA helicase Fbh1 prevents Rhp51-dependent recombination without mediator proteins.","citation":"Mol Cell Biol 2005 Sep;25(18):8084-96","abstract":"A key step in homologous recombination is the loading of Rad51 onto single-stranded DNA to form a nucleoprotein filament that promotes homologous DNA pairing and strand exchange. Mediator proteins, such as Rad52 and Rad55-Rad57, are thought to aid filament assembly by overcoming an inhibitory effect of the single-stranded-DNA-binding protein replication protein A. Here we show that mediator proteins are also required to enable fission yeast Rad51 (called Rhp51) to function in the presence of the F-box DNA helicase Fbh1. In particular, we show that the critical function of Rad22 (an orthologue of Rad52) in promoting Rhp51-dependent recombination and DNA repair can be mostly circumvented by deleting fbh1. Similarly, the reduced growth/viability and DNA damage sensitivity of an fbh1(-) mutant are variously suppressed by deletion of any one of the mediators Rad22, Rhp55, and Swi5. From these data we propose that Rhp51 action is controlled through an interplay between Fbh1 and the mediator proteins. Colocalization of Fbh1 with Rhp51 damage-induced foci suggests that this interplay occurs at the sites of nucleoprotein filament assembly. Furthermore, analysis of different fbh1 mutant alleles suggests that both the F-box and helicase activities of Fbh1 contribute to controlling Rhp51.","authors":"Osman F, Dixon J, Barr AR, Whitby MC","authors_abbrev":"Osman F et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-09-02","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.01","SPAC3C7.03c","SPAC2G11.12","SPAC4H3.05","SPBC409.03","SPAC30D11.10","SPAC644.14c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:15277777","title":"Interaction between a negative regulator (Msa2/Nrd1) and a positive regulator (Cpc2) of sexual differentiation in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2004 Jul;68(7):1621-6","abstract":"The sexual differentiation of Schizosaccharomyces pombe is controlled by many cellular components which have not been fully characterized. We isolated a gene called msa2 as a multi-copy suppressor of a sporulation abnormal mutant (sam1). Msa2p is identical with Nrd1p which has been characterized as a factor that blocks the onset of sexual differentiation. The yeast two-hybrid system was used to identify Cpc2p, a fission yeast homolog of the RACK1 protein, that interacted with Msa2p/Nrd1p. We confirmed that Msa2p/Nrd1p interacted with Cpc2p in S. pombe cells. An epistatic analysis of msa2/nrd1 and cpc2 suggests that Msa2p/Nrd1p was an upstream regulator for Cpc2p. A localization analysis of Cpc2p and Msa2p/Nrd1p indicates that both proteins were predominantly localized in the cytoplasm. The interaction of negative regulator Msa2p/Nrd1p with positive regulator Cpc2p suggests a new regulatory circuit in the sexual differentiation of S. pombe.","authors":"Jeong HT, Oowatari Y, Abe M, Tanaka K, Matsuda H, Kawamukai M","authors_abbrev":"Jeong HT et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-07-28","publication_year":"2004","canto_session_key":"5e0bcd0a5a6d9347","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-08 16:11:32","canto_approved_date":"2025-12-14 13:56:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-20 17:21:46","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.11","SPBC14F5.05c","SPBC1D7.05","SPAC13G7.13c","SPAC6B12.15","SPAC17H9.09c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-12-08"},{"uniquename":"PMID:16091782","title":"Functional expression and cellular localization of the Na+/H+ exchanger Sod2 of the fission yeast Schizosaccharomyces pombe.","citation":"Can J Physiol Pharmacol 2005 Jul;83(7):565-72","abstract":"In the fission yeast Schizosaccharomyces pombe, the Na+/H+ exchanger, Sod2, plays a major role in the removal of excess intracellular sodium, and its disruption results in a sodium-sensitive phenotype. We examined the subcellular distribution and dynamics of Sod2 expression in S. pombe using a sod2-GFP fusion protein under the control of an attenuated version of the inducible nmt promoter. Sod2 was localized throughout the plasma membrane, the nuclear envelope, and some internal membrane systems. In exponentially growing cells, in which sod2-GFP was expressed and then the promoter turned-off, previously synthesized sod2-GFP was stable for long periods and found localized to the plasma membrane in the medial regions of the cell. It was not present at the actively growing cell ends. This suggests that these regions of the cell contain old plasma membrane protein vs. newly synthesized plasma membrane without Sod2 at the growing ends. Sod2 localization was not affected by salt stress. The results suggest that Sod2 is both a plasma membrane protein and is present in intracellular membranes. It is likely tethered within discrete regions of the plasma membrane and is not free to diffuse throughout the bilayer.","authors":"Fliegel L, Wiebe C, Chua G, Young PG","authors_abbrev":"Fliegel L et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-08-11","publication_year":"2005","canto_session_key":"26a69f3ec672072f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-11-30 14:38:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-30 14:38:13","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-30"},{"uniquename":"PMID:9794798","title":"Mutant DNA polymerase delta from thermosensitive Schizosaccharomyces pombe strains display reduced stimulation by proliferating cell nuclear antigen.","citation":"Biochem J 1998 Nov 01;335 ( Pt 3)(Pt 3):581-8","abstract":"We have isolated and characterized DNA polymerase delta (pol delta) from two thermosensitive Schizosaccharomyces pombe strains, poldeltats1 and poldeltats3, mutated in two different evolutionarily conserved domains of the catalytic subunit. At the restrictive temperature of 37 degreesC poldeltats1 and poldeltats3 mutant strains arrest growth in the S phase of the cell cycle. We show that at low levels of primer ends, in vitro stimulation by proliferating cell nuclear antigen (PCNA) of mutant enzymes is lower than stimulation of wild-type pol delta. Affinity for primer (3'-OH) ends and processivity of mutant enzymes do not appear different from wild-type pol delta. In contrast, Vmax values are lower than the wild-type value. The major in vitro defect appears to be decreased stimulation of mutant enzymes by PCNA, resulting in reduced velocity of DNA synthesis. In addition, ts1 pol delta is not stimulated by low PCNA concentration at 37 degreesC, although low concentrations stimulate activity at 25 degreesC, suggesting that this thermolability at low levels of primer ends could be its critical defect in vivo. Thus, both ts1 and ts3 pol delta mutations are located in regions of the catalytic subunit that seem necessary, directly or indirectly, for its efficient interaction with PCNA.","authors":"Perderiset M, Maga G, Piard K, Francesconi S, Tratner I, Hübscher U, Baldacci G","authors_abbrev":"Perderiset M et al.","pubmed_publication_date":"01 Nov 1998","pubmed_entrez_date":"1998-10-31","publication_year":"1998","canto_session_key":"7fc40d32cfb206ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-04-09 15:10:06","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-04-09 15:10:00","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.04","SPBC16D10.09"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-04-09"},{"uniquename":"PMID:2721492","title":"Pre-mRNA splicing mutants of Schizosaccharomyces pombe.","citation":"EMBO J 1989 Feb;8(2):551-9","abstract":"A collection of temperature sensitive (ts-) mutants was prepared by chemical mutagenesis of a wild type Schizosaccharomyces pombe strain. To screen the ts- mutants for pre-mRNA splicing defects, an oligodeoxynucleotide that recognizes one of the introns of the beta-tubulin pre-mRNA was used as a probe in a Northern blot assay to detect accumulation of intron sequences. This screening procedure identified three pre-mRNA splicing mutants from 100 ts- strains. The three mutants are defective in an early step of the pre-mRNA splicing reaction; none accumulate intermediates. The precursors that accumulate at 37 degrees C are polyadenylated. Analysis of the splicing of another pre-mRNA showed that the mutations are not specific for beta-tubulin. The total RNA pattern in the three splicing mutants appears to be normal. In addition, the amounts of the spliceosomal snRNAs are not drastically changed compared to the wild type and splicing of pre-tRNAs is not blocked. Genetic analyses demonstrate that all three splicing mutations are tightly linked to the ts- growth defects and are recessive. Crosses among the mutants place them in three complementation groups. The mutants have been named prp1, prp2 and prp3.","authors":"Potashkin J, Li R, Frendewey D","authors_abbrev":"Potashkin J et al.","pubmed_publication_date":"Feb 1989","pubmed_entrez_date":"1989-02-01","publication_year":"1989","canto_session_key":"4e3ceae954553607","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-02-26 08:44:45","canto_approved_date":"2023-01-26 11:12:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-20 07:21:42","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.07","SPBC146.07","SPAC29E6.02"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-02-26"},{"uniquename":"PMID:21304827","title":"Role of the Small GTPase Rho3 in Golgi/Endosome trafficking through functional interaction with adaptin in Fission Yeast.","citation":"PLoS One 2011 Feb 03;6(2):e16842","abstract":"We had previously identified the mutant allele of apm1(+) that encodes a homolog of the mammalian µ1A subunit of the clathrin-associated adaptor protein-1 (AP-1) complex, and we demonstrated the role of Apm1 in Golgi/endosome trafficking, secretion, and vacuole fusion in fission yeast.\nIn the present study, we isolated rho3(+), which encodes a Rho-family small GTPase, an important regulator of exocystosis, as a multicopy-suppressor of the temperature-sensitive growth of the apm1-1 mutant cells. Overexpression of Rho3 suppressed the Cl(-) sensitivity and immunosuppressant sensitivity of the apm1-1 mutant cells. Overexpression of Rho3 also suppressed the fragmentation of vacuoles, and the accumulation of v-SNARE Syb1 in Golgi/endosomes and partially suppressed the defective secretion associated with apm1-deletion cells. Notably, electron microscopic observation of the rho3-deletion cells revealed the accumulation of abnormal Golgi-like structures, vacuole fragmentation, and accumulation of secretory vesicles; these phenotypes were very similar to those of the apm1-deletion cells. Furthermore, the rho3-deletion cells and apm1-deletion cells showed very similar phenotypic characteristics, including the sensitivity to the immunosuppressant FK506, the cell wall-damaging agent micafungin, Cl(-), and valproic acid. Green fluorescent protein (GFP)-Rho3 was localized at Golgi/endosomes as well as the plasma membrane and division site. Finally, Rho3 was shown to form a complex with Apm1 as well as with other subunits of the clathrin-associated AP-1 complex in a GTP- and effector domain-dependent manner.\nTaken together, our findings reveal a novel role of Rho3 in the regulation of Golgi/endosome trafficking and suggest that clathrin-associated adaptor protein-1 and Rho3 co-ordinate in intracellular transport in fission yeast. To the best of our knowledge, this study provides the first evidence of a direct link between the small GTPase Rho and the clathrin-associated adaptor protein-1 in membrane trafficking.","doi":"10.1371/journal.pone.0016842","authors":"Kita A, Li C, Yu Y, Umeda N, Doi A, Yasuda M, Ishiwata S, Taga A, Horiuchi Y, Sugiura R","authors_abbrev":"Kita A et al.","pubmed_publication_date":"03 Feb 2011","pubmed_entrez_date":"2011-02-10","publication_year":"2011","canto_session_key":"798a8837242cfe26","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.08","SPBP16F5.07","SPCP1E11.06","SPAP27G11.06c","SPBC947.02"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"EMBL:AB011825","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20018856","title":"Involvement of the spliceosomal U4 small nuclear RNA in heterochromatic gene silencing at fission yeast centromeres.","citation":"J Biol Chem 2010 Feb 19;285(8):5630-8","abstract":"prp13-1 is one of the mutants isolated in a screen for defective pre-mRNA splicing at a nonpermissive temperature in fission yeast Schizosaccharomyces pombe. We cloned the prp13(+) gene and found that it encodes U4 small nuclear RNA (snRNA) involved in the assembly of the spliceosome. The prp13-1 mutant produced elongated cells, a phenotype similar to cell division cycle mutants, and displays a high incidence of lagging chromosomes on anaphase spindles. The mutant is hypersensitive to the microtubule-destabilizing drug thiabendazole, supporting that prp13-1 has a defect in chromosomal segregation. We found that the prp13-1 mutation resulted in expression of the ura4(+) gene inserted in the pericentromeric heterochromatin region and reduced recruitment of the heterochromatin protein Swi6p to that region, indicating defects in the formation of pericentromeric heterochromatin, which is essential for the segregation of chromosomes, in prp13-1. The formation of centromeric heterochromatin is induced by the RNA interference (RNAi) system in S. pombe. In prp13-1, the processing of centromeric noncoding RNAs to siRNAs, which direct the heterochromatin formation, was impaired and unprocessed noncoding RNAs were accumulated. These results suggest that U4 snRNA is required for the RNAi-directed heterochromatic gene silencing at the centromeres. In relation to the linkage between the spliceosomal U4 snRNA and the RNAi-directed formation of heterochromatin, we identified a mRNA-type intron in the centromeric noncoding RNAs. We propose a model in which the assembly of the spliceosome or a sub-spliceosome complex on the intron-containing centromeric noncoding RNAs facilitates the RNAi-directed formation of heterochromatin at centromeres, through interaction with the RNA-directed RNA polymerase complex.","doi":"10.1074/jbc.M109.074393","authors":"Chinen M, Morita M, Fukumura K, Tani T","authors_abbrev":"Chinen M et al.","pubmed_publication_date":"19 Feb 2010","pubmed_entrez_date":"2009-12-19","publication_year":"2010","canto_session_key":"e8547aef6b97c8ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-04-11 17:05:34","canto_approved_date":"2024-02-26 12:22:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-18 15:47:50","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPJ698.03c","SPAC29E6.08","SPSNRNA.04","SPCC1739.03","SPBC19C2.01","SPAC3A12.11c","SPBC146.07","SPCC188.13c","SPCC736.11","SPAC664.01c","SPBC11B10.09","SPBC119.13c","SPBC1711.17","SPAC607.03c","SPAC27F1.09c","SPCC777.14","SPBC16D10.07c"],"gene_count":17,"ltp_gene_count":12,"approved_date":"2017-04-11"},{"uniquename":"PMID:3475186","title":"A fission yeast chromosome can replicate autonomously in mouse cells.","citation":"Cell 1987 Jul 31;50(3):391-403","abstract":"To test the functional capacity of a fission yeast chromosome in mouse cells, a strain of the fission yeast Schizosaccharomyces pombe, ED628 Int5, was constructed. A plasmid bearing the SV2NEO gene, which can confer G418 resistance to mouse cells, was integrated at the ura4 locus on S. pombe chromosome III. S. pombe Int5 chromosomes were introduced into mouse C127 cells by PEG-facilitated protoplast fusion. Here we describe two independent G418-resistant cell lines with distinct growth characteristics, F1.1 and F7.1, and examine the structure of material derived from S. pombe Int5 chromosome III in these lines. F1.1 is shown to contain a single rearranged block of chromatin from S. pombe chromosome III integrated into a mouse chromosome, maintained in the absence of selection. In contrast, the data for F7.1 are consistent with the presence of linear, unintegrated copies of S. pombe chromosome III, which are apparently intact and maintained in an unstable but autonomous state. The unstable maintenance of this chromosome may be due to defective centromere function leading to missegregation at mitosis or to over- or underreplication.","authors":"Allshire RC, Cranston G, Gosden JR, Maule JC, Hastie ND, Fantes PA","authors_abbrev":"Allshire RC et al.","pubmed_publication_date":"31 Jul 1987","pubmed_entrez_date":"1987-07-31","publication_year":"1987","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12686557","title":"Nucleoside diphosphatase and glycosyltransferase activities can localize to different subcellular compartments in Schizosaccharomyces pombe.","citation":"J Biol Chem 2003 Jun 20;278(25):22379-87","abstract":"Nucleoside diphosphates generated by glycosyltransferases in the fungal, plant, and mammalian cell secretory pathways are converted into monophosphates to relieve inhibition of the transferring enzymes and provide substrates for antiport transport systems by which the entrance of nucleotide sugars from the cytosol into the secretory pathway lumen is coupled to the exit of nucleoside monophosphates. Analysis of the yeast Schizosaccharomyces pombe genome revealed that it encodes two enzymes with potential nucleoside diphosphatase activity, Spgda1p and Spynd1p. Characterization of the overexpressed enzymes showed that Spgda1p is a GDPase/UDPase, whereas Spynd1p is an apyrase because it hydrolyzed both nucleoside tri and diphosphates. Subcellular fractionation showed that both activities localize to the Golgi. Individual disruption of their encoding genes did not affect cell viability, but disruption of both genes was synthetically lethal. Disruption of Spgda1+ did not affect Golgi N- or O-glycosylation, whereas disruption of Spynd1+ affected Golgi N-mannosylation but not O-mannosylation. Although no nucleoside diphosphatase activity was detected in the endoplasmic reticulum (ER), N-glycosylation mediated by the UDP-Glc:glycoprotein glucosyltransferase (GT) was not severely impaired in mutants because first, no ER accumulation of misfolded glycoproteins occurred as revealed by the absence of induction of BiP mRNA, and second, in vivo GT-dependent glucosylation monitored by incorporation of labeled Glc into folding glycoproteins showed a partial (35-50%) decrease in Spgda1 but was not affected in Spynd1 mutants. Results show that, contrary to what has been assumed to date for eukaryotic cells, in S. pombe nucleoside diphosphatase and glycosyltransferase activities can localize to different subcellular compartments. It is tentatively suggested that ER-Golgi vesicle transport might be involved in nucleoside diphosphate hydrolysis.","authors":"D'Alessio C, Trombetta ES, Parodi AJ","authors_abbrev":"D'Alessio C et al.","pubmed_publication_date":"20 Jun 2003","pubmed_entrez_date":"2003-04-11","publication_year":"2003","canto_session_key":"197fff91f52f0f50","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-30 12:37:59","canto_approved_date":"2021-06-16 14:26:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-10-30 12:38:11","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.05c","SPAC824.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-10-30"},{"uniquename":"PMID:19714215","title":"The fission yeast homeodomain protein Yox1p binds to MBF and confines MBF-dependent cell-cycle transcription to G1-S via negative feedback.","citation":"PLoS Genet 2009 Aug;5(8):e1000626","abstract":"The regulation of the G1- to S-phase transition is critical for cell-cycle progression. This transition is driven by a transient transcriptional wave regulated by transcription factor complexes termed MBF/SBF in yeast and E2F-DP in mammals. Here we apply genomic, genetic, and biochemical approaches to show that the Yox1p homeodomain protein of fission yeast plays a critical role in confining MBF-dependent transcription to the G1/S transition of the cell cycle. The yox1 gene is an MBF target, and Yox1p accumulates and preferentially binds to MBF-regulated promoters, via the MBF components Res2p and Nrm1p, when they are transcriptionally repressed during the cell cycle. Deletion of yox1 results in constitutively high transcription of MBF target genes and loss of their cell cycle-regulated expression, similar to deletion of nrm1. Genome-wide location analyses of Yox1p and the MBF component Cdc10p reveal dozens of genes whose promoters are bound by both factors, including their own genes and histone genes. In addition, Cdc10p shows promiscuous binding to other sites, most notably close to replication origins. This study establishes Yox1p as a new regulatory MBF component in fission yeast, which is transcriptionally induced by MBF and in turn inhibits MBF-dependent transcription. Yox1p may function together with Nrm1p to confine MBF-dependent transcription to the G1/S transition of the cell cycle via negative feedback. Compared to the orthologous budding yeast Yox1p, which indirectly functions in a negative feedback loop for cell-cycle transcription, similarities but also notable differences in the wiring of the regulatory circuits are evident.","doi":"10.1371/journal.pgen.1000626","authors":"Aligianni S, Lackner DH, Klier S, Rustici G, Wilhelm BT, Marguerat S, Codlin S, Brazma A, de Bruin RA, Bähler J","authors_abbrev":"Aligianni S et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-08-29","publication_year":"2009","canto_session_key":"23c5a42491be246e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-07-23 14:12:15","canto_approved_date":"2024-10-11 11:47:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-23 12:35:58","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":94,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.14","SPCC63.14","SPAC22H10.12c","SPBC11B10.10c","SPCC63.12c","SPAC144.14","SPBC725.16","SPBC336.12c","SPAC3H5.06c","SPAC110.02","SPBC14C8.05c","SPBC660.12c","SPBC336.13c","SPBC14C8.11c","SPCC338.17c","SPCC553.07c","SPAC17H9.17c","SPBC3B9.01","SPCC550.13","SPAC1F7.06","SPCC1450.16c","SPCPB1C11.02","SPBC16A3.07c","SPBC887.14c","SPAC513.04","SPBC1306.01c","SPAC1F7.05","SPBC660.15","SPCC622.09","SPAC11E3.06","SPBC14C8.10","SPAC144.13c","SPBC25D12.04","SPNCRNA.93","SPAC644.15","SPAC644.05c","SPAC17H9.19c","SPBC14C8.06","SPBC32C12.03c","SPCC338.08","SPAPB8E5.05","SPAC513.02","SPAC17H9.20","SPBC428.18","SPAP14E8.02","SPBC1347.02","SPAC644.14c","SPAC1F7.01c","SPAP14E8.03","SPAPB2B4.03","SPBC21B10.13c","SPCC622.08c","SPCC1442.01","SPAC17H9.18c","SPBC14C8.12","SPAP8A3.03","SPCC338.18","SPBC428.17c","SPCC63.13","SPBC1347.01c","SPCC290.03c","SPBC14C8.09c","SPAC11E3.07","SPBC14C8.07c","SPCC70.09c","SPCC290.04","SPBC1306.02","SPAC110.04c","SPAC513.03","SPCC70.08c","SPBC1778.04","SPAC513.05","SPBC25D12.03c","SPAC1F7.04","SPBC660.13c","SPAC694.06c","SPBC119.04","SPCC70.10","SPBC336.14c","SPBC1778.03c"],"gene_count":80,"ltp_gene_count":4,"approved_date":"2024-07-23"},{"uniquename":"PMID:39561776","title":"DNA nicks in both leading and lagging strand templates can trigger break-induced replication.","citation":"Mol Cell 2024 Nov 13;","abstract":"Encounters between replication forks and unrepaired DNA single-strand breaks (SSBs) can generate both single-ended and double-ended double-strand breaks (seDSBs and deDSBs). seDSBs can be repaired by break-induced replication (BIR), which is a highly mutagenic pathway that is thought to be responsible for many of the mutations and genome rearrangements that drive cancer development. However, the frequency of BIR's deployment and its ability to be triggered by both leading and lagging template strand SSBs were unclear. Using site- and strand-specific SSBs generated by nicking enzymes, including CRISPR-Cas9 nickase (Cas9n), we demonstrate that leading and lagging template strand SSBs in fission yeast are typically converted into deDSBs that are repaired by homologous recombination. However, both types of SSBs can also trigger BIR, and the frequency of these events increases when fork convergence is delayed and the non-homologous end joining protein Ku70 is deleted.","doi":"10.1016/j.molcel.2024.10.026","authors":"Xu Y, Morrow CA, Laksir Y, Holt OM, Taylor K, Tsiappourdhi C, Collins P, Jia S, Andreadis C, Whitby MC","authors_abbrev":"Xu Y et al.","pubmed_publication_date":"13 Nov 2024","pubmed_entrez_date":"2024-11-19","publication_year":"2024","canto_session_key":"4e574bb17f51f7e5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-11-22 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7982990","title":"Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme fro Saccharomyces cerevisiae.","citation":"J Biol Chem 1994 Dec 02;269(48):30701-6","abstract":"The UDP-Glc:glycoprotein glucosyltransferase was purified to homogeneity from the fission yeast Schizosaccharomyces pombe. The enzyme has been recently suggested to be involved in the mechanism by which unfolded, partially folded, or misfolded glycoproteins are retained in the endoplasmic reticulum. The pure yeast glucosyltransferase formed protein-linked Glc1-Man9GlcNAc2,Glc1Man8GlcNAc2, and Glc1Man7GlcNAc2 when incubated with UDP-Glc and denatured thyroglobulin. The same compounds were formed upon glucosylation of endogenous acceptors by crude microsomes. The enzyme was a soluble microsomal protein that required Ca2+ for activity, used UDP-Glc and not TDP-Glc, ADP-Glc, or UDP-Gal as sugar donor, had an almost neutral optimum pH value, and as the glucosyl-transferase obtained from rat liver, glucosylated denatured but not native glycoproteins or glycopeptides. A similar enzymatic activity could not be detected in Saccharomyces cerevisiae microsomes and transient glucosylation of glycoproteins (addition of a single glucose unit to glucose-free oligosaccharides by the glucosyltransferase followed by its removal by glucosidase II) could not be detected in intact S. cerevisiae cells. These are the only eukaryotic cells described so far in which these processing reactions of the endoplasmic reticulum do not occur. Availability of the pure S. pombe enzyme will eventually allow testing the possible involvement of the glucosyltransferase in sensing glycoprotein tertiary structures in the endoplasmic reticulum.","authors":"Fernández FS, Trombetta SE, Hellman U, Parodi AJ","authors_abbrev":"Fernández FS et al.","pubmed_publication_date":"02 Dec 1994","pubmed_entrez_date":"1994-12-02","publication_year":"1994","canto_session_key":"d2ff25bcf8c9c2ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-05 17:01:12","canto_approved_date":"2025-02-06 16:39:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-20 10:01:53","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-05"},{"uniquename":"PMID:15829570","title":"Impairment of the TFIIH-associated CDK-activating kinase selectively affects cell cycle-regulated gene expression in fission yeast.","citation":"Mol Biol Cell 2005 Jun;16(6):2734-45","abstract":"The fission yeast Mcs6-Mcs2-Pmh1 complex, homologous to metazoan Cdk7-cyclin H-Mat1, has dual functions in cell division and transcription: as a partially redundant cyclin-dependent kinase (CDK)-activating kinase (CAK) that phosphorylates the major cell cycle CDK, Cdc2, on Thr-167; and as the RNA polymerase (Pol) II carboxyl-terminal domain (CTD) kinase associated with transcription factor (TF) IIH. We analyzed conditional mutants of mcs6 and pmh1, which activate Cdc2 normally but cannot complete cell division at restrictive temperature and arrest with decreased CTD phosphorylation. Transcriptional profiling by microarray hybridization revealed only modest effects on global gene expression: a one-third reduction in a severe mcs6 mutant after prolonged incubation at 36 degrees C. In contrast, a small subset of transcripts ( approximately 5%) decreased by more than twofold after Mcs6 complex function was compromised. The signature of repressed genes overlapped significantly with those of cell separation mutants sep10 and sep15. Sep10, a component of the Pol II Mediator complex, becomes essential in mcs6 or pmh1 mutant backgrounds. Moreover, transcripts dependent on the forkhead transcription factor Sep1, which are expressed coordinately during mitosis, were repressed in Mcs6 complex mutants, and Mcs6 also interacts genetically with Sep1. Thus, the Mcs6 complex, a direct activator of Cdc2, also influences the cell cycle transcriptional program, possibly through its TFIIH-associated kinase function.","authors":"Lee KM, Miklos I, Du H, Watt S, Szilagyi Z, Saiz JE, Madabhushi R, Penkett CJ, Sipiczki M, Bähler J, Fisher RP","authors_abbrev":"Lee KM et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-04-15","publication_year":"2005","canto_session_key":"cf04c2f09512f3dd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-04 15:31:21","canto_approved_date":"2020-07-31 15:51:22","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-05-30 22:47:28","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4C3.12","SPBC19F8.07","SPBC21.04","SPCP31B10.03c","SPAC25G10.03","SPBP16F5.02","SPAC1D4.06c","SPBC11B10.09","SPBC28F2.12","SPBC776.18c"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2018-10-04"},{"uniquename":"PMID:18951798","title":"Mechanisms for maintaining microtubule bundles.","citation":"Trends Cell Biol 2008 Dec;18(12):580-6","abstract":"The dynamics of microtubules (MTs) are crucial to many of their functions. Certain MT structures, such as the mitotic spindle apparatus, exhibit high MT turnover yet maintain their mass stably through long periods of time. Here, we highlight what are emerging as two important mechanisms for maintaining MT bundles: the first, MT nucleation from pre-existing MTs by means of gamma-tubulin-containing complexes; and the second, MT 'rescue' by the stabilizing protein CLASP. As examples, we describe recent advances in understanding the assembly and maintenance of simple MT bundles in fission yeast and plant cells, which have implications for the bundles of the animal mitotic spindle.","doi":"10.1016/j.tcb.2008.09.004","authors":"Bratman SV, Chang F","authors_abbrev":"Bratman SV et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-10-28","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39527207","title":"Dissecting the Cell-Killing Mechanisms of Hydroxyurea Using Spot Assays.","citation":"Methods Mol Biol 2025;2862:267-276","abstract":"Hydroxyurea is an inhibitor of ribonucleotide reductase and is commonly used in laboratories to induce replication stress or arrest cells in the S phase for cell cycle or checkpoint studies. However, hydroxyurea also causes side effects such as oxidative stress, particularly under chronic exposure conditions. This complicates the interpretation of the cell-killing mechanisms, particularly in a previously uncharacterized mutant, and thus hampers the analyses. Here, we describe a few easy and simple spot assays in fission yeast that allow dissecting the cell-killing mechanisms of hydroxyurea.","doi":"10.1007/978-1-0716-4168-2_19","authors":"Dev K, Yurtsever I, Bhadra S, Guduri YA, Davi K, Xu YJ","authors_abbrev":"Dev K et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10198054","title":"Uridine diphosphate-glucose transport into the endoplasmic reticulum of Saccharomyces cerevisiae: in vivo and in vitro evidence.","citation":"Mol Biol Cell 1999 Apr;10(4):1019-30","abstract":"It has been proposed that synthesis of beta-1,6-glucan, one of Saccharomyces cerevisiae cell wall components, is initiated by a uridine diphosphate (UDP)-glucose-dependent reaction in the lumen of the endoplasmic reticulum (ER). Because this sugar nucleotide is not synthesized in the lumen of the ER, we have examined whether or not UDP-glucose can be transported across the ER membrane. We have detected transport of this sugar nucleotide into the ER in vivo and into ER-containing microsomes in vitro. Experiments with ER-containing microsomes showed that transport of UDP-glucose was temperature dependent and saturable with an apparent Km of 46 microM and a Vmax of 200 pmol/mg protein/3 min. Transport was substrate specific because UDP-N-acetylglucosamine did not enter these vesicles. Demonstration of UDP-glucose transport into the ER lumen in vivo was accomplished by functional expression of Schizosaccharomyces pombe UDP-glucose:glycoprotein glucosyltransferase (GT) in S. cerevisiae, which is devoid of this activity. Monoglucosylated protein-linked oligosaccharides were detected in alg6 or alg5 mutant cells, which transfer Man9GlcNAc2 to protein; glucosylation was dependent on the inhibition of glucosidase II or the disruption of the gene encoding this enzyme. Although S. cerevisiae lacks GT, it contains Kre5p, a protein with significant homology and the same size and subcellular location as GT. Deletion mutants, kre5Delta, lack cell wall beta-1,6 glucan and grow very slowly. Expression of S. pombe GT in kre5Delta mutants did not complement the slow-growth phenotype, indicating that both proteins have different functions in spite of their similarities.","authors":"Castro O, Chen LY, Parodi AJ, Abeijón C","authors_abbrev":"Castro O et al.","pubmed_publication_date":"Apr 1999","pubmed_entrez_date":"1999-04-10","publication_year":"1999","canto_session_key":"71ed6231aaaf81c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-05-23 07:02:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-22 13:45:50","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-22"},{"uniquename":"PMID:1839480","title":"A genomic sequence of the Schizosaccharomyces pombe 16 kDa vacuolar H(+)-ATPase.","citation":"Yeast 1991 Dec;7(9):989-91","abstract":"We have isolated the gene encoding the 16 kDa vacuolar H(+)-ATPase from Schizosaccharomyces pombe. On the basis of RNA splicing signals and amino acid sequence homology with other 16 kDa H(+)-ATPases, the genomic DNA sequence indicated the 16 kDa protein is encoded by five exons. The C-terminal 50 amino acids has more than 90% homology with vacuolar H(+)-ATPases of mammalian cells.","authors":"Toyama R, Goldstein DJ, Schlegel R, Dhar R","authors_abbrev":"Toyama R et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"b25d7ff674217d97","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 21:55:56","canto_approved_date":"2018-12-22 21:55:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 21:55:48","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:1656390","title":"O-ribosyl-phosphate purine as a constant modified nucleotide located at position 64 in cytoplasmic initiator tRNAs(Met) of yeasts.","citation":"Nucleic Acids Res 1991 Oct 11;19(19):5199-203","abstract":"The unknown modified nucleotide G*, isolated from both Schizosaccharomyces pombe and Torulopsis utilis initiator tRNAs(Met), has been identified as an O-ribosyl-(1\"----2')-guanosine-5\"-phosphate, called Gr(p), by means of HPLC, UV-absorption, mass spectrometry and periodate oxidation procedures. By comparison with the previously published structure of Ar(p) isolated from Saccharomyces cerevisiae initiator tRNA(Met), the (1\"----2')-glycosidic bond in Gr(p) has been postulated to have a beta-spatial conformation. The modified nucleotide Gr(p) is located at position 64 in the tRNA(Met) molecules, i.e. at the same position as Ar(p). Since we have also characterized Gr(p) in Candida albicans initiator tRNA(Met), the phosphoribosylation of purine 64 can be considered as a constant nucleotide modification in the cytoplasmic initiator tRNAs(Met) of all yeast species so far sequenced. Precise evidence for the presence of Gr(p) in initiator tRNAs(Met) of several plants is also reported.","authors":"Glasser AL, Desgres J, Heitzler J, Gehrke CW, Keith G","authors_abbrev":"Glasser AL et al.","pubmed_publication_date":"11 Oct 1991","pubmed_entrez_date":"1991-10-11","publication_year":"1991","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22095476","title":"Genes involved in glucose repression and oxidative stress response in the fission yeast Schizosaccharomyces pombe.","citation":"Genet Mol Res 2011 Nov 08;10(4):4041-7","abstract":"We looked for changes in gene expression and novel genes that could be involved in the interaction between glucose repression and oxidative stress response in the fission yeast, Schizosaccharomyces pombe, using a constitutive invertase mutant, ird11, which is resistant to glucose. BLAST analysis was made of the S. pombe genome database of cDNAs whose expression ratios differentially decreased or increased upon exposure to mild oxidative stress in this mutant compared to the wild type. Genes with this type of activity were identified as rpl302, encoding 60S ribosomal protein L3, and mpg1, encoding mannose-1-phosphate guanyltransferase; their expression patterns were measured using quantitative real-time PCR. We found that the expression levels of rpl302 and mpg1 genes in ird11 under unstressed conditions were increased compared to those of the wild type. Under stress conditions, the expression levels of the rpl302 gene were decreased in both strains, while mpg1 expression levels remained unchanged. These results suggest that these genes play a role in the response to oxidative stress in this mutant strain.","doi":"10.4238/2011.November.8.4","authors":"Suslu KG, Palabiyik B, Temizkan G","authors_abbrev":"Suslu KG et al.","pubmed_publication_date":"08 Nov 2011","pubmed_entrez_date":"2011-11-19","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9628362","title":"Substitution of the conserved phenylalanine in the S-adenosyl-L-methionine binding site of M.MspI with tyrosine modifies the kinetic properties of the enzyme.","citation":"Biol Chem 1998;379(4-5):591-4","abstract":"Cytosine (C-5)-specific DNA methyltransferases share a set of ten conserved motifs distributed evenly throughout the entire polypeptide chain. The first conserved motif contains a Phe, which is intimately associated with cofactor recognition. In the pseudo-DNA methyltransferase M.SpoI, encoded by the pmt1 gene in Schizosaccharomyces pombe, a Tyr replaces this Phe residue. We describe the properties of a mutant form of M.MspI, a typical cytosine (C-5)-specific DNA methyltransferase, in which Tyr replaces the conserved Phe. This mutant shows differences in ternary complex formation and in the pattern of covalent complex formation with an inhibitory, fluorinated DNA duplex which may be due to anomalous hydrogen bonding between the mutant Tyr hydroxyl group and the catalytic loop of the enzyme or through interference with cofactor binding.","authors":"Pinarbasi E, Kan MS, Duran C, Ford GC, Hornby DP","authors_abbrev":"Pinarbasi E et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-06-17","publication_year":"1998","canto_session_key":"60d3bea438a05331","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-01-24 18:02:10","canto_approved_date":"2021-01-24 18:02:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-24 18:02:04","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.02"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2021-01-24"},{"uniquename":"PMID:9790601","title":"A phosphorylation site mutant of Schizosaccharomyces pombe cdc2p fails to promote the metaphase to anaphase transition.","citation":"Mol Gen Genet 1998 Sep;259(4):437-48","abstract":"The protein kinase cdc2p is a key regulator of the G1-S and G2-M cell cycle transitions in the yeast Schizosaccharomyces pombe. Activation of cdc2p is regulated by its phosphorylation state and by interaction with other proteins. We have analyzed the consequences for cell cycle progression of altering the conserved threonine phosphorylation site, within the activation loop of cdc2p, to glutamic acid. This mutant, T167 E, promotes entry into mitosis, as judged by the accumulation of mitotic spindles and condensed chromosomes, despite the fact that it lacks demonstrable kinase activity both in vitro and in vivo. However, T167 E cannot promote the metaphase-anaphase transition. Since a component of the anaphase-promoting complex (APC) in S. pombe, cut9p, remains hypophosphorylated at the T167 E arrest point, the cell cycle block might be due to the inability of T167 E to activate the APC. T167 E is lethal when overexpressed, and overproduction also causes a mitotic arrest. Multicopy suppressors of the dominant negative phenotype were isolated, and identified as cdc13+ and suc1+. Overexpression of suc1+ suppresses the effects of T167 E overproduction by restoring sufficient amounts of suc1p to the cell to allow passage through mitosis.","authors":"Gould KL, Feoktistova A, Fleig U","authors_abbrev":"Gould KL et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-10-28","publication_year":"1998","canto_session_key":"7940bef1ad8a05ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-03-06 11:59:16","canto_approved_date":"2022-07-28 11:39:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-08 16:40:56","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.15c","SPBC582.03","SPBC11B10.09","SPBC1734.14c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-03-06"},{"uniquename":"PMID:8665408","title":"Mutational analysis of U1 function in Schizosaccharomyces pombe: pre-mRNAs differ in the extent and nature of their requirements for this snRNA in vivo.","citation":"RNA 1996 May;2(5):404-18","abstract":"The U1 snRNP is known to play a critical role in spliceosome assembly, at least in part through base pairing of its RNA moiety to the substrate, but many details remain to be elucidated. To further dissect U1 snRNA function, we have analyzed 14 single point mutations in the six nucleotides complementary to the 5' splice site for their effects on growth and splicing in the fission yeast Schizosaccharomyces pombe. Three of the four alleles previously found to support growth of Saccharomyces cerevisiae are lethal in S. pombe, implying a more critical role for the 5' end of U1 in fission yeast. Furthermore, a comparison of phenotypes for individual nucleotide substitutions suggests that the two yeasts use different strategies to modulate the extent of pairing between U1 and the 5' splice site. The importance of U1 function in S. pombe is further underscored by the lethality of several single point mutants not examined previously in S. cerevisiae. In total, only three alleles complement the U1 gene disruption, and these strains are temperature-sensitive for growth. Each viable mutant was tested for impaired splicing of three different S. pombe introns. Among these, only the second intron of the cdc2 gene (cdc2-I2) showed dramatic accumulation of linear precursor. Notably, cdc2-I2 is spliced inefficiently even in cells containing wild-type U1, at least in part due to the presence of a stable hairpin encompassing its 5' splice site. Although point mutations at the 5' end of U1 have no discernible effect on splicing of pre-U6, significant accumulation of unspliced RNA is observed in a metabolic depletion experiment. Taken together, these observations indicate that the repertoire of U1 activities is used to varying extents for splicing of different pre-mRNAs in fission yeast.","authors":"Alvarez CJ, Romfo CM, Vanhoy RW, Porter GL, Wise JA","authors_abbrev":"Alvarez CJ et al.","pubmed_publication_date":"May 1996","pubmed_entrez_date":"1996-05-01","publication_year":"1996","canto_session_key":"59504af0998e9fd3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-24 16:04:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-24 16:04:38","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_8665408_phaf.tsv"}],"genes":["SPBC26H8.07c","SPBC11B10.09","SPSNRNA.06","SPSNRNA.01"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2014-06-24"},{"uniquename":"EMBL:AU009688","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8188765","title":"Cisplatin sensitivity correlates with its ability to cause cell cycle arrest via a wee1 kinase-dependent pathway in Schizosaccharomyces pombe.","citation":"J Cell Physiol 1994 Jun;159(3):506-14","abstract":"Mutants of Schizosaccharomyces pombe were used to define genes involved in the cell cycle arrest produced by cisplatin (DDP), an agent that causes both DNA damage and inhibition of DNA synthesis. Previous work has demonstrated that strains with defective or absent wee1+ function fail to arrest in G2 when DNA is damaged, but do arrest when DNA synthesis is inhibited (Rowley et al., 1992a, Nature, 356:353-355). Strains defective in wee1+ function, or in the ability of the wee1+ kinase to regulate cdc2, failed to arrest following DDP exposure, as did a rad1-1 mutant. All strains failing to arrest in G2 were hypersensitive to DDP. Thus, DNA damage rather than inhibition of DNA synthesis is causative of DDP-induced cell cycle arrest. In addition, this work shows that the wee1+ and rad1+ gene products are required for successful DDP-induced arrest, and suggests that the ability of S. pombe to arrest is a major determinant of sensitivity to DDP.","authors":"Thiebaut F, Enns R, Howell SB","authors_abbrev":"Thiebaut F et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42109131","title":"Differential gene expression drives cell-cycle-dependent transition from monopolar to bipolar growth in Schizosaccharomyces pombe.","citation":"G3 (Bethesda) 2026 May 11;","abstract":"Cell polarity is important for maintaining cell structure and function. In S. pombe, after division, cells grow monopolarly from the old end, then transition to bipolar growth at a certain size when the new end activates. However, G1-arrested cells do not become bipolar despite continued growth, suggesting a role for the cell cycle in this process. To identify how the cell cycle impacts monopolar to bipolar transition, we performed high-throughput mRNA sequencing to detect differentially expressed genes in G1-arrested and G2-phase cells of the cell-cycle mutant cdc10-129. DESeq2 analysis identified 65 unique genes upregulated in G1 phase and 35 in G2 phase. Enrichment analysis shows that G1 phase cells upregulated the MAPK pheromone-response pathway, protein folding, rRNA processing, and heat-shock protein binding. G2 phase cells showed upregulation of plasma membrane maintenance and cell wall organization. In G2 phase cells, protein-protein interaction networks identified the cdc15-hob3-rho1-bgs1 hub, known to promote bipolar growth and regulate cell wall biogenesis. In G1 phase cells, the spk1-byr2-ste11 hub involved in pheromone-response and nutritional stress-dependent G1-arrest was identified. In agreement with these findings, we find that spk1Δ cells are precociously bipolar, indicating a role for this kinase in preventing bipolar growth. We hypothesize that bipolar growth in G2 cells requires a combination of factors that favor cell growth. In G2, stress response pathways are downregulated while anabolic pathways are upregulated enabling transition from monopolar to bipolar growth.","doi":"10.1093/g3journal/jkag126","authors":"Pathak S, Tramonte LM, Das M","authors_abbrev":"Pathak S et al.","pubmed_publication_date":"11 May 2026","pubmed_entrez_date":"2026-05-11","publication_year":"2026","canto_session_key":"942e2117c26f5612","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-05-11 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2034212","title":"The POL1 gene from the fission yeast, Schizosaccharomyces pombe, shows conserved amino acid blocks specific for eukaryotic DNA polymerases alpha.","citation":"Mol Gen Genet 1991 Apr;226(1-2):182-9","abstract":"The POL1 gene of the fission yeast, Schizosaccharomyces pombe, was isolated using a POL1 gene probe from the budding yeast Saccharomyces cerevisiae, cloned and sequenced. This gene is unique and located on chromosome II. It includes a single 91 bp intron and is transcribed into a mRNA of about 4500 nucleotides. The predicted protein coded for by the S. pombe POL1 gene is 1405 amino acid long and its calculated molecular weight is about 160,000 daltons. This peptide contains seven amino acid blocks conserved among several DNA polymerases from different organisms and shares overall 37% and 34% identity with DNA polymerases alpha from S. cerevisiae and human cells, respectively. These results indicate that this gene codes for the S. pombe catalytic subunit of DNA polymerase alpha. The comparisons with human DNA polymerase alpha and with the budding yeast DNA polymerases alpha, delta and epsilon reveal conserved blocks of amino acids which are structurally and/or functionally specific only for eukaryotic alpha-type DNA polymerases.","authors":"Damagnez V, Tillit J, de Recondo AM, Baldacci G","authors_abbrev":"Damagnez V et al.","pubmed_publication_date":"Apr 1991","pubmed_entrez_date":"1991-04-01","publication_year":"1991","canto_session_key":"702ccdb8869dcffc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-02 13:45:47","canto_approved_date":"2019-01-02 13:45:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 22:12:20","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-02"},{"uniquename":"PMID:24362309","title":"A genetic screen for functional partners of condensin in fission yeast.","citation":"G3 (Bethesda) 2014 Feb 19;4(2):373-81","abstract":"Mitotic chromosome condensation is a prerequisite for the accurate segregation of chromosomes during cell division, and the conserved condensin complex a central player of this process. However, how condensin binds chromatin and shapes mitotic chromosomes remain poorly understood. Recent genome-wide binding studies showing that in most species condensin is enriched near highly expressed genes suggest a conserved link between condensin occupancy and high transcription rates. To gain insight into the mechanisms of condensin binding and mitotic chromosome condensation, we searched for factors that collaborate with condensin through a synthetic lethal genetic screen in the fission yeast Schizosaccharomyces pombe. We isolated novel mutations affecting condensin, as well as mutations in four genes not previously implicated in mitotic chromosome condensation in fission yeast. These mutations cause chromosome segregation defects similar to those provoked by defects in condensation. We also identified a suppressor of the cut3-477 condensin mutation, which largely rescued chromosome segregation during anaphase. Remarkably, of the five genes identified in this study, four encode transcription co-factors. Our results therefore provide strong additional evidence for a functional connection between chromosome condensation and transcription.","doi":"10.1534/g3.113.009621","authors":"Robellet X, Fauque L, Legros P, Mollereau E, Janczarski S, Parrinello H, Desvignes JP, Thevenin M, Bernard P","authors_abbrev":"Robellet X et al.","pubmed_publication_date":"19 Feb 2014","pubmed_entrez_date":"2013-12-24","publication_year":"2014","canto_session_key":"4892604421dd765f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-24 11:04:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-24 11:03:31","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_24362309_phaf.tsv"}],"genes":["SPAC1250.01","SPBC146.03c","SPBP4H10.06c","SPBC776.13","SPAC17A5.07c","SPAC1071.06","SPAC2F7.07c","SPBC31F10.09c","SPCC306.03c","SPBC1A4.03c","SPCC320.13c","SPCC188.03"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2014-07-24"},{"uniquename":"PMID:11069763","title":"Live analysis of lagging chromosomes during anaphase and their effect on spindle elongation rate in fission yeast.","citation":"J Cell Sci 2000 Dec;113 Pt 23:4177-91","abstract":"The fission yeast Schizosaccharomyces pombe is widely used as a model system for studies of the cell cycle and chromosome biology. To enhance these studies we have fused GFP to the chromodomain protein Swi6p, thus allowing nuclear and chromosome behaviour to be followed in living cells using time-lapse fluorescence microscopy. Like endogenous Swi6p, GFP-Swi6p localises to the nucleus and is concentrated at the heterochromatic centromeres and telomeres. The nucleus is highly dynamic during interphase: the clustered centromeres, in particular, are highly mobile. By expressing GFP-(&agr;)2-tubulin and GFP-Swi6p in the same cells we observe that the clustered centromeres move in concert with the cytoplasmic microtubules, which is likely to reflect their association with the spindle pole body. Drug treatment indicates that this movement is dependent on intact cytoplasmic microtubules. We have also used GFP-Swi6p to investigate the properties of lagging chromosomes observed in mutants with defects in chromosome segregation. Lagging chromosomes display a variety of behaviours on anaphase spindles, most surprisingly, chromosomes appear to initiate microtubule interactions and move to the poles late in anaphase B. Interestingly, in cells displaying lagging chromosomes, the rate of spindle elongation is slowed by a factor of two. This suggests that cells are able to sense the presence of a lagging chromosome and slow anaphase B in order to allow it extra time to reach the pole. However, this mechanism is not dependent on the spindle checkpoint proteins Bub1p or Dma1p, raising the possibility that a novel checkpoint mechanism operates to retard spindle elongation if lagging chromosomes are detected. An alternative model is also discussed in which single defective kinetochores on lagging chromatids are able to interact simultaneously with microtubules emanating from both poles and affect spindle dynamics by counteracting the spindle elongation force.","authors":"Pidoux AL, Uzawa S, Perry PE, Cande WZ, Allshire RC","authors_abbrev":"Pidoux AL et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-09","publication_year":"2000","canto_session_key":"8674f369a10290b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-13 11:59:09","canto_approved_date":"2024-03-13 09:34:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-11 09:53:18","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPAC17G8.10c","SPCC663.12","SPAC18G6.02c","SPAC664.01c","SPCC1322.12c","SPCC11E10.08"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-11-13"},{"uniquename":"PMID:30072377","title":"Uncovering Natural Longevity Alleles from Intercrossed Pools of Aging Fission Yeast Cells.","citation":"Genetics 2018 Oct;210(2):733-744","abstract":"Quantitative traits often show large variation caused by multiple genetic factors . One such trait is the chronological lifespan of non-dividing yeast cells, serving as a model for cellular aging. Screens for genetic factors involved in aging typically assay mutants of protein-coding genes. To identify natural genetic variants contributing to cellular aging, we exploited two strains of the fission yeast,  Schizosaccharomyces pombe , that differ in chronological lifespan. We generated segregant pools from these strains and subjected them to advanced intercrossing over multiple generations to break up linkage groups. We chronologically aged the intercrossed segregant pool, followed by genome sequencing at different times to detect genetic variants that became reproducibly enriched as a function of age. A region on Chromosome II showed strong positive selection during aging. Based on expected functions, two candidate variants from this region in the long-lived strain were most promising to be causal: small insertions and deletions in the 5'-untranslated regions of  ppk31  and  SPBC409.08  Ppk31 is an ortholog of Rim15, a conserved kinase controlling cell proliferation in response to nutrients, while SPBC409.08 is a predicted spermine transmembrane transporter. Both Rim15 and the spermine-precursor, spermidine, are implicated in aging as they are involved in autophagy-dependent lifespan extension. Single and double allele replacement suggests that both variants, alone or combined, have subtle effects on cellular longevity. Furthermore, deletion mutants of both  ppk31  and  SPBC409.08  rescued growth defects caused by spermidine. We propose that Ppk31 and SPBC409.08 may function together to modulate lifespan, thus linking Rim15/Ppk31 with spermidine metabolism.","doi":"10.1534/genetics.118.301262","authors":"Ellis DA, Mustonen V, Rodríguez-López M, Rallis C, Malecki M, Jeffares DC, Bähler J","authors_abbrev":"Ellis DA et al.","pubmed_publication_date":"Oct 2018","pubmed_entrez_date":"2018-08-04","publication_year":"2018","canto_session_key":"b792e3d40839cdbd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jurg Bahler","canto_first_approved_date":"2019-01-11 13:12:04","canto_approved_date":"2024-04-05 07:13:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-11-28 17:50:35","canto_added_date":"2018-08-05 00:15:04","annotation_curators":[{"name":"Jurg Bahler","community_curator":true,"annotation_count":5,"orcid":"0000-0003-4036-1532","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.08","SPBC725.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-01-11"},{"uniquename":"PMID:15040950","title":"On the role of Trk1 and Trk2 in Schizosaccharomyces pombe under different ion stress conditions.","citation":"FEMS Yeast Res 2004 Mar;4(6):619-24","abstract":"Trk1 and Trk2 are the major K(+) transport systems in Schizosaccharomyces pombe. Both transporters individually seem to be able to cope with K(+) requirements of the cells under normal conditions, since only the double mutant shows defective K(+) transport and defective growth at limiting K(+) concentrations. We have studied in detail the role of SpTrk1 and SpTrk2 under different ion stress conditions. Results show that the strain with only Trk1 (trk1(+)) is less sensitive to Li(+) and to hygromycin B, it grows better at low K(+) and it survives longer in a medium without K(+) than the strain expressing only Trk2 (trk2(+)). We conclude that Trk1 contributes more efficiently than Trk2 to the performance of the fission yeast under ion stress conditions. In the wild type both trk1(+) and trk2(+) genes are expressed and probably collaborate for the performance of the cells.","authors":"Calero F, Montiel V, Caracuel Z, Cabello-Hurtado F, Ramos J","authors_abbrev":"Calero F et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-03-26","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17189857","title":"Mapping yeast origins of replication via single-stranded DNA detection.","citation":"Methods 2007 Feb;41(2):151-7","abstract":"Studies in th Saccharomyces cerevisiae have provided a framework for understanding how eukaryotic cells replicate their chromosomal DNA to ensure faithful transmission of genetic information to their daughter cells. In particular, S. cerevisiae is the first eukaryote to have its origins of replication mapped on a genomic scale, by three independent groups using three different microarray-based approaches. Here we describe a new technique of origin mapping via detection of single-stranded DNA in yeast. This method not only identified the majority of previously discovered origins, but also detected new ones. We have also shown that this technique can identify origins in Schizosaccharomyces pombe, illustrating the utility of this method for origin mapping in other eukaryotes.","authors":"Feng W, Raghuraman MK, Brewer BJ","authors_abbrev":"Feng W et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2006-12-27","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006978","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16317005","title":"The Schizosaccharomyces pombe replication inhibitor Spd1 regulates ribonucleotide reductase activity and dNTPs by binding to the large Cdc22 subunit.","citation":"J Biol Chem 2006 Jan 20;281(3):1778-83","abstract":"Ribonucleotide reductase (RNR) is an essential enzyme that provides the cell with a balanced supply of deoxyribonucleoside triphosphates for DNA replication and repair. Mutations that affect the regulation of RNR in yeast and mammalian cells can lead to genetic abnormalities and cell death. We have expressed and purified the components of the RNR system in fission yeast, the large subunit Cdc22p, the small subunit Suc22p, and the replication inhibitor Spd1p. It was proposed (Liu, C., Powell, K. A., Mundt, K., Wu, L., Carr, A. M., and Caspari, T. (2003) Genes Dev. 17, 1130-1140) that Spd1 is an RNR inhibitor, acting by anchoring the Suc22p inside the nucleus during G1 phase. Using in vitro assays with highly purified proteins we have demonstrated that Spd1 indeed is a very efficient inhibitor of fission yeast RNR, but acting on Cdc22p. Furthermore, biosensor technique showed that Spd1p binds to the Cdc22p with a KD of 2.4 microM, whereas the affinity to Suc22p is negligible. Therefore, Spd1p inhibits fission yeast RNR activity by interacting with the Cdc22p. Similar to the situation in budding yeast, logarithmically growing fission yeast increases the dNTP pools 2-fold after 3 h of incubation in the UV mimetic 4-nitroquinoline-N-oxide. This increase is smaller than the increase observed in budding yeast but of the same order as the dNTP pool increase when synchronous Schizosaccharomyces pombe cdc10 cells are going from G1 to S-phase.","authors":"Håkansson P, Dahl L, Chilkova O, Domkin V, Thelander L","authors_abbrev":"Håkansson P et al.","pubmed_publication_date":"20 Jan 2006","pubmed_entrez_date":"2005-12-01","publication_year":"2006","canto_session_key":"dfd6ea81df55ce19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-06 19:23:13","canto_approved_date":"2022-05-18 12:51:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-17 09:51:02","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPBC25D12.04","SPAC29B12.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-09-06"},{"uniquename":"PMID:20705239","title":"The methyltransferase activity of Clr4Suv39h triggers RNAi independently of histone H3K9 methylation.","citation":"Mol Cell 2010 Aug 13;39(3):360-72","abstract":"In fission yeast, the pericentromeric dg and dh repeats are transcribed and give rise to small interfering RNAs (siRNAs) by a mechanism that depends on the Clr4(suv39h) histone H3 lysine 9 (H3K9) methyltransferase. Here, we show that Clr4 activity promotes the assembly of a tripartite complex composed of the Clr4-containing CLRC complex and complexes involved in siRNA generation. However, unlike dh siRNAs, dg siRNAs accumulate to near wild-type levels in cells with H3K9 substitutions that cannot be methylated. Thus, Clr4 activity controls siRNA amplification from the different repeat regions by different mechanisms, H3K9 methylation dependent versus independent. Furthermore, artificial tethering of Rik1, a core subunit of the CLRC complex, to a euchromatic RNA mediates RNAi-dependent silencing that partially bypasses the requirement for other CLRC subunits. These findings establish Rik1 as a key link between CLRC and RNAi and reveal distinct centromeric siRNA amplification mechanisms that depend on the Clr4 methyltransferase activity.","doi":"10.1016/j.molcel.2010.07.017","authors":"Gerace EL, Halic M, Moazed D","authors_abbrev":"Gerace EL et al.","pubmed_publication_date":"13 Aug 2010","pubmed_entrez_date":"2010-08-14","publication_year":"2010","canto_session_key":"f0d3958e5f19567e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F12.09","SPAC18G6.02c","SPCC736.11","SPCC1739.03","SPBC83.03c","SPCC188.13c","SPAC1834.04","SPCC11E10.08","SPBC8D2.04","SPCC663.12","SPBC428.08c"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:24958269","title":"Metabolomic analysis of fission yeast at the onset of nitrogen starvation.","citation":"Metabolites 2013 Dec 13;3(4):1118-29","abstract":"Microorganisms naturally respond to changes in nutritional conditions by adjusting their morphology and physiology. The cellular response of the fission yeast S. pombe to nitrogen starvation has been extensively studied. Here, we report time course metabolomic analysis during one hour immediately after nitrogen starvation, prior to any visible changes in cell morphology except for a tiny increase of cell length per division cycle. We semi-quantitatively measured 75 distinct metabolites, 60% of which changed their level over 2-fold. The most significant changes occurred during the first 15 min, when trehalose, 2-oxoglutarate, and succinate increased, while purine biosynthesis intermediates rapidly diminished. At 30-60 min, free amino acids decreased, although several modified amino acids-including hercynylcysteine sulfoxide, a precursor to ergothioneine-accumulated. Most high-energy metabolites such as ATP, S-adenosyl-methionine or NAD+ remained stable during the whole time course. Very rapid metabolic changes such as the shut-off of purine biosynthesis and the rise of 2-oxoglutarate and succinate can be explained by the depletion of NH4Cl. The changes in the levels of key metabolites, particularly 2-oxoglutarate, might represent an important mechanistic step to trigger subsequent cellular regulations.","doi":"10.3390/metabo3041118","authors":"Sajiki K, Pluskal T, Shimanuki M, Yanagida M","authors_abbrev":"Sajiki K et al.","pubmed_publication_date":"13 Dec 2013","pubmed_entrez_date":"2014-06-25","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-06-28 00:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15616156","title":"Tfg3, a subunit of the general transcription factor TFIIF in Schizosaccharomyces pombe, functions under stress conditions.","citation":"Nucleic Acids Res 2004;32(22):6706-15","abstract":"TFIIF is a general transcription factor (GTF) that binds to RNA polymerase II (pol II) for subsequent recruitment of pol II to a promoter. TFIIF of Saccharomyces cerevisiae contains a small subunit, designated Tfg3, in addition to two conserved subunits, TFIIFalpha (Tfg1) and TFIIFbeta (Tfg2). In this study, we characterized Tfg3 of Schizosaccharomyces pombe. Using Tfg3 fused to green fluorescent protein (GFP), we found that Tfg3 is located in nuclei, and it is assembled into the C-terminal domain phosphatase (Fcp1)/TFIIF/pol II complex via interactions with TFIIFalpha and TFIIFbeta. As in the case of S.cerevisiae, Tfg3 in S.pombe forms part of another GTF, namely TFIID. The TFIID complex isolated from S.pombe that had been cultured at elevated temperatures included increased levels of Tfg3. The interaction of recombinant Tfg3 with TATA-binding protein (TBP), the central subunit of TFIID, was temperature-dependent. Moreover, a mutant of S.pombe that lacked the gene for Tfg3 was sensitive to a battery of stresses including temperature up-shift. Starting from a mutant with tfg3- mutation, we isolated five species of multicopy suppressors. Expression levels of the suppressor genes were lower in the mutant cell than in wild-type cell at an elevated temperature. Taken together, we propose that Tfg3 is involved in transcriptional regulation under stress conditions, in particular, at high temperatures.","authors":"Kimura M, Ishihama A","authors_abbrev":"Kimura M et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-12-24","publication_year":"2004","canto_session_key":"a62542172341f528","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-09 16:17:36","canto_approved_date":"2025-01-09 17:52:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-09 16:17:29","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.13c","SPCC5E4.03c","SPAC29E6.08","SPCC1620.09c","SPBC15D4.14","SPAC30D11.13","SPCC1529.01","SPAC25H1.02","SPAC22H12.02","SPBC3B8.09","SPAC19B12.05c","SPBC1734.11","SPAC16E8.16"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2024-06-09"},{"uniquename":"PMID:39527208","title":"Measuring Meiotic Recombination Frequency in Schizosaccharomyces pombe Using an Engineered Genetic Interval.","citation":"Methods Mol Biol 2025;2862:277-295","abstract":"The fission yeast Schizosaccharomyces pombe has been used to elucidate meiotic recombination mechanisms for decades. Alongside the budding yeast Saccharomyces cerevisiae, research employing fission yeast has been instrumental in advancing our knowledge of double-stranded DNA break (DSB) formation and repair during meiosis. Genetic recombination assays are the workhorses of gene conversion and crossover frequency analysis; these have been employed to investigate cis and trans determinants of meiotic recombination. Here, I describe meiotic recombination assays engineered by the introduction of nutritional markers up- and downstream of the ade6 and ade7 genes. These particular setups enable a comprehensive assessment of reproductive success in a single assay because spore viability and the frequency of gene conversion, crossovers, and crossovers associated with gene conversion events are simultaneously measured.","doi":"10.1007/978-1-0716-4168-2_20","authors":"Lorenz A","authors_abbrev":"Lorenz A","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24167549","title":"A molecular evolution approach to study the roles of tropomyosin in fission yeast.","citation":"PLoS One 2013;8(10):e76726","abstract":"Tropomyosin, a coiled-coil protein that binds along the length of the actin filament, is a universal regulator of the actin cytoskeleton. We have taken a bioinformatics/proteomic approach to studying structure-function relationships in this protein. The presence of a single, essential tropomyosin gene, cdc8, in fission yeast, Schizosaccharomyces pombe, enables a systems-based approach to define the residues that are important for cellular functions. Using molecular evolution methodologies we identified the most conserved residues and related them to the coiled coil structure. Mutants in which one or more of 21 of the most conserved surface residues was mutated to Ala were tested for the ability to rescue growth of a temperature-sensitive cdc8 mutant when overexpressed at the restrictive temperature. Based on altered morphology of the septum and actin cytoskeleton, we selected three sets of mutations for construction of mutant cdc8 strains using marker reconstitution mutagenesis and analysis of recombinant protein in vitro: D16A.K30A, V114S.E117A.H118A and R121A.D131A.E138A. The mutations have sequence-specific effects on cellular morphology including cell length, organization of cytoskeletal structures (actin patches, actin cables and contractile rings), and in vitro actin affinity, lending credence to the proteomic approach introduced here. We propose that bioinformatics is a valid analysis tool for defining structure-function relationships in conserved proteins in this model organism.","doi":"10.1371/journal.pone.0076726","authors":"Cranz-Mileva S, Pamula MC, Barua B, Desai B, Hong YH, Russell J, Trent R, Wang J, Walworth NC, Hitchcock-DeGregori SE","authors_abbrev":"Cranz-Mileva S et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-10-30","publication_year":"2013","canto_session_key":"2c01639d7a482b50","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC27F1.02c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11795888","title":"Regulation of thioredoxin peroxidase activity by C-terminal truncation.","citation":"Arch Biochem Biophys 2002 Jan 15;397(2):312-8","abstract":"Thioredoxin peroxidase is a member of peroxiredoxin (Prx) family, which uses a thioredoxin (Trx) as an immediate electron donor for the reduction of peroxide. We have identified C-terminal truncated TPx from Schizosaccharomyces pombe and also have found the truncated form is significantly tenacious against the inactivation of H2O2 than the intact form. Peroxidase assay of a series of recombinant C-terminal truncation mutants (Delta192, Delta191, Delta188, Delta184, Delta176, and Delta165) revealed that TPx could be inactivated (Delta192), reactivated (Delta191-Delta176) and reinactivated (Delta165) by serial truncation from C-terminus. We did not find any significant kinetic difference among reactivated forms; however, distinctive loss of affinity to H2O2 (K(m) = 5 microM) than that of the intact form (<<5 microM, undeterminable) was monitored. Characterization of a series of Lys(191) point mutants manifested that the loss of affinity caused by a deprivation of positive charge born in Lys(191) and the loss of affinity resulted in the resistibility to H2O2. Disk inhibition assay with S. pombe cells overexpressing wild-type, Delta192 and Delta191 mutants evidenced that the truncated forms functioning in vitro as well as in vivo.","authors":"Koo KH, Lee S, Jeong SY, Kim ET, Kim HJ, Kim K, Song K, Chae HZ","authors_abbrev":"Koo KH et al.","pubmed_publication_date":"15 Jan 2002","pubmed_entrez_date":"2002-02-06","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19211838","title":"The role of MRN in the S-phase DNA damage checkpoint is independent of its Ctp1-dependent roles in double-strand break repair and checkpoint signaling.","citation":"Mol Biol Cell 2009 Apr;20(7):2096-107","abstract":"The Mre11-Rad50-Nbs1 (MRN) complex has many biological functions: processing of double-strand breaks in meiosis, homologous recombination, telomere maintenance, S-phase checkpoint, and genome stability during replication. In the S-phase DNA damage checkpoint, MRN acts both in activation of checkpoint signaling and downstream of the checkpoint kinases to slow DNA replication. Mechanistically, MRN, along with its cofactor Ctp1, is involved in 5' resection to create single-stranded DNA that is required for both signaling and homologous recombination. However, it is unclear whether resection is essential for all of the cellular functions of MRN. To dissect the various roles of MRN, we performed a structure-function analysis of nuclease dead alleles and potential separation-of-function alleles analogous to those found in the human disease ataxia telangiectasia-like disorder, which is caused by mutations in Mre11. We find that several alleles of rad32 (the fission yeast homologue of mre11), along with ctp1Delta, are defective in double-strand break repair and most other functions of the complex, but they maintain an intact S phase DNA damage checkpoint. Thus, the MRN S-phase checkpoint role is separate from its Ctp1- and resection-dependent role in double-strand break repair. This observation leads us to conclude that other functions of MRN, possibly its role in replication fork metabolism, are required for S-phase DNA damage checkpoint function.","authors":"Porter-Goff ME, Rhind N","authors_abbrev":"Porter-Goff ME et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-02-13","publication_year":"2009","canto_session_key":"4ced25f5e52826a2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-02-10 17:22:43","canto_approved_date":"2024-06-28 10:52:35","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-02-10 17:22:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":103,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.08","SPAC3G6.06c","SPBC216.05","SPAC13C5.07","SPAC1556.01c","SPCC18B5.11c","SPBC6B1.09c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2017-02-10"},{"uniquename":"PMID:26205977","title":"Highly condensed chromatins are formed adjacent to subtelomeric and decondensed silent chromatin in fission yeast.","citation":"Nat Commun 2015 Jul 24;6:7753","abstract":"It is generally believed that silent chromatin is condensed and transcriptionally active chromatin is decondensed. However, little is known about the relationship between the condensation levels and gene expression. Here we report the condensation levels of interphase chromatin in the fission yeast Schizosaccharomyces pombe examined by super-resolution fluorescence microscopy. Unexpectedly, silent chromatin is less condensed than the euchromatin. Furthermore, the telomeric silent regions are flanked by highly condensed chromatin bodies, or 'knobs'. Knob regions span ∼50 kb of sequence devoid of methylated histones. Knob condensation is independent of HP1 homologue Swi6 and other gene silencing factors. Disruption of methylation at lysine 36 of histone H3 (H3K36) eliminates knob formation and gene repression at the subtelomeric and adjacent knob regions. Thus, epigenetic marks at H3K36 play crucial roles in the formation of a unique chromatin structure and in gene regulation at those regions in S. pombe.","doi":"10.1038/ncomms8753","authors":"Matsuda A, Chikashige Y, Ding DQ, Ohtsuki C, Mori C, Asakawa H, Kimura H, Haraguchi T, Hiraoka Y","authors_abbrev":"Matsuda A et al.","pubmed_publication_date":"24 Jul 2015","pubmed_entrez_date":"2015-07-25","publication_year":"2015","canto_session_key":"292fcc3259a4f5aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Atsushi Matsuda","canto_first_approved_date":"2016-10-26 14:17:43","canto_approved_date":"2021-10-19 16:06:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-01 05:39:56","canto_added_date":"2015-07-26 00:19:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Atsushi Matsuda","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.04","SPCC188.13c","SPCC4B3.12","SPBC336.12c","SPBC428.08c","SPBC1105.11c","SPAC29B12.02c","SPAC664.01c","SPBC36.05c","SPBC8D2.04","SPCC306.04c","SPBC800.03","SPAC343.11c"],"gene_count":13,"ltp_gene_count":8,"approved_date":"2016-10-26"},{"uniquename":"PMID:34848435","title":"RNA-binding protein Mub1 and the nuclear RNA exosome act to fine-tune environmental stress response.","citation":"Life Sci Alliance 2022 Feb;5(2)","abstract":"The nuclear RNA exosome plays a key role in controlling the levels of multiple protein-coding and non-coding RNAs. Recruitment of the exosome to specific RNA substrates is mediated by RNA-binding co-factors. The transient interaction between co-factors and the exosome as well as the rapid decay of RNA substrates make identification of exosome co-factors challenging. Here, we use comparative poly(A)+ RNA interactome capture in fission yeast expressing three different mutants of the exosome to identify proteins that interact with poly(A)+ RNA in an exosome-dependent manner. Our analyses identify multiple RNA-binding proteins whose association with RNA is altered in exosome mutants, including the zinc-finger protein Mub1. Mub1 is required to maintain the levels of a subset of exosome RNA substrates including mRNAs encoding for stress-responsive proteins. Removal of the zinc-finger domain leads to loss of RNA suppression under non-stressed conditions, altered expression of heat shock genes in response to stress, and reduced growth at elevated temperature. These findings highlight the importance of exosome-dependent mRNA degradation in buffering gene expression networks to mediate cellular adaptation to stress.","doi":"10.26508/lsa.202101111","authors":"Birot A, Kus K, Priest E, Al Alwash A, Castello A, Mohammed S, Vasiljeva L, Kilchert C","authors_abbrev":"Birot A et al.","pubmed_publication_date":"Feb 2022","pubmed_entrez_date":"2021-12-01","publication_year":"2022","canto_session_key":"b05547e76d5bbfc0","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-03 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1831760","title":"Beta subunit of mitochondrial F1-ATPase from the fission yeast. Deduced sequence of the wild type protein and identification of a mutation that increases nucleotide binding.","citation":"Eur J Biochem 1991 Aug 15;200(1):61-7","abstract":"The Schizosaccharomyces pombe nuclear gene, atp2, encoding the beta subunit of the mitochondrial ATP synthase, was sequenced and found to contain a 1575-bp open reading frame. Two adjacent transcription-initiation sites were found at positions 34 and 44 nucleotides upstream of the translation-initiation codon. The deduced polypeptide sequence was composed of 525 amino acid residues (molecular mass = 56875 Da). The mature polypeptide starts at residue 45 (molecular mass = 51,685 Da), indicating the presence of a presequence of 44 residues, presumably involved in mitochondrial targeting. The atp2 mutant B59-1 [Boutry, M. & Goffeau, A. (1982) Eur. J. Biochem. 125, 471-477] and its related revertant allele R4-3 [Jault, J. M., Di Pietro, A., Falson, P., Gautheron, D. C., Boutry, M. & Goffeau, A. (1989) Biochem. Biophys. Res. Commun. 158, 392-399] were also cloned and sequenced. A single nonsense mutation, CAG (Gln170)----TAG (stop) in mutant B59-1, became a missense mutation, TAG (stop)----TAC (Tyr) in revertant R4-3. Gln170 is located between the first and second elements belonging to the nucleotide-binding site. Its substitution by a tyrosine residue increases the enzyme affinity towards ADP, the amount of endogenous nucleotides and the apparent negative cooperativity for ATPase activity.","authors":"Falson P, Leterme S, Capiau C, Boutry M","authors_abbrev":"Falson P et al.","pubmed_publication_date":"15 Aug 1991","pubmed_entrez_date":"1991-08-15","publication_year":"1991","canto_session_key":"16d52afc5ba4cad9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-08 08:48:29","canto_approved_date":"2020-12-15 14:34:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-07 13:32:33","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC222.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-08"},{"uniquename":"PMID:10792724","title":"Sxa2 is a serine carboxypeptidase that degrades extracellular P-factor in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Microbiol 2000 Apr;36(2):377-90","abstract":"Stimulating the fission yeast Schizosaccharomyces pombe with mating pheromones brings about responses that lead to cell conjugation. Persistent stimulation does not, however, induce a continuous response as the cells become desensitized to the presence of the pheromone. One mechanism that contributes to desensitization in M-cells is the release of a carboxypeptidase that inactivates the extracellular P-factor pheromone. Production of the carboxypeptidase requires a functional sxa2 gene. In this study, we report the first molecular characterization of the Sxa2 protein and provide direct evidence that it is the carboxypeptidase that degrades P-factor. Sxa2 is synthesized as a precursor that undergoes an internal cleavage event catalysed by a protease with specificity for basic residues. This generates a series of catalytically active N-terminal fragments and an inactive C-terminal fragment. Cleavage is essential for activation of the carboxypeptidase and, although the C-terminal fragment is inactive, it is required for the N-terminal fragment to attain activity.","authors":"Ladds G, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-05-03","publication_year":"2000","canto_session_key":"a525406360ac556a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-29 12:46:32","canto_approved_date":"2026-04-08 11:08:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-26 11:57:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.06","SPAC1296.03c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2016-03-29"},{"uniquename":"PMID:9535802","title":"Secretion of heterologous proteins from Schizosaccharomyces pombe using the homologous leader sequence of pho1+ acid phosphatase.","citation":"Biochem Biophys Res Commun 1998 Apr 07;245(1):166-71","abstract":"In this study we report the use of the S. pombe leader sequence of pho1+ acid phosphatase (Elliott et al., J. Biol. Chem. 216, 2916-2941, 1986) for the secretion of heterologous proteins into the medium. The green fluorescent protein (GFP) and the Human Papillomavirus (HPV) type 16 E7 protein are normally not secreted; fusion of the S. pombe pho1 leader peptide (SPL) to GFP and HPV 16 E7 resulted in an efficient secretion of these proteins although the latter contains a nuclear targeting sequence. These data suggest that SPL fused constructs could be applied for the production of other recombinant proteins using the S. pombe expression system. Furthermore, since GFP retains its intrinsic fluorescence during the secretion, this system may be useful to study the secretory pathway of fission yeast in vivo.","authors":"Braspenning J, Meschede W, Marchini A, Müller M, Gissmann L, Tommasino M","authors_abbrev":"Braspenning J et al.","pubmed_publication_date":"07 Apr 1998","pubmed_entrez_date":"1998-05-16","publication_year":"1998","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6214396","title":"Alterations of the alpha or beta subunits of the mitochondrial ATPase in yeast mutants.","citation":"Eur J Biochem 1982 Jul;125(3):471-7","abstract":"Among 979 non-glycerol growers of the yeast Schizosaccharomyces pombe, 40 strains were found to be deficient in the mitochondrial ATPase activity. Three of them exhibited an alteration in either the alpha or beta subunits of the F1ATPase. The alpha subunit was not immunodetected in the A23/13 mutant. The beta subunit was not immuno-detected in the B59/1 mutant. The existence of these two mutants shows that the alpha and beta subunits can be present independently of each other in the inner mitochondrial membrane. The beta subunit of the mutant F25/28 had a slower electrophoretic mobility than that of the wild-type beta subunit. This phenotype indicates abnormal processing or specific modification of the beta subunit. All mutants showed reduced activities of the NADH-cytochrome c reductase and of the cytochrome oxidase and a decreased synthesis of cytochrome aa3 and cytochrome b. This pleiotropic phenotype appears to result from specific modifications in the mitochondrial protein synthesis. The mitochondrial synthesis of four polypeptides (three cytochrome oxidase and one cytochrome b subunits) was markedly decreased or absent while three new polypeptides (Mr = 54000, 20000 and 15000) were detected in all the mutants analysed. This observation suggests that a functional F1ATPase is necessary for the correct synthesis and/or assembly of the mitochondrially made components of the cytochrome oxidase and cytochrome b complexes.","authors":"Boutry M, Goffeau A","authors_abbrev":"Boutry M et al.","pubmed_publication_date":"Jul 1982","pubmed_entrez_date":"1982-07-01","publication_year":"1982","canto_session_key":"1509b9be31a0fb9f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-04-05 16:43:32","canto_approved_date":"2024-03-13 18:34:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-04-05 16:42:39","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.14","SPAC222.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-04-05"},{"uniquename":"PMID:7565716","title":"A phosphatidylinositol (PI) kinase gene family in Dictyostelium discoideum: biological roles of putative mammalian p110 and yeast Vps34p PI 3-kinase homologs during growth and development.","citation":"Mol Cell Biol 1995 Oct;15(10):5645-56","abstract":"Three groups of phosphatidylinositol (PI) kinases convert PI into PI(3)phosphate, PI(4)phosphate, PI(4,5) bisphosphate, and PI(3,4,5)trisphosphate. These phosphoinositides have been shown to function in vesicle-mediated protein sorting, and they serve as second-messenger signaling molecules for regulating cell growth. To further elucidate the mechanism of regulation and function of phosphoinositides, we cloned genes encoding five putative PI kinases from Dictyostelium discoideum. Database analysis indicates that D. discoideum PIK1 (DdPIK1), -2, and -3 are most closely related to the mammalian p110 PI 3-kinase, DdPIK5 is closest to the yeast Vps34p PI 3-kinase, and DdPIK4 is most homologous to PI 4-kinases. Together with other known PI kinases, a superfamily of PI kinase genes has been defined, with all of the encoded proteins sharing a common highly conserved catalytic core domain. DdPIK1, -2, and -3 may have redundant functions because disruption of any single gene had no effect on D. discoideum growth or development. However, strains in which both of the two most highly related genes, DdPIK1 and DdPIK2, were disrupted showed both growth and developmental defects, while double knockouts of DdPIK1 and DdPIK3 and DdPIK2 and DdPIK3 appear to be lethal. The delta Ddpik1 delta Ddpik2 null cells were smaller than wild-type cells and grew slowly both in association with bacteria and in axenic medium when attached to petri plates but were unable to grow in suspension in axenic medium. When delta Ddpik1 delta Ddpik2 null cells were plated for multicellular development, they formed aggregates having multiple tips and produced abnormal fruiting bodies. Antisense expression of DdPIK5 (a putative homolog of the Saccharomyces cerevisiae VPS34) led to a defect in the growth of D. discoideum cells on bacterial lawns and abnormal development. DdPIK5 complemented the temperature-sensitive growth defect of a Schizosaccharomyces pombe delta Svps34 mutant strain, suggesting DdPIK5 encodes a functional homolog of yeast Vps34p. These observations indicate that in D. discoideum, different PI kinases regulate distinct cellular processes, including cell growth, development, and protein trafficking.","authors":"Zhou K, Takegawa K, Emr SD, Firtel RA","authors_abbrev":"Zhou K et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_session_key":"14db822a0fce4f86","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 14:12:06","canto_session_submitted_date":"2012-03-03 14:11:35","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC458.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PANTHER:PTHR14360","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC27B12.07","HGNC:28108","HGNC:21097"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:31597736","title":"Centromere repositioning causes inversion of meiosis and generates a reproductive barrier.","citation":"Proc Natl Acad Sci U S A 2019 Oct 22;116(43):21580-21591","abstract":"The chromosomal position of each centromere is determined epigenetically and is highly stable, whereas incremental cases have supported the occurrence of centromere repositioning on an evolutionary time scale (evolutionary new centromeres, ENCs), which is thought to be important in speciation. The mechanisms underlying the high stability of centromeres and its functional significance largely remain an enigma. Here, in the fission yeast  Schizosaccharomyces pombe , we identify a feedback mechanism: The kinetochore, whose assembly is guided by the centromere, in turn, enforces centromere stability. Upon going through meiosis, specific inner kinetochore mutations induce centromere repositioning-inactivation of the original centromere and formation of a new centromere elsewhere-in 1 of the 3 chromosomes at random. Repositioned centromeres reside asymmetrically in the pericentromeric regions and cells carrying them are competent in mitosis and homozygotic meiosis. However, when cells carrying a repositioned centromere are crossed with those carrying the original centromere, the progeny suffer severe lethality due to defects in meiotic chromosome segregation. Thus, repositioned centromeres constitute a reproductive barrier that could initiate genetic divergence between 2 populations with mismatched centromeres, documenting a functional role of ENCs in speciation. Surprisingly, homozygotic repositioned centromeres tend to undergo meiosis in an inverted order-that is, sister chromatids segregate first, and homologous chromosomes separate second-whereas the original centromeres on other chromosomes in the same cell undergo meiosis in the canonical order, revealing hidden flexibility in the perceived rigid process of meiosis.","doi":"10.1073/pnas.1911745116","authors":"Lu M, He X","authors_abbrev":"Lu M et al.","pubmed_publication_date":"22 Oct 2019","pubmed_entrez_date":"2019-10-11","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-10-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16472019","title":"Validation of S. pombe sequence assembly by microarray hybridization.","citation":"J Comput Biol 2006;13(1):1-20","abstract":"We describe a method to make physical maps of genomes using correlative hybridization patterns of probes to random pools of BACs. We derive thereby an estimated distance between probes, and then use this estimated distance to order probes. To test the method, we used BAC libraries from Schizzosaccharomyces pombe. We compared our data to the known sequence assembly, in order to assess accuracy. We demonstrate a small number of significant discrepancies between our method and the map derived by sequence assembly. Some of these discrepancies may arise because genome order within a population is not stable; imposing a linear order on a population may not be biologically meaningful.","authors":"West J, Healy J, Wigler M, Casey W, Mishra B","authors_abbrev":"West J et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-02-14","publication_year":"2006","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1819507","title":"cdc25 M-phase inducer.","citation":"Cold Spring Harb Symp Quant Biol 1991;56:577-84","abstract":"In this paper, we have described the critical experiments leading to the discovery and analysis of the cdc25 M-phase inducer. We have shown that timing of mitosis is sensitive to the level of cdc25+ expression and that the cellular concentration of p80cdc25 increases as cells approach mitosis. From these observations we conclude that, in S. pombe, rate of accumulation of p80cdc25 plays an important role in determining the timing of mitosis. We postulate that under a given set of conditions, a critical level of p80cdc25 activity is required to undergo mitosis. The actual level that is required can vary depending on ploidy, growth rate, nutritional status of the cell, and perhaps other parameters. These signals may be monitored through the weel pathway leading to tyrosyl phosphorylation of p34cdc2. We have shown that p80cdc25 encodes a phosphate that acts by directly dephosphorylating the Tyr-15 residue of p34cdc2. Our studies strongly indicate that this aspect of the mitotic control network is generally conserved among eukaryotes. It is conceivable, however, that the mode of regulation of cdc25 activity may vary from species to species. Clearly, in S. cerevisiae the cdc25+ homolog, MIH1, in contrast to cdc25+, is not rate-limiting for M-phase onset. It will be important to determine whether the level of cdc25+ homologs in other organisms also oscillates during the cell cycle, or whether their activity is controlled by localization or posttranslational mechanisms, such as phosphorylation. Furthermore, our finding of more than one cdc25+ homolog in a single species suggests an additional level of complexity to the control of M-phase onset by cdc25 in higher eukaryotes that will require further investigation.","authors":"Millar J, McGowan C, Jones R, Sadhu K, Bueno A, Richardson H, Russell P","authors_abbrev":"Millar J et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_session_key":"dfe049938664b7ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-01-12 15:18:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-26 10:23:00","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-08-26"},{"uniquename":"PMID:33099301","title":"Calculating the most likely intron splicing orders in S. pombe, fruit fly, Arabidopsis thaliana, and humans.","citation":"BMC Bioinformatics 2020 Oct 24;21(1):478","abstract":"Introns have been shown to be spliced in a defined order, and this order influences both alternative splicing regulation and splicing fidelity, but previous studies have only considered neighbouring introns. The detailed intron splicing order remains unknown.\nIn this work, a method was developed that can calculate the intron splicing orders of all introns in each transcript. A simulation study showed that this method can accurately calculate intron splicing orders. I further applied this method to real S. pombe, fruit fly, Arabidopsis thaliana, and human sequencing datasets and found that intron splicing orders change from gene to gene and that humans contain more not in-order spliced transcripts than S. pombe, fruit fly and Arabidopsis thaliana. In addition, I reconfirmed that the first introns in humans are spliced slower than those in S. pombe, fruit fly, and Arabidopsis thaliana genome-widely. Both the calculated most likely orders and the method developed here are available on the web.\nA novel computational method was developed to calculate the intron splicing orders and applied the method to real sequencing datasets. I obtained intron splicing orders for hundreds or thousands of genes in four organisms. I found humans contain more number of not in-order spliced transcripts.","doi":"10.1186/s12859-020-03818-6","authors":"Li M","authors_abbrev":"Li M","pubmed_publication_date":"24 Oct 2020","pubmed_entrez_date":"2020-10-25","publication_year":"2020","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2020-10-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11934898","title":"Characterization of the CTD phosphatase Fcp1 from fission yeast. Preferential dephosphorylation of serine 2 versus serine 5.","citation":"J Biol Chem 2002 Jun 14;277(24):21213-20","abstract":"The C-terminal domain (CTD) of RNA polymerase II undergoes extensive phosphorylation and dephosphorylation at positions Ser2 and Ser5 during the transcription cycle. A single CTD phosphatase, Fcp1, has been identified in yeast and metazoans. Here we conducted a biochemical characterization of Fcp1 from the fission yeast Schizosaccharomyces pombe. The 723-amino acid Fcp1 protein was expressed at high levels in bacteria. Recombinant Fcp1 catalyzed the metal-dependent hydrolysis of para-nitrophenyl phosphate with a pH optimum of 5.5 (kcat = 2 s(-1); K(m) = 19 mm). Deletion analysis showed that 139- and 143-amino acid segments could be deleted from the N and C termini of Fcp1, respectively, without affecting phosphatase activity. A segment containing amino acids 487-580, deletion of which abolished activity, embraces a BRCT domain present in all known Fcp1 orthologs. Mutations of residues Asp170 and Asp172 abrogated Fcp1 phosphatase activity; the essential aspartates are located within a 170DXDXT172 motif that defines a superfamily of metal-dependent phosphotransferases. We exploited defined synthetic CTD phosphopeptide substrates to show for the first time that: (i) Fcp1 CTD phosphatase activity is not confined to native polymerase II and (ii) Fcp1 displays an inherent preference for a particular CTD phosphorylation array. Using equivalent concentrations (25 microm) of CTD peptides of identical amino acid sequence and phosphoserine content, which differed only in the positions of phosphoserine within the heptad, we found that Fcp1 was 10-fold more active in dephosphorylating Ser2-PO4 than Ser5-PO4.","authors":"Hausmann S, Shuman S","authors_abbrev":"Hausmann S et al.","pubmed_publication_date":"14 Jun 2002","pubmed_entrez_date":"2002-04-06","publication_year":"2002","canto_session_key":"220ebae26d2f06e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-07-06 12:33:40","canto_approved_date":"2022-02-23 11:54:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-15 10:44:30","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19B12.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-07-06"},{"uniquename":"PMID:2656692","title":"Molecular cloning of Saccharomyces cerevisiae CDC6 gene. Isolation, identification, and sequence analysis.","citation":"J Biol Chem 1989 May 25;264(15):9022-9","abstract":"The CDC6 gene product is required for entering the S phase of the cell cycle in Saccharomyces cerevisiae. It has been isolated on recombinant plasmids by selection for complementation of temperature-sensitive alleles with a yeast genomic library. The entire complementing activity is carried on a 1.8-kilobase chromosomal DNA fragment, as revealed by deletion mapping. Northern blotting shows that the size of the CDC6 mRNA is about 1.7 kilobases. A Southern blot of yeast chromosomes which were separated by the field inversion gel electrophoresis method indicates that the isolated DNA fragment is derived from chromosome X. The locus from which the clone was derived was marked by integration with a nutritional marker and found by meiotic mapping to cosegregate with CDC6. Thus, we conclude that we have isolated the authentic CDC6 gene. Nucleotide sequence analysis of the CDC6 gene has revealed an open reading frame that encodes a protein with Mr = 57,969. There are five potential Asn-X-(Ser/Thr) glycosylation sites and a highly conserved nucleotide-binding site in the CDC6 sequence. Although computer surveys indicate overall sequence homology between S. cerevisiae CDC6 protein and Saccharomyces pombe CDC10 START protein, they may not be functionally equivalent as evaluated by the complementation assay.","authors":"Zhou C, Huang SH, Jong AY","authors_abbrev":"Zhou C et al.","pubmed_publication_date":"25 May 1989","pubmed_entrez_date":"1989-05-25","publication_year":"1989","canto_session_key":"d193c1991c200540","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 13:38:54","canto_session_submitted_date":"2012-03-03 13:38:34","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:28765303","title":"Genetic Analysis of  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Aug 01;2017(8):pdb.top079772","abstract":"In this introduction we discuss some basic genetic tools and techniques that are used with the fission yeast  Schizosaccharomyces pombe  Genes commonly used for selection or as reporters are discussed, with an emphasis on genes that permit counterselection, intragenic complementation, or colony-color assays.  S. pombe  is most stable as a haploid organism. We describe its mating-type system, how to perform genetic crosses and methods for selecting and propagating diploids. We discuss the relative merits of tetrad dissection and random spore preparation in strain construction and genetic analyses. Finally, we present several types of mutant screens, with an evaluation of their respective strengths and limitations in the light of emerging technologies such as next-generation sequencing.","doi":"10.1101/pdb.top079772","authors":"Ekwall K, Thon G","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"01 Aug 2017","pubmed_entrez_date":"2017-08-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-08-04 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29967244","title":"Histone Chaperone Asf1 Is Required for the Establishment of Repressive Chromatin in Schizosaccharomyces pombe fbp1 Gene Repression.","citation":"Mol Cell Biol 2018 Sep 15;38(18)","abstract":"The arrangement of nucleosomes in chromatin plays a role in transcriptional regulation by restricting the accessibility of transcription factors and RNA polymerase II to  cis -acting elements and promoters. For gene activation, the chromatin structure is altered to an open configuration. The mechanism for this process has been extensively analyzed. However, the mechanism by which repressive chromatin is reconstituted to terminate transcription has not been fully elucidated. Here, we investigated the mechanisms by which chromatin is reconstituted in the fission yeast  Schizosaccharomyces pombe  fbp1  gene, which is robustly induced upon glucose starvation but tightly repressed under glucose-rich conditions. We found that the chromatin structure in the region upstream from  fbp1  is closed by a two-step process. When cells are returned to glucose-rich medium following glucose starvation, changes in the nucleosome pattern alter the chromatin configuration at the transcription factor binding site to an inaccessible state, after which the nucleosome density upstream from  fbp1  gradually increases via histone loading. Interestingly, this histone loading was observed in the absence of the Tup family corepressors Tup11 and Tup12. Analysis of strains carrying either gene disruptions or mutations affecting nine fission yeast histone chaperone genes demonstrated that the histone chaperone Asf1 induces nucleosome loading during glucose repression. These data establish a previously unappreciated chromatin reconstitution mechanism in  fbp1  repression.","doi":"10.1128/MCB.00194-18","authors":"Umeda M, Tsunekawa C, Senmatsu S, Asada R, Abe T, Ohta K, Hoffman CS, Hirota K","authors_abbrev":"Umeda M et al.","pubmed_publication_date":"15 Sep 2018","pubmed_entrez_date":"2018-07-04","publication_year":"2018","canto_session_key":"6237c6a837e9e19a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-07-17 13:00:24","canto_approved_date":"2018-07-17 13:01:07","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-07-07 09:16:44","canto_added_date":"2018-07-05 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31F10.13c","SPAC6F12.02","SPCC663.05c","SPBC1198.14c","SPAC1F7.01c","SPBC36B7.08c","SPBC609.05","SPAC6G9.03c","SPCC364.06","SPBC29A10.03c","SPAC18B11.10","SPAC4G9.06c","SPBC29B5.01","SPAC630.14c"],"gene_count":14,"ltp_gene_count":3,"approved_date":"2018-07-17"},{"uniquename":"PMID:8257099","title":"Chromosome segregation in yeast.","citation":"Annu Rev Microbiol 1993;47:231-61","abstract":"Because of their genetic tractability, much has been learned concerning the mechanisms of chromosome segregation in budding yeast, Saccharomyces cerevisiae, and fission yeast, Schizosaccharomyces pombe. This chapter reviews the cytology and molecular and cell biology of mitosis in both of these yeasts. Current knowledge about the components of the mitotic spindle apparatus, including spindle pole bodies, centromeres, and microtubule components and motors, is summarized. Mechanisms of mitosis such as establishment and positioning of the mitotic spindle apparatus, anaphase A, and anaphase B are reviewed.","authors":"Page BD, Snyder M","authors_abbrev":"Page BD et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24006256","title":"Fission yeast nucleolar protein Dnt1 regulates G2/M transition and cytokinesis by downregulating Wee1 kinase.","citation":"J Cell Sci 2013 Nov 01;126(Pt 21):4995-5004","abstract":"Cytokinesis involves temporally and spatially coordinated action of the cell cycle, cytoskeletal and membrane systems to achieve separation of daughter cells. The septation initiation network (SIN) and mitotic exit network (MEN) signaling pathways regulate cytokinesis and mitotic exit in the yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae, respectively. Previously, we have shown that in fission yeast, the nucleolar protein Dnt1 negatively regulates the SIN pathway in a manner that is independent of the Cdc14-family phosphatase Clp1/Flp1, but how Dnt1 modulates this pathway has remained elusive. By contrast, it is clear that its budding yeast relative, Net1/Cfi1, regulates the homologous MEN signaling pathway by sequestering Cdc14 phosphatase in the nucleolus before mitotic exit. In this study, we show that dnt1(+) positively regulates G2/M transition during the cell cycle. By conducting epistasis analyses to measure cell length at septation in double mutant (for dnt1 and genes involved in G2/M control) cells, we found a link between dnt1(+) and wee1(+). Furthermore, we showed that elevated protein levels of the mitotic inhibitor Wee1 kinase and the corresponding attenuation in Cdk1 activity is responsible for the rescuing effect of dnt1Δ on SIN mutants. Finally, our data also suggest that Dnt1 modulates Wee1 activity in parallel with SCF-mediated Wee1 degradation. Therefore, this study reveals an unexpected missing link between the nucleolar protein Dnt1 and the SIN signaling pathway, which is mediated by the Cdk1 regulator Wee1 kinase. Our findings also define a novel mode of regulation of Wee1 and Cdk1, which is important for integration of the signals controlling the SIN pathway in fission yeast.","doi":"10.1242/jcs.132845","authors":"Yu ZY, Zhang MT, Wang GY, Xu D, Keifenheim D, Franco A, Cansado J, Masuda H, Rhind N, Wang Y, Jin QW","authors_abbrev":"Yu ZY et al.","pubmed_publication_date":"01 Nov 2013","pubmed_entrez_date":"2013-09-06","publication_year":"2013","canto_session_key":"5d9d97db30265d3a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":" Quanwen Jin","canto_first_approved_date":"2017-01-03 16:51:10","canto_approved_date":"2019-06-14 12:53:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-11-05 07:36:30","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":" Quanwen Jin","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC24C6.07","SPBC25D12.02c","SPBC409.05","SPAC24H6.05","SPBC16G5.01","SPCC18B5.03","SPBC11B10.09","SPAC24B11.11c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-01-03"},{"uniquename":"PMID:28264193","title":"Substrate specificity of TOR complex 2 is determined by a ubiquitin-fold domain of the Sin1 subunit.","citation":"Elife 2017 Mar 07;6","abstract":"The target of rapamycin (TOR) protein kinase forms multi-subunit TOR complex 1 (TORC1) and TOR complex 2 (TORC2), which exhibit distinct substrate specificities. Sin1 is one of the TORC2-specific subunit essential for phosphorylation and activation of certain AGC-family kinases. Here, we show that Sin1 is dispensable for the catalytic activity of TORC2, but its conserved region in the middle (Sin1CRIM) forms a discrete domain that specifically binds the TORC2 substrate kinases. Sin1CRIM fused to a different TORC2 subunit can recruit the TORC2 substrate Gad8 for phosphorylation even in the  sin1  null mutant of fission yeast. The solution structure of Sin1CRIM shows a ubiquitin-like fold with a characteristic acidic loop, which is essential for interaction with the TORC2 substrates. The specific substrate-recognition function is conserved in human Sin1CRIM, which may represent a potential target for novel anticancer drugs that prevent activation of the mTORC2 substrates such as AKT.","doi":"10.7554/eLife.19594","authors":"Tatebe H, Murayama S, Yonekura T, Hatano T, Richter D, Furuya T, Kataoka S, Furuita K, Kojima C, Shiozaki K","authors_abbrev":"Tatebe H et al.","pubmed_publication_date":"07 Mar 2017","pubmed_entrez_date":"2017-03-07","publication_year":"2017","canto_session_key":"9917fbd53b49c243","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hisashi Tatebe","canto_first_approved_date":"2018-07-26 23:05:42","canto_approved_date":"2025-09-24 06:35:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-24 05:32:08","canto_added_date":"2017-03-08 01:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Hisashi Tatebe","community_curator":true,"annotation_count":29,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.08c","SPCC24B10.07","SPAC1B9.02c","SPBC216.07c","SPCC4G3.08","SPBC12D12.04c","SPAC22E12.14c","SPBC30D10.10c","SPAC57A7.11","SPBC21B10.05c","SPAPYUG7.02c","SPBC106.10","SPBC12C2.02c","SPAC17G8.14c"],"gene_count":14,"ltp_gene_count":6,"approved_date":"2018-07-26","pdb_entries":[{"pdb_id":"2rvk","gene_chains":[{"gene_uniquename":"SPAPYUG7.02c","chain":"A","position":"247-400"}],"title":"Refined solution structure of Schizosaccharomyces pombe Sin1 CRIM domain","entry_authors":"Furuita K,Kataoka S,Shiozaki K,Kojima C","entry_authors_abbrev":"Furuita K et al.","reference_uniquename":"PMID:28264193","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:16467377","title":"Rad22Rad52-dependent repair of ribosomal DNA repeats cleaved by Slx1-Slx4 endonuclease.","citation":"Mol Biol Cell 2006 Apr;17(4):2081-90","abstract":"Slx1 and Slx4 are subunits of a structure-specific DNA endonuclease that is found in Saccharomyces cerevisiae, Schizosaccharomyces pombe, and other eukaryotic species. It is thought to initiate recombination events or process recombination structures that occur during the replication of the tandem repeats of the ribosomal DNA (rDNA) locus. Here, we present evidence that fission yeast Slx1-Slx4 initiates homologous recombination events in the rDNA repeats that are processed by a mechanism that requires Rad22 (Rad52 homologue) but not Rhp51 (Rad51 homologue). Slx1 is required to generate approximately 50% of the spontaneous Rad22 DNA repair foci that occur in cycling cells. Most of these foci colocalize with the nucleolus, which contains the rDNA repeats. The increased fork pausing at the replication fork barriers in the rDNA repeats in a strain that lacks Rqh1 DNA helicase is further increased by expression of a dominant negative form of Slx1. These data suggest that Slx1-Slx4 cleaves paused replication forks in the rDNA, leading to Rad22-dependent homologous recombination that is used to maintain rDNA copy number.","authors":"Coulon S, Noguchi E, Noguchi C, Du LL, Nakamura TM, Russell P","authors_abbrev":"Coulon S et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-02-10","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPAC688.06c","SPAP27G11.15"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11683417","title":"Live observation of fission yeast meiosis in recombination-deficient mutants: a study on achiasmate chromosome segregation.","citation":"J Cell Sci 2001 Aug;114(Pt 15):2843-53","abstract":"Regular segregation of homologous chromosomes during meiotic divisions is essential for the generation of viable progeny. In recombination-proficient organisms, chromosome disjunction at meiosis I generally occurs by chiasma formation between the homologs (chiasmate meiosis). We have studied meiotic stages in living rec8 and rec7 mutant cells of fission yeast, with special attention to prophase and the first meiotic division. Both rec8 and rec7 are early recombination mutants, and in rec7 mutants, chromosome segregation at meiosis I occurs without any recombination (achiasmate meiosis). Both mutants showed distinct irregularities in nuclear prophase movements. Additionally, rec7 showed an extended first division of variable length and with single chromosomes changing back and forth between the cell poles. Two other early recombination deficient mutants (rec14 and rec15) showed very similar phenotypes to rec7 during the first meiotic division, and the fidelity of achiasmate chromosome segregation slightly exceeded the expected random level. We discuss possible regulatory mechanisms of fission yeast to deal with achiasmate chromosome segregation.","authors":"Molnar M, Bähler J, Kohli J, Hiraoka Y","authors_abbrev":"Molnar M et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-10-31","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10419486","title":"The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein.","citation":"J Biol Chem 1999 Jul 30;274(31):21735-40","abstract":"Aps1 from Schizosaccharomyces pombe (Ingram, S. W., Stratemann, S. A. , and Barnes, L. D. (1999) Biochemistry 38, 3649-3655) and YOR163w from Saccharomyces cerevisiae (Cartwright, J. L., and McLennan, A. G. (1999) J. Biol. Chem. 274, 8604-8610) have both previously been characterized as MutT family hydrolases with high specificity for diadenosine hexa- and pentaphosphates (Ap(6)A and Ap(5)A). Using purified recombinant preparations of these enzymes, we have now discovered that they have an important additional function, namely, the efficient hydrolysis of diphosphorylated inositol polyphosphates. This overlapping specificity of an enzyme for two completely different classes of substrate is not only of enzymological significance, but in addition, this finding provides important new information pertinent to the structure, function, and evolution of the MutT motif. Moreover, we report that the human protein previously characterized as a diphosphorylated inositol phosphate phosphohydrolase represents the first example, in any animal, of an enzyme that degrades Ap(6)A and Ap(5)A, in preference to other diadenosine polyphosphates. The emergence of Ap(6)A and Ap(5)A as extracellular effectors and intracellular ion-channel ligands points not only to diphosphorylated inositol phosphate phosphohydrolase as a candidate for regulating signaling by diadenosine polyphosphates, but also suggests that diphosphorylated inositol phosphates may competitively inhibit this process.","authors":"Safrany ST, Ingram SW, Cartwright JL, Falck JR, McLennan AG, Barnes LD, Shears SB","authors_abbrev":"Safrany ST et al.","pubmed_publication_date":"30 Jul 1999","pubmed_entrez_date":"1999-07-27","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8350245","title":"Physical and functional characterization of the cloned lys1+ gene of Schizosaccharomyces pombe.","citation":"J Basic Microbiol 1993;33(3):179-86","abstract":"The alpha-aminoadipate pathway for the biosynthesis of lysine is present in yeast and other higher fungi. The lys2 and lys5 mutants of Saccharomyces cerevisiae as well as the lys1- and lys7-mutants of Schizosacharomyces pombe are blocked at the alpha-aminoadipate reductase step of this pathway. The cloned lys1+ gene in the plasmid pLYS1 isolated from a S. pombe genomic library complemented lys1-mutant of S. pombe. The cloned LYS2 gene in the plasmid YEp620 and the LYS5 gene in the plasmid pSC5 of S. cerevisiae exhibited heterologous complementation of lys1- and lys7-mutants, respectively, of S. pombe. The homologous lys1+ transformed cells exhibited five fold higher alpha-aminoadipate reductase activity while the heterologous lys1+ and lys7+ transformed cells exhibited much less activity than the wild type cells. The DNA insert of the plasmid pLYS1 was determined to be 16.7 kb long and the lys1+ gene has been subcloned within a 9.1 kb Clal-Clal DNA insert of the recombinant plasmids pLYS1B and pLYS1C. The restriction pattern for 12 enzymes of the 9.1 kb DNA insert, (Apal, Aval, BamHI, Clal, EcoRI, EcoRV, HindIII, Hpal, Pstl, Pvull, Sphl, and Xbal), exhibited no obvious similarity to that of the LYS2 gene of S. cerevisiae. A 1.7 kb EcoRI-HindIII DNA fragment of pLYS1B and pLYS1C complemented the lys1-131 mutation in an integrative transformation. Although the lys1+ gene of S. pombe is isofunctional to the LYS2 gene of S. cerevisiae, the restriction sites, and expression of these two genes exhibited considerable divergence.","authors":"Ford RA, Ye ZH, Bhattacharjee JK","authors_abbrev":"Ford RA et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_session_key":"9aea962dee83bb5f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-09-11 17:18:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 17:08:32","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP7G5.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-11"},{"uniquename":"PMID:22064477","title":"The RecQ4 orthologue Hrq1 is critical for DNA interstrand cross-link repair and genome stability in fission yeast.","citation":"Mol Cell Biol 2012 Jan;32(2):276-87","abstract":"Of the five human RecQ family helicases, RecQ4, BLM, and WRN suppress distinct genome instability-linked diseases with severe phenotypes, often with indeterminate etiologies. Here, we functionally define Hrq1, a novel orthologue of RecQ4 from fission yeast. Biochemical analysis of Hrq1 reveals a DEAH box- and ATP-dependent 3'-5' helicase activity on various DNA substrates, including bubbles but not blunt duplexes, characteristic of the RecQ family. Cells lacking Hrq1 suffer spontaneous genomic instability and, consequently, require homologous recombination repair and the DNA damage checkpoint for viability. Hrq1 supports the nucleotide excision repair of DNA damage caused by the chemotherapeutic agent cisplatin and, in certain genetic contexts, UV light. Genetic epistasis analyses reveal that Hrq1 acts parallel to the PCNA/Ubc13/Mms2-dependent postreplication repair (PRR) pathway. Thus, in hrq1Δ cells, lesions are channeled through the PRR pathway, yielding hyper-recombinant and mutator phenotypes; analogous defects may underlie the genetic instability and diseases associated with RecQ4 dysfunction.","doi":"10.1128/MCB.06184-11","authors":"Groocock LM, Prudden J, Perry JJ, Boddy MN","authors_abbrev":"Groocock LM et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2011-11-09","publication_year":"2012","canto_session_key":"efa1583765ddce89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lynda Groocock","canto_first_approved_date":"2015-10-28 08:35:50","canto_approved_date":"2022-03-21 17:43:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-05 10:09:39","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Lynda Groocock","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPBC649.03","SPAC644.14c","SPCC338.05c","SPBC3E7.08c","SPBC16D10.09","SPAC11E3.08c","SPAC23A1.19c","SPBC1347.01c","SPAC688.10","SPCC970.01","SPBC1921.02","SPCC4G3.05c","SPAC11E3.04c","SPCC1259.13"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2015-10-28"},{"uniquename":"PMID:17300221","title":"Schizosaccharomyces pombe minimum genome factory.","citation":"Biotechnol Appl Biochem 2007 Mar;46(Pt 3):147-55","abstract":"Various systems for the production of useful proteins have been developed using the fission yeast Schizosaccharomyces pombe as a host, and some are now being used commercially. It is necessary, however, to improve the system further for the production of low-cost chemicals and commodities, so that the host becomes more economical and productive and can be widely used for the production of different molecules. We hypothesized that many S. pombe genes are not necessary under nutrient-rich growth conditions; or rather, they serve only to waste energy when seen from the viewpoint of protein production, because their products are necessary only for adaptation to different environments. Thus we have tried to create S. pombe mutants that are dedicated to heterologous protein production by deleting as many non-essential genes as possible. Putative essential genes were mapped using the genome information of S. pombe. The transcriptome of gene disruptants was analysed using microarrays and, using this system, a new promoter was identified. The method (called the Latour method) has been developed to delete efficiently a large region from the chromosome, resulting in the establishment of mutant strains lacking approx. 500 kb of genetic material. New experimental strains auxotrophic for six nutrients were established that were conveniently used for co-expression of proteins using multiple plasmids. An efficient transformation method has also been developed that is useful for investigating heterologous protein production in a variety of strains. Incidentally, in heterologous protein production systems, products are often degraded, leading to a decline in production efficiency. Thus, to examine heterologous protein production, we created 52 S. pombe mutant strains in each of which a single protease gene was destroyed. We also successfully constructed strains in which multiple protease genes were disrupted. As a result, it was shown that the production of a model protein, human growth hormone, was increased in this strain. Furthermore, we obtained many strains that lacked genes related to glucose metabolism, intracellular transport or biosynthesis of sugar chains. The present minireview covers the results of functional analysis of these strains. By preparing strains in which large chromosomal regions have been deleted and then combining strains defective in various functional genes, the establishment of effective hosts will become possible.","authors":"Giga-Hama Y, Tohda H, Takegawa K, Kumagai H","authors_abbrev":"Giga-Hama Y et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-02-16","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16710300","title":"Sws1 is a conserved regulator of homologous recombination in eukaryotic cells.","citation":"EMBO J 2006 Jun 07;25(11):2564-74","abstract":"Rad52-dependent homologous recombination (HR) is regulated by the antirecombinase activities of Srs2 and Rqh1/Sgs1 DNA helicases in fission yeast and budding yeast. Functional analysis of Srs2 in Schizosaccharomyces pombe led us to the discovery of Sws1, a novel HR protein with a SWIM-type Zn finger. Inactivation of Sws1 suppresses the genotoxic sensitivity of srs2Delta and rqh1Delta mutants and rescues the inviability of srs2Delta rqh1Delta cells. Sws1 functions at an early step of recombination in a pro-recombinogenic complex with Rlp1 and Rdl1, two RecA-like proteins that are most closely related to the human Rad51 paralogs XRCC2 and RAD51D, respectively. This finding indicates that the XRCC2-RAD51D complex is conserved in lower eukaryotes. A SWS1 homolog exists in human cells. It associates with RAD51D and ablating its expression reduces the number of RAD51 foci. These studies unveil a conserved pathway for the initiation and control of HR in eukaryotic cells.","authors":"Martín V, Chahwan C, Gao H, Blais V, Wohlschlegel J, Yates JR, McGowan CH, Russell P","authors_abbrev":"Martín V et al.","pubmed_publication_date":"07 Jun 2006","pubmed_entrez_date":"2006-05-20","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1685.11","SPAC17H9.03c","SPCC4G3.05c","SPAC4H3.05","SPBC11B10.06","SPAC2G11.12","SPBC216.06c","SPAC688.06c","SPBC30D10.04","SPAP27G11.15"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:16233628","title":"Characterization of two fructosyl-amino acid oxidase homologs of Schizosaccharomyces pombe.","citation":"J Biosci Bioeng 2004;97(4):278-80","abstract":"Two putative fructosyl-amino acid oxidase genes, FAP1 and FAP2, found in the Schizosaccharomyces pombe genome were cloned and expressed. Both of the gene products (Fap1 and Fap2) were flavoproteins and have no activity for fructosyl-amino acids. It was suggested that Fap1 and Fap2 are an L-pipecolic acid oxidase and L-saccharopine oxidase, respectively.","authors":"Yoshida N, Akazawa S, Katsuragi T, Tani Y","authors_abbrev":"Yoshida N et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2005-10-20","publication_year":"2004","canto_session_key":"0389ccc60bc739bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-08-06 08:11:31","canto_approved_date":"2026-03-25 19:29:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 08:42:46","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC139.04c","SPBC354.15"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-06"},{"uniquename":"EMBL:AU007272","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7520368","title":"S. pombe mei2+ encodes an RNA-binding protein essential for premeiotic DNA synthesis and meiosis I, which cooperates with a novel RNA species meiRNA.","citation":"Cell 1994 Aug 12;78(3):487-98","abstract":"The molecular controls over meiosis are poorly understood compared with those over mitosis. Here, we show that S. pombe mei2, which is essential for the initiation of premeiotic DNA synthesis, encodes an RNA-binding protein. A temperature-sensitive mei2 mutant performs premeiotic DNA synthesis but does not undergo meiotic divisions, suggesting that Mei2 is required also for meiosis I. A novel, polyadenylated RNA species (meiRNA), which suppresses this temperature-sensitive defect if overexpressed, specifically binds to Mei2 both in vivo and in vitro. Cells without meiRNA perform premeiotic DNA synthesis but cannot undergo meiosis I. Mutations that apparently block the RNA binding ability of Mei2 inhibit premeiotic DNA synthesis. Mei2 is thus likely to couple with another RNA species to promote premeiotic DNA synthesis.","authors":"Watanabe Y, Yamamoto M","authors_abbrev":"Watanabe Y et al.","pubmed_publication_date":"12 Aug 1994","pubmed_entrez_date":"1994-08-12","publication_year":"1994","canto_session_key":"33f8616f21c52155","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-26 17:10:25","canto_approved_date":"2024-03-27 06:40:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-07 16:19:06","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.103","SPAC27D7.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-07-26"},{"uniquename":"PMID:31564494","title":"Single-Turnover Activation of Arp2/3 Complex by Dip1 May Balance Nucleation of Linear versus Branched Actin Filaments.","citation":"Curr Biol 2019 Oct 07;29(19):3331-3338.e7","abstract":"Arp2/3 complex nucleates branched actin filaments important for cellular motility, endocytosis, meiosis, and cellular differentiation [1-4]. Wiskott-Aldrich syndrome proteins (WASPs), the prototypical Arp2/3 complex activators, activate Arp2/3 complex only once it is bound to the side of an actin filament [5, 6]. This ensures WASP-activated Arp2/3 complex only nucleates branched actin filaments but means branched actin networks must be seeded with an initial preformed filament. Dip1 and other WISH/DIP/SPIN90 family proteins activate Arp2/3 complex without preformed filaments [7], creating seed filaments that activate WASP-bound Arp2/3 complex [8]. Importantly, Dip1-mediated activation of Arp2/3 complex creates linear filaments instead of branches [7]. Cells may therefore need to limit Dip1 activity relative to WASP to preserve the dendritic nature of actin networks, although it is unclear whether such regulatory mechanisms exist. Here, we use total internal reflection fluorescence (TIRF) microscopy to show that Dip1 causes actin assembled with WASP and Arp2/3 complex to form disconnected networks with many linear filaments rather than highly branched arrays. We discover a key biochemical difference between Dip1 and WASP that may limit linear filament nucleation in cells; although WASP must be released for nucleation, Dip1 stays associated with Arp2/3 complex on the pointed ends of nucleated actin filaments, so Dip1 is consumed in the reaction. Using live-cell imaging of fission yeast, we provide evidence that Dip1 is a single-turnover activator of Arp2/3 complex in vivo, revealing a mechanism by which Dip1 can initiate branched actin networks at endocytic sites without disrupting their branched architectures.","doi":"10.1016/j.cub.2019.08.023","authors":"Balzer CJ, Wagner AR, Helgeson LA, Nolen BJ","authors_abbrev":"Balzer CJ et al.","pubmed_publication_date":"07 Oct 2019","pubmed_entrez_date":"2019-10-01","publication_year":"2019","canto_session_key":"741edb424fb306b5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-10-02 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC24C6.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37683616","title":"The difference is in the details: Structural and mechanistic variations in the LAMTOR-Gtr/Rag module.","citation":"Structure 2023 Sep 07;31(9):1010-1012","abstract":"In this issue of Structure, Tettoni et al. present the structure and biochemical characterization of the fission yeast LAMTOR-Gtr complex, which mediates nutrient-dependent control of cell growth. The study reveals specific differences to the homologous human LAMTOR-Rag complex that might represent means of evolutionary adaptation.","doi":"10.1016/j.str.2023.08.003","authors":"Titze S, Kümmel D","authors_abbrev":"Titze S et al.","pubmed_publication_date":"07 Sep 2023","pubmed_entrez_date":"2023-09-08","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-09-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41779599","title":"A CROSS-SPECIES ANALYSIS OF CELL WALL MECHANOSENSORS.","citation":"Mol Biol Cell 2026 Mar 04;:mbcE25110564","abstract":"The Cell Wall (CW) protects fungal cells from various challenges making its integrity essential for cell survival. CW integrity is monitored by transmembrane sensors that activate effectors to promote CW synthesis in response to injuries. Sensors of the WSC family are found in most fungi, and share a conserved architecture, with a cytoplasmic tail, a single transmembrane domain and a long Serine Threonine Rich domain (STR) prolonged by a WSC domain, both embedded in the CW. These extracellular domains promote force detection in the CW, sensor clustering and cell survival. Interestingly, Wsc sensors exhibit variations in domain sequence and size among fungal species. To understand how these variations impact force detection, we expressed Wsc sensors taken from  S. cerevisiae  and  C. albicans , in the fission yeast  S. pombe . Remarkably, we found that a subset of these foreign sensors cluster at sites of CW compression, but that others failed, suggesting divergences in mechanosensing abilities. By swapping sensor domains, we demonstrate that both the cytoplasmic tail and STR domain influence sensor re-localization to sites of CW compression. These findings reveal a high level of functional plasticity in fungal sensors, and identify tuneable modules that may regulate mechanosensing of various CWs.","doi":"10.1091/mbc.E25-11-0564","authors":"Municio-Diaz C, Minc N","authors_abbrev":"Municio-Diaz C et al.","pubmed_publication_date":"04 Mar 2026","pubmed_entrez_date":"2026-03-04","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-05 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30110882","title":"The Unfolded Protein Response Pathway in the Yeast  Kluyveromyces lactis . A Comparative View among Yeast Species.","citation":"Cells 2018 Aug 14;7(8)","abstract":"Eukaryotic cells have evolved signalling pathways that allow adaptation to harmful conditions that disrupt endoplasmic reticulum (ER) homeostasis. When the function of the ER is compromised in a condition known as ER stress, the cell triggers the unfolded protein response (UPR) in order to restore ER homeostasis. Accumulation of misfolded proteins due to stress conditions activates the UPR pathway. In mammalian cells, the UPR is composed of three branches, each containing an ER sensor (PERK, ATF6 and IRE1). However, in yeast species, the only sensor present is the inositol-requiring enzyme Ire1. To cope with unfolded protein accumulation, Ire1 triggers either a transcriptional response mediated by a transcriptional factor that belongs to the bZIP transcription factor family or an mRNA degradation process. In this review, we address the current knowledge of the UPR pathway in several yeast species:  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe ,  Candida glabrata ,  Cryptococcus neoformans,  and  Candida albicans . We also include unpublished data on the UPR pathway of the budding yeast  Kluyveromyces lactis . We describe the basic components of the UPR pathway along with similarities and differences in the UPR mechanism that are present in these yeast species.","doi":"10.3390/cells7080106","authors":"Hernández-Elvira M, Torres-Quiroz F, Escamilla-Ayala A, Domínguez-Martin E, Escalante R, Kawasaki L, Ongay-Larios L, Coria R","authors_abbrev":"Hernández-Elvira M et al.","pubmed_publication_date":"14 Aug 2018","pubmed_entrez_date":"2018-08-17","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-08-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC167.01","SPBC725.04"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:9322754","title":"Gene organization and protein sequence of the small subunits of Schizosaccharomyces pombe RNA polymerase II.","citation":"Gene 1997 Sep 01;196(1-2):165-74","abstract":"RNA polymerase II purified from the fission yeast Schizosaccharomyces pombe contains 10 different species of polypeptides. Previously, we cloned and sequenced both cDNA and the genes encoding the four large subunits, Rpb1, Rpb2, Rpb3 and Rpb5. Later, other groups isolated the genes for Rpb6 and Rpb12 and cDNA for Rpb10. Here, we cloned both cDNA and the genes encoding four small subunits, Rpb7, Rpb8, Rpb10 and Rpb11. These genes were found to encode Rpb7, Rpb8, Rpb10 and Rpb11 consisting of 172 (19,103 Da), 125 (14,300 Da), 71 (8276 Da) and 123 (14,127 Da) amino acid residues, respectively. All these four subunits are homologous to the corresponding subunits of Saccharomyces cerevisiae RNA polymerase II. The rpb7 gene contains one intron, whereas the rpb8, rpb10 and rpb11 genes contain two introns. Taken altogether, the gene organization and the predicted protein sequence have been determined for all 10 subunits of the S. pombe RNA polymerase II.","authors":"Sakurai H, Ishihama A","authors_abbrev":"Sakurai H et al.","pubmed_publication_date":"01 Sep 1997","pubmed_entrez_date":"1997-10-10","publication_year":"1997","canto_session_key":"118f6de7d1f90a66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-06-12 13:43:17","canto_approved_date":"2018-06-12 13:43:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 05:55:05","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1020.04c","SPAC23C4.15","SPBC19C2.03","SPCC1442.10c","SPAC23G3.01","SPACUNK4.06c","SPBC28F2.12","SPAC3A12.07","SPAC1B3.12c","SPBC14C8.12"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2018-06-12"},{"uniquename":"PMID:9693363","title":"The role of the Schizosaccharomyces pombe gar2 protein in nucleolar structure and function depends on the concerted action of its highly charged N terminus and its RNA-binding domains.","citation":"Mol Biol Cell 1998 Aug;9(8):2011-23","abstract":"Nonribosomal nucleolar protein gar2 is required for 18S rRNA and 40S ribosomal subunit production in Schizosaccharomyces pombe. We have investigated the consequences of the absence of each structural domain of gar2 on cell growth, 18S rRNA production, and nucleolar structure. Deletion of gar2 RNA-binding domains (RBDs) causes stronger inhibition of growth and 18S rRNA accumulation than the absence of the whole protein, suggesting that other factors may be titrated by its remaining N-terminal basic/acidic serine-rich domain. These drastic functional defects correlate with striking nucleolar hypertrophy. Point mutations in the conserved RNP1 motifs of gar2 RBDs supposed to inhibit RNA-protein interactions are sufficient to induce severe nucleolar modifications but only in the presence of the N-terminal domain of the protein. Gar2 and its mutants also distribute differently in glycerol gradients: gar2 lacking its RBDs is found either free or assembled into significantly larger complexes than the wild-type protein. We propose that gar2 helps the assembly on rRNA of factors necessary for 40S subunit synthesis by providing a physical link between them. These factors may be recruited by the N-terminal domain of gar2 and may not be released if interaction of gar2 with rRNA is impaired.","authors":"Sicard H, Faubladier M, Noaillac-Depeyre J, Léger-Silvestre I, Gas N, Caizergues-Ferrer M","authors_abbrev":"Sicard H et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-08-07","publication_year":"1998","canto_session_key":"739c64f329b534e9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-22 08:10:26","canto_approved_date":"2023-01-06 13:52:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-19 13:52:53","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC140.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-09-22"},{"uniquename":"PMID:26477565","title":"Evolution and structural organization of the mitochondrial contact site (MICOS) complex and the mitochondrial intermembrane space bridging (MIB) complex.","citation":"Biochim Biophys Acta 2016 Jan;1863(1):91-101","abstract":"We have analyzed the distribution of mitochondrial contact site and cristae organizing system (MICOS) complex proteins and mitochondrial intermembrane space bridging complex (MIB) proteins over (sub)complexes and over species. The MICOS proteins are associated with the formation and maintenance of mitochondrial cristae. Indeed, the presence of MICOS genes in genomes correlates well with the presence of cristae: all cristae containing species have at least one MICOS gene and cristae-less species have none. Mic10 is the most widespread MICOS gene, while Mic60 appears be the oldest one, as it originates in the ancestors of mitochondria, the proteobacteria. In proteobacteria the gene occurs in clusters with genes involved in heme synthesis while the protein has been observed in intracellular membranes of the alphaproteobacterium Rhodobacter sphaeroides. In contrast, Mic23 and Mic27 appear to be the youngest MICOS proteins, as they only occur in opisthokonts. The remaining MICOS proteins, Mic10, Mic19, Mic25 and Mic12, the latter we show to be orthologous to human C19orf70/QIL1, trace back to the root of the eukaryotes. Of the remaining MIB proteins, also DNAJC11 shows a high correlation with the presence of cristae. In mitochondrial protein complexome profiles, the MIB complex occurs as a defined complex and as separate subcomplexes, potentially reflecting various assembly stages. We find three main forms of the complex: A) The MICOS complex, containing all the MICOS proteins, B) a membrane bridging subcomplex, containing in addition SAMM50, MTX2 and the previously uncharacterized MTX3, and C) the complete MIB complex containing in addition DNAJC11 and MTX1.","doi":"10.1016/j.bbamcr.2015.10.009","authors":"Huynen MA, Mühlmeister M, Gotthardt K, Guerrero-Castillo S, Brandt U","authors_abbrev":"Huynen MA et al.","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2015-10-20","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:21906","SPBC25H2.09","HGNC:28184"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU012921","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8290356","title":"The fission yeast rad22 gene, having a function in mating-type switching and repair of DNA damages, encodes a protein homolog to Rad52 of Saccharomyces cerevisiae.","citation":"Nucleic Acids Res 1993 Dec 25;21(25):5940-4","abstract":"The gene rad22 of the fission yeast Schizosaccharomyces pombe has a function in DNA repair and mating-type switching. We have cloned the rad22 gene from a genomic gene bank by functional complementation of the switching defect. An open reading frame coding for a putative protein of 469 amino acids was found by sequence analyses. The rad22 gene contains no intron. A region of 126 amino acids in the N-terminal half of the Rad22 protein has significant homologies (56% identity and 36% similarity) to the Rad52 protein of Saccharomyces cerevisiae. A rad22 disruption strain was constructed which seems to be inviable in a homothallic background. Southern blot analyses have shown that the rad22-67 mutant frequently gives rise to deletions in the mating-type region. These data indicate that the Rad22 protein has a function in the repair of DNA double-strand breaks.","authors":"Ostermann K, Lorentz A, Schmidt H","authors_abbrev":"Ostermann K et al.","pubmed_publication_date":"25 Dec 1993","pubmed_entrez_date":"1993-12-25","publication_year":"1993","canto_session_key":"8f130ccba2456b85","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-02 11:53:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-15 11:54:31","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-15"},{"uniquename":"PMID:26804021","title":"Shugoshin forms a specialized chromatin domain at subtelomeres that regulates transcription and replication timing.","citation":"Nat Commun 2016 Jan 25;7:10393","abstract":"A chromosome is composed of structurally and functionally distinct domains. However, the molecular mechanisms underlying the formation of chromatin structure and the function of subtelomeres, the telomere-adjacent regions, remain obscure. Here we report the roles of the conserved centromeric protein Shugoshin 2 (Sgo2) in defining chromatin structure and functions of the subtelomeres in the fission yeast Schizosaccharomyces pombe. We show that Sgo2 localizes at the subtelomeres preferentially during G2 phase and is essential for the formation of a highly condensed subtelomeric chromatin body 'knob'. Furthermore, the absence of Sgo2 leads to the derepression of the subtelomeric genes and premature DNA replication at the subtelomeric late origins. Thus, the subtelomeric specialized chromatin domain organized by Sgo2 represses both transcription and replication to ensure proper gene expression and replication timing.","doi":"10.1038/ncomms10393","authors":"Tashiro S, Handa T, Matsuda A, Ban T, Takigawa T, Miyasato K, Ishii K, Kugou K, Ohta K, Hiraoka Y, Masukata H, Kanoh J","authors_abbrev":"Tashiro S et al.","pubmed_publication_date":"25 Jan 2016","pubmed_entrez_date":"2016-01-26","publication_year":"2016","canto_session_key":"1dadbd005c6e53cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junko Kanoh","canto_first_approved_date":"2017-10-30 12:01:28","canto_approved_date":"2025-12-23 12:31:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-20 02:36:41","canto_added_date":"2016-01-27 01:15:31","annotation_curators":[{"name":"Junko Kanoh","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPBC428.08c","SPCC962.02c","SPAC869.07c","SPCC188.13c","SPAC19G12.06c","SPAC186.01","SPAC23C4.03","SPBC725.12","SPAC16A10.07c","SPAC664.01c","SPBC26H8.07c","SPCC1322.12c","SPAC29B12.02c","SPAC1F8.01","SPBPB21E7.07","SPBPB2B2.13","SPCC622.08c","SPAC15A10.15","SPBC106.01","SPBC336.15","SPCC320.13c"],"gene_count":22,"ltp_gene_count":7,"approved_date":"2017-10-30"},{"uniquename":"PMID:4821071","title":"Biosynthesis of branched-chain amino acids in Schizosaccharomyces pombe: regulation of the enzymes involved in isoleucine, valine, and leucine synthesis.","citation":"Can J Biochem 1974 Jan;52(1):51-9","abstract":"","authors":"McDonald RA, Satyanarayana T, Kaplan JG","authors_abbrev":"McDonald RA et al.","pubmed_publication_date":"Jan 1974","pubmed_entrez_date":"1974-01-01","publication_year":"1974","canto_session_key":"b95bc9d658c77529","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-20 14:54:45","canto_approved_date":"2020-01-17 19:31:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-22 17:22:22","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-20"},{"uniquename":"PMID:12526757","title":"Chromatin silencing: RNA in the driving seat.","citation":"Curr Biol 2003 Jan 08;13(1):R13-5","abstract":"Recent studies have provided major new insights into the mechanism by which eukaryotic organisms initiate heterochromatin formation. Surprisingly, RNA appears to be a central component of the chromatin silencing machinery.","authors":"Stevenson DS, Jarvis P","authors_abbrev":"Stevenson DS et al.","pubmed_publication_date":"08 Jan 2003","pubmed_entrez_date":"2003-01-16","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38830842","title":"Fate of telomere entanglements is dictated by the timing of anaphase midregion nuclear envelope breakdown.","citation":"Nat Commun 2024 Jun 03;15(1):4707","abstract":"Persisting replication intermediates can confer mitotic catastrophe. Loss of the fission yeast telomere protein Taz1 (ortholog of mammalian TRF1/TRF2) causes telomeric replication fork (RF) stalling and consequently, telomere entanglements that stretch between segregating mitotic chromosomes. At ≤20 °C, these entanglements fail to resolve, resulting in lethality. Rif1, a conserved DNA replication/repair protein, hinders the resolution of telomere entanglements without affecting their formation. At mitosis, local nuclear envelope (NE) breakdown occurs in the cell's midregion. Here we demonstrate that entanglement resolution occurs in the cytoplasm following this NE breakdown. However, in response to taz1Δ telomeric entanglements, Rif1 delays midregion NE breakdown at ≤20 °C, in turn disfavoring entanglement resolution. Moreover, Rif1 overexpression in an otherwise wild-type setting causes cold-specific NE defects and lethality, which are rescued by membrane fluidization. Hence, NE properties confer the cold-specificity of taz1Δ lethality, which stems from postponement of NE breakdown. We propose that such postponement promotes clearance of simple stalled RFs, but resolution of complex entanglements (involving strand invasion between nonsister telomeres) requires rapid exposure to the cytoplasm.","doi":"10.1038/s41467-024-48382-2","authors":"Nageshan RK, Ortega R, Krogan N, Cooper JP","authors_abbrev":"Nageshan RK et al.","pubmed_publication_date":"03 Jun 2024","pubmed_entrez_date":"2024-06-03","publication_year":"2024","canto_session_key":"bb50be514603d369","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-06-04 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34680098","title":"Fission Yeast TORC2 Signaling Pathway Ensures Cell Proliferation under Glucose-Limited, Nitrogen-Replete Conditions.","citation":"Biomolecules 2021 Oct 06;11(10)","abstract":"Target of rapamycin (TOR) kinases form two distinct complexes, TORC1 and TORC2, which are evolutionarily conserved among eukaryotes. These complexes control intracellular biochemical processes in response to changes in extracellular nutrient conditions. Previous studies using the fission yeast,  Schizosaccharomyces pombe , showed that the TORC2 signaling pathway, which is essential for cell proliferation under glucose-limited conditions, ensures cell-surface localization of a high-affinity hexose transporter, Ght5, by downregulating its endocytosis. The TORC2 signaling pathway retains Ght5 on the cell surface, depending on the presence of nitrogen sources in medium. Ght5 is transported to vacuoles upon nitrogen starvation. In this review, we discuss the molecular mechanisms underlying this regulation to cope with nutritional stress, a response which may be conserved from yeasts to mammals.","doi":"10.3390/biom11101465","authors":"Toyoda Y, Saitoh S","authors_abbrev":"Toyoda Y et al.","pubmed_publication_date":"06 Oct 2021","pubmed_entrez_date":"2021-10-23","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-10-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8387356","title":"Isolation and characterization of the fission yeast protein phosphatase gene ppe1+ involved in cell shape control and mitosis.","citation":"Mol Biol Cell 1993 Mar;4(3):303-13","abstract":"We isolated a fission yeast putative protein serine/threonine phosphatase gene designated ppe1+ by hybridization. The predicted amino acid sequence is similar to those of the fission yeast ppa2 (53% identity) and dis2 (39%) phosphatases, and highly similar to those of the budding yeast SIT4 (72%), Drosophila PPV (68%) and rabbit PPX (61%) phosphatases. Antibodies against ppe1 protein identified a 37-kd polypeptide in fission yeast. A gene disruption (designated delta ppe1) caused cold-sensitive lethality and short, pear-shaped cells. These phenotypes were fully suppressed by a plasmid carrying ppe1+. Three classes of multicopy suppressor genes for delta ppe1 were identified as follows: 1) ppa1+ and ppa2+ encoding type 2A-like phosphatases, 2) mitotically essential dis3+ similar to the budding yeast SSD1/SRK1, a suppressor for sit4, and 3) pck1+ coding for a protein kinase C-like kinase. Consistently, the budding yeast SIT4 gene was also a multicopy suppressor for delta ppe1. Phosphatase ppe1 may play a role in cell morphogenesis and mitosis by either regulating or being regulated by these multicopy suppressor gene products. Consistent with this hypothesis, double mutants ppe1-ppa2 and ppe1-pck1 are lethal at the permissive temperature.","authors":"Shimanuki M, Kinoshita N, Ohkura H, Yoshida T, Toda T, Yanagida M","authors_abbrev":"Shimanuki M et al.","pubmed_publication_date":"Mar 1993","pubmed_entrez_date":"1993-03-01","publication_year":"1993","canto_session_key":"b6deaed8ee570a51","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-16 15:56:09","canto_approved_date":"2023-10-29 21:56:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 15:02:39","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16H5.07c","SPBC26H8.10","SPAC823.15","SPCC1739.12","SPCC31H12.05c","SPAC17G8.14c","SPBC776.02c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-11-16"},{"uniquename":"PMID:11380623","title":"Fission yeast homologues of the B' subunit of protein phosphatase 2A: multiple roles in mitotic cell division and functional interaction with calcineurin.","citation":"Genes Cells 2001 May;6(5):455-73","abstract":"Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase distributed in eukaryotes from yeast to human, and plays pivotal roles in diverse cellular functions such as metabolism, cell cycle progression, gene expression and development. PP2A holoenzyme is a heterodimer of a catalytic subunit C and a regulatory subunit A, or a heterotrimer of C, A and a variable regulatory subunit consisting of three families; B, B', and PR72. Specific functions for each variable subunit are not well understood.\nTwo fission yeast genes pbp1+ and pbp2+ homologous to the regulatory subunit B' were isolated. Physical in vivo interaction of the gene products with the catalytic subunit was demonstrated. A double disruption haploid mutant (Deltapbp1Deltapbp2) showed growth defect, cell shape and size abnormality, multiseptation and anucleated cell formation due to abnormality in septum positioning. These phenotypes were suppressed by human B' cDNA, indicating the striking conservation of the B' function from yeast to human. Over-expression of fission yeast B' led to growth defects, a loss of cell shape polarity, septal abnormality and anucleated cell formation. Deltapbp1Deltapbp2 and pbp1 null haploids were hypersensitive to calcineurin inhibitors, cyclosporin A and FK506, with which the mutants underwent arrest at post-anaphase and cell lysis. Double disruption of calcineurin and pbp1+, but not pbp2+, genes led to synthetic lethality.\nThe fission yeast B' subunit of PP2A plays critical roles in cell shape control and septum formation, and shares essential functions with calcineurin for viability, possibly through their roles in cytokinesis and cell wall integrity.","authors":"Tanabe O, Hirata D, Usui H, Nishito Y, Miyakawa T, Igarashi K, Takeda M","authors_abbrev":"Tanabe O et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-06-26","publication_year":"2001","canto_session_key":"2d667709aaa942a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-08-26 10:56:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-19 16:55:27","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":65,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPAC6F12.12","SPCC188.02","SPBC16H5.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-01-19"},{"uniquename":"PMID:3921260","title":"Concerted evolution of tRNA genes: intergenic conversion among three unlinked serine tRNA genes in S. pombe.","citation":"Cell 1985 Apr;40(4):879-86","abstract":"In many cases the multiple genes coding for one specific tRNA are dispersed throughout the genome. The members of such a gene family nevertheless maintain a common nucleotide sequence during evolution. A major mechanism contributing to this concerted evolution is intergenic conversion. Here we show that it occurs between three tRNA genes of related sequence residing on different chromosomes of Schizosaccharomyces pombe. Sequence analysis of converted genes indicates that blocks of a minimal length of 18-33 bp and of a maximal length of 190 bp can be transferred from one gene to the other. During meiosis the frequency of these transfers lies in the order of 10(-5) per progeny spore. Information transfer between any two members of the gene family occurs in both directions.","authors":"Amstutz H, Munz P, Heyer WD, Leupoid U, Kohli J","authors_abbrev":"Amstutz H et al.","pubmed_publication_date":"Apr 1985","pubmed_entrez_date":"1985-04-01","publication_year":"1985","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24914559","title":"Mechanism of cytokinetic contractile ring constriction in fission yeast.","citation":"Dev Cell 2014 Jun 09;29(5):547-561","abstract":"Cytokinesis involves constriction of a contractile actomyosin ring. The mechanisms generating ring tension and setting the constriction rate remain unknown because the organization of the ring is poorly characterized, its tension was rarely measured, and constriction is coupled to other processes. To isolate ring mechanisms, we studied fission yeast protoplasts, in which constriction occurs without the cell wall. Exploiting the absence of cell wall and actin cortex, we measured ring tension and imaged ring organization, which was dynamic and disordered. Computer simulations based on the amounts and biochemical properties of the key proteins showed that they spontaneously self-organize into a tension-generating bundle. Together with rapid component turnover, the self-organization mechanism continuously reassembles and remodels the constricting ring. Ring constriction depended on cell shape, revealing that the ring operates close to conditions of isometric tension. Thus, the fission yeast ring sets its own tension, but other processes set the constriction rate.","doi":"10.1016/j.devcel.2014.04.021","authors":"Stachowiak MR, Laplante C, Chin HF, Guirao B, Karatekin E, Pollard TD, O'Shaughnessy B","authors_abbrev":"Stachowiak MR et al.","pubmed_publication_date":"09 Jun 2014","pubmed_entrez_date":"2014-06-11","publication_year":"2014","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14711417","title":"A potential tension-sensing mechanism that ensures timely anaphase onset upon metaphase spindle orientation.","citation":"Curr Biol 2004 Jan 06;14(1):69-74","abstract":"The spindle orientation checkpoint (SOC) in fission yeast has been proposed to delay metaphase-to-anaphase transition when the spindle poles are misaligned with respect to the long axis of the cell. This checkpoint is activated in the absence of either an actomyosin division ring or astral microtubules. Although the SOC could be overridden in the absence of the transcription factor Atf1p, its mechanistic nature remained unclear. Here, we show that the SOC-triggered metaphase delay depends on a subset of the spindle assembly checkpoint (SAC) components Mph1p and Bub1p. Based on this finding and a detailed imaging of the spindle orientation process, we hypothesized that the spindle pole might contain proteins capable of sensing the achievement of spindle alignment. We identified the kendrin-like spindle pole body resident Pcp1p as a candidate molecule. A targeted mutation in its central domain specifically triggered the SOC in spite of the presence of oriented spindles, causing a metaphase delay that could be relieved in the absence of Mph1p, Bub1p, and Atf1p. Thus, Pcp1p might provide a link between the mechanical process of spindle alignment and the signal transduction that initiates anaphase.","authors":"Rajagopalan S, Bimbo A, Balasubramanian MK, Oliferenko S","authors_abbrev":"Rajagopalan S et al.","pubmed_publication_date":"06 Jan 2004","pubmed_entrez_date":"2004-01-09","publication_year":"2004","canto_session_key":"efa5f3791b35925f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-06-21 12:00:49","canto_approved_date":"2018-06-21 12:00:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-21 11:59:36","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6G9.06c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2018-06-21"},{"uniquename":"PMID:7616961","title":"Rescue of the fission yeast snRNA synthesis mutant snm1 by overexpression of the double-strand-specific Pac1 ribonuclease.","citation":"Mol Gen Genet 1995 Jun 25;247(6):698-708","abstract":"The Schizosaccharomyces pombe temperature-sensitive mutant snm1 maintains reduced steady-state quantities of the spliceosomal small nuclear RNAs (snRNAs) and the RNA subunit of the tRNA processing enzyme RNase P. We report here the isolation of the pac1+ gene as a multi-copy suppressor of snm1. The pac1+ gene was previously identified as a suppressor of the ran1 mutant and by its ability to cause sterility when overexpressed. The pac1+ gene encodes a double-strand-specific ribonuclease that is similar to RNase III, an RNA processing and turnover enzyme in Escherichia coli. To investigate the essential structural features of the Pac1 RNase, we altered the pac1+ gene by deletion and point mutation and tested the mutant constructs for their ability to complement the snm1 and ran1 mutants and to cause sterility. These experiments identified four essential amino acids in the Pac1 sequence: glycine 178, glutamic acid 251, and valines 346 and 347. These amino acids are conserved in all RNase III-like proteins. The glycine and glutamic acid residues were previously identified as essential for E. coli RNase III activity. The valines are conserved in an element found in a family of double-stranded RNA binding proteins. Our results support the hypothesis that the Pac1 RNase is an RNase III homolog and suggest a role for the Pac1 RNase in snRNA metabolism.","authors":"Rotondo G, Gillespie M, Frendewey D","authors_abbrev":"Rotondo G et al.","pubmed_publication_date":"25 Jun 1995","pubmed_entrez_date":"1995-06-25","publication_year":"1995","canto_session_key":"78374d69fcccdd6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-01-18 09:40:19","canto_approved_date":"2026-01-29 17:17:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-29 10:17:58","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.03","SPBC19C2.05","SPSNRNA.04","SPSNRNA.02","SPBC119.11c"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2014-01-18"},{"uniquename":"PMID:8167025","title":"Genetic and biochemical approaches to spindle function and chromosome segregation in eukaryotic microorganisms.","citation":"Curr Opin Cell Biol 1994 Feb;6(1):50-4","abstract":"The past year saw the molecular characterization of components of the Saccharomyces cerevisiae kinetochore and spindle pole body. In Schizosaccharomyces pombe, new cytological methods have been described for detection of centromeric DNA by light microscopy and probable kinetochores by electron microscopy.","authors":"Kilmartin JV","authors_abbrev":"Kilmartin JV","pubmed_publication_date":"Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12898217","title":"MCB-mediated regulation of cell cycle-specific cdc22+ transcription in fission yeast.","citation":"Mol Genet Genomics 2003 Sep;269(6):765-75","abstract":"The cdc22+ gene of the fission yeast, Schizosaccharomyces pombe, encodes the large subunit of ribonucleotide reductase, and is periodically expressed during the mitotic cell cycle, transcript abundance reaching a maximum at the G1-S boundary. This regulation of expression is controlled by a transcription factor complex called DSC1, which binds to MCB motifs (ACGCGT) present in the promoter of cdc22+. cdc22+ has a complex pattern of MCBs, including two clusters of four motifs each, one of which is located within the transcribed region. We show that both clusters of MCBs contribute to the regulation of cdc22+ expression during the cell cycle, each having a different role. The MCB cluster within the transcribed region has the major role in regulating cdc22+, as its removal results in loss of transcription. The upstream cluster, instead, controls cell cycle-specific transcription through a negative function, as its removal results in expression of cdc22+ throughout the cell cycle. Both MCB clusters bind DSC1. We show that the interaction of DSC1 with the MCB cluster within the transcribed region has a high \"on-off\" rate, suggesting a mechanism by which DSC1 could activate expression, and still allow RNA polymerase to pass during transcription. Finally, we show that both clusters are orientation-dependent in their function. The significance of these results, in the context of MCB-mediated regulation of G1-S expression in fission yeast, is discussed.","authors":"Maqbool Z, Kersey PJ, Fantes PA, McInerny CJ","authors_abbrev":"Maqbool Z et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-08-05","publication_year":"2003","canto_session_key":"f661418b8c3d3354","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-06-05 15:48:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-06-05 15:48:00","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAC1F7.05","SPBC336.12c","SPCC1442.01","SPBC428.18","SPAC17H9.20","SPAC17H9.19c"],"gene_count":7,"ltp_gene_count":1,"approved_date":"2015-06-05"},{"uniquename":"PMID:38197775","title":"A role for the carbon source of the cell and protein kinase A in regulating the S. pombe septation initiation network.","citation":"J Cell Sci 2024 Jan 01;137(1)","abstract":"The septation initiation network (SIN) is a conserved signal transduction network, which is important for cytokinesis in Schizosaccharomyces pombe. The SIN component Etd1p is required for association of some SIN proteins with the spindle pole body (SPB) during anaphase and for contractile ring formation. We show that tethering of Cdc7p or Sid1p to the SIN scaffold Cdc11p at the SPB, rescues etd1-Δ. Analysis of a suppressor of the mutant etd1-M9 revealed that SIN signalling is influenced by the carbon source of the cell. Growth on a non-fermentable carbon source glycerol reduces the requirement for SIN signalling but does not bypass it. The decreased need for SIN signalling is mediated largely by reduction of protein kinase A activity, and it is phenocopied by deletion of pka1 on glucose medium. We conclude that protein kinase A is an important regulator of the SIN, and that SIN signalling is regulated by the carbon source of the cell.","doi":"10.1242/jcs.261488","authors":"Uysal Özdemir Ö, Krapp A, Mangeat B, Spaltenstein M, Simanis V","authors_abbrev":"Uysal Özdemir Ö et al.","pubmed_publication_date":"01 Jan 2024","pubmed_entrez_date":"2024-01-10","publication_year":"2024","canto_session_key":"164198d48f8c6472","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-01-11 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26564949","title":"Genome-Wide Estimates of Mutation Rates and Spectrum in Schizosaccharomyces pombe Indicate CpG Sites are Highly Mutagenic Despite the Absence of DNA Methylation.","citation":"G3 (Bethesda) 2015 Nov 12;6(1):149-60","abstract":"We accumulated mutations for 1952 generations in 79 initially identical, haploid lines of the fission yeast Schizosaccharomyces pombe, and then performed whole-genome sequencing to determine the mutation rates and spectrum. We captured 696 spontaneous mutations across the 79 mutation accumulation (MA) lines. We compared the mutation spectrum and rate to a recently published equivalent experiment on the same species, and to another model ascomycetous yeast, the budding yeast Saccharomyces cerevisiae. While the two species are approximately 600 million years diverged from each other, they share similar life histories, genome size and genomic G/C content. We found that Sc. pombe and S. cerevisiae have similar mutation rates, but Sc. pombe exhibits a stronger insertion bias. Intriguingly, we observed an increased mutation rate at cytosine nucleotides, specifically CpG nucleotides, which is also seen in S. cerevisiae. However, the absence of methylation in Sc. pombe and the pattern of mutation at these sites, primarily C → A as opposed to C → T, strongly suggest that the increased mutation rate is not caused by deamination of methylated cytosines. This result implies that the high mutability of CpG dinucleotides in other species may be caused in part by a methylation-independent mechanism. Many of our findings mirror those seen in the recent study, despite the use of different passaging conditions, indicating that MA is a reliable method for estimating mutation rates and spectra.","doi":"10.1534/g3.115.022129","authors":"Behringer MG, Hall DW","authors_abbrev":"Behringer MG et al.","pubmed_publication_date":"12 Nov 2015","pubmed_entrez_date":"2015-11-14","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-11-15 01:19:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8663159","title":"Schizosaccharomyces pombe proliferating cell nuclear antigen mutations affect DNA polymerase delta processivity.","citation":"J Biol Chem 1996 Jul 05;271(27):15971-80","abstract":"We introduced nine site-directed mutations into seven conserved fission yeast proliferative cell nuclear antigen (PCNA) residues, Leu2, Asp63, Arg64, Gly69, Gln201, Glu259, and Glu260, either as single or as double mutants. Both the recombinant wild type and mutant PCNAs were able to form homotrimers in solution and to sustain growth of a null pcna strain (Deltapcna). Wild type Schizosaccharomyces pombe PCNA and PCNA proteins with mutations in Asp63, Gln201, Glu259, or Glu260 to Ala were able to stimulate DNA synthetic activity and to enhance the processivity of calf thymus DNA polymerase delta holoenzyme similar to calf thymus PCNA. Mutations of Leu2 to Val or Arg64 to Ala, either singly or as a double mutant, yielded PCNA mutant proteins that had reduced capacity in enhancing the processivity of DNA polymerase delta but showed no deficiency in stimulation of the ATPase activity of replication factor C. S. pombe Deltapcna strains sustained by these two mutant-pcna alleles had moderate defects in growth and displayed elongated phenotypes. These cells, however, were not sensitive to UV irradiation. Together, these in vitro and in vivo studies suggest that the side chains of Leu2 and Arg64 in one face of the PCNA trimer ring structure are two of the several sites involved in tethering DNA polymerase delta for processive DNA synthesis during DNA replication.","authors":"Arroyo MP, Downey KM, So AG, Wang TS","authors_abbrev":"Arroyo MP et al.","pubmed_publication_date":"05 Jul 1996","pubmed_entrez_date":"1996-07-05","publication_year":"1996","canto_session_key":"c4204412fc39e2fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-30 15:18:18","canto_approved_date":"2022-02-24 20:55:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-26 15:31:46","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_8663159_phaf.tsv"}],"genes":["SPBC16D10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-06-30"},{"uniquename":"PMID:12136004","title":"Genetic interaction between calcineurin and type 2 myosin and their involvement in the regulation of cytokinesis and chloride ion homeostasis in fission yeast.","citation":"Genetics 2002 Jul;161(3):971-81","abstract":"Calcineurin plays a critical role in Ca(2+) signaling in various cell types. In fission yeast, calcineurin is required for cytokinesis and chloride ion homeostasis. However, most of its physiological functions remain obscure. A genetic screen was performed to identify genes that share an essential function with calcineurin. We screened for mutations that confer sensitivity to the calcineurin inhibitor FK506 and to a high concentration of chloride ion and isolated a mutant, cis2-1/myp2-c2, which contains a novel allele of the myp2(+)/myo3(+) gene that encodes a type 2 myosin heavy chain. The myp2-c2 mutant showed morphological defects similar to those associated with a calcineurin deletion mutant, such as multiseptated and branched cells. Consistently, myp2-null cells were hypersensitive to chloride ion and showed the multiseptated phenotype in the presence of immunosuppressants or at high chloride concentrations. Overexpression of constitutively active calcineurin suppressed the chloride ion-sensitive growth defect and cytokinesis abnormality of the myp2-c2 mutant and myp2-null cells. Interestingly, the essential myosin light chain mutant cdc4-8 failed to grow and could not form a normal contractile ring in the presence of immunosuppressants. Furthermore, calcineurin-null cells exhibited aberrant contractile rings, suggesting impaired contraction of the rings. These results indicate that calcineurin is involved in the regulation of cytokinesis and that chloride ion homeostasis is mediated by type 2 myosin.","authors":"Fujita M, Sugiura R, Lu Y, Xu L, Xia Y, Shuntoh H, Kuno T","authors_abbrev":"Fujita M et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-07-24","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4A8.05c","SPBP4H10.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:23019579","title":"Structural evolution of the membrane-coating module of the nuclear pore complex.","citation":"Proc Natl Acad Sci U S A 2012 Oct 09;109(41):16498-503","abstract":"The coatomer module of the nuclear pore complex borders the cylinder-like nuclear pore-membrane domain of the nuclear envelope. In evolution, a single coatomer module increases in size from hetero-heptamer (Saccharomyces cerevisiae) to hetero-octamer (Schizosaccharomyces pombe) to hetero-nonamer (Metazoa). Notably, the heptamer-octamer transition proceeds through the acquisition of the nucleoporin Nup37. How Nup37 contacts the heptamer remained unknown. Using recombinant nucleoporins, we show that Sp-Nup37 specifically binds the Sp-Nup120 member of the hetero-heptamer but does not bind an Sc-Nup120 homolog. To elucidate the Nup37-Nup120 interaction at the atomic level, we carried out crystallographic analyses of Sp-Nup37 alone and in a complex with an N-terminal, ~110-kDa fragment of Sp-Nup120 comprising residues 1-950. Corroborating structural predictions, we determined that Nup37 folds into a seven-bladed β-propeller. Several disordered surface regions of the Nup37 β-propeller assume structure when bound to Sp-Nup120. The N-terminal domain of Sp-Nup120(1-950) also folds into a seven-bladed propeller with a markedly protruding 6D-7A insert and is followed by a contorted helical domain. Conspicuously, this 6D-7A insert contains an extension of 50 residues which also is highly conserved in Metazoa but is absent in Sc-Nup120. Strikingly, numerous contacts with the Nup37 β-propeller are located on this extension of the 6D-7A insert. Another contact region is situated toward the end of the helical region of Sp-Nup120(1-950). Our findings provide information about the evolution and the assembly of the coatomer module of the nuclear pore complex.","doi":"10.1073/pnas.1214557109","authors":"Liu X, Mitchell JM, Wozniak RW, Blobel G, Fan J","authors_abbrev":"Liu X et al.","pubmed_publication_date":"09 Oct 2012","pubmed_entrez_date":"2012-09-29","publication_year":"2012","canto_session_key":"d995d16b4115f8c8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-17 13:49:23","canto_approved_date":"2023-03-01 14:58:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 13:48:51","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F10.18","SPBC3B9.16c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-02-17","pdb_entries":[{"pdb_id":"4gq1","gene_chains":[{"gene_uniquename":"SPAC4F10.18","chain":"A","position":"1-391"}],"title":"Nup37 of S. pombe","entry_authors":"Liu X,Mitchell J,Wozniak R,Blobel G,Fan J","entry_authors_abbrev":"Liu X et al.","reference_uniquename":"PMID:23019579","experimental_method":"X-ray","resolution":"2.4"},{"pdb_id":"4gq2","gene_chains":[{"gene_uniquename":"SPAC4F10.18","chain":"P","position":"1-391"},{"gene_uniquename":"SPBC3B9.16c","chain":"M","position":"1-949"}],"title":"S. pombe Nup120-Nup37 complex","entry_authors":"Liu X,Mitchell J,Wozniak R,Blobel G,Fan J","entry_authors_abbrev":"Liu X et al.","reference_uniquename":"PMID:23019579","experimental_method":"X-ray","resolution":"2.4"}]},{"uniquename":"PMID:16615890","title":"Meiotic proteins bqt1 and bqt2 tether telomeres to form the bouquet arrangement of chromosomes.","citation":"Cell 2006 Apr 07;125(1):59-69","abstract":"In many organisms, meiotic chromosomes are bundled at their telomeres to form a \"bouquet\" arrangement. The bouquet formation plays an important role in homologous chromosome pairing and therefore progression of meiosis. As meiotic telomere clustering occurs in response to mating pheromone signaling in fission yeast, we looked for factors essential for bouquet formation among genes induced under mating pheromone signaling. This genome-wide search identified two proteins, Bqt1 and Bqt2, that connect telomeres to the spindle-pole body (SPB; the centrosome equivalent in fungi). Neither Bqt1 nor Bqt2 alone functions as a connector, but together the two proteins form a bridge between Rap1 (a telomere protein) and Sad1 (an SPB protein). Significantly, when both Bqt1 and Bqt2 are ectopically expressed in mitotic cells, they also form a bridge between Rap1 and Sad1. Thus, a complex including Bqt1 and Bqt2 is essential for connecting telomeres to the SPB.","authors":"Chikashige Y, Tsutsumi C, Yamane M, Okamasa K, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"07 Apr 2006","pubmed_entrez_date":"2006-04-18","publication_year":"2006","canto_session_key":"4dc7a761468f63e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-07 11:54:44","canto_approved_date":"2024-02-12 14:23:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-09 12:06:34","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":82,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_16615890_phaf.tsv"}],"genes":["SPBC28F2.07","SPAC227.06","SPBC577.05c","SPCC965.14c","SPAC6C3.05","SPAC1F8.05","SPAC1A6.06c","SPBC25B2.07c","SPAC22F8.04","SPBP8B7.04","SPAC57A10.04","SPBC1778.02","SPAC11D3.01c","SPAC8C9.16c","SPCC569.01c","SPBC1718.02","SPBC660.17c","SPBC31F10.02","SPAC1002.06c","SPBC3H7.06c","SPAC57A10.06","SPAC6F12.04","SPBC1685.01","SPAC31G5.10","SPAC17H9.18c","SPAC10F6.09c","SPAC12B10.16c","SPAC6B12.16","SPAP11E10.02c","SPBC1921.06c","SPCC622.02","SPBC660.14","SPAPB2B4.03","SPAC32A11.01","SPAC926.03","SPBC1652.01","SPCC613.11c","SPAC13G7.07","SPAC1F5.09c","SPAC11H11.03c","SPBC902.06","SPBC1347.12","SPAC22H10.07","SPAC29B12.11c","SPAC630.04c","SPCC162.04c","SPAC14C4.04","SPAC6G9.13c","SPAC458.05","SPCC162.10","SPBC23G7.17c","SPAC25A8.02","SPAP7G5.03","SPBC2G2.09c","SPAC1F5.08c","SPAC1006.04c","SPAC1002.05c","SPCC594.07c","SPAC29A4.12c","SPCC70.09c","SPBC15D4.01c","SPBC337.02c","SPAC630.05","SPAC27E2.07","SPBC29A10.14","SPAC31G5.07","SPBC1604.01","SPCC4G3.08","SPBC19C2.04c","SPCC1020.05","SPAC22F3.09c","SPCC1393.07c","SPAC806.06c","SPAC222.15","SPAC2C4.09","SPAC1556.06","SPAC13C5.03","SPAC23C4.07","SPAC458.04c","SPAC14C4.03","SPBC12D12.01","SPBC216.02","SPBC409.03","SPBC23E6.03c","SPCC306.11","SPBC29A10.02","SPBC36B7.06c","SPBC651.04"],"gene_count":88,"ltp_gene_count":85,"approved_date":"2018-03-07"},{"uniquename":"Pfam:PF02221","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB8E5.04c","HGNC:14537","HGNC:17156"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33754639","title":"Identification and structural analysis of the Schizosaccharomyces pombe SMN complex.","citation":"Nucleic Acids Res 2021 Jul 21;49(13):7207-7223","abstract":"The macromolecular SMN complex facilitates the formation of Sm-class ribonucleoproteins involved in mRNA processing (UsnRNPs). While biochemical studies have revealed key activities of the SMN complex, its structural investigation is lagging behind. Here we report on the identification and structural determination of the SMN complex from the lower eukaryote Schizosaccharomyces pombe, consisting of SMN, Gemin2, 6, 7, 8 and Sm proteins. The core of the SMN complex is formed by several copies of SMN tethered through its C-terminal alpha-helices arranged with alternating polarity. This creates a central platform onto which Gemin8 binds and recruits Gemins 6 and 7. The N-terminal parts of the SMN molecules extrude via flexible linkers from the core and enable binding of Gemin2 and Sm proteins. Our data identify the SMN complex as a multivalent hub where Sm proteins are collected in its periphery to allow their joining with UsnRNA.","doi":"10.1093/nar/gkab158","authors":"Veepaschit J, Viswanathan A, Bordonné R, Grimm C, Fischer U","authors_abbrev":"Veepaschit J et al.","pubmed_publication_date":"21 Jul 2021","pubmed_entrez_date":"2021-03-23","publication_year":"2021","canto_session_key":"fae46ef295058751","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Bordonne","canto_first_approved_date":"2021-04-13 15:03:48","canto_approved_date":"2022-03-23 18:10:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-24 15:08:03","canto_added_date":"2021-03-24 10:51:23","annotation_curators":[{"name":"Bordonne","community_curator":true,"annotation_count":32,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.02","SPSNRNA.01","SPAC2G11.08c","SPBC32F12.16","SPAC19B12.12c","SPAC4D7.15","SPSNRNA.05","HGNC:20044","HGNC:26044","SPBC16H5.15"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2021-04-13","pdb_entries":[{"pdb_id":"7bb3","gene_chains":[{"gene_uniquename":"SPAC2G11.08c","chain":"A/B","position":"2-152"}],"title":"Structure of S. pombe YG-box oligomer","entry_authors":"Veepaschit J,Grimm C,Fischer U","entry_authors_abbrev":"Veepaschit J et al.","reference_uniquename":"PMID:33754639","experimental_method":"X-ray","resolution":"2.158"}]},{"uniquename":"PMID:11359921","title":"Fission yeast Aip3p (spAip3p) is required for an alternative actin-directed polarity program.","citation":"Mol Biol Cell 2001 May;12(5):1275-91","abstract":"Aip3p is an actin-interacting protein that regulates cell polarity in budding yeast. The Schizosaccharomyces pombe-sequencing project recently led to the identification of a homologue of Aip3p that we have named spAip3p. Our results confirm that spAip3p is a true functional homologue of Aip3p. When expressed in budding yeast, spAip3p localizes similarly to Aip3p during the cell cycle and complements the cell polarity defects of an aip3Delta strain. Two-hybrid analysis shows that spAip3p interacts with actin similarly to Aip3p. In fission yeast, spAip3p localizes to both cell ends during interphase and later organizes into two rings at the site of cytokinesis. spAip3p localization to cell ends is dependent on microtubule cytoskeleton, its localization to the cell middle is dependent on actin cytoskeleton, and both patterns of localization require an operative secretory pathway. Overexpression of spAip3p disrupts the actin cytoskeleton and cell polarity, leading to morphologically aberrant cells. Fission yeast, which normally rely on the microtubule cytoskeleton to establish their polarity axis, can use the actin cytoskeleton in the absence of microtubule function to establish a new polarity axis, leading to the formation of branched cells. spAip3p localizes to, and is required for, branch formation, confirming its role in actin-directed polarized cell growth in both Schizosaccharomyces pombe and Saccharomyces cerevisiae.","authors":"Jin H, Amberg DC","authors_abbrev":"Jin H et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-22","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12415000","title":"Phosphorylation activates Chk1 and is required for checkpoint-mediated cell cycle arrest.","citation":"J Cell Sci 2002 Dec 01;115(Pt 23):4555-64","abstract":"In the fission yeast Schizosaccharomyces pombe, the protein kinase Chk1 has an essential role in transducing a delay signal to the cell cycle machinery in the presence of DNA damage. Fission yeast cells lacking the chk1 gene do not delay progression of the cell cycle in response to damage and are thus sensitive to DNA damaging agents. We have previously shown that Chk1 is phosphorylated following DNA damage induced by a variety of agents and that this is dependent on the integrity of the DNA damage checkpoint pathway, including Rad3, the ATR homolog. Through a combination of mutagenesis and phospho-specific antibodies, we have shown that serine at position 345 (S345) is phosphorylated in vivo in response to DNA damage, and that S345 phosphorylation is required for an intact checkpoint response. We have developed a kinase assay for Chk1, and have shown that basal Chk1 kinase activity is increased in response to DNA damage and that this increase, but not the basal activity, is dependent on S345. Furthermore, we show that S345 phosphorylation is required for Chk1 to associate with Rad24, a 14-3-3 protein, upon DNA damage. These results are consistent with a model whereby Chk1 phosphorylation results in increased Chk1 kinase activity that is necessary for both checkpoint delay and cellular survival following damage to the genome. These data are similar to observations made in mammalian cells and Xenopus oocyte extracts, suggesting that mechanisms leading to Chk1 activation have been conserved in evolution.","authors":"Capasso H, Palermo C, Wan S, Rao H, John UP, O'Connell MJ, Walworth NC","authors_abbrev":"Capasso H et al.","pubmed_publication_date":"01 Dec 2002","pubmed_entrez_date":"2002-11-05","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G8.01","SPAC8E11.02c","SPCC1259.13"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:24177582","title":"Mapping of rRNA genes by integration of hybrid plasmids in Schizosaccharomyces pombe.","citation":"Curr Genet 1984 Feb;8(2):93-7","abstract":"The major rRNA genes of the fission yeast Schizosaccharomyces pombe were mapped on chromosome III by plasmid integration. The integration vector YIp33 containing S. cerevisiae LEU2 gene was combined with the S. pombe rDNA. Since LEU2 complements S. pombe leu1 deficiency, it could be used as the genetic marker for integration. The 10.4 kb rDNA repeat contained ARS sequence, and therefore 2.4 kb and 0.7 kb subfragments not containing ARS were subcloned into YIp33 and transformed leu1 S. pombe cells to Leu(+). Genetic analyses of the transformants indicated that the integrated rDNA resides in the long arm of the shortest chromosome III, tightly linked to ade5 (1.4 cM). This result is consistent with our previous finding that the DAPI-stained smallest chromosomes were associated with the nucleolus (Umesono et al. 1983).","doi":"10.1007/BF00420224","authors":"Toda T, Nakaseko Y, Niwa O, Yanagida M","authors_abbrev":"Toda T et al.","pubmed_publication_date":"Feb 1984","pubmed_entrez_date":"2013-11-02","publication_year":"1984","canto_session_key":"51fa8b64f85bb40e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 20:26:41","canto_approved_date":"2019-01-31 20:26:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 20:26:32","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:16829518","title":"The replicative helicases of bacteria, archaea, and eukarya can unwind RNA-DNA hybrid substrates.","citation":"J Biol Chem 2006 Sep 15;281(37):26914-21","abstract":"Replicative helicases are hexameric enzymes that unwind DNA during chromosomal replication. They use energy from nucleoside triphosphate hydrolysis to translocate along one strand of the duplex DNA and displace the complementary strand. Here, the ability of a replicative helicase from each of the three domains, bacteria, archaea, and eukarya, to unwind RNA-containing substrate was determined. It is shown that all three helicases can unwind DNA-RNA hybrids while translocating along the single-stranded DNA. No unwinding could be observed when the helicases were provided with a single-stranded RNA overhang. Using DNA, RNA, and DNA-RNA chimeric oligonucleotides it was found that whereas the enzymes can bind both DNA and RNA, they could translocate only along DNA and only DNA stimulates the ATPase activity of the enzymes. Recent observations suggest that helicases may interact with enzymes participating in RNA metabolism and that RNA-DNA hybrids may be present on the chromosomes. Thus, the results presented here may suggest a new role for the replicative helicases during chromosomal replication or in other cellular processes.","authors":"Shin JH, Kelman Z","authors_abbrev":"Shin JH et al.","pubmed_publication_date":"15 Sep 2006","pubmed_entrez_date":"2006-07-11","publication_year":"2006","canto_session_key":"6452f378325f2048","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-10-27 17:07:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-10-27 17:07:06","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPBC25D12.03c","SPBC211.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-10-27"},{"uniquename":"PMID:28490498","title":"Shelterin components mediate genome reorganization in response to replication stress.","citation":"Proc Natl Acad Sci U S A 2017 May 23;114(21):5479-5484","abstract":"The dynamic nature of genome organization impacts critical nuclear functions including the regulation of gene expression, replication, and DNA damage repair. Despite significant progress, the mechanisms responsible for reorganization of the genome in response to cellular stress, such as aberrant DNA replication, are poorly understood. Here, we show that fission yeast cells carrying a mutation in the DNA-binding protein Sap1 show defects in DNA replication progression and genome stability and display extensive changes in genome organization. Chromosomal regions such as subtelomeres that show defects in replication progression associate with the nuclear envelope in  sap1  mutant cells. Moreover, high-resolution, genome-wide chromosome conformation capture (Hi-C) analysis revealed prominent contacts between telomeres and chromosomal arm regions containing replication origins proximal to binding sites for Taz1, a component of the Shelterin telomere protection complex. Strikingly, we find that Shelterin components are required for interactions between Taz1-associated chromosomal arm regions and telomeres. These analyses reveal an unexpected role for Shelterin components in genome reorganization in cells experiencing replication stress, with important implications for understanding the mechanisms governing replication and genome stability.","doi":"10.1073/pnas.1705527114","authors":"Mizuguchi T, Taneja N, Matsuda E, Belton JM, FitzGerald P, Dekker J, Grewal SIS","authors_abbrev":"Mizuguchi T et al.","pubmed_publication_date":"23 May 2017","pubmed_entrez_date":"2017-05-12","publication_year":"2017","canto_session_key":"60d0563d401c03d3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-05-13 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1672.02c","SPAC30D11.10"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:32303869","title":"Intragenic meiotic recombination in Schizosaccharomyces pombe is sensitive to environmental temperature changes.","citation":"Chromosome Res 2020 Jun;28(2):195-207","abstract":"Changes in environmental temperature influence cellular processes and their dynamics, and thus affect the life cycle of organisms that are unable to control their cell/body temperature. Meiotic recombination is the cellular process essential for producing healthy haploid gametes by providing physical links (chiasmata) between homologous chromosomes to guide their accurate segregation. Additionally, meiotic recombination-initiated by programmed DNA double-strand breaks (DSBs)-can generate genetic diversity and, therefore, is a driving force of evolution. Environmental temperature influencing meiotic recombination outcome thus may be a crucial determinant of reproductive success and genetic diversity. Indeed, meiotic recombination frequency in fungi, plants and invertebrates changes with temperature. In most organisms, these temperature-induced changes in meiotic recombination seem to be mediated through the meiosis-specific chromosome axis organization, the synaptonemal complex in particular. The fission yeast Schizosaccharomyces pombe does not possess a synaptonemal complex. Thus, we tested how environmental temperature modulates meiotic recombination frequency in the absence of a fully-fledged synaptonemal complex. We show that intragenic recombination (gene conversion) positively correlates with temperature within a certain range, especially at meiotic recombination hotspots. In contrast, crossover recombination, which manifests itself as chiasmata, is less affected. Based on our observations, we suggest that, in addition to changes in DSB frequency, DSB processing could be another temperature-sensitive step causing temperature-induced recombination rate alterations.","doi":"10.1007/s10577-020-09632-3","authors":"Brown SD, Audoynaud C, Lorenz A","authors_abbrev":"Brown SD et al.","pubmed_publication_date":"Jun 2020","pubmed_entrez_date":"2020-04-19","publication_year":"2020","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2020-04-20 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21880100","title":"Inner nuclear membrane protein Ima1 is dispensable for intranuclear positioning of centromeres.","citation":"Genes Cells 2011 Oct;16(10):1000-11","abstract":"Inner nuclear membrane (INM) proteins play a role in spatial organization of chromosomes within the nucleus. In the fission yeast Schizosaccharomyces pombe, Sad1, an INM protein of the conserved SUN-domain family, plays an active role in moving chromosomes along the nuclear membranes during meiotic prophase. Ima1 is another conserved INM protein recently identified. A previous study claimed that Ima1 is essential for mitotic cell growth, linking centromeric heterochromatin to the spindle-pole body. However, we obtained results contradictory to the previously proposed role for Ima1: Ima1 was dispensable for mitotic cell growth or centromere positioning. This discrepancy was attributed to incorrect ima1 deletion mutants used in the previous study. Our results show that Ima1 collaborates with two other conserved INM proteins of the LEM-domain family that are homologous to human Man1 and Lem2. Loss of any one of three INM proteins has no effect on mitotic cell growth; however, loss of all these proteins causes severe defects in mitotic cell growth and nuclear membrane morphology. Considering that all three INM proteins interact with Sad1, these results suggest that Ima1, Lem2 and Man1 play at least partially redundant roles for nuclear membrane organization.","doi":"10.1111/j.1365-2443.2011.01544.x","authors":"Hiraoka Y, Maekawa H, Asakawa H, Chikashige Y, Kojidani T, Osakada H, Matsuda A, Haraguchi T","authors_abbrev":"Hiraoka Y et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-09-02","publication_year":"2011","canto_session_key":"5c04846b8a231ac9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-02-11 13:21:31","canto_approved_date":"2024-04-12 08:45:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-06 19:55:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.05","SPAC14C4.05c","SPBC12D12.01","SPCC737.03c","SPAC18G6.10"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2014-02-11"},{"uniquename":"PMID:23093604","title":"RNA polymerase III mutants in TFIIFα-like C37 that cause terminator readthrough with no decrease in transcription output.","citation":"Nucleic Acids Res 2013 Jan 07;41(1):139-55","abstract":"How eukaryotic RNA polymerases switch from elongation to termination is unknown. Pol III subunits Rpc53 and Rpc37 (C53/37) form a heterodimer homologous to TFIIFβ/α. C53/37 promotes efficient termination and together with C11 also mediates pol III recycling in vitro. We previously developed Schizosaccharomyces pombe strains that report on two pol III termination activities: RNA oligo(U) 3'-end cleavage, and terminator readthrough. We randomly mutagenized C53 and C37 and isolated many C37 mutants with terminator readthrough but no comparable C53 mutants. The majority of C37 mutants have strong phenotypes with up to 40% readthrough and map to a C-terminal tract previously localized near Rpc2p in the pol III active center while a minority represent a distinct class with weaker phenotype, less readthrough and 3'-oligo(U) lengthening. Nascent pre-tRNAs released from a terminator by C37 mutants have shorter 3'-oligo(U) tracts than in cleavage-deficient C11 double mutants indicating RNA 3'-end cleavage during termination. We asked whether termination deficiency affects transcription output in the mutants in vivo both by monitoring intron-containing nascent transcript levels and (14)C-uridine incorporation. Surprisingly, multiple termination mutants have no decrease in transcript output relative to controls. These data are discussed in context of current models of pol III transcription.","doi":"10.1093/nar/gks985","authors":"Rijal K, Maraia RJ","authors_abbrev":"Rijal K et al.","pubmed_publication_date":"07 Jan 2013","pubmed_entrez_date":"2012-10-25","publication_year":"2013","canto_session_key":"439eed65cb3ae36d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17179073","title":"Opposite effects of tor1 and tor2 on nitrogen starvation responses in fission yeast.","citation":"Genetics 2007 Mar;175(3):1153-62","abstract":"The TOR protein kinases exhibit a conserved role in regulating cellular growth and proliferation. In the fission yeast two TOR homologs are present. tor1(+) is required for starvation and stress responses, while tor2(+) is essential. We report here that Tor2 depleted cells show a phenotype very similar to that of wild-type cells starved for nitrogen, including arrest at the G(1) phase of the cell cycle, induction of nitrogen-starvation-specific genes, and entrance into the sexual development pathway. The phenotype of tor2 mutants is in a striking contrast to the failure of tor1 mutants to initiate sexual development or arrest in G(1) under nitrogen starvation conditions. Tsc1 and Tsc2, the genes mutated in the human tuberous sclerosis complex syndrome, negatively regulate the mammalian TOR via inactivation of the GTPase Rheb. We analyzed the genetic relationship between the two TOR genes and the Schizosaccharomyces pombe orthologs of TSC1, TSC2, and Rheb. Our data suggest that like in higher eukaryotes, the Tsc1-2 complex negatively regulates Tor2. In contrast, the Tsc1-2 complex and Tor1 appear to work in parallel, both positively regulating amino acid uptake through the control of expression of amino acid permeases. Additionally, either Tsc1/2 or Tor1 are required for growth on a poor nitrogen source such as proline. Mutants lacking Tsc1 or Tsc2 are highly sensitive to rapamycin under poor nitrogen conditions, suggesting that the function of Tor1 under such conditions is sensitive to rapamycin. We discuss the complex genetic interactions between tor1(+), tor2(+), and tsc1/2(+) and the implications for rapamycin sensitivity in tsc1 or tsc2 mutants.","authors":"Weisman R, Roitburg I, Schonbrun M, Harari R, Kupiec M","authors_abbrev":"Weisman R et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2006-12-21","publication_year":"2007","canto_session_key":"650374502e2a8566","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-04 21:52:11","canto_approved_date":"2021-02-08 10:02:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-26 17:27:16","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":42,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.13c","SPBC216.07c","SPAC22F3.13","SPBC839.17c","SPAP7G5.06","SPBC428.16c","SPAC1039.09","SPBC30D10.10c","SPBC1A4.02c","SPAC630.13c"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2016-10-04"},{"uniquename":"PMID:12557273","title":"Role of phosphatidylinositol 3-phosphate in formation of forespore membrane in Schizosaccharomyces pombe.","citation":"Yeast 2003 Feb;20(3):193-206","abstract":"Phosphatidylinositol (PI) 3-kinase (encoded by the pik3(+) gene) in Schizosaccharomyces pombe has been identified as a homologue of VPS34p, a protein required for proper vesicular protein sorting. The clone defective in this protein carries enlarged vacuoles and exhibits sensitivity to high temperature or high ion concentration. The effect of disruption of pik3(+) on sporulation of Sz. pombe was examined. The diploid cells underwent G(1) arrest and meiosis. However, the spores formed by the deltapik3 cells were not viable. Electron-microscopic analysis revealed that the growth of the forespore membrane of deltapik3 cells was not correctly orientated, failing to engulf the nucleus or forming extremely small spores, as was confirmed by the use of Spo3p-GFP and GFP-Psy1p, which are markers of the forespore membrane. The coating materials found along the forespore membrane of the wild-type were greatly reduced in these cells. PI 3-P, the product of Pik3p, was detected on the forespore membrane, suggesting that PI 3-P-dependent vesicle transport may take place in formation of the forespore membrane. Misshaped forespore membrane, accumulation of vesicles, formation of small non-viable spores, and suppression by over expression of Psy1p were the phenotypes commonly seen in deltapik3 and deltaspo3 cells, suggesting a relationship between the functions of Pik3p and Spo3p in formation of the forespore membrane in Sz. pombe.","authors":"Onishi M, Koga T, Morita R, Nakamura Y, Nakamura T, Shimoda C, Takegawa K, Hirata A, Fukui Y","authors_abbrev":"Onishi M et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-01-31","publication_year":"2003","canto_session_key":"45b4bbb5f0235d01","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-16 14:18:35","canto_approved_date":"2020-01-23 20:04:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-05-31 10:11:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC458.05","SPAC607.10"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2017-09-16"},{"uniquename":"PMID:14718568","title":"TopBP1 and ATR colocalization at meiotic chromosomes: role of TopBP1/Cut5 in the meiotic recombination checkpoint.","citation":"Mol Biol Cell 2004 Apr;15(4):1568-79","abstract":"Mammalian TopBP1 is a BRCT domain-containing protein whose function in mitotic cells is linked to replication and DNA damage checkpoint. Here, we study its possible role during meiosis in mice. TopBP1 foci are abundant during early prophase I and localize mainly to histone gamma-H2AX-positive domains, where DNA double-strand breaks (required to initiate recombination) occur. Strikingly, TopBP1 showed a pattern almost identical to that of ATR, a PI3K-like kinase involved in mitotic DNA damage checkpoint. In the synapsis-defective Fkbp6(-/-) mouse, TopBP1 heavily stains unsynapsed regions of chromosomes. We also tested whether Schizosaccharomyces pombe Cut5 (the TopBP1 homologue) plays a role in the meiotic recombination checkpoint, like spRad3, the ATR homologue. Indeed, we found that a cut5 mutation suppresses the checkpoint-dependent meiotic delay of a meiotic recombination defective mutant, indicating a direct role of the Cut5 protein in the meiotic checkpoint. Our findings suggest that ATR and TopBP1 monitor meiotic recombination and are required for activation of the meiotic recombination checkpoint.","authors":"Perera D, Perez-Hidalgo L, Moens PB, Reini K, Lakin N, Syväoja JE, San-Segundo PA, Freire R","authors_abbrev":"Perera D et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-01-14","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC222.15","SPAC23C4.18c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:16627621","title":"Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis.","citation":"Proc Natl Acad Sci U S A 2006 May 02;103(18):6988-93","abstract":"Histone acetylation affects many nuclear processes including transcription, chromatin assembly, and DNA damage repair. Acetylation of histone H3 lysine 56 (H3 K56ac) in budding yeast occurs during mitotic S phase and persists during DNA damage repair. Here, we show that H3 K56ac is also present during premeiotic S phase and is conserved in fission yeast. Furthermore, the H3 K56ac modification is not observed in the absence of the histone chaperone Asf1. asf1delta and H3 K56R mutants exhibit similar sensitivity to DNA damaging agents. Mutational analysis of Asf1 demonstrates that DNA damage sensitivity correlates with (i) decreased levels of H3 K56ac and (ii) a region implicated in histone binding. In contrast, multiple asf1 mutants that are resistant to DNA damage display WT levels of K56ac. These data suggest that maintenance of H3 K56 acetylation is a primary contribution of Asf1 to genome stability in yeast.","authors":"Recht J, Tsubota T, Tanny JC, Diaz RL, Berger JM, Zhang X, Garcia BA, Shabanowitz J, Burlingame AL, Hunt DF, Kaufman PD, Allis CD","authors_abbrev":"Recht J et al.","pubmed_publication_date":"02 May 2006","pubmed_entrez_date":"2006-04-22","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19209379","title":"Low contents of carbon and nitrogen in highly abundant proteins: evidence of selection for the economy of atomic composition.","citation":"J Mol Evol 2009 Mar;68(3):248-55","abstract":"Proteins that assimilate particular elements were found to avoid using amino acids containing the element, which indicates that the metabolic constraints of amino acids may influence the evolution of proteins. We suspected that low contents of carbon, nitrogen, and sulfur may also be selected for economy in highly abundant proteins that consume large amounts of the resources of cells. By analyzing recently available proteomic data in Escherichia coli, Saccharomyces cerevisiae, and Schizosaccharomyces pombe, we found that at least the carbon and nitrogen contents in amino acid side chains are negatively correlated with protein abundance. An amino acid with a high number of carbon atoms in its side chain generally requires relatively more energy for its synthesis. Thus, it may be selected against in highly abundant proteins either because of economy in building blocks or because of economy in energy. Previous studies showed that highly abundant proteins preferentially use cheap (in terms of energy) amino acids. We found that the carbon content is still negatively correlated with protein abundance after controlling for the energetic cost of the amino acids. However, the negative correlation between protein abundance and energetic cost disappeared after controlling for carbon content. Building blocks seem to be more restricted than energy. It seems that the amino acid sequences of highly abundant proteins have to compromise between optimization for their biological functions and reducing the consumption of limiting resources. By contrast, the amino acid sequences of weakly expressed proteins are more likely to be optimized for their biological functions.","doi":"10.1007/s00239-009-9199-4","authors":"Li N, Lv J, Niu DK","authors_abbrev":"Li N et al.","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2009-02-12","publication_year":"2009","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25529221","title":"Spatial control of calcineurin in response to heat shock in fission yeast.","citation":"Genes Cells 2015 Feb;20(2):95-107","abstract":"In fission yeast, Ppb1, the Ca2+/calmodulin-dependent protein phosphatase calcineurin regulates multiple biological processes, such as cytokinesis, Ca2+-homeostasis, membrane trafficking and cell wall integrity. Calcineurin dephosphorylates the Prz1 transcription factor, leading to its nuclear translocation and gene expression under the control of CDRE (calcineurin-dependent response element). Although the calcineurin-mediated spatial control of downstream transcription factors has been intensively studied in many organisms, less is known about the spatial regulation of calcineurin on stresses. Here, we show that heat shock stimulates calcineurin-dependent nuclear translocation of Prz1 and CDRE-dependent gene expression. Notably, calcineurin exhibited a dramatic change in subcellular localization, translocating from diffuse cytoplasmic to dot-like structures on heat shock. The calcineurin dots colocalized with Dcp2 or Pabp, the constituent of P-bodies or stress granules, respectively, thus suggesting that calcineurin is a component of RNA granules under heat shock. Importantly, the calcineurin inhibitor FK506 markedly inhibited the accumulation of calcineurin granules, whereas the constitutively active calcineurin strongly accumulated in the granules on heat shock, suggesting that phosphatase activity is important for calcineurin localization. Notably, the depletion of calcineurin induced a rapid appearance of Nrd1- and Pabp-positive RNA granules. The possible roles of calcineurin in response to heat shock will be discussed.","doi":"10.1111/gtc.12203","authors":"Higa M, Kita A, Hagihara K, Kitai Y, Doi A, Nagasoko R, Satoh R, Sugiura R","authors_abbrev":"Higa M et al.","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2014-12-23","publication_year":"2015","canto_session_key":"42c2373c68901fb2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-12-24 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26430713","title":"Competition and collaboration between different actin assembly pathways allows for homeostatic control of the actin cytoskeleton.","citation":"Bioarchitecture 2014;5(1-2):27-34","abstract":"Tremendous insight into actin-associated proteins has come from careful biochemical and cell biological characterization of their activities and regulation. However, many studies of their cellular behavior have only considered each in isolation. Recent efforts reveal that assembly factors compete for polymerization-competent actin monomers, suggesting that actin is homeostatically regulated. It seems that a major regulatory component is competition between Arp2/3-activating nucleation promoting factors and profilin for actin monomers. The result is differential delivery of actin to different pathways, allowing for simultaneous assembly of competing F-actin structures and collaborative building of higher order cellular structures. Although there are likely to be additional factors that regulate actin homeostasis, especially in a cell type-dependent fashion, we advance the notion that competition between actin assembly factors results in a tunable system that can be adjusted according to extracellular and intracellular cues.","doi":"10.1080/19490992.2015.1090670","authors":"Rotty JD, Bear JE","authors_abbrev":"Rotty JD et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2015-10-03","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-05-01 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16930478","title":"The fission yeast DNA structure checkpoint protein Rad26ATRIP/LCD1/UVSD accumulates in the cytoplasm following microtubule destabilization.","citation":"BMC Cell Biol 2006 Aug 24;7:32","abstract":"DNA structure checkpoints are conserved eukaryotic signal transduction pathways that help preserve genomic integrity. Upon detecting checkpoint signals such as stalled replication forks or double-stranded DNA breaks, these pathways coordinate appropriate stress responses. Members of the PI-3 kinase related kinase (PIKK) family are essential elements of DNA structure checkpoints. In fission yeast, the Rad3 PIKK and its regulatory subunit Rad26 coordinate the detection of checkpoint signals with pathway outputs.\nWe found that untreated rad26Delta cells were defective for two microtubule-dependent processes: chromosome segregation and morphogenesis. Interestingly, cytoplasmic accumulation of Rad26-GFP occurred following treatment with microtubule destabilizing drugs, but not during treatment with the genotoxic agent Phleomycin. Cytoplasmic accumulation of Rad26-GFP depended on Rad24, a 14-3-3 protein also required for DNA structure checkpoints and morphogenesis. Results of over expression and epistasis experiments confirm that Rad26 and Rad24 define a response to microtubule destabilizing conditions.\nTwo DNA structure checkpoint proteins with roles in morphogenesis define a response to microtubule destabilizing conditions.","authors":"Baschal EE, Chen KJ, Elliott LG, Herring MJ, Verde SC, Wolkow TD","authors_abbrev":"Baschal EE et al.","pubmed_publication_date":"24 Aug 2006","pubmed_entrez_date":"2006-08-26","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPAC9E9.08"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8541877","title":"Epigenetic regulation of gene expression: the effect of altered chromatin structure from yeast to mammals.","citation":"Hum Mol Genet 1995;4 Spec No:1765-77","abstract":"Epigenetic gene regulation refers to different states of phenotypic expression caused by differential effects of chromosome or chromatin packaging rather than by differences in DNA sequence. Examples of epigenetic regulation can be found in organisms as diverse as the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, the fruit fly Drosophila melanogaster, the nematode Caenorhabditis elegans, and mammals. Three major types of epigenetic regulation are considered in this review: dosage compensation, imprinting and position effect variegation. While the specific details and mechanisms of each is quite different, they all involve either local or extensive alterations in chromatin structure. A number of genes implicated in epigenetic regulation have been isolated and their products identified as proteins or RNA molecules involved at various levels in DNA, chromatin or chromosome binding. While in general our understanding of mammalian epigenetic phenomena is not as advanced as that in model systems, the detailed molecular and genetic understanding of processes responsible for conditional gene silencing in invertebrate systems provides strong models for consideration of such effects in human and mouse genetics.","authors":"Hendrich BD, Willard HF","authors_abbrev":"Hendrich BD et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31640799","title":"The RNA-binding ubiquitin ligase MKRN1 functions in ribosome-associated quality control of poly(A) translation.","citation":"Genome Biol 2019 Oct 22;20(1):216","abstract":"Cells have evolved quality control mechanisms to ensure protein homeostasis by detecting and degrading aberrant mRNAs and proteins. A common source of aberrant mRNAs is premature polyadenylation, which can result in non-functional protein products. Translating ribosomes that encounter poly(A) sequences are terminally stalled, followed by ribosome recycling and decay of the truncated nascent polypeptide via ribosome-associated quality control.\nHere, we demonstrate that the conserved RNA-binding E3 ubiquitin ligase Makorin Ring Finger Protein 1 (MKRN1) promotes ribosome stalling at poly(A) sequences during ribosome-associated quality control. We show that MKRN1 directly binds to the cytoplasmic poly(A)-binding protein (PABPC1) and associates with polysomes. MKRN1 is positioned upstream of poly(A) tails in mRNAs in a PABPC1-dependent manner. Ubiquitin remnant profiling and in vitro ubiquitylation assays uncover PABPC1 and ribosomal protein RPS10 as direct ubiquitylation substrates of MKRN1.\nWe propose that MKRN1 mediates the recognition of poly(A) tails to prevent the production of erroneous proteins from prematurely polyadenylated transcripts, thereby maintaining proteome integrity.","doi":"10.1186/s13059-019-1814-0","authors":"Hildebrandt A, Brüggemann M, Rücklé C, Boerner S, Heidelberger JB, Busch A, Hänel H, Voigt A, Möckel MM, Ebersberger S, Scholz A, Dold A, Schmid T, Ebersberger I, Roignant JY, Zarnack K, König J, Beli P","authors_abbrev":"Hildebrandt A et al.","pubmed_publication_date":"22 Oct 2019","pubmed_entrez_date":"2019-10-24","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3A11.02","SPCC1739.01"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:9766521","title":"Molecular cloning and tissue-specific expression of Mrad9, a murine orthologue of the Schizosaccharomyces pombe rad9+ checkpoint control gene.","citation":"J Cell Physiol 1998 Nov;177(2):241-7","abstract":"We have isolated a murine cDNA, Mrad9, that is orthologous to the fission yeast rad9+ and human HRAD9 genes. Mrad9 encodes a 389 amino acid long, 42,032 Dalton protein that is 27% identical and 56% similar to Rad9p, and 82% identical and 88% similar to HRAD9, at the amino acid level. Expression of the Mrad9 cDNA in Schizosaccharomyces pombe rad9::ura4+ cells restores nearly wild-type levels of hydroxyurea resistance and early S phase checkpoint control to mutant fission yeast cell populations. However, UV resistance is only minimally restored, and mutant cells remain sensitive to gamma radiation. Mrad9 genomic DNA was isolated from a mouse 129/SvEv library. The Mrad9 gene was local ized to a 15-kbp genomic DNA fragment, and contains 10 exons separated by 9 introns. Northern blot analysis indicates that the gene is expressed in many different tissues of the adult mouse, but the mRNA is most abundant in the heart and present at very low levels in the liver. These studies demonstrate the existence of a murine orthologue of the fission yeast rad9+ gene and underscore at least the partial evolutionary conservation of rad9+-dependent checkpoint control mechanisms.","authors":"Hang H, Rauth SJ, Hopkins KM, Davey SK, Lieberman HB","authors_abbrev":"Hang H et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1998-10-10","publication_year":"1998","canto_session_key":"7e150d62fcbe1f72","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 17:11:14","canto_session_submitted_date":"2012-03-03 17:11:01","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:2274045","title":"Dissociation of meiotic and mitotic roles of the fission yeast cdc2 gene.","citation":"Mol Gen Genet 1990 Jul;222(2-3):473-5","abstract":"The fission yeast cdc2 gene is pleiotropic, functioning both in the cell division cycle and in meiosis. Here we show that cdc2 is allelic to tws1, a previously isolated meiotic gene. Dissociation of meiotic and mitotic roles of the gene is also demonstrated by finding mutant alleles specifically altered in only one of the two processes.","authors":"Grallert B, Sipiczki M","authors_abbrev":"Grallert B et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPRNASLT1","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19680239","title":"Structures of the tRNA export factor in the nuclear and cytosolic states.","citation":"Nature 2009 Sep 03;461(7260):60-5","abstract":"Transfer RNAs are among the most ubiquitous molecules in cells, central to decoding information from messenger RNAs on translating ribosomes. In eukaryotic cells, tRNAs are actively transported from their site of synthesis in the nucleus to their site of function in the cytosol. This is mediated by a dedicated nucleo-cytoplasmic transport factor of the karyopherin-beta family (Xpot, also known as Los1 in Saccharomyces cerevisiae). Here we report the 3.2 A resolution structure of Schizosaccharomyces pombe Xpot in complex with tRNA and RanGTP, and the 3.1 A structure of unbound Xpot, revealing both nuclear and cytosolic snapshots of this transport factor. Xpot undergoes a large conformational change on binding cargo, wrapping around the tRNA and, in particular, binding to the tRNA 5' and 3' ends. The binding mode explains how Xpot can recognize all mature tRNAs in the cell and yet distinguish them from those that have not been properly processed, thus coupling tRNA export to quality control.","doi":"10.1038/nature08394","authors":"Cook AG, Fukuhara N, Jinek M, Conti E","authors_abbrev":"Cook AG et al.","pubmed_publication_date":"03 Sep 2009","pubmed_entrez_date":"2009-08-15","publication_year":"2009","canto_session_key":"b31651e8e3efb0c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-15 17:39:02","canto_approved_date":"2023-02-23 20:16:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-15 17:38:55","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1289.03c","SPBP8B7.09c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2023-02-15","pdb_entries":[{"pdb_id":"3icq","gene_chains":[{"gene_uniquename":"SPBP8B7.09c","chain":"T/U","position":"1-978"}],"title":"Karyopherin nuclear state","entry_authors":"Cook AG,Fukuhara N,Jinek M,Conti E","entry_authors_abbrev":"Cook AG et al.","reference_uniquename":"PMID:19680239","experimental_method":"X-ray","resolution":"3.2"},{"pdb_id":"3ibv","gene_chains":[{"gene_uniquename":"SPBP8B7.09c","chain":"A/B","position":"1-978"}],"title":"Karyopherin cytosolic state","entry_authors":"Cook AG,Fukuhara N,Jinek M,Conti E","entry_authors_abbrev":"Cook AG et al.","reference_uniquename":"PMID:19680239","experimental_method":"X-ray","resolution":"3.1"}]},{"uniquename":"EMBL:AU010368","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12527786","title":"A comparison of three fission yeast mitochondrial genomes.","citation":"Nucleic Acids Res 2003 Jan 15;31(2):759-68","abstract":"The fission yeasts are members of the fungal order Schizosaccharomycetales, a candidate deep-diverging group within Ascomycota. Although a great deal of molecular information is available from Schizosaccharomyces pombe, a model eukaryote, very little is available from other members of this group. In order to better characterize mitochondrial genome evolution in this fungal lineage, the mitochondrial DNA (mtDNA) of two additional fission yeasts, Schizosaccharomyces octosporus and Schizosaccharomyces japonicus var. japonicus, was sequenced. Whereas the mtDNA of S.pombe is only 19 431 bp, the mtDNA of S.octosporus is 44 227 bp, and that of S.japonicus var. japonicus is over 80 kb. The size variation of these mtDNAs is due largely to non-coding regions. The gene content in the latter two mtDNAs is almost identical to that of the completely sequenced S.pombe mtDNA, which encodes 25 tRNA species, the large and small mitochondrial ribosomal RNAs (rnl and rns), the RNA component of mitochondrial RNaseP (rnpB), mitochondrial small subunit ribosomal protein 3 (rps3), cytochrome oxidase subunits 1, 2 and 3 (cox1, cox2 and cox3) and ATP-synthase subunits 6, 8 and 9 (atp6, atp8 and atp9). However, trnI2(cau) (C modified to lysidine) is absent in the S.octosporus mtDNA, as are corresponding ATA codons in its protein-coding genes, and rps3 and rnpB are not found in the mtDNA of S.japonicus var. japonicus. The mtDNA of S.octosporus contains five double hairpin elements, the first report of these elements in an ascomycete. This study provides further evidence in favor of the mobility of these elements, and supports their role in mitochondrial genome rearrangement. The results of our phylogenetic analysis support the monophyly of the Schizosaccharomycetales, but question their grouping within the Archiascomycota.","authors":"Bullerwell CE, Leigh J, Forget L, Lang BF","authors_abbrev":"Bullerwell CE et al.","pubmed_publication_date":"15 Jan 2003","pubmed_entrez_date":"2003-01-16","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010874","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12149471","title":"Absolute requirement of spermidine for growth and cell cycle progression of fission yeast (Schizosaccharomyces pombe).","citation":"Proc Natl Acad Sci U S A 2002 Aug 06;99(16):10330-4","abstract":"Schizosaccharomyces pombe cells that cannot synthesize spermidine or spermine because of a deletion-insertion in the gene coding for S-adenosylmethionine decarboxylase (Deltaspe2) have an absolute requirement for spermidine for growth. Flow cytometry studies show that in the absence of spermidine an overall delay of the cell cycle progression occurs with some accumulation of cells in the G(1) phase; as little as 10(-6) M spermidine is sufficient to maintain normal cell cycle distribution and normal growth. Morphologically some of the spermidine-deprived cells become spherical at an early stage with little evidence of cell division. On further incubation in the spermidine-deprived medium, growth occurs in most of the cells, not by cell division but rather by cell elongation, with an abnormal distribution of the actin cytoskeleton, DNA (4', 6-diamidino-2-phenylindole staining), and calcofluor-staining moieties. More prolonged incubation in the spermidine-deficient medium leads to profound morphological changes including nuclear degeneration.","authors":"Chattopadhyay MK, Tabor CW, Tabor H","authors_abbrev":"Chattopadhyay MK et al.","pubmed_publication_date":"06 Aug 2002","pubmed_entrez_date":"2002-08-01","publication_year":"2002","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.05c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:38768030","title":"Microscopy-based protocol for the quantification of cells viability for temperature-sensitive S. pombe.","citation":"STAR Protoc 2024 May 19;5(2):103076","abstract":"Conventional colony-forming unit assay to measure cell viability is laborious and results in large experimental variability, which prohibits accurate quantification of microbial viability. Here, we present a microscopy-based protocol for the quantification of cells viability for temperature-sensitive S. pombe. We describe steps for growing and treating yeast cells and visualization of individual cells viability based on Phloxine B staining. We then detail procedures for data processing using Nikon NIS Elements Advanced Research (AR) software. For complete details on the use and execution of this protocol, please refer to Lim et al. 1 .","doi":"10.1016/j.xpro.2024.103076","authors":"Lim KK, Chen ES","authors_abbrev":"Lim KK et al.","pubmed_publication_date":"19 May 2024","pubmed_entrez_date":"2024-05-20","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-05-20 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10983981","title":"Control of transfer RNA maturation by phosphorylation of the human La antigen on serine 366.","citation":"Mol Cell 2000 Aug;6(2):339-48","abstract":"Conversion of a nascent precursor tRNA to a mature functional species is a multipartite process that involves the sequential actions of several processing and modifying enzymes. La is the first protein to interact with pre-tRNAs in eukaryotes. An opal suppressor tRNA served as a functional probe to examine the activities of yeast and human (h)La proteins in this process in fission yeast. An RNA recognition motif and Walker motif in the metazoan-specific C-terminal domain (CTD) of hLa maintain pre-tRNA in an unprocessed state by blocking the 5'-processing site, impeding an early step in the pathway. Faithful phosphorylation of hLa on serine 366 reverses this block and promotes tRNA maturation. The results suggest that regulation of tRNA maturation at the level of RNase P cleavage may occur via phosphorylation of serine 366 of hLa.","authors":"Intine RV, Sakulich AL, Koduru SB, Huang Y, Pierstorff E, Goodier JL, Phan L, Maraia RJ","authors_abbrev":"Intine RV et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2000-09-13","publication_year":"2000","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A10.10c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:18556659","title":"The spindle checkpoint functions of Mad3 and Mad2 depend on a Mad3 KEN box-mediated interaction with Cdc20-anaphase-promoting complex (APC/C).","citation":"J Biol Chem 2008 Aug 22;283(34):23039-47","abstract":"Mitotic progression is driven by proteolytic destruction of securin and cyclins. These proteins are labeled for destruction by an ubiquitin-protein isopeptide ligase (E3) known as the anaphase-promoting complex or cyclosome (APC/C). The APC/C requires activators (Cdc20 or Cdh1) to efficiently recognize its substrates, which are specified by destruction (D box) and/or KEN box signals. The spindle assembly checkpoint responds to unattached kinetochores and to kinetochores lacking tension, both of which reflect incomplete biorientation of chromosomes, by delaying the onset of anaphase. It does this by inhibiting Cdc20-APC/C. Certain checkpoint proteins interact directly with Cdc20, but it remains unclear how the checkpoint acts to efficiently inhibit Cdc20-APC/C activity. In the fission yeast, Schizosaccharomyces pombe, we find that the Mad3 and Mad2 spindle checkpoint proteins interact stably with the APC/C in mitosis. Mad3 contains two KEN boxes, conserved from yeast Mad3 to human BubR1, and mutation of either of these abrogates the spindle checkpoint. Strikingly, mutation of the N-terminal KEN box abolishes incorporation of Mad3 into the mitotic checkpoint complex (Mad3-Mad2-Slp1 in S. pombe, where Slp1 is the Cdc20 homolog that we will refer to as Cdc20 hereafter) and stable association of both Mad3 and Mad2 with the APC/C. Our findings demonstrate that this Mad3 KEN box is a critical mediator of Cdc20-APC/C inhibition, without which neither Mad3 nor Mad2 can associate with the APC/C or inhibit anaphase onset.","doi":"10.1074/jbc.M803594200","authors":"Sczaniecka M, Feoktistova A, May KM, Chen JS, Blyth J, Gould KL, Hardwick KG","authors_abbrev":"Sczaniecka M et al.","pubmed_publication_date":"22 Aug 2008","pubmed_entrez_date":"2008-06-17","publication_year":"2008","canto_session_key":"42362e93a6f25aa8","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPAC6F12.14","SPAC6F12.15c","SPAC17C9.01c","SPAC19G12.01c","SPAC27D7.05c","SPBP23A10.04","SPBC1A4.01","SPAC23C11.12","SPBC83.04","SPAC343.03","SPBC106.09","SPBC28E12.01c","SPAC959.09c","SPAC821.08c","SPCC1795.01c"],"gene_count":16,"ltp_gene_count":16},{"uniquename":"PMID:17699598","title":"Regulation of cell cycle and stress responses to hydrostatic pressure in fission yeast.","citation":"Mol Biol Cell 2007 Oct;18(10):4168-79","abstract":"We have investigated the cellular responses to hydrostatic pressure by using the fission yeast Schizosaccharomyces pombe as a model system. Exposure to sublethal levels of hydrostatic pressure resulted in G2 cell cycle delay. This delay resulted from Cdc2 tyrosine-15 (Y-15) phosphorylation, and it was abrogated by simultaneous disruption of the Cdc2 kinase regulators Cdc25 and Wee1. However, cell cycle delay was independent of the DNA damage, cytokinesis, and cell size checkpoints, suggesting a novel mechanism of Cdc2-Y15 phosphorylation in response to hydrostatic pressure. Spc1/Sty1 mitogen-activated protein (MAP) kinase, a conserved member of the eukaryotic stress-activated p38, mitogen-activated protein (MAP) kinase family, was rapidly activated after pressure stress, and it was required for cell cycle recovery under these conditions, in part through promoting polo kinase (Plo1) phosphorylation on serine 402. Moreover, the Spc1 MAP kinase pathway played a key role in maintaining cell viability under hydrostatic pressure stress through the bZip transcription factor, Atf1. Further analysis revealed that prestressing cells with heat increased barotolerance, suggesting adaptational cross-talk between these stress responses. These findings provide new insight into eukaryotic homeostasis after exposure to pressure stress.","authors":"George VT, Brooks G, Humphrey TC","authors_abbrev":"George VT et al.","pubmed_publication_date":"Oct 2007","pubmed_entrez_date":"2007-08-19","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19186047","title":"Actin and endocytosis: mechanisms and phylogeny.","citation":"Curr Opin Cell Biol 2009 Feb;21(1):20-7","abstract":"The regulated assembly of actin filament networks is a crucial part of endocytosis, with crucial temporal and spatial relationships between proteins of the endocytic and actin assembly machinery. Of particular importance has been a wealth of studies in budding and fission yeast. Cell biology approaches, combined with molecular genetics, have begun to uncover the complexity of the regulation of actin dynamics during the endocytic process. In a wide range of organisms, clathrin-mediated endocytosis appears to be linked to Arp2/3-mediated actin assembly. The conservation of the components, across a wide range eukaryotic species, suggests that the partnership between endocytosis and actin may be evolutionarily ancient.","doi":"10.1016/j.ceb.2009.01.006","authors":"Galletta BJ, Cooper JA","authors_abbrev":"Galletta BJ et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2009-02-03","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12668671","title":"Regulation of Ste7 ubiquitination by Ste11 phosphorylation and the Skp1-Cullin-F-box complex.","citation":"J Biol Chem 2003 Jun 20;278(25):22284-9","abstract":"Ste7 is a mitogen-activated protein kinase kinase that mediates pheromone signaling in Saccharomyces cerevisiae. We showed previously that Ste7 is ubiquitinated upon prolonged stimulation by pheromone and that accumulation of ubiquitinated Ste7 results in enhanced transcription and cell division arrest responses (Wang, Y., and Dohlman, H. G. (2002) J. Biol. Chem. 277, 15766-15772). We now report that ubiquitination of Ste7 requires Ste11 kinase and Skp1/Cullin/F-box (SCF) ubiquitin-conjugating activities. Ste7 is not ubiquitinated in Ste11-deficient cells or when the Ste11 phosphorylation sites have been mutated. Ste7 ubiquitination and degradation (but not phosphorylation) is specifically blocked in mutants defective for the E2 ubiquitin-conjugating enzyme Cdc34 or the cullin homologue Cdc53. Both are components of the SCF complex that ubiquitinates proteins during the G1-S transition of the cell cycle. Our findings suggest that SCF promotes the ubiquitination and degradation of Ste7, thereby favoring the resumption of cell division cycling after pheromone-induced growth arrest.","authors":"Wang Y, Ge Q, Houston D, Thorner J, Errede B, Dohlman HG","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"20 Jun 2003","pubmed_entrez_date":"2003-04-02","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36288901","title":"Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II.","citation":"Life Sci Alliance 2023 Jan;6(1)","abstract":"We report a case in which sub-stoichiometric binding of an actin-binding protein has profound structural and functional consequences, providing an insight into the fundamental properties of actin regulation. Rng2 is an IQGAP contained in contractile rings in the fission yeast  Schizosaccharomyces pombe  Here, we used high-speed atomic force microscopy and electron microscopy and found that sub-stoichiometric binding of the calponin-homology actin-binding domain of Rng2 (Rng2CHD) induces global structural changes in skeletal muscle actin filaments, including shortening of the filament helical pitch. Sub-stoichiometric binding of Rng2CHD also reduced the affinity between actin filaments and muscle myosin II carrying ADP and strongly inhibited the motility of actin filaments on myosin II in vitro. On skeletal muscle myosin II-coated surfaces, Rng2CHD stopped the actin movements at a binding ratio of 11%. Rng2CHD also inhibited actin movements on myosin II of the amoeba  Dictyostelium , but in this case, by detaching actin filaments from myosin II-coated surfaces. Thus, sparsely bound Rng2CHD induces apparently cooperative structural changes in actin filaments and inhibits force generation by actomyosin II.","doi":"10.26508/lsa.202201469","authors":"Hayakawa Y, Takaine M, Ngo KX, Imai T, Yamada MD, Behjat AB, Umeda K, Hirose K, Yurtsever A, Kodera N, Tokuraku K, Numata O, Fukuma T, Ando T, Nakano K, Uyeda TQ","authors_abbrev":"Hayakawa Y et al.","pubmed_publication_date":"Jan 2023","pubmed_entrez_date":"2022-10-26","publication_year":"2023","canto_session_key":"599a12da3e8a49a1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-10-28 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18428330","title":"Pulsed-field gel electrophoresis for long-range restriction mapping.","citation":"Curr Protoc Hum Genet 2002 Feb;Chapter 5:Unit5.1","abstract":"This unit describes procedures for generating long-range restriction maps of genomic DNA and for analysis of large insert clones. The basic protocol details restriction digestion of agarose-embedded DNA, PFGE separation, Southern transfer, and hybridization. Support protocols describe the preparation of high-molecular-weight genomic DNA samples in agarose blocks and in agarose microbeads, respectively. Additional support protocols describe the preparation of DNA size standards from l phage and two yeast species, Saccharomyces cerevisiae and Schizosaccharomyces pombe. An alternative method of preparing S. cerevisiae size standards using lithium dodecyl sulfate (LiDS) solubilization is provided. The final protocol details the preparation of BAC DNA suitable for digestion, mapping, and sequencing.","doi":"10.1002/0471142905.hg0501s31","authors":"Gemmill RM, Bolin R, Albertsen H, Tomkins JP, Wing RA","authors_abbrev":"Gemmill RM et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2008-04-23","publication_year":"2002","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31201205","title":"Coordinated Roles of the Putative Ceramide-Conjugation Protein, Cwh43, and a Mn 2+ -Transporting, P-Type ATPase, Pmr1, in Fission Yeast.","citation":"G3 (Bethesda) 2019 Aug 08;9(8):2667-2676","abstract":"Genetically controlled mechanisms of cell division and quiescence are vital for responding to changes in the nutritional environment and for cell survival. Previously, we have characterized temperature-sensitive (ts) mutants of the  cwh43  gene in fission yeast,  Schizosaccharomyces pombe , which is required for both cell proliferation and nitrogen starvation-induced G0 quiescence. Cwh43 encodes an evolutionarily conserved transmembrane protein that localizes in endoplasmic reticulum (ER). Defects in this protein fail to divide in low glucose and lose mitotic competence under nitrogen starvation, and also affect lipid metabolism. Here, we identified mutations of the  pmr1  gene, which encodes an evolutionarily conserved Ca 2+ /Mn 2+ -transporting P-type ATPase, as potent extragenic suppressors of ts mutants of the  cwh43  gene. Intriguingly, these  pmr1  mutations specifically suppressed the ts phenotype of  cwh43  mutants, among five P-type Ca 2+ - and/or Mn 2+ -ATPases reported in this organism. Cwh43 and Pmr1 co-localized in the ER. In  cwh43  mutant cells, addition of excessive manganese to culture media enhanced the severe defect in cell morphology, and caused abnormal accumulation of a cell wall component, 1, 3-β-glucan. In contrast, these abnormal phenotypes were abolished by deletion of the  pmr1  +  gene, as well as by removal of Mn 2+  from the culture medium. Furthermore, nutrition-related phenotypes of  cwh43  mutant cells were rescued in the absence of Pmr1. Our findings indicate that the cellular processes regulated by Cwh43 are appropriately balanced with Pmr1-mediated Mn 2+  transport into the ER.","doi":"10.1534/g3.119.400281","authors":"Nakazawa N, Xu X, Arakawa O, Yanagida M","authors_abbrev":"Nakazawa N et al.","pubmed_publication_date":"08 Aug 2019","pubmed_entrez_date":"2019-06-16","publication_year":"2019","canto_session_key":"0572af570458b258","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Norihiko Nakazawa","canto_first_approved_date":"2019-06-23 21:25:51","canto_approved_date":"2022-01-05 14:19:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-21 06:52:06","canto_added_date":"2019-06-17 00:15:04","annotation_curators":[{"name":"Norihiko Nakazawa","community_curator":true,"annotation_count":10,"orcid":"0000-0001-8386-0812","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":41,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29A4.19c","SPAC27F1.08","SPAC823.07","SPAC589.12","SPBC31E1.02c","SPACUNK4.07c","SPAPB2B4.04c","SPBC839.06"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2019-06-23"},{"uniquename":"PMID:40841561","title":"Structures and mechanisms of U6 snRNA m 6 A modification by METTL16.","citation":"Nat Commun 2025 Aug 21;16(1):7708","abstract":"The N 6 -methyladenosine (m 6 A) modification in U6 snRNA, catalyzed by METTL16 using S-adenosylmethionine (SAM) as the methyl donor, is required for efficient and accurate pre-mRNA splicing. However, the mechanism by which METTL16 modifies U6 snRNA with m 6 A remains elusive. Here, we present cryo-EM structures of METTL16 in complex with U6 snRNA, providing insights into the METTL16-mediated modification of U6 snRNA with m 6 A. The structures reveal that U6 snRNA is recruited to METTL16 through specific interactions between the C-terminal kinase-associated 1 (KA-1) domain of METTL16 and the internal stem-loop (ISL) of U6 snRNA. Upon SAM binding to the catalytic pocket within the N-terminal methyltransferase domain (MTD), U6 snRNA undergoes a structural rearrangement that positions the target adenine-containing motif at the catalytic site. This conformational change is followed by an additional structural adjustment of U6 snRNA into a productive conformation, bringing the target adenosine closer to SAM within the catalytic pocket and thereby ensuring efficient m 6 A modification. The KA-1 domain functions as a scaffold for initial substrate recognition and facilitates the subsequent dynamic methylation process within the MTD, highlighting the cooperative roles of METTL16 domains for U6 snRNA modification.","doi":"10.1038/s41467-025-63021-0","authors":"Ju J, Tomita K","authors_abbrev":"Ju J et al.","pubmed_publication_date":"21 Aug 2025","pubmed_entrez_date":"2025-08-21","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27D7.08c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"9m86","gene_chains":[{"gene_uniquename":"SPAC27D7.08c","chain":"A/C","position":"257-385"}],"title":"Crystal structure of SpMETTL16 kinase associated 1 domain in complex with U6 snRNA internal stem loop","entry_authors":"Ju J,Tomita K","entry_authors_abbrev":"Ju J et al.","reference_uniquename":"PMID:40841561","experimental_method":"X-ray","resolution":"2.795"},{"pdb_id":"9u48","gene_chains":[{"gene_uniquename":"SPAC27D7.08c","chain":"A","position":"9-385"}],"title":"Cryo-EM structure of spMETTL16 in complex with U6 snRNA and SAM","entry_authors":"Ju J,Tomita K","entry_authors_abbrev":"Ju J et al.","reference_uniquename":"PMID:40841561","experimental_method":"EM","resolution":"2.99"},{"pdb_id":"9u47","gene_chains":[{"gene_uniquename":"SPAC27D7.08c","chain":"A","position":"9-385"}],"title":"Cryo-EM structure of spMETTL16 in complex with U6 snRNA_delta17","entry_authors":"Ju J,Tomita K","entry_authors_abbrev":"Ju J et al.","reference_uniquename":"PMID:40841561","experimental_method":"EM","resolution":"3.4"}]},{"uniquename":"PMID:24576557","title":"Mitochondrial membrane assembly of TMEM70 protein.","citation":"Mitochondrion 2014 Mar;15:1-9","abstract":"Dysfunction of TMEM70 disrupts the biogenesis of ATP synthase and represents the frequent cause of autosomal recessive encephalocardiomyopathy. We used tagged forms of TMEM70 and demonstrated that it has a hairpin structure with the N- and C-termini oriented towards the mitochondrial matrix. On BN-PAGE TMEM70 was detected in multiple forms including dimers and displayed partial overlap with assembled ATP synthase. Immunoprecipitation studies confirmed mutual interactions between TMEM70 molecules but, together with immunogold electron microscopy, not direct interaction with ATP synthase subunits. This indicates that the biological function of TMEM70 in the ATP synthase biogenesis may be mediated through interaction with other protein(s).","doi":"10.1016/j.mito.2014.02.010","authors":"Kratochvílová H, Hejzlarová K, Vrbacký M, Mráček T, Karbanová V, Tesařová M, Gombitová A, Cmarko D, Wittig I, Zeman J, Houštěk J","authors_abbrev":"Kratochvílová H et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-03-01","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1834.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16453698","title":"Mating pheromone-like diffusible factor released by Schizosaccharomyces pombe.","citation":"EMBO J 1986 Aug;5(8):1991-3","abstract":"We demonstrate that a diffusible factor is secreted by h cells of the fission yeast Schizosaccharomyces pombe, whose mating pheromones have not been described. This factor, tentatively named the h-factor, affects hS. pombe cells and induces their elongation under nitrogen-depleted conditions. Circumstantial evidence suggests its physiological significance in the mating process. Despite their sterility, hras1 cells secrete this factor. However, hras1 cells have apparently lost the ability to respond to it. This may suggest that the gene product of S. pombe ras1, a homologue of mammalian ras oncogenes, is involved in the mechanism for responding to mating pheromones.","authors":"Fukui Y, Kaziro Y, Yamamoto M","authors_abbrev":"Fukui Y et al.","pubmed_publication_date":"Aug 1986","pubmed_entrez_date":"1986-08-01","publication_year":"1986","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39848696","title":"Schizosaccharomyces pombe pus1 mutants are temperature sensitive due to decay of tRNAIle(UAU) by the 5'-3' exonuclease Dhp1, primarily targeting the unspliced pre-tRNA.","citation":"RNA 2025 Jan 23;","abstract":"The pseudouridylase Pus1 catalyzes pseudouridine (Ψ) formation at multiple uridine residues in tRNAs, and in some snRNAs and mRNAs. Although Pus1 is highly conserved, and mutations are associated with human disease, little is known about eukaryotic Pus1 biology. Here, we show that Schizosaccharomyces pombe pus1Δ mutants are temperature sensitive due to decay of tRNAIle(UAU), as tRNAIle(UAU) levels are reduced, and its overexpression suppresses the defect. We show that tRNAIle(UAU) is degraded by the 5'-3' exonuclease Dhp1 (ortholog of Saccharomyces cerevisiae Rat1), as each of four spontaneous pus1Δ suppressors had dhp1 mutations and restored tRNAIle(UAU) levels, and two suppressors that also restored tRNAIle(UAU) levels had mutations in tol1 (S. cerevisiae MET22 ortholog), predicted to inhibit Dhp1. We show that Pus1 modifies U27, U34, and U36 of tRNAIle(UAU), raising the question about how these modifications prevent decay. Our results suggests that Dhp1 targets unspliced pre-tRNAIle(UAU), as a pus1Δ strain in which the only copy of tRNAIle(UAU) has no intron (tI(UAU)-iΔ) is temperature resistant and undergoes no detectable decay, and the corresponding pus1Δ tI(UAU)-WT strain accumulates unspliced pre-tRNAIle(UAU). Moreover, the predicted exon-intron structure of pre-tRNAIle(UAU) differs from the canonical bulge-helix-loop structure compatible with tRNA splicing, and a pus1Δ tI(UAU)i-var strain with intron mutations predicted to improve exon-intron structure is temperature resistant and undergoes little decay. These results suggest that decay of tRNAIle(UAU) by Dhp1 in pus1Δ strains occurs at the level of unspliced pre-tRNAIle(UAU), implying a substantial role for one or more of the Ψ residues in stabilizing the pre-tRNA structure for splicing.","doi":"10.1261/rna.080315.124","authors":"Stegemann F, Marcus E, Neupert S, Ostrowski S, Mathews DH, Phizicky EM","authors_abbrev":"Stegemann F et al.","pubmed_publication_date":"23 Jan 2025","pubmed_entrez_date":"2025-01-23","publication_year":"2025","canto_session_key":"562b036a74784e05","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-01-25 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42049898","title":"RNase P/MRP subunits chaperone telomerase holoenzyme assembly in fission yeast.","citation":"EMBO Rep 2026 Apr 28;","abstract":"Telomerase biogenesis is a multistep process requiring the coordinated action of several accessory factors. In the fission yeast Schizosaccharomyces pombe, the telomerase RNA TER1 undergoes spliceosome-mediated 3'-end processing, followed by association with the Pof8/Bmc1/Thc1 complex, which facilitates binding of the Lsm2-8 complex. Lsm2-8 protects TER1 from nucleolytic degradation and promotes recruitment of the catalytic subunit Trt1. Here, we identify Pop6, Pop7, and Pop100, three subunits of the RNase P/MRP complex, as components of the active telomerase holoenzyme. These proteins associate with a stem-loop-stem structure near the TER1 pseudoknot that resembles the P3 domain found in RNase P/MRP RNAs. A single-nucleotide change within this P3-like loop disrupts Pop protein binding, resulting in reduced telomerase activity and severe telomere shortening. This mutation also impairs the assembly of key telomerase subunits and alters the folding of the template-pseudoknot region of TER1. Our findings reveal a critical role for Pop6, Pop7, and Pop100 in chaperoning TER1 into a conformation that promotes functional telomerase assembly and underscore the remarkable evolutionary plasticity of telomerase biogenesis.","doi":"10.1038/s44319-026-00782-9","authors":"Pan L, Patterson V, Möckel MM, Helston RM, Wellinger RJ, Zappulla DC, Baumann P","authors_abbrev":"Pan L et al.","pubmed_publication_date":"28 Apr 2026","pubmed_entrez_date":"2026-04-28","publication_year":"2026","canto_session_key":"9a0ddc2838a612b1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-29 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23870137","title":"Balancing chromatin remodeling and histone modifications in transcription.","citation":"Trends Genet 2013 Nov;29(11):621-9","abstract":"Chromatin remodelers use the energy of ATP hydrolysis to reposition or evict nucleosomes or to replace canonical histones with histone variants. By regulating nucleosome dynamics, remodelers gate access to the underlying DNA for replication, repair, and transcription. Nucleosomes are subject to extensive post-translational modifications that can recruit regulatory proteins or alter the local chromatin structure. Just as extensive crosstalk has been observed between different histone post-translational modifications, there is growing evidence for both coordinated and antagonistic functional relations between nucleosome remodeling and modifying machineries. Defining the combined functions of the complexes that alter nucleosome interactions, position, and stability is key to understanding processes that require access to DNA, particularly with growing appreciation of their contributions to human health and disease. Here, we highlight recent advances in the interactions between histone modifications and the imitation-switch (ISWI) and chromodomain helicase DNA-binding protein 1 (CHD1) chromatin remodelers from studies in budding yeast, fission yeast, flies, and mammalian cells, with a focus on yeast.","doi":"10.1016/j.tig.2013.06.006","authors":"Petty E, Pillus L","authors_abbrev":"Petty E et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-07-23","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11057444","title":"The genetic control of spontaneous and UV-induced mitotic intrachromosomal recombination in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 2000 Oct;38(3):113-25","abstract":"An artificially created non-tandem hetero-allelic duplication was constructed to assay mitotic intrachromosomal recombination in Schizosaccharomyces pombe. Two classes of recombinants could be distinguished: deletion-types, in which one copy of the duplicated sequence and the intervening sequence were lost, and conversion-types which retained the duplication. For spontaneous recombination, compared to wild-type cells, a rad22 mutant (corresponding to a Saccharomyces cerevisiae rad52 mutant) had wild-type levels of deletion-types, but was hypo-recombinant for conversion-types; rad16 (S. cerevisiae rad1), rad22 rad16 (S. cerevisiae rad52 rad1) and swi10 (S. cerevisiae rad10) mutants were hyper-recombinant for both types; rad22 swi10 (S. cerevisiae rad52 rad10) mutants were hypo-recombinant for both types; rhp51 (S. cerevisiae rad51) and rhp54 (S. cerevisiae rad54) mutants were hyper-recombinant for deletion-types, but almost completely lacked conversion-types. For wild-type cells, UV-irradiation induced both types of recombinant, but mainly conversion-types. All of the mutants lacked UV-induced recombination.","authors":"Osman F, Adriance M, McCready S","authors_abbrev":"Osman F et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-11-01","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4F6.15c","SPAC30D11.10","SPCC330.01c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:19713114","title":"Microtubule-dependent cell morphogenesis in the fission yeast.","citation":"Trends Cell Biol 2009 Sep;19(9):447-54","abstract":"In many systems, microtubules contribute spatial information to cell morphogenesis, for instance in cell migration and division. In rod-shaped fission yeast cells, microtubules control cell morphogenesis by transporting polarity factors, namely the Tea1-Tea4 complex, to cell tips. This complex then recruits the DYRK kinase Pom1 to cell ends. Interestingly, recent work has shown that these proteins also provide long-range spatial cues to position the division site in the middle of the cell and temporal signals to coordinate cell length with the cell cycle. Here I review how these microtubule-associated proteins form polar morphogenesis centers that control and integrate both spatial and temporal aspects of cell morphogenesis.","doi":"10.1016/j.tcb.2009.06.003","authors":"Martin SG","authors_abbrev":"Martin SG","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-08-29","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38718864","title":"H2B oncohistones cause homologous recombination defect and genomic instability through reducing H2B monoubiquitination in Schizosaccharomyces pombe.","citation":"J Biol Chem 2024 May 06;:107345","abstract":"Canonical oncohistones are histone H3 mutations in the N-terminal tail associated with tumors and affect gene expression by altering H3 post-translational modifications (PTMs) and the epigenetic landscape. Noncanonical oncohistone mutations occur in both tails and globular domains of all 4 core histones and alter gene expression by perturbing chromatin remodeling. However, the effects and mechanisms of noncanonical oncohistones remain largely unknown. Here we characterized 16 noncanonical H2B oncohistones in the fission yeast Schizosaccharomyces pombe. We found that 7 of them exhibited temperature sensitivities and 11 exhibited genotoxic sensitivities. A detailed study of 2 of these onco-mutants H2BG52D and H2BP102L revealed that they were defective in homologous recombination (HR) repair with compromised histone eviction and Rad51 recruitment. Interestingly, their genotoxic sensitivities and HR defects were rescued by inactivation of the H2BK119 deubiquitination function of Ubp8 in the Spt-Ada-Gcn5-Acetyltransferase (SAGA) complex. The levels of H2BK119 monoubiquitination (H2Bub) in the H2BG52D and H2BP102L mutants are reduced in global and local DNA break sites presumably due to enhanced recruitment of Ubp8 onto nucleosomes, and are recovered upon loss of H2B deubiquitination function of the SAGA complex. Moreover, H2BG52D and H2BP102L heterozygotes exhibit genotoxic sensitivities and reduced H2Bub in cis. We therefore conclude that H2BG52D and H2BP102L oncohistones affect HR repair and genome stability via reduction of H2Bub and propose that other noncanonical oncohistones may also affect histone PTMs to cause diseases.","doi":"10.1016/j.jbc.2024.107345","authors":"Qin B, Lu G, Chen X, Zheng C, Lin H, Liu Q, Shang J, Feng G","authors_abbrev":"Qin B et al.","pubmed_publication_date":"06 May 2024","pubmed_entrez_date":"2024-05-08","publication_year":"2024","canto_session_key":"037f5fa29955cd85","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-08-27 12:30:56","canto_approved_date":"2025-08-27 12:30:56","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-30 08:50:16","canto_added_date":"2024-05-09 23:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":450,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPAC18B11.07c","SPCC970.10c","SPAC13A11.04c","SPCC622.09","SPCC4G3.05c","SPCC18B5.11c","SPAC1952.05","SPBC32H8.12c","SPBC1734.06","SPAC22F8.12c","SPAC57A10.14","SPAC664.07c","SPBC216.05","SPCC1919.15","SPAC644.14c","SPAC11E3.04c","SPBC29A10.05","SPCC126.02c","SPCC1259.13"],"gene_count":20,"ltp_gene_count":15,"approved_date":"2025-08-27"},{"uniquename":"PMID:35359202","title":"Insights into the ecology of Schizosaccharomyces species in natural and artificial habitats.","citation":"Antonie Van Leeuwenhoek 2022 May;115(5):661-695","abstract":"The fission yeast genus Schizosaccharomyces contains important model organisms for biological research. In particular, S. pombe is a widely used model eukaryote. So far little is known about the natural and artificial habitats of species in this genus. Finding out where S. pombe and other fission yeast species occur and how they live in their habitats can promote better understanding of their biology. Here we investigate in which substrates S. pombe, S. octosporus, S. osmophilus and S. japonicus are present. To this end about 2100 samples consisting of soil, tree sap fluxes, fresh fruit, dried fruit, honey, cacao beans, molasses and other substrates were analyzed. Effective isolation methods that allow efficient isolation of the above mentioned species were developed. Based on the frequency of isolating different fission yeast species in various substrates and on extensive literature survey, conclusions are drawn on their ecology. The results suggest that the primary habitat of S. pombe and S. octosporus is honeybee honey. Both species were also frequently detected on certain dried fruit like raisins, mango or pineapple to which they could be brought by the honey bees during ripening or during drying. While S. pombe was regularly isolated from grape mash and from fermented raw cacao beans S. octosporus was never isolated from fresh fruit. The main habitat of S. osmophilus seems to be solitary bee beebread. It was rarely isolated from raisins. S. japonicus was mainly found in forest substrates although it occurs on fruit and in fruit fermentations, too.","doi":"10.1007/s10482-022-01720-0","authors":"Brysch-Herzberg M, Jia GS, Seidel M, Assali I, Du LL","authors_abbrev":"Brysch-Herzberg M et al.","pubmed_publication_date":"May 2022","pubmed_entrez_date":"2022-04-01","publication_year":"2022","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2022-04-03 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18632983","title":"Dual regulation of Mad2 localization on kinetochores by Bub1 and Dam1/DASH that ensure proper spindle interaction.","citation":"Mol Biol Cell 2008 Sep;19(9):3885-97","abstract":"The spindle assembly checkpoint monitors the state of spindle-kinetochore interaction to prevent premature onset of anaphase. Although checkpoint proteins, such as Mad2, are localized on kinetochores that do not interact properly with the spindle, it remains unknown how the checkpoint proteins recognize abnormalities in spindle-kinetochore interaction. Here, we report that Mad2 localization on kinetochores in fission yeast is regulated by two partially overlapping but distinct pathways: the Dam1/DASH and the Bub1 pathways. We show that Mad2 is localized on \"unattached\" as well as \"tensionless\" kinetochores. Our observations suggest that Bub1 is required for Mad2 to detect tensionless kinetochores, whereas Dam1/DASH is crucial for Mad2 to detect unattached kinetochores. In cells lacking both Bub1 and Dam1/DASH, Mad2 localization on kinetochores is diminished, and mitotic progression appears to be accelerated despite the frequent occurrence of abnormal chromosome segregation. Furthermore, we found that Dam1/DASH is required for promotion of spindle association with unattached kinetochores. In contrast, there is accumulating evidence that Bub1 is involved in resolution of erroneous spindle attachment on tensionless kinetochores. These pathways may act as molecular sensors determining the state of spindle association on each kinetochore, enabling proper regulation of the checkpoint activation as well as promotion/resolution of spindle attachment.","authors":"Saitoh S, Kobayashi Y, Ogiyama Y, Takahashi K","authors_abbrev":"Saitoh S et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-07-18","publication_year":"2008","canto_session_key":"226672e963bba076","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1322.12c","SPAC1805.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8876193","title":"Microtubules mediate mitochondrial distribution in fission yeast.","citation":"Proc Natl Acad Sci U S A 1996 Oct 15;93(21):11664-8","abstract":"The Schizosaccharomyces pombe mutant, ban5-4, displays aberrant mitochondrial distribution. Incubation of this conditional-lethal mutant at the nonpermissive temperature led to aggregated mitochondria that were distributed asymmetrically within the cell. Development of this mitochondrial asymmetry but not mitochondrial aggregation required progression through the cell division cycle. Genetic analysis revealed that ban5-4 is an allele of atb2 encoding alpha 2-tubulin. Consistent with this finding, cells with the cold-sensitive nda3 mutation in beta-tubulin displayed aggregated and asymmetrically distributed mitochondria after incubation at lowered temperatures. These results indicate that microtubules mediate mitochondrial distribution in fission yeast and provide the first genetic evidence for the role of microtubules in mitochondrial movement.","authors":"Yaffe MP, Harata D, Verde F, Eddison M, Toda T, Nurse P","authors_abbrev":"Yaffe MP et al.","pubmed_publication_date":"15 Oct 1996","pubmed_entrez_date":"1996-10-15","publication_year":"1996","canto_session_key":"e8bc7aa4408219ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-11-08 16:33:20","canto_approved_date":"2025-09-04 11:27:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-17 13:22:40","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":12,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.05c","SPBC25H2.13c","SPBC26H8.07c","SPBC11B10.09","SPBC21.06c","SPBC336.12c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-11-08"},{"uniquename":"PMID:10509024","title":"High-efficiency gene targeting in Schizosaccharomyces pombe using a modular, PCR-based approach with long tracts of flanking homology.","citation":"Yeast 1999 Sep 30;15(13):1419-27","abstract":"Bähler et al.(1998) recently described a PCR-based system for the deletion, tagging and overexpression of endogenous genes in the fission yeast Schizosaccharomyces pombe. A small set of PCR primers can be used to generate gene-targeting substrates from each of several modules that differ in the selectable marker (ura4(+) or kanMX6), the presence or absence of specific epitope tags (HA, Myc, GST or GFP), the position in which the epitopes will be inserted (C- or N-terminal), and the presence or absence of a regulatable promoter (the nmt1 promoter). This is a straightforward and powerful system: nine different genes were C-terminal tagged at an average efficiency of 73%, using primers producing only 60-81 bp of homology. In contrast, when studying three transcriptionally-silent genes (rec8(+), rec10(+) and rec11(+)) we obtained an average homologous integration efficiency of 4% for 12 targeting constructs when using primers that contained 80 bp of homology. By using a PCR-based increase in the amount of flanking homology to >/=250 bp, we obtained homologous integration efficiencies of up to 100%. Thus, loci of S. pombe that are refractory to gene targeting when using short tracts of homology can be readily modified by increasing the extent of homology flanking the targeting modules. This straightforward and cost-effective approach might therefore be the one of choice for the modification of S. pombe loci in general and of targeting-refractory loci in particular.","authors":"Krawchuk MD, Wahls WP","authors_abbrev":"Krawchuk MD et al.","pubmed_publication_date":"30 Sep 1999","pubmed_entrez_date":"1999-10-06","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41984257","title":"pka1 deletion induces hyperactivation of the transcription factor Mca1 and drives chromosome mis-segregation in Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2026 Apr 15;301(1)","abstract":"The online version contains supplementary material available at 10.1007/s00438-026-02379-2.","doi":"10.1007/s00438-026-02379-2","authors":"Yamawaki M, Nishioka S, Matsuo Y","authors_abbrev":"Yamawaki M et al.","pubmed_publication_date":"15 Apr 2026","pubmed_entrez_date":"2026-04-15","publication_year":"2026","canto_session_key":"a8a841d1e9cdfb10","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Matsuo","canto_first_approved_date":"2026-05-13 15:01:39","canto_approved_date":"2026-05-13 15:01:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-05-01 05:31:27","canto_added_date":"2026-04-15 23:25:05","annotation_curators":[{"name":"Yasuhiro Matsuo","community_curator":true,"annotation_count":32,"orcid":"0000-0002-2858-7179","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20H4.03c","SPBC106.10","SPAPB1A11.04c","SPAC6F12.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2026-05-13"},{"uniquename":"PMID:39461476","title":"Crystal structures of cables formed by the acetylated and unacetylated forms of the Schizosaccharomyces pombe tropomyosin orthologue Tpm Cdc8 .","citation":"J Biol Chem 2024 Oct 24;:107925","abstract":"Cables formed by head-to-tail polymerization of tropomyosin, localized along the length of sarcomeric and cytoskeletal actin filaments, play a key role in regulating a wide range of motile and contractile processes. The stability of tropomyosin cables, their interaction with actin filaments and the functional properties of the resulting co-filaments are thought to be affected by N-terminal acetylation of tropomyosin. Here, we present high-resolution structures of cables formed by acetylated and unacetylated Schizosaccharomyces pombe tropomyosin orthologue Tpm Cdc8 . The crystal structures represent different types of cables, each consisting of Tpm Cdc8  homodimers in a different conformation. The structures show how the interactions of the residues in the overlap junction contribute to cable formation and how local structural perturbations affect the conformational dynamics of the protein and its ability to transmit allosteric signals. In particular, N-terminal acetylation increases the helicity of the adjacent region, which leads to a local reduction in conformational dynamics and consequently to less fraying of the N-terminal region. This creates a more consistent complementary surface facilitating the formation of specific interactions across the overlap junction.","doi":"10.1016/j.jbc.2024.107925","authors":"Reinke PYA, Heiringhoff RS, Reindl T, Baker K, Taft MH, Meents A, Mulvihill DP, Davies OR, Fedorov R, Zahn M, Manstein DJ","authors_abbrev":"Reinke PYA et al.","pubmed_publication_date":"24 Oct 2024","pubmed_entrez_date":"2024-10-26","publication_year":"2024","canto_session_key":"215f894f8aa534b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-01-15 11:46:18","canto_approved_date":"2025-01-15 11:58:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-01-15 11:45:14","canto_added_date":"2024-10-28 00:25:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-01-15","pdb_entries":[{"pdb_id":"9ff9","gene_chains":[{"gene_uniquename":"SPAC27F1.02c","chain":"A/B","position":"1-161"}],"title":"Crystal structure of N-terminal acetylated tropomyosin Cdc8","entry_authors":"Zahn M,Heiringhoff RS,Fedorov R,Manstein DJ","entry_authors_abbrev":"Zahn M et al.","reference_uniquename":"PMID:39461476","experimental_method":"X-ray","resolution":"2.195"},{"pdb_id":"8puz","gene_chains":[{"gene_uniquename":"SPAC27F1.02c","chain":"A/B","position":"1-161"}],"title":"Crystal structure of tropomyosin (Cdc8) cables, Conformer 1","entry_authors":"Reinke PYA,Zahn M,Fedorov R,Manstein DJ","entry_authors_abbrev":"Reinke PYA et al.","reference_uniquename":"PMID:39461476","experimental_method":"X-ray","resolution":"2.2"},{"pdb_id":"8pv0","gene_chains":[{"gene_uniquename":"SPAC27F1.02c","chain":"A/B/C/D","position":"1-161"}],"title":"Crystal structure of tropomyosin (Cdc8) cables, Conformers 2 and 3","entry_authors":"Reinke PYA,Zahn M,Fedorov R,Manstein DJ","entry_authors_abbrev":"Reinke PYA et al.","reference_uniquename":"PMID:39461476","experimental_method":"X-ray","resolution":"2.43"}]},{"uniquename":"PMID:27031513","title":"Difference in the late ergosterol biosynthesis between yeast spheroplasts and intact cells.","citation":"Acta Biochim Pol 2016;63(2):371-5","abstract":"A comparative study on post-squalene sterol synthesis in intact yeast cells and spheroplasts was carried out with strains from three genera (Saccharomyces cerevisiae, Schizosaccharomyces pombe, Pichia pastoris) as well as with engineered S. cerevisiae cells altered in regard to the late ergosterol synthesis pathway. A common outcome of incubation experiments with radioactive acetate was that in intact cells the metabolic pathway flows till its specific end product (ergosterol and its precursor, depending on the enzyme deficiency), whereas in spheroplasts the pathway was stalled some step upstream. For example, in spheroplasts from wt strains, non-cyclic triterpenes squalene and oxidosqualene accumulated as though the metabolic path was kept from producing steroid-shaped molecules different from the end product. Accumulation of non-cyclic triterpenes was observed also in spheroplasts from S. cerevisiae cells lacking 3-ketosteroid reductase activity, an enzyme belonging to the C4-demethylase complex. When production of cyclic triterpenes was compromised by loss or poor functionality of oxidosqualene cyclase (EC 5.4.99.7), the difference between intact cells and spheroplasts was still remarkable, yet limited to the different oxido/dioxidosqualene ratio. The characteristics of spheroplasts as non-proliferating cells may partially explain the observed differences in post-squalene pathway from intact cells. We cannot say if the difference in metabolic pathways in spheroplasts and intact cells is a rule. We think, however, that it is worthwhile to search for an answer, as a wider picture of the points where the metabolic pathways are stalled in spheroplasts could provide original ideas about the metabolic network in yeast.","doi":"10.18388/abp.2015_1213","authors":"Ferrante T, Viola F, Balliano G, Oliaro-Bosso S","authors_abbrev":"Ferrante T et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-04-01","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-04-02 00:15:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40760724","title":"Effects of chromosome number reduction on mitotic and meiotic stability in fission yeast.","citation":"Genome Biol 2025 Aug 04;26(1):232","abstract":"Genetic information is stored on multiple chromosomes in eukaryotic organisms and is passed on to offspring through cell division. How chromosome number influences cell division and chromosome segregation is not yet understood.\nIn this study, we use artificial chromosome-fusion fission yeast cells, which contain one or two chromosomes, as models to investigate the effects of a reduced chromosome number on mitosis and meiosis. In mitosis, chromosome number reduction, particularly full fusion into one chromosome, prolongs mitotic duration in a manner dependent on the spindle assembly checkpoint and improves chromosome segregation accuracy in spindle assembly checkpoint-deficient cells. By contrast, in meiosis, chromosome number reduction impairs prophase oscillatory nuclear movement, prolongs meiosis I duration but shortens meiosis II duration, and severely compromises meiosis I chromosome segregation.\nOur work uncovers different effects of reduced chromosome number on mitotic and meiotic stability and offers insights into how organisms may select the appropriate number of chromosomes in evolution.","doi":"10.1186/s13059-025-03704-5","authors":"Jiang Y, Jian Y, Nie L, Gu X, Lu Z, Chu Y, Liu X, Yao X, Zhou JQ, Zheng S, Fu C","authors_abbrev":"Jiang Y et al.","pubmed_publication_date":"04 Aug 2025","pubmed_entrez_date":"2025-08-05","publication_year":"2025","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2025-08-05 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10864871","title":"Requirement of Mis6 centromere connector for localizing a CENP-A-like protein in fission yeast.","citation":"Science 2000 Jun 23;288(5474):2215-9","abstract":"Mammalian kinetochores contain the centromere-specific histone H3 variant CENP-A, whose incorporation into limited chromosomal regions may be important for centromere function and chromosome segregation during mitosis. However, regulation of CENP-A localization and its role have not been clear. Here we report that the fission yeast homolog SpCENP-A is essential for establishing centromere chromatin associated with equal chromosome segregation. SpCENP-A binding to the nonrepetitious inner centromeres depended on Mis6, an essential centromere connector protein acting during G1-S phase of the cell cycle. Mis6 is likely required for recruiting SpCENP-A to form proper connection of sister centromeres.","authors":"Takahashi K, Chen ES, Yanagida M","authors_abbrev":"Takahashi K et al.","pubmed_publication_date":"23 Jun 2000","pubmed_entrez_date":"2000-06-24","publication_year":"2000","canto_session_key":"c9666a1ab5592282","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-01-23 14:13:28","canto_approved_date":"2022-10-06 10:02:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-15 16:39:56","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.17","SPBC409.04c","SPAC1687.20c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-01-23"},{"uniquename":"PMID:20173420","title":"Plant-specific multisubunit RNA polymerase in gene silencing.","citation":"Epigenetics 2010 Jan 01;5(1):4-8","abstract":"In recent years, a major breakthrough in the study of epigenetic silencing in eukaryotes came with the discovery that the RNA-interference pathway (RNAi) is generally implicated in heterochromatin assembly and gene silencing. An important and paradoxical feature of the RNAi-mediated heterochromatin pathways is their requirement for some form of transcription. In fission yeast, Schizosaccharomyces pombe, centromeric siRNAs have been shown to derive from chromatin-bound nascent transcripts produced by RNA polymerase II (PolII) at the site of heterochromatin formation. Likewise, chromatin-bound nascent transcripts generated by a PolII-related DNA-dependent RNA polymerase, known as PolIVb/PolV, have recently been implicated in RNA-directed DNA methylation (RdDM), the prominent RNAi-mediated chromatin pathway in plants. In this review we discuss recent work on the plant-specific PolII variant enzymes and discuss the mechanistic convergences that have been observed in the role of these enzymes in their respective siRNA-mediated heterochromatin formation pathways.","authors":"Lahmy S, Bies-Etheve N, Lagrange T","authors_abbrev":"Lahmy S et al.","pubmed_publication_date":"01 Jan 2010","pubmed_entrez_date":"2010-02-23","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21892171","title":"Defects in RNA quality control factors reveal RNAi-independent nucleation of heterochromatin.","citation":"Nat Struct Mol Biol 2011 Sep 04;18(10):1132-8","abstract":"Heterochromatin assembly at Schizosaccharomyces pombe centromeres involves a self-reinforcing loop mechanism wherein chromatin-bound RNAi factors facilitate targeting of Clr4-Rik1 methyltransferase. However, the initial nucleation of heterochromatin has remained elusive. We show that cells lacking Mlo3, a protein involved in mRNP biogenesis and RNA quality control, assemble functional heterochromatin in RNAi-deficient cells. Heterochromatin restoration is linked to RNA surveillance because loss of Mlo3-associated TRAMP also rescues heterochromatin defects of RNAi mutants. mlo3Δ, which causes accumulation of bidirectional repeat-transcripts, restores Rik1 enrichment at repeats and triggers de novo heterochromatin formation in the absence of RNAi. RNAi-independent heterochromatin nucleation occurs at selected euchromatic loci that show upregulation of antisense RNAs in mlo3Δ cells. We find that the exosome RNA degradation machinery acts parallel to RNAi to promote heterochromatin formation at centromeres. These results suggest that RNAi-independent mechanisms exploit transcription and non-coding RNAs to nucleate heterochromatin.","doi":"10.1038/nsmb.2122","authors":"Reyes-Turcu FE, Zhang K, Zofall M, Chen E, Grewal SI","authors_abbrev":"Reyes-Turcu FE et al.","pubmed_publication_date":"04 Sep 2011","pubmed_entrez_date":"2011-09-06","publication_year":"2011","canto_session_key":"1456d39b083c07d3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-16 15:59:12","canto_approved_date":"2025-05-27 14:21:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-16 15:55:46","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPBC428.08c","SPAC20H4.03c","SPBC1D7.04","SPCC736.11","SPCC188.13c","SPAC1F3.01","SPBP8B7.21","SPCC11E10.08","SPAC12G12.13c","SPBC28F2.12"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2024-01-16"},{"uniquename":"PMID:16918916","title":"A Bayesian mixture model for partitioning gene expression data.","citation":"Biometrics 2006 Jun;62(2):515-25","abstract":"In recent years there has been great interest in making inference for gene expression data collected over time. In this article, we describe a Bayesian hierarchical mixture model for partitioning such data. While conventional approaches cluster the observed data, we assume a nonparametric, random walk model, and partition on the basis of the parameters of this model. The model is flexible and can be tuned to the specific context, respects the order of observations within each curve, acknowledges measurement error, and allows prior knowledge on parameters to be incorporated. The number of partitions may also be treated as unknown, and inferred from the data, in which case computation is carried out via a birth-death Markov chain Monte Carlo algorithm. We first examine the behavior of the model on simulated data, along with a comparison with more conventional approaches, and then analyze meiotic expression data collected over time on fission yeast genes.","authors":"Zhou C, Wakefield J","authors_abbrev":"Zhou C et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-08-22","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6447701","title":"The purified plasma membrane ATPase of the yeast Schizosaccharomyces pombe forms a phosphorylated intermediate.","citation":"J Biol Chem 1980 Oct 10;255(19):9353-7","abstract":"An acid slab gel electrophoresis method of high-resolving power allows detection of a phosphorylated form in the purified ATPase of the yeast Schizosaccharomyces pombe and identification of this catalytic intermediate among the different phosphopeptides of a plasma membrane preparation. At a maximum steady state rate of MgATP hydrolysis by the membrane-bound ATPase, 20 to 40% of the ATPase subunits of 100,000 daltons are in a phosphorylated form, while only 0.8% of the subunits of the purified ATPase are phosphorylated under the same conditions. The phosphorylated intermediate reaches the steady state level in less than 2 s and rapidly turns over. The phosphorylated substance is cleaved by hydroxylamine and is relatively stable in acids but is readily hydrolyzed in alkaline or in acid alcoholic media. These results suggest that the intermediate is an acylphosphate. The phosphorylation reaction has an apparent Km value of 3.0 mM MgATP for the plasma membrane-bound ATPase and 0.6 mM MgATP for the purified ATPase. Plasma membranes contain several other minor phosphorylated components whose kinetic behavior is typical of phosphorylation by protein kinase. Artifactual production of two forms of the ATPase by phenylmethanesulfonyl fluoride-sensitive proteases liberated during cell disruption is also demonstrated.","authors":"Amory A, Foury F, Goffeau A","authors_abbrev":"Amory A et al.","pubmed_publication_date":"10 Oct 1980","pubmed_entrez_date":"1980-10-10","publication_year":"1980","canto_session_key":"0c20cb59f36238e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-28 13:43:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-28 13:43:06","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-28"},{"uniquename":"PMID:2894685","title":"Control over the onset of DNA synthesis in fission yeast.","citation":"Philos Trans R Soc Lond B Biol Sci 1987 Dec 15;317(1187):507-16","abstract":"The fission yeast Schizosaccharomyces pombe has been used to identify gene functions required for the cell to become committed to the mitotic cell cycle and to initiate the processes leading to chromosome replication in S-phase. Two gene functions cdc2 and cdc10 must be executed for the cell to traverse 'start' and proceed from G1 into S-phase. Before the completion of these two functions the cell is in an uncommitted state and can undergo alternative developmental fates such as conjugation. A third gene, suc1, has also been identified whose product may interact directly with that of cdc2 at 'start'. The molecular functions of the genes involved in the completion of 'start' have been investigated. The cdc2 gene has been shown to be a protein kinase, suggesting that phosphorylation may be involved in the control over the transition from G1 into S-phase. The biochemical functions of the cdc10 and suc1 gene products have not yet been elucidated. A control at 'start' has also been shown to exist in the budding yeast Saccharomyces cerevisiae. Traverse of 'start' requires the execution of the CDC28 gene function. The cdc2 and CDC28 gene products (lower-case letters represent genes of Schizosaccharomyces pombe, and capital letters genes of Saccharomyces cerevisiae) are functionally homologous, suggesting that the processes involved in traverse of 'start' are highly conserved. An analogous control may also exist in the G1 period of mammalian cells, suggesting that the 'start' control step, after which cells become committed to the mitotic cell cycle, may have been conserved through evolution.","authors":"Simanis V, Hayles J, Nurse P","authors_abbrev":"Simanis V et al.","pubmed_publication_date":"15 Dec 1987","pubmed_entrez_date":"1987-12-15","publication_year":"1987","canto_session_key":"0e7635c95c54dded","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-10-08 14:54:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-26 10:00:18","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC1734.14c","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2015-08-26"},{"uniquename":"PMID:25916890","title":"A sigmoidal model for biosorption of heavy metal cations from aqueous media.","citation":"Math Biosci 2015 Jul;265:40-6","abstract":"A novel multi-input single output (MISO) black-box sigmoid model is developed to simulate the biosorption of heavy metal cations by the fission yeast from aqueous medium. Validation and verification of the model is done through statistical chi-squared hypothesis tests and the model is evaluated by uncertainty and sensitivity analyses. The simulated results are in agreement with the data of the studied system in which Schizosaccharomyces pombe biosorbs Ni(II) cations at various process conditions. Experimental data is obtained originally for this work using dead cells of an adapted variant of S. Pombe and represented by Freundlich isotherms. A process optimization scheme is proposed using the present model to build a novel application of a cost-merit objective function which would be useful to predict optimal operation conditions.","doi":"10.1016/j.mbs.2015.04.007","authors":"Özen R, Sayar NA, Durmaz-Sam S, Sayar AA","authors_abbrev":"Özen R et al.","pubmed_publication_date":"Jul 2015","pubmed_entrez_date":"2015-04-29","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-04-30 00:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28338982","title":"RNA Editing During Sexual Development Occurs in Distantly Related Filamentous Ascomycetes.","citation":"Genome Biol Evol 2017 Apr 01;9(4):855-868","abstract":"RNA editing is a post-transcriptional process that modifies RNA molecules leading to transcript sequences that differ from their template DNA. A-to-I editing was found to be widely distributed in nuclear transcripts of metazoa, but was detected in fungi only recently in a study of the filamentous ascomycete Fusarium graminearum that revealed extensive A-to-I editing of mRNAs in sexual structures (fruiting bodies). Here, we searched for putative RNA editing events in RNA-seq data from Sordaria macrospora and Pyronema confluens, two distantly related filamentous ascomycetes, and in data from the Taphrinomycete Schizosaccharomyces pombe. Like F. graminearum, S. macrospora is a member of the Sordariomycetes, whereas P. confluens belongs to the early-diverging group of Pezizomycetes. We found extensive A-to-I editing in RNA-seq data from sexual mycelium from both filamentous ascomycetes, but not in vegetative structures. A-to-I editing was not detected in different stages of meiosis of S. pombe. A comparison of A-to-I editing in S. macrospora with F. graminearum and P. confluens, respectively, revealed little conservation of individual editing sites. An analysis of RNA-seq data from two sterile developmental mutants of S. macrospora showed that A-to-I editing is strongly reduced in these strains. Sequencing of cDNA fragments containing more than one editing site from P. confluens showed that at the beginning of sexual development, transcripts were incompletely edited or unedited, whereas in later stages transcripts were more extensively edited. Taken together, these data suggest that A-to-I RNA editing is an evolutionary conserved feature during fruiting body development in filamentous ascomycetes.","doi":"10.1093/gbe/evx052","authors":"Teichert I, Dahlmann TA, Kück U, Nowrousian M","authors_abbrev":"Teichert I et al.","pubmed_publication_date":"01 Apr 2017","pubmed_entrez_date":"2017-03-25","publication_year":"2017","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2017-03-27 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18331722","title":"A mutual inhibition between APC/C and its substrate Mes1 required for meiotic progression in fission yeast.","citation":"Dev Cell 2008 Mar;14(3):446-54","abstract":"The anaphase-promoting complex/cyclosome (APC/C) is a cell-cycle-regulated essential E3 ubiquitin ligase; however, very little is known about its meiotic regulation. Here we show that fission yeast Mes1 is a substrate of the APC/C as well as an inhibitor, allowing autoregulation of the APC/C in meiosis. Both traits require a functional destruction box (D box) and KEN box. We show that Mes1 directly binds the WD40 domain of the Fizzy family of APC/C activators. Intriguingly, expression of nonubiquitylatable Mes1 blocks cells in metaphase I with high levels of APC/C substrates, suggesting that ubiquitylation of Mes1 is required for partial degradation of cyclin B in meiosis I by alleviating Mes1 inhibitory function. Consistently, a ternary complex, APC/C-Fizzy/Cdc20-Mes1, is stabilized by inhibiting Mes1 ubiquitylation. These results demonstrate that the fine-tuning of the APC/C activity, by a substrate that is also an inhibitor, is required for the precise coordination and transition through meiosis.","doi":"10.1016/j.devcel.2007.12.010","authors":"Kimata Y, Trickey M, Izawa D, Gannon J, Yamamoto M, Yamano H","authors_abbrev":"Kimata Y et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-03-12","publication_year":"2008","canto_session_key":"28d952f6d70d5b8f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-07-13 07:58:02","canto_approved_date":"2025-09-04 09:24:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-13 07:57:55","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":43,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.08c","SPBC25H2.13c","SPAC17C9.01c","SPAC5D6.08c","SPBC14C8.01c","SPBC1198.12","SPBC582.03"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2019-07-13"},{"uniquename":"Pfam:PF03987","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC227.04","YLL042C"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17038309","title":"Evolutionary and functional conservation of the DNA non-homologous end-joining protein, XLF/Cernunnos.","citation":"J Biol Chem 2006 Dec 08;281(49):37517-26","abstract":"Non-homologous end-joining is a major pathway of DNA double-strand break repair in mammalian cells, deficiency in which confers radiosensitivity and immune deficiency at the whole organism level. A core protein complex comprising the Ku70/80 heterodimer together with a complex between DNA ligase IV and XRCC4 is conserved throughout eukaryotes and assembles at double-strand breaks to mediate ligation of broken DNA ends. In Saccharomyces cerevisiae an additional NHEJ protein, Nej1p, physically interacts with the ligase IV complex and is required in vivo for ligation of DNA double-strand breaks. Recent studies with cells derived from radiosensitive and immune-deficient patients have identified the human protein, XLF (also named Cernunnos), as a crucial NHEJ protein. Here we show that XLF and Nej1p are members of the same protein superfamily and that this family has members in diverse eukaryotes. Indeed, we show that a member of this family encoded by a previously uncharacterized open-reading frame in the Schizosaccharomyces pombe genome is required for NHEJ in this organism. Furthermore, our data reveal that XLF family proteins can bind to DNA and directly interact with the ligase IV-XRCC4 complex to promote DSB ligation. We therefore conclude that XLF family proteins interact with the ligase IV-XRCC4 complex to constitute the evolutionarily conserved enzymatic core of the NHEJ machinery.","authors":"Hentges P, Ahnesorg P, Pitcher RS, Bruce CK, Kysela B, Green AJ, Bianchi J, Wilson TE, Jackson SP, Doherty AJ","authors_abbrev":"Hentges P et al.","pubmed_publication_date":"08 Dec 2006","pubmed_entrez_date":"2006-10-14","publication_year":"2006","canto_session_key":"c49a19fd6aa23bc4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pierre Hentges","canto_approved_date":"2015-07-29 13:34:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-28 11:55:22","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pierre Hentges","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC24B10.14c","SPCC1183.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-07-28"},{"uniquename":"PMID:14680630","title":"Structure and function of the conserved core of histone deposition protein Asf1.","citation":"Curr Biol 2003 Dec 16;13(24):2148-58","abstract":"Asf1 is a ubiquitous eukaryotic histone binding and deposition protein that mediates nucleosome formation in vitro and is required for genome stability in vivo. Studies in a variety of organisms have defined Asf1's role as a histone chaperone during DNA replication through specific interactions with histones H3/H4 and the histone deposition factor CAF-I. In addition to its role in replication, conserved interactions with proteins involved in chromatin silencing, transcription, chromatin remodeling, and DNA repair have also established Asf1 as an important component of a number of chromatin assembly and modulation complexes.\nWe demonstrate that the highly conserved N-terminal domain of S. cerevisiae Asf1 (Asf1N) is the core region that mediates all tested functions of the full-length protein. The crystal structure of this core domain, determined to 1.5 A resolution, reveals a compact immunoglobulin-like beta sandwich fold topped by three helical linkers. The surface of Asf1 displays a conserved hydrophobic groove flanked on one side by an area of strong electronegative surface potential. These regions represent potential binding sites for histones and other interacting proteins. The structural model also allowed us to interpret mutagenesis studies of the human Asf1a/HIRA interaction and to functionally define the region of Asf1 responsible for Hir1-dependent telomeric silencing in budding yeast.\nThe evolutionarily conserved, N-terminal 155 amino acids of histone deposition protein Asf1 are functional in vitro and in vivo. This core region of Asf1 adopts a compact immunoglobulin-fold structure with distinct surface characteristics, including a Hir protein binding region required for gene silencing.","authors":"Daganzo SM, Erzberger JP, Lam WM, Skordalakes E, Zhang R, Franco AA, Brill SJ, Adams PD, Berger JM, Kaufman PD","authors_abbrev":"Daganzo SM et al.","pubmed_publication_date":"16 Dec 2003","pubmed_entrez_date":"2003-12-19","publication_year":"2003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC663.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9509424","title":"Isolation of synthetic lethal mutants of ras1 in Schizosaccharomyces pombe.","citation":"Mol Cells 1997 Dec 31;7(6):800-6","abstract":"Ras proteins are membrane-associated guanine nucleotide-binding proteins that serve as molecular switches for signal transduction pathways in a diverse array of organisms. Various cellular factors are known to interact with Ras proteins. In order to find the novel cellular factors that are associated with Ras function, we have constructed synthetic lethal mutants of the ras1+ gene in Schizosaccharomyces pombe and used them to identify the genes that are functionally dependent on the Ras1. We first constructed S. pombe strains in which chromosomal ras1+ gene is placed under the nmt1 promoter that is regulated by thiamine. This strain shows ras1+ phenotype in the absence of thiamine, whereas it shows ras1- phenotype in the presence of thiamine. Second, we mutated the constructed strains with ultraviolet light (UV) and selected two synthetic lethal mutants that could not grow when Ras1 function was repressed (ras1-). One of the mutants, KSC3, showed a swollen cell shape, aberrant deposition of septum materials, and aberrant nuclei. The other mutant, KSC4, showed sensitivity to hyper-osmolarity when Ras1 function is absent. These mutants, however, grow normally when Ras1 is expressed (ras1+). These two novel synthetic lethal mutants of ras1 provide the means to isolate the corresponding genes that function in association with Ras1 in S. pombe. Screening of a genomic library of S. pombe complementing the mutant phenotype allowed us to identify several novel genes associated with Ras1 of S. pombe.","authors":"Chung KS, Kim KW, Yoo HS","authors_abbrev":"Chung KS et al.","pubmed_publication_date":"31 Dec 1997","pubmed_entrez_date":"1998-03-24","publication_year":"1997","canto_session_key":"a3d55040ee3e735e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-04-22 10:30:48","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-22 10:30:42","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.09c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-04-22"},{"uniquename":"PMID:9799358","title":"Cdm1, the smallest subunit of DNA polymerase d in the fission yeast Schizosaccharomyces pombe, is non-essential for growth and division.","citation":"Curr Genet 1998 Oct;34(4):250-8","abstract":"Highly purified DNA polymerase delta from the fission yeast Schizosaccharomyces pombe is a complex of at least four distinct subunits. Genes encoding three of these (pol3+/cdc6+, cdc1+ and cdc27+) have been characterised previously. Here we describe the isolation and characterisation of cdm1+, the gene encoding the smallest (22kDa) subunit of the Pol delta complex. Over-expression of cdm1+, which encodes a 160 amino-acid protein with no significant sequence similarity to proteins in current databases, is able to rescue cells carrying temperature-sensitive mutations in either pol3+/cdc6+, cdc1+ or cdc27+. Cells deleted for cdm1+ are viable, indicating that cdm1+ is non-essential for mitotic growth, and are no more sensitive to a variety of DNA replication inhibitors and DNA damaging agents than are wild-type cells. In addition, over-expression of cdm1+ suppresses the temperature-sensitive cdc24-M38 mutant suggesting that cdc24+ may also have a role in DNA polymerase delta function.","authors":"Reynolds N, Watt A, Fantes PA, MacNeill SA","authors_abbrev":"Reynolds N et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-11-03","publication_year":"1998","canto_session_key":"8806795bb66d255f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-09 15:33:00","canto_approved_date":"2020-01-27 12:13:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-04-09 15:32:54","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.02c","SPBC336.04","SPAC27E2.05","SPAC8F11.07c","SPBC1734.02c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-04-09"},{"uniquename":"PMID:22754237","title":"Methylenetetrahydrofolate reductase mutations, a genetic cause for familial recurrent neural tube defects.","citation":"Indian J Hum Genet 2012 Jan;18(1):122-4","abstract":"Methylenetetrahydrofolate reductase (MTHFR) gene mutations have been implicated as risk factors for neural tube defects (NTDs). The best-characterized MTHFR genetic mutation 677C→T is associated with a 2-4 fold increased risk of NTD if patient is homozygous for this mutation. This risk factor is modulated by folate levels in the body. A second mutation in the MTHFR gene is an A→C transition at position 1298. The 1298A→C mutation is also a risk factor for NTD, but with a smaller relative risk than 677C→T mutation. Under conditions of low folate intake or high folate requirements, such as pregnancy, this mutation could become of clinical importance. We present a case report with MTHFR genetic mutation, who presented with recurrent familial pregnancy losses due to anencephaly/NTDs.","doi":"10.4103/0971-6866.96680","authors":"Yaliwal LV, Desai RM","authors_abbrev":"Yaliwal LV et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2012-07-04","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC343.10","SPAC56F8.10"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:1863602","title":"Genetic and biochemical analysis of the adenylyl cyclase of Schizosaccharomyces pombe.","citation":"Cell Regul 1991 Feb;2(2):155-64","abstract":"The adenylyl cyclase gene, cyr1, of Schizosaccharomyces pombe has been cloned. We have begun an analysis of the function and regulation of adenylyl cyclase by disrupting this gene and by over-expressing all or parts of this gene in various strains. cyr1- strains are viable and contain no measurable cyclic AMP. They conjugate and sporulate under conditions that normally inhibit wild-type strains. Strains containing the cyr1 coding sequences transcribed from the strong adh1 promoter contain greatly elevated adenylyl cyclase activity, as measured in vitro, but only modestly elevated cAMP levels. Such strains conjugate and sporulate less frequently than wild-type cells upon nutrient limitation. Strains which carry the wild-type cyr1 gene but that also express high levels of the amino terminal domain of adenylyl cyclase behave much like cyr1-strains, suggesting that the amino terminal domain can bind a positive regulator. A protein that copurifies with the adenylyl cyclase of S. pombe cross-reacts to antiserum raised against the S. cerevisiae adenylyl cyclase-associated regulatory protein, CAP.","authors":"Kawamukai M, Ferguson K, Wigler M, Young D","authors_abbrev":"Kawamukai M et al.","pubmed_publication_date":"Feb 1991","pubmed_entrez_date":"1991-02-01","publication_year":"1991","canto_session_key":"cfe162f89d8c435c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-05-15 20:57:19","canto_approved_date":"2026-04-08 08:04:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-28 14:05:37","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.03","SPBC19C7.03","SPAC17H9.09c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-05-15"},{"uniquename":"PMID:34663418","title":"The chromatin remodeler Ino80 mediates RNAPII pausing site determination.","citation":"Genome Biol 2021 Oct 18;22(1):294","abstract":"Promoter-proximal pausing of RNA polymerase II (RNAPII) is a critical step for the precise regulation of gene expression. Despite the apparent close relationship between promoter-proximal pausing and nucleosome, the role of chromatin remodeler governing this step has mainly remained elusive.\nHere, we report highly confined RNAPII enrichments downstream of the transcriptional start site in Saccharomyces cerevisiae using PRO-seq experiments. This non-uniform distribution of RNAPII exhibits both similar and different characteristics with promoter-proximal pausing in Schizosaccharomyces pombe and metazoans. Interestingly, we find that Ino80p knockdown causes a significant upstream transition of promoter-proximal RNAPII for a subset of genes, relocating RNAPII from the main pausing site to the alternative pausing site. The proper positioning of RNAPII is largely dependent on nucleosome context. We reveal that the alternative pausing site is closely associated with the + 1 nucleosome, and nucleosome architecture around the main pausing site of these genes is highly phased. In addition, Ino80p knockdown results in an increase in fuzziness and a decrease in stability of the + 1 nucleosome. Furthermore, the loss of INO80 also leads to the shift of promoter-proximal RNAPII toward the alternative pausing site in mouse embryonic stem cells.\nBased on our collective results, we hypothesize that the highly conserved chromatin remodeler Ino80p is essential in establishing intact RNAPII pausing during early transcription elongation in various organisms, from budding yeast to mouse.","doi":"10.1186/s13059-021-02500-1","authors":"Cheon Y, Han S, Kim T, Hwang D, Lee D","authors_abbrev":"Cheon Y et al.","pubmed_publication_date":"18 Oct 2021","pubmed_entrez_date":"2021-10-19","publication_year":"2021","canto_session_key":"3878167ade0ae537","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-10-23 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28357352","title":"Chromatin binding and silencing: Two roles of the same protein Lem2.","citation":"Microb Cell 2016 Apr 04;3(4):185-188","abstract":"Transcriptionally repressed chromatin localizes to specific areas within the eukaryotic nucleus and is often found at the nuclear periphery, which is thought to provide a specialized compartment for gene silencing. However, the molecular mechanisms that establish this spatial chromatin organization are still poorly understood. In our recent work (Barrales  et al.  2016), we identified the nuclear envelope protein Lem2, a homolog of metazoan lamin-associated proteins (LAPs), as a relevant factor for heterochromatin silencing and perinuclear localization in the fission yeast  Schizosaccharomyces pombe . Several other LAPs have previously been reported to associate with heterochromatin, and it has been proposed that this interaction might directly contribute to gene repression, perhaps through tethering via chromatin-binding domains like the LEM domain. We demonstrated that the LEM domain of Lem2 is indeed essential for centromere binding and perinuclear tethering. However, we made the surprising finding that tethering via the LEM domain is functionally independent of Lem2's role in silencing, which instead is mediated by a different part of the protein, the MSC domain. Our study demonstrates that tethering and silencing, although mediated by the same molecule, Lem2, can be mechanistically separated. This further unveils a complex function of this protein at the interface between the nuclear periphery and silent chromatin, which might be preserved among the other members of this conserved family of LEM proteins.","doi":"10.15698/mic2016.04.495","authors":"Barrales RR, Braun S","authors_abbrev":"Barrales RR et al.","pubmed_publication_date":"04 Apr 2016","pubmed_entrez_date":"2017-03-31","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-04-01 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15882446","title":"Brl1p -- a novel nuclear envelope protein required for nuclear transport.","citation":"Traffic 2005 Jun;6(6):502-17","abstract":"In this article, we identify a cold-sensitive mutant of Xpo1p designated as xop1-2 (but will be referred to from here on as xpo1-ok) that is synthetically lethal with srm1-1, a Saccharomyces cerevisiae RCC1 homolog. xpo1-ok was a novel mutated allele with a single point mutation, T283P. Suppressors of xpo1-ok were isolated, and one of them was found to encode a novel nuclear envelope integral membrane protein designated as Brl1p (Brr6 like protein no. 1). Brl1p is homologous with Brr6p at the C-terminal domain, which is well conserved in the Brr6/Brl1 family. To characterize the function of Brl1p, a series of temperature-sensitive mutants of Brl1p were isolated. All of brl1 mutations were localized to the conserved C-terminal domain that is essential for a function of Brl1p. Some brl1 alleles showed defects in nuclear export of either mRNA or protein, and nuclear pore clustering, similar to brr6-1. The cellular localization of Brl1p is also similar to that of Brr6p. The genetic analysis suggested that Brl1p functionally interacts with Brr6p. An interaction of Brl1p with Brr6p was shown by the two-hybrid method. We hypothesize that Brl1p functions for nuclear export as a complex with Brr6p.","authors":"Saitoh YH, Ogawa K, Nishimoto T","authors_abbrev":"Saitoh YH et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-05-11","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YHR036W","YGL247W","SPAC8F11.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2406029","title":"Mutation of fission yeast cell cycle control genes abolishes dependence of mitosis on DNA replication.","citation":"Cell 1990 Feb 23;60(4):665-73","abstract":"Entry into mitosis in fission yeast is controlled by the p34cdc2 protein kinase, which is activated by cdc25+ and inhibited by wee1+. In \"wee\" mutants one or the other of these controls is circumvented resulting in advancement of mitosis. We report that dependence of mitosis on DNA synthesis is lost in wee mutants in which cdc25+ control is circumvented either by mutations in cdc2+ or by overproduction of cdc25+. In contrast, dependence is maintained when the wee1+ control is bypassed. We propose that cdc25+ activity requires completion of earlier cell-cycle events such as DNA synthesis, and thus links p34cdc2 kinase activation to completion of these earlier events. Constitutive expression of cdc25+ homologs could explain why mitosis is not dependent on DNA replication in some early embryos.","authors":"Enoch T, Nurse P","authors_abbrev":"Enoch T et al.","pubmed_publication_date":"23 Feb 1990","pubmed_entrez_date":"1990-02-23","publication_year":"1990","canto_session_key":"2db803bca64eaafd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-22 13:47:01","canto_approved_date":"2026-02-09 11:05:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-09-19 14:33:35","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPCC18B5.03","SPAC1F7.05","SPBC11B10.09","SPBC25H2.13c","SPAC20G8.01","SPAC24H6.05","SPAC644.06c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-12-22"},{"uniquename":"PMID:18604477","title":"Appropriate sampling for intracellular amino acid analysis in five phylogenetically different yeasts.","citation":"Biotechnol Lett 2008 Nov;30(11):1993-2000","abstract":"Methanol quenching and fast filtration, the two most common sampling protocols in microbial metabolome analysis, were validated for intracellular amino acid analysis in phylogenetically different yeast strains comprising Saccharomyces cerevisiae, Kluyveromyces marxianus, Pichia pastoris, Schizosaccharomyces pombe and Zygosaccharomyces bailii. With only few exceptions for selected amino acids, all yeasts exhibited negligible metabolite leakage during quenching with 60% cold buffered methanol. Slightly higher leakage was observed with increasing methanol content in the quenching solution. Fast filtration resulted in identical levels for intracellular amino acids in all strains tested. The results clearly demonstrate the validity of both approaches for leakage-free sampling of amino acids in yeast.","doi":"10.1007/s10529-008-9789-z","authors":"Bolten CJ, Wittmann C","authors_abbrev":"Bolten CJ et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-07-08","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21217703","title":"A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms.","citation":"Nat Struct Mol Biol 2011 Feb;18(2):213-21","abstract":"Repressor activator protein 1 (RAP1) is the most highly conserved telomere protein. It is involved in protecting chromosome ends in fission yeast and promoting gene silencing in Saccharomyces cerevisiae, whereas it represses homology-directed recombination at telomeres in mammals. To understand how RAP1 has such diverse functions at telomeres, we solved the crystal or solution structures of the RAP1 C-terminal (RCT) domains of RAP1 from multiple organisms in complex with their respective protein-binding partners. Our analysis establishes RAP1(RCT) as an evolutionarily conserved protein-protein interaction module. In mammalian and fission yeast cells, this module interacts with TRF2 and Taz1, respectively, targeting RAP1 to chromosome ends for telomere protection. In contrast, S. cerevisiae RAP1 uses its RCT domain to recruit Sir3 to telomeres to mediate gene silencing. Together, our results show that, depending on the organism, the evolutionarily conserved RAP1 RCT motif has diverse functional roles at telomeres.","doi":"10.1038/nsmb.1974","authors":"Chen Y, Rai R, Zhou ZR, Kanoh J, Ribeyre C, Yang Y, Zheng H, Damay P, Wang F, Tsujii H, Hiraoka Y, Shore D, Hu HY, Chang S, Lei M","authors_abbrev":"Chen Y et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2011-01-11","publication_year":"2011","canto_session_key":"eb3460dd813ce225","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-16 14:30:23","canto_approved_date":"2023-03-15 14:25:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-16 14:29:35","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.02","SPAC16A10.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-02-16","pdb_entries":[{"pdb_id":"2l3n","gene_chains":[{"gene_uniquename":"SPAC16A10.07c","chain":"A","position":"362-395"},{"gene_uniquename":"SPBC1778.02","chain":"A","position":"639-693"}],"title":"Solution structure of Rap1-Taz1 fusion protein","entry_authors":"Zhou ZR,Wang F,Chen Y,Lei M,Hu H","entry_authors_abbrev":"Zhou ZR et al.","reference_uniquename":"PMID:21217703","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:19940942","title":"Expression of the atf1+ gene is upregulated in fission yeast under nitrosative and nutritional stresses.","citation":"Can J Microbiol 2009 Nov;55(11):1323-7","abstract":"This work was designed to assess regulation of the atf1+ gene in the fission yeast Schizosaccharomyces pombe under nitrosative and nutritional stresses, using the atf1+-lacZ fusion gene and RT-PCR. Nitric oxide (NO)-generating sodium nitroprusside (SNP; 10 micromol/L) and nitrogen depletion significantly enhanced synthesis of beta-galactosidase from the atf1+-lacZ fusion gene in S. pombe Pap1-positive KP1 cells, but not in S. pombe Pap1-negative TP108-3C cells. SNP (10 micromol/L) and nitrogen depletion also caused a significant increase in atf1+ mRNA levels in Pap1-positive cells, but not in Pap1-negative cells. Depletion of glucose marginally increased synthesis of beta-galactosidase from the fusion gene in S. pombe Pap1-positive cells. Taken together, the S. pombe atf1+ gene is upregulated by nitrosative and nutritional stresses on a transcriptional level, possibly via the mediation of Pap1.","doi":"10.1139/w09-087","authors":"Song SH, Kim BM, Lim CJ, Song YS, Park EH","authors_abbrev":"Song SH et al.","pubmed_publication_date":"Nov 2009","pubmed_entrez_date":"2009-11-27","publication_year":"2009","canto_session_key":"f4b23d489231d55b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-03 16:56:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-03 16:56:49","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-12-03"},{"uniquename":"PMID:28980880","title":"Spurious transcription and its impact on cell function.","citation":"Transcription 2018;9(3):182-189","abstract":"Most RNA polymerases can initiate transcription from diverse DNA template sequences with relatively few outright sequence restraints. Recent reports have demonstrated that failure to subdue the promiscuity of RNA polymerase in vivo can severely impede cell function. This phenomenon appears common to all cell types with undesirable effects ranging from growth inhibition in prokaryotes to cancer in higher organisms. Here we discuss similarities and differences in strategies employed by cells to minimise spurious transcription across life's domains.","doi":"10.1080/21541264.2017.1381794","authors":"Wade JT, Grainger DC","authors_abbrev":"Wade JT et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2017-10-06","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-11-05 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10879493","title":"Identification and characterization of a novel gene, hos3+, the function of which is necessary for growth under high osmotic stress in fission yeast.","citation":"Biosci Biotechnol Biochem 2000 May;64(5):1099-102","abstract":"hos3 mutants of the fission yeast Schizosaccharomyces pombe showed the phenotype of high osmolarity sensitivity for growth. An S. pombe strain carrying the hos3-M26 allele cannot form colonies on agar plates containing 2 M glucose, but the parental strain can do so very well, as demonstrated previously. The hos3+ gene was cloned and identified as one that encodes a small protein of 94 amino acids, which shows no sequence similarity to any other proteins in the current databases. A hos3delta strain, which we then constructed, had the phenotype of high osmolarity sensitivity, as in the case of the original hos3-M26 mutant. More interestingly, when these hos- cells were grown in the non-permissive growth condition in the presence of 2 M glucose, we found that unusually many septated cells were accumulated after a prolonged incubation. A multicopy suppressor gene for hos- mutations was also isolated and identified as the dsk1+ gene encoding a protein kinase, which was previously suggested to be implicated in a process of the mitotic regulation of S. pombe. The function of the hos3+ gene is discussed from these results.","authors":"Aoyama K, Kawaura R, Yamada H, Aiba H, Mizuno T","authors_abbrev":"Aoyama K et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-07-06","publication_year":"2000","canto_session_key":"28dc33fbb04ba432","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-01 14:45:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-01 14:35:23","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC417.02","SPBC530.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-12-01"},{"uniquename":"PMID:23032292","title":"Chd1 chromatin remodelers maintain nucleosome organization and repress cryptic transcription.","citation":"EMBO Rep 2012 Nov 06;13(11):997-1003","abstract":"Chromatin organization is essential for defining transcription units and maintaining genomic integrity in eukaryotes. In this study, we found that deletion of the Schizosaccharomyces pombe Chd1 chromatin remodelers, hrp1 and hrp3, causes strong, genome-wide accumulation of antisense transcripts. Nucleosome mapping revealed a specific role for Chd1 remodelers in the positioning of nucleosomes in gene coding regions. Other mutations associated with enhanced cryptic transcription activity, such as set2Δ, alp13Δ and FACT complex subunit pob3Δ, did not, or only mildly, affect nucleosome positioning. These data indicate several mechanisms in the repression of cryptic promoter activity in eukaryotic cells.","doi":"10.1038/embor.2012.146","authors":"Hennig BP, Bendrin K, Zhou Y, Fischer T","authors_abbrev":"Hennig BP et al.","pubmed_publication_date":"06 Nov 2012","pubmed_entrez_date":"2012-10-04","publication_year":"2012","canto_session_key":"7c2f0cff132ea0bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-06 16:32:51","canto_approved_date":"2020-04-09 15:28:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-04-06 16:32:41","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.05","SPBC609.05","SPAC23H4.12","SPBP35G2.10","SPAC3G6.01","SPAC29B12.02c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-04-06"},{"uniquename":"PMID:34903663","title":"Adaptations in metabolism and protein translation give rise to the Crabtree effect in yeast.","citation":"Proc Natl Acad Sci U S A 2021 Dec 21;118(51)","abstract":"Aerobic fermentation, also referred to as the Crabtree effect in yeast, is a well-studied phenomenon that allows many eukaryal cells to attain higher growth rates at high glucose availability. Not all yeasts exhibit the Crabtree effect, and it is not known why Crabtree-negative yeasts can grow at rates comparable to Crabtree-positive yeasts. Here, we quantitatively compared two Crabtree-positive yeasts,  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe , and two Crabtree-negative yeasts,  Kluyveromyces marxianus  and  Scheffersomyces stipitis , cultivated under glucose excess conditions. Combining physiological and proteome quantification with genome-scale metabolic modeling, we found that the two groups differ in energy metabolism and translation efficiency. In Crabtree-positive yeasts, the central carbon metabolism flux and proteome allocation favor a glucose utilization strategy minimizing proteome cost as proteins translation parameters, including ribosomal content and/or efficiency, are lower. Crabtree-negative yeasts, however, use a strategy of maximizing ATP yield, accompanied by higher protein translation parameters. Our analyses provide insight into the underlying reasons for the Crabtree effect, demonstrating a coupling to adaptations in both metabolism and protein translation.","doi":"10.1073/pnas.2112836118","authors":"Malina C, Yu R, Björkeroth J, Kerkhoven EJ, Nielsen J","authors_abbrev":"Malina C et al.","pubmed_publication_date":"21 Dec 2021","pubmed_entrez_date":"2021-12-14","publication_year":"2021","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2021-12-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10523311","title":"Organization of DNA replication origins in the fission yeast genome.","citation":"EMBO J 1999 Oct 15;18(20):5683-90","abstract":"Eukaryotic DNA replication initiates at multiple points along the chromosomes known as replication origins (ORIs). We have developed a strategy to identify ORIs directly from replication intermediates in the fission yeast Schizosaccharomyces pombe. Mapping of a selection of the novel ORIs onto the genome reveals their preferential localization at intergenic regions upstream from genes. These results are supported by the observation that a large proportion of regions overlapping gene promoters contain active ORIs. Mapping of the genomic ars1 replication origin at nucleotide resolution shows that replication initiates at a defined position immediately upstream from the hus5(+) promoter. Deletion analysis indicates that the regulatory elements required to initiate transcription and replication lie in close proximity, suggesting a possible relationship between both processes in vivo.","authors":"Gómez M, Antequera F","authors_abbrev":"Gómez M et al.","pubmed_publication_date":"15 Oct 1999","pubmed_entrez_date":"1999-10-16","publication_year":"1999","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19308704","title":"Studies of meiosis disclose distinct roles of cohesion in the core centromere and pericentromeric regions.","citation":"Chromosome Res 2009;17(2):239-49","abstract":"During meiosis, a single round of genome duplication is followed by two sequential rounds of chromosome segregation. Through this process, a diploid parent cell generates gametes with a haploid set of chromosomes. A characteristic of meiotic chromosome segregation is a stepwise loss of sister chromatid cohesion along chromosomal arms and at centromeres. Whereas arm cohesion plays an important role in ensuring homologue disjunction at meiosis I, persisting cohesion at pericentromeric regions throughout meiosis I is essential for the faithful equational segregation of sisters in the following meiosis II, similar to mitosis. A widely conserved pericentromeric protein called shugoshin, which associates with protein phosphatase 2A (PP2A), plays a critical role in this protection of cohesin. Another key aspect of meiosis I is the establishment of monopolar attachment of sister kinetochores to spindle microtubules. Cohesion or physical linkage at the core centromeres, where kinetochores assemble, may conjoin sister kinetochores, leading to monopolar attachment. A meiosis-specific kinetochore factor such as fission yeast Moa1 or budding yeast monopolin contributes to this regulation. We propose that cohesion at the core centromere and pericentromeric regions plays distinct roles, especially in defining the orientation of kinetochores.","doi":"10.1007/s10577-008-9013-y","authors":"Sakuno T, Watanabe Y","authors_abbrev":"Sakuno T et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-03-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF010473","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35360049","title":"Dataset describing the genome wide effects on transcription resulting from alterations in the relative levels of the bZIP transcription factors Atf1 and Pcr1 in  Schizosaccharomyces pombe .","citation":"Data Brief 2022 Jun;42:108034","abstract":" Schizosaccharomyces pombe  has been used as an excellent model for studying eukaryotic cell cycle regulation and stress responses. The bZIP transcription factors Atf1(ATF2 homolog) and Pcr1(CREB homolog) have been shown to be important for regulating the expression of genes related to both stress response and cell cycle. Pcr1 has in fact been implicated as a determining factor in the segregation of the cell cycle and stress response related functions of Atf1. Interestingly Atf1 and Pcr1 levels are known to vary during the cell cycle thus giving rise to the possibility that their relative levels can influence the periodic transcriptional program of the cell. Here we report our observations on the changes in transcriptome of  S. pombe  cells which have been genetically manipulated to create relative differences in the levels of Atf1 and Pcr1. These results highlight new information regarding the potential role of Atf1 and Pcr1 in orchestrating the integration of the transcriptional programs of cell cycle and stress response.","doi":"10.1016/j.dib.2022.108034","authors":"Basu S, Sarkar P, Datta S, Sundaram G","authors_abbrev":"Basu S et al.","pubmed_publication_date":"Jun 2022","pubmed_entrez_date":"2022-04-01","publication_year":"2022","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-04-03 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC21E11.03c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:21670521","title":"Apoptotic cell death in the fission yeast Schizosaccharomyces pombe induced by valproic acid and its extreme susceptibility to pH change.","citation":"Biosci Biotechnol Biochem 2011;75(6):1113-8","abstract":"Schizosaccharomyces pombe treated with valproic acid died with apoptotic markers such as DNA fragmentation, loss of a mitochondrial electrochemical gradient and chromatin condensation, independently of metacaspase, a yeast homolog of metazoan caspase. Sensitivity to valproic acid was strongly dependent on growth phase. Cells in a later growth phase were much more sensitive to valproic acid than those in an earlier one. Altering the pH of the medium with HCl and with NaOH also caused remarkable changes in sensitivity. Cells in an acidic medium were more sensitive to valproic acid. This pH-dependent change in sensitivity did not require de novo protein synthesis, and a change in pH 60 min after the administration of valproic acid affected sensitivity. These results suggest that the intracellular cell death process was susceptible to extracellular pH. Although a sir2 mutant of Saccharomyces cerevisiae has been reported to be resistant to valproic acid, mutations in sir2 did not affect the sensitivity to valproic acid of S. pombe.","authors":"Mutoh N, Kitajima S, Ichihara S","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-06-15","publication_year":"2011","canto_session_key":"92f2d67c8a7271f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-06-06 15:57:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-06 15:56:54","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.04","SPBC16D10.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-06"},{"uniquename":"PMID:8852835","title":"Double-strand break-induced mitotic intrachromosomal recombination in the fission yeast Schizosaccharomyces pombe.","citation":"Genetics 1996 Feb;142(2):341-57","abstract":"The Saccharomyces cerevisiae HO gene and MATa cutting site were used to introduce site-specific double-strand breaks (DSBs) within intrachromosomal recombination substrates in Schizosaccharomyces pombe. The recombination substrates consisted of nontandem direct repeats of ade6 heteroalleles. DSB induction stimulated the frequency of recombinants 2000-fold. The spectrum of DSB-induced recombinants depended on whether the DSB was introduced within one of the ade6 repeats or in intervening unique DNA. When the DSB was introduced within unique DNA, over 99.8% of the recombinants lacked the intervening DNA but retained one copy of ade6 that was wild type or either one of the heteroalleles. When the DSB was located in duplicated DNA, 77% of the recombinants were similar to the deletion types described above, but the single ade6 copy was either wild type or exclusively that of the uncut repeat. The remaining 23% of the induced recombinants were gene convertants with two copies of ade6 and the intervening sequences; the ade6 heteroallele in which the DSB was induced was the recipient of genetic information. Half-sectored colonies were isolated, analyzed and interpreted as evidence of heteroduplex DNA formation. The results are discussed in terms of current models for recombination.","authors":"Osman F, Fortunato EA, Subramani S","authors_abbrev":"Osman F et al.","pubmed_publication_date":"Feb 1996","pubmed_entrez_date":"1996-02-01","publication_year":"1996","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2743431","title":"An abnormal cell division cycle in an AIR carboxylase-deficient mutant of the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1989 Jan;15(1):71-4","abstract":"Adenine-requiring mutant strains of S. pombe enter the stationary phase after depleting a culture medium of adenine or its analogues. Stationary phase cells of six mutants defective at different stages of the purine nucleotide synthetic pathway were examined for cell volume and DNA content, and then compared in these respects with those of a prototrophic wild-type strain. The cell cycle of the wild-type strain was arrested in the G2 phase (2C state) in the nitrogen rich medium, as is evident from DNA content per cell (0.0425 pg) and cell volume (47.7 microns 3). An AIR carboxylase-deficient (ade6) mutant strain was found to have an unusual cell volume (307.4 microns 3) and DNA content (0.1187 pg). By DAPI fluorescence microscopy, each mutant cell was seen to contain only one enlarged nucleus, which indicates the absence of cell populations containing cells in the 4C state of the S phase following nuclear division. It then follows that in ade6 mutant cells, DNA synthesis occurs in the absence of a completed nuclear division. Thus in S. pombe cells, the completion of nuclear division is not necessarily required for the next cycle initiation of DNA synthesis under certain physiological conditions.","authors":"Ishiguro J","authors_abbrev":"Ishiguro J","pubmed_publication_date":"Jan 1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_session_key":"178890d2bcf87d92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-03-28 11:17:24","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-11-02 11:05:28","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCPB16A4.03c","SPCC569.08c","SPBC14F5.09c","SPAC4D7.08c","SPCC1322.13","SPBC409.10"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2013-11-02"},{"uniquename":"EMBL:AU007071","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8861954","title":"PIG-B, a membrane protein of the endoplasmic reticulum with a large lumenal domain, is involved in transferring the third mannose of the GPI anchor.","citation":"EMBO J 1996 Aug 15;15(16):4254-61","abstract":"Many eukaryotic cell surface proteins are bound to the membrane via the glycosylphosphatidylinositol (GPI) anchor that is covalently linked to their carboxy-terminus. The GPI anchor precursor is synthesized in the endoplasmic reticulum (ER) and post-translationally linked to protein. We cloned a human gene termed PIG-B (phosphatidylinositol glycan of complementation class B) that is involved in transferring the third mannose. PIG-B encodes a 554 amino acid, ER transmembrane protein with an amino-terminal portion of approximately 60 amino acids on the cytoplasmic side and a large carboxy-terminal portion of 470 amino acids within the ER lumen. A mutant PIG-B lacking the cytoplasmic portion remains active, indicating that the functional site of PIG-B resides on the lumenal side of the ER membrane. The PIG-B gene was localized to chromosome 15 at q21-q22. This autosomal location would explain why PIG-B is not involved in the defective GPI anchor synthesis in paroxysmal nocturnal hemoglobinuria, which is always caused by a somatic mutation of the X-linked PIG-A gene.","authors":"Takahashi M, Inoue N, Ohishi K, Maeda Y, Nakamura N, Endo Y, Fujita T, Takeda J, Kinoshita T","authors_abbrev":"Takahashi M et al.","pubmed_publication_date":"15 Aug 1996","pubmed_entrez_date":"1996-08-15","publication_year":"1996","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9009208","title":"A complex structure in the mRNA of Tf1 is recognized and cleaved to generate the primer of reverse transcription.","citation":"Genes Dev 1997 Jan 15;11(2):270-85","abstract":"All retroviruses and LTR-containing retrotransposons are thought to require specific tRNA molecules to serve as primers of reverse transcription. An exception is the LTR-containing retrotransposon Tf1, isolated from Schizosaccharomyces pombe. Instead of requiring a tRNA, the reverse transcriptase of Tf1 uses the first 11 bases of the Tf1 transcript as the primer for reverse transcription. The primer is generated by a cleavage that occurs between bases 11 and 12 of the Tf1 mRNA. Sequence analysis of the 5' untranslated region of the Tf1 mRNA resulted in the identification of a region with the potential to form an RNA structure of 89 bases that included the primer binding site and the first 11 bases of the Tf1 mRNA. Systematic mutagenesis of this region revealed 34 single-point mutants in the structure that resulted in reduced transposition activity. The defects in transposition correlated with reduced level of Tf1 reverse transcripts as determined by DNA blot analysis. Evidence that the RNA structure did form in vivo included the result that strains with second site mutations that restored complementarity resulted in increased levels of reverse transcripts and Tf1 transposition. The majority of the mutants defective for reverse transcription were unable to cleave the Tf1 mRNA between bases 11 and 12. These data indicate that formation of an extensive RNA structure was required for the cleavage reaction that generated the primer for Tf1 reverse transcription.","authors":"Lin JH, Levin HL","authors_abbrev":"Lin JH et al.","pubmed_publication_date":"15 Jan 1997","pubmed_entrez_date":"1997-01-15","publication_year":"1997","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14990453","title":"Enrichment of transcriptional regulatory sites in non-coding genomic region.","citation":"Bioinformatics 2004 Mar 01;20(4):569-75","abstract":"Over-represented k-mers in non-coding genomic regions often lead to identification of potential transcriptional regulatory sites (TRS). This phenomenon has been employed by many algorithms to predict TRS in silico. Yet, the improvement of these algorithms should be based on deeper understanding of the enrichment feature. To obtain a general distributional profile of TRS in different regions of genomes as well as in different genomes, we here performed a systematic analysis on the over-representation of TRS in intergenic regions and gene upstream regions of yeasts and viral genomes, and the distributional pattern of TRS in intergenic and intron regions of the Drosophila genome. We also explored the way to evaluate the accuracy of TRS consensus sequences by measuring their enrichment.\nTo measure enrichment, a statistical background model was introduced by comparing TRS frequency in certain regions of genome to either the frequency in the whole genome or the frequency in exon region. This model was applied to different classes of non-coding genomic regions in four genomes. Most of the TRS were observed to be over-represented in the intergenic regions of the Saccharomyces cerevisiae, Schizosaccharomyces pombe and Epstein-Barr virus (EBV) genomes. The enrichment of S.cerevisiae TRS in the 600 bp upstream region of genes was also significant. In Drosophila genome, TRS did not show enrichment in intergenic and intron regions when TRS frequency in the whole genome was taken as background, as we did in other genomes. However, when we took TRS frequency in exon region as background, over 70% TRS are over-represented in those two classes of non-coding regions. This fact indicates the existence of transcriptional regulatory signals in introns. The analysis of some S.cerevisiae TRS, which have inconsistent consensus sequences with different levels of enrichment in intergenic region, suggests the possibility of evaluating the accuracy of experimentally determined TRS by measuring their enrichment in non-coding genomic regions.","authors":"Xue W, Wang J, Shen Z, Zhu H","authors_abbrev":"Xue W et al.","pubmed_publication_date":"01 Mar 2004","pubmed_entrez_date":"2004-03-03","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29422501","title":"LARP7 family proteins have conserved function in telomerase assembly.","citation":"Nat Commun 2018 Feb 08;9(1):557","abstract":"Understanding the intricacies of telomerase regulation is crucial due to the potential health benefits of modifying its activity. Telomerase is composed of an RNA component and reverse transcriptase. However, additional factors required during biogenesis vary between species. Here we have identified fission yeast Lar7 as a member of the conserved LARP7 family, which includes the Tetrahymena telomerase-binding protein p65 and human LARP7. We show that Lar7 has conserved RNA-recognition motifs, which bind telomerase RNA to protect it from exosomal degradation. In addition, Lar7 is required to stabilise the association of telomerase RNA with the protective complex LSm2-8, and telomerase reverse transcriptase. Lar7 remains a component of the mature telomerase complex and is required for telomerase localisation to the telomere. Collectively, we demonstrate that Lar7 is a crucial player in fission yeast telomerase biogenesis, similarly to p65 in Tetrahymena, and highlight the LARP7 family as a conserved factor in telomere maintenance.","doi":"10.1038/s41467-017-02296-4","authors":"Collopy LC, Ware TL, Goncalves T, Í Kongsstovu S, Yang Q, Amelina H, Pinder C, Alenazi A, Moiseeva V, Pearson SR, Armstrong CA, Tomita K","authors_abbrev":"Collopy LC et al.","pubmed_publication_date":"08 Feb 2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_session_key":"b5450581ac9e067c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kazunori Tomita","canto_first_approved_date":"2018-03-27 14:52:36","canto_approved_date":"2026-01-17 19:42:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-19 10:14:32","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[{"name":"Kazunori Tomita","community_curator":true,"annotation_count":29,"orcid":"0000-0003-1096-6725","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.09","SPAC17G6.17","SPBC9B6.05c","SPNCRNA.214","SPCC1840.10","SPCC1620.01c","SPBC29A3.14c","SPBC30D10.06","SPAC1F3.01","SPAC2F3.17c","SPCC285.12","SPAC16A10.07c","SPAC6F6.17","SPAC644.14c","SPBC1778.02","SPAC26A3.08"],"gene_count":16,"ltp_gene_count":9,"approved_date":"2018-03-27"},{"uniquename":"PMID:7932698","title":"On the identification of group II introns in nucleotide sequence data.","citation":"J Mol Biol 1994 Sep 30;242(4):389-96","abstract":"Four different consensus sequences (GTI, group II identifiers) have been derived from domains V of known group II introns and are used as query input sequences for sensitive database screenings with the FASTA and LFASTA programs. The set of four GTI sequences can identify all domains V of the 96 known group II introns in the completely sequenced chloroplast genomes of Marchantia polymorpha, Epifagus virginiana, Oryza sativa, Nicotiana tabacum and the completely sequenced mitochondrial genomes of Saccharomyces cerevisiae, Podospora anserina, Schizosaccharomyces pombe and Marchantia polymorpha. Seven moderately high-scoring hits can easily be rejected as false-positives since they do not fulfil secondary structure requirements. Large FASTA outputs obtained after screening the entire nucleotide sequence database are evaluated in a second step by a program (D5SCAN) that allows the assignment of variable selection criteria for potential domain V secondary structures. Database searches with these routines yield evidence for several group II intron sequences previously unrecognized. These include novel intron structures in the cyanobacterium Synechocystis and in the mitochondrial genomes of Marchantia, soybean, pea, broad bean, sugar beet and a heterobasidiomycete. Potential intron remnants are found contributing to the secondary structure of rRNAs in several trypanosome species. At a given sensitivity of 95% positively identified true domains V, the search routine produces one false positive hit per 10,000 kb.","authors":"Knoop V, Kloska S, Brennicke A","authors_abbrev":"Knoop V et al.","pubmed_publication_date":"30 Sep 1994","pubmed_entrez_date":"1994-09-30","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20719272","title":"A fast microfluidic temperature control device for studying microtubule dynamics in fission yeast.","citation":"Methods Cell Biol 2010;97:185-201","abstract":"Recent development in soft lithography and microfluidics enables biologists to create tools to control the cellular microenvironment. One such control is the ability to quickly change the temperature of the cells. Genetic model organism such as fission yeast has been useful for studies of the cell cytoskeleton. In particular, the dynamic microtubule cytoskeleton responds to changes in temperature. In addition, there are temperature-sensitive mutations of cytoskeletal proteins. We describe here the fabrication and use of a microfluidic device to quickly and reversibly change cellular temperature between 2 degrees C and 50 degrees C. We demonstrate the use of this device while imaging at high-resolution microtubule dynamics in fission yeast.","doi":"10.1016/S0091-679X(10)97011-8","authors":"Velve-Casquillas G, Costa J, Carlier-Grynkorn F, Mayeux A, Tran PT","authors_abbrev":"Velve-Casquillas G et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-08-20","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2834361","title":"Characterization of the gene for fructose-1,6-bisphosphatase from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Sequence, protein homology, and expression during growth on glucose.","citation":"J Biol Chem 1988 May 05;263(13):6051-7","abstract":"We have determined the nucleotide sequence of the gene for fructose-1,6-bisphosphatase from both Saccharomyces cerevisiae and Schizosaccharomyces pombe. The predicted protein sequence for fructose-1,6-bisphosphatase from S. cerevisiae contains 347 amino acids and has a molecular weight of 38,100; that from S. pombe, contains 346 amino acids and has a molecular weight of 38,380. Comparison of these amino acid sequences with each other and that of pig kidney fructose-1,6-bisphosphatase shows several regions of strong homology separated by regions of divergence. These homologous regions are likely candidates for functional domains. A gene cassette was constructed for fructose-1,6-bisphosphatase from S. cerevisiae and the gene cassette expressed from the regulated PHO5 and GAL1 promoters of yeast. Yeast cells expressing fructose-1,6-bisphosphatase, while growing on glucose, accumulated large amounts of enzyme intracellularly, suggesting that glucose-regulated proteolytic inactivation does not operate efficiently under these conditions. Growth on glucose was not inhibited by the expression of fructose 1,6-bisphosphatase.","authors":"Rogers DT, Hiller E, Mitsock L, Orr E","authors_abbrev":"Rogers DT et al.","pubmed_publication_date":"05 May 1988","pubmed_entrez_date":"1988-05-05","publication_year":"1988","canto_session_key":"948fca77c7f45004","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-31 17:10:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-31 17:10:42","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1198.14c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-31"},{"uniquename":"PMID:32336995","title":"Diverse transposable element landscapes in pathogenic and nonpathogenic yeast models: the value of a comparative perspective.","citation":"Mob DNA 2020;11:16","abstract":"Genomics and other large-scale analyses have drawn increasing attention to the potential impacts of transposable elements (TEs) on their host genomes. However, it remains challenging to transition from identifying potential roles to clearly demonstrating the level of impact TEs have on genome evolution and possible functions that they contribute to their host organisms. I summarize TE content and distribution in four well-characterized yeast model systems in this review: the pathogens  Candida albicans  and  Cryptococcus neoformans , and the nonpathogenic species  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe . I compare and contrast their TE landscapes to their lifecycles, genomic features, as well as the presence and nature of RNA interference pathways in each species to highlight the valuable diversity represented by these models for functional studies of TEs. I then review the regulation and impacts of the Ty1 and Ty3 retrotransposons from  Saccharomyces cerevisiae  and Tf1 and Tf2 retrotransposons from  Schizosaccharomyces pombe  to emphasize parallels and distinctions between these well-studied elements. I propose that further characterization of TEs in the pathogenic yeasts would enable this set of four yeast species to become an excellent set of models for comparative functional studies to address outstanding questions about TE-host relationships.","doi":"10.1186/s13100-020-00215-x","authors":"Maxwell PH","authors_abbrev":"Maxwell PH","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-04-28","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-04-29 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29136238","title":"Regulation of transcriptional silencing and chromodomain protein localization at centromeric heterochromatin by histone H3 tyrosine 41 phosphorylation in fission yeast.","citation":"Nucleic Acids Res 2018 Jan 09;46(1):189-202","abstract":"Heterochromatin silencing is critical for genomic integrity and cell survival. It is orchestrated by chromodomain (CD)-containing proteins that bind to methylated histone H3 lysine 9 (H3K9me), a hallmark of heterochromatin. Here, we show that phosphorylation of tyrosine 41 (H3Y41p)-a novel histone H3 modification-participates in the regulation of heterochromatin in fission yeast. We show that a loss-of-function mutant of H3Y41 can suppress heterochromatin de-silencing in the centromere and subtelomere repeat regions, suggesting a de-silencing role for H3Y41p on heterochromatin. Furthermore, we show both in vitro and in vivo that H3Y41p differentially regulates two CD-containing proteins without the change in the level of H3K9 methylation: it promotes the binding of Chp1 to histone H3 and the exclusion of Swi6. H3Y41p is preferentially enriched on centromeric heterochromatin during M- to early S phase, which coincides with the localization switch of Swi6/Chp1. The loss-of-function H3Y41 mutant could suppress the hypersensitivity of the RNAi mutants towards hydroxyurea (HU), which arrests replication in S phase. Overall, we describe H3Y41p as a novel histone modification that differentially regulates heterochromatin silencing in fission yeast via the binding of CD-containing proteins.","doi":"10.1093/nar/gkx1010","authors":"Ren B, Tan HL, Nguyen TTT, Sayed AMM, Li Y, Mok YK, Yang H, Chen ES","authors_abbrev":"Ren B et al.","pubmed_publication_date":"09 Jan 2018","pubmed_entrez_date":"2017-11-15","publication_year":"2018","canto_session_key":"e865b65eeb6f06b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Bingbing Ren","canto_first_approved_date":"2018-03-28 15:31:36","canto_approved_date":"2024-11-24 16:15:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-01 17:39:11","canto_added_date":"2017-11-16 01:15:13","annotation_curators":[{"name":"Bingbing Ren","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.11c","SPCC11E10.08","SPCC736.11","SPAC1834.04","SPAC18G6.02c","SPAC664.01c","SPBC8D2.04","SPBC428.08c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-03-28"},{"uniquename":"PMID:7772832","title":"Phosphatidylinositol-3 kinase in fission yeast: a possible role in stress responses.","citation":"Biosci Biotechnol Biochem 1995 Apr;59(4):678-82","abstract":"A DNA fragment coding for a part of a putative phosphatidylinositol 3 kinase was cloned from Schizosaccharomyces pombe by cross-hybridization with Saccharomyces cerevisiae VPS34 gene, a yeast homologue of mammalian PI-3 kinase. The clone contained an open reading frame of 797 amino acids but lacked the initiation codon, ATG. The predicted amino acid sequence was homologous to those of S. cerevisiae VPS34 and mammalian PI-3 kinase genes. Disruption of the gene resulted in extremely low levels of PI-3-P and higher levels of PI-4-P, supporting the idea that the gene codes for the PI-3 kinase of S. pombe. The disruptants harbored large vacuoles and were sensitive to stresses such as high temperature or high concentration of monovalent and divalent cations.","authors":"Kimura K, Miyake S, Makuuchi M, Morita R, Usui T, Yoshida M, Horinouchi S, Fukui Y","authors_abbrev":"Kimura K et al.","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_session_key":"67a45bb75e85f945","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-03-27 14:38:11","canto_approved_date":"2024-05-23 16:09:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-31 10:04:52","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC458.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-03-27"},{"uniquename":"EMBL:EF424786","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.82"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35041656","title":"Characterizing non-exponential growth and bimodal cell size distributions in fission yeast: An analytical approach.","citation":"PLoS Comput Biol 2022 Jan;18(1):e1009793","abstract":"Unlike many single-celled organisms, the growth of fission yeast cells within a cell cycle is not exponential. It is rather characterized by three distinct phases (elongation, septation, and reshaping), each with a different growth rate. Experiments also showed that the distribution of cell size in a lineage can be bimodal, unlike the unimodal distributions measured for the bacterium Escherichia coli. Here we construct a detailed stochastic model of cell size dynamics in fission yeast. The theory leads to analytic expressions for the cell size and the birth size distributions, and explains the origin of bimodality seen in experiments. In particular, our theory shows that the left peak in the bimodal distribution is associated with cells in the elongation phase, while the right peak is due to cells in the septation and reshaping phases. We show that the size control strategy, the variability in the added size during a cell cycle, and the fraction of time spent in each of the three cell growth phases have a strong bearing on the shape of the cell size distribution. Furthermore, we infer all the parameters of our model by matching the theoretical cell size and birth size distributions to those from experimental single-cell time-course data for seven different growth conditions. Our method provides a much more accurate means of determining the size control strategy (timer, adder or sizer) than the standard method based on the slope of the best linear fit between the birth and division sizes. We also show that the variability in added size and the strength of size control in fission yeast depend weakly on the temperature but strongly on the culture medium. More importantly, we find that stronger size homeostasis and larger added size variability are required for fission yeast to adapt to unfavorable environmental conditions.","doi":"10.1371/journal.pcbi.1009793","authors":"Jia C, Singh A, Grima R","authors_abbrev":"Jia C et al.","pubmed_publication_date":"Jan 2022","pubmed_entrez_date":"2022-01-18","publication_year":"2022","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2022-01-20 01:15:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8937982","title":"Mutations in the fission yeast silencing factors clr4+ and rik1+ disrupt the localisation of the chromo domain protein Swi6p and impair centromere function.","citation":"J Cell Sci 1996 Nov;109 ( Pt 11):2637-48","abstract":"Transcriptional silencing is known to occur at centromeres, telomeres and the mating type region in the nucleus of fission yeast, Schizosaccharomyces pombe. Mating-type silencing factors have previously been shown also to affect transcriptional repression within centromeres and to some extent at telomeres. Mutations in the clr4+, rik1+ and swi6+ genes dramatically reduce silencing at certain centromeric regions and cause elevated chromosome loss rates. Recently, Swi6p was found to co-localise with the three silent chromosomal regions. Here the involvement of clr4+, rik1+ and swi6+ in centromere function is investigated in further detail. Fluorescence in situ hybridisation (FISH) was used to show that, as in swi6 mutant cells, centromeres lag on late anaphase spindles in clr4 and rik1 mutant cells. This phenotype is consistent with a role for these three gene products in fission yeast centromere function. The Swi6 protein was found to be delocalised from all three silent chromosomal regions, and dispersed within the nucleus, in both clr4 and rik1 mutant cells. The phenotypic similarity observed in all three mutants is consistent with the products of both the clr4+ and rik1+ genes being required to recruit Swi6p to the centromere and other silent regions. Mutations in clr4, rik1 and swi6 also result in elevated sensitivity to reagents which destabilise microtubules and show a synergistic interaction with a mutation in the beta-tubulin gene (nda3). These observations suggest that clr4+ and rik1+ must play a role in the assembly of Swi6p into a transcriptionally silent, inaccessible chromatin structure at fission yeast centromeres which is required to facilitate interactions with spindle microtubules and to ensure normal chromosome segregation.","authors":"Ekwall K, Nimmo ER, Javerzat JP, Borgstrøm B, Egel R, Cranston G, Allshire R","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_session_key":"167fcf5adceaa9f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-16 17:37:57","canto_approved_date":"2024-04-04 07:38:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-16 17:37:50","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":63,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPAC664.01c","SPBC2D10.17","SPAC1B3.17","SPBC428.08c","SPAC3G6.06c","SPCC11E10.08","SPBC26H8.07c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-10-16"},{"uniquename":"PMID:24382491","title":"Identification of proteins that form specific complexes with the highly conserved protein Translin in Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2014 Apr;1844(4):767-77","abstract":"Translin is a single-stranded DNA and RNA binding protein that has a high affinity for G-rich sequences. TRAX is a Translin paralog that associates with Translin. Both Translin and TRAX were highly conserved in eukaryotes. The nucleic acid binding form of Translin is a barrel-shaped homo-octamer. A Translin-TRAX hetero-octamer having a similar structure also binds nucleic acids. Previous reports suggested that Translin may be involved in chromosomal translocations, telomere metabolism and the control of mRNA transport and translation. More recent studies have indicated that Translin-TRAX hetero-octamers are involved in RNA silencing. To gain a further insight into the functions of Translin, we have undertaken to systematically search for proteins with which it forms specific complexes in living cells. Here we report the results of such a search conducted in the fission yeast Schizosaccharomyces pombe, a suitable model system. This search was carried out by affinity purification and immuno-precipitation techniques, combined with differential labeling of the intracellular proteins with the stable isotopes ¹⁵N and ¹⁴N. We identified for the first time two proteins containing an RNA Recognition Motif (RRM), which are specifically associated with the yeast Translin: (1) the pre-mRNA-splicing factor srp1 that belongs to the highly conserved SR family of proteins and (2) vip1, a protein conserved in fungi. Our data also support the presence of RNA in these intracellular complexes. Our experimental approach should be generally applicable to studies of weak intracellular protein-protein interactions and provides a clear distinction between false positive vs. truly interacting proteins.","doi":"10.1016/j.bbapap.2013.12.016","authors":"Eliahoo E, Litovco P, Ben Yosef R, Bendalak K, Ziv T, Manor H","authors_abbrev":"Eliahoo E et al.","pubmed_publication_date":"Apr 2014","pubmed_entrez_date":"2014-01-03","publication_year":"2014","canto_session_key":"1aa134ff4369c6d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-14 09:17:21","canto_approved_date":"2022-02-02 16:46:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-14 09:17:14","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30.03c","SPAC10F6.06","SPCC736.09c","SPBC11C11.08"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-01-14"},{"uniquename":"PMID:17933563","title":"Characterization of the endo-beta-1,3-glucanase activity of S. cerevisiae Eng2 and other members of the GH81 family.","citation":"Fungal Genet Biol 2008 Apr;45(4):542-53","abstract":"The GH81 family includes proteins with endo-beta-1,3-glucanase widely distributed in yeast and fungi, which are also present in plants and bacteria. We have studied the activity of the Saccharomyces cerevisiae ScEng2 and the Schizosaccharomyces pombe SpEng1 and SpEng2 proteins. All three proteins exclusively hydrolyzed linear beta-1,3-glucan chains. Laminari-oligosaccharide degradation revealed that the minimum substrate length that the three endoglucanases were able to efficiently degrade was a molecule with at least 5 glucose residues, suggesting that the active site of the enzymes recognized five glucose units. Prediction of the secondary structure of ScEng2 and comparison with proteins of known structure allowed the identification of a 404-amino acid region with a structure similar to the Clostridium thermocellum endoglucanase CelA. This fragment showed similar enzymatic characteristics to those of the complete protein, suggesting that it contains the catalytic domain of this family of proteins. Within this domain, four conserved Asp and Glu residues (D518, D588, E609, and E613) are necessary for enzymatic activity.","authors":"Martín-Cuadrado AB, Fontaine T, Esteban PF, del Dedo JE, de Medina-Redondo M, del Rey F, Latgé JP, de Aldana CR","authors_abbrev":"Martín-Cuadrado AB et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2007-10-16","publication_year":"2008","canto_session_key":"37b94fa89fda5a2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-12 05:54:03","canto_approved_date":"2024-06-12 05:54:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 05:53:54","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23D3.10c","SPAC821.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-06-12"},{"uniquename":"PMID:39010328","title":"Fission yeast Pib2 localizes to vacuolar membranes and regulates TOR complex 1 through evolutionarily conserved domains.","citation":"FEBS Lett 2024 Jul 15;","abstract":"TOR complex 1 (TORC1) is a multi-protein kinase complex that coordinates cellular growth with environmental cues. Recent studies have identified Pib2 as a critical activator of TORC1 in budding yeast. Here, we show that loss of Pib2 causes severe growth defects in fission yeast cells, particularly when basal TORC1 activity is diminished by hypomorphic mutations in tor2, the gene encoding the catalytic subunit of TORC1. Consistently, TORC1 activity is significantly compromised in the tor2 hypomorphic mutants lacking Pib2. Moreover, as in budding yeast, fission yeast Pib2 localizes to vacuolar membranes via its FYVE domain, with its tail motif indispensable for TORC1 activation. These results strongly suggest that Pib2-mediated positive regulation of TORC1 is evolutionarily conserved between the two yeast species.","doi":"10.1002/1873-3468.14980","authors":"Morozumi Y, Hayashi Y, Chu CM, Sofyantoro F, Akikusa Y, Fukuda T, Shiozaki K","authors_abbrev":"Morozumi Y et al.","pubmed_publication_date":"15 Jul 2024","pubmed_entrez_date":"2024-07-16","publication_year":"2024","canto_session_key":"f601538f3543ef0e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yuichi Morozumi","canto_first_approved_date":"2024-08-01 13:45:21","canto_approved_date":"2024-08-01 13:45:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-01 04:41:33","canto_added_date":"2024-07-16 23:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":25,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Yuichi Morozumi","community_curator":true,"annotation_count":31,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.13c","SPCC777.05","SPBC216.07c","SPAC458.05","SPBC9B6.03","SPCC4G3.08"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2024-08-01"},{"uniquename":"PMID:36626368","title":"Perturbed fatty-acid metabolism is linked to localized chromatin hyperacetylation, increased stress-response gene expression and resistance to oxidative stress.","citation":"PLoS Genet 2023 Jan;19(1):e1010582","abstract":"Oxidative stress is associated with cardiovascular and neurodegenerative diseases, diabetes, cancer, psychiatric disorders and aging. In order to counteract, eliminate and/or adapt to the sources of stress, cells possess elaborate stress-response mechanisms, which also operate at the level of regulating transcription. Interestingly, it is becoming apparent that the metabolic state of the cell and certain metabolites can directly control the epigenetic information and gene expression. In the fission yeast Schizosaccharomyces pombe, the conserved Sty1 stress-activated protein kinase cascade is the main pathway responding to most types of stresses, and regulates the transcription of hundreds of genes via the Atf1 transcription factor. Here we report that fission yeast cells defective in fatty acid synthesis (cbf11, mga2 and ACC/cut6 mutants; FAS inhibition) show increased expression of a subset of stress-response genes. This altered gene expression depends on Sty1-Atf1, the Pap1 transcription factor, and the Gcn5 and Mst1 histone acetyltransferases, is associated with increased acetylation of histone H3 at lysine 9 in the corresponding gene promoters, and results in increased cellular resistance to oxidative stress. We propose that changes in lipid metabolism can regulate the chromatin and transcription of specific stress-response genes, which in turn might help cells to maintain redox homeostasis.","doi":"10.1371/journal.pgen.1010582","authors":"Princová J, Salat-Canela C, Daněk P, Marešová A, de Cubas L, Bähler J, Ayté J, Hidalgo E, Převorovský M","authors_abbrev":"Princová J et al.","pubmed_publication_date":"Jan 2023","pubmed_entrez_date":"2023-01-10","publication_year":"2023","canto_session_key":"e237eefe5c28c283","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-01-11 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12857865","title":"Fission yeast cdc31p is a component of the half-bridge and controls SPB duplication.","citation":"Mol Biol Cell 2003 Jul;14(7):2793-808","abstract":"The fission yeast spindle pole body (SPB) is a nucleus-associated organelle that duplicates once each cell cycle during interphase. Duplicated SPBs serve as the poles of an intranuclear mitotic spindle after their insertion into the nuclear envelope in mitosis (Ding et al., Mol. Biol. Cell 8, 1461-1479). Here, we report the identification and characterization of Schizosaccharomyces pombe cdc31p, a member of the conserved calcium-binding centrin/CDC31 family. Immunofluorescence and immunoelectron microscopy show that cdc31p is a SPB component localized at the half-bridge structure of the SPB. cdc31 is an essential gene and Deltacdc31 cells and cdc31 conditional mutant cells arrest in mitosis with a monopolar mitotic spindle organized from a single SPB. EM analysis demonstrates that mutant cdc31 cells fail to duplicate the SPB. In addition, cdc31p exhibits genetic interactions with the SPB component sad1p and is required for sad1p localization. Finally, cdc31 mutant can undergo single or multiple rounds of septation before the exit from mitosis, suggesting that cdc31p activity or SPB duplication may be required for the proper coordination between the exit from mitosis and the initiation of septation.","authors":"Paoletti A, Bordes N, Haddad R, Schwartz CL, Chang F, Bornens M","authors_abbrev":"Paoletti A et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-07-15","publication_year":"2003","canto_session_key":"4fa1a879e9d78db6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-06 21:48:41","canto_approved_date":"2026-01-31 13:52:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-06 20:46:26","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.01","SPCC1682.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-06"},{"uniquename":"PMID:3641190","title":"A mutant tRNA-Met gene in the mitochondrial genome of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1986 Nov 11;14(21):8687","abstract":"","authors":"Merlos-Lange AM, Wolf K","authors_abbrev":"Merlos-Lange AM et al.","pubmed_publication_date":"11 Nov 1986","pubmed_entrez_date":"1986-11-11","publication_year":"1986","canto_session_key":"66a96dcc9ef67f2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 14:46:02","canto_approved_date":"2019-01-07 14:46:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 14:45:55","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"GO_REF:0000068","title":"Representation of metabolic triad (metabolism, catabolism, biosynthesis) as biological process in the Gene Ontology","abstract":"We have created a standard template for classes each describing the metabolism, catabolism, or biosynthesis of a chemical entity (ChEBI) as a process. The underlying equivalence axiom templates are \"GO:0008152 and 'has participant' some X\" (metabolism), \"GO:0009056 and 'has input' some X\" (catabolism), \"GO:0009058 and 'has output' some X\" and (biosynthesis),  where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33829153","title":"cAMP export by the fission yeast  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2021 Apr 02;2021","abstract":"The fission yeast  Schizosaccharomyces pombe  produces a cAMP signal in response to glucose detection. Previous characterization of this signaling focused on intracellular levels of cAMP. Here, we find that the cAMP is secreted into the medium almost immediately. This is not due to PKA activation as might have been expected. In addition, a strain that is highly deficient in drug efflux shows only a modest reduction in the secretion of cAMP to the growth medium. These observations reveal a previously unappreciated aspect of cAMP metabolism in an important model organism, leading to new questions regarding the mechanism and benefit of cAMP export in  S. pombe .","doi":"10.17912/micropub.biology.000384","authors":"Eberhard J, Hoffman CS","authors_abbrev":"Eberhard J et al.","pubmed_publication_date":"02 Apr 2021","pubmed_entrez_date":"2021-04-08","publication_year":"2021","canto_session_key":"c4b723fee955f9ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Charlie Hoffman","canto_first_approved_date":"2025-01-08 11:39:20","canto_approved_date":"2025-01-08 11:39:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-01-01 12:25:44","canto_added_date":"2021-04-10 00:15:06","annotation_curators":[{"name":"Charlie Hoffman","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-01-08"},{"uniquename":"PMID:25747261","title":"Genome-wide analysis of core promoter structures in Schizosaccharomyces pombe with DeepCAGE.","citation":"RNA Biol 2015;12(5):525-37","abstract":"The core promoter, which immediately flanks the transcription start site (TSS), plays a critical role in transcriptional regulation of eukaryotes. Recent studies on higher eukaryotes have revealed an unprecedented complexity of core promoter structures that underscores diverse regulatory mechanisms of gene expression. For unicellular eukaryotes, however, the structures of core promoters have not been investigated in detail. As an important model organism, Schizosaccharomyces pombe still lacks the precise annotation for TSSs, thus hampering the analysis of core promoter structures and their relationship to higher eukaryotes. Here we used a deep sequencing-based approach (DeepCAGE) to generate 16 million uniquely mapped tags, corresponding to 93,736 positions in the S. pombe genome. The high-resolution TSS landscape enabled identification of over 8,000 core promoters, characterization of 4 promoter classes and observation of widespread alternative promoters. The landscape also allowed precise determination of the representative TSSs within core promoters, thus redefining the 5' UTR for 82.8% of S. pombe genes. We further identified the consensus initiator (Inr) sequence--PyPyPuN(A/C)(C/A), the TATA-enriched region (between position -25 and -37) and an Inr immediate downstream motif--CC(T/A)(T/C)(T/C/A)(A/G)CCA(A/T/C), all of which were associated with highly expressed promoters. In conclusion, the detailed analysis of core promoters not only significantly improves the genome annotation of S. pombe, but also reveals that this unicellular eukaryote shares a highly similar organization in the core promoters with higher eukaryotes. These findings lend additional evidence for the power of this model system in delineating complex regulatory processes in multicellular organisms, despite its perceived simplicity.","doi":"10.1080/15476286.2015.1022704","authors":"Li H, Hou J, Bai L, Hu C, Tong P, Kang Y, Zhao X, Shao Z","authors_abbrev":"Li H et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-10","publication_year":"2015","canto_session_key":"150d298a64370f52","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2015-10-28 18:02:49","canto_approved_date":"2021-01-31 01:44:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-28 18:00:52","canto_added_date":"2015-03-11 01:15:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-10-28"},{"uniquename":"PMID:16288715","title":"Alternative protein secretion: the Mam1 ABC transporter supports secretion of M-factor linked GFP in fission yeast.","citation":"Biochem Biophys Res Commun 2005 Dec 30;338(4):1853-9","abstract":"To examine whether the fission yeast Mam1 ABC transporter can be used for secretion of heterologous proteins, thereby bypassing the classical secretion pathway, we have analyzed chimeric forms of the M-factor precursor. It was demonstrated that GFP can be exported when fused to both the amino-terminal prosequence from mfm1 and a CaaX motif. This secretion was dependent on the Mam1 transporter and not the classical secretion pathway. The secretion efficiency of GFP, however, was relatively low and most of the reporter protein was trapped in the vacuolar membranes. Our findings suggest that the Mam1 ABC protein is a promiscuous peptide transporter that can accommodate globular proteins of a relatively large size. Furthermore, our results help in defining the sequences required for processing and secretion of natural M-factor.","authors":"Kjaerulff S, Müller S, Jensen MR","authors_abbrev":"Kjaerulff S et al.","pubmed_publication_date":"30 Dec 2005","pubmed_entrez_date":"2005-11-18","publication_year":"2005","canto_session_key":"5f32676a85e99635","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-13 17:14:36","canto_approved_date":"2021-05-22 19:04:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-18 11:46:57","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25B2.02c","SPAPB8E5.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-02-13"},{"uniquename":"EMBL:AY034033","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17277378","title":"Novel mad2 alleles isolated in a Schizosaccharomyces pombe gamma-tubulin mutant are defective in metaphase arrest activity, but remain functional for chromosome stability in unperturbed mitosis.","citation":"Genetics 2007 Apr;175(4):1571-84","abstract":"A previously isolated fission yeast gamma-tubulin mutant containing apparently stabilized microtubules proliferated at an approximately identical rate as wild type, yet the mutant mitosis spindle dynamics were aberrant, particularly the kinetochore microtubule dynamics. Progression through mitosis in the mutant, however, resulted in mostly accurate chromosome segregation. In the absence of the spindle assembly checkpoint gene, mad2+, the spindle dynamics in the gamma-tubulin mutant were greatly compromised, leading to a high incidence of chromosome missegregation. Unlike in wild-type cells, green fluorescent protein (GFP)-tagged Mad2 protein often accumulated near one of the poles of an elongating spindle in the gamma-tubulin mutant. We isolated novel mad2 mutants that were defective in arresting mitotic progression upon gross perturbation of the spindle formation but remained functional for the viability of the gamma-tubulin mutant. Further, the mad2 mutations did not appreciably destabilize minichromosomes in unperturbed mitoses. When overexpressed ectopically, these mutant Mad2 proteins sequestered wild-type Mad2, preventing its function in mitotic checkpoint arrest, but not in minichromosome stability. These results indicated that the Mad2 functions required for checkpoint arrest and chromosome stability in unperturbed mitosis are genetically discernible. Immunoprecipitation studies demonstrated that GFP-fused mutant Mad2 proteins formed a Mad1-containing complex with altered stability compared to that formed with wild-type Mad2, providing clues to the novel mad2 mutant phenotype.","authors":"Tange Y, Niwa O","authors_abbrev":"Tange Y et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-02-06","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1322.12c","SPBC106.01","SPBC32F12.04","SPBC20F10.06","SPCC1795.01c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:16022431","title":"[Sumoylation].","citation":"Seikagaku 2005 Jun;77(6):545-51","abstract":"","authors":"Kikuchi Y","authors_abbrev":"Kikuchi Y","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-07-19","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19109383","title":"The chromodomain of Tf1 integrase promotes binding to cDNA and mediates target site selection.","citation":"J Virol 2009 Mar;83(6):2675-85","abstract":"The long terminal repeat (LTR) retrotransposon Tf1 of Schizosaccharomyces pombe integrates specifically into the promoters of pol II-transcribed genes. Its integrase (IN) contains a C-terminal chromodomain related to the chromodomains that bind to the N-terminal tail of histone H3. Although we have been unable to detect an interaction between histone tails and the chromodomain of Tf1 IN, it is possible that the chromodomain plays a role in directing IN to its target sites. To test this idea, we generated transposons with single amino acid substitutions in highly conserved residues of the chromodomain and created a chromodomain-deleted mutant. The mutations, V1290A, Y1292A, W1305A, and CHDDelta, substantially reduced transposition activity in vivo. Blotting assays showed that there was little or no reduction in the levels of IN or cDNA. By measuring the homologous recombination between cDNA and the plasmid copy of Tf1, we found that two of the mutations did not reduce the import of cDNA into the nucleus, while another caused a 33% reduction. Chromatin immunoprecipitation assays revealed that CHDDelta caused an approximately threefold reduction in the binding of IN to the downstream LTR of the cDNA. These data indicate that the chromodomain contributed directly to integration. We therefore tested whether the chromodomain contributed to selecting insertion sites. Results of a target plasmid assay showed that the deletion of the chromodomain resulted in a drastic reduction in the preference for pol II promoters. Collectively, these data indicate that the chromodomain promotes binding of cDNA and plays a key role in efficient targeting.","doi":"10.1128/JVI.01588-08","authors":"Chatterjee AG, Leem YE, Kelly FD, Levin HL","authors_abbrev":"Chatterjee AG et al.","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2008-12-26","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22349141","title":"Small RNA in the nucleus: the RNA-chromatin ping-pong.","citation":"Curr Opin Genet Dev 2012 Apr;22(2):164-71","abstract":"Eukaryotes use several classes of small RNA molecules to guide diverse protein machineries to target messenger RNA. The role of small RNA in post-transcriptional regulation of mRNA stability and translation is now well established. Small RNAs can also guide sequence-specific modification of chromatin structure and thus contribute to establishment and maintenance of distinct chromatin domains. In this review we summarize the model for the inter-dependent interaction between small RNA and chromatin that has emerged from studies on fission yeast and plants. We focus on recent results that link a distinct class of small RNAs, the piRNAs, to chromatin regulation in animals.","doi":"10.1016/j.gde.2012.01.002","authors":"Olovnikov I, Aravin AA, Fejes Toth K","authors_abbrev":"Olovnikov I et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-02-22","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22442847","title":"High-frequency transformation of the fission yeast Schizosaccharomyces pombe.","citation":"Nature 1981 Mar 12;290(5802):140-2","abstract":"The fission yeast, Schizosaccharomyces pombe, has been used extensively for genetic studies but until now it has not been utilized as a host organism for DNA cloning. Here we describe a method for high-frequency transformation fo a leu 1(-) strain of this yeast with hybrid plasmids containing the Saccharomyces cerevisiae LEu 2(+) gene, a bacterial plasmid and either the S. cerevisiae 2 μm plasmid or autonomously replicating sequences (ars)(1) derived from S. pombe DNA. Some of the plasmids contain unique restriction sites which make them suitable for the isolation of S. pombe genes, and they can also be used for the exchange of DNA between S. pombe and S. cerevisiae.","authors":"Beach D, Nurse P","authors_abbrev":"Beach D et al.","pubmed_publication_date":"12 Mar 1981","pubmed_entrez_date":"2012-03-27","publication_year":"1981","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:23:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32034051","title":"How to turn an organism into a model organism in 10 'easy' steps.","citation":"J Exp Biol 2020 Feb 07;223(Pt Suppl 1)","abstract":"Many of the major biological discoveries of the 20th century were made using just six species:  Escherichia coli  bacteria,  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe  yeast,  Caenorhabditis elegans  nematodes,  Drosophila melanogaster  flies and  Mus musculus  mice. Our molecular understanding of the cell division cycle, embryonic development, biological clocks and metabolism were all obtained through genetic analysis using these species. Yet the 'big 6' did not start out as genetic model organisms (hereafter 'model organisms'), so how did they mature into such powerful systems? First, these model organisms are abundant human commensals: they are the bacteria in our gut, the yeast in our beer and bread, the nematodes in our compost pile, the flies in our kitchen and the mice in our walls. Because of this, they are cheaply, easily and rapidly bred in the laboratory and in addition were amenable to genetic analysis. How and why should we add additional species to this roster? We argue that specialist species will reveal new secrets in important areas of biology and that with modern technological innovations like next-generation sequencing and CRISPR-Cas9 genome editing, the time is ripe to move beyond the big 6. In this review, we chart a 10-step path to this goal, using our own experience with the  Aedes aegypti  mosquito, which we built into a model organism for neurobiology in one decade. Insights into the biology of this deadly disease vector require that we work with the mosquito itself rather than modeling its biology in another species.","doi":"10.1242/jeb.218198","authors":"Matthews BJ, Vosshall LB","authors_abbrev":"Matthews BJ et al.","pubmed_publication_date":"07 Feb 2020","pubmed_entrez_date":"2020-02-09","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34119521","title":"Schizosaccharomyces pombe Ppr10 and Mpa1 together mediate mitochondrial translational initiation.","citation":"J Biol Chem 2021 Jul;297(1):100869","abstract":"Pentatricopeptide repeat (PPR) proteins are a large family of proteins that act primarily at different posttranscriptional steps of organellar gene expression. We have previously found that the Schizosaccharomyces pombe PPR protein mpal10 interacts with mitochondrial translational activator Mpa1, and both are essential for mitochondrial protein synthesis. However, it is unclear how these two proteins function in mitochondrial protein synthesis in S. pombe. In this study, we further investigated the role of Ppr10 and Mpa1 in mitochondrial protein synthesis. Mitochondrial translational initiation requires two initiation factors, Mti2 and Mti3, which bind to the small subunit of the mitochondrial ribosome (mt-SSU) during the formation of the mitochondrial translational initiation complex. Using sucrose gradient sedimentation analysis, we found that disruption of ppr10, mpa1, or the PPR motifs in Ppr10 impairs the association of Mti2 and Mti3 with the mt-SSU, suggesting that both Ppr10 and Mpa1 may be required for the interaction of Mti2 and Mti3 with the mt-SSU during the assembly of mitochondrial translational initiation complex. Loss of Ppr10 perturbs the association of mitochondrially encoded cytochrome b (cob1) and cytochrome c oxidase subunit 1 (cox1) mRNAs with assembled mitochondrial ribosomes. Proteomic analysis revealed that a fraction of Ppr10 and Mpa1 copurified with a subset of mitoribosomal proteins. The PPR motifs of Ppr10 are necessary for its interaction with Mpa1 and that disruption of these PPR motifs impairs mitochondrial protein synthesis. Our results suggest that Ppr10 and Mpa1 function together to mediate mitochondrial translational initiation.","doi":"10.1016/j.jbc.2021.100869","authors":"Luo Y, Wang Y, Huang Y","authors_abbrev":"Luo Y et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-06-13","publication_year":"2021","canto_session_key":"811ad3c8dcd877f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying  Luo","canto_first_approved_date":"2024-10-29 08:35:03","canto_approved_date":"2024-10-30 15:54:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-10-21 15:14:34","canto_added_date":"2021-06-17 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying  Luo","community_curator":true,"annotation_count":38,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1E7.11c","SPAC29A4.03c","SPMIT.05","SPMIT.01","SPAC2F7.15","SPBC1105.03c","SPBC530.10c","SPMIT.07","SPBC13G1.01c","SPBC2D10.08c","SPBC2F12.02c","SPAC750.08c","SPBC18E5.13","SPBP4H10.18c","SPBC1271.15c","SPBP4H10.15","SPAC24C9.10c","SPBC11B10.04c","SPMIT.11","SPBC106.19","SPMIT.04","SPAC4F8.02c","SPAC4G9.17c"],"gene_count":23,"ltp_gene_count":12,"approved_date":"2024-10-29"},{"uniquename":"PMID:16458193","title":"Effect of nitrosative stress on Schizosaccharomyces pombe: inactivation of glutathione reductase by peroxynitrite.","citation":"Free Radic Biol Med 2006 Feb 15;40(4):625-31","abstract":"Oxidative stress has been shown to alter cellular redox status in various cell types. Changes in expressions of several antioxidative and antistress-responsive genes along with activation or inactivation of various proteins were also reported during oxidative insult as well as during nitrosative stress. In the present study, we show the effect of nitrosative stress on cellular redox status of fission yeast Schizosaccharomyces pombe. This is the first report of S-nitrosoglutathione (GSNO) reductase activity in S. pombe and its inactivation by GSNO. We also show the inactivation of glutathione reductase (GR) and glutathione peroxidase in the presence of various reactive nitrogen species in vivo. In addition, we first observe the inactivation of GR by peroxynitrite in vivo using S. pombe cells and also similar observations under in vitro conditions. An immunoreactive band against monoclonal anti-3-nitrotyrosine antibody confirms the modification of GR under in vitro conditions. We also show the effect of nitrosative stress on Deltapap1 cells of S. pombe, which are more sensitive to nitrosative stress, indicating the involvement of Pap1 in the protection against nitrosative stress. Finally, exposure of S. pombe cells to reactive nitrogen species reveals an important role of cellular thiol pool in protection against nitrosative stress.","authors":"Sahoo R, Dutta T, Das A, Sinha Ray S, Sengupta R, Ghosh S","authors_abbrev":"Sahoo R et al.","pubmed_publication_date":"15 Feb 2006","pubmed_entrez_date":"2006-02-07","publication_year":"2006","canto_session_key":"9ae9ed5e44a67f49","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:53:35","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 14:40:54","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-05"},{"uniquename":"Pfam:PF11559","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC13E7.06","HGNC:16509"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19597328","title":"Role of the protein kinase Kin1 and nuclear centering in actomyosin ring formation in fission yeast.","citation":"Cell Cycle 2009 Aug;8(15):2451-62","abstract":"Cytokinesis is the last step of the cell cycle, producing two daughter cells inheriting equal genetic information. This process involves the assembly of an actomyosin ring during mitosis. In the fission yeast Schizosaccharomyces pombe, cytokinesis occurs at the geometric cell centre, a position which is defined by the interphase nucleus and the anilin-related Mid1 protein. The pom1Delta, tea1Delta and tea4Delta mutants are defective in restricting Mid1 as a band around the nucleus and misplace the division site. We previously reported that inhibition of the protein kinase Kin1 promoted failure of cytokinesis in pom1Delta and tea1Delta cells but the mechanism involving Kin1 remained elusive. Here we investigated the contribution of Kin1 in cytokinesis. We show that Kin1-GFP has a dynamic cell cycle regulated distribution. Like pom1Delta and tea1Delta, tea4Delta exhibits a strong genetic interaction with kin1Delta. Using a conditional repressible kin1 allele that only alters interphase nuclear centering, we observed that Kin1 downregulation severely compromised actomyosin ring formation and septum synthesis in tea4Delta cells. In addition, nuclear displacement induced either by overexpression of a putative catalytically inactive Kin1 mutant, by chemically mediated microtubule depolymerization or by mutation in the par1Delta gene impaired cytokinesis in tea4Delta but not tea4(+) cells. We propose that nuclear mispositioning exacerbates the tea4Delta, pom1Delta and tea1Delta cell division phenotype. Our work reveal that nuclear centering becomes essential when Pom1/Tea1/Tea4 function is compromised and that Kin1 expression level is a key regulatory element in this situation. Our results suggest the existence of distinct overlapping control mechanisms to ensure efficient cell division.","authors":"Cadou A, La Carbona S, Couturier A, Le Goff C, Le Goff X","authors_abbrev":"Cadou A et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-07-15","publication_year":"2009","canto_session_key":"4a65f559e9059c86","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-11-27 14:59:34","canto_approved_date":"2024-11-27 14:59:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-27 14:59:28","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.16","SPBC530.04","SPBC1706.01","SPCC188.02","SPBC4F6.06","SPCC1322.01","SPAC6G10.02c","SPCC1223.06"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2024-11-27"},{"uniquename":"PMID:11605527","title":"[Recombinational repair in Schizosaccharomyces pombe: role in maintaining genomic integrity].","citation":"Mol Biol (Mosk) 2001;35(5):750-63","abstract":"Recombinational repair was first detected in budding yeast Saccharomyces cerevisiae and was also studied in fission yeast Schizosaccharomyces pombe over the recent decade. The discovery of Sch. pombe homologs of the S. cerevisiae RAD52 genes made it possible not only to identify and to clone their vertebrate counterparts, but also to study in detail the role of DNA recombination in certain cell processes. For instance, recombinational repair was shown to play a greater role in maintaining genome integrity in fission yeast and in vertebrates compared with S. cerevisiae. The present state of the problem of recombinational double-strand break repair in fission yeast is considered with a focus on comparisons between Sch. pombe and higher eukaryotes. The role of double-strand break repair in maintaining genome stability is discussed.","authors":"Khasanov FK, Bashkirov VI","authors_abbrev":"Khasanov FK et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-10-19","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15971585","title":"Enhancements in ethanol tolerance of a self-flocculating yeast by calcium ion through decrease in plasmalemma permeability.","citation":"Sheng Wu Gong Cheng Xue Bao 2003 Nov;19(6):715-9","abstract":"Ca2+ at 1.64 mmol/L markedly increased ethanol tolerance of a self-flocculating fusant of Schizosaccharomyces pombe and Saccharomyces cerevisiae. After 9 h of exposure to 20% (V/V) ethanol at 30 degrees C , no viability remained for the control whereas 50.0% remained for the cells both grown and incubated with ethanol in Ca2+ -added medium. Furthermore, when subjected to 15% (V/V) ethanol at 30 degrees C, the equilibrium nucleotide concentration and plasma membrane permeability coefficient (P' ) of the cells both grown and incubated with ethanol in Ca2+ -added medium accounted for only 50.0% and 29.3% those of the control respectively, indicating that adding Ca2+ can markedly reduce plasma membrane permeability of yeast cells under ethanol stress as compared with the control. Meanwhile, high viability levels acquired by the addition of Ca2+ exactly corresponded to the striking decreases in extracellular nucleotide concentration and P' achieved with identical approach. Therefore, the enhancing effect of Ca2+ on ethanol tolerance of this strain is closely related to its ability to decrease plasma membrane permeability of yeast cells subjected to ethanol stress.","authors":"Hu CK, Bai FW, An LJ","authors_abbrev":"Hu CK et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2005-06-24","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38740643","title":"Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP.","citation":"Cell Mol Life Sci 2024 May 13;81(1):216","abstract":"p50RhoGAP is a key protein that interacts with and downregulates the small GTPase RhoA. p50RhoGAP is a multifunctional protein containing the BNIP-2 and Cdc42GAP Homology (BCH) domain that facilitates protein-protein interactions and lipid binding and the GAP domain that regulates active RhoA population. We recently solved the structure of the BCH domain from yeast p50RhoGAP ( Y BCH) and showed that it maintains the adjacent GAP domain in an auto-inhibited state through the β5 strand. Our previous WT  Y BCH structure shows that a unique kink at position 116 thought to be made by a proline residue between alpha helices α6 and α7 is essential for the formation of intertwined dimer from asymmetric monomers. Here we sought to establish the role and impact of this Pro116. However, the kink persists in the structure of P116A mutant  Y BCH domain, suggesting that the scaffold is not dictated by the proline residue at this position. We further identified Tyr124 (or Tyr188 in  H BCH) as a conserved residue in the crucial β5 strand. Extending to the human ortholog, when substituted to acidic residues, Tyr188D or Tyr188E, we observed an increase in RhoA binding and self-dimerization, indicative of a loss of inhibition of the GAP domain by the BCH domain. These results point to distinct roles and impact of the non-conserved and conserved amino acid positions in regulating the structural and functional complexity of the BCH domain.","doi":"10.1007/s00018-024-05238-8","authors":"Shankar S, Chew TW, Chichili VPR, Low BC, Sivaraman J","authors_abbrev":"Shankar S et al.","pubmed_publication_date":"13 May 2024","pubmed_entrez_date":"2024-05-13","publication_year":"2024","canto_session_key":"9df678bde0965d0f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-06-15 08:46:15","canto_approved_date":"2024-06-15 08:48:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-15 08:46:07","canto_added_date":"2024-06-15 08:42:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-06-15","pdb_entries":[{"pdb_id":"8k70","gene_chains":[{"gene_uniquename":"SPAC1565.02c","chain":"A/B/C/D","position":"2-149"}],"title":"Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP","entry_authors":"Shankar S,Sivaraman J","entry_authors_abbrev":"Shankar S et al.","reference_uniquename":"PMID:38740643","experimental_method":"X-ray","resolution":"2.81"}]},{"uniquename":"PMID:14695938","title":"Pleiotropic phenotypes of fission yeast defective in ubiquinone-10 production. A study from the abc1Sp (coq8Sp) mutant.","citation":"Biofactors 2003;18(1-4):229-35","abstract":"We previously constructed two Schizosaccahromyces pombe ubiquinone-10 (or Coenzyme Q10) less mutants, which are either defective for decaprenyl diphosphate synthase or p-hydroxybenzoate polyprenyl diphosphate transferase. To further confirm the roles of ubiquinone in S. pombe, we examined the phenotype of the abc1Sp (coq8Sp) mutant, which is highly speculated to be defective in ubiquinone biosynthesis. We show here that the abc1Sp defective strain did not produce UQ-10 and could not grow on minimal medium. The abc1Sp-deficient strain required supplementation with antioxidants such as cysteine or glutathione to grow on minimal medium. In support of the antioxidant function of ubiquinone, the abc1Sp-deficient strain is sensitive to H2O2 and Cu2+. In addition, expression of the stress inducible ctt1 gene was much induced in the ubiquinone less mutant than wild type. Interestingly, we also found that the abc1-deficient strain as well as other ubiquinone less mutants produced a significant amount of H2S, which suggests that oxidation of sulfide by ubiquinone may be an important pathway for sulfur metabolism in S. pombe. Thus, analysis of the phenotypes of S. pombe ubiquinone less mutants clearly demonstrate that ubiquinone has multiple functions in the cell apart from being an integral component of the electron transfer system.","authors":"Saiki R, Ogiyama Y, Kainou T, Nishi T, Matsuda H, Kawamukai M","authors_abbrev":"Saiki R et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-12-30","publication_year":"2003","canto_session_key":"3153fb38b2948335","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-05-21 14:21:39","canto_approved_date":"2025-02-23 09:09:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-02 12:57:09","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.18","SPCC757.07c","SPBPJ4664.01","SPAC56F8.04c","SPBC2G5.06c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2013-05-21"},{"uniquename":"PMID:10388805","title":"Regulation of mRNA export by nutritional status in fission yeast.","citation":"Genetics 1999 Jul;152(3):827-38","abstract":"We have isolated a mutation in nup184(nup184-1) that is synthetically lethal with the mRNA export defective rae1-167 mutation in Schizosaccharomyces pombe. The consequence of the synthetic lethality is a defect in mRNA export. The predicted Nup184p is similar to Nup188p of Saccharomyces cerevisiae, and a Nup184p-GFP fusion localizes to the nuclear periphery in a punctate pattern. The Deltanup184 null mutant is viable and also is synthetically lethal with rae1-167. In a rae1(+) background, both the nup184-1 and Deltanup184 mutations confer sensitivity to growth in nutrient-rich medium (YES) that is accompanied by nuclear poly(A)+ RNA accumulation. Removal of the cAMP-dependent protein kinase, Pka1p, relieved the growth and mRNA export defects of nup184 mutants when grown in nutrient-rich medium. The activation of Pka1p is necessary, but not sufficient, to cause the severe poly(A)+ RNA export defects when nup184 mutant cells are incubated in YES, suggesting nutritional status can also regulate poly(A)+ RNA export. Our results suggest that the regulation of poly(A)+ RNA export by Pka1p kinase appears to be indirect, via a translation-dependent step, but post-translationally in response to YES.","authors":"Whalen WA, Yoon JH, Shen R, Dhar R","authors_abbrev":"Whalen WA et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-02","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP27G11.10c","SPBC16A3.05c","SPAC8C9.03","SPBC106.10"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"EMBL:AU009252","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12531008","title":"DNA structure dependent checkpoints as regulators of DNA repair.","citation":"DNA Repair (Amst) 2002 Dec 05;1(12):983-94","abstract":"Checkpoint proteins were initially identified because their loss of function resulted in defects in cell cycle arrest in response to genotoxic treatments. Initially, the analysis of checkpoint pathways concentrated on their function as signal transducers and how the checkpoint signals were communicated to the core cell cycle machinery and transcriptional apparatus. Although some of the early genetic analysis indicated a complex relationship between DNA replication, DNA repair and the checkpoint pathways, it is only now becoming apparent that checkpoint proteins regulate multiple DNA repair and replication functions. Furthermore, recent data suggest that some checkpoint proteins may participate directly in DNA repair events. In this review I summarise the current models for DNA structure-dependent checkpoint activation and review the evidence linking checkpoint proteins both directly and indirectly to DNA repair.","authors":"Carr AM","authors_abbrev":"Carr AM","pubmed_publication_date":"05 Dec 2002","pubmed_entrez_date":"2003-01-18","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32245232","title":"eIF4E and Interactors from Unicellular Eukaryotes.","citation":"Int J Mol Sci 2020 Mar 21;21(6)","abstract":"eIF4E, the mRNA cap-binding protein, is well known as a general initiation factor allowing for mRNA-ribosome interaction and cap-dependent translation in eukaryotic cells. In this review we focus on eIF4E and its interactors in unicellular organisms such as yeasts and protozoan eukaryotes. In a first part, we describe eIF4Es from yeast species such as  Saccharomyces cerevisiae ,  Candida albicans , and  Schizosaccharomyces pombe . In the second part, we will address eIF4E and interactors from parasite unicellular species-trypanosomatids and marine microorganisms-dinoflagellates. We propose that different strategies have evolved during evolution to accommodate cap-dependent translation to differing requirements. These evolutive \"adjustments\" involve various forms of eIF4E that are not encountered in all microorganismic species. In yeasts, eIF4E interactors, particularly p20 and Eap1 are found exclusively in Saccharomycotina species such as  S. cerevisiae  and  C. albicans . For protozoan parasites of the Trypanosomatidae family beside a unique cap4-structure located at the 5'UTR of all mRNAs, different eIF4Es and eIF4Gs are active depending on the life cycle stage of the parasite. Additionally, an eIF4E-interacting protein has been identified in  Leishmania major  which is important for switching from promastigote to amastigote stages. For dinoflagellates, little is known about the structure and function of the multiple and diverse eIF4Es that have been identified thanks to widespread sequencing in recent years.","doi":"10.3390/ijms21062170","authors":"Ross-Kaschitza D, Altmann M","authors_abbrev":"Ross-Kaschitza D et al.","pubmed_publication_date":"21 Mar 2020","pubmed_entrez_date":"2020-04-05","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-04-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733412","title":" Schizosaccharomyces japonicus : A Distinct Dimorphic Yeast among the Fission Yeasts.","citation":"Cold Spring Harb Protoc 2017 Dec 01;2017(12):pdb.top082651","abstract":"Genomic sequencing data and morphological properties demonstrate evolutionary relationships among groups of the fission yeast,  Schizosaccharomyces  Phylogenetically,  S. japonicus  is the furthest removed from other species of fission yeast. The basic characteristics of cell proliferation are shared among all fission yeast, including the process of binary fission during vegetative growth, conjugation and karyogamy with horsetail movement, mating-type switching, and sporulation. However,  S. japonicus  also exhibits characteristics that are unique to filamentous fungi.  S. japonicus  is a nonpathogenic yeast that exhibits dimorphism. Depending on the environmental conditions,  S. japonicus  transforms from yeast cells into filamentous cells (hyphae), and blue light triggers synchronous septation of hyphal cells. A rough version of the whole-genome sequence is now available, facilitating genetic manipulation of  S. japonicus.  Furthermore, the extensive genetic knowledge available for  S. pombe  is aiding the development of genetic tools for analyzing  S. japonicus. S. japonicus  will help shed light on the evolutionary relationships among the fission yeast.","doi":"10.1101/pdb.top082651","authors":"Aoki K, Furuya K, Niki H","authors_abbrev":"Aoki K et al.","pubmed_publication_date":"01 Dec 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40850401","title":"Optimized CUT&Tag enables robust epigenome profiling in Schizosaccharomyces pombe.","citation":"Methods 2025 Aug 22;","abstract":"We optimized permeabilization for CUT&Tag in S. pombe, enabling robust H3K9me3 profiling using lightly fixed permeabilized sepheroplasts, overcoming limitations of ChIP-seq including crosslinking artifacts and high cell input. We established an optimized Cleavage Under Targets and Tagmentation (CUT&Tag) protocol for high-resolution epigenome profiling inSchizosaccharomyces pombeusing Critical permeabilization refinements identified Lywallzyme as the optimal enzyme for spheroplast generation (>95 % efficiency in 60 min at 10 mg/mL), outperforming Zymolyase-20 T and combinatorial treatments. Systematic parameter optimization revealed concentration-dependent digestion kinetics and an inverse cell load-efficiency relationship (5 × 10 5  cells achieving > 90 % conversion in 50 min at 5 mg/mL). Validated through H3K9me3 mapping in wild-type andclr4Δstrains (10⁶ cells/replicate), this approach captured specific heterochromatic enrichment at centromeres/telomeres with complete signal ablation in mutants, while reduced spike-in DNA (0.2 pg) significantly enhanced signal-to-noise ratios. The protocol enables robust epigenomic analysis with minimal cell input and enhanced resolution.","doi":"10.1016/j.ymeth.2025.08.010","authors":"Huang CZ, Zhou KD, Ma W","authors_abbrev":"Huang CZ et al.","pubmed_publication_date":"22 Aug 2025","pubmed_entrez_date":"2025-08-24","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-08-25 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9443913","title":"Regulated vacuole fusion and fission in Schizosaccharomyces pombe: an osmotic response dependent on MAP kinases.","citation":"Curr Biol 1998 Jan 29;8(3):135-44","abstract":"The budding yeast Saccharomyces cerevisiae uses two mitogenactivated protein (MAP) kinase cascades, the Hog1p and the Mpk1p pathways, to signal responses to hypertonic and hypotonic stress, respectively. Mammalian cells and the fission yeast Schizosaccharomyces pombe have functional homologues of Hog1p - p38/RK/CSBP and Sty1 - which, unlike Hog1p, also mediate other responses. We have investigated the involvement of S. pombe MAP kinase pathways in signalling a newly described response to osmotic stress - that of vacuole fusion and fission.\nWhen S. pombe is placed into water, its vacuoles rapidly fuse into larger structures enclosing a greater proportion of the cell's volume. Under some conditions, its vacuoles can slowly fragment in response to salt. Fission requires the Sty1 pathway and also Pmk1, the homologue of S. cerevisiae Mpk1p. Fusion requires Pmk1, Ypt7 - the homologue of a protein involved in S. cerevisiae vacuole fusion - and part of the Sty1 pathway, although Sty1 phosphorylation is unaffected by hypotonic conditions.\nVacuole fusion and fission appear to be homeostatic mechanisms that restore the concentration of the cytosol. Vacuole fusion, like stimulated secretion in higher eukaryotes, is a rapid and specific process of membrane fusion in response to an external stimulus. The Sty1 pathway, in addition to its role in responding to hypertonic stress, is required at a basal level for the expression of factors required to respond to hypotonic stress - a mechanism that may allow the cell to use a common pathway for different responses.","authors":"Bone N, Millar JB, Toda T, Armstrong J","authors_abbrev":"Bone N et al.","pubmed_publication_date":"29 Jan 1998","pubmed_entrez_date":"1998-04-16","publication_year":"1998","canto_session_key":"771f80349bde5aa6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-07-28 16:38:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-28 16:38:41","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC405.04c","SPAC9G1.02","SPBC409.07c","SPAC1B3.11c","SPBC29B5.01","SPBC119.08"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2015-07-28"},{"uniquename":"PMID:18086878","title":"Two RNA polymerase I subunits control the binding and release of Rrn3 during transcription.","citation":"Mol Cell Biol 2008 Mar;28(5):1596-605","abstract":"Rpa34 and Rpa49 are nonessential subunits of RNA polymerase I, conserved in species from Saccharomyces cerevisiae and Schizosaccharomyces pombe to humans. Rpa34 bound an N-terminal region of Rpa49 in a two-hybrid assay and was lost from RNA polymerase in an rpa49 mutant lacking this Rpa34-binding domain, whereas rpa34Delta weakened the binding of Rpa49 to RNA polymerase. rpa34Delta mutants were caffeine sensitive, and the rpa34Delta mutation was lethal in a top1Delta mutant and in rpa14Delta, rpa135(L656P), and rpa135(D395N) RNA polymerase mutants. These defects were shared by rpa49Delta mutants, were suppressed by the overexpression of Rpa49, and thus, were presumably mediated by Rpa49 itself. rpa49 mutants lacking the Rpa34-binding domain behaved essentially like rpa34Delta mutants, but strains carrying rpa49Delta and rpa49-338::HIS3 (encoding a form of Rpa49 lacking the conserved C terminus) had reduced polymerase occupancy at 30 degrees C, failed to grow at 25 degrees C, and were sensitive to 6-azauracil and mycophenolate. Mycophenolate almost fully dissociated the mutant polymerase from its ribosomal DNA (rDNA) template. The rpa49Delta and rpa49-338::HIS3 mutations had a dual effect on the transcription initiation factor Rrn3 (TIF-IA). They partially impaired its recruitment to the rDNA promoter, an effect that was bypassed by an N-terminal deletion of the Rpa43 subunit encoded by rpa43-35,326, and they strongly reduced the release of the Rrn3 initiation factor during elongation. These data suggest a dual role of the Rpa49-Rpa34 dimer during the recruitment of Rrn3 and its subsequent dissociation from the elongating polymerase.","authors":"Beckouet F, Labarre-Mariotte S, Albert B, Imazawa Y, Werner M, Gadal O, Nogi Y, Thuriaux P","authors_abbrev":"Beckouet F et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2007-12-19","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733402","title":"Analysis of DNA Metabolism in Fission Yeast.","citation":"Cold Spring Harb Protoc 2018 Apr 02;2018(4)","abstract":"The fission yeast  Schizosaccharomyces pombe  is an excellent model organism to study DNA metabolism, in which the DNA replication and repair mechanisms are evolutionarily conserved. In this introduction we describe a range of methods commonly used to study aspects of DNA metabolism in fission yeast, focusing on approaches used for the analysis of genome stability, DNA replication, and DNA repair. We describe the use of a minichromosome, Ch 16 , for monitoring different aspects of genome stability. We introduce two-dimensional gel electrophoresis and immunofluorescent visualization of combed DNA molecules for the analysis of DNA replication. Further, we introduce a pulsed field gel electrophoresis (PFGE) assay to physically monitor chromosome integrity, which can be used in conjunction with a DNA double-strand break (DSB) repair assay to genetically quantitate different DSB repair and misrepair outcomes, including gross chromosomal rearrangements, in fission yeast.","doi":"10.1101/pdb.top079863","authors":"Antequera F, Humphrey TC","authors_abbrev":"Antequera F et al.","pubmed_publication_date":"02 Apr 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23555823","title":"Polypeptone induces dramatic cell lysis in ura4 deletion mutants of fission yeast.","citation":"PLoS One 2013;8(3):e59887","abstract":"Polypeptone is widely excluded from Schizosaccharomyces pombe growth medium. However, the reasons why polypeptone should be avoided have not been documented. Polypeptone dramatically induced cell lysis in the ura4 deletion mutant when cells approached the stationary growth phase, and this phenotype was suppressed by supplementation of uracil. To determine the specificity of this cell lysis phenotype, we created deletion mutants of other genes involved in de novo biosynthesis of uridine monophosphate (ura1, ura2, ura3, and ura5). Cell lysis was not observed in these gene deletion mutants. In addition, concomitant disruption of ura1, ura2, ura3, or ura5 in the ura4 deletion mutant suppressed cell lysis, indicating that cell lysis induced by polypeptone is specific to the ura4 deletion mutant. Furthermore, cell lysis was also suppressed when the gene involved in coenzyme Q biosynthesis was deleted. This is likely because Ura3 requires coenzyme Q for its activity. The ura4 deletion mutant was sensitive to zymolyase, which mainly degrades (1,3)-beta-D glucan, when grown in the presence of polypeptone, and cell lysis was suppressed by the osmotic stabiliser, sorbitol. Finally, the induction of cell lysis in the ura4 deletion mutant was due to the accumulation of orotidine-5-monophosphate. Cell wall integrity was dramatically impaired in the ura4 deletion mutant when grown in the presence of polypeptone. Because ura4 is widely used as a selection marker in S. pombe, caution needs to be taken when evaluating phenotypes of ura4 mutants.","doi":"10.1371/journal.pone.0059887","authors":"Matsuo Y, Nishino K, Mizuno K, Akihiro T, Toda T, Matsuo Y, Kaino T, Kawamukai M","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-04-05","publication_year":"2013","canto_session_key":"8bb15302799787a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai ","canto_first_approved_date":"2019-01-25 19:31:15","canto_approved_date":"2022-06-20 19:40:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-09 07:02:46","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Makoto Kawamukai ","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.18","SPBC725.15","SPAC22G7.06c","SPAC16.03c","SPCC330.05c","SPAC57A10.12c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-01-25"},{"uniquename":"PMID:15694304","title":"The Mad1/Mad2 complex as a template for Mad2 activation in the spindle assembly checkpoint.","citation":"Curr Biol 2005 Feb 08;15(3):214-25","abstract":"The spindle assembly checkpoint (SAC) imparts fidelity to chromosome segregation by delaying anaphase until all sister chromatid pairs have become bipolarly attached. Mad2 is a component of the SAC effector complex that sequesters Cdc20 to halt anaphase. In prometaphase, Mad2 is recruited to kinetochores with the help of Mad1, and it is activated to bind Cdc20. These events are linked to the existence of two distinct conformers of Mad2: a closed conformer bound to its kinetochore receptor Mad1 or its target in the checkpoint Cdc20 and an open conformer unbound to these ligands.\nWe investigated the mechanism of Mad2 recruitment to the kinetochore during checkpoint activation and subsequent transfer to Cdc20. We report that a closed conformer of Mad2 constitutively bound to Mad1, rather than Mad1 itself, is the kinetochore receptor for cytosolic open Mad2 and show that the interaction of open and closed Mad2 conformers is essential to sustain the SAC.\nWe propose that closed Mad2 bound to Mad1 represents a template for the conversion of open Mad2 into closed Mad2 bound to Cdc20. This simple model, which we have named the \"Mad2 template\" model, predicts a mechanism for cytosolic propagation of the spindle checkpoint signal away from kinetochores.","authors":"De Antoni A, Pearson CG, Cimini D, Canman JC, Sala V, Nezi L, Mapelli M, Sironi L, Faretta M, Salmon ED, Musacchio A","authors_abbrev":"De Antoni A et al.","pubmed_publication_date":"08 Feb 2005","pubmed_entrez_date":"2005-02-08","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-28 08:06:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7522655","title":"Localization of an alpha 1,2 galactosyltransferase activity to the Golgi apparatus of Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1994 May;5(5):519-28","abstract":"We have cloned a gene encoding an alpha 1,2 galactosyltransferase activity from Schizosaccharomyces pombe. The open reading frame of the gene (gma12 for galactomannan, alpha 1,2), combined with the previous protein purification (Chappell and Warren, 1989), predicts an O-linked glycoprotein with type II transmembrane topology. By homologous gene disruption, we have demonstrated that the gma12 gene product (gma12p) is nonessential. The deletion strain (gma12-D10::ura4) has a significantly reduced level of galactosyltransferase activity relative to the parental strain, but both in situ lectin binding and in vitro biochemical assays demonstrate the presence of further galactosyltransferase activity in addition to gma12p. Although gma12p is not the only galactosyltransferase in S. pombe, it produces a unique carbohydrate structure on the surface of the yeast cells. We have generated a polyclonal antiserum against this carbohydrate epitope and shown that gma12p is capable of synthesizing the epitope both in vitro and in vivo. Electron microscopic localization of the gma12+ specific epitope in gma12+ cells revealed that gma12p synthesizes the carbohydrate structure in the Golgi apparatus, and subsequent intracellular transport distributes the epitope to later stages of the secretory pathway. The immunolocalization studies confirm the presence of one or more galactosyltransferase activities in the Golgi apparatus in fission yeast.","authors":"Chappell TG, Hajibagheri MA, Ayscough K, Pierce M, Warren G","authors_abbrev":"Chappell TG et al.","pubmed_publication_date":"May 1994","pubmed_entrez_date":"1994-05-01","publication_year":"1994","canto_session_key":"8c6fa414440558a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-11-26 17:27:18","canto_approved_date":"2022-02-24 11:53:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-26 17:26:45","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-26"},{"uniquename":"PMID:18399988","title":"The endogenous adrenodoxin reductase-like flavoprotein arh1 supports heterologous cytochrome P450-dependent substrate conversions in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2008 May;8(3):432-41","abstract":"Mitochondrial cytochromes P450 are essential for biosynthesis of steroid hormones, vitamin D and bile acids. In mammals, the electrons needed for these reactions are provided via adrenodoxin and adrenodoxin reductase (AdR). Recently, Schizosaccharomyces pombe was introduced as a new host for the functional expression of human mitochondrial steroid hydroxylases without the coexpression of their natural redox partners. This fact qualifies S. pombe for the biotechnological production of steroids and for application as inhibitor test organism of heterologously expressed cytochromes P450. In this paper, we present evidence that the S. pombe ferredoxin reductase, arh1, and ferredoxin, etp1fd provide mammalian class I cytochromes P450 with reduction equivalents. The recombinant reductase showed an unusual weak binding of flavin adenine dinucleotide (FAD), which was mastered by modifying the FAD-binding region by site-directed mutagenesis yielding a stable holoprotein. The modified reductase arh1_A18G displayed spectroscopic characteristics similar to AdR and was shown to be capable of accepting electrons with no evident preference for NADH or NADPH, respectively. Arh1_A18G can substitute for AdR by interacting not only with its natural redox partner etp1fd but also with the mammalian homolog adrenodoxin. Cytochrome P450-dependent substrate conversion with all combinations of the mammalian and yeast redox proteins was evaluated in a reconstituted system.","doi":"10.1111/j.1567-1364.2008.00360.x","authors":"Ewen KM, Schiffler B, Uhlmann-Schiffler H, Bernhardt R, Hannemann F","authors_abbrev":"Ewen KM et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-04-11","publication_year":"2008","canto_session_key":"aeadfc528237dc96","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-12 10:30:20","canto_approved_date":"2018-04-09 14:22:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-03-12 10:30:01","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B8.01c","HGNC:3642","SPAC22E12.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-12"},{"uniquename":"PMID:10535928","title":"Identification and reconstitution of the origin recognition complex from Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1999 Oct 26;96(22):12367-72","abstract":"The origin recognition complex (ORC), first identified in Saccharomyces cerevisiae (sc), is a six-subunit protein complex that binds to DNA origins. Here, we report the identification and cloning of cDNAs encoding the six subunits of the ORC of Schizosaccharomyces pombe (sp). Sequence analyses revealed that spOrc1, 2, and 5 subunits are highly conserved compared with their counterparts from S. cerevisiae, Xenopus, Drosophila, and human. In contrast, both spOrc3 and spOrc6 subunits are poorly conserved. As reported by Chuang and Kelly [(1999) Proc. Natl. Acad. Sci. USA 96, 2656-2661], the C-terminal region of spOrc4 is also conserved whereas the N terminus uniquely contains repeats of a sequence that binds strongly to AT-rich DNA regions. Consistent with this, extraction of S. pombe chromatin with 1 M NaCl, or after DNase I treatment, yielded the six-subunit ORC, whereas extraction with 0.3 M resulted in five-subunit ORC lacking spOrc4p. The spORC can be reconstituted in vitro with all six recombinant subunits expressed in the rabbit reticulocyte system. The association of spOrc4p with the other subunits required the removal of DNA from reaction mixture by DNase I. This suggests that a strong interaction between spOrc4p and DNA can prevent the isolation of the six-subunit ORC. The unique DNA-binding properties of the spORC may contribute to our understanding of the sequence-specific recognition required for the initiation of DNA replication in S. pombe.","authors":"Moon KY, Kong D, Lee JK, Raychaudhuri S, Hurwitz J","authors_abbrev":"Moon KY et al.","pubmed_publication_date":"26 Oct 1999","pubmed_entrez_date":"1999-10-27","publication_year":"1999","canto_session_key":"051d2527dd3dd99c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2013-01-23 15:38:30","canto_approved_date":"2021-09-28 14:28:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-23 15:37:31","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2A9.12","SPAC3H1.01c","SPBP23A10.13","SPBC646.14c","SPBC29A10.15","SPBC685.09"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2013-01-23"},{"uniquename":"PMID:19833516","title":"Cellular quiescence: are controlling genes conserved?","citation":"Trends Cell Biol 2009 Dec;19(12):705-15","abstract":"The fission yeast Schizosaccharomyces pombe is an excellent model for cellular quiescence that can be achieved experimentally with nutritional limitations. The target of rapamycin complex (TORC) is known to be important for the transition between proliferation and quiescence from yeast to humans, and the recently identified TORC components, Tti1 and Tel2, might control all of the cellular phosphoinositide 3-kinase-related kinases. New pilot studies using deletion mutants and temperature-sensitive mutants suggest that up to approximately 1000 genes are required for quiescence, and approximately 300 of these, called superhousekeeping genes, also participate in proliferation. These latest findings suggest that genes controlling quiescence are conserved from yeast to humans, and support the use of S. pombe as a model to enhance our understanding of the causes of aging, diabetes, obesity and neurodegeneration.","doi":"10.1016/j.tcb.2009.09.006","authors":"Yanagida M","authors_abbrev":"Yanagida M","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-10-17","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8502556","title":"The SpGAR1 gene of Schizosaccharomyces pombe encodes the functional homologue of the snoRNP protein GAR1 of Saccharomyces cerevisiae.","citation":"Nucleic Acids Res 1993 May 11;21(9):2149-55","abstract":"GAR1 is a nucleolar protein which is associated with small nucleolar RNAs (snoRNAs) and which is required for pre-ribosomal RNA processing. In Saccharomyces cerevisiae, the GAR1 gene is essential for cell viability. We have cloned and sequenced the GAR1 gene from the distantly related yeast Schizosaccharomyces pombe. The SpGAR1 gene, which contains two small introns, codes for a 194 amino-acid protein of 20 kDa. A protein sequence comparison indicates that SpGAR1 is 65% identical to ScGAR1. Anti-ScGAR1 antibodies recognize SpGAR1, emphasizing the structural conservation of the protein. Immunostaining of S.pombe cells with these antibodies reveals that SpGAR1 is localized in the nucleolus, as is the case in S.cerevisiae. Moreover, SpGAR1 can substitute for GAR1 in S.cerevisiae, indicating that the two proteins are functionally equivalent. These results suggest a parallel evolutionary conservation of proteins and RNAs with which GAR1 interacts in mediating its pre-rRNA processing and viability functions. After fibrillarin, GAR1 is the second protein of the snoRNPs shown to have been conserved throughout evolution.","authors":"Girard JP, Caizergues-Ferrer M, Lapeyre B","authors_abbrev":"Girard JP et al.","pubmed_publication_date":"11 May 1993","pubmed_entrez_date":"1993-05-11","publication_year":"1993","canto_session_key":"e4ceedd8235af3f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-08-14 16:12:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-14 16:12:39","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-14"},{"uniquename":"PMID:32062975","title":"Phosphoproteomics Reveals Novel Targets and Phosphoprotein Networks in Cell Cycle Mediated by Dsk1 Kinase.","citation":"J Proteome Res 2020 Apr 03;19(4):1776-1787","abstract":"As the ortholog of human SR protein kinase 1 in fission yeast  Schizosaccharomyces pombe , Dsk1 specifically phosphorylates SR proteins (serine/arginine-rich proteins) and promotes splicing of nonconsensus introns. The SRPK (SR protein-specific kinase) family performs highly conserved functions in eukaryotic cells including cell proliferation, differentiation, development, and apoptosis. Although Dsk1 was originally identified as a mitotic regulator, its specific targets involved in cell cycle have yet been unexplored. In this study, using a phosphoproteomics approach, we examined differential protein phosphorylation between wild-type cells and  dsk1 -deletion mutants. We found reduced phosphorylation of 149 peptides corresponding to 133 proteins in the  dsk1 -null cells. These proteins are involved in various cellular processes, including cytoskeleton organization and signal transduction, and specifically enriched in multiple steps of cell cycle control. Further, targeted MS analyses and in vitro biochemical assays established Cdr2 protein kinase and kinesin motor Klp9 as novel substrates of Dsk1, which function in cell size control for mitotic entry and in chromosome segregation for mitotic exit, respectively. The phosphoprotein networks mediated by Dsk1 reveal, for the first time, the molecular links connecting Dsk1 to mitotic phase transition, sister-chromatid segregation, and cytokinesis, providing further evidence of Dsk1's diverse influence on cell cycle progression and regulation.","doi":"10.1021/acs.jproteome.0c00027","authors":"Wu M, Feng G, Zhang B, Xu K, Wang Z, Cheng S, Chang C, Vyas A, Tang Z, Liu X","authors_abbrev":"Wu M et al.","pubmed_publication_date":"03 Apr 2020","pubmed_entrez_date":"2020-02-18","publication_year":"2020","canto_session_key":"522133ffc88d3f1f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Zhaohua (Irene) Tang","canto_first_approved_date":"2021-01-09 16:46:03","canto_approved_date":"2023-12-24 11:00:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-29 02:51:12","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Zhaohua (Irene) Tang","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":149,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"PMID_32062975_modification.tsv"},{"name":"Val Wood","community_curator":false,"annotation_count":149,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_32062975_phaf.tsv"}],"genes":["SPAPB1A10.08","SPCC550.09","SPBC428.07","SPBC216.05","SPBC32H8.02c","SPCC16C4.02c","SPAC29B12.10c","SPBC2F12.03c","SPBC2D10.04","SPAC144.03","SPAC23H4.06","SPAC31A2.14","SPBC13A2.04c","SPAC15A10.13","SPAC30C2.08","SPBC21C3.15c","SPAC664.10","SPAC1635.01","SPBC13E7.01","SPCC162.12","SPAPB17E12.13","SPAC26A3.09c","SPAC27D7.03c","SPAC5D6.13","SPAC1B1.04c","SPBC3E7.10","SPBC1778.02","SPBC28F2.11","SPCC1682.13","SPBC19F5.03","SPAC24H6.09","SPAC4F10.13c","SPAC1805.05","SPCC1840.10","SPBC19C2.13c","SPBC18H10.08c","SPAC57A10.02","SPAC29A4.11","SPBC15D4.03","SPCP1E11.05c","SPAC521.04c","SPAC890.03","SPBC16H5.02","SPCC2H8.02","SPBC15D4.01c","SPBC4F6.06","SPCC285.13c","SPAC23D3.06c","SPAC18G6.10","SPBC28F2.12","SPAC19D5.06c","SPBC20F10.07","SPAC10F6.17c","SPBC12D12.04c","SPBC2F12.05c","SPBC36.02c","SPCC162.07","SPAC19A8.12","SPBC354.15","SPAC4H3.11c","SPAC24H6.05","SPBC1604.20c","SPBC557.04","SPBC1778.09","SPBC11C11.02","SPBC25B2.07c","SPCC23B6.04c","SPCC645.07","SPAC16E8.14c","SPAC13A11.01c","SPBC1271.09","SPCC584.03c","SPAC3F10.11c","SPBC18H10.04c","SPCC895.07","SPBC4C3.05c","SPAC821.08c","SPAC1952.16","SPAC17A2.09c","SPAC17A2.13c","SPBC36.11","SPCC962.01","SPAC19A8.01c","SPBC530.14c","SPBC13G1.02","SPCC1494.10","SPAC29B12.07","SPAC18G6.05c","SPAPYUK71.03c","SPCC1235.05c","SPAC22G7.06c","SPBC1289.01c","SPAC20G8.05c","SPAC9G1.10c","SPCC18B5.03","SPBC1685.10","SPAPB1A10.13","SPAC1786.03","SPAC1A6.07","SPBC800.10c","SPCC1919.10c","SPAC227.07c","SPBC30D10.15","SPBC32F12.10","SPCC663.01c","SPAC16C9.05","SPAC17A5.16","SPAC1782.10c","SPAC1782.09c","SPAC25G10.09c","SPBC725.09c","SPCC63.14","SPCC16C4.07","SPAC3H1.02c","SPAC23H4.17c","SPBC18E5.07","SPAC3A11.02","SPCC338.17c","SPCC1442.02","SPAC19E9.02","SPBC17G9.03c","SPAC3A12.13c","SPAC6B12.05c","SPAC13G7.04c","SPCC1919.15","SPCC70.05c","SPBC947.13","SPBC3E7.01","SPCC417.07c","SPAC20G8.06","SPAC10F6.06","SPAC343.14c","SPAC30D11.04c"],"gene_count":133,"ltp_gene_count":4,"approved_date":"2021-01-09"},{"uniquename":"EMBL:SPC00831","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19370027","title":"Kinetochore geometry defined by cohesion within the centromere.","citation":"Nature 2009 Apr 16;458(7240):852-8","abstract":"During cell division microtubules capture chromosomes by binding to the kinetochore assembled in the centromeric region of chromosomes. In mitosis sister chromatids are captured by microtubules emanating from both spindle poles, a process called bipolar attachment, whereas in meiosis I sisters are attached to microtubules originating from one spindle pole, called monopolar attachment. For determining chromosome orientation, kinetochore geometry or structure might be an important target of regulation. However, the molecular basis of this regulation has remained elusive. Here we show the link between kinetochore orientation and cohesion within the centromere in fission yeast Schizosaccharomyces pombe by strategies developed to visualize the concealed cohesion within the centromere, and to introduce artificial tethers that can influence kinetochore geometry. Our data imply that cohesion at the core centromere induces the mono-orientation of kinetochores whereas cohesion at the peri-centromeric region promotes bi-orientation. Our study may reveal a general mechanism for the geometric regulation of kinetochores, which collaborates with previously defined tension-dependent reorientation machinery.","doi":"10.1038/nature07876","authors":"Sakuno T, Tada K, Watanabe Y","authors_abbrev":"Sakuno T et al.","pubmed_publication_date":"16 Apr 2009","pubmed_entrez_date":"2009-04-17","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPAC31A2.15c","SPAC110.02","SPBC902.02c","SPAC15E1.07c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:34282727","title":"Pak1 kinase controls cell shape through ribonucleoprotein granules.","citation":"Elife 2021 Jul 20;10","abstract":"Fission yeast cells maintain a rod shape due to conserved signaling pathways that organize the cytoskeleton for polarized growth. We discovered a mechanism linking the conserved protein kinase Pak1 with cell shape through the RNA-binding protein Sts5. Pak1 (also called Shk1 and Orb2) prevents Sts5 association with P bodies by directly phosphorylating its intrinsically disordered region (IDR). Pak1 and the cell polarity kinase Orb6 both phosphorylate the Sts5 IDR but at distinct residues. Mutations preventing phosphorylation in the Sts5 IDR cause increased P body formation and defects in cell shape and polarity. Unexpectedly, when cells encounter glucose starvation, PKA signaling triggers Pak1 recruitment to stress granules with Sts5. Through retargeting experiments, we reveal that Pak1 localizes to stress granules to promote rapid dissolution of Sts5 upon glucose addition. Our work reveals a new role for Pak1 in regulating cell shape through ribonucleoprotein granules during normal and stressed growth conditions.","doi":"10.7554/eLife.67648","authors":"Magliozzi JO, Moseley JB","authors_abbrev":"Magliozzi JO et al.","pubmed_publication_date":"20 Jul 2021","pubmed_entrez_date":"2021-07-20","publication_year":"2021","canto_session_key":"6f48460fcf5d72c1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-07-22 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16C4.09","SPAC821.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:29925533","title":"Fission Yeast CENP-C (Cnp3) Plays a Role in Restricting the Site of CENP-A Accumulation.","citation":"G3 (Bethesda) 2018 Jul 31;8(8):2723-2733","abstract":"The centromere is a chromosomal locus where a microtubule attachment site, termed kinetochore, is assembled in mitosis. In most eukaryotes, with the exception of holocentric species, each chromosome contains a single distinct centromere. A chromosome with an additional centromere undergoes successive rounds of anaphase bridge formation and breakage, or triggers a cell cycle arrest imposed by DNA damage and replication checkpoints. We report here a study in  Schizosaccharomyces pombe  to characterize a mutant ( cnp3-1 ) in a gene encoding a homolog of mammalian centromere-specific protein, CENP-C. At the restrictive temperature 36°, the Cnp3-1 mutant protein loses its localization at the centromere. In the  cnp3-1  mutant, the level of the Cnp1 (a homolog of a centromere-specific histone CENP-A) also decreases at the centromere. Interestingly, the  cnp3-1  mutant is prone to promiscuous accumulation of Cnp1 at non-centromeric regions, when Cnp1 is present in excess. Unlike the wild type protein, Cnp3-1 mutant protein is found at the sites of promiscuous accumulation of Cnp1, suggesting that Cnp3-1 may stabilize or promote accumulation of Cnp1 at non-centromeric regions. From these results, we infer the role of Cnp3 in restricting the site of accumulation of Cnp1 and thus to prevent formation of  de novo  centromeres.","doi":"10.1534/g3.118.200486","authors":"Suma M, Kitagawa T, Nakase Y, Nakazawa N, Yanagida M, Matsumoto T","authors_abbrev":"Suma M et al.","pubmed_publication_date":"31 Jul 2018","pubmed_entrez_date":"2018-06-22","publication_year":"2018","canto_session_key":"0f27b899c5dbe35d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-06-23 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1861.01c","SPCC970.12"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:30573453","title":"Anti-silencing factor Epe1 associates with SAGA to regulate transcription within heterochromatin.","citation":"Genes Dev 2019 Jan 01;33(1-2):116-126","abstract":"Heterochromatin is a highly condensed form of chromatin that silences gene transcription. Although high levels of transcriptional activities disrupt heterochromatin, transcription of repetitive DNA elements and subsequent processing of the transcripts by the RNAi machinery are required for heterochromatin assembly. In fission yeast, a JmjC domain protein, Epe1, promotes transcription of DNA repeats to facilitate heterochromatin formation, but overexpression of Epe1 leads to heterochromatin defects. However, the molecular function of Epe1 is not well understood. By screening the fission yeast deletion library, we found that heterochromatin defects associated with Epe1 overexpression are alleviated by mutations of the SAGA histone acetyltransferase complex. Overexpressed Epe1 associates with SAGA and recruits SAGA to heterochromatin regions, which leads to increased histone acetylation, transcription of repeats, and the disruption of heterochromatin. At its normal expression levels, Epe1 also associates with SAGA, albeit weakly. Such interaction regulates histone acetylation levels at heterochromatin and promotes transcription of repeats for heterochromatin assembly. Our results also suggest that increases of certain chromatin protein levels, which frequently occur in cancer cells, might strengthen relatively weak interactions to affect the epigenetic landscape.","doi":"10.1101/gad.318030.118","authors":"Bao K, Shan CM, Moresco J, Yates J, Jia S","authors_abbrev":"Bao K et al.","pubmed_publication_date":"01 Jan 2019","pubmed_entrez_date":"2018-12-22","publication_year":"2019","canto_session_key":"4d56e9e82da23d80","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kehan Bao","canto_first_approved_date":"2019-06-28 13:54:28","canto_approved_date":"2025-07-02 16:24:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-25 19:54:53","canto_added_date":"2018-12-24 01:15:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":82,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kehan Bao","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPAC15A10.02","SPBP16F5.03c","SPCC5E4.03c","SPBC887.18c","SPAC13A11.04c","SPBC14C8.17c","SPCC622.16c","SPBC800.03","SPAC12G12.05c","SPBC25H2.11c","SPAC4D7.10c","SPCC16C4.18c","SPBC21H7.02","SPBC428.08c","SPBC16D10.07c","SPBC28F2.10c","SPBC1921.07c","SPAC1952.05","SPCC24B10.08c","SPAC57A10.14","SPCC61.02"],"gene_count":22,"ltp_gene_count":21,"approved_date":"2019-06-28"},{"uniquename":"PMID:39527193","title":"Live Imaging of Fission Yeast Single-Cell Lineages Using a Microfluidic Device.","citation":"Methods Mol Biol 2025;2862:61-76","abstract":"Mother machine (MM) is a microfluidic device originally developed for long-term live imaging of Escherichia coli bacterial cells under a microscope. The simple yet sophisticated design has enabled microbiologists to track multiple single-cell lineages cultured under highly controlled external environments. Here, I describe how to fabricate a fission yeast version of MM with photolithography and soft lithography. Procedures for setting up the microfluidic device for long-term live microscopy are also explained.","doi":"10.1007/978-1-0716-4168-2_5","authors":"Nakaoka H","authors_abbrev":"Nakaoka H","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39878217","title":"The ortholog of human DNAJC9 promotes histone H3-H4 degradation and is counteracted by Asf1 in fission yeast.","citation":"Nucleic Acids Res 2025 Jan 24;53(3)","abstract":"Mammalian J-domain protein DNAJC9 interacts with histones H3-H4 and is important for cell proliferation. However, its exact function remains unclear. Here, we show that, in the fission yeast Schizosaccharomyces pombe, loss of Djc9, the ortholog of DNAJC9, renders the histone chaperone Asf1 no longer essential for growth. Utilizing AlphaFold-based structural prediction, we identified a histone-binding surface on Djc9 that binds to helix α3 of H3 in a manner that precludes simultaneous helix α3-binding by Asf1. Djc9 and Asf1 indeed compete for binding to the H3-H4 dimer in vitro, and an H3-α3 mutation impeding Djc9 binding also renders Asf1 non-essential, indicating that the role of Asf1 needed for growth in fission yeast is to prevent histone binding by Djc9. In the absence of Asf1, cell growth is hindered due to unrestrained Djc9-mediated downregulation of H3 and H4. In the presence of Asf1, Djc9 confers resistance to the DNA replication inhibitor hydroxyurea and dominant negative disease-related histone mutants by promoting the degradation of superfluous or dysfunctional histones. Our findings provide new insights into the function and mechanism of this conserved histone-binding protein.","doi":"10.1093/nar/gkaf036","authors":"Ding Y, Li J, Jiang HL, Suo F, Shao GC, Zhang XR, Dong MQ, Liu CP, Xu RM, Du LL","authors_abbrev":"Ding Y et al.","pubmed_publication_date":"24 Jan 2025","pubmed_entrez_date":"2025-01-29","publication_year":"2025","canto_session_key":"ed6002ed7638d5e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yan Ding","canto_first_approved_date":"2025-03-25 17:32:34","canto_approved_date":"2026-02-03 07:41:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-02-17 02:24:36","canto_added_date":"2025-01-30 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":74,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Yan Ding","community_curator":true,"annotation_count":29,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.03c","SPAC13G7.02c","SPAC1834.04","SPBC1105.12","SPBC31F10.13c","SPBC342.06c","SPAC1071.09c","SPCC663.05c","SPAC23H4.12","SPBC8D2.04","SPBC1105.11c","SPAC1834.03c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2025-03-25"},{"uniquename":"PMID:1922021","title":"The conserved carboxy-terminal domain of Saccharomyces cerevisiae TFIID is sufficient to support normal cell growth.","citation":"Mol Cell Biol 1991 Oct;11(10):4809-21","abstract":"We have examined the structure-function relationships of TFIID through in vivo complementation tests. A yeast strain was constructed which lacked the chromosomal copy of SPT15, the gene encoding TFIID, and was therefore dependent on a functional plasmid-borne wild-type copy of this gene for viability. By using the plasmid shuffle technique, the plasmid-borne wild-type TFIID gene was replaced with a family of plasmids containing a series of systematically mutated TFIID genes. These various forms of TFIID were expressed from three different promoter contexts of different strengths, and the ability of each mutant form of TFIID to complement our chromosomal TFIID null allele was assessed. We found that the first 61 amino acid residues of TFIID are totally dispensable for vegetative cell growth, since yeast strains containing this deleted form of TFIID grow at wild-type rates. Amino-terminally deleted TFIID was further shown to be able to function normally in vivo by virtue of its ability both to promote accurate transcription initiation from a large number of different genes and to interact efficiently with the Gal4 protein to activate transcription of GAL1 with essentially wild-type kinetics. Any deletion removing sequences from within the conserved carboxy-terminal region of S. cerevisiae TFIID was lethal. Further, the exact sequence of the conserved carboxy-terminal portion of the molecule is critical for function, since of several heterologous TFIID homologs tested, only the highly related Schizosaccharomyces pombe gene could complement our S. cerevisiae TFIID null mutant. Taken together, these data indicate that all important functional domains of TFIID appear to lie in its carboxy-terminal 179 amino acid residues. The significance of these findings regarding TFIID function are discussed.","authors":"Poon D, Schroeder S, Wang CK, Yamamoto T, Horikoshi M, Roeder RG, Weil PA","authors_abbrev":"Poon D et al.","pubmed_publication_date":"Oct 1991","pubmed_entrez_date":"1991-10-01","publication_year":"1991","canto_session_key":"47d27b5313b683fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 12:28:32","canto_session_submitted_date":"2012-03-03 12:28:05","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:26098872","title":"Genetic Interactions between the Members of the SMN-Gemins Complex in Drosophila.","citation":"PLoS One 2015;10(6):e0130974","abstract":"The SMN-Gemins complex is composed of Gemins 2-8, Unrip and the survival motor neuron (SMN) protein. Limiting levels of SMN result in the neuromuscular disorder, spinal muscular atrophy (SMA), which is presently untreatable. The most-documented function of the SMN-Gemins complex concerns the assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs). Despite multiple genetic studies, the Gemin proteins have not been identified as prominent modifiers of SMN-associated mutant phenotypes. In the present report, we make use of the Drosophila model organism to investigate whether viability and motor phenotypes associated with a hypomorphic Gemin3 mutant are enhanced by changes in the levels of SMN, Gemin2 and Gemin5 brought about by various genetic manipulations. We show a modifier effect by all three members of the minimalistic fly SMN-Gemins complex within the muscle compartment of the motor unit. Interestingly, muscle-specific overexpression of Gemin2 was by itself sufficient to depress normal motor function and its enhanced upregulation in all tissues leads to a decline in fly viability. The toxicity associated with increased Gemin2 levels is conserved in the yeast S. pombe in which we find that the cytoplasmic retention of Sm proteins, likely reflecting a block in the snRNP assembly pathway, is a contributing factor. We propose that a disruption in the normal stoichiometry of the SMN-Gemins complex depresses its function with consequences that are detrimental to the motor system.","doi":"10.1371/journal.pone.0130974","authors":"Borg RM, Bordonne R, Vassallo N, Cauchi RJ","authors_abbrev":"Borg RM et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-06-23","publication_year":"2015","canto_session_key":"259aebc0ce336450","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-08-02 19:47:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-02 12:38:41","canto_added_date":"2015-06-24 00:20:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19B12.12c","SPAPB17E12.02","SPAC26A3.08","SPAC2G11.08c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2016-08-02"},{"uniquename":"PMID:25619998","title":"The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.","citation":"Structure 2015 Feb 03;23(2):332-41","abstract":"N-terminal acetylation is among the most common protein modifications in eukaryotes and is mediated by evolutionarily conserved N-terminal acetyltransferases (NATs). NatD is among the most selective NATs; its only known substrates are histones H4 and H2A, containing the N-terminal sequence SGRGK in humans. Here we characterize the molecular basis for substrate-specific acetylation by NatD by reporting its crystal structure bound to cognate substrates and performing related biochemical studies. A novel N-terminal segment wraps around the catalytic core domain to make stabilizing interactions, and the α1-α2 and β6-β7 loops adopt novel conformations to properly orient the histone N termini in the binding site. Ser1 and Arg3 of the histone make extensive contacts to highly conserved NatD residues in the substrate binding pocket, and flanking glycine residues also appear to contribute to substrate-specific binding by NatD, together defining a Ser-Gly-Arg-Gly recognition sequence. These studies have implications for understanding substrate-specific acetylation by NAT enzymes.","doi":"10.1016/j.str.2014.10.025","authors":"Magin RS, Liszczak GP, Marmorstein R","authors_abbrev":"Magin RS et al.","pubmed_publication_date":"03 Feb 2015","pubmed_entrez_date":"2015-01-27","publication_year":"2015","canto_session_key":"7c7509b7ad78573d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-20 08:20:35","canto_approved_date":"2026-02-04 17:13:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-19 18:59:40","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC825.04c","SPAC1834.03c","SPBC8D2.03c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2023-02-20","pdb_entries":[{"pdb_id":"4ua3","gene_chains":[{"gene_uniquename":"SPCC825.04c","chain":"A/B","position":"1-190"}],"title":"Crystal structure of selenomethionine labeled SpNatD","entry_authors":"Magin RS,Liszczak GP,Marmorstein R","entry_authors_abbrev":"Magin RS et al.","reference_uniquename":"PMID:25619998","experimental_method":"X-ray","resolution":"1.85"}]},{"uniquename":"PMID:12732265","title":"Evolutionary origins of mechanosensitive ion channels.","citation":"Prog Biophys Mol Biol 2003;82(1-3):11-24","abstract":"According to the recent revision, the universal phylogenetic tree is composed of three domains: Eukarya (eukaryotes), Bacteria (eubacteria) and Archaea (archaebacteria). Mechanosensitive (MS) ion channels have been documented in cells belonging to all three domains suggesting their very early appearance during evolution of life on Earth. The channels show great diversity in conductance, selectivity and voltage dependence, while sharing the property of being gated by mechanical stimuli exerted on cell membranes. In prokaryotes, MS channels were first documented in Bacteria followed by their discovery in Archaea. The finding of MS channels in archaeal cells helped to recognize and establish the evolutionary relationship between bacterial and archaeal MS channels and to show that this relationship extends to eukaryotic Fungi (Schizosaccharomyces pombe) and Plants (Arabidopsis thaliana). Similar to their bacterial and archaeal homologues, MS channels in eukaryotic cell-walled Fungi and Plants may serve in protecting the cellular plasma membrane from excessive dilation and rupture that may occur during osmotic stress. This review summarizes briefly some of the recent developments in the MS channel research field that may ultimately lead to elucidation of the biophysical and evolutionary principles underlying the mechanosensory transduction in living cells.","authors":"Martinac B, Kloda A","authors_abbrev":"Martinac B et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-05-07","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18003699","title":"In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain.","citation":"J Cell Sci 2007 Dec 01;120(Pt 23):4093-8","abstract":"Intracellular movement is a fundamental property of all cell types. Many organelles and molecules are actively transported throughout the cytoplasm by molecular motors, such as the dimeric type V myosins. These possess a long neck, which contains an IQ motif, that allow it to make 36-nm steps along the actin polymer. Live cell imaging of the fission yeast type V myosin Myo52 reveals that the protein moves rapidly throughout the cytoplasm. Here, we describe analysis of this movement and have established that Myo52 moves long distances on actin filaments in an ATP-dependent manner at approximately 0.5 mum/second. Myo51 and the microtubule cytoskeleton have no discernable role in modulating Myo52 movements, whereas rigour mutations in Myo52 abrogated its movement. We go on to show that, although dimerisation is required for Myo52 movement, deleting its neck has no discernable affect on Myo52 function or velocity in vivo.","authors":"Grallert A, Martín-García R, Bagley S, Mulvihill DP","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"01 Dec 2007","pubmed_entrez_date":"2007-11-16","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1919.10c","SPAC3A12.14"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:19233281","title":"Genome-wide mapping of nucleosome positions in Schizosaccharomyces pombe.","citation":"Methods 2009 Jul;48(3):218-25","abstract":"The majority of nuclear eukaryotic DNA is packaged into nucleosome cores where DNA is wrapped tightly around histone protein octamers. Such histone bound nucleosomal DNA is less accessible than the short linker DNA between nucleosome cores or the DNA in extended nucleosome free regions. Therefore, the positions of nucleosomes relative to a DNA sequence feature, like a transactivator binding site, a transcriptional start site or an origin of replication, can have profound effects on nuclear processes like transcription, replication, recombination and repair. Now that many DNA related processes are studied in a genome-wide manner, it is increasingly important to map the basic organization of their chromosomal DNA substrate, i.e., the positions of nucleosomes, on a genome-wide scale as well. To this end, the protection of nucleosomal DNA from digestion with micrococcal nuclease (MNase) is used as an assay for the presence of a nucleosome. The MNase protected DNA fragments, so called mononucleosomal DNA, can be mapped genome-wide by hybridization to microarrays. This method has been established for Saccharomyces cerevisiae, and we present here the adaptation of the method for Schizosaccharomyces pombe. As an independent method to validate genome-wide data for individual loci, we also include a protocol for the determination of locus specific nucleosome positioning by indirect end labeling.","doi":"10.1016/j.ymeth.2009.02.004","authors":"Lantermann A, Strålfors A, Fagerström-Billai F, Korber P, Ekwall K","authors_abbrev":"Lantermann A et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-02-24","publication_year":"2009","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22084197","title":"AP endonuclease independent repair of abasic sites in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2012 Mar;40(5):2000-9","abstract":"Abasic (AP) sites are formed spontaneously and are inevitably intermediates during base excision repair of DNA base damages. AP sites are both mutagenic and cytotoxic and key enzymes for their removal are AP endonucleases. However, AP endonuclease independent repair initiated by DNA glycosylases performing β,δ-elimination cleavage of the AP sites has been described in mammalian cells. Here, we describe another AP endonuclease independent repair pathway for removal of AP sites in Schizosaccharomyces pombe that is initiated by a bifunctional DNA glycosylase, Nth1 and followed by cleavage of the baseless sugar residue by tyrosyl phosphodiesterase Tdp1. We propose that repair is completed by the action of a polynucleotide kinase, a DNA polymerase and finally a DNA ligase to seal the gap. A fission yeast double mutant of the major AP endonuclease Apn2 and Tdp1 shows synergistic increase in MMS sensitivity, substantiating that Apn2 and Tdp1 process the same substrate. These results add new knowledge to the complex cellular response to AP sites, which could be exploited in chemotherapy where synthetic lethality is a key strategy of treatment.","doi":"10.1093/nar/gkr933","authors":"Nilsen L, Forstrøm RJ, Bjørås M, Alseth I","authors_abbrev":"Nilsen L et al.","pubmed_publication_date":"Mar 2012","pubmed_entrez_date":"2011-11-16","publication_year":"2012","canto_session_key":"6101d4a4d449a1cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-11-19 15:17:28","canto_approved_date":"2024-12-31 08:47:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-19 15:15:53","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.10","SPCP31B10.05","SPAC30D11.10","SPAC30D11.07"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2020-11-19"},{"uniquename":"PMID:7874752","title":"Physical mapping of the Schizosaccharomyces pombe histone genes.","citation":"Curr Genet 1994;26(5-6):553-6","abstract":"The histone-encoding genes in Schizosaccharomyces pombe were physically mapped by hybridisation to filters containing cosmid and P1 genomic libraries. The H2A.2 gene and the H2A.1-H2B.1 gene pair mapped between the ade6 and rikI genes on chromosome III. The three H4-H3 gene pairs were mapped to three different regions by a H4.1 probe. Southern analysis of clones from each region revealed the positions of the three H4-H3 gene pairs. H4.1-H3.1 was localised to chromosome I between the mei2 and rad1 genes; H4.2-H3.2 mapped between rad3 and cdc2 on chromosome II; H4.3-H3.3 was localised to a region between the nuc1 and puc1 genes on chromosome II.","authors":"Lind M, Lunderius C, Ekwall K, Olsson T","authors_abbrev":"Lind M et al.","pubmed_publication_date":"1994","pubmed_entrez_date":"1994-11-01","publication_year":"1994","canto_session_key":"0254dac718d99c7c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 14:57:52","canto_approved_date":"2019-01-07 14:57:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 14:57:45","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"EMBL:AJ632004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.34"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12124382","title":"The influence of the Cdc27 subunit on the properties of the Schizosaccharomyces pombe DNA polymerase delta.","citation":"J Biol Chem 2002 Sep 27;277(39):36853-62","abstract":"Schizosaccharomyces pombe DNA polymerase (pol) delta contains four subunits, pol 3, Cdc1, Cdc27, and Cdm1. In this report, we examined the role of Cdc27 on the structure and activity of pol delta. We show that the four-subunit complex is monomeric in structure, in contrast to the previous report that it was a dimer (Zuo, S., Bermudez, V., Zhang, G., Kelman, Z., and Hurwitz, J. (2000) J. Biol. Chem. 275, 5153-5162). This discrepancy between the earlier and recent observations was traced to the marked asymmetric shape of Cdc27. Cdc27 contains two critical domains that govern its role in activating pol delta. The N-terminal region (amino acids (aa) 1-160) binds to Cdc1 and its extreme C-terminal end (aa 362-369) interacts with proliferating cell nuclear antigen (PCNA). Mutants of S. pombe pol delta, containing truncated Cdc27 derivatives deficient in binding to PCNA, supported DNA replication less processively than the wild-type complex. Fusion of a minimal PCNA-binding motif (aa 352-372) to C-terminally truncated Cdc27 derivatives restored processive DNA synthesis in vitro. In vivo, the introduction of these fused Cdc27 derivatives into cdc27Delta cells conferred viability. These data support the model in which Cdc27 plays an essential role in DNA replication by recruiting PCNA to the pol delta holoenzyme.","authors":"Bermudez VP, MacNeill SA, Tappin I, Hurwitz J","authors_abbrev":"Bermudez VP et al.","pubmed_publication_date":"27 Sep 2002","pubmed_entrez_date":"2002-07-19","publication_year":"2002","canto_session_key":"206cc7cbc4e29e8a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-05-11 12:54:59","canto_approved_date":"2019-05-03 17:40:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-11 12:41:32","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":35,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPBC336.04","SPBC12D12.02c","SPBC1734.02c","SPAC27E2.05"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-05-11"},{"uniquename":"PMID:35584134","title":"Local chromatin context regulates the genetic requirements of the heterochromatin spreading reaction.","citation":"PLoS Genet 2022 May;18(5):e1010201","abstract":"Heterochromatin spreading, the expansion of repressive chromatin structure from sequence-specific nucleation sites, is critical for stable gene silencing. Spreading re-establishes gene-poor constitutive heterochromatin across cell cycles but can also invade gene-rich euchromatin de novo to steer cell fate decisions. How chromatin context (i.e. euchromatic, heterochromatic) or different nucleation pathways influence heterochromatin spreading remains poorly understood. Previously, we developed a single-cell sensor in fission yeast that can separately record heterochromatic gene silencing at nucleation sequences and distal sites. Here we couple our quantitative assay to a genetic screen to identify genes encoding nuclear factors linked to the regulation of heterochromatin nucleation and the distal spreading of gene silencing. We find that mechanisms underlying gene silencing distal to a nucleation site differ by chromatin context. For example, Clr6 histone deacetylase complexes containing the Fkh2 transcription factor are specifically required for heterochromatin spreading at constitutive sites. Fkh2 recruits Clr6 to nucleation-distal chromatin sites in such contexts. In addition, we find that a number of chromatin remodeling complexes antagonize nucleation-distal gene silencing. Our results separate the regulation of heterochromatic gene silencing at nucleation versus distal sites and show that it is controlled by context-dependent mechanisms. The results of our genetic analysis constitute a broad community resource that will support further analysis of the mechanisms underlying the spread of epigenetic silencing along chromatin.","doi":"10.1371/journal.pgen.1010201","authors":"Greenstein RA, Ng H, Barrales RR, Tan C, Braun S, Al-Sady B","authors_abbrev":"Greenstein RA et al.","pubmed_publication_date":"May 2022","pubmed_entrez_date":"2022-05-18","publication_year":"2022","canto_session_key":"41a01463c40db2a7","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-05-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18551545","title":"The fission yeast Schizosaccharomyces pombe in continuous culture.","citation":"Biotechnol Bioeng 1983 Aug;25(8):1989-94","abstract":"The fission yeast Schizosaccharomyces pombe was cultivated in a chemostat at dilution rates of D = 0.03, 0.05, 0.10, and 0.20 h(-1). After steady state had been reached, the amount of dry matter, number of cells, concentration of residual sugar, yield coefficient (Y), and some morphological properties of the cells were estimated. Curves reflecting the dry mass, number of cells, and cell mean volume show a changing coordination between the growth rate and the rate of cell division, with respect to D. In addition, it could be concluded that in dividing cells the cell septum is localized asymmetrically; Two nonidentical cells differing both in length and volume result. The degree of asymmetry is a function of the dilution rate.","authors":"Vraná D","authors_abbrev":"Vraná D","pubmed_publication_date":"Aug 1983","pubmed_entrez_date":"1983-08-01","publication_year":"1983","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30020956","title":"ProfPPIdb: Pairs of physical protein-protein interactions predicted for entire proteomes.","citation":"PLoS One 2018;13(7):e0199988","abstract":"Protein-protein interactions (PPIs) play a key role in many cellular processes. Most annotations of PPIs mix experimental and computational data. The mix optimizes coverage, but obfuscates the annotation origin. Some resources excel at focusing on reliable experimental data. Here, we focused on new pairs of interacting proteins for several model organisms based solely on sequence-based prediction methods.\nWe extracted reliable experimental data about which proteins interact (binary) for eight diverse model organisms from public databases, namely from Escherichia coli, Schizosaccharomyces pombe, Plasmodium falciparum, Drosophila melanogaster, Caenorhabditis elegans, Mus musculus, Rattus norvegicus, Arabidopsis thaliana, and for the previously used Homo sapiens and Saccharomyces cerevisiae. Those data were the base to develop a PPI prediction method for each model organism. The method used evolutionary information through a profile-kernel Support Vector Machine (SVM). With the resulting eight models, we predicted all possible protein pairs in each organism and made the top predictions available through a web application. Almost all of the PPIs made available were predicted between proteins that have not been observed in any interaction, in particular for less well-studied organisms. Thus, our work complements existing resources and is particularly helpful for designing experiments because of its uniqueness. Experimental annotations and computational predictions are strongly influenced by the fact that some proteins have many partners and others few. To optimize machine learning, recent methods explicitly ignored such a network-structure and rely either on domain knowledge or sequence-only methods. Our approach is independent of domain-knowledge and leverages evolutionary information. The database interface representing our results is accessible from https://rostlab.org/services/ppipair/. The data can also be downloaded from https://figshare.com/collections/ProfPPI-DB/4141784.","doi":"10.1371/journal.pone.0199988","authors":"Tran L, Hamp T, Rost B","authors_abbrev":"Tran L et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-07-19","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-07-20 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28502612","title":"MARRVEL: Integration of Human and Model Organism Genetic Resources to Facilitate Functional Annotation of the Human Genome.","citation":"Am J Hum Genet 2017 Jun 01;100(6):843-853","abstract":"One major challenge encountered with interpreting human genetic variants is the limited understanding of the functional impact of genetic alterations on biological processes. Furthermore, there remains an unmet demand for an efficient survey of the wealth of information on human homologs in model organisms across numerous databases. To efficiently assess the large volume of publically available information, it is important to provide a concise summary of the most relevant information in a rapid user-friendly format. To this end, we created MARRVEL (model organism aggregated resources for rare variant exploration). MARRVEL is a publicly available website that integrates information from six human genetic databases and seven model organism databases. For any given variant or gene, MARRVEL displays information from OMIM, ExAC, ClinVar, Geno2MP, DGV, and DECIPHER. Importantly, it curates model organism-specific databases to concurrently display a concise summary regarding the human gene homologs in budding and fission yeast, worm, fly, fish, mouse, and rat on a single webpage. Experiment-based information on tissue expression, protein subcellular localization, biological process, and molecular function for the human gene and homologs in the seven model organisms are arranged into a concise output. Hence, rather than visiting multiple separate databases for variant and gene analysis, users can obtain important information by searching once through MARRVEL. Altogether, MARRVEL dramatically improves efficiency and accessibility to data collection and facilitates analysis of human genes and variants by cross-disciplinary integration of 18 million records available in public databases to facilitate clinical diagnosis and basic research.","doi":"10.1016/j.ajhg.2017.04.010","authors":"Wang J, Al-Ouran R, Hu Y, Kim SY, Wan YW, Wangler MF, Yamamoto S, Chao HT, Comjean A, Mohr SE, UDN, Perrimon N, Liu Z, Bellen HJ","authors_abbrev":"Wang J et al.","pubmed_publication_date":"01 Jun 2017","pubmed_entrez_date":"2017-05-16","publication_year":"2017","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2017-05-17 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33983119","title":"Rapid adaptation of endocytosis, exocytosis, and eisosomes after an acute increase in membrane tension in yeast cells.","citation":"Elife 2021 May 13;10","abstract":"During clathrin-mediated endocytosis (CME) in eukaryotes, actin assembly is required to overcome large membrane tension and turgor pressure. However, the molecular mechanisms by which the actin machinery adapts to varying membrane tension remain unknown. In addition, how cells reduce their membrane tension when they are challenged by hypotonic shocks remains unclear. We used quantitative microscopy to demonstrate that cells rapidly reduce their membrane tension using three parallel mechanisms. In addition to using their cell wall for mechanical protection, yeast cells disassemble eisosomes to buffer moderate changes in membrane tension on a minute time scale. Meanwhile, a temporary reduction in the rate of endocytosis for 2-6 min and an increase in the rate of exocytosis for at least 5 min allow cells to add large pools of membrane to the plasma membrane. We built on these results to submit the cells to abrupt increases in membrane tension and determine that the endocytic actin machinery of fission yeast cells rapidly adapts to perform CME. Our study sheds light on the tight connection between membrane tension regulation, endocytosis, and exocytosis.","doi":"10.7554/eLife.62084","authors":"Lemière J, Ren Y, Berro J","authors_abbrev":"Lemière J et al.","pubmed_publication_date":"13 May 2021","pubmed_entrez_date":"2021-05-13","publication_year":"2021","canto_session_key":"d3da12ac766d9be6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-15 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19182789","title":"The heterochromatin protein Swi6/HP1 activates replication origins at the pericentromeric region and silent mating-type locus.","citation":"Nat Cell Biol 2009 Mar;11(3):357-62","abstract":"Heterochromatin is a structurally compacted region of chromosomes in which transcription and recombination are inactivated. DNA replication is temporally regulated in heterochromatin, but the molecular mechanism for regulation has not been elucidated. Among heterochromatin loci in Schizosaccharomyces pombe, the pericentromeric region and the silent mating-type (mat) locus replicate in early S phase, whereas the sub-telomeric region does not, suggesting complex mechanisms for regulation of replication in heterochromatic regions. Here, we show that Swi6, an S. pombe counterpart of heterochromatin protein 1 (HP1), is required for early replication of the pericentromeric region and the mat locus. Origin-loading of Sld3, which depends on Dfp1/Dbf4-dependent kinase Cdc7 (DDK), is stimulated by Swi6. An HP1-binding motif within Dfp1 is required for interaction with Swi6 in vitro and for early replication of the pericentromeric region and mat locus. Tethering of Dfp1 to the pericentromeric region and mat locus in swi6-deficient cells restores early replication of these loci. Our results show that a heterochromatic protein positively regulates initiation of replication in silenced chromatin by interacting with an essential kinase.","doi":"10.1038/ncb1845","authors":"Hayashi MT, Takahashi TS, Nakagawa T, Nakayama J, Masukata H","authors_abbrev":"Hayashi MT et al.","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2009-02-03","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11333219","title":"Control of GT repeat stability in Schizosaccharomyces pombe by mismatch repair factors.","citation":"Genetics 2001 May;158(1):77-85","abstract":"The mismatch repair (MMR) system ensures genome integrity by removing mispaired and unpaired bases that originate during replication. A major source of mutational changes is strand slippage in repetitive DNA sequences without concomitant repair. We established a genetic assay that allows measuring the stability of GT repeats in the ade6 gene of Schizosaccharomyces pombe. In repair-proficient strains most of the repeat variations were insertions, with addition of two nucleotides being the most frequent event. GT repeats were highly destabilized in strains defective in msh2 or pms1. In these backgrounds, mainly 2-bp insertions and 2-bp deletions occurred. Surprisingly, essentially the same high mutation rate was found with mutants defective in msh6. In contrast, a defect in swi4 (a homologue of Msh3) caused only slight effects, and instability was not further increased in msh6 swi4 double mutants. Also inactivation of exo1, which encodes an exonuclease that has an MMR-dependent function in repair of base-base mismatches, caused only slightly increased repeat instability. We conclude that Msh2, Msh6, and Pms1 have an important role in preventing tract length variations in dinucleotide repeats. Exo1 and Swi4 have a minor function, which is at least partially independent of MMR.","authors":"Mansour AA, Tornier C, Lehmann E, Darmon M, Fleck O","authors_abbrev":"Mansour AA et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-03","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8F11.03","SPCC285.16c","SPBC19G7.01c","SPAC19G12.02c","SPBC29A10.05"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:3530635","title":"Control of cell growth and division in Saccharomyces cerevisiae.","citation":"CRC Crit Rev Biochem 1986;21(2):153-223","abstract":"Considerable advances have been made in recent years in our understanding of the biochemistry of protein and nucleic acid synthesis and, particularly, the molecular biology of gene expression in eukaryotes. The yeast Saccharomyces cerevisiae, and to a lesser extent Schizosaccharomyces pombe, has had a preeminent role as a focus for these studies, principally because of the facility with which these organisms can be experimentally manipulated biochemically and genetically. This review will be designed to critically examine and integrate recent advances in several vital areas of regulatory control of enzyme synthesis in yeast: structure and organization of DNA, transcriptional regulation, post-transcriptional modification, control of translation, post-translational modification and secretion, and cell-cycle modulation. It will attempt to emphasize and illustrate, where detailed information is available, principal underlying molecular mechanisms, and it will attempt to make relevant comparisons of this material to inferred and demonstrated facets of regulatory control of enzyme and protein synthesis in higher eukaryotes.","authors":"Hanes SD, Koren R, Bostian KA","authors_abbrev":"Hanes SD et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6094974","title":"The mitochondrial genome of the fission yeast Schizosaccharomyces pombe. 2. Localization of genes by interspecific hybridization in strain ade7-50h- and cloning of the genome in small fragments.","citation":"Mol Gen Genet 1984;196(3):465-72","abstract":"A series of 18 small overlapping restriction fragments has been cloned, covering the complete mitochondrial genome of Schizosaccharomyces pombe. By hybridizing mitochondrial gene probes from Saccharomyces cerevisiae and Neurospora crassa with restriction fragments of Schizosaccharomyces pombe mitochondrial DNA, the following homologous genes were localized on the mitochondrial genome of S. pombe: cob, cox1, cox2 and cox3, ATPase subunit 6 and 9 genes, the large rRNA gene and both types of open reading frames occurring in mitochondrial introns of various ascomycetes. The region of the genome, hybridizing with cob exon probes is separated by an intervening sequence of about 2500 bp, which is homologous with the first two introns of the cox1 gene in Saccharomyces cerevisiae (class II introns according to Michel et al. 1982). Similarly, in the cox1 homologous region, which covers about 4000 bp, two regions were detected hybridizing with class I intron probes, suggesting the existence of two cox1 introns in Schizosaccharomyces pombe. Hybridization with several specific exon probes with a determined order has revealed that cob, cox1, cox3 and the large rRNA gene are all transcribed from the same DNA strand. The low intensities of hybridization signals suggest a large evolutionary distance between Schizosaccharomyces pombe and Saccharomyces cerevisiae or Neurospora crassa mitochondrial genes. Considering the length of the mitochondrial DNA of Schizosaccharomyces pombe (about 19.4 kbp) and the expected length of the localized genes and intron sequences there is enough space left for encoding the expected set of tRNAs and the small rRNA gene. The existence of leader-, trailer-, ori- and spacer sequences or further unassigned reading frames is then restricted to a total length of about 3000 bp only.","authors":"Lang BF, Wolf K","authors_abbrev":"Lang BF et al.","pubmed_publication_date":"1984","pubmed_entrez_date":"1984-01-01","publication_year":"1984","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18270439","title":"Involvement of 3-methyladenine DNA glycosylases Mag1p and Mag2p in base excision repair of methyl methanesulfonate-damaged DNA in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Genet Syst 2007 Dec;82(6):489-94","abstract":"Schizosaccharomyces pombe has two paralogues of 3-methyladenine DNA glycosylase, Mag1p and Mag2p, which share homology with Escherichia coli AlkA. To clarify the function of these redundant enzymes in base excision repair (BER) of alkylation damage, we performed several genetic analyses. The mag1 and mag2 single mutants as well as the double mutant showed no obvious methyl methanesulfonate (MMS) sensitivity. Deletion of mag1 or mag2 from an nth1 mutant resulted in tolerance to MMS damage, indicating that both enzymes generate AP sites in vivo by removal of methylated bases. A rad16 mutant that is deficient in nucleotide excision repair (NER) exhibited moderate MMS sensitivity. Deletion of mag1 from the rad16 mutant greatly enhanced MMS sensitivity, and the mag2 deletion also weakened the resistance to MMS of the rad16 mutant. A mag1/mag2/rad16 triple mutant was most sensitive to MMS. These results suggest that the NER pathway obscures the mag1 and mag2 functions in MMS resistance and that both paralogues initiate the BER pathway of MMS-induced DNA damage at the same level in NER-deficient cells or that Mag2p tends to make a little lower contribution than Mag1p. Mag1p and Mag2p functioned additively in vivo. Expression of mag1 and mag2 in the triple mutant confirmed the contribution of Mag1p and Mag2p to BER of MMS resistance.","authors":"Kanamitsu K, Tanihigashi H, Tanita Y, Inatani S, Ikeda S","authors_abbrev":"Kanamitsu K et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2008-02-14","publication_year":"2007","canto_session_key":"da5dd67da841ea04","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-03 10:43:07","canto_approved_date":"2020-11-30 10:46:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-11 18:11:22","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB24D3.04c","SPBC23G7.11","SPAC30D11.07","SPBC3D6.10","SPCC970.01"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-06-03"},{"uniquename":"PMID:27465359","title":"How do fission yeast cells grow and connect growth to the mitotic cycle?","citation":"Curr Genet 2017 May;63(2):165-173","abstract":"To maintain size homeostasis in a unicellular culture, cells should coordinate growth to the division cycle. This is achieved via size control mechanisms (also known as size checkpoints), i.e. some events during the mitotic cycle supervene only if the cell has reached a critical size. Rod-shaped cells like those of fission yeast are ideal model organisms to study these checkpoints via time-lapse microphotography. By applying this method, once we can analyse the growth process between two consecutive divisions at a single (or even at an 'average') cellular level, moreover, we can also position the size checkpoint(s) at the population level. Finally, any of these controls can be abolished in appropriate cell cycle mutants, either in steady-state or in induction synchronised cultures. In the latter case, we produce abnormally oversized cells, and microscopic experiments with them clearly show the existence of a critical size above which the size checkpoint ceases (becomes cryptic). In this review, we delineate the development of our knowledge both on the growth mode of fission yeast and on the operating size control(s) during its mitotic cycle. We finish these historical stories with our recent findings, arguing that three different size checkpoints exist in the fission yeast cell cycle, namely in late G1, in mid G2 and in late G2, which has been concluded by analysing these controls in several cell cycle mutants.","doi":"10.1007/s00294-016-0632-0","authors":"Sveiczer Á, Horváth A","authors_abbrev":"Sveiczer Á et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2016-07-29","publication_year":"2017","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-07-30 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12351775","title":"Molecular biology. An RNA-guided pathway for the epigenome.","citation":"Science 2002 Sep 27;297(5590):2215-8","abstract":"","authors":"Jenuwein T","authors_abbrev":"Jenuwein T","pubmed_publication_date":"27 Sep 2002","pubmed_entrez_date":"2002-09-28","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22342545","title":"Noise reduction in the intracellular pom1p gradient by a dynamic clustering mechanism.","citation":"Dev Cell 2012 Mar 13;22(3):558-72","abstract":"Chemical gradients can generate pattern formation in biological systems. In the fission yeast Schizosaccharomyces pombe, a cortical gradient of pom1p (a DYRK-type protein kinase) functions to position sites of cytokinesis and cell polarity and to control cell length. Here, using quantitative imaging, fluorescence correlation spectroscopy, and mathematical modeling, we study how its gradient distribution is formed. Pom1p gradients exhibit large cell-to-cell variability, as well as dynamic fluctuations in each individual gradient. Our data lead to a two-state model for gradient formation in which pom1p molecules associate with the plasma membrane at cell tips and then diffuse on the membrane while aggregating into and fragmenting from clusters, before disassociating from the membrane. In contrast to a classical one-component gradient, this two-state gradient buffers against cell-to-cell variations in protein concentration. This buffering mechanism, together with time averaging to reduce intrinsic noise, allows the pom1p gradient to specify positional information in a robust manner.","doi":"10.1016/j.devcel.2012.01.001","authors":"Saunders TE, Pan KZ, Angel A, Guan Y, Shah JV, Howard M, Chang F","authors_abbrev":"Saunders TE et al.","pubmed_publication_date":"13 Mar 2012","pubmed_entrez_date":"2012-02-21","publication_year":"2012","canto_session_key":"3f8d375062f500bb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37400983","title":"Cooperative DNA-binding activities of Chp2 are critical for its function in heterochromatin assembly.","citation":"J Biochem 2023 Sep 29;174(4):371-382","abstract":"Heterochromatin protein 1 (HP1) is an evolutionarily conserved protein that plays a critical role in heterochromatin assembly. HP1 proteins share a basic structure consisting of an N-terminal chromodomain (CD) and a C-terminal chromoshadow domain (CSD) linked by a disordered hinge region. The CD recognizes histone H3 lysine 9 methylation, a hallmark of heterochromatin, while the CSD forms a dimer to recruit other chromosomal proteins. HP1 proteins have been shown to bind DNA or RNA primarily through the hinge region. However, how DNA or RNA binding contributes to their function remains elusive. Here, we focus on Chp2, one of the two HP1 proteins in fission yeast, and investigate how Chp2's DNA-binding ability contributes to its function. Similar to other HP1 proteins, the Chp2 hinge exhibits clear DNA-binding activity. Interestingly, the Chp2 CSD also shows robust DNA-binding activity. Mutational analysis revealed that basic residues in the Chp2 hinge and at the N-terminus of the CSD are essential for DNA binding, and the combined amino acid substitutions of these residues alter Chp2 stability, impair Chp2 heterochromatin localization and lead to a silencing defect. These results demonstrate that the cooperative DNA-binding activities of Chp2 play an important role in heterochromatin assembly in fission yeast.","doi":"10.1093/jb/mvad050","authors":"Rahayu AF, Hayashi A, Yoshimura Y, Nakagawa R, Arita K, Nakayama JI","authors_abbrev":"Rahayu AF et al.","pubmed_publication_date":"29 Sep 2023","pubmed_entrez_date":"2023-07-04","publication_year":"2023","canto_session_key":"ef8c7a4f76471904","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-ichi Nakayama","canto_first_approved_date":"2023-09-08 11:20:05","canto_approved_date":"2024-02-20 13:43:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-20 13:43:20","canto_added_date":"2023-07-05 00:15:05","annotation_curators":[{"name":"Jun-ichi Nakayama","community_curator":true,"annotation_count":9,"orcid":"0000-0002-5597-8239","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPBP35G2.10","SPBC16C6.10","SPBC428.08c","SPCC330.05c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2023-09-08"},{"uniquename":"PMID:16793539","title":"Destabilizing heterochromatin: Does Swi6/HP1 make the choice?","citation":"Mol Cell 2006 Jun 23;22(6):709-710","abstract":"HP1 is well known as a key silencing protein. However, in the June 9 issue of Molecular Cell, report that Swi6/HP1 recruits an antisilencing protein, Epe1, to facilitate transcription, leading to a model in which Swi6/HP1 is used as a platform to recruit both silencing and antisilencing activities.","doi":"10.1016/j.molcel.2006.06.004","authors":"Verdel A","authors_abbrev":"Verdel A","pubmed_publication_date":"23 Jun 2006","pubmed_entrez_date":"2006-06-24","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29432178","title":"General amino acid control in fission yeast is regulated by a nonconserved transcription factor, with functions analogous to Gcn4/Atf4.","citation":"Proc Natl Acad Sci U S A 2018 Feb 20;115(8):E1829-E1838","abstract":"Eukaryotes respond to amino acid starvation by enhancing the translation of mRNAs encoding b-ZIP family transcription factors ( GCN4  in  Saccharomyces cerevisiae  and  ATF4  in mammals), which launch transcriptional programs to counter this stress. This pathway involves phosphorylation of the eIF2 translation factor by Gcn2-protein kinases and is regulated by upstream ORFs (uORFs) in the  GCN4 / ATF4  5' leaders. Here, we present evidence that the transcription factors that mediate this response are not evolutionarily conserved. Although cells of the fission yeast  Schizosaccharomyces pombe  respond transcriptionally to amino acid starvation, they lack clear Gcn4 and Atf4 orthologs. We used ribosome profiling to identify mediators of this response in  S. pombe , looking for transcription factors that behave like  GCN4  We discovered a transcription factor (Fil1) translationally induced by amino acid starvation in a 5' leader and Gcn2-dependent manner. Like Gcn4, Fil1 is required for the transcriptional response to amino acid starvation, and Gcn4 and Fil1 regulate similar genes. Despite their similarities in regulation, function, and targets, Fil1 and Gcn4 belong to different transcription factor families (GATA and b-ZIP, respectively). Thus, the same functions are performed by nonorthologous proteins under similar regulation. These results highlight the plasticity of transcriptional networks, which maintain conserved principles with nonconserved regulators.","doi":"10.1073/pnas.1713991115","authors":"Duncan CDS, Rodríguez-López M, Ruis P, Bähler J, Mata J","authors_abbrev":"Duncan CDS et al.","pubmed_publication_date":"20 Feb 2018","pubmed_entrez_date":"2018-02-13","publication_year":"2018","canto_session_key":"bf9cd1928a11ab87","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juan Mata","canto_first_approved_date":"2018-03-29 10:38:04","canto_approved_date":"2026-01-15 09:31:35","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-03-08 17:24:40","canto_added_date":"2018-02-14 01:15:14","annotation_curators":[{"name":"Juan Mata","community_curator":true,"annotation_count":3,"orcid":"0000-0002-5514-3653","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Juan Mata","file_curator_role":"community","annotation_file_curators":[{"name":"Juan Mata","community_curator":true,"annotation_count":30,"orcid":"0000-0002-5514-3653","file_type":"qualitative_gene_expression","file_name":"PMID_29432178_Duncan_Riboseq_qualitative_expression.txt"},{"name":"Juan Mata","community_curator":true,"annotation_count":579,"orcid":"0000-0002-5514-3653","file_type":"qualitative_gene_expression","file_name":"PMID_29432178_Duncan_RNAseq_qualitative_expression.txt"}],"genes":["SPBC776.05","SPAC13A11.05","SPAC9E9.03","SPBC1773.03c","SPAC15A10.04c","SPCC61.05","SPAC4G8.03c","SPCC965.04c","SPAC589.08c","SPCC24B10.03","SPCC757.04","SPCC338.18","SPBP16F5.04","SPCC584.16c","SPCC895.08c","SPAC22F3.09c","SPAC323.07c","SPBC29B5.02c","SPBC12C2.12c","SPAC11D3.18c","SPCC330.02","SPAC139.05","SPAC4H3.08","SPCC1620.08","SPCC18.09c","SPCC16A11.15c","SPAC3C7.05c","SPBC29A10.14","SPAC3C7.02c","SPAC23C4.05c","SPBC3B8.03","SPAC1687.16c","SPAC22F8.05","SPBC3E7.16c","SPAC3A11.10c","SPBC19C7.10","SPAC4H3.09","SPCC162.04c","SPBP8B7.04","SPAC513.05","SPAC343.06c","SPCC417.05c","SPAC186.03","SPBC660.05","SPAC19A8.15","SPAC167.06c","SPBC11B10.06","SPCC757.03c","SPAC26F1.14c","SPBC23E6.01c","SPAC1F8.01","SPAC3G6.05","SPBC23G7.06c","SPAPB1E7.04c","SPCC1020.14","SPCC757.11c","SPAC1F8.05","SPBC21H7.06c","SPCC63.14","SPBC1709.11c","SPAC22H12.03","SPCC594.04c","SPBC725.14","SPAC3G9.11c","SPAC630.04c","SPCP31B10.06","SPAC22E12.03c","SPAC630.07c","SPCC1322.08","SPAC1F3.10c","SPBC19C7.09c","SPBC725.03","SPAC6B12.13","SPBC18H10.05","SPAC1399.01c","SPAC17H9.06c","SPAC2E12.03c","SPBC29A3.03c","SPBC19C7.04c","SPBC19C2.11c","SPCC16A11.08","SPBC3E7.12c","SPAC750.05c","SPAC25A8.02","SPBP35G2.06c","SPAC5D6.07c","SPAC227.17c","SPAC56E4.03","SPBC16A3.02c","SPBC649.04","SPAC869.05c","SPBC6B1.05c","SPBC14C8.01c","SPAC2C4.09","SPAC15A10.05c","SPAC3F10.15c","SPBC1683.06c","SPAC2E1P3.03c","SPAC4A8.04","SPAC3G6.07","SPAC821.11","SPCC576.17c","SPCPB1C11.03","SPBC1289.17","SPCC1906.04","SPBC36B7.05c","SPAC22H12.05c","SPBC23G7.16","SPAC2C4.15c","SPBC16E9.16c","SPCC63.08c","SPBC800.14c","SPBC1683.08","SPBPB2B2.01","SPCC70.02c","SPCC1393.14","SPAC29B12.13","SPAP27G11.12","SPBC3B9.17","SPCC306.11","SPAC26F1.04c","SPAC19B12.10","SPAC607.09c","SPBC13G1.06c","SPBC30D10.16","SPBPB21E7.04c","SPAC14C4.01c","SPBC1105.14","SPBC646.13","SPCC1682.11c","SPAC20H4.08","SPAC1B3.21","SPAC2F3.08","SPBC1773.05c","SPCC1259.09c","SPAC13A11.04c","SPBPB2B2.13","SPCC645.03c","SPAC13D6.01","SPCC736.15","SPAC27E2.08","SPAC2E1P3.02c","SPBC1711.12","SPAC589.07c","SPCC1494.11c","SPAC6B12.03c","SPBC8E4.03","SPBC4B4.08","SPAC19A8.16","SPAC10F6.06","SPAC521.04c","SPAPB2B4.06","SPBC27.04","SPAC6G10.08","SPCC1739.15","SPAC11D3.01c","SPAC823.03","SPAC227.18","SPBC1105.19","SPBC1685.14c","SPCC777.13","SPBC713.14c","SPBC428.05c","SPAC328.08c","SPCC285.06c","SPCC1840.04","SPAC1B3.11c","SPAC1142.05","SPBPB21E7.07","SPBC1773.12","SPCC364.07","SPBC2G2.04c","SPCC191.06","SPBC1271.07c","SPCC320.05","SPBC215.08c","SPAP7G5.04c","SPAC26F1.11","SPBC1347.11","SPAC10F6.11c","SPAC10F6.13c","SPAC14C4.09","SPAC644.09","SPBC947.06c","SPBC56F2.09c","SPBC14F5.13c","SPBC215.05","SPAC1B3.06c","SPAC18G6.09c","SPAC24C9.08","SPAC1002.16c","SPAC22H12.01c","SPBC1685.13","SPBP35G2.16c","SPAPB1A11.03","SPCC24B10.16c","SPBC1E8.04","SPAC4G9.09c","SPAC637.13c","SPAC14C4.07","SPAC23C4.16c","SPCC1322.10","SPAPB1A11.01","SPAC31G5.18c","SPBC18A7.01","SPBC1271.05c","SPAC186.04c","SPCC191.01","SPCC1223.10c","SPAC5H10.06c","SPBPB21E7.09","SPBP26C9.03c","SPAC6B12.08","SPAP11E10.01","SPAC26A3.13c","SPBC27.05","SPCC162.06c","SPCC569.07","SPCC1183.09c","SPAC3F10.19","SPAC23C11.06c","SPAC139.02c","SPBC21C3.19","SPAC11D3.08c","SPBC106.10","SPAC4F10.16c","SPCC4F11.02","SPBC17D11.08","SPAC56E4.02c","SPCC1223.03c","SPBC460.02c","SPBC1709.12","SPCC965.12","SPCC306.10","SPAC6F12.03c","SPAC1002.09c","SPAC869.02c","SPAPB18E9.02c","SPAC2F3.16","SPAC16A10.04","SPBC1289.06c","SPBC713.02c","SPBC211.07c","SPAC2F7.06c","SPBC1683.03c","SPCC1739.04c","SPBP4H10.10","SPBC800.11","SPAC688.04c","SPBC1D7.05","SPAC22G7.11c","SPAC21E11.03c","SPBC16A3.17c","SPCC622.11","SPBC3H7.01","SPCC777.15","SPAC821.09","SPAC977.01","SPAC9E9.15","SPBC8E4.05c","SPCC285.05","SPBC1734.08","SPBC216.04c","SPAC6G10.06","SPBC1105.13c","SPAC1805.16c","SPCC569.03","SPAPJ691.02","SPAC19D5.09c","SPAC977.16c","SPAC1805.09c","SPAC1006.01","SPAC1F8.02c","SPAPB1A10.08","SPCC1840.07c","SPAC29B12.03","SPAC31G5.09c","SPBC215.11c","SPAC19B12.08","SPAC222.18","SPACUNK4.15","SPBC17G9.11c","SPCC4G3.03","SPAC4F8.10c","SPCC1442.09","SPAC1610.04","SPBC1348.12","SPCPB1C11.02","SPBC359.06","SPCC794.02","SPBC1271.08c","SPAC15E1.10","SPBC651.04","SPBC609.04","SPBC651.09c","SPAC16A10.05c","SPCC132.04c","SPAC23D3.12","SPAC22A12.17c","SPBC947.15c","SPAC3A11.06","SPAC1B3.20","SPAC3C7.13c","SPAC869.11","SPAPB24D3.08c","SPBC24C6.09c","SPBC83.05","SPAC11H11.01","SPBC19C2.05","SPAC144.09c","SPBC25B2.03","SPBC26H8.12","SPAC607.08c","SPBC19C2.04c","SPAC458.04c","SPAC6C3.04","SPAC57A10.09c","SPAC1F12.10c","SPAC13D1.01c","SPAC23D3.11","SPBC106.03","SPAC1F12.06c","SPAPB2B4.01c","SPCC191.09c","SPBC1198.13c","SPBPB2B2.02","SPAC1F12.07","SPBC11B10.02c","SPBPB21E7.01c","SPAC977.13c","SPBPB2B2.11","SPAC1B3.16c","SPCC18.01c","SPBC1773.13","SPCC1020.10","SPBPB8B6.03","SPCC1672.03c","SPBC1289.16c","SPAC25B8.09","SPAC5H10.02c","SPAPB8E5.04c","SPAC32A11.02c","SPCC285.09c","SPBPB2B2.12c","SPBC31F10.03","SPCC777.09c","SPBC106.13","SPAC1751.01c","SPBP4G3.02","SPBC418.01c","SPAP8A3.04c","SPAC22F8.11","SPAC9E9.13","SPAC140.01","SPAC17C9.06","SPAC1039.06","SPAC977.05c","SPBPB21E7.08","SPAC167.05","SPBC32F12.03c","SPBC29B5.01","SPBC1105.02c","SPBC23G7.11","SPBC1604.01","SPAC29B12.04","SPBC365.12c","SPAC1687.07","SPAC16E8.02","SPBC83.12","SPCC330.03c","SPAC17C9.12","SPBC1773.17c","SPCC576.04","SPAC13G7.05","SPAC29B12.11c","SPAC1142.07c","SPAC57A7.05","SPBC32H8.07","SPCC70.04c","SPAC9.04","SPAC26A3.14c","SPBC17D1.01","SPAC24B11.05","SPBPB2B2.10c","SPBC18E5.15","SPAC22H10.12c","SPAC20H4.11c","SPCC1235.11","SPBC9B6.02c","SPBC337.08c","SPBC119.10","SPBC36.12c","SPBC1778.10c","SPAC9G1.14","SPAC11D3.14c","SPBC2A9.02","SPAC6C3.03c","SPBC725.01","SPAC222.08c","SPBC428.10","SPBC1685.05","SPCC965.06","SPAC11D3.17","SPAC32A11.01","SPAC8C9.03","SPBC660.07","SPBC725.13c","SPBC106.02c","SPAC17C9.10","SPBC29A10.17","SPCC777.10c","SPCC663.02","SPCC1393.10","SPBC582.08","SPAPYUG7.03c","SPAC4H3.04c","SPAC3A12.08","SPAC1556.01c","SPAC343.12","SPAC56F8.15","SPCC1281.08","SPCC965.11c","SPAC10F6.16","SPAC19G12.16c","SPBC460.03","SPCC1020.09","SPBC543.04","SPAC2E1P3.05c","SPAC11D3.02c","SPAC15E1.02c","SPBPB2B2.06c","SPAPB2B4.02","SPAC688.03c","SPAC14C4.10c","SPBC1711.13","SPAC11D3.16c","SPAC25G10.01","SPAC4H3.03c","SPBC1348.02","SPAC26F1.02","SPBC428.02c","SPAPB15E9.03c","SPCC1281.04","SPBC19G7.18c","SPAC15A10.01","SPAC13C5.04","SPBC17D1.17","SPAC24B11.09","SPCC1840.12","SPCC757.07c","SPAC1782.12c","SPCC191.11","SPAC5H10.11","SPBC216.03","SPBC30B4.09","SPBC409.12c","SPCPB16A4.07","SPCC576.16c","SPCC70.12c","SPAC19A8.05c","SPBC19F5.04","SPAC20G8.10c","SPAC16A10.01","SPCC1742.01","SPAC17A5.11","SPBC16A3.18","SPCC285.07c","SPCC61.03","SPBP35G2.07","SPCC794.04c","SPCC569.01c","SPBC2F12.09c","SPCC1827.06c","SPBC11C11.06c","SPAC1783.06c","SPBC20F10.07","SPBC119.03","SPAC513.02","SPCC1393.12","SPAC22H10.13","SPCC1450.07c","SPBC1683.12","SPAC869.07c","SPAC6G9.16c","SPBC460.05","SPAC824.07","SPAC17C9.11c","SPBC1709.16c","SPCC1393.08","SPBC1198.14c","SPAC2G11.13","SPAC17G6.03","SPBC839.06","SPAC4G9.11c","SPAPJ760.03c","SPBC12D12.02c","SPBC1703.08c","SPAC6F6.12","SPBC56F2.06","SPBC32H8.02c","SPBC215.03c","SPAC12G12.12","SPCC70.10","SPAC630.05","SPAC57A10.08c","SPAC9G1.02","SPCPB16A4.06c","SPAC328.09","SPBC15D4.15","SPAC23H3.15c","SPAC144.13c","SPAC11E3.14","SPBPB21E7.11","SPCC285.11","SPBP35G2.12","SPBC660.06","SPAC328.03","SPAC11D3.09","SPCC330.01c","SPBC3B9.19","SPAC6G10.03c","SPAC5H10.10","SPBC1773.14","SPACUNK4.17","SPBC19G7.16","SPBC12C2.04","SPAC24C9.06c","SPAC29A4.17c","SPBC725.10","SPAC1952.09c","SPAC25H1.03","SPBC1773.02c","SPBPB2B2.15","SPBC409.23","SPAC4G8.10","SPAC13F5.03c","SPCC24B10.02c","SPAC1002.12c","SPCC11E10.01","SPCP1E11.05c","SPCC70.08c","SPBC713.07c","SPCC1223.12c","SPAC4F10.17","SPBC800.02","SPAC57A7.08","SPAC19G12.09","SPAC9E9.04","SPBC902.05c","SPAC56F8.14c","SPAPB24D3.04c","SPAC23C4.13","SPAC821.04c","SPAC14C4.02c","SPBC1711.11","SPCC1450.13c","SPBP8B7.28c","SPBC1348.06c","SPAC2F3.05c","SPAC6F6.11c","SPBC409.07c","SPBPB2B2.19c","SPBC405.04c","SPAC1B3.03c","SPCC306.05c","SPCC338.12","SPBPB8B6.02c","SPAC4D7.02c","SPBC2D10.05","SPAP27G11.16","SPBC609.01","SPAC23D3.17","SPCC777.17c","SPBC2G2.01c","SPAC977.18","SPCC1235.02","SPCC306.08c","SPAC20H4.02","SPAC19E9.03","SPBC56F2.15","SPBC106.08c","SPAC1687.14c","SPAC637.03","SPAC4G9.10","SPAC13G6.15c","SPAC167.08","SPBC36B7.09","SPAC16C9.01c","SPBP8B7.24c","SPAC19D5.01","SPBC409.10","SPAC1F3.09","SPAC21E11.04","SPACUNK4.10","SPAC17G8.06c","SPAC4F10.07c","SPCC320.06"],"gene_count":597,"ltp_gene_count":2,"approved_date":"2018-03-29"},{"uniquename":"PANTHER:PTHR46239","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.03c","HGNC:9820"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24687850","title":"H2A.Z-dependent regulation of cohesin dynamics on chromosome arms.","citation":"Mol Cell Biol 2014 Jun;34(11):2092-104","abstract":"Structural maintenance of chromosomes (SMC) complexes and DNA topoisomerases are major determinants of chromosome structure and dynamics. The cohesin complex embraces sister chromatids throughout interphase, but during mitosis most cohesin is stripped from chromosome arms by early prophase, while the remaining cohesin at kinetochores is cleaved at anaphase. This two-step removal of cohesin is required for sister chromatids to separate. The cohesin-related Smc5/6 complex has been studied mostly as a determinant of DNA repair via homologous recombination. However, chromosome segregation fails in Smc5/6 null mutants or cells treated with small interfering RNAs. This also occurs in Smc5/6 hypomorphs in the fission yeast Schizosaccharomyces pombe following genotoxic and replication stress, or topoisomerase II dysfunction, and these mitotic defects are due to the postanaphase retention of cohesin on chromosome arms. Here we show that mitotic and repair roles for Smc5/6 are genetically separable in S. pombe. Further, we identified the histone variant H2A.Z as a critical factor to modulate cohesin dynamics, and cells lacking H2A.Z suppress the mitotic defects conferred by Smc5/6 dysfunction. Together, H2A.Z and the SMC complexes ensure genome integrity through accurate chromosome segregation.","doi":"10.1128/MCB.00193-14","authors":"Tapia-Alveal C, Lin SJ, Yeoh A, Jabado OJ, O'Connell MJ","authors_abbrev":"Tapia-Alveal C et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-04-02","publication_year":"2014","canto_session_key":"5d1349babcbd0b5f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC5E4.06","SPBC342.06c","SPCC5E4.04","SPBC11B10.10c","SPAC1783.04c","SPCC550.05","SPBC8D2.04","SPAC11E3.04c","SPAC664.02c","SPAC11E3.01c","SPBC1A4.03c"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:24248599","title":"Regulation of Ras localization and cell transformation by evolutionarily conserved palmitoyltransferases.","citation":"Mol Cell Biol 2014 Feb;34(3):374-85","abstract":"Ras can act on the plasma membrane (PM) to mediate extracellular signaling and tumorigenesis. To identify key components controlling Ras PM localization, we performed an unbiased screen to seek Schizosaccharomyces pombe mutants with reduced PM Ras. Five mutants were found with mutations affecting the same gene, S. pombe erf2 (sp-erf2), encoding sp-Erf2, a palmitoyltransferase, with various activities. sp-Erf2 localizes to the trans-Golgi compartment, a process which is mediated by its third transmembrane domain and the Erf4 cofactor. In fission yeast, the human ortholog zDHHC9 rescues the phenotypes of sp-erf2 null cells. In contrast, expressing zDHHC14, another sp-Erf2-like human protein, did not rescue Ras1 mislocalization in these cells. Importantly, ZDHHC9 is widely overexpressed in cancers. Overexpressing ZDHHC9 promotes, while repressing it diminishes, Ras PM localization and transformation of mammalian cells. These data strongly demonstrate that sp-Erf2/zDHHC9 palmitoylates Ras proteins in a highly selective manner in the trans-Golgi compartment to facilitate PM targeting via the trans-Golgi network, a role that is most certainly critical for Ras-driven tumorigenesis.","doi":"10.1128/MCB.01248-13","authors":"Young E, Zheng ZY, Wilkins AD, Jeong HT, Li M, Lichtarge O, Chang EC","authors_abbrev":"Young E et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-11-20","publication_year":"2014","canto_session_key":"21e95d3288beff29","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26041456","title":"RPA prevents G-rich structure formation at lagging-strand telomeres to allow maintenance of chromosome ends.","citation":"EMBO J 2015 Jul 14;34(14):1942-58","abstract":"Replication protein A (RPA) is a highly conserved heterotrimeric single-stranded DNA-binding protein involved in DNA replication, recombination, and repair. In fission yeast, the Rpa1-D223Y mutation provokes telomere shortening. Here, we show that this mutation impairs lagging-strand telomere replication and leads to the accumulation of secondary structures and recruitment of the homologous recombination factor Rad52. The presence of these secondary DNA structures correlates with reduced association of shelterin subunits Pot1 and Ccq1 at telomeres. Strikingly, heterologous expression of the budding yeast Pif1 known to efficiently unwind G-quadruplex rescues all the telomeric defects of the D223Y cells. Furthermore, in vitro data show that the identical D to Y mutation in human RPA specifically affects its ability to bind G-quadruplex. We propose that RPA prevents the formation of G-quadruplex structures at lagging-strand telomeres to promote shelterin association and facilitate telomerase action at telomeres.","doi":"10.15252/embj.201490773","authors":"Audry J, Maestroni L, Delagoutte E, Gauthier T, Nakamura TM, Gachet Y, Saintomé C, Géli V, Coulon S","authors_abbrev":"Audry J et al.","pubmed_publication_date":"14 Jul 2015","pubmed_entrez_date":"2015-06-05","publication_year":"2015","canto_session_key":"e4b31ea722f9e274","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Stephane Coulon","canto_first_approved_date":"2015-08-28 14:21:22","canto_approved_date":"2024-12-21 12:18:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-19 13:27:57","canto_added_date":"2015-06-06 00:21:24","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Stephane Coulon","community_curator":true,"annotation_count":9,"orcid":"0000-0001-8090-914X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPAC2G11.12","SPAC30D11.10","SPAC644.14c","SPBC660.13c","SPAC26H5.06","SPCC188.07","SPAC3H5.06c","SPBC16D10.04c","SPBC887.14c"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2015-08-28"},{"uniquename":"PMID:17951524","title":"Schizosaccharomyces pombe Sst4p, a conserved Vps27/Hrs homolog, functions downstream of phosphatidylinositol 3-kinase Pik3p to mediate proper spore formation.","citation":"Eukaryot Cell 2007 Dec;6(12):2343-53","abstract":"Sporulation of the fission yeast Schizosaccharomyces pombe is a developmental process that generates gametes and that includes the formation of spore envelope precursors called the forespore membranes. Assembly and development of forespore membranes require vesicular trafficking from other intracellular membrane compartments. We have shown that phosphatidylinositol 3-kinase (PtdIns 3-kinase) is required for efficient and proper development of forespore membranes. The role of a FYVE domain protein, Sst4p, a homolog of Vps27p/Hrs, as a downstream factor for PtdIns 3-kinase in sporulation was investigated. sst4Delta asci formed spores with oval-shaped morphology and with reduced viability compared to that of the wild-type spores. The extension of forespore membranes was inefficient, and bubble-like structures emerged from the leading edges of the forespore membranes. Sst4p localization was examined using fluorescent protein fusions and was found to be adjacent to the forespore membranes during sporulation. The localization and function of Sst4p were dependent on its FYVE domain and on PtdIns 3-kinase. Sst4p colocalized and interacted with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM. Mutations in all three UIM domains of the Sst4p/Hse1p complex resulted in formation of spores with abnormal morphology. These results suggest that Sst4p is a downstream factor of PtdIns 3-kinase and functions in forespore membrane formation.","authors":"Onishi M, Iida M, Koga T, Yamada S, Hirata A, Iwaki T, Takegawa K, Fukui Y, Tachikawa H","authors_abbrev":"Onishi M et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-10-24","publication_year":"2007","canto_session_key":"5a17f9b473739de4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-27 14:20:29","canto_approved_date":"2019-11-26 18:55:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-26 18:52:07","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":48,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19A8.05c","SPBC1734.08","SPAC19B12.10","SPAC458.05","SPAC11H11.01","SPAC2G11.06","SPAC1142.07c","SPBC3E7.01","SPBC215.14c","SPAC1B3.07c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2017-09-27"},{"uniquename":"PMID:7672243","title":"The involvement of inositol lipids and phosphates in signalling in the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1995 May;23(2):223S","abstract":"","authors":"Stuart JA, Hughes PJ, Kirk CJ, Davey J, Michell RH","authors_abbrev":"Stuart JA et al.","pubmed_publication_date":"May 1995","pubmed_entrez_date":"1995-05-01","publication_year":"1995","canto_session_key":"72c2e89987736e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-09-21 13:34:48","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-09-21 13:33:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-09-21"},{"uniquename":"PMID:23422075","title":"The fission yeast Pvg1p has galactose-specific pyruvyltransferase activity.","citation":"FEBS Lett 2013 Apr 02;587(7):917-21","abstract":"N-Glycan from the fission yeast Schizosaccharomyces pombe contains outer-chain pyruvic acid 4,6-ketal-linked galactose (PvGal). Here, we characterized a putative S. pombe pyruvyltransferase, Pvg1p, reported to be essential for biosynthesis of PvGal. When p-nitrophenyl-β-Gal (pNP-β-Gal) was used as a substrate, the structure of the recombinant Pvg1p product was determined to be pNP-PvGal by one- and two-dimensional NMR spectroscopy. The recombinant Pvg1p transferred pyruvyl residues from phosphoenolpyruvate specifically to β-linked galactose.","doi":"10.1016/j.febslet.2013.02.016","authors":"Yoritsune K, Matsuzawa T, Ohashi T, Takegawa K","authors_abbrev":"Yoritsune K et al.","pubmed_publication_date":"02 Apr 2013","pubmed_entrez_date":"2013-02-21","publication_year":"2013","canto_session_key":"9b818e23e57cc278","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-07-20 15:53:18","canto_approved_date":"2020-01-17 19:01:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-09 08:26:07","canto_added_date":"2013-05-03 14:39:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1921.06c","SPAC8F11.10c","SPAC22F8.02c","SPAC27E2.07"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-07-20"},{"uniquename":"InterPro:IPR019166","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1442.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33723569","title":"Schizosaccharomyces pombe KAT5 contributes to resection and repair of a DNA double-strand break.","citation":"Genetics 2021 May 17;218(1)","abstract":"Chromatin remodeling is essential for effective repair of a DNA double-strand break (DSB). KAT5 (Schizosaccharomyces pombe Mst1, human TIP60) is a MYST family histone acetyltransferase conserved from yeast to humans that coordinates various DNA damage response activities at a DNA DSB, including histone remodeling and activation of the DNA damage checkpoint. In S. pombe, mutations in mst1+ causes sensitivity to DNA damaging drugs. Here we show that Mst1 is recruited to DSBs. Mutation of mst1+ disrupts recruitment of repair proteins and delays resection. These defects are partially rescued by deletion of pku70, which has been previously shown to antagonize repair by homologous recombination (HR). These phenotypes of mst1 are similar to pht1-4KR, a nonacetylatable form of histone variant H2A.Z, which has been proposed to affect resection. Our data suggest that Mst1 functions to direct repair of DSBs toward HR pathways by modulating resection at the DSB.","doi":"10.1093/genetics/iyab042","authors":"Li T, Petreaca RC, Forsburg SL","authors_abbrev":"Li T et al.","pubmed_publication_date":"17 May 2021","pubmed_entrez_date":"2021-03-16","publication_year":"2021","canto_session_key":"c57dbb2608ee460d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ting-ting Li","canto_first_approved_date":"2021-03-31 14:29:23","canto_approved_date":"2023-03-13 22:37:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-24 01:42:52","canto_added_date":"2021-03-18 01:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":30,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Ting-ting Li","community_curator":true,"annotation_count":28,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.10c","SPAC637.12c","SPCC1259.13","SPBC29A10.05","SPBC428.08c","SPBC342.05","SPBC216.05","SPCC126.02c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2021-03-31"},{"uniquename":"PMID:11416129","title":"Schizosaccharomyces pombe cells lacking the amino-terminal catalytic domains of DNA polymerase epsilon are viable but require the DNA damage checkpoint control.","citation":"Mol Cell Biol 2001 Jul;21(14):4495-504","abstract":"In Schizosaccharomyces pombe, the catalytic subunit of DNA polymerase epsilon (Pol epsilon) is encoded by cdc20(+) and is essential for chromosomal DNA replication. Here we demonstrate that the N-terminal half of Pol epsilon that includes the highly conserved polymerase and exonuclease domains is dispensable for cell viability, similar to observations made with regard to Saccharomyces cerevisiae. However, unlike budding yeast, we find that fission yeast cells lacking the N terminus of Pol epsilon (cdc20(DeltaN-term)) are hypersensitive to DNA-damaging agents and have a cell cycle delay. Moreover, the viability of cdc20(DeltaN-term) cells is dependent on expression of rad3(+), hus1(+), and chk1(+), three genes essential for the DNA damage checkpoint control. These data suggest that in the absence of the N terminus of Pol epsilon, cells accumulate DNA damage that must be repaired prior to mitosis. Our observation that S phase occurs more slowly for cdc20(DeltaN-term) cells suggests that DNA damage might result from defects in DNA synthesis. We hypothesize that the C-terminal half of Pol epsilon is required for assembly of the replicative complex at the onset of S phase. This unique and essential function of the C terminus is preserved in the absence of the N-terminal catalytic domains, suggesting that the C terminus can interact with and recruit other DNA polymerases to the site of initiation.","authors":"Feng W, D'Urso G","authors_abbrev":"Feng W et al.","pubmed_publication_date":"Jul 2001","pubmed_entrez_date":"2001-06-21","publication_year":"2001","canto_session_key":"e414534df48b7004","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-03-22 16:19:50","canto_approved_date":"2024-04-15 11:31:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-04 15:25:23","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC25H2.13c","SPBC336.04","SPBC216.05","SPCC1259.13","SPAC20G4.04c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-03-22"},{"uniquename":"PMID:22665798","title":"Induction of a G1-S checkpoint in fission yeast.","citation":"Proc Natl Acad Sci U S A 2012 Jun 19;109(25):9911-6","abstract":"Entry into S phase is carefully regulated and, in most organisms, under the control of a G(1)-S checkpoint. We have previously described a G(1)-S checkpoint in fission yeast that delays formation of the prereplicative complex at chromosomal replication origins after exposure to UV light (UVC). This checkpoint absolutely depends on the Gcn2 kinase. Here, we explore the signal for activation of the Gcn2-dependent G(1)-S checkpoint in fission yeast. If some form of DNA damage can activate the checkpoint, deficient DNA repair should affect the length of the checkpoint-induced delay. We find that the cell-cycle delay differs in repair-deficient mutants from that in wild-type cells. However, the duration of the delay depends not only on the repair capacity of the cells, but also on the nature of the repair deficiency. First, the delay is abolished in cells that are deficient in the early steps of repair. Second, the delay is prolonged in repair mutants that fail to complete repair after the incision stage. We conclude that the G(1)-S delay depends on damage to the DNA and that the activating signal derives not from the initial DNA damage, but from a repair intermediate(s). Surprisingly, we find that activation of Gcn2 does not depend on the processing of DNA damage and that activated Gcn2 alone is not sufficient to delay entry into S phase in UVC-irradiated cells. Thus, the G(1)-S delay depends on at least two different inputs.","doi":"10.1073/pnas.1204901109","authors":"Bøe CA, Krohn M, Rødland GE, Capiaghi C, Maillard O, Thoma F, Boye E, Grallert B","authors_abbrev":"Bøe CA et al.","pubmed_publication_date":"19 Jun 2012","pubmed_entrez_date":"2012-06-06","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC970.01","SPBC19C7.09c","SPBC3E7.08c","SPBC649.03"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:11901109","title":"UV irradiation causes the loss of viable mitotic recombinants in Schizosaccharomyces pombe cells lacking the G(2)/M DNA damage checkpoint.","citation":"Genetics 2002 Mar;160(3):891-908","abstract":"Elevated mitotic recombination and cell cycle delays are two of the cellular responses to UV-induced DNA damage. Cell cycle delays in response to DNA damage are mediated via checkpoint proteins. Two distinct DNA damage checkpoints have been characterized in Schizosaccharomyces pombe: an intra-S-phase checkpoint slows replication and a G(2)/M checkpoint stops cells passing from G(2) into mitosis. In this study we have sought to determine whether UV damage-induced mitotic intrachromosomal recombination relies on damage-induced cell cycle delays. The spontaneous and UV-induced recombination phenotypes were determined for checkpoint mutants lacking the intra-S and/or the G(2)/M checkpoint. Spontaneous mitotic recombinants are thought to arise due to endogenous DNA damage and/or intrinsic stalling of replication forks. Cells lacking only the intra-S checkpoint exhibited no UV-induced increase in the frequency of recombinants above spontaneous levels. Mutants lacking the G(2)/M checkpoint exhibited a novel phenotype; following UV irradiation the recombinant frequency fell below the frequency of spontaneous recombinants. This implies that, as well as UV-induced recombinants, spontaneous recombinants are also lost in G(2)/M mutants after UV irradiation. Therefore, as well as lack of time for DNA repair, loss of spontaneous and damage-induced recombinants also contributes to cell death in UV-irradiated G(2)/M checkpoint mutants.","authors":"Osman F, Tsaneva IR, Whitby MC, Doe CL","authors_abbrev":"Osman F et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-20","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12589755","title":"The fission yeast spSet1p is a histone H3-K4 methyltransferase that functions in telomere maintenance and DNA repair in an ATM kinase Rad3-dependent pathway.","citation":"J Mol Biol 2003 Feb 28;326(4):1081-94","abstract":"We have characterized spSet1p, the Schizosaccharomyces pombe ortholog of the budding yeast histone H3 methyltransferase Set1p. SpSet1p catalyzes methylation of H3 at K4, in vivo and in vitro. Deleting spset1 partially affects telomeric and centromeric silencing. Strikingly, lack of spSet1p causes elongation of telomeres in wild-type cells and in most DNA damage checkpoint rad mutant cells, but not in cells lacking the ATM kinase Rad3 or its associated protein Rad26. Interestingly, spset1 deletion specifically causes a reduction in sensitivity to ultraviolet radiation of the PCNA-like checkpoint mutants hus1 and rad1, but not of cells devoid of Rad3. This partial suppression was not due to restoration of checkpoint function or to transcriptional induction of DNA repair genes. Moreover, spset1 allows recovery specifically of the crb2 checkpoint mutant upon treatment with the replication inhibitor hydroxyurea but not upon UV irradiation. Nevertheless, the pathway induced in spset1 cells cannot substitute for the Mus81/Rqh1 DNA damage tolerance pathway. Our results suggest that SpSet1p and the ATM kinase Rad3 function in a common genetic pathway linking chromatin to telomere length regulation and DNA repair.","authors":"Kanoh J, Francesconi S, Collura A, Schramke V, Ishikawa F, Baldacci G, Géli V","authors_abbrev":"Kanoh J et al.","pubmed_publication_date":"28 Feb 2003","pubmed_entrez_date":"2003-02-19","publication_year":"2003","canto_session_key":"9340627d98142a43","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-06-18 14:31:34","canto_approved_date":"2026-02-09 09:59:31","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-12-23 15:01:49","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":35,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC594.05c","SPAC14C4.13","SPAC1834.04","SPBC342.05","SPAC2G11.12","SPCC18B5.11c","SPAC57A10.02","SPAC664.07c","SPAC1952.07","SPAC20G4.04c","SPCC306.04c","SPCC23B6.03c","SPBC216.05","SPCC1259.13","SPAC9E9.08","SPBC18H10.06c","SPBC25D12.04","SPAC644.14c","SPBC8D2.04","SPBC1105.11c","SPBC336.04","SPAC6B12.10c","SPCC4G3.05c"],"gene_count":23,"ltp_gene_count":21,"approved_date":"2018-06-18"},{"uniquename":"PMID:31089172","title":"Kinesin-6 Klp9 plays motor-dependent and -independent roles in collaboration with Kinesin-5 Cut7 and the microtubule crosslinker Ase1 in fission yeast.","citation":"Sci Rep 2019 May 14;9(1):7336","abstract":"Bipolar mitotic spindles play a critical part in accurate chromosome segregation. During late mitosis, spindle microtubules undergo drastic elongation in a process called anaphase B. Two kinesin motors, Kinesin-5 and Kinesin-6, are thought to generate outward forces to drive spindle elongation, and the microtubule crosslinker Ase1/PRC1 maintains structural integrity of antiparallel microtubules. However, how these three proteins orchestrate this process remains unknown. Here we explore the functional interplay among fission yeast Kinesin-5/Cut7, Kinesin-6/Klp9 and Ase1. Using total internal reflection fluorescence microscopy, we show that Klp9 forms homotetramers and that Klp9 is a processive plus end-directed motor. klp9Δase1Δ is synthetically lethal. Surprisingly, this lethality is not ascribable to the defective motor activity of Klp9; instead, it is dependent upon a nuclear localisation signal and coiled coil domains within the non-motor region. We isolated a cut7 mutant (cut7-122) that displays temperature sensitivity only in the absence of Klp9. Interestingly, cut7-122 alone is impaired in spindle elongation during anaphase B, and furthermore, cut7-122klp9Δ double mutants exhibit additive defects. We propose that Klp9 plays dual roles during anaphase B; one is motor-dependent that collaborates with Cut7 in force generation, while the other is motor-independent that ensures structural integrity of spindle microtubules together with Ase1.","doi":"10.1038/s41598-019-43774-7","authors":"Yukawa M, Okazaki M, Teratani Y, Furuta K, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"14 May 2019","pubmed_entrez_date":"2019-05-16","publication_year":"2019","canto_session_key":"c4f2687cd9a265cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-06-12 17:18:40","canto_approved_date":"2021-11-23 18:16:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-04 20:33:37","canto_added_date":"2019-05-17 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":58,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A11.14c","SPAC25G10.07c","SPBC15D4.01c","SPAPB1A10.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-06-12"},{"uniquename":"PMID:17482430","title":"Multiple fungal enzymes possess cysteine synthase activity in vitro.","citation":"Res Microbiol 2007 Jun;158(5):428-36","abstract":"We present evidence that there are at least three Aspergillus nidulans enzymes which catalyze in vitro the reaction of O-acetylserine (OAS) with sulfide forming cysteine. This activity is shared by cysteine synthase (CS) encoded by the cysB gene, homocysteine synthase encoded by cysD and by at least one more enzyme. Moreover, arginine, histidine or proline starvation leads to derepression of CS activity even in the cysB,cysD double mutant strains, while neither cysB nor cysD gene transcription is derepressed by amino acid starvation. Using a cpcA mutant, we show that starvation-inducible CS activity is under control of cross-pathway regulation. We identify CysF as a putative CS in A. nidulans. However, cysF gene transcription is not elevated by amino acid starvation. Therefore, it seems that there exists yet another enzyme, thus far unidentified, which possesses CS activity. Using mutants impaired during various steps of cysteine synthesis we prove that the cysB-encoded enzyme is the only CS of physiological importance in the studied fungus. Similar results were obtained with Schizosaccharomyces pombe mutant strains impaired in cysteine synthesis, indicating that the presence of multiple enzymes with in vitro CS activity may be a common feature of many fungal species.","authors":"Brzywczy J, Natorff R, Sieńko M, Paszewski A","authors_abbrev":"Brzywczy J et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-05-08","publication_year":"2007","canto_session_key":"7b60de39ffb9d91d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-11-13 16:08:24","canto_approved_date":"2026-02-12 11:42:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-08 15:10:01","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.11","SPBC1A4.02c","SPAC3A12.17c","SPBC106.17c","SPBC36.04"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2013-11-13"},{"uniquename":"PMID:25650245","title":"The spatial and temporal organization of origin firing during the S-phase of fission yeast.","citation":"Genome Res 2015 Mar;25(3):391-401","abstract":"Eukaryotes duplicate their genomes using multiple replication origins, but the organization of origin firing along chromosomes and during S-phase is not well understood. Using fission yeast, we report the first genome-wide analysis of the spatial and temporal organization of replication origin firing, analyzed using single DNA molecules that can approach the full length of chromosomes. At S-phase onset, origins fire randomly and sparsely throughout the chromosomes. Later in S-phase, clusters of fired origins appear embedded in the sparser regions, which form the basis of nuclear replication foci. The formation of clusters requires proper histone methylation and acetylation, and their locations are not inherited between cell cycles. The rate of origin firing increases gradually, peaking just before mid S-phase. Toward the end of S-phase, nearly all the available origins within the unreplicated regions are fired, contributing to the timely completion of genome replication. We propose that the majority of origins do not fire as a part of a deterministic program. Instead, origin firing, both individually and as clusters, should be viewed as being mostly stochastic.","doi":"10.1101/gr.180372.114","authors":"Kaykov A, Nurse P","authors_abbrev":"Kaykov A et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-02-05","publication_year":"2015","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2015-02-06 01:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39527213","title":"Automated Machine Learning Tools to Build Regression Models for Schizosaccharomyces pombe Omics Data.","citation":"Methods Mol Biol 2025;2862:353-361","abstract":"Machine learning is a powerful tool for analyzing biological data and making useful predictions. The surge of biological data from high-throughput omics technologies has raised the need for modeling approaches capable of tackling such amounts of data, which is pivotal to understanding the nature of complex molecular systems. Here, we show how to construct a simple model using automated machine learning (AutoML) to predict protein abundance in Schizosaccharomyces pombe, using data obtained from codon usage bias and quantitative proteomics.","doi":"10.1007/978-1-0716-4168-2_25","authors":"de Moura Ferreira MA, da Silveira WB","authors_abbrev":"de Moura Ferreira MA et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7749319","title":"Checkpoints in the cell cycle of fission yeast.","citation":"Curr Opin Genet Dev 1995 Feb;5(1):12-6","abstract":"When cell cycle progression in fission yeast is disrupted, checkpoint controls ensure that the normal sequence of cell cycle events is maintained. Activation of a checkpoint relies on monitoring signals that might involve assembly of macromolecular structures essential for specific cell cycle processes. The past year has seen further elucidation of two new checkpoints operating during the cell cycle of Schizosaccharomyces pombe. One involves the product of the rum1 gene and prevents cells from entering mitosis from the pre-Start G1 interval. The second checkpoint operates during the later stages of the cell cycle and is essential for coupling the events of mitosis and cell division.","authors":"D'Urso G, Nurse P","authors_abbrev":"D'Urso G et al.","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19034698","title":"Enhanced production of coenzyme Q10 by overexpressing HMG-CoA reductase and induction with arachidonic acid in Schizosaccharomyces pombe.","citation":"Appl Biochem Biotechnol 2010 Jan;160(2):523-31","abstract":"Coenzyme Q10 (CoQ10) is a vitamin-like substance which plays a crucial role in the respiratory chain ranging from bacteria to humans and in the radical scavenging in human body. In this study, the full-length hmgR gene (encoding 3-hydroxy-3-methyl-glutaryl-CoA reductase, HMG-CoA reductase) was cloned and overexpressed in Schizosaccharomyces pombe. Using the pREPG yeast depressed under the thiamine as the control, CoQ10 contents increased up to 2.68 and 3.09 times when recombinant cells were incubated without and with arachidonic acid, respectively. It demonstrated that arachidonic acid could upregulate the activity of HMG-CoA reductase and that hmgR gene played a significant role in CoQ10 biosynthesis. So, it has an importance to be utilized for fermentation.","doi":"10.1007/s12010-008-8386-x","authors":"Cheng B, Yuan QP, Sun XX, Li WJ","authors_abbrev":"Cheng B et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2008-11-27","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29343513","title":"Using genetic buffering relationships identified in fission yeast to reveal susceptibilities in cells lacking hamartin or tuberin function.","citation":"Biol Open 2018 Jan 17;7(1)","abstract":"Tuberous sclerosis complex is an autosomal dominant disorder characterized by benign tumors arising from the abnormal activation of mTOR signaling in cells lacking TSC1 (hamartin) or TSC2 (tuberin) activity. To expand the genetic framework surrounding this group of growth regulators, we utilized the model eukaryote  Schizosaccharomyces pombe  to uncover and characterize genes that buffer the phenotypic effects of mutations in the orthologous  tsc1  or  tsc2  loci. Our study identified two genes:  fft3  (encoding a DNA helicase) and  ypa1  (encoding a peptidyle-prolyl cis/trans isomerase). While the deletion of  fft3  or  ypa1  has little effect in wild-type fission yeast cells, their loss in  tsc1Δ  or  tsc2Δ  backgrounds results in severe growth inhibition. These data suggest that the inhibition of Ypa1p or Fft3p might represent an 'Achilles' heel' of cells defective in hamartin/tuberin function. Furthermore, we demonstrate that the interaction between  tsc1 / tsc2  and  ypa1  can be rescued through treatment with the mTOR inhibitor, torin-1, and that  ypa1Δ  cells are resistant to the glycolytic inhibitor, 2-deoxyglucose. This identifies  ypa1  as a novel upstream regulator of mTOR and suggests that the effects of  ypa1  loss, together with mTOR activation, combine to result in a cellular maladaptation in energy metabolism that is profoundly inhibitory to growth.","doi":"10.1242/bio.031302","authors":"Rayhan A, Faller A, Chevalier R, Mattice A, Karagiannis J","authors_abbrev":"Rayhan A et al.","pubmed_publication_date":"17 Jan 2018","pubmed_entrez_date":"2018-01-19","publication_year":"2018","canto_session_key":"4091fbf0f3d80884","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-01-20 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.04","SPAC22F3.13","SPAC630.13c","SPAC25A8.01c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:24291754","title":"Growth phenotype screening of Schizosaccharomyces pombe using a Lensless microscope.","citation":"Biosens Bioelectron 2014 Apr 15;54:345-50","abstract":"The Lensless microscope has a large field of view and allows the capture of the diffraction pattern from a large number of cells simultaneously. A simple algorithm to measure intensity changes in the Airy Disc First Fringe (ADFF) has been derived to follow the growth characteristics of the unicellular yeast Schizosaccharomyces pombe. The performance of the algorithm is calibrated using comparison between optical image and ADFF analysis of polystyrene microspheres with known dimensions and has an accuracy of 5% over all lengths above the diffraction-limited measurements. We have observed the growth characteristics of S. pombe for N=100 cells to determine the growth phenotype distributions of Length (L(t=0)) and width (W(t=0)) on arrival at the surface, lag phase adjustment to the new growth conditions (B), the length at birth, LB, and cell cycle length, tcell. The observed cell width distribution has a median width of 3.9 (±0.1) µm, as expected, but a non-normal distribution. Similarly, all growth parameters studied, L(t=0), LB and cell cycle time are phenotypes with non-normal distributions but with medians consistent with the literature values.","doi":"10.1016/j.bios.2013.11.010","authors":"Penwill LA, Batten GE, Castagnetti S, Shaw AM","authors_abbrev":"Penwill LA et al.","pubmed_publication_date":"15 Apr 2014","pubmed_entrez_date":"2013-12-03","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8824229","title":"Schizosaccharomyces pombe produces novel pyruvate-containing N-linked oligosaccharides.","citation":"J Biol Chem 1996 Oct 18;271(42):25945-9","abstract":"The large N-linked oligosaccharides released by endo-beta-N-acetylglucosaminidase H from Schizosaccharomyces pombe glycoproteins were analyzed for the presence of noncarbohydrate functional groups. No phosphate, sulfate, or acetate could be detected; however, approximately six molecules of pyruvic acid/molecule were found on 98% of the oligosaccharides. Pyruvate moieties were acetal (ketal)-linked to galactose residues in the R configuration to carbons 4 and 6. This is the first report of pyruvate functional groups being attached to N-linked oligosaccharides in yeast and appears only to be the second documentation of this sugar modification in eukaryotes.","authors":"Gemmill TR, Trimble RB","authors_abbrev":"Gemmill TR et al.","pubmed_publication_date":"18 Oct 1996","pubmed_entrez_date":"1996-10-18","publication_year":"1996","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2843820","title":"Construction of an expression vector for the fission yeast Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1988 Sep 12;16(17):8603-17","abstract":"We have isolated and characterized a S. pombe promoter using a functional heterologous gene product assay. Random S. pombe genomic fragments were cloned upstream from the promoterless 'lacZ gene and tested in vivo for their efficiency to promote expression of the beta-galactosidase protein in the fission yeast. An efficient S. pombe promoter called 54/1 was isolated and shown to drive up to 5% of total protein synthesis as beta-galactosidase. The structure and nucleotide sequence of this promoter were determined, precise localization of its mRNA transcriptional start points established. Translational fusion of the Pseudomonas putida XylE gene with the 54/1 gene was shown to allow expression of catechol oxidase activity in S. pombe. An expression vector suitable for transcriptional fusions was then constructed from engineered 54/1 promoter sequences and used to drive expression of the E. coli Tn5 ble gene, thus confering resistance to the fission yeast against bleomycin and phleomycin antibiotics.","authors":"Kudla B, Persuy MA, Gaillardin C, Heslot H","authors_abbrev":"Kudla B et al.","pubmed_publication_date":"12 Sep 1988","pubmed_entrez_date":"1988-09-12","publication_year":"1988","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28947618","title":"Sde2 is an intron-specific pre-mRNA splicing regulator activated by ubiquitin-like processing.","citation":"EMBO J 2018 Jan 04;37(1):89-101","abstract":"The expression of intron-containing genes in eukaryotes requires generation of protein-coding messenger RNAs (mRNAs) via RNA splicing, whereby the spliceosome removes non-coding introns from pre-mRNAs and joins exons. Spliceosomes must ensure accurate removal of highly diverse introns. We show that Sde2 is a ubiquitin-fold-containing splicing regulator that supports splicing of selected pre-mRNAs in an intron-specific manner in  Schizosaccharomyces pombe  Both fission yeast and human Sde2 are translated as inactive precursor proteins harbouring the ubiquitin-fold domain linked through an invariant GGKGG motif to a C-terminal domain (referred to as Sde2-C). Precursor processing after the first di-glycine motif by the ubiquitin-specific proteases Ubp5 and Ubp15 generates a short-lived activated Sde2-C fragment with an N-terminal lysine residue, which subsequently gets incorporated into spliceosomes. Absence of Sde2 or defects in Sde2 activation both result in inefficient excision of selected introns from a subset of pre-mRNAs. Sde2 facilitates spliceosomal association of Cactin/Cay1, with a functional link between Sde2 and Cactin further supported by genetic interactions and pre-mRNA splicing assays. These findings suggest that ubiquitin-like processing of Sde2 into a short-lived activated form may function as a checkpoint to ensure proper splicing of certain pre-mRNAs in fission yeast.","doi":"10.15252/embj.201796751","authors":"Thakran P, Pandit PA, Datta S, Kolathur KK, Pleiss JA, Mishra SK","authors_abbrev":"Thakran P et al.","pubmed_publication_date":"04 Jan 2018","pubmed_entrez_date":"2017-09-27","publication_year":"2018","canto_session_key":"6115bf31740b991f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shravan Mishra","canto_first_approved_date":"2018-01-08 18:59:57","canto_approved_date":"2025-12-23 12:42:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-09 13:00:40","canto_added_date":"2017-09-29 00:15:14","annotation_curators":[{"name":"Shravan Mishra","community_curator":true,"annotation_count":158,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17D4.01","SPBC4B4.05","SPAPB2B4.05","SPAP8A3.06","SPAC9.13c","SPBC2A9.09","SPBC646.02","SPAPJ698.03c","SPAC6F6.15","SPAC2C4.03c","SPAC212.06c","SPBC1711.17","SPBC31F10.11c","SPBC28F2.04c","SPBC21C3.05","SPBC4B4.07c","SPBC20F10.09","SPBP22H7.07","SPAC22A12.09c","SPBC28E12.03","SPBCPT2R1.08c","SPAC1F3.09","SPAC29E6.02","SPCC1795.08c","SPBC24C6.11","SPAC29A4.08c","SPAC212.11","SPAC222.18","SPBC8D2.09c","SPBC2G2.13c","SPBC16E9.15","SPAC17A5.16","SPAC4A8.09c","SPBP16F5.02","SPCC16A11.13","SPAC16A10.03c","SPCC550.02c","SPCC188.08c","SPBC3E7.14","SPCC16C4.12","SPBC3E7.13c","SPAC9.03c","SPBC4B4.10c","SPAC1420.01c","SPAC3A12.11c","SPBC32F12.05c","SPBC9B6.05c","SPBC1A4.01","SPAC22F8.10c","SPBC428.06c","SPAC29E6.08","SPAC31G5.18c","SPBC6B1.10","SPBC36.09","SPAC23A1.09","SPAC1782.10c","SPBC887.05c","SPCC594.07c","SPAP27G11.13c","SPAC644.12","SPCC1259.09c","SPBC1861.08c","SPAC23H3.02c","SPAC20H4.09","SPBC365.05c","SPCC1620.01c","SPCC126.02c","SPAC1786.01c","SPAC20H4.06c","SPAC15A10.11","SPBC4B4.09","SPBP35G2.09","SPAC227.16c","SPCC1259.15c","SPAC23D3.08","SPBC19C2.01","SPBC839.10","SPAC16.02c","SPCC10H11.01","SPBC25H2.16c","SPBC1289.11","SPCC1620.10","SPBC354.07c","SPAC10F6.02c","SPBC215.12","SPAC4D7.13","SPBC2F12.12c","SPBC119.13c","SPCC18B5.06","SPAC19A8.13","SPAC31G5.01","SPCP1E11.07c","SPBC11C11.08","SPBC29A3.07c","SPBC13E7.01","SPAC1952.06c","SPCC1235.09","SPBC336.13c","SPBC18H10.10c","SPAC27D7.07c","SPAC29A4.06c","SPCC364.02c","SPBC1861.04c","SPCC1223.10c","SPBC3B9.02c","SPBC6B1.07","SPAC26A3.08","SPBC11G11.06c","SPBC31E1.03","SPAC27F1.09c","SPBC146.07","SPCC188.11","SPAP8A3.09c","SPAC22H10.03c","SPBC1289.12","SPBC19C2.14","SPBC211.02c","SPBC660.16","SPAC607.03c","SPBC1778.02","SPCC1840.10","SPAC30D11.09","SPCC285.12","SPCC962.06c","SPCC1682.12c","SPBC146.05c","SPBC20F10.01","SPBC713.02c","SPAC4F8.12c","SPAC4G8.11c","SPCC1795.04c","SPBC337.06c"],"gene_count":132,"ltp_gene_count":70,"approved_date":"2018-01-08"},{"uniquename":"PANTHER:PTHR20996","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC902.03","HGNC:26759"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"Pfam:PF10341","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YIL009C-A","SPAC6F6.16c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:41844616","title":"Phosphoregulation of the novel hemi-arrestin MAPK scaffold Sms1 prevents untimely mating.","citation":"Nat Commun 2026 Mar 17;","abstract":"Mitogen-activated protein kinases (MAPK) are ancestral kinases that form essential signalling cascades. However, scaffolds that recruit kinases to subcellular locations and promote signal transduction have only been described in a few species. Notably, no scaffold was thought necessary for the MAPK cascade promoting sexual differentiation in fission yeast. Here, we identify the hemi-arrestin protein Sms1 as a novel scaffold of this MAPK cascade. Interactions with PIP2 and the pheromone receptor-coupled Gα subunit target Sms1 to plasma membrane patches, where it assembles the active cascade by binding each MAP kinase. These interactions are essential for signal transduction and local signal interpretation for polarised growth. Phosphorylation, including by the MAPK itself, antagonises Sms1 membrane translocation, establishing a negative feedback that underlies polarity patch turnover and prevents untimely mating attempts. Thus, Sms1 is a MAPK scaffold with canonical functions despite its distinct structural fold, highlighting convergent evolution of MAPK scaffolds across eukaryotes.","doi":"10.1038/s41467-026-70631-9","authors":"Sieber B, Merlini L, Li W, Besomi M, Michon L, Gordon-Lennox S, Martin SG","authors_abbrev":"Sieber B et al.","pubmed_publication_date":"17 Mar 2026","pubmed_entrez_date":"2026-03-18","publication_year":"2026","canto_session_key":"a592ac840145179f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Boris Sieber","canto_first_approved_date":"2026-04-11 07:59:00","canto_approved_date":"2026-06-09 08:07:58","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-04-15 09:55:10","canto_added_date":"2026-03-19 00:25:05","annotation_curators":[{"name":"Boris Sieber","community_curator":true,"annotation_count":72,"orcid":"0000-0002-8145-3364","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1442.01","SPAC1D4.13","SPAC17H9.09c","SPAC22H10.07","SPBC16G5.01","SPBC2F12.14c","SPAC17C9.10","SPBC16H5.06","SPAC19G12.14","SPAC31G5.09c","SPAC4F10.10c","SPBC11B10.09","SPCC1682.01","SPAC869.10c","SPAC23E2.03c","SPAC8E11.02c","SPBC24C6.06","SPAC13G7.02c","SPCC613.10","SPBC1D7.05","SPBC15D4.08c","SPCC1235.02","SPCC1795.11","SPAC17A2.02c","SPBC354.14c","SPAC139.02c","SPAC1565.04c","SPBC4B4.05","SPBC1861.05","SPCC18.06c"],"gene_count":30,"ltp_gene_count":29,"approved_date":"2026-04-11"},{"uniquename":"PMID:36476849","title":"Chromosome arm length, and a species-specific determinant, define chromosome arm width.","citation":"Cell Rep 2022 Dec 06;41(10):111753","abstract":"Mitotic chromosomes in different organisms adopt various dimensions. What defines these dimensions is scarcely understood. Here, we compare mitotic chromosomes in budding and fission yeasts harboring similarly sized genomes distributed among 16 or 3 chromosomes, respectively. Hi-C analyses and superresolution microscopy reveal that budding yeast chromosomes are characterized by shorter-ranging mitotic chromatin contacts and are thinner compared with the thicker fission yeast chromosomes that contain longer-ranging mitotic contacts. These distinctions persist even after budding yeast chromosomes are fused to form three fission-yeast-length entities, revealing a species-specific organizing principle. Species-specific widths correlate with the known binding site intervals of the chromosomal condensin complex. Unexpectedly, within each species, we find that longer chromosome arms are always thicker and harbor longer-ranging contacts, a trend that we also observe with human chromosomes. Arm length as a chromosome width determinant informs mitotic chromosome formation models.","doi":"10.1016/j.celrep.2022.111753","authors":"Kakui Y, Barrington C, Kusano Y, Thadani R, Fallesen T, Hirota T, Uhlmann F","authors_abbrev":"Kakui Y et al.","pubmed_publication_date":"06 Dec 2022","pubmed_entrez_date":"2022-12-08","publication_year":"2022","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2022-12-09 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33796794","title":"Increased expression of Polδ does not alter the canonical replication program  in vivo .","citation":"Wellcome Open Res 2021;6:44","abstract":" Background:   In vitro  experiments utilising the reconstituted  Saccharomyces cerevisiae  eukaryotic replisome indicated that the efficiency of the leading strand replication is impaired by a moderate increase in Polδ concentration. It was hypothesised that the slower rate of the leading strand synthesis characteristic for reactions containing two-fold and four-fold increased concentration of Polδ represented a consequence of a relatively rare event, during which Polδ stochastically outcompeted Polε and, in an inefficient manner, temporarily facilitated extension of the leading strand. Inspired by this observation, we aimed to determine whether similarly increased Polδ levels influence replication dynamics  in vivo  using the fission yeast  Schizosaccharomyces pombe  as a model system.  Methods:  To generate  S. pombe  strains over-expressing Polδ, we utilised Cre-Lox mediated cassette exchange and integrated one or three extra genomic copies of all four Polδ genes. To estimate expression of respective Polδ genes in Polδ-overexpressing mutants, we measured relative transcript levels of  cdc1  +   ,  cdc6  +   (or  cdc6  L591G   ),  cdc27  +   and  cdm1  +   by reverse transcription followed by quantitative PCR (RT-qPCR). To assess the impact of Polδ over-expression on cell physiology and replication dynamics, we used standard cell biology techniques and polymerase usage sequencing.  Results:  We provide an evidence that two-fold and four-fold over-production of Polδ does not significantly alter growth rate, cellular morphology and S-phase duration. Polymerase usage sequencing analysis further indicates that increased Polδ expression does not change activities of Polδ, Polε and Polα at replication initiation sites and across replication termination zones. Additionally, we show that mutants over-expressing Polδ preserve WT-like distribution of replication origin efficiencies.  Conclusions:  Our experiments do not disprove the existence of opportunistic polymerase switches; however, the data indicate that, if stochastic replacement of Polε for Polδ does occur i  n vivo , it represents a rare phenomenon that does not significantly influence canonical replication program.","doi":"10.12688/wellcomeopenres.16600.2","authors":"Zach R, Carr AM","authors_abbrev":"Zach R et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-05-11","publication_year":"2021","canto_session_key":"b5089e77a1ba9a37","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tony Carr","canto_first_approved_date":"2021-05-19 15:27:45","canto_approved_date":"2024-05-02 08:15:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-11 16:52:22","canto_added_date":"2021-04-07 00:15:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tony Carr","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.02c","SPBC336.04","SPAC27E2.05","SPBC12D12.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2021-05-19"},{"uniquename":"PMID:9251040","title":"Genetic and physiological analysis of DNA replication in fission yeast.","citation":"Methods Enzymol 1997;283:440-59","abstract":"Studies on DNA replication in S. pombe have provided powerful insights into the way in which the genome of this model eukaryote is replicated and how the replication process is controlled. These studies have been facilitated by the simplicity and range of methods available in this organism for physiological and genetic analysis of DNA replication mutants. In the future, continued focus on the analysis of such mutants, coupled with increasingly sophisticated biochemical investigation of the processes of DNA replication in both wild-type and mutant cells, will ensure continued rapid progress in this area.","authors":"MacNeill SA, Fantes PA","authors_abbrev":"MacNeill SA et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27889481","title":"Mitotic Nuclear Envelope Breakdown and Spindle Nucleation Are Controlled by Interphase Contacts between Centromeres and the Nuclear Envelope.","citation":"Dev Cell 2016 Dec 05;39(5):544-559","abstract":"Faithful genome propagation requires coordination between nuclear envelope (NE) breakdown, spindle formation, and chromosomal events. The conserved linker of nucleoskeleton and cytoskeleton (LINC) complex connects fission yeast centromeres and the centrosome, across the NE, during interphase. During meiosis, LINC connects the centrosome with telomeres rather than centromeres. We previously showed that loss of telomere-LINC contacts compromises meiotic spindle formation. Here, we define the precise events regulated by telomere-LINC contacts and address the analogous possibility that centromeres regulate mitotic spindle formation. We develop conditionally inactivated LINC complexes in which the conserved SUN-domain protein Sad1 remains stable but severs interphase centromere-LINC contacts. Strikingly, the loss of such contacts abolishes spindle formation. We pinpoint the defect to a failure in the partial NE breakdown required for centrosome insertion into the NE, a step analogous to mammalian NE breakdown. Thus, interphase chromosome-LINC contacts constitute a cell-cycle control device linking nucleoplasmic and cytoplasmic events.","doi":"10.1016/j.devcel.2016.10.021","authors":"Fernández-Álvarez A, Bez C, O'Toole ET, Morphew M, Cooper JP","authors_abbrev":"Fernández-Álvarez A et al.","pubmed_publication_date":"05 Dec 2016","pubmed_entrez_date":"2016-11-28","publication_year":"2016","canto_session_key":"9079e758e75e287f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-10-22 14:18:05","canto_approved_date":"2021-06-18 15:58:26","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-10-11 15:53:01","canto_added_date":"2016-11-29 01:15:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.15","SPAC14C4.05c","SPBC244.01c","SPAC1687.20c","SPAC18G6.10","SPBC1778.02","SPBC12D12.01","SPAC1786.03","SPAC6G9.06c","SPBC2G2.14","SPAC6G9.13c","SPAC16A10.07c","SPCC736.11"],"gene_count":13,"ltp_gene_count":6,"approved_date":"2020-10-22"},{"uniquename":"PMID:29891649","title":"All-atom simulations disentangle the functional dynamics underlying gene maturation in the intron lariat spliceosome.","citation":"Proc Natl Acad Sci U S A 2018 Jun 26;115(26):6584-6589","abstract":"The spliceosome (SPL) is a majestic macromolecular machinery composed of five small nuclear RNAs and hundreds of proteins. SPL removes noncoding introns from precursor messenger RNAs (pre-mRNAs) and ligates coding exons, giving rise to functional mRNAs. Building on the first SPL structure solved at near-atomic-level resolution, here we elucidate the functional dynamics of the intron lariat spliceosome (ILS) complex through multi-microsecond-long molecular-dynamics simulations of ∼1,000,000 atoms models. The ILS essential dynamics unveils ( i ) the leading role of the Spp42 protein, which heads the gene maturation by tuning the motions of distinct SPL components, and ( ii ) the critical participation of the Cwf19 protein in displacing the intron lariat/U2 branch helix. These findings provide unprecedented details on the SPL functional dynamics, thus contributing to move a step forward toward a thorough understanding of eukaryotic pre-mRNA splicing.","doi":"10.1073/pnas.1802963115","authors":"Casalino L, Palermo G, Spinello A, Rothlisberger U, Magistrato A","authors_abbrev":"Casalino L et al.","pubmed_publication_date":"26 Jun 2018","pubmed_entrez_date":"2018-06-13","publication_year":"2018","canto_session_key":"fe0328bd6000b3d8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-09-09 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11694582","title":"pkl1(+)and klp2(+): Two kinesins of the Kar3 subfamily in fission yeast perform different functions in both mitosis and meiosis.","citation":"Mol Biol Cell 2001 Nov;12(11):3476-88","abstract":"We have identified Klp2p, a new kinesin-like protein (KLP) of the KAR3 subfamily in fission yeast. The motor domain of this protein is 61% identical and 71% similar to Pkl1p, another fission yeast KAR3 protein, yet the two enzymes are different in behavior and function. Pkl1p is nuclear throughout the cell cycle, whereas Klp2p is cytoplasmic during interphase. During mitosis Klp2p enters the nucleus where it forms about six chromatin-associated dots. In metaphase-arrested cells these migrate back and forth across the nucleus. During early anaphase they segregate with the chromosomes into two sets of about three, fade, and are replaced by other dots that form on the spindle interzone. Neither klp2(+) nor pkl1(+) is essential, and the double deletion is also wild type for both vegetative and sexual reproduction. Each deletion rescues different alleles of cut7(ts), a KLP that contributes to spindle formation and elongation. When either or both deletions are combined with a dynein deletion, vegetative growth is normal, but sexual reproduction fails: klp2 Delta,dhc1-d1 in karyogamy, pkl1 Delta,dhc1-d1 in multiple phases of meiosis, and the triple deletion in both. Deletion of Klp2p elongates a metaphase-arrested spindle, but pkl1 Delta shortens it. The anaphase spindle of klp2 Delta becomes longer than the cell, leading it to curl around the cell's ends. Apparently, Klp2p promotes spindle disassembly and contributes to the behavior of mitotic chromosomes.","authors":"Troxell CL, Sweezy MA, West RR, Reed KD, Carson BD, Pidoux AL, Cande WZ, McIntosh JR","authors_abbrev":"Troxell CL et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2001-11-06","publication_year":"2001","canto_session_key":"cf85ace105b7712e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-11 21:17:59","canto_approved_date":"2022-05-12 10:37:58","canto_session_submitted_date":"2014-11-28 11:23:39","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC649.05","SPAC25G10.07c","SPAC3A11.14c","SPAC1786.03","SPAC1093.06c","SPAC664.10"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-10-11"},{"uniquename":"PMID:29917077","title":"USMG5 Ashkenazi Jewish founder mutation impairs mitochondrial complex V dimerization and ATP synthesis.","citation":"Hum Mol Genet 2018 Oct 01;27(19):3305-3312","abstract":"Leigh syndrome is a frequent, heterogeneous pediatric presentation of mitochondrial oxidative phosphorylation (OXPHOS) disease, manifesting with psychomotor retardation and necrotizing lesions in brain deep gray matter. OXPHOS occurs at the inner mitochondrial membrane through the integrated activity of five protein complexes, of which complex V (CV) functions in a dimeric form to directly generate adenosine triphosphate (ATP). Mutations in several different structural CV subunits cause Leigh syndrome; however, dimerization defects have not been associated with human disease. We report four Leigh syndrome subjects from three unrelated Ashkenazi Jewish families harboring a homozygous splice-site mutation (c.87 + 1G>C) in a novel CV subunit disease gene, USMG5. The Ashkenazi population allele frequency is 0.57%. This mutation produces two USMG5 transcripts, wild-type and lacking exon 3. Fibroblasts from two Leigh syndrome probands had reduced wild-type USMG5 mRNA expression and undetectable protein. The mutation did not alter monomeric CV expression, but reduced both CV dimer expression and ATP synthesis rate. Rescue with wild-type USMG5 cDNA in proband fibroblasts restored USMG5 protein, increased CV dimerization and enhanced ATP production rate. These data demonstrate that a recurrent USMG5 splice-site founder mutation in the Ashkenazi Jewish population causes autosomal recessive Leigh syndrome by reduction of CV dimerization and ATP synthesis.","doi":"10.1093/hmg/ddy231","authors":"Barca E, Ganetzky RD, Potluri P, Juanola-Falgarona M, Gai X, Li D, Jalas C, Hirsch Y, Emmanuele V, Tadesse S, Ziosi M, Akman HO, Chung WK, Tanji K, McCormick EM, Place E, Consugar M, Pierce EA, Hakonarson H, Wallace DC, Hirano M, Falk MJ","authors_abbrev":"Barca E et al.","pubmed_publication_date":"01 Oct 2018","pubmed_entrez_date":"2018-06-20","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25H1.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:14730319","title":"The conserved kinetochore protein shugoshin protects centromeric cohesion during meiosis.","citation":"Nature 2004 Feb 05;427(6974):510-7","abstract":"Meiosis comprises a pair of specialized nuclear divisions that produce haploid germ cells. To accomplish this, sister chromatids must segregate together during the first meiotic division (meiosis I), which requires that sister chromatid cohesion persists at centromeres. The factors that protect centromeric cohesion during meiosis I have remained elusive. Here we identify Sgo1 (shugoshin), a protector of the centromeric cohesin Rec8 in fission yeast. We also identify a homologue of Sgo1 in budding yeast. We provide evidence that shugoshin is widely conserved among eukaryotes. Moreover, we identify Sgo2, a paralogue of shugoshin in fission yeast, which is required for faithful mitotic chromosome segregation. Localization of Sgo1 and Sgo2 at centromeres requires the kinase Bub1, identifying shugoshin as a crucial target for the kinetochore function of Bub1. These findings provide insights into the evolution of meiosis and kinetochore regulation during mitosis and meiosis.","authors":"Kitajima TS, Kawashima SA, Watanabe Y","authors_abbrev":"Kitajima TS et al.","pubmed_publication_date":"05 Feb 2004","pubmed_entrez_date":"2004-01-20","publication_year":"2004","canto_session_key":"66a8c83f6f122a84","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-02-25 16:06:19","canto_approved_date":"2026-04-20 14:36:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-16 15:41:01","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.12c","SPBC29A10.14","SPBP35G2.03c","SPAC664.01c","SPAC15A10.15"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2021-02-25"},{"uniquename":"EMBL:AU010125","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2437396","title":"Effect of inhibition of central angiotensin pressor mechanisms on blood pressure in spontaneously hypertensive rats.","citation":"J Cardiovasc Pharmacol 1987 Mar;9(3):298-304","abstract":"The present experiments were designed to elucidate the role of central angiotensin II (AII) mechanisms in maintenance of established hypertension in adult spontaneously hypertensive rats (SHR) by determining the blood pressure response to chronic intraventricular (i.v.t.) infusion of the converting enzyme inhibitor teprotide or the AII receptor antagonist 1sar,8Thr-AII (sarthran). Male SHR (240-300 g) were given chronic indwelling arterial and venous catheters and bilateral lateral cerebral ventricular cannulae. The acute pressor responses to successive intravenous infusions of AII (sarthran experiments) or angiotensin I (AI; teprotide experiments) and to an intraventricular bolus injection of AII or AI were determined in the conscious rats. A 5-day intraventricular infusion of sarthran (1 or 6 micrograms/h) or teprotide (10 micrograms/h) in isotonic saline was maintained by subcutaneously implanted osmotic minipumps, and pressor responses were retested on the 5th day of intraventricular infusion. Five-day intraventricular sarthran infusion at 1 and 6 micrograms/h reduced the pressor response to intraventricular AII by 48 and 74%, respectively, while intraventricular teprotide (10 micrograms/h) inhibited the pressor response to intraventricular AI by 25%. None of the intraventricular infusions significantly decreased pressor responsiveness to intravenous AII or AI. In separate groups of SHR, tail-cuff blood pressure was monitored before, during, and after a 1-week intraventricular teprotide infusion (10 micrograms/h) or successive intraventricular infusions of sarthran at 1 microgram/h for 2 weeks followed by 6 micrograms/h for 1 week. Neither chronic intraventricular sarthran or teprotide caused a significant lowering of blood pressure in SHR.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Bruner CA, Kuslikis BI, Fink GD","authors_abbrev":"Bruner CA et al.","pubmed_publication_date":"Mar 1987","pubmed_entrez_date":"1987-03-01","publication_year":"1987","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C11.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32981237","title":"Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.","citation":"FEBS Open Bio 2020 Nov;10(11):2437-2451","abstract":"Fungal α-mannosidase Ams1 and its mammalian homolog MAN2C1 hydrolyze terminal α-linked mannoses in free oligosaccharides released from misfolded glycoproteins or lipid-linked oligosaccharide donors. Ams1 is transported by selective autophagy into vacuoles. Here, we determine the tetrameric structure of Ams1 from the fission yeast Schizosaccharomyces pombe at 3.2 Å resolution by cryo-electron microscopy. Distinct from a low resolution structure of S. cerevisiae Ams1, S. pombe Ams1 has a prominent N-terminal tail that mediates tetramerization and an extra β-sheet domain. Ams1 shares a conserved active site with other enzymes in glycoside hydrolase family 38, to which Ams1 belongs, but contains extra N-terminal domains involved in tetramerization. The atomic structure of Ams1 reported here will aid understanding of its enzymatic activity and transport mechanism.","doi":"10.1002/2211-5463.12988","authors":"Zhang J, Wang YY, Du LL, Ye K","authors_abbrev":"Zhang J et al.","pubmed_publication_date":"Nov 2020","pubmed_entrez_date":"2020-09-27","publication_year":"2020","canto_session_key":"b695daefeda7685b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-11-05 14:09:23","canto_approved_date":"2020-11-05 14:09:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-05 14:09:10","canto_added_date":"2020-09-30 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC513.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-11-05","pdb_entries":[{"pdb_id":"6lz1","gene_chains":[{"gene_uniquename":"SPAC513.05","chain":"A/B/C/D","position":"1-1077"}],"title":"Structure of S.pombe alpha-mannosidase Ams1","entry_authors":"Zhang J,Ye K","entry_authors_abbrev":"Zhang J et al.","reference_uniquename":"PMID:32981237","experimental_method":"EM","resolution":"3.2"}]},{"uniquename":"PMID:39527204","title":"Targeted Forward Genetics: Saturating Mutational Analyses of Specific Target Loci Within the Genome.","citation":"Methods Mol Biol 2025;2862:223-239","abstract":"Precise allele replacement by homologous recombination (also known as \"gene targeting\" or \"genome editing\") allows scientists to engineer altered DNA sequences, insertions, or deletions at specific locations in the genome. Such reverse genetics provides powerful tools to elucidate the structure and function of regulatory DNA elements, genes, RNAs, and proteins within their natural, endogenous context. Here, we describe in detail the methodology for Targeted Forward Genetics (TFG), which supports population-scale, saturating screens of allele replacements spanning thousands of base pairs at a specific target locus in the genome. The overall approach and detailed protocols, developed for the fission yeast Schizosaccharomyces pombe, are extensible to other organisms in which gene targeting is feasible.","doi":"10.1007/978-1-0716-4168-2_16","authors":"Protacio RU, Wahls WP","authors_abbrev":"Protacio RU et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC330.05c","SPCC1322.13"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:34028542","title":"TORC2 inhibition of α-arrestin Aly3 mediates cell surface persistence of S. pombe Ght5 glucose transporter in low glucose.","citation":"J Cell Sci 2021 May 15;134(10)","abstract":"In the fission yeast, Schizosaccharomyces pombe, the high-affinity hexose transporter, Ght5, must be transcriptionally upregulated and localized to the cell surface for cell division under limited glucose. Although cell-surface localization of Ght5 depends on Target of rapamycin complex 2 (TORC2), the molecular mechanisms by which TORC2 ensures proper localization of Ght5 remain unknown. We performed genetic screening for gene mutations that restore Ght5 localization on the cell surface in TORC2-deficient mutant cells, and identified a gene encoding an uncharacterized α-arrestin-like protein, Aly3/SPCC584.15c. α-arrestins are thought to recruit a ubiquitin ligase to membrane-associated proteins. Consistently, Ght5 is ubiquitylated in TORC2-deficient cells, and this ubiquitylation is dependent on Aly3. TORC2 supposedly enables cell-surface localization of Ght5 by preventing Aly3-dependent ubiquitylation and subsequent ubiquitylation-dependent translocation of Ght5 to vacuoles. Surprisingly, nitrogen starvation, but not glucose depletion, triggers Aly3-dependent transport of Ght5 to vacuoles in S. pombe, unlike budding yeast hexose transporters, vacuolar transport of which is initiated upon changes in hexose concentration. This study provides new insights into the molecular mechanisms controlling the subcellular localization of hexose transporters in response to extracellular stimuli.","doi":"10.1242/jcs.257485","authors":"Toyoda Y, Soejima S, Masuda F, Saitoh S","authors_abbrev":"Toyoda Y et al.","pubmed_publication_date":"15 May 2021","pubmed_entrez_date":"2021-05-24","publication_year":"2021","canto_session_key":"155dba22ce11dc4f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yusuke Toyoda","canto_first_approved_date":"2021-06-28 12:33:40","canto_approved_date":"2026-04-27 09:39:44","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-06-25 03:19:40","canto_added_date":"2021-05-26 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yusuke Toyoda","community_curator":true,"annotation_count":37,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11H11.01","SPBC2D10.04","SPAC19A8.05c","SPBC839.02","SPCC4B3.16","SPAC1B3.05","SPBC16H5.12c","SPBC337.13c","SPCC584.15c","SPAC630.13c","SPBC4B4.06","SPAC23H3.03c","SPBC30D10.10c","SPAC22F3.13","SPCC4G3.15c","SPCC1235.14","SPAC823.03","SPBC1734.08","SPAC4G8.05","SPAC630.07c","SPAC3H1.10","SPCC23B6.01c","SPAC31A2.12","SPCC24B10.07","SPBP35G2.14","SPAC17G6.05c","SPAC1296.01c","SPBC3D6.06c"],"gene_count":28,"ltp_gene_count":28,"approved_date":"2021-06-28"},{"uniquename":"PMID:33909078","title":"Substrate specificities of α1,2- and α1,3-galactosyltransferases and characterization of Gmh1p and Otg1p in Schizosaccharomyces pombe.","citation":"Glycobiology 2021 Sep 09;31(8):1037-1045","abstract":"In the fission yeast Schizosaccharomyces pombe, α1,2- and α1,3-linked D-galactose (Gal) residues are transferred to N- and O-linked oligosaccharides of glycoproteins by galactosyltransferases. Although the galactomannans are important for cell-cell communication in S. pombe (e.g., in nonsexual aggregation), the mechanisms underlying galactosylation in cells remain unclear. Schizosaccharomyces pombe has 10 galactosyltransferase-related genes: seven belonging to glycosyltransferase (GT) family 34 and three belonging GT family 8. Disruption of all 10 α-galactosyltransferases (strain Δ10GalT) has been shown to result in a complete lack of α-Gal residues. Here, we have investigated the function and substrate specificities of galactosyltransferases in S pombe by using strains expressing single α-galactosyltransferases in the Δ10GalT background. High-performance liquid chromatography (HPLC) analysis of pyridylaminated O-linked oligosaccharides showed that two GT family 34 α1,2-galactosyltransferases (Gma12p and Gmh6p) and two GT family 8 α1,3-galactosyltransferases (Otg2p and Otg3p) are involved in galactosylation of O-linked oligosaccharide. Moreover, 1H-NMR of N-glycans revealed that three GT family 34 α1,2-galactosyltransferases (Gmh1p, Gmh2p and Gmh3p) are required for the galactosylation of N-linked oligosaccharides. Furthermore, HPLC and lectin-blot analysis revealed that Otg1p showed α1,3-galactosyltransferase activity under conditions of co-expression with Gmh6p, indicating that α-1,2-linked galactose is required for the galactosylation activity of Otg1p in S. pombe. In conclusion, eight galactosyltransferases have been shown to have activity in S. pombe with different substrate specificities. These findings will be useful for genetically tailoring the galactosylation of both N- and O-glycans in fission yeast.","doi":"10.1093/glycob/cwab028","authors":"Fukunaga T, Tanaka N, Furumoto T, Nakakita S, Ohashi T, Higuchi Y, Maekawa H, Takegawa K","authors_abbrev":"Fukunaga T et al.","pubmed_publication_date":"09 Sep 2021","pubmed_entrez_date":"2021-04-28","publication_year":"2021","canto_session_key":"d6e965719f1ee102","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2021-05-19 08:56:53","canto_approved_date":"2025-10-07 06:58:58","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-05-11 00:56:38","canto_added_date":"2021-04-30 00:15:04","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.06c","SPBC4C3.09","SPAC5H10.11","SPBC1289.13c","SPAC5H10.13c","SPAC5H10.12c","SPBC8D2.17","SPAC637.06","SPCC736.04c","SPBC4C3.08"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2021-05-19"},{"uniquename":"PMID:9468529","title":"Purification and characterization of phosphatidylglycerolphosphate synthase from Schizosaccharomyces pombe.","citation":"J Biol Chem 1998 Feb 20;273(8):4681-8","abstract":"The enzyme CDP-diacylglycerol:sn-glycerol-3-phosphate 3-phosphatidyltransferase (phosphatidylglycerolphosphate synthase; PGPS4; EC 2.7.8.5) is located in the mitochondrial inner membrane and catalyzes the committed step in the cardiolipin branch of phospholipid synthesis. Previous studies revealed that PGPS is the most highly regulated enzyme in cardiolipin biosynthesis in both Saccharomyces cerevisiae and Schizosaccharomyces pombe. In this work, we report the purification to homogeneity of PGPS from S. pombe. The enzyme was solubilized from the mitochondrial membrane of S. pombe with Triton X-100. The solubilized enzyme, together with the associated detergent and intrinsic lipids, had a molecular mass of 120 kDa, as determined by gel filtration. The enzyme was further purified using salt-induced phase separation, gel filtration, and ionic exchange, hydroxylapatite, and affinity chromatographies. The procedure yielded a homogeneous protein preparation, evidenced by both SDS-polyacrylamide gel electrophoresis (PAGE) and agarose isoelectric focusing under nondenaturing conditions. The purified enzyme had an apparent molecular mass of 60 kDa as determined by SDS-PAGE. The enzyme showed a strong dependence on lipid cofactors for activity in vitro. While both phosphatidic acid and CDP-diacylglycerol appeared to be activators, the most significant activation was observed with cardiolipin. The possible physiological significance of the lipid cofactor effect is discussed. This is the first purification of a eucaryotic PGPS enzyme to date, and the first purification of a phospholipid biosynthetic enzyme from S. pombe.","authors":"Jiang F, Kelly BL, Hagopian K, Greenberg ML","authors_abbrev":"Jiang F et al.","pubmed_publication_date":"20 Feb 1998","pubmed_entrez_date":"1998-03-21","publication_year":"1998","canto_session_key":"33f9124906c1e55e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-28 14:29:28","canto_approved_date":"2020-01-17 19:46:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-22 10:41:40","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP18G5.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-06-28"},{"uniquename":"PMID:33533152","title":"Functional interaction between ELL transcription elongation factor and Epe1 reveals the role of Epe1 in the regulation of transcription outside heterochromatin.","citation":"Mol Microbiol 2021 Jul;116(1):80-96","abstract":"Eleven-nineteen lysine-rich leukemia (ELL) is a eukaryotic RNA polymerase II transcription elongation factor. In Schizosaccharomyces pombe, it is important for survival under genotoxic stress conditions. However, the molecular basis underlying this function of ELL in S. pombe is yet to be deciphered. Here, we carried out a genetic screen to identify multicopy suppressor(s) that could restore normal growth of ell1 deletion mutant in the presence of DNA damaging agent. Sequence analysis of the identified suppressors revealed the anti-silencing protein, Epe1, as one of the suppressors of ell1 deletion associated genotoxic stress sensitivity. Our results further demonstrate that the overexpression of Epe1 could suppress all other phenotypes associated with the absence of Ell1. Moreover, transcriptional defect of ell1Δ strain could also be alleviated by the overexpression of Epe1. Epe1 also showed a physical interaction with Ell1. Interestingly, we also observed that the region of Epe1 encompassing 403-948 amino acids was indispensable for all the above functions. Furthermore, our results show that the overexpression of Epe1 causes increased H3K9 acetylation and RNA polymerase II recruitment. Taken together, our results show a functional interaction between Epe1 and Ell1, and this function is independent of the well-known JmjC and N-terminal transcriptional activation domains of Epe1 in S. pombe.","doi":"10.1111/mmi.14691","authors":"Sweta K, Sharma N","authors_abbrev":"Sweta K et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-02-03","publication_year":"2021","canto_session_key":"8fbfc2228b1d145e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kumari Sweta","canto_first_approved_date":"2025-01-06 18:17:36","canto_approved_date":"2025-01-06 18:17:36","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-01-05 01:59:55","canto_added_date":"2021-02-05 01:15:06","annotation_curators":[{"name":"Kumari Sweta","community_curator":true,"annotation_count":1,"orcid":"0000-0003-4118-3870","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":45,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.09","SPCC622.16c","SPAPJ760.03c","SPBP23A10.14c","SPAC1952.05"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2025-01-06"},{"uniquename":"PMID:26749213","title":"The AP-2 complex is required for proper temporal and spatial dynamics of endocytic patches in fission yeast.","citation":"Mol Microbiol 2016 May;100(3):409-24","abstract":"In metazoans the AP-2 complex has a well-defined role in clathrin-mediated endocytosis. By contrast, its direct role in endocytosis in unicellular eukaryotes has been questioned. Here, we report co- immunoprecipitation between the fission yeast AP-2 component Apl3p and clathrin, as well as the genetic interactions between apl3Δ and clc1 and sla2Δ/end4Δ mutants. Furthermore, a double clc1 apl3Δ mutant was found to be defective in FM4-64 uptake. In an otherwise wild-type strain, apl3Δ cells exhibit altered dynamics of the endocytic sites, with a heterogeneous and extended lifetime of early and late markers at the patches. Additionally, around 50% of the endocytic patches exhibit abnormal spatial dynamics, with immobile patches and patches that bounce backwards to the cell surface, showing a pervasive effect of the absence of AP-2. These alterations in the endocytic machinery result in abnormal cell wall synthesis and morphogenesis. Our results complement those found in budding yeast and confirm that a direct role of AP-2 in endocytosis has been conserved throughout evolution.","doi":"10.1111/mmi.13327","authors":"de León N, Hoya M, Curto MA, Moro S, Yanguas F, Doncel C, Valdivieso MH","authors_abbrev":"de León N et al.","pubmed_publication_date":"May 2016","pubmed_entrez_date":"2016-01-11","publication_year":"2016","canto_session_key":"d5e1616053c30a60","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Henar Valdivieso","canto_approved_date":"2016-07-14 14:43:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-06 12:10:27","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[{"name":"Henar Valdivieso","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC9B6.08","SPBC2G2.06c","SPBC691.03c","SPBP4G3.02","SPBC19G7.05c","SPAC19G12.10c","SPAC31A2.09c","SPAC688.11","SPCC1840.02c"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2016-07-06"},{"uniquename":"PMID:1773660","title":"Structure of the fission yeast centromere cen3: direct analysis of the reiterated inverted region.","citation":"Chromosoma 1991 Dec;101(4):214-21","abstract":"We determined the structure of the Schizosaccharomyces pombe centromere cen3 using direct genomic mapping and cosmid walking. The repetitive region of cen3 is approximately 110 kb, much longer than that of the previously determined cen1 and cen2 regions. The approximately 30 kb long left and approximately 60 kb right repetitive sequences are arranged with an inverted symmetry and flank the 15 approximately 20 kb central domain. The repeat motifs in cen3, although they consist of the common centromeric repeat elements, are slightly different from those in cen1 and cen2. The cen3 repeat motifs appear to be reiterated four times in the left and nine times in the right side repetitive regions. We found that the central domain consists of the common approximately 5 kb core sequence associated with the pair of innermost inverted sequences, most of which are reiterated only twice in the genome. Although their sizes differ significantly, the general features of cen1, cen2 and cen3 are similar, and a prototype, consensus structure for the fission yeast centromere may be deduced.","authors":"Murakami S, Matsumoto T, Niwa O, Yanagida M","authors_abbrev":"Murakami S et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"4b432583d49b96b9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 19:01:21","canto_approved_date":"2018-12-22 19:01:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 19:01:13","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:30886144","title":"Network-based prediction of protein interactions.","citation":"Nat Commun 2019 Mar 18;10(1):1240","abstract":"Despite exceptional experimental efforts to map out the human interactome, the continued data incompleteness limits our ability to understand the molecular roots of human disease. Computational tools offer a promising alternative, helping identify biologically significant, yet unmapped protein-protein interactions (PPIs). While link prediction methods connect proteins on the basis of biological or network-based similarity, interacting proteins are not necessarily similar and similar proteins do not necessarily interact. Here, we offer structural and evolutionary evidence that proteins interact not if they are similar to each other, but if one of them is similar to the other's partners. This approach, that mathematically relies on network paths of length three (L3), significantly outperforms all existing link prediction methods. Given its high accuracy, we show that L3 can offer mechanistic insights into disease mechanisms and can complement future experimental efforts to complete the human interactome.","doi":"10.1038/s41467-019-09177-y","authors":"Kovács IA, Luck K, Spirohn K, Wang Y, Pollis C, Schlabach S, Bian W, Kim DK, Kishore N, Hao T, Calderwood MA, Vidal M, Barabási AL","authors_abbrev":"Kovács IA et al.","pubmed_publication_date":"18 Mar 2019","pubmed_entrez_date":"2019-03-20","publication_year":"2019","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2019-04-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3322810","title":"p13suc1 acts in the fission yeast cell division cycle as a component of the p34cdc2 protein kinase.","citation":"EMBO J 1987 Nov;6(11):3507-14","abstract":"cdc2+ encodes a protein kinase that is required during both G1 and G2 phases of the cell division cycle in fission yeast. suc1+ is an essential gene that was originally identified as a plasmid-borne sequence that could rescue certain temperature-sensitive cdc2 mutants. To investigate the role of the suc1+ gene product in the cell cycle p13suc1 has been expressed in Escherichia coli and purified. An immunoaffinity purified anti-p13suc1 polyclonal serum has been prepared and used to identify p13suc1 in fission yeast. The abundance of this protein did not alter either during the cell cycle or during entry into stationary phase. p13suc1 was found in yeast lysates in a complex with the cdc2+ gene product. Approximately 5% of cellular p34cdc2 was associated with p13suc1, and this fraction of p34cdc2 was active as a protein kinase. The stability of the complex was disrupted in yeast strains carrying temperature-sensitive alleles of cdc2 that are suppressible by overexpression of suc1+. The level of association between p13suc1 and p34cdc2 was not affected by cell cycle arrest in adverse nutritional conditions. p13suc1 is not a substrate of the p34cdc2 protein kinase. We propose instead that it acts as a regulatory component of p34cdc2 that facilitates interaction with other proteins.","authors":"Brizuela L, Draetta G, Beach D","authors_abbrev":"Brizuela L et al.","pubmed_publication_date":"Nov 1987","pubmed_entrez_date":"1987-11-01","publication_year":"1987","canto_session_key":"082c31c224ee26b3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-05 15:08:19","canto_approved_date":"2021-10-15 12:51:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-14 15:53:46","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC1734.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-07-05"},{"uniquename":"PMID:19486165","title":"Pleiotropic phenotypes caused by an opal nonsense mutation in an essential gene encoding HMG-CoA reductase in fission yeast.","citation":"Genes Cells 2009 Jun;14(6):759-71","abstract":"Schizosaccharomyces pombe genome contains an essential gene hmg1(+) encoding the sterol biosynthetic enzyme, 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR). Here, we isolated an allele of the hmg1(+) gene, hmg1-1/its12, as a mutant that showed sensitivities to high temperature and to FK506, a calcineurin inhibitor. The hmg1-1 allele contained an opal nonsense mutation in its N-terminal transmembrane domain, yet in spite of the mutation a full-length protein was produced, suggesting a read-through termination codon. Consistently, overexpression of the hmg1-1 mutant gene suppressed the mutant phenotypes. The hmg1-1 mutant showed hypersensitivity to pravastatin, an HMGR inhibitor, suggesting a defective HMGR activity. The mutant treated with FK506 caused dramatic morphological changes and showed defects in cell wall integrity, as well as displayed synthetic growth phenotypes with the mutant alleles of genes involved in cytokinesis and cell wall integrity. The mutant exhibited different phenotypes from those of the disruption mutants of ergosterol biosynthesis genes, and it showed normal filipin staining as well as showed normal subcellular localization of small GTPases. These data suggest that the pleiotropic phenotypes reflect the integrated effects of the reduced availability of ergosterol and various intermediates of the mevalonate pathway.","doi":"10.1111/j.1365-2443.2009.01308.x","authors":"Fang Y, Imagawa K, Zhou X, Kita A, Sugiura R, Jaiseng W, Kuno T","authors_abbrev":"Fang Y et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-06-03","publication_year":"2009","canto_session_key":"9665521870dab722","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-10-31 22:01:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-31 14:13:38","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.14c","SPBC12D12.04c","SPBC36.06c","SPAC13G6.11c","SPCC162.09c","SPCC1739.11c","SPAC16.01","SPAC19A8.04","SPAC20G4.07c","SPBC15C4.03","SPAC18G6.03","SPAC1687.16c","SPBP4H10.04","SPBC27B12.03c","SPBC21.06c"],"gene_count":15,"ltp_gene_count":14,"approved_date":"2016-10-31"},{"uniquename":"PMID:10816255","title":"Microtubule and actin-dependent movement of the formin cdc12p in fission yeast.","citation":"Microsc Res Tech 2000 Apr 15;49(2):161-7","abstract":"Although a number of gene products involved in cytokinesis have been identified, still little is known about how these proteins are localized to the proper site and assembled into a ring structure. How is the plane of cell division is positioned in the cell? Schizosaccharomyces pombe are simple rod-shaped eukaryotic cells that divide by medial fission using a medial contractile ring. S. pombe cdc12p encodes a member of the formin gene family, proteins with conserved roles in cytokinesis and actin organization. cdc12p is required specifically for the formation of the medial ring and is located in this ring during mitosis. Time-lapse microscopy of cells expressing GFP-cdc12p protein fusions reveals that during interphase, S. pombe cdc12p is present in a discrete, motile cytoplasmic particle that moves using both actin and microtubules. At the onset of mitosis, the spot moves to the future site of cell division and spreads out into a ring. These studies demonstrate that a cytokinesis factor may travel on both microtubule and actin networks to the site of contractile ring assembly. These findings suggest a potential mechanism for how the mitotic spindle positions the cell division plane in animal cells.","authors":"Chang F","authors_abbrev":"Chang F","pubmed_publication_date":"15 Apr 2000","pubmed_entrez_date":"2000-05-18","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008944","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010872","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR1396","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:27036","HGNC:29295","HGNC:51235","HGNC:48813","HGNC:5035","HGNC:51333","HGNC:15921","SPAC3H8.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26609339","title":"Pil1 cytoplasmic rods contain bundles of crosslinked tubules.","citation":"Commun Integr Biol 2015;8(1):e990848","abstract":"Cytoskeletal polymers are organized into a wide variety of higher-order structures in cells. The yeast BAR domain protein Pil1 self-assembles into tubules in vitro, and forms linear polymers at cortical eisosomes in cells. In the fission yeast S. pombe, over-expressed Pil1 forms thick rods that detach from the plasma membrane. In this study, we used thin-section electron microscopy to determine the ultrastructure of these cytoplasmic Pil1 rods. We found that cytoplasmic rods contained crosslinked Pil1 tubules that displayed regular, hexagonal spacing. These bundles were stained by filipin, a sterol-binding fluorescent dye, suggesting that they contained lipids. Cytoplasmic Pil1 rods were present but less abundant in sle1Δ and fhn1Δ mutant cells. We also found that endogenous Pil1 formed thick rods under saturated growth conditions. Taken together, our findings suggest the presence of cellular mechanisms that assemble Pil1 tubules into higher-order structures.","doi":"10.4161/19420889.2014.990848","authors":"Kabeche R, Howard L, Moseley JB","authors_abbrev":"Kabeche R et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-11-27","publication_year":"2015","canto_session_key":"9182dda58c6f59f3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-11-28 01:19:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.15"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8121488","title":"Regulation of progression through the G1 phase of the cell cycle by the rum1+ gene.","citation":"Nature 1994 Jan 20;367(6460):236-42","abstract":"The rum1+ gene is identified as a new regulator of G1 progression in fission yeast. It influences three aspects of G1 regulation: determination of the length of G1, dependence of S phase upon completion of mitosis, and restraint of mitosis until G1 is finished. We propose that it has a central role in regulating the G1 phase of the cell cycle.","authors":"Moreno S, Nurse P","authors_abbrev":"Moreno S et al.","pubmed_publication_date":"20 Jan 1994","pubmed_entrez_date":"1994-01-20","publication_year":"1994","canto_session_key":"904ada6c1059d0f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-03-02 14:11:29","canto_approved_date":"2026-01-30 07:09:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-09 06:35:22","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":10,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.09","SPAC24H6.05","SPBC336.12c","SPBC11B10.09","SPCC18B5.03"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2021-03-02"},{"uniquename":"PMID:26730850","title":"Prp4 Kinase Grants the License to Splice: Control of Weak Splice Sites during Spliceosome Activation.","citation":"PLoS Genet 2016 Jan;12(1):e1005768","abstract":"The genome of the fission yeast Schizosaccharomyces pombe encodes 17 kinases that are essential for cell growth. These include the cell-cycle regulator Cdc2, as well as several kinases that coordinate cell growth, polarity, and morphogenesis during the cell cycle. In this study, we further characterized another of these essential kinases, Prp4, and showed that the splicing of many introns is dependent on Prp4 kinase activity. For detailed characterization, we chose the genes res1 and ppk8, each of which contains one intron of typical size and position. Splicing of the res1 intron was dependent on Prp4 kinase activity, whereas splicing of the ppk8 intron was not. Extensive mutational analyses of the 5' splice site of both genes revealed that proper transient interaction with the 5' end of snRNA U1 governs the dependence of splicing on Prp4 kinase activity. Proper transient interaction between the branch sequence and snRNA U2 was also important. Therefore, the Prp4 kinase is required for recognition and efficient splicing of introns displaying weak exon1/5' splice sites and weak branch sequences.","doi":"10.1371/journal.pgen.1005768","authors":"Eckert D, Andrée N, Razanau A, Zock-Emmenthal S, Lützelberger M, Plath S, Schmidt H, Guerra-Moreno A, Cozzuto L, Ayté J, Käufer NF","authors_abbrev":"Eckert D et al.","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2016-01-06","publication_year":"2016","canto_session_key":"8fac2b6e6e2e1578","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Daniela Eckert","canto_first_approved_date":"2017-01-11 16:29:38","canto_approved_date":"2023-08-03 08:19:11","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2016-12-16 14:22:39","canto_added_date":"2016-01-07 01:19:13","annotation_curators":[{"name":"Daniela Eckert","community_curator":true,"annotation_count":24,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.14","SPAC29E6.08","SPAC22G7.08","SPAC22F3.09c","SPBC776.01","SPBC725.16"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2017-01-11"},{"uniquename":"PMID:37644673","title":"A novel role of the fission yeast sulfiredoxin Srx1 in heme acquisition.","citation":"Mol Microbiol 2023 Oct;120(4):608-628","abstract":"The transporter Str3 promotes heme import in Schizosaccharomyces pombe cells that lack the heme receptor Shu1 and are deficient in heme biosynthesis. Under microaerobic conditions, the peroxiredoxin Tpx1 acts as a heme scavenger within the Str3-dependent pathway. Here, we show that Srx1, a sulfiredoxin known to interact with Tpx1, is essential for optimal growth in the presence of hemin. The expression of Srx1 is induced in response to low iron and repressed under iron repletion. Coimmunoprecipitation and bimolecular fluorescence complementation experiments show that Srx1 interacts with Str3. Although the interaction between Srx1 and Str3 is weakened, it is still observed in tpx1Δ mutant cells or when Str3 is coexpressed with a mutant form of Srx1 (mutD) that cannot bind Tpx1. Further analysis by absorbance spectroscopy and hemin-agarose pull-down assays confirms the binding of Srx1 to hemin, with an equilibrium constant value of 2.56 μM. To validate the Srx1-hemin association, we utilize a Srx1 mutant (mutH) that fails to interact with hemin. Notably, when Srx1 binds to hemin, it partially shields hemin from degradation caused by hydrogen peroxide. Collectively, these findings elucidate an additional function of the sulfiredoxin Srx1, beyond its conventional role in oxidative stress defense.","doi":"10.1111/mmi.15146","authors":"Vahsen T, Brault A, Mourer T, Labbé S","authors_abbrev":"Vahsen T et al.","pubmed_publication_date":"Oct 2023","pubmed_entrez_date":"2023-08-30","publication_year":"2023","canto_session_key":"9635ec291bf95341","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-08-31 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16146630","title":"Small GTPase Rho5 is a functional homologue of Rho1, which controls cell shape and septation in fission yeast.","citation":"FEBS Lett 2005 Sep 26;579(23):5181-6","abstract":"The small GTPase Rho1 plays an essential role in controlling the organization of the actin cytoskeleton and synthesis of the cell wall in the fission yeast Schizosaccharomyces pombe. Here we studied the role of Rho5 whose primary structure is very similar to that of Rho1. It was found that elevated expression of Rho5 was able to compensate for the lethality of cells lacking Rho1. Rho5 was localized to the ends of interphase cells and the mid-region of mitotic cells. Overexpression of Rho5 caused depolarization of F-actin patches and abnormal formation of the cell wall, as did Rho1. Although rho5(+) was not essential for maintaining the cell shape, rho1 rho5-double null cells showed more severe defects in cell viability than rho1-null cells. Thus, it is likely that Rho5 has an overlapping function with Rho1 in controlling cell growth and division in S. pombe.","authors":"Nakano K, Arai R, Mabuchi I","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"26 Sep 2005","pubmed_entrez_date":"2005-09-09","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC20H4.11c","SPAC1F7.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11136464","title":"Functional characterization of the alpha-glucoside transporter Sut1p from Schizosaccharomyces pombe, the first fungal homologue of plant sucrose transporters.","citation":"Mol Microbiol 2001 Jan;39(2):445-54","abstract":"Disaccharide transporters have not previously been identified in Schizosaccharomyces pombe. This is in contrast to Saccharomyces cerevisiae in which several maltose permeases belonging to the sugar porter (SP) family have been characterized. Here we report that a novel S. pombe gene, sut1+, encodes a proton-coupled disaccharide uptake transporter in the glycoside-pentoside-hexuronide (GPH):cation symporter family. Previously, members of the GPH family were restricted to bacteria and plants. The closest homologues of sut1+ are the sucrose uptake transporters (SUTs) from higher plants that transport sucrose with a higher affinity than maltose. The transport function of Sut1p was analysed by expression in S. cerevisiae. Sut1p was found to transport maltose with a Km of 6.5 +/- 0.4 mM and sucrose with a Km of 36.3 +/- 9.7 mM. Therefore, the substrate specificity of Sut1p from S. pombe is different from that of its plant homologues. Glucose repression of sut1+ at the transcriptional level is also consistent with a physiological function for Sut1p in maltose uptake. These results indicate that, unlike S. cerevisiae, S. pombe utilizes maltose transporters derived from a common ancestor with the plant SUTs.","authors":"Reinders A, Ward JM","authors_abbrev":"Reinders A et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-01-03","publication_year":"2001","canto_session_key":"0089b9465b71c321","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-02 08:26:04","canto_approved_date":"2018-02-28 17:54:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-25 12:09:48","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC191.11","SPAC2F3.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-11-02"},{"uniquename":"PMID:27875300","title":"The Fission Yeast Pre-mRNA-processing Factor 18 (prp18+) Has Intron-specific Splicing Functions with Links to G1-S Cell Cycle Progression.","citation":"J Biol Chem 2016 Dec 30;291(53):27387-27402","abstract":"The fission yeast genome, which contains numerous short introns, is an apt model for studies on fungal splicing mechanisms and splicing by intron definition. Here we perform a domain analysis of the evolutionarily conserved Schizosaccharomyces pombe pre-mRNA-processing factor, SpPrp18. Our mutational and biophysical analyses of the C-terminal α-helical bundle reveal critical roles for the conserved region as well as helix five. We generate a novel conditional missense mutant, spprp18-5 To assess the role of SpPrp18, we performed global splicing analyses on cells depleted of prp18 +  and the conditional spprp18-5 mutant, which show widespread but intron-specific defects. In the absence of functional SpPrp18, primer extension analyses on a tfIId +  intron 1-containing minitranscript show accumulated pre-mRNA, whereas the lariat intron-exon 2 splicing intermediate was undetectable. These phenotypes also occurred in cells lacking both SpPrp18 and SpDbr1 (lariat debranching enzyme), a genetic background suitable for detection of lariat RNAs. These data indicate a major precatalytic splicing arrest that is corroborated by the genetic interaction between spprp18-5 and spprp2-1, a mutant in the early acting U2AF59 protein. Interestingly, SpPrp18 depletion caused cell cycle arrest before S phase. The compromised splicing of transcripts coding for G 1 -S regulators, such as Res2, a transcription factor, and Skp1, a regulated proteolysis factor, are shown. The cumulative effects of SpPrp18-dependent intron splicing partly explain the G 1  arrest upon the loss of SpPrp18. Our study using conditional depletion of spprp18 +  and the spprp18-5 mutant uncovers an intron-specific splicing function and early spliceosomal interactions and suggests links with cell cycle progression.","doi":"10.1074/jbc.M116.751289","authors":"Vijaykrishna N, Melangath G, Kumar R, Khandelia P, Bawa P, Varadarajan R, Vijayraghavan U","authors_abbrev":"Vijaykrishna N et al.","pubmed_publication_date":"30 Dec 2016","pubmed_entrez_date":"2016-11-23","publication_year":"2016","canto_session_key":"95881a0ddfd9e0d0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-11-24 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.02c","SPCC126.14","SPBC146.07"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:21731711","title":"Redundant mechanisms prevent mitotic entry following replication arrest in the absence of Cdc25 hyper-phosphorylation in fission yeast.","citation":"PLoS One 2011;6(6):e21348","abstract":"Following replication arrest the Cdc25 phosphatase is phosphorylated and inhibited by Cds1. It has previously been reported that expressing Cdc25 where 9 putative amino-terminal Cds1 phosphorylation sites have been substituted to alanine results in bypass of the DNA replication checkpoint. However, these results were acquired by expression of the phosphorylation mutant using a multicopy expression vector in a genetic background where the DNA replication checkpoint is intact. In order to clarify these results we constructed a Cdc25(9A)-GFP native promoter integrant and examined its effect on the replication checkpoint at endogenous expression levels. In this strain the replication checkpoint operates normally, conditional on the presence of the Mik1 kinase. In response to replication arrest the Cdc25(9A)-GFP protein is degraded, suggesting the presence of a backup mechanism to eliminate the phosphatase when it cannot be inhibited through phosphorylation.","doi":"10.1371/journal.pone.0021348","authors":"Frazer C, Young PG","authors_abbrev":"Frazer C et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-07-07","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19620394","title":"Distinctive responses to nitrogen starvation in the dominant active mutants of the fission yeast Rheb GTPase.","citation":"Genetics 2009 Oct;183(2):517-27","abstract":"Rheb, a Ras-like small GTPase conserved from human to yeast, controls Tor kinase and plays a central role in the regulation of cell growth depending on extracellular conditions. Rhb1 (a fission yeast homolog of Rheb) regulates amino acid uptake as well as response to nitrogen starvation. In this study, we generated two mutants, rhb1-DA4 and rhb1-DA8, and characterized them genetically. The V17A mutation within the G1 box defined for the Ras-like GTPases was responsible for rhb1-DA4 and Q52R I76F within the switch II domain for rhb1-DA8. In fission yeast, two events--the induction of the meiosis-initiating gene mei2+ and cell division without cell growth--are a typical response to nitrogen starvation. Under nitrogen-rich conditions, Rheb stimulates Tor kinase, which, in turn, suppresses the response to nitrogen starvation. While amino acid uptake was prevented by both rhb1-DA4 and rhb1-DA8 in a dominant fashion, the response to nitrogen starvation was prevented only by rhb1-DA4. rhb1-DA8 thereby allowed genetic dissection of the Rheb-dependent signaling cascade. We postulate that the signaling cascade may branch below Rhb1 or Tor2 and regulate the amino acid uptake and response to nitrogen starvation independently.","doi":"10.1534/genetics.109.105379","authors":"Murai T, Nakase Y, Fukuda K, Chikashige Y, Tsutsumi C, Hiraoka Y, Matsumoto T","authors_abbrev":"Murai T et al.","pubmed_publication_date":"Oct 2009","pubmed_entrez_date":"2009-07-22","publication_year":"2009","canto_session_key":"8cf2021a107c5629","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-30 16:11:01","canto_approved_date":"2024-01-01 11:38:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-19 14:31:10","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.02c","SPAC22F3.13","SPCC191.11","SPAC27D7.03c","SPBC428.16c","SPAC630.13c","SPBC216.07c","SPAC17G6.04c","SPBC30D10.10c"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2015-04-30"},{"uniquename":"PMID:10749871","title":"Crystal structure of a conformation-selective casein kinase-1 inhibitor.","citation":"J Biol Chem 2000 Jun 30;275(26):20052-60","abstract":"Members of the casein kinase-1 family of protein kinases play an essential role in cell regulation and disease pathogenesis. Unlike most protein kinases, they appear to function as constitutively active enzymes. As a result, selective pharmacological inhibitors can play an important role in dissection of casein kinase-1-dependent processes. To address this need, new small molecule inhibitors of casein kinase-1 acting through ATP-competitive and ATP-noncompetitive mechanisms were isolated on the basis of in vitro screening. Here we report the crystal structure of 3-[(2,4,6-trimethoxyphenyl) methylidenyl]-indolin-2-one (IC261), an ATP-competitive inhibitor with differential activity among casein kinase-1 isoforms, in complex with the catalytic domain of fission yeast casein kinase-1 refined to a crystallographic R-factor of 22.4% at 2.8 A resolution. The structure reveals that IC261 stabilizes casein kinase-1 in a conformation midway between nucleotide substrate liganded and nonliganded conformations. We propose that adoption of this conformation by casein kinase-1 family members stabilizes a delocalized network of side chain interactions and results in a decreased dissociation rate of inhibitor.","authors":"Mashhoon N, DeMaggio AJ, Tereshko V, Bergmeier SC, Egli M, Hoekstra MF, Kuret J","authors_abbrev":"Mashhoon N et al.","pubmed_publication_date":"30 Jun 2000","pubmed_entrez_date":"2000-04-06","publication_year":"2000","canto_session_key":"79478a3244b6313f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-05-02 18:04:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 21:14:23","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-29","pdb_entries":[{"pdb_id":"1eh4","gene_chains":[{"gene_uniquename":"SPBC1347.06c","chain":"A/B","position":"1-298"}],"title":"BINARY COMPLEX OF CASEIN KINASE-1 FROM S. POMBE WITH AN ATP COMPETITIVE INHIBITOR, IC261","entry_authors":"Mashhoon N,Demaggio AJ,Tereshko V,Bergmeier SC,Egli M,Hoekstra MF,Kuret J","entry_authors_abbrev":"Mashhoon N et al.","reference_uniquename":"PMID:10749871","experimental_method":"X-ray","resolution":"2.8"}]},{"uniquename":"PMID:1541389","title":"Seventeen complementation groups of mutations decreasing meiotic recombination in Schizosaccharomyces pombe.","citation":"Genetics 1992 Feb;130(2):251-62","abstract":"We have analyzed 43 recessive mutations reducing meiotic intragenic recombination in Schizosaccharomyces pombe. These mutations were isolated by a screen for reduced plasmid-by-chromosome recombination at the ade6 locus. Sixteen of the mutations define 10 new complementation groups, bringing to 17 the number of genes identified to be involved in meiotic recombination. The mutations were grouped into three discrete classes depending on the severity of the recombination deficiency in crosses involving the ade6-M26 recombination hotspot. Class I mutations caused at least a 1000-fold reduction in M26-stimulated intragenic recombination at the ade6 locus. Class II mutations reduced M26-stimulated recombination approximately 100-fold. Class III mutations caused a 3-10-fold reduction in either M26-stimulated or non-hotspot recombination. We obtained multiple alleles of class I and class II mutations, suggesting that we may be nearing saturation for mutations of this type. As a first step toward mapping, we used mitotic segregation to assign fourteen of the rec genes to chromosomes. Mutations in the six rec genes tested also caused a decrease in intragenic recombination at the ura4 locus; five of these mutations also reduced intergenic recombination between the pro2 and arg3 genes. These results indicate that these multiple rec gene products are required for high level meiotic recombination throughout the S. pombe genome.","authors":"De Veaux LC, Hoagland NA, Smith GR","authors_abbrev":"De Veaux LC et al.","pubmed_publication_date":"Feb 1992","pubmed_entrez_date":"1992-02-01","publication_year":"1992","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25G10.04c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:32723864","title":"Klp2 and Ase1 synergize to maintain meiotic spindle stability during metaphase I.","citation":"J Biol Chem 2020 Sep 18;295(38):13287-13298","abstract":"The spindle apparatus segregates bi-oriented sister chromatids during mitosis but mono-oriented homologous chromosomes during meiosis I. It has remained unclear if similar molecular mechanisms operate to regulate spindle dynamics during mitosis and meiosis I. Here, we employed live-cell microscopy to compare the spindle dynamics of mitosis and meiosis I in fission yeast cells and demonstrated that the conserved kinesin-14 motor Klp2 plays a specific role in maintaining metaphase spindle length during meiosis I but not during mitosis. Moreover, the maintenance of metaphase spindle stability during meiosis I requires the synergism between Klp2 and the conserved microtubule cross-linker Ase1, as the absence of both proteins causes exacerbated defects in metaphase spindle stability. The synergism is not necessary for regulating mitotic spindle dynamics. Hence, our work reveals a new molecular mechanism underlying meiotic spindle dynamics and provides insights into understanding differential regulation of meiotic and mitotic events.","doi":"10.1074/jbc.RA120.012905","authors":"Zheng F, Dong F, Yu S, Li T, Jian Y, Nie L, Fu C","authors_abbrev":"Zheng F et al.","pubmed_publication_date":"18 Sep 2020","pubmed_entrez_date":"2020-07-30","publication_year":"2020","canto_session_key":"b2b583def5375c2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-05-20 11:21:29","canto_approved_date":"2021-05-20 11:21:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-12 12:36:34","canto_added_date":"2020-07-31 00:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.13","SPAC1834.07","SPAC3A11.14c","SPBC1685.15c","SPBC15D4.01c","SPAC1093.06c","SPAC144.14","SPAPB1A10.09","SPAC664.10","SPBC1604.20c"],"gene_count":10,"ltp_gene_count":5,"approved_date":"2021-05-20"},{"uniquename":"PMID:16584827","title":"Regulation of the cadmium stress response through SCF-like ubiquitin ligases: comparison between Saccharomyces cerevisiae, Schizosaccharomyces pombe and mammalian cells.","citation":"Biochimie 2006 Nov;88(11):1673-85","abstract":"Saccharomyces cerevisiae has developed several mechanisms to cope with exposure to cadmium. In particular, the sulfur compound glutathione plays a pivotal role in cadmium detoxification, and exposure to cadmium leads to a wide reorganization of S. cerevisiae transcriptome and proteome, resulting in a significant increase in glutathione synthesis. Met4, the transcriptional activator of the sulfur metabolism enzymes, is a critical actor in this reorganization. Recent work has uncovered a part of the mechanism of cadmium-induced Met4 regulation, and showed that it occurs trough the SCF ubiquitin ligase complex SCF(Met30). We discuss this regulation in S. cerevisiae and compare it with the regulation of two other transcriptional activators involved in cadmium detoxification: the Schizosaccharomyces pombe Zip1, regulated by SCF(Pof1), and the mammalian Nrf2, regulated by the SCF-like ubiquitin ligase Cul3:Rbx1:Keap1.","authors":"Baudouin-Cornu P, Labarre J","authors_abbrev":"Baudouin-Cornu P et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-04-06","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36713198","title":"Synonymous mutations in the phosphoglycerate kinase 1 gene induce an altered response to protein misfolding in  Schizosaccharomyces pombe .","citation":"Front Microbiol 2022;13:1074741","abstract":"Taken together, these data suggest that codon usage bias of the gene encoding this highly-expressed protein is an important regulator of protein function and proteostasis.","doi":"10.3389/fmicb.2022.1074741","authors":"Moreira-Ramos S, Arias L, Flores R, Katz A, Levicán G, Orellana O","authors_abbrev":"Moreira-Ramos S et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2023-01-30","publication_year":"2022","canto_session_key":"94fe2a52d53356b7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-01-31 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10908351","title":"The nature of the 5'-terminus is a major determinant for DNA processing by Schizosaccharomyces pombe Rad2p, a FEN-1 family nuclease.","citation":"Nucleic Acids Res 2000 Aug 01;28(15):2893-901","abstract":"The nuclease activity of FEN-1 is essential for both DNA replication and repair. Intermediate DNA products formed during these processes possess a variety of structures and termini. We have previously demonstrated that the 5'-->3' exonuclease activity of the Schizosaccharomyces pombe FEN-1 protein Rad2p requires a 5'-phosphoryl moiety to efficiently degrade a nick-containing substrate in a reconstituted alternative excision repair system. Here we report the effect of different 5'-terminal moieties of a variety of DNA substrates on Rad2p activity. We also show that Rad2p possesses a 5'-->3' single-stranded exonuclease activity, similar to Saccharomyces cerevisiae Rad27p and phage T5 5'-->3' exonuclease (also a FEN-1 homolog). FEN-1 nucleases have been associated with the base excision repair pathway, specifically processing cleaved abasic sites. Because several enzymes cleave abasic sites through different mechanisms resulting in different 5'-termini, we investigated the ability of Rad2p to process several different types of cleaved abasic sites. With varying efficiency, Rad2p degrades the products of an abasic site cleaved by Escherichia coli endonuclease III and endonuclease IV (prototype AP endonucleases) and S.POMBE: Uve1p. These results provide important insights into the roles of Rad2p in DNA repair processes in S.POMBE:","authors":"Alleva JL, Doetsch PW","authors_abbrev":"Alleva JL et al.","pubmed_publication_date":"01 Aug 2000","pubmed_entrez_date":"2000-07-25","publication_year":"2000","canto_session_key":"5e293f0423563c16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-10-31 16:13:20","canto_approved_date":"2019-10-31 16:13:20","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-10-31 16:13:12","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-10-31"},{"uniquename":"PMID:20946810","title":"Synthetic genetic array (SGA) analysis in Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Methods Enzymol 2010;470:145-79","abstract":"A genetic interaction occurs when the combination of two mutations leads to an unexpected phenotype. Screens for synthetic genetic interactions have been used extensively to identify genes whose products are functionally related. In particular, synthetic lethal genetic interactions often identify genes that buffer one another or impinge on the same essential pathway. For the yeast Saccharomyces cerevisiae, we developed a method termed synthetic genetic array (SGA) analysis, which offers an efficient approach for the systematic construction of double mutants and enables a global analysis of synthetic genetic interactions. In a typical SGA screen, a query mutation is crossed to an ordered array of ~5000 viable gene deletion mutants (representing ~80% of all yeast genes) such that meiotic progeny harboring both mutations can be scored for fitness defects. This approach can be extended to all ~6000 genes through the use of yeast arrays containing mutants carrying conditional or hypomorphic alleles of essential genes. Estimating the fitness for the two single mutants and their corresponding double mutant enables a quantitative measurement of genetic interactions, distinguishing negative (synthetic lethal) and positive (within pathway and suppression) interactions. The profile of genetic interactions represents a rich phenotypic signature for each gene and clustering genetic interaction profiles group genes into functionally relevant pathways and complexes. This array-based approach automates yeast genetic analysis in general and can be easily adapted for a number of different genetic screens or combined with high-content screening systems to quantify the activity of specific reporters in genome-wide sets of single or more complex multiple mutant backgrounds. Comparison of genetic and chemical-genetic interaction profiles offers the potential to link bioactive compounds to their targets. Finally, we also developed an SGA system for the fission yeast Schizosaccharomyces pombe, providing another model system for comparative analysis of genetic networks and testing the conservation of genetic networks over millions of years of evolution.","doi":"10.1016/S0076-6879(10)70007-0","authors":"Baryshnikova A, Costanzo M, Dixon S, Vizeacoumar FJ, Myers CL, Andrews B, Boone C","authors_abbrev":"Baryshnikova A et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-10-16","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006802","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.112"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU008380","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22064476","title":"A U1-U2 snRNP interaction network during intron definition.","citation":"Mol Cell Biol 2012 Jan;32(2):470-8","abstract":"The assembly of prespliceosomes is responsible for selection of intron sites for splicing. U1 and U2 snRNPs recognize 5' splice sites and branch sites, respectively; although there is information regarding the composition of these complexes, little is known about interaction among the components or between the two snRNPs. Here we describe the protein network of interactions linking U1 and U2 snRNPs with the ATPase Prp5, important for branch site recognition and fidelity during the first steps of the reaction, using fission yeast Schizosaccharomyces pombe. The U1 snRNP core protein U1A binds to a novel SR-like protein, Rsd1, which has homologs implicated in transcription. Rsd1 also contacts S. pombe Prp5 (SpPrp5), mediated by SR-like domains in both proteins. SpPrp5 then contacts U2 snRNP through SF3b, mediated by a conserved DPLD motif in Prp5. We show that mutations in this motif have consequences not only in vitro (defects in prespliceosome formation) but also in vivo, yielding intron retention and exon skipping defects in fission yeast and altered intron recognition in budding yeast Saccharomyces cerevisiae, indicating that the U1-U2 network provides critical, evolutionarily conserved contacts during intron definition.","doi":"10.1128/MCB.06234-11","authors":"Shao W, Kim HS, Cao Y, Xu YZ, Query CC","authors_abbrev":"Shao W et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2011-11-09","publication_year":"2012","canto_session_key":"42c0feda9c41e26a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-19 12:11:06","canto_approved_date":"2026-01-29 13:03:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-19 12:02:12","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":35,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.07c","SPAC22F8.10c","SPCC10H11.01","SPAPJ698.03c","SPBC839.10","SPBC4B4.07c","SPAC27F1.09c","SPAC31G5.01","SPBC29A3.07c","SPSNRNA.06"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2014-08-19"},{"uniquename":"EMBL:AU013717","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.105"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2557578","title":"Nucleotide sequence of the gene encoding subunit 3 of cytochrome c oxidase (cox3) in the mitochondrial genome of Schizosaccharomyces pombe strain EF1.","citation":"Nucleic Acids Res 1989 Dec 11;17(23):10104","abstract":"","authors":"Trinkl H, Wolf K","authors_abbrev":"Trinkl H et al.","pubmed_publication_date":"11 Dec 1989","pubmed_entrez_date":"1989-12-11","publication_year":"1989","canto_session_key":"07bff8ad8c0501d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:19:44","canto_approved_date":"2018-12-22 20:19:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 20:19:37","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:17478483","title":"Rapid screen of human genes for relevance to cancer using fission yeast.","citation":"J Biomol Screen 2007 Jun;12(4):568-77","abstract":"A total of 437 human full-length cDNAs isolated by microarray analysis of liver and/or gastric cancer tissues were evaluated for their relevance to cancer using the fission yeast Schizosaccharomyces pombe. Overexpression of 161 human cDNAs in S. pombe caused growth inhibition and/or morphological changes, which can be considered as cancer-related phenotypes of S. pombe. Sixteen genes causing growth defects and morphological changes at the same time were chosen to validate their ostensible oncogenic properties. They were highly expressed in liver and/or gastric cancer cell lines. Also, when the mouse embryonic fibroblast cell type NIH3T3 was transfected with these genes, the proliferation rates of cells were increased by 32% to 120%. This study demonstrates that fission yeast can be used as an advantageous and powerful tool for the rapid screening of human genes relevant to cancer. Furthermore, the human genes screened can be tested further as diagnostic markers and potential therapeutic targets for liver and stomach cancers. They also can be studied further for the elucidation of mechanisms involved in carcinogenesis.","authors":"Chung KS, Jang YJ, Kim NS, Park SY, Choi SJ, Kim JY, Ahn JH, Lee HJ, Lim JH, Song JH, Ji JH, Oh JH, Song KB, Yoo HS, Won M","authors_abbrev":"Chung KS et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-05-05","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32841241","title":"Hypomodified tRNA in evolutionarily distant yeasts can trigger rapid tRNA decay to activate the general amino acid control response, but with different consequences.","citation":"PLoS Genet 2020 Aug;16(8):e1008893","abstract":"All tRNAs are extensively modified, and modification deficiency often results in growth defects in the budding yeast Saccharomyces cerevisiae and neurological or other disorders in humans. In S. cerevisiae, lack of any of several tRNA body modifications results in rapid tRNA decay (RTD) of certain mature tRNAs by the 5'-3' exonucleases Rat1 and Xrn1. As tRNA quality control decay mechanisms are not extensively studied in other eukaryotes, we studied trm8Δ mutants in the evolutionarily distant fission yeast Schizosaccharomyces pombe, which lack 7-methylguanosine at G46 (m7G46) of their tRNAs. We report here that S. pombe trm8Δ mutants are temperature sensitive primarily due to decay of tRNATyr(GUA) and that spontaneous mutations in the RAT1 ortholog dhp1+ restored temperature resistance and prevented tRNA decay, demonstrating conservation of the RTD pathway. We also report for the first time evidence linking the RTD and the general amino acid control (GAAC) pathways, which we show in both S. pombe and S. cerevisiae. In S. pombe trm8Δ mutants, spontaneous GAAC mutations restored temperature resistance and tRNA levels, and the trm8Δ temperature sensitivity was precisely linked to GAAC activation due to tRNATyr(GUA) decay. Similarly, in the well-studied S. cerevisiae trm8Δ trm4Δ RTD mutant, temperature sensitivity was closely linked to GAAC activation due to tRNAVal(AAC) decay; however, in S. cerevisiae, GAAC mutations increased tRNA loss and exacerbated temperature sensitivity. A similar exacerbated growth defect occurred upon GAAC mutation in S. cerevisiae trm8Δ and other single modification mutants that triggered RTD. Thus, these results demonstrate a conserved GAAC activation coincident with RTD in S. pombe and S. cerevisiae, but an opposite impact of the GAAC response in the two organisms. We speculate that the RTD pathway and its regulation of the GAAC pathway is widely conserved in eukaryotes, extending to other mutants affecting tRNA body modifications.","doi":"10.1371/journal.pgen.1008893","authors":"De Zoysa T, Phizicky EM","authors_abbrev":"De Zoysa T et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-08-26","publication_year":"2020","canto_session_key":"b237acc888396401","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Thareendra De Zoysa","canto_first_approved_date":"2021-01-25 11:34:40","canto_approved_date":"2026-02-17 15:26:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-14 15:48:39","canto_added_date":"2020-08-27 00:15:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Thareendra De Zoysa","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36B7.09","SPCC1393.08","SPCPB16A4.04c","SPAC26A3.12c","SPCC11E10.07c","SPAC18G6.05c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2021-01-25"},{"uniquename":"PMID:9427538","title":"sep1+ encodes a transcription-factor homologue of the HNF-3/forkhead DNA-binding-domain family in Schizosaccharomyces pombe.","citation":"Gene 1997 Nov 20;202(1-2):1-5","abstract":"We report on the cloning of sep1+, a gene whose mutation causes filamentous growth in Schizosaccharomyces pombe. Since cell growth and propagation are not affected by the mutation, it could not be cloned using selective conditions for the identification of the positive transformants. Instead, we cloned it from a cosmid of a contig (Hoheisel et al., Cell 73, 109-1120, 1993) supposed to cover the chromosomal region where the sep1-1 mutation mapped. The 1761 bp long ORF codes for a protein containing a sequence similar to the DNA-binding domains of the HNF-3/forkhead family of transcription factors.","authors":"Ribár B, Bánrévi A, Sipiczki M","authors_abbrev":"Ribár B et al.","pubmed_publication_date":"20 Nov 1997","pubmed_entrez_date":"1998-01-14","publication_year":"1997","canto_session_key":"1b1aa8610b1a99d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-02-28 17:09:09","canto_approved_date":"2019-02-28 17:09:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-02-28 17:08:36","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4C3.12"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-02-28"},{"uniquename":"PMID:30267671","title":"The mitochondrial phosphatase PPTC7 orchestrates mitochondrial metabolism regulating coenzyme Q 10  biosynthesis.","citation":"Biochim Biophys Acta Bioenerg 2018 Nov;1859(11):1235-1248","abstract":"Coenzyme Q 10  (CoQ 10 ) is a redox molecule critical for the proper function of energy metabolism and antioxidant defenses. Despite its essential role in cellular metabolism, the regulation of CoQ 10  biosynthesis in humans remains mostly unknown. Herein, we determined that PPTC7 is a regulatory protein of CoQ 10  biosynthesis required for human cell survival. We demonstrated by in vitro approaches that PPTC7 is a bona fide protein phosphatase that dephosphorylates the human COQ7. Expression modulation experiments determined that human PPTC7 dictates cellular CoQ 10  content. Using two different approaches (PPTC7 over-expression and caloric restriction), we demonstrated that PPTC7 facilitates and improves the human cell adaptation to respiratory conditions. Moreover, we determined that the physiological role of PPTC7 takes place in the adaptation to starvation and pro-oxidant conditions, facilitating the induction of mitochondrial metabolism while preventing the accumulation of ROS. Here we unveil the first post-translational mechanism regulating CoQ 10  biosynthesis in humans and propose targeting the induction of PPTC7 activity/expression for the treatment of CoQ 10 -related mitochondrial diseases.","doi":"10.1016/j.bbabio.2018.09.369","authors":"González-Mariscal I, Martin-Montalvo A, Vazquez-Fonseca L, Pomares-Viciana T, Sánchez-Cuesta A, Fernández-Ayala DJ, Navas P, Santos-Ocana C","authors_abbrev":"González-Mariscal I et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-09-30","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1556.03","SPBC337.15c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:19109429","title":"GINS inactivation phenotypes reveal two pathways for chromatin association of replicative alpha and epsilon DNA polymerases in fission yeast.","citation":"Mol Biol Cell 2009 Feb;20(4):1213-22","abstract":"The tetrameric GINS complex, consisting of Sld5-Psf1-Psf2-Psf3, plays an essential role in the initiation and elongation steps of eukaryotic DNA replication, although its biochemical function is unclear. Here we investigate the function of GINS in fission yeast, using fusion of Psf1 and Psf2 subunits to a steroid hormone-binding domain (HBD) to make GINS function conditional on the presence of beta-estradiol. We show that inactivation of Psf1-HBD causes a tight but rapidly reversible DNA replication arrest phenotype. Inactivation of Psf2-HBD similarly blocks premeiotic DNA replication and leads to loss of nuclear localization of another GINS subunit, Psf3. Inactivation of GINS has distinct effects on the replication origin association and chromatin binding of two of the replicative DNA polymerases. Inactivation of Psf1 leads to loss of chromatin binding of DNA polymerase epsilon, and Cdc45 is similarly affected. In contrast, chromatin association of the catalytic subunit of DNA polymerase alpha is not affected by defective GINS function. We suggest that GINS functions in a pathway that involves Cdc45 and is necessary for DNA polymerase epsilon chromatin binding, but that a separate pathway sets up the chromatin association of DNA polymerase alpha.","authors":"Pai CC, García I, Wang SW, Cotterill S, Macneill SA, Kearsey SE","authors_abbrev":"Pai CC et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-12-26","publication_year":"2009","canto_session_key":"893c30409873a782","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-08-06 13:58:23","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-06-18 05:28:41","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.13c","SPAC227.16c","SPBC25H2.13c","SPAC3H5.06c","SPBC336.12c","SPBC3D6.09","SPBC336.04","SPBP23A10.09","SPAC17D4.02"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2013-06-18"},{"uniquename":"PMID:9813085","title":"The UDP-Glc:Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress.","citation":"J Cell Biol 1998 Nov 02;143(3):625-35","abstract":"Interaction of monoglucosylated oligosaccharides with ER lectins (calnexin and/or calreticulin) facilitates glycoprotein folding but this interaction is not essential for cell viability under normal conditions. We obtained two distinct single Schizosaccharomyces pombe mutants deficient in either one of the two pathways leading to the formation of monoglucosylated oligosaccharides. The alg6 mutant does not glucosy- late lipid-linked oligosaccharides and transfers Man9GlcNAc2 to nascent polypeptide chains and the gpt1 mutant lacks UDP-Glc:glycoprotein glucosyltransferase (GT). Both single mutants grew normally at 28 degreesC. On the other hand, gpt1/alg6 double-mutant cells grew very slowly and with a rounded morphology at 28 degreesC and did not grow at 37 degreesC. The wild-type phenotype was restored by transfection of the double mutant with a GT-encoding expression vector or by addition of 1 M sorbitol to the medium, indicating that the double mutant is affected in cell wall formation. It is suggested that facilitation of glycoprotein folding mediated by the interaction of monoglucosylated oligosaccharides with calnexin is essential for cell viability under conditions of extreme ER stress such as underglycosylation of proteins caused by the alg6 mutation and high temperature. In contrast, gls2/alg6 double-mutant cells that transfer Man9GlcNAc2 and that are unable to remove the glucose units added by GT as they lack glucosidase II (GII), grew at 37 degreesC and had, when grown at 28 degreesC, a phenotype of growth and morphology almost identical to that of wild-type cells. These results indicate that facilitation of glycoprotein folding mediated by the interaction of calnexin and monoglucosylated oligosaccharides does not necessarily require cycles of reglucosylation-deglucosylation catalyzed by GT and GII.","authors":"Fanchiotti S, Fernández F, D'Alessio C, Parodi AJ","authors_abbrev":"Fanchiotti S et al.","pubmed_publication_date":"02 Nov 1998","pubmed_entrez_date":"1998-11-13","publication_year":"1998","canto_session_key":"b91556d0478e3dea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-30 13:37:52","canto_approved_date":"2025-10-07 06:59:37","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-10-03 16:04:01","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.15c","SPAC1002.03c","SPBPJ4664.06","SPBC342.01c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2017-10-30"},{"uniquename":"PMID:14752051","title":"Functional analysis of subcellular localization and protein-protein interaction sequences in the essential DNA ligase I protein of fission yeast.","citation":"Nucleic Acids Res 2004;32(2):632-42","abstract":"DNA ligase I (Lig I) has key roles in chromosomal DNA replication and repair in the eukaryotic cell nucleus. In the budding yeast Saccharomyces cerevisiae the Lig I enzyme Cdc9p is also required for mitochondrial DNA replication and repair. In this report, dual nuclear-mitochondrial localization is demonstrated to be a property of the essential Lig I enzyme Cdc17 from the distantly related fission yeast Schizosaccharomyces pombe. Expression of nuclear and mitochondrial forms of Cdc17 from separate genes shows that, whereas expression of either protein alone is insufficient to restore viability to cells lacking endogenous Cdc17, co-expression restores full viability. In the nucleus, Lig I interacts with the sliding clamp proliferating cell nuclear antigen (PCNA) via a conserved PCNA interacting sequence motif known as a PIP box. Deletion of the PIP motif from the N-terminus of the nuclear form of Cdc17 fails to abolish Cdc17 function, indicating that PCNA binding by Cdc17 is not an absolute requirement for completion of S-phase.","authors":"Martin IV, MacNeill SA","authors_abbrev":"Martin IV et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-01-31","publication_year":"2004","canto_session_key":"b2890d84738249aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-03-03 15:10:04","canto_approved_date":"2023-05-15 15:16:13","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2016-03-03 15:09:58","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":57,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.01","SPBC16D10.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-03-03"},{"uniquename":"PMID:34103492","title":"The zinc-finger protein Red1 orchestrates MTREC submodules and binds the Mtl1 helicase arch domain.","citation":"Nat Commun 2021 Jun 08;12(1):3456","abstract":"Cryptic unstable transcripts (CUTs) are rapidly degraded by the nuclear exosome in a process requiring the RNA helicase Mtr4 and specific adaptor complexes for RNA substrate recognition. The PAXT and MTREC complexes have recently been identified as homologous exosome adaptors in human and fission yeast, respectively. The eleven-subunit MTREC comprises the zinc-finger protein Red1 and the Mtr4 homologue Mtl1. Here, we use yeast two-hybrid and pull-down assays to derive a detailed interaction map. We show that Red1 bridges MTREC submodules and serves as the central scaffold. In the crystal structure of a minimal Mtl1/Red1 complex an unstructured region adjacent to the Red1 zinc-finger domain binds to both the Mtl1 KOW domain and stalk helices. This interaction extends the canonical interface seen in Mtr4-adaptor complexes. In vivo mutational analysis shows that this interface is essential for cell survival. Our results add to Mtr4 versatility and provide mechanistic insights into the MTREC complex.","doi":"10.1038/s41467-021-23565-3","authors":"Dobrev N, Ahmed YL, Sivadas A, Soni K, Fischer T, Sinning I","authors_abbrev":"Dobrev N et al.","pubmed_publication_date":"08 Jun 2021","pubmed_entrez_date":"2021-06-09","publication_year":"2021","canto_session_key":"b109e3c3ecaeaf4a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-11 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10219997","title":"Biosynthesis of phytochelatins in the fission yeast. Phytochelatin synthesis: a second role for the glutathione synthetase gene of Schizosaccharomyces pombe.","citation":"Yeast 1999 Mar 30;15(5):385-96","abstract":"By complementation screening of a cadmium-sensitive Schizosaccharomyces pombe mutant deficient in phytochelatin synthesis, but with 44% of the wild-type glutathione content, we cloned a DNA fragment involved in phytochelatin synthesis. Sequence analysis revealed that it encodes the second enzyme involved in glutathione (GSH) biosynthesis, glutathione synthetase (GSH2) (E.C.6.3.2.3, Wang and Oliver, 1997). The mutant allele shows a single base-pair exchange at the 3' end of the reading frame leading to a single amino acid change from glycine to aspartate. This mutation leads to a significant reduction of phytochelatin synthesis, whereas glutathione synthesis is impaired to a far lesser extent. Complementation with the Arabidopsis thaliana GSH2 cDNA led to a partial restoration of phytochelatin synthesis. These data strongly suggest that the GSH2 gene encodes a bifunctional enzyme that is able to catalyse both the synthesis of GSH by adding glycine to the dipeptide (gammaGlu-Cys) and the synthesis of phytochelatins. The sequence has been submitted to EMBL, Accession No. Y08414.","authors":"Al-Lahham A, Rohde V, Heim P, Leuchter R, Veeck J, Wunderlich C, Wolf K, Zimmermann M","authors_abbrev":"Al-Lahham A et al.","pubmed_publication_date":"30 Mar 1999","pubmed_entrez_date":"1999-04-29","publication_year":"1999","canto_session_key":"23584aea6fed32a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-21 13:17:55","canto_approved_date":"2026-01-23 13:41:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-20 09:41:46","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-21"},{"uniquename":"PMID:10748059","title":"Nic1p, a relative of bacterial transition metal permeases in Schizosaccharomyces pombe, provides nickel ion for urease biosynthesis.","citation":"J Biol Chem 2000 Jun 16;275(24):18029-33","abstract":"The Schizosaccharomyces pombe genome sequencing project identified an open reading frame (O74869 and O74912, named Nic1p in the present study) with significant similarity to members of a family of bacterial transition metal permeases. These uptake systems transport Ni(2+) ion with extremely high affinity across the bacterial cytoplasmic membrane, but they differ in selectivity toward divalent transition metal cations. An S. pombe mutant harboring an interrupted nic1 allele (nic1-1) was strongly impaired in (63)Ni(2+) uptake in the presence of a high molar ratio of Mg(2+) relative to Ni(2+), conditions that reflect the natural situation. Under these conditions, the nic1-1 mutant contained only background activities of the nickel-dependent cytoplasmic enzyme urease and could not catabolize urea. Among a series of divalent transition metal cations tested (Cd(2+), Co(2+), Cu(2+), Mn(2+), and Zn(2+)), only Co(2+) caused considerable inhibition of Nic1p-mediated Ni(2+) uptake. On the other hand, experiments with (57)Co(2+) (at nm concentrations) did not show significant differences in Co(2+) uptake between the nic1-1 mutant and the parental strain. Our data suggest that Nic1p acts as a plasma-membrane nickel transporter in fission yeast, a finding that invites searches for isologous counterparts in higher eukaryotes.","authors":"Eitinger T, Degen O, Bohnke U, Muller M","authors_abbrev":"Eitinger T et al.","pubmed_publication_date":"16 Jun 2000","pubmed_entrez_date":"2000-04-05","publication_year":"2000","canto_session_key":"947219ec962a1b36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-26 13:13:54","canto_approved_date":"2026-01-16 10:21:17","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-11-30 16:53:26","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1884.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-26"},{"uniquename":"PMID:24177740","title":"The pedigree pattern of mating-type switching in Schizosaccharomyces pombe.","citation":"Curr Genet 1984 Apr;8(3):205-10","abstract":"The previous ovservation that in dividing sister cells of Schizosaccharomyces pombe only one of two parallel divisions can be accompanied by a switch of mating type, herein termed \"Miyata's rule\", has been confirmed in pedigrees of diploid cells heterozygous for the mat2-Pm-B102 allele. Moreover, this rule appears to operate at the level of individual chromosomes, since in diploid cells simultaneous single-switch events were frequently observed in both sister cells, albeit on different chromosomes. Assuming two successive precursory states for the smt switching signal to the right of mat1, a deterministic 3-step model coupled to the cell cycle has been fitted to the empirical frequency distribution of conjugation in \"four-lined cells\" (a minipedigree of dividing sister cells). The nature of the first intermediate is still unknown, while the ultimate precursor of a switching event is probably a double-strand cut at smt, which can be revealed by molecular analyses.","doi":"10.1007/BF00417817","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"Apr 1984","pubmed_entrez_date":"2013-11-02","publication_year":"1984","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15917811","title":"Polo kinase links the stress pathway to cell cycle control and tip growth in fission yeast.","citation":"Nature 2005 May 26;435(7041):507-12","abstract":"Stress-activated mitogen-activated protein kinase cascades instigate a range of changes to enable eukaryotic cells to cope with particular insults. In Schizosaccharomyces pombe these responses include the transcription of specific gene sets and inhibition of entry into mitosis. The S. pombe stress response pathway (SRP) also promotes commitment to mitosis in unperturbed cell cycles to allow cells to match their rate of division with nutrient availability. The nature of this SRP function in cell cycle control is unknown. Entry into mitosis is controlled by mitosis-promoting factor (MPF; Cdc2/cyclin B) activity. Inhibitory phosphorylation of Cdc2 by Wee1 kinase inactivates MPF until Cdc25 removes this phosphate to promote mitosis. The balance between Wee1 and Cdc25 activities is influenced by the recruitment of polo kinase (Plo1) to the spindle pole body (SPB). The SPB component Cut12 mediates this recruitment. Hyper-activating mutations in either cut12 or plo1 enable Cdc25-defective cells to enter mitosis. The hyperactive cut12.s11 mutation suppresses cdc25.22, as it promotes recruitment of active Plo1 to interphase SPBs. Here we show that the SRP promotes phosphorylation of Plo1 on Ser 402. In unperturbed cell cycles, SRP-mediated phosphorylation of Ser 402 promotes Plo1 recruitment to SPBs and thus commitment to mitosis. Ser 402 phosphorylation also ensures efficient reinitiation of cell tip growth and cell division during recovery from particular stresses. Thus, phosphorylation of Plo1 Ser 402 not only enables SRP signalling to modulate the timing of mitotic commitment in response to nutrient status in unperturbed cycles, but also promotes the return to normal cell cycle control after stress.","authors":"Petersen J, Hagan IM","authors_abbrev":"Petersen J et al.","pubmed_publication_date":"26 May 2005","pubmed_entrez_date":"2005-05-27","publication_year":"2005","canto_session_key":"21507585ab1a2dfc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-27 13:00:43","canto_approved_date":"2020-12-16 17:02:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-10-03 13:19:33","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPBC409.07c","SPAC23C11.16","SPAC24B11.06c","SPBC649.05","SPAC24H6.05"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-04-27"},{"uniquename":"PMID:16127433","title":"Ubiquitin ligase component Cul4 associates with Clr4 histone methyltransferase to assemble heterochromatin.","citation":"Nat Cell Biol 2005 Oct;7(10):1007-13","abstract":"In eukaryotes, heterochromatin mediates diverse processes including gene silencing and regulation of long-range chromatin interactions. The formation of heterochromatin involves a conserved array of histone modifications; in particular, methylation of histone H3 at Lys 9 (H3K9me) is essential for recruiting HP1/Swi6 proteins. In fission yeast, the Clr4 methyltransferase is responsible for H3K9me across all heterochromatic domains. However, the mechanism of Clr4 recruitment to these loci is poorly understood. We show that Clr4 associates with Cul4, a cullin family protein that serves as a scaffold for assembling ubiquitin ligases. Mutations in Cul4 result in defective localization of Clr4 and loss of silencing at heterochromatic loci. This is accompanied by a severe reduction in H3K9me and Swi6 levels, and accumulation of transcripts corresponding to naturally silenced repeat elements within heterochromatic domains. Moreover, heterochromatin defects in Cul4 mutants could not be rescued by expression of Cul4 protein lacking Nedd8 modification, which is essential for its ubiquitin ligase activity. Rik1, a protein related to DNA damage binding protein DDB1 and required for H3K9me, also interacts with Cul4, the association of which might serve to target Clr4 to heterochromatic loci. These analyses uncover a role for Cul4-based protein ubiquitination in regulating H3K9me and heterochromatin formation.","authors":"Jia S, Kobayashi R, Grewal SI","authors_abbrev":"Jia S et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-08-30","publication_year":"2005","canto_session_key":"a63056e1f1822e23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-07 16:22:42","canto_approved_date":"2024-05-24 16:30:46","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-05-02 09:03:21","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":35,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A11.08","SPBC428.08c","SPAC664.01c","SPCC11E10.08"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2024-05-07"},{"uniquename":"PMID:10716991","title":"Mik1 levels accumulate in S phase and may mediate an intrinsic link between S phase and mitosis.","citation":"Proc Natl Acad Sci U S A 2000 Mar 14;97(6):2579-84","abstract":"Two paradigms exist for maintaining order during cell-cycle progression: intrinsic controls, where passage through one part of the cell cycle directly affects the ability to execute another, and checkpoint controls, where external pathways impose order in response to aberrant structures. By studying the mitotic inhibitor Mik1, we have identified evidence for an intrinsic link between unperturbed S phase and mitosis. We propose a model in which S/M linkage can be generated by the production and stabilization of Mik1 protein during S phase. The production of Mik1 during unperturbed S phase is independent of the Rad3- and Cds1-dependent checkpoint controls. In response to perturbed S phase, Rad3-Cds1 checkpoint controls are required to maintain high levels of Mik1, probably indirectly by extending the S phase period, where Mik1 is stable. In addition, we find that Mik1 protein can be moderately induced in response to irradiation of G(2) cells in a Chk1-dependent manner.","authors":"Christensen PU, Bentley NJ, Martinho RG, Nielsen O, Carr AM","authors_abbrev":"Christensen PU et al.","pubmed_publication_date":"14 Mar 2000","pubmed_entrez_date":"2000-03-16","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012946","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41873186","title":"Homologous recombination mutants cause differing lethality between h- and h+ Schizosaccharomyces pombe strains due to mat1 heterochromatin.","citation":"FEBS J 2026 Mar 23;","abstract":"Homologous recombination (HR) is generally considered dispensable in yeast and vertebrates, yet mounting evidence indicates that its essentiality depends on cellular context. Here, we dissect the basis of this context dependency in Schizosaccharomyces pombe. In the homothallic h 90  strain, regarded as wild type, mating-type switching (MTS) occurs every other cell division and requires HR to repair programmed double-strand breaks (DSBs) at the mat1 locus. We show that the widely used heterothallic h -S  strain is likewise dependent on HR for viability. HR-deficient h -S  mutants (rad51Δ, rad52Δ, or rad54Δ), still frequently employed in the literature, survive only when carrying secondary suppressor mutations that abolish mat1 DSB formation, such as smt-0, swi1Δ, or fml1Δ. In contrast, HR is dispensable in the h +N  strain, where duplication of the mat2/3 region into mat1 introduces the cenH and REIII elements. These elements nucleate H3K9 methylation and heterochromatin spreading across the imprint site, blocking imprintosome recruitment and thereby preventing both imprinting and DSB formation. Disruption of this heterochromatin, via deletion of cenH or key chromatin modifiers, restores DSB formation in h +N  cells and reinstates HR essentiality in the absence of the Clr4 methyltransferase. Collectively, our findings demonstrate that HR is indispensable for S. pombe survival due to its critical role in repairing mat1 DSBs, except under genetic or epigenetic conditions that suppress their formation.","doi":"10.1111/febs.70507","authors":"Kolesar P, Paliavoi S, Stefanovie B, Palecek JJ","authors_abbrev":"Kolesar P et al.","pubmed_publication_date":"23 Mar 2026","pubmed_entrez_date":"2026-03-24","publication_year":"2026","canto_session_key":"72d1b19a5566d798","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Kolesar","canto_first_approved_date":"2026-06-09 07:17:33","canto_approved_date":"2026-06-09 07:17:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-06-01 11:48:15","canto_added_date":"2026-03-25 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":10,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Peter Kolesar","community_curator":true,"annotation_count":11,"orcid":"0000-0002-3315-3586","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.03c","SPBC216.06c","SPBC428.08c","SPAC644.14c","SPAC9.05","SPAC30D11.10"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2026-06-09"},{"uniquename":"PMID:24013500","title":"A conserved ncRNA-binding protein recruits silencing factors to heterochromatin through an RNAi-independent mechanism.","citation":"Genes Dev 2013 Sep 01;27(17):1851-6","abstract":"Long noncoding RNAs (lncRNAs) can trigger repressive chromatin, but how they recruit silencing factors remains unclear. In Schizosaccharomyces pombe, heterochromatin assembly on transcribed noncoding pericentromeric repeats requires both RNAi and RNAi-independent mechanisms. In Saccharomyces cerevisiae, which lacks a repressive chromatin mark (H3K9me [methylated Lys9 on histone H3]), unstable ncRNAs are recognized by the RNA-binding protein Nrd1. We show that the S. pombe ortholog Seb1 is associated with pericentromeric lncRNAs. Individual mutation of dcr1+ (Dicer) or seb1+ results in equivalent partial reductions of pericentromeric H3K9me levels, but a double mutation eliminates this mark. Seb1 functions independently of RNAi by recruiting the NuRD (nucleosome remodeling and deacetylase)-related chromatin-modifying complex SHREC (Snf2-HDAC [histone deacetylase] repressor complex).","doi":"10.1101/gad.226019.113","authors":"Marina DB, Shankar S, Natarajan P, Finn KJ, Madhani HD","authors_abbrev":"Marina DB et al.","pubmed_publication_date":"01 Sep 2013","pubmed_entrez_date":"2013-09-10","publication_year":"2013","canto_session_key":"38f42cd29537f6be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-20 15:26:58","canto_approved_date":"2025-12-17 10:00:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-20 14:30:11","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.10","SPBC800.03","SPBC428.08c","SPAC222.09","SPBC2D10.17","SPCC1739.03","SPBC16C6.10","SPAC2F7.11","SPCC188.13c","SPAC1B3.17"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2024-06-20"},{"uniquename":"EMBL:SPD248","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15226438","title":"The fission yeast Nup107-120 complex functionally interacts with the small GTPase Ran/Spi1 and is required for mRNA export, nuclear pore distribution, and proper cell division.","citation":"Mol Cell Biol 2004 Jul;24(14):6379-92","abstract":"We have characterized Schizosaccharomyces pombe open reading frames encoding potential orthologues of constituents of the evolutionarily conserved Saccharomyces cerevisiae Nup84 vertebrate Nup107-160 nuclear pore subcomplex, namely Nup133a, Nup133b, Nup120, Nup107, Nup85, and Seh1. In spite of rather weak sequence conservation, in vivo analyses demonstrated that these S. pombe proteins are localized at the nuclear envelope. Biochemical data confirmed the organization of these nucleoporins within conserved complexes. Although examination of the S. cerevisiae and S. pombe deletion mutants revealed different viability phenotypes, functional studies indicated that the involvement of this complex in nuclear pore distribution and mRNA export has been conserved between these highly divergent yeasts. Unexpectedly, microscopic analyses of some of the S. pombe mutants revealed cell division defects at the restrictive temperature (abnormal septa and mitotic spindles and chromosome missegregation) that were reminiscent of defects occurring in several S. pombe GTPase Ran (Ran(Sp))/Spi1 cycle mutants. Furthermore, deletion of nup120 moderately altered the nuclear location of Ran(Sp)/Spi1, whereas overexpression of a nonfunctional Ran(Sp)/Spi1-GFP allele was specifically toxic in the Deltanup120 and Deltanup133b mutant strains, indicating a functional and genetic link between constituents of the S. pombe Nup107-120 complex and of the Ran(Sp)/Spi1 pathway.","authors":"Baï SW, Rouquette J, Umeda M, Faigle W, Loew D, Sazer S, Doye V","authors_abbrev":"Baï SW et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-07-01","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1486.05","SPAC15F9.02","SPBP35G2.06c","SPAC1805.04","SPBC17G9.04c","SPBC428.01c","SPBC3B9.16c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:16453733","title":"suc1 is an essential gene involved in both the cell cycle and growth in fission yeast.","citation":"EMBO J 1986 Dec 01;5(12):3373-9","abstract":"The gene suc1 encodes a product which suppresses certain temperature sensitive mutants of the cell cycle control gene cdc2 of Schizosaccharomyces pombe. Mutants in the suc1 gene or over-expression of its product leads to delays in mitotic and meiotic nuclear division. Deletion of the suc1 gene is lethal and generates some cells blocked in the cell cycle and others impaired in cellular growth. It is likely that the suc1 gene product binds and forms unstable complexes with the cdc2 protein kinase and with other proteins necessary for the cell cycle and cellular growth. suc1 may have a regulatory role in these processes.","authors":"Hayles J, Aves S, Nurse P","authors_abbrev":"Hayles J et al.","pubmed_publication_date":"01 Dec 1986","pubmed_entrez_date":"1986-12-01","publication_year":"1986","canto_session_key":"24b35cab14100485","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2015-09-06 07:10:29","canto_approved_date":"2026-01-31 16:09:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-25 10:30:00","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[{"name":"Jacky Hayles","community_curator":false,"annotation_count":17,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":10,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.14c","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-06"},{"uniquename":"PMID:3921825","title":"Mutations preventing expression of sup3 tRNASer nonsense suppressors of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1985 Apr;5(4):808-15","abstract":"Suppression of nonsense codons in Schizosaccharomyces pombe by sup3-e tRNASerUGA or sup3-i tRNASerUAA is reduced or abolished by mutations within the suppressor locus. Twenty-five suppressor-inactive sup3-e genes and thirteen mutant sup3-i genes were isolated from S. pombe genomic clone banks by colony hybridization. Sequence analysis of these revertant alleles corroborates genetic evidence for mutational hotspots within the sup3 tRNA gene. Fifteen types of point mutations or insertions were found. Many of these replace bases which are highly or completely conserved in eucaryotic tRNA genes. Transcription of the altered sup3 genes in a Saccharomyces cerevisiae extract enabled the identification of mutations which affect the rate of 5'-end maturation or splicing of the tRNA precursors or both. A total of seven mutations were found which alter transcriptional efficiencies. Of these, five are located outside the internal transcription control regions.","authors":"Pearson D, Willis I, Hottinger H, Bell J, Kumar A, Leupold U, Söll D","authors_abbrev":"Pearson D et al.","pubmed_publication_date":"Apr 1985","pubmed_entrez_date":"1985-04-01","publication_year":"1985","canto_session_key":"30266e1242d44807","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-10-29 15:00:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-29 15:00:20","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPATRNASER.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-10-29"},{"uniquename":"PMID:10734555","title":"[RNA polymerase II from Schizosaccharomyces pombe contains 12 various subunits: identification and characteristics of Rpb4 subunit].","citation":"Bioorg Khim 1999 Dec;25(12):938-42","abstract":"","authors":"Shpakovskiĭ GV, Baranova GM","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"2000-03-29","publication_year":"1999","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16324641","title":"[Repair of and checkpoint response to topoisomerase I-mediated DNA damage in Schizosaccharomyces pombe].","citation":"Med Sci (Paris) 2005 Dec;21(12):1031-3","abstract":"","authors":"Francesconi S","authors_abbrev":"Francesconi S","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-12-06","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21873461","title":"Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases.","citation":"RNA 2011 Oct;17(10):1846-57","abstract":"The N(6)-(isopentenyl)adenosine (i(6)A) modification of some tRNAs at position A37 is found in all kingdoms and facilitates codon-specific mRNA decoding, but occurs in different subsets of tRNAs in different species. Here we examine yeasts' tRNA isopentenyltransferases (i.e., dimethylallyltransferase, DMATase, members of the Δ(2)-isopentenylpyrophosphate transferase, IPPT superfamily) encoded by tit1(+) in Schizosaccharomyces pombe and MOD5 in Saccharomyces cerevisiae, whose homologs are Escherichia coli miaA, the human tumor suppressor TRIT1, and the Caenorhabditis elegans life-span gene product GRO-1. A major determinant of miaA activity is known to be the single-stranded tRNA sequence, A36A37A38, in a stem-loop. tRNA(Trp)(CCA) from either yeast is a Tit1p substrate, but neither is a Mod5p substrate despite the presence of A36A37A38. We show that Tit1p accommodates a broader range of substrates than Mod5p. tRNA(Trp)(CCA) is distinct from Mod5p substrates, which we sort into two classes based on the presence of G at position 34 and other elements. A single substitution of C34 to G converts tRNA(Trp)(CCA) to a Mod5p substrate in vitro and in vivo, consistent with amino acid contacts to G34 in existing Mod5p-tRNA(Cys)(GCA) crystal structures. Mutation of Mod5p in its G34 recognition loop region debilitates it differentially for its G34 (class I) substrates. Multiple alignments reveal that the G34 recognition loop sequence of Mod5p differs significantly from Tit1p, which more resembles human TRIT1 and other DMATases. We show that TRIT1 can also modify tRNA(Trp)(CCA) consistent with broad recognition similar to Tit1p. This study illustrates previously unappreciated molecular plasticity and biological diversity of the tRNA-isopentenyltransferase system of eukaryotes.","doi":"10.1261/rna.2628611","authors":"Lamichhane TN, Blewett NH, Maraia RJ","authors_abbrev":"Lamichhane TN et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-08-30","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-17 18:59:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5441394","title":"[Inositol transport in Schizosaccharomyces pombe].","citation":"Biochim Biophys Acta 1970 Apr 21;203(2):348-50","abstract":"","authors":"Cheneval JP, Deshusses J, Posternak T","authors_abbrev":"Cheneval JP et al.","pubmed_publication_date":"21 Apr 1970","pubmed_entrez_date":"1970-04-21","publication_year":"1970","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23294323","title":"The Kin1 kinase and the calcineurin phosphatase cooperate to link actin ring assembly and septum synthesis in fission yeast.","citation":"Biol Cell 2013 Mar;105(3):129-48","abstract":"The Kin1 protein kinase of fission yeast, which regulates cell surface cohesiveness during interphase cell growth, is also present at the cell division site during mitosis; however, its function in cell division has remained elusive.\nIn FK506-mediated calcineurin deficient cells, mitosis is extended and ring formation is transiently compromised but septation remains normal. Here, we show that Kin1 inhibition in these cells leads to polyseptation and defects in membrane closure. Actomyosin ring disassembly is prevented and ultimately the daughter cells fail to separate. We show that the Pmk1 MAP kinase pathway and the type V myosin Myo4 act downstream of the cytokinetic function of Kin1. Kin1 inhibition also promotes polyseptation in myo3Δ, a type II myosin heavy-chain mutant defective in ring assembly. In contrast, Kin1 inactivation rescues septation in a myosin light-chain cdc4-8 thermosensitive mutant. A structure/function analysis of the Kin1 protein sequence identified a novel motif outside the kinase domain that is important for its polarised localisation and its catalytic activity. This motif is remarkably conserved in all fungal Kin1 homologues but is absent in related kinases of metazoans.\nWe conclude that calcineurin and Kin1 activities must be tightly coordinated to link actomyosin ring assembly with septum synthesis and membrane closure and to ensure separation of the daughter cells.","doi":"10.1111/boc.201200042","authors":"Cadou A, Couturier A, Le Goff C, Xie L, Paulson JR, Le Goff X","authors_abbrev":"Cadou A et al.","pubmed_publication_date":"Mar 2013","pubmed_entrez_date":"2013-01-09","publication_year":"2013","canto_session_key":"82472160ff7e8899","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-03-13 17:02:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPAC4A8.05c","SPBC119.08","SPCC1919.10c","SPAC24B11.06c","SPBC12D12.04c","SPBC1685.01","SPBC543.07","SPAP8A3.08","SPBC4F6.06","SPAC1F3.02c","SPAC17G8.14c"],"gene_count":12,"ltp_gene_count":12},{"uniquename":"PMID:35741449","title":"Dimerization of Firing Factors for Replication Origin Activation in Eukaryotes: A Crucial Process for Simultaneous Assembly of Bidirectional Replication Forks?","citation":"Biology (Basel) 2022 Jun 17;11(6)","abstract":"Controlling the activity of the heterohexameric Mcm2-7 replicative helicase is crucial for regulation of replication origin activity in eukaryotes. Because bidirectional replication forks are generated from every replication origin, when origins are licensed for replication in the first step of DNA replication, two inactive Mcm2-7 heterohexiameric complexes are loaded around double stranded DNA as a head-to-head double hexamer. The helicases are subsequently activated via a 'firing' reaction, in which the Mcm2-7 double hexamer is converted into two active helicase units, the CMG complex, by firing factors. Dimerization of firing factors may contribute to this process by allowing simultaneous activation of two sets of helicases and thus efficient assembly of bidirectional replication forks. An example of this is dimerization of the firing factor Sld3/Treslin/Ticrr via its binding partner, Sld7/MTBP. In organisms in which no Sld7 ortholog has been identified, such as the fission yeast  Schizosaccharomyces pombe , Sld3 itself has a dimerization domain, and it has been suggested that this self-interaction is crucial for the firing reaction in this organism. Dimerization induces a conformational change in Sdl3 that appears to be critical for the firing reaction. Moreover, Mcm10 also seems to be regulated by self-interaction in yeasts. Although it is not yet clear to what extent dimerization of firing factors contributes to the firing reaction in eukaryotes, we discuss the possible roles of firing factor dimerization in simultaneous helicase activation.","doi":"10.3390/biology11060928","authors":"Tanaka S, Ogawa S","authors_abbrev":"Tanaka S et al.","pubmed_publication_date":"17 Jun 2022","pubmed_entrez_date":"2022-06-24","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-06-26 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24848109","title":"Extending the Schizosaccharomyces pombe molecular genetic toolbox.","citation":"PLoS One 2014;9(5):e97683","abstract":"Targeted alteration of the genome lies at the heart of the exploitation of S. pombe as a model system. The rate of analysis is often determined by the efficiency with which a target locus can be manipulated. For most loci this is not a problem, however for some loci, such as fin1+, rates of gene targeting below 5% can limit the scope and scale of manipulations that are feasible within a reasonable time frame. We now describe a simple modification of transformation procedure for directing integration of genomic sequences that leads to a 5-fold increase in the transformation efficiency when antibiotic based dominant selection markers are used. We also show that removal of the pku70+ and pku80+ genes, which encode DNA end binding proteins required for the non-homologous end joining DNA repair pathway, increases the efficiency of gene targeting at fin1+ to around 75-80% (a 16-fold increase). We describe how a natMX6/rpl42+ cassette can be used for positive and negative selection for integration at a targeted locus. To facilitate the evaluation of the impact of a series of mutations on the function of a gene of interest we have generated three vector series that rely upon different selectable markers to direct the expression of tagged/untagged molecules from distinct genomic integration sites. pINTL and pINTK vectors use ura4+ selection to direct disruptive integration of leu1+ and lys1+ respectively, while pINTH vectors exploit nourseothricin resistance to detect the targeted disruption of a hygromycin B resistance conferring hphMX6 cassette that has been integrated on chromosome III. Finally, we have generated a series of multi-copy expression vectors that use resistance to nourseothricin or kanamycin/G418 to select for propagation in prototrophic hosts. Collectively these protocol modifications and vectors extend the versatility of this key model system.","doi":"10.1371/journal.pone.0097683","authors":"Fennessy D, Grallert A, Krapp A, Cokoja A, Bridge AJ, Petersen J, Patel A, Tallada VA, Boke E, Hodgson B, Simanis V, Hagan IM","authors_abbrev":"Fennessy D et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-05-23","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17637568","title":"Spatial regulation of Cdc42 during cytokinesis.","citation":"Cell Cycle 2007 Jul 15;6(14):1687-91","abstract":"Cdc42 GTPase plays a critical role in the establishment of cell polarity in most eukaryotic organisms. Cdc42 active state, as that of other GTPases, depends on the bound nucleotide. The protein with GTP is active, and only in this state can it interact with different target effector proteins. The spatio-temporal control of Cdc42 activity is therefore necessary to generate growth polarity. In fission yeast cells, Cdc42 mainly localizes to the division area, and also to the growing tips and to some internal membranes. While the role of Cdc42 in apical growth is well defined, no role has been described for Cdc42 in the process of cell division. Fission yeast Cdc42 activity is regulated by two specific guanidine nucleotide exchange factors (GEFs), Scd1, and Gef1. We discuss here how Hob3, a BAR domain containing protein similar to human BIN3 and S. cerevisiaeRsv161, may be required to recruit Cdc42 to the cell division site as well as for the activation of this GTPase mediated by Gef1. We also discuss the possible role of Cdc42 in the contraction of the actomyosin ring necessary for cytokinesis.","authors":"Rincon S, Coll PM, Perez P","authors_abbrev":"Rincon S et al.","pubmed_publication_date":"15 Jul 2007","pubmed_entrez_date":"2007-07-20","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40185772","title":"A bifunctional snoRNA with separable activities in guiding rRNA 2'-O-methylation and scaffolding gametogenesis effectors.","citation":"Nat Commun 2025 Apr 05;16(1):3250","abstract":"Small nucleolar RNAs are non-coding transcripts that guide chemical modifications of RNA substrates and modulate gene expression at the epigenetic and post-transcriptional levels. However, the extent of their regulatory potential and the underlying molecular mechanisms remain poorly understood. Here, we identify a conserved, previously unannotated intronic C/D-box snoRNA, termed snR107, hosted in the fission yeast long non-coding RNA mamRNA and carrying two independent cellular functions. On the one hand, snR107 guides site-specific 25S rRNA 2'-O-methylation and promotes pre-rRNA processing and 60S subunit biogenesis. On the other hand, snR107 associates with the gametogenic RNA-binding proteins Mmi1 and Mei2, mediating their reciprocal inhibition and restricting meiotic gene expression during sexual differentiation. Both functions require distinct cis-motifs within snR107, including a conserved 2'-O-methylation guiding sequence. Together, our results position snR107 as a dual regulator of rRNA modification and gametogenesis effectors, expanding our vision on the non-canonical functions exerted by snoRNAs in cell fate decisions.","doi":"10.1038/s41467-025-58664-y","authors":"Leroy E, Challal D, Pelletier S, Goncalves C, Menant A, Marchand V, Jaszczyszyn Y, van Dijk E, Naquin D, Andreani J, Motorin Y, Palancade B, Rougemaille M","authors_abbrev":"Leroy E et al.","pubmed_publication_date":"05 Apr 2025","pubmed_entrez_date":"2025-04-04","publication_year":"2025","canto_session_key":"dcdf06bafb5cb58c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mathieu Rougemaille","canto_first_approved_date":"2025-07-03 08:00:00","canto_approved_date":"2025-12-03 12:23:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-23 13:24:36","canto_added_date":"2025-04-05 23:25:04","annotation_curators":[{"name":"Mathieu Rougemaille","community_curator":true,"annotation_count":118,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":32,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["HGNC:32708","SPBC646.10c","SPAC17A5.02c","SPSNORNA.55","SPAC1556.05c","SPNCRNA.1715","SPBC32H8.11","SPAC1F3.01","SPAC26A3.12c","SPSNORNA.21","HGNC:10105","SPAC23G3.06","SPAC27D7.13c","SPBC216.02","SPNCRNA.103","YNCJ0004C","SPAC12G12.13c","SPAC16C9.04c","SPAC27D7.03c","SPBC2D10.10c","SPCC736.12c","HGNC:33573","SPAC607.03c","SPRRNA.48"],"gene_count":20,"ltp_gene_count":15,"approved_date":"2025-07-03"},{"uniquename":"PMID:1373379","title":"Analysis of the BiP gene and identification of an ER retention signal in Schizosaccharomyces pombe.","citation":"EMBO J 1992 Apr;11(4):1583-91","abstract":"We have cloned the gene for the resident luminal ER protein BiP from the fission yeast, Schizosaccharomyces pombe. The predicted protein product is equally divergent from the budding yeast and mammalian homologues. Disruption of the BiP gene in S. pombe is lethal and BiP mRNA levels are regulated by a variety of stresses including heat shock. Immunofluorescence of cells expressing an epitope-tagged BiP protein show it to be localized to the nuclear envelope, around the cell periphery and in a reticular structure through the cytoplasm. Unexpectedly, we find the BiP protein contains an N-linked glycosylation site which can be utilized. The C-terminal four amino acids of BiP are Ala-Asp-Glu-Leu, a new variant of the XDEL sequence found at the C-termini of luminal endoplasmic reticulum proteins. To determine whether this sequence acts as a sorting signal in S.pombe we expressed an acid phosphatase fusion protein extended at its C-terminus with the amino acids ADEL. Analysis of the sorting of this fusion protein indicates that the ADEL sequence is sufficient to cause the retention of proteins in the endoplasmic reticulum. The sequences DDEL, HDEL and KDEL can also direct ER-retention of acid phosphatase in S.pombe.","authors":"Pidoux AL, Armstrong J","authors_abbrev":"Pidoux AL et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"24f64aba648fcdac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-01-09 17:37:18","canto_approved_date":"2021-04-15 16:30:03","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-12-03 17:01:47","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.15c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-09"},{"uniquename":"PMID:29934426","title":"The organization of genome duplication is a critical determinant of the landscape of genome maintenance.","citation":"Genome Res 2018 Aug;28(8):1179-1192","abstract":"Genome duplication is essential for cell proliferation, and the mechanisms regulating its execution are highly conserved. These processes give rise to a spatiotemporal organization of replication initiation across the genome, referred to as the replication program. Despite the identification of such programs in diverse eukaryotic organisms, their biological importance for cellular physiology remains largely unexplored. We address this fundamental question in the context of genome maintenance, taking advantage of the inappropriate origin firing that occurs when fission yeast cells lacking the Rad3/ATR checkpoint kinase are subjected to replication stress. Using this model, we demonstrate that the replication program quantitatively dictates the extent of origin de-regulation and the clustered localization of these events. Furthermore, our results uncover an accumulation of abnormal levels of single-stranded DNA (ssDNA) and the Rad52 repair protein at de-regulated origins. We show that these loci constitute a defining source of the overall ssDNA and Rad52 hotspots in the genome, generating a signature pattern of instability along the chromosomes. We then induce a genome-wide reprogramming of origin usage and evaluate its consequences in our experimental system. This leads to a complete redistribution of the sites of both inappropriate initiation and associated Rad52 recruitment. We therefore conclude that the organization of genome duplication governs the checkpoint control of origin-associated hotspots of instability and plays an integral role in shaping the landscape of genome maintenance.","doi":"10.1101/gr.224527.117","authors":"Gómez-Escoda B, Wu PJ","authors_abbrev":"Gómez-Escoda B et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-06-24","publication_year":"2018","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2018-06-25 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37991801","title":"POMBOX: A Fission Yeast Cloning Toolkit for Molecular and Synthetic Biology.","citation":"ACS Synth Biol 2023 Nov 22;","abstract":"The fission yeast  Schizosaccharomyces pombe  is a popular model organism in molecular biology and cell physiology. With its ease of genetic manipulation and growth, supported by in-depth functional annotations in the PomBase database and genome-wide metabolic models, S. pombe  is an attractive option for synthetic biology applications. However, S. pombe  currently lacks modular tools for generating genetic circuits with more than 1 transcriptional unit. We developed a toolkit to address this gap. Adapted from the MoClo-YTK plasmid kit for  Saccharomyces cerevisiae  and using the same modular cloning grammar, our POMBOX toolkit is designed to facilitate fast, efficient, and modular construction of genetic circuits in S. pombe . It allows for interoperability when working with DNA sequences that are functional in both S. cerevisiae  and  S. pombe  (e.g., protein tags, antibiotic resistance cassettes, and coding sequences). Moreover, POMBOX enables the modular assembly of multigene pathways and increases the possible pathway length from 6 to 12 transcriptional units. We also adapted the stable integration vector homology arms to Golden Gate assembly and tested the genomic integration success rates depending on different sequence sizes, from 4 to 24 kb. We included 14  S. pombe  promoters that we characterized using two fluorescent proteins, in both minimally defined (EMM2─Edinburgh minimal media) and complex (YES─yeast extract with supplements) media. Then, we examined the efficacy of 6  S. cerevisiae  and 6 synthetic terminators in  S. pombe . Finally, we used the POMBOX kit for a synthetic biology application in metabolic engineering and expressed plant enzymes in  S. pombe  to produce specialized metabolite precursors, namely, methylxanthine, amorpha-4,11-diene, and cinnamic acid from the purine, mevalonate, and aromatic amino acid pathways.","doi":"10.1021/acssynbio.3c00529","authors":"Hebra T, Smrčková H, Elkatmis B, Převorovský M, Pluskal T","authors_abbrev":"Hebra T et al.","pubmed_publication_date":"22 Nov 2023","pubmed_entrez_date":"2023-11-22","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-11-23 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37717872","title":"TORC1 mediated regulation of mitochondrial integrity and calcium ion homeostasis by Wat1/mLst8 in S. pombe.","citation":"Int J Biol Macromol 2023 Dec 31;253(Pt 3):126907","abstract":"The mTOR complexes play a fundamental role in mitochondrial biogenesis and cellular homeostasis. Wat1, an ortholog of mammalian Lst8 is an important component of TOR complex and is essential for the regulation of downstream signaling. Earlier we reported the role of Wat1 in oxidative stress response. Here, we have shown that the abrogation of wat1 causes respiratory defects and mitochondrial depolarization that leads to a decrease in ATP production. The confocal and electron microscopy in wat1Δ cells revealed the fragmented mitochondrial morphology implying its role in mitochondrial fission. Furthermore, we also showed its role in autophagy and the maintenance of calcium ion homeostasis. Additionally, tor2-287 mutant cells also exhibit defects in mitochondrial integrity indicating the TORC1-dependent involvement of Wat1 in the maintenance of mitochondrial homeostasis. The interaction studies of Wat1 and Tor2 with Por1 and Mmm1 proteins revealed a plausible cross-talk between mitochondria and endoplasmic reticulum through the Mitochondria-associated membranes (MAM) and endoplasmic reticulum-mitochondria encounter structure (ERMES) complex, involving TORC1. Taken together, this study demonstrates the involvement of Wat1/mLst8 in harmonizing various mitochondrial functions, redox status, and Ca 2+  homeostasis.","doi":"10.1016/j.ijbiomac.2023.126907","authors":"Anjum S, Srivastava S, Panigrahi L, Ansari UA, Trivedi AK, Ahmed S","authors_abbrev":"Anjum S et al.","pubmed_publication_date":"31 Dec 2023","pubmed_entrez_date":"2023-09-17","publication_year":"2023","canto_session_key":"2f2a248ab93ea5ea","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-09-19 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21B10.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26756885","title":"'An IPTG-inducible derivative of the fission yeast nmt promoter' Soeren Kjaerulff, Olaf Nielsen.","citation":"Yeast 2016 Jan;33(1):33","abstract":"","doi":"10.1002/yea.3136","authors":"","authors_abbrev":"","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2016-01-13","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19160543","title":"HIV-1 Vpr-induced cell death in Schizosaccharomyces pombe is reminiscent of apoptosis.","citation":"Cell Res 2008 Sep;18(9):961-73","abstract":"Human immunodeficiency virus type 1 (HIV-1) Vpr induces cell death in mammalian and fission yeast cells, suggesting that Vpr may affect a conserved cellular process. It is unclear, however, whether Vpr-induced yeast cell death mimics Vpr-mediated apoptosis in mammalian cells. We have recently identified a number of Vpr suppressors that not only suppress Vpr-induced cell death in fission yeast, but also block Vpr-induced apoptosis in mammalian cells. These findings suggest that Vpr-induced cell death in yeast may resemble some of the apoptotic processes of mammalian cells. The goal of this study was to develop and validate a fission yeast model system for future studies of apoptosis. Similar to Vpr-induced apoptosis in mammalian cells, we show here that Vpr in fission yeast promotes phosphatidylserine externalization and induces hyperpolarization of mitochondria, leading to changes of mitochondrial membrane potential. Moreover, Vpr triggers production of reactive oxygen species (ROS), indicating that the apoptotic-like cell death might be mediated by ROS. Interestingly, Vpr induces unique morphologic changes in mitochondria that may provide a simple marker for measuring the apoptotic-like process in fission yeast. To verify this possibility, we tested two Vpr suppressors (EF2 and Hsp16) that suppress Vpr-induced apoptosis in mammalian cells in addition to a newly identified Vpr suppressor (Skp1). All three proteins abolished cell death mediated by Vpr and restored normal mitochondrial morphology in the yeast cells. In conclusion, Vpr-induced cell death in fission yeast resembles the mammalian apoptotic process. Fission yeast may thus potentially be used as a simple model organism for the future study of the apoptotic-like process induced by Vpr and other proapoptotic agents.","doi":"10.1038/cr.2008.272","authors":"Huard S, Chen M, Burdette KE, Fenyvuesvolgyi C, Yu M, Elder RT, Zhao RY","authors_abbrev":"Huard S et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2009-01-23","publication_year":"2008","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35380656","title":"JaponicusDB: rapid deployment of a model organism database for an emerging model species.","citation":"Genetics 2022 Apr 04;220(4)","abstract":"The fission yeast Schizosaccharomyces japonicus has recently emerged as a powerful system for studying the evolution of essential cellular processes, drawing on similarities as well as key differences between S. japonicus and the related, well-established model Schizosaccharomyces pombe. We have deployed the open-source, modular code and tools originally developed for PomBase, the S. pombe model organism database (MOD), to create JaponicusDB (www.japonicusdb.org), a new MOD dedicated to S. japonicus. By providing a central resource with ready access to a growing body of experimental data, ontology-based curation, seamless browsing and querying, and the ability to integrate new data with existing knowledge, JaponicusDB supports fission yeast biologists to a far greater extent than any other source of S. japonicus data. JaponicusDB thus enables S. japonicus researchers to realize the full potential of studying a newly emerging model species and illustrates the widely applicable power and utility of harnessing reusable PomBase code to build a comprehensive, community-maintainable repository of species-relevant knowledge.","doi":"10.1093/genetics/iyab223","authors":"Rutherford KM, Harris MA, Oliferenko S, Wood V","authors_abbrev":"Rutherford KM et al.","pubmed_publication_date":"04 Apr 2022","pubmed_entrez_date":"2022-04-05","publication_year":"2022","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2022-04-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29299619","title":"Intron specificity in pre-mRNA splicing.","citation":"Curr Genet 2018 Aug;64(4):777-784","abstract":"The occurrence of spliceosomal introns in eukaryotic genomes is highly diverse and ranges from few introns in an organism to multiple introns per gene. Introns vary with respect to their lengths, strengths of splicing signals, and position in resident genes. Higher intronic density and diversity in genetically complex organisms relies on increased efficiency and accuracy of spliceosomes for pre-mRNA splicing. Since intron diversity is critical for functions in RNA stability, regulation of gene expression and alternative splicing, RNA-binding proteins, spliceosomal regulatory factors and post-translational modifications of splicing factors ought to make the splicing process intron-specific. We recently reported function and regulation of a ubiquitin fold harboring splicing regulator, Sde2, which following activation by ubiquitin-specific proteases facilitates excision of selected introns from a subset of multi-intronic genes in Schizosaccharomyces pombe (Thakran et al. EMBO J, https://doi.org/10.15252/embj.201796751 , 2017). By reviewing our findings with understandings of intron functions and regulated splicing processes, we propose possible functions and mechanism of intron-specific pre-mRNA splicing and suggest that this process is crucial to highlight importance of introns in eukaryotic genomes.","doi":"10.1007/s00294-017-0802-8","authors":"Mishra SK, Thakran P","authors_abbrev":"Mishra SK et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-01-05","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-01-09 01:15:23","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31G5.18c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21327068","title":"Space shuttling in the cell: nucleocytoplasmic transport and microtubule organization during the cell cycle.","citation":"Nucleus 2010;1(3):231-6","abstract":"Microtubules form a multifunctional filamentous structure essential for the cell. In interphase, microtubules form networks in the cytoplasm and play pivotal roles in cell polarity and intracellular transport of various biomolecules. In mitosis, microtubules dramatically change their morphology to assemble the mitotic spindle, thereby pulling the chromosomes toward the spindle poles. One long-standing question is how microtubules are reorganized upon mitotic entry. Yeast cells undergo closed mitosis, in which the nuclear envelope persists, whereas higher eukaryotes undergo open mitosis, in which the nuclear envelope breaks down. Microtubule reorganization must be controlled by selective localization of microtubule-assembly factors. Recent findings in fission yeast indicate that several microtubule-associated proteins (MAPs) shuttle between the cytoplasm and the nucleus through regulation by Ran GTPase, the universal organizer of nucleocytoplasmic transport. Furthermore, the synergistic interplay of Ran and cyclin-dependent kinase (CDK) induces the critical spatiotemporal shift of modes in microtubule assembly from cytoplasmic arrays to nuclear spindles. A MAP complex Alp7/TACC-Alp14/TOG undergoes nucleocytoplasmic shuttling in interphase, whereas it is retained in the mitotic nucleus through a decrease of its nuclear export by CDK. Our understanding of how microtubules are reorganized during the cell cycle is beginning to emerge.","authors":"Sato M, Toda T","authors_abbrev":"Sato M et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2011-02-18","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39965933","title":"Transcriptomic and proteomic effects of gene deletion are not evolutionarily conserved.","citation":"Genome Res 2025 Feb 18;","abstract":"Although the textbook definition of gene function is the effect for which the gene was selected and/or by which it is maintained, gene function is commonly inferred from the phenotypic effects of deleting the gene. Because some of the deletion effects are byproducts of other effects, they may not reflect the gene's selected-effect function. To evaluate the degree to which the phenotypic effects of gene deletion inform gene function, we compare the transcriptomic and proteomic effects of systematic gene deletions in budding yeast ( Saccharomyces cerevisiae ) with those effects in fission yeast ( Schizosaccharomyces pombe ). Despite evidence for functional conservation of orthologous genes, their deletions result in no more sharing of transcriptomic or proteomic effects than that from deleting non-orthologous genes. Because the wild-type mRNA and protein levels of orthologous genes are significantly correlated between the two yeasts and because transcriptomic effects of deleting the same gene strongly overlap between studies in the same  S. cerevisiae  strain by different laboratories, our observation cannot be explained by rapid evolution or large measurement error of gene expression. Analysis of transcriptomic and proteomic effects of gene deletions in multiple  S. cerevisiae  strains by the same laboratory reveals a high sensitivity of these effects to the genetic background, explaining why these effects are not evolutionarily conserved. Together, our results suggest that most transcriptomic and proteomic effects of gene deletion do not inform selected-effect function. This finding has important implications for assessing and/or understanding gene function, pleiotropy, and biological complexity. .","doi":"10.1101/gr.280008.124","authors":"Li Y, Zhang JG","authors_abbrev":"Li Y et al.","pubmed_publication_date":"18 Feb 2025","pubmed_entrez_date":"2025-02-18","publication_year":"2025","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2025-02-20 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8952948","title":"Cd2+-induced damage to yeast plasma membrane and its alleviation by Zn2+: studies on Schizosaccharomyces pombe cells and reconstituted plasma membrane vesicles.","citation":"Arch Microbiol 1996 Apr;165(4):279-84","abstract":"In Schizosaccharomyces pombe, Cd2+ shares the same uphill uptake system with Zn2+. Both heavy metals inhibited growth, respiration, H+/glucose uptake, and glucose-induced proton extrusion, Cd2+ being a 10-15-fold stronger inhibitor. In contrast, both had a similar effect on the plasma membrane H+-ATPase, enhancing its affinity for ATP and reducing the rate of ATP splitting. Cd2+ caused protracted strong fluidization of the plasma membrane of energized cells, whereas deenergized cells, phosphatidylcholine liposomes, and plasma membrane fragments, either purified or incorporated into the liposomes, exhibited only a short initial fluidization. Zn2+, which caused only a marginal membrane fluidization, suppressed the fluidizing action of Cd2+. The fluidizing effect of both heavy metals on liposomes was reduced by the presence of plasma membrane fragments in the liposome membrane. At 50 &mgr;M, Cd2+ brought about loss K+ (18 K+/1 Cd2+) from energized, but not from deenergized cells since Cd2+ must first accumulate in the cells before causing a detectable effect. A simple membrane disruption by external Cd2+ is, therefore, unlikely to be the main mechanism of cadmium-induced potassium loss in intact cells. Zn2+ had virtually no effect below 1 mM concentration, and it again weakened the K+-releasing effect of Cd2+. Cd2+ caused a strong loss of K+ also from K+-containing liposomes, probably because of a direct interaction with liposome phospholipids. Incorporation of plasma membrane fragments into the liposomes reduced the K+ loss sixfold.","authors":"A&szlig;mann S, Sigler K, H&ouml;fer M","authors_abbrev":"A&szlig;mann S et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16988828","title":"Spatial regulation of cytokinesis by the Kin1 and Pom1 kinases in fission yeast.","citation":"Curr Genet 2006 Dec;50(6):377-91","abstract":"Cytokinesis requires a tight spatio-temporal coordination with mitosis to ensure proper segregation of the genetic information during cell division. In fission yeast, an actomyosin contractile ring is assembled in mitosis and dictates the site of cytokinesis. Here we investigated the functions of Kin1 and Pom1, two conserved fission yeast kinases, in cell division. We found that kin1Delta is synthetically lethal with pom1Delta because double mutant cells fail to spatially organize the actomyosin ring during mitosis, leading to aberrant septum synthesis and accumulation of post-mitotic nuclei in the same cell compartment. Assembly of an Rlc1-GFP ring in the cell center at mitosis is also compromised. Similar cytokinetic defects are observed in a tea1Delta kin1Delta mutant. Furthermore, aberrant septation and nuclear accumulation are observed in a pom1Delta strain in which the Kin1 level is either down or up-regulated. Thus, a tight control of Kin1 level is critical for ensuring accurate cell division in a pom1Delta background. Since none of the kinases can substitute for each other, Kin1 and Pom1 have distinct complementary functions. We show that Kin1 is required for F-actin polarization in interphase and after completion of mitosis and this function may be essential for cytokinesis in a pom1Delta background.","authors":"La Carbona S, Le Goff X","authors_abbrev":"La Carbona S et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-09-22","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1223.06","SPBC4F6.06","SPAC2F7.03c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:33159083","title":"The nuclear pore primes recombination-dependent DNA synthesis at arrested forks by promoting SUMO removal.","citation":"Nat Commun 2020 Nov 06;11(1):5643","abstract":"Nuclear Pore complexes (NPCs) act as docking sites to anchor particular DNA lesions facilitating DNA repair by elusive mechanisms. Using replication fork barriers in fission yeast, we report that relocation of arrested forks to NPCs occurred after Rad51 loading and its enzymatic activity. The E3 SUMO ligase Pli1 acts at arrested forks to safeguard integrity of nascent strands and generates poly-SUMOylation which promote relocation to NPCs but impede the resumption of DNA synthesis by homologous recombination (HR). Anchorage to NPCs allows SUMO removal by the SENP SUMO protease Ulp1 and the proteasome, promoting timely resumption of DNA synthesis. Preventing Pli1-mediated SUMO chains was sufficient to bypass the need for anchorage to NPCs and the inhibitory effect of poly-SUMOylation on HR-mediated DNA synthesis. Our work establishes a novel spatial control of Recombination-Dependent Replication (RDR) at a unique sequence that is distinct from mechanisms engaged at collapsed-forks and breaks within repeated sequences.","doi":"10.1038/s41467-020-19516-z","authors":"Kramarz K, Schirmeisen K, Boucherit V, Ait Saada A, Lovo C, Palancade B, Freudenreich C, Lambert SAE","authors_abbrev":"Kramarz K et al.","pubmed_publication_date":"06 Nov 2020","pubmed_entrez_date":"2020-11-07","publication_year":"2020","canto_session_key":"6a42f3bfbbc08463","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Lambert","canto_first_approved_date":"2020-12-01 12:14:27","canto_approved_date":"2025-09-03 10:53:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-20 15:38:28","canto_added_date":"2020-11-11 01:15:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":64,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sarah Lambert","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC637.10c","SPAC1805.04","SPBC3D6.11c","SPBP35G2.06c","SPAC644.14c","SPAC1556.01c","SPCC338.08","SPAC343.18","SPCC1739.14","SPBC19G7.09","SPAC19A8.10","SPBC365.06","SPAC1687.05","SPBC29A10.05","SPAC30D11.10","SPCC126.02c"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2020-12-01"},{"uniquename":"PMID:1518041","title":"Chromatin structure of Schizosaccharomyces pombe. A nucleosome repeat length that is shorter than the chromatosomal DNA length.","citation":"J Mol Biol 1992 Aug 20;226(4):1009-25","abstract":"We have used new methods for chromatin isolation, together with conventional methods for measuring the nucleosome repeat length, to determine the repeat length of Schizosaccharomyces pombe chromatin. We obtain a result of 156(+/- 2) bp. Equivalent results are obtained using a psoralen crosslinking method for measuring the repeat length in viable spheroplasts. That result, together with other control experiments, rules out many possible artifacts. The measured value of 156(+/- 2) bp is smaller than the length of DNA found in the chromatosome. Thus, the chromatosome cannot be the fundamental unit of chromatin structure in all eukaryotes. The crossed linker model of chromatin higher order structure is incompatible with a nucleosome repeat length of 156 bp, and thus cannot apply to all eukaryotes. The solenoid model of higher order structure is compatible with this repeat length only if the solenoid is right-handed. We note two other properties of this chromatin. (1) Early in digestion, the DNA length of mononucleosomes from S. pombe and Aspergillus nidulans exceeds the nucleosome repeat length. (2) Many methods for isolating chromatin from S. pombe yield an apparent nucleosome repeat length of less than or equal to 140 bp; this result is found to be an artifactual consequence of nucleosome sliding.","authors":"Godde JS, Widom J","authors_abbrev":"Godde JS et al.","pubmed_publication_date":"20 Aug 1992","pubmed_entrez_date":"1992-08-20","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2074269","title":"Mitochondrial growth and DNA synthesis occur in the absence of nuclear DNA replication in fission yeast.","citation":"J Cell Sci 1990 Nov;97 ( Pt 3):509-16","abstract":"Cell growth and division require the doubling of cellular constituents followed by their equal distribution to the two daughter cells. Within a growing population, the ratio of mitochondrial to cellular volume is maintained, as is the number of mitochondrial genomes per cell. The mechanisms responsible for coordinating nuclear and mitochondrial DNA synthesis, and for balancing increases in cell and mitochondrial size are not well understood. In studies of the fission yeast Schizosaccharomyces pombe we quantified cellular and mitochondrial DNA content by both Southern blot analysis and flow cytometry of cells stained with a variety of DNA-binding fluorochromes, which we show are able to detect nuclear and mitochondrial DNA with different efficiencies. In the conditional cell division cycle mutant cdc10, which is unable to initiate nuclear DNA synthesis, we found that there was an increase in the mitochondrial DNA content in the absence of nuclear DNA replication. This demonstrates that mitochondrial and nuclear DNA synthesis are not obligately linked. We also show that mitochondrial DNA replication is not required for the increase in mitochondrial size that occurs as cells elongate, although this results in a decrease in the ratio of mitochondrial DNA to mitochondrial volume.","authors":"Sazer S, Sherwood SW","authors_abbrev":"Sazer S et al.","pubmed_publication_date":"Nov 1990","pubmed_entrez_date":"1990-11-01","publication_year":"1990","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1157826","title":"Germination of Schizosaccharomyces pombe spores separated by zonal centrifugation.","citation":"Exp Cell Res 1975 Jul;93(2):325-30","abstract":"","authors":"Padilla GM, Carter BL, Mitchison JM","authors_abbrev":"Padilla GM et al.","pubmed_publication_date":"Jul 1975","pubmed_entrez_date":"1975-07-01","publication_year":"1975","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19563746","title":"Common ancestry of the CENP-A chaperones Scm3 and HJURP.","citation":"Cell 2009 Jun 26;137(7):1173-4","abstract":"","doi":"10.1016/j.cell.2009.06.010","authors":"Sanchez-Pulido L, Pidoux AL, Ponting CP, Allshire RC","authors_abbrev":"Sanchez-Pulido L et al.","pubmed_publication_date":"26 Jun 2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_session_key":"328a3df08860c6c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 09:47:03","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-20 09:46:55","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:25444","SPAPB1A10.02"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:34005337","canto_session_key":"77487a4301f45921","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-20 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006594","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11685532","title":"A conserved protein, Nuf2, is implicated in connecting the centromere to the spindle during chromosome segregation: a link between the kinetochore function and the spindle checkpoint.","citation":"Chromosoma 2001 Sep;110(5):322-34","abstract":"The centromere is crucial for the proper segregation of chromosomes in all eukaryotic cells. We identified a centromeric protein, Nuf2, which is conserved in fission yeast, human, nematode, and budding yeast. Gene disruption of nuf2+ in the fission yeast Schizosaccharomyces pombe caused defects in chromosome segregation and the spindle checkpoint: the mitotic spindle elongated without segregating the chromosomes, indicating that spindle function was compromised, but that this abnormality did not result in metaphase arrest. Certain nuf2 temperature-sensitive mutations, however, caused metaphase arrest with condensed chromosomes and a short spindle, indicating that, while these mutations caused abnormalities in spindle function, the spindle checkpoint pathway remained intact. Metaphase arrest in these cells was dependent on the spindle checkpoint component Mad2. Interestingly, Nuf2 disappeared from the centromere during meiotic prophase when centromeres lose their connection to the spindle pole body. We propose that Nuf2 acts at the centromere to establish a connection with the spindle for proper chromosome segregation, and that Nuf2 function is also required for the spindle checkpoint.","authors":"Nabetani A, Koujin T, Tsutsumi C, Haraguchi T, Hiraoka Y","authors_abbrev":"Nabetani A et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-10-31","publication_year":"2001","canto_session_key":"0bf9eb6de2606a39","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-11-19 10:32:13","canto_approved_date":"2026-01-29 22:29:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-10 12:38:32","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-11-19"},{"uniquename":"PMID:22380713","title":"Treslin, DUE-B, and GEMC1 cannot complement Sld3 mutants in fission yeast.","citation":"FEMS Yeast Res 2012 Jun;12(4):486-90","abstract":"Initiation of DNA replication in eukaryotes is an evolutionarily conserved process that involves two distinct steps: the formation of prereplication complexes at replication origins in G1 and the assembly of preinitiation complexes (pre-ICs) in S phase, which leads to activation of the replication helicase. For the assembly of pre-ICs in yeast, formation of the Sld2-Dpb11-Sld3 complex is a critical event that requires phosphorylation of Sld2 and Sld3 by cyclin-dependent kinase. In mammals, RecQL4 and TopBP1 are excellent ortholog candidates for Sld2 and Dpb11, respectively. In this past year, three TopBP1-interacting proteins Treslin/Ticrr, GEMC1, and DUE-B have been identified in metazoans as possible functional orthologs of the yeast Sld3. To test this hypothesis, we carried out several complementation tests in fission yeast. The proteins were expressed at various levels in the temperature-sensitive sld3-10 mutant and in cells that lack endogenous Sld3. Our result showed that none of these metazoan proteins could rescue growth defect of the sld3 mutants. Although the result may have several interpretations, it is possible that the helicase activation in mammals has diverged in complexity during evolution from that in yeasts and may involve multiple players that interact with TopBP1.","doi":"10.1111/j.1567-1364.2012.00794.x","authors":"Wang Z, Kim E, Leffak M, Xu YJ","authors_abbrev":"Wang Z et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2012-03-03","publication_year":"2012","canto_session_key":"ceac0db6f64f92b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-03-13 08:27:15","canto_approved_date":"2023-03-13 08:27:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-13 08:26:23","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2023-03-13"},{"uniquename":"PMID:7953561","title":"Meiosis. Telomeres lead chromosome movement.","citation":"Curr Biol 1994 Aug 01;4(8):724-7","abstract":"The telomeres of fission yeast chromosomes are attached to the moving spindle pole body during karyogamy and meiotic prophase. Nuclear movement may also contribute to homologous chromosome pairing.","authors":"Kohli J","authors_abbrev":"Kohli J","pubmed_publication_date":"01 Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29237752","title":"Ser7 of RNAPII-CTD facilitates heterochromatin formation by linking ncRNA to RNAi.","citation":"Proc Natl Acad Sci U S A 2017 Dec 26;114(52):E11208-E11217","abstract":"Some long noncoding RNAs (ncRNAs) transcribed by RNA polymerase II (RNAPII) are retained on chromatin, where they regulate RNAi and chromatin structure. The molecular basis of this retention remains unknown. We show that in fission yeast serine 7 (Ser7) of the C-terminal domain (CTD) of RNAPII is required for efficient siRNA generation for RNAi-dependent heterochromatin formation. Surprisingly, Ser7 facilitates chromatin retention of nascent heterochromatic RNAs (hRNAs). Chromatin retention of hRNAs and siRNA generation requires both Ser7 and an RNA-binding activity of the chromodomain of Chp1, a subunit of the RNA-induced transcriptional silencing (RITS) complex. Furthermore, RITS associates with RNAPII in a Ser7-dependent manner. We propose that Ser7 promotes cotranscriptional chromatin retention of hRNA by recruiting the RNA-chromatin connector protein Chp1, which facilitates RNAi-dependent heterochromatin formation. Our findings reveal a function of the CTD code: linking ncRNA transcription to RNAi for heterochromatin formation.","doi":"10.1073/pnas.1714579115","authors":"Kajitani T, Kato H, Chikashige Y, Tsutsumi C, Hiraoka Y, Kimura H, Ohkawa Y, Obuse C, Hermand D, Murakami Y","authors_abbrev":"Kajitani T et al.","pubmed_publication_date":"26 Dec 2017","pubmed_entrez_date":"2017-12-15","publication_year":"2017","canto_session_key":"bae39dd755f241c3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-12-16 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.11","SPBC28F2.12","SPAC18G6.02c","SPCC188.13c","SPBC428.08c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:7784193","title":"arg3+, a new selection marker system for Schizosaccharomyces pombe: application of ura4+ as a removable integration marker.","citation":"Nucleic Acids Res 1995 May 25;23(10):1836-7","abstract":"","authors":"Waddell S, Jenkins JR","authors_abbrev":"Waddell S et al.","pubmed_publication_date":"25 May 1995","pubmed_entrez_date":"1995-05-25","publication_year":"1995","canto_session_key":"a4f578582cecc86d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-03-20 16:45:19","canto_approved_date":"2023-03-05 15:00:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 22:02:38","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-03-20"},{"uniquename":"PMID:8986778","title":"Identification of fission yeast nuclear markers using random polypeptide fusions with green fluorescent protein.","citation":"Proc Natl Acad Sci U S A 1996 Dec 24;93(26):15146-51","abstract":"We describe a method for identifying genes encoding proteins with stereospecific intracellular localizations in the fission yeast Schizosaccharomyces pombe. Yeast are transformed with a gene library in which S. pombe genomic sequences are fused to the gene encoding the Aequorea victoria green fluorescent protein (GFP), and intracellular localizations are subsequently identified by rapid fluorescence screening in vivo. In a model application of these methods to the fission yeast nucleus, we have identified several novel genes whose products are found in specific nuclear regions, including chromatin, the nucleolus, and the mitotic spindle, and sequence similarities between some of these genes and previously identified genes encoding nuclear proteins have validated the approach. These methods will be useful in identifying additional components of the S. pombe nucleus, and further extensions of this approach should also be applicable to a more comprehensive identification of the elements of intracellular architecture in fission yeast.","authors":"Sawin KE, Nurse P","authors_abbrev":"Sawin KE et al.","pubmed_publication_date":"24 Dec 1996","pubmed_entrez_date":"1996-12-24","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3535918","title":"Yeasts in molecular biology. Spheroplast preparation with Candida utilis, Schizosaccharomyces pombe and Saccharomyces cerevisiae.","citation":"Biosci Rep 1986 Jul;6(7):597-602","abstract":"","authors":"Mann W, Jeffery J","authors_abbrev":"Mann W et al.","pubmed_publication_date":"Jul 1986","pubmed_entrez_date":"1986-07-01","publication_year":"1986","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27053105","title":"Mga2 Transcription Factor Regulates an Oxygen-responsive Lipid Homeostasis Pathway in Fission Yeast.","citation":"J Biol Chem 2016 Jun 03;291(23):12171-83","abstract":"Eukaryotic lipid synthesis is oxygen-dependent with cholesterol synthesis requiring 11 oxygen molecules and fatty acid desaturation requiring 1 oxygen molecule per double bond. Accordingly, organisms evaluate oxygen availability to control lipid homeostasis. The sterol regulatory element-binding protein (SREBP) transcription factors regulate lipid homeostasis. In mammals, SREBP-2 controls cholesterol biosynthesis, whereas SREBP-1 controls triacylglycerol and glycerophospholipid biosynthesis. In the fission yeast Schizosaccharomyces pombe, the SREBP-2 homolog Sre1 regulates sterol homeostasis in response to changing sterol and oxygen levels. However, notably missing is an SREBP-1 analog that regulates triacylglycerol and glycerophospholipid homeostasis in response to low oxygen. Consistent with this, studies have shown that the Sre1 transcription factor regulates only a fraction of all genes up-regulated under low oxygen. To identify new regulators of low oxygen adaptation, we screened the S. pombe nonessential haploid deletion collection and identified 27 gene deletions sensitive to both low oxygen and cobalt chloride, a hypoxia mimetic. One of these genes, mga2, is a putative transcriptional activator. In the absence of mga2, fission yeast exhibited growth defects under both normoxia and low oxygen conditions. Mga2 transcriptional targets were enriched for lipid metabolism genes, and mga2Δ cells showed disrupted triacylglycerol and glycerophospholipid homeostasis, most notably with an increase in fatty acid saturation. Indeed, addition of exogenous oleic acid to mga2Δ cells rescued the observed growth defects. Together, these results establish Mga2 as a transcriptional regulator of triacylglycerol and glycerophospholipid homeostasis in S. pombe, analogous to mammalian SREBP-1.","doi":"10.1074/jbc.M116.723650","authors":"Burr R, Stewart EV, Shao W, Zhao S, Hannibal-Bach HK, Ejsing CS, Espenshade PJ","authors_abbrev":"Burr R et al.","pubmed_publication_date":"03 Jun 2016","pubmed_entrez_date":"2016-04-08","publication_year":"2016","canto_session_key":"c487bc6d6b5cb410","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Risa Burr","canto_first_approved_date":"2017-01-11 16:28:37","canto_approved_date":"2026-01-21 13:43:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-02 14:28:02","canto_added_date":"2016-04-09 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":41,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Risa Burr","community_curator":true,"annotation_count":132,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.09","SPAC17A2.05","SPCP1E11.04c","SPAC22F3.10c","SPAC1687.12c","SPCC1235.02","SPAC6B12.12","SPAC13G7.05","SPAC3G6.05","SPBC3B9.09","SPAC3F10.07c","SPBC146.13c","SPBC3B8.02","SPAC23C11.14","SPBC31F10.09c","SPCC364.06","SPBPJ4664.01","SPAC589.09","SPAC15E1.06","SPCC553.04","SPAC56F8.04c","SPBC4F6.06","SPBC2F12.12c","SPCC162.05","SPCC1281.08","SPAC1610.02c","SPAPJ696.01c","SPAC1486.01","SPCC663.12","SPCC188.13c","SPAC23C11.02c","SPAC4C5.02c","SPBC19G7.17","SPCC594.05c","SPBP4H10.11c","SPAC1002.15c","SPBC56F2.11","SPBC359.02","SPAC222.08c","SPAC30D11.11","SPAC13A11.01c","SPCC830.06","SPAC4G8.11c","SPBC409.20c","SPAC1486.02c","SPAC29A4.20","SPAC4G9.13c","SPBC1778.04","SPAC644.14c","SPAC23H3.13c","SPBC660.10","SPAC4A8.10","SPBC4F6.12","SPBC725.10","SPAC20H4.02","SPBC409.18","SPAC17G6.04c","SPBC18H10.02","SPAC17A2.06c","SPBC646.13","SPAC3A12.12","SPAC5H10.07","SPAC17A2.02c","SPAC56E4.04c","SPAC926.09c","SPBC3H7.09","SPBC27B12.10c","SPBC19C7.02","SPBC23E6.08","SPAC13C5.07","SPAC17G8.05","SPAC24B11.06c","SPAC30.02c","SPBC725.09c","SPBC16A3.03c","SPAC22A12.06c","SPCC736.08","SPCC18.06c","SPAC26H5.05","SPBP35G2.14","SPAC2F3.09","SPAC821.05","SPCC338.08","SPAC1783.02c","SPBP8B7.22","SPCC11E10.04","SPCC1450.16c","SPAC11E3.05","SPAC29B12.04","SPAC4D7.11","SPCC1919.03c","SPBC24C6.05","SPBC409.19c","SPBC359.04c","SPAC9E9.14","SPBC31F10.10c","SPAC4A8.11c","SPAC589.07c","SPBC4B4.03","SPAC4F8.01","SPAC1786.01c","SPAC1142.07c","SPBC646.07c","SPCC777.13","SPAC140.03","SPAC23H4.02","SPBC1198.11c","SPBC36.06c","SPBC4C3.08","SPBC106.10","SPCC1281.06c","SPBC12C2.03c","SPAC1D4.03c","SPAC3H8.05c","SPCC31H12.08c","SPBC1604.03c","SPAC13G6.14","SPAC11G7.02","SPAC1B3.16c","SPCC306.06c","SPAC23C11.04c","SPBC17G9.07","SPBC21C3.01c","SPCC794.07","SPAC824.02","SPBC12D12.07c","SPBC947.10","SPAC13G7.07"],"gene_count":128,"ltp_gene_count":105,"approved_date":"2017-01-11"},{"uniquename":"PMID:16580207","title":"New insights into the control of mRNA decapping.","citation":"Trends Biochem Sci 2006 May;31(5):241-3","abstract":"mRNA decapping irreversibly targets mRNAs for fast decay. Cap removal is catalyzed by decapping protein Dcp2 but also requires Dcp1. Recently, two groups have provided a first glimpse of the regulation mechanism of this crucial step in gene expression. Resolution of the yeast Dcp2 structure has enabled identification of the residues that are important for its interaction with Dcp1. However, the human decapping machinery seems to be more complex because a third component, Hedls, is required for a functional Dcp1-Dcp2 interaction.","authors":"Simon E, Camier S, Séraphin B","authors_abbrev":"Simon E et al.","pubmed_publication_date":"May 2006","pubmed_entrez_date":"2006-04-04","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009814","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26536126","title":"Cell Lysis in S. pombe ura4 Mutants Is Suppressed by Loss of Functional Pub1, Which Regulates the Uracil Transporter Fur4.","citation":"PLoS One 2015;10(11):e0141796","abstract":"Schizosaccharomyces pombe Δura4 cells lyse when grown on YPD medium. A S. pombe non-essential gene deletion library was screened to determine suppressors of the lysis phenotype. Deletion of the pub1 gene, which encoded E3 ubiquitin ligase, strongly suppressed cell lysis in Δura4 cells. The Δpub1 cells displayed high sensitivity to 5-fluorouracil, a toxic analog of uracil, and this sensitivity was suppressed by deletion of fur4, which encoded a uracil transporter. Fur4 localized primarily to the Golgi apparatus and vacuoles in wild-type cells, but localization was predominantly at the plasma membrane in Δpub1 cells. Fur4 was necessary for the utilization of extracellular uracil, cytosine, or UMP. Uracil uptake activity increased in the Δpub1 strain in a Fur4-dependent manner. In addition, uracil starvation was critical for induction of cell lysis of Δura4 strains and uracil supplementation suppressed lysis. In summary, the increased uracil uptake ability of Δpub1 cells, where Fur4 was predominantly localized to the plasma membrane, resulted in suppression of cell lysis in the Δura4 background.","doi":"10.1371/journal.pone.0141796","authors":"Nishino K, Kushima M, Matsuo Y, Matsuo Y, Kawamukai M","authors_abbrev":"Nishino K et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-11-05","publication_year":"2015","canto_session_key":"660a55ae599b5919","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_first_approved_date":"2017-12-07 20:33:46","canto_approved_date":"2022-07-01 08:14:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-17 15:01:05","canto_added_date":"2015-11-06 01:19:32","annotation_curators":[{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11G7.02","SPAC1399.03","SPCC330.05c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-12-07"},{"uniquename":"PMID:12187383","title":"Characterization of the I-Spom I endonuclease from fission yeast: insights into the evolution of a group I intron-encoded homing endonuclease.","citation":"J Mol Evol 2002 Sep;55(3):302-13","abstract":"The first group I intron in the cox1 gene (cox1I1b ) of the mitochondrial genome of the fission yeast Schizosaccharomyces pombe is a mobile DNA element. The mobility is dependent on an endonuclease protein that is encoded by an intronic open reading frame (ORF). The intron-encoded endonuclease is a typical member of the LAGLIDADG protein family of endonucleases with two consensus motifs. In addition to this, analysis of several intron mutants revealed that this protein is required for intron splicing. However, this protein is one of the few group I intron-encoded proteins that functions in RNA splicing simultaneously with its DNA endonuclease activity. We report here on the biochemical characterization of the endonuclease activity of this protein artificially expressed in Escherichia coli. Although the intronic ORF is expressed as a fusion protein with the upstream exon in vivo, the experiments showed that a truncated translation product consisting of the C-terminal 304 codons of the cox1I1b ORF restricted to loop 8 of the intron RNA secondary structure is sufficient for the specific endonuclease activity in vitro. Based on the results, we speculate on the evolution of site-specific homing endonucleases encoded by group I introns in eukaryotes.","authors":"Pellenz S, Harington A, Dujon B, Wolf K, Schäfer B","authors_abbrev":"Pellenz S et al.","pubmed_publication_date":"Sep 2002","pubmed_entrez_date":"2002-08-21","publication_year":"2002","canto_session_key":"bcb665a6909de528","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25404562","title":"Conservation of an intricate circuit for crucial modifications of the tRNAPhe anticodon loop in eukaryotes.","citation":"RNA 2015 Jan;21(1):61-74","abstract":"Post-transcriptional tRNA modifications are critical for efficient and accurate translation, and have multiple different roles. Lack of modifications often leads to different biological consequences in different organisms, and in humans is frequently associated with neurological disorders. We investigate here the conservation of a unique circuitry for anticodon loop modification required for healthy growth in the yeast Saccharomyces cerevisiae. S. cerevisiae Trm7 interacts separately with Trm732 and Trm734 to 2'-O-methylate three substrate tRNAs at anticodon loop residues C₃₂ and N₃₄, and these modifications are required for efficient wybutosine formation at m(1)G₃₇ of tRNA(Phe). Moreover, trm7Δ and trm732Δ trm734Δ mutants grow poorly due to lack of functional tRNA(Phe). It is unknown if this circuitry is conserved and important for tRNA(Phe) modification in other eukaryotes, but a likely human TRM7 ortholog is implicated in nonsyndromic X-linked intellectual disability. We find that the distantly related yeast Schizosaccharomyces pombe has retained this circuitry for anticodon loop modification, that S. pombe trm7Δ and trm734Δ mutants have more severe phenotypes than the S. cerevisiae mutants, and that tRNA(Phe) is the major biological target. Furthermore, we provide evidence that Trm7 and Trm732 function is widely conserved throughout eukaryotes, since human FTSJ1 and THADA, respectively, complement growth defects of S. cerevisiae trm7Δ and trm732Δ trm734Δ mutants by modifying C₃₂ of tRNA(Phe), each working with the corresponding S. cerevisiae partner protein. These results suggest widespread importance of 2'-O-methylation of the tRNA anticodon loop, implicate tRNA(Phe) as the crucial substrate, and suggest that this modification circuitry is important for human neuronal development.","doi":"10.1261/rna.047639.114","authors":"Guy MP, Phizicky EM","authors_abbrev":"Guy MP et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-11-19","publication_year":"2015","canto_session_key":"2c59b84cd1c55d1d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-08-01 17:02:51","canto_approved_date":"2025-07-02 05:36:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-06 05:10:03","canto_added_date":"2014-11-20 01:15:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPATRNAPHE.01","SPBC1306.02","SPAC4F10.03c","SPCC1494.07"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-08-01"},{"uniquename":"PMID:1068110","title":"Genetic studies on cycloheximide-resistant strains of Schizosaccharomyces pombe.","citation":"Heredity (Edinb) 1976 Oct;37(2):179-91","abstract":"Cycloheximide-resistant mutants of Schizosaccharomyces pombe were isolated either as spontaneous mutants or after mutagenic treatment with nitrous acid, UV and N-methyl-N'-nitro-N-nitrosoguanidine (MNNG). Twenty-three spontaneous mutants and 64 induced mutants were analysed genetically. Crosses revealed that at least four loci, designated cyh1, cyh2, cyh3 and cyh4 are responsible for resistance. Alleles of cyh1 show good growth on either high (100 mug/ml) or low (40 mug/ml) concentrations of cycloheximide whereas alleles at the cyh2, cyh3 and cyh4 loci gorw well on 40 mug/ml but poorly on 100 mug/ml. Some alleles at the cyh2 and cyh3 loci are also temperature sensitive (ts), the ts phenotype being conferred by the same gene as the resistance. In diploids, cyh1 and cyh4 are re-essive to wild type whereas cyh2 and cyh3 are semi-dominant. There was no intragenic complementation between three cyh1 alleles. Cross-resistance to trichodermin and anisomycin was shown by cyh2, cyh3 and cyh4 but not cyh1. Most cyh1 alleles, of spontaneous and UV origin only, were cold sensitive (cs) at 14 degrees and some of these were also cycloheximide dependent at the same temperature. It is suggested that the cyh1 and cyh4 genes are involved in ribosome formation or function and the other loci probably affect the uptake of cycloheximide by the cells.","authors":"Ibrahim MA, Coddington A","authors_abbrev":"Ibrahim MA et al.","pubmed_publication_date":"Oct 1976","pubmed_entrez_date":"1976-10-01","publication_year":"1976","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37431652","title":"The joy of the 11th International Fission Yeast Meeting in Hiroshima (POMBE2023 Hiroshima) after a long wait due to the COVID-19 pandemic.","citation":"Genes Cells 2023 Sep;28(9):646-652","abstract":"The 11th International Fission Yeast Meeting took place at Astel Plaza in Hiroshima, Japan, from May 28th to June 2nd, 2023. This highly anticipated gathering, originally scheduled for May 2021, had been postponed for 2 years due to the COVID-19 pandemic. Researchers from 21 countries, including 211 overseas and 157 domestic participants (overall gender ratio is roughly 60% male vs. 40% female), eagerly awaited the opportunity to meet in person, as virtual interactions had been the only means of communication during this challenging period. The meeting featured four kick-off special lectures, 101 regular talks, and 152 poster presentations. Additionally, a discussion session on upfront frontier research in fission yeast provided an interactive platform for both speakers and attendees. Throughout the event, participants shared cutting-edge knowledge, celebrated significant research findings, and relished the invaluable experience of an in-person meeting. The vibrant and friendly atmosphere, characteristic of this esteemed international conference, fostered collaboration and reinforced the significance of studying this exceptional model organism. Undoubtedly, the outcomes of this meeting will greatly contribute to our understanding of complex biological systems, not only in fission yeast but also in general eukaryotes.","doi":"10.1111/gtc.13055","authors":"Toda T, Kitamura K, Kume K, Yukawa M, Koyano T, Ueno M","authors_abbrev":"Toda T et al.","pubmed_publication_date":"Sep 2023","pubmed_entrez_date":"2023-07-11","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-07-12 00:15:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10850973","title":"Tol1, a fission yeast phosphomonoesterase, is an in vivo target of lithium, and its deletion leads to sulfite auxotrophy.","citation":"J Bacteriol 2000 Jul;182(13):3619-25","abstract":"Lithium is the drug of choice for the treatment of bipolar affective disorder. The identification of an in vivo target of lithium in fission yeast as a model organism may help in the understanding of lithium therapy. For this purpose, we have isolated genes whose overexpression improved cell growth under high LiCl concentrations. Overexpression of tol1(+), one of the isolated genes, increased the tolerance of wild-type yeast cells for LiCl but not for NaCl. tol1(+) encodes a member of the lithium-sensitive phosphomonoesterase protein family, and it exerts dual enzymatic activities, 3'(2'),5'-bisphosphate nucleotidase and inositol polyphosphate 1-phosphatase. tol1(+) gene-disrupted cells required high concentrations of sulfite in the medium for growth. Consistently, sulfite repressed the sulfate assimilation pathway in fission yeast. However, tol1(+) gene-disrupted cells could not fully recover from their growth defect and abnormal morphology even when the medium was supplemented with sulfite, suggesting the possible implication of inositol polyphosphate 1-phosphatase activity for cell growth and morphology. Given the remarkable functional conservation of the lithium-sensitive dual-specificity phosphomonoesterase between fission yeast and higher-eukaryotic cells during evolution, it may represent a likely in vivo target of lithium action across many species.","authors":"Miyamoto R, Sugiura R, Kamitani S, Yada T, Lu Y, Sio SO, Asakura M, Matsuhisa A, Shuntoh H, Kuno T","authors_abbrev":"Miyamoto R et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-06-13","publication_year":"2000","canto_session_key":"b42cb21b34629e92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-15 16:12:29","canto_approved_date":"2023-05-15 13:11:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-14 15:45:54","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1753.04","SPAC977.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-10-15"},{"uniquename":"PMID:28631612","title":" wtf  genes are prolific dual poison-antidote meiotic drivers.","citation":"Elife 2017 Jun 20;6","abstract":"Meiotic drivers are selfish genes that bias their transmission into gametes, defying Mendelian inheritance. Despite the significant impact of these genomic parasites on evolution and infertility, few meiotic drive loci have been identified or mechanistically characterized. Here, we demonstrate a complex landscape of meiotic drive genes on chromosome 3 of the fission yeasts  Schizosaccharomyces kambucha  and  S. pombe . We identify  S. kambucha wtf4  as one of these genes that acts to kill gametes (known as spores in yeast) that do not inherit the gene from heterozygotes.  wtf4  utilizes dual, overlapping transcripts to encode both a gamete-killing poison and an antidote to the poison. To enact drive, all gametes are poisoned, whereas only those that inherit  wtf4  are rescued by the antidote. Our work suggests that the  wtf  multigene family proliferated due to meiotic drive and highlights the power of selfish genes to shape genomes, even while imposing tremendous costs to fertility.","doi":"10.7554/eLife.26033","authors":"Nuckolls NL, Bravo Núñez MA, Eickbush MT, Young JM, Lange JJ, Yu JS, Smith GR, Jaspersen SL, Malik HS, Zanders SE","authors_abbrev":"Nuckolls NL et al.","pubmed_publication_date":"20 Jun 2017","pubmed_entrez_date":"2017-06-21","publication_year":"2017","canto_session_key":"06d77d7ac3f77bbc","canto_annotation_status":"APPROVED","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-04-16 15:10:33","canto_approved_date":"2021-12-22 12:03:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-16 15:10:27","canto_added_date":"2017-06-22 00:15:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC548.03c","SPCC663.02"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2020-04-16"},{"uniquename":"PMID:34738170","title":"Overexpression of cell-wall GPI-anchored proteins restores cell growth of N-glycosylation-defective och1 mutants in Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2021 Dec;105(23):8771-8781","abstract":"The glycoproteins of yeast contain a large outer chain on N-linked oligosaccharides; therefore, yeast is not suitable for producing therapeutic glycoproteins for human use. Using a deletion mutant strain of α1,6-mannosyltransferase (och1Δ), we previously produced humanized N-glycans in fission yeast; however, the Schizosaccharomyces pombe och1Δ cells displayed a growth delay even during vegetative growth, resulting in reduced productivity of heterologous proteins. To overcome this problem, here we performed a genome-wide screen for genes that would suppress the growth defect of temperature-sensitive och1Δ cells. Using a genomic library coupled with screening of 18,000 transformants, we identified two genes (pwp1 + , SPBC1E8.05), both encoding GPI-anchored proteins, that increased the growth rate of och1Δ cells, lacking the outer chain. We further showed that a high copy number of the genes was needed to improve the growth rate. Mutational analysis of Pwp1p revealed that the GPI-anchored region of Pwp1p is important in attenuating the growth defect. Analysis of disruptants of pwp1 +  and SPBC1E8.05 showed that neither gene was essential for cell viability; however, both mutants were sensitive β-glucanase, suggesting that Pwp1p and the protein encoded by SPBC1E8.05 non-enzymatically support β-glucan on the cell-surface of S. pombe. Collectively, our work not only sheds light on the functional relationships between GPI-anchored proteins and N-linked oligosaccharides of glycoproteins in S. pombe, but also supports the application of S. pombe to the production of human glycoprotein. KEY POINTS: • We screened for genes that suppress the growth defect of fission yeast och1Δ cells. • Appropriate expression of GPI-anchored proteins alleviates the growth delay of och1Δ cells. • The GPI-anchor domain of Pwp1p is important for suppressing the growth defect of och1Δ cells.","doi":"10.1007/s00253-021-11649-5","authors":"Fukunaga T, Sakurai Y, Ohashi T, Higuchi Y, Maekawa H, Takegawa K","authors_abbrev":"Fukunaga T et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-11-05","publication_year":"2021","canto_session_key":"4ac0ce427dd07a35","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-08-31 15:42:25","canto_approved_date":"2023-03-14 14:28:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-11-18 07:49:28","canto_added_date":"2021-11-07 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.05c","SPBC1A4.03c","SPCC1322.11","SPCC1322.10","SPBC1A4.01","SPCC1322.12c","SPBC1E8.05"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2022-08-31"},{"uniquename":"PMID:19158488","title":"All eukaryotes: before turning off G1-S transcription, please check your DNA.","citation":"Cell Cycle 2009 Jan 15;8(2):214-7","abstract":"The DNA replication and DNA damage checkpoints are required for the efficient response to genotoxic stress, which is critical for genome stability and cell survival. The DNA replication and damage checkpoints delay progression into mitosis, and at the same time induce the transcription of genes that promote repair of cellular lesions including stabilization of stalled replication forks and induction of DNA repair functions. The elucidation of the mechanism by which the DNA replication checkpoint activates transcription of G1/S genes is provided by our recent study reported in the August issue of Proceedings of the National Academy of Sciences. We show that, in response to stimulation of the DNA replication checkpoint, activation of G1-S transcription is established by inactivation, via phosphorylation by the checkpoint protein kinases, of the MBF-associated transcriptional corepressor Nrm1. This regulation is critical for the survival of cells responding to genotoxic stress. This provides a simple but elegant mechanism by which checkpoint activation can override the regular periodic transcriptional program by directly regulating a cell cycle dependent transcriptional repressor. We discuss the likely conservation of this regulatory pathway in yeast and man.","authors":"de Bruin RA, Wittenberg C","authors_abbrev":"de Bruin RA et al.","pubmed_publication_date":"15 Jan 2009","pubmed_entrez_date":"2009-01-23","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37910512","title":"Protocol for detecting threonine deaminase activity in fission yeast cell lysates.","citation":"STAR Protoc 2023 Oct 31;4(4):102675","abstract":"Threonine deaminase catalyzes the first step of isoleucine biosynthesis from threonine. In this protocol, we describe the process of measuring the enzymatic activity of threonine deaminase in the fission yeast cell lysate, which is catalyzed by Tda1. First, we describe the process of preparing cell lysates from fission yeast cell cultures. Subsequently, we explain how to measure the threonine deaminase activity using threonine or serine as a substrate. For complete details on the use and execution of this protocol, please refer to Sasaki et al. (2022). 1 .","doi":"10.1016/j.xpro.2023.102675","authors":"Sasaki M, Nishimura S, Matsuyama A, Yoshida M","authors_abbrev":"Sasaki M et al.","pubmed_publication_date":"31 Oct 2023","pubmed_entrez_date":"2023-11-01","publication_year":"2023","canto_session_key":"216300e88b20d04f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-11-02 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14622279","title":"Comparative importance in vivo of conserved glutamate residues in the EX7E motif retaining glycosyltransferase Gpi3p, the UDP-GlcNAc-binding subunit of the first enzyme in glycosylphosphatidylinositol assembly.","citation":"Eur J Biochem 2003 Nov;270(22):4507-14","abstract":"Saccharomyces cerevisiae Gpi3p is the UDP-GlcNAc-binding and presumed catalytic subunit of the enzyme that forms GlcNAc-phosphatidylinositol in glycosylphosphatidylinositol biosynthesis. It is an essential protein with an EX7E motif that is conserved in four families of retaining glycosyltransferases. All Gpi3ps contain a cysteine residue four residues C-terminal to EX7E. To test their importance for Gpi3p function in vivo, Glu289 and 297 in the EX7E motif of S. cerevisiae Gpi3p, as well as Cys301, were altered by site-specific mutagenesis, and the mutant proteins tested for their ability to complement nonviable GPI3-deleted haploids. Gpi3p-C301A supported growth but membranes from C301A-expressing cells had low in vitro N-acetylglucosaminylphosphatidylinositol (GlcNAc-PI) synthetic activity. Haploids harboring Gpi3p-E289A proved viable, although slow growing but Gpi3-E297A did not support growth. The E289D and E297D mutants both supported growth at 25 degrees C, but, whereas the E289D strain grew at 37 degrees C, the E297D mutant did not. Membranes from E289D mutants had severely reduced in vitro GlcNAc-PI synthetic activity and E297D membranes had none. The mutation of the first Glu in the EX7E motif of Schizosaccharomyces pombe Gpi3p (Glu277) to Asp complemented the lethal null mutation in gpi3+ and supported growth at 37 degrees C, but the E285D mutant was nonviable. Our results suggest that the second Glu residue of the EX7E motif in Gpi3p is of greater importance than the first for function in vivo. Further, our findings do not support previous suggestions that the first Glu of an EX7E protein is the nucleophile and that Cys301 has an important role in UDP-GlcNAc binding by Gpi3ps.","authors":"Kostova Z, Yan BC, Vainauskas S, Schwartz R, Menon AK, Orlean P","authors_abbrev":"Kostova Z et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-11-19","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26831106","title":"Chimera proteins with affinity for membranes and microtubule tips polarize in the membrane of fission yeast cells.","citation":"Proc Natl Acad Sci U S A 2016 Feb 16;113(7):1811-6","abstract":"Cell polarity refers to a functional spatial organization of proteins that is crucial for the control of essential cellular processes such as growth and division. To establish polarity, cells rely on elaborate regulation networks that control the distribution of proteins at the cell membrane. In fission yeast cells, a microtubule-dependent network has been identified that polarizes the distribution of signaling proteins that restricts growth to cell ends and targets the cytokinetic machinery to the middle of the cell. Although many molecular components have been shown to play a role in this network, it remains unknown which molecular functionalities are minimally required to establish a polarized protein distribution in this system. Here we show that a membrane-binding protein fragment, which distributes homogeneously in wild-type fission yeast cells, can be made to concentrate at cell ends by attaching it to a cytoplasmic microtubule end-binding protein. This concentration results in a polarized pattern of chimera proteins with a spatial extension that is very reminiscent of natural polarity patterns in fission yeast. However, chimera levels fluctuate in response to microtubule dynamics, and disruption of microtubules leads to disappearance of the pattern. Numerical simulations confirm that the combined functionality of membrane anchoring and microtubule tip affinity is in principle sufficient to create polarized patterns. Our chimera protein may thus represent a simple molecular functionality that is able to polarize the membrane, onto which additional layers of molecular complexity may be built to provide the temporal robustness that is typical of natural polarity patterns.","doi":"10.1073/pnas.1419248113","authors":"Recouvreux P, Sokolowski TR, Grammoustianou A, ten Wolde PR, Dogterom M","authors_abbrev":"Recouvreux P et al.","pubmed_publication_date":"16 Feb 2016","pubmed_entrez_date":"2016-02-03","publication_year":"2016","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-04 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16972065","title":"The fission yeast Rpb4 subunit of RNA polymerase II plays a specialized role in cell separation.","citation":"Mol Genet Genomics 2006 Dec;276(6):545-54","abstract":"RNA polymerase II is a complex of 12 subunits, Rpb1 to Rpb12, whose specific roles are only partly understood. Rpb4 is essential in mammals and fission yeast, but not in budding yeast. To learn more about the roles of Rpb4, we expressed the rpb4 gene under the control of regulatable promoters of different strength in fission yeast. We demonstrate that below a critical level of transcription, Rpb4 affects cellular growth proportional to its expression levels: cells expressing lower levels of rpb4 grew slower compared to cells expressing higher levels. Lowered rpb4 expression did not affect cell survival under several stress conditions, but it caused specific defects in cell separation similar to sep mutants. Microarray analysis revealed that lowered rpb4 expression causes a global reduction in gene expression, but the transcript levels of a distinct subset of genes were particularly responsive to changes in rpb4 expression. These genes show some overlap with those regulated by the Sep1-Ace2 transcriptional cascade required for cell separation. Most notably, the gene expression signature of cells with lowered rpb4 expression was highly similar to those of mcs6, pmh1, sep10 and sep15 mutants. Mcs6 and Pmh1 encode orthologs of metazoan TFIIH-associated cyclin-dependent kinase (CDK)-activating kinase (Cdk7-cyclin H-Mat1), while Sep10 and Sep15 encode mediator components. Our results suggest that Rpb4, along with some other general transcription factors, plays a specialized role in a transcriptional pathway that controls the cell cycle-regulated transcription of a specific subset of genes involved in cell division.","authors":"Sharma N, Marguerat S, Mehta S, Watt S, Bähler J","authors_abbrev":"Sharma N et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-09-15","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC337.14"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:19948143","title":"Cytokinesis: Closure resets your SIN.","citation":"Curr Biol 2009 Dec 01;19(22):R1040-2","abstract":"A new study of fission yeast cell division has revealed a coupling between cytoplasmic partitioning and the turning-off of cytokinesis signalling that may be mediated by asymmetric protein distribution.","doi":"10.1016/j.cub.2009.10.012","authors":"Lattmann E, Krapp A, Simanis V","authors_abbrev":"Lattmann E et al.","pubmed_publication_date":"01 Dec 2009","pubmed_entrez_date":"2009-12-02","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23098598","title":"Closed mitosis: A timely move before separation.","citation":"Curr Biol 2012 Oct 23;22(20):R880-2","abstract":"Faithful chromosome segregation entails long-range chromosome movement into newly dividing cells. A recent study implicates CDK1 function in releasing mitotic telomeres from the nuclear envelope, thereby liberating chromosomes for mitotic segregation.","doi":"10.1016/j.cub.2012.08.034","authors":"Ebrahimi H, Cooper JP","authors_abbrev":"Ebrahimi H et al.","pubmed_publication_date":"23 Oct 2012","pubmed_entrez_date":"2012-10-27","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3010354","title":"Vectors for the construction of gene banks and the integration of cloned genes in Schizosaccharomyces pombe and Saccharomyces cerevisiae.","citation":"Plasmid 1986 Mar;15(2):156-8","abstract":"We have constructed a variety of vectors for use in both budding yeast (Saccharomyces cerevisiae) and fission yeast (Schizosaccharomyces pombe). Four of these, pDB262, pWH4, pWH5, and pMAK262, have positive selection for the insertion of cloned DNA, making them convenient for the construction of gene banks. pDB262, pWH4 and pWH5 contain the 2 mu ARS and the LEU2 gene from S. cerevisiae and can be used for gene isolation. They can also be converted into integration vectors for use in the genetic mapping of cloned sequences. pMAK262 contains only the LEU2 gene from budding yeast and can be used to screen for ARS elements or for gene integration. We also describe two other integration vectors, pDAM3 and pDAM6, which have a variety of restriction sites suitable for subcloning.","authors":"Wright A, Maundrell K, Heyer WD, Beach D, Nurse P","authors_abbrev":"Wright A et al.","pubmed_publication_date":"Mar 1986","pubmed_entrez_date":"1986-03-01","publication_year":"1986","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:L49134","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39337578","title":"Differential Cytoophidium Assembly between  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe .","citation":"Int J Mol Sci 2024 Sep 19;25(18)","abstract":"The de novo synthesis of cytidine 5'-triphosphate (CTP) is catalyzed by the enzyme CTP synthase (CTPS), which is known to form cytoophidia across all three domains of life. In this study, we use the budding yeast  Saccharomyces cerevisiae  and the fission yeast  Schizosaccharomyces pombe  as model organisms to compare cytoophidium assembly under external environmental and intracellular CTPS alterations. We observe that under low and high temperature conditions, cytoophidia in fission yeast gradually disassemble, while cytoophidia in budding yeast remain unaffected. The effect of pH changes on cytoophidia maintenance in the two yeast species is different. When cultured in the yeast-saturated cultured medium, cytoophidia in fission yeast disassemble, while cytoophidia in budding yeast gradually form. Overexpression of CTPS results in the presence and maintenance of cytoophidia in both yeast species from the log phase to the stationary phase. In summary, our results demonstrate differential cytoophidium assembly between  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe , the two most studied yeast species.","doi":"10.3390/ijms251810092","authors":"Deng R, Li YL, Liu JL","authors_abbrev":"Deng R et al.","pubmed_publication_date":"19 Sep 2024","pubmed_entrez_date":"2024-09-28","publication_year":"2024","canto_session_key":"e88ba9cd92388369","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-09-29 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC10F6.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10684278","title":"Genetic studies with the fission yeast Schizosaccharomyces pombe suggest involvement of wee1, ppa2, and rad24 in induction of cell cycle arrest by human immunodeficiency virus type 1 Vpr.","citation":"J Virol 2000 Mar;74(6):2636-46","abstract":"Accessory protein Vpr of human immunodeficiency virus type 1 (HIV-1) arrests cell cycling at G(2)/M phase in human and simian cells. Recently, it has been shown that Vpr also causes cell cycle arrest in the fission yeast Schizosaccharomyces pombe, which shares the cell cycle regulatory mechanisms with higher eukaryotes including humans. In this study, in order to identify host cellular factors involved in Vpr-induced cell cycle arrest, the ability of Vpr to cause elongated cellular morphology (cdc phenotype) typical of G(2)/M cell cycle arrest in wild-type and various mutant strains of S. pombe was examined. Our results indicated that Vpr caused the cdc phenotype in wild-type S. pombe as well as in strains carrying mutations, such as the cdc2-3w, Deltacdc25, rad1-1, Deltachk1, Deltamik1, and Deltappa1 strains. However, other mutants, such as the cdc2-1w, Deltawee1, Deltappa2, and Deltarad24 strains, failed to show a distinct cdc phenotype in response to Vpr expression. Results of these genetic studies suggested that Wee1, Ppa2, and Rad24 might be required for induction of cell cycle arrest by HIV-1 Vpr. Cell proliferation was inhibited by Vpr expression in all of the strains examined including the ones that did not show the cdc phenotype. The results supported the previously suggested possibility that Vpr affects the cell cycle and cell proliferation through different pathways.","authors":"Masuda M, Nagai Y, Oshima N, Tanaka K, Murakami H, Igarashi H, Okayama H","authors_abbrev":"Masuda M et al.","pubmed_publication_date":"Mar 2000","pubmed_entrez_date":"2000-02-23","publication_year":"2000","canto_session_key":"912779b70ccb0c4b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2016-09-14 12:41:47","canto_approved_date":"2019-06-14 13:03:32","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-09-14 12:41:28","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05","SPBC660.14","SPBC11B10.09","SPBC16H5.07c"],"gene_count":5,"ltp_gene_count":0,"approved_date":"2016-09-14"},{"uniquename":"EMBL:AB084851","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.39"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26007660","title":"DNA3'pp5'G de-capping activity of aprataxin: effect of cap nucleoside analogs and structural basis for guanosine recognition.","citation":"Nucleic Acids Res 2015 Jul 13;43(12):6075-83","abstract":"DNA3'pp5'G caps synthesized by the 3'-PO4/5'-OH ligase RtcB have a strong impact on enzymatic reactions at DNA 3'-OH ends. Aprataxin, an enzyme that repairs A5'pp5'DNA ends formed during abortive ligation by classic 3'-OH/5'-PO4 ligases, is also a DNA 3' de-capping enzyme, converting DNAppG to DNA3'p and GMP. By taking advantage of RtcB's ability to utilize certain GTP analogs to synthesize DNAppN caps, we show that aprataxin hydrolyzes inosine and 6-O-methylguanosine caps, but is not adept at removing a deoxyguanosine cap. We report a 1.5 Å crystal structure of aprataxin in a complex with GMP, which reveals that: (i) GMP binds at the same position and in the same anti nucleoside conformation as AMP; and (ii) aprataxin makes more extensive nucleobase contacts with guanine than with adenine, via a hydrogen bonding network to the guanine O6, N1, N2 base edge. Alanine mutations of catalytic residues His147 and His149 abolish DNAppG de-capping activity, suggesting that the 3' de-guanylylation and 5' de-adenylylation reactions follow the same pathway of nucleotidyl transfer through a covalent aprataxin-(His147)-NMP intermediate. Alanine mutation of Asp63, which coordinates the guanosine ribose hydroxyls, impairs DNAppG de-capping.","doi":"10.1093/nar/gkv501","authors":"Chauleau M, Jacewicz A, Shuman S","authors_abbrev":"Chauleau M et al.","pubmed_publication_date":"13 Jul 2015","pubmed_entrez_date":"2015-05-27","publication_year":"2015","canto_session_key":"2f654283915413d8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-01-05 19:20:08","canto_approved_date":"2024-07-02 13:14:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-01-05 19:20:01","canto_added_date":"2015-10-28 01:19:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-01-05","pdb_entries":[{"pdb_id":"4xba","gene_chains":[{"gene_uniquename":"SPCC18.09c","chain":"A/B","position":"33-232"}],"title":"Hnt3","entry_authors":"Jacewicz A,Chauleau M,Shuman S","entry_authors_abbrev":"Jacewicz A et al.","reference_uniquename":"PMID:26007660","experimental_method":"X-ray","resolution":"1.5"},{"pdb_id":"4ykl","gene_chains":[{"gene_uniquename":"SPCC18.09c","chain":"B","position":"33-232"}],"title":"Hnt3 in complex with DNA and guanosine","entry_authors":"Jacewicz A,Chauleau M,Shuman S","entry_authors_abbrev":"Jacewicz A et al.","reference_uniquename":"PMID:26007660","experimental_method":"X-ray","resolution":"2.25"}]},{"uniquename":"PMID:7425782","title":"Lysis of growing fissin-yeast cells induced by aculeacin A, a new antifungal antibiotic.","citation":"Arch Microbiol 1980 Aug;127(1):11-6","abstract":"Cells of Schizosaccharomyces pombe grown in the presence of aculeacin A, a peptide antibiotic, were lysed resulting the death of cells. Under high osmolarity, the cellular lysis induced by aculeacin A was considerably reduced. The use of synchronous-culture systems distinguished cell elongation from cell division revealed that the sites of aculeacin A-induced lysis on the fission yeast were the end(s) and the cell plate region, corresponded to the regions of the cell wall synthesis. Aculeacin A-resistant survivors exhibited morphological alterations which were swollen at one or both ends of the cell and appeared drumstick or dumbbel like; the wall of the bulge region was observed to be stained with a fluorescent brightner, as well as that of the cell plate region. These effects of aculeacin A are discussed as compared with effects of 2-deoxy-D-glucose.","authors":"Miyata M, Kitamura J, Miyata H","authors_abbrev":"Miyata M et al.","pubmed_publication_date":"Aug 1980","pubmed_entrez_date":"1980-08-01","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11514435","title":"Coordination between fission yeast glucan formation and growth requires a sphingolipase activity.","citation":"Genetics 2001 Aug;158(4):1397-411","abstract":"css1 mutants display a novel defect in Schizosaccharomyces pombe cell wall formation. The mutant cells are temperature-sensitive and accumulate large deposits of material that stain with calcofluor and aniline blue in their periplasmic space. Biochemical analyses of this material indicate that it consists of alpha- and beta-glucans in the same ratio as found in cell walls of wild-type S. pombe. Strikingly, the glucan deposits in css1 mutant cells do not affect their overall morphology. The cells remain rod shaped, and the thickness of their walls is unaltered. Css1p is an essential protein related to mammalian neutral sphingomyelinase and is responsible for the inositolphosphosphingolipid-phospholipase C activity observed in S. pombe membranes. Furthermore, expression of css1(+) can compensate for loss of ISC1, the enzyme responsible for this activity in Saccharomyces cerevisiae membranes. Css1p localizes to the entire plasma membrane and secretory pathway; a C-terminal fragment of Css1p, predicted to encode a single membrane-spanning segment, is sufficient to direct membrane localization of the heterologous protein, GFP. Our results predict the existence of an enzyme(s) or process(es) essential for the coordination of S. pombe cell wall formation and division that is, in turn, regulated by a sphingolipid metabolite.","authors":"Feoktistova A, Magnelli P, Abeijon C, Perez P, Lester RL, Dickson RC, Gould KL","authors_abbrev":"Feoktistova A et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-08-22","publication_year":"2001","canto_session_key":"ea75ccdaa88fc91d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-12-04 20:54:29","canto_approved_date":"2022-02-23 12:02:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-27 18:17:28","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-12-04"},{"uniquename":"PMID:22207359","title":"DNA replication, RNAi and epigenetic inheritance.","citation":"Epigenetics 2012 Jan 01;7(1):14-9","abstract":"Epigenetic marks, such as histone methylation, play a central role in chromatin structure and gene expression. During DNA replication, chromatin undergoes a wave of disruption and reassembly. Little is known about how the epigenetic marks are faithfully inherited from one generation to the next. In fission yeast, the hallmark of heterochromatin, a condensed chromatin structure, is H3K9 methylation. This conserved epigenetic mark is mediated by small interference RNAs (siRNAs) in a cell cycle-dependent manner: at S phase, heterochromatin is briefly transcribed by RNAP II and the transcripts are subsequently processed into siRNAs. These small RNAs, together with other key silencing factors, including Dos1/Raf1/Clr8/Cmc1, Dos2/Raf2/Clr7/Cmc2 and Rik1, mediate H3K9 methylation by the histone H3K9 methyltransferase Clr4. Our recent findings indicate that the ε subunit of DNA polymerase, Cdc20, associates with the Dos2-Rik1 complex and is essential for H3K9 methylation and heterochromatin function. Moreover, Cdc20 regulates siRNA generation by promoting RNAP II transcription of heterochromatin. These data suggest that DNA polymerase components may play a key role in the inheritance of histone methylation by coordinating DNA replication, RNAi and histone methylation, and explain previously observed cell cycle-regulated RNAi-dependent heterochromatin silencing. We propose a model in which, at DNA replication forks, DNA polymerase subunits mediate the recruitment of epigenetic factors required for RNAi and histone modification to heterochromatin to promote the faithful transmission of histone methylation.","doi":"10.4161/epi.7.1.18545","authors":"Gonzalez M, Li F","authors_abbrev":"Gonzalez M et al.","pubmed_publication_date":"01 Jan 2012","pubmed_entrez_date":"2011-12-31","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33378677","title":"Quality-Control Mechanism for Telomerase RNA Folding in the Cell.","citation":"Cell Rep 2020 Dec 29;33(13):108568","abstract":"Long non-coding RNAs can often fold into different conformations. Telomerase RNA, an essential component of the telomerase ribonucleoprotein (RNP) enzyme, must fold into a defined structure to fulfill its function with the protein catalytic subunit (TERT) and other accessory factors. However, the mechanism by which the correct folding of telomerase RNA is warranted in a cell is still unknown. Here we show that La-related protein Pof8 specifically recognizes the conserved pseudoknot region of telomerase RNA and instructs the binding of the Lsm2-8 complex to its mature 3' end, thus selectively protecting the correctly folded RNA from exonucleolytic degradation. In the absence of Pof8, TERT assembles with misfolded RNA and produces little telomerase activity. Therefore, Pof8 plays a key role in telomerase RNA folding quality control, ensuring that TERT only assembles with functional telomerase RNA to form active telomerase. Our finding reveals a mechanism for non-coding RNA folding quality control.","doi":"10.1016/j.celrep.2020.108568","authors":"Hu X, Kim JK, Yu C, Jun HI, Liu J, Sankaran B, Huang L, Qiao F","authors_abbrev":"Hu X et al.","pubmed_publication_date":"29 Dec 2020","pubmed_entrez_date":"2020-12-30","publication_year":"2020","canto_session_key":"54907a8f92a3eb84","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Feng Qiao","canto_first_approved_date":"2021-11-17 14:54:34","canto_approved_date":"2025-09-03 11:02:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-10-24 08:49:19","canto_added_date":"2021-10-15 00:15:03","annotation_curators":[{"name":"Feng Qiao","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":44,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.10","SPBC30D10.06","SPBC29A3.14c","SPNCRNA.214","SPBC9B6.05c","SPAC17G6.17"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2021-11-17","pdb_entries":[{"pdb_id":"6u7v","gene_chains":[{"gene_uniquename":"SPAC17G6.17","chain":"A","position":"273-402"}],"title":"xRRM structure of spPof8","entry_authors":"Kim J-K,Hu X,Yu C,Jun H-I,Liu J,Sankaran B,Huang L,Qiao F","entry_authors_abbrev":"Kim J-K et al.","reference_uniquename":"PMID:33378677","experimental_method":"X-ray","resolution":"1.42"}]},{"uniquename":"PMID:9127201","title":"Identification of preussin as a selective inhibitor for cell growth of the fission yeast ts mutants defective in Cdc2-regulatory genes.","citation":"J Antibiot (Tokyo) 1997 Mar;50(3):267-9","abstract":"","authors":"Kasahara K, Yoshida M, Eishima J, Takesako K, Beppu T, Horinouchi S","authors_abbrev":"Kasahara K et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25298518","title":"Ectopic centromere nucleation by CENP--a in fission yeast.","citation":"Genetics 2014 Dec;198(4):1433-46","abstract":"The centromere is a specific chromosomal locus that organizes the assembly of the kinetochore. It plays a fundamental role in accurate chromosome segregation. In most eukaryotic organisms, each chromosome contains a single centromere the position and function of which are epigenetically specified. Occasionally, centromeres form at ectopic loci, which can be detrimental to the cell. However, the mechanisms that protect the cell against ectopic centromeres (neocentromeres) remain poorly understood. Centromere protein-A (CENP-A), a centromere-specific histone 3 (H3) variant, is found in all centromeres and is indispensable for centromere function. Here we report that the overexpression of CENP-A(Cnp1) in fission yeast results in the assembly of CENP-A(Cnp1) at noncentromeric chromatin during mitosis and meiosis. The noncentromeric CENP-A preferentially assembles near heterochromatin and is capable of recruiting kinetochore components. Consistent with this, cells overexpressing CENP-A(Cnp1) exhibit severe chromosome missegregation and spindle microtubule disorganization. In addition, pulse induction of CENP-A(Cnp1) overexpression reveals that ectopic CENP-A chromatin can persist for multiple generations. Intriguingly, ectopic assembly of CENP-A(cnp1) is suppressed by overexpression of histone H3 or H4. Finally, we demonstrate that deletion of the N-terminal domain of CENP-A(cnp1) results in an increase in the number of ectopic CENP-A sites and provide evidence that the N-terminal domain of CENP-A prevents CENP-A assembly at ectopic loci via the ubiquitin-dependent proteolysis. These studies expand our current understanding of how noncentromeric chromatin is protected from mistakenly assembling CENP-A.","doi":"10.1534/genetics.114.171173","authors":"Gonzalez M, He H, Dong Q, Sun S, Li F","authors_abbrev":"Gonzalez M et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-10-10","publication_year":"2014","canto_session_key":"42b4f0bd2e01ad3e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Fei Li","canto_first_approved_date":"2026-06-14 06:48:16","canto_approved_date":"2026-06-14 06:48:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-06-02 20:28:35","canto_added_date":"2014-10-11 00:15:51","annotation_curators":[{"name":"Fei Li","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.03c","SPAC1834.04","SPBC337.08c","SPBC1105.17"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2026-06-14"},{"uniquename":"PMID:25916713","title":"Chromatin immunoprecipitation to detect DNA replication and repair factors.","citation":"Methods Mol Biol 2015;1300:169-86","abstract":"DNA replication is tightly coupled with DNA repair processes in order to preserve genomic integrity. During DNA replication, the replication fork encounters a variety of obstacles including DNA damage/adducts, secondary structures, and programmed fork-blocking sites, which are all difficult to replicate. The replication fork also collides with the transcription machinery, which shares the template DNA with the replisome complex. Under these conditions, replication forks stall, causing replication stress and/or fork collapse, ultimately leading to genomic instability. The mechanisms to overcome these replication problems remain elusive. Therefore, it is important to investigate how DNA repair and replication factors are recruited and coordinated at chromosomal regions that are difficult to replicate. In this chapter, we describe a chromatin immunoprecipitation method to locate proteins required for DNA repair during DNA replication in the fission yeast Schizosaccharomyces pombe. This method can also easily be adapted to study replisome components or chromatin-associated factors.","doi":"10.1007/978-1-4939-2596-4_12","authors":"Gadaleta MC, Iwasaki O, Noguchi C, Noma K, Noguchi E","authors_abbrev":"Gadaleta MC et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-04-29","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-04-30 00:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18799626","title":"Fission yeast kinesin-8 Klp5 and Klp6 are interdependent for mitotic nuclear retention and required for proper microtubule dynamics.","citation":"Mol Biol Cell 2008 Dec;19(12):5104-15","abstract":"Fission yeast has two kinesin-8s, Klp5 and Klp6, which associate to form a heterocomplex. Here, we show that Klp5 and Klp6 are mutually dependent on each other for nuclear mitotic localization. During interphase, they are exported to the cytoplasm. In sharp contrast, during mitosis, Klp5 and Klp6 remain in the nucleus, which requires the existence of each counterpart. Canonical nuclear localization signal (NLS) is identified in the nonkinesin C-terminal regions. Intriguingly individual NLS mutants (NLSmut) exhibit loss-of-function phenotypes, suggesting that Klp5 and Klp6 enter the nucleus separately. Indeed, although neither Klp5-NLSmut nor Klp6-NLSmut enters the nucleus, wild-type Klp6 or Klp5, respectively, does so with different kinetics. In the absence of Klp5/6, microtubule catastrophe/rescue frequency and dynamicity are suppressed, whereas growth and shrinkage rates are least affected. Remarkably, chimera strains containing only the N-terminal Klp5 kinesin domains cannot disassemble interphase microtubules during mitosis, leading to the coexistence of cytoplasmic microtubules and nuclear spindles with massive chromosome missegregation. In this strain, a marked reduction of microtubule dynamism, even higher than in klp5/6 deletions, is evident. We propose that Klp5 and Klp6 play a vital role in promoting microtubule dynamics, which is essential for the spatiotemporal control of microtubule morphogenesis.","authors":"Unsworth A, Masuda H, Dhut S, Toda T","authors_abbrev":"Unsworth A et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-09-19","publication_year":"2008","canto_session_key":"d31bdd99cf204c6f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-15 08:04:09","canto_approved_date":"2021-04-22 16:14:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-03-28 10:29:29","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":42,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.13","SPBC1685.15c","SPAC1805.17"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2017-06-15"},{"uniquename":"PMID:24112980","title":"Cellular aging: symmetry evades senescence.","citation":"Curr Biol 2013 Oct 07;23(19):R871-3","abstract":"Cellular aging programs typically rely on the asymmetric shape and growth pattern of cells. A new study shows that symmetric fission yeast cells escape classic signs of aging until they encounter environmental stress.","doi":"10.1016/j.cub.2013.08.013","authors":"Moseley JB","authors_abbrev":"Moseley JB","pubmed_publication_date":"07 Oct 2013","pubmed_entrez_date":"2013-10-12","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12773392","title":"Alp13, an MRG family protein, is a component of fission yeast Clr6 histone deacetylase required for genomic integrity.","citation":"EMBO J 2003 Jun 02;22(11):2776-87","abstract":"The post-translational modifications of histones are key to the modulation of chromatin structure. Distinct patterns of modifications established by histone-modifying enzymes control diverse chromosomal processes. Here, we report the purification and molecular characterization of the fission yeast Clr6 histone deacetyl ase involved in higher order chromatin assembly. We show that a chromodomain protein Alp13, which belongs to the conserved MRG protein family linked to cellular senescence in humans, is associated with Clr6. In addition, Clr6 interacts with homologs of the mammalian transcriptional co-repressors Sin3, Pst1 and Pst2, and a WD40 repeat-containing protein, Prw1. Alp13, Pst2 and Prw1 form a stable complex with Clr6 in the nucleus. Deletion of any of these factors causes progressive loss of viability and sensitivity to DNA-damaging agents, and impairs condensation/resolution of chromosomes during mitosis. This is accompanied by hyperacetylation of histones and a reduction in histone H3 Ser10 phosphorylation, which correlates with chromosome condensation during mitosis. These results link the MRG family protein Alp13 to histone deacetylation, and suggest that Clr6 and its associated factors are essential for fundamental chromosomal events.","authors":"Nakayama J, Xiao G, Noma K, Malikzay A, Bjerling P, Ekwall K, Kobayashi R, Grewal SI","authors_abbrev":"Nakayama J et al.","pubmed_publication_date":"02 Jun 2003","pubmed_entrez_date":"2003-05-30","publication_year":"2003","canto_session_key":"669a6e624422bdf5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-03-21 07:54:32","canto_approved_date":"2024-03-21 07:54:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-20 18:19:55","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":53,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.05c","SPAC23C11.15","SPAC29A4.18","SPAC23H4.12"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-03-21"},{"uniquename":"PMID:16830049","title":"Correlating yeast cell stress physiology to changes in the cell surface morphology: atomic force microscopic studies.","citation":"ScientificWorldJournal 2006 Jul 06;6:777-80","abstract":"Atomic Force Microscopy (AFM) has emerged as a powerful biophysical tool in biotechnology and medicine to investigate the morphological, physical, and mechanical properties of yeasts and other biological systems. However, properties such as, yeasts' response to environmental stresses, metabolic activities of pathogenic yeasts, cell-cell/cell-substrate adhesion, and cell-flocculation have rarely been investigated so far by using biophysical tools. Our recent results obtained by AFM on one strain each of Saccharomyces cerevisiae and Schizosaccharomyces pombe show a clear correlation between the physiology of environmentally stressed yeasts and the changes in their surface morphology. The future directions of the AFM related techniques in relation to yeasts are also discussed.","authors":"Canetta E, Walker GM, Adya AK","authors_abbrev":"Canetta E et al.","pubmed_publication_date":"06 Jul 2006","pubmed_entrez_date":"2006-07-11","publication_year":"2006","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3357510","title":"A specific inhibitor of the ran1+ protein kinase regulates entry into meiosis in Schizosaccharomyces pombe.","citation":"Nature 1988 Apr 07;332(6164):509-14","abstract":"In fission yeast, meiosis is initiated by transcriptional activation of the mei3+ gene, under the combined influence of the four mating-type genes. The product of the mei3+ gene acts as a critical meiotic inducer by binding non-covalently to a newly identified protein kinase encoded by the ran1+ gene and inhibiting its enzymatic activity. Inactivation of the ran1+ protein kinase is both necessary and sufficient to divert a vegetative cell from mitotic division to meiotic differentiation.","authors":"McLeod M, Beach D","authors_abbrev":"McLeod M et al.","pubmed_publication_date":"07 Apr 1988","pubmed_entrez_date":"1988-04-07","publication_year":"1988","canto_session_key":"b2b393b33cecb3fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 09:51:08","canto_approved_date":"2024-03-27 06:35:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-03-08 08:41:09","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPBC119.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-10"},{"uniquename":"PMID:21459850","title":"In silico characterization and prediction of global protein-mRNA interactions in yeast.","citation":"Nucleic Acids Res 2011 Aug;39(14):5826-36","abstract":"Post-transcriptional gene regulation is mediated through complex networks of protein-RNA interactions. The targets of only a few RNA binding proteins (RBPs) are known, even in the well-characterized budding yeast. In silico prediction of protein-RNA interactions is therefore useful to guide experiments and to provide insight into regulatory networks. Computational approaches have identified RBP targets based on sequence binding preferences. We investigate here to what extent RBP-RNA interactions can be predicted based on RBP and mRNA features other than sequence motifs. We analyze global relationships between gene and protein properties in general and between selected RBPs and known mRNA targets in particular. Highly translated RBPs tend to bind to shorter transcripts, and transcripts bound by the same RBP show high expression correlation across different biological conditions. Surprisingly, a given RBP preferentially binds to mRNAs that encode interaction partners for this RBP, suggesting coordinated post-transcriptional auto-regulation of protein complexes. We apply a machine-learning approach to predict specific RBP targets in yeast. Although this approach performs well for RBPs with known targets, predictions for uncharacterized RBPs remain challenging due to limiting experimental data. We also predict targets of fission yeast RBPs, indicating that the suggested framework could be applied to other species once more experimental data are available.","doi":"10.1093/nar/gkr160","authors":"Pancaldi V, Bähler J","authors_abbrev":"Pancaldi V et al.","pubmed_publication_date":"Aug 2011","pubmed_entrez_date":"2011-04-05","publication_year":"2011","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29684020","title":"Black-boxing and cause-effect power.","citation":"PLoS Comput Biol 2018 Apr;14(4):e1006114","abstract":"Reductionism assumes that causation in the physical world occurs at the micro level, excluding the emergence of macro-level causation. We challenge this reductionist assumption by employing a principled, well-defined measure of intrinsic cause-effect power-integrated information (Φ), and showing that, according to this measure, it is possible for a macro level to \"beat\" the micro level. Simple systems were evaluated for Φ across different spatial and temporal scales by systematically considering all possible black boxes. These are macro elements that consist of one or more micro elements over one or more micro updates. Cause-effect power was evaluated based on the inputs and outputs of the black boxes, ignoring the internal micro elements that support their input-output function. We show how black-box elements can have more common inputs and outputs than the corresponding micro elements, revealing the emergence of high-order mechanisms and joint constraints that are not apparent at the micro level. As a consequence, a macro, black-box system can have higher Φ than its micro constituents by having more mechanisms (higher composition) that are more interconnected (higher integration). We also show that, for a given micro system, one can identify local maxima of Φ across several spatiotemporal scales. The framework is demonstrated on a simple biological system, the Boolean network model of the fission-yeast cell-cycle, for which we identify stable local maxima during the course of its simulated biological function. These local maxima correspond to macro levels of organization at which emergent cause-effect properties of physical systems come into focus, and provide a natural vantage point for scientific inquiries.","doi":"10.1371/journal.pcbi.1006114","authors":"Marshall W, Albantakis L, Tononi G","authors_abbrev":"Marshall W et al.","pubmed_publication_date":"Apr 2018","pubmed_entrez_date":"2018-04-24","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-04-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8878976","title":"Isolation of ptb1, a gene for the beta-subunit of a prenyltransferase from fission yeast.","citation":"Biochem Soc Trans 1996 Aug;24(3):432S","abstract":"","authors":"Godfrey R, Davey J","authors_abbrev":"Godfrey R et al.","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_session_key":"b08065e773e2b3b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:45:46","canto_session_submitted_date":"2012-02-27 11:07:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:27797071","title":"An In Vitro Assay for Monitoring Topological DNA Entrapment by the Chromosomal Cohesin Complex.","citation":"Methods Mol Biol 2017;1515:23-35","abstract":"The cohesin complex is involved in a broad range of chromosomal biology, including DNA repair, gene transcription as well as sister chromatid cohesion. Cohesin is a large, ring-shaped protein complex and is thought to entrap DNA molecules inside of its ring. The unique DNA association is central to cohesin function and requires its ATPase and another heterodimer complex called the cohesin loader. Here we describe the biochemical reconstitution of topological cohesin loading onto DNA using the purified fission yeast cohesin proteins.","authors":"Murayama Y, Uhlmann F","authors_abbrev":"Murayama Y et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2016-11-01","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-02 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29216371","title":"Fission yeast Ccq1 is a modulator of telomerase activity.","citation":"Nucleic Acids Res 2018 Jan 25;46(2):704-716","abstract":"Shelterin, the telomeric protein complex, plays a crucial role in telomere homeostasis. In fission yeast, telomerase is recruited to chromosome ends by the shelterin component Tpz1 and its binding partner Ccq1, where telomerase binds to the 3' overhang to add telomeric repeats. Recruitment is initiated by the interaction of Ccq1 with the telomerase subunit Est1. However, how telomerase is released following elongation remains to be established. Here, we show that Ccq1 also has a role in the suppression of telomere elongation, when coupled with the Clr4 histone H3 methyl-transferase complex and the Clr3 histone deacetylase and nucleosome remodelling complex, SHREC. We have dissected the functions of Ccq1 by establishing a Ccq1-Est1 fusion system, which bypasses the telomerase recruitment step. We demonstrate that Ccq1 forms two distinct complexes for positive and negative telomerase regulation, with Est1 and Clr3 respectively. The negative form of Ccq1 promotes dissociation of Ccq1-telomerase from Tpz1, thereby restricting local telomerase activity. The Clr4 complex also has a negative regulation activity with Ccq1, independently of SHREC. Thus, we propose a model in which Ccq1-Est1 recruits telomerase to mediate telomere extension, whilst elongated telomeric DNA recruits Ccq1 with the chromatin-remodelling complexes, which in turn releases telomerase from the telomere.","doi":"10.1093/nar/gkx1223","authors":"Armstrong CA, Moiseeva V, Collopy LC, Pearson SR, Ullah TR, Xi ST, Martin J, Subramaniam S, Marelli S, Amelina H, Tomita K","authors_abbrev":"Armstrong CA et al.","pubmed_publication_date":"25 Jan 2018","pubmed_entrez_date":"2017-12-08","publication_year":"2018","canto_session_key":"eda37cd3f3ffb2ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kazunori Tomita","canto_first_approved_date":"2017-12-18 14:38:13","canto_approved_date":"2022-09-04 08:18:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-11 12:42:09","canto_added_date":"2017-12-09 01:15:56","annotation_curators":[{"name":"Kazunori Tomita","community_curator":true,"annotation_count":17,"orcid":"0000-0003-1096-6725","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":63,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPNCRNA.214","SPBC2D10.13","SPBP35G2.10","SPCC188.07","SPBC29A3.14c","SPAC6F6.16c","SPAC644.14c","SPBC1778.02","SPBC428.08c","SPBC365.06","SPAC664.01c","SPAC6F6.17"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2017-12-18"},{"uniquename":"PMID:38773107","title":"The SUN-family protein Sad1 mediates heterochromatin spatial organization through interaction with histone H2A-H2B.","citation":"Nat Commun 2024 May 21;15(1):4322","abstract":"Heterochromatin is generally associated with the nuclear periphery, but how the spatial organization of heterochromatin is regulated to ensure epigenetic silencing remains unclear. Here we found that Sad1, an inner nuclear membrane SUN-family protein in fission yeast, interacts with histone H2A-H2B but not H3-H4. We solved the crystal structure of the histone binding motif (HBM) of Sad1 in complex with H2A-H2B, revealing the intimate contacts between Sad1 HBM  and H2A-H2B. Structure-based mutagenesis studies revealed that the H2A-H2B-binding activity of Sad1 is required for the dynamic distribution of Sad1 throughout the nuclear envelope (NE). The Sad1-H2A-H2B complex mediates tethering telomeres and the mating-type locus to the NE. This complex is also important for heterochromatin silencing. Mechanistically, H2A-H2B enhances the interaction between Sad1 and HDACs, including Clr3 and Sir2, to maintain epigenetic identity of heterochromatin. Interestingly, our results suggest that Sad1 exhibits the histone-enhanced liquid-liquid phase separation property, which helps recruit heterochromatin factors to the NE. Our results uncover an unexpected role of SUN-family proteins in heterochromatin regulation and suggest a nucleosome-independent role of H2A-H2B in regulating Sad1's functionality.","doi":"10.1038/s41467-024-48418-7","authors":"Sun W, Dong Q, Li X, Gao J, Ye X, Hu C, Li F, Chen Y","authors_abbrev":"Sun W et al.","pubmed_publication_date":"21 May 2024","pubmed_entrez_date":"2024-05-21","publication_year":"2024","canto_session_key":"118a3fcd1840e9b4","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-05-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.06c","SPCC622.09","SPBC12D12.01"],"gene_count":3,"ltp_gene_count":3,"pdb_entries":[{"pdb_id":"7ybf","gene_chains":[{"gene_uniquename":"SPAC19G12.06c","chain":"A/B","position":"15-108"},{"gene_uniquename":"SPCC622.09","chain":"A/B","position":"32-126"},{"gene_uniquename":"SPBC12D12.01","chain":"C","position":"110-126"}],"title":"Crystal structure of inner membrane protein Sad1 in complex with histone H2A-H2B","entry_authors":"Sun W,Hu C,Chen Y","entry_authors_abbrev":"Sun W et al.","reference_uniquename":"PMID:38773107","experimental_method":"X-ray","resolution":"2.15"}]},{"uniquename":"PMID:12810074","title":"A fission yeast homologue of the human uracil-DNA-glycosylase and their roles in causing DNA damage after overexpression.","citation":"Biochem Biophys Res Commun 2003 Jul 04;306(3):693-700","abstract":"A functional homologue (ung1) of the human uracil-DNA-glycosylase (UNG) gene was characterized from fission yeast (Schizosaccharomyces pombe). The ung1 gene is highly conserved and encodes a protein with uracil-DNA-glycosylase activity similar to human UNG. The Ung1 protein localizes predominantly to the nucleus, suggesting that it is more similar to the nuclear form (UNG2) than the mitochondrial form (UNG1) of human UNG. Even though deletion of ung1 does not cause any obvious defects, overexpression of ung1 increases the mutation frequency. Overexpression of ung1 or human UNG2 induces a DNA checkpoint-dependent cell cycle delay and causes cell death which is enhanced when the checkpoints are inactive. In addition, the steady-state level of AP (apurinic/apyrimidinic) sites increases after ung1 overexpression, indicating that AP sites are likely to be the DNA damage caused by overexpression. Analysis of mutant ung indicates that catalytic activity is not required for the effects of overexpression, but that binding of Ung1 or UNG2 to AP sites may be important.","authors":"Elder RT, Zhu X, Priet S, Chen M, Yu M, Navarro JM, Sire J, Zhao Y","authors_abbrev":"Elder RT et al.","pubmed_publication_date":"04 Jul 2003","pubmed_entrez_date":"2003-06-18","publication_year":"2003","canto_session_key":"45d907cccb67195b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-13 15:36:44","canto_approved_date":"2019-11-13 15:36:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-10-31 14:06:39","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1183.06","SPBC216.05","SPCC1259.13","SPCC18B5.11c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-11-13"},{"uniquename":"PMID:15302409","title":"Preferential loss and gain of introns in 3' portions of genes suggests a reverse-transcription mechanism of intron insertion.","citation":"Gene 2004 Aug 18;338(1):85-91","abstract":"In an attempt to gain insight into the dynamics of intron evolution in eukaryotic protein-coding genes, the distributions of old introns, that are conserved between distant phylogenetic lineages, and new, lineage-specific introns along the gene length, were examined. A significant excess of old introns in 5'-regions of genes was detected. New introns, when analyzed in bulk, showed a nearly flat distribution from the 5'- to the 3'-end. However, analysis of new intron distributions in individual genomes revealed notable lineage-specific features. While in intron-poor genomes, particularly yeast Schizosaccharomyces pombe (Sp), the 5'-portions of genes contain a significantly greater number of new introns than the 3'-portions, the intron-rich genomes of humans and Arabidopsis show the opposite trend. These observations seem to be compatible with the view that introns are both lost and inserted in 3'-terminal portions of genes more often than in 5'-portions. Overrepresentation of 3'-terminal sequences among cDNAs that mediate intron loss appears to be the most likely explanation for the apparent preferential loss of introns in the distal parts of genes. Preferential insertion of introns in the 3'-portions suggests that introns might be inserted via a reverse-transcription-mediated pathway similar to that implicated in intron loss. This mechanism could involve duplication of a portion of the coding region during reverse transcription followed by homologous recombination and subsequent rapid sequence divergence in the copy that becomes a new intron.","authors":"Sverdlov AV, Babenko VN, Rogozin IB, Koonin EV","authors_abbrev":"Sverdlov AV et al.","pubmed_publication_date":"18 Aug 2004","pubmed_entrez_date":"2004-08-11","publication_year":"2004","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15157496","title":"rum1: a CDK inhibitor regulating G1 progression in fission yeast.","citation":"Trends Cell Biol 1996 Feb;6(2):62-6","abstract":"In all eukaryotes, entry into mitosis from G2 phase is initiated by a complex of the cdc2 kinase and a B-type cyclin. It has now been shown that, in fission yeast, B-type cyclins also activate cdc2 in G1, thus governing cell-cycle commitment, as well as the onset of S phase. In this article, Karim Labib and Sergio Moreno review the evidence that ruml inhibits the kinase activity of cdc2 associated with B-type cyclins and is an important regulator o f G1 progression in fission yeast.","authors":"Labib K, Moreno S","authors_abbrev":"Labib K et al.","pubmed_publication_date":"Feb 1996","pubmed_entrez_date":"1996-02-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25313826","title":"The chromatin assembly factor 1 promotes Rad51-dependent template switches at replication forks by counteracting D-loop disassembly by the RecQ-type helicase Rqh1.","citation":"PLoS Biol 2014 Oct;12(10):e1001968","abstract":"At blocked replication forks, homologous recombination mediates the nascent strands to switch template in order to ensure replication restart, but faulty template switches underlie genome rearrangements in cancer cells and genomic disorders. Recombination occurs within DNA packaged into chromatin that must first be relaxed and then restored when recombination is completed. The chromatin assembly factor 1, CAF-1, is a histone H3-H4 chaperone involved in DNA synthesis-coupled chromatin assembly during DNA replication and DNA repair. We reveal a novel chromatin factor-dependent step during replication-coupled DNA repair: Fission yeast CAF-1 promotes Rad51-dependent template switches at replication forks, independently of the postreplication repair pathway. We used a physical assay that allows the analysis of the individual steps of template switch, from the recruitment of recombination factors to the formation of joint molecules, combined with a quantitative measure of the resulting rearrangements. We reveal functional and physical interplays between CAF-1 and the RecQ-helicase Rqh1, the BLM homologue, mutations in which cause Bloom's syndrome, a human disease associating genome instability with cancer predisposition. We establish that CAF-1 promotes template switch by counteracting D-loop disassembly by Rqh1. Consequently, the likelihood of faulty template switches is controlled by antagonistic activities of CAF-1 and Rqh1 in the stability of the D-loop. D-loop stabilization requires the ability of CAF-1 to interact with PCNA and is thus linked to the DNA synthesis step. We propose that CAF-1 plays a regulatory role during template switch by assembling chromatin on the D-loop and thereby impacting the resolution of the D-loop.","doi":"10.1371/journal.pbio.1001968","authors":"Pietrobon V, Fréon K, Hardy J, Costes A, Iraqui I, Ochsenbein F, Lambert SA","authors_abbrev":"Pietrobon V et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-10-15","publication_year":"2014","canto_session_key":"e8a53aa5aa4d49f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Lambert","canto_approved_date":"2015-12-22 16:38:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-21 09:03:33","canto_added_date":"2014-10-16 00:15:25","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sarah Lambert","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPAC13G6.01c","SPAC644.14c","SPBC1347.01c","SPAC4H3.05","SPAC26H5.03","SPBC29A10.03c","SPAC25H1.06","SPBC16D10.09"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2014-11-21"},{"uniquename":"PMID:31615333","title":"Condensin locates at transcriptional termination sites in mitosis, possibly releasing mitotic transcripts.","citation":"Open Biol 2019 Oct 31;9(10):190125","abstract":"Condensin is an essential component of chromosome dynamics, including mitotic chromosome condensation and segregation, DNA repair, and development. Genome-wide localization of condensin is known to correlate with transcriptional activity. The functional relationship between condensin accumulation and transcription sites remains unclear, however. By constructing the auxin-inducible degron strain of condensin, herein we demonstrate that condensin does not affect transcription itself. Instead, RNA processing at transcriptional termination appears to define condensin accumulation sites during mitosis, in the fission yeast  Schizosaccharomyces pombe . Combining the auxin-degron strain with the  nda3  β-tubulin cold-sensitive (cs) mutant enabled us to inactivate condensin in mitotically arrested cells, without releasing the cells into anaphase. Transcriptional activation and termination were not affected by condensin's degron-mediated depletion, at heat-shock inducible genes or mitotically activated genes. On the other hand, condensin accumulation sites shifted approximately 500 bp downstream in the auxin-degron of 5'-3' exoribonuclease Dhp1, in which transcripts became aberrantly elongated, suggesting that condensin accumulates at transcriptionally terminated DNA regions. Growth defects in mutant strains of 3'-processing ribonuclease and polyA cleavage factors were additive in condensin temperature-sensitive (ts) mutants. Considering condensin's  in vitro  activity to form double-stranded DNAs from unwound, single-stranded DNAs or DNA-RNA hybrids, condensin-mediated processing of mitotic transcripts at the 3'-end may be a prerequisite for faithful chromosome segregation.","doi":"10.1098/rsob.190125","authors":"Nakazawa N, Arakawa O, Yanagida M","authors_abbrev":"Nakazawa N et al.","pubmed_publication_date":"31 Oct 2019","pubmed_entrez_date":"2019-10-17","publication_year":"2019","canto_session_key":"f54275f3a8758cf5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Norihiko Nakazawa","canto_first_approved_date":"2020-09-24 18:49:34","canto_approved_date":"2023-01-30 16:34:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-19 14:58:43","canto_added_date":"2019-10-18 00:15:04","annotation_curators":[{"name":"Norihiko Nakazawa","community_curator":true,"annotation_count":14,"orcid":"0000-0001-8386-0812","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.03c","SPBP4H10.06c","SPBC26H8.10","SPAC926.04c","SPAC19B12.02c","SPAC6F12.17","SPAC222.09","SPAC26A3.12c","SPAC1705.03c","SPAC13G7.02c","SPBC1709.08"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2020-09-24"},{"uniquename":"PMID:8039497","title":"The cdc7 protein kinase is a dosage dependent regulator of septum formation in fission yeast.","citation":"EMBO J 1994 Jul 01;13(13):3011-9","abstract":"Mutation of the Schizosaccharomyces pombe cdc7 gene prevents formation of the division septum and cytokinesis. We have cloned the cdc7 gene and show that it encodes a protein kinase which is essential for cell division. In the absence of cdc7 function, spore germination, DNA synthesis and mitosis are unaffected, but cells are unable to initiate formation of the division septum. Overexpression of p120cdc7 causes cell cycle arrest; cells complete mitosis and then undergo multiple rounds of septum formation without cell cleavage. This phenotype, which is similar to that resulting from inactivation of cdc16 protein, requires the kinase activity of p120cdc7. Mutations inactivating the early septation gene, cdc11, suppress the formation of multiple septa and allow cells to proliferate normally. If formation of the division septum is prevented by inactivation of either cdc14 or cdc15, p120cdc7 overproduction does not interfere with other events in the mitotic cell cycle. Septation is not induced by overexpression of p120cdc7 in G2 arrested cells, indicating that it does not bypass the normal dependency of septation upon initiation of mitosis. These findings indicate that the p120cdc7 protein kinase plays a key role in initiation of septum formation and cytokinesis in fission yeast and suggest that p120cdc7 interacts with the cdc11 protein in the control of septation.","authors":"Fankhauser C, Simanis V","authors_abbrev":"Fankhauser C et al.","pubmed_publication_date":"01 Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_session_key":"619cffb818489e7f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-04 21:55:38","canto_approved_date":"2021-04-27 14:55:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-12 15:52:52","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPAC20G8.05c","SPBC24C6.07","SPCC1739.11c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2019-01-04"},{"uniquename":"PMID:26870731","title":"Virtual Nuclear Envelope Breakdown and Its Regulators in Fission Yeast Meiosis.","citation":"Front Cell Dev Biol 2016;4:5","abstract":"Ran, a small GTPase, is required for the spindle formation and nuclear envelope (NE) formation. After NE breakdown (NEBD) during mitosis in metazoan cells, the Ran-GTP gradient across the NE is lost and Ran-GTP becomes concentrated around chromatin, thus affecting the stability of microtubules and promoting the assembly of spindle microtubules and segregation of chromosomes. Mitosis in which chromosomes are segregated subsequent to NEBD is called \"open mitosis.\" In contrast, many fungi undergo a process termed \"closed mitosis\" in which chromosome segregation and spindle formation occur without NEBD. Although the fission yeast Schizosaccharomyces pombe undergoes a closed mitosis, it exhibits a short period during meiosis (anaphase of the second meiosis; called \"anaphase II\") when nuclear and cytoplasmic proteins are mixed in the presence of intact NE and nuclear pore complexes (NPC). This \"virtual\" nuclear envelope breakdown (vNEBD) involves changes in the localization of RanGAP1, an activator of Ran-GTP hydrolysis. Recently, Nup132, a component of the structural core Nup107-160 subcomplex of the NPC, has been shown to be involved in the maintenance of the nuclear cytoplasmic barrier in yeast meiosis. In this review, we highlight the possible roles of RanGAP1 and Nup132 in vNEBD and discuss the biological significance of vNEBD in S. pombe meiosis.","doi":"10.3389/fcell.2016.00005","authors":"Asakawa H, Yang HJ, Hiraoka Y, Haraguchi T","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-02-13","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-02-14 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1805.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"Pfam:PF12709","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YOR195W","SPAC890.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24911101","title":"Plant, animal, and fungal micronutrient queuosine is salvaged by members of the DUF2419 protein family.","citation":"ACS Chem Biol 2014 Aug 15;9(8):1812-25","abstract":"Queuosine (Q) is a modification found at the wobble position of tRNAs with GUN anticodons. Although Q is present in most eukaryotes and bacteria, only bacteria can synthesize Q de novo. Eukaryotes acquire queuine (q), the free base of Q, from diet and/or microflora, making q an important but under-recognized micronutrient for plants, animals, and fungi. Eukaryotic type tRNA-guanine transglycosylases (eTGTs) are composed of a catalytic subunit (QTRT1) and a homologous accessory subunit (QTRTD1) forming a complex that catalyzes q insertion into target tRNAs. Phylogenetic analysis of eTGT subunits revealed a patchy distribution pattern in which gene losses occurred independently in different clades. Searches for genes co-distributing with eTGT family members identified DUF2419 as a potential Q salvage protein family. This prediction was experimentally validated in Schizosaccharomyces pombe by confirming that Q was present by analyzing tRNA(Asp) with anticodon GUC purified from wild-type cells and by showing that Q was absent from strains carrying deletions in the QTRT1 or DUF2419 encoding genes. DUF2419 proteins occur in most Eukarya with a few possible cases of horizontal gene transfer to bacteria. The universality of the DUF2419 function was confirmed by complementing the S. pombe mutant with the Zea mays (maize), human, and Sphaerobacter thermophilus homologues. The enzymatic function of this family is yet to be determined, but structural similarity with DNA glycosidases suggests a ribonucleoside hydrolase activity.","doi":"10.1021/cb500278k","authors":"Zallot R, Brochier-Armanet C, Gaston KW, Forouhar F, Limbach PA, Hunt JF, de Crécy-Lagard V","authors_abbrev":"Zallot R et al.","pubmed_publication_date":"15 Aug 2014","pubmed_entrez_date":"2014-06-10","publication_year":"2014","canto_session_key":"59866e3fe9bebea8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-11-25 17:16:19","canto_approved_date":"2025-03-12 14:33:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-10 11:37:26","canto_added_date":"2014-06-10 11:00:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.19c","SPAC589.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-11-25"},{"uniquename":"PMID:11095668","title":"Cloning and characterization of the Schizosaccharomyces pombe tRNA:pseudouridine synthase Pus1p.","citation":"Nucleic Acids Res 2000 Dec 01;28(23):4604-10","abstract":"Saccharomyces cerevisiae cells that carry deletions in both the LOS1 (a tRNA export receptor) and the PUS1 (a tRNA:pseudouridine synthase) genes exhibit a thermosensitive growth defect. A Schizosaccharomyces pombe gene, named spPUS1, was cloned from a cDNA library by complementation of this conditional lethal phenotype. The corresponding protein, spPus1p, shows sequence similarity to S. cerevisiae and murine Pus1p as well as other known members of the pseudouridine synthase family. Accordingly, recombinant spPus1p can catalyze in vitro the formation of pseudouridines at positions 27, 28, 34, 35 and 36 of yeast tRNA transcripts. The sequence and functional conservation of the Pus1p proteins in fungi and mammalian species and their notable absence from prokaryotes suggest that this family of pseudouridine synthases is required for a eukaryote-specific step of tRNA biogenesis, such as nuclear export.","authors":"Hellmuth K, Grosjean H, Motorin Y, Deinert K, Hurt E, Simos G","authors_abbrev":"Hellmuth K et al.","pubmed_publication_date":"01 Dec 2000","pubmed_entrez_date":"2000-11-30","publication_year":"2000","canto_session_key":"aa630290a59266f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-06-26 15:56:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-26 15:56:39","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-06-26"},{"uniquename":"PMID:11514436","title":"Correct regulation of the septation initiation network in Schizosaccharomyces pombe requires the activities of par1 and par2.","citation":"Genetics 2001 Aug;158(4):1413-29","abstract":"In Schizosaccharomyces pombe, the initiation of cytokinesis is regulated by a septation initiation network (SIN). We previously reported that deletion of par1 and par2, two S. pombe genes encoding B' regulatory subunits of protein phosphatase 2A, causes a multiseptation phenotype, very similar to that seen in hyperactive SIN mutants. In this study, we examined the genetic interactions between par deletions and mutations in the genes encoding components of SIN and found that deletion of par1 and par2 suppressed the morphological and viability defects caused by overproduction of Byr4p and rescued a loss-of-function allele of spg1. However, par deletions could not suppress any mutations in genes downstream of spg1 in the SIN pathway. We showed further that, in suppressing the lethality of a spg1 loss-of-function allele, the correct localization of Cdc7p to the spindle pole body (SPB), which is normally lost in spg1 mutant cells, was restored. The fact that par mutant cells themselves exhibited a symmetric localization of Cdc7p to SPBs indicated a hyperactivity of SIN in such cells. On the basis of our epistasis analyses and cytological studies, we concluded that par genes normally negatively regulate SIN at or upstream of cdc7, ensuring that multiple rounds of septation do not occur.","authors":"Jiang W, Hallberg RL","authors_abbrev":"Jiang W et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-08-22","publication_year":"2001","canto_session_key":"e18451a565bca640","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-12-18 20:22:15","canto_approved_date":"2025-09-02 21:48:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-12-18 16:22:09","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.02","SPAC9G1.09","SPAC1565.06c","SPBC24C6.07","SPBC244.01c","SPBC21.06c","SPAC6F12.12","SPAC222.10c","SPAC24B11.11c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2021-12-18"},{"uniquename":"PMID:22467915","title":"DeOri: a database of eukaryotic DNA replication origins.","citation":"Bioinformatics 2012 Jun 01;28(11):1551-2","abstract":"DNA replication, a central event for cell proliferation, is the basis of biological inheritance. The identification of replication origins helps to reveal the mechanism of the regulation of DNA replication. However, only few eukaryotic replication origins were characterized not long ago; nevertheless, recent genome-wide approaches have boosted the number of mapped replication origins. To gain a comprehensive understanding of the nature of eukaryotic replication origins, we have constructed a Database of Eukaryotic ORIs (DeOri), which contains all the eukaryotic ones identified by genome-wide analyses currently available. A total of 16 145 eukaryotic replication origins have been collected from 6 eukaryotic organisms in which genome-wide studies have been performed, the replication-origin numbers being 433, 7489, 1543, 148, 348 and 6184 for humans, mice, Arabidopsis thaliana, Kluyveromyces lactis, Schizosaccharomyces pombe and Drosophila melanogaster, respectively.\nDatabase of Eukaryotic ORIs (DeOri) can be accessed from http://tubic.tju.edu.cn/deori/","doi":"10.1093/bioinformatics/bts151","authors":"Gao F, Luo H, Zhang CT","authors_abbrev":"Gao F et al.","pubmed_publication_date":"01 Jun 2012","pubmed_entrez_date":"2012-04-03","publication_year":"2012","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7880537","title":"Cdc2 regulatory factors.","citation":"Curr Opin Cell Biol 1994 Dec;6(6):877-82","abstract":"A growing family of kinases and phosphatases controls the activity of the cyclin-dependent kinase cdc2. The past year has seen the identification of the cdk activating kinase as well as considerable elucidation of the cdc25/wee1 regulatory pathways. Both cdc25 and wee1 appear to be regulated by upstream kinase/phosphatase networks. In addition, it is likely that other regulatory mechanisms cooperate with the wee1/cdc25 phosphorylation systems to control the action of cdc2. Together, these elaborate checks and balances ensure that cdc2 triggers mitosis at the appropriate time.","authors":"Coleman TR, Dunphy WG","authors_abbrev":"Coleman TR et al.","pubmed_publication_date":"Dec 1994","pubmed_entrez_date":"1994-12-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:X56189","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:14762213","title":"Fission yeast global repressors regulate the specificity of chromatin alteration in response to distinct environmental stresses.","citation":"Nucleic Acids Res 2004;32(2):855-62","abstract":"The specific induction of genes in response to distinct environmental stress is vital for all eukaryotes. To study the mechanisms that result in selective gene responses, we examined the role of the fission yeast Tup1 family repressors in chromatin regulation. We found that chromatin structure around a cAMP-responsive element (CRE)-like sequence in ade6-M26 that is bound by Atf1.Pcr1 transcriptional activation was altered in response to osmotic stress but not to heat and oxidative stresses. Such chromatin structure alteration occurred later than the Atf1 phosphorylation but correlated well with stress-induced transcriptional activation at ade6-M26. This chromatin structure alteration required components for the stress-activated protein kinase (SAPK) cascade and both subunits of the M26-binding CREB/ATF-type protein Atf1.Pcr1. Cation stress and glucose starvation selectively caused chromatin structure alteration around CRE-like sequences in cta3(+) and fbp1(+) promoters, respectively, in correlation with transcriptional activation. However, the tup11Delta tup12Delta double deletion mutants lost the selectivity of stress responses of chromatin structure and transcriptional regulation of cta3(+) and fbp1(+). These data indicate that the Tup1-like repressors regulate the chromatin structure to ensure the specificity of gene activation in response to particular stresses. Such a role for these proteins may serve as a paradigm for the regulation of stress response in higher eukaryotes.","authors":"Hirota K, Hasemi T, Yamada T, Mizuno KI, Hoffman CS, Shibata T, Ohta K","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-02-06","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26016518","title":"Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly Complex.","citation":"Biochemistry 2015 Jun 30;54(25):3880-9","abstract":"Iron-sulfur (Fe-S) clusters function as protein cofactors for a wide variety of critical cellular reactions. In human mitochondria, a core Fe-S assembly complex [called SDUF and composed of NFS1, ISD11, ISCU2, and frataxin (FXN) proteins] synthesizes Fe-S clusters from iron, cysteine sulfur, and reducing equivalents and then transfers these intact clusters to target proteins. In vitro assays have relied on reducing the complexity of this complicated Fe-S assembly process by using surrogate electron donor molecules and monitoring simplified reactions. Recent studies have concluded that FXN promotes the synthesis of [4Fe-4S] clusters on the mammalian Fe-S assembly complex. Here the kinetics of Fe-S synthesis reactions were determined using different electron donation systems and by monitoring the products with circular dichroism and absorbance spectroscopies. We discovered that common surrogate electron donor molecules intercepted Fe-S cluster intermediates and formed high-molecular weight species (HMWS). The HMWS are associated with iron, sulfide, and thiol-containing proteins and have properties of a heterogeneous solubilized mineral with spectroscopic properties remarkably reminiscent of those of [4Fe-4S] clusters. In contrast, reactions using physiological reagents revealed that FXN accelerates the formation of [2Fe-2S] clusters rather than [4Fe-4S] clusters as previously reported. In the preceding paper [Fox, N. G., et al. (2015) Biochemistry 54, DOI: 10.1021/bi5014485], [2Fe-2S] intermediates on the SDUF complex were shown to readily transfer to uncomplexed ISCU2 or apo acceptor proteins, depending on the reaction conditions. Our results indicate that FXN accelerates a rate-limiting sulfur transfer step in the synthesis of [2Fe-2S] clusters on the human Fe-S assembly complex.","doi":"10.1021/bi5014497","authors":"Fox NG, Das D, Chakrabarti M, Lindahl PA, Barondeau DP","authors_abbrev":"Fox NG et al.","pubmed_publication_date":"30 Jun 2015","pubmed_entrez_date":"2015-05-29","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11600706","title":"SUMO modification of Rad22, the Schizosaccharomyces pombe homologue of the recombination protein Rad52.","citation":"Nucleic Acids Res 2001 Oct 15;29(20):4179-86","abstract":"The Schizosaccharomyces pombe rad31 and hus5 genes are required for the DNA damage response, as mutants defective in these genes are sensitive to DNA damaging agents, such as UV and ionising radiation and to the DNA synthesis inhibitor hydroxyurea (HU). Sequence analysis has suggested that rad31 and hus5 encode components of the Pmt3 (SUMO) modification process in S.pombe. We show here that the rad31 null and hus5.62 mutants display reduced levels of Pmt3 modification. We have initiated a search for proteins required for the DNA damage response, which may be modified by Pmt3 and have identified Rad22, the fission yeast homologue of the recombination protein Rad52. Purification of myc + His-tagged Rad22 protein from cells expressing HA-tagged Pmt3 identifies an 83 kDa species which cross-reacts with anti-HA antisera. We show here that Rad22 interacts with Rhp51 and Rpa70 (the fission yeast homologues of Rad51 and the large subunit of RPA, respectively), but that neither of these proteins appears to be responsible for the 83 kDa species. The 83 kDa species is observed when extracts are prepared under both native and denaturing conditions, and is also observed when myc + His-tagged Rad22 and Pmt3 are expressed at wild type levels, suggesting that Rad22 is modified by Pmt3 in vivo. We have established an S.pombe in vitro Pmt3 modification system and have shown that Rad22 and Rhp51 are modified in vitro, but that Rpa70 is not.","authors":"Ho JC, Warr NJ, Shimizu H, Watts FZ","authors_abbrev":"Ho JC et al.","pubmed_publication_date":"15 Oct 2001","pubmed_entrez_date":"2001-10-16","publication_year":"2001","canto_session_key":"a8245a213e3baa92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-26 15:17:15","canto_approved_date":"2024-03-15 17:58:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-21 14:54:25","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4C5.04","SPBC16H5.03c","SPAC30D11.10","SPAC644.14c","SPAC30D11.13","SPBC660.13c","SPBC365.06"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2017-07-26"},{"uniquename":"PMID:17660542","title":"Mms22 preserves genomic integrity during DNA replication in Schizosaccharomyces pombe.","citation":"Genetics 2007 Sep;177(1):47-61","abstract":"The faithful replication of the genome, coupled with the accurate repair of DNA damage, is essential for the maintenance of chromosomal integrity. The MMS22 gene of Saccharomyces cerevisiae plays an important but poorly understood role in preservation of genome integrity. Here we describe a novel gene in Schizosaccharomyces pombe that we propose is a highly diverged ortholog of MMS22. Fission yeast Mms22 functions in the recovery from replication-associated DNA damage. Loss of Mms22 results in the accumulation of spontaneous DNA damage in the S- and G2-phases of the cell cycle and elevated genomic instability. There are severe synthetic interactions involving mms22 and most of the homologous recombination proteins but not the structure-specific endonuclease Mus81-Eme1, which is required for survival of broken replication forks. Mms22 forms spontaneous nuclear foci and colocalizes with Rad22 in cells treated with camptothecin, suggesting that it has a direct role in repair of broken replication forks. Moreover, genetic interactions with components of the DNA replication fork suggest that Mms2 functions in the coordination of DNA synthesis following damage. We propose that Mms22 functions directly at the replication fork to maintain genomic integrity in a pathway involving Mus81-Eme1.","authors":"Dovey CL, Russell P","authors_abbrev":"Dovey CL et al.","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-07-31","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPBC336.04","SPCC4G3.05c","SPAC30D11.10","SPBC582.05c","SPBC1347.10","SPBC216.06c","SPAC20H4.07","SPCC1259.13","SPAC15A10.03c","YLR320W","SPBC30D10.04","SPAC644.14c","SPAC6B12.02c"],"gene_count":13,"ltp_gene_count":11},{"uniquename":"EMBL:AU012130","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6450631","title":"Growth of yeasts on D-xylulose 1.","citation":"Can J Microbiol 1980 Sep;26(9):1165-8","abstract":"Nine of eleven yeasts of different species or genera grew in the presence of air on the intermediate of D-xylose catabolism, D-xylulose (D-threo-pentulose). Growth on this substrate was efficient as judged by the optical density in stationary phase being generally similar to that after growth on glucose. Yeasts which grew on D-xylose also did so on D-xylulose, but among those which grew are included several which utilise neither D-xylose nor xylitol: Saccharomyces cerevisiae, Saccharomyces carlsbergensis, and Schizosaccharomyces pombe. Since catabolism of a sugar generally requires an initial phosphorylation step, growth of these strains suggests that they contain an enzyme which can function as a D-xylulose kinase. The D-xylulose-5-phosphate formed thereby is considered to enter the pentose-phosphate pathway. Glucose-grown inocula of S. carlsbergensis and Schizosaccharomyces pombe, and of several other yeasts, began to grow logarithmically when placed on D-xylulose with no apparent delay, or one which was minimal, suggesting that the D-xylulose kinase was already present in such cells, or was rapidly induced. Petites of S. cerevisiae did not grow on D-xylulose indicating that, in this species, mitochondria are involved in its utilisation.","authors":"Wang PY, Schneider H","authors_abbrev":"Wang PY et al.","pubmed_publication_date":"Sep 1980","pubmed_entrez_date":"1980-09-01","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR23111","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:11735","HGNC:11736","SPAC17H9.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15743824","title":"Inactivation of the pre-mRNA cleavage and polyadenylation factor Pfs2 in fission yeast causes lethal cell cycle defects.","citation":"Mol Cell Biol 2005 Mar;25(6):2288-96","abstract":"Faithful chromosome segregation is fundamentally important for the maintenance of genome integrity and ploidy. By isolating conditional mutants defective in chromosome segregation in the fission yeast Schizosaccharomyces pombe, we identified a role for the essential gene pfs2 in chromosome dynamics. In the absence of functional Pfs2, chromosomal attachment to the mitotic spindle was defective, with consequent chromosome missegregation. Under these circumstances, multiple intracellular foci of spindle checkpoint proteins Bub1 and Mad2 were seen, and deletion of bub1 exacerbated the mitotic defects and the loss of cell viability that resulted from the loss of pfs2 function. Progression from G1 into S phase following release from nitrogen starvation also required pfs2+ function. The product of the orthologous Saccharomyces cerevisiae gene PFS2 is a component of a multiprotein complex required for 3'-end cleavage and polyadenylation of pre-mRNAs and, in keeping with the conservation of this essential function, an S. pombe pfs2 mutant was defective in mRNA 3'-end processing. Mutations in pfs2 were suppressed by overexpression of the putative mRNA 3'-end cleavage factor Cft1. These data suggest unexpected links between mRNA 3'-end processing and chromosome replication and segregation.","authors":"Wang SW, Asakawa K, Win TZ, Toda T, Norbury CJ","authors_abbrev":"Wang SW et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-03-04","publication_year":"2005","canto_session_key":"bc4758d407b2384c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-10-14 13:41:25","canto_approved_date":"2023-06-08 09:11:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-14 12:57:08","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1709.08","SPCC1322.12c","SPAC12G12.14c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-10-14"},{"uniquename":"PMID:15603750","title":"Yeast signaling pathways in the oxidative stress response.","citation":"Mutat Res 2005 Jan 06;569(1-2):13-27","abstract":"Oxidative stress that generates the reactive oxygen species (ROS) is one of the major causes of DNA damage and mutations. The \"DNA damage checkpoint\" that arrests cell cycle and repairs damaged DNA has been a focus of recent studies, and the genetically amenable model systems provided by yeasts have been playing a leading role in the eukaryotic checkpoint research. However, means to eliminate ROS are likely to be as important as the DNA repair mechanisms in order to suppress mutations in the chromosomal DNA, and yeasts also serve as excellent models to understand how eukaryotes combat oxidative stress. In this article, we present an overview of the signaling pathways that sense oxidative stress and induce expression of various anti-oxidant genes in the budding yeast Saccharomyces cerevisiae, the fission yeast Schizosaccharomyces pombe and the pathogenic yeast Candida albicans. Three conserved signaling modules have been identified in the oxidative stress response of these diverse yeast species: the stress-responsive MAP kinase cascade, the multistep phosphorelay and the AP-1-like transcription factor. The structure and function of these signaling modules are discussed.","authors":"Ikner A, Shiozaki K","authors_abbrev":"Ikner A et al.","pubmed_publication_date":"06 Jan 2005","pubmed_entrez_date":"2004-12-18","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33428031","title":"In silico analysis of promoter regions and regulatory elements (motifs and CpG islands) of the genes encoding for alcohol production in Saccharomyces cerevisiaea S288C and Schizosaccharomyces pombe 972h.","citation":"J Genet Eng Biotechnol 2021 Jan 11;19(1):8","abstract":"The crucial factor in the production of bio-fuels is the choice of potent microorganisms used in fermentation processes. Despite the evolving trend of using bacteria, yeast is still the primary choice for fermentation. Molecular characterization of many genes from baker's yeast (Saccharomyces cerevisiaea), and fission yeast (Schizosaccharomyces pombe), have improved our understanding in gene structure and the regulation of its expression. This in silico study was done with the aim of analyzing the promoter regions, transcription start site (TSS), and CpG islands of genes encoding for alcohol production in S. cerevisiaea S288C and S. pombe 972h-.\nThe analysis revealed the highest promoter prediction scores (1.0) were obtained in five sequences (AAD4, SFA1, GRE3, YKL071W, and YPR127W) for S. cerevisiaea S288C TSS while the lowest (0.8) were found in three sequences (AAD6, ADH5, and BDH2). Similarly, in S. pombe 972h-, the highest (0.99) and lowest (0.88) prediction scores were obtained in five (Adh1, SPBC8E4.04, SPBC215.11c, SPAP32A8.02, and SPAC19G12.09) and one (erg27) sequences, respectively. Determination of common motifs revealed that S. cerevisiaea S288C had 100% coverage at MSc1 with an E value of 3.7e-007 while S. pombe 972h- had 95.23% at MSp1 with an E value of 2.6e+002. Furthermore, comparison of identified transcription factor proteins indicated that 88.88% of MSp1 were exactly similar to MSc1. It also revealed that only 21.73% in S. cerevisiaea S288C and 28% in S. pombe 972h- of the gene body regions had CpG islands. A combined phylogenetic analysis indicated that all sequences from both S. cerevisiaea S288C and S. pombe 972h- were divided into four subgroups (I, II, III, and IV). The four clades are respectively colored in blue, red, green, and violet.\nThis in silico analysis of gene promoter regions and transcription factors through the actions of regulatory structure such as motifs and CpG islands of genes encoding alcohol production could be used to predict gene expression profiles in yeast species.","doi":"10.1186/s43141-020-00097-9","authors":"Aman Beshir J, Kebede M","authors_abbrev":"Aman Beshir J et al.","pubmed_publication_date":"11 Jan 2021","pubmed_entrez_date":"2021-01-11","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-01-13 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22144917","title":"The major roles of DNA polymerases epsilon and delta at the eukaryotic replication fork are evolutionarily conserved.","citation":"PLoS Genet 2011 Dec;7(12):e1002407","abstract":"Coordinated replication of eukaryotic genomes is intrinsically asymmetric, with continuous leading strand synthesis preceding discontinuous lagging strand synthesis. Here we provide two types of evidence indicating that, in fission yeast, these two biosynthetic tasks are performed by two different replicases. First, in Schizosaccharomyces pombe strains encoding a polδ-L591M mutator allele, base substitutions in reporter genes placed in opposite orientations relative to a well-characterized replication origin are strand-specific and distributed in patterns implying that Polδ is primarily involved in lagging strand replication. Second, in strains encoding a polε-M630F allele and lacking the ability to repair rNMPs in DNA due to a defect in RNase H2, rNMPs are selectively observed in nascent leading strand DNA. The latter observation demonstrates that abundant rNMP incorporation during replication can be tolerated and that they are normally removed in an RNase H2-dependent manner. This provides strong physical evidence that Polε is the primary leading strand replicase. Collectively, these data and earlier results in budding yeast indicate that the major roles of Polδ and Polε at the eukaryotic replication fork are evolutionarily conserved.","doi":"10.1371/journal.pgen.1002407","authors":"Miyabe I, Kunkel TA, Carr AM","authors_abbrev":"Miyabe I et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-12-07","publication_year":"2011","canto_session_key":"3a653a3669f74b82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-11-11 09:41:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-11 09:41:35","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.02","SPBC25H2.13c","SPBC336.04","SPBC19G7.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-11-11"},{"uniquename":"PMID:15777722","title":"Characterisation of two novel fork-head gene homologues of Schizosaccharomyces pombe: their involvement in cell cycle and sexual differentiation.","citation":"Gene 2005 Mar 28;348:101-9","abstract":"The fork-head type transcription factors are a class of regulators that function in a broad spectrum of cellular and developmental processes in many species ranging from yeasts to human. Previous data on yeast fork-head genes suggested roles for these regulators in the control of cell division, sexual differentiation and development. The genome of Schizosaccharomyces pombe has four genes that code for proteins containing fork-head domains (FKH), two of which have been characterised. Here we describe the remaining two genes, fhl1 and fkh2, that code for proteins containing fork-head-associated domains (FHA) besides their FKHs. Neither of them is essential for viability, although the deletion of either fhl1 (putative homologue of Saccharomyces cerevisiae FHL1) or fkh2 (similar to FKH1 and FKH2 of S. cerevisiae) reduced the growth rate and caused an extension of cell length due to delayed G2-to-M transition. Occasionally, multiseptate cells were also produced, indicating the involvement of fhl1 and fkh2 in efficient septum cleavage. The fkh2Delta cells were slightly more sensitive than the wild-type cells to certain environmental stresses, showed reduced fertility and occasional deficiencies in meiosis II, indicating that fkh2 might also act in stress response and sexual differentiation.","authors":"Szilagyi Z, Batta G, Enczi K, Sipiczki M","authors_abbrev":"Szilagyi Z et al.","pubmed_publication_date":"28 Mar 2005","pubmed_entrez_date":"2005-03-22","publication_year":"2005","canto_session_key":"4e98dd2ff85e7e86","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-08-21 11:18:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-21 12:04:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16G5.15c","SPAC1142.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-07-21"},{"uniquename":"PMID:34154323","title":"Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to Transform a [3Fe-4S] to a [4Fe-4S] Cluster in Dph1-Dph2.","citation":"J Am Chem Soc 2021 Jun 30;143(25):9314-9319","abstract":"All radical  S -adenosylmethionine (radical-SAM) enzymes, including the noncanonical radical-SAM enzyme diphthamide biosynthetic enzyme Dph1-Dph2, require at least one [4Fe-4S](Cys) 3  cluster for activity. It is well-known in the radical-SAM enzyme community that the [4Fe-4S](Cys) 3  cluster is extremely air-sensitive and requires strict anaerobic conditions to reconstitute activity in vitro. Thus, how such enzymes function in vivo in the presence of oxygen in aerobic organisms is an interesting question. Working on yeast Dph1-Dph2, we found that consistent with the known oxygen sensitivity, the [4Fe-4S] cluster is easily degraded into a [3Fe-4S] cluster. Remarkably, the small iron-containing protein Dph3 donates one Fe atom to convert the [3Fe-4S] cluster in Dph1-Dph2 to a functional [4Fe-4S] cluster during the radical-SAM enzyme catalytic cycle. This mechanism to maintain radical-SAM enzyme activity in aerobic environments is likely general, and Dph3-like proteins may exist to keep other radical-SAM enzymes functional in aerobic environments.","doi":"10.1021/jacs.1c03956","authors":"Zhang Y, Su D, Dzikovski B, Majer SH, Coleman R, Chandrasekaran S, Fenwick MK, Crane BR, Lancaster KM, Freed JH, Lin H","authors_abbrev":"Zhang Y et al.","pubmed_publication_date":"30 Jun 2021","pubmed_entrez_date":"2021-06-22","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8643524","title":"Functional expression of the Schizosaccharomyces pombe Na+/H+ antiporter gene, sod2, in Saccharomyces cerevisiae.","citation":"Proc Natl Acad Sci U S A 1996 May 14;93(10):5031-6","abstract":"In the fission yeast, Schizosaccharomyces pombe, tolerance to high sodium and lithium concentrations requires the functioning of the sod2, Na+/H+ antiporter. We have directly measured the activity of this antiporter and demonstrated reconstitution of the activity in gene deletion strains. In addition, we have shown that it can be transferred to, and its antiporter activity detected in, the budding yeast, Saccharomyces cerevisiae, where it also confers sodium and lithium tolerance. Proton flux through the S. pombe Na+/H+ antiporter was directly measured using microphysiometry. The direction of transmembrane proton flux mediated by this antiporter was reversible, with protons being imported or exported in response to the external concentration of sodium. This bidirectional activity was also detected in S. cerevisiae strains expressing sod2 and expression of this gene complemented the sodium and lithium sensitivity resulting from inactivation of the ENA1/PMR2 encoded Na+-exporting ATPases. This suggests that antiporters or sodium pumps can be utilized interchangeably by S. cerevisiae to regulate internal sodium concentration. Potent inhibitors of mammalian Na+/H+ exchangers were found to have no effect on sod2 activity. The proton flux mediated by sod2 was also found to be unaffected by perturbation of membrane potential or the plasma membrane proton gradient.","authors":"Hahnenberger KM, Jia Z, Young PG","authors_abbrev":"Hahnenberger KM et al.","pubmed_publication_date":"14 May 1996","pubmed_entrez_date":"1996-05-14","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF105077","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29036220","title":"Defective replication initiation results in locus specific chromosome breakage and a ribosomal RNA deficiency in yeast.","citation":"PLoS Genet 2017 Oct;13(10):e1007041","abstract":"A form of dwarfism known as Meier-Gorlin syndrome (MGS) is caused by recessive mutations in one of six different genes (ORC1, ORC4, ORC6, CDC6, CDT1, and MCM5). These genes encode components of the pre-replication complex, which assembles at origins of replication prior to S phase. Also, variants in two additional replication initiation genes have joined the list of causative mutations for MGS (Geminin and CDC45). The identity of the causative MGS genetic variants strongly suggests that some aspect of replication is amiss in MGS patients; however, little evidence has been obtained regarding what aspect of chromosome replication is faulty. Since the site of one of the missense mutations in the human ORC4 alleles is conserved between humans and yeast, we sought to determine in what way this single amino acid change affects the process of chromosome replication, by introducing the comparable mutation into yeast (orc4Y232C). We find that yeast cells with the orc4Y232C allele have a prolonged S-phase, due to compromised replication initiation at the ribosomal DNA (rDNA) locus located on chromosome XII. The inability to initiate replication at the rDNA locus results in chromosome breakage and a severely reduced rDNA copy number in the survivors, presumably helping to ensure complete replication of chromosome XII. Although reducing rDNA copy number may help ensure complete chromosome replication, orc4Y232C cells struggle to meet the high demand for ribosomal RNA synthesis. This finding provides additional evidence linking two essential cellular pathways-DNA replication and ribosome biogenesis.","doi":"10.1371/journal.pgen.1007041","authors":"Sanchez JC, Kwan EX, Pohl TJ, Amemiya HM, Raghuraman MK, Brewer BJ","authors_abbrev":"Sanchez JC et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-10-17","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPBC29A10.15","SPBP23A10.13","SPBC428.18"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:123768","title":"Physiological and genetic modifications of the expression of the yeast mitochondrial adenosine triphosphatase inhibitor.","citation":"Biochim Biophys Acta 1975 Mar 20;376(3):470-8","abstract":"1. The oligomycin-sensitive ATPase activity of submitochondrial particles of the glycerol-grown \"petite-negative\" yeast: Schizosaccharomyces pombe is markedly stimulated by incubation at 40 degrees C and by trypsin activations are treatment. Both increased in Triton-X 100 extracts of the submitochondrial particles. 2. A trypsin-sensitive inhibitory factor of mitochondrial ATPase with properties similar to that of beef heart has been extracted and purified from glycerol-grown and glucose-grown S. pombe wild type, from the nuclear pleiotropic respiratory-deficient mutant S. pombe M126 and from Saccharomyces cerevisiae. 3. ATPase activation by heat is more pronounced in submitochondrial particles isolated from glycerol-grown than from glucose-grown S. pombe. An activation of lower extent is observed in rat liver mitochondrial particles but is barely detectable in the \"petite-positive\" yeast: S. cerevisiae. No activation but inhibition by heat is observed in the pleitotropic respiratory-deficient nuclear mutant S. pombe M126. 4. The inhibition of S. pombe ATPase activity by low concentrations of dicyclohexylcarbodiimide dissapears at inhibitor concentrations above 25 muM. In Triton-extract of submitochondrial particles net stimulation of ATPase activity is observed at 100 muM dicyclohexylcarbodiimide. The pattern of stimulation of ATPase activity by dicyclohexylcarbodiimide in different genetic and physiological conditions parallels that produced by heat and trypsin. A similar mode of action is therefore proposed for the three agents: dissociation or inactivation of an ATPase inhibitory factor. 5. We conclude that \"petite-positive\" and \"petite-negative\" yeasts contain an ATPase inhibitor factor with properties similar to those of the bovine mitochondrial ATPase inhibitor. The expression of the ATPase inhibitor, measured by ATPase activation by heat, trypsin or high concentrations of dicyclohexylcarbodiimide, is sensitive to alterations of the hydrophobic membrane environment and dependent on both physiological state and genetic conditions of the yeast cells.","authors":"Landry Y, Goffeau A","authors_abbrev":"Landry Y et al.","pubmed_publication_date":"20 Mar 1975","pubmed_entrez_date":"1975-03-20","publication_year":"1975","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32415063","title":"Conserved protein Pir2 ARS2  mediates gene repression through cryptic introns in lncRNAs.","citation":"Nat Commun 2020 May 15;11(1):2412","abstract":"Long non-coding RNAs (lncRNAs) are components of epigenetic control mechanisms that ensure appropriate and timely gene expression. The functions of lncRNAs are often mediated through associated gene regulatory activities, but how lncRNAs are distinguished from other RNAs and recruit effector complexes is unclear. Here, we utilize the fission yeast Schizosaccharomyces pombe to investigate how lncRNAs engage silencing activities to regulate gene expression in cis. We find that invasion of lncRNA transcription into the downstream gene body incorporates a cryptic intron required for repression of that gene. Our analyses show that lncRNAs containing cryptic introns are targeted by the conserved Pir2 ARS2  protein in association with splicing factors, which recruit RNA processing and chromatin-modifying activities involved in gene silencing. Pir2 and splicing machinery are broadly required for gene repression. Our finding that human ARS2 also interacts with splicing factors suggests a conserved mechanism mediates gene repression through cryptic introns within lncRNAs.","doi":"10.1038/s41467-020-16280-y","authors":"Thillainadesan G, Xiao H, Holla S, Dhakshnamoorthy J, Jenkins LMM, Wheeler D, Grewal SIS","authors_abbrev":"Thillainadesan G et al.","pubmed_publication_date":"15 May 2020","pubmed_entrez_date":"2020-05-17","publication_year":"2020","canto_session_key":"63f563e7fdecebe3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-31 23:31:49","canto_approved_date":"2024-02-21 20:38:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-23 12:19:46","canto_added_date":"2020-05-18 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":44,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPAC1F3.01","SPAC1006.03c","SPNCRNA.1712","SPAC6G10.07","SPBC1D7.05","SPCC1739.03","SPCC736.12c","SPAC4A8.09c","SPCC736.11","SPNCRNA.1459","SPBC725.08","SPBC215.12","SPBC1289.04c","SPBC800.03"],"gene_count":15,"ltp_gene_count":12,"approved_date":"2024-01-31"},{"uniquename":"PMID:16931329","title":"Discovering new MAP kinase inhibitors.","citation":"Chem Biol 2006 Aug;13(8):807-9","abstract":"The current study by Kim et al. (in this issue of Chemistry & Biology) uses a genetic approach with the yeast Schizosaccharomyces pombe to identify a highly specific inhibitor of Spc1 MAP kinase that competes with protein substrates for Spc1 interactions, but not with ATP binding.","authors":"Shapiro P","authors_abbrev":"Shapiro P","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-26","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17627824","title":"The kinetochore proteins Pcs1 and Mde4 and heterochromatin are required to prevent merotelic orientation.","citation":"Curr Biol 2007 Jul 17;17(14):1190-200","abstract":"Accurate chromosome segregation depends on the establishment of correct-amphitelic-kinetochore orientation. Merotelic kinetochore orientation is an error that occurs when a single kinetochore attaches to microtubules emanating from opposite spindle poles, a condition that hinders segregation of the kinetochore to a spindle pole in anaphase. To avoid chromosome missegregation resulting from merotelic kinetochore orientation, cells have developed mechanisms to prevent or correct merotelic attachment. A protein called Pcs1 has been implicated in preventing merotelic attachment in mitosis and meiosis II in the fission yeast S. pombe.\nWe report that Pcs1 forms a complex with a protein called Mde4. Both Pcs1 and Mde4 localize to the central core of centromeres. Deletion of mde4(+), like that of pcs1(+), causes the appearance of lagging chromosomes during the anaphases of mitotic and meiosis II cells. We provide evidence that the kinetochores of lagging chromosomes in both pcs1 and mde4 mutant cells are merotelically attached. In addition, we find that lagging chromosomes in cells with defective centromeric heterochromatin also display features consistent with merotelic attachment.\nWe suggest that the Pcs1/Mde4 complex is the fission yeast counterpart of the budding yeast monopolin subcomplex Csm1/Lrs4, which promotes the segregation of sister kinetochores to the same pole during meiosis I. We propose that the Pcs1/Mde4 complex acts in the central kinetochore domain to clamp microtubule binding sites together, the centromeric heterochromatin coating the flanking domains provides rigidity, and both systems contribute to the prevention of merotelic attachment.","authors":"Gregan J, Riedel CG, Pidoux AL, Katou Y, Rumpf C, Schleiffer A, Kearsey SE, Shirahige K, Allshire RC, Nasmyth K","authors_abbrev":"Gregan J et al.","pubmed_publication_date":"17 Jul 2007","pubmed_entrez_date":"2007-07-14","publication_year":"2007","canto_session_key":"24e3e08acf5d7b17","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-11-10 20:01:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-12 17:09:58","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.04c","SPBC18E5.03c","SPAC1782.09c","SPAC27F1.04c","SPBC1861.01c","YDR439W","SPBC6B1.04","SPAC11E3.03","SPBC428.08c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2015-02-12"},{"uniquename":"PMID:1776364","title":"Repression of a mating type cassette in the fission yeast by four DNA elements.","citation":"Yeast 1991 Oct;7(7):745-55","abstract":"The fission yeast, Schizosaccharomyces pombe, expresses one of two alternative mating types. They are specified by one of two determinants (M or P) present at the mat1 locus. In addition, silent copies of M and P are present on the same chromosome. In the present work we demonstrate that the difference between the active and the silent stage of the P determinant is controlled by four repressive elements that are located at the silent locus. There are two elements to the left and two to the right of the mating type cassette. Both elements to the left and either one of the two elements to the right are required for an effective blockage of transcription. When they are combined, the four elements define a highly efficient silencer functionally similar to the HMRE and HMLE and HMLI silencers in Saccharomyces cerevisiae. In addition, the DNA surrounding the silent P locus confers symmetric partitioning in mitosis to Schizosaccharomyces pombe ars plasmids.","authors":"Ekwall K, Nielsen O, Ruusala T","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"Oct 1991","pubmed_entrez_date":"1991-10-01","publication_year":"1991","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17057391","title":"Effects of potentised substances on growth kinetics of Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Forsch Komplementmed 2006 Oct;13(5):298-306","abstract":"Homeopathic potencies are used as specific remedies in complementary medicine. Since the mode of action is unknown, the presumed specificity is discussed controversially.\nThis study investigated the effects of potentised substances on two yeast species, Saccharomyces cerevisiae and Schizosaccharomyces pombe, in a stable and reliable test system with systematic negative controls.\nYeast cells were cultivated in either potentised substances or water controls in microplates and their growth kinetics were measured photometrically. Water control runs were performed repeatedly to investigate the stability of the experimental set-up (systematic negative controls).\n4 out of 14 screened substances seem to have affected the growth curve parameters slope or yield. Out of these substances, azoxystrobin and phosphorus were chosen for 8 further replication experiments, which partly confirmed the results of the screening. On the average of all experiments, azoxystrobin affected the slope of the growth curve of Saccharomyces cerevisiae (p < 0.05), and phosphorus affected the slope of the growth curve of Schizosaccharomyces pombe (p < 0.05). No effects were seen in the water control runs. In addition, significant interactions between treatment with potentised substances and experiment number were observed in all experiments with potentised substances (p < 0.01), but not in the water control runs.\nBoth yeast species reacted to certain potentised substances by changing their growth kinetics. However, the interactions found point to additional factors of still unknown nature, that modulate the effects of potentised substances. This stable test system with yeasts may be suitable for further studies regarding the efficacy of homeopathic potencies.","authors":"Scherr C, Baumgartner S, Spranger J, Simon M","authors_abbrev":"Scherr C et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-10-24","publication_year":"2006","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26483559","title":"Nup132 modulates meiotic spindle attachment in fission yeast by regulating kinetochore assembly.","citation":"J Cell Biol 2015 Oct 26;211(2):295-308","abstract":"During meiosis, the kinetochore undergoes substantial reorganization to establish monopolar spindle attachment. In the fission yeast Schizosaccharomyces pombe, the KNL1-Spc7-Mis12-Nuf2 (KMN) complex, which constitutes the outer kinetochore, is disassembled during meiotic prophase and is reassembled before meiosis I. Here, we show that the nucleoporin Nup132 is required for timely assembly of the KMN proteins: In the absence of Nup132, Mis12 and Spc7 are precociously assembled at the centromeres during meiotic prophase. In contrast, Nuf2 shows timely dissociation and reappearance at the meiotic centromeres. We further demonstrate that depletion of Nup132 activates the spindle assembly checkpoint in meiosis I, possibly because of the increased incidence of erroneous spindle attachment at sister chromatids. These results suggest that precocious assembly of the kinetochores leads to the meiosis I defects observed in the nup132-disrupted mutant. Thus, we propose that Nup132 plays an important role in establishing monopolar spindle attachment at meiosis I through outer kinetochore reorganization at meiotic prophase.","doi":"10.1083/jcb.201501035","authors":"Yang HJ, Asakawa H, Haraguchi T, Hiraoka Y","authors_abbrev":"Yang HJ et al.","pubmed_publication_date":"26 Oct 2015","pubmed_entrez_date":"2015-10-21","publication_year":"2015","canto_session_key":"614edec10b9e3e6a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hui-Ju Yang","canto_first_approved_date":"2017-02-03 13:10:52","canto_approved_date":"2023-09-12 09:32:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-01 12:46:37","canto_added_date":"2015-10-22 00:19:31","annotation_curators":[{"name":"Hui-Ju Yang","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.03","SPCC1020.02","SPBP35G2.03c","SPAC27F1.04c","SPBC409.04c","SPCC1322.12c","SPBC2G2.14","SPBC20F10.06","SPAC1805.04"],"gene_count":9,"ltp_gene_count":5,"approved_date":"2017-02-03"},{"uniquename":"EMBL:AU008494","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9860839","title":"Calnexin and BiP interact with acid phosphatase independently of glucose trimming and reglucosylation in Schizosaccharomyces pombe.","citation":"Biochemistry 1998 Dec 08;37(49):17253-61","abstract":"The association of newly synthesized glycoproteins with the ER molecular chaperones calnexin and immunoglobulin binding protein (BiP) has been well documented in a variety of higher eukaryotes. Here we report that Cnx1p, the calnexin homologue in Schizosaccharomyces pombe, associates with newly synthesized molecules of the secreted glycoprotein acid phosphatase. Unlike ligand binding to mammalian calnexin, glucose trimming and reglucosylation of acid phosphatase by UDP-Glc:glycoprotein glucosyltransferase were shown to be dispensable for its binding to Cnx1p. Thus, despite the essentiality of Cnx1p for S. pombe viability, the glucose trimming and reglucosylation cycle does not appear to be required for protein folding in the fission yeast. The association of core-glycosylated acid phosphatase with Cnx1p after exposure of cells to heat shock or to DTT was shown to be reversible. However, Cnx1p stably associated with unglycosylated acid phosphatase after treatment with the core-glycosylation inhibitor tunicamycin. BiP was found to coprecipitate with Cnx1p, under normal and stress conditions, and following inhibition of protein synthesis by cycloheximide. We postulate that Cnx1p and BiP are part of a complex that is involved in the folding of both core-glycosylated trimmed ligands and unglycosylated proteins.","authors":"Jannatipour M, Callejo M, Parodi AJ, Armstrong J, Rokeach LA","authors_abbrev":"Jannatipour M et al.","pubmed_publication_date":"08 Dec 1998","pubmed_entrez_date":"1998-12-23","publication_year":"1998","canto_session_key":"321f6ad9992cc869","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-16 16:49:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-16 16:49:45","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.06","SPAC22A12.15c","SPAC3C7.11c","SPBC428.03c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-12-16"},{"uniquename":"PMID:32824370","title":"Nuclear Envelope Proteins Modulating the Heterochromatin Formation and Functions in Fission Yeast.","citation":"Cells 2020 Aug 16;9(8)","abstract":"The nuclear envelope (NE) consists of the inner and outer nuclear membranes (INM and ONM), and the nuclear pore complex (NPC), which penetrates the double membrane. ONM continues with the endoplasmic reticulum (ER). INM and NPC can interact with chromatin to regulate the genetic activities of the chromosome. Studies in the fission yeast  Schizosaccharomyces pombe  have contributed to understanding the molecular mechanisms underlying heterochromatin formation by the RNAi-mediated and histone deacetylase machineries. Recent studies have demonstrated that NE proteins modulate heterochromatin formation and functions through interactions with heterochromatic regions, including the pericentromeric and the sub-telomeric regions. In this review, we first introduce the molecular mechanisms underlying the heterochromatin formation and functions in fission yeast, and then summarize the NE proteins that play a role in anchoring heterochromatic regions and in modulating heterochromatin formation and functions, highlighting roles for a conserved INM protein, Lem2.","doi":"10.3390/cells9081908","authors":"Hirano Y, Asakawa H, Sakuno T, Haraguchi T, Hiraoka Y","authors_abbrev":"Hirano Y et al.","pubmed_publication_date":"16 Aug 2020","pubmed_entrez_date":"2020-08-23","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-08-24 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:36186482","title":"The DNA damage checkpoint: A tale from budding yeast.","citation":"Front Genet 2022;13:995163","abstract":"Studies performed in the yeasts  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe  have led the way in defining the DNA damage checkpoint and in identifying most of the proteins involved in this regulatory network, which turned out to have structural and functional equivalents in humans. Subsequent experiments revealed that the checkpoint is an elaborate signal transduction pathway that has the ability to sense and signal the presence of damaged DNA and transduce this information to influence a multifaceted cellular response that is essential for cancer avoidance. This review focuses on the work that was done in  Saccharomyces cerevisiae  to articulate the checkpoint concept, to identify its players and the mechanisms of activation and deactivation.","doi":"10.3389/fgene.2022.995163","authors":"Pizzul P, Casari E, Gnugnoli M, Rinaldi C, Corallo F, Longhese MP","authors_abbrev":"Pizzul P et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-10-03","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-10-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10077566","title":"The fission yeast homologue of Orc4p binds to replication origin DNA via multiple AT-hooks.","citation":"Proc Natl Acad Sci U S A 1999 Mar 16;96(6):2656-61","abstract":"The origin recognition complex (ORC) was originally identified in the yeast Saccharomyces cerevisiae as a protein that specifically binds to origins of DNA replication. Although ORC appears to play an essential role in the initiation of DNA replication in the cells of all eukaryotes, its interactions with DNA have not been defined in species other than budding yeast. We have characterized a Schizosaccharomyces pombe homologue of the ORC subunit, Orc4p. The homologue (Orp4p) consists of two distinct functional domains. The C-terminal domain shows strong sequence similarity to human, frog, and yeast Orc4 proteins, including conserved ATP-binding motifs. The N-terminal domain contains nine copies of the AT-hook motif found in a number of DNA-binding proteins, including the members of the HMG-I(Y) family of chromatin proteins. AT-hook motifs are known from biochemical and structural studies to mediate binding to the minor groove of AT-tracts in DNA. Orp4p is essential for viability of Sc. pombe and is expressed throughout the cell cycle. The Orp4 protein (and its isolated N-terminal domain) binds to the Sc. pombe replication origin, ars1. The DNA binding properties of Orp4p provide a plausible explanation for the characteristic features of Sc. pombe origins of replication, which differ significantly from those of Sa. cerevisiae.","authors":"Chuang RY, Kelly TJ","authors_abbrev":"Chuang RY et al.","pubmed_publication_date":"16 Mar 1999","pubmed_entrez_date":"1999-03-17","publication_year":"1999","canto_session_key":"f0bafc3507c42594","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-07-04 09:47:36","canto_approved_date":"2021-04-16 15:46:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-01 15:18:17","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-04"},{"uniquename":"PMID:11268035","title":"The Ras pathway and spindle assembly collide?","citation":"Bioessays 2001 Apr;23(4):307-10","abstract":"Although alterations in Ras signalling are found in about 30% of human cancers, the transforming activity of oncogenic Ras is not fully understood. In a recent paper, a putative Ras1 effector in S. pombe, named Scd1, was reported to localize to mitotic spindles. Scd1 physically associates with Moe1, a factor that may contribute to the inherent instability of microtubules (MTs) and appears to be needed for proper spindle function. Altered MT dynamics within the spindle are likely to affect spindle assembly and chromosome capture, processes that need to be delicately controlled if cells are to guard against genome instability and transformation. BioEssays 23:307-310, 2001.","authors":"Segal M, Clarke DJ","authors_abbrev":"Segal M et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-03-27","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23834287","title":"A cross-kingdom Nudix enzyme that pre-empts damage in thiamin metabolism.","citation":"Biochem J 2013 Sep 15;454(3):533-42","abstract":"Genes specifying the thiamin monophosphate phosphatase and adenylated thiazole diphosphatase steps in fungal and plant thiamin biosynthesis remain unknown, as do genes for ThDP (thiamin diphosphate) hydrolysis in thiamin metabolism. A distinctive Nudix domain fused to Tnr3 (thiamin diphosphokinase) in Schizosaccharomyces pombe was evaluated as a candidate for these functions. Comparative genomic analysis predicted a role in thiamin metabolism, not biosynthesis, because free-standing homologues of this Nudix domain occur not only in fungi and plants, but also in proteobacteria (whose thiamin biosynthesis pathway has no adenylated thiazole or thiamin monophosphate hydrolysis steps) and animals (which do not make thiamin). Supporting this prediction, recombinant Tnr3 and its Saccharomyces cerevisiae, Arabidopsis and maize Nudix homologues lacked thiamin monophosphate phosphatase activity, but were active against ThDP, and up to 60-fold more active against diphosphates of the toxic thiamin degradation products oxy- and oxo-thiamin. Deleting the S. cerevisiae Nudix gene (YJR142W) lowered oxythiamin resistance, overexpressing it raised resistance, and expressing its plant or bacterial counterparts restored resistance to the YJR142W deletant. By converting the diphosphates of damaged forms of thiamin into monophosphates, the Tnr3 Nudix domain and its homologues can pre-empt the misincorporation of damaged diphosphates into ThDP-dependent enzymes, and the resulting toxicity.","doi":"10.1042/BJ20130516","authors":"Goyer A, Hasnain G, Frelin O, Ralat MA, Gregory JF, Hanson AD","authors_abbrev":"Goyer A et al.","pubmed_publication_date":"15 Sep 2013","pubmed_entrez_date":"2013-07-10","publication_year":"2013","canto_session_key":"e050b57fa832737c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-02-09 15:28:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-01 13:19:40","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-08-01"},{"uniquename":"PMID:8196614","title":"Two types of RAS mutants that dominantly interfere with activators of RAS.","citation":"Mol Cell Biol 1994 Jun;14(6):3707-18","abstract":"In the fission yeast Schizosaccharomyces pombe, ras1 regulates both sexual development (conjugation and sporulation) and cellular morphology. Two types of dominant interfering mutants were isolated in a genetic screen for ras1 mutants that blocked sexual development. The first type of mutation, at Ser-22, analogous to the H-rasAsn-17 mutant (L. A. Feig and G. M. Cooper, Mol. Cell. Biol. 8:3235-3243, 1988), blocked only conjugation, whereas a second type of mutation, at Asp-62, interfered with conjugation, sporulation, and cellular morphology. Analogous mutations at position 64 of Saccharomyces cerevisiae RAS2 or position 57 of human H-ras also resulted in dominant interfering mutants that interfered specifically and more profoundly than mutants of the first type with RAS-associated pathways in both S. pombe or S. cerevisiae. Genetic evidence indicating that both types of interfering mutants function upstream of RAS is provided. Biochemical evidence showing that the mutants are altered in their interaction with the CDC25 class of exchange factors is presented. We show that both H-rasAsn-17 and H-rasTyr-57, compared with wild-type H-ras, are defective in their guanine nucleotide-dependent release from human cdc25 and that this defect is more severe for the H-rasTyr-57 mutant. Such a defect would allow the interfering mutants to remain bound to, thereby sequestering RAS exchange factors. The more severe interference phenotype of this novel interfering mutant suggests that it functions by titrating out other positive regulators of RAS besides those encoded by ste6 and CDC25.","authors":"Jung V, Wei W, Ballester R, Camonis J, Mi S, Van Aelst L, Wigler M, Broek D","authors_abbrev":"Jung V et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37932617","title":"Selenoneine Is Methylated in the Bodies of Mice and then Excreted in Urine as Se-Methylselenoneine.","citation":"Biol Trace Elem Res 2023 Nov 07;","abstract":"Oral intake of purified selenoneine and seafoods has been reported to result in selenoneine accumulation in erythrocytes in mice and human. In addition, Se-methylselenoneine was suggested to be produced as a metabolite of selenoneine in the urine and whole blood of humans. In order to confirm the molecular mechanism of production of Se-methylselenoneine, a stable isotope (Se-76) labeled selenoneine was biosynthesized using genetically modified fission yeast and administered to mice. The Se-76-labeled Se-methylselenoneine was detected in urine but Se-78 and Se-80-labeled Se-methylselenoneine arising from natural isotopes of Se was hardly detected. These results suggest that Se-methylselenoneine was a metabolite and the excreted form of selenoneine. The methylation of selenoneine in mice administered selenoneine continuously was evaluated by the analyses of organs using an online liquid chromatograph system with an inductively coupled plasma mass spectrometer (LC-ICP-MS). These experiments indicate that selenoneine is methylated in the liver and (or) kidneys.","doi":"10.1007/s12011-023-03936-1","authors":"Seko T, Uchida H, Sato Y, Imamura S, Ishihara K, Yamashita Y, Yamashita M","authors_abbrev":"Seko T et al.","pubmed_publication_date":"07 Nov 2023","pubmed_entrez_date":"2023-11-06","publication_year":"2023","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2023-11-08 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41926382","title":"Mitochondrial NAD kinase Pos5 is required for CoQ biosynthesis in yeasts.","citation":"PLoS One 2026;21(4):e0346295","abstract":"Coenzyme Q (CoQ) is an essential component of the electron transport chain, and ten genes involved in CoQ biosynthesis have been identified in Schizosaccharomyces pombe. To gain further insight into CoQ biosynthesis, we screened the Bioneer gene-deletion library and found that the Δpos5 strain produced only 0.2-fold of the wild-type CoQ10 level. Pos5 shares homology with Saccharomyces cerevisiae Pos5 (ScPos5), a mitochondrial NADH (or NAD+) kinase that generates NADPH (or NADP+). Heterologous expression of ScPOS5 in the S. pombe Δpos5 strain recovered CoQ content to 0.9-fold of the wild-type level, indicating functional conservation of Pos5 between the two yeasts. Consistently, CoQ6 level in ΔScpos5 was decreased to 0.2-fold of that in the wild-type strain. The Δpos5 strain exhibited several phenotypes characteristic of CoQ-deficient S. pombe, including inability to grow on non-fermentable carbon sources, hypersensitivity to oxidative stress, and high sulfide production. Among CoQ biosynthetic enzymes, Coq6 monooxygenase is thought to utilize NADPH. Supplementation with VA or PHB partially restored CoQ production in the Δpos5 strain, while overexpression of coq6 had negligible effect. These findings suggest that Pos5 is required for the earlier step of CoQ biosynthesis.","doi":"10.1371/journal.pone.0346295","authors":"Nishihara S, Nishida I, Matsuo Y, Kaino T, Kawamukai M","authors_abbrev":"Nishihara S et al.","pubmed_publication_date":"2026","pubmed_entrez_date":"2026-04-02","publication_year":"2026","canto_session_key":"0765b92a05fc46bf","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-02 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28007890","title":"Multiple Transcriptional and Post-transcriptional Pathways Collaborate to Control Sense and Antisense RNAs of Tf2 Retroelements in Fission Yeast.","citation":"Genetics 2017 Feb;205(2):621-632","abstract":"Retrotransposons are mobile genetic elements that colonize eukaryotic genomes by replicating through an RNA intermediate. As retrotransposons can move within the host genome, defense mechanisms have evolved to repress their potential mutagenic activities. In the fission yeast Schizosaccharomyces pombe, the mRNA of Tf2 long terminal repeat retrotransposons is targeted for degradation by the 3'-5' exonucleolytic activity of the exosome-associated protein Rrp6. Here, we show that the nuclear poly(A)-binding protein Pab2 functions with Rrp6 to negatively control Tf2 mRNA accumulation. Furthermore, we found that Pab2/Rrp6-dependent RNA elimination functions redundantly to the transcriptional silencing mediated by the CENP-B homolog, Abp1, in the suppression of antisense Tf2 RNA accumulation. Interestingly, the absence of Pab2 attenuated the derepression of Tf2 transcription and the increased frequency of Tf2 mobilization caused by the deletion of abp1 Our data also reveal that the expression of antisense Tf2 transcripts is developmentally regulated and correlates with decreased levels of Tf2 mRNA. Our findings suggest that transcriptional and post-transcriptional pathways cooperate to control sense and antisense RNAs expressed from Tf2 retroelements.","doi":"10.1534/genetics.116.193870","authors":"Mallet PL, Larochelle M, Bachand F","authors_abbrev":"Mallet PL et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-12-24","publication_year":"2017","canto_session_key":"cd63b8bce70b7881","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-12-24 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPJ760.02c","SPBC1105.04c","SPAC1F3.01","SPBC16E9.12c"],"gene_count":4,"ltp_gene_count":3},{"uniquename":"PMID:39991135","title":"Reversal of metformin's anti-proliferative effect in fission yeast  efr3  and  dnm1  (DRP1) mutants with elongated mitochondria.","citation":"NPJ Metab Health Dis 2025;3(1):5","abstract":"Metformin is a well-tolerated drug frequently prescribed for managing type 2 diabetes. Extended metformin use has been linked to a significant decrease in cancer incidence across both diabetic and non-diabetic populations. Here we investigate the anti-proliferative effects of metformin on fission yeast  S. pombe . Our findings demonstrate that metformin's inhibitory impact on cell proliferation is effective in the absence of AMP-activated protein kinase (AMPK). Using an unbiased genetic screen we identified the plasma membrane signalling scaffold Efr3, critical for phosphatidylinositol signalling and the generation of PI4Ps, as a key determinant of resistance to the anti-proliferative effect of metformin. Deletion of  efr3  resulted in both AMPK-dependent and AMPK-independent resistance to metformin. We show that Efr3 does not influence cell proliferation by controlling Ras1 activity or its cellular localization in yeast. We observe that  dnm1  (DRP1) mutants with elongated mitochondria are also resistant to the anti-proliferative effect of metformin and that metformin treatment promotes mitochondrial fusion. Metabolic measurements after prolonged metformin exposure demonstrated a reduction in respiration in both wild type and the  efr3  deletion, however, that reduction is less pronounced in the  efr3  deletion, which also contained elongated mitochondria. It is likely that mitochondrial fusion enhances yeast fitness in response to metformin exposure. Together we provide a new perspective on the cellular response to metformin.","doi":"10.1038/s44324-024-00048-9","authors":"Gillespie A, Mehdorn AS, Lim TQ, Wang T, Mooney BA, Ovens AJ, Orang A, Oakhill JS, Michael MZ, Petersen J","authors_abbrev":"Gillespie A et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-02-24","publication_year":"2025","canto_session_key":"bfc6f70ac887db05","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-02-25 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010979","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20178736","title":"Primal RNAs: The end of the beginning?","citation":"Cell 2010 Feb 19;140(4):452-4","abstract":"The amplification of small RNAs and the assembly of heterochromatin are mutually dependent processes in fission yeast. But which comes first? Halic and Moazed (2010) propose that primal small RNAs initiate the amplification of small interfering RNAs that drive heterochromatin formation and chromatin silencing.","doi":"10.1016/j.cell.2010.02.005","authors":"Conte D, Mello CC","authors_abbrev":"Conte D et al.","pubmed_publication_date":"19 Feb 2010","pubmed_entrez_date":"2010-02-25","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ617330","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.445"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8668536","title":"An essential domain in Saccharomyces cerevisiae U14 snoRNA is absent in vertebrates, but conserved in other yeasts.","citation":"Nucleic Acids Res 1996 Jun 01;24(11):2059-66","abstract":"U14 is a small nucleolar RNA (snoRNA) required for early cleavages of eukaryotic precursor rRNA. The U14 RNA from Saccharomyces cerevisiae is distinguished from its vertebrate homologues by the presence of a stem-loop domain that is essential for function. This element, known as the Y-domain, is located in the U14 sequence between two universal sequences that base pair with 18S rRNA. Sequence data obtained for the U14 homologues from four additional phylogenetically distinct yeasts showed the Y-domain is not unique to S.cerevisiae. Comparison of the five Y-domain sequences revealed a common stem-loop structure with a conserved loop sequence that includes eight invariant nucleotides. Conservation of these features suggests that the Y-domain is a recognition signal for an essential interaction. Several plant U14 RNAs were found to contain similar structures, though with an unrelated consensus sequence in the loop portion. The U14 gene from the most distantly related yeast, Schizosaccharomyces pombe, was found to be active in S.cerevisiae, showing that Y-domain function is conserved and that U14 function can be provided by variants in which the essential elements are embedded in dissimilar flanking sequences. This last result suggests that U14 function may be determined solely by the essential elements.","authors":"Samarsky DA, Schneider GS, Fournier MJ","authors_abbrev":"Samarsky DA et al.","pubmed_publication_date":"01 Jun 1996","pubmed_entrez_date":"1996-06-01","publication_year":"1996","canto_session_key":"c82ef50b8ec67d38","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-23 16:29:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-23 16:29:27","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.21"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-23"},{"uniquename":"PMID:18358811","title":"Cohesin complex promotes transcriptional termination between convergent genes in S. pombe.","citation":"Cell 2008 Mar 21;132(6):983-95","abstract":"Transcription analyses reported in these studies reveal that convergent genes in S. pombe generate overlapping transcripts in the G1 phase of the cell cycle. We show that this double-strand (ds) RNA induces localized RNAi (Dicer and RITS) dependent transient heterochromatin structures including histone H3 lysine 9 trimethylation marks and Swi6 association. Consequently cohesin is recruited to these chromosomal positions through interaction with Swi6. In G2, localized cohesin is further concentrated into the intergenic regions of the convergent genes tested. This results in a block to further dsRNA formation by promoting gene-proximal transcription termination between the convergent genes. Cohesin release at mitosis leads to a new G1 phase with repeated dsRNA formation, transient heterochromatin, and cohesin recruitment. Our results uncover a hitherto unanticipated role for cohesin and further suggest a widespread role for the selective formation of dsRNA, heterochromatin, and subsequent cohesin recruitment in regulated transcriptional termination.","doi":"10.1016/j.cell.2008.02.040","authors":"Gullerova M, Proudfoot NJ","authors_abbrev":"Gullerova M et al.","pubmed_publication_date":"21 Mar 2008","pubmed_entrez_date":"2008-03-25","publication_year":"2008","canto_session_key":"871b61856df0e30e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18182845","title":"Expression, characterization and regulation of a Saccharomyces cerevisiae monothiol glutaredoxin (Grx6) gene in Schizosaccharomyces pombe.","citation":"Mol Cells 2007 Dec 31;24(3):316-22","abstract":"Glutaredoxins (Grxs), also known as thioltransferases (TTases), are thiol oxidoreductases that regulate cellular redox state in a variety of organisms. In the budding yeast Saccharomyces cerevisiae, Grx1 and 2 are cytosolic dithiol Grxs, while Grx3, 4 and 5 are monothiol Grxs. A gene encoding a new monothiol Grx, Grx6, was cloned from the genomic DNA of S. cerevisiae by PCR. Its DNA sequence contains 1,080 bp, and encodes a putative protein of 203 amino acid residues containing Cys-Phe-Tyr-Ser at the active site. Grx6 is similar to other monothiol Grxs in the same organism and to Grx3 in the fission yeast Schizosaccharomyces pombe. and its predicted three-dimensional structure resembles that of S. pombe Grx3. S. pombe cells harboring plasmid pFGRX6 containing the Grx6 gene had about 1.3-fold elevated Grx activity in the exponential phase, and grew better than the control cells under some stressful conditions. Synthesis of beta-galactosidase from a Grx6-lacZ fusion gene in S. pombe was enhanced by potassium chloride, aluminum chloride and heat (37 degrees C) treatment. S. pombe cells harboring plasmid pFGRX6 had elevated ROS levels whereas S. pombe cells harboring extra copies of Grx3 had reduced ROS levels.","authors":"Lee JH, Kim K, Park EH, Ahn K, Lim CJ","authors_abbrev":"Lee JH et al.","pubmed_publication_date":"31 Dec 2007","pubmed_entrez_date":"2008-01-10","publication_year":"2007","canto_session_key":"19a41e4d5bb746f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-31 15:17:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-14 15:52:50","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.06","SPCC1450.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-10-14"},{"uniquename":"PMID:36515990","title":"Meiotic nuclear pore complex remodeling provides key insights into nuclear basket organization.","citation":"J Cell Biol 2023 Feb 06;222(2)","abstract":"Nuclear pore complexes (NPCs) are large proteinaceous assemblies that mediate nuclear compartmentalization. NPCs undergo large-scale structural rearrangements during mitosis in metazoans and some fungi. However, our understanding of NPC remodeling beyond mitosis remains limited. Using time-lapse fluorescence microscopy, we discovered that NPCs undergo two mechanistically separable remodeling events during budding yeast meiosis in which parts or all of the nuclear basket transiently dissociate from the NPC core during meiosis I and II, respectively. Meiosis I detachment, observed for Nup60 and Nup2, is driven by Polo kinase-mediated phosphorylation of Nup60 at its interface with the Y-complex. Subsequent reattachment of Nup60-Nup2 to the NPC core is facilitated by a lipid-binding amphipathic helix in Nup60. Preventing Nup60-Nup2 reattachment causes misorganization of the entire nuclear basket in gametes. Strikingly, meiotic nuclear basket remodeling also occurs in the distantly related fission yeast, Schizosaccharomyces pombe. Our study reveals a conserved and developmentally programmed aspect of NPC plasticity, providing key mechanistic insights into the nuclear basket organization.","doi":"10.1083/jcb.202204039","authors":"King GA, Wettstein R, Varberg JM, Chetlapalli K, Walsh ME, Gillet LCJ, Hernández-Armenta C, Beltrao P, Aebersold R, Jaspersen SL, Matos J, Ünal E","authors_abbrev":"King GA et al.","pubmed_publication_date":"06 Feb 2023","pubmed_entrez_date":"2022-12-14","publication_year":"2023","canto_session_key":"0f7ccc1cecc4d84c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-12-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22737087","title":"The CCR4-NOT complex is implicated in the viability of aneuploid yeasts.","citation":"PLoS Genet 2012;8(6):e1002776","abstract":"To identify the genes required to sustain aneuploid viability, we screened a deletion library of non-essential genes in the fission yeast Schizosaccharomyces pombe, in which most types of aneuploidy are eventually lethal to the cell. Aneuploids remain viable for a period of time and can form colonies by reducing the extent of the aneuploidy. We hypothesized that a reduction in colony formation efficiency could be used to screen for gene deletions that compromise aneuploid viability. Deletion mutants were used to measure the effects on the viability of spores derived from triploid meiosis and from a chromosome instability mutant. We found that the CCR4-NOT complex, an evolutionarily conserved general regulator of mRNA turnover, and other related factors, including poly(A)-specific nuclease for mRNA decay, are involved in aneuploid viability. Defective mutations in CCR4-NOT complex components in the distantly related yeast Saccharomyces cerevisiae also affected the viability of spores produced from triploid cells, suggesting that this complex has a conserved role in aneuploids. In addition, our findings suggest that the genes required for homologous recombination repair are important for aneuploid viability.","doi":"10.1371/journal.pgen.1002776","authors":"Tange Y, Kurabayashi A, Goto B, Hoe KL, Kim DU, Park HO, Hayles J, Chikashige Y, Tsutumi C, Hiraoka Y, Yamao F, Nurse P, Niwa O","authors_abbrev":"Tange Y et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-06-28","publication_year":"2012","canto_session_key":"1fc7b14866f0e4e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2020-06-16 16:53:16","canto_approved_date":"2026-02-11 09:37:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-05-29 11:02:31","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":42,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.06c","SPAC1B1.04c","SPBC20F10.06","SPAC20H4.07","SPAC1610.03c","SPBC1921.03c","SPAC1B3.05","SPCC4G3.15c","SPAC664.01c","SPCC31H12.08c","SPBC336.14c","SPBC342.05","SPAC13C5.07","SPAC1782.09c","SPAC664.15","SPAPB1E7.06c","SPAC29B12.06c","SPCC18.06c","SPAC20G4.01","SPBC216.05","SPAC4F10.14c","SPBC32F12.04","SPAC644.14c","SPAC3C7.03c"],"gene_count":24,"ltp_gene_count":22,"approved_date":"2020-06-16"},{"uniquename":"EMBL:AU007084","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11584278","title":"Proteins containing the UBA domain are able to bind to multi-ubiquitin chains.","citation":"Nat Cell Biol 2001 Oct;3(10):939-43","abstract":"The UBA domain is a motif found in a variety of proteins, some of which are associated with the ubiquitin-proteasome system. We describe the isolation of a fission-yeast gene, mud1+, which encodes a UBA domain containing protein that is able to bind multi-ubiquitin chains. We show that the UBA domain is responsible for this activity. Two other proteins containing this motif, the fission-yeast homologues of Rad23 and Dsk2, are also shown to bind multi-ubiquitin chains via their UBA domains. These two proteins are implicated, along with the fission-yeast Pus1(S5a/Rpn10) subunit of the 26 S proteasome, in the recognition and turnover of substrates by this proteolytic complex.","authors":"Wilkinson CR, Seeger M, Hartmann-Petersen R, Stone M, Wallace M, Semple C, Gordon C","authors_abbrev":"Wilkinson CR et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-10-05","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC637.10c","SPBP19A11.03c","SPBC4F6.15c","SPAC26A3.16","SPAC56F8.08","SPAC3F10.13","SPBC2D10.12","SPBC29B5.01"],"gene_count":8,"ltp_gene_count":7},{"uniquename":"PMID:28934464","title":"Recruitment and delivery of the fission yeast Rst2 transcription factor via a local genome structure counteracts repression by Tup1-family corepressors.","citation":"Nucleic Acids Res 2017 Sep 19;45(16):9361-9371","abstract":"Transcription factors (TFs) determine the transcription activity of target genes and play a central role in controlling the transcription in response to various environmental stresses. Three dimensional genome structures such as local loops play a fundamental role in the regulation of transcription, although the link between such structures and the regulation of TF binding to cis-regulatory elements remains to be elucidated. Here, we show that during transcriptional activation of the fission yeast fbp1 gene, binding of Rst2 (a critical C2H2 zinc-finger TF) is mediated by a local loop structure. During fbp1 activation, Rst2 is first recruited to upstream-activating sequence 1 (UAS1), then it subsequently binds to UAS2 (a critical cis-regulatory site located approximately 600 base pairs downstream of UAS1) through a loop structure that brings UAS1 and UAS2 into spatially close proximity. Tup11/12 (the Tup-family corepressors) suppress direct binding of Rst2 to UAS2, but this suppression is counteracted by the recruitment of Rst2 at UAS1 and following delivery to UAS2 through a loop structure. These data demonstrate a previously unappreciated mechanism for the recruitment and expansion of TF-DNA interactions within a promoter mediated by local three-dimensional genome structures and for timely TF-binding via counteractive regulation by the Tup-family corepressors.","doi":"10.1093/nar/gkx555","authors":"Asada R, Umeda M, Adachi A, Senmatsu S, Abe T, Iwasaki H, Ohta K, Hoffman CS, Hirota K","authors_abbrev":"Asada R et al.","pubmed_publication_date":"19 Sep 2017","pubmed_entrez_date":"2017-09-22","publication_year":"2017","canto_session_key":"aabe6ef236eda9f5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-21 19:42:11","canto_approved_date":"2022-09-28 10:40:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-11-11 15:37:42","canto_added_date":"2017-09-23 00:15:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.14c","SPAC3A12.14","SPBC29B5.01","SPAC18B11.10","SPAC6F12.02","SPBC3B8.02","SPBC725.11c","SPAC3G6.01","SPAC630.14c","SPCC1620.14c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2018-11-21"},{"uniquename":"PMID:24146607","title":"Model of fission yeast cell shape driven by membrane-bound growth factors and the cytoskeleton.","citation":"PLoS Comput Biol 2013;9(10):e1003287","abstract":"Fission yeast serves as a model for how cellular polarization machinery consisting of signaling molecules and the actin and microtubule cytoskeleton regulates cell shape. In this work, we develop mathematical models to investigate how these cells maintain a tubular shape of approximately constant diameter. Many studies identify active Cdc42, found in a cap at the inner membrane of growing cell tips, as an important regulator of local cell wall remodeling, likely through control of exocyst tethering and the targeting of other polarity-enhancing structures. First, we show that a computational model with Cdc42-dependent local cell wall remodeling under turgor pressure predicts a relationship between spatial extent of growth signal and cell diameter that is in agreement with prior experiments. Second, we model the consequences of feedback between cell shape and distribution of Cdc42 growth signal at cell tips. We show that stability of cell diameter over successive cell divisions places restrictions on their mutual dependence. We argue that simple models where the spatial extent of the tip growth signal relies solely on geometrical alignment of confined microtubules might lead to unstable width regulation. Third, we study a computational model that combines a growth signal distributed over a characteristic length scale (as, for example, by a reaction-diffusion mechanism) with an axis-sensing microtubules system that places landmarks at positions where microtubule tips touch the cortex. A two-dimensional implementation of this model leads to stable cell diameter for a wide range of parameters. Changes to the parameters of this model reproduce straight, bent, and bulged cell shapes, and we discuss how this model is consistent with other observed cell shapes in mutants. Our work provides an initial quantitative framework for understanding the regulation of cell shape in fission yeast, and a scaffold for understanding this process on a more molecular level in the future.","doi":"10.1371/journal.pcbi.1003287","authors":"Drake T, Vavylonis D","authors_abbrev":"Drake T et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-10-23","publication_year":"2013","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29038548","title":"Transmembrane Segment XI of the Na + /H +  Antiporter of S. pombe is a Critical Part of the Ion Translocation Pore.","citation":"Sci Rep 2017 Oct 16;7(1):12793","abstract":"The Na + /H +  exchanger of the plasma membrane of S. pombe (SpNHE1) removes intracellular sodium in exchange for an extracellular proton. We examined the structure and functional role of amino acids 360-393 of putative transmembrane (TM) segment XI of SpNHE1. Structural analysis suggested that it had a helical propensity over amino acids 360-368, an extended region from 369-378 and was helical over amino acids 379-386. TM XI was sensitive to side chain alterations. Mutation of eight amino acids to alanine resulted in loss of one or both of LiCl or NaCl tolerance when re-introduced into SpNHE1 deficient S. pombe. Mutation of seven other amino acids had minor effects. Analysis of structure and functional mutations suggested that Glu 361  may be involved in cation coordination on the cytoplasmic face of the protein with a negative charge in this position being important. His 367 , Ile 371  and Gly 372  were important in function. Ile 371  may have important hydrophobic interactions with other residues and Gly 372  may be important in maintaining an extended conformation. Several residues from Val 377  to Leu 384  are important in function possibly involved in hydrophobic interactions with other amino acids. We suggest that TM XI forms part of the ion translocation core of this Na + /H +  exchanger.","doi":"10.1038/s41598-017-12701-z","authors":"Dutta D, Shin K, Rainey JK, Fliegel L","authors_abbrev":"Dutta D et al.","pubmed_publication_date":"16 Oct 2017","pubmed_entrez_date":"2017-10-18","publication_year":"2017","canto_session_key":"7ba926c48292fb7d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-10-31 10:00:38","canto_approved_date":"2018-10-31 10:00:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-10-24 16:33:05","canto_added_date":"2017-10-20 00:15:52","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":154,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_29038548_phaf.tsv"}],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-31"},{"uniquename":"PMID:22505722","title":"Histone H2B ubiquitylation promotes activity of the intact Set1 histone methyltransferase complex in fission yeast.","citation":"J Biol Chem 2012 Jun 01;287(23):19040-7","abstract":"The methylation of histone H3 at lysine 4 (H3K4me) is critical for the formation of transcriptionally active chromatin in eukaryotes. In yeast, Drosophila, and some human cell lines, H3K4me is globally stimulated by the monoubiquitylation of histone H2B (H2Bub1), another histone modification associated with transcription. The mechanism of this \"trans-histone\" modification pathway remains uncertain, and studies carried out in different experimental systems have suggested that H2Bub1 could either influence the subunit composition of methyltransferase complexes or directly stimulate methyltransferase activity. We have reconstituted this pathway in vitro using the native H3K4-specific methyltransferase complex Set1C purified from the fission yeast Schizosaccharomyces pombe and chromatin substrates that contain semisynthetic H2Bub1. We found that the activity of S. pombe Set1C toward nucleosomal histone H3 is directly enhanced by H2Bub1 in vitro. Importantly, Set1C purified from cells lacking H2Bub1 retained activity on free histone substrates, suggesting that Set1C remains intact in the absence of H2Bub1. Chromatin immunoprecipitation assays revealed a defect in recruitment of intact Set1C to transcribed chromatin in H2Bub1-deficient mutants. Our data argue that trans-histone crosstalk in S. pombe involves direct enhancement of Set1C methyltransferase activity by H2Bub1 and suggest that this represents a conserved aspect of H2Bub1-H3K4me crosstalk in eukaryotes.","doi":"10.1074/jbc.M112.356253","authors":"Racine A, Pagé V, Nagy S, Grabowski D, Tanny JC","authors_abbrev":"Racine A et al.","pubmed_publication_date":"01 Jun 2012","pubmed_entrez_date":"2012-04-17","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR43490","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC977.08","HGNC:5211","HGNC:5209","HGNC:1027"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12827445","title":"Cordycepin in Schizosaccharomyces pombe: effects on the wild type and phenotypes of mutants resistant to the drug.","citation":"Curr Genet 2003 Sep;43(6):400-6","abstract":"The adenosine analogue cordycepin (3'-deoxyadenosine) inhibits growth and causes aberrant cell morphology in the fission yeast, Schizosaccharomyces pombe. Exogenously added thiamine, the pyrimidine moiety of the thiamine molecule, and adenine alleviate its growth-disturbing effect. At concentrations that do not inhibit growth, the drug reduces mating and sporulation and causes a decrease in the mRNA level of gene ste11 and the ste11-dependent gene, mei2. The mating- and sporulation-inhibiting effect of cordycepin is overcome by adenine. A mutant disrupted for the ado1 gene encoding adenosine kinase exhibits a cordycepin-resistant and methionine-sensitive phenotype, excretes adenosine into the medium and mates and sporulates poorly in the presence of adenine. A S. pombe mutant containing a frameshift mutation at the beginning of the carboxy-terminal half of gene ufd1 (the Saccharomyces cerevisiae UFD1 homologue) is cordycepin-resistant and sterile. Strains disrupted for the ufd1 gene only form microcolonies.","authors":"Naula N, Hilti N, Schweingruber AM, Schweingruber ME","authors_abbrev":"Naula N et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-06-27","publication_year":"2003","canto_session_key":"545c8d5d5cd1fec0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-22 20:27:25","canto_approved_date":"2022-03-31 17:05:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-30 09:14:56","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.14","SPAC27D7.03c","SPBC16A3.09c","SPBC32C12.02"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2016-06-22"},{"uniquename":"PMID:9679144","title":"Regulation of cell polarity by microtubules in fission yeast.","citation":"J Cell Biol 1998 Jul 27;142(2):457-71","abstract":"To investigate the role of microtubules in regulating cell polarity in Schizosaccharomyces pombe, we have developed a system in which normally cylindrical fission yeast synchronously form branched cells at high frequency upon treatment with the microtubule-depolymerizing drug thiabendazole (TBZ). Branching depends on both elevated temperature and cell cycle state and occurs at high frequency only when TBZ is added to cells that have not yet passed through New-End Take-Off (NETO), the normal transition from monopolar to bipolar growth. This suggests that microtubules may be of greatest physiological importance for the maintenance of cell shape at specific points in the cell cycle. The localization of three different proteins normally found at cell ends-cortical F-actin, tea1, and an ral3 (scd2)-green fluorescent protein (GFP) fusion-is disrupted by TBZ treatment. However, these proteins can eventually return to cell ends in the absence of microtubules, indicating that although their localization to ends normally depends on microtubules, they may recover by alternative mechanisms. In addition, TBZ induces a shift in ral3-GFP distribution from cell ends to the cell middle, suggesting that a protein complex containing ral3 may be part of the cue that specifies the position of branch formation.","authors":"Sawin KE, Nurse P","authors_abbrev":"Sawin KE et al.","pubmed_publication_date":"27 Jul 1998","pubmed_entrez_date":"1998-07-29","publication_year":"1998","canto_session_key":"6a1cd0660cdba7fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2020-05-28 17:30:41","canto_approved_date":"2022-05-31 06:49:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-05-04 10:06:04","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":20,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC25H2.13c","SPBC1604.14c","SPBC26H8.07c","SPBC14C8.07c","SPCC1223.06","SPAC2F7.03c","SPBC336.12c","SPBC4.04c","SPCC16A11.17","SPAC1F7.05","SPCC18B5.03","SPAC20G8.01","SPAC22H10.07"],"gene_count":14,"ltp_gene_count":11,"approved_date":"2020-05-28"},{"uniquename":"EMBL:AU012777","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17406492","title":"High-throughput knockout screen in fission yeast.","citation":"Nat Protoc 2006;1(5):2457-64","abstract":"We have designed the most efficient strategy to knock out genes in fission yeast Schizosaccharomyces pombe on a large scale. Our technique is based on knockout constructs that contain regions homologous to the target gene cloned into vectors carrying dominant drug-resistance markers. Most of the steps are carried out in a 96-well format, allowing simultaneous deletion of 96 genes in one batch. Based on our knockout technique, we designed a strategy for cloning knockout constructs for all predicted fission yeast genes, which is available in a form of a searchable database http://mendel.imp.ac.at/Pombe_deletion/. We validated this technique in a screen where we identified novel genes required for chromosome segregation during meiosis. Here, we present our protocol with detailed instructions. Using this protocol, one person can knock out 96 S. pombe genes in 8 days.","authors":"Gregan J, Rabitsch PK, Rumpf C, Novatchkova M, Schleiffer A, Nasmyth K","authors_abbrev":"Gregan J et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-04-05","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19798055","title":"Failed gene conversion leads to extensive end processing and chromosomal rearrangements in fission yeast.","citation":"EMBO J 2009 Nov 04;28(21):3400-12","abstract":"Loss of heterozygosity (LOH), a causal event in cancer and human genetic diseases, frequently encompasses multiple genetic loci and whole chromosome arms. However, the mechanisms by which such extensive LOH arises, and how it is suppressed in normal cells is poorly understood. We have developed a genetic system to investigate the mechanisms of DNA double-strand break (DSB)-induced extensive LOH, and its suppression, using a non-essential minichromosome, Ch(16), in fission yeast. We find extensive LOH to arise from a new break-induced mechanism of isochromosome formation. Our data support a model in which Rqh1 and Exo1-dependent end processing from an unrepaired DSB leads to removal of the broken chromosome arm and to break-induced replication of the intact arm from the centromere, a considerable distance from the initial lesion. This process also promotes genome-wide copy number variation. A genetic screen revealed Rhp51, Rhp55, Rhp57 and the MRN complex to suppress both isochromosome formation and chromosome loss, in accordance with these events resulting from extensive end processing associated with failed homologous recombination repair.","doi":"10.1038/emboj.2009.265","authors":"Tinline-Purvis H, Savory AP, Cullen JK, Davé A, Moss J, Bridge WL, Marguerat S, Bähler J, Ragoussis J, Mott R, Walker CA, Humphrey TC","authors_abbrev":"Tinline-Purvis H et al.","pubmed_publication_date":"04 Nov 2009","pubmed_entrez_date":"2009-10-03","publication_year":"2009","canto_session_key":"9d8a86ce7ba5c91b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-03-10 16:22:40","canto_approved_date":"2024-07-02 17:50:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-10 16:22:34","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":44,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.02c","SPCC1183.05c","SPAC20H4.07","SPAC30D11.10","SPAC3C7.03c","SPBC29A10.05","SPAC13C5.07","SPBC6B1.09c","SPAC2G11.12","SPAC644.14c","SPCC970.01"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2017-03-10"},{"uniquename":"PMID:26152587","title":"TORC1 Regulates Developmental Responses to Nitrogen Stress via Regulation of the GATA Transcription Factor Gaf1.","citation":"mBio 2015 Jul 07;6(4):e00959","abstract":"The TOR (target of rapamycin [sirolimus]) is a universally conserved kinase that couples nutrient availability to cell growth. TOR complex 1 (TORC1) in Schizosaccharomyces pombe positively regulates growth in response to nitrogen availability while suppressing cellular responses to nitrogen stress. Here we report the identification of the GATA transcription factor Gaf1 as a positive regulator of the nitrogen stress-induced gene isp7(+), via three canonical GATA motifs. We show that under nitrogen-rich conditions, TORC1 positively regulates the phosphorylation and cytoplasmic retention of Gaf1 via the PP2A-like phosphatase Ppe1. Under nitrogen stress conditions when TORC1 is inactivated, Gaf1 becomes dephosphorylated and enters the nucleus. Gaf1 was recently shown to negatively regulate the transcription induction of ste11(+), a major regulator of sexual development. Our findings support a model of a two-faceted role of Gaf1 during nitrogen stress. Gaf1 positively regulates genes that are induced early in the response to nitrogen stress, while inhibiting later responses, such as sexual development. Taking these results together, we identify Gaf1 as a novel target for TORC1 signaling and a step-like mechanism to modulate the nitrogen stress response.\nTOR complex 1 (TORC1) is an evolutionary conserved protein complex that positively regulates growth and proliferation, while inhibiting starvation responses. In fission yeast, the activity of TORC1 is downregulated in response to nitrogen starvation, and cells reprogram their transcriptional profile and prepare for sexual development. We identify Gaf1, a GATA-like transcription factor that regulates transcription and sexual development in response to starvation, as a downstream target for TORC1 signaling. Under nitrogen-rich conditions, TORC1 positively regulates the phosphorylation and cytoplasmic retention of Gaf1 via the PP2A-like phosphatase Ppe1. Under nitrogen stress conditions when TORC1 is inactivated, Gaf1 becomes dephosphorylated and enters the nucleus. Budding yeast TORC1 regulates GATA transcription factors via the phosphatase Sit4, a structural homologue of Ppe1. Thus, the TORC1-GATA transcription module appears to be conserved in evolution and may also be found in higher eukaryotes.","doi":"10.1128/mBio.00959-15","authors":"Laor D, Cohen A, Kupiec M, Weisman R","authors_abbrev":"Laor D et al.","pubmed_publication_date":"07 Jul 2015","pubmed_entrez_date":"2015-07-09","publication_year":"2015","canto_session_key":"8589306346786b20","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronit Weisman","canto_first_approved_date":"2018-05-17 13:35:58","canto_approved_date":"2024-02-21 20:24:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-02 06:30:42","canto_added_date":"2015-07-11 00:21:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ronit Weisman","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B9.02c","SPBC216.07c","SPBC16H5.07c","SPAC23E2.01","SPBC646.13","SPAC823.15","SPAC22E12.14c","SPAC57A7.11","SPBC30D10.10c","SPCC4G3.08","SPAC25B8.13c","SPAPYUG7.02c","SPCC1739.12","SPBC12C2.02c","SPCC24B10.07","SPCC1902.01","SPCC1393.08","SPCC290.04"],"gene_count":18,"ltp_gene_count":17,"approved_date":"2018-05-17"},{"uniquename":"PMID:22308326","title":"Tight coevolution of proliferating cell nuclear antigen (PCNA)-partner interaction networks in fungi leads to interspecies network incompatibility.","citation":"Proc Natl Acad Sci U S A 2012 Feb 14;109(7):E406-14","abstract":"The structure and connectivity of protein-protein interaction (PPI) networks are maintained throughout evolution by coordinated changes (coevolution) of network proteins. Despite extensive research, relatively little is known regarding the molecular basis and functional implications of the coevolution of PPI networks. Here, we used proliferating cell nuclear antigen, a hub protein that mediates DNA replication and repair in eukaryotes, as a model system to study the coevolution of PPI networks in fungi. Using a combined bioinformatics and experimental approach, we discovered that PCNA-partner interactions tightly coevolved in fungal species, leading to specific modes of recognition. We found that fungal proliferating cell nuclear antigen-partner interaction networks diverged into two distinct groups as a result of such coevolution and that hybrid networks of these groups are functionally noncompatible in Saccharomyces cerevisiae. Our results indicate that the coevolution of PPI networks can form functional barriers between fungal species, and thus can promote and fix speciation.","doi":"10.1073/pnas.1108633109","authors":"Zamir L, Zaretsky M, Fridman Y, Ner-Gaon H, Rubin E, Aharoni A","authors_abbrev":"Zamir L et al.","pubmed_publication_date":"14 Feb 2012","pubmed_entrez_date":"2012-02-07","publication_year":"2012","canto_session_key":"9f4172b1c9a958e9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-30 12:47:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-30 12:47:39","canto_added_date":"2016-09-21 00:19:46","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC285.16c","SPBC16D10.09","SPBC1734.02c","SPCC1183.06","SPCC1259.13","SPAC20G8.01","SPBC887.14c","SPBC16A3.11"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-09-30"},{"uniquename":"Pfam:PF17244","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8F11.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25799417","title":"Development of a targeted flip-in system in avian DT40 cells.","citation":"PLoS One 2015;10(3):e0122006","abstract":"Gene-targeting to create null mutants or designed-point mutants is a powerful tool for the molecular dissection of complex phenotypes involving DNA repair, signal transduction, and metabolism. Because gene-targeting is critically impaired in mutants exhibiting attenuated homologous recombination (HR), it is believed that gene-targeting is mediated via homologous recombination, though the precise mechanism remains unknown. We explored gene-targeting in yeast and avian DT40 cells. In animal cells, gene-targeting is activated by DNA double strand breaks introduced into the genomic region where gene-targeting occurs. This is evidenced by the fact that introducing double strand breaks at targeted genome sequences via artificial endonucleases such as TALEN and CRISPR facilitates gene-targeting. We found that in fission yeast, Schizosaccharomyces pombe, gene-targeting was initiated from double strand breaks on both edges of the homologous arms in the targeting construct. Strikingly, we also found efficient gene-targeting initiated on the edges of homologous arms in avian DT40 cells, a unique animal cell line in which efficient gene-targeting has been demonstrated. It may be that yeast and DT40 cells share some mechanism in which unknown factors detect and recombine broken DNA ends at homologous arms accompanied by crossover. We found efficient targeted integration of gapped plasmids accompanied by crossover in the DT40 cells. To take advantage of this finding, we developed a targeted flip-in system for avian DT40 cells. This flip-in system enables the rapid generation of cells expressing tag-fused proteins and the stable expression of transgenes from OVA loci.","doi":"10.1371/journal.pone.0122006","authors":"Kobayashi K, Fujii T, Asada R, Ooka M, Hirota K","authors_abbrev":"Kobayashi K et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-24","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-03-25 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7739540","title":"The Schizosaccharomyces pombe MBF complex requires heterodimerization for entry into S phase.","citation":"Mol Cell Biol 1995 May;15(5):2589-99","abstract":"In Schizosaccharomyces pombe, MBF is a DNA-binding complex suspected to activate the transcription of genes necessary for entry into S phase. The MBF complex contains both p85cdc10 and p72res1/sct1. To obtain a better understanding of how the MBF complex regulates gene expression at the G1/S transition, we have performed a genetic analysis of p72res1. We determined that p72res1 can bind specifically to the cdc22 promoter, when analyzed by gel mobility shift assay, and that the N-terminal 157 amino acids of p72res1 are sufficient for this specific binding. When overexpressed in vivo, a fragment of p72res1 containing this DNA-binding domain could rescue a strain carrying a temperature-sensitive cdc10 allele at the restrictive temperature as well as a strain with a cdc10 null allele. We also determined that the C-terminal region of p72res1 is necessary and sufficient for binding to p85cdc10. Overexpression of the cdc10-binding domain of p72res1 leads to a G1 arrest with a cdc phenotype and a decrease on MBF activity. Overexpression of full-length p72res1 also leads to a growth arrest that can be rescued by overexpression of p85cdc10. These results imply that the MBF activity in vivo is dependent on the interaction of p85cdc10 with p72res1.","authors":"Ayté J, Leis JF, Herrera A, Tang E, Yang H, DeCaprio JA","authors_abbrev":"Ayté J et al.","pubmed_publication_date":"May 1995","pubmed_entrez_date":"1995-05-01","publication_year":"1995","canto_session_key":"2e7e74bebcf07eb3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 17:59:34","canto_approved_date":"2023-09-11 10:19:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-08 08:15:35","canto_added_date":"2012-02-24 05:54:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPBC14C8.07c","SPBC336.12c","SPBC725.16"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2019-01-30"},{"uniquename":"PMID:8455610","title":"Two fission yeast B-type cyclins, cig2 and Cdc13, have different functions in mitosis.","citation":"Mol Cell Biol 1993 Apr;13(4):2286-97","abstract":"Cyclin B interacts with Cdc2 kinase to induce cell cycle events, particularly those of mitosis. The existence of cyclin B subtypes in several species has been known for some time, leading to speculation that key events of mitosis may be carried out by distinct functional classes of Cdc2/cyclin B. We report the discovery of cig2, a third B-type cyclin gene in Schizosaccharomyces pombe. Disruption of cig2 delays the onset of mitosis, to the degree that a cig2 null allele rescues mitotic catastrophe mutants, including those that are unable to carry out the inhibitory tyrosyl phosphorylation of Cdc2 kinase. Consistent with this, a cig2 null allele exhibits synthetic lethal interactions with cdc25ts and cdc2ts mutations. Mitotic phenotypes caused by disruption of cig2 are not reversed by increased production of Cdc13, the other fission yeast B-type cyclin that functions in mitosis. Likewise, a cdc13ts mutation is not rescued by increased gene dosage of cig2+. These data indicate that Cdc13 and Cig2 interact with Cdc2 to carry out different functions in mitosis. We suggest that some cyclin B subtypes found in other species, including humans, are also likely to have distinct, nonoverlapping functions in mitosis.","authors":"Bueno A, Russell P","authors_abbrev":"Bueno A et al.","pubmed_publication_date":"Apr 1993","pubmed_entrez_date":"1993-04-01","publication_year":"1993","canto_session_key":"c54c942aa08acf9b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-07-07 12:14:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-24 12:21:06","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAPB2B4.03","SPAC24H6.05","SPCC18B5.03","SPBC582.03","SPBC660.14"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-06-24"},{"uniquename":"PMID:41820706","title":"Cellular responses to prolonged non-thermal plasma exposure in Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2026 Mar 12;110(1)","abstract":"Non-thermal plasma (NTP) generates a complex mixture of reactive oxygen and nitrogen species (RONS) that can impose strong oxidative stress on eukaryotic cells. While the antimicrobial potential of NTP has been widely explored, much less is known about how eukaryotic cells respond to prolonged NTP-induced stress at the cellular and molecular level. Here, we investigated the cellular effects of extended NTP exposure using the fission yeast Schizosaccharomyces pombe as a non-pathogenic eukaryotic model. Our results indicate that extended exposure to NTP significantly reduces cell viability and is associated with increased oxidative stress, as evidenced by increased levels of intracellular RONS and mitochondrial superoxide. These oxidative changes were accompanied by pronounced cellular responses including tubulin depolymerisation, cell cycle arrest, and impaired cell division. In contrast, no significant changes were detected in the expression of genes involved in oxidative stress response and DNA repair. The observed effects are based on cellular, phenotypic, and transcriptomic analyses, while direct identification of oxidatively modified proteins remains to be addressed in future studies. KEY POINTS: • NTP increases intracellular RONS and mitochondrial superoxide levels • NTP causes tubulin depolymerisation, which is associated with cell cycle arrest • NTP alters the expression of genes involved in post-transcriptional regulation.","doi":"10.1007/s00253-026-13786-1","authors":"Petkova M, Durcanyova S, Kutka M, Kyzekova I, Gaplovska-Kysela K, Soltys K, Kyzek S, Medvecka V, Sevcovicova A","authors_abbrev":"Petkova M et al.","pubmed_publication_date":"12 Mar 2026","pubmed_entrez_date":"2026-03-13","publication_year":"2026","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2026-03-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18577519","title":"The cytokinesis formins from the nematode worm and fission yeast differentially mediate actin filament assembly.","citation":"J Biol Chem 2008 Aug 29;283(35):23872-83","abstract":"Formins drive actin filament assembly for diverse cellular processes including motility, establishing polarity, and cell division. To investigate the mechanism of contractile ring assembly in animal cells, we directly compared the actin assembly properties of formins required for cytokinesis in the nematode worm early embryo (CYK-1) and fission yeast (Cdc12p). Like Cdc12p and most other formins, CYK-1 nucleates actin filament assembly and remains processively associated with the elongating barbed end while facilitating the addition of profilin-actin above the theoretical diffusion-limited rate. However, specific properties differ significantly between Cdc12p and CYK-1. Cdc12p efficiently nucleates filaments that in the presence of profilin elongate at approximately the same rate as control filaments without formin (approximately 10.0 subunits/s). CYK-1 is an inefficient nucleator but allows filaments to elongate profilin-actin 6-fold faster than Cdc12p (approximately 60 subunits/s). Both Cdc12p and CYK-1 bind to pre-assembled actin filaments with low nanomolar affinity, but CYK-1 dissociates 2 orders of magnitude more quickly. However, CYK-1 rapidly re-associates with free barbed ends. Cdc12p allows barbed ends to elongate in the presence of excess capping protein, whereas capping protein inhibits CYK-1-mediated actin assembly. Therefore, these evolutionarily diverse formins can drive contractile ring assembly by a generally similar mechanism, but cells with unique dimensions and physical parameters might require proteins with carefully tuned actin assembly properties.","doi":"10.1074/jbc.M803734200","authors":"Neidt EM, Skau CT, Kovar DR","authors_abbrev":"Neidt EM et al.","pubmed_publication_date":"29 Aug 2008","pubmed_entrez_date":"2008-06-26","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16855399","title":"An extended anaphase signaling pathway for Mad2p includes microtubule organizing center proteins and multiple motor-dependent transitions.","citation":"Cell Cycle 2006 Jul;5(13):1456-63","abstract":"Signaling pathways within the mitotic mechanism temporally orchestrate spindle assembly with chromosome capture and alignment, and then coordinate initiation of chromosome segregation with spindle breakdown and cytokinesis for reproductive success. Kinetochore localized Mad2p acts in the spindle assembly checkpoint pathway during prophase and prometaphase to monitor bipolar attachment of chromosomes to spindle microtubules as well as proper tension at kinetochores. Once established, Mad2p is not degraded, but instead transits to spindle poles preceding the metaphase/anaphase transition in human and yeast cells. Whether conserved relocalization of Mad2p to poles is a final step in the spindle assembly checkpoint pathway or whether the post-metaphase transition allows Mad2p to cooperate in anaphase events leading to mitotic exit has been unknown. We examined post-metaphase localization of Mad2p in fission yeast. Our observations indicate an extended signaling pathway for Mad2p that includes kinetochore to bipolar localization at spindle poles, then additional transitions from bipolar to unipolar to equatorial. We determined that Mad2p associates with the microtubule organizing center complex through direct binding to Alp4p and that microtubule motor proteins Kinesin-14 Pkl1 and Dynein contribute to Mad2p anaphase transitions. At anaphase B onset, bipolar to unipolar transitions of both Mad2p and the septation inititiation network (SIN) kinase Cdc7 are observed. We determined that Mad2p and Cdc7p transitions monitor different events in anaphase, but that neither are required for anaphase B initiation. Our findings indicate that altered Mad2p anaphase spindle localizations can reflect changes in spindle function during mitotic exit that could contribute to fidelity in anaphase events.","authors":"Mayer C, Filopei J, Batac J, Alford L, Paluh JL","authors_abbrev":"Mayer C et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-07-21","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPBC20F10.06","SPBC365.15","SPAC3A11.14c","SPBC428.20c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"EMBL:SPD128","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22570787","title":"Role of translationally controlled tumor protein in cancer progression.","citation":"Biochem Res Int 2012;2012:369384","abstract":"Translationally controlled tumor protein (TCTP) is a highly conserved and ubiquitously expressed protein in all eukaryotes-highlighting its important functions in the cell. Previous studies revealed that TCTP is implicated in many biological processes, including cell growth, tumor reversion, and induction of pluripotent stem cell. A recent study on the solution structure from fission yeast orthologue classifies TCTP under a family of small chaperone proteins. There is growing evidence in the literature that TCTP is a multifunctional protein and exerts its biological activity at the extracellular and intracellular levels. Although TCTP is not a tumor-specific protein, our research group, among several others, focused on the role(s) of TCTP in cancer progression. In this paper, we will summarize the current scientific knowledge of TCTP in different aspects, and the precise oncogenic mechanisms of TCTP will be discussed in detail.","doi":"10.1155/2012/369384","authors":"Chan TH, Chen L, Guan XY","authors_abbrev":"Chan TH et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-05-10","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23592334","title":"Native SILAC: metabolic labeling of proteins in prototroph microorganisms based on lysine synthesis regulation.","citation":"Mol Cell Proteomics 2013 Jul;12(7):1995-2005","abstract":"Mass spectrometry (MS)-based quantitative proteomics has matured into a methodology able to detect and quantitate essentially all proteins of model microorganisms, allowing for unprecedented depth in systematic protein analyses. The most accurate quantitation approaches currently require lysine auxotrophic strains, which precludes analysis of most existing mutants, strain collections, or commercially important strains (e.g. those used for brewing or for the biotechnological production of metabolites). Here, we used MS-based proteomics to determine the global response of prototrophic yeast and bacteria to exogenous lysine. Unexpectedly, down-regulation of lysine synthesis in the presence of exogenous lysine is achieved via different mechanisms in different yeast strains. In each case, however, lysine in the medium down-regulates its biosynthesis, allowing for metabolic proteome labeling with heavy-isotope-containing lysine. This strategy of native stable isotope labeling by amino acids in cell culture (nSILAC) overcomes the limitations of previous approaches and can be used for the efficient production of protein standards for absolute SILAC quantitation in model microorganisms. As proof of principle, we have used nSILAC to globally analyze yeast proteome changes during salt stress.","doi":"10.1074/mcp.M112.025742","authors":"Fröhlich F, Christiano R, Walther TC","authors_abbrev":"Fröhlich F et al.","pubmed_publication_date":"Jul 2013","pubmed_entrez_date":"2013-04-18","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:47:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19474792","title":"Polar gradients of the DYRK-family kinase Pom1 couple cell length with the cell cycle.","citation":"Nature 2009 Jun 11;459(7248):852-6","abstract":"Cells normally grow to a certain size before they enter mitosis and divide. Entry into mitosis depends on the activity of Cdk1, which is inhibited by the Wee1 kinase and activated by the Cdc25 phosphatase. However, how cells sense their size for mitotic commitment remains unknown. Here we show that an intracellular gradient of the dual-specificity tyrosine-phosphorylation regulated kinase (DYRK) Pom1, which emanates from the ends of rod-shaped Schizosaccharomyces pombe cells, serves to measure cell length and control mitotic entry. Pom1 provides positional information both for polarized growth and to inhibit cell division at cell ends. We discovered that Pom1 is also a dose-dependent G2-M inhibitor. Genetic analyses indicate that Pom1 negatively regulates Cdr1 and Cdr2, two previously described Wee1 inhibitors of the SAD kinase family. This inhibition may be direct, because in vivo and in vitro evidence suggest that Pom1 phosphorylates Cdr2. Whereas Cdr1 and Cdr2 localize to a medial cortical region, Pom1 forms concentration gradients from cell tips that overlap with Cdr1 and Cdr2 in short cells, but not in long cells. Disturbing these Pom1 gradients leads to Cdr2 phosphorylation and imposes a G2 delay. In short cells, Pom1 prevents precocious M-phase entry, suggesting that the higher medial Pom1 levels inhibit Cdr2 and promote a G2 delay. Thus, gradients of Pom1 from cell ends provide a measure of cell length to regulate M-phase entry.","doi":"10.1038/nature08054","authors":"Martin SG, Berthelot-Grosjean M","authors_abbrev":"Martin SG et al.","pubmed_publication_date":"11 Jun 2009","pubmed_entrez_date":"2009-05-29","publication_year":"2009","canto_session_key":"a475a61f06526c04","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-05-08 19:14:19","canto_approved_date":"2026-01-27 16:23:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-27 19:24:33","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":45,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC644.06c","SPAC24H6.05","SPBC11B10.09","SPAC57A10.02","SPAC2F7.03c","SPCC1223.06","SPBC409.07c","SPBC23G7.04c","SPAC24B11.06c","SPBC1706.01","SPBC1A4.05"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2017-05-08"},{"uniquename":"PMID:32499408","title":"The molecular chaperone Hsp90 regulates heterochromatin assembly through stabilizing multiple complexes in fission yeast.","citation":"J Cell Sci 2020 Jul 07;133(13)","abstract":"In the fission yeast  Schizosaccharomyces pombe , both RNAi machinery and RNAi-independent factors mediate transcriptional and posttranscriptional silencing and heterochromatin formation. Here, we show that the silencing of reporter genes at major native heterochromatic loci (centromeres, telomeres, mating-type locus and rDNA regions) and an artificially induced heterochromatin locus is alleviated in a fission yeast  hsp90  mutant,  hsp90-G84C  Also, H3K9me2 enrichment at heterochromatin regions, especially at the mating-type locus and subtelomeres, is compromised, suggesting heterochromatin assembly defects. We further discovered that Hsp90 is required for stabilization or assembly of the RNA-induced transcriptional silencing (RITS) and Argonaute siRNA chaperone (ARC) RNAi effector complexes, the RNAi-independent factor Fft3, the shelterin complex subunit Poz1 and the Snf2/HDAC-containing repressor complex (SHREC). Our ChIP data suggest that Hsp90 regulates the efficient recruitment of the methyltransferase/ubiquitin ligase complex CLRC by shelterin to chromosome ends and targeting of the SHREC and Fft3 to mating type locus and/or rDNA region. Finally, our genetic analyses demonstrated that increased heterochromatin spreading restores silencing at subtelomeres in the  hsp90-G84C  mutant. Thus, this work uncovers a conserved factor critical for promoting RNAi-dependent and -independent heterochromatin assembly and gene silencing through stabilizing multiple effectors and effector complexes.","doi":"10.1242/jcs.244863","authors":"Sun L, Liu XM, Li WZ, Yi YY, He X, Wang Y, Jin QW","authors_abbrev":"Sun L et al.","pubmed_publication_date":"07 Jul 2020","pubmed_entrez_date":"2020-06-06","publication_year":"2020","canto_session_key":"a82c265e16b26ca6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-11 16:35:34","canto_approved_date":"2024-04-02 14:05:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-01 17:33:30","canto_added_date":"2020-06-07 00:15:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC212.11","SPCC188.13c","SPBC428.08c","SPBC83.03c","SPCC736.11","SPAC1805.09c","SPAC664.01c","SPAC25A8.01c","SPAC19G12.13c","SPAC140.03","SPAC926.04c","SPCC188.07","SPAC212.12"],"gene_count":13,"ltp_gene_count":1,"approved_date":"2020-12-11"},{"uniquename":"PMID:37162093","title":"Genetic knockdown of genes that are obscure, conserved and essential using CRISPR interference methods in the fission yeast S. pombe.","citation":"J Cell Sci 2023 May 01;136(9)","abstract":"Characterizing functions of essential genes is challenging, as perturbing them is generally lethal. Conditional gene perturbation, including use of temperature-sensitive mutants, has been widely utilized to reveal functions of essential genes in the fission yeast Schizosaccharomyces pombe. However, recently we implemented a systematic and less time-consuming knockdown method, CRISPR interference (CRISPRi), in this organism using catalytically inactive Cas9 (dCas9). This technology has been expected to facilitate characterization of essential genes in S. pombe, although this still has not occurred. Here, CRISPRi was harnessed to study uncharacterized essential genes that are evolutionally conserved from yeasts to mammals. Transcription of these genes, which we call conserved essential obscure (ceo) genes, was repressed using conventional dCas9-mediated CRISPRi and by implementing technologies that enhance repression efficiency or alleviate limitations on small guide RNA (sgRNA) design. These CRISPRi methods successfully reduced transcription of target genes and allowed us to characterize resulting phenotypes. Knockdown of ceo genes inhibited cell proliferation and altered cellular morphology. Thus, dCas9-based CRISPRi methods utilized in this study enhanced accessibility of genetic analyses targeting essential genes in S. pombe.","doi":"10.1242/jcs.261186","authors":"Ishikawa K, Soejima S, Saitoh S","authors_abbrev":"Ishikawa K et al.","pubmed_publication_date":"01 May 2023","pubmed_entrez_date":"2023-05-10","publication_year":"2023","canto_session_key":"744e598799f5d648","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ken Ishikawa","canto_first_approved_date":"2023-06-15 18:33:33","canto_approved_date":"2023-06-21 12:19:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-12 16:58:01","canto_added_date":"2023-05-11 00:15:04","annotation_curators":[{"name":"Ken Ishikawa","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19B12.01","SPAC19A8.06","SPCC584.14","SPCC16C4.02c","SPAC2C4.04c","SPAC3A12.02","SPAC56F8.07"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2023-06-15"},{"uniquename":"PMID:23934889","title":"TORC1 signaling is governed by two negative regulators in fission yeast.","citation":"Genetics 2013 Oct;195(2):457-68","abstract":"The target of rapamycin (TOR) is a highly conserved protein kinase that regulates cell growth and metabolism. Here we performed a genome-wide screen to identify negative regulators of TOR complex 1 (TORC1) in Schizosaccharomyces pombe by isolating mutants that phenocopy Δtsc2, in which TORC1 signaling is known to be up-regulated. We discovered that Δnpr2 displayed similar phenotypes to Δtsc2 in terms of amino acid uptake defects and mislocalization of the Cat1 permease. However, Δnpr2 and Δtsc2 clearly showed different phenotypes in terms of rapamycin supersensitivity and Isp5 transcription upon various treatments. Furthermore, we showed that Tor2 controls amino acid homeostasis at the transcriptional and post-transcriptional levels. Our data reveal that both Npr2 and Tsc2 negatively regulate TORC1 signaling, and Npr2, but not Tsc2, may be involved in the feedback loop of a nutrient-sensing pathway.","doi":"10.1534/genetics.113.154674","authors":"Ma N, Liu Q, Zhang L, Henske EP, Ma Y","authors_abbrev":"Ma N et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-08-13","publication_year":"2013","canto_session_key":"b63f265d4bdd37d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-27 15:27:51","canto_approved_date":"2021-10-15 13:17:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-31 16:34:21","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":65,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.13c","SPAC23H3.03c","SPAPB1E7.12","SPAC869.11","SPAC630.13c","SPBC216.07c","SPBC1A4.02c","SPAC1039.09","SPCC777.05"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2015-04-27"},{"uniquename":"PMID:8194753","title":"Cloning and sequence analysis of rhp51+, a Schizosaccharomyces pombe homolog of the Saccharomyces cerevisiae RAD51 gene.","citation":"Gene 1994 May 16;142(2):207-11","abstract":"A homology (rhp51+) of the RAD51 gene in Schizosaccharomyces pombe was cloned by screening a Sz. pombe genomic library using the 3'-end of RAD51 from Saccharomyces cerevisiae as a probe. As in S. cerevisiae, the sequence of rhp51+ showed two MluI cell-cycle boxes and a putative DNA damage-responsive element in its upstream region. The open reading frame codes for a 365-amino-acid (aa) polypeptide with an estimated molecular mass of 40,555 Da. The deduced aa sequence shows 27, 66, 75 and 80% identity with Escherichia coli RecA, S. cerevisiae Rad51 and the Rad51 homologs from chicken and humans, respectively. The aa sequence encoded by rhp51+ contains A- and B-type nucleotide-binding consensus sequences, as found in other RAD51 homologs. Northern blot analysis showed that rhp51+ encodes a 1.7-kb transcript. Methyl methanesulfonate treatment increased the level of this transcript three- to fivefold. Southern hybridization analysis suggests that a single copy of rhp51+ exists in the Sz. pombe genome.","authors":"Jang YK, Jin YH, Kim EM, Fabre F, Hong SH, Park SD","authors_abbrev":"Jang YK et al.","pubmed_publication_date":"16 May 1994","pubmed_entrez_date":"1994-05-16","publication_year":"1994","canto_session_key":"a80602e2b7138ea9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:23:50","canto_approved_date":"2018-12-22 20:23:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 19:20:16","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:8898895","title":"Species-specific inhibition of homologous enzymes by modification of nonconserved amino acids residues. The cysteine residues of triosephosphate isomerase.","citation":"Eur J Biochem 1996 Oct 01;241(1):114-20","abstract":"The possibility of using non-conserved amino acid residues to produce selective inhibition of homologous enzymes from different species has been further explored with triosephosphate isomerase. S-phenyl-p-toluenethiosulfonate (MePhSO2-SPh), which produces phenyl disulfides with accessible Cys residues, inhibits the activity of rabbit triosephosphate isomerase. The inhibition is due to derivatization of one of the five Cys residues of rabbit triosephosphate isomerase. The effect of MePhSO2-SPh on triosephosphate isomerase from Saccharomyces cerevisiae, Escherichia coli, chicken and Schizosaccharomyces pombe was also determined. MePhSO2-SPh did not affect the activity of triosephosphate isomerase from S. cerevisiae and E. coli but it inhibited triosephosphate isomerase from chicken and S. pombe. From an analysis of the Cys content of the various triosephosphate isomerases, it was evident that amongst the ones studied only those that have a Cys in position 217 (or in an equivalent position) were sensitive to MePhSO2-SPh. Methyl metanethiosulfonate (MeSO2-SMe), which produces methyl disulfides, had no effect on triosephosphate isomerases that lack Cys217 (S. cerevisiae and E. coli). In triosephosphate isomerases that have Cys217, MeSO2-SMe inhibited by 40-50% the activity of that from S. pombe, 20-25% that from rabbit but had no effect on the chicken enzyme. In the three latter triosephosphate isomerases, MeSO2-SMe protected against the strong inhibiting action of MePhSO2-SPh. The latter observations suggest that MeSO2-SMe and MePhSO2-SPh derivatize the same Cys and that significant inhibition of activity requires perturbation by the relatively large phenyl group. The intrinsic fluorescence of rabbit triosephosphate isomerase that had been derivatized to a phenyl disulfide was almost identical to that of the native enzyme. Thus, modification of Cys217 did not produce gross structural alterations, albeit it brought about important kinetic alterations, i.e. a nearly fivefold increase in the K(m) for glyceraldehyde 3-phosphate and a 65% decrease in Vmax. The effect of derivatizating Cys217 differs markedly from that produced by derivatization of Cys14 (another non-conserved cysteine). The differences may be explained from their position in the three-dimensional structure of the enzyme.","authors":"Garza-Ramos G, Pérez-Montfort R, Rojo-Domínguez A, de Gómez-Puyou MT, Gómez-Puyou A","authors_abbrev":"Garza-Ramos G et al.","pubmed_publication_date":"01 Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10759889","title":"Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library.","citation":"Genes Cells 2000 Mar;5(3):169-90","abstract":"Intracellular localization is an important part of the characterization of a gene product. In an attempt to search for genes based on the intracellular localization of their products, we constructed a green fluorescent protein (GFP)-fusion genomic DNA library of S. pombe.\nWe constructed the S. pombe GFP-fusion genomic DNA library by fusing, in all three reading frames, random fragments of genomic DNA to the 5' end of the GFP gene in such a way that expression of potential GFP-fusion proteins would be under the control of the own promoters contained in the genomic DNA fragments. Fission yeast cells were transformed with this plasmid library, and microscopic screening of 49 845 transformants yielded 6954 transformants which exhibited GFP fluorescence, of which 728 transformants showed fluorescence localized to distinct intracellular structures such as the nucleus, the nuclear membrane, and cytoskeletal structures. Plasmids were isolated from 516 of these transformants, and a determination of their DNA sequences identified 250 independent genes. The intracellular localizations of the 250 GFP-fusion constructs was categorized as an image database; using this database, DNA sequences can be searched for based on the localizations of their products.\nA number of new intracellular structural components were found in this library. The library of GFP-fusion constructs also provides useful fluorescent markers for various intracellular structures and cellular activities, which can be readily used for microscopic observation in living cells.","authors":"Ding DQ, Tomita Y, Yamamoto A, Chikashige Y, Haraguchi T, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"Mar 2000","pubmed_entrez_date":"2000-04-12","publication_year":"2000","canto_session_key":"36c133d470817288","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-11-18 11:34:13","canto_approved_date":"2022-09-16 11:05:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-15 17:12:24","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.04c","SPBC21C3.11","SPCC1902.02","SPCC1919.03c","SPAC6F12.10c","SPBC11B10.09","SPBC1709.17","SPBC146.09c","SPAC637.12c","SPBC1778.02","SPAC26A3.01","SPAC29A4.10","SPAC6B12.16","SPBC29A10.07","SPAC27F1.09c","SPAC328.04","SPBC32H8.02c","SPAC30D11.01c","SPAC22G7.02","SPAC3A11.08","SPAC24C9.05c","SPBC947.12","SPBC902.04","SPAC2C4.07c","SPBC428.17c","SPAC1D4.01","SPAC20G8.05c","SPCC1795.10c","SPAC22A12.11","SPCC1919.12c","SPBC16A3.19","SPAC17H9.06c","SPAC821.07c","SPBC800.13","SPAC57A7.08","SPAC5D6.02c","SPBC19C7.10","SPAC25B8.16","SPAC29A4.11","SPAC664.02c","SPAC1805.04","SPBC1685.08","SPAC31A2.14","SPCC794.10","SPBP8B7.23","SPBC3E7.06c","SPBC25B2.07c","SPBC30B4.05","SPCC830.03","SPAC6F12.02","SPAC20H4.10","SPAC23E2.02","SPCC4B3.07","SPBC29A3.13","SPAC25G10.09c","SPCC1840.03"],"gene_count":56,"ltp_gene_count":10,"approved_date":"2017-11-18"},{"uniquename":"PMID:14195446","title":"CHANGES IN THE ACID-SOLUBLE POOL DURING THE CELL CYCLE OF SCHIZOSACCHAROMYCES POMBE.","citation":"Exp Cell Res 1964 Jul;35:394-401","abstract":"","authors":"MITCHISON JM, CUMMINS JE","authors_abbrev":"MITCHISON JM et al.","pubmed_publication_date":"Jul 1964","pubmed_entrez_date":"1964-07-01","publication_year":"1964","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41385327","title":"Phosphorylation of HP1/Swi6 relieves competition with Suv39/Clr4 on nucleosomes and enables H3K9 trimethyl spreading.","citation":"Nucleic Acids Res 2025 Nov 26;53(22)","abstract":"Heterochromatin formation in Schizosaccharomyces pombe requires the spreading of histone 3 (H3) Lysine 9 (K9) methylation (me) from nucleation centers by the H3K9 methylase, Suv39/Clr4, and the reader protein, HP1/Swi6. To accomplish this, Suv39/Clr4 and HP1/Swi6 have to associate with nucleosomes both nonspecifically, binding DNA, and octamer surfaces and specifically, via recognition of methylated H3K9 by their respective chromodomains. However, how both proteins avoid competition for the same nucleosomes in this process is unclear. Here, we show that phosphorylation tunes oligomerization and the nucleosome affinity of HP1/Swi6 such that it preferentially partitions onto Suv39/Clr4's trimethyl product rather than its unmethylated substrates. Preferential partitioning enables efficient conversion from di-to trimethylation on nucleosomes in vitro and H3K9me3 spreading in vivo. Together, our data suggest that phosphorylation of HP1/Swi6 creates a regime that increases oligomerization and relieves competition with the \"read-write\" mechanism of Suv39/Clr4, together promoting for productive heterochromatin spreading.","doi":"10.1093/nar/gkaf1244","authors":"Kennedy DR, Lemière J, Amine AAA, Martin EW, Tan C, Simental E, Braxton J, Maxwell RA, Al-Sady B","authors_abbrev":"Kennedy DR et al.","pubmed_publication_date":"26 Nov 2025","pubmed_entrez_date":"2025-12-12","publication_year":"2025","canto_session_key":"c72564f1561f7822","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-13 00:25:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9154809","title":"A novel mutant allele of Schizosaccharomyces pombe rad26 defective in monitoring S-phase progression to prevent premature mitosis.","citation":"Mol Cell Biol 1997 Jun;17(6):3103-15","abstract":"A semipermissive growth condition was defined for a Schizosaccharomyces pombe strain carrying a thermosensitive allele of DNA polymerase delta (pol delta ts03). Under this condition, DNA polymerase delta is semidisabled and causes a delay in S-phase progression. Using a genetic strategy, we have isolated a panel of mutants that enter premature mitosis when DNA replication is incomplete but which are not defective for arrest in G2/M following DNA damage. We characterized the aya14 mutant, which enters premature mitosis when S phase is arrested by genetic or chemical means. However, this mutant is sensitive to neither UV nor gamma irradiation. Two genomic clones, rad26+ and cds1+, were found to suppress the hydroxyurea sensitivity of the aya14 mutant. Genetic analysis indicates that aya14 is a novel allele of the cell cycle checkpoint gene rad26+, which we have named rad26.a14. cds1+ is a suppressor which suppresses the S-phase feedback control defect of rad26.a14 when S phase is inhibited by either hydroxyurea or cdc22, but it does not suppress the defect when S phase is arrested by a mutant DNA polymerase. Analyses of rad26.a14 in a variety of cdc mutant backgrounds indicate that strains containing rad26.a14 bypass S-phase arrest but not G1 or late S/G2 arrest. A model of how Rad26 monitors S-phase progression to maintain the dependency of cell cycle events and coordinates with other rad/hus checkpoint gene products in responding to radiation damage is proposed.","authors":"Uchiyama M, Galli I, Griffiths DJ, Wang TS","authors_abbrev":"Uchiyama M et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"062ae65578cd43ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-03-26 16:49:48","canto_approved_date":"2024-03-28 12:06:20","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-03-26 16:49:42","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":47,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.04","SPAC8F11.07c","SPCC16A11.17","SPAC20G8.01","SPCC18B5.03","SPBC216.05","SPBC25H2.13c","SPAC3H5.06c","SPCC1259.13","SPBC1734.02c","SPAC9E9.08","SPBC336.12c","SPAC24H6.05","SPAC1F7.05","SPBC11B10.09","SPCC18B5.11c"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2015-03-26"},{"uniquename":"PMID:20622008","title":"A chromatin-remodeling protein is a component of fission yeast mediator.","citation":"J Biol Chem 2010 Sep 24;285(39):29729-37","abstract":"The multiprotein Mediator complex is an important regulator of RNA polymerase II-dependent genes in eukaryotic cells. In contrast to the situation in many other eukaryotes, the conserved Med15 protein is not a stable component of Mediator isolated from fission yeast. We here demonstrate that Med15 exists in a protein complex together with Hrp1, a CHD1 ATP-dependent chromatin-remodeling protein. The Med15-Hrp1 subcomplex is not a component of the core Mediator complex but can interact with the L-Mediator conformation. Deletion of med15(+) and hrp1(+) causes very similar effects on global steady-state levels of mRNA, and genome-wide analyses demonstrate that Med15 associates with a distinct subset of Hrp1-bound gene promoters. Our findings therefore indicate that Mediator may directly influence histone density at regulated promoters.","doi":"10.1074/jbc.M110.153858","authors":"Khorosjutina O, Wanrooij PH, Walfridsson J, Szilagyi Z, Zhu X, Baraznenok V, Ekwall K, Gustafsson CM","authors_abbrev":"Khorosjutina O et al.","pubmed_publication_date":"24 Sep 2010","pubmed_entrez_date":"2010-07-13","publication_year":"2010","canto_session_key":"77bdec1cc4f8a9e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-03 10:21:21","canto_approved_date":"2023-03-28 15:09:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-24 14:35:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC589.02c","SPAC688.08","SPAC17C9.05c","SPBC31F10.04c","SPBC14F5.08","SPAC1783.05","SPBC1A4.10c","SPBC146.01","SPCC191.11"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2016-10-03"},{"uniquename":"PMID:31665745","title":"Conserved HORMA domain-containing protein Hop1 stabilizes interaction between proteins of meiotic DNA break hotspots and chromosome axis.","citation":"Nucleic Acids Res 2019 Nov 04;47(19):10166-10180","abstract":"HORMA domain-containing proteins such as Hop1 play crucial regulatory roles in various chromosomal functions. Here, we investigated roles of the fission yeast Hop1 in the formation of recombination-initiating meiotic DNA double strand breaks (DSBs). Meiotic DSB formation in fission yeast relies on multiple protein-protein interactions such as the one between the chromosome axial protein Rec10 and the DSB-forming complex subunit Rec15. Chromatin immunoprecipitation sequencing demonstrated that Hop1 is colocalized with both Rec10 and Rec15, and we observed physical interactions of Hop1 to Rec15 and Rec10. These results suggest that Hop1 promotes DSB formation by interacting with both axis components and the DSB-forming complex. We also show that Hop1 binding to DSB hotspots requires Rec15 and Rec10, while Hop1 axis binding requires Rec10 only, suggesting that Hop1 is recruited to the axis via Rec10, and to hotspots by hotspot-bound Rec15. Furthermore, we introduced separation-of-function Rec10 mutations, deficient for interaction with either Rec15 or Hop1. These single mutations and hop1Δ conferred only partial defects in meiotic recombination, while the combining the Rec15-binding-deficient rec10 mutation with hop1Δ synergistically reduced meiotic recombination, at least at a model hotspot. Taken together, Hop1 likely functions as a stabilizer for Rec15-Rec10 interaction to promote DSB formation.","doi":"10.1093/nar/gkz754","authors":"Kariyazono R, Oda A, Yamada T, Ohta K","authors_abbrev":"Kariyazono R et al.","pubmed_publication_date":"04 Nov 2019","pubmed_entrez_date":"2019-10-31","publication_year":"2019","canto_session_key":"07b83651efed8a24","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-11-01 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1718.02","SPBC1711.14","SPAC25G10.04c","SPBC29A10.14"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:2","title":"Delineation of the intimate details of the backbone conformation of pyridine nucleotide coenzymes in aqueous solution.","citation":"Biochem Biophys Res Commun 1975 Oct 27;66(4):1173-9","abstract":"","authors":"Bose KS, Sarma RH","authors_abbrev":"Bose KS et al.","pubmed_publication_date":"27 Oct 1975","pubmed_entrez_date":"1975-10-27","publication_year":"1975","canto_session_key":"ba9d607d23dfef7d","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-10-12 14:48:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7621824","title":"hsk1+, a Schizosaccharomyces pombe gene related to Saccharomyces cerevisiae CDC7, is required for chromosomal replication.","citation":"EMBO J 1995 Jul 03;14(13):3094-104","abstract":"Degenerate oligonucleotide-directed polymerase chain reaction was conducted to clone a possible Schizosaccharomyces pombe homologue [hsk1 for a putative homologue of CDC7 (seven) kinase 1] of Saccharomyces cerevisiae Cdc7 kinase. The cloned cDNA for hsk1+ contains an open reading frame consisting of 507 amino acids with predicted mol. wt of 58,370 that possesses overall amino acid identity of 46% (65% including similar residues) to CDC7. In addition to conserved domains for serine-threonine kinases, the predicted primary structure of Hsk1 contains three 'kinase insert' sequences characteristic to Cdc7 at the positions identical to those of Cdc7. Whereas the length and sequences of the kinase inserts are diverged between the two yeast species, 58% identity (76% including similar residues) is detected within the kinase conserved domains. The hsk1+ gene, which is present as a single copy on the S.pombe chromosome, contains two introns within the coding frame. Disruption of the hsk1+ gene by insertion of the ura4+ gene is lethal to growth. Analysis of the DNA content of germinating spores that contain hsk1 null alleles indicates that DNA replication is inhibited in the mutant. The morphology of these mutant spores after germination indicates abnormal nuclear division in some population of germinating spores, suggesting either that Hsk1 may be required for inhibition of mitosis until completion of S phase or that it may also be involved in proper execution of mitosis. Our results suggest that hsk1+ is a strong candidate for the functional fission yeast homologue of budding yeast CDC7 and that a mechanism through which initiation of chromosomal replication is regulated may be conserved between the two yeast species.","authors":"Masai H, Miyake T, Arai K","authors_abbrev":"Masai H et al.","pubmed_publication_date":"03 Jul 1995","pubmed_entrez_date":"1995-07-03","publication_year":"1995","canto_session_key":"d0f47dc66e0ff761","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 16:00:33","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-03-13 17:41:13","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-03-13"},{"uniquename":"PMID:895757","title":"Mutation in continuous cultures of Schizosaccharomyces pombe. I. Dependence of the kinetics of mutation accumulation upon the growth-limiting nutrilite.","citation":"Mutat Res 1977 Aug;44(2):227-34","abstract":"The rate of spontaneous mutation to resistance to the 12,13-epoxytrichothecene trichodermin has been determined under different growth limiting conditions in continuous cultures of the microbial eukaryote Schizosaccharomyces pombe. In agreement with data obtained in bacterial systems by previous workers the kinetics observed for the accumulation of mutations is found to be dependent upon the nutrient used to limit the growth of the population. Under conditions of glucose-limitation mutation accumulation is directly proportional to the rate of cell division, while under histidine-limitation it is proportional to chronological time. Various possible explanations for these observations are discussed.","authors":"McAthey P, Kilbey BJ","authors_abbrev":"McAthey P et al.","pubmed_publication_date":"Aug 1977","pubmed_entrez_date":"1977-08-01","publication_year":"1977","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12649273","title":"The UDP-glucose:glycoprotein glucosyltransferase is organized in at least two tightly bound domains from yeast to mammals.","citation":"J Biol Chem 2003 Jun 06;278(23):20540-6","abstract":"The endoplasmic reticulum UDP-Glc:glycoprotein glucosyltransferase (GT) exclusively glucosylates nonnative glycoprotein conformers. GT sequence analysis suggests that it is composed of at least two domains: the N-terminal domain, which composes 80% of the molecule, has no significant similarity to other known proteins and was proposed to be involved in the recognition of non-native conformers and the C-terminal or catalytic domain, which displays a similar size and significant similarity to members of glycosyltransferase family 8. Here, we show that N- and C-terminal domains from Rattus norvegicus and Schizosaccharomyces pombe GTs remained tightly but not covalently bound upon a mild proteolytic treatment and could not be separated without loss of enzymatic activity. The notion of a two-domain protein was reinforced by the synthesis of an active enzyme upon transfection of S. pombe GT null mutants with two expression vectors, each of them encoding one of both domains. Transfection with the C-terminal domain-encoding vector alone yielded an inactive, rapidly degraded protein, thus indicating that the N-terminal domain is required for proper folding of the C-terminal catalytic portion. If, indeed, the N-terminal domain is, as proposed, also involved in glycoprotein conformation recognition, the tight association between N- and C-terminal domains may explain why only N-glycans in close proximity to protein structural perturbations are glucosylated by the enzyme. Although S. pombe and Drosophila melanogaster GT N-terminal domains display an extremely poor similarity (16.3%), chimeras containing either yeast N-terminal and fly C-terminal domains or the inverse construction were enzymatically and functionally active in vivo, thus indicating that the N-terminal domains of both GTs shared three-dimensional features.","authors":"Guerin M, Parodi AJ","authors_abbrev":"Guerin M et al.","pubmed_publication_date":"06 Jun 2003","pubmed_entrez_date":"2003-03-22","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15456843","title":"RNA-directed DNA methylation.","citation":"J Cell Sci 2004 Oct 01;117(Pt 21):4881-8","abstract":"Double-stranded RNAs (dsRNAs) and their 'diced' small RNA products can guide key developmental and defense mechanisms in eukaryotes. Some RNA-directed mechanisms act at a post-transcriptional level to degrade target messenger RNAs. However, dsRNA-derived species can also direct changes in the chromatin structure of DNA regions with which they share sequence identity. For example, plants use such RNA species to lay down cytosine methylation imprints on identical DNA sequences, providing a fundamental mark for the formation of transcriptionally silent heterochromatin. Thus, RNA can feed backwards to modulate the accessibility of information stored in the DNA of cognate genes. RNA triggers for DNA methylation can come from different sources, including invasive viral, transgene or transposon sequences, and in some cases are derived from single-stranded RNA precursors by RNA-dependent RNA polymerases. The mechanism by which RNA signals are translated into DNA methylation imprints is currently unknown, but two plant-specific types of cytosine methyltransferase have been implicated in this process. RNA can also direct heterochromatin formation in fission yeast and Drosophila, but in these organisms the process occurs in the absence of DNA methylation.","authors":"Mathieu O, Bender J","authors_abbrev":"Mathieu O et al.","pubmed_publication_date":"01 Oct 2004","pubmed_entrez_date":"2004-10-01","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10888871","title":"Mitotic replication initiation proteins are not required for pre-meiotic S phase.","citation":"Nat Genet 2000 Jul;25(3):263-8","abstract":"Initiation of mitotic DNA replication in eukaryotes requires conserved factors, including Cdc18/CDC6 and minichromosome maintenance (MCM) proteins. We show here that these proteins are not essential for meiotic DNA replication or subsequent meiotic divisions in fission yeast. In addition, vegetative replication checkpoint genes are not required for the arrest of meiotic divisions in response to pre-meiotic S-phase delays. Genes essential for other aspects of vegetative DNA replication, however, including polymerases and DNA ligase, are also required for pre-meiotic DNA synthesis. Our results indicate that the process of replication initiation and checkpoint control may be fundamentally different in mitotic and meiotic cells.","authors":"Forsburg SL, Hodson JA","authors_abbrev":"Forsburg SL et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-07-11","publication_year":"2000","canto_session_key":"46b903f22fd81cc5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-28 14:47:08","canto_approved_date":"2024-11-14 09:27:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-03 08:58:13","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":55,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPCC1259.13","SPAC3H5.06c","SPBC25H2.13c","SPAC23C4.18c","SPAC1F7.05","SPBC11B10.09","SPBC336.04","SPAC17A5.11","SPAC1B2.05","SPCC18B5.11c","SPBC29A10.15","SPBC660.13c","SPCC1682.02c","SPBC211.04c","SPAC20G8.01","SPAC8F11.07c","SPBC4.04c","SPBC14C8.07c","SPBC216.05","SPAC27E2.05","SPCC16A11.17"],"gene_count":22,"ltp_gene_count":18,"approved_date":"2016-01-28"},{"uniquename":"PMID:11572939","title":"Analysis of Schizosaccharomyces pombe mediator reveals a set of essential subunits conserved between yeast and metazoan cells.","citation":"Proc Natl Acad Sci U S A 2001 Oct 09;98(21):11985-90","abstract":"With the identification of eight new polypeptides, we here complete the subunit characterization of the Schizosaccharomyces pombe RNA polymerase II holoenzyme. The complex contains homologs to all 10 essential gene products present in the Saccharomyces cerevisiae Mediator, but lacks clear homologs to any of the 10 S. cerevisiae components encoded by nonessential genes. S. pombe Mediator instead contains three unique components (Pmc2, -3, and -6), which lack homologs in other cell types. Presently, pmc2(+) and pmc3(+) have been shown to be nonessential genes. The data suggest that S. pombe and S. cerevisiae share an essential protein module, which associates with nonessential speciesspecific subunits. In support of this view, sequence analysis of the conserved yeast Mediator components Med4 and Med8 reveals sequence homology to the metazoan Mediator components Trap36 and Arc32. Therefore, 8 of 10 essential genes conserved between S. pombe and S. cerevisiae also have a metazoan homolog, indicating that an evolutionary conserved Mediator core is present in all eukaryotic cells. Our data suggest a closer functional relationship between yeast and metazoan Mediator than previously anticipated.","authors":"Spåhr H, Samuelsen CO, Baraznenok V, Ernest I, Huylebroeck D, Remacle JE, Samuelsson T, Kieselbach T, Holmberg S, Gustafsson CM","authors_abbrev":"Spåhr H et al.","pubmed_publication_date":"09 Oct 2001","pubmed_entrez_date":"2001-09-27","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1105.06","SPAC17C9.05c","SPBC31F10.04c","SPBC31F10.09c","SPBC21.04","SPCC1450.05c","SPBC1A4.10c","SPAC5D6.05","SPBC28F2.12"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:24583014","title":"Slow checkpoint activation kinetics as a safety device in anaphase.","citation":"Curr Biol 2014 Mar 17;24(6):646-51","abstract":"Chromosome attachment to the mitotic spindle in early mitosis is guarded by an Aurora B kinase-dependent error correction mechanism [1, 2] and by the spindle assembly checkpoint (SAC), which delays cell-cycle progression in response to errors in chromosome attachment [3, 4]. The abrupt loss of sister chromatid cohesion at anaphase creates a type of chromosome attachment that in early mitosis would be recognized as erroneous, would elicit Aurora B-dependent destabilization of kinetochore-microtubule attachment, and would activate the checkpoint [5, 6]. However, in anaphase, none of these responses occurs, which is vital to ensure progression through anaphase and faithful chromosome segregation. The difference has been attributed to the drop in CDK1/cyclin B activity that accompanies anaphase and causes Aurora B translocation away from centromeres [7-12] and to the inactivation of the checkpoint by the time of anaphase [10, 11, 13, 14]. Here, we show that checkpoint inactivation may not be crucial because checkpoint activation by anaphase chromosomes is too slow to take effect on the timescale during which anaphase is executed. In addition, we observe that checkpoint activation can still occur for a considerable time after the anaphase-promoting complex/cyclosome (APC/C) becomes active, raising the question whether the checkpoint is indeed completely inactivated by the time of anaphase under physiologic conditions.","doi":"10.1016/j.cub.2014.02.005","authors":"Kamenz J, Hauf S","authors_abbrev":"Kamenz J et al.","pubmed_publication_date":"17 Mar 2014","pubmed_entrez_date":"2014-03-04","publication_year":"2014","canto_session_key":"ff759b3e7d7da717","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silke Hauf","canto_first_approved_date":"2020-06-25 20:18:20","canto_approved_date":"2024-03-28 14:45:38","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-06-14 19:44:35","canto_added_date":"2020-06-14 14:26:44","annotation_curators":[{"name":"Silke Hauf","community_curator":true,"annotation_count":11,"orcid":"0000-0001-5938-721X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.13c","SPBC14C8.01c","SPAC23H3.08c","SPAC19G12.01c","SPAC821.08c","SPCC5E4.04","SPBC3D6.04c","SPBC20F10.06","SPBC582.03","SPCC1795.01c"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2020-06-25"},{"uniquename":"PANTHER:PTHR11039","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:7988","HGNC:16932","SPAC9G1.06c","HGNC:6513","HGNC:7720"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18256467","title":"PXA domain-containing protein Pxa1 is required for normal vacuole function and morphology in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2008 Feb;72(2):548-56","abstract":"PhoX homology (PX) domain-containing proteins play critical roles in vesicular trafficking, protein sorting, and lipid modification in eukaryotic cells. Several proteins with PX domains contain an associated domain termed PXA (PX-associated). Although PXA domain-containing proteins are required for some important cellular processes, the function of the PXA domain is unknown. We identified three PXA domain-containing proteins in Schizosaccharomyces pombe. S. pombe Pxa1p (SPAC5D6.07c) contained only the PXA domain, not the PX domain. To elucidate the role of the PXA domain in eukaryotic cells, we constructed and characterized a disruption mutant, pxa1. The pxa1 disruptant contained enlarged vacuoles and exhibited mislocalization of vacuolar carboxypeptidase Y (CPY). The conversion rate from pro- to mature-CPY was greatly impaired in pxa1 cells, and fluorescence microscopy indicated that a sorting receptor for CPY, Vps10p, mislocalized to the vacuolar membrane. The mutants were also deficient in vacuolar sorting of a multivesicular body (MVB) marker, a ubiquitin-GFP-carboxypeptidase S (Ub-GFP-CPS) fusion protein. Taken together, these results indicate that Pxa1 protein is required for normal vacuole function and morphology in S. pombe.","authors":"Hosomi A, Kawanishi YY, Tanaka N, Takegawa K","authors_abbrev":"Hosomi A et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35901126","title":"Initiator tRNA lacking 1-methyladenosine is targeted by the rapid tRNA decay pathway in evolutionarily distant yeast species.","citation":"PLoS Genet 2022 Jul;18(7):e1010215","abstract":"All tRNAs have numerous modifications, lack of which often results in growth defects in the budding yeast Saccharomyces cerevisiae and neurological or other disorders in humans. In S. cerevisiae, lack of tRNA body modifications can lead to impaired tRNA stability and decay of a subset of the hypomodified tRNAs. Mutants lacking 7-methylguanosine at G46 (m7G46), N2,N2-dimethylguanosine (m2,2G26), or 4-acetylcytidine (ac4C12), in combination with other body modification mutants, target certain mature hypomodified tRNAs to the rapid tRNA decay (RTD) pathway, catalyzed by 5'-3' exonucleases Xrn1 and Rat1, and regulated by Met22. The RTD pathway is conserved in the phylogenetically distant fission yeast Schizosaccharomyces pombe for mutants lacking m7G46. In contrast, S. cerevisiae trm6/gcd10 mutants with reduced 1-methyladenosine (m1A58) specifically target pre-tRNAiMet(CAU) to the nuclear surveillance pathway for 3'-5' exonucleolytic decay by the TRAMP complex and nuclear exosome. We show here that the RTD pathway has an unexpected major role in the biology of m1A58 and tRNAiMet(CAU) in both S. pombe and S. cerevisiae. We find that S. pombe trm6Δ mutants lacking m1A58 are temperature sensitive due to decay of tRNAiMet(CAU) by the RTD pathway. Thus, trm6Δ mutants had reduced levels of tRNAiMet(CAU) and not of eight other tested tRNAs, overexpression of tRNAiMet(CAU) restored growth, and spontaneous suppressors that restored tRNAiMet(CAU) levels had mutations in dhp1/RAT1 or tol1/MET22. In addition, deletion of cid14/TRF4 in the nuclear surveillance pathway did not restore growth. Furthermore, re-examination of S. cerevisiae trm6 mutants revealed a major role of the RTD pathway in maintaining tRNAiMet(CAU) levels, in addition to the known role of the nuclear surveillance pathway. These findings provide evidence for the importance of m1A58 in the biology of tRNAiMet(CAU) throughout eukaryotes, and fuel speculation that the RTD pathway has a major role in quality control of body modification mutants throughout fungi and other eukaryotes.","doi":"10.1371/journal.pgen.1010215","authors":"Tasak M, Phizicky EM","authors_abbrev":"Tasak M et al.","pubmed_publication_date":"Jul 2022","pubmed_entrez_date":"2022-07-28","publication_year":"2022","canto_session_key":"d6f35a8bb66ac367","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Eric Phizicky","canto_first_approved_date":"2024-02-23 14:45:23","canto_approved_date":"2024-05-16 13:25:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-02 11:17:32","canto_added_date":"2022-07-30 00:15:05","annotation_curators":[{"name":"Eric Phizicky","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9G1.12","SPAC26A3.12c","SPAC12G12.13c","SPBTRNAMET.06","SPCC1753.04","SPBC800.08"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2024-02-23"},{"uniquename":"PMID:10591634","title":"Skh1, the MEK component of the mkh1 signaling pathway in Schizosaccharomyces pombe.","citation":"J Cell Sci 2000 Jan;113 ( Pt 1):153-60","abstract":"We previously reported the identification of Mkh1, a MEK kinase in Schizosaccharomyces pombe that is required for cell wall integrity, and we presented genetic evidence that Pmk1/Spm1, a MAP kinase, functions downstream from Mkh1 in the same pathway. Here, we report the identification of Skh1, a MEK (MAP kinase kinase) in S. pombe. The sequence of Skh1 is nearly identical to that of the recently reported Pek1 sequence. We present biochemical and genetic evidence that Skh1 is the MEK component of the Mkh1-Spm1 MAP kinase cascade. Our yeast two-hybrid results indicate that Mkh1, Skh1, and Spm1 physically interact to form a ternary complex. Deletion of mkh1, skh1 or spm1 results in identical phenotypes, including sensitivity to (beta)-glucanase treatment, growth inhibition on media containing KCl, and filamentous growth on medium containing caffeine. Double mutant strains exhibit phenotypes that are identical to the single mutant strains. Furthermore, expression of an activated HA-Skh1(DD )protein suppressed these defects in mkh1(delta) cells, and overexpression of Spm1 suppressed these defects in skh1(delta) cells. We also show that HA-Spm1 is hyper-phosphorylated on tyrosine residues in cells co-expressing the activated HA-Skh1(DD) protein. Furthermore, we found the phosphorylated/activated form of GFP-HA-Spm1 at detectable levels in wild-type cells, but not at appreciable levels in mkh1(delta) or skh1(delta) cells expressing this fusion protein. Together, our results indicate that Mkh1, Skh1 and Spm1 constitute a MAPK cascade in fission yeast.","authors":"Loewith R, Hubberstey A, Young D","authors_abbrev":"Loewith R et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"1999-12-11","publication_year":"2000","canto_session_key":"8df35cf35591f150","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-17 16:00:35","canto_approved_date":"2022-03-15 12:26:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-14 17:28:04","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC543.07","SPBC119.08","SPAC1F3.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-03-17"},{"uniquename":"PMID:11018050","title":"Tea2p is a kinesin-like protein required to generate polarized growth in fission yeast.","citation":"J Cell Biol 2000 Oct 02;151(1):15-28","abstract":"Cytoplasmic microtubules are critical for establishing and maintaining cell shape and polarity. Our investigations of kinesin-like proteins (klps) and morphological mutants in the fission yeast Schizosaccharomyces pombe have identified a kinesin-like gene, tea2(+), that is required for cells to generate proper polarized growth. Cells deleted for this gene are often bent during exponential growth and initiate growth from improper sites as they exit stationary phase. They have a reduced cytoplasmic microtubule network and display severe morphological defects in genetic backgrounds that produce long cells. The tip-specific marker, Tea1p, is mislocalized in both tea2-1 and tea2Delta cells, indicating that Tea2p function is necessary for proper localization of Tea1p. Tea2p is localized to the tips of the cell and in a punctate pattern within the cell, often coincident with the ends of cytoplasmic microtubules. These results suggest that this kinesin promotes microtubule growth, possibly through interactions with the microtubule end, and that it is important for establishing and maintaining polarized growth along the long axis of the cell.","authors":"Browning H, Hayles J, Mata J, Aveline L, Nurse P, McIntosh JR","authors_abbrev":"Browning H et al.","pubmed_publication_date":"02 Oct 2000","pubmed_entrez_date":"2000-10-06","publication_year":"2000","canto_session_key":"b19dfb2b27f82b53","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-03-26 12:48:17","canto_approved_date":"2026-01-04 13:21:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-28 15:39:13","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":29,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.20c","SPCC1223.06","SPAC1834.07","SPAC664.10","SPAC3A11.14c","SPAC24H6.05"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-03-26"},{"uniquename":"PMID:8126103","title":"Stacking of Golgi cisternae in Schizosaccharomyces pombe requires intact microtubules.","citation":"J Cell Sci 1993 Dec;106 ( Pt 4):1227-37","abstract":"Fission yeast was treated with the anti-microtubule agent, thiabendazole. Cytoplasmic microtubules broke down with a half-time of less than 10 minutes followed closely by the unstacking of Golgi cisternae. The final product appeared to be single Golgi cisternae. No other organelle seemed to be affected by this treatment, which was completely reversible. The nda3 mutant strain has an altered beta-tubulin and its cytoplasmic microtubules are resistant to thiabendazole. The Golgi in this cold-sensitive mutant was unaffected by treatment at the permissive temperature but unstacked at the non-permissive temperature even in the absence of thiabendazole. Taken together these data show that disruption of the microtubular network can cause dissociation of Golgi cisternae. Newly synthesised acid phosphatase was transported and secreted to the same extent and with the same kinetics whether or not the Golgi was unstacked. The possible role of microtubules in Golgi stacking and the lack of effect on secretion are discussed.","authors":"Ayscough K, Hajibagheri NM, Watson R, Warren G","authors_abbrev":"Ayscough K et al.","pubmed_publication_date":"Dec 1993","pubmed_entrez_date":"1993-12-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35482104","title":"Mechanisms of gene regulation by histone degradation in adaptation of yeast: an overview of recent advances.","citation":"Arch Microbiol 2022 Apr 28;204(5):287","abstract":"Histones are important component of eukaryotic cells chromatin and consist of arginine and lysine residues. Histones play an important role in the protection of DNA. Their contents significantly affect high-level chromatin structure formation, gene expression, DNA replication, and other important life activities. Protein degradation is an important regulatory mechanism of histone content. Recent studies have revealed that modification of amino acid sequence is directly related to histone breakdown. In addition, histone degradation is closely related to covalent modifications, such as ubiquitination and acetylation, which are considered to be driving factors in gene regulation. Gene regulation is an important mechanism in adaptation to the environment and survival of species. With the introduction of highly efficient technology, various mutations in histones have been identified in yeast. In the field of epigenetics and the transmission of chromatin states, two widely used model organisms are the budding yeast Saccharomyces cerevisiae and Schizosaccharomyces pombe. Higher eukaryotes can use their silent loci to maintain their epigenetic states and providing the base to investigate mechanisms underlying development. Therfore, both species have contributed a plethora of information on these mechanisms in both yeast and higher eukaryotes. This study focuses on the role of histone modifications in controlling telomeric silencing in Saccharomyces cerevisiae and centromeric silencing in S. pombe as examples of genetic loci that demonstrate epigenetic inheritance. In view of recent advances, this review focuses on the post-translational modification of histone amino acid residues and reviews the relationship between histone degradation and amino acid residue modification.","doi":"10.1007/s00203-022-02897-8","authors":"Khan SU, Khan MU, Kalsoom F, Khan MI, Gao S, Unar A, Zubair M, Bilal M","authors_abbrev":"Khan SU et al.","pubmed_publication_date":"28 Apr 2022","pubmed_entrez_date":"2022-04-28","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-04-30 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6294096","title":"The primary structure of the alcohol dehydrogenase gene from the fission yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1983 Jan 10;258(1):143-9","abstract":"We have cloned and sequenced the alcohol dehydrogenase gene of the fission yeast Schizosaccharomyces pombe. The gene was isolated by transformation and complementation of a Saccharomyces cerevisiae strain which lacked functional alcohol dehydrogenase with an S. pombe gene bank constructed in the autonomously replicating yeast plasmid YEp13. Southern hybridization analysis indicates that S. pombe contains only one alcohol dehydrogenase gene. The structural region of the gene is 50% homologous to the alcohol dehydrogenase encoding genes of the budding yeast S. cerevisiae. The gene exhibits a very strong codon usage bias; with the set of predominantly used codons generally resembling that which S. cerevisiae employs preferentially. All of the differences in codon usage bias between S. pombe and S. cerevisiae are in the direction of greater G + C content in S. pombe codons. It is argued that this observation supports the hypothesis that selection toward uniform codon-anticodon binding energies contributes to codon usage bias and that the optimum binding energy is, on the average, higher in S. pombe than S. cerevisiae.","authors":"Russell PR, Hall BD","authors_abbrev":"Russell PR et al.","pubmed_publication_date":"10 Jan 1983","pubmed_entrez_date":"1983-01-10","publication_year":"1983","canto_session_key":"5db90878ddf12f56","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-03-20 01:46:13","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-31 18:05:26","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC13B11.01"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-31"},{"uniquename":"PMID:19026779","title":"The structure of Fcp1, an essential RNA polymerase II CTD phosphatase.","citation":"Mol Cell 2008 Nov 21;32(4):478-90","abstract":"Kinases and phosphatases regulate mRNA synthesis and processing by phosphorylating and dephosphorylating the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. Fcp1 is an essential CTD phosphatase that preferentially hydrolyzes Ser2-PO(4) of the tandem YSPTSPS CTD heptad array. Fcp1 crystal structures were captured at two stages of the reaction pathway: a Mg-BeF(3) complex that mimics the aspartylphosphate intermediate and a Mg-AlF(4)(-) complex that mimics the transition state of the hydrolysis step. Fcp1 is a Y-shaped protein composed of an acylphosphatase domain located at the base of a deep canyon formed by flanking modules that are missing from the small CTD phosphatase (SCP) clade: an Fcp1-specific helical domain and a C-terminal BRCA1 C-terminal (BRCT) domain. The structure and mutational analysis reveals that Fcp1 and Scp1 (a Ser5-selective phosphatase) adopt different CTD-binding modes; we surmise the CTD threads through the Fcp1 canyon to access the active site.","doi":"10.1016/j.molcel.2008.09.021","authors":"Ghosh A, Shuman S, Lima CD","authors_abbrev":"Ghosh A et al.","pubmed_publication_date":"21 Nov 2008","pubmed_entrez_date":"2008-11-26","publication_year":"2008","canto_session_key":"bb6fc09fed8a5c2c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-15 08:57:53","canto_approved_date":"2024-05-16 13:13:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-15 08:57:46","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPAC19B12.05c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2023-02-15","pdb_entries":[{"pdb_id":"3ef0","gene_chains":[{"gene_uniquename":"SPAC19B12.05c","chain":"A","position":"149-580"}],"title":"The Structure of Fcp1, an essential RNA polymerase II CTD phosphatase","entry_authors":"Ghosh A,Lima CD","entry_authors_abbrev":"Ghosh A et al.","reference_uniquename":"PMID:19026779","experimental_method":"X-ray","resolution":"2.1"},{"pdb_id":"3ef1","gene_chains":[{"gene_uniquename":"SPAC19B12.05c","chain":"A","position":"140-580"}],"title":"The Structure of Fcp1, an essential RNA polymerase II CTD phosphatase","entry_authors":"Ghosh A,Lima CD","entry_authors_abbrev":"Ghosh A et al.","reference_uniquename":"PMID:19026779","experimental_method":"X-ray","resolution":"2.15"}]},{"uniquename":"PMID:1527180","title":"Genetic interactions in the control of septation in Schizosaccharomyces pombe.","citation":"J Cell Sci 1992 Apr;101 ( Pt 4):801-8","abstract":"We have used genetic and molecular techniques to investigate the interactions among genes required for the initiation and regulation of septum formation in Schizosaccharomyces pombe. Our data suggest that the products of the cdc7, cdc11, cdc14 and cdc16 genes interact. These activities may regulate the function of the cdc15 gene product. A model for the control of septation in fission yeast is presented.","authors":"Marks J, Fankhauser C, Simanis V","authors_abbrev":"Marks J et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPAC20G8.05c","SPBC24C6.07","SPCC1739.11c","SPBC21.06c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:38455543","title":"Initial nutrient condition determines the recovery speed of quiescent cells in fission yeast.","citation":"Heliyon 2024 Mar 15;10(5):e26558","abstract":"Most of microbe cells spend the majority of their times in quiescence due to unfavorable environmental conditions. The study of this dominant state is crucial for understanding the basic cell physiology. Retained recovery ability is a critical property of quiescent cells, which consists of two features: how long the cells can survive (the survivability) and how fast they can recover (the recovery activity). While the survivability has been extensively studied under the background of chronological aging, how the recovery activity depends on the quiescent time and what factors influence its dynamics have not been addressed quantitatively. In this work, we systematically quantified both the survivability and the recovery activity of long-lived quiescent fission yeast cells at the single cell level under various nutrient conditions. It provides the most profound evolutionary dynamics of quiescent cell regeneration ability described to date. We found that the single cell recovery time linearly increased with the starvation time before the survivability significantly declined. This linearity was robust under various nutrient conditions and the recovery speed was predetermined by the initial nutrient condition. Transcriptome profiling further revealed that quiescence states under different nutrient conditions evolve in a common trajectory but with different speed. Our results demonstrated that cellular quiescence has a continuous spectrum of depths and its physiology is greatly influenced by environmental conditions.","doi":"10.1016/j.heliyon.2024.e26558","authors":"Liu Q, Sheng N, Zhang Z, He C, Zhao Y, Sun H, Chen J, Yang X, Tang C","authors_abbrev":"Liu Q et al.","pubmed_publication_date":"15 Mar 2024","pubmed_entrez_date":"2024-03-08","publication_year":"2024","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2024-03-09 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37556551","title":"The minimal intrinsic stochasticity of constitutively expressed eukaryotic genes is sub-Poissonian.","citation":"Sci Adv 2023 Aug 09;9(32):eadh5138","abstract":"Gene expression inherently gives rise to stochastic variation (\"noise\") in the production of gene products. Minimizing noise is crucial for ensuring reliable cellular functions. However, noise cannot be suppressed below a certain intrinsic limit. For constitutively expressed genes, this limit is typically assumed to be Poissonian noise, wherein the variance in mRNA numbers is equal to their mean. Here, we demonstrate that several cell division genes in fission yeast exhibit mRNA variances significantly below this limit. The reduced variance can be explained by a gene expression model incorporating multiple transcription and mRNA degradation steps. Notably, in this sub-Poissonian regime, distinct from Poissonian or super-Poissonian regimes, cytoplasmic noise is effectively suppressed through a higher mRNA export rate. Our findings redefine the lower limit of eukaryotic gene expression noise and uncover molecular requirements for achieving ultralow noise, which is expected to be important for vital cellular functions.","doi":"10.1126/sciadv.adh5138","authors":"Weidemann DE, Holehouse J, Singh A, Grima R, Hauf S","authors_abbrev":"Weidemann DE et al.","pubmed_publication_date":"09 Aug 2023","pubmed_entrez_date":"2023-08-09","publication_year":"2023","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-08-10 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15793566","title":"CSN facilitates Cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability.","citation":"Nat Cell Biol 2005 Apr;7(4):387-91","abstract":"The COP9 signalosome (CSN) is known to bind cullin-RING ubiquitin ligases (CRLs) and to promote their activity in vivo. The mechanism of this stimulation has remained enigmatic because CSN's intrinsic and associated enzymatic activities paradoxically inhibit CRL activity in vitro. Reconciling this paradox, we show here that Csn5-catalysed cullin (Cul) deneddylation and Ubp12-mediated deubiquitination cooperate in maintaining the stability of labile substrate adapters, thus facilitating CRL function. Various fission-yeast csn and ubp12 deletion mutants have lower levels of the Cul3p adapter Btb3p. This decrease is due to increased autocatalytic, Cul3p-dependent, ubiquitination and the subsequent degradation of Btb3p. The CSN-Ubp12p pathway also maintains the stability of the Cul1p adapter Pop1p, a mechanism required for the efficient destruction of its cognate substrate Rum1p. Emphasizing the physiological importance of this mechanism, we found that the dispensable csn5 and ubp12 genes become essential for viability when adapter recruitment to Cul1p is compromised. Our data suggest that maintenance of adapter stability is a general mechanism of CRL control by the CSN.","authors":"Wee S, Geyer RK, Toda T, Wolf DA","authors_abbrev":"Wee S et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-03-29","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1687.13c","SPAC22A12.03c","SPBC409.05","SPCC1494.05c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:5439575","title":"DNA synthesis in the fission yeast Schizosaccharomyces pombe.","citation":"Exp Cell Res 1970 Apr;60(1):16-26","abstract":"","authors":"Bostock CJ","authors_abbrev":"Bostock CJ","pubmed_publication_date":"Apr 1970","pubmed_entrez_date":"1970-04-01","publication_year":"1970","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36430366","title":"Fission Yeast Rho1p-GEFs: From Polarity and Cell Wall Synthesis to Genome Stability.","citation":"Int J Mol Sci 2022 Nov 11;23(22)","abstract":"Rho1p is a membrane-associated protein that belongs to the Rho family of small GTPases. These proteins coordinate processes such as actin remodelling and polarised secretion to maintain the shape and homeostasis of yeast cells. In response to extracellular stimuli, Rho1p undergoes conformational switching between a guanosine triphosphate (GTP)-bound active state and a guanosine diphosphate (GDP)-bound inactive state. Cycling is improved with guanine nucleotide exchange factor (GEF) activity necessary to activate signalling and GTPase activating protein (GAP) activity required for subsequent signal depletion. This review focuses on fission yeast Rho1p GEFs, Rgf1p, Rgf2p, and Rgf3p that belong to the family of DH-PH domain-containing Dbl-related GEFs. They are multi-domain proteins that detect biological signals that induce or inhibit their catalytic activity over Rho1p. Each of them activates Rho1p in different places and times. Rgf1p acts preferentially during polarised growth. Rgf2p is required for sporulation, and Rgf3p plays an essential function in septum synthesis. In addition, we outline the noncanonical roles of Rho1p-GEFs in genomic instability.","doi":"10.3390/ijms232213888","authors":"García P, Celador R, Pérez-Parrilla J, Sánchez Y","authors_abbrev":"García P et al.","pubmed_publication_date":"11 Nov 2022","pubmed_entrez_date":"2022-11-26","publication_year":"2022","canto_session_key":"c73a8ef62dd30b2e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-11-27 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10756203","title":"Fission yeast hrp1, a chromodomain ATPase, is required for proper chromosome segregation and its overexpression interferes with chromatin condensation.","citation":"Nucleic Acids Res 2000 May 01;28(9):2004-11","abstract":"Hrp1 of Schizosaccharomyces pombe is a member of the CHD protein family, characterized by a chromodomain, a Myb-like telobox-related DNA-binding domain and a SNF2-related helicase/ATPase domain. CHD proteins are thought to be required for modification of the chromatin structure in transcription, but the exact roles of CHD proteins are not known. Here we examine the sub-cellular localization and biochemical activity of Hrp1 and the phenotypes of hrp1 Delta and Hrp1-overexpressing strains. Fluorescence microscopy revealed that Hrp1 protein is targeted to the nucleus. We found that Hrp1 exhibited DNA-dependent ATPase activity, stimulated by both single- and double-stranded DNA. Overexpression of Hrp1 caused slow cell growth accompanied by defective chromosome condensation in anaphase resulting in a 'cut' (celluntimelytorn) phenotype and chromosome loss. The hrp1 Delta mutation also caused abnormal anaphase and mini-chromosome loss phenotypes. Electron micrographs demonstrated that aberrantly shaped nucleoli appeared in Hrp1-overexpressing cells. Therefore, these results suggest that Hrp1 may play a role in mitotic chromosome segregation and maintenance of chromatin structure by utilizing the energy from ATP hydrolysis.","authors":"Yoo EJ, Jin YH, Jang YK, Bjerling P, Tabish M, Hong SH, Ekwall K, Park SD","authors_abbrev":"Yoo EJ et al.","pubmed_publication_date":"01 May 2000","pubmed_entrez_date":"2000-04-11","publication_year":"2000","canto_session_key":"45341b622c4aacd3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-02 11:43:25","canto_approved_date":"2021-06-21 19:19:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-02 11:43:16","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-02"},{"uniquename":"PMID:19808886","title":"Myosin V spatially regulates microtubule dynamics and promotes the ubiquitin-dependent degradation of the fission yeast CLIP-170 homologue, Tip1.","citation":"J Cell Sci 2009 Nov 01;122(Pt 21):3862-72","abstract":"Coordination between microtubule and actin cytoskeletons plays a crucial role during the establishment of cell polarity. In fission yeast, the microtubule cytoskeleton regulates the distribution of actin assembly at the new growing end during the monopolar-to-bipolar growth transition. Here, we describe a novel mechanism in which a myosin V modulates the spatial coordination of proteolysis and microtubule dynamics. In cells lacking a functional copy of the class V myosin, Myo52, the plus ends of microtubules fail to undergo catastrophe on contacting the cell end and continue to grow, curling around the end of the cell. We show that this actin-associated motor regulates the efficient ubiquitin-dependent proteolysis of the Schizosaccharomyces pombe CLIP-170 homologue, Tip1. Myo52 facilitates microtubule catastrophe by enhancing Tip1 removal from the plus end of growing microtubules at the cell tips. There, Myo52 and the ubiquitin receptor, Dph1, work in concert to target Tip1 for degradation.","doi":"10.1242/jcs.054460","authors":"Martín-García R, Mulvihill DP","authors_abbrev":"Martín-García R et al.","pubmed_publication_date":"01 Nov 2009","pubmed_entrez_date":"2009-10-08","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.16","SPCC1919.10c","SPAC3C7.12"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11758939","title":"Genetic analysis of the His-to-Asp phosphorelay implicated in mitotic cell cycle control: involvement of histidine-kinase genes of Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2001 Oct;65(10):2347-52","abstract":"Common histidine-to-aspartate (His-to-Asp) phosphorelay signaling systems involve three types of signaling components: a sensor His-kinase, a response regulator, and a histidine-containing phosphotransfer (HPt) protein. In the fission yeast Schizosaccharomyces pombe, two response regulators, Mcs4 and Prr1, have been identified, and it was shown that they are involved in signal transduction in stress responses. Furthermore, Mcs4 and Prr1 appear to be involved in mitotic cell-cycle control and meiosis, respectively. Recently we have identified Spy1 (also known as Mpr1), which encodes an HPt phosphotransmitter, and reported that Spy1, together with Mcs4, plays a role in cell cycle regulation. In this study, we identified and characterized three genes encoding histidine kinase, named Phk1, Phk2, and Phk3 (S. pombe histidine kinase) (also referred as Mak2, Mak3, and Mak1, respectively). Deletion of individual kinase genes has no apparent phenotypes but multiple deletion of these kinases showed the same phenotype of Spyl (Mpr1)-deficient cells, indicating precocious entry into M phase. These results indicated that three histidine kinases that work upstream of the HPt-transmitter, Spy1 (Mpr1), have a redundant function in cell cycle control.","authors":"Aoyama K, Aiba H, Mizuno T","authors_abbrev":"Aoyama K et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2002-01-05","publication_year":"2001","canto_session_key":"e6f10a2b668f63b5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-01-21 16:30:11","canto_approved_date":"2022-09-29 14:56:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-01-21 16:30:03","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.08","SPCC74.06","SPBC887.10","SPBC725.02","SPAC27E2.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-01-21"},{"uniquename":"PMID:31353023","title":"De Novo Heterozygous POLR2A Variants Cause a Neurodevelopmental Syndrome with Profound Infantile-Onset Hypotonia.","citation":"Am J Hum Genet 2019 Aug 01;105(2):283-301","abstract":"The RNA polymerase II complex (pol II) is responsible for transcription of all ∼21,000 human protein-encoding genes. Here, we describe sixteen individuals harboring de novo heterozygous variants in POLR2A, encoding RPB1, the largest subunit of pol II. An iterative approach combining structural evaluation and mass spectrometry analyses, the use of S. cerevisiae as a model system, and the assessment of cell viability in HeLa cells allowed us to classify eleven variants as probably disease-causing and four variants as possibly disease-causing. The significance of one variant remains unresolved. By quantification of phenotypic severity, we could distinguish mild and severe phenotypic consequences of the disease-causing variants. Missense variants expected to exert only mild structural effects led to a malfunctioning pol II enzyme, thereby inducing a dominant-negative effect on gene transcription. Intriguingly, individuals carrying these variants presented with a severe phenotype dominated by profound infantile-onset hypotonia and developmental delay. Conversely, individuals carrying variants expected to result in complete loss of function, thus reduced levels of functional pol II from the normal allele, exhibited the mildest phenotypes. We conclude that subtle variants that are central in functionally important domains of POLR2A cause a neurodevelopmental syndrome characterized by profound infantile-onset hypotonia and developmental delay through a dominant-negative effect on pol-II-mediated transcription of DNA.","doi":"10.1016/j.ajhg.2019.06.016","authors":"Haijes HA, Koster MJE, Rehmann H, Li D, Hakonarson H, Cappuccio G, Hancarova M, Lehalle D, Reardon W, Schaefer GB, Lehman A, van de Laar IMBH, Tesselaar CD, Turner C, Goldenberg A, Patrier S, Thevenon J, Pinelli M, Brunetti-Pierri N, Prchalová D, Havlovicová M, Vlckova M, Sedláček Z, Lopez E, Ragoussis V, Pagnamenta AT, Kini U, Vos HR, van Es RM, van Schaik RFMA, van Essen TAJ, Kibaek M, Taylor JC, Sullivan J, Shashi V, Petrovski S, Fagerberg C, Martin DM, van Gassen KLI, Pfundt R, Falk MJ, McCormick EM, Timmers HTM, van Hasselt PM","authors_abbrev":"Haijes HA et al.","pubmed_publication_date":"01 Aug 2019","pubmed_entrez_date":"2019-07-30","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.12"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9585506","title":"Phosphorylation and association with the transcription factor Atf1 regulate localization of Spc1/Sty1 stress-activated kinase in fission yeast.","citation":"Genes Dev 1998 May 15;12(10):1464-73","abstract":"Control of gene expression by stress-activated protein kinase (SAPK) cascades is crucial for combating cytotoxic stress. Elements of these cascades have been investigated in detail, but regulation of stress signal transduction from the cytoplasm to the nucleus is poorly understood. Herein are reported subcellular localization studies of fission yeast Spc1, a homolog of human p38 and budding yeast Hog1p SAPKs. Stress induces transient nuclear localization of Spc1. Nuclear translocation of Spc1 is coupled with disassociation from its activator kinase Wis1. However, Spc1 does not concentrate in the nucleus of Deltawis1 cells; therefore Wis1 does not tether Spc1 in the cytoplasm. Unphosphorylatable forms of Spc1 are dispersed in the cytoplasm and nucleus, even in cells that also produce wild-type Spc1. Thus, Spc1 must be phosphorylated by Wis1 to localize in the nucleus. Nuclear retention of Spc1 requires Atf1, a transcription factor that is the key nuclear substrate of Spc1. Nuclear localization of Atf1 requires Pcr1, a heterodimerization partner of Atf1. These studies show that phosphorylation and association with Atf1 are required for nuclear localization of Spc1.","authors":"Gaits F, Degols G, Shiozaki K, Russell P","authors_abbrev":"Gaits F et al.","pubmed_publication_date":"15 May 1998","pubmed_entrez_date":"1998-05-29","publication_year":"1998","canto_session_key":"3e62111aa45321c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-08 08:17:35","canto_approved_date":"2024-04-04 07:32:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-26 08:36:14","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC21E11.03c","SPAC24B11.06c","SPBC29B5.01","SPBC409.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-09-08"},{"uniquename":"PMID:3172236","title":"Two distinct mechanisms for deletion in mitochondrial DNA of Schizosaccharomyces pombe mutator strains. Slipped mispairing mediated by direct repeats and erroneous intron splicing.","citation":"J Mol Biol 1988 Aug 20;202(4):725-34","abstract":"Mutator strains of the fission yeast Schizosaccharomyces pombe produce mitochondrial respiratory deficient mutants at a high rate, and roughly 20% of these mutants carry deletions in the range of 50 to 1500 base-pairs. To elucidate the mechanism of deletion we have sequenced ten deletion mutants in the mosaic gene encoding apocytochrome b (cob) and three in the split gene coding for the first subunit of cytochrome c oxidase (cox1). Of 13 deletions, ten are correlated with the presence of direct repeats, which could promote deletions by slipped mispairing during DNA replication. In some of these mutants, the termini are located in possible DNA secondary structures. In three independently isolated mutants with identical deletions in the cob gene, the 5' deletion endpoint coincides with the 3' splice point of the intron, whereas the 3' endpoint of the deletion exhibits pronounced homology with the 5' splice point of the intron. This result suggests that these deletions might be initiated by erroneous RNA splicing.","authors":"Ahne A, Müller-Derlich J, Merlos-Lange AM, Kanbay F, Wolf K, Lang BF","authors_abbrev":"Ahne A et al.","pubmed_publication_date":"20 Aug 1988","pubmed_entrez_date":"1988-08-20","publication_year":"1988","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27803258","title":"Analysis of Heterochromatin in Schizosaccharomyces pombe.","citation":"Cold Spring Harb Protoc 2016 Nov 01;2016(11)","abstract":"This introduction briefly describes the biology of heterochromatin in the fission yeast Schizosaccharomyces pombe We highlight some of the salient features of fission yeast that render it an excellent unicellular eukaryote for studying heterochromatin. We then discuss key aspects of heterochromatin that are of interest to those in the field, and last we introduce experimental approaches often used to investigate heterochromatin.","doi":"10.1101/pdb.top079889","authors":"Cam HP, Whitehall S","authors_abbrev":"Cam HP et al.","pubmed_publication_date":"01 Nov 2016","pubmed_entrez_date":"2016-11-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-04 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20228279","title":"New classes of PDE7 inhibitors identified by a fission yeast-based HTS.","citation":"J Biomol Screen 2010 Apr;15(4):359-67","abstract":"Studies of the phosphodiesterase PDE7 family are impeded by there being only one commercially available PDE7 inhibitor, BRL50481. The authors have employed a high-throughput screen of commercial chemical libraries, using a fission yeast-based assay, to identify PDE7 inhibitors that include steroids, podocarpanes, and an unusual heterocyclic compound, BC30. In vitro enzyme assays measuring the potency of BC30 and 2 podocarpanes, in comparison with BRL50481, produce data consistent with those from yeast-based assays. In other enzyme assays, BC30 stimulates the PDE4D catalytic domain but not full-length PDE4D2, suggesting an allosteric site of action. BC30 significantly enhances the anti-inflammatory effect of the PDE4 inhibitor rolipram as measured by release of tumor necrosis factor alpha from activated monocytes. These studies introduce several new PDE7 inhibitors that may be excellent candidates for medicinal chemistry because of the requirements for drug-like characteristics placed on them by the nature of the yeast-based screen.","doi":"10.1177/1087057110362100","authors":"Alaamery MA, Wyman AR, Ivey FD, Allain C, Demirbas D, Wang L, Ceyhan O, Hoffman CS","authors_abbrev":"Alaamery MA et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-03-16","publication_year":"2010","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10748208","title":"Fidelity of eucaryotic DNA polymerase delta holoenzyme from Schizosaccharomyces pombe.","citation":"J Biol Chem 2000 Jun 09;275(23):17677-82","abstract":"The fidelity of Schizosaccharomyces pombe DNA polymerase delta was measured in the presence or absence of its processivity subunits, proliferating cell nuclear antigen (PCNA) sliding clamp and replication factor C (RFC) clamp-loading complex, using a synthetic 30-mer primer/100-mer template. Synthesis by pol delta alone was distributive. Processive synthesis occurred in the presence of PCNA, RFC, and Escherichia coli single strand DNA-binding protein (SSB) and required the presence of ATP. \"Passive\" self-loading of PCNA onto DNA takes place in the absence of RFC, in an ATP-independent reaction, which was strongly inhibited by SSB. The nucleotide substitution error rate for pol delta holoenzyme (HE) (pol delta + PCNA + RFC) was 4.6 x 10(-4) for T.G mispairs, 5.3 x 10(-5) for G.G mispairs, and 4.5 x 10(-6) for A.G mispairs. The T.G misincorporation frequency for pol delta without the accessory proteins was unchanged. The fidelity of pol delta HE was between 1 and 2 orders of magnitude lower than that measured for the E. coli pol III HE at the same template position. This relatively low fidelity was caused by inefficient proofreading by the S. pombe polymerase-associated proofreading exonuclease. The S. pombe 3'-exonuclease activity was also extremely inefficient in excising primer-3'-terminal mismatches in the absence of dNTP substrates and in hydrolyzing single-stranded DNA. A comparison of pol delta HE with E. coli pol IIIalpha HE (lacking the proofreading exonuclease subunit) showed that both holoenzymes exhibit similar error rates for each mispair.","authors":"Chen X, Zuo S, Kelman Z, O'Donnell M, Hurwitz J, Goodman MF","authors_abbrev":"Chen X et al.","pubmed_publication_date":"09 Jun 2000","pubmed_entrez_date":"2000-04-05","publication_year":"2000","canto_session_key":"e51a9842529e3033","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-22 13:37:27","canto_approved_date":"2024-09-27 07:04:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-22 13:36:58","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23E6.07c","SPBC336.04","SPAC23D3.02","SPAC1687.03c","SPBC12D12.02c","SPBC83.14c","SPBC16D10.09","SPAC27E2.10c","SPAC27E2.05","SPBC1734.02c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-04-22"},{"uniquename":"EMBL:AU012044","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9878845","title":"The Gas1 glycoprotein, a putative wall polymer cross-linker.","citation":"Biochim Biophys Acta 1999 Jan 06;1426(2):385-400","abstract":"The yeast cell wall, which for years has been regarded as a static cellular component, has been revealed to be dynamic in its structure and composition and complex in its enzymatic activity. The S. cerevisiae cell wall is composed of beta-1,3/beta-1,6-glucans, mannoproteins, and chitin, which are assembled into an extracellular matrix essential for maintenance of cell integrity. Gas1p, a glycoprotein anchored to the outer leaflet of the plasma membrane through a glycosylphosphatidylinositol, plays a key role in cell wall assembly. Loss of Gas1p leads to several morphogenetic defects and to a decrease in the amount of cross-links between the cell wall glucans. These defects in turn trigger a compensatory response that guarantees cell viability. Several Gas1p homologs have been isolated from Candida species and S. pombe. The Gas1p family also includes two plant proteins with endo-beta-1,3-glucanase activity. Sequence comparisons reveal that Gas1p family proteins have a modular organization of domains. The genetic and molecular analyses reviewed here suggest that Gas1p could play a role as a polymer cross-linker, presumably by catalyzing a transglycosylation reaction.","authors":"Popolo L, Vai M","authors_abbrev":"Popolo L et al.","pubmed_publication_date":"06 Jan 1999","pubmed_entrez_date":"1999-01-08","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19933165","title":"CYSTM, a novel cysteine-rich transmembrane module with a role in stress tolerance across eukaryotes.","citation":"Bioinformatics 2010 Jan 15;26(2):149-52","abstract":"Using sensitive sequence profile analysis, we identify a hitherto uncharacterized cysteine-rich, transmembrane (TM) module, CYSTM, found in a wide range of tail-anchored membrane proteins across eukaryotes. This superfamily includes Schizosaccharomyces Uvi15, Arabidopsis PCC1, Digtaria CDT1 and Saccharomyces proteins YDL012C and YDR210W, which have all been implicated in resistance/response to stress or pathogens. Based on the pattern of conserved cysteines and data from different chemical genetics studies, we suggest that CYSTM proteins might have critical role in responding to deleterious compounds at the plasma membrane via chelation or redox-based mechanisms. Thus, CYSTM proteins are likely to be part of a novel cellular protective mechanism that is widely active in eukaryotes, including humans.\nSupplementary data are available at Bioinformatics online.","doi":"10.1093/bioinformatics/btp647","authors":"Venancio TM, Aravind L","authors_abbrev":"Venancio TM et al.","pubmed_publication_date":"15 Jan 2010","pubmed_entrez_date":"2009-11-26","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC649.04","HGNC:30239"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18597043","title":"FHA-RING ubiquitin ligases in cell division cycle control.","citation":"Cell Mol Life Sci 2008 Nov;65(21):3458-66","abstract":"Despite the common occurrence of forkhead associated (FHA) phosphopeptide-binding domains and really interesting new gene (RING) E3 ubiquitin ligase domains, gene products containing both an N-terminal FHA domain and C-terminal RING domain constitute a highly distinctive intersection. Characterized FHA-RING ligases include the two vertebrate proteins, Checkpoint with FHA and RING (Chfr) and RING finger 8 (Rnf8), as well as three fungal proteins, Defective in mitosis (Dma1), Chf1 and Chf2. These FHA-RING ligases play roles in negative regulation of the cell division cycle, apparently by coupling protein phosphorylation events to specific ubiquitylation of target proteins. Here, the available data on upstream and downstream regulation of and by FHA-RING ligases are reviewed.","doi":"10.1007/s00018-008-8220-1","authors":"Brooks L, Heimsath EG, Loring GL, Brenner C","authors_abbrev":"Brooks L et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-07-04","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15130831","title":"Innovation from reduction: gene loss, domain loss and sequence divergence in genome evolution.","citation":"Appl Bioinformatics 2003;2(1):13-34","abstract":"Analyses of genome sequences have revealed a surprisingly variable distribution of genes, reflecting the generation of novel genes, lateral gene transfer and gene loss. The impact of gene loss on organisms has been difficult to examine, but the loss of protein coding genes, the loss of domains within proteins and the divergence of genes have made surprising contributions to the differences among organisms. This paper reviews surveys of gene loss and divergence in fungal and archaeal genomes that indicate suites of functionally related genes tend to undergo loss and divergence. Instances of fungal gene loss highlighted here suggest that specific cellular systems have changed, such as Ca 2+ biology in Saccharomyces cerevisiae and peroxisome function in Schizosaccharomyces pombe. Analyses of loss and divergence can provide specific predictions regarding protein-protein interactions, and the relationship between networks of protein interactions and loss may form a part of a parametric model of genome evolution.","authors":"Braun EL","authors_abbrev":"Braun EL","pubmed_publication_date":"2003","pubmed_entrez_date":"2004-05-08","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40651364","title":"Understanding the molecular basis of the mutation in the RNA polymerase III subunit Rpc10 (R41W)- associated with hypomyelinating leukodystrophy in the yeast homolog Rpc11.","citation":"Biochem Biophys Res Commun 2025 Sep 01;777:152310","abstract":"RNA Polymerase III (RNAP III) is crucial for synthesizing abundant non-coding RNAs like tRNAs and 5S rRNA. Its activity is tightly controlled, and disruptions often lead to severe diseases. Mutations in RNAP III subunits are linked to a range of human disorders, including hypomyelinating leukodystrophy (HLD). Among the various mutations identified in patients with HLD, the POLR3K (RPC10)-R41W mutation has drawn particular attention because of its localization in the linker domain of RPC10, a domain that connects the N-terminal (NTD) and C-terminal (CTD) zinc ribbon motifs. However, the mechanism by which the RPC10-R41W mutation contributes to the disease pathogenesis remains poorly understood. This study modeled the human POLR3K-R41W (RPC10-R41W) mutation in the yeast homolog C11 at the conserved position (R43W in S. cerevisiae and R41W in S. pombe). We systematically investigated its impact on RNAP III functions, including RNA 3'-end cleavage, transcription termination, and overall cell growth. Our findings demonstrate that this mutation specifically impairs the RNA 3' cleavage activity of C11 without compromising transcription termination. We observed slow growth in yeast models, particularly under lower temperatures, suggesting a potential stress response mechanism. Additionally, the mutation was associated with the lengthening of 3'-oligo(U) sequences in tRNAs. This C11 mutation also shows a fatal phenotype in the Sen1-deleted strain, an important helicase for RNAP III transcription termination in S. pombe. These observations provide valuable insight into how this linker domain mutation affects the cleavage activity, potentially contributing to cellular stress responses and the broader implications for HLD.","doi":"10.1016/j.bbrc.2025.152310","authors":"Mishra S, Sonika S, Khushbu K, Verma S","authors_abbrev":"Mishra S et al.","pubmed_publication_date":"01 Sep 2025","pubmed_entrez_date":"2025-07-12","publication_year":"2025","canto_session_key":"ea25fb3e5b3e88dd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-13 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27941123","title":"The RNA-induced transcriptional silencing complex targets chromatin exclusively via interacting with nascent transcripts.","citation":"Genes Dev 2016 Dec 01;30(23):2571-2580","abstract":"Small RNAs regulate chromatin modification and transcriptional gene silencing across the eukaryotic kingdom. Although these processes have been well studied, fundamental mechanistic aspects remain obscure. Specifically, it is unclear exactly how small RNA-loaded Argonaute protein complexes target chromatin to mediate silencing. Here, using fission yeast, we demonstrate that transcription of the target locus is essential for RNA-directed formation of heterochromatin. However, high transcriptional activity is inhibitory; thus, a transcriptional window exists that is optimal for silencing. We further found that pre-mRNA splicing is compatible with RNA-directed heterochromatin formation. However, the kinetics of pre-mRNA processing is critical. Introns close to the 5' end of a transcript that are rapidly spliced result in a bistable response whereby the target either remains euchromatic or becomes fully silenced. Together, our results discount siRNA-DNA base pairing in RNA-mediated heterochromatin formation, and the mechanistic insights further reveal guiding paradigms for the design of small RNA-directed chromatin silencing studies in multicellular organisms.","doi":"10.1101/gad.292599.116","authors":"Shimada Y, Mohn F, Bühler M","authors_abbrev":"Shimada Y et al.","pubmed_publication_date":"01 Dec 2016","pubmed_entrez_date":"2016-12-13","publication_year":"2016","canto_session_key":"e3a51e13e6e81a6b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-01-03 16:48:15","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-12-20 06:51:37","canto_added_date":"2016-12-14 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2016-12-20"},{"uniquename":"PMID:16460890","title":"Transcription of the Schizosaccharomyces pombe gene cdc18+: roles of MCB elements and the DSC1 complex.","citation":"Gene 2006 Mar 15;369:100-8","abstract":"In Schizosaccharomyces pombe, commitment to a round of DNA synthesis and entry into the cell cycle are dependent on the function of genes that are transcribed periodically during the cell cycle. Activation of these genes prior to S phase is primarily controlled through cis-acting elements known as MluI Cell-cycle Boxes, or MCBs, and by a family of transcription factors, including Cdc10, Res1, Res2 and Rep2. These transcription factors are also known to be present in a complex, DSC1, that binds to the promoters of pre-S genes. We have demonstrated that within the promoter of cdc18+, a representative pre-S gene, the orientation and spacing of MCBs are crucial for activation and cell-cycle dependence. To our surprise, electrophoretic mobility shift assays showed a highly active mutant form of the promoter, which alters the spacing of the MCB elements, does not bind DSC1 but does bind a higher mobility complex. The binding of this second complex is not dependent on Cdc10 or the Res/Rep proteins. We conclude that, DSC1 binding does not correlate with cell-cycle dependent transcriptional activation, and the higher mobility species may represent a novel transcriptional activation complex that is also likely to function in pre-S transcription.","authors":"Jackson WT, Martin GS","authors_abbrev":"Jackson WT et al.","pubmed_publication_date":"15 Mar 2006","pubmed_entrez_date":"2006-02-08","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22885303","title":"Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity.","citation":"Nucleic Acids Res 2012 Oct;40(19):9815-24","abstract":"Polyuridylation is emerging as a ubiquitous post-translational modification with important roles in multiple aspects of RNA metabolism. These poly (U) tails are added by poly (U) polymerases with homology to poly (A) polymerases; nevertheless, the selection for UTP over ATP remains enigmatic. We report the structures of poly (U) polymerase Cid1 from Schizoscaccharomyces pombe alone and in complex with UTP, CTP, GTP and 3'-dATP. These structures reveal that each of the 4 nt can be accommodated at the active site; however, differences exist that suggest how the polymerase selects UTP over the other nucleotides. Furthermore, we find that Cid1 shares a number of common UTP recognition features with the kinetoplastid terminal uridyltransferases. Kinetic analysis of Cid1's activity for its preferred substrates, UTP and ATP, reveal a clear preference for UTP over ATP. Ultimately, we show that a single histidine in the active site plays a pivotal role for poly (U) activity. Notably, this residue is typically replaced by an asparagine residue in Cid1-family poly (A) polymerases. By mutating this histidine to an asparagine residue in Cid1, we diminished Cid1's activity for UTP addition and improved ATP incorporation, supporting that this residue is important for UTP selectivity.","doi":"10.1093/nar/gks740","authors":"Lunde BM, Magler I, Meinhart A","authors_abbrev":"Lunde BM et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-14","publication_year":"2012","canto_session_key":"044c456b38c1dea5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-03-16 12:13:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-03-16 12:13:37","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-03-16","pdb_entries":[{"pdb_id":"4fh5","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A","position":"33-377"}],"title":"Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity - MgUTP bound","entry_authors":"Lunde BM,Magler I,Meinhart A","entry_authors_abbrev":"Lunde BM et al.","reference_uniquename":"PMID:22885303","experimental_method":"X-ray","resolution":"2.3"},{"pdb_id":"4fhw","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A","position":"33-377"}],"title":"Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity - MgGTP bound","entry_authors":"Lunde BM,Magler I,Meinhart A","entry_authors_abbrev":"Lunde BM et al.","reference_uniquename":"PMID:22885303","experimental_method":"X-ray","resolution":"2.5"},{"pdb_id":"4fhx","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A","position":"33-377"}],"title":"Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity - H336N mutant bound to MgATP","entry_authors":"Lunde BM,Magler I,Meinhart A","entry_authors_abbrev":"Lunde BM et al.","reference_uniquename":"PMID:22885303","experimental_method":"X-ray","resolution":"2.7"},{"pdb_id":"4fhp","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A","position":"33-377"}],"title":"Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity - CaUTP bound","entry_authors":"Lunde BM,Magler I,Meinhart A","entry_authors_abbrev":"Lunde BM et al.","reference_uniquename":"PMID:22885303","experimental_method":"X-ray","resolution":"2.5"},{"pdb_id":"4fh3","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A","position":"33-377"}],"title":"Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity","entry_authors":"Lunde BM,Magler I,Meinhart A","entry_authors_abbrev":"Lunde BM et al.","reference_uniquename":"PMID:22885303","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"4fhv","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A","position":"33-377"}],"title":"Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity - MgCTP bound","entry_authors":"Lunde BM,Magler I,Meinhart A","entry_authors_abbrev":"Lunde BM et al.","reference_uniquename":"PMID:22885303","experimental_method":"X-ray","resolution":"2.1"},{"pdb_id":"4fhy","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A","position":"33-377"}],"title":"Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP selectivity - Mg 3'-dATP bound","entry_authors":"Lunde BM,Magler I,Meinhart A","entry_authors_abbrev":"Lunde BM et al.","reference_uniquename":"PMID:22885303","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:19450504","title":"Growth pattern of single fission yeast cells is bilinear and depends on temperature and DNA synthesis.","citation":"Biophys J 2009 May 20;96(10):4336-47","abstract":"Cell growth and division have to be tightly coordinated to keep the cell size constant over generations. Changes in cell size can be easily studied in the fission yeast Schizosaccharomyces pombe because these cells have a cylindrical shape and grow only at the cell ends. However, the growth pattern of single cells is currently unclear. Linear, exponential, and bilinear growth models have been proposed. Here we measured the length of single fission yeast cells with high spatial precision and temporal resolution over the whole cell cycle by using time-lapse confocal microscopy of cells with green fluorescent protein-labeled plasma membrane. We show that the growth profile between cell separation and the subsequent mitosis is bilinear, consisting of two linear segments separated by a rate-change point (RCP). The change in growth rate occurred at the same relative time during the cell cycle and at the same relative extension for different temperatures. The growth rate before the RCP was independent of temperature, whereas the growth rate after the RCP increased with an increase in temperature, leading to clear bilinear growth profiles at higher temperatures. The RCP was not directly related to the initiation of growth at the new end (new end take-off). When DNA synthesis was inhibited by hydroxyurea, the RCP was not detected. This result suggests that completion of DNA synthesis is required for the increase in growth rate. We conclude that the growth of fission yeast cells is not a simple exponential growth, but a complex process with precise rates regulated by the events during the cell cycle.","doi":"10.1016/j.bpj.2009.02.051","authors":"Baumgärtner S, Tolić-Nørrelykke IM","authors_abbrev":"Baumgärtner S et al.","pubmed_publication_date":"20 May 2009","pubmed_entrez_date":"2009-05-20","publication_year":"2009","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733404","title":"High-Throughput Quantitative Genetic Interaction Mapping in the Fission Yeast  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2018 Feb 01;2018(2)","abstract":"Epistasis mapping, in which the phenotype that emerges from combining pairs of mutations is measured quantitatively, is a powerful tool for unbiased study of gene function. When performed at a large scale, this approach has been used to assign function to previously uncharacterized genes, define functional modules and pathways, and study their cross talk. These experiments rely heavily on methods for rapid sampling of binary combinations of mutant alleles by systematic generation of a series of double mutants. Epistasis mapping technologies now exist in various model systems. Here we provide an overview of different epistasis mapping technologies, including the pombe epistasis mapper (PEM) system designed for the collection of quantitative genetic interaction data in fission yeast  Schizosaccharomyces pombe  Comprising a series of high-throughput selection steps for generation and characterization of double mutants, the PEM system has provided insight into a wide range of biological processes as well as facilitated evolutionary analysis of genetic interactomes across different species.","doi":"10.1101/pdb.top079905","authors":"Roguev A, Ryan CJ, Hartsuiker E, Krogan NJ","authors_abbrev":"Roguev A et al.","pubmed_publication_date":"01 Feb 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20581441","title":"Filling out the gaps is the hardest (yet rewarding) task: the genome-wide collection of the fission yeast deletion mutants is near completion.","citation":"Cell Cycle 2010 Jun 15;9(12):2274","abstract":"","authors":"Tomáska L, Nosek J","authors_abbrev":"Tomáska L et al.","pubmed_publication_date":"15 Jun 2010","pubmed_entrez_date":"2010-06-29","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25724972","title":"Rho4 interaction with exocyst and septins regulates cell separation in fission yeast.","citation":"Microbiology (Reading) 2015 May;161(Pt 5):948-959","abstract":"Rho GTPases are small proteins present in all eukaryotic cells, from yeast to mammals, with a function in actin organization and morphogenetic processes. Schizosaccharomyces pombe Rho4 is not essential but it displays a role during cell separation at high temperature. In fact, Rho4 is involved in the secretion of the hydrolytic enzymes that are required for cell septum degradation during this process. In rho4Δ cells, vesicles accumulate in the septum area and the glucanases Eng1 and Agn1 are not secreted to the culture medium. The localization of Eng1 and Agn1 depends on the exocyst and the septins. The exocyst is a conserved multiprotein complex important for the targeting and fusion of Golgi-derived vesicles with the plasma membrane. Septins are a family of GTP-binding proteins conserved in eukaryotes that function during cytokinesis. Here we show that Rho4 is required for the proper localization of the exocyst and septins at high temperature. Moreover, pull-down experiments demonstrate that Rho4 can interact with exocyst subunits, such as Sec8 and Exo70, and septin proteins, such as Spn3. We observe that Sec8 preferentially binds to activated GTP-Rho4, suggesting that Sec8 could be an effector of this GTPase. We propose that the interaction of Rho4 with the exocyst and septins confers a precise regulation for the secretion of glucanases at the appropriate place and time during the cell cycle.","doi":"10.1099/mic.0.000062","authors":"Pérez P, Portales E, Santos B","authors_abbrev":"Pérez P et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-03-01","publication_year":"2015","canto_session_key":"51b4a124da971b9d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pilar Perez","canto_approved_date":"2018-03-07 16:38:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-14 12:32:34","canto_added_date":"2015-03-02 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":45,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pilar Perez","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.04","SPAC23C4.08","SPCC970.09","SPBC16A3.01","SPBC106.20","SPCC1235.10c","SPAC821.06","SPAC4F10.11","SPAC9G1.11c","SPCC895.05"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-10-14"},{"uniquename":"PMID:12006658","title":"Sum1, a component of the fission yeast eIF3 translation initiation complex, is rapidly relocalized during environmental stress and interacts with components of the 26S proteasome.","citation":"Mol Biol Cell 2002 May;13(5):1626-40","abstract":"Eukaryotic translation initiation factor 3 (eIF3) is a multisubunit complex that plays a central role in translation initiation. We show that fission yeast Sum1, which is structurally related to known eIF3 subunits in other species, is essential for translation initiation, whereas its overexpression results in reduced global translation. Sum1 is associated with the 40S ribosome and interacts stably with Int6, an eIF3 component, in vivo, suggesting that Sum1 is a component of the eIF3 complex. Sum1 is cytoplasmic under normal growth conditions. Surprisingly, Sum1 is rapidly relocalized to cytoplasmic foci after osmotic and thermal stress. Int6 and p116, another putative eIF3 subunit, behave similarly, suggesting that eIF3 is a dynamic complex. These cytoplasmic foci, which additionally comprise eIF4E and RNA components, may function as translation centers during environmental stress. After heat shock, Sum1 additionally colocalizes stably with the 26S proteasome at the nuclear periphery. The relationship between Sum1 and the 26S proteasome was further investigated, and we find cytoplasmic Sum1 localization to be dependent on the 26S proteasome. Furthermore, Sum1 interacts with the Mts2 and Mts4 components of the 26S proteasome. These data indicate a functional link between components of the structurally related eIF3 translation initiation and 26S proteasome complexes.","authors":"Dunand-Sauthier I, Walker C, Wilkinson C, Gordon C, Crane R, Norbury C, Humphrey T","authors_abbrev":"Dunand-Sauthier I et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-05-15","publication_year":"2002","canto_session_key":"207d1283e42dcc66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-02-25 19:06:29","canto_approved_date":"2026-01-29 11:49:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-03 14:29:11","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.13c","SPAC31G5.13","SPAC4D7.05","SPBC4.07c","SPBC646.09c","SPBP19A11.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-02-25"},{"uniquename":"PMID:30456601","title":"Mechanisms of contractile ring tension production and constriction.","citation":"Biophys Rev 2018 Dec;10(6):1667-1681","abstract":"The contractile ring is a remarkable tension-generating cellular machine that constricts and divides cells into two during cytokinesis, the final stage of the cell cycle. Since the ring's discovery, the parallels with muscle have been emphasized. Both are contractile actomyosin machineries, and long ago, a muscle-like sliding filament mechanism was proposed for the ring. This review focuses on the mechanisms that generate ring tension and constrict contractile rings. The emphasis is on fission yeast, whose contractile ring is sufficiently well characterized that realistic mathematical models are feasible, and possible lessons from fission yeast that may apply to animal cells are discussed. Recent discoveries relevant to the organization in fission yeast rings suggest a stochastic steady-state version of the classic sliding filament mechanism for tension. The importance of different modes of anchoring for tension production and for organizational stability of constricting rings is discussed. Possible mechanisms are discussed that set the constriction rate and enable the contractile ring to meet the technical challenge of maintaining structural integrity and tension-generating capacity while continuously disassembling throughout constriction.","doi":"10.1007/s12551-018-0476-6","authors":"O'Shaughnessy B, Thiyagarajan S","authors_abbrev":"O'Shaughnessy B et al.","pubmed_publication_date":"Dec 2018","pubmed_entrez_date":"2018-11-21","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-22 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6327053","title":"Identification of the pleiotropic cell division cycle gene NDA2 as one of two different alpha-tubulin genes in Schizosaccharomyces pombe.","citation":"Cell 1984 May;37(1):233-42","abstract":"Mutations in a cell-cycle gene NDA2 of Schizosaccharomyces pombe have pleiotropic effects on nuclear division, nuclear location, and thiabendazole sensitivity ( Toda et al., 1983). By transformation and nucleotide sequence determination, we identified NDA2 as one of two alpha-tubulin genes present in the genome of S. pombe. Two cloned sequences complemented cold-sensitive and thiabendazole-supersensitive nda2 mutations; one was derived from NDA2 that encodes alpha 1-tubulin, the other from an unidentified locus encoding alpha 2-tubulin. The predicted amino acid sequences showed that the alpha 1- and alpha 2-tubulins had respective residues of 455 and 449 (molecular weights 51,200 and 50,600). The homology to porcine alpha-tubulin was 76% in both cases. Frequent alterations took place in the two restricted regions. The alpha 1-tubulin (NDA2) clone had a 90 bp intervening sequence, the alpha 2-tubulin clone did not. RNA blot hybridization experiments indicated that both genes are transcribed. S. pombe tubulin was isolated by cycles of assembly and disassembly. Presumed alpha- and beta-tubulin polypeptide bands reacted with monoclonal antibodies specific for chicken alpha- and beta-tubulins.","authors":"Toda T, Adachi Y, Hiraoka Y, Yanagida M","authors_abbrev":"Toda T et al.","pubmed_publication_date":"May 1984","pubmed_entrez_date":"1984-05-01","publication_year":"1984","canto_session_key":"99595a23ee62af7e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-14 15:58:37","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-09-30 15:08:26","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPBC26H8.07c","SPBC800.05c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-09-30"},{"uniquename":"PMID:12975364","title":"Substrate requirements for duplex DNA translocation by the eukaryal and archaeal minichromosome maintenance helicases.","citation":"J Biol Chem 2003 Dec 05;278(49):49053-62","abstract":"Replicative DNA helicases are ring-shaped hexamers that play an essential role in DNA synthesis by separating the two strands of chromosomal DNA to provide the single-stranded (ss) substrate for replicative polymerases. Biochemical and structural studies suggest that these helicases translocate along one strand of the duplex, which passes through and interacts with the central channel of these ring-shaped hexamers, and displace the complementary strand. A number of these helicases were shown to also encircle both strands simultaneously and then translocate along double-stranded (ds)DNA. In this report it is shown that the Schizosaccharomyces pombe Mcm4,6,7 complex and archaeal minichromosome maintenance (MCM) helicase from Methanothermobacter thermautotrophicus move along duplex DNA. These two helicases, however, differ in the substrate required to support dsDNA translocation. Although the S. pombe Mcm4,6,7 complex required a 3'-overhang ssDNA region to initiate its association with the duplex, the archaeal protein initiated its transit along dsDNA in the absence of a 3'-overhang region, as well. Furthermore, DNA substrates containing a streptavidin-biotin steric block inhibited the movement of the eukaryotic helicase along ss and dsDNAs but not of the archaeal enzyme. The M. thermautotrophicus MCM helicase, however, was shown to displace a streptavidin-biotin complex from ss, as well as dsDNAs. The possible roles of dsDNA translocation by the MCM proteins during the initiation and elongation phases of chromosomal replication are discussed.","authors":"Shin JH, Jiang Y, Grabowski B, Hurwitz J, Kelman Z","authors_abbrev":"Shin JH et al.","pubmed_publication_date":"05 Dec 2003","pubmed_entrez_date":"2003-09-17","publication_year":"2003","canto_session_key":"fc8629194c1a8b54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-10-27 17:05:09","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-10-27 17:04:04","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC211.04c","SPBC25D12.03c","SPCC16A11.17"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-10-27"},{"uniquename":"PMID:24244195","title":"Fission yeast shelterin regulates DNA polymerases and Rad3(ATR) kinase to limit telomere extension.","citation":"PLoS Genet 2013 Nov;9(11):e1003936","abstract":"Studies in fission yeast have previously identified evolutionarily conserved shelterin and Stn1-Ten1 complexes, and established Rad3(ATR)/Tel1(ATM)-dependent phosphorylation of the shelterin subunit Ccq1 at Thr93 as the critical post-translational modification for telomerase recruitment to telomeres. Furthermore, shelterin subunits Poz1, Rap1 and Taz1 have been identified as negative regulators of Thr93 phosphorylation and telomerase recruitment. However, it remained unclear how telomere maintenance is dynamically regulated during the cell cycle. Thus, we investigated how loss of Poz1, Rap1 and Taz1 affects cell cycle regulation of Ccq1 Thr93 phosphorylation and telomere association of telomerase (Trt1(TERT)), DNA polymerases, Replication Protein A (RPA) complex, Rad3(ATR)-Rad26(ATRIP) checkpoint kinase complex, Tel1(ATM) kinase, shelterin subunits (Tpz1, Ccq1 and Poz1) and Stn1. We further investigated how telomere shortening, caused by trt1Δ or catalytically dead Trt1-D743A, affects cell cycle-regulated telomere association of telomerase and DNA polymerases. These analyses established that fission yeast shelterin maintains telomere length homeostasis by coordinating the differential arrival of leading (Polε) and lagging (Polα) strand DNA polymerases at telomeres to modulate Rad3(ATR) association, Ccq1 Thr93 phosphorylation and telomerase recruitment.","doi":"10.1371/journal.pgen.1003936","authors":"Chang YT, Moser BA, Nakamura TM","authors_abbrev":"Chang YT et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-11-19","publication_year":"2013","canto_session_key":"4790838a75d3b907","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.13c","SPBC1778.02","SPAC16A10.07c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:25487573","title":"Panspecies small-molecule disruptors of heterochromatin-mediated transcriptional gene silencing.","citation":"Mol Cell Biol 2015 Feb;35(4):662-74","abstract":"Heterochromatin underpins gene repression, genome integrity, and chromosome segregation. In the fission yeast Schizosaccharomyces pombe, conserved protein complexes effect heterochromatin formation via RNA interference-mediated recruitment of a histone H3 lysine 9 methyltransferase to cognate chromatin regions. To identify small molecules that inhibit heterochromatin formation, we performed an in vivo screen for loss of silencing of a dominant selectable kanMX reporter gene embedded within fission yeast centromeric heterochromatin. Two structurally unrelated compounds, HMS-I1 and HMS-I2, alleviated kanMX silencing and decreased repressive H3K9 methylation levels at the transgene. The decrease in methylation caused by HMS-I1 and HMS-I2 was observed at all loci regulated by histone methylation, including centromeric repeats, telomeric regions, and the mating-type locus, consistent with inhibition of the histone deacetylases (HDACs) Clr3 and/or Sir2. Chemical-genetic epistasis and expression profiles revealed that both compounds affect the activity of the Clr3-containing Snf2/HDAC repressor complex (SHREC). In vitro HDAC assays revealed that HMS-I1 and HMS-I2 inhibit Clr3 HDAC activity. HMS-I1 also alleviated transgene reporter silencing by heterochromatin in Arabidopsis and a mouse cell line, suggesting a conserved mechanism of action. HMS-I1 and HMS-I2 bear no resemblance to known inhibitors of chromatin-based activities and thus represent novel chemical probes for heterochromatin formation and function.","doi":"10.1128/MCB.01102-14","authors":"Castonguay E, White SA, Kagansky A, St-Cyr DJ, Castillo AG, Brugger C, White R, Bonilla C, Spitzer M, Earnshaw WC, Schalch T, Ekwall K, Tyers M, Allshire RC","authors_abbrev":"Castonguay E et al.","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2014-12-10","publication_year":"2015","canto_session_key":"2643ebdbe6c2a9e2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-12-11 01:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33711009","title":"Structure-function analysis of fission yeast cleavage and polyadenylation factor (CPF) subunit Ppn1 and its interactions with Dis2 and Swd22.","citation":"PLoS Genet 2021 Mar;17(3):e1009452","abstract":"Fission yeast Cleavage and Polyadenylation Factor (CPF), a 13-subunit complex, executes the cotranscriptional 3' processing of RNA polymerase II (Pol2) transcripts that precedes transcription termination. The three-subunit DPS sub-complex of CPF, consisting of a PP1-type phosphoprotein phosphatase Dis2, a WD-repeat protein Swd22, and a putative phosphatase regulatory factor Ppn1, associates with the CPF core to form the holo-CPF assembly. Here we probed the functional, physical, and genetic interactions of DPS by focusing on the Ppn1 subunit, which mediates association of DPS with the core. Transcriptional profiling by RNA-seq defined limited but highly concordant sets of protein-coding genes that were dysregulated in ppn1Δ, swd22Δ and dis2Δ cells, which included the DPSΔ down-regulated phosphate homeostasis genes pho1 and pho84 that are controlled by lncRNA-mediated transcriptional interference. Essential and inessential modules of the 710-aa Ppn1 protein were defined by testing the effects of Ppn1 truncations in multiple genetic backgrounds in which Ppn1 is required for growth. An N-terminal 172-aa disordered region was dispensable and its deletion alleviated hypomorphic phenotypes caused by deleting C-terminal aa 640-710. A TFIIS-like domain (aa 173-330) was not required for viability but was important for Ppn1 activity in phosphate homeostasis. Distinct sites within Ppn1 for binding to Dis2 (spanning Ppn1 aa 506 to 532) and Swd22 (from Ppn1 aa 533 to 578) were demarcated by yeast two-hybrid assays. Dis2 interaction-defective missense mutants of full-length Ppn1 (that retained Swd22 interaction) were employed to show that binding to Dis2 (or its paralog Sds21) was necessary for Ppn1 biological activity. Ppn1 function was severely compromised by missense mutations that selectively affected its binding to Swd22.","doi":"10.1371/journal.pgen.1009452","authors":"Benjamin B, Sanchez AM, Garg A, Schwer B, Shuman S","authors_abbrev":"Benjamin B et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2021-03-12","publication_year":"2021","canto_session_key":"fcfd9a50a6a6cb53","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Bradley Benjamin","canto_first_approved_date":"2022-10-19 08:02:54","canto_approved_date":"2024-11-13 12:09:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-10-04 17:31:11","canto_added_date":"2021-03-14 01:15:06","annotation_curators":[{"name":"Bradley Benjamin","community_curator":true,"annotation_count":131,"orcid":"0000-0002-8732-2330","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.11","SPBC1861.02","SPBC1861.01c","SPCC74.02c","SPAC4C5.04","SPAC9.06c","SPAC3A11.07","SPAC2H10.01","SPAC977.18","SPBC19C7.04c","SPAC23C4.04c","SPBC3B9.11c","SPBC32C12.02","SPBC8E4.01c","SPCC737.04","SPCC794.12c","SPAC31G5.09c","SPAC186.05c","SPBC1709.06","SPBC1709.08","SPCC1672.06c","SPBC8E4.12c","SPAC3G9.04","SPAC664.13","SPCC330.03c","SPCC16C4.03","SPAC16A10.01","SPAC4G8.13c","SPAC6B12.18","SPBPB8B6.06c","SPAPB24D3.07c","SPAC1002.19","SPAC824.04","SPCC31H12.05c","SPBC337.03","SPBC776.02c","SPAC750.05c","SPBPB2B2.18","SPAC750.01","SPAC18B11.03c","SPAC13C5.05c","SPCC622.19","SPAC1F5.07c","SPAC11E3.06","SPBC4F6.12","SPAC18B11.04","SPBP4G3.02","SPCC645.02","SPBC28F2.12","SPBC354.08c","SPBC23E6.03c","SPCC825.05c","SPAC27D7.03c","SPAC29A4.17c","SPAC1B3.04c","SPAC1002.17c"],"gene_count":56,"ltp_gene_count":10,"approved_date":"2022-10-19"},{"uniquename":"PMID:16884933","title":"Identification of Gnr1p, a negative regulator of G alpha signalling in Schizosaccharomyces pombe, and its complementation by human G beta subunits.","citation":"Fungal Genet Biol 2006 Dec;43(12):840-51","abstract":"G protein-coupled receptors (GPCRs) are involved in the response of eukaryotic cells to a wide variety of stimuli, traditionally mediating their effects through heterotrimeric G proteins comprised of G alpha, G beta and G gamma subunits. The fission yeast Schizosaccharomyces pombe is an established tool for GPCR research, possessing two G alpha-dependent signalling cascades. A complete G alpha beta gamma complex has been characterised for the glucose-sensing pathway, but only the G alpha subunit, Gpa1p, has been identified in the pheromone-response pathway. Here, we report the use of the yeast two-hybrid system to identify a novel protein, Gnr1p, which interacts with Gpa1p. Gnr1p is predicted to contain seven WD repeats and to adopt a structure similar to typical G beta subunits. Disruption and overexpression studies reveal that Gnr1p negatively regulates the pheromone-response pathway but is not required for signalling. Human G beta subunits complement the loss of Gnr1p, functioning as negative regulators of G alpha signalling in fission yeast.","authors":"Goddard A, Ladds G, Forfar R, Davey J","authors_abbrev":"Goddard A et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-08-04","publication_year":"2006","canto_session_key":"a0646080ac73a636","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-12 16:44:25","canto_approved_date":"2024-04-24 08:44:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-20 13:24:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["HGNC:25522","SPBC32H8.07","SPBC24C6.06","SPCC1020.09","SPAC343.04c","SPBC215.04"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-07-12"},{"uniquename":"PMID:16478984","title":"The Nse5-Nse6 dimer mediates DNA repair roles of the Smc5-Smc6 complex.","citation":"Mol Cell Biol 2006 Mar;26(5):1617-30","abstract":"Stabilization and processing of stalled replication forks is critical for cell survival and genomic integrity. We characterize a novel DNA repair heterodimer of Nse5 and Nse6, which are nonessential nuclear proteins critical for chromosome segregation in fission yeast. The Nse5/6 dimer facilitates DNA repair as part of the Smc5-Smc6 holocomplex (Smc5/6), the basic architecture of which we define. Nse5-Nse6 [corrected] (Nse5 and Nse6) [corrected] mutants display a high level of spontaneous DNA damage and mitotic catastrophe in the absence of the master checkpoint regulator Rad3 (hATR). Nse5/6 mutants are required for the response to genotoxic agents that block the progression of replication forks, acting in a pathway that allows the tolerance of irreparable UV lesions. Interestingly, the UV sensitivity of Nse5/6 [corrected] is suppressed by concomitant deletion of the homologous recombination repair factor, Rhp51 (Rad51). Further, the viability of Nse5/6 mutants depends on Mus81 and Rqh1, factors that resolve or prevent the formation of Holliday junctions. Consistently, the UV sensitivity of cells lacking Nse5/6 can be partially suppressed by overexpressing the bacterial resolvase RusA. We propose a role for Nse5/6 mutants in suppressing recombination that results in Holliday junction formation or in Holliday junction resolution.","authors":"Pebernard S, Wohlschlegel J, McDonald WH, Yates JR, Boddy MN","authors_abbrev":"Pebernard S et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-02-16","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC11E3.08c","SPBC651.10","SPBC1921.02","SPBC20F10.04c","SPAC644.14c","SPAC16A10.06c","SPCC4G3.05c","SPBC409.03","SPCC645.04","SPBC1734.06","SPBC3E7.08c","SPAC14C4.02c","SPCC550.05","SPCC5E4.06","SPAC2G11.12","SPBC19C7.09c","SPCC1259.13","SPAC3C7.03c"],"gene_count":19,"ltp_gene_count":19},{"uniquename":"PMID:30134042","title":"The INO80 complex activates the transcription of S-phase genes in a cell cycle-regulated manner.","citation":"FEBS J 2018 Oct;285(20):3870-3881","abstract":"Chromatin structure is an essential factor in the proper regulation of DNA repair, DNA replication and transcription. The INO80 complex and the SWR complex have been shown to play a fundamental role in transcription regulation through remodeling chromatin at specific genes and loci. Here, we report that the Schizosaccharomyces pombe INO80 complex physically interacts with the mlui-binding factor (MBF) complex. Furthermore, we are able to detect the INO80 complex in MBF-regulated promoters. Binding of INO80 to these genes is cell cycle regulated, with a maximum binding preceding their transcription and accumulation of their mRNAs. In fact, the INO80 complex is required to fully and timely activate the transcription of these genes. We also show that the accumulation of acetylated H2A.Z at the +1 nucleosome is cell cycle regulated. Cells in which H2A.Z acetylation is abolished still have some cell cycle-regulated transcription of MBF-dependent genes, although to a much lesser extent.","doi":"10.1111/febs.14640","authors":"Knezevic I, González-Medina A, Gaspa L, Hidalgo E, Ayté J","authors_abbrev":"Knezevic I et al.","pubmed_publication_date":"Oct 2018","pubmed_entrez_date":"2018-08-23","publication_year":"2018","canto_session_key":"d905b7844f55c1d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alberto Gonzalez-Medina","canto_first_approved_date":"2018-11-08 17:20:42","canto_approved_date":"2023-01-04 17:33:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-29 16:20:58","canto_added_date":"2018-08-24 00:15:04","annotation_curators":[{"name":"Alberto Gonzalez-Medina","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.11c","SPAC10F6.08c","SPAC29B12.01","SPAC1F7.05","SPBC336.12c","SPAPB1E7.14","SPCC1259.04","SPBP23A10.08","SPBC14C8.07c","SPBC365.10","SPBC11B10.10c","SPBC725.16","SPBC21B10.13c","SPAPB8E5.09","SPAC22F3.09c","SPAC6B12.05c","SPAC664.02c","SPAC23G3.04","SPAC222.04c"],"gene_count":19,"ltp_gene_count":16,"approved_date":"2018-11-08"},{"uniquename":"PMID:9428701","title":"Regulation of salt tolerance in fission yeast by a protein-phosphatase-Z-like Ser/Thr protein phosphatase.","citation":"Eur J Biochem 1997 Dec 01;250(2):476-83","abstract":"In the yeast Saccharomyces cerevisiae, Na+ efflux is mediated by the Ena1 ATPase, and the expression of the ENA1 gene is regulated by the Ppz1 and Ppz2 Ser/Thr protein phosphatases. On the contrary, in the fission yeast Schizosaccharomyces pombe, effective output of Na+ is attributed to the H+/Na+ antiporter encoded by the sod2 gene. We have isolated a S. pombe gene (pzh1) that encodes a 515-amino-acid protein that is 78% identical, from residue 193 to the COOH terminus, to the PPZ1 and PPZ2 gene products. Bacterially expressed Pzh1p shows enzymatic characteristics virtually identical to those of recombinant Ppz1p. When expressed in high-copy number from the PPZ1 promoter, the pzh1 ORF rescues the caffeine-induced lytic defect and slightly decreases the high salt tolerance of S. cerevisiae ppz1delta mutants. Disruption of pzh1 yields viable S. pombe cells and has virtually no effect on tolerance to caffeine or osmotic stress, but it renders the cells highly tolerant to Na+ and Li+, and hypersensitive to K+. Although lack of pzh1 results in a 2-3-fold increase in sod2 mRNA, the pzh1 mutation significantly increases salt tolerance in the absence of the sod2 gene, suggesting that the phosphatase also regulates a Sod2-independent mechanism. Therefore, the finding of a PPZ-like protein phosphatase involved in the regulation of salt tolerance in fission yeast reveals unexpected aspects of cation homeostasis in this organism.","authors":"Balcells L, Gómez N, Casamayor A, Clotet J, Ariño J","authors_abbrev":"Balcells L et al.","pubmed_publication_date":"01 Dec 1997","pubmed_entrez_date":"1998-01-15","publication_year":"1997","canto_session_key":"f23dc3453af59e3b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-11 08:21:28","canto_approved_date":"2020-01-23 13:36:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-28 14:08:34","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.08","SPAC977.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-04-11"},{"uniquename":"EMBL:AU010649","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29323270","title":"Two three-strand intermediates are processed during Rad51-driven DNA strand exchange.","citation":"Nat Struct Mol Biol 2018 Jan;25(1):29-36","abstract":"During homologous recombination, Rad51 forms a nucleoprotein filament with single-stranded DNA (ssDNA) that undergoes strand exchange with homologous double-stranded DNA (dsDNA). Here, we use real-time analysis to show that strand exchange by fission yeast Rad51 proceeds via two distinct three-strand intermediates, C1 and C2. Both intermediates contain Rad51, but whereas the donor duplex remains intact in C1, the ssDNA strand is intertwined with the complementary strand of the donor duplex in C2. Swi5-Sfr1, an evolutionarily conserved recombination activator, facilitates the C1-C2 transition and subsequent ssDNA release from C2 to complete strand exchange in an ATP-hydrolysis-dependent manner. In contrast, Ca 2+ , which activates the Rad51 filament by curbing ATP hydrolysis, facilitates the C1-C2 transition but does not promote strand exchange. These results reveal that Swi5-Sfr1 and Ca 2+  have different activation modes in the late synaptic phase, despite their common function in stabilizing the presynaptic filament.","doi":"10.1038/s41594-017-0002-8","authors":"Ito K, Murayama Y, Takahashi M, Iwasaki H","authors_abbrev":"Ito K et al.","pubmed_publication_date":"Jan 2018","pubmed_entrez_date":"2018-01-12","publication_year":"2018","canto_session_key":"3c9ecc4a8f0eb159","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroshi Iwasaki","canto_first_approved_date":"2020-02-19 15:41:58","canto_approved_date":"2020-02-19 15:41:58","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-02-08 02:45:58","canto_added_date":"2018-01-14 01:15:26","annotation_curators":[{"name":"Hiroshi Iwasaki","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.07","SPAC644.14c","SPBC409.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-02-19"},{"uniquename":"PMID:22955883","title":"Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex.","citation":"Proc Natl Acad Sci U S A 2012 Sep 18;109(38):15241-6","abstract":"Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous assemblies composed of multiple copies of ~30 different proteins called nucleoporins. To unravel the basic scaffold underlying the NPC, we have characterized the species-specific scaffold nucleoporin Nup37 and ELY5/ELYS. Both proteins integrate directly via Nup120/160 into the universally conserved heptameric Y-complex, the critical unit for the assembly and functionality of the NPC. We present the crystal structure of Schizosaccharomyces pombe Nup37 in complex with Nup120, a 174-kDa subassembly that forms one of the two short arms of the Y-complex. Nup37 binds near the bend of the L-shaped Nup120 protein, potentially stabilizing the relative orientation of its two domains. By means of reconstitution assays, we pinpoint residues crucial for this interaction. In vivo and in vitro results show that ELY5 binds near an interface of the Nup120-Nup37 complex. Complementary biochemical and cell biological data refine and consolidate the interactions of Nup120 within the current Y-model. Finally, we propose an orientation of the Y-complex relative to the pore membrane, consistent with the lattice model.","authors":"Bilokapic S, Schwartz TU","authors_abbrev":"Bilokapic S et al.","pubmed_publication_date":"18 Sep 2012","pubmed_entrez_date":"2012-09-08","publication_year":"2012","canto_session_key":"1ccb8cea48bf9230","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-08-29 13:30:36","canto_approved_date":"2023-03-05 14:59:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-17 19:13:02","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.16c","SPAC1486.05","SPBC17G9.04c","SPBC215.15","SPAC15F9.02","SPAC4F10.18","SPBC29A10.06c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2014-08-29","pdb_entries":[{"pdb_id":"4fhn","gene_chains":[{"gene_uniquename":"SPAC4F10.18","chain":"A/C","position":"1-391"},{"gene_uniquename":"SPBC3B9.16c","chain":"B/D","position":"1-1136"}],"title":"Nup37-Nup120 full-length complex from Schizosaccharomyces pombe","entry_authors":"Bilokapic S,Schwartz TU","entry_authors_abbrev":"Bilokapic S et al.","reference_uniquename":"PMID:22955883","experimental_method":"X-ray","resolution":"6.989"},{"pdb_id":"4fhl","gene_chains":[{"gene_uniquename":"SPAC4F10.18","chain":"A","position":"1-391"}],"title":"Nucleoporin Nup37 from Schizosaccharomyces pombe","entry_authors":"Bilokapic S,Schwartz TU","entry_authors_abbrev":"Bilokapic S et al.","reference_uniquename":"PMID:22955883","experimental_method":"X-ray","resolution":"2.6"},{"pdb_id":"4fhm","gene_chains":[{"gene_uniquename":"SPAC4F10.18","chain":"A","position":"1-391"},{"gene_uniquename":"SPBC3B9.16c","chain":"B","position":"1-961"}],"title":"Nup37-Nup120(aa1-961) complex from Schizosaccharomyces pombe","entry_authors":"Bilokapic S,Schwartz TU","entry_authors_abbrev":"Bilokapic S et al.","reference_uniquename":"PMID:22955883","experimental_method":"X-ray","resolution":"4.339"}]},{"uniquename":"PMID:19458260","title":"Schizosacharomyces pombe RNA polymerase II at 3.6-A resolution.","citation":"Proc Natl Acad Sci U S A 2009 Jun 09;106(23):9185-90","abstract":"The second structure of a eukaryotic RNA polymerase II so far determined, that of the enzyme from the fission yeast Schizosaccharomyces pombe, is reported here. Comparison with the previous structure of the enzyme from the budding yeast Saccharomyces cerevisiae reveals differences in regions implicated in start site selection and transcription factor interaction. These aspects of the transcription mechanism differ between S. pombe and S. cerevisiae, but are conserved between S. pombe and humans. Amino acid changes apparently responsible for the structural differences are also conserved between S. pombe and humans, suggesting that the S. pombe structure may be a good surrogate for that of the human enzyme.","doi":"10.1073/pnas.0903361106","authors":"Spåhr H, Calero G, Bushnell DA, Kornberg RD","authors_abbrev":"Spåhr H et al.","pubmed_publication_date":"09 Jun 2009","pubmed_entrez_date":"2009-05-22","publication_year":"2009","canto_session_key":"919c6b46bbf5706f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-09-07 13:38:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-09-07 13:38:13","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPACUNK4.06c","SPBC14C8.12","SPCC1020.04c","SPAPYUG7.04c","SPBC337.14","SPAC23C4.15","SPAC3A12.07","SPBC19C2.03","SPBC28F2.12","SPCC1442.10c","SPAC23G3.01","SPAC1B3.12c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2017-09-07","pdb_entries":[{"pdb_id":"3h0g","gene_chains":[{"gene_uniquename":"SPAC1B3.12c","chain":"J/V","position":"1-71"},{"gene_uniquename":"SPACUNK4.06c","chain":"G/S","position":"1-172"},{"gene_uniquename":"SPAPYUG7.04c","chain":"I/U","position":"1-113"},{"gene_uniquename":"SPBC337.14","chain":"D/P","position":"1-135"},{"gene_uniquename":"SPBC28F2.12","chain":"A/M","position":"1-1752"},{"gene_uniquename":"SPCC1020.04c","chain":"F/R","position":"1-142"},{"gene_uniquename":"SPCC1442.10c","chain":"C/O","position":"1-297"},{"gene_uniquename":"SPBC19C2.03","chain":"L/X","position":"1-63"},{"gene_uniquename":"SPAC3A12.07","chain":"K/W","position":"1-123"},{"gene_uniquename":"SPAC23G3.01","chain":"B/N","position":"1-1210"},{"gene_uniquename":"SPAC23C4.15","chain":"E/Q","position":"1-210"},{"gene_uniquename":"SPBC14C8.12","chain":"H/T","position":"1-125"}],"title":"RNA Polymerase II from Schizosaccharomyces pombe","entry_authors":"Spahr H,Calero G,Bushnell DA,Kornberg RD","entry_authors_abbrev":"Spahr H et al.","reference_uniquename":"PMID:19458260","experimental_method":"X-ray","resolution":"3.65"}]},{"uniquename":"PMID:41161313","title":"Transcription-replication conflict resolution by nuclear RNA interference.","citation":"Mol Cell 2025 Oct 28;","abstract":"Nuclear RNA interference (RNAi) is required for heterochromatin silencing, but Dicer also promotes genome stability by releasing RNA polymerase at sites of replication stress. R-loops are three-stranded DNA:RNA structures that accumulate at transcription-replication (T-R) collisions. We show that in RNase H-deficient cells, which accumulate pathological R-loops, Dcr1 processes R-loops at transcriptional start sites (TSSs) and end sites (TESs), releasing paused RNA polymerase and accounting for small RNAs (sRNAs) resembling DNA-damage-associated sense sRNAs (sdRNAs) found in cancer cells. Genetic evidence implicates nascent transcription-associated R-loops in genome instability in the absence of Dicer, with the helicase domain providing catalytic function reminiscent of related archaeal helicases involved in replication. The RNase H homolog Argonaute (Ago1) promotes genome instability by binding R-loops, and its removal relieves replication stress. Analysis of replication intermediates, DNA and RNA 3' ends, and fork processivity genome wide indicates Dicer resolves head-on T-R collisions, consistent with an ancient origin in DNA replication.","doi":"10.1016/j.molcel.2025.10.003","authors":"Cheng T, Roche B, Abderahmane F, Touat-Todeschini L, Fréon K, Lakhani AA, Bhattacharjee S, Spielmann LG, Jenen E, Choi C, Ren J, Verdel A, Lambert SAE, Martienssen RA","authors_abbrev":"Cheng T et al.","pubmed_publication_date":"28 Oct 2025","pubmed_entrez_date":"2025-10-29","publication_year":"2025","canto_session_key":"78110a420e2fcb26","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-31 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34959732","title":"Echinocandin Drugs Induce Differential Effects in Cytokinesis Progression and Cell Integrity.","citation":"Pharmaceuticals (Basel) 2021 Dec 20;14(12)","abstract":"Fission yeast contains three essential β(1,3)-D-glucan synthases (GSs), Bgs1, Bgs3, and Bgs4, with non-overlapping roles in cell integrity and morphogenesis. Only the  bgs4 +   mutants  pbr1-8  and  pbr1-6  exhibit resistance to GS inhibitors, even in the presence of the wild-type (WT) sequences of  bgs1 +   and  bgs3 +  . Thus, Bgs1 and Bgs3 functions seem to be unaffected by those GS inhibitors. To learn more about echinocandins' mechanism of action and resistance, cytokinesis progression and cell death were examined by time-lapse fluorescence microscopy in WT and  pbr1-8  cells at the start of treatment with sublethal and lethal concentrations of anidulafungin, caspofungin, and micafungin. In WT, sublethal concentrations of the three drugs caused abundant cell death that was either suppressed (anidulafungin and micafungin) or greatly reduced (caspofungin) in  pbr1-8  cells. Interestingly, the lethal concentrations induced differential phenotypes depending on the echinocandin used. Anidulafungin and caspofungin were mostly fungistatic, heavily impairing cytokinesis progression in both WT and  pbr1-8 . As with sublethal concentrations, lethal concentrations of micafungin were primarily fungicidal in WT cells, causing cell lysis without impairing cytokinesis. The lytic phenotype was suppressed again in  pbr1-8  cells. Our results suggest that micafungin always exerts its fungicidal effect by solely inhibiting Bgs4. In contrast, lethal concentrations of anidulafungin and caspofungin cause an early cytokinesis arrest, probably by the combined inhibition of several GSs.","doi":"10.3390/ph14121332","authors":"Yagüe N, Gómez-Delgado L, Curto MÁ, Carvalho VSD, Moreno MB, Pérez P, Ribas JC, Cortés JCG","authors_abbrev":"Yagüe N et al.","pubmed_publication_date":"20 Dec 2021","pubmed_entrez_date":"2021-12-28","publication_year":"2021","canto_session_key":"891bbad03583f932","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juan Carlos García Cortés","canto_first_approved_date":"2022-01-17 21:06:55","canto_approved_date":"2022-01-18 15:58:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-10 09:39:08","canto_added_date":"2021-12-30 01:15:04","annotation_curators":[{"name":"Juan Carlos García Cortés","community_curator":true,"annotation_count":6,"orcid":"0000-0002-2395-6668","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPAC19B12.03","SPCC1840.02c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2022-01-17"},{"uniquename":"PMID:35533728","title":"Analysis of functional surfaces on the actin nucleation promoting factor Dip1 required for Arp2/3 complex activation and endocytic actin network assembly.","citation":"J Biol Chem 2022 Jun;298(6):102019","abstract":"Arp2/3 complex nucleates branched actin filaments that drive processes like endocytosis and lamellipodial protrusion. WISH/DIP/SPIN90 (WDS) proteins form a class of Arp2/3 complex activators or nucleation promoting factors (NPFs) that, unlike WASP family NPFs, activate Arp2/3 complex without requiring preformed actin filaments. Therefore, activation of Arp2/3 complex by WDS proteins is thought to produce the initial actin filaments that seed branching nucleation by WASP-bound Arp2/3 complexes. However, whether activation of Arp2/3 complex by WDS proteins is important for the initiation of branched actin assembly in cells has not been directly tested. Here, we used structure-based point mutations of the Schizosaccharomyces pombe WDS protein Dip1 to test the importance of its Arp2/3-activating activity in cells. Six of thirteen Dip1 mutants caused severe defects in Arp2/3 complex activation in vitro, and we found a strong correlation between the ability of mutants to activate Arp2/3 complex and to rescue endocytic actin assembly defects caused by deleting Dip1. These data support a model in which Dip1 activates Arp2/3 complex to produce actin filaments that initiate branched actin assembly at endocytic sites. Dip1 mutants that synergized with WASP in activating Arp2/3 complex in vitro showed milder defects in cells compared to those that did not, suggesting that in cells the two NPFs may coactivate Arp2/3 complex to initiate actin assembly. Finally, the mutational data reveal important complementary electrostatic contacts at the Dip1-Arp2/3 complex interface and corroborate the previously proposed wedge model, which describes how Dip1 binding triggers structural changes that activate Arp2/3 complex.","doi":"10.1016/j.jbc.2022.102019","authors":"Liu SL, Narvaez-Ortiz HY, Miner M, Kiemel J, Oberhelman N, Watt A, Wagner AR, Luan Q, Helgeson LA, Nolen BJ","authors_abbrev":"Liu SL et al.","pubmed_publication_date":"Jun 2022","pubmed_entrez_date":"2022-05-09","publication_year":"2022","canto_session_key":"f5086f6358dfd36f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-05-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.15c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35101096","title":"The regional sequestration of heterochromatin structural proteins is critical to form and maintain silent chromatin.","citation":"Epigenetics Chromatin 2022 Jan 31;15(1):5","abstract":"Budding yeast Saccharomyces cerevisiae and fission yeast Schizosaccharomyces pombe are good models for heterochromatin study. In S. pombe, H3K9 methylation and Swi6, an ortholog of mammalian HP1, lead to heterochromatin formation. However, S. cerevisiae does not have known epigenetic silencing markers and instead has Sir proteins to regulate silent chromatin formation. Although S. cerevisiae and S. pombe form and maintain heterochromatin via mechanisms that appear to be fundamentally different, they share important common features in the heterochromatin structural proteins. Heterochromatin loci are localized at the nuclear periphery by binding to perinuclear membrane proteins, thereby producing distinct heterochromatin foci, which sequester heterochromatin structural proteins. In this review, we discuss the nuclear peripheral anchoring of heterochromatin foci and its functional relevance to heterochromatin formation and maintenance.","doi":"10.1186/s13072-022-00435-w","authors":"Oh J, Yeom S, Park J, Lee JS","authors_abbrev":"Oh J et al.","pubmed_publication_date":"31 Jan 2022","pubmed_entrez_date":"2022-02-01","publication_year":"2022","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-02-03 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28278249","title":"Expression of C-5 sterol desaturase from an edible mushroom in fisson yeast enhances its ethanol and thermotolerance.","citation":"PLoS One 2017;12(3):e0173381","abstract":"Bioethanol is an environment friendly and renewable source of energy produced by the fermentation of agricultural raw material by a variety of microorganisms including yeast. Obtaining yeast strains that are tolerant to stresses like high levels of ethanol and high temperature is highly desirable as it reduces cost and increases yield during bioethanol production. Here, we report that heterologous expression of C-5 Sterol desaturase (FvC5SD)-an ergosterol biosynthesis enzyme from an edible mushroom Flammulina velutipes in fission yeast, not only imparts increased thermotolerance but also tolerance towards high ethanol concentration and low pH. This tolerance could be attributed to an increase of ≈1.5 fold in the level of ergosterol and oleic acid (C-18 unsaturated fatty acid) as analysed by gas chromatography- mass spectrometry. FvC5SD is a membrane localized iron binding enzyme that introduces double bond at C-5 position into the Δ7-sterol substrates to yield Δ5, 7- sterols as products. In F. velutipes, FvC5SD transcript was observed to be upregulated by ≈5 fold under low pH condition and by ≈ 9 folds and ≈5 fold at 40°C and 4°C respectively when compared to normal growth temperature of 23°C. Besides, susceptibility to cell wall inhibiting drugs like Congo red and Calcoflour white was also found to increase in FvC5SD expressing S. pombe strain. Alteration in membrane sterol and fatty acid composition could also lead to increase in susceptibility to cell wall inhibiting drugs. Thus, this study has immense industrial application and can be employed to ensure competitiveness of fermentation process.","doi":"10.1371/journal.pone.0173381","authors":"Kamthan A, Kamthan M, Datta A","authors_abbrev":"Kamthan A et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-03-10","publication_year":"2017","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2017-03-11 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28807855","title":"Spatial Organization and Molecular Interactions of the Schizosaccharomyces pombe Ccq1-Tpz1-Poz1 Shelterin Complex.","citation":"J Mol Biol 2017 Sep 15;429(19):2863-2872","abstract":"The shelterin complex is a macromolecular assembly of proteins that binds to and protects telomeric DNA, which composes the ends of all linear chromosomes. Shelterin proteins prevent chromosome ends from fusing together and from eliciting erroneous induction of DNA damage response pathways. In addition, shelterin proteins play key roles in regulating the recruitment and activation of telomerase, an enzyme that extends telomeric DNA. In fission yeast, Schizosaccharomyces pombe, interactions between the shelterin proteins Ccq1, Tpz1, and Poz1 are important for regulating telomerase-mediated telomere synthesis and thus telomere length homeostasis. Here, we used electron microscopy combined with genetic labeling to define the three-dimensional arrangement of the S. pombe Ccq1-Tpz1-Poz1 (CTP) complex. Crosslinking mass spectrometry was used to identify individual residues that are in proximity to the protein-protein interfaces of the assembled CTP complex. Together, our data provide a first glimpse into the architectural design of the CTP complex and reveals unique interactions that are important in maintaining the S. pombe telomere in a non-extendible state.","doi":"10.1016/j.jmb.2017.08.002","authors":"Scott H, Kim JK, Yu C, Huang L, Qiao F, Taylor DJ","authors_abbrev":"Scott H et al.","pubmed_publication_date":"15 Sep 2017","pubmed_entrez_date":"2017-08-16","publication_year":"2017","canto_session_key":"3af25b0c9866554b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-08-17 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.13c","SPAC6F6.16c","SPCC188.07"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10637286","title":"Regulation of mitotic inhibitor Mik1 helps to enforce the DNA damage checkpoint.","citation":"Mol Biol Cell 2000 Jan;11(1):1-11","abstract":"The protein kinase Chk1 enforces the DNA damage checkpoint. This checkpoint delays mitosis until damaged DNA is repaired. Chk1 regulates the activity and localization of Cdc25, the tyrosine phosphatase that activates the cdk Cdc2. Here we report that Mik1, a tyrosine kinase that inhibits Cdc2, is positively regulated by the DNA damage checkpoint. Mik1 is required for checkpoint response in strains that lack Cdc25. Long-term DNA damage checkpoint arrest fails in Deltamik1 cells. DNA damage increases Mik1 abundance in a Chk1-dependent manner. Ubiquitinated Mik1 accumulates in a proteasome mutant, which indicates that Mik1 normally has a short half-life. Thus, the DNA damage checkpoint might regulate Mik1 degradation. Mik1 protein and mRNA oscillate during the unperturbed cell cycle, with peak amounts detected around S phase. These data indicate that regulation of Mik1 abundance helps to couple mitotic onset to the completion of DNA replication and repair. Coordinated negative regulation of Cdc25 and positive regulation of Mik1 ensure the effective operation of the DNA damage checkpoint.","authors":"Baber-Furnari BA, Rhind N, Boddy MN, Shanahan P, Lopez-Girona A, Russell P","authors_abbrev":"Baber-Furnari BA et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-19","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPCC18B5.03","SPBC216.05","SPBC337.08c","SPBC660.14","SPBC11B10.09","SPCC1259.13"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:20581291","title":"C terminus of Nce102 determines the structure and function of microdomains in the Saccharomyces cerevisiae plasma membrane.","citation":"Eukaryot Cell 2010 Aug;9(8):1184-92","abstract":"The plasma membrane of the yeast Saccharomyces cerevisiae contains stably distributed lateral domains of specific composition and structure, termed MCC (membrane compartment of arginine permease Can1). Accumulation of Can1 and other specific proton symporters within MCC is known to regulate the turnover of these transporters and is controlled by the presence of another MCC protein, Nce102. We show that in an NCE102 deletion strain the function of Nce102 in directing the specific permeases into MCC can be complemented by overexpression of the NCE102 close homolog FHN1 (the previously uncharacterized YGR131W) as well as by distant Schizosaccharomyces pombe homolog fhn1 (SPBC1685.13). We conclude that this mechanism of plasma membrane organization is conserved through the phylum Ascomycota. We used a hemagglutinin (HA)/Suc2/His4C reporter to determine the membrane topology of Nce102. In contrast to predictions, its N and C termini are oriented toward the cytosol. Deletion of the C terminus or even of its last 6 amino acids does not disturb protein trafficking, but it seriously affects the formation of MCC. We show that the C-terminal part of the Nce102 protein is necessary for localization of both Nce102 itself and Can1 to MCC and also for the formation of furrow-like membrane invaginations, the characteristic ultrastructural feature of MCC domains.","doi":"10.1128/EC.00006-10","authors":"Loibl M, Grossmann G, Stradalova V, Klingl A, Rachel R, Tanner W, Malinsky J, Opekarová M","authors_abbrev":"Loibl M et al.","pubmed_publication_date":"Aug 2010","pubmed_entrez_date":"2010-06-29","publication_year":"2010","canto_session_key":"2a6d7ca7d64c0214","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-11-22 12:56:45","canto_approved_date":"2017-11-22 12:56:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-22 12:56:35","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1685.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-11-22"},{"uniquename":"PMID:30201262","title":"Fission yeast Adf1 is necessary for reassembly of actin filaments into the contractile ring during cytokinesis.","citation":"Biochem Biophys Res Commun 2018 Nov 25;506(2):330-338","abstract":"ADF/cofilin family proteins quickly disassemble actin in vitro, and are thought to be involved in various actin dynamics in the cell. Adf1 is a member of this family proteins expressed in fission yeast, and is thought to play roles in actin patch dynamics and also contractile ring formation during cytokinesis. We aimed to understand the function of this protein in cytokinesis in detail using the temperature-sensitive mutant adf1-1. Adf1 inactivation at a restrictive temperature during late G2 phase led to a clustering of actin patches at the cell ends. It was apparent that the inactivation occurred only in a few minutes. Furthermore, we found that the actin clusters migrated to the division site during anaphase possibly by the function of both myosin 5-1 and a myosin II. The migrated actin clusters, however, were not organized into the contractile ring. When Adf1 was inactivated at mid-anaphase B before contractile ring assembly, the ring was not formed, but it was formed when Adf1 was inactivated after this point. We conclude that Adf1 functions in the interphase actin dynamics and formation of the contractile ring during mitosis.","doi":"10.1016/j.bbrc.2018.07.156","authors":"Ueda EI, Kashiwazaki J, Inoué S, Mabuchi I","authors_abbrev":"Ueda EI et al.","pubmed_publication_date":"25 Nov 2018","pubmed_entrez_date":"2018-09-12","publication_year":"2018","canto_session_key":"ab023f5573fbf770","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun Kashiwazaki","canto_first_approved_date":"2019-12-17 19:32:02","canto_approved_date":"2019-12-17 19:32:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-25 11:18:48","canto_added_date":"2018-09-13 00:15:04","annotation_curators":[{"name":"Jun Kashiwazaki","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC613.04c","SPAC4A8.05c","SPCC1919.10c","SPAC20G4.06c","SPBC2D10.14c","SPBC146.13c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2019-12-17"},{"uniquename":"PB_REF:0000001","title":"Protein modification annotation by manual transfer of experimentally-verified annotation data to orthologs based on curator judgment of sequence features.","abstract":"Method for transferring PSI-MOD protein modification annotations to a protein-coding gene based on a curator's judgment of its similarity to a putative ortholog that has annotations that are supported by experimental evidence. Annotations are created when a curator judges that the protein sequence contains a match to a sequence region or motif that is known to be a consensus site for the modification, and when an ortholog has been identified and experimentally determined to have the modification.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":57,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC4C5.02c","SPAC1834.03c","SPAC16.01","SPAC23C4.08","SPAC1834.04","SPBC354.14c","SPAC607.09c","SPAC56E4.04c","SPAC11E3.13c","SPAC25H1.09","SPCC1223.12c","SPAC26H5.02c","SPAC26H5.08c","SPBC29A10.08","SPBC1105.12","SPAC19G12.16c","SPAC3C7.05c","SPBC336.10c","SPBC8D2.04","SPCC1259.09c","SPBP8B7.24c","SPBC428.16c","SPBC1711.06","SPBC1198.06c","SPBP19A11.01","SPBP8B7.03c","SPCC794.07","SPAC17C9.14","SPAPJ760.03c","SPCC1742.01","SPAC1F7.04","SPBC8D2.03c","SPAPB18E9.04c","SPAC110.03","SPBC776.15c","SPAC1002.13c","SPBC1289.15","SPBC11C11.05","SPBC1105.11c","SPAC343.06c","SPBC1921.02","SPBC17G9.11c","SPAC17C9.13c","SPAC16A10.04","SPAC17H9.09c"],"gene_count":45,"ltp_gene_count":0},{"uniquename":"PMID:7663020","title":"Isolation of protein glycosylation mutants in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1995 May;6(5):485-96","abstract":"We have isolated mutants in the fission yeast Schizosaccharomyces pombe that are defective in protein glycosylation. A collection of osmotically sensitive mutants was prepared and screened for glycosylation defects using lectin staining as an assay. Mutants singly defective in four glycoprotein synthesis genes (gps1-4) were isolated, all of which bind less galactose-specific lectin. Acid phosphatase and other glycoproteins from the gps mutants have increased electrophoretic mobility, suggesting that these mutants make glycans of reduced size. N-linked glycan analysis revealed that terminal oligosaccharide modification is defective in the gps1 and gps2 mutants. Both mutants synthesize the Man9GlcNAc2 core glycan but have reduced amounts of larger structures. Modified core glycans from gps1 cells have normal amounts of galactose (Gal) residues, but reduced amounts of Man, consistent with a defect in a Golgi mannosyltransferase in this mutant. In contrast, N-linked oligosaccharides from gps2 mutants have much less Gal than wild type, because of reduced levels of the Gal donor, UDP-Gal. This reduction is caused by decreased activity of UDP-glucose 4-epimerase, which synthesizes UDP-Gal. Neither the gps1 or gps2 mutations are lethal, although the cells grow at reduced rates. These findings suggest that S. pombe cells can survive with incompletely glycosylated cell wall glycoproteins. In particular, these results suggest that Gal, which comprises approximately 30% by weight of cell wall glycoprotein glycans, is not crucial for cell growth or survival.","authors":"Huang KM, Snider MD","authors_abbrev":"Huang KM et al.","pubmed_publication_date":"May 1995","pubmed_entrez_date":"1995-05-01","publication_year":"1995","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24177581","title":"A revised chromosome map of the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1984 Feb;8(2):85-92","abstract":"The genetic map of the nuclear genome of the fission yeast Schizosaccharomyces pombe has been extended by mitotic and meiotic mapping data. A total of 158 markers are now assigned to the three linkage groups known in this organism, and 118 of them have been located on the corresponding chromosome map. Chromosome II and III each consist of one linkage group. There is some indication that the two large fragments which define chromosome I are meiotically linked, but the linkage observed is significant at the P = 0.05 level only. The length of the map is at least 1,700 map units, corresponding to an average of about 8 kilobases per map unit. The latter figure is comparable to the one obtained for intragenic recombination in the sup3 gene (Hofer et al. 1979). The basic frequency of gene conversion as measured for 21 genes varies according to a distribution of Poisson (with a modal value of 0.6% conversion per meiosis and per gene), in sharp contrast with Saccharomyces cerevisiae (Fogel et al. 1980) and Ascobolus immersus (Nicolas 1979). This may reflect the rarity of gene or region-specific rec alleles in S. pombe and may be related to the homothallism of this organism.","doi":"10.1007/BF00420223","authors":"Gygax A, Thuriaux P","authors_abbrev":"Gygax A et al.","pubmed_publication_date":"Feb 1984","pubmed_entrez_date":"2013-11-02","publication_year":"1984","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20123972","title":"Role of septins in the orientation of forespore membrane extension during sporulation in fission yeast.","citation":"Mol Cell Biol 2010 Apr;30(8):2057-74","abstract":"During yeast sporulation, a forespore membrane (FSM) initiates at each spindle-pole body and extends to form the spore envelope. We used Schizosaccharomyces pombe to investigate the role of septins during this process. During the prior conjugation of haploid cells, the four vegetatively expressed septins (Spn1, Spn2, Spn3, and Spn4) coassemble at the fusion site and are necessary for its normal morphogenesis. Sporulation involves a different set of four septins (Spn2, Spn5, Spn6, and the atypical Spn7) that does not include the core subunits of the vegetative septin complex. The four sporulation septins form a complex in vitro and colocalize interdependently to a ring-shaped structure along each FSM, and septin mutations result in disoriented FSM extension. The septins and the leading-edge proteins appear to function in parallel to orient FSM extension. Spn2 and Spn7 bind to phosphatidylinositol 4-phosphate [PtdIns(4)P] in vitro, and PtdIns(4)P is enriched in the FSMs, suggesting that septins bind to the FSMs via this lipid. Cells expressing a mutant Spn2 protein unable to bind PtdIns(4)P still form extended septin structures, but these structures fail to associate with the FSMs, which are frequently disoriented. Thus, septins appear to form a scaffold that helps to guide the oriented extension of the FSM.","doi":"10.1128/MCB.01529-09","authors":"Onishi M, Koga T, Hirata A, Nakamura T, Asakawa H, Shimoda C, Bähler J, Wu JQ, Takegawa K, Tachikawa H, Pringle JR, Fukui Y","authors_abbrev":"Onishi M et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-02-04","publication_year":"2010","canto_session_key":"f831b1df28d18c1a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masayuki Onishi","canto_first_approved_date":"2018-11-30 15:43:48","canto_approved_date":"2021-06-18 15:57:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-11-19 23:03:16","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Masayuki Onishi","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":67,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC825.03c","SPBC16A3.01","SPAC24C9.15c","SPAC9G1.11c","SPAC607.10","SPCC188.12","SPAC22E12.16c","SPBC1347.03","SPAC4F10.11","SPAC821.06","SPBC19F8.01c"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2018-11-30"},{"uniquename":"PMID:22243696","title":"Different means, same end-heterochromatin formation by RNAi and RNAi-independent RNA processing factors in fission yeast.","citation":"Curr Opin Genet Dev 2012 Apr;22(2):156-63","abstract":"The assembly of heterochromatin in eukaryotic genomes is critical for diverse chromosomal events including regulation of gene expression, silencing of repetitive DNA elements, proper segregation of chromosomes and maintenance of genomic integrity. Previous studies have shown that noncoding RNAs and the RNA interference (RNAi) machinery promote the assembly of heterochromatin that serves as a multipurpose platform for targeting effectors involved in various chromosomal processes. Recent work has revealed that RNAi-independent mechanisms, involving RNA processing activities that utilize both noncoding and coding RNAs, operate in the assembly of heterochromatin. These findings have established that, in addition to coding for proteins, mRNAs also function as signaling molecules that modify chromatin structure by targeting heterochromatin assembly factors.","doi":"10.1016/j.gde.2011.12.004","authors":"Reyes-Turcu FE, Grewal SI","authors_abbrev":"Reyes-Turcu FE et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-01-17","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36059259","title":"Rap1 prevents fusions between long telomeres in fission yeast.","citation":"EMBO J 2022 Oct 17;41(20):e110458","abstract":"The conserved Rap1 protein is part of the shelterin complex that plays critical roles in chromosome end protection and telomere length regulation. Previous studies have addressed how fission yeast Rap1 contributes to telomere length maintenance, but the mechanism by which the protein inhibits end fusions has remained elusive. Here, we use a mutagenesis screen in combination with high-throughput sequencing to identify several amino acid positions in Rap1 that have key roles in end protection. Interestingly, mutations at these sites render cells susceptible to genome instability in a conditional manner, whereby longer telomeres are prone to undergoing end fusions, while telomeres within the normal length range are sufficiently protected. The protection of long telomeres is in part dependent on their nuclear envelope attachment mediated by the Rap1-Bqt4 interaction. Our data demonstrate that long telomeres represent a challenge for the maintenance of genome integrity, thereby providing an explanation for species-specific upper limits on telomere length.","doi":"10.15252/embj.2021110458","authors":"Pan L, Tormey D, Bobon N, Baumann P","authors_abbrev":"Pan L et al.","pubmed_publication_date":"17 Oct 2022","pubmed_entrez_date":"2022-09-05","publication_year":"2022","canto_session_key":"a570b00532e4269b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-08 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1778.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:4834646","title":"On the nature of the forces involved in the sex-directed flocculation of a fission yeast.","citation":"Can J Microbiol 1974 Jun;20(6):797-803","abstract":"","authors":"Calleja GB","authors_abbrev":"Calleja GB","pubmed_publication_date":"Jun 1974","pubmed_entrez_date":"1974-06-01","publication_year":"1974","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31189902","title":"Using genetics to understand biology.","citation":"Heredity (Edinb) 2019 Jul;123(1):4-13","abstract":"","doi":"10.1038/s41437-019-0209-z","authors":"Nurse P, Hayles J","authors_abbrev":"Nurse P et al.","pubmed_publication_date":"Jul 2019","pubmed_entrez_date":"2019-06-14","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-05-31 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35099006","title":"Fission yeast polycystin Pkd2p promotes cell size expansion and antagonizes the Hippo-related SIN pathway.","citation":"J Cell Sci 2022 Feb 15;135(4)","abstract":"Polycystins are conserved mechanosensitive channels whose mutations lead to the common human renal disorder autosomal dominant polycystic kidney disease (ADPKD). Previously, we discovered that the plasma membrane-localized fission yeast polycystin homolog Pkd2p is an essential protein required for cytokinesis; however, its role remains unclear. Here, we isolated a novel temperature-sensitive pkd2 mutant, pkd2-B42. Among the strong growth defects of this mutant, the most striking was that many mutant cells often lost a significant portion of their volume in just 5 min followed by a gradual recovery, a process that we termed 'deflation'. Unlike cell lysis, deflation did not result in plasma membrane rupture and occurred independently of cell cycle progression. The tip extension of pkd2-B42 cells was 80% slower than that of wild-type cells, and their turgor pressure was 50% lower. Both pkd2-B42 and the hypomorphic depletion mutant pkd2-81KD partially rescued mutants of the septation initiation network (SIN), a yeast Hippo-related signaling pathway, by preventing cell lysis, enhancing septum formation and doubling the number of Sid2p and Mob1p molecules at the spindle pole bodies. We conclude that Pkd2p promotes cell size expansion during interphase by regulating turgor pressure and antagonizes the SIN during cytokinesis. This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.259046","authors":"Sinha D, Ivan D, Gibbs E, Chetluru M, Goss J, Chen Q","authors_abbrev":"Sinha D et al.","pubmed_publication_date":"15 Feb 2022","pubmed_entrez_date":"2022-01-31","publication_year":"2022","canto_session_key":"a6e8deacb9e3b2bd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Qian Chen","canto_first_approved_date":"2022-04-15 10:45:39","canto_approved_date":"2024-03-28 18:21:25","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2022-04-12 19:27:33","canto_added_date":"2022-02-02 01:15:05","annotation_curators":[{"name":"Qian Chen","community_curator":true,"annotation_count":16,"orcid":"0000-0002-2768-6570","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.03","SPBC21.06c","SPAC6F6.08c","SPBC428.13c","SPAC24B11.11c","SPAC821.12","SPCC1739.11c","SPAC6G10.12c","SPBC24C6.07","SPAC1565.06c","SPBP19A11.04c","SPBC244.01c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2022-04-15"},{"uniquename":"PMID:28552615","title":"SUMO-Targeted DNA Translocase Rrp2 Protects the Genome from Top2-Induced DNA Damage.","citation":"Mol Cell 2017 Jun 01;66(5):581-596.e6","abstract":"The action of DNA topoisomerase II (Top2) creates transient DNA breaks that are normally concealed inside Top2-DNA covalent complexes. Top2 poisons, including ubiquitously present natural compounds and clinically used anti-cancer drugs, trap Top2-DNA complexes. Here, we show that cells actively prevent Top2 degradation to avoid the exposure of concealed DNA breaks. A genome-wide screen revealed that fission yeast cells lacking Rrp2, an Snf2-family DNA translocase, are strongly sensitive to Top2 poisons. Loss of Rrp2 enhances SUMOylation-dependent ubiquitination and degradation of Top2, which in turn increases DNA damage at sites where Top2-DNA complexes are trapped. Rrp2 possesses SUMO-binding ability and prevents excessive Top2 degradation by competing against the SUMO-targeted ubiquitin ligase (STUbL) for SUMO chain binding and by displacing SUMOylated Top2 from DNA. The budding yeast homolog of Rrp2, Uls1, plays a similar role, indicating that this genome protection mechanism is widely employed, a finding with implications for cancer treatment.","doi":"10.1016/j.molcel.2017.04.017","authors":"Wei Y, Diao LX, Lu S, Wang HT, Suo F, Dong MQ, Du LL","authors_abbrev":"Wei Y et al.","pubmed_publication_date":"01 Jun 2017","pubmed_entrez_date":"2017-05-30","publication_year":"2017","canto_session_key":"205df3a82b504d79","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yi Wei","canto_first_approved_date":"2017-09-28 16:49:35","canto_approved_date":"2025-07-09 18:42:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-24 13:25:44","canto_added_date":"2017-05-31 00:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":87,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yi Wei","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.21c","SPBC119.02","SPAC1565.08","SPBC19G7.09","SPAC4C5.04","SPBC365.06","SPBC3D6.11c","SPAC1556.01c","SPAC1805.04","SPCC338.08","SPAC1687.05","SPAC13C5.07","SPAC30D11.13","SPBC16H5.03c","SPBC1A4.03c","SPAC343.18","SPBC23E6.02","SPAC19A8.10","SPAC17A2.12"],"gene_count":19,"ltp_gene_count":19,"approved_date":"2017-09-28"},{"uniquename":"PMID:33622106","title":"A visual atlas of meiotic protein dynamics in living fission yeast.","citation":"Open Biol 2021 Feb;11(2):200357","abstract":"Meiosis is a carefully choreographed dynamic process that re-purposes proteins from somatic/vegetative cell division, as well as meiosis-specific factors, to carry out the differentiation and recombination pathway common to sexually reproducing eukaryotes. Studies of individual proteins from a variety of different experimental protocols can make it difficult to compare details between them. Using a consistent protocol in otherwise wild-type fission yeast cells, this report provides an atlas of dynamic protein behaviour of representative proteins at different stages during normal zygotic meiosis in fission yeast. This establishes common landmarks to facilitate comparison of different proteins and shows that initiation of S phase likely occurs prior to nuclear fusion/karyogamy.","doi":"10.1098/rsob.200357","authors":"Escorcia W, Tripathi VP, Yuan JP, Forsburg SL","authors_abbrev":"Escorcia W et al.","pubmed_publication_date":"Feb 2021","pubmed_entrez_date":"2021-02-24","publication_year":"2021","canto_session_key":"3167349c4008d5ad","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-02-26 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38440330","title":"DNA sequences and distinct mechanisms for  ura4-595  and  ura4-294  alleles of  S. pombe .","citation":"MicroPubl Biol 2024;2024","abstract":"The  ura4  gene of the fission yeast  Schizosaccharomyces pombe  supports both positive and negative selection; consequently, this gene is widely employed as a powerful tool to study diverse biological processes. Here we report the DNA sequences of two functionally null alleles,  ura4-595  and  ura4-294  . The  ura4-595  allele has a four bp duplication of bp +63 to +66 (5'-CAAG-3') within the ORF and the  ura4-294  allele has a nonsynonymous substitution (G to A) at bp +679. We infer that these alleles arose, respectively, by DNA polymerase template slipping and by nucleotide misincorporation (likely via cytosine deamination).","doi":"10.17912/micropub.biology.001139","authors":"Protacio RU, Malone EG, Wahls WP","authors_abbrev":"Protacio RU et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-03-05","publication_year":"2024","canto_session_key":"affa9fa9c2cfeba0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Reine Protacio","canto_first_approved_date":"2024-03-21 17:37:17","canto_approved_date":"2024-03-21 17:37:18","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-13 14:43:53","canto_added_date":"2024-03-06 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Reine Protacio","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-03-21"},{"uniquename":"PMID:12020831","title":"Characterization and regulation of a second gene encoding thioredoxin from the fission yeast.","citation":"Biochim Biophys Acta 2002 May 03;1575(1-3):143-7","abstract":"A genomic DNA encoding a second thioredoxin (TRX2) was isolated from the chromosomal DNA of the fission yeast Schizosaccharomyces pombe. The cloned sequence contains 1823 bp and encodes a protein of 121 amino acids. It has extra N-terminal 17 amino acid residues compared to previously identified thioredoxin (TRX1), which are positively charged and hydrophobic amino acids. The additional N-terminal region contains a plausible prepeptidase cleavage site, indicating that the TRX2 protein exists in mitochondria. The cloned TRX2 gene produced functional TRX estimated with insulin reduction assay. The upstream region of the TRX2 gene was fused into the promoterless beta-galactosidase gene of the shuttle vector YEp357R. The 782 bp sequence in the region further upstream of the TRX2 gene was found to be inhibitory in its expression. Synthesis of beta-galactosidase from the fusion plasmid pYFX135-HRL was enhanced by the addition of aluminum chloride and ferrous chloride, indicating that the TRX2 protein is involved in stress response.","authors":"Lee YJ, Cho YW, Kim D, Park EH, Fuchs JA, Lim CJ","authors_abbrev":"Lee YJ et al.","pubmed_publication_date":"03 May 2002","pubmed_entrez_date":"2002-05-22","publication_year":"2002","canto_session_key":"80a097bd49504865","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:54:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 14:48:47","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.07c","SPAC7D4.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-05"},{"uniquename":"PMID:19888300","title":"Coffin-Lowry syndrome.","citation":"Eur J Hum Genet 2010 Jun;18(6):627-33","abstract":"Coffin-Lowry syndrome (CLS) is a syndromic form of X-linked mental retardation, which is characterized in male patients by psychomotor and growth retardation and various skeletal anomalies. Typical facial changes and specific clinical and radiological signs in the hand are useful aids in the diagnosis. CLS is caused by mutations in the RPS6KA3 gene located at Xp22.2, which encodes RSK2, a growth-factor-regulated protein kinase. RPS6KA3 mutations are extremely heterogeneous and lead to loss of phosphotransferase activity in the RSK2 kinase, most often because of premature termination of translation.","doi":"10.1038/ejhg.2009.189","authors":"Pereira PM, Schneider A, Pannetier S, Heron D, Hanauer A","authors_abbrev":"Pereira PM et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2009-11-06","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4G3.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR23099","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19G7.04","YGR196C"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18003976","title":"Multiple pathways differentially regulate global oxidative stress responses in fission yeast.","citation":"Mol Biol Cell 2008 Jan;19(1):308-17","abstract":"Cellular protection against oxidative damage is relevant to ageing and numerous diseases. We analyzed the diversity of genome-wide gene expression programs and their regulation in response to various types and doses of oxidants in Schizosaccharomyces pombe. A small core gene set, regulated by the AP-1-like factor Pap1p and the two-component regulator Prr1p, was universally induced irrespective of oxidant and dose. Strong oxidative stresses led to a much larger transcriptional response. The mitogen-activated protein kinase (MAPK) Sty1p and the bZIP factor Atf1p were critical for the response to hydrogen peroxide. A newly identified zinc-finger protein, Hsr1p, is uniquely regulated by all three major regulatory systems (Sty1p-Atf1p, Pap1p, and Prr1p) and in turn globally supports gene expression in response to hydrogen peroxide. Although the overall transcriptional responses to hydrogen peroxide and t-butylhydroperoxide were similar, to our surprise, Sty1p and Atf1p were less critical for the response to the latter. Instead, another MAPK, Pmk1p, was involved in surviving this stress, although Pmk1p played only a minor role in regulating the transcriptional response. These data reveal a considerable plasticity and differential control of regulatory pathways in distinct oxidative stress conditions, providing both specificity and backup for protection from oxidative damage.","authors":"Chen D, Wilkinson CR, Watt S, Penkett CJ, Toone WM, Jones N, Bähler J","authors_abbrev":"Chen D et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-11-16","publication_year":"2008","canto_session_key":"03d5a66915219549","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-12-09 10:51:57","canto_approved_date":"2022-06-01 15:28:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-13 18:23:57","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPAC3H1.11","SPBC119.08","SPAC8C9.14","SPAC1783.07c","SPBC29B5.01"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-12-09"},{"uniquename":"PMID:19232358","title":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN.","citation":"J Mol Biol 2009 Apr 10;387(4):935-48","abstract":"The N-terminal oligonucleotide/oligosaccharide-binding fold domain of the Schizosaccharomyces pombe protection of telomeres 1 (Pot1) protein, Pot1pN (residues 1-187 of full-length Pot1), specifically recognizes telomeric single-stranded DNA (ssDNA) via a complex series of molecular interactions that are punctuated by unusual internucleotide hydrogen bonds. While the structure of ssDNA-bound Pot1pN provides an initial model for understanding how the Pot1pN-ssDNA complex is assembled and how specific nucleotide recognition occurs, further refinement requires knowledge of the ssDNA-free state of Pot1pN and the dynamic changes that accompany the binding of ssDNA. Using NMR strategies, we found that ssDNA-free Pot1pN adopts a similar overall protein backbone topology as ssDNA-bound Pot1pN does. Although the backbone structure remained relatively unchanged, we observed unexpected differential dynamic changes within the ssDNA-binding pockets of Pot1pN upon binding of cognate ssDNA. These studies support a model in which conformational selection and induced fit play important roles in the recognition of ssDNA by Pot1pN. Furthermore, the studies presented here provide a more comprehensive understanding of how specific nucleotide recognition is achieved by the telomere-end protection family of essential proteins.","doi":"10.1016/j.jmb.2009.02.016","authors":"Croy JE, Wuttke DS","authors_abbrev":"Croy JE et al.","pubmed_publication_date":"10 Apr 2009","pubmed_entrez_date":"2009-02-24","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17339332","title":"Rct1, a nuclear RNA recognition motif-containing cyclophilin, regulates phosphorylation of the RNA polymerase II C-terminal domain.","citation":"Mol Cell Biol 2007 May;27(10):3601-11","abstract":"Phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (RNAP II) is a dynamic process that regulates transcription and coordinates it with pre-mRNA processing. We show here that Rct1, a nuclear multidomain cyclophilin from Schizosaccharomyces pombe, is encoded by an essential gene that interacts with the CTD and regulates its phosphorylation in vivo. Downregulation of Rct1 levels results in increased phosphorylation of the CTD at both Ser2 and Ser5 and in a commensurate decrease in RNAP II transcription. In contrast, overexpression of Rct1 decreases phosphorylation on both sites. The close association of Rct1 with transcriptionally active chromatin suggests a role in regulation of RNAP II transcriptional activity. These data, together with the pleiotropic phenotype upon Rct1 deregulation, suggest that this multidomain cyclophilin is an important player in maintaining the correct phosphorylation code of the CTD and thereby regulating CTD function.","authors":"Gullerova M, Barta A, Lorkovic ZJ","authors_abbrev":"Gullerova M et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-03-07","publication_year":"2007","canto_session_key":"789cb7143f17138e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-18 16:19:47","canto_approved_date":"2022-01-18 13:35:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-18 16:19:40","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17G9.05","SPBC28F2.12"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2016-02-18"},{"uniquename":"PMID:20659020","title":"3' Uridylation and the regulation of RNA function in the cytoplasm.","citation":"Biochem Soc Trans 2010 Aug;38(4):1150-3","abstract":"Degradation of cytoplasmic mRNAs is an important aspect of the regulation of gene function in eukaryotes. Much of what is currently known about the underlying pathways of mRNA decay is derived from studies of the budding yeast Saccharomyces cerevisiae, in which mRNA turnover is initiated by deadenylation, followed either by decapping and 5'-->3' degradation or by further 3'-->5' exonucleolysis. Our studies using RNA cRACE (circularization-based rapid amplification of cDNA ends) techniques indicate that mRNA decapping in the fission yeast Schizosaccharomyces pombe often does not require prior deadenylation. Furthermore, the poly(A) polymerase-related, cytoplasmic enzyme Cid1 catalyses uridylation of a variety of functionally diverse poly(A)(+) mRNAs and hence stimulates decapping as part of a novel mRNA turnover pathway. The pathways initiated by uridylation and deadenylation stimulate decapping in a partially redundant fashion, but urg1 mRNA is stabilized in mutants lacking cid1. Accumulation of uridylated RNAs in an lsm1 mutant suggests an involvement of the Lsm1-7 complex in recognition of the 3' uridylation tag and recruitment of the decapping machinery. Recent reports from other groups suggest that in metazoans, which unlike budding yeast contain Cid1 orthologues, 3' uridylation by such enzymes is used to regulate miRNA (microRNA) and siRNA (small interfering RNA) biogenesis and activity. It has further been suggested that uridylation is an important regulatory modification of non-polyadenylated replication-dependent histone mRNAs. This modification may also form the basis of a widespread mechanism for the initiation of the decay of polyadenylated mRNAs in organisms other than fission yeast.","doi":"10.1042/BST0381150","authors":"Norbury CJ","authors_abbrev":"Norbury CJ","pubmed_publication_date":"Aug 2010","pubmed_entrez_date":"2010-07-28","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007332","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1878997","title":"Synchronized meiosis and recombination in fission yeast: observations with pat1-114 diploid cells.","citation":"Curr Genet 1991 Jun;19(6):445-51","abstract":"The mutation pat1-114 has been used to synchronize meiosis in the fission yeast Schizosaccharomyces pombe. We have investigated several aspects of such synchronized meiotic cultures. In both pat1-114 and pat1+ diploids, meiotic landmark events are initiated at the same time after meiosis induction, but synchrony is much more pronounced in the pat1-114-driven meiosis. Commitment to recombination and to meiosis have been timed at 2 h after meiotic induction. Due to a seven-fold reduction of intragenic recombination frequency in the ade6 region of pat1-114 diploids, physical analysis of recombination has not been possible. We have distinguished three factors that influence intragenic recombination frequencies: temperature, azygotic versus zygotic meiosis, and the nature of the pat1 allele. Differences and similarities in the timing of meiotic landmarks in S. cerevisiae and S. pombe are discussed.","authors":"Bähler J, Schuchert P, Grimm C, Kohli J","authors_abbrev":"Bähler J et al.","pubmed_publication_date":"Jun 1991","pubmed_entrez_date":"1991-06-01","publication_year":"1991","canto_session_key":"f979341c5c3cd4a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-06 09:07:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-06 09:07:44","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13","SPBC19C2.05"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-08-06"},{"uniquename":"PMID:26221037","title":"Pli1(PIAS1) SUMO ligase protected by the nuclear pore-associated SUMO protease Ulp1SENP1/2.","citation":"J Biol Chem 2015 Sep 11;290(37):22678-85","abstract":"Covalent modification of the proteome by SUMO is critical for genetic stability and cell growth. Equally crucial to these processes is the removal of SUMO from its targets by the Ulp1 (HuSENP1/2) family of SUMO proteases. Ulp1 activity is normally spatially restricted, because it is localized to the nuclear periphery via interactions with the nuclear pore. Delocalization of Ulp1 causes DNA damage and cell cycle defects, phenotypes thought to be caused by inappropriate desumoylation of nucleoplasmic targets that are normally spatially protected from Ulp1. Here, we define a novel consequence of Ulp1 deregulation, with a major impact on SUMO pathway function. In fission yeast lacking Nup132 (Sc/HuNUP133), Ulp1 is delocalized and can no longer antagonize sumoylation of the PIAS family SUMO E3 ligase, Pli1. Consequently, SUMO chain-modified Pli1 is targeted for proteasomal degradation by the concerted action of a SUMO-targeted ubiquitin ligase (STUbL) and Cdc48-Ufd1-Npl4. Pli1 degradation causes the profound SUMO pathway defects and associated centromere dysfunction in cells lacking Nup132. Thus, perhaps counterintuitively, Ulp1-mediated desumoylation can promote SUMO modification by stabilizing a SUMO E3 ligase.","doi":"10.1074/jbc.M115.673038","authors":"Nie M, Boddy MN","authors_abbrev":"Nie M et al.","pubmed_publication_date":"11 Sep 2015","pubmed_entrez_date":"2015-07-30","publication_year":"2015","canto_session_key":"b3c499fa6bc66af4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Michael Boddy","canto_first_approved_date":"2016-08-30 14:31:14","canto_approved_date":"2026-01-31 14:07:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-27 19:49:56","canto_added_date":"2015-07-31 00:19:13","annotation_curators":[{"name":"Michael Boddy","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":85,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.11c","SPBC16G5.01","SPBC16A3.09c","SPBC19G7.09","SPAC1687.05","SPAC17A5.07c","SPBC365.06","SPAC1805.04"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-08-30"},{"uniquename":"PMID:10867235","title":"Positioning of medial actin rings affected by eccentrically located nuclei in a fission yeast mutant having large vacuoles.","citation":"FEMS Microbiol Lett 2000 Jul 01;188(1):63-7","abstract":"In Schizosaccharomyces pombe wild-type cells, the nucleus positions in the middle of the cell where the cortical actin ring is assembled prior to septum formation. ste12 mutants contain a few large vacuoles. In a considerable fraction of ste12 cells, the nuclei and septa were eccentrically positioned. Both extension of spindle microtubules in the anaphase and post-mitotic migration of sister nuclei to the cell poles were partially disrupted, probably due to enlarged vacuoles. In spite of the eccentric positioning of nuclei, the cortical actin ring overlays the displaced pre-mitotic nucleus. This observation supports the notion that the nucleus dictates the division site in fission yeast.","authors":"Morishita M, Shimoda C","authors_abbrev":"Morishita M et al.","pubmed_publication_date":"01 Jul 2000","pubmed_entrez_date":"2000-06-27","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9321395","title":"Multiple modes of activation of the stress-responsive MAP kinase pathway in fission yeast.","citation":"EMBO J 1997 Oct 15;16(20):6162-70","abstract":"The Schizosaccharomyces pombe wis1(+) gene is essential for cell survival under stress conditions. The MAPKK homologue Wis1 is required for activation of the MAPK homologue Spc1, and integrity of the Wis1-Spc1 pathway is required for survival in extreme conditions of heat, osmolarity, oxidation or limited nutrition. We show here that Wis4, a protein kinase of a new MAPKKK class, phosphorylates Wis1 in vitro and activates it in vivo. Win1 is also required for full activation of Wis1, and Win1 rather than Wis4 mediates the osmotic stress signal. Surprisingly, the pathway can still be activated by heat or oxidative stress independently of the phosphorylation of two conserved Wis1 residues. Evidence is presented that the Pyp1 protein tyrosine phosphatase, which dephosphorylates Spc1, is central to this alternative activation mechanism.","authors":"Samejima I, Mackie S, Fantes PA","authors_abbrev":"Samejima I et al.","pubmed_publication_date":"15 Oct 1997","pubmed_entrez_date":"1997-10-08","publication_year":"1997","canto_session_key":"37af2321f43c3188","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-10-26 12:47:29","canto_approved_date":"2026-01-11 17:52:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-26 12:47:22","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":48,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.09","SPAC26F1.10c","SPAC24B11.06c","SPAC19D5.01","SPAC9G1.02","SPBC409.07c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-10-26"},{"uniquename":"PMID:15338055","title":"Global gene expression of fission yeast in response to cisplatin.","citation":"Cell Mol Life Sci 2004 Sep;61(17):2253-63","abstract":"The cellular response to the antitumor drug cisplatin is complex, and resistance is widespread. To gain insights into the global transcriptional response and mechanisms of resistance, we used microarrays to examine the fission yeast cell response to cisplatin. In two isogenic strains with differing drug sensitivity, cisplatin activated a stress response involving glutathione-S-transferase, heat shock, and recombinational repair genes. Genes required for proteasome-mediated protein degradation were up-regulated in the sensitive strain, whereas genes for DNA damage recognition/repair and for mitotic progression were induced in the resistant strain. The response to cisplatin overlaps in part with the responses to cadmium and the DNA-damaging agent methylmethane sulfonate. The different gene groups involved in the cellular response to cisplatin help the cells to tolerate and repair DNA damage and to overcome cell cycle blocks. These findings are discussed with respect to known cisplatin response pathways in human cells.","authors":"Gatti L, Chen D, Beretta GL, Rustici G, Carenini N, Corna E, Colangelo D, Zunino F, Bähler J, Perego P","authors_abbrev":"Gatti L et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-09-01","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12548793","title":"[Comparative study of dependence of the cell proliferation of Saccharomyces cerevisiae and Schizosaccharomyces pombe on Ca2+].","citation":"Shi Yan Sheng Wu Xue Bao 1999 Mar;32(1):39-45","abstract":"Under the same experimental conditions, exogenous Ca2+ had no effect on the proliferation of S. cerevisiae, but it could obviously stimulate the proliferation of S. pombe. Ca2+ chelator EGTA had no inhibition effect on the proliferation of S. cerevisiae, but it apparently inhibited the proliferation of S. pombe and the inhibition could be effectively overcome by adding Ca2+. Non-special ion chelator EDTA could inhibit the proliferation of both S. cerevisiae and S. pombe, but the inhibition could not be overcome by adding Ca2+. The results above directly showed that the dependence of the proliferation of the two kinds of yeast on exogeneous Ca2+ was different. The growth rate of S. cerevisiae was about 3 times that of S. pombe and the proliferation of S. cerevisiae was independent on the exogenous Ca2+, which was similar to transformed cells. Therefore, in order to understand the relationship between the disorder of cell cycle and cell transformation, it was very important to study the mechanism of different effects of exogenous Ca2+ on the proliferation of the two kinds of yeast.","authors":"Yuan S, Lu ZM, Yin LH, Lu L","authors_abbrev":"Yuan S et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"2003-01-29","publication_year":"1999","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8114712","title":"Specific initiation at an origin of replication from Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1994 Mar;14(3):1796-805","abstract":"Using a genetic assay for efficient autonomous replication, we have isolated from Schizosaccharomyces pombe a 6.2-kb fragment which shows the properties expected of an origin of DNA replication in S. pombe. A 2.8-kb subclone of the fragment has the same replication properties. Two-dimensional gel analysis of replication intermediates throughout plasmids carrying the 6.2- or 2.8-kb fragments shows that replication initiates only in a specific region, which can be localized to within several hundred base pairs, in the fragments. This region is also a site of replication initiation in the S. pombe chromosome where the fragments normally reside. These results provide strong evidence that initiation of replication in S. pombe is localized and mediated by specific DNA sequence signals.","authors":"Caddle MS, Calos MP","authors_abbrev":"Caddle MS et al.","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37192628","title":"The mitochondrial intermembrane space protein mitofissin drives mitochondrial fission required for mitophagy.","citation":"Mol Cell 2023 Jun 15;83(12):2045-2058.e9","abstract":"Mitophagy plays an important role in mitochondrial homeostasis by selective degradation of mitochondria. During mitophagy, mitochondria should be fragmented to allow engulfment within autophagosomes, whose capacity is exceeded by the typical mitochondria mass. However, the known mitochondrial fission factors, dynamin-related proteins Dnm1 in yeasts and DNM1L/Drp1 in mammals, are dispensable for mitophagy. Here, we identify Atg44 as a mitochondrial fission factor that is essential for mitophagy in yeasts, and we therefore term Atg44 and its orthologous proteins mitofissin. In mitofissin-deficient cells, a part of the mitochondria is recognized by the mitophagy machinery as cargo but cannot be enwrapped by the autophagosome precursor, the phagophore, due to a lack of mitochondrial fission. Furthermore, we show that mitofissin directly binds to lipid membranes and brings about lipid membrane fragility to facilitate membrane fission. Taken together, we propose that mitofissin acts directly on lipid membranes to drive mitochondrial fission required for mitophagy.","doi":"10.1016/j.molcel.2023.04.022","authors":"Fukuda T, Furukawa K, Maruyama T, Yamashita SI, Noshiro D, Song C, Ogasawara Y, Okuyama K, Alam JM, Hayatsu M, Saigusa T, Inoue K, Ikeda K, Takai A, Chen L, Lahiri V, Okada Y, Shibata S, Murata K, Klionsky DJ, Noda NN, Kanki T","authors_abbrev":"Fukuda T et al.","pubmed_publication_date":"15 Jun 2023","pubmed_entrez_date":"2023-05-16","publication_year":"2023","canto_session_key":"42005ff3ae0fa290","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomoyuki Fukuda","canto_first_approved_date":"2023-06-13 14:13:43","canto_approved_date":"2023-10-11 19:19:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-09 07:02:59","canto_added_date":"2023-06-09 06:16:35","annotation_curators":[{"name":"Tomoyuki Fukuda","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.14c","SPBC1718.06"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-06-13","pdb_entries":[{"pdb_id":"7ydo","gene_chains":[{"gene_uniquename":"SPAC26A3.14c","chain":"A/B/C/D","position":"1-73"}],"title":"Crystal structure of Atg44","entry_authors":"Maruyama T,Noda NN","entry_authors_abbrev":"Maruyama T et al.","reference_uniquename":"PMID:37192628","experimental_method":"X-ray","resolution":"1.58"}]},{"uniquename":"PMID:18493947","title":"What controls TOR?","citation":"IUBMB Life 2008 Aug;60(8):483-96","abstract":"The target of rapamycin (TOR) is a protein kinase with numerous functions in cell growth control. Some of these functions can be potently inhibited by rapamycin, an immunosuppressive and potential anticancer drug. TOR exists as part of two functionally distinct protein complexes. The functions of TOR complex 1 (TORC1) are effectively inhibited by rapamycin, but the mechanism for this inhibition remains elusive. The identification of TORC2 and recent reports that rapamycin can inhibit TORC2 functions, in some cases, challenge current models of TOR regulation. This review discusses the latest findings in yeast and mammals on the possible mechanisms that control TOR activity leading to its many cellular functions","doi":"10.1002/iub.56","authors":"Jacinto E","authors_abbrev":"Jacinto E","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-05-22","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR019486","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC83.03c","HGNC:11969","HGNC:29318","HGNC:29190"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37076472","title":"Two assembly modes for SIN3 histone deacetylase complexes.","citation":"Cell Discov 2023 Apr 19;9(1):42","abstract":"The switch-independent 3 (SIN3)/histone deacetylase (HDAC) complexes play essential roles in regulating chromatin accessibility and gene expression. There are two major types of SIN3/HDAC complexes (named SIN3L and SIN3S) targeting different chromatin regions. Here we present the cryo-electron microscopy structures of the SIN3L and SIN3S complexes from Schizosaccharomyces pombe (S. pombe), revealing two distinct assembly modes. In the structure of SIN3L, each Sin3 isoform (Pst1 and Pst3) interacts with one histone deacetylase Clr6, and one WD40-containing protein Prw1, forming two lobes. These two lobes are bridged by two vertical coiled-coil domains from Sds3/Dep1 and Rxt2/Png2, respectively. In the structure of SIN3S, there is only one lobe organized by another Sin3 isoform Pst2; each of the Cph1 and Cph2 binds to an Eaf3 molecule, providing two modules for histone recognition and binding. Notably, the Pst1 Lobe in SIN3L and the Pst2 Lobe in SIN3S adopt similar conformation with their deacetylase active sites exposed to the space; however, the Pst3 Lobe in SIN3L is in a compact state with its active center buried inside and blocked. Our work reveals two classical organization mechanisms for the SIN3/HDAC complexes to achieve specific targeting and provides a framework for studying the histone deacetylase complexes.","doi":"10.1038/s41421-023-00539-x","authors":"Wang C, Guo Z, Chu C, Lu Y, Zhang X, Zhan X","authors_abbrev":"Wang C et al.","pubmed_publication_date":"19 Apr 2023","pubmed_entrez_date":"2023-04-19","publication_year":"2023","canto_session_key":"ef4650dd0b276332","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-05-11 13:43:03","canto_approved_date":"2023-05-11 13:43:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-05-11 13:42:52","canto_added_date":"2023-04-21 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.16c","SPAC16C9.05","SPBC428.06c","SPAC23H4.12","SPBC12C2.10c","SPAC2F7.07c","SPAC25B8.02","SPAC29A4.18","SPCC1259.07","SPBC36.05c","SPBC21C3.02c","SPBC1709.11c","SPAC23C11.15"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2023-05-11","pdb_entries":[{"pdb_id":"8i02","gene_chains":[{"gene_uniquename":"SPAC23C11.15","chain":"A","position":"1-1075"},{"gene_uniquename":"SPAC23H4.12","chain":"D/E","position":"1-337"},{"gene_uniquename":"SPAC29A4.18","chain":"C","position":"1-431"},{"gene_uniquename":"SPBC36.05c","chain":"B","position":"1-405"},{"gene_uniquename":"SPAC2F7.07c","chain":"G","position":"1-607"},{"gene_uniquename":"SPAC16C9.05","chain":"F","position":"1-404"}],"title":"Cryo-EM structure of the SIN3S complex from S. pombe","entry_authors":"Wang C,Guo Z,Zhan X","entry_authors_abbrev":"Wang C et al.","reference_uniquename":"PMID:37076472","experimental_method":"EM","resolution":"2.9"},{"pdb_id":"8i03","gene_chains":[{"gene_uniquename":"SPAC29A4.18","chain":"J/K","position":"1-431"},{"gene_uniquename":"SPBC36.05c","chain":"C/D","position":"1-405"},{"gene_uniquename":"SPBC1709.11c","chain":"H","position":"1-305"},{"gene_uniquename":"SPBC1734.16c","chain":"B","position":"1-1154"},{"gene_uniquename":"SPBC428.06c","chain":"F","position":"1-240"},{"gene_uniquename":"SPCC1259.07","chain":"I","position":"1-351"},{"gene_uniquename":"SPBC12C2.10c","chain":"A","position":"1-1522"},{"gene_uniquename":"SPBC21C3.02c","chain":"E","position":"1-491"},{"gene_uniquename":"SPAC25B8.02","chain":"G","position":"1-267"}],"title":"Cryo-EM structure of the SIN3L complex from S. pombe","entry_authors":"Wang C,Guo Z,Zhan X","entry_authors_abbrev":"Wang C et al.","reference_uniquename":"PMID:37076472","experimental_method":"EM","resolution":"3.2"}]},{"uniquename":"PMID:38778742","title":"The flavohemoglobin Yhb1 is a new interacting partner of the heme transporter Str3.","citation":"Mol Microbiol 2024 May 22;","abstract":"Nitric oxide (˙NO) is a free radical that induces nitrosative stress, which can jeopardize cell viability. Yeasts have evolved diverse detoxification mechanisms to effectively counteract ˙NO-mediated cytotoxicity. One mechanism relies on the flavohemoglobin Yhb1, whereas a second one requires the S-nitrosoglutathione reductase Fmd2. To investigate heme-dependent activation of Yhb1 in response to ˙NO, we use hem1Δ-derivative Schizosaccharomyces pombe strains lacking the initial enzyme in heme biosynthesis, forcing cells to assimilate heme from external sources. Under these conditions, yhb1 +  mRNA levels are repressed in the presence of iron through a mechanism involving the GATA-type transcriptional repressor Fep1. In contrast, when iron levels are low, the transcription of yhb1 +  is derepressed and further induced in the presence of the ˙NO donor DETANONOate. Cells lacking Yhb1 or expressing inactive forms of Yhb1 fail to grow in a hemin-dependent manner when exposed to DETANONOate. Similarly, the loss of function of the heme transporter Str3 phenocopies the effects of Yhb1 disruption by causing hypersensitivity to DETANONOate under hemin-dependent culture conditions. Coimmunoprecipitation and bimolecular fluorescence complementation assays demonstrate the interaction between Yhb1 and the heme transporter Str3. Collectively, our findings unveil a novel pathway for activating Yhb1, fortifying yeast cells against nitrosative stress.","doi":"10.1111/mmi.15281","authors":"Ping FLY, Vahsen T, Brault A, Néré R, Labbé S","authors_abbrev":"Ping FLY et al.","pubmed_publication_date":"22 May 2024","pubmed_entrez_date":"2024-05-23","publication_year":"2024","canto_session_key":"85ce758f4a611005","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-05-23 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21035573","title":"Drosophila vigilin, DDP1, localises to the cytoplasm and associates to the rough endoplasmic reticulum.","citation":"Biochim Biophys Acta 2011 Jan;1809(1):46-55","abstract":"Functional characterisation of vigilin, a highly conserved multi-KH-domain protein that binds RNA and ssDNA, remains elusive and, to some extent, controversial. Studies performed in Saccharomyces cerevisiae and human cells indicate that vigilin localises to the cytoplasm, binds ribosomes, associates to RER and regulates mRNA translation. On the other hand, we and others reported a contribution to heterochromatin-mediated gene silencing (PEV) and chromosome segregation in S. cerevisiae, Drosophila and human cells. Whether this contribution is direct remains, however, unclear. Here, we report that Drosophila vigilin, DDP1, vastly localises to the cytoplasm, being largely excluded from the nucleus. We also show that DDP1 preferentially associates to RER and co-purifies with several ribosomal proteins, suggesting a contribution to mRNA translation. In light of these results, the contribution of DDP1 to PEV was re-examined. Here, we show that a newly generated null ddp1(Δ) mutation is only a weak suppressor of PEV, which is in contrast with our own previous results showing dominant suppression in the presence of a strong hypomorphic ddp1(15.1) mutation. Similar results were obtained in the fission yeast Schizosaccharomyces pombe, where vigilin (Vgl1) also associates to RER, having no significant contribution to PEV at centromeres, telomeres and the mating-type locus. Altogether, these results indicate that cytoplasmic localisation and association to RER, but not contribution to heterochromatin organisation, are evolutionarily conserved features of vigilin, favouring a model by which vigilin acts in the cytoplasm, regulating RNA metabolism, and affects nuclear functions only indirectly.","doi":"10.1016/j.bbagrm.2010.10.005","authors":"Batlle M, Marsellach FX, Huertas D, Azorín F","authors_abbrev":"Batlle M et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-11-02","publication_year":"2011","canto_session_key":"dd7f90a794036d3d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-07-24 18:51:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-24 18:51:32","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC550.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-24"},{"uniquename":"PMID:23572080","title":"Distinct roles for Sir2 and RNAi in centromeric heterochromatin nucleation, spreading and maintenance.","citation":"EMBO J 2013 May 02;32(9):1250-64","abstract":"Epigenetically regulated heterochromatin domains govern essential cellular activities. A key feature of heterochromatin domains is the presence of hypoacetylated nucleosomes, which are methylated on lysine 9 of histone H3 (H3K9me). Here, we investigate the requirements for establishment, spreading and maintenance of heterochromatin using fission yeast centromeres as a paradigm. We show that establishment of heterochromatin on centromeric repeats is initiated at modular 'nucleation sites' by RNA interference (RNAi), ensuring the mitotic stability of centromere-bearing minichromosomes. We demonstrate that the histone deacetylases Sir2 and Clr3 and the chromodomain protein Swi6(HP1) are required for H3K9me spreading from nucleation sites, thus allowing formation of extended heterochromatin domains. We discovered that RNAi and Sir2 along with Swi6(HP1) operate in two independent pathways to maintain heterochromatin. Finally, we demonstrate that tethering of Sir2 is pivotal to the maintenance of heterochromatin at an ectopic locus in the absence of RNAi. These analyses reveal that Sir2, together with RNAi, are sufficient to ensure heterochromatin integrity and provide evidence for sequential establishment, spreading and maintenance steps in the assembly of centromeric heterochromatin.","doi":"10.1038/emboj.2013.72","authors":"Buscaino A, Lejeune E, Audergon P, Hamilton G, Pidoux A, Allshire RC","authors_abbrev":"Buscaino A et al.","pubmed_publication_date":"02 May 2013","pubmed_entrez_date":"2013-04-11","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.13c","SPCC663.12","SPBC800.03","SPBC16D10.07c","SPAC664.01c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:6924071","title":"Recombination between dispersed serine tRNA genes in Schizosaccharomyces pombe.","citation":"Nature 1982 Nov 18;300(5889):225-31","abstract":"","authors":"Munz P, Amstutz H, Kohli J, Leupold U","authors_abbrev":"Munz P et al.","pubmed_publication_date":"18 Nov 1982","pubmed_entrez_date":"1982-11-18","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31255284","title":"Nuclear aconitase antagonizes heterochromatic silencing by interfering with Chp1 binding to DNA.","citation":"Biochem Biophys Res Commun 2019 Aug 27;516(3):806-811","abstract":"In Schizosaccharomyces pombe, there are two aconitases, Aco1 and Aco2, involved in the Krebs cycle in mitochondria. Interestingly, Aco2 is localized to nucleus as well. Here, we investigated the nuclear role of Aco2 by deleting its nuclear localization signal. The aco2ΔNLS mutation suppressed the gene-silencing defects of RNAi mutants at the centromere, where heterochromatin formation depends on RNAi pathway. In Δago1, the aco2ΔNLS mutation restored heterochromatin through elevating Chp1 binding. Aco2 physically interacted with Chp1 via the N-terminal chromodomain that binds to methylated histone H3K9. In the sub-telomeric region, where heterochromatin forms independent of RNAi pathway, the single aco2ΔNLS mutation caused extra gene silencing via elevating Chp1 binding, without increasing histone methylation. The anti-silencing effect did not require the catalytic function of aconitase. Taken together, Aco2 functions as an epigenetic regulator of gene expression, through associating with chromodomain of Chp1 to maintain heterochromatin.","doi":"10.1016/j.bbrc.2019.06.090","authors":"Jung SJ, Choi Y, Lee D, Roe JH","authors_abbrev":"Jung SJ et al.","pubmed_publication_date":"27 Aug 2019","pubmed_entrez_date":"2019-07-01","publication_year":"2019","canto_session_key":"6c9c6f10143f1066","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-07-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11967147","title":"Two kinesin-like Kin I family proteins in fission yeast regulate the establishment of metaphase and the onset of anaphase A.","citation":"Curr Biol 2002 Apr 16;12(8):610-21","abstract":"Metaphase is thought to be a force-equilibrium state of \"tug of war,\" in which poleward forces are pulling kinetochores and counteracting the cohesive forces between the centromeres. Unlike conventional kinesins, members of the Kin I family are microtubule-depolymerizing enzymes, which are expected to be molecules that could generate poleward forces.\nWe have characterized mitotic roles of two Kin I homologs, Klp5 and Klp6, in fission yeast. Klp5 and Klp6 colocalize to the mitotic kinetochores and the spindle midzone. These two proteins form a heterocomplex, but not a homocomplex. Albeit not essential, both proteins are required for accurate chromosome segregation and normal morphology of interphase microtubules. Time-lapse live analysis using GFP-alpha-tubulin indicates that these mutants spend a much longer time (2-fold) in mitosis before the initiation of anaphase B. Further observation using kinetochore and centromere markers shows that, in these mutants, sister centromeres move back and forth between the two poles, indicating that entry into anaphase A is delayed. This is supported by live image analysis showing that Cut2 securin is retained during the prolonged mitosis. Furthermore, the mitotic extension is dependent upon the Mad2 spindle checkpoint.\nWe discuss two models of Kin I function in fission yeast. One proposes that Klp5 and Klp6 are required for efficient capturing of kinetochores by the spindles, while the other proposes that they are required to generate tension upon kinetochore capturing. Kin I, therefore, plays a fundamental role in the establishment of metaphase, probably by generating poleward forces at the kinetochores.","authors":"Garcia MA, Koonrugsa N, Toda T","authors_abbrev":"Garcia MA et al.","pubmed_publication_date":"16 Apr 2002","pubmed_entrez_date":"2002-04-23","publication_year":"2002","canto_session_key":"e1d7e0f4cb098e1f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-26 16:12:59","canto_approved_date":"2018-01-26 16:12:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-22 18:32:45","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":40,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.13","SPBC20F10.06","SPAC3A11.14c","SPBC1685.15c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-01-26"},{"uniquename":"PMID:859464","title":"[Production of hybrids between Schizosaccharomyces pombe and Octosporomyces japonicus].","citation":"Mikrobiologiia 1977;46(1):75-9","abstract":"","authors":"Kosikov KV, Medvedeva AA","authors_abbrev":"Kosikov KV et al.","pubmed_publication_date":"1977","pubmed_entrez_date":"1977-01-01","publication_year":"1977","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8223442","title":"The activity of S.pombe DSC-1-like factor is cell cycle regulated and dependent on the activity of p34cdc2.","citation":"EMBO J 1993 Nov;12(11):4325-34","abstract":"In the eukaryotic cell cycle, there are major control points in late G2 to determine the timing of the initiation of mitosis, and in late G1, regulating entry into S phase. In yeasts, this latter control is called start. Traverse of the start control and progression to S phase is accompanied by an increase in the expression of some of the genes whose products are required for DNA synthesis. In Saccharomyces cerevisiae, the coordinate expression of these genes in late G1 is dependent on a cis-acting sequence element called the MluI cell cycle box (MCB). A transcription factor called DSC-1 binds these elements and mediates cell cycle regulated transcription, though it is unclear whether this is by cell cycle-dependent changes in its activity. A DSC-1-like factor has also been identified in the fission yeast S.pombe. This is composed of at least the products of the cdc10 and sct1/res1 genes, and binds to the promoters of genes whose expression increases prior to S phase. We demonstrate that p85cdc10 is a nuclear protein and that the activity of the S.pombe DSC-1 factor varies through the cell cycle; it is high in cells that have passed start, decreases at the time of anaphase, remains low during the pre-start phase of G1 and increases at the time of the next S phase. We also show that the reactivation in late G1 is dependent on the G1 form of p34cdc2.","authors":"Reymond A, Marks J, Simanis V","authors_abbrev":"Reymond A et al.","pubmed_publication_date":"Nov 1993","pubmed_entrez_date":"1993-11-01","publication_year":"1993","canto_session_key":"d3b7363a1174a921","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-30 17:09:43","canto_approved_date":"2022-02-07 18:12:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-01 14:40:59","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPBC725.16","SPBC11B10.09","SPBC336.12c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2020-12-30"},{"uniquename":"EMBL:SPC00429","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31041892","title":"Fission yeast type 2 node proteins Blt1p and Gef2p cooperate to ensure timely completion of cytokinesis.","citation":"BMC Mol Cell Biol 2019 Jan 24;20(1):1","abstract":"The conserved NDR-family kinase Sid2p localizes to the contractile ring during fission yeast cytokinesis to promote ring constriction, septation, and completion of cell division. Previous studies have found that the Type 2 interphase node proteins Blt1p and Gef2p contribute to localization of Sid2p and its regulatory protein Mob1p at the division site. However, their relative contributions and whether they operate in the same or parallel pathways has been unclear. In this study, we quantify the respective roles of Blt1p and Gef2p in Sid2p/Mob1p recruitment and characterize the effect of single and double deletion mutants on contractile ring dynamics and completion of cell division.\nUsing quantitative confocal fluorescence microscopy, we measured Sid2p and Mob1p recruitment to the division site in blt1∆, gef2∆, and blt1∆/gef2∆ mutant cells. We observed an equivalent decrease in Sid2p/Mob1p localization for both single and double mutants. Though assembly of the contractile ring is normal in these mutants, the reduction in Sid2p/Mob1p at the division site delayed the onset of contractile ring constriction and completion of division. We quantified localization of Blt1p and Gef2p at the medial cortex throughout the cell cycle and found that Blt1p localization to interphase nodes and the contractile ring is independent of Gef2p. However, Gef2p localization to the contractile ring is decreased in blt1∆ mutants.\nBlt1p and Gef2p work in the same pathway, rather than in parallel, to localize the NDR-family kinase Sid2p and its regulatory partner Mob1p to the division site, thereby promoting timely completion of cell division. Future studies are necessary to understand how additional fission yeast cytokinesis proteins work with these Type 2 interphase node components to promote Sid2p/Mob1p recruitment.","doi":"10.1186/s12860-018-0182-z","authors":"Kwon L, Magee EM, Crayton A, Goss JW","authors_abbrev":"Kwon L et al.","pubmed_publication_date":"24 Jan 2019","pubmed_entrez_date":"2019-05-02","publication_year":"2019","canto_session_key":"57ac88324e0b82e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"John W Goss","canto_first_approved_date":"2019-11-14 16:38:25","canto_approved_date":"2025-09-04 11:53:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-12 14:58:03","canto_added_date":"2019-05-03 00:15:04","annotation_curators":[{"name":"John W Goss","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.16","SPAC24B11.11c","SPBC1A4.05","SPBC428.13c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-11-14"},{"uniquename":"PMID:25497836","title":"Heterochromatin assembly and transcriptome repression by Set1 in coordination with a class II histone deacetylase.","citation":"Elife 2014 Dec 15;3:e04506","abstract":"Histone modifiers play essential roles in controlling transcription and organizing eukaryotic genomes into functional domains. Here, we show that Set1, the catalytic subunit of the highly conserved Set1C/COMPASS complex responsible for histone H3K4 methylation (H3K4me), behaves as a repressor of the transcriptome largely independent of Set1C and H3K4me in the fission yeast Schizosaccharomyces pombe. Intriguingly, while Set1 is enriched at highly expressed and repressed loci, Set1 binding levels do not generally correlate with the levels of transcription. We show that Set1 is recruited by the ATF/CREB homolog Atf1 to heterochromatic loci and promoters of stress-response genes. Moreover, we demonstrate that Set1 coordinates with the class II histone deacetylase Clr3 in heterochromatin assembly at prominent chromosomal landmarks and repression of the transcriptome that includes Tf2 retrotransposons, noncoding RNAs, and regulators of development and stress-responses. Our study delineates a molecular framework for elucidating the functional links between transcriptome control and chromatin organization.","doi":"10.7554/eLife.04506","authors":"Lorenz DR, Meyer LF, Grady PJ, Meyer MM, Cam HP","authors_abbrev":"Lorenz DR et al.","pubmed_publication_date":"15 Dec 2014","pubmed_entrez_date":"2014-12-16","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-12-18 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC800.03","SPBC29B5.01","SPCC306.04c"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:16535475","title":"Purification and Characterization of Two Dihydroxyacetone Kinases from Schizosaccharomyces pombe IFO 0354.","citation":"Appl Environ Microbiol 1996 Dec;62(12):4663-5","abstract":"Two dihydroxyacetone kinases (DHAKs), DHAK I and DHAK II, were purified to homogeneity from Schizosaccharomyces pombe IFO 0354. They were immunologically different from each other. Although both of the enzymes had some affinity for glycerol and dl-glyceraldehyde in addition to dihydroxyacetone and glyceraldehyde, V(infmax) values for dihydroxyacetone were much higher than those for glycerol and dl-glyceraldehyde. On the basis of the K(infm) values of both enzymes for dihydroxyacetone, DHAK II plays a more important role than DHAK I in dissimilation of glycerol via dihydroxyacetone.","authors":"Yoshihara K, Shimada Y, Karita S, Kimura T, Sakka K, Ohmiya K","authors_abbrev":"Yoshihara K et al.","pubmed_publication_date":"Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_session_key":"8bfb58245e34adbd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-12-13 13:51:13","canto_approved_date":"2023-12-13 13:51:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-13 13:49:29","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.11","SPAC977.16c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-12-13"},{"uniquename":"EMBL:SPD241","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18375981","title":"Distinct regions of ATF/CREB proteins Atf1 and Pcr1 control recombination hotspot ade6-M26 and the osmotic stress response.","citation":"Nucleic Acids Res 2008 May;36(9):2838-51","abstract":"The Atf1 protein of Schizosaccharomyces pombe contains a bZIP (DNA-binding/protein dimerization) domain characteristic of ATF/CREB proteins, but no other functional domains or clear homologs have been reported. Atf1-containing, bZIP protein dimers bind to CRE-like DNA sites, regulate numerous stress responses, and activate meiotic recombination at hotspots like ade6-M26. We defined systematically the organization of Atf1 and its heterodimer partner Pcr1, which is required for a subset of Atf1-dependent functions. Surprisingly, only the bZIP domain of Pcr1 is required for hotspot activity and tethering of Atf1 to ade6 promotes recombination in the absence of its bZIP domain and the Pcr1 protein. Therefore the recombination-activation domain of Atf1-Pcr1 heterodimer resides exclusively in Atf1, and Pcr1 confers DNA-binding site specificity in vivo. Atf1 has a modular organization in which distinct regions affect differentially the osmotic stress response (OSA) and meiotic recombination (HRA, HRR). The HRA and HRR regions are necessary and sufficient to activate and repress recombination, respectively. Moreover, Atf1 defines a family of conserved proteins with discrete sequence motifs in the functional domains (OSA, HRA, HRR, bZIP). These findings reveal the functional organization of Atf1 and Pcr1, and illustrate several mechanisms by which bZIP proteins can regulate multiple, seemingly disparate activities.","doi":"10.1093/nar/gkn037","authors":"Gao J, Davidson MK, Wahls WP","authors_abbrev":"Gao J et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-04-01","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:26201080","title":"The DNA-Binding Domain of S. pombe Mrc1 (Claspin) Acts to Enhance Stalling at Replication Barriers.","citation":"PLoS One 2015;10(7):e0132595","abstract":"During S-phase replication forks can stall at specific genetic loci. At some loci, the stalling events depend on the replisome components Schizosaccharomyces pombe Swi1 (Saccharomyces cerevisiae Tof1) and Swi3 (S. cerevisiae Csm3) as well as factors that bind DNA in a site-specific manner. Using a new genetic screen we identified Mrc1 (S. cerevisiae Mrc1/metazoan Claspin) as a replisome component involved in replication stalling. Mrc1 is known to form a sub-complex with Swi1 and Swi3 within the replisome and is required for the intra-S phase checkpoint activation. This discovery is surprising as several studies show that S. cerevisiae Mrc1 is not required for replication barrier activity. In contrast, we show that deletion of S. pombe mrc1 leads to an approximately three-fold reduction in barrier activity at several barriers and that Mrc1's role in replication fork stalling is independent of its role in checkpoint activation. Instead, S. pombe Mrc1 mediated fork stalling requires the presence of a functional copy of its phylogenetically conserved DNA binding domain. Interestingly, this domain is on the sequence level absent from S. cerevisiae Mrc1. Our study indicates that direct interactions between the eukaryotic replisome and the DNA are important for site-specific replication stalling.","doi":"10.1371/journal.pone.0132595","authors":"Zech J, Godfrey EL, Masai H, Hartsuiker E, Dalgaard JZ","authors_abbrev":"Zech J et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-07-23","publication_year":"2015","canto_session_key":"e9eb8e4b99c0563d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-07-06 10:08:04","canto_approved_date":"2019-06-14 13:37:49","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-07-04 15:41:52","canto_added_date":"2015-07-24 00:20:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":33,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPCC18B5.11c","SPCC1259.13","SPAC6F6.17","SPBC336.12c","SPBC776.12c","SPBC30D10.04","SPAC694.06c","SPBC216.06c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2018-07-06"},{"uniquename":"PMID:27477394","title":"Comparative Proteome Analysis in Schizosaccharomyces pombe Identifies Metabolic Targets to Improve Protein Production and Secretion.","citation":"Mol Cell Proteomics 2016 Oct;15(10):3090-3106","abstract":"Protein secretion in yeast is a complex process and its efficiency depends on a variety of parameters. We performed a comparative proteome analysis of a set of Schizosaccharomyces pombe strains producing the α-glucosidase maltase in increasing amounts to investigate the overall proteomic response of the cell to the burden of protein production along the various steps of protein production and secretion. Proteome analysis of these strains, utilizing an isobaric labeling/two dimensional LC-MALDI MS approach, revealed complex changes, from chaperones and secretory transport machinery to proteins controlling transcription and translation. We also found an unexpectedly high amount of changes in enzyme levels of the central carbon metabolism and a significant up-regulation of several amino acid biosyntheses. These amino acids were partially underrepresented in the cellular protein compared with the composition of the model protein. Additional feeding of these amino acids resulted in a 1.5-fold increase in protein secretion. Membrane fluidity was identified as a second bottleneck for high-level protein secretion and addition of fluconazole to the culture caused a significant decrease in ergosterol levels, whereas protein secretion could be further increased by a factor of 2.1. In summary, we show that high level protein secretion causes global changes of protein expression levels in the cell and that precursor availability and membrane composition limit protein secretion in this yeast. In this respect, comparative proteome analysis is a powerful tool to identify targets for an efficient increase of protein production and secretion in S. pombe Data are available via ProteomeXchange with identifiers PXD002693 and PXD003016.","authors":"Hung CW, Klein T, Cassidy L, Linke D, Lange S, Anders U, Bureik M, Heinzle E, Schneider K, Tholey A","authors_abbrev":"Hung CW et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-08-02","publication_year":"2016","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2016-08-03 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19884503","title":"Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain.","citation":"Proc Natl Acad Sci U S A 2009 Nov 17;106(46):19298-303","abstract":"Telomeres must be capped to preserve chromosomal stability. The conserved Stn1 and Ten1 proteins are required for proper capping of the telomere, although the mechanistic details of how they contribute to telomere maintenance are unclear. Here, we report the crystal structures of the C-terminal domain of the Saccharomyces cerevisiae Stn1 and the Schizosaccharomyces pombe Ten1 proteins. These structures reveal striking similarities to corresponding subunits in the replication protein A complex, further supporting an evolutionary link between telomere maintenance proteins and DNA repair complexes. Our structural and in vivo data of Stn1 identify a new domain that has evolved to support a telomere-specific role in chromosome maintenance. These findings endorse a model of an evolutionarily conserved mechanism of DNA maintenance that has developed as a result of increased chromosomal structural complexity.","doi":"10.1073/pnas.0909203106","authors":"Gelinas AD, Paschini M, Reyes FE, Héroux A, Batey RT, Lundblad V, Wuttke DS","authors_abbrev":"Gelinas AD et al.","pubmed_publication_date":"17 Nov 2009","pubmed_entrez_date":"2009-11-04","publication_year":"2009","canto_session_key":"4af320247b10ecdd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-02-15 17:57:09","canto_approved_date":"2023-07-05 11:52:47","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-02-15 17:57:02","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1393.14","SPBC409.12c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2023-02-15","pdb_entries":[{"pdb_id":"3k0x","gene_chains":[{"gene_uniquename":"SPCC1393.14","chain":"A","position":"1-102"}],"title":"Crystal structure of telomere capping protein Ten1 from Saccharomyces pombe","entry_authors":"Gelinas AD,Reyes FE,Batey RT,Wuttke DS","entry_authors_abbrev":"Gelinas AD et al.","reference_uniquename":"PMID:19884503","experimental_method":"X-ray","resolution":"1.7"}]},{"uniquename":"PMID:33313903","title":"Ribosome profiling reveals ribosome stalling on tryptophan codons and ribosome queuing upon oxidative stress in fission yeast.","citation":"Nucleic Acids Res 2021 Jan 11;49(1):383-399","abstract":"Translational control is essential in response to stress. We investigated the translational programmes launched by the fission yeast Schizosaccharomyces pombe upon five environmental stresses. We also explored the contribution of defence pathways to these programmes: The Integrated Stress Response (ISR), which regulates translation initiation, and the stress-response MAPK pathway. We performed ribosome profiling of cells subjected to each stress, in wild type cells and in cells with the defence pathways inactivated. The transcription factor Fil1, a functional homologue of the yeast Gcn4 and the mammalian Atf4 proteins, was translationally upregulated and required for the response to most stresses. Moreover, many mRNAs encoding proteins required for ribosome biogenesis were translationally downregulated. Thus, several stresses trigger a universal translational response, including reduced ribosome production and a Fil1-mediated transcriptional programme. Surprisingly, ribosomes stalled on tryptophan codons upon oxidative stress, likely due to a decrease in charged tRNA-Tryptophan. Stalling caused ribosome accumulation upstream of tryptophan codons (ribosome queuing/collisions), demonstrating that stalled ribosomes affect translation elongation by other ribosomes. Consistently, tryptophan codon stalling led to reduced translation elongation and contributed to the ISR-mediated inhibition of initiation. We show that different stresses elicit common and specific translational responses, revealing a novel role in Tryptophan-tRNA availability.","doi":"10.1093/nar/gkaa1180","authors":"Rubio A, Ghosh S, Mülleder M, Ralser M, Mata J","authors_abbrev":"Rubio A et al.","pubmed_publication_date":"11 Jan 2021","pubmed_entrez_date":"2020-12-14","publication_year":"2021","canto_session_key":"190ddb12f4f3e614","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juan Mata","canto_first_approved_date":"2021-02-19 13:51:07","canto_approved_date":"2023-10-17 18:04:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-15 18:10:20","canto_added_date":"2020-12-16 01:15:07","annotation_curators":[{"name":"Juan Mata","community_curator":true,"annotation_count":12,"orcid":"0000-0002-5514-3653","file_type":null,"file_name":null}],"file_curator_name":"Angela 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and biochemical properties of fission yeast Arp2/3 complex lacking the Arp2 subunit.","citation":"J Biol Chem 2008 Sep 26;283(39):26490-8","abstract":"Arp2/3 (actin-related protein 2/3) complex is a seven-subunit complex that nucleates branched actin filaments in response to cellular signals. Nucleation-promoting factors such as WASp/Scar family proteins activate the complex by facilitating the activating conformational change and recruiting the first actin monomer for the daughter branch. Here we address the role of the Arp2 subunit in the function of Arp2/3 complex by isolating a version of the complex lacking Arp2 (Arp2Delta Arp2/3 complex) from fission yeast. An x-ray crystal structure of the DeltaArp2 Arp2/3 complex showed that the rest of the complex is unperturbed by the loss of Arp2. However, the Arp2Delta Arp2/3 complex was inactive in actin nucleation assays, indicating that Arp2 is essential to form a branch. A fluorescence anisotropy assay showed that Arp2 does not contribute to the affinity of the complex for Wsp1-VCA, a Schizosaccharomyces pombe nucleation-promoting factor protein. Fluorescence resonance energy transfer experiments showed that the loss of Arp2 does not prevent VCA from recruiting an actin monomer to the complex. Truncation of the N terminus of ARPC5, the smallest subunit in the complex, increased the yield of Arp2Delta Arp2/3 complex during purification but did not compromise nucleation activity of the full Arp2/3 complex.","doi":"10.1074/jbc.M802607200","authors":"Nolen BJ, Pollard TD","authors_abbrev":"Nolen BJ et al.","pubmed_publication_date":"26 Sep 2008","pubmed_entrez_date":"2008-07-22","publication_year":"2008","canto_session_key":"b9dddd6cca4a0b44","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-08-21 15:30:32","canto_approved_date":"2019-08-21 15:30:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-08-21 15:30:14","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.04c","SPAC6F6.10c","SPAC630.03","SPAC6G9.07c","SPBC14C8.06","SPAC11H11.06","SPBC1778.08c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2019-08-21","pdb_entries":[{"pdb_id":"3dwl","gene_chains":[{"gene_uniquename":"SPAC6F6.10c","chain":"D/I","position":"1-317"},{"gene_uniquename":"SPAC630.03","chain":"A/B","position":"1-427"},{"gene_uniquename":"SPBC14C8.06","chain":"C/H","position":"1-377"},{"gene_uniquename":"SPAC17G8.04c","chain":"G/L","position":"1-152"},{"gene_uniquename":"SPAC6G9.07c","chain":"F/K","position":"1-168"},{"gene_uniquename":"SPBC1778.08c","chain":"E/J","position":"1-174"}],"title":"Crystal Structure of Fission Yeast Arp2/3 Complex Lacking the Arp2 Subunit","entry_authors":"Nolen BJ,Pollard TD","entry_authors_abbrev":"Nolen BJ et al.","reference_uniquename":"PMID:18640983","experimental_method":"X-ray","resolution":"3.78"}]},{"uniquename":"PMID:28250214","title":"Improved Tandem Affinity Purification Tag and Methods for Isolation of Proteins and Protein Complexes from  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Mar 01;2017(3):pdb.prot091611","abstract":"The tandem affinity purification (TAP) method uses an epitope that contains two different affinity purification tags separated by a site-specific protease site to isolate a protein rapidly and easily. Proteins purified via the TAP tag are eluted under mild conditions, allowing them to be used for structural and biochemical analyses. The original TAP tag contains a calmodulin-binding peptide and the IgG-binding domain from protein A separated by a tobacco etch virus (TEV) protease cleavage site. After capturing the Protein A epitope on an IgG resin, bound proteins are released by incubation with the TEV protease and then isolated on a calmodulin matrix in the presence of calcium; elution from this resin is achieved by chelating calcium with EGTA. However, because the robustness of the calmodulin-binding step in this procedure is highly variable, we replaced the calmodulin-binding peptide with three copies of the FLAG epitope, (3× FLAG)-TEV-Protein A, which can be isolated using an anti-FLAG resin. Elution from this matrix is achieved in the presence of an excess of a 3× FLAG peptide. In addition to allowing proteins to be released under mild conditions, elution by the 3× FLAG peptide adds an extra layer of specificity to the TAP procedure, because it liberates only FLAG-tagged proteins.","doi":"10.1101/pdb.prot091611","authors":"Zilio N, Boddy MN","authors_abbrev":"Zilio N et al.","pubmed_publication_date":"01 Mar 2017","pubmed_entrez_date":"2017-03-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-03-04 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23980030","title":"A novel factor Iss10 regulates Mmi1-mediated selective elimination of meiotic transcripts.","citation":"Nucleic Acids Res 2013 Nov;41(21):9680-7","abstract":"A number of meiosis-specific transcripts are selectively eliminated during the mitotic cell cycle in fission yeast. Mmi1, an RNA-binding protein, plays a crucial role in this selective elimination. Mmi1 recognizes a specific region, namely, the determinant of selective removal (DSR) on meiotic transcripts and induces nuclear exosome-mediated elimination. During meiosis, Mmi1 is sequestered by a chromosome-associated dot structure, Mei2 dot, allowing meiosis-specific transcripts to be stably expressed. Red1, a zinc-finger protein, is also known to participate in the Mmi1/DSR elimination system, although its molecular function has remained elusive. To uncover the detailed molecular mechanisms underlying the Mmi1/DSR elimination system, we sought to identify factors that interact genetically with Mmi1. Here, we show that one of the identified factors, Iss10, is involved in the Mmi1/DSR system by regulating the interaction between Mmi1 and Red1. In cells lacking Iss10, association of Red1 with Mmi1 is severely impaired, and target transcripts of Mmi1 are ectopically expressed in the mitotic cycle. During meiosis, Iss10 is downregulated, resulting in dissociation of Red1 from Mmi1 and subsequent suppression of Mmi1 activity.","doi":"10.1093/nar/gkt763","authors":"Yamashita A, Takayama T, Iwata R, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-08-28","publication_year":"2013","canto_session_key":"4f633d62f95cab65","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-03-20 13:34:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-11-15 01:41:44","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":58,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22G7.10","SPBC16E9.12c","SPBC29A10.02","SPAC19G12.17","SPNCRNA.103","SPCC736.12c","SPBC2A9.11c","SPBC29A10.14","SPBC646.04","SPBC337.03","SPAC27D7.03c","SPAC7D4.14c","SPAC27D7.13c","SPBC32H8.11","SPAC1006.03c"],"gene_count":15,"ltp_gene_count":11,"approved_date":"2013-11-15"},{"uniquename":"PMID:21153812","title":"Processing and maturation of carboxypeptidase Y and alkaline phosphatase in Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2011 Apr;90(1):203-13","abstract":"Schizosaccharomyces pombe carboxypeptidase Y (CPY) is synthesized as a zymogen and transported into the vacuole where maturation and activation occurs. The 110-kDa S. pombe CPY precursor is processed twice and finally converted to a mature form consisting of polypeptides of approximately 19 and 32 kDa linked by a single disulfide bond. In Saccharomyces cerevisiae, maturation of CPY occurs mostly through the activity of vacuolar aspartyl protease Pep4p, whereas a Pep4p homolog has not been found in the S. pombe genome database. Based on analysis of protease-deficient mutants, we found that S. pombe CPY was not able to be processed or activated in isp6Δpsp3Δ double disruptants. Both Isp6p and Psp3p are subtilase-type serine proteases with related sequences. Moreover, alkaline phosphatase of S. pombe was found to be localized at the vacuolar membrane and was also unprocessed in isp6Δpsp3Δ double disruptants. Vacuolar localization of GFP-fused Isp6p and Psp3p was determined by fluorescence microscopy. These results suggest that the two serine proteases Isp6p and Psp3p are functional in the vacuole and are involved in proteolytic processing of vacuolar proteins.","doi":"10.1007/s00253-010-3031-3","authors":"Mukaiyama H, Iwaki T, Idiris A, Takegawa K","authors_abbrev":"Mukaiyama H et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2010-12-15","publication_year":"2011","canto_session_key":"71662226413c7ee0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2017-09-16 14:05:36","canto_approved_date":"2020-01-17 11:58:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-01-27 09:26:26","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1711.12","SPAC1296.03c","SPAC4F10.02","SPAP14E8.04","SPAC19B12.08","SPAC19G12.10c","SPBC14F5.13c","SPBC14C8.03","SPAC4A8.04","SPAC1006.01"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2017-09-16"},{"uniquename":"PMID:32049412","title":"Human Ebp1 rescues the synthetic lethal growth of fission yeast cells lacking Cdb4 and Nup184.","citation":"Genes Cells 2020 Apr;25(4):288-295","abstract":"Cdb4 is a protein with unknown functions that binds to curved DNA in vitro in the fission yeast Schizosaccharomyces pombe. Homologues of Cdb4 were identified in a wide range of eukaryotes, including human Ebp1. Both S. pombe Cdb4 and human Ebp1 are nonpeptidase members of the methionine aminopeptidase family. It has been reported that Ebp1 homologues are involved in cell growth regulation and differentiation. However, opposing functions have also been considered and debated upon, and the precise biological functions of this conserved protein are largely unknown. S. pombe cdb4 is a nonessential gene, and no obvious phenotypes have been detected in cells with cdb4 gene deletion. In this study, we identified nup184, encoding a component of the nuclear pore complex, as a gene responsible for the synthetic lethal phenotype associated with cdb4. Furthermore, the synthetic lethal phenotype of Cdb4 was suppressed by over-expression of human Ebp1, suggesting that it has conserved crucial functions in S. pombe Cdb4 and human Ebp1. This synthetic lethal phenotype associated with Cdb4 and Nup184 provides a molecular genetics tool to study the functions of S. pombe Cdb4 and its conserved members of proteins, including human Ebp1.","doi":"10.1111/gtc.12757","authors":"Osemwenkhae OP, Sakuno T, Hirano Y, Asakawa H, Hayashi-Takanaka Y, Haraguchi T, Hiraoka Y","authors_abbrev":"Osemwenkhae OP et al.","pubmed_publication_date":"Apr 2020","pubmed_entrez_date":"2020-02-13","publication_year":"2020","canto_session_key":"eeb535d880fd6e98","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP27G11.10c","SPAC23H4.09","SPAC6G9.15c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:11274192","title":"Identification of a novel high affinity copper transport complex in the fission yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 2001 Jun 08;276(23):20529-35","abstract":"Copper is an essential nutrient that serves as a co-factor for enzymes involved in critical cellular processes including energy generation, peptide hormone maturation, oxidative stress protection, and iron homeostasis. Although genes have been identified from yeast and mammals encoding a homologous subunit of a plasma membrane high affinity copper transporter, the presence of additional subunits that function as part of a copper transport complex has not been reported. We observed that ctr4(+), a previously identified copper transport protein from the fission yeast Schizosaccharomyces pombe, fails to complement bakers' yeast cells defective in high affinity copper transport and fails to be targeted to the plasma membrane. However, selection for S. pombe genes, which, when co-expressed with Ctr4, confer high affinity copper transport to S. cerevisiae cells resulted in the identification of ctr5(+). Both Ctr4 and Ctr5 are integral membrane proteins, are co-regulated by copper levels and the copper-sensing transcription factor Cuf1, physically associate in vivo, are interdependent for secretion to the plasma membrane, and are each essential for high affinity copper transport. These studies in S. pombe identify Ctr4 and Ctr5 as components of a novel eukaryotic heteromeric plasma membrane complex that is essential for high affinity copper transport.","authors":"Zhou H, Thiele DJ","authors_abbrev":"Zhou H et al.","pubmed_publication_date":"08 Jun 2001","pubmed_entrez_date":"2001-03-29","publication_year":"2001","canto_session_key":"e5c9525f47b835c5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-31 14:43:56","canto_approved_date":"2026-03-13 17:11:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-14 15:53:15","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1142.05","SPAC31A2.11c","SPCC1393.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-03-31"},{"uniquename":"PMID:40093821","title":"Loss of  epe1  +   extends chronological lifespan in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2025;2025","abstract":"Aging is a complex phenomenon that is characterized by the altered regulation of various biological processes over time. One of these, epigenetics, play a crucial role throughout the different stages of eukaryotic life and its alteration is considered a key molecular hallmark of aging. However, the epigenetic factors which are important for lifespan control remain elusive. Here, we used  S. pombe  as a model organism to study the epigenetic basis of aging. Our study reveals that loss of the  epe1  + gene, encoding for the JmjC domain protein Epe1 , extends chronological lifespan and increases H3K9me3 in aged  S. pombe  cells  . ","doi":"10.17912/micropub.biology.001507","authors":"Basu S, Xu Y, Vo T","authors_abbrev":"Basu S et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-03-17","publication_year":"2025","canto_session_key":"9b08e4a8102fdd6a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tommy Vo","canto_first_approved_date":"2025-04-10 14:02:12","canto_approved_date":"2025-04-10 14:02:12","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-09 04:52:40","canto_added_date":"2025-03-18 00:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Tommy Vo","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.16c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-04-10"},{"uniquename":"PMID:9542324","title":"The molecular biology and pyridoxine responsiveness of X-linked sideroblastic anaemia.","citation":"Haematologica 1998 Jan;83(1):56-70","abstract":"Pyridoxine-responsive, X-linked sideroblastic anaemia (XLSA) has been shown to be caused by missense mutations in the erythroid-specific ALA synthase gene, ALAS2. These are scattered widely across the part of the gene encoding the catalytic domain and in half the cases affect residues conserved throughout evolution. Only a loose correlation has been found between the in vitro kinetics and stability of the catalytic activity of the recombinant variant enzymes and the in vivo severity and pyridoxine-responsiveness of the anaemia. Enhanced instability in the absence of pyridoxal phosphate (PLP) or decreased PLP and substrate binding have been noted. A detailed explanation of the anaemia and its response to pyridoxine, however, requires greater insight into the structure-function relationships of this protein than we have at present. Knowledge of its tertiary structure and further knowledge of intracellular factors which impinge on the ability of normal and variant ALAS2 to contribute to haemoglobin production are also required. Mutations in the same gene which affect mitochondrial processing, terminate translation prematurely, or are thought to abolish function altogether cause an XLSA that is refractory to treatment with pyridoxine. A major complication of this disorder is its accompanying increased iron absorption and iron overload which occurs in patients and female heterozygotes. Mutation detection enables the early diagnosis of those affected, targeted education of families, early treatment with pyridoxine and prevention of iron overload. It also allows for a distinction to be made between late-onset variants of this condition and the more insidious refractory anaemia with ring sideroblasts. The next few years of investigation should be illuminating as tools now exist to study all aspects of this protein from the gene to the mitochondrial matrix.","authors":"May A, Bishop DF","authors_abbrev":"May A et al.","pubmed_publication_date":"Jan 1998","pubmed_entrez_date":"1998-05-16","publication_year":"1998","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F3.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38917328","title":"SUMO protease and proteasome recruitment at the nuclear periphery differently affect replication dynamics at arrested forks.","citation":"Nucleic Acids Res 2024 Jun 25;","abstract":"Nuclear pore complexes (NPCs) have emerged as genome organizers, defining a particular nuclear compartment enriched for SUMO protease and proteasome activities, and act as docking sites for the repair of DNA damage. In fission yeast, the anchorage of perturbed replication forks to NPCs is an integral part of the recombination-dependent replication restart mechanism (RDR) that resumes DNA synthesis at terminally dysfunctional forks. By mapping DNA polymerase usage, we report that SUMO protease Ulp1-associated NPCs ensure efficient initiation of restarted DNA synthesis, whereas proteasome-associated NPCs sustain the progression of restarted DNA polymerase. In contrast to Ulp1-dependent events, this last function is not alleviated by preventing SUMO chain formation. By analyzing the role of the nuclear basket, the nucleoplasmic extension of the NPC, we reveal that the activities of Ulp1 and the proteasome cannot compensate for each other and affect the dynamics of RDR in distinct ways. Our work probes two distinct mechanisms by which the NPC environment ensures optimal RDR, both controlled by different NPC components.","doi":"10.1093/nar/gkae526","authors":"Schirmeisen K, Naiman K, Fréon K, Besse L, Chakraborty S, Saada AA, Carr AM, Kramarz K, Lambert SAE","authors_abbrev":"Schirmeisen K et al.","pubmed_publication_date":"25 Jun 2024","pubmed_entrez_date":"2024-06-25","publication_year":"2024","canto_session_key":"a40d7474e17bb4c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Lambert","canto_first_approved_date":"2024-08-02 09:39:25","canto_approved_date":"2026-06-26 11:06:50","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-15 10:24:04","canto_added_date":"2024-06-25 23:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":27,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Sarah Lambert","community_curator":true,"annotation_count":28,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.06","SPAC1805.04","SPAC637.10c","SPBC19G7.09","SPCC285.13c","SPAC30D11.04c","SPAC1486.04c","SPAC1786.03","SPCC18B5.07c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2024-08-02"},{"uniquename":"PMID:39387272","title":"The DNA Damage Repair Function of Fission Yeast CK1 Involves Targeting Arp8, a Subunit of the INO80 Chromatin Remodeling Complex.","citation":"Mol Cell Biol 2024 Oct 10;:1-15","abstract":"The CK1 family are conserved serine/threonine kinases with numerous substrates and cellular functions. The fission yeast CK1 orthologues Hhp1 and Hhp2 were first characterized as regulators of DNA repair, but the mechanism(s) by which CK1 activity promotes DNA repair had not been investigated. Here, we found that deleting Hhp1 and Hhp2 or inhibiting CK1 catalytic activities in yeast or in human cells increased double-strand breaks (DSBs). The primary pathways to repair DSBs, homologous recombination and nonhomologous end joining, were both less efficient in cells lacking Hhp1 and Hhp2 activity. To understand how Hhp1 and Hhp2 promote DNA damage repair, we identified new substrates of these enzymes using quantitative phosphoproteomics. We confirmed that Arp8, a component of the INO80 chromatin remodeling complex, is a bona fide substrate of Hhp1 and Hhp2 important for DNA repair. Our data suggest that Hhp1 and Hhp2 facilitate DNA repair by phosphorylating multiple substrates, including Arp8.","doi":"10.1080/10985549.2024.2408016","authors":"Cullati SN, Akizuki K, Shan Y, Zhang E, Ren L, Guillen RX, Turner LA, Chen JS, Navarrete-Perea J, Elmore ZC, Gygi SP, Gould KL","authors_abbrev":"Cullati SN et al.","pubmed_publication_date":"10 Oct 2024","pubmed_entrez_date":"2024-10-10","publication_year":"2024","canto_session_key":"316171a7a08d7ce8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kazutoshi Akizuki","canto_first_approved_date":"2024-12-17 15:50:40","canto_approved_date":"2024-12-17 15:50:41","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-12-12 20:42:29","canto_added_date":"2024-10-14 23:25:09","annotation_curators":[{"name":"Kazutoshi Akizuki","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":65,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC3H7.15","SPAC29B12.01","SPBC216.05","SPAC23C4.12","SPAC664.02c","SPCC1259.13","SPCC18B5.11c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2024-12-17"},{"uniquename":"PMID:16896214","title":"Spo5/Mug12, a putative meiosis-specific RNA-binding protein, is essential for meiotic progression and forms Mei2 dot-like nuclear foci.","citation":"Eukaryot Cell 2006 Aug;5(8):1301-13","abstract":"We report here a functional analysis of spo5(+)(mug12(+)) of Schizosaccharomyces pombe, which encodes a putative RNA-binding protein. The disruption of spo5(+) caused abnormal sporulation, generating inviable spores due to failed forespore membrane formation and the absence of a spore wall, as determined by electron microscopy. Spo5 regulates the progression of meiosis I because spo5 mutant cells display normal premeiotic DNA synthesis and the timely initiation of meiosis I but they show a delay in the peaking of cells with two nuclei, abnormal tyrosine 15 dephosphorylation of Cdc2, incomplete degradation of Cdc13, retarded formation and repair of double strand breaks, and a reduced frequency of intragenic recombination. Immunostaining showed that Spo5-green fluorescent protein (GFP) appeared in the cytoplasm at the horsetail phase, peaked around the metaphase I to anaphase I transition, and suddenly disappeared after anaphase II. Images of Spo5-GFP in living cells revealed that Spo5 forms a dot in the nucleus at prophase I that colocalized with the Mei2 dot. Unlike the Mei2 dot, however, the Spo5 dot was observed even in sme2Delta cells. Taken together, we conclude that Spo5 is a novel regulator of meiosis I and that it may function in the vicinity of the Mei2 dot.","authors":"Kasama T, Shigehisa A, Hirata A, Saito TT, Tougan T, Okuzaki D, Nojima H","authors_abbrev":"Kasama T et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-10","publication_year":"2006","canto_session_key":"2a809a0d2e35ee91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-09 16:26:32","canto_approved_date":"2026-01-04 17:27:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-21 08:33:20","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC825.03c","SPBC11B10.09","SPBC29A10.02","SPAC4G9.05","SPCC1682.08c"],"gene_count":5,"ltp_gene_count":1,"approved_date":"2018-03-09"},{"uniquename":"PMID:17595166","title":"4-Methyl sterols regulate fission yeast SREBP-Scap under low oxygen and cell stress.","citation":"J Biol Chem 2007 Aug 17;282(33):24388-96","abstract":"In fission yeast, orthologs of mammalian SREBP and Scap, called Sre1 and Scp1, monitor oxygen-dependent sterol synthesis as a measure of cellular oxygen supply. Under low oxygen conditions, sterol synthesis is inhibited, and Sre1 cleavage is activated. However, the sterol signal for Sre1 activation is unknown. In this study, we characterized the sterol signal for Sre1 activation using a combination of Sre1 cleavage assays and gas chromatography sterol analysis. We find that Sre1 activation is regulated by levels of the 4-methyl sterols 24-methylene lanosterol and 4,4-dimethylfecosterol under conditions of low oxygen and cell stress. Both increases and decreases in the level of these ergosterol pathway intermediates induce Sre1 proteolysis in a Scp1-dependent manner. The SREBP ortholog in the pathogenic fungus Cryptococcus neoformans is also activated by high levels of 4-methyl sterols, suggesting that this signal for SREBP activation is conserved among unicellular eukaryotes. Finally, we provide evidence that the sterol-sensing domain of Scp1 is important for regulating Sre1 proteolysis. The conserved mutations Y247C, L264F, and D392N in Scp1 that render Scap insensitive to sterols cause constitutive Sre1 activation. These findings indicate that unlike Scap, fission yeast Scp1 responds to 4-methyl sterols and thus shares properties with mammalian HMG-CoA reductase, a sterol-sensing domain protein whose degradation is regulated by the 4-methyl sterol lanosterol.","authors":"Hughes AL, Lee CY, Bien CM, Espenshade PJ","authors_abbrev":"Hughes AL et al.","pubmed_publication_date":"17 Aug 2007","pubmed_entrez_date":"2007-06-28","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31465495","title":"Crystal structure of L-aspartate aminotransferase from Schizosaccharomyces pombe.","citation":"PLoS One 2019;14(8):e0221975","abstract":"L-aspartate aminotransferase is a pyridoxal 5'-phosphate-dependent transaminase that catalyzes reversible transfer of an α-amino group from aspartate to α-ketoglutarate or from glutamate to oxaloacetate. L-aspartate aminotransferase not only mediates amino acid and carbohydrate metabolism but also regulates the cellular level of amino acids by catalyzing amino acid degradation and biosynthesis. To expand our structural information, we determined the crystal structure of L-aspartate aminotransferase from Schizosaccharomyces pombe at 2.1 Å resolution. A structural comparison between two yeast L-aspartate aminotransferases revealed conserved enzymatic mechanism mediated by the open-closed conformational change. Compared with higher eukaryotic species, L-aspartate aminotransferases showed distinguishable inter-subunit interaction between the N-terminal arm and a large domain of the opposite subunit. Interestingly, structural homology search showed varied conformation of the N-terminal arm among 71 structures of the family. Therefore, we classified pyridoxal 5'-phosphate-dependent enzymes into eight subclasses based on the structural feature of N-terminal arms. In addition, structure and sequence comparisons showed strong relationships among the eight subclasses. Our results may provide insights into structure-based evolutionary aspects of pyridoxal 5'-phosphate-dependent enzymes.","doi":"10.1371/journal.pone.0221975","authors":"Jeong SY, Jin H, Chang JH","authors_abbrev":"Jeong SY et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-08-30","publication_year":"2019","canto_session_key":"efa1fecea755653b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-25 18:24:10","canto_approved_date":"2019-11-25 18:24:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-25 18:24:03","canto_added_date":"2019-08-31 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC10F6.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-25","pdb_entries":[{"pdb_id":"6jpk","gene_chains":[{"gene_uniquename":"SPAC10F6.13c","chain":"A/B","position":"1-409"}],"title":"Crystal structure of S. pombe aspartate aminotransferase","entry_authors":"Jin H,Chang JH","entry_authors_abbrev":"Jin H et al.","reference_uniquename":"PMID:31465495","experimental_method":"X-ray","resolution":"2.102"}]},{"uniquename":"PMID:1532582","title":"Purification and complete sequence of a small proteolipid associated with the plasma membrane H(+)-ATPase of Saccharomyces cerevisiae.","citation":"J Biol Chem 1992 Mar 25;267(9):6425-8","abstract":"The purified plasma membrane H(+)-ATPase of Schizosaccharomyces pombe and Saccharomyces cerevisiae display, in addition to the catalytic subunit of 100 kDa, a highly mobile component, soluble in chloroform/methanol. Chloroform/methanol extraction of S. cerevisiae plasma membranes led to isolation of a low molecular weight proteolipid identical to that present in purified H(+)-ATPase. NH2-terminal amino acid sequencing revealed a 38-residue polypeptide with a calculated molecular mass of 4250 Da. The polypeptide lacks the first two NH2-terminal amino acids as compared with the deduced sequence of the PMP1 gene (for plasma membrane proteolipid) isolated by hybridization with an oligonucleotide probe corresponding to an internal amino acid sequence of the proteolipid. The polypeptide is predicted to contain an NH2-terminal transmembrane segment followed by a very basic hydrophilic domain.","authors":"Navarre C, Ghislain M, Leterme S, Ferroud C, Dufour JP, Goffeau A","authors_abbrev":"Navarre C et al.","pubmed_publication_date":"25 Mar 1992","pubmed_entrez_date":"1992-03-25","publication_year":"1992","canto_session_key":"a5714cb89fb66cc8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-12-01 13:36:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-30 13:16:30","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1071.10c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-11-30"},{"uniquename":"PMID:31040179","title":"Mitochondria export iron-sulfur and sulfur intermediates to the cytoplasm for iron-sulfur cluster assembly and tRNA thiolation in yeast.","citation":"J Biol Chem 2019 Jun 14;294(24):9489-9502","abstract":"Iron-sulfur clusters are essential cofactors of proteins. In eukaryotes, iron-sulfur cluster biogenesis requires a mitochondrial iron-sulfur cluster machinery (ISC) and a cytoplasmic iron-sulfur protein assembly machinery (CIA). Here we used mitochondria and cytoplasm isolated from yeast cells, and [ 35 S]cysteine to detect cytoplasmic Fe- 35 S cluster assembly on a purified apoprotein substrate. We showed that mitochondria generate an intermediate, called (Fe-S) int , needed for cytoplasmic iron-sulfur cluster assembly. The mitochondrial biosynthesis of (Fe-S) int  required ISC components such as Nfs1 cysteine desulfurase, Isu1/2 scaffold, and Ssq1 chaperone. Mitochondria then exported (Fe-S) int  via the Atm1 transporter in the inner membrane, and we detected (Fe-S) int  in active form. When (Fe-S) int  was added to cytoplasm, CIA utilized it for iron-sulfur cluster assembly without any further help from the mitochondria. We found that both iron and sulfur for cytoplasmic iron-sulfur cluster assembly originate from the mitochondria, revealing a surprising and novel mitochondrial role. Mitochondrial (Fe-S) int  export was most efficient in the presence of cytoplasm containing an apoprotein substrate, suggesting that mitochondria respond to the cytoplasmic demand for iron-sulfur cluster synthesis. Of note, the (Fe-S) int  is distinct from the sulfur intermediate called S int , which is also made and exported by mitochondria but is instead used for cytoplasmic tRNA thiolation. In summary, our findings establish a direct and vital role of mitochondria in cytoplasmic iron-sulfur cluster assembly in yeast cells.","doi":"10.1074/jbc.RA119.008600","authors":"Pandey AK, Pain J, Dancis A, Pain D","authors_abbrev":"Pandey AK et al.","pubmed_publication_date":"14 Jun 2019","pubmed_entrez_date":"2019-05-02","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15A10.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7924618","title":"Analysis of Schizosaccharomyces pombe mitochondrial DNA replication by two dimensional gel electrophoresis.","citation":"Chromosoma 1994 Jun;103(3):162-70","abstract":"The entire mitochondrial genome of Schizosaccharomyces pombe ura4-294h- was analyzed by the 2D pulsed field gel electrophoresis technique developed by Brewer and Fangman. The genome consists of multimers with an average size of 100 kb and analysis of the overlapping restriction fragments of the complete mitochondrial DNA (mtDNA) genome resulted in simple Y 2D gel patterns. Large single-stranded DNA molecules or double-stranded DNA molecules containing large or numerous single-stranded regions were found in the S. pombe mtDNA preparation. The replication of mtDNA monomers was found to occur in either direction. On the basis of these results, a replication mechanism for S. pombe mtDNA that is most consistent with a rolling circle model is suggested.","authors":"Han Z, Stachow C","authors_abbrev":"Han Z et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D76431","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31826924","title":"Interactions between the 5' UTR mRNA of the  spe2  gene and spermidine regulate translation in  S. pombe .","citation":"RNA 2020 Feb;26(2):137-149","abstract":"The 5' untranslated regions (5' UTR) of mRNAs play an important role in the eukaryotic translation initiation process. Additional levels of translational regulation may be mediated through interactions between structured mRNAs that can adopt interchangeable secondary or tertiary structures and the regulatory protein/RNA factors or components of the translational apparatus. Here we report a regulatory function of the 5' UTR mRNA of the  spe2  gene (SAM decarboxylase) in polyamine metabolism of the fission yeast  Schizosaccharomyces pombe  Reporter assays, biochemical experiments, and mutational analysis demonstrate that this 5' UTR mRNA of  spe2  can bind to spermidine to regulate translation. A tertiary structure transition in the 5' UTR RNA upon spermidine binding is essential for translation regulation. This study provides biochemical evidence for spermidine binding to regulate translation of the  spe2  gene through interactions with the 5' UTR mRNA. The identification of such a regulatory RNA that is directly associated with an essential eukaryotic metabolic process suggests that other ligand-binding RNAs may also contribute to eukaryotic gene regulation.","doi":"10.1261/rna.072975.119","authors":"Sun W, Zhang X, Chen D, Murchie AIH","authors_abbrev":"Sun W et al.","pubmed_publication_date":"Feb 2020","pubmed_entrez_date":"2019-12-13","publication_year":"2020","canto_session_key":"bf24864f1f31947a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18546112","title":"Measurements and models of synchronous growth of fission yeast induced by temperature oscillations.","citation":"Biotechnol Bioeng 1982 Jan;24(1):217-36","abstract":"Pulsing of temperature in a fermentor at intervals coincident with cell generation time was used to induce synchrony in a population of the fission yeast Schizosaccharomyces pombe. Measurements of culture protein, RNA, and DNA during synchronous growth confirm continuous synthesis of protein and RNA and discontinuous synthesis of DNA as previously reported. Flow microfluorometry of populations at different times during the synchrony cycle was used to monitor the changes in single-cell protein. RNA, and DNA frequency functions. These measurements illustrate very clearly the degree of synchrony and patterns of macromolecular synthesis and also confirm previous estimates of the cellular protein contents characteristic of dividing cells. Additional insights into single-cell kinetics and division controls are provided by two-parameter flow microfluorometry measurements and by mathematical modeling of population dynamics. Such data are necessary foundations for robust population balance models of microbial processes.","authors":"Agar DW, Bailey JE","authors_abbrev":"Agar DW et al.","pubmed_publication_date":"Jan 1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD199","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15809658","title":"Methylation: lost in hydroxylation?","citation":"EMBO Rep 2005 Apr;6(4):315-20","abstract":"Methylation of histone tails is a key determinant in forming active and silent states of chromatin. Histone methylation was regarded as irreversible until the recent identification of a lysine-specific histone demethylase (LSD1), which acts specifically on mono- and dimethylated histone H3 lysine 4. Here, we propose that the fission yeast protein Epe1 is a putative histone demethylase that could act by oxidative demethylation. Epe1 modulates the stability of silent chromatin and contains a JmjC domain. The Epe1 protein can be modelled onto the structure of the 2-oxoglutarate-Fe(II)-dependent dioxygenase, factor inhibiting hypoxia inducible factor (FIH), which is a protein hydroxylase that also contains a JmjC domain. Thus, Epe1 and certain other chromatin-associated JmjC-domain proteins may be protein hydroxylases that catalyse a novel histone modification. Another intriguing possibility is that, by hydroxylating the methyl groups, Epe1 and certain other JmjC-domain proteins may be able to demethylate mono-, di- or trimethylated histones.","authors":"Trewick SC, McLaughlin PJ, Allshire RC","authors_abbrev":"Trewick SC et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-04-06","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17802953","title":"Method for protein tagging in Schizosaccharomyces pombe.","citation":"Rev Med Chir Soc Med Nat Iasi 2006;110(2):403-8","abstract":"Tagging is a useful method for the investigation of proteins. It allows the localization of the proteins in the cell, their purification in order to investigate their function and the determination of their expression. The aim of the present study was to tag the Rad32 protein of fission yeast (which is the homologue of Mre11 protein from humans) at its N-terminus. Rad32p as well as Mre11p are involved in the repair of DNA double strand breaks and in the DNA damage checkpoint. We carried out this tagging using the Cre-loxp recombination system. In a first step, a 2 kb DNA fragment was integrated upstream of the initiating codon of rad32 gene. This fragment encoded the TAP-tag (tandem affinity purification), a loxp site, a selectable marker (sup3-5), an exogenous promoter (nmt1) and a second loxp site, in this sequence. Following transformation of this DNA fragment into S. pombe cells, rad32 was under the control of the artificial promotor, which allows a controlled expression of the gene by thiamine. In a second step, the cells were transformed with a plasmid coding for Cre recombinase, which catalyses the excision of the DNA sequence between the two loxp sites, removing the marker and the artificial promotor. Thus the tag became attached to the rad32 gene upstream of the ATG, placing the gene under the control of its native promotor. The strain thus obtained will be subsequently used for evidencing the tagged protein by Western blotting and then for its purification in order to investigate its function.","authors":"Petrescu-Dănilă E, Voicu PM, Poiţelea M, Stoica B, Stănescu R, Rusu M","authors_abbrev":"Petrescu-Dănilă E et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-09-07","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19334523","title":"[Exon-intron structure of genes of fungi genomes].","citation":"Mol Biol (Mosk) 2009;43(1):28-35","abstract":"Objects of research--genes of A. fumigatus, C. glabrata, C. neoformans, D. hansenii, E. cuniculi, E. gossypii, K. lactis, M. grisea, N. crassa, S. cerevisiae, S. pombe, U. maydis and Y. lipolytica fungi genomes. Methods of research are computer calculation. The content of genes with exon-intron structure in fungi genomes are from 0.7 to 97.0%. The exon-intron gene structure was changed when the portion of genes with introns increased. In A. fumigatus, C. neoformans, M. grisea, N. crassa, S. pombe and U. maydis genomes that linear dependence between gene lengths, sum of exon lengths and intron number in genes was established.","authors":"Ivashchenko AT, Tauasarova MK, Atambaeva ShA","authors_abbrev":"Ivashchenko AT et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-04-02","publication_year":"2009","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF127914","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19129247","title":"Development of valuable yeast strains using a novel mutagenesis technique for the effective production of therapeutic glycoproteins.","citation":"Glycobiology 2009 Apr;19(4):428-36","abstract":"Yeast cells producing mammalian-type N-linked oligosaccharide show severe growth defects and the decreased protein productivity because of the disruption of yeast-specific glycosyltransferases. This decreased protein productivity in engineered yeast strains is an obstacle to the development of efficient glycoprotein production in yeast. For economic and effective synthesis of such therapeutic glycoproteins in yeast, the development of appropriate strains is highly desirable. We applied a novel mutagenesis technique that utilized the proofreading-deficient DNA polymerase delta variant encoded by the pol3-01 gene of Saccharomyces cerevisiae or the cdc6-1 gene of Schizosaccharomyces pombe to the engineered S. cerevisiae TIY20 strain and S. pombe KT97 strain, respectively. TIY20, which is deficient in the outer chain of mannan due to the disruption of three genes (och1Delta, mnn1 Delta, mnn4 Delta), and KT97, which is an och1 disruptant, are impractical as hosts for the production of therapeutic glycoproteins since they show a temperature-sensitive (ts) phenotype, a growth defect phenotype, and decreased protein productivity. We successfully isolated YAB mutants that alleviated the growth defect of the TIY20 strain. Surprisingly, these mutants generally secreted foreign proteins better than the wild-type strain. Furthermore, we successfully isolated YPAB mutants that alleviated the growth defect of the KT97 strain, too. The development of these new mutants by the combination of genetic engineering of yeast and this mutagenesis technique are major breakthroughs for the production of therapeutic glycoproteins in engineered yeast cells.","doi":"10.1093/glycob/cwn157","authors":"Abe H, Takaoka Y, Chiba Y, Sato N, Ohgiya S, Itadani A, Hirashima M, Shimoda C, Jigami Y, Nakayama K","authors_abbrev":"Abe H et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-01-09","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011494","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9001228","title":"A fission yeast homolog of CDC20/p55CDC/Fizzy is required for recovery from DNA damage and genetically interacts with p34cdc2.","citation":"Mol Cell Biol 1997 Feb;17(2):742-50","abstract":"Successful recovery from DNA damage requires coordination of several biological processes. Eukaryotic cell cycle progression is delayed when the cells encounter DNA-damaging agents. This cell cycle delay allows the cells to cope with DNA damage by utilizing DNA repair enzymes. Thus, at least two processes, induction of the cell cycle delay and repair of damaged DNA, are coordinately required for recovery. In this study, a fission yeast rad mutant (slp1-362) was genetically investigated. In response to radiation, slp1 stops cell division; however, it does not restart it. This defect is suppressed when slp1-362 is combined with wee1-50 or cdc2-3w; in these mutants, the onset of mitosis is advanced due to the premature activation of p34cdc2. In contrast, slp1 is synthetically lethal with cdc25, nim1/cdr1, or cdr2, all of which are unable to activate the p34cdc2 kinase correctly. These genetic interactions of slp1 with cdc2 and its modulators imply that slp1 is not defective in either \"induction of cell cycle delay\" or \"DNA repair.\" slp1+ may be involved in a critical process which restarts cell cycle progression after the completion of DNA repair. Molecular cloning of slp1+ revealed that slp1+ encodes a putative 488-amino-acid polypeptide exhibiting significant homology to WD-domain proteins, namely, CDC20 (budding yeast), p55CDC (human), and Fizzy (fly). A possible role of slp1+ is proposed.","authors":"Matsumoto T","authors_abbrev":"Matsumoto T","pubmed_publication_date":"Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPAC24H6.05","SPAC821.08c","SPAC644.06c","SPAC6F12.15c","SPCC18B5.03","SPBC216.05","SPBC11B10.09"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:5519686","title":"UV-sensitivity of the wild-type and different UVS mutants of Schizosaccharomyces pombe.","citation":"Mutat Res 1970 Nov;10(5):415-26","abstract":"","authors":"Fabre F","authors_abbrev":"Fabre F","pubmed_publication_date":"Nov 1970","pubmed_entrez_date":"1970-11-01","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20721547","title":"Effects of calorie restriction on life span of microorganisms.","citation":"Appl Microbiol Biotechnol 2010 Oct;88(4):817-28","abstract":"Calorie restriction (CR) in microorganisms such as budding and fission yeasts has a robust and well-documented impact on longevity. In order to efficiently utilize the limited energy during CR, these organisms shift from primarily fermentative metabolism to mitochondrial respiration. Respiration activates certain conserved longevity factors such as sirtuins and is associated with widespread physiological changes that contribute to increased survival. However, the importance of respiration during CR-mediated longevity has remained controversial. The emergence of several novel metabolically distinct microbial models for longevity has enabled CR to be studied from new perspectives. The majority of CR and life span studies have been conducted in the primarily fermentative Crabtree-positive yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, but studies in primarily respiratory Crabtree-negative yeast and obligate aerobes can offer complementary insight into the more complex mammalian response to CR. Not only are microorganisms helping characterize a conserved cellular mechanism for CR-mediated longevity, but they can also directly impact mammalian metabolism as part of the natural gut flora. Here, we discuss the contributions of microorganisms to our knowledge of CR and longevity at the level of both the cell and the organism.","doi":"10.1007/s00253-010-2824-8","authors":"Skinner C, Lin SJ","authors_abbrev":"Skinner C et al.","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2010-08-20","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37039135","title":"Cdc42 prevents precocious Rho1 activation during cytokinesis in a Pak1-dependent manner.","citation":"J Cell Sci 2023 Apr 15;136(8)","abstract":"During cytokinesis, a series of coordinated events partition a dividing cell. Accurate regulation of cytokinesis is essential for proliferation and genome integrity. In fission yeast, these coordinated events ensure that the actomyosin ring and septum start ingressing only after chromosome segregation. How cytokinetic events are coordinated remains unclear. The GTPase Cdc42 promotes recruitment of certain cell wall-building enzymes whereas the GTPase Rho1 activates these enzymes. We show that Cdc42 prevents early Rho1 activation during fission yeast cytokinesis. Using an active Rho probe, we find that although the Rho1 activators Rgf1 and Rgf3 localize to the division site in early anaphase, Rho1 is not activated until late anaphase, just before the onset of ring constriction. We find that loss of Cdc42 activation enables precocious Rho1 activation in early anaphase. Furthermore, we provide functional and genetic evidence that Cdc42-dependent Rho1 inhibition is mediated by the Cdc42 target Pak1 kinase. Our work proposes a mechanism of Rho1 regulation by active Cdc42 to coordinate timely septum formation and cytokinesis fidelity.","doi":"10.1242/jcs.261160","authors":"Onwubiko UN, Kalathil D, Koory E, Pokharel S, Roberts H, Mitoubsi A, Das M","authors_abbrev":"Onwubiko UN et al.","pubmed_publication_date":"15 Apr 2023","pubmed_entrez_date":"2023-04-11","publication_year":"2023","canto_session_key":"76625df886d53d47","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maitreyi Das","canto_first_approved_date":"2024-09-26 13:42:50","canto_approved_date":"2025-03-03 16:36:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-27 19:34:55","canto_added_date":"2023-04-12 00:15:04","annotation_curators":[{"name":"Maitreyi Das","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":29,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.04","SPCC645.07","SPCC645.06c","SPAC110.03","SPBC1604.14c","SPBC17F3.01c","SPAC24B11.11c","SPAC1006.06","SPAC24H6.09"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2024-09-26"},{"uniquename":"PMID:8334307","title":"The Schizosaccharomyces pombe cdc14 gene is required for septum formation and can also inhibit nuclear division.","citation":"Mol Biol Cell 1993 May;4(5):531-9","abstract":"A conditional heat-sensitive mutation in the cdc14 gene of the fission yeast Schizosaccharomyces pombe results in failure to form a septum. Cells become highly elongated and multinucleate as growth and nuclear division continue in the absence of cell division. This article describes the cloning of the cdc14 gene and the identification of its product, a protein of 240 amino acids, p28cdc14. A null allele of the cdc14 gene shows that the gene is essential for septum formation and completion of the cell-division cycle. Overexpression of the gene product, p28cdc14, causes cell-cycle arrest in late G2 before mitosis. Cells leaking past the block activate p34cdc2 kinase and show condensed chromosomes, but the normal rearrangements of the microtubules and microfilaments that are associated with the transition from interphase to mitosis do not occur. Overexpression of p28cdc14 in mutants, in which the timing of mitosis is altered, suggests that these effects may be mediated upstream of the mitotic inhibitor wee1. These data are consistent with the idea that p28cdc14 may play a role in both the initiation of mitosis and septum formation and, by doing so, be part of the mechanism that coordinates these two cell-cycle events.","authors":"Fankhauser C, Simanis V","authors_abbrev":"Fankhauser C et al.","pubmed_publication_date":"May 1993","pubmed_entrez_date":"1993-05-01","publication_year":"1993","canto_session_key":"3ae99cc2f14b317b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-11 16:00:12","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-10-11 15:59:06","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC11B10.09","SPBC24C6.07"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-10-11"},{"uniquename":"PMID:16294010","title":"Cooperation of EB1-Mal3 and the Bub1 spindle checkpoint.","citation":"Cell Cycle 2006 Jan;5(1):27-30","abstract":"EB1 is a conserved microtubule binding protein that preferentially localizes to the growing tips of the microtubule plus end. Whilst the function of EB1 in cell polarity control is well established, its role during mitosis remains largely elusive. Here we discuss our recent work of roles for Mal3, the fission yeast EB1 homologue, in mitotic progression and chromosome stability. Our analysis sheds light upon the requirement of Mal3 for bipolar microtubule attachment and its cooperative role with the spindle assembly checkpoint. In particular Mal3 collaborates with a specific branch of this checkpoint pathway, which is dependent upon Bub1, but not Mad2. As malfunctioning of the EB1-mediated pathway might be directly related to chromosome instability in some types of human cancers, a new knowledge of Mal3's mitotic role would be of direct relevance to understanding the molecular defects in these cancer cells.","authors":"Asakawa K, Toda T","authors_abbrev":"Asakawa K et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2005-11-19","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31219728","title":"Identification of proteins associated with splicing factors Ntr1, Ntr2, Brr2 and Gpl1 in the fission yeast  Schizosaccharomyces pombe .","citation":"Cell Cycle 2019 Jul;18(14):1532-1536","abstract":"The spliceosome is a complex molecular machine assembled from many components, which catalyzes the removal of introns from mRNA precursors. Our previous study revealed that the Nrl1 (NRDE-2 like 1) protein associates with spliceosome proteins and regulates pre-mRNA splicing and homologous recombination-dependent R-loop formation in the fission yeast  Schizosaccharomyces pombe . Here, we identify proteins associated with splicing factors Ntr1, Ntr2, Brr2 and Gpl1, a poorly characterized G-patch domain-containing protein required for efficient splicing. This work provides new evidence that Nrl1 and splicing factors physically interact and reveals additional insights into the protein interaction network of the spliceosome. We discuss implications of these findings in the light of recent progress in our understanding of how Nrl1 and splicing factors ensure genome stability.","doi":"10.1080/15384101.2019.1632126","authors":"Cipakova I, Jurcik M, Rubintova V, Borbova M, Mikolaskova B, Jurcik J, Bellova J, Barath P, Gregan J, Cipak L","authors_abbrev":"Cipakova I et al.","pubmed_publication_date":"Jul 2019","pubmed_entrez_date":"2019-06-21","publication_year":"2019","canto_session_key":"1816e0aa1523ef6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lubos Cipak","canto_first_approved_date":"2019-07-25 07:50:13","canto_approved_date":"2019-07-25 07:50:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-07-12 09:58:24","canto_added_date":"2019-06-22 00:15:04","annotation_curators":[{"name":"Lubos Cipak","community_curator":true,"annotation_count":186,"orcid":"0000-0001-7897-6001","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.05c","SPBC19C2.14","SPAC4F8.12c","SPAC513.01c","SPAC57A7.04c","SPCP1E11.07c","SPAC926.04c","SPBC13E7.01","SPBC11G11.06c","SPBC211.02c","SPBC1861.08c","SPAC27D7.07c","SPBC4B4.05","SPAC140.04","SPAC26A3.08","SPCC188.11","SPBC24C6.11","SPBC3E7.14","SPAC20H4.06c","SPAC30D11.09","SPAC644.12","SPAC1486.03c","SPAC17H9.02","SPBC1289.11","SPBC646.02","SPCC1739.13","SPAC9.03c","SPBC337.06c","SPBC20F10.05","SPBC713.05","SPAC17A2.08c","SPAC3A12.11c","SPAC20H4.09","SPBC6B1.10","SPCC10H11.01","SPBC32F12.11","SPBC16H5.10c","SPCC550.02c","SPAC31G5.18c","SPBC3E7.13c","SPBC1815.01","SPBC31F10.11c","SPAC1F8.07c","SPBC8D2.09c","SPBP22H7.07","SPBC215.12","SPAC29A4.08c","SPCC364.02c","SPBC28F2.04c","SPAC2C4.03c"],"gene_count":50,"ltp_gene_count":49,"approved_date":"2019-07-25"},{"uniquename":"PMID:18957202","title":"Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin.","citation":"Cell 2008 Oct 17;135(2):272-83","abstract":"In most eukaryotes, histone methylation patterns regulate chromatin architecture and function: methylation of histone H3 lysine-9 (H3K9) demarcates heterochromatin, whereas H3K4 methylation demarcates euchromatin. We show here that the S. pombe JmjC-domain protein Lid2 is a trimethyl H3K4 demethylase responsible for H3K4 hypomethylation in heterochromatin. Lid2 interacts with the histone lysine-9 methyltransferase, Clr4, through the Dos1/Clr8-Rik1 complex, which also functions in the RNA interference pathway. Disruption of the JmjC domain alone results in severe heterochromatin defects and depletion of siRNA, whereas overexpressing Lid2 enhances heterochromatin silencing. The physical and functional link between H3K4 demethylation and H3K9 methylation suggests that the two reactions act in a coordinated manner. Surprisingly, crossregulation of H3K4 and H3K9 methylation in euchromatin also requires Lid2. We suggest that Lid2 enzymatic activity in euchromatin is regulated through a dynamic interplay with other histone-modification enzymes. Our findings provide mechanistic insight into the coordination of H3K4 and H3K9 methylation.","doi":"10.1016/j.cell.2008.08.036","authors":"Li F, Huarte M, Zaratiegui M, Vaughn MW, Shi Y, Martienssen R, Cande WZ","authors_abbrev":"Li F et al.","pubmed_publication_date":"17 Oct 2008","pubmed_entrez_date":"2008-10-30","publication_year":"2008","canto_session_key":"31a2874ab03c580a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-04-23 13:46:29","canto_approved_date":"2023-03-23 14:23:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-07 20:10:19","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":49,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.11","SPAC3A11.08","SPBC428.08c","SPCC306.04c","SPCC613.12c","SPAC664.01c","SPBP19A11.06","SPBC146.09c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2020-04-23"},{"uniquename":"PMID:15282184","title":"Structural insight into the cooperativity between catalytic and noncatalytic sites of F1-ATPase.","citation":"Biochim Biophys Acta 2004 Jul 23;1658(1-2):133-40","abstract":"F1-ATPase, the catalytic sector of Fo-F1 ATPases-ATPsynthases, displays an apparent negative cooperativity for ATP hydrolysis at high ATP concentrations which involves noncatalytic and catalytic nucleotide binding sites. The molecular mechanism of such cooperativity is currently unknown. To get further insights, we have investigated the structural consequences of the single mutation of two residues: Q173L in the alpha-subunit and Q170Y in the beta-subunit of the F1-ATPase of the yeast Schizosaccharomyces pombe. These residues are localized in or near the Walker-A motifs of each subunit and their mutation produces an opposite effect on the negative cooperativity. The betaQ170 residue (M167 in beef heart) is located close to the binding site for the phosphate-Mg moiety of the nucleotide. Its replacement by tyrosine converts this site into a close state with increased affinity for the bound nucleotide and leads to an increase of negative cooperativity. In contrast, the alphaQ173L mutation (Q172 in beef heart) abolishes negative cooperativity due to the loss of two H-bonds: one stabilizing the nucleotide bound to the noncatalytic site and the other linking alphaQ173 to the adjacent betaT354, localized at the alpha(DP)-beta(TP) interface. The properties of these mutants suggest that negative cooperativity occurs through interactions between neighbor alpha- and beta-subunits. Indeed, in the beef heart enzyme, (i) the alpha(DP)-beta(TP) interface is stabilized by a vicinal alphaR171-betaD352 salt bridge (ii) betaD352 and betaT354 belong to a short peptidic stretch close to betaY345, the aromatic group of which interacts with the adenine moiety of the nucleotide bound to the catalytic site. We therefore propose that the betaY345-betaT354 stretch (beef heart numbering) constitutes a short link that drives structural modifications from a noncatalytic site to the neighbor catalytic site in which, as a result, the affinity for ADP is modulated.","authors":"Falson P, Goffeau A, Boutry M, Jault JM","authors_abbrev":"Falson P et al.","pubmed_publication_date":"23 Jul 2004","pubmed_entrez_date":"2004-07-30","publication_year":"2004","canto_session_key":"b30d4bcf66bf81ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-13 12:05:33","canto_approved_date":"2024-03-13 12:05:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-13 12:03:45","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":4,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.14","SPAC222.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-03-13"},{"uniquename":"EMBL:SPC00255","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28640807","title":"Lack of a peroxiredoxin suppresses the lethality of cells devoid of electron donors by channelling electrons to oxidized ribonucleotide reductase.","citation":"PLoS Genet 2017 Jun;13(6):e1006858","abstract":"The thioredoxin and glutaredoxin pathways are responsible of recycling several enzymes which undergo intramolecular disulfide bond formation as part of their catalytic cycles such as the peroxide scavengers peroxiredoxins or the enzyme ribonucleotide reductase (RNR). RNR, the rate-limiting enzyme of deoxyribonucleotide synthesis, is an essential enzyme relying on these electron flow cascades for recycling. RNR is tightly regulated in a cell cycle-dependent manner at different levels, but little is known about the participation of electron donors in such regulation. Here, we show that cytosolic thioredoxins Trx1 and Trx3 are the primary electron donors for RNR in fission yeast. Unexpectedly, trx1 transcript and Trx1 protein levels are up-regulated in a G1-to-S phase-dependent manner, indicating that the supply of electron donors is also cell cycle-regulated. Indeed, genetic depletion of thioredoxins triggers a DNA replication checkpoint ruled by Rad3 and Cds1, with the final goal of up-regulating transcription of S phase genes and constitutive RNR synthesis. Regarding the thioredoxin and glutaredoxin cascades, one combination of gene deletions is synthetic lethal in fission yeast: cells lacking both thioredoxin reductase and cytosolic dithiol glutaredoxin. We have isolated a suppressor of this lethal phenotype: a mutation at the Tpx1-coding gene, leading to a frame shift and a loss-of-function of Tpx1, the main client of electron donors. We propose that in a mutant strain compromised in reducing equivalents, the absence of an abundant and competitive substrate such as the peroxiredoxin Tpx1 has been selected as a lethality suppressor to favor RNR function at the expense of the non-essential peroxide scavenging function, to allow DNA synthesis and cell growth.","doi":"10.1371/journal.pgen.1006858","authors":"Boronat S, Domènech A, Carmona M, García-Santamarina S, Bañó MC, Ayté J, Hidalgo E","authors_abbrev":"Boronat S et al.","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2017-06-23","publication_year":"2017","canto_session_key":"bfd3f85ba1c4e658","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Susanna Boronat","canto_approved_date":"2017-08-08 11:50:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-07-31 11:23:58","canto_added_date":"2017-06-25 00:15:16","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":56,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Susanna Boronat","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21B10.13c","SPAC1F7.05","SPBC17A3.07","SPCC576.03c","SPCC1259.13","SPAC4F10.20","SPCC18B5.11c","SPAC22F3.10c","SPAC15E1.09","SPBC12D12.07c","SPAC7D4.07c","SPBC3F6.03","SPBC577.08c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2017-07-31"},{"uniquename":"PMID:7828917","title":"Cloning and sequence of a gene encoding the pyruvate dehydrogenase E1 beta subunit of Schizosaccharomyces pombe.","citation":"Gene 1995 Jan 11;152(1):117-20","abstract":"A 4906-bp DNA fragment, which complemented Schizosaccharomyces pombe strains partly defective in pyruvate dehydrogenase (PDH), was cloned and sequenced. The fragment contained an open reading frame (ORF) of 366 amino acids (aa), which showed 62% identity with the Saccharomyces cerevisiae gene encoding the PDH E1 beta subunit, and significant similarity to subunits from a number of other 2-oxo-acid dehydrogenase complexes from mammals, Gram+ and some Gram- bacteria. The clone hybridised to a 1.6-1.7-kb mRNA from wild type, and the 5' ends of the mRNA were mapped 73-83 bp upstream from the AUG start codon of the ORF. No other ORFs were found in this 4.9-kb segment of the Sz. pombe genome. Plasmids containing the ORF complemented the PDH-defective strains of Sz. pombe both for growth and for enzyme activity.","authors":"Cavan G, MacDonald D","authors_abbrev":"Cavan G et al.","pubmed_publication_date":"11 Jan 1995","pubmed_entrez_date":"1995-01-11","publication_year":"1995","canto_session_key":"0b3d460aeaeeeb91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-04 07:51:42","canto_approved_date":"2025-04-02 13:27:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-22 11:30:42","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-04"},{"uniquename":"PMID:15563717","title":"Survey of simple sequence repeats in completed fungal genomes.","citation":"Mol Biol Evol 2005 Mar;22(3):639-49","abstract":"The use of simple sequence repeats or microsatellites as genetic markers has become very popular because of their abundance and length variation between different individuals. SSRs are tandem repeat units of 1 to 6 base pairs that are found abundantly in many prokaryotic and eukaryotic genomes. This is the first study examining and comparing SSRs in completely sequenced fungal genomes. We analyzed and compared the occurrences, relative abundance, relative density, most common, and longest SSRs in nine taxonomically different fungal species: Aspergillus nidulans, Cryptococcus neoformans, Encephalitozoon cuniculi, Fusarium graminearum, Magnaporthe grisea, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe, and Ustilago maydis. Our analysis revealed that, in all of the genomes studied, the occurrence, abundance, and relative density of SSRs varied and was not influenced by the genome sizes. No correlation between relative abundance and the genome sizes was observed, but it was shown that N. crassa, the largest genome analyzed had the highest relative abundance of SSRs. In most genomes, mononucleotide, dinucleotide, and trinucleotide repeats were more abundant than the longer repeated SSRs. Generally, in each organism, the occurrence, relative abundance, and relative density of SSRs decreased as the repeat unit increased. Furthermore, each organism had its own common and longest SSRs. Our analysis showed that the relative abundance of SSRs in fungi is low compared with the human genome and that longer SSRs in fungi are rare. In addition to providing new information concerning the abundance of SSRs for each of these fungi, the results provide a general source of molecular markers that could be useful for a variety of applications such as population genetics and strain identification of fungal organisms.","authors":"Karaoglu H, Lee CM, Meyer W","authors_abbrev":"Karaoglu H et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2004-11-26","publication_year":"2005","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24074952","title":"Phosphorylation-dependent assembly and coordination of the DNA damage checkpoint apparatus by Rad4(TopBP1).","citation":"Mol Cell 2013 Sep 26;51(6):723-736","abstract":"The BRCT-domain protein Rad4(TopBP1) facilitates activation of the DNA damage checkpoint in Schizosaccharomyces pombe by physically coupling the Rad9-Rad1-Hus1 clamp, the Rad3(ATR) -Rad26(ATRIP) kinase complex, and the Crb2(53BP1) mediator. We have now determined crystal structures of the BRCT repeats of Rad4(TopBP1), revealing a distinctive domain architecture, and characterized their phosphorylation-dependent interactions with Rad9 and Crb2(53BP1). We identify a cluster of phosphorylation sites in the N-terminal region of Crb2(53BP1) that mediate interaction with Rad4(TopBP1) and reveal a hierarchical phosphorylation mechanism in which phosphorylation of Crb2(53BP1) residues Thr215 and Thr235 promotes phosphorylation of the noncanonical Thr187 site by scaffolding cyclin-dependent kinase (CDK) recruitment. Finally, we show that the simultaneous interaction of a single Rad4(TopBP1) molecule with both Thr187 phosphorylation sites in a Crb2(53BP1) dimer is essential for establishing the DNA damage checkpoint.","doi":"10.1016/j.molcel.2013.08.030","authors":"Qu M, Rappas M, Wardlaw CP, Garcia V, Ren JY, Day M, Carr AM, Oliver AW, Du LL, Pearl LH","authors_abbrev":"Qu M et al.","pubmed_publication_date":"26 Sep 2013","pubmed_entrez_date":"2013-10-01","publication_year":"2013","canto_session_key":"9937be178c9390b9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-09-18 15:56:11","canto_approved_date":"2022-02-23 15:00:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-11 16:13:41","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":119,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c","SPAC23C4.18c","SPCC1259.13","SPBC216.05","SPBC11B10.09","SPBC342.05","SPBC582.03"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-09-18","pdb_entries":[{"pdb_id":"4bmc","gene_chains":[{"gene_uniquename":"SPAC23C4.18c","chain":"A","position":"1-186"}],"title":"Crystal structure of s.pombe Rad4 BRCT1,2","entry_authors":"Meng Q,Rappas M,Wardlaw CP,Garcia V,Carr AM,Oliver AW,Du LL,Pearl LH","entry_authors_abbrev":"Meng Q et al.","reference_uniquename":"PMID:24074952","experimental_method":"X-ray","resolution":"1.982"},{"pdb_id":"4bu0","gene_chains":[{"gene_uniquename":"SPAC23C4.18c","chain":"A","position":"1-186"},{"gene_uniquename":"SPBC342.05","chain":"B/C","position":"180-193"}],"title":"Crystal structure of Rad4 BRCT1,2 in complex with a Crb2 phosphopeptide","entry_authors":"Qu M,Rappas M,Wardlaw CP,Garcia V,Carr AM,Oliver AW,Du LL,Pearl LH","entry_authors_abbrev":"Qu M et al.","reference_uniquename":"PMID:24074952","experimental_method":"X-ray","resolution":"1.5"},{"pdb_id":"4bmd","gene_chains":[{"gene_uniquename":"SPAC23C4.18c","chain":"A","position":"291-494"}],"title":"Crystal structure of S.pombe Rad4 BRCT3,4","entry_authors":"Meng Q,Rappas M,Wardlaw CP,Garcia V,Carr AM,Oliver AW,Du LL,Pearl LH","entry_authors_abbrev":"Meng Q et al.","reference_uniquename":"PMID:24074952","experimental_method":"X-ray","resolution":"2.5"},{"pdb_id":"4bu1","gene_chains":[{"gene_uniquename":"SPAC23C4.18c","chain":"A/B","position":"1-186"},{"gene_uniquename":"SPBC342.05","chain":"C/D","position":"229-241"}],"title":"Crystal structure of Rad4 BRCT1,2 in complex with a Crb2 phosphopeptide","entry_authors":"Qu M,Rappas M,Wardlaw CP,Garcia V,Carr AM,Oliver AW,Du LL,Pearl LH","entry_authors_abbrev":"Qu M et al.","reference_uniquename":"PMID:24074952","experimental_method":"X-ray","resolution":"2.1"}]},{"uniquename":"PMID:27746023","title":"Remodeling of the Fission Yeast Cdc42 Cell-Polarity Module via the Sty1 p38 Stress-Activated Protein Kinase Pathway.","citation":"Curr Biol 2016 Nov 07;26(21):2921-2928","abstract":"The Rho family GTPase Cdc42 is a key regulator of eukaryotic cellular organization and cell polarity [1]. In the fission yeast Schizosaccharomyces pombe, active Cdc42 and associated effectors and regulators (the \"Cdc42 polarity module\") coordinate polarized growth at cell tips by controlling the actin cytoskeleton and exocytosis [2-4]. Localization of the Cdc42 polarity module to cell tips is thus critical for its function. Here we show that the fission yeast stress-activated protein kinase Sty1, a homolog of mammalian p38 MAP kinase, regulates localization of the Cdc42 polarity module. In wild-type cells, treatment with latrunculin A, a drug that leads to actin depolymerization, induces dispersal of the Cdc42 module from cell tips and cessation of polarized growth [5, 6]. We show that latrunculin A treatment also activates the Sty1 MAP kinase pathway and, strikingly, we find that loss of Sty1 MAP kinase signaling prevents latrunculin A-induced dispersal of the Cdc42 module, allowing polarized growth even in complete absence of the actin cytoskeleton. Regulation of the Cdc42 module by Sty1 is independent of Sty1's role in stress-induced gene expression. We also describe a system for activation of Sty1 kinase \"on demand\" in the absence of any external stress, and use this to show that Sty1 activation alone is sufficient to disperse the Cdc42 module from cell tips in otherwise unperturbed cells. During nitrogen-starvation-induced quiescence, inhibition of Sty1 converts non-growing, depolarized cells into growing, polarized cells. Our results place MAP kinase Sty1 as an important physiological regulator of the Cdc42 polarity module.","doi":"10.1016/j.cub.2016.08.048","authors":"Mutavchiev DR, Leda M, Sawin KE","authors_abbrev":"Mutavchiev DR et al.","pubmed_publication_date":"07 Nov 2016","pubmed_entrez_date":"2016-10-18","publication_year":"2016","canto_session_key":"f938aca48cd3f966","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-18 15:04:56","canto_approved_date":"2024-04-02 17:20:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-18 12:43:55","canto_added_date":"2016-10-19 00:15:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC110.03","SPAC26F1.10c","SPAC19D5.01","SPAC22H10.07","SPAC24B11.06c","SPBC29B5.01","SPAC23C11.16"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2020-11-18"},{"uniquename":"EMBL:AU008358","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21680738","title":"Glucose controls phosphoregulation of hydroxymethylglutaryl coenzyme A reductase through the protein phosphatase 2A-related phosphatase protein, Ppe1, and Insig in fission yeast.","citation":"J Biol Chem 2011 Aug 05;286(31):27139-46","abstract":"HMG-CoA reductase (HMGR) catalyzes a rate-limiting step in sterol biosynthesis and is a key control point in the feedback inhibition that regulates this pathway. Through the action of the membrane protein Insig, HMGR synthesis and degradation are regulated to maintain sterol homeostasis. The fission yeast Schizosaccharomyces pombe encodes homologs of HMGR and Insig called hmg1(+) and ins1(+), respectively. In contrast to the mammalian system, Ins1 regulates Hmg1 by a nondegradative mechanism involving phosphorylation of the Hmg1 active site. Here, we investigate the role of the Ins1-Hmg1 system in coupling glucose sensing to regulation of sterol biosynthesis. We show that Ins1-dependent Hmg1 phosphorylation is strongly induced in response to glucose withdrawal and that HMGR activity is correspondingly reduced. We also find that inability to activate Hmg1 phosphorylation under nutrient limiting conditions results in overaccumulation of sterol pathway intermediates. Furthermore, we show that regulation of Hmg1 phosphorylation requires the protein phosphatase 2A-related phosphatase Ppe1 and its regulator Sds23. These results describe a mechanism by which cells tune the rate of sterol synthesis to match nutrient availability.","doi":"10.1074/jbc.M111.233452","authors":"Burg JS, Espenshade PJ","authors_abbrev":"Burg JS et al.","pubmed_publication_date":"05 Aug 2011","pubmed_entrez_date":"2011-06-18","publication_year":"2011","canto_session_key":"af743f1eacf15fc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-07 18:33:14","canto_approved_date":"2025-08-26 14:44:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-16 08:35:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC162.09c","SPCC1739.12","SPBC646.13","SPCC306.05c","SPCC1919.03c","SPCC74.03c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-09-07"},{"uniquename":"PMID:29423857","title":"Tetrad Dissection in Fission Yeast.","citation":"Methods Mol Biol 2018;1721:179-187","abstract":"Tetrad dissection is a powerful tool in yeast genetics that allows the analysis of products of a single meiosis. With just a few tetrads, it is possible to determine linkage, identify unique phenotypes associated with double mutants, or assess specific meiotic defects. Strains are crossed on nitrogen-limiting medium for 3 days. With the help of a micromanipulator, ripe asci are isolated to spots 5 mm apart on a YES plate. Incubation at 36 °C for about 3-5 h is necessary for the ascus walls to break down. Once the spores are released, they are individually placed in a row containing four tetrad products, separated by 5 mm. The spores are then put in the appropriate temperature for the cross until colonies form, and phenotypes are assessed by replica plating or microscopic analysis.","doi":"10.1007/978-1-4939-7546-4_16","authors":"Escorcia W, Forsburg SL","authors_abbrev":"Escorcia W et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1699136","title":"Distinct nuclear and spindle pole body population of cyclin-cdc2 in fission yeast.","citation":"Nature 1990 Oct 18;347(6294):680-2","abstract":"Cyclins, as subunits of the protein kinase encoded by the cdc2 gene are major controlling elements of the eukaryotic cell cycle. The fission yeast Schizosaccharomyces pombe has a B-type cyclin, which is a nuclear protein encoded by the cdc13 gene. Here we demonstrate the presence of two spatially distinct cdc13 cyclin populations in the nucleus of S. pombe, one of which is associated with the mitotic spindle poles. Both populations colocalize with the product of the cdc2 gene (p34cdc2). Treatment of cells with the antimicrotubule drug thiabendazole prevents cyclin degradation and blocks the tyrosine dephosphorylation and activation of cdc2. These results suggest a key regulatory role of the cdc2-cyclin complex in the initiation of mitotic spindle formation and also that mitotic microtubule function is required for cdc2 activation.","authors":"Alfa CE, Ducommun B, Beach D, Hyams JS","authors_abbrev":"Alfa CE et al.","pubmed_publication_date":"18 Oct 1990","pubmed_entrez_date":"1990-10-18","publication_year":"1990","canto_session_key":"5696e14c1250e01e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-22 08:03:58","canto_approved_date":"2022-09-22 08:03:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-18 07:43:01","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC11B10.09","SPAC24H6.05"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2022-09-22"},{"uniquename":"PMID:11923314","title":"A RAC protein-binding site in the internal transcribed spacer 2 of Pre-rRNA transcripts from Schizosaccharomyces pombe.","citation":"J Biol Chem 2002 Jun 14;277(24):21291-9","abstract":"The interdependence of steps in the processing of the eukaryotic preribosomal rRNA transcripts indicate that rRNA processing, at least in part, acts as a quality control mechanism to help ensure that only functional rRNA is incorporated into mature ribosomes. In search of structural components that underlie this interdependence, we have isolated a large protein complex or RAC that contains an independent binding site for all four of the transcribed spacers in the nascent pre-rRNA. In this study the RAC-binding site in the internal transcribed spacer 2 sequence of Schizosaccharomyces pombe rRNA transcripts was identified, and the influence of this site on rRNA maturation was assessed. Modification exclusion analyses indicate that the protein complex interacts with a helical domain previously shown to contain features common to both the internal transcribed spacer 1 and the 3'-external transcribed spacer. Mutagenic analyses in vitro confirm an interaction with this sequence, and parallel analyses in vivo indicated a critical role in both the maturation of the rRNA components of the large subunit as well as the 18 S rRNA component of the small subunit. Hybridization analyses also indicated greatly elevated levels of unprocessed nascent RNA. These effects are contrasted with mutations in other regions of the secondary structure that resulted in some reduction of plasmid-derived mature rRNA but no elevated levels of the precursor molecules. The significance with respect to rRNA maturation and the interdependences in rRNA processing are discussed.","authors":"Abeyrathne PD, Lalev AI, Nazar RN","authors_abbrev":"Abeyrathne PD et al.","pubmed_publication_date":"14 Jun 2002","pubmed_entrez_date":"2002-03-30","publication_year":"2002","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15569151","title":"Hub1 is an essential ubiquitin-like protein without functioning as a typical modifier in fission yeast.","citation":"Genes Cells 2004 Dec;9(12):1189-97","abstract":"Hub1 exhibits 23% sequence identity to ubiquitin. However, Hub1 lacks the C-terminal Gly, which is essential for covalent attachment to target protein(s) of ubiquitin and other ubiquitin-like (UBL) modifiers. Instead, Hub1 proteins in all eukaryotes retain the di-Tyr just before a single variable residue at the C-terminus, so one intriguing question is whether Hub1 could be linked to substrate through the conserved Tyr or not. Here we studied Hub1 in Schizosaccharomyces pombe. Gene disruption experiment revealed that hub1+ is essential. Remarkably, the mutant cells harbouring Hub1 lacking the di-Tyr could grow similar to wild-type cells, indicating that the di-Tyr is dispensable for the essential function of Hub1. Moreover, we could not observe cleavage of Flag-tag fused with C-terminus of Hub1. It suggests that the processing for conjugation via conserved Tyr is not likely to occur in Hub1, and Hub1 is a novel class of the UBL protein family. Finally, we isolated a temperature-sensitive allele, hub1-1. This temperature sensitivity could be suppressed by overproduction of Rpb10 or Snu66, the former of which is one of the common subunits of the RNA polymerases and the other is the component of the spliceosome. We also observed that pre-mRNA splicing was impaired in hub1-1.","authors":"Yashiroda H, Tanaka K","authors_abbrev":"Yashiroda H et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-12-01","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B3.12c","SPAC167.03c","SPBC31E1.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:24462781","title":"RNAi mediates post-transcriptional repression of gene expression in fission yeast Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2014 Feb 07;444(2):254-9","abstract":"RNA interference (RNAi) is a gene silencing mechanism conserved from fungi to mammals. Small interfering RNAs are products and mediators of the RNAi pathway and act as specificity factors in recruiting effector complexes. The Schizosaccharomyces pombe genome encodes one of each of the core RNAi proteins, Dicer, Argonaute and RNA-dependent RNA polymerase (dcr1, ago1, rdp1). Even though the function of RNAi in heterochromatin assembly in S. pombe is established, its role in controlling gene expression is elusive. Here, we report the identification of small RNAs mapped anti-sense to protein coding genes in fission yeast. We demonstrate that these genes are up-regulated at the protein level in RNAi mutants, while their mRNA levels are not significantly changed. We show that the repression by RNAi is not a result of heterochromatin formation. Thus, we conclude that RNAi is involved in post-transcriptional gene silencing in S. pombe.","doi":"10.1016/j.bbrc.2014.01.057","authors":"Smialowska A, Djupedal I, Wang J, Kylsten P, Swoboda P, Ekwall K","authors_abbrev":"Smialowska A et al.","pubmed_publication_date":"07 Feb 2014","pubmed_entrez_date":"2014-01-28","publication_year":"2014","canto_session_key":"9247a0d448037da0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27E2.05","SPCC188.13c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:4664534","title":"Inhibitory effect of 2-deoxy-glucose on cell wall synthesis in cells and protoplasts of Schizosaccharomyces pombe.","citation":"Z Allg Mikrobiol 1972;12(8):685-99","abstract":"","authors":"Svoboda A, Smith DG","authors_abbrev":"Svoboda A et al.","pubmed_publication_date":"1972","pubmed_entrez_date":"1972-01-01","publication_year":"1972","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24868378","title":"X-linked dystonia parkinsonism: clinical phenotype, genetics and therapeutics.","citation":"J Mov Disord 2010 Oct;3(2):32-8","abstract":"The clinical phenotype of X-Linked Dystonia Parkinsonism (XDP) is typically one that involves a Filipino adult male whose ancestry is mostly traced in the Philippine island of Panay. Dystonia usually starts focally in the lower limbs or oromandibular regions, then spreads to become generalized eventually. Parkinsonism sets in later into the disease and usually in combination with dystonia. /DYT3/ and /TAF1/ are the two genes associated with XDP. An SVA retrotransposon insertion in an intron of /TAF1/ may reduce neuron-specific expression of the /TAF1/ isoform in the caudate nucleus, and subsequently interfere with the transcription of many neuronal genes. Polypharmacy with oral benzodiazepines, anticholinergic agents and muscle relaxants leaves much to be desired in terms of efficacy. The medications to date that may appear beneficial, especially in disabling dystonias, are zolpidem, muscle afferent block with lidocaine-ethanol and botulinum toxin type A. Despite the few cases undergoing deep brain stimulation, this functional surgery has shown the greatest promise in XDP. An illustrative case of XDP in a family depicts the variable course of illness, including a bout of \"status dystonicus,\" challenges in therapy, reckoning with the social impact of the disease, and eventual patient demise. Indeed, there remains some gaps in understanding some phenomenological, genetic and treatment aspects of XDP, the areas upon which future research directions may be worthwhile.","doi":"10.14802/jmd.10009","authors":"Rosales RL","authors_abbrev":"Rosales RL","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2014-05-29","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU006521","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16453822","title":"7SL RNA from Schizosaccharomyces pombe is encoded by a single copy essential gene.","citation":"EMBO J 1988 Jan;7(1):231-7","abstract":"We have identified an abundant ribonucleoprotein particle from Schizosaccharomyces pombe with properties related to those of the vertebrate signal recognition particle (SRP), including cytoplasmic localization, association with microsomes and ribosomes at low, but not high, salt concentrations and high resistance to micrococcal nuclease. The 256-nucleotide RNA component carries a 5'-triphosphate group and shows close secondary structure, and limited primary sequence homology to vertebrate 7SL RNA. 7SL-like RNAs were also detected in a number of other fungi. The single copy gene (SRP7) encoding S.pombe 7SL was disrupted by insertion of a transposon carrying the selective marker LEU2, and the disrupted gene was used to replace one chromosomal SRP7 gene in a diploid strain. Haploid srp7[unk] strains fail to germinate.","authors":"Ribes V, Dehoux P, Tollervey D","authors_abbrev":"Ribes V et al.","pubmed_publication_date":"Jan 1988","pubmed_entrez_date":"1988-01-01","publication_year":"1988","canto_session_key":"065a5d3851a4f583","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-10-26 13:23:55","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-10 16:12:21","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.98"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-10"},{"uniquename":"PMID:34309512","title":"The loopy world of cohesin.","citation":"Elife 2021 Jul 26;10","abstract":"DNA loops can be formed by a mechanism in which the cohesin complex pulls DNA strands through its ring structure using biased Brownian motion.","doi":"10.7554/eLife.71585","authors":"Maeshima K, Iida S","authors_abbrev":"Maeshima K et al.","pubmed_publication_date":"26 Jul 2021","pubmed_entrez_date":"2021-07-26","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-07-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31321383","title":"Noncatalytic Function of a JmjC Domain Protein Disrupts Heterochromatin.","citation":"Epigenet Insights 2019;12:2516865719862249","abstract":"Chromatin-modifying enzymes are frequently overexpressed in cancer cells, and their enzymatic activities play important roles in changing the epigenetic landscape responsible for tumorigenesis. However, many of these proteins also execute noncatalytic functions, which are poorly understood. In fission yeast, overexpression of Epe1, a histone demethylase homolog, causes heterochromatin defects. Interestingly, in our recent work, we discovered that overexpressed Epe1 recruits SAGA, a histone acetyltransferase complex important for transcriptional regulation, to disrupt heterochromatin, independent of its demethylase activity. Our findings suggest that overexpressed chromatin-modifying enzymes can alter the epigenetic landscape through changing their proteomic environments, an area that needs to be further explored in dissecting disease etiology associated with overexpression of chromatin regulators.","doi":"10.1177/2516865719862249","authors":"Bao K, Jia S","authors_abbrev":"Bao K et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-07-20","publication_year":"2019","canto_session_key":"3db33cdf68115e9d","canto_annotation_status":"APPROVED","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_first_approved_date":"2023-04-05 17:27:31","canto_approved_date":"2023-09-23 10:05:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-04-05 14:39:06","canto_added_date":"2019-07-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.16c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2023-04-05"},{"uniquename":"PMID:19749351","title":"Interaction between tetraplex structure of yeast telomeric DNA and tetraplex-binding ligand.","citation":"Nucleic Acids Symp Ser (Oxf) 2009;(53):243-4","abstract":"Fission yeast telomeric DNA sequence, SP4G4: 5'-(GGGGTTAC)(4)-3' has been reported to form the antiparallel tetraplex in the presence of K(+). We examined the structural properties of budding yeast telomeric DNA sequences, SCTELG4: 5'-(TGGGTGT G)(4)-3' and SCTELGG4: 5'-(TGGGTGTGG)(4)-3', in the presence of K(+). The major conformation of SCTELG4 and SCTELGG4 was a parallel tetraplex DNA. We also examined the interaction between tetraplex-binding ligand, TMPyP4, and each of the antiparallel tetraplex of SP4G4 and the parallel tetraplex of SCTELG4 and SCTELGG4. The ability of TMPyP4 to bind with all of the tetraplexes was observed. We conclude that TMPyP4 has the ability to bind with both the parallel and antiparallel tetraplex of the telomeric DNA sequences from budding and fission yeasts.","doi":"10.1093/nass/nrp122","authors":"Torigoe H, Horio E, Takehara T, Kaneda K, Kozasa T","authors_abbrev":"Torigoe H et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-09-15","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8289788","title":"Cdc42p GTPase is involved in controlling polarized cell growth in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1994 Feb;14(2):1075-83","abstract":"Cdc42p is a highly conserved low-molecular-weight GTPase that is involved in controlling cellular morphogenesis. We have isolated the Cdc42p homolog from the fission yeast Schizosaccharomyces pombe by its ability to complement the Saccharomyces cerevisiae cdc42-1ts mutation. S. pombe Cdc42p is 85% identical in predicted amino acid sequence to S. cerevisiae Cdc42p and 83% identical to the human Cdc42p homolog. The Cdc42p protein fractionates to both soluble and particulate fractions, suggesting that it exists in two cellular pools. We have disrupted the cdc42+ gene and shown that it is essential for growth. The cdc42 null phenotype is an arrest as small, round, dense cells. In addition, we have generated three site-specific mutations, G12V, Q61L, and D118A, in the Cdc42p GTP-binding domains that correspond to dominant-lethal mutations in S. cerevisiae CDC42. In contrast to the S. cerevisiae cdc42 mutations, the S. pombe cdc42 mutant alleles were not lethal when overexpressed. However, the cdc42 mutants did exhibit an abnormal morphological phenotype of large, misshapen cells, suggesting that S. pombe Cdc42p is involved in controlling polarized cell growth.","authors":"Miller PJ, Johnson DI","authors_abbrev":"Miller PJ et al.","pubmed_publication_date":"Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:10908327","title":"Dmc1 of Schizosaccharomyces pombe plays a role in meiotic recombination.","citation":"Nucleic Acids Res 2000 Jul 15;28(14):2709-16","abstract":"We report here a Schizosaccharomyces pombe gene (dmc1(+)) that resembles budding yeast DMC1 in the region immediately upstream of the rad24(+) gene. We showed by northern and Southern blot analysis that dmc1(+) and rad24(+) are co-transcribed as a bicistronic mRNA of 2.8 kb with meiotic specificity, whereas rad24(+) itself is constitutively transcribed as a 1.0-kb mRNA species during meiosis. Induction of the bicistronic transcript is under the control of a meiosis-specific transcription factor, Ste11. Disruption of both dmc1(+) and rad24(+) had no effect on mitosis or spore formation, and dmc1Delta cells displayed no change in sensitivity to UV or gamma irradiation relative to the wild type. Tetrad analysis indicated that Dmc1 is involved in meiotic recombination. Analysis of gene conversion frequencies using single and double mutants of dmc1 and rhp51 indicated that both Dmc1 and Rhp51 function in meiotic gene conversion. These observations, together with a high level of sequence identity, indicate that the dmc1(+) gene of S. POMBE: is a structural homolog of budding yeast DMC1, sharing both similar and distinct functions in meiosis.","authors":"Fukushima K, Tanaka Y, Nabeshima K, Yoneki T, Tougan T, Tanaka S, Nojima H","authors_abbrev":"Fukushima K et al.","pubmed_publication_date":"15 Jul 2000","pubmed_entrez_date":"2000-07-25","publication_year":"2000","canto_session_key":"8dbd89752b2823d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-03-27 12:34:16","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-19 07:12:29","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPBC32C12.02","SPAC8E11.03c","SPAC644.14c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-05-19"},{"uniquename":"PMID:10394909","title":"The function of the chicken p34CDC2 protein kinase in fission yeast is cold sensitive for cell cycle progression through the G1 phase and temperature sensitive for traversal of mitosis.","citation":"Mol Gen Genet 1999 Jun;261(4-5):716-24","abstract":"The protein kinase p34cdc2 is required at the onset of DNA replication and for entry into mitosis. The catalytic subunit and its regulatory proteins, notably the cyclins, are conserved from yeast to man. This suggests that the control mechanisms necessary for progression through the cell cycle in fission yeast are conserved throughout evolution. This work describes the characterization of a fission yeast strain that is dependent for cell cycle progression on the activity of the p34CDC2 protein kinase from chicken. The response of the chicken p34CDC2 protein kinase to cell cycle components of fission yeast was examined. Cells expressing the chicken p34CDC2 protein divide at reduced size at 31 degrees C. Cells are temperature sensitive at 35.5 degrees C and die as a result of mitotic catastrophe. This phenotype can be rescued by delaying cell cycle progression at the G1-S transition by adding low concentrations of hydroxyurea. Schizosaccharomyces pombe cells that are dependent on chicken p34CDC2 are cold sensitive. At 19 degrees C to 25 degrees C cells arrest in the G1 phase, while traversal of the G2-M transition is not blocked at low temperature. Expression of chicken p34CDC2 in the cold-sensitive G2-M mutant cdc2A21 suppresses the G1 arrest.","authors":"Schmitz N","authors_abbrev":"Schmitz N","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-07-08","publication_year":"1999","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34440781","title":" ChroMo , an Application for Unsupervised Analysis of Chromosome Movements in Meiosis.","citation":"Cells 2021 Aug 06;10(8)","abstract":"Nuclear movements during meiotic prophase, driven by cytoskeleton forces, are a broadly conserved mechanism in opisthokonts and plants to promote pairing between homologous chromosomes. These forces are transmitted to the chromosomes by specific associations between telomeres and the nuclear envelope during meiotic prophase. Defective chromosome movements (CMs) harm pairing and recombination dynamics between homologues, thereby affecting faithful gametogenesis. For this reason, modelling the behaviour of CMs and their possible microvariations as a result of mutations or physico-chemical stress is important to understand this crucial stage of meiosis. Current developments in high-throughput imaging and image processing are yielding large CM datasets that are suitable for data mining approaches. To facilitate adoption of data mining pipelines, we present  ChroMo , an interactive, unsupervised cloud application specifically designed for exploring CM datasets from live imaging.  ChroMo  contains a wide selection of algorithms and visualizations for time-series segmentation, motif discovery, and assessment of causality networks. Using  ChroMo  to analyse meiotic CMs in fission yeast, we found previously undiscovered features of CMs and causality relationships between chromosome morphology and trajectory.  ChroMo  will be a useful tool for understanding the behaviour of meiotic CMs in yeast and other model organisms.","doi":"10.3390/cells10082013","authors":"León-Periñán D, Fernández-Álvarez A","authors_abbrev":"León-Periñán D et al.","pubmed_publication_date":"06 Aug 2021","pubmed_entrez_date":"2021-08-27","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-08-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012409","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:872890","title":"Controls over the timing of DNA replication during the cell cycle of fission yeast.","citation":"Exp Cell Res 1977 Jul;107(2):365-75","abstract":"","authors":"Nurse P, Thuriaux P","authors_abbrev":"Nurse P et al.","pubmed_publication_date":"Jul 1977","pubmed_entrez_date":"1977-07-01","publication_year":"1977","canto_session_key":"0d41be15f3286108","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2014-07-07 12:54:57","canto_approved_date":"2019-06-13 07:19:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-05-26 16:18:41","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jacky Hayles","community_curator":true,"annotation_count":8,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC18B5.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-07-07"},{"uniquename":"PMID:12356913","title":"Localization of the (1,3)beta-D-glucan synthase catalytic subunit homologue Bgs1p/Cps1p from fission yeast suggests that it is involved in septation, polarized growth, mating, spore wall formation and spore germination.","citation":"J Cell Sci 2002 Nov 01;115(Pt 21):4081-96","abstract":"Schizosaccharomyces pombe Bgs1p/Cps1p has been identified as a putative (1,3)beta-D-glucan synthase (GS) catalytic subunit with a possible function during cytokinesis and polarized growth. To study this possibility, double mutants of cps1-12 and cdc septation mutants were made. The double mutants displayed several hypersensitive phenotypes and altered actin distribution. Epistasis analysis showed mutations prior to septum synthesis were dominant over cps1-12, while cps1-12 was dominant over the end of septation mutant cdc16-116, suggesting Bgs1p is involved in septum cell-wall (1,3)beta-D-glucan synthesis at cytokinesis. We have studied the in vivo physiological localization of Bgs1p in a bgs1delta strain containing a functional GFP-bgs1(+) gene (integrated single copy and expressed under its own promoter). During vegetative growth, Bgs1p always localizes to the growing zones: one or both ends during cell growth and contractile ring and septum during cytokinesis. Bgs1p localization in cdc septation mutants indicates that Bgs1p needs the medial ring and septation initiation network (SIN) proteins to localize properly with the rest of septation components. Bgs1p localization in the actin mutant cps8-188 shows it depends on actin localization. In addition, Bgs1p remains polarized in the mislocalized growing poles and septa of tea1-1 and tea2-1 mutants. During the meiotic process of the life cycle, Bgs1p localizes to the mating projection, to the cell-to-cell contact zone during cell fusion and to the neck area during zygote formation. Also, Bgs1p localization suggests that it collaborates in forespore and spore wall synthesis. During spore germination, Bgs1p localizes first around the spore during isotropic growth, then to the zone of polarized growth and finally, to the medial ring and septum. At the end of spore-cell division, the Bgs1p displacement to the old end occurs only in the new cell. All these data show that Bgs1p is localized to the areas of polarized cell wall growth and so we propose that it might be involved in synthesizing the lineal (1,3)beta-D-glucan of the primary septum, as well as a similar lineal (1,3)beta-D-glucan when other processes of cell wall growth or repair are needed.","authors":"Cortés JC, Ishiguro J, Durán A, Ribas JC","authors_abbrev":"Cortés JC et al.","pubmed_publication_date":"01 Nov 2002","pubmed_entrez_date":"2002-10-03","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPAC6F6.08c"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:1703321","title":"Complementation of the mitotic activator, p80cdc25, by a human protein-tyrosine phosphatase.","citation":"Science 1990 Dec 14;250(4987):1573-6","abstract":"The onset of M phase requires the activation of the pp34 protein kinase in all eukaryotes thus far examined. In Schizosaccharomyces pombe, pp34 is phosphorylated on Tyr15, and dephosphorylation of this residue regulates the initiation of mitosis. In this study, it is shown that dephosphorylation of Tyr15 triggered activation of the pp34-cyclin complex from fission yeast, that a human protein-tyrosine phosphatase can catalyze this event both in vitro and in vivo, and that activation of fission yeast pp34 does not require threonine dephosphorylation. The complementary DNA that encoded the tyrosine phosphatase replaced the mitotic activator p80cdc25, closely associating the cdc25(+)-activating pathway with tyrosine dephosphorylation of pp34.","authors":"Gould KL, Moreno S, Tonks NK, Nurse P","authors_abbrev":"Gould KL et al.","pubmed_publication_date":"14 Dec 1990","pubmed_entrez_date":"1990-12-14","publication_year":"1990","canto_session_key":"50a71e0348432087","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-08-21 15:52:37","canto_approved_date":"2026-01-26 21:51:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-26 10:05:49","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":13,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPCC18B5.03","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-08-21"},{"uniquename":"PMID:16904908","title":"Cdc48 is required for the stability of Cut1/separase in mitotic anaphase.","citation":"J Struct Biol 2006 Oct;156(1):50-61","abstract":"Separase, a large protease essential for sister chromatid separation, cleaves the cohesin subunit Scc1/Rad21 during anaphase and leads to dissociation of the link between sister chromatids. Securin, a chaperone and inhibitor of separase, is ubiquitinated by APC/cyclosome, and degraded by 26S proteasome in anaphase. Cdc48/VCP/p97, an AAA ATPase, is involved in a variety of cellular activities, many of which are implicated in the proteasome-mediated degradation. We previously reported that temperature-sensitive (ts) fission yeast Schizosaccharomyces pombe cdc48 mutants were suppressed by multicopy plasmid carrying the cut1(+)/separase gene and that the defective mitotic phenotypes of cut1 and cdc48 were similar. We here describe characterizations of Cdc48 mutant protein and the role of Cdc48 in sister chromatid separation. Mutant residue resides in the conserved D1 domain within the central hole of hexamer, while Cdc48 mutant protein possesses the ATPase activity. Consistent with the phenotypic similarity and the rescue of cdc48 mutant by overproduced Cut1/separase, the levels of Cut1 and also Cut2 are diminished in cdc48 mutant. We show that the stability of Cut1 during anaphase requires Cdc48. Cells lose viability during the traverse of anaphase in cdc48 mutant cells. Cdc48 may protect Cut1/separase and Cut2/securin against the instability during polyubiquitination and degradation in the metaphase-anaphase transition.","authors":"Ikai N, Yanagida M","authors_abbrev":"Ikai N et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-08-15","publication_year":"2006","canto_session_key":"7338c1c2d966b6e6","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14C8.01c","SPCC5E4.04","SPAC1565.08","SPBC106.09","SPBC16G5.01"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:36690741","title":"Convolutional networks for supervised mining of molecular patterns within cellular context.","citation":"Nat Methods 2023 Feb;20(2):284-294","abstract":"Cryo-electron tomograms capture a wealth of structural information on the molecular constituents of cells and tissues. We present DeePiCt (deep picker in context), an open-source deep-learning framework for supervised segmentation and macromolecular complex localization in cryo-electron tomography. To train and benchmark DeePiCt on experimental data, we comprehensively annotated 20 tomograms of Schizosaccharomyces pombe for ribosomes, fatty acid synthases, membranes, nuclear pore complexes, organelles, and cytosol. By comparing DeePiCt to state-of-the-art approaches on this dataset, we show its unique ability to identify low-abundance and low-density complexes. We use DeePiCt to study compositionally distinct subpopulations of cellular ribosomes, with emphasis on their contextual association with mitochondria and the endoplasmic reticulum. Finally, applying pre-trained networks to a HeLa cell tomogram demonstrates that DeePiCt achieves high-quality predictions in unseen datasets from different biological species in a matter of minutes. The comprehensively annotated experimental data and pre-trained networks are provided for immediate use by the community.","doi":"10.1038/s41592-022-01746-2","authors":"de Teresa-Trueba I, Goetz SK, Mattausch A, Stojanovska F, Zimmerli CE, Toro-Nahuelpan M, Cheng DWC, Tollervey F, Pape C, Beck M, Diz-Muñoz A, Kreshuk A, Mahamid J, Zaugg JB","authors_abbrev":"de Teresa-Trueba I et al.","pubmed_publication_date":"Feb 2023","pubmed_entrez_date":"2023-01-23","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-01-25 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9450957","title":"The Win1 mitotic regulator is a component of the fission yeast stress-activated Sty1 MAPK pathway.","citation":"Mol Biol Cell 1998 Feb;9(2):311-22","abstract":"The fission yeast Sty1 mitogen-activated protein (MAP) kinase (MAPK) and its activator the Wis1 MAP kinase kinase (MAPKK) are required for cell cycle control, initiation of sexual differentiation, and protection against cellular stress. Like the mammalian JNK/SAPK and p38/CSBP1 MAPKs, Sty1 is activated by a range of environmental insults including osmotic stress, hydrogen peroxide, UV light, menadione, heat shock, and the protein synthesis inhibitor anisomycin. We have recently identified two upstream regulators of the Wis1 MAPKK, namely the Wak1 MAPKKK and the Mcs4 response regulator. Cells lacking Mcs4 or Wak1, however, are able to proliferate under stressful conditions and undergo sexual differentiation, suggesting that additional pathway(s) control the Wis1 MAPKK. We now show that this additional signal information is provided, at least in part, by the Win1 mitotic regulator. We show that Wak1 and Win1 coordinately control activation of Sty1 in response to multiple environmental stresses, but that Wak1 and Win1 perform distinct roles in the control of Sty1 under poor nutritional conditions. Our results suggest that the stress-activated Sty1 MAPK integrates information from multiple signaling pathways.","authors":"Shieh JC, Wilkinson MG, Millar JB","authors_abbrev":"Shieh JC et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-04-04","publication_year":"1998","canto_session_key":"b0cec9bfaa7f68ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-02 21:13:34","canto_approved_date":"2023-06-07 05:12:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-18 16:22:06","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.10","SPBC29B5.01","SPAC9G1.02","SPBC409.07c","SPAC1006.09","SPAC24B11.06c","SPAC19D5.01","SPCC757.07c"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2016-10-02"},{"uniquename":"PMID:17191912","title":"Sequence-specific binding of the Schizosaccharomyces pombe His1 protein to fission yeast telomeric DNA.","citation":"Chem Biodivers 2004 Sep;1(9):1344-53","abstract":"Sequence-specific protein-DNA interaction is critical for many important cellular processes such as transcription, DNA replication, and chromosome segregation. Identification of additional proteins that bind to DNA in a sequence-specific manner will contribute to the understanding of the mechanism of molecular recognition between protein and DNA. We found that the ATP phosphoribosyl transferase His1, which catalyzes the first step in histidine biosynthesis, is bound to both single- and double-stranded telomeric DNA. Competition experiments revealed that His1 is bound to a fission yeast telomeric DNA in a sequence-specific manner. Previously identified sequence-specific telomere-binding proteins contain Myb domain. In contrast, Schizosaccharomyces pombe His1 does not contain Myb domain. These findings indicate that His1 has a novel DNA-recognition domain.","authors":"Tomita K, Uritani M, Ushimaru T, Yoshinaga K, Ueno M","authors_abbrev":"Tomita K et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2006-12-29","publication_year":"2004","canto_session_key":"c91f0941add6bf0a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-07-02 19:14:47","canto_approved_date":"2023-07-02 19:14:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-02 19:14:41","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25G10.05c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2023-07-02"},{"uniquename":"PMID:8675018","title":"Cloning of the gene encoding the mitochondrial adenine nucleotide carrier of Schizosaccharomyces pombe by functional complementation in Saccharomyces cerevisiae.","citation":"Gene 1996 May 24;171(1):113-7","abstract":"We describe the isolation and sequencing of both cDNA and genomic clones encoding the mitochondrial ADP/ATP carrier (Anc) of Schizosaccharomyces pombe (Sp). The cDNA clone was isolated from a cDNA library of this fission yeast by complementation of a Saccharomyces cerevisiae (Sc) strain defective in adenine nucleotide carrier. The predicted amino acid (aa) sequence (322 aa) shared similarity with the known Anc sequences. It is more closely related to Neurospora crassa (Nc) Anc than to ScAnc1, 2, or 3 or Kluyveromyces lactis (Kl) Anc. Hybridization experiments with ordered libraries of Sp genomic DNA led to the physical mapping (chromosome II, NotI-B region) and the isolation of the Sp ANC1 gene. We also conclude that a single-copy gene encodes the Sp Anc.","authors":"Couzin N, Trézéguet V, Le Saux A, Lauquin GJ","authors_abbrev":"Couzin N et al.","pubmed_publication_date":"24 May 1996","pubmed_entrez_date":"1996-05-24","publication_year":"1996","canto_session_key":"0aebdda141c6e800","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-06-04 13:04:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-06-04 13:04:04","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC530.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-06-04"},{"uniquename":"PMID:41144523","title":"The Ync13-Rga7-Rng10 complex selectively coordinates secretory vesicle trafficking and secondary septum formation during cytokinesis.","citation":"PLoS Biol 2025 Oct 27;23(10):e3003466","abstract":"Cytokinesis requires precise coordination of contractile-ring constriction, vesicle trafficking and fusion to the plasma membrane, and extracellular matrix assembly/remodeling at the cleavage furrow to ensure faithful cell division and maintain cell integrity. These processes and proteins involved are broadly conserved across eukaryotes, yet molecular mechanisms controlling the spatiotemporal pathways of membrane trafficking remain poorly understood. Here, using fission yeast genetics, microscopy, and in vitro binding assays, we identify a conserved module including the Munc13 protein Ync13, F-BAR protein Rga7, and coiled-coil protein Rng10 to be critical for precise and selective vesicle targeting to the plasma membrane during cytokinesis. The module specifically recruits the TRAPP-II but not the exocyst complex to tether vesicles containing the glucan synthases Bgs4 and Ags1 along the cleavage furrow. Ync13 subsequently interacts with the SM protein Sec1 for vesicle fusion. Mutations in this pathway disrupt septum integrity and lead to cell lysis. Our work provides key insights into how membrane trafficking is tightly controlled to maintain cell integrity during cytokinesis.","doi":"10.1371/journal.pbio.3003466","authors":"Zhang S, Singh D, Zhu YH, Zhang KJ, Melero A, Martin SG, Wu JQ","authors_abbrev":"Zhang S et al.","pubmed_publication_date":"27 Oct 2025","pubmed_entrez_date":"2025-10-27","publication_year":"2025","canto_session_key":"0280b99733fb1aa0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Davinder Singh","canto_first_approved_date":"2025-12-04 08:04:29","canto_approved_date":"2026-04-16 06:24:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-11-27 14:34:23","canto_added_date":"2025-10-28 00:25:06","annotation_curators":[{"name":"Davinder Singh","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":42,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.08c","SPAC11E3.02c","SPBC19G7.05c","SPAC688.07c","SPAC6G10.05c","SPCC584.05","SPCC1281.01","SPBC30D10.17c","SPCC1840.02c"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2025-12-04"},{"uniquename":"PMID:12081640","title":"Calcineurin phosphatase in signal transduction: lessons from fission yeast.","citation":"Genes Cells 2002 Jul;7(7):619-27","abstract":"Calcineurin (protein phosphatase 2B), the only serine/threonine phosphatase under the control of Ca2+/calmodulin, is an important mediator in signal transmission, connecting the Ca2+-dependent signalling to a wide variety of cellular responses. Furthermore, calcineurin is specifically inhibited by the immunosuppressant drugs cyclosporin A and tacrolimus (FK506), and these drugs have been a powerful tool for identifying many of the roles of calcineurin. Calcineurin is enriched in the neural tissues, and also distributes broadly in other tissues. The structure of the protein is highly conserved from yeast to man. The combined use of powerful genetics and of specific calcineurin inhibitors in fission yeast Schizosaccharomyces pombe (S. pombe) identified new components of the calcineurin pathway, and defined new roles of calcineurin in the regulation of the many cellular processes. Recent data has revealed functional interactions in which calcineurin phosphatase is involved, such as the cross-talk between the Pmk1 MAP kinase signalling, or the PI signalling. Calcineurin also participates in membrane traffic and cytokinesis of fission yeast through its functional connection with members of the small GTPase Rab/Ypt family, and Type II myosin, respectively. These findings highlight the potential of fission yeast genetic studies to elucidate conserved elements of signal transduction cascades.","authors":"Sugiura R, Sio SO, Shuntoh H, Kuno T","authors_abbrev":"Sugiura R et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-06-26","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:S60039","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12904290","title":"Characterization of the Schizosaccharomyces pombe Cdk9/Pch1 protein kinase: Spt5 phosphorylation, autophosphorylation, and mutational analysis.","citation":"J Biol Chem 2003 Oct 31;278(44):43346-56","abstract":"Schizosaccharomyces pombe Cdk9/Pch1 protein kinase is a functional ortholog of the essential Saccharomyces cerevisiae Bur1/Bur2 kinase and a putative ortholog of metazoan P-TEFb (Cdk9/cyclin T). SpCdk9/Pch1 phosphorylates of the carboxyl-terminal domain (CTD) of the S. pombe transcription elongation factor Spt5, which consists of 18 tandem repeats of a nonapeptide of consensus sequence 1TPAWNSGSK9. We document the divalent cation dependence and specificity of SpCdk9/Pch1, its NTP dependence and specificity, the dependence of Spt5-CTD phosphorylation on the number of tandem nonamer repeats, and the specificity for phosphorylation of the Spt5-CTD on threonine at position 1 within the nonamer element. SpCdk9/Pch1 also phosphorylates the CTD heptaptide repeat array of the largest subunit of S. pombe RNA polymerase II (consensus sequence YSPTSPS) and does so exclusively on serine. SpCdk9/Pch1 catalyzes autophosphorylation of the kinase and cyclin subunits of the kinase complex. The distribution of phosphorylation sites on SpCdk9 (86% Ser(P), 11% Thr(P), 3% Tyr(P)) is distinct from that on Pch1 (2% Ser(P), 98% Thr(P)). We conducted a structure-guided mutational analysis of SpCdk9, whereby a total of 29 new mutations of 12 conserved residues were tested for in vivo function by complementation of a yeast bur1Delta mutant. We identified many lethal and conditional mutations of side chains implicated in binding ATP and the divalent cation cofactor, phosphoacceptor substrate recognition, and T-loop dynamics. We surmise that the lethality of the of T212A mutation in the T-loop reflects an essential phosphorylation event, insofar as the conservative T212S change rescued wild-type growth; the phosphomimetic T212E change rescued growth at 30 degrees C; and the effects of mutating the T-loop threonine were phenocopied by mutations in the three conserved arginines predicted to chelate the phosphate on the T-loop threonine.","authors":"Pei Y, Shuman S","authors_abbrev":"Pei Y et al.","pubmed_publication_date":"31 Oct 2003","pubmed_entrez_date":"2003-08-09","publication_year":"2003","canto_session_key":"038bf84d1f40d1e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-10-05 15:18:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-10 11:27:37","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPBC32H8.10","SPBC32F12.06","SPAC23C4.19"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-10-10"},{"uniquename":"PMID:25640420","title":"Single-molecule imaging of cytoplasmic dynein in vivo.","citation":"Methods Cell Biol 2015;125:1-12","abstract":"While early fluorescence microscopy experiments employing fluorescent probes afforded snapshots of the cell, the power of live-cell microscopy is required to understand complex dynamics in biological processes. The first successful cloning of green fluorescent protein in the 1990s paved the way for development of approaches that we now utilize for visualization in a living cell. In this chapter, we discuss a technique to observe fluorescently tagged single molecules in fission yeast. With a few simple modifications to the established total internal reflection fluorescence microscopy, cytoplasmic dynein molecules in the cytoplasm and on the microtubules can be visualized and their intracellular dynamics can be studied. We illustrate a technique to study motor behavior, which is not apparent in conventional ensemble studies of motors. In general, this technique can be employed to study single-molecule dynamics of fluorescently tagged proteins in the cell interior.","doi":"10.1016/bs.mcb.2014.10.001","authors":"Ananthanarayanan V, Tolić IM","authors_abbrev":"Ananthanarayanan V et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-02-03","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-02-04 01:15:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32327557","title":"Kinesin-14 family proteins and microtubule dynamics define  S. pombe  mitotic and meiotic spindle assembly, and elongation.","citation":"J Cell Sci 2020 Jun 08;133(11)","abstract":"To segregate the chromosomes faithfully during cell division, cells assemble a spindle that captures the kinetochores and pulls them towards opposite poles. Proper spindle function requires correct interplay between microtubule motors and non-motor proteins. Defects in spindle assembly or changes in spindle dynamics are associated with diseases, such as cancer or developmental disorders. Here, we compared mitotic and meiotic spindles in fission yeast. We show that, even though mitotic and meiotic spindles underwent the typical three phases of spindle elongation, they have distinct features. We found that the relative concentration of the kinesin-14 family protein Pkl1 is decreased in meiosis I compared to mitosis, while the concentration of the kinesin-5 family protein Cut7 remains constant. We identified the second kinesin-14 family protein Klp2 and microtubule dynamics as factors necessary for proper meiotic spindle assembly. This work defines the differences between mitotic and meiotic spindles in fission yeast  Schizosaccharomyces pombe , and provides prospect for future comparative studies.This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.240234","authors":"Loncar A, Rincon SA, Lera Ramirez M, Paoletti A, Tran PT","authors_abbrev":"Loncar A et al.","pubmed_publication_date":"08 Jun 2020","pubmed_entrez_date":"2020-04-25","publication_year":"2020","canto_session_key":"5885cef5c51f3f2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-07-14 08:33:50","canto_approved_date":"2023-07-21 13:57:07","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-07-14 08:33:21","canto_added_date":"2020-04-26 00:15:04","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":24,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c","SPAC664.10","SPBC1685.15c","SPAC3A11.14c","SPAC589.08c","SPAC1093.06c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2022-07-14"},{"uniquename":"PMID:18540885","title":"Heteromer formation of a long-chain prenyl diphosphate synthase from fission yeast Dps1 and budding yeast Coq1.","citation":"FEBS J 2008 Jul;275(14):3653-68","abstract":"Ubiquinone is an essential factor for the electron transfer system and is also a known lipid antioxidant. The length of the ubiquinone isoprenoid side-chain differs amongst living organisms, with six isoprene units in the budding yeast Saccharomyces cerevisiae, eight units in Escherichia coli and 10 units in the fission yeast Schizosaccharomyces pombe and in humans. The length of the ubiquinone isoprenoid is determined by the product generated by polyprenyl diphosphate synthases (poly-PDSs), which are classified into homodimer (i.e. octa-PDS IspB in E. coli) and heterotetramer [i.e. deca-PDSs Dps1 and D-less polyprenyl diphosphate synthase (Dlp1) in Sc. pombe and in humans] types. In this study, we characterized the hexa-PDS (Coq1) of S. cerevisiae to identify whether this enzyme was a homodimer (as in bacteria) or a heteromer (as in fission yeast). When COQ1 was expressed in an E. coli ispB disruptant, only hexa-PDS activity and ubiquinone-6 were detected, indicating that the expression of Coq1 alone results in bacterial enzyme-like functionality. However, when expressed in fission yeast Deltadps1 and Deltadlp1 strains, COQ1 restored growth on minimal medium in the Deltadlp1 but not Deltadps1 strain. Intriguingly, ubiquinone-9 and ubiquinone-10, but not ubiquinone-6, were identified and deca-PDS activity was detected in the COQ1-expressing Deltadlp1 strain. No enzymatic activity or ubiquinone was detected in the COQ1-expressing Deltadps1 strain. These results indicate that Coq1 partners with Dps1, but not with Dlp1, to be functional in fission yeast. Binding of Coq1 and Dps1 was demonstrated by coimmunoprecipitation, and the formation of a tetramer consisting of Coq1 and Dps1 was detected in Sc. pombe. Thus, Coq1 is functional when expressed alone in E. coli and in budding yeast, but is only functional as a partner with Dps1 in fission yeast. This unusual observation indicates that different folding processes or protein modifications in budding yeast/E. coli versus those in fission yeast might affect the formation of an active enzyme. These results provide important insights into the process of how PDSs have evolved from homo- to hetero-types.","doi":"10.1111/j.1742-4658.2008.06510.x","authors":"Zhang M, Luo J, Ogiyama Y, Saiki R, Kawamukai M","authors_abbrev":"Zhang M et al.","pubmed_publication_date":"Jul 2008","pubmed_entrez_date":"2008-06-11","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39252397","title":"RNA-DNA hybrids on protein coding genes are stabilized by loss of RNase H and are associated with DNA damages during S-phase in fission yeast.","citation":"Genes Cells 2024 Sep 09;","abstract":"RNA-DNA hybrid is a part of the R-loop which is an important non-standard nucleic acid structure. RNA-DNA hybrid/R-loop causes genomic instability by inducing DNA damages or inhibiting DNA replication. It also plays biologically important roles in regulation of transcription, replication, recombination and repair. Here, we have employed catalytically inactive human RNase H1 mutant (D145N) to visualize RNA-DNA hybrids and map their genomic locations in fission yeast cells. The RNA-DNA hybrids appear as multiple nuclear foci in rnh1∆rnh201∆ cells lacking cellular RNase H activity, but not in the wild-type. The majority of RNA-DNA hybrid loci are detected at the protein coding regions and tRNA. In rnh1∆rnh201∆ cells, cells with multiple Rad52 foci increase during S-phase and about 20% of the RNA-DNA hybrids overlap with Rad52 loci. During S-phase, more robust association of Rad52 with RNA-DNA hybrids was observed in the protein coding region than in M-phase. These results suggest that persistent RNA-DNA hybrids in the protein coding region in rnh1∆rnh201∆ cells generate DNA damages during S-phase, potentially through collision with DNA replication forks.","doi":"10.1111/gtc.13157","authors":"Sagi T, Sadato D, Takayasu K, Sasanuma H, Kanoh Y, Masai H","authors_abbrev":"Sagi T et al.","pubmed_publication_date":"09 Sep 2024","pubmed_entrez_date":"2024-09-10","publication_year":"2024","canto_session_key":"66a349efeb8d5786","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-09-10 23:25:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37531259","title":"Membrane binding of endocytic myosin-1s is inhibited by a class of ankyrin repeat proteins.","citation":"Mol Biol Cell 2023 Oct 01;34(11):br17","abstract":"Myosin-1s are monomeric actin-based motors that function at membranes. Myo1 is the single myosin-1 isoform in  Schizosaccharomyces pombe  that works redundantly with Wsp1-Vrp1 to activate the Arp2/3 complex for endocytosis. Here, we identified Ank1 as an uncharacterized cytoplasmic Myo1 binding partner. We found that in  ank1Δ  cells, Myo1 dramatically redistributed from endocytic patches to decorate the entire plasma membrane and endocytosis was defective. Biochemical analysis and structural predictions suggested that the Ank1 ankyrin repeats bind the Myo1 lever arm and the Ank1 acidic tail binds the Myo1 TH1 domain to prevent TH1-dependent Myo1 membrane binding. Indeed, Ank1 overexpression precluded Myo1 membrane localization and recombinant Ank1 reduced purified Myo1 liposome binding in vitro. Based on biochemical and cell biological analyses, we propose budding yeast Ank1 and human OSTF1 are functional Ank1 orthologs and that cytoplasmic sequestration by small ankyrin repeat proteins is a conserved mechanism regulating myosin-1s in endocytosis.","doi":"10.1091/mbc.E23-06-0233","authors":"Willet AH, Chen JS, Ren L, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"01 Oct 2023","pubmed_entrez_date":"2023-08-02","publication_year":"2023","canto_session_key":"0ae5e45bd4264f63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2023-08-10 13:31:04","canto_approved_date":"2026-04-02 12:26:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-08-09 15:31:51","canto_added_date":"2023-08-03 00:15:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":36,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.13c","SPAC105.02c","SPBC1778.06c","SPAC4F10.15c","SPCC162.07","SPAC20G8.05c","SPBC32H8.12c","SPAC29A4.05","SPAC3A12.14","SPAC23A1.17","SPBC13E7.09","SPAC630.03"],"gene_count":12,"ltp_gene_count":9,"approved_date":"2023-08-10"},{"uniquename":"PMID:18669302","title":"[Evolution of meiosis of unicellulate and multicellular eucaryotes. Aromorphosis at the cellular level].","citation":"Zh Obshch Biol 2008;69(2):102-17","abstract":"An attempt was undertaken to apply the concept elaborated for the evolution of multicellular organisms to that of unicellular eucaryotes. The latter's meiosis was formed on the basis of combination on three intracellular processes: 1) homologous DNA recombination, 2) chromosome disjunction with the assistance of mitotic apparatus, and 3) formation of \"linear\" chromosome elements consisting of specific proteins. Mechanism of homologous chromosome recombination was inherited from the archibacteria, while both the mitotic apparatus and \"linear\" chromosome elements emerged de novo. These elements appeared (resulting from appearance of the meiosis-specific proteins) as a complication of cohesion filaments, arising at the boundary between the sister chromatids after DNA replication. Homologous chromosome recombination made it possible for the chromosomes of diploid organisms to join pairwise by means of Holliday structures, while temporary blocking of hydrolysis of the linear elements at centromeres made it possible for the kinetochores to acquire unipolarity and for the sister chromatids to move to the same pole. All these provided for reduction of the chromosome number. Such a type of the reduction of chromosome number was retained by the extant imperfect ascomycetes Schizosaccharomyces pombe and Aspergillus nidulans, and by the infusorian Tetrahyrmena thermophila. It was the derivative of specific proteins, i.e. synaptonemal complexes (SCs). that appeared to be aromorphosis; they came to existence due to the pairwise joining of the chromosome \"linear\" elements by means of protein \"zipper\". The SCs join homologous chromosomes temporarily at the prophase of meiotic reduction division, thus optimizing condition for the crossing over and chiasma formation. The latter and the kinetochore unipolarity both provide for the chromosome disjunction. Kinetochore unipolarity is caused by the protein shugoshin which appears at meiotic prophase I and blocks cohesin hydrolysis at centromeres when anaphase I begins. This type of reductional division became the basis of the classical meiosis in the overwhelming majority of unicellular and multicellular organisms over all eucaryote kingdoms.","authors":"Bogdanov IuF","authors_abbrev":"Bogdanov IuF","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-08-02","publication_year":"2008","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37445861","title":"Resistance to Chemotherapeutic 5-Fluorouracil Conferred by Modulation of Heterochromatic Integrity through Ino80 Function in Fission Yeast.","citation":"Int J Mol Sci 2023 Jun 26;24(13)","abstract":"5-Fluorouracil (5-FU) is a conventional chemotherapeutic drug widely used in clinics worldwide, but development of resistance that compromises responsiveness remains a major hurdle to its efficacy. The mechanism underlying 5-FU resistance is conventionally attributed to the disruption of nucleotide synthesis, even though research has implicated other pathways such as RNA processing and chromatin dysregulation. Aiming to clarify resistance mechanisms of 5-FU, we tested the response of a collection of fission yeast ( Schizosaccharomyces pombe ) null mutants, which confer multiple environmental factor responsiveness (MER). Our screen identified disruption of membrane transport, chromosome segregation and mitochondrial oxidative phosphorylation to increase cellular susceptibility towards 5-FU. Conversely, we revealed several null mutants of Ino80 complex factors exhibited resistance to 5-FU. Furthermore, attenuation of Ino80 function via deleting several subunit genes reversed loss of chromosome-segregation fidelity in 5-FU in the loss-of-function mutant of the Argonaute protein, which regulates RNA interference (RNAi)-dependent maintenance of pericentromeric heterochromatin. Our study thus uncovered a critical role played by chromatin remodeling Ino80 complex factors in 5-FU resistance, which may constitute a possible target to modulate in reversing 5-FU resistance.","doi":"10.3390/ijms241310687","authors":"Lim KK, Koh NZH, Zeng YB, Chuan JK, Raechell R, Chen ES","authors_abbrev":"Lim KK et al.","pubmed_publication_date":"26 Jun 2023","pubmed_entrez_date":"2023-07-14","publication_year":"2023","canto_session_key":"527b6a62edc40016","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lim Kim Kiat","canto_first_approved_date":"2024-04-18 13:42:58","canto_approved_date":"2024-04-30 13:20:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-17 13:35:00","canto_added_date":"2023-07-15 00:15:12","annotation_curators":[{"name":"Lim Kim Kiat","community_curator":true,"annotation_count":92,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":98,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.03c","SPBC83.03c","SPAC23H3.06","SPAC3H8.05c","SPBC215.03c","SPBC28F2.10c","SPCC31H12.08c","SPBC18H10.04c","SPAC1687.12c","SPBC2D10.13","SPAC23D3.09","SPBPJ4664.01","SPCC18.06c","SPBC21B10.13c","SPBC2F12.12c","SPAC6G9.14","SPAC664.02c","SPBC32H8.07","SPAC513.03","SPCC16C4.20c","SPAC1B2.04","SPAC6B12.05c","SPCC1840.09","SPCC777.13","SPBC21C3.20c","SPCC417.02","SPCC11E10.08","SPAC56F8.04c","SPBP8B7.28c","SPBC651.07","SPBC106.05c","SPBC365.10","SPAC8E11.02c","SPAC23G3.04","SPBC36.05c","SPBC2D10.16","SPAC13C5.07","SPAPB1A10.09","SPCC338.08","SPBC17D1.02","SPBC4B4.03","SPAC644.14c","SPAPB17E12.04c","SPCC970.07c","SPAC2F3.11","SPAC823.10c","SPCC1259.03","SPBC18H10.02","SPBC32F12.08c","SPAC2C4.05","SPCC23B6.05c","SPAC17H9.19c","SPBC1105.10","SPAC1805.07c","SPBP8B7.22","SPCC757.10","SPAC11E3.12","SPAC16A10.05c","SPCC663.03","SPAC222.04c","SPAC144.06","SPCC1259.04","SPAC14C4.16","SPBC337.15c","SPAC31G5.19","SPAC144.02","SPCC736.11","SPCC16A11.07","SPAC15A10.03c","SPCC162.05","SPBC1604.02c","SPCC576.12c","SPAC1952.05","SPAC23C11.08","SPAC29B12.08","SPBC27B12.10c","SPCC1739.14","SPCC1672.04c","SPCC18.02","SPAC17H9.08","SPBC19G7.10c","SPAC630.14c","SPAC9E9.09c","SPAC6F12.09","SPBC26H8.07c","SPBC1734.15","SPBC800.03","SPBC146.12","SPAC17G8.07","SPAPB1E7.02c","SPAC2F7.07c","SPBC4F6.10","SPBC947.14c","SPAC10F6.08c","SPCC24B10.08c","SPBC16H5.13","SPBC428.08c","SPBC16A3.07c","SPCC1223.15c","SPBC106.04","SPAC4F10.04","SPCC663.12"],"gene_count":102,"ltp_gene_count":102,"approved_date":"2024-04-18"},{"uniquename":"PMID:41136340","title":"Conserved protein Seb1 that interacts with RNA polymerase II and RNA is an anti-pausing transcription elongation factor.","citation":"RNA 2025 Oct 24;","abstract":"Maturation of protein-coding precursor messenger RNA (pre-mRNA) is closely linked to RNA polymerase II (Pol II) transcription. However, the mechanistic understanding of how RNA processing is coordinated with transcription remains incomplete. Conserved proteins interacting with the C-terminal domain of the largest catalytic subunits of Pol II and nascent RNA (CID-RRM factors) were demonstrated to play a role in pre-mRNA 3'-end processing and termination of Pol II transcription. Here, we employ a fully reconstituted system to demonstrate that the fission yeast CID-RRM factor Seb1 acts as a bona fide elongation factor in vitro. Our analyses show that Seb1 exhibits context-dependent regulation of Pol II pausing, capable of either promoting or inhibiting pause site entry. We propose that CID-RRM factors coordinate Pol II transcription and pre-mRNA 3'-end processing by modulating the rate of Pol II transcription.","doi":"10.1261/rna.080765.125","authors":"Kuś K, Nielsen S, Zenkin N, Vasiljeva L","authors_abbrev":"Kuś K et al.","pubmed_publication_date":"24 Oct 2025","pubmed_entrez_date":"2025-10-24","publication_year":"2025","canto_session_key":"15eae7cee63b438f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-25 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28671615","title":"TORC1-Dependent Phosphorylation Targets in Fission Yeast.","citation":"Biomolecules 2017 Jul 03;7(3)","abstract":"Target of rapamycin (TOR) kinase controls cell metabolism and growth in response to environmental cues such as nutrients, growth factors, and stress. TOR kinase is widely conserved across eukaryotes. As in other organisms, the fission yeast  Schizosaccharomyces pombe  has two types of TOR complex, namely TOR complex 1 (TORC1) and TORC2. It is interesting that the two TOR complexes in  S. pombe  have opposite roles in sexual differentiation, which is induced by nutrient starvation. TORC1, which contains Tor2 as a catalytic subunit, promotes vegetative growth and represses sexual differentiation in nutrient-rich conditions, while TORC2 is required for the initiation of sexual differentiation. Multiple targets of TORC1 have been identified. Some of these, such as S6 kinase and an autophagy regulator Atg13, are known targets in other organisms. In addition, there is a novel group of TORC1 targets involved in the regulation of sexual differentiation. Here, we review recent findings on phosphorylation targets of TORC1 in  S. pombe.  Furthermore, we briefly report a novel S. pombe target of TORC1.","doi":"10.3390/biom7030050","authors":"Otsubo Y, Nakashima A, Yamamoto M, Yamashita A","authors_abbrev":"Otsubo Y et al.","pubmed_publication_date":"03 Jul 2017","pubmed_entrez_date":"2017-07-04","publication_year":"2017","canto_session_key":"dcfa45e46e99ecef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Akira Yamashita","canto_first_approved_date":"2018-10-04 16:02:55","canto_approved_date":"2024-01-03 11:23:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-13 03:16:00","canto_added_date":"2017-07-05 00:15:15","annotation_curators":[{"name":"Akira Yamashita","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.08","SPAC4F10.07c","SPBC216.07c","SPBC32C12.02"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2018-10-04"},{"uniquename":"PMID:25342311","title":"Protective roles of osmotic stress-resistant Hos3 against oxidative, nitrosative and nutritional stresses in Schizosaccharomyces pombe.","citation":"World J Microbiol Biotechnol 2015 Jan;31(1):237-45","abstract":"Hos3 is involved in cellular growth under osmotic stress in Schizosaccharomyces pombe. The recombinant plasmid pYFHos3 harboring the structural gene encoding Hos3 was constructed. The S. pombe cells harboring pYFHos3 contained the increased hos3 (+) mRNA content and exhibited an enhanced growth in high osmotic conditions, such as 1.5 M KCl and 2.5 M D-glucose, compared with the vector control cells. In the presence of hydrogen peroxide (H2O2), superoxide anion-generating menadione (MD) and nitric oxide (NO)-generating sodium nitroprusside (SNP), they could grow better than the vector control cells. In the presence of H2O2, MD and SNP and in the absence of a nitrogen source, the S. pombe cells harboring pYFHos3 contained less elevated NO and reactive oxygen species (ROS) levels than the vector control cells. Collectively, the S. pombe Hos3 also participate in the cellular defense against oxidative, nitrosative and nutritional stresses through down-regulating ROS and NO levels.","doi":"10.1007/s11274-014-1762-5","authors":"Lim CJ, Jo H, Kim K","authors_abbrev":"Lim CJ et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-10-25","publication_year":"2015","canto_session_key":"fdda499d9208a1d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-10-26 00:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9372443","title":"Localisation of the Schizosaccharomyces pombe rho1p GTPase and its involvement in the organisation of the actin cytoskeleton.","citation":"J Cell Sci 1997 Oct;110 ( Pt 20):2547-55","abstract":"The Schizosaccharomyces pombe rho1p GTPase directly activates the (1-3) beta-D-glucan synthase and participates in the regulation of cell wall growth and morphogenesis in this fission yeast. Indirect immunofluorescence experiments using rho1p tagged with hemagglutinin have revealed that rho1p was located at the growing tips during interphase and at the septum prior to cytokinesis, localising to the same areas as actin patches. In S. pombe cdc10-129 mutant cells, arrested in G1, HA-rho1p accumulates at one tip whereas in cdc25-22 mutants, arrested in G2, HA-rho1p accumulates at both tips. In tea1-1 and tea2-1 cdc11-119 mutant cells, HA-rho1p is localised to the new growing tips. Overexpression of different rho1 mutant alleles caused different effects on cortical actin patch distribution, (1-3) beta-D-glucan synthase activation, and sensitivity to cell wall specific antifungal drugs. These results indicate that multiple cellular components are activated by rho1p. Overexpression of the dominant negative rho1T20N allele was lethal as was the rho1+ deletion. Moreover, when rho1+ expression was repressed in actively growing S. pombe, cells died in about 10 to 12 hours. Under these conditions, normal cell morphology was maintained but the level of (1-3) beta-D-glucan synthase activity decreased and the actin patches disappeared. Most cells lysed after cytokinesis during the process of separation, and lysis was not prevented by an osmotic stabiliser. We conclude that rho1p localisation is restricted to growth areas and regulated during the cell cycle and that rho1p is involved in cell wall growth and actin cytoskeleton organisation in S. pombe.","authors":"Arellano M, Duran A, Perez P","authors_abbrev":"Arellano M et al.","pubmed_publication_date":"Oct 1997","pubmed_entrez_date":"1998-02-12","publication_year":"1997","canto_session_key":"88f668cbb0dd4816","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-07-16 15:37:21","canto_approved_date":"2022-07-11 16:32:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-30 16:18:14","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":55,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.20c","SPAC1F7.04","SPCC1223.06","SPCC1739.11c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2020-07-16"},{"uniquename":"PMID:19266076","title":"Pro-aging effects of glucose signaling through a G protein-coupled glucose receptor in fission yeast.","citation":"PLoS Genet 2009 Mar;5(3):e1000408","abstract":"Glucose is the preferred carbon and energy source in prokaryotes, unicellular eukaryotes, and metazoans. However, excess of glucose has been associated with several diseases, including diabetes and the less understood process of aging. On the contrary, limiting glucose (i.e., calorie restriction) slows aging and age-related diseases in most species. Understanding the mechanism by which glucose limits life span is therefore important for any attempt to control aging and age-related diseases. Here, we use the yeast Schizosaccharomyces pombe as a model to study the regulation of chronological life span by glucose. Growth of S. pombe at a reduced concentration of glucose increased life span and oxidative stress resistance as reported before for many other organisms. Surprisingly, loss of the Git3 glucose receptor, a G protein-coupled receptor, also increased life span in conditions where glucose consumption was not affected. These results suggest a role for glucose-signaling pathways in life span regulation. In agreement, constitutive activation of the Galpha subunit acting downstream of Git3 accelerated aging in S. pombe and inhibited the effects of calorie restriction. A similar pro-aging effect of glucose was documented in mutants of hexokinase, which cannot metabolize glucose and, therefore, are exposed to constitutive glucose signaling. The pro-aging effect of glucose signaling on life span correlated with an increase in reactive oxygen species and a decrease in oxidative stress resistance and respiration rate. Likewise, the anti-aging effect of both calorie restriction and the Deltagit3 mutation was accompanied by increased respiration and lower reactive oxygen species production. Altogether, our data suggest an important role for glucose signaling through the Git3/PKA pathway to regulate S. pombe life span.","doi":"10.1371/journal.pgen.1000408","authors":"Roux AE, Leroux A, Alaamery MA, Hoffman CS, Chartrand P, Ferbeyre G, Rokeach LA","authors_abbrev":"Roux AE et al.","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2009-03-07","publication_year":"2009","canto_session_key":"5c7e25166dfbc44f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-04 13:21:12","canto_approved_date":"2020-12-09 15:40:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-23 16:24:25","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H3.13c","SPAC4F8.07c","SPBC106.10","SPAC24H6.04","SPCC1753.02c","SPBC1198.14c","SPAC821.10c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2015-06-04"},{"uniquename":"PMID:26338468","title":"Spontaneous cell polarization: Feedback control of Cdc42 GTPase breaks cellular symmetry.","citation":"Bioessays 2015 Nov;37(11):1193-201","abstract":"Spontaneous polarization without spatial cues, or symmetry breaking, is a fundamental problem of spatial organization in biological systems. This question has been extensively studied using yeast models, which revealed the central role of the small GTPase switch Cdc42. Active Cdc42-GTP forms a coherent patch at the cell cortex, thought to result from amplification of a small initial stochastic inhomogeneity through positive feedback mechanisms, which induces cell polarization. Here, I review and discuss the mechanisms of Cdc42 activity self-amplification and dynamic turnover. A robust Cdc42 patch is formed through the combined effects of Cdc42 activity promoting its own activation and active Cdc42-GTP displaying reduced membrane detachment and lateral diffusion compared to inactive Cdc42-GDP. I argue the role of the actin cytoskeleton in symmetry breaking is not primarily to transport Cdc42 to the active site. Finally, negative feedback and competition mechanisms serve to control the number of polarization sites.","doi":"10.1002/bies.201500077","authors":"Martin SG","authors_abbrev":"Martin SG","pubmed_publication_date":"Nov 2015","pubmed_entrez_date":"2015-09-05","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-09-06 00:19:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D85030","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22084420","title":"DNA sequence-mediated, evolutionarily rapid redistribution of meiotic recombination hotspots.","citation":"Genetics 2011 Nov;189(3):685-94","abstract":"Hotspots regulate the position and frequency of Spo11 (Rec12)-initiated meiotic recombination, but paradoxically they are suicidal and are somehow resurrected elsewhere in the genome. After the DNA sequence-dependent activation of hotspots was discovered in fission yeast, nearly two decades elapsed before the key realizations that (A) DNA site-dependent regulation is broadly conserved and (B) individual eukaryotes have multiple different DNA sequence motifs that activate hotspots. From our perspective, such findings provide a conceptually straightforward solution to the hotspot paradox and can explain other, seemingly complex features of meiotic recombination. We describe how a small number of single-base-pair substitutions can generate hotspots de novo and dramatically alter their distribution in the genome. This model also shows how equilibrium rate kinetics could maintain the presence of hotspots over evolutionary timescales, without strong selective pressures invoked previously, and explains why hotspots localize preferentially to intergenic regions and introns. The model is robust enough to account for all hotspots of humans and chimpanzees repositioned since their divergence from the latest common ancestor.","doi":"10.1534/genetics.111.134130","authors":"Wahls WP, Davidson MK","authors_abbrev":"Wahls WP et al.","pubmed_publication_date":"Nov 2011","pubmed_entrez_date":"2011-11-16","publication_year":"2011","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30704594","title":"Volatile composition of bilberry wines fermented with non-Saccharomyces and Saccharomyces yeasts in pure, sequential and simultaneous inoculations.","citation":"Food Microbiol 2019 Jun;80:25-39","abstract":"Bilberry (Vaccinium myrtillus L.) juice was fermented with Torulaspora delbrueckii (TD291 and TD70526) and Schizosaccharomyces pombe (SP3796 and SP70572) in pure fermentation as well as in sequential and simultaneous inoculations with Saccharomyces cerevisiae 1116 (SC1116). Altogether, 56 volatile compounds were identified and semi-quantified with HS-SPME-GC/MS in bilberry products. Yeast fermentation prominently enhanced the aroma complexity of bilberry with a sharp increase in alcohols, esters, aldehydes, and acetals. Compared to S. cerevisiae, T. delbrueckii produced less ethanol but more fusel alcohols that potentially enhance \"alcohol\" and \"nail polish\" odors in TD70526 and less \"fruity\" esters in TD291. SP70572 resulted in high productions of undesirable compounds of acetoin and acetaldehyde but a low content of higher alcohols and esters, SP3796 produced a high content of fatty acid ethyl esters and acetoin. In comparison with monoculture of non-Saccharomyces yeast, sequential and simultaneous cultures of S. pombe and S. cerevisiae significantly decreased the content of acetoin while increased the relative level of esters; sequential cultures of T. delbrueckii and S. cerevisiae remarkably increased the concentration of acetaldehyde; simultaneous inoculations of S. cerevisiae with TD70526 and TD291 significantly decreased the content of fusel alcohols and increased the content of esters, respectively. The findings suggested that non-Saccharomyces yeasts possess the potential to affect and modulate the aromatic profile of fermented bilberry products. Sequential and simultaneous inoculations with S. pombe strains and S. cerevisiae as well as simultaneous fermentation using T. delbrueckii strains and S. cerevisiae are optimal strategies to positively influence the aroma profile of bilberry wines.","doi":"10.1016/j.fm.2018.12.015","authors":"Liu S, Laaksonen O, Yang B","authors_abbrev":"Liu S et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-02-02","publication_year":"2019","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2019-02-03 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19636559","title":"The pleiotropic cell separation mutation spl1-1 is a nucleotide substitution in the internal promoter of the proline tRNACGG gene of Schizosaccharomyces pombe.","citation":"Curr Genet 2009 Oct;55(5):511-20","abstract":"spl1-1 was originally identified as a spontaneous mutation genetically interacting with sep1-1 and cdc4-8 in producing multinucleate syncytia. This study shows that it is allelic with the proline-tRNA(CGG) gene SPATRNAPRO.02. Its nucleotide sequence contains a C-->T substitution in the region corresponding to the B-box of the putative intragenic promoter and the TpsiC loop of the mature tRNA. The substitution drastically reduces the transcription efficiency of the gene and pleiotropically affects numerous cellular processes. spl1-1 cells are temperature sensitive, osmosensitive, bend at higher temperatures, have extended G2 phase and are defective in cell separation (septum cleavage). The proline-tRNA(TGG) gene SPATRNAPRO.01 can partially suppress the spl1-1 mutation when introduced into the cells on a multicopy plasmid. The effect of a mutation in a tRNA gene on cell separation brings a new element into the complexity of the regulation of cell division and its co-ordination with other cellular processes in Schizosaccharomyces pombe.","doi":"10.1007/s00294-009-0262-x","authors":"Miklos I, Ludanyi K, Sipiczki M","authors_abbrev":"Miklos I et al.","pubmed_publication_date":"Oct 2009","pubmed_entrez_date":"2009-07-29","publication_year":"2009","canto_session_key":"1305068212b0226d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-31 10:41:41","canto_approved_date":"2019-06-14 09:04:50","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-01-31 10:40:58","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPATRNAPRO.03","SPATRNAPRO.02","SPATRNAPRO.01"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-01-31"},{"uniquename":"PMID:24674059","title":"Coimmunoprecipitation of proteins from yeast.","citation":"Methods Enzymol 2014;541:13-26","abstract":"This protocol outlines a procedure for testing whether two proteins interact. A target protein will be immunoprecipitated using an antibody that recognizes it (or a tagged version of the protein). The immunoprecipitated material will be separated by SDS-PAGE and analyzed by Western blotting to assess the presence of a candidate interacting protein(s).","doi":"10.1016/B978-0-12-420119-4.00002-1","authors":"Gerace E, Moazed D","authors_abbrev":"Gerace E et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-03-29","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF15477","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14C8.19"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:4868355","title":"Lysis of yeast cell walls induced by 2-deoxyglucose at their sites of glucan synthesis.","citation":"J Bacteriol 1968 Mar;95(3):1169-72","abstract":"Six sites of 2-deoxyglucose (2DG)-induced lysis on three yeasts (Schizosaccharomyces pombe, Pichia farinosa, and Saccharomyces cerevisiae) coincided with the regions of growth of their glucan layers. Identification of the glucan layer as the site of lysis suggests a mechanism of attack by 2DG or by its derivatives. It is proposed that the glucan layer grows by addition of glucose into internal breaks of polysaccharide molecules. 2DG inhibited resynthesis (insertion of glucose) of the broken glycosidic linkage.","authors":"Johnson BF","authors_abbrev":"Johnson BF","pubmed_publication_date":"Mar 1968","pubmed_entrez_date":"1968-03-01","publication_year":"1968","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18406330","title":"Retrotransposon Tf1 is targeted to Pol II promoters by transcription activators.","citation":"Mol Cell 2008 Apr 11;30(1):98-107","abstract":"The LTR-retrotransposon Tf1 preserves the coding capacity of its host Schizosaccharomyces pombe by integrating upstream of open reading frames (ORFs). To determine which features of the target sites were recognized by the transposon, we introduced plasmids containing candidate insertion sites into S. pombe and mapped the positions of integration. We found that Tf1 was targeted specifically to the promoters of Pol II-transcribed genes. A detailed analysis of integration in plasmids that contained either ade6 or fbp1 revealed insertions occurred in the promoters at positions where transcription factors bound. Further experiments revealed that the activator Atf1p and its binding site were required for directing integration to the promoter of fbp1. An interaction between Tf1 integrase and Atf1p was observed, indicating that integration at fbp1 was mediated by the activator bound to its promoter. Surprisingly, we found Tf1 contained sequences that activated transcription, and these substituted for elements of the ade6 promoter disrupted by integration.","doi":"10.1016/j.molcel.2008.02.016","authors":"Leem YE, Ripmaster TL, Kelly FD, Ebina H, Heincelman ME, Zhang K, Grewal SI, Hoffman CS, Levin HL","authors_abbrev":"Leem YE et al.","pubmed_publication_date":"11 Apr 2008","pubmed_entrez_date":"2008-04-15","publication_year":"2008","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31597680","title":"Two  S. pombe  septation phases differ in ingression rate, septum structure, and response to F-actin loss.","citation":"J Cell Biol 2019 Dec 02;218(12):4171-4194","abstract":"In fission yeast, cytokinesis requires a contractile actomyosin ring (CR) coupled to membrane and septum ingression. Septation proceeds in two phases. In anaphase B, the septum ingresses slowly. During telophase, the ingression rate increases, and the CR becomes dispensable. Here, we explore the relationship between the CR and septation by analyzing septum ultrastructure, ingression, and septation proteins in cells lacking F-actin. We show that the two phases of septation correlate with septum maturation and the response of cells to F-actin removal. During the first phase, the septum is immature and, following F-actin removal, rapidly loses the Bgs1 glucan synthase from the membrane edge and fails to ingress. During the second phase, the rapidly ingressing mature septum can maintain a Bgs1 ring and septum ingression without F-actin, but ingression becomes Cdc42 and exocyst dependent. Our results provide new insights into fungal cytokinesis and reveal the dual function of CR as an essential landmark for the concentration of Bgs1 and a contractile structure that maintains septum shape and synthesis.","doi":"10.1083/jcb.201808163","authors":"Ramos M, Cortés JCG, Sato M, Rincón SA, Moreno MB, Clemente-Ramos JÁ, Osumi M, Pérez P, Ribas JC","authors_abbrev":"Ramos M et al.","pubmed_publication_date":"02 Dec 2019","pubmed_entrez_date":"2019-10-11","publication_year":"2019","canto_session_key":"a7b77eeafc270cf2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-10-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22727667","title":"Intrinsic nucleic acid-binding activity of Chp1 chromodomain is required for heterochromatic gene silencing.","citation":"Mol Cell 2012 Jul 27;47(2):228-41","abstract":"Centromeric heterochromatin assembly in fission yeast requires the RNAi pathway. Chp1, a chromodomain (CD) protein, forms the Ago1-containing RNA-induced transcriptional silencing (RITS) complex and recruits siRNA-bound RITS to methylated histone H3 lysine 9 (H3K9me) via its CD. Here, we show that the CD of Chp1 (Chp1-CD) possesses unique nucleic acid-binding activities that are essential for heterochromatic gene silencing. Detailed electrophoretic-mobility shift analyses demonstrated that Chp1 binds to RNA via the CD in addition to its central RNA-recognition motif. Interestingly, robust RNA- and DNA-binding activity of Chp1-CD was strongly enhanced when it was bound to H3K9me, which was revealed to involve a positively charged domain within the Chp1-CD by structural analyses. These results demonstrate a role for the CD that provides a link between RNA, DNA, and methylated histone tails to ensure heterochromatic gene silencing.","doi":"10.1016/j.molcel.2012.05.017","authors":"Ishida M, Shimojo H, Hayashi A, Kawaguchi R, Ohtani Y, Uegaki K, Nishimura Y, Nakayama J","authors_abbrev":"Ishida M et al.","pubmed_publication_date":"27 Jul 2012","pubmed_entrez_date":"2012-06-26","publication_year":"2012","canto_session_key":"f96ed996276b8e88","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-ichi Nakayama","canto_first_approved_date":"2016-02-09 09:31:53","canto_approved_date":"2025-04-16 09:39:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-10-27 12:15:32","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jun-ichi Nakayama","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16C6.10","SPBC1105.11c","SPBC428.08c","SPAC664.01c","SPBC83.03c","SPBC8D2.04","SPAC1834.04","SPAC18G6.02c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2016-02-09","pdb_entries":[{"pdb_id":"2rsn","gene_chains":[{"gene_uniquename":"SPAC18G6.02c","chain":"A","position":"1-75"}],"title":"Solution structure of the chromodomain of Chp1 in complex with H3K9me3 peptide","entry_authors":"Shimojo H,Nishimura Y","entry_authors_abbrev":"Shimojo H et al.","reference_uniquename":"PMID:22727667","experimental_method":"NMR","resolution":""},{"pdb_id":"2rso","gene_chains":[{"gene_uniquename":"SPAC664.01c","chain":"A","position":"55-142"}],"title":"Solution structure of the chromodomain of Swi6","entry_authors":"Shimojo H,Nishimura Y","entry_authors_abbrev":"Shimojo H et al.","reference_uniquename":"PMID:22727667","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:9157844","title":"[Cloning of cDNA for RNA polymerase subunit from the fission yeast Schizosaccharomyces pombe by heterospecific complementation in Saccharomyces cerevisiae].","citation":"Bioorg Khim 1997 Feb;23(2):110-7","abstract":"The rpb10 cDNA of the fission yeast Schizosaccharomyces pombe, encoding one of the five small subunits common to all three nuclear DNA-dependent RNA polymerases, was isolated from an expression cDNA library by two independent approaches: PCR-based screening and direct suppression by means of heterospecific complementation of a temperature-sensitive mutant defective in the corresponding gene of Saccharomyces cerevisiae. The cloned Sz. pombe cDNA encodes a protein Rpb10 of 71 amino acids with an M of 8,275 Da, sharing 51 amino acids (71% identity) with the subunit ABC10 beta of RNA polymerases I-III from S. cerevisiae. All eukaryotic members of this protein family have the same general organization featuring two highly conserved motifs (RCFT/SCGK and RYCCRRM) around an atypical zinc finger and an additional invariant HVDLIEK motif toward the C-terminal end. The last motif is only characteristics for homologs from eukaryotes. In keeping with this remarkable structural conservation, the Sz. pombe cDNA also fully complemented a S. cerevisiae deletion mutant lacking subunit ABC10 beta (null allele rpb10-delta 1::HIS3).","authors":"Shpakovskiĭ GV, Lebedenko EN, Thuriaux P","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B3.12c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:20432054","title":"NSC126188, a piperazine alkyl derivative, induces apoptosis via upregulation of RhoB in HeLa cells.","citation":"Invest New Drugs 2011 Oct;29(5):853-60","abstract":"We describe here a piperazine alkyl derivative, NSC126188, which induced apoptosis of HeLa cells by upregulating RhoB expression. NSC126188 caused multi-septation of fission yeast and hypersensitized a ∆rho3 mutant, which implicates the involvement of functional human homolog RhoB. The treatment of cells with NSC126188 induced apoptosis and a dramatic increase in RhoB expression. In addition, RhoB knockdown using siRNA rescued cells from apoptosis, indicating a crucial role of RhoB in NSC126188-induced apoptosis. In a reporter assay using luciferase and EGFP under control of the RhoB promoter, NSC126188 increased both luciferase activity and the expression of EGFP, implicating transcriptional activation of RhoB by NSC126188. Furthermore, NSC126188 demonstrated in vivo anti-tumor activity, inhibiting tumor growth by 66.8% in a nude mouse xenograft using PC-3 human prostate cancer cells. These results suggest that NSC126188 is a potential lead compound and that upregulation of RhoB is associated with NSC126188-induced apoptosis.","doi":"10.1007/s10637-010-9433-3","authors":"Kim BK, Kim DM, Chung KS, Park SK, Choi SJ, Song A, Lee K, Lee CW, Song KB, Han G, Simon J, Kim HM, Won M","authors_abbrev":"Kim BK et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2010-05-01","publication_year":"2011","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9302019","title":"Trehalose synthesis is important for the acquisition of thermotolerance in Schizosaccharomyces pombe.","citation":"Mol Microbiol 1997 Aug;25(3):571-81","abstract":"Yeast cells show an adaptive response to a mild heat shock, resulting in thermotolerance acquisition. This is accompanied by induction of heat-shock protein (hsp) synthesis and rapid accumulation of trehalose. Genetic approaches to determine the specific role of trehalose in heat-induced thermotolerance in Saccharomyces cerevisiae have been hampered by the finding that deletion of TPS1, the gene encoding trehalose-6-phosphate synthase, causes a variety of pleiotropic effects, including inability to grow on glucose-containing media. Here, we have studied a tps1 mutant of the yeast Schizosaccharomyces pombe that reportedly has no such growth defects. We show that tps1 mutants have a serious defect in heat shock-induced acquisition of thermotolerance if conditioned at highly elevated temperatures (40-42.5 degrees C), which, in wild-type cells, prevent hsp but not trehalose synthesis. In contrast, hsp synthesis appears to become particularly important under conditions in which trehalose synthesis is either absent (in tps1 mutant strains) or not fully induced (conditioning at moderately elevated temperatures, i.e. 35 degrees C). In addition, pka1 mutants deficient in cAMP-dependent protein kinase were examined. Unconditioned pka1 cells had low levels of trehalose but a high basal level of thermotolerance. It was found that pka1 mutant cells, contrary to wild-type cells, accumulated large amounts of trehalose, even during a 50 degrees C treatment. pka1 tps1 double mutants lacked this ability and showed reduced intrinsic thermotolerance, indicating a particularly important role for trehalose synthesis, which takes place during the challenging heat shock.","authors":"Ribeiro MJ, Reinders A, Boller T, Wiemken A, De Virgilio C","authors_abbrev":"Ribeiro MJ et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"5c56c39ee0f18486","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-09-11 09:27:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-10 16:12:26","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10","SPAC328.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-09-10"},{"uniquename":"PMID:27066066","title":"Rif1: A Conserved Regulator of DNA Replication and Repair Hijacked by Telomeres in Yeasts.","citation":"Front Genet 2016;7:45","abstract":"Rap1-interacting factor 1 (Rif1) was originally identified in the budding yeast Saccharomyces cerevisiae as a telomere-binding protein that negatively regulates telomerase-mediated telomere elongation. Although this function is conserved in the distantly related fission yeast Schizosaccharomyces pombe, recent studies, both in yeasts and in metazoans, reveal that Rif1 also functions more globally, both in the temporal control of DNA replication and in DNA repair. Rif1 proteins are large and characterized by N-terminal HEAT repeats, predicted to form an elongated alpha-helical structure. In addition, all Rif1 homologs contain two short motifs, abbreviated RVxF/SILK, that are implicated in recruitment of the PP1 (yeast Glc7) phosphatase. In yeasts the RVxF/SILK domains have been shown to play a role in control of DNA replication initiation, at least in part through targeted de-phosphorylation of proteins in the pre-Replication Complex. In human cells Rif1 is recruited to DNA double-strand breaks through an interaction with 53BP1 where it counteracts DNA resection, thus promoting repair by non-homologous end-joining. This function requires the N-terminal HEAT repeat-containing domain. Interestingly, this domain is also implicated in DNA end protection at un-capped telomeres in yeast. We conclude by discussing the deployment of Rif1 at telomeres in yeasts from both an evolutionary perspective and in light of its recently discovered global functions.","doi":"10.3389/fgene.2016.00045","authors":"Mattarocci S, Hafner L, Lezaja A, Shyian M, Shore D","authors_abbrev":"Mattarocci S et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-04-12","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-04-13 00:15:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.17","SPBC1778.02"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"GO_REF:0000101","title":"Automated transfer of experimentally-verified GO annotation data to close orthologs","abstract":"This reference is used to describe functional annotations transferred from one or more reference (\"source\") organisms to a newly annotated (\"target\") organism on the basis of ortholog cluster membership. In detail, predicted (e.g. by AUGUSTUS, see doi:10.1186/1471-2105-7-62) or transferred (e.g. via RATT, see doi:10:1093/nar/gkg1268) gene models in the target genome are translated and processed by OrthoMCL 1.4 together with reference protein sequences to produce clusters of gene products derived from orthologous genes. For each cluster, GO terms are automatically transferred from source products to the target gene products if they are experimentally verified (IDA (ECO:0000314), IMP (ECO:0000315), IPI (ECO:0000353), IGI (ECO:0000316), (EXP ECO:0000269). They are tagged with the ISO evidence code and the \"with/from\" is populated with the source feature references (e.g. \"GeneDB:LmjF.28.0960\"). OrthoMCL runs are done using the parameterization suggested in the OrthoMCL algorithm document (blastall -F 'm S' -e 1e-5).","authors":"Sascha Steinbiss, GeneDB curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10922370","title":"The Saccharomyces cerevisiae PCD1 gene encodes a peroxisomal nudix hydrolase active toward coenzyme A and its derivatives.","citation":"J Biol Chem 2000 Oct 20;275(42):32925-30","abstract":"The PCD1 nudix hydrolase gene of Saccharomyces cerevisiae has been cloned and the Pcd1p protein characterized as a diphosphatase (pyrophosphatase) with specificity for coenzyme A and CoA derivatives. Oxidized CoA disulfide is preferred over CoA as a substrate with K(m) and k(cat) values of 24 micrometer and 5.0 s(-1), respectively, compared with values for CoA of 280 micrometer and 4.6 s(-1) respectively. The products of CoA hydrolysis were 3'-phosphoadenosine 5'-monophosphate and 4'-phosphopantetheine. F(-) ions inhibited the activity with an IC(50) of 22 micrometer. The sequence of Pcd1p contains a potential PTS2 peroxisomal targeting signal. When fused to the N terminus of yeast-enhanced green fluorescent protein, Pcd1p was shown to locate to peroxisomes by confocal microscopy. It was also shown to co-localize with peroxisomal thiolase by immunofluorescence microscopy. N-terminal sequence analysis of the expressed protein revealed the loss of 7 or 8 amino acids, suggesting processing of the proposed PTS2 signal after import. The function of Pcd1p may be to remove potentially toxic oxidized CoA disulfide from peroxisomes in order to maintain the capacity for beta-oxidation of fatty acids.","authors":"Cartwright JL, Gasmi L, Spiller DG, McLennan AG","authors_abbrev":"Cartwright JL et al.","pubmed_publication_date":"20 Oct 2000","pubmed_entrez_date":"2000-08-03","publication_year":"2000","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6G9.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9606213","title":"FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation.","citation":"J Cell Biol 1998 Jun 01;141(5):1217-28","abstract":"Formins are involved in diverse aspects of morphogenesis, and share two regions of homology: FH1 and FH2. We describe a new formin homology region, FH3. FH3 is an amino-terminal domain that differs from the Rho binding site identified in Bni1p and p140mDia. The Schizosaccharomyces pombe formin Fus1 is required for conjugation, and is localized to the projection tip in cells of mating pairs. We replaced genomic fus1+ with green fluorescent protein (GFP)- tagged versions that lacked either the FH1, FH2, or FH3 domain. Deletion of any FH domain essentially abolished mating. FH3, but neither FH1 nor FH2, was required for Fus1 localization. An FH3 domain-GFP fusion protein localized to the projection tips of mating pairs. Thus, the FH3 domain alone can direct protein localization. The FH3 domains of both Fus1 and the S. pombe cytokinesis formin Cdc12 were able to localize GFP to the spindle pole body in half of the late G2 cells in a vegetatively growing population. Expression of both FH3-GFP fusions also affected cytokinesis. Overexpression of the spindle pole body component Sad1 altered the distribution of both Sad1 and the FH3-GFP domain. Together these data suggest that proteins at multiple sites can interact with FH3 domains.","authors":"Petersen J, Nielsen O, Egel R, Hagan IM","authors_abbrev":"Petersen J et al.","pubmed_publication_date":"01 Jun 1998","pubmed_entrez_date":"1998-06-12","publication_year":"1998","canto_session_key":"0d2e132805615e6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-03-03 10:33:29","canto_approved_date":"2022-11-14 13:52:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-24 14:37:32","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.02c","SPAC11H11.04","SPBC32H8.12c","SPAC4A8.15c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2021-03-03"},{"uniquename":"Pfam:PF12632","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21B10.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21131906","title":"Dma1 ubiquitinates the SIN scaffold, Sid4, to impede the mitotic localization of Plo1 kinase.","citation":"EMBO J 2011 Jan 19;30(2):341-54","abstract":"Proper cell division requires strict coordination between mitotic exit and cytokinesis. In the event of a mitotic error, cytokinesis must be inhibited to ensure equal partitioning of genetic material. In the fission yeast, Schizosaccharomyces pombe, the checkpoint protein and E3 ubiquitin ligase, Dma1, delays cytokinesis by inhibiting the septation initiation network (SIN) when chromosomes are not attached to the mitotic spindle. To elucidate the mechanism by which Dma1 inhibits the SIN, we screened all SIN components as potential Dma1 substrates and found that the SIN scaffold protein, Sid4, is ubiquitinated in vivo in a Dma1-dependent manner. To investigate the role of Sid4 ubiquitination in checkpoint function, a ubiquitination deficient sid4 allele was generated and our data indicate that Sid4 ubiquitination by Dma1 is required to prevent cytokinesis during a mitotic checkpoint arrest. Furthermore, Sid4 ubiquitination delays recruitment of the Polo-like kinase and SIN activator, Plo1, to spindle pole bodies (SPBs), while at the same time prolonging residence of the SIN inhibitor, Byr4, providing a mechanistic link between Dma1 activity and cytokinesis inhibition.","doi":"10.1038/emboj.2010.317","authors":"Johnson AE, Gould KL","authors_abbrev":"Johnson AE et al.","pubmed_publication_date":"19 Jan 2011","pubmed_entrez_date":"2010-12-07","publication_year":"2011","canto_session_key":"c2aaa605ef48b5f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2019-02-02 16:30:31","canto_approved_date":"2026-06-09 07:12:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-16 08:16:31","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC649.05","SPCC1739.11c","SPAC17G8.10c","SPAC1565.06c","SPAC4H3.11c","SPAC6F6.08c","SPBC21.06c","SPBC24C6.07","SPAC23C11.16","SPAC9G1.09","SPAC24B11.11c","SPAC222.10c","SPBC428.13c","SPBC244.01c"],"gene_count":14,"ltp_gene_count":4,"approved_date":"2019-02-02"},{"uniquename":"PMID:19023408","title":"Indistinguishable landscapes of meiotic DNA breaks in rad50+ and rad50S strains of fission yeast revealed by a novel rad50+ recombination intermediate.","citation":"PLoS Genet 2008 Nov;4(11):e1000267","abstract":"The fission yeast Schizosaccharomyces pombe Rec12 protein, the homolog of Spo11 in other organisms, initiates meiotic recombination by creating DNA double-strand breaks (DSBs) and becoming covalently linked to the DNA ends of the break. This protein-DNA linkage has previously been detected only in mutants such as rad50S in which break repair is impeded and DSBs accumulate. In the budding yeast Saccharomyces cerevisiae, the DSB distribution in a rad50S mutant is markedly different from that in wild-type (RAD50) meiosis, and it was suggested that this might also be true for other organisms. Here, we show that we can detect Rec12-DNA linkages in Sc. pombe rad50(+) cells, which are proficient for DSB repair. In contrast to the results from Sa. cerevisiae, genome-wide microarray analysis of Rec12-DNA reveals indistinguishable meiotic DSB distributions in rad50(+) and rad50S strains of Sc. pombe. These results confirm our earlier findings describing the occurrence of widely spaced DSBs primarily in large intergenic regions of DNA and demonstrate the relevance and usefulness of fission yeast studies employing rad50S. We propose that the differential behavior of rad50S strains reflects a major difference in DSB regulation between the two species--specifically, the requirement for the Rad50-containing complex for DSB formation in budding yeast but not in fission yeast. Use of rad50S and related mutations may be a useful method for DSB analysis in other species.","doi":"10.1371/journal.pgen.1000267","authors":"Hyppa RW, Cromie GA, Smith GR","authors_abbrev":"Hyppa RW et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-11-22","publication_year":"2008","canto_session_key":"9e870ff297c803f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-02-02 14:03:32","canto_approved_date":"2025-09-02 17:29:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-02 14:00:46","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPAC664.01c","SPAC1556.01c","SPAC20H4.07"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-02-02"},{"uniquename":"PMID:29466359","title":"CDK activity provides temporal and quantitative cues for organizing genome duplication.","citation":"PLoS Genet 2018 Feb;14(2):e1007214","abstract":"In eukaryotes, the spatial and temporal organization of genome duplication gives rise to distinctive profiles of replication origin usage along the chromosomes. While it has become increasingly clear that these programs are important for cellular physiology, the mechanisms by which they are determined and modulated remain elusive. Replication initiation requires the function of cyclin-dependent kinases (CDKs), which associate with various cyclin partners to drive cell proliferation. Surprisingly, although we possess detailed knowledge of the CDK regulators and targets that are crucial for origin activation, little is known about whether CDKs play a critical role in establishing the genome-wide pattern of origin selection. We have addressed this question in the fission yeast, taking advantage of a simplified cell cycle network in which cell proliferation is driven by a single cyclin-CDK module. This system allows us to precisely control CDK activity in vivo using chemical genetics. First, in contrast to previous reports, our results clearly show that distinct cyclin-CDK pairs are not essential for regulating specific subsets of origins and for establishing a normal replication program. Importantly, we then demonstrate that the timing at which CDK activity reaches the S phase threshold is critical for the organization of replication in distinct efficiency domains, while the level of CDK activity at the onset of S phase is a dose-dependent modulator of overall origin efficiencies. Our study therefore implicates these different aspects of CDK regulation as versatile mechanisms for shaping the architecture of DNA replication across the genome.","doi":"10.1371/journal.pgen.1007214","authors":"Perrot A, Millington CL, Gómez-Escoda B, Schausi-Tiffoche D, Wu PJ","authors_abbrev":"Perrot A et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2018-02-22","publication_year":"2018","canto_session_key":"9796274ccbc96683","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-11-26 11:01:18","canto_approved_date":"2018-11-26 11:01:18","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-11-13 17:54:41","canto_added_date":"2018-02-28 22:13:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2018-11-26"},{"uniquename":"PMID:15664183","title":"MAPKAP kinase-2: three's company at the G(2) checkpoint.","citation":"Mol Cell 2005 Jan 21;17(2):163-4","abstract":"Elegant studies in fission yeast by and in mammalian cells by offer new insights into the mechanism through which stress-induced p38 activation inhibits mitotic entry in eukaryotic cells.","authors":"Abraham RT","authors_abbrev":"Abraham RT","pubmed_publication_date":"21 Jan 2005","pubmed_entrez_date":"2005-01-25","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28450455","title":"MAARS: a novel high-content acquisition software for the analysis of mitotic defects in fission yeast.","citation":"Mol Biol Cell 2017 Jun 15;28(12):1601-1611","abstract":"Faithful segregation of chromosomes during cell division relies on multiple processes such as chromosome attachment and correct spindle positioning. Yet mitotic progression is defined by multiple parameters, which need to be quantitatively evaluated. To study the spatiotemporal control of mitotic progression, we developed a high-content analysis (HCA) approach that combines automated fluorescence microscopy with real-time quantitative image analysis and allows the unbiased acquisition of multiparametric data at the single-cell level for hundreds of cells simultaneously. The Mitotic Analysis and Recording System (MAARS) provides automatic and quantitative single-cell analysis of mitotic progression on an open-source platform. It can be used to analyze specific characteristics such as cell shape, cell size, metaphase/anaphase delays, and mitotic abnormalities including spindle mispositioning, spindle elongation defects, and chromosome segregation defects. Using this HCA approach, we were able to visualize rare and unexpected events of error correction during anaphase in wild-type or mutant cells. Our study illustrates that such an expert system of mitotic progression is able to highlight the complexity of the mechanisms required to prevent chromosome loss during cell division.","doi":"10.1091/mbc.E16-10-0723","authors":"Li T, Mary H, Grosjean M, Fouchard J, Cabello S, Reyes C, Tournier S, Gachet Y","authors_abbrev":"Li T et al.","pubmed_publication_date":"15 Jun 2017","pubmed_entrez_date":"2017-04-29","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-05-01 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:714017","title":"Extrachromosomal inheritance in Schizosaccharomyces pombe. VII. Studies by zygote clone analysis on transmission, segregation, recombination, and uniparental inheritance of mitochondrial markers conferring resistance to antimycin, chloramphenicol, and erythromycin.","citation":"Mol Gen Genet 1978 Sep 08;164(3):309-20","abstract":"Crosses involving mitochondrial markers conferring resistance to antimycin (anar, AR), chloramphenicol (capr, CR), and erythromycin (eryr, ER) in cis- and trans-configuration were studied by zygote clone analysis. Mutant anar-8, from which all other drug--resistant isolates were derived, exhibits a highly biased transmission (6.8% anar) in an analysis of 100 individual zygote clones. Important results of zygote clone analyses were:--Zygote clones may contain one, two, three, or four mitochondrial genotypes.--The proportion of the two parental and the two recombinant genotypes in individual zygote clones can vary almost over the entire range of percentages.--Proportions of the two corresponding recombinant types in individual clones are usually unequal.--Transmission rates of markers are higher in trans- than in cis-crosses, indicating additivity of bias by two mutated alleles in coupling.--Transmission rates are different for the three markers both in cis- and trans-crosses, being lowest for CR and highest for ER.--Up to more than 80% uniform clones, expressing only one genotype, can be produced in cis- and trans-crosses. In cis-crosses always the double-sensitive parental type becomes uniform, in trans-crosses this may be the case for parental and/or recombinant genotypes. A tentative map is presented using data from cis- and trans-crosses, including a correction by omission of uniform clones. Phenomena of transmission, segregation, and formation of uniform clones are discussed with special regard to the difference brought about by fission versus budding. A comparison with relevant data from Saccharomyces cerevisiae and other organisms is presented.","authors":"Seitz-Mayr G, Wolf K, Kaudewitz F","authors_abbrev":"Seitz-Mayr G et al.","pubmed_publication_date":"08 Sep 1978","pubmed_entrez_date":"1978-09-08","publication_year":"1978","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9535840","title":"Processing of the presequence of the Schizosaccharomyces pombe Rieske iron-sulfur protein occurs in a single step and can be converted to two-step processing by mutation of a single proline to serine in the presequence.","citation":"J Biol Chem 1998 Apr 10;273(15):8652-8","abstract":"The iron-sulfur proteins of the cytochrome bc1 complexes of Schizosaccharomyces pombe and Saccharomyces cerevisiae contain the three amino acid motif RX( downward arrow)(F/L/I)XX(T/S/G)XXXX (downward arrow) that is typical for proteins that are cleaved sequentially in two steps by matrix processing peptidase (MPP) and mitochondrial intermediate peptidase (MIP). Despite the presence of this recognition sequence the S. pombe iron-sulfur protein is processed only once during import into mitochondria, whereas the S. cerevisiae protein is processed in two steps. Import of S. pombe iron-sulfur protein in which the putative MIP or MPP recognition sites are eliminated by site-directed mutagenesis and import of iron-sulfur protein into mitochondria from yeast mutants that lack MIP activity indicate that one step processing of the S. pombe iron-sulfur protein is independent of those sites and of MIP activity. Sequencing of the mature protein obtained after import in vitro and of the endogenous iron-sulfur protein isolated from mitochondrial membranes by preparative 2D-electrophoresis shows that MPP recognizes a second site in the presequence and processing occurs between residues 43 and 44. If proline-20 of the S. pombe presequence is changed into a serine, a second cleavage step is induced. Conversely, if serine-24 of the S. cerevisiae presequence is changed to a proline, the first cleavage step that is normally catalyzed by MPP is blocked, causing precursor iron-sulfur protein to accumulate. Together these results indicate that a single amino acid change in the presequence is responsible for one-step processing in S. pombe versus two-step processing in S. cerevisiae.","authors":"Nett JH, Schägger H, Trumpower BL","authors_abbrev":"Nett JH et al.","pubmed_publication_date":"10 Apr 1998","pubmed_entrez_date":"1998-05-16","publication_year":"1998","canto_session_key":"79bf98abb0a7788b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-02-06 14:28:58","canto_approved_date":"2023-07-05 11:29:00","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2020-02-06 14:28:43","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16H5.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2020-02-06"},{"uniquename":"PMID:15611163","title":"Differential activation of eIF2 kinases in response to cellular stresses in Schizosaccharomyces pombe.","citation":"Genetics 2004 Dec;168(4):1867-75","abstract":"Phosphorylation of eukaryotic initiation factor-2 (eIF2) is an important mechanism mitigating cellular injury in response to diverse environmental stresses. While all eukaryotic organisms characterized to date contain an eIF2 kinase stress response pathway, the composition of eIF2 kinases differs, with mammals containing four distinct family members and the well-studied lower eukaryote Saccharomyces cerevisiae expressing only a single eIF2 kinase. We are interested in the mechanisms by which multiple eIF2 kinases interface with complex stress signals and elicit response pathways. In this report we find that in addition to two previously described eIF2 kinases related to mammalian HRI, designated Hri1p and Hri2p, the yeast Schizosaccharomyces pombe expresses a third eIF2 kinase, a Gcn2p ortholog. To delineate the roles of each eIF2 kinase, we constructed S. pombe strains expressing only a single eIF2 kinase gene or deleted for the entire eIF2 kinase family. We find that Hri2p is the primary activated eIF2 kinase in response to exposure to heat shock, arsenite, or cadmium. Gcn2p serves as the primary eIF2 kinase induced during a nutrient downshift, treatment with the amino acid biosynthetic inhibitor 3-aminotriazole, or upon exposure to high concentrations of sodium chloride. In one stress example, exposure to H(2)O(2), there is early tandem activation of both Hri2p and Gcn2p. Interestingly, with extended stress conditions there is activation of alternative secondary eIF2 kinases, suggesting that eukaryotes have mechanisms of coordinate activation of eIF2 kinase in their stress remediation responses. Deletion of these eIF2 kinases renders S. pombe more sensitive to many of these stress conditions.","authors":"Zhan K, Narasimhan J, Wek RC","authors_abbrev":"Zhan K et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-12-22","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24925530","title":"Tpz1TPP1 SUMOylation reveals evolutionary conservation of SUMO-dependent Stn1 telomere association.","citation":"EMBO Rep 2014 Aug;15(8):871-7","abstract":"Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang-binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang-binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO-Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation.","doi":"10.15252/embr.201438919","authors":"Garg M, Gurung RL, Mansoubi S, Ahmed JO, Davé A, Watts FZ, Bianchi A","authors_abbrev":"Garg M et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-06-14","publication_year":"2014","canto_session_key":"9c76de107a5d2e55","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alessandro Bianchi","canto_first_approved_date":"2017-02-21 17:24:53","canto_approved_date":"2026-01-21 13:42:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-07 19:58:38","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Alessandro Bianchi","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":38,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.17","SPBC409.12c","SPCC1393.14","SPAC19G12.13c","SPCC23B6.03c","SPCC126.02c","SPAC16A10.07c","SPAC16A10.06c","SPAC30D11.10","SPAC1687.05","SPCC188.07","SPBC29A3.14c","SPBC365.06","SPAC6F6.16c","SPBC1778.02","SPAC26H5.06"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2017-02-21"},{"uniquename":"PMID:30814334","title":"Import of extracellular ATP in yeast and man modulates AMPK and TORC1 signalling.","citation":"J Cell Sci 2019 Apr 03;132(7)","abstract":"AMP-activated kinase (AMPK) and target of rapamycin (TOR) signalling coordinate cell growth, proliferation, metabolism and cell survival with the nutrient environment of cells. The poor vasculature and nutritional stress experienced by cells in solid tumours raises the question: how do they assimilate sufficient nutrients to survive? Here, we show that human and fission yeast cells import ATP and AMP from their external environment to regulate AMPK and TOR signalling. Exposure of fission yeast ( Schizosaccharomyces pombe ) and human cells to external AMP impeded cell growth; however, in yeast this restraining impact required AMPK. In contrast, external ATP rescued the growth defect of yeast mutants with reduced TORC1 signalling; furthermore, exogenous ATP transiently enhanced TORC1 signalling in both yeast and human cell lines. Addition of the PANX1 channel inhibitor probenecid blocked ATP import into human cell lines suggesting that this channel may be responsible for both ATP release and uptake in mammals. In light of these findings, it is possible that the higher extracellular ATP concentration reported in solid tumours is both scavenged and recognized as an additional energy source beneficial for cell growth.","doi":"10.1242/jcs.223925","authors":"Forte GM, Davie E, Lie S, Franz-Wachtel M, Ovens AJ, Wang T, Oakhill JS, Maček B, Hagan IM, Petersen J","authors_abbrev":"Forte GM et al.","pubmed_publication_date":"03 Apr 2019","pubmed_entrez_date":"2019-03-01","publication_year":"2019","canto_session_key":"300317113fa0edf5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-03-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.13c","SPAC22F3.13","SPCC74.03c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:25891397","title":"The critical glucose concentration for respiration-independent proliferation of fission yeast, Schizosaccharomyces pombe.","citation":"Mitochondrion 2015 May;22:91-5","abstract":"Glucose is the fundamental energy source for life; thus cells need to respond appropriately to changes in available glucose concentration. We investigated the relationship between media glucose concentration and respiration-dependency of proliferation, using Schizosaccharomyces pombe. In media containing ≥ 0.2% glucose, neither antimycin A, an inhibitor of Complex III, nor gene deletions of essential electron transfer chain components, impaired cell division, while these factors completely inhibited cell division in media containing ≤ 0.1% glucose. These results indicate the existence of a threshold in glucose concentration that governs respiration-dependency of S. pombe proliferation.","doi":"10.1016/j.mito.2015.04.003","authors":"Takeda K, Starzynski C, Mori A, Yanagida M","authors_abbrev":"Takeda K et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-04-21","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-04-23 00:19:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21314938","title":"Auxin-inducible protein depletion system in fission yeast.","citation":"BMC Cell Biol 2011 Feb 11;12:8","abstract":"Inducible inactivation of a protein is a powerful approach for analysis of its function within cells. Fission yeast is a useful model for studying the fundamental mechanisms such as chromosome maintenance and cell cycle. However, previously published strategies for protein-depletion are successful only for some proteins in some specific conditions and still do not achieve efficient depletion to cause acute phenotypes such as immediate cell cycle arrest. The aim of this work was to construct a useful and powerful protein-depletion system in Shizosaccaromyces pombe.\nWe constructed an auxin-inducible degron (AID) system, which utilizes auxin-dependent poly-ubiquitination of Aux/IAA proteins by SCFTIR1 in plants, in fission yeast. Although expression of a plant F-box protein, TIR1, decreased Mcm4-aid, a component of the MCM complex essential for DNA replication tagged with Aux/IAA peptide, depletion did not result in an evident growth defect. We successfully improved degradation efficiency of Mcm4-aid by fusion of TIR1 with fission yeast Skp1, a conserved F-box-interacting component of SCF (improved-AID system; i-AID), and the cells showed severe defect in growth. The i-AID system induced degradation of Mcm4-aid in the chromatin-bound MCM complex as well as those in soluble fractions. The i-AID system in conjunction with transcription repression (off-AID system), we achieved more efficient depletion of other proteins including Pol1 and Cdc45, causing early S phase arrest.\nImprovement of the AID system allowed us to construct conditional null mutants of S. pombe. We propose that the off-AID system is the powerful method for in vivo protein-depletion in fission yeast.","doi":"10.1186/1471-2121-12-8","authors":"Kanke M, Nishimura K, Kanemaki M, Kakimoto T, Takahashi TS, Nakagawa T, Masukata H","authors_abbrev":"Kanke M et al.","pubmed_publication_date":"11 Feb 2011","pubmed_entrez_date":"2011-02-15","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32282918","title":"Genetic interactions and transcriptomics implicate fission yeast CTD prolyl isomerase Pin1 as an agent of RNA 3' processing and transcription termination that functions via its effects on CTD phosphatase Ssu72.","citation":"Nucleic Acids Res 2020 May 21;48(9):4811-4826","abstract":"The phosphorylation pattern of Pol2 CTD Y1S2P3T4S5P6S7 repeats comprises an informational code coordinating transcription and RNA processing. cis-trans isomerization of CTD prolines expands the scope of the code in ways that are not well understood. Here we address this issue via analysis of fission yeast peptidyl-prolyl isomerase Pin1. A pin1Δ allele that does not affect growth per se is lethal in the absence of cleavage-polyadenylation factor (CPF) subunits Ppn1 and Swd22 and elicits growth defects absent CPF subunits Ctf1 and Dis2 and termination factor Rhn1. Whereas CTD S2A, T4A, and S7A mutants thrive in combination with pin1Δ, a Y1F mutant does not, nor do CTD mutants in which half the Pro3 or Pro6 residues are replaced by alanine. Phosphate-acquisition genes pho1, pho84 and tgp1 are repressed by upstream lncRNAs and are sensitive to changes in lncRNA 3' processing/termination. pin1Δ hyper-represses PHO gene expression and erases the de-repressive effect of CTD-S7A. Transcriptional profiling delineated sets of 56 and 22 protein-coding genes that are down-regulated and up-regulated in pin1Δ cells, respectively, 77% and 100% of which are downregulated/upregulated when the cis-proline-dependent Ssu72 CTD phosphatase is inactivated. Our results implicate Pin1 as a positive effector of 3' processing/termination that acts via Ssu72.","doi":"10.1093/nar/gkaa212","authors":"Sanchez AM, Garg A, Shuman S, Schwer B","authors_abbrev":"Sanchez AM et al.","pubmed_publication_date":"21 May 2020","pubmed_entrez_date":"2020-04-14","publication_year":"2020","canto_session_key":"ff1e67fe7824549f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2022-11-28 14:18:05","canto_approved_date":"2024-11-13 12:04:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-22 22:47:59","canto_added_date":"2020-04-15 00:15:04","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":285,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.05c","SPAC13D6.01","SPBC776.02c","SPBC1709.14","SPAC824.04","SPBC29B5.02c","SPCC1672.06c","SPBC1683.09c","SPCC794.03","SPAC1565.04c","SPBC19C7.04c","SPBC32C12.02","SPBC106.02c","SPAC23C4.19","SPCC70.08c","SPBC947.04","SPAC513.03","SPBC28F2.12","SPBC8E4.01c","SPAC186.05c","SPAC27D7.11c","SPBC713.05","SPBC337.03","SPBC2G2.15c","SPAC1039.02","SPAC343.12","SPBC12D12.02c","SPBC3B9.11c","SPAC1B3.04c","SPBP4G3.02","SPAC23H3.15c","SPBC29A3.18","SPCC1223.03c","SPCC18B5.01c","SPBC1703.08c","SPAC15E1.02c","SPAC3A11.07","SPAC11H11.04","SPAC27D7.14c","SPAC13G6.14","SPBC725.10","SPBP23A10.15c","SPAPJ695.02","SPCC569.09","SPAC56F8.15","SPAC1F7.07c","SPBC11C11.06c","SPAC977.16c","SPBC23E6.03c","SPBC1685.17","SPBC8E4.12c","SPBC1709.13c","SPAC11E3.06","SPAC25B8.12c","SPAC18G6.12c","SPACUNK4.17","SPCC794.04c","SPCC1020.09","SPBC428.07","SPAC1399.02","SPAC688.06c","SPBC1861.02","SPAC3G9.04","SPCC645.02","SPAC186.01","SPAC2H10.01","SPAC9E9.09c","SPAC13G7.13c","SPBC1703.13c","SPBC16A3.13","SPBC354.12","SPAC750.01","SPAC1F7.08","SPCC16C4.03","SPBPB2B2.01","SPAC31G5.09c","SPCC794.01c","SPAC27D7.09c","SPAC13A11.06","SPCC74.02c","SPBPB8B6.04c","SPCC622.12c","SPBC1271.09","SPBC530.10c","SPBC83.13","SPAC1782.07","SPCC70.02c","SPAC27D7.03c","SPBC4F6.09","SPAC11D3.01c"],"gene_count":90,"ltp_gene_count":10,"approved_date":"2022-11-28"},{"uniquename":"PMID:34157114","title":"Rrp1 translocase and ubiquitin ligase activities restrict the genome destabilising effects of Rad51 in fission yeast.","citation":"Nucleic Acids Res 2021 Jul 09;49(12):6832-6848","abstract":"Rad51 is the key protein in homologous recombination that plays important roles during DNA replication and repair. Auxiliary factors regulate Rad51 activity to facilitate productive recombination, and prevent inappropriate, untimely or excessive events, which could lead to genome instability. Previous genetic analyses identified a function for Rrp1 (a member of the Rad5/16-like group of SWI2/SNF2 translocases) in modulating Rad51 function, shared with the Rad51 mediator Swi5-Sfr1 and the Srs2 anti-recombinase. Here, we show that Rrp1 overproduction alleviates the toxicity associated with excessive Rad51 levels in a manner dependent on Rrp1 ATPase domain. Purified Rrp1 binds to DNA and has a DNA-dependent ATPase activity. Importantly, Rrp1 directly interacts with Rad51 and removes it from double-stranded DNA, confirming that Rrp1 is a translocase capable of modulating Rad51 function. Rrp1 affects Rad51 binding at centromeres. Additionally, we demonstrate in vivo and in vitro that Rrp1 possesses E3 ubiquitin ligase activity with Rad51 as a substrate, suggesting that Rrp1 regulates Rad51 in a multi-tiered fashion.","doi":"10.1093/nar/gkab511","authors":"Muraszko J, Kramarz K, Argunhan B, Ito K, Baranowska G, Kurokawa Y, Murayama Y, Tsubouchi H, Lambert S, Iwasaki H, Dziadkowiec D","authors_abbrev":"Muraszko J et al.","pubmed_publication_date":"09 Jul 2021","pubmed_entrez_date":"2021-06-22","publication_year":"2021","canto_session_key":"1e356348936e6132","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-24 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A2.12","SPAC644.14c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:3104606","title":"Examination of protein sequence homologies: III. Ribosomal protein YS25 from Saccharomyces cerevisiae and its counterparts from Schizosaccharomyces pombe, rat liver, and Escherichia coli.","citation":"J Mol Evol 1986;23(4):337-42","abstract":"The sequences of the ribosomal proteins YS25, SP-S28, RL-S21, and Ec-S6, from Saccharomyces cerevisiae, Schizosaccharomyces pombe, rat liver, and Escherichia coli, respectively, have been examined using a computer program that searches for homologous tertiary structures. Matrices of comparisons among the eukaryotic sequences show that they match each other sequentially without any internal gaps. The average values of the correlation coefficients obtained from the comparison matrices are higher for the first halves of the sequences than for the latter halves. This result suggests that the first halves of the sequences may represent a more important domain than the latter halves. The comparison matrices between the eukaryotic and bacterial sequences of ribosomal proteins, however, do not show sequentially arranged homology, though there are six well-matching segments arranged in different orders in the two types of sequences. This implies that the eukaryotic sequences of the ribosomal protein were reconstituted by two internal transpositions and six deletions of 4-12 residues each from the ancestral sequence during the divergence between bacterial and eukaryotic genes. These findings may give insight into structural and quantitative studies of evolutionary divergence between eukaryotes and prokaryotes.","authors":"Otaka E, Ooi T, Itoh T, Kumazaki T","authors_abbrev":"Otaka E et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_session_key":"34aa5f6f541d7f0d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-09 15:33:30","canto_approved_date":"2019-01-09 15:33:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-09 15:33:22","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-09"},{"uniquename":"PMID:18187560","title":"Hydrogen peroxide-induced gene expression across kingdoms: a comparative analysis.","citation":"Mol Biol Evol 2008 Mar;25(3):507-16","abstract":"Cells react to oxidative stress conditions by launching a defense response through the induction of nuclear gene expression. The advent of microarray technologies allowed monitoring of oxidative stress-dependent changes of transcript levels at a comprehensive and genome-wide scale, resulting in a series of inventories of differentially expressed genes in different organisms. We performed a meta-analysis on hydrogen peroxide (H(2)O(2))-induced gene expression in the cyanobacterium Synechocystis PCC 6803, the yeast Saccharomyces cerevisiae and Schizosaccharomyces pombe, the land plant Arabidopsis thaliana, and the human HeLa cell line. The H(2)O(2)-induced gene expression in both yeast species was highly conserved and more similar to the A. thaliana response than that of the human cell line. Based on the expression characteristics of genuine antioxidant genes, we show that the antioxidant capacity of microorganisms and higher eukaryotes is differentially regulated. Four families of evolutionarily conserved eukaryotic proteins could be identified that were H(2)O(2) responsive across kingdoms: DNAJ domain-containing heat shock proteins, small guanine triphosphate-binding proteins, Ca(2+)-dependent protein kinases, and ubiquitin-conjugating enzymes.","doi":"10.1093/molbev/msm276","authors":"Vandenbroucke K, Robbens S, Vandepoele K, Inzé D, Van de Peer Y, Van Breusegem F","authors_abbrev":"Vandenbroucke K et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-01-12","publication_year":"2008","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28180297","title":"Fission yeast Stn1 is crucial for semi-conservative replication at telomeres and subtelomeres.","citation":"Nucleic Acids Res 2017 Feb 17;45(3):1255-1269","abstract":"The CST complex is a phylogenetically conserved protein complex consisting of CTC1/Cdc13, Stn1 and Ten1 that protects telomeres on linear chromosomes. Deletion of the fission yeast homologs stn1 and ten1 results in complete telomere loss; however, the precise function of Stn1 is still largely unknown. Here, we have isolated a high-temperature sensitive stn1 allele (termed stn1-1). stn1-1 cells abruptly lost telomeric sequence almost completely at the restrictive temperature. The loss of chromosomal DNA happened without gradual telomere shortening, and extended to 30 kb from the ends of chromosomes. We found transient and modest single-stranded G-strand exposure, but did not find any evidence of checkpoint activation in stn1-1 at the restrictive temperature. When we probed neutral-neutral 2D gels for subtelomere regions, we found no Y-arc-shaped replication intermediates in cycling cells. We conclude that the loss of telomere and subtelomere DNAs in stn1-1 cells at the restrictive temperature is caused by very frequent replication fork collapses specifically in subtelomere regions. Furthermore, we identified two independent suppressor mutants of the high-temperature sensitivity of stn1-1: a multi-copy form of pmt3 and a deletion of rif1. Collectively, we propose that fission yeast Stn1 primarily safeguards the semi-conservative DNA replication at telomeres and subtelomeres.","doi":"10.1093/nar/gkw1176","authors":"Takikawa M, Tarumoto Y, Ishikawa F","authors_abbrev":"Takikawa M et al.","pubmed_publication_date":"17 Feb 2017","pubmed_entrez_date":"2017-02-10","publication_year":"2017","canto_session_key":"06fd9dfa12149262","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-11 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC776.02c","SPAC6F6.17","SPBC409.12c","SPBC365.06","SPCC31H12.05c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:12868587","title":"Ultrastructure and behavior of actin cytoskeleton during cell wall formation in the fission yeast Schizosaccharomyces pombe.","citation":"J Electron Microsc (Tokyo) 2003;52(2):161-74","abstract":"Fluorescence microscopy has shown that F-actin of the fission yeast Schizosaccharomyces pombe forms patch, cable and ring structures. To study the relationship between cell wall formation and the actin cytoskeleton, the process of cell wall regeneration from the protoplast was investigated by transmission electron microscopy (TEM), immunoelectron microscopy (IEM) and three-dimensional reconstruction analysis. During cell wall regeneration from the protoplast, localization of F-actin patches was similar to that of the newly synthesized cell wall materials, as shown by confocal laser scanning microscopy (CLSM). In serial sectioned TEM images, filasomes were spherical, 100-300 nm in diameter and consisted of a single microvesicle (35-70 nm diameter) surrounded by fine filaments. Filasomes were adjacent to the newly formed glucan fibrils in single, cluster or rosary forms. By IEM analysis, we found that colloidal gold particles indicating actin molecules were present in the filamentous area of filasomes. Three-dimensional reconstruction images of serial sections clarified that the distribution of filasomes corresponded to the distribution of F-actin patches revealed by CLSM. Thus, a filasome is one of the F-actin patch structures appearing in the cytoplasm at the site of the initial formation of the cell wall and it may play an important role in this action.","authors":"Takagi T, Ishijima SA, Ochi H, Osumi M","authors_abbrev":"Takagi T et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-07-19","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19778961","title":"Autophagy-deficient Schizosaccharomyces pombe mutants undergo partial sporulation during nitrogen starvation.","citation":"Microbiology (Reading) 2009 Dec;155(Pt 12):3816-3826","abstract":"Autophagy is triggered when organisms sense radical environmental changes, including nutritional starvation. During autophagy, cytoplasmic components, including organelles, are enclosed within autophagosomes and are degraded upon lysosome-vacuole fusion. In this study, we show that processing of GFP-tagged Atg8 can serve as a marker for autophagy in the fission yeast Schizosaccharomyces pombe. Using this marker, 13 Atg homologues were also found to be required for autophagy in fission yeast. In budding yeast, autophagy-deficient mutants are known to be sterile, whereas in fission yeast we found that up to 30 % of autophagy-defective cells with amino acid auxotrophy were able to recover sporulation when an excess of required amino acids was supplied. Furthermore, we found that approximately 15 % of the autophagy-defective cells were also able to sporulate when a prototrophic strain was subjected to nitrogen starvation, which suggested that fission yeast may store sufficient intracellular nitrogen to allow partial sporulation under nitrogen-limiting conditions, although the majority of the nitrogen source is supplied by autophagy. Monitoring of the sporulation process revealed that the process was blocked non-specifically at various stages in the atg1Delta and atg12Delta mutants, possibly due to a shortage of amino acids. Taking advantage of this partial sporulation ability of fission yeast, we sought evidence for the existence of a recycling system for nitrogen sources during starvation.","doi":"10.1099/mic.0.034389-0","authors":"Mukaiyama H, Kajiwara S, Hosomi A, Giga-Hama Y, Tanaka N, Nakamura T, Takegawa K","authors_abbrev":"Mukaiyama H et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-09-26","publication_year":"2009","canto_session_key":"0230ba8a65e7444f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-16 14:06:50","canto_approved_date":"2023-04-21 10:08:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-27 11:06:37","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":59,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC823.16c","SPAC2G11.13","SPBC1685.07c","SPCC63.08c","SPBC1A4.02c","SPAC4F10.07c","SPBC31E1.01c","SPAC19B12.08","SPBC15D4.07c","SPAC458.06","SPBP8B7.24c","SPAC589.07c","SPAC10F6.11c","SPAC20G8.10c","SPAC1783.06c","SPAC23C4.16c","SPAC3H1.09c","SPAC4A8.04","SPBC6B1.05c","SPBC4B4.10c","SPBC3B9.06c"],"gene_count":21,"ltp_gene_count":20,"approved_date":"2017-09-16"},{"uniquename":"PMID:4744878","title":"Gene-enzyme relationships in the tryptophan pathway of Schizosaccharomyces pombe.","citation":"Experientia 1973 Sep 15;29(9):1152-4","abstract":"","authors":"Schweingruber ME, Dietrich R","authors_abbrev":"Schweingruber ME et al.","pubmed_publication_date":"15 Sep 1973","pubmed_entrez_date":"1973-09-15","publication_year":"1973","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14645538","title":"Novel methyltransferase for modified uridine residues at the wobble position of tRNA.","citation":"Mol Cell Biol 2003 Dec;23(24):9283-92","abstract":"We have identified a novel tRNA methyltransferase in Saccharomyces cerevisiae that we designate Trm9. This enzyme, the product of the YML014w gene, catalyzes the esterification of modified uridine nucleotides, resulting in the formation of 5-methylcarbonylmethyluridine in tRNA(Arg3) and 5-methylcarbonylmethyl-2-thiouridine in tRNA(Glu). In intact yeast cells, disruption of the TRM9 gene results in the complete loss of these modified wobble bases and increased sensitivity at 37 degrees C to paromomycin, a translational inhibitor. These results suggest a role for this potentially reversible methyl esterification reaction when cells are under stress.","authors":"Kalhor HR, Clarke S","authors_abbrev":"Kalhor HR et al.","pubmed_publication_date":"Dec 2003","pubmed_entrez_date":"2003-12-04","publication_year":"2003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16554715","title":"Transcriptional analysis and pap1-dependence of the unique gene encoding thioredoxin reductase from the fission yeast.","citation":"J Microbiol 2006 Feb;44(1):35-41","abstract":"The unique gene encoding thioredoxin reductase (TrxR) was previously cloned and characterized from the fission yeast Schizosaccharomyces pombe, and its expression was induced by oxidative stress. To elucidate the regulatory mechanism of the S. pombe TrxR gene, three fusion plasmids were generated using polymerase chain reaction: pYUTR20, pYUTR30, and pYUTR40. Plasmid pYUTR20 has an upstream region of 891 base pairs, pYUTR30 has 499 in this region, and pYUTR40 has an 186 bp upstream region. Negatively acting sequence is located between -1,526 approximately -891 bp upstream of the gene. The upstream sequence, responsible for the induction of TrxR by menadione (MD), is situated on the -499 approximately -186 bp region, which is also required for TrxR induction by mercuric chloride. The same region also appeared to be required for Pap1-mediated transcriptional regulation of the TrxR gene, which contains the two plausible Pap1 binding sites, TTACGAAT and TTACGCGA. Consistently, basal and inducible expression of the TrxR gene was markedly lower in the Pap1-negative TP108-3C cells than in wild-type yeast cells. In summary, up-regulation of the S. pombe TrxR gene is mediated by Pap1 via the transcriptional motif( s) located on the -499 approximately -186 bp region.","authors":"Kang HJ, Hong SM, Kim BC, Kim K, Park EH, Lim CJ","authors_abbrev":"Kang HJ et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-03-24","publication_year":"2006","canto_session_key":"ddf3500ef60cfa36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-19 10:08:46","canto_approved_date":"2022-08-29 17:10:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-06 09:40:18","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPBC3F6.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-19"},{"uniquename":"PMID:10886372","title":"The Schizosaccharomyces pombe spo6+ gene encoding a nuclear protein with sequence similarity to budding yeast Dbf4 is required for meiotic second division and sporulation.","citation":"Genes Cells 2000 Jun;5(6):463-79","abstract":"Sporulation of the fission yeast Schizosaccharomyces pombe is a cell differentiation process which accompanies meiosis. The spo6+ gene was identified as a sporulation-specific gene, whose transcription was regulated by the forkhead family transcription factor Mei4.\nspo6+ encodes a protein with sequence similarity to Saccharomyces cerevisiae Dbf4p, which is required for the initiation of DNA replication. However, doubling time and cell morphology of spo6 deletion mutants and spo6-cDNA over-expressing cells were indistinguishable from wild-type cells. Spliced mature mRNAs of spo6+ appeared when diploid cells committed to meiosis. Spo6p fused to green fluorescent protein (GFP) preferentially localized in a nucleus. Although spo6Delta diploids normally underwent premeiotic DNA replication and meiosis-I, approximately 80% of cells were blocked at the binucleate stage during meiosis and virtually no asci were formed. Anti-tubulin staining revealed that only 25% of the binucleate cells assembled spindle microtubules for meiosis-II. In a small number of tetranucleate cells, sister nuclei insufficiently separated and spindles were frequently fragmented. The meiosis-II arrest phenotype was exaggerated at low temperature and in the presence of caffeine.\nThese results indicate that Spo6p is a novel Dbf4-related nuclear protein, which is expressed during meiosis and is indispensable for normal progression of meiosis-II and sporulation.","authors":"Nakamura T, Kishida M, Shimoda C","authors_abbrev":"Nakamura T et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-07-25","publication_year":"2000","canto_session_key":"c41da3dd62aad5eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-01 12:09:48","canto_approved_date":"2026-01-06 17:45:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-22 08:28:13","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.04","SPBC776.12c","SPCC550.13"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-06-01"},{"uniquename":"PMID:27354703","title":"Evolving specificity of tRNA 3-methyl-cytidine-32 (m3C32) modification: a subset of tRNAsSer requires N6-isopentenylation of A37.","citation":"RNA 2016 Sep;22(9):1400-10","abstract":"Post-transcriptional modifications of anticodon loop (ACL) nucleotides impact tRNA structure, affinity for the ribosome, and decoding activity, and these activities can be fine-tuned by interactions between nucleobases on either side of the anticodon. A recently discovered ACL modification circuit involving positions 32, 34, and 37 is disrupted by a human disease-associated mutation to the gene encoding a tRNA modification enzyme. We used tRNA-HydroSeq (-HySeq) to examine (3)methyl-cytidine-32 (m(3)C32), which is found in yeast only in the ACLs of tRNAs(Ser) and tRNAs(Thr) In contrast to that reported for Saccharomyces cerevisiae in which all m(3)C32 depends on a single gene, TRM140, the m(3)C32 of tRNAs(Ser) and tRNAs(Thr) of the fission yeast S. pombe, are each dependent on one of two related genes, trm140(+) and trm141(+), homologs of which are found in higher eukaryotes. Interestingly, mammals and other vertebrates contain a third homolog and also contain m(3)C at new sites, positions 32 on tRNAs(Arg) and C47:3 in the variable arm of tRNAs(Ser) More significantly, by examining S. pombe mutants deficient for other modifications, we found that m(3)C32 on the three tRNAs(Ser) that contain anticodon base A36, requires N(6)-isopentenyl modification of A37 (i(6)A37). This new C32-A37 ACL circuitry indicates that i(6)A37 is a pre- or corequisite for m(3)C32 on these tRNAs. Examination of the tRNA database suggests that such circuitry may be more expansive than observed here. The results emphasize two contemporary themes, that tRNA modifications are interconnected, and that some specific modifications on tRNAs of the same anticodon identity are species-specific.","doi":"10.1261/rna.056259.116","authors":"Arimbasseri AG, Iben J, Wei FY, Rijal K, Tomizawa K, Hafner M, Maraia RJ","authors_abbrev":"Arimbasseri AG et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-06-30","publication_year":"2016","canto_session_key":"e51cd4d3b32419b9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-01 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21C3.07c","SPBC3H7.11"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12928332","title":"Distinct centromere domain structures with separate functions demonstrated in live fission yeast cells.","citation":"J Cell Sci 2003 Oct 01;116(Pt 19):4035-42","abstract":"Fission yeast (Saccharomyces pombe) centromere DNA is organized in a central core region flanked on either side by a region of outer repeat (otr) sequences. The otr region is known to be heterochromatic and bound by the Swi6 protein whereas the central core region contains an unusual chromatin structure involving the histone H3 variant Cnp1 (S. pombe CENP-A). The central core is the base for formation of the kinetochore structure whereas the flanking region is important for sister centromere cohesion. We have previously shown that the ultrastructural domain structure of S. pombe centromeres in interphase is similar to that of human centromeres. Here we demonstrate that S. pombe centromeres are organized in cytologically distinct domains even in mitosis. Fluorescence in situ hybridization of fixed metaphase cells revealed that the otr regions of the centromere were still held together by cohesion even after the sister kinetochores had separated. In live cells, the central cores and kinetochores of sister chromosomes could be distinguished from one another when they were subjected to mitotic tension. The function of the different centromeric domains was addressed. Transacting mutations affecting the kinetochore (nuf2) central core domain (mis6) and the heterochromatin domain (rik1) were analyzed in live cells. In interphase, both nuf2 and mis6 caused declustering of centromeres from the spindle pole body whereas centromere clustering was normal in rik1 despite an apparent decondensation defect. The declustering of centromeres in mis6 cells correlated with loss the Ndc80 kinetochore marker protein from the centromeres. Interestingly the declustered centromeres were still restricted to the nuclear periphery thus revealing a kinetochore-independent peripheral localization mechanism for heterochromatin. Time-lapse microscopy of live mis6 and nuf2-1 mutant cells in mitosis showed similar severe misaggregation phenotypes whereas the rik1 mutants showed a mild cohesion defect. Thus, S. pombe centromeres have two distinguishable domains even during mitosis, and our functional analyses support the previous observations that the kinetochore/central core and the heterochromatin domains have distinct functions both in interphase and mitosis.","authors":"Appelgren H, Kniola B, Ekwall K","authors_abbrev":"Appelgren H et al.","pubmed_publication_date":"01 Oct 2003","pubmed_entrez_date":"2003-08-21","publication_year":"2003","canto_session_key":"ce6e2e1a805be580","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-01-24 10:58:30","canto_approved_date":"2023-03-23 14:23:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-22 13:11:24","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.08","SPAC664.01c","SPAC1687.20c","SPAC27F1.04c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2015-01-24"},{"uniquename":"PMID:1347456","title":"Transport of L-glutamic acid in the fission yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1992 Jan 31;1103(2):205-11","abstract":"Transport of L-glutamic acid into the fission yeast Schizosaccharomyces pombe grown to the early stationary phase and preincubated for 60 min with 1% D-glucose is practically unidirectional and is mediated by a single uphill transport system with a KT of 170 microM and Jmax of 4.8 nmol min-1 (mg dry wt.)-1. The system proved to be rather non-specific since all the amino acids transported into the cells acted as potent competitive inhibitors. It has a pH optimum at 3.0-4.0, the accumulation ratio of L-glutamic acid is highest at a suspension density of 0.6-1.0 mg dry wt. per ml and decreases with increasing L-glutamic acid concentrations in the external medium. The system present in the cells after preincubation with D-glucose is unstable and its activity decays after washing the cells with water or after stopping the cytosolic proteinsynthesis with cycloheximide, with a half-time of 24 min in a reaction significantly retarded by phenylmethylsulfonyl fluoride, a serine proteinase inhibitor. The synthesis of the transport protein appears to be repressible by ammonium ions.","authors":"Rezková K, Horák J, Sychrová H, Kotyk A","authors_abbrev":"Rezková K et al.","pubmed_publication_date":"31 Jan 1992","pubmed_entrez_date":"1992-01-31","publication_year":"1992","canto_session_key":"b4fa054643bab22f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-02-04 14:01:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-30 16:27:39","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-01-30"},{"uniquename":"PMID:29632066","title":"TOR complex 2 in fission yeast is required for chromatin-mediated gene silencing and assembly of heterochromatic domains at subtelomeres.","citation":"J Biol Chem 2018 May 25;293(21):8138-8150","abstract":"The conserved serine/threonine protein kinase target of rapamycin (TOR) is a major regulator of eukaryotic cellular and organismal growth and a valuable target for drug therapy. TOR forms the core of two evolutionary conserved complexes, TOR complex 1 (TORC1) and TORC2. In the fission yeast  Schizosaccharomyces pombe , TORC2 responds to glucose levels and, by activating the protein kinase Gad8 (an orthologue of human AKT), is required for well-regulated cell cycle progression, starvation responses, and cell survival. Here, we report that TORC2-Gad8 is also required for gene silencing and the formation of heterochromatin at the  S. pombe  mating-type locus and at subtelomeric regions. Deletion of TORC2-Gad8 resulted in loss of the heterochromatic modification of histone 3 lysine 9 dimethylation (H3K9me2) and an increase in euchromatic modifications, including histone 3 lysine 4 trimethylation (H3K4me3) and histone 4 lysine 16 acetylation (H4K16Ac). Accumulation of RNA polymerase II (Pol II) at subtelomeric genes in TORC2-Gad8 mutant cells indicated a defect in silencing at the transcriptional level. Moreover, a concurrent decrease in histone 4 lysine 20 dimethylation (H4K20me2) suggested elevated histone turnover. Loss of gene silencing in cells lacking TORC2-Gad8 is partially suppressed by loss of the anti-silencer Epe1 and fully suppressed by loss of the Pol II-associated Paf1 complex, two chromatin regulators that have been implicated in heterochromatin stability and spreading. Taken together, our findings suggest that TORC2-Gad8 signaling contributes to epigenetic stability at subtelomeric regions and the mating-type locus in  S. pombe .","doi":"10.1074/jbc.RA118.002270","authors":"Cohen A, Habib A, Laor D, Yadav S, Kupiec M, Weisman R","authors_abbrev":"Cohen A et al.","pubmed_publication_date":"25 May 2018","pubmed_entrez_date":"2018-04-11","publication_year":"2018","canto_session_key":"b9fe9740c46775d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronit Weisman","canto_first_approved_date":"2018-11-21 19:44:15","canto_approved_date":"2018-11-21 19:44:16","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-11-06 09:00:23","canto_added_date":"2018-04-12 00:15:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":79,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ronit Weisman","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.02c","SPCC622.16c","SPAC212.11","SPBPB2B2.18","SPCC306.04c","SPCC24B10.07","SPMTR.01","SPAC750.01","SPAC977.02","SPAC186.06","SPAPYUG7.02c","SPAC664.03","SPCC1322.13","SPAC1F3.01","SPAC186.05c","SPBC428.08c","SPBC1348.03","SPAC186.04c","SPBC30D10.10c","SPAC4C5.02c","SPAC664.01c","SPBCPT2R1.08c"],"gene_count":22,"ltp_gene_count":10,"approved_date":"2018-11-21"},{"uniquename":"PMID:20298435","title":"Contribution of dynein light intermediate and intermediate chains to subcellular localization of the dynein-dynactin motor complex in Schizosaccharomyces pombe.","citation":"Genes Cells 2010 Apr 01;15(4):359-72","abstract":"In fission yeast Schizosaccharomyces pombe, cytoplasmic dynein drives oscillatory nuclear movement during meiotic prophase, which may facilitate pairing of homologous chromosomes. Here, we report the identification of a dynein light intermediate chain (LIC) in fission yeast, termed Dli1p, and show that Dli1p and dynein intermediate chain (IC) Dic1p are essential for the appropriate subcellular localization and proper function of dynein during meiotic prophase. Expression of both the dli1 and dic1 genes was observed only in cells undergoing meiosis. Dli1p interacted and colocalized with dynein heavy chain Dhc1p. The subcellular localization of Dli1p was dependent on Dhc1p, and vice versa. The Dhc1p-Dli1p subcomplex could localize to the spindle pole body (SPB) with no aid of Dic1p and dynactin subunit Ssm4p, but its localization to microtubules was dependent on these two proteins. Dic1p localized to microtubules depending on Ssm4p, but not on Dhc1p and Dli1p. Its localization to the SPB, however, was dependent on Dhc1p and Dli1p. Localization of Ssm4p to the SPB was largely dependent on Dhc1p, Dli1p and Dic1p. Thus, Dli1p and Dic1p contribute differently in localizing the dynein-dynactin motor complex to organelles, providing novel insight into the in vivo function of dynein subunits in fission yeast.","doi":"10.1111/j.1365-2443.2010.01386.x","authors":"Fujita I, Yamashita A, Yamamoto M","authors_abbrev":"Fujita I et al.","pubmed_publication_date":"01 Apr 2010","pubmed_entrez_date":"2010-03-20","publication_year":"2010","canto_session_key":"c7fac5251ee4f493","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-16 16:55:11","canto_approved_date":"2022-07-27 12:13:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-01 11:52:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":32,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPAC458.04c","SPBC646.17c","SPAC27D7.13c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-06-16"},{"uniquename":"PMID:2674650","title":"Molecular cloning and sequence analysis of mutant alleles of the fission yeast cdc2 protein kinase gene: implications for cdc2+ protein structure and function.","citation":"Mol Gen Genet 1989 Jul;218(1):41-9","abstract":"The cdc2+ gene function plays a central role in the control of the mitotic cell cycle of the fission yeast Schizosaccharomyces pombe. Recessive temperature-sensitive mutations in the cdc2 gene cause cell cycle arrest when shifted to the restrictive temperature, while a second class of mutations within the cdc2 gene causes a premature advancement into mitosis. Previously the cdc2+ gene has been cloned and has been shown to encode a 34 kDa phosphoprotein with in vitro protein kinase activity. Here we describe the cloning of 11 mutant alleles of the cdc2 gene using two simple methods, one of which is presented here for the first time. We have sequenced these alleles and find a variety of single amino acid substitutions mapping throughout the cdc2 protein. Analysis of these mutations has identified a number of regions within the cdc2 protein that are important for cdc2+ activity and regulation. These include regions which may be involved in the interaction of the cdc2+ gene product with the proteins encoded by the wee1+, cdc13+ and suc1+ genes.","authors":"Carr AM, MacNeill SA, Hayles J, Nurse P","authors_abbrev":"Carr AM et al.","pubmed_publication_date":"Jul 1989","pubmed_entrez_date":"1989-07-01","publication_year":"1989","canto_session_key":"57f3a3b217f0cd70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ryoko Mandeville","canto_first_approved_date":"2014-12-15 18:30:56","canto_approved_date":"2023-12-10 13:39:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-09 15:23:14","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ryoko Mandeville","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-12-15"},{"uniquename":"PMID:32518066","title":"Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes.","citation":"RNA 2020 Oct;26(10):1400-1413","abstract":"Eukaryotes possess eight highly conserved Lsm (like Sm) proteins that assemble into circular, heteroheptameric complexes, bind RNA, and direct a diverse range of biological processes. Among the many essential functions of Lsm proteins, the cytoplasmic Lsm1-7 complex initiates mRNA decay, while the nuclear Lsm2-8 complex acts as a chaperone for U6 spliceosomal RNA. It has been unclear how these complexes perform their distinct functions while differing by only one out of seven subunits. Here, we elucidate the molecular basis for Lsm-RNA recognition and present four high-resolution structures of Lsm complexes bound to RNAs. The structures of Lsm2-8 bound to RNA identify the unique 2',3' cyclic phosphate end of U6 as a prime determinant of specificity. In contrast, the Lsm1-7 complex strongly discriminates against cyclic phosphates and tightly binds to oligouridylate tracts with terminal purines. Lsm5 uniquely recognizes purine bases, explaining its divergent sequence relative to other Lsm subunits. Lsm1-7 loads onto RNA from the 3' end and removal of the Lsm1 carboxy-terminal region allows Lsm1-7 to scan along RNA, suggesting a gated mechanism for accessing internal binding sites. These data reveal the molecular basis for RNA binding by Lsm proteins, a fundamental step in the formation of molecular assemblies that are central to eukaryotic mRNA metabolism.","doi":"10.1261/rna.075879.120","authors":"Montemayor EJ, Virta JM, Hayes SM, Nomura Y, Brow DA, Butcher SE","authors_abbrev":"Montemayor EJ et al.","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-06-11","publication_year":"2020","canto_session_key":"5fb962029c56cdd6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-20 16:49:06","canto_approved_date":"2024-07-09 17:39:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-20 16:48:57","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1620.01c","SPCC285.12","SPBC3D6.08c","SPBC9B6.05c","SPCC1840.10","SPBC1861.04c","SPBC30D10.06","SPSNRNA.06","SPAC2F3.17c","SPBC20F10.09"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2023-02-20","pdb_entries":[{"pdb_id":"6ppq","gene_chains":[{"gene_uniquename":"SPBC30D10.06","chain":"D","position":"1-121"},{"gene_uniquename":"SPBC20F10.09","chain":"E","position":"1-80"},{"gene_uniquename":"SPCC285.12","chain":"G","position":"1-113"},{"gene_uniquename":"SPCC1620.01c","chain":"B","position":"1-96"},{"gene_uniquename":"SPBC3D6.08c","chain":"A","position":"1-84"},{"gene_uniquename":"SPAC2F3.17c","chain":"F","position":"1-75"},{"gene_uniquename":"SPBC9B6.05c","chain":"C","position":"1-93"}],"title":"Structure of S. pombe Lsm1-7 with RNA, polyuridine with 3' adenosine","entry_authors":"Montemayor EJ,Butcher SE","entry_authors_abbrev":"Montemayor EJ et al.","reference_uniquename":"PMID:32518066","experimental_method":"X-ray","resolution":"1.81"},{"pdb_id":"6ppn","gene_chains":[{"gene_uniquename":"SPBC30D10.06","chain":"D/L","position":"1-121"},{"gene_uniquename":"SPBC20F10.09","chain":"E/M","position":"1-80"},{"gene_uniquename":"SPCC1840.10","chain":"H/P","position":"1-94"},{"gene_uniquename":"SPCC285.12","chain":"G/O","position":"1-113"},{"gene_uniquename":"SPCC1620.01c","chain":"B/J","position":"1-96"},{"gene_uniquename":"SPAC2F3.17c","chain":"F/N","position":"1-75"},{"gene_uniquename":"SPBC9B6.05c","chain":"C/K","position":"1-93"}],"title":"Structure of S. pombe Lsm2-8 with unprocessed U6 snRNA","entry_authors":"Montemayor EJ,Butcher SE","entry_authors_abbrev":"Montemayor EJ et al.","reference_uniquename":"PMID:32518066","experimental_method":"X-ray","resolution":"1.91"},{"pdb_id":"6ppp","gene_chains":[{"gene_uniquename":"SPBC30D10.06","chain":"D/L","position":"1-121"},{"gene_uniquename":"SPBC20F10.09","chain":"E/M","position":"1-80"},{"gene_uniquename":"SPCC1840.10","chain":"H/P","position":"1-94"},{"gene_uniquename":"SPCC285.12","chain":"G/O","position":"1-113"},{"gene_uniquename":"SPCC1620.01c","chain":"B/J","position":"1-96"},{"gene_uniquename":"SPAC2F3.17c","chain":"F/N","position":"1-75"},{"gene_uniquename":"SPBC9B6.05c","chain":"C/K","position":"1-93"}],"title":"Structure of S. pombe Lsm2-8 with processed U6 snRNA","entry_authors":"Montemayor EJ,Butcher SE","entry_authors_abbrev":"Montemayor EJ et al.","reference_uniquename":"PMID:32518066","experimental_method":"X-ray","resolution":"2.33"},{"pdb_id":"6ppv","gene_chains":[{"gene_uniquename":"SPBC30D10.06","chain":"D","position":"1-121"},{"gene_uniquename":"SPBC20F10.09","chain":"E","position":"1-80"},{"gene_uniquename":"SPCC285.12","chain":"G","position":"1-113"},{"gene_uniquename":"SPCC1620.01c","chain":"B","position":"1-96"},{"gene_uniquename":"SPBC3D6.08c","chain":"A","position":"1-84"},{"gene_uniquename":"SPAC2F3.17c","chain":"F","position":"1-75"},{"gene_uniquename":"SPBC9B6.05c","chain":"C","position":"1-93"}],"title":"Structure of S. pombe Lsm1-7 with RNA, polyuridine with 3' guanosine","entry_authors":"Montemayor EJ,Butcher SE","entry_authors_abbrev":"Montemayor EJ et al.","reference_uniquename":"PMID:32518066","experimental_method":"X-ray","resolution":"2.05"}]},{"uniquename":"PMID:12597277","title":"Abundant poly(A)-bearing RNAs that lack open reading frames in Schizosaccharomyces pombe.","citation":"DNA Res 2002 Dec 31;9(6):209-15","abstract":"We report here that 6.9% (68/987) of randomly selected cDNA clones from an S. pombe cDNA library lack apparently long open reading frames which we denote prl. One of them, prl1, was examined further because multiple bands were observed when it was used as a probe in northern blot analysis. These multiple bands appear to be derived from overlapping transcripts from both DNA strands, including non-coding RNAs and antisense RNAs in addition to mRNA. Such mechanisms may increase the transcriptional variation in S. pombe cells.","authors":"Watanabe T, Miyashita K, Saito TT, Nabeshima K, Nojima H","authors_abbrev":"Watanabe T et al.","pubmed_publication_date":"31 Dec 2002","pubmed_entrez_date":"2003-02-25","publication_year":"2002","canto_session_key":"3e8e2356f65b2b6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-09 15:48:01","canto_approved_date":"2019-01-09 15:48:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-09 15:47:53","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.42","SPNCRNA.51","SPNCRNA.14","SPNCRNA.34","SPNCRNA.24","SPAC19A8.16","SPNCRNA.68","SPNCRNA.66","SPNCRNA.11","SPNCRNA.37","SPNCRNA.35","SPAC144.19","SPNCRNA.1493","SPNCRNA.1649","SPNCRNA.40","SPNCRNA.03","SPNCRNA.50","SPNCRNA.07","SPNCRNA.56","SPNCRNA.02","SPNCRNA.23","SPNCRNA.817","SPNCRNA.928","SPNCRNA.1519","SPNCRNA.26","SPNCRNA.21","SPNCRNA.36","SPNCRNA.13","SPNCRNA.12","SPNCRNA.62","SPNCRNA.33","SPNCRNA.19","SPNCRNA.53","SPBC21B10.14","SPNCRNA.39","SPNCRNA.22","SPNCRNA.58","SPNCRNA.61","SPNCRNA.16","SPNCRNA.1234","SPNCRNA.05","SPNCRNA.47","SPNCRNA.04","SPNCRNA.54","SPNCRNA.17","SPNCRNA.25","SPNCRNA.587","SPNCRNA.28","SPNCRNA.43","SPNCRNA.67","SPNCRNA.29","SPNCRNA.52","SPNCRNA.15","SPNCRNA.27","SPNCRNA.45","SPNCRNA.57","SPNCRNA.32","SPAC6B12.18"],"gene_count":58,"ltp_gene_count":0,"approved_date":"2019-01-09"},{"uniquename":"PMID:8087848","title":"Temporal order of S phase and mitosis in fission yeast is determined by the state of the p34cdc2-mitotic B cyclin complex.","citation":"Cell 1994 Sep 09;78(5):813-22","abstract":"We show here that the state of the p34cdc2-p56cdc13 mitotic B cyclin complex determines whether a fission yeast cell undergoes S phase or mitosis. Mutants defective for p56cdc13 reset to G1 and rereplicate their DNA, while cells completely lacking the p34cdc2-p56cdc13 complex undergo multiple rounds of S phase. In contrast, formation of the p34cdc2-p56cdc13 complex in G1 promotes cells inappropriately into mitosis. We propose that the temporal order of S phase and mitosis is maintained by the presence or absence of the p34cdc2-p56cdc13 complex.","authors":"Hayles J, Fisher D, Woollard A, Nurse P","authors_abbrev":"Hayles J et al.","pubmed_publication_date":"09 Sep 1994","pubmed_entrez_date":"1994-09-09","publication_year":"1994","canto_session_key":"86f72e4a0d568a17","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2016-11-24 15:38:34","canto_approved_date":"2024-11-11 12:37:15","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-09-29 13:45:45","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":12,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC11B10.09","SPBC582.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-11-24"},{"uniquename":"PMID:17940212","title":"Convergent domestication of pogo-like transposases into centromere-binding proteins in fission yeast and mammals.","citation":"Mol Biol Evol 2008 Jan;25(1):29-41","abstract":"The mammalian centromere-associated protein B (CENP-B) shares significant sequence similarity with 3 proteins in fission yeast (Abp1, Cbh1, and Cbh2) that also bind centromeres and have essential function for chromosome segregation and centromeric heterochromatin formation. Each of these proteins displays extensive sequence similarity with pogo-like transposases, which have been previously identified in the genomes of various insects and vertebrates, in the protozoan Entamoeba and in plants. Based on this distribution, it has been proposed that the mammalian and fission yeast centromeric proteins are derived from \"domesticated\" pogo-like transposons. Here we took advantage of the vast amount of sequence information that has become recently available for a wide range of fungal and animal species to investigate the origin of the mammalian CENP-B and yeast CENP-B-like genes. A highly conserved ortholog of CENP-B was detected in 31 species of mammals, including opossum and platypus, but was absent from all nonmammalian species represented in the databases. Similarly, no ortholog of the fission yeast centromeric proteins was identified in any of the various fungal genomes currently available. In contrast, we discovered a plethora of novel pogo-like transposons in diverse invertebrates and vertebrates and in several filamentous fungi. Phylogenetic analysis revealed that the mammalian and fission yeast CENP-B proteins fall into 2 distinct monophyletic clades, each of which includes a different set of pogo-like transposons. These results are most parsimoniously explained by independent domestication events of pogo-like transposases into centromeric proteins in the mammalian and fission yeast lineages, a case of \"convergent domestication.\" These findings highlight the propensity of transposases to give rise to new host proteins and the potential of transposons as sources of genetic innovation.","authors":"Casola C, Hucks D, Feschotte C","authors_abbrev":"Casola C et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-10-18","publication_year":"2008","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22160912","title":"A thiamine-regulatable epitope-tagged protein expression system in fission yeast.","citation":"Methods Mol Biol 2012;824:417-32","abstract":"Schizosaccharomyces pombe, the fission yeast, has been a popular and useful model system for investigating the mechanisms of biological processes for a long time. To facilitate purification, localization, and functional analysis of gene products, a wide range of expression vectors have been developed. Several of these vectors utilize the inducible/repressible promoter systems and enable the episomal expression of proteins as fusion proteins with epitope tags attached to their N terminus or C terminus.This chapter provides a detailed protocol for expression of the epitope-tagged proteins from thiamine-regulatable nmt promoter in fission yeast. The yeast culture conditions and procedures for yeast transformation, expression induction, preparation of whole-cell extracts, and analysis of epitope-tagged protein expression by Western blotting are described.","doi":"10.1007/978-1-61779-433-9_22","authors":"Tamm T","authors_abbrev":"Tamm T","pubmed_publication_date":"2012","pubmed_entrez_date":"2011-12-14","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11341272","title":"Cell biology. New clue to how the cell controls its proteins.","citation":"Science 2001 May 04;292(5518):838-9","abstract":"","authors":"Marx J","authors_abbrev":"Marx J","pubmed_publication_date":"04 May 2001","pubmed_entrez_date":"2001-05-09","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6411073","title":"Glycolysis and respiration in yeasts. The Pasteur effect studied by mass spectrometry.","citation":"Biochem J 1983 Jun 15;212(3):749-54","abstract":"Simultaneous and continuous measurements of changes in CO2 and O2 concentrations in glucose-metabolizing yeast suspensions by mass spectrometry enabled a study of the Pasteur effect (aerobic inhibition of glycolysis) in Saccharomyces uvarum and Schizosaccharomyces pombe. A different control mechanism operates in Candida utilis to give a damped oscillation after the anaerobic-aerobic transition. The apparent Km values for respiration of the three yeasts were in the range 1.3-1.8 microM-O2. The apparent Km values for O2 of the Pasteur effect were 5 and 13 microM for catabolite-repressed and derepressed S. uvarum respectively and 7 microM for Sch. pombe. These results are discussed with respect to currently accepted mechanisms for the control of glycolysis.","authors":"Lloyd D, Kristensen B, Degn H","authors_abbrev":"Lloyd D et al.","pubmed_publication_date":"15 Jun 1983","pubmed_entrez_date":"1983-06-15","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12374757","title":"Site-specific ORC binding, pre-replication complex assembly and DNA synthesis at Schizosaccharomyces pombe replication origins.","citation":"EMBO J 2002 Oct 15;21(20):5567-76","abstract":"Previous studies have shown that the Schizo saccharomyces pombe Orc4 subunit is solely responsible for in vitro binding of origin recognition complex (ORC) to specific AT-rich sites within S.pombe replication origins. Using ARS3001, a S.pombe replication origin consisting of four genetically required sites, we show that, in situ as well as in vitro, Orc4 binds strongly to the Delta3 site, weakly to the Delta6 site and not at all to the remaining sequences. In situ, the footprint over Delta3 is extended during G(1) phase, but only when Cdc18 is present and Mcm proteins are bound to chromatin. Moreover, this footprint extends into the adjacent Delta2 site, where leading strand DNA synthesis begins. Therefore, we conclude that ARS3001 consists of a single primary ORC binding site that assembles a pre-replication complex and initiates DNA synthesis, plus an additional novel origin element (Delta9) that neither binds ORC nor functions as a centromere, but does bind an as yet unidentified protein throughout the cell cycle. Schizosaccharomyces pombe may be an appropriate paradigm for the complex origins found in the metazoa.","authors":"Kong D, DePamphilis ML","authors_abbrev":"Kong D et al.","pubmed_publication_date":"15 Oct 2002","pubmed_entrez_date":"2002-10-11","publication_year":"2002","canto_session_key":"e1abf4687b53b73e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-08-21 15:52:09","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-21 15:51:51","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-21"},{"uniquename":"PMID:20719271","title":"Optical trapping and laser ablation of microtubules in fission yeast.","citation":"Methods Cell Biol 2010;97:173-83","abstract":"Manipulation has been used as a powerful investigation technique since the early history of biology. Every technical advance resulted in more refined instruments that led to the discovery of new phenomena and to the solution of old problems. The invention of laser in 1960 gave birth to what is now called optical manipulation: the use of light to interact with matter. Since then, the tremendous progress of laser technology made optical manipulation not only an affordable, reliable alternative to traditional manipulation techniques but disclosed also new, intriguing applications that were previously impossible, such as contact-free manipulation. Currently, optical manipulation is used in many fields, yet has the potential of becoming an everyday technique in a broader variety of contexts. Here, we focus on two main optical manipulation techniques: optical trapping and laser ablation. We illustrate with selected applications in fission yeast how in vivo optical manipulation can be used to study organelle positioning and the force balance in the microtubule cytoskeleton.","doi":"10.1016/S0091-679X(10)97010-6","authors":"Maghelli N, Tolić-Nørrelykke IM","authors_abbrev":"Maghelli N et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-08-20","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36779416","title":"The ecl family gene ecl3+ is induced by phosphate starvation and contributes to sexual differentiation in fission yeast.","citation":"J Cell Sci 2023 Mar 15;136(6)","abstract":"In Schizosaccharomyces pombe, ecl family genes are induced by several signals, such as starvation of various nutrients, including sulfur, amino acids and Mg2+, and environmental stress, including heat or oxidative stress. These genes mediate appropriate cellular responses and contribute to the maintenance of cell viability and induction of sexual differentiation. Although this yeast has three ecl family genes with overlapping functions, any environmental conditions that induce ecl3+ remain unidentified. We demonstrate that ecl3+ is induced by phosphate starvation, similar to its chromosomally neighboring genes, pho1+ and pho84+, which respectively encode an extracellular acid phosphatase and an inorganic phosphate transporter. ecl3+ expression was induced by the transcription factor Pho7 and affected by the cyclin-dependent kinase (CDK)-activating kinase Csk1. Phosphate starvation induced G1 arrest and sexual differentiation via ecl family genes. Biochemical analyses suggested that this G1 arrest was mediated by the stabilization of the CDK inhibitor Rum1, which was dependent on ecl family genes. This study shows that ecl family genes are required for appropriate responses to phosphate starvation and provides novel insights into the diversity and similarity of starvation responses.","doi":"10.1242/jcs.260759","authors":"Ohtsuka H, Sakata H, Kitazaki Y, Tada M, Shimasaki T, Otsubo Y, Maekawa Y, Kobayashi M, Imada K, Yamashita A, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"15 Mar 2023","pubmed_entrez_date":"2023-02-13","publication_year":"2023","canto_session_key":"aeaa06c0eac76f9e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2023-03-09 19:05:01","canto_approved_date":"2025-09-04 09:06:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-02 03:05:55","canto_added_date":"2023-02-14 01:15:04","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":12,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27B12.11c","SPBC1718.07c","SPBC8E4.01c","SPBP35G2.16c","SPAC1851.03","SPBC32F12.09","SPBP4G3.02","SPBC8E4.12c","SPCC70.12c"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2023-03-09"},{"uniquename":"PMID:12449626","title":"[Involvement of microbial alkyl hydroxybenzenes in the regulation of autolytic degradation of yeast cells].","citation":"Mikrobiologiia 2002;71(5):611-8","abstract":"A comparative study was performed of the processes of autolytic degradation of the cells of Saccharomyces cerevisiae and Schizosaccharomyces pombe under conditions simulating the phase of cell death in microbial cultures: (1) during autolysis induced by oleic acid, which is the chemical analogue of factors d2 (autolysis autoinducer), (2) under the effect of extracellular microbial proteinases (enzymatic lysis), and (3) under concomitant effect of the enzymes of the endogenous autolytic complex and exogenous proteinases (heterolysis). Regulatory mechanisms controlling the rate and profundity of autolysis were elucidated, relying on the stabilization of hydrolytic enzymes and enhancement of their activity in their complexes with a chemical analogue of microbial autoregulatory factors d1, which belong to alkylhydroxybenzenes and fulfil functions of chemical chaperons. The changes in the activity of proteinases and enzymes of the autolytic complex were shown to be dependent on the concentration of the analogue at the moment of complex formation.","authors":"Karpekina TA, Stepanenko IIu, Krylova EI, Kozlova AN, Gracheva IM, El'-Registan GI","authors_abbrev":"Karpekina TA et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-11-27","publication_year":"2002","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD270","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18084898","title":"Functions of typical 2-Cys peroxiredoxins in yeast.","citation":"Subcell Biochem 2007;44:253-65","abstract":"Peroxiredoxins are ubiquitous proteins that are found from bacteria to humans. Until recently they were thought to solely act as antioxidants catalysing the reduction of peroxides through their associated thioredoxin peroxidase activity. However, recent work has begun to uncover hitherto unsuspected roles for one group of these proteins, the typical 2-Cys peroxiredoxins (2-Cys Prx). For example, typical 2-Cys Prxs have been found to have roles in the model organisms Schizosaccharomvces pombe and Saccharomyces cerevisiae in regulating signal transduction, in DNA damage responses and as molecular chaperones. There is increasing evidence that H2O2 is utilised as a signalling molecule to regulate a range of important cellular processes. As abundant and ubiquitous peroxidase enzymes the peroxidase activity of typical 2-Cys Prxs is important in the regulation of these functions. Significantly, studies in yeast suggest that the regulation of the thioredoxin peroxidase and chaperone activities of these multifunction enzymes is an important aspect of H2O2-mediated signal transduction and consequently have provided important insight into the roles of these proteins in higher eukaryotes.","authors":"Morgan BA, Veal EA","authors_abbrev":"Morgan BA et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-12-19","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AY293737","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8392683","title":"[Control of cell division in eucaryotes].","citation":"Pathol Biol (Paris) 1993 Mar;41(3):260-7","abstract":"In eucaryotes, M-phase promoting factor (MPF) triggers meiosis in germ cells and mitosis in somatic cells. MPF is composed of two proteins of which one is homologous with the protein kinase encoded by gene cdc2 of Schizosaccharomyces pombe (p34cdc2) and the other is a cyclin whose concentration oscillates during the cell cycle. Inactivation of p34cdc2 (MPF) requires cyclin degradation, which occurs during the metaphase-anaphase transition of the M-phase. Cyclin degradation is not only associated with cell cycle progression, but is also required for this event. At the G2/M transition, p34cdc2 protein kinase is activated and catalyzes phosphorylation of numerous key proteins, thus enabling cell changes to occur. p34cdc2 undergoes multiple-site phosphorylation in a cell cycle-dependent manner. At onset of mitosis, the protein phosphatase cdc25 catalyzes dephosphorylation of the p34cdc2 kinase at the threonine 14 and tyrosine 15 sites. This event may be the rate-limiting step controlling onset of mitosis in cells of vertebrates. A second protein kinase, encoded by the proto-oncogene c-mos, acts as a cytostatic factor preventing cyclin degradation and keeping unfertilized eggs from progressing beyond the second meiotic metaphase.","authors":"Lorca T","authors_abbrev":"Lorca T","pubmed_publication_date":"Mar 1993","pubmed_entrez_date":"1993-03-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF188642","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11294886","title":"A millennial myosin census.","citation":"Mol Biol Cell 2001 Apr;12(4):780-94","abstract":"The past decade has seen a remarkable explosion in our knowledge of the size and diversity of the myosin superfamily. Since these actin-based motors are candidates to provide the molecular basis for many cellular movements, it is essential that motility researchers be aware of the complete set of myosins in a given organism. The availability of cDNA and/or draft genomic sequences from humans, Drosophila melanogaster, Caenorhabditis elegans, Arabidopsis thaliana, Saccharomyces cerevisiae, Schizosaccharomyces pombe, and Dictyostelium discoideum has allowed us to tentatively define and compare the sets of myosin genes in these organisms. This analysis has also led to the identification of several putative myosin genes that may be of general interest. In humans, for example, we find a total of 40 known or predicted myosin genes including two new myosins-I, three new class II (conventional) myosins, a second member of the class III/ninaC myosins, a gene similar to the class XV deafness myosin, and a novel myosin sharing at most 33% identity with other members of the superfamily. These myosins are in addition to the recently discovered class XVI myosin with N-terminal ankyrin repeats and two human genes with similarity to the class XVIII PDZ-myosin from mouse. We briefly describe these newly recognized myosins and extend our previous phylogenetic analysis of the myosin superfamily to include a comparison of the complete or nearly complete inventories of myosin genes from several experimentally important organisms.","authors":"Berg JS, Powell BC, Cheney RE","authors_abbrev":"Berg JS et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-04-11","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31397327","title":"Crystal structure of the Schizosaccharomyces pombe U7BR E2-binding region in complex with Ubc7.","citation":"Acta Crystallogr F Struct Biol Commun 2019 Aug 01;75(Pt 8):552-560","abstract":"Endoplasmic reticulum (ER)-associated degradation (ERAD) is a protein quality-control pathway in eukaryotes in which misfolded ER proteins are polyubiquitylated, extracted and ultimately degraded by the proteasome. This process involves ER membrane-embedded ubiquitin E2 and E3 enzymes, as well as a soluble E2 enzyme (Ubc7 in Saccharomyces cerevisiae and UBE2G2 in mammals). E2-binding regions (E2BRs) that recruit these soluble ERAD E2s to the ER have been identified in humans and S. cerevisiae, and structures of E2-E2BR complexes from both species have been determined. In addition to sequence and structural differences between the human and S. cerevisiae E2BRs, the binding of E2BRs also elicits different biochemical outcomes with respect to E2 charging by E1 and E2 discharge. Here, the Schizosaccharomyces pombe E2BR was identified and purified with Ubc7 to resolve a 1.7 Å resolution co-crystal structure of the E2BR in complex with Ubc7. The S. pombe E2BR binds to the back side of the E2 as an α-helix and, while differences exist, it exhibits greater similarity to the human E2BR. Structure-based sequence alignments reveal differences and conserved elements among these species. Structural comparisons and biochemistry reveal that the S. pombe E2BR presents a steric impediment to E1 binding and inhibits E1-mediated charging, respectively.","doi":"10.1107/S2053230X19009786","authors":"Hann ZS, Metzger MB, Weissman AM, Lima CD","authors_abbrev":"Hann ZS et al.","pubmed_publication_date":"01 Aug 2019","pubmed_entrez_date":"2019-08-10","publication_year":"2019","canto_session_key":"1dfe9f28281e05b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-08-13 09:32:45","canto_approved_date":"2019-08-13 09:32:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-13 09:32:38","canto_added_date":"2019-08-11 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP16F5.04","SPBC1604.21c","SPCC4G3.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-08-13","pdb_entries":[{"pdb_id":"6op8","gene_chains":[{"gene_uniquename":"SPBP16F5.04","chain":"A","position":"1-166"},{"gene_uniquename":"SPCC4G3.13c","chain":"B","position":"152-215"}],"title":"S. pombe Ubc7/U7BR complex","entry_authors":"Hann ZS,Lima CD","entry_authors_abbrev":"Hann ZS et al.","reference_uniquename":"PMID:31397327","experimental_method":"X-ray","resolution":"1.703"}]},{"uniquename":"PMID:23936074","title":"Telomeric repeats facilitate CENP-A(Cnp1) incorporation via telomere binding proteins.","citation":"PLoS One 2013;8(7):e69673","abstract":"The histone H3 variant, CENP-A, is normally assembled upon canonical centromeric sequences, but there is no apparent obligate coupling of sequence and assembly, suggesting that centromere location can be epigenetically determined. To explore the tolerances and constraints on CENP-A deposition we investigated whether certain locations are favoured when additional CENP-A(Cnp1) is present in fission yeast cells. Our analyses show that additional CENP-A(Cnp1) accumulates within and close to heterochromatic centromeric outer repeats, and over regions adjacent to rDNA and telomeres. The use of minichromosome derivatives with unique DNA sequences internal to chromosome ends shows that telomeres are sufficient to direct CENP-A(Cnp1) deposition. However, chromosome ends are not required as CENP-A(Cnp1) deposition also occurs at telomere repeats inserted at an internal locus and correlates with the presence of H3K9 methylation near these repeats. The Ccq1 protein, which is known to bind telomere repeats and recruit telomerase, was found to be required to induce H3K9 methylation and thus promote the incorporation of CENP-A(Cnp1) near telomere repeats. These analyses demonstrate that at non-centromeric chromosomal locations the presence of heterochromatin influences the sites at which CENP-A is incorporated into chromatin and, thus, potentially the location of centromeres.","doi":"10.1371/journal.pone.0069673","authors":"Castillo AG, Pidoux AL, Catania S, Durand-Dubief M, Choi ES, Hamilton G, Ekwall K, Allshire RC","authors_abbrev":"Castillo AG et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-08-13","publication_year":"2013","canto_session_key":"c6ced0325cbf00af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-26 10:42:29","canto_approved_date":"2024-04-08 16:56:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-29 08:51:38","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.07","SPBC428.08c","SPAC6F6.17","SPBC1105.17","SPBC1861.01c","SPAC16A10.07c"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2016-10-26"},{"uniquename":"PMID:33130996","title":"Expression of the Neural REST/NRSF-SIN3 Transcriptional Corepressor Complex as a Target for Small-Molecule Inhibitors.","citation":"Mol Biotechnol 2021 Jan;63(1):53-62","abstract":"The repressor element 1 (RE1) silencing transcription factor/neuron-restrictive silencing factor (REST/NRSF) modulates the expression of genes with RE1/neuron-restrictive silencing element (RE1/NRSE) sites by recruiting the switch independent 3 (SIN3) factor and the REST corepressor (COREST) to its N and C-terminal repressor domain, respectively. Both, SIN3 and COREST assemble into protein complexes that are composed of multiple subunits including a druggable histone deacetylase (HDAC) enzyme. The SIN3 core complex comprises the eponymous proteins SIN3A or SIN3B, the catalytically active proteins HDAC1 or HDAC2, the histone chaperone retinoblastoma-associated protein 46/retinoblastoma-binding protein 7 (RBAP46/RBBP7) or RBAP48/RBBP4, the SIN3-associated protein 30 (SAP30), and the suppressor of defective silencing 3 (SDS3). Here, we overcome a bottleneck limiting the molecular characterization of the REST/NRSF-SIN3 transcriptional corepressor complex. To this end, SIN3 genes were amplified from the complementary DNA of neural stem/progenitor cells, and expressed in a baculovirus/insect cell expression system. We show that the isolates bind to DNA harboring RE1/NRSE sites and demonstrate that the histone deacetylase activity is blocked by small-molecule inhibitors. Thus, our isolates open up for future biomedical research on this critical transcriptional repressor complex and are envisioned as tool for drug testing.","doi":"10.1007/s12033-020-00283-7","authors":"Jayaprakash S, Le LTM, Sander B, Golas MM","authors_abbrev":"Jayaprakash S et al.","pubmed_publication_date":"Jan 2021","pubmed_entrez_date":"2020-11-01","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29A4.18"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1934119","title":"Sterile UGA nonsense mutants of fission yeast.","citation":"Curr Genet 1991 Jul;20(1-2):67-73","abstract":"Eight sterile mutants, which regain their fertility upon reactivation of an inactivated UGA suppressor allele of the serine tRNA gene sup3, are shown to carry UGA nonsense alleles of two established ste genes, ste1 (one mutant) and ste6 (two mutants), and of two novel genes, ste9 (four mutants) and ste10 (one leaky mutant of ras1-/ste5-like cell morphology). The mutant alleles of ste1 and ste9 lead to a defect in both conjugation and meiosis, whereas those of ste6 and ste10 affect mating only. Two of the four genes map to chromosome I, ste1 in the left arm 6 cM distal of ura1, and ste9 in the right arm 3 cM distal of ade2. The ste10 and ste6 genes are located in the right arms of chromosomes II and III, respectively, the former 4 cM distal of trp1 and the latter 1 cM proximal or distal of trp3.","authors":"Leupold U, Sipiczki M","authors_abbrev":"Leupold U et al.","pubmed_publication_date":"Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17072888","title":"DNA replication in the fission yeast: robustness in the face of uncertainty.","citation":"Yeast 2006 Oct 15;23(13):951-62","abstract":"DNA replication, the process of duplication of a cell's genetic content, must be carried out with great precision every time the cell divides, so that genetic information is preserved. Control mechanisms must ensure that every base of the genome is replicated within the allocated time (S-phase) and only once per cell cycle, thereby safeguarding genomic integrity. In eukaryotes, replication starts from many points along the chromosome, termed origins of replication, and then proceeds continuously bidirectionally until an opposing moving fork is encountered. In contrast to bacteria, where a specific site on the genome serves as an origin in every cell division, in most eukaryotes origin selection appears highly stochastic: many potential origins exist, of which only a subset is selected to fire in any given cell, giving rise to an apparently random distribution of initiation events across the genome. Origin states change throughout the cell cycle, through the ordered formation and modification of origin-associated multisubunit protein complexes. State transitions are governed by fluctuations of cyclin-dependent kinase (CDK) activity and guards in these transitions ensure system memory. We present here DNA replication dynamics, emphasizing recent data from the fission yeast Schizosaccharomyces pombe, and discuss how robustness may be ensured in spite of (or even assisted by) system randomness.","authors":"Legouras I, Xouri G, Dimopoulos S, Lygeros J, Lygerou Z","authors_abbrev":"Legouras I et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15850809","title":"ATP-binding motifs play key roles in Krp1p, kinesin-related protein 1, function for bi-polar growth control in fission yeast.","citation":"Biochem Biophys Res Commun 2005 Jun 03;331(2):658-68","abstract":"Kinesin is a microtubule-based motor protein with various functions related to the cell growth and division. It has been reported that Krp1p, kinesin-related protein 1, which belongs to the kinesin heavy chain superfamily, localizes on microtubules and may play an important role in cytokinesis. However, the function of Krp1p has not been fully elucidated. In this study, we overexpressed an intact form and three different mutant forms of Krp1p in fission yeast constructed by site-directed mutagenesis in two ATP-binding motifs or by truncation of the leucine zipper-like motif (LZiP). We observed hyper-extended microtubules and the aberrant nuclear shape in Krp1p-overexpressed fission yeast. As a functional consequence, a point mutation of ATP-binding domain 1 (G89E) in Krp1p reversed the effect of Krp1p overexpression in fission yeast, whereas the specific mutation in ATP-binding domain 2 (G238E) resulted in the altered cell polarity. Additionally, truncation of the leucine zipper-like domain (LZiP) at the C-terminal of Krp1p showed a normal nuclear division. Taken together, we suggest that krp1p is involved in regulation of cell-polarized growth through ATP-binding motifs in fission yeast.","authors":"Rhee DK, Cho BA, Kim HB","authors_abbrev":"Rhee DK et al.","pubmed_publication_date":"03 Jun 2005","pubmed_entrez_date":"2005-04-27","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1834.07"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:28572513","title":"Domain alternation and active site remodeling are conserved structural features of ubiquitin E1.","citation":"J Biol Chem 2017 Jul 21;292(29):12089-12099","abstract":"E1 enzymes for ubiquitin (Ub) and Ub-like modifiers (Ubls) harbor two catalytic activities that are required for Ub/Ubl activation: adenylation and thioester bond formation. Structural studies of the E1 for the Ubl  s mall  u biquitin-like  mo difier (SUMO) revealed a single active site that is transformed by a conformational switch that toggles its competency for catalysis of these two distinct chemical reactions. Although the mechanisms of adenylation and thioester bond formation revealed by SUMO E1 structures are thought to be conserved in Ub E1, there is currently a lack of structural data supporting this hypothesis. Here, we present a structure of  Schizosaccharomyces pombe  Uba1 in which the second catalytic cysteine half-domain (SCCH domain) harboring the catalytic cysteine has undergone a 106° rotation that results in a completely different network of intramolecular interactions between the SCCH and adenylation domains and translocation of the catalytic cysteine 12 Å closer to the Ub C terminus compared with previous Uba1 structures. SCCH domain alternation is accompanied by conformational changes within the Uba1 adenylation domains that effectively disassemble the adenylation active site. Importantly, the structural and biochemical data suggest that domain alternation and remodeling of the adenylation active site are interconnected and are intrinsic structural features of Uba1 and that the overall structural basis for adenylation and thioester bond formation exhibited by SUMO E1 is indeed conserved in Ub E1. Finally, the mechanistic insights provided by the novel conformational snapshot of Uba1 presented in this study may guide efforts to develop small molecule inhibitors of this critically important enzyme that is an active target for anticancer therapeutics.","doi":"10.1074/jbc.M117.787622","authors":"Lv Z, Yuan L, Atkison JH, Aldana-Masangkay G, Chen Y, Olsen SK","authors_abbrev":"Lv Z et al.","pubmed_publication_date":"21 Jul 2017","pubmed_entrez_date":"2017-06-03","publication_year":"2017","canto_session_key":"af829a0c1e586f34","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-28 13:10:15","canto_approved_date":"2023-02-28 13:10:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-20 13:24:25","canto_added_date":"2017-06-04 00:15:15","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.02","SPBC1604.21c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-02-28","pdb_entries":[{"pdb_id":"5um6","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"}],"title":"Crystal Structure of S. pombe Uba1 in a closed conformation","entry_authors":"Lv Z,Yuan L,Aldana-Masangkay G,Atkison JH,Chen Y,Olsen SK","entry_authors_abbrev":"Lv Z et al.","reference_uniquename":"PMID:28572513","experimental_method":"X-ray","resolution":"2.794"}]},{"uniquename":"PMID:10546218","title":"[Telomere-binding activity of Schizosaccharomyces pombe yeasts].","citation":"Mol Biol (Mosk) 1999;33(4):644-50","abstract":"","authors":"Vasetskiĭ NS, Gilson E, Gasser SM","authors_abbrev":"Vasetskiĭ NS et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-11-05","publication_year":"1999","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15216885","title":"Multiple-color fluorescence imaging of chromosomes and microtubules in living cells.","citation":"Cell Struct Funct 1999 Oct;24(5):291-8","abstract":"Microscopic observation of fluorescently-stained intracellular molecules within a living cell provides a straightforward approach to understanding their temporal and spatial relationships. However, exposure to the excitation light used to visualize these fluorescently-stained molecules can be toxic to the cells. Here we describe several important considerations in microscope instrumentation and experimental conditions for avoiding the toxicity associated with observing living fluorescently-stained cells. Using a computer-controlled fluorescence microscope system designed for live observation, we recorded time-lapse, multi-color images of chromosomes and microtubules in living human and fission yeast cells. In HeLa cells, a human cell line, microtubules were stained with rhodamine-conjugated tubulin, and chromosomes were stained with a DNA-specific fluorescent dye, Hoechst33342, or with rhodamine-conjugated histone. In fission yeast cells, microtubules were stained with alpha-tubulin fused with the jellyfish green fluorescent protein (GFP), and chromosomes were stained with Hoechst33342.","authors":"Haraguchi T, Ding DQ, Yamamoto A, Kaneda T, Koujin T, Hiraoka Y","authors_abbrev":"Haraguchi T et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"2004-06-26","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14613978","title":"Correlations between gene expression and gene conservation in fission yeast.","citation":"Genome Res 2003 Dec;13(12):2686-90","abstract":"Genes can be expressed at a wide range of levels, and they show different degrees of cross-species conservation. We compared gene expression levels to gene conservation by integrating microarray data from fission yeast (Schizosaccharomyces pombe) with lists of \"core\" genes (present in worm and budding and fission yeasts), \"yeast-specific\" genes (present in budding and fission yeasts, but not in worm), and \"pombe-specific\" genes (present in fission yeast only). Whereas a disproportionate number of core genes are highly expressed in vegetatively growing cells, many pombe-specific genes are expressed at lower levels. This bias is less pronounced in cells undergoing sexual development, when many pombe-specific genes become highly expressed. This implies that organism-specific proteins are more likely to function during specialized processes such as cellular differentiation. Accordingly, pombe-specific genes were overrepresented among genes induced during sexual development; they were particularly enriched in a group of genes induced during meiotic prophase, when homologous chromosomes pair and recombine. This raises the possibility that organism-specific genes with functions in meiotic prophase favor speciation by preventing fruitful meiosis between closely related organisms. Finally, the set of genes induced late during sexual differentiation, at the time of spore formation, was enriched in yeast-specific genes, indicating that these genes play specialized roles in ascospore development.","authors":"Mata J, Bahler J","authors_abbrev":"Mata J et al.","pubmed_publication_date":"Dec 2003","pubmed_entrez_date":"2003-11-14","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25024163","title":"Evolutionarily diverse determinants of meiotic DNA break and recombination landscapes across the genome.","citation":"Genome Res 2014 Oct;24(10):1650-64","abstract":"Fission yeast Rec12 (Spo11 homolog) initiates meiotic recombination by forming developmentally programmed DNA double-strand breaks (DSBs). DSB distributions influence patterns of heredity and genome evolution, but the basis of the highly nonrandom choice of Rec12 cleavage sites is poorly understood, largely because available maps are of relatively low resolution and sensitivity. Here, we determined DSBs genome-wide at near-nucleotide resolution by sequencing the oligonucleotides attached to Rec12 following DNA cleavage. The single oligonucleotide size class allowed us to deeply sample all break events. We find strong evidence across the genome for differential DSB repair accounting for crossover invariance (constant cM/kb in spite of DSB hotspots). Surprisingly, about half of all crossovers occur in regions where DSBs occur at low frequency and are widely dispersed in location from cell to cell. These previously undetected, low-level DSBs thus play an outsized and crucial role in meiosis. We further find that the influence of underlying nucleotide sequence and chromosomal architecture differs in multiple ways from that in budding yeast. DSBs are not strongly restricted to nucleosome-depleted regions, as they are in budding yeast, but are nevertheless spatially influenced by chromatin structure. Our analyses demonstrate that evolutionarily fluid factors contribute to crossover initiation and regulation.","doi":"10.1101/gr.172122.114","authors":"Fowler KR, Sasaki M, Milman N, Keeney S, Smith GR","authors_abbrev":"Fowler KR et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-07-16","publication_year":"2014","canto_session_key":"2e52479a5dddb88c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-07-17 00:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11870208","title":"F-actin ring formation and the role of F-actin cables in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 2002 Mar 01;115(Pt 5):887-98","abstract":"Cells of the fission yeast Schizosaccharomyces pombe divide by the contraction of the F-actin ring formed at the medial region of the cell. We investigated the process of F-actin ring formation in detail using optical sectioning and three-dimensional reconstruction fluorescence microscopy. In wild-type cells, formation of an aster-like structure composed of F-actin cables and accumulation of F-actin cables were recognized at the medial cortex of the cell during prophase to metaphase. The formation of the aster-like structure seemed to initiate from branching of the longitudinal F-actin cables at a site near the spindle pole bodies, which had been duplicated but not yet separated. A single cable extended from the aster and encircled the cell at the equator to form a primary F-actin ring during metaphase. During anaphase, the accumulated F-actin cables were linked to the primary F-actin ring, and then all of these structures seemed to be packed to form the F-actin ring. These observations suggest that formation of the aster-like structure and the accumulation of the F-actin cables at the medial region of the cell during metaphase may be required to initiate the F-actin ring formation. In the nda3 mutant, which has a mutation in ss-tubulin and has been thought to be arrested at prophase, an F-actin ring with accumulated F-actin cables similar to that of anaphase wild-type cells was formed at a restrictive temperature. Immediately after shifting to a permissive temperature, this structure changed into a tightly packed ring. This suggests that the F-actin ring formation progresses beyond prophase in the nda3 cells once the cells enter prophase. We further examined F-actin structures in both cdc12 and cdc15 early cytokinesis mutants. As a result, Cdc12 seemed to be required for the primary F-actin ring formation during prophase, whereas Cdc15 may be involved in both packing the F-actin cables to form the F-actin ring and rearrangement of the F-actin after anaphase. In spg1, cdc7 and sid2 septum initiation mutants, the F-actin ring seemed to be formed in order.","authors":"Arai R, Mabuchi I","authors_abbrev":"Arai R et al.","pubmed_publication_date":"01 Mar 2002","pubmed_entrez_date":"2002-03-01","publication_year":"2002","canto_session_key":"e88640ffa62ff569","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-18 17:19:08","canto_approved_date":"2022-11-04 15:30:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-18 17:19:02","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPAC24B11.11c","SPAC20G8.05c","SPAC1F5.04c","SPAC1565.06c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2022-09-18"},{"uniquename":"PMID:26254313","title":"Cell-Size Control.","citation":"Cold Spring Harb Perspect Biol 2016 Apr 01;8(4):a019083","abstract":"Cells of a given type maintain a characteristic cell size to function efficiently in their ecological or organismal context. They achieve this through the regulation of growth rates or by actively sensing size and coupling this signal to cell division. We focus this review on potential size-sensing mechanisms, including geometric, external cue, and titration mechanisms. Mechanisms that titrate proteins against DNA are of particular interest because they are consistent with the robust correlation of DNA content and cell size. We review the literature, which suggests that titration mechanisms may underlie cell-size sensing in Xenopus embryos, budding yeast, and Escherichia coli, whereas alternative mechanisms may function in fission yeast.","doi":"10.1101/cshperspect.a019083","authors":"Amodeo AA, Skotheim JM","authors_abbrev":"Amodeo AA et al.","pubmed_publication_date":"01 Apr 2016","pubmed_entrez_date":"2015-08-09","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-08-10 00:19:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007799","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11719193","title":"Mus81-Eme1 are essential components of a Holliday junction resolvase.","citation":"Cell 2001 Nov 16;107(4):537-48","abstract":"Mus81, a fission yeast protein related to the XPF subunit of ERCC1-XPF nucleotide excision repair endonuclease, is essential for meiosis and important for coping with stalled replication forks. These processes require resolution of X-shaped DNA structures known as Holliday junctions. We report that Mus81 and an associated protein Eme1 are components of an endonuclease that resolves Holliday junctions into linear duplex products. Mus81 and Eme1 are required during meiosis at a late step of meiotic recombination. The mus81 meiotic defect is rescued by expression of a bacterial Holliday junction resolvase. These findings constitute strong evidence that Mus81 and Eme1 are subunits of a nuclear Holliday junction resolvase.","authors":"Boddy MN, Gaillard PHL, McDonald WH, Shanahan P, Yates JR, Russell P","authors_abbrev":"Boddy MN et al.","pubmed_publication_date":"16 Nov 2001","pubmed_entrez_date":"2001-11-24","publication_year":"2001","canto_session_key":"1352d0cf7b415a6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2016-09-03 11:46:48","canto_approved_date":"2022-09-23 14:03:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-27 22:43:28","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":31,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.05c","SPBC19C7.09c","SPAC644.14c","SPBC3E7.08c","SPBC4F6.15c","SPBC21B10.12","SPAPB1E7.06c","SPAC17A5.11","SPCC970.01"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2016-09-03"},{"uniquename":"PMID:14092430","title":"THE METABOLISM OF L-MALATE AND OTHER COMPOUNDS BY SCHIZOSACCHAROMYCES POMBE.","citation":"Arch Mikrobiol 1963 Sep 16;46:320-8","abstract":"","authors":"MAYER K, TEMPERLI A","authors_abbrev":"MAYER K et al.","pubmed_publication_date":"16 Sep 1963","pubmed_entrez_date":"1963-09-16","publication_year":"1963","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17284820","title":"Loss of a GPI-anchored membrane protein Aah3p causes a defect in vacuolar protein sorting in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2007 Feb;71(2):623-6","abstract":"Schizosaccharomyces pombe has four alpha-amylase homologs (Aah1p-Aah4p) with a glycosylphosphatidylinositol (GPI) modification site at the C-terminal end. Disruption mutants of aah genes were tested for mislocalization of vacuolar carboxypeptidase Y (CPY), and aah3Delta was found to secrete CPY. The conversion rate from pro- to mature CPY was greatly impaired in aah3Delta, and fluorescence microscopy inidicated that a sorting receptor for CPY, Vps10p, mislocalized to the vacuolar membrane. These results indicate that aah3Delta had a defect in the retrograde transport of Vps10p, and that Aah3p is the first S. pombe specific protein required for vacuolar protein sorting.","authors":"Iwaki T, Morita T, Tanaka N, Giga-Hama Y, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-02-08","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12214236","title":"Actin dynamics in the contractile ring during cytokinesis in fission yeast.","citation":"Nature 2002 Sep 05;419(6902):82-6","abstract":"Cytokinesis in many eukaryotes requires a contractile ring of actin and myosin that cleaves the cell in two. Little is known about how actin filaments and other components assemble into this ring structure and generate force. Here we show that the contractile ring in the fission yeast Schizosaccharomyces pombe is an active site of actin assembly. This actin polymerization activity requires Arp3, the formin Cdc12, profilin and WASP, but not myosin II or IQGAP proteins. Both newly polymerized actin filaments and pre-existing actin cables can contribute to the initial assembly of the ring. Once formed, the ring remains a dynamic structure in which actin and other ring components continuously assemble and disassemble from the ring every minute. The rate of actin polymerization can influence the rate of cleavage. Thus, actin polymerization driven by the Arp2/3 complex and formins is a central process in cytokinesis. Our studies show that cytokinesis is a more dynamic process than previously thought and provide a perspective on the mechanism of cell division.","authors":"Pelham RJ, Chang F","authors_abbrev":"Pelham RJ et al.","pubmed_publication_date":"05 Sep 2002","pubmed_entrez_date":"2002-09-06","publication_year":"2002","canto_session_key":"4698c66468ab5560","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-08-21 15:29:32","canto_approved_date":"2022-09-23 18:01:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-21 15:29:23","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.04c","SPAC4F10.15c","SPCC895.05","SPAC1F5.04c","SPAC4A8.15c","SPAC630.03"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-08-21"},{"uniquename":"PMID:16272747","title":"A fission yeast SNAP-25 homologue, SpSec9, is essential for cytokinesis and sporulation.","citation":"Cell Struct Funct 2005;30(2):15-24","abstract":"The soluble NSF attachment protein 25 (SNAP-25) is a component of the SNARE complex that is essential for regulated exocytosis in diverse cell types. Here, we identified a fission yeast SNAP-25 homologue, SpSec9. The sec9+ gene was essential for vegetative growth. sec9 mRNA was detected in vegetative cells and further increased during sporulation. This increase during sporulation was dependent on Mei4, a meiosis-specific transcription factor. A sporulation-deficient sec9 mutant was isolated by random PCR mutagenesis (sec9-10). The sec9-10 mutant also exhibited temperature sensitivity for growth and cell division was found to arrest before completion of cell separation at restrictive temperatures. In sec9-10 cells, the forespore membrane was normally initiated near spindle pole bodies during meiosis II. However, subsequent extension of the membrane was severely impaired. These results indicate that SpSec9 plays an important role both in cytokinesis and in sporulation.","authors":"Nakamura T, Kashiwazaki J, Shimoda C","authors_abbrev":"Nakamura T et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-11-08","publication_year":"2005","canto_session_key":"1d3f48e98af7ffd6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-12-15 12:45:38","canto_approved_date":"2024-05-16 13:10:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-11 18:05:59","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC825.03c","SPBC3H7.01","SPBC32H8.11","SPBC26H8.02c","SPBC31F10.06c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2023-12-15"},{"uniquename":"PMID:28103117","title":"Wee1 and Cdc25 are controlled by conserved PP2A-dependent mechanisms in fission yeast.","citation":"Cell Cycle 2017 Mar 04;16(5):428-435","abstract":"Wee1 and Cdc25 are conserved regulators of mitosis. Wee1 is a kinase that delays mitosis via inhibitory phosphorylation of Cdk1, while Cdc25 is a phosphatase that promotes mitosis by removing the inhibitory phosphorylation. Although Wee1 and Cdc25 are conserved proteins, it has remained unclear whether their functions and regulation are conserved across diverse species. Here, we analyzed regulation of Wee1 and Cdc25 in fission yeast. Both proteins undergo dramatic cell cycle-dependent changes in phosphorylation that are dependent upon PP2A associated with the regulatory subunit Pab1. The mechanisms that control Wee1 and Cdc25 in fission yeast appear to share similarities to those in budding yeast and vertebrates, which suggests that there may be common mechanisms that control mitotic entry in all eukaryotic cells.","doi":"10.1080/15384101.2017.1281476","authors":"Lucena R, Alcaide-Gavilán M, Anastasia SD, Kellogg DR","authors_abbrev":"Lucena R et al.","pubmed_publication_date":"04 Mar 2017","pubmed_entrez_date":"2017-01-20","publication_year":"2017","canto_session_key":"b27ca821f4f21986","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rafael Lucena","canto_first_approved_date":"2018-01-12 16:20:40","canto_approved_date":"2025-09-03 16:47:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-23 16:08:31","canto_added_date":"2017-01-21 01:15:10","annotation_curators":[{"name":"Rafael Lucena","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05","SPAC227.07c","SPAC1782.09c","SPBC11B10.09","SPBC582.03"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-01-12"},{"uniquename":"PMID:9584612","title":"Not so peculiar: fission yeast telomere repeats.","citation":"Trends Biochem Sci 1998 Apr;23(4):126","abstract":"","authors":"Hiraoka Y, Henderson E, Blackburn EH","authors_abbrev":"Hiraoka Y et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-05-19","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24256271","title":"Modelling the CDK-dependent transcription cycle in fission yeast.","citation":"Biochem Soc Trans 2013 Dec;41(6):1660-5","abstract":"CDKs (cyclin-dependent kinases) ensure directionality and fidelity of the eukaryotic cell division cycle. In a similar fashion, the transcription cycle is governed by a conserved subfamily of CDKs that phosphorylate Pol II (RNA polymerase II) and other substrates. A genetic model organism, the fission yeast Schizosaccharomyces pombe, has yielded robust models of cell-cycle control, applicable to higher eukaryotes. From a similar approach combining classical and chemical genetics, fundamental principles of transcriptional regulation by CDKs are now emerging. In the present paper, we review the current knowledge of each transcriptional CDK with respect to its substrate specificity, function in transcription and effects on chromatin modifications, highlighting the important roles of CDKs in ensuring quantity and quality control over gene expression in eukaryotes.","doi":"10.1042/BST20130238","authors":"Sansó M, Fisher RP","authors_abbrev":"Sansó M et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22986818","title":"D-amino acid-induced expression of D-amino acid oxidase in the yeast Schizosaccharomyces pombe.","citation":"Curr Microbiol 2012 Dec;65(6):764-9","abstract":"We investigated D-amino acid oxidase (DAO) induction in the popular model yeast Schizosaccharomyces pombe. The product of the putative DAO gene of the yeast expressed in E. coli displayed oxidase activity to neutral and basic D-amino acids, but not to an L-amino acid or acidic D-amino acids, showing that the putative DAO gene encodes catalytically active DAO. DAO activity was weakly detected in yeast cells grown on a culture medium without D-amino acid, and was approximately doubled by adding D-alanine. The elimination of ammonium chloride from culture medium induced activity by up to eight-fold. L-Alanine also induced the activity, but only by about half of that induced by D-alanine. The induction by D-alanine reached a maximum level at 2 h cultivation; it remained roughly constant until cell growth reached a stationary phase. The best inducer was D-alanine, followed by D-proline and then D-serine. Not effective were N-carbamoyl-D,L-alanine (a better inducer of DAO than D-alanine in the yeast Trigonopsis variabilis), and both basic and acidic D-amino acids. These results showed that S. pombe DAO could be a suitable model for analyzing the regulation of DAO expression in eukaryotic organisms.","doi":"10.1007/s00284-012-0227-z","authors":"Takahashi S, Okada H, Abe K, Kera Y","authors_abbrev":"Takahashi S et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-09-19","publication_year":"2012","canto_session_key":"00b05bd314e12321","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-05-23 15:46:20","canto_approved_date":"2025-12-05 19:24:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-13 23:32:54","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1450.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-05-23"},{"uniquename":"PMID:2682257","title":"Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis.","citation":"Nature 1989 Nov 02;342(6245):39-45","abstract":"The cdc2+ protein kinase (pp34) is found to be phosphorylated on tyrosine as well as serine and threonine residues in exponentially growing Schizosaccharomyces pombe. At mitosis, the level of pp34 phosphorylation on both threonine and tyrosine residues decreases. The single detectable site of tyrosine phosphorylation in pp34 has been mapped to Tyr 15, a residue within the presumptive ATP-binding domain. Substitution of this tyrosine by phenylalanine advances cells prematurely into mitosis, establishing that tyrosine phosphorylation/dephosphorylation directly regulates pp34 function.","authors":"Gould KL, Nurse P","authors_abbrev":"Gould KL et al.","pubmed_publication_date":"02 Nov 1989","pubmed_entrez_date":"1989-11-02","publication_year":"1989","canto_session_key":"3e2f643b12155f98","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-08-20 14:49:10","canto_approved_date":"2021-10-11 16:00:23","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-02-22 13:54:28","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":9,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2018-08-20"},{"uniquename":"PMID:12923256","title":"Mitochondrial RNase P RNAs in ascomycete fungi: lineage-specific variations in RNA secondary structure.","citation":"RNA 2003 Sep;9(9):1073-83","abstract":"The RNA subunit of mitochondrial RNase P (mtP-RNA) is encoded by a mitochondrial gene (rnpB) in several ascomycete fungi and in the protists Reclinomonas americana and Nephroselmis olivacea. By searching for universally conserved structural elements, we have identified previously unknown rnpB genes in the mitochondrial DNAs (mtDNAs) of two fission yeasts, Schizosaccharomyces pombe and Schizosaccharomyces octosporus; in the budding yeast Pichia canadensis; and in the archiascomycete Taphrina deformans. The expression of mtP-RNAs of the predicted size was experimentally confirmed in the two fission yeasts, and their precise 5' and 3' ends were determined by sequencing of cDNAs generated from circularized mtP-RNAs. Comparative RNA secondary structure modeling shows that in contrast to mtP-RNAs of the two protists R. americana and N. olivacea, those of ascomycete fungi all have highly reduced secondary structures. In certain budding yeasts, such as Saccharomycopsis fibuligera, we find only the two most conserved pairings, P1 and P4. A P18 pairing is conserved in Saccharomyces cerevisiae and its close relatives, whereas nearly half of the minimum bacterial consensus structure is retained in the RNAs of fission yeasts, Aspergillus nidulans and Taphrina deformans. The evolutionary implications of the reduction of mtP-RNA structures in ascomycetes will be discussed.","authors":"Seif ER, Forget L, Martin NC, Lang BF","authors_abbrev":"Seif ER et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-08-19","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35075549","title":"Schizosaccharomyces pombe Fzo1 is subjected to the ubiquitin-proteasome-mediated degradation during the stationary phase.","citation":"Int Microbiol 2022 May;25(2):397-404","abstract":"Mitochondria are highly dynamic organelles that undergo fission and fusion to adapt to the metabolic needs of the cell. Mitofusins are dynamin-like GTPases that play a key role in the regulation of mitochondrial fusion and metabolism. In Saccharomyces cerevisiae, mitofusin Fzo1 levels are controlled by post-translational ubiquitination and degradation. However, it is not clear whether the levels of the Schizosaccharomyces pombe mitofusin Fzo1 are similarly regulated. In this study, we examined the expression S. pombe Fzo1 during normal growth. We showed that Fzo1 protein levels but not mRNA expression levels were reduced during the stationary phase. The protein was stabilized by the proteasome inhibitor bortezomib. Disruption of ubc8 encoding a ubiquitin-conjugating enzyme and rsv2 encoding an S. pombe homolog of S. cerevisiae RPN4 known for activating the expression of genes required for proteasomal biogenesis suppresses the proteasomal degradation of Fzo1 during the stationary phase. Overexpression of fzo1 prevents its degradation. Our results suggest that like S. pombe Fzo1 expression is not regulated by transcription but rather by proteolytic degradation during the stationary phase. Our findings also suggest that although S. cerevisiae and S. pombe Fzo1 proteins are regulated by ubiquitin-proteasomal degradation, different ubiquitin-conjugating enzymes (E2) and ubiquitin ligases (E3) are involved in their degradation.","doi":"10.1007/s10123-022-00231-2","authors":"Ahmad F, Zhang Y, Yin H, Luo Y, Huang Y","authors_abbrev":"Ahmad F et al.","pubmed_publication_date":"May 2022","pubmed_entrez_date":"2022-01-25","publication_year":"2022","canto_session_key":"4a2275697a944b76","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2022-04-02 13:10:04","canto_approved_date":"2025-07-02 07:24:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-04-01 02:52:37","canto_added_date":"2022-01-27 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.15c","SPBC1706.03","SPBC1105.09","SPCC338.05c","SPAC18B11.07c","SPAC1250.03","SPAC10F6.05c","SPBC1105.14","SPBC211.07c","SPAC11E3.04c","SPBC2D10.20","SPBC119.02","SPBC1198.09","SPBP16F5.04"],"gene_count":14,"ltp_gene_count":3,"approved_date":"2022-04-02"},{"uniquename":"PMID:12697806","title":"Replication proteins influence the maintenance of telomere length and telomerase protein stability.","citation":"Mol Cell Biol 2003 May;23(9):3031-42","abstract":"We investigated the effects of fission yeast replication genes on telomere length maintenance and identified 20 mutant alleles that confer lengthening or shortening of telomeres. The telomere elongation was telomerase dependent in the replication mutants analyzed. Furthermore, the telomerase catalytic subunit, Trt1, and the principal initiation and lagging-strand synthesis DNA polymerase, Polalpha, were reciprocally coimmunoprecipitated, indicating these proteins physically coexist as a complex in vivo. In a polalpha mutant that exhibited abnormal telomere lengthening and slightly reduced telomere position effect, the cellular level of the Trt1 protein was significantly lower and the coimmunoprecipitation of Trt1 and Polalpha was severely compromised compared to those in the wild-type polalpha cells. Interestingly, ectopic expression of wild-type polalpha in this polalpha mutant restored the cellular Trt1 protein to the wild-type level and shortened the telomeres to near-wild-type length. These results suggest that there is a close physical relationship between the replication and telomerase complexes. Thus, mutation of a component of the replication complex can affect the telomeric complex in maintaining both telomere length equilibrium and telomerase protein stability.","authors":"Dahlén M, Sunnerhagen P, Wang TS","authors_abbrev":"Dahlén M et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-04-17","publication_year":"2003","canto_session_key":"6c7fa98f457520e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-06-28 16:32:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-16 16:11:23","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.04","SPAC20G8.01","SPAC3G6.06c","SPBC25H2.13c","SPBC1734.02c","SPBC29A3.14c","SPAC6B12.10c","SPAC3H5.06c","SPAC27E2.05","SPBC17D11.06"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-02-16"},{"uniquename":"PMID:8094323","title":"Mating configurations in Schizosaccharomyces pombe strains of different geographical origins.","citation":"Curr Genet 1993 Feb;23(2):108-14","abstract":"In genetic research with Schizosaccharomyces pombe the strains used are almost exclusively descendants of the clones originally isolated by Leupold. In the \"standard\" homothallic (h90) strain three closely linked mating-type (MT) genes are present in the MT region: the actual MT locus, mat1, and two silent cassettes, mat2 and mat3, respectively. Various rearrangements are known in the MT region, e.g., heterothallic h+ or h- strains arise by duplications or deletions. In the present paper we analysed the mating behavior and the configurations of the MT regions of 19 S. pombe isolates from different parts of the world. In comparison with the Leupold strains several new MT configurations were found.","authors":"Schlake T, Gutz H","authors_abbrev":"Schlake T et al.","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33574613","title":"TOR targets an RNA processing network to regulate facultative heterochromatin, developmental gene expression and cell proliferation.","citation":"Nat Cell Biol 2021 Mar;23(3):243-256","abstract":"Cell proliferation and differentiation require signalling pathways that enforce appropriate and timely gene expression. We find that Tor2, the catalytic subunit of the TORC1 complex in fission yeast, targets a conserved nuclear RNA elimination network, particularly the serine and proline-rich protein Pir1, to control gene expression through RNA decay and facultative heterochromatin assembly. Phosphorylation by Tor2 protects Pir1 from degradation by the ubiquitin-proteasome system involving the polyubiquitin Ubi4 stress-response protein and the Cul4-Ddb1 E3 ligase. This pathway suppresses widespread and untimely gene expression and is critical for sustaining cell proliferation. Moreover, we find that the dynamic nature of Tor2-mediated control of RNA elimination machinery defines gene expression patterns that coordinate fundamental chromosomal events during gametogenesis, such as meiotic double-strand-break formation and chromosome segregation. These findings have important implications for understanding how the TOR signalling pathway reprogrammes gene expression patterns and contributes to diseases such as cancer.","doi":"10.1038/s41556-021-00631-y","authors":"Wei Y, Lee NN, Pan L, Dhakshnamoorthy J, Sun LL, Zofall M, Wheeler D, Grewal SIS","authors_abbrev":"Wei Y et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2021-02-12","publication_year":"2021","canto_session_key":"c75277b83a634a8d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-03-18 15:32:06","canto_approved_date":"2024-02-07 07:38:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-11 08:36:26","canto_added_date":"2021-02-14 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":65,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.03c","SPAC19G12.17","SPBC32H8.11","SPAC27D7.13c","SPAC17H9.10c","SPNCRNA.103","SPAC7D4.14c","SPAC17A5.18c","SPAC3A11.08","SPAC27D7.03c","SPBC30D10.10c","SPBC4.07c","SPBC36B7.06c","SPBC337.08c","SPCC736.12c","SPBC216.07c","SPAC17H9.02","SPBC577.05c"],"gene_count":18,"ltp_gene_count":9,"approved_date":"2021-03-18"},{"uniquename":"PMID:11676925","title":"spRap1 and spRif1, recruited to telomeres by Taz1, are essential for telomere function in fission yeast.","citation":"Curr Biol 2001 Oct 16;11(20):1624-30","abstract":"Telomeres are essential for genome integrity. scRap1 (S. cerevisiae Rap1) directly binds to telomeric DNA and regulates telomere length and telomere position effect (TPE) by recruiting two different groups of proteins to its RCT (Rap1 C-terminal) domain. The first group, Rif1 and Rif2, regulates telomere length. The second group, Sir3 and Sir4, is involved in heterochromatin formation. On the other hand, human TRF1 and TRF2, as well as their fission yeast homolog, Taz1, directly bind to telomeric DNA and negatively regulate telomere length. Taz1 also plays important roles in TPE and meiosis. Human Rap1, the ortholog of scRap1, negatively regulates telomere length and appears to be recruited to telomeres by interacting with TRF2. Here, we describe two novel fission yeast proteins, spRap1 (S. pombe Rap1) and spRif1 (S. pombe Rif1), which are orthologous to scRap1 and scRif1, respectively. spRap1 and spRif1 are independently recruited to telomeres by interacting with Taz1. The rap1 mutant is severely defective in telomere length control, TPE, and telomere clustering toward the spindle pole body (SPB) at the premeiotic horsetail stage, indicating that spRap1 has critical roles in these telomere functions. The rif1 mutant also shows some defects in telomere length control and meiosis. Our results indicate that Taz1 provides binding sites for telomere regulators, spRap1 and spRif1, which perform the essential telomere functions. This study establishes the similarity of telomere organization in fission yeast and humans.","authors":"Kanoh J, Ishikawa F","authors_abbrev":"Kanoh J et al.","pubmed_publication_date":"16 Oct 2001","pubmed_entrez_date":"2001-10-26","publication_year":"2001","canto_session_key":"c0214f69cfa8d073","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-21 15:39:57","canto_approved_date":"2020-04-02 11:39:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-28 16:39:56","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.07c","SPAC6F6.17","SPBC1778.02"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-03-21"},{"uniquename":"PMID:39527209","title":"Label-Free Quantitative Phosphoproteomics in the Fission Yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2025;2862:297-307","abstract":"Protein phosphorylation is a dynamic, reversible posttranslational modification that plays an important role in the regulation of cell signaling. Recently, label-free quantitative (LFQ) phosphoproteomics has become a powerful tool to analyze the phosphorylation of proteins within complex samples. In this chapter, we describe how to apply LFQ phosphoproteomics that is based on Fe-IMAC phosphopeptide enrichment followed by strong anion exchange (SAX) and porous graphitic carbon (PGC) fractionation strategies for identification and quantification of changes in the phosphoproteome in the fission yeast Schizosaccharomyces pombe.","doi":"10.1007/978-1-0716-4168-2_21","authors":"Sivakova B, Jurcik J, Lukacova V, Lalakova LO, Selicky T, Cipakova I, Barath P, Cipak L","authors_abbrev":"Sivakova B et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6343851","title":"Studies on mutagenicity of 2 bronchodilators under development in Cuba.","citation":"Mutat Res 1983;117(3-4):225-36","abstract":"2 pyridoquinazolones, 2-amino-11H-pyrido[2,1-b]quinazolin-11-one (2-APQ) and 11H-pyrido[2,1-b]quinazolin-11-one (PQ), under development as anti-asthma drugs, were studied for mutagenicity. 2-APQ was found to be a strong mutagen in 5 strains of Salmonella typhimurium and a mild one in the forward-mutation system of the yeast Schizosaccharomyces pombe. Furthermore, 2-APQ had strong clastogenic effects in mouse bone marrow. Because of these results, development of 2-APQ as a bronchodilator was stopped. PQ, on the other hand, did not induce mutation in the 5 Salmonella strains or in S. pombe. S9 mix generally increased the response of 2-APQ in Salmonella dramatically. On the contrary, the mutagenic effectiveness of this compound in S. pombe was only slightly higher in the presence of S9 than without it, suggesting that metabolic activation was not effective in this system.","authors":"Jiménez MA, Torroella M, Fernández SI, Pellón R","authors_abbrev":"Jiménez MA et al.","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-05-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16143612","title":"Schizosaccharomyces pombe adenylate cyclase suppressor mutations suggest a role for cAMP phosphodiesterase regulation in feedback control of glucose/cAMP signaling.","citation":"Genetics 2005 Dec;171(4):1523-33","abstract":"Mutations affecting the Schizosaccharomyces pombe cAMP phosphodiesterase (PDE) gene cgs2+ were identified in a screen for suppressors of mutant alleles of the adenylate cyclase gene (git2+/cyr1+), which encode catalytically active forms of the enzyme that cannot be stimulated by extracellular glucose signaling. These mutations suppress both the git2(-) mutant alleles used in the suppressor selection and mutations in git1+, git3+, git5+, git7+, git10+, and git11+, which are all required for adenylate cyclase activation. Notably, these cgs2 mutant alleles fail to suppress mutations in gpa2+, which encodes the Galpha subunit of a heterotrimeric G protein required for adenylate cyclase activation, although the previously identified cgs2-2 allele does suppress loss of gpa2+. Further analysis of the cgs2-s1 allele reveals a synthetic interaction with the gpa2(R176H)-activated allele, with respect to derepression of fbp1-lacZ transcription in glucose-starved cells. In addition, direct measurements of cAMP levels show that cgs2-s1 cells maintain normal basal cAMP levels, but are severely defective in feedback regulation upon glucose detection. These results suggest that PDE activity in S. pombe may be coordinately regulated with adenylate cyclase activity as part of the feedback regulation mechanism to limit the cAMP response to glucose detection.","authors":"Wang L, Griffiths K, Zhang YH, Ivey FD, Hoffman CS","authors_abbrev":"Wang L et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-09-07","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC56F8.16","SPBC887.10","SPAC23H3.13c","SPAC24B11.06c","SPCC285.09c","SPBC19C7.03","SPBC106.10","SPAC22E12.14c","SPAC26F1.10c","SPBC21C3.20c","SPCC1753.02c"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:28674280","title":"Interplay between chromatin modulators and histone acetylation regulates the formation of accessible chromatin in the upstream regulatory region of fission yeast fbp1.","citation":"Genes Genet Syst 2018 May 03;92(6):267-276","abstract":"Numerous noncoding RNA transcripts are detected in eukaryotic cells. Noncoding RNAs transcribed across gene promoters are involved in the regulation of mRNA transcription via chromatin modulation. This function of noncoding RNA transcription was first demonstrated for the fission yeast fbp1 gene, where a cascade of noncoding RNA transcription events induces chromatin remodeling to facilitate transcription factor binding. We recently demonstrated that the noncoding RNAs from the fbp1 upstream region facilitate binding of the transcription activator Atf1 and thereby promote histone acetylation. Histone acetylation by histone acetyl transferases (HATs) and ATP-dependent chromatin remodelers (ADCRs) are implicated in chromatin remodeling, but the interplay between HATs and ADCRs in this process has not been fully elucidated. Here, we examine the roles played by two distinct ADCRs, Snf22 and Hrp3, and by the HAT Gcn5 in the transcriptional activation of fbp1. Snf22 and Hrp3 redundantly promote disassembly of chromatin in the fbp1 upstream region. Gcn5 critically contributes to nucleosome eviction in the absence of either Snf22 or Hrp3, presumably by recruiting Hrp3 in snf22∆ cells and Snf22 in hrp3∆ cells. Conversely, Gcn5-dependent histone H3 acetylation is impaired in snf22∆/hrp3∆ cells, suggesting that both redundant ADCRs induce recruitment of Gcn5 to the chromatin array in the fbp1 upstream region. These results reveal a previously unappreciated interplay between ADCRs and histone acetylation in which histone acetylation facilitates recruitment of ADCRs, while ADCRs are required for histone acetylation.","doi":"10.1266/ggs.17-00018","authors":"Adachi A, Senmatsu S, Asada R, Abe T, Hoffman CS, Ohta K, Hirota K","authors_abbrev":"Adachi A et al.","pubmed_publication_date":"03 May 2018","pubmed_entrez_date":"2017-07-05","publication_year":"2018","canto_session_key":"309444609ae01ccf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-02-08 16:22:56","canto_approved_date":"2025-09-03 15:04:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-14 22:29:27","canto_added_date":"2017-07-06 00:15:16","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.14c","SPCC1620.14c","SPAC664.02c","SPAC11E3.01c","SPAC1250.01","SPAC1952.05","SPAC3G6.01"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-02-08"},{"uniquename":"PMID:12215653","title":"Establishment and maintenance of a heterochromatin domain.","citation":"Science 2002 Sep 27;297(5590):2232-7","abstract":"The higher-order assembly of chromatin imposes structural organization on the genetic information of eukaryotes and is thought to be largely determined by posttranslational modification of histone tails. Here, we study a 20-kilobase silent domain at the mating-type region of fission yeast as a model for heterochromatin formation. We find that, although histone H3 methylated at lysine 9 (H3 Lys9) directly recruits heterochromatin protein Swi6/HP1, the critical determinant for H3 Lys9 methylation to spread in cis and to be inherited through mitosis and meiosis is Swi6 itself. We demonstrate that a centromere-homologous repeat (cenH) present at the silent mating-type region is sufficient for heterochromatin formation at an ectopic site, and that its repressive capacity is mediated by components of the RNA interference (RNAi) machinery. Moreover, cenH and the RNAi machinery cooperate to nucleate heterochromatin assembly at the endogenous mat locus but are dispensable for its subsequent inheritance. This work defines sequential requirements for the initiation and propagation of regional heterochromatic domains.","authors":"Hall IM, Shankaranarayana GD, Noma K, Ayoub N, Cohen A, Grewal SI","authors_abbrev":"Hall IM et al.","pubmed_publication_date":"27 Sep 2002","pubmed_entrez_date":"2002-09-07","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010274","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33410907","title":"The fission yeast Pin1 peptidyl-prolyl isomerase promotes dissociation of Sty1 MAPK from RNA polymerase II and recruits Ssu72 phosphatase to facilitate oxidative stress induced transcription.","citation":"Nucleic Acids Res 2021 Jan 25;49(2):805-817","abstract":"Pin1 is a peptidyl-prolyl isomerase that regulates the structure and function of eukaryotic RNA polymerase II (Pol II) through interaction with the C-terminal domain (CTD) of Rpb1, the largest subunit of Pol II. We demonstrated that this function is important for cellular response to oxidative stress in the fission yeast Schizosaccharomyces pombe. In response to oxidative stress, the Atf1 transcription factor targets Sty1, the mitogen-activated protein kinase (MAPK), to specific stress-responsive promoters. Anchored Sty1 recruits Pol II through direct association with Rpb1-CTD and phosphorylates the reiterated heptad sequence at Serine 5. Pin1 binds phosphorylated CTD to promote dissociation of Sty1 from it, and directly recruits Ssu72 phosphatase to facilitate dephosphorylation of CTD for transcription elongation. In the absence of Pin1, the association of Sty1-Atf1 with Rpb1 persists on stress-responsive promoters failed to generate transcripts of the corresponding genes effectively. The identified characteristic features of the fission yeast Pin1 are conserved in humans. We demonstrated that elevated Pin1 level in cancer cells might help to sustain survival under oxidative stress generated from their altered metabolic pathways. Together, these results suggest a conserved function of Pin1 in cellular response to oxidative stress among eukaryotic cells that might have clinical implication.","doi":"10.1093/nar/gkaa1243","authors":"Wang YT, Hsiao WY, Wang SW","authors_abbrev":"Wang YT et al.","pubmed_publication_date":"25 Jan 2021","pubmed_entrez_date":"2021-01-07","publication_year":"2021","canto_session_key":"7c2513328f82d364","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shao-Win Wang","canto_first_approved_date":"2021-01-28 11:59:29","canto_approved_date":"2025-09-03 11:03:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-19 07:17:56","canto_added_date":"2021-01-09 01:15:06","annotation_curators":[{"name":"Shao-Win Wang","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16C4.03","SPBC215.05","SPBC29B5.01","SPBC28F2.12","SPCC757.07c","SPAC24B11.06c","SPAP8A3.04c","SPAC3G9.04"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2021-01-28"},{"uniquename":"PMID:2953599","title":"Fungal small nuclear ribonucleoproteins share properties with plant and vertebrate U-snRNPs.","citation":"EMBO J 1987 Feb;6(2):469-76","abstract":"snRNAs with properties closely related to those of the major vertebrate U-snRNAs are present in the fungi Aspergillus nidulans, Neurospora crassa and Schizosaccharomyces pombe. These RNAs possess a tri-methyl guanosine cap structure and a subset cross-hybridizes with human U1 and U2 clones. In the form of snRNPs, snRNAs from these fungi as well as from Saccharomyces cerevisiae and pea plants are immunoprecipitated by human and anti-Sm or anti-(U1)RNP autoimmune antibodies. On micro-injection into the cytoplasm of Xenopus oocytes, the snRNAs are packaged into ribonucleoprotein particles and migrate into the nucleus. The results demonstrate a hitherto unsuspected degree of evolutionary conservation in snRNA structure, snRNP protein structure, and sites of RNA-protein interaction within snRNPs.","authors":"Tollervey D, Mattaj IW","authors_abbrev":"Tollervey D et al.","pubmed_publication_date":"Feb 1987","pubmed_entrez_date":"1987-02-01","publication_year":"1987","canto_session_key":"ec2f4ec0e8aa346d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-18 18:06:06","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-18 18:03:48","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.01","SPSNRNA.02","SPSNRNA.05","SPSNRNA.04"],"gene_count":4,"ltp_gene_count":0,"approved_date":"2014-06-18"},{"uniquename":"PMID:19237545","title":"The fission yeast SEL1 domain protein Cfh3p: a novel regulator of the glucan synthase Bgs1p whose function is more relevant under stress conditions.","citation":"J Biol Chem 2009 Apr 24;284(17):11070-9","abstract":"In Schizosaccharomyces pombe, Bgs1/Cps1p is a beta(1,3)-glucan synthase required for linear beta(1,3)-glucan synthesis and primary septum formation. Here, we have studied the regulation of Bgs1p by Cfh3/Chr4p, a member of a family of conserved adaptor proteins, which resembles the chitin synthase regulator Chs4p from Saccharomyces cerevisiae and Candida albicans. cfh3Delta cells showed a genetic interaction with cps1-191, and Cfh3p co-immunoprecipitated with Bgs1/Cps1p. In the absence of cfh3(+), cells were more sensitive to digestion by glucanases, and both Calcofluor staining and glucan synthesis were reduced. We found that in a wild-type strain, beta(1,3)-glucan synthesis was reduced under stress conditions. In the cfh3Delta, cps1-191, and cfh3Delta cps1-191 strains, beta(1,3)-glucan synthesis was further reduced, and growth was impaired under stress conditions, suggesting that Cfh3p and Bgs1p might play a role in ensuring growth in unfavorable environments. In a cfh3Delta mutant, Bgs1p was delocalized when the cells were distressed, but a blockade in endocytosis prevented this delocalization. Finally, we found that the SEL1 repeats are required for Cfh3p function. These results show that Cfh3p is a regulatory protein for Bgs1p and that its function is particularly necessary when the cells are undergoing stress.","doi":"10.1074/jbc.M808353200","authors":"Sharifmoghadam MR, Valdivieso MH","authors_abbrev":"Sharifmoghadam MR et al.","pubmed_publication_date":"24 Apr 2009","pubmed_entrez_date":"2009-02-25","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC1289.01c","SPBC19G7.05c","SPAC1F7.04","SPBC24C6.07"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PB_REF:0000008,PMID:37156916","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP27G11.08c","SPBC19G7.18c","SPAC57A7.15c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:33602740","title":"Microtubule-independent movement of the fission yeast nucleus.","citation":"J Cell Sci 2021 Mar 26;134(6)","abstract":"Movement of the cell nucleus typically involves the cytoskeleton and either polymerization-based pushing forces or motor-based pulling forces. In the fission yeast  Schizosaccharomyces pombe , nuclear movement and positioning are thought to depend on microtubule polymerization-based pushing forces. Here, we describe a novel, microtubule-independent, form of nuclear movement in fission yeast. Microtubule-independent nuclear movement is directed towards growing cell tips, and it is strongest when the nucleus is close to a growing cell tip, and weakest when the nucleus is far from that tip. Microtubule-independent nuclear movement requires actin cables but does not depend on actin polymerization-based pushing or myosin V-based pulling forces. The vesicle-associated membrane protein (VAMP)-associated proteins (VAPs) Scs2 and Scs22, which are critical for endoplasmic reticulum-plasma membrane contact sites in fission yeast, are also required for microtubule-independent nuclear movement. We also find that in cells in which microtubule-based pushing forces are present, disruption of actin cables leads to increased fluctuations in interphase nuclear positioning and subsequent altered septation. Our results suggest two non-exclusive mechanisms for microtubule-independent nuclear movement, which may help illuminate aspects of nuclear positioning in other cells.","doi":"10.1242/jcs.253021","authors":"Ashraf S, Tay YD, Kelly DA, Sawin KE","authors_abbrev":"Ashraf S et al.","pubmed_publication_date":"26 Mar 2021","pubmed_entrez_date":"2021-02-19","publication_year":"2021","canto_session_key":"e1a5bef02f357fd8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-02-21 01:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19215754","title":"Chapter 4. Evaluating the control of mRNA decay in fission yeast.","citation":"Methods Enzymol 2008;449:73-95","abstract":"Abnormalities in rates of mRNA decay can lead to changes in steady-state levels of transcripts, which in turn can result in changes in protein production and abnormal phenotypes. For example, mice deficient in the gene encoding tristetraprolin (TTP), a tandem CCCH zinc finger domain protein, develop a complex syndrome that includes wasting, arthritis, and myeloid hyperplasia, all secondary to elevated levels of tumor necrosis factor (TNF). This in turn reflects elevated levels of TNF mRNA, which is a direct \"target\" of TTP binding and TTP-promoted deadenylation and decay. Three TTP-like proteins are expressed in human and four in mice, all of which bind mRNA and control transcript decay. In contrast, the Schizosaccharomyces pombe genome contains only one TTP-like protein, named Zfs1. Microarray analysis revealed that S. pombe cells deficient in zfs1 overexpress the arz1 mRNA, which has several ideal TTP-like binding sites in its 3'-untranslated region (UTR). We used the \"no message in thiamine (nmt)\" repressible system, in which thiamine rapidly shuts off gene transcription, to evaluate the relative stability of the arz1 mRNA in wild-type and zfs1-deficient cells. We found that the arz1 mRNA decayed much more rapidly in the presence of endogenous zfs1 than in its absence. The nmt system also proved useful for the study of mRNA sequence elements that are essential for interactions with zfs1, which eventually results in accelerated transcript decay. These studies illustrate the utility of the S. pombe nmt system for evaluating protein-mRNA interactions that affect mRNA decay in vivo and provide an alternative to the use of transcription inhibitors or heat-sensitive polymerase promoters that are used more commonly to evaluate mRNA decay in Saccharomyces cerevesiae. We hope to use this convenient experimental system to unravel the mechanism by which TTP family members, in this and other organisms, bind to mRNAs and promote their instability.","doi":"10.1016/S0076-6879(08)02404-X","authors":"Cuthbertson BJ, Blackshear PJ","authors_abbrev":"Cuthbertson BJ et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2009-02-14","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3295780","title":"An electrophoretic karyotype for Schizosaccharomyces pombe by pulsed field gel electrophoresis.","citation":"Nucleic Acids Res 1987 Jun 11;15(11):4481-9","abstract":"The three chromosomal DNAs of S. pombe have been fractionated by pulsed field gel electrophoresis. The resulting molecular karyotype will greatly speed gene mapping in this organism, and it indicates that the separation range of the technique extends to DNA molecules as large as 9,000,000 base pairs.","authors":"Smith CL, Matsumoto T, Niwa O, Klco S, Fan JB, Yanagida M, Cantor CR","authors_abbrev":"Smith CL et al.","pubmed_publication_date":"11 Jun 1987","pubmed_entrez_date":"1987-06-11","publication_year":"1987","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38844045","title":"Structure-guided evolutionary analysis of interactome network rewiring at single residue resolution in yeasts.","citation":"J Mol Biol 2024 Jun 04;:168641","abstract":"Protein-protein interactions (PPIs) are known to rewire extensively during evolution leading to lineage-specific and species-specific changes in molecular processes. However, the detailed molecular evolutionary mechanisms underlying interactome network rewiring are not well-understood. Here, we combine high-confidence PPI data, high-resolution three-dimensional structures of protein complexes, and homology-based structural annotation transfer to construct structurally-resolved interactome networks for the two yeasts S. cerevisiae and S. pombe. We then classify PPIs according to whether they are preserved or different between the two yeast species and compare site-specific evolutionary rates of interfacial versus non-interfacial residues for these different categories of PPIs. We find that residues in PPI interfaces evolve significantly more slowly than non-interfacial residues when using lineage-specific measures of evolutionary rate, but not when using non-lineage-specific measures. Furthermore, both lineage-specific and non-lineage-specific evolutionary rate measures can distinguish interfacial residues from non-interfacial residues for preserved PPIs between the two yeasts, but only the lineage-specific measure is appropriate for rewired PPIs. Finally, both lineage-specific and non-lineage-specific evolutionary rate measures are appropriate for elucidating structural determinants of protein evolution for residues outside of PPI interfaces. Overall, our results demonstrate that unlike tertiary structures of single proteins, PPIs and PPI interfaces can be highly volatile in their evolution, thus requiring the use of lineage-specific measures when studying their evolution. These results yield insight into the evolutionary design principles of PPIs and the mechanisms by which interactions are preserved or rewired between species, improving our understanding of the molecular evolution of PPIs and PPI interfaces at the residue level.","doi":"10.1016/j.jmb.2024.168641","authors":"Pollet L, Xia Y","authors_abbrev":"Pollet L et al.","pubmed_publication_date":"04 Jun 2024","pubmed_entrez_date":"2024-06-06","publication_year":"2024","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2024-06-07 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27736299","title":"A genome-wide screen to identify genes controlling the rate of entry into mitosis in fission yeast.","citation":"Cell Cycle 2016 Nov 16;15(22):3121-3130","abstract":"We have carried out a haploinsufficiency (HI) screen in fission yeast using heterozygous deletion diploid mutants of a genome-wide set of cell cycle genes to identify genes encoding products whose level determines the rate of progression through the cell cycle. Cell size at division was used as a measure of advancement or delay of the G2-M transition of rod-shaped fission yeast cells. We found that 13 mutants were significantly longer or shorter (greater than 10%) than control cells at cell division. These included mutants of the cdc2, cdc25, wee1 and pom1 genes, which have previously been shown to play a role in the timing of entry into mitosis, and which validate this approach. Seven of these genes are involved in regulation of the G2-M transition, 5 for nuclear transport and one for nucleotide metabolism. In addition we identified 4 more genes that were 8-10% longer or shorter than the control that also had roles in regulation of the G2-M transition or in nuclear transport. The genes identified here are all conserved in human cells, suggesting that this dataset will be useful as a basis for further studies to identify rate-limiting steps for progression through the cell cycle in other eukaryotes.","authors":"Moris N, Shrivastava J, Jeffery L, Li JJ, Hayles J, Nurse P","authors_abbrev":"Moris N et al.","pubmed_publication_date":"16 Nov 2016","pubmed_entrez_date":"2016-10-14","publication_year":"2016","canto_session_key":"c7dfdbd8467f6d60","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-04-27 16:06:44","canto_approved_date":"2026-02-25 09:23:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-11-09 16:34:57","canto_added_date":"2016-10-15 00:15:12","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":34,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP27G11.10c","SPAC24H6.05","SPCC1840.03","SPCC18B5.03","SPAC644.06c","SPBC11B10.09","SPBC1734.14c","SPAC6B12.15","SPBC16H5.07c","SPBC582.03","SPAC26A3.15c","SPAC2F7.03c","SPCC1620.11","SPBC1198.02","SPCC290.03c","SPAC22G7.09c","SPAC1486.05"],"gene_count":17,"ltp_gene_count":17,"approved_date":"2017-04-27"},{"uniquename":"EMBL:SPD250","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2663184","title":"The Saccharomyces cerevisiae RAD2 gene complements a Schizosaccharomyces pombe repair mutation.","citation":"Curr Genet 1989 Jan;15(1):27-30","abstract":"Two Saccharomyces cerevisiae genes necessary for excision repair of UV damage in DNA, RAD1 and RAD2, were introduced individually, on a yeast shuttle vector, into seven Schizosaccharomyces pombe mutants - rads 1, 2, 5, 13, 15, 16 and 17. The presence of the cloned RAD1 gene did not affect survival of any of the S. pombe mutants. The RAD2 gene increased survival of S. pombe rad13 to near the wild-type level after UV irradiation and had no effect on any of the other mutants tested. S. pombe rad13 mutants are somewhat defective in removal of pyrimidine dimers so complementation by the S. cerevisiae RAD2 gene suggests that the genes may code for equivalent proteins in the two yeasts.","authors":"McCready SJ, Burkill H, Evans S, Cox BS","authors_abbrev":"McCready SJ et al.","pubmed_publication_date":"Jan 1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_session_key":"6c6a7b3bd357790c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 13:44:29","canto_session_submitted_date":"2012-03-03 13:43:57","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:12617726","title":"Mutagenesis of the HMGB (high-mobility group B) protein Cmb1 (cytosine-mismatch binding 1) of Schizosaccharomyces pombe: effects on recognition of DNA mismatches and damage.","citation":"Biochem J 2003 Jun 01;372(Pt 2):651-60","abstract":"Cmb1 (cytosine-mismatch binding 1) is a high-mobility group (HMG) protein of Schizosaccharomyces pombe, which consists of 223 amino acids and has a single HMG domain at the C-terminal end. We have created several mutant and deletion forms of the Cmb1 protein and studied the effects on general DNA binding and specific binding to DNA mismatches and damaged DNA. Cmb1Delta41 (i.e. Cmb1 from which the 41 N-terminal amino acids have been deleted) bound specifically to cytosine-containing mismatches, to the cisplatin-induced intrastrand cross-links cis -GG and cis -AG and to an O (6)-methylguanine lesion. DNA binding was not affected when the 45 N-terminal amino acids were deleted, but was abolished in the absence of the 50 N-terminal amino acids, and was reduced when Cmb1 was truncated by between five and eleven C-terminal amino acids. Cmb1, both with and without the C-terminal truncations, retained its DNA binding affinity after heating at 95 degrees C. The cmb1 gene was induced when S. pombe cells were treated with cisplatin. Mitotic mutation rates were increased in a S. pombe cmb1 null mutant and in a cmb1-(1-212) mutant, which encodes a Cmb1 protein lacking the 11 C-terminal amino acids. We conclude that mutation avoidance by Cmb1 is distinct from Msh2-dependent mismatch repair, but related to nucleotide excision repair.","authors":"Kunz C, Zurbriggen K, Fleck O","authors_abbrev":"Kunz C et al.","pubmed_publication_date":"01 Jun 2003","pubmed_entrez_date":"2003-03-06","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19G7.01c","SPAC4G9.11c","SPBC4F6.15c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23841919","title":"Antimicrobial activity of aurein 2.5 against yeasts.","citation":"FEMS Microbiol Lett 2013 Sep;346(2):140-5","abstract":"Fungal infections with multiple resistance to conventional antifungals are increasingly becoming a medical problem, and there is an urgent need for new antifungal compounds with novel mechanisms of action. Here, we show that aurein 2.5, a naturally occurring peptide antibiotic, displays activity against the fungal strains: Rhodotorula rubra and Schizosaccharomyces pombe (MICs < 130 μM). The peptide adopted high levels of membrane-interactive α-helical structure (> 65%) in the presence of lipid membranes derived from these organisms and showed strong propensities to penetrate (π ≥ 13 mN m(-1) ) and lyse them (> 70%). Based on these data, we suggest that aurein 2.5 kills yeasts via membranolytic mechanisms and may act as a template for the development of therapeutically useful antifungal agents.","doi":"10.1111/1574-6968.12212","authors":"Dennison SR, Harris F, Morton LH, Phoenix DA","authors_abbrev":"Dennison SR et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-07-12","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24906325","title":"Analyzing Cdc2/Cdk1 activation during stress response in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2014;1170:383-92","abstract":"Stress leads to multiple changes in the physiology of the cell. One of the most important is the adaptation of the cell cycle to the changing conditions of the environment. Cellular responses after stress can be followed by cellular synchronization previous to the insult. In this chapter, we use centrifugal elutriation to synchronize Schizosaccharomyces pombe cells and outline methods to investigate the hallmarks of cell cycle progression upon stress. These include analyses of cyclin-dependent kinase phosphorylation and cell size change.","doi":"10.1007/978-1-4939-0888-2_20","authors":"Rodríguez-Gabriel MA","authors_abbrev":"Rodríguez-Gabriel MA","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-06-08","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23297348","title":"Comprehensive proteomics analysis reveals new substrates and regulators of the fission yeast clp1/cdc14 phosphatase.","citation":"Mol Cell Proteomics 2013 May;12(5):1074-86","abstract":"The conserved family of Cdc14 phosphatases targets cyclin-dependent kinase substrates in yeast, mediating late mitotic signaling events. To discover substrates and regulators of the Schizosaccharomyces pombe Cdc14 phosphatase Clp1, TAP-tagged Clp1, and a substrate trapping mutant (Clp1-C286S) were purified from asynchronous and mitotic (prometaphase and anaphase) cells and binding partners were identified by 2D-LC-MS/MS. Over 100 Clp1-interacting proteins were consistently identified, over 70 of these were enriched in Clp1-C286S-TAP (potential substrates) and we and others detected Cdk1 phosphorylation sites in over half (44/73) of these potential substrates. According to GO annotations, Clp1-interacting proteins are involved in many essential cellular processes including mitosis, cytokinesis, ribosome biogenesis, transcription, and trafficking among others. We confirmed association and dephosphorylation of multiple candidate substrates, including a key scaffolding component of the septation initiation network called Cdc11, an essential kinase of the conserved morphogenesis-related NDR kinase network named Shk1, and multiple Mlu1-binding factor transcriptional regulators. In addition, we identified Sal3, a nuclear β-importin, as the sole karyopherin required for Clp1 nucleoplasmic shuttling, a key mode of Cdc14 phosphatase regulation. Finally, a handful of proteins were more abundant in wild type Clp1-TAP versus Clp1-C286S-TAP, suggesting that they may directly regulate Clp1 signaling or serve as scaffolding platforms to localize Clp1 activity.","doi":"10.1074/mcp.M112.025924","authors":"Chen JS, Broadus MR, McLean JR, Feoktistova A, Ren L, Gould KL","authors_abbrev":"Chen JS et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-01-09","publication_year":"2013","canto_session_key":"db3533d819cff33d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-Song Chen","canto_first_approved_date":"2018-10-04 15:57:21","canto_approved_date":"2026-02-04 11:31:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-09 14:12:06","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jun-Song Chen","community_curator":true,"annotation_count":67,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Jun-Song Chen","file_curator_role":"community","annotation_file_curators":[{"name":"Jun-Song Chen","community_curator":true,"annotation_count":490,"orcid":null,"file_type":"protein_modification","file_name":"PMID_23297348_modifications.tsv"}],"genes":["SPAC23A1.10","SPAC17H9.04c","SPBC18H10.02","SPCP1E11.04c","SPAC2G11.15c","SPAC9G1.06c","SPAC6F12.11c","SPAC18G6.07c","SPCC4G3.14","SPAC31A2.12","SPAC6F6.07c","SPAC23C11.05","SPBC21C3.13","SPBP4H10.15","SPCC613.05c","SPAC139.02c","SPCC1183.08c","SPAC1071.08","SPCC794.12c","SPAC17A2.09c","SPBC11B10.09","SPAC926.08c","SPBC8D2.18c","SPBC30D10.18c","SPAC3G9.01","SPBC18H10.03","SPBC1604.14c","SPBC16A3.18","SPBC11G11.03","SPCC962.02c","SPAC6F12.02","SPBP8B7.16c","SPBC56F2.12","SPAC1834.11c","SPBC1703.13c","SPCC895.07","SPBC3B8.02","SPCC1827.05c","SPBC21B10.13c","SPCC4G3.13c","SPBC13E7.03c","SPAC9E9.09c","SPBC336.12c","SPBC1289.04c","SPCP1E11.08","SPAC11E3.03","SPAC3F10.03","SPBC31E1.06","SPCC1739.01","SPAC14C4.14","SPAC3G9.03","SPBC83.08","SPAC4A8.15c","SPCC70.03c","SPAC18G6.14c","SPBC16A3.07c","SPAC3G6.04","SPBC646.07c","SPBC16H5.12c","SPBC17G9.09","SPBP4H10.04","SPBC336.15","SPBC146.13c","SPAPJ760.02c","SPAC18G6.05c","SPCC584.01c","SPCC1840.03","SPBC2F12.14c","SPAC926.09c","SPBC9B6.08","SPAC16E8.06c","SPAC3A11.12c","SPAC14C4.05c","SPAC30D11.04c","SPBC6B1.04","SPAC23G3.06","SPAC9G1.10c","SPCC1494.10","SPAC6F6.03c","SPCC645.06c","SPBC2F12.04","SPBC1A4.07c","SPAC29A4.20","SPBP8B7.03c","SPAC22F8.09","SPAC31A2.07c","SPBC354.13","SPAC29B12.01","SPAC20G8.06","SPAC27E2.03c","SPBC1A4.05","SPBC800.06","SPBC725.12","SPBC1685.15c","SPCC132.01c","SPAPB1A10.09","SPBP22H7.08","SPCC1827.03c","SPACUNK4.07c","SPBC21B10.03c","SPAC57A7.12","SPCC1919.09","SPCC16C4.13c","SPAC2C4.11c","SPCC1672.02c","SPBC1D7.04","SPAC1F7.02c","SPAC1782.09c","SPCC1682.03c","SPBC32F12.11","SPAC1687.06c","SPAC31G5.17c","SPCC1183.07","SPAC2G11.11c","SPBC23E6.04c","SPCC1840.02c","SPCPJ732.01","SPAC4F8.13c","SPBC16G5.11c","SPAP8A3.08","SPBC354.10","SPAC12G12.07c","SPBC32H8.05","SPCC16C4.14c","SPBC13G1.01c","SPAC9G1.09","SPBC16D10.04c","SPAC23G3.01","SPAC227.18","SPAC20G8.05c","SPCC576.08c","SPCC1795.11","SPCC1223.15c","SPAC6B12.12","SPAC3H5.12c","SPCC1223.07c","SPAC23A1.08c","SPAC4A8.11c","SPBC16A3.08c","SPCC1902.01","SPAP7G5.05","SPAC22H10.11c","SPAC17C9.03","SPBC15D4.01c","SPAC19G12.17","SPAC222.12c","SPAC664.08c","SPBC651.01c","SPBC3H7.13","SPBC8D2.07c","SPCPB16A4.05c","SPAC10F6.01c","SPBP19A11.03c","SPCC16C4.09","SPAC17A2.13c","SPCP1E11.11","SPAC17A5.14","SPBC800.04c","SPCC1281.01","SPAC23H3.08c","SPBC2F12.05c","SPAC16C9.06c","SPAC6G9.09c","SPBC2G2.08","SPAC4A8.05c","SPBC4F6.18c","SPCC1739.11c","SPAC1805.08","SPAC27D7.02c","SPBC31A8.01c","SPAC17H9.12c","SPBC25B2.07c","SPBC2F12.13","SPCC1682.12c","SPBC354.05c","SPCC417.08","SPAC12G12.04","SPAC24H6.05","SPCC1235.01","SPBC725.16","SPBP35G2.14","SPAC8E11.02c","SPBC21.06c","SPBP35G2.07","SPBC4F6.06","SPCC1682.09c","SPAC57A7.04c","SPBC32F12.08c","SPCC736.12c","SPBC1347.02","SPBC1778.01c","SPBC106.18","SPBC691.04","SPBP8B7.06","SPAC1A6.07","SPAC4F10.13c","SPBC26H8.08c","SPBC23G7.12c","SPBC776.08c","SPCC162.07","SPBC32H8.12c","SPBC19G7.06","SPAPB8E5.06c","SPAC22F3.09c","SPBC4F6.14","SPBC16G5.14c","SPAC22H12.04c","SPCC1322.12c","SPAC1F8.06","SPAC26F1.06","SPBPJ4664.04","SPBC83.15","SPAC56E4.04c","SPCC663.04","SPBC776.02c","SPAC13G6.02c","SPAC1071.10c","SPAC644.17c","SPAC1783.08c","SPCP1E11.06","SPBC336.07","SPBC4C3.12","SPBC146.07","SPBC16H5.08c","SPAC821.03c","SPCC4B3.15","SPCC16C4.07","SPAC32A11.04c","SPAC17G6.13","SPBC3F6.04c","SPAC664.11","SPCC1322.04","SPCC14G10.04","SPAC6G10.02c","SPAC12G12.03","SPAPB17E12.13","SPBC776.11","SPAC1565.06c","SPBC646.10c","SPAC8F11.04"],"gene_count":240,"ltp_gene_count":42,"approved_date":"2018-10-04"},{"uniquename":"PMID:30318352","title":"A Positive Feedback between Growth and Polarity Provides Directional Persistency and Flexibility to the Process of Tip Growth.","citation":"Curr Biol 2018 Oct 22;28(20):3342-3351.e3","abstract":"Polar cell growth is a conserved morphogenetic process needed for survival, mating, and infection [1, 2]. It typically implicates the assembly and spatial stabilization of a cortical polar domain of the active form of a small GTPase of the Rho family, such as Cdc42, which promotes cytoskeleton assembly and secretion needed for local surface expansion [3-6]. In multiple physiological instances, polarity domains may switch from being spatially unstable, exhibiting a wandering behavior around the cell surface, to being stable at a fixed cellular location [7-11]. Here, we show that the rate of surface growth may be a key determinant in controlling the spatial stability of active Cdc42 domains. Reducing the growth rate of single rod-shaped fission yeast cells using chemical, genetic, and mechanical means systematically causes polar domains to detach from cell tips and oscillate around the cell surface within minutes. Conversely, an abrupt increase in growth rate improves domain stabilization. A candidate screen identifies vesicular transport along actin cables as an important module mediating this process. Similar behavior observed in distant filamentous fungi suggests that this positive feedback between growth and polarity could represent a basal property of eukaryotic polarization, promoting persistent polar growth as well as growth redirection with respect to the mechanical environment of cells.","doi":"10.1016/j.cub.2018.09.022","authors":"Haupt A, Ershov D, Minc N","authors_abbrev":"Haupt A et al.","pubmed_publication_date":"22 Oct 2018","pubmed_entrez_date":"2018-10-16","publication_year":"2018","canto_session_key":"c41c0c9bff608b9c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-10-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28E12.03","SPAC4C5.02c","SPCC1223.06","SPCC1919.10c","SPCC895.05","SPAC24B11.06c","SPBC215.05"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:597860","title":"Temperature-sensitive lethal mutants in the structural gene for DNA ligase in the yeast Schizosaccharomyces pombe.","citation":"Cell 1977 Dec;12(4):1109-20","abstract":"","authors":"Nasmyth KA","authors_abbrev":"Nasmyth KA","pubmed_publication_date":"Dec 1977","pubmed_entrez_date":"1977-12-01","publication_year":"1977","canto_session_key":"b9876bd1c639eba1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-09-25 08:10:55","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-23 11:13:22","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-11-23"},{"uniquename":"PMID:23041194","title":"Plasma membrane tethering of the cortical ER necessitates its finely reticulated architecture.","citation":"Curr Biol 2012 Nov 06;22(21):2048-52","abstract":"The cortical endoplasmic reticulum (ER) is an intricate network of tubules and cisternae tightly associated with the plasma membrane (PM) in plants, yeast, and the excitable cell types in metazoans [1-5]. How the ER is attached to the cell cortex and what necessitates its highly reticulated architecture remain largely unknown. Here, we identify the integral ER vesicle-associated membrane protein-associated proteins (VAPs), previously shown to control the composition of phosphoinositides at the ER-PM contact sites [6, 7], as major players in sustaining the ER-PM tethering in fission yeast. We show that genetic conversion of the reticulated ER structure to the cisternal morphology shields large areas of the PM, preventing the actomyosin division ring assembly at the equatorial cortex. Using a combination of VAP mutants where the cortical ER is detached from the PM and a set of artificial ER-PM tethers suppressing this phenotype, we demonstrate that the PM footprint of the cortical ER is functionally insulated from the cytosol. In cells with prominent ER-PM contacts, fine reticulation of the ER network may have emerged as a critical adaptation enabling a uniform access of peripheral protein complexes to the inner surface of the plasma membrane.","doi":"10.1016/j.cub.2012.08.047","authors":"Zhang D, Vjestica A, Oliferenko S","authors_abbrev":"Zhang D et al.","pubmed_publication_date":"06 Nov 2012","pubmed_entrez_date":"2012-10-09","publication_year":"2012","canto_session_key":"8c85c01f83c1d4eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dan Zhang","canto_first_approved_date":"2016-12-18 13:06:38","canto_approved_date":"2026-04-22 15:33:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-15 17:24:29","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Dan Zhang","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31A8.01c","SPCC1919.10c","SPCC830.08c","SPCC895.05","SPCC1223.06","SPBC1539.04","SPBC16G5.05c","SPAC17C9.12","SPAPYUG7.03c","SPBC2D10.14c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2016-12-18"},{"uniquename":"PMID:16797182","title":"Conserved ribonuclease, Eri1, negatively regulates heterochromatin assembly in fission yeast.","citation":"Curr Biol 2006 Jul 25;16(14):1459-64","abstract":"RNA interference (RNAi) is a conserved silencing mechanism that has widespread roles in RNA degradation, translational repression, and the epigenetic control of chromatin structure [1]. In fission yeast, heterochromatin assembly requires RNAi machinery and is initiated by small interference RNAs (siRNAs) derived from heterochromatic regions and by the RNA-induced transcriptional silencing (RITS) complex [2-7]. Although recent studies have been successful in uncovering the functions of effector complexes in the RNAi pathway [4, 5, 8-10], exactly how heterochromatic siRNAs are processed and function in assembling heterochromatin remains unclear. In this study we focused on a conserved ribonuclease, Eri1, which was originally identified as a negative regulator of RNAi in C. elegans [11], and show the importance of the Eri1 protein in RNAi-mediated heterochromatin assembly in fission yeast. Eri1 specifically degrades double-stranded siRNAs through two functional domains and represses the accumulation of cellular siRNAs in vivo. Deletion of eri1(+) causes an increase in siRNAs associated with the RITS complex and enhances heterochromatic silencing, which is accompanied by increased levels of histone H3-K9 methylation and the Swi6 protein. Our findings suggest that the fission yeast Eri1 controls the accumulation of heterochromatic siRNAs and negatively regulates the RNAi-mediated heterochromatin assembly.","authors":"Iida T, Kawaguchi R, Nakayama J","authors_abbrev":"Iida T et al.","pubmed_publication_date":"25 Jul 2006","pubmed_entrez_date":"2006-06-27","publication_year":"2006","canto_session_key":"2c86d2eb654cc74c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-11 00:34:28","canto_approved_date":"2024-02-05 15:58:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-02 20:41:07","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPCC188.13c","SPCC736.11","SPBC30B4.08","SPAC6F12.09"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-12-11"},{"uniquename":"PMID:10835380","title":"Four chromo-domain proteins of Schizosaccharomyces pombe differentially repress transcription at various chromosomal locations.","citation":"Genetics 2000 Jun;155(2):551-68","abstract":"Transcription is repressed in regions of the fission yeast genome close to centromeres, telomeres, or the silent mating-type cassettes mat2-P and mat3-M. The repression involves the chromo-domain proteins Swi6 and Clr4. We report that two other chromo-domain proteins, Chp1 and Chp2, are also important for these position effects. Chp1 showed a specificity for centromeric regions. Its essentiality for the transcriptional repression of centromeric markers correlates with its importance for chromosome stability. Chp2 appeared more pleiotropic. Its effects on centromeric silencing were less pronounced than those of Chp1, and it participated in telomeric position effects and transcriptional silencing in the mating-type region. We also found that PolII-transcribed genes were repressed when placed in one of the Schizosaccharomyces pombe rDNA clusters, a situation analogous to that in the budding yeast Saccharomyces cerevisiae. Chp2, Swi6, Clr4, and, to a lesser extent, Chp1 participated in that repression.","authors":"Thon G, Verhein-Hansen J","authors_abbrev":"Thon G et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-06-03","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c","SPBC16C6.10","SPAC18G6.02c","SPAC664.01c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:11298745","title":"Hsp90 chaperone complexes are required for the activity and stability of yeast protein kinases Mik1, Wee1 and Swe1.","citation":"Eur J Biochem 2001 Apr;268(8):2281-9","abstract":"The Wee1 protein kinase negatively regulates entry into mitosis by mediating the inhibitory tyrosine phosphorylation of Cdc2-cyclin B kinase. The stability and activity of Wee1 from the fission yeast Schizosaccharomyces pombe is critically dependent on functional Hsp90 chaperones. Here we identify two related tyrosine protein kinases, Mik1 from fission yeast and its Saccharomyces cerevisiae homolog Swe1, as Hsp90 substrates and show that the kinase domain is sufficient to mediate this interaction. Morphological and biochemical defects arising from overexpression of the kinases in fission yeast are suppressed in the conditional Hsp90 mutant swo1-26. A subset of all three kinases is associated with the Hsp90 cochaperones cyclophilin 40 and p23. Under conditions of impaired chaperone function or treatment with the Hsp90 inhibitory drug geldanamycin, intracellular levels of the kinases are reduced and the proteins become rapidly degraded by the proteasome machinery, indicating that Wee1, Mik1 and Swe1 require Hsp90 heterocomplexes for their stability and maintenance of function.","authors":"Goes FS, Martin J","authors_abbrev":"Goes FS et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-04-12","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC926.04c","SPBC660.14","SPAC9E9.13"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:19029808","title":"Mec1 function in the DNA damage response does not require its interaction with Tel2.","citation":"Cell Cycle 2008 Dec;7(23):3695-8","abstract":"The essential, conserved Tel2 protein plays a role in the response to DNA damage and replication stress in a wide range of eukaryotes. Tel2 interacts physically with multiple members of the PI3-kinase related protein kinase (PIKK) family in mammalian cells and fission yeast. In mammalian cells, loss of Tel2 leads to destabilization of PIKKs. Our previous work in the yeast Saccharomyces cerevisiae showed that Tel2 interacts with the PIKK Tel1 (yeast ATM kinase), and that this interaction is abrogated by the only known non-lethal TEL2 mutation in S. cerevisiae, tel2-1. We showed that this mutation specifically disrupts the function of Tel1 and not the function of the closely related protein Mec1 (yeast ATR kinase) in DNA damage responses. Here we show that Tel2 and Mec1 interact in S. cerevisiae, and that surprisingly, this physical interaction is also disrupted by the tel2-1 mutation. Although the tel2-1 mutation leads to moderately lower Mec1 levels, the ability of Mec1 to localize to a site of DNA damage and to function in DNA damage signaling remains intact. These results suggest that the model of Tel2 as solely a global regulator of PIKK stability is insufficient. Rather, Tel2 can specifically and differentially regulate the function of individual PIKKs.","authors":"Anderson CM, Blackburn EH","authors_abbrev":"Anderson CM et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-11-26","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15042280","title":"Identification of thermostable glyoxalase I in the fission yeast Schizosaccharomyces pombe.","citation":"Arch Microbiol 2004 May;181(5):371-7","abstract":"Glyoxalase I is a ubiquitous enzyme that detoxifies methylglyoxal, which is derived from glycolysis but inhibits the growth of cells from microorganisms to mammals. Here, the structural gene for glyoxalase I ( glo1(+)) from the fission yeast Schizosaccharomyces pombe was identified. Disruption of glo1(+) enhanced susceptibility to methylglyoxal, while expression of glo1(+) in a Delta glo1 mutant of Saccharomyces cerevisiae restored tolerance to this aldehyde. The glo1(+) gene product was purified. The glyoxalase I of S. pombe was a monomeric enzyme with a molecular weight of 34000 and the k(cat)/ K(m) value for methylglyoxal was 4.3 x 10(7) M(-1) x min(-1). Treatment of purified enzyme with EDTA in imidazole buffer completely abolished enzyme activity, whereas the EDTA-treated enzyme was reactivated by several divalent metal ions, such as Zn(2+), Co(2+), Ni(2+) and Mn(2+). The glyoxalase I of S. pombe exhibited fairly high thermal stability, and almost 100% activity was retained after incubating the enzyme at 60 degrees C for 4 h.","authors":"Takatsume Y, Izawa S, Inoue Y","authors_abbrev":"Takatsume Y et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-03-26","publication_year":"2004","canto_session_key":"4712d5987610575b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-03-28 13:40:56","canto_approved_date":"2026-03-28 13:40:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-02-26 11:00:16","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2026-03-28"},{"uniquename":"PMID:15974010","title":"Influence of phospholipid fatty acid composition of plasma membrane on sensitivity of plasma membrane ATPase of a self-flocculating yeast to in vivo ethanol activation and its relationship to ethanol tolerance.","citation":"Sheng Wu Gong Cheng Xue Bao 2004 Sep;20(5):784-9","abstract":"Although alterations in fatty acid composition of phospholipids in plasma membranes had no effect on activities of plasma membrane ATPases of a self-flocculating fusant of Schizosaccharomyces pombe and Saccharomyces cerevisiae cells grown in the absence of ethanol (basal enzymes), they significantly affected the susceptibilities of the enzymes to in vivo activation induced by ethanol: the maximal values for the activated enzymes in cells pregrown with 0.6 mmol/L palmitic, linoleic or linolenic acid respectively were 3.6, 1.5 and 1.2-fold higher than their respective basal levels (in cells grown without ethanol), whereas the corresponding value for cells pregrown in the absence of fatty acid was 2.3-fold, with the concentrations of ethanol for the above maximal in vivo activation of enzymes being 7%, 6%, 6% and 7% (V/V) respectively. The Km values for ATP, the pH profiles, and the sensitivities to orthovanadate of the basal and the activated plasma membrane ATPases were essentially identical; however, the v(max) values of activated enzymes increased significantly. It was found that the characteristics of phospholipid fatty acid composition of plasma membrane leading to the enhanced ethanol tolerance of this strain, were also efficacious to increase the percentage of activation of plasma membrane ATPase per unit of ethanol. These data support a close correlation between the ethanol tolerance of this strain and the sensitivity of its plasma membrane ATPase to the in vivo ethanol-induced activation.","authors":"Hu CK, Bai FW, An LJ","authors_abbrev":"Hu CK et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2005-06-25","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24952478","title":"Recent advances in the genetics of dystonia.","citation":"Curr Neurol Neurosci Rep 2014 Aug;14(8):462","abstract":"Dystonia, a common and genetically heterogeneous neurological disorder, was recently defined as \"a movement disorder characterized by sustained or intermittent muscle contractions causing abnormal, often repetitive, movements, postures, or both.\" Via the application of whole-exome sequencing, the genetic landscape of dystonia and closely related movement disorders is becoming exposed. In particular, several \"novel\" genetic causes have been causally associated with dystonia or dystonia-related disorders over the past 2 years. These genes include PRRT2 (DYT10), CIZ1 (DYT23), ANO3 (DYT24), GNAL (DYT25), and TUBB4A (DYT4). Despite these advances, major gaps remain in identifying the genetic origins for most cases of adult-onset isolated dystonia. Furthermore, model systems are needed to study the biology of PRRT2, CIZ1, ANO3, Gαolf, and TUBB4A in the context of dystonia. This review focuses on these recent additions to the family of dystonia genes, genotype-phenotype correlations, and possible cellular contributions of the encoded proteins to the development of dystonia.","doi":"10.1007/s11910-014-0462-8","authors":"Xiao J, Vemula SR, LeDoux MS","authors_abbrev":"Xiao J et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-06-23","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC800.05c","SPBC16A3.15c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:32421152","title":"Calcineurin-dependent regulation of endocytosis by a plasma membrane ubiquitin ligase adaptor, Rcr1.","citation":"J Cell Biol 2020 Aug 03;219(8)","abstract":"Rsp5, the Nedd4 family member in yeast, is an E3 ubiquitin ligase involved in numerous cellular processes, many of which require Rsp5 to interact with PY-motif containing adaptor proteins. Here, we show that two paralogous transmembrane Rsp5 adaptors, Rcr1 and Rcr2, are sorted to distinct cellular locations: Rcr1 is a plasma membrane (PM) protein, whereas Rcr2 is sorted to the vacuole. Rcr2 is delivered to the vacuole using ubiquitin as a sorting signal. Rcr1 is delivered to the PM by the exomer complex using a newly uncovered PM sorting motif. Further, we show that Rcr1, but not Rcr2, is up-regulated via the calcineurin/Crz1 signaling pathway. Upon exogenous calcium treatment, Rcr1 ubiquitinates and down-regulates the chitin synthase Chs3. We propose that the PM-anchored Rsp5/Rcr1 ubiquitin ligase-adaptor complex can provide an acute response to degrade unwanted proteins under stress conditions, thereby maintaining cell integrity.","doi":"10.1083/jcb.201909158","authors":"Zhu L, Sardana R, Jin DK, Emr SD","authors_abbrev":"Zhu L et al.","pubmed_publication_date":"03 Aug 2020","pubmed_entrez_date":"2020-05-19","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.05","SPBP4H10.04"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:4537088","title":"A -glucan endo-hydrolase from Schizosaccharomyces pombe and its role in cell wall growth.","citation":"Antonie Van Leeuwenhoek 1972;38(1):65-80","abstract":"","authors":"Barras DR","authors_abbrev":"Barras DR","pubmed_publication_date":"1972","pubmed_entrez_date":"1972-01-01","publication_year":"1972","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7876346","title":"The fission yeast cdc19+ gene encodes a member of the MCM family of replication proteins.","citation":"J Cell Sci 1994 Oct;107 ( Pt 10):2779-88","abstract":"We have cloned and characterized the fission yeast cdc19+ gene. We demonstrate that it encodes a structural homologue of the budding yeast MCM2 protein. In fission yeast, the cdc19+ gene is constitutively expressed, and essential for viability. Deletion delays progression through S phase, and cells arrest in the first cycle with an apparent 2C DNA content, with their checkpoint control intact. The temperature-sensitive cdc19-P1 mutation is synthetically lethal with cdc21-M68. In addition, we show by classical and molecular genetics that cdc19+ is allelic to the nda1+ locus. We conclude that cdc19p plays a potentially conserved role in S phase.","authors":"Forsburg SL, Nurse P","authors_abbrev":"Forsburg SL et al.","pubmed_publication_date":"Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_session_key":"c1136816cdaa2d17","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-11-16 16:41:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-04-17 18:19:43","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPBC4.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-04-17"},{"uniquename":"PMID:17486116","title":"Gamma-tubulin complex-mediated anchoring of spindle microtubules to spindle-pole bodies requires Msd1 in fission yeast.","citation":"Nat Cell Biol 2007 Jun;9(6):646-53","abstract":"The anchoring of microtubules to subcellular structures is critical for cell polarity and motility. Although the process of anchoring cytoplasmic microtubules to the centrosome has been studied in some detail, it is not known how spindle microtubules are anchored to the mitotic centrosome and, particularly, whether anchoring and nucleation of mitotic spindles are functionally separate. Here, we show that a fission yeast coiled-coil protein, Msd1, is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body (SPB). msd1 deletion causes spindle microtubules to abnormally extend beyond SPBs, which results in chromosome missegregation. Importantly, this protruding spindle is phenocopied by the amino-terminal deletion mutant of Alp4, a component of the gamma-tubulin complex (gamma-TuC), which lacks the potential Msd1-interacting domain. We propose that Msd1 interacts with gamma-TuC, thereby specifically anchoring the minus end of microtubules to SPBs without affecting microtubule nucleation.","authors":"Toya M, Sato M, Haselmann U, Asakawa K, Brunner D, Antony C, Toda T","authors_abbrev":"Toya M et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-05-09","publication_year":"2007","canto_session_key":"3adb4fd16e0b2a9a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-04-29 11:09:58","canto_approved_date":"2022-07-09 12:03:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-05 13:48:01","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC13E7.06","SPBC365.15"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-04-29"},{"uniquename":"PMID:8246900","title":"In vivo species specificity of DNA polymerase alpha.","citation":"Mol Gen Genet 1993 Nov;241(3-4):457-66","abstract":"The DNA polymerase alpha enzymes from human, and budding (Saccharomyces cerevisiae) and fission yeast (Schizosaccharomyces pombe) are homologous proteins involved in initiation and replication of chromosomal DNA. Sequence comparison of human DNA polymerase alpha with that of S. cerevisiae and S. pombe shows overall levels of amino acid sequence identity of 32% and 34%, respectively. We report here that, despite the sequence conservation among these three enzymes, functionally active human DNA polymerase alpha fails to rescue several different conditional lethal alleles of the budding yeast POL1 gene at nonpermissive temperature. Furthermore, human DNA polymerase alpha cannot complement a null allele of budding yeast POL1 either in germinating spores or in vegetatively growing cells. In fission yeast, functionally active human DNA polymerase alpha is also unable to complement the disrupted pol alpha::ura4+ allele in germinating spores. Thus, in vivo, DNA polymerase alpha has stringent species specificity for initiation and replication of chromosomal DNA.","authors":"Francesconi S, Copeland WC, Wang TS","authors_abbrev":"Francesconi S et al.","pubmed_publication_date":"Nov 1993","pubmed_entrez_date":"1993-11-01","publication_year":"1993","canto_session_key":"1ca3d3194a428d2b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:33:52","canto_session_submitted_date":"2012-03-03 15:33:35","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3H5.06c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:30566651","title":"Comprehensive profiling of the fission yeast transcription start site activity during stress and media response.","citation":"Nucleic Acids Res 2019 Feb 28;47(4):1671-1691","abstract":"Fission yeast, Schizosaccharomyces pombe, is an attractive model organism for transcriptional and chromatin biology research. Such research is contingent on accurate annotation of transcription start sites (TSSs). However, comprehensive genome-wide maps of TSSs and their usage across commonly applied laboratory conditions and treatments for S. pombe are lacking. To this end, we profiled TSS activity genome-wide in S. pombe cultures exposed to heat shock, nitrogen starvation, hydrogen peroxide and two commonly applied media, YES and EMM2, using Cap Analysis of Gene Expression (CAGE). CAGE-based annotation of TSSs is substantially more accurate than existing PomBase annotation; on average, CAGE TSSs fall 50-75 bp downstream of PomBase TSSs and co-localize with nucleosome boundaries. In contrast to higher eukaryotes, dispersed TSS distributions are not common in S. pombe. Our data recapitulate known S. pombe stress expression response patterns and identify stress- and media-responsive alternative TSSs. Notably, alteration of growth medium induces changes of similar magnitude as some stressors. We show a link between nucleosome occupancy and genetic variation, and that the proximal promoter region is genetically diverse between S. pombe strains. Our detailed TSS map constitutes a central resource for S. pombe gene regulation research.","doi":"10.1093/nar/gky1227","authors":"Thodberg M, Thieffry A, Bornholdt J, Boyd M, Holmberg C, Azad A, Workman CT, Chen Y, Ekwall K, Nielsen O, Sandelin A","authors_abbrev":"Thodberg M et al.","pubmed_publication_date":"28 Feb 2019","pubmed_entrez_date":"2018-12-20","publication_year":"2019","canto_session_key":"d422700f21f8e048","canto_annotation_status":"APPROVED","canto_triage_status":"Browser datasets, hosted","canto_curator_role":"PomBase","canto_first_approved_date":"2020-03-11 17:51:03","canto_approved_date":"2020-03-11 17:51:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-11 17:47:23","canto_added_date":"2018-12-21 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2020-03-11"},{"uniquename":"PMID:30498568","title":"The inhibition of checkpoint activation by telomeres does not involve exclusion of dimethylation of histone H4 lysine 20 (H4K20me2).","citation":"F1000Res 2018;7:1027","abstract":"DNA double-strand breaks (DSBs) activate the DNA damage checkpoint machinery to pause or halt the cell cycle.  Telomeres, the specific DNA-protein complexes at linear eukaryotic chromosome ends, are capped DSBs that do not activate DNA damage checkpoints.  This \"checkpoint privileged\" status of telomeres was previously investigated in the yeast   Schizosaccharomyces pombe lacking the major double-stranded telomere DNA binding protein Taz1. Telomeric DNA repeats in cells lacking Taz1 are 10 times longer than normal and contain single-stranded DNA regions. DNA damage checkpoint proteins associate with these damaged telomeres, but the DNA damage checkpoint is not activated. This severing of the DNA damage checkpoint signaling pathway was reported to stem from exclusion of histone H4 lysine 20 dimethylation (H4K20me2) from telomeric nucleosomes in both wild type cells and cells lacking Taz1.  However, experiments to identify the mechanism of this exclusion failed, prompting our re-evaluation of H4K20me2 levels at telomeric chromatin.  In this short report, we used an extensive series of controls to identify an antibody specific for the H4K20me2 modification and show that the level of this modification is the same at telomeres and internal loci in both wild type cells and those lacking Taz1.  Consequently, telomeres must block activation of the DNA Damage Response by another mechanism that remains to be determined.","doi":"10.12688/f1000research.15166.2","authors":"Audry J, Wang J, Eisenstatt JR, Berkner KL, Runge KW","authors_abbrev":"Audry J et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-12-04","publication_year":"2018","canto_session_key":"b0c74f66c791b22e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-12-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18622392","title":"Fission yeast SWI/SNF and RSC complexes show compositional and functional differences from budding yeast.","citation":"Nat Struct Mol Biol 2008 Aug;15(8):873-80","abstract":"SWI/SNF chromatin-remodeling complexes have crucial roles in transcription and other chromatin-related processes. The analysis of the two members of this class in Saccharomyces cerevisiae, SWI/SNF and RSC, has heavily contributed to our understanding of these complexes. To understand the in vivo functions of SWI/SNF and RSC in an evolutionarily distant organism, we have characterized these complexes in Schizosaccharomyces pombe. Although core components are conserved between the two yeasts, the compositions of S. pombe SWI/SNF and RSC differ from their S. cerevisiae counterparts and in some ways are more similar to metazoan complexes. Furthermore, several of the conserved proteins, including actin-like proteins, are markedly different between the two yeasts with respect to their requirement for viability. Finally, phenotypic and microarray analyses identified widespread requirements for SWI/SNF and RSC on transcription including strong evidence that SWI/SNF directly represses iron-transport genes.","doi":"10.1038/nsmb.1452","authors":"Monahan BJ, Villén J, Marguerat S, Bähler J, Gygi SP, Winston F","authors_abbrev":"Monahan BJ et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-07-16","publication_year":"2008","canto_session_key":"f78ad3d74aa426ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-25 02:58:46","canto_approved_date":"2023-11-02 18:06:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-29 17:46:52","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":91,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.15","SPAC17D4.01","SPCC16A11.14","SPAC23G3.10c","SPBP4G3.02","SPAC23H3.10","SPAC1071.06","SPBC30B4.04c","SPCC1620.14c","SPAC18B11.10","SPAC3C7.14c","SPBP23A10.05","SPCC1281.05","SPAC23D3.09","SPBC1703.02","SPAC630.14c","SPAC2F7.08c","SPBC26H8.09c","SPAC17G6.10","SPAC1250.01","SPAC22H12.02","SPAC23G3.07c","SPBC4B4.03","SPAC1F3.07c"],"gene_count":24,"ltp_gene_count":21,"approved_date":"2018-04-25"},{"uniquename":"PMID:6818425","title":"Nonsense suppression in Schizosaccharomyces pombe: the S. pombe Sup3-e tRNASerUGA gene is active in S. cerevisiae.","citation":"Mol Gen Genet 1982;188(2):219-24","abstract":"The gene encoding the efficient UGA suppressor sup3-e of Schizosaccharomyces pombe was isolated by in vivo transformation of Saccharomyces cerevisiae UGA mutants with S. pombe sup3-e DNA. DNA from a clone bank of EcoRI fragments from a S. pombe sup3-e strain in the hybrid yeast vector YRp17 was used to transform the S. cerevisiae multiple auxotroph his4-260 leu2-2 trp1-1 to prototrophy. Transformants were isolated at a low frequency; they lost the ability to grow in minimal medium after passaging in non-selective media. This suggested the presence of the suppressor gene on the non-integrative plasmid. Plasmid DNA, isolated from the transformed S. cerevisiae cells and subsequently amplified in E. coli, transformed S. cerevisiae his4-260 leu2-2 trp1-1 to prototrophy. In this way a 2.4 kb S. pombe DNA fragment carrying the sup3-e gene was isolated. Sequence analysis revealed the presence of two tRNA coding regions separated by a spacer of only seven nucleotides. The sup3-e tRNASerUGA tRNA gene is followed by a sequence coding for the initiator tRNAMet. The transformation results demonstrate that the cloned S. pombe UGA suppressor is active in S. cerevisiae UGA mutant strains.","authors":"Hottinger H, Pearson D, Yamao F, Gamulin V, Cooley L, Cooper T, Söll D","authors_abbrev":"Hottinger H et al.","pubmed_publication_date":"1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_session_key":"0ab24f740bba8f08","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-23 13:15:57","canto_approved_date":"2021-11-10 16:41:24","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-10-23 13:15:46","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPATRNASER.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-23"},{"uniquename":"PMID:31837996","title":"The Chaperone FACT and Histone H2B Ubiquitination Maintain S. pombe Genome Architecture through Genic and Subtelomeric Functions.","citation":"Mol Cell 2020 Feb 06;77(3):501-513.e7","abstract":"The histone chaperone FACT and histone H2B ubiquitination (H2Bub) facilitate RNA polymerase II (Pol II) passage through chromatin, yet it is not clear how they cooperate mechanistically. We used genomics, genetic, biochemical, and microscopic approaches to dissect their interplay in Schizosaccharomyces pombe. We show that FACT and H2Bub globally repress antisense transcripts near the 5' end of genes and inside gene bodies, respectively. The accumulation of these transcripts is accompanied by changes at genic nucleosomes and Pol II redistribution. H2Bub is required for FACT activity in genic regions. In the H2Bub mutant, FACT binding to chromatin is altered and its association with histones is stabilized, which leads to the reduction of genic nucleosomes. Interestingly, FACT depletion globally restores nucleosomes in the H2Bub mutant. Moreover, in the absence of Pob3, the FACT Spt16 subunit controls the 3' end of genes. Furthermore, FACT maintains nucleosomes in subtelomeric regions, which is crucial for their compaction.","doi":"10.1016/j.molcel.2019.11.016","authors":"Murawska M, Schauer T, Matsuda A, Wilson MD, Pysik T, Wojcik F, Muir TW, Hiraoka Y, Straub T, Ladurner AG","authors_abbrev":"Murawska M et al.","pubmed_publication_date":"06 Feb 2020","pubmed_entrez_date":"2019-12-16","publication_year":"2020","canto_session_key":"e2d6e48248e1c105","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Magdalena Murawska","canto_first_approved_date":"2021-07-22 15:09:48","canto_approved_date":"2025-12-11 10:14:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-07-16 08:41:41","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Magdalena Murawska","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC609.05","SPBC8D2.04","SPBP8B7.19","SPCC622.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2021-07-22"},{"uniquename":"PMID:31618757","title":"HP1 reshapes nucleosome core to promote phase separation of heterochromatin.","citation":"Nature 2019 Nov;575(7782):390-394","abstract":"Heterochromatin affects genome function at many levels. It enables heritable gene repression, maintains chromosome integrity and provides mechanical rigidity to the nucleus 1,2 . These diverse functions are proposed to arise in part from compaction of the underlying chromatin 2 . A major type of heterochromatin contains at its core the complex formed between HP1 proteins and chromatin that is methylated on histone H3, lysine 9 (H3K9me). HP1 is proposed to use oligomerization to compact chromatin into phase-separated condensates 3-6 . Yet, how HP1-mediated phase separation relates to chromatin compaction remains unclear. Here we show that chromatin compaction by the Schizosaccharomyces pombe HP1 protein Swi6 results in phase-separated liquid condensates. Unexpectedly, we find that Swi6 substantially increases the accessibility and dynamics of buried histone residues within a nucleosome. Restraining these dynamics impairs compaction of chromatin into liquid droplets by Swi6. Our results indicate that Swi6 couples its oligomerization to the phase separation of chromatin by a counterintuitive mechanism, namely the dynamic exposure of buried nucleosomal regions. We propose that such reshaping of the octamer core by Swi6 increases opportunities for multivalent interactions between nucleosomes, thereby promoting phase separation. This mechanism may more generally drive chromatin organization beyond heterochromatin.","doi":"10.1038/s41586-019-1669-2","authors":"Sanulli S, Trnka MJ, Dharmarajan V, Tibble RW, Pascal BD, Burlingame AL, Griffin PR, Gross JD, Narlikar GJ","authors_abbrev":"Sanulli S et al.","pubmed_publication_date":"Nov 2019","pubmed_entrez_date":"2019-10-17","publication_year":"2019","canto_session_key":"4aa187e950e89fa9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-10-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20829797","title":"Telomeres avoid end detection by severing the checkpoint signal transduction pathway.","citation":"Nature 2010 Sep 09;467(7312):228-32","abstract":"Telomeres protect the normal ends of chromosomes from being recognized as deleterious DNA double-strand breaks. Recent studies have uncovered an apparent paradox: although DNA repair is prevented, several proteins involved in DNA damage processing and checkpoint responses are recruited to telomeres in every cell cycle and are required for end protection. It is currently not understood how telomeres prevent DNA damage responses from causing permanent cell cycle arrest. Here we show that fission yeast (Schizosaccharomyces pombe) cells lacking Taz1, an orthologue of human TRF1 and TRF2 (ref. 2), recruit DNA repair proteins (Rad22(RAD52) and Rhp51(RAD51), where the superscript indicates the human orthologue) and checkpoint sensors (RPA, Rad9, Rad26(ATRIP) and Cut5/Rad4(TOPBP1)) to telomeres. Despite this, telomeres fail to accumulate the checkpoint mediator Crb2(53BP1) and, consequently, do not activate Chk1-dependent cell cycle arrest. Artificially recruiting Crb2(53BP1) to taz1Δ telomeres results in a full checkpoint response and cell cycle arrest. Stable association of Crb2(53BP1) to DNA double-strand breaks requires two independent histone modifications: H4 dimethylation at lysine 20 (H4K20me2) and H2A carboxy-terminal phosphorylation (γH2A). Whereas γH2A can be readily detected, telomeres lack H4K20me2, in contrast to internal chromosome locations. Blocking checkpoint signal transduction at telomeres requires Pot1 and Ccq1, and loss of either Pot1 or Ccq1 from telomeres leads to Crb2(53BP1) foci formation, Chk1 activation and cell cycle arrest. Thus, telomeres constitute a chromatin-privileged region of the chromosomes that lack essential epigenetic markers for DNA damage response amplification and cell cycle arrest. Because the protein kinases ATM and ATR must associate with telomeres in each S phase to recruit telomerase, exclusion of Crb2(53BP1) has a critical role in preventing telomeres from triggering cell cycle arrest.","doi":"10.1038/nature09353","authors":"Carneiro T, Khair L, Reis CC, Borges V, Moser BA, Nakamura TM, Ferreira MG","authors_abbrev":"Carneiro T et al.","pubmed_publication_date":"09 Sep 2010","pubmed_entrez_date":"2010-09-11","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24322298","title":"A critical switch in the enzymatic properties of the Cid1 protein deciphered from its product-bound crystal structure.","citation":"Nucleic Acids Res 2014 Mar;42(5):3372-80","abstract":"The addition of uridine nucleotide by the poly(U) polymerase (PUP) enzymes has a demonstrated impact on various classes of RNAs such as microRNAs (miRNAs), histone-encoding RNAs and messenger RNAs. Cid1 protein is a member of the PUP family. We solved the crystal structure of Cid1 in complex with non-hydrolyzable UMPNPP and a short dinucleotide compound ApU. These structures revealed new residues involved in substrate/product stabilization. In particular, one of the three catalytic aspartate residues explains the RNA dependence of its PUP activity. Moreover, other residues such as residue N165 or the β-trapdoor are shown to be critical for Cid1 activity. We finally suggest that the length and sequence of Cid1 substrate RNA influence the balance between Cid1's processive and distributive activities. We propose that particular processes regulated by PUPs require the enzymes to switch between the two types of activity as shown for the miRNA biogenesis where PUPs can either promote DICER cleavage via short U-tail or trigger miRNA degradation by adding longer poly(U) tail. The enzymatic properties of these enzymes may be critical for determining their particular function in vivo.","doi":"10.1093/nar/gkt1278","authors":"Munoz-Tello P, Gabus C, Thore S","authors_abbrev":"Munoz-Tello P et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2013-12-11","publication_year":"2014","canto_session_key":"173b353377d08cd6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-02-25 14:09:09","canto_approved_date":"2023-01-27 16:34:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-28 22:09:54","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-02-25","pdb_entries":[{"pdb_id":"4nku","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A/B","position":"40-377"}],"title":"Structure of Cid1 in complex with its short product ApU","entry_authors":"Munoz-Tello P,Gabus C,Thore S","entry_authors_abbrev":"Munoz-Tello P et al.","reference_uniquename":"PMID:24322298","experimental_method":"X-ray","resolution":"1.94"},{"pdb_id":"4nkt","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A/B","position":"40-377"}],"title":"Structure of Cid1 in complex with the UTP analog UMPNPP","entry_authors":"Munoz-Tello P,Gabus C,Thore S","entry_authors_abbrev":"Munoz-Tello P et al.","reference_uniquename":"PMID:24322298","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:9774699","title":"Reverse transcription of a self-primed retrotransposon requires an RNA structure similar to the U5-IR stem-loop of retroviruses.","citation":"Mol Cell Biol 1998 Nov;18(11):6859-69","abstract":"An inverted repeat (IR) within the U5 region of the Rous sarcoma virus (RSV) mRNA forms a structure composed of a 7-bp stem and a 5-nucleotide (nt) loop. This U5-IR structure has been shown to be required for the initiation of reverse transcription. The mRNA of Tf1, long terminal repeat-containing retrotransposon from fission yeast (Schizosaccharomyces pombe) contains nucleotides with the potential to form a U5-IR stem-loop that is strikingly similar to that of RSV. The putative U5-IR stem-loop of Tf1 consists of a 7-bp stem and a 25-nt loop. Results from mutagenesis studies indicate that the U5-IR stem-loop in the mRNA of Tf1 does form and that it is required for Tf1 transposition. Although the loop is required for transposition, we were surprised that the specific sequence of the nucleotides within the loop was unimportant for function. Additional investigation indicates that the loss of transposition activity due to a reduction in the loop size to 6 nt could be rescued by increasing the GC content of the stem. This result indicates that the large loop in the Tf1 mRNA relative to that of the RSV allows the formation of the relatively weak U5-IR stem. The levels of Tf1 proteins expressed and the amounts of Tf1 RNA packaged into the virus-like particles were not affected by mutations in the U5-IR structure. However, all of the mutations in the U5-IR structure that caused defects in transposition produced low amounts of reverse transcripts. A unique feature in the initiation of Tf1 reverse transcription is that, instead of a tRNA, the first 11 nt of the Tf1 mRNA serve as the minus-strand primer. Analysis of the 5' end of Tf1 mRNA revealed that the mutations in the U5-IR stem-loop that resulted in defects in reverse transcription caused a reduction in the cleavage activity required to generate the Tf1 primer. Our results indicate that the U5-IR stems of Tf1 and RSV are conserved in size, position, and function.","authors":"Lin JH, Levin HL","authors_abbrev":"Lin JH et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1998-10-17","publication_year":"1998","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8896278","title":"Molecular, functional and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe.","citation":"Yeast 1996 Sep 15;12(11):1107-24","abstract":"The synthesis of mevalonate, a molecule required for both sterol and isoprene biosynthesis in eukaryotes, is catalysed by 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase. Using a gene dosage approach, we have isolated the gene encoding HMG-CoA reductase hmgl+, from the fission yeast Schizosaccharomyces pombe (Accession Number L76979). Specifically, hmgl+ was isolated on the basis of its ability to confer resistance to lovastatin, a competitive inhibitor of HMG-CoA reductase. Gene disruption analysis showed that hmgl+ was an essential gene. This result provided evidence that, unlike Saccharomyces cerevisiae, S. pombe contained only a single functional HMG-CoA reductase gene. The presence of a single HMG-CoA reductase gene was confirmed by genomic hybridization analysis. As observed for the S. cerevisiae HMGlp, the hmgl+ protein induced membrane proliferations known as karmellae. A previously undescribed 'feed-forward' regulation was observed in which elevated levels of HMG-CoA synthase, the enzyme catalysing the synthesis of the HMG-CoA reductase substrate, induced elevated levels of hmgl+ protein in the cell and conferred partial resistance to lovastatin. The amino acid sequences of yeast and human HMG-CoA reductase were highly divergent in the membrane domains, but were extensively conserved in the catalytic domains. We tested whether the gene duplication that produced the two functional genes in S. cerevisiae occurred before or after S. pombe and S. cerevisiae diverged by comparing the log likelihoods of trees specified by these hypotheses. We found that the tree specifying post-divergence duplication had significantly higher likelihood. Moreover, phylogenetic analyses of available HMG-CoA reductase sequences also suggested that the lineages of S. pombe and S. cerevisiae diverged approximately 420 million years ago but that the duplication event that produced two HMG-CoA reductase genes in the budding yeast occurred only approximately 56 million years ago. To date, S. pombe is the only unicellular eukaryote that has been found to contain a single HMG-CoA reductase gene. Consequently, S. pombe may provide important opportunities to study aspects of the regulation of sterol biosynthesis that have been difficult to address in other organisms and serve as a test organism to identify novel therapies for modulating cholesterol synthesis.","authors":"Lum PY, Edwards S, Wright R","authors_abbrev":"Lum PY et al.","pubmed_publication_date":"15 Sep 1996","pubmed_entrez_date":"1996-09-15","publication_year":"1996","canto_session_key":"234a6b34cd32c361","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-09-10 16:26:53","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-10 16:26:47","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.14c","SPCC162.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-09-10"},{"uniquename":"PMID:21149262","title":"A failure of meiotic chromosome segregation in a fbh1Delta mutant correlates with persistent Rad51-DNA associations.","citation":"Nucleic Acids Res 2011 Mar;39(5):1718-31","abstract":"The F-box DNA helicase Fbh1 constrains homologous recombination in vegetative cells, most likely through an ability to displace the Rad51 recombinase from DNA. Here, we provide the first evidence that Fbh1 also serves a vital meiotic role in fission yeast to promote normal chromosome segregation. In the absence of Fbh1, chromosomes remain entangled or segregate unevenly during meiosis, and genetic and cytological data suggest that this results in part from a failure to efficiently dismantle Rad51 nucleofilaments that form during meiotic double-strand break repair.","doi":"10.1093/nar/gkq977","authors":"Sun W, Lorenz A, Osman F, Whitby MC","authors_abbrev":"Sun W et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2010-12-15","publication_year":"2011","canto_session_key":"7f2b8021cbcd1936","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPAC644.14c","SPBC336.01","SPBC119.14","SPAC30D11.10"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:8704325","title":"Construction and characterization of a deletion mutant of gpd2 that encodes an isozyme of NADH-dependent glycerol-3-phosphate dehydrogenase in fission yeast.","citation":"Biosci Biotechnol Biochem 1996 May;60(5):918-20","abstract":"Schizosaccharomyces pombe has two genes each encoding an isozyme of NADH-dependent glycerol-3-phosphate dehydrogenases (gpd1+ and gpd2+). To gain an insight into the function of these genes, here we constructed a gpd2 deletion mutant, in addition to the previously constructed gpd1 deletion mutant. We showed that the gpd1+ and gpd2+ gene-products are both functional in terms of the de novo glycerol synthesis. Furthermore, the gpd1(+)-mediated glycerol production is primarily responsible for the osmoregulation, but the gpd2+ gene is not. Interestingly, however, the gpd2 deletion mutant had histidine- or lysine-auxotrophy for growth on a minimal medium.","authors":"Yamada H, Ohmiya R, Aiba H, Mizuno T","authors_abbrev":"Yamada H et al.","pubmed_publication_date":"May 1996","pubmed_entrez_date":"1996-05-01","publication_year":"1996","canto_session_key":"56aa925b00bb840b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-09-30 08:45:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 15:46:09","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23D3.04c","SPBC215.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-09-11"},{"uniquename":"PMID:15722486","title":"Biochemical characterization and DNA repair pathway interactions of Mag1-mediated base excision repair in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2005;33(3):1123-31","abstract":"The Schizosaccharomyces pombe mag1 gene encodes a DNA repair enzyme with sequence similarity to the AlkA family of DNA glycosylases, which are essential for the removal of cytotoxic alkylation products, the premutagenic deamination product hypoxanthine and certain cyclic ethenoadducts such as ethenoadenine. In this paper, we have purified the Mag1 protein and characterized its substrate specificity. It appears that the substrate range of Mag1 is limited to the major alkylation products, such as 3-mA, 3-mG and 7-mG, whereas no significant activity was found towards deamination products, ethenoadducts or oxidation products. The efficiency of 3-mA and 3-mG removal was 5-10 times slower for Mag1 than for Escherichia coli AlkA whereas the rate of 7-mG removal was similar to the two enzymes. The relatively low efficiency for the removal of cytotoxic 3-methylpurines is consistent with the moderate sensitivity of the mag1 mutant to methylating agents. Furthermore, we studied the initial steps of Mag1-dependent base excision repair (BER) and genetic interactions with other repair pathways by mutant analysis. The double mutants mag1 nth1, mag1 apn2 and mag1 rad2 displayed increased resistance to methyl methanesulfonate (MMS) compared with the single mutants nth1, apn2 and rad2, respectively, indicating that Mag1 initiates both short-patch (Nth1-dependent) and long-patch (Rad2-dependent) BER of MMS-induced damage. Spontaneous intrachromosomal recombination frequencies increased 3-fold in the mag1 mutant suggesting that Mag1 and recombinational repair (RR) are both involved in repair of alkylated bases. Finally, we show that the deletion of mag1 in the background of rad16, nth1 and rad2 single mutants reduced the total recombination frequencies of all three double mutants, indicating that abasic sites formed as a result of Mag1 removal of spontaneous base lesions are substrates for nucleotide excision repair, long- and short-patch BER and RR.","authors":"Alseth I, Osman F, Korvald H, Tsaneva I, Whitby MC, Seeberg E, Bjørås M","authors_abbrev":"Alseth I et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-02-22","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.06c","SPAC3C7.03c","SPBC3D6.10","SPAC30D11.07","SPAPB24D3.04c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:18849471","title":"Thiol-independent action of mitochondrial thioredoxin to support the urea cycle of arginine biosynthesis in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2008 Dec;7(12):2160-7","abstract":"Thioredoxins usually perform a role as a thiol-disulfide oxidoreductase using their active-site cysteines. The fission yeast Schizosaccharomyces pombe contains two thioredoxins: Trx1 for general stress protection and Trx2 for mitochondrial functions. The Deltatrx2 mutant grows as well as the wild type on complex media containing glucose. However, on nonfermentable carbon source such as glycerol, the mutant did not grow, indicating a defect in mitochondrial function. The mutant also exhibited auxotrophy for arginine and cysteine on minimal medium. In order to find the reason for the unexpected arginine auxotrophy, we searched for multicopy suppressors and found that the arg3(+) gene encoding ornithine carbamoyltransferase (OCTase) in the urea cycle of the arginine biosynthetic pathway rescued the arginine auxotrophy. The levels of arg3(+) transcript, Arg3 protein, and OCTase activity were all decreased in Deltatrx2. Through immunocoprecipitation, we observed a direct interaction between Trx2 and Arg3 in cell extracts. The mutant forms of Trx2 lacking either one or both of the active site cysteines through substitution to serines also rescued the arginine auxotrophy and restored the decreased OCTase activity. They also rescued the growth defect of Deltatrx2 on glycerol medium. This contrasts with the thiol-dependent action of overproduced Trx2 in complementing glutathione reductase. Therefore, Trx2 serves multiple functions in mitochondria, protecting mitochondrial components against thiol-oxidative damage as a thiol-disulfide oxidoreductase, and supporting urea cycle and respiration in mitochondria in a manner independent of active site thiols.","doi":"10.1128/EC.00106-08","authors":"Song JY, Kim KD, Roe JH","authors_abbrev":"Song JY et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-10-14","publication_year":"2008","canto_session_key":"7f9fcf3e0233cf42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-25 12:27:16","canto_approved_date":"2026-03-09 16:06:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-13 13:48:24","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.10","SPBC12D12.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-01-25"},{"uniquename":"PMID:9001235","title":"Severe growth defect in a Schizosaccharomyces pombe mutant defective in intron lariat degradation.","citation":"Mol Cell Biol 1997 Feb;17(2):809-18","abstract":"The cDNAs and genes encoding the intron lariat-debranching enzyme were isolated from the nematode Caenorhabditis elegans and the fission yeast Schizosaccharomyces pombe based on their homology with the Saccharomyces cerevisiae gene. The cDNAs were shown to be functional in an interspecific complementation experiment; they can complement an S. cerevisiae dbr1 null mutant. About 2.5% of budding yeast S. cerevisiae genes have introns, and the accumulation of excised introns in a dbr1 null mutant has little effect on cell growth. In contrast, many S. pombe genes contain introns, and often multiple introns per gene, so that S. pombe is estimated to contain approximately 40 times as many introns as S. cerevisiae. The S. pombe dbr1 gene was disrupted and shown to be nonessential. Like the S. cerevisiae mutant, the S. pombe null mutant accumulated introns to high levels, indicating that intron lariat debranching represents a rate-limiting step in intron degradation in both species. Unlike the S. cerevisiae mutant, the S. pombe dbr1::leu1+ mutant had a severe growth defect and exhibited an aberrant elongated cell shape in addition to an intron accumulation phenotype. The growth defect of the S. pombe dbr1::leu1+ strain suggests that debranching activity is critical for efficient intron RNA degradation and that blocking this pathway interferes with cell growth.","authors":"Nam K, Lee G, Trambley J, Devine SE, Boeke JD","authors_abbrev":"Nam K et al.","pubmed_publication_date":"Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_session_key":"df02b7e5271f29d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-02-17 14:02:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-14 16:05:38","canto_added_date":"2012-02-24 05:53:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.02c","SPAC3H5.07","SPAC664.06","SPSNRNA.06"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2013-02-14"},{"uniquename":"PMID:8557055","title":"Genetic analysis of an ARS element from the fission yeast Schizosaccharomyces pombe.","citation":"EMBO J 1995 Dec 15;14(24):6348-57","abstract":"ARS (autonomously replicating sequence) elements are DNA fragments that can function as origins of DNA replication in yeast. We report the first fine-structure analysis of ars1, an ARS element of the fission yeast Schizosaccharomyces pombe. Characterization of a series of nested deletion mutations indicated that the minimal fragment of DNA encompassing ars1 is surprisingly large. No fragment < 650 bp retained significant ARS activity. Analysis of deletion and substitution mutations scanning the entire minimal ars1 identified a single essential 50 bp fragment (segment 1). Only one other 50 bp mutation reduced activity as much as 5-fold and most deletions were without effect. Thus, the minimal ars1 is composed of two general types of genetic elements, a small segment that is absolutely required for efficient ARS activity and a much larger region that is tolerant of internal structural alterations. Higher resolution analysis of segment 1 defined a critical 30 bp A/T-rich segment which appears to contain redundant genetic elements. Schizosaccharomyces pombe ars1 promoted high frequency transformation in the budding yeast S.cerevisiae but this heterologous activity was not dependent on segment 1. Our analysis indicates that the functional elements required for ARS function in S.pombe and S.cerevisiae are clearly different.","authors":"Clyne RK, Kelly TJ","authors_abbrev":"Clyne RK et al.","pubmed_publication_date":"15 Dec 1995","pubmed_entrez_date":"1995-12-15","publication_year":"1995","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2906715","title":"Plasma membrane ATPase from the yeast Schizosaccharomyces pombe.","citation":"Methods Enzymol 1988;157:513-28","abstract":"","authors":"Dufour JP, Amory A, Goffeau A","authors_abbrev":"Dufour JP et al.","pubmed_publication_date":"1988","pubmed_entrez_date":"1988-01-01","publication_year":"1988","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009832","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35447271","title":"Heterologous expression of novel SUMO proteases from Schizosaccharomyces pombe in E. coli: Catalytic domain identification and optimization of product yields.","citation":"Int J Biol Macromol 2022 Jun 01;209(Pt A):1001-1019","abstract":"Small ubiquitin-related modifier (SUMO) proteins are efficiently used to target the soluble expression of various difficult-to-express proteins in E. coli. However, its utilization in large scale protein production is restricted by the higher cost of Ulp, which is required to cleave SUMO fusion tag from protein-of-interest to generate an authentic N-terminus. This study identified and characterized two novel SUMO proteases i.e., Ulp1 and Ulp2 from Schizosaccharomyces pombe. Codon-optimized gene sequences were cloned and expressed in E. coli. The sequence and structure of SpUlp1 and SpUlp2 catalytic domains were deduced using bioinformatics tools. Protein-protein interaction studies predicted the higher affinity of SpUlp1 towards SUMO compared to its counterpart from Saccharomyces cerevisiae (ScUlp1). The catalytic domain of SpUlp1 was purified using Ni-NTA chromatography with 83.33% recovery yield. Moreover, In vitro activity data further confirmed the fast-acting nature of SpUlp1 catalytic domain, where a 90% cleavage of fusion proteins was obtained within 1 h of incubation, indicating novelty and commercial relevance of S. pombe Ulp1. Biophysical characterization showed 8.8% α-helices, 36.7% β-sheets in SpUlp1SD. From thermal CD and fluorescence data, SpUlp1SD T m  was found to be 45 °C. Further, bioprocess optimization using fed-batch cultivation resulted in 3.5 g/L of SpUlp1SD production with Y P/X  of 77.26 mg/g DCW and volumetric productivity of 205.88 mg/L/h.","doi":"10.1016/j.ijbiomac.2022.04.078","authors":"Babbal, Mohanty S, Dabburu GR, Kumar M, Khasa YP","authors_abbrev":"Babbal et al.","pubmed_publication_date":"01 Jun 2022","pubmed_entrez_date":"2022-04-21","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-04-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41114153","title":"Cluster Based Association Measures with Applications.","citation":"Sankhya Ser B 2025 May 07;","abstract":"It is well recognized that relationships between variables are not always linear or even monotonic. For example, the expressions of cell-cycle, or circadian clock genes, or the abundance of microbes in a dynamic ecology are not expected to be linear. Furthermore, unknown to the researcher, there may be heterogeneous subgroups or clusters in the data. Researchers may be interested in discovering those clusters and derive an overall measure of association between variables of interest accounting for the different clusters as well as deriving associations within each cluster. Although standard concepts of correlations, such as the Pearson or Spearman, are widely used to describe overall associations, they can be misleading in such situations. As researchers continue to generate complex high dimensional data with hidden substructures or clusters, there is an urgent need for a measure that correctly quantifies associations between variables while agnostically accounting for hidden clusters in the data. Using clustering algorithms which are able to detect hidden clusters and association measures which are suitable for quantifying arbitrary relationships within each clusters, we develop a novel association procedure called CLuster based Association Measures (CLAM) to describe association between pairs of univariate as well as multivariate variables. The method is not limited to any specific form of association and is well-suited for heterogeneous data with hidden clusters, which are common in biomedical research. Performance of CLAM is evaluated using a synthetic data as well as real data from diverse applications, such as fission yeast (S. pombe) cell-cycle genes data, intestinal microbiome data from IBD patients, and three well-known imaging data sets, namely DrivFace data, Landsat data, and COIL data.","doi":"10.1007/s13571-025-00360-4","authors":"Bera S, Fouladi F, Peddada S","authors_abbrev":"Bera S et al.","pubmed_publication_date":"07 May 2025","pubmed_entrez_date":"2025-10-20","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-10-20 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15031652","title":"Accumulation and release of the osmolyte glycerol is independent of the putative MIP channel Spac977.17p in Schizosaccharomyces pombe.","citation":"Antonie Van Leeuwenhoek 2004 Feb;85(2):85-92","abstract":"Schizosaccharomyces pombe accumulates glycerol as an osmotic regulatory solute in response to hyper-osmotic conditions. Upon a decrease in the external osmolarity, the intracellular glycerol levels should be adjusted in order to attain osmotic homeostasis. In this study, the patterns and kinetics of glycerol export from S. pombe were investigated. Upon a decrease in external osmolarity, glycerol was rapidly exported from cells to the external medium. The amount of glycerol released from the cells was proportional to the degree of change in the external osmolarity. The export process was well controlled and was not affected by reduced temperature. This points to S. pombe controlling glycerol export using specialized facilitating proteins as has been found in Saccharomyces cerevisiae where a MIP family channel protein Fps1p is involved. Analysis of the S. pombe databases revealed a putative transport protein (Spac977.17p) with homology to glycerol channel proteins of the MIP family. However, expression of the gene into the S. cerevisiae strain lacking a glycerol channel protein (fps1Delta mutant), did not complement the defect in glycerol export during hypo-osmotic stress. Deletion of spac977.17, did not affect glycerol accumulation or release in S. pombe. The patterns and kinetics of glycerol release in the mutant were similar to those of the wild type strains suggesting that the export process is independent of Spac977.17p, the only putative MIP family glycerol channel homologue in S. pombe. While the process of glycerol export in response to hypo-osmotic stress is similar to budding yeast, the underlying molecular mechanism in S. pombe appears distinct from that described in S. cerevisiae. Further studies are needed to elucidate the physiological role of the Spac977.17p channel.","authors":"Kayingo G, Sirotkin V, Hohmann S, Prior BA","authors_abbrev":"Kayingo G et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2004-03-20","publication_year":"2004","canto_session_key":"c8ee2cf2f4fd55b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-09-28 13:17:09","canto_approved_date":"2025-09-28 13:17:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-09-01 17:53:15","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-09-28"},{"uniquename":"PMID:24666325","title":"Caffeine stabilizes Cdc25 independently of Rad3 in Schizosaccharomyces pombe contributing to checkpoint override.","citation":"Mol Microbiol 2014 May;92(4):777-96","abstract":"Cdc25 is required for Cdc2 dephosphorylation and is thus essential for cell cycle progression. Checkpoint activation requires dual inhibition of Cdc25 and Cdc2 in a Rad3-dependent manner. Caffeine is believed to override activation of the replication and DNA damage checkpoints by inhibiting Rad3-related proteins in both Schizosaccharomyces pombe and mammalian cells. In this study, we have investigated the impact of caffeine on Cdc25 stability, cell cycle progression and checkpoint override. Caffeine induced Cdc25 accumulation in S. pombe independently of Rad3. Caffeine delayed cell cycle progression under normal conditions but advanced mitosis in cells treated with replication inhibitors and DNA-damaging agents. In the absence of Cdc25, caffeine inhibited cell cycle progression even in the presence of hydroxyurea or phleomycin. Caffeine induces Cdc25 accumulation in S. pombe by suppressing its degradation independently of Rad3. The induction of Cdc25 accumulation was not associated with accelerated progression through mitosis, but rather with delayed progression through cytokinesis. Caffeine-induced Cdc25 accumulation appears to underlie its ability to override cell cycle checkpoints. The impact of Cdc25 accumulation on cell cycle progression is attenuated by Srk1 and Mad2. Together our findings suggest that caffeine overrides checkpoint enforcement by inducing the inappropriate nuclear localization of Cdc25.","doi":"10.1111/mmi.12592","authors":"Alao JP, Sjölander JJ, Baar J, Özbaki-Yagan N, Kakoschky B, Sunnerhagen P","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2014-03-27","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11599715","title":"Transformation systems of non-Saccharomyces yeasts.","citation":"Crit Rev Biotechnol 2001;21(3):177-218","abstract":"This review describes the transformation systems including vectors, replicons, genetic markers, transformation methods, vector stability, and copy numbers of 13 genera and 31 species of non-Saccharomyces yeasts. Schizosaccharomyces pombe was the first non-Saccharomyces yeast studied for transformation and genetics. The replicons of non-Saccharomyces yeast vectors are from native plasmids, chromosomal DNA, and mitochondrial DNA of Saccharomyces cerevisiae, non-Saccharomyces yeasts, protozoan, plant, and animal. Vectors such as YAC, YCp, YEp, YIp, and YRp were developed for non-Saccharomyces yeasts. Forty-two types of genes from bacteria, yeasts, fungi, and plant were used as genetic markers that could be classified into biosynthetic, dominant, and colored groups to construct non-Saccharomyces yeasts vectors. The LEU2 gene and G418 resistance gene are the two most popular markers used in the yeast transformation. All known transformation methods such as spheroplast-mediating method, alkaline ion treatment method, electroporation, trans-kingdom conjugation, and biolistics have been developed successfully for non-Saccharomyces yeasts, among which the first three are most widely used. The highest copy number detected from non-Saccharomyces yeasts is 60 copies in Kluyveromyces lactis. No general rule is known to illustrate the transformation efficiency, vector stability, and copy number, although factors such as vector composition, host strain, transformation method, and selective pressure might influence them.","authors":"Wang TT, Choi YJ, Lee BH","authors_abbrev":"Wang TT et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-10-16","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11717425","title":"The Schizosaccharomyces pombe origin recognition complex interacts with multiple AT-rich regions of the replication origin DNA by means of the AT-hook domains of the spOrc4 protein.","citation":"Proc Natl Acad Sci U S A 2001 Nov 20;98(24):13589-94","abstract":"The interaction between an origin sequence and the origin recognition complex (ORC), which is highly conserved in eukaryotes, is critical for the initiation of DNA replication. In this report, we have examined the interaction between the Schizosaccharomyces pombe (sp) autonomously replicating sequence 1 (ars1) and the spORC. For this purpose, we have purified the spORC containing all six subunits, a six-subunit complex containing the N-terminal-deleted spOrc4 subunit (spORC(Delta N-Orc4)), and the spOrc4 subunit by using the baculovirus expression system. Wild-type spORC showed sequence-specific binding to ars1, and the spOrc4 protein alone showed the same DNA-binding properties as wild-type spORC. In contrast, the spORC(Delta N-Orc4) and the Delta N-spOrc4p alone did not bind significantly to ars1. These findings indicate that the N-terminal domain of the spOrc4 protein that contains multiple AT-hook motifs is essential for the ars1-binding activity. DNA-binding competition assays with fragments of ars1 and DNase I footprinting studies with full-length ars1 revealed that the spORC interacted with several AT-rich sequence regions of ars1. These DNA-binding properties of spORC correlate with the previously determined sequence requirements of the S. pombe ars1. These studies indicate that because of its unique Orc4 subunit, S. pombe uses a mechanism to recognize its origins different from that used by Saccharomyces cerevisiae.","authors":"Lee JK, Moon KY, Jiang Y, Hurwitz J","authors_abbrev":"Lee JK et al.","pubmed_publication_date":"20 Nov 2001","pubmed_entrez_date":"2001-11-22","publication_year":"2001","canto_session_key":"24cc84e2bcc157d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2013-12-20 17:32:49","canto_approved_date":"2022-02-24 11:57:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-20 17:20:20","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2A9.12","SPBC29A10.15","SPBP23A10.13","SPBC646.14c","SPAC3H1.01c","SPBC685.09"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2013-12-20"},{"uniquename":"PMID:1617727","title":"Mutations at the 3' splice site can be suppressed by compensatory base changes in U1 snRNA in fission yeast.","citation":"Cell 1992 Jun 26;69(7):1159-69","abstract":"U1 snRNA is an essential splicing factor known to base pair with 5' splice sites of premessenger RNAs. We demonstrate that pairing between the universally conserved CU just downstream from the 5' junction interaction region and the 3' splice site AG contributes to efficient splicing of Schizosaccharomyces pombe introns that typify the AG-dependent class described in mammals. Strains carrying mutations in the 3' AG of an artificial intron accumulate linear precursor, indicative of a first step block. Lariat formation is partially restored in these mutants by compensatory changes in nucleotides C7 and U8 of U1 snRNA. Consistent with a general role in fission yeast splicing, mutations at C7 are lethal, while U8 mutants are growth impaired and accumulate linear, unspliced precursor to U6 snRNA. U1 RNA-mediated recognition of the 3' splice site may have origins in analogous intramolecular interactions in an ancestral self-splicing RNA.","authors":"Reich CI, VanHoy RW, Porter GL, Wise JA","authors_abbrev":"Reich CI et al.","pubmed_publication_date":"26 Jun 1992","pubmed_entrez_date":"1992-06-26","publication_year":"1992","canto_session_key":"7fb114bb93891bd9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-02-24 18:42:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-27 12:20:18","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-27"},{"uniquename":"PMID:7916653","title":"Sct1 functions in partnership with Cdc10 in a transcription complex that activates cell cycle START and inhibits differentiation.","citation":"Cell 1993 Feb 26;72(4):607-19","abstract":"A fission yeast cell cycle START gene has been identified, sct1. Loss of sct1 function results in cell cycle arrest at START and simultaneously in derepression of the mating pathway. sct1 therefore functions both as an essential activator of the mitotic cell cycle and as a repressor of differentiation. p72sct1 shares 36% sequence similarity with p85cdc10. p72sct1 is shown to act in partnership with p85cdc10 in a cell cycle regulatory transcription complex. A single dominant mutation within the putative DNA-binding domain of p72sct1 renders the cell independent of cdc10 function for the execution of START.","authors":"Caligiuri M, Beach D","authors_abbrev":"Caligiuri M et al.","pubmed_publication_date":"26 Feb 1993","pubmed_entrez_date":"1993-02-26","publication_year":"1993","canto_session_key":"69615b5c56b7a12f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-05 10:54:25","canto_approved_date":"2023-09-11 10:23:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-09 18:00:01","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC725.16"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-09-05"},{"uniquename":"PMID:30756233","title":"Comparison of Deterministic and Stochastic Regime in a Model for Cdc42 Oscillations in Fission Yeast.","citation":"Bull Math Biol 2019 May;81(5):1268-1302","abstract":"Oscillations occur in a wide variety of essential cellular processes, such as cell cycle progression, circadian clocks and calcium signaling in response to stimuli. It remains unclear how intrinsic stochasticity can influence these oscillatory systems. Here, we focus on oscillations of Cdc42 GTPase in fission yeast. We extend our previous deterministic model by Xu and Jilkine to construct a stochastic model, focusing on the fast diffusion case. We use SSA (Gillespie's algorithm) to numerically explore the low copy number regime in this model, and use analytical techniques to study the long-time behavior of the stochastic model and compare it to the equilibria of its deterministic counterpart. Numerical solutions suggest noisy limit cycles exist in the parameter regime in which the deterministic system converges to a stable limit cycle, and quasi-cycles exist in the parameter regime where the deterministic model has a damped oscillation. Near an infinite period bifurcation point, the deterministic model has a sustained oscillation, while stochastic trajectories start with an oscillatory mode and tend to approach deterministic steady states. In the low copy number regime, metastable transitions from oscillatory to steady behavior occur in the stochastic model. Our work contributes to the understanding of how stochastic chemical kinetics can affect a finite-dimensional dynamical system, and destabilize a deterministic steady state leading to oscillations.","doi":"10.1007/s11538-019-00573-5","authors":"Xu B, Kang HW, Jilkine A","authors_abbrev":"Xu B et al.","pubmed_publication_date":"May 2019","pubmed_entrez_date":"2019-02-14","publication_year":"2019","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2019-02-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25501816","title":"Analysis of S. pombe SIN protein association to the SPB reveals two genetically separable states of the SIN.","citation":"J Cell Sci 2015 Feb 15;128(4):741-54","abstract":"The Schizosaccharomyces pombe septation initiation network (SIN) regulates cytokinesis, and asymmetric association of SIN proteins with the mitotic spindle pole bodies (SPBs) is important for its regulation. Here, we have used semi-automated image analysis to study SIN proteins in large numbers of wild-type and mutant cells. Our principal conclusions are: first, that the association of Cdc7p with the SPBs in early mitosis is frequently asymmetric, with a bias in favour of the new SPB; second, that the early association of Cdc7p-GFP to the SPB depends on Plo1p but not Spg1p, and is unaffected by mutations that influence its asymmetry in anaphase; third, that Cdc7p asymmetry in anaphase B is delayed by Pom1p and by activation of the spindle assembly checkpoint, and is promoted by Rad24p; and fourth, that the length of the spindle, expressed as a fraction of the length of the cell, at which Cdc7p becomes asymmetric is similar in cells dividing at different sizes. These data reveal that multiple regulatory mechanisms control the SIN in mitosis and lead us to propose a two-state model to describe the SIN.","doi":"10.1242/jcs.160150","authors":"Wachowicz P, Chasapi A, Krapp A, Cano Del Rosario E, Schmitter D, Sage D, Unser M, Xenarios I, Rougemont J, Simanis V","authors_abbrev":"Wachowicz P et al.","pubmed_publication_date":"15 Feb 2015","pubmed_entrez_date":"2014-12-16","publication_year":"2015","canto_session_key":"633e0de153a1fdcf","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-12-18 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5958447","title":"Synthesis of enzymes and DNA in synchronous cultures of Schizosaccharomyces pombe.","citation":"Nature 1966 May 21;210(5038):808-10","abstract":"","authors":"Bostock CJ, Donachie WD, Masters M, Mitchison JM","authors_abbrev":"Bostock CJ et al.","pubmed_publication_date":"21 May 1966","pubmed_entrez_date":"1966-05-21","publication_year":"1966","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34608864","title":"DDK/Hsk1 phosphorylates and targets fission yeast histone deacetylase Hst4 for degradation to stabilize stalled DNA replication forks.","citation":"Elife 2021 Oct 05;10","abstract":"In eukaryotes, paused replication forks are prone to collapse, which leads to genomic instability, a hallmark of cancer. Dbf4-dependent kinase (DDK)/Hsk1 Cdc7  is a conserved replication initiator kinase with conflicting roles in replication stress response. Here, we show that fission yeast DDK/Hsk1 phosphorylates sirtuin, Hst4 upon replication stress at C-terminal serine residues. Phosphorylation of Hst4 by DDK marks it for degradation via the ubiquitin ligase SCF pof3 . Phosphorylation-defective  hst4  mutant ( 4SA-hst4 ) displays defective recovery from replication stress, faulty fork restart, slow S-phase progression and decreased viability. The highly conserved fork protection complex (FPC) stabilizes stalled replication forks. We found that the recruitment of FPC components, Swi1 and Mcl1 to the chromatin is compromised in the  4SA-hst4  mutant, although whole cell levels increased. These defects are dependent upon H3K56ac and independent of intra S-phase checkpoint activation. Finally, we show conservation of H3K56ac-dependent regulation of Timeless, Tipin, and And-1 in human cells. We propose that degradation of Hst4 via DDK increases H3K56ac, changing the chromatin state in the vicinity of stalled forks facilitating recruitment and function of FPC. Overall, this study identified a crucial role of DDK and FPC in the regulation of replication stress response with implications in cancer therapeutics.","doi":"10.7554/eLife.70787","authors":"Aricthota S, Haldar D","authors_abbrev":"Aricthota S et al.","pubmed_publication_date":"05 Oct 2021","pubmed_entrez_date":"2021-10-05","publication_year":"2021","canto_session_key":"e183fe7f2ecde817","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-11-05 12:20:36","canto_approved_date":"2021-11-05 12:20:36","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-11-05 12:20:28","canto_added_date":"2021-10-07 00:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":71,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.04c","SPCC16A11.17","SPBC776.12c","SPBC409.05","SPCC550.13","SPCC18B5.11c","SPAPB1E7.02c","SPBC30D10.04","SPBC8D2.04","SPBC1718.01","SPBC4.07c","SPAC694.06c","SPBC216.06c","SPCC338.16","SPAC1687.15"],"gene_count":15,"ltp_gene_count":12,"approved_date":"2021-11-05"},{"uniquename":"PMID:35357307","title":"Dedicated chaperones coordinate co-translational regulation of ribosomal protein production with ribosome assembly to preserve proteostasis.","citation":"Elife 2022 Mar 31;11","abstract":"The biogenesis of eukaryotic ribosomes involves the ordered assembly of around 80 ribosomal proteins. Supplying equimolar amounts of assembly-competent ribosomal proteins is complicated by their aggregation propensity and the spatial separation of their location of synthesis and pre-ribosome incorporation. Recent evidence has highlighted that dedicated chaperones protect individual, unassembled ribosomal proteins on their path to the pre-ribosomal assembly site. Here, we show that the co-translational recognition of Rpl3 and Rpl4 by their respective dedicated chaperone, Rrb1 or Acl4, reduces the degradation of the encoding  RPL3  and  RPL4  mRNAs in the yeast  Saccharomyces cerevisiae . In both cases, negative regulation of mRNA levels occurs when the availability of the dedicated chaperone is limited and the nascent ribosomal protein is instead accessible to a regulatory machinery consisting of the nascent-polypeptide-associated complex and the Caf130-associated Ccr4-Not complex. Notably, deregulated expression of Rpl3 and Rpl4 leads to their massive aggregation and a perturbation of overall proteostasis in cells lacking the E3 ubiquitin ligase Tom1. Taken together, we have uncovered an unprecedented regulatory mechanism that adjusts the de novo synthesis of Rpl3 and Rpl4 to their actual consumption during ribosome assembly and, thereby, protects cells from the potentially detrimental effects of their surplus production.","doi":"10.7554/eLife.74255","authors":"Pillet B, Méndez-Godoy A, Murat G, Favre S, Stumpe M, Falquet L, Kressler D","authors_abbrev":"Pillet B et al.","pubmed_publication_date":"31 Mar 2022","pubmed_entrez_date":"2022-03-31","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP8B7.03c","SPAPB8E5.06c","SPAC17A5.03","SPBC1711.07","SPBC1711.06","SPBC16D10.01c"],"gene_count":6,"ltp_gene_count":0},{"uniquename":"PMID:27532772","title":"Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins.","citation":"Elife 2016 Aug 17;5","abstract":"Assembly of mitochondrial iron-sulfur (Fe/S) proteins is a key process of cells, and defects cause many rare diseases. In the first phase of this pathway, ten Fe/S cluster (ISC) assembly components synthesize and insert [2Fe-2S] clusters. The second phase is dedicated to the assembly of [4Fe-4S] proteins, yet this part is poorly understood. Here, we characterize the BOLA family proteins Bol1 and Bol3 as specific mitochondrial ISC assembly factors that facilitate [4Fe-4S] cluster insertion into a subset of mitochondrial proteins such as lipoate synthase and succinate dehydrogenase. Bol1-Bol3 perform largely overlapping functions, yet cannot replace the ISC protein Nfu1 that also participates in this phase of Fe/S protein biogenesis. Bol1 and Bol3 form dimeric complexes with both monothiol glutaredoxin Grx5 and Nfu1. Complex formation differentially influences the stability of the Grx5-Bol-shared Fe/S clusters. Our findings provide the biochemical basis for explaining the pathological phenotypes of patients with mutations in BOLA3.","doi":"10.7554/eLife.16673","authors":"Uzarska MA, Nasta V, Weiler BD, Spantgar F, Ciofi-Baffoni S, Saviello MR, Gonnelli L, Mühlenhoff U, Banci L, Lill R","authors_abbrev":"Uzarska MA et al.","pubmed_publication_date":"17 Aug 2016","pubmed_entrez_date":"2016-08-18","publication_year":"2016","canto_session_key":"7d1ac1b70b5fac83","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-09-02 10:16:46","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-08-20 14:47:54","canto_added_date":"2016-08-20 13:29:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB2B4.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-08-20"},{"uniquename":"PMID:42074057","title":"Mixing Is Dispensable for Optical Density-Based High-Throughput Growth Screening Assay in Fission Yeast.","citation":"Int J Mol Sci 2026 Apr 10;27(8)","abstract":"Optical density (OD)-based cell growth measurement is commonly used in high-throughput screening (HTS) during drug discovery or when deciphering the pharmaceutical mechanism of action. While resuspending the cells via a mixing step is often assumed to be necessary prior to OD measurement, its essentiality in HTS workflows has not been systematically verified. Here, through the measurement of the growth of several strains of the microbial yeast  Schizosaccharomyces pombe  cells, we compared the overall growth dynamics between samples that have been mixed and not mixed. Using statistical quantification by a two-tailed paired  t -test followed by multiple comparison corrections, we concluded from the comparison of the doubling time of cells growing in the exponential phase that mixing did not significantly affect the biological interpretation compared to unmixed samples. Doubling time quantification between mixed and unmixed samples showed a difference of approximately 10% on average based on the assessment of the growth of eight strains. As such, if the experimental outcome can accommodate this level of variability, incorporating a mixing step before OD determination would not be necessary. These observations support the simplification of HTS processes, improving the cost efficacy and process efficiency of readouts, yet maintaining the accuracy of data acquisition.","doi":"10.3390/ijms27083410","authors":"Lim KK, Chung JJ, Ma S, Yen CC, Zhang L, Chen ES","authors_abbrev":"Lim KK et al.","pubmed_publication_date":"10 Apr 2026","pubmed_entrez_date":"2026-05-04","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-05-04 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36758804","title":"Multifaceted functions of RNA-binding protein vigilin in gene silencing, genome stability, and autism-related disorders.","citation":"J Biol Chem 2023 Mar;299(3):102988","abstract":"RNA-binding proteins (RBPs) are emerging as important players in regulating eukaryotic gene expression and genome stability. Specific RBPs have been shown to mediate various chromatin-associated processes ranging from transcription to gene silencing and DNA repair. One of the prominent classes of RBPs is the KH domain-containing proteins. Vigilin, an evolutionarily conserved KH domain-containing RBP has been shown to be associated with diverse biological processes like RNA transport and metabolism, sterol metabolism, chromosome segregation, and carcinogenesis. We have previously reported that vigilin is essential for heterochromatin-mediated gene silencing in fission yeast. More recently, we have identified that vigilin in humans plays a critical role in efficient repair of DNA double-stranded breaks and functions in homology-directed DNA repair. In this review, we highlight the multifaceted functions of vigilin and discuss the findings in the context of gene expression, genome organization, cancer, and autism-related disorders.","doi":"10.1016/j.jbc.2023.102988","authors":"Mushtaq A, Mir US, Altaf M","authors_abbrev":"Mushtaq A et al.","pubmed_publication_date":"Mar 2023","pubmed_entrez_date":"2023-02-09","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-02-11 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12172965","title":"Identifying regulators of pheromone signalling in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 2002 Jul;41(4):241-53","abstract":"The rate and extent of a cell's response to an extracellular stimulus is influenced by regulators that act on the intracellular signalling machinery. Although not directly involved in propagating the intracellular signal, regulators control the activity of the proteins that transmit the signals. To understand this aspect of cell signalling, we studied the pheromone-response pathway in the fission yeast Schizosaccharomyces pombe, a relatively simple signalling system in a genetically tractable organism. Here, we describe the development of yeast strains containing ura4 and lacZ reporter genes under the control of the pheromone-regulated sxa2 promoter and the use of these strains to isolate mutants defective in their ability to regulate signalling. Several different types of mutant were identified. Some mutants were defective in proteins already known to regulate the pheromone-signalling pathway (Rgs1, Map1, Map2). Our approach also identified the MAP kinase phosphatase Pmp1 as a regulator of the pheromone-response pathway. Although previously shown to regulate other MAP kinase pathways in Sz. pombe, this is the first demonstration of a role for Pmp1 in pheromone signalling.","authors":"Didmon M, Davis K, Watson P, Ladds G, Broad P, Davey J","authors_abbrev":"Didmon M et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-08-13","publication_year":"2002","canto_session_key":"3d8e1af5e6b75514","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-20 09:07:22","canto_approved_date":"2020-12-03 17:39:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-02-16 17:08:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.05c","SPAC11E3.06","SPBC1685.01","SPAC22F3.12c","SPCC1795.06","SPAC26F1.10c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2017-07-20"},{"uniquename":"EMBL:AB084823","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10692375","title":"Role of cell shape in determination of the division plane in Schizosaccharomyces pombe: random orientation of septa in spherical cells.","citation":"J Bacteriol 2000 Mar;182(6):1693-701","abstract":"The establishment of growth polarity in Schizosaccharomyces pombe cells is a combined function of the cytoplasmic cytoskeleton and the shape of the cell wall inherited from the mother cell. The septum that divides the cylindrical cell into two siblings is formed midway between the growing poles and perpendicularly to the axis that connects them. Since the daughter cells also extend at their ends and form their septa at right angles to the longitudinal axis, their septal (division) planes lie parallel to those of the mother cell. To gain a better understanding of how this regularity is ensured, we investigated septation in spherical cells that do not inherit morphologically predetermined cell ends to establish poles for growth. We studied four mutants (defining four novel genes), over 95% of whose cells displayed a completely spherical morphology and a deficiency in mating and showed a random distribution of cytoplasmic microtubules, Tea1p, and F-actin, indicating that the cytoplasmic cytoskeleton was poorly polarized or apolar. Septum positioning was examined by visualizing septa and division scars by calcofluor staining and by the analysis of electron microscopic images. Freeze-substitution, freeze-etching, and scanning electron microscopy were used. We found that the elongated bipolar shape is not essential for the determination of a division plane that can separate the postmitotic nuclei. However, it seems to be necessary for the maintenance of the parallel orientation of septa over the generations. In the spherical cells, the division scars and septa usually lie at angles to each other on the cell surface. We hypothesize that the shape of the cell indirectly affects the positioning of the septum by directing the extension of the spindle.","authors":"Sipiczki M, Yamaguchi M, Grallert A, Takeo K, Zilahi E, Bozsik A, Miklos I","authors_abbrev":"Sipiczki M et al.","pubmed_publication_date":"Mar 2000","pubmed_entrez_date":"2000-02-29","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11104907","title":"Characterization of RAD52 homologs in the fission yeast Schizosaccharomyces pombe.","citation":"Mutat Res 2001 Jan 05;461(4):311-23","abstract":"The RAD52 gene of Saccharomyces cerevisiae is essential for repair of DNA double-strand breaks (DSBs) by homologous recombination. Inactivation of this gene confers hypersensitivity to DSB-inducing agents and defects in most forms of recombination. The rad22+ gene in Schizosaccharomyces pombe (here referred to as rad22A+) has been characterized as a homolog of RAD52 in fission yeast. Here, we report the identification of a second RAD52 homolog in Schizosaccharomyces pombe, called rad22B+. The amino acid sequences of Rad22A and Rad22B show significant conservation (38% identity). Deletion mutants of respectively, rad22A and rad22B, show different phenotypes with respect to sensitivity to X-rays and the ability to perform homologous recombination as measured by the integration of plasmid DNA. Inactivation of rad22A+ leads to a severe sensitivity to X-rays and a strong decrease in recombination (13-fold), while the rad22B mutation does not result in a decrease in homologous recombination or a change in radiation sensitivity. In a rad22A-rad22B double mutant the radiation sensitivity is further enhanced in comparison with the rad22A single mutant. Overexpression of the rad22B+ gene results in partial suppression of the DNA repair defects of the rad22A mutant strain. Meiotic recombination and spore viability are only slightly affected in either single mutant, but outgrowth of viable spores is almost 31-fold reduced in the rad22A-rad22B double mutant. The results obtained imply a crucial role for rad22A+ in repair and recombination in vegetative cells just like RAD52 in S. cerevisiae. The rad22B+ gene presumably has an auxiliary role in the repair of DSBs. The drastic reduced spore viability in the double mutant suggests that meiosis in S. pombe is dependent on the presence of either rad22A+ or rad22B+.","authors":"van den Bosch M, Vreeken K, Zonneveld JB, Brandsma JA, Lombaerts M, Murray JM, Lohman PH, Pastink A","authors_abbrev":"van den Bosch M et al.","pubmed_publication_date":"05 Jan 2001","pubmed_entrez_date":"2000-12-06","publication_year":"2001","canto_session_key":"c5b8ec8554d221e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-22 15:33:26","canto_approved_date":"2022-09-23 16:57:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-22 15:33:19","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPBC119.14","SPAC644.14c","SPCC1322.13"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2014-10-22"},{"uniquename":"PMID:26609955","title":"Keeping Order in Anaphase.","citation":"Dev Cell 2015 Nov 23;35(4):403-4","abstract":"The critical components of chromosome segregation machinery are well established, but how they orchestrate the relative order of events during mitosis remains unclear. Kamenz et al. (2015) now report in Molecular Cell quantitative data suggesting competing networks and adaptive thresholds in the control of mitotic exit by the anaphase-promoting complex.","doi":"10.1016/j.devcel.2015.11.011","authors":"Malumbres M","authors_abbrev":"Malumbres M","pubmed_publication_date":"23 Nov 2015","pubmed_entrez_date":"2015-11-27","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-03-06 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17173028","title":"Slicer and the argonautes.","citation":"Nat Chem Biol 2007 Jan;3(1):36-43","abstract":"Though they started out as somewhat mysterious components of the RNAi effector complexes, Argonaute proteins have since taken center stage in RNAi gene silencing. They interact with small RNAs to effect gene silencing in all RNAi-related pathways known so far. We will review the dramatic advances in our understanding of the role of the Argonautes in RNAi through studies of their structure and function.","authors":"Tolia NH, Joshua-Tor L","authors_abbrev":"Tolia NH et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2006-12-19","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31635174","title":"Nuclear Mechanics in the Fission Yeast.","citation":"Cells 2019 Oct 20;8(10)","abstract":"In eukaryotic cells, the organization of the genome within the nucleus requires the nuclear envelope (NE) and its associated proteins. The nucleus is subjected to mechanical forces produced by the cytoskeleton. The physical properties of the NE and the linkage of chromatin in compacted conformation at sites of cytoskeleton contacts seem to be key for withstanding nuclear mechanical stress. Mechanical perturbations of the nucleus normally occur during nuclear positioning and migration. In addition, cell contraction or expansion occurring for instance during cell migration or upon changes in osmotic conditions also result innuclear mechanical stress. Recent studies in  Schizosaccharomyces pombe  (fission yeast) have revealed unexpected functions of cytoplasmic microtubules in nuclear architecture and chromosome behavior, and have pointed to NE-chromatin tethers as protective elements during nuclear mechanics. Here, we review and discuss how fission yeast cells can be used to understand principles underlying the dynamic interplay between genome organization and function and the effect of forces applied to the nucleus by the microtubule cytoskeleton.","doi":"10.3390/cells8101285","authors":"Gallardo P, Barrales RR, Daga RR, Salas-Pino S","authors_abbrev":"Gallardo P et al.","pubmed_publication_date":"20 Oct 2019","pubmed_entrez_date":"2019-10-23","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-10-24 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20622014","title":"Negative regulation of meiotic gene expression by the nuclear poly(a)-binding protein in fission yeast.","citation":"J Biol Chem 2010 Sep 03;285(36):27859-68","abstract":"Meiosis is a cellular differentiation process in which hundreds of genes are temporally induced. Because the expression of meiotic genes during mitosis is detrimental to proliferation, meiotic genes must be negatively regulated in the mitotic cell cycle. Yet, little is known about mechanisms used by mitotic cells to repress meiosis-specific genes. Here we show that the poly(A)-binding protein Pab2, the fission yeast homolog of mammalian PABPN1, controls the expression of several meiotic transcripts during mitotic division. Our results from chromatin immunoprecipitation and promoter-swapping experiments indicate that Pab2 controls meiotic genes post-transcriptionally. Consistently, we show that the nuclear exosome complex cooperates with Pab2 in the negative regulation of meiotic genes. We also found that Pab2 plays a role in the RNA decay pathway orchestrated by Mmi1, a previously described factor that functions in the post-transcriptional elimination of meiotic transcripts. Our results support a model in which Mmi1 selectively targets meiotic transcripts for degradation via Pab2 and the exosome. Our findings have therefore uncovered a mode of gene regulation whereby a poly(A)-binding protein promotes RNA degradation in the nucleus to prevent untimely expression.","doi":"10.1074/jbc.M110.150748","authors":"St-André O, Lemieux C, Perreault A, Lackner DH, Bähler J, Bachand F","authors_abbrev":"St-André O et al.","pubmed_publication_date":"03 Sep 2010","pubmed_entrez_date":"2010-07-13","publication_year":"2010","canto_session_key":"1f45b30d29eccb96","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-11-13 15:42:06","canto_approved_date":"2024-02-11 09:56:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-13 15:41:59","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":62,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC12G12.13c","SPAC1556.06","SPAC27D7.13c","SPAP8A3.05","SPBC16E9.12c","SPAC25G10.04c","SPNCRNA.103","SPAC27D7.03c","SPCC1223.12c","SPBC29A10.02","SPCC736.12c","SPBC28F2.12","SPAC14C4.03","SPBC26H8.10","SPAC1F3.01"],"gene_count":15,"ltp_gene_count":8,"approved_date":"2020-11-13"},{"uniquename":"PMID:28493118","title":"Position matters: multiple functions of LINC-dependent chromosome positioning during meiosis.","citation":"Curr Genet 2017 Dec;63(6):1037-1052","abstract":"Chromosome positioning is crucial for multiple chromosomal events, including DNA replication, repair, and recombination. The linker of nucleoskeleton and cytoskeleton (LINC) complexes, which consist of conserved nuclear membrane proteins, were shown to control chromosome positioning and facilitate various biological processes by interacting with the cytoskeleton. However, the precise functions and regulation of LINC-dependent chromosome positioning are not fully understood. During meiosis, the LINC complexes induce clustering of telomeres, forming the bouquet chromosome arrangement, which promotes homologous chromosome pairing. In fission yeast, the bouquet forms through LINC-dependent clustering of telomeres at the spindle pole body (SPB, the centrosome equivalent in fungi) and detachment of centromeres from the SPB-localized LINC. It was recently found that, in fission yeast, the bouquet contributes to formation of the spindle and meiotic centromeres, in addition to homologous chromosome pairing, and that centromere detachment is linked to telomere clustering, which is crucial for proper spindle formation. Here, we summarize these findings and show that the bouquet chromosome arrangement also contributes to nuclear fusion during karyogamy. The available evidence suggests that these functions are universal among eukaryotes. The findings demonstrate that LINC-dependent chromosome positioning performs multiple functions and controls non-chromosomal as well as chromosomal events, and that the chromosome positioning is stringently regulated for its functions. Thus, chromosome positioning plays a much broader role and is more strictly regulated than previously thought.","doi":"10.1007/s00294-017-0699-2","authors":"Katsumata K, Nishi E, Afrin S, Narusawa K, Yamamoto A","authors_abbrev":"Katsumata K et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-05-12","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-05-13 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPRUM1","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18676809","title":"Structural and functional analysis of the Crb2-BRCT2 domain reveals distinct roles in checkpoint signaling and DNA damage repair.","citation":"Genes Dev 2008 Aug 01;22(15):2034-47","abstract":"Schizosaccharomyces pombe Crb2 is a checkpoint mediator required for the cellular response to DNA damage. Like human 53BP1 and Saccharomyces cerevisiae Rad9 it contains Tudor(2) and BRCT(2) domains. Crb2-Tudor(2) domain interacts with methylated H4K20 and is required for recruitment to DNA dsDNA breaks. The BRCT(2) domain is required for dimerization, but its precise role in DNA damage repair and checkpoint signaling is unclear. The crystal structure of the Crb2-BRCT(2) domain, alone and in complex with a phosphorylated H2A.1 peptide, reveals the structural basis for dimerization and direct interaction with gamma-H2A.1 in ionizing radiation-induced foci (IRIF). Mutational analysis in vitro confirms the functional role of key residues and allows the generation of mutants in which dimerization and phosphopeptide binding are separately disrupted. Phenotypic analysis of these in vivo reveals distinct roles in the DNA damage response. Dimerization mutants are genotoxin sensitive and defective in checkpoint signaling, Chk1 phosphorylation, and Crb2 IRIF formation, while phosphopeptide-binding mutants are only slightly sensitive to IR, have extended checkpoint delays, phosphorylate Chk1, and form Crb2 IRIF. However, disrupting phosphopeptide binding slows formation of ssDNA-binding protein (Rpa1/Rad11) foci and reduces levels of Rad22(Rad52) recombination foci, indicating a DNA repair defect.","doi":"10.1101/gad.472808","authors":"Kilkenny ML, Doré AS, Roe SM, Nestoras K, Ho JC, Watts FZ, Pearl LH","authors_abbrev":"Kilkenny ML et al.","pubmed_publication_date":"01 Aug 2008","pubmed_entrez_date":"2008-08-05","publication_year":"2008","canto_session_key":"914a897d725c3b1c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-16 19:10:13","canto_approved_date":"2023-02-16 19:10:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-15 11:27:58","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.08c","SPBC342.05","SPAC19G12.06c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2023-02-16","pdb_entries":[{"pdb_id":"2vxc","gene_chains":[{"gene_uniquename":"SPBC342.05","chain":"A/B","position":"537-778"}],"title":"Structure of the Crb2-BRCT2 domain complex with phosphopeptide.","entry_authors":"Kilkenny ML,Roe SM,Pearl LH","entry_authors_abbrev":"Kilkenny ML et al.","reference_uniquename":"PMID:18676809","experimental_method":"X-ray","resolution":"3.1"},{"pdb_id":"2vxb","gene_chains":[{"gene_uniquename":"SPBC342.05","chain":"A/B","position":"538-778"}],"title":"Structure of the Crb2-BRCT2 domain","entry_authors":"Kilkenny ML,Roe SM,Pearl LH","entry_authors_abbrev":"Kilkenny ML et al.","reference_uniquename":"PMID:18676809","experimental_method":"X-ray","resolution":"2.3"}]},{"uniquename":"PMID:12163175","title":"PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance.","citation":"FEBS Lett 2002 Aug 14;525(1-3):131-4","abstract":"In Saccharomyces cerevisiae, the overexpression of ROD1 confers resistance to o-dinitrobenzene (o-DNB), a representative of target drugs of glutathione S-transferase. The roles of Rod1 in drug resistance have remained to be determined. We isolated the rog3 mutation as a suppressor mutation of the temperature sensitivity of the strain, in that two of the total four glycogen synthase kinase 3 homologs were deleted. Rog3 is homologous to Rod1, and its overexpression also conferred resistance to o-DNB. Furthermore, these two proteins have PY-motifs, and bound to Rsp5, a hect-type ubiquitin ligase. The rsp5-101 mutant showed sensitivity to o-DNB as did the rod1 mutant, a mutant Rod1 containing altered PY motifs was defective in ability to bind to Rsp5 and in conferring o-DNB resistance. These results suggest that interaction of Rod1 and Rsp5 is important for drug resistance.","authors":"Andoh T, Hirata Y, Kikuchi A","authors_abbrev":"Andoh T et al.","pubmed_publication_date":"14 Aug 2002","pubmed_entrez_date":"2002-08-07","publication_year":"2002","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC584.15c","SPAC31A2.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8305731","title":"p63cdc13, a B-type cyclin, is associated with both the nucleolar and chromatin domains of the fission yeast nucleus.","citation":"Mol Biol Cell 1993 Nov;4(11):1087-96","abstract":"The cellular distribution of the fission yeast mitotic cyclin B, p63cdc13, was investigated by a combination of indirect immunofluorescence light microscopy, immunogold electron microscopy, and nuclear isolation and fractionation. Immunofluorescence microscopy of wild-type cells and the cold-sensitive mutant dis2.11 with a monospecific anti-p63cdc13 antiserum was consistent with the association of a major subpopulation of fission yeast M-phase protein kinase with the nucleolus. Immunogold electron microscopy of freeze-substituted wild-type cells identified two nuclear populations of p63cdc13, one associated with the nucleolus, the other with the chromatin domain. To investigate the cell cycle regulation of nuclear labeling, the mutant cdc25.22 was synchronized through mitosis by temperature arrest and release. Immunogold labeling of cells arrested at G2M revealed gold particles present abundantly over the nucleolus and less densely over the chromatin region of the nucleus. Small vesicles around the nucleus were also labeled by anti-p63cdc13, but few gold particles were detected over the cytoplasm. Labeling of all cell compartments declined to zero through mitosis. Cell fractionation confirmed that p63cdc13 was substantially enriched in both isolated nuclei and in a fraction containing small vesicles and organelles. p63cdc13 was not extracted from nuclei by treatment with RNase A, Nonidet P40 (NP-40), Triton X-100, and 0.1 M NaCl, although partial solubilization was observed with DNase I and 1 M NaCl. A known nucleolar protein NOP1, partitioned in a similar manner to p63cdc13, as did p34cdc2, the other subunit of the M-phase protein kinase. We conclude that a major subpopulation of the fission yeast mitotic cyclin B is targeted to structural elements of the nucleus and nucleolus.","authors":"Gallagher IM, Alfa CE, Hyams JS","authors_abbrev":"Gallagher IM et al.","pubmed_publication_date":"Nov 1993","pubmed_entrez_date":"1993-11-01","publication_year":"1993","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15620689","title":"Glyceraldehyde-3-phosphate dehydrogenase and actin associate with RNA polymerase II and interact with its Rpb7 subunit.","citation":"FEBS Lett 2005 Jan 03;579(1):48-52","abstract":"RNA polymerase II (pol II) purified from the fission yeast Schizosaccharomyces pombe was previously reported to be associated with the general transcription factor TFIIF and the C-terminal domain phosphatase Fcp1, as well as glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which has recently been implicated in transcriptional activation in human cells. Here, we provide evidence that the Rpb7 subunit of pol II interacts with GAPDH. Two-hybrid screen identified GAPDH as an Rpb7-binding protein. In addition, GAPDH was affinity-purified from S. pombe extract by using an Rpb4/Rpb7-coupled column. We also identified actin as a pol II-associated protein and revealed the interaction between actin and Rpb7.","authors":"Mitsuzawa H, Kimura M, Kanda E, Ishihama A","authors_abbrev":"Mitsuzawa H et al.","pubmed_publication_date":"03 Jan 2005","pubmed_entrez_date":"2004-12-29","publication_year":"2005","canto_session_key":"cb8f7133d0ae3b28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-18 15:27:52","canto_approved_date":"2024-07-18 15:27:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-18 15:27:42","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":24,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.13c","SPAC3A12.07","SPAC23C4.15","SPAC1B3.12c","SPBC14C8.12","SPBC19C2.03","SPBC28F2.12","SPBC337.14","SPCC1020.04c","SPCC1620.09c","SPBC354.12","SPCC1442.10c","SPAC23G3.01","SPCC306.09c","SPAC19B12.05c","SPAPYUG7.04c","SPBC32H8.12c","SPBC32F12.11","SPACUNK4.06c","SPAC22H12.02"],"gene_count":20,"ltp_gene_count":20,"approved_date":"2024-07-18"},{"uniquename":"PMID:37937348","title":"Functional Consequences of Shifting Transcript Boundaries in Glucose Starvation.","citation":"Mol Cell Biol 2023;43(11):611-628","abstract":"Glucose is a major source of carbon and essential for the survival of many organisms, ranging from yeast to human. A sudden 60-fold reduction of glucose in exponentially growing fission yeast induces transcriptome-wide changes in gene expression. This regulation is multilayered, and the boundaries of transcripts are known to vary, with functional consequences at the protein level. By combining direct RNA sequencing with 5'-CAGE and short-read sequencing, we accurately defined the 5'- and 3'-ends of transcripts that are both poly(A) tailed and 5'-capped in glucose starvation, followed by proteome analysis. Our results confirm previous experimentally validated loci with alternative isoforms and reveal several transcriptome-wide patterns. First, we show that sense-antisense gene pairs are more strongly anticorrelated when a time lag is taken into account. Second, we show that the glucose starvation response initially elicits a shortening of 3'-UTRs and poly(A) tails, followed by a shortening of the 5'-UTRs at later time points. These result in domain gains and losses in proteins involved in the stress response. Finally, the relatively poor overlap both between differentially expressed genes (DEGs), differential transcript usage events (DTUs), and differentially detected proteins (DDPs) highlight the need for further study on post-transcriptional regulation mechanisms in glucose starvation.","doi":"10.1080/10985549.2023.2270406","authors":"Nguyen LAC, Mori M, Yasuda Y, Galipon J","authors_abbrev":"Nguyen LAC et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-11-08","publication_year":"2023","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2023-11-09 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29722648","title":"Distinct 'safe zones' at the nuclear envelope ensure robust replication of heterochromatic chromosome regions.","citation":"Elife 2018 May 03;7","abstract":"Chromosome replication and transcription occur within a complex nuclear milieu whose functional subdomains are beginning to be mapped out. Here we delineate distinct domains of the fission yeast nuclear envelope (NE), focusing on regions enriched for the inner NE protein, Bqt4, or the lamin interacting domain protein, Lem2. Bqt4 is relatively mobile around the NE and acts in two capacities. First, Bqt4 tethers chromosome termini and the  mat  locus to the NE specifically while these regions are replicating. This positioning is required for accurate heterochromatin replication. Second, Bqt4 mobilizes a subset of Lem2 molecules around the NE to promote pericentric heterochromatin maintenance. Opposing Bqt4-dependent Lem2 mobility are factors that stabilize Lem2 beneath the centrosome, where Lem2 plays a crucial role in kinetochore maintenance. Our data prompt a model in which Bqt4-rich nuclear subdomains are 'safe zones' in which collisions between transcription and replication are averted and heterochromatin is reassembled faithfully.","doi":"10.7554/eLife.32911","authors":"Ebrahimi H, Masuda H, Jain D, Cooper JP","authors_abbrev":"Ebrahimi H et al.","pubmed_publication_date":"03 May 2018","pubmed_entrez_date":"2018-05-04","publication_year":"2018","canto_session_key":"871174866cddff22","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-05-05 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.10","SPBC19C7.10","SPBC2G2.14","SPCC188.13c","SPBC428.08c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"EMBL:SPC06207","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8931154","title":"Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains?","citation":"Protein Sci 1996 Nov;5(11):2353-7","abstract":"Two SH3 domain-containing cytosolic components of the NADPH oxidase, p47phox and p40phox, are shown by analyses of their sequences to contain single copies of a novel class of domain, the PX (phox) domain. Homologous domains are demonstrated to be present in the Cpk class of phosphatidylinositol 3-kinase, S. cerevisiae Bem1p, and S. pombe Scd2, and a large family of human sorting nexin 1 (SNX1) homologues. The majority of these domains contains a polyproline motif, typical of SH3 domain-binding proteins. Two further findings are reported. A third NADPH oxidase subunit, p67phox, is shown to contain four tetratricopeptide repeats (TPRs) within its N-terminal RaclGTP-binding region, and a 28 residue motif in p40phox is demonstrated to be present in protein kinase C isoforms iota/lambda and zeta, and in three ZZ domain-containing proteins.","authors":"Ponting CP","authors_abbrev":"Ponting CP","pubmed_publication_date":"Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6228552","title":"Complementation of a Schizosaccharomyces pombe mutant lacking the beta subunit of the mitochondrial ATPase by the ATP2 gene of Saccharomyces cerevisiae.","citation":"J Biol Chem 1983 Dec 25;258(24):15214-9","abstract":"A chimeric plasmid carrying the structural gene (ATP2) for the mitochondrial ATPase beta subunit of Saccharomyces cerevisiae has been used to complement a mutant of Schizosaccharomyces pombe lacking the beta subunit (Boutry, M., and Goffeau, A. (1982) Eur. J. Biochem. 125, 471-477). Transformation with ATP2 restored the growth rate of S. pombe mutant on glycerol as well as the mitochondrial ATPase and 32Pi-ATP exchange activities to approximately 20% of the parental strain. Mitochondria prepared from the transformant contained a normal amount of a hybrid F1-ATPase consisting of the S. cerevisiae beta subunit assembled with the remaining subunits of the S. pombe ATPase complex. The presence of the S. cerevisiae beta subunit in the S. pombe ATPase complex conferred a sensitivity to the energy transfer inhibitors citreoviridin and oligomycin which was like that of the intact S. cerevisiae enzyme. The S. cerevisiae beta subunit assembled into the hybrid ATPase complex was the same size as the mature subunit in S. cerevisiae. These data indicate that the mechanism of mitochondrial import and the assembly of the cytoplasmically synthesized subunits is similar or identical in these evolutionary divergent yeasts. In addition, this study provides a new approach for the construction of hybrid mitochondrial ATPase complexes which can be used to examine the function of selected subunits in energy transduction.","authors":"Boutry M, Douglas MG","authors_abbrev":"Boutry M et al.","pubmed_publication_date":"25 Dec 1983","pubmed_entrez_date":"1983-12-25","publication_year":"1983","canto_session_key":"f3c450f429a51d04","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2012-11-20 16:08:59","canto_approved_date":"2024-12-11 08:52:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-19 17:43:26","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC222.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-11-20"},{"uniquename":"PMID:31563844","title":"The roles of fission yeast exonuclease 5 in nuclear and mitochondrial genome stability.","citation":"DNA Repair (Amst) 2019 Nov;83:102720","abstract":"The Exo5 family consists of bi-directional, single-stranded DNA-specific exonucleases that contain an iron-sulfur cluster as a structural motif and have multiple roles in DNA metabolism. S. cerevisiae Exo5 is essential for mitochondrial genome maintenance, while the human ortholog is important for nuclear genome stability and DNA repair. Here, we identify the Exo5 ortholog in Schizosaccharomyes pombe (spExo5). The activity of spExo5 is highly similar to that of the human enzyme. When the single-stranded DNA is coated with single-stranded DNA binding protein RPA, spExo5 become a 5'-specific exonuclease. Exo5Δ mutants are sensitive to various DNA damaging agents, particularly interstrand crosslinking agents. An epistasis analysis places exo5 +  in the Fanconi pathway for interstrand crosslink repair. Exo5 +  is in a redundant pathway with rad2 + , which encodes the flap endonuclease FEN1, for mitochondrial genome maintenance. Deletion of both genes lead to severe depletion of the mitochondrial genome, and defects in respiration, indicating that either spExo5 or spFEN1 is necessary for mitochondrial DNA metabolism.","doi":"10.1016/j.dnarep.2019.102720","authors":"Sparks JL, Gerik KJ, Stith CM, Yoder BL, Burgers PM","authors_abbrev":"Sparks JL et al.","pubmed_publication_date":"Nov 2019","pubmed_entrez_date":"2019-09-30","publication_year":"2019","canto_session_key":"957765f909e36351","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Burgers","canto_first_approved_date":"2023-11-10 17:22:07","canto_approved_date":"2024-07-02 11:50:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-08 21:06:20","canto_added_date":"2019-10-01 00:15:04","annotation_curators":[{"name":"Peter Burgers","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":40,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC685.02","SPBC16D10.09","SPBC3E7.08c","SPBC660.13c","SPAC17A2.13c","SPAC22A12.01c","SPAC2F3.04c","SPAC9.05","SPAPB8E5.09","SPAC3G6.06c","SPBC216.05","SPAC8E11.02c","SPAC1565.08","SPCC1753.01c","SPBC29A10.05","SPBC660.11","SPBC83.08","SPBC146.06c","SPAC644.14c","SPAC13C5.07","SPAC1687.05"],"gene_count":21,"ltp_gene_count":14,"approved_date":"2023-11-10"},{"uniquename":"PMID:8524313","title":"The retrotransposon Tf1 assembles virus-like particles that contain excess Gag relative to integrase because of a regulated degradation process.","citation":"Mol Cell Biol 1996 Jan;16(1):338-46","abstract":"The retrotransposon Tf1, isolated from Schizosaccharomyces pombe, contains a single open reading frame with sequences encoding Gag, protease, reverse transcriptase, and integrase (IN). Tf1 has previously been shown to possess significant transposition activity. Although Tf1 proteins do assemble into virus-like particles, the assembly does not require readthrough of a translational reading frame shift or stop codon, common mechanisms used by retroelements to express Gag in molar excess of the polymerase proteins. This study was designed to determine if Tf1 particles contain equal amounts of Gag and polymerase proteins or whether they contain the typical molar excess of Gag. After using two separate methods to calibrate the strength of our antibodies, we found that both S. pombe extracts and partially purified Tf1 particles contained a 26-fold molar excess of Gag relative to IN. Knowing that Gag and IN are derived from the same Tf1 primary translation product, we concluded that the excess Gag most likely resulted from specific degradation of IN. We obtained evidence of regulated IN degradation in comparisons of Tf1 protein extracted from log-phase cells and that extracted from stationary-phase cells. The log-phase cells contained equal molar amounts of Gag and IN, whereas cells approaching stationary phase rapidly degraded IN, leaving an excess of Gag. Analysis of the reverse transcripts indicated that the bulk of reverse transcription occurred within the particles that possess a molar excess of Gag.","authors":"Atwood A, Lin JH, Levin HL","authors_abbrev":"Atwood A et al.","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19076239","title":"Centaurin-like protein Cnt5 contributes to arsenic and cadmium resistance in fission yeast.","citation":"FEMS Yeast Res 2009 Mar;9(2):257-69","abstract":"Arsenic (As) and cadmium (Cd) are two of the most hazardous substances in the environment and have been implicated in a number of human diseases including cancer. Their mechanisms of toxicity and subsequent carcinogenesis are not understood. To identify the genes involved in As/Cd detoxification, we screened a random insertional mutagenesis library of Schizosaccharomyces pombe for mutants that are hypersensitive to As/Cd. Mutations were mapped to spc1(+) (sty1(+)) and SPBC17G9.08c. Spc1 is a stress-activated protein kinase orthologous to human p38. A fragment of SPBC17G9.08c was previously identified as csx2, a high-copy suppressor of cut6 that encodes an acetyl-CoA carboxylase involved in fatty acid biosynthesis. SPBC17G9.08c is a member of the centaurin ADP ribosylation factor GTPase activating protein family found in a variety of fungi, plants and metazoans, but not in Saccharomyces cerevisiae. Cnt5, so named because its closest human homolog is centaurin beta-5, binds to phosphatidic acid and phosphatidyl serine in vitro. Microscopic localization of Cnt5-GFP indicates significant redistribution of Cnt5 from the cytoplasm to the cell membranes in response to As stress. These data suggest a model in which Cnt5 contributes to As/Cd resistance by maintaining membrane integrity or by modulating membrane trafficking.","doi":"10.1111/j.1567-1364.2008.00467.x","authors":"Vashisht AA, Kennedy PJ, Russell P","authors_abbrev":"Vashisht AA et al.","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2008-12-17","publication_year":"2009","canto_session_key":"6b9c58aec7dfe14c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-03-27 14:44:35","canto_approved_date":"2021-11-15 14:49:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-26 13:54:30","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC17G9.08c","SPAC26A3.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-03-27"},{"uniquename":"PMID:21405366","title":"In vivo anomalous diffusion and weak ergodicity breaking of lipid granules.","citation":"Phys Rev Lett 2011 Jan 28;106(4):048103","abstract":"Combining extensive single particle tracking microscopy data of endogenous lipid granules in living fission yeast cells with analytical results we show evidence for anomalous diffusion and weak ergodicity breaking. Namely we demonstrate that at short times the granules perform subdiffusion according to the laws of continuous time random walk theory. The associated violation of ergodicity leads to a characteristic turnover between two scaling regimes of the time averaged mean squared displacement. At longer times the granule motion is consistent with fractional Brownian motion.","authors":"Jeon JH, Tejedor V, Burov S, Barkai E, Selhuber-Unkel C, Berg-Sørensen K, Oddershede L, Metzler R","authors_abbrev":"Jeon JH et al.","pubmed_publication_date":"28 Jan 2011","pubmed_entrez_date":"2011-03-17","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28373490","title":" Schizosaccharomyces pombe  Polysome Profile Analysis and RNA Purification.","citation":"Cold Spring Harb Protoc 2017 Apr 03;2017(4):pdb.prot091637","abstract":"Polysome profile analysis is widely used by investigators studying the mechanism and regulation of translation. The method described here uses high-velocity centrifugation of whole cell extracts on linear sucrose gradients to separate 40S and 60S ribosomal subunits from 80S monosomes and polysomes. Cycloheximide is included in the lysis buffer to \"freeze\" polysomes by blocking translation. After centrifugation, the gradient is fractionated and RNA (and/or protein) is prepared from each fraction for subsequent analysis of individual species using northern or western blots. The entire RNA population in each fraction can be analyzed by hybridization to microarrays or by high-throughput RNA sequencing, and the proteins present can be identified by mass spectrometry analysis.","doi":"10.1101/pdb.prot091637","authors":"Wolf DA, Bähler J, Wise JA","authors_abbrev":"Wolf DA et al.","pubmed_publication_date":"03 Apr 2017","pubmed_entrez_date":"2017-04-05","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-04-06 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30165961","title":"Drug delivery and temperature control in microfluidic chips during live-cell imaging experiments.","citation":"Methods Cell Biol 2018;147:3-28","abstract":"Microfluidic technologies have become a standard tool in cell biological studies, offering unprecedented control of the chemical and physical environment of cells grown in microdevices, the possibility of multiplexing assays, as well as the capacity to monitor the behavior of single cells in real time while dynamically manipulating their growth medium. However, the properties of the materials employed for the fabrication of microchips that are compatible with live-cell imaging has limited the use of these techniques for a broad range of experiments. In particular, the strong absorption of a large panel of small molecules by these materials prevents the accurate delivery of compounds of interest. Here we describe a novel microsystem dedicated to live-cell imaging that (1) uses alternative materials devoid of absorptive properties, and (2) allows for dynamic in-chip control of sample temperature. Based on a proof-of-concept design that we have routinely used with non-adherent fission yeast cells, this chapter details all the steps for the fabrication and utilization of these microdevices.","doi":"10.1016/bs.mcb.2018.06.004","authors":"Muñoz-Garcia J, Babic J, Coudreuse D","authors_abbrev":"Muñoz-Garcia J et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-09-01","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-09-02 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25361784","title":"Homozygous splice mutation in CWF19L1 in a Turkish family with recessive ataxia syndrome.","citation":"Neurology 2014 Dec 02;83(23):2175-82","abstract":"To elucidate the genetic cause of a rare recessive ataxia presented by 2 siblings from a consanguineous Turkish family with a nonprogressive, congenital ataxia with mental retardation of unknown etiology.\nWhole-exome sequencing was combined with homozygosity mapping, linkage, and expression analysis to identify candidate genes, confirmed by Sanger sequencing. Reverse transcription-PCR and immunoblotting were used to determine the functional consequences of the gene variant. A zebrafish model was developed using morpholino-mediated knockdown.\nWe identified a homozygous mutation at the invariant +1 position (c.964+1G>A) in intron 9 of the CWF19L1 (complexed with cdc5 protein 19-like 1) gene. This mutation is absent in >6,500 European and African American individuals and 200 Turkish control DNAs. The mutation causes exon skipping, reduction in messenger RNA levels, and protein loss in cell lines of affected individuals. Morpholino-mediated knockdown in a zebrafish model demonstrates that loss of the evolutionarily highly conserved CWF19L1, whose normal biological function is unknown, alters cerebellar morphology and causes movement abnormalities.\nOur results suggest that CWF19L1 mutations may be a novel cause of recessive ataxia with developmental delay. Our research may help with diagnosis, especially in Turkey, identify causes of other ataxias, and may lead to novel therapies.","doi":"10.1212/WNL.0000000000001053","authors":"Burns R, Majczenko K, Xu J, Peng W, Yapici Z, Dowling JJ, Li JZ, Burmeister M","authors_abbrev":"Burns R et al.","pubmed_publication_date":"02 Dec 2014","pubmed_entrez_date":"2014-11-02","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18326292","title":"[Is spindle formation in fission yeast specific to the species?: from the viewpoint of nuclear transport and spindle pole body].","citation":"Tanpakushitsu Kakusan Koso 2008 Mar;53(3):197-206","abstract":"","authors":"Sato M, Toya M, Toda T","authors_abbrev":"Sato M et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-03-11","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22264609","title":"A role for metaphase spindle elongation forces in correction of merotelic kinetochore attachments.","citation":"Curr Biol 2012 Feb 07;22(3):225-30","abstract":"During mitosis, equal segregation of chromosomes depends on proper kinetochore-microtubule attachments. Merotelic kinetochore orientation, in which a single kinetochore binds microtubules from both spindle poles [1], is a major cause of chromosome instability [2], which is commonly observed in solid tumors [3, 4]. Using the fission yeast Schizosaccharomyces pombe, we show that a proper force balance between kinesin motors on interpolar spindle microtubules is critical for correcting merotelic attachments. Inhibition of the plus-end-directed spindle elongation motors kinesin-5 (Cut7) and kinesin-6 (Klp9) reduces spindle length, tension at kinetochores, and the frequency of merotelic attachments. In contrast, merotely is increased by deletion of the minus-end-directed kinesin-14 (Klp2) or overexpression of Klp9. Also, Cdk1 regulates spindle elongation forces to promote merotelic correction by phosphorylating and inhibiting Klp9. The role of spindle elongation motors in merotelic correction is conserved, because partial inhibition of the human kinesin-5 homolog Eg5 using the drug monastrol reduces spindle length and lagging chromosome frequency in both normal (RPE-1) and tumor (CaCo-2) cells. These findings reveal unexpected links between spindle forces and correction of merotelic attachments and show that pharmacological manipulation of spindle elongation forces might be used to reduce chromosome instability in cancer cells.","doi":"10.1016/j.cub.2011.12.022","authors":"Choi SH, McCollum D","authors_abbrev":"Choi SH et al.","pubmed_publication_date":"07 Feb 2012","pubmed_entrez_date":"2012-01-24","publication_year":"2012","canto_session_key":"2aa2213600dbe8e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-02-28 12:26:07","canto_approved_date":"2020-11-08 12:33:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-13 14:43:46","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPBC582.03","SPAC664.10","SPBC15D4.01c","SPBC6B1.04","SPCC320.13c","SPAC1782.09c","SPCC962.02c","SPAC25G10.07c","SPBC11B10.09","SPBC336.15"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2018-02-28"},{"uniquename":"PMID:20188637","title":"Interaction between human mismatch repair recognition proteins and checkpoint sensor Rad9-Rad1-Hus1.","citation":"DNA Repair (Amst) 2010 May 04;9(5):478-87","abstract":"In eukaryotic cells, the cell cycle checkpoint proteins Rad9, Rad1, and Hus1 form the 9-1-1 complex which is structurally similar to the proliferating cell nuclear antigen (PCNA) sliding clamp. hMSH2/hMSH6 (hMutS alpha) and hMSH2/hMSH3 (hMutS beta) are the mismatch recognition factors of the mismatch repair pathway. hMutS alpha has been shown to physically and functionally interact with PCNA. Moreover, DNA methylating agent N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) treatment induces the G2/M cell cycle arrest that is dependent on the presence of hMutS alpha and hMutL alpha. In this study, we show that each subunit of the human 9-1-1 complex physically interacts with hMSH2, hMSH3, and hMSH6. The 9-1-1 complex from both humans and Schizosaccharomyces pombe can stimulate hMutS alpha binding with G/T-containing DNA. Rad9, Rad1, and Hus1 individual subunits can also stimulate the DNA binding activity of hMutS alpha. Human Rad9 and hMSH6 colocalize to nuclear foci of HeLa cells after exposure to MNNG. However, Rad9 does not form foci in MSH6 defective cells following MNNG treatment. In Rad9 knockdown untreated cells, the majority of the MSH6 is in cytoplasm. Following MNNG treatment, Rad9 knockdown cells has abnormal nuclear morphology and MSH6 is distributed around nuclear envelop. Our findings suggest that the 9-1-1 complex is a component of the mismatch repair involved in MNNG-induced damage response.","doi":"10.1016/j.dnarep.2010.01.011","authors":"Bai H, Madabushi A, Guan X, Lu AL","authors_abbrev":"Bai H et al.","pubmed_publication_date":"04 May 2010","pubmed_entrez_date":"2010-03-02","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27245259","title":"Telomerase RNA is more than a DNA template.","citation":"RNA Biol 2016 Aug 02;13(8):683-9","abstract":"The addition of telomeric DNA to chromosome ends is an essential cellular activity that compensates for the loss of genomic DNA that is due to the inability of the conventional DNA replication apparatus to duplicate the entire chromosome. The telomerase reverse transcriptase and its associated RNA bind to the very end of the telomere via a sequence in the RNA and specific protein-protein interactions. Telomerase RNA also provides the template for addition of new telomeric repeats by the reverse-transcriptase protein subunit. In addition to the template, there are 3 other conserved regions in telomerase RNA that are essential for normal telomerase activity. Here we briefly review the conserved core regions of telomerase RNA and then focus on a recent study in fission yeast that determined the function of another conserved region in telomerase RNA called the Stem Terminus Element (STE). (1) The STE is distant from the templating core of telomerase in both the linear and RNA secondary structure, but, nonetheless, affects the fidelity of telomere sequence addition and, in turn, the ability of telomere binding proteins to bind and protect chromosome ends. We will discuss possible mechanisms of STE action and the suitability of the STE as an anti-cancer target.","doi":"10.1080/15476286.2016.1191725","authors":"Webb CJ, Zakian VA","authors_abbrev":"Webb CJ et al.","pubmed_publication_date":"02 Aug 2016","pubmed_entrez_date":"2016-06-02","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-06-03 00:15:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06","SPAC16A10.07c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:24256274","title":"Copper transport and regulation in Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 2013 Dec;41(6):1679-86","abstract":"The fission yeast Schizosaccharomyces pombe has been successfully used as a model to gain fundamental knowledge in understanding how eukaryotic cells acquire copper during vegetative growth. These studies have revealed the existence of a heteromeric Ctr4-Ctr5 plasma membrane complex that mediates uptake of copper within the cells. Furthermore, additional studies have led to the identification of one of the first vacuolar copper transporters, Ctr6, as well as the copper-responsive Cuf1 transcription factor. Recent investigations have extended the use of S. pombe to elucidate new roles for copper metabolism in meiotic differentiation. For example, these studies have led to the discovery of Mfc1, which turned out to be the first example of a meiosis-specific copper transporter. Whereas copper-dependent transcriptional regulation of the Ctr family members is under the control of Cuf1 during mitosis or meiosis, meiosis-specific copper transporter Mfc1 is regulated by the recently discovered transactivator Mca1. It is foreseeable that identification of novel meiotic copper-related proteins will serve as stepping stones to unravel fundamental aspects of copper homoeostasis.","doi":"10.1042/BST2013089","authors":"Beaudoin J, Ekici S, Daldal F, Ait-Mohand S, Guérin B, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38508182","title":"Synchronized assembly of the oxidative phosphorylation system controls mitochondrial respiration in yeast.","citation":"Dev Cell 2024 Apr 22;59(8):1043-1057.e8","abstract":"Control of protein stoichiometry is essential for cell function. Mitochondrial oxidative phosphorylation (OXPHOS) presents a complex stoichiometric challenge as the ratio of the electron transport chain (ETC) and ATP synthase must be tightly controlled, and assembly requires coordinated integration of proteins encoded in the nuclear and mitochondrial genome. How correct OXPHOS stoichiometry is achieved is unknown. We identify the Mitochondrial Regulatory hub for respiratory Assembly (MiRA) platform, which synchronizes ETC and ATP synthase biogenesis in yeast. Molecularly, this is achieved by a stop-and-go mechanism: the uncharacterized protein Mra1 stalls complex IV assembly. Two \"Go\" signals are required for assembly progression: binding of the complex IV assembly factor Rcf2 and Mra1 interaction with an Atp9-translating mitoribosome induce Mra1 degradation, allowing synchronized maturation of complex IV and the ATP synthase. Failure of the stop-and-go mechanism results in cell death. MiRA controls OXPHOS assembly, ensuring correct stoichiometry of protein machineries encoded by two different genomes.","doi":"10.1016/j.devcel.2024.02.011","authors":"Moretti-Horten DN, Peselj C, Taskin AA, Myketin L, Schulte U, Einsle O, Drepper F, Luzarowski M, Vögtle FN","authors_abbrev":"Moretti-Horten DN et al.","pubmed_publication_date":"22 Apr 2024","pubmed_entrez_date":"2024-03-20","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB8E5.10","SPBC3H7.08c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:21165758","title":"Evaluation of the acetaldehyde production and degradation potential of 26 enological Saccharomyces and non-Saccharomyces yeast strains in a resting cell model system.","citation":"J Ind Microbiol Biotechnol 2011 Sep;38(9):1391-8","abstract":"Acetaldehyde is relevant for wine aroma, wine color, and microbiological stability. Yeast are known to play a crucial role in production and utilization of acetaldehyde during fermentations but comparative quantitative data are scarce. This research evaluated the acetaldehyde metabolism of 26 yeast strains, including commercial Saccharomyces and non-Saccharomyces, in a reproducible resting cell model system. Acetaldehyde kinetics and peak values were highly genus, species, and strain dependent. Peak acetaldehyde values varied from 2.2 to 189.4 mg l(-1) and correlated well (r(2) = 0.92) with the acetaldehyde production yield coefficients that ranged from 0.4 to 42 mg acetaldehyde per g of glucose in absence of SO(2). S. pombe showed the highest acetaldehyde production yield coefficients and peak values. All other non-Saccharomyces species produced significantly less acetaldehyde than the S. cerevisiae strains and were less affected by SO(2) additions. All yeast strains could degrade acetaldehyde as sole substrate, but the acetaldehyde degradation rates did not correlate with acetaldehyde peak values or acetaldehyde production yield coefficients in incubations with glucose as sole substrate.","doi":"10.1007/s10295-010-0924-1","authors":"Li E, de Orduña RM","authors_abbrev":"Li E et al.","pubmed_publication_date":"Sep 2011","pubmed_entrez_date":"2010-12-18","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27140919","title":"Colony Polymerase Chain Reaction with Schizosaccharomyces pombe.","citation":"Cold Spring Harb Protoc 2016 May 02;2016(5)","abstract":"When screening a large number of individual Schizosaccharomyces pombe strains by polymerase chain reaction (PCR), a rapid \"colony PCR\" approach may be used. Numerous colony PCR protocols are available, and fundamental to them all is that the colony must be fresh (grown overnight) and that as few cells as possible are used. In this protocol, we present three reliable methods for preparing S. pombe cells for colony PCR.","doi":"10.1101/pdb.prot090993","authors":"Murray JM, Watson AT, Carr AM","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"02 May 2016","pubmed_entrez_date":"2016-05-04","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-05-05 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1115508","title":"Microbial reduction of 1,3-dioxo-2-methyl-2-(3'0oxo-6'-carbomethoxyhexyl)-cyclopentane to form 1 beta-hydroxy-3-oxo-2beta-methyl-2alpha-(3'-oxo-6'-carbomethoxyhexyl)-cyclopentane, an intermediate for steroid total syntheses.","citation":"Appl Microbiol 1975 Mar;29(3):427-9","abstract":"The rate and extent of stereoselective reduction of 1,3-dioxo-2-methyl-2-(3'-oxo-6'-carbomethoxyhexyl)-cyclopentane to form the 1beta-hydroxy-2beta-methyl isomer by cultures of Schizosaccharomyces pombe ATCC 2476 was dramatically increased by addition to the fermentation of certain alpha,beta-unsaturated ketones and allyl alcohol.","authors":"Lanzilotta RP, Bradley DG, Beard CC","authors_abbrev":"Lanzilotta RP et al.","pubmed_publication_date":"Mar 1975","pubmed_entrez_date":"1975-03-01","publication_year":"1975","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12963832","title":"Polo-like kinase 1 in the life and death of cancer cells.","citation":"Cell Cycle 2003;2(5):424-5","abstract":"The polo-like kinase family plays a vital role in many cell cycle related events. The family includes mammalian Plkl, Snk (Plk2), and Fnk/Prk (Plk3), Xenopus laevis Plxl,Drosophila polo, fission yeast Plol, and budding yeast Cdc5. These enzymes, in addition to a conserved kinase domain at the N-terminus, have highly conserved sequences called polo-box(s) in the non-catalytic C-terminal domain. Genetic and biochemical experiments with several different organisms have documented that polo-like kinases are involved in many aspects of the cell cycle, such as activation of Cdc2, centrosome assembly and maturation, activation of the anaphase-promoting complex (APC) during the metaphase-anaphase transition, and cytokinesis.","authors":"Liu X, Erikson RL","authors_abbrev":"Liu X et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-09-10","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22723423","title":"The fission yeast FANCM ortholog directs non-crossover recombination during meiosis.","citation":"Science 2012 Jun 22;336(6088):1585-8","abstract":"The formation of healthy gametes depends on programmed DNA double-strand breaks (DSBs), which are each repaired as a crossover (CO) or non-crossover (NCO) from a homologous template. Although most of these DSBs are repaired without giving COs, little is known about the genetic requirements of NCO-specific recombination. We show that Fml1, the Fanconi anemia complementation group M (FANCM)-ortholog of Schizosaccharomyces pombe, directs the formation of NCOs during meiosis in competition with the Mus81-dependent pro-CO pathway. We also define the Rad51/Dmc1-mediator Swi5-Sfr1 as a major determinant in biasing the recombination process in favor of Mus81, to ensure the appropriate amount of COs to guide meiotic chromosome segregation. The conservation of these proteins from yeast to humans suggests that this interplay may be a general feature of meiotic recombination.","doi":"10.1126/science.1220111","authors":"Lorenz A, Osman F, Sun W, Nandi S, Steinacher R, Whitby MC","authors_abbrev":"Lorenz A et al.","pubmed_publication_date":"22 Jun 2012","pubmed_entrez_date":"2012-06-23","publication_year":"2012","canto_session_key":"37ebf9ba3b26613d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Matthew whitby","canto_first_approved_date":"2015-09-29 16:10:27","canto_approved_date":"2020-11-11 10:25:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-07 15:07:05","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Matthew whitby","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20H4.04","SPBC336.01","SPAC2G11.12","SPAC4H3.05","SPCC4G3.05c","SPCC576.12c","SPAC17A5.11","SPBC2D10.16","SPBC28F2.07","SPAC9.05"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2015-09-29"},{"uniquename":"PMID:28479325","title":"Size-Dependent Expression of the Mitotic Activator Cdc25 Suggests a Mechanism of Size Control in Fission Yeast.","citation":"Curr Biol 2017 May 22;27(10):1491-1497.e4","abstract":"Proper cell size is essential for cellular function. Nonetheless, despite more than 100 years of work on the subject, the mechanisms that maintain cell-size homeostasis are largely mysterious [1]. Cells in growing populations maintain cell size within a narrow range by coordinating growth and division. Bacterial and eukaryotic cells both demonstrate homeostatic size control, which maintains population-level variation in cell size within a certain range and returns the population average to that range if it is perturbed [1, 2]. Recent work has proposed two different strategies for size control: budding yeast has been proposed to use an inhibitor-dilution strategy to regulate size at the G1/S transition [3], whereas bacteria appear to use an adder strategy, in which a fixed amount of growth each generation causes cell size to converge on a stable average [4-6]. Here we present evidence that cell size in the fission yeast Schizosaccharomyces pombe is regulated by a third strategy: the size-dependent expression of the mitotic activator Cdc25. cdc25 transcript levels are regulated such that smaller cells express less Cdc25 and larger cells express more Cdc25, creating an increasing concentration of Cdc25 as cells grow and providing a mechanism for cells to trigger cell division when they reach a threshold concentration of Cdc25. Because regulation of mitotic entry by Cdc25 is well conserved, this mechanism may provide a widespread solution to the problem of size control in eukaryotes.","doi":"10.1016/j.cub.2017.04.016","authors":"Keifenheim D, Sun XM, D'Souza E, Ohira MJ, Magner M, Mayhew MB, Marguerat S, Rhind N","authors_abbrev":"Keifenheim D et al.","pubmed_publication_date":"22 May 2017","pubmed_entrez_date":"2017-05-09","publication_year":"2017","canto_session_key":"5b029ec9b56c8283","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nick Rhind","canto_first_approved_date":"2022-02-15 15:00:35","canto_approved_date":"2025-09-03 16:54:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-31 18:24:10","canto_added_date":"2017-05-11 00:15:13","annotation_curators":[{"name":"Nick Rhind","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC28F2.12","SPAC24H6.05","SPCC18B5.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2022-02-15"},{"uniquename":"PMID:11015725","title":"Purification, molecular and kinetic characterization of phosphofructokinase-1 from the yeast Schizosaccharomyces pombe: evidence for an unusual subunit composition.","citation":"Yeast 2000 Oct;16(14):1273-85","abstract":"Phosphofructokinase-1 (Pfk-1) from Schizosaccharomyces pombe was purified by 54-fold enrichment to homogeneity elaborating the following steps: (a) Disruption of the cells with glass beads; (b) fractionated precipitation with polyethylene glycol 6000; (c) affinity chromatography on Cibacron-Blue F3G-A-Sephadex G 100; (d) ion exchange chromatography on Resource Q. The native enzyme exhibits a mass of 790+/-30 kDa, as detected by sedimentation equilibrium measurements. The apparent sedimentation coefficient was found to be s(20,c)=20.2+/-0.3 S. No significant dependence of the s-value on the protein concentration was observed in the range 0. 07-0.7 mg/ml. Polyacrylamide gel electrophoresis in presence of sodium dodecyl sulphate and MALDI-TOF spectra showed that the enzyme is composed of subunits of identical size of 100+/-5 kDa, forming an octameric structure. The N-terminus of the enzyme was found to be blocked. Sequences of tryptic and chymotryptic peptides of the subunit coincide with the proposed amino acid sequence as deduced from the gene from the EMBL library. The Pfk-1 coding sequence of S. pombe was transformed into a Pfk-1 double deletion mutants of Saccharomyces cerevisiae resulting in glucose-positive cells with enzyme activity in the crude cell extract. The kinetic analysis revealed less cooperativity to fructose 6-phosphate (n(H)=1.6) and less inhibition by ATP as compared to the enzyme from baker's yeast. Fructose 2,6-bisphosphate (in micromolar range) and AMP (in millimolar range) were found to overcome ATP inhibition and to increase the affinity to fructose 6-phosphate.","authors":"Reuter R, Naumann M, Bär J, Haferburg D, Kopperschläger G","authors_abbrev":"Reuter R et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-10-04","publication_year":"2000","canto_session_key":"693ca3ebfd69a3c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-09-23 15:07:07","canto_approved_date":"2024-05-25 11:46:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-23 15:03:16","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16H5.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-23"},{"uniquename":"PMID:18406331","title":"Glycolytic enzyme GAPDH promotes peroxide stress signaling through multistep phosphorelay to a MAPK cascade.","citation":"Mol Cell 2008 Apr 11;30(1):108-13","abstract":"Phosphorelay signaling of environmental stimuli by two-component systems is prevailing in bacteria and also utilized by fungi and plants. In the fission yeast Schizosaccharomyces pombe, peroxide stress signals are transmitted from the Mak2/3 sensor kinases to the Mpr1 histidine-containing phosphotransfer (HPt) protein and finally to the Mcs4 response regulator, which activates a MAP kinase cascade. Here we show that, unexpectedly, the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) physically associates with the Mcs4 response regulator and stress-responsive MAP kinase kinase kinases (MAPKKKs). In response to H2O2 stress, Cys-152 of the Tdh1 GAPDH is transiently oxidized, which enhances the association of Tdh1 with Mcs4. Furthermore, Tdh1 is essential for the interaction between the Mpr1 HPt protein and the Mcs4 response regulator and thus for phosphorelay signaling. These results demonstrate that the glycolytic enzyme GAPDH plays an essential role in the phosphorelay signaling, where its redox-sensitive cysteine residue may provide additional input signals.","doi":"10.1016/j.molcel.2008.01.017","authors":"Morigasaki S, Shimada K, Ikner A, Yanagida M, Shiozaki K","authors_abbrev":"Morigasaki S et al.","pubmed_publication_date":"11 Apr 2008","pubmed_entrez_date":"2008-04-15","publication_year":"2008","canto_session_key":"5f3b07c1f6fbede1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Susumu Morigasaki","canto_first_approved_date":"2019-01-28 23:26:36","canto_approved_date":"2024-05-25 07:35:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-11 07:27:13","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":38,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Susumu Morigasaki","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC354.12","SPAC24B11.06c","SPBC725.02","SPAC1006.09","SPBC32F12.11","SPBC887.10","SPAC9G1.02"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2019-01-28"},{"uniquename":"PMID:37891889","title":"Comparing Mitochondrial Activity, Oxidative Stress Tolerance, and Longevity of Thirteen  Ascomycota  Yeast Species.","citation":"Antioxidants (Basel) 2023 Sep 28;12(10)","abstract":"Aging is characterized by a number of hallmarks including loss of mitochondrial homeostasis and decay in stress tolerance, among others. Unicellular eukaryotes have been widely used to study chronological aging. As a general trait, calorie restriction and activation of mitochondrial respiration has been proposed to contribute to an elongated lifespan. Most aging-related studies have been conducted with the Crabtree-positive yeasts  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe , and with deletion collections deriving from these conventional yeast models. We have performed an unbiased characterization of longevity using thirteen fungi species, including  S. cerevisiae  and  S. pombe , covering a wide range of the  Ascomycota  clade. We have determined their mitochondrial activity by oxygen consumption, complex IV activity, and mitochondrial redox potential, and the results derived from these three methodologies are highly overlapping. We have phenotypically compared the lifespans of the thirteen species and their capacity to tolerate oxidative stress. Longevity and elevated tolerance to hydrogen peroxide are correlated in some but not all yeasts. Mitochondrial activity per se cannot anticipate the length of the lifespan. We have classified the strains in four groups, with members of group 1 ( Kluyveromyces lactis ,  Saccharomyces bayanus  and  Lodderomyces elongisporus ) displaying high mitochondrial activity, elevated resistance to oxidative stress, and elongated lifespan.","doi":"10.3390/antiox12101810","authors":"Gröger A, Martínez-Albo I, Albà MM, Ayté J, Vega M, Hidalgo E","authors_abbrev":"Gröger A et al.","pubmed_publication_date":"28 Sep 2023","pubmed_entrez_date":"2023-10-28","publication_year":"2023","canto_session_key":"1dfd55448d831cb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-11-28 13:34:21","canto_approved_date":"2023-11-28 13:34:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-27 12:35:32","canto_added_date":"2023-10-28 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2023-11-28"},{"uniquename":"PMID:18723604","title":"Copper distributed by Atx1 is available to copper amine oxidase 1 in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2008 Oct;7(10):1781-94","abstract":"Copper amine oxidases (CAOs) have been proposed to be involved in the metabolism of xenobiotic and biogenic amines. The requirement for copper is absolute for their activity. In the fission yeast Schizosaccharomyces pombe, cao1(+) and cao2(+) genes are predicted to encode members of the CAO family. While both genes are expressed in wild-type cells, we determined that the expression of only cao1(+) but not cao2(+) results in the production of an active enzyme. Site-directed mutagenesis identified three histidine residues within the C-terminal region of Cao1 that are necessary for amine oxidase activity. By use of a cao1(+)-GFP allele that retained wild-type function, Cao1-GFP was localized in the cytosol (GFP is green fluorescent protein). Under copper-limiting conditions, disruption of ctr4(+), ctr5(+), and cuf1(+) produced a defect in amine oxidase activity, indicating that a functionally active Cao1 requires Ctr4/5-mediated copper transport and the transcription factor Cuf1. Likewise, atx1 null cells exhibited substantially decreased levels of amine oxidase activity. In contrast, deletion of ccc2, cox17, and pccs had no significant effect on Cao1 activity. Residual amine oxidase activity in cells lacking atx1(+) can be restored to normal levels by returning an atx1(+) allele, underscoring the critical importance of the presence of Atx1 in cells. Using two-hybrid analysis, we demonstrated that Cao1 physically interacts with Atx1 and that this association is comparable to that of Atx1 with the N-terminal region of Ccc2. Collectively, these results describe the first example of the ability of Atx1 to act as a copper carrier for a molecule other than Ccc2 and its critical role in delivering copper to Cao1.","doi":"10.1128/EC.00230-08","authors":"Peter C, Laliberté J, Beaudoin J, Labbé S","authors_abbrev":"Peter C et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-08-30","publication_year":"2008","canto_session_key":"2671173a533b649f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-12-16 13:07:55","canto_approved_date":"2024-10-25 23:16:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-20 14:36:17","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.04","SPBC29A3.01","SPAC2E1P3.04","SPAC1142.05","SPCC1393.10","SPBC1709.10c","SPBC1289.16c","SPBC26H8.14c","SPAC31A2.11c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2014-12-16"},{"uniquename":"PMID:11884604","title":"Functional divergence between histone deacetylases in fission yeast by distinct cellular localization and in vivo specificity.","citation":"Mol Cell Biol 2002 Apr;22(7):2170-81","abstract":"Histone deacetylases (HDACs) are important for gene regulation and the maintenance of heterochromatin in eukaryotes. Schizosaccharomyces pombe was used as a model system to investigate the functional divergence within this conserved enzyme family. S. pombe has three HDACs encoded by the hda1(+), clr3(+), and clr6(+) genes. Strains mutated in these genes have previously been shown to display strikingly different phenotypes when assayed for viability, chromosome loss, and silencing. Here, conserved differences in the substrate binding pocket identify Clr6 and Hda1 as class I HDACs, while Clr3 belongs in the class II family. Furthermore, these HDACs were shown to have strikingly different subcellular localization patterns. Hda1 was localized to the cytoplasm, while most of Clr3 resided throughout the nucleus. Finally, Clr6 was localized exclusively on the chromosomes in a spotted pattern. Interestingly, Clr3, the only HDAC present in the nucleolus, was required for ribosomal DNA (rDNA) silencing. Clr3 presumably acts directly on heterochromatin, since it colocalized with the centromere, mating-type region, and rDNA as visualized by in situ hybridization. In addition, Clr3 could be cross-linked to mat3 in chromatin immunoprecipitation experiments. Western analysis of bulk histone preparations indicated that Hda1 (class I) had a generally low level of activity in vivo and Clr6 (class I) had a high level of activity and broad in vivo substrate specificity, whereas Clr3 (class II) displayed its main activity on acetylated lysine 14 of histone H3. Thus, the distinct functions of the S. pombe HDACs are likely explained by their distinct cellular localization and their different in vivo specificities.","authors":"Bjerling P, Silverstein RA, Thon G, Caudy A, Grewal S, Ekwall K","authors_abbrev":"Bjerling P et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-03-09","publication_year":"2002","canto_session_key":"c04525e422559462","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-02-12 15:58:28","canto_approved_date":"2025-09-02 17:35:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-12 15:46:18","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":27,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.11c","SPAC1834.04","SPBC800.03","SPBC36.05c","SPAC3G9.07c","SPBC8D2.04"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2021-02-12"},{"uniquename":"EMBL:D89120","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14745200","title":"Truncated Sla1 induces haploid meiosis through the Pat1-Mei2 system in fission yeast.","citation":"Biosci Biotechnol Biochem 2004 Jan;68(1):266-70","abstract":"We previously reported that expression of Sla1DeltaC, a truncated form of Sla1, induces ectopic meiosis in heterothallic fission yeast and this was possibly due to the inhibition of Pat1 kinase by Sla1DeltaC. Here we found mei2 mRNA and the Mei2 protein accumulated and stability of the Mei2 protein increased when Sla1DeltaC was expressed. The former two results are considered to be the consequence of de-repression of Ste11, which is the transcription factor of mei2 and negatively regulated by Pat1 kinase. The latter result reflects the consequence of deregulation of Mei2 by Pat1 kinase. In addition, Ste11 accumulated in the nucleus when Sla1DeltaC was expressed. All these data consistently support the idea that the action of Sla1DeltaC is to inactivate Pat1 kinase.","authors":"Tanabe K, Tanaka K, Matsuda H, Kawamukai M","authors_abbrev":"Tanabe K et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2004-01-28","publication_year":"2004","canto_session_key":"830538b82282c5fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-29 13:31:20","canto_approved_date":"2022-07-22 19:49:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-01 09:52:21","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.10c","SPBC19C2.05","SPBC365.06","SPBC32C12.02","SPAC27D7.03c","SPBC1A4.02c"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2015-01-29"},{"uniquename":"EMBL:AF059906","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC02754","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16087744","title":"Distinct signaling pathways respond to arsenite and reactive oxygen species in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2005 Aug;4(8):1396-402","abstract":"Exposure to certain metal and metalloid species, such as arsenic, cadmium, chromium, and nickel, has been associated with an increased risk of cancer in humans. The biological effects of these metals are thought to result from induction of reactive oxygen species (ROS) and inhibition of DNA repair enzymes, although alterations in signal transduction pathways may also be involved in tumor development. To better understand metal toxicity and its connection to ROS, we have compared the effects of arsenite and hydrogen peroxide in wild-type and mutant strains of the fission yeast Schizosaccharomyces pombe. An atf1Delta pap1Delta strain, which is defective in two transcription factors that control stress responses, is extremely sensitive to hydrogen peroxide but not to arsenite. A strain that lacks the transcription factor Zip1 has the opposite relationship. Spc1 (Sty1) mitogen-activated protein kinase (MAPK), a homologue of mammalian p38 MAPK, and the upstream MAPK kinase (MAPKK) Wis1 are essential for survival of both arsenite and hydrogen peroxide. Inactivation of two MAPKK kinases, Win1 and Wis4, almost completely eliminates Spc1 activation by arsenite, yet these cells survive arsenite treatment. The two-component phosphorelay protein Mcs4, which acts upstream of Win1 and Wis4 and is required for Spc1 activation in response to oxidative stress, is not required for Spc1 activation in response to arsenite. We conclude that the toxic effects of arsenic are not strongly connected to oxidative stress and that although Spc1 is activated by arsenic exposure, the basal activity of Spc1 is largely sufficient for the survival of arsenic.","authors":"Rodríguez-Gabriel MA, Russell P","authors_abbrev":"Rodríguez-Gabriel MA et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-08-10","publication_year":"2005","canto_session_key":"494b77521c380009","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-13 10:08:23","canto_approved_date":"2022-02-02 11:49:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-07 07:40:26","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":37,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.03","SPAC26F1.10c","SPAC1006.09","SPBC409.07c","SPBC887.10","SPAC1783.07c","SPAC19D5.01","SPAC24B11.06c","SPBC29B5.01","SPAC9G1.02"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2017-07-13"},{"uniquename":"EMBL:AU008522","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28882993","title":"The condensin complex is a mechanochemical motor that translocates along DNA.","citation":"Science 2017 Nov 03;358(6363):672-676","abstract":"Condensin plays crucial roles in chromosome organization and compaction, but the mechanistic basis for its functions remains obscure. We used single-molecule imaging to demonstrate that  Saccharomyces cerevisiae  condensin is a molecular motor capable of adenosine triphosphate hydrolysis-dependent translocation along double-stranded DNA. Condensin's translocation activity is rapid and highly processive, with individual complexes traveling an average distance of ≥10 kilobases at a velocity of ~60 base pairs per second. Our results suggest that condensin may take steps comparable in length to its ~50-nanometer coiled-coil subunits, indicative of a translocation mechanism that is distinct from any reported for a DNA motor protein. The finding that condensin is a mechanochemical motor has important implications for understanding the mechanisms of chromosome organization and condensation.","doi":"10.1126/science.aan6516","authors":"Terakawa T, Bisht S, Eeftens JM, Dekker C, Haering CH, Greene EC","authors_abbrev":"Terakawa T et al.","pubmed_publication_date":"03 Nov 2017","pubmed_entrez_date":"2017-09-09","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.06c","SPBC146.03c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:11226158","title":"Specificity of Cdk activation in vivo by the two Caks Mcs6 and Csk1 in fission yeast.","citation":"EMBO J 2001 Jan 15;20(1-2):82-90","abstract":"Activating phosphorylation of cyclin-dependent kinases (Cdks) is mediated by at least two structurally distinct types of Cdk-activating kinases (Caks): the trimeric Cdk7-cyclin H-Mat1 complex in metazoans and the single-subunit Cak1 in budding yeast. Fission yeast has both Cak types: Mcs6 is a Cdk7 ortholog and Csk1 a single-subunit kinase. Both phosphorylate Cdks in vitro and rescue a thermosensitive budding yeast CAK1 strain. However, this apparent redundancy is not observed in fission yeast in vivo. We have identified mutants that exhibit phenotypes attributable to defects in either Mcs6-activating phosphorylation or in Cdc2-activating phosphorylation. Mcs6, human Cdk7 and budding yeast Cak1 were all active as Caks for Cdc2 when expressed in fission yeast. Although Csk1 could activate Mcs6, it was unable to activate Cdc2. Biochemical experiments supported these genetic results: budding yeast Cak1 could bind and phosphorylate Cdc2 from fission yeast lysates, whereas fission yeast Csk1 could not. These results indicate that Mcs6 is the direct activator of Cdc2, and Csk1 only activates Mcs6. This demonstrates in vivo specificity in Cdk activation by Caks.","authors":"Hermand D, Westerling T, Pihlak A, Thuret JY, Vallenius T, Tiainen M, Vandenhaute J, Cottarel G, Mann C, Mäkelä TP","authors_abbrev":"Hermand D et al.","pubmed_publication_date":"15 Jan 2001","pubmed_entrez_date":"2001-02-28","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1D4.06c","SPBC19F8.07"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:26108218","title":"Module-based construction of plasmids for chromosomal integration of the fission yeast Schizosaccharomyces pombe.","citation":"Open Biol 2015 Jun;5(6):150054","abstract":"Integration of an external gene into a fission yeast chromosome is useful to investigate the effect of the gene product. An easy way to knock-in a gene construct is use of an integration plasmid, which can be targeted and inserted to a chromosome through homologous recombination. Despite the advantage of integration, construction of integration plasmids is energy- and time-consuming, because there is no systematic library of integration plasmids with various promoters, fluorescent protein tags, terminators and selection markers; therefore, researchers are often forced to make appropriate ones through multiple rounds of cloning procedures. Here, we establish materials and methods to easily construct integration plasmids. We introduce a convenient cloning system based on Golden Gate DNA shuffling, which enables the connection of multiple DNA fragments at once: any kind of promoters and terminators, the gene of interest, in combination with any fluorescent protein tag genes and any selection markers. Each of those DNA fragments, called a 'module', can be tandemly ligated in the order we desire in a single reaction, which yields a circular plasmid in a one-step manner. The resulting plasmids can be integrated through standard methods for transformation. Thus, these materials and methods help easy construction of knock-in strains, and this will further increase the value of fission yeast as a model organism.","doi":"10.1098/rsob.150054","authors":"Kakui Y, Sunaga T, Arai K, Dodgson J, Ji L, Csikász-Nagy A, Carazo-Salas R, Sato M","authors_abbrev":"Kakui Y et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-06-26","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-06-27 00:20:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26433224","title":"Acentric chromosome ends are prone to fusion with functional chromosome ends through a homology-directed rearrangement.","citation":"Nucleic Acids Res 2016 Jan 08;44(1):232-44","abstract":"The centromeres of many eukaryotic chromosomes are established epigenetically on potentially variable tandem repeats; hence, these chromosomes are at risk of being acentric. We reported previously that artificially created acentric chromosomes in the fission yeast Schizosaccharomyces pombe can be rescued by end-to-end fusion with functional chromosomes. Here, we show that most acentric/functional chromosome fusion events in S. pombe cells harbouring an acentric chromosome I differed from the non-homologous end-joining-mediated rearrangements that result in deleterious dicentric fusions in normal cells, and were elicited by a previously unidentified homologous recombination (HR) event between chromosome end-associated sequences. The subtelomere repeats associated with the non-fusogenic ends were also destabilized in the surviving cells, suggesting a causal link between general subtelomere destabilization and acentric/functional chromosome fusion. A mutational analysis indicated that a non-canonical HR pathway was involved in the rearrangement. These findings are indicative of a latent mechanism that conditionally induces general subtelomere instability, presumably in the face of accidental centromere loss events, resulting in rescue of the fatal acentric chromosomes by interchromosomal HR.","doi":"10.1093/nar/gkv997","authors":"Ohno Y, Ogiyama Y, Kubota Y, Kubo T, Ishii K","authors_abbrev":"Ohno Y et al.","pubmed_publication_date":"08 Jan 2016","pubmed_entrez_date":"2015-10-04","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-10-05 00:18:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17261596","title":"Loss of the TOR kinase Tor2 mimics nitrogen starvation and activates the sexual development pathway in fission yeast.","citation":"Mol Cell Biol 2007 Apr;27(8):3154-64","abstract":"Fission yeast has two TOR (target of rapamycin) kinases, namely Tor1 and Tor2. Tor1 is required for survival under stressed conditions, proper G(1) arrest, and sexual development. In contrast, Tor2 is essential for growth. To analyze the functions of Tor2, we constructed two temperature-sensitive tor2 mutants. Interestingly, at the restrictive temperature, these mutants mimicked nitrogen starvation by arresting the cell cycle in G(1) phase and initiating sexual development. Microarray analysis indicated that expression of nitrogen starvation-responsive genes was induced extensively when Tor2 function was suppressed, suggesting that Tor2 normally mediates a signal from the nitrogen source. As with mammalian and budding yeast TOR, we find that fission yeast TOR also forms multiprotein complexes analogous to TORC1 and TORC2. The raptor homologue, Mip1, likely forms a complex predominantly with Tor2, producing TORC1. The rictor/Avo3 homologue, Ste20, and the Avo1 homologue, Sin1, appear to form TORC2 mainly with Tor1 but may also bind Tor2. The Lst8 homologue, Wat1, binds to both Tor1 and Tor2. Our analysis shows, with respect to promotion of G(1) arrest and sexual development, that the loss of Tor1 (TORC2) and the loss of Tor2 (TORC1) exhibit opposite effects. This highlights an intriguing functional relationship among TOR kinase complexes in the fission yeast Schizosaccharomyces pombe.","authors":"Matsuo T, Otsubo Y, Urano J, Tamanoi F, Yamamoto M","authors_abbrev":"Matsuo T et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-01-31","publication_year":"2007","canto_session_key":"b414bd2e9981203d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-26 17:26:05","canto_approved_date":"2024-01-03 11:22:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-26 17:25:58","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":40,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC24B10.07","SPBC32C12.02","SPBC12C2.02c","SPBC216.07c","SPAC4A8.04","SPAC630.13c","SPCC1322.13","SPAPYUG7.02c","SPAC57A7.11","SPBC106.10","SPBC428.16c","SPBC12C2.13c","SPBC1198.14c","SPBC21B10.05c","SPBC30D10.10c"],"gene_count":15,"ltp_gene_count":10,"approved_date":"2015-11-26"},{"uniquename":"PMID:2651864","title":"Transformation in fungi.","citation":"Microbiol Rev 1989 Mar;53(1):148-70","abstract":"Transformation with exogenous deoxyribonucleic acid (DNA) now appears to be possible with all fungal species, or at least all that can be grown in culture. This field of research is at present dominated by Saccharomyces cerevisiae and two filamentous members of the class Ascomycetes, Aspergillus nidulans and Neurospora crassa, with substantial contributions also from fission yeast (Schizosaccharomyces pombe) and another filamentous member of the class Ascomycetes, Podospora anserina. However, transformation has been demonstrated, and will no doubt be extensively used, in representatives of most of the main fungal classes, including Phycomycetes, Basidiomycetes (the order Agaricales and Ustilago species), and a number of the Fungi Imperfecti. The list includes a number of plant pathogens, and transformation is likely to become important in the analysis of the molecular basis of pathogenicity. Transformation may be maintained either by using an autonomously replicating plasmid as a vehicle for the transforming DNA or through integration of the DNA into the chromosomes. In S. cerevisiae and other yeasts, a variety of autonomously replicating plasmids have been used successfully, some of them designed for use as shuttle vectors for Escherichia coli as well as for yeast transformation. Suitable plasmids are not yet available for use in filamentous fungi, in which stable transformation is dependent on chromosomal integration. In Saccharomyces cerevisiae, integration of transforming DNA is virtually always by homology; in filamentous fungi, in contrast, it occurs just as frequently at nonhomologous (ectopic) chromosomal sites. The main importance of transformation in fungi at present is in connection with gene cloning and the analysis of gene function. The most advanced work is being done with S. cerevisiae, in which the virtual restriction of stable DNA integration to homologous chromosome loci enables gene disruption and gene replacement to be carried out with greater precision and efficiency than is possible in other species that show a high proportion of DNA integration events at nonhomologous (ectopic) sites. With a little more trouble, however, the methodology pioneered for S. cerevisiae can be applied to other fungi too. Transformation of fungi with DNA constructs designed for high gene expression and efficient secretion of gene products appears to have great commercial potential.","authors":"Fincham JR","authors_abbrev":"Fincham JR","pubmed_publication_date":"Mar 1989","pubmed_entrez_date":"1989-03-01","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28065315","title":"Nuclear displacement and fluorescence recovery after photobleaching (FRAP) assays to study division site placement and cytokinesis in fission yeast.","citation":"Methods Cell Biol 2017;137:341-353","abstract":"Cytokinesis is an essential cellular event that completes the cell division cycle. It begins with the assembly of an actomyosin contractile ring that undergoes constriction concomitant with the septum formation to divide the cell in two. Placement of the septum at the right position is important to ensure fidelity of the division process. In fission yeast, the medially placed nucleus is a major spatial cue to position the site of division. In this chapter, we describe a simple synthetic biology-based approach to displace the nucleus and study the consequence on division site positioning. We also describe how to perform fluorescence recovery after photobleaching to follow the dynamics of cytokinetic proteins at defined time points by live-cell microscopy.","doi":"10.1016/bs.mcb.2016.03.031","authors":"Ullal P, Bhatia P, Martin SG","authors_abbrev":"Ullal P et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-01-10","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-01-11 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10747035","title":"Chromatin binding of the fission yeast replication factor mcm4 occurs during anaphase and requires ORC and cdc18.","citation":"EMBO J 2000 Apr 03;19(7):1681-90","abstract":"We describe an in situ technique for studying the chromatin binding of proteins in the fission yeast Schizosaccharomyces pombe. After tagging the protein of interest with green fluorescent protein (GFP), chromatin-associated protein is detected by GFP fluorescence following cell permeabilization and washing with a non-ionic detergent. Cell morphology and nuclear structure are preserved in this procedure, allowing structures such as the mitotic spindle to be detected by indirect immunofluorescence. Cell cycle changes in the chromatin association of proteins can therefore be determined from individual cells in asynchronous cultures. We have applied this method to the DNA replication factor mcm4/cdc21, and find that chromatin association occurs during anaphase B, significantly earlier than is the case in budding yeast. Binding of mcm4 to chromatin requires orc1 and cdc18 (homologous to Cdc6 in budding yeast). Release of mcm4 from chromatin occurs during S phase and requires DNA replication. Upon overexpressing cdc18, we show that mcm4 is required for re-replication of the genome in the absence of mitosis and is associated with chromatin in cells undergoing re-replication.","authors":"Kearsey SE, Montgomery S, Labib K, Lindner K","authors_abbrev":"Kearsey SE et al.","pubmed_publication_date":"03 Apr 2000","pubmed_entrez_date":"2000-04-04","publication_year":"2000","canto_session_key":"b4e1296fce6fa566","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-10 10:25:43","canto_approved_date":"2020-12-04 15:15:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-05-01 12:57:57","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPBC29A10.15","SPCC16A11.17"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-06-10"},{"uniquename":"PMID:16630887","title":"Genome-wide occupancy profile of mediator and the Srb8-11 module reveals interactions with coding regions.","citation":"Mol Cell 2006 Apr 21;22(2):169-78","abstract":"Mediator exists in a free form containing the Med12, Med13, CDK8, and CycC subunits (the Srb8-11 module) and a smaller form, which lacks these four subunits and associates with RNA polymerase II (Pol II), forming a holoenzyme. We use chromatin immunoprecipitation (ChIP) and DNA microarrays to investigate genome-wide localization of Mediator and the Srb8-11 module in fission yeast. Mediator and the Srb8-11 module display similar binding patterns, and interactions with promoters and upstream activating sequences correlate with increased transcription activity. Unexpectedly, Mediator also interacts with the downstream coding region of many genes. These interactions display a negative bias for positions closer to the 5' ends of open reading frames (ORFs) and appear functionally important, because downregulation of transcription in a temperature-sensitive med17 mutant strain correlates with increased Mediator occupancy in the coding region. We propose that Mediator coordinates transcription initiation with transcriptional events in the coding region of eukaryotic genes.","authors":"Zhu X, Wirén M, Sinha I, Rasmussen NN, Linder T, Holmberg S, Ekwall K, Gustafsson CM","authors_abbrev":"Zhu X et al.","pubmed_publication_date":"21 Apr 2006","pubmed_entrez_date":"2006-04-25","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8569679","title":"Mutational analysis of the RNase-like domain in subunit 2 of fission yeast RNA polymerase II.","citation":"Mol Gen Genet 1996 Jan 15;250(1):1-6","abstract":"Local sequence similarity exists between the subunit 2 of eukaryotic RNA polymerases II and the barnase-type bacterial RNases. The RNase-like domain from the Rpb2 of Schizosaccharomyces pombe was expressed in Escherichia coli as a GST fusion protein and examined for its RNase activity. When the GST fusion protein was incubated in vitro with 32P-labeled RNA, the RNA degradation activity was less than 0.1%, if any, of the level of synthetic barnase. In order to check the in vivo function of this region, we constructed two mutant rpb2 alleles, rpb2E357A and rpb2H386L, each carrying a single amino acid substitution at the site corresponding to one of the three essential amino acid residues forming the catalytic site in barnase (mutation of barnase at the corresponding sites results in complete loss of RNase activity) and five other mutant rpb2 alleles, each carrying a single mutation at various positions within the RNase-like domain but outside the putative catalytic site for RNase activity. When these mutant rpb2 alleles were expressed in an rpb2-disrupted S. pombe strain, all the mutants grew as well as the wild-type parent and did not show any clear defective phenotypes. These results suggest either that the RNase-like domain in Rpb2 does not function as an RNase in vivo or that the RNase activity of this domain, if present at all, is not essential for cell growth.","authors":"Kawagishi-Kobayashi M, Yamamoto M, Ishihama A","authors_abbrev":"Kawagishi-Kobayashi M et al.","pubmed_publication_date":"15 Jan 1996","pubmed_entrez_date":"1996-01-15","publication_year":"1996","canto_session_key":"21f56eb78da62621","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-24 17:48:55","canto_approved_date":"2021-01-24 17:48:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-24 17:48:49","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23G3.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-01-24"},{"uniquename":"PMID:15546490","title":"Size control in growing yeast and mammalian cells.","citation":"Theor Biol Med Model 2004 Nov 16;1:12","abstract":"In a recent publication it was claimed that cultured mammalian cells, in contrast to yeasts, maintain a constant size distribution in the population without a size checkpoint. This inference may be challengeable.\n(1) It is argued that \"weak\" size control implies the existence of a checkpoint, and unfortunately the technique used by Conlon and Raff might obscure such a weak mechanism. (2) Previous investigations of size control in yeasts have shown that individual cell data, rather than means and variances of cell populations, are prerequisites for reliable interpretation. (3) No experimental data so far obtained suggest that in any cell culture a linear growth pattern in cell mass can maintain size homeostasis on its own without size control. (4) Studies on fission yeast mutants indicate that the molecular mechanisms of size control vary with genetic background, implying that no single mechanism is likely to apply to any cell type, including cultured mammalian cells, under all conditions.\nThe claim that cultured mammalian cells maintain size homeostasis without a checkpoint needs to be re-evaluated by measurements on individual cells.","authors":"Sveiczer A, Novak B, Mitchison JM","authors_abbrev":"Sveiczer A et al.","pubmed_publication_date":"16 Nov 2004","pubmed_entrez_date":"2004-11-18","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17452625","title":"Acetylation regulates tropomyosin function in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 2007 May 01;120(Pt 9):1635-45","abstract":"Tropomyosin is an evolutionarily conserved alpha-helical coiled-coil protein that promotes and maintains actin filaments. In yeast, Tropomyosin-stabilised filaments are used by molecular motors to transport cargoes or to generate motile forces by altering the dynamics of filament growth and shrinkage. The Schizosaccharomyces pombe tropomyosin Cdc8 localises to the cytokinetic actomyosin ring during mitosis and is absolutely required for its formation and function. We show that Cdc8 associates with actin filaments throughout the cell cycle and is subjected to post-translational modification that does not vary with cell cycle progression. At any given point in the cell cycle 80% of Cdc8 molecules are acetylated, which significantly enhances their affinity for actin. Reconstructions of electron microscopic images of actin-Cdc8 filaments establish that the majority of Cdc8 strands sit in the 'closed' position on actin filaments, suggesting a role in the regulation of myosin binding. We show that Cdc8 regulates the equilibrium binding of myosin to actin without affecting the rate of myosin binding. Unacetylated Cdc8 isoforms bind actin, but have a reduced ability to regulate myosin binding to actin. We conclude that although acetylation of Cdc8 is not essential, it provides a regulatory mechanism for modulating actin filament integrity and myosin function.","authors":"Skoumpla K, Coulton AT, Lehman W, Geeves MA, Mulvihill DP","authors_abbrev":"Skoumpla K et al.","pubmed_publication_date":"01 May 2007","pubmed_entrez_date":"2007-04-25","publication_year":"2007","canto_session_key":"3e3589df2ec0053d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-15 15:36:34","canto_approved_date":"2024-03-28 15:55:27","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-08-15 15:36:29","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPBC16A3.15c","SPAC4A8.15c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-08-15"},{"uniquename":"PMID:37664592","title":"Mechanism of assembly of snRNP cores assisted by ICln and the SMN complex in fission yeast.","citation":"iScience 2023 Sep 15;26(9):107604","abstract":"The spliceosomal snRNP cores, each comprised of a snRNA and a seven-membered Sm ring (D1/D2/F/E/G/D3/B), are assembled by twelve chaperoning proteins in human. However, only six assembly-assisting proteins, ICln and the SMN complex (SMN/Gemin2/Gemin6-8), have been found in  Schizosaccharomyces pombe  (Sp). Here, we used recombinant proteins to reconstitute the chaperone machinery and investigated the roles of these proteins systematically. We found that, like the human system, the assembly in  S. pombe  requires ICln and the SMN complex sequentially. However, there are several significant differences. For instance, h_F/E/G forms heterohexamers and heterotrimers, while Sp_F/E/G only forms heterohexamers; h_Gemin2 alone can bind D1/D2/F/E/G, but Sp_Gemin2 cannot. Moreover, we found that Sp_Gemin2 is essential using genetic approaches. These mechanistic studies reveal that these six proteins are necessary and sufficient for Sm core assembly at the molecular level, and enrich our understanding of the chaperone systems in species variation and evolution.","doi":"10.1016/j.isci.2023.107604","authors":"Hu Y, Hou Y, Zhou S, Wang Y, Shen C, Mu L, Su D, Zhang R","authors_abbrev":"Hu Y et al.","pubmed_publication_date":"15 Sep 2023","pubmed_entrez_date":"2023-09-04","publication_year":"2023","canto_session_key":"7ac8133e6587e8bd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-09-05 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34108240","title":"The intra-S phase checkpoint directly regulates replication elongation to preserve the integrity of stalled replisomes.","citation":"Proc Natl Acad Sci U S A 2021 Jun 15;118(24)","abstract":"DNA replication is dramatically slowed down under replication stress. The regulation of replication speed is a conserved response in eukaryotes and, in fission yeast, requires the checkpoint kinases Rad3 ATR  and Cds1 Chk2  However, the underlying mechanism of this checkpoint regulation remains unresolved. Here, we report that the Rad3 ATR -Cds1 Chk2  checkpoint directly targets the Cdc45-MCM-GINS (CMG) replicative helicase under replication stress. When replication forks stall, the Cds1 Chk2  kinase directly phosphorylates Cdc45 on the S275, S322, and S397 residues, which significantly reduces CMG helicase activity. Furthermore, in  cds1   Chk2   -mutated cells, the CMG helicase and DNA polymerases are physically separated, potentially disrupting replisomes and collapsing replication forks. This study demonstrates that the intra-S phase checkpoint directly regulates replication elongation, reduces CMG helicase processivity, prevents CMG helicase delinking from DNA polymerases, and therefore helps preserve the integrity of stalled replisomes and replication forks.","doi":"10.1073/pnas.2019183118","authors":"Liu Y, Wang L, Xu X, Yuan Y, Zhang B, Li Z, Xie Y, Yan R, Zheng Z, Ji J, Murray JM, Carr AM, Kong D","authors_abbrev":"Liu Y et al.","pubmed_publication_date":"15 Jun 2021","pubmed_entrez_date":"2021-06-10","publication_year":"2021","canto_session_key":"b5cb9923445666fc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lu Wang","canto_first_approved_date":"2021-06-30 15:13:16","canto_approved_date":"2021-06-30 15:13:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-06-25 11:29:55","canto_added_date":"2021-06-12 00:15:04","annotation_curators":[{"name":"Lu Wang","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":53,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC553.09c","SPAC17D4.02","SPBC25D12.03c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2021-06-30"},{"uniquename":"PMID:24256268","title":"A snapshot of Snf2 enzymes in fission yeast.","citation":"Biochem Soc Trans 2013 Dec;41(6):1640-7","abstract":"Eukaryotic chromatin is remodelled by the evolutionarily conserved Snf2 family of enzymes in an ATP-dependent manner. Several Snf2 enzymes are part of CRCs (chromatin remodelling complexes). In the present review we focus our attention on the functions of Snf2 enzymes and CRCs in fission yeast. We discuss their molecular mechanisms and roles and in regulating gene expression, DNA recombination, euchromatin and heterochromatin structure.","doi":"10.1042/BST20130145","authors":"Prasad P, Ekwall K","authors_abbrev":"Prasad P et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26223200","title":"Knowledge-based reasoning to annotate noncoding RNA using multi-agent system.","citation":"J Bioinform Comput Biol 2015 Dec;13(6):1550021","abstract":"Noncoding RNAs (ncRNAs) have been focus of intense research over the last few years. Since characteristics and signals of ncRNAs are not entirely known, researchers use different computational tools together with their biological knowledge to predict putative ncRNAs. In this context, this work presents ncRNA-Agents, a multi-agent system to annotate ncRNAs based on the output of different tools, using inference rules to simulate biologists' reasoning. Experiments with data from the fungus Saccharomyces cerevisiae allowed to measure the performance of ncRNA-Agents, with better sensibility, when compared to Infernal, a widely used tool for annotating ncRNA. Besides, data of the Schizosaccharomyces pombe and Paracoccidioides brasiliensis fungi identified novel putative ncRNAs, which demonstrated the usefulness of our approach. NcRNA-Agents can be be found at: http://www.biomol.unb.br/ncrna-agents.","doi":"10.1142/S0219720015500213","authors":"Arruda WC, Souza DS, Ralha CG, Walter ME, Raiol T, Brigido MM, Stadler PF","authors_abbrev":"Arruda WC et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-07-31","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-08-02 00:19:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15486101","title":"The plant-specific kinase CDKF;1 is involved in activating phosphorylation of cyclin-dependent kinase-activating kinases in Arabidopsis.","citation":"Plant Cell 2004 Nov;16(11):2954-66","abstract":"Cyclin-dependent kinases (CDKs) play essential roles in coordinate control of cell cycle progression. Activation of CDKs requires interaction with specific cyclin partners and phosphorylation of their T-loops by CDK-activating kinases (CAKs). The Arabidopsis thaliana genome encodes four potential CAKs. CAK2At (CDKD;3) and CAK4At (CDKD;2) are closely related to the vertebrate CAK, CDK7/p40MO15; they interact with cyclin H and phosphorylate CDKs, as well as the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. CAK1At (CDKF;1) shows cyclin H-independent CDK-kinase activity and can activate a heterologous CAK, Mcs6, in fission yeast. In Arabidopsis, CAK1At is a subunit of a protein complex of 130 kD, which phosphorylates the T-loop of CAK2At and CAK4At and activates the CTD-kinase activity of CAK4At in vitro and in root protoplasts. These results suggest that CAK1At is a novel CAK-activating kinase that modulates the activity of CAK2At and CAK4At, thereby controlling CDK activities and basal transcription in Arabidopsis.","authors":"Shimotohno A, Umeda-Hara C, Bisova K, Uchimiya H, Umeda M","authors_abbrev":"Shimotohno A et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-16","publication_year":"2004","canto_session_key":"1ddcc53256c55d1c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-01-19 10:48:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-21 12:18:09","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.06c","SPBC19F8.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-11-21"},{"uniquename":"PMID:21444751","title":"Microtubule stabilization in vivo by nucleation-incompetent γ-tubulin complex.","citation":"J Cell Sci 2011 Apr 15;124(Pt 8):1207-13","abstract":"Although the fission yeast Schizosaccharomyces pombe contains many of the γ-tubulin ring complex (γ-TuRC)-specific proteins of the γ-tubulin complex (γ-TuC), several questions about the organizational state and function of the fission yeast γ-TuC in vivo remain unresolved. Using 3×GFP-tagged γ-TuRC-specific proteins, we show here that γ-TuRC-specific proteins are present at all microtubule organizing centers in fission yeast and that association of γ-TuRC-specific proteins with the γ-tubulin small complex (γ-TuSC) does not depend on Mto1, which is a key regulator of the γ-TuC. Through sensitive imaging in mto1Δ mutants, in which cytoplasmic microtubule nucleation is abolished, we unexpectedly found that γ-TuC incapable of nucleating microtubules can nevertheless associate with microtubule minus-ends in vivo. The presence of γ-TuC at microtubule ends is independent of γ-TuRC-specific proteins and strongly correlates with the stability of microtubule ends. Strikingly, microtubule bundles lacking γ-TuC at microtubule ends undergo extensive treadmilling in vivo, apparently induced by geometrical constraints on plus-end growth. Our results indicate that microtubule stabilization by the γ-TuC, independently of its nucleation function, is important for maintaining the organization and dynamic behavior of microtubule arrays in vivo.","doi":"10.1242/jcs.083741","authors":"Anders A, Sawin KE","authors_abbrev":"Anders A et al.","pubmed_publication_date":"15 Apr 2011","pubmed_entrez_date":"2011-03-30","publication_year":"2011","canto_session_key":"b6c50bbff2ebe7ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-08-25 09:53:24","canto_approved_date":"2022-08-25 09:53:24","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-08-25 09:53:08","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":5,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC417.07c","SPBC902.06","SPBC365.15","SPBC211.06","SPAC806.08c","SPCC4G3.19","SPBC800.05c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2022-08-25"},{"uniquename":"PMID:25618337","title":"Fission yeast-based high-throughput screens for PKA pathway inhibitors and activators.","citation":"Methods Mol Biol 2015;1263:77-91","abstract":"Features of the fission yeast Schizosaccharomyces pombe cAMP/PKA pathway make S. pombe particularly amenable for heterologous expression of cAMP pathway proteins such as GαS subunits and their cognate adenylyl cyclases, PKA catalytic and regulatory subunits, and cyclic nucleotide phosphodiesterases. We have constructed two PKA-repressed reporters for use in high-throughput screens to detect compounds that elevate or reduce PKA activity, thus facilitating the discovery of both inhibitors and activators of these target proteins. Here, we describe steps to construct screening strains and to optimize and conduct these screens.","doi":"10.1007/978-1-4939-2269-7_6","authors":"de Medeiros AS, Kwak G, Vanderhooft J, Rivera S, Gottlieb R, Hoffman CS","authors_abbrev":"de Medeiros AS et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-01-26","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-01-28 01:15:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27852900","title":"Gradients of phosphatidylserine contribute to plasma membrane charge localization and cell polarity in fission yeast.","citation":"Mol Biol Cell 2017 Jan 01;28(1):210-220","abstract":"Surface charges at the inner leaflet of the plasma membrane may contribute to regulate the surface recruitment of key signaling factors. Phosphatidylserine (PS) is an abundant charged lipid that may regulate charge distribution in different cell types. Here we characterize the subcellular distribution and function of PS in the rod-shaped, polarized fission yeast. We find that PS preferably accumulates at cell tips and defines a gradient of negative charges along the cell surface. This polarization depends on actin-mediated endocytosis and contributes to the subcellular partitioning of charged polarity-regulating Rho GTPases like Rho1 or Cdc42 in a protein charge-dependent manner. Cells depleted of PS have altered cell dimensions and fail to properly regulate growth from the second end, suggesting a role for PS and membrane charge in polarized cell growth.","doi":"10.1091/mbc.E16-06-0353","authors":"Haupt A, Minc N","authors_abbrev":"Haupt A et al.","pubmed_publication_date":"01 Jan 2017","pubmed_entrez_date":"2016-11-18","publication_year":"2017","canto_session_key":"23dda2714be075ae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Armin Haupt","canto_first_approved_date":"2018-05-16 18:03:21","canto_approved_date":"2021-04-08 07:00:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-30 10:51:16","canto_added_date":"2016-11-19 01:15:23","annotation_curators":[{"name":"Armin Haupt","community_curator":true,"annotation_count":17,"orcid":"0000-0003-2847-0672","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.11","SPCC895.05","SPCC1919.10c","SPBC1706.01","SPBC2D10.14c","SPCC1223.06","SPAC110.03","SPAC2F7.03c","SPAC1F7.04","SPAC821.12","SPBC146.13c","SPCC970.09","SPCC1442.12"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2018-05-16"},{"uniquename":"PMID:37792890","title":"Elevated levels of sphingolipid MIPC in the plasma membrane disrupt the coordination of cell growth with cell wall formation in fission yeast.","citation":"PLoS Genet 2023 Oct;19(10):e1010987","abstract":"Coupling cell wall expansion with cell growth is a universal challenge faced by walled organisms. Mutations in Schizosaccharomyces pombe css1, which encodes a PM inositol phosphosphingolipid phospholipase C, prevent cell wall expansion but not synthesis of cell wall material. To probe how Css1 modulates cell wall formation we used classical and chemical genetics coupled with quantitative mass spectrometry. We found that elevated levels of the sphingolipid biosynthetic pathway's final product, mannosylinositol phosphorylceramide (MIPC), specifically correlated with the css1-3 phenotype. We also found that an apparent indicator of sphingolipids and a sterol biosensor accumulated at the cytosolic face of the PM at cell tips and the division site of css1-3 cells and, in accord, the PM in css1-3 was less dynamic than in wildtype cells. Interestingly, disrupting the protein glycosylation machinery recapitulated the css1-3 phenotype and led us to investigate Ghs2, a glycosylated PM protein predicted to modify cell wall material. Disrupting Ghs2 function led to aberrant cell wall material accumulation suggesting Ghs2 is dysfunctional in css1-3. We conclude that preventing an excess of MIPC in the S. pombe PM is critical to the function of key PM-localized proteins necessary for coupling growth with cell wall formation.","doi":"10.1371/journal.pgen.1010987","authors":"Willet AH, Wos M, Igarashi MG, Ren L, Turner LA, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"Oct 2023","pubmed_entrez_date":"2023-10-04","publication_year":"2023","canto_session_key":"4364335d0ce165e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2023-10-17 13:40:31","canto_approved_date":"2024-07-04 06:39:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-11 17:39:52","canto_added_date":"2023-10-04 23:25:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":52,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F3.01","SPAC20G4.07c","SPAC27F1.07","SPAC17G8.14c","SPBC19G7.05c","SPAC637.13c","SPBC119.08","SPCC794.08","SPAC19A8.04","SPAC17G8.11c","SPBC32F12.01c","SPCC11E10.02c","SPAC16.01","SPCC4F11.04c","SPAC1A6.09c","SPBC12D12.04c","SPAC1F3.02c","SPAC4G8.05","SPCC1281.01","SPAC56E4.04c","SPAC11G7.01","SPBC3E7.15c","SPCC1840.02c","SPAC821.13c","SPBC887.15c","SPAC19B12.03","SPAC1786.03","SPAC17G6.11c","SPBC30B4.01c","SPBC543.07"],"gene_count":30,"ltp_gene_count":25,"approved_date":"2023-10-17"},{"uniquename":"PMID:16098195","title":"Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90.","citation":"FEBS J 2005 Aug;272(16):4129-40","abstract":"Cdc37 is a molecular chaperone that interacts with a range of clients and co-chaperones, forming various high molecular mass complexes. Cdc37 sequence homology among species is low. High homology between yeast and metazoan proteins is restricted to the extreme N-terminal region, which is known to bind clients that are predominantly protein kinases. We show that despite the low homology, both Saccharomyces cerevisiae and human Cdc37 are able to substitute for the Schizosaccharomyces pombe protein in a strain deleted for the endogenous cdc37 gene. Expression of a construct consisting of only the N-terminal domain of S. pombe Cdc37, lacking the postulated heat-shock protein (Hsp) 90-binding and homodimerization domains, can also sustain cellular viability, indicating that Cdc37 dimerization and interactions with the cochaperone Hsp90 may not be essential for Cdc37 function in S. pombe. Biochemical investigations showed that a small proportion of total cellular Cdc37 occurs in a high molecular mass complex that also contains Hsp90. These data indicate that the N-terminal domain of Cdc37 carries out essential functions independently of the Hsp90-binding domain and dimerization of the chaperone itself.","authors":"Turnbull EL, Martin IV, Fantes PA","authors_abbrev":"Turnbull EL et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-08-16","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC9B6.10","SPAC926.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8799335","title":"Molecular cloning of GAF2, a Schizosaccharomyces pombe GATA factor, which has two zinc-finger sequences.","citation":"Biochem Mol Biol Int 1996 May;39(1):127-35","abstract":"By low stringency screening of a lambda-Shizosaccharomyces pombe genomic library, we have cloned a GATA factor homologous gene, gaf2+, within a 3.1-kb EcoRI fragment. The gaf2 ORF predicts a protein of M(r) 61 kDa consisting of intronless 564 amino acids corresponding to 1,692 bp. Gaf2 has two zinc-fingers as Urbs1 of Ustilago maydis, whereas most of fungal GATA factors have only one zinc-finger. The separation between two zinc-fingers of Gaf2 is rather long. In addition to gaf2, the sequence analysis revealed a Val-tRNA gene in the 3'-flanking region of gaf2. Northern blot analysis indicated that the gaf2 gene is transcribed constitutively irrespective of the nitrogen source in a medium.","authors":"Hoe KL, Won MS, Yoo OJ, Yoo HS","authors_abbrev":"Hoe KL et al.","pubmed_publication_date":"May 1996","pubmed_entrez_date":"1996-05-01","publication_year":"1996","canto_session_key":"1bdb389b19f988cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-07 15:19:56","canto_approved_date":"2021-01-22 15:47:28","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-01-22 15:47:21","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23E2.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-01-07"},{"uniquename":"PMID:11033806","title":"[Overexpression of the apc10+ gene in the fission yeast Schizosaccharomyces pombe can suppress temperature sensitivity of the nuc2-663 mutant,but not its sterility].","citation":"Mol Biol (Mosk) 2000;34(5):809-15","abstract":"","authors":"Grishchuk EL, Frolov DIu, Savchenko GV","authors_abbrev":"Grishchuk EL et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-10-18","publication_year":"2000","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17C9.01c","SPBC1A4.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:25658828","title":"Single site suppressors of a fission yeast temperature-sensitive mutant in cdc48 identified by whole genome sequencing.","citation":"PLoS One 2015;10(2):e0117779","abstract":"The protein called p97 in mammals and Cdc48 in budding and fission yeast is a homo-hexameric, ring-shaped, ubiquitin-dependent ATPase complex involved in a range of cellular functions, including protein degradation, vesicle fusion, DNA repair, and cell division. The cdc48+ gene is essential for viability in fission yeast, and point mutations in the human orthologue have been linked to disease. To analyze the function of p97/Cdc48 further, we performed a screen for cold-sensitive suppressors of the temperature-sensitive cdc48-353 fission yeast strain. In total, 29 independent pseudo revertants that had lost the temperature-sensitive growth defect of the cdc48-353 strain were isolated. Of these, 28 had instead acquired a cold-sensitive phenotype. Since the suppressors were all spontaneous mutants, and not the result of mutagenesis induced by chemicals or UV irradiation, we reasoned that the genome sequences of the 29 independent cdc48-353 suppressors were most likely identical with the exception of the acquired suppressor mutations. This prompted us to test if a whole genome sequencing approach would allow us to map the mutations. Indeed genome sequencing unambiguously revealed that the cold-sensitive suppressors were all second site intragenic cdc48 mutants. Projecting these onto the Cdc48 structure revealed that while the original temperature-sensitive G338D mutation is positioned near the central pore in the hexameric ring, the suppressor mutations locate to subunit-subunit and inter-domain boundaries. This suggests that Cdc48-353 is structurally compromized at the restrictive temperature, but re-established in the suppressor mutants. The last suppressor was an extragenic frame shift mutation in the ufd1 gene, which encodes a known Cdc48 co-factor. In conclusion, we show, using a novel whole genome sequencing approach, that Cdc48-353 is structurally compromized at the restrictive temperature, but stabilized in the suppressors.","doi":"10.1371/journal.pone.0117779","authors":"Marinova IN, Engelbrecht J, Ewald A, Langholm LL, Holmberg C, Kragelund BB, Gordon C, Nielsen O, Hartmann-Petersen R","authors_abbrev":"Marinova IN et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-02-07","publication_year":"2015","canto_session_key":"16d769aa2fc305a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_first_approved_date":"2015-07-20 13:37:48","canto_approved_date":"2022-08-03 11:15:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-19 05:38:28","canto_added_date":"2015-02-08 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1565.08","SPBC16A3.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-07-20"},{"uniquename":"PMID:22164259","title":"The global transcriptional response of fission yeast to hydrogen sulfide.","citation":"PLoS One 2011;6(12):e28275","abstract":"Hydrogen sulfide (H(2)S) is a newly identified member of the small family of gasotransmitters that are endogenous gaseous signaling molecules that have a fundamental role in human biology and disease. Although it is a relatively recent discovery and the mechanism of H(2)S activity is not completely understood, it is known to be involved in a number of cellular processes; H(2)S can affect ion channels, transcription factors and protein kinases in mammals.\nIn this paper, we have used fission yeast as a model organism to study the global gene expression profile in response to H(2)S by microarray. We initially measured the genome-wide transcriptional response of fission yeast to H(2)S. Through the functional classification of genes whose expression profile changed in response to H(2)S, we found that H(2)S mainly influences genes that encode putative or known stress proteins, membrane transporters, cell cycle/meiotic proteins, transcription factors and respiration protein in the mitochondrion. Our analysis showed that there was a significant overlap between the genes affected by H(2)S and the stress response. We identified that the target genes of the MAPK pathway respond to H(2)S; we also identified that a number of transporters respond to H(2)S, these include sugar/carbohydrate transporters, ion transporters, and amino acid transporters. We found many mitochondrial genes to be down regulated upon H(2)S treatment and that H(2)S can reduce mitochondrial oxygen consumption.\nThis study identifies potential molecular targets of the signaling molecule H(2)S in fission yeast and provides clues about the identity of homologues human proteins and will further the understanding of the cellular role of H(2)S in human diseases.","doi":"10.1371/journal.pone.0028275","authors":"Jia X, He W, Murchie AI, Chen D","authors_abbrev":"Jia X et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-12-14","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29774234","title":"The fission yeast Stn1-Ten1 complex limits telomerase activity via its SUMO-interacting motif and promotes telomeres replication.","citation":"Sci Adv 2018 May;4(5):eaar2740","abstract":"Mammalian CST (CTC1-STN1-TEN1) complex fulfills numerous functions including rescue of the stalled replication forks and termination of telomerase action. In fission yeast lacking the CTC1 ortholog, the Stn1-Ten1 complex restricts telomerase action via its sumoylation-mediated interaction with Tpz1 TPP1 . We identify a small ubiquitin-like modifier (SUMO)-interacting motif (SIM) in the carboxyl-terminal part of Stn1 and show that this domain is crucial for SUMO and Tpz1-SUMO interactions. Point mutations in the SIM (Stn1-226) lead to telomere elongation, impair Stn1-Ten1 recruitment to telomeres, and enhance telomerase binding, revealing that Stn1 SIM domain contributes to the inhibition of telomerase activity at chromosome ends. Our results suggest that Stn1-Ten1 promotes DNA synthesis at telomeres to limit single-strand DNA accumulation. We further demonstrate that Stn1 functions in the replication of telomeric and subtelomeric regions in a Taz1-independent manner. Genetic analysis reveals that misregulation of origin firing and/or telomerase inhibition circumvents the replication defects of the  stn1-226  mutant. Together, our results show that the Stn1-Ten1 complex has a dual function at telomeres by limiting telomerase action and promoting chromosome end replication.","doi":"10.1126/sciadv.aar2740","authors":"Matmati S, Vaurs M, Escandell JM, Maestroni L, Nakamura TM, Ferreira MG, Géli V, Coulon S","authors_abbrev":"Matmati S et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-05-19","publication_year":"2018","canto_session_key":"ff16cae20b63db89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Stéphane COULON","canto_first_approved_date":"2018-06-08 12:22:50","canto_approved_date":"2025-09-03 14:59:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-25 13:21:13","canto_added_date":"2018-05-20 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":66,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Stéphane COULON","community_curator":true,"annotation_count":12,"orcid":"0000-0001-8090-914X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.13c","SPAC16A10.07c","SPAC6F6.16c","SPAC6F6.17","SPBC365.06","SPBC1778.02","SPCC1393.14","SPBC29A10.05","SPAC644.14c","SPAC3H5.06c","SPBC2D10.13","SPBC409.12c"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2018-06-08"},{"uniquename":"EMBL:AU010927","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29423860","title":"Schizosaccharomyces pombe Biotechnological Applications in Winemaking.","citation":"Methods Mol Biol 2018;1721:217-226","abstract":"The traditional way of producing wine is through the use of Saccharomyces cerevisiae in order to convert glucose and fructose into alcohol. In the case of red wines, after this alcoholic fermentation lactic bacteria Oenococus oeni is used to stabilize wine from a microbiological point of view by converting malic acid into lactic acid that it is not a microbiological substract. The yeast species Schizosaccharomyces pombe was traditionally considered spoilage yeast. Nevertheless, during the last decade it started to be used due to its unique malic acid deacidification ability to reduce the harsh acidity of wines from northern Europe, by converting malic acid to ethanol and CO 2  without producing lactic acid as lactic bacteria does. Additionally, during the last years, S. pombe has started to be used to solve the problems of modern winemaking industry such as increasing food quality or food safety. Some of those new uses, different from its traditional malic acid deacidification, are: high autolytic polysaccharides release, gluconic acid reduction, urease activity that make impossible ethyl carbamate (toxic compound) formation, high pyruvic acid production, that is related to color improvement, and removing lactic bacteria subtracts while avoiding biogenic amines (toxic compounds such as histamine) formation.","doi":"10.1007/978-1-4939-7546-4_19","authors":"Benito Á, Calderón F, Benito S","authors_abbrev":"Benito Á et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41824417","title":"Nucleosome positioning shapes cryptic antisense transcription.","citation":"PLoS Genet 2026 Mar 13;22(3):e1012078","abstract":"Maintaining transcriptional fidelity is essential for precise gene regulation and genome stability. Despite this, cryptic antisense transcription, occurring opposite to canonical coding sequences, is a pervasive feature across all domains of life. How such potentially harmful cryptic sites are regulated remains incompletely understood. Here, we show that nucleosome arrays within gene bodies play a key role in suppressing cryptic transcription. Using the fission yeast Schizosaccharomyces pombe as a model, we demonstrate that the CHD-family chromatin remodeler Hrp3 coordinates with the transcription elongation machinery, via the transcriptional regulator Prf1/RTF1, to position nucleosomes at sites of cryptic transcription initiation within gene bodies. In the absence of Hrp3, AT-rich sequences within gene bodies lose nucleosome occupancy, exposing promoter-like sequences that drive cryptic initiation. While cryptic transcription is generally detrimental, we identify a subset of antisense transcripts that encode critical meiotic genes, suggesting that cryptic transcription can also serve as a source of regulatory innovation. These findings define an elongation‑coupled chromatin pathway that preserves transcriptional fidelity and reveal how nucleosome remodeling shapes antisense transcription, cellular homeostasis, and adaptive potential.","doi":"10.1371/journal.pgen.1012078","authors":"Kok JY, Harvey ZH, Axelsson E, Berger F","authors_abbrev":"Kok JY et al.","pubmed_publication_date":"13 Mar 2026","pubmed_entrez_date":"2026-03-13","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733394","title":"Genetic Interaction Mapping in  Schizosaccharomyces pombe  Using the Pombe Epistasis Mapper (PEM) System and a ROTOR HDA Colony Replicating Robot in a 1536 Array Format.","citation":"Cold Spring Harb Protoc 2018 Feb 01;2018(2)","abstract":"This protocol describes an optimized high-throughput procedure for generating double deletion mutants in  Schizosaccharomyces pombe  using the colony replicating robot ROTOR HDA and the PEM (pombe epistasis mapper) system. The method is based on generating high-density colony arrays (1536 colonies per agar plate) and passaging them through a series of antidiploid and mating-type selection (ADS-MTS) and double-mutant selection (DMS) steps. Detailed program parameters for each individual replication step are provided. Using this procedure, batches of 25 or more screens can be routinely performed.","doi":"10.1101/pdb.prot091975","authors":"Roguev A, Xu J, Krogan N","authors_abbrev":"Roguev A et al.","pubmed_publication_date":"01 Feb 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38399762","title":"Identification of Flo11-like Adhesin in  Schizosaccharomyces pombe  and the Mechanism of Small-Molecule Compounds Mediating Biofilm Formation in Yeasts.","citation":"Microorganisms 2024 Feb 09;12(2)","abstract":"Fungal infection is initiated by the adhesion of pathogens to biotic and abiotic surfaces, with various manifestations including biofilm formation and invasive growth, etc. A previous report, though devoid of functional data, speculated that the  Schizosaccharomyces pombe  glycoprotein SPBPJ4664.02 could be the homology of  Saccharomyces cerevisiae  Flo11. Here, our studies with  S. pombe  substantiated the previously proposed speculation by (1) the deletion of  SPBPJ4664.02  attenuated biofilm formation and invasive growth in  S. pombe ; (2) the  S. pombe 's lack of  SPBPJ4664.02  could be complemented by expressing  S. cerevisiae flo11 . Furthermore, indole-3-acetic acid (IAA) and dodecanol were examined in  S. pombe  for their respective effects on biofilm formation. IAA and dodecanol at high concentrations could inhibit biofilm formation, whereas opposing effects were observed with low concentrations of these molecules. Mechanism studies with the  SPBPJ4664.02 Δ and  SPBPJ4664.02 Δ/ flo11  OE  versus the wild type have demonstrated that IAA or dodecanol might exert regulatory effects downstream of SPBPJ4664.02 in the signaling pathway for biofilm formation. Moreover, our research extrapolated to  Candida albicans  has pinpointed that IAA inhibited biofilm formation at high concentrations, consistent with the transcriptional downregulation of the biofilm-related genes. Dodecanol suppressed  C. albicans  biofilm formation at all the concentrations tested, in accord with the downregulation of biofilm-related transcripts.","doi":"10.3390/microorganisms12020358","authors":"Zhang YG, Zhang T, Lin L","authors_abbrev":"Zhang YG et al.","pubmed_publication_date":"09 Feb 2024","pubmed_entrez_date":"2024-02-24","publication_year":"2024","canto_session_key":"f30e4e8e80944595","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-29 12:34:01","canto_approved_date":"2024-02-29 12:34:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-29 12:33:54","canto_added_date":"2024-02-25 00:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-02-29"},{"uniquename":"PMID:20233458","title":"Analysis of DNA strand-specific differential expression with high density tiling microarrays.","citation":"BMC Bioinformatics 2010 Mar 17;11:136","abstract":"DNA microarray technology allows the analysis of genome structure and dynamics at genome-wide scale. Expression microarrays (EMA) contain probes for annotated open reading frames (ORF) and are widely used for the analysis of differential gene expression. By contrast, tiling microarrays (TMA) have a much higher probe density and provide unbiased genome-wide coverage. The purpose of this study was to develop a protocol to exploit the high resolution of TMAs for quantitative measurement of DNA strand-specific differential expression of annotated and non-annotated transcripts.\nWe extensively filtered probes present in Affymetrix Genechip Yeast Genome 2.0 expression and GeneChip S. pombe 1.0FR tiling microarrays to generate custom Chip Description Files (CDF) in order to compare their efficiency. We experimentally tested the potential of our approach by measuring the differential expression of 4904 genes in the yeast Schizosaccharomyces pombe growing under conditions of oxidative stress. The results showed a Pearson correlation coefficient of 0.943 between both platforms, indicating that TMAs are as reliable as EMAs for quantitative expression analysis. A significant advantage of TMAs over EMAs is the possibility of detecting non-annotated transcripts generated only under specific physiological conditions. To take full advantage of this property, we have used a target-labelling protocol that preserves the original polarity of the transcripts and, therefore, allows the strand-specific differential expression of non-annotated transcripts to be determined. By using a segmentation algorithm prior to generating the corresponding custom CDFs, we identified and quantitatively measured the expression of 510 transcripts longer than 180 nucleotides and not overlapping previously annotated ORFs that were differentially expressed at least 2-fold under oxidative stress.\nWe show that the information derived from TMA hybridization can be processed simultaneously for high-resolution qualitative and quantitative analysis of the differential expression of well-characterized genes and of previously non-annotated and antisense transcripts. The consistency of the performance of TMA, their genome-wide coverage and adaptability to updated genome annotations, and the possibility of measuring strand-specific differential expression makes them a tool of choice for the analysis of gene expression in any organism for which TMA platforms are available.","doi":"10.1186/1471-2105-11-136","authors":"Quintales L, Sánchez M, Antequera F","authors_abbrev":"Quintales L et al.","pubmed_publication_date":"17 Mar 2010","pubmed_entrez_date":"2010-03-18","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28869610","title":"Mutations in ACTRT1 and its enhancer RNA elements lead to aberrant activation of Hedgehog signaling in inherited and sporadic basal cell carcinomas.","citation":"Nat Med 2017 Oct;23(10):1226-1233","abstract":"Basal cell carcinoma (BCC), the most common human cancer, results from aberrant activation of the Hedgehog signaling pathway. Although most cases of BCC are sporadic, some forms are inherited, such as Bazex-Dupré-Christol syndrome (BDCS)-a cancer-prone genodermatosis with an X-linked, dominant inheritance pattern. We have identified mutations in the ACTRT1 gene, which encodes actin-related protein T1 (ARP-T1), in two of the six families with BDCS that were examined in this study. High-throughput sequencing in the four remaining families identified germline mutations in noncoding sequences surrounding ACTRT1. These mutations were located in transcribed sequences encoding enhancer RNAs (eRNAs) and were shown to impair enhancer activity and ACTRT1 expression. ARP-T1 was found to directly bind to the GLI1 promoter, thus inhibiting GLI1 expression, and loss of ARP-T1 led to activation of the Hedgehog pathway in individuals with BDCS. Moreover, exogenous expression of ACTRT1 reduced the in vitro and in vivo proliferation rates of cell lines with aberrant activation of the Hedgehog signaling pathway. In summary, our study identifies a disease mechanism in BCC involving mutations in regulatory noncoding elements and uncovers the tumor-suppressor properties of ACTRT1.","doi":"10.1038/nm.4368","authors":"Bal E, Park HS, Belaid-Choucair Z, Kayserili H, Naville M, Madrange M, Chiticariu E, Hadj-Rabia S, Cagnard N, Kuonen F, Bachmann D, Huber M, Le Gall C, Côté F, Hanein S, Rosti RÖ, Aslanger AD, Waisfisz Q, Bodemer C, Hermine O, Morice-Picard F, Labeille B, Caux F, Mazereeuw-Hautier J, Philip N, Levy N, Taieb A, Avril MF, Headon DJ, Gyapay G, Magnaldo T, Fraitag S, Crollius HR, Vabres P, Hohl D, Munnich A, Smahi A","authors_abbrev":"Bal E et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-09-05","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9843577","title":"The cdr2(+) gene encodes a regulator of G2/M progression and cytokinesis in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1998 Dec;9(12):3399-415","abstract":"Schizosaccharomyces pombe cells respond to nutrient deprivation by altering G2/M cell size control. The G2/M transition is controlled by activation of the cyclin-dependent kinase Cdc2p. Cdc2p activation is regulated both positively and negatively. cdr2(+) was identified in a screen for regulators of mitotic control during nutrient deprivation. We have cloned cdr2(+) and have found that it encodes a putative serine-threonine protein kinase that is related to Saccharomyces cerevisiae Gin4p and S. pombe Cdr1p/Nim1p. cdr2(+) is not essential for viability, but cells lacking cdr2(+) are elongated relative to wild-type cells, spending a longer period of time in G2. Because of this property, upon nitrogen deprivation cdr2(+) mutants do not arrest in G1, but rather undergo another round of S phase and arrest in G2 from which they are able to enter a state of quiescence. Genetic evidence suggests that cdr2(+) acts as a mitotic inducer, functioning through wee1(+), and is also important for the completion of cytokinesis at 36 degrees C. Defects in cytokinesis are also generated by the overproduction of Cdr2p, but these defects are independent of wee1(+), suggesting that cdr2(+) encodes a second activity involved in cytokinesis.","authors":"Breeding CS, Hudson J, Balasubramanian MK, Hemmingsen SM, Young PG, Gould KL","authors_abbrev":"Breeding CS et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1998-12-08","publication_year":"1998","canto_session_key":"9a207bd4727d5b29","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-11-05 15:17:49","canto_approved_date":"2025-09-04 12:44:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-05 15:17:42","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPBC11B10.09","SPCC18B5.03","SPBC582.03","SPAC24H6.05"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-11-05"},{"uniquename":"PMID:28536259","title":"Differential functional regulation of protein kinase C (PKC) orthologs in fission yeast.","citation":"J Biol Chem 2017 Jul 07;292(27):11374-11387","abstract":"The two PKC orthologs Pck1 and Pck2 in the fission yeast  Schizosaccharomyces pombe  operate in a redundant fashion to control essential functions, including morphogenesis and cell wall biosynthesis, as well as the activity of the cell integrity pathway and its core element, the MAPK Pmk1. We show here that, despite the strong structural similarity and functional redundancy of these two enzymes, the mechanisms regulating their maturation, activation, and stabilization have a remarkably distinct biological impact on both kinases. We found that, in contrast to Pck2, putative  in vivo  phosphorylation of Pck1 within the conserved activation loop, turn, and hydrophobic motifs is essential for Pck1 stability and biological functions. Constitutive Pck activation promoted dephosphorylation and destabilization of Pck2, whereas it enhanced Pck1 levels to interfere with proper downstream signaling to the cell integrity pathway via Pck2. Importantly, although catalytic activity was essential for Pck1 function, Pck2 remained partially functional independent of its catalytic activity. Our findings suggest that early divergence from a common ancestor in fission yeast involved important changes in the mechanisms regulating catalytic activation and stability of PKC family members to allow for flexible and dynamic control of downstream functions, including MAPK signaling.","doi":"10.1074/jbc.M117.786087","authors":"Madrid M, Vázquez-Marín B, Soto T, Franco A, Gómez-Gil E, Vicente-Soler J, Gacto M, Pérez P, Cansado J","authors_abbrev":"Madrid M et al.","pubmed_publication_date":"07 Jul 2017","pubmed_entrez_date":"2017-05-25","publication_year":"2017","canto_session_key":"242f67b63e305a4c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-05-27 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.04","SPAC16.01","SPBC12D12.04c","SPAC17G8.14c","SPCC576.15c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:14704357","title":"Domainal organization of the lower eukaryotic homologs of the yeast RNA polymerase II core subunit Rpb7 reflects functional conservation.","citation":"Nucleic Acids Res 2004;32(1):201-10","abstract":"The subcomplex of Rpb4 and Rpb7 subunits of RNA pol II in Saccharomyces cerevisiae is known to be an important determinant of transcription under a variety of physiological stresses. In S.cerevisiae, RPB7 is essential for cell viability while rpb4 null strains are temperature sensitive at low and high temperatures. The rpb4 null strain also shows defect in sporulation and a predisposed state of pseudohyphal growth. We show here that, apart from S.cerevisiae Rpb7, the Rpb7 homologs from other lower eukaryotes like Schizosaccharomyces pombe, Candida albicans and Dictyostelium discoideum can complement for the absence of S.cerevisiae RPB7. This is the first report where we have shown that both the C.albicans and D.discoideum homologs are functional orthologs of the yeast RPB7. We also show that high expression levels of S.cerevisiae RPB7 and its homologs rescue the sporulation defect of rpb4 homozygous null diploids, but only some of them cause significant enhancement of the pseudohyphal phenotype. Structural modeling of Rpb7 and its homologs show a high degree of conservation in the overall structure. This study indicates a structural and functional conservation of different Rpb7 across species and also a conserved role of Rpb7 in the subcomplex with respect to nutritional stress.","authors":"Singh SR, Rekha N, Pillai B, Singh V, Naorem A, Sampath V, Srinivasan N, Sadhale PP","authors_abbrev":"Singh SR et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-01-06","publication_year":"2004","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3531364","title":"[Cadmium binding peptides in fission yeast].","citation":"Seikagaku 1986 Mar;58(3):182-7","abstract":"","authors":"Murasugi A","authors_abbrev":"Murasugi A","pubmed_publication_date":"Mar 1986","pubmed_entrez_date":"1986-03-01","publication_year":"1986","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7957061","title":"Fission yeast cut3 and cut14, members of a ubiquitous protein family, are required for chromosome condensation and segregation in mitosis.","citation":"EMBO J 1994 Oct 17;13(20):4938-52","abstract":"Fission yeast temperature-sensitive mutants cut3-477 and cut14-208 fail to condense chromosomes but small portions of the chromosomes can separate along the spindle during mitosis, producing phi-shaped chromosomes. Septation and cell division occur in the absence of normal nuclear division, causing the cut phenotype. Fluorescence in situ hybridization demonstrated that the contraction of the chromosome arm during mitosis was defective. Mutant chromosomes are apparently not rigid enough to be transported poleward by the spindle. Loss of the cut3 protein by gene disruption fails to maintain the nuclear chromatin architecture even in interphase. Both cut3 and cut14 proteins contain a putative nucleoside triphosphate (NTP)-binding domain and belong to the same ubiquitous protein family which includes the budding yeast Smc1 protein. The cut3 mutant was suppressed by an increase in the cut14+ gene dosage. The cut3 protein, having the highest similarity to the mouse protein, is localized in the nucleus throughout the cell cycle. Plasmids carrying the DNA topoisomerase I gene partly suppressed the temperature sensitive phenotype of cut3-477, suggesting that the cut3 protein might be involved in chromosome DNA topology.","authors":"Saka Y, Sutani T, Yamashita Y, Saitoh S, Takeuchi M, Nakaseko Y, Yanagida M","authors_abbrev":"Saka Y et al.","pubmed_publication_date":"17 Oct 1994","pubmed_entrez_date":"1994-10-17","publication_year":"1994","canto_session_key":"384f03fb73e35a13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-03 14:04:46","canto_approved_date":"2026-01-29 14:59:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-03 16:21:00","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.03c","SPBP4H10.06c","SPBC1703.14c","SPBC146.03c","SPCC5E4.04"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-06-03"},{"uniquename":"PMID:21976488","title":"Implications for proteasome nuclear localization revealed by the structure of the nuclear proteasome tether protein Cut8.","citation":"Proc Natl Acad Sci U S A 2011 Oct 11;108(41):16950-5","abstract":"Degradation of nuclear proteins by the 26S proteasome is essential for cell viability. In yeast, the nuclear envelope protein Cut8 mediates nuclear proteasomal sequestration by an uncharacterized mechanism. Here we describe structures of Schizosaccharomyces pombe Cut8, which shows that it contains a unique, modular fold composed of an extended N-terminal, lysine-rich segment that when ubiquitinated binds the proteasome, a dimer domain followed by a six-helix bundle connected to a flexible C tail. The Cut8 six-helix bundle shows structural similarity to 14-3-3 phosphoprotein-binding domains, and binding assays show that this domain is necessary and sufficient for liposome and cholesterol binding. Moreover, specific mutations in the 14-3-3 regions corresponding to putative cholesterol recognition/interaction amino acid consensus motifs abrogate cholesterol binding. In vivo studies confirmed that the 14-3-3 region is necessary for Cut8 membrane localization and that dimerization is critical for its function. Thus, the data reveal the Cut8 organization at the nuclear envelope. Reconstruction of Cut8 evolution suggests that it was present in the last common ancestor of extant eukaryotes and accordingly that nuclear proteasomal sequestration is an ancestral eukaryotic feature. The importance of Cut8 for cell viability and its absence in humans suggests it as a possible target for the development of specific chemotherapeutics against invasive fungal infections.","doi":"10.1073/pnas.1103617108","authors":"Takeda K, Tonthat NK, Glover T, Xu W, Koonin EV, Yanagida M, Schumacher MA","authors_abbrev":"Takeda K et al.","pubmed_publication_date":"11 Oct 2011","pubmed_entrez_date":"2011-10-07","publication_year":"2011","canto_session_key":"16802f31036c5732","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-05-26 16:55:23","canto_approved_date":"2022-07-26 20:44:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-06 14:01:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-26"},{"uniquename":"PMID:18094750","title":"Bub1 is a fission yeast kinetochore scaffold protein, and is sufficient to recruit other spindle checkpoint proteins to ectopic sites on chromosomes.","citation":"PLoS One 2007 Dec 19;2(12):e1342","abstract":"The spindle checkpoint delays anaphase onset until all chromosomes have attached in a bi-polar manner to the mitotic spindle. Mad and Bub proteins are recruited to unattached kinetochores, and generate diffusible anaphase inhibitors. Checkpoint models propose that Mad1 and Bub1 act as stable kinetochore-bound scaffolds, to enhance recruitment of Mad2 and Mad3/BubR1, but this remains untested for Bub1. Here, fission yeast FRAP experiments confirm that Bub1 stably binds kinetochores, and by tethering Bub1 to telomeres we demonstrate that it is sufficient to recruit anaphase inhibitors in a kinase-independent manner. We propose that the major checkpoint role for Bub1 is as a signalling scaffold.","authors":"Rischitor PE, May KM, Hardwick KG","authors_abbrev":"Rischitor PE et al.","pubmed_publication_date":"19 Dec 2007","pubmed_entrez_date":"2007-12-21","publication_year":"2007","canto_session_key":"ab2b489e115feb73","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41091213","title":"Phosphorylation as a regulatory mechanism of HP1 protein multifunctionality.","citation":"Chromosoma 2025 Oct 15;134(1):9","abstract":"The Heterochromatin Protein 1 (HP1) family proteins are key regulators of chromatin structure and genome function, acting as \"reader\" proteins that recognize and bind to histone H3 lysine 9 methylation (H3K9me). Beyond their canonical role in heterochromatin formation and transcriptional repression, HP1 proteins exhibit functional versatility, participating in transcriptional activation, RNA processing, DNA repair, and chromosome segregation. This multifunctionality is mediated partially by post-translational modifications (PTMs), with phosphorylation emerging as a central regulatory mechanism. This review explores the diverse effects of HP1 phosphorylation on protein function and chromatin interactions, focusing on Drosophila melanogaster HP1a and its orthologs, mammalian HP1α and S. pombe Swi6. Phosphorylation in the N-terminal tail enhances HP1's affinity for H3K9me, promoting transcriptional silencing. Mitotic phosphorylation of serine residues in the hinge region, regulated by kinases such as AURKB and NDR1/2, leads to chromatin release and relocalization to the kinetochore, enabling proper chromosome segregation. Additionally, phosphorylation modulates HP1 phase separation dynamics, influencing nuclear compartmentalization and chromatin condensation. These findings highlight phosphorylation as a versatile molecular switch that enables HP1 proteins to transition between structural and regulatory roles, contributing to their evolutionary conserved multifunctionality in genome regulation and cell division. Further investigation into HP1 phosphorylation across species and contexts is essential to fully understand its contributions to chromatin biology.","doi":"10.1007/s00412-025-00838-0","authors":"Walts JC, Riddle NC","authors_abbrev":"Walts JC et al.","pubmed_publication_date":"15 Oct 2025","pubmed_entrez_date":"2025-10-15","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-10-15 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36825467","title":"Shotgun knockdown of RNA by CRISPR-Cas13d in fission yeast.","citation":"J Cell Sci 2023 Mar 15;136(6)","abstract":"The CRISPR-Cas13d system has a single small effector protein that targets RNA and does not require the presence of a protospacer flanking site in the targeted transcript. These features make CRISPR-Cas13d an attractive system for RNA manipulation. Here, we report the successful implementation of the CRISPR-Cas13d system in fission yeast for RNA knockdown. A high effectiveness of the CRISPR-Cas13d system was ensured by using an array of CRISPR RNAs (crRNAs) that are flanked by two self-cleaving ribozymes and are expressed from an RNA polymerase II promoter. Given the repressible nature of the promoter, RNA knockdown by the CRISPR-Cas13d system is reversible. Moreover, using the CRISPR-Cas13d system, we identified an effective crRNA array targeting the transcript of gfp and the effectiveness was demonstrated by successful knockdown of the transcripts of noc4-gfp, bub1-gfp and ade6-gfp. In principle, the effective GFP crRNA array allows knockdown of any transcript carrying the GFP sequences. This new CRISPR-Cas13d-based toolkit is expected to have a wide range of applications in many aspects of biology, including dissection of gene function and visualization of RNA.","doi":"10.1242/jcs.260769","authors":"Chen Z, Zheng S, Fu C","authors_abbrev":"Chen Z et al.","pubmed_publication_date":"15 Mar 2023","pubmed_entrez_date":"2023-02-24","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-02-25 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29343550","title":"Cdk1-dependent phosphoinhibition of a formin-F-BAR interaction opposes cytokinetic contractile ring formation.","citation":"Mol Biol Cell 2018 Mar 15;29(6):713-721","abstract":"In  Schizosaccharomyces pombe , cytokinesis requires the assembly and constriction of an actomyosin-based contractile ring (CR). A single essential formin, Cdc12, localizes to the cell middle upon mitotic onset and nucleates the F-actin of the CR. Cdc12 medial recruitment is mediated in part by its direct binding to the F-BAR scaffold Cdc15. Given that Cdc12 is hyperphosphorylated in M phase, we explored whether Cdc12 phosphoregulation impacts its association with Cdc15 during mitosis. We found that Cdk1, a major mitotic kinase, phosphorylates Cdc12 on six N-terminal residues near the Cdc15-binding site, and phosphorylation on these sites inhibits its interaction with the Cdc15 F-BAR domain. Consistent with this finding, a  cdc12  mutant with all six Cdk1 sites changed to phosphomimetic residues ( cdc12-6D ) displays phenotypes similar to  cdc12-P31A , in which the Cdc15-binding motif is disrupted; both show reduced Cdc12 at the CR and delayed CR formation. Together, these results indicate that Cdk1 phosphorylation of formin Cdc12 antagonizes its interaction with Cdc15 and thereby opposes Cdc12's CR localization. These results are consistent with a general role for Cdk1 in inhibiting cytokinesis until chromosome segregation is complete.","doi":"10.1091/mbc.E17-11-0646","authors":"Willet AH, Bohnert KA, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"15 Mar 2018","pubmed_entrez_date":"2018-01-19","publication_year":"2018","canto_session_key":"1068c5e5c8e4b6df","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2018-01-31 15:15:43","canto_approved_date":"2026-02-14 09:15:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-22 21:33:41","canto_added_date":"2018-01-20 01:15:17","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":29,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.05c","SPAC1782.09c","SPAC15A10.08","SPBC11B10.09","SPCC4B3.15","SPAC1F5.04c","SPCC645.05c","SPAC4F8.13c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2018-01-31"},{"uniquename":"PMID:9398685","title":"Identification of a second myosin-II in Schizosaccharomyces pombe: Myp2p is conditionally required for cytokinesis.","citation":"Mol Biol Cell 1997 Dec;8(12):2693-705","abstract":"As in many eukaryotic cells, fission yeast cytokinesis depends on the assembly of an actin ring. We cloned myp2(+), a myosin-II in Schizosaccharomyces pombe, conditionally required for cytokinesis. myp2(+), the second myosin-II identified in S. pombe, does not completely overlap in function with myo2(+). The catalytic domain of Myp2p is highly homologous to known myosin-IIs, and phylogenetic analysis places Myp2p in the myosin-II family. The Myp2p sequence contains well-conserved ATP- and actin-binding motifs, as well as two IQ motifs. However, the tail sequence is unusual, since it is predicted to form two long coiled-coils separated by a stretch of sequence containing 19 prolines. Disruption of myp2(+) is not lethal but under nutrient limiting conditions cells lacking myp2(+) function are multiseptated, elongated, and branched, indicative of a defect in cytokinesis. The presence of salt enhances these morphological defects. Additionally, Deltamyp2 cells are cold sensitive in high salt, failing to form colonies at 17 degrees C. Thus, myp2(+) is required under conditions of stress, possibly linking extracellular growth conditions to efficient cytokinesis and cell growth. GFP-Myp2p localizes to a ring in the middle of late mitotic cells, consistent with a role in cytokinesis. Additionally, we constructed double mutants of Deltamyp2 with temperature-sensitive mutant strains defective in cytokinesis. We observed synthetic lethal interactions between Deltamyp2 and three alleles of cdc11ts, as well as more modest synthetic interactions with cdc14ts and cdc16ts, implicating myp2(+) function for efficient cytokinesis under normal conditions.","authors":"Bezanilla M, Forsburg SL, Pollard TD","authors_abbrev":"Bezanilla M et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1997-12-17","publication_year":"1997","canto_session_key":"b787234f0fe60f52","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-09-28 10:08:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-09-28 10:08:24","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.11c","SPAC4A8.05c","SPAC6F6.08c","SPBC24C6.07"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-09-28"},{"uniquename":"PMID:17722984","title":"A discrete class of intergenic DNA dictates meiotic DNA break hotspots in fission yeast.","citation":"PLoS Genet 2007 Aug;3(8):e141","abstract":"Meiotic recombination is initiated by DNA double-strand breaks (DSBs) made by Spo11 (Rec12 in fission yeast), which becomes covalently linked to the DSB ends. Like recombination events, DSBs occur at hotspots in the genome, but the genetic factors responsible for most hotspots have remained elusive. Here we describe in fission yeast the genome-wide distribution of meiosis-specific Rec12-DNA linkages, which closely parallel DSBs measured by conventional Southern blot hybridization. Prominent DSB hotspots are located approximately 65 kb apart, separated by intervals with little or no detectable breakage. Most hotspots lie within exceptionally large intergenic regions. Thus, the chromosomal architecture responsible for hotspots in fission yeast is markedly different from that of budding yeast, in which DSB hotspots are much more closely spaced and, in many regions of the genome, occur at each promoter. Our analysis in fission yeast reveals a clearly identifiable chromosomal feature that can predict the majority of recombination hotspots across a whole genome and provides a basis for searching for the chromosomal features that dictate hotspots of meiotic recombination in other organisms, including humans.","authors":"Cromie GA, Hyppa RW, Cam HP, Farah JA, Grewal SI, Smith GR","authors_abbrev":"Cromie GA et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-08-29","publication_year":"2007","canto_session_key":"9aa605254ded0d28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-09-16 13:36:19","canto_approved_date":"2020-09-16 13:36:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-09-16 13:36:13","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-09-16"},{"uniquename":"PMID:8313905","title":"A fission yeast RCC1-related protein is required for the mitosis to interphase transition.","citation":"EMBO J 1994 Feb 01;13(3):606-15","abstract":"The isolation and characterization of the mutant dcdts (defect in chromatin decondensation) has led to the identification of two conserved proteins required for the re-establishment of the interphase state following the completion of mitosis. The gene that rescues the dcdts mutant encodes a protein similar to the human chromatin binding protein, RCC1. A suppressor of dcdts encodes a protein nearly identical to the human GTP-binding protein, RAN, encoded by the TC4 gene. These results indicate that completion of mitosis is regulated at least in part by a GTPase molecular switch. The gene and suppressor of dcdts are identical to the previously described Schizosaccharomyces pombe genes pim1 (premature initiation of mitosis) and spi1 (suppressor of pim), but the dcdts mutant does not enter mitosis prematurely, a phenotype that has been reported for the pim1-46ts mutant. Based on our studies we propose that the pim1 gene product is required for regulating chromatin condensation with a primary role at the end of mitosis and pleiotropic effects on other aspects of cell behavior.","authors":"Sazer S, Nurse P","authors_abbrev":"Sazer S et al.","pubmed_publication_date":"01 Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1289.03c","SPBC557.03c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:26630677","title":"A Tool for Multiple Targeted Genome Deletions that Is Precise, Scar-Free, and Suitable for Automation.","citation":"PLoS One 2015;10(12):e0142494","abstract":"Many advances in synthetic biology require the removal of a large number of genomic elements from a genome. Most existing deletion methods leave behind markers, and as there are a limited number of markers, such methods can only be applied a fixed number of times. Deletion methods that recycle markers generally are either imprecise (remove untargeted sequences), or leave scar sequences which can cause genome instability and rearrangements. No existing marker recycling method is automation-friendly. We have developed a novel openly available deletion tool that consists of: 1) a method for deleting genomic elements that can be repeatedly used without limit, is precise, scar-free, and suitable for automation; and 2) software to design the method's primers. Our tool is sequence agnostic and could be used to delete large numbers of coding sequences, promoter regions, transcription factor binding sites, terminators, etc in a single genome. We have validated our tool on the deletion of non-essential open reading frames (ORFs) from S. cerevisiae. The tool is applicable to arbitrary genomes, and we provide primer sequences for the deletion of: 90% of the ORFs from the S. cerevisiae genome, 88% of the ORFs from S. pombe genome, and 85% of the ORFs from the L. lactis genome.","doi":"10.1371/journal.pone.0142494","authors":"Aubrey W, Riley MC, Young M, King RD, Oliver SG, Clare A","authors_abbrev":"Aubrey W et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-12-03","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-12-04 01:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20739285","title":"Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12.","citation":"J Biol Chem 2010 Oct 29;285(44):33992-4003","abstract":"Schizosaccharomyces pombe Rpn10 (SpRpn10) is a proteasomal ubiquitin (Ub) receptor located within the 19 S regulatory particle where it binds to subunits of both the base and lid subparticles. We have solved the structure of full-length SpRpn10 by determining the crystal structure of the von Willebrand factor type A domain and characterizing the full-length protein by NMR. We demonstrate that the single Ub-interacting motif (UIM) of SpRpn10 forms a 1:1 complex with Lys(48)-linked diUb, which it binds selectively over monoUb and Lys(63)-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid subparticle, with an affinity comparable with Lys(48)-linked diUb. This is the first observation of a UIM binding other than a Ub fold and suggests that SpRpn12 could modulate the activity of SpRpn10 as a proteasomal Ub receptor.","doi":"10.1074/jbc.M110.134510","authors":"Riedinger C, Boehringer J, Trempe JF, Lowe ED, Brown NR, Gehring K, Noble ME, Gordon C, Endicott JA","authors_abbrev":"Riedinger C et al.","pubmed_publication_date":"29 Oct 2010","pubmed_entrez_date":"2010-08-27","publication_year":"2010","canto_session_key":"52cf624aef9da796","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-09-20 14:08:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 10:03:34","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.12c","SPBC16G5.01","SPAC637.10c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-09-20","pdb_entries":[{"pdb_id":"2x5n","gene_chains":[{"gene_uniquename":"SPAC637.10c","chain":"A","position":"2-193"}],"title":"Crystal Structure of the SpRpn10 VWA domain","entry_authors":"Riedinger C,Boehringer J,Trempe J-F,Lowe ED,Brown NR,Gehring K,Noble MEM,Gordon C,Endicott JA","entry_authors_abbrev":"Riedinger C et al.","reference_uniquename":"PMID:20739285","experimental_method":"X-ray","resolution":"1.3"}]},{"uniquename":"GO_REF:0000065","title":"Representation of transport of a chemical entity as a biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing transport of a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom template is \"GO:0006810 and 'transports or maintains localization of' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14643670","title":"Sub-families of alpha/beta barrel enzymes: a new adenine deaminase family.","citation":"J Mol Biol 2003 Dec 12;334(5):1117-31","abstract":"No gene coding for an adenine deaminase has been described in eukaryotes. However, physiological and genetical evidence indicates that adenine deaminases are present in the ascomycetes. We have cloned and characterised the genes coding for the adenine deaminases of Aspergillus nidulans, Saccharomyces cerevisiae and Schizosaccharomyces pombe. The A.nidulans gene was expressed in Escherichia coli and the purified enzyme shows adenine but not adenosine deaminase activity. The open reading frames coded by the three genes are very similar and obviously related to the bacterial and eukaryotic adenosine deaminases rather than to the bacterial adenine deaminases. The latter are related to allantoinases, ureases and dihydroorotases. The fungal adenine deaminases and the homologous adenosine deaminases differ in a number of residues, some of these being clearly involved in substrate specificity. Other prokaryotic enzymes in the database, while clearly related to the above, do not fit into either sub-class, and may even have a different specificity. These results imply that adenine deaminases have appeared twice in the course of evolution, from different ancestral enzymes constructed both around the alpha/beta barrel scaffold.","authors":"Ribard C, Rochet M, Labedan B, Daignan-Fornier B, Alzari P, Scazzocchio C, Oestreicher N","authors_abbrev":"Ribard C et al.","pubmed_publication_date":"12 Dec 2003","pubmed_entrez_date":"2003-12-04","publication_year":"2003","canto_session_key":"ead523be4bbc7dc2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-06 16:40:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 22:35:51","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1683.02","SPBC1198.02"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:18060866","title":"ADP-ribosylation factor arf6p may function as a molecular switch of new end take off in fission yeast.","citation":"Biochem Biophys Res Commun 2008 Feb 01;366(1):193-8","abstract":"Small GTPases act as molecular switches in a wide variety of cellular processes. In fission yeast Schizosaccharomyces pombe, the directions of cell growth change from a monopolar manner to a bipolar manner, which is known as 'New End Take Off' (NETO). Here I report the identification of a gene, arf6(+), encoding an ADP-ribosylation factor small GTPase, that may be essential for NETO. arf6Delta cells completely fail to undergo NETO. arf6p localizes at both cell ends and presumptive septa in a cell-cycle dependent manner. And its polarized localization is not dependent on microtubules, actin cytoskeletons and some NETO factors (bud6p, for3p, tea1p, tea3p, and tea4p). Notably, overexpression of a fast GDP/GTP-cycling mutant of arf6p can advance the timing of NETO. These findings suggest that arf6p functions as a molecular switch for the activation of NETO in fission yeast.","authors":"Fujita A","authors_abbrev":"Fujita A","pubmed_publication_date":"01 Feb 2008","pubmed_entrez_date":"2007-12-07","publication_year":"2008","canto_session_key":"bbcfc3c19fa85d53","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-07 14:47:33","canto_approved_date":"2024-04-04 15:12:36","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-07-27 15:56:08","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.16","SPBC1706.01","SPCC895.05","SPAC6G10.02c","SPBC1539.08"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-10-07"},{"uniquename":"PMID:30829327","title":"Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51.","citation":"J Vis Exp 2019 Feb 13;(144)","abstract":"The DNA strand exchange reaction mediated by Rad51 is a critical step of homologous recombination. In this reaction, Rad51 forms a nucleoprotein filament on single-stranded DNA (ssDNA) and captures double-stranded DNA (dsDNA) non-specifically to interrogate it for a homologous sequence. After encountering homology, Rad51 catalyzes DNA strand exchange to mediate pairing of the ssDNA with the complementary strand of the dsDNA. This reaction is highly regulated by numerous accessary proteins in vivo. Although conventional biochemical assays have been successfully employed to examine the role of such accessory protein in vitro, kinetic analysis of intermediate formation and its progression into a final product has proven challenging due to the unstable and transient nature of the reaction intermediates. To observe these reaction steps directly in solution, fluorescence resonance energy transfer (FRET)-based real-time observation systems of this reaction were established. Kinetic analysis of real-time observations shows that the DNA strand exchange reaction mediated by Rad51 obeys a three-step reaction model involving the formation of a three-strand DNA intermediate, maturation of this intermediate, and the release of ssDNA from the mature intermediate. The Swi5-Sfr1 complex, an accessary protein conserved in eukaryotes, strongly enhances the second and third steps of this reaction. The FRET-based assays presented here enable us to uncover the molecular mechanisms through which recombination accessary proteins stimulate the DNA strand exchange activity of Rad51. The primary goal of this protocol is to enhance the repertoire of techniques available to researchers in the field of homologous recombination, particularly those working with proteins from species other than Schizosaccharomyces pombe, so that the evolutionary conservation of the findings presented herein can be determined.","doi":"10.3791/59073","authors":"Ito K, Argunhan B, Tsubouchi H, Iwasaki H","authors_abbrev":"Ito K et al.","pubmed_publication_date":"13 Feb 2019","pubmed_entrez_date":"2019-03-05","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-03-06 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41348546","title":"Protocol for the analysis of proteasome activity, assembly state, and composition in fission yeast extracts using native gels.","citation":"STAR Protoc 2025 Dec 04;6(4):104233","abstract":"The proteasome is a macromolecular complex responsible for degrading short-lived or damaged proteins. Proteasome analysis presents challenges due to its high molecular weight and low stability. Here, we present a protocol to assess proteasome activity, assembly, and composition in Schizosaccharomyces pombe. We describe steps for lysate preparation and native electrophoresis to separate proteasome complexes. We then detail procedures for detecting proteasome activity using fluorescent substrates, fluorescently-tagged native proteins, and non-tagged proteasome components by immunodetection in a single gel. For complete details on the use and execution of this protocol, please refer to Ruiz-Romero et al. 1 .","doi":"10.1016/j.xpro.2025.104233","authors":"Ruiz-Romero G, Daga RR, Salas-Pino S","authors_abbrev":"Ruiz-Romero G et al.","pubmed_publication_date":"04 Dec 2025","pubmed_entrez_date":"2025-12-05","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-12-06 00:25:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24790095","title":"Characterization of the roles of Blt1p in fission yeast cytokinesis.","citation":"Mol Biol Cell 2014 Jul 01;25(13):1946-57","abstract":"Spatial and temporal regulation of cytokinesis is essential for cell division, yet the mechanisms that control the formation and constriction of the contractile ring are incompletely understood. In the fission yeast Schizosaccharomyces pombe proteins that contribute to the cytokinetic contractile ring accumulate during interphase in nodes-precursor structures around the equatorial cortex. During mitosis, additional proteins join these nodes, which condense to form the contractile ring. The cytokinesis protein Blt1p is unique in being present continuously in nodes from early interphase through to the contractile ring until cell separation. Blt1p was shown to stabilize interphase nodes, but its functions later in mitosis were unclear. We use analytical ultracentrifugation to show that purified Blt1p is a tetramer. We find that Blt1p interacts physically with Sid2p and Mob1p, a protein kinase complex of the septation initiation network, and confirm known interactions with F-BAR protein Cdc15p. Contractile rings assemble normally in blt1∆ cells, but the initiation of ring constriction and completion of cell division are delayed. We find three defects that likely contribute to this delay. Without Blt1p, contractile rings recruited and retained less Sid2p/Mob1p and Clp1p phosphatase, and β-glucan synthase Bgs1p accumulated slowly at the cleavage site.","doi":"10.1091/mbc.E13-06-0300","authors":"Goss JW, Kim S, Bledsoe H, Pollard TD","authors_abbrev":"Goss JW et al.","pubmed_publication_date":"01 Jul 2014","pubmed_entrez_date":"2014-05-03","publication_year":"2014","canto_session_key":"cf28246afde3f15f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-13 12:02:06","canto_approved_date":"2022-11-03 19:26:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-05 12:47:23","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPAC4F8.13c","SPBC19G7.05c","SPBC11B10.09","SPBC24C6.07","SPAC6F6.08c","SPAC24B11.11c","SPAC20G8.05c","SPAC1782.09c","SPBC1A4.05","SPAC57A10.02","SPCC1739.11c","SPAC27F1.02c","SPAC24H6.05","SPAC4A8.15c","SPBC21.06c","SPAC1F5.04c","SPAP8A3.08","SPBC244.01c","SPBC428.13c","SPCC4B3.15","SPAC31A2.16","SPAC9G1.09","SPAC1565.06c","SPCC645.05c"],"gene_count":25,"ltp_gene_count":24,"approved_date":"2015-11-13"},{"uniquename":"PMID:22444194","title":"Convenient and efficient syntheses of oligodeoxyribonucleotides containing O(6)-(carboxymethyl)guanine and O(6)-(4-oxo-4-(3-pyridyl)butyl)guanine.","citation":"Nucleosides Nucleotides Nucleic Acids 2012 Apr;31(4):328-38","abstract":"O(6)-(carboxymethyl)guanine (O(6)-CMG) and O(6)-(4-oxo-4-(3-pyridyl)butyl)guanine (O(6)-pobG) are toxic lesions formed in DNA following exposure to alkylating agents. O(6)-CMG results from exposure to nitrosated glycine or nitrosated bile acid conjugates and may be associated with diets rich in red meat. O(6)-pobG lesions are derived from alkylating agents found in tobacco smoke. Efficient syntheses of oligodeoxyribonucleotides (ODNs) containing O(6)-CMG and O(6)-pobG are described that involve nucleophilic displacement by the appropriate alcohol on a common synthetic ODN containing the reactive base 2-amino-6-methylsulfonylpurine. ODNs containing O(6)-pobG and O (6)-CMG were found to be good substrates for the S. pombe alkyltransferase-like protein Atl1.","doi":"10.1080/15257770.2012.656784","authors":"Millington CL, Watson AJ, Marriott AS, Margison GP, Povey AC, Williams DM","authors_abbrev":"Millington CL et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-03-27","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10102372","title":"The fission yeast rpa17+ gene encodes a functional homolog of AC19, a subunit of RNA polymerases I and III of Saccharomyces cerevisiae.","citation":"Mol Gen Genet 1999 Mar;261(2):364-73","abstract":"Eukaryotic RNA polymerases I and III consist of multiple subunits. Each of these enzymes includes two distinct and evolutionarily conserved subunits called alpha-related subunits which are shared only by polymerases I and III. The alpha-related subunits show limited homology with the alpha-subunit of prokaryotic RNA polymerase. To gain further insight into the structure and function of alpha-related subunits, we cloned and characterized a gene from Schizosaccharomyces pombe that encodes a protein of 17 kDa which can functionally replace AC19 - an alpha-related subunit of RNA polymerases I and III of Saccharomyces cerevisiae - and was thus named rpa17+. RPA17 has 125 amino acids and shows 63% identity to AC19 over a 108-residue stretch, whereas the N-terminal regions of the two proteins are highly divergent. Disruption of rpa17+ shows that the gene is essential for cell growth. Sequence comparison with other alpha-related subunits from different species showed that RPA17 contains an 81-amino acid block that is evolutionarily conserved. Deletion analysis of the N- and C-terminal regions of RPA17 and AC19 confirms that the 81-amino acid block is important for the function of the alpha-related subunits.","authors":"Imai K, Imazawa Y, Yao Y, Yamamoto K, Hisatake K, Muramatsu M, Nogi Y","authors_abbrev":"Imai K et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-04-02","publication_year":"1999","canto_session_key":"b88e92800ec97ee1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-02 15:49:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-03 09:16:47","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-03"},{"uniquename":"PMID:8873451","title":"The translation initiation factor eIF4A from Schizosaccharomyces pombe is closely related to its mammalian counterpart.","citation":"Yeast 1996 Aug;12(10):977-81","abstract":"We have isolated a cDNA clone encoding eIF4A from Schizosaccharomyces pombe. The deduced protein sequence is similar in length and sequence to other eIF4A proteins and exhibits highest similarity with the mammalian eIF4A protein. Hybridization with genomic DNA reveals two eIF4A genes located on two different chromosomes.","authors":"Fischli A, Schmid SR, Coppolecchia R, Linder P","authors_abbrev":"Fischli A et al.","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_session_key":"dc044f1c8e034fa1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-20 15:54:17","canto_approved_date":"2019-11-20 15:54:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-20 15:54:09","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1006.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-11-20"},{"uniquename":"PMID:15157884","title":"Protocols for experimentation with Schizosaccharomyces pombe.","citation":"Methods 2004 Jul;33(3):187-8","abstract":"","authors":"Gould KL","authors_abbrev":"Gould KL","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24758716","title":"Identification of glutathione (GSH)-independent glyoxalase III from Schizosaccharomyces pombe.","citation":"BMC Evol Biol 2014 Apr 23;14:86","abstract":"Reactive carbonyl species (RCS), such as methylglyoxal (MG) and glyoxal (GO), are synthesized as toxic metabolites in living systems. Mechanisms of RCS detoxification include the glutathione (GSH)-dependent system consisting of glyoxalase I (GLO1) and glyoxalase II (GLO2), and GSH-independent system involving glyoxalase III (GLO3). Hsp31 and DJ-1 proteins are weakly homologous to each other and belong to two different subfamilies of the DJ-1/Hsp31/PfpI superfamily. Recently, the Escherichia coli Hsp31 protein and the DJ-1 proteins from Arabidopsis thaliana and metazoans have been demonstrated to have GLO3 activity.\nWe performed a systematic survey of homologs of DJ-1 and Hsp31 in fungi. We found that DJ-1 proteins have a very limited distribution in fungi, whereas Hsp31 proteins are widely distributed among different fungal groups. Phylogenetic analysis revealed that fungal and metazoan DJ-1 proteins and bacterial YajL proteins are most closely related and together form a sister clade to bacterial and fungal Hsp31 proteins. We showed that two Schizosaccharomyces pombe Hsp31 proteins (Hsp3101 and Hsp3102) and one Saccharomyces cerevisiae Hsp31 protein (ScHsp31) displayed significantly higher in vitro GLO3 activity than S. pombe DJ-1 (SpDJ-1). Overexpression of hsp3101, hsp3102 and ScHSP31 could confer MG and GO resistance on either wild-type S. pombe cells or GLO1 deletion of S. pombe. S. pombe DJ-1 and Hsp31 proteins exhibit different patterns of subcellular localization.\nOur results suggest that fungal Hsp31 proteins are the major GLO3 that may have some role in protecting cells from RCS toxicity in fungi. Our results also support the view that the GLO3 activity of Hsp31 proteins may have evolved independently from that of DJ-1 proteins.","doi":"10.1186/1471-2148-14-86","authors":"Zhao Q, Su Y, Wang Z, Chen C, Wu T, Huang Y","authors_abbrev":"Zhao Q et al.","pubmed_publication_date":"23 Apr 2014","pubmed_entrez_date":"2014-04-25","publication_year":"2014","canto_session_key":"134ecf3bebd24e1a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2016-01-25 12:26:48","canto_approved_date":"2024-04-04 07:06:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-29 11:36:40","canto_added_date":"2014-05-07 00:23:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.03c","SPBC12C2.12c","SPBC947.09","SPAC1F7.06","SPAC11D3.13","SPAC5H10.02c","SPCC757.03c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2016-01-25"},{"uniquename":"PMID:23656778","title":"Brc1 links replication stress response and centromere function.","citation":"Cell Cycle 2013 Jun 01;12(11):1665-71","abstract":"Protection of genome integrity depends on the coordinated activities of DNA replication, DNA repair, chromatin assembly and chromosome segregation mechanisms. DNA lesions are detected by the master checkpoint kinases ATM (Tel1) and ATR (Rad3/Mec1), which phosphorylate multiple substrates, including a C-terminal SQ motif in histone H2A or H2AX. The 6-BRCT domain protein Brc1, which is required for efficient recovery from replication fork arrest and collapse in fission yeast, binds phospho-histone H2A (γH2A)-coated chromatin at stalled and damaged replication forks. We recently found that Brc1 co-localizes with γH2A that appears in pericentromeric heterochromatin during S-phase. Our studies indicate that Brc1 contributes to the maintenance of pericentromeric heterochromatin, which is required for efficient chromosome segregation during mitosis. Here, we review these studies and present additional results that establish the functional requirements for the N-terminal BRCT domains of Brc1 in the replication stress response and resistance to the microtubule destabilizing drug thiabendazole (TBZ). We also identify the nuclear localization signal (NLS) in Brc1, which closely abuts the C-terminal pair of BRCT domains that form the γH2A-binding pocket. This compact arrangement of localization domains may be a shared feature of other γH2A-binding proteins, including Rtt107, PTIP and Mdc1.","doi":"10.4161/cc.24900","authors":"Lee SY, Russell P","authors_abbrev":"Lee SY et al.","pubmed_publication_date":"01 Jun 2013","pubmed_entrez_date":"2013-05-10","publication_year":"2013","canto_session_key":"5313616a6253c909","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2013-07-12 15:03:33","canto_approved_date":"2019-05-02 22:36:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-07-09 18:10:12","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Paul Russell","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.05c","SPAC19G12.06c","SPCC622.08c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2013-07-12"},{"uniquename":"PMID:9303310","title":"p25rum1 promotes proteolysis of the mitotic B-cyclin p56cdc13 during G1 of the fission yeast cell cycle.","citation":"EMBO J 1997 Aug 01;16(15):4657-64","abstract":"The fission yeast Schizosaccharomyces pombe CDK inhibitor p25rum1 plays a major role in regulating cell cycle progression during G1. Here we show that p25rum1 associates with the CDK p34cdc2/p56cdc13 during G1 in normally cycling cells and is required for the rapid proteolysis of p56cdc13. In vitro binding data indicate that p25rum1 has specificity for the B-cyclin p56cdc13 component of the CDK and can bind the cyclin even in the absence of the cyclin destruction box. At the G1-S-phase transition, p25rum1 levels decrease and p56cd13 levels increase. We also show that on release from a G1 block, the rapid disappearance of p25rum1 requires the activity of the CDK p34cdc2/cig1p and that this same CDK phosphorylates p25rum1 in vitro. We propose that the binding of p25rum1 to p56cdc13 promotes cyclin proteolysis during G1, with p25rum1 possibly acting as an adaptor protein, promoting transfer of p56cdc13 to the proteolytic machinery. At the G1-S-phase transition, p25rum1 becomes targeted for proteolysis by a mechanism which may involve p34cdc2/cig1p phosphorylation. As a consequence, at this point in the cell cycle p56cdc13 proteolysis is inhibited, leading to a rise of p56cdc13 levels in preparation for mitosis.","authors":"Correa-Bordes J, Gulli MP, Nurse P","authors_abbrev":"Correa-Bordes J et al.","pubmed_publication_date":"01 Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"370824a189ad6763","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-05-30 12:41:28","canto_approved_date":"2024-04-02 17:08:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-08 05:41:01","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":12,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB2B4.03","SPBC336.12c","SPBC582.03","SPBC32F12.09","SPCC4E9.02","SPBC11B10.09"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-05-30"},{"uniquename":"PMID:1840262","title":"cdc2 protein kinase: interactions with cyclins and suc1.","citation":"Cold Spring Harb Symp Quant Biol 1991;56:515-21","abstract":"","authors":"Brambilla P, Ducommun B, Draetta G","authors_abbrev":"Brambilla P et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10443406","title":"Isolation of DNA structure-dependent checkpoint mutants in S. pombe.","citation":"Methods Mol Biol 1999;113:1-9","abstract":"","authors":"Martinho RG, Carr AM","authors_abbrev":"Martinho RG et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-08-12","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12185500","title":"Fission yeast Cdc23 interactions with DNA replication initiation proteins.","citation":"Curr Genet 2002 Aug;41(5):342-8","abstract":"Schizosaccharomyces pombe Cdc23 is an essential DNA replication protein, conserved in eukaryotes and functionally homologous with Saccharomyces cerevisiae Dna43 (Mcm10). We sought evidence for interactions between Cdc23 and the MCM2-7 complex, a component of both the pre-replicative complex and the replication fork. Cdc23 shows genetic interactions with four MCM subunits: cdc23-M36 and cdc23-1E2 alleles both show synthetic phenotypes with mcm2 (cdc19-P1) and mcm6 (mis5-268), and cdc23-M36 is synthetically lethal with mcm4 (cdc21-K46) and with mcm5 (nda4-108). The wild-type cdc23 gene on multicopy plasmids can partially suppress temperature-dependent defects in mcm5 (nda4-108). Two-hybrid analysis demonstrates interactions at the protein-protein level between Cdc23 and Mcm4, Mcm5 and Mcm6. Cdc23 also interacts with four subunits of the Schizosaccharomyces pombe origin recognition complex (ORC) in yeast two-hybrid assay: Orc1, Orc2, Orc5 and Orc6. We found no evidence for interaction between Cdc23 and the MCM recruitment factor Cdc18 (the homologue of Saccharomyces cerevisiae Cdc6). Unlike Cdc18, Cdc23 mRNA shows no significant fluctuation in level through the cell cycle. These data suggest that fission yeast Cdc23 is an MCM-associated factor which has a role in the initiation of DNA replication.","authors":"Hart EA, Bryant JA, Moore K, Aves SJ","authors_abbrev":"Hart EA et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-08-20","publication_year":"2002","canto_session_key":"7bf893a86d94196c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-15 12:56:25","canto_approved_date":"2025-09-03 13:58:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-06-15 12:56:18","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.15","SPCC16A11.17","SPBC685.09","SPBC4.04c","SPAC1B2.05","SPBC1347.10","SPBC211.04c","SPBC2A9.12","SPBC646.14c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2015-06-15"},{"uniquename":"PMID:14668334","title":"The Schizosaccharomyces pombe corepressor Tup11 interacts with the iron-responsive transcription factor Fep1.","citation":"J Biol Chem 2004 Mar 05;279(10):9462-74","abstract":"The Schizosaccharomyces pombe fep1(+) gene encodes a GATA transcription factor that represses the expression of iron transport genes in response to elevated iron concentrations. This transcriptional response is altered only in strains harboring a combined deletion of both tup11(+) and tup12(+) genes. This suggests that Tup11 is capable of negatively regulating iron transport gene expression in the absence of Tup12 and vice versa. The tup11(+)- and tup12(+)-encoded proteins resemble the Saccharomyces cerevisiae Tup1 corepressor. Using yeast two-hybrid analysis we show that Tup11 and Fep1 physically interact with each other. The C-terminal region from amino acids 242 to 564 of Fep1 is required for interaction with Tup11. Within this region, a minimal domain encompassing amino acids 405-541 was sufficient for Tup11-Fep1 association. Deletion mapping analysis revealed that the WD40-repeat sequence motifs of Tup11 are necessary for its interaction with Fep1. Analysis of Tup11 mutants with single amino acid substitutions in the WD40 repeats suggested that the Fep1 transcription factor interacts with a putative flat upper surface on the predicted beta-propeller structure of this motif. Further analysis by in vivo coimmunoprecipitation showed that Tup11 and Fep1 are physically associated. In vitro pull-down experiments further verified a direct interaction between the Fep1 C terminus and the Tup11 C-terminal WD40 repeat domain. Taken together, these results describe the first example of a physical interaction between a corepressor and an iron-sensing factor controlling the expression of iron uptake genes.","authors":"Znaidi S, Pelletier B, Mukai Y, Labbé S","authors_abbrev":"Znaidi S et al.","pubmed_publication_date":"05 Mar 2004","pubmed_entrez_date":"2003-12-12","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18B11.10","SPAC23E2.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:10705460","title":"Identification of a 14-3-3 protein from Lentinus edodes that interacts with CAP (adenylyl cyclase-associated protein), and conservation of this interaction in fission yeast.","citation":"Biosci Biotechnol Biochem 2000 Jan;64(1):149-59","abstract":"We previously identified a gene encoding a CAP (adenylyl cyclase-associated protein) homologue from the edible Basidiomycete Lentinus edodes. To further discover the cellular functions of the CAP protein, we searched for CAP-interacting proteins using a yeast two-hybrid system. Among the candidates thus obtained, many clones encoded the C-terminal half of an L. edodes 14-3-3 homologue (designated cip3). Southern blot analysis indicated that L. edodes contains only one 14-3-3 gene. Overexpression of the L. edodes 14-3-3 protein in the fission yeast Schizosaccharomyces pombe rad24 null cells complemented the loss of endogenous 14-3-3 protein functions in cell morphology and UV sensitivity, suggesting functional conservation of 14-3-3 proteins between L. edodes and S. pombe. The interaction between L. edodes CAP and 14-3-3 protein was restricted to the N-terminal domain of CAP and was confirmed by in vitro co-precipitation. Results from both the two-hybrid system and in vivo co-precipitation experiments showed the conservation of this interaction in S. pombe. The observation that a 14-3-3 protein interacts with the N-terminal portion of CAP but not with full-length CAP in L. edodes and S. pombe suggests that the C-terminal region of CAP may have a negative effect on the interaction between CAP and 14-3-3 proteins, and 14-3-3 proteins may play a role in regulation of CAP function.","authors":"Zhou GL, Yamamoto T, Ozoe F, Yano D, Tanaka K, Matsuda H, Kawamukai M","authors_abbrev":"Zhou GL et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-03-08","publication_year":"2000","canto_session_key":"8d11b1d68b5b6e67","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-12 16:51:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 15:43:14","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A2.13c","SPAC8E11.02c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2015-03-12"},{"uniquename":"PMID:42002879","title":"Mislocalized Cytosolic Polyphosphate Forms Potentially Toxic Droplets, Highlighting the Essentiality of Vacuolar Polyphosphate in Pi Homeostasis.","citation":"Genes Cells 2026 May;31(3):e70118","abstract":"Inorganic polyphosphate is a phosphate polymer found in nearly all species examined to date. Over decades of research, this biopolymer has been revealed to participate in a broad range of biological phenomena, from phosphate storage to human diseases. Despite these advances, its essential physiological roles that are critical for cellular or organismal survival remain elusive. In the fission yeast Schizosaccharomyces pombe, the vacuolar transporter chaperone (VTC) complex synthesizes polyphosphate within the vacuolar lumen and supports cell viability synergistically with two additional phosphate regulators with the SPX domain, the phosphate sensor: Pqr1, restricting phosphate import, and Xpr1, a phosphate exporter. In this study, we show that the polyphosphate level increases in response to the elevated extracellular Pi concentration or severe phosphate stress upon the loss of both Pqr1 and Xpr1. The VTC complex may alleviate the lethal phosphate stress by polymerizing and sequestering excess phosphates into the vacuoles. Notably, artificial cytoplasmic synthesis of polyphosphate by the bacterial polyphosphate synthase PPK failed to compensate for the essential function of the VTC complex, forming cytoplasmic polyphosphate droplets via liquid-liquid phase separation, which are potentially cytotoxic. These findings highlight the critical importance of spatial regulation of polyphosphate synthesis for its physiological function.","doi":"10.1111/gtc.70118","authors":"Takeda K, Okuyama R, Takechi H, Fujiyama K, Hatori M, Miwatari A","authors_abbrev":"Takeda K et al.","pubmed_publication_date":"May 2026","pubmed_entrez_date":"2026-04-20","publication_year":"2026","canto_session_key":"0256ca3205d47ba8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-20 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8879272","title":"Cloning of Schizosaccharomyces pombe rph16+, a gene homologous to the Saccharomyces cerevisiae RAD16 gene.","citation":"Mutat Res 1996 Oct 18;364(2):57-71","abstract":"The RAD16 gene is involved in the nucleotide excision repair of UV damage in the transcriptional silenced mating type loci (Terleth et al., 1990 and Bang et al., 1992) and in non-transcribed stands of active genes in Saccharomyces cerevisiae (Verhage et al., 1994). Using touchdown-PCR with primers derived from various domains of the S. cerevisiae Rad 16 protein, a specific Schizosaccharomyces pombe probe was isolated. This probe was used to obtain the complete RAD16 homologous gene from a S. pombe chromosomal bank. DNA sequence analysis of the rph16+ gene revealed an open reading frame of 854 amino acids. Comparison of the amino acid sequences of the Rhp16 and Rad16 proteins showed a high level of conservation: 68% similarity. The Rhp16 protein sequence contains the two Zn-finger motifs and the putative helicase domains as found in the Rad16 protein. Like the RAD16, the rph16+ gene is UV-inducible (Bang et al., 1995). In analogy with the rad16 mutant, the rhp16 disruption mutant is viable and grows normally, indicating that the gene does not have an essential function. The rhp16 disruption mutant is not sensitive for UV but is sensitive for cisplatin. The rhp16+ gene cloned behind the GAI 1 promoter partially complements the UV sensitivity and the defect in the non-transcribed strand DNA repair of a S. cerevisiae rad16 mutant, indicating functional homology between the rhp16+ and RAD16 genes. The structural and functional homology between the two genes suggests that the RAD16 dependent subpathway of NER for the repair of non-transcribed DNA is evolutionary conserved.","authors":"Bang DD, Ketting R, de Ruijter M, Brandsma JA, Verhage RA, van de Putte P, Brouwer J","authors_abbrev":"Bang DD et al.","pubmed_publication_date":"18 Oct 1996","pubmed_entrez_date":"1996-10-18","publication_year":"1996","canto_session_key":"1fe1313ed251b669","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-02-11 17:14:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-05 12:43:45","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.01c","SPBC3E7.08c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-02-05"},{"uniquename":"EMBL:AU009422","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18851838","title":"The FANCM ortholog Fml1 promotes recombination at stalled replication forks and limits crossing over during DNA double-strand break repair.","citation":"Mol Cell 2008 Oct 10;32(1):118-28","abstract":"The Fanconi anemia (FA) core complex promotes the tolerance/repair of DNA damage at stalled replication forks by catalyzing the monoubiquitination of FANCD2 and FANCI. Intriguingly, the core complex component FANCM also catalyzes branch migration of model Holliday junctions and replication forks in vitro. Here we have characterized the ortholog of FANCM in fission yeast Fml1 in order to understand the physiological significance of this activity. We show that Fml1 has at least two roles in homologous recombination-it promotes Rad51-dependent gene conversion at stalled/blocked replication forks and limits crossing over during mitotic double-strand break repair. In vitro Fml1 catalyzes both replication fork reversal and D loop disruption, indicating possible mechanisms by which it can fulfill its pro- and antirecombinogenic roles.","doi":"10.1016/j.molcel.2008.08.024","authors":"Sun W, Nandi S, Osman F, Ahn JS, Jakovleska J, Lorenz A, Whitby MC","authors_abbrev":"Sun W et al.","pubmed_publication_date":"10 Oct 2008","pubmed_entrez_date":"2008-10-15","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9.05"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:16258244","title":"Characterization and regulation of the gene encoding monothiol glutaredoxin 3 in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Cells 2005 Aug 31;20(1):74-82","abstract":"Glutaredoxins (Grxs) are thioloxidoreductases which are required for maintaining thiol/disulfide equilibrium in living cells. The Grx3 gene, which encodes one of the three monothiol Grxs in the fission yeast Schizosaccharomyces pombe, was characterized, and its transcriptional regulation studied. Genomic DNA encoding Grx3 was isolated by PCR, and a plasmid pTT3 carrying this DNA was produced. The DNA sequence has 1,267 bp, which would encode a monothiol Grx of 166 amino acids with a molecular mass of 18.3 kDa. The putative protein has 27% homology with Grx5, and contains many hydrophobic amino acid residues in its N-terminal region. S. pombe cells harboring pTT3 had increased Grx activity and enhanced survival on minimal medium plates containing aluminum (5 mM), BSO (0.05 mM), menadione (0.01 mM) or cadmium (0.2 mM). The 568 bp upstream region of Grx3 was fused into the promoterless beta-galactosidase gene of the shuttle vector YEp367R to generate fusion plasmid pMJS10. Potassium chloride (KCl) and metals including aluminum and cadmium enhanced the synthesis of beta-galactosidase from the fusion gene. The synthesis of beta-galactosidase was also enhanced, in a Pap1-dependent manner, by fermentable carbon sources such as glucose (at low concentrations) and sucrose, but not by non-fermentable carbon sources such as ethanol and acetate. Grx3 mRNA increased in response to treatment with BSO. These observations indicate that S. pombe Grx3 is involved in the response to stress, and is regulated by stress.","authors":"Moon JS, Lim HW, Park EH, Lim CJ","authors_abbrev":"Moon JS et al.","pubmed_publication_date":"31 Aug 2005","pubmed_entrez_date":"2005-11-01","publication_year":"2005","canto_session_key":"7659b64bff1c7702","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:32:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-06 10:00:39","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPCC1450.06c","SPBC29B5.01","SPAC1783.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-11-06"},{"uniquename":"PMID:16149916","title":"Fission yeast Dss1 associates with the proteasome and is required for efficient ubiquitin-dependent proteolysis.","citation":"Biochem J 2006 Jan 01;393(Pt 1):303-9","abstract":"Human DSS1 associates with BRCA2, a tumour suppressor protein required for efficient recombinational DNA repair, but the biochemical function of DSS1 is not known. Orthologues of DSS1 are found in organisms such as budding yeast and fission yeast that do not have BRCA2-related proteins, indicating that DSS1 has a physiological role independent of BRCA2. The DSS1 orthologue in Saccharomyces cerevisiae has been shown to associate with the 26 S proteasome and, in the present paper, we report that in the distantly related fission yeast Schizosaccharomyces pombe, Dss1 associates with the 19 S RP (regulatory particle) of the 26 S proteasome. A role for S. pombe Dss1 in proteasome function is supported by three lines of evidence. First, overexpression of two components of the 19 S RP, namely Pad1/Rpn11 and Mts3/Rpn12, rescued the temperature-sensitive growth defect of the dss1 mutant. Secondly, the dss1 mutant showed phenotypes indicative of a defect in proteasome function: growth of the dss1 mutant was inhibited by low concentrations of L-canavanine, an amino acid analogue, and cells of the dss1 mutant accumulated high molecular mass poly-ubiquitylated proteins. Thirdly, synthetic growth defects were found when the dss1 mutation was combined with mutations in other proteasome subunit genes. These findings show that DSS1 has an evolutionarily conserved role as a regulator of proteasome function and suggest that DSS1 may provide a link between BRCA2 and ubiquitin-mediated proteolysis in human cells.","authors":"Jossé L, Harley ME, Pires IM, Hughes DA","authors_abbrev":"Jossé L et al.","pubmed_publication_date":"01 Jan 2006","pubmed_entrez_date":"2005-09-10","publication_year":"2006","canto_session_key":"b0e73c6381f45bbd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-04-23 14:58:34","canto_approved_date":"2025-04-16 20:16:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-11 14:51:03","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6C3.08","SPAC3A11.12c","SPCC1682.10","SPAC3G6.02","SPAC31G5.13","SPBC16G5.01","SPBC4.07c","SPBC119.01","SPCC576.10c","SPBP19A11.03c","SPCC126.03","SPBC409.06","SPBC582.07c","SPAC19G12.01c","SPAC1420.03","SPAC637.10c","SPBC17D11.07c"],"gene_count":17,"ltp_gene_count":17,"approved_date":"2015-04-23"},{"uniquename":"PMID:41178225","title":"Mitotic Phosphorylation of Swi6/HP1 Regulates Its Chromatin Binding and Chromosome Segregation.","citation":"FASEB J 2025 Nov 15;39(21):e71190","abstract":"In eukaryotic cells, heterochromatin assembly is critical for chromosome segregation and transcriptional gene silencing. Heterochromatin protein 1 (HP1) is a conserved chromosomal protein that plays an important role in heterochromatin assembly. We have previously shown that mammalian HP1α and Schizosaccharomyces pombe Swi6 are phosphorylated by casein kinase II (CK2) and that this phosphorylation is essential for their function in heterochromatin assembly. In addition to CK2-mediated phosphorylation, several studies have shown that HP1 proteins undergo additional phosphorylation during mitosis. However, functional significance of the mitotic phosphorylation of HP1 remains unclear. Here, we identified mitotic phosphorylation sites within fission yeast Swi6 and showed that this phosphorylation is involved in chromosome segregation. Using an Escherichia coli co-expression system, we showed that Swi6 is phosphorylated by Ark1, a solo Aurora kinase in S. pombe, and mutational analyses revealed that serine residues in the conserved N-terminal region of Swi6 are the primary targets of Ark1. By expressing mutant Swi6, we confirmed that these serine residues are phosphorylated during mitosis in vivo. Although non-phosphorylatable or phosphomimic mutations in Swi6 had little effect on heterochromatic silencing, they caused defects in early chromosome segregation and modulated the temperature-sensitive growth of mutant cells for chromosome passenger complex components. These results suggest that the Ark1-mediated mitotic phosphorylation of Swi6 is involved in chromosome segregation during mitosis and implicates a conserved regulatory role for the mitotic phosphorylation of HP1 proteins.","doi":"10.1096/fj.202500384R","authors":"Yoshimura Y, Hayashi A, Tanaka M, Suzuki-Matsubara M, Nakagawa R, Nishibuchi G, Tagami H, Oki M, Nakayama JI","authors_abbrev":"Yoshimura Y et al.","pubmed_publication_date":"15 Nov 2025","pubmed_entrez_date":"2025-11-03","publication_year":"2025","canto_session_key":"9707497b75834b89","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-11-04 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31170156","title":"Asymmetrical localization of Nup107-160 subcomplex components within the nuclear pore complex in fission yeast.","citation":"PLoS Genet 2019 Jun;15(6):e1008061","abstract":"The nuclear pore complex (NPC) forms a gateway for nucleocytoplasmic transport. The outer ring protein complex of the NPC (the Nup107-160 subcomplex in humans) is a key component for building the NPC. Nup107-160 subcomplexes are believed to be symmetrically localized on the nuclear and cytoplasmic sides of the NPC. However, in S. pombe immunoelectron and fluorescence microscopic analyses revealed that the homologous components of the human Nup107-160 subcomplex had an asymmetrical localization: constituent proteins spNup132 and spNup107 were present only on the nuclear side (designated the spNup132 subcomplex), while spNup131, spNup120, spNup85, spNup96, spNup37, spEly5 and spSeh1 were localized only on the cytoplasmic side (designated the spNup120 subcomplex), suggesting the complex was split into two pieces at the interface between spNup96 and spNup107. This contrasts with the symmetrical localization reported in other organisms. Fusion of spNup96 (cytoplasmic localization) with spNup107 (nuclear localization) caused cytoplasmic relocalization of spNup107. In this strain, half of the spNup132 proteins, which interact with spNup107, changed their localization to the cytoplasmic side of the NPC, leading to defects in mitotic and meiotic progression similar to an spNup132 deletion strain. These observations suggest the asymmetrical localization of the outer ring spNup132 and spNup120 subcomplexes of the NPC is necessary for normal cell cycle progression in fission yeast.","doi":"10.1371/journal.pgen.1008061","authors":"Asakawa H, Kojidani T, Yang HJ, Ohtsuki C, Osakada H, Matsuda A, Iwamoto M, Chikashige Y, Nagao K, Obuse C, Hiraoka Y, Haraguchi T","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-06-07","publication_year":"2019","canto_session_key":"704414a1c4cfb092","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-06-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29194511","title":"Prolyl isomerization of the CENP-A N-terminus regulates centromeric integrity in fission yeast.","citation":"Nucleic Acids Res 2018 Feb 16;46(3):1167-1179","abstract":"Centromeric identity and chromosome segregation are determined by the precise centromeric targeting of CENP-A, the centromere-specific histone H3 variant. The significance of the amino-terminal domain (NTD) of CENP-A in this process remains unclear. Here, we assessed the functional significance of each residue within the NTD of CENP-A from Schizosaccharomyces pombe (SpCENP-A) and identified a proline-rich 'GRANT' (Genomic stability-Regulating site within CENP-A N-Terminus) motif that is important for CENP-A function. Through sequential mutagenesis, we show that GRANT proline residues are essential for coordinating SpCENP-A centromeric targeting. GRANT proline-15 (P15), in particular, undergoes cis-trans isomerization to regulate chromosome segregation fidelity, which appears to be carried out by two FK506-binding protein (FKBP) family prolyl cis-trans isomerases. Using proteomics analysis, we further identified the SpCENP-A-localizing chaperone Sim3 as a SpCENP-A NTD interacting protein that is dependent on GRANT proline residues. Ectopic expression of sim3+ complemented the chromosome segregation defect arising from the loss of these proline residues. Overall, cis-trans proline isomerization is a post-translational modification of the SpCENP-A NTD that confers precise propagation of centromeric integrity in fission yeast, presumably via targeting SpCENP-A to the centromere.","doi":"10.1093/nar/gkx1180","authors":"Tan HL, Lim KK, Yang Q, Fan JS, Sayed AMM, Low LS, Ren B, Lim TK, Lin Q, Mok YK, Liou YC, Chen ES","authors_abbrev":"Tan HL et al.","pubmed_publication_date":"16 Feb 2018","pubmed_entrez_date":"2017-12-02","publication_year":"2018","canto_session_key":"a7a3831a50c4517f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hwei-Ling Tan","canto_first_approved_date":"2018-05-03 19:06:55","canto_approved_date":"2023-12-27 21:36:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-03 07:36:12","canto_added_date":"2017-12-03 01:15:17","annotation_curators":[{"name":"Hwei-Ling Tan","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.06c","SPBC8D2.04","SPAC9E9.10c","SPBC1105.17","SPBC1347.02","SPBC577.15c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-05-03"},{"uniquename":"PMID:11283163","title":"Origins and complexes: the initiation of DNA replication.","citation":"J Exp Bot 2001 Feb;52(355):193-202","abstract":"Eukaryotic DNA is organized for replication as multiple replicons. DNA synthesis in each replicon is initiated at an origin of replication. In both budding yeast, Saccharomyces cerevisiae and fission yeast, Schizosaccharomyces pombe, origins contain specific sequences that are essential for initiation, although these differ significantly between the two yeasts with those of S. pombe being more complex then those of S. cerevisiae. However, it is not yet clear whether the replication origins of plants contain specific essential sequences or whether origin sites are determined by features of chromatin structure. In all eukaryotes there are several biochemical events that must take place before initiation can occur. These are the marking of the origins by the origin recognition complex (ORC), the loading onto the origins, in a series of steps, of origin activation factors including the MCM proteins, and the initial denaturation of the double helix to form a replication \"bubble\". Only then can the enzymes that actually initiate replication, primase and DNA polymerase-alpha, gain access to the template. In many cells this complex series of events occurs only once per cell cycle, ensuring that DNA is not re-replicated within one cycle. However, regulated re-replication of DNA within one cell cycle (DNA endoreduplication) is relatively common in plants, indicating that the \"once-per-cycle\" controls can be overridden.","authors":"Bryant JA, Moore K, Aves SJ","authors_abbrev":"Bryant JA et al.","pubmed_publication_date":"Feb 2001","pubmed_entrez_date":"2001-04-03","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29464330","title":"The interplay of histone H2B ubiquitination with budding and fission yeast heterochromatin.","citation":"Curr Genet 2018 Aug;64(4):799-806","abstract":"Mono-ubiquitinated histone H2B (H2B-Ub) is important for chromatin regulation of transcription, chromatin assembly, and also influences heterochromatin. In this review, we discuss the effects of H2B-Ub from nucleosome to higher-order chromatin structure. We then assess what is currently known of the role of H2B-Ub in heterochromatic silencing in budding and fission yeasts (S. cerevisiae and S. pombe), which have distinct silencing mechanisms. In budding yeast, the SIR complex initiates heterochromatin assembly with the aid of a H2B-Ub deubiquitinase, Ubp10. In fission yeast, the RNAi-dependent pathway initiates heterochromatin in the context of low H2B-Ub. We examine how the different silencing machineries overcome the challenge of H2B-Ub chromatin and highlight the importance of using these microorganisms to further our understanding of H2B-Ub in heterochromatic silencing pathways.","doi":"10.1007/s00294-018-0812-1","authors":"Zukowski A, Johnson AM","authors_abbrev":"Zukowski A et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-02-22","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-02-28 22:13:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC577.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35474054","title":"Involvement of Sec71 and Ubp2 in tunicamycin-induced ER stress response in the fission yeast.","citation":"Mol Biol Rep 2022 Jun;49(6):4719-4726","abstract":"Accumulation of unfolded or misfolded proteins in the cellular environment result in ER stress and activates the unfolded protein response (UPR). The UPR alleviates ER stress and restores homeostasis, but it triggers cell death under prolonged stress. Here, we aimed to investigate the involvement of Sec71, an Arf-GEF involved in vesicular transport, in the tunicamycin-induced ER stress response. Since deubiquitinases and ER stress are known to be closely linked, we investigated this response by evaluating the potential role of Ubp2, a deubiquitinase, in the ER stress response in fission yeast.\nTunicamycin-induced ER stress responses were assessed by analyzing cell viability, apoptosis, intracellular oxidation levels, and proteasomal activities in sec71 and ubp2-deficient cells. The cell viability of Δsec71 and Δubp2 decreased after exposure to 0.5 µg/mL tunicamycin. Deleting either ubp2 or sec71 genes significantly decreased proteasomal activity and sensitized cells to ER stress, resulting in increased apoptosis compared with wild-type cells after tunicamycin treatment. DCFDA (2,7-dichlorodihydrofluorescein diacetate) reduction increased in correlation with apoptosis observed in the mutant cells, indicating higher levels of reactive oxygen species.\nThe results highlight the involvement of S. pombe Ubp2 in the known role of the ubiquitin-proteasome system in the ER stress response. We hypothesise that Sec71 is associated with ER homeostasis, and our findings on Sec71 provide new insight into the regulation of cell death mechanisms arising from the ER stress.","doi":"10.1007/s11033-022-07321-4","authors":"Yemenici M, Kartal Sural B, Karaer Uzuner S, Palabiyik B","authors_abbrev":"Yemenici M et al.","pubmed_publication_date":"Jun 2022","pubmed_entrez_date":"2022-04-27","publication_year":"2022","canto_session_key":"6edfe038e6750756","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-04-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31077324","title":"Fitness Landscape of the Fission Yeast Genome.","citation":"Mol Biol Evol 2019 Aug 01;36(8):1612-1623","abstract":"The relationship between DNA sequence, biochemical function, and molecular evolution is relatively well-described for protein-coding regions of genomes, but far less clear in noncoding regions, particularly, in eukaryote genomes. In part, this is because we lack a complete description of the essential noncoding elements in a eukaryote genome. To contribute to this challenge, we used saturating transposon mutagenesis to interrogate the Schizosaccharomyces pombe genome. We generated 31 million transposon insertions, a theoretical coverage of 2.4 insertions per genomic site. We applied a five-state hidden Markov model (HMM) to distinguish insertion-depleted regions from insertion biases. Both raw insertion-density and HMM-defined fitness estimates showed significant quantitative relationships to gene knockout fitness, genetic diversity, divergence, and expected functional regions based on transcription and gene annotations. Through several analyses, we conclude that transposon insertions produced fitness effects in 66-90% of the genome, including substantial portions of the noncoding regions. Based on the HMM, we estimate that 10% of the insertion depleted sites in the genome showed no signal of conservation between species and were weakly transcribed, demonstrating limitations of comparative genomics and transcriptomics to detect functional units. In this species, 3'- and 5'-untranslated regions were the most prominent insertion-depleted regions that were not represented in measures of constraint from comparative genomics. We conclude that the combination of transposon mutagenesis, evolutionary, and biochemical data can provide new insights into the relationship between genome function and molecular evolution.","doi":"10.1093/molbev/msz113","authors":"Grech L, Jeffares DC, Sadée CY, Rodríguez-López M, Bitton DA, Hoti M, Biagosch C, Aravani D, Speekenbrink M, Illingworth CJR, Schiffer PH, Pidoux AL, Tong P, Tallada VA, Allshire R, Levin HL, Bähler J","authors_abbrev":"Grech L et al.","pubmed_publication_date":"01 Aug 2019","pubmed_entrez_date":"2019-05-12","publication_year":"2019","canto_session_key":"169f8b58e39ba129","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-03-11 17:51:36","canto_approved_date":"2020-03-11 17:51:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-11 17:44:50","canto_added_date":"2019-05-13 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2020-03-11"},{"uniquename":"PMID:31152053","title":"Molecular mechanisms of chemotropism and cell fusion in unicellular fungi.","citation":"J Cell Sci 2019 May 31;132(11)","abstract":"In all eukaryotic phyla, cell fusion is important for many aspects of life, from sexual reproduction to tissue formation. Fungal cells fuse during mating to form the zygote, and during vegetative growth to connect mycelia. Prior to fusion, cells first detect gradients of pheromonal chemoattractants that are released by their partner and polarize growth in their direction. Upon pairing, cells digest their cell wall at the site of contact and merge their plasma membrane. In this Review, I discuss recent work on the chemotropic response of the yeast models  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe , which has led to a novel model of gradient sensing: the cell builds a motile cortical polarized patch, which acts as site of communication where pheromones are released and sensed. Initial patch dynamics serve to correct its position and align it with the gradient from the partner cell. Furthermore, I highlight the transition from cell wall expansion during growth to cell wall digestion, which is imposed by physical and signaling changes owing to hyperpolarization that is induced by cell proximity. To conclude, I discuss mechanisms of membrane fusion, whose characterization remains a major challenge for the future.","doi":"10.1242/jcs.230706","authors":"Martin SG","authors_abbrev":"Martin SG","pubmed_publication_date":"31 May 2019","pubmed_entrez_date":"2019-06-02","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-06-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:6953308","title":"Multiple drug resistance in the fission yeast Schizosaccharomyces pombe: evidence for the existence of pleiotropic mutations affecting dependent transport systems.","citation":"Mol Gen Genet 1982;185(2):311-4","abstract":"The uptake of L-tyrosine into wild type and antibiotic resistant strains of Schizosaccharomyces pombe requires an energy source, is initially linear with respect to time, is inhibited by 2,4-dinitrophenol and sodium azide and is saturable. However the initial uptake rates and the amount of L-tyrosine accummulated by antibiotic resistant strains are much less than wild type. Comparison of the kinetic constants of uptake shows that mutant strains have a reduced maximum velocity of uptake compared to wild type and a larger Km. Since the three mutant strains possess a permeability barrier to L-tyrosine as well as being drug resistant this is an indication that antibiotic resistance may be caused by a decrease in plasma membrane permeability.","authors":"Johnston PA, Coddington A","authors_abbrev":"Johnston PA et al.","pubmed_publication_date":"1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17898859","title":"Overexpression of a metacaspase gene stimulates cell growth and stress response in Schizosaccharomyces pombe.","citation":"Can J Microbiol 2007 Aug;53(8):1016-23","abstract":"A unique gene named pca1(+), encoding a metacaspase, was cloned from the fission yeast Schizosaccharomyces pombe and was used to create a recombinant plasmid, pPMC. The metacaspase mRNA level was markedly elevated in the fission yeast cells harboring the plasmid pPMC. Overexpressed Pca1(+) appeared to stimulate the growth of the fission yeast cells instead of arresting their growth. Its expression was enhanced by stress-inducing agents such as H(2)O(2), sodium nitroprusside, and CdCl(2), and it conferred cytoprotection, especially against CdCl(2). However, such protection was not reproducible in the budding yeast Saccharomyces cerevisiae harboring pPMC. Taken together, these results propose that Pca1(+) may be involved in the growth and stress response of the fission yeast.","authors":"Lim HW, Kim SJ, Park EH, Lim CJ","authors_abbrev":"Lim HW et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-09-28","publication_year":"2007","canto_session_key":"6217de6768711c23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-04 18:42:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-04 18:42:15","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-12-04"},{"uniquename":"PMID:36311347","title":"Analysis of Lipid-linked Oligosaccharides Synthesized  in vivo  in  Schizosaccharomyces pombe .","citation":"Bio Protoc 2022 Sep 20;12(18)","abstract":"Dolichol diphosphate-linked oligosaccharides (LLO) are the sugar donors in  N  -glycosylation, a fundamental protein post-translational modification of the eukaryotic secretory pathway. Defects in LLO biosynthesis produce human Congenital Disorders of Glycosylation Type I. The synthesis of LLOs and the transfer reactions to their protein acceptors is highly conserved among animal, plant, and fungi kingdoms, making the fission yeast  Schizosaccharomyces pombe  a suitable model to study these processes. Here, we present a protocol to determine the LLO patterns produced  in vivo  by  S. pombe  cells that may be easily adapted to other cell types. First, exponentially growing cultures are labeled with a pulse of [  14  C]-glucose. LLOs are then purified by successive extractions with organic solvents, and glycans are separated from the lipid moieties in mild acid hydrolysis and a new solvent extraction. The purified glycans are then run on paper chromatography. We use a deconvolution process to adjust the profile obtained to the minimal number of Gaussian functions needed to fit the data and determine the proportion of each species with respect to total glycan species present in the cell. The method we provide here might be used without any expensive or specialized equipment. The deconvolution process described here might also be useful to analyze species in non-completely resolved chromatograms. Graphical abstract: Workflow for the labeling, extraction, separation, and identification of LLO species in  S. pombe  . (A) Radioactive pulse of  S. pombe  cells with [  14  C]-glucose for 15 min at 28 °C. (B) Organic extraction of LLOs from labeled yeasts sequentially using methanol, chloroform, H  2  O, chloroform:methanol:H  2  O (1:1:0.3), 0.02 M HCl (to separate glycans from dolichol), and chloroform:methanol:H  2  O (1:16:16). (C) Preparation of the sample for chromatography on paper: drying by airflow and radioactivity check. (D) Loading of samples in chromatographic paper and descendent chromatography in a glass chamber. The obtained plots (CPM versus running distance) need to be analyzed to identify single glycan species.","doi":"10.21769/BioProtoc.4508","authors":"Valko A, Gallo GL, Weisz AD, Parodi AJ, D'Alessio C","authors_abbrev":"Valko A et al.","pubmed_publication_date":"20 Sep 2022","pubmed_entrez_date":"2022-10-31","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-11-02 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25143407","title":"Synergies between Aip1p and capping protein subunits (Acp1p and Acp2p) in clathrin-mediated endocytosis and cell polarization in fission yeast.","citation":"Mol Biol Cell 2014 Nov 05;25(22):3515-27","abstract":"Aip1p cooperates with actin-depolymerizing factor (ADF)/cofilin to disassemble actin filaments in vitro and in vivo, and is proposed to cap actin filament barbed ends. We address the synergies between Aip1p and the capping protein heterodimer Acp1p/Acp2p during clathrin-mediated endocytosis in fission yeast. Using quantitative microscopy and new methods we have developed for data alignment and analysis, we show that heterodimeric capping protein can replace Aip1p, but Aip1p cannot replace capping protein in endocytic patches. Our quantitative analysis reveals that the actin meshwork is organized radially and is compacted by the cross-linker fimbrin before the endocytic vesicle is released from the plasma membrane. Capping protein and Aip1p help maintain the high density of actin filaments in meshwork by keeping actin filaments close enough for cross-linking. Our experiments also reveal new cellular functions for Acp1p and Acp2p independent of their capping activity. We identified two independent pathways that control polarization of endocytic sites, one depending on acp2(+) and aip1(+) during interphase and the other independent of acp1(+), acp2(+), and aip1(+) during mitosis.","doi":"10.1091/mbc.E13-01-0005","authors":"Berro J, Pollard TD","authors_abbrev":"Berro J et al.","pubmed_publication_date":"05 Nov 2014","pubmed_entrez_date":"2014-08-22","publication_year":"2014","canto_session_key":"ac818fd20413ca1a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-08-23 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC12B10.07","SPAC631.01c","SPAC9G1.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10398679","title":"Heat-shock-induced activation of stress MAP kinase is regulated by threonine- and tyrosine-specific phosphatases.","citation":"Genes Dev 1999 Jul 01;13(13):1653-63","abstract":"In eukaryotic species from yeast to human, stress-activated protein kinases (SAPKs), members of a MAP kinase (MAPK) subfamily, regulate the transcriptional response to various environmental stress. It is poorly understood how diverse forms of stress are sensed and transmitted to SAPKs. Here, we report the heat shock regulation of the fission yeast Spc1 SAPK, a homolog of human p38 and budding yeast Hog1p. Although osmostress and oxidative stress induce strong activation of the Wis1 MAPK kinase (MEK), which activates Spc1 through Thr-171/Tyr-173 phosphorylation, activation of Wis1 upon heat shock is relatively weak and transient. However, in heat-shocked cells, Pyp1, the major tyrosine phosphatase that dephosphorylates and inactivates Spc1, is inhibited for its interaction with Spc1, which leads to strong activation of Spc1. Subsequently, Spc1 activity is rapidly attenuated by Thr-171 dephosphorylation, whereas Tyr-173 remains phosphorylated. Thr-171 dephosphorylation is compromised in a strain lacking functional type 2C serine/threonine phosphatases (PP2C), Ptc1 and Ptc3. Moreover, Ptc1 and Ptc3 can dephosphorylate Thr-171 of Spc1 both in vivo and in vitro. These observations strongly suggest that PP2C enzymes play an important role in the attenuation of Spc1 activity in heat-shocked cells. Thus, transient activation of Spc1 upon heat shock is ensured by differential regulation of threonine and tyrosine phosphorylation.","authors":"Nguyen AN, Shiozaki K","authors_abbrev":"Nguyen AN et al.","pubmed_publication_date":"01 Jul 1999","pubmed_entrez_date":"1999-07-10","publication_year":"1999","canto_session_key":"2fed9a1e695623df","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-04 10:11:17","canto_approved_date":"2025-06-12 05:53:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-06-09 09:51:18","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC24B11.06c","SPAC2G11.07c","SPAC26F1.10c","SPCC4F11.02","SPBC409.07c","SPCC1223.11"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-10-04"},{"uniquename":"EMBL:AU008616","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29550859","title":"Genetic interactions between the chromosome axis-associated protein Hop1 and homologous recombination determinants in Schizosaccharomyces pombe.","citation":"Curr Genet 2018 Oct;64(5):1089-1104","abstract":"Hop1 is a component of the meiosis-specific chromosome axis and belongs to the evolutionarily conserved family of HORMA domain proteins. Hop1 and its orthologs in higher eukaryotes are a major factor in promoting double-strand DNA break formation and inter-homolog recombination. In budding yeast and mammals, they are also involved in a meiotic checkpoint kinase cascade monitoring the completion of double-strand DNA break repair. We used the fission yeast, Schizosaccharomyces pombe, which lacks a canonical synaptonemal complex to test whether Hop1 has a role beyond supporting the generation of double-strand DNA breaks and facilitating inter-homolog recombination events. We determined how mutants of homologous recombination factors genetically interact with hop1, studied the role(s) of the HORMA domain of Hop1, and characterized a bio-informatically predicted interactor of Hop1, Aho1 (SPAC688.03c). Our observations indicate that in fission yeast, Hop1 does require its HORMA domain to support wild-type levels of meiotic recombination and localization to meiotic chromatin. Furthermore, we show that hop1∆ only weakly interacts genetically with mutants of homologous recombination factors, and in fission yeast likely has no major role beyond break formation and promoting inter-homolog events. We speculate that after the evolutionary loss of the synaptonemal complex, Hop1 likely has become less important for modulating recombination outcome during meiosis in fission yeast, and that this led to a concurrent rewiring of genetic pathways controlling meiotic recombination.","doi":"10.1007/s00294-018-0827-7","authors":"Brown SD, Jarosinska OD, Lorenz A","authors_abbrev":"Brown SD et al.","pubmed_publication_date":"Oct 2018","pubmed_entrez_date":"2018-03-19","publication_year":"2018","canto_session_key":"3d2e312d8e777c14","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-03-21 01:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.07","SPCC4G3.05c","SPBC1685.11","SPAC3C7.03c","SPBC1718.02"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"EMBL:AU006902","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23503588","title":"The exoribonuclease Dis3L2 defines a novel eukaryotic RNA degradation pathway.","citation":"EMBO J 2013 Jul 03;32(13):1842-54","abstract":"The final step of cytoplasmic mRNA degradation proceeds in either a 5'-3' direction catalysed by Xrn1 or in a 3'-5' direction catalysed by the exosome. Dis3/Rrp44, an RNase II family protein, is the catalytic subunit of the exosome. In humans, there are three paralogues of this enzyme: DIS3, DIS3L, and DIS3L2. In this work, we identified a novel Schizosaccharomyces pombe exonuclease belonging to the conserved family of human DIS3L2 and plant SOV. Dis3L2 does not interact with the exosome components and localizes in the cytoplasm and in cytoplasmic foci, which are docked to P-bodies. Deletion of dis3l2(+) is synthetically lethal with xrn1Δ, while deletion of dis3l2(+) in an lsm1Δ background results in the accumulation of transcripts and slower mRNA degradation rates. Accumulated transcripts show enhanced uridylation and in vitro Dis3L2 displays a preference for uridylated substrates. Altogether, our results suggest that in S. pombe, and possibly in most other eukaryotes, Dis3L2 is an important factor in mRNA degradation. Therefore, this novel 3'-5' RNA decay pathway represents an alternative to degradation by Xrn1 and the exosome.","doi":"10.1038/emboj.2013.63","authors":"Malecki M, Viegas SC, Carneiro T, Golik P, Dressaire C, Ferreira MG, Arraiano CM","authors_abbrev":"Malecki M et al.","pubmed_publication_date":"03 Jul 2013","pubmed_entrez_date":"2013-03-19","publication_year":"2013","canto_session_key":"99c47a6d111cc12a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-12-21 10:55:11","canto_approved_date":"2024-02-07 07:14:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-04-19 19:59:42","canto_added_date":"2013-04-02 21:52:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":42,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.14c","SPAC3G9.10c","SPAC2C4.07c","SPCC1840.11","SPCC338.11c","SPACUNK4.11c","SPAC22A12.12c","SPCC1739.07","SPBC115.01c","SPBC211.08c","SPBC17D1.03c","SPAC22E12.16c","SPAC17A5.14","SPAC1F3.01","SPBC26H8.10","SPAP8A3.05","SPCC757.08","SPBC3D6.08c","SPCC550.03c","SPBC16G5.10"],"gene_count":20,"ltp_gene_count":18,"approved_date":"2016-12-21"},{"uniquename":"EMBL:AU013491","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23236291","title":"Deciphering the transcriptional-regulatory network of flocculation in Schizosaccharomyces pombe.","citation":"PLoS Genet 2012;8(12):e1003104","abstract":"In the fission yeast Schizosaccharomyces pombe, the transcriptional-regulatory network that governs flocculation remains poorly understood. Here, we systematically screened an array of transcription factor deletion and overexpression strains for flocculation and performed microarray expression profiling and ChIP-chip analysis to identify the flocculin target genes. We identified five transcription factors that displayed novel roles in the activation or inhibition of flocculation (Rfl1, Adn2, Adn3, Sre2, and Yox1), in addition to the previously-known Mbx2, Cbf11, and Cbf12 regulators. Overexpression of mbx2(+) and deletion of rfl1(+) resulted in strong flocculation and transcriptional upregulation of gsf2(+)/pfl1(+) and several other putative flocculin genes (pfl2(+)-pfl9(+)). Overexpression of the pfl(+) genes singly was sufficient to trigger flocculation, and enhanced flocculation was observed in several combinations of double pfl(+) overexpression. Among the pfl1(+) genes, only loss of gsf2(+) abrogated the flocculent phenotype of all the transcription factor mutants and prevented flocculation when cells were grown in inducing medium containing glycerol and ethanol as the carbon source, thereby indicating that Gsf2 is the dominant flocculin. In contrast, the mild flocculation of adn2(+) or adn3(+) overexpression was likely mediated by the transcriptional activation of cell wall-remodeling genes including gas2(+), psu1(+), and SPAC4H3.03c. We also discovered that Mbx2 and Cbf12 displayed transcriptional autoregulation, and Rfl1 repressed gsf2(+) expression in an inhibitory feed-forward loop involving mbx2(+). These results reveal that flocculation in S. pombe is regulated by a complex network of multiple transcription factors and target genes encoding flocculins and cell wall-remodeling enzymes. Moreover, comparisons between the flocculation transcriptional-regulatory networks of Saccharomyces cerevisiae and S. pombe indicate substantial rewiring of transcription factors and cis-regulatory sequences.","doi":"10.1371/journal.pgen.1003104","authors":"Kwon EJ, Laderoute A, Chatfield-Reed K, Vachon L, Karagiannis J, Chua G","authors_abbrev":"Kwon EJ et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-12-14","publication_year":"2012","canto_session_key":"9cf15ade89e44016","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Gordon Chua","canto_approved_date":"2017-01-10 02:10:19","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-07-07 00:08:56","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Gordon Chua","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1742.01","SPCC1494.10","SPBC21B10.13c","SPCC736.08","SPBC29A10.08","SPAPB15E9.01c","SPBC359.04c","SPCC1223.13","SPCC188.09c","SPBC646.06c","SPBC317.01","SPAC1002.13c","SPBC15D4.02","SPBC1289.10c","SPAC977.07c","SPBC1289.15","SPBC947.04","SPAC1F8.06","SPAC4H3.03c","SPBC354.05c","SPAC186.01"],"gene_count":21,"ltp_gene_count":21,"approved_date":"2016-07-07"},{"uniquename":"PMID:16215171","title":"Rho4 GTPase is involved in secretion of glucanases during fission yeast cytokinesis.","citation":"Eukaryot Cell 2005 Oct;4(10):1639-45","abstract":"Rho GTPases are regulators of signaling pathways that control actin organization and cell polarity processes in all eukaryotic cells. In Schizosaccharomyces pombe, Rho4p is involved in the regulation of septum degradation during cytokinesis. Here we show that Rho4p participates in the secretion of the glucanases Eng1p and Agn1p, which are responsible for the septum degradation. First, eng1+ or agn1+ overexpression suppressed the rho4delta multiseptation phenotype, and simultaneous overproduction of Rho4p and Eng1p or of Rho4p and Agn1p caused a dramatic lysis. Second, Rho4p was not necessary for Eng1p-mediated glucanase activity as measured in cell extracts; however, rho4delta cells have a lower level of (1,3)-beta-D-glucanase activity in the culture medium. Additionally, Eng1- or Agn1-green fluorescent protein did not properly localize to the septum in rho4delta cells grown at 37 degrees C. There was a decreased amount of these enzymes in the cell wall and in the culture medium of rho4delta cells at 37 degrees C. These results provide evidence that Rho4p is involved in the regulation of Eng1p and Agn1p secretion during cytokinesis.","authors":"Santos B, Martín-Cuadrado AB, Vázquez de Aldana CR, del Rey F, Pérez P","authors_abbrev":"Santos B et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-10-11","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.09","SPAC16A10.04","SPAC14C4.09"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11739799","title":"Localization of fission yeast type II myosin, Myo2, to the cytokinetic actin ring is regulated by phosphorylation of a C-terminal coiled-coil domain and requires a functional septation initiation network.","citation":"Mol Biol Cell 2001 Dec;12(12):4044-53","abstract":"Myo2 truncations fused to green fluorescent protein (GFP) defined a C-terminal domain essential for the localization of Myo2 to the cytokinetic actin ring (CAR). The localization domain contained two predicted phosphorylation sites. Mutation of serine 1518 to alanine (S(1518)A) abolished Myo2 localization, whereas Myo2 with a glutamic acid at this position (S(1518)E) localized to the CAR. GFP-Myo2 formed rings in the septation initiation kinase (SIN) mutant cdc7-24 at 25 degrees C but not at 36 degrees C. GFP-Myo2S(1518)E rings persisted at 36 degrees C in cdc7-24 but not in another SIN kinase mutant, sid2-250. To further examine the relationship between Myo2 and the SIN pathway, the chromosomal copy of myo2(+) was fused to GFP (strain myo2-gc). Myo2 ring formation was abolished in the double mutants myo2-gc cdc7.24 and myo2-gc sid2-250 at the restrictive temperature. In contrast, activation of the SIN pathway in the double mutant myo2-gc cdc16-116 resulted in the formation of Myo2 rings which subsequently collapsed at 36 degrees C. We conclude that the SIN pathway that controls septation in fission yeast also regulates Myo2 ring formation and contraction. Cdc7 and Sid2 are involved in ring formation, in the case of Cdc7 by phosphorylation of a single serine residue in the Myo2 tail. Other kinases and/or phosphatases may control ring contraction.","authors":"Mulvihill DP, Barretto C, Hyams JS","authors_abbrev":"Mulvihill DP et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-12-12","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1739.11c","SPBC244.01c","SPAC1565.06c","SPBC21.06c","SPCC645.05c","SPAC24B11.11c","SPAC6F6.08c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:17072884","title":"Comparative analysis of regulatory transcription factors in Schizosaccharomyces pombe and budding yeasts.","citation":"Yeast 2006 Oct 15;23(13):929-35","abstract":"Regulatory transcription factors (rTFs), which bind specific DNA sequences in the regulatory regions of genes and subsequently activate or repress transcription, play a central role in programming genomic expression. The number of rTFs in a species might therefore reflect its functional complexity. For simple organisms like yeast, a relatively small number of rTFs might be expected that is fairly constant between yeast species. We show that the budding yeast, Saccharomyces cerevisiae, contains 201 rTfs, which is one of the largest rTF numbers found in yeast species for which genome sequences are available. This is a much higher number than the 129 rTFs found in the fission yeast, Schizosaccharomyces pombe, which is currently the yeast with the lowest number of rTFs. Comparative analysis of several different budding yeast species shows that most of the 'extra' rTFs found in S. cerevisiae were probably acquired as a result of a whole genome duplication (WGD) event that occurred in an ancestor of a subset of budding yeast species. However, we also show that budding yeast species that have not been affected by the WGD contain a greater number of rTFs than S. pombe (mean = 145). Thus, two or more mechanisms have led to the 60% increase in rTFs in S. cerevisiae compared to S. pombe. This difference may correlate with a more extensive functional divergence in budding yeasts compared to fission yeasts. The relatively small number of rTFs in S. pombe make this organism an attractive model for global studies of mechanisms that programme gene expression.","authors":"Beskow A, Wright AP","authors_abbrev":"Beskow A et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9076725","title":"Region-specific meiotic recombination in Schizosaccharomyces pombe: the rec11 gene.","citation":"Mol Microbiol 1997 Mar;23(5):869-78","abstract":"Mutations in the rec11 gene of Schizosaccharomyces pombe reduce meiotic recombinant frequencies by as much as a factor of 300 on chromosome III but less than a factor of 4 in the intervals tested on chromosomes I and II. To gain insight into the function of this region- (or chromosome-) specific activator of recombination, we have cloned and sequenced the rec11 gene. Meiotic crosses with rec11 disruption mutations placed the rec11 gene 6 cM from ade6 on chromosome III. Transcripts of rec11 accumulated transiently at 2-3 h after induction of melosis in a pat1-114 (Ts) mutant. Reverse transcriptase/polymerase chain reaction (RT-PCR) analysis of these transcripts revealed eight introns. The spliced RNA is predicted to encode a polypeptide of 923 amino acids with only very limited homology to reported proteins. The transient accumulation of rec11 transcripts and the phenotype of rec11 mutations suggest that the novel rec11 gene product acts early in meiosis to activate recombination preferentially on chromosome III.","authors":"Li YF, Numata M, Wahls WP, Smith GR","authors_abbrev":"Li YF et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_session_key":"d41294b6eddd9962","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-07 08:36:27","canto_approved_date":"2018-06-07 08:36:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-06-07 08:36:18","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13","SPCC4E9.01c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2018-06-07"},{"uniquename":"PMID:5124491","title":"Synthesis of soluble protein during the cell cycle of the fission yeast Schizosaccharomyces pombe.","citation":"Exp Cell Res 1971 Nov;69(1):49-56","abstract":"","authors":"Wain WH","authors_abbrev":"Wain WH","pubmed_publication_date":"Nov 1971","pubmed_entrez_date":"1971-11-01","publication_year":"1971","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1409592","title":"Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts.","citation":"Proc Natl Acad Sci U S A 1992 Oct 01;89(19):8966-70","abstract":"A cDNA encoding the dihydroorotate dehydrogenase (DHOdehase; EC 1.3.3.1) of the yeast Schizosaccharomyces pombe was isolated by functional complementation in Saccharomyces cerevisiae. A divergent subcellular compartmentation of the DHOdehase of each yeast was shown. The DHOdehase from Sch. pombe was localized in the mitochondria whereas its homolog from S. cerevisiae was found to be cytosolic. The heterologous expression of the Sch. pombe enzyme in S. cerevisiae allowed us to demonstrate that the Sch. pombe DHOdehase activity requires the integrity of the mitochondrial electron transport chain. Indeed, the presence of a mutation inactivating cytochrome b abolished the complementation of a S. cerevisiae ura1 mutant by the corresponding Sch. pombe gene. By contrast, in vitro studies have revealed that the DHOdehase of S. cerevisiae uses fumarate as terminal electron acceptor. These results are discussed in relation to the anaerobic growth competence of the two yeasts and to the fermentative processes they use.","authors":"Nagy M, Lacroute F, Thomas D","authors_abbrev":"Nagy M et al.","pubmed_publication_date":"01 Oct 1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_session_key":"587647b862359000","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-02-26 16:27:19","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-02-26 16:27:08","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A10.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-26"},{"uniquename":"PMID:30673600","title":"Analysis of the S. pombe Meiotic Proteome Reveals a Switch from Anabolic to Catabolic Processes and Extensive Post-transcriptional Regulation.","citation":"Cell Rep 2019 Jan 22;26(4):1044-1058.e5","abstract":"Meiotic progression in S. pombe is regulated by stage-specific gene expression and translation, changes in RNA stability, expression of anti-sense transcripts, and targeted proteolysis of regulatory proteins. We have used SILAC labeling to examine the relative levels of proteins in diploid S. pombe cells during meiosis. Among the 3,268 proteins quantified at all time points, the levels of 880 proteins changed at least 2-fold; the majority of proteins showed stepwise increases or decreases during the meiotic divisions, while some changed transiently. Overall, we observed reductions in proteins involved in anabolism and increases in proteins involved in catabolism. We also observed increases in the levels of proteins of the ESCRT-III complex and revealed a role for ESCRT-III components in chromosome segregation and spore formation. Correlation with studies of meiotic gene expression and ribosome occupancy reveals that many of the changes in steady-state protein levels are post-transcriptional.","doi":"10.1016/j.celrep.2018.12.075","authors":"Krapp A, Hamelin R, Armand F, Chiappe D, Krapp L, Cano E, Moniatte M, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"22 Jan 2019","pubmed_entrez_date":"2019-01-24","publication_year":"2019","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-01-25 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2491312","title":"Continuous fermentation with yeast (Shizosaccharomyces pombe) floccules for ethanol production.","citation":"Chin J Biotechnol 1989;5(1):55-63","abstract":"This paper describes an experimental study of continuous fermentation of saccharified starch solution to produce ethanol with yeast particles of a highly flocculent strain of Schizosaccharomyces pombe, which were treated as immobilized microbial cells. Observations were initially made on yeast floccule characteristics during fermentation. An aeration-type fluidized-bed bioreactor that retained virtually all the yeast particles was built and operated continuously for 3 months. Bioreactor operation was found to be quite favorable for this fermentation system. The yeast concentration exceeded 40 g (dry mass)/liter; delivery of a limited amount of supplementary oxygen enhanced throughput to give levels as high as 20-24 g/liter.hr. The kinetic equations were also determined.","authors":"Feng PS, Xu GL, Zhao Y, Huang YH","authors_abbrev":"Feng PS et al.","pubmed_publication_date":"1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21115488","title":"Differential activities of three families of specific beta(1,3)glucan synthase inhibitors in wild-type and resistant strains of fission yeast.","citation":"J Biol Chem 2011 Feb 04;286(5):3484-96","abstract":"Three specific β(1,3)glucan synthase (GS) inhibitor families, papulacandins, acidic terpenoids, and echinocandins, have been analyzed in Schizosaccharomyces pombe wild-type and papulacandin-resistant cells and GS activities. Papulacandin and enfumafungin produced similar in vivo effects, different from that of echinocandins. Also, papulacandin was the strongest in vitro GS inhibitor (IC(50) 10(3)-10(4)-fold lower than with enfumafungin or pneumocandin), but caspofungin was by far the most efficient antifungal because of the following. 1) It was the only drug that affected resistant cells (minimal inhibitory concentration close to that of the wild type). 2) It was a strong inhibitor of wild-type GS (IC(50) close to that of papulacandin). 3) It was the best inhibitor of mutant GS. Moreover, caspofungin showed a special effect for two GS inhibition activities, of high and low affinity, separated by 2 log orders, with no increase in inhibition. pbr1-8 and pbr1-6 resistances are due to single substitutions in the essential Bgs4 GS, located close to the resistance hot spot 1 region described in Saccharomyces and Candida Fks mutants. Bgs4(pbr)(1-8) contains the E700V change, four residues N-terminal from hot spot 1 defining a larger resistance hot spot 1-1 of 13 amino acids. Bgs4(pbr)(1-6) contains the W760S substitution, defining a new resistance hot spot 1-2. We observed spontaneous revertants of the spherical pbr1-6 phenotype and found that an additional A914V change is involved in the recovery of the wild-type cell shape, but it maintains the resistance phenotype. A better understanding of the mechanism of action of the antifungals available should help to improve their activity and to identify new antifungal targets.","doi":"10.1074/jbc.M110.174300","authors":"Martins IM, Cortés JC, Muñoz J, Moreno MB, Ramos M, Clemente-Ramos JA, Durán A, Ribas JC","authors_abbrev":"Martins IM et al.","pubmed_publication_date":"04 Feb 2011","pubmed_entrez_date":"2010-12-01","publication_year":"2011","canto_session_key":"0fc4857a96667cda","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-17 18:18:38","canto_approved_date":"2019-05-02 22:31:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-17 18:18:30","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-17"},{"uniquename":"PMID:2836064","title":"Expression of the SV40 promoter in fission yeast: identification and characterization of an AP-1-like factor.","citation":"Cell 1988 May 20;53(4):659-67","abstract":"The SV40 promoter is expressed well in the fission yeast S. pombe, and it initiates transcription at the same site as in mammalian cells. The majority of the enhancer sequences, however, do not contribute to this activity. DNAase I footprint analysis of the promoter revealed the presence of an AP-1-like factor in S. pombe cells that protects a region of the promoter almost identical to that protected by human AP-1. The specificity of binding of the yeast and mammalian AP-1 proteins was found to be similar. We have found two AP-1-like binding activities in budding yeast cells, one of which appears quite distinct from the binding activity of the product of the budding yeast GCN4 gene. We also demonstrate that in fission yeast the AP-1 binding site can act as an upstream activating sequence. The DNA-protein complexes containing the mammalian AP-1 and fission yeast AP-1-like factors are sensitive to phosphatase treatment, indicating that they may be phosphorylated.","authors":"Jones RH, Moreno S, Nurse P, Jones NC","authors_abbrev":"Jones RH et al.","pubmed_publication_date":"20 May 1988","pubmed_entrez_date":"1988-05-20","publication_year":"1988","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D87870","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15716270","title":"Identification and functional analysis of 20 Box H/ACA small nucleolar RNAs (snoRNAs) from Schizosaccharomyces pombe.","citation":"J Biol Chem 2005 Apr 22;280(16):16446-55","abstract":"Considering all small nucleolar RNAs (snoRNAs) enriched in the nucleolus, we generated a specialized cDNA library of small nuclear RNAs from Schizosaccharomyces pombe and isolated, for the first time, 20 novel box H/ACA snoRNAs. Thirteen of these were characterized as novel guides that were predicted to direct 19 pseudouridylations in 18 S and 25 S rRNAs. The remaining seven snoRNAs were considered as orphan guides that lack sequence complementarity to either rRNAs or snRNAs. We have experimentally demonstrated the function of the 10 novel snoRNAs by gene deletion in the fission yeast. The snoRNAs were shown to be dispensable for the viability of S. pombe, although an impact of snR94 depletion on yeast growth, especially at 23 degrees C, was revealed. A total of 30 pseudouridylation sites were precisely mapped in the S. pombe rRNAs, showing a distinctive pseudouridylation pattern in the budding yeast. Interestingly, the absence of pseudouridylation on U2347 in S. pombe 25 S rRNA pointed out a critical role for Psi2345 in conferring a growth advantage for yeast. In contrast to the intron-encoded box C/D sno-RNAs in yeast, all box H/ACA snoRNAs appeared to be transcribed independently from intergenic regions between two protein-coding genes, except for snR35, which was nested in an open reading frame encoding for a hypothetical protein, although expressed from the opposite strand. Remarkably, snR90 was cotranscribed with an intron-encoded box C/D snoRNA, and this is the first demonstration of a non-coding RNA gene that encodes two different types of snoRNAs by its exon and intron. A detailed comparison of the S. pombe snoRNAs, with their functional homologues in diverse organisms, suggests a mechanism by which the snoRNAs have evolved in coordination with rRNAs to preserve the post-transcriptional modification sites among distant eukaryotes.","authors":"Li SG, Zhou H, Luo YP, Zhang P, Qu LH","authors_abbrev":"Li SG et al.","pubmed_publication_date":"22 Apr 2005","pubmed_entrez_date":"2005-02-18","publication_year":"2005","canto_session_key":"1f6155a543ea7508","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-08-19 12:26:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-19 12:23:07","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":60,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNORNA.48","SPSNORNA.44","SPSNORNA.38","SPSNORNA.47","SPSNORNA.32","SPSNORNA.34","SPSNORNA.45","SPSNORNA.52","SPSNORNA.41","SPSNORNA.33","SPSNORNA.49","SPSNORNA.39","SPSNORNA.35","SPSNORNA.40","SPSNORNA.50","SPSNORNA.42","SPSNORNA.43","SPSNORNA.46","SPSNORNA.37","SPSNORNA.36"],"gene_count":20,"ltp_gene_count":10,"approved_date":"2014-08-19"},{"uniquename":"PMID:32160539","title":"Telomerase Repairs Collapsed Replication Forks at Telomeres.","citation":"Cell Rep 2020 Mar 10;30(10):3312-3322.e3","abstract":"Telomeres are difficult-to-replicate sites whereby replication itself may threaten telomere integrity. We investigate, in fission yeast, telomere replication dynamics in telomerase-negative cells to unmask problems associated with telomere replication. Two-dimensional gel analysis reveals that replication of telomeres is severely impaired and correlates with an accumulation of replication intermediates that arises from stalled and collapsed forks. In the absence of telomerase, Rad51, Mre11-Rad50-Nbs1 (MRN) complex, and its co-factor CtIP Ctp1  become critical to maintain telomeres, indicating that homologous recombination processes these intermediates to facilitate fork restart. We further show that a catalytically dead mutant of telomerase prevents Ku recruitment to telomeres, suggesting that telomerase and Ku both compete for the binding of telomeric-free DNA ends that are likely to originate from a reversed fork. We infer that Ku removal at collapsed telomeric forks allows telomerase to repair broken telomeres, thereby shielding telomeres from homologous recombination.","doi":"10.1016/j.celrep.2020.02.065","authors":"Matmati S, Lambert S, Géli V, Coulon S","authors_abbrev":"Matmati S et al.","pubmed_publication_date":"10 Mar 2020","pubmed_entrez_date":"2020-03-12","publication_year":"2020","canto_session_key":"54cef077088c3a22","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-03-13 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC10828","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9654085","title":"Phosphatidylinositol 4-kinases.","citation":"Eur J Biochem 1998 Apr 15;253(2):357-70","abstract":"Polyphosphoinositides are involved in many signal transduction pathways in eukaryotic cells. The first committed step is catalysed by phosphatidylinositol 4-kinase leading to the formation of phosphatidylinositol 4-phosphate. In the last four years, ten cDNA molecules have been cloned which code isoforms of phosphatidylinositol 4-kinase; some of which are highly related. Characteristically, they contain a C-terminal catalytic domain which is similar to that of (poly)phosphoinositide 3-kinases and to that of more distantly related lipid/protein kinases. Alignment has characterised cDNAs from Chaenorabditis, Dictyostelium and Schizostaphyloccus pombe as those of phosphatidylinositol 4-kinases also. All these lipid kinases are related to the superfamily of protein kinases. Several amino acids are highly conserved in catalytic domains of lipid and protein kinases. Employing the catalytic subunit of the cAMP-dependent protein kinase as template, these residues can be assigned functionally. On the basis of the alignment, a phylogenetic tree of the superfamily of phosphatidylinositol kinases has been constructed. Three families, the phosphatidylinositol 4-kinases, phosphoinositide 3-kinases, and the phosphatidylinositol related lipid/protein kinases, can be recognised. Each family comprises two subfamilies. The involvement of the phosphatidylinositol 4-kinases in signal transduction processes is summarised and a new hypothesis for the function of their isoforms in polyphosphoinositide signalling is presented. The involvement of phosphatidylinositol 4-kinases in formation of lipid-protein interactions with cytoskeleton proteins and the metabolism of polyphosphoinositide in the nucleus is discussed.","authors":"Gehrmann T, Heilmeyer LM","authors_abbrev":"Gehrmann T et al.","pubmed_publication_date":"15 Apr 1998","pubmed_entrez_date":"1998-07-08","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39906711","title":"Structure simulation-based comparison of active site variations in fungal ornithine decarboxylases.","citation":"Commun Integr Biol 2025;18(1):2458872","abstract":"Polyamines play crucial roles in various biological processes, including cell proliferation and differentiation, immune response modulation, and signal transduction. Ornithine decarboxylase (ODC) initiates polyamine biosynthesis by catalyzing the conversion of ornithine to putrescine in a pyridoxal phosphate (PLP)-dependent manner. While the structures of mammalian and protozoan ODCs have been elucidated, fungal ODCs remain uncharacterized. In this study, AlphaFold2 was employed to simulate the structures of ODCs from four fungi:  Kluyveromyces lactis ,  Candida albicans ,  Debaryomyces hansenii , and  Schizosaccharomyces pombe . The results indicated that, although these ODCs share α/β-barrel and β-sheet domains, their active site conformations exhibit subtle differences. Additionally, substrate selectivity among ODCs and related decarboxylases varied depending on the distance between the Cα of aspartate or glutamate residues within the specificity helix and the C4α of PLP. Notably, the bacterial  Campylobacter jejuni  decarboxylase ( Cj CANSDC), which binds the largest substrate, exhibits the longest distance, whereas fungal ODC, which binds the smallest substrate, displays the shortest distance. Furthermore, significant differences in the composition of amino acid residues within the active sites were also observed. This study provides insights into the structural diversity and catalytic activity of ODCs across a broad range of organisms, advancing the understanding of structure-dependent evolutionary processes.","doi":"10.1080/19420889.2025.2458872","authors":"Kim MJ, Chang JH","authors_abbrev":"Kim MJ et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-02-05","publication_year":"2025","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2025-02-06 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22771993","title":"Distinct requirement of RNA polymerase II CTD phosphorylations in budding and fission yeast.","citation":"Transcription 2012;3(5):231-4","abstract":"The \"CTD code\" links the combinatorial potential of the modifications found on the Rpb1 C-terminal domain (CTD) to the growing group of CTD binding effectors. The genetic dissection of serine 2 and serine 7 function within the CTD in both budding and fission yeast reveals distinct in vivo requirement.","doi":"10.4161/trns.21066","authors":"Cassart C, Drogat J, Migeot V, Hermand D","authors_abbrev":"Cassart C et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-07-10","publication_year":"2012","canto_session_key":"c0fbec3401e0d808","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-31 10:25:46","canto_approved_date":"2022-11-17 23:21:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-21 12:46:40","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPBC28F2.12"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-01-31"},{"uniquename":"PMID:9148953","title":"Regulation of Schizosaccharomyces pombe Wee1 tyrosine kinase.","citation":"J Biol Chem 1997 May 16;272(20):13320-5","abstract":"Wee1 tyrosine kinase regulates mitosis by carrying out the inhibitory tyrosine 15 phosphorylation of Cdc2 M-phase inducing kinase. Schizosaccharomyces pombe Wee1 is a large protein, consisting of a C-terminal catalytic domain of approximately 350 amino acids preceded by a N-terminal domain of approximately 550 residues. The functional properties of the Wee1 N-terminal domain were investigated by expressing truncated forms of Wee1 in S. pombe. Both positive and negative regulatory domains were identified. Sequences important for Wee1 function were mapped to a central region (residues 363-408). This region is not required for kinase activity or nuclear localization, suggesting it may be involved in substrate recognition. The negative regulatory domain resides in the N-terminal third of Wee1, Wee1 constructs lacking this domain are more effective at delaying mitosis than wild-type Wee1. The negative regulatory domain contains clusters of potential Cdc2 phosphorylation sites. Investigations to monitor the abundance of Wee1 mRNA and protein during the cell cycle were also carried out.","authors":"Aligue R, Wu L, Russell P","authors_abbrev":"Aligue R et al.","pubmed_publication_date":"16 May 1997","pubmed_entrez_date":"1997-05-16","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19328067","title":"TFIIH and P-TEFb coordinate transcription with capping enzyme recruitment at specific genes in fission yeast.","citation":"Mol Cell 2009 Mar 27;33(6):738-51","abstract":"Cyclin-dependent kinases (CDKs) are subunits of transcription factor (TF) IIH and positive transcription elongation factor b (P-TEFb). To define their functions, we mutated the TFIIH-associated kinase Mcs6 and P-TEFb homologs Cdk9 and Lsk1 of fission yeast, making them sensitive to inhibition by bulky purine analogs. Selective inhibition of Mcs6 or Cdk9 blocks cell division, alters RNA polymerase (Pol) II carboxyl-terminal domain (CTD) phosphorylation, and represses specific, overlapping subsets of transcripts. At a common target gene, both CDKs must be active for normal Pol II occupancy, and Spt5-a CDK substrate and regulator of elongation-accumulates disproportionately to Pol II when either kinase is inhibited. In contrast, Mcs6 activity is sufficient-and necessary-to recruit the Cdk9/Pcm1 (mRNA cap methyltransferase) complex. In vitro, phosphorylation of the CTD by Mcs6 stimulates subsequent phosphorylation by Cdk9. We propose that TFIIH primes the CTD and promotes recruitment of P-TEFb/Pcm1, serving to couple elongation and capping of select pre-mRNAs.","doi":"10.1016/j.molcel.2009.01.029","authors":"Viladevall L, St Amour CV, Rosebrock A, Schneider S, Zhang C, Allen JJ, Shokat KM, Schwer B, Leatherwood JK, Fisher RP","authors_abbrev":"Viladevall L et al.","pubmed_publication_date":"27 Mar 2009","pubmed_entrez_date":"2009-03-31","publication_year":"2009","canto_session_key":"a7c6118865e72409","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-03-06 16:43:42","canto_approved_date":"2024-08-02 06:22:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-25 13:24:16","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC2F3.15","SPCC330.10","SPBC32H8.10","SPBC28F2.12","SPBC19F8.07","SPAC16C9.06c","SPAC821.09","SPAC23C4.19"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2017-03-06"},{"uniquename":"PMID:1320960","title":"Fission yeast sts1+ gene encodes a protein similar to the chicken lamin B receptor and is implicated in pleiotropic drug-sensitivity, divalent cation-sensitivity, and osmoregulation.","citation":"Mol Biol Cell 1992 Mar;3(3):263-73","abstract":"The Schizosaccharomyces pombe sts1+ gene, identified by supersensitive mutations to a protein kinase inhibitor, staurosporine, was isolated by complementation by the use of a fission yeast genomic library. Nucleotide sequencing shows that the sts1+ gene encodes a 453 amino acid putative membrane-associated protein that is significantly similar (26% identity) to the chicken lamin B receptor. It is also highly related (53% identity) to a budding yeast ORF, YGL022. These three proteins contain a similar hydrophobicity pattern consisting of eight or nine putative transmembrane domains. By gene disruption we demonstrate that the sts1+ gene is not essential for viability. These disruptants exhibit pleiotropic defects, such as cold-sensitivity for growth and at the permissive temperature, a supersensitivity to divalent cations and several unrelated drugs including staurosporine, caffeine, chloramphenicol, sorbitol, and SDS. Disruption of the sts1+ gene does not lead to a sensitivity to thiabendazole or hydroxyurea.","authors":"Shimanuki M, Goebl M, Yanagida M, Toda T","authors_abbrev":"Shimanuki M et al.","pubmed_publication_date":"Mar 1992","pubmed_entrez_date":"1992-03-01","publication_year":"1992","canto_session_key":"c3d01351db39b353","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-12-15 15:41:20","canto_approved_date":"2023-03-28 07:50:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-21 15:56:37","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-15"},{"uniquename":"PMID:35213692","title":"HEATR3 variants impair nuclear import of uL18 (RPL5) and drive Diamond-Blackfan anemia.","citation":"Blood 2022 May 26;139(21):3111-3126","abstract":"The congenital bone marrow failure syndrome Diamond-Blackfan anemia (DBA) is typically associated with variants in ribosomal protein (RP) genes impairing erythroid cell development. Here we report multiple individuals with biallelic HEATR3 variants exhibiting bone marrow failure, short stature, facial and acromelic dysmorphic features, and intellectual disability. These variants destabilize a protein whose yeast homolog is known to synchronize the nuclear import of RPs uL5 (RPL11) and uL18 (RPL5), which are both critical for producing ribosomal subunits and for stabilizing the p53 tumor suppressor when ribosome biogenesis is compromised. Expression of HEATR3 variants or repression of HEATR3 expression in primary cells, cell lines of various origins, and yeast models impairs growth, differentiation, pre-ribosomal RNA processing, and ribosomal subunit formation reminiscent of DBA models of large subunit RP gene variants. Consistent with a role of HEATR3 in RP import, HEATR3-depleted cells or patient-derived fibroblasts display reduced nuclear accumulation of uL18. Hematopoietic progenitor cells expressing HEATR3 variants or small-hairpin RNAs knocking down HEATR3 synthesis reveal abnormal acceleration of erythrocyte maturation coupled to severe proliferation defects that are independent of p53 activation. Our study uncovers a new pathophysiological mechanism leading to DBA driven by biallelic HEATR3 variants and the destabilization of a nuclear import protein important for ribosome biogenesis.","doi":"10.1182/blood.2021011846","authors":"O'Donohue MF, Da Costa L, Lezzerini M, Unal S, Joret C, Bartels M, Brilstra E, Scheijde-Vermeulen M, Wacheul L, De Keersmaecker K, Vereecke S, Labarque V, Saby M, Lefevre SD, Platon J, Montel-Lehry N, Laugero N, Lacazette E, van Gassen K, Houtkooper RH, Simsek-Kiper PO, Leblanc T, Yarali N, Cetinkaya A, Akarsu NA, Gleizes PE, Lafontaine DLJ, MacInnes AW","authors_abbrev":"O'Donohue MF et al.","pubmed_publication_date":"26 May 2022","pubmed_entrez_date":"2022-02-25","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1703.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18441123","title":"Loss of regulators of vacuolar ATPase function and ceramide synthesis results in multidrug sensitivity in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2008 Jun;7(6):926-37","abstract":"We undertook a screen to isolate determinants of drug resistance in fission yeast and identified two genes that, when mutated, result in sensitivity to a range of structurally unrelated compounds, some of them commonly used in the clinic. One gene, rav1, encodes the homologue of a budding yeast protein which regulates the assembly of the vacuolar ATPase. The second gene, lac1, encodes a homologue of genes that are required for ceramide synthesis. Both mutants are sensitive to the chemotherapeutic agent doxorubicin, and using the naturally fluorescent properties of this compound, we found that both rav1 and lac1 mutations result in an increased accumulation of the drug in cells. The multidrug-sensitive phenotype of rav1 mutants can be rescued by up-regulation of the lag1 gene which encodes a homologue of lac1, whereas overexpression of either lac1 or lag1 confers multidrug resistance on wild-type cells. These data suggest that changing the amount of ceramide synthase activity in cells can influence innate drug resistance. The function of Rav1 appears to be conserved, as we show that SpRav1 is part of a RAVE-like complex in fission yeast and that loss of rav1 results in defects in vacuolar (H(+))-ATPase activity. Thus, we conclude that loss of normal V-ATPase function results in an increased sensitivity of Schizosaccharomyces pombe cells to drugs. The rav1 and lac1 genes are conserved in both higher eukaryotes and various pathogenic fungi. Thus, our data could provide the basis for strategies to sensitize tumor cells or drug-resistant pathogenic fungi to drugs.","doi":"10.1128/EC.00037-08","authors":"Dawson K, Toone WM, Jones N, Wilkinson CR","authors_abbrev":"Dawson K et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-29","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3E7.15c","SPAC1A6.09c","SPBC409.05","YDR202C","SPAC637.05c","SPBC3H7.12","SPBC1105.10"],"gene_count":6,"ltp_gene_count":5},{"uniquename":"PMID:18215152","title":"TOR regulation of AGC kinases in yeast and mammals.","citation":"Biochem J 2008 Feb 15;410(1):19-37","abstract":"The TOR (target of rapamycin), an atypical protein kinase, is evolutionarily conserved from yeast to man. Pharmacological studies using rapamycin to inhibit TOR and yeast genetic studies have provided key insights on the function of TOR in growth regulation. One of the first bona fide cellular targets of TOR was the mammalian protein kinase p70 S6K (p70 S6 kinase), a member of a family of kinases called AGC (protein kinase A/protein kinase G/protein kinase C-family) kinases, which include PKA (cAMP-dependent protein kinase A), PKG (cGMP-dependent kinase) and PKC (protein kinase C). AGC kinases are also highly conserved and play a myriad of roles in cellular growth, proliferation and survival. The AGC kinases are regulated by a common scheme that involves phosphorylation of the kinase activation loop by PDK1 (phosphoinositide-dependent kinase 1), and phosphorylation at one or more sites at the C-terminal tail. The identification of two distinct TOR protein complexes, TORC1 (TOR complex 1) and TORC2, with different sensitivities to rapamycin, revealed that TOR, as part of either complex, can mediate phosphorylation at the C-terminal tail for optimal activation of a number of AGC kinases. Together, these studies elucidated that a fundamental function of TOR conserved throughout evolution may be to balance growth versus survival signals by regulating AGC kinases in response to nutrients and environmental conditions. This present review highlights this emerging function of TOR that is conserved from budding and fission yeast to mammals.","doi":"10.1042/BJ20071518","authors":"Jacinto E, Lorberg A","authors_abbrev":"Jacinto E et al.","pubmed_publication_date":"15 Feb 2008","pubmed_entrez_date":"2008-01-25","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40018908","title":"Label-free differentiation of living  versus  dead single yeast cells using broadband electrical impedance spectroscopy.","citation":"Lab Chip 2025 Feb 28;","abstract":"The use of the intrinsic electrical properties of a single cell by broadband electrical impedance spectroscopy (EIS) as a label-free and non-invasive method to monitor cellular and intracellular features is an emerging field. Here, we present a novel EIS-based sheathless microfluidic platform with an integrated coplanar waveguide to probe the interior of a single cell. This platform allows for precise single-cell trapping by dielectrophoresis, hydrodynamic focusing, and sensing the electrical properties of the trapped single cell. We measured the impedance characteristics of a single  Schizosaccharomyces pombe  (fission) yeast cell by a single frequency sweep (30 kHz to 6GHz) in a stagnant sucrose solution using two-port scattering ( S ) parameters. The measurements revealed a clear distinction between the cytoplasm impedance of live  versus  dead cells at 3 GHz. This platform could provide real-time monitoring of cellular electrical responses to chemical and physical antagonists for diagnostic purposes.","doi":"10.1039/d5lc00043b","authors":"Favakeh A, Mokhtare A, Asadi MJ, Hwang JCM, Abbaspourrad A","authors_abbrev":"Favakeh A et al.","pubmed_publication_date":"28 Feb 2025","pubmed_entrez_date":"2025-02-28","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-03-01 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084866","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.54"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:27930825","title":"Modulation of meiotic homologous recombination by DNA helicases.","citation":"Yeast 2017 May;34(5):195-203","abstract":"DNA helicases are ATP-driven motor proteins which translocate along DNA capable of dismantling DNA-DNA interactions and/or removing proteins bound to DNA. These biochemical capabilities make DNA helicases main regulators of crucial DNA metabolic processes, including DNA replication, DNA repair, and genetic recombination. This budding topic will focus on reviewing the function of DNA helicases important for homologous recombination during meiosis, and discuss recent advances in how these modulators of meiotic recombination are themselves regulated. The emphasis is placed on work in the two model yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe, which has vastly expanded our understanding of meiotic homologous recombination, a process whose correct execution is instrumental for healthy gamete formation, and thus functioning sexual reproduction. Copyright © 2016 John Wiley & Sons, Ltd.","doi":"10.1002/yea.3227","authors":"Lorenz A","authors_abbrev":"Lorenz A","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2016-12-09","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-12-10 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9090836","title":"Putative K+ channel in the plasma membrane of the yeast Schizosaccharomyces pombe: evidence of transcription-level regulation.","citation":"Folia Microbiol (Praha) 1996;41(1):93-5","abstract":"","authors":"Golubnitchaya-Labudova O, Vacata V, Höfer M","authors_abbrev":"Golubnitchaya-Labudova O et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36087798","title":"Ubiquitination regulates cytoophidium assembly in Schizosaccharomyces pombe.","citation":"Exp Cell Res 2022 Nov 01;420(1):113337","abstract":"CTP synthase (CTPS), a metabolic enzyme responsible for the de novo synthesis of CTP, can form filamentous structures termed cytoophidia, which are evolutionarily conserved from bacteria to humans. Here we used Schizosaccharomyces pombe to study the cytoophidium assembly regulation by ubiquitination. We tested the CTP synthase's capacity to be post-translationally modified by ubiquitin or be affected by the ubiquitination state of the cell and showed that ubiquitination is important for the maintenance of the CTPS filamentous structure in fission yeast. We have identified proteins which are in complex with CTPS, including specific ubiquitination regulators which significantly affect CTPS filamentation, and mapped probable ubiquitination targets on CTPS. Furthermore, we discovered that a cohort of deubiquitinating enzymes is important for the regulation of cytoophidium's filamentous morphology. Our study provides a framework for the analysis of the effects that ubiquitination and deubiquitination have on the formation of cytoophidia.","doi":"10.1016/j.yexcr.2022.113337","authors":"Andreadis C, Li T, Liu JL","authors_abbrev":"Andreadis C et al.","pubmed_publication_date":"01 Nov 2022","pubmed_entrez_date":"2022-09-10","publication_year":"2022","canto_session_key":"30cb7de4ef7848e9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-13 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14726691","title":"Upregulation of mRNA in MAPK signaling: transcriptional activation or mRNA stabilization?","citation":"Cell Cycle 2004 Mar;3(3):286-8","abstract":"Mitogen-activated protein kinases (MAPKs), found in all eukaryotes, are signal-transducing enzymes that play a central role in a variety of biological processes. MAPK phosphatase has dual catalytic activity toward phosphotyrosine- and phosphothreonine-containing proteins, and is known to inactivate ERKs and JNKs/SAPKs, thus playing a crucial role in MAPK regulation. Although MAPK phosphatase has been implicated in a feedback loop that inactivates MAPKs after stimulation by mitogens and during the cellular response to stress, signaling pathways leading to MAPK phosphatase gene expression have not been fully elucidated. Recently, we have shown that a novel RNA-binding protein Rnc1 plays a crucial role in negative feedback regulation of MAPK signaling by stabilizing the mRNA of a MAPK phosphatase at the post-transcriptional level. One important aspect of our findings is that the increase in mRNA levels involves not only the transcriptional upregulation, but also the post-transcriptional gene regulation, especially the regulation of mRNA stability. Our discovery highlights a potential role and an emerging view of RNA-binding protein as a regulator of cell signaling and as a future target of drug discovery.","authors":"Sugiura R, Kita A, Kuno T","authors_abbrev":"Sugiura R et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-01-17","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-10-15 11:31:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17138626","title":"A new evolutionary paradigm for the Parkinson disease gene DJ-1.","citation":"Mol Biol Evol 2007 Feb;24(2):551-61","abstract":"The DJ-1 gene is extensively studied because of its involvement in familial Parkinson disease. DJ-1 belongs to a complex superfamily of genes that includes both prokaryotic and eukaryotic representatives. We determine that many prokaryotic groups, such as proteobacteria, cyanobacteria, spirochaetes, firmicutes, or fusobacteria, have genes, often incorrectly called \"Thij,\" that are very close relatives of DJ-1, to the point that they cannot be clearly separated from the eukaryotic DJ-1 genes by phylogenetic analyses of their sequences. In addition, and contrary to a previous study that suggested that DJ-1 genes were animal specific, we show that DJ-1 genes are found in at least 5 of the 6 main eukaryotic groups: opisthokonta (both animals and fungi), plantae, chromalveolata, excavata, and amoebozoa. Our results thus provide strong evidence for DJ-1 genes originating before the origin of eukaryotes. Interestingly, we found that some fungal species, among them the model yeast Schizosaccharomyces pombe, have DJ-1-like genes, most likely orthologous to the animal genes. This finding opens new ways for the analysis of the functions of this group of genes.","authors":"Lucas JI, Marín I","authors_abbrev":"Lucas JI et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2006-12-02","publication_year":"2007","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22E12.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32575506","title":"SSADH Variants Increase Susceptibility of U87 Cells to Mitochondrial Pro-Oxidant Insult.","citation":"Int J Mol Sci 2020 Jun 19;21(12)","abstract":"Succinate semialdehyde dehydrogenase (SSADH) is a mitochondrial enzyme, encoded by  ALDH5A1 , mainly involved in γ-aminobutyric acid (GABA) catabolism and energy supply of neuronal cells, possibly contributing to antioxidant defense. This study aimed to further investigate the antioxidant role of SSADH, and to verify if common SNPs of  ALDH5A1  may affect SSADH activity, stability, and mitochondrial function. In this study, we used U87 glioblastoma cells as they represent a glial cell line. These cells were transiently transfected with a cDNA construct simultaneously harboring three SNPs encoding for a triple mutant (TM) SSADH protein (p.G36R/p.H180Y/p.P182L) or with wild type (WT) cDNA. SSADH activity and protein level were measured. Cell viability, lipid peroxidation, mitochondrial morphology, membrane potential (ΔΨ), and protein markers of mitochondrial stress were evaluated upon Paraquat treatment, in TM and WT transfected cells. TM transfected cells show lower SSADH protein content and activity, fragmented mitochondria, higher levels of peroxidized lipids, and altered ΔΨ than WT transfected cells. Upon Paraquat treatment, TM cells show higher cell death, lipid peroxidation, 4-HNE protein adducts, and lower ΔΨ, than WT transfected cells. These results reinforce the hypothesis that SSADH contributes to cellular antioxidant defense; furthermore, common SNPs may produce unstable, less active SSADH, which could per se negatively affect mitochondrial function and, under oxidative stress conditions, fail to protect mitochondria.","doi":"10.3390/ijms21124374","authors":"Menduti G, Vitaliti A, Capo CR, Lettieri-Barbato D, Aquilano K, Malaspina P, Rossi L","authors_abbrev":"Menduti G et al.","pubmed_publication_date":"19 Jun 2020","pubmed_entrez_date":"2020-06-25","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31542296","title":"Rad52 Restrains Resection at DNA Double-Strand Break Ends in Yeast.","citation":"Mol Cell 2019 Dec 05;76(5):699-711.e6","abstract":"Rad52 is a key factor for homologous recombination (HR) in yeast. Rad52 helps assemble Rad51-ssDNA nucleoprotein filaments that catalyze DNA strand exchange, and it mediates single-strand DNA annealing. We find that Rad52 has an even earlier function in HR in restricting DNA double-stranded break ends resection that generates 3' single-stranded DNA (ssDNA) tails. In fission yeast, Exo1 is the primary resection nuclease, with the helicase Rqh1 playing a minor role. We demonstrate that the choice of two extensive resection pathways is regulated by Rad52. In rad52 cells, the resection rate increases from ∼3-5 kb/h up to ∼10-20 kb/h in an Rqh1-dependent manner, while Exo1 becomes dispensable. Budding yeast Rad52 similarly inhibits Sgs1-dependent resection. Single-molecule analysis with purified budding yeast proteins shows that Rad52 competes with Sgs1 for DNA end binding and inhibits Sgs1 translocation along DNA. These results identify a role for Rad52 in limiting ssDNA generated by end resection.","doi":"10.1016/j.molcel.2019.08.017","authors":"Yan Z, Xue C, Kumar S, Crickard JB, Yu Y, Wang W, Pham N, Li Y, Niu H, Sung P, Greene EC, Ira G","authors_abbrev":"Yan Z et al.","pubmed_publication_date":"05 Dec 2019","pubmed_entrez_date":"2019-09-23","publication_year":"2019","canto_session_key":"cbe742e3539b32cd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-09-24 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPBC342.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9447985","title":"Novel factor highly conserved among eukaryotes controls sexual development in fission yeast.","citation":"Mol Cell Biol 1998 Feb;18(2):887-95","abstract":"In the fission yeast Schizosaccharomyces pombe, the onset of sexual development is controlled mainly by two external signals, nutrient starvation and mating pheromone availability. We have isolated a novel gene named rcd1+ as a key factor required for nitrogen starvation-induced sexual development. rcd1+ encodes a 283-amino-acid protein with no particular motifs. However, genes highly homologous to rcd1+ (encoding amino acids with >70% identity) are present at least in budding yeasts, plants, nematodes, and humans. Cells with rcd1+ deleted are sterile if sexual development is induced by nitrogen starvation but fertile if it is induced by glucose starvation. This results largely from a defect in nitrogen starvation-invoked induction of ste11+, a key transcriptional factor gene required for the onset of sexual development. The striking conservation of the gene throughout eukaryotes may suggest the presence of an evolutionarily conserved differentiation controlling system.","authors":"Okazaki N, Okazaki K, Watanabe Y, Kato-Hayashi M, Yamamoto M, Okayama H","authors_abbrev":"Okazaki N et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-02-03","publication_year":"1998","canto_session_key":"d6aa62bd60a4b84f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-03 08:03:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-18 16:33:41","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPBC106.10","SPAC31G5.11","SPBC1198.14c","SPBC19C2.05","SPAC29B12.06c","SPAPB2B4.03","SPBC32C12.02"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2014-12-18"},{"uniquename":"PMID:39695344","title":"Rapamycin Abrogates Aggregation of Human α-Synuclein Expressed in Fission Yeast via an Autophagy-Independent Mechanism.","citation":"Genes Cells 2025 Jan;30(1):e13185","abstract":"Aggregation of alpha-synuclein (α-Syn) is implicated in the pathogenesis of several neurodegenerative disorders, such as Parkinson's disease and Dementia with Lewy bodies, collectively termed synucleinopathies. Thus, tremendous efforts are being made to develop strategies to prevent or inhibit α-Syn aggregation. Here, we genetically engineered fission yeast to express human α-Syn C-terminally fused to green fluorescent protein (GFP) at low and high levels. α-Syn was localized at the cell tips and septa at low-level expression. At high-level expression, α-Syn was observed to form cytoplasmic aggregates. Notably, rapamycin, a natural product that allosterically inhibits the mammalian target of rapamycin (mTOR) by forming a complex with FKBP12, and Torin1, a synthetic mTOR inhibitor that blocks ATP binding to mTOR, markedly reduced the number of cells harboring α-Syn aggregates. These mTOR inhibitors abrogate α-Syn aggregation without affecting α-Syn expression levels. Rapamycin, but not Torin1, failed to reduce α-Syn aggregation in the deletion cells of fkh1 + , encoding FKBP12, indicating the requirement of FKBP12 for rapamycin-mediated inhibition of α-Syn aggregation. Importantly, the effect of rapamycin was also observed in the cells lacking atg1 + , a key regulator of autophagy. Collectively, rapamycin abrogates human α-Syn aggregation expressed in fission yeast via an autophagy-independent mechanism mediated by FKBP12.","doi":"10.1111/gtc.13185","authors":"Sugimoto Y, Takasaki T, Yamada R, Kurosaki R, Yamane T, Sugiura R","authors_abbrev":"Sugimoto Y et al.","pubmed_publication_date":"Jan 2025","pubmed_entrez_date":"2024-12-18","publication_year":"2025","canto_session_key":"8ba27a8546d69805","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-12-20 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8358431","title":"Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA.","citation":"Nat Genet 1993 Jul;4(3):239-43","abstract":"Rad51, of Saccharomyces cerevisiae, is a homologue of recA of Escherichia coli and plays crucial roles in both mitotic and meiotic recombination and in repair of double-strand breaks of DNA. We have cloned genes from human, mouse and fission yeast that are homologous to rad51. The 339 amino acid proteins predicted for the two mammalian genes are almost identical and are highly homologous (83%) with the yeast proteins. The mouse gene is transcribed at a high level in thymus, spleen, testis and ovary and at a lower level in brain and other tissues. The rad51 homologues fail to complement the DNA repair defect of rad51 mutants of S. cerevisiae. The mouse gene is located in the F1 region of chromosome 2 and the human gene maps to chromosome 15.","authors":"Shinohara A, Ogawa H, Matsuda Y, Ushio N, Ikeo K, Ogawa T","authors_abbrev":"Shinohara A et al.","pubmed_publication_date":"Jul 1993","pubmed_entrez_date":"1993-07-01","publication_year":"1993","canto_session_key":"e07fdd042552c54a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 13:56:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 13:55:43","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-07-31"},{"uniquename":"PMID:11273706","title":"Solution structure, domain features, and structural implications of mutants of the chromo domain from the fission yeast histone methyltransferase Clr4.","citation":"J Mol Biol 2001 Mar 30;307(3):861-70","abstract":"The encapsulation of otherwise transcribable loci within transcriptionally inactive heterochromatin is rapidly gaining recognition as an important mechanism of epigenetic gene regulation. In the fission yeast Schizosaccharomyces pombe, heterochromatinization of the mat2/mat3 loci silences the mating-type information encoded within these loci. Here, we present the solution structure of the chromo domain from the cryptic loci regulator protein Clr4. Clr4 is known to regulate silencing and switching at the mating-type loci and to affect chromatin structure at centromeres. Clr4 and its human and Drosophila homologs have been identified as histone H3-specific methyltransferases, further implicating this family of proteins in chromatin remodeling. Our structure highlights a conserved surface that may be involved in chromo domain-ligand interactions. We have also analyzed two chromo domain mutants (W31G and W41G) that previously were shown to affect silencing and switching in full-length Clr4. Both mutants are significantly destabilized relative to wild-type.","authors":"Horita DA, Ivanova AV, Altieri AS, Klar AJ, Byrd RA","authors_abbrev":"Horita DA et al.","pubmed_publication_date":"30 Mar 2001","pubmed_entrez_date":"2001-03-29","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"1g6z","gene_chains":[{"gene_uniquename":"SPBC428.08c","chain":"A","position":"2-69"}],"title":"SOLUTION STRUCTURE OF THE CLR4 CHROMO DOMAIN","entry_authors":"Horita DA,Ivanova AV,Altieri AS,Klar AJ,Byrd RA","entry_authors_abbrev":"Horita DA et al.","reference_uniquename":"PMID:11273706","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:38311173","title":"Factors governing the transcriptome changes and chronological lifespan of fission yeast during phosphate starvation.","citation":"J Biol Chem 2024 Feb 02;:105718","abstract":"Starvation of Schizosaccharomyces pombe for inorganic phosphate elicits adaptive transcriptome changes in which mRNAs driving ribosome biogenesis, tRNA biogenesis, and translation are globally downregulated while those for autophagy and phosphate mobilization are upregulated. Here, we interrogated three components of the starvation response: upregulated autophagy; the role of transcription factor Pho7 (an activator of the PHO regulon); and upregulated expression of ecl3, one of three paralogous genes (ecl1, ecl2, ecl3) collectively implicated in cell survival during other nutrient stresses. Ablation of autophagy factor Atg1 resulted in early demise of phosphate-starved fission yeast, as did ablation of Pho7. Transcriptome profiling of phosphate-starved pho7Δ cells highlighted Pho7 as an activator of genes involved in phosphate acquisition and mobilization, not limited to the original three-gene PHO regulon, and additional starvation-induced genes (including ecl3) not connected to phosphate dynamics. Pho7-dependent gene induction during phosphate starvation tracked with the presence of Pho7 DNA-binding elements in the gene promoter regions. Fewer ribosome protein genes were downregulated in phosphate-starved pho7Δ cells versus wild-type, which might contribute to their shortened lifespan. An ecl3Δ mutant elicited no gene expression changes in phosphate-replete cells and had no impact on survival during phosphate starvation. By contrast, pan-ecl deletion (ecl123Δ) curtailed lifespan during chronic phosphate starvation. Phosphate-starved ecl123Δ cells experienced a more widespread downregulation of mRNAs encoding aminoacyl tRNA synthetases vis-à-vis wild-type or pho7Δ cells. Collectively, these results enhance our understanding of fission yeast phosphate homeostasis and survival during nutrient deprivation.","doi":"10.1016/j.jbc.2024.105718","authors":"Garg A, Sanchez AM, Schwer B, Shuman S","authors_abbrev":"Garg A et al.","pubmed_publication_date":"02 Feb 2024","pubmed_entrez_date":"2024-02-04","publication_year":"2024","canto_session_key":"8fbe66ae0b15f950","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-02-06 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7803855","title":"Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity.","citation":"Mol Biol Cell 1994 Aug;5(8):877-86","abstract":"We have examined the activity and substrate specificity of the Saccharomyces cerevisiae Hrr25p and the Schizosaccharomyces pombe Hhp1, Hhp2, and Cki1 protein kinase isoforms. These four gene products are isotypes of casein kinase I (CKI), and the sequence of these protein kinases predicts that they are protein serine/threonine kinases. However, each of these four protein kinases, when expressed in Escherichia coli in an active form, was recognized by anti-phosphotyrosine antibodies. Phosphoamino acid analysis of 32P-labeled proteins showed phosphorylation on serine, threonine, and tyrosine residues. The E. coli produced forms of Hhp1, Hhp2, and Cki1 were autophosphorylated on tyrosine, and both Hhp1 and Hhp2 were capable of phosphorylating the tyrosine-protein kinase synthetic peptide substrate polymer poly-E4Y1. Immune complex protein kinases assays from S. pombe cells showed that Hhp1-containing precipitates were associated with a protein-tyrosine kinase activity, and the Hhp1 present in these immunoprecipitates was phosphorylated on tyrosine residues. Although dephosphorylation of Hhp1 and Hhp2 by Ser/Thr phosphatase had little effect on the specific activity, tyrosine dephosphorylation of Hhp1 and Hhp2 caused a 1.8-to 3.1-fold increase in the Km for poly-E4Y1 and casein. These data demonstrate that four different CKI isoforms from two different yeasts are capable of protein-tyrosine kinase activity and encode dual-specificity protein kinases.","authors":"Hoekstra MF, Dhillon N, Carmel G, DeMaggio AJ, Lindberg RA, Hunter T, Kuret J","authors_abbrev":"Hoekstra MF et al.","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_session_key":"6c7982aab7b18539","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-23 17:25:25","canto_approved_date":"2021-09-28 17:09:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-08 08:49:04","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3H7.15","SPAC23C4.12","SPBC1347.06c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-01-23"},{"uniquename":"EMBL:AB012387","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8978670","title":"Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function.","citation":"EMBO J 1996 Dec 02;15(23):6426-37","abstract":"Profilins bind to monomeric actin and also interact with ligands such as phosphoinositide 4,5-bisphosphate, the proline-rich protein VASP and a complex of four to six polypeptides identified in Acanthamoeba that includes two actin-related proteins. Here, we report the identification and characterization of an essential gene from Schizosaccharomyces pombe, sop2+, a mutation in which rescues the temperature-sensitive lethality of a profilin mutation, cdc3-124. The sop2-1 mutant is defective for cell elongation and septation, suggesting that it is involved in multiple cortical actin-requiring processes. Consistent with a role in actin cytoskeletal function, negative interactions have been identified between sop2-1 and act1-48, a mutant allele of actin. Sop2p is a novel 377 amino acid polypeptide with similarity to proteins of the beta-transducin repeat family. Sop2p-related proteins have been identified by sequencing projects in diverse species, and we have isolated a human cDNA highly related to sop2+, SOP2 Hs, which functionally complements the sop2-1 mutation. Sop2p proteins from all species contain peptide sequences identical or highly similar to two peptide sequences from an Acanthamoeba beta-transducin repeat protein present in the profilin binding complex. Biochemical analyses demonstrate that Sop2p is present in a complex which also contains the actin-related protein, Arp3p. Immunofluorescence studies reveal the presence of Sop2p in (i) punctate structures distributed throughout the cell, (ii) cables that extend the length of the cell, and (iii) a medial band in a small percentage of septating cells. Collectively these data demonstrate the interaction of Sop2p with Arp3p, profilin and actin.","authors":"Balasubramanian MK, Feoktistova A, McCollum D, Gould KL","authors_abbrev":"Balasubramanian MK et al.","pubmed_publication_date":"02 Dec 1996","pubmed_entrez_date":"1996-12-02","publication_year":"1996","canto_session_key":"7a6602af54fdea54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-08-22 21:36:52","canto_approved_date":"2026-06-17 12:54:51","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-06-29 11:16:55","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.04c","SPAC630.03","SPAC4A8.15c","SPBC32H8.12c","SPCC1739.11c","SPBC14C8.06","SPAC27F1.02c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-08-22"},{"uniquename":"PMID:25535331","title":"Antagonistic controls of chromatin and mRNA start site selection by Tup family corepressors and the CCAAT-binding factor.","citation":"Mol Cell Biol 2015 Mar;35(5):847-55","abstract":"The Tup family corepressors contribute to critical cellular responses, such as the stress response and differentiation, presumably by inducing repressive chromatin, though the precise repression mechanism remains to be elucidated. The Schizosaccharomyces pombe fission yeast Tup family corepressors Tup11 and Tup12 (Tup11/12), which are orthologs of Tup1 in Saccharomyces cerevisiae budding yeast and Groucho in Drosophila, negatively control chromatin and the transcriptional activity of some stress-responsive genes. Here, we demonstrate that Tup11/12 repress transcription of a gluconeogenesis gene, fbp1⁺, by three distinct mechanisms. First, Tup11/12 inhibit chromatin remodeling in the fbp1⁺ promoter region where the Atf1 and Rst2 transcriptional activators bind. Second, they repress the formation of an open chromatin configuration at the fbp1⁺ TATA box. Third, they repress mRNA transcription per se by regulating basic transcription factors. These inhibitory actions of Tup11/12 are antagonized by three different types of transcriptional activators: CREB/ATF-type Atf1, C₂H₂zinc finger-type Rst2, and CBF/NF-Y-type Php5 proteins. We also found that impaired chromatin remodeling and fbp1⁺ mRNA transcription in php5Δ strains are rescued by the double deletions of tup11⁺ and tup12⁺, although the distribution of the transcription start sites becomes broader than that in wild-type cells. These data reveal a new mechanism of precise determination of the mRNA start site by Tup family corepressors and CBF/NF-Y proteins.","doi":"10.1128/MCB.00924-14","authors":"Asada R, Takemata N, Hoffman CS, Ohta K, Hirota K","authors_abbrev":"Asada R et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2014-12-24","publication_year":"2015","canto_session_key":"a8b01e5fddee3159","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-12-25 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPBC3B8.02","SPAC6F12.02","SPAC18B11.10","SPAC630.14c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:11102318","title":"Yeast perspectives on HIV-1 VPR.","citation":"Front Biosci 2000 Dec 01;5:D905-16","abstract":"Increasing evidence suggests that HIV-1 viral protein R (Vpr) plays an important role in viral pathogenesis, as its functions are being linked to viral activation, suppression of human immune functions and depletion of human CD4 lymphocytes, which are the major clinical manifestation of AIDS. In vitro, Vpr shows multiple activities both in mammalian and yeast cells, which include nuclear transport, induction of cell cycle G2 arrest, morphological changes and cell death. The occurrence of these activities in yeast indicates that Vpr interacts with highly conserved cellular processes to cause these effects and allows Vpr activities to be studied in these genetically well characterized organisms. Studies of Vpr in fission yeast (Schizosaccharomyces pombe) and budding yeast (Saccharomyces cerevisiae) have helped to establish these major conclusions. 1) Vpr induces G2 arrest through inhibitory phosphorylation of the cyclin-dependent kinase by a pathway in which protein phosphatase 2A plays an important role. 2) Vpr fulfills its essential role in the nuclear transport of the viral pre-integration complex by binding to a novel site on importin ?. 3) Vpr induces apoptosis by directly permeabilizing the mitochondrial membrane. 4) Vpr also appears to kill cells by mitochondrial-independent mechanisms. 5) G2 arrest and cell death induced by Vpr are two independent functions, and 6) amino acid residues of Vpr at position 29, 33 and 71 are important sites for maintaining the overall structure of Vpr. Future studies of Vpr in yeast are expected to make additional contributions to understanding the mechanisms of Vpr activities and may also help address the importance of these activities during the course of a HIV-1 infection.","authors":"Zhao Y, Elder RT","authors_abbrev":"Zhao Y et al.","pubmed_publication_date":"01 Dec 2000","pubmed_entrez_date":"2000-12-05","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8886983","title":"The fission yeast sts5+ gene is required for maintenance of growth polarity and functionally interacts with protein kinase C and an osmosensing MAP-kinase pathway.","citation":"J Cell Sci 1996 Sep;109 ( Pt 9):2331-42","abstract":"Cell morphogenesis is a fundamental phenomenon that involves understanding a number of biological processes including the developmental program, polarity and cell division. Fission yeast sts5 mutant cells are round rather than cylindrical with cortical actin randomly dispersed. Genetic analyses demonstrate that the sts5+ gene is required for maintenance of cell shape during interphase when the cell normally exhibits polarised growth. The sts5 mutant is not defective in cell wall integrity. Deletion of ppe1+, which encodes a type 2A-like protein phosphatase, shows similar phenotypes to the sts5 mutant and these two mutations are synthetically lethal. Multicopy plasmids containing either the protein kinase C-like gene pck1+ or the protein tyrosine phosphatase pyp1+, an inhibitor of an osmosensing Sty1/Spc1 MAP-kinase, are capable of suppressing the sts5 mutation. Consistent with this, we have found that the wis1 mutation, which is defective in a MAP-kinase kinase of the pathway, suppresses the sts5 mutation. The predicted sts5+ gene product exhibits sequence similarity to two yeast proteins, Dis3 and Ssd1 and a nematode protein, F46E8.6, where the former two yeast proteins have been shown to be involved in cell cycle control and cell morphogenesis. The sts5+ gene is not essential for cell viability, but is absolutely required for polarised growth as the gene disruption showed the same phenotypes as those of the original mutants. Overexpression of the sts5+ gene resulted in altered cell morphology and, cortical actin in these overproducing cells was also abnormal, fainter and often dispersed. Anti-Sts5 antibody specifically detected a 130 kDa protein by western blotting. A green fluorescent protein-Sts5 fusion protein localised in the cytoplasm with a discrete punctate pattern, suggesting that the Sts5 protein is a component of a novel structure. These results have indicated that the Sts5 protein is a crucial determinant of polarised growth and that it functionally interacts with the serine/threonine phosphatase, protein kinase C, and an osmosensing MAP-kinase to maintain cell morphology.","authors":"Toda T, Niwa H, Nemoto T, Dhut S, Eddison M, Matsusaka T, Yanagida M, Hirata D","authors_abbrev":"Toda T et al.","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_session_key":"abaef95bc38c0982","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-01-28 19:20:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-20 15:11:23","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC74.03c","SPBP4H10.04","SPCC16C4.09","SPBC12D12.04c","SPAC24B11.06c","SPCC1739.12","SPBC409.07c","SPBC21.06c","SPBC336.12c","SPAC26F1.10c","SPAC24H6.05","SPAC17G8.14c","SPCC297.03"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2014-01-20"},{"uniquename":"PMID:18910671","title":"Studies on the nutritional requirements of Schizosaccharomyces pombe (2478).","citation":"Arch Biochem 1948 Apr;17(1):3-9","abstract":"","authors":"CLARK FM, BANISTER NC, MITCHELL WR","authors_abbrev":"CLARK FM et al.","pubmed_publication_date":"Apr 1948","pubmed_entrez_date":"1948-04-01","publication_year":"1948","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19457258","title":"BRNI: Modular analysis of transcriptional regulatory programs.","citation":"BMC Bioinformatics 2009 May 20;10:155","abstract":"Transcriptional responses often consist of regulatory modules - sets of genes with a shared expression pattern that are controlled by the same regulatory mechanisms. Previous methods allow dissecting regulatory modules from genomics data, such as expression profiles, protein-DNA binding, and promoter sequences. In cases where physical protein-DNA data are lacking, such methods are essential for the analysis of the underlying regulatory program.\nHere, we present a novel approach for the analysis of modular regulatory programs. Our method - Biochemical Regulatory Network Inference (BRNI) - is based on an algorithm that learns from expression data a biochemically-motivated regulatory program. It describes the expression profiles of gene modules consisting of hundreds of genes using a small number of regulators and affinity parameters. We developed an ensemble learning algorithm that ensures the robustness of the learned model. We then use the topology of the learned regulatory program to guide the discovery of a library of cis-regulatory motifs, and determined the motif compositions associated with each module.We test our method on the cell cycle regulatory program of the fission yeast. We discovered 16 coherent modules, covering diverse processes from cell division to metabolism and associated them with 18 learned regulatory elements, including both known cell-cycle regulatory elements (MCB, Ace2, PCB, ACCCT box) and novel ones, some of which are associated with G2 modules. We integrate the regulatory relations from the expression- and motif-based models into a single network, highlighting specific topologies that result in distinct dynamics of gene expression in the fission yeast cell cycle.\nOur approach provides a biologically-driven, principled way for deconstructing a set of genes into meaningful transcriptional modules and identifying their associated cis-regulatory programs. Our analysis sheds light on the architecture and function of the regulatory network controlling the fission yeast cell cycle, and a similar approach can be applied to the regulatory underpinnings of other modular transcriptional responses.","doi":"10.1186/1471-2105-10-155","authors":"Nachman I, Regev A","authors_abbrev":"Nachman I et al.","pubmed_publication_date":"20 May 2009","pubmed_entrez_date":"2009-05-22","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29925950","title":"Epigenetic inheritance mediated by coupling of RNAi and histone H3K9 methylation.","citation":"Nature 2018 Jun;558(7711):615-619","abstract":"Histone post-translational modifications (PTMs) are associated with epigenetic states that form the basis for cell-type-specific gene expression 1,2 . Once established, histone PTMs can be maintained by positive feedback involving enzymes that recognize a pre-existing histone modification and catalyse the same modification on newly deposited histones. Recent studies suggest that in wild-type cells, histone PTM-based positive feedback is too weak to mediate epigenetic inheritance in the absence of other inputs 3-7 . RNA interference (RNAi)-mediated histone H3 lysine 9 methylation (H3K9me) and heterochromatin formation define a potential epigenetic inheritance mechanism in which positive feedback involving short interfering RNA (siRNA) amplification can be directly coupled to histone PTM positive feedback 8-14 . However, it is not known whether the coupling of these two feedback loops can maintain epigenetic silencing independently of DNA sequence and in the absence of enabling mutations that disrupt genome-wide chromatin structure or transcription 15-17 . Here, using the fission yeast Schizosaccharomyces pombe, we show that siRNA-induced H3K9me and silencing of a euchromatic gene can be epigenetically inherited in cis during multiple mitotic and meiotic cell divisions in wild-type cells. This inheritance involves the spreading of secondary siRNAs and H3K9me3 to the targeted gene and surrounding areas, and requires both RNAi and H3K9me, suggesting that the siRNA and H3K9me positive-feedback loops act synergistically to maintain silencing. By contrast, when maintained solely by histone PTM positive feedback, silencing is erased by H3K9 demethylation promoted by Epe1, or by interallelic interactions that occur after mating to cells containing an expressed allele even in the absence of Epe1. These findings demonstrate that the RNAi machinery can mediate transgenerational epigenetic inheritance independently of DNA sequence or enabling mutations, and reveal a role for the coupling of the siRNA and H3K9me positive-feedback loops in the protection of epigenetic alleles from erasure.","doi":"10.1038/s41586-018-0239-3","authors":"Yu R, Wang X, Moazed D","authors_abbrev":"Yu R et al.","pubmed_publication_date":"Jun 2018","pubmed_entrez_date":"2018-06-22","publication_year":"2018","canto_session_key":"79e47bcf18232a7e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-06-23 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15226405","title":"S. pombe meiotic linear elements contain proteins related to synaptonemal complex components.","citation":"J Cell Sci 2004 Jul 01;117(Pt 15):3343-51","abstract":"The fission yeast Schizosaccharomyces pombe does not form synaptonemal complexes (SCs) in meiotic prophase nuclei. Instead, thin threads, the so-called linear elements (LEs), are observed at the corresponding stages by electron microscopy. Here, we demonstrate that S. pombe Rec10 is a protein related to the Saccharomyces cerevisiae SC protein Red1 and that it localizes to LEs. Moreover, a homologue to S. cerevisiae Hop1 does exist in S. pombe and we show by in situ immunostaining that it, and the kinase Mek1 (a homologue of which is also known to be associated with SCs), localizes to LEs. These observations indicate the evolutionary relationship of LEs with the lateral elements of SCs and suggest that these structures might exert similar functions in S. cerevisiae and S. pombe.","authors":"Lorenz A, Wells JL, Pryce DW, Novatchkova M, Eisenhaber F, McFarlane RJ, Loidl J","authors_abbrev":"Lorenz A et al.","pubmed_publication_date":"01 Jul 2004","pubmed_entrez_date":"2004-07-01","publication_year":"2004","canto_session_key":"a4fee2d59c2592b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-16 22:27:18","canto_approved_date":"2025-09-04 09:46:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-16 22:27:11","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.02","SPAC17A5.11","YIL072W","SPAC25G10.04c","SPAC14C4.03","YLR263W","SPCC4E9.01c","SPBC29A10.14"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-12-16"},{"uniquename":"PMID:9383050","title":"Mutational analysis of Cdc19p, a Schizosaccharomyces pombe MCM protein.","citation":"Genetics 1997 Nov;147(3):1025-41","abstract":"The cdc19+ gene encodes an essential member of the MCM family of replication proteins in Schizosaccharomyces pombe. We have examined the structure and function of the Cdc19p protein using molecular and genetic approaches. We find that overproduction of wild-type Cdc19p in wild-type cells has no effect, but cdc19-P1 mutant cells do not tolerate elevated levels of other MCM proteins or overexpression of mutant forms of Cdc19p. We have found genetic interactions between cdc19+ and genes encoding subunits of DNA polymerase delta and the replication initiator cdc18+. We have constructed a series of point mutations and sequence deletions throughout Cdc19p, which allow us to distinguish essential from nonessential regions of the protein. Not surprisingly, conserved residues in the MCM homology domain are required for protein function, but some residues outside the core homology domain are dispensable.","authors":"Forsburg SL, Sherman DA, Ottilie S, Yasuda JR, Hodson JA","authors_abbrev":"Forsburg SL et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-02-07","publication_year":"1997","canto_session_key":"9c558fe25d636ef5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-10 16:22:41","canto_approved_date":"2023-01-12 18:17:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-29 15:57:02","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC336.04","SPBC4.04c","SPBC211.04c","SPCC16A11.17","SPBC14C8.07c","SPAC1B2.05","SPAC17C9.01c","SPAC27E2.05"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2015-04-10"},{"uniquename":"PMID:9251043","title":"Cytokinesis in fission yeast Schizosaccharomyces pombe.","citation":"Methods Enzymol 1997;283:494-506","abstract":"","authors":"Balasubramanian MK, McCollum D, Gould KL","authors_abbrev":"Balasubramanian MK et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16845020","title":"YOGY: a web-based, integrated database to retrieve protein orthologs and associated Gene Ontology terms.","citation":"Nucleic Acids Res 2006 Jul 01;34(Web Server issue):W330-4","abstract":"We present YOGY a web-based resource for orthologous proteins from nine eukaryotic organisms: Homo sapiens, Mus musculus, Rattus norvegicus, Arabidopsis thaliana, Drosophila melanogaster, Caenorhabditis elegans, Plasmodium falciparum, Schizosaccharomyces pombe and Saccharomyces cerevisiae. Using a gene name from any of these organisms as a query, this database provides comprehensive, combined information on orthologs in other species using data from five independent resources: KOGs, Inparanoid, HomoloGene, OrthoMCL and a table of curated fission and budding yeast orthologs. Associated Gene Ontology (GO) terms of orthologs can also be retrieved for functional inference. Integrating these different and complementary datasets provides a straightforward tool to identify known and predicted orthologs of proteins from a variety of species. This resource should be useful for bench scientists looking for functional clues for their genes of interest as well as for curators looking for information that can be transferred based on orthology and for rapidly identifying the relevant GO terms as an aid to literature curation. YOGY is accessible online at http://www.sanger.ac.uk/PostGenomics/S_pombe/YOGY/.","authors":"Penkett CJ, Morris JA, Wood V, Bähler J","authors_abbrev":"Penkett CJ et al.","pubmed_publication_date":"01 Jul 2006","pubmed_entrez_date":"2006-07-18","publication_year":"2006","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30355493","title":"Expanded Interactome of the Intrinsically Disordered Protein Dss1.","citation":"Cell Rep 2018 Oct 23;25(4):862-870","abstract":"Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes. Accordingly, Dss1 functions in protein degradation, DNA repair, transcription, and mRNA export. Here in Schizosaccharomyces pombe, we expand its interactome further to include eIF3, the COP9 signalosome, and the mitotic septins. Within its intrinsically disordered ensemble, Dss1 forms a transiently populated C-terminal helix that dynamically interacts with and shields a central binding region. The helix interfered with the interaction to ATP-citrate lyase but was required for septin binding, and in strains lacking Dss1, ATP-citrate lyase solubility was reduced and septin rings were more persistent. Thus, even weak, transient interactions within Dss1 may dynamically rewire its interactome.","doi":"10.1016/j.celrep.2018.09.080","authors":"Schenstrøm SM, Rebula CA, Tatham MH, Hendus-Altenburger R, Jourdain I, Hay RT, Kragelund BB, Hartmann-Petersen R","authors_abbrev":"Schenstrøm SM et al.","pubmed_publication_date":"23 Oct 2018","pubmed_entrez_date":"2018-10-26","publication_year":"2018","canto_session_key":"9a676547ac396223","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_first_approved_date":"2018-12-16 12:12:18","canto_approved_date":"2019-01-25 09:17:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-01-25 08:14:59","canto_added_date":"2018-10-27 00:15:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.05","SPAC328.03","SPBC3H7.10","SPAC1F7.04","SPAC3H5.05c","SPAC4H3.13","SPBC119.07","SPBC800.03","SPCC16A11.16c","SPCC830.11c","SPCC584.15c","SPAC22F3.05c","SPAC23H4.15","SPBC18H10.03","SPCC1682.01","SPAC23H4.03c","SPAC17H9.12c","SPAC4A8.15c","SPBC19C2.13c","SPBC2G2.08","SPAC23D3.07","SPBC14C8.02","SPBC17G9.02c","SPBC6B1.05c","SPAC29E6.08","SPAC19A8.04","SPAC23A1.03","SPBC902.05c","SPAC17G8.10c","SPBC21.04","SPAC1B3.08","SPAC869.07c","SPBC2A9.11c","SPCC576.08c","SPCC23B6.05c","SPBC577.10","SPAP11E10.01","SPBC1539.04","SPBC4C3.07","SPCC622.12c","SPBC1778.08c","SPAC27D7.05c","SPBC17D11.07c","SPBC19F5.03","SPAC631.01c","SPBC582.07c","SPBC660.16","SPBC16A3.01","SPAC644.18c","SPCC1682.16","SPAC31A2.04c","SPBC2D10.11c","SPBC1604.07","SPCC663.02","SPBP8B7.25","SPBC1718.05","SPAC26A3.12c","SPBC2G5.02c","SPAC521.03","SPAC19G12.15c","SPBC4.02c","SPAC13G6.02c","SPAC3G6.02","SPBPJ4664.04","SPCC794.11c","SPAC6F12.14","SPAC6F12.15c","SPAC3G9.11c","SPCC1795.04c","SPAC1A6.02","SPCC1753.01c","SPAC23D3.04c","SPAC323.02c","SPAC4A8.11c","SPAC23G3.01","SPBC215.15","SPBC577.08c","SPAC31G5.04","SPBC30B4.06c","SPBC31A8.01c","SPBC409.21","SPBC577.07","SPAC1556.08c","SPAC926.09c","SPBC530.10c","SPCC1682.10","SPAC1952.12c","SPBC14C8.12","SPBC1778.10c","SPBC14F5.05c","SPAC22F8.05","SPAC24H6.10c","SPAC2F3.04c","SPAC694.05c","SPBC30D10.08","SPCC645.08c","SPCC895.06","SPAC4D7.05","SPCC1827.01c","SPAC18G6.14c","SPAC6B12.12","SPBC16C6.07c","SPBC25H2.07","SPAC31A2.12","SPAC637.10c","SPAC688.03c","SPBC3D6.04c","SPBC4C3.10c","SPCC1739.08c","SPBC646.09c","SPAC4F10.11","SPCC11E10.06c","SPBC646.16","SPAC17A2.13c","SPBC609.01","SPAC821.06","SPAC1071.11","SPAC1B2.04","SPCC553.06","SPAC167.07c","SPAC3A11.10c","SPBC24C6.05","SPCC1620.09c","SPBC691.03c","SPBC725.10","SPCC576.05","SPCC24B10.17","SPBC26H8.06","SPAC13G6.06c","SPAC1834.02","SPAC24B11.05","SPBC11C11.06c","SPBC146.01","SPBC365.12c","SPBP23A10.09","SPBP8B7.24c","SPCC1235.15","SPAC13C5.01c","SPAC607.05","SPBC1198.04c","SPAC17H9.16","SPAC29A4.20","SPBC409.06","SPAC9G1.11c","SPCC622.09","SPAC17A2.05","SPAC1782.01","SPBC16G5.01","SPCC1919.03c","SPAC6G10.08","SPAC56E4.02c","SPBC1685.13","SPAC19G12.06c","SPBC2G5.06c","SPAC31G5.13","SPBC1271.12","SPBC337.16","SPBC31F10.07","SPBC106.16","SPAC30.01c","SPCC63.12c","SPBC337.14","SPCC162.09c","SPBC2G5.03","SPBC21C3.05","SPAC6G9.05","SPAC31G5.16c","SPBC1105.07c","SPCC338.10c","SPBC1A4.02c","SPAC17C9.01c","SPBC106.09","SPAC19G12.01c","SPBC18E5.06","SPBC16A3.14","SPAPB1A10.06c","SPBC337.09","SPBC530.03c","SPCC338.15","SPAC18G6.01c","SPAC25G10.08","SPBC23G7.05","SPBC3B9.12","SPBC26H8.11c","SPBC409.05","SPAC664.03","SPBC14F5.09c","SPCC1281.06c","SPAC2E1P3.01","SPAC959.09c","SPAC29B12.06c","SPAC31G5.18c","SPAC16E8.11c","SPBC1A4.01","SPCC737.06c","SPBC32F12.03c","SPBP19A11.03c","SPAC32A11.02c","SPBC713.10","SPAC17G8.04c","SPAC23C4.15","SPAC4A8.13c","SPBC1604.10","SPBC28F2.12","SPBC660.13c","SPBC13G1.13","SPAC24C9.12c","SPAC18G6.03","SPAC23C11.06c","SPCC576.07","SPAC22A12.16","SPAC1B1.02c","SPAC6G9.11","SPBC211.01","SPAC694.02","SPBC725.09c","SPCC16C4.11","SPBC16G5.05c","SPBC1703.13c","SPCC364.06","SPAC5D6.05","SPBC428.13c","SPBC13E7.08c","SPBC83.16c","SPAC17C9.12","SPAC821.11","SPAC31G5.15","SPBP8B7.06","SPAC6G9.08","SPBC29A10.16c","SPCC417.07c","SPAC1687.13c","SPBC543.04","SPBC215.01","SPAC6F6.10c","SPBC12D12.08c","SPAC9E9.04","SPAC19D5.04","SPBC8E4.01c","SPBC216.06c","SPBC8D2.09c","SPCC736.11","SPCC613.10","SPAC2H10.02c","SPAC4D7.08c","SPAC6G9.06c","SPAC22F8.06","SPAC27D7.14c","SPBC18H10.13","SPAC1250.01","SPAC3A12.12","SPAC10F6.17c","SPAC3H8.02","SPBC119.06","SPAC1F8.03c","SPAC1635.01","SPAC17H9.09c","SPAC20G8.04c","SPAC637.03","SPBC215.03c","SPAC3G6.09c","SPBC119.01","SPBC12C2.05c","SPAC26F1.04c","SPBC3E7.07c","SPAC6G10.04c","SPBC1198.01","SPAC1F12.07","SPCC1442.06","SPAC1565.01","SPAC1851.03","SPBC14C8.06","SPBC725.14","SPAC10F6.02c","SPAC56E4.04c","SPAC31G5.09c","SPBC1685.10","SPAC6C3.08","SPBC342.04","SPCC1223.08c","SPAC12B10.02c","SPBC30D10.13c","SPAC6C3.04","SPCC757.03c","SPAC17G6.13","SPBC27B12.14","SPAC24B11.11c","SPBC2G2.06c","SPBP16F5.03c","SPBC11G11.06c","SPBC119.02","SPAC15E1.02c","SPAC27F1.07","SPAC31A2.09c","SPBC839.16","SPAC1486.04c","SPAC821.05","SPBC428.02c","SPBC839.07","SPCC576.10c","SPBC18H10.02","SPAC3H8.05c","SPBP8B7.14c","SPAC23C4.12","SPBC56F2.12","SPAC23G3.11","SPAC926.06c","SPBC1703.07","SPBC16H5.13","SPAPB1E7.07","SPBC1685.09","SPAC3C7.13c","SPAC23C11.11","SPAC19D5.06c","SPBC3E7.02c","SPAC637.07","SPAC17G6.12","SPAC5D6.09c","SPBC17D11.05","SPCC1919.10c"],"gene_count":320,"ltp_gene_count":12,"approved_date":"2018-12-16"},{"uniquename":"PMID:35561747","title":"Post-transcriptional regulation during stress.","citation":"FEMS Yeast Res 2022 Jun 30;22(1)","abstract":"To remain competitive, cells exposed to stress of varying duration, rapidity of onset, and intensity, have to balance their expenditure on growth and proliferation versus stress protection. To a large degree dependent on the time scale of stress exposure, the different levels of gene expression control: transcriptional, post-transcriptional, and post-translational, will be engaged in stress responses. The post-transcriptional level is appropriate for minute-scale responses to transient stress, and for recovery upon return to normal conditions. The turnover rate, translational activity, covalent modifications, and subcellular localisation of RNA species are regulated under stress by multiple cellular pathways. The interplay between these pathways is required to achieve the appropriate signalling intensity and prevent undue triggering of stress-activated pathways at low stress levels, avoid overshoot, and down-regulate the response in a timely fashion. As much of our understanding of post-transcriptional regulation has been gained in yeast, this review is written with a yeast bias, but attempts to generalise to other eukaryotes. It summarises aspects of how post-transcriptional events in eukaryotes mitigate short-term environmental stresses, and how different pathways interact to optimise the stress response under shifting external conditions.","doi":"10.1093/femsyr/foac025","authors":"Hernández-Elvira M, Sunnerhagen P","authors_abbrev":"Hernández-Elvira M et al.","pubmed_publication_date":"30 Jun 2022","pubmed_entrez_date":"2022-05-13","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-07-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29348174","title":"Oligomer formation and G-quadruplex binding by purified murine Rif1 protein, a key organizer of higher-order chromatin architecture.","citation":"J Biol Chem 2018 Mar 09;293(10):3607-3624","abstract":"Rap1-interacting protein 1 (Rif1) regulates telomere length in budding yeast. We previously reported that, in metazoans and fission yeast, Rif1 also plays pivotal roles in controlling genome-wide DNA replication timing. We proposed that Rif1 may assemble chromatin compartments that contain specific replication-timing domains by promoting chromatin loop formation. Rif1 also is involved in DNA lesion repair, restart after replication fork collapse, anti-apoptosis activities, replicative senescence, and transcriptional regulation. Although multiple physiological functions of Rif1 have been characterized, biochemical and structural information on mammalian Rif1 is limited, mainly because of difficulties in purifying the full-length protein. Here, we expressed and purified the 2418-amino-acid-long, full-length murine Rif1 as well as its partially truncated variants in human 293T cells. Hydrodynamic analyses indicated that Rif1 forms elongated or extended homo-oligomers in solution, consistent with the presence of a HEAT-type helical repeat segment known to adopt an elongated shape. We also observed that the purified murine Rif1 bound G-quadruplex (G4) DNA with high specificity and affinity, as was previously shown for Rif1 from fission yeast. Both the N-terminal (HEAT-repeat) and C-terminal segments were involved in oligomer formation and specifically bound G4 DNA, and the central intrinsically disordered polypeptide segment increased the affinity for G4. Of note, pulldown assays revealed that Rif1 simultaneously binds multiple G4 molecules. Our findings support a model in which Rif1 modulates chromatin loop structures through binding to multiple G4 assemblies and by holding chromatin fibers together.","doi":"10.1074/jbc.RA117.000446","authors":"Moriyama K, Yoshizawa-Sugata N, Masai H","authors_abbrev":"Moriyama K et al.","pubmed_publication_date":"09 Mar 2018","pubmed_entrez_date":"2018-01-20","publication_year":"2018","canto_session_key":"fa4933abfb986993","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-01-21 01:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20832719","title":"CST meets shelterin to keep telomeres in check.","citation":"Mol Cell 2010 Sep 10;39(5):665-76","abstract":"Telomere protection in budding yeast requires the heterotrimer named CST (for Cdc13-Stn1-Ten1). Recent data show that CST components are conserved and required for telomere stability in a wide range of eukaryotes, even those utilizing the shelterin complex to protect their telomeres. A common function of these proteins might be to stimulate priming at the C-strand gap that remains after telomerase elongation, replication termination, and terminal processing. In light of the budding yeast situation, another conserved function of CST might well be the regulation of telomerase. The cohabitation at telomeres of CST and shelterin components highlights the complexity of telomere biology.","doi":"10.1016/j.molcel.2010.08.024","authors":"Giraud-Panis MJ, Teixeira MT, Géli V, Gilson E","authors_abbrev":"Giraud-Panis MJ et al.","pubmed_publication_date":"10 Sep 2010","pubmed_entrez_date":"2010-09-14","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26950930","title":"The Natural Product Resveratrol Inhibits Yeast Cell Separation by Extensively Modulating the Transcriptional Landscape and Reprogramming the Intracellular Metabolome.","citation":"PLoS One 2016;11(3):e0150156","abstract":"An increasing number of studies have shown that the promising compound resveratrol treats multiple diseases, such as cancer and aging; however, the resveratrol mode-of-action (MoA) remains largely unknown. Here, by virtue of multiple omics approaches, we adopted fission yeast as a model system with the goal of dissecting the common MoA of the anti-proliferative activity of resveratrol. We found that the anti-proliferative activity of resveratrol is mainly due to its unique role of inhibiting the separation of sister cells, similar phenotype with the C2H2 zinc finger transcription factor Ace2 knock-out strain. Microarray analysis shown that resveratrol has extensive impact on the fission yeast transcription levels. Among the changed gene's list, 40% of up-regulated genes are Core Environmental Stress Responses genes, and 57% of the down-regulated genes are periodically expressed. Moreover, resveratrol leverages the metabolome, which unbalances the intracellular pool sizes of several classes of amino acids, nucleosides, sugars and lipids, thus reflecting the remodulated metabolic networks. The complexity of the resveratrol MoA displayed in previous reports and our work demonstrates that multiple omics approaches must be applied together to obtain a complete picture of resveratrol's anti-proliferative function.","doi":"10.1371/journal.pone.0150156","authors":"Wang Z, Gu Z, Shen Y, Wang Y, Li J, Lv H, Huo K","authors_abbrev":"Wang Z et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-03-08","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-03-09 01:15:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7954893","title":"Identification and characterization of genes induced during sexual differentiation in Schizosaccharomyces pombe.","citation":"Curr Genet 1994 Jul;26(1):31-7","abstract":"Five cDNA clones, harboring genetic messages preferentially expressed during the sexual differentiation process, were isolated from a cDNA library of Schizosaccharomyces pombe by subtractive screening. Transcription of the corresponding genes, termed isp3, 4, 5, 6, and 7, was dependent on nitrogen starvation and their induction occurred at several stages of spore formation. Analysis of the cDNA primary structures revealed a capacity for the coding of polypeptides of 19.2 kDa, 88.3 kDa, 60.1 kDa, 49.7 kDa, and 43.8 kDa, respectively. The translated amino-acid sequences of isp5 and isp6 were found to show significant similarities to those of amino-acid permeases and proteinase B of Saccharomyces cerevisiae, respectively. Disruption of isp6 arrested the cell cycle prior to conjugation and caused a drastic blocking effect on spore formation.","authors":"Sato S, Suzuki H, Widyastuti U, Hotta Y, Tabata S","authors_abbrev":"Sato S et al.","pubmed_publication_date":"Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_session_key":"538a1559c9d9f13a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-09 19:12:04","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-08 06:32:04","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.13c","SPAC1F8.05","SPAC1039.09","SPBC29B5.02c","SPAC4A8.04"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-05-08"},{"uniquename":"PMID:8554540","title":"Cloning of the Schizosaccharomyces pombe gene encoding diadenosine 5',5\"'-P1,P4-tetraphosphate (Ap4A) asymmetrical hydrolase: sequence similarity with the histidine triad (HIT) protein family.","citation":"Biochem J 1995 Dec 15;312 ( Pt 3)(Pt 3):925-32","abstract":"Diadenosine 5',5\"'-P1,P4-tetraphosphate (Ap4A) asymmetric hydrolase (EC 3.6.1.17) is a specific catabolic enzyme of Ap4A found in Schizosaccharomyces pombe. We have previously described the partial purification of Ap4A hydrolase from S. pombe [Robinson, de la Peña and Barnes (1993) Biochim. Biophys. Acta 1161, 139-148]. We determined the sequence of the N-terminal 20 amino acids of Ap4A hydrolase and designed two degenerate PCR primers based on the sequence. The 60 bp DNA fragment obtained by PCR, which is specific to Ap4A hydrolase, was used to isolate the Ap4A hydrolase gene, aph1, from S. pombe by screening a genomic DNA library in a multicopy plasmid. Ap4A hydrolase activity from the crude supernatant of a positive S. pombe transformant was about 25-fold higher than the control. There was no detectable stimulation of enzymic activity by phosphate. The aph1 gene from S. pombe contains three introns. The intron boundaries were confirmed by sequencing the cDNA of the aph1 gene from a S. pombe cDNA library. The deduced open reading frame of the aph1 gene codes for 182 amino acids. Two regions of significant local similarity were identified between the Ap4A hydrolase and the histidine triad (HIT) protein family [Séraphin (1992) DNA Sequence 3, 177-179]. HIT proteins are present in prokaryotes, yeast, plants and mammals. Their functions are unknown, except that the bovine protein inhibits protein kinase C in vitro. All four histidine residues which are conserved among the HIT proteins, including the HxHxH putative Zn(2+)-binding motif, are conserved in the Ap4A hydrolase. In addition, there are two regions of similarity between the Ap4A phosphorylases I and II from Saccharomyces cerevisiae and Ap4A hydrolase from S. pombe. These regions overlap with the HIT protein similarity regions. The aph1 gene from S. pombe is the first asymmetrical Ap4A hydrolase gene to be cloned and sequenced.","authors":"Huang Y, Garrison PN, Barnes LD","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"15 Dec 1995","pubmed_entrez_date":"1995-12-15","publication_year":"1995","canto_session_key":"dd66da97a27c3554","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-05-13 07:28:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-13 07:28:39","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-05-13"},{"uniquename":"PMID:9388670","title":"Proteolysis of Sxa2, a carboxypeptidase involved in pheromone adaptation in yeast.","citation":"Biochem Soc Trans 1997 Aug;25(3):446S","abstract":"","authors":"Ladds G, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"7a0647a630a18f51","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:49:35","canto_session_submitted_date":"2012-02-27 11:07:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:31532702","title":"Kinetochore-mediated outward force promotes spindle pole separation in fission yeast.","citation":"Mol Biol Cell 2019 Oct 15;30(22):2802-2813","abstract":"Bipolar spindles are organized by motor proteins that generate microtubule--dependent forces to separate the two spindle poles. The fission yeast Cut7 (kinesin-5) is a plus-end-directed motor that generates the outward force to separate the two spindle poles, whereas the minus-end-directed motor Pkl1 (kinesin-14) generates the inward force. Balanced forces by these antagonizing kinesins are essential for bipolar spindle organization in mitosis. Here, we demonstrate that chromosomes generate another outward force that contributes to the bipolar spindle assembly. First, it was noted that the  cut7 pkl1  double knockout failed to separate spindle poles in meiosis I, although the mutant is known to succeed it in mitosis. It was assumed that this might be because meiotic kinetochores of bivalent chromosomes joined by cross-overs generate weaker tensions in meiosis I than the strong tensions in mitosis generated by tightly tethered sister kinetochores. In line with this idea, when meiotic mono-oriented kinetochores were artificially converted to a mitotic bioriented layout, the  cut7 pkl1  mutant successfully separated spindle poles in meiosis I. Therefore, we propose that spindle pole separation is promoted by outward forces transmitted from kinetochores to spindle poles through microtubules.","doi":"10.1091/mbc.E19-07-0366","authors":"Shirasugi Y, Sato M","authors_abbrev":"Shirasugi Y et al.","pubmed_publication_date":"15 Oct 2019","pubmed_entrez_date":"2019-09-19","publication_year":"2019","canto_session_key":"ae5f72244ad85ad1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2019-10-14 22:14:12","canto_approved_date":"2024-03-29 09:18:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-10-03 13:07:52","canto_added_date":"2019-09-20 00:15:04","annotation_curators":[{"name":"Masamitsu Sato","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c","SPAC3A11.14c","SPAC17A5.11","SPAC664.10","SPAC664.01c","SPCC338.17c","SPAC15E1.07c","SPAC5D6.08c","SPAC27F1.04c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2019-10-14"},{"uniquename":"PMID:41335110","title":"High-resolution mapping of the actin fusion focus reveals myosin V-dependent formin transport for aster formation.","citation":"J Cell Biol 2026 Feb 02;225(2)","abstract":"Many processes such as polarized growth and secretion require specific actin networks. In fungi, cell-cell fusion requires cell wall digestion mediated by local secretion of lytic enzymes. In Schizosaccharomyces pombe, the myosin V Myo52 transports enzyme-containing secretory vesicles on the actin fusion focus, an aster-like actin network assembled by the condensate-forming formin Fus1. The fusion focus also concentrates proteins regulating cell polarity, communication, cytoskeleton, exocytosis, and membrane merging. Here, using centroid tracking and averaging, we present a spatiotemporal map of the fusion site with 8-nm precision. We show that a pool of vesicles remains at constant distance from the membrane as the actin structure condenses. Unexpectedly, Myo52 detaches from this pool and colocalizes with Fus1 closer to the membrane. We show that Myo52 binds Fus1 and transports it along actin filaments, and that Myo52 and Fus1 actin assembly activity contribute to focus compaction. Thus, myosin V-driven transport of formin Fus1 along Fus1-nucleated actin filaments underlies positive feedback for actin aster formation.","doi":"10.1083/jcb.202510018","authors":"Thomas V, Mase H, Michon L, Picco A, Kaksonen M, Martin SG","authors_abbrev":"Thomas V et al.","pubmed_publication_date":"02 Feb 2026","pubmed_entrez_date":"2025-12-03","publication_year":"2026","canto_session_key":"2329bd85ea05d9aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2026-03-28 13:38:06","canto_approved_date":"2026-04-24 14:09:56","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-03-25 14:21:13","canto_added_date":"2025-12-04 00:25:05","annotation_curators":[{"name":"Sophie Martin","community_curator":true,"annotation_count":26,"orcid":"0000-0002-5317-2557","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22H10.07","SPBC4.01","SPAC27F1.02c","SPAC6F12.08c","SPAC20G4.02c","SPAC18G6.03","SPAP7G5.03","SPBC2D10.14c","SPAC31G5.07","SPAC9E9.07c","SPBC106.20","SPCC1235.10c","SPCC1919.10c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2026-03-28"},{"uniquename":"PMID:11250164","title":"Replication checkpoint: preventing mitotic catastrophe.","citation":"Curr Biol 2001 Feb 20;11(4):R121-4","abstract":"A conserved network of signal transduction pathways prevents mitosis if DNA is damaged or its synthesis incomplete. Loss of this checkpoint control is detrimental to the developing embryo. Recent studies have shed new light on how the essential ATR and Chk1 protein kinases cooperate to prevent such a crisis.","authors":"Canman CE","authors_abbrev":"Canman CE","pubmed_publication_date":"20 Feb 2001","pubmed_entrez_date":"2001-03-16","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10582240","title":"Two distinct ubiquitin-proteolysis pathways in the fission yeast cell cycle.","citation":"Philos Trans R Soc Lond B Biol Sci 1999 Sep 29;354(1389):1551-7","abstract":"The SCF complex (Skp1-Cullin-1-F-box) and the APC/cyclosome (anaphase-promoting complex) are two ubiquitin ligases that play a crucial role in eukaryotic cell cycle control. In fission yeast F-box/WD-repeat proteins Pop1 and Pop2, components of SCF are required for cell-cycle-dependent degradation of the cyclin-dependent kinase (CDK) inhibitor Rum1 and the S-phase regulator Cdc18. Accumulation of these proteins in pop1 and pop2 mutants leads to re-replication and defects in sexual differentiation. Despite structural and functional similarities, Pop1 and Pop2 are not redundant homologues. Instead, these two proteins form heterodimers as well as homodimers, such that three distinct complexes, namely SCFPop1/Pop1, SCFPop1/Pop2 and SCFPop2/Pop2, appear to exist in the cell. The APC/cyclosome is responsible for inactivation of CDK/cyclins through the degradation of B-type cyclins. We have identified two novel components or regulators of this complex, called Apc10 and Ste9, which are evolutionarily highly conserved. Apc10 (and Ste9), together with Rum1, are required for the establishment of and progression through the G1 phase in fission yeast. We propose that dual downregulation of CDK, one via the APC/cyclosome and the other via the CDK inhibitor, is a universal mechanism that is used to arrest the cell cycle at G1.","authors":"Toda T, Ochotorena I, Kominami K","authors_abbrev":"Toda T et al.","pubmed_publication_date":"29 Sep 1999","pubmed_entrez_date":"1999-12-03","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31209062","title":"Molecular form and function of the cytokinetic ring.","citation":"J Cell Sci 2019 Jun 17;132(12)","abstract":"Animal cells, amoebas and yeast divide using a force-generating, actin- and myosin-based contractile ring or 'cytokinetic ring' (CR). Despite intensive research, questions remain about the spatial organization of CR components, the mechanism by which the CR generates force, and how other cellular processes are coordinated with the CR for successful membrane ingression and ultimate cell separation. This Review highlights new findings about the spatial relationship of the CR to the plasma membrane and the arrangement of molecules within the CR from studies using advanced microscopy techniques, as well as mechanistic information obtained from  in vitro  approaches. We also consider advances in understanding coordinated cellular processes that impact the architecture and function of the CR.","doi":"10.1242/jcs.226928","authors":"Mangione MC, Gould KL","authors_abbrev":"Mangione MC et al.","pubmed_publication_date":"17 Jun 2019","pubmed_entrez_date":"2019-06-19","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-07-24 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39330577","title":"Development and Application of a Slot-Blot Assay Using the Damage Sensing Protein Atl1 to Detect and Quantify  O  6 -Alkylated Guanine Bases in DNA.","citation":"Toxics 2024 Sep 04;12(9)","abstract":"Humans are unavoidably exposed to numerous different mutagenic DNA alkylating agents (AAs), but their role in the initiation of cancers is uncertain, in part due to difficulties in assessing human exposure. To address this, we have developed a screening method that measures promutagenic  O  6 -alkylguanines ( O  6 -AlkGs) in DNA and applied it to human DNA samples. The method exploits the ability of the  Schizosaccharomyces pombe  alkyltransferase-like protein (Atl1) to recognise and bind to a wide range of  O  6 -AlkGs in DNA. We established an Atl1-based slot-blot (ASB) assay and validated it using calf thymus DNA alkylated in vitro with a range of alkylating agents and both calf thymus and human placental DNA methylated in vitro with temozolomide (TMZ). ASB signals were directly proportional to the levels of  O  6 -meG in these controls. Pre-treatment of DNA with the DNA repair protein  O  6 -methylguanine-DNA methyltransferase (MGMT) reduced binding of Atl1, confirming its specificity. In addition, MCF 10A cells were treated with 500 μM TMZ and the extracted DNA, analysed using the ASB, was found to contain 1.34 fmoles  O  6  -meG/μg DNA. Of six human breast tumour DNA samples assessed, five had detectable  O  6 -AlkG levels (mean ± SD 1.24 ± 0.25  O  6 -meG equivalents/μg DNA. This study shows the potential usefulness of the ASB assay to detect and quantify total  O  6 -AlkGs in human DNA samples.","doi":"10.3390/toxics12090649","authors":"Yaakub H, Howell A, Margison GP, Povey AC","authors_abbrev":"Yaakub H et al.","pubmed_publication_date":"04 Sep 2024","pubmed_entrez_date":"2024-09-27","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-09-27 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1250.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21818608","title":"The abc1-/coq8- respiratory-deficient mutant of Schizosaccharomyces pombe suffers from glutathione underproduction and hyperaccumulates Cd2+.","citation":"Folia Microbiol (Praha) 2011 Jul;56(4):353-9","abstract":"The abc1(-)/coq8(-) gene deletion respiratory-deficient mutant NBp17 of fission yeast Schizosaccharomyces pombe displayed a phenotypic fermentation pattern with enhanced production of glycerol and acetate, and also possessed oxidative stress-sensitive phenotypes to H(2)O(2), menadione, tBuOOH, Cd(2+), and chromate in comparison with its parental respiratory-competent strain HNT. As a consequence of internal stress-inducing mutation, adaptation processes to restore the redox homeostasis of mutant NBp17 cells were detected in minimal glucose medium. Mutant NBp17 produced significantly increased amounts of O(2)•- and H(2)O(2) as a result of the decreased internal glutathione concentration and the only slightly increased glutathione reductase activity. The Cr(VI) reduction capacity and hence the •OH production ability were decreased. The mutant cells demonstrated increased specific activities of superoxide dismutases and glutathione reductase (but not catalase) to detoxify at least partially the overproduction of reactive oxygen species. All these features may be explained by the decreased redox capacity of the mutant cells. Most notably, mutant NBp17 hyperaccumulated yellow CdS.","doi":"10.1007/s12223-011-0058-5","authors":"Gazdag Z, Fujs S, Koszegi B, Kálmán N, Papp G, Emri T, Belágyi J, Pócsi I, Raspor P, Pesti M","authors_abbrev":"Gazdag Z et al.","pubmed_publication_date":"Jul 2011","pubmed_entrez_date":"2011-08-06","publication_year":"2011","canto_session_key":"5900a3d7d2aeb03c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-03 08:44:23","canto_approved_date":"2022-06-22 13:56:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-03 08:44:15","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.18"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-03"},{"uniquename":"EMBL:AU008311","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4F6.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15930132","title":"Spindle checkpoint signaling requires the mis6 kinetochore subcomplex, which interacts with mad2 and mitotic spindles.","citation":"Mol Biol Cell 2005 Aug;16(8):3666-77","abstract":"The spindle checkpoint coordinates cell cycle progression and chromosome segregation by inhibiting anaphase promoting complex/cyclosome until all kinetochores interact with the spindle properly. During early mitosis, the spindle checkpoint proteins, such as Mad2 and Bub1, accumulate at kinetochores that do not associate with the spindle. Here, we assess the requirement of various kinetochore components for the accumulation of Mad2 and Bub1 on the kinetochore in fission yeast and show that the necessity of the Mis6-complex and the Nuf2-complex is an evolutionarily conserved feature in the loading of Mad2 onto the kinetochore. Furthermore, we demonstrated that Nuf2 is required for maintaining the Mis6-complex on the kinetochore during mitosis. The Mis6-complex physically interacts with Mad2 under the condition that the Mad2-dependent checkpoint is activated. Ectopically expressed N-terminal fragments of Mis6 localize along the mitotic spindle, highlighting the potential binding ability of Mis6 not only to the centromeric chromatin but also to the spindle microtubules. We propose that the Mis6-complex, in collaboration with the Nuf2-complex, monitors the spindle-kinetochore attachment state and acts as a platform for Mad2 to accumulate at unattached kinetochores.","authors":"Saitoh S, Ishii K, Kobayashi Y, Takahashi K","authors_abbrev":"Saitoh S et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-06-03","publication_year":"2005","canto_session_key":"9a148299ab274c61","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-04-29 11:49:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-26 17:49:33","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.20c","SPBC1861.01c","SPBC20F10.06","SPAC27F1.04c","SPBC1105.17","SPCC1322.12c","SPBC18E5.03c","SPBC409.04c","SPCC1795.01c","SPAC821.08c"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2015-11-26"},{"uniquename":"EMBL:AU008147","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000004","title":"Comments","abstract":"Transitive assignments using UniProtKB keywords. The UniProtKB keyword controlled vocabulary has been created and used by the UniProt Knowledgebase (UniProtKB) to supply 10 different categories of information to UniProtKB entries. Further information on the UniProtKB keyword resource can be found at http://www.uniprot.org/docs/keywlist. <br>Further information on the UniProt annotation methods is available at  https://www.uniprot.org/help/manual_curation and https://www.uniprot.org/help/automatic_annotation.","authors":"GOA curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25269894","title":"Fission yeast Drp1 is an essential protein required for recovery from DNA damage and chromosome segregation.","citation":"DNA Repair (Amst) 2014 Dec;24:98-106","abstract":"DNA double strand breaks (DSBs) are the most critical types of DNA damage that can leads to chromosomal aberrations, genomic instability and cancer. Several genetic disorders such as Xeroderma pigmentosum are linked with defects in DNA repair. Human Rint1, a TIP1 domain containing protein is involved in membrane trafficking but its role in DNA damage response is elusive. In this study we characterized the role of Drp1 (damage responsive protein 1), a Rint1 family protein during DNA damage response in fission yeast. We identified that Drp1 is an essential protein and indispensable for survival and growth. Using in vitro random mutagenesis approach we isolated a temperature sensitive mutant allele of drp1 gene (drp1-654) that exhibits sensitivity to DNA damaging agents, in particular to alkylation damage and UV associated DNA damage. The drp1-654 mutant cells are also sensitive to double strand break inducing agent bleomycin. Genetic interaction studies identified that Rad50 and Drp1 act in the same pathway during DNA damage response and the physical interaction of Drp1 with Rad50 was unaffected in drp1-654 mutant at permissive as well as non permissive temperature. Furthermore Drp1 was found to be required for the recovery from MMS induced DNA damage. We also demonstrated that the Drp1 protein localized to nucleus and was required to maintain the chromosome stability.","doi":"10.1016/j.dnarep.2014.09.006","authors":"Ranjan R, Ahamad N, Ahmed S","authors_abbrev":"Ranjan R et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-10-02","publication_year":"2014","canto_session_key":"282e0461e85eb34d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-13 15:07:53","canto_approved_date":"2020-01-14 11:59:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-13 16:42:29","canto_added_date":"2014-10-03 00:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC691.02c","SPAC1556.01c","SPCC1259.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-06-13"},{"uniquename":"PMID:7983142","title":"A calcineurin-like gene ppb1+ in fission yeast: mutant defects in cytokinesis, cell polarity, mating and spindle pole body positioning.","citation":"J Cell Sci 1994 Jul;107 ( Pt 7):1725-35","abstract":"A calcineurin (type 2B)-like protein phosphatase gene designated ppb1+ was isolated from the fission yeast Schizosaccharomyces pombe. The predicted amino acid sequence was 57% identical to rat PP2B alpha. ppb1 null mutant could form colonies at 33 degrees C but the size of the colonies was small at 22 degrees C. Cytokinesis was greatly delayed at 22 degrees C, and a large number of multi-septate cells were produced. The cell polarity control was impaired, causing branched cells. ppb1 null was virtually sterile. These phenotypes were rescued by a plasmid carrying the ppb1+ gene. Multi-septate cells were also produced in wild type at 22 degrees C by cyclosporin A, an inhibitor of calcineurin. This drug effect was enhanced in stst1 null mutant, which was hypersensitive to various drugs and cations. ppb1 null was not affected by cyclosporin A, consistent with the hypothesis that ppb1 is its target. Double-mutant analysis indicated that ppb1 had a function related to that of two other phosphatases, type 1-like dis2 and 2A-like ppa2.ppb1 null-sts1 null showed the severe multi-septate phenotype in the absence of cyclosporin A. ppb1+ and sts1+ gene functions are related. The double mutant ppb1-sts5 was lethal, indicating that the ppb1+ gene shared an essential function with the sts5+ gene. Overexpression of ppb1+ caused anomalies in cell and nuclear shape, microtubule arrays and spindle pole body positioning in interphase cells. Thus the ppb1+ gene appears to be involved in cytokinesis, mating, transport, nuclear and spindle pole body positioning, and cell shape.","authors":"Yoshida T, Toda T, Yanagida M","authors_abbrev":"Yoshida T et al.","pubmed_publication_date":"Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_session_key":"ece9176a66feeefa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-03 10:30:08","canto_approved_date":"2025-12-23 12:53:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-28 16:05:06","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16C4.09","SPAC823.15","SPCC31H12.05c","SPBP4H10.04","SPBC16H5.07c","SPCC1739.12","SPBC776.02c","SPAC20G4.07c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-06-03"},{"uniquename":"PMID:26131711","title":"Two Distinct Cdc2 Pools Regulate Cell Cycle Progression and the DNA Damage Response in the Fission Yeast S.pombe.","citation":"PLoS One 2015;10(7):e0130748","abstract":"The activity of Cdc2 (CDK1) kinase, which coordinates cell cycle progression and DNA break repair, is blocked upon its phosphorylation at tyrosine 15 (Y15) by Wee1 kinase in the presence of DNA damage. How Cdc2 can support DNA repair whilst being inactivated by the DNA damage checkpoint remains to be explained. Human CDK1 is phosphorylated by Myt1 kinase at threonine 14 (T14) close to its ATP binding site before being modified at threonine 161 (T167Sp) in its T-loop by the CDK-activating kinase (CAK). While modification of T161 promotes association with the cyclin partner, phosphorylation of T14 inhibits the CDK1-cyclin complex. This inhibition is further enforced by the modification of Y15 by Wee1 in the presence of DNA lesions. In S.pombe, the dominant inhibition of Cdc2 is provided by the phosphorylation of Y15 and only a small amount of Cdc2 is modified at T14 when cells are in S phase. Unlike human cells, both inhibitory modifications are executed by Wee1. Using the novel IEFPT technology, which combines isoelectric focusing (IEF) with Phos-tag SDS electrophoresis (PT), we report here that S.pombe Cdc2 kinase exists in seven forms. While five forms are phosphorylated, two species are not. Four phospho-forms associate with cyclin B (Cdc13) of which only two are modified at Y15 by Wee1. Interestingly, only one Y15-modified species carries also the T14 modification. The fifth phospho-form has a low affinity for cyclin B and is neither Y15 nor T14 modified. The two unphosphorylated forms may contribute directly to the DNA damage response as only they associate with the DNA damage checkpoint kinase Chk1. Interestingly, cyclin B is also present in the unphosphorylated pool. We also show that the G146D mutation in Cdc2.1w, which renders Cdc2 insensitive to Wee1 inhibition, is aberrantly modified in a Wee1-dependent manner. In conclusion, our work adds support to the idea that two distinct Cdc2 pools regulate cell cycle progression and the response to DNA damage.","doi":"10.1371/journal.pone.0130748","authors":"Caspari T, Hilditch V","authors_abbrev":"Caspari T et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-07-02","publication_year":"2015","canto_session_key":"8c798b5961e500db","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Thomas Caspari","canto_first_approved_date":"2016-11-21 10:51:50","canto_approved_date":"2025-09-03 16:25:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-01 15:14:30","canto_added_date":"2015-07-03 00:20:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Thomas Caspari","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.14","SPCC1259.13","SPBC11B10.09","SPBC582.03","SPCC18B5.03"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-11-21"},{"uniquename":"PMID:11370745","title":"Microtubules and actin cytoskeleton in Cryptococcus neoformans compared with ascomycetous budding and fission yeasts.","citation":"Eur J Cell Biol 2001 Apr;80(4):303-11","abstract":"Actin cytoskeleton and microtubules were studied in a human fungal pathogen, the basidiomycetous yeast Cryptococcus neoformans (haploid phase of Filobasidiella neoformans), during its asexual reproduction by budding using fluorescence and electron microscopy. Staining with rhodamine-conjugated phalloidin revealed an F-actin cytoskeleton consisting of cortical patches, cables and cytokinetic ring. F-actin patches accumulated at the regions of cell wall growth, i. e. in sterigma, bud and septum. In mother cells evenly distributed F-actin patches were joined to F-actin cables, which were directed to the growing sterigma and bud. Some F-actin cables were associated with the cell nucleus. The F-actin cytokinetic ring was located in the bud neck, where the septum originated. Antitubulin TAT1 antibody revealed a microtubular cytoskeleton consisting of cytoplasmic and spindle microtubules. In interphase cells cytoplasmic microtubules pointed to the growing sterigma and bud. As the nucleus was translocated to the bud for mitosis, the cytoplasmic microtubules disassembled and were replaced by a short intranuclear spindle. Astral microtubules then emanated from the spindle poles. Elongation of the mitotic spindle from bud to mother cell preceded nuclear division, followed by cytokinesis (septum formation in the bud neck). Electron microscopy of ultrathin sections of chemically fixed and freeze-substituted cells revealed filamentous bundles directed to the cell cortex. The bundles corresponded in width to the actin microfilament cables. At the bud neck numerous ribosomes accumulated before septum synthesis. We conclude: (i) the topology of F-actin patches, cables and rings in C. neoformans resembles ascomycetous budding yeast Saccharomyces, while the arrangement of interphase and mitotic microtubules resembles ascomycetous fission yeast Schizosaccharomyces. The organization of the cytoskeleton of the mitotic nucleus, however, is characteristic of basidiomycetous yeasts. (ii) A specific feature of C. neoformans was the formation of a cylindrical sterigma, characterized by invasion of F-actin cables and microtubules, followed by accumulation of F-actin patches around its terminal region resulting in development of an isodiametrical bud.","authors":"Kopecká M, Gabriel M, Takeo K, Yamaguchi M, Svoboda A, Ohkusu M, Hata K, Yoshida S","authors_abbrev":"Kopecká M et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-05-24","publication_year":"2001","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25989903","title":"The fission yeast MTREC complex targets CUTs and unspliced pre-mRNAs to the nuclear exosome.","citation":"Nat Commun 2015 May 20;6:7050","abstract":"Cryptic unstable transcripts (CUTs) are rapidly degraded by the nuclear exosome. However, the mechanism by which they are recognized and targeted to the exosome is not fully understood. Here we report that the MTREC complex, which has recently been shown to promote degradation of meiotic mRNAs and regulatory ncRNAs, is also the major nuclear exosome targeting complex for CUTs and unspliced pre-mRNAs in Schizosaccharomyces pombe. The MTREC complex specifically binds to CUTs, meiotic mRNAs and unspliced pre-mRNA transcripts and targets these RNAs for degradation by the nuclear exosome, while the TRAMP complex has only a minor role in this process. The MTREC complex physically interacts with the nuclear exosome and with various RNA-binding and RNA-processing complexes, coupling RNA processing to the RNA degradation machinery. Our study reveals the central role of the evolutionarily conserved MTREC complex in RNA quality control, and in the recognition and elimination of CUTs.","doi":"10.1038/ncomms8050","authors":"Zhou Y, Zhu J, Schermann G, Ohle C, Bendrin K, Sugioka-Sugiyama R, Sugiyama T, Fischer T","authors_abbrev":"Zhou Y et al.","pubmed_publication_date":"20 May 2015","pubmed_entrez_date":"2015-05-21","publication_year":"2015","canto_session_key":"aebb22b799de8e58","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-20 09:19:33","canto_approved_date":"2024-04-04 11:00:57","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-11-19 20:48:00","canto_added_date":"2015-05-22 00:19:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16E9.12c","SPAC57A7.04c","SPCC794.09c","SPAC6G10.07","SPBC660.15","SPAC140.04","SPBC902.04","SPBC725.08","SPAC7D4.14c","SPAC1F3.01","SPAC12G12.13c","SPAC1006.03c","SPAC17H9.02","SPCC736.12c","SPBC13A2.01c","SPBC20F10.05","SPBC646.04","SPBC337.12"],"gene_count":18,"ltp_gene_count":9,"approved_date":"2024-01-20"},{"uniquename":"PMID:15449309","title":"Chr4, a Schizosaccharomyces pombe homologue of the Saccharomyces cerevisiae Chs4p/Skt5p protein, is related to septum formation and is required for the proper localization of Chs2.","citation":"Yeast 2004 Sep;21(12):1005-19","abstract":"In Saccharomyces cerevisiae, Chs4p directly interacts with chitin synthase III (Chs3p) to act as a post-translational regulator of the Chs3p complex. We identified four Chs4p homologous proteins in Schizosaccharomyces pombe which we named Chr1, Chr2, Chr3 and Chr4 (putative chitin synthase regulatory factor). We assessed the functions of these proteins and found that while overproduction of Chr1, Chr2 or Chr3 did not affect the cellular morphology of wild-type Sz. pombe cells, overproduction of Chr4 caused the cells to form multi-septa and delayed their growth. All multiple disruptants of chr1, chr2, chr3 and chr4 grew normally under a variety of growth conditions. However, while chitin synthase II (Chs2) normally localizes exclusively at the septum, in many chr4-disrupted cells it was found in the cytoplasm and the septa. Chs2 did localize at the abnormal septa caused by the overproduction of chr4+. Chr4-13Myc expression was unaffected by the different media or growth conditions in both wild-type and the chs2 disruptant. Chs2 expression was also unaltered by the absence of Chr4. Moreover, Chr4-13Myc localized mostly at the tips and the septum during vegetative growth in chs2, chr1, chr2 and chr3 disruptants as well as in wild-type. Thus, chr4+ is involved in septum formation and is required for the proper localization of Chs2 at the septum in Sz. pombe.","authors":"Matsuo Y, Matsuura Y, Tanaka K, Matsuda H, Kawamukai M","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-09-28","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1289.01c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:15047724","title":"Disruption of the plr1+ gene encoding pyridoxal reductase of Schizosaccharomyces pombe.","citation":"J Biochem 2004 Feb;135(2):225-30","abstract":"Pyridoxal (PL) reductase encoded by the plr1(+) gene practically catalyzes the irreversible reduction of PL by NADPH to form pyridoxine (PN). The enzyme has been suggested to be involved in the salvage synthesis of pyridoxal 5'-phosphate (PLP), a coenzyme form of vitamin B(6), or the excretion of PL as PN from yeast cells. In this study, a PL reductase-disrupted (plr1 Delta) strain was constructed and its phenotype was examined. The plr1 Delta cells showed almost the same growth curve as that of wild-type cells in YNB and EMM media. In EMM, the plr1 Delta strain became flocculent at the late stationary phase for an unknown reason. The plr1 Delta cells showed low but measurable PL reductase activity catalyzed by some other protein(s) than the enzyme encoded by the plr1(+) gene, which maintained the flow of \"PL --> PN --> PNP --> PLP\" in the salvage synthesis of PLP. The total vitamin B(6) and pyridoxamine 5'-phosphate contents in the plr1 Delta cells were significantly lower than those in the wild-type ones. The percentages of the PLP amount as to the other vitamin B(6) compounds were similar in the two cell types. The amount of PL in the culture medium of the disruptant was significantly higher than that in the wild-type. In contrast, PN was much higher in the latter than the former. The plr1 Delta cells accumulated a 6.1-fold higher amount of PL than the wild-type ones when they were incubated with PL. The results showed that PL reductase encoded by the plr1(+ )gene is involved in the excretion of PL after reducing it to PN, and may not participate in the salvage pathway for PLP synthesis.","authors":"Morita T, Takegawa K, Yagi T","authors_abbrev":"Morita T et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2004-03-30","publication_year":"2004","canto_session_key":"36a8fd70fcda9d3d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-16 04:05:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-18 16:35:38","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-12-18"},{"uniquename":"PMID:22030861","title":"Generation of a set of conditional analog-sensitive alleles of essential protein kinases in the fission yeast Schizosaccharomyces pombe.","citation":"Cell Cycle 2011 Oct 15;10(20):3527-32","abstract":"The genome of the fission yeast Schizosaccharomyces pombe encodes for 17 protein kinases that are essential for viability. Studies of the essential kinases often require the use of mutant strains carrying conditional alleles. To inactivate these kinases conditionally, we applied a recently developed chemical genetic strategy. The mutation of a single residue in the ATP-binding pocket confers sensitivity to small-molecule inhibitors, allowing for specific inactivation of the modified kinase. Using this approach, we constructed conditional analog-sensitive alleles of 13 essential protein kinases in the fission yeast S. pombe.","doi":"10.4161/cc.10.20.17792","authors":"Cipak L, Zhang C, Kovacikova I, Rumpf C, Miadokova E, Shokat KM, Gregan J","authors_abbrev":"Cipak L et al.","pubmed_publication_date":"15 Oct 2011","pubmed_entrez_date":"2011-10-28","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7502077","title":"Conserved initiator proteins in eukaryotes.","citation":"Science 1995 Dec 08;270(5242):1667-71","abstract":"The origin recognition complex (ORC), a multisubunit protein identified in Saccharomyces cerevisiae, binds to chromosomal replicators and is required for the initiation of cellular DNA replication. Complementary DNAs (cDNAs) encoding proteins related to the two largest subunits of ORC were cloned from various eukaryotes. The cDNAs encoding proteins related to S. cerevisiae Orc1p were cloned from the budding yeast Kluyveromyces lactis, the fission yeast Schizosaccharomyces pombe, and human cells. These proteins show similarity to regulators of the S and M phases of the cell cycle. Genetic analysis of orc1+ from S. pombe reveals that it is essential for cell viability. The cDNAs encoding proteins related to S. cerevisiae Orc2p were cloned from Arabidopsis thaliana, Caenorhabditis elegans, and human cells. The human ORC-related proteins interact in vivo to form a complex. These studies studies suggest that ORC subunits are conserved and that the role of ORC is a general feature of eukaryotic DNA replication.","authors":"Gavin KA, Hidaka M, Stillman B","authors_abbrev":"Gavin KA et al.","pubmed_publication_date":"08 Dec 1995","pubmed_entrez_date":"1995-12-08","publication_year":"1995","canto_session_key":"583e1c4287dab5f2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2012-12-03 17:09:33","canto_approved_date":"2021-04-16 12:53:20","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-12-03 17:09:09","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-03"},{"uniquename":"PMID:16394105","title":"The V260I mutation in fission yeast alpha-tubulin Atb2 affects microtubule dynamics and EB1-Mal3 localization and activates the Bub1 branch of the spindle checkpoint.","citation":"Mol Biol Cell 2006 Mar;17(3):1421-35","abstract":"We have identified a novel temperature-sensitive mutant of fission yeast alpha-tubulin Atb2 (atb2-983) that contains a single amino acid substitution (V260I). Atb2-983 is incorporated into the microtubules, and their overall structures are not altered noticeably, but microtubule dynamics is compromised during interphase. atb2-983 displays a high rate of chromosome missegregation and is synthetically lethal with deletions in a subset of spindle checkpoint genes including bub1, bub3, and mph1, but not with mad1, mad2, and mad3. During early mitosis in this mutant, Bub1, but not Mad2, remains for a prolonged period in the kinetochores that are situated in proximity to one of the two SPBs (spindle pole bodies). High dosage mal3(+), encoding EB1 homologue, rescues atb2-983, suggesting that Mal3 function is compromised. Consistently, Mal3 localization and binding between Mal3 and Atb2-983 are impaired significantly, and a mal3 single mutant, such as atb2-983, displays prolonged Bub1 kinetochore localization. Furthermore in atb2-983 back-and-forth centromere oscillation during prometaphase is abolished. Intriguingly, this oscillation still occurs in the mal3 mutant, indicating that there is another defect independent of Mal3. These results show that microtubule dynamics is important for coordinated execution of mitotic events, in which Mal3 plays a vital role.","authors":"Asakawa K, Kume K, Kanai M, Goshima T, Miyahara K, Dhut S, Tee WW, Hirata D, Toda T","authors_abbrev":"Asakawa K et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-01-06","publication_year":"2006","canto_session_key":"a4361279dd5b39bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-12-18 14:36:43","canto_approved_date":"2025-09-02 16:49:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-28 09:49:18","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":50,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.14c","SPBC800.05c","SPAC23H3.08c","SPBC26H8.07c","SPBC16A3.15c","SPCC1322.12c","SPAC12G12.14c","SPAC18G6.15","SPBC106.01","SPCC1795.01c","SPBC3D6.04c","SPBC20F10.06","SPCC18.04"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2016-12-18"},{"uniquename":"PMID:17947424","title":"Msc1 acts through histone H2A.Z to promote chromosome stability in Schizosaccharomyces pombe.","citation":"Genetics 2007 Nov;177(3):1487-97","abstract":"As a central component of the DNA damage checkpoint pathway, the conserved protein kinase Chk1 mediates cell cycle progression when DNA damage is generated. Msc1 was identified as a multicopy suppressor capable of facilitating survival in response to DNA damage of cells mutant for chk1. We demonstrate that loss of msc1 function results in an increased rate of chromosome loss and that an msc1 null allele exhibits genetic interactions with mutants in key kinetochore components. Multicopy expression of msc1 robustly suppresses a temperature-sensitive mutant (cnp1-1) in the centromere-specific histone H3 variant CENP-A, and localization of CENP-A to the centromere is compromised in msc1 null cells. We present several lines of evidence to suggest that Msc1 carries out its function through the histone H2A variant H2A.Z, encoded by pht1 in fission yeast. Like an msc1 mutant, a pht1 mutant also exhibits chromosome instability and genetic interactions with kinetochore mutants. Suppression of cnp1-1 by multicopy msc1 requires pht1. Likewise, suppression of the DNA damage sensitivity of a chk1 mutant by multicopy msc1 also requires pht1. We present the first genetic evidence that histone H2A.Z may participate in centromere function in fission yeast and propose that Msc1 acts through H2A.Z to promote chromosome stability and cell survival following DNA damage.","authors":"Ahmed S, Dul B, Qiu X, Walworth NC","authors_abbrev":"Ahmed S et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-10-20","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC343.11c","SPBC1105.17","SPAC1687.20c","SPBC11B10.10c","SPBC409.04c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:21920317","title":"Repositioning of aurora B promoted by chiasmata ensures sister chromatid mono-orientation in meiosis I.","citation":"Dev Cell 2011 Sep 13;21(3):534-45","abstract":"During meiosis I, kinetochores of sister chromatids are juxtaposed or fused and mono-orient, while homologous chromosomes that are paired by chiasmata (bivalents) have to biorient. In the absence of chiasmata, biorientation of sister chromatids (univalents), which carries a risk of aneuploidy, has been occasionally detected in several species, including humans. We show in fission yeast that biorientation of fused sister kinetochores predominates during early prometaphase I. Without chiasmata, this undesirable biorientation of univalents persists and eventually evades the spindle assembly checkpoint, provoking abnormal anaphase. When univalents are connected by chiasmata or by an artificial tether, this erroneous attachment is converted to monopolar attachment and stabilized. This stabilization is apparently achieved by a chromosome configuration that brings kinetochores to the outer edge of the bivalent, while bringing Aurora B, a destabilizer of kinetochore-microtubule attachment, inward. Our results elucidate how chiasmata favor biorientation of bivalents over that of univalents at meiosis I.","doi":"10.1016/j.devcel.2011.08.012","authors":"Sakuno T, Tanaka K, Hauf S, Watanabe Y","authors_abbrev":"Sakuno T et al.","pubmed_publication_date":"13 Sep 2011","pubmed_entrez_date":"2011-09-17","publication_year":"2011","canto_session_key":"c83c3de5e5b69049","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takeshi Sakuno","canto_first_approved_date":"2018-01-20 20:54:17","canto_approved_date":"2025-09-02 20:35:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-02 21:10:07","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Takeshi Sakuno","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.03c","SPAC17A5.11","SPBC20F10.06","SPCC1753.03c","SPCC4E9.01c","SPBC29A10.14","SPCC320.13c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-01-20"},{"uniquename":"PMID:27694842","title":"Structural basis of mRNA-cap recognition by Dcp1-Dcp2.","citation":"Nat Struct Mol Biol 2016 Nov;23(11):987-994","abstract":"Removal of the 5' cap on mRNA by the decapping enzyme Dcp2 is a critical step in 5'-to-3' mRNA decay. Understanding the structural basis of Dcp2 activity has been a challenge because Dcp2 is dynamic and has weak affinity for the cap substrate. Here we present a 2.6-Å-resolution crystal structure of a heterotrimer of fission yeast Dcp2, its essential activator Dcp1, and the human NMD cofactor PNRC2, in complex with a tight-binding cap analog. Cap binding is accompanied by a conformational change in Dcp2, thereby forming a composite nucleotide-binding site comprising conserved residues in the catalytic and regulatory domains. Kinetic analysis of PNRC2 revealed that a conserved short linear motif enhances both substrate affinity and the catalytic step of decapping. These findings explain why Dcp2 requires a conformational change for efficient catalysis and reveals that coactivators promote RNA binding and the catalytic step of decapping, possibly through different conformational states.","doi":"10.1038/nsmb.3301","authors":"Mugridge JS, Ziemniak M, Jemielity J, Gross JD","authors_abbrev":"Mugridge JS et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-11-05","publication_year":"2016","canto_session_key":"79469c0fd3b894c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-07-25 15:38:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-25 15:38:24","canto_added_date":"2016-10-07 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19A8.12","SPBC3B9.21"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-07-25","pdb_entries":[{"pdb_id":"5kq4","gene_chains":[{"gene_uniquename":"SPAC19A8.12","chain":"B/E","position":"1-244"},{"gene_uniquename":"SPBC3B9.21","chain":"A/D","position":"1-127"}],"title":"Crystal structure of S. pombe Dcp1/Dcp2 in complex with H. sapiens PNRC2 and synthetic cap analog","entry_authors":"Mugridge JS,Ziemniak M,Jemielity J,Gross JD","entry_authors_abbrev":"Mugridge JS et al.","reference_uniquename":"PMID:27694842","experimental_method":"X-ray","resolution":"2.56"},{"pdb_id":"5kq1","gene_chains":[{"gene_uniquename":"SPAC19A8.12","chain":"B/E","position":"1-244"},{"gene_uniquename":"SPBC3B9.21","chain":"A/D","position":"1-127"}],"title":"Crystal structure of S. pombe Dcp1/Dcp2 in complex with H. sapiens PNRC2","entry_authors":"Mugridge JS,Ziemniak M,Jemielity J,Gross JD","entry_authors_abbrev":"Mugridge JS et al.","reference_uniquename":"PMID:27694842","experimental_method":"X-ray","resolution":"3.002"}]},{"uniquename":"EMBL:SPD179","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9459302","title":"Identification of Myo3, a second type-II myosin heavy chain in the fission yeast Schizosaccharomyces pombe.","citation":"FEBS Lett 1997 Dec 29;420(2-3):161-6","abstract":"We cloned the myo3+ gene of Schizosaccharomyces pombe which encodes a type-II myosin heavy chain. myo3 null cells showed a defect in cytokinesis under certain conditions. Overproduction of Myo3 also showed a defect in cytokinesis. Double mutant analysis indicated that Myo3 genetically interacts with Cdc8 tropomyosin and actin. Myo3 may be implicated in cytokinesis and stabilization of F-actin cables. Moreover, the function of Myo2 can be replaced by overexpressed Myo3. We observed a modest synthetic interaction between Myo2 and Myo3. Thus, Myo2 and Myo3 seem to cooperate in the formation of the F-actin ring in S. pombe.","authors":"Motegi F, Nakano K, Kitayama C, Yamamoto M, Mabuchi I","authors_abbrev":"Motegi F et al.","pubmed_publication_date":"29 Dec 1997","pubmed_entrez_date":"1998-02-12","publication_year":"1997","canto_session_key":"8db0c2a727e8b74f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-03 17:01:10","canto_approved_date":"2023-01-18 09:24:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-28 17:46:25","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPAC4A8.05c","SPBC32H8.12c","SPCC645.05c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-09-03"},{"uniquename":"PMID:11118633","title":"Cloning, expression and regulation of Schizosaccharomyces pombe gene encoding thioltransferase.","citation":"Biochim Biophys Acta 2000 Dec 15;1517(1):171-5","abstract":"The genomic DNA encoding thioltransferase was isolated from Schizosaccharomyces pombe using the polymerase chain reaction. The amplified DNA fragment was confirmed by Southern hybridization, completely digested with HindIII and BamHI, and then ligated into the yeast-Escherichia coli shuttle vector pRS316, which resulted in plasmid pEH1. The insert of plasmid pEH1 was transferred into the multi-copy vector YEp357 to generate plasmid pYEH1. The determined nucleotide sequence harbors an open reading frame consisting of four exons and three introns, which encodes a polypeptide of 101 amino acids with a molecular mass of 11261 Da. Thioltransferase activity was increased 1.6-fold in Saccharomyces cerevisiae containing plasmid pYEH1, and 1.8- and 2.7-fold in S. pombe containing plasmid pEH1 and pYEH1, respectively. The upstream sequence and the region encoding the N-terminal six amino acids were fused into promoterless beta-galactosidase gene of the shuttle vector YEp357R to generate the fusion plasmid pYEHR1. Synthesis of beta-galactosidase from the fusion plasmid was found to be enhanced by zinc and NO-generating S-nitroso-N-acetylpenicillamine.","authors":"Cho YW, Kim HG, Park EH, Fuchs JA, Lim CJ","authors_abbrev":"Cho YW et al.","pubmed_publication_date":"15 Dec 2000","pubmed_entrez_date":"2000-12-19","publication_year":"2000","canto_session_key":"e103a19b812149e7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:53:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 14:46:56","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F10.20"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-05"},{"uniquename":"PMID:19101542","title":"Cbf11 and Cbf12, the fission yeast CSL proteins, play opposing roles in cell adhesion and coordination of cell and nuclear division.","citation":"Exp Cell Res 2009 May 01;315(8):1533-47","abstract":"The CSL (CBF1/RBP-Jkappa/Suppressor of Hairless/LAG-1) family is comprised of transcription factors essential for metazoan development, mostly due to their involvement in the Notch receptor signaling pathway. Recently, we identified two novel classes of CSL genes in the genomes of several fungal species, organisms lacking the Notch pathway. In this study, we characterized experimentally cbf11+ and cbf12+, the two CSL genes of Schizosaccharomyces pombe, in order to elucidate the CSL function in fungi. We provide evidence supporting their identity as genuine CSL genes. Both cbf11+ and cbf12+ are non-essential; they have distinct expression profiles and code for nuclear proteins with transcription activation potential. Significantly, we demonstrated that Cbf11 recognizes specifically the canonical CSL response element GTGA/GGAA in vitro. The deletion of cbf11+ is associated with growth phenotypes and altered colony morphology. Furthermore, we found that Cbf11 and Cbf12 play opposite roles in cell adhesion, nuclear and cell division and their coordination. Disturbed balance of the two CSL proteins leads to cell separation defects (sep phenotype), cut phenotype, and high-frequency diploidization in heterothallic strains. Our data show that CSL proteins operate in an organism predating the Notch pathway, which should be of relevance to the understanding of (Notch-independent) CSL functions in metazoans.","doi":"10.1016/j.yexcr.2008.12.001","authors":"Prevorovský M, Grousl T, Stanurová J, Rynes J, Nellen W, Půta F, Folk P","authors_abbrev":"Prevorovský M et al.","pubmed_publication_date":"01 May 2009","pubmed_entrez_date":"2008-12-23","publication_year":"2009","canto_session_key":"4bb1e87e6d6b95f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-04-07 16:15:25","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-08-17 11:25:22","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.13","SPCC736.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-08-17"},{"uniquename":"PMID:9062192","title":"Phosphorylation of RNA-binding protein controls cell cycle switch from mitotic to meiotic in fission yeast.","citation":"Nature 1997 Mar 13;386(6621):187-90","abstract":"Meiosis generates haploid gametes from diploid cells and is an almost universal feature of eukaryotic organisms. But little is known about how the switch from mitotic to meiotic cell cycles is molecularly controlled. In the fission yeast Schizosaccharomyces pombe, inactivation of the protein kinase Pat1(Ran1) upon nutrient deprivation triggers entry into the meiotic cell cycle. Here we show that the RNA-binding protein Mei2 is a substrate of Pat1 kinase and that dephosphorylation of Mei2 is sufficient to switch cells from the mitotic cell cycle into meiosis. Mei2 is localized mainly in the cytoplasm of proliferating cells but is seen as a single spot close to the microtubule organizing centre in prophase nuclei during meiosis. Our results, and others from a metazoan, emphasize the crucial role of RNA-binding proteins in the initiation and execution of meiosis.","authors":"Watanabe Y, Shinozaki-Yabana S, Chikashige Y, Hiraoka Y, Yamamoto M","authors_abbrev":"Watanabe Y et al.","pubmed_publication_date":"13 Mar 1997","pubmed_entrez_date":"1997-03-13","publication_year":"1997","canto_session_key":"6dfef8615eb3cdaa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-09 23:20:35","canto_approved_date":"2025-09-22 06:37:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-12 17:02:26","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPBC19C2.05","SPNCRNA.103","SPBC119.04"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2018-06-09"},{"uniquename":"PMID:8001162","title":"Mutations in cyr1 and pat1 reveal pheromone-induced G1 arrest in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1994 Aug;26(2):105-12","abstract":"Investigations into sexual differentiation and pheromone response in the fission yeast Schizosaccharomyces pombe are complicated by the need to first starve the cells of nitrogen. Most mating-related experiments are therefore performed on non-dividing cells. Here we overcome this problem by using two mutants that bypass the nutritional requirements and respond to the M-factor mating pheromone in rich medium. The first mutant lacks the cyr1 gene which encodes adenylate cyclase and these cells contain no measurable amounts of cAMP. When M-factor is added to a growing h+ cyr1- strain it causes a transient G1 arrest of cell division, transcription of mat1-Pm, and elongation of the cells to form shmoos. The second mutant contains the temperature-sensitive pat1-114 allele. At 30 degrees C this mutant was previously shown not only to bypass the nutritional signal but also to stop growing in a state derepressed for pheromone-controlled functions. We now report that an h+ pat1-114 strain growing mitotically at 23 degrees C responds to M-factor. This shows that the pat1 protein kinase can be tuned to derepress nutritional signalling while repressing the other stages in the differentiation process.","authors":"Davey J, Nielsen O","authors_abbrev":"Davey J et al.","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_session_key":"b526b46d83c3fcf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-29 13:27:52","canto_approved_date":"2026-04-08 08:05:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-04-27 15:40:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPBC19C7.03","SPMTR.02"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2016-03-29"},{"uniquename":"PMID:16913842","title":"Analysis of aldosterone-induced differential receptor-independent protein patterns using 2D-electrophoresis and mass spectrometry.","citation":"Biol Chem 2006 Jul;387(7):917-29","abstract":"In the human body the mineralocorticoid aldosterone is responsible for maintaining water and electrolyte homeostasis and therefore controlling blood pressure. In addition, aldosterone has recently been associated with severe heart failure. Besides receptor-dependent action, the damaging effects of aldosterone may also be partly mediated through non-genomic mechanisms. The present study focuses on the mineralocorticoid receptor-independent action of aldosterone at the protein level. We chose the fission yeast Schizosaccharomyces pombe as a model organism, since this yeast does not contain nuclear steroid receptors, but many genes and regulatory mechanisms that are close to those of mammals. Using 2D-electrophoresis we identified for the first time protein spots affected by aldosterone in a nuclear receptor-free system. Mass spectrometry analysis using MALDI-TOF MS and nanoLC-MS/MS approaches allowed the unambiguous identification of 11 proteins that showed increased or decreased levels, which may represent newly identified players and pathways of aldosterone-induced action. Two proteins with a connection to osmotic regulation (NAD-dependent malic enzyme and glycerol-3-phosphate-dehydrogenase), as well as two proteins involved in the overall organization of the cytoskeleton, vip1 and glyceraldehyde-3-phosphate dehydrogenase, which was also found to be specifically affected by aldosterone in human HCT116 cells, are discussed.","authors":"Böhmer S, Carapito C, Wilzewski B, Leize E, Van Dorsselaer A, Bernhardt R","authors_abbrev":"Böhmer S et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-08-18","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17085965","title":"Function of rax2p in the polarized growth of fission yeast.","citation":"Mol Cells 2006 Oct 31;22(2):146-53","abstract":"Cell polarity is critical for the division, differentiation, migration, and signaling of eukaryotic cells. RAX2 of budding yeast encodes a membrane protein localized at the cell cortex that helps maintain the polarity of the bipolar pattern. Here, we designate SPAC6f6.06c as rax2+ of Schizosaccharomyces pombe, based on its sequence homology with RAX2, and examine its function in cell polarity. S. pombe rax2+ is not essential, but Deltarax2 cells are slightly smaller and grow slower than wild type cells. During vegetative growth or arrest at G1 by mutation of cdc10, deletion of rax2+ increases the number of cells failing old end growth just after division. In addition, this failure of old end growth is dramatically increased in Deltatea1Deltarax2, pointing to genetic interaction of rax2+ with tea1+. Deltarax2 cells contain normal actin and microtubule cytoskeletons, but lack actin cables, and the polarity factor for3p is not properly localized at the growing tip. In Deltarax2 cells, and endogenous rax2p is localized at the cell cortex of growing cell tips in an actin- and microtubule-dependent manner. However, Deltarax2 cells show no defects in cell polarity during shmoo formation and conjugation. Taken together, these observations suggest that rax2p controls the cell polarity of fission yeast during vegetative growth by regulating for3p localization.","authors":"Choi E, Lee K, Song K","authors_abbrev":"Choi E et al.","pubmed_publication_date":"31 Oct 2006","pubmed_entrez_date":"2006-11-07","publication_year":"2006","canto_session_key":"6601e49e3b15b194","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-08-18 11:02:48","canto_approved_date":"2023-04-24 18:45:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-25 11:10:22","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPCC1223.06","SPAC6F6.06c","SPCC895.05"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-08-18"},{"uniquename":"EMBL:AB084886","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:872891","title":"Control of cell size at division in fission yeast by a growth-modulated size control over nuclear division.","citation":"Exp Cell Res 1977 Jul;107(2):377-86","abstract":"","authors":"Fantes P, Nurse P","authors_abbrev":"Fantes P et al.","pubmed_publication_date":"Jul 1977","pubmed_entrez_date":"1977-07-01","publication_year":"1977","canto_session_key":"1725c65795f1d1b9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2015-07-20 12:13:42","canto_approved_date":"2019-06-14 13:15:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-07 10:26:15","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-07-20"},{"uniquename":"PMID:12552808","title":"[Mapping the interaction site of Rpb2 and Rpb3 subunit of fission yeast RNA polymerase II].","citation":"Wei Sheng Wu Xue Bao 2001 Oct;41(5):592-7","abstract":"To map the interacting site of subunit Rpb2 to subunit Rpb3 of RNA polymerase II in fission yeast Schizosaccharomyces pombe, the yeast two-hybrid system was employed in this paper to screen the interacting clones between Rpb2 and Rpb3.4 fragments of Rpb2 cDNA were cloned into the Ga14 BD vector pAS2. The 4 clones were named as pAS2 Rpb2-1, 2-2, 2-3 and 2-4, respectively. The complete cDNA of Rpb3 was cloned into the Gal 4 AD vector pGADGH. The clone was named as pGADGH Rpb3. The two-hybrid plasmids pGADGH Rpb3 and pAS2Rpb2-1, 2-2, 2-3 or 2-4 respectively were cotransformed into host cell yeast Y190. The interaction positive cotransformants were identified by beta-gal activity assay. The beta-gal positive cotransformants were selected from pGADGH Rpb3 and pAS2Rpb2-4 two-hybrid system. DNA sequencing and alignment results showed that the interacting site of Rpb2 to Rpb3 located within the fragment from base 2701 to 2966 of Rpb2 cDNA, or within the C-termini polypeptide from amino acid 902 to 989 of Rpb2 protein.","authors":"Qu Z, Zheng S, Gu H, Shi B","authors_abbrev":"Qu Z et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2003-01-30","publication_year":"2001","canto_session_key":"7a7b32e7d70e8443","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-04 22:05:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 22:05:02","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23G3.01","SPCC1442.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-04"},{"uniquename":"PMID:7878053","title":"Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport.","citation":"Proc Natl Acad Sci U S A 1995 Feb 28;92(5):1749-53","abstract":"RanGAP1 is the GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. Here, we report the amino acid sequence of RanGAP1, derived from cDNA and peptide sequences. We found it to be homologous to murine Fug1, implicated in early embryonic development, and to Rna1p from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Mutations of budding yeast RNA1 are known to result in defects in RNA processing and nucleocytoplasmic mRNA transport. Concurrently, we have isolated Rna1p as the major RanGAP activity from Sc. pombe. Both this protein and recombinant Rna1p were found to stimulate RanGTPase activity to an extent almost identical to that of human RanGAP1, indicating the functional significance of the sequence homology. The Ran-specific guanine nucleotide exchange factor RCC1 and its yeast homologues are restricted to the nucleus, while Rna1p is reported to be localized to the cytoplasm. We suggest a model in which both activities, nuclear GDP-to-GTP exchange on Ran and cytoplasmic hydrolysis of Ran-bound GTP, are essential for shuttling of Ran between the two cellular compartments. Thus, a defect in either of the two antagonistic regulators of Ran would result in a shutdown of Ran-dependent transport processes, in agreement with the almost identical phenotypes described for such defects in budding yeast.","authors":"Bischoff FR, Krebber H, Kempf T, Hermes I, Ponstingl H","authors_abbrev":"Bischoff FR et al.","pubmed_publication_date":"28 Feb 1995","pubmed_entrez_date":"1995-02-28","publication_year":"1995","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12861005","title":"Competition between the Rad50 complex and the Ku heterodimer reveals a role for Exo1 in processing double-strand breaks but not telomeres.","citation":"Mol Cell Biol 2003 Aug;23(15):5186-97","abstract":"The Mre11-Rad50-Nbs1(Xrs2) complex and the Ku70-Ku80 heterodimer are thought to compete with each other for binding to DNA ends. To investigate the mechanism underlying this competition, we analyzed both DNA damage sensitivity and telomere overhangs in Schizosaccharomyces pombe rad50-d, rad50-d pku70-d, rad50-d exo1-d, and pku70-d rad50-d exo1-d cells. We found that rad50 exo1 double mutants are more methyl methanesulfonate (MMS) sensitive than the respective single mutants. The MMS sensitivity of rad50-d cells was suppressed by concomitant deletion of pku70+. However, the MMS sensitivity of the rad50 exo1 double mutant was not suppressed by the deletion of pku70+. The G-rich overhang at telomere ends in taz1-d cells disappeared upon deletion of rad50+, but the overhang reappeared following concomitant deletion of pku70+. Our data suggest that the Rad50 complex can process DSB ends and telomere ends in the presence of the Ku heterodimer. However, the Ku heterodimer inhibits processing of DSB ends and telomere ends by alternative nucleases in the absence of the Rad50-Rad32 protein complex. While we have identified Exo1 as the alternative nuclease targeting DNA break sites, the identity of the nuclease acting on the telomere ends remains elusive.","authors":"Tomita K, Matsuura A, Caspari T, Carr AM, Akamatsu Y, Iwasaki H, Mizuno K, Ohta K, Uritani M, Ushimaru T, Yoshinaga K, Ueno M","authors_abbrev":"Tomita K et al.","pubmed_publication_date":"Aug 2003","pubmed_entrez_date":"2003-07-16","publication_year":"2003","canto_session_key":"77dd875a9dd1dce4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-05-05 16:07:24","canto_approved_date":"2020-04-02 11:48:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-05 16:07:17","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPCC1183.05c","SPAC644.14c","SPBC543.03c","SPCC126.02c","SPBC29A10.05","SPAC16A10.07c","SPBC29A3.14c","SPAC13C5.07"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-05-05"},{"uniquename":"PMID:38896689","title":"CDP-DAG synthesis by peripheral membrane-bound Tam41-type enzymes.","citation":"J Biochem 2024 Jun 19;","abstract":"Cytidine diphosphate diacylglycerol (CDP-DAG) is a critical intermediate that is converted to multiple phospholipids in prokaryotes and eukaryotes. In budding yeast, CDP-DAG synthesis from cytidine triphosphate (CTP) and phosphatidic acid (PA) is catalyzed by the membrane-integrated protein Cds1 in the endoplasmic reticulum and the peripheral membrane-bound protein Tam41 in mitochondria. Although a recent study revealed that the fission yeast SpTam41 consists of a nucleotidyltransferase domain and a winged helix domain, forming an active-site pocket for CTP binding between the two domains together with a C-terminal amphipathic helix for membrane association, how CTP and Mg2+, a most-favored divalent cation, are accommodated with PA remains obscure. A more recent report by Kimura et al. (J. Biochem. 2022; 171:429-441) solved the crystal structure of FbTam41, a functional ortholog from a Firmicutes bacterium, with CTP-Mg2+, successfully providing a detailed molecular view of CDP-DAG synthesis. In this commentary, our current understanding of Tam41-mediated reaction is discussed.","doi":"10.1093/jb/mvae046","authors":"Okamoto K","authors_abbrev":"Okamoto K","pubmed_publication_date":"19 Jun 2024","pubmed_entrez_date":"2024-06-19","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-06-19 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15905142","title":"The role of heterochromatin in centromere function.","citation":"Philos Trans R Soc Lond B Biol Sci 2005 Mar 29;360(1455):569-79","abstract":"Chromatin at centromeres is distinct from the chromatin in which the remainder of the genome is assembled. Two features consistently distinguish centromeres: the presence of the histone H3 variant CENP-A and, in most organisms, the presence of heterochromatin. In fission yeast, domains of silent \"heterochromatin\" flank the CENP-A chromatin domain that forms a platform upon which the kinetochore is assembled. Thus, fission yeast centromeres resemble their metazoan counterparts where the kinetochore is embedded in centromeric heterochromatin. The centromeric outer repeat chromatin is underacetylated on histones H3 and H4, and methylated on lysine 9 of histone H3, which provides a binding site for the chromodomain protein Swi6 (orthologue of Heterochromatin Protein 1, HP1). The remarkable demonstration that the assembly of repressive heterochromatin is dependent on the RNA interference machinery provokes many questions about the mechanisms of this process that may be tractable in fission yeast. Heterochromatin ensures that a high density of cohesin is recruited to centromeric regions, but it could have additional roles in centromere architecture and the prevention of merotely, and it might also act as a trigger for kinetochore assembly. In addition, we discuss an epigenetic model for ensuring that CENP-A is targeted and replenished at the kinetochore domain.","authors":"Pidoux AL, Allshire RC","authors_abbrev":"Pidoux AL et al.","pubmed_publication_date":"29 Mar 2005","pubmed_entrez_date":"2005-05-21","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31483748","title":"Effects of the microtubule nucleator Mto1 on chromosomal movement, DNA repair, and sister chromatid cohesion in fission yeast.","citation":"Mol Biol Cell 2019 Oct 01;30(21):2695-2708","abstract":"Although the function of microtubules (MTs) in chromosomal segregation during mitosis is well characterized, much less is known about the role of MTs in chromosomal functions during interphase. In the fission yeast  Schizosaccharomyces pombe , dynamic cytoplasmic MT bundles move chromosomes in an oscillatory manner during interphase via linkages through the nuclear envelope (NE) at the spindle pole body (SPB) and other sites. Mto1 is a cytoplasmic factor that mediates the nucleation and attachment of cytoplasmic MTs to the nucleus. Here, we test the function of these cytoplasmic MTs and Mto1 on DNA repair and recombination during interphase. We find that  mto1Δ  cells exhibit defects in DNA repair and homologous recombination (HR) and abnormal DNA repair factory dynamics. In these cells, sister chromatids are not properly paired, and binding of Rad21 cohesin subunit along chromosomal arms is reduced. Our findings suggest a model in which cytoplasmic MTs and Mto1 facilitate efficient DNA repair and HR by promoting dynamic chromosomal organization and cohesion in the nucleus.","doi":"10.1091/mbc.E19-05-0301","authors":"Zhurinsky J, Salas-Pino S, Iglesias-Romero AB, Torres-Mendez A, Knapp B, Flor-Parra I, Wang J, Bao K, Jia S, Chang F, Daga RR","authors_abbrev":"Zhurinsky J et al.","pubmed_publication_date":"01 Oct 2019","pubmed_entrez_date":"2019-09-05","publication_year":"2019","canto_session_key":"fdc8926d3d89d0b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silvia Salas Pino","canto_first_approved_date":"2019-12-17 19:54:35","canto_approved_date":"2021-11-09 20:14:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-02 17:34:36","canto_added_date":"2019-09-06 00:15:04","annotation_curators":[{"name":"Silvia Salas Pino","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPBC216.05","SPCC338.17c","SPBC902.06","SPCC18B5.11c","SPCC417.07c","SPAC18G6.10","SPAC17H9.20","SPAC3C7.12","SPBC2G2.14","SPCC1259.13"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2019-12-17"},{"uniquename":"PMID:37903220","title":"Quantifying turgor pressure in budding and fission yeasts based upon osmotic properties.","citation":"Mol Biol Cell 2023 Dec 01;34(13):ar133","abstract":"Walled cells, such as plants, fungi, and bacteria cells, possess a high internal hydrostatic pressure, termed turgor pressure, that drives volume growth and contributes to cell shape determination. Rigorous measurement of turgor pressure, however, remains challenging, and reliable quantitative measurements, even in budding yeast are still lacking. Here, we present a simple and robust experimental approach to access turgor pressure in yeasts based upon the determination of isotonic concentration using protoplasts as osmometers. We propose three methods to identify the isotonic condition - three-dimensional cell volume, cytoplasmic fluorophore intensity, and mobility of a cytGEMs nano-rheology probe - that all yield consistent values. Our results provide turgor pressure estimates of 1.0 ± 0.1 MPa for  Schizosaccharomyces pombe , 0.49 ± 0.01 MPa for  Schizosaccharomyces japonicus , 0.5 ± 0.1 MPa for  Saccharomyces cerevisiae   W303a  and 0.31 ± 0.03 MPa for  Saccharomyces cerevisiae BY4741 . Large differences in turgor pressure and nano-rheology measurements between the  Saccharomyces cerevisiae  strains demonstrate how fundamental biophysical parameters can vary even among wild-type strains of the same species. These side-by-side measurements of turgor pressure in multiple yeast species provide critical values for quantitative studies on cellular mechanics and comparative evolution.","doi":"10.1091/mbc.E23-06-0215","authors":"Lemière J, Chang F","authors_abbrev":"Lemière J et al.","pubmed_publication_date":"01 Dec 2023","pubmed_entrez_date":"2023-10-30","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-10-31 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10556596","title":"Mechanisms of genome maintenance and rearrangement: current research and recent advances in DNA repair and recombination.","citation":"Mutat Res 1999 Oct 22;435(2):163-9","abstract":"The topics of the talks at the annual DNA Repair Network Meeting at City University, London were as usual wide-ranging and provided an absorbing programme. Covered in the 17 talks were the autoproteolysis of O(6)-methylguanine DNA alkyltransferase in Escherichia coli; identification of new intermediates in meiotic recombination in Saccharomyces cerevisiae; the SMC (structural maintenance of chromosomes) family of proteins in Schizosaccharomyces pombe; transposition and V(D)J recombination; mammalian Rad51 foci formation in Rad54, Rad52, XRCC2 and XRCC3 mutants; biochemical analysis of DNA-PK, ATM (ataxia telangiectasia mutated) and ATR (AT related); other human DNA repair deficiencies and their incidence, including xeroderma pigmentosum and a new DNA ligase IV-deficient patient, and back, once again, to alkyltransferase, this time in humans and its manipulation for engineering drug resistance in bone marrow for cancer treatment.","authors":"Strike P, Jones NJ","authors_abbrev":"Strike P et al.","pubmed_publication_date":"22 Oct 1999","pubmed_entrez_date":"1999-11-11","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19461952","title":"Evolutionary conservation levels of subunits of histone-modifying protein complexes in fungi.","citation":"Comp Funct Genomics 2009;2009:379317","abstract":"Eukaryotes possess a variety of histone-modifying protein complexes. Generally, a histone-modifying protein complex consists of multiple subunits, that is, a catalytic subunit and the associated subunits. In this study, I analyzed 62 and 48 subunits of the histone-modifying protein complexes of Saccharomyces cerevisiae and Schizosaccharomyces pombe, respectively. The evolutionary conservation levels of the 110 subunits were measured. The measurements revealed that the conservation levels of the catalytic subunits are significantly higher than those of the associated subunits of the histone acetyltransferase and deacetylase complexes; however, the conservation level of the catalytic subunits is similar to that of the associated subunits of the histone methyltransferase complexes. Thus, in the fungal histone acetylation and deacetylation systems, the catalytic subunits of histone-modifying protein complexes are conserved and the associated subunits are evolutionary lineage-specific. In contrast, in the fungal histone methylation system, both the catalytic and the associated subunits are evolutionary lineage-specific.","doi":"10.1155/2009/379317","authors":"Nishida H","authors_abbrev":"Nishida H","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-05-23","publication_year":"2009","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11121785","title":"Cell cycle regulation in Schizosaccharomyces pombe.","citation":"Curr Opin Microbiol 2000 Dec;3(6):631-6","abstract":"Cdc2, a cyclin-dependent kinase, controls cell cycle progression in fission yeast. New details of Cdc2 regulation and function have been uncovered in recent studies. These studies involve cyclins that associate with Cdc2 in G1-phase and the proteins that regulate inhibitory phosphorylation of Cdc2 during S-phase and G2-phase. Recent investigations have also provided a better understanding of proteins that regulate DNA replication and that are directly or indirectly controlled by Cdc2.","authors":"Moser BA, Russell P","authors_abbrev":"Moser BA et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-12-21","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20403971","title":"Proteomic and functional analysis of the noncanonical poly(A) polymerase Cid14.","citation":"RNA 2010 Jun;16(6):1124-9","abstract":"The fission yeast Cid14 protein belongs to a family of noncanonical poly(A) polymerases which have been implicated in a broad range of biological functions. Here we describe an extensive Cid14 protein-protein interaction network and its biochemical dissection. Cid14 most stably interacts with the zinc-knuckle protein Air1 to form the Cid14-Air1 complex (CAC). Providing a link to ribosomal RNA processing, Cid14 sediments with 60S ribosomal subunits and copurifies with 60S assembly factors. In contrast, no physical link to chromatin has been identified, although gene expression profiling revealed that efficient silencing of a few heterochromatic genes depends on Cid14 and/or Air1.","doi":"10.1261/rna.2053710","authors":"Keller C, Woolcock K, Hess D, Bühler M","authors_abbrev":"Keller C et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-04-21","publication_year":"2010","canto_session_key":"58c42674621b27cb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2013-07-18 13:04:02","canto_approved_date":"2020-03-27 08:41:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-11 16:12:19","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC13B11.01","SPAC694.05c","SPBC18E5.04","SPAC13G6.02c","SPBC1815.01","SPAC8C9.08","SPAC6F6.03c","SPBC651.01c","SPBP8B7.20c","SPBC29A3.04","SPAC19B12.04","SPBC106.18","SPAC12G12.13c","SPBC29B5.03c","SPAC26A3.07c","SPBC365.03c","SPBC776.11","SPAC1805.11c","SPAC3A12.10","SPBC1711.06","SPBC18H10.12c","SPCC613.05c","SPAC17A5.03","SPAC23A1.08c","SPCC74.05","SPBC1105.12","SPBC14F5.04c","SPAC6F6.07c","SPBC2D10.10c","SPAC26A3.04","SPAC1071.07c","SPAPB17E12.05","SPAC31G5.03","SPAC890.08","SPBC19C2.07","SPCC576.08c","SPBC29A3.12","SPAC1834.03c","SPAC18G6.14c","SPAC1687.06c","SPCC1183.08c","SPBC685.07c","SPBC8D2.03c","SPAC3H5.05c","SPBC18H10.14","SPAC24H6.07","SPBC18H10.13","SPAC11E3.15","SPBC16D10.11c","SPAC22H12.04c","SPAC806.03c","SPAC1783.08c","SPBC11C11.07","SPBP35G2.08c","SPBC800.04c","SPAC9G1.03c","SPCC5E4.07","SPCC622.18","SPCC622.09","SPBP8B7.16c","SPCC794.09c","SPAC6F12.16c","SPAC23A1.11","SPBC16G5.14c","SPBC56F2.02","SPBC1D7.04","SPAC1805.13","SPBC17G9.10","SPCC18.14c","SPCC364.03","SPAC140.02","SPAC17G6.06","SPCC1322.11","SPAC22A12.04c","SPAC664.05","SPBC2F12.07c","SPAC3G9.03","SPBC16C6.11","SPAC144.11","SPAC2C4.16c","SPAC959.08","SPAC664.04c","SPAC5D6.01","SPAPB17E12.13","SPAPB1E7.12","SPBC839.04","SPBC839.05c","SPAC3H5.07","SPAC6G9.09c","SPCC1259.01c","SPCC576.11","SPCC970.05","SPBP8B7.03c","SPBC17G9.07","SPBC19G7.03c","SPBC32F12.11","SPAC1F7.13c"],"gene_count":97,"ltp_gene_count":97,"approved_date":"2013-07-18"},{"uniquename":"PMID:12446769","title":"The Ran GTPase system in fission yeast affects microtubules and cytokinesis in cells that are competent for nucleocytoplasmic protein transport.","citation":"Mol Cell Biol 2002 Dec;22(24):8491-505","abstract":"Misregulation of the evolutionarily conserved GTPase Ran in fission yeast results in defects in several cellular processes in cells that are competent for nucleocytoplasmic protein transport. These results suggest that transport is neither the only nor the primary Ran-dependent process in living cells. The ability of Ran to independently regulate multiple cellular processes in vivo is demonstrated by showing that (i) eight different transport-competent RanGEF (guanine nucleotide exchange factor) mutants have defects in mitotic spindle formation; (ii) the RanGEF temperature-sensitive mutant pim1-d1 has abnormal actin ring structures at the septum. Overexpression of Imp2p, which specifically destabilizes these structures, restores viability. (iii) Ran-dependent processes differ in their requirements for active Ran in vivo. Microtubule function, cytokinesis, and nuclear envelope structure are the Ran-dependent processes most sensitive to the amount of Ran protein in the cell, whereas nucleocytoplasmic protein transport is the most robust. Therefore, the ability of Ran from Schizosaccharomyces pombe to independently regulate multiple cellular processes may reflect differences in its interactions with the binding proteins that mediate these functions and explain the complex phenotypic consequences of its misregulation in vivo.","authors":"Salus SS, Demeter J, Sazer S","authors_abbrev":"Salus SS et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2002-11-26","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC106.01","SPAC27F1.02c","SPCC1739.11c","SPBC557.03c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:36074901","title":"ATP6V0C variants impair V-ATPase function causing a neurodevelopmental disorder often associated with epilepsy.","citation":"Brain 2023 Apr 19;146(4):1357-1372","abstract":"The vacuolar H+-ATPase is an enzymatic complex that functions in an ATP-dependent manner to pump protons across membranes and acidify organelles, thereby creating the proton/pH gradient required for membrane trafficking by several different types of transporters. We describe heterozygous point variants in ATP6V0C, encoding the c-subunit in the membrane bound integral domain of the vacuolar H+-ATPase, in 27 patients with neurodevelopmental abnormalities with or without epilepsy. Corpus callosum hypoplasia and cardiac abnormalities were also present in some patients. In silico modelling suggested that the patient variants interfere with the interactions between the ATP6V0C and ATP6V0A subunits during ATP hydrolysis. Consistent with decreased vacuolar H+-ATPase activity, functional analyses conducted in Saccharomyces cerevisiae revealed reduced LysoSensor fluorescence and reduced growth in media containing varying concentrations of CaCl2. Knockdown of ATP6V0C in Drosophila resulted in increased duration of seizure-like behaviour, and the expression of selected patient variants in Caenorhabditis elegans led to reduced growth, motor dysfunction and reduced lifespan. In summary, this study establishes ATP6V0C as an important disease gene, describes the clinical features of the associated neurodevelopmental disorder and provides insight into disease mechanisms.","doi":"10.1093/brain/awac330","authors":"Mattison KA, Tossing G, Mulroe F, Simmons C, Butler KM, Schreiber A, Alsadah A, Neilson DE, Naess K, Wedell A, Wredenberg A, Sorlin A, McCann E, Burghel GJ, Menendez B, Hoganson GE, Botto LD, Filloux FM, Aledo-Serrano Á, Gil-Nagel A, Tatton-Brown K, Verbeek NE, van der Zwaag B, Aleck KA, Fazenbaker AC, Balciuniene J, Dubbs HA, Marsh ED, Garber K, Ek J, Duno M, Hoei-Hansen CE, Deardorff MA, Raca G, Quindipan C, van Hirtum-Das M, Breckpot J, Hammer TB, Møller RS, Whitney A, Douglas AGL, Kharbanda M, Brunetti-Pierri N, Morleo M, Nigro V, May HJ, Tao JX, Argilli E, Sherr EH, Dobyns WB, Genomics England Research Consortium, Baines RA, Warwicker J, Parker JA, Banka S, Campeau PM, Escayg A","authors_abbrev":"Mattison KA et al.","pubmed_publication_date":"19 Apr 2023","pubmed_entrez_date":"2022-09-08","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC732.01","SPAC1B3.14"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:28366744","title":"Fission Yeast Apc15 Stabilizes MCC-Cdc20-APC/C Complexes, Ensuring Efficient Cdc20 Ubiquitination and Checkpoint Arrest.","citation":"Curr Biol 2017 Apr 24;27(8):1221-1228","abstract":"During mitosis, cells must segregate the replicated copies of their genome to their daughter cells with extremely high fidelity. Segregation errors lead to an abnormal chromosome number (aneuploidy), which typically results in disease or cell death [1]. Chromosome segregation and anaphase onset are initiated through the action of the multi-subunit E3 ubiquitin ligase known as the anaphase-promoting complex or cyclosome (APC/C [2]). The APC/C is inhibited by the spindle checkpoint in the presence of kinetochore attachment defects [3, 4]. Here we demonstrate that two non-essential APC/C subunits (Apc14 and Apc15) regulate association of spindle checkpoint proteins, in the form of the mitotic checkpoint complex (MCC), with the APC/C. apc14Δ mutants display increased MCC association with the APC/C and are unable to silence the checkpoint efficiently. Conversely, apc15Δ mutants display reduced association between the MCC and APC/C, are defective in poly-ubiquitination of Cdc20, and are checkpoint defective. In vitro reconstitution studies have shown that human MCC-APC/C can contain two molecules of Cdc20 [5-7]. Using a yeast strain expressing two Cdc20 genes with different epitope tags, we show by co-immunoprecipitation that this is true in vivo. MCC binding to the second molecule of Cdc20 is mediated via the C-terminal KEN box in Mad3. Somewhat surprisingly, complexes containing both molecules of Cdc20 accumulate in apc15Δ cells, and the implications of this observation are discussed.","doi":"10.1016/j.cub.2017.03.013","authors":"May KM, Paldi F, Hardwick KG","authors_abbrev":"May KM et al.","pubmed_publication_date":"24 Apr 2017","pubmed_entrez_date":"2017-04-04","publication_year":"2017","canto_session_key":"f21f4f173822b0e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Karen May","canto_first_approved_date":"2019-12-10 18:20:30","canto_approved_date":"2025-09-03 19:44:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-23 16:51:28","canto_added_date":"2017-04-05 00:15:12","annotation_curators":[{"name":"Karen May","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.01","SPCC320.13c","SPAC27D7.05c","SPBC20F10.06","SPAC19G12.01c","SPBC26H8.07c","SPAC6F12.15c","SPBC582.03","SPBC106.09","SPCC1795.01c","SPAC821.08c","SPBC83.04","SPBC25H2.13c","SPBC16G5.01"],"gene_count":14,"ltp_gene_count":12,"approved_date":"2019-12-10"},{"uniquename":"PMID:9808627","title":"Faithful anaphase is ensured by Mis4, a sister chromatid cohesion molecule required in S phase and not destroyed in G1 phase.","citation":"Genes Dev 1998 Nov 01;12(21):3408-18","abstract":"The loss of sister chromatid cohesion triggers anaphase spindle movement. The budding yeast Mcd1/Scc1 protein, called cohesin, is required for associating chromatids, and proteins homologous to it exist in a variety of eukaryotes. Mcd1/Scc1 is removed from chromosomes in anaphase and degrades in G1. We show that the fission yeast protein, Mis4, which is required for equal sister chromatid separation in anaphase is a different chromatid cohesion molecule that behaves independent of cohesin and is conserved from yeast to human. Its inactivation in G1 results in cell lethality in S phase and subsequent premature sister chromatid separation. Inactivation in G2 leads to cell death in subsequent metaphase-anaphase progression but missegregation occurs only in the next round of mitosis. Mis4 is not essential for condensation, nor does it degrade in G1. Rather, it associates with chromosomes in a punctate fashion throughout the cell cycle. mis4 mutants are hypersensitive to hydroxyurea (HU) and UV irradiation but retain the ability to restrain cell cycle progression when damaged or sustaining a block to replication. The mis4 mutation results in synthetic lethality with a DNA ligase mutant. Mis4 may form a stable link between chromatids in S phase that is split rather than removed in anaphase.","authors":"Furuya K, Takahashi K, Yanagida M","authors_abbrev":"Furuya K et al.","pubmed_publication_date":"01 Nov 1998","pubmed_entrez_date":"1998-11-10","publication_year":"1998","canto_session_key":"a935efede4be6aa8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-05-10 16:01:43","canto_approved_date":"2019-07-30 15:25:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-01 17:36:46","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPAC20G8.01","SPAC6F12.15c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-05-10"},{"uniquename":"PMID:18794845","title":"Mal3, the Schizosaccharomyces pombe homolog of EB1, changes the microtubule lattice.","citation":"Nat Struct Mol Biol 2008 Oct;15(10):1102-8","abstract":"In vitro studies of pure tubulin have suggested that tubulin heterodimers in cells assemble into B-lattice microtubules, where the 8-nm dimers in adjacent protofilaments are staggered by 0.9 nm. This arrangement requires the tube to close by forming a seam with an A-lattice, in which the protofilaments are staggered by 4.9 nm. Here we show that Mal3, an EB1 family tip-tracking protein, drives tubulin to assemble in vitro into exclusively 13-protofilament microtubules with a high proportion of A-lattice protofilament contacts. We present a three-dimensional cryo-EM reconstruction of a purely A-lattice microtubule decorated with Mal3, in which Mal3 occupies the groove between protofilaments and associates closely with one tubulin monomer. We propose that Mal3 promotes assembly by binding to freshly formed tubulin polymer and particularly favors any with A-lattice arrangement. These results reopen the question of microtubule structure in cells.","doi":"10.1038/nsmb.1482","authors":"des Georges A, Katsuki M, Drummond DR, Osei M, Cross RA, Amos LA","authors_abbrev":"des Georges A et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-09-17","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPBC16A3.15c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7559789","title":"Degradation of HMG-CoA reductase-induced membranes in the fission yeast, Schizosaccharomyces pombe.","citation":"J Cell Biol 1995 Oct;131(1):81-94","abstract":"Elevated levels of certain membrane proteins, including the sterol biosynthetic enzyme HMG-CoA reductase, induce proliferation of the endoplasmic reticulum. When the amounts of these proteins return to basal levels, the proliferated membranes are degraded, but the molecular details of this degradation remain unknown. We have examined the degradation of HMG-CoA reductase-induced membranes in the fission yeast, Schizosaccharomyces pombe. In this yeast, increased levels of the Saccharomyces cerevisiae HMG-CoA reductase isozyme encoded by HMG1 induced several types of membranes, including karmellae, which formed a cap of stacked membranes that partially surrounded the nucleus. When expression of HMG1 was repressed, the karmellae detached from the nucleus and formed concentric, multilayered membrane whorls that were then degraded. During the degradation process, CDCFDA-stained compartments distinct from preexisting vacuoles formed within the interior of the whorls. In addition to these compartments, particles that contained neutral lipids also formed within the whorl. As the thickness of the whorl decreased, the lipid particle became larger. When degradation was complete, only the lipid particle remained. Cycloheximide treatment did not prevent the formation of whorls. Thus, new protein synthesis was not needed for the initial stages of karmellae degradation. On the contrary, cycloheximide promoted the detachment of karmellae to form whorls, suggesting that a short lived protein may be involved in maintaining karmellae integrity. Taken together, these results demonstrate that karmellae membranes differentiated into self-degradative organelles. This process may be a common pathway by which ER membranes are turned over in cells.","authors":"Lum PY, Wright R","authors_abbrev":"Lum PY et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25533340","title":"Cdk1 restrains NHEJ through phosphorylation of XRCC4-like factor Xlf1.","citation":"Cell Rep 2014 Dec 24;9(6):2011-7","abstract":"Eukaryotic cells use two principal mechanisms for repairing DNA double-strand breaks (DSBs): homologous recombination (HR) and nonhomologous end-joining (NHEJ). DSB repair pathway choice is strongly regulated during the cell cycle. Cyclin-dependent kinase 1 (Cdk1) activates HR by phosphorylation of key recombination factors. However, a mechanism for regulating the NHEJ pathway has not been established. Here, we report that Xlf1, a fission yeast XLF ortholog, is a key regulator of NHEJ activity in the cell cycle. We show that Cdk1 phosphorylates residues in the C terminus of Xlf1 over the course of the cell cycle. Mutation of these residues leads to the loss of Cdk1 phosphorylation, resulting in elevated levels of NHEJ repair in vivo. Together, these data establish that Xlf1 phosphorylation by Cdc2(Cdk1) provides a molecular mechanism for downregulation of NHEJ in fission yeast and indicates that XLF is a key regulator of end-joining processes in eukaryotic organisms.","doi":"10.1016/j.celrep.2014.11.044","authors":"Hentges P, Waller H, Reis CC, Ferreira MG, Doherty AJ","authors_abbrev":"Hentges P et al.","pubmed_publication_date":"24 Dec 2014","pubmed_entrez_date":"2014-12-24","publication_year":"2014","canto_session_key":"c23b5043b024b0a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pierre Hentges","canto_first_approved_date":"2017-02-24 15:45:24","canto_approved_date":"2026-06-26 11:08:41","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-07-28 12:05:49","canto_added_date":"2014-12-25 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pierre Hentges","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC16A10.07c","YLR265C","SPCC1183.05c","SPCC338.08","HGNC:25737","SPCC24B10.14c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-02-24"},{"uniquename":"PMID:12006645","title":"SpSld3 is required for loading and maintenance of SpCdc45 on chromatin in DNA replication in fission yeast.","citation":"Mol Biol Cell 2002 May;13(5):1462-72","abstract":"Initiation of DNA replication in eukaryotic cells is regulated through the ordered assembly of replication complexes at origins of replication. Association of Cdc45 with the origins is a crucial step in assembly of the replication machinery, hence can be considered a target for the regulation of origin activation. To examine the process required for SpCdc45 loading, we isolated fission yeast SpSld3, a counterpart of budding yeast Sld3 that interacts with Cdc45. SpSld3 associates with the replication origin during G1-S phases and this association depends on Dbf4-dependent (DDK) kinase activity. In the corresponding period, SpSld3 interacts with minichromosome maintenance (MCM) proteins and then with SpCdc45. A temperature-sensitive sld3-10 mutation suppressed by the multicopy of the sna41+ encoding SpCdc45 impairs loading of SpCdc45 onto chromatin. In addition, this mutation leads to dissociation of preloaded Cdc45 from chromatin in the hydroxyurea-arrested S phase, and DNA replication upon removal of hydroxyurea is retarded. Thus, we conclude that SpSld3 is required for stable association of Cdc45 with chromatin both in initiation and elongation of DNA replication. The DDK-dependent origin association suggests that SpSld3 is involved in temporal regulation of origin firing.","authors":"Nakajima R, Masukata H","authors_abbrev":"Nakajima R et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-05-15","publication_year":"2002","canto_session_key":"a0db0af7ec94b4a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-08-09 16:26:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-07-01 15:44:50","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":33,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.06","SPAC17D4.02","SPBC25D12.03c","SPBC211.04c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-07-01"},{"uniquename":"PMID:18265320","title":"Growth and manipulation of S. pombe.","citation":"Curr Protoc Mol Biol 2003 Nov;Chapter 13:Unit 13.16","abstract":"This unit presents aspects specific to genetic and cytological manipulation of fission yeast, including mating type testing, crosses, preparingmaking diploids, and analysis of meiotic products, and basic methods of cell cycle synchronization and analysis. These methods are different from those used in budding yeast because they depend upon the distinct biology of S. pombe, particularly its unwillingness to be a diploid in normal growth conditions. Similarly, the different cell shape and growth behavior of S. pombe require different approaches to basic cell cycle analysis.","doi":"10.1002/0471142727.mb1316s64","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2008-02-12","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16585273","title":"Mcp5, a meiotic cell cortex protein, is required for nuclear movement mediated by dynein and microtubules in fission yeast.","citation":"J Cell Biol 2006 Apr 10;173(1):27-33","abstract":"During meiotic prophase I of the fission yeast Schizosaccharomyces pombe, oscillatory nuclear movement occurs. This promotes homologous chromosome pairing and recombination and involves cortical dynein, which plays a pivotal role by generating a pulling force with the help of an unknown dynein anchor. We show that Mcp5, the homologue of the budding yeast dynein anchor Num1, may be this putative dynein anchor. mcp5+ is predominantly expressed during meiotic prophase, and GFP-Mcp5 localizes at the cell cortex. Moreover, the mcp5Delta strain lacks the oscillatory nuclear movement. Accordingly, homologous pairing and recombination rates of the mcp5Delta strain are significantly reduced. Furthermore, the cortical localization of dynein heavy chain 1 appears to be reduced in mcp5Delta cells. Finally, the full function of Mcp5 requires its coiled-coil and pleckstrin homology (PH) domains. Our results suggest that Mcp5 localizes at the cell cortex through its PH domain and functions as a dynein anchor, thereby facilitating nuclear oscillation.","authors":"Saito TT, Okuzaki D, Nojima H","authors_abbrev":"Saito TT et al.","pubmed_publication_date":"10 Apr 2006","pubmed_entrez_date":"2006-04-06","publication_year":"2006","canto_session_key":"9c368b73d2d16728","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-23 10:40:55","canto_approved_date":"2022-07-27 12:36:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-19 14:21:48","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPBC216.02"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-11-23"},{"uniquename":"PMID:1533643","title":"In vitro microtubule-nucleating activity of spindle pole bodies in fission yeast Schizosaccharomyces pombe: cell cycle-dependent activation in xenopus cell-free extracts.","citation":"J Cell Biol 1992 Jun;117(5):1055-66","abstract":"The spindle pole body (SPB) is the equivalent of the centrosome in fission yeast. In vivo it nucleates microtubules (MTs) during mitosis, but, unlike animal centrosomes, does not act as a microtubule organizing center (MTOC) during interphase. We have studied the MT-nucleating activity of SPBs in vitro and have found that SPBs in permeabilized cells retain in vivo characteristics. SPBs in cells permeabilized during mitosis can nucleate MTs, and are recognized by two antibodies: anti-gamma-tubulin and MPM-2 which recognizes phosphoepitopes. SPBs in cells permeabilized during interphase cannot nucleate MTs and are only recognized by anti-gamma-tubulin. Interphase SPBs which cannot nucleate can be converted to a nucleation competent state by incubation in cytostatic factor (CSF)-arrested Xenopus egg extracts. After incubation, they are recognized by MPM-2, and can nucleate MTs. The conversion does not occur in Xenopus interphase extract, but occurs in Xenopus interphase extract driven into mitosis by preincubation with exogenous cyclin B. The conversion is ATP dependent and inhibited by protein kinase inhibitors and alkaline phosphatase. Purified, active, cdc2 kinase/cyclin B complex in itself is not effective for activation of MT nucleation, although some interphase SPBs are now stained with MPM-2. These results suggest that the ability of SPBs in vitro to nucleate MTs after exposure to CSF-arrested extracts is activated through a downstream pathway which is regulated by cdc2 kinase.","authors":"Masuda H, Sevik M, Cande WZ","authors_abbrev":"Masuda H et al.","pubmed_publication_date":"Jun 1992","pubmed_entrez_date":"1992-06-01","publication_year":"1992","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12428377","title":"[Analysis of the general transcription factor TFIID using the fission yeast Schizosaccharomyces pombe].","citation":"Tanpakushitsu Kakusan Koso 2002 Nov;47(14):1931-8","abstract":"","authors":"Mitsuzawa H","authors_abbrev":"Mitsuzawa H","pubmed_publication_date":"Nov 2002","pubmed_entrez_date":"2002-11-14","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013691","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20587776","title":"Mathematical modeling of endocytic actin patch kinetics in fission yeast: disassembly requires release of actin filament fragments.","citation":"Mol Biol Cell 2010 Aug 15;21(16):2905-15","abstract":"We used the dendritic nucleation hypothesis to formulate a mathematical model of the assembly and disassembly of actin filaments at sites of clathrin-mediated endocytosis in fission yeast. We used the wave of active WASp recruitment at the site of the patch formation to drive assembly reactions after activation of Arp2/3 complex. Capping terminated actin filament elongation. Aging of the filaments by ATP hydrolysis and gamma-phosphate dissociation allowed actin filament severing by cofilin. The model could simulate the assembly and disassembly of actin and other actin patch proteins using measured cytoplasmic concentrations of the proteins. However, to account quantitatively for the numbers of proteins measured over time in the accompanying article (Sirotkin et al., 2010, MBoC 21: 2792-2802), two reactions must be faster in cells than in vitro. Conditions inside the cell allow capping protein to bind to the barbed ends of actin filaments and Arp2/3 complex to bind to the sides of filaments faster than the purified proteins in vitro. Simulations also show that depolymerization from pointed ends cannot account for rapid loss of actin filaments from patches in 10 s. An alternative mechanism consistent with the data is that severing produces short fragments that diffuse away from the patch.","doi":"10.1091/mbc.E10-06-0494","authors":"Berro J, Sirotkin V, Pollard TD","authors_abbrev":"Berro J et al.","pubmed_publication_date":"15 Aug 2010","pubmed_entrez_date":"2010-07-01","publication_year":"2010","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15317867","title":"A novel type of silencing factor, Clr2, is necessary for transcriptional silencing at various chromosomal locations in the fission yeast Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2004;32(15):4421-8","abstract":"The mating-type region of the fission yeast Schizosaccharomyces pombe comprises three loci: mat1, mat2-P and mat3-M. mat1 is expressed and determines the mating type of the cell. mat2-P and mat3-M are two storage cassettes located in a 17 kb heterochromatic region with features identical to those of mammalian heterochromatin. Mutations in the swi6+, clr1+, clr2+, clr3+, clr4+ and clr6+ genes were obtained in screens for factors necessary for silencing the mat2-P-mat3-M region. swi6+ encodes a chromodomain protein, clr3+ and clr6+ histone deacetylases, and clr4+ a histone methyltransferase. Here, we describe the cloning and characterization of clr2+. The clr2+ gene encodes a 62 kDa protein with no obvious sequence homologs. Deletion of clr2+ not only affects transcriptional repression in the mating-type region, but also centromeric silencing and silencing of a PolII-transcribed gene inserted in the rDNA repeats. Using chromatin immunoprecipitation, we show that Clr2 is necessary for histone hypoacetylation in the mating-type region, suggesting that Clr2 acts upstream of histone deacetylases to promote transcriptional silencing.","authors":"Bjerling P, Ekwall K, Egel R, Thon G","authors_abbrev":"Bjerling P et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-08-20","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35274981","title":"Laser ablation reveals the impact of Cdc15p on the stiffness of the contractile ring.","citation":"Mol Biol Cell 2022 May 15;33(6):br9","abstract":"The mechanics that govern the constriction of the contractile ring remain poorly understood yet are critical to understanding the forces that drive cytokinesis. We used laser ablation in fission yeast cells to unravel these mechanics focusing on the role of Cdc15p as a putative anchoring protein. Our work shows that the severed constricting contractile ring recoils to a finite point leaving a gap that can heal if less than ∼1 µm. Severed contractile rings in Cdc15p-depleted cells exhibit an exaggerated recoil, which suggests that the recoil is limited by the anchoring of the ring to the plasma membrane. Based on a physical model of the severed contractile ring, we propose that Cdc15p impacts the stiffness of the contractile ring more than the viscous drag.","doi":"10.1091/mbc.E21-10-0515","authors":"Moshtohry M, Bellingham-Johnstun K, Elting MW, Laplante C","authors_abbrev":"Moshtohry M et al.","pubmed_publication_date":"15 May 2022","pubmed_entrez_date":"2022-03-11","publication_year":"2022","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2022-03-13 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19139265","title":"The SH3 domains of two PCH family members cooperate in assembly of the Schizosaccharomyces pombe contractile ring.","citation":"J Cell Biol 2009 Jan 12;184(1):113-27","abstract":"Schizosaccharomyces pombe cdc15 homology (PCH) family members participate in many cellular processes by bridging the plasma membrane and cytoskeleton. Their F-BAR domains bind and curve membranes, whereas other domains, typically SH3 domains, are expected to provide cytoskeletal links. We tested this prevailing model of functional division in the founding member of the family, Cdc15, which is essential for cytokinesis in S. pombe, and in the related PCH protein, Imp2. We find that the distinct functions of Imp2 and Cdc15 are SH3 domain independent. However, the Cdc15 and Imp2 SH3 domains share an essential role in recruiting proteins to the contractile ring, including Pxl1 and Fic1. Together, Pxl1 and Fic1, a previously uncharacterized C2 domain protein, add structural integrity to the contractile ring and prevent it from fragmenting during division. Our data indicate that the F-BAR proteins Cdc15 and Imp2 contribute to a single biological process with both distinct and overlapping functions.","doi":"10.1083/jcb.200806044","authors":"Roberts-Galbraith RH, Chen JS, Wang J, Gould KL","authors_abbrev":"Roberts-Galbraith RH et al.","pubmed_publication_date":"12 Jan 2009","pubmed_entrez_date":"2009-01-14","publication_year":"2009","canto_session_key":"83c8a0868d64f0a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2018-02-28 15:52:09","canto_approved_date":"2023-06-23 15:16:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-28 15:51:47","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC11C11.02","SPAC26H5.10c","SPBC9B6.04c","SPCC4B3.15","SPAC6B12.12","SPCC1223.08c","SPBC4F6.12","SPAC1420.02c","SPAC20G8.05c","SPAC4A8.15c","SPAC1F7.05","SPBC19C2.07","SPBC1773.10c","SPBC244.01c","SPBC31F10.06c","SPAC24B11.11c","SPBC6B1.08c","SPAC1782.09c","SPAC1420.03","SPAC2F3.09","SPAC926.03","SPBC106.06","SPBC1347.02","SPAC9G1.03c","SPBP4H10.04","SPAP8A3.08","SPCC645.05c","SPAC1F5.04c","SPBC83.18c","SPAC4A8.05c","SPBC337.08c","SPAC15A10.08","SPAC26A3.05","SPCC794.12c","SPBC56F2.09c","SPBC646.09c","SPAC4F8.13c"],"gene_count":37,"ltp_gene_count":37,"approved_date":"2018-02-28"},{"uniquename":"PMID:16101442","title":"Targeting chk2 kinase: molecular interaction maps and therapeutic rationale.","citation":"Curr Pharm Des 2005;11(22):2855-72","abstract":"Most anticancer drugs presently used clinically target genomic DNA. The selectivity of these anticancer drugs for tumor tissues is probably due to tumor-specific defects suppressing cell cycle checkpoints and DNA repair, and enhancing apoptotic response in the tumor. We will review the molecular interactions within the ATM-Chk2 pathway implicating the DNA damage sensor kinases (ATM, ATR and DNA-PK), the adaptor BRCT proteins (Nbs1, Brca1, 53BP1, MDC1) and the effector kinases (Chk2, Chk1, Plk3, JNK, p38). The molecular interaction map convention (MIM) will be used for presenting this molecular network (http://discover.nci.nih.gov/mim/). A characteristic of the ATM-Chk2 pathway is its redundancy. First, ATM and Chk2 phosphorylate common substrates including p53, E2F1, BRCA1, and Chk2 itself, which suggests that Chk2 (also known as CHECK2, Cds1 in fission yeast, and Dmchk2 or Dmnk or Loki in the fruit fly) acts as a relay for ATM and/or as a salvage pathway when ATM is inactivated. Secondly, redundancy is apparent for the substrates, which can be phosphorylated/activated at similar residues by Chk2, Chk1, and the polo kinases (Plk's). Functionally, Chk2 can activate both apoptosis (via p53, E2F1 and PML) and cell cycle checkpoint (via Cdc25A and Cdc25C, p53, and BRCA1). We will review the short list of published Chk2 inhibitors. We will also propose a novel paradigm for screening interfacial inhibitors of Chk2. Chk2 inhibitors might be used to enhance the tumor selectivity of DNA targeted agents in p53-deficient tumors, and for the treatment of tumors whose growth depends on enhanced Chk2 activity.","authors":"Pommier Y, Sordet O, Rao VA, Zhang H, Kohn KW","authors_abbrev":"Pommier Y et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-08-17","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24403053","title":"Human COX20 cooperates with SCO1 and SCO2 to mature COX2 and promote the assembly of cytochrome c oxidase.","citation":"Hum Mol Genet 2014 Jun 01;23(11):2901-13","abstract":"Cytochrome c oxidase (CIV) deficiency is one of the most common respiratory chain defects in patients presenting with mitochondrial encephalocardiomyopathies. CIV biogenesis is complicated by the dual genetic origin of its structural subunits, and assembly of a functional holoenzyme complex requires a large number of nucleus-encoded assembly factors. In general, the functions of these assembly factors remain poorly understood, and mechanistic investigations of human CIV biogenesis have been limited by the availability of model cell lines. Here, we have used small interference RNA and transcription activator-like effector nucleases (TALENs) technology to create knockdown and knockout human cell lines, respectively, to study the function of the CIV assembly factor COX20 (FAM36A). These cell lines exhibit a severe, isolated CIV deficiency due to instability of COX2, a mitochondrion-encoded CIV subunit. Mitochondria lacking COX20 accumulate CIV subassemblies containing COX1 and COX4, similar to those detected in fibroblasts from patients carrying mutations in the COX2 copper chaperones SCO1 and SCO2. These results imply that in the absence of COX20, COX2 is inefficiently incorporated into early CIV subassemblies. Immunoprecipitation assays using a stable COX20 knockout cell line expressing functional COX20-FLAG allowed us to identify an interaction between COX20 and newly synthesized COX2. Additionally, we show that SCO1 and SCO2 act on COX20-bound COX2. We propose that COX20 acts as a chaperone in the early steps of COX2 maturation, stabilizing the newly synthesized protein and presenting COX2 to its metallochaperone module, which in turn facilitates the incorporation of mature COX2 into the CIV assembly line.","doi":"10.1093/hmg/ddu003","authors":"Bourens M, Boulet A, Leary SC, Barrientos A","authors_abbrev":"Bourens M et al.","pubmed_publication_date":"01 Jun 2014","pubmed_entrez_date":"2014-01-10","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC25H2.18","SPMIT.11"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:33856529","title":"Dynamical analysis of the fission yeast cell cycle via Markov chain.","citation":"Curr Genet 2021 Oct;67(5):785-797","abstract":"The cell cycle is a complex network involved in the regulation of cell growth and proliferation. Intrinsic molecular noise in gene expression in the cell cycle network can generate fluctuations in protein concentration. How the cell cycle network maintains its robust transitions between cell cycle phases in the presence of these fluctuations remains unclear. To understand the complex and robust behavior of the cell cycle system in the presence of intrinsic noise, we developed a Markov model for the fission yeast cell cycle system. We quantified the effect of noise on gene and protein activity and on the probability of transition between different phases of the cell cycle. Our analysis shows how network perturbations decide the fate of the cell. Our model predicts that the cell cycle pathway (subsequent transitions from [Formula: see text]) is the most robust and probable pathway among all possible trajectories in the cell cycle network. We performed a sensitivity analysis to find correlations between protein interaction weights and transition probabilities between cell cycle phases. The sensitivity analysis predicts how network perturbations affect the transition probability between different cell cycle phases and, consequently, affect different cell fates, thus, forming testable in vitro/in vivo hypotheses. Our simulation results agree with published experimental findings and reveal how noise in the cell cycle regulatory network can affect cell cycle progression.","doi":"10.1007/s00294-020-01146-z","authors":"Shafiekhani S, Kraikivski P, Gheibi N, Ahmadian M, Jafari AH","authors_abbrev":"Shafiekhani S et al.","pubmed_publication_date":"Oct 2021","pubmed_entrez_date":"2021-04-15","publication_year":"2021","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2021-04-19 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27806301","title":"Meiotic Nuclear Oscillations Are Necessary to Avoid Excessive Chromosome Associations.","citation":"Cell Rep 2016 Nov 01;17(6):1632-1645","abstract":"Pairing of homologous chromosomes is a crucial step in meiosis, which in fission yeast depends on nuclear oscillations. However, how nuclear oscillations help pairing is unknown. Here, we show that homologous loci typically pair when the spindle pole body is at the cell pole and the nucleus is elongated, whereas they unpair when the spindle pole body is in the cell center and the nucleus is round. Inhibition of oscillations demonstrated that movement is required for initial pairing and that prolonged association of loci leads to mis-segregation. The double-strand break marker Rec25 accumulates in elongated nuclei, indicating that prolonged chromosome stretching triggers recombinatory pathways leading to mis-segregation. Mis-segregation is rescued by overexpression of the Holliday junction resolvase Mus81, suggesting that prolonged pairing results in irresolvable recombination intermediates. We conclude that nuclear oscillations exhibit a dual role, promoting initial pairing and restricting the time of chromosome associations to ensure proper segregation.","doi":"10.1016/j.celrep.2016.10.014","authors":"Chacón MR, Delivani P, Tolić IM","authors_abbrev":"Chacón MR et al.","pubmed_publication_date":"01 Nov 2016","pubmed_entrez_date":"2016-11-03","publication_year":"2016","canto_session_key":"083563072b9df80a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-11-04 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.18c","SPCC4G3.05c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8005432","title":"Transient, meiosis-induced expression of the rec6 and rec12 genes of Schizosaccharomyces pombe.","citation":"Genetics 1994 Mar;136(3):769-79","abstract":"Two meiotic recombination genes, rec6 and rec12, from Schizosaccharomyces pombe have been cloned by genetic complementation and their DNA sequences determined. Gene replacements demonstrated that the cloned fragments contained the rec6 and rec12 genes. Further analysis showed that the functional rec6 gene was within a 1.3-kb fragment and rec12 within a 1.7-kb fragment. The nucleotide sequences of these fragments revealed open reading frames (ORFs) predicting 143 amino acids for the rec6 gene product and 139 amino acids for the rec12 gene product. After pat1-114 temperature-induced meiosis, the transcripts of rec6 and rec12 were induced to maximal levels at 2-3 hr, at about the time of premeiotic DNA synthesis, but were present at much lower levels before and after this time. The transient induction of the transcripts and the phenotypes of the mutants suggest that the rec6 and rec12 gene products are involved primarily in the early steps of meiotic recombination in S. pombe. Near the rec6 gene are two additional ORFs potentially encoding proteins with homology to ribosomal protein S7 of Saccharomyces cerevisiae (ORF137) and to the homeodomain of developmental regulatory proteins (ORF201). The roles of these S. pombe ORFs remain to be determined.","authors":"Lin Y, Smith GR","authors_abbrev":"Lin Y et al.","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_session_key":"d0d13d53c87497c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-05 09:18:13","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-05 09:17:58","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPBC21B10.12","SPCC1322.13"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2014-08-05"},{"uniquename":"PMID:8146661","title":"Telomere-led premeiotic chromosome movement in fission yeast.","citation":"Science 1994 Apr 08;264(5156):270-3","abstract":"The movement of chromosomes that precedes meiosis was observed in living cells of fission yeast by fluorescence microscopy. Further analysis by in situ hybridization revealed that the telomeres remain clustered at the leading end of premeiotic chromosome movement, unlike mitotic chromosome movement in which the centromere leads. Once meiotic chromosome segregation starts, however, centromeres resume the leading position in chromosome movement, as they do in mitosis. Although the movement of the telomere first has not been observed before, the clustering of telomeres is reminiscent of the bouquet structure of meiotic-prophase chromosomes observed in higher eukaryotes, which suggests that telomeres perform specific functions required for premeiotic chromosomal events generally in eukaryotes.","authors":"Chikashige Y, Ding DQ, Funabiki H, Haraguchi T, Mashiko S, Yanagida M, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"08 Apr 1994","pubmed_entrez_date":"1994-04-08","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2192258","title":"Differential distribution of factors involved in pre-mRNA processing in the yeast cell nucleus.","citation":"Mol Cell Biol 1990 Jul;10(7):3524-34","abstract":"The yeast cell nucleus has previously been shown to be divided into two regions by a variety of microscopic approaches. We used antibodies specific for the 2,2,7-trimethylguanosine cap structure of small nuclear ribonucleic acids (snRNAs) and for a protein component of small nuclear ribonucleoprotein particles to identify the distribution of small nuclear ribonucleoprotein particles within the yeast cell nucleus. These studies were performed with the fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae. By using immunofluorescence microscopy and immunoelectron microscopy, most of the abundant snRNAs were localized to the portion of the nucleus which has heretofore been referred to as the nucleolus. This distribution of snRNAs is different from that found in mammalian cells and suggests that the nucleolar portion of the yeast nucleus contains functional domains in addition to those associated with RNA polymerase I activity.","authors":"Potashkin JA, Derby RJ, Spector DL","authors_abbrev":"Potashkin JA et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_session_key":"299d5b04b7d7e42e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-06-20 12:59:51","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-20 12:59:04","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.02","SPSNRNA.03","SPSNRNA.04","SPSNRNA.06","SPSNRNA.07","SPSNRNA.01","SPSNRNA.05"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2014-06-20"},{"uniquename":"PMID:3481026","title":"Strains of Schizosaccharomyces pombe with a disrupted swi1 gene still show some mating-type switching.","citation":"Mol Gen Genet 1987 Dec;210(3):485-9","abstract":"The swi1+ gene is necessary for effective mating-type (MT) switching in Schizosaccharomyces pombe. It was cloned on a 4.2 kb genomic DNA fragment. By site-directed integration into the genome and gene disruption experiments it was proved that the swi1+ gene itself and not a suppressor had been isolated. Disruption of the swi1+ gene causes a phenotype identical to that of the original swi1 mutant, i.e. the strain still shows some MT switching. The swi1 gene is unique in the genome and gives rise to a 3 kb mRNA.","authors":"Schmidt H","authors_abbrev":"Schmidt H","pubmed_publication_date":"Dec 1987","pubmed_entrez_date":"1987-12-01","publication_year":"1987","canto_session_key":"05f7d09930433392","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-10-26 13:14:50","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-09-24 15:44:40","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-24"},{"uniquename":"PMID:22226725","title":"Production and NMR analysis of the human ibuprofen metabolite 3-hydroxyibuprofen.","citation":"J Biotechnol 2012 Feb 10;157(3):417-20","abstract":"The anti-inflammatory drug ibuprofen (Ibu) is metabolized in the human liver to a number of metabolites including 1-hydroxyibuprofen (1-OH-Ibu), 2-OH-Ibu, and 3-OH-Ibu, respectively. The only human CYP known to produce relevant amounts of 3-OH-Ibu is CYP2C9 and as genetic polymorphisms of CYP2C9 influence the metabolization of numerous drugs, the availability of reference standards for CYP2C9-specific metabolites is of considerable interest. The aim of this study was to develop a biological production process for 3-OH-Ibu and to affirm its NMR characteristics. The recombinant fission yeast strain CAD68 coexpressing human CYP2C9 and CPR was used for the whole-cell biotransformation of Ibu to 3-OH-Ibu in 1L batch-scale for 75h. The average space-time yield for the bioproduction of 3-OH-Ibu (125±34μmol/Ld) considerably exceeded that of 2-OH-Ibu (44±10μmol/Ld). Accordingly, average biotransformation activities normalized to dry biomass weight were 5.0±0.8μmol/gd (3-OH-Ibu) and 1.9±0.7μmol/gd (2-OH-Ibu). The metabolite was prepurified on preparative TLC-plates, isolated by HPLC fractionation, and characterized by LC-MS and NMR. As expected, differential fragmentation patterns of 2-OH-Ibu and 3-OH-Ibu were detected in ESI-LC-MS analysis. 44mg of 3-OH-Ibu was efficiently purified from four 1L batch cultures and its structure was clearly confirmed by one- and two-dimensional NMR.","doi":"10.1016/j.jbiotec.2011.12.016","authors":"Neunzig I, Göhring A, Drăgan CA, Zapp J, Peters FT, Maurer HH, Bureik M","authors_abbrev":"Neunzig I et al.","pubmed_publication_date":"10 Feb 2012","pubmed_entrez_date":"2012-01-10","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17473896","title":"Stress-dependent regulation of Pbh1, a BIR domain-containing protein, in the fission yeast.","citation":"Can J Microbiol 2006 Dec;52(12):1261-5","abstract":"To elicit the physiological roles of Pbh1, a baculoviral IAP repeat (BIR) domain-containing protein, in Schizosaccharomyces pombe, we investigated if Pbh1 expression is regulated by stress. The upstream region (1221 bp) of the pbh1 gene was fused into the promoterless beta-galactosidase gene of the shuttle vector YEp367R, and the resultant fusion plasmid was named pPbh04. The synthesis of beta-galactosidase from the pbh1-lacZ fusion gene was markedly enhanced by sodium nitroprusside (SNP) generating nitric oxide. The basal expression of the pbh1 gene required the presence of Pap1. Pap1 also mediated the induction of the pbh1 gene by SNP and nitrogen starvation. Pap1-dependent induction of the pbh1 gene by SNP was confirmed by the enhanced level of the pbh1 mRNA in Pap1-positive cells but not in Pap1-negative cells. Taken together, it was demonstrated that the pbh1 genes are positively regulated by nitrosative and nitrogen starvation stresses in Pap1-dependent manner.","authors":"Cho NC, Kang HJ, Lim HW, Kim BC, Park EH, Lim CJ","authors_abbrev":"Cho NC et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2007-05-03","publication_year":"2006","canto_session_key":"c0f8c39242fadfbd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-03 22:21:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-03 22:21:18","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPCC962.02c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-12-03"},{"uniquename":"PMID:23843742","title":"Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast.","citation":"PLoS Biol 2013 Jul;11(7):e1001597","abstract":"Protein S-palmitoylation, a lipid modification mediated by members of the palmitoyltransferase family, serves as an important membrane-targeting mechanism in eukaryotes. Although changes in palmitoyltransferase expression are associated with various physiological and disease states, how these changes affect global protein palmitoylation and cellular function remains unknown. Using a bioorthogonal chemical reporter and labeling strategy to identify and analyze multiple cognate substrates of a single Erf2 palmitoyltransferase, we demonstrate that control of Erf2 activity levels underlies the differential modification of key substrates such as the Rho3 GTPase in vegetative and meiotic cells. We show further that modulation of Erf2 activity levels drives changes in the palmitoylome as cells enter meiosis and affects meiotic entry. Disruption of Erf2 function delays meiotic entry, while increasing Erf2 palmitoyltransferase activity triggers aberrant meiosis in sensitized cells. Erf2-induced meiosis requires the function of the Rho3 GTPase, which is regulated by its palmitoylation state. We propose that control of palmitoyltransferase activity levels provides a fundamental mechanism for modulating palmitoylomes and cellular functions.","doi":"10.1371/journal.pbio.1001597","authors":"Zhang MM, Wu PY, Kelly FD, Nurse P, Hang HC","authors_abbrev":"Zhang MM et al.","pubmed_publication_date":"Jul 2013","pubmed_entrez_date":"2013-07-12","publication_year":"2013","canto_session_key":"0f9cbe164dbdc4a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-01 15:20:20","canto_approved_date":"2022-11-08 18:00:19","canto_session_submitted_date":"2013-08-12 13:31:42","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPAC1F8.05","SPBC691.01","SPAC2F7.10","SPBC13G1.07","SPAC27D7.03c","SPBC3H7.09","SPAC23C4.08","SPBC32H8.11","SPBC19C2.05","SPAC3F10.07c","SPBC2F12.15c"],"gene_count":12,"ltp_gene_count":7,"approved_date":"2015-05-01"},{"uniquename":"PMID:37610834","title":"Design principles of Cdr2 node patterns in fission yeast cells.","citation":"Mol Biol Cell 2023 Oct 01;34(11):br18","abstract":"Pattern-forming networks have diverse roles in cell biology. Rod-shaped fission yeast cells use pattern formation to control the localization of mitotic signaling proteins and the cytokinetic ring. During interphase, the kinase Cdr2 forms membrane-bound multiprotein complexes termed nodes, which are positioned in the cell middle due in part to the node inhibitor Pom1 enriched at cell tips. Node positioning is important for timely cell cycle progression and positioning of the cytokinetic ring. Here, we combined experimental and modeling approaches to investigate pattern formation by the Pom1-Cdr2 system. We found that Cdr2 nodes accumulate near the nucleus, and Cdr2 undergoes nucleocytoplasmic shuttling when cortical anchoring is reduced. We generated particle-based simulations based on tip inhibition, nuclear positioning, and cortical anchoring. We tested model predictions by investigating Pom1-Cdr2 localization patterns after perturbing each positioning mechanism, including in both anucleate and multinucleated cells. Experiments show that tip inhibition and cortical anchoring alone are sufficient for the assembly and positioning of nodes in the absence of the nucleus, but that the nucleus and Pom1 facilitate the formation of unexpected node patterns in multinucleated cells. These findings have implications for spatial control of cytokinesis by nodes and for spatial patterning in other biological systems.","doi":"10.1091/mbc.E23-04-0135","authors":"Opalko H, Geng S, Hall AR, Vavylonis D, Moseley JB","authors_abbrev":"Opalko H et al.","pubmed_publication_date":"01 Oct 2023","pubmed_entrez_date":"2023-08-23","publication_year":"2023","canto_session_key":"432df2300582f190","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-08-24 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12052858","title":"A conserved domain of Schizosaccharomyces pombe dfp1(+) is uniquely required for chromosome stability following alkylation damage during S phase.","citation":"Mol Cell Biol 2002 Jul;22(13):4477-90","abstract":"The fission yeast Dbf4 homologue Dfp1 has a well-characterized role in regulating the initiation of DNA replication. Sequence analysis of Dfp1 homologues reveals three highly conserved regions, referred to as motifs N, M, and C. To determine the roles of these conserved regions in Dfp1 function, we have generated dfp1 alleles with mutations in these regions. Mutations in motif N render cells sensitive to a broad range of DNA-damaging agents and replication inhibitors, yet these mutant proteins are efficient activators of Hsk1 kinase in vitro. In contrast, mutations in motif C confer sensitivity to the alkylating agent methyl methanesulfonate (MMS) but, surprisingly, not to UV, ionizing radiation, or hydroxyurea. Motif C mutants are poor activators of Hsk1 in vitro but can fulfill the essential function(s) of Dfp1 in vivo. Strains carrying dfp1 motif C mutants have an intact mitotic and intra-S-phase checkpoint, and epistasis analysis indicates that dfp1 motif C mutants function outside of the known MMS damage repair pathways, suggesting that the observed MMS sensitivity is due to defects in recovery from DNA damage. The motif C mutants are most sensitive to MMS during S phase and are partially suppressed by deletion of the S-phase checkpoint kinase cds1. Following treatment with MMS, dfp1 motif C mutants exhibit nuclear fragmentation, chromosome instability, precocious recombination, and persistent checkpoint activation. We propose that Dfp1 plays at least two genetically separable roles in the DNA damage response in addition to its well-characterized role in the initiation of DNA replication and that motif C plays a critical role in the response to alkylation damage, perhaps by restarting or stabilizing stalled replication forks.","authors":"Fung AD, Ou J, Bueler S, Brown GW","authors_abbrev":"Fung AD et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-06-08","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC550.13","SPBC776.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"GO_REF:0000075","title":"Representation of transport of a chemical into a cellular component as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the transport of a chemical entity (ChEBI) into a cellular component as a biological process. The underlying equivalence axiom template is \"GO:0006810 and 'has_target_end_location' some T and 'imports' some S\", where T is a cellular component and S is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42275414","title":"A tti1 mutation in the Tel2-Tti1-Tti2 complex specifically eliminates the cellular function of Rad3ATR, but not that of other PIKKs in fission yeast.","citation":"PLoS Genet 2026 Jun 11;22(6):e1012206","abstract":"The Tel2-Tti1-Tti2, or TTT complex, is the co-chaperone for co-translational maturation of all phosphatidylinositol 3-kinase-related kinases (PIKKs). The complex is highly conserved in eukaryotes and controls multiple cellular processes through PIKKs. Mutations of the TTT complex have recently been linked to disease syndromes and cancer. In Schizosaccharomyces pombe, six PIKKs are expressed: Rad3ATR, Tel1ATM, Tor1 and Tor2 (homologs of mTOR), and Tra1 and Tra2 (homologs of TRRAP). While Rad3ATR and Tel1ATM are the central cell-cycle checkpoint kinases in response to DNA damage and replication stress, the other four PIKKs govern cell growth, nutrient sensing, and transcriptional regulation. Here, we report the identification of seven tti1 mutants in fission yeast that are sensitive to genotoxins. Characterization of one of the mutants, tti1-N18, reveals that the mutation selectively eliminates the kinase function of Rad3ATR, but not that of Tel1ATM. Further examination shows that, like Tel1ATM, the functions of the other four PIKKs are also largely uncompromised in the tti1-N18 mutant. These findings suggest a mechanism by which the TTT complex confers functional specificity towards Rad3ATR among the PIKKs. Since human Tel2 has been identified as a target of the antiparasitic drug Ivermectin, further investigation of the substrate specificity of the TTT complex may reveal a therapeutic vulnerability for treatment of cancer or other diseases.","doi":"10.1371/journal.pgen.1012206","authors":"Bhadra S, Ahamad N, Khan S, Xu YJ","authors_abbrev":"Bhadra S et al.","pubmed_publication_date":"11 Jun 2026","pubmed_entrez_date":"2026-06-11","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-11 23:25:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22198627","title":"Use of a ura5+-lys7+ cassette to construct unmarked gene knock-ins in Schizosaccharomyces pombe.","citation":"Curr Genet 2012 Feb;58(1):59-64","abstract":"While the counterselectable Schizosaccharomyces pombe ura4(+) gene can be used to prepare a site in the S. pombe genome to receive an unmarked mutant allele (loss of ura4(+) confers 5FOA-resistant (5FOA(R)) growth), the desired unmarked knock-in strains are generally outnumbered by spontaneously arising 5FOA(R) mutants. Relative to the same approach using the homologous URA3(+) gene in Saccharomyces cerevisiae, knock-ins in S. pombe are harder to identify due to a lower efficiency of homologous recombination and a relatively high background of spontaneous 5FOA(R) colonies. To develop an improved method for identifying cells receiving unmarked mutant alleles, we first determined that 5FOA(R) strains carry mutations in either of two genes; ura4(+) and ura5(+). We then cloned the S. pombe ura5(+) orotate phosphoribosyltransferase gene and constructed a 2.1 kb cassette containing ura5(+) together with the S. pombe lys7(+) gene. Using this doubly marked cassette to disrupt the sck1(+) kinase gene, we can distinguish between strains created by homologous knock-in of unmarked wild-type or kinase-dead alleles and spontaneously arising ura4(-) and ura5(-) mutants by screening 5FOA(R) colonies for the loss of the lys7(+) marker. The utility of this system, especially when the phenotype for the strain carrying the knock-in allele is indistinguishable from that of the disruption strain, is borne out by the fact that ~95% of 5FOA(R) colonies in our studies arose from background ura4(-) and ura5(-) mutations.","doi":"10.1007/s00294-011-0360-4","authors":"Mudge DK, Hoffman CA, Lubinski TJ, Hoffman CS","authors_abbrev":"Mudge DK et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-12-27","publication_year":"2012","canto_session_key":"ae01a084cba177d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2012-09-07 12:54:15","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-07-26 19:03:26","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.02c","SPBC725.15"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-07-26"},{"uniquename":"PMID:37099380","title":"Microtubule competition and cell growth recenter the nucleus after anaphase in fission yeast.","citation":"Mol Biol Cell 2023 Jul 01;34(8):ar77","abstract":"Cells actively position their nuclei based on their activity. In fission yeast, microtubule-dependent nuclear centering is critical for symmetrical cell division. After spindle disassembly at the end of anaphase, the nucleus recenters over an ∼90-min period, approximately half of the duration of the cell cycle. Live-cell and simulation experiments support the cooperation of two distinct microtubule competition mechanisms in the slow recentering of the nucleus. First, a push-push mechanism acts from spindle disassembly to septation and involves the opposing actions of the mitotic spindle pole body microtubules that push the nucleus away from the ends of the cell, while a postanaphase array of microtubules baskets the nucleus and limits its migration toward the division plane. Second, a slow-and-grow mechanism slowly centers the nucleus in the newborn cell by a combination of microtubule competition and asymmetric cell growth. Our work underlines how intrinsic properties of microtubules differently impact nuclear positioning according to microtubule network organization and cell size.","doi":"10.1091/mbc.E23-01-0034","authors":"Bellingham-Johnstun K, Thorn A, Belmonte JM, Laplante C","authors_abbrev":"Bellingham-Johnstun K et al.","pubmed_publication_date":"01 Jul 2023","pubmed_entrez_date":"2023-04-26","publication_year":"2023","canto_session_key":"0083e32788245bc8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kimberly Bellingham-Johnstun","canto_first_approved_date":"2023-07-04 08:19:00","canto_approved_date":"2023-09-08 08:39:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-30 22:28:36","canto_added_date":"2023-04-27 00:15:05","annotation_curators":[{"name":"Kimberly Bellingham-Johnstun","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":1,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.05c","SPAC18G6.15","SPCC417.07c","SPCC645.05c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2023-07-04"},{"uniquename":"PMID:20605454","title":"A gene-specific requirement of RNA polymerase II CTD phosphorylation for sexual differentiation in S. pombe.","citation":"Curr Biol 2010 Jun 22;20(12):1053-64","abstract":"The switch from cellular proliferation to differentiation occurs to a large extent through specific programs of gene expression. In fission yeast, the master regulator of sexual differentiation, ste11, is induced by environmental conditions leading to mating and meiosis.\nWe show that phosphorylation of serine 2 (S2P) in the C-terminal domain of the largest subunit of the RNA polymerase II (PolII) enzyme by the Lsk1 cyclin-dependent kinase has only a minor impact on global gene expression during vegetative growth but is critical for the induction of ste11 transcription during sexual differentiation. The recruitment of the Lsk1 kinase initiates in the vicinity of the transcription start site of ste11, resulting in a marked increase of S2P on the ste11 unit, including an extended 5' untranslated region (5'UTR). This pattern contrasts with the classical gradient of S2P toward the 3' region. In the absence of S2P, both PolII occupancy at the ste11 locus and ste11 expression are impaired. This results in sterility, which is rescued by expression of the ste11 coding sequence from the adh1 promoter.\nThus, the S2P polymerase plays a specific, regulatory role in cell differentiation through the induction of ste11.","doi":"10.1016/j.cub.2010.04.054","authors":"Coudreuse D, van Bakel H, Dewez M, Soutourina J, Parnell T, Vandenhaute J, Cairns B, Werner M, Hermand D","authors_abbrev":"Coudreuse D et al.","pubmed_publication_date":"22 Jun 2010","pubmed_entrez_date":"2010-07-08","publication_year":"2010","canto_session_key":"33497d588756c658","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 14:25:22","canto_approved_date":"2026-04-11 20:11:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-29 09:57:14","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":80,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.10","SPCC13B11.01","SPAC2F3.15","SPAC27D7.03c","SPCC4B3.08","SPCC1442.10c","SPBC32C12.02","SPBC14F5.05c","SPBC28F2.12","SPBC19F8.07","SPBC32H8.12c","SPBC530.13"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2019-01-30"},{"uniquename":"PMID:10449724","title":"The C-terminal region of Schizosaccaromyces pombe proliferating cell nuclear antigen is essential for DNA polymerase activity.","citation":"Proc Natl Acad Sci U S A 1999 Aug 17;96(17):9515-20","abstract":"Proliferating cell nuclear antigen (PCNA), the processivity factor (sliding clamp) of DNA polymerases (Pols), plays essential roles in DNA metabolism. In this report, we examined the functional role of the C-terminal region of Schizosaccaromyces pombe PCNA both in vitro and in vivo. The deletion or Ala substitution of the last 9 aa (252-260A), as well as Ala replacement of only 4 aa (252-255A) at the C terminus, failed to substitute for the wild-type PCNA protein for cell growth in S. pombe. Two other PCNA mutant proteins, A251V and K253E, exhibited cold-sensitive phenotypes. Several yeast strains harboring mutations, including those at the acidic C-terminal region, showed elevated sensitivity to DNA damage. The ability of the mutant PCNA proteins to stimulate DNA synthesis by Poldelta and Polepsilon also was studied in vitro. The mutant proteins that did not support cell growth and a mutant protein containing a single amino acid substitution at position 252, where Pro is replaced by Ala, stimulated Poldelta and Polepsilon activities poorly. All mutant PCNA proteins, however, were assembled around DNA by the clamp loader, replication factor C, efficiently. Thus, the C-terminal region of PCNA is important for interactions with both Poldelta and Polepsilon and for cell survival after DNA damage. The C terminus of sliding clamps from other organisms has been shown to be important for clamp loading as well as polymerase interactions. The relationship between the conserved sequence in this region in different organisms is discussed.","authors":"Kelman Z, Zuo S, Arroyo MP, Wang TS, Hurwitz J","authors_abbrev":"Kelman Z et al.","pubmed_publication_date":"17 Aug 1999","pubmed_entrez_date":"1999-08-18","publication_year":"1999","canto_session_key":"b213d2cd17d77060","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-04 14:47:03","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-02-04 14:46:57","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":79,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_10449724_phaf.tsv"}],"genes":["SPBC16D10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-02-04"},{"uniquename":"PMID:15755912","title":"Except in every detail: comparing and contrasting G-protein signaling in Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2005 Mar;4(3):495-503","abstract":"","authors":"Hoffman CS","authors_abbrev":"Hoffman CS","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-03-10","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18445486","title":"Chronological aging-induced apoptosis in yeast.","citation":"Biochim Biophys Acta 2008 Jul;1783(7):1280-5","abstract":"Saccharomyces cerevisiae is the simplest among the major eukaryotic model organisms for aging and diseases. Longevity in the chronological life span paradigm is measured as the mean and maximum survival period of populations of non-dividing yeast. This paradigm has been used successfully to identify several life-regulatory genes and three evolutionary conserved pro-aging pathways. More recently, Schizosaccharomyces pombe has been shown to age chronologically in a manner that resembles that of S. cerevisiae and that depends on the activity of the homologues of two pro-aging proteins previously identified in the budding yeast. Both yeast show features of apoptotic death during chronological aging. Here, we review some fundamental aspects of the genetics of chronological aging and the overlap between yeast aging and apoptotic processes with particular emphasis on the identification of an aging/death program that favors the dedifferentiation and regrowth of a few better adapted mutants generated within populations of aging S. cerevisiae. We also describe the use of a genome-wide screening technique to gain further insights into the mechanisms of programmed death in populations of chronologically aging S. cerevisiae.","doi":"10.1016/j.bbamcr.2008.03.017","authors":"Fabrizio P, Longo VD","authors_abbrev":"Fabrizio P et al.","pubmed_publication_date":"Jul 2008","pubmed_entrez_date":"2008-05-01","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30602572","title":"Association of mitochondria with microtubules inhibits mitochondrial fission by precluding assembly of the fission protein Dnm1.","citation":"J Biol Chem 2019 Mar 08;294(10):3385-3396","abstract":"Mitochondria are organized as tubular networks in the cell and undergo fission and fusion. Although several of the molecular players involved in mediating mitochondrial dynamics have been identified, the precise cellular cues that initiate mitochondrial fission or fusion remain largely unknown. In fission yeast ( Schizosaccharomyces pombe ), mitochondria are organized along microtubule bundles. Here, we employed deletions of kinesin-like proteins to perturb microtubule dynamics and used high-resolution and time-lapse fluorescence microscopy, revealing that mitochondrial lengths mimic microtubule lengths. Furthermore, we determined that compared with WT cells, mutant cells with long microtubules exhibit fewer mitochondria, and mutant cells with short microtubules have an increased number of mitochondria because of reduced mitochondrial fission in the former and elevated fission in the latter. Correspondingly, upon onset of closed mitosis in fission yeast, wherein interphase microtubules assemble to form the spindle within the nucleus, we observed increased mitochondrial fission. We found that the consequent rise in the mitochondrial copy number is necessary to reduce partitioning errors during independent segregation of mitochondria between daughter cells. We also discovered that the association of mitochondria with microtubules physically impedes the assembly of the fission protein Dnm1 around mitochondria, resulting in inhibition of mitochondrial fission. Taken together, we demonstrate a mechanism for the regulation of mitochondrial fission that is dictated by the interaction between mitochondria and the microtubule cytoskeleton.","doi":"10.1074/jbc.RA118.006799","authors":"Mehta K, Chacko LA, Chug MK, Jhunjhunwala S, Ananthanarayanan V","authors_abbrev":"Mehta K et al.","pubmed_publication_date":"08 Mar 2019","pubmed_entrez_date":"2019-01-04","publication_year":"2019","canto_session_key":"ecdd339b2776e271","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Leeba Ann Chacko","canto_first_approved_date":"2019-12-19 06:55:20","canto_approved_date":"2019-12-19 06:55:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-09 06:46:43","canto_added_date":"2019-01-05 01:15:04","annotation_curators":[{"name":"Leeba Ann Chacko","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.15c","SPBC25B2.07c","SPBC1604.20c","SPBC12C2.08","SPBC2F12.13"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-12-19"},{"uniquename":"PMID:12359329","title":"Cloning, expression and functional characterization of Schizosaccharomyces pombe TFIIB.","citation":"Biochim Biophys Acta 2002 Sep 27;1577(3):395-400","abstract":"The transcription factor TFIIB has been identified and cloned from the yeast Schizosaccharomyces pombe. The cloned polypeptide is highly homologous to human TFIIB and to Saccharomyces cerevisiae TFIIB. S. pombe TFIIB is a 340-amino-acid-long protein and it possesses a repeated motif of 75 amino acids near the carboxy-terminal region. The purified recombinant protein is able to bind to the TBP-DNA promoter complex in gel retardation experiments. Recombinant S. pombe TFIIB is active in in vitro transcription assays, since it can complement the transcription activity of a S. pombe cell extract in which TFIIB was depleted by using antibodies.","authors":"Tamayo E, Maldonado E","authors_abbrev":"Tamayo E et al.","pubmed_publication_date":"27 Sep 2002","pubmed_entrez_date":"2002-10-03","publication_year":"2002","canto_session_key":"2c038458800235f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-06-08 06:28:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-07 16:29:46","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16E8.16"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-09-07"},{"uniquename":"PMID:29423846","title":"Molecular Cloning and Characterization of Small Viral Genome in Fission Yeast.","citation":"Methods Mol Biol 2018;1721:47-61","abstract":"Fission yeast is a single-cell eukaryote that has been used extensively as a model organism to study cell biology and virology of higher eukaryotes including plants and humans. In particular, it is a very well-tested model to study evolutionary highly conserved cellular activities such as cell proliferation, cell cycle regulation, and cell death. Some of the advantages of using fission yeast as a surrogate system: easy to carry out functional and genome-wide analysis of small viral genome, easy to maintain in the laboratory with a relatively short doubling time. It is genetically amendable and can be used to test the effect of gain-of-function or loss-of-function of a gene product. Here, we describe a streamlined and large-scale molecular cloning strategy for genome-wide characterization of small viruses in fission yeast.","doi":"10.1007/978-1-4939-7546-4_5","authors":"Li G, Zhao RY","authors_abbrev":"Li G et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15114862","title":"Characterization of chromate-sensitive and -tolerant mutants of Schizosaccharomyces pombe.","citation":"Folia Microbiol (Praha) 2004;49(1):31-6","abstract":"Stable chromium(VI)-sensitive and -tolerant mutants were obtained by induced mutagenesis of Schizosaccharomyces pombe lysine and leucine auxotrophic heterothallic strains 6chr+ and 9chr+. Eleven of them were selected for further studies. Fast transport of 51CrO4(2-) was detected in a representative sensitive mutant, chr-51S, while the tolerant mutant chr1-66T and the parental strain 6chr+ exhibited significantly lower 51CrO4(2-) uptake. The segregation of tetrads of three selected CrVI-tolerant mutants, chr1-66T, chr1-14T and chr2-04T, strongly indicated that tolerance was determined by single mutations. Random spore analysis proved that the mutations of chr1-66T and chr1-14T were allelic and the mutation of mutant chr2-04T was not allelic with the mutation of chr1-66T. Recombinants carrying the ura4D18 selective marker were created for transformation experiments. Two of them (chr1-661T and chr2-046T) can be used to clone and identify the genes responsible for their CrVI tolerance phenotype.","authors":"Czakó-Vér K, Koósz Z, Antal J, Rácz T, Sipiczki M, Pesti M","authors_abbrev":"Czakó-Vér K et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-04-30","publication_year":"2004","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22158711","title":"Posttranslational modifications of proteins in the pathobiology of medically relevant fungi.","citation":"Eukaryot Cell 2012 Feb;11(2):98-108","abstract":"Posttranslational modifications of proteins drive a wide variety of cellular processes in eukaryotes, regulating cell growth and division as well as adaptive and developmental processes. With regard to the fungal kingdom, most information about posttranslational modifications has been generated through studies of the model yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, where, for example, the roles of protein phosphorylation, glycosylation, acetylation, ubiquitination, sumoylation, and neddylation have been dissected. More recently, information has begun to emerge for the medically important fungal pathogens Candida albicans, Aspergillus fumigatus, and Cryptococcus neoformans, highlighting the relevance of posttranslational modifications for virulence. We review the available literature on protein modifications in fungal pathogens, focusing in particular upon the reversible peptide modifications sumoylation, ubiquitination, and neddylation.","doi":"10.1128/EC.05238-11","authors":"Leach MD, Brown AJ","authors_abbrev":"Leach MD et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-12-14","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20040595","title":"Roles of heterochromatin and telomere proteins in regulation of fission yeast telomere recombination and telomerase recruitment.","citation":"J Biol Chem 2010 Feb 19;285(8):5327-37","abstract":"When the telomerase catalytic subunit (Trt1/TERT) is deleted, a majority of fission yeast cells survives by circularizing chromosomes. Alternatively, a small minority survives by maintaining telomeric repeats through recombination among telomeres. The recombination-based telomere maintenance in trt1Delta cells is inhibited by the telomere protein Taz1. In addition, catalytically inactive full-length Trt1 (Trt1-CI) and truncated Trt1 lacking the T-motif and reverse transcriptase (RT) domain (Trt1-DeltaT/RT) can strongly inhibit recombination-based survival. Here, we investigated the effects of deleting the heterochromatin proteins Swi6 (HP1 ortholog) and Clr4 (Suv39 family of histone methyltransferases) and the telomere capping complex subunits Poz1 and Ccq1 on Taz1- and Trt1-dependent telomere recombination inhibition. The ability of Taz1 to inhibit telomere recombination did not require Swi6, Clr4, Poz1, or Ccq1. Although Swi6, Clr4, and Poz1 were dispensable for the inhibition of telomere recombination by Trt1-CI, Ccq1 was required for efficient telomere recruitment of Trt1 and Trt1-CI-dependent inhibition of telomere recombination. We also found that Swi6, Clr4, Ccq1, the checkpoint kinase Rad3 (ATR ortholog), and the telomerase regulatory subunit Est1 are all required for Trt1-DeltaT/RT to inhibit telomere recombination. However, because loss of Swi6, Clr4, Rad3, Ccq1, or Est1 did not significantly alter the recruitment efficiency of Trt1-DeltaT/RT to telomeres, these factors are likely to enhance the ability of Trt1-DeltaT/RT to inhibit recombination-based survival by contributing to the negative regulation of telomere recombination.","doi":"10.1074/jbc.M109.078840","authors":"Khair L, Subramanian L, Moser BA, Nakamura TM","authors_abbrev":"Khair L et al.","pubmed_publication_date":"19 Feb 2010","pubmed_entrez_date":"2009-12-31","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.07","SPAC16A10.07c","SPBC29A3.14c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU007385","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3514248","title":"Colcemid-resistant mutants of fission yeast have an altered cell cycle.","citation":"Exp Cell Res 1986 Apr;163(2):467-76","abstract":"Cell-cycle progression is altered in some colcemid-resistant mutants of fission yeast. The duration of particular stages of the cell cycle is different but total doubling time is unchanged from that of wild type. Cell-plate formation is prolonged relative to wild type but concomitant DNA synthesis is not affected. Separation of daughter cells is inhibited in some strains, giving rise to unusual cell morphologies. Control of cell division is altered in two ways: Critical size for division is increased. The probability of division a function of size is decreased.","authors":"Sackett DL, Lederberg S","authors_abbrev":"Sackett DL et al.","pubmed_publication_date":"Apr 1986","pubmed_entrez_date":"1986-04-01","publication_year":"1986","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22095407","title":"Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding.","citation":"Chem Commun (Camb) 2012 Jan 07;48(2):296-8","abstract":"A new route to the synthesis of triazole-linked ubiquitin dimers (diUbs) as structural analogs of the seven diUbs is reported. Binding studies with the Lys48-specific UBA domain of the Mud1 protein suggest that they represent functionally suitable surrogates of their native counterparts linked by an isopeptide bond.","doi":"10.1039/c1cc15834a","authors":"Weikart ND, Sommer S, Mootz HD","authors_abbrev":"Weikart ND et al.","pubmed_publication_date":"07 Jan 2012","pubmed_entrez_date":"2011-11-19","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC56F8.08","SPBC337.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:2544298","title":"The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases.","citation":"Cell 1989 Jun 16;57(6):997-1007","abstract":"S. pombe dis mutants block mitotic chromosome disjunction in a manner reminiscent of aneuploidy formation, and belong to three distinct genes, dis1-dis3. We cloned two independent genomic DNAs that complemented both the cold-sensitive and caffeine-hypersensitive phenotype of dis2-11. These genes, dis2+ and a suppressor sds21+, encode proteins (calculated MW 37,000) with similar predicted amino acid sequences. dis2+ and sds21+ have overlapping functions, and disruptants are lethal only when both genes are disrupted. The gene products identified by anti-dis2 serum are enriched in nuclei. By hybridization, we obtained two cDNA clones from mouse and one genomic clone from S. cerevisiae; the latter complements S. pombe dis2-11. These dis2+ and similar polypeptides of yeasts and mouse are found to be highly homologous (75%-90% identical) to rabbit protein phosphatase 1. The implications of these findings are discussed with regard to mitotic control.","authors":"Ohkura H, Kinoshita N, Miyatani S, Toda T, Yanagida M","authors_abbrev":"Ohkura H et al.","pubmed_publication_date":"16 Jun 1989","pubmed_entrez_date":"1989-06-16","publication_year":"1989","canto_session_key":"f29ec3e2ad255c60","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-09-22 14:10:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 14:37:46","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.02c","SPCC31H12.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-01-25"},{"uniquename":"PMID:5672967","title":"The role of lethal sectoring in the origin of complete mutations in Schizosaccharomyces pombe.","citation":"Mutat Res 1968;5(2):225-9","abstract":"","authors":"Guglielminetti R","authors_abbrev":"Guglielminetti R","pubmed_publication_date":"1968","pubmed_entrez_date":"1968-03-01","publication_year":"1968","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26246602","title":"Replication stress in early S phase generates apparent micronuclei and chromosome rearrangement in fission yeast.","citation":"Mol Biol Cell 2015 Oct 01;26(19):3439-50","abstract":"DNA replication stress causes genome mutations, rearrangements, and chromosome missegregation, which are implicated in cancer. We analyze a fission yeast mutant that is unable to complete S phase due to a defective subunit of the MCM helicase. Despite underreplicated and damaged DNA, these cells evade the G2 damage checkpoint to form ultrafine bridges, fragmented centromeres, and uneven chromosome segregations that resembles micronuclei. These micronuclei retain DNA damage markers and frequently rejoin with the parent nucleus. Surviving cells show an increased rate of mutation and chromosome rearrangement. This first report of micronucleus-like segregation in a yeast replication mutant establishes underreplication as an important factor contributing to checkpoint escape, abnormal chromosome segregation, and chromosome instability.","doi":"10.1091/mbc.E15-05-0318","authors":"Sabatinos SA, Ranatunga NS, Yuan JP, Green MD, Forsburg SL","authors_abbrev":"Sabatinos SA et al.","pubmed_publication_date":"01 Oct 2015","pubmed_entrez_date":"2015-08-07","publication_year":"2015","canto_session_key":"3b47172334668987","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-09 00:19:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37499161","title":"Discovering the effect of co-fermentation involving Saccharomyces cerevisiae and Schizosaccharomyces pombe on the sensory quality improvement of mandarin wine based on metabolites and transcriptomic profiles.","citation":"J Sci Food Agric 2023 Dec;103(15):7932-7940","abstract":"Mandarin wine has high added value, which can extend the industry chain of mandarins with excellent economic results. However, innovative fermentation methods are urgently needed to improve the typical taste and flavor characteristics of mandarin wine. In this study, the effect and underlying mechanism of co-fermentation with Saccharomyces cerevisiae and Schizosaccharomyces pombe on the characteristics of mandarin wine were investigated based on integrated metabolomic and transcriptomic analyses.\nIn comparison with fermentation with only S. cerevisiae, the mandarin wine produced from co-fermentation with S. cerevisiae and Sc. pombe had a higher pH value, lower malic acid content, and more abundant free amino acids, resulting in better sensory evaluation scores. The introduction of Sc. pombe extended the stage of alcoholic fermentation and enhanced the richness and diversity of volatile compounds, especially floral and fruity aroma compounds, including ethyl hexanoate, ethyl caprylate, ethyl enanthate, 1-heptanol, and phenylethyl alcohol. he significantly differential metabolites and varying genes were mainly found in pathways of glycolysis, pyruvate metabolism, the citrate cycle, and amino acid metabolism.\nCo-fermentation with S. cerevisiae and Sc. pombe showed advantages in producing distinctive taste and flavor of mandarin wine in comparison with fermentation with only S. cerevisiae. This study can inspire new co-fermentation strategies to improve the sensory quality of mandarin wine. © 2023 Society of Chemical Industry.","doi":"10.1002/jsfa.12885","authors":"Luo X, Li Y, Zhong K, Luo D, Wu Y, Gao H","authors_abbrev":"Luo X et al.","pubmed_publication_date":"Dec 2023","pubmed_entrez_date":"2023-07-27","publication_year":"2023","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2023-07-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14765111","title":"Formation, maintenance and consequences of the imprint at the mating-type locus in fission yeast.","citation":"EMBO J 2004 Feb 25;23(4):930-8","abstract":"Mating-type switching in the fission yeast Schizosaccharomyces pombe is initiated by a strand-specific imprint located at the mating-type (mat1) locus. We show that the imprint corresponds to a single-strand DNA break (SSB), which is site- but not sequence-specific. We identified three novel cis-acting elements, involved in the formation and stability of the SSB. One of these elements is essential for a replication fork pause next to mat1 and interacts in vivo with the Swi1 protein. Another element is essential for maintaining the SSB during cell cycle progression. These results suggest that the DNA break appears during the S-phase and is actively protected against repair. Consequently, during the following round of replication, a polar double-strand break is formed. We show that when the replication fork encounters the SSB, the leading-strand DNA polymerase is able to synthesize DNA to the edge of the SSB, creating a blunt-ended recombination intermediate.","authors":"Kaykov A, Holmes AM, Arcangioli B","authors_abbrev":"Kaykov A et al.","pubmed_publication_date":"25 Feb 2004","pubmed_entrez_date":"2004-02-07","publication_year":"2004","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10198041","title":"Cdc25 inhibited in vivo and in vitro by checkpoint kinases Cds1 and Chk1.","citation":"Mol Biol Cell 1999 Apr;10(4):833-45","abstract":"In the fission yeast Schizosaccharomyces pombe, the protein kinase Cds1 is activated by the S-M replication checkpoint that prevents mitosis when DNA is incompletely replicated. Cds1 is proposed to regulate Wee1 and Mik1, two tyrosine kinases that inhibit the mitotic kinase Cdc2. Here, we present evidence from in vivo and in vitro studies, which indicates that Cds1 also inhibits Cdc25, the phosphatase that activates Cdc2. In an in vivo assay that measures the rate at which Cdc25 catalyzes mitosis, Cds1 contributed to a mitotic delay imposed by the S-M replication checkpoint. Cds1 also inhibited Cdc25-dependent activation of Cdc2 in vitro. Chk1, a protein kinase that is required for the G2-M damage checkpoint that prevents mitosis while DNA is being repaired, also inhibited Cdc25 in the in vitro assay. In vitro, Cds1 and Chk1 phosphorylated Cdc25 predominantly on serine-99. The Cdc25 alanine-99 mutation partially impaired the S-M replication and G2-M damage checkpoints in vivo. Thus, Cds1 and Chk1 seem to act in different checkpoint responses to regulate Cdc25 by similar mechanisms.","authors":"Furnari B, Blasina A, Boddy MN, McGowan CH, Russell P","authors_abbrev":"Furnari B et al.","pubmed_publication_date":"Apr 1999","pubmed_entrez_date":"1999-04-10","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPCC1259.13","SPCC18B5.11c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:32160533","title":"The GATA Transcription Factor Gaf1 Represses tRNAs, Inhibits Growth, and Extends Chronological Lifespan Downstream of Fission Yeast TORC1.","citation":"Cell Rep 2020 Mar 10;30(10):3240-3249.e4","abstract":"Target of Rapamycin Complex 1 (TORC1) signaling promotes growth and aging. Inhibition of TORC1 leads to reduced protein translation, which promotes longevity. TORC1-dependent post-transcriptional regulation of protein translation has been well studied, while analogous transcriptional regulation is less understood. Here we screen fission yeast mutants for resistance to Torin1, which inhibits TORC1 and cell growth. Cells lacking the GATA factor Gaf1 (gaf1Δ) grow normally even in high doses of Torin1. The gaf1Δ mutation shortens the chronological lifespan of non-dividing cells and diminishes Torin1-mediated longevity. Expression profiling and genome-wide binding experiments show that upon TORC1 inhibition, Gaf1 directly upregulates genes for small-molecule metabolic pathways and indirectly represses genes for protein translation. Surprisingly, Gaf1 binds to and downregulates the tRNA genes, so it also functions as a transcription factor for RNA polymerase III. Thus, Gaf1 controls the transcription of both protein-coding and tRNA genes to inhibit translation and growth downstream of TORC1.","doi":"10.1016/j.celrep.2020.02.058","authors":"Rodríguez-López M, Gonzalez S, Hillson O, Tunnacliffe E, Codlin S, Tallada VA, Bähler J, Rallis C","authors_abbrev":"Rodríguez-López M et al.","pubmed_publication_date":"10 Mar 2020","pubmed_entrez_date":"2020-03-12","publication_year":"2020","canto_session_key":"133b1ecfd4427aac","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-03-13 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37674027","title":"Fission yeast Cdc14-like phosphatase Flp1/Clp1 modulates the transcriptional response to oxidative stress.","citation":"Sci Rep 2023 Sep 06;13(1):14677","abstract":"Reactive oxygen species (ROS) are an important source of cellular damage. When ROS intracellular levels increase, oxidative stress takes place affecting DNA stability and metabolic functions. To prevent these effects, stress-activated protein kinases (SAPKs) delay cell cycle progression and induce a transcriptional response that activates antioxidant mechanisms ensuring cell adaptation and survival. Fission yeast Cdc14-like phosphatase Flp1 (also known as Clp1) has a well-established role in cell cycle regulation. Moreover, Flp1 contributes to checkpoint activation during replication stress. Here, we show that Flp1 has a role in fine-tuning the cellular oxidative stress response. Phosphorylation-dependent nucleolar release of Flp1 in response to oxidative stress conditions plays a role in the cellular transcriptional response. Thus, Flp1 ablation increases the transcriptional response to oxidative stress, in both intensity and duration, upregulating both Atf1/Pcr1- and Pap1-dependent stress induced genes. Remarkably, we found that Flp1 interacts with the Atf1/Pcr1 complex with Pcr1 acting as a direct substrate. Our results provide evidence that Flp1 modulates the oxidative stress response by limiting the Atf1/Pcr1-mediated transcription.","doi":"10.1038/s41598-023-41869-w","authors":"Canete JA, Andrés S, Muñoz S, Zamarreño J, Rodríguez S, Díaz-Cuervo H, Bueno A, Sacristán MP","authors_abbrev":"Canete JA et al.","pubmed_publication_date":"06 Sep 2023","pubmed_entrez_date":"2023-09-06","publication_year":"2023","canto_session_key":"bc93c6ff0cf35a01","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-09-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19474788","title":"Structural insight into the autoinhibition mechanism of AMP-activated protein kinase.","citation":"Nature 2009 Jun 25;459(7250):1146-9","abstract":"The AMP-activated protein kinase (AMPK) is characterized by its ability to bind to AMP, which enables it to adjust enzymatic activity by sensing the cellular energy status and maintain the balance between ATP production and consumption in eukaryotic cells. It also has important roles in the regulation of cell growth and proliferation, and in the establishment and maintenance of cell polarity. These important functions have rendered AMPK an important drug target for obesity, type 2 diabetes and cancer treatments. However, the regulatory mechanism of AMPK activity by AMP binding remains unsolved. Here we report the crystal structures of an unphosphorylated fragment of the AMPK alpha-subunit (KD-AID) from Schizosaccharomyces pombe that contains both the catalytic kinase domain and an autoinhibitory domain (AID), and of a phosphorylated kinase domain from Saccharomyces cerevisiae (Snf1-pKD). The AID binds, from the 'backside', to the hinge region of its kinase domain, forming contacts with both amino-terminal and carboxy-terminal lobes. Structural analyses indicate that AID binding might constrain the mobility of helix alphaC, hence resulting in an autoinhibited KD-AID with much lower kinase activity than that of the kinase domain alone. AMP activates AMPK both allosterically and by inhibiting dephosphorylation. Further in vitro kinetic studies demonstrate that disruption of the KD-AID interface reverses the autoinhibition and these AMPK heterotrimeric mutants no longer respond to the change in AMP concentration. The structural and biochemical data have shown the primary mechanism of AMPK autoinhibition and suggest a conformational switch model for AMPK activation by AMP.","doi":"10.1038/nature08075","authors":"Chen L, Jiao ZH, Zheng LS, Zhang YY, Xie ST, Wang ZX, Wu JW","authors_abbrev":"Chen L et al.","pubmed_publication_date":"25 Jun 2009","pubmed_entrez_date":"2009-05-29","publication_year":"2009","canto_session_key":"853eca813b9575cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-15 17:17:54","canto_approved_date":"2023-02-15 17:17:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-15 17:17:46","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC74.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-15","pdb_entries":[{"pdb_id":"3h4j","gene_chains":[{"gene_uniquename":"SPCC74.03c","chain":"A/B","position":"25-351"}],"title":"crystal structure of pombe AMPK KDAID fragment","entry_authors":"Chen L,Jiao Z-H,Zheng L-S,Zhang Y-Y,Xie S-T,Wang Z-X,Wu J-W","entry_authors_abbrev":"Chen L et al.","reference_uniquename":"PMID:19474788","experimental_method":"X-ray","resolution":"2.8"}]},{"uniquename":"PMID:16516201","title":"The ribosomal protein L32-2 (RPL32-2) of S. pombe exhibits a novel extraribosomal function by acting as a potential transcriptional regulator.","citation":"FEBS Lett 2006 Mar 20;580(7):1827-32","abstract":"Ribosomal proteins play important roles in stabilizing the rRNA structure to facilitate protein synthesis in ribosome. In the present study, we analyzed the potential extraribosomal function of the ribosomal protein L32-2 (RPL32-2), which was expressed by a gene clone isolated from a cDNA library of Schizosaccharomyces pombe (S. pombe). RPL32-2 fused with the GAL4 DNA-bind domain or the GAL4 transcriptional activating domain could, respectively, activate transcriptions of reporter genes in yeast strain AH109. The RPL32-2 mutants with truncation of either the N- or the C-terminal domain resulted in abolishment of this regulatory effect. The DNA binding site for RPL32-2 of S. pombe was identified by using a random oligonucleotide selection strategy and gel motility shift assay and Western blotting confirmed its binding specificity. Moreover, we found RPL32-2 was also able to interact with a to-be-identified AT sequence binding protein. These data suggest that RPL32-2 of S. pombe, besides its ribosomal function, may also act as a potential transcriptional regulator in nucleus.","authors":"Wang J, Yuan S, Jiang S","authors_abbrev":"Wang J et al.","pubmed_publication_date":"20 Mar 2006","pubmed_entrez_date":"2006-03-07","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2115527","title":"CO2 production after induction synchrony of the fission yeast Schizosaccharomyces pombe: the origin and nature of entrainment.","citation":"J Cell Sci 1990 May;96 ( Pt 1):79-91","abstract":"Earlier work has shown that there is a periodic change in the rate of production of CO2 during the cell cycle of fission yeast and that this periodicity persists after a block to the DNA-division cycle and also after a block to protein synthesis. It appears that there is a periodic control or 'oscillator' affecting CO2 production that is normally closely entrained to the cell cycle, but which can 'free-run' after a block. In this paper, we examine what events in the DNA-division cycle can generate the entrainment signals and what is the nature of such signals. In the first set of experiments, CO2 production was measured by manometry during induction synchrony produced by blocking the DNA-division cycle in an asynchronous culture for a period and then releasing the block. Synchronous cell division occurs after the release with cell cycles shorter than normal. After release from a block imposed by shifting up the mutant cdc2.33 to the restrictive temperature, oscillations in CO2 production started rapidly and remained closely entrained to the division cycles (with slightly different patterns and timing from those after selection synchrony). This showed that there was an entrainment signal but did not show whether it came from start, the S period or mitosis. A similar experiment with cdc10.129 showed that an early signal came from either start or the S period, as did an experiment with release from N-starvation. The results with cdc25.22 were similar to those with cdc2.33. After a block with hydroxyurea, there was entrainment but with no signs of the early signal that occurred with cdc10. This showed that the early signal came from start and not from the S period. In a second set of double-block experiments, the first block was followed by a second different block. With cdc25.22 followed by MBC (an inhibitor of nuclear division) the cells passed through a narrow window of the cell cycle between the transition point of cdc25.22 and mitosis. This was sufficient to start the oscillations, showing that an entrainment signal could be generated at about the time of mitosis. The results from using hydroxyurea followed by cdc2.33 showed no genuine oscillations, confirming the conclusion from the single hydroxyurea block. The results from using hydroxyurea followed by cdc10.129 confirmed the existence of a mitotic signal.(ABSTRACT TRUNCATED AT 400 WORDS)","authors":"Novak B, Mitchison JM","authors_abbrev":"Novak B et al.","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18411246","title":"Mug27 is a meiosis-specific protein kinase that functions in fission yeast meiosis II and sporulation.","citation":"J Cell Sci 2008 May 01;121(Pt 9):1547-58","abstract":"Several meiosis-specific proteins of Schizosaccharomyces pombe play essential roles in meiotic progression. We report here that a novel meiosis-specific protein kinase, Mug27 (also known as Ppk35), is required for proper spore formation. This kinase is expressed by the mug27(+) gene, which is abruptly transcribed after horsetail movement. This transcription is maintained until the second meiotic division. Green fluorescent protein (GFP)-tagged Mug27 appears at the start of prometaphase I, localizes to the spindle pole body (SPB) and then translocates to the forespore membrane (FSM) at late anaphase II. In the mug27Delta strain, smaller spores are produced compared with those of the mug27(+) strain. Moreover, spore viability was reduced by half or more compared with that of the mug27(+) strain. The protein-kinase activity of Mug27 appears to be important for its function: the putative kinase-dead Mug27 mutant had similar phenotypes to mug27Delta. Our results here indicate that the Mug27 kinase localizes at the SPB and regulates FSM formation and sporulation.","doi":"10.1242/jcs.022830","authors":"Ohtaka A, Okuzaki D, Nojima H","authors_abbrev":"Ohtaka A et al.","pubmed_publication_date":"01 May 2008","pubmed_entrez_date":"2008-04-16","publication_year":"2008","canto_session_key":"d30203723a93539d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-06-15 08:17:20","canto_approved_date":"2020-03-07 19:04:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-05-25 16:02:16","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.06c","SPCC417.06c","SPBC244.01c","SPCC1739.11c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-06-15"},{"uniquename":"PMID:7808417","title":"A Drosophila gene encoding a DEAD box RNA helicase can suppress loss of wee1/mik1 function in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1994 Dec 01;245(5):654-7","abstract":"We describe a screen to isolate cDNAs encoding Drosophila mitosis inhibitors capable of suppressing the mitotic catastrophe phenotype resulting in Schizosaccharomyces pombe from the combination of the wee1-50 mutation with either a deletion allele of mik1, or with overexpression of cdc25+. One plasmid was isolated which could suppress the temperature sensitive lethality of both these strains. The cDNA in this plasmid encodes a protein highly homologous to the DEAD-box family of ATP-dependent RNA helicases, rather than to protein kinases as might be expected. It is possible that the RNA helicase described here may regulate entry into mitosis by down regulating the expression of other genes whose activity may be rate-limiting for entry into mitosis.","authors":"Warbrick E, Glover D","authors_abbrev":"Warbrick E et al.","pubmed_publication_date":"01 Dec 1994","pubmed_entrez_date":"1994-12-01","publication_year":"1994","canto_session_key":"e746aa285c240062","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 14:35:16","canto_session_submitted_date":"2012-03-03 14:34:28","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.14","SPCC18B5.03","SPAC24H6.05"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:11447596","title":"Characterization of a Schizosaccharomyces pombe mutant deficient in UDP-galactose transport activity.","citation":"Yeast 2001 Jul;18(10):903-14","abstract":"In fission yeast, Schizosaccharomyces pombe, the carbohydrate components of the cell wall consist of galactomannan, unlike in Saccharomyces cerevisiae. We previously found that the disruption of gms1+, a gene encoding the UDP-galactose transporter required for the synthesis of galactomannan, led to the complete defect of cell surface galactosylation in Sz. pombe. The Deltagms1 strain is therefore useful for the analysis of physiological properties of galactose residues in Sz. pombe. The deletion strain of gms1+ was viable; however, itshowed an aberrant cell morphology and increased sensitivities to digestion with beta-glucanase and to various drugs, such as hygromycin B, sodium orthovanadate and Calcofluor white. A reduction of galactomannan layers of the cell wall in the Deltagms1 strain was observed by scanning and transmission electron microscopic analyses. The addition of osmotic stabilizer suppressed the morphologic defect of the Deltagms1 cells, while other phenotypes were weakly suppressed. The Deltagms1 (h90) strain was incapable of sexual conjugation during nutritional starvation. These results suggest that the cell surface galactosylation is required not only for non-sexual flocculation but also for sexual conjugation in Sz. pombe.","authors":"Tanaka N, Konomi M, Osumi M, Takegawa K","authors_abbrev":"Tanaka N et al.","pubmed_publication_date":"Jul 2001","pubmed_entrez_date":"2001-07-12","publication_year":"2001","canto_session_key":"d54dffa450d60b15","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-18 11:49:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-02-18 11:49:31","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-02-18"},{"uniquename":"PMID:23123849","title":"Structure of the Mediator head module.","citation":"Nature 2012 Dec 20;492(7429):448-51","abstract":"Gene transcription by RNA polymerase (Pol) II requires the coactivator complex Mediator. Mediator connects transcriptional regulators and Pol II, and is linked to human disease. Mediator from the yeast Saccharomyces cerevisiae has a molecular mass of 1.4 megadaltons and comprises 25 subunits that form the head, middle, tail and kinase modules. The head module constitutes one-half of the essential Mediator core, and comprises the conserved subunits Med6, Med8, Med11, Med17, Med18, Med20 and Med22. Recent X-ray analysis of the S. cerevisiae head module at 4.3 Å resolution led to a partial architectural model with three submodules called neck, fixed jaw and moveable jaw. Here we determine de novo the crystal structure of the head module from the fission yeast Schizosaccharomyces pombe at 3.4 Å resolution. Structure solution was enabled by new structures of Med6 and the fixed jaw, and previous structures of the moveable jaw and part of the neck, and required deletion of Med20. The S. pombe head module resembles the head of a crocodile with eight distinct elements, of which at least four are mobile. The fixed jaw comprises tooth and nose domains, whereas the neck submodule contains a helical spine and one limb, with shoulder, arm and finger elements. The arm and the essential shoulder contact other parts of Mediator. The jaws and a central joint are implicated in interactions with Pol II and its carboxy-terminal domain, and the joint is required for transcription in vitro. The S. pombe head module structure leads to a revised model of the S. cerevisiae module, reveals a high conservation and flexibility, explains known mutations, and provides the basis for unravelling a central mechanism of gene regulation.","doi":"10.1038/nature11670","authors":"Larivière L, Plaschka C, Seizl M, Wenzeck L, Kurth F, Cramer P","authors_abbrev":"Larivière L et al.","pubmed_publication_date":"20 Dec 2012","pubmed_entrez_date":"2012-11-06","publication_year":"2012","canto_session_key":"b8ea8cb21d9f0b36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-09-03 14:56:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-03 14:56:09","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.04","SPBC31F10.04c","SPAC29A4.07","SPAC1002.15c","SPAC644.10","SPAC5D6.05","SPAC17G8.05"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2014-09-03","pdb_entries":[{"pdb_id":"4h63","gene_chains":[{"gene_uniquename":"SPAC29A4.07","chain":"V","position":"2-136"},{"gene_uniquename":"SPAC5D6.05","chain":"R","position":"1-207"},{"gene_uniquename":"SPBC21.04","chain":"H","position":"1-200"},{"gene_uniquename":"SPBC31F10.04c","chain":"Q","position":"78-545"},{"gene_uniquename":"SPAC644.10","chain":"K","position":"1-112"},{"gene_uniquename":"SPAC1002.15c","chain":"F","position":"1-180"}],"title":"Structure of the Schizosaccharomyces pombe Mediator head module","entry_authors":"Lariviere L,Plaschka C,Seizl M,Wenzeck L,Kurth F,Cramer P","entry_authors_abbrev":"Lariviere L et al.","reference_uniquename":"PMID:23123849","experimental_method":"X-ray","resolution":"3.4"},{"pdb_id":"4h61","gene_chains":[{"gene_uniquename":"SPAC1002.15c","chain":"A/B","position":"10-180"}],"title":"Structure of the Schizosaccharomyces pombe Mediator subunit Med6","entry_authors":"Lariviere L,Plaschka C,Seizl M,Wenzeck L,Kurth F,Cramer P","entry_authors_abbrev":"Lariviere L et al.","reference_uniquename":"PMID:23123849","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:24711368","title":"The Dnmt2 RNA methyltransferase homolog of Geobacter sulfurreducens specifically methylates tRNA-Glu.","citation":"Nucleic Acids Res 2014 Jun;42(10):6487-96","abstract":"Dnmt2 enzymes are conserved in eukaryotes, where they methylate C38 of tRNA-Asp with high activity. Here, the activity of one of the very few prokaryotic Dnmt2 homologs from Geobacter species (GsDnmt2) was investigated. GsDnmt2 was observed to methylate tRNA-Asp from flies and mice. Unexpectedly, it had only a weak activity toward its matching Geobacter tRNA-Asp, but methylated Geobacter tRNA-Glu with good activity. In agreement with this result, we show that tRNA-Glu is methylated in Geobacter while the methylation is absent in tRNA-Asp. The activities of Dnmt2 enzymes from Homo sapiens, Drosophila melanogaster, Schizosaccharomyces pombe and Dictyostelium discoideum for methylation of the Geobacter tRNA-Asp and tRNA-Glu were determined showing that all these Dnmt2s preferentially methylate tRNA-Asp. Hence, the GsDnmt2 enzyme has a swapped transfer ribonucleic acid (tRNA) specificity. By comparing the different tRNAs, a characteristic sequence pattern was identified in the variable loop of all preferred tRNA substrates. An exchange of two nucleotides in the variable loop of murine tRNA-Asp converted it to the corresponding variable loop of tRNA-Glu and led to a strong reduction of GsDnmt2 activity. Interestingly, the same loss of activity was observed with human DNMT2, indicating that the variable loop functions as a specificity determinant in tRNA recognition of Dnmt2 enzymes.","doi":"10.1093/nar/gku256","authors":"Shanmugam R, Aklujkar M, Schäfer M, Reinhardt R, Nickel O, Reuter G, Lovley DR, Ehrenhofer-Murray A, Nellen W, Ankri S, Helm M, Jurkowski TP, Jeltsch A","authors_abbrev":"Shanmugam R et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-04-09","publication_year":"2014","canto_session_key":"a47e9d9392fe4fa6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-05-15 21:33:39","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-15 21:31:44","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-15"},{"uniquename":"PMID:19669754","title":"Enhanced protein secretion from multiprotease-deficient fission yeast by modification of its vacuolar protein sorting pathway.","citation":"Appl Microbiol Biotechnol 2010 Jan;85(3):667-77","abstract":"Previously, we achieved approximately 30-fold enhanced secretion of the protease-sensitive model protein human growth hormone (hGH) by multiple gene deletion of seven obstructive proteases in the fission yeast Schizosaccharomyces pombe. However, intracellular retention of secretory hGH was found in the resultant multiprotease-deficient strains. As a solution, genetic modification of the intracellular trafficking pathway that is related to intracellular retention of hGH was attempted on a protease octuple deletant strain. Vacuolar accumulation of the intracellularly retained hGH was identified by secretory expression of hGH fused with EGFP, and three vacuolar protein sorting (vps)-deficient strains, vps10Delta, vps22Delta, and vps34Delta, were determined on account of their hGH secretion efficiency. The mutant vps10Delta was found to be effective for hGH secretion, which suggested a role for vps10 in the vacuolar accumulation of the intracellularly retained hGH. Finally, vps10 deletion was performed on the protease octuple deletant strain, which led to an approximately 2-fold increase in hGH secretion. This indicated the possible application of secretory-pathway modification and multiple protease deletion for improving heterologous protein secretion from the fission yeast S. pombe.","doi":"10.1007/s00253-009-2151-0","authors":"Idiris A, Tohda H, Sasaki M, Okada K, Kumagai H, Giga-Hama Y, Takegawa K","authors_abbrev":"Idiris A et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-08-12","publication_year":"2010","canto_session_key":"433b4930c599dc93","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-02-16 11:13:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-02-16 11:13:17","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC458.05","SPBC651.05c","SPAC1006.01","SPAP14E8.04","SPBC14C8.03","SPAC4F10.02","SPAC4A8.04","SPAC19B12.08","SPAC1296.03c","SPBC16C6.06","SPBC1711.12"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2016-02-16"},{"uniquename":"PMID:19549493","title":"Chromosome segregation: monopolin goes spindle.","citation":"Curr Biol 2009 Jun 23;19(12):R482-4","abstract":"At anaphase onset the mitotic spindle undergoes dramatic changes in order to segregate sister chromatids. Surprisingly, the monopolin complex, best known for its role at kinetochores in meiosis, is now shown to localize to, and stabilize, the mitotic anaphase spindle.","doi":"10.1016/j.cub.2009.05.006","authors":"Khmelinskii A, Schiebel E","authors_abbrev":"Khmelinskii A et al.","pubmed_publication_date":"23 Jun 2009","pubmed_entrez_date":"2009-06-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17176760","title":"The dose-dependent H2O2 stress response promotes increased survival for Schizosaccharomyces pombe cells expressing HIV-1 Vpr.","citation":"Folia Microbiol (Praha) 2006;51(5):406-12","abstract":"Human immunodeficiency virus type 1 (HIV-1) viral protein R (Vpr) exerts multiple effects on viral and host cellular activities during infection, including induction of the cell cycle G2 arrest, and cell death in both human cells and the fission yeast Schizosaccharomyces pombe. We show that treament of exponential-phase wild-type Vpr-expressing S. pombe cells with a low, subinhibitory concentration (0.15 mmol/L) of hydrogen peroxide and 0.1 mmol/L thiamine significantly increased both cell proliferation and survival rates and decreased the number of elongated G2-arrested cells. Short-term, H2O2-induced adaptive stress increased the survival of the cells while acute stress conditions interrupted the Vpr-mediated death of the cells; however, no changes in cell length or cell phase were detected. The results suggest the importance of the oxidative status of the cells in Vpr-mediated processes. Our findings contribute to the development of a new approach via which to investigate the contribution of Vpr to HIV pathogenesis and to reduce the Vpr-mediated effects in HIV-infected patients.","authors":"Antal J, Pesti M","authors_abbrev":"Antal J et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-12-21","publication_year":"2006","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18268844","title":"RNAi-mediated chromatin silencing in fission yeast.","citation":"Curr Top Microbiol Immunol 2008;320:157-83","abstract":"In the fission yeast Schizosaccharomyces pombe, the RNAi pathway plays an important role in the formation and maintenance of heterochromatin. Heterochromatin, or silent chromatin, is an epigenetically inherited attribute of eukaryotic chromosomes which is required for gene regulation, chromosome segregation and maintenance of genome stability. In S. pombe, heterochromatin forms on related repetitive DNA sequences at specific loci. These repetitive sequences, in concert with the RNAi machinery, are thought to attract several proteins including chromatin-modifying enzymes which act to promote heterochromatin formation. The purification of complexes participating in heterochromatin formation has allowed us to begin to analyse in detail the processes involved. In the future this will help us to understand how the RNAi machinery acts to induce the chromatin modifications which lead to heterochromatin assembly in fission yeast.","authors":"White SA, Allshire RC","authors_abbrev":"White SA et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-02-14","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9204519","title":"Growth of Schizosaccharomyces pombe on glucose-malate mixtures in continuous cell-recycle cultures. Kinetics of substrate utilization.","citation":"Appl Biochem Biotechnol 1997 Apr;66(1):69-81","abstract":"The aerobic growth of Schizosaccharomyces pombe on mixtures of glucose and malate was investigated during continuous high cell density cultures with partial cell-recycle using a membrane bioreactor. Determination of the specific metabolic rates relative to substrates and products allowed the capacity of the yeast to metabolize malic acid under both oxidative metabolism (carbon limited cultures) and oxidofermentative metabolism (carbon sufficient cultures) situations to be characterized. Under carbon limiting conditions, the specific rate of malate utilization was dependent on the residual concentration and a limit for a purely oxidative breakdown without ethanol formation was observed for a characteristic ratio between the rates of substrate consumption qM/qG of 1.63 g.g-1. In addition, the mass balance analysis revealed the incorporation of malic acid into biomass. In carbon excess environments, the specific rate of malate utilization was dependent on both the residual malate and the specific rate of glucose consumption indicating that in addition to its conversion into ethanol malate can be respiratively metabolized for qM/qG ratios higher than 0.4 g.g-1.","authors":"Uribelarrea JL, De Queiroz JH, Pareilleux A","authors_abbrev":"Uribelarrea JL et al.","pubmed_publication_date":"Apr 1997","pubmed_entrez_date":"1997-04-01","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20040583","title":"High-throughput sequencing of retrotransposon integration provides a saturated profile of target activity in Schizosaccharomyces pombe.","citation":"Genome Res 2010 Feb;20(2):239-48","abstract":"The biological impact of transposons on the physiology of the host depends greatly on the frequency and position of integration. Previous studies of Tf1, a long terminal repeat retrotransposon in Schizosaccharomyces pombe, showed that integration occurs at the promoters of RNA polymerase II (Pol II) transcribed genes. To determine whether specific promoters are preferred targets of integration, we sequenced large numbers of insertions using high-throughput pyrosequencing. In four independent experiments we identified a total of 73,125 independent integration events. These data provided strong support for the conclusion that Pol II promoters are the targets of Tf1 integration. The size and number of the integration experiments resulted in reproducible measures of integration for each intergenic region and ORF in the S. pombe genome. The reproducibility of the integration activity from experiment to experiment demonstrates that we have saturated the full set of insertion sites that are actively targeted by Tf1. We found Tf1 integration was highly biased in favor of a specific set of Pol II promoters. The overwhelming majority (76%) of the insertions were distributed in intergenic sequences that contained 31% of the promoters of S. pombe. Interestingly, there was no correlation between the amount of integration at these promoters and their level of transcription. Instead, we found Tf1 had a strong preference for promoters that are induced by conditions of stress. This targeting of stress response genes coupled with the ability of Tf1 to regulate the expression of adjacent genes suggests Tf1 may improve the survival of S. pombe when cells are exposed to environmental stress.","doi":"10.1101/gr.099648.109","authors":"Guo Y, Levin HL","authors_abbrev":"Guo Y et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2009-12-31","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26031557","title":"Loss of kinesin-14 results in aneuploidy via kinesin-5-dependent microtubule protrusions leading to chromosome cut.","citation":"Nat Commun 2015 Jun 02;6:7322","abstract":"Aneuploidy-chromosome instability leading to incorrect chromosome number in dividing cells-can arise from defects in centrosome duplication, bipolar spindle formation, kinetochore-microtubule attachment, chromatid cohesion, mitotic checkpoint monitoring or cytokinesis. As most tumours show some degree of aneuploidy, mechanistic understanding of these pathways has been an intense area of research, to provide potential therapeutics. Here we present a mechanism for aneuploidy in fission yeast based on spindle pole microtubule defocusing by loss of kinesin-14 Pkl1, leading to kinesin-5 Cut7-dependent aberrant long spindle microtubule minus-end protrusions that push the properly segregated chromosomes to the site of cell division, resulting in chromosome cut at cytokinesis. Pkl1 localization and function at the spindle pole is mutually dependent on spindle pole-associated protein Msd1. This mechanism of aneuploidy bypasses the known spindle assembly checkpoint that monitors chromosome segregation.","doi":"10.1038/ncomms8322","authors":"Syrovatkina V, Tran PT","authors_abbrev":"Syrovatkina V et al.","pubmed_publication_date":"02 Jun 2015","pubmed_entrez_date":"2015-06-03","publication_year":"2015","canto_session_key":"59904c3249cbb80b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-05-30 17:59:13","canto_approved_date":"2022-07-11 17:51:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-05-30 17:58:21","canto_added_date":"2015-06-04 00:19:17","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":17,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC13E7.06","SPAC24H6.05","SPAC3A11.14c","SPBC20F10.06","SPAC25G10.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2022-05-30"},{"uniquename":"PMID:7908005","title":"M26 recombinational hotspot and physical conversion tract analysis in the ade6 gene of Schizosaccharomyces pombe.","citation":"Genetics 1994 Jan;136(1):41-51","abstract":"At the ade6 locus of Schizosaccharomyces pombe flanking markers have been introduced as well as five silent restriction site polymorphisms: four in the 5' upstream region and one in the middle of the gene. The mutations ade6-706, ade6-M26 (both at the 5' end) and ade6-51 (middle of the gene) were used as partners for crosses with the 3' mutation ade6-469. From these three types of crosses, wild-type recombinants were selected and analyzed genetically to assess association with crossing-over and physically to determine conversion tract lengths. The introduced restriction site polymorphisms (five vs. only one) neither influenced the pattern of recombinant types nor the distribution of conversion tracts. The hotspot mutation M26 enhances crossing-over and conversion to the same proportion. M26 not only stimulates conversion at the 5' end, but does this also (to a lower extent) at the 3' end of ade6 at a distance of more than 1 kb. The majority of meiotic conversion tracts are continuous and postmeiotic segregation of polymorphic sites is rare. Conversion tracts are slightly shorter with M26 in comparison with its control 706. The mean minimal length of tracts varies from 670 bp (M26) to 890 bp (706) to 1290 bp (51). It is concluded that M26 acts as an initiation site of recombination or enhances initiation of recombination. M26 does not act by termination of conversion. A region of recombination initiation exists at the 5' end of the ade6 gene also in the absence of the ade6-M26 hotspot mutation.","authors":"Grimm C, Bähler J, Kohli J","authors_abbrev":"Grimm C et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24452856","title":"Identification and refinement of two strong constitutive promoters for gene expression system of Schizosaccharomyces pombe.","citation":"World J Microbiol Biotechnol 2014 Jun;30(6):1809-17","abstract":"Fission yeast Schizosaccharomyces pombe shares various important properties with higher eukaryotes and is now considered a useful host for elevated production of mammalian proteins for medicinal applications. The full-length nmt1 promoter has been widely used as a strong promoter in S. pombe expression system. In the present study, the promoters of the eno101 and gpd3 genes in S. pombe were identified as strong constitutive promoters. For convenient applications in the plasmids of S. pombe, these promoters were refined to 276-bp eno and 273-bp gpd promoters by deleting undesired sequences and examining the expression of reporter genes including lacZ and xynA. Both the refined eno and gpd promoters provided approximately 1.5-fold higher expression of LacZ than nmt1 promoter. Furthermore, gene expression under the control of the eno or gpd promoter was not repressed by the components of YES medium while nmt1 promoter was inhibited by thiamine in yeast extract. Therefore, both eno and gpd promoters offer opportunities for efficient production of recombinant proteins by S. pombe in high cell-density fermentation.","doi":"10.1007/s11274-014-1603-6","authors":"Wang H, Wang H, Wang M, Zhang L, Wang R, Mei Y, Shao W","authors_abbrev":"Wang H et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-01-24","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29065217","title":"The fission yeast MAPK Spc1 senses perturbations in Cdc25 and Wee1 activities and targets Rad24 to restore this balance.","citation":"Yeast 2018 Mar;35(3):261-271","abstract":"Mitogen-activated protein kinases (MAPKs) play vital roles in multiple cellular processes and represent prominently pursued targets for development of therapeutic regimes. The MAPK Spc1 (p38 homologue) is known to be very important for both mitotic promotion and delay in Schizosaccharomyces pombe. However, the mechanism responsible for mitotic inhibition has remained elusive. Cdc25 (Cdc2 activator) and Wee1 (Cdc2 inhibtor) are important determinants of mitotic timing in all eukaryotes. Our results show that Spc1 can sense the perturbations in the balance of Cdc25 and Wee1 activities in S. pombe and that its function as a mitotic inhibitor is very important for controlling the same. An Spc1-Srk1-Rad24-dependent pathway for mitotic inhibition has been reported earlier.Here we report the presence of an alternative mechanism wherein Spc1 targets the 14-3-3 protein, Rad24, independently of Srk1, leading to relocalization of Cdc25 and mitotic inhibition. Our observations suggest that this pathway can serve as a backup mechanism for Cdc2 inactivation in the absence of Wee1.","doi":"10.1002/yea.3289","authors":"Paul M, Ghosal A, Bandyopadhyay S, G P, Selvam U, Rai N, Sundaram G","authors_abbrev":"Paul M et al.","pubmed_publication_date":"Mar 2018","pubmed_entrez_date":"2017-10-25","publication_year":"2018","canto_session_key":"bfd24f1d8129fc47","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-02-19 13:55:03","canto_approved_date":"2026-05-27 09:23:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-05-27 09:22:34","canto_added_date":"2017-10-26 00:15:16","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.22","SPBC11B10.09","SPCC1322.08","SPAC24B11.06c","SPAC24H6.05","SPCC18B5.03","SPAC8E11.02c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2020-02-19"},{"uniquename":"PMID:12034844","title":"Dominant genetic screen for cofactors that enhance antisense RNA-mediated gene silencing in fission yeast.","citation":"Nucleic Acids Res 2002 Jun 01;30(11):2546-54","abstract":"Specific gene silencing has been demonstrated in a number of organisms by the introduction of antisense RNA. Mutagenesis of host-encoded factors has begun to unravel the mechanism of several forms of RNA-mediated gene silencing and has suggested that it may have been conserved through evolution. This has led to the identification of certain host genes, which, when mutated, abrogate this phenomenon. Conversely, the identification of other factors that, when co-expressed or overexpressed, can enhance gene inhibition is equally important for both elucidating the mechanism of this process and enhancing gene silencing in recalcitrant systems. We have taken such a dominant genetic approach to identify several host-encoded factors that dramatically enhance target gene silencing when co-expressed with antisense RNA in fission yeast. The transcription factor thi1 and, surprisingly, the ATP-dependent RNA helicase ded1 were initially shown to enhance gene silencing in this system. Additionally, screening of a Schizosaccharomyces pombe cDNA library identified four novel antisense-enhancing sequences (aes factors) all of which are homologous to genes encoding proteins with natural affinities for nucleic acids. These findings demonstrate the utility of this strategy in identifying host-encoded factors that can modulate gene silencing when co-expressed with antisense RNA and possibly other forms of gene-silencing activators.","authors":"Raponi M, Arndt GM","authors_abbrev":"Raponi M et al.","pubmed_publication_date":"01 Jun 2002","pubmed_entrez_date":"2002-05-30","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35409400","title":"In Mitosis You Are Not: The NIMA Family of Kinases in  Aspergillus , Yeast, and Mammals.","citation":"Int J Mol Sci 2022 Apr 06;23(7)","abstract":"The Never in mitosis gene A (NIMA) family of serine/threonine kinases is a diverse group of protein kinases implicated in a wide variety of cellular processes, including cilia regulation, microtubule dynamics, mitotic processes, cell growth, and DNA damage response. The founding member of this family was initially identified in  Aspergillus  and was found to play important roles in mitosis and cell division. The yeast family has one member each, Fin1p in fission yeast and Kin3p in budding yeast, also with functions in mitotic processes, but, overall, these are poorly studied kinases. The mammalian family, the main focus of this review, consists of 11 members named Nek1 to Nek11. With the exception of a few members, the functions of the mammalian Neks are poorly understood but appear to be quite diverse. Like the prototypical NIMA, many members appear to play important roles in mitosis and meiosis, but their functions in the cell go well beyond these well-established activities. In this review, we explore the roles of fungal and mammalian NIMA kinases and highlight the most recent findings in the field.","doi":"10.3390/ijms23074041","authors":"Bachus S, Graves D, Fulham L, Akkerman N, Stephanson C, Shieh J, Pelka P","authors_abbrev":"Bachus S et al.","pubmed_publication_date":"06 Apr 2022","pubmed_entrez_date":"2022-04-12","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-04-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9479823","title":"Cyclin-dependent kinase inhibitors of Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Curr Top Microbiol Immunol 1998;227:1-24","abstract":"","authors":"Mendenhall MD","authors_abbrev":"Mendenhall MD","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-02-28","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10788621","title":"Rad24 is essential for proliferation of diploid cells in fission yeast.","citation":"FEBS Lett 2000 Apr 28;472(2-3):254-8","abstract":"The rad24(+) gene of Schizosaccharomyces pombe encodes a ubiquitously expressed 14-3-3 protein. We report here that Deltarad24 cells displayed a defect in diploid colony formation, although they conjugated efficiently. We found that a cumulative deletion of mei2(+) gene almost completely suppressed this defect, and demonstrated using two-hybrid analysis that Rad24 protein directly associates with Mei2 protein by recognizing Ser-438 which is a phosphorylation target of Pat1 kinase. We conclude that constitutive progression to meiosis, caused by lack of Mei2 inhibition due to the absence of Rad24 protein, is the primary cause of the proliferative deficiency observed in Deltarad24 cells.","authors":"Tanaka Y, Okuzaki D, Yabuta N, Yoneki T, Nojima H","authors_abbrev":"Tanaka Y et al.","pubmed_publication_date":"28 Apr 2000","pubmed_entrez_date":"2000-05-02","publication_year":"2000","canto_session_key":"c8cdfb930f378170","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-02 14:54:36","canto_approved_date":"2019-06-14 08:05:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-02 14:50:51","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A2.13c","SPAC8E11.02c","SPAC27D7.03c","SPBC32C12.02"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-12-02"},{"uniquename":"PMID:28202541","title":"Coordinate Regulation of Yeast Sterol Regulatory Element-binding Protein (SREBP) and Mga2 Transcription Factors.","citation":"J Biol Chem 2017 Mar 31;292(13):5311-5324","abstract":"The Mga2 and Sre1 transcription factors regulate oxygen-responsive lipid homeostasis in the fission yeast  Schizosaccharomyces pombe  in a manner analogous to the mammalian sterol regulatory element-binding protein (SREBP)-1 and SREBP-2 transcription factors. Mga2 and SREBP-1 regulate triacylglycerol and glycerophospholipid synthesis, whereas Sre1 and SREBP-2 regulate sterol synthesis. In mammals, a shared activation mechanism allows for coordinate regulation of SREBP-1 and SREBP-2. In contrast, distinct pathways activate fission yeast Mga2 and Sre1. Therefore, it is unclear whether and how these two related pathways are coordinated to maintain lipid balance in fission yeast. Previously, we showed that Sre1 cleavage is defective in the absence of  mga2  Here, we report that this defect is due to deficient unsaturated fatty acid synthesis, resulting in aberrant membrane transport. This defect is recapitulated by treatment with the fatty acid synthase inhibitor cerulenin and is rescued by addition of exogenous unsaturated fatty acids. Furthermore, sterol synthesis inhibition blocks Mga2 pathway activation. Together, these data demonstrate that Sre1 and Mga2 are each regulated by the lipid product of the other transcription factor pathway, providing a source of coordination for these two branches of lipid synthesis.","doi":"10.1074/jbc.M117.778209","authors":"Burr R, Stewart EV, Espenshade PJ","authors_abbrev":"Burr R et al.","pubmed_publication_date":"31 Mar 2017","pubmed_entrez_date":"2017-02-17","publication_year":"2017","canto_session_key":"a73f39d811302361","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2017-06-16 09:19:27","canto_approved_date":"2025-09-03 15:26:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-28 17:50:22","canto_added_date":"2017-02-18 01:15:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Peter Espenshade","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.15c","SPAC1B3.16c","SPCC1281.06c","SPAC20H4.02","SPBC354.05c","SPCC285.11","SPAC1486.02c","SPAC27F1.07","SPBC19C2.09","SPBC947.10","SPAC4D7.11","SPAC26H5.05","SPBC1734.04"],"gene_count":13,"ltp_gene_count":8,"approved_date":"2017-06-16"},{"uniquename":"PMID:23022730","title":"Convergent transcription induces transcriptional gene silencing in fission yeast and mammalian cells.","citation":"Nat Struct Mol Biol 2012 Nov;19(11):1193-201","abstract":"We show that convergent transcription induces transcriptional gene silencing (TGS) in trans for both fission yeast and mammalian cells. This method has advantages over existing strategies to induce gene silencing. Previous studies in fission yeast have characterized TGS as a cis-specific process involving RNA interference that maintains heterochromatic regions such as centromeres. In contrast, in mammalian cells, gene silencing is known to occur through a post-transcriptional mechanism that uses exogenous short interfering RNAs or endogenous microRNAs to inactivate mRNA. We now show that the introduction of convergent transcription plasmids into either Schizosaccharomyces pombe or mammalian cells allows the production of double-stranded RNA from inserted gene fragments, resulting in TGS of endogenous genes. We predict that using convergent transcription to induce gene silencing will be a generally useful strategy and allow for a fuller molecular understanding of the biology of TGS.","doi":"10.1038/nsmb.2392","authors":"Gullerova M, Proudfoot NJ","authors_abbrev":"Gullerova M et al.","pubmed_publication_date":"Nov 2012","pubmed_entrez_date":"2012-10-02","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34818062","title":"ER-localized phosphatidylethanolamine synthase plays a conserved role in lipid droplet formation.","citation":"Mol Biol Cell 2022 Jan 01;33(1):ar11","abstract":"The asymmetric distribution of phospholipids in membranes is a fundamental principle of cellular compartmentalization and organization. Phosphatidylethanolamine (PE), a nonbilayer phospholipid that contributes to organelle shape and function, is synthesized at several subcellular localizations via semiredundant pathways. Previously, we demonstrated in budding yeast that the PE synthase Psd1, which primarily operates on the mitochondrial inner membrane, is additionally targeted to the ER. While ER-localized Psd1 is required to support cellular growth in the absence of redundant pathways, its physiological function is unclear. We now demonstrate that ER-localized Psd1 sublocalizes on the ER to lipid droplet (LD) attachment sites and show it is specifically required for normal LD formation. We also find that the role of phosphatidylserine decarboxylase (PSD) enzymes in LD formation is conserved in other organisms. Thus we have identified PSD enzymes as novel regulators of LDs and demonstrate that both mitochondria and LDs in yeast are organized and shaped by the spatial positioning of a single PE synthesis enzyme.","doi":"10.1091/mbc.E21-11-0558-T","authors":"Gok MO, Speer NO, Henne WM, Friedman JR","authors_abbrev":"Gok MO et al.","pubmed_publication_date":"01 Jan 2022","pubmed_entrez_date":"2021-11-24","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25B8.03","SPBC16E9.18"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8890754","title":"Construction of vectors and a genomic library for use with his3-deficient strains of Schizosaccharomyces pombe.","citation":"Gene 1996 Oct 03;174(2):315-8","abstract":"The construction of vectors for use in Schizosaccharomyces pombe using the his3+ gene as a selectable marker is described. In addition, we report the construction of a genomic library in a his3(+)-containing shuttle vector to facilitate the cloning of genes by complementation of mutant function in strains defective for His3 activity.","authors":"Ohi R, Feoktistova A, Gould KL","authors_abbrev":"Ohi R et al.","pubmed_publication_date":"03 Oct 1996","pubmed_entrez_date":"1996-10-03","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11483497","title":"Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions.","citation":"EMBO J 2001 Aug 01;20(15):3938-46","abstract":"Modular domains mediating specific protein-protein interactions play central roles in the formation of complex regulatory networks to execute various cellular activities. Here we identify a novel domain PB1 in the budding yeast protein Bem1p, which functions in polarity establishment, and mammalian p67(phox), which activates the microbicidal phagocyte NADPH oxidase. Each of these specifically recognizes an evolutionarily conserved PC motif to interact directly with Cdc24p (an essential protein for cell polarization) and p40(phox) (a component of the signaling complex for the oxidase), respectively. Swapping the PB1 domain of Bem1p with that of p67(phox), which abolishes its interaction with Cdc24p, confers on cells temperature- sensitive growth and a bilateral mating defect. These phenotypes are suppressed by a mutant Cdc24p harboring the PC motif-containing region of p40(phox), which restores the interaction with the altered Bem1p. This domain-swapping experiment demonstrates that Bem1p function requires interaction with Cdc24p, in which the PB1 domain and the PC motif participate as responsible modules.","authors":"Ito T, Matsui Y, Ago T, Ota K, Sumimoto H","authors_abbrev":"Ito T et al.","pubmed_publication_date":"01 Aug 2001","pubmed_entrez_date":"2001-08-03","publication_year":"2001","canto_session_key":"6f86a74f47c913cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-29 15:51:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-29 15:51:11","canto_added_date":"2016-09-21 00:11:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22H10.07","SPAC16E8.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-09-29"},{"uniquename":"PMID:3442828","title":"Isolation of a novel type of mutation in the mitotic control of Schizosaccharomyces pombe whose phenotypic expression is dependent on the genetic background and nutritional environment.","citation":"Curr Genet 1986;10(7):509-14","abstract":"The major cell cycle control in the fission yeast Schizosaccharomyces pombe acts at entry to mitosis, and involves three previously identified genes cdc2, cdc25 and wee1. The presence of a wee1 mutation phenotypically suppresses cdc25 mutations. This paper describes the isolation and subsequent analysis of a strain in which the suppression is reversed by the presence of a new mutation, designated win1.1. The mutation causes a slight increase in cell size at division in most genetic backgrounds. However, when combined with a wee1 mutation and cdc25.22, the win1.1 mutation interacts strongly to generate a novel phenotype: cells are phenotypically cdc during growth on minimal medium but cdc+ when cultured on complex medium. The win1 locus is unlinked to previously identified genes involved in mitosis.","authors":"Ogden JE, Fantes PA","authors_abbrev":"Ogden JE et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_session_key":"20c49543a65c7422","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-13 15:23:20","canto_approved_date":"2021-06-14 15:18:30","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-18 17:08:30","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":40,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC1006.09","SPAC24H6.05","SPCC18B5.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-07-13"},{"uniquename":"PMID:21548894","title":"Extraction of genomic DNA from yeasts for PCR-based applications.","citation":"Biotechniques 2011 May;50(5):325-8","abstract":"We have developed a quick and low-cost genomic DNA extraction protocol from yeast cells for PCR-based applications. This method does not require any enzymes, hazardous chemicals, or extreme temperatures, and is especially powerful for simultaneous analysis of a large number of samples. DNA can be efficiently extracted from different yeast species (Kluyveromyces lactis, Hansenula polymorpha, Schizosaccharomyces pombe, Candida albicans, Pichia pastoris, and Saccharomyces cerevisiae). The protocol involves lysis of yeast colonies or cells from liquid culture in a lithium acetate (LiOAc)-SDS solution and subsequent precipitation of DNA with ethanol. Approximately 100 nanograms of total genomic DNA can be extracted from 1 × 10(7) cells. DNA extracted by this method is suitable for a variety of PCR-based applications (including colony PCR, real-time qPCR, and DNA sequencing) for amplification of DNA fragments of ≤ 3500 bp.","doi":"10.2144/000113672","authors":"Lõoke M, Kristjuhan K, Kristjuhan A","authors_abbrev":"Lõoke M et al.","pubmed_publication_date":"May 2011","pubmed_entrez_date":"2011-05-10","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37284815","title":"Impact of 1,6-hexanediol on Schizosaccharomyces pombe genome stability.","citation":"G3 (Bethesda) 2023 Aug 09;13(8)","abstract":"Phase separation is a major mechanism of macromolecular condensation within cells. A frequently chosen tool for global disruption of phase separation via weak hydrophobic interactions is treatment with 1,6-hexanediol. This study evaluates the cytotoxic and genotoxic effects of treating live fission yeast with 1,6-hexanediol. We find that 1,6-hexanediol causes a drastic decrease in cell survival and growth rate. We also see a reduction in HP1 protein foci and increase in DNA damage foci. However, there is no evidence for increased genomic instability in two classically phase-separated domains, the heterochromatic pericentromere and the nucleolar rDNA repeats. This study reveals that 1,6-hexanediol is a blunt tool for phase separation inhibition and its secondary effects must be taken into consideration during its in vivo use.","doi":"10.1093/g3journal/jkad123","authors":"Jones CE, Forsburg SL","authors_abbrev":"Jones CE et al.","pubmed_publication_date":"09 Aug 2023","pubmed_entrez_date":"2023-06-07","publication_year":"2023","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2023-06-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25639242","title":"Nitrogen regulates AMPK to control TORC1 signaling.","citation":"Curr Biol 2015 Feb 16;25(4):445-54","abstract":"Cell growth and cell-cycle progression are tightly coordinated to enable cells to adjust their size (timing of division) to the demands of proliferation in varying nutritional environments. In fission yeast, nitrogen stress results in sustained proliferation at a reduced size.\nHere, we show that cells can sense nitrogen stress to reduce target of rapamycin complex-1 (TORC1) activity. Nitrogen-stress-induced TORC1 inhibition differs from amino-acid-dependent control of TORC1 and requires the Ssp2 (AMPKα) kinase, the Tsc1/2 complex, and Rhb1 GTPase. Importantly, the β and γ regulatory subunits of AMPK are not required to control cell division in response to nitrogen stress, providing evidence for a nitrogen-sensing mechanism that is independent of changes in intracellular ATP/AMP levels. The CaMKK homolog Ssp1 is constitutively required for phosphorylation of the AMPKα(Ssp2) T loop. However, we find that a second homolog CaMKK(Ppk34) is specifically required to stimulate AMPKα(Ssp2) activation in response to nitrogen stress. Finally, ammonia also controls mTORC1 activity in human cells; mTORC1 is activated upon the addition of ammonium to glutamine-starved Hep3B cancer cells.\nThe alternative nitrogen source ammonia can simulate TORC1 activity to support growth and division under challenging nutrient settings, a situation often seen in cancer.","doi":"10.1016/j.cub.2014.12.034","authors":"Davie E, Forte GM, Petersen J","authors_abbrev":"Davie E et al.","pubmed_publication_date":"16 Feb 2015","pubmed_entrez_date":"2015-02-03","publication_year":"2015","canto_session_key":"652d207adb4776b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-13 11:28:59","canto_approved_date":"2023-03-23 13:57:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-26 11:28:14","canto_added_date":"2015-02-04 01:15:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4F11.02","SPAC2G11.07c","SPAC1556.08c","SPAC23H4.02","SPCC1919.03c","SPCC1919.01","SPCC74.03c","SPBC11B10.09","SPAC3G9.09c","SPBC428.16c","SPAC31G5.12c","SPAC22F3.13","SPCC1223.11","SPCC297.03","SPAC4A8.03c","SPAC630.13c"],"gene_count":16,"ltp_gene_count":14,"approved_date":"2016-09-13"},{"uniquename":"PMID:18493607","title":"A DNA polymerase alpha accessory protein, Mcl1, is required for propagation of centromere structures in fission yeast.","citation":"PLoS One 2008 May 21;3(5):e2221","abstract":"Specialized chromatin exists at centromeres and must be precisely transmitted during DNA replication. The mechanisms involved in the propagation of these structures remain elusive. Fission yeast centromeres are composed of two chromatin domains: the central CENP-A(Cnp1) kinetochore domain and flanking heterochromatin domains. Here we show that fission yeast Mcl1, a DNA polymerase alpha (Pol alpha) accessory protein, is critical for maintenance of centromeric chromatin. In a screen for mutants that alleviate both central domain and outer repeat silencing, we isolated several cos mutants, of which cos1 is allelic to mcl1. The mcl1-101 mutation causes reduced CENP-A(Cnp1) in the central domain and an aberrant increase in histone acetylation in both domains. These phenotypes are also observed in a mutant of swi7(+), which encodes a catalytic subunit of Pol alpha. Mcl1 forms S-phase-specific nuclear foci, which colocalize with those of PCNA and Pol alpha. These results suggest that Mcl1 and Pol alpha are required for propagation of centromere chromatin structures during DNA replication.","doi":"10.1371/journal.pone.0002221","authors":"Natsume T, Tsutsui Y, Sutani T, Dunleavy EM, Pidoux AL, Iwasaki H, Shirahige K, Allshire RC, Yamao F","authors_abbrev":"Natsume T et al.","pubmed_publication_date":"21 May 2008","pubmed_entrez_date":"2008-05-22","publication_year":"2008","canto_session_key":"cfa0410c2c949ac3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-28 06:57:04","canto_approved_date":"2025-09-04 10:22:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-18 09:26:56","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":88,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.06c","SPAC3H5.06c","SPBC800.03","SPBC16D10.04c","SPCC1672.10","SPCC290.04","SPAPB1E7.02c","SPBC16D10.07c","SPBC1105.17","SPAC1687.20c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2016-04-28"},{"uniquename":"PMID:40128540","title":"Asymmetric activation of dimeric ATM/Tel1 kinase.","citation":"Cell Discov 2025 Mar 25;11(1):30","abstract":"","doi":"10.1038/s41421-025-00786-0","authors":"Wang P, Zheng Z, Wang G, Zhao Z, Qian D, Cai G, Wang X","authors_abbrev":"Wang P et al.","pubmed_publication_date":"25 Mar 2025","pubmed_entrez_date":"2025-03-25","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC23B6.03c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"9iz0","gene_chains":[{"gene_uniquename":"SPCC23B6.03c","chain":"A/B","position":"1-2812"}],"title":"ATM/Tel1 bound to CHK2 peptide","entry_authors":"Wang P","entry_authors_abbrev":"Wang P","reference_uniquename":"PMID:40128540","experimental_method":"EM","resolution":"3.63"},{"pdb_id":"9iz7","gene_chains":[{"gene_uniquename":"SPCC23B6.03c","chain":"A","position":"1-2812"}],"title":"ATM/Tel1 in Basal state","entry_authors":"Wang P","entry_authors_abbrev":"Wang P","reference_uniquename":"PMID:40128540","experimental_method":"EM","resolution":"4.32"}]},{"uniquename":"PMID:12750522","title":"Distinct cohesin complexes organize meiotic chromosome domains.","citation":"Science 2003 May 16;300(5622):1152-5","abstract":"Meiotic cohesin complexes at centromeres behave differently from those along chromosome arms, but the basis for these differences has remained elusive. The fission yeast cohesin molecule Rec8 largely replaces its mitotic counterpart, Rad21/Scc1, along the entire chromosome during meiosis. Here we show that Rec8 complexes along chromosome arms contain Rec11, whereas those in the vicinity of centromeres have a different partner subunit, Psc3. The arm associated Rec8-Rec11 complexes are critical for meiotic recombination. The Rec8-Psc3 complexes comprise two different types of assemblies. First, pericentromeric Rec8-Psc3 complexes depend on histone methylation-directed heterochromatin for their localization and are required for cohesion during meiosis II. Second, central core Rec8-Psc3 complexes form independently of heterochromatin and are presumably required for establishing monopolar attachment at meiosis I. These findings define distinct modes of assembly and functions for cohesin complexes at different regions along chromosomes.","authors":"Kitajima TS, Yokobayashi S, Yamamoto M, Watanabe Y","authors_abbrev":"Kitajima TS et al.","pubmed_publication_date":"16 May 2003","pubmed_entrez_date":"2003-05-17","publication_year":"2003","canto_session_key":"53fad494a10fe0a6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-11-21 15:13:18","canto_approved_date":"2025-09-02 16:32:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-21 14:10:45","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":41,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPAC10F6.09c","SPAC17A5.11","SPAC664.01c","SPCC4E9.01c","SPBC428.08c","SPAC17H9.20"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2024-11-21"},{"uniquename":"PMID:24709818","title":"LaSSO, a strategy for genome-wide mapping of intronic lariats and branch points using RNA-seq.","citation":"Genome Res 2014 Jul;24(7):1169-79","abstract":"Both canonical and alternative splicing of RNAs are governed by intronic sequence elements and produce transient lariat structures fastened by branch points within introns. To map precisely the location of branch points on a genomic scale, we developed LaSSO (Lariat Sequence Site Origin), a data-driven algorithm which utilizes RNA-seq data. Using fission yeast cells lacking the debranching enzyme Dbr1, LaSSO not only accurately identified canonical splicing events, but also pinpointed novel, but rare, exon-skipping events, which may reflect aberrantly spliced transcripts. Compromised intron turnover perturbed gene regulation at multiple levels, including splicing and protein translation. Notably, Dbr1 function was also critical for the expression of mitochondrial genes and for the processing of self-spliced mitochondrial introns. LaSSO showed better sensitivity and accuracy than algorithms used for computational branch-point prediction or for empirical branch-point determination. Even when applied to a human data set acquired in the presence of debranching activity, LaSSO identified both canonical and exon-skipping branch points. LaSSO thus provides an effective approach for defining high-resolution maps of branch-site sequences and intronic elements on a genomic scale. LaSSO should be useful to validate introns and uncover branch-point sequences in any eukaryote, and it could be integrated into RNA-seq pipelines.","doi":"10.1101/gr.166819.113","authors":"Bitton DA, Rallis C, Jeffares DC, Smith GC, Chen YY, Codlin S, Marguerat S, Bähler J","authors_abbrev":"Bitton DA et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-04-09","publication_year":"2014","canto_session_key":"5ef2251d810b470b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-03-11 17:49:16","canto_approved_date":"2020-03-11 17:49:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-11 17:49:09","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2020-03-11"},{"uniquename":"PMID:19020097","title":"Selective benefits of damage partitioning in unicellular systems and its effects on aging.","citation":"Proc Natl Acad Sci U S A 2008 Dec 02;105(48):18764-9","abstract":"Cytokinesis in unicellular organisms sometimes entails a division of labor between cells leading to lineage-specific aging. To investigate the potential benefits of asymmetrical cytokinesis, we created a mathematical model to simulate the robustness and fitness of dividing systems displaying different degrees of damage segregation and size asymmetries. The model suggests that systems dividing asymmetrically (size-wise) or displaying damage segregation can withstand higher degrees of damage before entering clonal senescence. When considering population fitness, a system producing different-sized progeny like budding yeast is predicted to benefit from damage retention only at high damage propagation rates. In contrast, the fitness of a system of equal-sized progeny is enhanced by damage segregation regardless of damage propagation rates, suggesting that damage partitioning may also provide an evolutionary advantage in systems dividing by binary fission. Indeed, by using Schizosaccharomyces pombe as a model, we experimentally demonstrate that damaged proteins are unevenly partitioned during cytokinesis and the damage-enriched sibling suffers from a prolonged generation time and accelerated aging. This damage retention in S. pombe is, like in Saccharomyces cerevisiae, Sir2p- and cytoskeleton-dependent, suggesting this to be an evolutionarily conserved mechanism. We suggest that sibling-specific aging may be a result of the strong selective advantage of damage segregation, which may be more common in nature than previously anticipated.","doi":"10.1073/pnas.0804550105","authors":"Erjavec N, Cvijovic M, Klipp E, Nyström T","authors_abbrev":"Erjavec N et al.","pubmed_publication_date":"02 Dec 2008","pubmed_entrez_date":"2008-11-21","publication_year":"2008","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12193658","title":"Histone H3 lysine 4 methylation is mediated by Set1 and promotes maintenance of active chromatin states in fission yeast.","citation":"Proc Natl Acad Sci U S A 2002 Dec 10;99 Suppl 4(Suppl 4):16438-45","abstract":"Methylation of histone H3 at lysine 4 (H3 Lys-4) or lysine 9 (H3 Lys-9) is known to define active and silent chromosomal domains respectively from fission yeast to humans. However, in budding yeast, H3 Lys-4 methylation is also necessary for silent chromatin assembly at telomeres and ribosomal DNA. Here we demonstrate that deletion of set1, which encodes a protein containing an RNA recognition motif at its amino terminus and a SET domain at the carboxy terminus, abolishes H3 Lys-4 methylation in fission yeast. Unlike in budding yeast, Set1-mediated H3 Lys-4 methylation is not required for heterochromatin assembly at the silent mating-type region and centromeres in fission yeast. Our analysis suggests that H3 Lys-4 methylation is a stable histone modification present throughout the cell cycle, including mitosis. The loss of H3 Lys-4 methylation in set1Delta cells is correlated with a decrease in histone H3 acetylation levels, suggesting a mechanistic link between H3 Lys-4 methylation and acetylation of the H3 tail. We suggest that methylation of H3 Lys-4 primarily acts in the maintenance of transcriptionally poised euchromatic domains, and that this modification is dispensable for heterochromatin formation in fission yeast, which instead utilizes H3 Lys-9 methylation.","authors":"Noma K, Grewal SI","authors_abbrev":"Noma K et al.","pubmed_publication_date":"10 Dec 2002","pubmed_entrez_date":"2002-08-24","publication_year":"2002","canto_session_key":"5d56484ae06b3498","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-04 10:33:42","canto_approved_date":"2024-06-21 16:27:07","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-03-04 10:31:21","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.05c","SPBC800.03","SPAC664.01c","SPCC306.04c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2016-03-04"},{"uniquename":"PMID:2146164","title":"Heat shock induces enzymes of trehalose metabolism, trehalose accumulation, and thermotolerance in Schizosaccharomyces pombe, even in the presence of cycloheximide.","citation":"FEBS Lett 1990 Oct 29;273(1-2):107-10","abstract":"Exponentially growing cells of the fission yeast, Schizosaccharomyces pombe, contained virtually no trehalose at 27 degrees C but rapidly accumulated large quantities during heat shock at 40 degrees C. Activities of trehalose-6-phosphate synthase and trehalase also increased upon heat shock. Thermotolerance of the cells, measured as survival at 52 degrees C, increased in parallel to trehalose accumulation and decreased in parallel to the trehalose levels when cells were shifted back to 27 degrees C. Trehalose levels, activities of enzymes of trehalose metabolism and thermotolerance strongly increased upon heat shock even in the presence of cycloheximide, indicating that none of these effects requires protein synthesis. The data support the hypothesis that trehalose acts as a thermoprotectant in Schizosaccharomyces pombe.","authors":"De Virgilio C, Simmen U, Hottiger T, Boller T, Wiemken A","authors_abbrev":"De Virgilio C et al.","pubmed_publication_date":"29 Oct 1990","pubmed_entrez_date":"1990-10-29","publication_year":"1990","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35942733","title":"Iterative bicluster-based Bayesian principal component analysis and least squares for missing-value imputation in microarray and RNA-sequencing data.","citation":"Math Biosci Eng 2022 Jun 16;19(9):8741-8759","abstract":"Microarray and RNA-sequencing (RNA-seq) techniques each produce gene expression data that can be expressed as a matrix that often contains missing values. Thus, a process of missing-value imputation that uses coherence information of the dataset is necessary. Existing imputation methods, such as iterative bicluster-based least squares (bi-iLS), use biclustering to estimate the missing values because genes are only similar under correlative experimental conditions. Also, they use the row average to obtain a temporary complete matrix, but the use of the row average is considered to be a flaw. The row average cannot reflect the real structure of the dataset because the row average only uses the information of an individual row. Therefore, we propose the use of Bayesian principal component analysis (BPCA) to obtain the temporary complete matrix instead of using the row average in bi-iLS. This alteration produces new missing values imputation method called iterative bicluster-based Bayesian principal component analysis and least squares (bi-BPCA-iLS). Several experiments have been conducted on two-dimension independent gene expression datasets, which are microarray (e.g., cell-cycle expression dataset of yeast saccharomyces cerevisiae) and RNA-seq (gene expression data from schizosaccharomyces pombe) datasets. In the case of the microarray dataset, our proposed bi-BPCA-iLS method showed a significant overall improvement in the normalized root mean square error (NRMSE) values of 10.6% from the local least squares (LLS) and 0.6% from the bi-iLS. In the case of the RNA-seq dataset, our proposed bi-BPCA-iLS method showed an overall improvement in the NRMSE values of 8.2% from the LLS and 3.1% from the bi-iLS. The additional computational time of bi-BPCA-iLS is not significant compared to bi-iLS.","doi":"10.3934/mbe.2022405","authors":"Soemartojo SM, Siswantining T, Fernando Y, Sarwinda D, Al-Ash HS, Syarofina S, Saputra N","authors_abbrev":"Soemartojo SM et al.","pubmed_publication_date":"16 Jun 2022","pubmed_entrez_date":"2022-08-09","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-08-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012703","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17875412","title":"Control of cell cycle in response to osmostress: lessons from yeast.","citation":"Methods Enzymol 2007;428:63-76","abstract":"To maximize the probability of survival and proliferation, cells coordinate various intracellular activities in response to changes in the extracellular environment. Eukaryotic cells transduce diverse cellular stimuli by multiple mitogen-activated protein kinase (MAPK) cascades. Exposure of cells to stress results in rapid activation of a highly conserved family of MAPKs, known as stress-activated protein kinases (SAPKs). Activation of SAPKs results in the generation of a set of adaptive responses that leads to the modulation of several aspects of cell physiology essential for cell survival, such as gene expression, translation, and morphogenesis. This chapter proposes that regulation of cell cycle progression is another general stress response critical for cell survival. Studies from yeast, both Schizosaccharomyces pombe and Saccharomyces cerevisiae, have served to start understanding how SAPKs control cell cycle progression in response to stress.","authors":"Clotet J, Posas F","authors_abbrev":"Clotet J et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-09-19","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19307292","title":"The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn2+ and Mn2+ in the active site.","citation":"RNA 2009 May;15(5):850-61","abstract":"In eukaryotic organisms, initiation of mRNA turnover is controlled by progressive shortening of the poly-A tail, a process involving the mega-Dalton Ccr4-Not complex and its two associated 3'-5' exonucleases, Ccr4p and Pop2p (Caf1p). RNA degradation by the 3'-5' DEDDh exonuclease, Pop2p, is governed by the classical two metal ion mechanism traditionally assumed to be dependent on Mg(2+) ions bound in the active site. Here, we show biochemically and structurally that fission yeast (Schizosaccharomyces pombe) Pop2p prefers Mn(2+) and Zn(2+) over Mg(2+) at the concentrations of the ions found inside cells and that the identity of the ions in the active site affects the activity of the enzyme. Ion replacement experiments further suggest that mRNA deadenylation could be subtly regulated by local Zn(2+) levels in the cell. Finally, we use site-directed mutagenesis to propose a mechanistic model for the basis of the preference for poly-A sequences exhibited by the Pop2p-type deadenylases as well as their distributive enzymatic behavior.","doi":"10.1261/rna.1489409","authors":"Andersen KR, Jonstrup AT, Van LB, Brodersen DE","authors_abbrev":"Andersen KR et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-03-25","publication_year":"2009","canto_session_key":"58a1d507d7511f93","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-28 13:08:09","canto_approved_date":"2026-03-17 08:50:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-26 09:46:29","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-28","pdb_entries":[{"pdb_id":"3g0z","gene_chains":[{"gene_uniquename":"SPCC18.06c","chain":"A","position":"4-335"}],"title":"Structure of S. pombe Pop2p - Zn2+ and Mn2+ bound form","entry_authors":"Andersen KR,Jonstrup AT,Van LB,Brodersen DE","entry_authors_abbrev":"Andersen KR et al.","reference_uniquename":"PMID:19307292","experimental_method":"X-ray","resolution":"2.004"},{"pdb_id":"3g10","gene_chains":[{"gene_uniquename":"SPCC18.06c","chain":"A","position":"4-335"}],"title":"Structure of S. pombe Pop2p - Mg2+ and Mn2+ bound form","entry_authors":"Andersen KR,Jonstrup AT,Van LB,Brodersen DE","entry_authors_abbrev":"Andersen KR et al.","reference_uniquename":"PMID:19307292","experimental_method":"X-ray","resolution":"2.597"}]},{"uniquename":"PMID:19879140","title":"The fission yeast TACC protein Mia1p stabilizes microtubule arrays by length-independent crosslinking.","citation":"Curr Biol 2009 Nov 17;19(21):1861-8","abstract":"Microtubule (MT) arrays are mechanistic effectors of polarity specification and cell division. Linear bundles in which MTs are bridged laterally are dynamically assembled in systems ranging from differentiated metazoan cells to fungi in a process that remains poorly understood. Often, bundled MTs slide with respect to each other via molecular motors. In interphase cells of the fission yeast Schizosaccharomyces pombe, MT nucleation frequently occurs at preexisting arrays. As the nascent MT lengthens, stable antiparallel MT overlaps are thought to form through competition between motion of the minus-end-directed kinesin Klp2p and braking force exerted by the accumulating lateral crosslinker Ase1p. Here we show that Mia1p/Alp7p, a transforming acidic coiled-coil (TACC) protein, functions as a length-independent MT crosslinker. In cells lacking Mia1p MT-bundling activity, linear arrays frequently disassemble, accompanied by a marked increase in Ase1p off rate and erratic motion of sliding MTs. We propose that the combined action of lateral length-dependent (Ase1p) and terminal length-independent (Mia1p) crosslinkers is crucial for robust assembly and stability of linear MT arrays. Such use of qualitatively distinct crosslinking mechanisms in tandem may point to a general design principle in the engineering of stable cytoskeletal assemblies.","doi":"10.1016/j.cub.2009.09.063","authors":"Thadani R, Ling YC, Oliferenko S","authors_abbrev":"Thadani R et al.","pubmed_publication_date":"17 Nov 2009","pubmed_entrez_date":"2009-11-03","publication_year":"2009","canto_session_key":"b5faa30667b9677e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-07-14 08:09:56","canto_approved_date":"2022-07-14 08:09:56","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-07-14 08:09:48","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":13,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC890.02c","SPAPB1A10.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-07-14"},{"uniquename":"PMID:32332728","title":"Nitrogen starvation reveals the mitotic potential of mutants in the S/MAPK pathways.","citation":"Nat Commun 2020 Apr 24;11(1):1973","abstract":"The genetics of quiescence is an emerging field compared to that of growth, yet both states generate spontaneous mutations and genetic diversity fueling evolution. Reconciling mutation rates in dividing conditions and mutation accumulation as a function of time in non-dividing situations remains a challenge. Nitrogen-starved fission yeast cells reversibly arrest proliferation, are metabolically active and highly resistant to a variety of stresses. Here, we show that mutations in stress- and mitogen-activated protein kinase (S/MAPK) signaling pathways are enriched in aging cultures. Targeted resequencing and competition experiments indicate that these mutants arise in the first month of quiescence and expand clonally during the second month at the expense of the parental population. Reconstitution experiments show that S/MAPK modules mediate the sacrifice of many cells for the benefit of some mutants. These findings suggest that non-dividing conditions promote genetic diversity to generate a social cellular environment prone to kin selection.","doi":"10.1038/s41467-020-15880-y","authors":"Makarenko R, Denis C, Francesconi S, Gangloff S, Arcangioli B","authors_abbrev":"Makarenko R et al.","pubmed_publication_date":"24 Apr 2020","pubmed_entrez_date":"2020-04-26","publication_year":"2020","canto_session_key":"c130fb9f5e62c0bc","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-04-27 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8286404","title":"Molecular cloning and nucleotide sequencing of Schizosaccharomyces pombe homologue of the class II fructose-1,6-bisphosphate aldolase gene.","citation":"Biochim Biophys Acta 1994 Jan 04;1183(3):550-2","abstract":"DNA fragment containing Schizosaccharomyces pombe homologue of the class II fructose-1,6-bisphosphate aldolase gene was cloned and sequenced. A long open reading frame, which encodes a polypeptide of 358 amino acid residues, was found in the sequence. Amino acid sequence deduced from the nucleotide sequence is 63% homologous to the amino acid sequence of the enzyme of Saccharomyces cerevisiae. Northern blot analysis revealed that 1.3 kb poly(A)+ RNA is transcribed from this DNA sequence.","authors":"Mutoh N, Hayashi Y","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"04 Jan 1994","pubmed_entrez_date":"1994-01-04","publication_year":"1994","canto_session_key":"6592972c5ed4692c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-06-12 12:58:13","canto_session_submitted_date":"2012-05-25 15:33:57","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-05-25"},{"uniquename":"PMID:3428262","title":"Interaction between cdc13+ and cdc2+ in the control of mitosis in fission yeast; dissociation of the G1 and G2 roles of the cdc2+ protein kinase.","citation":"EMBO J 1987 Nov;6(11):3441-7","abstract":"A cold-sensitive (cs) allele of cdc2, a gene that acts in both the G1 and G2 phases of the fission yeast cell cycle, has been isolated by classical mutagenesis. Further mutagenesis of a cdc2cs strain yielded an extragenic suppressor that rescued the cs cell cycle defect but simultaneously conferred a temperature-sensitive (ts) cdc phenotype. This suppressor mutation was shown to be an allele of cdc13, a previously identified gene. A variety of allele-specific interactions between cdc2 and cdc13 were discovered. These included suppression of cdc13ts alleles by introduction of the cdc2+ gene on a multi-copy plasmid vector. cdc13+ is required in G2 for mitotic initiation and was shown to play no role in the G1 phase of the cell cycle. cdc2+, however, is essential in G1 for DNA replication and in G2 for mitosis. The newly isolated cs allele of cdc2 that is rescued by a ts allele of cdc13 is defective only in its G2 function. cdc13+ cooperates with cdc2+ in the initiation of mitosis but not in the regulation of DNA replication. We propose that the cdc13+ gene product might be a G2-specific substrate of the cdc2+ protein kinase.","authors":"Booher R, Beach D","authors_abbrev":"Booher R et al.","pubmed_publication_date":"Nov 1987","pubmed_entrez_date":"1987-11-01","publication_year":"1987","canto_session_key":"be37fa1a04795ddd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-04-04 07:58:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-24 12:09:25","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-24"},{"uniquename":"PMID:20301539","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1604.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8298192","title":"Function of the ypt2 gene in the exocytic pathway of Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1993 Oct;4(10):1069-76","abstract":"The ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the ypt/rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian rab8. We have introduced a mutation into the gene corresponding to a mutation identified in ypt1, in which a conserved valine residue was altered to asparagine. The mutated ypt2 gene was introduced into the S. pombe genome by gene replacement. The resulting strain was temperature-sensitive for growth. Normal growth was restored by introduction of a plasmid-borne wild-type ypt2 cDNA or by cDNA for rab8 but not by various other rab or ypt sequences. At restrictive temperature the mutant cells accumulated the secretory protein acid phosphatase in a form that appeared to be fully glycosylated and acquired a population of vesicles detectable by electron microscopy. Thus the ypt2 protein, and by inference rab8, appear to function in the last stage of the secretory pathway.","authors":"Craighead MW, Bowden S, Watson R, Armstrong J","authors_abbrev":"Craighead MW et al.","pubmed_publication_date":"Oct 1993","pubmed_entrez_date":"1993-10-01","publication_year":"1993","canto_session_key":"e5679fed14e6512c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-22 08:32:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-22 08:31:54","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-22"},{"uniquename":"PMID:9802907","title":"Dynamics of centromeres during metaphase-anaphase transition in fission yeast: Dis1 is implicated in force balance in metaphase bipolar spindle.","citation":"Mol Biol Cell 1998 Nov;9(11):3211-25","abstract":"In higher eukaryotic cells, the spindle forms along with chromosome condensation in mitotic prophase. In metaphase, chromosomes are aligned on the spindle with sister kinetochores facing toward the opposite poles. In anaphase A, sister chromatids separate from each other without spindle extension, whereas spindle elongation takes place during anaphase B. We have critically examined whether such mitotic stages also occur in a lower eukaryote, Schizosaccharomyces pombe. Using the green fluorescent protein tagging technique, early mitotic to late anaphase events were observed in living fission yeast cells. S. pombe has three phases in spindle dynamics, spindle formation (phase 1), constant spindle length (phase 2), and spindle extension (phase 3). Sister centromere separation (anaphase A) rapidly occurred at the end of phase 2. The centromere showed dynamic movements throughout phase 2 as it moved back and forth and was transiently split in two before its separation, suggesting that the centromere was positioned in a bioriented manner toward the poles at metaphase. Microtubule-associating Dis1 was required for the occurrence of constant spindle length and centromere movement in phase 2. Normal transition from phase 2 to 3 needed DNA topoisomerase II and Cut1 but not Cut14. The duration of each phase was highly dependent on temperature.","authors":"Nabeshima K, Nakagawa T, Straight AF, Murray A, Chikashige Y, Yamashita YM, Hiraoka Y, Yanagida M","authors_abbrev":"Nabeshima K et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1998-11-05","publication_year":"1998","canto_session_key":"41f753fbed9bec67","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-08-08 07:26:41","canto_approved_date":"2021-12-20 13:37:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-28 15:07:25","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.06c","SPCC5E4.04","SPBC12D12.01","SPCC736.14","SPBC1A4.03c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-08-08"},{"uniquename":"PMID:31442344","title":"Heme acquisition by Shu1 requires Nbr1 and proteins of the ESCRT complex in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2019 Nov;112(5):1499-1518","abstract":"Assimilation of heme is mediated by the cell surface protein Shu1 in Schizosaccharomyces pombe. Shu1 undergoes internalization from the cell surface to the vacuole in response to high concentrations of hemin. Here, we have identified cellular components that are involved in mediating vacuolar targeting of Shu1. Cells deficient in heme biosynthesis and lacking the polyubiquitin gene ubi4 +  exhibit poor growth in the presence of exogenous hemin as a sole source of heme. Microscopic analyses of hem1Δ shu1Δ ubi4Δ cells expressing a functional HA 4  -tagged Shu1 show that Shu1 localizes to the cell surface. Ubiquitinated Nbr1 functions as a receptor for the endosomal sorting complexes required for transport (ESCRT) that delivers cargos to the vacuole. Inactivation of nbr1 +  , ESCRT-0 hse1 +  or ESCRT-I sst6 +  results in hem1Δ cells being unable to use exogenous hemin for the growth. Using lysate preparations from hemin-treated cells, Shu1-Nbr1 and Shu1-Hse1 complexes are detected by coimmunoprecipitation experiments. Further analysis by immunofluorescence microscopy shows that Shu1 is unable to reach vacuoles of hemin-treated cells harboring a deletion for one of the following genes: ubi4 +  , nbr1 +  , hse1 +  and sst6 +  . Together, these results reveal that hemin-mediated vacuolar targeting of Shu1 requires Ubi4-dependent ubiquitination, the receptor Nbr1 and the ESCRT proteins Hse1 and Sst6.","doi":"10.1111/mmi.14374","authors":"Mourer T, Brault A, Labbé S","authors_abbrev":"Mourer T et al.","pubmed_publication_date":"Nov 2019","pubmed_entrez_date":"2019-08-24","publication_year":"2019","canto_session_key":"eb200bf258521e43","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-08-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10567352","title":"Complementation analysis in PtdInsP kinase-deficient yeast mutants demonstrates that Schizosaccharomyces pombe and murine Fab1p homologues are phosphatidylinositol 3-phosphate 5-kinases.","citation":"J Biol Chem 1999 Nov 26;274(48):33905-12","abstract":"Phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P(2)) is widespread in eukaryotic cells. In Saccharomyces cerevisiae, PtdIns(3,5)P(2) synthesis is catalyzed by the PtdIns3P 5-kinase Fab1p, and loss of this activity results in vacuolar morphological defects, indicating that PtdIns(3,5)P(2) is essential for vacuole homeostasis. We have therefore suggested that all Fab1p homologues may be PtdIns3P 5-kinases involved in membrane trafficking. It is unclear which phosphatidylinositol phosphate kinases (PIPkins) are responsible for PtdIns(3,5)P(2) synthesis in higher eukaryotes. To clarify how PtdIns(3,5)P(2) is synthesized in mammalian and other cells, we determined whether yeast and mammalian Fab1p homologues or mammalian Type I PIPkins (PtdIns4P 5-kinases) make PtdIns(3,5)P(2) in vivo. The recently cloned murine (p235) and Schizosaccharomyces pombe FAB1 homologues both restored basal PtdIns(3,5)P(2) synthesis in Deltafab1 cells and made PtdIns(3,5)P(2) in vitro. Only p235 corrected the growth and vacuolar defects of fab1 S. cerevisiae. A mammalian Type I PIPkin supported no PtdIns(3,5)P(2) synthesis. Thus, FAB1 and its homologues constitute a distinct class of Type III PIPkins dedicated to PtdIns(3,5)P(2) synthesis. The differential abilities of p235 and of SpFab1p to complement the phenotypic defects of Deltafab1 cells suggests that interaction(s) with other protein factors may be important for spatial and/or temporal regulation of PtdIns(3,5)P(2) synthesis. These results also suggest that p235 may regulate a step in membrane trafficking in mammalian cells that is analogous to its function in yeast.","authors":"McEwen RK, Dove SK, Cooke FT, Painter GF, Holmes AB, Shisheva A, Ohya Y, Parker PJ, Michell RH","authors_abbrev":"McEwen RK et al.","pubmed_publication_date":"26 Nov 1999","pubmed_entrez_date":"1999-11-24","publication_year":"1999","canto_session_key":"b602005716acb06e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-06-21 15:48:10","canto_session_submitted_date":"2012-04-25 07:51:08","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3E7.01"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-04-25"},{"uniquename":"PMID:18503029","title":"Identification of twenty-three mutations in fission yeast Scap that constitutively activate SREBP.","citation":"J Lipid Res 2008 Sep;49(9):2001-12","abstract":"The endoplasmic reticulum membrane protein SREBP cleavage-activating protein (Scap) senses sterols and regulates activation of sterol-regulatory element binding proteins (SREBPs), membrane-bound transcription factors that control lipid homeostasis in fission yeast and mammals. Transmembrane segments 2-6 of Scap function as a sterol-sensing domain (SSD) that recognizes changes in cellular sterols and facilitates activation of SREBP. Previous studies identified conserved mutations Y298C, L315F, and D443N in the SSD of mammalian Scap and fission yeast Scap (Scp1) that render cells insensitive to sterols and cause constitutive SREBP activation. In this study, we utilized fission yeast genetics to identify additional functionally important residues in the SSD of Scp1 and Scap. Using a site-directed mutagenesis selection, we sampled all possible amino acid substitutions at 50 conserved residues in the SSD of Scp1 for their effects on yeast SREBP (Sre1) activation. We found mutations at 23 different amino acids in Scp1 that rendered Scp1 insensitive to sterols and caused constitutive activation of Sre1. To our surprise, the majority of the homologous Scap mutants displayed wild-type function, and only one mutation, V439G, caused constitutive activation of SREBP in mammals. These results suggest that the sterol-sensing mechanism of Scap and the functional requirements for SREBP activation are different between fission yeast and mammals.","doi":"10.1194/jlr.M800207-JLR200","authors":"Hughes AL, Stewart EV, Espenshade PJ","authors_abbrev":"Hughes AL et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-05-27","publication_year":"2008","canto_session_key":"4b6ca64fc3a8be26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-03-09 15:57:10","canto_approved_date":"2018-03-09 15:57:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-03-09 15:57:04","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_18503029_phaf.tsv"}],"genes":["SPBC3B9.15c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-03-09"},{"uniquename":"PMID:16049013","title":"Regulation of Cdc2p and Cdc13p is required for cell cycle arrest induced by defective RNA splicing in fission yeast.","citation":"J Biol Chem 2005 Sep 23;280(38):32640-8","abstract":"Screening of cdc mutants of fission yeast for those whose cell cycle arrest is independent of the DNA damage checkpoint identified the RNA splicing-deficient cdc28 mutant. A search for mutants of cdc28 cells that enter mitosis with unspliced RNA resulted in the identification of an orb5 point mutant. The orb5+ gene, which encodes a catalytic subunit of casein kinase II, was found to be required for cell cycle arrest in other mutants with defective RNA metabolism but not for operation of the DNA replication or DNA damage checkpoints. Loss of function of wee1+ or rad24+ also suppressed the arrest of several splicing mutants. Overexpression of the major B-type cyclin Cdc13p induced cdc28 cells to enter mitosis. The abundance of Cdc13p was reduced, and the phosphorylation of Cdc2p on tyrosine 15 was maintained in splicing-defective cells. These results suggest that regulation of Cdc13p and Cdc2p is required for G2 arrest in splicing mutants.","authors":"Shimada M, Namikawa-Yamada C, Nakanishi M, Murakami H","authors_abbrev":"Shimada M et al.","pubmed_publication_date":"23 Sep 2005","pubmed_entrez_date":"2005-07-29","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC19C2.01","SPAPJ698.03c","SPAC8E11.02c","SPBC582.03","SPAC23C11.11","SPAC17A5.02c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:12825973","title":"[Mechanisms of degradation of the fungal ornithine decarboxylase].","citation":"Rev Iberoam Micol 2003 Mar;20(1):1-5","abstract":"Ornithine decarboxylase (ODC) is the first enzyme in polyamine biosynthesis in numerous living organisms, from bacteria to mammalian cells. Its control is under negative feedback regulation by the end products of the pathway. In dimorphic fungi, ODC activity and therefore polyamine concentrations are related to the morphogenetic process. From the fission yeast Schizosaccharomyces pombe to human, polyamines induce antizyme synthesis which in turn inactivates ODC. This is hydrolyzed by the 26S proteasome without ubiquitination. The regulatory mechanism of antizyme on polyamines is conserved, although to date no antizyme homology has been identified in some fungal species. The components that are responsible for regulating polyamine levels in cells and the current knowledge of ODC regulation in dimorphic fungi are presented in this review. ODC degradation is of particular interest because inhibitors of this pathway may lead to the discovery of novel antifungal drugs.","authors":"Sorais F, Niño-Vega G, San-Blas G","authors_abbrev":"Sorais F et al.","pubmed_publication_date":"Mar 2003","pubmed_entrez_date":"2003-06-27","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17308036","title":"The p21-activated protein kinase inhibitor Skb15 and its budding yeast homologue are 60S ribosome assembly factors.","citation":"Mol Cell Biol 2007 Apr;27(8):2897-909","abstract":"Ribosome biogenesis is driven by a large number of preribosomal factors that associate with and dissociate from the preribosomal particles along the maturation pathway. We have previously shown that budding yeast Mak11, whose homologues in other eukaryotes were described as modulating a p21-activated protein kinase function, accumulates in Rlp24-associated pre-60S complexes when their maturation is impeded in Saccharomyces cerevisiae. The functional inactivation of WD40 repeat protein Mak11 interfered with the 60S rRNA maturation, led to a cell cycle delay in G(1), and blocked green fluorescent protein-tagged Rpl25 in the nucleoli of yeast cells, indicating an early role of Mak11 in ribosome assembly. Surprisingly, Mak11 inactivation also led to a dramatic destabilization of Rlp24. The suppression of the thermosensitive phenotype of a mak11 mutant by RLP24 overexpression and a direct in vitro interaction between Rlp24 and Mak11 suggest that Mak11 acts as an Rlp24 cofactor during early steps of 60S ribosomal subunit assembly. Moreover, we found that Skb15, the Mak11 homologue in Schizosaccharomyces pombe, also associated with preribosomes and affected 60S biogenesis in fission yeast. It is thus likely that the previously observed phenotypes for MAK11 homologues in other eukaryotes are secondary to the main function of these proteins in ribosome formation.","authors":"Saveanu C, Rousselle JC, Lenormand P, Namane A, Jacquier A, Fromont-Racine M","authors_abbrev":"Saveanu C et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-02-20","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16C4.08c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:32392819","title":"How Essential Kinesin-5 Becomes Non-Essential in Fission Yeast: Force Balance and Microtubule Dynamics Matter.","citation":"Cells 2020 May 07;9(5)","abstract":"The bipolar mitotic spindle drives accurate chromosome segregation by capturing the kinetochore and pulling each set of sister chromatids to the opposite poles. In this review, we describe recent findings on the multiple pathways leading to bipolar spindle formation in fission yeast and discuss these results from a broader perspective. The roles of three mitotic kinesins (Kinesin-5, Kinesin-6 and Kinesin-14) in spindle assembly are depicted, and how a group of microtubule-associated proteins, sister chromatid cohesion and the kinetochore collaborate with these motors is shown. We have paid special attention to the molecular pathways that render otherwise essential Kinesin-5 to become non-essential: how cells build bipolar mitotic spindles without the need for Kinesin-5 and where the alternate forces come from are considered. We highlight the force balance for bipolar spindle assembly and explain how outward and inward forces are generated by various ways, in which the proper fine-tuning of microtubule dynamics plays a crucial role. Overall, these new pathways have illuminated the remarkable plasticity and adaptability of spindle mechanics. Kinesin molecules are regarded as prospective targets for cancer chemotherapy and many specific inhibitors have been developed. However, several hurdles have arisen against their clinical implementation. This review provides insight into possible strategies to overcome these challenges.","doi":"10.3390/cells9051154","authors":"Yukawa M, Teratani Y, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"07 May 2020","pubmed_entrez_date":"2020-05-13","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-05-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18079165","title":"Expression of a novel 90-kDa protein, Lsd90, involved in the metabolism of very long-chain fatty acid-containing phospholipids in a mitosis-defective fission yeast mutant.","citation":"J Biochem 2008 Mar;143(3):369-75","abstract":"The fission yeast lsd1/fas2 strain carries a temperature-sensitive mutation of the fatty-acid-synthase alpha-subunit, exhibiting an aberrant mitosis lsd phenotype, with accumulation of very-long-chain fatty-acid-containing phospholipid (VLCFA-PL). A novel 90-kDa protein, Lsd90 (SPBC16E9.16c), was found to be newly expressed in small particle-like structures in lsd1/fas2 cells under restrictive conditions. Two mismatches leading to a double frame shift were found between the sequences of the lsd90(+) gene registered in the genomic database and the sequences determined experimentally at the amino acid, cDNA and genomic DNA levels. Unexpectedly, overexpression and disruption of the lsd90(+) gene in either lsd1/fas2 or wild-type cells did not affect either cell growth or expression of the lsd phenotype. The amounts of VLCFA-PL that accumulated in lsd90-overexpressing lsd1/fas2 cells were significantly lower than those in lsd1/fas2 cells, suggesting the involvement of Lsd90 in the metabolism of VLCFA-PL.","authors":"Yokoyama K, Nakagawa M, Satoh M, Saitoh S, Dohmae N, Harada A, Satoh N, Karasawa K, Takio K, Yanagida M, Inoue K","authors_abbrev":"Yokoyama K et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2007-12-15","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16E9.16c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:40161431","title":"Characterization of temperature-sensitive alleles of anillin-like Mid1 and polo kinase Plo1 in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2025;2025","abstract":"The  Schizosaccharomyces pombe  anillin-like Mid1 is important for the correct positioning of the cell division site. A key regulator of Mid1 is the polo kinase Plo1 which is important for several mitotic and cytokinetic events including spindle formation and division site placement. Here, we defined the mutations within a set of temperature-sensitive  mid1  and  plo1  alleles and compared the growth and morphological defects of the strains. This work expands the repertoire of  mid1  and  plo1  mutants for studying cytokinesis and highlights the requirement of the Mid1 C2 domain and the Plo1 kinase domain C-terminal lobe as particularly important for cytokinesis.","doi":"10.17912/micropub.biology.001552","authors":"Park JS, Turner LA, Gould KL, Willet AH","authors_abbrev":"Park JS et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-03-31","publication_year":"2025","canto_session_key":"5f14bab21adf5958","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2025-04-09 04:47:01","canto_approved_date":"2025-08-15 14:19:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-08 20:34:17","canto_added_date":"2025-04-01 23:25:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":14,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPAC23C11.16"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2025-04-09"},{"uniquename":"PMID:5487147","title":"The effect of 2-phenyl ethanol on the DNA synthesis cycle of Schizosaccharomyces pombe.","citation":"J Cell Sci 1970 Sep;7(2):523-30","abstract":"","authors":"Bostock CJ","authors_abbrev":"Bostock CJ","pubmed_publication_date":"Sep 1970","pubmed_entrez_date":"1970-09-01","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32784607","title":"The Chromatin Response to Double-Strand DNA Breaks and Their Repair.","citation":"Cells 2020 Aug 07;9(8)","abstract":"Cellular DNA is constantly being damaged by numerous internal and external mutagenic factors. Probably the most severe type of insults DNA could suffer are the double-strand DNA breaks (DSBs). They sever both DNA strands and compromise genomic stability, causing deleterious chromosomal aberrations that are implicated in numerous maladies, including cancer. Not surprisingly, cells have evolved several DSB repair pathways encompassing hundreds of different DNA repair proteins to cope with this challenge. In eukaryotic cells, DSB repair is fulfilled in the immensely complex environment of the chromatin. The chromatin is not just a passive background that accommodates the multitude of DNA repair proteins, but it is a highly dynamic and active participant in the repair process. Chromatin alterations, such as changing patterns of histone modifications shaped by numerous histone-modifying enzymes and chromatin remodeling, are pivotal for proficient DSB repair. Dynamic chromatin changes ensure accessibility to the damaged region, recruit DNA repair proteins, and regulate their association and activity, contributing to DSB repair pathway choice and coordination. Given the paramount importance of DSB repair in tumorigenesis and cancer progression, DSB repair has turned into an attractive target for the development of novel anticancer therapies, some of which have already entered the clinic.","doi":"10.3390/cells9081853","authors":"Aleksandrov R, Hristova R, Stoynov S, Gospodinov A","authors_abbrev":"Aleksandrov R et al.","pubmed_publication_date":"07 Aug 2020","pubmed_entrez_date":"2020-08-14","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.04c","SPBC29A10.05"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8203159","title":"Structural modification of spindle pole bodies during meiosis II is essential for the normal formation of ascospores in Schizosaccharomyces pombe: ultrastructural analysis of spo mutants.","citation":"Yeast 1994 Feb;10(2):173-83","abstract":"In order to characterize the morphological steps defined by sporulation (spo) genes during the formation of ascospores in the fission yeast Schizosaccharomyces pombe, we performed an electron microscopic study of the ultrastructure of the spindle pole body (SPB) and of the development of the forespore membrane during the second meiotic division (meiosis II) in sporulation-deficient (spo) mutants (spo4, spo5, spo14 and spo18). No difference was found in terms of the function and the structure of the SPB during the first meiotic division (meiosis I) between the four mutants and wild-type cells. However, during meiosis II, the spo4 and spo18 mutants underwent nuclear division but in neither case were the SPBs modified nor were forespore membranes formed. The SPBs of the spo18 mutant diminished in size after meiosis II and eventually disappeared after 18 h in sporulation medium. By contrast, the SPBs of the spo4 mutant remained unchanged even after an 18-h incubation. The outer plaques of SPBs of spo5 and spo14 mutants were sufficiently modified to allow them to initiate development of the forespore membrane, but the membrane had an abnormally expanded lumen and did not enclose the nuclei during meiosis II. The spo5 mutant produced anucleate spore-like bodies while the spo14 mutant formed unorganized structures with irregular peripheries which, presumably, contained spore-wall precursors, instead of anucleate spore-like bodies. We conclude that the modification of the SPB is essential for the formation of ascospores and at least two genes (spo5 and spo14) participate in the development of the forespore membrane. The defective phenotypes define discrete steps in the development of ascospores, which proceeds via steps defined by the mutant spo4, spo18, spo14 and spo5 genes respectively. Our observations provide further substantial evidence that the SPB plays a pivotal role in the normal development of ascospores in yeasts.","authors":"Hirata A, Shimoda C","authors_abbrev":"Hirata A et al.","pubmed_publication_date":"Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_session_key":"6aac558546fde9fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-05 16:38:40","canto_approved_date":"2026-01-06 17:49:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-05 16:38:33","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.02","SPBC21C3.18","SPBC3H7.01"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-05-05"},{"uniquename":"PMID:10430579","title":"Genetic control of telomere integrity in Schizosaccharomyces pombe: rad3(+) and tel1(+) are parts of two regulatory networks independent of the downstream protein kinases chk1(+) and cds1(+).","citation":"Genetics 1999 Aug;152(4):1501-12","abstract":"The Schizosaccharomyces pombe checkpoint gene named rad3(+) encodes an ATM-homologous protein kinase that shares a highly conserved motif with proteins involved in DNA metabolism. Previous studies have shown that Rad3 fulfills its function via the regulation of the Chk1 and Cds1 protein kinases. Here we describe a novel role for Rad3 in the control of telomere integrity. Mutations in the rad3(+) gene alleviated telomeric silencing and produced shortened lengths in the telomere repeat tracts. Genetic analysis revealed that the other checkpoint rad mutations rad1, rad17, and rad26 belong to the same phenotypic class with rad3 with regard to control of the telomere length. Of these mutations, rad3 and rad26 have a drastic effect on telomere shortening. tel1(+), another ATM homologue in S. pombe, carries out its telomere maintenance function in parallel with the checkpoint rad genes. Furthermore, either a single or double disruption of cds1(+) and chk1(+) caused no obvious changes in the telomeric DNA structure. Our results demonstrate a novel role of the S. pombe ATM homologues that is independent of chk1(+) and cds1(+).","authors":"Matsuura A, Naito T, Ishikawa F","authors_abbrev":"Matsuura A et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-08-03","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.07","SPAC9E9.08","SPCC1259.13","SPCC18B5.11c","SPCC23B6.03c","SPBC216.05"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:22718785","title":"Topology of functional networks predicts physical binding of proteins.","citation":"Bioinformatics 2012 Aug 15;28(16):2137-45","abstract":"It has been recognized that the topology of molecular networks provides information about the certainty and nature of individual interactions. Thus, network motifs have been used for predicting missing links in biological networks and for removing false positives. However, various different measures can be inferred from the structure of a given network and their predictive power varies depending on the task at hand.\nHerein, we present a systematic assessment of seven different network features extracted from the topology of functional genetic networks and we quantify their ability to classify interactions into different types of physical protein associations. Using machine learning, we combine features based on network topology with non-network features and compare their importance of the classification of interactions. We demonstrate the utility of network features based on human and budding yeast networks; we show that network features can distinguish different sub-types of physical protein associations and we apply the framework to fission yeast, which has a much sparser known physical interactome than the other two species. Our analysis shows that network features are at least as predictive for the tasks we tested as non-network features. However, feature importance varies between species owing to different topological characteristics of the networks. The application to fission yeast shows that small maps of physical interactomes can be extended based on functional networks, which are often more readily available.\nThe R-code for computing the network features is available from www.cellularnetworks.org","doi":"10.1093/bioinformatics/bts351","authors":"Saraç OS, Pancaldi V, Bähler J, Beyer A","authors_abbrev":"Saraç OS et al.","pubmed_publication_date":"15 Aug 2012","pubmed_entrez_date":"2012-06-22","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31125408","title":"Microtubule nucleation and dynamic instability in interphase fission yeast.","citation":"J Mol Cell Biol 2019 Dec 23;11(11):941-943","abstract":"","doi":"10.1093/jmcb/mjz044","authors":"Liang X","authors_abbrev":"Liang X","pubmed_publication_date":"23 Dec 2019","pubmed_entrez_date":"2019-05-25","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-29 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1645660","title":"Characterisation of the specific p-nitrophenylphosphatase gene and protein of Schizosaccharomyces pombe.","citation":"Eur J Biochem 1991 Jun 01;198(2):493-7","abstract":"Cloning and sequencing of the pho2 gene which codes for a specific p-nitrophenylphosphatase from Schizosaccharomyces pombe is described. The gene has an open contiguous reading frame of 269 amino acids corresponding to a protein with a molecular mass of 29.5 kDa and a calculated pI of 6.6. The sequence reveals four regions that share significant sequence similarity with the corresponding gene PHO13 of Saccharomyces cerevisiae. Purification of the enzyme to apparent homogeneity is reported. The amino acid composition of the purified protein matches well the values predicted from the nucleotide sequence. On SDS/polyacrylamide gels, the enzyme runs as a protein with a molecular mass of 33 kDa, and by Sephadex chromatography under nondenaturing conditions as 70 kDa. This indicates that the enzyme is a homodimer in its native form. The enzyme is not glycosylated. Its activity is stimulated by Mg2+ and inhibited by Zn2+. The available data on p-nitrophenylphosphatase do not give any clues to its biological role and its physiological substrates.","authors":"Yang JW, Dhamija SS, Schweingruber ME","authors_abbrev":"Yang JW et al.","pubmed_publication_date":"01 Jun 1991","pubmed_entrez_date":"1991-06-01","publication_year":"1991","canto_session_key":"3c565105aae56085","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-30 13:57:33","canto_approved_date":"2020-01-23 13:50:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-16 15:47:53","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC15D4.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-06-30"},{"uniquename":"PMID:8188690","title":"A multifunctional exonuclease from vegetative Schizosaccharomyces pombe cells exhibiting in vitro strand exchange activity.","citation":"J Biol Chem 1994 May 13;269(19):14094-102","abstract":"A 140-kDa polypeptide (p140) has been purified over 2000-fold from vegetative Schizosaccharomyces pombe cells using an assay of homologous pairing and strand exchange between linear double-stranded DNA (dsDNA) and circular single-stranded DNA (ssDNA) in vitro. Electron microscopic analysis of the reaction products showed displacement of one strand of the linear duplex DNA by the circular ssDNA molecule. In addition, the protein contained 5' to 3' exonuclease activity on ssDNA and dsDNA (with a 50-fold preference on the single-stranded substrate) as well as on single-stranded RNA. Furthermore, p140 was capable of renaturing complementary ssDNA as shown by S1 nuclease assays. p140 behaved like a monomer in solution under reaction conditions. Direct comparison of the biochemical properties, sequence analysis, and cross-reactivity to a monoclonal antibody suggests that p140 is probably identical with ExoII, purified from S. pombe meiotic cells as a ssDNA exonuclease (Szankasi, P., and Smith, G. R. (1992) Biochemistry 31, 6769-6773). Given the diverse activities of p140, the protein might be involved in DNA and/or RNA metabolism in vivo.","authors":"Käslin E, Heyer WD","authors_abbrev":"Käslin E et al.","pubmed_publication_date":"13 May 1994","pubmed_entrez_date":"1994-05-13","publication_year":"1994","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.14"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:27168121","title":"Discovery of genes involved in mitosis, cell division, cell wall integrity and chromosome segregation through construction of Schizosaccharomyces pombe deletion strains.","citation":"Yeast 2016 Sep;33(9):507-17","abstract":"The fission yeast model system Schizosaccharomyces pombe is used to study fundamental biological processes. To continue to fill gaps in the Sz. pombe gene deletion collection, we constructed a set of 90 haploid gene deletion strains covering many previously uncharacterized genes. To begin to understand the function of these genes, we exposed this collection of strains to a battery of stress conditions. Using this information in combination with microscopy, proteomics and mini-chromosome loss assays, we identified genes involved in cell wall integrity, cytokinesis, chromosome segregation and DNA metabolism. This subset of non-essential gene deletions will add to the toolkits available for the study of biological processes in Sz. pombe. Copyright © 2016 John Wiley & Sons, Ltd.","doi":"10.1002/yea.3172","authors":"Chen JS, Beckley JR, Ren L, Feoktistova A, Jensen MA, Rhind N, Gould KL","authors_abbrev":"Chen JS et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-05-12","publication_year":"2016","canto_session_key":"26a7509190100074","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-Song Chen","canto_first_approved_date":"2016-09-05 10:38:07","canto_approved_date":"2023-05-03 16:05:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-29 16:42:52","canto_added_date":"2016-05-13 00:15:13","annotation_curators":[{"name":"Jun-Song Chen","community_curator":true,"annotation_count":105,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":178,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_27168121_phaf.tsv"}],"genes":["SPBC29A3.01","SPAC824.03c","SPBC12D12.04c","SPAPB18E9.02c","SPAC24B11.11c","SPBC713.02c","SPAC343.09","SPCC1442.15c","SPBP26C9.03c","SPAC1F12.10c","SPBC582.05c","SPAC977.10","SPBC28F2.11","SPBC14C8.19","SPCC1183.05c","SPAC24B11.10c","SPAC688.07c","SPAC12B10.03","SPACUNK4.14","SPBC1A4.05","SPBC16G5.19","SPBP35G2.16c","SPCC645.14c","SPAC1250.07","SPBC646.12c","SPBC17G9.06c","SPAP4C9.02","SPAC23A1.10","SPAC3A11.08","SPBC685.08","SPAC27E2.12","SPBC2F12.13","SPAC1F3.02c","SPBC56F2.12","SPBC11C11.02","SPBC19C7.04c","SPAC4F10.15c","SPBC28E12.03","SPBC16E9.19","SPBC16C6.10","SPBC6B1.12c","SPAC959.04c","SPBC1271.11","SPBC23G7.08c","SPBC1347.06c","SPBC12D12.05c","SPBPB8B6.06c","SPAC7D4.06c","SPAC1F12.06c","SPBC1289.01c","SPAPJ760.03c","SPAC1565.02c","SPAC23C4.04c","SPAC2F7.16c","SPAC31A2.10","SPAC328.07c","SPBC11G11.02c","SPCC4G3.12c","SPAC4G9.07","SPAC9.09","SPAC8E11.12","SPBC530.14c","SPCC16C4.02c","SPAC18G6.09c","SPAC1006.05c","SPBC19C7.11","SPAC806.03c","SPAC6F12.02","SPAPB1A10.16","SPCC4G3.03","SPBC800.14c","SPAC23D3.17","SPAC2E1P5.01c","SPCC970.01","SPBC19G7.05c","SPBC902.06","SPCC1393.14","SPAC2F3.13c","SPBP23A10.11c","SPAC167.05","SPAC821.04c","SPCC4G3.13c","SPAC19E9.03","SPAC26F1.01","SPBC32F12.09","SPAC12B10.06c","SPBC2F12.07c","SPCC16A11.12c","SPBC36.11","SPBC211.07c","SPBP23A10.03c","SPCC777.09c","SPCP1E11.09c","SPBC1778.06c","SPAC144.13c","SPAPB24D3.10c","SPBC1289.04c","SPCC645.06c","SPBC29A3.17","SPCC1840.02c","SPAC18B11.10","SPAC222.19"],"gene_count":102,"ltp_gene_count":102,"approved_date":"2016-09-05"},{"uniquename":"EMBL:SPD230","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32795531","title":"Phosphorylation of the Transcription Factor Atf1 at Multiple Sites by the MAP Kinase Sty1 Controls Homologous Recombination and Transcription.","citation":"J Mol Biol 2020 Sep 04;432(19):5430-5446","abstract":"Transcription factors are often the downstream effectors of signaling cascades. In fission yeast, the transcription factor Atf1 is phosphorylated by the MAP kinase Sty1 under several environmental stressors to promote transcription initiation of stress genes. However, Sty1 and Atf1 have also been involved in other cellular processes such as homologous recombination at hotspots, ste11 gene expression during mating and meiosis, or regulation of fbp1 gene transcription under glucose starvation conditions. Using different phospho-mutants of Atf1, we have investigated the role of Atf1 phosphorylation by Sty1 in those biological processes. An Atf1 mutant lacking the canonical MAP kinase phosphorylation sites cannot activate fbp1 transcription when glucose is depleted, but it is still able to induce recombination at ade6.M26 and to induce ste11 after nitrogen depletion; in these last cases, Sty1 is still required, suggesting that additional non-canonical sites are activating the transcription factor. In all cases, an Atf1 phosphomimetic mutant bypasses the requirement of the Sty1 kinase in these diverse biological processes, highlighting the essential role of the DNA binding factor Atf1 on chromatin remodeling and cell adaptation to nutritional changes. We propose that post-translational modifications of Atf1 by Sty1, either at canonical or non-canonical sites, are sufficient to activate some of the functions of Atf1, those involving chromatin remodeling and transcription initiation. However, in the case of fbp1 where Atf1 acts synergistically with other transcription factors, elimination of the canonical sites is sufficient to hamper some of the interactions required in this complex scenario and to impair transcription initiation.","doi":"10.1016/j.jmb.2020.08.004","authors":"Sánchez-Mir L, Fraile R, Ayté J, Hidalgo E","authors_abbrev":"Sánchez-Mir L et al.","pubmed_publication_date":"04 Sep 2020","pubmed_entrez_date":"2020-08-16","publication_year":"2020","canto_session_key":"906f50f91b15da8f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-08-18 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC29B5.01"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:30709916","title":"A Cdc42 GEF, Gef1, through endocytosis organizes F-BAR Cdc15 along the actomyosin ring and promotes concentric furrowing.","citation":"J Cell Sci 2019 Feb 28;132(5)","abstract":"During cytokinesis, fission yeast coordinates actomyosin ring constriction with septum ingression, resulting in concentric furrow formation by a poorly defined mechanism. We report that  Schizosaccharomyces pombe  cells lacking the Cdc42 activator Gef1, combined with an activated allele of the formin, Cdc12, display non-concentric furrowing. Non-concentrically furrowing cells display uneven distribution of the scaffold Cdc15 along the ring. This suggests that, after ring assembly, uniform Cdc15 distribution along the ring enables proper furrow formation. We find that, after assembly, Cdc15 is recruited to the ring in an Arp2/3 complex-dependent manner and is decreased in the activated  cdc12  mutant. Cdc15 at cortical endocytic patches shows increased levels and extended lifetimes in  gef1  and activated  cdc12  mutants. We hypothesize endocytosis helps recruit Cdc15 to assembled rings; uneven Cdc15 distribution at the ring occurs when endocytic patches contain increased Cdc15 levels and the patch-association rate is slow. Based on this, we developed a mathematical model that captures experimentally observed Cdc15 distributions along the ring. We propose that, at the ring, Gef1 and endocytic events promote uniform Cdc15 organization to enable proper septum ingression and concentric furrow formation.","doi":"10.1242/jcs.223776","authors":"Onwubiko UN, Mlynarczyk PJ, Wei B, Habiyaremye J, Clack A, Abel SM, Das ME","authors_abbrev":"Onwubiko UN et al.","pubmed_publication_date":"28 Feb 2019","pubmed_entrez_date":"2019-02-03","publication_year":"2019","canto_session_key":"70672a5b4182aefe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maitreyi Das","canto_first_approved_date":"2019-07-03 15:32:58","canto_approved_date":"2026-05-02 09:25:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-25 20:01:33","canto_added_date":"2019-02-04 01:15:04","annotation_curators":[{"name":"Maitreyi Das","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.09","SPAC1F5.04c","SPAC110.03","SPBC32H8.12c","SPAC20G8.05c","SPAC926.03","SPAC630.03"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2019-07-03"},{"uniquename":"PMID:41236300","title":"Molecular identification of yeasts involved in the alcoholic fermentation of Tchoukoutou and Atan in Benin using sequencing.","citation":"Cell Mol Biol (Noisy-le-grand) 2025 Nov 02;71(10):58-66","abstract":"In Benin, the consumption of local beverages is increasing, particularly \"Tchoukoutou\" and \"Atan\". However, they face numerous challenges that hinder their recognition as fermented drinks with potential medical and cultural benefits. This study aims to determine the biodiversity of yeasts responsible for the fermentation of \"Tchoukoutou\" and \"Atan\" produced in Benin to promote their production and commercialization. To achieve this, beverage samples were randomly collected from six (06) municipalities in Benin and subjected to physicochemical and microbiological analysis. Yeast identification was performed through sequencing of the D1/D2 region of the 26S ribosomal RNA (26S rRNA) gene. Physicochemical analysis revealed that the pH values ranged between 3.65 and 3.92 for \"Tchoukoutou\" and between 3.71 and 4.04 for \"Atan.\" Regarding sugar content (Brix degree), \"Tchoukoutou\" values ranged from 1 to 12° Brix, while those of \"Atan\" ranged from 1° to 14° Brix. Microbiological analysis showed that the yeast count in \"Tchoukoutou\" and \"Atan\" was 1.57 × 10³ and 5.29 × 10³ CFU/mL, respectively. A total of five (05) different yeast species were identified in \"Tchoukoutou\" and six (06) in \"Atan\". Schizosaccharomyces pombe (44.44%) was the predominant yeast species in the fermentation of \"Tchoukoutou\", followed by Saccharomyces cerevisiae (22.22%). In contrast, for \"Atan\", Saccharomyces cerevisiae (53.33%) was the most dominant species, followed by Saccharomyces boulardii (13.33%), and Candida parapsilosis (13.33%). Other yeast species present in lower percentages included Candida parapsilosis (11.11%), Pichia sp. Feni (11.11%) and Pichia manshurica (11.11%) in \"Tchoukoutou\" and Pichia kudriavzevii (6.66%), Pichia ethanolica (6.66%) and Schizosaccharomyces osmophilus (6.66%) in \"Atan\". These results indicate that Beninese \"Tchoukoutou\" and \"Atan\" fermentation is primarily driven by Schizosaccharomyces pombe, a yeast not commonly found in traditional Benin beverages, and Saccharomyces cerevisiae, respectively. This information is valuable for developing genetic engineering strategies to control their alcoholic fermentation, improve packaging, and extend shelf life.","doi":"10.14715/cmb/2025.71.10.8","authors":"Nanoukon CNM, Tchekessi C, Badoussi M, Accrombessi B, Ohin B, N'tcha C, Havivi A, Déguénon L, Loumèdjinon P, Baba-Moussa F, Djèdatin LG","authors_abbrev":"Nanoukon CNM et al.","pubmed_publication_date":"02 Nov 2025","pubmed_entrez_date":"2025-11-14","publication_year":"2025","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2025-11-15 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19799187","title":"Analysis of chromatin structure at meiotic DSB sites in yeasts.","citation":"Methods Mol Biol 2009;557:253-66","abstract":"One of the major features of meiosis is a high frequency of homologous recombination that not only confers genetic diversity to a successive generation but also ensures proper segregation of chromosomes. Meiotic recombination is initiated by DNA double-strand breaks that require many proteins including the catalytic core, Spo11. In this regard, like transcription and repair, etc., recombination is hindered by a compacted chromatin structure because trans-acting factors cannot easily access the DNA. Such inhibitory effects must be alleviated prior to recombination initiation. Indeed, a number of groups showed that chromatin around recombination hotspots is less condensed, by using nucleases as a probe to assess local DNA accessibility. Here we describe a method to analyze chromatin structure of a recombination hotspot in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. This method, combining micrococcal nuclease (MNase) digestion ofchromatin DNA and subsequent Southern blotting, is expected to provide information as to chromatin context around a hotspot. Moreover, by virtue of MNase preferentially targeting linker DNA, positions of several nucleosomes surrounding a hotspot can also be determined. Our protocol is a very powerful way to analyze several-kb regions of interest and can be applied to other purposes.","doi":"10.1007/978-1-59745-527-5_16","authors":"Hirota K, Fukuda T, Yamada T, Ohta K","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-10-06","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35333350","title":"Rec8 Cohesin-mediated Axis-loop chromatin architecture is required for meiotic recombination.","citation":"Nucleic Acids Res 2022 Apr 22;50(7):3799-3816","abstract":"During meiotic prophase, cohesin-dependent axial structures are formed in the synaptonemal complex (SC). However, the functional correlation between these structures and cohesion remains elusive. Here, we examined the formation of cohesin-dependent axial structures in the fission yeast Schizosaccharomyces pombe. This organism forms atypical SCs composed of linear elements (LinEs) resembling the lateral elements of SC but lacking the transverse filaments. Hi-C analysis using a highly synchronous population of meiotic S. pombe cells revealed that the axis-loop chromatin structure formed in meiotic prophase was dependent on the Rec8 cohesin complex. In contrast, the Rec8-mediated formation of the axis-loop structure occurred in cells lacking components of LinEs. To dissect the functions of Rec8, we identified a rec8-F204S mutant that lost the ability to assemble the axis-loop structure without losing cohesion of sister chromatids. This mutant showed defects in the formation of the axis-loop structure and LinE assembly and thus exhibited reduced meiotic recombination. Collectively, our results demonstrate that the Rec8-dependent axis-loop structure provides a structural platform essential for LinE assembly, facilitating meiotic recombination of homologous chromosomes, independently of its role in sister chromatid cohesion.","doi":"10.1093/nar/gkac183","authors":"Sakuno T, Tashiro S, Tanizawa H, Iwasaki O, Ding DQ, Haraguchi T, Noma KI, Hiraoka Y","authors_abbrev":"Sakuno T et al.","pubmed_publication_date":"22 Apr 2022","pubmed_entrez_date":"2022-03-25","publication_year":"2022","canto_session_key":"9ef8610874465dee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takeshi Sakuno","canto_first_approved_date":"2022-05-08 12:38:59","canto_approved_date":"2022-11-11 15:03:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-04-15 10:46:26","canto_added_date":"2022-03-27 01:00:05","annotation_curators":[{"name":"Takeshi Sakuno","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.04c","SPBC428.17c","SPAC17A5.11","SPBC29A10.14"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2022-05-08"},{"uniquename":"PMID:39142658","title":"Tracking live-cell single-molecule dynamics enables measurements of heterochromatin-associated protein-protein interactions.","citation":"Nucleic Acids Res 2024 Aug 15;","abstract":"Visualizing and measuring molecular-scale interactions in living cells represents a major challenge, but recent advances in single-molecule super-resolution microscopy are bringing us closer to achieving this goal. Single-molecule super-resolution microscopy enables high-resolution and sensitive imaging of the positions and movement of molecules in living cells. HP1 proteins are important regulators of gene expression because they selectively bind and recognize H3K9 methylated (H3K9me) histones to form heterochromatin-associated protein complexes that silence gene expression, but several important mechanistic details of this process remain unexplored. Here, we extended live-cell single-molecule tracking studies in fission yeast to determine how HP1 proteins interact with their binding partners in the nucleus. We measured how genetic perturbations that affect H3K9me alter the diffusive properties of HP1 proteins and their binding partners, and we inferred their most likely interaction sites. Our results demonstrate that H3K9 methylation spatially restricts HP1 proteins and their interactors, thereby promoting ternary complex formation on chromatin while simultaneously suppressing off-chromatin binding. As opposed to being an inert platform to direct HP1 binding, our studies propose a novel function for H3K9me in promoting ternary complex formation by enhancing the specificity and stimulating the assembly of HP1-protein complexes in living cells.","doi":"10.1093/nar/gkae692","authors":"Chen Z, Seman M, Fyodorova Y, Farhat A, Ames A, Levashkevich A, Biswas S, Huang F, Freddolino L, Biteen JS, Ragunathan K","authors_abbrev":"Chen Z et al.","pubmed_publication_date":"15 Aug 2024","pubmed_entrez_date":"2024-08-14","publication_year":"2024","canto_session_key":"272000a33ab56fda","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_session_submitted_date":"2024-09-26 11:28:43","canto_added_date":"2024-08-15 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24270073","title":"The 3-hydroxy-3-methylglutaryl coenzyme-A reductases from fungi: a proposal as a therapeutic target and as a study model.","citation":"Rev Iberoam Micol 2014;31(1):81-5","abstract":"The enzyme 3-hydroxy-3-methylglutaryl coenzyme-A reductase (HMGR) catalyzes the conversion of HMG-Co-A into mevalonate. This step is the limiting point for the synthesis of cholesterol in mammals and ergosterol in fungi. We describe in this article the genome organization of HMGR coding genes and those deduced from different fungi, recount the evidence showing statins as HMGR inhibitors for ergosterol synthesis and its effect in yeast viability, and propose fungal HMGR (HMGRf) as a model to study the use of pharmaceutical compounds to inhibit cholesterol and ergosterol synthesis. Bibliographical search and bioinformatic analyses were performed and discussed. HMGRfs belong to the class I with a high homology in the catalytic region. The sterol biosynthetic pathway in humans and fungi share many enzymes in the initial steps (such as the HMGR enzyme), but in the last steps enzymes are different rendering the two final products: cholesterol in mammals and ergosterol in fungi. With regards to inhibitors such as statins and other compounds, these affect also fungal viability. Since HMGR from Schizosaccharomyces pombe and Ustilago maydis are very similar to the human HMGR in the catalytic regions, we propose that fungal enzymes can be used to test inhibitors for a potential use in humans. We consider that HMGRf is a good therapeutic target to design and test new antifungal compounds. This manuscript is part of the series of works presented at the \"V International Workshop: Molecular genetic approaches to the study of human pathogenic fungi\" (Oaxaca, Mexico, 2012).","doi":"10.1016/j.riam.2013.10.004","authors":"Andrade-Pavón D, Sánchez-Sandoval E, Rosales-Acosta B, Ibarra JA, Tamariz J, Hernández-Rodríguez C, Villa-Tanaca L","authors_abbrev":"Andrade-Pavón D et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2013-11-26","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40731013","title":"Artificial chromosome reorganization reveals high plasticity of the budding and fission yeast genomes.","citation":"Genome Biol 2025 Jul 29;26(1):229","abstract":"The genome of a eukaryotic cell is usually organized on a set of chromosomes. Recently, karyotype engineering has been applied to various organisms, but whether and to what extent a naturally evolved genome can resist or tolerate massive artificial manipulations remains unexplored.\nUsing unicellular yeast models of both Saccharomyces cerevisiae and Schizosaccharomyces pombe, we deliberately construct dozens of single-chromosome strains with different chromosome architectures. Three S. cerevisiae strains have the individual chromosomes fused into a single chromosome, but with the individual chromosomes in different orders. Eighteen S. cerevisiae strains have a single chromosome but with different centromeric sequences. Fifteen S. cerevisiae strains have a single chromosome with the centromere at different distances relative to the telomeres. Two S. pombe strains have a single, circular chromosome, and three strains have a single, linear chromosome with the centromere at different distances relative to the telomeres. All of these single-chromosome strains are viable, but the strains with an acrocentric or a telocentric chromosome have abnormal cell morphologies, and grow more slowly than those with a metacentric or sub-metacentric chromosome, and show increased genome instability with chromosome segregation abnormalities or genome diploidization.\nThe functional genomes of both the evolutionarily distant yeasts S. cerevisiae and S. pombe are highly tolerant of diversified genome organizations. The phenotypic abnormalities and increased genome instability of the acrocentric/telocentric single-chromosome yeasts suggest that yeasts with metacentric chromosomes have an evolutionary advantage.","doi":"10.1186/s13059-025-03689-1","authors":"Zhu X, Liu S, Ye T, Gu X, Pu F, Zhou Z, Wu ZJ, Zhou JQ","authors_abbrev":"Zhu X et al.","pubmed_publication_date":"29 Jul 2025","pubmed_entrez_date":"2025-07-29","publication_year":"2025","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2025-07-30 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012313","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34390209","title":"L-malic acid production from xylose by engineered Saccharomyces cerevisiae.","citation":"Biotechnol J 2022 Mar;17(3):e2000431","abstract":"L-malic acid is widely used in the food, chemical, and pharmaceutical industries. Here, we report on production of malic acid from xylose, the second most abundant sugar in lignocellulosic hydrolysates, by engineered Saccharomyces cerevisiae. To enable malic acid production in a xylose-assimilating S. cerevisiae, we overexpressed PYC1 and PYC2, coding for pyruvate carboxylases, a truncated MDH3 coding for malate dehydrogenase, and SpMAE1, coding for a Schizosaccharomyces pombe malate transporter. Additionally, both the ethanol and glycerol-producing pathways were blocked to enhance malic acid production. The resulting strain produced malic acid from both glucose and xylose, but it produced much higher titers of malic acid from xylose than glucose. Interestingly, the engineered strain had higher malic acid yield from lower concentrations (10 g L -1  ) of xylose, with no ethanol production, than from higher xylose concentrations (20 and 40 g L -1  ). As such, a fed-batch culture maintaining xylose concentrations at low levels was conducted and 61.2 g L -1  of malic acid was produced, with a productivity of 0.32 g L -1  h. These results represent successful engineering of S. cerevisiae for the production of malic acid from xylose, confirming that that xylose offers the efficient production of various biofuels and chemicals by engineered S. cerevisiae.","doi":"10.1002/biot.202000431","authors":"Kang NK, Lee JW, Ort DR, Jin YS","authors_abbrev":"Kang NK et al.","pubmed_publication_date":"Mar 2022","pubmed_entrez_date":"2021-08-14","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-08-16 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23613905","title":"Electron tomography reveals novel microtubule lattice and microtubule organizing centre defects in +TIP mutants.","citation":"PLoS One 2013;8(4):e61698","abstract":"Mal3p and Tip1p are the fission yeast (Schizosaccharomyces pombe) homologues of EB1 and CLIP-170, two conserved microtubule plus end tracking proteins (+TIPs). These proteins are crucial regulators of microtubule dynamics. Using electron tomography, we carried out a high-resolution analysis of the phenotypes caused by mal3 and tip1 deletions. We describe the 3-dimensional microtubule organization, quantify microtubule end structures and uncover novel defects of the microtubule lattices. We also reveal unexpected structural modifications of the spindle pole bodies (SPBs), the yeast microtubule organizing centers. In both mutants we observe an increased SPB volume and a reduced number of MT/SPB attachments. The discovered defects alter previous interpretations of the mutant phenotypes and provide new insights into the molecular functions of the two protein families.","doi":"10.1371/journal.pone.0061698","authors":"Höög JL, Huisman SM, Brunner D, Antony C","authors_abbrev":"Höög JL et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-04-25","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPAC3C7.12"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:14967138","title":"The RITS complex-A direct link between small RNA and heterochromatin.","citation":"Mol Cell 2004 Feb 13;13(3):304-5","abstract":"In a recent report, Moazed, Grewal, and colleagues (Verdel et al., 2004) characterize the RITS (RNA induced initiation of transcriptional silencing) protein complex in fission yeast. They provide a sought-for link between the small RNA produced by the RNA interference machinery and heterochromatin components, suggesting a mechanism for how heterochromatin formation can be targeted in trans to specific chromosomal regions.","authors":"Ekwall K","authors_abbrev":"Ekwall K","pubmed_publication_date":"13 Feb 2004","pubmed_entrez_date":"2004-02-18","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8832415","title":"The wis1 signal transduction pathway is required for expression of cAMP-repressed genes in fission yeast.","citation":"J Cell Sci 1996 Jul;109 ( Pt 7):1927-35","abstract":"The wis1 protein kinase of Schizosaccharomyces pombe is a member of the MAP kinase kinase family. Loss of wis1 function has previously been reported to lead to a delay in the G2-mitosis transition, loss of viability in stationary phase, and hypersensitivity to osmotic shock. It acts at least in part by activating the MAP kinase homologue sty1; loss-of-function sty1 mutants share many phenotypes with wis1 deletion mutants. We show here that, in addition, loss of wis1 function leads to defective conjugation, and to suppression of the hyperconjugation phenotype of the pat1-114 mutation. Consistent with this, the induction of the mei2 gene, which is normally induced by nitrogen starvation, is defective in wis1 mutants. In wild-type cells, nitrogen starvation leads to mei2 induction through a fall in intracellular cyclic AMP (cAMP) level and activity of the cAMP-dependent protein kinase. We show here that wis1 function is required for mei2 induction following nitrogen starvation. Expression of the fbp1 gene is negatively regulated by cAMP in response to glucose limitation: induction of fbp1 also requires wis1 and sty1 function. Loss of wis1 is epistatic over increased fbp1 expression brought about by loss of adenylate cyclase (git2/cyr1) or cAMP-dependent protein kinase (pka1) function. These observations can be explained by a model in which the pka1 pathway negatively regulates the wis1 pathway, or the two pathways might act independently on downstream targets. The latter explanation is supported, at least as regards regulation of cell division, by the observation that loss of function of the regulatory subunit of the cAMP-dependent protein kinase (cgs1) brings about a modest increase in cell length at division in both wis1+ and wis1 delta genetic backgrounds.","authors":"Stettler S, Warbrick E, Prochnik S, Mackie S, Fantes P","authors_abbrev":"Stettler S et al.","pubmed_publication_date":"Jul 1996","pubmed_entrez_date":"1996-07-01","publication_year":"1996","canto_session_key":"a55bbcd907960445","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-03 08:16:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-08 19:09:27","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPAC8C9.03","SPBC19C2.05","SPBC1198.14c","SPAC27D7.03c","SPBC409.07c","SPBC19C7.03"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2015-01-08"},{"uniquename":"PMID:9054344","title":"[Three regions of Rpb10 mini-subunit of nuclear RNA polymerases are strictly conserved in all eukaryotes].","citation":"Bioorg Khim 1996 Dec;22(12):938-40","abstract":"The rpb10+ cDNA from the fission yeast Schizosaccharomyces pombe was cloned using two independent approaches (PCR and genetic suppression). The cloned cDNA encoded the Rpb10 subunit common for all three RNA polymerases. Comparison of the deduced amino acid sequence of the Sz. pombe Rbp10 subunit (71 amino acid residues) with those of the homologous subunits of RNA polymerases I, II, and III from Saccharomyces cerevisiae and Home sapiens revealed that heptapeptides RCFT/SCGK (residues 6-12), RYCCRRM (residues 43-49), and HVDLIEK (residues 53-59) were evolutionarily the most conserved structural motifs of these subunits. It is shown that the Rbp10 subunit from Sz. pombe can substitute its homolog (ABC10 beta) in the baker's yeast S. cerevisiae.","authors":"Shpakovskiĭ GV, Lebedenko EN","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_session_key":"1f13b980f1913b17","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:53:11","canto_approved_date":"2018-12-22 20:53:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 20:53:07","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:30295604","title":"BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligands.","citation":"Elife 2018 Oct 08;7","abstract":"TOPBP1 and its fission yeast homologueRad4, are critical players in a range of DNA replication, repair and damage signalling processes. They are composed of multiple BRCT domains, some of which bind phosphorylated motifs in other proteins. They thus act as multi-point adaptors bringing proteins together into functional combinations, dependent on post-translational modifications downstream of cell cycle and DNA damage signals. We have now structurally and/or biochemically characterised a sufficient number of high-affinity complexes for the conserved N-terminal region of TOPBP1 and Rad4 with diverse phospho-ligands, including human RAD9 and Treslin, and  Schizosaccharomyces pombe  Crb2 and Sld3, to define the determinants of BRCT domain specificity. We use this to identify and characterise previously unknown phosphorylation-dependent TOPBP1/Rad4-binding motifs in human RHNO1 and the fission yeast homologue of MDC1, Mdb1. These results provide important insights into how multiple BRCT domains within TOPBP1/Rad4 achieve selective and combinatorial binding of their multiple partner proteins.","doi":"10.7554/eLife.39979","authors":"Day M, Rappas M, Ptasinska K, Boos D, Oliver AW, Pearl LH","authors_abbrev":"Day M et al.","pubmed_publication_date":"08 Oct 2018","pubmed_entrez_date":"2018-10-09","publication_year":"2018","canto_session_key":"2d2cae4a6af2b8b6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-10-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPACUNK4.14","SPBC6B1.09c","SPAC24H6.06","SPAC23C4.18c"],"gene_count":4,"ltp_gene_count":4,"pdb_entries":[{"pdb_id":"6hm4","gene_chains":[{"gene_uniquename":"SPACUNK4.14","chain":"B","position":"106-120"},{"gene_uniquename":"SPAC23C4.18c","chain":"A","position":"1-186"}],"title":"Crystal structure of Rad4 BRCT1,2 in complex with a Mdb1 phosphopeptide","entry_authors":"Day M,Rappas M,Oliver AW,Pearl LH","entry_authors_abbrev":"Day M et al.","reference_uniquename":"PMID:30295604","experimental_method":"X-ray","resolution":"1.770186"},{"pdb_id":"6hm3","gene_chains":[{"gene_uniquename":"SPAC23C4.18c","chain":"A","position":"1-186"},{"gene_uniquename":"SPAC24H6.06","chain":"B","position":"629-656"}],"title":"Crystal structure of Rad4 BRCT1,2 in complex with a Sld3 phosphopeptide","entry_authors":"Day M,Rappas M,Oliver AW,Pearl LH","entry_authors_abbrev":"Day M et al.","reference_uniquename":"PMID:30295604","experimental_method":"X-ray","resolution":"1.7726362"}]},{"uniquename":"PMID:8816472","title":"Identification of Ste4 as a potential regulator of Byr2 in the sexual response pathway of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1996 Oct;16(10):5597-603","abstract":"A conserved MAP kinase cascade is central to signal transduction in both simple and complex eukaryotes. In the yeast Schizosaccharomyces pombe, Byr2, a homolog of mammalian MAPK/ERK kinase kinase and Saccharomyces cerevisiae STE11, is required for pheromone-induced sexual differentiation. A screen for S. pombe proteins that interact with Byr2 in a two-hybrid system led to the isolation of Ste4, a protein that is known to be required for sexual function. Ste4 binds to the regulatory region of Byr2. This binding site is separable from the binding site for Ras1. Both Ste4 and Ras1 act upstream of Byr2 and act at least partially independently. Ste4 contains a leucine zipper and is capable of homotypic interaction. Ste4 has regions of homology with STE50, an S. cerevisiae protein required for sexual differentiation that we show can bind to STE11.","authors":"Barr MM, Tu H, Van Aelst L, Wigler M","authors_abbrev":"Barr MM et al.","pubmed_publication_date":"Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_session_key":"0dd384fe368bd279","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-13 13:52:50","canto_approved_date":"2024-09-24 09:46:25","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-05-26 16:39:12","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC24C6.06","SPAC1D4.13","SPAC1565.04c","SPBC1D7.05"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-11-13"},{"uniquename":"PMID:9757832","title":"MAPs, MARKs and microtubule dynamics.","citation":"Trends Biochem Sci 1998 Aug;23(8):307-11","abstract":"Microtubules (MTs) serve as tracks for cellular transport, and regulate cell shape and polarity. Rapid transitions between stable and dynamic forms of MTs are central to these processes. This dynamic instability is regulated by a number of cellular factors, including the structural MT-associated proteins (MAPs), which in turn are regulated by phosphorylation. MT-affinity-regulating kinases (MARKs) are novel mammalian serine/threonine kinases that phosphorylate the tubulin-binding domain of MAPs and thereby cause their detachment from MTs and increased MT dynamics. Molecular cloning of MARKs revealed a family of four closely related protein kinases that share homology with genes from the nematode Caenorhabditis elegans and fission yeast that are involved in the generation of cell shape and polarity. Hence, MARKs might play a role in the regulation of MT stability during morphogenesis.","authors":"Drewes G, Ebneth A, Mandelkow EM","authors_abbrev":"Drewes G et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-10-03","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30680437","title":"Down-regulation of Cdk1 activity in G1 coordinates the G1/S gene expression programme with genome replication.","citation":"Curr Genet 2019 Jun;65(3):685-690","abstract":"Cell division is regulated by cyclin-dependent kinases (Cdks) and requires the periodic activation and inactivation of transcription factors that generate waves of gene expression in different cell-cycle phases. In fission yeast, the MCB-binding transcription factor (MBF) is activated at the end of G1 and regulates the expression of a set of genes that encode for proteins involved in the G1/S transition and DNA replication. Here, we review the importance of controlling MBF by Cdk activity at the onset of S phase. Furthermore, we emphasize that MBF regulation by Cdk is particularly critical under conditions in which G1 is extended, such as in nitrogen-poor environments, where down-regulation of Cdk activity in G1 is crucial to generate a proper wave of MBF-dependent transcription at the end of G1, which is critical to promote a successful S phase.","doi":"10.1007/s00294-018-00926-y","authors":"García-Blanco N, Moreno S","authors_abbrev":"García-Blanco N et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-01-26","publication_year":"2019","canto_session_key":"984346bc25da8b7a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-01-28 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.09","SPCC24B10.07"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:34347508","title":"Sequestration of the exocytic SNARE Psy1 into multiprotein nodes reinforces polarized morphogenesis in fission yeast.","citation":"Mol Biol Cell 2021 Oct 01;32(20):ar7","abstract":"Polarized morphogenesis is achieved by targeting or inhibiting growth in distinct regions. Rod-shaped fission yeast cells grow exclusively at their ends by restricting exocytosis and secretion to these sites. This growth pattern implies the existence of mechanisms that prevent exocytosis and growth along nongrowing cell sides. We previously identified a set of 50-100 megadalton-sized node structures along the sides of fission yeast cells that contained the interacting proteins Skb1 and Slf1. Here, we show that Skb1-Slf1 nodes contain the syntaxin-like soluble N-ethylmaleimide-sensitive factor attachment protein receptor Psy1, which mediates exocytosis in fission yeast. Psy1 localizes in a diffuse pattern at cell tips, where it likely promotes exocytosis and growth, but is sequestered in Skb1-Slf1 nodes at cell sides where growth does not occur. Mutations that prevent node assembly or inhibit Psy1 localization to nodes lead to aberrant exocytosis at cell sides and increased cell width. Genetic results indicate that this Psy1 node mechanism acts in parallel to actin cables and Cdc42 regulation. Our work suggests that sequestration of syntaxin-like Psy1 at nongrowing regions of the cell cortex reinforces cell morphology by restricting exocytosis to proper sites of polarized growth.","doi":"10.1091/mbc.E20-05-0277","authors":"Miller KE, Magliozzi JO, Picard NA, Moseley JB","authors_abbrev":"Miller KE et al.","pubmed_publication_date":"01 Oct 2021","pubmed_entrez_date":"2021-08-04","publication_year":"2021","canto_session_key":"c179fc21f5ef1e1d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-08-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18457900","title":"Cracking the RNA polymerase II CTD code.","citation":"Trends Genet 2008 Jun;24(6):280-8","abstract":"The carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II comprises multiple tandem conserved heptapeptide repeats, unique to this eukaryotic RNA polymerase. This unusual structure provides a docking platform for factors involved in various co-transcriptional events. Recruitment of the appropriate factors at different stages of the transcription cycle is achieved through changing patterns of post-translational modification of the CTD repeats, which create a readable 'code'. A new phosphorylation mark both expands the CTD code and provides the first example of a CTD signal read in a gene type-specific manner. How and when is the code written and read? How does it contribute to transcription and coordinate RNA processing?","doi":"10.1016/j.tig.2008.03.008","authors":"Egloff S, Murphy S","authors_abbrev":"Egloff S et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-05-07","publication_year":"2008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26744405","title":"Accurate concentration control of mitochondria and nucleoids.","citation":"Science 2016 Jan 08;351(6269):169-72","abstract":"All cellular materials are partitioned between daughters at cell division, but by various mechanisms and with different accuracy. In the yeast Schizosaccharomyces pombe, the mitochondria are pushed to the cell poles by the spindle. We found that mitochondria spatially reequilibrate just before division, and that the mitochondrial volume and DNA-containing nucleoids instead segregate in proportion to the cytoplasm inherited by each daughter. However, nucleoid partitioning errors are suppressed by control at two levels: Mitochondrial volume is actively distributed throughout a cell, and nucleoids are spaced out in semiregular arrays within mitochondria. During the cell cycle, both mitochondria and nucleoids appear to be produced without feedback, creating a net control of fluctuations that is just accurate enough to avoid substantial growth defects.","doi":"10.1126/science.aaa8714","authors":"Jajoo R, Jung Y, Huh D, Viana MP, Rafelski SM, Springer M, Paulsson J","authors_abbrev":"Jajoo R et al.","pubmed_publication_date":"08 Jan 2016","pubmed_entrez_date":"2016-01-09","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23149940","title":"Blt1 and Mid1 provide overlapping membrane anchors to position the division plane in fission yeast.","citation":"Mol Cell Biol 2013 Jan;33(2):418-28","abstract":"Spatial control of cytokinesis is essential for proper cell division. The molecular mechanisms that anchor the dynamic assembly and constriction of the cytokinetic ring at the plasma membrane remain unclear. In the fission yeast Schizosaccharomyces pombe, the cytokinetic ring is assembled in the cell middle from cortical node precursors that are positioned by the anillin-like protein Mid1. During mitotic entry, cortical nodes mature and then compact into a contractile ring positioned in the cell middle. The molecular link between Mid1 and medial cortical nodes remains poorly defined. Here we show that Blt1, a previously enigmatic cortical node protein, promotes the robust association of Mid1 with cortical nodes. Blt1 interacts with Mid1 through the RhoGEF Gef2 to stabilize nodes at the cell cortex during the early stages of contractile ring assembly. The Blt1 N terminus is required for localization and function, while the Blt1 C terminus promotes cortical localization by interacting with phospholipids. In cells lacking membrane binding by both Mid1 and Blt1, nodes detach from the cell cortex and generate aberrant cytokinetic rings. We conclude that Blt1 acts as a scaffolding protein for precursors of the cytokinetic ring and that Blt1 and Mid1 provide overlapping membrane anchors for proper division plane positioning.","doi":"10.1128/MCB.01286-12","authors":"Guzman-Vendrell M, Baldissard S, Almonacid M, Mayeux A, Paoletti A, Moseley JB","authors_abbrev":"Guzman-Vendrell M et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2012-11-15","publication_year":"2013","canto_session_key":"d77c8e04bc2a8fba","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPAC57A10.02","SPBC1A4.05","SPAC31A2.16"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:19502236","title":"Both Php4 function and subcellular localization are regulated by iron via a multistep mechanism involving the glutaredoxin Grx4 and the exportin Crm1.","citation":"J Biol Chem 2009 Jul 24;284(30):20249-62","abstract":"In Schizosaccharomyces pombe, the CCAAT-binding factor is a multisubunit complex that contains the proteins Php2, Php3, Php4, and Php5. Under low iron conditions, Php4 acts as a negative regulatory subunit of the CCAAT-binding factor and fosters repression of genes encoding iron-using proteins. Under conditions of iron excess, Php4 expression is turned off by the iron-dependent transcriptional repressor Fep1. In this study, we developed a biological system that allows us to unlink iron-dependent behavior of Php4 protein from its transcriptional regulation by Fep1. Microscopic analyses revealed that a functional GFP-Php4 protein accumulates in the nucleus under conditions of iron starvation. Conversely, in cells undergoing a transition from low to high iron, GFP-Php4 is exported from the nucleus to the cytoplasm. We mapped a leucine-rich nuclear export signal that is necessary for nuclear exclusion of Php4. This latter process was blocked by leptomycin B. By using coimmunoprecipitation analysis, we showed that Php4 and Crm1 physically interact with each other. Although we determined that nuclear retention of Php4 per se is not sufficient to cause a constitutive repression of iron-using genes, we found that deletion of the grx4(+)-encoded glutaredoxin-4 renders Php4 constitutively active and invariably localized in the nucleus. Further analysis by bimolecular fluorescence complementation assay and by two-hybrid assays showed that Php4 and Grx4 are physically associated in vivo. Taken together, our findings indicate that Grx4 and Crm1 are novel components involved in the mechanism by which Php4 is inactivated by iron in a Fep1-independent manner.","doi":"10.1074/jbc.M109.009563","authors":"Mercier A, Labbé S","authors_abbrev":"Mercier A et al.","pubmed_publication_date":"24 Jul 2009","pubmed_entrez_date":"2009-06-09","publication_year":"2009","canto_session_key":"f86a4c2ed458dac5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-09 12:06:20","canto_approved_date":"2026-06-17 13:13:05","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-09 12:06:14","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":25,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16E9.01c","SPCC645.03c","SPAC1805.17","SPBC26H8.06"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2024-08-09"},{"uniquename":"PMID:40441328","title":"Influence of H3K9 methylation on gene mutation rates in yeast: Advancing epigenetic research with controlled experimental design.","citation":"Fungal Genet Biol 2025 May 27;:104003","abstract":"Mutations drive genetic variation, fueling both oncogenesis and species evolution. The mutation rate varies across the genome, potentially influenced by chromatin organization through histone modifications and other factors. However, the precise relationship between chromatin structure and mutation rate remains poorly understood and needs further investigation. One such modification, the methylation of histone H3 at lysine 9 (H3K9me), is known to form heterochromatin and repress transcription in euchromatin, thereby maintaining genome stability essential for organism survival. This study aimed to elucidate the effect of H3K9 methylation, in isolation from other histone markers, on the mutation rate in fission yeast. Employing fluctuation assays and statistical analysis, our innovative methodology estimates the mutation rates of a single gene under two different conditions within a single experiment using an isogenic clone in Fission yeast. Our findings highlight a potential association between H3K9 methylation and the phenotypic mutation rate of the same gene, ura4 + . For prospective researchers, this study introduces a new experimental approach that offers unprecedented accuracy in gene analysis, with implications for both genetic research and epigenetic therapy.","doi":"10.1016/j.fgb.2025.104003","authors":"Abdalla O, Walker C","authors_abbrev":"Abdalla O et al.","pubmed_publication_date":"27 May 2025","pubmed_entrez_date":"2025-05-29","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-05-30 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25598145","title":"Diverse mechanisms for spliceosome-mediated 3' end processing of telomerase RNA.","citation":"Nat Commun 2015 Jan 19;6:6104","abstract":"The 3' end of Schizosaccharomyces pombe telomerase RNA (SpTER1) is generated by spliceosomal cleavage, a reaction that corresponds to the first step of splicing. The observation that the spliceosome functions in 3' end processing raised questions about the evolutionary origin and conservation of this mechanism. We now present data in support of spliceosomes generating 3' ends of telomerase RNAs in other fungi. Strikingly, the mechanistic basis for restricting spliceosomal splicing to the first transesterification reaction differs substantially among species. Unlike S. pombe, two other fission yeasts rely on hyperstabilization of the U6 snRNA-5' splice site interaction to impede the 2nd step of splicing. In contrast, a non-canonical 5' splice site blocks the second transesterification reaction in Aspergillus species. These results demonstrate a conserved role for spliceosomes functioning in 3' end processing. Divergent mechanisms of uncoupling the two steps of splicing argue for multiple origins of this pathway.","doi":"10.1038/ncomms7104","authors":"Kannan R, Helston RM, Dannebaum RO, Baumann P","authors_abbrev":"Kannan R et al.","pubmed_publication_date":"19 Jan 2015","pubmed_entrez_date":"2015-01-20","publication_year":"2015","canto_session_key":"e67e273f28fdb46f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-01-21 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12171939","title":"Oligomerization-dependent association of the SAM domains from Schizosaccharomyces pombe Byr2 and Ste4.","citation":"J Biol Chem 2002 Oct 18;277(42):39585-93","abstract":"SAM (sterile alpha motif) domains are protein-protein interaction modules found in a large number of regulatory proteins. Byr2 and Ste4 are two SAM domain-containing proteins in the mating pheromone response pathway of the fission yeast, Schizosaccharomyces pombe. Byr2 is a mitogen-activated protein kinase kinase kinase that is regulated by Ste4. Tu et al. (Tu, H., Barr, M., Dong, D. L., and Wigler, M. (1997) Mol. Cell. Biol. 17, 5876-5887) showed that the isolated SAM domain of Byr2 binds a fragment of Ste4 that contains both a leucine zipper (Ste4-LZ) domain as well as a SAM domain, suggesting that Byr2-SAM and Ste4-SAM may form a hetero-oligomer. Here, we show that the individual SAM domains of Ste4 and Byr2 are monomeric at low concentrations and bind to each other in a 1:1 stoichiometry with a relatively weak dissociation constant of 56 +/- 3 microm. Inclusion of the Ste4-LZ domain, which determines the oligomeric state of Ste4, has a dramatic effect on binding affinity, however. We find that the Ste4-LZ domain is trimeric and, when included with the Ste4-SAM domain, yields a 3:1 Ste4-LZ-SAM:Byr2-SAM complex with a tight dissociation constant of 19 +/- 4 nm. These results suggest that the Ste4-LZ-SAM protein may recognize multiple binding sites on Byr2-SAM, indicating a new mode of oligomeric organization for SAM domains. The fact that high affinity binding occurs only with the addition of an oligomerization domain suggests that it may be necessary to include ancillary oligomerization modules when searching for binding partners of SAM domains.","authors":"Ramachander R, Kim CA, Phillips ML, Mackereth CD, Thanos CD, McIntosh LP, Bowie JU","authors_abbrev":"Ramachander R et al.","pubmed_publication_date":"18 Oct 2002","pubmed_entrez_date":"2002-08-13","publication_year":"2002","canto_session_key":"94a3906082f94a67","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-28 13:31:59","canto_approved_date":"2018-04-28 14:25:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-04-28 13:31:51","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1D7.05","SPAC1565.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-04-28"},{"uniquename":"PMID:16738605","title":"Telomeric proteins: clearing the way for the replication fork.","citation":"Nat Struct Mol Biol 2006 May;13(5):386-7","abstract":"Protein complexes at telomeres have been assumed to present an obstacle to the passing replication fork. The observation that the Schizosaccharomyces pombe telomere-binding protein Taz1 is required for replication suggests otherwise.","authors":"Karlseder J","authors_abbrev":"Karlseder J","pubmed_publication_date":"May 2006","pubmed_entrez_date":"2006-06-02","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19758558","title":"CENP-C functions as a scaffold for effectors with essential kinetochore functions in mitosis and meiosis.","citation":"Dev Cell 2009 Sep;17(3):334-43","abstract":"The conserved kinetochore protein CENP-C plays a fundamental role in chromosome segregation, but its specific functions remain elusive. We have gained insights into the role of CENP-C through identification of interacting effector proteins required for kinetochore function in fission yeast. Fta1/CENP-L is a primary effector that associates directly with Cnp3/CENP-C, and ectopic localization of Fta1 largely suppresses the mitotic kinetochore defects of cnp3Delta cells. Pcs1 functions downstream of Cnp3 to prevent merotelic attachment. In meiosis, Cnp3 further associates with and recruits Moa1, a meiosis-specific protein exclusively required for the mono-orientation of kinetochores. Genetic and biochemical analyses identified Cnp3 mutants that preserve intact mitotic kinetochore function but abolish the association with Moa1 and meiotic mono-orientation. Overall, therefore, our studies identify effectors of CENP-C in mitosis and meiosis and establish the concept that CENP-C serves as a scaffold for the specific recruitment of essential kinetochore proteins.","doi":"10.1016/j.devcel.2009.08.004","authors":"Tanaka K, Chang HL, Kagami A, Watanabe Y","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-09-18","publication_year":"2009","canto_session_key":"20128de7e05e2f96","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-11 13:01:49","canto_approved_date":"2026-01-30 07:47:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-18 16:31:07","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":65,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15E1.07c","SPAC11E3.03","SPBC800.13","SPBC1861.01c","SPBC1105.17","SPAC23C11.15","SPAC4F10.12","SPBC18E5.03c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2016-10-11"},{"uniquename":"PMID:8354238","title":"Capillary zone electrophoresis of large DNA.","citation":"Electrophoresis 1993;14(5-6):523-30","abstract":"Capillary zone electrophoresis (CZE) of DNA 23.1 to 48.5 kb in length in polyacrylamide solutions of several concentrations provides evidence for polymer concentration and DNA length-dependent stretching and orientation of these species and suggests an effective separation at a polymer concentration of about 0.6%. Applying a 0.1% polyacrylamide concentration to the lambda-phage DNA ladder, at least 5 components are separated; separation improves with lowering of the field strength to 2 V/cm and, correspondingly, extended duration of CZE. Saccharomyces pombe chromosomal DNA separates into 3 major components on CZE at high field strength (270 V/cm) in 0.9% polyacrylamide solution, confirming a previous finding made on electrophoresis in a 1.1 mm ID tube at low field strength. However, the finding is limited to one source of the DNA plug, and the chromosomal identity of the components remains unknown. Methodological problems in the CZE of large DNA relate to the need for extended duration of pressure injection if absorbance detection is applied, the need to define the starting zone after extended pressure injection, the need to melt and digest agarose plugs prior to loading, and related needs for thermostating of the sample chamber and for software compatible with low voltage operation.","authors":"Guszczynski T, Pulyaeva H, Tietz D, Garner MM, Chrambach A","authors_abbrev":"Guszczynski T et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-05-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6120168","title":"Potassium transport coupled to ATP hydrolysis in reconstituted proteoliposomes of yeast plasma membrane ATPase.","citation":"J Biol Chem 1982 Feb 25;257(4):1824-8","abstract":"Potassium transport coupled to ATP hydrolysis has been reconstituted in proteoliposomes using a highly purified plasma membrane Mg2+-dependent ATPase of the yeast Schizosaccharomyces pombe. The ATPase activity in the incorporated enzyme was strongly stimulated (2.2-fold) by the H+-conducting agent carbonyl cyanide m-chlorophenylhydrazone (CCCP). The H+/K+ exchanger nigericin (in the presence of K+) stimulated 1.6-fold the ATPase activity. When both ionophores were added together, the stimulation was increased up to 2.7-fold. When a potassium concentration gradient (high K+ in) was applied to the proteoliposome membrane, a significant drop in the CCCP-stimulated ATPase activity was observed. Inversion of the K+ concentration gradient (high K+ out) did not decrease the stimulation by CCCP. High Na+ in also decreased the stimulation induced by CCCP in the absence but not in the presence of external K+. However, high Li+ in had no effect. Direct potassium efflux from the proteolyposomes was detected upon addition of MgATP using a selective K+ electrode. The ATP-dependent potassium efflux was abolished in CCCP and/or nigericin-pretreated proteoliposomes. However, during steady state ATP hydrolysis, a transient and small K+ efflux was observed upon addition of a CCCP pulse. I propose that the plasma membrane Mg2+-dependent ATPase in yeast cells not only carries out electrogenic H+ ejection but also drives the uptake of potassium via a voltage-sensitive gate which is closed in the absence and open in the presence of the membrane potential.","authors":"Villalobo A","authors_abbrev":"Villalobo A","pubmed_publication_date":"25 Feb 1982","pubmed_entrez_date":"1982-02-25","publication_year":"1982","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21145239","title":"Three's company: the fission yeast actin cytoskeleton.","citation":"Trends Cell Biol 2011 Mar;21(3):177-87","abstract":"How the actin cytoskeleton assembles into different structures to drive diverse cellular processes is a fundamental cell biological question. In addition to orchestrating the appropriate combination of regulators and actin-binding proteins, different actin-based structures must insulate themselves from one another to maintain specificity within a crowded cytoplasm. Actin specification is particularly challenging in complex eukaryotes where a multitude of protein isoforms and actin structures operate within the same cell. Fission yeast Schizosaccharomyces pombe possesses a single actin isoform that functions in three distinct structures throughout the cell cycle. In this review we explore recent studies in fission yeast that help unravel how different actin structures operate in cells.","doi":"10.1016/j.tcb.2010.11.001","authors":"Kovar DR, Sirotkin V, Lord M","authors_abbrev":"Kovar DR et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2010-12-15","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8001792","title":"Glucose repression of fbp1 transcription of Schizosaccharomyces pombe is partially regulated by adenylate cyclase activation by a G protein alpha subunit encoded by gpa2 (git8).","citation":"Genetics 1994 Sep;138(1):39-45","abstract":"In the fission yeast Schizosaccharomyces pombe, genetic studies have identified genes that are required for glucose repression of fbp1 transcription. The git2 gene, also known as cyr1, encodes adenylate cyclase. Adenylate cyclase converts ATP into the second messenger cAMP as part of many eukaryotic signal transduction pathways. The git1, git3, git5, git7, git8 and git10 genes act upstream of adenylate cyclase, presumably encoding an adenylate cyclase activation pathway. In mammalian cells, adenylate cyclase enzymatic activity is regulated by heterotrimeric guanine nucleotide-binding proteins (G proteins). In the budding yeast Saccharomyces cerevisiae, adenylate cyclase enzymatic activity is regulated by monomeric, guanine nucleotide-binding Ras proteins. We show here that git8 is identical to the gpa2 gene that encodes a protein homologous to the alpha subunit of a G protein. Mutations in two additional genes, git3 and git5 are suppressed by gpa2+ in high copy number. Furthermore, a mutation in either git3 or git5 has an additive effect in strains deleted for gpa2 (git8), as it significantly increases expression of an fbp1-lacZ reporter gene. Therefore, git3 and git5 appear to act either in concert with or independently from gpa2 (git8) to regulate adenylate cyclase activity.","authors":"Nocero M, Isshiki T, Yamamoto M, Hoffman CS","authors_abbrev":"Nocero M et al.","pubmed_publication_date":"Sep 1994","pubmed_entrez_date":"1994-09-01","publication_year":"1994","canto_session_key":"30f38f2aa9fa78d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-02-15 17:19:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-08-14 09:58:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21C3.20c","SPBC19C7.03","SPAC926.04c","SPBC36.12c","SPBC32H8.07","SPBC1198.14c","SPAC23H3.13c","SPCC1753.02c","SPBC106.10"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2012-08-14"},{"uniquename":"PMID:2516868","title":"Cell wall formation in regenerating protoplasts of Schizosaccharomyces pombe: study by high resolution, low voltage scanning electron microscopy.","citation":"J Electron Microsc (Tokyo) 1989;38(6):457-68","abstract":"The ultrastructure of regenerating cell wall in Schizosaccharomyces pombe protoplasts was studied with a high resolution, low voltage scanning electron microscope (LVSEM). In contrast to the transmission electron microscopy, the LVSEM images give three-dimensional information on the cell wall regeneration in yeast protoplasts. We found that, after only a few minutes of incubation, the protoplasts began to show protuberances in a unipolar manner, and a fibrilar network was formed asymmetrically which covered the whole surface of the protoplasts after 5 hr. The network consisted of microfibrils about 8 to 10 nm wide, forming flat and wavy bundles of various widths and lengths, up to about 200 nm wide and 1 micron long, mainly made of yeast glucan. Free ends of microfibrils were seldom found. Interfibrillar spaces were progressively filled with granular particles and finally the complete cell wall was formed after 12 hr. The fibrillar network was destroyed by the digestion with beta (1----3)-glucanase. When protoplasts were regenerating in the presence of aculeacin A, the fibrillar networks were not formed, resulting in incomplete cell wall formation. These observations suggest that beta-glucan is the main component of the microfibrils and that it plays an important role in the formation of the cell wall in S. pombe.","authors":"Osumi M, Yamada N, Kobori H, Taki A, Naito N, Baba M, Nagatani T","authors_abbrev":"Osumi M et al.","pubmed_publication_date":"1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21445296","title":"Mis17 is a regulatory module of the Mis6-Mal2-Sim4 centromere complex that is required for the recruitment of CenH3/CENP-A in fission yeast.","citation":"PLoS One 2011 Mar 21;6(3):e17761","abstract":"The centromere is the chromosome domain on which the mitotic kinetochore forms for proper segregation. Deposition of the centromeric histone H3 (CenH3, CENP-A) is vital for the formation of centromere-specific chromatin. The Mis6-Mal2-Sim4 complex of the fission yeast S. pombe is required for the recruitment of CenH3 (Cnp1), but its function remains obscure.\nMass spectrometry was performed on the proteins precipitated with Mis6- and Mis17-FLAG. The results together with the previously identified Sim4- and Mal2-TAP precipitated proteins indicated that the complex contains 12 subunits, Mis6, Sim4, Mal2, Mis15, Mis17, Cnl2, Fta1-4, Fta6-7, nine of which have human centromeric protein (CENP) counterparts. Domain dissection indicated that the carboxy-half of Mis17 is functional, while its amino-half is regulatory. Overproduction of the amino-half caused strong negative dominance, which led to massive chromosome missegregation and hypersensitivity to the histone deacetylase inhibitor TSA. Mis17 was hyperphosphorylated and overproduction-induced negative dominance was abolished in six kinase-deletion mutants, ssp2 (AMPK), ppk9 (AMPK), ppk15 (Yak1), ppk30 (Ark1), wis4 (Ssk2), and lsk1 (P-TEFb).\nMis17 may be a regulatory module of the Mis6 complex. Negative dominance of the Mis17 fragment is exerted while the complex and CenH3 remain at the centromere, a result that differs from the mislocalization seen in the mis17-362 mutant. The known functions of the kinases suggest an unexpected link between Mis17 and control of the cortex actin, nutrition, and signal/transcription. Possible interpretations are discussed.","doi":"10.1371/journal.pone.0017761","authors":"Shiroiwa Y, Hayashi T, Fujita Y, Villar-Briones A, Ikai N, Takeda K, Ebe M, Yanagida M","authors_abbrev":"Shiroiwa Y et al.","pubmed_publication_date":"21 Mar 2011","pubmed_entrez_date":"2011-03-30","publication_year":"2011","canto_session_key":"4a36913fd1f9b7a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-12-19 09:27:29","canto_approved_date":"2025-12-08 19:28:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-18 16:26:28","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.01","SPAC11H11.05c","SPBP8B7.12c","SPBC11C11.03","SPBC31F10.06c","SPAC4F10.12","SPCC1393.04","SPAC25B8.14","SPAC16A10.05c","SPAC9G1.02","SPAC17C9.06","SPBC409.04c","SPBC6B1.02","SPAC29A4.08c","SPAC23H4.11c","SPAC823.03","SPAC2F3.15","SPBP22H7.09c","SPBC18E5.03c","SPCC1235.07","SPAC23H4.02","SPAC1687.20c","SPAC1783.03","SPCC74.03c"],"gene_count":24,"ltp_gene_count":18,"approved_date":"2014-12-19"},{"uniquename":"EMBL:AB084879","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.67"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17804800","title":"Mei4p coordinates the onset of meiosis I by regulating cdc25+ in fission yeast.","citation":"Proc Natl Acad Sci U S A 2007 Sep 11;104(37):14688-93","abstract":"The kinase Cdc2p is a central regulator of entry into and progression through nuclear division during mitosis and meiosis in eukaryotes. Cdc2p is activated at the onset of mitosis by dephosphorylation on tyrosine-15, the phosphorylation status of which is determined mainly by the kinase Wee1p and the phosphatase Cdc25p. In fission yeast, the forkhead-type transcription factor Mei4p is required for expression of many genes during meiosis, with mei4 mutant cells arresting before meiosis I. The mechanism of cell cycle arrest in mei4 cells has remained unknown, however. We now show that cdc25(+) is an important target of Mei4p in control of entry into meiosis I. Forced dephosphorylation of Cdc2p on tyrosine-15 thus induced meiosis I in mei4 mutant cells without a delay, although no spores were formed. We propose that Mei4p acts as a rate-limiting regulator of meiosis I by activating cdc25(+) transcription in coordination with other meiotic events.","authors":"Murakami-Tonami Y, Yamada-Namikawa C, Tochigi A, Hasegawa N, Kojima H, Kunimatsu M, Nakanishi M, Murakami H","authors_abbrev":"Murakami-Tonami Y et al.","pubmed_publication_date":"11 Sep 2007","pubmed_entrez_date":"2007-09-07","publication_year":"2007","canto_session_key":"0cad091b0886ebbf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-27 10:09:13","canto_approved_date":"2021-10-14 10:49:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-16 17:53:41","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC1778.04","SPBC32H8.11","SPBC11B10.09","SPCC18B5.03","SPBC660.14"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-04-27"},{"uniquename":"EMBL:AU010322","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.86"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16355535","title":"Regulation of actin assembly by microtubules in fission yeast cell polarity.","citation":"Novartis Found Symp 2005;269:59-66; discussion 66-72, 223-30","abstract":"It has been speculated that microtubule plus ends function to regulate the actin cytoskeleton in processes such as cytokinesis, cell polarization and cell migration. In the fission yeast Schizosaccharomyces pombe, interphase microtubules regulate cell polarity through proteins such as tea1p, a kelch repeat protein, and for3p, a formin that nucleates actin cable assembly at cell tips. Here, we review recent progress on understanding tea1p regulation and function. Microtubules may govern the localization of tea1p by transporting it on the plus ends of microtubules and depositing it directly onto the cell tip when the microtubule catastrophes. The interaction of tea1p with the CLIP170 protein tip1p is responsible for its localization at growing microtubule plus ends. Tea1p may regulate cell polarity by associating with large 'polarisome' complexes that include for3p. For3p is present at both cell tips, but is not on the microtubules. Tea1p is needed to localize the formin to establish polarized cell growth at cell tips that have not grown previously. These studies begin to elucidate a molecular pathway for how microtubules contribute to the proper spatial regulation of actin assembly and polarized cell growth.","authors":"Chang F, Feierbach B, Martin S","authors_abbrev":"Chang F et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-12-17","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41353921","title":"Actin dynamics during contractile ring assembly drives mitotic nuclear displacement in fission yeast.","citation":"Biochem Biophys Res Commun 2025 Dec 04;795:153098","abstract":"Nuclear positioning during mitosis is crucial for cell survival, yet its regulation remains unclear. We previously observed that, during a prolonged mitotic arrest in fission yeast, the nucleus becomes displaced from the cell center in an actin-dependent manner. Here, we examined the role of actin cable dynamics in nuclear displacement, which is essential for contractile actomyosin ring (CAR) assembly. Time-lapse imaging revealed that nuclear movement begins before CAR formation. Further genetic analysis indicated that proper CAR assembly is a prerequisite for mitotic nuclear displacement. Forced tethering of the actin-cable-nucleator formin to the nuclear pore component altered actin cable localization and abolished nuclear displacement, underscoring the importance of non-medial actin cable transport required for CAR assembly. These findings demonstrate that nuclear displacement is driven by the spatial organization of actin cables during CAR assembly, providing new insight into the mechanical regulation of nuclear positioning.","doi":"10.1016/j.bbrc.2025.153098","authors":"Hwang W, Toda T, Yukawa M","authors_abbrev":"Hwang W et al.","pubmed_publication_date":"04 Dec 2025","pubmed_entrez_date":"2025-12-07","publication_year":"2025","canto_session_key":"5f2467f3cea0e613","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-09 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11163211","title":"The spike of S phase cyclin Cig2 expression at the G1-S border in fission yeast requires both APC and SCF ubiquitin ligases.","citation":"Mol Cell 2000 Dec;6(6):1377-87","abstract":"We describe a novel set of oscillation mechanisms for the fission yeast S phase cyclin Cig2, which contains an authentic destruction box and is destroyed at anaphase via the APC/cyclosome (APC/C). Unlike the mitotic cyclin Cdc13, however, Cig2 mRNA and protein peak at the G1/S boundary and decline to low levels in G2 and M phases. We show here that SCF(Pop1, Pop2) plays a role in transcriptional periodicity, as pop mutations result in constitutive cig2(+) transcripts. The instability of Cig2 during G2 and M is independent of either the APC/C or Pop1/Pop2, but requires Skp1, a core component of SCF. These data indicate that the APC/C and SCF control Cig2 levels differentially at different stages of the cell cycle.","authors":"Yamano H, Kitamura K, Kominami K, Lehmann A, Katayama S, Hunt T, Toda T","authors_abbrev":"Yamano H et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2001-02-13","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAPB2B4.03","SPBC409.05","SPBC32F12.09"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:26912660","title":"Gad8 Protein Is Found in the Nucleus Where It Interacts with the MluI Cell Cycle Box-binding Factor (MBF) Transcriptional Complex to Regulate the Response to DNA Replication Stress.","citation":"J Biol Chem 2016 Apr 22;291(17):9371-81","abstract":"The target of rapamycin (TOR) kinase is found at the core of two evolutionarily conserved complexes known as TOR complexes 1 and 2 (TORC1 and TORC2). In fission yeast, TORC2 is dispensable for proliferation under optimal growth conditions but is required for starvation and stress responses. We have previously reported that loss of function of TORC2 renders cells highly sensitive to DNA replication stress; however, the mechanism underlying this sensitivity is unknown. TORC2 has one known direct substrate, the kinase Gad8, which is related to AKT in human cells. Here we show that both TORC2 and its substrate Gad8 are found in the nucleus and are bound to the chromatin. We also demonstrate that Gad8 physically interacts with the MluI cell cycle box-binding factor (MBF) transcription complex that regulates the G1/S progression and the response to DNA stress. In mutant cells lacking TORC2 or Gad8, the binding of the MBF complex to its cognate promoters is compromised, and the induction of MBF target genes in response to DNA replication stress is reduced. Consistently, the protein levels of Cdt2 and Cig2, two MBF target genes, are reduced in the absence of TORC2-Gad8 signaling. Taken together, our findings highlight critical functions of TORC2 in the nucleus and suggest a role in surviving DNA replication stress via transcriptional regulation of MBF target genes.","doi":"10.1074/jbc.M115.705251","authors":"Cohen A, Kupiec M, Weisman R","authors_abbrev":"Cohen A et al.","pubmed_publication_date":"22 Apr 2016","pubmed_entrez_date":"2016-02-26","publication_year":"2016","canto_session_key":"09a0a50064982418","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronit Weisman","canto_first_approved_date":"2016-03-04 10:34:52","canto_approved_date":"2024-03-28 12:20:14","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-03-01 11:41:02","canto_added_date":"2016-02-28 01:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":49,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ronit Weisman","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC22F3.09c","SPAC1F7.05","SPBC660.14","SPBC725.16","SPCC24B10.07","SPBC21B10.13c","SPBC30D10.10c","SPAC17H9.19c","SPAPB2B4.03","SPBC11B10.09","SPBC216.07c","SPBC336.12c","SPBC14C8.07c","SPCC1259.13"],"gene_count":15,"ltp_gene_count":10,"approved_date":"2016-03-04"},{"uniquename":"PMID:26279681","title":"Role of Ccr4-Not complex in heterochromatin formation at meiotic genes and subtelomeres in fission yeast.","citation":"Epigenetics Chromatin 2015;8:28","abstract":"Heterochromatin is essential for chromosome segregation, gene silencing and genome integrity. The fission yeast Schizosaccharomyces pombe contains heterochromatin at centromeres, subtelomeres, and mating type genes, as well as at small islands of meiotic genes dispersed across the genome. This heterochromatin is generated by partially redundant mechanisms, including the production of small interfering RNAs (siRNAs) that are incorporated into the RITS protein complex (RNAi-Induced Transcriptional Silencing). The assembly of heterochromatin islands requires the function of the RNA-binding protein Mmi1, which recruits RITS to its mRNA targets and to heterochromatin islands. In addition, Mmi1 directs its targets to an exosome-dependent RNA elimination pathway.\nCcr4-Not is a conserved multiprotein complex that regulates gene expression at multiple levels, including RNA degradation and translation. We show here that Ccr4-Not is recruited by Mmi1 to its RNA targets. Surprisingly, Ccr4 and Caf1 (the mRNA deadenylase catalytic subunits of the Ccr4-Not complex) are not necessary for the degradation or translation of Mmi1 RNA targets, but are essential for heterochromatin integrity at Mmi1-dependent islands and, independently of Mmi1, at subtelomeric regions. Both roles require the deadenylase activity of Ccr4 and the Mot2/Not4 protein, a ubiquitin ligase that is also part of the complex. Genetic evidence shows that Ccr4-mediated silencing is essential for normal cell growth, indicating that this novel regulation is physiologically relevant. Moreover, Ccr4 interacts with components of the RITS complex in a Mmi1-independent manner.\nTaken together, our results demonstrate that the Ccr4-Not complex is required for heterochromatin integrity in both Mmi1-dependent and Mmi1-independent pathways.","doi":"10.1186/s13072-015-0018-4","authors":"Cotobal C, Rodríguez-López M, Duncan C, Hasan A, Yamashita A, Yamamoto M, Bähler J, Mata J","authors_abbrev":"Cotobal C et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-08-18","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-20 00:18:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4092931","title":"Cloning and characterization of two genes restoring acid phosphatase activity in pho1- mutants of Schizosaccharomyces pombe.","citation":"Gene 1985;39(2-3):223-30","abstract":"Schizosaccharomyces pombe acid phosphatase (APh) is a secreted cell surface glycoprotein which is deficient in pho1 mutants. By screening an S. pombe gene bank for sequences which can functionally rescue the pho1-44 mutation, we have isolated two genomic clones carried in plasmids pSp4B and pSp4C/2. These two sequences map of different genetic loci and show no cross hybridization by Southern blotting. pSp4C/2 was found to contain the PHO1 gene, and cells transformed with this plasmid produce a protein which cross-reacts with antibodies raised against the protein moiety of APh. Data from Northern blotting experiments show that pSp4C/2 encodes a 1.6-kb transcript, and that mRNA levels are increased when cells are grown in low concentrations of inorganic phosphate. The results indicate that pSp4C/2 contains the structural gene for APh, PHO1, whereas pSp4B appears to carry a gene coding for a minor species of APh, PHO4 which is not regulated by extracellular phosphate.","authors":"Maundrell K, Nurse P, Schönholzer F, Schweingruber ME","authors_abbrev":"Maundrell K et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_session_key":"dad0d98fa4da533e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-07 15:04:56","canto_approved_date":"2024-06-22 12:15:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-18 08:25:07","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPBC428.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-12-07"},{"uniquename":"PMID:8972853","title":"Fission yeast genes which disrupt mitotic chromosome segregation when overexpressed.","citation":"Nucleic Acids Res 1996 Dec 01;24(23):4676-83","abstract":"An interference assay has been devised in Schizosaccharomyces pombe to rapidly identify and clone genes involved in chromosome segregation. Random S.pombe cDNAs were overexpressed from an inducible promoter in a strain carrying an additional, non-essential minichromosome. Overexpression of cDNAs derived from four genes, two known (nda3+and ubc4+, encoding beta-tubulin and a ubiquitin conjugating enzyme, respectively) and two unknown, named mlo2+ and mlo3+ (missegregation & lethal when over expressed) caused phenotypes consistent with a failure to segregate chromosomes. Full overexpression of all four cDNAs was lethal. Cells overexpressing nda3+ and ubc4+ cDNAs arrested with condensed unsegregated chromosomes and cells overexpressing mlo2+ displayed an asymmetric distribution of nuclear chromatin. Sublethal levels of overexpression of nda3+, ubc4+ and mlo2+ cDNAs caused elevated rates of minichromosome loss. A third cDNA mlo3+, displayed no increase in the frequency of minichromosome loss at sublethal levels of overexpression but full overexpression caused a complete failure to segregate chromosomes. Our results confirm the assumption that beta-tubulin overexpression is lethal in S.pombe, implicate ubc4+ in the control of metaphase-anaphase transition in fission yeast and finally identify two new genes, mlo2+and mlo3+, likely to play an important role for chromosome transmission fidelity in mitosis.","authors":"Javerzat JP, Cranston G, Allshire RC","authors_abbrev":"Javerzat JP et al.","pubmed_publication_date":"01 Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_session_key":"06b4ab309bde03c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-07 09:16:09","canto_approved_date":"2018-06-07 09:16:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-06-07 09:15:59","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.10c","SPCC31H12.03c","SPBC119.02","SPBC26H8.07c","SPBC4.05","SPBC1D7.04","SPBC32H8.12c","SPAC1687.01","SPAC25G10.07c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2018-06-07"},{"uniquename":"PMID:16002654","title":"Hyphal Growth in the Fission Yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2005 Jul;4(7):1287-97","abstract":"The fission yeast Schizosaccharomyces pombe grows in a single-celled form or can mate and undergo meiosis and sporulation. Here we show that wild-type S. pombe can also differentiate to form elaborately branched hyphae which invade deep into solid medium. Branches appear in the hyphae adjacent to unseparated septa. Electron microscopy reveals unusual multivesicular structures within the hyphae. Nitrogen deprivation appears to be the main stimulus for hyphal growth. No mitogen-activated protein kinase is necessary for the response. Inhibition of cyclic AMP (cAMP) production or signaling prevents the response, and exogenous cAMP promotes it, suggesting that detection of a good carbon source is required for hyphal growth but not for mating.","authors":"Amoah-Buahin E, Bone N, Armstrong J","authors_abbrev":"Amoah-Buahin E et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-07-09","publication_year":"2005","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32213462","title":"Inter-organelle lipid transfer: a channel model for Vps13 and chorein-N motif proteins.","citation":"Curr Opin Cell Biol 2020 Aug;65:66-71","abstract":"Membrane contact sites, where two organelles are in close proximity, are critical regulators of cellular membrane homeostasis, with roles in signaling, lipid metabolism, and ion dynamics. A growing catalog of specialized lipid transfer proteins carry out lipid exchange at these sites. Currently characterized eukaryotic lipid transport proteins are shuttles that typically extract a single lipid from the membrane of the donor organelle, solubilize it during transport through the cytosol, and deposit it in the acceptor organelle membrane. Here, we highlight the recently identified chorein_N family of lipid transporters, including the Vps13 proteins and the autophagy protein Atg2. These are elongated proteins that, distinct from previously characterized transport proteins, bind tens of lipids at once. They feature an extended channel, most likely lined with hydrophobic residues. We discuss the possibility that they are not shuttles but instead are bridges between membranes, with lipids traversing the cytosol via the hydrophobic channel.","doi":"10.1016/j.ceb.2020.02.008","authors":"Lees JA, Reinisch KM","authors_abbrev":"Lees JA et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-03-28","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16C6.02c","SPBC21C3.01c","SPBC31E1.01c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:12764130","title":"The kelch repeat protein, Tea1, is a potential substrate target of the p21-activated kinase, Shk1, in the fission yeast, Schizosaccharomyces pombe.","citation":"J Biol Chem 2003 Aug 08;278(32):30074-82","abstract":"The p21-activated kinase (PAK) homolog, Shk1, is a critical component of a multifunctional Ras/Cdc42/PAK complex required for viability, polarized growth and cell shape, and sexual differentiation in the fission yeast, Schizosaccharomyces pombe. Substrate targets of the Shk1 kinase have not previously been described. Here we show that the S. pombe cell polarity factor, Tea1, is directly phosphorylated by Shk1 in vitro. We demonstrate further that Tea1 is phosphorylated in S. pombe cells and that its level of phosphorylation is significantly reduced in cells defective in Shk1 function. Consistent with a role for Tea1 as a potential downstream effector of Shk1, we show that a tea1 null mutation rescues the Shk1 hyperactivity-induced lethal phenotype caused by loss of function of the essential Shk1 inhibitor, Skb15. All phenotypes associated with Skb15 loss, including defects in actin cytoskeletal organization, chromosome segregation, and cytokinesis, are suppressed by tea1 Delta, suggesting that Tea1 is a potential mediator of multiple Shk1 functions. S. pombe cells carrying a weak hypomorphic allele of shk1 together with a tea1 Delta mutation exhibit a cytokinesis defective phenotype that is significantly more severe than that observed in the respective single mutants, providing evidence that Shk1 and Tea1 cooperate to regulate cytokinesis. In addition, we show that S. pombe cells carrying the orb2-34 allele of shk1 exhibit a pattern of monopolar growth similar to that observed in tea1 Delta cells, suggesting that Shk1 and Tea1 may regulate one or more common processes involved in the regulation of polarized cell growth. Taken together, our results strongly implicate Tea1 as a potential substrate-effector of the Shk1 kinase.","authors":"Kim H, Yang P, Catanuto P, Verde F, Lai H, Du H, Chang F, Marcus S","authors_abbrev":"Kim H et al.","pubmed_publication_date":"08 Aug 2003","pubmed_entrez_date":"2003-05-24","publication_year":"2003","canto_session_key":"b3bc9cbfdcacc24c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-05-30 16:36:22","canto_approved_date":"2024-03-29 09:25:41","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-12-06 12:22:11","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":21,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.06","SPCC16C4.08c","SPBC1604.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-05-30"},{"uniquename":"PMID:27140918","title":"Extraction of Chromosomal DNA from Schizosaccharomyces pombe.","citation":"Cold Spring Harb Protoc 2016 May 02;2016(5)","abstract":"Extraction of DNA from Schizosaccharomyces pombe cells is required for various uses, including templating polymerase chain reactions (PCRs), Southern blotting, library construction, and high-throughput sequencing. To purify high-quality DNA, the cell wall is removed by digestion with Zymolyase or Lyticase and the resulting spheroplasts lysed using sodium dodecyl sulfate (SDS). Cell debris, SDS, and SDS-protein complexes are subsequently precipitated by the addition of potassium acetate and removed by centrifugation. Finally, DNA is precipitated using isopropanol. At this stage, purity is usually sufficient for PCR. However, for more sensitive procedures, such as restriction enzyme digestion, additional purification steps, including proteinase K digestion and phenol-chloroform extraction, are recommended. All of these steps are described in detail here.","doi":"10.1101/pdb.prot090985","authors":"Murray JM, Watson AT, Carr AM","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"02 May 2016","pubmed_entrez_date":"2016-05-04","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-05-05 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21920295","title":"Organelle transport: mitochondria hitch a ride on dynamic microtubules.","citation":"Curr Biol 2011 Sep 13;21(17):R654-6","abstract":"","doi":"10.1016/j.cub.2011.07.035","authors":"Pon LA","authors_abbrev":"Pon LA","pubmed_publication_date":"13 Sep 2011","pubmed_entrez_date":"2011-09-17","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16436428","title":"Homocysteine accumulation causes a defect in purine biosynthesis: further characterization of Schizosaccharomyces pombe methionine auxotrophs.","citation":"Microbiology (Reading) 2006 Feb;152(Pt 2):397-404","abstract":"Methionine synthase (EC2.1.1.14) catalyses the final step in methionine synthesis, i.e. methylation of homocysteine. A search of the Schizosaccharomyces pombe genomic database revealed a gene designated SPAC9.09, encoding a protein with significant homology to methionine synthase. Disruption of SPAC9.09 caused methionine auxotrophy, and thus the gene was identified as a methionine synthase and designated met26. The met26 mutant was found to exhibit a remarkable growth defect in the absence of adenine even in medium supplemented with methionine. This phenotype was not observed in other methionine auxotrophs. In the budding yeast Saccharomyces cerevisiae, which has been reported to utilize homocysteine in cysteine synthesis, lack of a functional methionine synthase did not cause a requirement for adenine. The introduction of genes from Sac. cerevisiae constituting the cystathionine pathway (CYS4 and CYS3) into Sch. pombe Deltamet26 cells restored growth in the absence of adenine. HPLC analysis showed that total homocysteine content in Deltamet26 cells was higher than in other methionine auxotrophs and that introduction of the Sac. cerevisiae cystathionine pathway decreased total homocysteine levels. These data demonstrate that accumulation of homocysteine causes a defect in purine biosynthesis in the met26 mutant.","doi":"10.1099/mic.0.28398-0","authors":"Fujita Y, Ukena E, Iefuji H, Giga-Hama Y, Takegawa K","authors_abbrev":"Fujita Y et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-01-27","publication_year":"2006","canto_session_key":"6baeea8b0c85742f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-06 12:07:32","canto_approved_date":"2026-02-16 16:47:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-06 12:07:25","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9.09","SPBC409.10","SPBC56F2.11","SPAC1782.11","SPAC13G7.06"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-02-06"},{"uniquename":"PMID:24413667","title":"Gathering up meiotic telomeres: a novel function of the microtubule-organizing center.","citation":"Cell Mol Life Sci 2014 Jun;71(11):2119-34","abstract":"During meiosis, telomeres cluster and promote homologous chromosome pairing. Telomere clustering depends on conserved SUN and KASH domain nuclear membrane proteins, which form a complex called the linker of nucleoskeleton and cytoskeleton (LINC) and connect telomeres with the cytoskeleton. It has been thought that LINC-mediated cytoskeletal forces induce telomere clustering. However, how cytoskeletal forces induce telomere clustering is not fully understood. Recent study of fission yeast has shown that the LINC complex forms the microtubule-organizing center (MTOC) at the telomere, which has been designated as the \"telocentrosome\", and that microtubule motors gather telomeres via telocentrosome-nucleated microtubules. This MTOC-dependent telomere clustering might be conserved in other eukaryotes. Furthermore, the MTOC-dependent clustering mechanism appears to function in various other biological events. This review presents an overview of the current understanding of the mechanism of meiotic telomere clustering and discusses the universality of the MTOC-dependent clustering mechanism.","doi":"10.1007/s00018-013-1548-1","authors":"Yamamoto A","authors_abbrev":"Yamamoto A","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-01-14","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34279603","title":"Response to sulfur in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2021 Jul 24;21(5)","abstract":"Sulfur is an essential component of various biologically important molecules, including methionine, cysteine and glutathione, and it is also involved in coping with oxidative and heavy metal stress. Studies using model organisms, including budding yeast (Saccharomyces cerevisiae) and fission yeast (Schizosaccharomyces pombe), have contributed not only to understanding various cellular processes but also to understanding the utilization and response mechanisms of each nutrient, including sulfur. Although fission yeast can use sulfate as a sulfur source, its sulfur metabolism pathway is slightly different from that of budding yeast because it does not have a trans-sulfuration pathway. In recent years, it has been found that sulfur starvation causes various cellular responses in S. pombe, including sporulation, cell cycle arrest at G2, chronological lifespan extension, autophagy induction and reduced translation. This MiniReview identifies two sulfate transporters in S. pombe, Sul1 (encoded by SPBC3H7.02) and Sul2 (encoded by SPAC869.05c), and summarizes the metabolic pathways of sulfur assimilation and cellular response to sulfur starvation. Understanding these responses, including metabolism and adaptation, will contribute to a better understanding of the various stress and nutrient starvation responses and chronological lifespan regulation caused by sulfur starvation.","doi":"10.1093/femsyr/foab041","authors":"Ohtsuka H, Shimasaki T, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"24 Jul 2021","pubmed_entrez_date":"2021-07-19","publication_year":"2021","canto_session_key":"e6d8d31b0daf77a7","canto_annotation_status":"APPROVED","canto_triage_status":"Review or comment","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2021-08-03 14:45:38","canto_approved_date":"2024-08-01 14:35:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-07-29 02:06:04","canto_added_date":"2021-07-21 00:15:04","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":3,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3H7.02","SPAC869.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-08-03"},{"uniquename":"PMID:20959444","title":"Ergosterol regulates sterol regulatory element binding protein (SREBP) cleavage in fission yeast.","citation":"J Biol Chem 2010 Dec 24;285(52):41051-61","abstract":"In fission yeast, the endoplasmic reticulum membrane-bound proteins Sre1 and Scp1, orthologs of mammalian sterol regulatory element binding protein (SREBP) and Scap, monitor sterol synthesis as an indirect measure of oxygen supply. When cellular oxygen levels are low, sterol synthesis is inhibited, and the Sre1-Scp1 complex responds by increasing transcription of genes required for adaptation to hypoxia. Sre1 and Scp1 are believed to detect a blockage in sterol synthesis by monitoring levels of particular sterols, but the evidence concerning which sterol signals this condition is unclear. Here, we demonstrate that Sre1-Scp1 senses ergosterol. Processing experimental data with a mathematical model of Sre1 and Scp1 function reveals a clear quantitative relationship between ergosterol concentration in the endoplasmic reticulum and Sre1 activation. Based on this relationship, we predict that the Sre1-Scp1 complex exists under \"active\" and \"inactive\" states and that the transition between these states is cooperatively mediated by ergosterol.","doi":"10.1074/jbc.M110.144337","authors":"Porter JR, Burg JS, Espenshade PJ, Iglesias PA","authors_abbrev":"Porter JR et al.","pubmed_publication_date":"24 Dec 2010","pubmed_entrez_date":"2010-10-21","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010734","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR12126","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1840.09","HGNC:7693"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33099217","title":"The necessity of NEDD8/Rub1 for vitality and its association with mitochondria-derived oxidative stress.","citation":"Redox Biol 2020 Oct;37:101765","abstract":"Access of molecular oxygen to the respiratory electron transport chain at the mitochondria costs in the generation of reactive oxygen-derived species (ROS). ROS induces progressive damage to macromolecules in all living cells, hence, rapid defense mechanisms to maintain cellular redox homeostasis are vital. NEDD8/Rub1 is a highly conserved ubiquitin-like modifier that has recently been identified as a key regulator of cellular redox homeostasis. In this review, I will present NEDD8/Rub1, its modification cascade of enzymes, substrates and hydrolases. After introduction, I will show that the NEDD8/Rub1 pathway is linked with mitochondria physiology, namely, oxidative stress. In the rest of the review, I will approach the Ascomycota phylum of the kingdom fungi instrumentally, to present existing links between NEDD8/Rub1 vitality and the aerobic lifestyle of model species belonging to three subphyla: Saccharomycotina (S. cerevisiae and C. albicans), Pezizomycotina (A. nidulans and N. crassa), and Taphrinomycotina (S. pombe).","doi":"10.1016/j.redox.2020.101765","authors":"Pick E","authors_abbrev":"Pick E","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-10-25","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-10-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35950759","title":"A Computational Toolbox to Investigate the Metabolic Potential and Resource Allocation in Fission Yeast.","citation":"mSystems 2022 Aug 30;7(4):e0042322","abstract":"The fission yeast, Schizosaccharomyces pombe, is a popular eukaryal model organism for cell division and cell cycle studies. With this extensive knowledge of its cell and molecular biology, S. pombe also holds promise for use in metabolism research and industrial applications. However, unlike the baker's yeast, Saccharomyces cerevisiae, a major workhorse in these areas, cell physiology and metabolism of S. pombe remain less explored. One way to advance understanding of organism-specific metabolism is construction of computational models and their use for hypothesis testing. To this end, we leverage existing knowledge of S. cerevisiae to generate a manually curated high-quality reconstruction of S. pombe 's  metabolic network, including a proteome-constrained version of the model. Using these models, we gain insights into the energy demands for growth, as well as ribosome kinetics in S. pombe. Furthermore, we predict proteome composition and identify growth-limiting constraints that determine optimal metabolic strategies under different glucose availability regimes and reproduce experimentally determined metabolic profiles. Notably, we find similarities in metabolic and proteome predictions of S. pombe with S. cerevisiae, which indicate that similar cellular resource constraints operate to dictate metabolic organization. With these cases, we show, on the one hand, how these models provide an efficient means to transfer metabolic knowledge from a well-studied to a lesser-studied organism, and on the other, how they can successfully be used to explore the metabolic behavior and the role of resource allocation in driving different strategies in fission yeast.  IMPORTANCE  Our understanding of microbial metabolism relies mostly on the knowledge we have obtained from a limited number of model organisms, and the diversity of metabolism beyond the handful of model species thus remains largely unexplored in mechanistic terms. Computational modeling of metabolic networks offers an attractive platform to bridge the knowledge gap and gain new insights into physiology of lesser-studied organisms. Here we showcase an example of successful knowledge transfer from the budding yeast Saccharomyces cerevisiae to a popular model organism in molecular and cell biology, fission yeast Schizosaccharomyces pombe, using computational models.","doi":"10.1128/msystems.00423-22","authors":"Grigaitis P, Grundel DAJ, van Pelt-KleinJan E, Isaku M, Xie G, Mendoza Farias S, Teusink B, van Heerden JH","authors_abbrev":"Grigaitis P et al.","pubmed_publication_date":"30 Aug 2022","pubmed_entrez_date":"2022-08-11","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-08-13 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC03862","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26068101","title":"Evolution of the SH3 Domain Specificity Landscape in Yeasts.","citation":"PLoS One 2015;10(6):e0129229","abstract":"To explore the conservation of Src homology 3 (SH3) domain-mediated networks in evolution, we compared the specificity landscape of these domains among four yeast species, Saccharomyces cerevisiae, Ashbya gossypii, Candida albicans, and Schizosaccharomyces pombe, encompassing 400 million years of evolution. We first aligned and catalogued the families of SH3-containing proteins in these four species to determine the relationships between homologous domains. Then, we tagged and purified all soluble SH3 domains (82 in total) to perform a quantitative peptide assay (SPOT) for each SH3 domain. All SPOT readouts were hierarchically clustered and we observed that the organization of the SH3 specificity landscape in three distinct profile classes remains conserved across these four yeast species. We also produced a specificity profile for each SH3 domain from manually aligned top SPOT hits and compared the within-family binding motif consensus. This analysis revealed a striking example of binding motif divergence in a C. albicans Rvs167 paralog, which cannot be explained by overall SH3 sequence or interface residue divergence, and we validated this specificity change with a yeast two-hybrid (Y2H) assay. In addition, we show that position-weighted matrices (PWM) compiled from SPOT assays can be used for binding motif screening in potential binding partners and present cases where motifs are either conserved or lost among homologous SH3 interacting proteins. Finally, by comparing pairwise SH3 sequence identity to binding profile correlation we show that for ~75% of all analyzed families the SH3 specificity profile was remarkably conserved over a large evolutionary distance. Thus, a high sequence identity within an SH3 domain family predicts conserved binding specificity, whereas divergence in sequence identity often coincided with a change in binding specificity within this family. As such, our results are important for future studies aimed at unraveling complex specificity networks of peptide recognition domains in higher eukaryotes, including mammals.","doi":"10.1371/journal.pone.0129229","authors":"Verschueren E, Spiess M, Gkourtsa A, Avula T, Landgraf C, Mancilla VT, Huber A, Volkmer R, Winsor B, Serrano L, Hochstenbach F, Distel B","authors_abbrev":"Verschueren E et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-06-13","publication_year":"2015","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2015-06-14 00:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9013334","title":"The novel human protein serine/threonine phosphatase 6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, which are involved in cell cycle regulation.","citation":"J Cell Sci 1996 Dec;109 ( Pt 12):2865-74","abstract":"We identified a novel human protein serine/threonine phosphatase cDNA, designated protein phosphatase 6 (PP6) by using a homology-based polymerase chain reaction. The predicted amino acid sequence indicates a 35 kDa protein showing high homology to other protein phosphatases including human PP2A (57%), human PP4 (59%), rat PPV (98%), Drosophila PPV (74%), Schizosaccharomyces pombe ppe1 (68%) and Saccharomyces cerevisiae Sit4p (61%). In human cells, three forms of PP6 mRNA were found with highest levels of expression in testis, heart and skeletal muscle. The PP6 protein was detected in lysates of human heart muscle and in bull testis. Complementation studies using a temperature sensitive mutant strain of S. cerevisiae SIT4, which is required for the G1 to S transition of the cell cycle, showed that PP6 can rescue the mutant growth arrest. In addition, a loss of function mutant of S. pombe ppe1, described as a gene interacting with the pim1/spi1 mitotic checkpoint and involved in cell shape control, can be complemented by expression of human PP6. These data indicate that human PP6 is a functional homologue of budding yeast Sit4p and fission yeast ppe1, implying a function of PP6 in cell cycle regulation.","authors":"Bastians H, Ponstingl H","authors_abbrev":"Bastians H et al.","pubmed_publication_date":"Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_session_key":"c00835f95dba0345","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 16:14:27","canto_session_submitted_date":"2012-03-03 16:14:11","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1739.12"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:32682352","title":"Chemical genetic analysis of FTY720- and Ca 2+  -sensitive mutants reveals a functional connection between FTY720 and membrane trafficking.","citation":"Genes Cells 2020 Sep;25(9):637-645","abstract":"FTY720, a sphingosine-1-phosphate (S1P) analog, is used as an immune modulator to treat multiple sclerosis. Accumulating evidence has suggested the mode of action of FTY720 independent of an S1P modulator. In fission yeast, FTY720 induces an increase in intracellular Ca 2+  and ROS levels. We have previously identified 49 genes of which deletion causes FTY720 sensitivity. Here, we characterized the FTY720-sensitive mutants in terms of their relevance to the Ca 2+  homeostasis and identified the 16 FTY720- and Ca 2+  -sensitive mutants (fcs mutants). Most of the FTY720-sensitive mutants showed elevated Ca 2+  levels and exhibited Ca 2+  dysregulation by FTY720 treatment. One of the functional categories among the genes whose deletion renders cells susceptible to FTY720 and Ca 2+  include the Golgi/endosomal membrane trafficking. Notably, FTY720, but not phosphorylated FTY720 incapable of inducing Ca 2+  increase, inhibited the secretion of acid phosphatase in the wild-type cells. Importantly, secretory defects of the Golgi/endosomal trafficking mutants, Vps45, or Ryh1 deletion, were further exacerbated by FTY720. Our fcs mutant screen also identified the adenylyl cyclase-associated protein Cap1 and a Rictor homolog Ste20, whose deletion markedly exacerbated FTY720-sensitive secretory impairment. Collectively, our data may suggest a synergistic impact of FTY720 combined with secretion perturbation on proliferation and Ca 2+  homeostasis.","doi":"10.1111/gtc.12800","authors":"Hagihara K, Kanda Y, Ishida K, Satoh R, Takasaki T, Maeda T, Sugiura R","authors_abbrev":"Hagihara K et al.","pubmed_publication_date":"Sep 2020","pubmed_entrez_date":"2020-07-19","publication_year":"2020","canto_session_key":"4327c7364c8c71f0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-07-20 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24081582","title":"Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate.","citation":"Nucleic Acids Res 2014 Jan;42(1):509-25","abstract":"Transfer RNA (tRNA) methylation is necessary for the proper biological function of tRNA. The N(1) methylation of guanine at Position 9 (m(1)G9) of tRNA, which is widely identified in eukaryotes and archaea, was found to be catalyzed by the Trm10 family of methyltransferases (MTases). Here, we report the first crystal structures of the tRNA MTase spTrm10 from Schizosaccharomyces pombe in the presence and absence of its methyl donor product S-adenosyl-homocysteine (SAH) and its ortholog scTrm10 from Saccharomyces cerevisiae in complex with SAH. Our crystal structures indicated that the MTase domain (the catalytic domain) of the Trm10 family displays a typical SpoU-TrmD (SPOUT) fold. Furthermore, small angle X-ray scattering analysis reveals that Trm10 behaves as a monomer in solution, whereas other members of the SPOUT superfamily all function as homodimers. We also performed tRNA MTase assays and isothermal titration calorimetry experiments to investigate the catalytic mechanism of Trm10 in vitro. In combination with mutational analysis and electrophoretic mobility shift assays, our results provide insights into the substrate tRNA recognition mechanism of Trm10 family MTases.","doi":"10.1093/nar/gkt869","authors":"Shao Z, Yan W, Peng J, Zuo X, Zou Y, Li F, Gong D, Ma R, Wu J, Shi Y, Zhang Z, Teng M, Li X, Gong Q","authors_abbrev":"Shao Z et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2013-10-02","publication_year":"2014","canto_session_key":"ce811a54fcf0c195","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-20 02:21:44","canto_approved_date":"2022-01-19 13:02:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-09 15:06:14","canto_added_date":"2013-10-07 09:38:24","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPATRNAGLY.02","SPBTRNAGLY.03","SPCTRNAGLY.10","SPCTRNAGLY.11","SPAC6B12.09","SPBTRNAGLY.08","SPATRNAGLY.01","SPBTRNAGLY.06","SPBTRNAGLY.07"],"gene_count":9,"ltp_gene_count":1,"approved_date":"2015-10-20","pdb_entries":[{"pdb_id":"4jwg","gene_chains":[{"gene_uniquename":"SPAC6B12.09","chain":"A","position":"74-281"}],"title":"Crystal structure of spTrm10(74)","entry_authors":"Yan W,Shao Z","entry_authors_abbrev":"Yan W et al.","reference_uniquename":"PMID:24081582","experimental_method":"X-ray","resolution":"2.5"},{"pdb_id":"4jwf","gene_chains":[{"gene_uniquename":"SPAC6B12.09","chain":"A/B","position":"74-281"}],"title":"Crystal structure of spTrm10(74)-SAH complex","entry_authors":"Yan W,Shao Z","entry_authors_abbrev":"Yan W et al.","reference_uniquename":"PMID:24081582","experimental_method":"X-ray","resolution":"2.4"},{"pdb_id":"4jwh","gene_chains":[{"gene_uniquename":"SPAC6B12.09","chain":"A/B","position":"1-304"}],"title":"Crystal structure of spTrm10(Full length)-SAH complex","entry_authors":"Yan W,Shao Z","entry_authors_abbrev":"Yan W et al.","reference_uniquename":"PMID:24081582","experimental_method":"X-ray","resolution":"2.04"}]},{"uniquename":"PMID:8805536","title":"Crystal structure of the yeast cell-cycle control protein, p13suc1, in a strand-exchanged dimer.","citation":"Structure 1996 Mar 15;4(3):299-309","abstract":"p13(suc1) from fission yeast is a member of the CDC28 kinase specific (CKS) class of cell-cycle control proteins, that includes CKS1 from budding yeast and the human homologues CksHs1 and CksHs2. p13(suc1) participates in the regulation of p34(cdc2), a cyclin-dependent kinase controlling the G1-S and the G2-M transitions of the cell cycle. The CKS proteins are believed to exert their regulatory activity by binding to the kinase, in which case their function may be governed by their conformation or oligomerization state. Previously determined X-ray structures of p13(suc1), CksHs1 and CksHs2 show that these proteins share a common fold but adopt different oligomeric states. Monomeric forms of p13(suc1) and CksHs1 have been solved. In addition, CksHs2 and p13(suc1) have been observed by X-ray crystallography in assemblies of strand-exchanged dimers. Analysis of various assemblies of the CKS proteins, as found in different crystal forms, should help to clarify their role in cell-cycle control.\nWe report the X-ray crystal structure of p13(suc1) to 1.95 A resolution in space group C2221. It is present in the crystals as a strand-exchanged dimer. The overall monomeric fold is preserved in each lobe of the dimer but a single beta-strand (Ile94-Asp102) is exchanged between the central beta-sheets of each molecule.\nStrand exchange, which has been observed for p13(suc1) in two different space groups, and for CksHs2, is now confirmed to be an intrinsic feature of the CKS family. A switch between levels of assembly may serve to coordinate the function of the CKS proteins in cell-cycle control.","authors":"Khazanovich N, Bateman K, Chernaia M, Michalak M, James M","authors_abbrev":"Khazanovich N et al.","pubmed_publication_date":"15 Mar 1996","pubmed_entrez_date":"1996-03-15","publication_year":"1996","canto_session_key":"11a4a259d1263f36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-02-28 14:39:50","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-01 15:55:55","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1734.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-01","pdb_entries":[{"pdb_id":"1puc","gene_chains":[{"gene_uniquename":"SPBC1734.14c","chain":"A","position":"2-106"}],"title":"P13SUC1 IN A STRAND-EXCHANGED DIMER","entry_authors":"Khazanovich N,Bateman KS,Chernaia M,Michalak M,James MNG","entry_authors_abbrev":"Khazanovich N et al.","reference_uniquename":"PMID:8805536","experimental_method":"X-ray","resolution":"1.95"}]},{"uniquename":"PMID:25580011","title":"Imp2, the PSTPIP homolog in fission yeast, affects sensitivity to the immunosuppressant FK506 and membrane trafficking in fission yeast.","citation":"Biochem Biophys Res Commun 2015 Feb 13;457(3):273-9","abstract":"Cytokinesis is a highly ordered process that divides one cell into two cells, which is functionally linked to the dynamic remodeling of the plasma membrane coordinately with various events such as membrane trafficking. Calcineurin is a highly conserved serine/threonine protein phosphatase, which regulates multiple biological functions, such as membrane trafficking and cytokinesis. Here, we isolated imp2-c3, a mutant allele of the imp2(+) gene, encoding a homolog of the mouse PSTPIP1 (proline-serine-threonine phosphatase interacting protein 1), using a genetic screen for mutations that are synthetically lethal with calcineurin deletion in fission yeast. The imp2-c3 mutants showed a defect in cytokinesis with multi-septated phenotypes, which was further enhanced upon treatment with the calcineurin inhibitor FK506. Notably, electron micrographs revealed that the imp2-c3 mutant cells accumulated aberrant multi-lamella Golgi structures and putative post-Golgi secretory vesicles, and exhibited fragmented vacuoles in addition to thickened septa. Consistently, imp2-c3 mutants showed a reduced secretion of acid phosphatase and defects in vacuole fusion. The imp2-c3 mutant cells exhibited a weakened cell wall, similar to the membrane trafficking mutants identified in the same genetic screen such as ypt3-i5. These findings implicate the PSTPIP1 homolog Imp2 in Golgi/vacuole function, thereby affecting various cellular processes, including cytokinesis and cell integrity.","doi":"10.1016/j.bbrc.2014.12.100","authors":"Kita A, Higa M, Doi A, Satoh R, Sugiura R","authors_abbrev":"Kita A et al.","pubmed_publication_date":"13 Feb 2015","pubmed_entrez_date":"2015-01-13","publication_year":"2015","canto_session_key":"47322fee98b70ba6","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-01-14 01:15:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11C11.02","SPBP4H10.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:28342076","title":"Schizosaccharomyces pombe rsv1 Transcription Factor and its Putative Homologues Preserved their Functional Homology and are Evolutionarily Conserved.","citation":"Curr Microbiol 2017 Jun;74(6):710-717","abstract":"Environmental glucose is an important regulator of biological processes, as it can launch different cell processes depending on its concentration. Thus, low glucose concentration can induce entry into quiescence, which ensures long-term viability for the cells or in other cases mycelial growth in the dimorphic species, which, in turn, provides the cells with fresh nutrients. Several genes, such as the genes of cAMP cascade, are involved in glucose sensing and response. Since this signal transduction pathway seemed to be an evolutionarily conserved process, we assumed that its genes were also conserved and preserved their functional homology. To obtain evidence, Schizosaccharomyces pombe rsv1 and its orthologous genes were investigated using in silico and experimental approaches. Our results supported that the Rsv1 zinc-finger transcription factors of Schizosaccharomyces japonicus and Schizosaccharomyces octosporus and the Candida albicans cas5p were really functional homologues of the S. pombe Rsv1. Namely, the homologous proteins were able to restore mutant phenotype of the S. pombe rsv1-deleted cells. Bioinformatic anaysis revealed that the most conserved parts of the proteins always contained the C2H2 domains and the complementation abilities of the counterpart genes were not uniform regarding the investigated features, which can be in connection with the conserved regions outside C2H2.","doi":"10.1007/s00284-017-1227-9","authors":"Pataki E, Sipiczki M, Miklos I","authors_abbrev":"Pataki E et al.","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2017-03-26","publication_year":"2017","canto_session_key":"a5c3d1e83c25ea24","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ida Miklos","canto_approved_date":"2017-04-19 07:18:59","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-04-05 10:38:45","canto_added_date":"2017-03-29 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ida Miklos","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-04-05"},{"uniquename":"PMID:25972440","title":"Global regulation of heterochromatin spreading by Leo1.","citation":"Open Biol 2015 May;5(5)","abstract":"Heterochromatin plays important roles in eukaryotic genome regulation. However, the repressive nature of heterochromatin combined with its propensity to self-propagate necessitates robust mechanisms to contain heterochromatin within defined boundaries and thus prevent silencing of expressed genes. Here we show that loss of the PAF complex (PAFc) component Leo1 compromises chromatin boundaries, resulting in invasion of heterochromatin into flanking euchromatin domains. Similar effects are seen upon deletion of other PAFc components, but not other factors with related functions in transcription-associated chromatin modification, indicating a specific role for PAFc in heterochromatin regulation. Loss of Leo1 results in reduced levels of H4K16 acetylation at boundary regions, while tethering of the H4K16 acetyltransferase Mst1 to boundary chromatin suppresses heterochromatin spreading in leo1Δ cells, suggesting that Leo1 antagonises heterochromatin spreading by promoting H4K16 acetylation. Our findings reveal a previously undescribed role for PAFc in regulating global heterochromatin distribution.","doi":"10.1098/rsob.150045","authors":"Verrier L, Taglini F, Barrales RR, Webb S, Urano T, Braun S, Bayne EH","authors_abbrev":"Verrier L et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-05-15","publication_year":"2015","canto_session_key":"341a050d011a7bfa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elizabeth Bayne","canto_first_approved_date":"2016-07-20 08:51:02","canto_approved_date":"2023-03-13 22:35:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-14 13:52:21","canto_added_date":"2015-05-16 00:19:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Elizabeth Bayne","community_curator":true,"annotation_count":27,"orcid":"0000-0001-8775-999X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.08","SPBC30D10.10c","SPAPYUG7.04c","SPCC970.07c","SPAC631.02","SPAPB1E7.02c","SPAC27D7.14c","SPBC428.08c","SPAC18G6.02c","SPBC17G9.02c","SPBC13E7.08c","SPAC1006.03c","SPAC664.03","SPAC17H9.10c","SPAC3H1.12c","SPBC16E9.12c","SPAC637.12c","SPBC83.03c","SPBC4B4.07c","SPCC613.12c","SPAC664.01c","SPBC651.09c","SPCC622.16c"],"gene_count":23,"ltp_gene_count":21,"approved_date":"2016-07-20"},{"uniquename":"PMID:28087675","title":"DNA repair and mutations during quiescence in yeast.","citation":"FEMS Yeast Res 2017 Jan 01;17(1)","abstract":"Life is maintained through alternating phases of cell division and quiescence. The causes and consequences of spontaneous mutations have been extensively explored in proliferating cells, and the major sources include errors of DNA replication and DNA repair. The foremost consequences are genetic variations within a cell population that can lead to heritable diseases and drive evolution. While most of our knowledge on DNA damage response and repair has been gained through cells actively dividing, it remains essential to also understand how DNA damage is metabolized in cells which are not dividing. In this review, we summarize the current knowledge concerning the type of lesions that arise in non-dividing budding and fission yeast cells, as well as the pathways used to repair them. We discuss the contribution of these models to our current understanding of age-related pathologies.","doi":"10.1093/femsyr/fox002","authors":"Gangloff S, Arcangioli B","authors_abbrev":"Gangloff S et al.","pubmed_publication_date":"01 Jan 2017","pubmed_entrez_date":"2017-01-15","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-01-16 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24391665","title":"The cellular roles of Ccr4-NOT in model and pathogenic fungi-implications for fungal virulence.","citation":"Front Genet 2013;4:302","abstract":"The fungal Ccr4-NOT complex has been implicated in orchestrating gene expression networks that impact on pathways key for virulence in pathogenic species. The activity of Ccr4-NOT regulates cell wall integrity, antifungal drug susceptibility, adaptation to host temperature, and the developmental switches that enable the formation of pathogenic structures, such as filamentous hyphae. Moreover, Ccr4-NOT impacts on DNA repair pathways and genome stability, opening the possibility that this gene regulator could control adaptive responses in pathogens that are driven by chromosomal alterations. Here we provide a synthesis of the cellular roles of the fungal Ccr4-NOT, focusing on pathways important for virulence toward animals. Our review is based on studies in models yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, and two species that cause serious human infections, Candida albicans and Cryptococcus neoformans. We hypothesize that the activity of Ccr4-NOT could be targeted for future antifungal drug discovery, a proposition supported by the fact that inactivation of the genes encoding subunits of Ccr4-NOT in C. albicans and C. neoformans reduces virulence in the mouse infection model. We performed bioinformatics analysis to identify similarities and differences between Ccr4-NOT subunits in fungi and animals, and discuss this knowledge in the context of future antifungal strategies.","doi":"10.3389/fgene.2013.00302","authors":"Panepinto JC, Heinz E, Traven A","authors_abbrev":"Panepinto JC et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2014-01-07","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10523506","title":"The fission yeast origin recognition complex is constitutively associated with chromatin and is differentially modified through the cell cycle.","citation":"J Cell Sci 1999 Nov;112 ( Pt 21):3703-12","abstract":"The origin recognition complex (ORC) binds to the well defined origins of DNA replication in budding yeast. Homologous proteins in other eukaryotes have been identified but are less well characterised. We report here the characterisation of a fission yeast ORC complex (SpORC). Database searches identified a fission yeast Orc5 homologue. SpOrc5 is essential for cell viability and its deletion phenotype is identical to that of two previously identified ORC subunit homologues, SpOrc1 (Orp1/Cdc30) and SpOrc2 (Orp2). Co-immunoprecipitation experiments demonstrate that SpOrc1 forms a complex with SpOrc2 and SpOrc5 and gel filtration chromatography shows that SpOrc1 and SpOrc5 fractionate as high molecular mass complexes. SpORC subunits localise to the nucleus in a punctate distribution which persists throughout interphase and mitosis. We developed a chromatin isolation protocol and show that SpOrc1, 2 and 5 are associated with chromatin at all phases of the cell cycle. While the levels, nuclear localisation and chromatin association of SpORC remain constant through the cell cycle, one of its subunits, SpOrc2, is differentially modified. We show that SpOrc2 is a phosphoprotein which is hypermodified in mitosis and is rapidly converted to a faster migrating isoform as cells proceed into G(1) in preparation for S-phase.","authors":"Lygerou Z, Nurse P","authors_abbrev":"Lygerou Z et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-10-19","publication_year":"1999","canto_session_key":"f203140be1f71f81","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 16:28:05","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-19 14:56:04","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC685.09","SPBC29A10.15","SPBC646.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-09-19"},{"uniquename":"PMID:16141205","title":"The glycolytic metabolite methylglyoxal activates Pap1 and Sty1 stress responses in Schizosaccharomyces pombe.","citation":"J Biol Chem 2005 Nov 04;280(44):36708-13","abstract":"Methylglyoxal, a toxic metabolite synthesized in vivo during glycolysis, inhibits cell growth. One of the mechanisms protecting eukaryotic cells against its toxicity is the glyoxalase system, composed of glyoxalase I and II (glo1 and glo2), which converts methylglyoxal into d-lactic acid in the presence of glutathione. Here we have shown that the two principal oxidative stress response pathways of Schizosaccharomyces pombe, Sty1 and Pap1, are involved in the response to methylglyoxal toxicity. The mitogen-activated protein kinase Sty1 is phosphorylated and accumulates in the nucleus following methylglyoxal treatment. Moreover, glo2 expression is induced by methylglyoxal and environmental stresses in a Sty1-dependent manner. The transcription factor Pap1 also accumulates in the nucleus, activating the expression of its target genes following methylglyoxal treatment. Our studies showed that the C-terminal cysteine-rich domain of Pap1 is sufficient for methylglyoxal sensing. Furthermore, the redox status of Pap1 is not changed by methylglyoxal. We propose that methylglyoxal treatment triggers Pap1 and Sty1 nuclear accumulation, and we describe the molecular basis of such activation mechanisms. In addition, we discuss the potential physiological significance of these responses to a natural toxic metabolite.","authors":"Zuin A, Vivancos AP, Sansó M, Takatsume Y, Ayté J, Inoue Y, Hidalgo E","authors_abbrev":"Zuin A et al.","pubmed_publication_date":"04 Nov 2005","pubmed_entrez_date":"2005-09-06","publication_year":"2005","canto_session_key":"36867162cb7ee60c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-30 15:32:20","canto_approved_date":"2022-11-07 11:00:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-30 15:32:11","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC824.07","SPBC12C2.12c","SPAC21E11.03c","SPBC3F6.03","SPBC29B5.01","SPAC24B11.06c","SPAC1783.07c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2015-01-30"},{"uniquename":"PMID:16101908","title":"Microtubules guide root hair tip growth.","citation":"New Phytol 2005 Sep;167(3):711-9","abstract":"The ability to establish cell polarity is crucial to form and function of an individual cell. Polarity underlies critical processes during cell development, such as cell growth, cell division, cell differentiation and cell signalling. Interphase cytoplasmic microtubules in tip-growing fission yeast cells have been shown to play a particularly important role in regulating cell polarity. By placing proteins that serve as spatial cues in the cell cortex of the expanding tip, microtubules determine the site where exocytosis, and therefore growth, takes place. Transport and the targeting of exocytotic vesicles to the very tip depend on the actin cytoskeleton. Recently, endoplasmic microtubules have been identified in tip-growing root hairs, which are an experimental system for plant cell growth. Here, we review the data that demonstrate involvement of microtubules in hair elongation and polarity of the model plants Medicago truncatula and Arabidopsis thaliana. Differences and similarities between the microtubule organization and function in these two species are discussed and we compare the observations in root hairs with the microtubule-based polarity mechanism in fission yeast.","authors":"Sieberer BJ, Ketelaar T, Esseling JJ, Emons AM","authors_abbrev":"Sieberer BJ et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-08-17","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15932060","title":"The telomere-binding protein Taz1p as a target for modification by a SUMO-1 homologue in fission yeast.","citation":"Biochem Genet 2005 Apr;43(3-4):103-17","abstract":"In fission yeast (Schizosaccharomyces pombe) the homologue of the mammalian SUMO-1 ubiquitin-like modifier is encoded by the pmt3 gene. A two-hybrid screen using the telomere-binding protein Taz1p as bait identified Pmt3p as an interacting factor. In vitro experiments using purified components of the fission yeast Pmt3p modification system demonstrated that Taz1p could be modified directly by Pmt3p. The amino acid sequence of Taz1p contains a close match to the consensus modification site for SUMO-1, and a PEST sequence similar to those found in established SUMO-1 targets. Although previous experiments have identified an increase in telomere length as one consequence of the pmt3--genotype, we could not detect Pmt3p modification of Taz1p in protein extracts made from exponentially growing haploid cells or any effect of Pmt3p on the localization of GFP-Taz1p at discrete foci in the haploid cell nucleus.","authors":"Spink K, Ho JC, Tanaka K, Watts FZ, Chambers A","authors_abbrev":"Spink K et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-06-04","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC16A10.07c","SPBC365.06"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:33462960","title":"Analyzing biological models and data sets using Jupyter notebooks as an alternate to laboratory-based exercises during COVID-19.","citation":"Biochem Mol Biol Educ 2020 Sep;48(5):532-534","abstract":"Jupyter notebooks are widely used for data analysis across a large number of scientific disciplines. As a result of the COVID-19 pandemic, I developed a series of computational exercises using the Jupyter notebook to replace the laboratory exercises usually undertaken in my course. My students had no prior coding knowledge and therefore these exercises were structured in a \"cookbook\" format using the susceptible-infected-resistant model for disease, data from the Lenski long-term evolutionary experiment, and a fission yeast transcriptomic data set. Despite limited internet connectivity and on-line instruction, my students completed these computational exercises and then tested their own hypotheses. Because Jupyter notebooks can be annotated with text and images, student notebooks were submitted for assessment in the form of a structured scientific report. An advantage of this approach was that all the computational analyses presented in these reports could be easily replicated. The notebook and complete instructions used in my course are provided for others who want to adopt this approach.","doi":"10.1002/bmb.21443","authors":"Pillay CS","authors_abbrev":"Pillay CS","pubmed_publication_date":"Sep 2020","pubmed_entrez_date":"2021-01-19","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-01-21 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10222126","title":"Subunits and substrates of the anaphase-promoting complex.","citation":"Exp Cell Res 1999 May 01;248(2):339-49","abstract":"The initiation of anaphase and exit from mitosis depend on a ubiquitination complex called the anaphase-promoting complex (APC) or cyclosome. The APC is composed of more than 10 constitutive subunits and associates with additional regulatory factors in mitosis and during the G1 phase of the cell cycle. At the metaphase-anaphase transition the APC ubiquitinates proteins such as Pds1 in budding yeast and Cut2 in fission yeast whose subsequent degradation by the 26S proteasome is essential for the initiation of sister chromatid separation. Later in anaphase and telophase the APC promotes the inactivation of the mitotic cyclin-dependent protein kinase 1 by ubiquitinating its activating subunit cyclin B. The APC also mediates the ubiquitin-dependent proteolysis of several other mitotic regulators, including other protein kinases, APC activators, spindle-associated proteins, and inhibitors of DNA replication.","authors":"Peters JM","authors_abbrev":"Peters JM","pubmed_publication_date":"01 May 1999","pubmed_entrez_date":"1999-05-01","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11389847","title":"Transcriptional termination factors for RNA polymerase II in yeast.","citation":"Mol Cell 2001 May;7(5):1003-11","abstract":"The molecular connections between mRNA 3' end processing and transcriptional termination have been investigated in S. pombe using a genetic screen. By this approach, we have identified a RNAP II termination domain in the well-defined cleavage polyadenylation factor called CstF-64 in metazoans and Rna15p in S. cerevisiae. Furthermore, this C-terminal domain interacts with Res2, previously identified as a component of the G1/S transition-specific transcription factor MBF. Deletion of res2 in both fission and budding yeast results in a defect in 3' end formation. This raises the possibility that RNAP II transcriptional termination may in some situations be integrated with cell cycle events.","authors":"Aranda A, Proudfoot N","authors_abbrev":"Aranda A et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-06-08","publication_year":"2001","canto_session_key":"3309874a19179607","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-20 15:27:53","canto_approved_date":"2024-08-20 15:27:53","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-20 15:27:47","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":6,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.09c","SPBC3B9.11c","SPBC725.16","SPBC336.12c","SPBC2F12.11c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2024-08-20"},{"uniquename":"PMID:16824200","title":"Schizosaccharomyces pombe homolog of Survivin, Bir1p, exhibits a novel dynamic behavior at the spindle mid-zone.","citation":"Genes Cells 2006 Jul;11(7):815-27","abstract":"Members of the BIR-domain containing Survivin family of proteins have been identified in a variety of eukaryotes and are known to play important roles in the regulation of mitosis. The Schizosaccharomyces pombe homolog of Survivin, Bir1p, is essential for chromosome condensation and spindle elongation and integrity. Bir1p, a nuclear protein, resides at the kinetochores in metaphase and anaphase A and spreads to the spindle mid-zone in anaphase B. Here we show that this relocation requires Cdk (Cyclin dependent kinase) inactivation and intact microtubules. With the aid of a kinesin mutant, klp5Delta, we also show that completion of anaphase A is vital for effecting Bir1p re-location to the spindle mid-zone. Although minimal exchange of Bir1p sub-units occurs between the spindle and the nucleoplasm, the protein redistributes laterally within the mid-zone region. Bir1p dynamics therefore significantly differs from that of tubulin on an anaphase B spindle, which is loaded at the plus ends of growing microtubules and shows no lateral redistribution within the spindle. Thus, Bir1p, and possibly its associated proteins, might organize a dynamic mid-zone region that helps spindle elongation and maintenance.","authors":"Rajagopalan S, Mishra M, Balasubramanian MK","authors_abbrev":"Rajagopalan S et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-07-11","publication_year":"2006","canto_session_key":"973dc493726740c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-28 05:13:41","canto_approved_date":"2025-09-04 10:25:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-13 17:06:34","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPBC582.03","SPBC26H8.07c","SPCC962.02c","SPBC1685.15c","SPBC2F12.13"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-04-28"},{"uniquename":"PMID:29016658","title":"Probing the interaction between NatA and the ribosome for co-translational protein acetylation.","citation":"PLoS One 2017;12(10):e0186278","abstract":"N-terminal acetylation is among the most abundant protein modifications in eukaryotic cells. Over the last decade, significant progress has been made in elucidating the function of N-terminal acetylation for a number of diverse systems, involved in a wide variety of biological processes. The enzymes responsible for the modification are the N-terminal acetyltransferases (NATs). The NATs are a highly conserved group of enzymes in eukaryotes, which are responsible for acetylating over 80% of the soluble proteome in human cells. Importantly, many of these NATs act co-translationally; they interact with the ribosome near the exit tunnel and acetylate the nascent protein chain as it is being translated. While the structures of many of the NATs have been determined, the molecular basis for the interaction with ribosome is not known. Here, using purified ribosomes and NatA, a very well-studied NAT, we show that NatA forms a stable complex with the ribosome in the absence of other stabilizing factors and through two conserved regions; primarily through an N-terminal domain and an internal basic helix. These regions may orient the active site of the NatA to face the peptide emerging from the exit tunnel. This work provides a framework for understanding how NatA and potentially other NATs interact with the ribosome for co-translational protein acetylation and sets the foundation for future studies to decouple N-terminal acetyltransferase activity from ribosome association.","doi":"10.1371/journal.pone.0186278","authors":"Magin RS, Deng S, Zhang H, Cooperman B, Marmorstein R","authors_abbrev":"Magin RS et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-10-11","publication_year":"2017","canto_session_key":"1b2a13292870d3d4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-10-21 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7744953","title":"The product of the spindle formation gene sad1+ associates with the fission yeast spindle pole body and is essential for viability.","citation":"J Cell Biol 1995 May;129(4):1033-47","abstract":"Spindle formation in fission yeast occurs by the interdigitation of two microtubule arrays extending from duplicated spindle pole bodies which span the nuclear membrane. By screening a bank of temperature-sensitive mutants by anti-tubulin immunofluorescence microscopy, we previously identified the sad1.1 mutation (Hagan, I., and M. Yanagida. 1990. Nature (Lond.). 347:563-566). Here we describe the isolation and characterization of the sad1+ gene. We show that the sad1.1 mutation affected both spindle formation and function. The sad1+ gene is a novel essential gene that encodes a protein with a predicted molecular mass of 58 kD. Deletion of the gene was lethal resulting in identical phenotypes to the sad1.1 mutation. Sequence analysis predicted a potential membrane-spanning domain and an acidic amino terminus. Sad1 protein migrated as two bands of 82 and 84 kD on SDS-PAGE, considerably slower than its predicted mobility, and was exclusively associated with the spindle pole body (SPB) throughout the mitotic and meiotic cycles. Microtubule integrity was not required for Sad1 association with the SPB. Upon the differentiation of the SPB in metaphase of meiosis II, Sad1-staining patterns similarly changed from a dot to a crescent supporting an integral role in SPB function. Moderate overexpression of Sad1 led to association with the nuclear periphery. As Sad1 was not detected in the cytoplasmic microtubule-organizing centers activated at the end of anaphase or kinetochores, we suggest that Sad1 is not a general component of microtubule-interacting structures per se, but is an essential mitotic component that associates with the SPB but is not required for microtubule nucleation. Sad1 may play a role in SPB structure, such as maintaining a functional interface with the nuclear membrane or in providing an anchor for the attachment of microtubule motor proteins.","authors":"Hagan I, Yanagida M","authors_abbrev":"Hagan I et al.","pubmed_publication_date":"May 1995","pubmed_entrez_date":"1995-05-01","publication_year":"1995","canto_session_key":"b0c3bd95702f2fcc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-28 15:31:39","canto_approved_date":"2024-03-29 09:23:44","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-08-28 15:31:33","canto_added_date":"2012-02-24 05:54:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-28"},{"uniquename":"PMID:12724408","title":"Two ubiquitin-conjugating enzymes, UbcP1/Ubc4 and UbcP4/Ubc11, have distinct functions for ubiquitination of mitotic cyclin.","citation":"Mol Cell Biol 2003 May;23(10):3497-505","abstract":"Cell cycle events are regulated by sequential activation and inactivation of Cdk kinases. Mitotic exit is accomplished by the inactivation of mitotic Cdk kinase, which is mainly achieved by degradation of cyclins. The ubiquitin-proteasome system is involved in this process, requiring APC/C (anaphase-promoting complex/cyclosome) as a ubiquitin ligase. In Xenopus and clam oocytes, the ubiquitin-conjugating enzymes that function with APC/C have been identified as two proteins, UBC4 and UBCx/E2-C. Previously we reported that the fission yeast ubiquitin-conjugating enzyme UbcP4/Ubc11, a homologue of UBCx/E2-C, is required for mitotic transition. Here we show that the other fission yeast ubiquitin-conjugating enzyme, UbcP1/Ubc4, which is homologous to UBC4, is also required for mitotic transition in the same manner as UbcP4/Ubc11. Both ubiquitin-conjugating enzymes are essential for cell division and directly required for the degradation of mitotic cyclin Cdc13. They function nonredundantly in the ubiquitination of CDC13 because a defect in ubcP1/ubc4+ cannot be suppressed by high expression of UbcP4/Ubc11 and a defect in ubcP4/ubc11+ cannot be suppressed by high expression of UbcP1/Ubc4. In vivo analysis of the ubiquitinated state of Cdc13 shows that the ubiquitin chains on Cdc13 were short in ubcP1/ubc4 mutant cells while ubiquitinated Cdc13 was totally reduced in ubcP4/ubc11 mutant cells. Taken together, these results indicate that the two ubiquitin-conjugating enzymes play distinct and essential roles in the degradation of mitotic cyclin Cdc13, with the UbcP4/Ubc11-pathway initiating ubiquitination of Cdc13 and the UbcP1/Ubc4-pathway elongating the short ubiquitin chains on Cdc13.","authors":"Seino H, Kishi T, Nishitani H, Yamao F","authors_abbrev":"Seino H et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-05-02","publication_year":"2003","canto_session_key":"a48edd53bda96efe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-05-31 19:37:24","canto_approved_date":"2024-03-01 16:42:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-01 12:26:26","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.15c","SPCC1259.15c","SPBC582.03","SPBC119.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-05-31"},{"uniquename":"PMID:29043956","title":"The amino-terminal domain of ELL transcription elongation factor is essential for ELL function in Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 2017 Nov;163(11):1641-1653","abstract":"Transcriptional elongation is a critical step for regulating expression of protein-coding genes. Multiple transcription elongation factors have been identified in vitro, but the physiological roles of many of them are still not clearly understood. The ELL (Eleven nineteen Lysine rich Leukemia) family of transcription elongation factors are conserved from fission yeast to humans. Schizosaccharomyces pombe contains a single ELL homolog (SpELL) that is not essential for its survival. Therefore to gain insights into the in vivo cellular functions of SpELL, we identified phenotypes associated with deletion of ell1 in S. pombe. Our results demonstrate that SpELL is required for normal growth of S. pombe cells. Furthermore, cells lacking ell1 +  exhibit a decrease in survival when exposed to DNA-damaging conditions, but their growth is not affected under environmental stress conditions. ELL orthologs in different organisms contain three conserved domains, an amino-terminal domain, a middle domain and a carboxyl-terminal domain. We also carried out an in vivo functional mapping of these conserved domains within S. pombe ELL and uncovered a critical role for its amino-terminus in regulating all its cellular functions, including growth under different conditions, transcriptional elongation potential and interaction with S. pombe EAF. Taken together our results suggest that the domain organization of ELL proteins is conserved across species, but the in vivo functions as well as the relationship between the various domains and roles of ELL show species-specific differences.","doi":"10.1099/mic.0.000554","authors":"Sweta K, Dabas P, Jain K, Sharma N","authors_abbrev":"Sweta K et al.","pubmed_publication_date":"Nov 2017","pubmed_entrez_date":"2017-10-19","publication_year":"2017","canto_session_key":"eebda46280bfa20f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kumari Sweta","canto_first_approved_date":"2019-06-05 07:01:35","canto_approved_date":"2019-06-05 07:01:35","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-05-31 17:15:36","canto_added_date":"2017-10-20 00:15:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":50,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kumari Sweta","community_curator":true,"annotation_count":5,"orcid":"0000-0003-4118-3870","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.14c","SPCC1223.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-06-05"},{"uniquename":"PMID:32012158","title":"Meiotic gene silencing complex MTREC/NURS recruits the nuclear exosome to YTH-RNA-binding protein Mmi1.","citation":"PLoS Genet 2020 Feb;16(2):e1008598","abstract":"Accurate target recognition in transcript degradation is crucial for regulation of gene expression. In the fission yeast Schizosaccharomyces pombe, a number of meiotic transcripts are recognized by a YTH-family RNA-binding protein, Mmi1, and selectively degraded by the nuclear exosome during mitotic growth. Mmi1 forms nuclear foci in mitotically growing cells, and the nuclear exosome colocalizes to such foci. However, it remains elusive how Mmi1 and the nuclear exosome are connected. Here, we show that a complex called MTREC (Mtl1-Red1 core) or NURS (nuclear RNA silencing) that consists of a zinc-finger protein, Red1, and an RNA helicase, Mtl1, is required for the recruitment of the nuclear exosome to Mmi1 foci. Physical interaction between Mmi1 and the nuclear exosome depends on Red1. Furthermore, a chimeric protein involving Mmi1 and Rrp6, which is a nuclear-specific component of the exosome, suppresses the ectopic expression phenotype of meiotic transcripts in red1Δ cells and mtl1 mutant cells. These data indicate that the primary function of MTREC/NURS in meiotic transcript elimination is to link Mmi1 to the nuclear exosome physically.","doi":"10.1371/journal.pgen.1008598","authors":"Shichino Y, Otsubo Y, Yamamoto M, Yamashita A","authors_abbrev":"Shichino Y et al.","pubmed_publication_date":"Feb 2020","pubmed_entrez_date":"2020-02-04","publication_year":"2020","canto_session_key":"57d00be9a0ffdd97","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-03-26 14:47:47","canto_approved_date":"2024-04-04 09:49:50","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-03-09 10:51:42","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":38,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.13c","SPBC646.04","SPAC2F7.14c","SPBC29A10.02","SPAC1006.03c","SPBC29A10.14","SPAC7D4.14c","SPBC26H8.10","SPBC16E9.12c","SPBC32H8.11","SPAC1F3.01","SPNCRNA.1365","SPBC1685.08","SPCC736.12c","SPAC17H9.02"],"gene_count":15,"ltp_gene_count":6,"approved_date":"2020-03-26"},{"uniquename":"PMID:2474475","title":"cdc2 and the regulation of mitosis: six interacting mcs genes.","citation":"Genetics 1989 Aug;122(4):773-82","abstract":"A cdc2-3w weel-50 double mutant of fission yeast displays a temperature-sensitive lethal phenotype that is associated with gross abnormalities of chromosome segregation and has been termed mitotic catastrophe. In order to identify new genetic elements that might interact with the cdc2 protein kinase in the regulation of mitosis, we have isolated revertants of the lethal double mutant. The suppressor mutations define six mcs genes (mcs: mitotic catastrophe suppressor) that are not allelic to any of the following mitotic control genes: cdc2, wee 1, cdc13, cdc25, suc1 or nim1. Each mcs mutation is recessive with respect to wild-type in its ability to suppress mitotic catastrophe. None confer a lethal phenotype as a single mutant but few of the mutants are expected to be nulls. A diverse range of genetic interactions between the mcs mutants and other mitotic regulators were uncovered, including the following examples. First, mcs2 cdc2w or mcs6 cdc2w double mutants display a cell cycle defect dependent on the specific wee allele of cdc2. Second, both mcs1 cdc25-22 or mcs4 cdc25-22 double mutants are nonconditionally lethal, even at a temperature normally permissive for cdc25-22. Finally, the characteristic suppression of the cdc25 phenotype by a loss-of-function wee1 mutation is reversed in a mcs3 mutant background. The mcs genes define new mitotic elements that might be activators or substrates of the cdc2 protein kinase.","authors":"Molz L, Booher R, Young P, Beach D","authors_abbrev":"Molz L et al.","pubmed_publication_date":"Aug 1989","pubmed_entrez_date":"1989-08-01","publication_year":"1989","canto_session_key":"69acd91fe4ac8649","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-25 11:21:20","canto_approved_date":"2019-06-14 12:27:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-25 11:19:37","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC19F8.07","SPBC11B10.09","SPBP16F5.02","SPBC887.10","SPAC24H6.05","SPBC582.03","SPAC22F3.09c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-11-25"},{"uniquename":"PMID:15123683","title":"Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis.","citation":"J Biol Chem 2004 Jun 18;279(25):25943-6","abstract":"Human ferrochelatase, a mitochondrial membrane-associated protein, catalyzes the terminal step of heme biosynthesis by insertion of ferrous iron into protoporphyrin IX. The recently solved x-ray structure of human ferrochelatase identifies a potential binding site for an iron donor protein on the matrix side of the homodimer. Herein we demonstrate Hs holofrataxin to be a high affinity iron binding partner for Hs ferrochelatase that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis. A general regulatory mechanism for mitochondrial iron metabolism is described that defines frataxin involvement in both heme and iron-sulfur cluster biosyntheses. In essence, the distinct binding affinities of holofrataxin to the target proteins, ferrochelatase (heme synthesis) and ISU (iron-sulfur cluster synthesis), allows discrimination between the two major iron-dependent pathways and facilitates targeted heme biosynthesis following down-regulation of frataxin.","authors":"Yoon T, Cowan JA","authors_abbrev":"Yoon T et al.","pubmed_publication_date":"18 Jun 2004","pubmed_entrez_date":"2004-05-05","publication_year":"2004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25146394","title":"The meiosis-specific nuclear passenger protein is required for proper assembly of forespore membrane in fission yeast.","citation":"J Cell Sci 2014 Oct 15;127(Pt 20):4429-42","abstract":"Sporulation, gametogenesis in yeast, consists of meiotic nuclear division and spore morphogenesis. In the fission yeast Schizosaccharomyces pombe, the four haploid nuclei produced after meiosis II are encapsulated by the forespore membrane (FSM), which is newly synthesized from spindle pole bodies (SPBs) in the cytoplasm of the mother cell as spore precursors. Although the coordination between meiosis and FSM assembly is vital for proper sporulation, the underlying mechanism remains unclear. In the present study, we identified a new meiosis-specific protein Npg1, and found that it was involved in the efficient formation of spores and spore viability. The accumulation and organization of the FSM was compromised in npg1-null cells, leading to the error-prone envelopment of nuclei. Npg1 was first seen as internuclear dots and translocated to the SPBs before the FSM assembled. Genetic analysis revealed that Npg1 worked in conjunction with the FSM proteins Spo3 and Meu14. These results suggest a possible signaling link from the nucleus to the meiotic SPBs in order to associate the onset of FSM assembly with meiosis II, which ensures the successful partitioning of gametic nuclei.","doi":"10.1242/jcs.151738","authors":"Takaine M, Imada K, Numata O, Nakamura T, Nakano K","authors_abbrev":"Takaine M et al.","pubmed_publication_date":"15 Oct 2014","pubmed_entrez_date":"2014-08-23","publication_year":"2014","canto_session_key":"3c4b277977998eee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masak Takaine","canto_first_approved_date":"2015-04-29 13:21:09","canto_approved_date":"2023-05-03 15:29:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-03 02:31:47","canto_added_date":"2014-08-27 00:15:24","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Masak Takaine","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC607.10","SPBC17D1.07c","SPBC1347.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-04-29"},{"uniquename":"PMID:9161410","title":"A novel HSP70 gene of Schizosaccharomyces pombe that confers K-252a resistance.","citation":"Gene 1997 Apr 11;189(1):43-7","abstract":"A new gene encoding a heat shock protein 70 family protein of Schizosaccharomyces pombe (Sp), named sks2+, was cloned as a weak suppressor for the K-252a-sensitive mutation, ucm1. The nucleotide sequence of sks2+ revealed an open reading frame of a 613-amino-acid (aa) protein. The deduced aa sequence of sks2+ showed significant homology with Saccharomyces cerevisiae (Sc) Ssb1p and Ssb2p responsible for protein synthesis by non-organelle-localized ribosomes, as well as with other proteins of the HSP70 family. The cells lacking the functional sks2+ gene were viable and showed no increased sensitivity to K-252a but grew slowly with an elongated morphology. These results suggest that the sks2+ gene product plays a role in the cell cycle progression and is able to confer drug resistance in a multicopy state.","authors":"Usui T, Yoshida M, Kasahara K, Honda A, Beppu T, Horinouchi S","authors_abbrev":"Usui T et al.","pubmed_publication_date":"11 Apr 1997","pubmed_entrez_date":"1997-04-11","publication_year":"1997","canto_session_key":"f56e6d2643d711c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-02-17 08:36:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-16 10:18:50","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1709.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-16"},{"uniquename":"EMBL:AU009771","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41326690","title":"Heterochromatin epimutations impose mitochondrial dysfunction to confer antifungal resistance.","citation":"EMBO J 2025 Dec 01;","abstract":"Antifungal resistance in pathogenic fungi endanger global health and food supply. Wild-type fission yeast, Schizosaccharomyces pombe, can gain resistance to insults including caffeine and antifungal compounds through reversible epimutations. Resistant epimutants exhibit ectopic histone-H3K9 methylation-dependent heterochromatin islands, repressing underlying genes. Two genes whose heterochromatin island-induced repression causes resistance encode mitochondrial proteins: LYR-domain protein Cup1 and Cox1 translation regulator Ppr4. Genetic mutations, cup1-tt and ppr4Δ, that phenocopy epimutants, cause mitochondrial dysfunction, including respiratory deficiency, poor growth on non-glucose carbon sources, and elevated reactive oxygen species. Transcriptomic analyses indicate cup1-tt and ppr4Δ cells activate Pap1 transcription factor-dependent oxidative stress response and mitonuclear retrograde pathways. Pap1 nuclear localisation and recruitment to promoters of oxidoreductase and membrane transporter genes is increased, causing increased efflux activity. cup1 and ppr4 epimutants likewise show mitochondrial dysfunction phenotypes and increased efflux, explaining how heterochromatin-island epimutations cause drug resistance. Thus, wild-type cells harness epimutations that impose mitochondrial dysfunction to bypass external insults. As mitochondrial dysfunction is linked to antifungal resistance in several fungi, similar epimutations likely contribute to development of resistance in fungal pathogens.","doi":"10.1038/s44318-025-00649-0","authors":"Fellas A, Pidoux AL, Tong P, Hewes HH, Wallace EC, Allshire RC","authors_abbrev":"Fellas A et al.","pubmed_publication_date":"01 Dec 2025","pubmed_entrez_date":"2025-12-01","publication_year":"2025","canto_session_key":"918dbc7854d8a810","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-03 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32414915","title":"Two auxiliary factors promote Dmc1-driven DNA strand exchange via stepwise mechanisms.","citation":"Proc Natl Acad Sci U S A 2020 Jun 02;117(22):12062-12070","abstract":"Homologous recombination (HR) is a universal mechanism operating in somatic and germ-line cells, where it contributes to the maintenance of genome stability and ensures the faithful distribution of genetic material, respectively. The ability to identify and exchange the strands of two homologous DNA molecules lies at the heart of HR and is mediated by RecA-family recombinases. Dmc1 is a meiosis-specific RecA homolog in eukaryotes, playing a predominant role in meiotic HR. However, Dmc1 cannot function without its two major auxiliary factor complexes, Swi5-Sfr1 and Hop2-Mnd1. Through biochemical reconstitutions, we demonstrate that Swi5-Sfr1 and Hop2-Mnd1 make unique contributions to stimulate Dmc1-driven strand exchange in a synergistic manner. Mechanistically, Swi5-Sfr1 promotes establishment of the Dmc1 nucleoprotein filament, whereas Hop2-Mnd1 defines a critical, rate-limiting step in initiating strand exchange. Following execution of this function, we propose that Swi5-Sfr1 then promotes strand exchange with Hop2-Mnd1. Thus, our findings elucidate distinct yet complementary roles of two auxiliary factors in Dmc1-driven strand exchange, providing mechanistic insights into some of the most critical steps in meiotic HR.","doi":"10.1073/pnas.1917419117","authors":"Tsubouchi H, Argunhan B, Ito K, Takahashi M, Iwasaki H","authors_abbrev":"Tsubouchi H et al.","pubmed_publication_date":"02 Jun 2020","pubmed_entrez_date":"2020-05-17","publication_year":"2020","canto_session_key":"428266f53197a2f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hideo Tsubouchi","canto_first_approved_date":"2020-06-16 10:02:46","canto_approved_date":"2020-06-23 11:00:07","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-05-20 01:14:26","canto_added_date":"2020-05-18 00:15:04","annotation_curators":[{"name":"Hideo Tsubouchi","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.03c","SPAC13A11.03","SPAC644.14c","SPAC222.15","SPBC409.03","SPBC28F2.07"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2020-06-16"},{"uniquename":"PMID:20729203","title":"MAP kinase kinase kinase (MAPKKK)-dependent and -independent activation of Sty1 stress MAPK in fission yeast.","citation":"J Biol Chem 2010 Oct 22;285(43):32818-32823","abstract":"In fission yeast, the Sty1/Spc1/Phh1 mitogen-activated protein kinase (MAPK) pathway is known to be involved in multiple-stress responses. It is currently thought that the Sty1 MAPK cascade is mediated by histidine kinases and phosphorelay proteins in response to oxidative stress signals. However, studies of the exact transduction mechanism of multiple-stress responses are lacking. Thus, in response to various stimuli, we monitored the Sty1 MAPK pathway through the downstream transcription factor Atf1 in living cells using a highly sensitive luciferase reporter gene. Surprisingly, in cadmium and low glucose (LG) medium, Atf1 activation was observed even in the absence of all of the four fission yeast MAPK kinase kinases (MAPKKKs); whereas in osmotic stress, Atf1 activation was abolished. Thus, the osmotic stress likely mediates the MAPK activation via MAPKKKs, whereas a cadmium or LG condition activates the MAPK in a MAPKKK-independent manner. On the other hand, knockout of tyrosine phosphatase gene pyp1(+) abolished the Atf1 response to cadmium and LG, but not to osmotic stress, suggesting that Pyp1 is a sensor for cadmium and LG.","doi":"10.1074/jbc.M110.135764","authors":"Zhou X, Ma Y, Sugiura R, Kobayashi D, Suzuki M, Deng L, Kuno T","authors_abbrev":"Zhou X et al.","pubmed_publication_date":"22 Oct 2010","pubmed_entrez_date":"2010-08-24","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1006.09","SPBC1D7.05","SPAC9G1.02","SPAC1F3.02c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:33381837","title":"Matrix (factorization) reloaded: flexible methods for imputing genetic interactions with cross-species and side information.","citation":"Bioinformatics 2020 Dec 30;36(Suppl_2):i866-i874","abstract":"Mapping genetic interactions (GIs) can reveal important insights into cellular function and has potential translational applications. There has been great progress in developing high-throughput experimental systems for measuring GIs (e.g. with double knockouts) as well as in defining computational methods for inferring (imputing) unknown interactions. However, existing computational methods for imputation have largely been developed for and applied in baker's yeast, even as experimental systems have begun to allow measurements in other contexts. Importantly, existing methods face a number of limitations in requiring specific side information and with respect to computational cost. Further, few have addressed how GIs can be imputed when data are scarce.\nIn this article, we address these limitations by presenting a new imputation framework, called Extensible Matrix Factorization (EMF). EMF is a framework of composable models that flexibly exploit cross-species information in the form of GI data across multiple species, and arbitrary side information in the form of kernels (e.g. from protein-protein interaction networks). We perform a rigorous set of experiments on these models in matched GI datasets from baker's and fission yeast. These include the first such experiments on genome-scale GI datasets in multiple species in the same study. We find that EMF models that exploit side and cross-species information improve imputation, especially in data-scarce settings. Further, we show that EMF outperforms the state-of-the-art deep learning method, even when using strictly less data, and incurs orders of magnitude less computational cost.\nImplementations of models and experiments are available at: https://github.com/lrgr/EMF.\nSupplementary data are available at Bioinformatics online.","doi":"10.1093/bioinformatics/btaa818","authors":"Fan J, Li XC, Crovella M, Leiserson MDM","authors_abbrev":"Fan J et al.","pubmed_publication_date":"30 Dec 2020","pubmed_entrez_date":"2020-12-31","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-01-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23280723","title":"Mutations in the N-terminal region of the Schizosaccharomyces pombe glutathione transporter pgt1⁺ allows functional expression in Saccharomyces cerevisiae.","citation":"Yeast 2013 Feb;30(2):45-54","abstract":"Pgt1p encodes a glutathione transporter in Schizosaccharomyces pombe, orthologous to the Saccharomyces cerevisiae glutathione transporter, Hgt1p. Despite high similarity to Hgt1p, Pgt1p failed to display functionality during heterologous expression in S. cerevisiae. In the present study we employed a genetic strategy to investigate the reason behind the non-functionality of pgt1⁺ in S. cerevisiae. Functional mutants were isolated after in vitro mutagenesis. Several mutants were obtained and four mutants analysed. Among these, three yielded different point mutations in the N-terminal region (301-350 bp) of the transporter before the first transmembrane domain, while one mutant contained a deletion of 42 nucleotides within the same region. The mutant pgt1⁺ proteins not only expressed and localized correctly, but displayed high-affinity glutathione transport capabilities in S. cerevisae. Comparison of wild-type pgt1⁺ with the functional mutants revealed that a loss in protein expression was responsible for lack of functionality of wild-type pgt1⁺ in S. cerevisiae. The mRNA levels in wild-type and mutants were comparable, suggesting that the block was in translation. The formation of a strong stem-loop structure appeared to be responsible for inefficient translation in pgt1⁺ and disruption of these structures in the mutants was probably permitting translation. This was confirmed by making silent mutations in this region of wild-type pgt1⁺, which led to their functionality in S. cerevisiae. This genetic strategy to relieve functional blocks in expression should greatly facilitate the study of these and other transporters from more intractable genetic organisms in a heterologous expression system.","doi":"10.1002/yea.2939","authors":"Thakur A, Bachhawat AK","authors_abbrev":"Thakur A et al.","pubmed_publication_date":"Feb 2013","pubmed_entrez_date":"2013-01-03","publication_year":"2013","canto_session_key":"ab583a42bebeda77","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-08-13 10:00:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-01 15:28:59","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.10c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-08-01"},{"uniquename":"PMID:8771710","title":"Isolation and characterization of Schizosaccharomyces pombe fragile mutants.","citation":"Yeast 1996 May;12(6):555-64","abstract":"Three Schizosaccharomyces pombe fragile mutants requiring the presence of an osmotic stabilizer to grow, that lyse when transferred into hypotonic solutions and that secrete to the extracellular medium more protein than the parental strain were isolated. In the three mutants, the fragile phenotype segregated in a Mendelian fashion, indicating a single chromosomal gene mutation, and behaved as a recessive character. By complementation analysis, the three fragile mutants fell in a single complementation group, defining the same gene (SRB1). Mutations of this gene are responsible for alterations in the cells such as fragile character, increase in the cell wall porosity, changes in the cell morphology and floc-forming ability. The study of the three srb1 alleles indicated that the degree of these alterations is proportional to a significant decrease in the galactomannan fraction of the mutants cell wall. The data presented in this report suggest that the product of the SRB1 gene is critical for the maintenance of the integrity and structure of Sz. pombe cell wall.","authors":"Belda F, Zárate V","authors_abbrev":"Belda F et al.","pubmed_publication_date":"May 1996","pubmed_entrez_date":"1996-05-01","publication_year":"1996","canto_session_key":"6df27752f6a9b451","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-21 14:17:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-21 14:17:22","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-08-21"},{"uniquename":"PMID:20200159","title":"The LAMMER kinase homolog, Lkh1, regulates Tup transcriptional repressors through phosphorylation in Schizosaccharomyces pombe.","citation":"J Biol Chem 2010 Apr 30;285(18):13797-806","abstract":"Disruption of the fission yeast LAMMER kinase, Lkh1, gene resulted in diverse phenotypes, including adhesive filamentous growth and oxidative stress sensitivity, but an exact cellular function had not been assigned to Lkh1. Through an in vitro pull-down approach, a transcriptional repressor, Tup12, was identified as an Lkh1 binding partner. Interactions between Lkh1 and Tup11 or Tup12 were confirmed by in vitro and in vivo binding assays. Tup proteins were phosphorylated by Lkh1 in a LAMMER motif-dependent manner. The LAMMER motif was also necessary for substrate recognition in vitro and cellular function in vivo. Transcriptional activity assays using promoters negatively regulated by Tup11 and Tup12 showed 6 or 2 times higher activity in the Delta lkh1 mutant than the wild type, respectively. Northern analysis revealed derepressed expression of the fbp1(+) mRNA in Delta lkh1 and in Delta tup11 Delta tup12 mutant cells under repressed conditions. Delta lkh1 and Delta tup11 Delta tup12 mutant cells showed flocculation, which was reversed by co-expression of Tup11 and -12 with Ssn6. Here, we presented a new aspect of the LAMMER kinase by demonstrating that the activities of global transcriptional repressors, Tup11 and Tup12, were positively regulated by Lkh1-mediated phosphorylation.","doi":"10.1074/jbc.M110.113555","authors":"Kang WH, Park YH, Park HM","authors_abbrev":"Kang WH et al.","pubmed_publication_date":"30 Apr 2010","pubmed_entrez_date":"2010-03-05","publication_year":"2010","canto_session_key":"04b16267fe7a710d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-15 16:03:21","canto_approved_date":"2022-06-06 06:39:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-14 14:34:26","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":52,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.07c","SPAC630.14c","SPAC1D4.11c","SPBC1198.14c","SPBC23E6.09","SPAC18B11.10"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2018-08-15"},{"uniquename":"PMID:17927811","title":"Transcriptional regulatory network for sexual differentiation in fission yeast.","citation":"Genome Biol 2007;8(10):R217","abstract":"Changes in gene expression are hallmarks of cellular differentiation. Sexual differentiation in fission yeast (Schizosaccharomyces pombe) provides a model system for gene expression programs accompanying and driving cellular specialization. The expression of hundreds of genes is modulated in successive waves during meiosis and sporulation in S. pombe, and several known transcription factors are critical for these processes.\nWe used DNA microarrays to investigate meiotic gene regulation by examining transcriptomes after genetic perturbations (gene deletion and/or overexpression) of rep1, mei4, atf21 and atf31, which encode known transcription factors controlling sexual differentiation. This analysis reveals target genes at a genome-wide scale and uncovers combinatorial control by Atf21p and Atf31p. We also studied two transcription factors not previously implicated in sexual differentiation whose meiotic induction depended on Mei4p: Rsv2p induces stress-related genes during spore formation, while Rsv1p represses glucose-metabolism genes. Our data further reveal negative feedback interactions: both Rep1p and Mei4p not only activate specific gene expression waves (early and middle genes, respectively) but are also required for repression of genes induced in the previous waves (Ste11p-dependent and early genes, respectively).\nThese data give insight into regulatory principles controlling the extensive gene expression program driving sexual differentiation and highlight sophisticated interactions and combinatorial control among transcription factors. Besides triggering simultaneous expression of gene waves, transcription factors also repress genes in the previous wave and induce other factors that in turn regulate a subsequent wave. These dependencies ensure an ordered and timely succession of transcriptional waves during cellular differentiation.","authors":"Mata J, Wilbrey A, Bähler J","authors_abbrev":"Mata J et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-10-12","publication_year":"2007","canto_session_key":"a69a17d6ccdc273b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-16 16:20:10","canto_approved_date":"2024-04-25 16:28:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-16 16:20:01","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.06","SPAC22F3.02","SPBP4H10.09","SPBC1105.14","SPBC32H8.11","SPBC2F12.09c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-12-16"},{"uniquename":"PMID:14767070","title":"Mmd1p, a novel, conserved protein essential for normal mitochondrial morphology and distribution in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2004 Apr;15(4):1656-65","abstract":"The mmd1 mutation causes temperature-sensitive growth and defects in mitochondrial morphology and distribution in the fission yeast Schizosaccharomyces pombe. In mutant cells, mitochondria aggregate at the two cell ends, with increased aggregation at elevated temperatures. Microtubules, which mediate mitochondrial positioning in fission yeast, seem normal in mmd1 cells at permissive temperature and after several hours at the nonpermissive temperature but display aberrant organization after prolonged periods at 37 degrees C. Additionally, cells harboring both mmd1 and ban5-4, a temperature-sensitive allele of alpha2-tubulin, display synthetic defects in growth and mitochondrial distribution. The mmd1 mutation maps to an open reading frame encoding a novel 35.7-kDa protein. The Mmd1p sequence features repeating EZ-HEAT motifs and displays high conservation with uncharacterized homologues found in a variety of organisms. Saccharomyces cerevisiae cells depleted for their MMD1 homologue show increased sensitivity to the antimicrotubule drug benomyl, and the S. cerevisiae gene complemented the S. pombe mutation. Mmd1p was localized to the cytosol. Mmd1p is the first identified component required for the alignment of mitochondria along microtubules in fission yeast.","authors":"Weir BA, Yaffe MP","authors_abbrev":"Weir BA et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-02-10","publication_year":"2004","canto_session_key":"0ab184fae7a11f18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-06-29 10:22:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-06-29 10:21:45","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30C2.02","SPBC800.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-06-29"},{"uniquename":"PMID:23051734","title":"Myosin Vs organize actin cables in fission yeast.","citation":"Mol Biol Cell 2012 Dec;23(23):4579-91","abstract":"Myosin V motors are believed to contribute to cell polarization by carrying cargoes along actin tracks. In Schizosaccharomyces pombe, Myosin Vs transport secretory vesicles along actin cables, which are dynamic actin bundles assembled by the formin For3 at cell poles. How these flexible structures are able to extend longitudinally in the cell through the dense cytoplasm is unknown. Here we show that in myosin V (myo52 myo51) null cells, actin cables are curled, bundled, and fail to extend into the cell interior. They also exhibit reduced retrograde flow, suggesting that formin-mediated actin assembly is impaired. Myo52 may contribute to actin cable organization by delivering actin regulators to cell poles, as myoV defects are partially suppressed by diverting cargoes toward cell tips onto microtubules with a kinesin 7-Myo52 tail chimera. In addition, Myo52 motor activity may pull on cables to provide the tension necessary for their extension and efficient assembly, as artificially tethering actin cables to the nuclear envelope via a Myo52 motor domain restores actin cable extension and retrograde flow in myoV mutants. Together these in vivo data reveal elements of a self-organizing system in which the motors shape their own tracks by transporting cargoes and exerting physical pulling forces.","doi":"10.1091/mbc.E12-07-0499","authors":"Lo Presti L, Chang F, Martin SG","authors_abbrev":"Lo Presti L et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-10-12","publication_year":"2012","canto_session_key":"1a58c3ee1e7be06d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2016-10-02 23:11:17","canto_approved_date":"2025-05-27 20:21:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-11 16:57:24","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.14c","SPAC821.12","SPAC18G6.15","SPBC1604.14c","SPCC895.05","SPCC1919.10c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-10-02"},{"uniquename":"PMID:18682200","title":"Association of mitochondria with spindle poles facilitates spindle alignment.","citation":"Curr Biol 2008 Aug 05;18(15):R646-R647","abstract":"","doi":"10.1016/j.cub.2008.06.069","authors":"Krüger N, Tolić-Nørrelykke IM","authors_abbrev":"Krüger N et al.","pubmed_publication_date":"05 Aug 2008","pubmed_entrez_date":"2008-08-07","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39471327","title":"New mutations in the core Schizosaccharomyces pombe spindle pole body scaffold Ppc89 reveal separable functions in regulating cell division.","citation":"G3 (Bethesda) 2024 Oct 29;","abstract":"Centrosomes and spindle pole bodies (SPB) are important for mitotic spindle formation and also serve as signaling platforms. In the fission yeast Schizosaccharomyces pombe, genetic ablation and high-resolution imaging indicate that the ɑ-helical Ppc89 is central to SPB structure and function. Here, we developed and characterized conditional and truncation mutants of ppc89. Alleles with mutations in two predicted ɑ-helices near the C-terminus were specifically defective in anchoring Sid4, the scaffold for the septation initiation network (SIN), and proteins dependent on Sid4 (Cdc11, Dma1, Mto1 and Mto2). Artificial tethering of Sid4 to the SPB fully rescued these ppc89 mutants. Another ppc89 allele had mutations located throughout the coding region. While this mutant was also defective in Sid4 anchoring, it displayed additional defects including fragmented SPBs and forming and constricting a second cytokinetic ring in one daughter cell. These defects were shared with a ppc89 allele truncated of the most C-terminal predicted ɑ-helices that is still able to recruit Sid4 and the SIN. We conclude that Ppc89 not only tethers the SIN to the SPB but is also necessary for the integrity of the SPB and faithful coordination of cytokinesis with mitosis.","doi":"10.1093/g3journal/jkae249","authors":"Hanna SM, Tavafoghi B, Chen JS, Howard I, Ren L, Willet AH, Gould KL","authors_abbrev":"Hanna SM et al.","pubmed_publication_date":"29 Oct 2024","pubmed_entrez_date":"2024-10-29","publication_year":"2024","canto_session_key":"09ee8fea7eb8ca88","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2024-11-02 20:29:50","canto_approved_date":"2025-04-14 06:32:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-01 12:41:00","canto_added_date":"2024-10-30 00:25:05","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":47,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.10c","SPBC244.01c","SPBC428.13c","SPAC4H3.11c","SPBC8D2.05c","SPCC1739.11c","SPAC6G9.06c","SPCC417.07c","SPBC902.06","SPAC23C11.16","SPAC1565.06c"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2024-11-02"},{"uniquename":"PMID:22891673","title":"Fission yeast sec3 bridges the exocyst complex to the actin cytoskeleton.","citation":"Traffic 2012 Nov;13(11):1481-95","abstract":"The exocyst complex tethers post-Golgi secretory vesicles to the plasma membrane prior to docking and fusion. In this study, we identify Sec3, the missing component of the Schizosaccharomyces pombe exocyst complex (SpSec3). SpSec3 shares many properties with its orthologs, and its mutants are rescued by human Sec3/EXOC1. Although involved in exocytosis, SpSec3 does not appear to mark the site of exocyst complex assembly at the plasma membrane. It does, however, mark the sites of actin cytoskeleton recruitment and controls the organization of all three yeast actin structures: the actin cables, endocytic actin patches and actomyosin ring. Specifically, SpSec3 physically interacts with For3 and sec3 mutants have no actin cables as a result of a failure to polarize this nucleating formin. SpSec3 also interacts with actin patch components and sec3 mutants have depolarized actin patches of reduced endocytic capacity. Finally, the constriction and disassembly of the cytokinetic actomyosin ring is compromised in these sec3 mutant cells. We propose that a role of SpSec3 is to spatially couple actin machineries and their independently polarized regulators. As a consequence of its dual role in secretion and actin organization, Sec3 appears as a major co-ordinator of cell morphology in fission yeast.","doi":"10.1111/j.1600-0854.2012.01408.x","authors":"Jourdain I, Dooley HC, Toda T","authors_abbrev":"Jourdain I et al.","pubmed_publication_date":"Nov 2012","pubmed_entrez_date":"2012-08-16","publication_year":"2012","canto_session_key":"b86c94d0c7fb4dcc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Isabelle Jourdain","canto_first_approved_date":"2016-08-08 14:10:07","canto_approved_date":"2026-04-16 09:02:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-30 13:18:52","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Isabelle Jourdain","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.09","SPAC688.11","SPCC895.05","SPAC18G6.03","SPAC110.03","SPAC6G9.11","SPAC4F10.15c","SPCC1919.10c","SPAC15A10.16","SPAC17G8.12","SPAC19G12.14","SPBC106.20"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2016-08-08"},{"uniquename":"PMID:34649166","title":"Effects of ultrasound treatments on wine microorganisms.","citation":"Ultrason Sonochem 2021 Nov;79:105775","abstract":"Ultrasound is one of the most promising non-thermal an emerging technique in food technology. The objective of the present work was to evaluate the effect of different ultrasonic treatments on the most important wine microbiota (Saccharomyces and non-Saccharomyces yeasts and lactic acid bacteria). Two stages were carried out: the assessment step, where six different ultrasonic treatments (with varying power, time, and pulses) were used on Saccharomyces cerevisiae, Brettanomyces spp., and Lactiplantibacillus plantarum; and the validation step, where two chosen ultrasonic treatments were used on Zigosaccharomyces bailli, Brettanomyces spp., Saccharomyces cerevisiae, Saccharomyces bayanus, Pichia membranifaciens, Schizosaccharomyces pombe, and Hanseniaspora osmophila. The most sensitive microorganism was Brettanomyces spp., and the most resistant was Lactiplantibacillus plantarum. Ultrasonic treatments had varying effects on vitality (delay of growth or maximum OD reduction) and on viability (reduction of microbial growth).","doi":"10.1016/j.ultsonch.2021.105775","authors":"Muñoz R, Viveros N, Bevilacqua A, Pérez MS, Arévalo-Villena M","authors_abbrev":"Muñoz R et al.","pubmed_publication_date":"Nov 2021","pubmed_entrez_date":"2021-10-14","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-10-16 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013135","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25777942","title":"A novel protein, Rsf1/Pxd1, is critical for the single-strand annealing pathway of double-strand break repair in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2015 Jun;96(6):1211-25","abstract":"The process of single-strand annealing (SSA) repairs DNA double-strand breaks that are flanked by direct repeat sequences through the coordinated actions of a series of proteins implicated in recombination, mismatch repair and nucleotide excision repair (NER). Many of the molecular and mechanistic insights gained in SSA repair have principally come from studies in the budding yeast Saccharomyces cerevisiae. However, there is little molecular understanding of the SSA pathway in the fission yeast Schizosaccharomyces pombe. To further our understanding of this important process, we established a new chromosome-based SSA assay in fission yeast. Our genetic analyses showed that, although many homologous components participate in SSA repair in these species indicating that some evolutionary conservation, Saw1 and Slx4 are not principal agents in the SSA repair pathway in fission yeast. This is in marked contrast to the function of Saw1 and Slx4 in budding yeast. Additionally, a novel genus-specific protein, Rsf1/Pxd1, physically interacts with Rad16, Swi10 and Saw1 in vitro and in vivo. We find that Rsf1/Pxd1 is not required for NER and demonstrate that, in fission yeast, Rsf1/Pxd1, but not Saw1, plays a critical role in SSA recombination.","doi":"10.1111/mmi.13001","authors":"Wang H, Zhang Z, Zhang L, Zhang Q, Zhang L, Zhao Y, Wang W, Fan Y, Wang L","authors_abbrev":"Wang H et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-03-18","publication_year":"2015","canto_session_key":"e32056417ad1d374","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-19 01:15:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1322.02","SPBC4F6.15c","SPCC970.01","SPBC409.16c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:12748297","title":"Cohesins determine the attachment manner of kinetochores to spindle microtubules at meiosis I in fission yeast.","citation":"Mol Cell Biol 2003 Jun;23(11):3965-73","abstract":"During mitosis, sister kinetochores attach to microtubules that extend to opposite spindle poles (bipolar attachment) and pull the chromatids apart at anaphase (equational segregation). A multisubunit complex called cohesin, including Rad21/Scc1, plays a crucial role in sister chromatid cohesion and equational segregation at mitosis. Meiosis I differs from mitosis in having a reductional pattern of chromosome segregation, in which sister kinetochores are attached to the same spindle (monopolar attachment). During meiosis, Rad21/Scc1 is largely replaced by its meiotic counterpart, Rec8. If Rec8 is inactivated in fission yeast, meiosis I is shifted from reductional to equational division. However, the reason rec8Delta cells undergo equational rather than random division has not been clarified; therefore, it has been unclear whether equational segregation is due to a loss of cohesin in general or to a loss of a specific requirement for Rec8. We report here that the equational segregation at meiosis I depends on substitutive Rad21, which relocates to the centromeres if Rec8 is absent. Moreover, we demonstrate that even if sufficient amounts of Rad21 are transferred to the centromeres at meiosis I, thereby establishing cohesion at the centromeres, rec8Delta cells never recover monopolar attachment but instead secure bipolar attachment. Thus, Rec8 and Rad21 define monopolar and bipolar attachment, respectively, at meiosis I. We conclude that cohesin is a crucial determinant of the attachment manner of kinetochores to the spindle microtubules at meiosis I in fission yeast.","authors":"Yokobayashi S, Yamamoto M, Watanabe Y","authors_abbrev":"Yokobayashi S et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-05-16","publication_year":"2003","canto_session_key":"ae1c2b254e8c3cee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-11-18 17:09:41","canto_approved_date":"2024-11-18 17:09:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-18 17:09:10","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAC15E1.07c","SPBC29A10.14"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2024-11-18"},{"uniquename":"PMID:15704459","title":"[Dynamics of homologous chromosome pairing as observed in living cells of fission yeast].","citation":"Tanpakushitsu Kakusan Koso 2005 Feb;50(2):131-5","abstract":"","authors":"Ding DQ, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2005-02-12","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20656950","title":"Pneumocystis carinii expresses an active Rtt109 histone acetyltransferase.","citation":"Am J Respir Cell Mol Biol 2011 Jun;44(6):768-76","abstract":"Species in the genus Pneumocystis can cause severe pneumonia in immune-compromised hosts. The identification of specific targets present in Pneumocystis species, but lacking in mammalian hosts, is paramount to developing new means to treat this infection. One such potential protein is Rtt109, which is a type of histone acetyltransferase (HAT) required for DNA replication in fungi, but not found in mammals. Sequence orthologues of Rtt109 are present in other fungi, but are absent in mammals, making it a potential pan-specific target against medically relevant fungi. Accordingly, we sought to identify the presence of an Rtt109 in P. carinii. A Pneumocystis carinii (Pc) Rtt109 165-bp partial sequence was initially identified from the incomplete P. carinii genome database. Subsequently, a full-length, 1,128-bp cDNA with homology to Saccharomyces cerevisiae Rtt109 (39% Basic Local Alignment Search Tool (BLASTP)) was cloned and characterized. Sequence analysis of PcRtt109 indicated that the P. carinii molecule contains the putative catalytic aspartate present in yeast. We further demonstrated that the PcRtt109 expressed in rtt109Δ S. cerevisiae cells restored H3-K56 acetylation and the sensitivity toward DNA-damaging agents of rtt109Δ mutant cells. Purified PcRtt109 had the ability to acetylate lysine-56 of histone H3, similar to the ability of Schizosaccharomyces pombe Rtt109 protein. The site-directed mutagenesis of PcRtt109 D84A, a potential regulatory site in the Rtt109 HAT family, abolished H3 acetylation, whereas a DD218/219AA mutation that compromised the activity of ScRtt109 had little effect, demonstrating similarities and differences in Pneumocystis PcRtt109 compared with yeast Saccharomyces cerevisiae Rtt109. These results indicate that P. carinii contains an Rtt109 HAT molecule, and represent the complete identification and characterization of a HAT molecule from this important opportunistic fungal pathogen.","doi":"10.1165/rcmb.2009-0443OC","authors":"Kottom TJ, Han J, Zhang Z, Limper AH","authors_abbrev":"Kottom TJ et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2010-07-27","publication_year":"2011","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC342.06c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:18673302","title":"Hydrolytic cleavage of N6-substituted adenine derivatives by eukaryotic adenine and adenosine deaminases.","citation":"Biosci Rep 2008 Dec;28(6):335-47","abstract":"Homogeneous adenine deaminases (EC 3.5.4.2) from the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe and a putative ADA (adenosine deaminase; EC 3.5.4.4) from Arabidopsis thaliana were obtained for the first time as purified recombinant proteins by molecular cloning of the corresponding genes and their overexpression in Escherichia coli. The enzymes showed comparable molecular properties with well-known mammalian ADAs, but exhibited much lower k(cat) values. Adenine was the most favoured substrate for the yeast enzymes, whereas the plant enzyme showed only very low activities with either adenine, adenosine, AMP or ATP. Interestingly, the yeast enzymes also hydrolysed N6-substituted adenines from cytokinins, a group of plant hormones, cleaving them to inosine and the corresponding side chain amine. The hydrolytic cleavage of synthetic cytokinin 2,6-di-substituted analogues that are used in cancer therapy, such as olomoucine, roscovitine and bohemine, was subsequently shown for a reference sample of human ADA1. ADA1, however, showed a different reaction mechanism to that of the yeast enzymes, hydrolysing the compounds to an adenine derivative and a side chain alcohol. The reaction products were identified using reference compounds on HPLC coupled to UV and Q-TOF (quadrupole-time-of-flight) detectors.The ADA1 activity may constitute the debenzylation metabolic route already described for bohemine and, as a consequence, it may compromise the physiological or therapeutic effects of exogenously applied cytokinin derivatives.","doi":"10.1042/BSR20080081","authors":"Pospísilová H, Sebela M, Novák O, Frébort I","authors_abbrev":"Pospísilová H et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-08-05","publication_year":"2008","canto_session_key":"74a22684ab11802a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-06-20 15:58:50","canto_approved_date":"2025-04-28 15:50:51","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-06-20 15:58:43","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1198.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-06-20"},{"uniquename":"PMID:37787768","title":"Broad functional profiling of fission yeast proteins using phenomics and machine learning.","citation":"Elife 2023 Oct 03;12","abstract":"Many proteins remain poorly characterized even in well-studied organisms, presenting a bottleneck for research. We applied phenomics and machine-learning approaches with  Schizosaccharomyces pombe  for broad cues on protein functions. We assayed colony-growth phenotypes to measure the fitness of deletion mutants for 3509 non-essential genes in 131 conditions with different nutrients, drugs, and stresses. These analyses exposed phenotypes for 3492 mutants, including 124 mutants of 'priority unstudied' proteins conserved in humans, providing varied functional clues. For example, over 900 proteins were newly implicated in the resistance to oxidative stress. Phenotype-correlation networks suggested roles for poorly characterized proteins through 'guilt by association' with known proteins. For complementary functional insights, we predicted Gene Ontology (GO) terms using machine learning methods exploiting protein-network and protein-homology data (NET-FF). We obtained 56,594 high-scoring GO predictions, of which 22,060 also featured high information content. Our phenotype-correlation data and NET-FF predictions showed a strong concordance with existing PomBase GO annotations and protein networks, with integrated analyses revealing 1675 novel GO predictions for 783 genes, including 47 predictions for 23 priority unstudied proteins. Experimental validation identified new proteins involved in cellular aging, showing that these predictions and phenomics data provide a rich resource to uncover new protein functions.","doi":"10.7554/eLife.88229","authors":"Rodríguez-López M, Bordin N, Lees J, Scholes H, Hassan S, Saintain Q, Kamrad S, Orengo C, Bähler J","authors_abbrev":"Rodríguez-López M et al.","pubmed_publication_date":"03 Oct 2023","pubmed_entrez_date":"2023-10-03","publication_year":"2023","canto_session_key":"b3a44dcb34e53067","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-10-04 09:10:14","canto_approved_date":"2023-10-04 09:10:14","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-10-04 09:10:05","canto_added_date":"2023-10-03 23:25:04","annotation_curators":[],"file_curator_name":"Manuel Lera-Ramirez","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Manuel 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regulation of the gene encoding thioredoxin reductase from the fission yeast.","citation":"FEMS Microbiol Lett 2004 May 15;234(2):379-85","abstract":"The unique putative gene for thioredoxin reductase (TrxR) was isolated from the chromosomal DNA of the fission yeast Schizosaccharomyces pombe. The determined DNA sequence carries 3125 bp, and encodes the plausible 322 amino acid sequence of TrxR with a molecular mass of 34,618 Da. The S. pombe cells harboring the cloned TrxR gene contain increased TrxR activity, and shows higher survivals on solid media with mercuric chloride or aluminum chloride. The 1526 bp upstream region was fused into promoterless beta-galactosidase gene of the shuttle vector YEp367R to generate the fusion plasmid. The synthesis of beta-galactosidase from the fusion plasmid pYUTR10 was enhanced by menadione, mercuric chloride, hydrogen peroxide, aluminium chloride and sodium selenite. Menadione significantly enhanced the TrxR mRNA level in the S. pombe cells, which was detected by RT-PCR. Induction of the S. pombe TrxR gene by menadione and mercuric chloride occurs through the mediation of the transcription factor Pap1. These results suggest that the S. pombe TrxR gene is one of the stress response-related genes.","authors":"Hong SM, Lim HW, Kim IH, Kim K, Park EH, Lim CJ","authors_abbrev":"Hong SM et al.","pubmed_publication_date":"15 May 2004","pubmed_entrez_date":"2004-05-12","publication_year":"2004","canto_session_key":"8048f8fcdc4f54ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-26 08:25:48","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-26 08:25:41","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPBC29B5.01","SPAC24B11.06c","SPAC1783.07c","SPBC3F6.03"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2014-11-26"},{"uniquename":"PMID:14463416","title":"Interaction of the ribosomes of Schizosaccharomyces pombe and Escherichia coli.","citation":"Biochim Biophys Acta 1962 Jan 22;55:104-9","abstract":"","authors":"LEDERBERG S, MITCHISON JM","authors_abbrev":"LEDERBERG S et al.","pubmed_publication_date":"22 Jan 1962","pubmed_entrez_date":"1962-01-22","publication_year":"1962","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9065388","title":"Homologous recombination in the fission yeast Schizosaccharomyces pombe: different requirements for the rhp51+, rhp54+ and rad22+ genes.","citation":"Curr Genet 1997 Mar;31(3):248-54","abstract":"The Schizosaccharomyces pombe rhp51+, rad22+ and rhp54+ genes are homologous to RAD51, RAD52 and RAD54 respectively, which are indispensable in the recombinational repair of double-strand breaks (DSBs) in Saccharomyces cerevisiae. The rhp51Delta and rhp54Delta strains are extremely sensitive to ionizing radiation; the rad22Delta mutant turned out to be much less sensitive. Homologous recombination in these mutants was studied by targeted integration at the leu1-32 locus. These experiments revealed that rhp51Delta and rhp54Delta are equally impaired in the integration of plasmid molecules (15-fold reduction), while integration in the rad22Delta mutant is only reduced by a factor of two. Blot-analysis demonstrated that the majority of the leu+ transformants of the wild-type and rad22Delta strains have integrated one or more copies of the vector. Gene conversion events were observed in less than 10% of the transformants. Interestingly, the relative contribution of gene conversion events is much higher in a rhp51Delta and a rhp54Delta background. Meiotic recombination is hardly affected in the rad22Delta mutant. The rhp51Delta and rhp54Delta strains also show minor deficiencies in this type of recombination. The viability of spores is 46% in the rad22Delta strain and 27% in the rhp54Delta strain, as compared with wild-type cells. However, in the rhp51Delta mutant the spore viability is only 1.7%, suggesting an essential role for Rhp51 in meiosis. The function of Rhp51 and Rhp54 in damage repair and recombination resembles the role of Rad51 and Rad54 in S. cerevisiae. Compared with Rad52 from S. cerevisiae, Rad22 has a much less prominent role in the recombinational repair pathway in S. pombe.","authors":"Muris DF, Vreeken K, Schmidt H, Ostermann K, Clever B, Lohman PH, Pastink A","authors_abbrev":"Muris DF et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30104346","title":"Mre11 complex links sister chromatids to promote repair of a collapsed replication fork.","citation":"Proc Natl Acad Sci U S A 2018 Aug 28;115(35):8793-8798","abstract":"Collapsed replication forks, which are a major source of DNA double-strand breaks (DSBs), are repaired by sister chromatid recombination (SCR). The Mre11-Rad50-Nbs1 (MRN) protein complex, assisted by CtIP/Sae2/Ctp1, initiates SCR by nucleolytically resecting the single-ended DSB (seDSB) at the collapsed fork. The molecular architecture of the MRN intercomplex, in which zinc hooks at the apices of long Rad50 coiled-coils connect two Mre11 2 -Rad50 2  complexes, suggests that MRN also structurally assists SCR. Here, Rad50 ChIP assays in  Schizosaccharomyces pombe  show that MRN sequentially localizes with the seDSB and sister chromatid at a collapsed replication fork. Ctp1, which has multivalent DNA-binding and DNA-bridging activities, has the same DNA interaction pattern. Provision of an intrachromosomal repair template alleviates the nonnucleolytic requirement for MRN to repair the broken fork. Mutations of zinc-coordinating cysteines in the Rad50 hook severely impair SCR. These data suggest that the MRN complex facilitates SCR by linking the seDSB and sister chromatid.","doi":"10.1073/pnas.1808189115","authors":"Zhu M, Zhao H, Limbo O, Russell P","authors_abbrev":"Zhu M et al.","pubmed_publication_date":"28 Aug 2018","pubmed_entrez_date":"2018-08-15","publication_year":"2018","canto_session_key":"7e7c2c9e26201c7d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2018-09-18 12:08:06","canto_approved_date":"2018-09-29 20:14:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-29 23:05:31","canto_added_date":"2018-08-16 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.06c","SPBC30D10.04","SPAC13C5.07","SPCC338.08","SPAC1556.01c","SPCC126.02c","SPAC30D11.10","SPBC216.05","SPAC20G8.01"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2018-09-18"},{"uniquename":"PMID:40584586","title":"Dissecting the cell cycle regulation, DNA damage sensitivity and lifespan effects of caffeine in fission yeast.","citation":"Microb Cell 2025;12:141-156","abstract":"Caffeine can modulate cell cycle progression, override DNA damage checkpoint signalling and increase chronological lifespan (CLS) in various model systems. Early studies suggested that caffeine inhibits the phosphatidylinositol 3-kinase-related kinase (PIKK) Rad3 to override DNA damage-induced cell cycle arrest in fission yeast. We have previously suggested that caffeine modulates cell cycle progression and lifespan by inhibiting the Target of Rapamycin Complex 1 (TORC1). Nevertheless, whether this inhibition is direct or not, has remained elusive. TORC1 controls metabolism and mitosis timing by integrating nutrients and environmental stress response (ESR) signalling. Nutritional or other stresses activate the Sty1-Ssp1-Ssp2 (AMP-activated protein kinase complex, AMPK) pathway, which inhibits TORC1 and accelerates mitosis through Sck2 inhibition. Additionally, activation of the ESR pathway can extend lifespan in fission yeast. Here, we demonstrate that caffeine indirectly activates Ssp1, Ssp2 and the AMPKβ regulatory subunit Amk2 to advance mitosis. Ssp2 is phosphorylated in an Ssp1-dependent manner following exposure to caffeine. Furthermore, Ssp1 and Amk2, are required for resistance to caffeine under conditions of prolonged genotoxic stress. The effects of caffeine on DNA damage sensitivity are uncoupled from mitosis in AMPK pathway mutants. We propose that caffeine interacts synergistically with other genotoxic agents to increase DNA damage sensitivity. Our findings show that caffeine accelerates mitotic division and is beneficial for CLS through AMPK. Direct pharmacological targeting of AMPK may serve towards healthspan and lifespan benefits beyond yeasts, given the highly conserved nature of this key regulatory cellular energy sensor.","doi":"10.15698/mic2025.06.852","authors":"Alao JP, Kumar J, Stamataki D, Rallis C","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-06-30","publication_year":"2025","canto_session_key":"80677c0e2271aa43","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-01 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1687.15"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18616168","title":"[Expression, purification and characterization of N-glycanase from Schizosaccharomyces pombe in Escherichia coli].","citation":"Sheng Wu Gong Cheng Xue Bao 2008 Apr;24(4):592-7","abstract":"One pair of primers were designed and synthesized on the base of the cDNA sequence encoding Schizosaccharomyces pombe N-glycanase reported on the GenBank. The cDNA sequence encoding Peptide N-glycanase was cloned from the Schizosaccharomyces pombe by RT-PCR. And then the RT-PCR product was cloned into the expression vector pET-15b. The expression vector pET-15b(+)/Png1p was transformed into E. coli BL21(DE3). The results showed that the relative molecular weight of the enzyme was determined to be approximately 39 kD using SDS-PAGE. The expression products after induction and purification can catalyze the cleavage of N-linked oligosaccharides from glycoprotein coped with heat, but have no action on the native glycoprotein with the help of DTT. The percentage of deglycosylated RNase B treated with equate Png1p in different reaction temperature, pH, concentration of DTT and denatured temperature showed that the optimum temperature, the optimum pH is 30 degrees C; the optimum concentration of DTT is 10 mmol/L and the optimum denatured temperature is 100 degrees C.","authors":"Xin F, Wang P, Zhong S, Qi Q","authors_abbrev":"Xin F et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-07-12","publication_year":"2008","canto_session_key":"6d64c085e3595ba6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-02 20:17:51","canto_approved_date":"2023-07-02 20:17:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-02 20:17:44","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1709.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-07-02"},{"uniquename":"PMID:1417417","title":"Electron microscopic examination of sporulation-deficient mutants of the fission yeast Schizosaccharomyces pombe.","citation":"Arch Microbiol 1992;158(4):249-55","abstract":"A homothallic haploid strain of the fission yeast Schizosaccharomyces pombe initiates sexual reproduction (mating, meiosis and sporulation) in nitrogen-free sporulation medium. Cellular fine structures of eleven sporulation-deficient mutants (spo2, spo3, spo4, spo5, spo6, spo13, spo14, spo15, spo18, spo19 and spo20) of S. pombe in sporulation medium were examined by serial section-electron microscopy. The striking features of these spo mutants were: 1) the disappearance of the spindle pole bodies (SPBs) after the second meiotic division, and 2) the accumulation of unorganized structures. Based on histochemical staining, these structures were presumably unorganized spore wall precursors. In some mutants (spo3, spo5, spo6, spo19 and spo20), diploid zygotes contained four spore-like bodies which had walls similar to complete spore walls but failed to enclose any nuclei. After completion of the second meiotic division the nuclei were abnormally distributed in zygotic diploid cells. In the spo5, spo13, spo14, spo15 and spo19 mutants, the nuclei remained attached to each other. In spo5 and spo19, the inner membrane of the nuclear envelope was separated, but its outer membrane was shared by two sister nuclei. These observations suggest that the spo+ gene products play important roles in spatial and temporal organization of cellular structures during ascospore development.","authors":"Hirata A, Shimoda C","authors_abbrev":"Hirata A et al.","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_session_key":"193a1a23b912484d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-11-01 14:11:37","canto_approved_date":"2022-12-12 17:18:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-12 12:17:01","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"vw253 cam.ac.uk","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.06c","SPBC1778.04","SPAC607.10","SPBC3H7.01","SPBC29A10.02","SPBC21C3.18","SPAC3H8.10","SPBC16C6.14","SPCC1183.12"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2013-11-01"},{"uniquename":"PMID:20370606","title":"Oxidative stress in yeast.","citation":"Biochemistry (Mosc) 2010 Mar;75(3):281-96","abstract":"The mechanisms of production and elimination of reactive oxygen species in the cells of the budding yeast Saccharomyces cerevisiae are analyzed. Coordinative role of special regulatory proteins including Yap1p, Msn2/4p, and Skn7p (Pos9p) in regulation of defense mechanisms in S. cerevisiae is described. A special section is devoted to two other well-studied species from the point of view of oxidative stress -- Schizosaccharomyces pombe and Candida albicans. Some examples demonstrating the use of yeast for investigation of apoptosis, aging, and some human diseases are given in the conclusion part.","authors":"Lushchak VI","authors_abbrev":"Lushchak VI","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2010-04-08","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19640845","title":"Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe.","citation":"J Biol Chem 2009 Sep 18;284(38):25944-52","abstract":"D-serine is an endogenous coagonist for the N-methyl-D-aspartate receptor and is involved in excitatory neurotransmission in the brain. Mammalian pyridoxal 5'-phosphate-dependent serine racemase, which is localized in the mammalian brain, catalyzes the racemization of L-serine to yield D-serine and vice versa. The enzyme also catalyzes the dehydration of D- and L-serine. Both reactions are enhanced by Mg.ATP in vivo. We have determined the structures of the following three forms of the mammalian enzyme homolog from Schizosaccharomyces pombe: the wild-type enzyme, the wild-type enzyme in the complex with an ATP analog, and the modified enzyme in the complex with serine at 1.7, 1.9, and 2.2 A resolution, respectively. On binding of the substrate, the small domain rotates toward the large domain to close the active site. The ATP binding site was identified at the domain and the subunit interface. Computer graphics models of the wild-type enzyme complexed with L-serine and D-serine provided an insight into the catalytic mechanisms of both reactions. Lys-57 and Ser-82 located on the protein and solvent sides, respectively, with respect to the cofactor plane, are acid-base catalysts that shuttle protons to the substrate. The modified enzyme, which has a unique \"lysino-D-alanyl\" residue at the active site, also exhibits catalytic activities. The crystal-soaking experiment showed that the substrate serine was actually trapped in the active site of the modified enzyme, suggesting that the lysino-D-alanyl residue acts as a catalytic base in the same manner as inherent Lys-57 of the wild-type enzyme.","doi":"10.1074/jbc.M109.010470","authors":"Goto M, Yamauchi T, Kamiya N, Miyahara I, Yoshimura T, Mihara H, Kurihara T, Hirotsu K, Esaki N","authors_abbrev":"Goto M et al.","pubmed_publication_date":"18 Sep 2009","pubmed_entrez_date":"2009-07-31","publication_year":"2009","canto_session_key":"cf585b9c734ef177","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-25 15:21:51","canto_approved_date":"2026-02-13 09:05:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-25 14:34:56","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-25","pdb_entries":[{"pdb_id":"1wtc","gene_chains":[{"gene_uniquename":"SPCC320.14","chain":"A","position":"1-323"}],"title":"Crystal Structure of S.pombe Serine Racemase complex with AMPPCP","entry_authors":"Goto M,Miyahara I,Hirotsu K","entry_authors_abbrev":"Goto M et al.","reference_uniquename":"PMID:19640845","experimental_method":"X-ray","resolution":"1.9"},{"pdb_id":"2zr8","gene_chains":[{"gene_uniquename":"SPCC320.14","chain":"A","position":"1-323"}],"title":"Crystal Structure of Modified Serine Racemase complexed with Serine","entry_authors":"Goto M","entry_authors_abbrev":"Goto M","reference_uniquename":"PMID:19640845","experimental_method":"X-ray","resolution":"2.2"}]},{"uniquename":"EMBL:AU006805","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.117"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22669973","title":"Fission yeast Dma1 requires RING domain dimerization for its ubiquitin ligase activity and mitotic checkpoint function.","citation":"J Biol Chem 2012 Jul 27;287(31):25741-8","abstract":"In fission yeast (Schizosaccharomyces pombe), the E3 ubiquitin ligase Dma1 delays cytokinesis if chromosomes are not properly attached to the mitotic spindle. Dma1 contains a C-terminal RING domain, and we have found that the Dma1 RING domain forms a stable homodimer. Although the RING domain is required for dimerization, residues in the C-terminal tail are also required to help form or stabilize the dimeric structure because mutation of specific residues in this region disrupts Dma1 dimerization. Further analyses showed that Dma1 dimerization is required for proper localization at spindle pole bodies and the cell division site, E3 ligase activity, and mitotic checkpoint function. Thus, Dma1 forms an obligate dimer via its RING domain, which is essential for efficient transfer of ubiquitin to its substrate(s). This study further supports the mechanistic paradigm that many RING E3 ligases function as RING dimers.","doi":"10.1074/jbc.M112.349712","authors":"Johnson AE, Collier SE, Ohi MD, Gould KL","authors_abbrev":"Johnson AE et al.","pubmed_publication_date":"27 Jul 2012","pubmed_entrez_date":"2012-06-07","publication_year":"2012","canto_session_key":"6b153a4a0b268a6c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2019-02-02 16:24:29","canto_approved_date":"2026-03-05 08:04:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-15 14:52:33","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPAC17G8.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-02-02"},{"uniquename":"EMBL:AY007252","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16043696","title":"Cohesins are required for meiotic DNA breakage and recombination in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 2005 Aug 02;102(31):10952-7","abstract":"In preparation for the unique segregation of homologs at the first meiotic division, chromosomes undergo dramatic changes. The meiosis-specific sister chromatid cohesins Rec8 and Rec11 of Schizosaccharomyces pombe are recruited around the time of premeiotic replication, and Rec10, a component of meiosis-specific linear elements, is subsequently added. Here we report that Rec10 is essential for meiosis-specific DNA breakage by Rec12 (Spo11 homolog) and for meiotic recombination. DNA breakage and recombination also depend on the Rec8 and Rec11 cohesins, strictly in some genomic intervals but less so in others. Thus, in addition to their previously recognized role in meiotic chromosome segregation, cohesins have a direct role, as do linear element components, in meiotic recombination by enabling double-strand DNA break formation by Rec12. Our results reveal a pathway, whose regulation is significantly different from that in the distantly related yeast Saccharomyces cerevisiae, for meiosis-specific chromosome differentiation and high-frequency recombination.","authors":"Ellermeier C, Smith GR","authors_abbrev":"Ellermeier C et al.","pubmed_publication_date":"02 Aug 2005","pubmed_entrez_date":"2005-07-27","publication_year":"2005","canto_session_key":"ff30295f5d32f513","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-07 13:29:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-07 13:29:18","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.04c","SPAC13C5.07","SPBC29A10.14","SPCC4E9.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-08-07"},{"uniquename":"PMID:9658208","title":"Sensitivity to cisplatin and platinum-containing compounds of Schizosaccharomyces pombe rad mutants.","citation":"Mol Pharmacol 1998 Jul;54(1):213-9","abstract":"The role of genes that affect response to radiation in determining sensitivity to platinum-containing compounds was studied using a panel of 23 strains of the yeast Schizosaccharomyces pombe. The radiation-hypersensitive mutants all had the same genetic background and most of them contained mutations that disabled either cell cycle checkpoints or DNA repair. The tested platinum compounds included cisplatin and two complexes containing diaminocyclohexane (oxaliplatin and tetraplatin), two ammine/cyclohexylamine complexes with different orientation of the leaving groups (JM216 and JM335) and a multinuclear platinum complex (BBR 3464). The cytotoxic effect of the selected platinum complexes was evaluated by using a microtiter growth inhibition assay with a 48 hr exposure to drug. The mutants fell into three groups with respect to sensitivity to cisplatin: four mutants (rad2, -7, -11, -15) exhibited minimal change in sensitivity; fifteen mutants (rad4-6, -8-10, -12-14, -16-17, -19-21, and -22) were 5.1-21.7-fold hypersensitive; only rad1 and -3 mutants, defective in checkpoints, and rad18, defective in repair, displayed a marked hypersensitivity. None of the mutants demonstrated appreciable change in sensitivity to JM216 presumably as a consequence of a lack of resistance of the wild-type strain, whereas a moderate increase in sensitivity to JM335 was observed for most of the mutants, and hypersensitivity to BBR3464 was observed only in rad1 and -3. No relevant changes in sensitivity to tetraplatin were observed. Most of the mutants, with the exception of rad2, -7, and -15, were hypersensitive to oxaliplatin. These findings demonstrate that specific mutations have disparate effects on the profile of sensitivity to different members of the same class of cytotoxic agents, which provides genetic evidence that different mechanisms are involved in differential cytotoxicity induced by Pt compounds. The results also demonstrate the utility of such a panel of mutants, constructed on the same genetic background, for detecting specific cellular response; presumably, this reflects the recognition or processing of specific DNA adducts. In conclusion, because the rad1 and rad3 gene products are determinants of cellular response to a large number of platinum-containing compounds, the present results support a critical role of genes involved in cell cycle control in cellular sensitivity to these agents.","authors":"Perego P, Zunino F, Carenini N, Giuliani F, Spinelli S, Howell SB","authors_abbrev":"Perego P et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-07-11","publication_year":"1998","canto_session_key":"06c34b4476712d4c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"antonia lock","canto_first_approved_date":"2017-06-30 10:56:54","canto_approved_date":"2024-04-04 08:37:36","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-04-04 08:30:50","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"antonia lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":147,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_9658208_phaf.tsv"}],"genes":["SPAC14C4.13","SPAC3G6.06c","SPAC1952.07","SPBC660.13c","SPAC1D4.12","SPCC338.17c","SPCC970.01","SPAC23C4.18c","SPAC18B11.07c","SPAC30D11.10","SPBC216.05","SPAC2G11.12","SPAC664.07c","SPBC3E7.08c","SPCC5E4.06","SPCC330.02","SPAC13G6.01c"],"gene_count":17,"ltp_gene_count":17,"approved_date":"2017-06-30"},{"uniquename":"PMID:37291244","title":"A set of vectors and strains for chromosomal integration in fission yeast.","citation":"Sci Rep 2023 Jun 08;13(1):9295","abstract":"The expression of heterologous genes is an important technique in yeast genetics. In fission yeast, the leu1 and ura4 genes have been used mainly as selectable markers for heterologous expression. To expand the repertoire of selection markers available for heterologous expression of genes, here we developed new host-vector systems employing lys1 and arg3. By employing genome editing with the CRISPR/Cas9 system, we isolated several alleles of lys1 and arg3, each having a critical mutation in the ORF region. In parallel, we developed a set of vectors that complement the amino acid auxotrophy of lys1 and arg3 mutants when integrated into each locus. Using these vectors in combination with the previously developed integration vector pDUAL, we successfully observed the localization of three proteins in a cell simultaneously by fusing them with different fluorescent proteins. Thus, these vectors enable combinatorial expression of heterologous genes, which addresses increasingly diverse experimental challenges.","doi":"10.1038/s41598-023-36267-1","authors":"Matsuyama A, Hashimoto A, Nishimura S, Yoshida M","authors_abbrev":"Matsuyama A et al.","pubmed_publication_date":"08 Jun 2023","pubmed_entrez_date":"2023-06-08","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-06-10 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31239353","title":"Zinc-dependent activation of the Pho8 alkaline phosphatase in  Schizosaccharomyces pombe .","citation":"J Biol Chem 2019 Aug 16;294(33):12392-12404","abstract":"Genome-wide analyses have revealed that during metal ion starvation, many cells undergo programmed changes in their transcriptome or proteome that lower the levels of abundant metalloproteins, conserving metal ions for more critical functions. Here we investigated how changes in cellular zinc status affect the expression and activity of the zinc-requiring Pho8 alkaline phosphatase from fission yeast ( Schizosaccharomyces pombe ). In  S. pombe , Pho8 is a membrane-tethered and processed glycoprotein that resides in the vacuole. Using alkaline phosphatase activity assays along with various biochemical analyses, we found that Pho8 is active when zinc is plentiful and inactive when zinc is limited. Although Pho8 activity depended on zinc, we also found that higher levels of  pho8  mRNAs and Pho8 protein accumulate in zinc-deficient cells. To gain a better understanding of the inverse relationship between  pho8  mRNA levels and Pho8 activity, we examined the effects of zinc on the stability and processing of the Pho8 protein. We show that Pho8 is processed regardless of zinc status and that mature Pho8 accumulates under all conditions. We also noted that alkaline phosphatase activity is rapidly restored when zinc is resupplied to cells, even in the presence of the protein synthesis inhibitor cycloheximide. Our results suggest that  S. pombe  cells maintain inactive pools of Pho8 proteins under low-zinc conditions and that these pools facilitate rapid restoration of Pho8 activity when zinc ions become available.","doi":"10.1074/jbc.RA119.007371","authors":"Hu YM, Boehm DM, Chung H, Wilson S, Bird AJ","authors_abbrev":"Hu YM et al.","pubmed_publication_date":"16 Aug 2019","pubmed_entrez_date":"2019-06-27","publication_year":"2019","canto_session_key":"2c0b3f9b052bea9e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Amanda Bird","canto_first_approved_date":"2019-08-23 08:25:28","canto_approved_date":"2026-03-23 21:53:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-09 14:16:00","canto_added_date":"2019-06-28 00:15:03","annotation_curators":[{"name":"Amanda Bird","community_curator":true,"annotation_count":22,"orcid":"0000-0002-1846-7050","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H4.09","SPAC1296.03c","SPBC16E9.14c","SPAC17D4.03c","SPBC15D4.15","SPAC1006.01","SPAC4A8.04","SPAC25B8.19c","SPAC23C11.14","SPBC14F5.13c","SPBC18A7.01"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2019-08-23"},{"uniquename":"PMID:3031478","title":"Sucl+ encodes a predicted 13-kilodalton protein that is essential for cell viability and is directly involved in the division cycle of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1987 Jan;7(1):504-11","abstract":"Sucl+ was originally identified as a DNA sequence that, at high copy number, rescued Schizosaccharomyces pombe strains carrying certain temperature-sensitive alleles of the cdc2 cell cycle control gene. We determined the nucleotide sequence of a 1,083-base-pair Sucl+ DNA fragment and S1 mapped its 866-nucleotide RNA transcript. The protein-coding sequence of the gene is interrupted by two intervening sequences of 115 and 51 base pairs. The predicted translational product of the gene is a protein of 13 kilodaltons. A chromosomal gene disruption of Sucl+ was constructed in a diploid S. pombe strain. Germinating spores carrying a null allele of the gene were capable of very limited cell division, following which many cells became highly elongated. The Sucl+ gene was also strongly overexpressed under the control of a heterologous S. pombe promoter. Overexpression of Sucl+ is not lethal but causes a division delay such that cells are approximately twice the normal length at division. These data suggest that Sucl+ encodes a protein which plays a direct role in the cell division cycle of S. pombe.","authors":"Hindley J, Phear G, Stein M, Beach D","authors_abbrev":"Hindley J et al.","pubmed_publication_date":"Jan 1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_session_key":"8a3e6d23ff2153d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-09-17 14:42:16","canto_approved_date":"2022-03-31 16:54:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 13:49:38","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-17"},{"uniquename":"PMID:7626804","title":"The Wee1 protein kinase regulates T14 phosphorylation of fission yeast Cdc2.","citation":"Mol Biol Cell 1995 Apr;6(4):371-85","abstract":"The Cdc2 protein kinase is a key regulator of the G1-S and G2-M cell cycle transitions in the fission yeast Schizosaccharomyces pombe. The activation of Cdc2 at the G2-M transition is triggered by dephosphorylation at a conserved tyrosine residue Y15. The level of Y15 phosphorylation is controlled by the Wee1 and Mik1 protein kinases acting in opposition to the Cdc25 protein phosphatase. Here, we demonstrate that Wee1 overexpression leads to a high stoichiometry of phosphorylation at a previously undetected site in S. pombe Cdc2, T14. T14 phosphorylation was also detected in certain cell cycle mutants blocked in progression through S phase, indicating that T14 phosphorylation might normally occur at low stoichiometry during DNA replication or early G2. Strains in which the chromosomal copy of cdc2 was replaced with either a T14A or a T14S mutant allele were generated and the phenotypes of these strains are consistent with T14 phosphorylation playing an inhibitory role in the activation of Cdc2 as it does in higher eukaryotes. We have also obtained evidence that Wee1 but not Mik1 or Chk1 is required for phosphorylation at this site, that the Mik1 and Chk1 protein kinases are unable to drive T14 phosphorylation in vivo, that residue 14 phosphorylation requires previous phosphorylation at Y15, and that the T14A mutant, unlike Y15F, is recessive to wild-type Cdc2 activity. Finally, the normal duration of G2 delay after irradiation or hydroxyurea treatment in a T14A mutant strain indicates that T14 phosphorylation is not required for the DNA damage or replication checkpoint controls.","authors":"Den Haese GJ, Walworth N, Carr AM, Gould KL","authors_abbrev":"Den Haese GJ et al.","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_session_key":"9a3197e7865f3d22","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-05-14 16:33:52","canto_approved_date":"2025-07-02 06:37:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-17 15:26:06","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":20,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC11B10.09","SPCC18B5.03","SPAC20G8.01","SPCC1259.13","SPBC660.14"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2021-05-14"},{"uniquename":"PMID:27368341","title":"A general method for rapid and cost-efficient large-scale production of 5' capped RNA.","citation":"RNA 2016 Sep;22(9):1454-66","abstract":"The eukaryotic mRNA 5' cap structure is indispensible for pre-mRNA processing, mRNA export, translation initiation, and mRNA stability. Despite this importance, structural and biophysical studies that involve capped RNA are challenging and rare due to the lack of a general method to prepare mRNA in sufficient quantities. Here, we show that the vaccinia capping enzyme can be used to produce capped RNA in the amounts that are required for large-scale structural studies. We have therefore designed an efficient expression and purification protocol for the vaccinia capping enzyme. Using this approach, the reaction scale can be increased in a cost-efficient manner, where the yields of the capped RNA solely depend on the amount of available uncapped RNA target. Using a large number of RNA substrates, we show that the efficiency of the capping reaction is largely independent of the sequence, length, and secondary structure of the RNA, which makes our approach generally applicable. We demonstrate that the capped RNA can be directly used for quantitative biophysical studies, including fluorescence anisotropy and high-resolution NMR spectroscopy. In combination with (13)C-methyl-labeled S-adenosyl methionine, the methyl groups in the RNA can be labeled for methyl TROSY NMR spectroscopy. Finally, we show that our approach can produce both cap-0 and cap-1 RNA in high amounts. In summary, we here introduce a general and straightforward method that opens new means for structural and functional studies of proteins and enzymes in complex with capped RNA.","doi":"10.1261/rna.056614.116","authors":"Fuchs AL, Neu A, Sprangers R","authors_abbrev":"Fuchs AL et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-07-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-09-08 00:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18418381","title":"Oxygen-regulated degradation of fission yeast SREBP by Ofd1, a prolyl hydroxylase family member.","citation":"EMBO J 2008 May 21;27(10):1491-501","abstract":"Sre1, the fission yeast sterol regulatory element binding protein, is an endoplasmic reticulum membrane-bound transcription factor that responds to changes in oxygen-dependent sterol synthesis as an indirect measure of oxygen availability. Under low oxygen, Sre1 is proteolytically cleaved and the released N-terminal transcription factor (Sre1N) activates gene expression essential for hypoxic growth. Here, we describe an oxygen-dependent mechanism for regulation of Sre1 that is independent of sterol-regulated proteolysis. Using yeast expressing only Sre1N, we show that Sre1N turnover is regulated by oxygen. Ofd1, an uncharacterized prolyl 4-hydroxylase-like 2-oxoglutarate-Fe(II) dioxygenase, accelerates Sre1N degradation in the presence of oxygen. However, unlike the prolyl 4-hydroxylases that regulate mammalian hypoxia-inducible factor, Ofd1 uses multiple domains to regulate Sre1N degradation by oxygen; the Ofd1 N-terminal dioxygenase domain is required for oxygen sensing and the Ofd1 C-terminal domain accelerates Sre1N degradation. Our data support a model whereby the Ofd1 N-terminal dioxygenase domain is an oxygen sensor that regulates the activity of the C-terminal degradation domain.","doi":"10.1038/emboj.2008.83","authors":"Hughes BT, Espenshade PJ","authors_abbrev":"Hughes BT et al.","pubmed_publication_date":"21 May 2008","pubmed_entrez_date":"2008-04-18","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP8A3.02c","SPBC6B1.08c","SPBC19C2.09"],"gene_count":3,"ltp_gene_count":1},{"uniquename":"EMBL:AB084835","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.23"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9828139","title":"RAD1, a human structural homolog of the Schizosaccharomyces pombe RAD1 cell cycle checkpoint gene.","citation":"Genomics 1998 Dec 01;54(2):344-7","abstract":"Cell cycle checkpoints are gating mechanisms that govern cell cycle progression in the presence of DNA damage and incomplete DNA replication. The Schizosaccharomyces pombe Rad1 protein is an essential component of cell cycle checkpoints activated by both types of genomic stress. In this study, we report the isolation of a human homolog of the S. pombe RAD1 gene. The hRAD1 protein is also similar to the Saccharomyces cerevisiae cell cycle checkpoint protein Rad17 and the Ustilago maydis 3' --> 5' exonuclease, Rec1. We show that human RAD1 partially complements the hydroxyurea and ionizing radiation hypersensitivities of a S. pombe rad1 mutant, suggesting phylogenetic conservation of the DNA damage and replication checkpoints. The human RAD1 locus was mapped to human chromosome 5p13.2, a locus frequently altered in non-small-cell lung cancer and bladder cancer.","authors":"Marathi UK, Dahlen M, Sunnerhagen P, Romero AV, Ramagli LS, Siciliano MJ, Li L, Legerski RJ","authors_abbrev":"Marathi UK et al.","pubmed_publication_date":"01 Dec 1998","pubmed_entrez_date":"1998-11-26","publication_year":"1998","canto_session_key":"e3826dfa18c1a8fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 17:15:06","canto_session_submitted_date":"2012-03-03 17:14:43","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:4062484","title":"Subcellular localization and glycoprotein nature of the invertase from the fission yeast Schizosaccharomyces pombe.","citation":"Arch Microbiol 1985 Sep;142(4):370-4","abstract":"The subcellular localization of the enzyme invertase in Schizosaccharomyces pombe cells, both repressed and derepressed for synthesis of the enzyme, was studied. Most of the invertase was found to be located outside the plasma membrane and only a small percentage was found to be associated to membranes. A substantial portion of the external enzyme remained firmly bound to cell-wall material. All of the invertase recovered in soluble form from cellular extracts reacted with concanavalin A and with the lectin from Bandeiraea simplicifolia seeds, indicating the presence in the enzyme of a carbohydrate moiety which probably contains terminal mannosyl (or structurally related) and galactosyl residues. The possibility of the presence of two different forms of invertase in S. pombe was considered. An intracellular, soluble form of invertase, devoid of carbohydrate, similar to the small invertase of the budding yeast Saccharomyces cerevisiae, was not found in S. pombe. However, the Michaelis constant for sucrose of the enzyme present in repressed cells was smaller than that of the invertase synthesized under derepressing conditions, although this difference could also be the result of a different pattern of glycosylation of the invertase synthesized under different growth conditions.","authors":"Moreno S, Ruíz T, Sánchez Y, Villanueva JR, Rodríguez L","authors_abbrev":"Moreno S et al.","pubmed_publication_date":"Sep 1985","pubmed_entrez_date":"1985-09-01","publication_year":"1985","canto_session_key":"30cfe6cb5fb477b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-03-04 16:10:30","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-27 09:25:50","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-02-27"},{"uniquename":"PMID:11252721","title":"Fission yeast Prp4p kinase regulates pre-mRNA splicing by phosphorylating a non-SR-splicing factor.","citation":"EMBO Rep 2001 Jan;2(1):35-41","abstract":"We provide evidence that Prp4p kinase activity is required for pre-mRNA splicing in vivo and show that loss of activity impairs G1-S and G2-M progression in the cell cycle. Prp4p interacts genetically with the non-SR (serine/arginine) splicing factors Prp1p and Prp5p. Bacterially produced Prp1p is phosphorylated by Prp4p in vitro. Prp4p and Prp1p also interact in the yeast two-hybrid system. In vivo labelling studies using a strain with a mutant allele of the prp4 gene in the genetic background indicate a change in phosphorylation of the Prp1p protein. These results are consistent with the notion that Prp4p kinase is involved in the control of the formation of active spliceosomes, targeting non-SR splicing factors.","authors":"Schwelnus W, Richert K, Opitz F, Gross T, Habara Y, Tani T, Käufer NF","authors_abbrev":"Schwelnus W et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-03-17","publication_year":"2001","canto_session_key":"bdeb75b22f017c39","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-08-10 15:42:52","canto_approved_date":"2023-12-30 10:36:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-25 14:06:34","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP22H7.07","SPBC146.07","SPCC777.14","SPAC2G11.14","SPBC6B1.07"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-08-10"},{"uniquename":"PMID:11080156","title":"The fission yeast gamma-tubulin complex is required in G(1) phase and is a component of the spindle assembly checkpoint.","citation":"EMBO J 2000 Nov 15;19(22):6098-111","abstract":"Microtubule polymerization is initiated from the microtubule organizing centre (MTOC), which contains the gamma-tubulin complex. We have identified fission yeast Alp4 and Alp6, which are homologues of the gamma-tubulin-interacting proteins Sc.Spc97/Hs.Gcp2 and Sc. Spc98/Hs.Gcp3, respectively. The size of the fission yeast gamma-tubulin complex is large (>2000 kDa), comparable to that in metazoans. Both Alp4 and Alp6 localize to the spindle pole body (SPB) and also to the equatorial MTOC. Temperature-sensitive (ts) alp4 and alp6 mutants show two types of microtubular defects. First, monopolar mitotic spindles form. Secondly, abnormally long cytoplasmic microtubules appear that do not stop at the cell tips and are still associated with the SPB. Alp4 function is required in G(1) phase and ts mutants become lethal before S-phase. alp4 and alp6 mutants are hypersensitive to the microtubule- destabilizing drug thiabendazole (TBZ) and show a lethal 'cut' phenotype in its presence. Furthermore, alp4mad2 double mutants show an exaggerated multiple septation phenotype in TBZ. These results indicate that Alp4 and Alp6 may play a crucial role in the spindle pole-mediated checkpoint pathway.","authors":"Vardy L, Toda T","authors_abbrev":"Vardy L et al.","pubmed_publication_date":"15 Nov 2000","pubmed_entrez_date":"2000-11-18","publication_year":"2000","canto_session_key":"fc488fcc50f328f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-05 15:05:03","canto_approved_date":"2026-01-29 17:09:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-23 12:38:18","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPBC428.20c","SPCC1223.06","SPBC365.15","SPBC32F12.04"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2016-10-05"},{"uniquename":"PMID:19503081","title":"'Injecting' yeast.","citation":"Nat Methods 2009 Jul;6(7):513-4","abstract":"Yeast is a powerful genetic model system, but its rigid cell wall has prohibited microinjection. Using microfabricated channels to constrain the fission yeast Schizosaccharomyces pombe, we sheared local regions of individual cells with a piezoelectric unit. The cells remained viable, we detected actin patches in the cell after introduction of fluorescent phalloidin into the medium, and the cytokinetic ring was disrupted after injection of the myosin II inhibitor blebbistatin.","doi":"10.1038/nmeth.1335","authors":"Riveline D, Nurse P","authors_abbrev":"Riveline D et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-06-09","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16251348","title":"The homologous putative GTPases Grn1p from fission yeast and the human GNL3L are required for growth and play a role in processing of nucleolar pre-rRNA.","citation":"Mol Biol Cell 2006 Jan;17(1):460-74","abstract":"Grn1p from fission yeast and GNL3L from human cells, two putative GTPases from the novel HSR1_MMR1 GTP-binding protein subfamily with circularly permuted G-motifs play a critical role in maintaining normal cell growth. Deletion of Grn1 resulted in a severe growth defect, a marked reduction in mature rRNA species with a concomitant accumulation of the 35S pre-rRNA transcript, and failure to export the ribosomal protein Rpl25a from the nucleolus. Deleting any of the Grn1p G-domain motifs resulted in a null phenotype and nuclear/nucleolar localization consistent with the lack of nucleolar export of preribosomes accompanied by a distortion of nucleolar structure. Heterologous expression of GNL3L in a Deltagrn1 mutant restored processing of 35S pre-rRNA, nuclear export of Rpl25a and cell growth to wild-type levels. Genetic complementation in yeast and siRNA knockdown in HeLa cells confirmed the homologous proteins Grn1p and GNL3L are required for growth. Failure of two similar HSR1_MMR1 putative nucleolar GTPases, Nucleostemin (NS), or the dose-dependent response of breast tumor autoantigen NGP-1, to rescue deltagrn1 implied the highly specific roles of Grn1p or GNL3L in nucleolar events. Our analysis uncovers an important role for Grn1p/GNL3L within this unique group of nucleolar GTPases.","authors":"Du X, Rao MR, Chen XQ, Wu W, Mahalingam S, Balasundaram D","authors_abbrev":"Du X et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2005-10-28","publication_year":"2006","canto_session_key":"bcaeb3349b4e8973","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-09-28 15:27:06","canto_approved_date":"2022-02-02 14:04:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-14 13:06:36","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.08c","SPBC106.18"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2017-09-28"},{"uniquename":"PMID:36006032","title":"Analysis of the potential role of fission yeast PP2A in spindle assembly checkpoint inactivation.","citation":"FASEB J 2022 Sep;36(9):e22524","abstract":"As a surveillance mechanism, the activated spindle assembly checkpoint (SAC) potently inhibits the E3 ubiquitin ligase APC/C (anaphase-promoting complex/cyclosome) to ensure accurate chromosome segregation. Although the protein phosphatase 2A (PP2A) has been proposed to be both, directly and indirectly, involved in spindle assembly checkpoint inactivation in mammalian cells, whether it is similarly operating in the fission yeast Schizosaccharomycer pombe has never been demonstrated. Here, we investigated whether fission yeast PP2A is involved in SAC silencing by following the rate of cyclin B (Cdc13) destruction at SPBs during the recovery phase in nda3-KM311 cells released from the inhibition of APC/C by the activated spindle checkpoint. The timing of the SAC inactivation is only slightly delayed when two B56 regulatory subunits (Par1 and Par2) of fission yeast PP2A are absent. Overproduction of individual PP2A subunits either globally in the nda3-KM311 arrest-and-release system or locally in the synthetic spindle checkpoint activation system only slightly suppresses the SAC silencing defects in PP1 deletion (dis2Δ) cells. Our study thus demonstrates that the fission yeast PP2A is not a key regulator actively involved in SAC inactivation.","doi":"10.1096/fj.202101884R","authors":"Deng DJ, Wang X, Yue KY, Wang Y, Jin QW","authors_abbrev":"Deng DJ et al.","pubmed_publication_date":"Sep 2022","pubmed_entrez_date":"2022-08-25","publication_year":"2022","canto_session_key":"9b42d44e8fba951f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xi Wang","canto_first_approved_date":"2023-03-08 10:14:53","canto_approved_date":"2023-10-07 17:50:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-01-12 03:10:27","canto_added_date":"2022-08-27 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Xi Wang","community_curator":true,"annotation_count":13,"orcid":"0000-0003-3894-5440","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.02c","SPAC6F12.12","SPAP8A3.09c","SPAC823.15","SPAC227.07c","SPAC22H10.04","SPCC188.02","SPBC16H5.07c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2023-03-08"},{"uniquename":"PMID:12175809","title":"Checking cell size in yeast.","citation":"Trends Genet 2002 Sep;18(9):479-85","abstract":"To remain viable, cells have to coordinate cell growth with cell division. In yeast, this occurs at two control points: the boundaries between G1 and S phases, also known as Start, and between G2 and M phases. Theoretically, coordination can be achieved by independent regulation of growth and division, or by participation of surveillance mechanisms in which cell size feeds back into cell-cycle control. This article discusses recent advances in the identification of sizing mechanisms in budding and in fission yeast, and how these mechanisms integrate with environmental stimuli. A comparison of the G1-S and G2-M size-control modules in the two species reveals a degree of conservation higher than previously thought. This reinforces the notion that internal sizing could be a conserved feature of cell-cycle control throughout eukaryotes.","authors":"Rupes I","authors_abbrev":"Rupes I","pubmed_publication_date":"Sep 2002","pubmed_entrez_date":"2002-08-15","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPAB1023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40982005","title":"E2 ubiquitin-conjugating enzyme Ubc11 regulates Rst2 protein stability in the fission yeast Schizosaccharomyces pombe.","citation":"Arch Microbiol 2025 Sep 22;207(11):275","abstract":"In Schizosaccharomyces pombe, many transcription factors, including Rst2, remain poorly understood. Rst2 functions downstream of the cAMP-PKA pathway, but its protein stability and potential degradation via the ubiquitin-proteasome system, are not well characterized. This study investigates the -regulation of Rst2 in S. pombe, focusing on expression and degradation via the ubiquitin-proteasome system and E2 enzymes. Protein expression and stability were analyzed by western blotting to assess the impact of E2 mutations on Rst2 regulation. Rst2 transcription remained low at early time points but increased over fourfold by 24 h, remaining elevated through 48 h. Protein stability assays showed rapid Rst2 degradation under cycloheximide (CHX) treatment, while CHX and bortezomib (BZ) treatment preserved Rst2 protein levels, indicating the proteasome-dependent degradation of Rst2. To determine which E2 enzyme(s) are invovled in Rst2 degradation, we individually deleted all non-essential E2 genes and generated two point mutants ubc4-P61S and ubc11-P93L mutant and found that Rst2 is stabilized only in ubc11-P93L. This study shows the role of the ubiquitin-proteasome system and E2 enzyme Ubc11 in regulating Rst2 in S. pombe.","doi":"10.1007/s00203-025-04485-y","authors":"Huang Y, Nawaz Y","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"22 Sep 2025","pubmed_entrez_date":"2025-09-22","publication_year":"2025","canto_session_key":"7bd8205f54002a79","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-22 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.15c","SPAC6F12.02"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:17043360","title":"Interactions between the RNA interference effector protein Ago1 and 14-3-3 proteins: consequences for cell cycle progression.","citation":"J Biol Chem 2006 Dec 08;281(49):37646-51","abstract":"The Argonaute family member Ago1 is required for formation of pericentric heterochromatin and small interfering RNA (siRNA)-mediated post-transcriptional gene silencing in the fission yeast Schizosaccharomyces pombe. In addition, we have recently demonstrated that Ago1 function is required for enactment of cell cycle checkpoints (Carmichael, J. B., Provost, P., Ekwall, K., and Hobman, T. C. (2004) Mol. Biol. Cell 15, 1425-1435). Here, we provide evidence that the amino terminus of Ago1 binds to proteins that function in cell cycle regulation including 14-3-3 proteins. Interestingly, the amino terminus of human Ago2, the endonuclease that cleaves siRNA-targeted mRNAs, was also demonstrated to bind 14-3-3 proteins. Overexpression of the Ago1 amino terminus in yeast resulted in cell cycle delay at the G(2)/M boundary. Further investigation revealed that nuclear import of the mitosis-inducing phosphatase Cdc25 is inhibited by overexpression of the Ago1 amino terminus. Under these conditions, we found that the cyclin-dependent kinase Cdc2 is constitutively phosphorylated on tyrosine 15, thereby reducing the activity of this kinase, a situation that delays entry into mitosis. We hypothesize that 14-3-3 proteins are required for Argonaute protein functions in cell cycle and/or gene-silencing pathways.","authors":"Stoica C, Carmichael JB, Parker H, Pare J, Hobman TC","authors_abbrev":"Stoica C et al.","pubmed_publication_date":"08 Dec 2006","pubmed_entrez_date":"2006-10-18","publication_year":"2006","canto_session_key":"0c47374a70735395","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-06-05 13:11:18","canto_approved_date":"2024-06-05 13:11:18","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-06-05 13:11:11","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":6,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPAC17A2.13c","SPCC736.11","SPAC24H6.05","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2024-06-05"},{"uniquename":"PMID:10733588","title":"Fission yeast homologs of human CENP-B have redundant functions affecting cell growth and chromosome segregation.","citation":"Mol Cell Biol 2000 Apr;20(8):2852-64","abstract":"Two functionally important DNA sequence elements in centromeres of the fission yeast Schizosaccharomyces pombe are the centromeric central core and the K-type repeat. Both of these DNA elements show internal functional redundancy that is not correlated with a conserved DNA sequence. Specific, but degenerate, sequences in these elements are bound in vitro by the S. pombe DNA-binding proteins Abp1p (also called Cbp1p) and Cbhp, which are related to the mammalian centromere DNA-binding protein CENP-B. In this study, we determined that Abp1p binds to at least one of its target sequences within S. pombe centromere II central core (cc2) DNA with an affinity (K(s) = 7 x 10(9) M(-1)) higher than those of other known centromere DNA-binding proteins for their cognate targets. In vivo, epitope-tagged Cbhp associated with centromeric K repeat chromatin, as well as with noncentromeric regions. Like abp1(+)/cbp1(+), we found that cbh(+) is not essential in fission yeast, but a strain carrying deletions of both genes (Deltaabp1 Deltacbh) is extremely compromised in growth rate and morphology and missegregates chromosomes at very high frequency. The synergism between the two null mutations suggests that these proteins perform redundant functions in S. pombe chromosome segregation. In vitro assays with cell extracts with these proteins depleted allowed the specific assignments of several binding sites for them within cc2 and the K-type repeat. Redundancy observed at the centromere DNA level appears to be reflected at the protein level, as no single member of the CENP-B-related protein family is essential for proper chromosome segregation in fission yeast. The relevance of these findings to mammalian centromeres is discussed.","authors":"Baum M, Clarke L","authors_abbrev":"Baum M et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-03-25","publication_year":"2000","canto_session_key":"b1f93197a5f7b23e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-03 13:15:15","canto_approved_date":"2021-09-07 14:54:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-03 08:54:13","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.04c","SPAC9E9.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-01-03"},{"uniquename":"PMID:11406279","title":"Isolation and characterization of the Schizosaccharomyces pombe cDNA encoding the mitochondrial endonuclease(1).","citation":"Biochim Biophys Acta 2001 May 28;1519(1-2):111-6","abstract":"We isolated the cDNA of the fission yeast mitochondrial endonuclease SpNUC1, which consists of 322 amino acids and has a significant homology with the budding yeast NUC1 and mammalian endonuclease G. Comparison of the cDNA sequence with the genomic sequence showed that the gene consists of three exons and two introns and spans 1.31 kb. The enzyme localization in mitochondria was demonstrated by expressing the SpNUC1-green fluorescent protein fusion in the yeast. The endonuclease was activated by truncation of the amino-terminal region of the protein, indicating that the enzyme is encoded as an inactive precursor. The active enzyme degraded single-stranded DNA and RNA, the activity being dependent on Mg(2+) (Mn(2+)).","authors":"Ikeda S, Kawasaki N","authors_abbrev":"Ikeda S et al.","pubmed_publication_date":"28 May 2001","pubmed_entrez_date":"2001-06-19","publication_year":"2001","canto_session_key":"6245444c45856292","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-08-04 21:55:39","canto_approved_date":"2025-06-26 08:29:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 20:41:02","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"EMBL:SPC11163","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.100"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU010138","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20885950","title":"Characterisation of the SUMO-like domains of Schizosaccharomyces pombe Rad60.","citation":"PLoS One 2010 Sep 27;5(9):e13009","abstract":"The S. pombe Rad60 protein is required for the repair of DNA double strand breaks, recovery from replication arrest, and is essential for cell viability. It has two SUMO-like domains (SLDs) at its C-terminus, an SXS motif and three sequences that have been proposed to be SUMO-binding motifs (SBMs). SMB1 is located in the middle of the protein, SBM2 is in SLD1 and SBM3 is at the C-terminus of SLD2. We have probed the functions of the two SUMO-like domains, SLD1 and SLD2, and the putative SBMs. SLD1 is essential for viability, while SLD2 is not. rad60-SLD2Δ cells are sensitive to DNA damaging agents and hydroxyurea. Neither ubiquitin nor SUMO can replace SLD1 or SLD2. Cells in which either SBM1 or SBM2 has been mutated are viable and are wild type for response to MMS and HU. In contrast mutation of SBM3 results in significant sensitivity to MMS and HU. These results indicate that the lethality resulting from deletion of SLD1 is not due to loss of SBM2, but that mutation of SBM3 produces a more severe phenotype than does deletion of SLD2. Using chemical denaturation studies, FPLC and dynamic light scattering we show this is likely due to the destabilisation of SLD2. Thus we propose that the region corresponding to the putative SBM3 forms part of the hydrophobic core of SLD2 and is not a SUMO-interacting motif. Over-expression of Hus5, which is the SUMO conjugating enzyme and known to interact with Rad60, does not rescue rad60-SLD2Δ, implying that as well as having a role in the sumoylation process as previously described, Rad60 has a Hus5-independent function.","doi":"10.1371/journal.pone.0013009","authors":"Boyd LK, Mercer B, Thompson D, Main E, Watts FZ","authors_abbrev":"Boyd LK et al.","pubmed_publication_date":"27 Sep 2010","pubmed_entrez_date":"2010-10-02","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1921.02","SPCC5E4.06"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:24574118","title":"Canto: an online tool for community literature curation.","citation":"Bioinformatics 2014 Jun 15;30(12):1791-2","abstract":"Detailed curation of published molecular data is essential for any model organism database. Community curation enables researchers to contribute data from their papers directly to databases, supplementing the activity of professional curators and improving coverage of a growing body of literature. We have developed Canto, a web-based tool that provides an intuitive curation interface for both curators and researchers, to support community curation in the fission yeast database, PomBase. Canto supports curation using OBO ontologies, and can be easily configured for use with any species.\nCanto code and documentation are available under an Open Source license from http://curation.pombase.org/. Canto is a component of the Generic Model Organism Database (GMOD) project (http://www.gmod.org/).","doi":"10.1093/bioinformatics/btu103","authors":"Rutherford KM, Harris MA, Lock A, Oliver SG, Wood V","authors_abbrev":"Rutherford KM et al.","pubmed_publication_date":"15 Jun 2014","pubmed_entrez_date":"2014-02-28","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2834100","title":"Cloning and expression of the OMP decarboxylase gene URA4 from Schizosaccharomyces pombe.","citation":"Curr Genet 1987;12(7):527-34","abstract":"URA4, the gene coding for orotidine monophosphate decarboxylase (OMPdecase), has been cloned from the fission yeast by homologous complementation and restricted in an Escherichia coli-Schizosaccharomyces pombe (E. coli-S. pombe) replicative plasmid to a 1.76 kb HindIII fragment. This plasmid is maintained at a high copy number in S. pombe and allows OMPdecase expression in Saccharomyces cerevisiae (S. cerevisiae) as well as in E. coli. After characterisation by restriction mapping and Southern hybridisation, the cloned gene was used as a probe to measure URA4 transcription and to examine its regulation. Messenger RNA levels were measured by DNA/RNA filter-hybridisation with pulse labelled RNAs during 6-azauridine (6-AUR) inhibited growth in wild type and 6-AUR sensitive strains. We found that in S. pombe the OMP analogue 6-AUR does not regulate the level of OMPdecase formation as it does in S. cerevisiae but rather modifies the ratio of total polyA+ to polyA- RNAs in the cell. Based on these results and on corresponding enzyme activities this study demonstrates divergent pyrimidine pathway regulation in the two yeasts S. cerevisiae and S. pombe. Finally, we propose the use of the URA4 gene as a convenient selective marker for genetic engineering in S. pombe.","authors":"Bach ML","authors_abbrev":"Bach ML","pubmed_publication_date":"1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_session_key":"ddea10281db0aed1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:43:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 21:14:14","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC330.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-25"},{"uniquename":"PMID:31197198","title":"Rif1 promotes association of G-quadruplex (G4) by its specific G4 binding and oligomerization activities.","citation":"Sci Rep 2019 Jun 13;9(1):8618","abstract":"Rif1 is a conserved protein regulating replication timing and binds preferentially to the vicinity of late-firing/dormant origins in fission yeast. The Rif1 binding sites on the fission yeast genome have an intrinsic potential to generate G-quadruplex (G4) structures to which purified Rif1 preferentially binds. We previously proposed that Rif1 generates chromatin architecture that may determine replication timing by facilitating the chromatin loop formation. Here, we conducted detailed biochemical analyses on Rif1 and its G4 binding. Rif1 prefers sequences containing long stretches of guanines and binds preferentially to the multimeric G4 of parallel or hybrid/mix topology. Rif1 forms oligomers and binds simultaneously to multiple G4. We present a model on how Rif1 may facilitate the formation of chromatin architecture through its G4 binding and oligomerization properties.","doi":"10.1038/s41598-019-44736-9","authors":"Masai H, Fukatsu R, Kakusho N, Kanoh Y, Moriyama K, Ma Y, Iida K, Nagasawa K","authors_abbrev":"Masai H et al.","pubmed_publication_date":"13 Jun 2019","pubmed_entrez_date":"2019-06-15","publication_year":"2019","canto_session_key":"c4da22bf45ff8c05","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-06-16 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34464389","title":"R-loops and regulatory changes in chronologically ageing fission yeast cells drive non-random patterns of genome rearrangements.","citation":"PLoS Genet 2021 Aug;17(8):e1009784","abstract":"Aberrant repair of DNA double-strand breaks can recombine distant chromosomal breakpoints. Chromosomal rearrangements compromise genome function and are a hallmark of ageing. Rearrangements are challenging to detect in non-dividing cell populations, because they reflect individually rare, heterogeneous events. The genomic distribution of de novo rearrangements in non-dividing cells, and their dynamics during ageing, remain therefore poorly characterized. Studies of genomic instability during ageing have focussed on mitochondrial DNA, small genetic variants, or proliferating cells. To characterize genome rearrangements during cellular ageing in non-dividing cells, we interrogated a single diagnostic measure, DNA breakpoint junctions, using Schizosaccharomyces pombe as a model system. Aberrant DNA junctions that accumulated with age were associated with microhomology sequences and R-loops. Global hotspots for age-associated breakpoint formation were evident near telomeric genes and linked to remote breakpoints elsewhere in the genome, including the mitochondrial chromosome. Formation of breakpoint junctions at global hotspots was inhibited by the Sir2 histone deacetylase and might be triggered by an age-dependent de-repression of chromatin silencing. An unexpected mechanism of genomic instability may cause more local hotspots: age-associated reduction in an RNA-binding protein triggering R-loops at target loci. This result suggests that biological processes other than transcription or replication can drive genome rearrangements. Notably, we detected similar signatures of genome rearrangements that accumulated in old brain cells of humans. These findings provide insights into the unique patterns and possible mechanisms of genome rearrangements in non-dividing cells, which can be promoted by ageing-related changes in gene-regulatory proteins.","doi":"10.1371/journal.pgen.1009784","authors":"Ellis DA, Reyes-Martín F, Rodríguez-López M, Cotobal C, Sun XM, Saintain Q, Jeffares DC, Marguerat S, Tallada VA, Bähler J","authors_abbrev":"Ellis DA et al.","pubmed_publication_date":"Aug 2021","pubmed_entrez_date":"2021-08-31","publication_year":"2021","canto_session_key":"ed99f40936cc1718","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jurg Bahler","canto_first_approved_date":"2022-01-29 20:48:19","canto_approved_date":"2022-02-01 08:24:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-08 17:39:48","canto_added_date":"2021-09-02 00:15:06","annotation_curators":[{"name":"Jurg Bahler","community_curator":true,"annotation_count":8,"orcid":"0000-0003-4036-1532","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBCPT2R1.08c","SPAC4G9.02","SPBC16D10.07c","SPBC336.06c","SPCC16C4.07"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2022-01-29"},{"uniquename":"PMID:15238514","title":"Conserved and nonconserved proteins for meiotic DNA breakage and repair in yeasts.","citation":"Genetics 2004 Jun;167(2):593-605","abstract":"During meiosis DNA double-strand breaks initiate recombination in the distantly related budding and fission yeasts and perhaps in most eukaryotes. Repair of broken meiotic DNA is essential for formation of viable gametes. We report here distinct but overlapping sets of proteins in these yeasts required for formation and repair of double-strand breaks. Meiotic DNA breakage in Schizosaccharomyces pombe did not require Rad50 or Rad32, although the homologs Rad50 and Mre11 are required in Saccharomyces cerevisiae; these proteins are required for meiotic DNA break repair in both yeasts. DNA breakage required the S. pombe midmeiosis transcription factor Mei4, but the structurally unrelated midmeiosis transcription factor Ndt80 is not required for breakage in S. cerevisiae. Rhp51, Swi5, and Rad22 + Rti1 were required for full levels of DNA repair in S. pombe, as are the related S. cerevisiae proteins Rad51, Sae3, and Rad52. Dmc1 was not required for repair in S. pombe, but its homolog Dmc1 is required in the well-studied strain SK1 of S. cerevisiae. Additional proteins required in one yeast have no obvious homologs in the other yeast. The occurrence of conserved and nonconserved proteins indicates potential diversity in the mechanism of meiotic recombination and divergence of the machinery during the evolution of eukaryotes.","authors":"Young JA, Hyppa RW, Smith GR","authors_abbrev":"Young JA et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-07-09","publication_year":"2004","canto_session_key":"ce88fdccd4b3e0b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-17 18:15:52","canto_approved_date":"2021-10-14 11:00:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-17 18:15:44","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPAC644.14c","SPBC119.14","SPAC1556.01c","SPBC21B10.12","SPAC30D11.10","SPAC8E11.03c","SPBC32H8.11","SPBC409.03","SPAC17A5.11","SPAC13C5.07","SPCC4G3.05c"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2015-12-17"},{"uniquename":"PMID:7903653","title":"Enzyme defects in glutamate-requiring strains of Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 1993 Nov 01;113(3):267-72","abstract":"Among the glutamate-requiring strains of Schizosaccharomyces pombe previously described [1], glu2 and glu3 strains were both shown to lack NAD-specific isocitrate dehydrogenase. glu4 strains were shown to lack glutamine:2-oxoglutarate aminotransferase (GOGAT), and to be defective in ammonia assimilation. The regulation of GOGAT activity in wild-type cells was investigated and was consistent with GOGAT and glutamine synthetase being involved in ammonium assimilation, particularly under conditions of nitrogen limitation.","authors":"Barel I, MacDonald DW","authors_abbrev":"Barel I et al.","pubmed_publication_date":"01 Nov 1993","pubmed_entrez_date":"1993-11-01","publication_year":"1993","canto_session_key":"600ec028617b4964","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-19 09:06:41","canto_approved_date":"2025-12-23 12:40:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-19 09:06:36","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11G7.03","SPAPB1E7.07","SPBC902.05c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2022-09-19"},{"uniquename":"EMBL:AU012254","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9203579","title":"The Spg1p GTPase is an essential, dosage-dependent inducer of septum formation in Schizosaccharomyces pombe.","citation":"Genes Dev 1997 Jun 15;11(12):1519-34","abstract":"The spg1 gene (septum-promoting GTPase) was cloned as a multicopy suppressor of a dominant-negative mutant of the Cdc7p kinase. It encodes a small GTPase of the Ras superfamily. spg1 is an essential gene. Null or heat-sensitive alleles do not make a division septum, but growth, S-phase, and mitosis continue in the absence of cell division, producing elongated, multinucleate cells. Increased expression of Spg1p induces septum formation in G2, S-phase, and pre-Start G1-arrested cells. This requires the activity of Cdc7p kinase, but not p34(cdc2). Increased expression of Cdc7p bypasses the requirement for Spg1p. Spg1p and Cdc7p can be coimmunoprecipitated from cell extracts, and interact in the two-hybrid system. These data indicate that Spg1p is a key element in controlling the onset of septum formation in Schizosaccharomyces pombe, and that it acts through the Cdc7p kinase.","authors":"Schmidt S, Sohrmann M, Hofmann K, Woollard A, Simanis V","authors_abbrev":"Schmidt S et al.","pubmed_publication_date":"15 Jun 1997","pubmed_entrez_date":"1997-06-15","publication_year":"1997","canto_session_key":"583bc6e2762656b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-04 21:51:56","canto_approved_date":"2026-01-31 13:58:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-04-30 12:56:09","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPBC24C6.07","SPBC11B10.09","SPCC1739.11c","SPBC336.12c","SPBC21.06c","SPAC1565.06c","SPAC20G8.05c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2019-01-04"},{"uniquename":"PMID:37330173","title":"Phosphoregulation of DNA repair via the Rad51 auxiliary factor Swi5-Sfr1.","citation":"J Biol Chem 2023 Aug;299(8):104929","abstract":"Homologous recombination (HR) is a major pathway for the repair of DNA double-strand breaks, the most severe form of DNA damage. The Rad51 protein is central to HR, but multiple auxiliary factors regulate its activity. The heterodimeric Swi5-Sfr1 complex is one such factor. It was previously shown that two sites within the intrinsically disordered domain of Sfr1 are critical for the interaction with Rad51. Here, we show that phosphorylation of five residues within this domain regulates the interaction of Swi5-Sfr1 with Rad51. Biochemical reconstitutions demonstrated that a phosphomimetic mutant version of Swi5-Sfr1 is defective in both the physical and functional interaction with Rad51. This translated to a defect in DNA repair, with the phosphomimetic mutant yeast strain phenocopying a previously established interaction mutant. Interestingly, a strain in which Sfr1 phosphorylation was blocked also displayed sensitivity to DNA damage. Taken together, we propose that controlled phosphorylation of Sfr1 is important for the role of Swi5-Sfr1 in promoting Rad51-dependent DNA repair.","doi":"10.1016/j.jbc.2023.104929","authors":"Liang P, Lister K, Yates L, Argunhan B, Zhang X","authors_abbrev":"Liang P et al.","pubmed_publication_date":"Aug 2023","pubmed_entrez_date":"2023-06-17","publication_year":"2023","canto_session_key":"e8f05dfe37bfb540","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-09-13 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20H4.07","SPAC644.14c","SPAC3C7.03c","SPBC28F2.07","SPBC409.03"],"gene_count":5,"ltp_gene_count":0},{"uniquename":"EMBL:SPC03287","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21449051","title":"Schizosaccharomyces pombe Arc3 is a conserved subunit of the Arp2/3 complex required for polarity, actin organization, and endocytosis.","citation":"Yeast 2011 Jun;28(6):495-503","abstract":"We characterized the Schizosaccharomyces pombe arc3 gene, whose product shares sequence homology with that of the budding yeast ARC18 and human ARPC3/p21 subunits of the Arp2/3 complex. Our data showed that Arc3p co-localizes with F-actin patches at the cell ends, but not with F-actin cables or the equatorial actin ring, and binds other subunits of the Arp2/3 complex. Gene deletion analysis showed that arc3 is essential for viability. When arc3 expression was repressed, F-actin patches became dispersed throughout the cell with greatly reduced mobility. Furthermore, in arc3-repressed cells, endocytosis was also inhibited. Human ARPC3 rescued the viability of the Sz. pombe arc3 null mutant; in addition, ARPC3 also localized to F-actin patches in human cells. These data suggest that Arc3p is an evolutionarily conserved subunit of the Arp2/3 complex required for proper F-actin organization and efficient endocytosis.","doi":"10.1002/yea.1853","authors":"Cabrera R, Suo J, Young E, Chang EC","authors_abbrev":"Cabrera R et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-03-31","publication_year":"2011","canto_session_key":"85853385252614cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-20 16:20:27","canto_approved_date":"2025-12-19 10:42:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-16 22:02:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.03","SPAC6G9.07c","SPBC1778.08c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-02-20"},{"uniquename":"PMID:1849107","title":"Glucose repression of transcription of the Schizosaccharomyces pombe fbp1 gene occurs by a cAMP signaling pathway.","citation":"Genes Dev 1991 Apr;5(4):561-71","abstract":"Transcription of the fbp1 gene, encoding fructose-1,6-bisphosphatase, of Schizosaccharomyces pombe is subject to glucose repression. Previous work has demonstrated that several genes (git genes) are required for this repression. In this report we demonstrate that one of these genes, git2, is the same as the cyr1 gene, which encodes adenylate cyclase, and that loss-of-function mutations in git2 cause constitutive fbp1 transcription. Addition of cAMP to the growth medium suppresses the transcriptional defect in git2 mutants as well as in strains that carry mutations in any of six additional git genes. Similarly, exogenous cAMP represses fbp1 transcription in wild-type cells grown on a derepressing carbon source. Different levels of adenylate cyclase activity in different git2 mutants, coupled with the result that some git2 mutants display intragenic complementation, strongly suggest that adenylate cyclase acts as a multimer and that different git2 mutations alter distinct activities of adenylate cyclase, including catalytic activity and response to glucose. Additional experiments demonstrate that this cAMP signaling pathway is independent of the S. pombe ras1 gene and works by activation of cAMP-dependent protein kinase.","authors":"Hoffman CS, Winston F","authors_abbrev":"Hoffman CS et al.","pubmed_publication_date":"Apr 1991","pubmed_entrez_date":"1991-04-01","publication_year":"1991","canto_session_key":"39e9205957ce5637","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-18 15:46:57","canto_approved_date":"2025-12-23 12:54:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-29 18:03:03","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":40,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.07","SPBC21C3.20c","SPAC926.04c","SPAC8C9.03","SPAC23H3.13c","SPBC36.12c","SPAC17H9.09c","SPCC1753.02c","SPBC19C7.03","SPBC1198.14c","SPBC106.10"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2018-04-18"},{"uniquename":"PMID:22825872","title":"Mph1 kinetochore localization is crucial and upstream in the hierarchy of spindle assembly checkpoint protein recruitment to kinetochores.","citation":"J Cell Sci 2012 Oct 15;125(Pt 20):4720-7","abstract":"The spindle assembly checkpoint (SAC) blocks entry into anaphase until all chromosomes have stably attached to the mitotic spindle through their kinetochores. The checkpoint signal originates from unattached kinetochores, where there is an enrichment of SAC proteins. Whether the enrichment of all SAC proteins is crucial for SAC signaling is unclear. Here, we provide evidence that, in fission yeast, recruitment of the kinase Mph1 is of vital importance for a stable SAC arrest. An Mph1 mutant that eliminates kinetochore enrichment abolishes SAC signaling, whereas forced recruitment of this mutant to kinetochores restores SAC signaling. In bub3Δ cells, the SAC is functional when only Mph1 and the Aurora kinase Ark1, but no other SAC proteins, are enriched at kinetochores. We analyzed the network of dependencies for SAC protein localization to kinetochores and identify a three-layered hierarchy with Ark1 and Mph1 on top, Bub1 and Bub3 in the middle, and Mad3 as well as the Mad1-Mad2 complex at the lower end of the hierarchy. If Mph1 is artificially recruited to kinetochores, Ark1 becomes dispensable for SAC activity. Our results highlight the crucial role of Mph1 at kinetochores and suggest that the Mad1-Mad2 complex does not necessarily need to be enriched at kinetochores for functional SAC signaling.","doi":"10.1242/jcs.110387","authors":"Heinrich S, Windecker H, Hustedt N, Hauf S","authors_abbrev":"Heinrich S et al.","pubmed_publication_date":"15 Oct 2012","pubmed_entrez_date":"2012-07-25","publication_year":"2012","canto_session_key":"7341b39d1e6a56ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silke Hauf","canto_first_approved_date":"2020-06-05 09:39:53","canto_approved_date":"2025-12-23 12:28:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-01 14:38:08","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Silke Hauf","community_curator":true,"annotation_count":25,"orcid":"0000-0001-5938-721X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.01c","SPBC8D2.04","SPAC23H3.08c","SPCC1322.12c","SPAC1834.04","SPCC320.13c","SPBC106.01","SPBC3D6.04c","SPBC20F10.06","SPBC1105.11c"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2020-06-05"},{"uniquename":"PMID:10512870","title":"A double-strand break repair component is essential for S phase completion in fission yeast cell cycling.","citation":"Mol Biol Cell 1999 Oct;10(10):3331-43","abstract":"Fission yeast rad22(+), a homologue of budding yeast RAD52, encodes a double-strand break repair component, which is dispensable for proliferation. We, however, have recently obtained a cell division cycle mutant with a temperature-sensitive allele of rad22(+), designated rad22-H6, which resulted from a point mutation in the conserved coding sequence leading to one amino acid alteration. We have subsequently isolated rad22(+) and its novel homologue rti1(+) as multicopy suppressors of this mutant. rti1(+) suppresses all the defects of cells lacking rad22(+). Mating type switch-inactive heterothallic cells lacking either rad22(+) or rti1(+) are viable, but those lacking both genes are inviable and arrest proliferation with a cell division cycle phenotype. At the nonpermissive temperature, a synchronous culture of rad22-H6 cells performs DNA synthesis without delay and arrests with chromosomes seemingly intact and replication completed and with a high level of tyrosine-phosphorylated Cdc2. However, rad22-H6 cells show a typical S phase arrest phenotype if combined with the rad1-1 checkpoint mutation. rad22(+) genetically interacts with rad11(+), which encodes the large subunit of replication protein A. Deletion of rad22(+)/rti1(+) or the presence of rad22-H6 mutation decreases the restriction temperature of rad11-A1 cells by 4-6 degrees C and leads to cell cycle arrest with chromosomes incompletely replicated. Thus, in fission yeast a double-strand break repair component is required for a certain step of chromosome replication unlinked to repair, partly via interacting with replication protein A.","authors":"Suto K, Nagata A, Murakami H, Okayama H","authors_abbrev":"Suto K et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-10-08","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPBC660.13c","SPBC119.14"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10423510","title":"[The future of antifungal agents. Non azole antifungal agents].","citation":"Nihon Ishinkin Gakkai Zasshi 1999;40(3):157-61","abstract":"We investigated the efficacy of non-azole antifungal agents. Long circulating immunoliposomal amphotericin B was potent in murine invasive pulmonary aspergillosis. The concentration of AMPH-B was still high in the lung after 6 hours of 34A-PEG-liposomal AMPH-B. Lipid nanosphere amphotericin B (NS-718) showed efficacy against pulmonary aspergillosis in rats and pulmonary cryptococcosis in mice. The renal toxicity of NS-718 was estimated to be lower than that of AMPH-B from the results of the toxicity study in the rat infusion model. FK 463, a novel (1,3)-beta-D-glucan synthase inhibitor, showed efficacy against azole-resistant Candida albicans in murine experimental disseminated candidiasis. FK463 could be a promising drug and the therapy of choice for azole resistant C. albicans infection.","authors":"Maesaki S, Hossain MA, Sasaki E, Hashiguchi K, Higashiyama Y, Yoshitsugu Y, Tomono K, Tashiro T, Kohno S","authors_abbrev":"Maesaki S et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-07-29","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39199403","title":"Creating Meiotic Recombination-Regulating DNA Sites by  SpEDIT  in Fission Yeast Reveals Inefficiencies, Target-Site Duplications, and Ectopic Insertions.","citation":"Biomolecules 2024 Aug 16;14(8)","abstract":"Recombination hotspot-activating DNA sites (e.g.,  M26 ,  CCAAT ,  Oligo-C ) and their binding proteins (e.g., Atf1-Pcr1 heterodimer; Php2-Php3-Php5 complex, Rst2, Prdm9) regulate the distribution of Spo11 (Rec12)-initiated meiotic recombination. We sought to create 14 different candidate regulatory DNA sites via bp substitutions in the  ade6  gene of  Schizosaccharomyces pombe . We used a fission yeast-optimized CRISPR-Cas9 system ( SpEDIT ) and 196 bp-long dsDNA templates with centrally located bp substitutions designed to ablate the genomic PAM site, create specific 15 bp-long DNA sequences, and introduce a stop codon. After co-transformation with a plasmid that encoded both the guide RNA and Cas9 enzyme, about one-third of colonies had a phenotype diagnostic for DNA sequence changes at  ade6 . PCR diagnostics and DNA sequencing revealed a diverse collection of alterations at the target locus, including: (A) complete or (B) partial template-directed substitutions; (C) non-homologous end joinings; (D) duplications; (E) bp mutations, and (F) insertions of ectopic DNA. We concluded that  SpEDIT  can be used successfully to generate a diverse collection of DNA sequence elements within a reporter gene of interest. However, its utility is complicated by low efficiency, incomplete template-directed repair events, and undesired alterations to the target locus.","doi":"10.3390/biom14081016","authors":"Protacio RU, Dixon S, Davidson MK, Wahls WP","authors_abbrev":"Protacio RU et al.","pubmed_publication_date":"16 Aug 2024","pubmed_entrez_date":"2024-08-29","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-08-31 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11292845","title":"Gain- and loss-of-function of Rhp51, a Rad51 homolog in fission yeast, reveals dissimilarities in chromosome integrity.","citation":"Nucleic Acids Res 2001 Apr 15;29(8):1724-32","abstract":"Rad51 is crucial not only in homologous recombination and recombinational repair but also in normal cellular growth. To address the role of Rad51 in normal cell growth we investigated morphological changes of cells after overexpression of wild-type and a dominant negative form of Rad51 in fission yeast. Rhp51, a Rad51 homolog in Schizosaccharomyces pombe, has a highly conserved ATP-binding motif. Rhp51 K155A, which has a single substitution in this motif, failed to rescue hypersensitivity of a rhp51 mutant to methyl methanesulfonate (MMS) and UV, whereas it binds normally to Rhp51 and Rad22, a Rad52 homolog. Two distinct cellular phenotypes were observed when Rhp51 or Rhp51 K155A was overexpressed in normal cells. Overexpression of Rhp51 caused lethality in the absence of DNA-damaging agents, with acquisition of a cell cycle mutant phenotype and accumulation of a 1C DNA population. On the other hand, overexpression of Rhp51 K155A led to a delay in G(2) with decondensed nuclei, which resembled the phenotype of rhp51. The latter also exhibited MMS and UV sensitivity, indicating that Rhp51 K155A has a dominant negative effect. These results suggest an association between DNA replication and Rad51 function.","authors":"Kim WJ, Lee H, Park EJ, Park JK, Park SD","authors_abbrev":"Kim WJ et al.","pubmed_publication_date":"15 Apr 2001","pubmed_entrez_date":"2001-04-09","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPAC644.14c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:22900017","title":"The fission yeast GATA factor, Gaf1, modulates sexual development via direct down-regulation of ste11+ expression in response to nitrogen starvation.","citation":"PLoS One 2012;7(8):e42409","abstract":"Gaf1 is the first GATA family zinc-finger transcription factor identified in Schizosaccharomyces pombe. Here, we report that Gaf1 functions as a negatively acting transcription factor of ste11(+), delaying the entrance of cells exposed to transient nitrogen starvation into the meiotic cycle. gaf1Δ strains exhibited accelerated G(1)-arrest upon nitrogen starvation. Moreover, gaf1Δ mutation caused increased mating and sporulation frequency under both nitrogen-starved and unstarved conditions, while overexpression of gaf1(+) led to a significant impairment of sporulation. By microarray analysis, we found that approximately 63% (116 genes) of the 183 genes up-regulated in unstarved gaf1Δ cells were nitrogen starvation-responsive genes, and furthermore that 25 genes among the genes up-regulated by gaf1Δ mutation are Ste11 targets (e.g., gpa1(+), ste4(+), spk1(+), ste11(+), and mei2(+)). The phenotype caused by gaf1Δ mutation was masked by ste11Δ mutation, indicating that ste11(+) is epistatic to gaf1(+) with respect to sporulation efficiency, and accordingly that gaf1(+) functions upstream of ste11(+) in the signaling pathway governing sexual development. gaf1Δ strains showed accelerated ste11(+) expression under nitrogen starvation and increased ste11(+) expression even under normal conditions. Electrophoretic mobility shift assay analysis demonstrated that Gaf1 specifically binds to the canonical GATA motif (5'-HGATAR-3') spanning from -371 to -366 in ste11(+) promoter. Consequently, Gaf1 provides the prime example for negative regulation of ste11(+) transcription through direct binding to a cis-acting motif of its promoter.","doi":"10.1371/journal.pone.0042409","authors":"Kim L, Hoe KL, Yu YM, Yeon JH, Maeng PJ","authors_abbrev":"Kim L et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-18","publication_year":"2012","canto_session_key":"19ff38e31ee375f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-03 08:34:36","canto_approved_date":"2026-04-11 20:24:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 14:48:32","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1902.01","SPBC32C12.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-08-03"},{"uniquename":"PMID:34493069","title":"Identification of novel microtubule inhibitors effective in fission yeast and human cells and their effects on breast cancer cell lines.","citation":"Open Biol 2021 Sep;11(9):210161","abstract":"Microtubules are critical for a variety of cellular processes such as chromosome segregation, intracellular transport and cell shape. Drugs against microtubules have been widely used in cancer chemotherapies, though the acquisition of drug resistance has been a significant issue for their use. To identify novel small molecules that inhibit microtubule organization, we conducted sequential phenotypic screening of fission yeast and human cells. From a library of diverse 10 371 chemicals, we identified 11 compounds that inhibit proper mitotic progression both in fission yeast and in HeLa cells. An  in vitro  assay revealed that five of these compounds are strong inhibitors of tubulin polymerization. These compounds directly bind tubulin and destabilize the structures of tubulin dimers. We showed that one of the compounds, L1, binds to the colchicine-binding site of microtubules and exhibits a preferential potency against a panel of human breast cancer cell lines compared with a control non-cancer cell line. In addition, L1 overcomes cellular drug resistance mediated by βIII tubulin overexpression and has a strong synergistic effect when combined with the Plk1 inhibitor BI2536. Thus, we have established an economically effective drug screening strategy to target mitosis and microtubules, and have identified a candidate compound for cancer chemotherapy.","doi":"10.1098/rsob.210161","authors":"Morishita J, Nurse P","authors_abbrev":"Morishita J et al.","pubmed_publication_date":"Sep 2021","pubmed_entrez_date":"2021-09-08","publication_year":"2021","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2021-09-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8431959","title":"The smt-0 mutation which abolishes mating-type switching in fission yeast is a deletion.","citation":"Curr Genet 1993 Feb;23(2):184-6","abstract":"Mating-type switching in the fission yeast, S. pombe, is initiated by a DNA double-strand break (DSB) between the mat1 cassette and the H1 homology box. The mat1-cis-acting mutant, smt-0, abolishes mating-type switching and is shown here to be a 263-bp deletion. This deletion starts in the middle of the H1 homology box, 31 bp from the site of the DSB, and extends into the flanking region distal to mat1. The sequence of the region distal to H1 in the wild-type is also presented. In this region we observe a bias in the distribution of purine residues between the two DNA strands.","authors":"Styrkársdóttir U, Egel R, Nielsen O","authors_abbrev":"Styrkársdóttir U et al.","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41256635","title":"Contrasting mutation patterns in haploid and diploid cells from two yeast species.","citation":"bioRxiv 2025 Oct 01;","abstract":"There is significant variation in the rate and spectrum of spontaneous mutations among taxa. How this variation is shaped by natural selection remains a subject of debate. The drift barrier hypothesis proposes that selection generally favors lower mutation rates due to the risk of deleterious mutations but acts less effectively against weak mutator alleles in smaller populations, allowing the mutation rate to increase due to genetic drift. Given this model, we propose that mutation rates may also be elevated in cell types that appear rarely in a population, where DNA replication and repair processes are subject to selection less often. We can begin to test this prediction in yeast species, some of which can be grown in either a haploid or diploid cell state. Existing data on the budding yeast  Saccharomyces cerevisiae  support this prediction, with a higher mutation rate observed in haploids, which is the rare cell type in natural populations. However, this pattern could also appear if haploidy is inherently mutagenic, regardless of the dominant cell type. To test these alternatives, we conducted a mutation accumulation experiment with haploid and diploid cells of the fission yeast  Schizosaccharomyces pombe , in which diploidy is the rare cell type. In this species, we found a higher mutation rate in diploids, consistent with our prediction. In both species, the spectrum of mutations is also influenced by ploidy state. Our findings suggest that limits to selection on mutation may be evident as variation within species.","doi":"10.1101/2025.09.30.679554","authors":"Bao K, Gupte R, Braker N, Sharp NP","authors_abbrev":"Bao K et al.","pubmed_publication_date":"01 Oct 2025","pubmed_entrez_date":"2025-11-19","publication_year":"2025","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2025-11-20 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12759375","title":"Fission yeast meu14+ is required for proper nuclear division and accurate forespore membrane formation during meiosis II.","citation":"J Cell Sci 2003 Jul 01;116(Pt 13):2721-35","abstract":"Using a meiosis-specific subtracted cDNA library of Schizosaccharomyces pombe, we identified meu14+ as a gene whose expression is upregulated during meiosis. Transcription of meu14+ is induced abruptly after the cell enters meiosis. Its transcription is dependent on the meiosis-specific transcription factor Mei4. In meu14Delta cells, the segregation and modification of the SPBs (spindle pole bodies) and microtubule elongation during meiosis II were aberrant. Meiotic meu14Delta cells consequently produced a high frequency of abnormal tetranucleate cells harboring aberrant forespore membranes and failed to produce asci. In wild-type cells harboring the integrated meu14+-gfp fusion gene, Meu14-GFP first appeared inside the nuclear region at prophase II, after which it accumulated beside the two SPBs at metaphase II. Thereafter, it formed two ring-shaped structures that surrounded the nucleus at early anaphase II. At post-anaphase II, it disappeared. Meu14-GFP appears to localize at the border of the forespore membrane that later develops into spore walls at the end of sporulation. This was confirmed by coexpressing Spo3-HA, a component of the forespore membrane, with Meu14-GFP. Taken together, we conclude that meu14+ is crucial in meiosis in that it participates in both the nuclear division during meiosis II and the accurate formation of the forespore membrane.","authors":"Okuzaki D, Satake W, Hirata A, Nojima H","authors_abbrev":"Okuzaki D et al.","pubmed_publication_date":"01 Jul 2003","pubmed_entrez_date":"2003-05-22","publication_year":"2003","canto_session_key":"90ac205089d49c8b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-05-25 16:09:35","canto_approved_date":"2026-03-06 10:47:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-11 17:51:01","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.11","SPAC1F3.06c","SPBC1347.03","SPAC607.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-05-25"},{"uniquename":"PMID:9445033","title":"The application of a homologous recombination assay revealed amino acid residues in an LTR-retrotransposon that were critical for integration.","citation":"J Virol 1998 Feb;72(2):1324-33","abstract":"Retroviruses and their relatives, the LTR-retrotransposons, possess an integrase protein (IN) that is required for the insertion of reverse transcripts into the genome of host cells. Schizosaccharomyces pombe is the host of Tf1, an LTR-retrotransposon with integration activity that can be studied by using techniques of yeast genetics. In this study, we sought to identify amino acid substitutions in Tf1 that specifically affected the integration step of transposition. In addition to seeking amino acid substitutions in IN, we also explored the possibility that other Tf1 proteins contributed to integration. By comparing the results of genetic assays that monitored both transposition and reverse transcription, we were able to seek point mutations throughout Tf1 that blocked transposition but not the synthesis of reverse transcripts. These mutant versions of Tf1 were candidates of elements that possessed defects in the integration step of transposition. Five mutations in Tf1 that resulted in low levels of integration were found to be located in the IN protein: two substitutions in the N-terminal Zn domain, two in the catalytic core, and one in the C-terminal domain. These results suggested that each of the three IN domains was required for Tf1 transposition. The potential role of these five amino acid residues in the function of IN is discussed. Two of the mutations that reduced integration mapped to the RNase H (RH) domain of Tf1 reverse transcriptase. The Tf1 elements with the RH mutations produced high levels of reverse transcripts, as determined by recombination and DNA blot analysis. These results indicated that the RH of Tf1 possesses a function critical for transposition that is independent of the accumulation of reverse transcripts.","authors":"Atwood A, Choi J, Levin HL","authors_abbrev":"Atwood A et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-01-28","publication_year":"1998","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26791325","title":"Predicting chemotherapeutic drug combinations through gene network profiling.","citation":"Sci Rep 2016 Jan 21;6:18658","abstract":"Contemporary chemotherapeutic treatments incorporate the use of several agents in combination. However, selecting the most appropriate drugs for such therapy is not necessarily an easy or straightforward task. Here, we describe a targeted approach that can facilitate the reliable selection of chemotherapeutic drug combinations through the interrogation of drug-resistance gene networks. Our method employed single-cell eukaryote fission yeast (Schizosaccharomyces pombe) as a model of proliferating cells to delineate a drug resistance gene network using a synthetic lethality workflow. Using the results of a previous unbiased screen, we assessed the genetic overlap of doxorubicin with six other drugs harboring varied mechanisms of action. Using this fission yeast model, drug-specific ontological sub-classifications were identified through the computation of relative hypersensitivities. We found that human gastric adenocarcinoma cells can be sensitized to doxorubicin by concomitant treatment with cisplatin, an intra-DNA strand crosslinking agent, and suberoylanilide hydroxamic acid, a histone deacetylase inhibitor. Our findings point to the utility of fission yeast as a model and the differential targeting of a conserved gene interaction network when screening for successful chemotherapeutic drug combinations for human cells.","doi":"10.1038/srep18658","authors":"Nguyen TT, Chua JK, Seah KS, Koo SH, Yee JY, Yang EG, Lim KK, Pang SY, Yuen A, Zhang L, Ang WH, Dymock B, Lee EJ, Chen ES","authors_abbrev":"Nguyen TT et al.","pubmed_publication_date":"21 Jan 2016","pubmed_entrez_date":"2016-01-22","publication_year":"2016","canto_session_key":"a5357dbd0df23004","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-03-04 14:39:47","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-03-04 14:39:40","canto_added_date":"2016-01-24 01:15:24","annotation_curators":[],"file_curator_name":"Nguyen Thi Thuy Trang","file_curator_role":"community","annotation_file_curators":[{"name":"Nguyen Thi Thuy Trang","community_curator":true,"annotation_count":343,"orcid":null,"file_type":"PHAF","file_name":"PMID_26791325_phaf.tsv"}],"genes":["SPBC18H10.04c","SPAC1687.12c","SPCC777.13","SPBP8B7.22","SPAC1952.05","SPAC14C4.16","SPBC27B12.10c","SPBC28F2.10c","SPAC17H9.08","SPBC106.04","SPAC17H9.19c","SPBC215.03c","SPBC365.13c","SPBC106.05c","SPAC644.14c","SPAC823.10c","SPCC16C4.20c","SPCC162.05","SPBC17D1.02","SPAC1805.07c","SPBC2D10.13","SPBC4B4.03","SPCC338.08","SPBC1604.02c","SPAC15A10.03c","SPCC757.10","SPAPB17E12.04c","SPBC146.12","SPAC2F3.11","SPBC2D10.16","SPAC23H3.06","SPBPJ4664.01","SPCC1259.04","SPAC23C11.08","SPAC4F10.04","SPCC24B10.08c","SPAC630.14c","SPAC2C4.05","SPAC23D3.09","SPAC6B12.05c","SPCC16A11.07","SPBC18H10.02","SPAC17G8.07","SPCC23B6.05c","SPAC16A10.05c","SPBC1105.10","SPAC31G5.19","SPBC16H5.13","SPBC32H8.07","SPAC10F6.08c","SPAC13C5.07","SPCC1672.04c","SPCC663.03","SPBC651.06","SPAPB1E7.02c","SPCC576.12c","SPCC1840.09","SPAC2F7.07c","SPBC32F12.08c","SPAC9E9.09c","SPAC1B2.04","SPBC365.10","SPAC222.04c","SPAC513.03","SPAC3H8.05c","SPCC1259.03","SPAC6G9.14","SPAPB1A10.09","SPCC1223.15c","SPAC144.02","SPAC664.02c","SPBC337.15c","SPAC23G3.04","SPBC947.14c","SPCC18.02","SPAC29B12.08","SPCC1739.14","SPBC2F12.12c","SPCC417.02","SPBC21C3.20c","SPAC8E11.02c","SPBC16A3.07c","SPBC21B10.13c","SPAC56F8.04c","SPBC1734.15","SPAC3C7.03c","SPCC31H12.08c","SPAC144.06","SPBC19G7.10c","SPBC4F6.10"],"gene_count":90,"ltp_gene_count":0,"approved_date":"2016-03-04"},{"uniquename":"PMID:30310662","title":"Oxidative stress and mitochondrial impairment mediated apoptotic cell death induced by terpinolene in  Schizosaccharomyces pombe .","citation":"Toxicol Res (Camb) 2018 Sep 01;7(5):848-858","abstract":"Terpinolene is one of the most abundant monoterpenes used as a food supplement or odorant in cosmetics and the pharmaceutical industry. In this study, we aimed to assess apoptotic, oxidative and cytotoxic effects of terpinolene. We used the fission yeast ( Schizosaccharomyces pombe ) as a promising uni-cellular model organism in molecular toxicology and cell death research, due to its resemblance to mammalian cells at the molecular level. After terpinolene exposure (200-800 mg L -1 ), the IC 50  and LC 50  were calculated as 349.17 mg L -1  and 593.87 mg L -1 . Cells, stained with acridine orange/ethidium bromide and DAPI, showed apoptotic nuclear morphology, chromatin condensation and fragmentation. 2,7-Dichlorodihydrofluorescein diacetate (DCFDA) fluorescence gradually increased (1.5-2-fold increase) in correlation with increasing concentrations of terpinolene (200-800 mg L -1 ). Mitochondrial impairment at higher concentrations of terpinolene (400-800 mg L -1 ) was shown by Rhodamine 123 staining. Real-time PCR experiments showed significant increases (1.5-3-fold) in SOD1 and GPx1 levels ( p  < 0.05) as well as 2-2.5-fold increases ( p  < 0.05) in pro-apoptotic factors, Pca1 and Sprad9. The potential effects of terpinolene on programmed cell death and the underlying mechanisms were clarified in unicellular model fungi,  Schizosaccharomyces pombe .","doi":"10.1039/c8tx00100f","authors":"Agus HH, Sarp C, Cemiloglu M","authors_abbrev":"Agus HH et al.","pubmed_publication_date":"01 Sep 2018","pubmed_entrez_date":"2018-10-13","publication_year":"2018","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2018-10-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27037076","title":"Transformation of Schizosaccharomyces pombe: Protoplast Procedure.","citation":"Cold Spring Harb Protoc 2016 Apr 01;2016(4):pdb.prot090977","abstract":"Transformation of Schizosaccharomyces pombe with DNA requires the conditioning of cells to promote DNA uptake followed by cell growth under conditions that select and maintain the plasmid or integration event. The three main methodologies are electroporation, treatment with lithium cations, and transformation of protoplasts. The protocol for protoplast transformation, which is described here, is more complicated than those for electroporation or lithium acetate and thus less often used. However, for some strains, it remains the only reliable protocol.","doi":"10.1101/pdb.prot090977","authors":"Murray JM, Watson AT, Carr AM","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"01 Apr 2016","pubmed_entrez_date":"2016-04-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-04-04 00:15:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31533197","title":"Coordinating septum formation and the actomyosin ring during cytokinesis in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2019 Dec;112(6):1645-1657","abstract":"During cytokinesis, animal and fungal cells form a membrane furrow via actomyosin ring constriction. Our understanding of actomyosin ring-driven cytokinesis stems extensively from the fission yeast model system. However, unlike animal cells, actomyosin ring constriction occurs simultaneously with septum formation in fungi. While the formation of an actomyosin ring is essential for cytokinesis in fission yeast, proper furrow formation also requires septum deposition. The molecular mechanisms of spatiotemporal coordination of septum deposition with actomyosin ring constriction are poorly understood. Although the role of the actomyosin ring as a mechanical structure driving furrow formation is better understood, its role as a spatiotemporal landmark for septum deposition is not widely discussed. Here we review and discuss the recent advances describing how the actomyosin ring spatiotemporally regulates membrane traffic to promote septum-driven cytokinesis in fission yeast. Finally, we explore emerging questions in cytokinesis, and discuss the role of extracellular matrix during cytokinesis in other organisms.","doi":"10.1111/mmi.14387","authors":"Hercyk BS, Onwubiko UN, Das ME","authors_abbrev":"Hercyk BS et al.","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-09-19","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-09-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22216090","title":"A higher-order generalized singular value decomposition for comparison of global mRNA expression from multiple organisms.","citation":"PLoS One 2011;6(12):e28072","abstract":"The number of high-dimensional datasets recording multiple aspects of a single phenomenon is increasing in many areas of science, accompanied by a need for mathematical frameworks that can compare multiple large-scale matrices with different row dimensions. The only such framework to date, the generalized singular value decomposition (GSVD), is limited to two matrices. We mathematically define a higher-order GSVD (HO GSVD) for N≥2 matrices D(i)∈R(m(i) × n), each with full column rank. Each matrix is exactly factored as D(i)=U(i)Σ(i)V(T), where V, identical in all factorizations, is obtained from the eigensystem SV=VΛ of the arithmetic mean S of all pairwise quotients A(i)A(j)(-1) of the matrices A(i)=D(i)(T)D(i), i≠j. We prove that this decomposition extends to higher orders almost all of the mathematical properties of the GSVD. The matrix S is nondefective with V and Λ real. Its eigenvalues satisfy λ(k)≥1. Equality holds if and only if the corresponding eigenvector v(k) is a right basis vector of equal significance in all matrices D(i) and D(j), that is σ(i,k)/σ(j,k)=1 for all i and j, and the corresponding left basis vector u(i,k) is orthogonal to all other vectors in U(i) for all i. The eigenvalues λ(k)=1, therefore, define the \"common HO GSVD subspace.\" We illustrate the HO GSVD with a comparison of genome-scale cell-cycle mRNA expression from S. pombe, S. cerevisiae and human. Unlike existing algorithms, a mapping among the genes of these disparate organisms is not required. We find that the approximately common HO GSVD subspace represents the cell-cycle mRNA expression oscillations, which are similar among the datasets. Simultaneous reconstruction in the common subspace, therefore, removes the experimental artifacts, which are dissimilar, from the datasets. In the simultaneous sequence-independent classification of the genes of the three organisms in this common subspace, genes of highly conserved sequences but significantly different cell-cycle peak times are correctly classified.","doi":"10.1371/journal.pone.0028072","authors":"Ponnapalli SP, Saunders MA, Van Loan CF, Alter O","authors_abbrev":"Ponnapalli SP et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2012-01-05","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15292395","title":"AtSGP1, AtSGP2 and MAP4K alpha are nucleolar plant proteins that can complement fission yeast mutants lacking a functional SIN pathway.","citation":"J Cell Sci 2004 Aug 15;117(Pt 18):4265-75","abstract":"In the fission yeast Schizosaccharomyces pombe, the onset of septum formation is signalled via the septation initiation network (SIN) involving several protein kinases and a GTPase. Arabidopsis thaliana and Brassica napus proteins homologous to fission yeast spg1p (AtSGP1, AtSGP2), cdc7p (AtMAP3K epsilon 1, AtMAP3K epsilon 2, BnMAP3K epsilon 1) and sid1p (AtMAP4K alpha 1, AtMAP4K alpha 2, BnMAP4K alpha 2) exhibit a significant similarity. The plant proteins AtSGP1/2 and BnMAP4K alpha 2 are able to complement the S. pombe mutant proteins spg1-B8 and sid1-239, respectively and to induce mutisepta when overexpressed in wild-type yeast. Yeast two-hybrid assays demonstrated interactions both between plant proteins and between plant and yeast proteins of the SIN pathway. However, the primary structure of the proteins as well as the partial complementation of yeast mutants indicates that plant homologous proteins and their yeast counterparts have diverged during evolution. Real-time RT-PCR studies demonstrated plant SIN-related gene expression in all organs tested and a co-expression pattern during the cell cycle, with a higher accumulation at G(2)-M. During interphase, the plant SIN-related proteins were found to co-localise predominantly in the nucleolus of the plant cells, as shown by fusions to green fluorescent protein. These data suggest the existence of a plant SIN-related pathway.","authors":"Champion A, Jouannic S, Guillon S, Mockaitis K, Krapp A, Picaud A, Simanis V, Kreis M, Henry Y","authors_abbrev":"Champion A et al.","pubmed_publication_date":"15 Aug 2004","pubmed_entrez_date":"2004-08-05","publication_year":"2004","canto_session_key":"1a30ba36ba3e6fcc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-10-12 18:59:59","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-12 18:59:50","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.06c","SPAC9G1.09"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2015-10-12"},{"uniquename":"EMBL:AF156541","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPATRNAPRO.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25844404","title":"INSIGHTS INTO THE MECHANICS OF CYTOKINETIC RING ASSEMBLY USING 3D MODELING.","citation":"Int Mech Eng Congress Expo 2014;9","abstract":"During fission yeast cytokinesis, actin filaments nucleated by cortical formin Cdc12 are captured by myosin motors bound to a band of cortical nodes. The myosin motors exert forces that pull nodes together into a contractile ring. Cross-linking interactions help align actin filaments and nodes into a single bundle. Mutations in the myosin motor domain and changes in the concentration of cross-linkers alpha-actinin and fimbrin alter the morphology of the condensing network, leading to clumps, rings or extended meshworks. How the contractile tension developing during ring formation depends on the interplay between network morphology, myosin motor activity, cross-linking and actin filament turnover remains to be elucidated. We addressed this question using a 3D computational model in which semiflexible actin filaments (represented as beads connected by springs) grow from formins, can be captured by myosin in neighboring nodes, and get cross-linked with one another through an attractive interaction. We identify regimes of tension generation between connected nodes under a wide set of conditions regarding myosin dynamics and strength of cross-linking between actin filaments. We find conditions that maximize circumferential tension, correlate them with network morphology and propose experiments to test these predictions. This work addresses \"Morphogenesis of soft and living matter\" using computational modeling to simulate cytokinetic ring assembly from the key molecular mechanisms of viscoelastic cross-linked actin networks that include active molecular motors.","authors":"Bidone TC, Tang H, Vavylonis D","authors_abbrev":"Bidone TC et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2015-04-07","publication_year":"2014","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2015-04-10 00:19:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2690071","title":"Substitution at position 116 of Schizosaccharomyces pombe calmodulin decreases its stability under nitrogen starvation and results in a sporulation-deficient phenotype.","citation":"Proc Natl Acad Sci U S A 1989 Dec;86(24):9737-41","abstract":"We constructed Schizosaccharomyces pombe strains that carry phenylalanine, instead of arginine, as residue 116 of calmodulin by site-directed mutagenesis of the cam1 gene. Whereas haploid strains carrying the mutant allele, designated cam1-F116, exhibit no defects in growth and mating, diploid strains homozygous for cam1-F116 are deficient in sporulation. The four nuclei generated by the two serial meiotic divisions are not encapsulated in these diploids. The mutation is recessive. Semiquantitative analysis using polyclonal antibodies showed that vegetatively growing cam1-F116 cells have a smaller amount of calmodulin than wild-type cells. The quantitative difference becomes more remarkable if the cells are starved for nitrogen, which is a condition for induction of sporulation. In addition to this in vivo observation, we showed in vitro that the mutant protein is susceptible to a proteolytic activity induced by nitrogen starvation that hardly affects the wild-type calmodulin. Thus, the sporulation deficiency of the cam1-F116 mutant may be ascribed to shortage of calmodulin due to proteolysis of the mutant molecules under nitrogen starvation. Two other mutations at position 116 resulted in similar but leakier Spo- phenotypes.","authors":"Takeda T, Imai Y, Yamamoto M","authors_abbrev":"Takeda T et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_session_key":"7f19390df16a5511","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-07-01 10:41:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-13 12:46:28","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-06-13"},{"uniquename":"PMID:34005220","canto_session_key":"b6bf71a072b430c7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32347926","title":"Involvement of Pca1 in ROS-mediated apoptotic cell death induced by alpha-thujone in the fission yeast (Schizosaccharomyces pombe).","citation":"FEMS Yeast Res 2020 Jun 01;20(4)","abstract":"Alpha-thujone, widely used in beverages (1-5 mg/kg), is known to have cytotoxic effects, but the mode of action and the role of potential apoptotic proteins in yeast cell death should be unraveled. In this study, we used Schizosaccharomyces pombe, which is a promising unicellular model organism in mechanistic toxicology and cell biology, to investigate the involvement of pro-apoptotic factors in alpha-thujone-induced cell death. We showed alpha-thujone-induced ROS accumulation-dependent cytotoxicity and apoptosis. In addition, we used superoxide dismutase-deficient cells (sod1 and sod2 mutants) to understand the effect of oxidative stress. Alpha-thujone caused significant cytotoxicity and apoptotic cell death, particularly in sod mutants. Moreover, two potential apoptotic factors, pca1 and pnu1 (pombe caspase-1 and pombe nuc1) were investigated to understand which factor mediates alpha-thujone-induced cell death. Pca1-deficient cells showed increased survival rates and reduced apoptosis in comparison to parental cells after chemical treatment while pnu1 mutation did not cause any significant change and the response was found identical as of parental cells. Yeast responded to alpha-thujone in caspase-dependent manner which was very similar to that for acetic acid. In conclusion, alfa-thujone-induced apoptosis and accounting mechanisms, which were mediated by ROS and driven by Pca1, were clarified in the unicellular model, S. pombe.","doi":"10.1093/femsyr/foaa022","authors":"Agus HH, Kok G, Derinoz E, Oncel D, Yilmaz S","authors_abbrev":"Agus HH et al.","pubmed_publication_date":"01 Jun 2020","pubmed_entrez_date":"2020-04-30","publication_year":"2020","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2020-05-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1840.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34951983","title":"Force by minus-end motors Dhc1 and Klp2 collapses the S. pombe spindle after laser ablation.","citation":"Biophys J 2022 Jan 18;121(2):263-276","abstract":"A microtubule-based machine called the mitotic spindle segregates chromosomes when eukaryotic cells divide. In the fission yeast Schizosaccharomyces pombe, which undergoes closed mitosis, the spindle forms a single bundle of microtubules inside the nucleus. During elongation, the spindle extends via antiparallel microtubule sliding by molecular motors. These extensile forces from the spindle are thought to resist compressive forces from the nucleus. We probe the mechanism and maintenance of this force balance via laser ablation of spindles at various stages of mitosis. We find that spindle pole bodies collapse toward each other after ablation, but spindle geometry is often rescued, allowing spindles to resume elongation. Although this basic behavior has been previously observed, many questions remain about the phenomenon's dynamics, mechanics, and molecular requirements. In this work, we find that previously hypothesized viscoelastic relaxation of the nucleus cannot explain spindle shortening in response to laser ablation. Instead, spindle collapse requires microtubule dynamics and is powered by the minus-end-directed motor proteins dynein Dhc1 and kinesin-14 Klp2, but it does not require the minus-end-directed kinesin Pkl1.","doi":"10.1016/j.bpj.2021.12.019","authors":"Zareiesfandabadi P, Elting MW","authors_abbrev":"Zareiesfandabadi P et al.","pubmed_publication_date":"18 Jan 2022","pubmed_entrez_date":"2021-12-24","publication_year":"2022","canto_session_key":"99bae54ee5a8b7f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mary Williard Elting","canto_first_approved_date":"2023-06-08 08:32:01","canto_approved_date":"2023-06-08 08:32:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-07 19:45:32","canto_added_date":"2021-12-28 01:15:04","annotation_curators":[{"name":"Mary Williard Elting","community_curator":true,"annotation_count":4,"orcid":"0000-0002-1662-9802","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.10","SPAC1093.06c","SPAC3A11.14c","SPBC800.05c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2023-06-08"},{"uniquename":"PMID:20152181","title":"Nuclear retention of fission yeast dicer is a prerequisite for RNAi-mediated heterochromatin assembly.","citation":"Dev Cell 2010 Jan 19;18(1):102-13","abstract":"RNaseIII ribonucleases act at the heart of RNA silencing pathways by processing precursor RNAs into mature microRNAs and siRNAs. In the fission yeast Schizosaccharomyces pombe, siRNAs are generated by the RNaseIII enzyme Dcr1 and are required for heterochromatin formation at centromeres. In this study, we have analyzed the subcellular localization of Dcr1 and found that it accumulates in the nucleus and is enriched at the nuclear periphery. Nuclear accumulation of Dcr1 depends on a short motif that impedes nuclear export promoted by the double-stranded RNA binding domain of Dcr1. Absence of this motif renders Dcr1 mainly cytoplasmic and is accompanied by remarkable changes in gene expression and failure to assemble heterochromatin. Our findings suggest that Dicer proteins are shuttling proteins and that the steady-state subcellular levels can be shifted toward either compartment.","doi":"10.1016/j.devcel.2009.11.011","authors":"Emmerth S, Schober H, Gaidatzis D, Roloff T, Jacobeit K, Bühler M","authors_abbrev":"Emmerth S et al.","pubmed_publication_date":"19 Jan 2010","pubmed_entrez_date":"2010-02-16","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7820554","title":"Cell cycle. In and out of the cell cycle.","citation":"Curr Biol 1994 Sep 01;4(9):828-30","abstract":"Studies of fission yeast are shedding light on how the same genes allow cells to respond to their environment either by growing and proliferating mitotically or by arresting growth to allow differentiation and meiosis.","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"01 Sep 1994","pubmed_entrez_date":"1994-09-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17671430","title":"Bin1 interacts with and restrains the DNA end-binding protein complex Ku.","citation":"Cell Cycle 2007 Aug 01;6(15):1914-8","abstract":"The Bin1 gene encodes a BAR adapter protein that suppresses cancer by poorly defined mechanisms. In an effort to gain insights, we identified cellular proteins that form biochemical complexes with Bin1 protein. Here we report that Bin1 physically binds to Ku, a DNA end-binding protein that functions in telomere maintenance, apoptosis, and DNA repair. Both Ku70 and Ku80 were purified from human and murine cell extracts using the Bin1 BAR domain as an affinity matrix. A BAR domain mutation that destroys antioncogenic activity completely abolished Ku binding, supporting functional relevance. To further evaluate meaning, we investigated interactions between the Bin1 homolog hob1+ and the Ku homologs pku70+ and pku80+ in fission yeast. Notably, deleting pku70+ or pku80+ relieved the survival defect displayed by hob1delta cells after treatment with the DNA damaging agent phleomycin, suggesting that hob1+ may restrain Ku. Consistent with this notion, telomere length was altered in hob1delta cells. The potential relevance of Bin1-Ku interaction to cancer are discussed in light of these findings.","authors":"Ramalingam A, Farmer GE, Stamato TD, Prendergast GC","authors_abbrev":"Ramalingam A et al.","pubmed_publication_date":"01 Aug 2007","pubmed_entrez_date":"2007-08-03","publication_year":"2007","canto_session_key":"e1c9a87d40aa450e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-03-06 15:36:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-03-06 15:36:24","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC543.03c","SPCC126.02c","SPBC21D10.12"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-03-06"},{"uniquename":"EMBL:AU013266","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7597098","title":"Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signaling module in the fission yeast Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1995 Jun 20;92(13):6180-4","abstract":"We describe a protein kinase, Shk1, from the fission yeast Schizosaccharomyces pombe, which is structurally related to the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases. We provide genetic evidence for physical and functional interaction between Shk1 and the Cdc42 GTP-binding protein required for normal cell morphology and mating in S. pombe. We further show that expression of the STE20 gene complements the shk1 null mutation and that Shk1 is capable of signaling to the pheromone-responsive mitogen-activated protein kinase cascade in S. cerevisiae. Our results lead us to propose that signaling modules composed of small GTP-binding proteins and protein kinases related to Shk1, Ste20, and p65PAK, are highly conserved in evolution and participate in both cytoskeletal functions and mitogen-activated protein kinase signaling pathways.","authors":"Marcus S, Polverino A, Chang E, Robbins D, Cobb MH, Wigler MH","authors_abbrev":"Marcus S et al.","pubmed_publication_date":"20 Jun 1995","pubmed_entrez_date":"1995-06-20","publication_year":"1995","canto_session_key":"d357e9118dee486d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-31 14:52:31","canto_approved_date":"2022-07-27 12:35:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-12 15:36:16","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC1604.14c","SPAC110.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-07-31"},{"uniquename":"PMID:29092815","title":"The kinase domain residue serine 173 of  S  chizosaccharomyce  s pombe  Chk1 kinase is critical for the response to DNA replication stress.","citation":"Biol Open 2017 Dec 15;6(12):1840-1850","abstract":"While mammalian Chk1 kinase regulates replication origins, safeguards fork integrity and promotes fork progression, yeast Chk1 acts only in G1 and G2. We report here that the mutation of serine 173 (S173A) in the kinase domain of fission yeast Chk1 abolishes the G1-M and S-M checkpoints with little impact on the G2-M arrest. This separation-of-function mutation strongly reduces the Rad3-dependent phosphorylation of Chk1 at serine 345 during logarithmic growth, but not when cells experience exogenous DNA damage. Loss of S173 lowers the restrictive temperature of a catalytic DNA polymerase epsilon mutant ( cdc20.M10 ) and is epistatic with a mutation in DNA polymerase delta ( cdc6.23 ) when DNA is alkylated by methyl-methanesulfate (MMS). The  chk1-S173A  allele is uniquely sensitive to high MMS concentrations where it displays a partial checkpoint defect. A complete checkpoint defect occurs only when DNA replication forks break in cells without the intra-S phase checkpoint kinase Cds1. Chk1-S173A is also unable to block mitosis when the G1 transcription factor Cdc10 ( cdc10.V50 ) is impaired. We conclude that serine 173, which is equivalent to lysine 166 in the activation loop of human Chk1, is only critical in DNA polymerase mutants or when forks collapse in the absence of Cds1.","doi":"10.1242/bio.029272","authors":"Coulton N, Caspari T","authors_abbrev":"Coulton N et al.","pubmed_publication_date":"15 Dec 2017","pubmed_entrez_date":"2017-11-03","publication_year":"2017","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-11-04 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC25H2.13c","SPBC336.04","SPCC1259.13"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:29212877","title":"High-speed superresolution imaging of the proteins in fission yeast clathrin-mediated endocytic actin patches.","citation":"Mol Biol Cell 2018 Feb 01;29(3):295-303","abstract":"To internalize nutrients and cell surface receptors via clathrin-mediated endocytosis, cells assemble at least 50 proteins, including clathrin, clathrin-interacting proteins, actin filaments, and actin binding proteins, in a highly ordered and regulated manner. The molecular mechanism by which actin filament polymerization deforms the cell membrane is unknown, largely due to lack of knowledge about the organization of the regulatory proteins and actin filaments. We used high-speed superresolution localization microscopy of live fission yeast cells to improve the spatial resolution to ∼35 nm with 1-s temporal resolution. The nucleation promoting factors Wsp1p (WASp) and Myo1p (myosin-I) define two independent pathways that recruit Arp2/3 complex, which assembles two zones of actin filaments. Myo1p concentrates at the site of endocytosis and initiates a zone of actin filaments assembled by Arp2/3 complex. Wsp1p appears simultaneously at this site but subsequently moves away from the cell surface as it stimulates Arp2/3 complex to assemble a second zone of actin filaments. Cells lacking either nucleation-promoting factor assemble only one, stationary, zone of actin filaments. These observations support our two-zone hypothesis to explain endocytic tubule elongation and vesicle scission in fission yeast.","doi":"10.1091/mbc.E17-06-0415","authors":"Arasada R, Sayyad WA, Berro J, Pollard TD","authors_abbrev":"Arasada R et al.","pubmed_publication_date":"01 Feb 2018","pubmed_entrez_date":"2017-12-08","publication_year":"2018","canto_session_key":"9e31f7379bd4a3d4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-12-09 01:15:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011818","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32061930","title":"Telomeric Transcription and Telomere Rearrangements in Quiescent Cells.","citation":"J Mol Biol 2020 Jul 10;432(15):4220-4231","abstract":"Despite the condensed nature of terminal sequences, the telomeres are transcribed into a group of noncoding RNAs, including the TElomeric Repeat-containing RNA (TERRA). Since the discovery of TERRA, its evolutionary conserved function has been confirmed, and its involvement in telomere length regulation, heterochromatin establishment, and telomere recombination has been demonstrated. We previously reported that TERRA is upregulated in quiescent fission yeast cells, although the global transcription is highly reduced. Elevated telomeric transcription was also detected when telomeres detach from the nuclear periphery. These intriguing observations unveil unexpected facets of telomeric transcription in arrested cells. In this review, we present the different aspects of TERRA transcription during quiescence and discuss their implications for telomere maintenance and cell fate.","doi":"10.1016/j.jmb.2020.01.034","authors":"Coulon S, Vaurs M","authors_abbrev":"Coulon S et al.","pubmed_publication_date":"10 Jul 2020","pubmed_entrez_date":"2020-02-17","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8335253","title":"Identification and genetic analysis of Schizosaccharomyces pombe cDNAs that suppress deletion of IRA1 in Saccharomyces cerevisiae.","citation":"Gene 1993 Jul 15;129(1):147-52","abstract":"Ira1 is a negative regulator of Ras proteins in Saccharomyces cerevisiae. Deletion of IRA1 leads to constitutive activation of the Ras/cyclic AMP (cAMP) pathway, which results in several phenotypes including sensitivity to heat-shock (HS) treatment. We have identified eight Schizosaccharomyces pombe cDNAs that, when overexpressed, suppress the HS-sensitive phenotype associated with the deletion of IRA1 in S. cerevisiae. To determine where these cDNAs act, we tested their ability to suppress other mutations that activate the Ras/cAMP pathway in S. cerevisiae. Two of the cDNA clones, pPSI1 and pPSI2, failed to suppress the HS-sensitive phenotype induced by the activating RAS2Val19 mutation. Clone pPSI2 encodes Gap1/Sar1, a Sz. pombe homologue of Ira1, which has been previously identified. Three of the six RAS2Val19 suppressors could suppress the deletion of PDE1 and PDE2, the cAMP phosphodiesterase (Pde)-encoding genes, suggesting that they act downstream from adenylyl cyclase (Cyr). The remaining three clones, pPSI3, pPSI6 and pPSI7, encode proteins that may suppress the HS-sensitive phenotype by reducing Ras and/or Cyr activity. One of these, pPSI3, contains a cDNA that encodes the C-terminal region (aa 166-550) of the Sz. pombe Dbp2 protein, a homologue of the human p68 RNA helicase. We have amplified cDNAs encoding the full-length Sz. pombe Dbp2 protein by the polymerase chain reaction method and have cloned them into a S. cerevisiae expression vector. The ira1- cells harboring these plasmids retained their HS-sensitive phenotype. These results suggest that the truncated Dbp2, but not the full-length protein, is capable of interfering with Ras and/or Cyr activity.","authors":"Matviw H, Yu G, Young D","authors_abbrev":"Matviw H et al.","pubmed_publication_date":"15 Jul 1993","pubmed_entrez_date":"1993-07-15","publication_year":"1993","canto_session_key":"c25ddc6c90f4611a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-07 14:44:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-07 14:44:36","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC24C6.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-05-07"},{"uniquename":"PMID:34851357","title":"A novel fission yeast platform to model N-glycosylation and the bases of congenital disorders of glycosylation type I.","citation":"J Cell Sci 2022 Mar 01;135(5)","abstract":"Congenital disorders of glycosylation type I (CDG-I) are inherited human diseases caused by deficiencies in lipid-linked oligosaccharide (LLO) synthesis or the glycan transfer to proteins during N-glycosylation. We constructed a platform of 16 Schizosaccharomyces pombe strains that synthesize all possible theoretical combinations of LLOs containing three to zero glucose (Glc) residues and nine to five mannose (Man) residues. The occurrence of unexpected LLOs suggested the requirement of specific Man residues for glucosyltransferase activities. We then quantified protein hypoglycosylation in each strain and found that in S. pombe the presence of Glc in the LLO is more relevant to the transfer efficiency than the number of Man residues. Surprisingly, a decrease in the number of Man residues in glycans somehow improved the glycan transfer. The most severe hypoglycosylation was produced in cells that synthesized LLOs completely lacking Glc and having a high number of Man residues. This deficiency could be reverted by expressing a single-subunit oligosaccharyltransferase with a broad range of substrate specificity. Our work shows the usefulness of this new S. pombe set of mutants as a platform to model the molecular bases of human CDG-I diseases. This article has an associated First Person interview with the first authors of the paper.","doi":"10.1242/jcs.259167","authors":"Gallo GL, Valko A, Herrera Aguilar N, Weisz AD, D'Alessio C","authors_abbrev":"Gallo GL et al.","pubmed_publication_date":"01 Mar 2022","pubmed_entrez_date":"2021-12-01","publication_year":"2022","canto_session_key":"2887815629698aa3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Giovanna Gallo","canto_first_approved_date":"2025-07-02 09:52:51","canto_approved_date":"2025-07-02 09:52:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-25 08:05:14","canto_added_date":"2021-12-03 01:15:04","annotation_curators":[{"name":"Giovanna Gallo","community_curator":true,"annotation_count":31,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.07","SPBC342.01c","SPAC56F8.06c","SPBC1734.12c","SPAC7D4.06c","SPAC1834.05"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2025-07-02"},{"uniquename":"PMID:12234926","title":"Fission yeast Mor2/Cps12, a protein similar to Drosophila Furry, is essential for cell morphogenesis and its mutation induces Wee1-dependent G(2) delay.","citation":"EMBO J 2002 Sep 16;21(18):4863-74","abstract":"Fission yeast cells identify growing regions at the opposite ends of the cell, producing the rod-like shape. The positioning of the growth zone(s) and the polarized growth require CLIP170-like protein Tip1 and the Ndr kinase Orb6, respectively. Here, we show that the mor2/cps12 mutation disrupts the localization of F-actin at the cell ends, producing spherical cells and concomitantly inducing a G(2) delay at 36 degrees C. Mor2 is important for the localization of F-actin at the cell end(s) but not at the medial region, and is essential for the restriction of the growth zone(s) where Tip1 targets. Mor2 is homologous to the Drosophila Furry protein, which is required to maintain the integrity of cellular extensions, and is localized at both cell ends and the medial region of the cell in an actin-dependent fashion. Cellular localization of Mor2 and Orb6 was interdependent. The tyrosine kinase Wee1 is necessary for the G(2) delay and maintenance of viability of the mor2 mutant. These results indicate that Mor2 plays an essential role in cell morphogenesis in concert with Orb6, and the mutation activates the mechanism coordinating morphogenesis with cell cycle progression.","authors":"Hirata D, Kishimoto N, Suda M, Sogabe Y, Nakagawa S, Yoshida Y, Sakai K, Mizunuma M, Miyakawa T, Ishiguro J, Toda T","authors_abbrev":"Hirata D et al.","pubmed_publication_date":"16 Sep 2002","pubmed_entrez_date":"2002-09-18","publication_year":"2002","canto_session_key":"81b8cfb37d11fd46","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-17 14:49:27","canto_approved_date":"2021-03-26 16:48:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-17 14:49:01","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.12","SPAC4A8.15c","SPBC26H8.07c","SPBP19A11.04c","SPAC821.12","SPBC21.06c","SPCC18B5.03"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-08-17"},{"uniquename":"PMID:18563926","title":"Phosphorylation-specific MS/MS scoring for rapid and accurate phosphoproteome analysis.","citation":"J Proteome Res 2008 Aug;7(8):3373-81","abstract":"The promise of mass spectrometry as a tool for probing signal-transduction is predicated on reliable identification of post-translational modifications. Phosphorylations are key mediators of cellular signaling, yet are hard to detect, partly because of unusual fragmentation patterns of phosphopeptides. In addition to being accurate, MS/MS identification software must be robust and efficient to deal with increasingly large spectral data sets. Here, we present a new scoring function for the Inspect software for phosphorylated peptide tandem mass spectra for ion-trap instruments, without the need for manual validation. The scoring function was modeled by learning fragmentation patterns from 7677 validated phosphopeptide spectra. We compare our algorithm against SEQUEST and X!Tandem on testing and training data sets. At a 1% false positive rate, Inspect identified the greatest total number of phosphorylated spectra, 13% more than SEQUEST and 39% more than X!Tandem. Spectra identified by Inspect tended to score better in several spectral quality measures. Furthermore, Inspect runs much faster than either SEQUEST or X!Tandem, making desktop phosphoproteomics feasible. Finally, we used our new models to reanalyze a corpus of 423,000 LTQ spectra acquired for a phosphoproteome analysis of Saccharomyces cerevisiae DNA damage and repair pathways and discovered 43% more phosphopeptides than the previous study.","doi":"10.1021/pr800129m","authors":"Payne SH, Yau M, Smolka MB, Tanner S, Zhou H, Bafna V","authors_abbrev":"Payne SH et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-06-20","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3194197","title":"The sequence of U3 from Schizosaccharomyces pombe suggests structural divergence of this snRNA between metazoans and unicellular eukaryotes.","citation":"Nucleic Acids Res 1988 Nov 11;16(21):10131-52","abstract":"We have cloned and sequenced one of the two genes encoding a 255 nucleotide small nuclear RNA from the fission yeast Schizosaccharomyces pombe. Based on the presence of four regions of primary sequence conservation and a predicted secondary structure similar to that previously proposed for human U3, we conclude that this molecule is the fission yeast homologue of this mammalian snRNA. The 5' one-third of fission yeast U3 is, however, unable to form a single stable hairpin as proposed for this region of the human RNA, but rather folds into two stem-loop structures. By analogy to fission yeast U3, we propose revised secondary structures containing two hairpins for this portion of the U3-like snRNAs from Saccharomyces cerevisiae and Dictyostelium discoideum. Thus, our data suggest that the structure of U3 snRNA has diverged in lower and higher eukaryotes.","authors":"Porter GL, Brennwald PJ, Holm KA, Wise JA","authors_abbrev":"Porter GL et al.","pubmed_publication_date":"11 Nov 1988","pubmed_entrez_date":"1988-11-11","publication_year":"1988","canto_session_key":"cc00984f3fa095dc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-06-19 15:40:34","canto_approved_date":"2025-10-09 13:10:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-19 15:40:29","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.02","SPSNRNA.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-19"},{"uniquename":"PMID:35940128","title":"Queuosine salvage in fission yeast by Qng1-mediated hydrolysis to queuine.","citation":"Biochem Biophys Res Commun 2022 Oct 08;624:146-150","abstract":"Queuosine (Q) is a hypermodified 7-deaza-guanosine nucleoside that is found at position 34, also known as the wobble position, of tRNAs with a GUN anticodon, and Q ensures faithful translation of the respective C- and U-ending codons. While Q is present in tRNAs in most eukaryotes, only bacteria can synthesize it denovo. In contrast, eukaryotes rely on external sources like their food and the gut microbiome in order to Q-modify their tRNAs, and Q therefore can be regarded as a micronutrient. The eukaryotic tRNA guanine transglycosylase (eTGT) uses the base queuine (q) as a substrate to replace G34 by Q in the tRNAs. Eukaryotic cells can uptake both q and Q, raising the question how the Q nucleoside is converted to q for incorporation into the tRNAs. Here, we identified Qng1 (also termed Duf2419) as a queuosine nucleoside glycosylase in Schizosaccharomyces pombe. S. pombe cells with a deletion of qng1 +  contained Q-modified tRNAs only when cultured in the presence of the nucleobase q, but not with the nucleoside Q, indicating that the cells are proficient at q incorporation, but not in Q hydrolysis. Furthermore, purified recombinant Qng1 hydrolyzed Q to q in vitro. Qng1 displays homology to DNA glycosylases and has orthologs across eukaryotes, including flies, mice and humans. Qng1 therefore plays an essential role in allowing eukaryotic cells to salvage Q from bacterial sources and to recycle Q from endogenous tRNAs.","doi":"10.1016/j.bbrc.2022.07.104","authors":"Patel BI, Heiss M, Samel-Pommerencke A, Carell T, Ehrenhofer-Murray AE","authors_abbrev":"Patel BI et al.","pubmed_publication_date":"08 Oct 2022","pubmed_entrez_date":"2022-08-08","publication_year":"2022","canto_session_key":"33c9bd391789a775","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ann Ehrenhofer-Murray","canto_first_approved_date":"2022-08-17 17:08:53","canto_approved_date":"2025-05-28 10:10:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-08-19 19:16:50","canto_added_date":"2022-08-10 00:15:04","annotation_curators":[{"name":"Ann Ehrenhofer-Murray","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC589.05c","SPAC17G8.02","SPBC1683.06c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2022-08-17"},{"uniquename":"PMID:20075862","title":"Lifespan extension by calorie restriction relies on the Sty1 MAP kinase stress pathway.","citation":"EMBO J 2010 Mar 03;29(5):981-91","abstract":"Either calorie restriction, loss-of-function of the nutrient-dependent PKA or TOR/SCH9 pathways, or activation of stress defences improves longevity in different eukaryotes. However, the molecular links between glucose depletion, nutrient-dependent pathways and stress responses are unknown. Here, we show that either calorie restriction or inactivation of nutrient-dependent pathways induces lifespan extension in fission yeast, and that such effect is dependent on the activation of the stress-dependent Sty1 mitogen-activated protein (MAP) kinase. During transition to stationary phase in glucose-limiting conditions, Sty1 becomes activated and triggers a transcriptional stress programme, whereas such activation does not occur under glucose-rich conditions. Deletion of the genes coding for the SCH9-homologue, Sck2 or the Pka1 kinases, or mutations leading to constitutive activation of the Sty1 stress pathway increase lifespan under glucose-rich conditions, and importantly such beneficial effects depend ultimately on Sty1. Furthermore, cells lacking Pka1 display enhanced oxygen consumption and Sty1 activation under glucose-rich conditions. We conclude that calorie restriction favours oxidative metabolism, reactive oxygen species production and Sty1 MAP kinase activation, and this stress pathway favours lifespan extension.","doi":"10.1038/emboj.2009.407","authors":"Zuin A, Carmona M, Morales-Ivorra I, Gabrielli N, Vivancos AP, Ayté J, Hidalgo E","authors_abbrev":"Zuin A et al.","pubmed_publication_date":"03 Mar 2010","pubmed_entrez_date":"2010-01-16","publication_year":"2010","canto_session_key":"2d3035d3cfa925ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elena Hidalgo","canto_first_approved_date":"2018-10-31 16:33:46","canto_approved_date":"2024-03-28 15:21:02","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-07-05 14:55:24","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Elena Hidalgo","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC24B11.06c","SPAC22E12.14c","SPBC32F12.03c","SPBC106.10","SPBC409.07c","SPAC26F1.10c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-10-31"},{"uniquename":"PMID:37259828","title":"The cytoplasmic tail of the mechanosensitive channel Pkd2 regulates its internalization and clustering in eisosomes.","citation":"J Cell Sci 2023 Jun 15;136(12)","abstract":"Polycystins are a family of conserved ion channels, mutations of which lead to one of the most common human genetic disorders, namely, autosomal dominant polycystic kidney disease. Schizosacchromyces pombe possesses an essential polycystin homologue, Pkd2, which directs Ca2+ influx on the cell surface in response to membrane tension, but its structure remains unsolved. Here, we analyzed the structure-function relationship of Pkd2 based on its AlphaFold-predicted structure. Pkd2 consists of three domains, the extracellular lipid-binding domain (LBD), nine-helix transmembrane domain (TMD) and C-terminal cytoplasmic domain (CCD). Our genetic and microscopy data revealed that LBD and TMD are essential for targeting Pkd2 to the plasma membrane from the endoplasmic reticulum. In comparison, CCD ensures the polarized distribution of Pkd2 by promoting its internalization and preventing its clustering in the eisosome, a caveolae-like membrane compartment. The domains of Pkd2 and their functions are conserved in other fission yeast species. We conclude that both extracellular and cytoplasmic domains of Pkd2 are crucial for its intracellular trafficking and function. We propose that mechanosensitive channels can be desensitized through either internalization or clustering in low-tension membrane compartments.","doi":"10.1242/jcs.260598","authors":"Malla M, Sinha D, Chowdhury P, Bisesi BT, Chen Q","authors_abbrev":"Malla M et al.","pubmed_publication_date":"15 Jun 2023","pubmed_entrez_date":"2023-06-01","publication_year":"2023","canto_session_key":"9a3b3bfbe73e2390","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-06-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10545449","title":"Fission yeast mutants that alleviate transcriptional silencing in centromeric flanking repeats and disrupt chromosome segregation.","citation":"Genetics 1999 Nov;153(3):1153-69","abstract":"In the fission yeast Schizosaccharomyces pombe genes are transcriptionally silenced when placed within centromeres, within or close to the silent mating-type loci or adjacent to telomeres. Factors required to maintain mating-type silencing also affect centromeric silencing and chromosome segregation. We isolated mutations that alleviate repression of marker genes in the inverted repeats flanking the central core of centromere I. Mutations csp1 to 13 (centromere: suppressor of position effect) defined 12 loci. Ten of the csp mutants have no effect on mat2/3 or telomere silencing. All csp mutants allow some expression of genes in the centromeric flanking repeat, but expression in the central core is undetectable. Consistent with defective centromere structure and function, chromosome loss rates are elevated in all csp mutants. Mutants csp1 to 6 are temperature-sensitive lethal and csp3 and csp6 cells are defective in mitosis at 36 degrees. csp7 to 13 display a high incidence of lagging chromosomes on late anaphase spindles. Thus, by screening for mutations that disrupt silencing in the flanking region of a fission yeast centromere a novel collection of mutants affecting centromere architecture and chromosome segregation has been isolated.","authors":"Ekwall K, Cranston G, Allshire RC","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-11-05","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19243310","title":"Identification of a conserved F-box protein 6 interactor essential for endocytosis and cytokinesis in fission yeast.","citation":"Biochem J 2009 May 13;420(2):169-77","abstract":"The F-box domain is a degenerated motif consisting of approximately 40 amino acid residues that specifically bind Skp1, a core component of the SCF (Skp1-Cdc53/Cullin 1-F-box protein) ubiquitin ligase. Recent work, mainly performed in budding yeast, indicates that certain F-box proteins form non-SCF complexes together with Skp1 in the absence of cullins and play various roles in cell cycle and signalling pathways. However, it is not established whether these non-SCF complexes are unique to budding yeast or common in other eukaryotes. In the present paper, using TAP (tandem affinity purification) coupled to MudPIT (Multidimensional Protein Identification Technology) analysis, we have identified a novel conserved protein, Sip1, in fission yeast, as an interacting partner of an essential F-box protein Pof6. Sip1 is a large HEAT (huntingtin, elongation factor 3, the PR65/A subunit of protein phosphatase 2A and the lipid kinase Tor)-repeats containing protein (217 kDa) and forms a complex with Pof6 and Skp1. This complex does not contain cullins, indicating that it is a novel non-SCF complex. Like Pof6 and Skp1, Sip1 is essential for cell viability and temperature-sensitive sip1 mutants display cell division arrest as binucleate cells with septa. Sip1 localizes to the nucleus and dynamic cytoplasmic dots, which are shown in the present study to be endocytic vesicles. Consistent with this, sip1 mutants are defective in endocytosis. Furthermore, towards the end of cytokinesis, constriction of the actomyosin ring and dissociation of type II myosin and septum materials are substantially delayed in the absence of functional Sip1. These results indicate that the conserved Sip1 protein comprises a novel non-SCF F-box complex that plays an essential role in endocytosis, cytokinesis and cell division.","doi":"10.1042/BJ20081659","authors":"Jourdain I, Spielewoy N, Thompson J, Dhut S, Yates JR, Toda T","authors_abbrev":"Jourdain I et al.","pubmed_publication_date":"13 May 2009","pubmed_entrez_date":"2009-02-27","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC27B12.08","SPBC409.05","SPCC18.04"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:9802209","title":"Molecular cloning and sequence analysis of the Schizosaccharomyces pombe ade10+ gene.","citation":"Yeast 1998 Oct;14(14):1307-10","abstract":"We have cloned and sequenced the Schizosaccharomyces pombe ade10 gene encoding 5-phosphoribosyl-4-carboxamide 5-aminoimidazole transformylase inosine monophosphate cyclohydrolase. The sequence has an uninterrupted open reading frame of 1755 nucleotides corresponding to 585 amino acid residues. The deduced amino acid sequence shows a high degree of similarity to the purH gene product of many species, including Saccharomyces cerevisiae, human, chicken and Escherichia coli. Moreover our data indicate that intrachromosomal recombination in Schiz. pombe is enhanced if the ade10 gene product is defective.","authors":"Liedtke C, Schmidt H","authors_abbrev":"Liedtke C et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-11-05","publication_year":"1998","canto_session_key":"c56d4e90dd925805","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-30 10:30:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-30 10:27:35","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCPB16A4.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-30"},{"uniquename":"PMID:30973898","title":"Mal3 is a multi-copy suppressor of the sensitivity to microtubule-depolymerizing drugs and chromosome mis-segregation in a fission yeast pka1 mutant.","citation":"PLoS One 2019;14(4):e0214803","abstract":"The cAMP-dependent protein kinase Pka1 is known as a regulator of glycogenesis, transition into meiosis, chronological aging, and stress responses in the fission yeast, Schizosaccharomyces pombe. We demonstrated here that Pka1 is responsible for normal growth in the presence of the microtubule-destabilization drug TBZ and proper chromosome segregation. The deletion of the pka1 gene resulted in the TBZ-sensitive phenotype and chromosome mis-segregation. We isolated the mal3 gene as a multi-copy suppressor of the TBZ-sensitive phenotype in the pka1Δ strains. Overexpression of the CH domain (1-143) or the high-affinity microtubule binding mutant (1-143 Q89R) of Mal3 rescued the TBZ-sensitive phenotype in the pka1Δ and mal3Δ strains, while the EB1 domain (135-308) and the mutants defective in microtubule binding (1-143 Q89E) failed to do so in the same strains. Chromosome mis-segregation caused by TBZ in the pka1Δ or mal3Δ strains was suppressed by the overexpression of the Mal3 CH domain (1-143), Mal3 CH domain with the coiled-coil domain (1-197), or full-length Mal3. Overexpression of EB1 orthologs from Saccharomyces cerevisiae, Arabidopsis thaliana, Mus musculus, or Homo sapiens suppressed the TBZ-sensitive phenotype in the pka1Δ strains, indicating their conserved functions. These findings suggest that Pka1 and the microtubule binding of the Mal3 CH domain play a role in the maintenance of proper chromosome segregation.","doi":"10.1371/journal.pone.0214803","authors":"Tanabe T, Yamaga M, Kawamukai M, Matsuo Y","authors_abbrev":"Tanabe T et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-04-12","publication_year":"2019","canto_session_key":"9df2954cb30abd20","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Matsuo","canto_first_approved_date":"2019-04-24 16:21:33","canto_approved_date":"2026-05-13 14:42:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-04-17 01:58:08","canto_added_date":"2019-04-13 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yasuhiro Matsuo","community_curator":true,"annotation_count":36,"orcid":"0000-0002-2858-7179","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPAC8C9.03","SPAC3C7.12","SPBC106.10","SPBC19C7.03","SPBC1604.20c","SPAC890.02c","SPCC895.07","SPCC1223.06"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2019-04-24"},{"uniquename":"PMID:17222800","title":"Characterization and functional analysis of a novel double-guide C/D box snoRNA in the fission yeast.","citation":"Biochem Biophys Res Commun 2007 Mar 02;354(1):302-8","abstract":"Ribose methylation of eukaryotic rRNA is directed by box C/D small nucleolar RNAs (snoRNAs), which pinpoint the nucleotide to be methylated in specific position within the rRNA sequence. Here, we report the identification of a novel double-guide C/D box snoRNA termed snR88 that directs methylation of two previously undetermined sites in 25S rRNA from the fission yeast. Knockout of the predicted TATA box of the snR88 gene resulted in the complete blocking of its expression, showing that snR88 is an independently transcribed gene and dispensable for yeast viability. The depletion of snR88 abolished 25S rRNA methylation at U2304 and U2497 simultaneously. Interestingly, an unusual pause of reverse transcription at U2495 was observed, which implies an unknown structure of 25S rRNA related to ribose methylation at U2497 in the fission yeast.","authors":"Bi YZ, Qu LH, Zhou H","authors_abbrev":"Bi YZ et al.","pubmed_publication_date":"02 Mar 2007","pubmed_entrez_date":"2007-01-16","publication_year":"2007","canto_session_key":"e9b6581da99a35cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 16:25:51","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-28 15:11:30","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNORNA.53"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-28"},{"uniquename":"PMID:17277362","title":"Brc1-mediated rescue of Smc5/6 deficiency: requirement for multiple nucleases and a novel Rad18 function.","citation":"Genetics 2007 Apr;175(4):1585-95","abstract":"Smc5/6 is a structural maintenance of chromosomes complex, related to the cohesin and condensin complexes. Recent studies implicate Smc5/6 as being essential for homologous recombination. Each gene is essential, but hypomorphic alleles are defective in the repair of a diverse array of lesions. A particular allele of smc6 (smc6-74) is suppressed by overexpression of Brc1, a six-BRCT domain protein that is required for DNA repair during S-phase. This suppression requires the postreplication repair (PRR) protein Rhp18 and the structure-specific endonucleases Slx1/4 and Mus81/Eme1. However, we show here that the contribution of Rhp18 is via a novel pathway that is independent of PCNA ubiquitination and PRR. Moreover, we identify Exo1 as an additional nuclease required for Brc1-mediated suppression of smc6-74, independent of mismatch repair. Further, the Apn2 endonuclease is required for the viability of smc6 mutants without extrinsic DNA damage, although this is not due to a defect in base excision repair. Several nucleotide excision repair genes are similarly shown to ensure viability of smc6 mutants. The requirement for excision factors for the viability of smc6 mutants is consistent with an inability to respond to spontaneous lesions by Smc5/6-dependent recombination.","authors":"Lee KM, Nizza S, Hayes T, Bass KL, Irmisch A, Murray JM, O'Connell MJ","authors_abbrev":"Lee KM et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-02-06","publication_year":"2007","canto_session_key":"2874cbc5bcdadd84","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-03-31 15:43:49","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-03-31 15:43:31","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":70,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.06","SPBC16A3.11","SPBC29A10.05","SPBC1734.06","SPAC3G6.06c","SPAC12B10.12c","SPCC553.07c","SPBC649.03","SPBC3D6.10","SPBC582.05c","SPBC4F6.15c","SPBC16D10.09","SPAC688.10","SPAPB24D3.04c","SPAC30D11.07"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2016-03-31"},{"uniquename":"PMID:40931936","title":"Oligomerization and exocyst coupling underlie Spa2-mediated focusing of polarized growth in fission yeast.","citation":"J Cell Sci 2025 Sep 01;138(17)","abstract":"Polarized cell growth in fungi requires the spatial restriction of exocytosis to discrete cortical domains. Defined by a characteristic domain architecture, the evolutionarily conserved scaffold protein Spa2 localizes to sites of polarized growth in fungi and has been implicated in morphogenic processes including hyphal extension in filamentous fungi and budding yeast mating. Schizosaccharomyces pombe is a well-studied and powerful model organism for elucidating mechanisms of polarized growth. However, identifying a role for Spa2 in S. pombe morphogenesis has been elusive, highlighting a gap in defining a broadly conserved Spa2 function. Here, we undertook a comprehensive and comparative dissection of the targeting mechanisms, interactome and function of Spa2 in S. pombe. We find that all of the conserved domains in Spa2 influence Spa2 localization to sites of polarized growth in an exocyst-dependent and largely cytoskeleton-independent manner. At cell tips, stable complexes of oligomerized Spa2 contribute to constraining the growth zone, in part by delivering the Rab GTPase-activating protein for the Sec4 homolog Ypt2. Despite species-specific wiring of Spa2 protein networks, our results underscore an evolutionarily conserved role for Spa2 in sharpening the spatial focus of polarized growth.","doi":"10.1242/jcs.264071","authors":"Ren L, Willet AH, Gould KL","authors_abbrev":"Ren L et al.","pubmed_publication_date":"01 Sep 2025","pubmed_entrez_date":"2025-09-11","publication_year":"2025","canto_session_key":"ab49b41515f67754","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2025-12-11 16:59:34","canto_approved_date":"2026-02-16 16:33:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-12-01 17:41:20","canto_added_date":"2025-09-11 23:25:05","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":40,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.16","SPAC821.12","SPAC3G9.05","SPAC9E9.07c","SPBC106.20","SPAC19G12.14","SPCC4G3.09c","SPAC17G8.12","SPAC16E8.08"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2025-12-11"},{"uniquename":"PMID:17332498","title":"Modulation of cell cycle-specific gene expressions at the onset of S phase arrest contributes to the robust DNA replication checkpoint response in fission yeast.","citation":"Mol Biol Cell 2007 May;18(5):1756-67","abstract":"Fission yeast replication checkpoint kinases Rad3p and Cds1p are essential for maintaining cell viability after transient treatment with hydroxyurea (HU), an agent that blocks DNA replication. Although current studies have focused on the cyclin-dependent protein kinase Cdc2p that is regulated by these checkpoint kinases, other aspects of their functions at the onset of S phase arrest have not been fully understood. In this study, we use genome-wide DNA microarray analyses to show that HU-induced change of expression profiles in synchronized G(2) cells occurs specifically at the onset of S phase arrest. Induction of many core environmental stress response genes and repression of ribosomal genes happen during S phase arrest. Significantly, peak expression level of the MluI-like cell cycle box (MCB)-cluster (G(1)) genes is maintained at the onset of S phase arrest in a Rad3p- and Cds1p-dependent manner. Expression level maintenance of the MCB-cluster is mediated through the accumulation of Rep2p, a putative transcriptional activator of the MBF complex. Conversely, the FKH-cluster (M) genes are repressed during the onset of S phase arrest in a Rad3p-dependent manner. Repression of the FKH-cluster genes is mediated through the decreased levels of one of the putative forkhead transcription factors, Sep1p, but not Fkh2p. Together, our results demonstrate that Rad3p and Cds1p modulate transcriptional response during the onset of S phase arrest.","authors":"Chu Z, Li J, Eshaghi M, Peng X, Karuturi RK, Liu J","authors_abbrev":"Chu Z et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-03-03","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17452359","title":"The 1.4-A crystal structure of the S. pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme.","citation":"Nucleic Acids Res 2007;35(9):3153-64","abstract":"Deadenylation is the first and probably also rate-limiting step of controlled mRNA decay in eukaryotes and therefore central for the overall rate of gene expression. In yeast, the process is maintained by the mega-Dalton Ccr4-Not complex, of which both the Ccr4p and Pop2p subunits are 3'-5' exonucleases potentially responsible for the deadenylation reaction. Here, we present the crystal structure of the Pop2p subunit from Schizosaccharomyces pombe determined to 1.4 A resolution and show that the enzyme is a competent ribonuclease with a tunable specificity towards poly-A. In contrast to S. cerevisiae Pop2p, the S. pombe enzyme contains a fully conserved DEDDh active site, and the high resolution allows for a detailed analysis of its configuration, including divalent metal ion binding. Functional data further indicates that the identity of the ions in the active site can modulate both activity and specificity of the enzyme, and finally structural superposition of single nucleotides and poly-A oligonucleotides provide insight into the catalytic cycle of the protein.","authors":"Jonstrup AT, Andersen KR, Van LB, Brodersen DE","authors_abbrev":"Jonstrup AT et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-04-25","publication_year":"2007","canto_session_key":"4309db72789d2e45","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-09-12 13:00:13","canto_approved_date":"2022-11-07 11:53:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-12 13:00:02","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-12","pdb_entries":[{"pdb_id":"2p51","gene_chains":[{"gene_uniquename":"SPCC18.06c","chain":"A","position":"4-335"}],"title":"Crystal structure of the S. pombe Pop2p deadenylation subunit","entry_authors":"Thyssen Jonstrup A,Andersen KR,Van LB,Brodersen DE","entry_authors_abbrev":"Thyssen Jonstrup A et al.","reference_uniquename":"PMID:17452359","experimental_method":"X-ray","resolution":"1.4"}]},{"uniquename":"PMID:18202361","title":"Examination of interchromosomal interactions in vegetatively growing diploid Schizosaccharomyces pombe cells by Cre/loxP site-specific recombination.","citation":"Genetics 2008 Jan;178(1):99-112","abstract":"The probability with which different regions of a genome come in contact with one another is a question of general interest. The current study addresses this subject for vegetatively growing diploid cells of fission yeast Schizosaccharomyces pombe by application of the Cre/loxP site-specific recombination assay. High levels of allelic interactions imply a tendency for chromosomes to be colocalized along their lengths. Significant homology-dependent pairing at telomere proximal loci and robust nonspecific clustering of centromeres appear to be the primary determinants of this feature. Preference for direct homolog-directed interactions at interstitial chromosomal regions was ambiguous, perhaps as a consequence of chromosome flexibility and the constraints and dynamic nature of the nucleus. Additional features of the data provide evidence for chromosome territories and reveal an intriguing phenomenon in which interaction frequencies are favored for nonhomologous loci that are located at corresponding relative (rather than absolute) positions within their respective chromosome arms. The latter feature, and others, can be understood as manifestations of transient, variable, and/or occasional nonspecific telomeric associations. We discuss the factors whose interplay sets the probabilities of chromosomal interactions in this organism and implications of the inferred organization for ectopic recombination.","doi":"10.1534/genetics.107.082826","authors":"Molnar M, Kleckner N","authors_abbrev":"Molnar M et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2008-01-19","publication_year":"2008","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7045651","title":"Mutations induced by X-rays and UV radiation during the nuclear cell cycle in the yeast Schizosaccharomyces pombe.","citation":"Mutat Res 1982 Feb 22;92(1-2):39-47","abstract":"The availability of a cell-division-cycle (cdc) mutant in the fission yeast S. pombe, wee 1-50, has made possible the production of a large population of G1 nuclear-stage synchronized cells. During their development, yeast cells from the G1 into the G2 nuclear stages were treated with X-rays and UV radiation at various doses. The DNA pre-replicative and replicative phases were the most sensitive to both cell lethality and mutant induction with either X-rays or UV radiation. The trends of induced biological effects that were observed suggest that the induction of mutations is dependent on the number of unrepaired DNA lesions that reach the replicating fork or of those that occur at that time. The X-ray-induced mutations were earlier saturated, possibly because of the higher number of lethal lesions so induced.","authors":"Barale R, Rusciano D, Loprieno N","authors_abbrev":"Barale R et al.","pubmed_publication_date":"22 Feb 1982","pubmed_entrez_date":"1982-02-22","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000110","title":"Gene Ontology annotation of Drosophila melanogaster nuclear genes encoding proteins targeted to the mitochondrion.","abstract":"Gene Ontology annotation of Drosophila melanogaster nuclear genes encoding proteins targeted to the mitochondrion based on analysis by MitoDrome (http://mitodrome.ba.itb.cnr.it/) by comparison of human mitochondrial proteins available in SWISSPROT vs. the Drosophila genome, ESTs and cDNA sequences available in the FlyBase database (PMID:12520013).","authors":"FlyBase","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9191274","title":"Pro-sequence removal is not sufficient for activation of the kexin Krp1.","citation":"Biochem Soc Trans 1997 May;25(2):230S","abstract":"","authors":"Powner D, Davey J","authors_abbrev":"Powner D et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"64f7cb8bd028f4bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:48:45","canto_session_submitted_date":"2012-02-27 11:07:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:22042620","title":"Brr6 drives the Schizosaccharomyces pombe spindle pole body nuclear envelope insertion/extrusion cycle.","citation":"J Cell Biol 2011 Oct 31;195(3):467-84","abstract":"The fission yeast interphase spindle pole body (SPB) is a bipartite structure in which a bulky cytoplasmic domain is separated from a nuclear component by the nuclear envelope. During mitosis, the SPB is incorporated into a fenestra that forms within the envelope during mitotic commitment. Closure of this fenestra during anaphase B/mitotic exit returns the cytoplasmic component to the cytoplasmic face of an intact interphase nuclear envelope. Here we show that Brr6 is transiently recruited to SPBs at both SPB insertion and extrusion. Brr6 is required for both SPB insertion and nuclear envelope integrity during anaphase B/mitotic exit. Genetic interactions with apq12 and defective sterol assimilation suggest that Brr6 may alter envelope composition at SPBs to promote SPB insertion and extrusion. The restriction of the Brr6 domain to eukaryotes that use a polar fenestra in an otherwise closed mitosis suggests a conserved role in fenestration to enable a single microtubule organizing center to nucleate both cytoplasmic and nuclear microtubules on opposing sides of the nuclear envelope.","doi":"10.1083/jcb.201106076","authors":"Tamm T, Grallert A, Grossman EP, Alvarez-Tabares I, Stevens FE, Hagan IM","authors_abbrev":"Tamm T et al.","pubmed_publication_date":"31 Oct 2011","pubmed_entrez_date":"2011-11-02","publication_year":"2011","canto_session_key":"42ad3cde8bd52174","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-06-25 14:41:46","canto_approved_date":"2025-12-08 18:42:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-25 14:39:11","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1786.03","SPBC428.04","SPBC649.05","SPBC12D12.01","SPCC1682.04","SPBC947.12","SPAC3A11.05c","SPAC8F11.06"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2020-06-25"},{"uniquename":"PMID:29694899","title":"To Make a Long Spindle Short: Nuclear Envelope Breakdown during Meiosis.","citation":"Cell Rep 2018 Apr 24;23(4):931-932","abstract":"In fission yeast, the nuclear envelope (NE) remains intact during mitosis and meiosis I but is compromised during meiosis II. In this issue of Cell Reports, Flor-Parra et al. (2018) demonstrate that this NE alteration regulates meiosis II spindle disassembly and the ploidy of meiotic products.","doi":"10.1016/j.celrep.2018.04.030","authors":"Varberg JM, Jaspersen SL","authors_abbrev":"Varberg JM et al.","pubmed_publication_date":"24 Apr 2018","pubmed_entrez_date":"2018-04-26","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-04-27 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007398","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38068960","title":"Novel  COX11  Mutations Associated with Mitochondrial Disorder: Functional Characterization in Patient Fibroblasts and  Saccharomyces cerevisiae .","citation":"Int J Mol Sci 2023 Nov 23;24(23)","abstract":"Genetic defects in the nuclear encoded subunits and assembly factors of cytochrome c oxidase (mitochondrial complex IV) are very rare and are associated with a wide variety of phenotypes. Biallelic pathogenic variants in the COX11 protein were previously identified in two unrelated children with infantile-onset mitochondrial encephalopathies. Through comprehensive clinical, genetic and functional analyses, here we report on a new patient harboring novel heterozygous variants in  COX11 , presenting with Leigh-like features, and provide additional experimental evidence for a direct correlation between COX11 protein expression and sensitivity to oxidative stress. To sort out the contribution of the single mutations to the phenotype, we employed a multi-faceted approach using  Saccharomyces cerevisiae  as a genetically manipulable system, and in silico structure-based analysis of human COX11. Our results reveal differential effects of the two novel  COX11  mutations on yeast growth, respiration, and cellular redox status, as well as their potential impact on human protein stability and function. Strikingly, the functional deficits observed in patient fibroblasts are recapitulated in yeast models, validating the conservation of COX11's role in mitochondrial integrity across evolutionarily distant organisms. This study not only expands the mutational landscape of COX11-associated mitochondrial disorders but also underscores the continued translational relevance of yeast models in dissecting complex molecular pathways.","doi":"10.3390/ijms242316636","authors":"Caron-Godon CA, Della Vecchia S, Romano A, Doccini S, Dal Canto F, Pasquariello R, Rubegni A, Battini R, Santorelli FM, Glerum DM, Nesti C","authors_abbrev":"Caron-Godon CA et al.","pubmed_publication_date":"23 Nov 2023","pubmed_entrez_date":"2023-12-09","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1420.04c","SPAC19B12.13"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:28143396","title":"Unsupervised detection of regulatory gene expression information in different genomic regions enables gene expression ranking.","citation":"BMC Bioinformatics 2017 Feb 01;18(1):77","abstract":"The regulation of all gene expression steps (e.g., Transcription, RNA processing, Translation, and mRNA Degradation) is known to be primarily encoded in different parts of genes and in genomic regions in proximity to genes (e.g., promoters, untranslated regions, coding regions, introns, etc.). However, the entire gene expression codes and the genomic regions where they are encoded are still unknown.\nHere, we employ an unsupervised approach to estimate the concentration of gene expression codes in different non-coding parts of genes and transcripts, such as introns and untranslated regions, focusing on three model organisms (Escherichia coli, Saccharomyces cerevisiae, and Schizosaccharomyces pombe). Our analyses support the conjecture that regions adjacent to the beginning and end of ORFs and the beginning and end of introns tend to include higher concentration of gene expression information relatively to regions further away. In addition, we report the exact regions with elevated concentration of gene expression codes. Furthermore, we demonstrate that the concentration of these codes in different genetic regions is correlated with the expression levels of the corresponding genes, and with splicing efficiency measurements and meiotic stage gene expression measurements in S. cerevisiae.\nWe suggest that these discoveries improve our understanding of gene expression regulation and evolution; they can also be used for developing improved models of genome/gene evolution and for engineering gene expression in various biotechnological and synthetic biology applications.","doi":"10.1186/s12859-017-1497-z","authors":"Zafrir Z, Tuller T","authors_abbrev":"Zafrir Z et al.","pubmed_publication_date":"01 Feb 2017","pubmed_entrez_date":"2017-02-02","publication_year":"2017","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2017-02-03 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9373147","title":"Using Schizosaccharomyces pombe as a host for expression and purification of eukaryotic proteins.","citation":"Gene 1997 Oct 24;200(1-2):135-44","abstract":"We have established a eukaryotic protein expression and purification system by using the yeast Schizosaccharomyces pombe as the host and the glutathione S-transferase (GST) as a protein purification tag. This system provides opportunities for rapid, inexpensive, and high yield production of proteins in a eukaryotic organism. Unlike E. coli, S. pombe provides for post-translational modifications of the proteins, which are often critical for the structure and function of eukaryotic proteins. Two vectors have been constructed for protein expression in S. pombe, pESP-1 and pESP-2. Both vectors use the nmt1 promoter for constitutive or induced expression of the gene of interest. Expressed GST-tagged proteins are easily and rapidly purified using glutathione agarose beads. The GST tag can be removed from the fusion proteins by treatment with either the thrombin or enterokinase protease. Proteins expressed from the pESP-2 vector will yield native amino acid sequence when the GST tag is removed by treatment with enterokinase. Nine proteins have been purified by using the system with yields ranging from 1.0 mg/l to 12.5 mg/l of induced culture.","authors":"Lu Q, Bauer JC, Greener A","authors_abbrev":"Lu Q et al.","pubmed_publication_date":"24 Oct 1997","pubmed_entrez_date":"1997-12-31","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000085","title":"Representation of cell apoptotic process as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the apoptotic process for a cell type as a biological process. The underlying equivalence axiom template is \"'apoptotic process' and 'occurs in' some C\", where C is a native cell (CL:0000003).","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28917635","title":"Evolutionary analysis of nucleosome positioning sequences based on New Symmetric Relative Entropy.","citation":"Genomics 2018 May;110(3):154-161","abstract":"New Symmetric Relative Entropy (NSRE) was applied innovatively to analyze the nucleosome sequences in S. cerevisiae, S. pombe and Drosophila. NSRE distributions could well reflect the characteristic differences of nucleosome sequences among three organisms, and the differences indicate a concerted evolution in the sequence usage of nucleosome. Further analysis about the nucleosomes around TSS shows that the constitutive property of +1/-1 nucleosomes in S. cerevisiae is different from that in S. pombe and Drosophila, which indicates that S. cerevisiae has a different transcription regulation mechanism based on nucleosome. However, in either case, the nucleosome dyad region is conserved and always has a higher NSRE. Base composition analysis shows that this conservative property in nucleosome dyad region is mainly determined by base A and T, and the dependence degrees on base A and T are consistent in three organisms.","doi":"10.1016/j.ygeno.2017.09.007","authors":"Meng H, Li H, Zheng Y, Yang Z, Jia Y, Bo S","authors_abbrev":"Meng H et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2017-09-18","publication_year":"2018","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2017-09-19 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32324744","title":"Targeting mitochondrial and cytosolic substrates of TRIT1 isopentenyltransferase: Specificity determinants and tRNA-i6A37 profiles.","citation":"PLoS Genet 2020 Apr;16(4):e1008330","abstract":"The tRNA isopentenyltransferases (IPTases), which add an isopentenyl group to N6 of A37 (i6A37) of certain tRNAs, are among a minority of enzymes that modify cytosolic and mitochondrial tRNAs. Pathogenic mutations to the human IPTase, TRIT1, that decrease i6A37 levels, cause mitochondrial insufficiency that leads to neurodevelopmental disease. We show that TRIT1 encodes an amino-terminal mitochondrial targeting sequence (MTS) that directs mitochondrial import and modification of mitochondrial-tRNAs. Full understanding of IPTase function must consider the tRNAs selected for modification, which vary among species, and in their cytosol and mitochondria. Selection is principally via recognition of the tRNA A36-A37-A38 sequence. An exception is unmodified tRNATrpCCA-A37-A38 in Saccharomyces cerevisiae, whereas tRNATrpCCA is readily modified in Schizosaccharomyces pombe, indicating variable IPTase recognition systems and suggesting that additional exceptions may account for some of the tRNA-i6A37 paucity in higher eukaryotes. Yet TRIT1 had not been characterized for restrictive type substrate-specific recognition. We used i6A37-dependent tRNA-mediated suppression and i6A37-sensitive northern blotting to examine IPTase activities in S. pombe and S. cerevisiae lacking endogenous IPTases on a diversity of tRNA-A36-A37-A38 substrates. Point mutations to the TRIT1 MTS that decrease human mitochondrial import, decrease modification of mitochondrial but not cytosolic tRNAs in both yeasts. TRIT1 exhibits clear substrate-specific restriction against a cytosolic-tRNATrpCCA-A37-A38. Additional data suggest that position 32 of tRNATrpCCA is a conditional determinant for substrate-specific i6A37 modification by the restrictive IPTases, Mod5 and TRIT1. The cumulative biochemical and phylogenetic sequence analyses provide new insights into IPTase activities and determinants of tRNA-i6A37 profiles in cytosol and mitochondria.","doi":"10.1371/journal.pgen.1008330","authors":"Khalique A, Mattijssen S, Haddad AF, Chaudhry S, Maraia RJ","authors_abbrev":"Khalique A et al.","pubmed_publication_date":"Apr 2020","pubmed_entrez_date":"2020-04-24","publication_year":"2020","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-04-25 00:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18362178","title":"Dissection of the essential steps for condensin accumulation at kinetochores and rDNAs during fission yeast mitosis.","citation":"J Cell Biol 2008 Mar 24;180(6):1115-31","abstract":"The condensin complex has a fundamental role in chromosome dynamics. In this study, we report that accumulation of Schizosaccharomyces pombe condensin at mitotic kinetochores and ribosomal DNAs (rDNAs) occurs in multiple steps and is necessary for normal segregation of the sister kinetochores and rDNAs. Nuclear entry of condensin at the onset of mitosis requires Cut15/importin alpha and Cdc2 phosphorylation. Ark1/aurora and Cut17/Bir1/survivin are needed to dock the condensin at both the kinetochores and rDNAs. Furthermore, proteins that are necessary to form the chromatin architecture of the kinetochores (Mis6, Cnp1, and Mis13) and rDNAs (Nuc1 and Acr1) are required for condensin to accumulate specifically at these sites. Acr1 (accumulation of condensin at rDNA 1) is an rDNA upstream sequence binding protein that physically interacts with Rrn5, Rrn11, Rrn7, and Spp27 and is required for the proper accumulation of Nuc1 at rDNAs. The mechanism of condensin accumulation at the kinetochores may be conserved, as human condensin II fails to accumulate at kinetochores in hMis6 RNA interference-treated cells.","doi":"10.1083/jcb.200708170","authors":"Nakazawa N, Nakamura T, Kokubu A, Ebe M, Nagao K, Yanagida M","authors_abbrev":"Nakazawa N et al.","pubmed_publication_date":"24 Mar 2008","pubmed_entrez_date":"2008-03-26","publication_year":"2008","canto_session_key":"0e41810c76efe2f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-09-14 17:09:30","canto_approved_date":"2026-01-31 15:48:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-23 21:18:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":53,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.17","SPCC962.03c","SPAC29A4.10","SPCC962.02c","SPBC409.09c","SPBP4H10.06c","SPBC17D1.04","SPAC29E6.08","SPCC970.12","SPAC1687.20c","SPCC1672.10","SPBC26H8.07c","SPBC146.03c","YMR270C","SPCC320.13c","SPBC4C3.05c","SPBC14C8.06","SPBC776.13","SPBC409.04c"],"gene_count":18,"ltp_gene_count":16,"approved_date":"2017-09-14"},{"uniquename":"PMID:11731324","title":"Cytokinesis and the contractile ring in fission yeast.","citation":"Curr Opin Microbiol 2001 Dec;4(6):713-9","abstract":"The fission yeast Schizosaccharomyces pombe provides a genetic model system for the study of cytokinesis. As in many eukaryotes, cell division in the fission yeast requires an actin-myosin-based contractile ring. Numerous components of the contractile ring that function in ring assembly, positioning and contraction have been characterized. Many of these proteins are evolutionarily conserved, suggesting that common molecular mechanisms may govern aspects of eukaryotic cell division. Recent advances in the assembly and placement of the contractile ring are discussed. In particular, major findings have been made in the characterization of myosins in cytokinesis, and in how the cell division site may be positioned by the nucleus.","authors":"Feierbach B, Chang F","authors_abbrev":"Feierbach B et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-12-04","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10634318","title":"Faithful in vitro transcription by fission yeast RNA polymerase III reveals unique alpha-amanitin sensitivity.","citation":"Gene Expr 1999;8(3):165-74","abstract":"Transcription with fission yeast (Schizosaccharomyces pombe) RNA polymerase III (pol III) was studied in two different in vitro systems. Reactions performed with isolated nuclei gave rise to 5S and pre-tRNA molecules. Because the alpha-amanitin sensitivity of that reaction clearly differed from what has been observed with pol III enzymes of other eukaryotes, a cell-free S. pombe transcription extract was developed and analyzed with the homologous 7S L RNA (srp RNA; signal recognition particle RNA) gene. Synthesis of 7S L RNA was found to be sensitive to high concentrations of alpha-amanitin, with 50% reduction seen at 400 microg/ml of the toxin. However, even with very high alpha-amanitin concentrations, exceeding 1 mg/ml, no full inhibition of the S. pombe pol III enzyme could be obtained. Together, these results demonstrate that in contrast to the yeast Saccharomyces cerevisiae, pol III from S. pombe is sensitive to high concentrations of alpha-amanitin, yet with a clearly different dose response than that observed with the corresponding RNA polymerase of higher eukaryotes. Furthermore, while the S. pombe 7S L RNA gene was efficiently transcribed in HeLa cell extracts, the human 7S L RNA gene was not actively transcribed in the S. pombe system. This finding of divergent promoter structures of both genes was verified by the analysis of 5' deletion mutants of the S. pombe 7S L RNA gene.","authors":"Rödicker F, Ossenbühl F, Michels D, Benecke BJ","authors_abbrev":"Rödicker F et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"2000-01-14","publication_year":"1999","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR013020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1D4.12"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25111393","title":"Population genomics of the fission yeast Schizosaccharomyces pombe.","citation":"PLoS One 2014;9(8):e104241","abstract":"The fission yeast Schizosaccharomyces pombe has been widely used as a model eukaryote to study a diverse range of biological processes. However, population genetic studies of this species have been limited to date, and we know very little about the evolutionary processes and selective pressures that are shaping its genome. Here, we sequenced the genomes of 32 worldwide S. pombe strains and examined the pattern of polymorphisms across their genomes. In addition to introns and untranslated regions (UTRs), intergenic regions also exhibited lower levels of nucleotide diversity than synonymous sites, suggesting that a considerable amount of noncoding DNA is under selective constraint and thus likely to be functional. A number of genomic regions showed a reduction of nucleotide diversity probably caused by selective sweeps. We also identified a region close to the end of chromosome 3 where an extremely high level of divergence was observed between 5 of the 32 strains and the remain 27, possibly due to introgression, strong positive selection, or that region being responsible for reproductive isolation. Our study should serve as an important starting point in using a population genomics approach to further elucidate the biology of this important model organism.","doi":"10.1371/journal.pone.0104241","authors":"Fawcett JA, Iida T, Takuno S, Sugino RP, Kado T, Kugou K, Mura S, Kobayashi T, Ohta K, Nakayama J, Innan H","authors_abbrev":"Fawcett JA et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-08-12","publication_year":"2014","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2014-08-13 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11294895","title":"The Schizosaccharomyces pombe spo20(+) gene encoding a homologue of Saccharomyces cerevisiae Sec14 plays an important role in forespore membrane formation.","citation":"Mol Biol Cell 2001 Apr;12(4):901-17","abstract":"The Schizosaccharomyces pombe spo20-KC104 mutation was originally isolated in a screen for sporulation-deficient mutants, and the spo20-KC104 mutant exhibits temperature-sensitive growth. Herein, we report that S. pombe, spo20(+) is essential for fission yeast cell viability and is constitutively expressed throughout the life cycle. We also demonstrate that the spo20(+) gene product is structurally homologous to Saccharomyces cerevisiae Sec14, the major phosphatidylinositol transfer protein of budding yeast. This structural homology translates to a significant degree of functional relatedness because reciprocal complementation experiments demonstrate that each protein is able to fulfill the essential function of the other. Moreover, biochemical experiments show that, like Sec14, Spo20 is a phosphatidylinositol/phosphatidylcholine-transfer protein. That Spo20 is required for Golgi secretory function in vegetative cells is indicated by our demonstration that the spo20-KC104 mutant accumulates aberrant Golgi cisternae at restrictive temperatures. However, a second phenotype observed in Spo20-deficient fission yeast is arrest of cell division before completion of cell separation. Consistent with a direct role for Spo20 in controlling cell septation in vegetatively growing cells, localization experiments reveal that Spo20 preferentially localizes to the cell poles and to sites of septation of fission yeast cells. We also report that, when fission yeasts are challenged with nitrogen starvation, Spo20 translocates to the nucleus. This nuclear localization persists during conjugation and meiosis. On completion of meiosis, Spo20 translocates to forespore membranes, and it is the assembly of forespore membranes that is abnormal in spo20-KC104 cells. In such mutants, a considerable fraction of forming prespores fail to encapsulate the haploid nucleus. Our results indicate that Spo20 regulates the formation of specialized membrane structures in addition to its recognized role in regulating Golgi secretory function.","authors":"Nakase Y, Nakamura T, Hirata A, Routt SM, Skinner HB, Bankaitis VA, Shimoda C","authors_abbrev":"Nakase Y et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-04-11","publication_year":"2001","canto_session_key":"48abddffaf7fd1e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-11-06 16:17:58","canto_approved_date":"2026-05-04 13:36:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-02 20:46:52","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H8.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-06"},{"uniquename":"PMID:11841224","title":"Functional expression of human mitochondrial CYP11B2 in fission yeast and identification of a new internal electron transfer protein, etp1.","citation":"Biochemistry 2002 Feb 19;41(7):2311-21","abstract":"Mitochondrial cytochrome P450 enzymes play a crucial role in the steroid biosynthesis in human adrenals, catalyzing regio- and stereospecific hydroxylations. In search of a new model system for the study of these enzymes, we expressed the human CYP11B2 (aldosterone synthase, P450(aldo)) in fission yeast Schizosaccharomyces pombe. Analysis of the subcellular localization of the P450 enzyme by Western blot analysis, fluorescence microscopy, and electron microscopy demonstrated that the mitochondrial localization signal of the human protein is functional in S. pombe. The transformed yeasts show the inducible ability to convert in vivo considerable amounts of 11-deoxycortisol to cortisol and 11-deoxycorticosterone to corticosterone, 18-hydroxycorticosterone, and aldosterone, respectively. Although in mammalian cells, mitochondrial steroid hydroxylases depend for their activity on an electron transport chain that consists of two proteins, adrenodoxin and adrenodoxin reductase, no coexpression of these proteins is needed for efficient substrate conversion by intact fission yeast cells. Searching the fission yeast genome for adrenodoxin homologues, a gene was identified that codes for a protein with an amino terminal domain homologous to COX15 of Saccharomyces cerevisiae and a carboxy terminal ferredoxin domain. It was found that overexpression of this gene significantly enhances steroid hydroxylase activity of CYP11B2 expressing fission yeast cells. Moreover, the bacterially expressed ferredoxin domain of this protein can replace adrenodoxin in a reconstituted steroid hydroxylation assay and transfer electrons from adrenodoxin reductase to a mammalian or a bacterial cytochrome P450. Therefore, we suggest to name this protein etp1 (electron-transfer protein 1).","authors":"Bureik M, Schiffler B, Hiraoka Y, Vogel F, Bernhardt R","authors_abbrev":"Bureik M et al.","pubmed_publication_date":"19 Feb 2002","pubmed_entrez_date":"2002-02-14","publication_year":"2002","canto_session_key":"a9061cef3d7636f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-12-18 16:51:36","canto_approved_date":"2024-01-10 14:15:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-15 15:07:08","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-12-18"},{"uniquename":"PMID:5114552","title":"Flocculation in a fission yeast: an initial step in the conjugation process.","citation":"Can J Microbiol 1971 Sep;17(9):1175-7","abstract":"","authors":"Calleja GB, Johnson BF","authors_abbrev":"Calleja GB et al.","pubmed_publication_date":"Sep 1971","pubmed_entrez_date":"1971-09-01","publication_year":"1971","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25730778","title":"Small-RNA loading licenses Argonaute for assembly into a transcriptional silencing complex.","citation":"Nat Struct Mol Biol 2015 Apr;22(4):328-35","abstract":"Argonautes and their small-RNA cofactors form the core effectors of ancient and diverse gene-silencing mechanisms whose roles include regulation of gene expression and defense against foreign genetic elements. Although Argonautes generally act within multisubunit complexes, what governs their assembly into these machineries is not well defined. Here, we show that loading of small RNAs onto Argonaute is a checkpoint for Argonaute's association with conserved GW-protein components of silencing complexes. We demonstrate that the Argonaute small interfering RNA chaperone (ARC) complex mediates loading of small RNAs onto Ago1 in Schizosaccharomyces pombe and that deletion of its subunits, or mutations in Ago1 that prevent small-RNA loading, abolish the assembly of the GW protein-containing RNA-induced transcriptional silencing (RITS) complex. Our studies uncover a mechanism that ensures that Argonaute loading precedes RITS assembly and thereby averts the formation of inert and potentially deleterious complexes.","doi":"10.1038/nsmb.2979","authors":"Holoch D, Moazed D","authors_abbrev":"Holoch D et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-03-03","publication_year":"2015","canto_session_key":"e9df66776770f8e6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-04 01:15:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13G7.07","SPCC736.11","SPBC83.03c","SPAC140.03"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:17353264","title":"Efficient RNA polyuridylation by noncanonical poly(A) polymerases.","citation":"Mol Cell Biol 2007 May;27(10):3612-24","abstract":"Nuclear poly(A) polymerase (PAP) polyadenylates nascent mRNAs, promoting their nuclear export, stability, and translation, while the related cytoplasmic polymerase GLD-2 activates translation of deadenylated mRNAs. Here we characterize the biochemical activity of fission yeast Schizosaccharomyces pombe Cid1, a putative cytoplasmic PAP implicated in cell cycle checkpoint controls. Surprisingly, Cid1 has robust poly(U) polymerase activity in vitro, especially when isolated in native multiprotein complexes. Furthermore, we found that upon S-phase arrest, the 3' ends of actin mRNAs were posttranscriptionally uridylated in a Cid1-dependent manner. Finally, Hs2 (ZCCHC6), a human ortholog of Cid1, shows similar activity. These data suggest that uridylation of mRNA forms the basis of an evolutionarily conserved mechanism of gene regulation.","authors":"Rissland OS, Mikulasova A, Norbury CJ","authors_abbrev":"Rissland OS et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-03-14","publication_year":"2007","canto_session_key":"d604bc516ecb12dc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chris Norbury","canto_first_approved_date":"2014-07-03 16:06:54","canto_approved_date":"2024-12-02 12:51:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-31 14:42:10","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Chris Norbury","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC19D5.03"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-07-03"},{"uniquename":"PMID:32814900","title":"An intramembrane chaperone complex facilitates membrane protein biogenesis.","citation":"Nature 2020 Aug;584(7822):630-634","abstract":"Integral membrane proteins are encoded by approximately 25% of all protein-coding genes 1 . In eukaryotes, the majority of membrane proteins are inserted, modified and folded at the endoplasmic reticulum (ER) 2 . Research over the past several decades has determined how membrane proteins are targeted to the ER and how individual transmembrane domains (TMDs) are inserted into the lipid bilayer 3 . By contrast, very little is known about how multi-spanning membrane proteins with several TMDs are assembled within the membrane. During the assembly of TMDs, interactions between polar or charged amino acids typically stabilize the final folded configuration 4-8 . TMDs with hydrophilic amino acids are likely to be chaperoned during the co-translational biogenesis of membrane proteins; however, ER-resident intramembrane chaperones are poorly defined. Here we identify the PAT complex, an abundant obligate heterodimer of the widely conserved ER-resident membrane proteins CCDC47 and Asterix. The PAT complex engages nascent TMDs that contain unshielded hydrophilic side chains within the lipid bilayer, and it disengages concomitant with substrate folding. Cells that lack either subunit of the PAT complex show reduced biogenesis of numerous multi-spanning membrane proteins. Thus, the PAT complex is an intramembrane chaperone that protects TMDs during assembly to minimize misfolding of multi-spanning membrane proteins and maintain cellular protein homeostasis.","doi":"10.1038/s41586-020-2624-y","authors":"Chitwood PJ, Hegde RS","authors_abbrev":"Chitwood PJ et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-08-21","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18B11.08c","SPBC2G5.01"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:37811872","title":"Detection of queuosine and queuosine precursors in tRNAs by direct RNA sequencing.","citation":"Nucleic Acids Res 2023 Nov 10;51(20):11197-11212","abstract":"Queuosine (Q) is a complex tRNA modification found in bacteria and eukaryotes at position 34 of four tRNAs with a GUN anticodon, and it regulates the translational efficiency and fidelity of the respective codons that differ at the Wobble position. In bacteria, the biosynthesis of Q involves two precursors, preQ0 and preQ1, whereas eukaryotes directly obtain Q from bacterial sources. The study of queuosine has been challenging due to the limited availability of high-throughput methods for its detection and analysis. Here, we have employed direct RNA sequencing using nanopore technology to detect the modification of tRNAs with Q and Q precursors. These modifications were detected with high accuracy on synthetic tRNAs as well as on tRNAs extracted from Schizosaccharomyces pombe and Escherichia coli by comparing unmodified to modified tRNAs using the tool JACUSA2. Furthermore, we present an improved protocol for the alignment of raw sequence reads that gives high specificity and recall for tRNAs ex cellulo that, by nature, carry multiple modifications. Altogether, our results show that 7-deazaguanine-derivatives such as queuosine are readily detectable using direct RNA sequencing. This advancement opens up new possibilities for investigating these modifications in native tRNAs, furthering our understanding of their biological function.","doi":"10.1093/nar/gkad826","authors":"Sun Y, Piechotta M, Naarmann-de Vries I, Dieterich C, Ehrenhofer-Murray AE","authors_abbrev":"Sun Y et al.","pubmed_publication_date":"10 Nov 2023","pubmed_entrez_date":"2023-10-09","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-10-09 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22553990","title":"Gene-specific requirement of RNA polymerase II CTD phosphorylation.","citation":"Mol Microbiol 2012 Jun;84(6):995-1004","abstract":"The largest subunit of RNA polymerase II, Rpb1, contains an unusual C-terminal domain (CTD) composed of numerous repeats of the YSPTSPS consensus sequence. This sequence is the target of post-translational modifications such as phosphorylation, glycosylation, methylation and transitions between stereoisomeric states, resulting in a vast combinatorial potential referred to as the CTD code. In order to gain insight into the biological significance of this code, several studies recently reported the genome-wide distribution of some of these modified polymerases and associated factors in either fission yeast (Schizosaccharomyces pombe) or budding yeast (Saccharomyces cerevisiae). The resulting occupancy maps reveal that a general RNA polymerase II transcription complex exists and undergoes uniform transitions from initiation to elongation to termination. Nevertheless, CTD phosphorylation dynamics result in a gene-specific effect on mRNA expression. In this review, we focus on the gene-specific requirement of CTD phosphorylation and discuss in more detail the case of serine 2 phosphorylation (S2P) within the CTD, a modification that is dispensable for general transcription in fission yeast but strongly affects transcription reprogramming and cell differentiation in response to environmental cues. The recent discovery of Cdk12 as a genuine CTD S2 kinase and its requirement for gene-specific expression are discussed in the wider context of metazoa.","doi":"10.1111/j.1365-2958.2012.08071.x","authors":"Drogat J, Hermand D","authors_abbrev":"Drogat J et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2012-05-05","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28485554","title":"Identification of ACA-28, a 1'-acetoxychavicol acetate analogue compound, as a novel modulator of ERK MAPK signaling, which preferentially kills human melanoma cells.","citation":"Genes Cells 2017 Jul;22(7):608-618","abstract":"The extracellular signal-regulated kinase (ERK) signaling pathway is essential for cell proliferation and is frequently deregulated in human tumors such as melanoma. Melanoma remains incurable despite the use of conventional chemotherapy; consequently, development of new therapeutic agents for melanoma is highly desirable. Here, we carried out a chemical genetic screen using a fission yeast phenotypic assay and showed that ACA-28, a synthetic derivative of 1'-acetoxychavicol acetate (ACA), which is a natural ginger compound, effectively inhibited the growth of melanoma cancer cells wherein ERK MAPK signaling is hyperactivated due to mutations in the upstream activating regulators. ACA-28 more potently inhibited the growth of melanoma cells than did the parental compound ACA. Importantly, the growth of normal human epidermal melanocytes (NHEM) was less affected by ACA-28 at the same 50% inhibitory concentration. In addition, ACA-28 specifically induced apoptosis in NIH/3T3 cells which were oncogenically transformed with human epidermal growth factor receptor-2 (HER2/ErbB2), but not in the parental cells. Notably, the ACA-28-induced apoptosis in melanoma and HER2-transformed cells was abrogated when ERK activation was blocked with a specific MEK inhibitor U0126. Consistently, ACA-28 more strongly stimulated ERK phosphorylation in melanoma cells, as compared in NHEM. ACA-28 might serve as a promising seed compound for melanoma treatment.","doi":"10.1111/gtc.12499","authors":"Satoh R, Hagihara K, Matsuura K, Manse Y, Kita A, Kunoh T, Masuko T, Moriyama M, Moriyama H, Tanabe G, Muraoka O, Sugiura R","authors_abbrev":"Satoh R et al.","pubmed_publication_date":"Jul 2017","pubmed_entrez_date":"2017-05-10","publication_year":"2017","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2017-05-11 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23628763","title":"Cuf2 boosts the transcription of APC/C activator Fzr1 to terminate the meiotic division cycle.","citation":"EMBO Rep 2013 Jun;14(6):553-60","abstract":"The number of nuclear divisions in meiosis is strictly limited to two. Although the precise mechanism remains unknown, this seems to be achieved by adjusting the anaphase-promoting complex/cyclosome (APC/C) activity to degrade cyclin. Here, we describe a fission yeast cuf2 mutant that enters into a third nuclear division cycle, represented by ectopic spindle assembly and abnormal chromosome segregation. Cuf2 is a meiotic transcription factor, and its critical target is fzr1(+)/mfr1(+), which encodes a meiotic APC/C activator. fzr1Δ also enters a third nuclear division. Thus, Cuf2 ensures termination of the M-phase cycle by boosting Fzr1 expression to generate functional gametes.","doi":"10.1038/embor.2013.52","authors":"Aoi Y, Arai K, Miyamoto M, Katsuta Y, Yamashita A, Sato M, Yamamoto M","authors_abbrev":"Aoi Y et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-05-01","publication_year":"2013","canto_session_key":"9d547e188c364e28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2019-10-11 13:42:13","canto_approved_date":"2025-09-04 10:22:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-03 13:29:12","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Masamitsu Sato","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5D6.08c","SPBC582.03","SPBC1198.12","SPCC584.02"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2019-10-11"},{"uniquename":"PMID:20821071","title":"Breeding an amylolytic yeast strain for alcoholic beverage production.","citation":"Appl Biochem Biotechnol 2011 Mar;163(6):693-706","abstract":"A starch-utilizing, yeast-like fusant was successfully created from fused protoplasts of Schizosaccharomyces pombe and Monascus anka, and the feasibility of using this fusant as a new strain for alcoholic beverage development was reported. The new fusant utilized various carbon sources more efficiently than its parent cells did. Rice koji prepared separately by cultivating the fusant and its parental strains on rice was compared to explore the effect of yeast strain on the production of α-amylase, glucoamylase, and acid protease that are crucial in wine making using cereal grains. It was found that the fusant produced greater levels of the above-mentioned enzymes than its parental strain does. Consequently, the usage of this fusant in the alcoholic fermentation of polished rice was found to reduce approximately 50% consumption of added glucoamylase than when its parental strain was used. Besides, at the end of fermentation, the fusant yeast resulted in a mash with distribution of flavor components very different from that produced by its parental strains. Thus, the fusant can be used as a new yeast strain for creating novel alcoholic beverages.","doi":"10.1007/s12010-010-9075-0","authors":"Cheng MC, Chang RC, Dent DF, Hsieh PC","authors_abbrev":"Cheng MC et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2010-09-08","publication_year":"2011","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR13357","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1706.01","HGNC:15486"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30089908","title":"Gamete fusion triggers bipartite transcription factor assembly to block re-fertilization.","citation":"Nature 2018 Aug;560(7718):397-400","abstract":"The ploidy cycle, which is integral to sexual reproduction, requires meiosis to halve chromosome numbers as well as mechanisms that ensure zygotes are formed by exactly two partners 1-4 . During sexual reproduction of the fungal model organism Schizosaccharomyces pombe, haploid P and M cells fuse to form a diploid zygote that immediately enters meiosis 5 . Here we reveal that rapid post-fusion reconstitution of a bipartite transcription factor blocks re-fertilization. We first identify mutants that undergo transient cell fusion involving cytosol exchange but not karyogamy, and show that this drives distinct cell fates in the two gametes. The P partner undergoes lethal haploid meiosis, whereas the M cell persists in mating. The zygotic transcription that drives meiosis is rapidly initiated first from the P parental genome, even in wild-type cells. This asymmetric gene expression depends on a bipartite complex formed post-fusion between the cytosolic M-cell-specific peptide Mi and the nuclear P-cell-specific homeobox protein Pi 6,7 , which captures Mi in the P nucleus. Zygotic transcription is thus poised to initiate in the P nucleus as fast as Mi reaches it after fusion, a design that we reconstruct using two synthetic interactors localized to the nucleus and the cytosol of two respective partner cells. Notably, delaying zygotic transcription-by postponing Mi expression or deleting its transcriptional target in the P genome-leads to zygotes fusing with additional gametes, thus forming polyploids and eventually aneuploid progeny. The signalling cascade to block re-fertilization shares components with, but bifurcates from, meiotic induction 8-10 . Thus, a cytoplasmic connection upon gamete fusion leads to asymmetric reconstitution of a bipartite transcription factor to rapidly block re-fertilization and induce meiosis, ensuring genome maintenance during sexual reproduction.","doi":"10.1038/s41586-018-0407-5","authors":"Vještica A, Merlini L, Nkosi PJ, Martin SG","authors_abbrev":"Vještica A et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-08-10","publication_year":"2018","canto_session_key":"46c89f342f117ca5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Aleksandar Vjestica","canto_first_approved_date":"2018-09-27 13:18:23","canto_approved_date":"2026-02-26 14:28:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-19 14:55:44","canto_added_date":"2018-08-11 00:15:04","annotation_curators":[{"name":"Aleksandar Vjestica","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPAC1F5.09c","SPBC119.04","SPBC23G7.17c","SPMTR.02","SPAC20G4.02c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-09-27"},{"uniquename":"PMID:27328748","title":"Biallelic Mutations in DNM1L are Associated with a Slowly Progressive Infantile Encephalopathy.","citation":"Hum Mutat 2016 Sep;37(9):898-903","abstract":"Mitochondria are highly dynamic organelles, undergoing continuous fission and fusion, and mitochondrial dynamics is important for several cellular functions. DNM1L is the most important mediator of mitochondrial fission, with a role also in peroxisome division. Few reports of patients with genetic defects in DNM1L have been published, most of them describing de novo dominant mutations. We identified compound heterozygous DNM1L variants in two brothers presenting with an infantile slowly progressive neurological impairment. One variant was a frame-shift mutation, the other was a missense change, the pathogenicity of which was validated in a yeast model. Fluorescence microscopy revealed abnormally elongated mitochondria and aberrant peroxisomes in mutant fibroblasts, indicating impaired fission of these organelles. In conclusion, we described a recessive disease caused by DNM1L mutations, with a clinical phenotype resembling mitochondrial disorders but without any biochemical features typical of these syndromes (lactic acidosis, respiratory chain complex deficiency) or indicating a peroxisomal disorder.","doi":"10.1002/humu.23033","authors":"Nasca A, Legati A, Baruffini E, Nolli C, Moroni I, Ardissone A, Goffrini P, Ghezzi D","authors_abbrev":"Nasca A et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-06-23","publication_year":"2016","canto_session_key":"cc4030fa41b5dc7b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-06-29 14:52:39","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-06-29 14:52:23","canto_added_date":"2016-06-29 14:51:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2016-06-29"},{"uniquename":"PMID:24196839","title":"Fission yeast tropomyosin specifies directed transport of myosin-V along actin cables.","citation":"Mol Biol Cell 2014 Jan;25(1):66-75","abstract":"A hallmark of class-V myosins is their processivity--the ability to take multiple steps along actin filaments without dissociating. Our previous work suggested, however, that the fission yeast myosin-V (Myo52p) is a nonprocessive motor whose activity is enhanced by tropomyosin (Cdc8p). Here we investigate the molecular mechanism and physiological relevance of tropomyosin-mediated regulation of Myo52p transport, using a combination of in vitro and in vivo approaches. Single molecules of Myo52p, visualized by total internal reflection fluorescence microscopy, moved processively only when Cdc8p was present on actin filaments. Small ensembles of Myo52p bound to a quantum dot, mimicking the number of motors bound to physiological cargo, also required Cdc8p for continuous motion. Although a truncated form of Myo52p that lacked a cargo-binding domain failed to support function in vivo, it still underwent actin-dependent movement to polarized growth sites. This result suggests that truncated Myo52p lacking cargo, or single molecules of wild-type Myo52p with small cargoes, can undergo processive movement along actin-Cdc8p cables in vivo. Our findings outline a mechanism by which tropomyosin facilitates sorting of transport to specific actin tracks within the cell by switching on myosin processivity.","doi":"10.1091/mbc.E13-04-0200","authors":"Clayton JE, Pollard LW, Sckolnick M, Bookwalter CS, Hodges AR, Trybus KM, Lord M","authors_abbrev":"Clayton JE et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2013-11-08","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1919.10c","SPBC32H8.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:15837517","title":"Spectrin, alpha-actinin, and dystrophin.","citation":"Adv Protein Chem 2005;70:203-46","abstract":"Spectrin family proteins represent an important group of actin-bundling and membrane-anchoring proteins found in diverse structures from yeast to man. Arising from a common ancestral alpha-actinin gene through duplications and rearrangements, the family has increased to include the spectrins and dystrophin/utrophin. The spectrin family is characterized by the presence of spectrin repeats, actin binding domains, and EF hands. With increasing divergence, new domains and functions have been added such that spectrin and dystrophin also contain specialized protein-protein interaction motifs and regions for interaction with membranes and phospholipids. The acquisition of new domains also increased the functional complexity of the family such that the proteins perform a range of tasks way beyond the simple bundling of actin filaments by alpha-actinin in S. pombe. We discuss the evolutionary, structural, functional, and regulatory roles of the spectrin family of proteins and describe some of the disease traits associated with loss of spectrin family protein function.","authors":"Broderick MJ, Winder SJ","authors_abbrev":"Broderick MJ et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-04-20","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10430583","title":"A new recombinational DNA repair gene from Schizosaccharomyces pombe with homology to Escherichia coli RecA.","citation":"Genetics 1999 Aug;152(4):1557-72","abstract":"A new DNA repair gene from Schizosaccharomyces pombe with homology to RecA was identified and characterized. Comparative analysis showed highest similarity to Saccharomyces cerevisiae Rad55p. rhp55(+) (rad homologue pombe 55) encodes a predicted 350-amino-acid protein with an M(r) of 38,000. The rhp55Delta mutant was highly sensitive to methyl methanesulfonate (MMS), ionizing radiation (IR), and, to a lesser degree, UV. These phenotypes were enhanced at low temperatures, similar to deletions in the S. cerevisiae RAD55 and RAD57 genes. Many rhp55Delta cells were elongated with aberrant nuclei and an increased DNA content. The rhp55 mutant showed minor deficiencies in meiotic intra- and intergenic recombination. Sporulation efficiency and spore viability were significantly reduced. Double-mutant analysis showed that rhp55(+) acts in one DNA repair pathway with rhp51(+) and rhp54(+), homologs of the budding yeast RAD51 and RAD54 genes, respectively. However, rhp55(+) is in a different epistasis group for repair of UV-, MMS-, or gamma-ray-induced DNA damage than is rad22(+), a putative RAD52 homolog of fission yeast. The structural and functional similarity suggests that rhp55(+) is a homolog of the S. cerevisiae RAD55 gene and we propose that the functional diversification of RecA-like genes in budding yeast is evolutionarily conserved.","authors":"Khasanov FK, Savchenko GV, Bashkirova EV, Korolev VG, Heyer WD, Bashkirov VI","authors_abbrev":"Khasanov FK et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-08-03","publication_year":"1999","canto_session_key":"23bb4638a11a6ec8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-12-22 13:53:57","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-19 16:11:36","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC15A10.03c","SPAC3C7.03c","SPAC30D11.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-09-19"},{"uniquename":"PMID:9749530","title":"Thioltransferase from Schizosaccharomyces pombe: purification to homogeneity and some properties.","citation":"Mol Cells 1998 Aug 31;8(4):431-7","abstract":"Two types of thioltransferase were identified in the cytosolic extract of Schizosaccharomyces pombe, a fission yeast. In the present study, the major one of them was purified to homogeneity using chromatography processes such as ion-exchange chromatography and gel filtration. Purification was monitored by the transhydrogenase activity of thioltransferase with 2-hydroxyethyl disulfide as a substrate. Its molecular weight was estimated to be about 14,000 on SDS-polyacrylamide gel electrophoresis. The purified enzyme catalyzes the reduction of various disulfide compounds such as S-sulfocysteine, L-cystine, and insulin. It was also found to contain the reducing activity on non-disulfide substrates such as dehydroascorbic acid and alloxan. Its activity was greatly activated by high concentrations of reduced glutathione. It was found to be very heat-stable as like other thioltransferases. It was characterized on other aspects such as kinetic parameters and optimal reaction conditions.","authors":"Kim HG, Park EH, Lim CJ","authors_abbrev":"Kim HG et al.","pubmed_publication_date":"31 Aug 1998","pubmed_entrez_date":"1998-09-28","publication_year":"1998","canto_session_key":"8244700c3afd0fae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-11-07 11:53:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 12:38:35","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-11-05"},{"uniquename":"PMID:28223368","title":"Phosphatases Generate Signal Specificity Downstream of Ssp1 Kinase in Fission Yeast.","citation":"Mol Cell Biol 2017 May 15;37(10)","abstract":"AMPK-related protein kinases (ARKs) coordinate cell growth, proliferation, and migration with environmental status. It is unclear how specific ARKs are activated at specific times. In the fission yeast  Schizosaccharomyces pombe , the CaMKK-like protein kinase Ssp1 promotes cell cycle progression by activating the ARK Cdr2 according to cell growth signals. Here, we demonstrate that Ssp1 activates a second ARK, Ssp2/AMPKα, for cell proliferation in low environmental glucose. Ssp1 activates these two related targets by the same biochemical mechanism: direct phosphorylation of a conserved residue in the activation loop (Cdr2-T166 and Ssp2-T189). Despite a shared upstream kinase and similar phosphorylation sites, Cdr2 and Ssp2 have distinct regulatory input cues and distinct functional outputs. We investigated this specificity and found that distinct protein phosphatases counteract Ssp1 activity toward its different substrates. We identified the PP6 family phosphatase Ppe1 as the primary phosphatase for Ssp2-T189 dephosphorylation. The phosphatase inhibitor Sds23 acts upstream of PP6 to regulate Ssp2-T189 phosphorylation in a manner that depends on energy but not on the intact AMPK heterotrimer. In contrast, Cdr2-T166 phosphorylation is regulated by protein phosphatase 2A but not by the Sds23-PP6 pathway. Thus, our study provides a phosphatase-driven mechanism to induce specific physiological responses downstream of a master protein kinase.","doi":"10.1128/MCB.00494-16","authors":"Deng L, Lee ME, Schutt KL, Moseley JB","authors_abbrev":"Deng L et al.","pubmed_publication_date":"15 May 2017","pubmed_entrez_date":"2017-02-23","publication_year":"2017","canto_session_key":"b5354310eddcf526","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-24 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPCC74.03c","SPAC1556.08c","SPCC663.01c","SPCC297.03","SPBC646.13"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:42231419","title":"Acyl CoA reductases useful for bioproduction of hydrocarbons.","citation":"Microb Cell Fact 2026 Jun 02;","abstract":"Hydrocarbon-based biofuels-so-called drop-in fuels-have gained attention as sustainable alternatives to petroleum-derived fuels, yet their biological production remains limited by the availability of efficient enzymatic pathways for generating hydrocarbon precursors. Medium-chain alkanes produced by microorganisms represent a promising target, but the aldehyde-producing capabilities of acyl-CoA reductases (ACRs) from bacteria, plants, and animals have not been systematically compared. Because ACRs generate fatty aldehydes-key intermediates in hydrocarbon biosynthesis-understanding their diversity is essential for expanding biological fuel production strategies. In this study, we established a whole‑cell proxy screening framework in E. coli, a widely used microbial production host, to identify promising ACR candidates in this chassis and to provide new insights into ACR diversity and performance in a microbial production host that can help inform future development of microbial hydrocarbon bioproduction pathways.\nSixteen acyl-CoA reductases (ACRs) from microorganisms, plants, and animals were cloned and expressed in Escherichia coli and screened using hydrocarbon formation as a practical proxy readout by coexpressing each enzyme with a cyanobacterial aldehyde decarbonylase. Several Arabidopsis thaliana ACRs produced higher alkane levels than microbial and animal enzymes. To further examine plant-derived enzymes, ACR homologs with high amino acid similarity to A. thaliana ACR1 and ACR2 were cloned from multiple plant species and tested. In the E. coli proxy‑screening context used here, some plant ACR homologs yield detectable medium‑chain hydrocarbon proxy readouts. Among these, introduction of ACR2 from Glycine max resulted in the highest alkane and alkene formation levels. Phylogenetic analysis of fourteen plant ACRs with considerable medium chain hydrocarbon proxy-readout showed that ACRs similar to GmACR2 generated higher levels of C13 alkanes, although no clear trend was observed for C15 alkane or C17 alkene. In an E. coli strain coexpressing GmACR2 and SpALDH, we detected a small C17 alkene (1‑heptadecene) signal above the empty‑vector background under the conditions tested, although enzyme‑specific attribution remains unresolved in the absence of single‑expression controls. This preliminary observation suggests that a C17 alkene signal can be detected in an ACR-ALDH coexpression background, suggesting a potentially broader space of ACR-ALDH combinations for future exploration in microbial hydrocarbon production.\nThis study identifies multiple microbial and plant-derived ACRs, particularly GmACR2, as a strong candidate in this E. coli whole‑cell proxy screening assay for medium-chain hydrocarbon biosynthesis. Coexpression of GmACR2 with S. pombe aldehyde dehydrogenase provides an initial proof-of-concept indication that hydrocarbon formation can be detected in an ACR-ALDH coexpression background in E. coli. Because ACR and ALDH homologs are widely distributed across taxa, our findings highlight broadly accessible enzymatic components that can be repurposed for engineered microbial hydrocarbon biosynthesis.","doi":"10.1186/s12934-026-03038-2","authors":"Ito M, Kishino S, Muramatsu M, Ogawa J","authors_abbrev":"Ito M et al.","pubmed_publication_date":"02 Jun 2026","pubmed_entrez_date":"2026-06-03","publication_year":"2026","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2026-06-03 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11729194","title":"Pnk1, a DNA kinase/phosphatase required for normal response to DNA damage by gamma-radiation or camptothecin in Schizosaccharomyces pombe.","citation":"J Biol Chem 2002 Feb 08;277(6):4050-5","abstract":"We report the characterization of Pnk1, a 45-kDa homolog of the human polynucleotide kinase PNKP in Schizosaccharomyces pombe. Recombinant Pnk1 like human PNKP exhibits both 5'-DNA kinase and 3'-DNA phosphatase activities in vitro. Furthermore, we detected 3'-DNA phosphatase activity with a single-stranded substrate in extracts from wild-type yeast, but no activity was detected in pnk1delta strains. We have shown that GFP-tagged Pnk1 like mammalian PNKP localizes to the nucleus. Deletion of pnk1 does not affect cell growth under normal conditions but results in significant hypersensitivity to gamma-radiation or camptothecin, an inhibitor of topoisomerase I, suggesting that Pnk1 plays an important role in the repair of DNA strand breaks produced by these agents. The pnk1 deletion mutants were not hypersensitive to ethyl methanesulfonate, methyl methanesulfonate, or 4-nitroquinoline N-oxide. Expression of human PNKP in pnk1delta cells restores resistance to gamma-radiation or camptothecin, suggesting that the functions of yeast Pnk1 and human PNKP have been conserved.","authors":"Meijer M, Karimi-Busheri F, Huang TY, Weinfeld M, Young D","authors_abbrev":"Meijer M et al.","pubmed_publication_date":"08 Feb 2002","pubmed_entrez_date":"2001-12-01","publication_year":"2002","canto_session_key":"0e75134c69a78468","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-20 13:50:50","canto_approved_date":"2019-12-03 19:15:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 09:33:01","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-20"},{"uniquename":"EMBL:AU006956","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27611590","title":"Pfh1 Is an Accessory Replicative Helicase that Interacts with the Replisome to Facilitate Fork Progression and Preserve Genome Integrity.","citation":"PLoS Genet 2016 Sep;12(9):e1006238","abstract":"Replicative DNA helicases expose the two strands of the double helix to the replication apparatus, but accessory helicases are often needed to help forks move past naturally occurring hard-to-replicate sites, such as tightly bound proteins, RNA/DNA hybrids, and DNA secondary structures. Although the Schizosaccharomyces pombe 5'-to-3' DNA helicase Pfh1 is known to promote fork progression, its genomic targets, dynamics, and mechanisms of action are largely unknown. Here we address these questions by integrating genome-wide identification of Pfh1 binding sites, comprehensive analysis of the effects of Pfh1 depletion on replication and DNA damage, and proteomic analysis of Pfh1 interaction partners by immunoaffinity purification mass spectrometry. Of the 621 high confidence Pfh1-binding sites in wild type cells, about 40% were sites of fork slowing (as marked by high DNA polymerase occupancy) and/or DNA damage (as marked by high levels of phosphorylated H2A). The replication and integrity of tRNA and 5S rRNA genes, highly transcribed RNA polymerase II genes, and nucleosome depleted regions were particularly Pfh1-dependent. The association of Pfh1 with genomic integrity at highly transcribed genes was S phase dependent, and thus unlikely to be an artifact of high transcription rates. Although Pfh1 affected replication and suppressed DNA damage at discrete sites throughout the genome, Pfh1 and the replicative DNA polymerase bound to similar extents to both Pfh1-dependent and independent sites, suggesting that Pfh1 is proximal to the replication machinery during S phase. Consistent with this interpretation, Pfh1 co-purified with many key replisome components, including the hexameric MCM helicase, replicative DNA polymerases, RPA, and the processivity clamp PCNA in an S phase dependent manner. Thus, we conclude that Pfh1 is an accessory DNA helicase that interacts with the replisome and promotes replication and suppresses DNA damage at hard-to-replicate sites. These data provide insight into mechanisms by which this evolutionarily conserved helicase helps preserve genome integrity.","doi":"10.1371/journal.pgen.1006238","authors":"McDonald KR, Guise AJ, Pourbozorgi-Langroudi P, Cristea IM, Zakian VA, Capra JA, Sabouri N","authors_abbrev":"McDonald KR et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-09-10","publication_year":"2016","canto_session_key":"c131e5fc09dccabc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nasim Sabouri","canto_first_approved_date":"2016-11-10 14:29:47","canto_approved_date":"2024-07-04 15:47:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-04 09:24:19","canto_added_date":"2016-09-11 00:15:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Nasim Sabouri","community_curator":true,"annotation_count":52,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP8B7.19","SPBC800.07c","SPCC23B6.05c","SPCC1753.01c","SPAC31G5.19","SPCC330.13","SPAC1556.02c","SPAC6G10.02c","SPBC30D10.08","SPCC18.07","SPBC16G5.12c","SPAC2F3.04c","SPCC16A11.17","SPCC285.16c","SPBC216.05","SPAC15A10.11","SPCC553.09c","SPBC11C11.11c","SPCC553.01c","SPCC126.02c","SPAC167.05","SPBC1105.04c","SPAC1B2.05","SPBC25D12.03c","SPBC336.01","SPAPB1E7.03","SPBC887.14c","SPCC162.05","SPAC26H5.12","SPBC651.08c","SPBC19G7.01c","SPBC4.04c","SPBC543.03c","SPAC1F5.11c","SPBC2G5.07c","SPAC26A3.03c","SPAC2G11.12","SPAPB17E12.10c","SPAC3H5.06c","SPAC4G9.08c","SPAC9.05","SPAC13F5.01c","SPBC16D10.04c","SPBC16D10.09","SPAC30D11.10","SPAC8F11.03","SPBC25H2.13c","SPBC3B8.08","SPBC609.05","SPBC211.04c","SPBC660.13c"],"gene_count":51,"ltp_gene_count":51,"approved_date":"2016-11-10"},{"uniquename":"PMID:34493579","title":"Ccq1-Raf2 interaction mediates CLRC recruitment to establish heterochromatin at telomeres.","citation":"Life Sci Alliance 2021 Nov;4(11)","abstract":"Telomeres, highly ordered DNA-protein complexes at eukaryotic linear chromosome ends, are specialized heterochromatin loci conserved among eukaryotes. In  Schizosaccharomyces pombe , the shelterin complex is important for subtelomeric heterochromatin establishment. Despite shelterin has been demonstrated to mediate the recruitment of the Snf2/histone deacetylase-containing repressor complex (SHREC) and the Clr4 methyltransferase complex (CLRC) to telomeres, the mechanism involved in telomeric heterochromatin assembly remains elusive due to the multiple functions of the shelterin complex. Here, we found that CLRC plays a dominant role in heterochromatin establishment at telomeres. In addition, we identified a series of amino acids in the shelterin subunit Ccq1 that are important for the specific interaction between Ccq1 and the CLRC subunit Raf2. Finally, we demonstrated that the Ccq1-Raf2 interaction is essential for the recruitment of CLRC to telomeres, that contributes to histone H3 lysine 9 methylation, nucleosome stability and the shelterin-chromatin association, promoting a positive feedback mechanism for the nucleation and spreading of heterochromatin at subtelomeres. Together, our findings provide a mechanistic understanding of subtelomeric heterochromatin assembly by shelterin-dependent CLRC recruitment to chromosomal ends.","doi":"10.26508/lsa.202101106","authors":"Shi S, Zhou Y, Lu Y, Sun H, Xue J, Wu Z, Lei M","authors_abbrev":"Shi S et al.","pubmed_publication_date":"Nov 2021","pubmed_entrez_date":"2021-09-08","publication_year":"2021","canto_session_key":"48197abbbf9deb5d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-09-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37238680","title":"Roles of Specialized Chromatin and DNA Structures at Subtelomeres in  Schizosaccharomyces pombe .","citation":"Biomolecules 2023 May 10;13(5)","abstract":"Eukaryotes have linear chromosomes with domains called telomeres at both ends. The telomere DNA consists of a simple tandem repeat sequence, and multiple telomere-binding proteins including the shelterin complex maintain chromosome-end structures and regulate various biological reactions, such as protection of chromosome ends and control of telomere DNA length. On the other hand, subtelomeres, which are located adjacent to telomeres, contain a complex mosaic of multiple common segmental sequences and a variety of gene sequences. This review focused on roles of the subtelomeric chromatin and DNA structures in the fission yeast  Schizosaccharomyces pombe . The fission yeast subtelomeres form three distinct chromatin structures; one is the shelterin complex, which is localized not only at the telomeres but also at the telomere-proximal regions of subtelomeres to form transcriptionally repressive chromatin structures. The others are heterochromatin and knob, which have repressive effects in gene expression, but the subtelomeres are equipped with a mechanism that prevents these condensed chromatin structures from invading adjacent euchromatin regions. On the other hand, recombination reactions within or near subtelomeric sequences allow chromosomes to be circularized, enabling cells to survive in telomere shortening. Furthermore, DNA structures of the subtelomeres are more variable than other chromosomal regions, which may have contributed to biological diversity and evolution while changing gene expression and chromatin structures.","doi":"10.3390/biom13050810","authors":"Kanoh J","authors_abbrev":"Kanoh J","pubmed_publication_date":"10 May 2023","pubmed_entrez_date":"2023-05-27","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-05-28 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16772338","title":"The fission yeast Chs2 protein interacts with the type-II myosin Myo3p and is required for the integrity of the actomyosin ring.","citation":"J Cell Sci 2006 Jul 01;119(Pt 13):2768-79","abstract":"In Schizosaccharomyces pombe cytokinesis requires the function of a contractile actomyosin ring. Fission yeast Chs2p is a transmembrane protein structurally similar to chitin synthases that lacks such enzymatic activity. Chs2p localisation and assembly into a ring that contracts during division requires the general system for polarised secretion, some components of the actomyosin ring, and an active septation initiation network. Chs2p interacts physically with the type-II myosin Myo3p revealing a physical link between the plasma membrane and the ring. In chs2Delta mutants, actomyosin ring integrity is compromised during the last stages of contraction and it remains longer in the midzone. In synchronous cultures, chs2Delta cells exhibit a delay in septation with respect to the control strain. All these results show that Chs2p participates in the correct functioning of the medial ring.","authors":"Martín-García R, Valdivieso MH","authors_abbrev":"Martín-García R et al.","pubmed_publication_date":"01 Jul 2006","pubmed_entrez_date":"2006-06-15","publication_year":"2006","canto_session_key":"fa68bb8cf0eff996","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-02-09 18:13:58","canto_approved_date":"2020-01-23 10:57:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-13 16:35:37","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":47,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPCC645.05c","SPAC4A8.05c","SPCC1919.10c","SPAC4F8.13c","SPAP8A3.08","SPCC1739.11c","SPBC1709.01","SPBC19G7.05c","SPBC106.20","SPBC11C11.02","SPAC4A8.15c","SPAC20G8.05c","SPAC926.03"],"gene_count":14,"ltp_gene_count":11,"approved_date":"2016-02-09"},{"uniquename":"PMID:8673017","title":"A simple and efficient method for the isolation of total RNA from the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Mol Biol Int 1995 Oct;37(2):339-44","abstract":"A simple and efficient procedure was described for the isolation of total RNA from the fission yeast Schizosaccharomyces pombe. The present study demonstrated that the quality and the quantity of S. pombe RNA were increased by substituting phenol/chloroform mixture for phenol as a deproteinizing agent in the first vortexing step and using an ice bath instead of a dry ice-ethanol bath in the freezing step. Additionally, this protocol had the advantage of extracting total RNA without any degradation of S. pombe cells. Furthermore, the high amounts and quality of RNA extracted by this modified procedure enabled us to perform some experiments such as Northern blot, S1 mapping, primer extension, and reverse transcriptase reaction-polymerase chain reaction (RT-PCR) without further RNA purification. We suggest that this procedure is very useful to analyse primary structures and steady-state levels of RNA from S. pombe.","authors":"Jang YK, Jin YH, Kim MJ, Seong RH, Hong SH, Park SD","authors_abbrev":"Jang YK et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28765295","title":"Mating-Type Determination in  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Aug 01;2017(8):pdb.prot091728","abstract":"Here we describe how mating-type tests are conducted in  Schizosaccharomyces pombe  Two methods can be employed: matings with  h -   and  h +   tester strains and polymerase chain reaction (PCR) for  mat1  content.","doi":"10.1101/pdb.prot091728","authors":"Ekwall K, Thon G","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"01 Aug 2017","pubmed_entrez_date":"2017-08-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-08-04 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9778252","title":"RNA-assisted nuclear transport of the meiotic regulator Mei2p in fission yeast.","citation":"Cell 1998 Oct 02;95(1):115-23","abstract":"Fission yeast Mei2p is an RNA-binding protein required for both premeiotic DNA synthesis and meiosis I. Mei2p binds to a polyadenylated RNA molecule, meiRNA, loss of which blocks meiosis I. Mei2p forms a dot in meiotic prophase nuclei. Here, we show that meiRNA is required for the nuclear localization of Mei2p and is detectable in the dot. However, Mei2p carrying a nuclear localization signal can produce a nuclear dot and promote meiosis I in the absence of meiRNA. Mei2p expressed in cultured mammalian cells stays in the cytoplasm, but it accumulates in the nucleolus if meiRNA is coexpressed. These results indicate that meiRNA contributes to the promotion of meiosis I exclusively as a cofactor that assists nuclear transport of Mei2p.","authors":"Yamashita A, Watanabe Y, Nukina N, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"02 Oct 1998","pubmed_entrez_date":"1998-10-20","publication_year":"1998","canto_session_key":"738fa42d26db17a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-13 15:35:41","canto_approved_date":"2025-07-02 07:27:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-07 11:59:39","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.13c","SPAC27D7.03c","SPNCRNA.103","SPBC29A10.14"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-11-13"},{"uniquename":"PMID:27587782","title":"Synchronization of S Phase in Schizosaccharomyces pombe Cells by Transient Exposure to M-Factor Pheromone.","citation":"Cold Spring Harb Protoc 2016 Sep 01;2016(9)","abstract":"A well-characterized S phase, a unicellular lifestyle, and a plethora of mutations in key components of DNA metabolism make fission yeast a particularly attractive system in which to study DNA replication. However, synchronization of passage through a normal S phase has proved challenging. This protocol describes how combining nitrogen starvation with M-factor mating pheromone treatment presents a highly effective method for synchronizing passage through an ostensibly normal S phase.","doi":"10.1101/pdb.prot091272","authors":"Nielsen O","authors_abbrev":"Nielsen O","pubmed_publication_date":"01 Sep 2016","pubmed_entrez_date":"2016-09-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-09-04 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18204818","title":"Identification of small molecules inducing apoptosis by cell-based assay using fission yeast deletion mutants.","citation":"Invest New Drugs 2008 Aug;26(4):299-307","abstract":"The cell-based assay using yeast deletion mutants has been recognized as an efficient analysis to discover therapeutic compounds and reveal their mode of action. In this study, S. pombe deletion mutants-based HTS screening was carried out to identify potential anti-cancer agents. The NCI chemical library of 5700 compounds was screened using kit strains, which consisted of S. pombe mutants harboring deletions in genes involved in DNA repair and mitotic control. During the screening, we identified 40 compounds conferring growth inhibition of S. pombe. Their anti-tumorigenic properties were examined by phenotypic effect on S. pombe, flow cytometry and apoptosis analysis of human cancer. Here, we report hit compounds inducing apoptosis for development of anti-cancer agents suggesting that S. pombe deletion mutants are useful in identifying potential anti-cancer agents in human cancer therapeutics.","doi":"10.1007/s10637-007-9100-5","authors":"Chung KS, Yim NH, Lee SH, Choi SJ, Hur KS, Hoe KL, Kim DU, Goehle S, Kim HB, Song KB, Yoo HS, Bae KH, Simon J, Won M","authors_abbrev":"Chung KS et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-01-22","publication_year":"2008","canto_session_key":"894e3c36003ab516","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-24 15:51:19","canto_approved_date":"2019-06-12 14:04:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-24 15:51:03","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.04c","SPAC2E12.02","SPAC6F6.08c","SPBC25D12.04","SPBC216.05","SPBC1A4.03c","SPBC428.08c","SPAC3H1.11","SPAC8E11.02c","SPBP4H10.06c","SPAC23H3.08c","SPAC20G4.04c","SPAC25G10.07c","SPBC1289.03c","SPCC1739.12","SPAP8A3.09c","SPAC3A12.14","SPAC17C9.10"],"gene_count":18,"ltp_gene_count":13,"approved_date":"2015-02-24"},{"uniquename":"PANTHER:PTHR11759","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:14050","SPAC1B3.18c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:41751767","title":"Yeast as a Model for Human Disease.","citation":"Int J Mol Sci 2026 Feb 07;27(4)","abstract":"Yeasts, especially the conventional species  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe , as well as some unconventional species such as  Pichia pastoris ,  Kluyveromyces marxianus  and  Yarrowia lipolytica , have become fundamental model organisms for understanding the molecular mechanisms underlying human diseases. Their eukaryotic cell organization, genetic simplicity, and strong conservation of essential biological pathways make them indispensable in biomedical research. This review provides a comprehensive overview of the role of different yeast species in modeling human disorders, highlighting historical milestones and groundbreaking discoveries that have shaped current knowledge. The article discusses the applications of yeast models in studying neurodegenerative diseases such as Alzheimer's and Huntington's, as well as metabolic diseases, infectious diseases and mitochondrial disorders, and their growing importance in cancer research and drug discovery. Special attention is given to humanized yeast models, which enable the expression and functional analysis of human genes and the heterologous synthesis of human proteins within yeast cells. Finally, the paper addresses the limitations and challenges of yeast as a model system while outlining future directions and emphasizing the organism's continued relevance in personalized medicine and functional genomics.","doi":"10.3390/ijms27041632","authors":"Zieniuk B, Wierzchowska K, Jasińska K, Kobus J, Piotrowicz A, Uğur Ş, Fabiszewska A","authors_abbrev":"Zieniuk B et al.","pubmed_publication_date":"07 Feb 2026","pubmed_entrez_date":"2026-02-27","publication_year":"2026","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2026-02-28 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2821024","title":"Nucleoside diphosphokinase, an enzyme with step changes in activity during the cell cycle of the fission yeast Schizosaccharomyces pombe. I. Persistence of steps after a block to the DNA-division cycle.","citation":"J Cell Sci 1986 Dec;86:207-15","abstract":"In confirmation of earlier results, nucleoside diphosphokinase is shown to be a 'step' enzyme in Schizosaccharomyces pombe with a sharp doubling in activity at the beginning of the cell cycle. These doubling steps occur at the same time in the cycle in the smaller cells of the mutant wee1.6. An important result is that the activity steps persist with normal cell cycle timing after a block to the DNA-division cycle imposed by the cycle mutants cdc2.33 and cdc2.33wee1.6. This is clear proof that oscillatory controls of some cell cycle events can persist after the main periodic events of the DNA-division cycle have been abolished.","authors":"Creanor J, Mitchison JM","authors_abbrev":"Creanor J et al.","pubmed_publication_date":"Dec 1986","pubmed_entrez_date":"1986-12-01","publication_year":"1986","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37970674","title":"SUMOylation regulates Lem2 function in centromere clustering and silencing.","citation":"J Cell Sci 2023 Dec 01;136(23)","abstract":"Regulation by the small modifier SUMO is heavily dependent on spatial control of enzymes that mediate the attachment and removal of SUMO on substrate proteins. Here, we show that in the fission yeast Schizosaccharomyces pombe, delocalisation of the SUMO protease Ulp1 from the nuclear envelope results in centromeric defects that can be attributed to hyper-SUMOylation at the nuclear periphery. Unexpectedly, we find that although this localised hyper-SUMOylation impairs centromeric silencing, it can also enhance centromere clustering. Moreover, both effects are at least partially dependent on SUMOylation of the inner nuclear membrane protein Lem2. Lem2 has previously been implicated in diverse biological processes, including the promotion of both centromere clustering and silencing, but how these distinct activities are coordinated was unclear; our observations suggest a model whereby SUMOylation serves as a regulatory switch, modulating Lem2 interactions with competing partner proteins to balance its roles in alternative pathways. Our findings also reveal a previously unappreciated role for SUMOylation in promoting centromere clustering.","doi":"10.1242/jcs.260868","authors":"Strachan J, Leidecker O, Spanos C, Le Coz C, Chapman E, Arsenijevic A, Zhang H, Zhao N, Spoel SH, Bayne EH","authors_abbrev":"Strachan J et al.","pubmed_publication_date":"01 Dec 2023","pubmed_entrez_date":"2023-11-16","publication_year":"2023","canto_session_key":"c56a652b8b068e66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Joanna Strachan","canto_first_approved_date":"2024-03-28 10:06:37","canto_approved_date":"2024-09-26 10:18:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-11 15:27:28","canto_added_date":"2023-11-16 13:05:08","annotation_curators":[{"name":"Elizabeth Bayne","community_curator":true,"annotation_count":55,"orcid":"0000-0001-8775-999X","file_type":null,"file_name":null},{"name":"Joanna Strachan","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Joanna Strachan","file_curator_role":"community","annotation_file_curators":[{"name":"Joanna 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inosine tRNA modification is essential to cell cycle progression in G(1)/S and G(2)/M transitions in fission yeast.","citation":"J Biol Chem 2007 Nov 16;282(46):33459-33465","abstract":"Inosine (I) at position 34 (wobble position) of tRNA is formed by the hydrolytic deamination of a genomically encoded adenosine (A). The enzyme catalyzing this reaction, termed tRNA A:34 deaminase, is the heterodimeric Tad2p/ADAT2.Tad3p/ADAT3 complex in eukaryotes. In budding yeast, deletion of each subunit is lethal, indicating that the wobble inosine tRNA modification is essential for viability; however, most of its physiological roles remain unknown. To identify novel cell cycle mutants in fission yeast, we isolated the tad3-1 mutant that is allelic to the tad3(+) gene encoding a homolog of budding yeast Tad3p. Interestingly, the tad3-1 mutant cells principally exhibited cell cycle-specific phenotype, namely temperature-sensitive and irreversible cell cycle arrest both in G(1) and G(2). Further analyses revealed that in the tad3-1 mutant cells, the S257N mutation that occurred in the catalytically inactive Tad3 subunit affected its association with catalytically active Tad2 subunit, leading to an impairment in the A to I conversion at position 34 of tRNA. In tad3-1 mutant cells, the overexpression of the tad3(+) gene completely suppressed the decreased tRNA inosine content. Notably, the overexpression of the tad2(+) gene partially suppressed the temperature-sensitive phenotype and the decreased tRNA inosine content, indicating that the tad3-1 mutant phenotype is because of the insufficient I(34) formation of tRNA. These results suggest that the wobble inosine tRNA modification is essential for cell cycle progression in the G(1)/S and G(2)/M transitions in fission yeast.","doi":"10.1074/jbc.M706869200","authors":"Tsutsumi S, Sugiura R, Ma Y, Tokuoka H, Ohta K, Ohte R, Noma A, Suzuki T, Kuno T","authors_abbrev":"Tsutsumi S et al.","pubmed_publication_date":"16 Nov 2007","pubmed_entrez_date":"2007-09-19","publication_year":"2007","canto_session_key":"fec781c2e8599d7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-04-20 16:43:11","canto_approved_date":"2025-01-08 13:39:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-03-12 11:48:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.10","SPAP27G11.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-04-20"},{"uniquename":"PMID:35194019","title":"Dicer promotes genome stability via the bromodomain transcriptional co-activator BRD4.","citation":"Nat Commun 2022 Feb 22;13(1):1001","abstract":"RNA interference is required for post-transcriptional silencing, but also has additional roles in transcriptional silencing of centromeres and genome stability. However, these roles have been controversial in mammals. Strikingly, we found that Dicer-deficient embryonic stem cells have strong proliferation and chromosome segregation defects as well as increased transcription of centromeric satellite repeats, which triggers the interferon response. We conducted a CRISPR-Cas9 genetic screen to restore viability and identified transcriptional activators, histone H3K9 methyltransferases, and chromosome segregation factors as suppressors, resembling Dicer suppressors identified in independent screens in fission yeast. The strongest suppressors were mutations in the transcriptional co-activator Brd4, which reversed the strand-specific transcription of major satellite repeats suppressing the interferon response, and in the histone acetyltransferase Elp3. We show that identical mutations in the second bromodomain of Brd4 rescue Dicer-dependent silencing and chromosome segregation defects in both mammalian cells and fission yeast. This remarkable conservation demonstrates that RNA interference has an ancient role in transcriptional silencing and in particular of satellite repeats, which is essential for cell cycle progression and proper chromosome segregation. Our results have pharmacological implications for cancer and autoimmune diseases characterized by unregulated transcription of satellite repeats.","doi":"10.1038/s41467-022-28554-8","authors":"Gutbrod MJ, Roche B, Steinberg JI, Lakhani AA, Chang K, Schorn AJ, Martienssen RA","authors_abbrev":"Gutbrod MJ et al.","pubmed_publication_date":"22 Feb 2022","pubmed_entrez_date":"2022-02-23","publication_year":"2022","canto_session_key":"d96802a70862fa93","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Benjamin Roche","canto_first_approved_date":"2022-03-10 11:27:11","canto_approved_date":"2022-03-21 13:00:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-09 19:07:49","canto_added_date":"2022-02-25 01:15:05","annotation_curators":[{"name":"Benjamin Roche","community_curator":true,"annotation_count":41,"orcid":"0000-0003-3912-6340","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c","SPCC1450.02","SPAC631.02"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2022-03-10"},{"uniquename":"PMID:27628706","title":"The power of fission: yeast as a tool for understanding complex splicing.","citation":"Curr Genet 2017 Jun;63(3):375-380","abstract":"Pre-mRNA splicing is an essential component of eukaryotic gene expression. Many metazoans, including humans, regulate alternative splicing patterns to generate expansions of their proteome from a limited number of genes. Importantly, a considerable fraction of human disease causing mutations manifest themselves through altering the sequences that shape the splicing patterns of genes. Thus, understanding the mechanistic bases of this complex pathway will be an essential component of combating these diseases. Dating almost to the initial discovery of splicing, researchers have taken advantage of the genetic tractability of budding yeast to identify the components and decipher the mechanisms of splicing. However, budding yeast lacks the complex splicing machinery and alternative splicing patterns most relevant to humans. More recently, many researchers have turned their efforts to study the fission yeast, Schizosaccharomyces pombe, which has retained many features of complex splicing, including degenerate splice site sequences, the usage of exonic splicing enhancers, and SR proteins. Here, we review recent work using fission yeast genetics to examine pre-mRNA splicing, highlighting its promise for modeling the complex splicing seen in higher eukaryotes.","doi":"10.1007/s00294-016-0647-6","authors":"Fair BJ, Pleiss JA","authors_abbrev":"Fair BJ et al.","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2016-09-16","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-09-17 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23391388","title":"Cell biology: polar expeditions for PP1.","citation":"Curr Biol 2013 Feb 04;23(3):R120-2","abstract":"A new study shows that phospho-dependent expulsion of type-1-phosphatase (PP1) from the spindle pole by Fin1 (NIMA) kinase ensures switch-like activation of Cyclin B-Cdk1 at the G2/M transition.","doi":"10.1016/j.cub.2012.12.020","authors":"Meadows JC, Millar JB","authors_abbrev":"Meadows JC et al.","pubmed_publication_date":"04 Feb 2013","pubmed_entrez_date":"2013-02-09","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-08-22 05:19:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12509501","title":"RNA interference machinery regulates chromosome dynamics during mitosis and meiosis in fission yeast.","citation":"Proc Natl Acad Sci U S A 2003 Jan 07;100(1):193-8","abstract":"The regulation of higher-order chromosome structure is central to cell division and sexual reproduction. Heterochromatin assembly at the centromeres facilitates both kinetochore formation and sister chromatid cohesion, and the formation of specialized chromatin structures at telomeres serves to maintain the length of telomeric repeats, to suppress recombination, and to aid in formation of a bouquet-like structure that facilitates homologous chromosome pairing during meiosis. In fission yeast, genes encoding the Argonaute, Dicer, and RNA-dependent RNA polymerase factors involved in RNA interference (RNAi) are required for heterochromatin formation at the centromeres and mating type region. In this study, we examine the effects of deletions of the fission yeast RNAi machinery on chromosome dynamics during mitosis and meiosis. We find that the RNAi machinery is required for the accurate segregation of chromosomes. Defects in mitotic chromosome segregation are correlated with loss of cohesin at centromeres. Although the telomeres of RNAi mutants maintain silencing, length, and localization of the heterochromatin protein Swi6, we discovered defects in the proper clustering of telomeres in interphase mitotic cells. Furthermore, a small proportion of RNAi mutant cells display aberrant telomere clustering during meiotic prophase. This study demonstrates that the fission yeast RNAi machinery is required for the proper regulation of chromosome architecture during mitosis and meiosis.","authors":"Hall IM, Noma K, Grewal SI","authors_abbrev":"Hall IM et al.","pubmed_publication_date":"07 Jan 2003","pubmed_entrez_date":"2003-01-02","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22144909","title":"The fission yeast stress-responsive MAPK pathway promotes meiosis via the phosphorylation of Pol II CTD in response to environmental and feedback cues.","citation":"PLoS Genet 2011 Dec;7(12):e1002387","abstract":"The RRM-type RNA-binding protein Mei2 is a master regulator of meiosis in fission yeast, in which it stabilizes meiosis-specific mRNAs by blocking their destruction. Artificial activation of Mei2 can provoke the entire meiotic process, and it is suspected that Mei2 may do more than the stabilization of meiosis-specific mRNAs. In our current study using a new screening system, we show that Mei2 genetically interacts with subunits of CTDK-I, which phosphorylates serine-2 residues on the C-terminal domain of RNA polymerase II (Pol II CTD). Phosphorylation of CTD Ser-2 is essential to enable the robust transcription of ste11, which encodes an HMG-type transcription factor that regulates the expression of mei2 and other genes necessary for sexual development. CTD Ser-2 phosphorylation increases under nitrogen starvation, and the stress-responsive MAP kinase pathway, mediated by Wis1 MAPKK and Sty1 MAPK, is critical for this stress response. Sty1 phosphorylates Lsk1, the catalytic subunit of CTDK-I. Furthermore, a feedback loop stemming from activated Mei2 to Win1 and Wis4 MAPKKKs operates in this pathway and eventually enhances CTD Ser-2 phosphorylation and ste11 transcription. Hence, in addition to starting meiosis, Mei2 functions to reinforce the commitment to it, once cells have entered this process. This study also demonstrates clearly that the stress-responsive MAP kinase pathway can modulates gene expression through phosphorylation of Pol II CTD.","doi":"10.1371/journal.pgen.1002387","authors":"Sukegawa Y, Yamashita A, Yamamoto M","authors_abbrev":"Sukegawa Y et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-12-07","publication_year":"2011","canto_session_key":"f14b30da9b0b94c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-28 16:13:18","canto_approved_date":"2026-04-11 20:16:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-11 09:44:58","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":66,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPBC32C12.02","SPBC29B5.01","SPAC19B12.05c","SPBC19C2.05","SPBC409.07c","SPAC24B11.06c","SPBC530.13","SPAC2F3.15","SPAC9G1.02","SPBC887.10","SPBC28F2.12","SPCC4B3.08","SPAC1006.09"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2017-07-28"},{"uniquename":"PMID:41419316","title":"Chromosome Ends in Motion: Telomeres as Hazards and Hubs in Meiosis.","citation":"Cold Spring Harb Perspect Biol 2025 Dec 19;","abstract":"Beyond their well-known roles in chromosome end protection, telomeres play critical roles in ensuring the fidelity of meiosis, the specialized cell division underlying sexual reproduction. Central to this process is the conserved telomere bouquet, a polarized nuclear arrangement in which telomeres cluster beneath the centrosome. The telomere bouquet orchestrates movements of meiotic chromosomes that facilitate pairing and recombination between homologous chromosomes, the defining events of meiosis. Here, we review both this canonical function and newly discovered meiotic telomere functions. We focus on three species-fission yeast, budding yeast, and mouse-that highlight both general principles and novel insights likely to be broadly applicable across eukaryotes. We propose that these diverse telomere functions provided early eukaryotes with a powerful adaptive advantage, contributing to the evolutionary success of linear chromosomes.","doi":"10.1101/cshperspect.a041705","authors":"Thadani R, Johnson N, Cooper JP","authors_abbrev":"Thadani R et al.","pubmed_publication_date":"19 Dec 2025","pubmed_entrez_date":"2025-12-19","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-12-21 00:25:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26204128","title":"Condensin targets and reduces unwound DNA structures associated with transcription in mitotic chromosome condensation.","citation":"Nat Commun 2015 Jul 23;6:7815","abstract":"Chromosome condensation is a hallmark of mitosis in eukaryotes and is a prerequisite for faithful segregation of genetic material to daughter cells. Here we show that condensin, which is essential for assembling condensed chromosomes, helps to preclude the detrimental effects of gene transcription on mitotic condensation. ChIP-seq profiling reveals that the fission yeast condensin preferentially binds to active protein-coding genes in a transcription-dependent manner during mitosis. Pharmacological and genetic attenuation of transcription largely rescue bulk chromosome segregation defects observed in condensin mutants. We also demonstrate that condensin is associated with and reduces unwound DNA segments generated by transcription, providing a direct link between an in vitro activity of condensin and its in vivo function. The human condensin isoform condensin I also binds to unwound DNA regions at the transcription start sites of active genes, implying that our findings uncover a fundamental feature of condensin complexes.","doi":"10.1038/ncomms8815","authors":"Sutani T, Sakata T, Nakato R, Masuda K, Ishibashi M, Yamashita D, Suzuki Y, Hirano T, Bando M, Shirahige K","authors_abbrev":"Sutani T et al.","pubmed_publication_date":"23 Jul 2015","pubmed_entrez_date":"2015-07-24","publication_year":"2015","canto_session_key":"72550f54ce3fc90d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-07-25 00:20:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.06c","SPBC146.03c","SPAC1002.15c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:12668659","title":"An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation.","citation":"J Cell Biol 2003 Mar 31;160(7):1093-103","abstract":"Anillin is a conserved protein required for cell division (Field, C.M., and B.M. Alberts. 1995. J. Cell Biol. 131:165-178; Oegema, K., M.S. Savoian, T.J. Mitchison, and C.M. Field. 2000. J. Cell Biol. 150:539-552). One fission yeast homologue of anillin, Mid1p, is necessary for the proper placement of the division site within the cell (Chang, F., A. Woollard, and P. Nurse. 1996. J. Cell Sci. 109(Pt 1):131-142; Sohrmann, M., C. Fankhauser, C. Brodbeck, and V. Simanis. 1996. Genes Dev. 10:2707-2719). Here, we identify and characterize a second fission yeast anillin homologue, Mid2p, which is not orthologous with Mid1p. Mid2p localizes as a single ring in the middle of the cell after anaphase in a septin- and actin-dependent manner and splits into two rings during septation. Mid2p colocalizes with septins, and mid2 Delta cells display disorganized, diffuse septin rings and a cell separation defect similar to septin deletion strains. mid2 gene expression and protein levels fluctuate during the cell cycle in a sep1- and Skp1/Cdc53/F-box (SCF)-dependent manner, respectively, implying that Mid2p activity must be carefully regulated. Overproduction of Mid2p depolarizes cell growth and affects the organization of both the septin and actin cytoskeletons. In the presence of a nondegradable Mid2p fragment, the septin ring is stabilized and cell cycle progression is delayed. These results suggest that Mid2p influences septin ring organization at the site of cell division and its turnover might normally be required to permit septin ring disassembly.","authors":"Tasto JJ, Morrell JL, Gould KL","authors_abbrev":"Tasto JJ et al.","pubmed_publication_date":"31 Mar 2003","pubmed_entrez_date":"2003-04-02","publication_year":"2003","canto_session_key":"5e5f2a97efafec91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-08-15 14:08:42","canto_approved_date":"2025-09-03 13:27:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-30 14:05:22","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPYUG7.03c","SPBC1718.01","SPBC14C8.01c","SPBC409.05","SPAC4D7.03","SPBC16G5.01","SPAC9G1.11c","SPAC19G12.01c","SPCC4B3.15","SPBC4C3.12"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2019-08-15"},{"uniquename":"PMID:18310102","title":"Two conserved modules of Schizosaccharomyces pombe Mediator regulate distinct cellular pathways.","citation":"Nucleic Acids Res 2008 May;36(8):2489-504","abstract":"Mediator is an evolutionary conserved coregulator complex required for transcription of almost all RNA polymerase II-dependent genes. The Schizosaccharomyces pombe Mediator consists of two dissociable components-a core complex organized into a head and middle domain as well as the Cdk8 regulatory subcomplex. In this work we describe a functional characterization of the S. pombe Mediator. We report the identification of the S. pombe Med20 head subunit and the isolation of ts alleles of the core head subunit encoding med17+. Biochemical analysis of med8(ts), med17(ts), Deltamed18, Deltamed20 and Deltamed27 alleles revealed a stepwise head domain molecular architecture. Phenotypical analysis of Cdk8 and head module alleles including expression profiling classified the Mediator mutant alleles into one of two groups. Cdk8 module mutants flocculate due to overexpression of adhesive cell-surface proteins. Head domain-associated mutants display a hyphal growth phenotype due to defective expression of factors required for cell separation regulated by transcription factor Ace2. Comparison with Saccharomyces cerevisiae Mediator expression data reveals that these functionally distinct modules are conserved between S. pombe and S. cerevisiae.","doi":"10.1093/nar/gkn070","authors":"Linder T, Rasmussen NN, Samuelsen CO, Chatzidaki E, Baraznenok V, Beve J, Henriksen P, Gustafsson CM, Holmberg S","authors_abbrev":"Linder T et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-03-04","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F7.04","SPAC17G8.05","SPCP31B10.03c","SPBC14F5.08","SPAC5D6.05","SPAC17C9.05c","SPBC21.04","SPAC688.08","SPAC589.02c","SPBC31F10.04c"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:9167972","title":"Microtubule-associated coiled-coil protein Ssm4 is involved in the meiotic development in fission yeast.","citation":"Genes Cells 1997 Feb;2(2):155-66","abstract":"In fission yeast, an RNA species named meiRNA is specifically required for the promotion of the first meiotic division. To dissect the function of this RNA and its partner RNA-binding protein Mei2, we screened for high-copy-number suppressors of the arrest prior to the first meiotic division caused by loss of meiRNA.\nAnalysis of one of the suppressors, named ssm4, suggested that it encodes a coiled-coil protein carrying a microtubule-binding motif at its N-terminus. Expression of ssm4 was restricted to cells undergoing meiosis. Disruption of ssm4 affected neither vegetative growth nor conjugation, but resulted in frequent generation of asci carrying less than four spores. Tagged Ssm4 could colocalize with microtubules in mitotic cells, and was seen to localize at spindles during both the first and the second meiotic division. The microtubule-binding motif was essential for the association of Ssm4 with microtubules and for its function during meiosis, but not for the suppression of loss of meiRNA. Ssm4 appeared to possess a potential to migrate to the nucleus.\nSsm4 is a microtubule-colocalizing protein that plays a role specifically in meiosis. Ssm4 appears to modify the structure or the function of nuclear microtubules in order to promote the meiotic nuclear division.","authors":"Yamashita A, Watanabe Y, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_session_key":"da635e081661568b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-11-16 16:11:22","canto_approved_date":"2026-04-05 18:58:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 21:01:45","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPAC27D7.03c","SPNCRNA.103","SPAC27D7.13c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-11-16"},{"uniquename":"Pfam:PF08728","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC27B12.05","YOL063C"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10753748","title":"Fission yeast myosin-II isoforms assemble into contractile rings at distinct times during mitosis.","citation":"Curr Biol 2000 Apr 06;10(7):397-400","abstract":"Myosin-II is required for cytokinesis in Schizosaccharomyces pombe [1-3], but unlike other unicellular organisms, S. pombe has two structurally distinct myosin-IIs, Myo2p and Myp2p, which are required under different conditions [4]. Disruption of myo2(+) is lethal, whereas disruption of myp2(+) leads to defects in cytokinesis when nutrients are limiting and to cold-sensitivity in 1 M KCl. In dividing cells, both myosin-IIs localize to a ring in the center of the cell, which is thought to contract, separating the cytoplasms of the daughter cells. Using deconvolution microscopy, we obtained three-dimensional reconstructions of fission yeast cells expressing green fluorescent protein-labeled (GFP)-myosin-II, providing for the first time detailed images of GFP-myosin-II rings. By time-lapse microscopy, we observed ring assembly and contraction in three dimensions using GFP-tubulin as a cell cycle marker. We determined that the Myo2p ring forms in metaphase/anaphase A whereas the Myp2p ring forms much later, at the end of anaphase B. Myo2p initiates ring formation while Myp2p acts later to increase the efficiency of cytokinesis.","authors":"Bezanilla M, Wilson JM, Pollard TD","authors_abbrev":"Bezanilla M et al.","pubmed_publication_date":"06 Apr 2000","pubmed_entrez_date":"2001-02-07","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12739049","title":"Genetic conservation versus variability in mitochondria: the architecture of the mitochondrial genome in the petite-negative yeast Schizosaccharomyces pombe.","citation":"Curr Genet 2003 Aug;43(5):311-26","abstract":"The great amount of molecular information and the many molecular genetic techniques available make Schizosaccharomyces pombe an ideal model eukaryote, complementary to the budding yeast Saccharomyces cerevisiae. In particular, mechanisms involved in mitochiondrial (mt) biogenesis in fission yeast are more similar to higher eukaryotes than to budding yeast. In this review, recent findings on mt morphogenesis, DNA replication and gene expression in this model organism are summarised. A second aspect is the organisation of the mt genome in fission yeast. On the one hand, fission yeast has a strong tendency to maintain mtDNA intact; and, on the other hand, the mt genomes of naturally occurring strains show a great variability. Therefore, the molecular mechanisms behind the susceptibility to mutations in the mtDNA and the mechanisms that promote sequence variations during the evolution of the genome in fission yeast mitochondria are discussed.","authors":"Schäfer B","authors_abbrev":"Schäfer B","pubmed_publication_date":"Aug 2003","pubmed_entrez_date":"2003-05-10","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17369398","title":"A novel checkpoint mechanism regulating the G1/S transition.","citation":"Genes Dev 2007 Mar 15;21(6):649-54","abstract":"Ultraviolet irradiation of fission yeast cells in G1 phase induced a delay in chromatin binding of replication initiation factors and, consistently, a transient delay in S-phase entry. The cell cycle delay was totally dependent on the Gcn2 kinase, a sensor of the nutritional status, and was accompanied by phosphorylation of the translation initiation factor eIF2alpha and by a general depression of translation. However, the G1-specific synthesis of factors required for DNA replication was not reduced by ultraviolet radiation. The cell cycle delay represents a novel checkpoint with a novel mechanism of action that is not activated by ionizing radiation.","authors":"Tvegård T, Soltani H, Skjølberg HC, Krohn M, Nilssen EA, Kearsey SE, Grallert B, Boye E","authors_abbrev":"Tvegård T et al.","pubmed_publication_date":"15 Mar 2007","pubmed_entrez_date":"2007-03-21","publication_year":"2007","canto_session_key":"2cd215dbb75af387","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-11-16 14:48:24","canto_approved_date":"2021-09-27 19:53:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-16 14:48:15","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.09c","SPBC36B7.09","SPAC24B11.06c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-11-16"},{"uniquename":"PMID:22990236","title":"Hrp3 controls nucleosome positioning to suppress non-coding transcription in eu- and heterochromatin.","citation":"EMBO J 2012 Nov 28;31(23):4375-87","abstract":"The positioning of the nucleosome by ATP-dependent remodellers provides the fundamental chromatin environment for the regulation of diverse cellular processes acting on the underlying DNA. Recently, genome-wide nucleosome mapping has revealed more detailed information on the chromatin-remodelling factors. Here, we report that the Schizosaccharomyces pombe CHD remodeller, Hrp3, is a global regulator that drives proper nucleosome positioning and nucleosome stability. The loss of Hrp3 resulted in nucleosome perturbation across the chromosome, and the production of antisense transcripts in the hrp3Δ cells emphasized the importance of nucleosome architecture for proper transcription. Notably, perturbation of the nucleosome in hrp3 deletion mutant was also associated with destabilization of the DNA-histone interaction and cell cycle-dependent alleviation of heterochromatin silencing. Furthermore, the effect of Hrp3 in the pericentric region was found to be accomplished via a physical interaction with Swi6, and appeared to cooperate with other heterochromatin factors for gene silencing. Taken together, our data indicate that a well-positioned nucleosome by Hrp3 is important for the spatial-temporal control of transcription-associated processes.","doi":"10.1038/emboj.2012.267","authors":"Shim YS, Choi Y, Kang K, Cho K, Oh S, Lee J, Grewal SI, Lee D","authors_abbrev":"Shim YS et al.","pubmed_publication_date":"28 Nov 2012","pubmed_entrez_date":"2012-09-20","publication_year":"2012","canto_session_key":"f2e1d2aee3b4e851","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoonjung Choi","canto_first_approved_date":"2016-07-18 09:14:44","canto_approved_date":"2025-12-11 10:11:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-05 04:53:34","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Yoonjung Choi","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.05","SPAC16C9.05","SPBC800.03","SPAC664.01c","SPAC3G6.01","SPAC23H4.12","SPAC29B12.02c","SPBP35G2.10","SPAC25B8.02","SPBC6B1.07","SPAC24H6.05","SPBC428.08c","SPAC18G6.02c"],"gene_count":13,"ltp_gene_count":7,"approved_date":"2016-07-18"},{"uniquename":"PMID:6943408","title":"Cell division cycle mutants altered in DNA replication and mitosis in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1981;182(1):119-24","abstract":"A total of 59 new temperature sensitive cdc mutants are described which grow normally at 25 degrees C but become blocked at DNA replication or mitosis when incubated at 36 degrees C. Thirty-nine of the mutants are altered in cdc genes which have been identified previously. The remaining 20 mutants define 10 new cdc genes. These have been characterised physiologically, and 6 of the genes (cdc 17, 20, 21, 22, 23, 24) were found to be required for DNA replication, 2 for mitosis (cdc 27, 28), and 2 (cdc 18, 19), could not be unambiguously assigned to either DNA replication or mitosis but were definitely required for one or the other. Three genes, the previously identified cdc 10, and cdc 20, 22 are likely to be required for the initiation of DNA replication. Mutants in two genes, cdc 17, 24 undergo bulk DNA synthesis at 36 degrees C, but this DNA is defective. In the case of cdc 17 the defect is in the ligation of Okazaki fragments. cdc 23 is required for bulk DNA synthesis, whilst cdc 21 may possibly be required for the initiation of a particular sub-set of replicons. A previously isolated mutant cdc 13.117 is also further described. This mutant becomes blocked in the middle of mitosis with apparently condensed chromosomes.","authors":"Nasmyth K, Nurse P","authors_abbrev":"Nasmyth K et al.","pubmed_publication_date":"1981","pubmed_entrez_date":"1981-01-01","publication_year":"1981","canto_session_key":"1fc9028e783f6d2f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2015-01-05 14:17:25","canto_approved_date":"2026-03-11 15:58:47","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-18 12:32:23","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":12,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC19C2.01","SPBC14C8.07c","SPBC1734.02c","SPBC25H2.13c","SPBC1347.10","SPBC4.04c","SPAC1F7.05","SPAC20G8.01","SPCC16A11.17","SPBC336.12c","SPBC21.06c","SPAC8F11.07c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2015-01-05"},{"uniquename":"PMID:30652128","title":"Heterochromatin suppresses gross chromosomal rearrangements at centromeres by repressing Tfs1/TFIIS-dependent transcription.","citation":"Commun Biol 2019;2:17","abstract":"Heterochromatin, characterized by histone H3 lysine 9 (H3K9) methylation, assembles on repetitive regions including centromeres. Although centromeric heterochromatin is important for correct segregation of chromosomes, its exact role in maintaining centromere integrity remains elusive. Here, we found in fission yeast that heterochromatin suppresses gross chromosomal rearrangements (GCRs) at centromeres. Mutations in Clr4/Suv39 methyltransferase increased the formation of isochromosomes, whose breakpoints were located in centromere repeats. H3K9A and H3K9R mutations also increased GCRs, suggesting that Clr4 suppresses centromeric GCRs via H3K9 methylation. HP1 homologs Swi6 and Chp2 and the RNAi component Chp1 were the chromodomain proteins essential for full suppression of GCRs. Remarkably, mutations in RNA polymerase II (RNAPII) or Tfs1/TFIIS, the transcription factor that facilitates restart of RNAPII after backtracking, specifically bypassed the requirement of Clr4 for suppressing GCRs. These results demonstrate that heterochromatin suppresses GCRs by repressing Tfs1-dependent transcription of centromere repeats.","doi":"10.1038/s42003-018-0251-z","authors":"Okita AK, Zafar F, Su J, Weerasekara D, Kajitani T, Takahashi TS, Kimura H, Murakami Y, Masukata H, Nakagawa T","authors_abbrev":"Okita AK et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-01-18","publication_year":"2019","canto_session_key":"bad7d44a253000ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takuro Nakagawa","canto_first_approved_date":"2019-02-04 16:16:34","canto_approved_date":"2025-07-02 16:37:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-26 05:20:56","canto_added_date":"2019-01-19 01:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":100,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Takuro Nakagawa","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPBP23A10.14c","SPAC6F12.09","SPCC188.13c","SPAC20H4.03c","SPBC21C3.16c","SPBC1D7.04","SPBC36.05c","SPBC8D2.04","SPCC622.16c","SPBC28F2.12","SPCC736.11","SPCC1442.10c","SPAC18G6.02c","SPBC16D10.07c","SPAC140.03","SPAC12G12.13c","SPCC11E10.08","SPAC664.01c","SPBC13E7.08c","SPBC83.03c","SPAC13G7.07","SPBC428.08c","SPAC644.14c","SPBC16C6.10"],"gene_count":25,"ltp_gene_count":24,"approved_date":"2019-02-04"},{"uniquename":"PMID:23416107","title":"Structure of a ubiquitin E1-E2 complex: insights to E1-E2 thioester transfer.","citation":"Mol Cell 2013 Mar 07;49(5):884-96","abstract":"Ubiquitin (Ub) conjugation is initiated by an E1 enzyme that catalyzes carboxy-terminal Ub adenylation, thioester bond formation to a catalytic cysteine in the E1 Cys domain, and thioester transfer to a catalytic cysteine in E2 conjugating enzymes. How the E1 and E2 active sites come together during thioester transfer and how Ub E1 interacts with diverse Ub E2s remains unclear. Here we present a crystal structure of a Ub E1-E2(Ubc4)/Ub/ATP·Mg complex that was stabilized by induction of a disulfide bond between the E1 and E2 active sites. The structure reveals combinatorial recognition of the E2 by the E1 ubiquitin-fold domain (UFD) and Cys domain and mutational analysis, coupled with thioester transfer assays with E1, Ubc4, and other Ub E2s, show that both interfaces are important for thioester transfer. Comparison to a Ub E1/Ub/ATP·Mg structure reveals conformational changes in the E1 that bring the E1 and E2 active sites together.","doi":"10.1016/j.molcel.2013.01.013","authors":"Olsen SK, Lima CD","authors_abbrev":"Olsen SK et al.","pubmed_publication_date":"07 Mar 2013","pubmed_entrez_date":"2013-02-19","publication_year":"2013","canto_session_key":"285ddfe564bdf7e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-28 15:10:04","canto_approved_date":"2024-03-28 14:26:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-10-09 15:36:36","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":132,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC211.07c","SPAC11E3.04c","SPBC2D10.20","SPAC1250.03","SPBC119.02","SPAC18B11.07c","SPBC337.08c","SPAC1805.12c","SPCC1259.15c","SPBC1604.21c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2017-01-28","pdb_entries":[{"pdb_id":"4ii3","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A/C","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-76"}],"title":"Crystal structure of S. pombe Ubiquitin activating enzyme 1 (Uba1) in complex with ubiquitin and ATP/Mg","entry_authors":"Olsen SK,Lima CD","entry_authors_abbrev":"Olsen SK et al.","reference_uniquename":"PMID:23416107","experimental_method":"X-ray","resolution":"2.9"},{"pdb_id":"4ii2","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B","position":"1-76"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Crystal structure of Ubiquitin activating enzyme 1 (Uba1) in complex with the Ub E2 Ubc4, ubiquitin, and ATP/Mg","entry_authors":"Olsen SK,Lima CD","entry_authors_abbrev":"Olsen SK et al.","reference_uniquename":"PMID:23416107","experimental_method":"X-ray","resolution":"2.2"}]},{"uniquename":"PMID:39312221","title":"Agar lot-specific inhibition in the plating efficiency of yeast spores and cells.","citation":"G3 (Bethesda) 2024 Sep 23;","abstract":"The fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae are highly diverged (530 mya), single-celled, model eukaryotic organisms. Scientists employ mating, meiosis, and the plating of ascospores and cells to generate strains with novel genotypes and to discover biological processes. Our three laboratories encountered independently sudden-onset, major impediments to such research. Spore suspensions and vegetative cells no longer plated effectively on minimal media. By systematically analyzing multiple different media components from multiple different suppliers, we identified the source of the problem. Specific lots of agar were toxic. We report that this sporadic toxicity affects independently the agar stocks of multiple vendors, has occurred repeatedly over at least three decades, and extends to species in highly diverged taxa. Interestingly, the inhibitory effects displayed variable penetrance and were attenuated on rich media. Consequently, quality control checks that use only rich media can provide false assurances on the quality of the agar. Lastly, we describe likely sources of the toxicity and we provide specific guidance for quality control measures that should be applied by all vendors as preconditions for their sale of agar.","doi":"10.1093/g3journal/jkae229","authors":"Protacio RU, Davidson MK, Malone EG, Helmlinger D, Smith JR, Gibney PA, Wahls WP","authors_abbrev":"Protacio RU et al.","pubmed_publication_date":"23 Sep 2024","pubmed_entrez_date":"2024-09-23","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-09-23 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17374714","title":"Ubiquitylation of histone H2B controls RNA polymerase II transcription elongation independently of histone H3 methylation.","citation":"Genes Dev 2007 Apr 01;21(7):835-47","abstract":"Transcription by RNA polymerase II (polII) is accompanied by dramatic changes in chromatin structure. Numerous enzymatic activities contribute to these changes, including ATP-dependent nucleosome remodeling enzymes and histone modifying enzymes. Recent studies in budding yeast document a histone modification pathway associated with polII transcription, whereby ubiquitylation of histone H2B leads to methylation of histone H3 on specific lysine residues. Although this series of events appears to be highly conserved among eukaryotes, its mechanistic function in transcription is unknown. Here we document a significant functional divergence between ubiquitylation of H2B and methylation of Lys 4 on histone H3 in the fission yeast Schizosaccharomyces pombe. Loss of H2B ubiquitylation results in defects in cell growth, septation, and nuclear structure, phenotypes not observed in cells lacking H3 Lys 4 methylation. Consistent with these results, gene expression microarray analysis reveals a greater role for H2B ubiquitylation in gene regulation than for H3 Lys 4 methylation. Chromatin immunoprecipitation (ChIP) experiments demonstrate that loss of H2B ubiquitylation alters the distribution of polII and histones in gene coding regions. We propose that ubiquitylation of H2B impacts transcription elongation and nuclear architecture through its effects on chromatin dynamics.","authors":"Tanny JC, Erdjument-Bromage H, Tempst P, Allis CD","authors_abbrev":"Tanny JC et al.","pubmed_publication_date":"01 Apr 2007","pubmed_entrez_date":"2007-03-22","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPCC622.09","SPCC1919.15","SPAC18B11.07c","SPCC970.10c"],"gene_count":4,"ltp_gene_count":3},{"uniquename":"PMID:22244753","title":"Telomerase and telomere-associated proteins: structural insights into mechanism and evolution.","citation":"Structure 2012 Jan 11;20(1):28-39","abstract":"Recent advances in our structural understanding of telomerase and telomere-associated proteins have contributed significantly to elucidating the molecular mechanisms of telomere maintenance. The structures of telomerase TERT domains have provided valuable insights into how experimentally identified conserved motifs contribute to the telomerase reverse transcriptase reaction. Additionally, structures of telomere-associated proteins in a variety of organisms have revealed that, across evolution, telomere-maintenance mechanisms employ common structural elements. For example, the single-stranded 3' overhang of telomeric DNA is specifically and tightly bound by an OB-fold in nearly all species, including ciliates (TEBP and Pot1a), fission yeast (SpPot1), budding yeast (Cdc13), and humans (hPOT1). Structures of the yeast Cdc13, Stn1, and Ten1 proteins demonstrated that telomere maintenance is regulated by a complex that bears significant similarity to the RPA heterotrimer. Similarly, proteins that specifically bind double-stranded telomeric DNA in divergent species use homeodomains to execute their functions (human TRF1 and TRF2 and budding yeast ScRap1). Likewise, the conserved protein Rap1, which is found in budding yeast, fission yeast, and humans, contains a structural motif that is known to be critical for protein-protein interaction. In addition to revealing the common underlying themes of telomere maintenance, structures have also elucidated the specific mechanisms by which many of these proteins function, including identifying a telomere-specific domain in Stn1 and how the human TRF proteins avoid heterodimerization. In this review, we summarize the high-resolution structures of telomerase and telomere-associated proteins and discuss the emergent common structural themes among these proteins. We also address how these high-resolution structures complement biochemical and cellular studies to enhance our understanding of telomere maintenance and function.","doi":"10.1016/j.str.2011.10.017","authors":"Lewis KA, Wuttke DS","authors_abbrev":"Lewis KA et al.","pubmed_publication_date":"11 Jan 2012","pubmed_entrez_date":"2012-01-17","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33434270","title":"Comparison of loop extrusion and diffusion capture as mitotic chromosome formation pathways in fission yeast.","citation":"Nucleic Acids Res 2021 Feb 22;49(3):1294-1312","abstract":"Underlying higher order chromatin organization are Structural Maintenance of Chromosomes (SMC) complexes, large protein rings that entrap DNA. The molecular mechanism by which SMC complexes organize chromatin is as yet incompletely understood. Two prominent models posit that SMC complexes actively extrude DNA loops (loop extrusion), or that they sequentially entrap two DNAs that come into proximity by Brownian motion (diffusion capture). To explore the implications of these two mechanisms, we perform biophysical simulations of a 3.76 Mb-long chromatin chain, the size of the long Schizosaccharomyces pombe chromosome I left arm. On it, the SMC complex condensin is modeled to perform loop extrusion or diffusion capture. We then compare computational to experimental observations of mitotic chromosome formation. Both loop extrusion and diffusion capture can result in native-like contact probability distributions. In addition, the diffusion capture model more readily recapitulates mitotic chromosome axis shortening and chromatin compaction. Diffusion capture can also explain why mitotic chromatin shows reduced, as well as more anisotropic, movements, features that lack support from loop extrusion. The condensin distribution within mitotic chromosomes, visualized by stochastic optical reconstruction microscopy (STORM), shows clustering predicted from diffusion capture. Our results inform the evaluation of current models of mitotic chromosome formation.","doi":"10.1093/nar/gkaa1270","authors":"Gerguri T, Fu X, Kakui Y, Khatri BS, Barrington C, Bates PA, Uhlmann F","authors_abbrev":"Gerguri T et al.","pubmed_publication_date":"22 Feb 2021","pubmed_entrez_date":"2021-01-12","publication_year":"2021","canto_session_key":"ae47abf8322de31d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasutaka Kakui","canto_first_approved_date":"2021-02-11 13:01:55","canto_approved_date":"2022-07-27 16:31:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-03 03:38:45","canto_added_date":"2021-01-14 01:15:06","annotation_curators":[{"name":"Yasutaka Kakui","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-02-11"},{"uniquename":"EMBL:AU011817","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8589058","title":"Effect of phenylarsine oxide on the fission yeast Schizosaccharomyces pombe cell cycle.","citation":"Biochimie 1995;77(4):279-87","abstract":"Phosphotyrosyl turnover is an essential regulatory mechanism for many biological processes, and the balance between tyrosine kinases and phosphatases plays a major role in the control of cell proliferation. Phenylarsine oxide (PAO), a potent inhibitor of tyrosine phosphatases (PTPase), was used to investigate the involvement of PTPase in the growth and control of the cell cycle of the fission yeast Schizosaccharomyces pombe. Cell proliferation was arrested by treatment with PAO, which was found to inhibit cdc25 PTPase in vitro but appeared not to act in vivo on this mitosis inducer. The PAO-treated cells displayed a mono- or binucleated phenotype and a DNA content that was either 2C or 4C, indicating a cell cycle arrest with a failure to complete cytokinesis. Entry into the cell division cycle from the G0 quiescent stage was also delayed by treatment with PAO. These results suggest that a number of key events in the mitotic cell cycle are regulated by as yet unidentified PTPases.","authors":"Oustrin ML, Belenguer P, Leroy D, Hoffmann I, Ducommun B","authors_abbrev":"Oustrin ML et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40187481","title":"Where to grow and where to go.","citation":"Fungal Genet Biol 2025 Apr 03;:103983","abstract":"Filamentous fungi grow as very elongated tubular cells that extend by membrane extension and cell-wall biosynthesis. Membrane and enzyme delivery depend on secretory vesicles that travel along microtubules, accumulate in a structure called the Spitzenkörper and then move along actin cables towards the apical membrane. Whereas vesicle fusion and membrane insertion are well studied, less is known about the mechanisms with which the zones of vesicle fusion and hence the growth zones are defined. One mechanism by how polarity is established and maintained is the polar localization of cell-end marker proteins (CEMPs). They form multi-protein complexes with formin as F-actin polymerase. CEMPs delivery depends on microtubules, and hence CEMPs coordinate the microtubule with the actin cytoskeleton. Actin filaments capture microtubule ends, and this positive feed-back loop quickly establishes active growth sites. However, CEMP complexes are self-limiting, because fusing vesicles disturb local growth zones and Ca 2+  influx pulses lead to F-actin disassembly. This model emerged from studies in Schizosaccharomyces pombe and Aspergillus nidulans. Surprisingly, deletion of CEMP-coding genes is not lethal. S. pombe mutants form T-shaped cells and A. nidulans germlings grow less straight. In comparison, CEMP-mutants had a strong phenotype in Arthrobotrys flagrans, a nematode-trapping fungus which produces ring-like trapping structures. CEMP-mutants fail to form adhesive rings and instead form sticks. CEMP overexpression caused a hyperbranching phenotype. Hence, CEMPs are involved in polarity maintenance and play critical roles during modulations of polarity. Here, we are going to discuss the functions of CEMPs and their connections to other polarity determinants.","doi":"10.1016/j.fgb.2025.103983","authors":"Kriegler M, Herrero S, Fischer R","authors_abbrev":"Kriegler M et al.","pubmed_publication_date":"03 Apr 2025","pubmed_entrez_date":"2025-04-05","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-04-06 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1604.20c","SPCC1223.06","SPAC110.03"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"EMBL:AU013303","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25884495","title":"Virtual-'light-sheet' single-molecule localisation microscopy enables quantitative optical sectioning for super-resolution imaging.","citation":"PLoS One 2015;10(4):e0125438","abstract":"Single-molecule super-resolution microscopy allows imaging of fluorescently-tagged proteins in live cells with a precision well below that of the diffraction limit. Here, we demonstrate 3D sectioning with single-molecule super-resolution microscopy by making use of the fitting information that is usually discarded to reject fluorophores that emit from above or below a virtual-'light-sheet', a thin volume centred on the focal plane of the microscope. We describe an easy-to-use routine (implemented as an open-source ImageJ plug-in) to quickly analyse a calibration sample to define and use such a virtual light-sheet. In addition, the plug-in is easily usable on almost any existing 2D super-resolution instrumentation. This optical sectioning of super-resolution images is achieved by applying well-characterised width and amplitude thresholds to diffraction-limited spots that can be used to tune the thickness of the virtual light-sheet. This allows qualitative and quantitative imaging improvements: by rejecting out-of-focus fluorophores, the super-resolution image gains contrast and local features may be revealed; by retaining only fluorophores close to the focal plane, virtual-'light-sheet' single-molecule localisation microscopy improves the probability that all emitting fluorophores will be detected, fitted and quantitatively evaluated.","doi":"10.1371/journal.pone.0125438","authors":"Palayret M, Armes H, Basu S, Watson AT, Herbert A, Lando D, Etheridge TJ, Endesfelder U, Heilemann M, Laue E, Carr AM, Klenerman D, Lee SF","authors_abbrev":"Palayret M et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-04-18","publication_year":"2015","canto_session_key":"7a54711bfaff58df","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-06-02 00:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25618338","title":"A method for high-throughput analysis of chronological aging in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2015;1263:93-101","abstract":"The measurement of chronological life span (CLS) in Schizosaccharomyces pombe is traditionally performed by plating back aliquots of aging liquid cultures on solid medium and counting the number of colony-forming units (CFU). However, this method is labor and cost intensive and therefore not amenable to high-throughput screening. Here, we describe a simple method for CLS measurement using aging minicultures in microtiter plates and batch plate-back for the determination of culture viability. This assay can be used to screen a large number of strains, conditions, or compounds in parallel for effects on aging.","doi":"10.1007/978-1-4939-2269-7_7","authors":"Stephan J, Ehrenhofer-Murray AE","authors_abbrev":"Stephan J et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-01-26","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-01-28 01:15:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733410","title":"Radioactive Labeling and Fractionation of Fission Yeast Walls.","citation":"Cold Spring Harb Protoc 2017 Nov 01;2017(11):pdb.prot091744","abstract":"Fungal cells contain an essential structure external to the cell, made of polysaccharides and proteins, termed the cell wall. Polysaccharides represent ∼96% of the cell wall on a dry-weight basis. They are complex insoluble polymers connected to each other by covalent linkages and hydrogen bonds with specific localizations in the cell wall and septum. Fission yeast contains three β-glucans (a major branched β(1,3)-glucan, a minor linear β(1,3)-glucan, and a minor branched β(1,6)-glucan), two α-glucans (a major α(1,3)-glucan and a minor α(1,4)-glucan), and a minor amount of galactomannan-linked glycoproteins. We provide here a simple protocol to label uniformly the cell wall using d-[U- 14 C]-glucose as a carbon source and to fractionate the cell wall into the three or four main cell wall components: galactomannoproteins, α-glucan, and β-glucan, which can be subdivided into β(1,3)-glucan and β(1,6)-glucan. This simple protocol uses enzymatic and chemical fractionations of the different cell wall components that permit the quantification of each polysaccharide in the cell wall and in the cell. This protocol is very useful for the analysis of the many morphological alterations caused by a variety of cellular processes that ultimately affect the cell wall and thus cell morphogenesis.","doi":"10.1101/pdb.prot091744","authors":"Pérez P, Ribas JC","authors_abbrev":"Pérez P et al.","pubmed_publication_date":"01 Nov 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22426534","title":"DNA replication through hard-to-replicate sites, including both highly transcribed RNA Pol II and Pol III genes, requires the S. pombe Pfh1 helicase.","citation":"Genes Dev 2012 Mar 15;26(6):581-93","abstract":"Replication forks encounter impediments as they move through the genome, including natural barriers due to stable protein complexes and highly transcribed genes. Unlike lesions generated by exogenous damage, natural barriers are encountered in every S phase. Like humans, Schizosaccharomyces pombe encodes a single Pif1 family DNA helicase, Pfh1. Here, we show that Pfh1 is required for efficient fork movement in the ribosomal DNA, the mating type locus, tRNA, 5S ribosomal RNA genes, and genes that are highly transcribed by RNA polymerase II. In addition, converged replication forks accumulated at all of these sites in the absence of Pfh1. The effects of Pfh1 on DNA replication are likely direct, as it had high binding to sites whose replication was impaired in its absence. Replication in the absence of Pfh1 resulted in DNA damage specifically at those sites that bound high levels of Pfh1 in wild-type cells and whose replication was slowed in its absence. Cells depleted of Pfh1 were inviable if they also lacked the human TIMELESS homolog Swi1, a replisome component that stabilizes stalled forks. Thus, Pfh1 promotes DNA replication and separation of converged replication forks and suppresses DNA damage at hard-to-replicate sites.","doi":"10.1101/gad.184697.111","authors":"Sabouri N, McDonald KR, Webb CJ, Cristea IM, Zakian VA","authors_abbrev":"Sabouri N et al.","pubmed_publication_date":"15 Mar 2012","pubmed_entrez_date":"2012-03-20","publication_year":"2012","canto_session_key":"79ecbc11c0699149","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nasim Sabouri","canto_first_approved_date":"2015-12-22 14:59:25","canto_approved_date":"2022-07-29 08:32:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-22 11:18:49","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Nasim Sabouri","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.08c","SPCC622.09","SPBC887.14c","SPBC216.06c","SPBC32H8.12c","SPCC330.05c"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2015-12-22"},{"uniquename":"PMID:31777167","title":"A new adaptation strategy to glucose starvation: modulation of the gluconate shunt and pentose phosphate pathway by the transcriptional repressor Rsv1.","citation":"FEBS J 2020 Mar;287(5):874-877","abstract":"Survival upon glucose starvation requires a delicate balance between different metabolic pathways. A recent work by the Roe laboratory provides a mechanistic link between glucose deprivation and the regulation of the pentose phosphate pathway, with the transcriptional repressor Rsv1 playing a key role in the process. Rsv1 regulates the flow of glucose into its possible metabolic fates and promotes long-term survival under low glucose.","doi":"10.1111/febs.15131","authors":"Fraile R, Sánchez-Mir L, Hidalgo E","authors_abbrev":"Fraile R et al.","pubmed_publication_date":"Mar 2020","pubmed_entrez_date":"2019-11-29","publication_year":"2020","canto_session_key":"b73717b23fe09691","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-11-30 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.09","SPBC106.10"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:12695334","title":"Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms.","citation":"Genes Dev 2003 May 01;17(9):1130-40","abstract":"The signalosome is implicated in regulating cullin-dependent ubiquitin ligases. We find that two signalosome subunits, Csn1 and Csn2, are required to regulate ribonucleotide reductase (RNR) through the degradation of a small protein, Spd1, that acts to anchor the small RNR subunit in the nucleus. Spd1 destruction correlates with the nuclear export of the small RNR subunit, which, in turn, correlates with a requirement for RNR in replication and repair. Spd1 degradation is promoted by two separate CSN-dependent mechanisms. During unperturbed S phase, Spd1 degradation is independent of checkpoint proteins. In irradiated G2 cells, Spd1 degradation requires the DNA damage checkpoint. The signalosome copurifies with Pcu4 (cullin 4). Pcu4, Csn1, and Csn2 promote the degradation of Spd1, identifying a new function for the signalosome as a regulator of Pcu4-containing E3 ubiquitin ligase.","authors":"Liu C, Powell KA, Mundt K, Wu L, Carr AM, Caspari T","authors_abbrev":"Liu C et al.","pubmed_publication_date":"01 May 2003","pubmed_entrez_date":"2003-04-16","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.03","SPBC25D12.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12206458","title":"Initiation of eukaryotic DNA replication: regulation and mechanisms.","citation":"Prog Nucleic Acid Res Mol Biol 2002;72:41-94","abstract":"The accurate and timely duplication of the genome is a major task for eukaryotic cells. This process requires the cooperation of multiple factors to ensure the stability of the genetic information of each cell. Mutations, rearrangements, or loss of chromosomes can be detrimental to a single cell as well as to the whole organism, causing failures, disease, or death. Because of the size of eukaryotic genomes, chromosomal duplication is accomplished in a multiparallel process. In human somatic cells between 10,000 and 100,000 parallel synthesis sites are present. This raises fundamental problems for eukaryotic cells to coordinate the start of DNA replication at each origin and to prevent replication of already duplicated DNA regions. Since these general phenomena were recognized in the middle of the 20th century the regulation and mechanisms of the initiation of eukaryotic DNA replication have been intensively investigated. These studies were carried out to find the essential factors involved in the process and to determine their functions during DNA replication. These studies gave rise to a model of the organization and the coordination of DNA replication within the eukaryotic cell. The elegant experiments carried out by Rao and Johnson (1970) (1), who fused cells in different phases of the cell cycle, showed that G1 cells are competent for replication of their chromosomes, but lack a specific diffusible factor required to activate their replicaton machinery and showed that G2 cells are incompetent for DNA replication. These findings suggested that eukaryotic cells exist in two states. In G1 phase, cells are competent to initiate DNA replication, which is subsequently triggered in S phase. After completion of S phase, cells in G2 are no longer able to initiate DNA replication and they require a transition through mitosis to reenable initiation of DNA replication to take place in the next S phase. The Xenopus cell-free replication system has proved a good model system in which to study DNA replication in vitro as well as the mechanism preventing rereplication within a single cell cycle (2). Studies using this system resulted in the development of a model postulating the existence of a replication licensing factor, which binds to chromatin before the G1-S transition and which is displaced during replication (2, 3). These results were supported by genetic and biochemical experiments in Saccharomyces cerevisiae (budding yeast) and Schizosaccharomyces pombe (fission yeast) (4, 5). The investigation of cell division cycle mutants and the budding yeast origin of replication resulted in the concept of a prereplicative and a postreplicative complex of initiation proteins (6-9). These three individual concepts have recently started to merge and it has become obvious that initiation in eukaryotes is generally governed by the same ubiquitous mechanisms.","authors":"Nasheuer HP, Smith R, Bauerschmidt C, Grosse F, Weisshart K","authors_abbrev":"Nasheuer HP et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-09-11","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28228545","title":"Ablation of RNA interference and retrotransposons accompany acquisition and evolution of transposases to heterochromatin protein CENPB.","citation":"Mol Biol Cell 2017 Apr 15;28(8):1132-1146","abstract":"Inactivation of retrotransposons is accompanied by the emergence of centromere-binding protein-B (CENPB) in  Schizosaccharomyces , as well as in metazoans. The RNA interference (RNAi)-induced transcriptional silencing (RITS) complex, comprising chromodomain protein-1 (Chp1), Tas3 (protein with unknown function), and Argonaute (Ago1), plays an important role in RNAi-mediated heterochromatinization. We find that whereas the Ago1 subunit of the RITS complex is highly conserved, Tas3 is lost and Chp1 is truncated in  Schizosaccharomyces cryophilus  and  Schizosaccharomyces octosporus  We show that truncated Chp1 loses the property of heterochromatin localization and silencing when transformed in  Schizosaccharomyces pombe  Furthermore, multiple copies of CENPB, related to  Tc1/mariner and Tc5  transposons, occur in all  Schizosaccharomyces  species, as well as in humans, but with loss of transposase function (except  Schizosaccharomyces japonicus ). We propose that acquisition of  Tc1/mariner and Tc5  elements by horizontal transfer in  S. pombe  (and humans) is accompanied by alteration of their function from a transposase/endonuclease to a heterochromatin protein, designed to suppress transposon expression and recombination. The resulting redundancy of RITS may have eased the selection pressure, resulting in progressive loss or truncation of  tas3  and  chp1  genes in  S. octosporus  and  S. cryophilus  and triggered similar evolutionary dynamics in the metazoan orthologues.","doi":"10.1091/mbc.E16-07-0485","authors":"Upadhyay U, Srivastava S, Khatri I, Nanda JS, Subramanian S, Arora A, Singh J","authors_abbrev":"Upadhyay U et al.","pubmed_publication_date":"15 Apr 2017","pubmed_entrez_date":"2017-02-24","publication_year":"2017","canto_session_key":"a46b0a94a546ba4b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-04-28 09:57:06","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-04-21 21:02:14","canto_added_date":"2017-02-25 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPMTR.02","SPAC26H5.06","SPCC736.11","SPAC6F12.09","SPBC14F5.12c","SPBP35G2.10","SPBC4F6.15c","SPCC613.12c","SPAC8F11.03","SPAC3A11.08","SPBC2D10.17","SPBC1778.02","SPCC11E10.08","SPBP8B7.28c","SPCC338.17c","SPAC13G7.07","SPAC688.02c","SPAC25B8.14","SPAC1783.04c","SPBC18E5.03c","SPCC1672.10","SPAC18G6.02c","SPBC1105.04c","SPCC663.12","SPCC970.07c","SPBC83.03c","SPBC1105.17","SPBC21D10.12","SPBC21.01","SPAC1B3.17","SPAC6F6.17","SPAC9E9.10c","SPCC1739.03","SPBC30D10.04","SPAC140.03","SPCC550.12","SPBC16C6.10"],"gene_count":37,"ltp_gene_count":2,"approved_date":"2017-04-21"},{"uniquename":"PMID:28567704","title":"Fission yeast Ctf1, a cleavage and polyadenylation factor subunit is required for the maintenance of genomic integrity.","citation":"Mol Genet Genomics 2017 Oct;292(5):1027-1036","abstract":"Accurate segregation of chromosome during mitosis requires the coordinated action of several cell cycle checkpoints that monitor replication of the genome and the attachment of sister chromatids to the mitotic spindle apparatus. Here we have characterized the fission yeast Ctf1, an ortholog of S. cerevisiae Rna15 in the maintenance of genomic integrity. The ctf1 is nonessential for the cell survival and its deletion strain exhibit cold sensitivity. The ctf1 deleted cells exhibit genetic interaction with spindle checkpoint protein Mad2 and Bub1. The deletion of ctf1 gene affects the chromosomal attachment to the mitotic spindle leading to the accumulation of Bub1-GFP foci. Ctf1 localizes to the nucleus and physically interacts with Rna14, a cleavage and polyadenylation factor.","doi":"10.1007/s00438-017-1329-x","authors":"Sonkar A, Gaurav S, Ahmed S","authors_abbrev":"Sonkar A et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-06-02","publication_year":"2017","canto_session_key":"429dbca477dfe4e7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-14 16:22:41","canto_approved_date":"2023-06-08 09:15:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-20 14:13:49","canto_added_date":"2017-06-03 00:15:15","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.11c","SPBC20F10.06","SPBC902.02c","SPAC644.16","SPAC6F12.17","SPCC1322.12c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2017-11-14"},{"uniquename":"PMID:40406582","title":"The  Schizosaccharomyces pombe  nucleolar protein Nsk1 modulates rDNA silencing during interphase.","citation":"MicroPubl Biol 2025;2025","abstract":" Schizosaccharomyces pombe  Nsk1 acts at kinetochores during mitosis to prevent error-prone chromosome segregation and it is phosphoregulated by Cdk1 . The Clp1 / Cdc14 protein phosphatase, to which Nsk1 binds, reverses Cdk1-mediated phosphorylation of Nsk1 during anaphase. During interphase, Nsk1 localizes exclusively to the nucleolus and its function there is unknown. In this study, we examined whether Nsk1 shares functions in the nucleolus with other known Clp1 / Cdc14 phosphatase substrates that localize there. We found that Nsk1 participates in rRNA silencing but not rDNA segregation, rDNA transcription, or nucleolar organization.","doi":"10.17912/micropub.biology.001616","authors":"Chen JS, Hanna SM, Willet AH, Gould KL","authors_abbrev":"Chen JS et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-05-23","publication_year":"2025","canto_session_key":"125b5fa1f851c229","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2025-06-10 14:39:22","canto_approved_date":"2025-06-10 14:39:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-09 20:05:19","canto_added_date":"2025-05-23 23:25:05","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":4,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP8B7.20c","SPAC140.02","SPBC25D12.02c","SPAC3G9.01","SPBC4C3.05c"],"gene_count":5,"ltp_gene_count":1,"approved_date":"2025-06-10"},{"uniquename":"PMID:3032459","title":"Negative regulation of mitosis by wee1+, a gene encoding a protein kinase homolog.","citation":"Cell 1987 May 22;49(4):559-67","abstract":"Fission yeast wee1- mutants initiate mitosis at half the cell size of wild type. The wee1+ activity is required to prevent lethal premature mitosis in cells that overproduce the mitotic inducer cdc25+. This lethal phenotype was used to clone wee1+ by complementation. When wee1+ expression is increased, mitosis is delayed until cells grow to a larger size. Thus wee1+ functions as a dose-dependent inhibitor of mitosis, the first such element to be specifically identified and cloned. The carboxy-terminal region of the predicted 112 kd wee1+ protein contains protein kinase consensus sequences, suggesting that negative regulation of mitosis involves protein phosphorylation. Genetic evidence indicates that wee1+ and cdc25+ compete in a control system regulating the cdc2+ protein kinase, which is required for mitotic initiation.","authors":"Russell P, Nurse P","authors_abbrev":"Russell P et al.","pubmed_publication_date":"22 May 1987","pubmed_entrez_date":"1987-05-22","publication_year":"1987","canto_session_key":"890568af6939d0d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-10 13:50:26","canto_approved_date":"2019-06-14 12:52:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-05 18:45:18","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPCC18B5.03","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-09-10"},{"uniquename":"PMID:22280061","title":"DNA-RNA hybrid formation mediates RNAi-directed heterochromatin formation.","citation":"Genes Cells 2012 Mar;17(3):218-33","abstract":"Certain noncoding RNAs (ncRNAs) implicated in the regulation of chromatin structure associate with chromatin. During the formation of RNAi-directed heterochromatin in fission yeast, ncRNAs transcribed from heterochromatin are thought to recruit the RNAi machinery to chromatin for the formation of heterochromatin; however, the molecular details of this association are not clear. Here, using RNA immunoprecipitation assay, we showed that the heterochromatic ncRNA was associated with chromatin via the formation of a DNA-RNA hybrid and bound to the RNA-induced transcriptional silencing (RITS) complex. The presence of DNA-RNA hybrid in the cell was also confirmed by immunofluorescence analysis using anti-DNA-RNA hybrid antibody. Over-expression and depletion of RNase H in vivo decreased and increased the amount of DNA-RNA hybrid formed, respectively, and both disturbed heterochromatin. Moreover, DNA-RNA hybrid was formed on, and over-expression of RNase H inhibited the formation of, artificial heterochromatin induced by tethering of RITS to mRNA. These results indicate that heterochromatic ncRNAs are retained on chromatin via the formation of DNA-RNA hybrids and provide a platform for the RNAi-directed heterochromatin assembly and suggest that DNA-RNA hybrid formation plays a role in chromatic ncRNA function.","doi":"10.1111/j.1365-2443.2012.01583.x","authors":"Nakama M, Kawakami K, Kajitani T, Urano T, Murakami Y","authors_abbrev":"Nakama M et al.","pubmed_publication_date":"Mar 2012","pubmed_entrez_date":"2012-01-28","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18923417","title":"Localization of Smc5/6 to centromeres and telomeres requires heterochromatin and SUMO, respectively.","citation":"EMBO J 2008 Nov 19;27(22):3011-23","abstract":"The Smc5/6 holocomplex executes key functions in genome maintenance that include ensuring the faithful segregation of chromosomes at mitosis and facilitating critical DNA repair pathways. Smc5/6 is essential for viability and therefore, dissecting its chromosome segregation and DNA repair roles has been challenging. We have identified distinct epigenetic and post-translational modifications that delineate roles for fission yeast Smc5/6 in centromere function, versus replication fork-associated DNA repair. We monitored Smc5/6 subnuclear and genomic localization in response to different replicative stresses, using fluorescence microscopy and chromatin immunoprecipitation (ChIP)-on-chip methods. Following hydroxyurea treatment, and during an unperturbed S phase, Smc5/6 is transiently enriched at the heterochromatic outer repeats of centromeres in an H3-K9 methylation-dependent manner. In contrast, methyl methanesulphonate treatment induces the accumulation of Smc5/6 at subtelomeres, in an Nse2 SUMO ligase-dependent, but H3-K9 methylation-independent manner. Finally, we determine that Smc5/6 loads at all genomic tDNAs, a phenomenon that requires intact consensus TFIIIC-binding sites in the tDNAs.","doi":"10.1038/emboj.2008.220","authors":"Pebernard S, Schaffer L, Campbell D, Head SR, Boddy MN","authors_abbrev":"Pebernard S et al.","pubmed_publication_date":"19 Nov 2008","pubmed_entrez_date":"2008-10-17","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10950958","title":"Phosphatidylinositol 4-phosphate 5-kinase Its3 and calcineurin Ppb1 coordinately regulate cytokinesis in fission yeast.","citation":"J Biol Chem 2000 Nov 10;275(45):35600-6","abstract":"The ppb1(+) gene encodes a fission yeast homologue of the mammalian calcineurin. We have recently shown that Ppb1 is essential for chloride ion homeostasis, and acts antagonistically with Pmk1 mitogen-activated protein kinase pathway. In an attempt to identify genes that share an essential function with calcineurin, we screened for mutations that confer sensitivity to the calcineurin inhibitor FK506 and high temperature, and isolated a mutant, its3-1. its3(+) was shown to be an essential gene encoding a functional homologue of phosphatidylinositol-4-phosphate 5-kinase (PI(4)P5K). The temperature upshift or addition of FK506 induced marked disorganization of actin patches and dramatic increase in the frequency of septation in the its3-1 mutants but not in the wild-type cells. Expression of a green fluorescent protein-tagged Its3 and the phospholipase Cdelta pleckstrin homology domain indicated plasma membrane localization of PI(4)P5K and phosphatidylinositol 4,5-bisphosphate. These green fluorescent protein-tagged proteins were concentrated at the septum of dividing cells, and the mutant Its3 was no longer localized to the plasma membrane. These data suggest that fission yeast PI(4)P5K Its3 functions coordinately with calcineurin and plays a key role in cytokinesis, and that the plasma membrane localization of Its3 is the crucial event in cytokinesis.","authors":"Zhang Y, Sugiura R, Lu Y, Asami M, Maeda T, Itoh T, Takenawa T, Shuntoh H, Kuno T","authors_abbrev":"Zhang Y et al.","pubmed_publication_date":"10 Nov 2000","pubmed_entrez_date":"2000-08-22","publication_year":"2000","canto_session_key":"7fecd247a7c91847","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-11-10 12:46:53","canto_approved_date":"2026-01-22 11:16:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-10 12:40:23","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.14","SPBP4H10.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-11-10"},{"uniquename":"PMID:31050340","title":"Multi-phosphorylation reaction and clustering tune Pom1 gradient mid-cell levels according to cell size.","citation":"Elife 2019 May 03;8","abstract":"Protein concentration gradients pattern developing organisms and single cells. In  Schizosaccharomyces pombe  rod-shaped cells, Pom1 kinase forms gradients with maxima at cell poles. Pom1 controls the timing of mitotic entry by inhibiting Cdr2, which forms stable membrane-associated nodes at mid-cell. Pom1 gradients rely on membrane association regulated by a phosphorylation-dephosphorylation cycle and lateral diffusion modulated by clustering. Using quantitative PALM imaging, we find individual Pom1 molecules bind the membrane too transiently to diffuse from pole to mid-cell. Instead, we propose they exchange within longer lived clusters forming the functional gradient unit. An allelic series blocking auto-phosphorylation shows that multi-phosphorylation shapes and buffers the gradient to control mid-cell levels, which represent the critical Cdr2-regulating pool. TIRF imaging of this cortical pool demonstrates more Pom1 overlaps with Cdr2 in short than long cells, consistent with Pom1 inhibition of Cdr2 decreasing with cell growth. Thus, the gradients modulate Pom1 mid-cell levels according to cell size.","doi":"10.7554/eLife.45983","authors":"Gerganova V, Floderer C, Archetti A, Michon L, Carlini L, Reichler T, Manley S, Martin SG","authors_abbrev":"Gerganova V et al.","pubmed_publication_date":"03 May 2019","pubmed_entrez_date":"2019-05-04","publication_year":"2019","canto_session_key":"f3fd6bfb182a2df3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-05-04 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1289815","title":"Synthesis of chimeric RNAs between U6 small nuclear RNA and (-)sTRSV and analysis of their cleavage activities against the substrate RNA.","citation":"Nucleic Acids Symp Ser 1992;(27):19-20","abstract":"U6 small nuclear RNA (U6 snRNA) is one of the spliceosomal RNAs essential for pre-mRNA splicing. Highly conserved region of U6 snRNA shows a structural similarity with the catalytic center of the negative strand of the satellite RNA of tobacco ring spot virus [(-)sTRSV], supporting the hypothesis that U6 snRNA has a catalytic role in pre-mRNA splicing. To test this hypothesis, we examined in vitro whether synthetic RNAs consisting of the sequence of the highly conserved region of U6 snRNA or various chimeric RNAs between the U6 region and the catalytic center of (-)sTRSV could cleave a substrate RNA that can partially base-pair with them and has a GU sequence between the pairing regions. Chimeric RNAs with 70 to 83% sequence identity with the conserved region of S. pombe U6 snRNA cleaved the substrate RNA at the 5' side of the GU sequence. In addition, we found that the highly conserved region of U6 snRNA is similar in structure to the catalytic core region of the group I self-splicing intron in cyanobacteria. These results support the hypothesis that U6 snRNA catalyzes the pre-mRNA splicing reaction and U6 snRNA may originate from the catalytic domain of an ancient self-splicing intron.","authors":"Tani T, Takahashi Y, Ohshima Y","authors_abbrev":"Tani T et al.","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11283013","title":"Antizyme regulates the degradation of ornithine decarboxylase in fission yeast Schizosaccharomyces pombe. Study in the spe2 knockout strains.","citation":"J Biol Chem 2001 Jun 15;276(24):21235-41","abstract":"The mechanism of the regulatory degradation of ornithine decarboxylase (ODC) by polyamines was studied in fission yeast, Schizosaccharomyces pombe. To regulate cellular spermidine experimentally, we cloned and disrupted S-adenosylmethionine decarboxylase gene (spe2) in S. pombe. The null mutant of spe2 was devoid of spermidine and spermine, accumulated putrescine, and contained a high level of ODC. Addition of spermidine to the culture medium resulted in rapid decrease in the ODC activity caused by the acceleration of ODC degradation, which was dependent on de novo protein synthesis. A fraction of ODC forming an inactive complex concomitantly increased. The accelerated ODC degradation was prevented either by knockout of antizyme gene or by selective inhibitors of proteasome. Thus, unlike budding yeast, mammalian type antizyme-mediated ODC degradation by proteasome is operating in S. pombe.","authors":"Chattopadhyay MK, Murakami Y, Matsufuji S","authors_abbrev":"Chattopadhyay MK et al.","pubmed_publication_date":"15 Jun 2001","pubmed_entrez_date":"2001-04-03","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36406126","title":"A comparative analysis of telomere length maintenance circuits in fission and budding yeast.","citation":"Front Genet 2022;13:1033113","abstract":"The natural ends of the linear eukaryotic chromosomes are protected by telomeres, which also play an important role in aging and cancer development. Telomere length varies between species, but it is strictly controlled in all organisms. The process of Telomere Length Maintenance (TLM) involves many pathways, protein complexes and interactions that were first discovered in budding and fission yeast model organisms ( Saccharomyces cerevisiae ,  Schizosaccharomyces pombe ). In particular, large-scale systematic genetic screens in budding yeast uncovered a network of   ≈   500 genes that, when mutated, cause telomeres to lengthen or to shorten. In contrast, the TLM network in fission yeast remains largely unknown and systematic data is still lacking. In this work we try to close this gap and develop a unified interpretable machine learning framework for TLM gene discovery and phenotype prediction in both species. We demonstrate the utility of our framework in pinpointing the pathways by which TLM homeostasis is maintained and predicting novel TLM genes in fission yeast. The results of this study could be used for better understanding of telomere biology and serve as a step towards the adaptation of computational methods based on telomeric data for human prognosis.","doi":"10.3389/fgene.2022.1033113","authors":"Peretz I, Kupiec M, Sharan R","authors_abbrev":"Peretz I et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-11-21","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-11-23 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17102632","title":"Cdc2 tyrosine phosphorylation is not required for the S-phase DNA damage checkpoint in fission yeast.","citation":"Cell Cycle 2006 Nov 01;5(21):2495-500","abstract":"The S-phase DNA damage checkpoint slows replication when damage occurs during S phase. Cdc25, which activates Cdc2 by dephosphorylating tyrosine-15, has been shown to be a downstream target of the checkpoint in metazoans, but its role is not clear in fission yeast. The dephosphorylation of Cdc2 has been assumed not to play a role in S-phase regulation because cells replicate in the absence of Cdc25, demonstrating that tyrosine-15 phosphorylated dc2 is sufficient for S phase. However, it has been reported recently that Cdc25 is involved in the slowing of S phase in response to damage in fission yeast, suggesting a modulatory role for Cdc2 dephosphorylation in S phase. We have investigated the role of Cdc25 and the tyrosine phosphorylation of Cdc2 in the S-phase damage checkpoint, and our results show that Cdc2 phosphorylation is not a target of the checkpoint. The checkpoint was not compromised in a Cdc25 overexpressing strain, a strain carrying nonphosphorylatable form of Cdc2, or in a strain lacking Cdc25. Our results are consistent with a strictly Cdc2-Y15 phosphorylation-independent mechanism of the fission yeast S-phase DNA damage checkpoint.","authors":"Kommajosyula N, Rhind N","authors_abbrev":"Kommajosyula N et al.","pubmed_publication_date":"01 Nov 2006","pubmed_entrez_date":"2006-11-15","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36112198","title":"Synergistic roles of the phospholipase B homolog Plb1 and the cAMP-dependent protein kinase Pka1 in the hypertonic stress response of Schizosaccharomyces pombe.","citation":"Curr Genet 2022 Dec;68(5-6):661-674","abstract":"The phospholipase B homolog Plb1 and the cAMP-dependent protein kinase (PKA) pathway are required by fission yeast, also known as to Schizosaccharomyces pombe, to grow under KCl-stress conditions. Here, we report the relative contributions of Plb1 and the cAMP/PKA pathway during the hypertonic stress response. We show that the plb1∆, cyr1∆, and pka1∆ single mutants are sensitive to high concentrations of KCl but insensitive to sorbitol-induced osmotic stress. In contrast, the plb1∆ cyr1∆ and plb1∆ pka1∆ double mutants are hypersensitive to KCl and sorbitol. The cyr1∆ pka1∆ double mutants showed the same phenotype of each single mutant. Growth inhibition due to hypertonic stress in the plb1∆, plb1∆ cyr1∆, and plb1∆ pka1∆ strains was partially rescued by cgs1 deletion-cgs1∆ has constitutively active Pka1-or by the deletion of transcription factor Rst2, which is negatively regulated by Pka1. Pka1-GFP localized in the nucleus and cytoplasm in plb1∆, whereas it is localized only in the cytoplasm in cyr1∆, indicating that Plb1 does not regulate Pka1 localization. Glucose limitation downregulates the PKA pathway, and it was accordingly observed that glucose limitation in plb1∆ further increased the strain's sensitivity to KCl. Growth inhibition by KCl in plb1∆ under glucose-limited conditions was significantly rescued by cgs1∆ and slightly rescued by rst2∆. These findings indicate that, in fission yeast, Plb1 and the glucose-sensing cAMP/PKA pathway play a synergistic role in responding to hypertonic stress.","doi":"10.1007/s00294-022-01253-z","authors":"Matsuo Y, Marcus S, Kawamukai M","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"Dec 2022","pubmed_entrez_date":"2022-09-16","publication_year":"2022","canto_session_key":"8bfda07133be8ba6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Matsuo","canto_first_approved_date":"2022-11-16 16:35:26","canto_approved_date":"2025-09-02 22:34:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-11 00:20:20","canto_added_date":"2022-09-20 00:15:04","annotation_curators":[{"name":"Yasuhiro Matsuo","community_curator":true,"annotation_count":53,"orcid":"0000-0002-2858-7179","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.03","SPBC19C7.03","SPAC1A6.04c","SPAC6F12.02","SPCC1753.02c","SPBC106.10"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2022-11-16"},{"uniquename":"PMID:9745017","title":"Cell-division-cycle defects associated with fission yeast pre-mRNA splicing mutants.","citation":"Curr Genet 1998 Sep;34(3):153-63","abstract":"We have isolated six new pre-mRNA splicing mutants (prp) from a collection of temperature-sensitive (ts-) Schizosaccharomyces pombe strains. The prp mutants are defective in the splicing of both messenger RNA and U6 small nuclear RNA precursors. A single recessive mutation is responsible for both the ts- growth and the splicing phenotypes in each of the prp mutants. The six prp mutations are unlinked and fall into separate complementation groups. Two are allelic with the previously described prp3 and prp4 mutations; the remaining four define the new alleles prp5-1, prp6-1, prp7-1, and prp9-1. The six mutants exhibit three splicing phenotypes: accumulation of unspliced precursor at the restrictive but not at the permissive temperature; accumulation of unspliced precursor at both the permissive and restrictive temperatures; and accumulation of unspliced precursor, the intron-exon lariat intermediate, and the intron lariat final product. In addition to their aberrant splicing phenotypes, the prp5-1 and prp6-1 mutants express classical cell-division-cycle defects, while prp7-1 exhibits an unusual hyphal morphology. These results suggest a connection between pre-mRNA splicing and the control of cell division in fission yeast.","authors":"Potashkin J, Kim D, Fons M, Humphrey T, Frendewey D","authors_abbrev":"Potashkin J et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-09-24","publication_year":"1998","canto_session_key":"0401b77ec79d27fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-17 16:18:20","canto_approved_date":"2026-01-29 17:05:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-17 16:18:12","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.14","SPAC29E6.02","SPBC26H8.07c","SPBP22H7.07","SPSNRNA.06"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2017-08-17"},{"uniquename":"PMID:15591044","title":"Structures of complete RNA polymerase II and its subcomplex, Rpb4/7.","citation":"J Biol Chem 2005 Feb 25;280(8):7131-4","abstract":"We determined the x-ray structure of the RNA polymerase (Pol) II subcomplex Rpb4/7 at 2.3 A resolution, combined it with a previous structure of the 10-subunit polymerase core, and refined an atomic model of the complete 12-subunit Pol II at 3.8-A resolution. Comparison of the complete Pol II structure with structures of the Pol II core and free Rpb4/7 shows that the core-Rpb4/7 interaction goes along with formation of an alpha-helix in the linker region of the largest Pol II subunit and with folding of the conserved Rpb7 tip loop. Details of the core-Rpb4/7 interface explain facilitated Rpb4/7 dissociation in a temperature-sensitive Pol II mutant and specific assembly of Pol I with its Rpb4/7 counterpart, A43/14. The refined atomic model of Pol II serves as the new reference structure for analysis of the transcription mechanism and enables structure solution of complexes of the complete enzyme with additional factors and nucleic acids by molecular replacement.","authors":"Armache KJ, Mitterweger S, Meinhart A, Cramer P","authors_abbrev":"Armache KJ et al.","pubmed_publication_date":"25 Feb 2005","pubmed_entrez_date":"2004-12-14","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPACUNK4.06c","SPBC337.14"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12080074","title":"The Srk1 protein kinase is a target for the Sty1 stress-activated MAPK in fission yeast.","citation":"J Biol Chem 2002 Sep 06;277(36):33411-21","abstract":"The fission yeast stress-activated Sty1/Spc1 MAPK pathway responds to a similar range of stresses as do the mammalian p38 and SAPK/JNK MAPK pathways. In addition, sty1(-) cells are sterile and exhibit a G(2) cell cycle delay, indicating additional roles of Sty1 in meiosis and cell cycle progression. To identify novel proteins involved in stress responses, a microarray analysis of the Schizosaccharomyces pombe genome was performed to find genes that are up-regulated following exposure to stress in a Sty1-dependent manner. One such gene identified, srk1(+) (Sty1-regulated kinase 1), encodes a putative serine/threonine kinase homologous to mammalian calmodulin kinases. At the C terminus of Srk1 is a putative MAPK binding motif similar to that in the p38 substrates, MAPK-activated protein kinases 2 and 3. Indeed, we find that Srk1 is present in a complex with the Sty1 MAPK and is directly phosphorylated by Sty1. Furthermore, upon stress, Srk1 translocates from the cytoplasm to the nucleus in a process that is dependent on the Sty1 MAPK. Finally, we show that Srk1 has a role in regulating meiosis in fission yeast; following nitrogen limitation, srk1(-) cells enter meiosis significantly faster than wild-type cells and overexpression of srk1(+) inhibits the nitrogen starvation-induced arrest in G(1).","authors":"Smith DA, Toone WM, Chen D, Bahler J, Jones N, Morgan BA, Quinn J","authors_abbrev":"Smith DA et al.","pubmed_publication_date":"06 Sep 2002","pubmed_entrez_date":"2002-06-25","publication_year":"2002","canto_session_key":"ec6c2870725e0368","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-19 12:58:58","canto_approved_date":"2026-04-08 10:59:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-12 16:00:24","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":43,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.08","SPAC24B11.06c","SPBC29B5.01","SPBC409.07c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-09-19"},{"uniquename":"PMID:7898434","title":"A large circular minichromosome of Schizosaccharomyces pombe requires a high dose of type II DNA topoisomerase for its stabilization.","citation":"Mol Gen Genet 1995 Mar 20;246(6):671-9","abstract":"We have constructed circular minichromosomes, ranging in size from 36 to 110 kb, containing the centromeric repeats of Schizosaccharomyces pombe cen3. Comparison of their mitotic stability showed that the circular minichromosomes became more unstable with increasing in size, however, a linear cen3 minichromosome, which is almost the same size as the largest circular one tested, does not show such instability. High levels of expression of the top2+ (type II DNA topoisomerase; topo II) but not top1+ gene (type I DNA topoisomerase) suppressed the instability of the largest circular minichromosome, whereas partial inactivation of topo II dramatically destabilized the minichromosome. A mutant topo II, defective in nuclear localization but still retaining its in vitro relaxation activity, did not stabilize the circular minichromosome. These results indicate that endogenous type II DNA topoisomerase is insufficient for accurate segregation of the circular minichromosome. In addition, the replication of the minichromosomal DNA appears to proceed normally, because the presence of the unstable minichromosome did not cause G2 delay. A likely cause of the instability is intertwining of the minichromosome DNA possibly occurring after DNA replication. An interaction between topo II and the centromeric repeats is implied by the finding that multiple copies of the centromeric repeat, dg-dh, affect stability of the minichromosome similarly to top2+ gene dosage.","authors":"Murakami S, Yanagida M, Niwa O","authors_abbrev":"Murakami S et al.","pubmed_publication_date":"20 Mar 1995","pubmed_entrez_date":"1995-03-20","publication_year":"1995","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22328580","title":"Analysis of stress granule assembly in Schizosaccharomyces pombe.","citation":"RNA 2012 Apr;18(4):694-703","abstract":"Stress granules (SGs) are cytoplasmic aggregates of RNA and proteins in eukaryotic cells that are rapidly induced in response to environmental stress, but are not seen in cells growing under favorable conditions. SGs have been primarily studied in mammalian cells. The existence of SGs in the fission yeast and the distantly related budding yeast was demonstrated only recently. In both species, they contain many orthologs of the proteins seen in mammalian SGs. In this study, we have characterized these proteins and determined their involvement in the assembly of fission yeast SGs, in particular, the homolog of human G3BP proteins. G3BP interacts with the deubiquitinating protease USP10 and plays an important role in the assembly of SGs. We have also identified Ubp3, an ortholog of USP10, as an interaction partner of the fission yeast G3BP-like protein Nxt3 and required for its stability. Under thermal stress, like their human orthologs, both Nxt3 and Ubp3 rapidly relocalize to cytoplasmic foci that contain the SG marker poly(A)-binding protein Pabp. However, in contrast to G3BP1 and USP10, neither deletion nor overexpression of nxt3(+) or ubp3(+) affected the assembly of fission yeast SGs as judged by the relocalization of Pabp. Similar results were observed in mutants defective in orthologs of SG components that are known to affect SG assembly in human and in budding yeast, such as ataxia-2 and TIA-like proteins. Together, our data indicate that despite similar protein compositions, the underlying molecular mechanisms for the assembly of SGs could be distinct between species.","doi":"10.1261/rna.030270.111","authors":"Wang CY, Wen WL, Nilsson D, Sunnerhagen P, Chang TH, Wang SW","authors_abbrev":"Wang CY et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-02-14","publication_year":"2012","canto_session_key":"ac29fd3d76564172","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shao-Win Wang","canto_first_approved_date":"2017-04-12 17:03:55","canto_approved_date":"2023-09-26 07:21:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-06 07:32:42","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Shao-Win Wang","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP8B7.21","SPBC1711.06","SPAC17A2.09c","SPBP8B7.11","SPAC664.05","SPAPB8E5.06c","SPAC57A7.04c","SPAC13G6.02c","SPAC24H6.07","SPBC23E6.01c","SPBC21B10.03c"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2017-04-12"},{"uniquename":"PMID:20140190","title":"A kinase-independent role for the Rad3(ATR)-Rad26(ATRIP) complex in recruitment of Tel1(ATM) to telomeres in fission yeast.","citation":"PLoS Genet 2010 Feb 05;6(2):e1000839","abstract":"ATM and ATR are two redundant checkpoint kinases essential for the stable maintenance of telomeres in eukaryotes. Previous studies have established that MRN (Mre11-Rad50-Nbs1) and ATRIP (ATR Interacting Protein) interact with ATM and ATR, respectively, and recruit their partner kinases to sites of DNA damage. Here, we investigated how Tel1(ATM) and Rad3(ATR) recruitment to telomeres is regulated in fission yeast. Quantitative chromatin immunoprecipitation (ChIP) assays unexpectedly revealed that the MRN complex could also contribute to the recruitment of Tel1(ATM) to telomeres independently of the previously established Nbs1 C-terminal Tel1(ATM) interaction domain. Recruitment of Tel1(ATM) to telomeres in nbs1-c60Delta cells, which lack the C-terminal 60 amino acid Tel1(ATM) interaction domain of Nbs1, was dependent on Rad3(ATR)-Rad26(ATRIP), but the kinase domain of Rad3(ATR) was dispensable. Thus, our results establish that the Rad3(ATR)-Rad26(ATRIP) complex contributes to the recruitment of Tel1(ATM) independently of Rad3(ATR) kinase activity, by a mechanism redundant with the Tel1(ATM) interaction domain of Nbs1. Furthermore, we found that the N-terminus of Nbs1 contributes to the recruitment of Rad3(ATR)-Rad26(ATRIP) to telomeres. In response to replication stress, mammalian ATR-ATRIP also contributes to ATM activation by a mechanism that is dependent on the MRN complex but independent of the C-terminal ATM interaction domain of Nbs1. Since telomere protection and DNA damage response mechanisms are very well conserved between fission yeast and mammalian cells, mammalian ATR-ATRIP may also contribute to the recruitment of ATM to telomeres and to sites of DNA damage independently of ATR kinase activity.","doi":"10.1371/journal.pgen.1000839","authors":"Subramanian L, Nakamura TM","authors_abbrev":"Subramanian L et al.","pubmed_publication_date":"05 Feb 2010","pubmed_entrez_date":"2010-02-09","publication_year":"2010","canto_session_key":"5de6e47f8f999ca9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-03-23 16:52:41","canto_approved_date":"2024-11-29 17:02:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-23 16:52:26","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":93,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPBC660.13c","SPCC23B6.03c","SPBC6B1.09c","SPAC9E9.08"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-03-23"},{"uniquename":"PMID:40234053","title":"Structural Biology of Telomerase and Associated Factors.","citation":"Cold Spring Harb Perspect Biol 2025 Apr 15;","abstract":"Telomerase ribonucleoprotein (RNP) plays a crucial role in maintaining telomere length by processively adding telomeric repeats to the 3' ends of chromosomes. Telomerase activation is linked to cancer, while mutations that compromise telomerase function result in diseases such as dyskeratosis congenita. The synthesis of telomeric repeats necessitates two core telomerase components: telomerase reverse transcriptase (TERT) and telomerase RNA (TER). However, cellular telomerase holoenzymes encompass a diverse range of protein factors, both constitutively and transiently interacting. These factors are integral to telomerase assembly or regulation at telomeres. This review emphasizes recent advancements in structural studies of telomerase holoenzymes and their associated factors from  Tetrahymena thermophila ,  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe , and humans. These studies have significantly deepened our molecular understanding not only of the mechanism underlying telomeric repeat synthesis but also of the biological roles of telomerase-associated proteins.","doi":"10.1101/cshperspect.a041697","authors":"Sekne Z, Ludzia P, Balch S, Nguyen THD","authors_abbrev":"Sekne Z et al.","pubmed_publication_date":"15 Apr 2025","pubmed_entrez_date":"2025-04-15","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-04-16 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF06395","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16E8.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:39228923","title":"Finding new roles of classic biomolecular condensates in the nucleus: Lessons from fission yeast.","citation":"Cell Insight 2024 Oct;3(5):100194","abstract":"Decades have passed since the initial discovery of membrane-less nuclear compartments, commonly called nuclear bodies or nuclear condensates. These compartments have drawn attention to their unique characteristics and functions, especially after introducing \"liquid-liquid phase separation\" to this research field. While the majority of the studies on nuclear condensates have been conducted in multicellular organisms, recent genetic, biochemical, and cell biological analyses using the fission yeast  Schizosaccharomyces pombe  have yielded valuable insights into biomolecular condensates. This review article focuses on two 'classic' nuclear condensates and discusses how research using fission yeast has unveiled previously unknown functions of these known nuclear bodies.","doi":"10.1016/j.cellin.2024.100194","authors":"Sugiyama T","authors_abbrev":"Sugiyama T","pubmed_publication_date":"Oct 2024","pubmed_entrez_date":"2024-09-04","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-09-04 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38938413","title":"Characterization of temperature-sensitive  Schizosaccharomyces pombe  mutants in the septation initiation network Spg1 GTPase.","citation":"MicroPubl Biol 2024;2024","abstract":"The  Schizosaccharomyces pombe  GTPase, Spg1 , activates the septation initiation network (SIN) protein kinase cascade to trigger septation. In the absence of functional Spg1 , cells fail cytokinesis and become multinucleate. In this study, we characterize a set of temperature-sensitive  spg1  alleles isolated in the 1990s. We identify the mutations within each new and previously characterized allele, characterize the extent of relative growth defects, and assess their interaction with other SIN alleles.","doi":"10.17912/micropub.biology.001193","authors":"Fletcher AB, Turner LA, Ren L, Willet AH, Gould KL","authors_abbrev":"Fletcher AB et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-06-28","publication_year":"2024","canto_session_key":"8c28cad70ebc804d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2024-07-12 09:23:40","canto_approved_date":"2026-01-31 13:55:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-10 18:01:46","canto_added_date":"2024-06-28 23:25:05","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":12,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPAC1565.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-07-12"},{"uniquename":"PMID:15979093","title":"Structure of the mediator subunit cyclin C and its implications for CDK8 function.","citation":"J Mol Biol 2005 Jul 29;350(5):833-42","abstract":"Cyclin C binds the cyclin-dependent kinases CDK8 and CDK3, which regulate mRNA transcription and the cell cycle, respectively. The crystal structure of cyclin C reveals two canonical five-helix repeats and a specific N-terminal helix. In contrast to other cyclins, the N-terminal helix is short, mobile, and in an exposed position that allows for interactions with proteins other than the CDKs. A model of the CDK8/cyclin C pair reveals two regions in the interface with apparently distinct roles. A conserved region explains promiscuous binding of cyclin C to CDK8 and CDK3, and a non-conserved region may be responsible for discrimination of CDK8 against other CDKs involved in transcription. A conserved and cyclin C-specific surface groove may recruit substrates near the CDK8 active site. Activation of CDKs generally involves phosphorylation of a loop at a threonine residue. In CDK8, this loop is longer and the threonine is absent, suggesting an alternative mechanism of activation that we discuss based on a CDK8-cyclin C model.","authors":"Hoeppner S, Baumli S, Cramer P","authors_abbrev":"Hoeppner S et al.","pubmed_publication_date":"29 Jul 2005","pubmed_entrez_date":"2005-06-28","publication_year":"2005","canto_session_key":"94b2e3d784023fe8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-02-19 17:58:30","canto_approved_date":"2023-02-19 17:58:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-19 17:58:23","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12D12.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-19","pdb_entries":[{"pdb_id":"1zp2","gene_chains":[{"gene_uniquename":"SPBC12D12.06","chain":"A","position":"5-228"}],"title":"Structure of the Mediator subunit cyclin C","entry_authors":"Hoeppner S,Baumli S,Cramer P","entry_authors_abbrev":"Hoeppner S et al.","reference_uniquename":"PMID:15979093","experimental_method":"X-ray","resolution":"3.0"}]},{"uniquename":"Pfam:CL0159","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP35G2.11c","YOL082W"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19590885","title":"At the right place at the right time: novel CENP-A binding proteins shed light on centromere assembly.","citation":"Chromosoma 2009 Oct;118(5):567-74","abstract":"Centromeres, the chromosomal loci that form the sites of attachment for spindle microtubules during mitosis, are identified by a unique chromatin structure generated by nucleosomes containing the histone H3 variant CENP-A. The apparent epigenetic mode of centromere inheritance across mitotic and meiotic divisions has generated much interest in how CENP-A assembly occurs and how structurally divergent centromeric nucleosomes can specify the centromere complex. Although a substantial number of proteins have been implicated in centromere assembly, factors that can bind CENP-A specifically and deliver nascent protein to the centromere were, thus far, lacking. Several recent reports on experiments in fission yeast and human cells have now shown significant progress on this problem. Here, we discuss these new developments and their implications for epigenetic centromere inheritance.","doi":"10.1007/s00412-009-0227-3","authors":"Silva MC, Jansen LE","authors_abbrev":"Silva MC et al.","pubmed_publication_date":"Oct 2009","pubmed_entrez_date":"2009-07-11","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31822915","title":"Mkt1 is required for RNAi-mediated silencing and establishment of heterochromatin in fission yeast.","citation":"Nucleic Acids Res 2020 Feb 20;48(3):1239-1253","abstract":"Constitutive domains of repressive heterochromatin are maintained within the fission yeast genome through self-reinforcing mechanisms involving histone methylation and small RNAs. Non-coding RNAs generated from heterochromatic regions are processed into small RNAs by the RNA interference pathway, and are subject to silencing through both transcriptional and post-transcriptional mechanisms. While the pathways involved in maintenance of the repressive heterochromatin state are reasonably well understood, less is known about the requirements for its establishment. Here, we describe a novel role for the post-transcriptional regulatory factor Mkt1 in establishment of heterochromatin at pericentromeres in fission yeast. Loss of Mkt1 does not affect maintenance of existing heterochromatin, but does affect its recovery following depletion, as well as de novo establishment of heterochromatin on a mini-chromosome. Pathway dissection revealed that Mkt1 is required for RNAi-mediated post-transcriptional silencing, downstream of small RNA production. Mkt1 physically associates with pericentromeric transcripts, and is additionally required for maintenance of silencing and heterochromatin at centromeres when transcriptional silencing is impaired. Our findings provide new insight into the mechanism of RNAi-mediated post-transcriptional silencing in fission yeast, and unveil an important role for post-transcriptional silencing in establishment of heterochromatin that is dispensable when full transcriptional silencing is imposed.","doi":"10.1093/nar/gkz1157","authors":"Taglini F, Chapman E, van Nues R, Theron E, Bayne EH","authors_abbrev":"Taglini F et al.","pubmed_publication_date":"20 Feb 2020","pubmed_entrez_date":"2019-12-12","publication_year":"2020","canto_session_key":"d9182b3ccf6650bd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elizabeth bayne","canto_first_approved_date":"2020-01-08 15:16:23","canto_approved_date":"2022-01-15 10:43:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-01-03 13:33:42","canto_added_date":"2019-12-21 14:45:44","annotation_curators":[{"name":"Elizabeth bayne","community_curator":true,"annotation_count":19,"orcid":"0000-0001-8775-999X","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1442.04c","SPAC16E8.15","SPAC20G8.05c","SPBC902.04","SPAC139.01c","SPBC16H5.12c","SPBC776.08c","SPBC776.09","SPAC1006.03c","SPBC776.17","SPBC1706.01","SPAC1F3.01","SPBC428.08c","SPBC16D10.07c","SPCC188.13c","SPBC17F3.01c","SPBC21B10.03c","SPAC18G6.07c","SPCC1223.06"],"gene_count":19,"ltp_gene_count":15,"approved_date":"2020-01-08"},{"uniquename":"EMBL:SPC08792","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:BAA09171","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8154184","title":"Role of O-acetylhomoserine sulfhydrylase in sulfur amino acid synthesis in various yeasts.","citation":"Yeast 1993 Dec;9(12):1335-42","abstract":"Mutants defective in O-acetylhomoserine sulfhydrylase (OAH-SHLase) were obtained in five yeast strains representative of different yeast genera: Saccharomyces cerevisiae, Kluyveromyces lactis, Yarrowia lipolytica, Schizosaccharomyces pombe and Trichosporon cutaneum. In vitro, in all five strains, the enzyme also had O-acetylserine (OAS) sulfhydrylase activity so it is a 'bifunctional' OAH/OAS-SHLase (Yamagata, 1989). The enzyme was only found to be essential in S. cerevisiae (OAH SHLase-negative mutants are auxotrophs). Its impairment in K. lactis caused a slower growth rate and a decrease of the sulfur amino acid pool. In T. cutaneum only the pool was affected whereas in Y. lipolytica and S. pombe the lesion caused no change in the growth rate nor in the pool. In all strains where OAH SHLase-negative mutants were prototrophs, a monofunctional OAS sulhydrylase was detected. The results indicate that OAH SHLase may play different physiological roles in various yeasts.","authors":"Brzywczy J, Paszewski A","authors_abbrev":"Brzywczy J et al.","pubmed_publication_date":"Dec 1993","pubmed_entrez_date":"1993-12-01","publication_year":"1993","canto_session_key":"8667777f46de570e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-06-08 07:41:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-03 09:58:52","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-06-03"},{"uniquename":"PMID:10589835","title":"Budding yeast Cdc6p induces re-replication in fission yeast by inhibition of SCF(Pop)-mediated proteolysis.","citation":"Mol Gen Genet 1999 Oct;262(3):473-80","abstract":"In fission yeast, overexpression of the replication initiator protein Cdc18p induces re-replication, a phenotype characterized by continuous DNA synthesis in the absence of cell division. In contrast, overexpression of Cdc6p, the budding yeast homolog of Cdc18p, does not cause re-replication in S. cerevisiae. However, we have found that Cdc6p has the ability to induce rereplication in fission yeast. Cdc6p cannot functionally replace Cdc18p, but instead interferes with the proteolysis of both Cdc18p and Rum1p, the inhibitor of the protein kinase Cdc2p. This activity of Cdc6p is entirely contained within a short N-terminal peptide, which forms a tight complex with Cdc2p and the F-box/WD-repeat protein Sud1p/Pop2p, a component of the SCF(Pop) ubiquitin ligase in fission yeast. These interactions are mediated by two distinct regions within the N-terminal region of Cdc6p and depend on the integrity of its Cdc2p phosphorylation sites. The data suggest that disruption of re-replication control by overexpression of Cdc6p in fission yeast is a consequence of sequestration of Cdc2p and Pop2p, two factors involved in the negative regulation of Rum1p, Cdc18p and potentially other replication proteins.","authors":"Wolf DA, McKeon F, Jackson PK","authors_abbrev":"Wolf DA et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-12-10","publication_year":"1999","canto_session_key":"4e8faa616d23a184","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-07 13:19:28","canto_approved_date":"2026-01-30 14:07:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-07 13:18:40","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-06-07"},{"uniquename":"PMID:34561737","title":"DNA interaction, anticancer, cytotoxicity and genotoxicity studies with potential pyrazine-bipyrazole dinuclear µ-oxo bridged Au(III) complexes.","citation":"Mol Divers 2022 Aug;26(4):2085-2101","abstract":"Pyrazine-bipyrazole-based µ-oxo bridged dinuclear Au(III) complexes were synthesized and characterized by various spectrometric ( 1 H-NMR,  13 C (APT) NMR, FT-IR, Mass spectrometry) and analytical techniques (elemental analysis and conductance measurement). The evaluation of DNA binding activity by UV-Vis absorption spectra and viscosity measurement demonstrated that all the compounds intercalate in between the stacks of DNA base pair and the binding constant values were observed in the range of 5.4 × 10 4 -2.17 × 10 5  M -1 . The molecular docking study also supports the intercalation mode of binding. The anti-proliferation activity of complexes on A549 (Lung adenocarcinoma) cells by MTT assay demonstrated IC 50  values in the range of 47.46 -298.12 μg/mL. The genotoxicity of compounds was checked by smearing observed in the DNA of S. pombe cell under the influence of complexes. The in vivo cytotoxicity of compounds against brine shrimp demonstrated the LC 50  values in the range of 4.59-27.22 μg/mL. The promising results of the Au(III) complexes received significant attention and make them suitable for the new metallodrugs after the detailed mechanistic biological study.","doi":"10.1007/s11030-021-10317-0","authors":"Kanthecha DN, Bhatt BS, Patel MN, Vaidya FU, Pathak C","authors_abbrev":"Kanthecha DN et al.","pubmed_publication_date":"Aug 2022","pubmed_entrez_date":"2021-09-25","publication_year":"2022","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2021-09-27 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25103238","title":"Tts1, the fission yeast homologue of the TMEM33 family, functions in NE remodeling during mitosis.","citation":"Mol Biol Cell 2014 Oct 01;25(19):2970-83","abstract":"The fission yeast Schizosaccharomyces pombe undergoes \"closed\" mitosis in which the nuclear envelope (NE) stays intact throughout chromosome segregation. Here we show that Tts1, the fission yeast TMEM33 protein that was previously implicated in organizing the peripheral endoplasmic reticulum (ER), also functions in remodeling the NE during mitosis. Tts1 promotes insertion of spindle pole bodies (SPBs) in the NE at the onset of mitosis and modulates distribution of the nuclear pore complexes (NPCs) during mitotic NE expansion. Structural features that drive partitioning of Tts1 to the high-curvature ER domains are crucial for both aspects of its function. An amphipathic helix located at the C-terminus of Tts1 is important for ER shaping and modulating the mitotic NPC distribution. Of interest, the evolutionarily conserved residues at the luminal interface of the third transmembrane region function specifically in promoting SPB-NE insertion. Our data illuminate cellular requirements for remodeling the NE during \"closed\" nuclear division and provide insight into the structure and functions of the eukaryotic TMEM33 family.","doi":"10.1091/mbc.E13-12-0729","authors":"Zhang D, Oliferenko S","authors_abbrev":"Zhang D et al.","pubmed_publication_date":"01 Oct 2014","pubmed_entrez_date":"2014-08-09","publication_year":"2014","canto_session_key":"7f17aec8a060844d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Snezhana Oliferenko","canto_first_approved_date":"2015-06-11 10:15:13","canto_approved_date":"2025-09-04 11:18:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-02 12:36:22","canto_added_date":"2014-08-13 00:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":48,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Snezhana Oliferenko","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.15","SPBC428.20c","SPBC31A8.01c","SPCC830.08c","SPAC1786.03","SPBC1539.04"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2015-06-11"},{"uniquename":"EMBL:AU006649","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1497669","title":"Protein transport in the permeabilized cell of Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 1992 Jul 31;186(2):838-45","abstract":"We reconstituted a protein translocation-transport system composed of permeabilized spheroplasts (P-cells) of the fission yeast Schizosaccharomyces pombe and the precursor of alpha sex pheromone, prepro-alpha-factor of the budding yeast Saccharomyces cerevisiae. We found that P-cells prepared from the spheroplasts formed in 0.7M KCl as an osmotic stabilizer had the activity to transport pro-alpha-factor to the Golgi apparatus. Electron microscopic observations showed that membranes were preserved more intact in the P-cells prepared from the spheroplasts formed in 0.7M KCl than in 0.7M sorbitol. A glycoprotein of S. pombe contains galactose residues, and we detected incorporation of radiolabeled galactose residues into the anti-prepro-alpha-factor immunoprecipitable fractions in this S. pombe system, but not in the S. cerevisiae system. This paper reports that a heterologous system of in vitro protein transport was performed, and prepro-alpha-factor has the signals necessary for early steps of the transport in S. pombe.","authors":"Kambe-Honjoh H, Yoda K, Yamasaki M","authors_abbrev":"Kambe-Honjoh H et al.","pubmed_publication_date":"31 Jul 1992","pubmed_entrez_date":"1992-07-31","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24768994","title":"The Schizosaccharomyces pombe Hikeshi/Opi10 protein has similar biochemical functions to its human homolog but acts in different physiological contexts.","citation":"FEBS Lett 2014 May 21;588(10):1899-905","abstract":"Human Hikeshi (HsHikeshi) is a nuclear import carrier for Hsp70s and is required for cell survival after heat shock. The Hikeshi homolog in Schizosaccharomyces pombe (SpHikeshi/Opi10) localizes to the nuclear rim, interacts with the Hsp70 homolog Ssa2, and mediates its nuclear import in a reconstituted mammalian nuclear transport system. However, SpHikeshi/Opi10 is not required for heat stress response and survival after heat stress. Instead, SpHikeshi/Opi10 is required for the normal expression of stress response genes under optimal conditions and for cell growth during glucose deprivation. Here, the functions of SpHikeshi/Opi10 are discussed and compared to the functions of HsHikeshi.","doi":"10.1016/j.febslet.2014.04.018","authors":"Oda Y, Kimura M, Kose S, Fasken MB, Corbett AH, Imamoto N","authors_abbrev":"Oda Y et al.","pubmed_publication_date":"21 May 2014","pubmed_entrez_date":"2014-04-29","publication_year":"2014","canto_session_key":"6631b1666d57256f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Naoko Imamoto","canto_approved_date":"2017-06-25 09:31:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-23 09:47:11","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Naoko Imamoto","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.13","SPBC21H7.06c","SPAC2E12.02","SPAC13G7.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-01-23"},{"uniquename":"PMID:25590601","title":"Fission yeast Ryh1 GTPase activates TOR Complex 2 in response to glucose.","citation":"Cell Cycle 2015;14(6):848-56","abstract":"The Target Of Rapamycin (TOR) is an evolutionarily conserved protein kinase that forms 2 distinct protein complexes referred to as TOR complex 1 (TORC1) and 2 (TORC2). Recent extensive studies have demonstrated that TORC1 is under the control of the small GTPases Rheb and Rag that funnel multiple input signals including those derived from nutritional sources; however, information is scarce as to the regulation of TORC2. A previous study using the model system provided by the fission yeast Schizosaccharomyces pombe identified Ryh1, a Rab-family GTPase, as an activator of TORC2. Here, we show that the nucleotide-binding state of Ryh1 is regulated in response to glucose, mediating this major nutrient signal to TORC2. In glucose-rich growth media, the GTP-bound form of Ryh1 induces TORC2-dependent phosphorylation of Gad8, a downstream target of TORC2 in fission yeast. Upon glucose deprivation, Ryh1 becomes inactive, which turns off the TORC2-Gad8 pathway. During glucose starvation, however, Gad8 phosphorylation by TORC2 gradually recovers independently of Ryh1, implying an additional TORC2 activator that is regulated negatively by glucose. The paired positive and negative regulatory mechanisms may allow fine-tuning of the TORC2-Gad8 pathway, which is essential for growth under glucose-limited environment.","doi":"10.1080/15384101.2014.1000215","authors":"Hatano T, Morigasaki S, Tatebe H, Ikeda K, Shiozaki K","authors_abbrev":"Hatano T et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-01-16","publication_year":"2015","canto_session_key":"2f1c2ad9160b5b20","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaz Shiozaki","canto_first_approved_date":"2018-08-16 16:42:43","canto_approved_date":"2026-03-29 08:44:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-27 07:21:16","canto_added_date":"2015-01-17 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kaz Shiozaki","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.08","SPBC16G5.15c","SPCC24B10.07","SPCC1753.02c","SPBC30D10.10c","SPBC12C2.02c","SPAC4C5.02c","SPBC19C7.03","SPBC21B10.05c","SPCC777.08c","SPCC285.09c","SPBC106.10","SPAPYUG7.02c","SPAC23H3.13c"],"gene_count":14,"ltp_gene_count":12,"approved_date":"2018-08-16"},{"uniquename":"PMID:22525225","title":"Hippo signalling in the G2/M cell cycle phase: lessons learned from the yeast MEN and SIN pathways.","citation":"Semin Cell Dev Biol 2012 Sep;23(7):794-802","abstract":"Over the past decade Hippo kinase signalling has been established as an essential tumour suppressor pathway controlling tissue growth in flies and mammals. All members of the Hippo core signalling cassette are conserved from yeast to humans, whereby the yeast analogues of Hippo, Mats and Lats are central components of the mitotic exit network and septation initiation network in budding and fission yeast, respectively. Here, we discuss how far core Hippo signalling components in Drosophila melanogaster and mammals have reported similar mitotic functions as already established for their highly conserved yeast counterparts.","doi":"10.1016/j.semcdb.2012.04.001","authors":"Hergovich A, Hemmings BA","authors_abbrev":"Hergovich A et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-04-25","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28282023","title":"Competition between Tropomyosin, Fimbrin, and ADF/Cofilin drives their sorting to distinct actin filament networks.","citation":"Elife 2017 Mar 10;6","abstract":"The fission yeast actin cytoskeleton is an ideal, simplified system to investigate fundamental mechanisms behind cellular self-organization. By focusing on the stabilizing protein tropomyosin Cdc8, bundling protein fimbrin Fim1, and severing protein coffin Adf1, we examined how their pairwise and collective interactions with actin filaments regulate their activity and segregation to functionally diverse F-actin networks. Utilizing multi-color TIRF microscopy of in vitro reconstituted F-actin networks, we observed and characterized two distinct Cdc8 cables loading and spreading cooperatively on individual actin filaments. Furthermore, Cdc8, Fim1, and Adf1 all compete for association with F-actin by different mechanisms, and their cooperative association with actin filaments affects their ability to compete. Finally, competition between Fim1 and Adf1 for F-actin synergizes their activities, promoting rapid displacement of Cdc8 from a dense F-actin network. Our findings reveal that competitive and cooperative interactions between actin binding proteins help define their associations with different F-actin networks.","doi":"10.7554/eLife.23152","authors":"Christensen JR, Hocky GM, Homa KE, Morganthaler AN, Hitchcock-DeGregori SE, Voth GA, Kovar DR","authors_abbrev":"Christensen JR et al.","pubmed_publication_date":"10 Mar 2017","pubmed_entrez_date":"2017-03-11","publication_year":"2017","canto_session_key":"5af60caf995a2cc1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-12 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPBC1778.06c","SPAC20G4.06c","SPBC32H8.12c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:12939254","title":"The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomyces pombe.","citation":"J Cell Biol 2003 Sep 01;162(5):851-62","abstract":"Cytokinetic actin ring (CAR) formation in Schizosaccharomyces pombe requires two independent actin nucleation pathways, one dependent on the Arp2/3 complex and another involving the formin Cdc12p. Here we investigate the role of the S. pombe Cdc15 homology family protein, Cdc15p, in CAR assembly and find that it interacts with proteins from both of these nucleation pathways. Cdc15p binds directly to the Arp2/3 complex activator Myo1p, which likely explains why actin patches and the Arp2/3 complex fail to be medially recruited during mitosis in cdc15 mutants. Cdc15p also binds directly to Cdc12p. Cdc15p and Cdc12p not only display mutual dependence for CAR localization, but also exist together in a ring-nucleating structure before CAR formation. The disruption of these interactions in cdc15 null cells is likely to be the reason for their complete lack of CARs. We propose a model in which Cdc15p plays a critical role in recruiting and coordinating the pathways essential for the assembly of medially located F-actin filaments and construction of the CAR.","authors":"Carnahan RH, Gould KL","authors_abbrev":"Carnahan RH et al.","pubmed_publication_date":"01 Sep 2003","pubmed_entrez_date":"2003-08-27","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.15c","SPBC13E7.09","SPAC1F5.04c","SPAC20G8.05c","SPBC146.13c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:35129352","title":"Unphosphorylated Form of the PAQosome Core Subunit RPAP3 Binds Ribosomal Preassembly Complexes to Modulate Ribosome Biogenesis.","citation":"J Proteome Res 2022 Apr 01;21(4):1073-1082","abstract":"The PAQosome (particle for arrangement of quaternary structure) is a 12-subunit HSP90 co-chaperone involved in the biogenesis of several human protein complexes. Two mechanisms of client selection have previously been identified, namely, the selective recruitment of specific adaptors and the differential use of homologous core subunits. Here, we describe a third client selection mechanism by showing that RPAP3, one of the core PAQosome subunits, is phosphorylated at several Ser residues in HEK293 cells. Affinity purification coupled with mass spectrometry (AP-MS) using the expression of tagged RPAP3 with single phospho-null mutations at Ser116, Ser119, or Ser121 reveals binding of the unphosphorylated form to several proteins involved in ribosome biogenesis.  In vitro  phosphorylation assays indicate that the kinase CK2 phosphorylates these RPAP3 residues. This finding is supported by data showing that pharmacological inhibition of CK2 enhances the binding of RPAP3 to ribosome preassembly factors in AP-MS experiments. Moreover, the silencing of PAQosome subunits interferes with ribosomal assembly factors' interactome. Altogether, these results indicate that RPAP3 phosphate group addition/removal at specific residues modulates binding to subunits of preribosomal complexes and allows speculating that PAQosome posttranslational modification is a mechanism of client selection.","doi":"10.1021/acs.jproteome.1c00938","authors":"Pinard M, Cloutier P, Poitras C, Gauthier MS, Coulombe B","authors_abbrev":"Pinard M et al.","pubmed_publication_date":"01 Apr 2022","pubmed_entrez_date":"2022-02-07","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34005412","canto_session_key":"7233e293012402f5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-20 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12758069","title":"Reverse transcriptase and reverse splicing activities encoded by the mobile group II intron cobI1 of fission yeast mitochondrial DNA.","citation":"J Mol Biol 2003 May 30;329(2):191-206","abstract":"Mobile group II introns encode multidomain proteins with maturase activity involved in splicing and reverse transcriptase (RT) and (often) endonuclease activities involved in intron mobility. These activities are present in a ribonucleoprotein complex that contains the excised intron RNA and the intron-encoded protein. Here, we report biochemical studies of the protein encoded by the group IIA1 intron in the cob gene of fission yeast Schizosaccharomyces pombe mitochondria (cobI1). RNP particle fractions from the wild-type fission yeast strain with cobI1 in its mtDNA have RT activity even without adding an exogenous primer. Characterization of the cDNA products of such reactions showed a strong preference for excised intron RNA as template. Two main regions for initiation of cDNA synthesis were mapped within the intron, one near the DIVa putative high-affinity binding site for the intron-encoded protein and the other near domain VI. Adding exogenous primers complementary to cob exon 2 sequences near the intron/exon boundary stimulated RT activity but mainly for pre-mRNA rather than mRNA templates. Further in vitro experiments demonstrated that cobI1 RNA in RNP particle fractions can reverse splice into double-stranded DNA substrates containing the intron homing site. Target DNA primed reverse transcription was not detected unless a DNA target was used that was already nicked in the antisense strand of exon 2. This study shows that S.pombe cobI1 encodes RNP particles that have most of the biochemical activities needed for it to be a retroelement. Interestingly, it appears to lack an endonuclease activity, suggesting that the active homing exhibited by this intron in crosses may differ somewhat from that of the better-characterized introns.","authors":"Schäfer B, Gan L, Perlman PS","authors_abbrev":"Schäfer B et al.","pubmed_publication_date":"30 May 2003","pubmed_entrez_date":"2003-05-22","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24530531","title":"Mcp1p tracks microtubule plus ends to destabilize microtubules at cell tips.","citation":"FEBS Lett 2014 Mar 18;588(6):859-65","abstract":"Microtubule plus ends are dynamically regulated by a wide variety of proteins for performing diverse cellular functions. Here, we show that the fission yeast Schizosaccharomyces pombe uncharacterized protein mcp1p is a microtubule plus-end tracking protein which depends on the kinesin-8 klp6p for transporting along microtubules towards microtubule plus ends. In the absence of mcp1p, microtubule catastrophe and rescue frequencies decrease, leading to an increased dwell time of microtubule plus ends at cell tips. Thus, these findings suggest that mcp1p may synergize with klp6p at microtubule plus-ends to destabilize microtubules.","doi":"10.1016/j.febslet.2014.01.055","authors":"Zheng F, Li T, Cheung M, Syrovatkina V, Fu C","authors_abbrev":"Zheng F et al.","pubmed_publication_date":"18 Mar 2014","pubmed_entrez_date":"2014-02-18","publication_year":"2014","canto_session_key":"be313e7e41a1bde1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-03 14:20:07","canto_approved_date":"2020-06-05 14:07:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-12 09:12:46","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPBC1685.15c","SPAC18G6.15","SPAC1687.10"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2017-02-03"},{"uniquename":"PMID:17920745","title":"Genotoxicity study with special reference to DNA damage by comet assay in fission yeast, Schizosaccharomyces pombe exposed to drinking water.","citation":"Food Chem Toxicol 2008 Jan;46(1):402-7","abstract":"The objective of this study was to investigate genotoxicity, especially DNA damage, in drinking water samples collected from tap by using fission yeast Schizosaccharomyces pombe as a model organism. Generally raw water potabolization is done by treatment with polymeric coagulant, alum, chlorine, etc. In the comet test, highly significant (P<0.001) effects of DNA damage were detected in treated water (tap water) when compared to negative control (raw water) as well as laboratory control (distilled water) samples for both 1 h and 2 h exposure. In the water treatment plant, raw water treatment is done by the process of prechlorination, alum and polymeric coagulant (CatflocT) dosing, postchlorination, filtration and final discharge for consumption. In conclusion it can be stated from the results that chlorinated disinfectant, alum and polymeric coagulant (CatflocT) mixture used in drinking water has a potent cumulative genotoxic effect in the eukaryotic cells and may pose potential genotoxic risk for human health following long-term consumption.","authors":"Banerjee P, Talapatra SN, Mandal N, Sundaram G, Mukhopadhyay A, Chattopadhyay D, Banerjee SK","authors_abbrev":"Banerjee P et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-10-09","publication_year":"2008","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26842963","title":"ADAT3-related intellectual disability: Further delineation of the phenotype.","citation":"Am J Med Genet A 2016 May;170A(5):1142-7","abstract":"ADAT3-related intellectual disability has been recently described in 24 individuals from eight Saudi families who had cognitive impairment and strabismus. Other common features included growth failure, microcephaly, tone abnormalities, epilepsy, and nonspecific brain abnormalities. A single homozygous founder mutation (c.382G>A:p.(V128M)) in the ADAT3 gene, which encodes a protein that functions in tRNA editing, was identified in all affected individuals. In this report, we present additional 15 individuals from 11 families (10 Saudis and 1 Emirati) who are homozygous for the same founder mutation. In addition to the universal findings of intellectual disability and strabismus, the majority exhibited microcephaly and growth failure. Additional features not reported in the original cohort include dysmorphic facial features (prominent forehead, up-slanted palpebral fissures, epicanthus, and depressed nasal bridge), behavioral problems (hyperactivity and aggressiveness), recurrent otitis media, and growth hormone deficiency. ADAT3-related intellectual disability is an important recognizable cause of intellectual disability in Arabia.","doi":"10.1002/ajmg.a.37578","authors":"El-Hattab AW, Saleh MA, Hashem A, Al-Owain M, Asmari AA, Rabei H, Abdelraouf H, Hashem M, Alazami AM, Patel N, Shaheen R, Faqeih EA, Alkuraya FS","authors_abbrev":"El-Hattab AW et al.","pubmed_publication_date":"May 2016","pubmed_entrez_date":"2016-02-05","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP27G11.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"Pfam:PF15159","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC227.19c","HGNC:28213"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15743411","title":"Studies of Schizosaccharomyces pombe TFIIE indicate conformational and functional changes in RNA polymerase II at transcription initiation.","citation":"Genes Cells 2005 Mar;10(3):207-24","abstract":"The general transcription factor TFIIE plays essential roles in transcription by RNA polymerase II (PolII). Despite recent progress, the elucidation of its precise mechanisms including biological functions awaits further characterization. We report the isolation and characterization of Schizosaccharomyces pombe TFIIE (spTFIIE). Like human and other eukaryotic TFIIE proteins, spTFIIE consists of alpha and beta subunits and the genes encoding both subunits are essential for viability. Chromatin immunoprecipitation assays demonstrated that spTFIIE localizes to promoters in vivo. Mutational analysis of the C-terminal basic helix-loop region of TFIIEbeta, which is involved in the transition from transcription initiation to elongation, revealed that transcription-defective mutants affected in this region are also cold sensitive. The spTFIIEbeta subunit binds both spTFIIEbeta and spTFIIEalpha but spTFIIEalpha binds only spTFIIEbeta. These results indicate that TFIIE forms an alpha2beta2 heterotetramer in which two alphabeta heterodimers are connected via beta subunits. Further analysis of binding specificities showed that spTFIIEbeta binds the Rpb2 and Rpb12 subunits of PolII, whereas spTFIIEalpha predominantly binds Rpb5, which is located at the clamp region and changes conformation upon transcription initiation.","authors":"Hayashi K, Watanabe T, Tanaka A, Furumoto T, Sato-Tsuchiya C, Kimura M, Yokoi M, Ishihama A, Hanaoka F, Ohkuma Y","authors_abbrev":"Hayashi K et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-03-04","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1198.13c","SPAC3A12.07","SPBC14C8.12","SPAC458.07","SPBC337.14","SPACUNK4.06c","SPAPYUG7.04c","SPCC1442.10c","SPAC23G3.01","SPBC28F2.12","SPBC19C2.03","SPAC23C4.15","SPCC1020.04c","SPAC1B3.12c","SPCC1672.08c"],"gene_count":15,"ltp_gene_count":15},{"uniquename":"PMID:2686985","title":"A selection for mutants of the RNA polymerase III transcription apparatus: PCF1 stimulates transcription of tRNA and 5S RNA genes.","citation":"EMBO J 1989 Dec 20;8(13):4281-8","abstract":"A genetic approach has been developed to study transcription by RNA polymerase III. A pair of Schizosaccharomyces pombe nonsense suppressor tRNA genes were arranged in tandem such that expression of the downstream (supS1) tRNA suppressor was dependent upon transcription initiated by the internal promoter of the upstream (sup9-e) gene. Dominant mutant strains of Saccharomyces cerevisiae were isolated that suppress in trans the effect of an A block promoter mutation (A19) in the sup9-e gene and restore supS1 suppressor activity. Fifteen mutant strains, eight of which were independently isolated, all have elevated steady-state levels of sup9-e A19 RNA consistent with an increase in gene transcription. Extracts of a strain carrying the dominant mutant gene, PCF1, show a general 6-fold stimulation in transcription of mutant (A19) and wild-type tRNA genes and increase 5S gene transcription 4-fold compared with extracts from a wild-type strain. A transcription factor exclusion assay was used to show that the PCF1 mutation affects two distinct stages in transcription: one prior to and one after stable complex formation; and that these effects are mediated by a component of the stable complex. Further evidence of an effect during complex assembly was obtained in a time-course experiment that showed a shortened lag phase in the PCF1 extract. The results indicate that PCF1 is either a component of the stable complex or a positive regulator of its activity.","authors":"Willis I, Schmidt P, Söll D","authors_abbrev":"Willis I et al.","pubmed_publication_date":"20 Dec 1989","pubmed_entrez_date":"1989-12-20","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15196464","title":"Those interfering little RNAs! Silencing and eliminating chromatin.","citation":"Curr Opin Genet Dev 2004 Apr;14(2):174-80","abstract":"RNA interference (RNAi) is widely used for knocking down expression of genes of interest and in systematic screens for desired phenotypes. In post-transcriptional gene silencing, double-stranded RNA triggers are processed to small interfering RNAs, which act to seek out and destroy homologous transcripts. A variety of organisms utilise the RNAi pathway to silence expression of potentially harmful endogenous mobile elements and to eliminate unnecessary sequences. In plants and fission yeast, RNAi can also mediate chromatin-based silencing resulting in transcriptional shutdown of homologous transcription units (transcriptional gene silencing) and the formation of centromeric heterochromatin. In metazoans, the expression of non-coding RNAs is often associated with the formation of silent chromatin domains but it remains to be determined if RNAi is involved.","authors":"Schramke V, Allshire R","authors_abbrev":"Schramke V et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-06-16","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18410345","title":"Characterization of Sro1, a novel stress responsive protein in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2008 Jun;8(4):564-73","abstract":"The large amount of available genome sequencing data presents a huge challenge in the form of orphan sequences. This study reports the detailed functional characterization of one such orphan sequence in Schizosaccharomyces pombe. We identified this gene as a prominently upregulated 1.4 kb transcript in a screen for Cigarette smoke extract responsive genes in S. pombe and named it Stress Responsive Orphan 1 (Sro1). We report various functions of Sro1 in regulation of cellular behaviour under stress conditions. We show that this gene (Sro1) responds to a variety of stress conditions and that the expression of the gene is regulated mainly through the stress activated protein kinase (SAPK) Sty1 and its downstream transcription factor Atf1. Deletion of Sro1 also significantly alters the reactive oxygen species (ROS) generation profiles and the cell-cycle progression of S. pombe during stress conditions. The stress-specific alteration of the ROS generation profiles and checkpoint activation resulting from deletion of the gene suggest that Sro1 might be a key player in determining cellular responses/fate under stress conditions.","doi":"10.1111/j.1567-1364.2008.00373.x","authors":"Sundaram G, Palchaudhuri S, Chaudhuri S, Karunanithi S, Chattopadhyay D","authors_abbrev":"Sundaram G et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-16","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1347.11","SPBC106.10","SPBC29B5.01"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:15357289","title":"Schizosaccharomyces pombe rsm1 genetically interacts with spmex67, which is involved in mRNA export.","citation":"J Microbiol 2004 Mar;42(1):32-6","abstract":"We have previously isolated three synthetic lethal mutants from Schizosaccharomyces pombe in order to identify mutations in the genes that are functionally linked to spmex67 with respect to mRNA export. A novel rsm1 gene was isolated by complementation of the growth defect in one of the synthetic lethal mutants, SLMexl. The rsm1 gene contains no introns and encodes a 296 amino-acid-long protein with the RING finger domain, a C3HC4 in the N-terminal half. The deltarsm1 null mutant is viable, but it showed a slight poly(A)+ RNA accumulation in the nucleus. Also, the combination of deltarsm1 and deltaspmex67 mutations confers synthetic lethality that is accompanied by the severe poly(A)+ RNA export defect. These results suggest that rsm1 is involved in mRNA export from the nucleus.","authors":"Yoon JH","authors_abbrev":"Yoon JH","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-09-11","publication_year":"2004","canto_session_key":"20d4bca6fcf12ef5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-02 17:27:44","canto_approved_date":"2024-04-12 17:09:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-01 20:24:09","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1921.03c","SPCC1753.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-06-02"},{"uniquename":"PMID:40085649","title":"Protocol for chromatin immunoprecipitation of chromatin-binding proteins in Schizosaccharomyces pombe using a dual-crosslinking approach.","citation":"STAR Protoc 2025 Mar 13;6(1):103695","abstract":"Single-crosslink chromatin immunoprecipitation (ChIP) is often ineffective at mapping the binding sites of chromatin-binding proteins that indirectly interact with DNA. Here, we present a protocol to map the genomic occupancy of different chromatin regulators and an RNA exosome adapter subunit in Schizosaccharomyces pombe using dual-crosslinking ChIP. We describe steps for cell growth, dual-crosslinking, cell lysis, sonification, and immunoprecipitation. We then detail procedures for washing, crosslink reversal, and DNA purification for downstream analysis using ChIP-qPCR and ChIP sequencing. For complete details on the use and execution of this protocol, please refer to Khanduja et al. 1 .","doi":"10.1016/j.xpro.2025.103695","authors":"Khanduja JS, Motamedi M","authors_abbrev":"Khanduja JS et al.","pubmed_publication_date":"13 Mar 2025","pubmed_entrez_date":"2025-03-14","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-03-15 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12455694","title":"mcl1+, the Schizosaccharomyces pombe homologue of CTF4, is important for chromosome replication, cohesion, and segregation.","citation":"Eukaryot Cell 2002 Oct;1(5):758-73","abstract":"The fission yeast minichromosome loss mutant mcl1-1 was identified in a screen for mutants defective in chromosome segregation. Missegregation of the chromosomes in mcl1-1 mutant cells results from decreased centromeric cohesion between sister chromatids. mcl1+ encodes a beta-transducin-like protein with similarity to a family of eukaryotic proteins that includes Ctf4p from Saccharomyces cerevisiae, sepB from Aspergillus nidulans, and AND-1 from humans. The previously identified fungal members of this protein family also have chromosome segregation defects, but they primarily affect DNA metabolism. Chromosomes from mcl1-1 cells were heterogeneous in size or structure on pulsed-field electrophoresis gels and had elongated heterogeneous telomeres. mcl1-1 was lethal in combination with the DNA checkpoint mutations rad3delta and rad26delta, demonstrating that loss of Mcl1p function leads to DNA damage. mcl1-1 showed an acute sensitivity to DNA damage that affects S-phase progression. It interacts genetically with replication components and causes an S-phase delay when overexpressed. We propose that Mcl1p, like Ctf4p, has a role in regulating DNA replication complexes.","authors":"Williams DR, McIntosh JR","authors_abbrev":"Williams DR et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-11-29","publication_year":"2002","canto_session_key":"298401f5017b6d28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-22 15:49:23","canto_approved_date":"2026-02-01 19:09:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-06 14:43:08","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC1F7.05","SPAC8F11.07c","SPCC1322.12c","SPCC18B5.03","SPAC2G11.12","SPAC3H5.06c","SPBC660.14","SPCC1259.13","SPAC24H6.05","SPBC216.05","SPAC9E9.08","SPBC1734.06","SPAC664.07c","SPAC1952.07","SPAPB1E7.02c","SPCC338.17c","SPBC16D10.04c","SPBC776.12c"],"gene_count":19,"ltp_gene_count":19,"approved_date":"2015-12-22"},{"uniquename":"PMID:21672643","title":"The oxidized thiol proteome in fission yeast--optimization of an ICAT-based method to identify H2O2-oxidized proteins.","citation":"J Proteomics 2011 Oct 19;74(11):2476-86","abstract":"Major intracellular disulfide formation is prevented in the cytosol by potent reducing systems. However, protein thiols can be oxidized as a consequence of redox-mediated physiological reactions or due to the unwanted toxicity of reactive oxygen species. In addition, the reactivity of cysteine residues towards peroxides is used by H(2)O(2) sensors in signal transduction pathways in a gain-of-function process to induce transcriptional antioxidant responses. Thus, the Schizosaccharomyces pombe peroxiredoxin Tpx1 and the transcription factor Pap1 are sensors of H(2)O(2) meant to promote cell survival. In an attempt to compare signaling events versus global thiol oxidation, we have optimized thiol-labeling approaches to characterize the disulfide proteome of fission yeast in response to added H(2)O(2). We propose a method based on (i) freezing the redox state of thiols with strong acids prior to cell lysis; (ii) blocking thiol groups with iodoacetamide, and reversibly oxidized thiols with heavy and light isotope-coded affinity tags (ICAT) reagents; and (iii) quantifying individual relative protein concentrations with stable-isotope dimethyl labeling. We have applied this highly sensitive strategy to provide a map of H(2)O(2)-dependent oxidized thiols in fission yeast, and found Tpx1 and Pap1 as some of the major targets.","doi":"10.1016/j.jprot.2011.05.030","authors":"García-Santamarina S, Boronat S, Espadas G, Ayté J, Molina H, Hidalgo E","authors_abbrev":"García-Santamarina S et al.","pubmed_publication_date":"19 Oct 2011","pubmed_entrez_date":"2011-06-16","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30321329","title":"The Contribution of Purifying Selection, Linkage, and Mutation Bias to the Negative Correlation between Gene Expression and Polymorphism Density in Yeast Populations.","citation":"Genome Biol Evol 2018 Nov 01;10(11):2986-2996","abstract":"The negative correlation between the rate of protein evolution and expression level of a gene has been recognized as a universal law of the evolutionary biology (Koonin 2011). In our study, we apply a population-based approach to systematically investigate the relative importance of unequal mutation rate, linkage, and selection in the origin of the expression-polymorphism anticorrelation. We analyzed the DNA sequence of protein coding genes of 24 Saccharomyces cerevisiae and 58 Schizosaccharomyces pombe strains. We found that highly expressed genes had a substantially decreased number of polymorphic sites when compared with genes transcribed less extensively. This expression-dependent reduction was especially strong in the nonsynonymous sites, although it was also present in the synonymous sites and untranslated regions, both up and down of a gene. Most importantly, no such trend was found in introns. We used these observations, as well as analyses of site frequency spectra and data from mutation accumulation experiments, to show that the purifying selection acting on nonsynonymous sites was the main, but not exclusive, factor impeding molecular evolution within the coding sequences of highly expressed genes. Linkage could not fully explain the observed pattern of polymorphism within the untranslated regions and synonymous sites, although the contribution of selection acting directly on synonymous variants was extremely small. Finally, we found that the impact of mutational bias was rather negligible.","doi":"10.1093/gbe/evy225","authors":"Marek A, Tomala K","authors_abbrev":"Marek A et al.","pubmed_publication_date":"01 Nov 2018","pubmed_entrez_date":"2018-10-16","publication_year":"2018","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2018-10-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11533255","title":"Study of cyclin proteolysis in anaphase-promoting complex (APC) mutant cells reveals the requirement for APC function in the final steps of the fission yeast septation initiation network.","citation":"Mol Cell Biol 2001 Oct;21(19):6681-94","abstract":"Cytokinesis in eukaryotic cells requires the inactivation of mitotic cyclin-dependent kinase complexes. An apparent exception to this relationship is found in Schizosaccharomyces pombe mutants with mutations of the anaphase-promoting complex (APC). These conditional lethal mutants arrest with unsegregated chromosomes because they cannot degrade the securin, Cut2p. Although failing at nuclear division, these mutants septate and divide. Since septation requires Cdc2p inactivation in wild-type S. pombe, it has been suggested that Cdc2p inactivation occurs in these mutants by a mechanism independent of cyclin degradation. In contrast to this prediction, we show that Cdc2p kinase activity fluctuates in APC cut mutants due to Cdc13/cyclin B destruction. In APC-null mutants, however, septation and cutting do not occur and Cdc13p is stable. We conclude that APC cut mutants are hypomorphic with respect to Cdc13p degradation. Indeed, overproduction of nondestructible Cdc13p prevents septation in APC cut mutants and the normal reorganization of septation initiation network components during anaphase.","authors":"Chang L, Morrell JL, Feoktistova A, Gould KL","authors_abbrev":"Chang L et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-09-05","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.01c","SPCC1739.11c","SPBC582.03","SPAC17C9.01c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:8165279","title":"[Molecular control of G1/S transition in fission yeast].","citation":"Tanpakushitsu Kakusan Koso 1994 Mar;39(4):345-54","abstract":"","authors":"Tanaka K, Okayama H","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28049778","title":"Immunolocalization of Proteins in Fission Yeast by Electron Microscopy.","citation":"Cold Spring Harb Protoc 2017 Jan 03;2017(1)","abstract":"Electron microscopy (EM) immunolocalization of antigens in fission yeast can be accomplished with cells processed by rapid freezing and freeze-substitution followed by embedding in acrylic or methacrylate resins. Microtome sections of embedded cells are collected onto EM grids. Primary antibodies to the antigen of interest, followed by secondary antibodies conjugated to colloidal gold, are allowed to bind to antigens at the surface of these plastic sections. This type of postembed labeling provides information on antigen localization to a resolution of 10-20 nm, depending on the size of the metal particle used, the form of the antibody (Fab vs. complete IgG or IgM), and whether direct or indirect labeling is used. The method has the potential to map macromolecules in three dimensions in a relatively large volume when thin (30-60-nm) serial sections are labeled, imaged, aligned, and modeled to create a representative volume. The biggest challenge of this technique is the necessary compromise between the preservation of cellular ultrastructure and the preservation of antigen reactivity. The protocols described here show how to immunolabel samples for EM and include suggestions for overcoming challenges related to antigen preservation.","doi":"10.1101/pdb.prot091322","authors":"Morphew MK, Giddings TH, McIntosh JR","authors_abbrev":"Morphew MK et al.","pubmed_publication_date":"03 Jan 2017","pubmed_entrez_date":"2017-01-05","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-01-06 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23213482","title":"TORC2 and the AGC kinase Gad8 regulate phosphorylation of the ribosomal protein S6 in fission yeast.","citation":"Biol Open 2012 Sep 15;1(9):884-8","abstract":"TOR (Target Of Rapamycin) signalling coordinates cell growth and division in response to changes in the nutritional environment of the cell. TOR kinases form two distinct complexes: TORC1 and TORC2. In mammals, the TORC1 controlled S6K1 kinase phosphorylates the ribosomal protein S6 thereby co-ordinating cell size and nutritional status. We show that the Schizosaccharomyces pombe AGC kinase Gad8 co-immunoprecipitates with the ribosomal protein S6 (Rps6) and regulates its phosphorylation status. It has previously been shown that Gad8 is phosphorylated by TORC2. Consistent with this, we find that TORC2 as well as TORC1 modulates Rps6 phosphorylation. Therefore, S6 phosphorylation in fission yeast actually represents a read-out of the combined activities of TORC1 and TORC2. In contrast, we find that the in vivo phosphorylation status of Maf1 (a repressor of RNA polymerase III) specifically correlates with TORC1 activity.","doi":"10.1242/bio.20122022","authors":"Du W, Hálová L, Kirkham S, Atkin J, Petersen J","authors_abbrev":"Du W et al.","pubmed_publication_date":"15 Sep 2012","pubmed_entrez_date":"2012-12-06","publication_year":"2012","canto_session_key":"20cb5afb210529f7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.07","SPAC21E11.04","SPBC354.12","SPAC3C7.14c","SPCC1902.02","SPAC31G5.12c","SPAPB1E7.12","SPCC364.03","SPBC649.02","SPAC11G7.03"],"gene_count":10,"ltp_gene_count":9},{"uniquename":"PB_REF:0000007","title":"Prediction of GPI-anchored proteins with pointer neural networks","abstract":"GPI-anchors constitute a very important post-translational modification, linking many proteins to the outer face of the plasma membrane in eukaryotic cells. Since experimental validation of GPI-anchoring signals is slow and costly, computatinal approaches for predicting them from amino acid sequences are needed. However, the most recent GPI predictor is more than a decade old and considerable progress has been made in machine learning since then. We present a new dataset and a novel method, NetGPI, for GPI signal prediction. NetGPI is based on recurrent neural networks, incorporating an attention mechanism that simultaneously detects GPI-anchoring signals and points out the location of their ω-sites. The performance of NetGPI is superior to existing methods with regards to discrimination between GPI-anchored proteins and other secretory proteins and approximate (±1 position) placement of the ω-site.","authors":"Magnús Halldór Gíslason, Henrik Nielsen, José Juan Almagro Armenteros, Alexander Rosenberg Johansen.","canto_curator_role":"PomBase","annotation_curators":[],"file_curator_name":"Pascal Carme","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":47,"orcid":"0009-0003-9059-1333","file_type":"protein_modification","file_name":"PB_REF_0000007_modifications.tsv"}],"genes":["SPAC11E3.13c","SPCC970.02","SPCC1795.12c","SPAC11D3.19","SPBC16A3.13","SPCC63.02c","SPBC2A9.08c","SPCC24B10.06","SPAC23C4.13","SPAPB8E5.08","SPAC27E2.11c","SPBPB7E8.01","SPAPB18E9.04c","SPBC31E1.04","SPAC23D3.14c","SPCC757.12","SPCC553.10","SPAC4D7.02c","SPCC825.03c","SPBC36B7.07","SPAC1786.02","SPCC895.04c","SPAC1F5.08c","SPAPB15E9.01c","SPAC17A5.04c","SPBPJ4664.02","SPAC1A6.03c","SPCC1795.09","SPBP19A11.02c","SPAC1705.03c","SPAC23A1.15c","SPAC26A3.01","SPAC750.07c","SPCC1322.10","SPBC1198.07c","SPBC1E8.05","SPAC31A2.13c","SPBC215.13","SPAC19B12.02c","SPAC1F8.02c","SPBC29A3.21","SPAC212.12","SPCC1322.07c","SPBC405.02c","SPCC1742.01","SPAC19G12.16c","SPBC146.11c"],"gene_count":47,"ltp_gene_count":0},{"uniquename":"PMID:4767133","title":"The role of repair mechanisms in the variations of ultraviolet and gamma-radiation sensitivity during the cell cycle of Schizosaccharomyces pombe.","citation":"Radiat Res 1973 Dec;56(3):528-39","abstract":"","authors":"Fabre F","authors_abbrev":"Fabre F","pubmed_publication_date":"Dec 1973","pubmed_entrez_date":"1973-12-01","publication_year":"1973","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35890048","title":"Improving Drug Sensitivity of HIV-1 Protease Inhibitors by Restriction of Cellular Efflux System in a Fission Yeast Model.","citation":"Pathogens 2022 Jul 16;11(7)","abstract":"Fission yeast can be used as a cell-based system for high-throughput drug screening. However, higher drug concentrations are often needed to achieve the same effect as in mammalian cells. Our goal here was to improve drug sensitivity so reduced drugs could be used. Three different methods affecting drug uptakes were tested using an FDA-approved HIV-1 protease inhibitor (PI) drug Darunavir (DRV). First, we tested whether spheroplasts without cell walls increase the drug sensitivity. Second, we examined whether electroporation could be used. Although small improvements were observed, neither of these two methods showed significant increase in the EC 50  values of DRV compared with the traditional method. In contrast, when DRV was tested in a mutant strain PR836 that lacks key proteins regulating cellular efflux, a significant increase in the EC 50  was observed. A comparison of nine FDA-approved HIV-1 PI drugs between the wild-type RE294 strain and the mutant PR836 strain showed marked enhancement of the drug sensitivities ranging from an increase of 0.56 log to 2.48 logs. Therefore, restricting cellular efflux through the adaption of the described fission yeast mutant strain enhances the drug sensitivity, reduces the amount of drug used, and increases the chance of success in future drug discovery.","doi":"10.3390/pathogens11070804","authors":"Zhang J, Li Q, Kawashima SA, Nasr M, Xue F, Zhao RY","authors_abbrev":"Zhang J et al.","pubmed_publication_date":"16 Jul 2022","pubmed_entrez_date":"2022-07-27","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-07-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9745018","title":"The essential schizosaccharomyces pombe cdc23 DNA replication gene shares structural and functional homology with the Saccharomyces cerevisiae DNA43 (MCM10) gene.","citation":"Curr Genet 1998 Sep;34(3):164-71","abstract":"The fission yeast cdc23 gene is required for correct DNA replication: cdc23 mutants show reduced rates of DNA synthesis and become elongated after cell-cycle arrest. We have cloned the Schizosaccharomyces pombe cdc23 gene by complementation of the temperature-sensitive phenotype of cdc23-M36 and confirmed the identity of the gene by integrative mapping. Analysis of the DNA sequence reveals that cdc23 can encode a protein of 593 amino acids (Mr=67 kDa) with 22% overall identity and many structural homologies with the product of the Saccharomyces cerevisiae DNA43 (MCM10) gene which is required for correct initiation of DNA synthesis at chromosomal origins of replication. Construction of a cdc23 null allele has established that the cdc23 gene is essential for viability, with cdc23 deletion mutant spores germinating but undergoing arrest with undivided nuclei in the first or second cell cycle. The S. pombe cdc23 gene on an expression plasmid is able to complement the S. cerevisiae dna43-1 mutant. These structural and functional homologies between two distantly related species suggest that cdc23 and DNA43 may represent genes for a conserved essential eukaryotic DNA replication function.","authors":"Aves SJ, Tongue N, Foster AJ, Hart EA","authors_abbrev":"Aves SJ et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-09-24","publication_year":"1998","canto_session_key":"485846ecb05d07fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-04 13:58:53","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-09-04 13:58:48","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-04"},{"uniquename":"EMBL:AB176672","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:672898","title":"Mutants altered in the control co-ordinating cell division with cell growth in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1978 May 03;161(2):215-20","abstract":"The control co-ordinating cell division with cell growth has been investigated in the fission yeast Schizosaccharomyces pombe. Twenty-five mutants altered in this control have been isolated which have the same growth rate as wild type but divide at a smaller cell size. The mutants define two genes wee 1 and wee 2, both of which are involved in a control initiating mitosis when the cell attains a critical size.","authors":"Thuriaux P, Nurse P, Carter B","authors_abbrev":"Thuriaux P et al.","pubmed_publication_date":"03 May 1978","pubmed_entrez_date":"1978-05-03","publication_year":"1978","canto_session_key":"5bd08da8d2043fd0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ryoko Mandeville","canto_first_approved_date":"2013-07-17 14:26:56","canto_approved_date":"2022-03-13 12:27:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-16 14:57:49","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Ryoko Mandeville","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC18B5.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-07-17"},{"uniquename":"PMID:28426144","title":"A multiplex culture system for the long-term growth of fission yeast cells.","citation":"Yeast 2017 Aug;34(8):343-355","abstract":"Maintenance of long-term cultures of yeast cells is central to a broad range of investigations, from metabolic studies to laboratory evolution assays. However, repeated dilutions of batch cultures lead to variations in medium composition, with implications for cell physiology. In Saccharomyces cerevisiae, powerful miniaturized chemostat setups, or ministat arrays, have been shown to allow for constant dilution of multiple independent cultures. Here we set out to adapt these arrays for continuous culture of a morphologically and physiologically distinct yeast, the fission yeast Schizosaccharomyces pombe, with the goal of maintaining constant population density over time. First, we demonstrated that the original ministats are incompatible with growing fission yeast for more than a few generations, prompting us to modify different aspects of the system design. Next, we identified critical parameters for sustaining unbiased vegetative growth in these conditions. This requires deletion of the gsf2 flocculin-encoding gene, along with addition of galactose to the medium and lowering of the culture temperature. Importantly, we improved the flexibility of the ministats by developing a piezo-pump module for the independent regulation of the dilution rate of each culture. This made it possible to easily grow strains that have different generation times in the same assay. Our system therefore allows for maintaining multiple fission yeast cultures in exponential growth, adapting the dilution of each culture over time to keep constant population density for hundreds of generations. These multiplex culture systems open the door to a new range of long-term experiments using this model organism. © 2017 The Authors. Yeast published by John Wiley & Sons, Ltd.","doi":"10.1002/yea.3237","authors":"Callens C, Coelho NC, Miller AW, Sananes MRD, Dunham MJ, Denoual M, Coudreuse D","authors_abbrev":"Callens C et al.","pubmed_publication_date":"Aug 2017","pubmed_entrez_date":"2017-04-21","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-04-22 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9251042","title":"Analysis of radiation-sensitive mutants of fission yeast.","citation":"Methods Enzymol 1997;283:471-94","abstract":"","authors":"Edwards RJ, Carr AM","authors_abbrev":"Edwards RJ et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35622511","title":"Genetic interaction of the histone chaperone  hip1  +   with double strand break repair genes in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2022;2022","abstract":" Schizosaccharomyces pombe    hip1  +    (human HIRA) is a histone chaperone and transcription factor involved in establishment of the centromeric chromatin and chromosome segregation, regulation of histone transcription, and cellular response to stress. We carried out a double mutant genetic screen of  Δhip1  and mutations in double strand break repair pathway. We find that   hip1  +    functions after the MRN complex which initiates resection of blunt double strand break ends but before recruitment of the DNA damage repair machinery. Further, deletion of   hip1  +    partially suppresses sensitivity to DNA damaging agents of mutations in genes involved in Break Induced Replication (BIR), one mechanism of rescue of stalled or collapses replication forks (   rad51  +    ,   cdc27  +    ).  Δhip1  also suppresses mutations in two checkpoint genes (   cds1  +    ,   rad3  +    ) on hydroxyurea a drug that stalls replication forks. Our results show that   hip1  +    forms complex interactions with the DNA double strand break repair genes and may be involved in facilitating communication between damage sensors and downstream factors.","doi":"10.17912/micropub.biology.000545","authors":"Disbennett WM, Hawk TM, Rollins PD, Nelakurti DD, Lucas BE, McPherson MT, Hylton HM, Petreaca RC","authors_abbrev":"Disbennett WM et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-05-27","publication_year":"2022","canto_session_key":"b9d31bce0a94d5d1","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-05-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8413241","title":"Schizosaccharomyces pombe Spk1 is a tyrosine-phosphorylated protein functionally related to Xenopus mitogen-activated protein kinase.","citation":"Mol Cell Biol 1993 Oct;13(10):6427-34","abstract":"Mitogen-activated protein kinase (MAPK) and its direct activator, MAPK kinase (MAPKK), have been suggested to play a pivotal role in a variety of signal transduction pathways in higher eukaryotes. The fission yeast Schizosaccharomyces pombe carries a gene, named spk1, whose product is structurally related to vertebrate MAPK. Here we show that Spk1 is functionally related to Xenopus MAPK. (i) Xenopus MAPK partially complemented a defect in the spk1- mutant. An spk1- diploid strain could not sporulate, but one carrying Xenopus MAPK could. (ii) Both Spk1 and Xenopus MAPK interfered with sporulation if overexpressed in S. pombe cells. (iii) Spk1 underwent tyrosine phosphorylation as does Xenopus MAPK. Tyrosine phosphorylation of Spk1 appeared to be dependent upon mating signals because it occurred in homothallic cells but not in heterothallic cells. Furthermore, this phosphorylation was diminished in a byr1 disruptant strain, suggesting that spk1 lies downstream of byr1, which encodes a MAPKK homolog in S. pombe. Taken together, the MAPKK-MAPK cascade may be evolutionarily conserved in signaling pathways in yeasts and vertebrates.","authors":"Gotoh Y, Nishida E, Shimanuki M, Toda T, Imai Y, Yamamoto M","authors_abbrev":"Gotoh Y et al.","pubmed_publication_date":"Oct 1993","pubmed_entrez_date":"1993-10-01","publication_year":"1993","canto_session_key":"ad5cdccac663e13f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-02 13:17:43","canto_approved_date":"2025-12-12 12:32:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 13:58:49","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC1D4.13","SPAC31G5.09c","SPBC1D7.05"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-10-02"},{"uniquename":"PMID:20062850","title":"Probing intracellular oxygen by quenched phosphorescence lifetimes of nanoparticles containing polyacrylamide-embedded [Ru(dpp(SO3Na)2)3]Cl2.","citation":"Photochem Photobiol Sci 2010 Jan;9(1):103-9","abstract":"Methods for measuring O(2) within living cells that rely on luminescent probes are hampered by several factors: local conditions of hydrophobicity, pH, ionic composition, dielectric constant, and photobleaching by free radical species. Use of a polymer-embedded luminophore should minimize these problems. Here we use a Ru(II) coordination complex embedded within 45 nm hydrodynamic diameter nanoparticles, and demonstrate that both phosphorescence intensity and lifetimes are O(2)-sensitive, both in aqueous suspensions and intracellularly (e.g. 4.06 versus 1.55 microseconds under anaerobic or aerobic conditions, respectively). Electroporation is necessary for incorporation of the nanoparticles into yeasts: it is more effective with the fission yeast, Schizosaccharomyces pombe, than for the budding yeast, Saccharomyces cerevisiae. However, electroporation was not required for particle uptake into a cultured human cell-line (mammary adenosarcoma MCF-7), although the intracellular distribution of the probe is more general to intracellular compartments when electroporation is employed. These procedures did not compromise vitality of cells over periods of 6 h, as judged by retention of structural characteristics evident in Nomarski interference or confocal microscopy images. Spatial resolution of intracellular structures defined by nanoparticle phosphorescence intensity imaging indicates potential usefulness of the application of lifetime imaging techniques for mapping of intracellular O(2) distributions.","doi":"10.1039/b9pp00071b","authors":"Coogan MP, Court JB, Gray VL, Hayes AJ, Lloyd SH, Millet CO, Pope SJ, Lloyd D","authors_abbrev":"Coogan MP et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2010-01-12","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10753785","title":"Think global, act local--how to regulate S phase from individual replication origins.","citation":"Curr Opin Genet Dev 2000 Apr;10(2):178-86","abstract":"All eukaryotes use similar proteins to licence replication origins but, paradoxically, origin DNA is much less conserved. Specific binding sites for these proteins have now been identified on fission yeast and Drosophila chromosomes, suggesting that the DNA-binding activity of the origin recognition complex has diverged to recruit conserved initiation factors on polymorphic replication origins. Once formed, competent origins are activated by cyclin- and Dbf4-dependent kinases. The latter have been shown to control S phase in several organisms but, in contrast to cyclin-dependent kinases, seem regulated at the level of individual origins. Global and local regulations generate specific patterns of DNA replication that help establish epigenetic chromosome states.","authors":"Pasero P, Schwob E","authors_abbrev":"Pasero P et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-04-08","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8221938","title":"Effective long range mapping in Schizosaccharomyces pombe with the help of swi5.","citation":"Curr Genet 1993 Sep;24(3):271-3","abstract":"The switching gene swi5 has a function in mating-type switching. In addition, the swi5 mutation causes an increased radiation sensitivity and reduces meiotic recombination about ten-fold. Based on the latter property, an experimental protocol was developed for using swi5 in long-range mapping in S. pombe. It is suitable for a speedy mapping of any new gene which has not yet been cloned. The procedure was used to clarify the map positions of some genes.","authors":"Schmidt H","authors_abbrev":"Schmidt H","pubmed_publication_date":"Sep 1993","pubmed_entrez_date":"1993-09-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30647069","title":"Spore Germination Requires Ferrichrome Biosynthesis and the Siderophore Transporter Str1 in  Schizosaccharomyces pombe .","citation":"Genetics 2019 Mar;211(3):893-911","abstract":"Spore germination is a process whereby spores exit dormancy to become competent for mitotic cell division. In  Schizosaccharomyces pombe , one critical step of germination is the formation of a germ tube that hatches out the spore wall in a stage called outgrowth. Here, we show that iron deficiency blocks the outgrowth of germinating spores. The siderophore synthetase Sib1 and the ornithine N 5 -oxygenase Sib2 participate in ferrichrome biosynthesis, whereas Str1 functions as a ferrichrome transporter. Expression profiles of  sib1 +   ,  sib2 +   , and  str1 +   transcripts reveal that they are induced shortly after induction of germination and their expression remains upregulated throughout the germination program under low-iron conditions.  sib1 Δ  sib2 Δ mutant spores are unable to form a germ tube under iron-poor conditions. Supplementation with exogenous ferrichrome suppresses this phenotype when  str1 +   is present. Str1 localizes at the contour of swollen spores 4 hr after induction of germination. At the onset of outgrowth, localization of Str1 changes and it moves away from the mother spore to primarily localize at the periphery of the new daughter cell. Two conserved Tyr residues (Tyr 553  and Tyr 567 ) are predicted to be located in the last extracellular loop region of Str1. Results show that these amino acid residues are critical to ensure timely completion of the outgrowth phase of spores in response to exogenous ferrichrome. Taken together, the results reveal the essential requirement of ferrichrome biosynthesis to promote outgrowth, as well as the necessity to take up ferrichrome from an external source via Str1 when ferrichrome biosynthesis is blocked.","doi":"10.1534/genetics.118.301843","authors":"Plante S, Labbé S","authors_abbrev":"Plante S et al.","pubmed_publication_date":"Mar 2019","pubmed_entrez_date":"2019-01-17","publication_year":"2019","canto_session_key":"9e718e289b49a63c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-01-18 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26334349","title":"Inhibition of the Arg/N-end rule pathway-mediated proteolysis by dipeptide-mimetic molecules.","citation":"Amino Acids 2016 Jan;48(1):235-43","abstract":"Ubr11 in the fission yeast Schizosaccharomyces pombe is an evolutionarily conserved ubiquitin ligase functioning in the Arg/N-end rule pathway, which promotes degradation of substrate proteins via the proteasome. Ubr11 recognizes the N-degron sequence in substrates. The primary N-degron contains a destabilization-inducing N-terminal amino acid, which is either a basic (type 1) or bulky hydrophobic (type 2) residue. Dipeptides are known to inhibit proteolytic degradation via the Arg/N-end rule pathway. Here, I examined the potency of some amino acid- or dipeptide-related molecules in their inhibition of Ubr11/N-end rule-mediated degradation. An amide form of L-arginine and L-tryptophan had weak inhibitory activity for type 1 and type 2 substrates, respectively, although the unmodified amino acid monomer and its carboxymethylated ester were ineffective. Among the naturally occurring dipeptides tested, Lys-Leu and Tyr-Leu showed potent inhibitory activity, but their effect was transient, especially at submillimolar concentrations. L-arginine-β-naphthylamide (Arg-βNA) showed stronger activity than several dipeptides for type 1 substrates, but all Lys-Leu, Tyr-Leu, and Arg-βNA caused growth retardation. The inhibitory activity of the L-phenylalanine carbobenzoxy-hydrazide for type 2 substrates was not very strong, but it prolonged the action of Tyr-Leu at low concentrations and, importantly, did not interfere with cell growth. Apart from their utility, these dipeptidomimetics provide a clue for understanding the determinants of recognition by Ubr ubiquitin ligase and further designing novel inhibitors of the Arg/N-end rule pathway.","doi":"10.1007/s00726-015-2083-1","authors":"Kitamura K","authors_abbrev":"Kitamura K","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2015-09-04","publication_year":"2016","canto_session_key":"d086aed7ecfc96f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-10-13 01:20:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-09 00:33:24","canto_added_date":"2015-09-05 00:19:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15A10.11","SPBC13A2.04c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2015-10-09"},{"uniquename":"PMID:5347640","title":"The uptake of bases and their incorporation into RNA during the cell cycle of Schizosaccharomyces pombe in normal growth and after a step-down.","citation":"Exp Cell Res 1969 Oct;57(2):411-22","abstract":"","authors":"Mitchison JM, Cummins JE, Gross PR, Creanor J","authors_abbrev":"Mitchison JM et al.","pubmed_publication_date":"Oct 1969","pubmed_entrez_date":"1969-10-01","publication_year":"1969","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10620770","title":"Gene sam1 encoding adenosylmethionine synthetase: effects of its expression in the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2000 Jan 15;16(1):1-10","abstract":"By screening gene libraries of Schizosaccharomyces pombe with a DNA fragment encoding part of the Saccharomyces cerevisiae S-adenosylmethionine synthetase (SAMS), we isolated the fission yeast sam1 gene. Its sequence exhibits good homology to SAMSs of other organisms and reveals the motifs characteristic for SAMSs. SAMS activity and sam1 mRNA levels decrease when cells enter stationary phase. In haploid strains, gene sam1 is essential for growth; if weakly expressed, cells mate and sporulate at a reduced rate. Strains overexpressing sam1 exhibit methionine-sensitive growth. This methionine-induced growth inhibition is partially relieved by adenine. We assume that methionine reduces the level of one or several adenine nucleotides by a SAMS-mediated mechanism. Intracellular SAM levels increase drastically by exogenously added methionine. This increase predicts that mutants exhibiting methionine revertible phenotypes can be indicative for mutations in proteins exhibiting SAM-dependent functions. In agreement with this prediction, we show that mutant pmt2-5 has this phenotype and that gene pmt2 encodes a potential SAM-dependent enzyme.","authors":"Hilti N, Gräub R, Jörg M, Arnold P, Schweingruber AM, Schweingruber ME","authors_abbrev":"Hilti N et al.","pubmed_publication_date":"15 Jan 2000","pubmed_entrez_date":"2000-01-06","publication_year":"2000","canto_session_key":"d131e3d5b6ca57f2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-01-27 23:40:41","canto_approved_date":"2026-01-27 23:40:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-01-25 15:00:57","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14F5.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2026-01-27"},{"uniquename":"PMID:10944588","title":"Fission yeast on the brink of meiosis.","citation":"Bioessays 2000 Sep;22(9):854-60","abstract":"The fission yeast Schizosaccharomyces pombe (S. pombe) is now well established as a versatile genetic model organism. It is widely used to analyse the basic eukaryotic cell cycle during vegetative growth and it is also well suited to studies on the elementary processes of sexual reproduction, including intercellular communication and signal transduction in zygote formation, as well as meiosis before sporulation. Systematic mutant screening has contributed much to our current understanding of unicellular differentiation in S. pombe, and structural analysis has revealed a simplified meiotic prophase with abundant crossing-over but no homologue synapsis. This article is a personal account of how this branch of fission yeast genetics has developed.","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-08-17","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12692246","title":"A long terminal repeat-containing retrotransposon of Schizosaccharomyces pombe expresses a Gag-like protein that assembles into virus-like particles which mediate reverse transcription.","citation":"J Virol 2003 May;77(9):5451-63","abstract":"The Tf1 element of Schizosaccharomyces pombe is a long terminal repeat-containing retrotransposon that encodes functional protease, reverse transcriptase, and integrase proteins. Although these proteins are known to be necessary for protein processing, reverse transcription, and integration, respectively, the function of the protein thought to be Gag has not been determined. We present here the first electron microscopy of Tf1 particles. We tested whether the putative Gag of Tf1 was required for particle formation, packaging of RNA, and reverse transcription. We generated deletions of 10 amino acids in each of the four hydrophilic domains of the protein and found that all four mutations reduced transposition activity. The N-terminal deletion removed a nuclear localization signal and inhibited nuclear import of the transposon. The two mutations in the center of Gag destabilized the protein and resulted in no virus-like particles. The C-terminal deletion caused a defect in RNA packaging and, as a result, low levels of cDNA. The electron microscopy of cells expressing a truncated Tf1 showed that Gag alone was sufficient for the formation of virus-like particles. Taken together, these results indicate that Tf1 encodes a Gag protein that is a functional equivalent of the Gag proteins of retroviruses.","authors":"Teysset L, Dang VD, Kim MK, Levin HL","authors_abbrev":"Teysset L et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-04-15","publication_year":"2003","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29761456","title":"PomBase: The Scientific Resource for Fission Yeast.","citation":"Methods Mol Biol 2018;1757:49-68","abstract":"The fission yeast Schizosaccharomyces pombe has become well established as a model species for studying conserved cell-level biological processes, especially the mechanics and regulation of cell division. PomBase integrates the S. pombe genome sequence with traditional genetic, molecular, and cell biological experimental data as well as the growing body of large datasets generated by emerging high-throughput methods. This chapter provides insight into the curation philosophy and data organization at PomBase, and provides a guide to using PomBase for infrequent visitors and anyone considering exploring S. pombe in their research.","doi":"10.1007/978-1-4939-7737-6_4","authors":"Lock A, Rutherford K, Harris MA, Wood V","authors_abbrev":"Lock A et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-05-16","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-05-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:133982","title":"Action of intracellular proteinases on mitochondrial translation products of Neurospora crassa Schizosaccharomyces pombe.","citation":"Hoppe Seylers Z Physiol Chem 1976 Mar;357(3):415-26","abstract":"Gel electrophoretic analysis of mitochondrial membranes from Neurospora crassa shows the presence of a polypeptide fraction with apparent molecular weights of 7000 - 1200, which is synthesized on mitochondrial ribosomes. This fraction comprises between 10 and 50% of total mitochondrial translation products. Evidence is presented that the major part of this fraction is derived from components with higher apparent molecular weights by proteolytic activity. The proteolytic activity is located in vesicles which are co-isolated with mitochondria upon differential centrifugation. The activity is strongly enhanced by application of detergents such as sodium dodecylsulfate and Triton. Proteins synthesized on mitochondrial as well as cytoplasmic ribosomes are subject to proteolytic breakdown. This proteolysis can be blocked by addition of inhibitors such as diisopropylfluorphosphate to isolated mitochondria. Similar observations were made with Schizosaccharomyces pombe. In Neurospora, the amount of mitochondrial translation products with apparent molecular weights of less than 12000 is low in mitochondria from cells treated with cycloheximide for 1 h and high in mitochondria from cells treated with cycloheximide for 5 min. This observation is explained by the finding that proteinase activity in mitochondrial preparations decreases exponentially with a t1/2 of 20 min during preincubation of cells with cycloheximide. Procedures are described to remove or block contaminating proteinase activity. The results appear to be relevant for the interpretation of many data obtained from experiments in which this puzzling kind of artifact has not been sufficiently considered.","authors":"Michel R, Liebl A, Hartmann A, Neupert W","authors_abbrev":"Michel R et al.","pubmed_publication_date":"Mar 1976","pubmed_entrez_date":"1976-03-01","publication_year":"1976","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28349391","title":"Ribosome Profiling for the Analysis of Translation During Yeast Meiosis.","citation":"Methods Mol Biol 2017;1471:99-122","abstract":"Ribosome profiling provides a genome-wide view of translation with unprecedented resolution. Application of this approach to fission and budding yeast revealed widespread regulation of translational efficiency, translation of short open reading frames on unannotated transcripts, and frequent translation of open reading frames in 5' leader sequences. We present here a detailed protocol for the application of ribosome profiling to meiotic fission yeast cells, although the approach should be easily adapted to budding yeast.","doi":"10.1007/978-1-4939-6340-9_4","authors":"Duncan C, Mata J","authors_abbrev":"Duncan C et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-03-29","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-03-31 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15380095","title":"Comparative analysis of cytokinesis in budding yeast, fission yeast and animal cells.","citation":"Curr Biol 2004 Sep 21;14(18):R806-18","abstract":"Cytokinesis is a temporally and spatially regulated process through which the cellular constituents of the mother cell are partitioned into two daughter cells, permitting an increase in cell number. When cytokinesis occurs in a polarized cell it can create daughters with distinct fates. In eukaryotes, cytokinesis is carried out by the coordinated action of a cortical actomyosin contractile ring and targeted membrane deposition. Recent use of model organisms with facile genetics and improved light-microscopy methods has led to the identification and functional characterization of many proteins involved in cytokinesis. To date, this analysis indicates that some of the basic components involved in cytokinesis are conserved from yeast to humans, although their organization into functional machinery that drives cytokinesis and the associated regulatory mechanisms bear species-specific features. Here, we briefly review the current status of knowledge of cytokinesis in the budding yeast Saccharomyces cerevisiae, the fission yeast Schizosaccharomyces pombe and animal cells, in an attempt to highlight both the common and the unique features. Although these organisms diverged from a common ancestor about a billion years ago, there are eukaryotes that are far more divergent. To evaluate the overall evolutionary conservation of cytokinesis, it will be necessary to include representatives of these divergent branches. Nevertheless, the three species discussed here provide substantial mechanistic diversity.","authors":"Balasubramanian MK, Bi E, Glotzer M","authors_abbrev":"Balasubramanian MK et al.","pubmed_publication_date":"21 Sep 2004","pubmed_entrez_date":"2004-09-24","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12574132","title":"Multiple ORC-binding sites are required for efficient MCM loading and origin firing in fission yeast.","citation":"EMBO J 2003 Feb 17;22(4):964-74","abstract":"In most eukaryotes, replication origins are composed of long chromosome regions, and the exact sequences required for origin recognition complex (ORC) and minichromosome maintenance (MCM) complex association remain elusive. Here, we show that two stretches of adenine/thymine residues are collectively essential for a fission yeast chromosomal origin. Chromatin immunoprecipitation assays revealed that the ORC subunits are located within a 1 kb region of ori2004. Analyses of deletion derivatives of ori2004 showed that adenine stretches are required for ORC binding in vivo. Synergistic interaction between ORC and adenine stretches was observed. On the other hand, MCM subunits were localized preferentially to a region near the initiation site, which is distant from adenine stretches. This association was dependent on adenine stretches and stimulated by a non-adenine element. Our results suggest that association of multiple ORC molecules with a replication origin is required for efficient MCM loading and origin firing in fission yeast.","authors":"Takahashi T, Ohara E, Nishitani H, Masukata H","authors_abbrev":"Takahashi T et al.","pubmed_publication_date":"17 Feb 2003","pubmed_entrez_date":"2003-02-08","publication_year":"2003","canto_session_key":"9bada760dbf01004","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-10 10:01:00","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-10 09:57:38","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.15","SPBC211.04c","SPBC25D12.03c","SPBC4.04c"],"gene_count":4,"ltp_gene_count":0,"approved_date":"2014-09-10"},{"uniquename":"PMID:15716492","title":"Optimizing the nucleotide sequence of a meiotic recombination hotspot in Schizosaccharomyces pombe.","citation":"Genetics 2005 Apr;169(4):1973-83","abstract":"The ade6-M26 mutation of Schizosaccharomyces pombe created a meiotic recombination hotspot. Previous analyses indicated that the heptamer 5'-ATGACGT-3' was necessary and sufficient for hotspot activity; the Atf1-Pcr1 transcription factor binds to this sequence and activates M26. After finding cases in which the M26 heptamer in ade6 was, surprisingly, not active as a hotspot, we used an in vitro selection method (SELEX) that revealed an 18-bp consensus sequence for Atf1-Pcr1 binding, 5'-GNVTATGACGTCATNBNC-3', containing the M26 heptamer at its core. Using this consensus sequence as a guide, we made mutations on each side of the heptamer at two separate sites in ade6. These mutations increased the intracellular hotspot activity of the heptamer, in some cases by >15-fold. These results show that M26, the eukaryotic recombination hotspot with the most precisely defined nucleotide sequence, is larger than previously thought, and they provide valuable information for clarifying the role of M26, and perhaps other hotspots, in meiotic recombination.","authors":"Steiner WW, Smith GR","authors_abbrev":"Steiner WW et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-02-18","publication_year":"2005","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27334362","title":"Inner nuclear membrane protein Lem2 augments heterochromatin formation in response to nutritional conditions.","citation":"Genes Cells 2016 Aug;21(8):812-32","abstract":"Inner nuclear membrane proteins interact with chromosomes in the nucleus and are important for chromosome activity. Lem2 and Man1 are conserved members of the LEM-domain nuclear membrane protein family. Mutations of LEM-domain proteins are associated with laminopathy, but their cellular functions remain unclear. Here, we report that Lem2 maintains genome stability in the fission yeast Schizosaccharomyces pombe. S. pombe cells disrupted for the lem2(+) gene (lem2∆) showed slow growth and increased rate of the minichromosome loss. These phenotypes were prominent in the rich culture medium, but not in the minimum medium. Centromeric heterochromatin formation was augmented upon transfer to the rich medium in wild-type cells. This augmentation of heterochromatin formation was impaired in lem2∆ cells. Notably, lem2∆ cells occasionally exhibited spontaneous duplication of genome sequences flanked by the long-terminal repeats of retrotransposons. The resulting duplication of the lnp1(+) gene, which encodes an endoplasmic reticulum membrane protein, suppressed lem2∆ phenotypes, whereas the lem2∆ lnp1∆ double mutant showed a severe growth defect. A combination of mutations in Lem2 and Bqt4, which encodes a nuclear membrane protein that anchors telomeres to the nuclear membrane, caused synthetic lethality. These genetic interactions imply that Lem2 cooperates with the nuclear membrane protein network to regulate genome stability.","doi":"10.1111/gtc.12385","authors":"Tange Y, Chikashige Y, Takahata S, Kawakami K, Higashi M, Mori C, Kojidani T, Hirano Y, Asakawa H, Murakami Y, Haraguchi T, Hiraoka Y","authors_abbrev":"Tange Y et al.","pubmed_publication_date":"Aug 2016","pubmed_entrez_date":"2016-06-24","publication_year":"2016","canto_session_key":"20f80169cf2b419d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Haruhiko Asakawa","canto_first_approved_date":"2016-09-02 17:05:13","canto_approved_date":"2023-06-08 10:24:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-14 09:41:21","canto_added_date":"2016-06-25 00:15:17","annotation_curators":[{"name":"Haruhiko Asakawa","community_curator":true,"annotation_count":20,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.03c","SPBC8D2.04","SPBC1105.11c","SPAC14C4.05c","SPBC2G2.14","SPBC428.08c","SPAC18G6.10","SPCC188.13c","SPAC1834.04","SPBC1778.02","SPCC1620.07c","SPBC19C7.10","SPBC1105.17"],"gene_count":13,"ltp_gene_count":9,"approved_date":"2016-09-02"},{"uniquename":"PMID:29974204","title":"How does Hsp90 function in RNAi-dependent heterochromatin assembly?","citation":"Curr Genet 2019 Feb;65(1):87-91","abstract":"Heat-shock protein 90 (Hsp90) was recently identified as a silencing factor required for RNA interference (RNAi)-dependent heterochromatin assembly in the fission yeast Schizosaccharomyces pombe. As Hsp90 is known to contribute to the formation of small RNA-containing effector complexes, it would be expected that Hsp90 is also involved in the RNAi pathway in fission yeast. However, upon investigation, we found it very difficult to determine how Hsp90 modulates RNAi-dependent heterochromatin assembly in the cell. A lack of detectable small interfering RNAs in hsp90 mutant cells prevented us from examining the role of Hsp90 in the siRNA loading in the cell. In addition, deletion of genes encoding co-chaperones for Hsp90 appears not to affect RNAi-dependent pericentromeric silencing. One possible approach for elucidating the role of Hsp90 in RNAi-dependent heterochromatin assembly is the use of forward genetic screens to identify novel factors linking Hsp90 with other known RNAi factors. Here, we discuss the benefits of conducting further screenings and present some technical hints to help identify new factors.","doi":"10.1007/s00294-018-0866-0","authors":"Kato H, Okazaki K, Urano T","authors_abbrev":"Kato H et al.","pubmed_publication_date":"Feb 2019","pubmed_entrez_date":"2018-07-06","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-07-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22302936","title":"Tel1(ATM) and Rad3(ATR) phosphorylate the telomere protein Ccq1 to recruit telomerase and elongate telomeres in fission yeast.","citation":"Genes Dev 2012 Feb 01;26(3):241-6","abstract":"In fission yeast, the DNA damage sensor kinases Tel1(ATM) and Rad3(ATR) exist at telomeres and are required for telomere maintenance, but the biological role they play at telomeres is not known. Here we show that the telomere protein Ccq1 is phosphorylated at Thr 93 (threonine residue at amino acid 93) by Tel1(ATM) and Rad3(ATR) both in vitro and in vivo. A ccq1 mutant in which alanine was substituted for Thr 93 failed to recruit telomerase to telomeres and showed gradual shortening of telomeres. These results indicate that the direct phosphorylation of Ccq1 Thr 93 by Tel1 and Rad3 is involved in the recruitment of telomerase to elongate telomeres.","doi":"10.1101/gad.177873.111","authors":"Yamazaki H, Tarumoto Y, Ishikawa F","authors_abbrev":"Yamazaki H et al.","pubmed_publication_date":"01 Feb 2012","pubmed_entrez_date":"2012-02-04","publication_year":"2012","canto_session_key":"f2fc4254b3b5ddca","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPNCRNA.214","SPCC23B6.03c","SPBC216.05","SPCC188.07","SPBC800.03"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:16453756","title":"Histone transcription in cell cycle mutants of fission yeast.","citation":"EMBO J 1987 Apr;6(4):1093-7","abstract":"The level of histone H2B transcripts peak during S-phase of the fission yeast Schizosaccharomyces pombe. The pattern of transcript accumulation has been monitored in temperature-sensitive mutants which block at different times during the cell cycle, at start in G1 where the cell becomes committed to the mitotic cycle, in G1 after start, and during S-phase. Cells blocked before start using cdc10-129 do not accumulate histone H2B transcripts, but cells blocked after start using cdc22-C11 do show accumulation. Transcript levels increase in another mutant cdc20-M10 which also blocks in G1. These experiments establish that histone H2B transcripts increase in level in preparation for S-phase during late G1 before any DNA synthesis. Passage of start begins a sequence of events leading to S-phase which includes an increase in histone H2B transcript levels. In the cdc20 and cdc22 mutants transcript levels do not decrease normally suggesting that the signals which lead to the fall in level are not given in these G1-arrested cells. The mutants cdc17-K42 (defective in DNA ligase) and cdc24-M38 block in late S-phase after the DNA content has doubled. Histone H2B transcripts increase normally but remain at a high level. In these mutants even though DNA content has doubled, the mechanisms which lead to a fall in transcript levels appear not to be brought into play.","authors":"Matsumoto S, Yanagida M, Nurse P","authors_abbrev":"Matsumoto S et al.","pubmed_publication_date":"Apr 1987","pubmed_entrez_date":"1987-04-01","publication_year":"1987","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19001497","title":"Two distinct regions of Mto1 are required for normal microtubule nucleation and efficient association with the gamma-tubulin complex in vivo.","citation":"J Cell Sci 2008 Dec 01;121(Pt 23):3971-80","abstract":"Cytoplasmic microtubule nucleation in the fission yeast Schizosaccharomyces pombe involves the interacting proteins Mto1 and Mto2, which are thought to recruit the gamma-tubulin complex (gamma-TuC) to prospective microtubule organizing centres. Mto1 contains a short amino-terminal region (CM1) that is conserved in higher eukaryotic proteins implicated in microtubule organization, centrosome function and/or brain development. Here we show that mutations in the Mto1 CM1 region generate mutant proteins that are functionally null for cytoplasmic microtubule nucleation and interaction with the gamma-TuC (phenocopying mto1Delta), even though the Mto1-mutant proteins localize normally in cells and can bind Mto2. Interestingly, the CM1 region is not sufficient for efficient interaction with the gamma-TuC. Mutation within a different region of Mto1, outside CM1, abrogates Mto2 binding and also impairs cytoplasmic microtubule nucleation and Mto1 association with the gamma-TuC. However, this mutation allows limited microtubule nucleation in vivo, phenocopying mto2Delta rather than mto1Delta. Further experiments suggest that Mto1 and Mto2 form a complex (Mto1/2 complex) independent of the gamma-TuC and that Mto1 and Mto2 can each associate with the gamma-TuC in the absence of the other, albeit extremely weakly compared to when both Mto1 and Mto2 are present. We propose that Mto2 acts cooperatively with Mto1 to promote association of the Mto1/2 complex with the gamma-TuC.","doi":"10.1242/jcs.038414","authors":"Samejima I, Miller VJ, Groocock LM, Sawin KE","authors_abbrev":"Samejima I et al.","pubmed_publication_date":"01 Dec 2008","pubmed_entrez_date":"2008-11-13","publication_year":"2008","canto_session_key":"ed8fef19dce7d13a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-08-15 22:08:46","canto_approved_date":"2021-11-09 20:12:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-27 14:20:40","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":54,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC417.07c","SPBC365.15","SPBC902.06","SPBC32F12.04"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2018-08-15"},{"uniquename":"PMID:27058310","title":"Nutrients control cell size.","citation":"Cell Cycle 2016 Jul 02;15(13):1655-6","abstract":"","doi":"10.1080/15384101.2016.1172471","authors":"Pérez-Hidalgo L, Moreno S","authors_abbrev":"Pérez-Hidalgo L et al.","pubmed_publication_date":"02 Jul 2016","pubmed_entrez_date":"2016-04-09","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-04-10 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5993687","title":"[First finding of Schizosaccharomyces pombe on grapes].","citation":"Ric Sci 1966 Oct;36(10):1096-8","abstract":"","authors":"Balloni W, Florenzano G, Materassi R","authors_abbrev":"Balloni W et al.","pubmed_publication_date":"Oct 1966","pubmed_entrez_date":"1966-10-01","publication_year":"1966","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2611912","title":"A ribosomal protein gene family from Schizosaccharomyces pombe consisting of three active members.","citation":"Curr Genet 1989 Dec;16(5-6):361-7","abstract":"Recently, we have reported the isolation and characterization of a ribosomal protein gene from the fission yeast Schizosaccharomyces pombe. This gene was called K37. Here we describe the isolation of two genes which are related to the K37 gene. Sequence analysis of these genes revealed open reading frames encoding proteins which are almost identical to the ribosomal protein K37. Furthermore, all three genes are functional as determined by Northern analysis using transformed and wild type cells. The results indicate that S. pombe contains a ribosomal protein gene family, designated the K-family, consisting of three active members. The promoter regions of the three members are compared and several common motifes are identified which might serve as transcriptional activators in these genes.","authors":"Gatermann KB, Teletski C, Gross T, Käufer NF","authors_abbrev":"Gatermann KB et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_session_key":"4759f08b6fa59ce7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 17:38:49","canto_approved_date":"2019-01-31 17:38:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 17:38:39","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC839.04","SPAC1F7.13c","SPBC2F12.07c"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"EMBL:SPC05253","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17406560","title":"A simple method for quantitative determination of polysaccharides in fungal cell walls.","citation":"Nat Protoc 2006;1(6):2995-3000","abstract":"A simple and reliable method for quantitative determination of cell wall polymers in fungal cell with an s.e.m. of 5% is described. This protocol is based on the hydrolysis by sulfuric acid of beta-glucan, mannan, galactomannan and chitin present at different levels in the wall of yeasts and filamentous fungi into their corresponding monomers glucose, mannose, galactose and glucosamine. The released monosaccharides are subsequently separated and quantified by high-performance ionic chromatography coupled to pulse amperometry detection, with a detection limit of 1.0 mug ml(-1). This procedure is well suited to screening a large collection of yeast mutants or to evaluating effects of environmental conditions on cell wall polysaccharide content. This procedure is also applicable to other fungal species, including Schizosaccharomyces pombe, Candida albicans and Aspergillus fumigatus. Results can be obtained in 3 d.","authors":"François JM","authors_abbrev":"François JM","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-04-05","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40152110","title":"The HP1 hinge region: more than just a linker for heterochromatin.","citation":"J Biochem 2025 Mar 27;","abstract":"Heterochromatin plays an important role in eukaryotic cellular functions, including gene silencing, high-order chromatin structure, genome stability, and so on. Heterochromatin protein 1 (HP1), a key component of heterochromatin, is conserved from fission yeast to mammals. HP1 binds to histone H3K9me, a hallmark of heterochromatin, through its N-terminal chromodomain (CD) and self-dimerizes and recruits other chromatin proteins through its C-terminal chromo shadow domain (CSD), acting as an epigenetic reader. Between the CD and CSD is an unstructured, less conserved hinge region, which has been implicated in nucleic acid binding. The molecular dissection of the fission yeast HP1 orthologue, Chp2, recently reported in this journal, elucidated the cooperative DNA binding of the hinge and N-terminus of the CSD, which contributes to the stable association with heterochromatin and gene silencing. In this commentary, we focus on the mechanisms involving the HP1 hinge region, which is more than a simple linker.","doi":"10.1093/jb/mvaf005","authors":"Tachiwana H, Saitoh N","authors_abbrev":"Tachiwana H et al.","pubmed_publication_date":"27 Mar 2025","pubmed_entrez_date":"2025-03-28","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-03-29 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41171630","title":"Septins function in exocytosis via physical interactions with the exocyst complex in fission yeast cytokinesis.","citation":"Elife 2025 Oct 31;13","abstract":"Septins can function as scaffolds for protein recruitment, membrane-bound diffusion barriers, or membrane curvature sensors. Septins are important for cytokinesis, but their exact roles are still obscure. In fission yeast, four septins (Spn1-Spn4) accumulate at the rim of the division plane as rings. The octameric exocyst complex, which tethers exocytic vesicles to the plasma membrane, exhibits a similar localization and is essential for plasma membrane deposition during cytokinesis. Without septins, the exocyst spreads across the division plane but is absent from the rim during septum formation. These results suggest that septins and the exocyst physically interact for proper localization and function. Indeed, we predicted six pairs of interactions between septin and exocyst subunits by AlphaFold, most of them are confirmed by co-immunoprecipitation and yeast two-hybrid assays. Exocyst mislocalization results in mistargeting of secretory vesicles and their cargos, which leads to cell-separation delay in septin mutants. Our results indicate that septins guide the targeting of the exocyst complex on the plasma membrane for vesicle tethering during cytokinesis through physical interactions.","doi":"10.7554/eLife.101113","authors":"Singh D, Liu Y, Zhu YH, Zhang S, Naegele SM, Wu JQ","authors_abbrev":"Singh D et al.","pubmed_publication_date":"31 Oct 2025","pubmed_entrez_date":"2025-10-31","publication_year":"2025","canto_session_key":"7f2bf3a83827909a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Davinder Singh","canto_first_approved_date":"2025-12-11 16:09:00","canto_approved_date":"2026-02-26 16:39:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-11-27 14:10:00","canto_added_date":"2025-11-01 00:25:05","annotation_curators":[{"name":"Davinder Singh","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F10.11","SPAC6F12.08c","SPBC16A3.01","SPAC6G10.05c","SPAC6G9.11","SPAC821.06","SPAC13F5.06c","SPBC106.20","SPCC1235.10c","SPAC18G6.03","SPCC970.09","SPAC17G8.12","SPCC1183.01","SPAC9G1.11c","SPCC622.10c"],"gene_count":15,"ltp_gene_count":10,"approved_date":"2025-12-11"},{"uniquename":"PANTHER:PTHR13155","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23G3.05c","HGNC:368"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:36990657","title":"Iron affects localization of Ght5 in fission yeast.","citation":"FEMS Microbiol Lett 2023 Jan 17;370","abstract":"Iron is an essential cofactor for eukaryotic cells, as well as a toxic metal under certain conditions. On the other hand, glucose is the preferred energy and carbon source by most organisms and is an important signaling molecule in the regulation of biological processes. In Schizosaccharomyces pombe, the Ght5 hexose transporter, known as a high affinity glucose transporter, is required for cell proliferation in low glucose concentrations. Herein, we aimed to investigate the effects of iron stress on the Ght5 hexose transporter under glucose repression and derepression conditions. The effect of iron stress on the expression profile of the ght5 gene was analyzed by RT-qPCR and western blot. The localization of the Ght5-mNeonGreen fusion protein examined with confocal microscopy. Our results revealed that iron stress had an inhibitory effect on ght5 expression, and it altered Ght5 localization on the cell surface, causing it to accumulate in the cytoplasm.","doi":"10.1093/femsle/fnad022","authors":"Akyüz SN, Kina UY, Aly ASI, Palabiyik B","authors_abbrev":"Akyüz SN et al.","pubmed_publication_date":"17 Jan 2023","pubmed_entrez_date":"2023-03-29","publication_year":"2023","canto_session_key":"c17ff0cc4f2c7b7a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-03-31 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1235.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19855184","title":"Spindle function in yeast: a human motor to the rescue.","citation":"Cell Cycle 2009 Nov 01;8(21):3453-4","abstract":"","authors":"Liu H, Endow SA","authors_abbrev":"Liu H et al.","pubmed_publication_date":"01 Nov 2009","pubmed_entrez_date":"2009-10-27","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29423859","title":"Duplication and Transformation of the Schizosaccharomyces pombe Collection of Deletion Strains.","citation":"Methods Mol Biol 2018;1721:197-215","abstract":"We present an efficient and organized method of lithium acetate and polyethylene glycol-based transformation of plasmid DNA into the commercially available collection of Schizosaccharomyces pombe with single-gene deletions. We also describe how to prepare a duplicate collection of the deletion strains in order to preserve the longevity of the master set. These protocols are adapted to the 96-well format of the 3004 strains of the Version 2.0 Bioneer set but can also be used for later releases of the collection. This transformation method typically yields efficiencies in the range between 1.0 × 10 3  and 1.0 × 10 4  transformants per microgram of plasmid DNA. However, some deletion strains transformed with significantly lower efficiencies. We provide a list of these difficult-to-transform strains. Applications for this methodology include the transformation of the deletion set with plasmids necessary for genetic screens.","doi":"10.1007/978-1-4939-7546-4_18","authors":"Rai SK, Atwood-Moore A, Levin HL","authors_abbrev":"Rai SK et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28729673","title":"Distinct functional relevance of dynamic GTPase cysteine methylation in fission yeast.","citation":"Sci Rep 2017 Jul 20;7(1):6057","abstract":"The final step in post-translational processing of Ras and Rho GTPases involves methylation of the prenylated cysteine residue by an isoprenylcysteine-O-carboxyl methyltransferase (ICMT). ICMT activity is essential for cell growth and development in higher eukaryotes, and inhibition of GTPase methylation has become an attractive target in cancer therapy to inactivate prenylated oncoproteins. However, the specificity and dynamics of the GTPase methylation process remain to be fully clarified. Notably, cells lacking Mam4, the ICMT ortholog in the fission yeast Schizosaccharomyces pombe, are viable. We have exploited this feature to analyze the role of methylation on GTPase localization and function. We show that methylation differentially affects GTPase membrane localization, being particularly relevant for plasma membrane tethering and downstream signaling of palmitoylated and farnesylated GTPases Ras1 and Rho2 lacking C-terminal polybasic motifs. Indeed, Ras1 and Rho2 cysteine methylation is required for proper regulation of differentiation elicited by MAPK Spk1 and for stress-dependent activation of the cell integrity pathway (CIP) and its main effector MAPK Pmk1. Further, Mam4 negatively regulates TORC2 signaling by a cross-inhibitory mechanism relying on Rho GTPase methylation. These results highlight the requirement for a tight control of GTPase methylation in vivo to allow adequate GTPase function.","doi":"10.1038/s41598-017-06053-x","authors":"Franco A, Soto T, Martín-García R, Madrid M, Vázquez-Marín B, Vicente-Soler J, Coll PM, Gacto M, Pérez P, Cansado J","authors_abbrev":"Franco A et al.","pubmed_publication_date":"20 Jul 2017","pubmed_entrez_date":"2017-07-22","publication_year":"2017","canto_session_key":"39fe395aaf65be54","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-07-23 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3H7.09","SPAC10F6.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PANTHER:PTHR23284","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:9356","SPBC3H7.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:6032031","title":"Adenine uptake and pool formation in the fission yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1967 Feb 07;136(1):108-20","abstract":"","authors":"Cummins JE, Mitchison JM","authors_abbrev":"Cummins JE et al.","pubmed_publication_date":"07 Feb 1967","pubmed_entrez_date":"1967-02-07","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20089861","title":"Structural basis for L-lysine feedback inhibition of homocitrate synthase.","citation":"J Biol Chem 2010 Apr 02;285(14):10446-53","abstract":"The alpha-aminoadipate pathway of lysine biosynthesis is modulated at the transcriptional and biochemical levels by feedback inhibition. The first enzyme in the alpha-aminoadipate pathway, homocitrate synthase (HCS), is the target of the feedback regulation and is strongly inhibited by l-lysine. Here we report the structure of Schizosaccharomyces pombe HCS (SpHCS) in complex with l-lysine. The structure illustrates that the amino acid directly competes with the substrate 2-oxoglutarate for binding within the active site of HCS. Differential recognition of the substrate and inhibitor is achieved via a switch position within the (alpha/beta)(8) TIM barrel of the enzyme that can distinguish between the C5-carboxylate group of 2-oxoglutarate and the epsilon-ammonium group of l-lysine. In vitro and in vivo assays demonstrate that mutations of the switch residues, which interact with the l-lysine epsilon-ammonium group, abrogate feedback inhibition, as do substitutions of residues within the C-terminal domain that were identified in a previous study of l-lysine-insensitive HCS mutants in Saccharomyces cerevisiae. Together, these results yield new insights into the mechanism of feedback regulation of an enzyme central to lysine biosynthesis.","doi":"10.1074/jbc.M109.094383","authors":"Bulfer SL, Scott EM, Pillus L, Trievel RC","authors_abbrev":"Bulfer SL et al.","pubmed_publication_date":"02 Apr 2010","pubmed_entrez_date":"2010-01-22","publication_year":"2010","canto_session_key":"ba7771dd7ab8e04e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-02-28 13:09:22","canto_approved_date":"2026-03-09 15:58:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-16 13:36:47","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":2,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-28","pdb_entries":[{"pdb_id":"3mi3","gene_chains":[{"gene_uniquename":"SPBC1105.02c","chain":"A/B","position":"1-418"}],"title":"Homocitrate Synthase Lys4 bound to Lysine","entry_authors":"Bulfer SL,Scott EM,Pillus L,Trievel RC","entry_authors_abbrev":"Bulfer SL et al.","reference_uniquename":"PMID:20089861","experimental_method":"X-ray","resolution":"2.38"}]},{"uniquename":"PMID:19450689","title":"The Hermes transposon of Musca domestica and its use as a mutagen of Schizosaccharomyces pombe.","citation":"Methods 2009 Nov;49(3):243-7","abstract":"Transposon mutagenesis allows for the discovery and characterization of genes by creating mutations that can be easily mapped and sequenced. Moreover, this method allows for a relatively unbiased approach to isolating genes of interest. Recently, a system of transposon based mutagenesis for Schizosaccharomyces pombe became available. This mutagenesis relies on Hermes, a DNA transposon from the house fly that readily integrates into the chromosomes of S. pombe. The Hermes system is distinct from the retrotransposons of S. pombe because it efficiently integrates into open reading frames. To mutagenize S. pombe, cells are transformed with a plasmid that contains a drug resistance marker flanked by the terminal inverted repeats of Hermes. The Hermes transposase expressed from a second plasmid excises the resistance marker with the inverted repeats and inserts this DNA into chromosomal sites. After S. pombe with these two plasmids grow 25 generations, approximately 2% of the cells contain insertions. Of the cells with insertions, 68% contain single integration events. The protocols listed here provide the detailed information necessary to mutagenize a strain of interest, screen for specific phenotypes, and sequence the positions of insertion.","doi":"10.1016/j.ymeth.2009.05.004","authors":"Park JM, Evertts AG, Levin HL","authors_abbrev":"Park JM et al.","pubmed_publication_date":"Nov 2009","pubmed_entrez_date":"2009-05-20","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38964378","title":"Prohibitins, Phb1 and Phb2, function as Atg8 receptors to support yeast mitophagy and also play a negative regulatory role in Atg32 processing.","citation":"Autophagy 2024 Jul 04;:1-12","abstract":"The prohibitins Phb1 and Phb2 assemble at the mitochondrial inner membrane to form a multi-dimeric complex. These scaffold proteins are highly conserved in eukaryotic cells, from yeast to mammals, and have been implicated in a variety of mitochondrial functions including aging, proliferation, and degenerative and metabolic diseases. In mammals, PHB2 regulates PINK1-PRKN mediated mitophagy by interacting with lipidated MAP1LC3B/LC3B. Despite their high conservation, prohibitins have not been linked to mitophagy in budding yeasts. In this study, we demonstrate that both Phb1 and Phb2 are required to sustain mitophagy in  Saccharomyces cerevisiae . Prohibitin-dependent mitophagy requires formation of the Phb1-Phb2 complex and a conserved AIM/LIR-like motif identified in both yeast prohibitins. Furthermore, both Phb1 and Phb2 interact and exhibit mitochondrial colocalization with Atg8. Interestingly, we detected a basal C terminus processing of the mitophagy receptor Atg32 that depends on the presence of the i-AAA Yme1. In the absence of prohibitins this processing is highly enhanced but reverted by the inactivation of the rhomboid protease Pcp1. Together our results revealed a novel role of yeast prohibitins in mitophagy through its interaction with Atg8 and regulating an Atg32 proteolytic event.  Abbreviation : AIM/LIR: Atg8-family interacting motif/LC3-interacting region; ANOVA: analysis of variance; ATG/Atg: autophagy related; C terminus/C-terminal: carboxyl terminus/carboxyl-terminal; GFP: green fluorescent protein; HA: human influenza hemagglutinin; Idh1: isocitrate dehydrogenase 1; MAP1C3B/LC3B: microtubule associated protein 1 light chain 3 beta; mCh: mCherry; MIM: mitochondrial inner membrane; MOM: mitochondrial outer membrane; N starvation: nitrogen starvation; N terminus: amino terminus; PARL: presenilin associated rhomboid like; Pcp1: processing of cytochrome c peroxidase 1; PCR: polymerase chain reaction; PGAM5: PGAM family member 5 mitochondrial serine/threonine protein phosphatase; PHBs/Phb: prohibitins; PINK1: PTEN induced kinase 1; PMSF: phenylmethylsulfonyl fluoride; PRKN: parkin RBR E3 ubiquitin protein ligase; SD: synthetic defined medium; SDS: sodium dodecyl sulfate; SMD-N: synthetic defined medium lacking nitrogen; WB: western blot; WT: wild type; Yme1: yeast mitochondrial escape 1; YPD: yeast extract-peptone-dextrose medium; YPLac: yeast extract-peptone-lactate medium.","doi":"10.1080/15548627.2024.2371717","authors":"García-Chávez D, Domínguez-Martín E, Kawasaki L, Ongay-Larios L, Ruelas-Ramírez H, Mendoza-Martinez AE, Pardo JP, Funes S, Coria R","authors_abbrev":"García-Chávez D et al.","pubmed_publication_date":"04 Jul 2024","pubmed_entrez_date":"2024-07-04","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1322.16","SPBP8B7.24c","SPAC1782.06c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:18713859","title":"Stochastic hybrid modeling of DNA replication across a complete genome.","citation":"Proc Natl Acad Sci U S A 2008 Aug 26;105(34):12295-300","abstract":"DNA replication in eukaryotic cells initiates from hundreds of origins along their genomes, leading to complete duplication of genetic information before cell division. The large number of potential origins, coupled with system uncertainty, dictates the need for new analytical tools to capture spatial and temporal patterns of DNA replication genome-wide. We have developed a stochastic hybrid model that reproduces DNA replication throughout a complete genome. The model can capture different modes of DNA replication and is applicable to various organisms. Using genome-wide data on the location and firing efficiencies of origins in the fission yeast, we show how the DNA replication process evolves during S-phase in the presence of stochastic origin firing. Simulations reveal small regions of the genome that extend S-phase to three times its reported duration. The low levels of late replication predicted by the model are below the detection limit of techniques used to measure S-phase length. Parameter sensitivity analysis shows that increased replication fork speeds genome-wide, or additional origins are not sufficient to reduce S-phase to its reported length. We model the redistribution of a limiting initiation factor during S-phase and show that it could shorten S-phase to the reported duration. Alternatively, S-phase may be extended, and what has traditionally been defined as G2 may be occupied by low levels of DNA synthesis with the onset of mitosis delayed by activation of the G2/M checkpoint.","doi":"10.1073/pnas.0805549105","authors":"Lygeros J, Koutroumpas K, Dimopoulos S, Legouras I, Kouretas P, Heichinger C, Nurse P, Lygerou Z","authors_abbrev":"Lygeros J et al.","pubmed_publication_date":"26 Aug 2008","pubmed_entrez_date":"2008-08-21","publication_year":"2008","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1899230","title":"Fission yeast genes that confer resistance to staurosporine encode an AP-1-like transcription factor and a protein kinase related to the mammalian ERK1/MAP2 and budding yeast FUS3 and KSS1 kinases.","citation":"Genes Dev 1991 Jan;5(1):60-73","abstract":"Staurosporine, a potent inhibitor of protein kinase C, arrests fission yeast cell elongation specifically at a stage immediately after cell division. We isolated two genes, which, when carried on multicopy plasmids, confer drug resistance in fission yeast. One, spk1+, encodes a protein kinase highly similar (54% identity) to those encoded by the mammalian ERK1/MAP2 kinase and the budding yeast KSS1 and FUS3 genes. It is not essential for vegetative growth of Schizosaccharomyces pombe cells but is required for conjugation. The spk1+ gene product is a 45-kD protein enriched in the nucleus, and its level increases 10-fold after addition of staurosporine. The other gene pap1+ encodes an AP-1-like transcription factor that contains a region rich in basic amino acids followed by a \"leucine zipper\" motif. The pap1+ gene is required for spk1(+)-conferred staurosporine resistance. These two genes appear to function as a part of the fission yeast growth control pathway.","authors":"Toda T, Shimanuki M, Yanagida M","authors_abbrev":"Toda T et al.","pubmed_publication_date":"Jan 1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_session_key":"b047e0c4a7554079","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-08-22 19:06:03","canto_approved_date":"2022-11-07 11:39:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-10 23:10:02","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.09c","SPAC1783.07c","SPBC12D12.04c","SPBC11B10.09","SPCC16C4.09","SPAC20G4.07c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-08-22"},{"uniquename":"PMID:8898363","title":"Characterization of novel mutations at the Schizosaccharomyces pombe cdc2 regulatory phosphorylation site, tyrosine 15.","citation":"Mol Biol Cell 1996 Oct;7(10):1573-86","abstract":"The cdc2 protein kinase family is regulated negatively by phosphorylation in the glycine ATP-binding loop at a conserved tyrosine residue, Y15, alone or in combination with T14 phosphorylation. In Schizosaccharomyces pombe and other systems, substitution of these residues with structurally similar but nonphosphorylatable amino acids has generated proteins (Y15F or T14AY15F) that behave as constitutively tyrosine-dephosphorylated proteins or threonine and tyrosine-dephosphorylated proteins. Here we report the characteristics of three additional mutants at Y15--Y15E, Y15S, and Y15T--in S. pombe cdc2p. All three mutant proteins are active in in vitro kinase assays, but are unable to functionally complement cdc2 loss-of-function mutations in vivo. Additionally, all three mutants are dominant negatives. A more detailed analysis of the Y15T mutant indicates that it can initiate chromosome condensation and F-actin contractile ring formation, but is unable to drive the reorganization of microtubules into a mitotic spindle.","authors":"Gould KL, Feoktistova A","authors_abbrev":"Gould KL et al.","pubmed_publication_date":"Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:363733","title":"Carbon dioxide evolution during the cell cycle of the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1978 Oct;33:385-97","abstract":"The rate of CO2 evolution was measured in synchronous cultures of the fission yeast Schizosaccharomyces pombe growing in a minimal medium. The rate of CO2 evolution was found to double sharply at about the time of nuclear division (0.75 of the way through the cell cycle). For the remainder of the cell cycle the rate remained constant. Addition of inhibitors of DNA synthesis or nuclear division did not affect the pattern of CO2 evolution in synchronous cultures. Similarly, in an induced synchronous culture, in which DNA synthesis, nuclear division and cell division--but not growth, were synchronized, CO2 evolution showed a continuous pattern and not the step-wise increase associated with the normal synchronous cultures. When S. pombe was grown in a complete medium, the evolution of CO2 in a synchronous cultures was shown to increase in a continuous manner but at a rate faster than the growth of the culture.","authors":"Creanor J","authors_abbrev":"Creanor J","pubmed_publication_date":"Oct 1978","pubmed_entrez_date":"1978-10-01","publication_year":"1978","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15371542","title":"The fission yeast kinetochore component Spc7 associates with the EB1 family member Mal3 and is required for kinetochore-spindle association.","citation":"Mol Biol Cell 2004 Dec;15(12):5255-67","abstract":"A critical aspect of mitosis is the interaction of the kinetochore with spindle microtubules. Fission yeast Mal3 is a member of the EB1 family of microtubule plus-end binding proteins, which have been implicated in this process. However, the Mal3 interaction partner at the kinetochore had not been identified. Here, we show that the mal3 mutant phenotype can be suppressed by the presence of extra Spc7, an essential kinetochore protein associated with the central centromere region. Mal3 and Spc7 interact physically as both proteins can be coimmunoprecipitated. Overexpression of a Spc7 variant severely compromises kinetochore-microtubule interaction, indicating that the Spc7 protein plays a role in this process. Spc7 function seems to be conserved because, Spc105, a Saccharomyces cerevisiae homolog of Spc7, identified by mass spectrometry as a component of the conserved Ndc80 complex, can rescue mal3 mutant strains.","authors":"Kerres A, Vietmeier-Decker C, Ortiz J, Karig I, Beuter C, Hegemann J, Lechner J, Fleig U","authors_abbrev":"Kerres A et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-09-17","publication_year":"2004","canto_session_key":"b68179e7a7d13aff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-06-29 04:42:38","canto_approved_date":"2022-02-03 20:13:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-28 09:02:23","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.08","SPAC27F1.04c","SPCC188.04c","SPBC11C11.03","SPAC18G6.15","SPCC1020.02","SPBC1289.03c","SPBC26H8.07c","SPCC895.07","SPAC25B8.14"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2017-06-29"},{"uniquename":"PMID:10436019","title":"Vacuole fusion regulated by protein phosphatase 2C in fission yeast.","citation":"Mol Biol Cell 1999 Aug;10(8):2647-54","abstract":"The gene ptc4+ encodes one of four type 2C protein phosphatases (PP2C) in the fission yeast Schizosaccharomyces pombe. Deletion of ptc4+ is not lethal; however, Deltaptc4 cells grow slowly in defined minimal medium and undergo premature growth arrest in response to nitrogen starvation. Interestingly, Deltaptc4 cells are unable to fuse vacuoles in response to hypotonic stress or nutrient starvation. Conversely, Ptc4 overexpression appears to induce vacuole fusion. These findings reveal a hitherto unrecognized function of type 2C protein phosphatases: regulation of vacuole fusion. Ptc4 localizes in vacuole membranes, which suggests that Ptc4 regulates vacuole fusion by dephosphorylation of one or more proteins in the vacuole membrane. Vacuole function is required for the process of autophagy that is induced by nutrient starvation; thus, the vacuole defect of Deltaptc4 cells might explain why these cells undergo premature growth arrest in response to nitrogen starvation.","authors":"Gaits F, Russell P","authors_abbrev":"Gaits F et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-08-06","publication_year":"1999","canto_session_key":"ab4cda039a50feae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-03 14:47:23","canto_approved_date":"2020-11-13 17:03:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-12 12:55:41","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-03"},{"uniquename":"PMID:9070843","title":"Detection of DNA bending in a DNA-PAP1 protein complex by fluorescence resonance energy transfer.","citation":"Biochem Biophys Res Commun 1997 Feb 24;231(3):553-6","abstract":"The structure of DNA in a DNA-protein complex was studied by means of fluorescence resonance energy transfer (FRET) method. Oligonucleotide phosphorothioates were labeled with fluorescein and eosin to obtain a donor- and acceptor-labeled DNA. The formation of a complex of the DNA with PAP1(70), which is a DNA binding site fragment derived from transcription regulatory protein, PAP1, of fission yeast, was confirmed by gel retardation analysis and fluorescence measurements. FRET of the donor- and acceptor-labeled DNA with and without PAP1(70) indicated that the DNA in the complex was bent about 26 degrees toward the protein-binding surface.","authors":"Ozaki H, Iwase N, Sawai H, Kodama T, Kyogoku Y","authors_abbrev":"Ozaki H et al.","pubmed_publication_date":"24 Feb 1997","pubmed_entrez_date":"1997-02-24","publication_year":"1997","canto_session_key":"6e173c4c2e24fbf5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-29 12:03:57","canto_approved_date":"2019-11-29 12:03:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-29 12:03:51","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-29"},{"uniquename":"PMID:10514568","title":"Replicative ageing in the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 1999 Oct;15(14):1511-8","abstract":"Saccharomyces cerevisiae has been widely used as a model organism in studies of replicative ageing and senescence. The relevance of these studies to ageing in other organisms has, however, been questioned, since this yeast divides by budding rather than fission, the more common pattern in higher organisms. Here we report that, contrary to popular belief, the fission yeast Schizosaccharomyces pombe also undergoes replicative senescence and in a manner superficially analogous to budding yeast. These experiments provide the first evidence of age asymmetry in cell fission and are consistent with the hypothesis of Jazwinski, that asymmetric division underlies culture immortality. Given their evolutionary divergence, comparison of the ageing determinants in fission and budding yeasts may help identify common mechanisms of the ageing process.","authors":"Barker MG, Walmsley RM","authors_abbrev":"Barker MG et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-10-09","publication_year":"1999","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39580958","title":"Novel pof1 mutation suppresses the sensitivity to DNA replication inhibitor in fission yeast RecQ helicase mutant.","citation":"Biochem Biophys Res Commun 2024 Nov 20;741:151014","abstract":"Homologous recombination is vital for DNA double-strand break repair. Dysfunction in homologous recombination can lead to cell death, mutations, and cancer. In fission yeast (Schizosaccharomyces pombe), RecQ helicase Rqh1 resolves recombination intermediates. We found that rqh1-hd strain impaired growth in media containing hydroxyurea and thiabendazole. Using this condition, we identified a novel pof1 mutation (pof1-A81T) that suppress the poor growth of the rqh1-hd strain on the plate containing hydroxyurea and thiabendazole. Compared to rqh1-hd, rqh1-hd pof1-A81T cells displayed reduced Replication Protein A foci on chromosome bridges after hydroxyurea treatment. This suggests that pof1-A81T mutation suppresses the accumulation of recombination intermediates in hydroxyurea-treated rqh1-hd cells. Additionally, pof1-A81T mutation rescued the segregation defect of nucleolar protein Gar2 observed in hydroxyurea-treated rqh1-hd cells, potentially by mitigating recombination intermediate accumulation in rDNA. These results suggest that the pof1-A81T mutation suppresses the accumulation of recombination intermediates, particularly in rDNA, and alleviates the rqh1 deficiency phenotype in S. pombe.","doi":"10.1016/j.bbrc.2024.151014","authors":"Tang J, Nakamura M, Ng WY, Feng N, Ueno M","authors_abbrev":"Tang J et al.","pubmed_publication_date":"20 Nov 2024","pubmed_entrez_date":"2024-11-24","publication_year":"2024","canto_session_key":"6dabfec38357f1d6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-11-26 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A10.05c","SPAC2G11.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:21110984","title":"The role of MutY homolog (Myh1) in controlling the histone deacetylase Hst4 in the fission yeast Schizosaccharomyces pombe.","citation":"J Mol Biol 2011 Jan 21;405(3):653-65","abstract":"The DNA glycosylase MutY homolog (Myh1) excises adenines misincorporated opposite guanines or 7,8-dihydro-8-oxo-guanines on DNA by base excision repair thereby preventing G:C to T:A mutations. Schizosaccharomyces pombe (Sp) Hst4 is an NAD(+)-dependent histone/protein deacetylase involved in gene silencing and maintaining genomic integrity. Hst4 regulates deacetylation of histone 3 Lys56 at the entry and exit points of the nucleosome core particle. Here, we demonstrate that the hst4 mutant is more sensitive to H(2)O(2) than wild-type cells. H(2)O(2) treatment results in an SpMyh1-dependent decrease in SpHst4 protein level and hyperacetylation of histone 3 Lys56. Furthermore, SpHst4 interacts with SpMyh1 and the cell cycle checkpoint Rad9-Rad1-Hus1 (9-1-1) complex. SpHst4, SpMyh1, and SpHus1 are physically bound to telomeres. Following oxidative stress, there is an increase in the telomeric association of SpMyh1. Conversely, the telomeric association of spHst4 is decreased. Deletion of SpMyh1 strongly abrogated telomeric association of SpHst4 and SpHus1. However, telomeric association of SpMyh1 is enhanced in hst4Δ cells in the presence of chronic DNA damage. These results suggest that SpMyh1 repair regulates the functions of SpHst4 and the 9-1-1 complex in maintaining genomic stability.","doi":"10.1016/j.jmb.2010.11.037","authors":"Chang DY, Shi G, Durand-Dubief M, Ekwall K, Lu AL","authors_abbrev":"Chang DY et al.","pubmed_publication_date":"21 Jan 2011","pubmed_entrez_date":"2010-11-30","publication_year":"2011","canto_session_key":"b9a72545ffa319cd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.02","SPAC1783.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:41580672","title":"HDGS-Net: nucleosome occupancy prediction based on a hybrid dilated gated separable convolutional neural network.","citation":"BMC Genomics 2026 Jan 24;27(1):209","abstract":"Nucleosome positioning plays a central role in chromatin organization and gene regulation, yet its accurate computational prediction remains challenging. This study introduces a Hybrid Dilated Gated Separable Convolutional Neural Network (HDGS-Net), which integrates dilated convolution, gated convolution, and depthwise separable convolution to achieve continuous prediction of in vitro nucleosome occupancy at single-base resolution across the entire Saccharomyces cerevisiae genome. On benchmark datasets, HDGS-Net attained an average Pearson correlation coefficient of 0.87, outperforming conventional methods and demonstrating excellent cross-chromosome generalization capability. Sequence analysis confirms that DNA dinucleotide physical properties dominate nucleosome positioning, with AT-rich sequences inhibiting binding and GC-rich sequences promoting binding. Analysis of transcription start regions verifies that flanking nucleosome sequence features are highly conserved across different chromatin environments, supporting the universal regulatory role of sequence preference. Cross-species analysis demonstrates that the guiding efficacy of DNA sequence on nucleosome positioning varies among species, showing quantitatively decreasing contributions in Caenorhabditis elegans, Saccharomyces cerevisiae, and Schizosaccharomyces pombe. This study provides a high-accuracy predictive tool for investigating dynamic nucleosome positioning.\nThe online version contains supplementary material available at 10.1186/s12864-026-12523-2.","doi":"10.1186/s12864-026-12523-2","authors":"Shi F, Wang M, Teng Z, Cai L, Liu G, Xing Y, Cui X, Liu G, Yang Z, Meng H","authors_abbrev":"Shi F et al.","pubmed_publication_date":"24 Jan 2026","pubmed_entrez_date":"2026-01-24","publication_year":"2026","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2026-02-19 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16273369","title":"Moc3, a novel Zn finger type protein involved in sexual development, ascus formation, and stress response of Schizosaccharomyces pombe.","citation":"Curr Genet 2005 Dec;48(6):345-55","abstract":"The cAMP pathway in Schizosaccharomyces pombe is the major nutrient sensing pathway to initiate sexual development when opposite mating type cells exist. We identified moc1-moc4 as genes that overcome a partially sterile S. pombe strain due to an elevation of cAMP. When we compared the strength of inducing ability of sexual development in the same S. pombe strain, Moc1 had highest, Moc2 had lowest, and both Moc3 and Moc4 had intermediate effects. Moc1/Sds23 and Moc2/Ded1 are known to be a potential regulator of M-phase progression and an essential RNA helicase, respectively. While Moc4 was found to be identical with a Zn-finger protein Zfs1, Moc3 (SPAC821.07c) was a novel protein containing a Zn-finger (Zn(2)-Cys(6)) motif. Deletion mutant of the moc3 gene was constructed and its disruptant was found to be lower in mating efficiency and formed aberrant asci. In addition, unexpectedly, a moc3 disruptant was sensitive to CaCl(2) and DNA damaging agents such as MMS and UV. Those phenotypes were opposite to the phenotypes observed in a zfs1 disruptant, and quite different from the ones in a moc1 disruptant. Moc3 localized in the nucleus as observed for Zfs1. Moc3 bound with Moc4/Zfs1 weakly in the two hybrid system, but no other combination of Moc(s) bound each other in the same analysis. Thus, Moc3 is not only involved in sexual development, but also in ascus formation and DNA integrity in an independent manner with Moc1 and Moc2 in S. pombe.","authors":"Goldar MM, Jeong HT, Tanaka K, Matsuda H, Kawamukai M","authors_abbrev":"Goldar MM et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-11-08","publication_year":"2005","canto_session_key":"31a8468e085bee29","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-02 11:07:49","canto_approved_date":"2022-02-02 16:56:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-29 11:24:27","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPBC1D7.05","SPAC17H9.09c","SPCC1795.11","SPBC646.13","SPAC821.07c","SPBC1718.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-02-02"},{"uniquename":"PMID:1944283","title":"Mutations at sites involved in Suc1 binding inactivate Cdc2.","citation":"Mol Cell Biol 1991 Dec;11(12):6177-84","abstract":"suc1+ encodes an essential cell cycle regulator of the fission yeast Schizosaccharomyces pombe. Its product, a 13-kDa protein, interacts with the Cdc2 protein kinase. Both positive and negative effects on cell cycle progression have been attributed to Suc1. To date, the exact mechanisms and the physiological role of the interaction between Suc1 and Cdc2 remain unclear. Here we have studied the molecular basis of this association. We show that Cdc2 can bind Suc1 or its mammalian homolog directly in the absence of any additional protein component. Using an alanine scanning mutagenesis method, we analyzed the interaction between Cdc2 and Suc1. We show that the integrity of several domains on the Cdc2 protein, including sites directly involved in catalytic activity, is required for binding to Suc1. Furthermore, Cdc2 mutant proteins unable to bind Suc1 (but able to bind cyclins) are nonfunctional when overexpressed in S. pombe, indicating that a specific interaction with Suc1 is required for Cdc2 function.","authors":"Ducommun B, Brambilla P, Draetta G","authors_abbrev":"Ducommun B et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"87ea97c9517f37fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-02-21 12:26:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-02-21 12:25:54","canto_added_date":"2012-02-24 05:55:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1734.14c","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2013-02-21"},{"uniquename":"PMID:12663528","title":"Nonrandom homolog segregation at meiosis I in Schizosaccharomyces pombe mutants lacking recombination.","citation":"Genetics 2003 Mar;163(3):857-74","abstract":"Physical connection between homologous chromosomes is normally required for their proper segregation to opposite poles at the first meiotic division (MI). This connection is generally provided by the combination of reciprocal recombination and sister-chromatid cohesion. In the absence of meiotic recombination, homologs are predicted to segregate randomly at MI. Here we demonstrate that in rec12 mutants of the fission yeast Schizosaccharomyces pombe, which are devoid of meiosis-induced recombination, homologs segregate to opposite poles at MI 63% of the time. Residual, Rec12-independent recombination appears insufficient to account for the observed nonrandom homolog segregation. Dyad asci are frequently produced by rec12 mutants. More than half of these dyad asci contain two viable homozygous-diploid spores, the products of a single reductional division. This set of phenotypes is shared by other S. pombe mutants that lack meiotic recombination, suggesting that nonrandom MI segregation and dyad formation are a general feature of meiosis in the absence of recombination and are not peculiar to rec12 mutants. Rec8, a meiosis-specific sister-chromatid cohesin, is required for the segregation phenotypes displayed by rec12 mutants. We propose that S. pombe possesses a system independent of recombination that promotes homolog segregation and discuss possible mechanisms.","authors":"Davis L, Smith GR","authors_abbrev":"Davis L et al.","pubmed_publication_date":"Mar 2003","pubmed_entrez_date":"2003-03-29","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23457617","title":"Haploinsufficiency of the Sec7 guanine nucleotide exchange factor gea1 impairs septation in fission yeast.","citation":"PLoS One 2013;8(2):e56807","abstract":"Membrane trafficking is essential to eukaryotic life and is controlled by a complex network of proteins that regulate movement of proteins and lipids between organelles. The GBF1/GEA family of Guanine nucleotide Exchange Factors (GEFs) regulates trafficking between the endoplasmic reticulum and Golgi by catalyzing the exchange of GDP for GTP on ADP Ribosylation Factors (Arfs). Activated Arfs recruit coat protein complex 1 (COP-I) to form vesicles that ferry cargo between these organelles. To further explore the function of the GBF1/GEA family, we have characterized a fission yeast mutant lacking one copy of the essential gene gea1 (gea1+/-), the Schizosaccharomyces pombe ortholog of GBF1. The haploinsufficient gea1+/- strain was shown to be sensitive to the GBF1 inhibitor brefeldin A (BFA) and was rescued from BFA sensitivity by gea1p overexpression. No overt defects in localization of arf1p or arf6p were observed in gea1+/- cells, but the fission yeast homolog of the COP-I cargo sac1 was mislocalized, consistent with impaired COP-I trafficking. Although Golgi morphology appeared normal, a slight increase in vacuolar size was observed in the gea1+/- mutant strain. Importantly, gea1+/- cells exhibited dramatic cytokinesis-related defects, including disorganized contractile rings, an increased septation index, and alterations in septum morphology. Septation defects appear to result from altered secretion of enzymes required for septum dynamics, as decreased secretion of eng1p, a β-glucanase required for septum breakdown, was observed in gea1+/- cells, and overexpression of eng1p suppressed the increased septation phenotype. These observations implicate gea1 in regulation of septum breakdown and establish S. pombe as a model system to explore GBF1/GEA function in cytokinesis.","doi":"10.1371/journal.pone.0056807","authors":"Eckler AM, Wilder C, Castanon A, Ferris VM, Lamere RA, Perrin BA, Pearlman R, White B, Byrd C, Ludvik N, Nichols N, Poole-Sumrall K, Sztul E, Styers ML","authors_abbrev":"Eckler AM et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-03-05","publication_year":"2013","canto_session_key":"fa30fa9e2e0880e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Melanie Styers","canto_first_approved_date":"2013-09-27 16:43:33","canto_approved_date":"2021-12-29 18:56:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-27 07:34:03","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Melanie Styers","community_curator":true,"annotation_count":33,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1539.08","SPBC4F6.18c","SPBC19F5.03","SPAC821.09","SPBC211.03c","SPAC3C7.01c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2013-09-27"},{"uniquename":"PMID:28472520","title":"A synergistic network of interactions promotes the formation of in vitro processing bodies and protects mRNA against decapping.","citation":"Nucleic Acids Res 2017 Jun 20;45(11):6911-6922","abstract":"Cellular liquid-liquid phase separation (LLPS) results in the formation of dynamic granules that play an important role in many biological processes. On a molecular level, the clustering of proteins into a confined space results from an indefinite network of intermolecular interactions. Here, we introduce and exploit a novel high-throughput bottom-up approach to study how the interactions between RNA, the Dcp1:Dcp2 mRNA decapping complex and the scaffolding proteins Edc3 and Pdc1 result in the formation of processing bodies. We find that the LLPS boundaries are close to physiological concentrations upon inclusion of multiple proteins and RNA. Within in vitro processing bodies the RNA is protected against endonucleolytic cleavage and the mRNA decapping activity is reduced, which argues for a role of processing bodies in temporary mRNA storage. Interestingly, the intrinsically disordered region (IDR) in the Edc3 protein emerges as a central hub for interactions with both RNA and mRNA decapping factors. In addition, the Edc3 IDR plays a role in the formation of irreversible protein aggregates that are potentially detrimental for cellular homeostasis. In summary, our data reveal insights into the mechanisms that lead to cellular LLPS and into the way this influences enzymatic activity.","doi":"10.1093/nar/gkx353","authors":"Schütz S, Nöldeke ER, Sprangers R","authors_abbrev":"Schütz S et al.","pubmed_publication_date":"20 Jun 2017","pubmed_entrez_date":"2017-05-05","publication_year":"2017","canto_session_key":"9c1e9f06ffd9e9c6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-11-09 01:15:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19A8.12","SPBC3B9.21"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:24186301","title":"Genetic and functional analysis of the complex locus ade10 in Schizosaccharomyces pombe.","citation":"Curr Genet 1982 Aug;5(3):233-44","abstract":"The complex locus ade10 of Schizosaccharomyces pombe was subjected to genetical fine structure analysis and characterized for enzymatic activities. Out of twenty alleles isolated, fifteen were found to complement and to be localized in two adjacent regions. Complementing alleles mapping in region I lack AICAR-formyltransferase activity while complementing alleles mapping in region II lack IMP-cyclohydrolase activity. In both cases, the remaining activity was generally normal. Three of these alleles were identified as missense and one as nonsense. Interallelic complementation was found to occur inside each region. The five other alleles are completely pleiotropic, suggesting that the two regions belong to a single transcription unit. These alleles are distributed over both regions. Two of them appear to be frameshift. The genetic map shows the occurrence of map expansion.","doi":"10.1007/BF00391812","authors":"Richter R, Heslot H","authors_abbrev":"Richter R et al.","pubmed_publication_date":"Aug 1982","pubmed_entrez_date":"2013-11-05","publication_year":"1982","canto_session_key":"5918a303b131ae03","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-05-26 17:02:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-17 16:07:29","canto_added_date":"2014-02-16 06:09:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCPB16A4.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-17"},{"uniquename":"PMID:1128539","title":"Mutation and nuclear stage in Schizosaccharomyces pombe. I. An experimental approach to the role of recombination in mutation induction.","citation":"Mutat Res 1975 Feb;27(2):225-33","abstract":"A reverse mutation system using G1 and G2 cells of Schizosaccharomyces pombe is described. In order to enable the system to deal with the problem of mutation dependence on recombination, tests were performed on (i) the homogeneity of cell populations with respect to nuclear stage;(ii) the fate of cells during post-irradiation incubation;(iii) the colony-forming ability of G1 and G2 revertants, and (iv) cell viability on the mutation plates. On the basis of the results, it is thought that, using this system, information can be obtained on the role of recombinational events in the process of mutation induction.","authors":"Abbondandolo A","authors_abbrev":"Abbondandolo A","pubmed_publication_date":"Feb 1975","pubmed_entrez_date":"1975-02-01","publication_year":"1975","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1314171","title":"Gene amplification at a locus encoding a putative Na+/H+ antiporter confers sodium and lithium tolerance in fission yeast.","citation":"EMBO J 1992 Apr;11(4):1631-40","abstract":"We have identified a new locus, sodium 2 (sod2) based on selection for increased LiCl tolerance in fission yeast, Schizosaccharomyces pombe. Tolerant strains have enhanced pH-dependent Na+ export capacity and sodium transport experiments suggest that the gene encodes an Na+/H+ antiport. The predicted sod2 gene product can be placed in the broad class of transporters which possess 12 hydrophobic transmembrane domains. The protein shows some sequence similarity to the human and bacterial Na+/H+ antiporters. Overexpression of sod2 increased Na+ export capacity and conferred sodium tolerance. Osmotolerance was not affected and sod2 cells were unaffected for growth in K+. In a sod2 disruption strain cells were incapable of exporting sodium. They were hypersensitive to Na+ or Li+ and could not grow under conditions that approximate pH7. The sod2 gene amplification could be selected stepwise and the degree of such amplification correlated with the level of Na+ or Li+ tolerance.","authors":"Jia ZP, McCullough N, Martel R, Hemmingsen S, Young PG","authors_abbrev":"Jia ZP et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"eb4340d44f575950","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-19 08:37:39","canto_approved_date":"2024-04-08 16:58:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-30 16:09:08","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-19"},{"uniquename":"PMID:40972526","title":"The histone chaperone Spt6 controls chromatin structure through its conserved N-terminal domain.","citation":"Mol Cell 2025 Sep 18;85(18):3407-3424.e8","abstract":"The disassembly and reassembly of nucleosomes by histone chaperones is an essential activity during eukaryotic transcription elongation. This highly conserved process maintains chromatin integrity by transiently removing nucleosomes as barriers and then restoring them in the wake of transcription. While transcription elongation requires multiple histone chaperones, there is little understanding of how most of them function and why so many are required. Here, we show that the histone chaperone Spt6 acts through its acidic, intrinsically disordered N-terminal domain (NTD) to bind histones and control chromatin structure. The Spt6 NTD is essential for viability, and its histone-binding activity is conserved between yeast and humans. The essential nature of the Spt6 NTD can be bypassed by changes in another histone chaperone, FACT, revealing a close functional connection between the two. Our results have led to a mechanistic model for dynamic cooperation between multiple histone chaperones during transcription elongation.","doi":"10.1016/j.molcel.2025.08.020","authors":"Warner JL, Lux V, Veverka V, Winston F","authors_abbrev":"Warner JL et al.","pubmed_publication_date":"18 Sep 2025","pubmed_entrez_date":"2025-09-19","publication_year":"2025","canto_session_key":"efdfce9005356071","canto_annotation_status":"APPROVED","canto_triage_status":"Wrong organism","canto_curator_role":"PomBase","canto_first_approved_date":"2026-02-06 12:16:00","canto_approved_date":"2026-02-06 12:16:00","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-02-06 12:15:48","canto_added_date":"2025-11-04 19:36:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.01c","SPAC4F10.11","SPAC3C7.08c"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2026-02-06"},{"uniquename":"PMID:27458047","title":"ICRF-193, an anticancer topoisomerase II inhibitor, induces arched telophase spindles that snap, leading to a ploidy increase in fission yeast.","citation":"Genes Cells 2016 Sep;21(9):978-93","abstract":"ICRF-193 [meso-4,4-(2,3-butanediyl)-bis(2,6-piperazinedione)] is a complex-stabilizing inhibitor of DNA topoisomerase II (topo II) that is used as an effective anticancer drug. ICRF-193 inhibits topo II catalytic activity in vitro and blocks nuclear division in vivo. Here, we examined the effects of ICRF-193 treatment on chromatin behavior and spindle dynamics using detailed live mitotic cell analysis in the fission yeast, Schizosaccharomyces pombe. Time-lapse movie analysis showed that ICRF-193 treatment leads to an elongation of presumed chromatin fibers connected to kinetochores during mid-mitosis. Anaphase spindles begin to arch, and eventually spindle poles come together abruptly, as if the spindle snapped at the point of spindle microtubule overlap in telophase. Segregating chromosomes appeared as elastic clumps and subsequently pulled back and merged. The snapped spindle phenotype was abolished by microtubule destabilization after thiabendazole treatment, accompanied by unequal chromosome segregation or severe defects in spindle extension. Thus, we conclude that ICRF-193-treated, unseparated sister chromatids pulling toward opposite spindle poles produce the arched and snapped telophase spindle. ICRF-193 treatment increased DNA content, suggesting that the failure of sister chromatids to separate properly in anaphase, causes the spindle to break in telophase, resulting in polyploidization.","doi":"10.1111/gtc.12397","authors":"Nakazawa N, Mehrotra R, Arakawa O, Yanagida M","authors_abbrev":"Nakazawa N et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-07-27","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-07-28 11:58:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD124","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16199881","title":"Natural meiotic recombination hot spots in the Schizosaccharomyces pombe genome successfully predicted from the simple sequence motif M26.","citation":"Mol Cell Biol 2005 Oct;25(20):9054-62","abstract":"The M26 hot spot of meiotic recombination in Schizosaccharomyces pombe is the eukaryotic hot spot most thoroughly investigated at the nucleotide level. The minimum sequence required for M26 activity was previously determined to be 5'-ATGACGT-3'. Originally identified by a mutant allele, ade6-M26, the M26 heptamer sequence occurs in the wild-type S. pombe genome approximately 300 times, but it has been unclear whether any of these are active hot spots. Recently, we showed that the M26 heptamer forms part of a larger consensus sequence, which is significantly more active than the heptamer alone. We used this expanded sequence as a guide to identify a smaller number of sites most likely to be active hot spots. Ten of the 15 sites tested showed meiotic DNA breaks, a hallmark of recombination hot spots, within 1 kb of the M26 sequence. Among those 10 sites, one occurred within a gene, cds1(+), and hot spot activity of this site was confirmed genetically. These results are, to our knowledge, the first demonstration in any organism of a simple, defined nucleotide sequence accurately predicting the locations of natural meiotic recombination hot spots. M26 may be the first example among a diverse group of simple sequences that determine the distribution, and hence predictability, of meiotic recombination hot spots in eukaryotic genomes.","authors":"Steiner WW, Smith GR","authors_abbrev":"Steiner WW et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-10-04","publication_year":"2005","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25864229","title":"Mutants of Schizosaccharomyces pombe which sporulate in the haploid state.","citation":"Mol Gen Genet 1985;198(3):416-21","abstract":"Suppressor mutants of mei1–102, a mutation in one of the mating type cassette genes (mat2-P) which blocks the progression into meiosis, were isolated and characterized in Schizosaccharomyces pombe. These suppressor mutations conferred either temperature-sensitivity or cold-sensitivity. The growth of these strains is halted and sporulation initiated at the restrictive temperatures, regardless of other conditions usually required for the initiation of meiosis i.e. they sporulate in the presence of a nitrogen source and mating type homozygosity. Their most striking feature is that they can sporulate from the haploid state. The haploidy of these mutants was confirmed by genetical analysis and by measurement of the DNA content of the cells. The mutants are all recessive and define a single gene pat1. The pat1 gene maps very close to the centromere of chromosome II. A meiosis defective mutation in mei5 can suppress the temperature-sensitivity caused by pat1, indicating some interaction between them. Spores produced from a haploid cell have poor viability and appear to contain only 1/2C DNA on average.","authors":"Lino Y, Yamamoto M","authors_abbrev":"Lino Y et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"2015-04-14","publication_year":"1985","canto_session_key":"28dcc60c23d4c00a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-04-16 00:19:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPBC28F2.07"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:22186733","title":"Programmed fluctuations in sense/antisense transcript ratios drive sexual differentiation in S. pombe.","citation":"Mol Syst Biol 2011 Dec 20;7:559","abstract":"Strand-specific RNA sequencing of S. pombe revealed a highly structured programme of ncRNA expression at over 600 loci. Waves of antisense transcription accompanied sexual differentiation. A substantial proportion of ncRNA arose from mechanisms previously considered to be largely artefactual, including improper 3' termination and bidirectional transcription. Constitutive induction of the entire spk1+, spo4+, dis1+ and spo6+ antisense transcripts from an integrated, ectopic, locus disrupted their respective meiotic functions. This ability of antisense transcripts to disrupt gene function when expressed in trans suggests that cis production at native loci during sexual differentiation may also control gene function. Consistently, insertion of a marker gene adjacent to the dis1+ antisense start site mimicked ectopic antisense expression in reducing the levels of this microtubule regulator and abolishing the microtubule-dependent 'horsetail' stage of meiosis. Antisense production had no impact at any of these loci when the RNA interference (RNAi) machinery was removed. Thus, far from being simply 'genome chatter', this extensive ncRNA landscape constitutes a fundamental component in the controls that drive the complex programme of sexual differentiation in S. pombe.","doi":"10.1038/msb.2011.90","authors":"Bitton DA, Grallert A, Scutt PJ, Yates T, Li Y, Bradford JR, Hey Y, Pepper SD, Hagan IM, Miller CJ","authors_abbrev":"Bitton DA et al.","pubmed_publication_date":"20 Dec 2011","pubmed_entrez_date":"2011-12-22","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28160081","title":"Ecl1 is a zinc-binding protein involved in the zinc-limitation-dependent extension of chronological life span in fission yeast.","citation":"Mol Genet Genomics 2017 Apr;292(2):475-481","abstract":"Overexpression of Ecl1-family genes (ecl1  + , ecl2  + , and ecl3  + ) results in the extension of the chronological life span in Schizosaccharomyces pombe. However, the mechanism for this extension has not been defined clearly. Ecl1-family proteins consist of approximately 80 amino acids, and four cysteine residues are conserved in their N-terminal domains. This study focused on the Ecl1 protein, mutating its cysteine residues sequentially to confirm their importance. As a result, all mutated Ecl1 proteins nearly lost the function to extend the chronological life span, suggesting that these four cysteine residues are essential for the Ecl1 protein. Utilizing ICP-AES (inductively coupled plasma atomic emission spectroscopy) analysis, we found that wild-type Ecl1 proteins contain zinc, while cysteine-mutated Ecl1 proteins do not. We also analyzed the effect of environmental zinc on the chronological life span. We found that zinc limitation extends the chronological life span, and this extension depends on the Ecl1-family proteins.","doi":"10.1007/s00438-016-1285-x","authors":"Shimasaki T, Ohtsuka H, Naito C, Azuma K, Tenno T, Hiroaki H, Murakami H, Aiba H","authors_abbrev":"Shimasaki T et al.","pubmed_publication_date":"Apr 2017","pubmed_entrez_date":"2017-02-05","publication_year":"2017","canto_session_key":"cb56c06e21e64b64","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_first_approved_date":"2018-01-26 16:25:29","canto_approved_date":"2019-10-24 08:50:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-14 22:30:17","canto_added_date":"2017-02-07 01:15:11","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC70.12c","SPBP35G2.16c","SPBC8E4.12c","SPBC16D10.06"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-01-26"},{"uniquename":"PMID:16041152","title":"Functional conservation between fission yeast moc1/sds23 and its two orthologs, budding yeast SDS23 and SDS24, and phenotypic differences in their disruptants.","citation":"Biosci Biotechnol Biochem 2005 Jul;69(7):1422-6","abstract":"The moc1/sds23 gene was isolated to induce sexual development of a sterile strain due to overexpression of adenylate cyclase in Schizosaccharomyces pombe. Here, we studied the functional conservation between moc1/sds23 and its two orthologs SDS23 and SDS24 in Saccharomyces cerevisiae. We observed that the temperature sensitivity, salt tolerance, cell morphology, and sterility of the Deltamoc1 mutant in S. pombe were recovered by expressing either S. cerevisiae SDS23 or SDS24. We found that deletion of both SDS23 and SDS24 resulted in the production of a large vacuole that was reversed by the expression of S. pombe moc1/sds23. In these ways we found that S. pombe Moc1/Sds23 and S. cerevisiae SDS23p or SDS24p are functional homologs. In addition we found that the Deltasds23 Deltasds24 diploid strain reduces cell separation in forming pseudohyphal-like growth in S. cerevisiae. Thus S. pombe moc1/sds23 and S. cerevisiae SDS23 or SDS24 are interchangeable with each other, but their disruptants are phenotypically dissimilar.","authors":"Goldar MM, Nishie T, Ishikura Y, Fukuda T, Takegawa K, Kawamukai M","authors_abbrev":"Goldar MM et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-07-26","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC646.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9209031","title":"Vacuolar protein sorting in fission yeast: cloning, biosynthesis, transport, and processing of carboxypeptidase Y from Schizosaccharomyces pombe.","citation":"J Bacteriol 1997 Jul;179(13):4179-89","abstract":"PCR was used to isolate a carboxypeptidase Y (CPY) homolog gene from the fission yeast Schizosaccharomyces pombe. The cloned S. pombe cpy1+ gene has a single open reading frame, which encodes 950 amino acids with one potential N-glycosylation site. It appears to be synthesized as an inactive pre-pro protein that likely undergoes processing following translocation into appropriate intracellular organelles. The C-terminal mature region is highly conserved in other serine carboxypeptidases. In contrast, the N-terminal pro region containing the vacuolar sorting signal in CPY from Saccharomyces cerevisiae shows fewer identical residues. The pro region contains two unusual repeating sequences; repeating sequence I consists of seven contiguous repeating segments of 13 amino acids each, and repeating sequence II consists of seven contiguous repeating segments of 9 amino acids each. Pulse-chase radiolabeling analysis revealed that Cpy1p was initially synthesized in a 110-kDa pro-precursor form and via the 51-kDa single-polypeptide-chain intermediate form which has had its pro segment removed is finally converted to a heterodimer, the mature form, which is detected as a 32-kDa protein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions. Like S. cerevisiae CPY, S. pombe Cpy1p does not require the N-linked oligosaccharide moiety for vacuolar delivery. To investigate the vacuolar sorting signal of S. pombe Cpy1p, we have constructed cpy1+-SUC2 gene fusions that direct the synthesis of hybrid proteins consisting of N-terminal segments of various lengths of S. pombe Cpy1p fused to the secreted enzyme S. cerevisiae invertase. The N-terminal 478 amino acids of Cpy1 are sufficient to direct delivery of a Cpy1-Inv hybrid protein to the vacuole. These results showed that the pro peptide of Cpy1 contains the putative vacuolar sorting signal.","authors":"Tabuchi M, Iwaihara O, Ohtani Y, Ohuchi N, Sakurai J, Morita T, Iwahara S, Takegawa K","authors_abbrev":"Tabuchi M et al.","pubmed_publication_date":"Jul 1997","pubmed_entrez_date":"1997-07-01","publication_year":"1997","canto_session_key":"7ebeb88afdef3218","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-10-10 19:54:54","canto_approved_date":"2018-10-10 19:54:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-10 19:54:46","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC458.05","SPAC19G12.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-10-10"},{"uniquename":"PMID:19942139","title":"Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly.","citation":"Chem Biol 2009 Nov 25;16(11):1158-68","abstract":"Formins stimulate actin filament assembly for fundamental cellular processes including division, adhesion, establishing polarity, and motility. A formin inhibitor would be useful because most cells express multiple formins whose functions are not known and because metastatic tumor formation depends on the deregulation of formin-dependent processes. We identified a general small molecule inhibitor of formin homology 2 domains (SMIFH2) by screening compounds for the ability to prevent formin-mediated actin assembly in vitro. SMIFH2 targets formins from evolutionarily diverse organisms including yeast, nematode worm, and mice, with a half-maximal inhibitor concentration of approximately 5 to 15 microM. SMIFH2 prevents both formin nucleation and processive barbed end elongation and decreases formin's affinity for the barbed end. Furthermore, low micromolar concentrations of SMIFH2 disrupt formin-dependent, but not Arp2/3 complex-dependent, actin cytoskeletal structures in fission yeast and mammalian NIH 3T3 fibroblasts.","doi":"10.1016/j.chembiol.2009.10.006","authors":"Rizvi SA, Neidt EM, Cui J, Feiger Z, Skau CT, Gardel ML, Kozmin SA, Kovar DR","authors_abbrev":"Rizvi SA et al.","pubmed_publication_date":"25 Nov 2009","pubmed_entrez_date":"2009-11-28","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16816416","title":"Antagonism of Chk1 signaling in the G2 DNA damage checkpoint by dominant alleles of Cdr1.","citation":"Genetics 2006 Sep;174(1):113-23","abstract":"Activation of the Chk1 protein kinase by DNA damage enforces a checkpoint that maintains Cdc2 in its inactive, tyrosine-15 (Y15) phosphorylated state. Chk1 downregulates the Cdc25 phosphatases and concomitantly upregulates the Wee1 kinases that control the phosphorylation of Cdc2. Overproduction of Chk1 causes G(2) arrest/delay independently of DNA damage and upstream checkpoint genes. We utilized this to screen fission yeast for mutations that alter sensitivity to Chk1 signaling. We describe three dominant-negative alleles of cdr1, which render cells supersensitive to Chk1 levels, and suppress the checkpoint defects of chk1Delta cells. Cdr1 encodes a protein kinase previously identified as a negative regulator of Wee1 activity in response to limited nutrition, but Cdr1 has not previously been linked to checkpoint signaling. Overproduction of Cdr1 promotes checkpoint defects and exacerbates the defective response to DNA damage of cells lacking Chk1. We conclude that regulation of Wee1 by Cdr1 and possibly by related kinases is an important antagonist of Chk1 signaling and represents a novel negative regulation of cell cycle arrest promoted by this checkpoint.","authors":"Calonge TM, O'Connell MJ","authors_abbrev":"Calonge TM et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-07-04","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC644.06c","SPCC18B5.03","SPBC216.05","SPBC342.05","SPAC14C4.13","SPAC8E11.02c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:7929623","title":"Fission yeast protein kinase C gene homologues are required for protoplast regeneration: a functional link between cell wall formation and cell shape control.","citation":"J Cell Sci 1994 May;107 ( Pt 5):1131-6","abstract":"Two novel protein kinase C (n PKC) gene homologues, pck1+ and pck2+ were isolated from the fission yeast Schizosaccharomyces pombe (Toda et al. (1993) EMBO J. 12, 1987). We examined the functional differences of pck1+ and pck2+ in cell wall formation and actin organization of S. pombe. Regenerating protoplasts of a wild-type strain, single gene disruptants of pck1+ (delta pck1) and pck2+ (delta pck2) were used as a simple model to examine the functional links between PKC, cell wall formation and actin organization. Protoplasts of the wild-type strain and those of delta pck1 reverted to intact cells in osmotically stabilized liquid medium. A close spatial association between new cell wall formation and actin was observed in these two strains. In delta pck2, protoplasts did not revert to intact cells: (1) scarcely any new cell wall material was formed; (2) actin was not reorganized; and (3) nuclear division and an increase in the amount of cytoplasm were observed in the regenerating protoplasts. These findings demonstrate that the pck2+ gene has a function essential for protoplast regeneration but the pck1+ gene does not. Involvement of n PKCs in cell wall formation and actin organization was also clarified. The effect of staurosporine (a potent inhibitor of protein kinases) on regenerating protoplasts of the three strains confirmed the assumption that the pck2 protein is an in vivo target of staurosporine in the fission yeast.","authors":"Kobori H, Toda T, Yaguchi H, Toya M, Yanagida M, Osumi M","authors_abbrev":"Kobori H et al.","pubmed_publication_date":"May 1994","pubmed_entrez_date":"1994-05-01","publication_year":"1994","canto_session_key":"551c5df484f39afb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-08 08:49:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-08 08:49:45","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.04c","SPAC17G8.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-08"},{"uniquename":"PMID:23066505","title":"The unfolded protein response in fission yeast modulates stability of select mRNAs to maintain protein homeostasis.","citation":"Elife 2012 Oct 15;1:e00048","abstract":"The unfolded protein response (UPR) monitors the protein folding capacity of the endoplasmic reticulum (ER). In all organisms analyzed to date, the UPR drives transcriptional programs that allow cells to cope with ER stress. The non-conventional splicing of Hac1 (yeasts) and XBP1 (metazoans) mRNA, encoding orthologous UPR transcription activators, is conserved and dependent on Ire1, an ER membrane-resident kinase/endoribonuclease. We found that the fission yeast Schizosaccharomyces pombe lacks both a Hac1/XBP1 ortholog and a UPR-dependent-transcriptional-program. Instead, Ire1 initiates the selective decay of a subset of ER-localized-mRNAs that is required to survive ER stress. We identified Bip1 mRNA, encoding a major ER-chaperone, as the sole mRNA cleaved upon Ire1 activation that escapes decay. Instead, truncation of its 3' UTR, including loss of its polyA tail, stabilized Bip1 mRNA, resulting in increased Bip1 translation. Thus, S. pombe uses a universally conserved stress-sensing machinery in novel ways to maintain homeostasis in the ER.DOI:http://dx.doi.org/10.7554/eLife.00048.001.","doi":"10.7554/eLife.00048","authors":"Kimmig P, Diaz M, Zheng J, Williams CC, Lang A, Aragón T, Li H, Walter P","authors_abbrev":"Kimmig P et al.","pubmed_publication_date":"15 Oct 2012","pubmed_entrez_date":"2012-10-16","publication_year":"2012","canto_session_key":"3f3648af903ea59c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-23 14:16:35","canto_approved_date":"2020-11-16 18:11:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-23 14:11:17","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC830.08c","SPBC29A10.08","SPAC167.01","SPAC22A12.15c","SPCC550.03c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2017-11-23"},{"uniquename":"PMID:22733737","title":"Ers1 links HP1 to RNAi.","citation":"Proc Natl Acad Sci U S A 2012 Jul 10;109(28):11258-63","abstract":"Pericentromeric heterochromatin formation is mediated by repressive histone H3 lysine 9 methylation (H3K9Me) and its recognition by HP1 proteins. Intriguingly, in many organisms, RNAi is coupled to this process through poorly understood mechanisms. In Schizosaccharomyces pombe, the H3-K9 methyltransferase Clr4 and the heterochromatin protein 1 (HP1) ortholog Swi6 are critical for RNAi, whereas RNAi stimulates H3K9Me. In addition to the endoribonuclease Dcr1, RNAi in S. pombe requires two interacting protein complexes, the RITS complex, which contains an Argonaute subunit, and the RDRC complex, which contains an RNA-dependent RNA polymerase subunit. We previously identified Ers1 (essential for RNAi-dependent silencing) as an orphan protein that genetically acts in the RNAi pathway. Using recombinant proteins, we show here that Ers1 directly and specifically interacts with HP1/Swi6. Two-hybrid assays indicate that Ers1 also directly interacts with several RNAi factors. Consistent with these interactions, Ers1 associates in vivo with the RITS complex, the RDRC complex, and Dcr1, and it promotes interactions between these factors. Ers1, like Swi6, is also required for RNAi complexes to associate with pericentromeric noncoding RNAs. Overexpression of Ers1 results in a dominant-negative phenotype that can be specifically suppressed by increasing levels of the RDRC subunit Hrr1 or of Dcr1, further supporting a functional role for Ers1 in promoting the assembly of the RNAi machinery. Through the interactions described here, Ers1 may promote RNAi by tethering the corresponding enzyme complexes to HP1-coated chromatin, thereby placing them in proximity to the nascent noncoding RNA substrate.","doi":"10.1073/pnas.1204947109","authors":"Rougemaille M, Braun S, Coyle S, Dumesic PA, Garcia JF, Isaac RS, Libri D, Narlikar GJ, Madhani HD","authors_abbrev":"Rougemaille M et al.","pubmed_publication_date":"10 Jul 2012","pubmed_entrez_date":"2012-06-27","publication_year":"2012","canto_session_key":"75d6b2ffa7c95853","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F12.09","SPCC663.12","SPAC18G6.02c","SPAC21E11.03c","SPCC1393.05","SPCC188.13c","SPBP8B7.28c","SPBC83.03c","SPAC664.01c","SPCC1739.03"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"EMBL:AU007427","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29162938","title":"RNA metabolism is the primary target of formamide in vivo.","citation":"Sci Rep 2017 Nov 21;7(1):15895","abstract":"The synthesis, processing and function of coding and non-coding RNA molecules and their interacting proteins has been the focus of a great deal of research that has boosted our understanding of key molecular pathways that underlie higher order events such as cell cycle control, development, innate immune response and the occurrence of genetic diseases. In this study, we have found that formamide preferentially weakens RNA related processes in vivo. Using a non-essential Schizosaccharomyces pombe gene deletion collection, we identify deleted loci that make cells sensitive to formamide. Sensitive deletions are significantly enriched in genes involved in RNA metabolism. Accordingly, we find that previously known temperature-sensitive splicing mutants become lethal in the presence of the drug under permissive temperature. Furthermore, in a wild type background, splicing efficiency is decreased and R-loop formation is increased in the presence of formamide. In addition, we have also isolated 35 formamide-sensitive mutants, many of which display remarkable morphology and cell cycle defects potentially unveiling new players in the regulation of these processes. We conclude that formamide preferentially targets RNA related processes in vivo, probably by relaxing RNA secondary structures and/or RNA-protein interactions, and can be used as an effective tool to characterize these processes.","doi":"10.1038/s41598-017-16291-8","authors":"Hoyos-Manchado R, Reyes-Martín F, Rallis C, Gamero-Estévez E, Rodríguez-Gómez P, Quintero-Blanco J, Bähler J, Jiménez J, Tallada VA","authors_abbrev":"Hoyos-Manchado R et al.","pubmed_publication_date":"21 Nov 2017","pubmed_entrez_date":"2017-11-23","publication_year":"2017","canto_session_key":"6b8d0fd1b5bcd2a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rafael Hoyos-Manchado","canto_first_approved_date":"2018-01-05 14:33:54","canto_approved_date":"2023-03-15 17:42:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-18 17:47:22","canto_added_date":"2017-11-24 01:15:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Rafael Hoyos-Manchado","community_curator":true,"annotation_count":42,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.14","SPAC31A2.06","SPAC27D7.14c","SPAC22F8.12c","SPAC15E1.03","SPBC83.12","SPAPJ698.03c","SPBC337.03","SPBC337.06c","SPBC32F12.05c","SPAC644.12","SPBP22H7.07","SPAC869.03c","SPAC29E6.02","SPAC30D11.13","SPAC8C9.07","SPAC22A12.07c","SPAC3G9.08","SPAC31G5.18c","SPBC24C6.11","SPAC4F10.06","SPCC794.12c","SPAC17G8.05","SPAC3H8.05c","SPBC17A3.05c","SPAPB1E7.02c","SPCC10H11.01","SPAC9.13c","SPAC13F5.07c","SPCC338.16","SPBC1718.03","SPBP23A10.16","SPBC16H5.03c","SPBC3D6.08c","SPCC777.14","SPBC19G7.10c","SPCC297.03","SPCC4B3.10c","SPAC23H3.13c","SPAC20H4.02","SPAC1F7.13c","SPBC365.06","SPBC9B6.07"],"gene_count":43,"ltp_gene_count":43,"approved_date":"2018-01-05"},{"uniquename":"PMID:25451933","title":"Aip1 promotes actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring.","citation":"J Biol Chem 2015 Jan 23;290(4):2289-300","abstract":"Aip1 (actin interacting protein 1) is ubiquitous in eukaryotic organisms, where it cooperates with cofilin to disassemble actin filaments, but neither its mechanism of action nor its biological functions have been clear. We purified both fission yeast and human Aip1 and investigated their biochemical activities with or without cofilin. Both types of Aip1 bind actin filaments with micromolar affinities and weakly nucleate actin polymerization. Aip1 increases up to 12-fold the rate that high concentrations of yeast or human cofilin sever actin filaments, most likely by competing with cofilin for binding to the side of actin filaments, reducing the occupancy of the filaments by cofilin to a range favorable for severing. Aip1 does not cap the barbed ends of filaments severed by cofilin. Fission yeast lacking Aip1 are viable and assemble cytokinetic contractile rings normally, but rings in these Δaip1 cells accumulate 30% less myosin II. Further, these mutant cells initiate the ingression of cleavage furrows earlier than normal, shortening the stage of cytokinetic ring maturation by 50%. The Δaip1 mutation has negative genetic interactions with deletion mutations of both capping protein subunits and cofilin mutations with severing defects, but no genetic interaction with deletion of coronin.","doi":"10.1074/jbc.M114.612978","authors":"Chen Q, Courtemanche N, Pollard TD","authors_abbrev":"Chen Q et al.","pubmed_publication_date":"23 Jan 2015","pubmed_entrez_date":"2014-12-03","publication_year":"2015","canto_session_key":"cb15339cd6cc0df8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-08 11:46:45","canto_approved_date":"2026-01-29 15:13:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-05 11:58:16","canto_added_date":"2014-12-04 01:15:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.04c","SPAC23C4.02","SPAC4F10.15c","SPAC12B10.07","SPAC9G1.05","SPAC631.01c","SPAC926.03","SPBC32H8.12c","SPAC20G4.06c"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2021-01-08"},{"uniquename":"EMBL:AU012610","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.123"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21110009","title":"Use of recombinantly produced 15N3-labelled nicotianamine for fast and sensitive stable isotope dilution ultra-performance liquid chromatography/electrospray ionization time-of-flight mass spectrometry.","citation":"Anal Bioanal Chem 2011 Jan;399(3):1355-61","abstract":"Nicotianamine (NA) is an important metal chelator, implicated in the intra- and intercellular trafficking of several transition metal ions in plants. To decipher its roles in physiological processes such as micronutrient acquisition, distribution or storage, fast and sensitive analytical techniques for quantification of this non-proteinogenic amino acid will be required. The use of a recombinant Schizosaccharomyces pombe strain expressing a nicotianamine synthase (NAS) gene allowed for the production of [(15)N(3)]-NA, which was enriched from cell extracts through cation exchange and used for stable isotope dilution analysis of NA. Such an approach should be widely applicable to important bioanalytes that are difficult to synthesize. The analytical procedure comprises mild aqueous extraction and rapid Fmoc derivatization, followed by fast separation using ultra-performance liquid chromatography (UPLC) and sensitive detection by positive ion electrospray ionization time-of-flight mass spectrometry (ESI-TOF-MS) with a chromatographic cycle time of only 8 min. Derivatization was optimized with respect to incubation time and species suitable for quantification. The limit of detection was 0.14 to 0.23 pmol in biological matrices with the response being linear up to 42 pmol. Recovery rates were between 83% and 104% in various biological matrices including fission yeast cells, fungal mycelium, plant leaves and roots.","doi":"10.1007/s00216-010-4436-7","authors":"Schmidt H, Böttcher C, Trampczynska A, Clemens S","authors_abbrev":"Schmidt H et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-11-27","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32374864","title":"DXO/Rai1 enzymes remove 5'-end FAD and dephospho-CoA caps on RNAs.","citation":"Nucleic Acids Res 2020 Jun 19;48(11):6136-6148","abstract":"In eukaryotes, the DXO/Rai1 enzymes can eliminate most of the incomplete and non-canonical NAD caps through their decapping, deNADding and pyrophosphohydrolase activities. Here, we report that these enzymes can also remove FAD and dephospho-CoA (dpCoA) non-canonical caps from RNA, and we have named these activities deFADding and deCoAping. The crystal structures of mammalian DXO with 3'-FADP or CoA and fission yeast Rai1 with 3'-FADP provide elegant insight to these activities. FAD and CoA are accommodated in the DXO/Rai1 active site by adopting folded conformations. The flavin of FAD and the pantetheine group of CoA contact the same region at the bottom of the active site tunnel, which undergoes conformational changes to accommodate the different cap moieties. We have developed FAD-capQ to detect and quantify FAD-capped RNAs and determined that FAD caps are present on short RNAs (with less than ∼200 nucleotides) in human cells and that these RNAs are stabilized in the absence of DXO.","doi":"10.1093/nar/gkaa297","authors":"Doamekpor SK, Grudzien-Nogalska E, Mlynarska-Cieslak A, Kowalska J, Kiledjian M, Tong L","authors_abbrev":"Doamekpor SK et al.","pubmed_publication_date":"19 Jun 2020","pubmed_entrez_date":"2020-05-07","publication_year":"2020","canto_session_key":"915a0799824f1f52","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-24 07:51:00","canto_approved_date":"2024-02-16 19:38:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-23 16:44:56","canto_added_date":"2020-05-08 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-24","pdb_entries":[{"pdb_id":"6wug","gene_chains":[{"gene_uniquename":"SPAC19D5.06c","chain":"A","position":"1-352"}],"title":"Crystal Structure of S. pombe Rai1 in complex with 3'-FADP","entry_authors":"Doamekpor SK,Tong L","entry_authors_abbrev":"Doamekpor SK et al.","reference_uniquename":"PMID:32374864","experimental_method":"X-ray","resolution":"1.9"},{"pdb_id":"6wui","gene_chains":[{"gene_uniquename":"SPAC19D5.06c","chain":"A","position":"1-352"}],"title":"Crystal Structure of mutant S. pombe Rai1 (E150S/E199Q/E239Q) in complex with 3'-FADP","entry_authors":"Doamekpor SK,Tong L","entry_authors_abbrev":"Doamekpor SK et al.","reference_uniquename":"PMID:32374864","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:9090839","title":"Assessment of delta muH+ in Schizosaccharomyces pombe; intracellular inclusion of impermeable agents by electroporation.","citation":"Folia Microbiol (Praha) 1996;41(1):98-100","abstract":"","authors":"Höfer M, Calahorra M, Klein B, Peña A","authors_abbrev":"Höfer M et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12557275","title":"Isolation and characterization of the plasma membrane biotin transporter from Schizosaccharomyces pombe.","citation":"Yeast 2003 Feb;20(3):221-31","abstract":"The fission yeast Schizosaccharomyces pombe is auxotrophic for biotin (vitamin H) and growth depends on biotin uptake over the plasma membrane. Here a biotin transport mutant of Saccharomyces cerevisiae is used to identify the vht1(+) gene encoding the Schizosaccharomyces pombe plasma membrane transport protein for biotin. SpVht1p belongs to the family of allantoate transporters and has only little sequence homology to the S. cerevisiae biotin transporter. Although having dissimilar primary structures, the biotin transporters in Sz. pombe and S. cerevisiae share similar biochemical properties and regulation. Like in S. cerevisiae, biotin uptake in Sz. pombe is a high-affinity process, is optimal at acidic pH values and inhibited by protonophores, indicating that SpVht1p acts as a proton-biotin symporter. Desthiobiotin, the metabolic precursor of biotin, is also imported by SpVht1p. Deletion of vht1(+) abolishes growth on low external concentrations of the vitamin, showing that vht1(+) encodes the only protein that mediates biotin uptake in Sz. pombe. Expression of vht1(+) is maximal at low external biotin concentrations, indicating that Sz. pombe can adjust the rate of biotin uptake to meet the requirement for the vitamin.","authors":"Stolz J","authors_abbrev":"Stolz J","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-01-31","publication_year":"2003","canto_session_key":"9569cc1253e3417a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-07 16:19:13","canto_approved_date":"2017-11-07 16:19:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-03-29 15:09:01","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.16c","SPAC1B3.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-11-07"},{"uniquename":"PMID:38424265","title":"Identification of plb1 mutation that extends longevity via activating Sty1 MAPK in Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2024 Feb 29;299(1):20","abstract":"To understand the lifespan of higher organisms, including humans, it is important to understand lifespan at the cellular level as a prerequisite. So, fission yeast is a good model organism for the study of lifespan. To identify the novel factors involved in longevity, we are conducting a large-scale screening of long-lived mutant strains that extend chronological lifespan (cell survival in the stationary phase) using fission yeast. One of the newly acquired long-lived mutant strains (No.98 mutant) was selected for analysis and found that the long-lived phenotype was due to a missense mutation (92Phe → Ile) in the plb1 +  gene. plb1 +  gene in fission yeast is a nonessential gene encoding a homolog of phospholipase B, but its functions under normal growth conditions, as well as phospholipase B activity, remain unresolved. Our analysis of the No.98 mutant revealed that the plb1 mutation reduces the integrity of the cellular membrane and cell wall and activates Sty1 via phosphorylation.","doi":"10.1007/s00438-024-02107-8","authors":"Maekawa Y, Matsui K, Okamoto K, Shimasaki T, Ohtsuka H, Tani M, Ihara K, Aiba H","authors_abbrev":"Maekawa Y et al.","pubmed_publication_date":"29 Feb 2024","pubmed_entrez_date":"2024-02-29","publication_year":"2024","canto_session_key":"0d1bc3ee794002e7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_first_approved_date":"2024-06-26 08:59:37","canto_approved_date":"2024-06-27 13:03:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-25 08:58:37","canto_added_date":"2024-03-02 00:25:04","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":3,"orcid":"0000-0002-7775-0446","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":19,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1A6.04c","SPAC24B11.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-06-26"},{"uniquename":"PMID:19264558","title":"Screening a genome-wide S. pombe deletion library identifies novel genes and pathways involved in genome stability maintenance.","citation":"DNA Repair (Amst) 2009 May 01;8(5):672-9","abstract":"The maintenance of genome stability is essential for an organism to avoid cell death and cancer. Based on screens for mutant sensitivity against DNA damaging agents a large number of DNA repair and DNA damage checkpoint genes have previously been identified in genetically amenable model organisms. These screens have however not been exhaustive and various genes have been, and remain to be, identified by other means. We therefore screened a genome-wide Schizosaccharomyces pombe deletion library for mutants sensitive against various DNA damaging agents. Screening the library on different concentrations of these genotoxins allowed us to assign a semi-quantitative score to each mutant expressing the degree of sensitivity. We isolated a total of 229 mutants which show sensitivity to one or more of the DNA damaging agents used. This set of mutants was significantly enriched for processes involved in DNA replication, DNA repair, DNA damage checkpoint, response to UV, mating type switching, telomere length maintenance and meiosis, and also for processes involved in the establishment and maintenance of chromatin architecture (notably members of the SAGA complex), transcription (members of the CCR4-Not complex) and microtubule related processes (members of the DASH complex). We also identified 23 sensitive mutants which had previously been classified as \"sequence orphan\" or as \"conserved hypothetical\". Among these, we identified genes showing extensive homology to CtIP, Stra13, Ybp1/Ybp2, Human Fragile X mental retardation interacting protein NUFIP1, and Aprataxin. The identification of these homologues will provide a basis for the further characterisation of the role of these conserved proteins in the genetically amenable model organism S. pombe.","doi":"10.1016/j.dnarep.2009.01.016","authors":"Deshpande GP, Hayles J, Hoe KL, Kim DU, Park HO, Hartsuiker E","authors_abbrev":"Deshpande GP et al.","pubmed_publication_date":"01 May 2009","pubmed_entrez_date":"2009-03-07","publication_year":"2009","canto_session_key":"56c1003eeaf5d093","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-24 11:12:49","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-24 11:12:35","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":413,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_19264558_phaf.tsv"}],"genes":["SPBC27B12.11c","SPCC74.09","SPBC1289.14","SPCC553.04","SPCC1442.02","SPAC513.03","SPCC338.08","SPAC1142.07c","SPCC364.03","SPCC757.09c","SPAC144.02","SPAC23E2.01","SPCC126.15c","SPBC2D10.18","SPAC4F10.18","SPAC20H4.07","SPCC1393.11","SPAC694.06c","SPAC3H8.10","SPCC645.05c","SPBC1105.10","SPCC18.06c","SPAC22F3.10c","SPAC16C9.06c","SPAC23H3.13c","SPAC644.14c","SPAC222.08c","SPAC6B12.08","SPBC21C3.18","SPBC27B12.06","SPAC821.05","SPAC19B12.04","SPAC19B12.10","SPCC417.02","SPAC19G12.08","SPBC2G2.14","SPAC8C9.03","SPAC13G7.07","SPAC13C5.07","SPCC11E10.06c","SPAC6B12.02c","SPAC11G7.02","SPAC31A2.13c","SPBC660.14","SPBC3E7.08c","SPBC4F6.10","SPAC110.02","SPBC2G2.01c","SPAC17H9.10c","SPAC11G7.04","SPBC342.05","SPCC1450.02","SPCC1393.10","SPCC970.07c","SPAC29B12.04","SPAC31A2.15c","SPAC144.06","SPBC31F10.09c","SPAC328.10c","SPAC9G1.05","SPAC2F3.15","SPAC8E11.02c","SPBC29A3.14c","SPAC23C11.04c","SPBC649.03","SPAC17H9.19c","SPBC1604.08c","SPBC365.14c","SPBC25H2.10c","SPCC61.02","SPAC23D3.09","SPCC1682.12c","SPAC13C5.04","SPAC1071.02","SPBC1105.05","SPAC4C5.02c","SPAC4D7.03","SPAC26H5.05","SPBC16A3.17c","SPAC20G4.04c","SPAC1002.14","SPBC3B8.10c","SPAC17C9.13c","SPBP35G2.08c","SPAC29B12.06c","SPAC29B12.08","SPCC31H12.08c","SPCC777.13","SPBC1773.12","SPAC13G6.01c","SPBC119.08","SPAPJ696.01c","SPBC2G2.13c","SPAC15A10.03c","SPCP1E11.05c","SPAC31A2.11c","SPAC9.02c","SPBC839.03c","SPBC28F2.02","SPCC553.01c","SPBC21B10.10","SPAC6F12.09","SPBC18H10.11c","SPCC126.13c","SPCC594.02c","SPCC188.07","SPCC4G3.11","SPCC1739.05","SPAC1952.05","SPBC21D10.10","SPAC1952.07","SPAC18G6.15","SPAC4G9.16c","SPBPB2B2.10c","SPBC56F2.08c","SPCC18B5.11c","SPAC664.07c","SPBC11B10.07c","SPAC824.02","SPCC306.06c","SPCC2H8.05c","SPBC27.02c","SPAC1805.07c","SPAC3H5.11","SPAC1610.02c","SPAC20H4.02","SPBC32F12.07c","SPAC22H12.04c","SPBC106.10","SPAC1782.05","SPAC22F8.11","SPCC18.09c","SPBC146.13c","SPBC30D10.04","SPBC28F2.10c","SPBC56F2.11","SPAC1F3.02c","SPBC9B6.07","SPBC713.07c","SPBC1921.07c","SPAC30D11.04c","SPBC19C7.12c","SPBC16A3.03c","SPCC338.16","SPAC25H1.02","SPBC21.02","SPCC18B5.06","SPAC23C11.14","SPBC1861.03","SPBC428.08c","SPBC19G7.18c","SPBC16G5.06","SPBC902.02c","SPAC56F8.02","SPCP31B10.05","SPAC664.01c","SPBC216.05","SPBC365.06","SPCC23B6.05c","SPBC342.06c","SPAPB1A11.01","SPAC11E3.08c","SPAC24H6.03","SPAC4H3.05","SPCC895.07","SPAC12B10.12c","SPBC27.06c","SPAC227.07c","SPBC26H8.12","SPBC839.05c","SPAC1805.14","SPBC1778.09","SPAC16.01","SPAC8C9.10c","SPAC2E1P3.04","SPCC576.12c","SPBC947.08c","SPAC4F10.19c","SPAC9E9.13","SPAC6F6.01","SPAC1F12.09","SPAC3C7.03c","SPBC20F10.07","SPBC1105.04c","SPBC56F2.05c","SPBC215.03c","SPBC12C2.02c","SPCC1020.07","SPAC12G12.12","SPAC3H8.05c","SPAC13A11.04c","SPBC2A9.08c","SPBC543.07","SPAC14C4.13","SPBC21H7.04","SPCC126.08c","SPAC25B8.05","SPBC14C8.17c","SPAC688.10","SPBC725.10","SPCC4G3.15c","SPBC16C6.03c","SPAPB1A10.09","SPCC285.13c","SPAC9G1.07","SPCC330.02","SPBC21B10.03c","SPAC4G8.05","SPBC25D12.06","SPCC1753.02c","SPBC725.12","SPBC1718.07c","SPCC162.10","SPBC651.10","SPBC651.09c","SPCC126.04c","SPAC9.05","SPBC17G9.07","SPBC4F6.06","SPAC9E9.08","SPAC1783.07c","SPAC4D7.11","SPCC1259.08","SPAPB1E7.06c","SPBC557.02c","SPBC1347.01c","SPCC895.05","SPBC23E6.08","SPBC543.03c"],"gene_count":229,"ltp_gene_count":0,"approved_date":"2014-07-24"},{"uniquename":"EMBL:AU011039","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10769204","title":"The G(2) DNA damage checkpoint targets both Wee1 and Cdc25.","citation":"J Cell Sci 2000 May;113 ( Pt 10):1727-36","abstract":"The onset of mitosis is controlled by the cyclin dependent kinase Cdc2p. Cdc2p activity is controlled through the balance of phosphorylation and dephosphorylation of tyrosine-15 (Y15) by the Wee1p kinase and Cdc25p phosphatase. In the fission yeast Schizosaccharomyces pombe, detection of DNA damage in G(2) activates a checkpoint that prevents entry into mitosis through the maintenance of Y15 phosphorylation of Cdc2p, thus ensuring DNA repair precedes chromosome segregation. The protein kinase Chk1p is the endpoint of this checkpoint pathway. We have previously reported that overexpression of Chk1p causes a wee1(+)-dependent G(2) arrest, and this or irradiation leads to hyperphosphorylation of Wee1p. Moreover, Chk1p directly phosphorylates Wee1p in vitro. These data suggested that Wee1p is a key target of Chk1p action in checkpoint control. However, cells lacking wee1(+) are checkpoint proficient and sustained Chk1p overexpression arrests cell cycle progression independently of Wee1p. Therefore, up-regulation of Wee1p alone cannot enforce a checkpoint arrest. Chk1p can also phosphorylate Cdc25p in vitro. These phosphorylation events are thought to promote the interaction with 14-3-3 proteins the cytoplasmic retention of the 14-3-3/Cdc25p complexes. However, we show here that the G(2) DNA damage checkpoint is intact in cells that regulate mitotic entry independently of Cdc25p. Further, these cells are still sensitive to Chk1p-mediated arrest, and so down-regulation of Cdc25p is also insufficient to regulate checkpoint arrest. Conversely, inactivation of both wee1(+) and cdc25(+ )abolishes checkpoint control. We also show that activation of the G(2) DNA damage checkpoint induces a transient increase in Wee1p levels. We conclude that the G(2) DNA damage checkpoint simultaneously signals via both up-regulation of Wee1p and down-regulation of Cdc25p, thus providing a double-lock mechanism to ensure cell cycle arrest and genomic stability.","authors":"Raleigh JM, O'Connell MJ","authors_abbrev":"Raleigh JM et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-04-19","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24748152","title":"Fission yeast Rad52 phosphorylation restrains error prone recombination pathways.","citation":"PLoS One 2014;9(4):e95788","abstract":"Rad52 is a key protein in homologous recombination (HR), a DNA repair pathway dedicated to double strand breaks and recovery of blocked or collapsed replication forks. Rad52 allows Rad51 loading on single strand DNA, an event required for strand invasion and D-loop formation. In addition, Rad52 functions also in Rad51 independent pathways because of its ability to promote single strand annealing (SSA) that leads to loss of genetic material and to promote D-loops formation that are cleaved by Mus81 endonuclease. We have previously reported that fission yeast Rad52 is phosphorylated in a Sty1 dependent manner upon oxidative stress and in cells where the early step of HR is impaired because of lack of Rad51. Here we show that Rad52 is also constitutively phosphorylated in mus81 null cells and that Sty1 partially impinges on such phosphorylation. As upon oxidative stress, the Rad52 phosphorylation in rad51 and mus81 null cells appears to be independent of Tel1, Rad3 and Cdc2. Most importantly, we show that mutating serine 365 to glycine (S365G) in Rad52 leads to loss of the constitutive Rad52 phosphorylation observed in cells lacking Rad51 and to partial loss of Rad52 phosphorylation in cells lacking Mus81. Contrariwise, phosphorylation of Rad52-S365G protein is not affected upon oxidative stress. These results indicate that different Rad52 residues are phosphorylated in a Sty1 dependent manner in response to these distinct situations. Analysis of spontaneous HR at direct repeats shows that mutating serine 365 leads to an increase in spontaneous deletion-type recombinants issued from mitotic recombination that are Mus81 dependent. In addition, the recombination rate in the rad52-S365G mutant is further increased by hydroxyurea, a drug to which mutant cells are sensitive.","doi":"10.1371/journal.pone.0095788","authors":"Bellini A, Girard PM, Tessier L, Sage E, Francesconi S","authors_abbrev":"Bellini A et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-04-22","publication_year":"2014","canto_session_key":"f9ed87074b4f1c93","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPCC4G3.05c","SPAC24B11.06c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11433012","title":"Comparison of the RNA polymerase III transcription machinery in Schizosaccharomyces pombe, Saccharomyces cerevisiae and human.","citation":"Nucleic Acids Res 2001 Jul 01;29(13):2675-90","abstract":"Multi-subunit transcription factors (TF) direct RNA polymerase (pol) III to synthesize a variety of essential small transcripts such as tRNAs, 5S rRNA and U6 snRNA. Use by pol III of both TATA-less and TATA-containing promoters, together with progress in the Saccharomyces cerevisiae and human systems towards elucidating the mechanisms of actions of the pol III TFs, provides a paradigm for eukaryotic gene transcription. Human and S.cerevisiae pol III components reveal good general agreement in the arrangement of orthologous TFs that are distributed along tRNA gene control elements, beginning upstream of the transcription initiation site and extending through the 3' terminator element, although some TF subunits have diverged beyond recognition. For this review we have surveyed the Schizosaccharomyces pombe database and identified 26 subunits of pol III and associated TFs that would appear to represent the complete core set of the pol III machinery. We also compile data that indicate in vivo expression and/or function of 18 of the fission yeast proteins. A high degree of homology occurs in pol III, TFIIIB, TFIIIA and the three initiation-related subunits of TFIIIC that are associated with the proximal promoter element, while markedly less homology is apparent in the downstream TFIIIC subunits. The idea that the divergence in downstream TFIIIC subunits is associated with differences in pol III termination-related mechanisms that have been noted in the yeast and human systems but not reviewed previously is also considered.","authors":"Huang Y, Maraia RJ","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"01 Jul 2001","pubmed_entrez_date":"2001-07-04","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24059229","title":"P-glycoprotein and vacuolar ATPase synergistically confer anthracycline resistance to fission yeast and human cells.","citation":"Curr Med Chem 2014;21(2):251-60","abstract":"Drug resistance is a major hurdle to the success of chemotherapy. The permeability glycoprotein (P-gp) is an important factor dictating drug access to the cells, as it controls the efflux of chemotherapeutic agents against the concentration gradient. Pmd1, a P-gp-like protein, was recently isolated as a doxorubicin resistance gene in fission yeast. Although the null mutant of pmd1 (Δpmd1) exhibited sensitivity to doxorubicin, it showed an unexpectedly high resistance to the drug at relatively high concentrations. The data presented here suggest that this is due to the presence of cooperative processes that can complement and counteract drug cytotoxicity in the absence of Pmd1. One such factor, Rav1, is an essential factor in controlling the assembly of the pH-regulating transporter vacuolar-ATPase (V-ATPase) in fission yeast. The simultaneous disruption of Pmd1 and Rav1 resulted in a prominent accumulation of doxorubicin in the cytoplasm of cells, accompanied by a decline in cell viability. With concurrent treatment of pharmacological inhibitors in human cervical cancer cells, P-gp and V-ATPase were further shown to act synergistically to sensitize cells to doxorubicin also in the human cells. Furthermore, a novel Cornichon-like protein SPAC2C4.05 (herein named as Cor1) was demonstrated for the first time to be involved in the interaction with P-gp and V-ATPase to counteract doxorubicin-dependent cytotoxicity. Therefore this study identified a molecular cooperation between multiple membrane transporter proteins that confers chemoresistance to cells against the chemical insult of doxorubicin. Interestingly, this network exhibited differential effects to doxorubicin as compared with its close epimeric analog epirubicin, suggestive of the intricacy of the drug response regulated by this synergistic interaction. A model is discussed on how the versatility of this network can differentiate closely related chemical drug structures yet allow for the robustness to counteract a vast range of drugs.","authors":"Tay Z, Koo SH, Nguyen TT, Tan TS, Chen ML, Chin CF, Lim KK, Ang WH, Bay BH, Lee EJ, Chen ES","authors_abbrev":"Tay Z et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2013-09-25","publication_year":"2014","canto_session_key":"a256e92839edbc12","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-04 14:00:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-15 12:07:14","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2C4.05","SPBC1105.10","SPCC663.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-08-15"},{"uniquename":"PMID:21187966","title":"The prevalence and regulation of antisense transcripts in Schizosaccharomyces pombe.","citation":"PLoS One 2010 Dec 20;5(12):e15271","abstract":"A strand-specific transcriptome sequencing strategy, directional ligation sequencing or DeLi-seq, was employed to profile antisense transcriptome of Schizosaccharomyces pombe. Under both normal and heat shock conditions, we found that polyadenylated antisense transcripts are broadly expressed while distinct expression patterns were observed for protein-coding and non-coding loci. Dominant antisense expression is enriched in protein-coding genes involved in meiosis or stress response pathways. Detailed analyses further suggest that antisense transcripts are independently regulated with respect to their sense transcripts, and diverse mechanisms might be potentially involved in the biogenesis and degradation of antisense RNAs. Taken together, antisense transcription may have profound impacts on global gene regulation in S. pombe.","doi":"10.1371/journal.pone.0015271","authors":"Ni T, Tu K, Wang Z, Song S, Wu H, Xie B, Scott KC, Grewal SI, Gao Y, Zhu J","authors_abbrev":"Ni T et al.","pubmed_publication_date":"20 Dec 2010","pubmed_entrez_date":"2010-12-29","publication_year":"2010","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40063661","title":"Fission yeast Caprin protein is required for efficient heterochromatin establishment.","citation":"PLoS Genet 2025 Mar 10;21(3):e1011620","abstract":"Heterochromatin is a key feature of eukaryotic genomes that serves important regulatory and structural roles in regions such as centromeres. In fission yeast, maintenance of existing heterochromatic domains relies on positive feedback loops involving histone methylation and non-coding RNAs. However, requirements for de novo establishment of heterochromatin are less well understood. Here, through a cross-based assay we have identified a novel factor influencing the efficiency of heterochromatin establishment. We determine that the previously uncharacterised protein is an ortholog of human Caprin1, an RNA-binding protein linked to stress granule formation. We confirm that the fission yeast ortholog, here named Cpn1, also associates with stress granules, and we uncover evidence of interplay between heterochromatin integrity and ribonucleoprotein (RNP) granule formation, with heterochromatin mutants showing reduced granule formation in the presence of stress, but increased granule formation in the absence of stress. We link this to regulation of non-coding heterochromatic transcripts, since in heterochromatin-deficient cells, Cpn1 can be seen to colocalise with accumulating pericentromeric transcripts, and absence of Cpn1 leads to hyperaccumulation of these RNAs at centromeres. Together, our findings unveil a novel link between RNP homeostasis and heterochromatin assembly, and implicate Cpn1 and associated factors in facilitating efficient heterochromatin establishment by enabling removal of excess transcripts that would otherwise impair assembly processes.","doi":"10.1371/journal.pgen.1011620","authors":"Zhang H, Kapitonova E, Orrego A, Spanos C, Strachan J, Bayne EH","authors_abbrev":"Zhang H et al.","pubmed_publication_date":"10 Mar 2025","pubmed_entrez_date":"2025-03-10","publication_year":"2025","canto_session_key":"157faab66755d6ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elizabeth Bayne","canto_first_approved_date":"2025-07-02 09:22:22","canto_approved_date":"2025-07-04 19:41:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-22 16:56:18","canto_added_date":"2025-03-11 00:25:04","annotation_curators":[{"name":"Elizabeth Bayne","community_curator":true,"annotation_count":58,"orcid":"0000-0001-8775-999X","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":39,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC12G12.08","SPBP8B7.21","SPBC31A8.01c","SPAC1952.05","SPCC663.06c","SPAC57A7.04c","SPBC29A10.09c","SPBC16D10.07c","SPCC736.11","SPBCPT2R1.06c","SPNCRNA.362","SPNCRNA.774","SPRRNA.05","SPAC139.01c","SPBP8B7.11","SPBC776.07","SPBC29A10.08","SPBPB10D8.03","SPAC12G12.07c","SPBC23G7.10c","SPAC26A3.12c","SPBC8E4.12c","SPAC750.07c","SPBPB8B6.04c","SPNCRNA.232","SPCC188.13c","SPBPB21E7.07","SPAC212.08c","SPAC15F9.01c","SPBPB21E7.01c","SPNCRNA.1241","SPCC1442.04c","SPNCRNA.230","SPNCRNA.1487","SPBC428.08c","SPAC212.12","SPBC800.03","SPNCRNA.1271","SPBP4G3.02","SPBC3E7.02c","SPBPB2B2.06c","SPBC460.04c","SPNCRNA.388","SPCC11E10.08"],"gene_count":44,"ltp_gene_count":16,"approved_date":"2025-07-02"},{"uniquename":"PMID:6079735","title":"Biochemical characterization of arginine muants in Schizosaccharomyces pombe and the possibility of repression.","citation":"Can J Genet Cytol 1967 Sep;9(3):462-72","abstract":"","authors":"Ali AM","authors_abbrev":"Ali AM","pubmed_publication_date":"Sep 1967","pubmed_entrez_date":"1967-09-01","publication_year":"1967","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19158664","title":"Smc5/6 maintains stalled replication forks in a recombination-competent conformation.","citation":"EMBO J 2009 Jan 21;28(2):144-55","abstract":"The Smc5/6 structural maintenance of chromosomes complex is required for efficient homologous recombination (HR). Defects in Smc5/6 result in chromosome mis-segregation and fragmentation. By characterising two Schizosaccharomyces pombe smc6 mutants, we define two separate functions for Smc5/6 in HR. The first represents the previously described defect in processing recombination-dependent DNA intermediates when replication forks collapse, which leads to increased rDNA recombination. The second novel function defines Smc5/6 as a positive regulator of recombination in the rDNA and correlates mechanistically with a requirement to load RPA and Rad52 onto chromatin genome-wide when replication forks are stably stalled by nucleotide depletion. Rad52 is required for all HR repair, but Rad52 loading in response to replication fork stalling is unexpected and does not correlate with damage-induced foci. We propose that Smc5/6 is required to maintain stalled forks in a stable recombination-competent conformation primed for replication restart.","doi":"10.1038/emboj.2008.273","authors":"Irmisch A, Ampatzidou E, Mizuno K, O'Connell MJ, Murray JM","authors_abbrev":"Irmisch A et al.","pubmed_publication_date":"21 Jan 2009","pubmed_entrez_date":"2009-01-23","publication_year":"2009","canto_session_key":"28bb12c162a98275","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jo Murray","canto_first_approved_date":"2020-12-10 17:26:13","canto_approved_date":"2021-01-25 16:05:12","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-12-05 10:57:25","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Jo Murray","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPAC30D11.10","SPCC5E4.06","SPAC664.01c","SPBC660.13c","SPCC18B5.11c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2020-12-10"},{"uniquename":"PMID:11318103","title":"Sequence of Crm1/exportin 1 mutant alleles reveals critical sites associated with multidrug resistance.","citation":"Curr Genet 2001 Feb;39(1):2-9","abstract":"We have previously shown that genes involved in a novel pathway of multidrug resistance (MDR) in the fission yeast Schizosaccharomyces pombe are functionally conserved in human cells (V. Spataro et al. (1997) J Biol Chem 272: 30470-30475). The human homologue of one of these genes, hCRM1, has recently been identified and found to function in nucleocytoplasmic export, a process which controls the subcellular localization and hence activity of a number of key cell cycle regulators and transcription factors. Several mutant alleles of crm1 confer a phenotype of MDR in S. pombe, through the nuclear accumulation of the AP-1 transcription factor Pap1. We therefore sequenced mutations of crm1 in fission yeast in order to guide the search for analogous hCRM1 mutations which could play a role in tumour-drug resistance. Fifteen yeast crm1 mutants were assessed by PCR and DNA sequencing. Four mis-sense mutations were identified in the open reading frame, three of which (G to A transitions at nucleotide positions 385, 895 and 1,288) were capable of conferring the MDR phenotype alone. For three of the four mutations found, the corresponding amino acid changes affect residues which are conserved in the human homologue hCRM1 and lie in highly conserved regions of the CRM1 protein. We analysed the corresponding hCRM1 coding regions by RT-PCR and sequencing in a panel of ten tumour cell lines, including three ovarian lines resistant either to cisplatin or paclitaxel, or to both and one MDR breast cancer cell line with nuclear accumulation of the transcription factor YB-1. No hCRM1 mutations were found in the three cDNA fragments examined in this panel of tumour cell lines. However, the identification of amino acid residues within the CRM1 protein that are critical for the export of the MDR-associated transcription factor Pap1 in fission yeast can guide further analysis of hCRM1 mutations in tumours with a MDR phenotype.","authors":"Carobbio S, Realini C, Norbury CJ, Toda T, Cavalli F, Spataro V","authors_abbrev":"Carobbio S et al.","pubmed_publication_date":"Feb 2001","pubmed_entrez_date":"2001-04-25","publication_year":"2001","canto_session_key":"f6bbb1302b15a4e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-11-05 09:43:29","canto_approved_date":"2022-01-04 18:33:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-27 14:59:02","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.17","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2013-11-05"},{"uniquename":"PMID:9372918","title":"Role of Schizosaccharomyces pombe RecQ homolog, recombination, and checkpoint genes in UV damage tolerance.","citation":"Mol Cell Biol 1997 Dec;17(12):6868-75","abstract":"The cellular responses to DNA damage are complex and include direct DNA repair pathways that remove the damage and indirect damage responses which allow cells to survive DNA damage that has not been, or cannot be, removed. We have identified the gene mutated in the rad12.502 strain as a Schizosaccharomyces pombe recQ homolog. The same gene (designated rqh1) is also mutated in the hus2.22 mutant. We show that Rqhl is involved in a DNA damage survival mechanism which prevents cell death when UV-induced DNA damage cannot be removed. This pathway also requires the correct functioning of the recombination machinery and the six checkpoint rad gene products plus the Cdsl kinase. Our data suggest that Rqh1 operates during S phase as part of a mechanism which prevents DNA damage causing cell lethality. This process may involve the bypass of DNA damage sites by the replication fork. Finally, in contrast with the reported literature, we do not find that rqh1 (rad12) mutant cells are defective in UV dimer endonuclease activity.","authors":"Murray JM, Lindsay HD, Munday CA, Carr AM","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1997-12-31","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3E7.08c","SPAC2G11.12","SPBC19C7.09c","SPCC1259.13"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:21730056","title":"Phylogenetic comparison of small RNA-triggered transcriptional gene silencing.","citation":"J Biol Chem 2011 Aug 26;286(34):29443-8","abstract":"The discovery of RNA interference has revealed complex roles for small RNAs in regulating gene expression and cellular physiology. Small RNAs have been demonstrated to be involved in post-transcriptional suppression of translation, targeted degradation of messenger RNAs, and transcriptional suppression via epigenetic modifications of histones and DNA. In fission yeast, RNAi mediates suppression of centromeric transcripts, whereas in plants, transcriptional gene silencing appears to be primarily an antiviral mechanism. In mammals, the well annotated functional role of RNAi is primarily post-transcriptional, but there is increasing evidence that this mechanism can also work to suppress or modulate gene transcription, although it is not clear what primary function this serves. We overview, compare, and contrast the transcriptional silencing pathways in yeast, plants, and mammals in this article. This minireview is intended to provide the reader with a framework of how the RNAi machinery appears to be universally involved in various aspects of transcriptional regulation with discussions of similarities and differences in the components and mechanisms of achieving transcriptional silencing.","doi":"10.1074/jbc.R111.276378","authors":"Zhang X, Rossi JJ","authors_abbrev":"Zhang X et al.","pubmed_publication_date":"26 Aug 2011","pubmed_entrez_date":"2011-07-07","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32796726","title":"Biology and Physics of Heterochromatin- Like  Domains/Complexes.","citation":"Cells 2020 Aug 11;9(8)","abstract":"The hallmarks of constitutive heterochromatin, HP1 and H3K9me2/3, assemble heterochromatin- like  domains/complexes outside canonical constitutively heterochromatic territories where they regulate chromatin template-dependent processes. Domains are more than 100 kb in size; complexes less than 100 kb. They are present in the genomes of organisms ranging from fission yeast to human, with an expansion in size and number in mammals. Some of the likely functions of domains/complexes include silencing of the donor mating type region in fission yeast, preservation of DNA methylation at imprinted germline differentially methylated regions (gDMRs) and regulation of the phylotypic progression during vertebrate development. Far  cis - and  trans -contacts between micro-phase separated domains/complexes in mammalian nuclei contribute to the emergence of epigenetic compartmental domains (ECDs) detected in Hi-C maps. A thermodynamic description of micro-phase separation of heterochromatin- like  domains/complexes may require a gestalt shift away from the monomer as the \" unit of incompatibility \" that determines the sign and magnitude of the Flory-Huggins parameter, χ. Instead, a more dynamic structure, the oligo-nucleosomal \"clutch\", consisting of between 2 and 10 nucleosomes is both the long sought-after secondary structure of chromatin and its unit of incompatibility. Based on this assumption we present a simple theoretical framework that enables an estimation of χ for domains/complexes flanked by euchromatin and thereby an indication of their tendency to phase separate. The degree of phase separation is specified by χN, where N is the number of \"clutches\" in a domain/complex. Our approach could provide an additional tool for understanding the biophysics of the 3D genome.","doi":"10.3390/cells9081881","authors":"Singh PB, Belyakin SN, Laktionov PP","authors_abbrev":"Singh PB et al.","pubmed_publication_date":"11 Aug 2020","pubmed_entrez_date":"2020-08-16","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-08-18 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28031482","title":"Involvement of fission yeast Pdc2 in RNA degradation and P-body function.","citation":"RNA 2017 Apr;23(4):493-503","abstract":"In this study we identified Pdc2, the fission yeast ortholog of human Pat1b protein, which forms a complex with Lsm1-7 and plays a role in coupling deadenylation and decapping. The involvement of Pdc2 in RNA degradation and P-body function was also determined. We found that Pdc2 interacts with Dcp2 and is required for decapping in vivo. Although not absolutely essential for P-body assembly, overexpression of Pdc2 enhanced P-body formation even in the absence of Pdc1, the fission yeast functional homolog of human Edc4 protein, indicating that Pdc2 also plays a role in P-body formation. Intriguingly, in the absence of Pdc2, Lsm1 was found to accumulate in the nucleus, suggesting that Pdc2 shuttling between nucleus and cytoplasm plays a role in decreasing the nuclear concentration of Lsm1 to increase Lsm1 in the cytoplasm. Furthermore, unlike other components of P-bodies, the deadenylase Ccr4 did not accumulate in P-bodies in cells growing under favorable conditions and was only recruited to P-bodies after deprivation of glucose in a Pdc2-Lsm1-dependent manner, indicating a function of Pdc2 in cellular response to environmental stress. In supporting this idea,  pdc2  mutants are defective in recovery from glucose starvation with a much longer time to re-enter the cell cycle. In keeping with the notion that Pat1 is a nucleocytoplasmic protein, functioning also in the nucleus, we found that Pdc2 physically and genetically interacts with the nuclear 5'-3' exonuclease Dhp1. A function of Pdc2-Lsm1, in concert with Dhp1, regulating RNA by promoting its decapping/destruction in the nucleus was suggested.","doi":"10.1261/rna.059766.116","authors":"Wang CY, Wang YT, Hsiao WY, Wang SW","authors_abbrev":"Wang CY et al.","pubmed_publication_date":"Apr 2017","pubmed_entrez_date":"2016-12-30","publication_year":"2017","canto_session_key":"4f36d75cf334acbc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shao-Win Wang","canto_first_approved_date":"2017-11-20 16:37:40","canto_approved_date":"2023-01-03 16:50:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-11 06:13:32","canto_added_date":"2016-12-31 01:15:10","annotation_curators":[{"name":"Shao-Win Wang","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":35,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.12c","SPBC4.07c","SPBC19G7.10c","SPNCRNA.1702","SPNCRNA.1705","SPAC20G4.08","SPNCRNA.1706","SPNCRNA.5748","SPAC23C11.02c","SPCC31H12.08c","SPNCRNA.1701","SPNCRNA.1704","SPAC1805.17","SPBC776.09","SPNCRNA.1703","SPBC18E5.11c","SPBC3D6.08c","SPAC19A8.12","SPNCRNA.1708","SPAC17A5.14"],"gene_count":20,"ltp_gene_count":6,"approved_date":"2017-11-20"},{"uniquename":"PMID:28330934","title":"Fundamental mechanisms of telomerase action in yeasts and mammals: understanding telomeres and telomerase in cancer cells.","citation":"Open Biol 2017 Mar;7(3)","abstract":"Aberrant activation of telomerase occurs in 85-90% of all cancers and underpins the ability of cancer cells to bypass their proliferative limit, rendering them immortal. The activity of telomerase is tightly controlled at multiple levels, from transcriptional regulation of the telomerase components to holoenzyme biogenesis and recruitment to the telomere, and finally activation and processivity. However, studies using cancer cell lines and other model systems have begun to reveal features of telomeres and telomerase that are unique to cancer. This review summarizes our current knowledge on the mechanisms of telomerase recruitment and activation using insights from studies in mammals and budding and fission yeasts. Finally, we discuss the differences in telomere homeostasis between normal cells and cancer cells, which may provide a foundation for telomere/telomerase targeted cancer treatments.","doi":"10.1098/rsob.160338","authors":"Armstrong CA, Tomita K","authors_abbrev":"Armstrong CA et al.","pubmed_publication_date":"Mar 2017","pubmed_entrez_date":"2017-03-24","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-03-25 01:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8468345","title":"Unusual nuclear structures in meiotic prophase of fission yeast: a cytological analysis.","citation":"J Cell Biol 1993 Apr;121(2):241-56","abstract":"Earlier results from sectioned nuclei indicating that Schizosaccharomyces pombe does not develop a classical tripartite synaptonemal complex (SC) during meiotic prophase are confirmed by spreading of whole nuclei. The linear elements appearing during prophase I resemble the axial cores (SC precursors) of other organisms. The number of linear elements in haploid, diploid, and tetraploid strains is always higher than the chromosome number, implying that they are not formed continuously along the chromosomes. Time course experiments reveal that the elements appear after DNA replication and form networks and bundles. Later they separate and approximately 24 individual elements with a total length of 34 microns are observed before degradation and meiotic divisions. Parallel staining of DNA reveals changes in nuclear shape during meiotic prophase. Strains with a mei4 mutation are blocked at a late prophase stage. In serial sections we additionally observed a constant arrangement of the spindle pole body, the nucleolus, and the presumptive centromere cluster. Thus, S. pombe manages to recombine and segregate its chromosomes without SC. This might correlate with the absence of crossover interference. We propose a mechanism for chromosome pairing with initial recognition of the homologs at the centromeres and suggest functions of the linear elements in preparation of the chromosomes for meiosis I disjunction. With the spreading technique combined genetic, molecular, and cytological approaches become feasible in S. pombe. This provides an opportunity to study essential meiotic functions in the absence of SCs which may help to clarify the significance of the SC and its components for meiotic chromosome structure and function.","authors":"Bähler J, Wyler T, Loidl J, Kohli J","authors_abbrev":"Bähler J et al.","pubmed_publication_date":"Apr 1993","pubmed_entrez_date":"1993-04-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22001694","title":"Structure of the LSm657 complex: an assembly intermediate of the LSm1-7 and LSm2-8 rings.","citation":"J Mol Biol 2011 Nov 25;414(2):165-76","abstract":"The nuclear LSm2-8 (like Sm) complex and the cytoplasmic LSm1-7 complex play a central role in mRNA splicing and degradation, respectively. The LSm proteins are related to the spliceosomal Sm proteins that form a heteroheptameric ring around small nuclear RNA. The assembly process of the heptameric Sm complex is well established and involves several smaller Sm assembly intermediates. The assembly of the LSm complex, however, is less well studied. Here, we solved the 2.5 Å-resolution structure of the LSm assembly intermediate that contains LSm5, LSm6, and LSm7. The three monomers display the canonical Sm fold and arrange into a hexameric LSm657-657 ring. We show that the order of the LSm proteins within the ring is consistent with the order of the related SmE, SmF, and SmG proteins in the heptameric Sm ring. Nonetheless, differences in RNA binding pockets prevent the prediction of the nucleotide binding preferences of the LSm complexes. Using high-resolution NMR spectroscopy, we confirm that LSm5, LSm6, and LSm7 also assemble into a 60-kDa hexameric ring in solution. With a combination of pull-down and NMR experiments, we show that the LSm657 complex can incorporate LSm23 in order to assemble further towards native LSm rings. Interestingly, we find that the NMR spectra of the LSm57, LSm657-657, and LSm23-657 complexes differ significantly, suggesting that the angles between the LSm building blocks change depending on the ring size of the complex. In summary, our results identify LSm657 as a plastic and functional building block on the assembly route towards the LSm1-7 and LSm2-8 complexes.","doi":"10.1016/j.jmb.2011.09.051","authors":"Mund M, Neu A, Ullmann J, Neu U, Sprangers R","authors_abbrev":"Mund M et al.","pubmed_publication_date":"25 Nov 2011","pubmed_entrez_date":"2011-10-18","publication_year":"2011","canto_session_key":"98265a4966964762","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-20 16:19:06","canto_approved_date":"2023-02-20 16:19:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-20 16:18:12","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC285.12","SPCC1840.10","SPAC2F3.17c","SPCC1620.01c","SPBC20F10.09","SPBC9B6.05c","SPBC30D10.06","SPBC3D6.08c"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2023-02-20","pdb_entries":[{"pdb_id":"3swn","gene_chains":[{"gene_uniquename":"SPBC20F10.09","chain":"A/D/P/S","position":"1-80"},{"gene_uniquename":"SPCC285.12","chain":"C/F/O/R","position":"1-113"},{"gene_uniquename":"SPAC2F3.17c","chain":"B/E/Q/T","position":"1-75"}],"title":"Structure of the LSm657 Complex: An Assembly Intermediate of the LSm1 7 and LSm2 8 Rings","entry_authors":"Mund M,Neu A,Ullmann JL,Neu U,Sprangers R","entry_authors_abbrev":"Mund M et al.","reference_uniquename":"PMID:22001694","experimental_method":"X-ray","resolution":"2.5"}]},{"uniquename":"PMID:10639340","title":"S. pombe sporulation-specific coiled-coil protein Spo15p is localized to the spindle pole body and essential for its modification.","citation":"J Cell Sci 2000 Feb;113 ( Pt 3):545-54","abstract":"Spindle pole bodies in the fission yeast Schizosaccharomyces pombe are required during meiosis, not only for spindle formation but also for the assembly of forespore membranes. The spo15 mutant is defective in the formation of forespore membranes, which develop into spore envelopes. The spo15(+)gene encodes a protein with a predicted molecular mass of 223 kDa, containing potential coiled-coil regions. The spo15 gene disruptant was not lethal, but was defective in spore formation. Northern and western analyses indicated that spo15(+) was expressed not only in meiotic cells but also in vegetative cells. When the spo15-GFP fusion gene was expressed by the authentic spo15 promoter during vegetative growth and sporulation, the fusion protein colocalized with Sad1p, which is a component of spindle pole bodies. Meiotic divisions proceeded in spo15delta cells with kinetics similar to those in wild-type cells. In addition, the morphology of the mitotic and meiotic spindles and the nuclear segregation were normal in spo15delta. Intriguingly, transformation of spindle pole bodies from a punctate to a crescent form prior to forespore membrane formation was not observed in spo15delta cells. We conclude that Spo15p is associated with spindle pole bodies throughout the life cycle and plays an indispensable role in the initiation of spore membrane formation.","authors":"Ikemoto S, Nakamura T, Kubo M, Shimoda C","authors_abbrev":"Ikemoto S et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-01-20","publication_year":"2000","canto_session_key":"f51c10788015bf25","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-26 13:22:42","canto_approved_date":"2019-07-11 22:54:00","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-19 11:41:34","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-26"},{"uniquename":"PMID:20974849","title":"Fission yeast receptor of activated C kinase (RACK1) ortholog Cpc2 regulates mitotic commitment through Wee1 kinase.","citation":"J Biol Chem 2010 Dec 31;285(53):41366-73","abstract":"In the fission yeast Schizosaccharomyces pombe, Wee1-dependent inhibitory phosphorylation of the highly conserved Cdc2/Cdk1 kinase determines the mitotic onset when cells have reached a defined size. The receptor of activated C kinase (RACK1) is a scaffolding protein strongly conserved among eukaryotes which binds to other proteins to regulate multiple processes in mammalian cells, including the modulation of cell cycle progression during G(1)/S transition. We have recently described that Cpc2, the fission yeast ortholog to RACK1, controls from the ribosome the activation of MAPK cascades and the cellular defense against oxidative stress by positively regulating the translation of specific genes whose products participate in the above processes. Intriguingly, mutants lacking Cpc2 display an increased cell size at division, suggesting the existence of a specific cell cycle defect at the G(2)/M transition. In this work we show that protein levels of Wee1 mitotic inhibitor are increased in cells devoid of Cpc2, whereas the levels of Cdr2, a Wee1 inhibitor, are down-regulated in the above mutant. On the contrary, the kinetics of G(1)/S transition was virtually identical both in control and Cpc2-less strains. Thus, our results suggest that in fission yeast Cpc2/RACK1 positively regulates from the ribosome the mitotic onset by modulating both the protein levels and the activity of Wee1. This novel mechanism of translational control of cell cycle progression might be conserved in higher eukaryotes.","doi":"10.1074/jbc.M110.173815","authors":"Núñez A, Franco A, Soto T, Vicente J, Gacto M, Cansado J","authors_abbrev":"Núñez A et al.","pubmed_publication_date":"31 Dec 2010","pubmed_entrez_date":"2010-10-27","publication_year":"2010","canto_session_key":"8c288b3ac3dc79cb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-23 10:09:17","canto_approved_date":"2026-01-31 16:06:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-17 15:44:32","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":44,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPCC18B5.03","SPAC24B11.06c","SPBC11B10.09","SPBC409.07c","SPAC2F7.03c","SPAC644.06c","SPAC24H6.05","SPAC6B12.15"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2024-04-23"},{"uniquename":"PMID:15800213","title":"A computational study of off-target effects of RNA interference.","citation":"Nucleic Acids Res 2005;33(6):1834-47","abstract":"RNA interference (RNAi) is an intracellular mechanism for post-transcriptional gene silencing that is frequently used to study gene function. RNAi is initiated by short interfering RNA (siRNA) of approximately 21 nt in length, either generated from the double-stranded RNA (dsRNA) by using the enzyme Dicer or introduced experimentally. Following association with an RNAi silencing complex, siRNA targets mRNA transcripts that have sequence identity for destruction. A phenotype resulting from this knockdown of expression may inform about the function of the targeted gene. However, 'off-target effects' compromise the specificity of RNAi if sequence identity between siRNA and random mRNA transcripts causes RNAi to knockdown expression of non-targeted genes. The complete off-target effects must be investigated systematically on each gene in a genome by adjusting a group of parameters, which is too expensive to conduct experimentally and motivates a study in silico. This computational study examined the potential for off-target effects of RNAi, employing the genome and transcriptome sequence data of Homo sapiens, Caenorhabditis elegans and Schizosaccharomyces pombe. The chance for RNAi off-target effects proved considerable, ranging from 5 to 80% for each of the organisms, when using as parameter the exact identity between any possible siRNA sequences (arbitrary length ranging from 17 to 28 nt) derived from a dsRNA (range 100-400 nt) representing the coding sequences of target genes and all other siRNAs within the genome. Remarkably, high-sequence specificity and low probability for off-target reactivity were optimally balanced for siRNA of 21 nt, the length observed mostly in vivo. The chance for off-target RNAi increased (although not always significantly) with greater length of the initial dsRNA sequence, inclusion into the analysis of available untranslated region sequences and allowing for mismatches between siRNA and target sequences. siRNA sequences from within 100 nt of the 5' termini of coding sequences had low chances for off-target reactivity. This may be owing to coding constraints for signal peptide-encoding regions of genes relative to regions that encode for mature proteins. Off-target distribution varied along the chromosomes of C.elegans, apparently owing to the use of more unique sequences in gene-dense regions. Finally, biological and thermodynamical descriptors of effective siRNA reduced the number of potential siRNAs compared with those identified by sequence identity alone, but off-target RNAi remained likely, with an off-target error rate of approximately 10%. These results also suggest a direction for future in vivo studies that could both help in calibrating true off-target rates in living organisms and also in contributing evidence toward the debate of whether siRNA efficacy is correlated with, or independent of, the target molecule. In summary, off-target effects present a real but not prohibitive concern that should be considered for RNAi experiments.","authors":"Qiu S, Adema CM, Lane T","authors_abbrev":"Qiu S et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-04-01","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9223296","title":"The Schizosaccharomyces pombe spindle checkpoint protein mad2p blocks anaphase and genetically interacts with the anaphase-promoting complex.","citation":"Proc Natl Acad Sci U S A 1997 Jul 22;94(15):7965-70","abstract":"The spindle checkpoint monitors mitotic spindle integrity and the attachment of kinetochores to the spindle. Upon sensing a defect the checkpoint blocks cell cycle progression and thereby prevents chromosome missegregation. Previous studies in budding yeast show that the activated spindle checkpoint inhibits the onset of anaphase by an unknown mechanism. One possible target of the spindle checkpoint is anaphase promoting complex (APC), which controls all postmetaphase events that are blocked by spindle checkpoint activation. We have isolated mad2, a spindle checkpoint component in fission yeast, and shown that mad2 overexpression activates the checkpoint and causes a cell cycle arrest at the metaphase-to-anaphase transition. In addition to the observation that mad2-induced arrest can be partially relieved by mitosis-promoting factor inactivation, we present genetic evidence consistent with the hypothesis that the spindle checkpoint imposes a cell cycle arrest by inhibiting APC-dependent proteolysis.","authors":"He X, Patterson TE, Sazer S","authors_abbrev":"He X et al.","pubmed_publication_date":"22 Jul 1997","pubmed_entrez_date":"1997-07-22","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F12.15c","SPBC20F10.06","SPBC26H8.07c","SPAC17C9.01c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:9552418","title":"Myt1: a Wee1-type kinase that phosphorylates Cdc2 on residue Thr14.","citation":"Prog Cell Cycle Res 1997;3:233-40","abstract":"Most somatic cell division cycles contain a gap period (G2 phase) between the completion of DNA synthesis and the initiation of mitosis. This delay of mitotic entry is controlled, at least in part, by the repression of Cdc2 kinase activity by the phosphorylation of two conserved residues (Thr14 and Tyr15) within the ATP-binding pocket of the Cdc2 catalytic subunit. The kinases responsible for these two phosphorylation events include the Myt1 and Wee1 kinases, which phosphorylate Cdc2 on Thr14 and Tyr15, respectively. In this discussion, we summarise our current knowledge of the Myt1 kinase and its regulation of Cdc2 kinase activity during the G2-to -M phase transition.","authors":"Fattaey A, Booher RN","authors_abbrev":"Fattaey A et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2450045","title":"Electroporation: high frequency of occurrence of a transient high-permeability state in erythrocytes and intact yeast.","citation":"FEBS Lett 1988 Feb 29;229(1):30-4","abstract":"We present the first determinations of population distributions of macromolecule uptake due to electroporation, the percentage of cells which participate and, for the yeast, the subpopulation of cells whose membranes exhibit significant recovery following macromolecule uptake. Flow cytometry is used to measure the uptake of a first test molecule (green fluorescence, FITC-dextran; 70 kDa) and also, for the yeast, the subsequent uptake of a second, much smaller, test molecule (red fluorescence, propidium iodide; 660 Da), which provides a measure of membrane recovery. A dramatic 20% (erythrocytes) to 75% (intact Schizosaccharomyces pombe) of cells can take up the first test molecule within 5 min of a pulse.","authors":"Weaver JC, Harrison GI, Bliss JG, Mourant JR, Powell KT","authors_abbrev":"Weaver JC et al.","pubmed_publication_date":"29 Feb 1988","pubmed_entrez_date":"1988-02-29","publication_year":"1988","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31936815","title":" Schizosaccharomyces pombe  Assays to Study Mitotic Recombination Outcomes.","citation":"Genes (Basel) 2020 Jan 10;11(1)","abstract":"The fission yeast- Schizosaccharomyces pombe -has emerged as a powerful tractable system for studying DNA damage repair. Over the last few decades, several powerful in vivo genetic assays have been developed to study outcomes of mitotic recombination, the major repair mechanism of DNA double strand breaks and stalled or collapsed DNA replication forks. These assays have significantly increased our understanding of the molecular mechanisms underlying the DNA damage response pathways. Here, we review the assays that have been developed in fission yeast to study mitotic recombination.","doi":"10.3390/genes11010079","authors":"Hylton HM, Lucas BE, Petreaca RC","authors_abbrev":"Hylton HM et al.","pubmed_publication_date":"10 Jan 2020","pubmed_entrez_date":"2020-01-16","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9932460","title":"DNA damage and replication checkpoints in the fission yeast, Schizosaccharomyces pombe.","citation":"Prog Nucleic Acid Res Mol Biol 1999;62:369-95","abstract":"Eukaryotic organisms have developed an array of mechanisms for minimizing the consequences of damage to their DNA molecules and the consequences of interference with their DNA replication. Among these mechanisms are the DNA damage and replication checkpoints, which inhibit passage from one cell cycle stage to the next when DNA is damaged or replication is incomplete. Studies of these checkpoints in the fission yeast, Schizosaccharomyces pombe, complement studies in other organisms and provide valuable insight into the nature of the proteins responsible for these checkpoints and how such proteins may function.","authors":"Huberman JA","authors_abbrev":"Huberman JA","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-02-05","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15972699","title":"Oxygen sensing: getting pumped by sterols.","citation":"Sci STKE 2005 Jun 21;2005(289):pe30","abstract":"Oxygen plays a pivotal role in the maintenance of life for all eukaryotes, with the exception of strict anaerobes. Eukaryotes have developed mechanisms to sense and respond to decreased oxygen levels. How eukaryotes sense oxygen is still not fully understood. What is (or are) the oxygen sensor(s)? This question has vital physiological and pathophysiological implications, because all living aerobic organisms have adaptive mechanisms to maintain oxygen homeostasis. A recent report describes a novel eukaryotic oxygen-sensing mechanism in the fission yeast Schizosaccharomyces pombe, involving the depletion of sterols as a trigger to induce gene expression in response to decreased oxygen levels. It is not yet clear whether this mechanism is involved in the mammalian response to hypoxia, possibly in conjunction with activation of one or both of the hypoxia-inducible factor (HIF-1 or HIF-2) transcription factors.","authors":"Emerling BM, Chandel NS","authors_abbrev":"Emerling BM et al.","pubmed_publication_date":"21 Jun 2005","pubmed_entrez_date":"2005-06-24","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27053664","title":"Synergistic role of fission yeast Alp16GCP6 and Mzt1MOZART1 in γ-tubulin complex recruitment to mitotic spindle pole bodies and spindle assembly.","citation":"Mol Biol Cell 2016 Jun 01;27(11):1753-63","abstract":"In fission yeast, γ-tubulin ring complex (γTuRC)-specific components Gfh1(GCP4), Mod21(GCP5), and Alp16(GCP6) are nonessential for cell growth. Of these deletion mutants, only alp16Δ shows synthetic lethality with temperature-sensitive mutants of Mzt1(MOZART1), a component of the γTuRC required for recruitment of the complex to microtubule-organizing centers. γ-Tubulin small complex levels at mitotic spindle pole bodies (SPBs, the centrosome equivalent in fungi) and microtubule levels for preanaphase spindles are significantly reduced in alp16Δ cells but not in gfh1Δ or mod21Δ cells. Furthermore, alp16Δ cells often form monopolar spindles and frequently lose a minichromosome when the spindle assembly checkpoint is inactivated. Alp16(GCP6) promotes Mzt1-dependent γTuRC recruitment to mitotic SPBs and enhances spindle microtubule assembly in a manner dependent on its expression levels. Gfh1(GCP4) and Mod21(GCP5) are not required for Alp16(GCP6)-dependent γTuRC recruitment. Mzt1 has an additional role in the activation of the γTuRC for spindle microtubule assembly. The ratio of Mzt1 to γTuRC levels for preanaphase spindles is higher than at other stages of the cell cycle. Mzt1 overproduction enhances spindle microtubule assembly without affecting γTuRC levels at mitotic SPBs. We propose that Alp16(GCP6) and Mzt1 act synergistically for efficient bipolar spindle assembly to ensure faithful chromosome segregation.","doi":"10.1091/mbc.E15-08-0577","authors":"Masuda H, Toda T","authors_abbrev":"Masuda H et al.","pubmed_publication_date":"01 Jun 2016","pubmed_entrez_date":"2016-04-08","publication_year":"2016","canto_session_key":"4dc2c4129add9a12","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-13 18:14:15","canto_approved_date":"2025-04-18 16:14:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-13 17:56:38","canto_added_date":"2016-04-09 00:15:13","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":32,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.06c","SPCC4G3.19","SPBC211.06","SPAC806.08c","SPAC9G1.15c","SPBC20F10.06","SPBC365.15","SPBC800.05c"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2024-03-13"},{"uniquename":"GO_REF:0000071","title":"Representation of response to and cellular response to a chemical as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the response to and cellular response to a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom templates are \"GO:0050896 and 'has input' some X\" (response to) and \"GO:0070887 and 'has input' some X\" (cellular response to), where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16162496","title":"Discovery of a gene family critical to wyosine base formation in a subset of phenylalanine-specific transfer RNAs.","citation":"J Biol Chem 2005 Nov 11;280(45):37616-22","abstract":"A large number of post-transcriptional base modifications in transfer RNAs have been described (Sprinzl, M., Horn, C., Brown, M., Ioudovitch, A., and Steinberg, S. (1998) Nucleic Acids Res. 26, 148-153). These modifications enhance and expand tRNA function to increase cell viability. The intermediates and genes essential for base modifications in many instances remain unclear. An example is wyebutosine (yW), a fluorescent tricyclic modification of an invariant guanosine situated on the 3'-side of the tRNA(Phe) anticodon. Although biosynthesis of yW involves several reaction steps, only a single pathway-specific enzyme has been identified (Kalhor, H. R., Penjwini, M., and Clarke, S. (2005) Biochem. Biophys. Res. Commun. 334, 433-440). We used comparative genomics analysis to identify a cluster of orthologous groups (COG0731) of wyosine family biosynthetic proteins. Gene knock-out and complementation studies in Saccharomyces cerevisiae established a role for YPL207w, a COG0731 ortholog that encodes an 810-amino acid polypeptide. Further analysis showed the accumulation of N(1)-methylguanosine (m(1)G(37)) in tRNA from cells bearing a YPL207w deletion. A similar lack of wyosine base and build-up of m(1)G(37) is seen in certain mammalian tumor cell lines. We proposed that the 810-amino acid COG0731 polypeptide participates in converting tRNA(Phe)-m(1)G(37) to tRNA(Phe)-yW.","authors":"Waas WF, de Crécy-Lagard V, Schimmel P","authors_abbrev":"Waas WF et al.","pubmed_publication_date":"11 Nov 2005","pubmed_entrez_date":"2005-09-16","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39276354","title":"Cross-regulations of two connected domains form a mechanical circuit for steady force transmission during clathrin-mediated endocytosis.","citation":"Cell Rep 2024 Sep 12;43(9):114725","abstract":"Mechanical forces are transmitted from the actin cytoskeleton to the membrane during clathrin-mediated endocytosis (CME) in the fission yeast Schizosaccharomyces pombe. End4p directly transmits force in CME by binding to both the membrane (through the AP180 N-terminal homology [ANTH] domain) and F-actin (through the talin-HIP1/R/Sla2p actin-tethering C-terminal homology [THATCH] domain). We show that 7 pN force is required for stable binding between THATCH and F-actin. We also characterized a domain in End4p, Rend (rod domain in End4p), that resembles R12 of talin. Membrane localization of Rend primes the binding of THATCH to F-actin, and force-induced unfolding of Rend at 15 pN terminates the transmission of force. We show that the mechanical properties (mechanical stability, unfolding extension, hysteresis) of Rend and THATCH are tuned to form a circuit for the initiation, transmission, and termination of force between the actin cytoskeleton and membrane. The mechanical circuit by Rend and THATCH may be conserved and coopted evolutionarily in cell adhesion complexes.","doi":"10.1016/j.celrep.2024.114725","authors":"Ren Y, Yang J, Fujita B, Zhang Y, Berro J","authors_abbrev":"Ren Y et al.","pubmed_publication_date":"12 Sep 2024","pubmed_entrez_date":"2024-09-14","publication_year":"2024","canto_session_key":"aaac35de67e48eb3","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-09-15 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC688.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9427389","title":"Cloning of SEC61 homologues from Schizosaccharomyces pombe and Yarrowia lipolytica reveals the extent of functional conservation within this core component of the ER translocation machinery.","citation":"J Cell Sci 1997 Nov;110 ( Pt 21):2715-27","abstract":"The Sec61 protein is required for protein translocation across the ER membrane in both yeast and mammals and is found in close association with polypeptides during their membrane transit. In Saccharomyces cerevisiae Sec61p is essential for viability and the extent of sequence similarity between the yeast and mammalian proteins (55% sequence identity) suggests that the role of Sec61p in the translocation mechanism is likely to be conserved. In order to further our understanding of the structure and function of Sec61p we have cloned homologues from both Schizosaccharomyces pombe and Yarrowia lipolytica. The S. pombe gene comprises six exons encoding a 479 residue protein which we have immunolocalised to the endoplasmic reticulum. Sequence comparisons reveal that S. pombe Sec61p is 58.6% identical to that of S. cerevisiae. The deduced amino acid sequence of the Y. lipolytica protein shares 68.8% sequence identity with S. cerevisiae Sec61p. Gene disruption studies have shown that the SEC61 is required for viability in both S. pombe and Y. lipolytica demonstrating that the essential nature of this protein is not unique to S. cerevisiae. Moreover, heterologous complementation studies indicate that the Y. lipolytica SEC61 gene can complement a null mutation in S. cerevisiae. Sequence comparisons between the various eukaryotic Sec61p homologues reveal a number of highly conserved domains, including several transmembrane sequences and the majority of cytosolic loops. These comparisons will provide an important framework for the detailed analysis of interactions between Sec61p and other components of the translocation machinery and between Sec61p and translocating polypeptide chains.","authors":"Broughton J, Swennen D, Wilkinson BM, Joyet P, Gaillardin C, Stirling CJ","authors_abbrev":"Broughton J et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-01-14","publication_year":"1997","canto_session_key":"ae590c5c93d4cceb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-20 16:26:40","canto_approved_date":"2021-04-13 16:43:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-22 18:10:06","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC354.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-20"},{"uniquename":"PMID:2195549","title":"Human homolog of fission yeast cdc25 mitotic inducer is predominantly expressed in G2.","citation":"Proc Natl Acad Sci U S A 1990 Jul;87(13):5139-43","abstract":"Entry into mitosis during the somatic cell cycle is regulated in response to signals that monitor the completion of DNA replication, the integrity of the nuclear genome, and, possibly, the increase in cellular mass during the cell cycle. It has been postulated that the operation of this cell cycle control involves the gradual accumulation of rate-limiting mitotic inducers, which trigger nuclear division when their cellular concentration reaches a critical level. We have cloned a human gene, which we call CDC25, whose product may function as a mitotic inducer. This human gene encodes a protein with a predicted molecular mass of 53,000 daltons whose C-terminal domain shares about 37% sequence identity with the fission yeast cdc25+ mitotic inducer. The human CDC25 gene rescues the defect of a fission yeast temperature-sensitive (ts) cdc25ts mutant that is unable to initiate mitosis. In HeLa cells CDC25 mRNA levels are very low in G1 and increase at least 4-fold as cells progress towards M phase. These data suggest that in human cells, as in fission yeast, the accumulation of CDC25 mitotic inducer during G2 may play a key role in regulating the timing of mitosis.","authors":"Sadhu K, Reed SI, Richardson H, Russell P","authors_abbrev":"Sadhu K et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_session_key":"a8f47119570db1e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 13:19:36","canto_session_submitted_date":"2012-03-03 13:19:18","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:27862378","title":"Identification of Compounds that Selectively Stabilize Specific G-Quadruplex Structures by Using a Thioflavin T-Displacement Assay as a Tool.","citation":"Chemistry 2016 Dec 23;22(52):18932-18943","abstract":"Small molecules are used in the G-quadruplex (G4) research field in vivo and in vitro, and there are increasing demands for ligands that selectively stabilize different G4 structures. Thioflavin T (ThT) emits an enhanced fluorescence signal when binding to G4 structures. Herein, we show that ThT can be competitively displaced by the binding of small molecules to G4 structures and develop a ThT-displacement high-throughput screening assay to find novel and selective G4-binding compounds. We screened approximately 28 000 compounds by using three different G4 structures and identified eight novel G4 binders. Analysis of the structural conformation and stability of the G4 structures in presence of these compounds demonstrated that the four compounds enhance the thermal stabilization of the structures without affecting their structural conformation. In addition, all four compounds also increased the G4-structure block of DNA synthesis by Taq DNA polymerase. Also, two of these compounds showed selectivity between certain Schizosaccharomyces pombe G4 structures, thus suggesting that these compounds or their analogues can be used as selective tools for G4 DNA studies.","doi":"10.1002/chem.201603463","authors":"Jamroskovic J, Livendahl M, Eriksson J, Chorell E, Sabouri N","authors_abbrev":"Jamroskovic J et al.","pubmed_publication_date":"23 Dec 2016","pubmed_entrez_date":"2016-11-19","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-21 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15371329","title":"A single Argonaute protein mediates both transcriptional and posttranscriptional silencing in Schizosaccharomyces pombe.","citation":"Genes Dev 2004 Oct 01;18(19):2359-67","abstract":"The Schizosaccharomyces pombe genome encodes only one of each of the three major classes of proteins implicated in RNA silencing: Dicer (Dcr1), RNA-dependent RNA polymerase (RdRP; Rdp1), and Argonaute (Ago1). These three proteins are required for silencing at centromeres and for the initiation of transcriptionally silent heterochromatin at the mating-type locus. Here, we show that the introduction of a double-stranded RNA (dsRNA) hairpin corresponding to a green fluorescent protein (GFP) transgene triggers classical RNA interference (RNAi) in S. pombe. That is, GFP silencing triggered by dsRNA reflects a change in the steady-state concentration of GFP mRNA, but not in the rate of GFP transcription. RNAi in S. pombe requires dcr1, rdp1, and ago1, but does not require chp1, tas3, or swi6, genes required for transcriptional silencing. Thus, the RNAi machinery in S. pombe can direct both transcriptional and posttranscriptional silencing using a single Dicer, RdRP, and Argonaute protein. Our findings suggest that these three proteins fulfill a common biochemical function in distinct siRNA-directed silencing pathways.","authors":"Sigova A, Rhind N, Zamore PD","authors_abbrev":"Sigova A et al.","pubmed_publication_date":"01 Oct 2004","pubmed_entrez_date":"2004-09-17","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26704981","title":"Involvement of condensin-directed gene associations in the organization and regulation of chromosome territories during the cell cycle.","citation":"Nucleic Acids Res 2016 May 05;44(8):3618-28","abstract":"Chromosomes are not randomly disposed in the nucleus but instead occupy discrete sub-nuclear domains, referred to as chromosome territories. The molecular mechanisms that underlie the formation of chromosome territories and how they are regulated during the cell cycle remain largely unknown. Here, we have developed two different chromosome-painting approaches to address how chromosome territories are organized in the fission yeast model organism. We show that condensin frequently associates RNA polymerase III-transcribed genes (tRNA and 5S rRNA) that are present on the same chromosomes, and that the disruption of these associations by condensin mutations significantly compromises the chromosome territory arrangement. We also find that condensin-dependent intra-chromosomal gene associations and chromosome territories are co-regulated during the cell cycle. For example, condensin-directed gene associations occur to the least degree during S phase, with the chromosomal overlap becoming largest. In clear contrast, condensin-directed gene associations become tighter in other cell-cycle phases, especially during mitosis, with the overlap between the different chromosomes being smaller. This study suggests that condensin-driven intra-chromosomal gene associations contribute to the organization and regulation of chromosome territories during the cell cycle.","doi":"10.1093/nar/gkv1502","authors":"Iwasaki O, Corcoran CJ, Noma K","authors_abbrev":"Iwasaki O et al.","pubmed_publication_date":"05 May 2016","pubmed_entrez_date":"2015-12-26","publication_year":"2016","canto_session_key":"04dc14ffe9dc92b0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-12-27 01:19:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC146.03c","SPBC336.07"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:31509478","title":"The intrinsically disordered region of the cytokinetic F-BAR protein Cdc15 performs a unique essential function in maintenance of cytokinetic ring integrity.","citation":"Mol Biol Cell 2019 Oct 15;30(22):2790-2801","abstract":"Successful separation of two daughter cells (i.e., cytokinesis) is essential for life. Many eukaryotic cells divide using a contractile apparatus called the cytokinetic ring (CR) that associates dynamically with the plasma membrane (PM) and generates force that contributes to PM ingression between daughter cells. In  Schizosaccharomyces pombe,  important membrane-CR scaffolds include the paralogous F-BAR proteins Cdc15 and Imp2. Their conserved protein structure consists of the archetypal F-BAR domain linked to an SH3 domain by an intrinsically disordered region (IDR). Functions have been assigned to the F-BAR and SH3 domains. In this study we probed the function of the central IDR. We found that the IDR of Cdc15 is essential for viability and cannot be replaced by that of Imp2, whereas the F-BAR domain of Cdc15 can be swapped with several different F-BAR domains, including that of Imp2. Deleting part of the IDR results in CR defects and abolishes calcineurin phosphatase localization to the CR. Together these results indicate that Cdc15's IDR has a nonredundant essential function that coordinates regulation of CR architecture.","doi":"10.1091/mbc.E19-06-0314","authors":"Mangione MC, Snider CE, Gould KL","authors_abbrev":"Mangione MC et al.","pubmed_publication_date":"15 Oct 2019","pubmed_entrez_date":"2019-09-12","publication_year":"2019","canto_session_key":"a75a0c4b091bc54c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"MariaSanta Mangione","canto_first_approved_date":"2020-01-07 16:27:02","canto_approved_date":"2023-12-22 10:22:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-31 21:59:30","canto_added_date":"2019-09-13 00:15:04","annotation_curators":[{"name":"MariaSanta Mangione","community_curator":true,"annotation_count":26,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPAC15A10.08","SPAC1F5.04c","SPBC1778.06c","SPAC20G4.06c","SPAC20G8.05c","SPCC4B3.15","SPAC6F6.08c","SPAC12B10.07","SPAC926.03","SPBP4H10.04","SPAC4A8.15c","SPCC794.08","SPBC4F6.12"],"gene_count":14,"ltp_gene_count":12,"approved_date":"2020-01-07"},{"uniquename":"PMID:23389339","title":"Metabolic fluxes in Schizosaccharomyces pombe grown on glucose and mixtures of glycerol and acetate.","citation":"Appl Microbiol Biotechnol 2013 Jun;97(11):5013-26","abstract":"Growth on glycerol has already been a topic of research for several yeast species, and recent publications deal with the regulatory mechanisms of glycerol assimilation by the fission yeast Schizosaccharomyces pombe. We investigated glycerol metabolism of S. pombe from a physiological point of view, characterizing growth and metabolism on a mixture of glycerol and acetate and comparing it to growth on glucose under respirative growth conditions in chemostat experiments. On glycerol/acetate mixtures, the cells grew with a maximum specific growth rate of 0.11 h(-1) where 46 % of the carbon was channeled into biomass and the key fermentation product ethanol was not detectable. (13)C-assisted metabolic flux analysis resolved substrate distributions through central carbon metabolism, proving that glycerol is used as a precursor for glycolysis, gluconeogenesis, and the pentose phosphate pathway, while acetate enters the tricarboxylic acid cycle via acetyl-CoA. Considering compartmentalization between cytosol and mitochondria in the metabolic model, we found compartmentalization of biosynthesis for the amino acids aspartate and leucine. Balancing of redox cofactors revealed an abundant production of cytosolic NADPH that must be finally regenerated via the respiratory chain shown by the simulated and measured CO2 production and oxygen consumption rates which were in good agreement.","doi":"10.1007/s00253-013-4718-z","authors":"Klein T, Heinzle E, Schneider K","authors_abbrev":"Klein T et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-02-08","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19298215","title":"Effectiveness of Cymbopogon citratus L. essential oil to inhibit the growth of some filamentous fungi and yeasts.","citation":"J Med Food 2009 Feb;12(1):193-7","abstract":"Lemon grass (Cymbopogon citratus L.) oil has been known as having therapeutic and antibacterial properties, and its antifungal activity is currently the subject of renewed interest. This study aimed to verify the effectivenesses of C. citratus essential oil to inhibit the growth/survival of some fungi (Alternaria alternata, Aspergillus niger, Fusarium oxysporum, and Penicillium roquefortii) and yeasts (Candida albicans, Candida oleophila, Hansenula anomala, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Saccharomyces uvarum, and Metschnikowia fructicola). C. citratus essential oil showed effectiveness in inhibiting the growth of all fungi by disc diffusion and broth dilution bioassay. Minimum inhibitory and minimum fungicidal concentrations between 0.062 and 20 microL/mL were determined. The Clinical and Laboratory Standards Institute agar-based method was also applied for A. niger and C. albicans. Data show the strong antifungal properties of lemon grass oil (C. citratus) in vitro.","doi":"10.1089/jmf.2008.0108","authors":"Irkin R, Korukluoglu M","authors_abbrev":"Irkin R et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2009-03-21","publication_year":"2009","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17827346","title":"Multiple modes of chromatin configuration at natural meiotic recombination hot spots in fission yeast.","citation":"Eukaryot Cell 2007 Nov;6(11):2072-80","abstract":"The ade6-M26 meiotic recombination hot spot of fission yeast is defined by a cyclic AMP-responsive element (CRE)-like heptanucleotide sequence, 5'-ATGACGT-3', which acts as a binding site for the Atf1/Pcr1 heterodimeric transcription factor required for hot spot activation. We previously demonstrated that the local chromatin around the M26 sequence motif alters to exhibit higher sensitivity to micrococcal nuclease before the initiation of meiotic recombination. In this study, we have examined whether or not such alterations in chromatin occur at natural meiotic DNA double-strand break (DSB) sites in Schizosaccharomyces pombe. At one of the most prominent DSB sites, mbs1 (meiotic break site 1), the chromatin structure has a constitutively accessible configuration at or near the DSB sites. The establishment of the open chromatin state and DSB formation are independent of the CRE-binding transcription factor, Atf1. Analysis of the chromatin configuration at CRE-dependent DSB sites revealed both differences from and similarities to mbs1. For example, the tdh1+ locus, which harbors a CRE consensus sequence near the DSB site, shows a meiotically induced open chromatin configuration, similar to ade6-M26. In contrast, the cds1+ locus is similar to mbs1 in that it exhibits a constitutive open configuration. Importantly, Atf1 is required for the open chromatin formation in both tdh1+ and cds1+. These results suggest that CRE-dependent meiotic chromatin changes are intrinsic processes related to DSB formation in fission yeast meiosis. In addition, the results suggest that the chromatin configuration in natural meiotic recombination hot spots can be classified into at least three distinct categories: (i) an Atf1-CRE-independent constitutively open chromatin configuration, (ii) an Atf1-CRE-dependent meiotically induced open chromatin configuration, and (iii) an Atf1-CRE-dependent constitutively open chromatin configuration.","authors":"Hirota K, Steiner WW, Shibata T, Ohta K","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-09-11","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20705471","title":"Differential regulation of unconventional fission yeast myosins via the actin track.","citation":"Curr Biol 2010 Aug 24;20(16):1423-31","abstract":"Fission yeast possesses three unconventional myosins: Myo1p (a class I myosin that functions at endocytic actin patches) and Myo51p and Myo52p (class V myosins that function at contractile rings and actin cables, respectively). Here we used a combination of in vivo and in vitro approaches to investigate how changes in the actin track influence the motor activity and spatial regulation of these myosins.\nWe optimized the isolation of Myo1p, Myo51p, and Myo52p. All three myosins exhibited robust motor activity in ATPase and actin filament gliding assays. However, decoration of actin with tropomyosin differentially regulates the activity of these motors. Tropomyosin inhibits Myo1p by blocking its ability to form productive associations with actin filaments, whereas tropomyosin increases the actin affinity and ATPase activity of Myo51p and Myo52p. The actin filament crosslinking protein fimbrin rescues Myo1p motor activity by displacing tropomyosin from actin filaments. Consistent with our in vitro findings, fimbrin and tropomyosin have opposing effects on Myo1p function at actin patches. Defects in tropomyosin function led to shorter Myo1p patch lifetimes, whereas loss of fimbrin extended Myo1p lifetimes. Furthermore, defects in tropomyosin function decreased the efficiency of Myo52p-directed motility along actin cables in the cell.\nTropomyosin promotes myosin-V motility along actin cables. Accumulation of fimbrin at actin patches relieves Myo1p from tropomyosin-mediated inhibition, ensuring maximal myosin-I motor activity at these sites. Thus, spatial regulation of myosin motor function is in part controlled by specific changes in the composition of the actin track.","doi":"10.1016/j.cub.2010.07.026","authors":"Clayton JE, Sammons MR, Stark BC, Hodges AR, Lord M","authors_abbrev":"Clayton JE et al.","pubmed_publication_date":"24 Aug 2010","pubmed_entrez_date":"2010-08-14","publication_year":"2010","canto_session_key":"14d6b12f621eebfe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-12 15:56:15","canto_approved_date":"2022-09-17 19:10:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-12 15:56:09","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.06c","SPAC27F1.02c","SPBC146.13c","SPBC2D10.14c","SPCC1919.10c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-07-12"},{"uniquename":"PMID:33263569","title":"The X-ray crystal structure of the N-terminal domain of Ssr4, a Schizosaccharomyces pombe chromatin-remodelling protein.","citation":"Acta Crystallogr F Struct Biol Commun 2020 Dec 01;76(Pt 12):583-589","abstract":"Ssr4 is a yeast protein from Schizosaccharomyces pombe and is an essential part of the chromatin-remodelling [SWI/SNF and RSC (remodelling the structure of chromatin)] complexes found in S. pombe. These complexes (or their homologues) regulate gene expression in eukaryotic organisms, affecting a large number of genes both positively and negatively. The downstream effects are seen in development, and in humans have implications for disease such as cancer. The chromatin structure is altered by modifying the DNA-histone contacts, thus opening up or closing down sections of DNA to specific transcription factors that regulate the transcription of genes. The Ssr4 sequence has little homology to other sequences in the Protein Data Bank, so the structure was solved using an iodine derivative with SAD phasing. The structure of the N-terminal domain is an antiparallel β-sheet of seven strands with α-helices on one side and random coil on the other. The structure is significantly different to deposited structures and was used as a target in the most recent Critical Assessment of Techniques for Protein Structure Prediction (CASP; https://predictioncenter.org/) competition.","doi":"10.1107/S2053230X20015216","authors":"Newman J, Nebl T, Van H, Peat TS","authors_abbrev":"Newman J et al.","pubmed_publication_date":"01 Dec 2020","pubmed_entrez_date":"2020-12-02","publication_year":"2020","canto_session_key":"0db4f358afd43973","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-12-11 17:02:50","canto_approved_date":"2020-12-11 17:02:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-11 17:02:38","canto_added_date":"2020-12-04 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP23A10.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-12-11","pdb_entries":[{"pdb_id":"7k7v","gene_chains":[{"gene_uniquename":"SPBP23A10.05","chain":"A","position":"2-180"}],"title":"The X-ray crystal structure of SSR4, an S. pombe chromatin remodelling protein: iodide derivative","entry_authors":"Peat TS,Newman J","entry_authors_abbrev":"Peat TS et al.","reference_uniquename":"PMID:33263569","experimental_method":"X-ray","resolution":"1.882"},{"pdb_id":"7k82","gene_chains":[{"gene_uniquename":"SPBP23A10.05","chain":"A","position":"2-180"}],"title":"The X-ray crystal structure of SSR4, an S. pombe chromatin remodelling protein: sulfur SAD","entry_authors":"Peat TS,Newman J","entry_authors_abbrev":"Peat TS et al.","reference_uniquename":"PMID:33263569","experimental_method":"X-ray","resolution":"2.1"},{"pdb_id":"7k7w","gene_chains":[{"gene_uniquename":"SPBP23A10.05","chain":"A","position":"2-180"}],"title":"The X-ray crystal structure of SSR4, an S. pombe chromatin remodelling protein: native","entry_authors":"Peat TS,Newman J","entry_authors_abbrev":"Peat TS et al.","reference_uniquename":"PMID:33263569","experimental_method":"X-ray","resolution":"1.77"}]},{"uniquename":"PMID:17684567","title":"Global profiling of DNA replication timing and efficiency reveals that efficient replication/firing occurs late during S-phase in S. pombe.","citation":"PLoS One 2007 Aug 08;2(8):e722","abstract":"During S. pombe S-phase, initiation of DNA replication occurs at multiple sites (origins) that are enriched with AT-rich sequences, at various times. Current studies of genome-wide DNA replication profiles have focused on the DNA replication timing and origin location. However, the replication and/or firing efficiency of the individual origins on the genomic scale remain unclear.\nUsing the genome-wide ORF-specific DNA microarray analysis, we show that in S. pombe, individual origins fire with varying efficiencies and at different times during S-phase. The increase in DNA copy number plotted as a function of time is approximated to the near-sigmoidal model, when considering the replication start and end timings at individual loci in cells released from HU-arrest. Replication efficiencies differ from origin to origin, depending on the origin's firing efficiency. We have found that DNA replication is inefficient early in S-phase, due to inefficient firing at origins. Efficient replication occurs later, attributed to efficient but late-firing origins. Furthermore, profiles of replication timing in cds1Delta cells are abnormal, due to the failure in resuming replication at the collapsed forks. The majority of the inefficient origins, but not the efficient ones, are found to fire in cds1Delta cells after HU removal, owing to the firing at the remaining unused (inefficient) origins during HU treatment.\nTaken together, our results indicate that efficient DNA replication/firing occurs late in S-phase progression in cells after HU removal, due to efficient late-firing origins. Additionally, checkpoint kinase Cds1p is required for maintaining the efficient replication/firing late in S-phase. We further propose that efficient late-firing origins are essential for ensuring completion of DNA duplication by the end of S-phase.","authors":"Eshaghi M, Karuturi RK, Li J, Chu Z, Liu ET, Liu J","authors_abbrev":"Eshaghi M et al.","pubmed_publication_date":"08 Aug 2007","pubmed_entrez_date":"2007-08-09","publication_year":"2007","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7916658","title":"The fission yeast cdc18+ gene product couples S phase to START and mitosis.","citation":"Cell 1993 Jul 30;74(2):371-82","abstract":"Commitment to the cell cycle in fission yeast requires the function of the cdc10+ transcriptional activator at START. The product of the cdc18+ gene is a major downstream target of cdc10+, and transcription of cdc18+ is activated by cdc10+ during passage through START. The cdc18+ function is required for entry into S phase. In addition, the product of the cdc18+ gene is part of the checkpoint control that prevents mitosis from occurring until S phase is completed. Thus, cdc18+ plays a key role in coupling S phase to START and mitosis.","authors":"Kelly TJ, Martin GS, Forsburg SL, Stephen RJ, Russo A, Nurse P","authors_abbrev":"Kelly TJ et al.","pubmed_publication_date":"30 Jul 1993","pubmed_entrez_date":"1993-07-30","publication_year":"1993","canto_session_key":"277ac92c6cd07f54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-02-01 16:22:22","canto_approved_date":"2019-10-04 14:31:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-02-01 16:22:10","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPBC336.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-02-01"},{"uniquename":"PMID:18387313","title":"Quantitative 3-D imaging of eukaryotic cells using soft X-ray tomography.","citation":"J Struct Biol 2008 Jun;162(3):380-6","abstract":"Imaging has long been one of the principal techniques used in biological and biomedical research. Indeed, the field of cell biology grew out of the first electron microscopy images of organelles in a cell. Since this landmark event, much work has been carried out to image and classify the organelles in eukaryotic cells using electron microscopy. Fluorescently labeled organelles can now be tracked in live cells, and recently, powerful light microscope techniques have pushed the limit of optical resolution to image single molecules. In this paper, we describe the use of soft X-ray tomography, a new tool for quantitative imaging of organelle structure and distribution in whole, fully hydrated eukaryotic Schizosaccharomyces pombe cells. In addition to imaging intact cells, soft X-ray tomography has the advantage of not requiring the use of any staining or fixation protocols--cells are simply transferred from their growth environment to a sample holder and immediately cryofixed. In this way the cells can be imaged in a near native state. Soft X-ray tomography is also capable of imaging relatively large numbers of cells in a short period of time, and is therefore a technique that has the potential to produce information on organelle morphology from statistically significant numbers of cells.","doi":"10.1016/j.jsb.2008.02.003","authors":"Parkinson DY, McDermott G, Etkin LD, Le Gros MA, Larabell CA","authors_abbrev":"Parkinson DY et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-05","publication_year":"2008","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17530441","title":"Molecular cloning, characterization and regulation of a peroxiredoxin gene from Schizosaccharomyces pombe.","citation":"Mol Biol Rep 2008 Sep;35(3):387-95","abstract":"A gene encoding a putative peroxiredoxin (Prx) of the fission yeast Schizosaccharomyces pombe was characterized and its regulation was studied. The full length of the prx gene was introduced into the shuttle vector pRS316 after PCR amplification, resulting in the recombinant plasmid pPrx10. The determined DNA sequence carries 1,327 bp encoding a putative Prx with a molecular mass of 19,510 Da. Prx activity was significantly increased in the S. pombe cells harboring pPrx10. The accelerated growth was observed in the S. pombe/pPrx10 cells, implying the involvement of the cloned gene in the yeast growth. To study transcriptional regulation of the prx gene, the prx-lacZ fusion gene was constructed using the yeast-E. coli shuttle vector YEp367R, and named pPrxup10. The synthesis of beta-galactosidase from the fusion gene was enhanced under carbon source-limited conditions and nitrogen starvation. Under the same growth conditions, the prx mRNA levels of the wild-type yeast cells were increased. The prx mRNA level was markedly decreased in the Pap1-negative mutant, compared with that in the wild-type yeast, suggesting that the basal expression of the prx gene is mediated by a transcription factor, Pap1. The reactive oxygen species (ROS) level was diminished in the S. pombe/pPrx10 cells than in the control cells. The extra copies of the prx gene were able to resist elevation of ROS level under limited carbon source condition and menadione treatment. In brief, the S. pombe Prx is linked with the yeast growth and up-regulated by metabolic oxidative stress on a transcriptional level. The Prx protein is partly responsible for maintaining low ROS level under normal and stressful growth conditions in the fission yeast.","authors":"Kang GY, Park EH, Lim CJ","authors_abbrev":"Kang GY et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2007-05-29","publication_year":"2008","canto_session_key":"a13487f993c5b649","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-09 19:54:06","canto_approved_date":"2017-11-09 19:54:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-30 10:15:30","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC27D7.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-11-09"},{"uniquename":"EMBL:AU008298","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084813","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12834310","title":"Inportance of phosphatidylinositol 3-phosphate in sporulation of Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2003 May;67(5):1191-3","abstract":"In Schizosaccharomyces pombe, Pik3p phosphorylates phosphatidylinositol (PI) to produce PI 3-P, which is further phosphorylated by Ste12p to yield PI 3,5-P2. Pik3p is required for both conjugation and sporulation. To test which of PI 3-P and PI 3,5-P2 is required for sporulation, diploid cells defective in production of PI 3,5-P2 were used. They underwent sporulation almost normally provided that the osmotic pressure of the medium was controlled, suggesting that not PI 3,5-P2 but PI 3-P was important. Electron microscopic analysis confirmed normal sporulation in the absence of PI 3,5-P2 although the forespore membrane was found to be less dense in these cells.","authors":"Onishi M, Nakamura Y, Koga T, Hirata A, Fukui Y","authors_abbrev":"Onishi M et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-07-02","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7962194","title":"A single p34cdc2 protein kinase (encoded by nimXcdc2) is required at G1 and G2 in Aspergillus nidulans.","citation":"J Cell Sci 1994 Jun;107 ( Pt 6):1519-28","abstract":"We have cloned and sequenced a homolog of cdc2 from Aspergillus nidulans that can complement the Schizosaccharomyces pombe cdc2-33 mutation. The gene was deleted and is required for continued nuclear DNA replication but not for mitochondrial DNA replication. Three different temperature-sensitive alleles were generated by reverse genetics. All of the mutations generate the nim phenotype of A. nidulans. The new gene was designated nimXcdc2 as it is not allelic to any of the other nim genes (nimA to nimW) of A. nidulans. Reciprocal shift experiments place an essential function for nimXcdc2 in G1 and G2. Antipeptide antibodies were generated that detect NIMXcdc2, and antisera were also generated to detect NIMEcyclinB. The two p34cdc2 protein species previously detected in A. nidulans, p34 and p37, both precipitate using NIMXcdc2 C-terminus-specific antibodies but only p34 co-precipitates with NIMEcyclinB. Dephosphorylation of denatured p34 converts it to the p37 form, showing p37 to be the non-phosphorylated form of NIMXcdc2. The phosphorylation of p34 is therefore associated with its interaction with NIMEcyclinB.","authors":"Osmani AH, van Peij N, Mischke M, O'Connell MJ, Osmani SA","authors_abbrev":"Osmani AH et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_session_key":"d26acfa6120dcca2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 14:49:19","canto_session_submitted_date":"2012-03-03 14:49:03","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:24710337","title":"Long-term single cell analysis of S. pombe on a microfluidic microchemostat array.","citation":"PLoS One 2014;9(4):e93466","abstract":"Although Schyzosaccharomyces pombe is one of the principal model organisms for studying the cell cycle, surprisingly few methods have characterized S. pombe growth on the single cell level, and no methods exist capable of analyzing thousands of cells and tens of thousands of cell division events. We developed an automated microfluidic platform permitting S. pombe to be grown on-chip for several days under defined and changeable conditions. We developed an image processing pipeline to extract and quantitate several physiological parameters including cell length, time to division, and elongation rate without requiring synchronization of the culture. Over a period of 50 hours our platform analyzed over 100000 cell division events and reconstructed single cell lineages up to 10 generations in length. We characterized cell lengths and division times in a temperature shift experiment in which cells were initially grown at 30°C and transitioned to 25°C. Although cell length was identical at both temperatures at steady-state, we observed transient changes in cell length if the temperature shift took place during a critical phase of the cell cycle. We further show that cells born with normal length do divide over a wide range of cell lengths and that cell length appears to be controlled in the second generation, were large newly born cells have a tendency to divide more rapidly and thus at a normalized cell size. The platform is thus applicable to measure fine-details in cell cycle dynamics, should be a useful tool to decipher the molecular mechanism underlying size homeostasis, and will be generally applicable to study processes on the single cell level that require large numbers of precision measurements and single cell lineages.","doi":"10.1371/journal.pone.0093466","authors":"Nobs JB, Maerkl SJ","authors_abbrev":"Nobs JB et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-04-09","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26942678","title":"Enhancer of Rudimentary Cooperates with Conserved RNA-Processing Factors to Promote Meiotic mRNA Decay and Facultative Heterochromatin Assembly.","citation":"Mol Cell 2016 Mar 03;61(5):747-759","abstract":"Erh1, the fission yeast homolog of Enhancer of rudimentary, is implicated in meiotic mRNA elimination during vegetative growth, but its function is poorly understood. We show that Erh1 and the RNA-binding protein Mmi1 form a stoichiometric complex, called the Erh1-Mmi1 complex (EMC), to promote meiotic mRNA decay and facultative heterochromatin assembly. To perform these functions, EMC associates with two distinct complexes, Mtl1-Red1 core (MTREC) and CCR4-NOT. Whereas MTREC facilitates assembly of heterochromatin islands coating meiotic genes silenced by the nuclear exosome, CCR4-NOT promotes RNAi-dependent heterochromatin domain (HOOD) formation at EMC-target loci. CCR4-NOT also assembles HOODs at retrotransposons and regulated genes containing cryptic introns. We find that CCR4-NOT facilitates HOOD assembly through its association with the conserved Pir2/ARS2 protein, and also maintains rDNA integrity and silencing by promoting heterochromatin formation. Our results reveal connections among Erh1, CCR4-NOT, Pir2/ARS2, and RNAi, which target heterochromatin to regulate gene expression and protect genome integrity.","doi":"10.1016/j.molcel.2016.01.029","authors":"Sugiyama T, Thillainadesan G, Chalamcharla VR, Meng Z, Balachandran V, Dhakshnamoorthy J, Zhou M, Grewal SIS","authors_abbrev":"Sugiyama T et al.","pubmed_publication_date":"03 Mar 2016","pubmed_entrez_date":"2016-03-05","publication_year":"2016","canto_session_key":"08fa7aa06148221f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"TOMOYASU SUGIYAMA","canto_first_approved_date":"2016-12-19 20:37:57","canto_approved_date":"2022-10-25 21:41:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-15 16:16:59","canto_added_date":"2016-03-06 01:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":46,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"TOMOYASU SUGIYAMA","community_curator":true,"annotation_count":13,"orcid":"0000-0001-5704-6606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.05","SPAC20G8.06","SPAC29B12.06c","SPBC32H8.11","SPCC4G3.15c","SPAC1006.04c","SPAC16C9.04c","SPAC13A11.03","SPAC19G12.17","SPBC32H8.10","SPCC550.14","SPCC736.12c","SPAC1006.03c","SPAC27D7.13c","SPBC16E9.12c","SPBC725.08","SPBC216.02","SPAC57A7.04c","SPAC7D4.14c","SPCC1442.04c","SPAC17H9.02","SPCC18.06c","SPCC31H12.08c"],"gene_count":23,"ltp_gene_count":17,"approved_date":"2016-12-19"},{"uniquename":"PMID:36292582","title":"GRANT Motif Regulates CENP-A Incorporation and Restricts RNA Polymerase II Accessibility at Centromere.","citation":"Genes (Basel) 2022 Sep 22;13(10)","abstract":"Precise chromosome segregation is essential for maintaining genomic stability, and its proper execution centers on the centromere, a chromosomal locus that mounts the kinetochore complex to mediate attachment of chromosomes to the spindle microtubules. The location of the centromere is epigenetically determined by a centromere-specific histone H3 variant, CENP-A. Many human cancers exhibit overexpression of CENP-A, which correlates with occurrence of aneuploidy in these malignancies. Centromeric targeting of CENP-A depends on its histone fold, but recent studies showed that the N-terminal tail domain (NTD) also plays essential roles. Here, we investigated implications of NTD in conferring aneuploidy formation when CENP-A is overexpressed in fission yeast. A series of mutant genes progressively lacking one amino acid of the NTD have been constructed for overexpression in wild-type cells using the intermediate strength  nmt41  promoter. Constructs hosting disrupted GRANT (Genomic stability-Regulating site within CENP-A N-Terminus) motif in NTD results in growth retardation, aneuploidy, increased localization to the centromere, upregulated RNA polymerase II accessibility and transcriptional derepression of the repressive centromeric chromatin, suggesting that GRANT residues fine-tune centromeric CENP-A incorporation and restrict RNA polymerase II accessibility. This work highlighted the importance of CENP-A NTD, particularly the GRANT motif, in aneuploidy formation of overexpressed CENP-A in fission yeast.","doi":"10.3390/genes13101697","authors":"Tan HL, Chen ES","authors_abbrev":"Tan HL et al.","pubmed_publication_date":"22 Sep 2022","pubmed_entrez_date":"2022-10-27","publication_year":"2022","canto_session_key":"f96b098d77745e6d","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-10-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008479","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8299177","title":"Isolation and structure of an acetolactate synthase gene from Schizosaccharomyces pombe and complementation of the ilv2 mutation in Saccharomyces cerevisiae.","citation":"Curr Genet 1993 Dec;24(6):544-7","abstract":"A gene encoding a functional acetolactate synthase (ALS) subunit has been isolated from the fission yeast Schizosaccharomyces pombe, and has been structurally and genetically characterized. The approximate 5-kbp cloned DNA segment was found to contain a 2007-bp open reading frame capable of encoding a 669 aminoacid polypeptide which exhibited 57.1% similarity to the corresponding ALS subunit from Saccharomyces cerevisiae. The putative ilv1 isolated from S. pombe was shown to encode a functional subunit of acetolactate synthase by complementation of an S. cerevisiae strain deleted for the ILV2 locus.","authors":"Bekkaoui F, Nadin-Davis SA, Crosby WL","authors_abbrev":"Bekkaoui F et al.","pubmed_publication_date":"Dec 1993","pubmed_entrez_date":"1993-12-01","publication_year":"1993","canto_session_key":"8e4c72aac9c8ba27","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-07-31 13:42:20","canto_approved_date":"2024-07-30 05:27:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 13:42:10","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP35G2.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:6526818","title":"O-Acetylhomoserine sulfhydrylase of the fission yeast Schizosaccharomyces pombe: partial purification, characterization, and its probable role in homocysteine biosynthesis.","citation":"J Biochem 1984 Nov;96(5):1511-23","abstract":"A crude extract of Schizosaccharomyces pombe cells catalyzed sulfhydrylation of both O-acetyl-L-serine and O-acetyl-L-homoserine with H2S, but did not synthesize cystathionine from O-acetyl-L-homoserine and L-cysteine. The O-acetylhomoserine sulfhydrylase [EC 4.2.99.10] was very unstable; however, it could be stabilized by the addition of 25% (w/w) sucrose or glycerol. The optimal pH for activity was 8.0 and that for stability was 7.0. The enzyme was purified approximately 300-fold from an ammonium sulfate-precipitated fraction. L-Methionine was the most effective inhibitor among the amino acids examined. It inhibited the enzyme competitively with respect to OAH with a Ki value of 2.6 mM. Sulfhydrylase activity was inhibited to various extents by some carbonyl reagents, but sulfhydryl reagents such as p-chloromercuribenzoic acid, 5,5'-dithio-bis(2-nitrobenzoic acid), and monoiodoacetic acid had no inhibitory effect. The enzyme also reacted with O-succinylhomoserine and L-homoserine to synthesize homocysteine directly, but could not utilize cysteine as a co-substrate in place of H2S. In the sulfhydrylation reactions, Km values for the substrates ranged from 10.4-12.5 mM. The enzyme was resolved to the apoenzyme by incubation with phenylhydrazine and reactivated by the addition of pyridoxal 5'-phosphate, whose Km value was 0.083 microM. The molecular weight of the enzyme was estimated to be approximately 186,000 by gel filtration and 170,000 by ultracentrifugation in sucrose density gradients. The isolectric point of the protein was pH 4.1. The characteristics of this enzyme are compared with those of physiologically functional sulfhydrylases reported for other organisms, and the possibility of the enzyme functioning as a homocysteine synthase is discussed.","authors":"Yamagata S","authors_abbrev":"Yamagata S","pubmed_publication_date":"Nov 1984","pubmed_entrez_date":"1984-11-01","publication_year":"1984","canto_session_key":"04c76a23c253368a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-25 13:18:17","canto_approved_date":"2025-02-06 16:12:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-01-28 08:28:44","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-25"},{"uniquename":"PMID:15769255","title":"Nep1, a Schizosaccharomyces pombe deneddylating enzyme.","citation":"Biochem J 2005 Jul 15;389(Pt 2):307-14","abstract":"Nedd8 is a ubiquitin-like modifier that is attached to the cullin components of E3 ubiquitin ligases. More recently, p53 has also been shown to be Nedd8-modified. Nedd8 attachment occurs in a manner similar to that observed for other ubiquitin-like modifiers. In the present study, we report on the characterization of Nep1, a deneddylating enzyme in fission yeast (Schizosaccharomyces pombe). Unlike loss of ned8, deletion of the nep1 gene is not lethal, although nep1.d cells are heterogeneous in length, suggesting a defect in cell-cycle progression. Viability of nep1.d cells is dependent on a functional spindle checkpoint but not on the DNA integrity checkpoint. Deletion of a related gene (nep2), either alone or in combination with nep1.d, also has little effect on cell viability. We show that Nep1 can deneddylate the Pcu1, Pcu3 and Pcu4 cullins in vitro and that its activity is sensitive to N-ethylmaleimide, consistent with the idea that it is a member of the cysteine protease family. nep1.d cells accumulate Nedd8-modified proteins, although these do not correspond to modified forms of the cullins, suggesting that, although Nep1 can deneddylate cullins in vitro, this is not its main function in vivo. Nep1 can be co-precipitated with the signalosome subunit Csn5. Nep1 itself is present in a high-molecular-mass complex, but the presence of this complex is not dependent on the production of intact signalosomes. Our results suggest that, in vivo, Nep1 may be responsible for deneddylating proteins other than cullins.","authors":"Zhou L, Watts FZ","authors_abbrev":"Zhou L et al.","pubmed_publication_date":"15 Jul 2005","pubmed_entrez_date":"2005-03-17","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC32H8.02c","SPAC3A11.08","SPBC20F10.06","SPAC1687.13c","SPBC17D11.01","SPAC24H6.03","SPAC17G6.12"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:20719270","title":"New and old reagents for fluorescent protein tagging of microtubules in fission yeast; experimental and critical evaluation.","citation":"Methods Cell Biol 2010;97:147-72","abstract":"The green fluorescent protein (GFP) has become a mainstay of in vivo imaging in many experimental systems. In this chapter, we first discuss and evaluate reagents currently available to image GFP-labeled microtubules in the fission yeast Schizosaccharomyces pombe, with particular reference to time-lapse applications. We then describe recent progress in the development of robust monomeric and tandem dimer red fluorescent proteins (RFPs), including mCherry, TagRFP-T, mOrange2, mKate, and tdTomato, and we present data assessing their suitability as tags in S. pombe. As part of this analysis, we introduce new PCR tagging cassettes for several RFPs, new pDUAL-based plasmids for RFP-tagging, and new RFP-tubulin strains. These reagents should improve and extend the study of microtubules and microtubule-associated proteins in S. pombe.","doi":"10.1016/S0091-679X(10)97009-X","authors":"Snaith HA, Anders A, Samejima I, Sawin KE","authors_abbrev":"Snaith HA et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-08-20","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35136165","title":"An extended motif in the SARS-CoV-2 spike modulates binding and release of host coatomer in retrograde trafficking.","citation":"Commun Biol 2022 Feb 08;5(1):115","abstract":"β-Coronaviruses such as SARS-CoV-2 hijack coatomer protein-I (COPI) for spike protein retrograde trafficking to the progeny assembly site in endoplasmic reticulum-Golgi intermediate compartment (ERGIC). However, limited residue-level details are available into how the spike interacts with COPI. Here we identify an extended COPI binding motif in the spike that encompasses the canonical K-x-H dibasic sequence. This motif demonstrates selectivity for αCOPI subunit. Guided by an in silico analysis of dibasic motifs in the human proteome, we employ mutagenesis and binding assays to show that the spike motif terminal residues are critical modulators of complex dissociation, which is essential for spike release in ERGIC. αCOPI residues critical for spike motif binding are elucidated by mutagenesis and crystallography and found to be conserved in the zoonotic reservoirs, bats, pangolins, camels, and in humans. Collectively, our investigation on the spike motif identifies key COPI binding determinants with implications for retrograde trafficking.","doi":"10.1038/s42003-022-03063-y","authors":"Dey D, Singh S, Khan S, Martin M, Schnicker NJ, Gakhar L, Pierce BG, Hasan SS","authors_abbrev":"Dey D et al.","pubmed_publication_date":"08 Feb 2022","pubmed_entrez_date":"2022-02-09","publication_year":"2022","canto_session_key":"51245441d5d2def9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-02-23 13:05:27","canto_approved_date":"2023-09-05 04:13:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-23 13:05:18","canto_added_date":"2023-02-23 08:44:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBPJ4664.04"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2023-02-23"},{"uniquename":"PMID:30907886","title":"A Deep-sequencing-assisted, Spontaneous Suppressor Screen in the Fission Yeast Schizosaccharomyces pombe.","citation":"J Vis Exp 2019 Mar 07;(145)","abstract":"A genetic screen for mutant alleles that suppress phenotypic defects caused by a mutation is a powerful approach to identify genes that belong to closely related biochemical pathways. Previous methods such as the Synthetic Genetic Array (SGA) analysis, and random mutagenesis techniques using ultraviolet (UV) or chemicals like ethyl methanesulfonate (EMS) or N-ethyl-N- nitrosourea (ENU), have been widely used but are often costly and laborious. Also, these mutagen-based screening methods are frequently associated with severe side effects on the organism, inducing multiple mutations that add to the complexity of isolating the suppressors. Here, we present a simple and effective protocol to identify suppressor mutations in mutants which confer a growth defect in Schizosaccharomyces pombe. The fitness of cells with a growth deficiency in standard rich liquid media or synthetic liquid media can be monitored for recovery using an automated 96-well plate reader over an extended period. Once a cell acquires a suppressor mutation in the culture, its descendants outcompete those of the parental cells. The recovered cells that have a competitive growth advantage over the parental cells can then be isolated and backcrossed with the parental cells. The suppressor mutations are then identified using whole-genome sequencing. Using this approach, we have successfully isolated multiple suppressors that alleviate the severe growth defects caused by loss of Elf1, an AAA+ family ATPase that is important in nuclear mRNA transport and maintenance of genomic stability. There are currently over 400 genes in S. pombe with mutants conferring a growth defect. As many of these genes are uncharacterized, we propose that our method will hasten the identification of novel functional interactions with this user-friendly, high-throughput approach.","doi":"10.3791/59133","authors":"Marayati BF, Pease JB, Zhang K","authors_abbrev":"Marayati BF et al.","pubmed_publication_date":"07 Mar 2019","pubmed_entrez_date":"2019-03-26","publication_year":"2019","canto_session_key":"0528f094c790d127","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-03-27 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6784938","title":"Inhibition of RNA synthesis in yeast protoplasts by a peptide factor from Tetrahymena cells.","citation":"Cell Biol Int Rep 1981 Feb;5(2):187-94","abstract":"Protoplasts of Schizosaccharomyces pombe, grown on a rich nutrient medium, were treated with a peptide factor isolated from cultures of the protozoan Tetrahymena pyriformis. The peptide factor is known to inhibit RNA synthesis in Tetrahymena. It has now been shown that the peptide factor also inhibits RNA synthesis in yeast protoplasts without affecting protein synthesis.","authors":"Andersen HA, Kramhøft B","authors_abbrev":"Andersen HA et al.","pubmed_publication_date":"Feb 1981","pubmed_entrez_date":"1981-02-01","publication_year":"1981","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB044536","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:309889","title":"Oxygen uptake during the cell cycle of the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1978 Oct;33:399-411","abstract":"Oxygen uptake was measured in synchronous cultures of the fission yeast Schizosaccharomyces pombe. The rate of oxygen uptake was found to increase in a step-wise manner at the beginning of the cycle and again in the middle of the cycle. The increases in rate were such that overall, oxygen uptake doubled in rate once per cell cycle. Addition of inhibitors of DNA synthesis or nuclear division to a synchronous culture did not affect the uptake of oxygen. In an induced synchronous culture, in which DNA synthesis, cell division, and nuclear division, but not 'growth' were synchronized, oxygen uptake increased continuously in rate and did not show the step-wise rises which were shown in the selection-synchronized culture. These results were compared with previous measurements of oxygen uptake in yeast and an explanation is suggested for the many different patterns which have been reported.","authors":"Creanor J","authors_abbrev":"Creanor J","pubmed_publication_date":"Oct 1978","pubmed_entrez_date":"1978-10-01","publication_year":"1978","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6411749","title":"Absence of step changes in activity of certain enzymes during the cell cycle of budding and fission yeasts in synchronous cultures.","citation":"J Cell Sci 1983 May;61:339-49","abstract":"Synchronous cultures prepared by selection from an elutriating rotor were used to measure activity changes during the cell cycle of the following enzymes: acid phosphatase in Schizosaccharomyces pombe and Saccharomyces cerevisiae, alpha-glucosidase in S. cerevisiae and beta-galactosidase in Kluyveromyces lactis. There was no sign of step rises in activity in acid phosphatase but there were indications in S. cerevisiae of the linear pattern with rate doublings once per cycle that had been found previously in S. pombe. There was also no sign of step rises in the other two enzymes, in contrast to earlier results using different techniques. Asynchronous control cultures showed little or no perturbations after the first hour.","authors":"Creanor J, Elliott SG, Bisset YC, Mitchison JM","authors_abbrev":"Creanor J et al.","pubmed_publication_date":"May 1983","pubmed_entrez_date":"1983-05-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23978339","title":"Yeast community associated with the solid state fermentation of traditional Chinese Maotai-flavor liquor.","citation":"Int J Food Microbiol 2013 Sep 02;166(2):323-30","abstract":"Yeasts are the most important group of microorganisms contributing to liquor quality in the solid-state fermentation process of Chinese Maotai-flavor liquor. There occurred a complex yeast community structure during this process, including stages of Daqu (the starter) making, stacking fermentation on the ground and liquor fermentation in the pits. In the Daqu making stage, few yeast strains accumulated. However, the stacking fermentation stage accumulated nine yeast species with different physio-biochemical characteristics. But only four species kept dominant until liquor fermentation, which were Zygosaccharomyces bailii, Saccharomyces cerevisiae, Pichia membranifaciens, and Schizosaccharomyces pombe, implying their important functions in liquor making. The four species tended to inhabit in different locations of the stack and pits during stacking and liquor fermentation, due to the condition heterogeneity of the solid-state fermentation, including the different fermentation temperature profiles and oxygen density in different locations. Moreover, yeast population was much larger in the upper layer than that in the middle and bottom layers in liquor fermentation, which was in accordance with the profile of reducing sugar consumption and ethanol production. This was a systematical investigation of yeast community structure dynamics in the Maotai-flavor liquor fermentation process. It would be of help to understand the fermentative mechanism in solid-state fermentation for Maotai-flavor liquor.","doi":"10.1016/j.ijfoodmicro.2013.07.003","authors":"Wu Q, Chen L, Xu Y","authors_abbrev":"Wu Q et al.","pubmed_publication_date":"02 Sep 2013","pubmed_entrez_date":"2013-08-28","publication_year":"2013","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8710510","title":"Purification and characterization of the Pac1 ribonuclease of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1996 Jun 15;24(12):2377-86","abstract":"The pac1+ gene of the fission yeast Schizosaccharomyces pombe is essential for viability and its overexpression induces sterility and suppresses mutations in the pat1+ and snm1+ genes. The pac1+ gene encodes a protein that is structurally similar to RNase III from Escherichia coli, but its normal function is unknown. We report here the purification and characterization of the Pac1 protein after overexpression in E. coli. The purified protein is a highly active, double-strand-specific endoribonuclease that converts long double-stranded RNAs into short oligonucleotides and also cleaves a small hairpin RNA substrate. The Pac1 RNase is inhibited by a variety of double- and single-stranded polynucleotides, but polycytidylic acid greatly enhances activity and also promotes cleavage specificity. The Pac1 RNase produces 5'-phosphate termini and requires Mg2+; Mn2+ supports activity but causes a loss of cleavage specificity. Optimal activity was obtained at pH 8.5, at low ionic strength, in the presence of a reducing agent. The enzyme is relatively insensitive to N-ethylmaleimide but is strongly inhibited by ethidium bromide and vanadyl ribonucleoside complexes. The properties of the Pac1 RNase support the hypothesis that it is a eukaryotic homolog of RNase III.","authors":"Rotondo G, Frendewey D","authors_abbrev":"Rotondo G et al.","pubmed_publication_date":"15 Jun 1996","pubmed_entrez_date":"1996-06-15","publication_year":"1996","canto_session_key":"e4f166bfc2c8530c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-29 12:27:03","canto_approved_date":"2020-01-23 13:21:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-17 17:23:44","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-29"},{"uniquename":"PMID:34201031","title":"Rice ( Oryza sativa ) TIR1 and 5'adamantyl-IAA Significantly Improve the Auxin-Inducible Degron System in  Schizosaccharomyces pombe .","citation":"Genes (Basel) 2021 Jun 08;12(6)","abstract":"The auxin-inducible degron (AID) system is a powerful tool to induce targeted degradation of proteins in eukaryotic model organisms. The efficiency of the existing  Schizosaccharomyces pombe  AID system is limited due to the fusion of the F-box protein TIR1 protein to the SCF component, Skp1 (Skp1-TIR1). Here, we report an improved AID system for  S. pombe  that uses the TIR1 from  Oryza sativa  (OsTIR1) not fused to Skp1. Furthermore, we demonstrate that degradation efficiency can be improved by pairing an OsTIR1 auxin-binding site mutant, OsTIR1 F74A , with an auxin analogue, 5'adamantyl-IAA (AID2). We provide evidence for the enhanced functionality of the OsTIR1 AID and AID2 systems by application to the essential DNA replication factor Mcm4 and to a non-essential recombination protein, Rad52. Unlike AID, no detectable auxin-independent depletion of AID-tagged proteins was observed using AID2.","doi":"10.3390/genes12060882","authors":"Watson AT, Hassell-Hart S, Spencer J, Carr AM","authors_abbrev":"Watson AT et al.","pubmed_publication_date":"08 Jun 2021","pubmed_entrez_date":"2021-07-02","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-07-04 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:X74274","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36854376","title":"Identification of a small RhoA GTPase inhibitor effective in fission yeast and human cells.","citation":"Open Biol 2023 Mar;13(3):220185","abstract":"The Rho GTPase family proteins are key regulators of cytoskeletal dynamics. Deregulated activity of Rho GTPases is associated with cancers and neurodegenerative diseases, and their potential as drug targets has long been recognized. Using an economically effective drug screening workflow in fission yeast and human cells, we have identified a Rho GTPase inhibitor, O1. By a suppressor mutant screen in fission yeast, we find a point mutation in the  rho1  gene that confers resistance to O1. Consistent with the idea that O1 is the direct inhibitor of Rho1, O1 reduced the cellular amount of activated, GTP-bound Rho1 in wild-type cells, but not in the O1-resistant mutant cells, in which the evolutionarily conserved Ala62 residue is mutated to Thr. Similarly, O1 inhibits activity of the human orthologue RhoA GTPase in tissue culture cells. Our studies illustrate the power of yeast phenotypic screens in the identification and characterization of drugs relevant to human cells and have identified a novel GTPase inhibitor for fission yeast and human cells.","doi":"10.1098/rsob.220185","authors":"Morishita J, Nurse P","authors_abbrev":"Morishita J et al.","pubmed_publication_date":"Mar 2023","pubmed_entrez_date":"2023-02-28","publication_year":"2023","canto_session_key":"25c4a68249a1036f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-05-09 08:07:50","canto_approved_date":"2024-05-09 08:07:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-09 08:07:43","canto_added_date":"2023-03-02 01:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-05-09"},{"uniquename":"PMID:10982385","title":"A pcl-like cyclin activates the Res2p-Cdc10p cell cycle \"start\" transcriptional factor complex in fission yeast.","citation":"Mol Biol Cell 2000 Sep;11(9):2845-62","abstract":"In the fission yeast Schizosaccharomyces pombe, the \"start\" of the cell cycle is controlled by the two functionally redundant transcriptional regulator complexes, Res1p-Cdc10p and Res2p-Cdc10p, that activate genes essential for the onset and progression of S phase. The activity of the Res2p-Cdc10p complex is regulated at least by the availability of the Rep2 trans-activator subunit in the mitotic cell cycle. We have recently isolated the pas1(+) gene as a multicopy suppressor of the res1 null mutant. This gene encodes a novel cyclin that shares homology with the Pho85 kinase-associated cyclins of the budding yeast Saccharomyces cerevisiae. Genetic analysis reveals that Pas1 cyclin is unrelated to phosphate metabolism and stimulates the G(1)-S transition by specifically activating the Res2p-Cdc10p complex independently of Rep2p. Pas1 cyclin also controls mating pheromone signaling. Cells lacking pas1(+) are highly sensitive to mating pheromone, responding with facilitated G(1) arrest and premature commitment to conjugation. Pas1 cyclin associates in vivo with both Cdc2 and Pef1 kinases, the latter of which is a fission yeast counterpart of the budding yeast Pho85 kinase, but genetic analysis indicates that the Pef1p-associated Pas1p is responsible for the activation of Res2p-Cdc10p during the G(1)-S transition.","authors":"Tanaka K, Okayama H","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-09-12","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC19E9.03","SPBC725.16","SPAPB2B4.03","SPAC22F3.09c","SPAC2F7.11","SPCC16C4.11","SPBC2F12.11c","SPBC19F5.01c","SPCC4E9.02"],"gene_count":10,"ltp_gene_count":9},{"uniquename":"PMID:16377914","title":"Isolation and characterization of glucose derepressed invertase mutants from Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2005 Dec;69(12):2475-8","abstract":"We have isolated 14 different Schizosaccharomyces pombe mutants that synthesize invertase enzyme constitutively. Analyses of invertase activities revealed that the degrees of resistance to glucose repression were not similar among different complementation groups. One of the complementation groups appeared to be associated with functional and/or regulatory defects in hexose transport. Another complementation group appeared to be specific for the regulation of the inv1 gene alone, implying that these mutations might be associated with different genes acting on the glucose sensing and signaling pathway. In addition, we found that the wild-type level glucose uptake is essential for the full-level repression of inv1 expression.","authors":"Kig C, Turkel S, Temizkan G","authors_abbrev":"Kig C et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-12-27","publication_year":"2005","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12681321","title":"Myosin-cell wall interactions during cytokinesis in fission yeast: a framework for understanding plant cytokinesis?","citation":"Cell Biol Int 2003;27(3):239-40","abstract":"","authors":"Mulvihill DP, Hyams JS","authors_abbrev":"Mulvihill DP et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-04-12","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16198156","title":"A new SUMO ligase in the DNA damage response.","citation":"DNA Repair (Amst) 2006 Jan 05;5(1):138-41","abstract":"SUMO is a small ubiquitin-like protein that is attached to target proteins, altering their localization and function. The condensin and cohesin-related Smc5/6 complex has been linked to DNA repair and checkpoint responses, but details of its molecular function have remained obscure. Recent reports show one subunit of the complex is a SUMO ligase, providing another link between protein sumoylation and DNA damage responses.","authors":"Lee KM, O'Connell MJ","authors_abbrev":"Lee KM et al.","pubmed_publication_date":"05 Jan 2006","pubmed_entrez_date":"2005-10-04","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012156","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21528443","title":"Purification of native Argonaute complexes from the fission yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2011;725:1-13","abstract":"Small interfering (si) RNAs, produced by the RNA interference (RNAi)-mediated processing of long double-stranded (ds) RNAs, can inhibit gene expression by post-transcriptional or transcriptional gene silencing mechanisms. At the heart of all small RNA-mediated silencing lies the key RNAi effector protein Argonaute, which once loaded with small RNAs can recognize its target transcript by siRNA-RNA Watson-Crick base pairing interactions. In the fission yeast Schizosaccharomyces pombe, the formation of the epigenetically heritable centromeric heterochromatin requires RNAi proteins including the sole fission yeast Argonaute homolog, Ago1. Two distinct native Ago1 complexes have been purified and studied extensively, both of which are required for siRNA production and heterochromatin formation at the fission yeast centromeres. The purification and analysis of the Argonaute siRNA chaperone (ARC) complex and RNA-induced transcriptional silencing (RITS) complex have provided insight into the mechanism of siRNA-Ago1 loading and the cis recruitment of silencing complexes at fission yeast centromeres, respectively. These discoveries have been instrumental in shaping the current models of RNA-mediated epigenetic silencing in eukaryotes. Below, we describe the protocol used for affinity purification of the native Ago1 complexes from S. pombe.","doi":"10.1007/978-1-61779-046-1_1","authors":"Buker SM, Motamedi MR","authors_abbrev":"Buker SM et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-04-30","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11739717","title":"Protein kinase A regulates sexual development and gluconeogenesis through phosphorylation of the Zn finger transcriptional activator Rst2p in fission yeast.","citation":"Mol Cell Biol 2002 Jan;22(1):1-11","abstract":"Protein kinase A (PKAi a cyclic AMP-dependent protein kinase) negatively regulates sexual development and gluconeogenesis in fission yeast by suppressing the transcription of ste11 required for the former and the transcription of fbp1 required for the latter. Here we show that Rst2p, a zinc finger protein that can bind to the upstream region of ste11 and fbp1 via the STREP motif, mediates the activity of PKA to transcription of these genes. A simple reporter system confirmed that PKA could cause its negative effect on transcription through the combination of Rst2p and STREP. Rst2p was phosphorylated by PKA in vitro at two consensus sequences on it. Substitution of the target threonine residues by alanine made the protein active even in the presence of high PKA activity. Rst2p underwent hyperphosphorylation in the medium lacking glucose, and PKA inhibited this hyperphosphorylation. Rst2p was mainly cytoplasmic under high PKA activity but was concentrated in the nucleus when this activity was lowered, suggesting that PKA might regulate ste11 and fbp1 negatively by excluding Rst2p from the nucleus. However, the shift of Rst2p localization was not perfect under physiological conditions, leaving the possibility that PKA inhibits Rst2p function in another way as well. Although the PKA-Rst2p-STREP pathway is apparently central to the regulation of ste11 and fbp1 transcription in accordance with nutritional conditions, some additional paths are likely to connect nitrogen to repression of ste11 and glucose to repression of fbp1. These paths may ensure the specificity between the type of nutrients in shortage and the type of genes to be expressed.","authors":"Higuchi T, Watanabe Y, Yamamoto M","authors_abbrev":"Higuchi T et al.","pubmed_publication_date":"Jan 2002","pubmed_entrez_date":"2001-12-12","publication_year":"2002","canto_session_key":"d1d283a2ef48f053","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 19:56:42","canto_approved_date":"2026-04-24 06:42:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-03-20 14:07:34","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":45,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPBC1198.14c","SPBC106.10","SPAC8C9.03","SPAC6F12.02","SPBC19C7.03"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2018-06-10"},{"uniquename":"PMID:9168469","title":"Isolation and molecular characterization of mRNA transport mutants in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1997 May;8(5):825-41","abstract":"Nucleocytoplasmic transport of mRNA is essential for eukaryotic gene expression. However, how mRNA is exported from the nucleus is mostly unknown. To elucidate the mechanisms of mRNA transport, we took a genetic approach to identify genes, the products of which play a role in that process. From about 1000 temperature -sensitive (ts- or cs-) mutants, we identified five ts- mutants that are defective in poly(A)+ RNA transport by using a situ hybridization with an oligo(dT)50 as a probe. These mutants accumulate poly(A)+ RNA in the nuclei when shifted to a nonpermissive temperature. All five mutations are tightly linked to the ts- growth defects, are recessive, and fall into four different groups designated as ptr 1-4 (poly(A)+ RNA transport). Interestingly, each group of mutants has a differential localization pattern of poly(A)+ RNA in the nuclei at the nonpermissive temperature, suggesting that they have defects at different steps of the mRNA transport pathway. Localization of a nucleoplasmin-green fluorescent protein fusion suggests that ptr2 and ptr3 have defects also in nuclear protein import. Among the isolated mutants, only ptr2 showed a defect in pre-mRNA splicing. We cloned the ptr2+ and ptr3+ genes and found that they encode Schizosaccharomyces pombe homologues of the mammalian RCC1, a guanine nucleotide exchange factor for RAN/TC4, and the ubiquitin-activating enzyme E1 involved in ubiquitin conjugation, respectively. The ptr3+ gene is essential for cell viability, and Ptr3p tagged with green fluorescent protein was localized in both the nucleus and the cytoplasm. This is the first report suggesting that the ubiquitin system plays a role in mRNA export.","authors":"Azad AK, Tani T, Shiki N, Tsuneyoshi S, Urushiyama S, Ohshima Y","authors_abbrev":"Azad AK et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"96f18b755b0832a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-03-11 16:48:14","canto_approved_date":"2026-01-30 12:53:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-11 16:47:14","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.04","SPBC1604.21c","SPBC557.03c","SPCC5E4.04"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-03-11"},{"uniquename":"EMBL:AU011120","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12411492","title":"Plo1(+) regulates gene transcription at the M-G(1) interval during the fission yeast mitotic cell cycle.","citation":"EMBO J 2002 Nov 01;21(21):5745-55","abstract":"The regulation of gene expression plays an important part in cell cycle controls. We describe the molecular machinery that co-ordinates gene transcription at the M-G(1) interval during the fission yeast mitotic cell cycle. A sequence is identified in the cdc15(+) promoter that we call a PCB (pombe cell cycle box), which confers M-G(1)-specific transcription. Sequences similar to the PCB are present in the promoters of seven other genes, spo12(+), cdc19(+), fin1(+), sid2(+), ppb1(+), mid1(+)/dmf1(+) and plo1(+), which we find to be transcribed at M-G(1). A transcription factor complex is identified that binds to the PCB sequence, which we name PBF, for PCB-binding factor. Finally, we show that PBF binding activity and consequent gene transcription are regulated by the Plo1p protein kinase, thus invoking a potential auto-feedback loop mechanism that regulates mitotic gene transcription and passage through septation and cytokinesis.","authors":"Anderson M, Ng SS, Marchesi V, MacIver FH, Stevens FE, Riddell T, Glover DM, Hagan IM, McInerny CJ","authors_abbrev":"Anderson M et al.","pubmed_publication_date":"01 Nov 2002","pubmed_entrez_date":"2002-11-02","publication_year":"2002","canto_session_key":"2039b43f720bf7a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-10-19 15:29:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-10-19 14:44:13","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.15c","SPBC4.04c","SPBC16G5.15c","SPBC19G7.06","SPCC4B3.15","SPAC25G10.07c","SPAC19E9.02","SPAC23C11.16","SPBP4H10.04","SPBC4C3.12","SPAC20G8.05c","SPBC21.06c","SPBC336.12c","SPAC24B11.11c"],"gene_count":14,"ltp_gene_count":4,"approved_date":"2015-10-19"},{"uniquename":"PMID:18414064","title":"Schizosaccharomyces pombe Orc5 plays multiple roles in the maintenance of genome stability throughout the cell cycle.","citation":"Cell Cycle 2008 Apr 15;7(8):1085-96","abstract":"The six-subunit origin recognition complex (ORC) acts as a landing pad for factors that initiate DNA replication by binding to replication origins. In addition, ORC is involved in other processes such as transcriptional gene silencing and sister chromatid cohesion in Saccharomyces cerevisiae. However, whether these functions of ORC are specific to Saccharomyces cerevisiae or are shared by the ORC of other organisms is currently unclear. Analysis of two temperature-sensitive alleles of the fifth ORC subunit of Schizosaccharomyces pombe, orc5-H19 and orc5-H37, indicates that Orc5 of Schizosaccharomyces pombe has similar multiple functions to those of Orc5 of Saccharomyces cerevisiae. The orc5-H19 cells were defective in DNA replication initiation, and execution point analysis of this mutant revealed that ORC functions before metaphase to prepare for the initiation of replication in the next cell cycle. The orc5-H37 cells seemed to complete DNA synthesis but were arrested before entering M phase. In both mutants, the rads-chk1 checkpoint was activated to prevent mitosis, suggesting that this checkpoint pathway monitors the functional integrity of ORC. In addition, orc5-H37 cells showed premature separation of sister chromatids, which resulted in cell growth being dependent on the mad2-dependent spindle checkpoint. Consistently, this mutant showed a defect in the loading of Rad21, a cohesin component. Based on these observations, we propose that Orc5 has at least two distinct functions that can be separated genetically. Taken together, our results provide further support for the idea that ORC plays multiple functions during the cell cycle.","authors":"Kato H, Matsunaga F, Miyazaki S, Yin L, D'Urso G, Tanaka K, Murakami Y","authors_abbrev":"Kato H et al.","pubmed_publication_date":"15 Apr 2008","pubmed_entrez_date":"2008-04-17","publication_year":"2008","canto_session_key":"44220f03945c034e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-21 14:55:37","canto_approved_date":"2026-01-30 15:07:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-21 14:55:29","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":59,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC646.14c","SPBC20F10.06","SPAC1952.07","SPCC338.17c","SPBC16A3.11","SPAC6F12.15c","SPAC664.07c","SPAC31A2.05c","SPCC1259.13"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-12-21"},{"uniquename":"PMID:22936388","title":"Isolation of a novel rmn1 gene genetically linked to spnab2 with respect to mRNA export in fission yeast.","citation":"Mol Cells 2012 Sep;34(3):315-21","abstract":"In fission yeast, Schizosaccharomyces pombe, the spnab2 gene encodes an ortholog of the budding yeast nuclear abundant poly(A)(+) RNA-binding protein 2 (Nab2) that is an essential protein required for both mRNA biogenesis and nuclear export of mRNA to the cytoplasm. We have previously isolated three mutants (SLnab1-3) that showed synthetic lethality under the repressed condition of spnab2 expression. In this study, we isolated a novel rmn1 gene as a multicopy suppressor that complemented the defects in growth and mRNA export of SLnab1 mutant cells. The rmn1 gene contained three introns and encoded a 589 amino-acid protein with the RNA recognition motif (RRM) in the central region. The Δrmn1 null mutant was viable but showed a s light mRNA export defect. However, its over-expression caused a deleterious effect on growth accompanied by intense accumulation of poly(A)(+) RNA in the nucleus. The combination of Δrmn1 with Δspnab2 or Δspmex67 also inhibited growth. In addition, Rmn1p was associated with Rae1p in vivo. These results suggest that rmn1 is a novel gene that is functionally linked to spnab2.","authors":"Cho YS, Jang S, Yoon JH","authors_abbrev":"Cho YS et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-09-01","publication_year":"2012","canto_session_key":"5c021623b341ddb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-20 10:46:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-02-20 10:46:21","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.05c","SPBC1921.03c","SPBC902.04","SPAC14C4.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-02-20"},{"uniquename":"PMID:14985109","title":"Cdk inhibitor ste9p/srw1p is involved in response to protein synthesis inhibition in fission yeast.","citation":"Biochem Biophys Res Commun 2004 Mar 19;315(4):984-90","abstract":"It remains unknown whether the cell cycle system responds properly to protein synthesis inhibition. In this paper I report finding in Schizosaccharomyces pombe that partially deleted elongation factor 3 genes rescue various mitotic catastrophe mutants depending on deltaste9 in a dominant-negative manner. In response to protein synthesis inhibitors, deltaste9 and some other mutants delay halting the cell cycle at G2-M and the combined cdc2-M26 deltaste9 mutant greatly loses viability. It is suggested that cell cycle be positively controlled in an ste9-dependent manner before essential factors for viability and other important functions are exhausted when protein synthesis is inhibited.","authors":"Sakai T","authors_abbrev":"Sakai T","pubmed_publication_date":"19 Mar 2004","pubmed_entrez_date":"2004-02-27","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC144.13c","SPBC11B10.09","SPAC29A4.02c","SPCC18B5.03","SPBC582.03","SPBC660.14","SPAC1952.07","SPBC216.05"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:20157622","title":"Meiotic Recombination in Schizosaccharomyces pombe: A Paradigm for Genetic and Molecular Analysis.","citation":"Genome Dyn Stab 2008 Jan 01;3:195","abstract":"The fission yeast Schizosaccharomyces pombe is especially well-suited for both genetic and biochemical analysis of meiotic recombination. Recent studies have revealed ~50 gene products and two DNA intermediates central to recombination, which we place into a pathway from parental to recombinant DNA. We divide recombination into three stages - chromosome alignment accompanying nuclear \"horsetail\" movement, formation of DNA breaks, and repair of those breaks - and we discuss the roles of the identified gene products and DNA intermediates in these stages. Although some aspects of recombination are similar to those in the distantly related budding yeast Saccharomyces cerevisiae, other aspects are distinctly different. In particular, many proteins required for recombination in one species have no clear ortholog in the other, and the roles of identified orthologs in regulating recombination often differ. Furthermore, in S. pombe the dominant joint DNA molecule intermediates contain single Holliday junctions, and intersister joint molecules are more frequent than interhomolog types, whereas in S. cerevisiae interhomolog double Holliday junctions predominate. We speculate that meiotic recombination in other organisms shares features of each of these yeasts.","authors":"Cromie G, Smith GR","authors_abbrev":"Cromie G et al.","pubmed_publication_date":"01 Jan 2008","pubmed_entrez_date":"2010-02-17","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15486206","title":"DNA repair by a Rad22-Mus81-dependent pathway that is independent of Rhp51.","citation":"Nucleic Acids Res 2004;32(18):5570-81","abstract":"In budding yeast most Rad51-dependent and -independent recombination depends on Rad52. In contrast, its homologue in fission yeast, Rad22, was assumed to play a less critical role possibly due to functional redundancy with another Rad52-like protein Rti1. We show here that this is not the case. Rad22 like Rad52 plays a central role in recombination being required for both Rhp51-dependent and -independent events. Having established this we proceed to investigate the involvement of the Mus81-Eme1 endonuclease in these pathways. Mus81 plays a relatively minor role in the Rhp51-dependent repair of DNA damage induced by ultraviolet light. In contrast Mus81 has a key role in the Rad22-dependent (Rhp51-independent) repair of damage induced by camptothecin, hydroxyurea and methyl-methanesulfonate. Furthermore, spontaneous intrachromosomal recombination that gives rise to deletion recombinants is impaired in a mus81 mutant. From these data we propose that a Rad22-Mus81-dependent (Rhp51-independent) pathway is an important mechanism for the repair of DNA damage in fission yeast. Consistent with this we show that in vitro Rad22 can promote strand invasion to form a D-loop that can be cleaved by Mus81.","authors":"Doe CL, Osman F, Dixon J, Whitby MC","authors_abbrev":"Doe CL et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-10-16","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC30D11.10","SPCC4G3.05c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11378902","title":"Functional characterization of Gms1p/UDP-galactose transporter in Schizosaccharomyces pombe.","citation":"Yeast 2001 Jun;18(8):745-57","abstract":"Galactosylation of glycoproteins in the fission yeast Schizosaccharomyces pombe requires the transport of UDP-galactose as substrate for the galactosyltransferase into the lumen of the Golgi apparatus, which is achieved by the UDP-galactose transporter. We isolated a mutant (gms1) that is deficient in galactosylation of cell surface glycoproteins in Sz.pombe, and found that the gms1(+) gene encodes a UDP-galactose transporter. In the prediction of secondary structure of the Gms1 protein, an eight-membrane-spanning structure was obtained. Fluorescent microscopy revealed the functional Gms1-GFP fusion protein to be stably localized at the Golgi membrane. Sequencing analysis of the coding region of Gms1p derived from galactosylation-defective mutants identified a single amino acid mutation (A102T or A258E) located within the putative transmembrane region, helix 2 or helix 7, respectively. The mutagenized Gms1(A102T or A258E)p exhibited loss of UDP-galactose transport activity but no change in the localization to the Golgi membrane. The C-terminal truncated Gms1p mutants demonstrated that the C-terminal hydrophilic region was dispensable for targeting and function as UDP-galactose transporter at the Golgi membrane. We suggest that the putative eighth (the most C-terminus-proximal) transmembrane helix of Gms1p is critical to targeting from ER to the Golgi membrane.","authors":"Tanaka N, Takegawa K","authors_abbrev":"Tanaka N et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-05-30","publication_year":"2001","canto_session_key":"1f46f7473f4ec0a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-09-12 13:18:28","canto_approved_date":"2023-01-18 09:21:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-07 10:06:51","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-12"},{"uniquename":"PMID:10775265","title":"The role of the sid1p kinase and cdc14p in regulating the onset of cytokinesis in fission yeast.","citation":"EMBO J 2000 Apr 17;19(8):1803-15","abstract":"Coordination of mitosis and cytokinesis is crucial for ensuring proper chromosome segregation and genomic stability. In Schizosaccharomyces pombe, the sid genes (cdc7, cdc11, cdc14, spg1, sid1, sid2 and sid4) define a signaling pathway that regulates septation and cytokinesis. Here we describe the characterization of a novel protein kinase, Sid1p. Sid1p localizes asymmetrically to one spindle pole body (SPB) in anaphase. Sid1p localization is maintained during medial ring constriction and septum synthesis and disappears prior to cell separation. Additionally, we found that Cdc14p is in a complex with Sid1p. Epistasis analysis places Sid1p-Cdc14p downstream of Spg1p-Cdc7p but upstream of Sid2p. Finally, we show that cyclin proteolysis during mitosis is unaffected by inactivating the sid pathway; in fact, loss of Cdc2-cyclin activity promotes Sid1p-Cdc14p association with the SPB, possibly providing a mechanism that couples cytokinesis with mitotic exit.","authors":"Guertin DA, Chang L, Irshad F, Gould KL, McCollum D","authors_abbrev":"Guertin DA et al.","pubmed_publication_date":"17 Apr 2000","pubmed_entrez_date":"2000-04-25","publication_year":"2000","canto_session_key":"9d76f3efe27ac062","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-08 11:41:11","canto_approved_date":"2025-09-03 10:29:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-30 11:42:41","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPAC9G1.09","SPCC1739.11c","SPBC24C6.07","SPBC26H8.07c","SPBC20F10.06","SPAC6F6.08c","SPBC244.01c","SPBC21.06c","SPAC1565.06c","SPBC11B10.09"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2021-01-08"},{"uniquename":"PMID:31515876","title":"The Loz1 transcription factor from Schizosaccharomyces pombe binds to Loz1 response elements and represses gene expression when zinc is in excess.","citation":"Mol Microbiol 2019 Dec;112(6):1701-1717","abstract":"In Schizosaccharomyces pombe, the expression of the zrt1 zinc uptake gene is tightly regulated by zinc status. When intracellular zinc levels are low, zrt1 is highly expressed. However, when zinc levels are high, transcription of zrt1 is blocked in a manner that is dependent upon the transcription factor Loz1. To gain additional insight into the mechanism by which Loz1 inhibits gene expression in high zinc, we used RNA-seq to identify Loz1-regulated genes, and ChIP-seq to analyze the recruitment of Loz1 to target gene promoters. We find that Loz1 is recruited to the promoters of 27 genes that are also repressed in high zinc in a Loz1-dependent manner. We also find that the recruitment of Loz1 to the majority of target gene promoters is dependent upon zinc and the motif 5'-CGN(A/C)GATCNTY-3', which we have named the Loz1 response element (LRE). Using reporter assays, we show that LREs are both required and sufficient for Loz1-mediated gene repression, and that the level of gene repression is dependent upon the number and sequence of LREs. Our results elucidate the Loz1 regulon in fission yeast and provide new insight into how eukaryotic cells are able to respond to changes in zinc availability in the environment.","doi":"10.1111/mmi.14384","authors":"Wilson S, Liu YH, Cardona-Soto C, Wadhwa V, Foster MP, Bird AJ","authors_abbrev":"Wilson S et al.","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-09-14","publication_year":"2019","canto_session_key":"e3188b7c6757274d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Amanda Bird","canto_first_approved_date":"2019-10-14 12:32:38","canto_approved_date":"2024-04-04 09:35:04","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-10-02 18:55:36","canto_added_date":"2019-09-15 00:15:04","annotation_curators":[{"name":"Amanda Bird","community_curator":true,"annotation_count":14,"orcid":"0000-0002-1846-7050","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.05c","SPCC569.05c","SPAC977.16c","SPBC1348.06c","SPNCRNA.1710","SPBC16D10.06","SPAC25B8.19c","SPAC5H10.06c","SPCC794.01c","SPAC1F12.10c","SPBPB2B2.15","SPCC576.03c","SPAC2E1P3.05c"],"gene_count":13,"ltp_gene_count":1,"approved_date":"2019-10-14"},{"uniquename":"PMID:7681363","title":"Negative regulation of the wee1 protein kinase by direct action of the nim1/cdr1 mitotic inducer.","citation":"Cell 1993 Mar 26;72(6):919-29","abstract":"The wee1 protein kinase suppresses the entry into mitosis by mediating the inhibitory tyrosine phosphorylation of p34cdc2. Genetic studies have suggested that the nim1 protein kinase (also known as cdr1) acts as a positive regulator of mitosis by down-regulating the wee1 pathway in yeast cells. We have overexpressed the nim1 protein in both bacteria and insect cells. The recombinant nim1 protein autophosphorylates on both tyrosine and serine residues and can phosphorylate the isolated wee1 protein directly in a cell-free system. The nim1-catalyzed phosphorylation of the wee1 protein occurs in its C-terminal region and leads to a substantial drop in its activity as a cdc2-specific tyrosine kinase. This nim1-dependent inhibition of the wee1 protein kinase can be reversed readily in vitro by treatment with a protein phosphatase. These experiments provide direct biochemical evidence that the wee1 protein is subject to negative regulation by phosphorylation and indicate that the nim1 protein acts as an inhibitory, wee1-specific kinase.","authors":"Coleman TR, Tang Z, Dunphy WG","authors_abbrev":"Coleman TR et al.","pubmed_publication_date":"26 Mar 1993","pubmed_entrez_date":"1993-03-26","publication_year":"1993","canto_session_key":"99d738aeffea2fa6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-30 09:32:13","canto_approved_date":"2023-12-31 19:39:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-12 11:30:42","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC644.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-03-30"},{"uniquename":"PMID:26092938","title":"An actin-myosin-II interaction is involved in maintaining the contractile ring in fission yeast.","citation":"J Cell Sci 2015 Aug 01;128(15):2903-18","abstract":"The actomyosin-based contractile ring, which assembles at the cell equator, maintains its circularity during cytokinesis in many eukaryotic cells, ensuring its efficient constriction. Although consistent maintenance of the ring is one of the mechanisms underpinning cytokinesis, it has not yet been fully addressed. We here investigated the roles of fission yeast myosin-II proteins [Myo2 and Myo3 (also known as Myp2)] in ring maintenance during cytokinesis, with a focus on Myo3. A site-directed mutational analysis showed that the motor properties of Myo3 were involved in its accumulation in the contractile ring. The assembled ring was often deformed and not properly maintained under conditions in which the activities of myosin-II proteins localizing to the contractile ring were decreased, leading to inefficient cell division. Moreover, Myo3 appeared to form motile clusters on the ring. We propose that large assemblies of myosin-II proteins consolidate the contractile ring by continuously binding to F-actin in the ring, thereby contributing to its maintenance.","doi":"10.1242/jcs.171264","authors":"Takaine M, Numata O, Nakano K","authors_abbrev":"Takaine M et al.","pubmed_publication_date":"01 Aug 2015","pubmed_entrez_date":"2015-06-21","publication_year":"2015","canto_session_key":"f7db522593008e9c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masak Takaine","canto_first_approved_date":"2017-01-25 15:16:47","canto_approved_date":"2025-09-03 16:29:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-20 01:25:00","canto_added_date":"2015-06-22 00:20:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Masak Takaine","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPAC4A8.05c","SPCC645.05c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-01-25"},{"uniquename":"PMID:10090752","title":"Schizosaccharomyces pombe Aps1, a diadenosine 5',5' \"-P1, P6-hexaphosphate hydrolase that is a member of the nudix (MutT) family of hydrolases: cloning of the gene and characterization of the purified enzyme.","citation":"Biochemistry 1999 Mar 23;38(12):3649-55","abstract":"The fission yeast Schizosaccharomyces pombe contains a gene on chromosome I that encodes a hypothetical nudix hydrolase, YA9E. The gene, designated aps1, has been cloned and the protein has been purified from Escherichia coli with a yield of 10 mg of Aps1/L of culture. Aps1, composed of 210 amino acids with a calculated molecular mass of 23 724 Da, behaves as a monomer with a sedimentation coefficient of 1.92 S as determined by analytical ultracentrifugation. The effective hydrodynamic radius is about 29 A as determined by both analytical ultracentrifugation and gel-filtration chromatography. Aps1, whose expression was detected in S. pombe by Western blotting, is an enzyme that catalyzes the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4A from Ap6A and ADP and ATP from Ap5A. Values of Km for Ap6A and Ap5A are 19 microM and 22 microM, respectively, and the corresponding values of kcat are 2.0 s-1 and 1.7 s-1, respectively. The enzyme has limited activity on Ap4A and negligible activity on Ap3A, ADP-ribose, and NADH. Aps1 catalyzes the hydrolysis of mononucleotides with decreasing activity in order from p5A to AMP. Optimal activity with Ap6A as substrate is observed at pH 7.6 and in the presence of 0.1-1 mM MnCl2. Aps1 is the first nudix hydrolase isolated from S. pombe, and it is the first enzyme identified with this specific substrate specificity and reaction products.","authors":"Ingram SW, Stratemann SA, Barnes LD","authors_abbrev":"Ingram SW et al.","pubmed_publication_date":"23 Mar 1999","pubmed_entrez_date":"1999-03-26","publication_year":"1999","canto_session_key":"a14a41cb81cccbbe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-03-06 16:15:47","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-26 10:04:13","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G6.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-26"},{"uniquename":"PMID:5768841","title":"Electron microscopy study of cell structures and their changes during growth and regeneration of Schizosaccharomyces pombe protoplasts.","citation":"Folia Microbiol (Praha) 1969;14(2):155-64","abstract":"","authors":"Havelková M","authors_abbrev":"Havelková M","pubmed_publication_date":"1969","pubmed_entrez_date":"1969-01-01","publication_year":"1969","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1465447","title":"Repair of DNA damaged by UV light and ionizing radiation by cell-free extracts prepared from Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1992 Dec 15;89(24):12112-6","abstract":"A whole cell extract prepared from Schizosaccharomyces pombe was shown to be active in an assay for repair of plasmid DNA damaged by either ultraviolet (UV) light or gamma-radiation. The assay allows for analysis of repair synthesis at single-strand nicks generated by gamma-rays and analysis of the incision step and repair synthesis in UV-light-damaged DNA. Repair synthesis of DNA damaged by either UV light or gamma-rays was shown to depend on the presence of ATP in the reaction mixture. However, incision at pyrimidine dimers did not require the addition of exogenous ATP. These studies showed that plasmid DNA containing a single pyrimidine dimer or one single-strand nick is a suitable substrate in this assay system. S. pombe is a genetically well-defined eukaryotic organism and many radiation-sensitive mutant derivatives have already been described, making this a powerful system in which to study DNA excision repair.","authors":"Sidik K, Lieberman HB, Freyer GA","authors_abbrev":"Sidik K et al.","pubmed_publication_date":"15 Dec 1992","pubmed_entrez_date":"1992-12-15","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21357609","title":"Identification and characterization of the mitochondrial RNA polymerase and transcription factor in the fission yeast Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2011 Jul;39(12):5119-30","abstract":"We have characterized the mitochondrial transcription factor (Mtf1) and RNA polymerase (Rpo41) of Schizosaccharomyces pombe. Deletion mutants show Mtf1 or Rpo41 to be essential for cell growth, cell morphology and mitochondrial membrane potential. Overexpression of Mtf1 and Rpo41 can induce mitochondrial transcription. Mtf1 and Rpo41 can bind and transcribe mitochondrial promoters in vitro and the initiating nucleotides were the same in vivo and in vitro. Mtf1 is required for efficient transcription. We discuss the functional differences between Mtf1 and Rpo41 of S. pombe with Saccharomyces cerevisiae and higher organisms. In contrast to S. cerevisiae, the established model for mitochondrial transcription, S. pombe, a petite-negative yeast, resembles higher organisms that cannot tolerate the loss of mitochondrial function. The S. pombe and human mitochondrial genomes are similar in size and much smaller than that of S. cerevisiae. This is an important first step in the development of S. pombe as an alternative and complementary model system for molecular genetic and biochemical studies of mitochondrial transcription and mitochondrial-nuclear interactions. This is the first systematic study of the cellular function and biochemistry of Rpo41 and Mtf1 in S. pombe.","doi":"10.1093/nar/gkr103","authors":"Jiang H, Sun W, Wang Z, Zhang J, Chen D, Murchie AI","authors_abbrev":"Jiang H et al.","pubmed_publication_date":"Jul 2011","pubmed_entrez_date":"2011-03-02","publication_year":"2011","canto_session_key":"a509333787c2c0d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-02 13:15:00","canto_approved_date":"2025-09-04 07:22:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-28 14:52:33","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26H5.12","SPAC1002.08c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-11-02"},{"uniquename":"PMID:1672838","title":"Microtubules in the fission yeast Schizosaccharomyces pombe contain only the tyrosinated form of alpha-tubulin.","citation":"Cell Motil Cytoskeleton 1991;18(2):86-93","abstract":"The state of tubulin tyrosination in the fission yeast Schizosaccharomyces pombe was investigated using a combination of indirect immunofluorescence microscopy and Western blotting. Antibodies specific for the tyrosinated form of alpha-tubulin stained all microtubule arrays in wild type cells and recognised the two alpha-tubulin polypeptides in Western blots of cell extracts enriched for tubulin by DEAE-Sephadex chromatography. Antisera that specifically recognised the detyrosinated, glu, form, on the other hand, gave consistently negative results, both in cells undergoing rapid exponential growth and in those allowed to accumulate in stationary phase. Neither the \"ageing\" of microtubules, by arresting cells at different points (late G1 or G2/M) in the cell division cycle, nor stabilising them, using D2O, lead to any detectable tubulin detryrosination. These results suggest that S. pombe lacks the carboxypeptidase that carries out the tubulin detyrosination reaction. This is the first report of an organism that possesses the correct C-terminal alpha-tubulin sequence yet fails to carry out this post-translational modification. The implication of this novel finding for the biological role of these events is discussed.","authors":"Alfa CE, Hyams JS","authors_abbrev":"Alfa CE et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30664646","title":"Cellular geometry scaling ensures robust division site positioning.","citation":"Nat Commun 2019 Jan 21;10(1):268","abstract":"Cells of a specific cell type may divide within a certain size range. Yet, functionally optimal cellular organization is typically maintained across different cell sizes, a phenomenon known as scaling. The mechanisms underlying scaling and its physiological significance remain elusive. Here we approach this problem by interfering with scaling in the rod-shaped fission yeast Schizosaccharomyces japonicus that relies on cellular geometry cues to position the division site. We show that S. japonicus uses the Cdc42 polarity module to adjust its geometry to changes in the cell size. When scaling is prevented resulting in abnormal cellular length-to-width aspect ratio, cells exhibit severe division site placement defects. We further show that despite the generally accepted view, a similar scaling phenomenon can occur in the sister species, Schizosaccharomyces pombe. Our results demonstrate that scaling is required for normal cell function and delineate possible rules for cellular geometry maintenance in populations of proliferating cells.","doi":"10.1038/s41467-018-08218-2","authors":"Gu Y, Oliferenko S","authors_abbrev":"Gu Y et al.","pubmed_publication_date":"21 Jan 2019","pubmed_entrez_date":"2019-01-22","publication_year":"2019","canto_session_key":"1273d24d151c9db5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-01-23 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24551071","title":"Asymmetric segregation of damaged cellular components in spatially structured multicellular organisms.","citation":"PLoS One 2014;9(2):e87917","abstract":"The asymmetric distribution of damaged cellular components has been observed in species ranging from fission yeast to humans. To study the potential advantages of damage segregation, we have developed a mathematical model describing ageing mammalian tissue, that is, a multicellular system of somatic cells that do not rejuvenate at cell division. To illustrate the applicability of the model, we specifically consider damage incurred by mutations to mitochondrial DNA, which are thought to be implicated in the mammalian ageing process. We show analytically that the asymmetric distribution of damaged cellular components reduces the overall damage level and increases the longevity of the cell population. Motivated by the experimental reports of damage segregation in human embryonic stem cells, dividing symmetrically with respect to cell-fate, we extend the model to consider spatially structured systems of cells. Imposing spatial structure reduces, but does not eliminate, the advantage of asymmetric division over symmetric division. The results suggest that damage partitioning could be a common strategy for reducing the accumulation of damage in a wider range of cell types than previously thought.","doi":"10.1371/journal.pone.0087917","authors":"Strandkvist C, Juul J, Bendtsen KM","authors_abbrev":"Strandkvist C et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-20","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22918954","title":"Characterization of structural and functional domains of the anillin-related protein Mid1p that contribute to cytokinesis in fission yeast.","citation":"Mol Biol Cell 2012 Oct;23(20):3993-4007","abstract":"Fission yeast cells depend on the anillin-related protein Mid1p for reliable cytokinesis. Insolubility limits the purification of full-length Mid1p for biophysical analysis, and lack of knowledge about the structural domains of Mid1p limits functional analysis. We addressed these limitations by identifying in a bacterial expression screen of random Mid1p fragments five soluble segments that can be purified and one insoluble segment. Using complementation experiments in Δmid1 cells, we tested the biological functions of these six putative domains that account for full-length Mid1p. The N-terminal domain (residues 1-149) is essential for correct positioning and orientation of septa. The third domain (residues 309-452) allows the construct composed of the first three domains (residues 1-452) to form hydrodynamically well-behaved octamers. Constructs consisting of residues 1-452 or 1-578 carry out most functions of full-length Mid1p, including concentration at the equatorial cortex in nodes that accumulate myosin-II and other contractile ring proteins during mitosis. However, cells depending on these constructs without the insoluble domain (residues 579-797) form equatorially located rings slowly from strands rather than by direct condensation of nodes. We conclude that residues 1-578 assemble node components myosin-II, Rng2p, and Cdc15p, and the insoluble domain facilitates the normal, efficient condensation of nodes into rings.","doi":"10.1091/mbc.E12-07-0536","authors":"Saha S, Pollard TD","authors_abbrev":"Saha S et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-25","publication_year":"2012","canto_session_key":"38a5be55b66fa29b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-04-01 11:08:17","canto_approved_date":"2023-03-10 07:50:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-31 17:45:00","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-04-01"},{"uniquename":"PMID:35612306","title":"Smc5/6 Complex Promotes Rad3 ATR  Checkpoint Signaling at the Perturbed Replication Fork through Sumoylation of the RecQ Helicase Rqh1.","citation":"Mol Cell Biol 2022 Jun 16;42(6):e0004522","abstract":"Smc5/6, like cohesin and condensin, is a structural maintenance of chromosomes complex crucial for genome stability. Unlike cohesin and condensin, Smc5/6 carries an essential Nse2 subunit with SUMO E3 ligase activity. While screening for new DNA replication checkpoint mutants in fission yeast, we have identified two previously uncharacterized mutants in Smc5/6. Characterization of the mutants and a series of previously reported Smc5/6 mutants uncovered that sumoylation of the RecQ helicase Rqh1 by Nse2 facilitates the checkpoint signaling at the replication fork. We found that mutations that eliminate the sumoylation sites or the helicase activity of Rqh1 compromised the checkpoint signaling similar to a  nse2  mutant lacking the ligase activity. Surprisingly, introducing a sumoylation site mutation to a helicase-inactive  rqh1  mutant promoted cell survival under stress. These findings, together with other genetic data, support a mechanism that sumoylation of Rqh1 by Smc5/6-Nse2 recruits Rqh1 or modulates its helicase activity at the fork to facilitate the checkpoint signaling. Since the Smc5/6 complex, Rqh1, and the replication checkpoint are conserved in eukaryotes, a similar checkpoint mechanism may be operating in human cells.","doi":"10.1128/mcb.00045-22","authors":"Khan S, Ahamad N, Bhadra S, Xu Z, Xu YJ","authors_abbrev":"Khan S et al.","pubmed_publication_date":"16 Jun 2022","pubmed_entrez_date":"2022-05-25","publication_year":"2022","canto_session_key":"3cf2b08c5a03d380","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-05-27 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC1259.13","SPAC16A10.06c","SPAC2G11.12","SPBC216.05"],"gene_count":5,"ltp_gene_count":0},{"uniquename":"PMID:20233411","title":"Phylogenetic analysis of fungal ABC transporters.","citation":"BMC Genomics 2010 Mar 16;11:177","abstract":"The superfamily of ABC proteins is among the largest known in nature. Its members are mainly, but not exclusively, involved in the transport of a broad range of substrates across biological membranes. Many contribute to multidrug resistance in microbial pathogens and cancer cells. The diversity of ABC proteins in fungi is comparable with those in multicellular animals, but so far fungal ABC proteins have barely been studied.\nWe performed a phylogenetic analysis of the ABC proteins extracted from the genomes of 27 fungal species from 18 orders representing 5 fungal phyla thereby covering the most important groups. Our analysis demonstrated that some of the subfamilies of ABC proteins remained highly conserved in fungi, while others have undergone a remarkable group-specific diversification. Members of the various fungal phyla also differed significantly in the number of ABC proteins found in their genomes, which is especially reduced in the yeast S. cerevisiae and S. pombe.\nData obtained during our analysis should contribute to a better understanding of the diversity of the fungal ABC proteins and provide important clues about their possible biological functions.","doi":"10.1186/1471-2164-11-177","authors":"Kovalchuk A, Driessen AJ","authors_abbrev":"Kovalchuk A et al.","pubmed_publication_date":"16 Mar 2010","pubmed_entrez_date":"2010-03-18","publication_year":"2010","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:X75072","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013494","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20854854","title":"Production of heterologous glycoproteins by a glycosylation-defective alg3och1 mutant of Schizosaccharomyces pombe.","citation":"J Biotechnol 2010 Nov;150(3):348-56","abstract":"The early stages of N-linked glycosylation are highly conserved between fungal and mammalian cells. Such N-linked oligosaccharides are synthesized through the ordered assembly of a dolichyl pyrophosphate (Dol-PP)-linked Glc(3)Man(9)GlcNAc(2) structure by the sequential actions of several glycosyltransferases located in the endoplasmic reticulum (ER). Of the glycosyltransferase genes, Saccharomyces cerevisiae ALG3 has been identified to encode the Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol α1,3-mannosyltransferase, and an alg3 mutant has been shown to accumulate an Endo H-resistant M5B (Manα1,2-Manα1,2-Manα1,3(Manα1,6-)-Manβ1,4-GlcNAcβ1,4-GlcNAc) structure. Although Schizosaccharomyces pombe contains a homolog of the ALG3 gene (SPAC7D4.06c), the role of this gene in oligosaccharide biosynthesis is not at all clear. In this study, we deleted the alg3(+) gene in the och1Δ mutant and analyzed the detailed oligosaccharide structures in alg3Δoch1Δ double mutant. The oligosaccharides were prepared from cell-surface glycoproteins by hydrazinolysis and fluorescent labeling with 2-aminopyridine. The labeled oligosaccharides were analyzed by high performance liquid chromatography, in combination with sequential glycosidase digestion and methylation analysis. These analyses revealed that the N-linked oligosaccharides of S. pombe alg3Δoch1Δ cells mainly consisted of two or three α-galactose-capped M5B structures. Finally, western blot analysis of recombinant human transferrin suggested that heterologously expressed glycoproteins in alg3Δoch1Δ cells have Endo H-resistant N-linked oligosaccharide structures similar to those of alg3Δoch1Δ cell-surface glycoproteins.","doi":"10.1016/j.jbiotec.2010.09.942","authors":"Ohashi T, Nakakita S, Sumiyoshi W, Takegawa K","authors_abbrev":"Ohashi T et al.","pubmed_publication_date":"Nov 2010","pubmed_entrez_date":"2010-09-22","publication_year":"2010","canto_session_key":"3e7e104742b500a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-31 11:41:13","canto_approved_date":"2025-10-07 06:51:38","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-10-30 18:05:23","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC7D4.06c","SPAC1006.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-10-31"},{"uniquename":"PMID:25266290","title":"Mammalian CORVET is required for fusion and conversion of distinct early endosome subpopulations.","citation":"Traffic 2014 Dec;15(12):1366-89","abstract":"Early endosomes are organized in a network of vesicles shaped by cycles of fusion, fission, and conversion to late endosomes. In yeast, endosome fusion and conversion are regulated, among others, by CORVET, a hexameric protein complex. In the mammalian endocytic system, distinct subpopulations of early endosomes labelled by the Rab5 effectors APPL1 and EEA1 are present. Here, the function of mammalian CORVET with respect to these endosomal subpopulations was investigated. Tgfbrap1 as CORVET-specific subunit and functional ortholog of Vps3p was identified, demonstrating that it is differentially distributed between APPL1 and EEA1 endosomes. Surprisingly, depletion of CORVET-specific subunits caused fragmentation of APPL1-positive endosomes but not EEA1 endosomes in vivo. These and in vitro data suggest that CORVET plays a role in endosome fusion independently of EEA1. Depletion of CORVET subunits caused accumulation of large EEA1 endosomes indicative of another role in the conversion of EEA1 endosomes into late endosomes. In addition, depletion of CORVET-specific subunits caused alterations in transport depending on both the type of cargo and the specific endosomal subpopulation. These results demonstrate that CORVET plays distinct roles at multiple stages in the mammalian endocytic pathway.","doi":"10.1111/tra.12232","authors":"Perini ED, Schaefer R, Stöter M, Kalaidzidis Y, Zerial M","authors_abbrev":"Perini ED et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-10-01","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC364.05","HGNC:16836"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:U72150","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38448160","title":"Phosphorylation of Rec8 cohesin complexes regulates mono-orientation of kinetochores in meiosis I.","citation":"Life Sci Alliance 2024 May;7(5)","abstract":"In meiosis I, unlike in mitosis, sister kinetochores are captured by microtubules emanating from the same spindle pole (mono-orientation) and centromeric cohesion mediated by cohesin is protected in the following anaphase I. The conserved meiosis-specific kinetochore protein meikin (Moa1 in fission yeast) associates with polo-like kinase: Plo1 and regulates both mono-orientation and cohesion protection. Although the phosphorylation of Rec8-S450 by Plo1 associated with Moa1 plays a key role in cohesion protection, how Moa1-Plo1 regulates mono-orientation remains elusive. Here, we identify Plo1 phosphorylation sites in the cohesin subunits, Rec8 and Psm3. The non-phosphorylatable mutations at these sites showed specific defects in mono-orientation. These results enabled the genetic dissection of meikin functions at the centromeres.","doi":"10.26508/lsa.202302556","authors":"Liu Y, Min Y, Liu Y, Watanabe Y","authors_abbrev":"Liu Y et al.","pubmed_publication_date":"May 2024","pubmed_entrez_date":"2024-03-06","publication_year":"2024","canto_session_key":"f0575bfe108d54e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2024-03-31 08:31:22","canto_approved_date":"2024-05-16 14:08:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-26 07:44:09","canto_added_date":"2024-03-09 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":39,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPBC29A10.14","SPAC10F6.09c","SPBC428.17c","SPAC31A2.05c","SPAC15E1.07c","SPAC110.02","SPAC23C11.16"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2024-03-31"},{"uniquename":"PMID:1896017","title":"Isolation, characterisation and molecular cloning of new mutant alleles of the fission yeast p34cdc2+ protein kinase gene: identification of temperature-sensitive G2-arresting alleles.","citation":"Mol Gen Genet 1991 Sep;229(1):109-18","abstract":"The protein serine-threonine kinase p34cdc2+ plays a central role in the control of the mitotic cell cycle of the fission yeast Schizosaccharomyces pombe. p34cdc2+ function is required both for the initiation of DNA replication and for entry into mitosis, and is also required for the initiation of the second meiotic nuclear division. Recent extensive analysis of p34cdc2+ homologue proteins in higher eukaryotes has demonstrated that p34cdc2+ function is likely to be conserved in all eukaryotic cells. Here we report the isolation and characterisation of five new temperature-sensitive alleles of the cdc2+ gene. All five have been cloned and sequenced, together with the meiotically defective cdc2-N22 allele, bringing the total of p34cdc2+ mutants cloned in this and previous reports to seventeen. The five temperature-sensitive alleles define four separate mutations within the p34cdc2+ protein sequence, two of which give rise to cell cycle arrest in G2 only, when shifted to the restrictive temperature. The nature of the mutation in each protein is described and possible implications for the structure and function of p34cdc2+ discussed.","authors":"MacNeill SA, Creanor J, Nurse P","authors_abbrev":"MacNeill SA et al.","pubmed_publication_date":"Sep 1991","pubmed_entrez_date":"1991-09-01","publication_year":"1991","canto_session_key":"0fdb9d39a84d84ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ryoko Mandeville","canto_first_approved_date":"2013-04-19 07:47:02","canto_approved_date":"2021-03-23 17:08:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-07-09 15:47:43","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ryoko Mandeville","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC1734.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-04-19"},{"uniquename":"PMID:25579976","title":"Phosphorylation of cohesin Rec11/SA3 by casein kinase 1 promotes homologous recombination by assembling the meiotic chromosome axis.","citation":"Dev Cell 2015 Jan 26;32(2):220-30","abstract":"In meiosis, cohesin is required for sister chromatid cohesion, as well as meiotic chromosome axis assembly and recombination. However, mechanisms underlying the multifunctional nature of cohesin remain elusive. Here, we show that fission yeast casein kinase 1 (CK1) plays a crucial role in assembling the meiotic chromosome axis (so-called linear element: LinE) and promoting recombination. An in vitro phosphorylation screening assay identified meiotic cohesin subunit Rec11/SA3 as an excellent substrate of CK1. The phosphorylation of Rec11 by CK1 mediates the interaction with the Rec10/Red1/SCP2 axis component, a key step in meiotic chromosome axis assembly, and is dispensable for sister chromatid cohesion. Crucially, the expression of Rec11-Rec10 fusion protein nearly completely bypasses the requirement for CK1 or cohesin phosphorylation for LinE assembly and recombination. This study uncovers a central mechanism of the cohesin-dependent assembly of the meiotic chromosome axis and recombination apparatus that acts independently of sister chromatid cohesion.","doi":"10.1016/j.devcel.2014.11.033","authors":"Sakuno T, Watanabe Y","authors_abbrev":"Sakuno T et al.","pubmed_publication_date":"26 Jan 2015","pubmed_entrez_date":"2015-01-13","publication_year":"2015","canto_session_key":"ed7f95ec599f51aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takeshi Sakuno","canto_first_approved_date":"2018-03-09 16:32:58","canto_approved_date":"2024-04-13 07:37:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-01 07:34:09","canto_added_date":"2015-01-14 01:15:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":46,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Takeshi Sakuno","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.12","SPBC29A10.14","SPBC1718.02","SPBC577.05c","SPBC36B7.06c","SPBC21B10.12","SPAC25G10.04c","SPBP35G2.03c","SPCC4E9.01c","SPAC15E1.07c","SPAC17A5.11","SPAC17A5.18c","SPBC3H7.15"],"gene_count":13,"ltp_gene_count":9,"approved_date":"2018-03-09"},{"uniquename":"PMID:18621924","title":"Regulation of the subcellular localization of cyclic AMP-dependent protein kinase in response to physiological stresses and sexual differentiation in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2008 Sep;7(9):1450-9","abstract":"We describe regulation of the subcellular localization of cyclic AMP (cAMP)-dependent protein kinase (PKA) regulatory (Cgs1p) and catalytic (Pka1p) subunits in the fission yeast Schizosaccharomyces pombe in response to physiological stresses and during sexual differentiation as determined by fluorescence microscopy of the Cgs1-green fluorescent protein (GFP) and Pka1-GFP fusion proteins, respectively. In wild-type S. pombe cells cultured to log phase under normal growth conditions, Cgs1p and Pka1p are concentrated in the nucleus and more diffusely present in the cytoplasm. Nuclear localization of both proteins is dependent on cAMP, since in cells lacking adenylate cyclase they are detectable only in the cytoplasm. In cells lacking Cgs1p or both Cgs1p and adenylate cyclase, Pka1p is concentrated in the nucleus, demonstrating a role for Cgs1p in the nuclear exclusion of Pka1p. Nuclear-cytoplasmic redistribution of Cgs1p and Pka1p is triggered by growth in glucose-limited or hyperosmotic media and in response to stationary-phase growth. In addition, both proteins are excluded from the nucleus in mating cells undergoing karyogamy and subsequently concentrated in postmeiotic spores. Cgs1p is required for subcellular redistribution of Pka1p induced by growth in glucose-limited and hyperosmotic media and during karyogamy but is not required for Pka1p redistribution triggered by stationary-phase growth or for the enrichment of Pka1p in spores. Our results demonstrate that PKA localization is regulated by cAMP and regulatory subunit-dependent and -independent mechanisms in S. pombe.","doi":"10.1128/EC.00168-08","authors":"Matsuo Y, McInnis B, Marcus S","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-07-16","publication_year":"2008","canto_session_key":"fea227a10e1c6a8d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-23 10:34:04","canto_approved_date":"2020-01-23 12:41:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-23 10:33:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPAC8C9.03","SPBC106.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-02-23"},{"uniquename":"PMID:25528445","title":"Transcriptional profiling analysis of individual kinase-deletion strains of fission yeast in response to nitrogen starvation.","citation":"Mol Genet Genomics 2015 Jun;290(3):1067-83","abstract":"Nitrogen starvation (NS) induces sexual development when mating partners are available or enter into quiescent state (G0) in heterothallic background in fission yeast. However, little is known whether the two processes share common signaling molecules or cells defective in the two processes share common transcriptional signatures. To address these questions, we first assessed 77 kinase-deletion strains for NS-induced G0-arrest phenotypes. Our result indicated that 10 out of 77 kinase-deletion strains exhibited defect in G0-arrest, only 3 of which were defective in sexual development based on a previous study, suggesting that the two processes hardly share common signaling components. We subsequently performed transcriptional profiling analysis. Our result indicated that NS-induced transcriptional change was so robust that it prevailed the alteration by individual kinase-deletion alleles. Based on comparison between kinase-deletion strains proficient and deficient in sexual development or G0-arrest, we identified subsets of genes that were associated with sexual development-deficient or G0-arrest-deficient kinase-deletion strains. Multiple pairing analyses allowed grouping of functional related kinases. Furthermore, we showed that Pka1-mediated pathways were required for upregulation of NS-induced genes upon NS and downregulation of the same set of genes under the N-replete conditions. Taken together, our analyses indicate that sexual development and NS-induced G0-arrest are unrelated; and sexual development-deficient and G0-arrest-deficient kinase-deletion strains possess distinct transcriptional signatures. We propose that Pka1 is a key regulator of nitrogen metabolic pathways and Pka1-mediated signaling pathways play roles in regulation of NS-induced genes under both N-depleted and N-replete conditions.","doi":"10.1007/s00438-014-0966-6","authors":"Liu J, Jia Y, Li J, Chu Z","authors_abbrev":"Liu J et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2014-12-22","publication_year":"2015","canto_session_key":"b5456b0a95d3a4d2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-12-23 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38203781","title":"Cytoophidia Influence Cell Cycle and Size in  Schizosaccharomyces pombe .","citation":"Int J Mol Sci 2024 Jan 03;25(1)","abstract":"Cytidine triphosphate synthase (CTPS) forms cytoophidia in all three domains of life. Here we focus on the function of cytoophidia in cell proliferation using  Schizosaccharomyces pombe  as a model system. We find that converting His 359  of CTPS into Ala 359  leads to cytoophidium disassembly. By reducing the level of CTPS protein or specific mutation, the loss of cytoophidia prolongs the G2 phase and expands cell size. In addition, the loss-filament mutant of CTPS leads to a decrease in the expression of genes related to G2/M transition and cell growth, including histone chaperone  slm9 . The overexpression of  slm9  alleviates the G2 phase elongation and cell size enlargement induced by CTPS loss-filament mutants. Overall, our results connect cytoophidia with cell cycle and cell size control in  Schizosaccharomyces pombe .","doi":"10.3390/ijms25010608","authors":"Deng R, Li YL, Liu JL","authors_abbrev":"Deng R et al.","pubmed_publication_date":"03 Jan 2024","pubmed_entrez_date":"2024-01-11","publication_year":"2024","canto_session_key":"c19987873a850b39","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-01-12 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC15D4.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21303925","title":"Electron tomography reveals a flared morphology on growing microtubule ends.","citation":"J Cell Sci 2011 Mar 01;124(Pt 5):693-8","abstract":"Microtubules (MTs) exhibit dynamic instability, alternating between phases of growth and shortening, mostly at their uncapped plus ends. Based on results from cryo-electron microscopy it was proposed that growing MTs display mainly curved sheets and blunt ends; during depolymerisation curled 'ramshorns' predominate. Observations of MTs in mitotic cells have suggested that the situation in vivo differs from that in vitro, but so far, a clear comparison between in vivo and in vitro results has not been possible because MT end structures could not be correlated directly with the dynamic state of that particular MT. Here we combine light microscopy and electron tomography (ET) to show that growing MT plus ends in the fission yeast Schizosaccharomyces pombe display predominantly a flared morphology. This indicates that MT polymerisation in vivo and in vitro can follow different paths.","doi":"10.1242/jcs.072967","authors":"Höög JL, Huisman SM, Sebö-Lemke Z, Sandblad L, McIntosh JR, Antony C, Brunner D","authors_abbrev":"Höög JL et al.","pubmed_publication_date":"01 Mar 2011","pubmed_entrez_date":"2011-02-10","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17362205","title":"Dsk1p kinase phosphorylates SR proteins and regulates their cellular localization in fission yeast.","citation":"Biochem J 2007 Jul 01;405(1):21-30","abstract":"Evolutionarily conserved SR proteins (serine/arginine-rich proteins) are important factors for alternative splicing and their activity is modulated by SRPKs (SR protein-specific kinases). We previously identified Dsk1p (dis1-suppressing protein kinase) as the orthologue of human SRPK1 in fission yeast. In addition to its similarity of gene structure to higher eukaryotes, fission yeast Schizosaccharomyces pombe is a unicellular eukaryotic organism in which alternative splicing takes place. In the present study, we have revealed for the first time that SR proteins, Srp1p and Srp2p, are the in vivo substrates of Dsk1p in S. pombe. Moreover, the cellular localization of the SR proteins and Prp2p splicing factor is dependent on dsk1(+): Dsk1p is required for the efficient nuclear localization of Srp2p and Prp2p, while it promotes the cytoplasmic distribution of Srp1p, thereby differentially influencing the destinations of these proteins in the cell. The present study offers the first biochemical and genetic evidence for the in vivo targets of the SRPK1 orthologue, Dsk1p, in S. pombe and the significant correlation between Dsk1p-mediated phosphorylation and the cellular localization of the SR proteins, providing information about the physiological functions of Dsk1p. Furthermore, the results demonstrate that the regulatory function of SRPKs in the nuclear targeting of SR proteins is conserved from fission yeast to human, indicating a general mechanism of reversible phosphorylation to control the activities of SR proteins in RNA metabolism through cellular partitioning.","authors":"Tang Z, Tsurumi A, Alaei S, Wilson C, Chiu C, Oya J, Ngo B","authors_abbrev":"Tang Z et al.","pubmed_publication_date":"01 Jul 2007","pubmed_entrez_date":"2007-03-17","publication_year":"2007","canto_session_key":"9dcc2301b378df4a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-15 10:48:00","canto_approved_date":"2023-12-24 11:04:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-23 10:45:45","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.11c","SPBC530.14c","SPBC146.07","SPAC16.02c","SPBC11C11.08"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-09-15"},{"uniquename":"EMBL:AU008586","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18378696","title":"Molecular characterization of the role of the Schizosaccharomyces pombe nip1+/ctp1+ gene in DNA double-strand break repair in association with the Mre11-Rad50-Nbs1 complex.","citation":"Mol Cell Biol 2008 Jun;28(11):3639-51","abstract":"The Schizosaccharomyces pombe nip1(+)/ctp1(+) gene was previously identified as an slr (synthetically lethal with rad2) mutant. Epistasis analysis indicated that Nip1/Ctp1 functions in Rhp51-dependent recombinational repair, together with the Rad32 (spMre11)-Rad50-Nbs1 complex, which plays important roles in the early steps of DNA double-strand break repair. Nip1/Ctp1 was phosphorylated in asynchronous, exponentially growing cells and further phosphorylated in response to bleomycin treatment. Overproduction of Nip1/Ctp1 suppressed the DNA repair defect of an nbs1-s10 mutant, which carries a mutation in the FHA phosphopeptide-binding domain of Nbs1, but not of an nbs1 null mutant. Meiotic DNA double-strand breaks accumulated in the nip1/ctp1 mutant. The DNA repair phenotypes and epistasis relationships of nip1/ctp1 are very similar to those of the Saccharomyces cerevisiae sae2/com1 mutant, suggesting that Nip1/Ctp1 is a functional homologue of Sae2/Com1, although the sequence similarity between the proteins is limited to the C-terminal region containing the RHR motif. We found that the RxxL and CxxC motifs are conserved in Schizosaccharomyces species and in vertebrate CtIP, originally identified as a cofactor of the transcriptional corepressor CtBP. However, these two motifs are not found in other fungi, including Saccharomyces and Aspergillus species. We propose that Nip1/Ctp1 is a functional counterpart of Sae2/Com1 and CtIP.","doi":"10.1128/MCB.01828-07","authors":"Akamatsu Y, Murayama Y, Yamada T, Nakazaki T, Tsutsui Y, Ohta K, Iwasaki H","authors_abbrev":"Akamatsu Y et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-02","publication_year":"2008","canto_session_key":"94b54d8b1a931fb9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-03-31 13:13:15","canto_approved_date":"2023-09-21 09:45:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-18 10:29:10","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":46,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_18378696_phaf.tsv"}],"genes":["SPCC18B5.11c","SPBC6B1.09c","SPAC644.14c","SPAC664.07c","SPAC20H4.07","SPCC1259.13","SPBC216.05","SPAC14C4.13","SPCC126.02c","SPCC338.08","SPAC694.06c","SPAC17A5.11","SPAC9E9.08","SPAC1952.07","SPBC342.05","SPAC13C5.07","SPCC23B6.03c","SPAC3G6.06c"],"gene_count":18,"ltp_gene_count":18,"approved_date":"2017-03-31"},{"uniquename":"PMID:11016847","title":"Schizosaccharomyces pombe ehs1p is involved in maintaining cell wall integrity and in calcium uptake.","citation":"Mol Gen Genet 2000 Sep;264(1-2):173-83","abstract":"The Schizosaccharomyces pombe mutant ehs1-1 mutant was isolated on the basis of its hypersensitivity to Echinocandin and Calcofluor White, which inhibit cell wall synthesis. The mutant shows a thermosensitive growth phenotype that is suppressed in the presence of an osmotic stabiliser. The mutant also showed other cell wall-associated phenotypes, such as enhanced sensitivity to enzymatic cell wall degradation and an imbalance in polysaccharide synthesis. The ehs1 + gene encodes a predicted integral membrane protein that is 30% identical to Saccharomyces cerevisiae Mid1p, a protein that has been proposed to form part of a calcium channel. As expected for such a function, we found that ehs1+ is involved in intracellular Ca2+ accumulation. High external Ca2+ concentrations suppressed all phenotypes associated with the ehs1 null mutation, suggesting that the cell integrity defects of ehs1 mutants result from inadequate levels of calcium in the cell. We observed a genetic relationship between ehs1+ and the protein kinase C homologue pck2+. pck2+ suppressed all phenotypes of ehs1-1 mutant cells. Overproduction of pck2p is deleterious to wild-type cells, increasing 1,3-beta-D-glucan synthase activity and promoting accumulation of extremely high levels of Ca2+. The lethality associated with pck2p, the increase in 1,3-beta-D-glucan synthase production and the strong Ca2+ accumulation are all dependent on the presence of ehs1p. Our results suggest that in fission yeast ehs1p forms part of a calcium channel that is involved in the cell wall integrity pathway that includes the kinase pck2p.","authors":"Carnero E, Ribas JC, García B, Durán A, Sánchez Y","authors_abbrev":"Carnero E et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-10-04","publication_year":"2000","canto_session_key":"373f4c6a1e37adf9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-07-13 10:54:39","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-07-09 14:53:00","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":56,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.08c","SPAC17G8.14c","SPBC12D12.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-07-09"},{"uniquename":"PMID:10978320","title":"The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II.","citation":"J Biol Chem 2000 Dec 22;275(51):39935-43","abstract":"We showed previously that the WW domain of the prolyl isomerase, Ess1, can bind the phosphorylated carboxyl-terminal domain (phospho-CTD) of the largest subunit of RNA Polymerase II. Analysis of phospho-CTD binding by four other WW domain-containing Saccharomyces cerevisiae proteins indicates the splicing factor, Prp40, and the RNA polymerase II ubiquitin ligase, Rsp5, can also bind the phospho-CTD. The identification of Prp40 as a phospho-CTD binding protein represents the first demonstration of direct interaction between a documented splicing factor and the phospho-CTD. Domain dissection studies reveal that phospho-CTD binding occurs at multiple locations in Prp40, including sites in both the WW and FF domain regions. Because the conserved repeats of the CTD make it an ideal ligand for multi-site binding events, the implications of multi-site binding are discussed. Our data suggest a mechanism by which the phospho-CTD of elongating RNA polymerase II facilitates commitment complex formation by juxtaposing the 5' and 3' splice sites.","authors":"Morris DP, Greenleaf AL","authors_abbrev":"Morris DP et al.","pubmed_publication_date":"22 Dec 2000","pubmed_entrez_date":"2000-09-09","publication_year":"2000","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4D7.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33175606","title":"Calcium spikes accompany cleavage furrow ingression and cell separation during fission yeast cytokinesis.","citation":"Mol Biol Cell 2021 Jan 01;32(1):15-27","abstract":"The role of calcium signaling in cytokinesis has long remained ambiguous. Past studies of embryonic cell division discovered that calcium concentration increases transiently at the division plane just before cleavage furrow ingression, suggesting that these calcium transients could trigger contractile ring constriction. However, such calcium transients have only been found in animal embryos and their function remains controversial. We explored cytokinetic calcium transients in the fission yeast  Schizosaccharomyces pombe  by adopting GCaMP, a genetically encoded calcium indicator, to determine the intracellular calcium level of this model organism. We validated GCaMP as a highly sensitive calcium reporter in fission yeast, allowing us to capture calcium transients triggered by osmotic shocks. We identified a correlation between the intracellular calcium level and cell division, consistent with the existence of calcium transients during cytokinesis. Using time-lapse microscopy and quantitative image analysis, we discovered calcium spikes both at the start of cleavage furrow ingression and the end of cell separation. Inhibition of these calcium spikes slowed the furrow ingression and led to frequent lysis of daughter cells. We conclude that like the larger animal embryos, fission yeast triggers calcium transients that may play an important role in cytokinesis (197).","doi":"10.1091/mbc.E20-09-0609","authors":"Poddar A, Sidibe O, Ray A, Chen Q","authors_abbrev":"Poddar A et al.","pubmed_publication_date":"01 Jan 2021","pubmed_entrez_date":"2020-11-11","publication_year":"2021","canto_session_key":"a37028485cb56a1b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Qian Chen","canto_first_approved_date":"2020-12-18 13:59:13","canto_approved_date":"2020-12-18 13:59:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-16 19:16:04","canto_added_date":"2020-11-13 01:15:05","annotation_curators":[{"name":"Qian Chen","community_curator":true,"annotation_count":1,"orcid":"0000-0002-2768-6570","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31E1.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-12-18"},{"uniquename":"PMID:28986587","title":"The drinking water contaminant dibromoacetonitrile delays G1-S transition and suppresses Chk1 activation at broken replication forks.","citation":"Sci Rep 2017 Oct 06;7(1):12730","abstract":"Chlorination of drinking water protects humans from water-born pathogens, but it also produces low concentrations of dibromoacetonitrile (DBAN), a common disinfectant by-product found in many water supply systems. DBAN is not mutagenic but causes DNA breaks and elevates sister chromatid exchange in mammalian cells. The WHO issued guidelines for DBAN after it was linked with cancer of the liver and stomach in rodents. How this haloacetonitrile promotes malignant cell transformation is unknown. Using fission yeast as a model, we report here that DBAN delays G1-S transition. DBAN does not hinder ongoing DNA replication, but specifically blocks the serine 345 phosphorylation of the DNA damage checkpoint kinase Chk1 by Rad3 (ATR) at broken replication forks. DBAN is particularly damaging for cells with defects in the lagging-strand DNA polymerase delta. This sensitivity can be explained by the dependency of pol delta mutants on Chk1 activation for survival. We conclude that DBAN targets a process or protein that acts at the start of S phase and is required for Chk1 phosphorylation. Taken together, DBAN may precipitate cancer by perturbing S phase and by blocking the Chk1-dependent response to replication fork damage.","doi":"10.1038/s41598-017-13033-8","authors":"Caspari T, Dyer J, Fenner N, Dunn C, Freeman C","authors_abbrev":"Caspari T et al.","pubmed_publication_date":"06 Oct 2017","pubmed_entrez_date":"2017-10-08","publication_year":"2017","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-10-09 00:15:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007400","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25353621","title":"Transcriptome-wide mapping of pseudouridines: pseudouridine synthases modify specific mRNAs in S. cerevisiae.","citation":"PLoS One 2014;9(10):e110799","abstract":"We developed a novel technique, called pseudouridine site identification sequencing (PSI-seq), for the transcriptome-wide mapping of pseudouridylation sites with single-base resolution from cellular RNAs based on the induced termination of reverse transcription specifically at pseudouridines following CMCT treatment. PSI-seq analysis of RNA samples from S. cerevisiae correctly detected all of the 43 known pseudouridines in yeast 18S and 25S ribosomal RNA with high specificity. Moreover, application of PSI-seq to the yeast transcriptome revealed the presence of site-specific pseudouridylation within dozens of mRNAs, including RPL11a, TEF1, and other genes implicated in translation. To identify the mechanisms responsible for mRNA pseudouridylation, we genetically deleted candidate pseudouridine synthase (Pus) enzymes and reconstituted their activities in vitro. These experiments demonstrated that the Pus1 enzyme was necessary and sufficient for pseudouridylation of RPL11a mRNA, whereas Pus4 modified TEF1 mRNA, and Pus6 pseudouridylated KAR2 mRNA. Finally, we determined that modification of RPL11a at Ψ -68 was observed in RNA from the related yeast S. mikitae, and Ψ -239 in TEF1 mRNA was maintained in S. mikitae as well as S. pombe, indicating that these pseudouridylations are ancient, evolutionarily conserved RNA modifications. This work establishes that site-specific pseudouridylation of eukaryotic mRNAs is a genetically programmed RNA modification that naturally occurs in multiple yeast transcripts via distinct mechanisms, suggesting that mRNA pseudouridylation may provide an important novel regulatory function. The approach and strategies that we report here should be generally applicable to the discovery of pseudouridylation, or other RNA modifications, in diverse biological contexts.","doi":"10.1371/journal.pone.0110799","authors":"Lovejoy AF, Riordan DP, Brown PO","authors_abbrev":"Lovejoy AF et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-10-30","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-10-31 01:15:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10087262","title":"Fission yeast alpha-glucan synthase Mok1 requires the actin cytoskeleton to localize the sites of growth and plays an essential role in cell morphogenesis downstream of protein kinase C function.","citation":"J Cell Biol 1999 Mar 22;144(6):1173-86","abstract":"In fission yeast protein kinase C homologues (Pck1 and Pck2) are essential for cell morphogenesis. We have isolated mok1(+) in a genetic screen to identify downstream effectors for Pck1/2. mok1(+) is essential for viability and encodes a protein that has several membrane-spanning domains and regions homologous to glucan metabolic enzymes. mok1 mutant shows abnormal cell shape, randomization of F-actin and weak cell wall. Biochemical analysis shows that Mok1 appears to have alpha-glucan synthase activity. Mok1 localization undergoes dramatic alteration during the cell cycle. It localizes to the growing tips in interphase, the medial ring upon mitosis, a double ring before and dense dot during cytokinesis. Double immunofluorescence staining shows that Mok1 exists in close proximity to actin. The subcellular localization of Mok1 is dependent upon the integrity of the F-actin cytoskeleton. Conversely, overexpression of mok1(+) blocks the translocation of cortical actin from one end of the cell to the other. pck2 mutant is synthetically lethal with mok1 mutant, delocalizes Mok1 and shows a lower level of alpha-glucan. These results indicate that Mok1 plays a crucial role in cell morphogenesis interdependently of the actin cytoskeleton and works as one of downstream effectors for Pck1/2.","authors":"Katayama S, Hirata D, Arellano M, Pérez P, Toda T","authors_abbrev":"Katayama S et al.","pubmed_publication_date":"22 Mar 1999","pubmed_entrez_date":"1999-03-24","publication_year":"1999","canto_session_key":"97822a9fb07b8414","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-04-03 10:37:49","canto_approved_date":"2025-09-02 21:16:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-18 16:17:55","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.14c","SPCC1281.01","SPBC32H8.13c","SPBC16D10.05","SPAC1F5.04c","SPCC63.04","SPAC4A8.15c","SPCC16C4.09","SPAC1527.01","SPAC27F1.02c","SPBC12D12.04c"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2020-04-03"},{"uniquename":"PMID:23182517","title":"Global control of cell growth in fission yeast and its coordination with the cell cycle.","citation":"Curr Opin Cell Biol 2012 Dec;24(6):833-7","abstract":"Cell growth is a fundamental process for every cell but its pleiotropic complexity makes it difficult to comprehend. Global aspects of cellular growth, like the overall determinants of growth rate are not well understood. Here we examine the cell growth pattern of the fission yeast Schizosaccharomyces pombe during the mitotic and meiotic cell cycles. We also explore recent findings illuminating aspects of cell size homeostasis and cell growth regulation, and propose that there are global controls over growth acting at the level of the cell.","doi":"10.1016/j.ceb.2012.10.015","authors":"Navarro FJ, Weston L, Nurse P","authors_abbrev":"Navarro FJ et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-11-28","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11559751","title":"Cytoplasmic microtubular system implicated in de novo formation of a Rabl-like orientation of chromosomes in fission yeast.","citation":"J Cell Sci 2001 Jul;114(Pt 13):2427-35","abstract":"Chromosomes are not packed randomly in the nucleus. The Rabl orientation is an example of the non-random arrangement of chromosomes, centromeres are grouped in a limited area near the nuclear periphery and telomeres are located apart from centromeres. This orientation is established during mitosis and maintained through subsequent interphase in a range of species. We report that a Rabl-like configuration can be formed de novo without a preceding mitosis during the transition from the sexual phase to the vegetative phase of the life cycle in fission yeast. In this process, each of the dispersed centromeres is often associated with a novel Sad1-containing body that is contacting a cytoplasmic microtubule laterally (Sad1 is a component of the spindle pole body (SPB)). The Sad1-containing body was colocalized with other known SPB components, Kms1 and Spo15 but not with Cut12, indicating that it represents a novel SPB-related complex. The existence of the triplex structure (centromere-microtubule-Sad1 body) suggests that the clustering of centromeres is controlled by a cytoplasmic microtubular system. Accordingly, when microtubules are destabilized, clustering is markedly reduced.","authors":"Goto B, Okazaki K, Niwa O","authors_abbrev":"Goto B et al.","pubmed_publication_date":"Jul 2001","pubmed_entrez_date":"2001-09-18","publication_year":"2001","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28765280","title":"The exocyst subunit Sec3 is regulated by a protein quality control pathway.","citation":"J Biol Chem 2017 Sep 15;292(37):15240-15253","abstract":"Exocytosis involves fusion of secretory vesicles with the plasma membrane, thereby delivering membrane proteins to the cell surface and releasing material into the extracellular space. The tethering of the secretory vesicles before membrane fusion is mediated by the exocyst, an essential phylogenetically conserved octameric protein complex. Exocyst biogenesis is regulated by several processes, but the mechanisms by which the exocyst is degraded are unknown. Here, to unravel the components of the exocyst degradation pathway, we screened for extragenic suppressors of a temperature-sensitive fission yeast strain mutated in the exocyst subunit Sec3 ( sec3-913 ). One of the suppressing DNAs encoded a truncated dominant-negative variant of the 26S proteasome subunit, Rpt2, indicating that exocyst degradation is controlled by the ubiquitin-proteasome system. The temperature-dependent growth defect of the  sec3-913  strain was gene dosage-dependent and suppressed by blocking the proteasome, Hsp70-type molecular chaperones, the Pib1 E3 ubiquitin-protein ligase, and the deubiquitylating enzyme Ubp3. Moreover, defects in cell septation, exocytosis, and endocytosis in  sec3  mutant strains were similarly alleviated by mutation of components in this pathway. We also found that, particularly under stress conditions, wild-type Sec3 degradation is regulated by Pib1 and the 26S proteasome. In conclusion, our results suggest that a cytosolic protein quality control pathway monitors folding and proteasome-dependent turnover of an exocyst subunit and, thereby, controls exocytosis in fission yeast.","doi":"10.1074/jbc.M117.789867","authors":"Kampmeyer C, Karakostova A, Schenstrøm SM, Abildgaard AB, Lauridsen AM, Jourdain I, Hartmann-Petersen R","authors_abbrev":"Kampmeyer C et al.","pubmed_publication_date":"15 Sep 2017","pubmed_entrez_date":"2017-08-03","publication_year":"2017","canto_session_key":"85bcd881821a0d07","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_first_approved_date":"2017-08-16 09:35:12","canto_approved_date":"2026-04-16 06:20:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-07 09:06:51","canto_added_date":"2017-08-04 00:15:13","annotation_curators":[{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.13","SPBC409.06","SPBP8B7.21","SPAC11G7.02","SPBC36B7.05c","SPAC17G8.12","SPBC4.07c","SPAC6C3.08","SPAC11G7.04","SPBC1709.05","SPAC13G7.02c","SPBC106.20"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2017-08-16"},{"uniquename":"PMID:18634753","title":"A novel series of vectors for chromosomal integration in fission yeast.","citation":"Biochem Biophys Res Commun 2008 Sep 19;374(2):315-9","abstract":"A series of fission yeast targeting vectors that can be used for wild-type strains having no selectable markers have been designed. The functions of one of three marker genes, lys1(+), arg1(+), and his3(+), involved in amino acid synthesis, are impaired by integration of the fragments generated by restriction enzyme digestion of the plasmids. Successful integration of the fragments into the targeted loci can be readily verified by their requirement for amino acids, or by the PCR diagnostic analysis. Since these selection markers are not used commonly in fission yeast, these plasmids are likely to facilitate studies that require the co-expression of genes such as co-localization and co-immunoprecipitation experiments, by employing them in combination with most of the previously reported markers.","doi":"10.1016/j.bbrc.2008.07.015","authors":"Matsuyama A, Shirai A, Yoshida M","authors_abbrev":"Matsuyama A et al.","pubmed_publication_date":"19 Sep 2008","pubmed_entrez_date":"2008-07-19","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24663817","title":"Rad4 mainly functions in Chk1-mediated DNA damage checkpoint pathway as a scaffold protein in the fission yeast Schizosaccharomyces pombe.","citation":"PLoS One 2014;9(3):e92936","abstract":"Rad4/Cut5 is a scaffold protein in the Chk1-mediated DNA damage checkpoint in S. pombe. However, whether it contains a robust ATR-activation domain (AAD) required for checkpoint signaling like its orthologs TopBP1 in humans and Dpb11 in budding yeast has been incompletely clear. To identify the putative AAD in Rad4, we carried out an extensive genetic screen looking for novel mutants with an enhanced sensitivity to replication stress or DNA damage in which the function of the AAD can be eliminated by the mutations. Two new mutations near the N-terminus were identified that caused significantly higher sensitivities to DNA damage or chronic replication stress than all previously reported mutants, suggesting that most of the checkpoint function of the protein is eliminated. However, these mutations did not affect the activation of Rad3 (ATR in humans) yet eliminated the scaffolding function of the protein required for the activation of Chk1. Several mutations were also identified in or near the recently reported AAD in the C-terminus of Rad4. However, all mutations in the C-terminus only slightly sensitized the cells to DNA damage. Interestingly, a mutant lacking the whole C-terminus was found resistant to DNA damage and replication stress almost like the wild type cells. Consistent with the resistance, all known Rad3 dependent phosphorylations of checkpoint proteins remained intact in the C-terminal deletion mutant, indicating that unlike that in Dpb11, the C-terminus of Rad4 does not contain a robust AAD. These results, together with those from the biochemical studies, show that Rad4 mainly functions as a scaffold protein in the Chk1, not the Cds1(CHK2 in humans), checkpoint pathway. It plays a minor role or is functionally redundant with an unknown factor in Rad3 activation.","doi":"10.1371/journal.pone.0092936","authors":"Yue M, Zeng L, Singh A, Xu Y","authors_abbrev":"Yue M et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-03-26","publication_year":"2014","canto_session_key":"d2d1a8fb3af2e67e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yongjie Xu","canto_first_approved_date":"2020-03-09 15:10:32","canto_approved_date":"2022-11-10 16:29:33","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2020-02-22 20:02:14","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yongjie Xu","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPCC18B5.11c","SPAC23C4.18c","SPBC342.05","SPBC216.05","SPAC9E9.08","SPAC664.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2020-03-09"},{"uniquename":"PMID:14765108","title":"Recovery from DNA damage checkpoint arrest by PP1-mediated inhibition of Chk1.","citation":"EMBO J 2004 Feb 25;23(4):908-18","abstract":"The G2 DNA damage checkpoint delays mitotic entry via the upregulation of Wee1 kinase and the downregulation of Cdc25 phosphatase by Chk1 kinase, and resultant inhibitory phosphorylation of Cdc2. While checkpoint activation is well understood, little is known about how the checkpoint is switched off to allow cell cycle re-entry. To identify proteins required for checkpoint release, we screened for genes in Schizosaccharomyces pombe that, when overexpressed, result in precocious mitotic entry in the presence of DNA damage. We show that overexpression of the type I protein phosphatase Dis2 sensitises S. pombe cells to DNA damage, causing aberrant mitoses. Dis2 abrogates Chk1 phosphorylation and activation in vivo, and dephosphorylates Chk1 and a phospho-S345 Chk1 peptide in vitro. dis2Delta cells have a prolonged chk1-dependent arrest and a compromised ability to downregulate Chk1 activity for checkpoint release. These effects are specific for the DNA damage checkpoint, because Dis2 has no effect on the chk1-independent response to stalled replication forks. We propose that inactivation of Chk1 by Dis2 allows mitotic entry following repair of DNA damage in the G2-phase.","authors":"den Elzen NR, O'Connell MJ","authors_abbrev":"den Elzen NR et al.","pubmed_publication_date":"25 Feb 2004","pubmed_entrez_date":"2004-02-07","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC776.02c","SPBC3E7.08c","SPCC1259.13","SPBC1734.06","SPAC644.14c"],"gene_count":5,"ltp_gene_count":4},{"uniquename":"PMID:12151111","title":"Characterization, expression and regulation of a third gene encoding glutathione S-transferase from the fission yeast.","citation":"Biochim Biophys Acta 2002 Aug 19;1577(1):164-70","abstract":"A third gene encoding glutathione S-transferase (GSTIII) was cloned from the fission yeast Schizosaccharomyces pombe. The nucleotide sequence determined was found to contain 2110 base pairs including an open reading frame of 242 amino acids that would encode a protein of a molecular mass of 26,620 Da. The cloned GSTIII gene could be expressed in S. pombe, S. cerevisiae and Escherichia coli cells which gave 1.4-, 2.1-, and 3.0-fold higher GST activity in an assay using 1-chloro-2,4-dinitrobenzene as a substrate, respectively. The cloned GSTIII gene caused higher survivals of S. pombe cells on solid media with cadmium chloride or mercuric chloride. The GSTIII protein has 16% and 18% homologies with the GSTI and GSTII proteins, respectively. To independently monitor the regulation of the GSTIII gene, its 1168 bp upstream region and N-terminal 33 amino acid-coding region was fused into the promoterless beta-galactosidase gene of the shuttle vector YEp357. The synthesis of beta-galactosidase from the fusion plasmid pGY357 was greatly enhanced by cadmium chloride (50 microM), cupric chloride (10 microM), aluminum chloride (5 mM, 10 mM), mercuric chloride (1 microM), and zinc chloride (10 mM). However, the synthesis of beta-galactosidase from the fusion plasmid pGY357 was not affected by superoxide-generating menadione, and o-dinitrobenzene, whereas they could significantly induce the expression of the GSTI and GSTII genes of S. pombe. The overproduced Pap1 inhibited the induction of beta-galactosidase synthesis from the fusion plasmid pGY357 by cadmium chloride, which is opposite to the previously known role of Pap1 in the response to oxidative stress. Our results collectively indicate that the three GST genes of S. pombe are subjected to different regulatory mechanisms. The major role of the GSTIII protein in S. pombe may be the detoxification of various metals.","authors":"Shin YH, Park EH, Fuchs JA, Lim CJ","authors_abbrev":"Shin YH et al.","pubmed_publication_date":"19 Aug 2002","pubmed_entrez_date":"2002-08-02","publication_year":"2002","canto_session_key":"dd810ecabf33dadf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:52:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 14:50:00","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-05"},{"uniquename":"PMID:24906327","title":"Telomere regulation during the cell cycle in fission yeast.","citation":"Methods Mol Biol 2014;1170:411-24","abstract":"The fission yeast Schizosaccharomyces pombe has emerged as a useful model organism to study telomere maintenance mechanisms. In this chapter, we provide detailed protocols for quantitative ChIP and BrdU incorporation analyses to investigate how fission yeast telomeres are regulated during the cell cycle by utilizing cdc25-22 synchronized cell cultures.","doi":"10.1007/978-1-4939-0888-2_22","authors":"Moser BA, Chang YT, Nakamura TM","authors_abbrev":"Moser BA et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-06-08","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17449473","title":"The nuclear export signal of splicing factor Uap56p interacts with nuclear pore-associated protein Rae1p for mRNA export in Schizosaccharomyces pombe.","citation":"J Biol Chem 2007 Jun 15;282(24):17507-16","abstract":"Mammalian UAP56 or its homolog Sub2p in Saccharomyces cerevisiae are members of the ATP-dependent RNA helicase family and are required for splicing and nuclear export of mRNA. Previously we showed that in Schizosaccharomyces pombe Uap56p is critical for mRNA export. It links the mRNA adapter Mlo3p, a homolog of Yra1p in S. cerevisiae or Aly in mammals, to nuclear pore-associated mRNA export factor Rae1p. In this study we show that, in contrast to S. cerevisiae, Uap56p in S. pombe is not required for pre-mRNA splicing. The putative RNA helicase function of Uap56p is not required for mRNA export. However, the RNA-binding motif of Uap56p is critical for nuclear export of mRNA. Within Uap56p we identified nuclear import and export signals that may allow it to shuttle between the nucleus and the cytoplasm. We found that Uap56p interacts with Rae1p directly via its nuclear export signal, and this interaction is critical for the nuclear export activity of Uap56p as well as for exporting mRNA. RNA binding and the ability to shuttle between the nucleus and cytoplasm are important features of mRNA export carriers such as HIV-Rev. Our results suggest that Uap56p could function similarly as an export carrier of mRNA in S. pombe.","authors":"Thakurta AG, Selvanathan SP, Patterson AD, Gopal G, Dhar R","authors_abbrev":"Thakurta AG et al.","pubmed_publication_date":"15 Jun 2007","pubmed_entrez_date":"2007-04-24","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD205","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23188080","title":"The fission yeast MRN complex tethers dysfunctional telomeres for NHEJ repair.","citation":"EMBO J 2012 Dec 12;31(24):4576-86","abstract":"Telomeres protect the natural ends of chromosomes from being repaired as deleterious DNA breaks. In fission yeast, absence of Taz1 (homologue of human TRF1 and TRF2) renders telomeres vulnerable to DNA repair. During the G1 phase, when non-homologous end joining (NHEJ) is upregulated, taz1Δ cells undergo telomere fusions with consequent loss of viability. Here, we show that disruption of the fission yeast MRN (Rad23(MRE11)-Rad50-Nbs1) complex prevents NHEJ at telomeres and, as a result, rescues taz1Δ lethality in G1. Neither Tel1(ATM) activation nor 5'-end resection was required for telomere fusion. Nuclease activity of Rad32(MRE11) was also dispensable for NHEJ. Mutants unable to coordinate metal ions required for nuclease activity were proficient in NHEJ repair. In contrast, Rad32(MRE11) mutations that affect binding and/or positioning of DNA ends leaving the nuclease function largely unaffected also impaired NHEJ at telomeres and restored the viability of taz1Δ in G1. Consistently, MRN structural integrity but not nuclease function is also required for NHEJ of independent DNA ends in a novel split-molecule plasmid assay. Thus, MRN acts to tether unlinked DNA ends, allowing for efficient NHEJ.","doi":"10.1038/emboj.2012.313","authors":"Reis CC, Batista S, Ferreira MG","authors_abbrev":"Reis CC et al.","pubmed_publication_date":"12 Dec 2012","pubmed_entrez_date":"2012-11-29","publication_year":"2012","canto_session_key":"95b85083b1b32feb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-10-15 14:40:04","canto_approved_date":"2020-10-15 14:40:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-10-12 13:43:41","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":50,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.09c","SPCC338.08","SPCC1020.06c","SPCC1183.05c","SPBC543.03c","SPBC1778.02","SPCC23B6.03c","SPAC16A10.07c","SPBC29A10.05","SPAC1556.01c","SPBC216.05","SPCC126.02c","SPBC342.05","SPBC29A3.14c","SPAC13C5.07","SPCC970.01","SPBC16D10.04c"],"gene_count":17,"ltp_gene_count":15,"approved_date":"2020-10-15"},{"uniquename":"EMBL:AU009204","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10421424","title":"Suppression of oncogenic transformation by hypothemycin associated with accelerated cyclin D1 degradation through ubiquitin-proteasome pathway.","citation":"Life Sci 1999;65(4):381-94","abstract":"Hypothemycin was originally isolated as an antifungal metabolite of Hypomyces trichothecoides. Here we report that treatment on v-K-ras-transformed NIH3T3 cells (DT cells) with hypothemycin caused drastic decrease in amount of cyclin D1 protein with concomitant prolongation of G1 phase in their cell cycle. Analysis using hypothemycin-resistant mutant of Schizosaccharomyces pombe (S. pombe) was carried out to show that S. pombe rhp6+ (homologue of Saccharomyces cerevisiae RAD6) and mammalian ubiquitin-conjugating enzyme 2 (ubc2) are the targets of hypothemycin or its downstream molecules in ubiquitin-conjugation process. Furthermore, in the presence of lactacystin, a specific inhibitor for proteasome, hypothemycin greatly enhanced the accumulation of multi-ubiquitinated form of cyclin D1 in DT cells. Therefore, it is indicated that hypothemycin facilitates ubiquitinating process of cyclin D1. In terms of malignant phenotype, hypothemycin inhibited anchorage-independent growth and reverted the morphology of DT cells. On the contrary, their morphology still remained transformed in the additional presence of lactacystin. Our results suggest that cyclin D1 is a key molecule working downstream in ras-signaling and that the transformation can be inhibited by the compound which can activate ubiquitin-proteasome pathway including degradation of cyclin D1.","authors":"Sonoda H, Omi K, Hojo K, Nishida K, Omura S, Sugita K","authors_abbrev":"Sonoda H et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-07-27","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084848","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.36"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24302734","title":"A glutathione-independent glyoxalase of the DJ-1 superfamily plays an important role in managing metabolically generated methylglyoxal in Candida albicans.","citation":"J Biol Chem 2014 Jan 17;289(3):1662-74","abstract":"Methylglyoxal is a cytotoxic reactive carbonyl compound produced by central metabolism. Dedicated glyoxalases convert methylglyoxal to d-lactate using multiple catalytic strategies. In this study, the DJ-1 superfamily member ORF 19.251/GLX3 from Candida albicans is shown to possess glyoxalase activity, making this the first demonstrated glutathione-independent glyoxalase in fungi. The crystal structure of Glx3p indicates that the protein is a monomer containing the catalytic triad Cys(136)-His(137)-Glu(168). Purified Glx3p has an in vitro methylglyoxalase activity (Km = 5.5 mM and kcat = 7.8 s(-1)) that is significantly greater than that of more distantly related members of the DJ-1 superfamily. A close Glx3p homolog from Saccharomyces cerevisiae (YDR533C/Hsp31) also has glyoxalase activity, suggesting that fungal members of the Hsp31 clade of the DJ-1 superfamily are all probable glutathione-independent glyoxalases. A homozygous glx3 null mutant in C. albicans strain SC5314 displays greater sensitivity to millimolar levels of exogenous methylglyoxal, elevated levels of intracellular methylglyoxal, and carbon source-dependent growth defects, especially when grown on glycerol. These phenotypic defects are complemented by restoration of the wild-type GLX3 locus. The growth defect of Glx3-deficient cells in glycerol is also partially complemented by added inorganic phosphate, which is not observed for wild-type or glucose-grown cells. Therefore, C. albicans Glx3 and its fungal homologs are physiologically relevant glutathione-independent glyoxalases that are not redundant with the previously characterized glutathione-dependent GLO1/GLO2 system. In addition to its role in detoxifying glyoxals, Glx3 and its close homologs may have other important roles in stress response.","doi":"10.1074/jbc.M113.505784","authors":"Hasim S, Hussin NA, Alomar F, Bidasee KR, Nickerson KW, Wilson MA","authors_abbrev":"Hasim S et al.","pubmed_publication_date":"17 Jan 2014","pubmed_entrez_date":"2013-12-05","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22E12.03c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:39892319","title":"The 1-acylglycerol-3-phosphate acyltransferase Slc1 is required to regulate mitochondria and lipid droplets.","citation":"Microbiol Res 2025 Jan 31;293:128080","abstract":"Mitochondria are organelles involved in energy metabolism and biosynthesis. As the metabolites released from mitochondria are raw materials used for lipid synthesis, mitochondria also play important roles in lipid metabolism. Here we report that Slc1, a 1-acylglycerol-3-phosphate O-acyltransferase in the fission yeast Schizosaccharomyces pombe, is required to maintain tubular mitochondrial morphology and normal mitochondrial functions. The absence of Slc1 causes mitochondrial fragmentation, increases mitochondrial fission frequency, reduces mitochondrial respiration, and slows down nitrogen starvation-induced mitophagy. In addition, the absence of Slc1 significantly increases the protein level of Ptl2, which is the triacylglycerol lipase localized on lipid droplets. The phenotypes caused by the absence of Slc1 depend on its acyltransferase enzymatic activity. Therefore, our study uncovers new roles of a lipid synthesis enzyme Slc1 in regulating mitochondria and lipid droplets.","doi":"10.1016/j.micres.2025.128080","authors":"Zhao C, Liu K, Wu Y, Yan S, He J, Fu C","authors_abbrev":"Zhao C et al.","pubmed_publication_date":"31 Jan 2025","pubmed_entrez_date":"2025-02-01","publication_year":"2025","canto_session_key":"0a7ef9d95870b098","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-02-03 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18488015","title":"Dynamic repertoire of a eukaryotic transcriptome surveyed at single-nucleotide resolution.","citation":"Nature 2008 Jun 26;453(7199):1239-43","abstract":"Recent data from several organisms indicate that the transcribed portions of genomes are larger and more complex than expected, and that many functional properties of transcripts are based not on coding sequences but on regulatory sequences in untranslated regions or non-coding RNAs. Alternative start and polyadenylation sites and regulation of intron splicing add additional dimensions to the rich transcriptional output. This transcriptional complexity has been sampled mainly using hybridization-based methods under one or few experimental conditions. Here we applied direct high-throughput sequencing of complementary DNAs (RNA-Seq), supplemented with data from high-density tiling arrays, to globally sample transcripts of the fission yeast Schizosaccharomyces pombe, independently from available gene annotations. We interrogated transcriptomes under multiple conditions, including rapid proliferation, meiotic differentiation and environmental stress, as well as in RNA processing mutants to reveal the dynamic plasticity of the transcriptional landscape as a function of environmental, developmental and genetic factors. High-throughput sequencing proved to be a powerful and quantitative method to sample transcriptomes deeply at maximal resolution. In contrast to hybridization, sequencing showed little, if any, background noise and was sensitive enough to detect widespread transcription in >90% of the genome, including traces of RNAs that were not robustly transcribed or rapidly degraded. The combined sequencing and strand-specific array data provide rich condition-specific information on novel, mostly non-coding transcripts, untranslated regions and gene structures, thus improving the existing genome annotation. Sequence reads spanning exon-exon or exon-intron junctions give unique insight into a surprising variability in splicing efficiency across introns, genes and conditions. Splicing efficiency was largely coordinated with transcript levels, and increased transcription led to increased splicing in test genes. Hundreds of introns showed such regulated splicing during cellular proliferation or differentiation.","doi":"10.1038/nature07002","authors":"Wilhelm BT, Marguerat S, Watt S, Schubert F, Wood V, Goodhead I, Penkett CJ, Rogers J, Bähler J","authors_abbrev":"Wilhelm BT et al.","pubmed_publication_date":"26 Jun 2008","pubmed_entrez_date":"2008-05-20","publication_year":"2008","canto_session_key":"a364c09276926eb9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-05 13:53:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 10:21:00","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC222.18","SPNCRNA.137","SPNCRNA.171","SPNCRNA.280","SPNCRNA.147","SPNCRNA.185","SPNCRNA.469","SPNCRNA.545","SPAC23C4.04c","SPNCRNA.604","SPNCRNA.985","SPNCRNA.322","SPNCRNA.301","SPNCRNA.365","SPNCRNA.451","SPNCRNA.189","SPNCRNA.217","SPNCRNA.361","SPNCRNA.199","SPNCRNA.291","SPNCRNA.493","SPNCRNA.148","SPNCRNA.484","SPNCRNA.573","SPNCRNA.298","SPNCRNA.571","SPNCRNA.307","SPNCRNA.247","SPCC1739.10","SPNCRNA.188","SPNCRNA.209","SPNCRNA.218","SPNCRNA.243","SPNCRNA.526","SPNCRNA.30","SPNCRNA.174","SPNCRNA.187","SPNCRNA.772","SPNCRNA.432","SPNCRNA.464","SPNCRNA.414","SPNCRNA.394","SPNCRNA.427","SPNCRNA.452","SPNCRNA.445","SPNCRNA.586","SPNCRNA.519","SPNCRNA.359","SPNCRNA.258","SPAC1751.02c","SPNCRNA.525","SPNCRNA.512","SPNCRNA.275","SPNCRNA.392","SPNCRNA.173","SPNCRNA.266","SPNCRNA.417","SPNCRNA.286","SPNCRNA.500","SPNCRNA.360","SPNCRNA.311","SPNCRNA.562","SPNCRNA.442","SPNCRNA.921","SPNCRNA.398","SPAC1556.01c","SPAP4C9.02","SPNCRNA.294","SPNCRNA.449","SPNCRNA.363","SPNCRNA.297","SPNCRNA.400","SPNCRNA.425","SPNCRNA.466","SPNCRNA.413","SPNCRNA.478","SPNCRNA.372","SPNCRNA.441","SPNCRNA.483","SPNCRNA.550","SPNCRNA.1132","SPNCRNA.158","SPNCRNA.1657","SPAC22F3.15","SPNCRNA.399","SPNCRNA.554","SPNCRNA.1228","SPNCRNA.583","SPNCRNA.625","SPNCRNA.136","SPNCRNA.212","SPNCRNA.505","SPNCRNA.580","SPAC23H3.04","SPNCRNA.1714","SPNCRNA.477","SPNCRNA.1303","SPNCRNA.177","SPNCRNA.276","SPCC757.15","SPNCRNA.660","SPNCRNA.268","SPNCRNA.240","SPNCRNA.200","SPAC212.12","SPNCRNA.1032","SPNCRNA.848","SPNCRNA.319","SPNCRNA.190","SPNCRNA.261","SPNCRNA.324","SPNCRNA.160","SPNCRNA.577","SPNCRNA.384","SPAC13G6.04","SPNCRNA.487","SPNCRNA.111","SPNCRNA.438","SPNCRNA.536","SPNCRNA.567","SPNCRNA.270","SPNCRNA.456","SPNCRNA.387","SPNCRNA.662","SPNCRNA.823","SPNCRNA.907","SPNCRNA.226","SPNCRNA.293","SPNCRNA.305","SPNCRNA.941","SPNCRNA.348","SPNCRNA.186","SPAC227.19c","SPNCRNA.585","SPNCRNA.332","SPAC15A10.12c","SPNCRNA.366","SPNCRNA.563","SPNCRNA.570","SPAC16E8.12c","SPNCRNA.333","SPNCRNA.358","SPNCRNA.529","SPAC6F6.19","SPNCRNA.318","SPNCRNA.368","SPNCRNA.316","SPNCRNA.549","SPNCRNA.556","SPNCRNA.1235","SPNCRNA.412","SPNCRNA.242","SPAC222.17","SPNCRNA.154","SPNCRNA.370","SPAC17C9.08","SPAC17A5.02c","SPNCRNA.1399","SPNCRNA.202","SPNCRNA.304","SPNCRNA.471","SPCC70.12c","SPNCRNA.323","SPNCRNA.435","SPNCRNA.284","SPNCRNA.402","SPNCRNA.485","SPNCRNA.1387","SPCC1442.19","SPNCRNA.1333","SPNCRNA.256","SPNCRNA.453","SPNCRNA.279","SPNCRNA.653","SPNCRNA.338","SPNCRNA.220","SPNCRNA.326","SPBC1604.25","SPNCRNA.396","SPNCRNA.237","SPNCRNA.511","SPNCRNA.540","SPNCRNA.281","SPNCRNA.390","SPNCRNA.182","SPNCRNA.516","SPBC29A10.17","SPNCRNA.296","SPNCRNA.421","SPNCRNA.335","SPAC1639.01c","SPNCRNA.1582","SPAC20G4.09","SPNCRNA.178","SPNCRNA.457","SPNCRNA.560","SPNCRNA.391","SPNCRNA.475","SPAPB1E7.14","SPCC16C4.22","SPNCRNA.566","SPAC144.17c","SPNCRNA.292","SPNCRNA.300","SPAC688.16","SPAC15A10.10","SPNCRNA.581","SPAC3F10.19","SPNCRNA.561","SPNCRNA.460","SPNCRNA.568","SPAC24H6.01c","SPNCRNA.163","SPNCRNA.181","SPNCRNA.228","SPNCRNA.480","SPNCRNA.380","SPNCRNA.450","SPNCRNA.1115","SPNCRNA.271","SPNCRNA.362","SPNCRNA.253","SPNCRNA.219","SPNCRNA.351","SPNCRNA.627","SPNCRNA.1379","SPNCRNA.393","SPNCRNA.269","SPAC1556.03","SPNCRNA.164","SPNCRNA.166","SPNCRNA.249","SPNCRNA.232","SPNCRNA.168","SPNCRNA.1205","SPNCRNA.124","SPNCRNA.222","SPNCRNA.371","SPNCRNA.513","SPNCRNA.169","SPNCRNA.328","SPNCRNA.1598","SPNCRNA.273","SPNCRNA.1208","SPNCRNA.257","SPNCRNA.1187","SPNCRNA.192","SPNCRNA.274","SPNCRNA.282","SPNCRNA.382","SPNCRNA.408","SPNCRNA.439","SPNCRNA.1561","SPNCRNA.501","SPNCRNA.194","SPNCRNA.831","SPNCRNA.184","SPNCRNA.473","SPNCRNA.1533","SPNCRNA.443","SPNCRNA.1037","SPCC569.09","SPNCRNA.230","SPNCRNA.1696","SPNCRNA.628","SPNCRNA.352","SPBC26H8.16","SPNCRNA.216","SPNCRNA.389","SPNCRNA.383","SPNCRNA.1619","SPNCRNA.467","SPNCRNA.491","SPNCRNA.569","SPAC23D3.16","SPNCRNA.558","SPNCRNA.405","SPNCRNA.455","SPNCRNA.576","SPNCRNA.1474","SPNCRNA.579","SPAC25H1.10c","SPNCRNA.406","SPNCRNA.313","SPNCRNA.454","SPNCRNA.575","SPNCRNA.175","SPNCRNA.142","SPNCRNA.472","SPNCRNA.431","SPNCRNA.555","SPNCRNA.198","SPNCRNA.572","SPNCRNA.156","SPNCRNA.367","SPNCRNA.481","SPNCRNA.517","SPNCRNA.865","SPNCRNA.306","SPAC12G12.17","SPNCRNA.312","SPAC1F12.08","SPNCRNA.376","SPNCRNA.239","SPAC227.11c","SPNCRNA.388","SPNCRNA.215","SPNCRNA.440","SPNCRNA.446","SPNCRNA.403","SPNCRNA.482","SPNCRNA.486","SPNCRNA.337","SPNCRNA.327","SPNCRNA.229","SPNCRNA.346","SPNCRNA.364","SPNCRNA.565","SPNCRNA.373","SPNCRNA.520","SPNCRNA.1608","SPNCRNA.369","SPNCRNA.255","SPNCRNA.283","SPAC23H4.21","SPNCRNA.141","SPAC57A7.15c","SPNCRNA.233","SPNCRNA.264","SPNCRNA.267","SPNCRNA.397","SPNCRNA.234","SPNCRNA.448","SPAC23D3.17","SPNCRNA.1624","SPNCRNA.463","SPNCRNA.204","SPNCRNA.231","SPNCRNA.488","SPNCRNA.506","SPNCRNA.1559","SPNCRNA.401","SPNCRNA.213","SPNCRNA.858","SPNCRNA.317","SPNCRNA.415","SPNCRNA.524","SPNCRNA.584","SPNCRNA.1693","SPNCRNA.423","SPNCRNA.374","SPCC736.14","SPNCRNA.437","SPNCRNA.534","SPNCRNA.159","SPNCRNA.260","SPAC167.09","SPNCRNA.195","SPAC27E2.14","SPNCRNA.244","SPNCRNA.278","SPNCRNA.287","SPNCRNA.315","SPNCRNA.201","SPNCRNA.377","SPNCRNA.385","SPAC22E12.10c","SPNCRNA.428","SPNCRNA.462","SPNCRNA.155"],"gene_count":370,"ltp_gene_count":0,"approved_date":"2014-08-05"},{"uniquename":"PMID:9722643","title":"The fission yeast chromo domain encoding gene chp1(+) is required for chromosome segregation and shows a genetic interaction with alpha-tubulin.","citation":"Nucleic Acids Res 1998 Sep 15;26(18):4222-9","abstract":"In eukaryotes, the segregation of chromosomes is co-ordinated by the centromere and must proceed accurately if aneuploidy and cell death are to be avoided. The fission yeast centromere is complex, containing highly repetitive regions of DNA showing the characteristics of heterochromatin. Two proteins, Swi6p and Clr4p, that are associated with the fission yeast centromere also contain a chromo (chromatin organisation modifier) domain and are required for centromere function. We have analysed a novel fission yeast gene encoding a putative chromo domain called chp 1(+) (chromo domain protein in Schizosaccharomyces p ombe ). In the absence of Chp1p protein, cells are viable but show chromosome segregation defects such as lagging chromosomes on the spindle during anaphase and high rates of minichromosome loss, phenotypes which are also displayed by swi 6 and clr 4. A fusion protein between green fluorescent protein (GFP) and Chp1p, like Swi6p, is localized to discrete sites within the nucleus. In contrast to Swi6p and Clr4p, Chp1p is not required to repress silent mating-type genes. We demonstrate a genetic interaction between chp 1(+) and alpha-tubulin ( nda 2(+)) and between swi 6(+) and beta-tubulin ( nda 3(+)). Chp1p and Swi6p proteins may be components of the kinetochore which captures and stabilizes the microtubules of the spindle.","authors":"Doe CL, Wang G, Chow C, Fricker MD, Singh PB, Mellor EJ","authors_abbrev":"Doe CL et al.","pubmed_publication_date":"15 Sep 1998","pubmed_entrez_date":"1998-09-02","publication_year":"1998","canto_session_key":"858ecbd8337e9ead","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-02 04:56:54","canto_approved_date":"2025-05-19 08:20:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-02 04:56:45","canto_added_date":"2012-02-24 05:53:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPAC18G6.02c","SPAC664.01c","SPBC26H8.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2021-01-02"},{"uniquename":"PANTHER:PTHR15486","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:891","SPCC4G3.13c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:40002888","title":"Perioperative Multi-Kingdom Gut Microbiota Alters in Coronary Artery Bypass Grafting.","citation":"Biomedicines 2025 Feb 14;13(2)","abstract":" Background : Coronary artery bypass grafting (CABG) is one of the main treatments for coronary heart disease (CHD). Gut microbiota, including bacteria, fungi, archaea, and virus, has been reported to be associated with CHD. However, the changes in the multi-kingdom gut microbiota after CABG are not yet clear. This study aimed to explore the changes in multi-kingdom gut microbiota during the early postoperative period of CABG.  Methods : We collected fecal samples from 40 patients before and 1 week after CABG surgery. Metagenomic sequencing was used to detect the microbial spectrum and gene functions in the patients' fecal samples.  Results : Post-CABG patients exhibited significant changes in the composition of multi-kingdom gut microbiota and gene functions. Among bacteria, beneficial species such as  Bifidobacterium ,  Bacteroides , and  Blautia  were significantly reduced after CABG, while the harmful species  Enterococcus  was significantly increased. In fungi,  Schizosaccharomyces pombe  was significantly decreased in the postoperative group, while  Saccharomyces cerevisiae  and  Aspergillus chevalieri  were significantly increased postoperatively. Spearman correlation analysis indicated that  Schizosaccharomyces pombe  had positive interactions with beneficial bacteria such as  Lachnospiraceae ,  Ruminococcus , and  Blautia . Among archaea, the preoperatively enriched  Methanomethylovorans-SGB40959  was significantly reduced postoperatively, and Spearman correlation analysis showed a significant positive interaction with probiotics  Ruminococcus  and  Dorea . In viruses, the phage  Enterococcus virus EFP01 , which infects  Enterococcus , was significantly increased postoperatively and showed a significant positive interaction with  Enterococcus . Additionally, postoperative dysregulation of gene functions such as the Phosphoenolpyruvate-dependent Sugar Phosphotransferase System (PTS), Transposition, DNA-mediated, and Transposase Activity was observed, and Spearman correlation analysis indicated significant correlations between the dysregulated gene functions and the microbial communities.  Conclusions : This study comprehensively revealed the changes in multi-kingdom species post-CABG. The reduction of beneficial microorganisms and the increase of harmful microorganisms after surgery are of significant clinical importance for understanding the overall health status of post-CABG patients and for optimizing postoperative treatment plans. Future research needs to further explore how to improve the prognosis of post-CABG patients by modulating the gut microbiota.","doi":"10.3390/biomedicines13020475","authors":"Fu Z, Jia Y, Zhao J, Guo Y, Xie B, An K, Yuan W, Chen Y, Zhong J, Tong Z, Liu X, Su P","authors_abbrev":"Fu Z et al.","pubmed_publication_date":"14 Feb 2025","pubmed_entrez_date":"2025-02-26","publication_year":"2025","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2025-02-27 00:25:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32507598","title":"Resurrection from lethal knockouts: Bypass of gene essentiality.","citation":"Biochem Biophys Res Commun 2020 Jul 30;528(3):405-412","abstract":"Understanding genotype-phenotype relationships is a central pursuit in biology. Gene knockout generates a complete loss-of-function genotype and is a commonly used approach for probing gene functions. The most severe phenotypic consequence of gene knockout is lethality. Genes with a lethal knockout phenotype are called essential genes. Based on genome-wide knockout analyses in yeasts, up to approximately a quarter of genes in a genome can be essential. Like other genotype-phenotype relationships, gene essentiality is subject to background effects and can vary due to gene-gene interactions. In particular, for some essential genes, lethality caused by knockout can be rescued by extragenic suppressors. Such \"bypass of essentiality\" (BOE) gene-gene interactions have been an understudied type of genetic suppression. A recent systematic analysis revealed that, remarkably, the essentiality of nearly 30% of essential genes in the fission yeast Schizosaccharomyces pombe can be bypassed by BOE interactions. Here, I review the history and recent progress on uncovering and understanding the bypass of gene essentiality.","doi":"10.1016/j.bbrc.2020.05.207","authors":"Du LL","authors_abbrev":"Du LL","pubmed_publication_date":"30 Jul 2020","pubmed_entrez_date":"2020-06-09","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-06-10 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25303522","title":"ESCRTs take on a job in surveillance.","citation":"Cell 2014 Oct 09;159(2):240-1","abstract":"Nuclear pore assembly can go awry, but how the cell handles defective intermediates has been an ongoing question. In this issue, Lusk and colleagues describe a surveillance pathway during nuclear pore assembly and, in doing so, identify a new role for proteins that function at the endosome and plasma membrane.","doi":"10.1016/j.cell.2014.09.046","authors":"Odorizzi G","authors_abbrev":"Odorizzi G","pubmed_publication_date":"09 Oct 2014","pubmed_entrez_date":"2014-10-11","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-03-08 01:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9498808","title":"A negative regulatory function for the protein tyrosine phosphatase PTP2C revealed by reconstruction of platelet-derived growth factor receptor signalling in Schizosaccharomyces pombe.","citation":"FEBS Lett 1998 Feb 06;422(3):321-7","abstract":"We have exploited reconstitution in the fission yeast Schizosaccharomyces pombe to investigate how activation of phospholipase Cgamma (PLCgamma) by the platelet-derived growth factor-beta receptor (PDGFbetaR) is regulated by the SH2 domain-containing protein tyrosine phosphatase PTP2C (also known as SHP-2). When co-expressed in S. pombe, PTP2C abolished PDGFbetaR autophosphorylation as well as its ability to phosphorylate and activate PLCgamma. Inhibition of PDGFbetaR signalling by PTP2C appears specific insofar that PTPIC, a close homologue of PTP2C, does not suppress activation of either PDGFbetaR or PLCgamma. Surprisingly, an inactive PTP2C mutant (C459S), which dephosphorylates neither PDGFbetaR nor PLCgamma, remains fully effective as an inhibitor of [3H]inositol phosphate generation indicating that negative regulation is at least in part independent of catalytic activity. This contrasts with PLCgamma activation by c-Src which, although blocked by active PTP2C, is not inhibited by the mutant PTP2C C459S. These observations indicate that in addition to a reported positive role relaying trophic signals, PTP2C can also exert a negative effect on the PDGFbetaR and its signalling to PLCgamma.","authors":"Arkinstall S, Gillieron C, Vial-Knecht E, Maundrell K","authors_abbrev":"Arkinstall S et al.","pubmed_publication_date":"06 Feb 1998","pubmed_entrez_date":"1998-03-14","publication_year":"1998","canto_session_key":"8b9cc8c5ce1edc2a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-03-01 10:24:10","canto_approved_date":"2019-03-01 10:24:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-03-01 10:24:03","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-03-01"},{"uniquename":"PMID:20404181","title":"Postreplication gaps at UV lesions are signals for checkpoint activation.","citation":"Proc Natl Acad Sci U S A 2010 May 04;107(18):8219-24","abstract":"Exposure of eukaryotic cells to UV light induces a checkpoint response that delays cell-cycle progression after cells enter S phase. It has been hypothesized that this checkpoint response provides time for repair by signaling the presence of structures generated when the replication fork encounters UV-induced DNA damage. To gain insight into the nature of the signaling structures, we used time-lapse microscopy to determine the effects of deficiencies in translesion DNA polymerases on the checkpoint response of the fission yeast Schizosaccharomyces pombe. We found that disruption of the genes encoding translesion DNA polymerases Polkappa and Poleta significantly prolonged the checkpoint response, indicating that the substrates of these enzymes are signals for checkpoint activation. Surprisingly, we found no evidence that the translesion polymerases Rev1 and Polzeta repair structures that are recognized by the checkpoint despite their role in maintaining viability after UV irradiation. Quantitative flow cytometry revealed that cells lacking translesion polymerases replicate UV-damaged DNA at the same rate at WT cells, indicating that the enhanced checkpoint response of cells lacking Polkappa and Poleta is not the result of stalled replication forks. These observations support a model in which postreplication DNA gaps with unrepaired UV lesions in the template strand act both as substrates for translesion polymerases and as signals for checkpoint activation.","doi":"10.1073/pnas.1003449107","authors":"Callegari AJ, Clark E, Pneuman A, Kelly TJ","authors_abbrev":"Callegari AJ et al.","pubmed_publication_date":"04 May 2010","pubmed_entrez_date":"2010-04-21","publication_year":"2010","canto_session_key":"961441fff5b656f5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"A. John Callegari","canto_first_approved_date":"2014-06-18 08:35:27","canto_approved_date":"2021-11-01 09:23:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-11 21:54:30","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"A. John Callegari","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.11","SPCC553.07c","SPBC1347.01c","SPAC688.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-06-18"},{"uniquename":"PMID:28502666","title":"Purification and characterisation of the fission yeast Ndc80 complex.","citation":"Protein Expr Purif 2017 Jul;135:61-69","abstract":"The Ndc80 complex is a conserved outer kinetochore protein complex consisting of Ndc80 (Hec1), Nuf2, Spc24 and Spc25. This complex comprises a major, if not the sole, platform with which the plus ends of the spindle microtubules directly interact. In fission yeast, several studies indicate that multiple microtubule-associated proteins including the Dis1/chTOG microtubule polymerase and the Mal3/EB1 microtubule plus-end tracking protein directly or indirectly bind Ndc80, thereby ensuring stable kinetochore-microtubule attachment. However, the purification of the Ndc80 complex from this yeast has not been achieved, which hampers the in-depth investigation as to how the outer kinetochore attaches to the plus end of the spindle microtubule. Here we report the two-step purification of the fission yeast Ndc80 holo complex from bacteria. First, we purified separately two sub-complexes consisting of Ndc80-Nuf2 and Spc24-Spc25. Then, these two sub-complexes were mixed and applied to size-exclusion chromatography. The reconstituted Ndc80 holo complex is composed of four subunits with equal stoichiometry. The complex possesses microtubule-binding activity, and Total Internal Reflection Fluorescence (TIRF)-microscopy assays show that the complex binds the microtubule lattice. Interestingly, unlike the human complex, the fission yeast complex does not track depolymerising microtubule ends. Further analysis shows that under physiological ionic conditions, the Ndc80 holo complex does not detectably bind Dis1, but instead it interacts with Mal3/EB1, by which the Ndc80 complex tracks the growing microtubule plus end. This result substantiates the notion that the Ndc80 complex plays a crucial role in establishment of the dynamic kinetochore-microtubule interface by cooperating with chTOG and EB1.","doi":"10.1016/j.pep.2017.05.002","authors":"Matsuo Y, Maurer SP, Surrey T, Toda T","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"Jul 2017","pubmed_entrez_date":"2017-05-16","publication_year":"2017","canto_session_key":"009b997767d7a3c7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-06-04 00:04:53","canto_approved_date":"2019-06-04 00:04:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-31 07:28:58","canto_added_date":"2017-05-17 00:15:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.03","SPCC188.04c","SPBC16A3.15c","SPAC27F1.04c","SPCC736.14","SPBC336.08"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-06-04"},{"uniquename":"EMBL:AU011802","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20661279","title":"Genomic binding profiling of the fission yeast stress-activated MAPK Sty1 and the bZIP transcriptional activator Atf1 in response to H2O2.","citation":"PLoS One 2010 Jul 16;5(7):e11620","abstract":"The evolutionally conserved MAPK Sty1 and bZIP transcriptional activator Atf1 are known to play a pivotal role in response to the reactive oxygen species in S. pombe. However, it is unclear whether all of the H(2)O(2)-induced genes are directly regulated by the Sty1-Atf1 pathway and involved in growth fitness under H(2)O(2)-induced stress conditions.\nHere we present the study on ChIP-chip mapping of the genomic binding sites for Sty1, Atf1, and the Atf1's binding partner Pcr1; the genome-wide transcriptional profiling of the atf1 and pcr1 strains in response to H(2)O(2); and the phenotypic assessment of approximately 90 Atf1/Pcr1-bound or unbound genes for growth fitness under H(2)O(2) conditions. ChIP-chip analysis shows that Atf1 and Pcr1 binding sites are overlapped in the genome and constitutively present before H(2)O(2) stress. On the other hand, Sty1 recruitment primarily occurs at the Atf1/Pcr1 binding sites and is induced by H(2)O(2). We found that Atf1/Pcr1 is clearly responsible for the high-level transcriptional response to H(2)O(2). Furthermore, phenotypic assessment indicates that among the H(2)O(2)-induced genes, Atf1/Pcr1-bound genes exhibit a higher likelihood of functional requirement for growth fitness under the stress condition than the Atf1/Pcr1-unbound genes do. Notably, we found that the Atf1/Pcr1-bound genes regardless of their responsiveness to H(2)O(2) show a high probability of requirement for growth fitness.\nTogether, our analyses on global mapping of protein binding sites, genome-wide transcriptional profiling, and phenotypic assessment provide insight into mechanisms for global transcriptional regulation by the Sty1-Atf1 pathway in response to H(2)O(2)-induced reactive oxygen species.","doi":"10.1371/journal.pone.0011620","authors":"Eshaghi M, Lee JH, Zhu L, Poon SY, Li J, Cho KH, Chu Z, Karuturi RK, Liu J","authors_abbrev":"Eshaghi M et al.","pubmed_publication_date":"16 Jul 2010","pubmed_entrez_date":"2010-07-28","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8513883","title":"Use of reference libraries and hybridisation fingerprinting for relational genome analysis.","citation":"FEBS Lett 1993 Jun 28;325(1-2):118-22","abstract":"The concept of relational genome analysis by hybridisation has been developed into a working system. Various genomic and cDNA libraries have been generated and are distributed via a reference system. Analysis procedures have been tested successfully in the mapping of the entire Schizosaccharomyces pombe genome. In another test-case for their refinement, analyses on the Drosophila genome are well under way. Human and mouse libraries are being studied on all levels, from generating YAC maps to partially sequencing representative cDNA libraries. The automation of the involved processes and the development of improved image detection and analysis are well advanced.","authors":"Hoheisel JD, Lehrach H","authors_abbrev":"Hoheisel JD et al.","pubmed_publication_date":"28 Jun 1993","pubmed_entrez_date":"1993-06-28","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF083335","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38897204","title":"On the importance of the diffusivity gradient term in Brownian dynamics simulations.","citation":"Biophys J 2024 Jun 18;","abstract":"In a recent study, Garner et al. investigated diffusion in the cytoplasm of fission yeasts, revealing vast heterogeneity in intracellular viscosity. Their conclusion was based on a combination of single-particle-tracking experiments and Brownian dynamics simulations. However, in their simulations, the diffusivity gradient term has been neglected-an assumption common in some biophysical applications but unjustified in this particular case due to spatial variations in diffusivity. Here, we aim to comment on the importance of the diffusivity gradient term and the physical consequences of not including it. We also demonstrate that omitting this term likely leads to overestimating fission yeast intracellular viscosity variance and underestimating its mean. Additionally, we propose modifications to the simulations to incorporate the gradient term.","doi":"10.1016/j.bpj.2024.05.034","authors":"Skóra T","authors_abbrev":"Skóra T","pubmed_publication_date":"18 Jun 2024","pubmed_entrez_date":"2024-06-19","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-06-20 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25959226","title":"Mechanistic insights into the anchorage of the contractile ring by anillin and Mid1.","citation":"Dev Cell 2015 May 26;33(4):413-26","abstract":"Anillins and Mid1 are scaffold proteins that play key roles in anchorage of the contractile ring at the cell equator during cytokinesis in animals and fungi, respectively. Here, we report crystal structures and functional analysis of human anillin and S. pombe Mid1. The combined data show anillin contains a cryptic C2 domain and a Rho-binding domain. Together with the tethering PH domain, three membrane-associating elements synergistically bind to RhoA and phospholipids to anchor anillin at the cleavage furrow. Surprisingly, Mid1 also binds to the membrane through a cryptic C2 domain. Dimerization of Mid1 leads to high affinity and preference for PI(4,5)P2, which stably anchors Mid1 at the division plane, bypassing the requirement for Rho GTPase. These findings uncover the unexpected general machinery and the divergent regulatory logics for the anchorage of the contractile ring through the anillin/Mid1 family proteins from yeast to humans.","doi":"10.1016/j.devcel.2015.03.003","authors":"Sun L, Guan R, Lee IJ, Liu Y, Chen M, Wang J, Wu JQ, Chen Z","authors_abbrev":"Sun L et al.","pubmed_publication_date":"26 May 2015","pubmed_entrez_date":"2015-05-12","publication_year":"2015","canto_session_key":"88f3e63970618c74","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Zhucheng Chen","canto_first_approved_date":"2023-03-09 08:32:41","canto_approved_date":"2025-01-28 15:41:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 19:06:00","canto_added_date":"2015-05-13 00:19:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Zhucheng Chen","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPAC31A2.16"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-03-09","pdb_entries":[{"pdb_id":"4xoh","gene_chains":[{"gene_uniquename":"SPCC4B3.15","chain":"A/B/C","position":"579-920"}],"title":"Mechanistic insights into anchorage of the contractile ring from yeast to humans","entry_authors":"Chen Z,Wu J-Q,Wang J,Guan R,Sun L,Lee I-J,Liu Y,Chen M","entry_authors_abbrev":"Chen Z et al.","reference_uniquename":"PMID:25959226","experimental_method":"X-ray","resolution":"2.801"}]},{"uniquename":"PMID:10022921","title":"A new member of the Sin3 family of corepressors is essential for cell viability and required for retroelement propagation in fission yeast.","citation":"Mol Cell Biol 1999 Mar;19(3):2351-65","abstract":"Tf1 is a long terminal repeat (LTR)-containing retrotransposon that propagates within the fission yeast Schizosaccharomyces pombe. LTR-retrotransposons possess significant similarity to retroviruses and therefore serve as retrovirus models. To determine what features of the host cell are important for the proliferation of this class of retroelements, we screened for mutations in host genes that reduced the transposition activity of Tf1. We report here the isolation and characterization of pst1(+), a gene required for Tf1 transposition. The predicted amino acid sequence of Pst1p possessed high sequence homology with the Sin3 family of proteins, known for their interaction with histone deacetylases. However, unlike the SIN3 gene of Saccharomyces cerevisiae, pst1(+) is essential for cell viability. Immunofluorescence microscopy indicated that Pst1p was localized in the nucleus. Consistent with the critical role previously reported for Sin3 proteins in the histone acetylation process, we found that the growth of the strain with the pst1-1 allele was supersensitive to the specific histone deacetylase inhibitor trichostatin A. However, our analysis of strains with the pst1-1 mutation was unable to detect any changes in the acetylation of specific lysines of histones H3 and H4 as measured in bulk chromatin. Interestingly, the pst1-1 mutant strain produced wild-type levels of Tf1-encoded proteins and cDNA, indicating that the defect in transposition occurred after reverse transcription. The results of immunofluorescence microscopy showed that the nuclear localization of the Tf1 capsid protein was disrupted in the strain with the pst1-1 mutation, indicating an important role of pst1(+) in modulating the nuclear import of Tf1 virus-like particles.","authors":"Dang VD, Benedik MJ, Ekwall K, Choi J, Allshire RC, Levin HL","authors_abbrev":"Dang VD et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-02-18","publication_year":"1999","canto_session_key":"9786a292cff06a8a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-09-10 16:15:56","canto_approved_date":"2024-06-26 08:50:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-10 16:15:44","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.10c","SPCC1322.13"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-09-10"},{"uniquename":"PMID:3856727","title":"The mitochondrial genome of the fission yeast Schizosaccharomyces pombe. 7. Continuous gene for apocytochrome b in strain EF1 (CBS 356) and sequence variation in the region of intron insertion in strain ade 7-50h.","citation":"Mol Gen Genet 1985;198(2):360-3","abstract":"The third BamHI fragment, containing most of gene for apocytochrome b, has been cloned and sequenced in the Schizosaccharomyces pombe strain EF1 (CBS 356). In contrast to strain ade 7-50h- (50) from the Leupold collection, in which the gene is interrupted by an intron of group II (Lang et al. 1984), the homologous gene in strain EF1 is continuous. This demonstrates that the intron in the gene for apocytochrome b is optional. Aligning the EF1 sequence with the homologous regions in strain 50, 2 base pair changes were found in the leader and 14 in the coding region. These changes led to 12 altered triplets, but 9 of them specify the same amino acid. Seven base changes were clustered within a stretch of 30 base pairs in the region in which the intron is inserted in strain 50. Five out of the resulting six triplet changes were also silent. These sequence variations around the highly conserved splice point region may be linked to the insertion or excision of the intron.","authors":"Trinkl H, Lang BF, Wolf K","authors_abbrev":"Trinkl H et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18776903","title":"TRAMP-mediated RNA surveillance prevents spurious entry of RNAs into the Schizosaccharomyces pombe siRNA pathway.","citation":"Nat Struct Mol Biol 2008 Oct;15(10):1015-23","abstract":"In the fission yeast Schizosaccharomyces pombe, the RNA interference (RNAi) machinery is required to generate small interfering RNAs (siRNAs) that mediate heterochromatic gene silencing. Efficient silencing also requires the TRAMP complex, which contains the noncanonical Cid14 poly(A) polymerase and targets aberrant RNAs for degradation. Here we use high-throughput sequencing to analyze Argonaute-associated small RNAs (sRNAs) in both the presence and absence of Cid14. Most sRNAs in fission yeast start with a 5' uracil, and we argue these are loaded most efficiently into Argonaute. In wild-type cells most sRNAs match to repeated regions of the genome, whereas in cid14Delta cells the sRNA profile changes to include major new classes of sRNAs originating from ribosomal RNAs and a tRNA. Thus, Cid14 prevents certain abundant RNAs from becoming substrates for the RNAi machinery, thereby freeing the RNAi machinery to act on its proper targets.","doi":"10.1038/nsmb.1481","authors":"Bühler M, Spies N, Bartel DP, Moazed D","authors_abbrev":"Bühler M et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-09-09","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26988418","title":"The proper connection between shelterin components is required for telomeric heterochromatin assembly.","citation":"Genes Dev 2016 Apr 01;30(7):827-39","abstract":"Telomeric regions contain prominent sites of heterochromatin, which is associated with unique histone modification profiles such as the methylation of histone H3 at Lys9 (H3K9me). In fission yeast, the conserved telomeric shelterin complex recruits the histone H3K9 methyltransferase complex CLRC to establish subtelomeric heterochromatin. Although many shelterin mutations affect subtelomeric heterochromatin assembly, the mechanism remains elusive due to the diverse functions of shelterin. Through affinity purification, we found that shelterin directly associates with CLRC through the Ccq1 subunit. Surprisingly, mutations that disrupt interactions between shelterin subunits compromise subtelomeric heterochromatin without affecting CLRC interaction with shelterin component Pot1, located at chromosome ends. We further discovered that telomeric repeats are refractory to heterochromatin spreading and that artificial restoration of shelterin connections or increased heterochromatin spreading rescued heterochromatin defects in these shelterin mutants. Thus, subtelomeric heterochromatin assembly requires both the recruitment of CLRC by shelterin to chromosome ends and the proper connection of shelterin components, which allows CLRC to skip telomeric repeats to internal regions.","doi":"10.1101/gad.266718.115","authors":"Wang J, Cohen AL, Letian A, Tadeo X, Moresco JJ, Liu J, Yates JR, Qiao F, Jia S","authors_abbrev":"Wang J et al.","pubmed_publication_date":"01 Apr 2016","pubmed_entrez_date":"2016-03-19","publication_year":"2016","canto_session_key":"0ff6580286bdf366","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16G5.13","SPAC3A11.08","SPCC188.07","SPCC970.07c","SPAC6F6.16c","SPBC800.03","SPBC17D11.04c","SPBC1778.02","SPAC664.01c","SPAC16A10.07c","SPBC428.08c","SPAC17G8.13c","SPCC622.16c","SPAC19G12.13c","SPAC26H5.06","SPCC11E10.08","SPCC613.12c"],"gene_count":17,"ltp_gene_count":17},{"uniquename":"PMID:21610214","title":"Structural and functional analysis of Nro1/Ett1: a protein involved in translation termination in S. cerevisiae and in O2-mediated gene control in S. pombe.","citation":"RNA 2011 Jul;17(7):1213-24","abstract":"In Saccharomyces cerevisiae, the putative 2-OG-Fe(II) dioxygenase Tpa1 and its partner Ett1 have been shown to impact mRNA decay and translation. Hence, inactivation of these factors was shown to influence stop codon read-though. In addition, Tpa1 represses, by an unknown mechanism, genes regulated by Hap1, a transcription factor involved in the response to levels of heme and O(2). The Schizosaccharomyces pombe orthologs of Tpa1 and Ett1, Ofd1, and its partner Nro1, respectively, have been shown to regulate the stability of the Sre1 transcription factor in response to oxygen levels. To gain insight into the function of Nro1/Ett1, we have solved the crystal structure of the S. pombe Nro1 protein deleted of its 54 N-terminal residues. Nro1 unexpectedly adopts a Tetratrico Peptide Repeat (TPR) fold, a motif often responsible for protein or peptide binding. Two ligands, a sulfate ion and an unknown molecule, interact with a cluster of highly conserved amino acids on the protein surface. Mutation of these residues demonstrates that these ligand binding sites are essential for Ett1 function in S. cerevisiae, as investigated by assaying for efficient translation termination.","doi":"10.1261/rna.2697111","authors":"Rispal D, Henri J, van Tilbeurgh H, Graille M, Séraphin B","authors_abbrev":"Rispal D et al.","pubmed_publication_date":"Jul 2011","pubmed_entrez_date":"2011-05-26","publication_year":"2011","canto_session_key":"ed309cb97e2a45db","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-16 15:34:49","canto_approved_date":"2023-02-17 07:59:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-16 15:34:29","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.07","SPBC6B1.08c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2023-02-16","pdb_entries":[{"pdb_id":"3qtm","gene_chains":[{"gene_uniquename":"SPCC4B3.07","chain":"A/B","position":"56-393"}],"title":"Structure of S. pombe nuclear import adaptor Nro1 (Space group P21)","entry_authors":"Rispal D,Henri J,van Tilbeurgh H,Graille M,Seraphin B","entry_authors_abbrev":"Rispal D et al.","reference_uniquename":"PMID:21610214","experimental_method":"X-ray","resolution":"2.15"},{"pdb_id":"3qtn","gene_chains":[{"gene_uniquename":"SPCC4B3.07","chain":"B","position":"56-393"}],"title":"Structure of S. pombe nuclear import adaptor Nro1 (Space group P6522)","entry_authors":"Rispal D,Henri J,van Tilbeurgh H,Graille M,Seraphin B","entry_authors_abbrev":"Rispal D et al.","reference_uniquename":"PMID:21610214","experimental_method":"X-ray","resolution":"3.499"}]},{"uniquename":"PMID:31855180","title":"Single-molecule turnover dynamics of actin and membrane coat proteins in clathrin-mediated endocytosis.","citation":"Elife 2019 Dec 19;8","abstract":"Actin dynamics generate forces to deform the membrane and overcome the cell's high turgor pressure during clathrin-mediated endocytosis (CME) in yeast, but precise molecular details are still unresolved. Our previous models predicted that actin filaments of the endocytic meshwork continually polymerize and disassemble, turning over multiple times during an endocytic event, similar to other actin systems. We applied single-molecule speckle tracking in live fission yeast to directly measure molecular turnover within CME sites for the first time. In contrast with the overall ~20 s lifetimes of actin and actin-associated proteins in endocytic patches, we detected single-molecule residence times around 1 to 2 s, and similarly high turnover rates of membrane-associated proteins in CME. Furthermore, we find heterogeneous behaviors in many proteins' motions. These results indicate that endocytic proteins turn over up to five times during the formation of an endocytic vesicle, and suggest revising quantitative models of force production.","doi":"10.7554/eLife.52355","authors":"Lacy MM, Baddeley D, Berro J","authors_abbrev":"Lacy MM et al.","pubmed_publication_date":"19 Dec 2019","pubmed_entrez_date":"2019-12-20","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22025288","title":"Cellular senescence and tumor suppressor gene p16.","citation":"Int J Cancer 2012 Apr 15;130(8):1715-25","abstract":"Cellular senescence is an irreversible arrest of cell growth. Biochemical and morphological changes occur during cellular senescence, including the formation of a unique cellular morphology such as flattened cytoplasm. Function of mitochondria, endoplasmic reticulum and lysosomes are affected resulting in the inhibition of lysosomal and proteosomal pathways. Cellular senescence can be triggered by a number of factors including, aging, DNA damage, oncogene activation and oxidative stress. While the molecular mechanism of senescence involves p16 and p53 tumor suppressor genes and telomere shortening, this review is focused on the mechanism of p16 control. The p16-mediated senescence acts through the retinoblastoma (Rb) pathway inhibiting the action of the cyclin dependant kinases leading to G1 cell cycle arrest. Rb is maintained in a hypophosphorylated state resulting in the inhibition of transcription factor E2F1. Regulation of p16 expression is complex and involves epigenetic control and multiple transcription factors. PRC1 (Pombe repressor complex (1) and PRC2 (Pombe repressor complex (2) proteins and histone deacetylases play an important role in the promoter hypermethylation for suppressing p16 expression. While transcription factors YY1 and Id1 suppress p16 expression, transcription factors CTCF, Sp1 and Ets family members activate p16 transcription. Senescence occurs with the inactivation of suppressor elements leading to the enhanced expression of p16.","doi":"10.1002/ijc.27316","authors":"Rayess H, Wang MB, Srivatsan ES","authors_abbrev":"Rayess H et al.","pubmed_publication_date":"15 Apr 2012","pubmed_entrez_date":"2011-10-26","publication_year":"2012","canto_session_key":"84214c0f59004d04","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-17 09:38:39","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-17 09:37:56","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-01-17"},{"uniquename":"PMID:24793650","title":"Structural basis for protein-RNA recognition in telomerase.","citation":"Nat Struct Mol Biol 2014 Jun;21(6):507-12","abstract":"Telomerase is a large ribonucleoprotein complex minimally composed of a catalytic telomerase reverse transcriptase (TERT) and an RNA component (TR) that provides the template for telomeric DNA synthesis. However, it remains unclear how TERT and TR assemble into a functional telomerase. Here we report the crystal structure of the conserved regions 4 and 5 (CR4/5) of TR in complex with the TR-binding domain (TRBD) of TERT from the teleost fish Oryzias latipes. The structure shows that CR4/5 adopts an L-shaped three-way-junction conformation with its two arms clamping onto TRBD. Both the sequence and conformation of CR4/5 are required for the interaction. Our structural and mutational analyses suggest that the observed CR4/5-TRBD recognition is common to most eukaryotes, and CR4/5 in vertebrate TR might have a similar role in telomerase regulation as that of stem-loop IV in Tetrahymena TR.","doi":"10.1038/nsmb.2819","authors":"Huang J, Brown AF, Wu J, Xue J, Bley CJ, Rand DP, Wu L, Zhang R, Chen JJ, Lei M","authors_abbrev":"Huang J et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-05-06","publication_year":"2014","canto_session_key":"27bb67e8e01cdc18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-06-16 10:32:38","canto_approved_date":"2020-06-16 10:32:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-06-16 10:32:31","canto_added_date":"2016-09-21 00:20:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.214","SPBC29A3.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-06-16"},{"uniquename":"PMID:27666591","title":"Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading.","citation":"Mol Cell 2016 Oct 06;64(1):79-91","abstract":"CENP-A is a centromere-specific histone 3 variant essential for centromere specification. CENP-A partially replaces canonical histone H3 at the centromeres. How the particular CENP-A/H3 ratio at centromeres is precisely maintained is unknown. It also remains unclear how CENP-A is excluded from non-centromeric chromatin. Here, we identify Ccp1, an uncharacterized NAP family protein in fission yeast that antagonizes CENP-A loading at both centromeric and non-centromeric regions. Like the CENP-A loading factor HJURP, Ccp1 interacts with CENP-A and is recruited to centromeres at the end of mitosis in a Mis16-dependent manner. These data indicate that factors with opposing CENP-A loading activities are recruited to centromeres. Furthermore, Ccp1 also cooperates with H2A.Z to evict CENP-A assembled in euchromatin. Structural analyses indicate that Ccp1 forms a homodimer that is required for its anti-CENP-A loading activity. Our study establishes mechanisms for maintenance of CENP-A homeostasis at centromeres and the prevention of ectopic assembly of centromeres.","doi":"10.1016/j.molcel.2016.08.022","authors":"Dong Q, Yin FX, Gao F, Shen Y, Zhang F, Li Y, He H, Gonzalez M, Yang J, Zhang S, Su M, Chen YH, Li F","authors_abbrev":"Dong Q et al.","pubmed_publication_date":"06 Oct 2016","pubmed_entrez_date":"2016-09-27","publication_year":"2016","canto_session_key":"c2a8d0f860ace791","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Fei Li","canto_first_approved_date":"2017-05-07 08:14:05","canto_approved_date":"2024-04-03 16:32:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-28 23:14:47","canto_added_date":"2016-09-28 00:15:11","annotation_curators":[{"name":"Fei Li","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC290.04","SPBC1105.17","SPBC609.05","SPBC36B7.08c","SPBP8B7.19","SPBC800.13","SPCC1672.10","SPBC11B10.10c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2017-05-07","pdb_entries":[{"pdb_id":"5gpk","gene_chains":[{"gene_uniquename":"SPBC36B7.08c","chain":"A/B","position":"1-244"}],"title":"Crystal structure of Ccp1 mutant","entry_authors":"Yin F,Gao F,Chen Y","entry_authors_abbrev":"Yin F et al.","reference_uniquename":"PMID:27666591","experimental_method":"X-ray","resolution":"2.103"},{"pdb_id":"5gpl","gene_chains":[{"gene_uniquename":"SPBC36B7.08c","chain":"A/B","position":"1-244"}],"title":"Crystal structure of Ccp1","entry_authors":"Yin F,Gao F,Chen Y","entry_authors_abbrev":"Yin F et al.","reference_uniquename":"PMID:27666591","experimental_method":"X-ray","resolution":"2.1"}]},{"uniquename":"PMID:27030795","title":"C1D family proteins in coordinating RNA processing, chromosome condensation and DNA damage response.","citation":"Cell Div 2016;11:2","abstract":"Research on the involvement of C1D and its yeast homologues Rrp47 (S. cerevisiae) and Cti1 (S. pombe) in DNA damage repair and RNA processing has remained mutually exclusive, with most studies predominantly concentrating on Rrp47. This review will look to reconcile the functions of these proteins in their involvement with the RNA exosome, in the regulation of chromatin architecture, and in the repair of DNA double-strand breaks, focusing on non-homologous end joining and homologous recombination. We propose that C1D is situated in a central position to maintain genomic stability at highly transcribed gene loci by coordinating these processes through the timely recruitment of relevant regulatory factors. In the event that the damage is beyond repair, C1D induces apoptosis in a p53-dependent manner.","doi":"10.1186/s13008-016-0014-5","authors":"Jackson RA, Wu JS, Chen ES","authors_abbrev":"Jackson RA et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-04-01","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-04-02 00:15:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26046468","title":"Fission yeast mitochondria are distributed by dynamic microtubules in a motor-independent manner.","citation":"Sci Rep 2015 Jun 05;5:11023","abstract":"The cytoskeleton plays a critical role in regulating mitochondria distribution. Similar to axonal mitochondria, the fission yeast mitochondria are distributed by the microtubule cytoskeleton, but this is regulated by a motor-independent mechanism depending on the microtubule associated protein mmb1p as the absence of mmb1p causes mitochondria aggregation. In this study, using a series of chimeric proteins to control the subcellular localization and motility of mitochondria, we show that a chimeric molecule containing a microtubule binding domain and the mitochondria outer membrane protein tom22p can restore the normal interconnected mitochondria network in mmb1-deletion (mmb1∆) cells. In contrast, increasing the motility of mitochondria by using a chimeric molecule containing a kinesin motor domain and tom22p cannot rescue mitochondria aggregation defects in mmb1∆ cells. Intriguingly a chimeric molecule carrying an actin binding domain and tom22p results in mitochondria associated with actin filaments at the actomyosin ring during mitosis, leading to cytokinesis defects. These findings suggest that the passive motor-independent microtubule-based mechanism is the major contributor to mitochondria distribution in wild type fission yeast cells. Hence, we establish that attachment to microtubules, but not kinesin-dependent movement and the actin cytoskeleton, is required and crucial for proper mitochondria distribution in fission yeast.","doi":"10.1038/srep11023","authors":"Li T, Zheng F, Cheung M, Wang F, Fu C","authors_abbrev":"Li T et al.","pubmed_publication_date":"05 Jun 2015","pubmed_entrez_date":"2015-06-06","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-06-07 00:20:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.16","SPBC25B2.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:22281223","title":"Kinase activity of fission yeast Mph1 is required for Mad2 and Mad3 to stably bind the anaphase promoting complex.","citation":"Curr Biol 2012 Feb 21;22(4):296-301","abstract":"Defects in chromosome segregation result in aneuploidy, which can lead to disease or cell death [1, 2]. The spindle checkpoint delays anaphase onset until all chromosomes are attached to spindle microtubules in a bipolar fashion [3, 4]. Mad2 is a key checkpoint component that undergoes conformational activation, catalyzed by a Mad1-Mad2 template enriched at unattached kinetochores [5]. Mad2 and Mad3 (BubR1) then bind and inhibit Cdc20 to form the mitotic checkpoint complex (MCC), which binds and inhibits the anaphase promoting complex (APC/C). Checkpoint kinases (Aurora, Bub1, and Mps1) are critical for checkpoint signaling, yet they have poorly defined roles and few substrates have been identified [6-8]. Here we demonstrate that a kinase-dead allele of the fission yeast MPS1 homolog (Mph1) is checkpoint defective and that levels of APC/C-associated Mad2 and Mad3 are dramatically reduced in this mutant. Thus, MCC binding to fission yeast APC/C is dependent on Mph1 kinase activity. We map and mutate several phosphorylation sites in Mad2, producing mutants that display reduced Cdc20-APC/C binding and an inability to maintain checkpoint arrest. We conclude that Mph1 kinase regulates the association of Mad2 with its binding partners and thereby mitotic arrest.","doi":"10.1016/j.cub.2011.12.049","authors":"Zich J, Sochaj AM, Syred HM, Milne L, Cook AG, Ohkura H, Rappsilber J, Hardwick KG","authors_abbrev":"Zich J et al.","pubmed_publication_date":"21 Feb 2012","pubmed_entrez_date":"2012-01-28","publication_year":"2012","canto_session_key":"4d4822dbe566aaac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-14 08:57:53","canto_approved_date":"2022-10-08 12:26:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-13 08:05:55","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":48,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.01c","SPCC1795.01c","SPBC106.01","SPCC1322.12c","SPBC26H8.07c","SPBC3D6.04c","SPCC320.13c","SPBC20F10.06"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2017-09-14"},{"uniquename":"PMID:10379403","title":"Genetics, physiology and cytology of yeast-mycelial dimorphism in fission yeasts.","citation":"Acta Microbiol Immunol Hung 1999;46(2-3):297-302","abstract":"The order Schizosaccharomycetales contains a dimorphic and two yeast species. Sch. japonicus can form both yeast cells and mycelium, depending on the substrate and the culturing conditions. Sch. pombe is a strictly unicellular organism, but it can be forced to form mycelial cell chains by inactivating members of the sep gene family. The mutations in most of the sep genes confer pleitropic phenotypes indicating functional involvement in MAP-kinase-mediated signalling pathways. Two of them were found to encode transcription factor homologues of other eukaryotes.","authors":"Sipiczki M, Grallert A, Miklós I, Zilahi E, Bozsik A, Szilágyi Z","authors_abbrev":"Sipiczki M et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-06-24","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39318285","title":"An improved tetracycline-inducible expression system for fission yeast.","citation":"J Cell Sci 2024 Sep 25;","abstract":"The ability to manipulate gene expression is valuable for elucidating gene function. In the fission yeast Schizosaccharomyces pombe, the most widely used regulatable expression system is the nmt1 promoter and its two attenuated variants. However, these promoters have limitations, including a long lag, incompatibility with rich media, and unsuitability for non-dividing cells. Here, we present a tetracycline-inducible system free of these shortcomings. Our system features the enotetS promoter, which achieves a similar induced level and a higher induction ratio compared to the nmt1 promoter, without exhibiting a lag. Additionally, our system includes four weakened enotetS variants, offering an expression range similar to the nmt1 series promoters but with more intermediate levels. To enhance usability, each promoter is combined with a Tet-repressor-expressing cassette in an integration plasmid. Importantly, our system can be used in non-dividing cells, enabling the development of a synchronous meiosis induction method with high spore viability. Moreover, our system allows for the shutdown of gene expression and the generation of conditional loss-of-function mutants. This system provides a versatile and powerful tool for manipulating gene expression in fission yeast.","doi":"10.1242/jcs.263404","authors":"Lyu XH, Yang YS, Pan ZQ, Ning SK, Suo F, Du LL","authors_abbrev":"Lyu XH et al.","pubmed_publication_date":"25 Sep 2024","pubmed_entrez_date":"2024-09-25","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-09-25 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16861909","title":"Fission yeast MAP kinase is required for the increased securin-separase interaction that rescues separase mutants under stresses.","citation":"Cell Cycle 2006 Aug;5(16):1831-9","abstract":"Sister chromatid separation requires two steps of proteolysis. Securin, the chaperon and inhibitor of separase, is destructed in anaphase after polyubiquitination, and resulting activated separase cleaves the cohesin subunit Scc1/Rad21. Fission yeast securin/Cut2 and separase/Cut1 that form the complex are essential for viability and a number of temperature-sensitive (ts) mutants have been isolated. We here report that the stresses such as 1.2 M sorbitol, 0.6 M KCl and 0.1 M CaCl(2) in the medium suppress the ts phenotypes of all the cut1 mutants and two of the three cut2 mutants examined. This unexpected finding led us to study how the ts phenotypes of cut1 and cut2 mutants were rescued by the increased stresses. The stresses caused a temporal arrest in the cell number increase, and this arrest was dependent on Spc1/Sty1 but not Rad3 and Mad2. During the 2-3 hr arrested period that occurred prior to the restart of division cycle, the level of securin dramatically increased, apparently accompanying the increased complex formation with mutant separase protein. Securin bound to separase was hyperphosphorylated. The stresses could not rescue the indestructible Cut2 and Rad21 mutants. We postulate that the stresses produce the hyperchaperonic form of Cut2 that can rescue separase mutations.","authors":"Kawasaki Y, Nagao K, Nakamura T, Yanagida M","authors_abbrev":"Kawasaki Y et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-07-25","publication_year":"2006","canto_session_key":"1a99b288004256e2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPBC106.10","SPAC24B11.06c","SPBC409.07c","SPBC14C8.01c","SPCC5E4.04"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:35609605","title":"Coordinated cortical ER remodeling facilitates actomyosin ring assembly.","citation":"Curr Biol 2022 Jun 20;32(12):2694-2703.e4","abstract":"The cortical endoplasmic reticulum (cER) is a reticulated network closely attached to the plasma membrane (PM). In the fission yeast Schizosaccharomyces pombe (S. pombe), ER-PM contacts have been suggested to restrict both the allocation and compaction of large-sized actomyosin assemblies along the lateral cell cortex. However, how cells orchestrate ER-PM contact remodeling in accordance with actomyosin coalescence for contractile ring assembly is unclear. Here, we reveal that actomyosin compaction directs the remodeling of the free tubular cER edges, whereas active exocytosis subsequently promotes the reorganization of the eisosome-bound cER rims by weakening their association or repatterning the eisosome-coated PM furrows. cER-eisosome contacts also act to reserve tubular cER edges and, hence, the ER shaping machinery at the lateral cell cortex. By manipulating or rerouting exocytosis in mutants with compromised actomyosin compaction, due to either the loss of myosin II activity or sheet-like cER morphology, we show that exocytosis facilitates ring formation likely by creating free tubular cER rims allowing robust cER remodeling. We thus propose that coordinated cER remodeling driven by both actomyosin forces and active exocytosis ensures proper contractile ring assembly. Our work also provides mechanistic insights into cER-related modulation in actomyosin ring assembly.","doi":"10.1016/j.cub.2022.04.086","authors":"Zhang D, See T","authors_abbrev":"Zhang D et al.","pubmed_publication_date":"20 Jun 2022","pubmed_entrez_date":"2022-05-24","publication_year":"2022","canto_session_key":"fa2bda2a002ecb74","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dan Zhang","canto_first_approved_date":"2022-06-30 14:00:34","canto_approved_date":"2025-07-02 07:52:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-06-11 16:30:00","canto_added_date":"2022-05-26 00:15:03","annotation_curators":[{"name":"Dan Zhang","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC830.08c","SPCC736.15","SPAC17C9.12","SPAC1A6.07","SPCC645.05c","SPBC31A8.01c","SPBC1685.13","SPBC1539.04","SPBC16G5.05c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2022-06-30"},{"uniquename":"PMID:24943839","title":"A role for nuclear envelope-bridging complexes in homology-directed repair.","citation":"Mol Biol Cell 2014 Aug 15;25(16):2461-71","abstract":"Unless efficiently and faithfully repaired, DNA double-strand breaks (DSBs) cause genome instability. We implicate a Schizosaccharomyces pombe nuclear envelope-spanning linker of nucleoskeleton and cytoskeleton (LINC) complex, composed of the Sad1/Unc84 protein Sad1 and Klarsicht/Anc1/SYNE1 homology protein Kms1, in the repair of DSBs. An induced DSB associates with Sad1 and Kms1 in S/G2 phases of the cell cycle, connecting the DSB to cytoplasmic microtubules. DSB resection to generate single-stranded DNA and the ATR kinase drive the formation of Sad1 foci in response to DNA damage. Depolymerization of microtubules or loss of Kms1 leads to an increase in the number and size of DSB-induced Sad1 foci. Further, Kms1 and the cytoplasmic microtubule regulator Mto1 promote the repair of an induced DSB by gene conversion, a type of homology-directed repair. kms1 genetically interacts with a number of genes involved in homology-directed repair; these same gene products appear to attenuate the formation or promote resolution of DSB-induced Sad1 foci. We suggest that the connection of DSBs with the cytoskeleton through the LINC complex may serve as an input to repair mechanism choice and efficiency.","doi":"10.1091/mbc.E13-10-0569","authors":"Swartz RK, Rodriguez EC, King MC","authors_abbrev":"Swartz RK et al.","pubmed_publication_date":"15 Aug 2014","pubmed_entrez_date":"2014-06-20","publication_year":"2014","canto_session_key":"bac60a761036eb2c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Megan King","canto_first_approved_date":"2015-04-23 15:15:28","canto_approved_date":"2020-12-28 15:13:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-08 14:29:07","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Megan King","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPBC12D12.01","SPBC29A10.05","SPBC365.15","SPAC20G4.04c","SPAC3A11.05c","SPAC3C7.03c","SPCC126.02c","SPCC417.07c","SPAC664.07c","SPBC216.05","SPAC30D11.10"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2015-04-23"},{"uniquename":"PMID:14745133","title":"Vesicle-mediated protein transport pathways to the vacuole in Schizosaccharomyces pombe.","citation":"Cell Struct Funct 2003 Oct;28(5):399-417","abstract":"The vacuole of Saccharomyces cerevisiae plays essential roles not only for osmoregulation and ion homeostasis but also down-regulation (degradation) of cell surface proteins and protein and organellar turnover. Genetic selections and genome-wide screens in S. cerevisiae have resulted in the identification of a large number of genes required for delivery of proteins to the vacuole. Although the complete genome sequence of the fission yeast Schizosaccharomyces pombe has been reported, there have been few reports on the proteins required for vacuolar protein transport and vacuolar biogenesis in S. pombe. Recent progress in the S. pombe genome project of has revealed that most of the genes required for vacuolar biogenesis and protein transport are conserved between S. pombe and S. cerevisiae. This suggests that the basic machinery of vesicle-mediated protein delivery to the vacuole is conserved between the two yeasts. Identification and characterization of the fission yeast counterparts of the budding yeast Vps and Vps-related proteins have facilitated our understanding of protein transport pathways to the vacuole in S. pombe. This review focuses on the recent advances in vesicle-mediated protein transport to the vacuole in S. pombe.","authors":"Takegawa K, Iwaki T, Fujita Y, Morita T, Hosomi A, Tanaka N","authors_abbrev":"Takegawa K et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2004-01-28","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC651.11c","YBR288C","SPAC11H11.01"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:27343236","title":"Restriction of Retrotransposon Mobilization in Schizosaccharomyces pombe by Transcriptional Silencing and Higher-Order Chromatin Organization.","citation":"Genetics 2016 Aug;203(4):1669-78","abstract":"Uncontrolled propagation of retrotransposons is potentially detrimental to host genome integrity. Therefore, cells have evolved surveillance mechanisms to restrict the mobility of these elements. In Schizosaccharomyces pombe the Tf2 LTR retrotransposons are transcriptionally silenced and are also clustered in the nucleus into structures termed Tf bodies. Here we describe the impact of silencing and clustering on the mobility of an endogenous Tf2 element. Deletion of genes such as set1(+) (histone H3 lysine 4 methyltransferase) or abp1(+) (CENP-B homolog) that both alleviate silencing and clustering, result in a corresponding increase in mobilization. Furthermore, expression of constitutively active Sre1, a transcriptional activator of Tf2 elements, also alleviates clustering and induces mobilization. In contrast, clustering is not disrupted by loss of the HIRA histone chaperone, despite high levels of expression, and in this background, mobilization frequency is only marginally increased. Thus, mutations that compromise transcriptional silencing but not Tf bodies are insufficient to drive mobilization. Furthermore, analyses of mutant alleles that separate the transcriptional repression and clustering functions of Set1 are consistent with control of Tf2 propagation via a combination of silencing and spatial organization. Our results indicate that host surveillance mechanisms operate at multiple levels to restrict Tf2 retrotransposon mobilization.","doi":"10.1534/genetics.116.189118","authors":"Murton HE, Grady PJ, Chan TH, Cam HP, Whitehall SK","authors_abbrev":"Murton HE et al.","pubmed_publication_date":"Aug 2016","pubmed_entrez_date":"2016-06-26","publication_year":"2016","canto_session_key":"8cba8e32b55041be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Simon Whitehall","canto_first_approved_date":"2016-12-19 22:03:05","canto_approved_date":"2022-11-17 16:23:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-12 15:09:14","canto_added_date":"2016-06-29 00:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Simon Whitehall","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPCC188.13c","SPBC15D4.03","SPBC36.05c","SPBC1105.04c","SPBC19C2.09","SPCC306.04c","SPBC31F10.13c","SPBC31F10.14c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-12-19"},{"uniquename":"PMID:26493332","title":"Stress-induced inhibition of translation independently of eIF2α phosphorylation.","citation":"J Cell Sci 2015 Dec 01;128(23):4420-7","abstract":"Exposure of fission yeast cells to ultraviolet (UV) light leads to inhibition of translation and phosphorylation of the eukaryotic initiation factor-2α (eIF2α). This phosphorylation is a common response to stress in all eukaryotes. It leads to inhibition of translation at the initiation stage and is thought to be the main reason why stressed cells dramatically reduce protein synthesis. Phosphorylation of eIF2α has been taken as a readout for downregulation of translation, but the role of eIF2α phosphorylation in the downregulation of general translation has not been much investigated. We show here that UV-induced global inhibition of translation in fission yeast cells is independent of eIF2α phosphorylation and the eIF2α kinase general control nonderepressible-2 protein (Gcn2). Also, in budding yeast and mammalian cells, the UV-induced translational depression is largely independent of GCN2 and eIF2α phosphorylation. Furthermore, exposure of fission yeast cells to oxidative stress generated by hydrogen peroxide induced an inhibition of translation that is also independent of Gcn2 and of eIF2α phosphorylation. Our findings show that stress-induced translational inhibition occurs through an unknown mechanism that is likely to be conserved through evolution.","doi":"10.1242/jcs.176545","authors":"Knutsen JH, Rødland GE, Bøe CA, Håland TW, Sunnerhagen P, Grallert B, Boye E","authors_abbrev":"Knutsen JH et al.","pubmed_publication_date":"01 Dec 2015","pubmed_entrez_date":"2015-10-24","publication_year":"2015","canto_session_key":"e171be475000981e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-03 14:09:15","canto_approved_date":"2021-10-30 17:09:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-15 12:08:22","canto_added_date":"2015-10-25 00:19:22","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.09c","SPBC4B4.04","SPBC36B7.09"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2016-02-03"},{"uniquename":"PMID:9388668","title":"Analysis of Prk1, a putative receptor kinase from fission yeast.","citation":"Biochem Soc Trans 1997 Aug;25(3):444S","abstract":"","authors":"Watson P, Davey J","authors_abbrev":"Watson P et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"176dcc6242e7abfe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:49:06","canto_session_submitted_date":"2012-02-27 11:04:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:9714831","title":"Molecular cloning of gaf1, a Schizosaccharomyces pombe GATA factor, which can function as a transcriptional activator.","citation":"Gene 1998 Jul 30;215(2):319-28","abstract":"As a first step to elucidate the functions of Schizosaccharomyces pombe (S. pombe) GATA factors, we have isolated the gaf1+ gene (GATA-factor like gene) in S. pombe. The predicted amino acid (aa) sequence of Gaf1 reveals a single zinc finger domain typical of fungal GATA factors, and the zinc finger exhibits 60% aa identity to that of human GATA-1. The open reading frame of Gaf1 predicts a protein of Mr 32 kDa consisting of 290 intronless amino acids. Disruption of this gene has no effect on cell viability and growth rate. The GST-Gaf1 fusion protein binds specifically to GATA motifs of its own promoter as well as DAL7 UAS, a canonical GATA motif of Saccharomyces cerevisiae (S. cerevisiae) The specific DNA-binding activity resides within the N-terminal half of Gaf1 (Gaf1N; aa 1-120) containing the zinc finger, whereas the C-terminal half (Gaf1C; aa 121-290) contains transactivation sequences that induce the expression of the lacZ reporter when fused to the GAL4 DNA binding domain. These results demonstrate that Gaf1 may function as a transcriptional activator consisting of DNA-binding and transactivation domains.","authors":"Hoe KL, Won MS, Chung KS, Park SK, Kim DU, Jang YJ, Yoo OJ, Yoo HS","authors_abbrev":"Hoe KL et al.","pubmed_publication_date":"30 Jul 1998","pubmed_entrez_date":"1998-08-26","publication_year":"1998","canto_session_key":"c3bdc1e547b6330a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-30 15:38:40","canto_approved_date":"2024-03-31 08:03:12","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-06-30 09:56:52","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1902.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-30"},{"uniquename":"PMID:2958638","title":"High level of complexity of small nuclear RNAs in fungi and plants.","citation":"J Mol Biol 1987 Jul 20;196(2):355-61","abstract":"The complexity of the trimethylguanosine-capped, small nuclear RNA (snRNA) populations in a number of organisms has been examined using immunoprecipitation and two-dimensional gels. From the fungi Aspergillus nidulans and Schizosaccharomyces pombe, over 30 major snRNAs can be resolved. The most abundant of these correspond to the putative analogues of vertebrate U1, U2, U4 and U5, which have been reported to be precipitated by anti-Sm antibodies, but other snRNAs are little less abundant than the major Sm-precipitable species. A similarly high level of complexity of snRNAs is detected in pea plants. In Candida albicans, the snRNAs are somewhat less numerous (about 22 major species) and are substantially less abundant than those of the above fungi, features shared with another budding yeast, Saccharomyces cerevisiae. Ten species of human snRNA have been reported; on two-dimensional gels, a number of additional snRNAs can be resolved from human cells. Each fungus, as well as pea plants, contains snRNAs substantially larger than any reported from vertebrates or detected in the human RNA used here. It appears that many eukaryotes contain substantially more species of snRNA than was previously believed.","authors":"Tollervey D","authors_abbrev":"Tollervey D","pubmed_publication_date":"20 Jul 1987","pubmed_entrez_date":"1987-07-20","publication_year":"1987","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39228319","title":"Natural transposable element insertions contribute to host fitness in model yeasts.","citation":"Genome Biol Evol 2024 Sep 04;","abstract":"Transposable elements (TEs) are ubiquitous in the eukaryote genomes, but their evolutionary and functional significance remains largely obscure and contentious. Here, we explore the evolution and functional impact of TEs in two model unicellular eukaryotes, the fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae, which diverged around 330-420 million years ago. We analyze the distribution of LTR retrotransposons (LTR-RTs, the only TE order identified in both species) and their solo-LTR derivatives in 35 strains of S. pombe and 128 strains of S. cerevisiae. We find that natural LTR-RT and solo-LTR insertions exhibit high presence-absence polymorphism among individuals in both species. Population genetics analyses show that solo-LTR insertions experienced functional constraints similar to synonymous sites of host genes in both species, indicating a majority of solo-LTR insertions might have evolved in a neutral manner. When knocking out 9 representative solo-LTR insertions separately in the S. pombe strain 972h- and 12 representative solo-LTR insertions separately in the S. cerevisiae strain S288C, we find that one solo-LTR insertion in S. pombe has significant effect on the fitness and transcriptomes of its host. Together, our findings indicate that a fraction of natural TE insertions likely shape their host transcriptomes and thereby contribute to their host fitness, with implications for understanding the functional significance of TEs in eukaryotes.","doi":"10.1093/gbe/evae193","authors":"Wang Y, Xu H, He Q, Wu Z, Han GZ","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"04 Sep 2024","pubmed_entrez_date":"2024-09-04","publication_year":"2024","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2024-09-04 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29121084","title":"Fission yeast strains with circular chromosomes require the 9-1-1 checkpoint complex for the viability in response to the anti-cancer drug 5-fluorodeoxyuridine.","citation":"PLoS One 2017;12(11):e0187775","abstract":"Thymidine kinase converts 5-fluorodeoxyuridine to 5-fluorodeoxyuridine monophosphate, which causes disruption of deoxynucleotide triphosphate ratios. The fission yeast Schizosaccharomyces pombe does not express endogenous thymidine kinase but 5-fluorodeoxyuridine inhibits growth when exogenous thymidine kinase is expressed. Unexpectedly, we found that 5-fluorodeoxyuridine causes S phase arrest even without thymidine kinase expression. DNA damage checkpoint proteins such as the 9-1-1 complex were required for viability in the presence of 5-fluorodeoxyuridine. We also found that strains with circular chromosomes, due to loss of pot1+, which have higher levels of replication stress, were more sensitive to loss of the 9-1-1 complex in the presence of 5-fluorodeoxyuridine. Thus, our results suggest that strains carrying circular chromosomes exhibit a greater dependence on DNA damage checkpoints to ensure viability in the presence of 5-fluorodeoxyuridine compared to stains that have linear chromosomes.","doi":"10.1371/journal.pone.0187775","authors":"Shamim HM, Minami Y, Tanaka D, Ukimori S, Murray JM, Ueno M","authors_abbrev":"Shamim HM et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-11-10","publication_year":"2017","canto_session_key":"3dfeaa1aef6b51a4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-11-11 01:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G4.04c","SPAC1952.07","SPAC664.07c","SPAC26H5.06"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:16137929","title":"Apoptosis and lipoapoptosis in the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2005 Dec;5(12):1199-206","abstract":"Yeasts being simple eukaryotes are established genetic systems that are often employed to solve important biological questions. Recently, it has become evident that certain cell death programs exist in these unicellular organisms. For example, it has been shown recently that strains of the fission yeast Schizosaccharomyces pombe deficient in triacylglycerol synthesis undergo cell death with prominent apoptotic markers. This minireview is intended to discuss key developments that have rendered fission yeast useful both as a tool and as a model for apoptosis and lipoapoptosis research. It is attempted to delineate a putative signaling pathway leading to the execution of lipoapoptosis in the fission yeast. Although in its infancy, apoptosis research in the fission yeast promises exciting breakthroughs in the near future.","authors":"Low CP, Liew LP, Pervaiz S, Yang H","authors_abbrev":"Low CP et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-09-03","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30617184","title":"A stable tetramer is not the only oligomeric state that mitochondrial single-stranded DNA binding proteins can adopt.","citation":"J Biol Chem 2019 Mar 15;294(11):4137-4144","abstract":"Mitochondrial single-stranded DNA (ssDNA)-binding proteins (mtSSBs) are required for mitochondrial DNA replication and stability and are generally assumed to form homotetramers, and this species is proposed to be the one active for ssDNA binding. However, we recently reported that the mtSSB from  Saccharomyces cerevisiae  ( Sc Rim1) forms homotetramers at high protein concentrations, whereas at low protein concentrations, it dissociates into dimers that bind ssDNA with high affinity. In this work, using a combination of analytical ultracentrifugation techniques and DNA binding experiments with fluorescently labeled DNA oligonucleotides, we tested whether the ability of  Sc Rim1 to form dimers is unique among mtSSBs. Although human mtSSBs and those from  Schizosaccharomyces pombe ,  Xenopus laevis , and  Xenopus tropicalis  formed stable homotetramers, the mtSSBs from  Candida albicans  and  Candida parapsilosis  formed stable homodimers. Moreover, the mtSSBs from  Candida nivariensis  and  Candida castellii  formed tetramers at high protein concentrations, whereas at low protein concentrations, they formed dimers, as did  Sc Rim1. Mutational studies revealed that the ability to form either stable tetramers or dimers depended on a complex interplay of more than one amino acid at the dimer-dimer interface and the C-terminal unstructured tail. In conclusion, our findings indicate that mtSSBs can adopt different oligomeric states, ranging from stable tetramers to stable dimers, and suggest that a dimer of mtSSB may be a physiologically relevant species that binds to ssDNA in some yeast species.","doi":"10.1074/jbc.RA118.007048","authors":"Singh SP, Kukshal V, Galletto R","authors_abbrev":"Singh SP et al.","pubmed_publication_date":"15 Mar 2019","pubmed_entrez_date":"2019-01-09","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F3.04c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:7320083","title":"Polypeptide synthesis in cell cycle mutants of fission yeast.","citation":"J Cell Sci 1981 Oct;51:203-17","abstract":"The cell cycle of a growing cel is characterized by 3 main periodic events: DNA synthesis mitosis and cell division. These events generally lie in a dependent sequence, in which one event cannot occur unless preceding events have occurred. The existence of dependent sequences of events raises the possibility that at least some of the gene products involved in the events are synthesized in a dependent sequence parallel to the observable events. To test this hypothesis, the patterns of polypeptide synthesis were investigated in 2 types of cell cycle mutant of the fission yeast Schizosaccharomyces pombe: temperature-sensitive cell cycle (ts cdc) mutants. which become blocked in cell cycle progress at the restrictive temperature; and wee I mutants, which are defective in size control over nuclear division, and which divide at a small size. Cells of mutants and wild-type cells were labelled with [35S[ sulphate under conditions designed to maximize any differences between the labelling patterns of wild-type and mutant cell polypeptides. The polypeptides were then separated by O'Farrell 2-dimensional gel electrophoresis, and the patterns compared. Although both types of mutation affect cell cycle control, and cause a considerable alteration in the relative proportions of cellular components, an examination of over 700 polypeptides detected on gels revealed no qualitative differences between wild-type and mutant cell polypeptides. These results suggest that a large majority of the more abundant polypeptides in the growing cell are synthesized independently of cell cycle controls directly related to DNA synthesis and division, and that the synthesis of these polypeptides can occur in the absence of normal progress through the cell cycle. Dependent sequences of gene expression do not appear to make a significant contribution to total polypeptide synthesis during the cell cycle, or to the occurrence of periodic cell cycle events such as mitosis. It is suggested that such cell cycle events may result largely through the reorganization of existing cellular components, rather than by the synthesis of new ones. An unsuccessful attempt was made to detect the wee I gene product on gels by surveying a range of mutants for changes in an individual spot. The limitations of gel electrophoresis for this type of survey, and other cell cycle experiments, are discussed.","authors":"Dickinson DP","authors_abbrev":"Dickinson DP","pubmed_publication_date":"Oct 1981","pubmed_entrez_date":"1981-10-01","publication_year":"1981","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28765164","title":"Selective termination of lncRNA transcription promotes heterochromatin silencing and cell differentiation.","citation":"EMBO J 2017 Sep 01;36(17):2626-2641","abstract":"Long non-coding RNAs (lncRNAs) regulating gene expression at the chromatin level are widespread among eukaryotes. However, their functions and the mechanisms by which they act are not fully understood. Here, we identify new fission yeast regulatory lncRNAs that are targeted, at their site of transcription, by the YTH domain of the RNA-binding protein Mmi1 and degraded by the nuclear exosome. We uncover that one of them,  nam1 , regulates entry into sexual differentiation. Importantly, we demonstrate that Mmi1 binding to this lncRNA not only triggers its degradation but also mediates its transcription termination, thus preventing lncRNA transcription from invading and repressing the downstream gene encoding a mitogen-activated protein kinase kinase kinase (MAPKKK) essential to sexual differentiation. In addition, we show that Mmi1-mediated termination of lncRNA transcription also takes place at pericentromeric regions where it contributes to heterochromatin gene silencing together with RNA interference (RNAi). These findings reveal an important role for selective termination of lncRNA transcription in both euchromatic and heterochromatic lncRNA-based gene silencing processes.","doi":"10.15252/embj.201796571","authors":"Touat-Todeschini L, Shichino Y, Dangin M, Thierry-Mieg N, Gilquin B, Hiriart E, Sachidanandam R, Lambert E, Brettschneider J, Reuter M, Kadlec J, Pillai R, Yamashita A, Yamamoto M, Verdel A","authors_abbrev":"Touat-Todeschini L et al.","pubmed_publication_date":"01 Sep 2017","pubmed_entrez_date":"2017-08-03","publication_year":"2017","canto_session_key":"79c4b71f272e27d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-09 17:28:48","canto_approved_date":"2022-11-07 12:01:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-25 15:25:54","canto_added_date":"2017-08-04 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":64,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1393.07c","SPCC736.12c","SPBC29A10.14","SPAC1F3.01","SPAC13A11.03","SPBC1347.12","SPBC1652.01","SPAC17A5.18c","SPCC70.09c","SPBP8B7.04","SPAC23C4.07","SPAC27D7.13c","SPBC428.08c","SPBC2G2.09c","SPNCRNA.1459","SPBC2D10.06","SPAC5D6.01","SPAC6B12.16","SPCC188.13c","SPCC4E9.01c","SPNCRNA.230","SPNCRNA.361","SPBC1D7.05","SPAC6C3.05","SPAC32A11.01","SPAP27G11.08c","SPBC216.02","SPNCRNA.1366","SPSNRNA.04","SPBC29A10.02","SPAC57A10.04","SPBC32H8.11","SPCC11E10.03","SPNCRNA.1696"],"gene_count":34,"ltp_gene_count":6,"approved_date":"2018-02-09","pdb_entries":[{"pdb_id":"5o8m","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A/B/C/D","position":"347-488"}],"title":"Crystal structure of the MmI1 YTH domain","entry_authors":"Brettschneider J,Verdel A,Kadlec J","entry_authors_abbrev":"Brettschneider J et al.","reference_uniquename":"PMID:28765164","experimental_method":"X-ray","resolution":"1.45"}]},{"uniquename":"GO_REF:0000089","title":"Representation of single-organism and multi-organism biological processes in the Gene Ontology","abstract":"We have created a standard template for classes describing the single-organism and multi-organism biological processes. The underlying equivalence axiom templates are \"P and 'bearer_of' some PATO:0002487\" (single-organism) and \"P and 'bearer_of' some PATO:0002486\" (multi-organism), where P is a biological process.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15555586","title":"Mcs2 and a novel CAK subunit Pmh1 associate with Skp1 in fission yeast.","citation":"Biochem Biophys Res Commun 2004 Dec 24;325(4):1424-32","abstract":"The Mcs6 CDK together with its cognate cyclin Mcs2 represents the CDK-activating kinase (CAK) of fission yeast Cdc2. We have attempted to determine complexes in which Mcs6 and Mcs2 mediate this and possible other functions. Here we characterize a novel interaction between Mcs2 and Skp1, a component of the SCF (Skp1-Cullin-F box protein) ubiquitin ligase. Furthermore, we identify a novel protein termed Pmh1 through its association with Skp1. Pmh1 associates with the Mcs6-Mcs2 complex, enhancing its kinase activity, and represents the apparent homolog of metazoan Mat1. Association of Mcs2 or Pmh1 with Skp1 does not appear to be involved in proteolytic degradation, as these complexes do not contain Pcu1, and levels of Mcs2 or Pmh1 are not sensitive to inhibition of SCF and the 26S proteasome. The identified interactions between Skp1 and two regulatory CAK subunits may reflect a novel mechanism to modulate activity and specificity of the Mcs6 kinase.","authors":"Bamps S, Westerling T, Pihlak A, Tafforeau L, Vandenhaute J, Mäkelä TP, Hermand D","authors_abbrev":"Bamps S et al.","pubmed_publication_date":"24 Dec 2004","pubmed_entrez_date":"2004-11-24","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC776.18c","SPBC19F8.07","SPBC409.05","SPAC17G6.12","SPBP16F5.02"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:10623474","title":"The polyubiquitin gene is essential for meiosis in fission yeast.","citation":"Exp Cell Res 2000 Jan 10;254(1):143-52","abstract":"We isolated a novel sporulation-deficient mutant of Schizosaccharomyces pombe. The mutant did not have a mitotic growth defect but aborted meiosis at the first or the second division with condensed chromosomes that failed to separate, abnormal spindle(s), and disintegrated spindle pole bodies (SPBs). During the first division, the centromeres were pulled to near the spindle poles but condensed divalent chromosomes remained at the center. The failure to proceed to anaphase was also observed during a time-lapse recording of a SPB protein tagged with green fluorescent protein. The polyubiquitin gene ubi4(+), which encoded eight ubiquitins fused in tandem, complemented this mutant. The mutation, an A to G substitution, was identified within the ubi4(+) gene at the ATG initiation codon. Disruption of the ubi4(+) gene produced the same phenotypes. The ubi4(+) mRNA was strongly induced for meiosis. However, ubiquitin increases only slightly, suggesting that the role of the polyubiquitin gene is to supply ubiquitin that is consumed by unidentified mechanisms. Before the ubi4 mutant cells entered meiosis, ubiquitin was greatly decreased indicating that shortage of ubiquitin caused abortion of meiosis. This work provides insights for the role of polyubiquitin gene and importance of ubiquitination in SPB integrity at the meiotic divisions.","authors":"Okazaki K, Okayama H, Niwa O","authors_abbrev":"Okazaki K et al.","pubmed_publication_date":"10 Jan 2000","pubmed_entrez_date":"2000-01-07","publication_year":"2000","canto_session_key":"ee139b613d53efbe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-08 17:12:51","canto_approved_date":"2024-03-29 12:18:58","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-09-24 14:30:27","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-08"},{"uniquename":"PMID:37160310","title":"BiFCo: visualizing cohesin assembly/disassembly cycle in living cells.","citation":"Life Sci Alliance 2023 Jul;6(7)","abstract":"Cohesin is a highly conserved, ring-shaped protein complex found in all eukaryotes. It consists of at least two structural maintenance of chromosomes (SMC) proteins, SMC1 and SMC3 in humans (Psm1 and Psm3 in fission yeast), and the kleisin RAD21 (Rad21 in fission yeast). Mutations in its components or regulators can lead to genetic syndromes, known as cohesinopathies, and various types of cancer. Studies in several organisms have shown that only a small fraction of each subunit assembles into complexes, making it difficult to investigate dynamic chromatin loading and unloading using fluorescent fusions in vivo because of excess soluble components. In this study, we introduce bimolecular fluorescent cohesin (BiFCo), based on bimolecular fluorescent complementation in the fission yeast  Schizosaccharomyces pombe  BiFCo selectively excludes signals from individual proteins, enabling the monitoring of complex assembly and disassembly within a physiological context throughout the entire cell cycle in living cells. This versatile system can be expanded and adapted for various genetic backgrounds and other eukaryotic models, including human cells.","doi":"10.26508/lsa.202301945","authors":"González-Martín E, Jiménez J, Tallada VA","authors_abbrev":"González-Martín E et al.","pubmed_publication_date":"Jul 2023","pubmed_entrez_date":"2023-05-09","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-05-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15047861","title":"Loss of Apm1, the micro1 subunit of the clathrin-associated adaptor-protein-1 complex, causes distinct phenotypes and synthetic lethality with calcineurin deletion in fission yeast.","citation":"Mol Biol Cell 2004 Jun;15(6):2920-31","abstract":"Calcineurin is a highly conserved regulator of Ca(2+) signaling in eukaryotes. In fission yeast, calcineurin is not essential for viability but is required for cytokinesis and Cl(-) homeostasis. In a genetic screen for mutations that are synthetically lethal with calcineurin deletion, we isolated a mutant, cis1-1/apm1-1, an allele of the apm1(+) gene that encodes a homolog of the mammalian micro1A subunit of the clathrin-associated adaptor protein-1 (AP-1) complex. The cis1-1/apm1-1 mutant as well as the apm1-deleted (Deltaapm1) cells showed distinct phenotypes: temperature sensitivity; tacrolimus (FK506) sensitivity; and pleiotropic defects in cytokinesis, cell integrity, and vacuole fusion. Electron micrographs revealed that Deltaapm1 cells showed large vesicular structures associated with Golgi stacks and accumulated post-Golgi secretory vesicles. Deltaapm1 cells also showed the massive accumulation of the exocytic v-SNARE Syb1 in the Golgi/endosomes and a reduced secretion of acid phosphatase. These phenotypes observed in apm1 mutations were accentuated upon temperature up-shift and FK506 treatment. Notably, Apm1-GFP localized to the Golgi/endosomes, the spindle pole bodies, and the medial region. These findings suggest a role for Apm1 associated with the Golgi/endosome function, thereby affecting various cellular processes, including secretion, cytokinesis, vacuole fusion, and cell integrity and also suggest that calcineurin is involved in these events.","authors":"Kita A, Sugiura R, Shoji H, He Y, Deng L, Lu Y, Sio SO, Takegawa K, Sakaue M, Shuntoh H, Kuno T","authors_abbrev":"Kita A et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-03-30","publication_year":"2004","canto_session_key":"94fed49a02da5f4a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-02-18 18:01:27","canto_approved_date":"2021-02-18 18:01:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-16 17:45:50","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP16F5.07","SPAC6G9.11","SPBC12D12.01","SPBP4H10.04","SPAC18G6.03"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2021-02-18"},{"uniquename":"PANTHER:PTHR16461","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16E9.02c","HGNC:16476"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32586625","title":"Detection of cellular G-quadruplex by using a loop structure as a structural determinant.","citation":"Biochem Biophys Res Commun 2020 Oct 08;531(1):75-83","abstract":"G-quadrupex is now known to play crucial roles in various biological reactions. However, direct evidence for its presence in cells has been limited, due to the lack of versatile and non-biased methodology. We use Rif1 binding sites on the fission yeast genome, which has been shown to adopt G4 structures, as a model to prove that Rif1 BS indeed adopt G4 structure in cells. We take advantage of the presence of a single-stranded loop in the G4 structure. Rif1BS is unique in that they contain unusually long loop sequences, and we replace them with a 18 bp I-SceI restriction site. We show in vitro that I-SceI in the loop is not cleaved when G4 is formed on duplex Rif1BS DNA, but is cleaved when G4 is not formed due to a mutation in the G-tracts. This is observed both heat-induced and transcription-induced G4 structure, and gives proof of evidence for this procedure. We apply this strategy for detection of a G4 structure at the same Rif1BS in fission yeast cells. We present evidence that in vivo cleavage of I-SceI can be a measure for the presence of G4 at the target sequence in cells as well. The method described here gives a platform strategy for genome-wide analyses of cellular G4 and their dynamic formation and disruption.","doi":"10.1016/j.bbrc.2020.05.191","authors":"Masai H, Kanoh Y, Kakusho N, Fukatsu R","authors_abbrev":"Masai H et al.","pubmed_publication_date":"08 Oct 2020","pubmed_entrez_date":"2020-06-27","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-06-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.17"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18079366","title":"Assembly mechanism of the contractile ring for cytokinesis by fission yeast.","citation":"Science 2008 Jan 04;319(5859):97-100","abstract":"Animals and fungi assemble a contractile ring of actin filaments and the motor protein myosin to separate into individual daughter cells during cytokinesis. We used fluorescence microscopy of live fission yeast cells to observe that membrane-bound nodes containing myosin were broadly distributed around the cell equator and assembled into a contractile ring through stochastic motions, after a meshwork of dynamic actin filaments appeared. Analysis of node motions and numerical simulations supported a mechanism whereby transient connections are established when myosins in one node capture and exert force on actin filaments growing from other nodes.","authors":"Vavylonis D, Wu JQ, Hao S, O'Shaughnessy B, Pollard TD","authors_abbrev":"Vavylonis D et al.","pubmed_publication_date":"04 Jan 2008","pubmed_entrez_date":"2007-12-15","publication_year":"2008","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11453251","title":"Factors involved in the regulation of the Schizosaccharomyces pombe malic enzyme gene.","citation":"Curr Genet 2001 Jun;39(4):222-30","abstract":"Transcription of the Schizosaccharomyces pombe malic enzyme gene, mae2, is induced when cells are grown on high glucose concentrations or under nonaerated conditions. Two cis-acting elements in the mae2 promoter, upstream activator sequences UAS1 and UAS2, are required for basal expression, whilst three negative-acting, upstream repressor sequences are involved in general derepression of mae2. Both the Pka1 and Sty1 signal transduction pathways are involved in the induced expression of mae2 under fermentative conditions. Expression of mae2 seems to be regulated in response to the carbon source, lack of oxygen and osmotic stress conditions, probably to assist in maintaining the intracellular redox balance.","authors":"Groenewald M, Viljoen-Bloom M","authors_abbrev":"Groenewald M et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-07-17","publication_year":"2001","canto_session_key":"a990ea85501ed7d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-28 16:04:27","canto_approved_date":"2022-12-13 13:30:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-06 06:47:13","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPCC794.12c","SPBC29B5.01","SPBC409.07c","SPBC106.10","SPAC8C9.03"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2013-10-28"},{"uniquename":"PMID:17964939","title":"Structural investigations into microtubule-MAP complexes.","citation":"Methods Cell Biol 2008;84:425-44","abstract":"Microtubules interact with a large variety of factors commonly referred to as either molecular motors (kinesins, dyneins) or structural microtubule-associated proteins (MAPs). MAPs do not exhibit motor activity, but regulate microtubule dynamics and their interactions with molecular motors, and organelles such as kinetochores or centrosomes. Structural investigations into microtubule-kinesin motor complexes are quite advanced today and by helical three-dimensional (3-D) analysis reveal a resolution of the motor-tubulin interface at <1.0 nm. However, due to their flexible structure MAPs like tau or MAP2C cannot be visualized in the same straightforward manner. Helical averaging usually reveals only the location of strong binding sites while the overall structure of the MAP remains unsolved. Other MAPs such as EB1 bind very selectively only to some parts of the microtubule lattice such as the lattice seam. Thus, they do not reveal a stoichiometric tubulin:MAP-binding ratio that would allow for a quantitative helical 3-D analysis. Therefore, to get a better view on the structure of microtubule-MAP complexes we often used a strategy that combined cryo-electron microscopy and helical or tomographic 3-D analysis with freeze-drying and high-resolution unidirectional surface shadowing. 3-D analysis of ice-embedded specimens reveals their full 3-D volume. This relies either on a repetitive structure following a helical symmetry that can be used for averaging or suffers from the limited resolution that is currently achievable with cryotomography. Surface metal shadowing exclusively images surface-exposed features at very high contrast, adding highly valuable information to 2-D or 3-D data of vitrified structures.","authors":"Hoenger A, Gross H","authors_abbrev":"Hoenger A et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2007-10-30","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24463734","title":"Ectopic A-lattice seams destabilize microtubules.","citation":"Nat Commun 2014;5:3094","abstract":"Natural microtubules typically include one A-lattice seam within an otherwise helically symmetric B-lattice tube. It is currently unclear how A-lattice seams influence microtubule dynamic instability. Here we find that including extra A-lattice seams in GMPCPP microtubules, structural analogues of the GTP caps of dynamic microtubules, destabilizes them, enhancing their median shrinkage rate by >20-fold. Dynamic microtubules nucleated by seeds containing extra A-lattice seams have growth rates similar to microtubules nucleated by B-lattice seeds, yet have increased catastrophe frequencies at both ends. Furthermore, binding B-lattice GDP microtubules to a rigor kinesin surface stabilizes them against shrinkage, whereas microtubules with extra A-lattice seams are stabilized only slightly. Our data suggest that introducing extra A-lattice seams into dynamic microtubules destabilizes them by destabilizing their GTP caps. On this basis, we propose that the single A-lattice seam of natural B-lattice MTs may act as a trigger point, and potentially a regulation point, for catastrophe.","doi":"10.1038/ncomms4094","authors":"Katsuki M, Drummond DR, Cross RA","authors_abbrev":"Katsuki M et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-01-28","publication_year":"2014","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-10-29 01:33:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41542546","title":"Love-thy-neighbor: Neural networks for tracking and lineage tracing in budding yeast.","citation":"bioRxiv 2026 Jan 09;","abstract":"Tracking and lineage tracing are widely needed tasks in biological image analysis. For cells that grow and divide, tracking is challenging because cells change in number, shape, and size throughout a recording. As the time interval between images increases, it becomes more difficult to establish correspondences between cells across timepoints. Consequently, tracking has to be performed between consecutive or temporally close images, which leads to exponentially decreasing tracking accuracy and thus high sensitivity to error rates. For budding yeast, this challenge is further heightened by the similarity of cells in colonies, their dense packing, the asymmetric nature of cell divisions, and movement due to growth of the colony. A related task, lineage tracing, is similarly challenging without fluorescent markers due to multiple potential mother cells surrounding a new daughter cell. Here, we present neural networks for budding yeast tracking and lineage tracing, named LYN-track and LYN-trace, respectively. These methods leverage fine geometric features of cells and their neighborhoods. To train and test the algorithms, we recorded and annotated new budding and fission yeast microscopy movies (78,852 frame-to-frame tracklets, 2,512 images), which we make freely available. On these and existing datasets, our neural network-based methods demonstrate robust, above state-of-the-art performance. Both tools have been integrated into graphical user interfaces (GUIs), available on Github, and can be straightforwardly retrained with custom data if desired.","doi":"10.64898/2026.01.09.698579","authors":"Zelic M, Gligorovski V, Labbaf F, Labagnara M, Oesterle R, Brenna G, Massard F, Chethan SG, Li W, Martin SG, Hauf S, Rahi SJ","authors_abbrev":"Zelic M et al.","pubmed_publication_date":"09 Jan 2026","pubmed_entrez_date":"2026-01-16","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-01-17 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16256112","title":"Stg 1 is a novel SM22/transgelin-like actin-modulating protein in fission yeast.","citation":"FEBS Lett 2005 Nov 21;579(28):6311-6","abstract":"We identified a novel actin-modulating protein Stg 1 in the fission yeast Schizosaccharomyces pombe. Stg 1 is similar to mammalian SM22/transgelin, and biochemical experiments showed that Stg 1 crosslinked F-actin. Microscopic observation suggested that Stg 1 was a component of actin patch. Overexpression of Stg 1 caused a defect in cytokinesis by suppressing the formation of a contractile ring and formation of abnormal aggregates of F-actin in the ends and mid-region of cells. Although distribution of the actin cytoskeleton was not affected by disrupting Stg 1(+), genetic interaction suggested that Stg 1 was likely involved in controlling the organization of the actin cytoskeleton in cell morphogenesis and cytokinesis in fission yeast.","authors":"Nakano K, Bunai F, Numata O","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"21 Nov 2005","pubmed_entrez_date":"2005-11-01","publication_year":"2005","canto_session_key":"b7d4f36518d2b9c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-16 15:28:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-29 08:30:37","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.10c","SPAC12B10.07","SPBC32H8.12c","SPAC631.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-08-29"},{"uniquename":"PMID:6285312","title":"The 5.8S RNA gene sequence and the ribosomal repeat of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1982 May 11;10(9):2851-64","abstract":"We have characterized the rRNA gene repeat in Schizosaccharomyces pombe. This repeat, which does not contain the 5S RNA gene, is found in a 10.4 kb HindIII DNA fragment. We have determined the nucleotide sequences of the S. pombe 5.8S RNA gene and intergenic spacers from two different 10.4 kb DNA fragments. Analysis of isolated total cellular 5.8S RNA revealed the presence of eight species of 5.8S RNA, differing in the number of nucleotides at the 5'-end. The eight 4.8S RNA species vary in length from 158 to 165 nucleotides. Apart from the heterogeneity observed at the 5'-end, the sequence of the eight 5.8S RNA species appears to be identical and is the same sequence as coded for by the 5.8S genes. The gene sequence shows great homology to the 5.8S RNA genes or S. cerevisiae and N. crassa. Most of the base differences are confined to the highly variable stem though to be involved in co-axial helix stacking with the 25S RNA, where base pairing is nearly identical despite the sequence differences. Secondary structure models are examined in light of 5.8S RNA oligonucleotide conservation across species from yeasts to higher eukaryotes.","authors":"Schaak J, Mao J, Söll D","authors_abbrev":"Schaak J et al.","pubmed_publication_date":"11 May 1982","pubmed_entrez_date":"1982-05-11","publication_year":"1982","canto_session_key":"92d938673088c2a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-20 15:49:38","canto_approved_date":"2019-11-20 15:49:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-20 15:49:28","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPRRNA.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-11-20"},{"uniquename":"PMID:12955454","title":"Genetic and cytological characterization of the RecA-homologous proteins Rad51 and Dmc1 of Schizosaccharomyces pombe.","citation":"Curr Genet 2004 Jan;44(6):317-28","abstract":"The Schizosaccharomyces pombe rad51(+) and dmc1(+) genes code for homologues of the Escherichia coli recombination protein RecA. Deletion of rad51(+) causes slow growth, retardation of cell division and a decrease in viability. rad51Delta cells have a defect in mating-type switching. The DNA modification at the mating-type locus required for mating-type switching contributes to slow growth in the rad51 mutant. Cell mating is reduced in crosses homozygous for rad51Delta. Ectopic expression of the dmc1(+) gene allowed us to demonstrate that the reduction in meiotic recombination in dmc1 mutants is not caused by a disturbance of rad24 expression from the dmc1- rad24 bicistronic RNA. We describe the functional defects of terminally epitope-tagged Dmc1 and Rad51 and discuss it in terms of protein interaction. Presumptive Rad51 and Dmc1 foci were detected on spreads of meiotic chromatin.","authors":"Grishchuk AL, Kraehenbuehl R, Molnar M, Fleck O, Kohli J","authors_abbrev":"Grishchuk AL et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2003-09-05","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25106870","title":"ATP insertion opposite 8-oxo-deoxyguanosine by Pol4 mediates error-free tolerance in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2014 Sep;42(15):9821-37","abstract":"7,8-Dihydro-8-oxo-deoxyguanosine (8oxodG) is a highly premutagenic DNA lesion due to its ability to mispair with adenine. Schizosaccharomyces pombe lacks homologs for relevant enzymes that repair 8oxodG, which suggests that this lesion could be persistent and must be tolerated. Here we show that SpPol4, the unique PolX in fission yeast, incorporates ATP opposite 8oxodG almost exclusively when all nucleotides (ribos and deoxys) are provided at physiological concentrations. Remarkably, this SpPol4-specific reaction could also occur during the NHEJ of DSBs. In cell extracts, misincorporation of ATP opposite 8oxodG was shown to be SpPol4-specific, although RNase H2 efficiently recognized the 8oxodG:AMP mispair to remove AMP and trigger error-free incorporation of dCTP. These data are the first evidence that ribonucleotides can be used safely for 8oxodG tolerance, suggesting that insertion of the highly abundant ATP substrate could be beneficial to promote efficient and error-free repair of 8oxodG-associated DSBs. Moreover, we demonstrate that purified SpPol4 uses 8oxo-dGTP and 8oxo-GTP as substrates for DNA polymerization, although with poor efficiency compared to the incorporation of undamaged nucleotides opposite either 8oxodG or undamaged templates. This suggests that SpPol4 is specialized in tolerating 8oxodG as a DNA template, without contributing significantly to the accumulation of this lesion in the DNA.","doi":"10.1093/nar/gku711","authors":"Sastre-Moreno G, Sánchez A, Esteban V, Blanco L","authors_abbrev":"Sastre-Moreno G et al.","pubmed_publication_date":"Sep 2014","pubmed_entrez_date":"2014-08-10","publication_year":"2014","canto_session_key":"985b694ee778db28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Luis Blanco","canto_first_approved_date":"2014-10-22 15:34:34","canto_approved_date":"2025-09-04 10:36:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-21 12:00:49","canto_added_date":"2014-08-13 00:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Luis Blanco","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.06c","SPAC4G9.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-10-22"},{"uniquename":"","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC902.06","SPCC1393.13","SPAC23A1.14c","SPAC17C9.13c","SPAC1A6.10","SPAC27E2.03c","SPBC119.03","SPCC1827.07c","SPCC825.02","SPBPJ4664.04","SPAC1565.02c","SPCC663.05c","SPBC19G7.13","SPCC970.12","SPAP8A3.02c","SPAC13F5.03c","SPAC18B11.04","SPCC24B10.08c","SPCC320.14","SPCC24B10.21","SPAC1527.03","SPAC27D7.03c","SPAC1834.02","SPAC25A8.01c","SPAC19B12.10","SPBC8D2.04"],"gene_count":26,"ltp_gene_count":0},{"uniquename":"PMID:25414009","title":"Fission yeast RNA triphosphatase reads an Spt5 CTD code.","citation":"RNA 2015 Jan;21(1):113-23","abstract":"mRNA capping enzymes are directed to nascent RNA polymerase II (Pol2) transcripts via interactions with the carboxy-terminal domains (CTDs) of Pol2 and transcription elongation factor Spt5. Fission yeast RNA triphosphatase binds to the Spt5 CTD, comprising a tandem repeat of nonapeptide motif TPAWNSGSK. Here we report the crystal structure of a Pct1·Spt5-CTD complex, which revealed two CTD docking sites on the Pct1 homodimer that engage TPAWN segments of the motif. Each Spt5 CTD interface, composed of elements from both subunits of the homodimer, is dominated by van der Waals contacts from Pct1 to the tryptophan of the CTD. The bound CTD adopts a distinctive conformation in which the peptide backbone makes a tight U-turn so that the proline stacks over the tryptophan. We show that Pct1 binding to Spt5 CTD is antagonized by threonine phosphorylation. Our results fortify an emerging concept of an \"Spt5 CTD code\" in which (i) the Spt5 CTD is structurally plastic and can adopt different conformations that are templated by particular cellular Spt5 CTD receptor proteins; and (ii) threonine phosphorylation of the Spt5 CTD repeat inscribes a binary on-off switch that is read by diverse CTD receptors, each in its own distinctive manner.","doi":"10.1261/rna.048181.114","authors":"Doamekpor SK, Schwer B, Sanchez AM, Shuman S, Lima CD","authors_abbrev":"Doamekpor SK et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-11-22","publication_year":"2015","canto_session_key":"9b977cf97803274d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-11-23 01:15:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.19","SPBC25H2.13c","SPAC644.04"],"gene_count":3,"ltp_gene_count":3,"pdb_entries":[{"pdb_id":"4pn0","gene_chains":[{"gene_uniquename":"SPAC644.04","chain":"A/B/C/D","position":"1-303"}],"title":"Structure of S. pombe Pct1 RNA triphosphatase","entry_authors":"Lima CD,Doamekpor SK","entry_authors_abbrev":"Lima CD et al.","reference_uniquename":"PMID:25414009","experimental_method":"X-ray","resolution":"2.6"},{"pdb_id":"4pn1","gene_chains":[{"gene_uniquename":"SPAC644.04","chain":"A/B/C/D","position":"1-303"}],"title":"Structure of S. pombe Pct1 RNA triphosphatase in complex with the Spt5 CTD","entry_authors":"Lima CD,Doamekpor SK","entry_authors_abbrev":"Lima CD et al.","reference_uniquename":"PMID:25414009","experimental_method":"X-ray","resolution":"2.803"}]},{"uniquename":"PMID:9819443","title":"Regulation of the Mts1-Mts2-dependent ade6-M26 meiotic recombination hot spot and developmental decisions by the Spc1 mitogen-activated protein kinase of fission yeast.","citation":"Mol Cell Biol 1998 Dec;18(12):7575-83","abstract":"The M26 meiotic recombination hot spot in the ade6 gene of Schizosaccharomyces pombe is activated by the heterodimeric M26 binding protein Mts1-Mts2. The individual Mts1 (Atf1, Gad7) and Mts2 (Pcr1) proteins are also transcription factors involved in developmental decisions. We report that the Mts proteins are key effectors of at least two distinct classes of developmental decisions regulated by the mitogen-activated protein (MAP) kinase cascade. The first class (osmoregulation, spore viability, and spore quiescence) requires the Spc1 MAP kinase and the Mts1 protein but does not require the Mts2 protein. The second class (mating, meiosis, and recombination hot spot activation) requires the Spc1 kinase and the Mts1-Mts2 heterodimer. Northern and Western blotting eliminated any significant role for the Spc1 kinase in regulating the expression levels of the Mts proteins. Gel mobility shift experiments indicated that the Mts1-Mts2 heterodimer does not need to be phosphorylated to bind to ade6-M26 DNA in vitro. However, in vivo dimethyl sulfate footprinting demonstrated that protein-DNA interaction within cells is dependent upon the Spc1 MAP kinase, which phosphorylates the Mts1 protein. Thus, the Spc1 kinase helps regulate the effector activities of the Mts1-Mts2 heterodimer in part by modulating its ability to occupy the M26 DNA site in vivo. Meiotic recombination hot spot function is likely the result of DNA conformational changes imparted by binding of the Mts1-Mts2 meiotic transcription factor.","authors":"Kon N, Schroeder SC, Krawchuk MD, Wahls WP","authors_abbrev":"Kon N et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1998-11-20","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:17174892","title":"Single Holliday junctions are intermediates of meiotic recombination.","citation":"Cell 2006 Dec 15;127(6):1167-78","abstract":"Crossing-over between homologous chromosomes facilitates their accurate segregation at the first division of meiosis. Current models for crossing-over invoke an intermediate in which homologs are connected by two crossed-strand structures called Holliday junctions. Such double Holliday junctions are a prominent intermediate in Saccharomyces cerevisiae meiosis, where they form preferentially between homologs rather than between sister chromatids. In sharp contrast, we find that single Holliday junctions are the predominant intermediate in Schizosaccharomyces pombe meiosis. Furthermore, these single Holliday junctions arise preferentially between sister chromatids rather than between homologs. We show that Mus81 is required for Holliday junction resolution, providing further in vivo evidence that the structure-specific endonuclease Mus81-Eme1 is a Holliday junction resolvase. To reconcile these observations, we present a unifying recombination model applicable for both meiosis and mitosis in which single Holliday junctions arise from single- or double-strand breaks, lesions postulated by previous models to initiate recombination.","authors":"Cromie GA, Hyppa RW, Taylor AF, Zakharyevich K, Hunter N, Smith GR","authors_abbrev":"Cromie GA et al.","pubmed_publication_date":"15 Dec 2006","pubmed_entrez_date":"2006-12-19","publication_year":"2006","canto_session_key":"17284db3695fec9a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22238674","title":"Repression of meiotic genes by antisense transcription and by Fkh2 transcription factor in Schizosaccharomyces pombe.","citation":"PLoS One 2012;7(1):e29917","abstract":"In S. pombe, about 5% of genes are meiosis-specific and accumulate little or no mRNA during vegetative growth. Here we use Affymetrix tiling arrays to characterize transcripts in vegetative and meiotic cells. In vegetative cells, many meiotic genes, especially those induced in mid-meiosis, have abundant antisense transcripts. Disruption of the antisense transcription of three of these mid-meiotic genes allowed vegetative sense transcription. These results suggest that antisense transcription represses sense transcription of meiotic genes in vegetative cells. Although the mechanism(s) of antisense mediated transcription repression need to be further explored, our data indicates that RNAi machinery is not required for repression. Previously, we and others used non-strand specific methods to study splicing regulation of meiotic genes and concluded that 28 mid-meiotic genes are spliced only in meiosis. We now demonstrate that the \"unspliced\" signal in vegetative cells comes from the antisense RNA, not from unspliced sense RNA, and we argue against the idea that splicing regulates these mid-meiotic genes. Most of these mid-meiotic genes are induced in mid-meiosis by the forkhead transcription factor Mei4. Interestingly, deletion of a different forkhead transcription factor, Fkh2, allows low levels of sense expression of some mid-meiotic genes in vegetative cells. We propose that vegetative expression of mid-meiotic genes is repressed at least two independent ways: antisense transcription and Fkh2 repression.","doi":"10.1371/journal.pone.0029917","authors":"Chen HM, Rosebrock AP, Khan SR, Futcher B, Leatherwood JK","authors_abbrev":"Chen HM et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-01-13","publication_year":"2012","canto_session_key":"e7cc4d83818c4b9a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33169133","title":"G-quadruplex binding protein Rif1, a key regulator of replication timing.","citation":"J Biochem 2021 Feb 06;169(1):1-14","abstract":"DNA replication is spatially and temporally regulated during S phase to execute efficient and coordinated duplication of entire genome. Various epigenomic mechanisms operate to regulate the timing and locations of replication. Among them, Rif1 plays a major role to shape the 'replication domains' that dictate which segments of the genome are replicated when and where in the nuclei. Rif1 achieves this task by generating higher-order chromatin architecture near nuclear membrane and by recruiting a protein phosphatase. Rif1 is a G4 binding protein, and G4 binding activity of Rif1 is essential for replication timing regulation in fission yeast. In this article, we first summarize strategies by which cells regulate their replication timing and then describe how Rif1 and its interaction with G4 contribute to regulation of chromatin architecture and replication timing.","doi":"10.1093/jb/mvaa128","authors":"Alavi S, Ghadiri H, Dabirmanesh B, Moriyama K, Khajeh K, Masai H","authors_abbrev":"Alavi S et al.","pubmed_publication_date":"06 Feb 2021","pubmed_entrez_date":"2020-11-10","publication_year":"2021","canto_session_key":"705646c40c95a84a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-11-12 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18948543","title":"Splicing factors facilitate RNAi-directed silencing in fission yeast.","citation":"Science 2008 Oct 24;322(5901):602-6","abstract":"Heterochromatin formation at fission yeast centromeres is directed by RNA interference (RNAi). Noncoding transcripts derived from centromeric repeats are processed into small interfering RNAs (siRNAs) that direct the RNA-induced transcriptional silencing (RITS) effector complex to engage centromere transcripts, resulting in recruitment of the histone H3 lysine 9 methyltransferase Clr4, and hence silencing. We have found that defects in specific splicing factors, but not splicing itself, affect the generation of centromeric siRNAs and consequently centromeric heterochromatin integrity. Moreover, splicing factors physically associate with Cid12, a component of the RNAi machinery, and with centromeric chromatin, consistent with a direct role in RNAi. We propose that spliceosomal complexes provide a platform for siRNA generation and hence facilitate effective centromere repeat silencing.","doi":"10.1126/science.1164029","authors":"Bayne EH, Portoso M, Kagansky A, Kos-Braun IC, Urano T, Ekwall K, Alves F, Rappsilber J, Allshire RC","authors_abbrev":"Bayne EH et al.","pubmed_publication_date":"24 Oct 2008","pubmed_entrez_date":"2008-10-25","publication_year":"2008","canto_session_key":"7d409d497eb075ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-30 14:21:05","canto_approved_date":"2024-04-03 14:00:36","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-01-30 14:12:30","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":43,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.03","SPAC27F1.09c","SPBP22H7.07","SPCC188.13c","SPAC664.01c","SPCC777.14","SPBC215.12","SPCC736.11","SPBC19C2.01","SPCC663.12","SPBC4B4.09","SPBC146.07","SPBC428.08c","SPAC227.12","SPAPJ698.03c","SPAC3A12.11c","SPBC6B1.07"],"gene_count":17,"ltp_gene_count":15,"approved_date":"2024-01-30"},{"uniquename":"PMID:12135491","title":"Rum1, an inhibitor of cyclin-dependent kinase in fission yeast, is negatively regulated by mitogen-activated protein kinase-mediated phosphorylation at Ser and Thr residues.","citation":"Eur J Biochem 2002 Jul;269(14):3511-21","abstract":"The p25(rum1) is an inhibitor of Cdc2 kinase expressed in fission yeast and plays an important role in cell-cycle control. As its amino-acid sequence suggests that p25(rum1) has putative phosphorylation sites for mitogen-activated protein kinase (MAPK), we investigated the ability of MAPK to phosphorylate p25(rum1). Direct in vitro kinase assay using GST-fusion proteins of wild-type as well as various mutants of p25(rum1) demonstrated that MAPK phosphorylates the N-terminal portion of p25(rum1) and residues Thr13 and Ser19 are major phosphorylation sites for MAPK. In addition, phosphorylation of p25(rum1) by MAPK revealed markedly reduced Cdc2 kinase inhibitor ability of the protein. Together with the fact that replacement of both Thr13 and Ser19 with Glu, which mimics the phosphorylated state of these residues, also significantly reduces the activity of p25(rum1) as a Cdc2 inhibitor, it was suggested that the phosphorylation of Thr13 and Ser19 negatively regulates the function of p25(rum1). Further evidence indicates that phosphorylation of Thr13 and Ser19 may retain a negative effect on the function of p25(rum1) even in vivo. Therefore, MAPK may regulate the function of p25(rum1) via phosphorylation of its Thr and Ser residues and thus participate in cell cycle control in fission yeast.","authors":"Matsuoka K, Kiyokawa N, Taguchi T, Matsui J, Suzuki T, Mimori K, Nakajima H, Takenouchi H, Weiran T, Katagiri YU, Fujimoto J","authors_abbrev":"Matsuoka K et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-07-24","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC32F12.09"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:7623848","title":"An alternative eukaryotic DNA excision repair pathway.","citation":"Mol Cell Biol 1995 Aug;15(8):4572-7","abstract":"DNA lesions induced by UV light, cyclobutane pyrimidine dimers, and (6-4)pyrimidine pyrimidones are known to be repaired by the process of nucleotide excision repair (NER). However, in the fission yeast Schizosaccharomyces pombe, studies have demonstrated that at least two mechanisms for excising UV photo-products exist; NER and a second, previously unidentified process. Recently we reported that S. pombe contains a DNA endonuclease, SPDE, which recognizes and cleaves at a position immediately adjacent to cyclobutane pyrimidine dimers and (6-4)pyrimidine pyrimidones. Here we report that the UV-sensitive S. pombe rad12-502 mutant lacks SPDE activity. In addition, extracts prepared from the rad12-502 mutant are deficient in DNA excision repair, as demonstrated in an in vitro excision repair assay. DNA repair activity was restored to wild-type levels in extracts prepared from rad12-502 cells by the addition of partially purified SPDE to in vitro repair reaction mixtures. When the rad12-502 mutant was crossed with the NER rad13-A mutant, the resulting double mutant was much more sensitive to UV radiation than either single mutant, demonstrating that the rad12 gene product functions in a DNA repair pathway distinct from NER. These data directly link SPDE to this alternative excision repair process. We propose that the SPDE-dependent DNA repair pathway is the second DNA excision repair process present in S. pombe.","authors":"Freyer GA, Davey S, Ferrer JV, Martin AM, Beach D, Doetsch PW","authors_abbrev":"Freyer GA et al.","pubmed_publication_date":"Aug 1995","pubmed_entrez_date":"1995-08-01","publication_year":"1995","canto_session_key":"ab4820f788afe927","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-12-22 17:08:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-20 15:13:42","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPAC1D4.12","SPAC3G6.06c","SPBC3E7.08c","SPAC30D11.10"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-11-20"},{"uniquename":"PMID:17872511","title":"RNA-specific ribonucleotidyl transferases.","citation":"RNA 2007 Nov;13(11):1834-49","abstract":"RNA-specific nucleotidyl transferases (rNTrs) are a diverse family of template-independent polymerases that add ribonucleotides to the 3'-ends of RNA molecules. All rNTrs share a related active-site architecture first described for DNA polymerase beta and a catalytic mechanism conserved among DNA and RNA polymerases. The best known examples are the nuclear poly(A) polymerases involved in the 3'-end processing of eukaryotic messenger RNA precursors and the ubiquitous CCA-adding enzymes that complete the 3'-ends of tRNA molecules. In recent years, a growing number of new enzymes have been added to the list that now includes the \"noncanonical\" poly(A) polymerases involved in RNA quality control or in the readenylation of dormant messenger RNAs in the cytoplasm. Other members of the group are terminal uridylyl transferases adding single or multiple UMP residues in RNA-editing reactions or upon the maturation of small RNAs and poly(U) polymerases, the substrates of which are still not known. 2'-5'Oligo(A) synthetases differ from the other rNTrs by synthesizing oligonucleotides with 2'-5'-phosphodiester bonds de novo.","authors":"Martin G, Keller W","authors_abbrev":"Martin G et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-09-18","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8660462","title":"Comparison of three 3' non-coding regions in Schizosaccharomyces pombe expression vectors: efficiencies of transcription termination and mRNA 3'-end formation.","citation":"Curr Genet 1996 Jul 31;30(2):151-8","abstract":"Analysis of an established Schizosaccharomyces pombe episomal shuttle vector suggested that inefficient transcription termination was deleterious to plasmid function. We undertook a study to determine if transcription in the presence and absence of 3'-processing within a vector could affect the ability of the plasmid to transform, transcribe and translate the RNA produced. This report provides an analysis of the effects that three S. pombe 3' non-coding regions have on the transformation and expression efficiencies of a fission yeast plasmid vector. The 3' regions from adh1, act1 and ura4 were tested for their ability to terminate and process adh1 promoter-driven transcription of a lacZ reporter gene. Differences between the 3'-processing sequences were observed, with transcription termination mediated by the ura4 3' region being more efficient than termination by the 3' regions of adh1 and act1. We show that plasmids containing inefficient transcription termination signals result in readthrough transcription and reduced transformation efficiencies. In addition, the readthrough transcripts containing 3' non-coding regions show impaired translation efficiencies. We describe an S. pombe vector (pURAS) with a high transformation efficiency that directs the production of highly translatable, discrete-sized transcripts.","authors":"Patrikakis M, Izant JG, Atkins D","authors_abbrev":"Patrikakis M et al.","pubmed_publication_date":"31 Jul 1996","pubmed_entrez_date":"1996-07-31","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24670227","title":"Structure and biological activity of 8-deoxyheronamide C from a marine-derived Streptomyces sp.: heronamides target saturated hydrocarbon chains in lipid membranes.","citation":"J Am Chem Soc 2014 Apr 09;136(14):5209-12","abstract":"Polyene macrolactams are a class of microbial metabolites, many of which show potent biological activities with unidentified modes of action. Here we report that 8-deoxyheronamide C, a new 20-membered polyene macrolactam from a marine-derived actinomycete Streptomyces sp., is a unique membrane binder. 8-Deoxyheronamide C showed a characteristic sensitivity profile against fission yeast sterol mutant cells, indicating that the metabolite targets cell membranes. We detected tight physical interaction between heronamides including 8-deoxyheronamide C and heronamide C and saturated hydrocarbon chains in lipid membranes using surface plasmon resonance experiments. We further show that heronamides induced abnormal cell wall morphology in fission yeast probably by perturbing the structure of membrane microdomains. This work will accelerate the biological and medical investigation of polyene macrolactams.","doi":"10.1021/ja500128u","authors":"Sugiyama R, Nishimura S, Matsumori N, Tsunematsu Y, Hattori A, Kakeya H","authors_abbrev":"Sugiyama R et al.","pubmed_publication_date":"09 Apr 2014","pubmed_entrez_date":"2014-03-28","publication_year":"2014","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18076567","title":"Tel2: a common partner of PIK-related kinases and a link between DNA checkpoint and nutritional response?","citation":"Genes Cells 2007 Dec;12(12):1301-4","abstract":"A recent paper (Hayashi et al. 2007) in this issue of Genes to Cells shows that the fission yeast Schizosaccharomyces pombe Tel2, a homologue of mammalian/worm CLK2/Clk-2/Rad-5, physically interacts with all the phosphoinositide 3-kinase-related kinases (PIKKs) that include Rad3/Tel1 (ATR/ATM homologues), Tor1/Tor2 (TOR kinases) and Tra1/Tra2 (TRRAP homologues), raising the possibility that Tel2 family proteins link various PIKK-related cellular processes by interacting with PIKK family proteins. In this minireview, implications and impact of the findings, and a possibility that PIKKs are functionally related through Tel2, are discussed.","authors":"Kanoh J, Yanagida M","authors_abbrev":"Kanoh J et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-12-14","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F5.11c","SPBP16F5.03c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:9251044","title":"Stress-activated protein kinase pathway in cell cycle control of fission yeast.","citation":"Methods Enzymol 1997;283:506-20","abstract":"","authors":"Shiozaki K, Russell P","authors_abbrev":"Shiozaki K et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC29B5.01"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:4716873","title":"Genes involved in mating type expression of fission yeast.","citation":"Mol Gen Genet 1973 May 28;122(4):339-43","abstract":"","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"28 May 1973","pubmed_entrez_date":"1973-05-28","publication_year":"1973","canto_session_key":"cd202708cc47017a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-18 10:38:37","canto_approved_date":"2019-11-26 19:59:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-18 10:38:30","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11H11.04","SPAC11E3.06","SPBC25B2.02c","SPCC1795.06"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2014-06-18"},{"uniquename":"PMID:18426916","title":"The anaphase-promoting complex/cyclosome controls repair and recombination by ubiquitylating Rhp54 in fission yeast.","citation":"Mol Cell Biol 2008 Jun;28(12):3905-16","abstract":"Homologous recombination (HR) is important for maintaining genome integrity and for the process of meiotic chromosome segregation and the generation of variation. HR is regulated throughout the cell cycle, being prevalent in the S and G2 phases and suppressed in the G1 phase. Here we show that the anaphase-promoting complex/cyclosome (APC/C) regulates homologous recombination in the fission yeast Schizosaccharomyces pombe by ubiquitylating Rhp54 (an ortholog of Rad54). We show that Rhp54 is a novel APC/C substrate that is destroyed in G1 phase in a KEN-box- and Ste9/Fizzy-related manner. The biological consequences of failing to temporally regulate HR via Rhp54 degradation are seen in haploid cells only in the absence of antirecombinase Srs2 function and are more extensive in diploid cells, which become sensitive to a range of DNA-damaging agents, including hydroxyurea, methyl methanesulfonate, bleomycin, and UV. During meiosis, expression of nondegradable Rhp54 inhibits interhomolog recombination and stimulates sister chromatid recombination. We thus propose that it is critical to control levels of Rhp54 in G1 to suppress HR repair of double-strand breaks and during meiosis to coordinate interhomolog recombination.","doi":"10.1128/MCB.02116-07","authors":"Trickey M, Grimaldi M, Yamano H","authors_abbrev":"Trickey M et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-23","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC15A10.03c","SPAC4H3.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7758091","title":"Smashed fission yeast walls. Structural discontinuities related to wall growth.","citation":"Cell Biophys 1995 Feb;26(1):57-75","abstract":"Twenty-three samples of fission yeast cells (Schizosaccharomyces pombe) were smashed by shaking them with glass beads. The samples represented all phases of the culture cycle, with the lag and log phases emphasized. Ruptured walls of the smashed cells were observed by phase-contrast and electron microscopy. Ruptures were tabulated with respect to their magnitudes and locations. Ruptures occurred not at random, nor at sites directed by geometry, but predominated in certain definable wall regions. These discontinuities were correlated with morphogenetic activities of the cell. Thus, the extensile end was found to be most fragile through most of the culture cycle. Also fragile was the nonextensile end, its edge more than its middle. Further, the data were applied to the testing of predictions from extant models (Johnson endohydrolytic softening model and Wessels presoftened-posthardened and crosslinking model) for hyphal tip extension. The frequency of rupture at the extensile (old) end of the cell was qualitatively predicted by both models; the frequency at the nonextensile (new) end was not predictable by either. Rupture frequencies and characteristics at other regions conformed to predictions by one or the other model, but rarely by both.","authors":"Johnson BF, Yoo BY, Calleja GB","authors_abbrev":"Johnson BF et al.","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41435824","title":"Chimeras of kinesin-6 and kinesin-14 reveal head-neck-tail domain functions and dysfunctions that lead to aneuploidy in fission yeast.","citation":"Curr Biol 2025 Dec 24;","abstract":"Kinesin motors play diverse roles in cells, including spindle assembly and chromosome segregation. Each kinesin has three general domains-the motor head, neck, and tail. As microtubule (MT) motors, kinesins have directionality, walking toward the plus or minus end of an MT. Plus-end kinesins have their motor head at the N terminus, while minus-end kinesins have their motor head at the C terminus. Interestingly, in vitro data indicate that the motor head does not dictate directionality; instead, it is the neck. Here, we seek to understand the cellular function of each kinesin domain. We systematically created chimeras of fission yeast kinesin-6 Klp9 (a plus-end kinesin localized at the spindle midzone to slide the MTs and elongate the spindle) and kinesin-14 Pkl1 (a minus-end kinesin localized at the spindle poles to focus MTs). Our in vivo data reveal that the tail dictates cellular localization, and in some cases directionality of the motor head; the motor head produces binding and sliding forces affecting spindle function; and the neck modulates the forces of the motor head. Specifically, Pkl1-head, when put on Klp9-neck-tail, walks toward the spindle midzone and slides MTs faster than the wild-type Klp9. This results in spindle breakage and aneuploidy. In contrast, Klp9-head, when put on Pkl1-neck-tail, localizes to the spindle poles but fails to properly focus MTs, leading to abnormal MT protrusions. This results in asymmetric displacement of the chromosomes and aneuploidy. Our studies reveal domain-dependent control of motor localization, direction, and force production, whose dysfunctions lead to different modes of aneuploidy.","doi":"10.1016/j.cub.2025.11.073","authors":"Sasmal P, Miyazaki M, Carlier-Grynkorn F, Tran PT","authors_abbrev":"Sasmal P et al.","pubmed_publication_date":"24 Dec 2025","pubmed_entrez_date":"2025-12-23","publication_year":"2025","canto_session_key":"438863d8dd74859d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-25 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22792081","title":"Phosphorylation-dependent interactions between Crb2 and Chk1 are essential for DNA damage checkpoint.","citation":"PLoS Genet 2012 Jul;8(7):e1002817","abstract":"In response to DNA damage, the eukaryotic genome surveillance system activates a checkpoint kinase cascade. In the fission yeast Schizosaccharomyces pombe, checkpoint protein Crb2 is essential for DNA damage-induced activation of downstream effector kinase Chk1. The mechanism by which Crb2 mediates Chk1 activation is unknown. Here, we show that Crb2 recruits Chk1 to double-strand breaks (DSBs) through a direct physical interaction. A pair of conserved SQ/TQ motifs in Crb2, which are consensus phosphorylation sites of upstream kinase Rad3, is required for Chk1 recruitment and activation. Mutating both of these motifs renders Crb2 defective in activating Chk1. Tethering Crb2 and Chk1 together can rescue the SQ/TQ mutations, suggesting that the main function of these phosphorylation sites is promoting interactions between Crb2 and Chk1. A 19-amino-acid peptide containing these SQ/TQ motifs is sufficient for Chk1 binding in vitro when one of the motifs is phosphorylated. Remarkably, the same peptide, when tethered to DSBs by fusing with either recombination protein Rad22/Rad52 or multi-functional scaffolding protein Rad4/Cut5, can rescue the checkpoint defect of crb2Δ. The Rad22 fusion can even bypass the need for Rad9-Rad1-Hus1 (9-1-1) complex in checkpoint activation. These results suggest that the main role of Crb2 and 9-1-1 in DNA damage checkpoint signaling is recruiting Chk1 to sites of DNA lesions.","doi":"10.1371/journal.pgen.1002817","authors":"Qu M, Yang B, Tao L, Yates JR, Russell P, Dong MQ, Du LL","authors_abbrev":"Qu M et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-07-14","publication_year":"2012","canto_session_key":"fb81220ce61d5104","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li-Lin Du","canto_first_approved_date":"2017-03-17 16:17:57","canto_approved_date":"2024-06-27 15:07:20","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-06-21 05:47:24","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Li-Lin Du","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c","SPBC342.05","SPAC23C4.18c","SPBC216.05","SPCC1259.13","SPAC14C4.13"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-03-17"},{"uniquename":"PMID:22510268","title":"Evidence that RNA polymerase II and not TFIIB is responsible for the difference in transcription initiation patterns between Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2012 Aug;40(14):6495-507","abstract":"The basal eukaryotic transcription machinery for protein coding genes is highly conserved from unicellular yeast to higher eukaryotes. Whereas TATA-containing promoters in human cells usually contain a single transcription start site (TSS) located ∼ 30 bp downstream of the TATA element, transcription in the yeast Schizosaccharomyces pombe and Saccharomyces cerevisiae typically initiates at multiple sites within a window ranging from 30 to 70 bp or 40 to 200 bp downstream of a TATA element, respectively. By exchanging highly purified factors between reconstituted S. pombe and S. cerevisiae transcription systems, we confirmed previous observations that the dual exchange of RNA polymerase II (RNAPII) and transcription factor IIB (TFIIB) confer the distinct initiation patterns between these yeast species. Surprisingly, however, further genetic and biochemical assays of TFIIB chimeras revealed that TFIIB and the proposed B-finger/reader domain do not play a role in determining the distinct initiation patterns between S. pombe and S. cerevisiae, but rather, these patterns are solely due to differences in RNAPII. These results are discussed within the context of a proposed model for the mechanistic coupling of the efficiency of early phosphodiester bond formation during productive TSS utilization and intrinsic elongation proficiency.","doi":"10.1093/nar/gks323","authors":"Yang C, Ponticelli AS","authors_abbrev":"Yang C et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-04-19","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12823554","title":"Functional dissection of the Schizosaccharomyces pombe Holliday junction resolvase Ydc2: in vivo role in mitochondrial DNA maintenance.","citation":"Eur J Biochem 2003 Jul;270(13):2837-47","abstract":"The crystal structure of the Schizosaccharomyces pombe Holliday junction resolvase Ydc2 revealed significant structural homology with the Escherichia coli resolvase RuvC but Ydc2 contains a small triple helical bundle that has no equivalent in RuvC. Two of the alpha-helices that form this bundle show homology to a putative DNA-binding motif known as SAP. To investigate the biochemical function of the triple-helix domain, truncated Ydc2 mutants were expressed in E. coli and in fission yeast. Although the truncated proteins retained all amino-acid residues that map to the structural core of RuvC including the catalytic site, deletion of the SAP motif alone or the whole triple-helix domain of Ydc2 resulted in the complete loss of resolvase activity and impaired significantly the binding of Ydc2 to synthetic junctions in vitro. These results are in full agreement with our proposal for a DNA-binding role of the triple-helix motif [Ceschini et al. (2001) EMBO J. 20, 6601-6611]. The biological effect of Ydc2 on mtDNA in yeast was probed using wild-type and several Ydc2 mutants expressed in Deltaydc2 S. pombe. The truncated mutants were shown to localize exclusively to yeast mitochondria ruling out a possible role of the helical bundle in mitochondrial targeting. Cells that lacked Ydc2 showed a significant depletion of mtDNA content. Plasmids expressing full-length Ydc2 but not the truncated or catalytically inactive Ydc2 mutants could rescue the mtDNA 'phenotype'. These results provide evidence that the Holliday junction resolvase activity of Ydc2 is required for mtDNA transmission and affects mtDNA content in S. pombe.","authors":"Sigala B, Tsaneva IR","authors_abbrev":"Sigala B et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-06-26","publication_year":"2003","canto_session_key":"68c407dfd4d11f5e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-17 08:00:29","canto_approved_date":"2022-07-22 13:30:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-17 08:00:21","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-17"},{"uniquename":"PMID:5092541","title":"Oxygen toxicity in a fission yeast.","citation":"J Cell Physiol 1971 Jun;77(3):363-72","abstract":"","authors":"Vaughan GL","authors_abbrev":"Vaughan GL","pubmed_publication_date":"Jun 1971","pubmed_entrez_date":"1971-06-01","publication_year":"1971","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25040903","title":"Eng2 is a component of a dynamic protein complex required for endocytic uptake in fission yeast.","citation":"Traffic 2014 Oct;15(10):1122-42","abstract":"Eng2 is a glucanase required for spore release, although it is also expressed during vegetative growth, suggesting that it might play other cellular functions. Its homology to the Saccharomyces cerevisiae Acf2 protein, previously shown to promote actin polymerization at endocytic sites in vitro, prompted us to investigate its role in endocytosis. Interestingly, depletion of Eng2 caused profound defects in endocytic uptake, which were not due to the absence of its glucanase activity. Analysis of the dynamics of endocytic proteins by fluorescence microscopy in the eng2Δ strain unveiled a previously undescribed phenotype, in which assembly of the Arp2/3 complex appeared uncoupled from the internalization of the endocytic coat and resulted in a fission defect. Strikingly also, we found that Eng2-GFP dynamics did not match the pattern of other endocytic proteins. Eng2-GFP localized to bright cytosolic spots that moved around the cellular poles and occasionally contacted assembling endocytic patches just before recruitment of Wsp1, the Schizosaccharomyces pombe WASP. Interestingly, Csh3-YFP, a WASP-interacting protein, interacted with Eng2 by co-immunoprecipitation and was recruited to Eng2 in bright cytosolic spots. Altogether, our work defines a novel endocytic functional module, which probably couples the endocytic coat to the actin module.","doi":"10.1111/tra.12198","authors":"Encinar del Dedo J, Idrissi FZ, Arnáiz-Pita Y, James M, Dueñas-Santero E, Orellana-Muñoz S, del Rey F, Sirotkin V, Geli MI, Vázquez de Aldana CR","authors_abbrev":"Encinar del Dedo J et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-07-22","publication_year":"2014","canto_session_key":"338dbe24db5aa2ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-07-23 18:08:06","canto_approved_date":"2025-12-19 15:34:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-23 18:07:59","canto_added_date":"2014-07-23 00:15:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC70.07c","SPAC767.01c","SPBC119.05c","SPBC21D10.12","SPAC17G8.04c","SPAC4F10.15c","SPAC23D3.10c","SPBC146.13c","SPAC688.11"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2019-07-23"},{"uniquename":"PMID:28841135","title":"Ubiquitination-dependent control of sexual differentiation in fission yeast.","citation":"Elife 2017 Aug 25;6","abstract":"In fission yeast, meiosis-specific transcripts are selectively eliminated during vegetative growth by the combined action of the YTH-family RNA-binding protein Mmi1 and the nuclear exosome. Upon nutritional starvation, the master regulator of meiosis Mei2 inactivates Mmi1, thereby allowing expression of the meiotic program. Here, we show that the E3 ubiquitin ligase subunit Not4/Mot2 of the evolutionarily conserved Ccr4-Not complex, which associates with Mmi1, promotes suppression of meiotic transcripts expression in mitotic cells. Our analyses suggest that Mot2 directs ubiquitination of Mei2 to preserve the activity of Mmi1 during vegetative growth. Importantly, Mot2 is not involved in the constitutive pathway of Mei2 turnover, but rather plays a regulatory role to limit its accumulation or inhibit its function. We propose that Mmi1 recruits the Ccr4-Not complex to counteract its own inhibitor Mei2, thereby locking the system in a stable state that ensures the repression of the meiotic program by Mmi1.","doi":"10.7554/eLife.28046","authors":"Simonetti F, Candelli T, Leon S, Libri D, Rougemaille M","authors_abbrev":"Simonetti F et al.","pubmed_publication_date":"25 Aug 2017","pubmed_entrez_date":"2017-08-26","publication_year":"2017","canto_session_key":"9197675c3ba9f5d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mathieu Rougemaille","canto_first_approved_date":"2018-03-02 15:13:10","canto_approved_date":"2024-04-04 09:42:15","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-02-17 12:26:52","canto_added_date":"2017-08-27 00:15:14","annotation_curators":[{"name":"Mathieu Rougemaille","community_curator":true,"annotation_count":28,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPBC29A10.02","SPBC29A10.14","SPBC4.07c","SPAC27D7.13c","SPBC2G2.09c","SPBC32H8.11","SPAC20G8.06","SPNCRNA.103","SPAC29B12.06c","SPBC725.08","SPCC18.06c","SPAC1006.03c","SPAC1B3.05","SPBC902.04","SPBC19C7.02","SPAC7D4.14c","SPCC31H12.08c","SPCC4G3.15c","SPAC16C9.04c","SPAC1F3.01","SPAC19G12.17","SPAC17H9.02","SPBC2D10.06","SPCC736.12c","SPBC337.12","SPBC216.02"],"gene_count":27,"ltp_gene_count":7,"approved_date":"2018-03-02"},{"uniquename":"PMID:22173629","title":"Investigation of the relationship between oxidative stress and glucose signaling in Schizosaccharomyces pombe.","citation":"Biochem Genet 2012 Jun;50(5-6):336-49","abstract":"The invertase mutant defective in the glucose signaling pathway of Schizosaccharomyces pombe (ird11) is resistant to glucose repression. This mutant is able to consume sucrose alongside glucose and grows in glucose-containing media with a generation time close to that of the wild type. Intracellular oxidation, protein carbonyl, and reduced glutathione levels and catalase, superoxide dismutase, and glutathione peroxidase activity were investigated in ird11, to determine the relationship between oxidative stress response and glucose signaling. The expression profiles of some genes involved in regulation of glucose repression (fbp1, fructose-1,6-bis-phosphatase; hxk2, hexokinase) and stress response (atf1 and pap1 transcription factors; ctt1, catalase; sod1, Cu,Zn superoxide dismutase) were analyzed using the quantitative real-time PCR technique. Oxidative stress response in ird11 seems to be affected by glucose signaling in a manner different from that caused by glucose deprivation.","doi":"10.1007/s10528-011-9477-x","authors":"Palabiyik B, Kig C, Pekmez M, Dalyan L, Arda N, Temizkan G","authors_abbrev":"Palabiyik B et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2011-12-17","publication_year":"2012","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34006868","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-05-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24478943","title":"Pcf1, a large subunit of CAF-1, required for maintenance of checkpoint kinase Cds1 activity.","citation":"Springerplus 2014;3:30","abstract":"Highly conserved chromatin assembly factor 1 (CAF-1) is required for histone deposition onto newly synthesized DNA to maintain genome stability. This study shows that the fission yeast Pcf1, the large subunit in CAF-1, is crucial for maintaining checkpoint kinase Cds1. Chromatin recruitment of Cds1 is enhanced by Pcf1 overproduction but is attenuated by the Δpcf1 mutation. Mutation of acetylation sites in the histone H4 tail abrogates the chromatin recruitment of Pcf1, which resembles that of Cds1 as reported previously. The present results provide evidence that chromatin recruitment of Pcf1, moderated by Clr6-HDAC activity, is essential for inactivating Cds1.","doi":"10.1186/2193-1801-3-30","authors":"Kunoh T, Habu T","authors_abbrev":"Kunoh T et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-01-31","publication_year":"2014","canto_session_key":"2c03fd218529dd82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-06 16:36:25","canto_approved_date":"2023-09-13 05:46:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-31 14:26:06","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.03c","SPBC29A10.03c","SPCC18B5.11c","SPAC1834.03c","SPBC1105.12","SPBC36.05c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-04-06"},{"uniquename":"PMID:15147872","title":"Fission yeast Skp1 is required for spindle morphology and nuclear membrane segregation at anaphase.","citation":"FEBS Lett 2004 May 21;566(1-3):77-82","abstract":"Skp1 is a core component of the Skp1-Cullin-1-F-box ubiquitin ligase. Here, we show a novel role for fission yeast Skp1 in mitotic progression. Temperature-sensitive skp1-A7 mutants enter mitosis, but fail to execute anaphase. Time-lapse imaging shows that spindles in this mutant form intranuclear arch-like structures, which eventually collapse abruptly. The two spindle poles are also seen to move backward to the cell centre rather than towards the cell ends. These abnormal phenotypes appear to stem from defects in nuclear membrane segregation. Our results show that Skp1 is required for coordinated structural alterations of mitotic spindles and nuclear membranes.","authors":"Lehmann A, Toda T","authors_abbrev":"Lehmann A et al.","pubmed_publication_date":"21 May 2004","pubmed_entrez_date":"2004-05-19","publication_year":"2004","canto_session_key":"5bd37a86db70f418","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-12-04 20:38:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-12 11:04:40","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.05","SPCC338.16"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2016-10-12"},{"uniquename":"PMID:9079882","title":"Functional analysis of homologs of translation initiation factor 2gamma in yeast.","citation":"Mol Gen Genet 1997 Feb 27;253(6):711-9","abstract":"The gamma subunit of eukaryotic translation initiation factor 2 is an EF-Tu-like protein that plays an essential role in protein synthesis. We have isolated an eIF-2gamma homolog from the fission yeast Schizosaccharomyces pombe that complements a gcd11 null allele in Saccharomyces cerevisiae. GCD11 is an essential gene that encodes S. cerevisiae eIF-2gamma. Comparison among three eIF-2gamma homologs from humans, S. cerevisiae, and S. pombe, and a putative Drosophila homolog, reveals the presence of a domain N-terminal to the GTP-binding (G) domain that varies in length (relative to EF-Tu) from 12 residues in S. pombe to 89 residues in S. cerevisiae. In S. cerevisiae, these sequences are not essential for function. However, unlike a deletion, a missense mutation in this domain confers a slow growth phenotype and constitutively derepresses expression of the GCN4 transcriptional activator. The eIF-2gamma homologs also contain a partially conserved 35-37 amino acid insertion in the G domain that is absent from EF-Tu and other G proteins. Unlike the variable N-terminal domain, these residues are required for the essential function of eIF-2gamma.","authors":"Erickson FL, Harding LD, Dorris DR, Hannig EM","authors_abbrev":"Erickson FL et al.","pubmed_publication_date":"27 Feb 1997","pubmed_entrez_date":"1997-02-27","publication_year":"1997","canto_session_key":"8c93e982d786b7ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-01 12:43:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-01 12:43:39","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC17G9.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-01"},{"uniquename":"PMID:39543681","title":"Cohesin distribution alone predicts chromatin organization in yeast via conserved-current loop extrusion.","citation":"Genome Biol 2024 Nov 14;25(1):293","abstract":"Inhomogeneous patterns of chromatin-chromatin contacts within 10-100-kb-sized regions of the genome are a generic feature of chromatin spatial organization. These features, termed topologically associating domains (TADs), have led to the loop extrusion factor (LEF) model. Currently, our ability to model TADs relies on the observation that in vertebrates TAD boundaries are correlated with DNA sequences that bind CTCF, which therefore is inferred to block loop extrusion. However, although TADs feature prominently in their Hi-C maps, non-vertebrate eukaryotes either do not express CTCF or show few TAD boundaries that correlate with CTCF sites. In all of these organisms, the counterparts of CTCF remain unknown, frustrating comparisons between Hi-C data and simulations.\nTo extend the LEF model across the tree of life, here, we propose the conserved-current loop extrusion (CCLE) model that interprets loop-extruding cohesin as a nearly conserved probability current. From cohesin ChIP-seq data alone, we derive a position-dependent loop extrusion rate, allowing for a modified paradigm for loop extrusion, that goes beyond solely localized barriers to also include loop extrusion rates that vary continuously. We show that CCLE accurately predicts the TAD-scale Hi-C maps of interphase Schizosaccharomyces pombe, as well as those of meiotic and mitotic Saccharomyces cerevisiae, demonstrating its utility in organisms lacking CTCF.\nThe success of CCLE in yeasts suggests that loop extrusion by cohesin is indeed the primary mechanism underlying TADs in these systems. CCLE allows us to obtain loop extrusion parameters such as the LEF density and processivity, which compare well to independent estimates.","doi":"10.1186/s13059-024-03432-2","authors":"Yuan T, Yan H, Li KC, Surovtsev I, King MC, Mochrie SGJ","authors_abbrev":"Yuan T et al.","pubmed_publication_date":"14 Nov 2024","pubmed_entrez_date":"2024-11-15","publication_year":"2024","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2024-11-16 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39239853","title":"Fission yeast Duc1 links to ER-PM contact sites and influences PM lipid composition and cytokinetic ring anchoring.","citation":"J Cell Sci 2024 Sep 06;","abstract":"Cytokinesis is the final stage of the cell cycle that results in the physical separation of daughter cells. To accomplish cytokinesis, many organisms build an actin- and myosin-based cytokinetic ring (CR) anchored to the plasma membrane (PM). Defects in CR-PM anchoring can arise when the PM lipid, phosphatidylinositol-4,5- bisphosphate [PI(4,5)P2], is depleted. In Schizosaccharomyces pombe, reduced PM PI(4,5)P2 results in a CR that cannot maintain its medial position and slides toward one cell end, resulting in two differently sized daughter cells. S. pombe PM PI(4,5)P2 is synthesized by the PI5-kinase Its3, but what regulates this enzyme to maintain appropriate PM PI(4,5)P2 levels is not known in S. pombe. To identify Its3 regulators, we used proximity-based biotinylation and the uncharacterized protein Duc1 was specifically detected. We discovered that Duc1 decorates the PM except at the cell division site and that its unique localization pattern is dictated by binding to the ER-PM contact site proteins, Scs2 and Scs22. Our evidence suggests Duc1 also binds PI(4,5)P2 and helps enrich Its3 at the lateral PM, thereby promoting PM PI(4,5)P2 synthesis and robust CR-PM anchoring.","doi":"10.1242/jcs.262347","authors":"Willet AH, Park JS, Snider CE, Huang JJ, Chen JS, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"06 Sep 2024","pubmed_entrez_date":"2024-09-06","publication_year":"2024","canto_session_key":"8f43f684255db562","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2024-09-11 15:20:56","canto_approved_date":"2024-11-05 17:31:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-09-09 15:29:11","canto_added_date":"2024-09-06 23:25:06","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":41,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC962.01","SPCC594.01","SPAC19G12.14","SPCP31B10.06","SPAC17C9.12","SPAC19A8.02","SPCC794.08","SPBC16G5.05c","SPAPYUK71.03c","SPBC691.05c","SPAC3H5.09c","SPCPB16A4.02c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2024-09-11"},{"uniquename":"PMID:7504624","title":"Two distinct mechanisms for negative regulation of the Wee1 protein kinase.","citation":"EMBO J 1993 Sep;12(9):3427-36","abstract":"The Wee1 protein kinase negatively regulates the entry into mitosis by catalyzing the inhibitory tyrosine phosphorylation of the Cdc2 protein. To examine the potential mechanisms for Wee1 regulation during the cell cycle, we have introduced a recombinant form of the fission yeast Wee1 protein kinase into Xenopus egg extracts. We find that the Wee1 protein undergoes dramatic changes in its phosphorylation state and kinase activity during the cell cycle. The Wee1 protein oscillates between an underphosphorylated 107 kDa form during interphase and a hyperphosphorylated 170 kDa version at mitosis. The mitosis-specific hyperphosphorylation of the Wee1 protein results in a substantial reduction in its activity as a Cdc2-specific tyrosine kinase. This phosphorylation occurs in the N-terminal region of the protein that lies outside the C-terminal catalytic domain, which was recently shown to be a substrate for the fission yeast Nim1 protein kinase. These experiments demonstrate the existence of a Wee1 regulatory system, consisting of both a Wee1-inhibitory kinase and a Wee1-stimulatory phosphatase, which controls the phosphorylation of the N-terminal region of the Wee1 protein. Moreover, these findings indicate that there are apparently two potential mechanisms for negative regulation of the Wee1 protein, one involving phosphorylation of its C-terminal domain by the Nim1 protein and the other involving phosphorylation of its N-terminal region by a different kinase.","authors":"Tang Z, Coleman TR, Dunphy WG","authors_abbrev":"Tang Z et al.","pubmed_publication_date":"Sep 1993","pubmed_entrez_date":"1993-09-01","publication_year":"1993","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23497645","title":"Ndc80 Loop as a protein-protein interaction motif.","citation":"Cell Div 2013 Mar 15;8(1):2","abstract":"Our understanding of the structure and function of kinetochores has advanced dramatically over the past 10 years, yet how the plus end of spindle microtubules interacts with the kinetochore and establishes amphitelic attachment for proper sister chromatid segregation remains unresolved. However, several recent reports from different organisms have shed new light on this issue. A key player in microtubule-kinetochore interaction is the conserved Ndc80 outer kinetochore complex. In both yeast and human cells in particular, a ubiquitous internal 'loop' found in the Ndc80 molecule interrupting its C-terminal coiled-coil domain plays critical roles in protein-protein interaction, by recruiting microtubule-binding proteins to ensure proper kinetochore-microtubule attachment. In this commentary, we summarise the recent progress made and discuss the evolutionary significance of this loop's role in microtubule dynamics at the kinetochore for accurate chromosome segregation.","doi":"10.1186/1747-1028-8-2","authors":"Tang NH, Toda T","authors_abbrev":"Tang NH et al.","pubmed_publication_date":"15 Mar 2013","pubmed_entrez_date":"2013-03-19","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-07-12 15:43:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1293882","title":"Transport of malic acid in the yeast Schizosaccharomyces pombe: evidence for a proton-dicarboxylate symport.","citation":"Yeast 1992 Dec;8(12):1025-31","abstract":"The transport system for malic acid present in Schizosaccharomyces pombe cells, growing in batch culture on several carbon sources, has been studied. It was found that the dicarboxylic acid carrier of S. pombe is a proton-dicarboxylate symporter that allows uphill transport and accumulation as a function of delta pH with the following kinetic parameters at pH 5.0: Vmax = 0.1 nmol of total malic acid s-1 mg (dry weight) of cells-1 and Km = 1.0 mM total malic acid. Malic acid uptake (pH 5.0) was accompanied by disappearance of extracellular protons, the uptake rates of which followed Michaelis-Menten kinetics as a function of the acid concentration. The Km values calculated as the concentrations either of anions or of undissociated acid, at various extracellular pH values, pointed to the monoanionic form as the transported species. Furthermore, accumulated free acid suffered rapid efflux after the addition of the protonophore carbonyl cyanid m-chlorophenyl hydrazone. These results suggested that the transport system was a dicarboxylate-proton symporter. Growth of cells in a medium with glucose (up to 14%, w/v) and malic acid (1.5%, w/v) also resulted in proton-dicarboxylate activity, suggesting that the system, besides being constitutive, was still active at high glucose concentrations. The following dicarboxylic acids acted as competitive inhibitors of malic acid transport at pH 5.0: D-malic acid, succinic acid, fumaric acid, oxaloacetic acid, alpha-ketoglutaric acid, maleic acid and malonic acid. In addition, all of these dicarboxylic acids induced proton movements that followed Michaelis-Menten kinetics.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Sousa MJ, Mota M, Leão C","authors_abbrev":"Sousa MJ et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"514dd7a2a9dcca89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-03 12:59:36","canto_approved_date":"2020-01-17 19:25:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-03-25 15:50:45","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB8E5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-04-03"},{"uniquename":"PMID:18508483","title":"Centromeric chromatin in fission yeast.","citation":"Front Biosci 2008 May 01;13:3896-905","abstract":"A fundamental requirement for life is the ability of cells to divide properly and to pass on to their daughters a full complement of genetic material. The centromere of the chromosome is essential for this process, as it provides the DNA sequences on which the kinetochore (the proteinaceous structure that links centromeric DNA to the spindle microtubules) assembles to allow segregation of the chromosomes during mitosis. It has long been recognized that kinetochore assembly is subject to epigenetic control, and deciphering how centromeres promote faithful chromosome segregation provides a fascinating intellectual challenge. This challenge is made more difficult by the scale and complexity of DNA sequences in metazoan centromeres, thus much research has focused on dissecting centromere function in the single celled eukaryotic yeasts. Interestingly, in spite of similarities in the genome size of budding and fission yeasts, they seem to have adopted some striking differences in their strategy for passing on their chromosomes. Budding yeast have \"point\" centromeres, where a 125 base sequence is sufficient for mitotic propagation, whereas fission yeast centromeres are more reminiscent of the large repetitive centromeres of metazoans. In addition, the centromeric heterochromatin which coats centromeric domains of fission yeast and metazoan centromeres and is critical for their function, is largely absent from budding yeast centromeres. This review focuses on the assembly and maintenance of centromeric chromatin in the fission yeast.","authors":"Partridge JF","authors_abbrev":"Partridge JF","pubmed_publication_date":"01 May 2008","pubmed_entrez_date":"2008-05-30","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20008938","title":"Stn1-Ten1 is an Rpa2-Rpa3-like complex at telomeres.","citation":"Genes Dev 2009 Dec 15;23(24):2900-14","abstract":"In budding yeast, Cdc13, Stn1, and Ten1 form a heterotrimeric complex (CST) that is essential for telomere protection and maintenance. Previous bioinformatics analysis revealed a putative oligonucleotide/oligosaccharide-binding (OB) fold at the N terminus of Stn1 (Stn1N) that shows limited sequence similarity to the OB fold of Rpa2, a subunit of the eukaryotic ssDNA-binding protein complex replication protein A (RPA). Here we present functional and structural analyses of Stn1 and Ten1 from multiple budding and fission yeast. The crystal structure of the Candida tropicalis Stn1N complexed with Ten1 demonstrates an Rpa2N-Rpa3-like complex. In both structures, the OB folds of the two components pack against each other through interactions between two C-terminal helices. The structure of the C-terminal domain of Saccharomyces cerevisiae Stn1 (Stn1C) was found to comprise two related winged helix-turn-helix (WH) motifs, one of which is most similar to the WH motif at the C terminus of Rpa2, again supporting the notion that Stn1 resembles Rpa2. The crystal structure of the fission yeast Schizosaccharomyces pombe Stn1N-Ten1 complex exhibits a virtually identical architecture as the C. tropicalis Stn1N-Ten1. Functional analyses of the Candida albicans Stn1 and Ten1 proteins revealed critical roles for these proteins in suppressing aberrant telomerase and recombination activities at telomeres. Mutations that disrupt the Stn1-Ten1 interaction induce telomere uncapping and abolish the telomere localization of Ten1. Collectively, our structural and functional studies illustrate that, instead of being confined to budding yeast telomeres, the CST complex may represent an evolutionarily conserved RPA-like telomeric complex at the 3' overhangs that works in parallel with or instead of the well-characterized POT1-TPP1/TEBPalpha-beta complex.","doi":"10.1101/gad.1851909","authors":"Sun J, Yu EY, Yang Y, Confer LA, Sun SH, Wan K, Lue NF, Lei M","authors_abbrev":"Sun J et al.","pubmed_publication_date":"15 Dec 2009","pubmed_entrez_date":"2009-12-17","publication_year":"2009","canto_session_key":"e4434f2a5f2dde6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-16 13:02:21","canto_approved_date":"2023-02-16 13:02:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-16 13:02:13","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.12c","SPCC1393.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-02-16","pdb_entries":[{"pdb_id":"3kf6","gene_chains":[{"gene_uniquename":"SPCC1393.14","chain":"B","position":"2-102"},{"gene_uniquename":"SPBC409.12c","chain":"A","position":"2-159"}],"title":"Crystal structure of S. pombe Stn1-ten1 complex","entry_authors":"Sun J,Yu EY,Yang YT,Confer LA,Sun SH,Wan K,Lue NF,Lei M","entry_authors_abbrev":"Sun J et al.","reference_uniquename":"PMID:20008938","experimental_method":"X-ray","resolution":"1.65"}]},{"uniquename":"PMID:8088549","title":"The fission yeast Schizosaccharomyces pombe rpb6 gene encodes the common phosphorylated subunit of RNA polymerase and complements a mutation in the corresponding gene of Saccharomyces cerevisiae.","citation":"Gene 1994 Sep 15;147(1):63-9","abstract":"A single-copy gene, homologous to the RPB6 gene from Saccharomyces cerevisiae, encoding a small phosphorylated subunit common to all three forms of nuclear DNA-dependent RNA polymerase was isolated from the fission yeast Schizosaccharomyces pombe. Its cDNA copy consists of an open reading frame of 142 codons and encodes an acidic protein (predicted pI 4.1) with a M(r) of 15,730. The genomic copy of Sz. pombe rpb6 contains an intron (219 nucleotides) located at codon 92, a position which does not correspond to the single intron of the S. cerevisiae gene. The sequencing of both genomic and cDNA copies of rpb6 allowed us to determine the probable positions of the start and stop of rpb6 transcription and to identify a putative TATA box. The primary structures of the Sz. pombe and S. cerevisiae Rpb6 proteins have 60.7% identity, with the same general organization: a highly acidic N-terminal region followed by a short basic region and a C terminus featuring a putative heptad Leu repeat. The C-terminal half of the sequence is particularly well conserved and, therefore, probably contains the most important functional domain. Moreover, a heterospecific complementation test showed that rpb6 from Sz. pombe fully complements a complete deletion of its S. cerevisiae homologue.","authors":"Shpakovski GV","authors_abbrev":"Shpakovski GV","pubmed_publication_date":"15 Sep 1994","pubmed_entrez_date":"1994-09-15","publication_year":"1994","canto_session_key":"e771a4b2fd55b3cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 13:15:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 13:15:45","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1020.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:10368185","title":"Phytochelatin synthase genes from Arabidopsis and the yeast Schizosaccharomyces pombe.","citation":"Plant Cell 1999 Jun;11(6):1153-64","abstract":"Phytochelatins (PCs), a family of heavy metal-inducible peptides important in the detoxification of heavy metals, have been identified in plants and some microorganisms, including Schizosaccharomyces pombe, but not in animals. PCs are synthesized enzymatically from glutathione (GSH) by PC synthase in the presence of heavy metal ions. In Arabidopsis, the CAD1 gene, identified by using Cd-sensitive, PC-deficient cad1 mutants, has been proposed to encode PC synthase. Using a positional cloning strategy, we have isolated the CAD1 gene. Database searches identified a homologous gene in S. pombe, and a mutant with a targeted deletion of this gene was also Cd sensitive and PC deficient. Extracts of Escherichia coli cells expressing a CAD1 cDNA or the S. pombe gene catalyzing GSH-dependent, heavy metal-activated synthesis of PCs in vitro demonstrated that both genes encode PC synthase activity. Both enzymes were activated by a range of metal ions. In contrast, reverse transcription-polymerase chain reaction experiments showed that expression of the CAD1 mRNA is not influenced by the presence of Cd. A comparison of the two predicted amino acid sequences revealed a highly conserved N-terminal region, which is presumed to be the catalytic domain, and a variable C-terminal region containing multiple Cys residues, which is proposed to be involved in activation of the enzyme by metal ions. Interestingly, a similar gene was identified in the nematode, Caenorhabditis elegans, suggesting that PCs may also be expressed in some animal species.","authors":"Ha SB, Smith AP, Howden R, Dietrich WM, Bugg S, O'Connell MJ, Goldsbrough PB, Cobbett CS","authors_abbrev":"Ha SB et al.","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-06-15","publication_year":"1999","canto_session_key":"f8be2979bdfda749","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-21 14:44:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-10 15:57:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H1.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-10"},{"uniquename":"PMID:9752725","title":"Control of meiotic recombination in Schizosaccharomyces pombe.","citation":"Prog Nucleic Acid Res Mol Biol 1998;61:345-78","abstract":"Homologous recombination occurs at high frequency during meiosis and is essential for the proper segregation of chromosomes and the generation of genetic diversity. Meiotic recombination is controlled in numerous ways. In the fission yeast Schizosaccharomyces pombe nutritional starvation induces meiosis and high-level expression of many genes, including numerous recombination (rec) genes, whose products are required for recombination. Accompanying the two meiotic divisions are profound changes in nuclear and chromosomal structure and movement, which may play an important role in meiotic recombination. Although recombination occurs throughout the genome, it occurs at high frequency in some intervals (hotspots) and at low frequency in others (coldspots). The well-characterized hotspot M26 is activated by the Mts1/Mts2 protein; this site and its binding proteins interact with the local chromosomal structure to enhance recombination. A coldspot between the silent mating-type loci is repressed by identified proteins, which may also alter local chromatin. We discuss in detail the rec genes and the possible functions of their products, some but not all of which share homology with other identified proteins. Although some of the rec gene products are required for recombination throughout the genome, others demonstrate regional specificity and are required in certain genomic regions but not in others. Throughout the review contrasts are made with meiotic recombination in the more thoroughly studied budding yeast Saccharomyces cerevisiae.","authors":"Fox ME, Smith GR","authors_abbrev":"Fox ME et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-09-30","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21343700","title":"Subtle interactions between heterochromatin and DNA replication timing.","citation":"Cell Cycle 2011 Mar 15;10(6):873-8","abstract":"","authors":"Huberman JA","authors_abbrev":"Huberman JA","pubmed_publication_date":"15 Mar 2011","pubmed_entrez_date":"2011-02-24","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1827691","title":"G1-specific cyclins: in search of an S-phase-promoting factor.","citation":"Trends Genet 1991 Mar;7(3):95-9","abstract":"In budding yeast, Saccharomyces cerevisiae, the two principal cell cycle transitions, from G1 to S phase and from G2 to M phase, are controlled by the same protein from G2 to M phase, are controlled by the same protein kinase, CDC28, a homolog of the cdc2 protein kinase in fission yeast and other organisms. The G1 to S phase activity of the kinase is associated with accumulation of a novel family of G1 cyclins, distinct from cyclins that are required to activate the kinase for G2 to M phase functions. It remains to be determined whether G1 cyclins with similar functions exist in higher cells.","authors":"Reed SI","authors_abbrev":"Reed SI","pubmed_publication_date":"Mar 1991","pubmed_entrez_date":"1991-03-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15341759","title":"Microtubule dynamics: faint speckle, hidden dragon.","citation":"Curr Biol 2004 Sep 07;14(17):R702-4","abstract":"The results of recent experiments in budding and fission yeast show that there is a diversity of mechanisms for targeting proteins to the plus ends of microtubules in eukaryotic cells.","authors":"Sawin KE","authors_abbrev":"Sawin KE","pubmed_publication_date":"07 Sep 2004","pubmed_entrez_date":"2004-09-03","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4417303","title":"Dark repair inhibitors and pathways for repair of radiation damage in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1974;132(1):13-22","abstract":"","authors":"Nasim A, Smith BP","authors_abbrev":"Nasim A et al.","pubmed_publication_date":"1974","pubmed_entrez_date":"1974-01-01","publication_year":"1974","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC06182","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36784258","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-02-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36509793","title":"Functional crosstalk between the cohesin loader and chromatin remodelers.","citation":"Nat Commun 2022 Dec 13;13(1):7698","abstract":"The cohesin complex participates in many structural and functional aspects of genome organization. Cohesin recruitment onto chromosomes requires nucleosome-free DNA and the Scc2-Scc4 cohesin loader complex that catalyzes topological cohesin loading. Additionally, the cohesin loader facilitates promoter nucleosome clearance in a yet unknown way, and it recognizes chromatin receptors such as the RSC chromatin remodeler. Here, we explore the cohesin loader-RSC interaction. Amongst multi-pronged contacts by Scc2 and Scc4, we find that Scc4 contacts a conserved patch on the RSC ATPase motor module. The cohesin loader directly stimulates in vitro nucleosome sliding by RSC, providing an explanation how it facilitates promoter nucleosome clearance. Furthermore, we observe cohesin loader interactions with a wide range of chromatin remodelers. Our results provide mechanistic insight into how the cohesin loader recognizes, as well as influences, the chromatin landscape, with implications for our understanding of human developmental disorders including Cornelia de Lange and Coffin-Siris syndromes.","doi":"10.1038/s41467-022-35444-6","authors":"Muñoz S, Jones A, Bouchoux C, Gilmore T, Patel H, Uhlmann F","authors_abbrev":"Muñoz S et al.","pubmed_publication_date":"13 Dec 2022","pubmed_entrez_date":"2022-12-12","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.01","SPAC1687.18c","SPAC1250.01","SPCC1620.14c","SPAC29B12.01","SPAC1783.05"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"EMBL:AU006556","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18201975","title":"Characterization of Thi9, a novel thiamine (Vitamin B1) transporter from Schizosaccharomyces pombe.","citation":"J Biol Chem 2008 Mar 21;283(12):7379-89","abstract":"Thiamine is an essential component of the human diet and thiamine diphosphate-dependent enzymes play an important role in carbohydrate metabolism in all living cells. Although the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe can derive thiamine from biosynthesis, both are also able to take up thiamine from external sources, leading to the down-regulation of the enzymes involved in its formation. We have isolated the S. pombe thiamine transporter Thi9 by genetic complementation of mutants defective in thiamine biosynthesis and transport. Thi9 localizes to the S. pombe cell surface and works as a high-affinity proton/thiamine symporter. The uptake of thiamine was reduced in the presence of pyrithiamine, oxythiamine, amprolium, and the thiazole part of thiamine, indicating that these compounds are substrates of Thi9. In pyrithiamine-resistant mutants, a conserved glutamate residue close to the first of the 12 transmembrane domains is exchanged by a lysine and this causes aberrant localization of the protein. Thiamine uptake is significantly increased in thiamine-deficient medium and this is associated with an increase in thi9(+) mRNA and protein levels. Upon addition of thiamine, the thi9(+) mRNA becomes undetectable within minutes, whereas the Thi9 protein appears to be stable. The protein is distantly related to transporters for amino acids, gamma-aminobutyric acid and polyamines, and not to any of the known thiamine transporters. We also found that the pyridoxine transporter Bsu1 has a marked contribution to the thiamine uptake activity of S. pombe cells.","doi":"10.1074/jbc.M708275200","authors":"Vogl C, Klein CM, Batke AF, Schweingruber ME, Stolz J","authors_abbrev":"Vogl C et al.","pubmed_publication_date":"21 Mar 2008","pubmed_entrez_date":"2008-01-19","publication_year":"2008","canto_session_key":"7af453947f7b7e9d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-08-28 14:03:46","canto_approved_date":"2023-09-08 09:09:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 15:44:21","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9.10","SPAC17A2.01","SPBC26H8.01","SPAC19D5.04"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-08-28"},{"uniquename":"PMID:7917418","title":"The role of glutathione biosynthesis in heavy metal resistance in the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Microbiol Rev 1994 Aug;14(4):303-8","abstract":"Plants and the fission yeast Schizosaccharomyces pombe synthesize small cadmium-binding peptides, called phytochelatins, in response to cadmium. Derived from glutathione (GSH: gamma-Glu-Cys-Gly), they have the general structure (gamma-Glu-Cys)nGly, where n is 2-11. In order to study the biosynthesis of phytochelatins, we used the mutagen N-methyl-N'-nitro-N nitrosoguanidine (MNNG) to select mutants with a lowered GSH content. GSH-deficient mutants show a Cd-sensitive phenotype, whereas resistance to Cu is only slightly influenced. These Cd-sensitive mutants contain 2-15% of the wild-type GSH level. For three mutants a lowered activity of gamma-glutamylcysteine synthetase was measured. One of the mutants was transformed to Cd-resistance and the complementing fragment was analyzed further. The complementing fragment hybridized with chromosome III. In the transformants, GSH content was restored up to wild-type levels, whereas the activity of gamma-glutamylcysteine synthetase was significantly increased compared with the wild-type. Possible mechanisms for Cd-resistance in the transformants are discussed.","authors":"Coblenz A, Wolf K","authors_abbrev":"Coblenz A et al.","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_session_key":"5307881eb46fd6f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-12-05 23:11:21","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-05 23:11:14","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-12-05"},{"uniquename":"PMID:37921038","title":"Structural insights into coordinating 5S RNP rotation with ITS2 pre-RNA processing during ribosome formation.","citation":"EMBO Rep 2023 Dec 06;24(12):e57984","abstract":"The rixosome defined in Schizosaccharomyces pombe and humans performs diverse roles in pre-ribosomal RNA processing and gene silencing. Here, we isolate and describe the conserved rixosome from Chaetomium thermophilum, which consists of two sub-modules, the sphere-like Rix1-Ipi3-Ipi1 and the butterfly-like Las1-Grc3 complex, connected by a flexible linker. The Rix1 complex of the rixosome utilizes Sda1 as landing platform on nucleoplasmic pre-60S particles to wedge between the 5S rRNA tip and L1-stalk, thereby facilitating the 180° rotation of the immature 5S RNP towards its mature conformation. Upon rixosome positioning, the other sub-module with Las1 endonuclease and Grc3 polynucleotide-kinase can reach a strategic position at the pre-60S foot to cleave and 5' phosphorylate the nearby ITS2 pre-rRNA. Finally, inward movement of the L1 stalk permits the flexible Nop53 N-terminus with its AIM motif to become positioned at the base of the L1-stalk to facilitate Mtr4 helicase-exosome participation for completing ITS2 removal. Thus, the rixosome structure elucidates the coordination of two central ribosome biogenesis events, but its role in gene silencing may adapt similar strategies.","doi":"10.15252/embr.202357984","authors":"Thoms M, Lau B, Cheng J, Fromm L, Denk T, Kellner N, Flemming D, Fischer P, Falquet L, Berninghausen O, Beckmann R, Hurt E","authors_abbrev":"Thoms M et al.","pubmed_publication_date":"06 Dec 2023","pubmed_entrez_date":"2023-11-03","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16C6.12c","SPCC830.03"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:10835386","title":"Slm9, a novel nuclear protein involved in mitotic control in fission yeast.","citation":"Genetics 2000 Jun;155(2):623-31","abstract":"In the fission yeast Schizosaccharomyces pombe, as in other eukaryotic cells, Cdc2/cyclin B complex is the key regulator of mitosis. Perhaps the most important regulation of Cdc2 is the inhibitory phosphorylation of tyrosine-15 that is catalyzed by Wee1 and Mik1. Cdc25 and Pyp3 phosphatases dephosphorylate tyrosine-15 and activate Cdc2. To isolate novel activators of Cdc2 kinase, we screened synthetic lethal mutants in a cdc25-22 background at the permissive temperature (25 degrees ). One of the genes, slm9, encodes a novel protein of 807 amino acids. Slm9 is most similar to Hir2, the histone gene regulator in budding yeast. Slm9 protein level is constant and Slm9 is localized to the nucleus throughout the cell cycle. The slm9 disruptant is delayed at the G(2)-M transition as indicated by cell elongation and analysis of DNA content. Inactivation of Wee1 fully suppressed the cell elongation phenotype caused by the slm9 mutation. The slm9 mutant is defective in recovery from G(1) arrest after nitrogen starvation. The slm9 mutant is also UV sensitive, showing a defect in recovery from the cell cycle arrest after UV irradiation.","authors":"Kanoh J, Russell P","authors_abbrev":"Kanoh J et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-06-03","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC15D4.03","SPAC57A10.02","SPAC644.06c","SPCC18B5.03"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:37340985","title":"Structural polymorphism of the PH domain in TFIIH.","citation":"Biosci Rep 2023 Jul 26;43(7)","abstract":"The general transcription factor TFIIH is a multi-subunit complex involved in transcription, DNA repair, and cell cycle in eukaryotes. In the human p62 subunit and the budding yeast Saccharomyces cerevisiae Tfb1 subunit of TFIIH, the pleckstrin homology (PH) domain (hPH/scPH) recruits TFIIH to transcription-start and DNA-damage sites by interacting with an acidic intrinsically disordered region in transcription and repair factors. Whereas metazoan PH domains are highly conserved and adopt a similar structure, fungal PH domains are divergent and only the scPH structure is available. Here, we have determined the structure of the PH domain from Tfb1 of fission yeast Schizosaccharomyces pombe (spPH) by NMR. spPH holds an architecture, including the core and external backbone structures, that is closer to hPH than to scPH despite having higher amino acid sequence identity to scPH. In addition, the predicted target-binding site of spPH shares more amino acid similarity with scPH, but spPH contains several key residues identified in hPH as required for specific binding. Using chemical shift perturbation, we have identified binding modes of spPH to spTfa1, a homologue of hTFIIEα, and to spRhp41, a homologue of the repair factors hXPC and scRad4. Both spTfa1 and spRhp41 bind to a similar but distinct surface of spPH by modes that differ from those of target proteins binding to hPH and scPH, revealing that the PH domain of TFIIH interacts with its target proteins in a polymorphic manner in Metazoa, and budding and fission yeasts.","doi":"10.1042/BSR20230846","authors":"Okuda M, Nishimura Y","authors_abbrev":"Okuda M et al.","pubmed_publication_date":"26 Jul 2023","pubmed_entrez_date":"2023-06-21","publication_year":"2023","canto_session_key":"f016e2e64dba9a36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-09-23 10:00:52","canto_approved_date":"2023-12-15 12:51:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-09-23 10:00:45","canto_added_date":"2023-06-22 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16E8.11c","SPAC458.07","SPAC12B10.12c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-09-23","pdb_entries":[{"pdb_id":"8i53","gene_chains":[{"gene_uniquename":"SPAC16E8.11c","chain":"A","position":"1-108"}],"title":"Solution structure of the PH domain from the Tfb1 subunit of fission yeast TFIIH","entry_authors":"Okuda M,Nishimura Y","entry_authors_abbrev":"Okuda M et al.","reference_uniquename":"PMID:37340985","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:17455792","title":"The fission yeast ortholog of eIF3a subunit is not functional in Saccharomyces cerevisiae.","citation":"Folia Microbiol (Praha) 2006;51(6):555-64","abstract":"The Schizosaccharomyces pombe eIF3a ortholog (SpeIF3a) was shown to be unable to substitute for S. cerevisiae eIF3a (SceIF3a) in its essential function in the initiation of translation. Overproduction of SpeIF3a altered the distribution of SceIF3a but formation of the endogenous eIF3 complex was not affected. SpeIF3a was found to be more tightly bound to S. cerevisiae ribosomes than SceIF3a and other eIF3 subunits (eIF3g, eIF3i, eIF3j). The host cells displayed aberrant morphology and altered chitin deposition. SpeIF3a probably competes with SceIF3a for binding to either ribosomes or yet to be identified substrates.","authors":"Malcová-Janatová I, Koubek Z, Malínská K, Raková R, Hasek J","authors_abbrev":"Malcová-Janatová I et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-04-26","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10625684","title":"Purification and characterization of RNA polymerase II holoenzyme from Schizosaccharomyces pombe.","citation":"J Biol Chem 2000 Jan 14;275(2):1351-6","abstract":"We have purified the RNA polymerase II holoenzyme from Schizosaccharomyces pombe to near homogeneity. The Mediator complex is considerably smaller than its counterpart in Saccharomyces cerevisiae, containing only nine polypeptides larger than 19 kDa. Five of these Mediator subunits have been identified as the S. pombe homologs to Rgr1, Srb4, Med7, and Nut2 found in S. cerevisiae and the gene product of a previously uncharacterized open reading frame, PMC2, with no clear homologies to any described protein. The presence of Mediator in a S. pombe RNA polymerase II holoenzyme stimulated phosphorylation of the C-terminal domain by TFIIH purified from S. pombe. This stimulation was species-specific, because S. pombe Mediator could not stimulate TFIIH purified from S. cerevisiae. We suggest that the overall structure and mechanism of the Mediator is evolutionary conserved. The subunit composition, however, has evolved to respond properly to physiological signals.","authors":"Spåhr H, Bève J, Larsson T, Bergström J, Karlsson KA, Gustafsson CM","authors_abbrev":"Spåhr H et al.","pubmed_publication_date":"14 Jan 2000","pubmed_entrez_date":"2000-01-08","publication_year":"2000","canto_session_key":"49e56c53ef24f960","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-10-07 17:06:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-08 18:05:29","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5D6.05","SPBC21.04","SPBC31F10.04c","SPAC23C4.15","SPAC2F7.04","SPBC19F8.07","SPAC29A4.07","SPAC23G3.01","SPBC12D12.06","SPAC1002.15c","SPACUNK4.06c","SPBC31F10.09c","SPCC1020.04c","SPAC17C9.05c","SPBC1105.06","SPBC14F5.08","SPAC23H4.17c","SPBC28F2.12","SPCC1442.10c","SPBC1604.10"],"gene_count":20,"ltp_gene_count":17,"approved_date":"2016-09-08"},{"uniquename":"PMID:31514053","title":"Identification of ubiquitin-proteasome system components affecting the degradation of the transcription factor Pap1.","citation":"Redox Biol 2020 Jan;28:101305","abstract":"Signaling cascades respond to specific inputs, but also require active interventions to be maintained in their basal/inactive levels in the absence of the activating signal(s). In a screen to search for protein quality control components required for wild-type tolerance to oxidative stress in fission yeast, we have isolated eight gene deletions conferring resistance not only to H 2 O 2  but also to caffeine. We show that dual resistance acquisition is totally or partially dependent on the transcription factor Pap1. Some gene products, such as the ribosomal-ubiquitin fusion protein Ubi1, the E2 conjugating enzyme Ubc2 or the E3 ligase Ubr1, participate in basal ubiquitin labeling of Pap1, and others, such as Rpt4, are non-essential constituents of the proteasome. We demonstrate here that basal nucleo-cytoplasmic shuttling of Pap1, occurring even in the absence of stress, is sufficient for the interaction of the transcription factor with nuclear Ubr1, and we identify a 30 amino acids peptide in Pap1 as the degron for this important E3 ligase. The isolated gene deletions increase only moderately the concentration of the transcription factor, but it is sufficient to enhance basal tolerance to stress, probably by disturbing the inactive stage of this signaling cascade.","doi":"10.1016/j.redox.2019.101305","authors":"Marte L, Boronat S, García-Santamarina S, Ayté J, Kitamura K, Hidalgo E","authors_abbrev":"Marte L et al.","pubmed_publication_date":"Jan 2020","pubmed_entrez_date":"2019-09-13","publication_year":"2020","canto_session_key":"124cd3035fe6a6d4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-09-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPBC19C7.02"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:36327116","title":"Experimental and Computational Studies on the Biotransformation of Pseudopyronines with Human Cytochrome P450 CYP4F2.","citation":"J Nat Prod 2022 Nov 25;85(11):2603-2609","abstract":"The secondary metabolite pseudopyronine B, isolated from  Pseudomonas   mosselii  P33, was biotransformed by human P450 enzymes, heterologously expressed in the fission yeast  Schizosaccharomyces pombe . Small-scale studies confirmed that both CYP4F2 and CYP4F3A were capable of oxidizing the substrate, with the former achieving a higher yield. In larger-scale studies using CYP4F2, three new oxidation products were obtained, the structures of which were elucidated by UV-vis, 1D and 2D NMR, and HR-MS spectroscopy. These corresponded to hydroxylated, carboxylated, and ester derivatives ( 1 - 3 ) of pseudopyronine B, all of which had been oxidized exclusively at the ω-position of the C-6 alkyl chain.  In silico  homology modeling experiments highlighted key interactions between oxygen atoms of the pyrone ring and two serine residues and a histidine residue of CYP4F2, which hold the substrate in a suitable orientation for oxidation at the terminus of the C-6 alkyl chain. Additional modeling studies with all three pseudopyronines revealed that the seven-carbon alkyl chain of pseudopyronine B was the perfect length for oxidation, with the terminal carbon lying close to the heme iron. The antibacterial activity of the substrates and three oxidation products was also assessed, revealing that oxidation at the ω-position removes all antimicrobial activity. This study both increases the range of known substrates for human CYF4F2 and CYP4F3A enzymes and demonstrates their utility in producing additional natural product derivatives.","doi":"10.1021/acs.jnatprod.2c00616","authors":"Lu Y, Liu X, Lotfy R, Liu S, Tesfa AF, Wolber G, Bureik M, Clark BR","authors_abbrev":"Lu Y et al.","pubmed_publication_date":"25 Nov 2022","pubmed_entrez_date":"2022-11-03","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-11-05 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19120452","title":"Coq10, a mitochondrial coenzyme Q binding protein, is required for proper respiration in Schizosaccharomyces pombe.","citation":"FEBS J 2009 Feb;276(3):748-59","abstract":"It has been widely accepted that most coenzyme Q (CoQ) exists freely in the mitochondrial membrane as a CoQ pool. However, the recent identification of a mitochondrial CoQ-binding protein, termed Coq10, in budding yeast has the potential to change our current view of CoQ status in membranes. Here, we studied the counterpart of budding yeast Coq10 (also termed Coq10) in fission yeast. Fission yeast coq10 null mutants exhibited a similar, but less severe, phenotype to CoQ-deficient fission yeast, including the requirement for antioxidants for proper growth on minimal medium, increased sensitivity to H(2)O(2), high levels of H(2)S production, and a deficiency in respiration. The coq10 null mutant produced nearly normal levels of CoQ10, suggesting that coq10 does not belong to the group of CoQ biosynthetic genes. To elucidate the role of Coq10, we expressed recombinant coq10 in Escherichia coli, and found that CoQ8 was present in purified recombinant Coq10. Mutational analysis of 13 conserved residues of Coq10 revealed that two hydrophobic amino acid residues, leucine 63 (L63) and tryptophan 104 (W104), play an important role in Coq10 binding to CoQ. An L63A/W104A double mutant of Coq10 exhibited lower CoQ-binding activity than either of the single mutants, and was unable to complement the coq10 deletion in fission yeast. A human Coq10 ortholog was able to functionally compensate for the absence of coq10 in fission yeast, suggesting that Coq10 is important for proper respiration in a variety of organisms.","doi":"10.1111/j.1742-4658.2008.06821.x","authors":"Cui TZ, Kawamukai M","authors_abbrev":"Cui TZ et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2009-01-06","publication_year":"2009","canto_session_key":"d1539912edaf907e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 16:32:09","canto_approved_date":"2022-06-16 07:17:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-04 09:05:59","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.18","SPCC16A11.07","SPCC191.07","SPBPJ4664.01"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-10-31"},{"uniquename":"PMID:9417919","title":"Isolation of human and fission yeast homologues of the budding yeast origin recognition complex subunit ORC5: human homologue (ORC5L) maps to 7q22.","citation":"Genomics 1997 Dec 01;46(2):294-8","abstract":"Orc5p is a subunit of the origin recognition complex in the budding yeast Saccharomyces cerevisiae, which has been shown to play a critical role in both chromosomal DNA replication and transcriptional silencing. We have cloned cDNAs from both human and fission yeast Schizosaccharomyces pombe that encode proteins homologous to the budding yeast and Drosophila Orc5p. Human Orc5p showed 35.1, 22.3, and 19.4% identity to the Drosophila, S. pombe, and S. cerevisiae Orc5p, respectively. We have localized the human ORC5 gene (ORC5L) to chromosome 7 using Southern and PCR analysis of DNA isolated from a panel of human/rodent somatic cell hybrids and mapped the gene locus to 7q22 using fluorescence in situ hybridization. We have identified a YAC clone that contains human ORC5L and maps to chromosome band 7q22.1. We have identified the S. pombe ORC5 gene and located it in a cosmid mapped on chromosome II.","authors":"Ishiai M, Dean FB, Okumura K, Abe M, Moon KY, Amin AA, Kagotani K, Taguchi H, Murakami Y, Hanaoka F, O'Donnell M, Hurwitz J, Eki T","authors_abbrev":"Ishiai M et al.","pubmed_publication_date":"01 Dec 1997","pubmed_entrez_date":"1998-01-07","publication_year":"1997","canto_session_key":"5475c87e44155c06","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-30 15:59:09","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-30 15:57:22","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-30"},{"uniquename":"PMID:41033841","title":"Structural and mechanistic insights into Dis3L2-mediated degradation of structured RNA.","citation":"RNA 2025 Oct 01;","abstract":"The RNase II/RNB family of exoribonucleases is present in all domains of life and includes three main eukaryotic members, the Dis3-like proteins (Dis3, Dis3L1, Dis3L2). At the cellular level, Dis3L2 is distinguished by the unique preference for uridylated RNA substrates and the highest efficiency in degrading double-stranded RNA. Defects in these enzymes have been linked to some types of cancers and overgrowth disorders in humans. In this work, we used the Dis3L2 protein from the model organism Schizosaccharomyces pombe (SpDis3L2) to better understand the mechanism of action of Dis3-like exoribonucleases, and to elucidate how single amino acid substitutions in these proteins can affect the biochemical properties of the enzymes, potentially contributing to the molecular basis of the related human diseases. We determined the crystal structure of SpDis3L2 bound to a U13 RNA, in which the protein displays a typical vase-like conformation, accommodating 6 nucleotides of the RNA 3'-end. Furthermore, we constructed two SpDis3L2 protein variants, harbouring single amino acid substitutions mimicking the ones already found in human patients, to test their catalytic activity in vitro. We highlight the A756R SpDis3L2 variant, which loses the ability to degrade double-stranded RNA substrates and accumulates intermediate degradation products when degrading single-stranded RNA substrates. As such, A756 seems to be a key residue responsible for the normal cellular function of Dis3L2, specifically regarding its important role in the degradation of structured RNA substrates.","doi":"10.1261/rna.080685.125","authors":"Matos RG, Garg A, Costa SM, Pereira P, Arraiano CM, Joshua-Tor L, Viegas SC","authors_abbrev":"Matos RG et al.","pubmed_publication_date":"01 Oct 2025","pubmed_entrez_date":"2025-10-01","publication_year":"2025","canto_session_key":"d6dab1402f9b8967","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-02 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2C4.07c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"9cy7","gene_chains":[{"gene_uniquename":"SPAC2C4.07c","chain":"A/B","position":"168-927"}],"title":"Structure of S.pombe Dis3L2 in complex with oligoU RNA substrate","entry_authors":"Garg A,Joshua-Tor L","entry_authors_abbrev":"Garg A et al.","reference_uniquename":"PMID:41033841","experimental_method":"X-ray","resolution":"3.52"}]},{"uniquename":"PMID:24722954","title":"Zinc'ing sensibly: controlling zinc homeostasis at the transcriptional level.","citation":"Metallomics 2014 Jul;6(7):1198-215","abstract":"Zinc-responsive transcription factors are found in all kingdoms of life and include the transcriptional activators ZntR, SczA, Zap1, bZip19, bZip23, and MTF-1, and transcriptional repressors Zur, AdcR, Loz1, and SmtB. These factors have two defining features; their activity is regulated by zinc and they all play a central role in zinc homeostasis by controlling the expression of genes that directly affect zinc levels or its availability. This review summarizes what is known about the mechanisms by which each of these factors sense changes in intracellular zinc levels and how they control zinc homeostasis through target gene regulation. Other factors that influence zinc ion sensing are also discussed.","doi":"10.1039/c4mt00064a","authors":"Choi S, Bird AJ","authors_abbrev":"Choi S et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-04-12","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-02-12 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31900332","title":"Mutational Analysis of N-Ethyl-N-Nitrosourea (ENU) in the Fission Yeast  Schizosaccharomyces pombe .","citation":"G3 (Bethesda) 2020 Mar 05;10(3):917-923","abstract":"Forward genetics in model organisms has boosted our knowledge of the genetic bases of development, aging, and human diseases. In this experimental pipeline, it is crucial to start by inducing a large number of random mutations in the genome of the model organism to search for phenotypes of interest. Many chemical mutagens are used to this end because most of them display particular reactivity properties and act differently over DNA. Here we report the use of N-ethyl-N-nitrosourea (ENU) as a mutagen in the fission yeast  Schizosaccharomyces pombe  As opposed to many other alkylating agents, ENU only induces an S   N   1-type reaction with a low  s  constant ( s  = 0.26), attacking preferentially O2 and O4 in thymine and O6 deoxyguanosine, leading to base substitutions rather than indels, which are extremely rare in its resulting mutagenic repertoire. Using ENU, we gathered a collection of 13 temperature-sensitive mutants and 80 auxotrophic mutants including two deleterious alleles of the human ortholog ATIC. Defective alleles of this gene cause AICA-ribosiduria, a severe genetic disease. In this screen, we also identified 13 aminoglycoside-resistance inactivating mutations in APH genes. Mutations reported here may be of interest for metabolism related diseases and antibiotic resistance research fields.","doi":"10.1534/g3.119.400936","authors":"Hoyos-Manchado R, Villa-Consuegra S, Berraquero M, Jiménez J, Tallada VA","authors_abbrev":"Hoyos-Manchado R et al.","pubmed_publication_date":"05 Mar 2020","pubmed_entrez_date":"2020-01-05","publication_year":"2020","canto_session_key":"a21157faa0edefaf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rafael Hoyos-Manchado","canto_first_approved_date":"2020-03-27 09:18:47","canto_approved_date":"2020-03-27 09:18:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-20 12:43:35","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Rafael Hoyos-Manchado","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCPB16A4.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-03-27"},{"uniquename":"PMID:18314720","title":"Studying mitochondria in an attractive model: Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2007;372:91-105","abstract":"The fission yeast Schizosaccharomyces pombe, widely used for studies of cell cycle control and differentiation, provides an alternative and complementary model to the budding yeast Saccharomyces cerevisiae for studies of nucleo-mitochondrial interactions. There are striking similarities between S. pombe and mammalian cells, in both their respiratory physiology and their mitochondrial genome structure. This technical review briefly lists the general and specific properties that are helpful to know when starting to use fission yeast as a model system for mitochondrial studies. In addition, advice is given for cell growth and genetic techniques, tips for disruption of genes involved in respiration are presented. and a basic differential centrifugation protocol is provided for the isolation of purified mitochondria that are suitable for diverse applications such as subfractionation and in vitro import.","doi":"10.1007/978-1-59745-365-3_7","authors":"Chiron S, Gaisne M, Guillou E, Belenguer P, Clark-Walker GD, Bonnefoy N","authors_abbrev":"Chiron S et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2008-03-05","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33786793","title":"Generation and Analysis of dsDNA Breaks for Checkpoint and Repair Studies in Fission Yeast.","citation":"Methods Mol Biol 2021;2267:191-205","abstract":"Damage to DNA elicits both checkpoint and repair responses. These are complex events that involve many genes whose products assemble at lesions and form signaling cascades to recruit additional factors and regulate the cell cycle. The fission yeast Schizosaccharomyces pombe has proven to be an excellent model to study these events, and has led gene and pathway discovery efforts. Recent progress has involved a more detailed analysis of the earliest events at lesions, particularly double-stranded DNA breaks (DSBs). Here we describe several methods for the analysis of events at DSBs, both on the DNA and the recruitment of proteins to these lesions, using S. pombe as a model. However, each of these methods is easily applicable to any experimental system with minor modifications to the protocols.","doi":"10.1007/978-1-0716-1217-0_13","authors":"Ramalingam R, O'Connell MJ","authors_abbrev":"Ramalingam R et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-03-31","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-04-02 00:15:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32554781","title":"System-wide analyses of the fission yeast poly(A) +  RNA interactome reveal insights into organization and function of RNA-protein complexes.","citation":"Genome Res 2020 Jul;30(7):1012-1026","abstract":"Large RNA-binding complexes play a central role in gene expression and orchestrate production, function, and turnover of mRNAs. The accuracy and dynamics of RNA-protein interactions within these molecular machines are essential for their function and are mediated by RNA-binding proteins (RBPs). Here, we show that fission yeast whole-cell poly(A) +  RNA-protein crosslinking data provide information on the organization of RNA-protein complexes. To evaluate the relative enrichment of cellular RBPs on poly(A) +  RNA, we combine poly(A) +  RNA interactome capture with a whole-cell extract normalization procedure. This approach yields estimates of in vivo RNA-binding activities that identify subunits within multiprotein complexes that directly contact RNA. As validation, we trace RNA interactions of different functional modules of the 3' end processing machinery and reveal additional contacts. Extending our analysis to different mutants of the RNA exosome complex, we explore how substrate channeling through the complex is affected by mutation. Our data highlight the central role of the RNA helicase Mtl1 in regulation of the complex and provide insights into how different components contribute to engagement of the complex with substrate RNA. In addition, we characterize RNA-binding activities of novel RBPs that have been recurrently detected in the RNA interactomes of multiple species. We find that many of these, including cyclophilins and thioredoxins, are substoichiometric RNA interactors in vivo. Because RBPomes show very good overall agreement between species, we propose that the RNA-binding characteristics we observe in fission yeast are likely to apply to related proteins in higher eukaryotes as well.","doi":"10.1101/gr.257006.119","authors":"Kilchert C, Kecman T, Priest E, Hester S, Aydin E, Kus K, Rossbach O, Castello A, Mohammed S, Vasiljeva L","authors_abbrev":"Kilchert C et al.","pubmed_publication_date":"Jul 2020","pubmed_entrez_date":"2020-06-20","publication_year":"2020","canto_session_key":"8314c9208c075b3d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-06-21 00:15:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35343949","title":"Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique.","citation":"J Vis Exp 2022 Mar 09;(181)","abstract":"Chromatin is a higher-order structure that packages eukaryotic DNA. Chromatin undergoes dynamic alterations according to the cell cycle phase and in response to environmental stimuli. These changes are essential for genomic integrity, epigenetic regulation, and DNA metabolic reactions such as replication, transcription, and repair. Chromatin assembly is crucial for chromatin dynamics and is catalyzed by histone chaperones. Despite extensive studies, the mechanisms by which histone chaperones enable chromatin assembly remains elusive. Moreover, the global features of nucleosomes organized by histone chaperones are poorly understood. To address these problems, this work describes a unique single-molecule imaging technique named DNA curtain, which facilitates the investigation of the molecular details of nucleosome assembly by histone chaperones. DNA curtain is a hybrid technique that combines lipid fluidity, microfluidics, and total internal reflection fluorescence microscopy (TIRFM) to provide a universal platform for real-time imaging of diverse protein-DNA interactions.Using DNA curtain, the histone chaperone function of Abo1, the Schizosaccharomyces pombe bromodomain-containing AAA+ ATPase, is investigated, and the molecular mechanism underlying histone assembly of Abo1 is revealed. DNA curtain provides a unique approach for studying chromatin dynamics.","doi":"10.3791/63501","authors":"Kang Y, Bae S, An S, Lee JY","authors_abbrev":"Kang Y et al.","pubmed_publication_date":"09 Mar 2022","pubmed_entrez_date":"2022-03-28","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-03-30 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23297345","title":"Fission yeast RecQ helicase Rqh1 is required for the maintenance of circular chromosomes.","citation":"Mol Cell Biol 2013 Mar;33(6):1175-87","abstract":"Protection of telomeres protein 1 (Pot1) binds to single-stranded telomere overhangs and protects chromosome ends. RecQ helicases regulate homologous recombination at multiple stages, including resection, strand displacement, and resolution. Fission yeast pot1 and RecQ helicase rqh1 double mutants are synthetically lethal, but the mechanism is not fully understood. Here, we show that the synthetic lethality of pot1Δ rqh1Δ double mutants is due to inappropriate homologous recombination, as it is suppressed by the deletion of rad51(+). The expression of Rad51 in the pot1Δ rqh1Δ rad51Δ triple mutant, which has circular chromosomes, is lethal. Reduction of the expression of Rqh1 in a pot1 disruptant with circular chromosomes caused chromosome missegregation, and this defect was partially suppressed by the deletion of rad51(+). Taken together, our results suggest that Rqh1 is required for the maintenance of circular chromosomes when homologous recombination is active. Crossovers between circular monomeric chromosomes generate dimers that cannot segregate properly in Escherichia coli. We propose that Rqh1 inhibits crossovers between circular monomeric chromosomes to suppress the generation of circular dimers.","doi":"10.1128/MCB.01713-12","authors":"Nanbu T, Takahashi K, Murray JM, Hirata N, Ukimori S, Kanke M, Masukata H, Yukawa M, Tsuchiya E, Ueno M","authors_abbrev":"Nanbu T et al.","pubmed_publication_date":"Mar 2013","pubmed_entrez_date":"2013-01-09","publication_year":"2013","canto_session_key":"f121e43e3c51f6e7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20H4.07","SPBC29A10.05","SPAC26H5.06","SPAC2G11.12","SPAC644.14c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:23173672","title":"Identification of novel genes involved in DNA damage response by screening a genome-wide Schizosaccharomyces pombe deletion library.","citation":"BMC Genomics 2012 Nov 23;13:662","abstract":"DNA damage response (DDR) plays pivotal roles in maintaining genome integrity and stability. An effective DDR requires the involvement of hundreds of genes that compose a complicated network. Because DDR is highly conserved in evolution, studies in lower eukaryotes can provide valuable information to elucidate the mechanism in higher organisms. Fission yeast (Schizosaccharomyces pombe) has emerged as an excellent model for DDR research in recent years. To identify novel genes involved in DDR, we screened a genome-wide S. pombe haploid deletion library against six different DNA damage reagents. The library covered 90.5% of the nonessential genes of S. pombe.\nWe have identified 52 genes that were actively involved in DDR. Among the 52 genes, 20 genes were linked to DDR for the first time. Flow cytometry analysis of the repair defective mutants revealed that most of them exhibited a defect in cell cycle progression, and some caused genome instability. Microarray analysis and genetic complementation assays were carried out to characterize 6 of the novel DDR genes in more detail. Data suggested that SPBC2A9.02 and SPAC27D7.08c were required for efficient DNA replication initiation because they interacted genetically with DNA replication initiation proteins Abp1 and Abp2. In addition, deletion of sgf73+, meu29+, sec65+ or pab1+ caused improper cytokinesis and DNA re-replication, which contributed to the diploidization in the mutants.\nA genome-wide screen of genes involved in DDR emphasized the key role of cell cycle control in the DDR network. Characterization of novel genes identified in the screen helps to elucidate the mechanism of the DDR network and provides valuable clues for understanding genome stability in higher eukaryotes.","doi":"10.1186/1471-2164-13-662","authors":"Pan X, Lei B, Zhou N, Feng B, Yao W, Zhao X, Yu Y, Lu H","authors_abbrev":"Pan X et al.","pubmed_publication_date":"23 Nov 2012","pubmed_entrez_date":"2012-11-24","publication_year":"2012","canto_session_key":"0d0cc4c77c2f062b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-20 12:00:08","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-03-06 16:28:15","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":704,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_23173672_phaf.tsv"}],"genes":["SPAC1952.07","SPCC794.01c","SPBC25H2.16c","SPBC26H8.09c","SPAC1F3.09","SPACUNK4.16c","SPCC1259.08","SPCC338.16","SPBPJ4664.06","SPBC428.18","SPBC1711.13","SPAC212.04c","SPAC22H12.03","SPAC2E1P3.02c","SPAC3H1.06c","SPBC8D2.17","SPAC24H6.03","SPAC6G10.11c","SPAC19G12.08","SPAPB8E5.04c","SPBC1711.04","SPBC14C8.07c","SPBC23E6.08","SPAC13A11.01c","SPBC20F10.07","SPBC409.15","SPBC2G2.08","SPAC8C9.04","SPAPB1E7.03","SPAC14C4.05c","SPBC428.08c","SPAC17G6.06","SPAC1F3.10c","SPAC6F6.01","SPBC18H10.08c","SPBC25H2.08c","SPCC11E10.04","SPBPB2B2.19c","SPAC11E3.10","SPCC1393.08","SPAC139.02c","SPAC31G5.12c","SPAC110.02","SPBC3D6.04c","SPAC212.02","SPCC1620.13","SPBC691.01","SPBC354.01","SPBC31E1.02c","SPBC1734.12c","SPBC16H5.04","SPBC16G5.03","SPAC3C7.03c","SPBC16G5.07c","SPAC3F10.17","SPBC13G1.10c","SPBP19A11.02c","SPAC869.05c","SPCC550.10","SPBC1778.03c","SPBC1685.14c","SPAC17A5.11","SPCC1919.01","SPAC18B11.10","SPAC328.01c","SPBC1198.08","SPBC21B10.10","SPAC56F8.14c","SPCC1259.11c","SPAC22H10.13","SPAC607.06c","SPCC126.12","SPAC12B10.16c","SPAC1687.14c","SPBC577.14c","SPAC821.09","SPBC1683.11c","SPAC9G1.12","SPAC186.05c","SPCC4G3.14","SPCC737.09c","SPAC57A10.09c","SPAC11G7.02","SPBP35G2.03c","SPAC16E8.09","SPAC23G3.12c","SPAC9G1.11c","SPAC1687.09","SPBC2F12.03c","SPAC823.13c","SPAC664.01c","SPAC19G12.16c","SPAC1B3.08","SPBC409.08","SPBC577.13","SPCC126.04c","SPBC1778.02","SPCC1682.08c","SPBC11B10.10c","SPAC8C9.12c","SPAC1783.01","SPCC364.01","SPBC1604.19c","SPAC19A8.11c","SPBC1711.12","SPCC74.06","SPAC24H6.13","SPAC17A2.05","SPAC20H4.09","SPBC1105.04c","SPBC215.10","SPBC3H7.09","SPAPB1A10.14","SPBC660.11","SPAPB1E7.02c","SPBC25B2.04c","SPBC13E7.04","SPCC622.08c","SPAC13A11.05","SPBP8B7.18c","SPBP8B7.13","SPBC11G11.01","SPBC342.01c","SPAC824.09c","SPAC343.15","SPBC16D10.05","SPAC3F10.07c","SPAC22A12.11","SPCC1672.03c","SPAP8A3.07c","SPAC1952.10c","SPBC2G2.05","SPBC17D1.06","SPBC4F6.12","SPBC1734.07c","SPAC688.13","SPAC29B12.14c","SPAC17G6.17","SPAC869.04","SPAC1805.06c","SPCC1753.03c","SPBC1861.07","SPAC9E9.04","SPCC553.01c","SPBC14F5.03c","SPBC660.06","SPBC530.01","SPAC1556.06","SPAC1805.05","SPBC12C2.01c","SPAC110.01","SPAC4G9.13c","SPCC622.15c","SPAC1F3.03","SPBC16C6.04","SPBC342.05","SPAC31G5.11","SPBP4H10.09","SPBC215.01","SPBC428.14","SPAC7D4.02c","SPAC1805.02c","SPBC215.14c","SPAC9E9.09c","SPBC1773.03c","SPAPB1A10.08","SPAC13G7.02c","SPAC15A10.06","SPAC144.04c","SPAC4A8.04","SPAC27F1.05c","SPAC12B10.11","SPAC823.05c","SPAC4F8.11","SPBC2F12.11c","SPCC4B3.03c","SPAC14C4.09","SPAC4A8.05c","SPCC1393.03","SPCC830.06","SPBC83.16c","SPAC688.14","SPAC17G8.14c","SPAC1A6.05c","SPAP8A3.12c","SPAC186.01","SPBC27B12.10c","SPAC1805.14","SPAC23C11.15","SPCPB16A4.04c","SPAC17C9.10","SPBC713.11c","SPAC8C9.03","SPBC428.10","SPBC800.05c","SPBC17F3.01c","SPAC13D6.03c","SPBC365.12c","SPAC22F3.04","SPAC17A5.07c","SPAC664.07c","SPCC63.02c","SPBC1348.02","SPBC30D10.09c","SPAC25B8.17","SPBC902.02c","SPAC3G6.01","SPAC1486.04c","SPAC22F8.04","SPAC4G8.08","SPCC364.04c","SPAC5H10.06c","SPCC1494.03","SPAC2F7.08c","SPAP8A3.04c","SPAC11D3.05","SPAC15A10.03c","SPBC146.13c","SPBC19C2.10","SPCC1393.05","SPAC1B2.04","SPBC20F10.10","SPBC3D6.06c","SPCC1840.08c","SPBC1D7.04","SPAC637.10c","SPAC25B8.18","SPBC25B2.10","SPCC613.03","SPCC663.14c","SPCPB1C11.03","SPAC26A3.01","SPAC4F8.01","SPAPB1A10.13","SPBC1105.13c","SPBC365.01","SPBC1347.02","SPAC824.02","SPCC162.12","SPBC19C7.01","SPBC1778.09","SPAC1F3.02c","SPCC1223.09","SPAC2F7.06c","SPCC895.09c","SPBC947.01","SPCC584.02","SPBC2A9.02","SPAC1610.02c","SPBC18A7.01","SPAC14C4.12c","SPBC3B9.08c","SPBC409.20c","SPCC1259.03","SPCC1020.10","SPBC30B4.06c","SPAPB24D3.04c","SPAC1527.01","SPAC1D4.02c","SPAC2F3.08","SPBC1347.07","SPAC19B12.08","SPAC25H1.03","SPAC22H12.01c","SPAC922.03","SPAC1783.06c","SPCC1682.15","SPBC1198.14c","SPAC823.09c","SPBC4B4.04","SPAC31A2.12","SPCC126.15c","SPAC27D7.08c","SPAC12G12.09","SPAC15F9.01c","SPBC530.08","SPAC19D5.03","SPBC32H8.13c","SPAC12G12.12","SPAP14E8.04","SPBC13G1.08c","SPCC417.02","SPBP8B7.09c","SPBC23G7.04c","SPBPB2B2.18","SPAC26F1.12c","SPBP8B7.11","SPAC20H4.02","SPAC2F7.10","SPBC2F12.12c","SPAC3F10.02c","SPCC338.14","SPAC27D7.05c","SPBC1861.02","SPBC21C3.02c","SPAC1093.01","SPAC1952.05","SPAC6G9.10c","SPAC23H3.15c","SPAC3A11.04","SPAC4H3.05","SPBC29A10.02","SPBC11G11.03","SPAC227.07c","SPAC25B8.13c","SPAC1687.19c","SPAC4D7.10c","SPAC1B3.16c","SPAC6G9.15c","SPBC21B10.07","SPAC1782.11","SPBC16H5.12c","SPBC1289.10c","SPAC2C4.17c","SPAC25H1.05","SPAC24C9.08","SPBC8D2.04","SPBC4B4.06","SPCC306.04c","SPAC926.07c","SPBC3E7.02c","SPAC1B3.07c","SPBC1652.01","SPCP1E11.05c","SPBC56F2.03","SPBC119.05c","SPAC22E12.11c"],"gene_count":327,"ltp_gene_count":4,"approved_date":"2014-03-06"},{"uniquename":"PMID:42286093","title":"Thermosensitivity of cellular translation restricts the growth of fission yeast at high temperatures.","citation":"Commun Biol 2026 Jun 12;","abstract":"Living organisms have thermal limits above which they are unable to operate and survive. Our previous genetic screen identified proteins that impede the high-temperature growth of fission yeast, including the RNA-binding protein Dri1 and a fission yeast-specific protein termed Rhs1. Here, we show that Dri1 and Rhs1 form a complex and physically interact with the Ccr4-Not complex, a master regulator of mRNA metabolism. Gene expression analysis revealed that the Dri1-Rhs1 and Ccr4-Not complexes negatively regulate a set of genes implicated in ribosome biogenesis (Ribi genes). Loss of the Dri1-Rhs1 complex results in the augmented expression of Ribi genes, thereby suppressing the translation defects and the growth inhibition under high-temperature conditions. The thermosensitivity of the translational processes may be a determinant of the upper limit of the growth temperature in fission yeast.","doi":"10.1038/s42003-026-10292-y","authors":"Akikusa Y, Yamaguchi A, Funahashi Y, Tan ACW, Mahayot F, Naka T, Matsuo A, Nakase Y, Izawa S, Shiozaki K, Morozumi Y","authors_abbrev":"Akikusa Y et al.","pubmed_publication_date":"12 Jun 2026","pubmed_entrez_date":"2026-06-12","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-13 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25793410","title":"Suppression of sensitivity to drugs and antibiotics by high external cation concentrations in fission yeast.","citation":"PLoS One 2015;10(3):e0119297","abstract":"Potassium ion homeostasis plays an important role in regulating membrane potential and therefore resistance to cations, antibiotics and chemotherapeutic agents in Schizosaccharomyces pombe and other yeasts. However, the precise relationship between drug resistance in S. pombe and external potassium concentrations (particularly in its natural habitats) remains unclear. S. pombe can tolerate a wide range of external potassium concentrations which in turn affect plasma membrane polarization. We thus hypothesized that high external potassium concentrations suppress the sensitivity of this yeast to various drugs.\nWe have investigated the effect of external KCl concentrations on the sensitivity of S. pombe cells to a wide range of antibiotics, antimicrobial agents and chemotherapeutic drugs. We employed survival assays, immunoblotting and microscopy for these studies.\nWe demonstrate that KCl, and to a lesser extent NaCl and RbCl can suppress the sensitivity of S. pombe to a wide range of antibiotics. Ammonium chloride and potassium hydrogen sulphate also suppressed drug sensitivity. This effect appears to depend in part on changes to membrane polarization and membrane transport proteins. Interestingly, we have found little relationship between the suppressive effect of KCl on sensitivity and the structure, polarity or solubility of the various compounds investigated.\nHigh concentrations of external potassium and other cations suppress sensitivity to a wide range of drugs in S. pombe. Potassium-rich environments may thus provide S. pombe a competitive advantage in nature. Modulating potassium ion homeostasis may sensitize pathogenic fungi to antifungal agents.","doi":"10.1371/journal.pone.0119297","authors":"Alao JP, Weber AM, Shabro A, Sunnerhagen P","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-21","publication_year":"2015","canto_session_key":"ecbfda73cbbd469b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Per Sunnerhagen","canto_first_approved_date":"2015-08-12 15:48:29","canto_approved_date":"2023-09-08 08:54:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-09-08 08:53:55","canto_added_date":"2015-03-22 01:15:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Per Sunnerhagen","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.08","SPAC3F10.02c","SPAC1639.02c","SPAC8E11.02c","SPAC29A4.16","SPBC216.05","SPCC1259.13","SPAC977.10","SPAC24B11.06c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2015-08-12"},{"uniquename":"PMID:23361460","title":"Mini-chromosome maintenance complexes form a filament to remodel DNA structure and topology.","citation":"Nucleic Acids Res 2013 Mar 01;41(5):3446-56","abstract":"Deregulation of mini-chromosome maintenance (MCM) proteins is associated with genomic instability and cancer. MCM complexes are recruited to replication origins for genome duplication. Paradoxically, MCM proteins are in excess than the number of origins and are associated with chromatin regions away from the origins during G1 and S phases. Here, we report an unusually wide left-handed filament structure for an archaeal MCM, as determined by X-ray and electron microscopy. The crystal structure reveals that an α-helix bundle formed between two neighboring subunits plays a critical role in filament formation. The filament has a remarkably strong electro-positive surface spiraling along the inner filament channel for DNA binding. We show that this MCM filament binding to DNA causes dramatic DNA topology change. This newly identified function of MCM to change DNA topology may imply a wider functional role for MCM in DNA metabolisms beyond helicase function. Finally, using yeast genetics, we show that the inter-subunit interactions, important for MCM filament formation, play a role for cell growth and survival.","doi":"10.1093/nar/gkt022","authors":"Slaymaker IM, Fu Y, Toso DB, Ranatunga N, Brewster A, Forsburg SL, Zhou ZH, Chen XS","authors_abbrev":"Slaymaker IM et al.","pubmed_publication_date":"01 Mar 2013","pubmed_entrez_date":"2013-01-31","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-01-15 18:46:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17450151","title":"Distinct roles of HDAC complexes in promoter silencing, antisense suppression and DNA damage protection.","citation":"Nat Struct Mol Biol 2007 May;14(5):372-80","abstract":"Histone acetylation is important in regulating DNA accessibility. Multifunctional Sin3 proteins bind histone deacetylases (HDACs) to assemble silencing complexes that selectively target chromatin. We show that, in fission yeast, an essential HDAC, Clr6, exists in two distinct Sin3 core complexes. Complex I contains an essential Sin3 homolog, Pst1, and other factors, and predominantly targets gene promoters. Complex II contains a nonessential Sin3 homolog, Pst2, and several conserved proteins. It preferentially targets transcribed chromosomal regions and centromere cores. Defects in complex II abrogate global protective functions of chromatin, causing increased accessibility of DNA to genotoxic agents and widespread antisense transcripts that are processed by the exosome. Notably, the two Clr6 complexes differentially repress forward and reverse centromeric repeat transcripts, suggesting that these complexes regulate transcription in heterochromatin and euchromatin in similar manners, including suppression of spurious transcripts from cryptic start sites.","authors":"Nicolas E, Yamada T, Cam HP, Fitzgerald PC, Kobayashi R, Grewal SI","authors_abbrev":"Nicolas E et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-04-24","publication_year":"2007","canto_session_key":"c6fe4aad56b8dbb9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-02-12 17:07:30","canto_approved_date":"2026-02-07 06:35:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-12 17:07:23","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":134,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.01","SPAC16C9.05","SPBC1709.11c","SPAC1783.05","SPAC25B8.02","SPAC29A4.18","SPBC2D10.17","SPBC36.05c","SPAC23C11.15","SPAC29B12.02c","SPAC23H4.12","SPBC12C2.10c","SPAC2F7.07c","SPBC6B1.07","SPBC336.07"],"gene_count":15,"ltp_gene_count":12,"approved_date":"2021-02-12"},{"uniquename":"PMID:9425081","title":"Substrate specificity of Schizosaccharomyces pombe Nth protein for products of oxidative DNA damage.","citation":"Biochemistry 1998 Jan 13;37(2):590-5","abstract":"A gene from Schizosaccharomyces pombe, which encodes a protein with a strong sequence similarity to the Nth protein of Escherichia coli, has recently been identified [Roldán-Arjona, T., Anselmino, C., and Lindahl, T. (1996) Nucleic Acids Res. 24, 3307-3312]. The functional analysis of this eukaryotic enzyme indicated that it is a homologue of E. coli Nth protein. The gene has been subcloned and the protein (Nth-Spo) purified to apparent homogeneity. We investigated the substrate specificity of this eukaryotic enzyme for modified bases in oxidatively damaged DNA, using the technique of gas chromatography/isotope-dilution mass spectrometry (GC/IDMS). DNA substrates containing up to 17 types of modified bases were prepared by gamma-irradiation or by treatment with H2O2 in the presence of Fe(III)-EDTA or Cu(II). The results revealed an efficient excision of five pyrimidine-derived lesions, 5-hydroxycytosine, thymine glycol, 5-hydroxy-6-hydrothymine, 5,6-dihydroxycytosine, and 5-hydroxyuracil. None of the other pyrimidine or purine lesions was excised. Excision was measured as a function of enzyme concentration, time, substrate concentration, and temperature. Kinetic constants were determined. Although some DNA base lesions removed by Nth-Spo protein were similar to those previously described for E. coli Nth protein, differences between substrate specificities of these two enzymes were noted.","authors":"Karahalil B, Roldán-Arjona T, Dizdaroglu M","authors_abbrev":"Karahalil B et al.","pubmed_publication_date":"13 Jan 1998","pubmed_entrez_date":"1998-02-21","publication_year":"1998","canto_session_key":"f4358a2f4c80d37e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-06 16:56:39","canto_approved_date":"2019-11-06 16:56:39","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-06 16:56:32","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-06"},{"uniquename":"PMID:26261211","title":"Widespread alternative and aberrant splicing revealed by lariat sequencing.","citation":"Nucleic Acids Res 2015 Sep 30;43(17):8488-501","abstract":"Alternative splicing is an important and ancient feature of eukaryotic gene structure, the existence of which has likely facilitated eukaryotic proteome expansions. Here, we have used intron lariat sequencing to generate a comprehensive profile of splicing events in Schizosaccharomyces pombe, amongst the simplest organisms that possess mammalian-like splice site degeneracy. We reveal an unprecedented level of alternative splicing, including alternative splice site selection for over half of all annotated introns, hundreds of novel exon-skipping events, and thousands of novel introns. Moreover, the frequency of these events is far higher than previous estimates, with alternative splice sites on average activated at ∼3% the rate of canonical sites. Although a subset of alternative sites are conserved in related species, implying functional potential, the majority are not detectably conserved. Interestingly, the rate of aberrant splicing is inversely related to expression level, with lowly expressed genes more prone to erroneous splicing. Although we validate many events with RNAseq, the proportion of alternative splicing discovered with lariat sequencing is far greater, a difference we attribute to preferential decay of aberrantly spliced transcripts. Together, these data suggest the spliceosome possesses far lower fidelity than previously appreciated, highlighting the potential contributions of alternative splicing in generating novel gene structures.","doi":"10.1093/nar/gkv763","authors":"Stepankiw N, Raghavan M, Fogarty EA, Grimson A, Pleiss JA","authors_abbrev":"Stepankiw N et al.","pubmed_publication_date":"30 Sep 2015","pubmed_entrez_date":"2015-08-12","publication_year":"2015","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2015-08-13 00:20:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2606378","title":"Peculiarities of amino acid transport in Schizosaccharomyces pombe: effects of growth medium.","citation":"Folia Microbiol (Praha) 1989;34(4):279-85","abstract":"Transport systems for amino acids in the wild-type strain of Schizosaccharomyces pombe are not constitutive. During growth on different media no transport of acidic, neutral and basic amino acids is detectable. To acquire the ability to transport amino acids, cells must be preincubated with a metabolic source of energy, such as glucose. The appearance of transport activity is associated with protein synthesis (suppression by cycloheximide) at all phases of culture growth. After such preincubation the initial rate of amino acid uptake depends on the phase of growth of the culture and on the amount of glucose in the growth medium but not on the nitrogen source used. L-Proline and 2-aminoisobutyric acid are practically not transported under any of the conditions tested.","authors":"Sychrová H, Horák J, Kotyk A","authors_abbrev":"Sychrová H et al.","pubmed_publication_date":"1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40562899","title":"Change of venue: fission-yeast cell-division cues actually initiate in the nucleus.","citation":"Nature 2025 Jun 25;","abstract":"","doi":"10.1038/d41586-025-01712-w","authors":"Kamenz J, Ferrell JE","authors_abbrev":"Kamenz J et al.","pubmed_publication_date":"25 Jun 2025","pubmed_entrez_date":"2025-06-25","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-06-26 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22150237","title":"RNA and epigenetic silencing: insight from fission yeast.","citation":"Dev Growth Differ 2012 Jan;54(1):129-41","abstract":"Post-translational modifications of histones are critical not only for local regulation of gene expression, but also for higher-order structure of the chromosome and genome organization in general. These modifications enable a preset state to be maintained over subsequent generations and thus provide an epigenetic level of regulation. Heterochromatic regions of the genome are epigenetically regulated to maintain a \"silent state\" and protein coding genes inserted into these regions are subject to the same epigenetic silencing. The fission yeast Schizosaccharomyces pombe has well characterized regions of heterochromatin and has proven to be a powerful model for elucidation of epigenetic silencing mechanisms. Research in S. pombe led to the breakthrough discovery that epigenetic silencing is not solely a chromatin-driven transcriptional repression and that RNA interference of nascent transcripts can guide epigenetic silencing and associated histone modifications. Over the last 10 years, an eloquent integration of genetic and biochemical studies have greatly propelled our understanding of major players and effector complexes for regulation of RNAi-mediated epigenetic silencing in S. pombe. Here, we review recent research related to regulation of the epigenetic state in S. pombe heterochromatin, focusing specifically on the mechanisms by which transcription and RNA processing interact with the chromatin modification machinery to maintain the epigenetically silent state.","doi":"10.1111/j.1440-169X.2011.01310.x","authors":"Goto DB, Nakayama J","authors_abbrev":"Goto DB et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2011-12-14","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8065916","title":"A new ATP-independent DNA endonuclease from Schizosaccharomyces pombe that recognizes cyclobutane pyrimidine dimers and 6-4 photoproducts.","citation":"Nucleic Acids Res 1994 Aug 11;22(15):3026-32","abstract":"We have discovered a new DNA endonuclease in the fission yeast Schizosaccharomyces pombe which recognizes cyclobutane pyrimidine dimers and (6-4) pyrimidine-pyrimidone photoproducts. S. pombe DNA endonuclease (SPDE) catalyzes a single ATP-independent incision immediately 5' to the UV photoproduct and generates termini containing 3' hydroxyl and 5' phosphoryl groups. Based on these properties, we propose that SPDE may function in a DNA repair capacity, representing the initial recognition/cleavage step of a DNA excision repair pathway.","authors":"Bowman KK, Sidik K, Smith CA, Taylor JS, Doetsch PW, Freyer GA","authors_abbrev":"Bowman KK et al.","pubmed_publication_date":"11 Aug 1994","pubmed_entrez_date":"1994-08-11","publication_year":"1994","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.09c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:29234668","title":"A genome-wide screen for FTY720-sensitive mutants reveals genes required for ROS homeostasis.","citation":"Microb Cell 2017 Nov 27;4(12):390-401","abstract":"Fingolimod hydrochloride (FTY720), a sphingosine-1-phosphate (S1P) analogue, is an approved immune modulator for the treatment of multiple sclerosis (MS). Notably, in addition to its well-known mode of action as an S1P modulator, accumulating evidence suggests that FTY720 induces apoptosis in various cancer cells via reactive oxygen species (ROS) generation. Although the involvement of multiple signaling molecules, such as JNK (Jun N-terminal kinase), Akt (alpha serine/threonine-protein kinase) and Sphk has been reported, the exact mechanisms how FTY720 induces cell growth inhibition and the functional relationship between FTY720 and these signaling pathways remain elusive. Our previous reports using the fission yeast  Schizosaccharomyces pombe  as a model system to elucidate FTY720-mediated signaling pathways revealed that FTY720 induces an increase in intracellular Ca 2+  concentrations and ROS generation, which resulted in the activation of the transcriptional responses downstream of Ca 2+ /calcineurin signaling and stress-activated MAPK signaling, respectively. Here, we performed a genome-wide screening for genes whose deletion induces FTY720-sensitive growth in  S. pombe  and identified 49 genes. These gene products are related to the biological processes involved in metabolic processes, transport, transcription, translation, chromatin organization, cytoskeleton organization and intracellular signal transduction. Notably, most of the FTY720-sensitive deletion cells exhibited NAC-remedial FTY720 sensitivities and dysregulated ROS homeostasis. Our results revealed a novel gene network involving ROS homeostasis and the possible mechanisms of the FTY720 toxicity.","doi":"10.15698/mic2017.12.601","authors":"Hagihara K, Kinoshita K, Ishida K, Hojo S, Kameoka Y, Satoh R, Takasaki T, Sugiura R","authors_abbrev":"Hagihara K et al.","pubmed_publication_date":"27 Nov 2017","pubmed_entrez_date":"2017-12-14","publication_year":"2017","canto_session_key":"b5103ffec4a18925","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-12-15 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20624911","title":"Asp1, a conserved 1/3 inositol polyphosphate kinase, regulates the dimorphic switch in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2010 Sep;30(18):4535-47","abstract":"The ability to undergo dramatic morphological changes in response to extrinsic cues is conserved in fungi. We have used the model yeast Schizosaccharomyces pombe to determine which intracellular signal regulates the dimorphic switch from the single-cell yeast form to the filamentous invasive growth form. The S. pombe Asp1 protein, a member of the conserved Vip1 1/3 inositol polyphosphate kinase family, is a key regulator of the morphological switch via the cAMP protein kinase A (PKA) pathway. Lack of a functional Asp1 kinase domain abolishes invasive growth which is monopolar, while an increase in Asp1-generated inositol pyrophosphates (PP) increases the cellular response. Remarkably, the Asp1 kinase activity encoded by the N-terminal part of the protein is regulated negatively by the C-terminal domain of Asp1, which has homology to acid histidine phosphatases. Thus, the fine tuning of the cellular response to environmental cues is modulated by the same protein. As the Saccharomyces cerevisiae Asp1 ortholog is also required for the dimorphic switch in this yeast, we propose that Vip1 family members have a general role in regulating fungal dimorphism.","doi":"10.1128/MCB.00472-10","authors":"Pöhlmann J, Fleig U","authors_abbrev":"Pöhlmann J et al.","pubmed_publication_date":"Sep 2010","pubmed_entrez_date":"2010-07-14","publication_year":"2010","canto_session_key":"f6ce93c34292522d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.03","SPAC24B11.06c","SPAC18G6.15","SPCC1672.06c","SPAC3G9.12","SPBC119.08","SPBC1604.20c","SPCC1223.06"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:26635866","title":"AnGeLi: A Tool for the Analysis of Gene Lists from Fission Yeast.","citation":"Front Genet 2015;6:330","abstract":"Genome-wide assays and screens typically result in large lists of genes or proteins. Enrichments of functional or other biological properties within such lists can provide valuable insights and testable hypotheses. To systematically detect these enrichments can be challenging and time-consuming, because relevant data to compare against query gene lists are spread over many different sources. We have developed AnGeLi (Analysis of Gene Lists), an intuitive, integrated web-tool for comprehensive and customized interrogation of gene lists from the fission yeast, Schizosaccharomyces pombe. AnGeLi searches for significant enrichments among multiple qualitative and quantitative information sources, including gene and phenotype ontologies, genetic and protein interactions, numerous features of genes, transcripts, translation, and proteins such as copy numbers, chromosomal positions, genetic diversity, RNA polymerase II and ribosome occupancy, localization, conservation, half-lives, domains, and molecular weight among others, as well as diverse sets of genes that are co-regulated or lead to the same phenotypes when mutated. AnGeLi uses robust statistics which can be tailored to specific needs. It also provides the option to upload user-defined gene sets to compare against the query list. Through an integrated data submission form, AnGeLi encourages the community to contribute additional curated gene lists to further increase the usefulness of this resource and to get the most from the ever increasing large-scale experiments. AnGeLi offers a rigorous yet flexible statistical analysis platform for rich insights into functional enrichments and biological context for query gene lists, thus providing a powerful exploratory tool through which S. pombe researchers can uncover fresh perspectives and unexpected connections from genomic data. AnGeLi is freely available at: www.bahlerlab.info/AnGeLi.","doi":"10.3389/fgene.2015.00330","authors":"Bitton DA, Schubert F, Dey S, Okoniewski M, Smith GC, Khadayate S, Pancaldi V, Wood V, Bähler J","authors_abbrev":"Bitton DA et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-12-05","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-12-06 01:18:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16371652","title":"Production of reactive oxygen species in response to replication stress and inappropriate mitosis in fission yeast.","citation":"J Cell Sci 2006 Jan 01;119(Pt 1):124-31","abstract":"Previous studies have indicated that replication stress can trigger apoptosis-like cell death, accompanied (where tested) by production of reactive oxygen species (ROS), in mammalian cells and budding yeast (Saccharomyces cerevisiae). In mammalian cells, inappropriate entry into mitosis also leads to cell death. Here, we report similar responses in fission yeast (Schizosaccharomyces pombe). We used ROS- and death-specific fluorescent stains to measure the effects of mutations in replication initiation and checkpoint genes in fission yeast on the frequencies of ROS production and cell death. We found that certain mutant alleles of each of the four tested replication initiation genes caused elevated ROS and cell death. Where tested, these effects were not enhanced by checkpoint-gene mutations. Instead, when cells competent for replication but defective in both the replication and damage checkpoints were treated with hydroxyurea, which slows replication fork movement, the frequencies of ROS production and cell death were greatly increased. This was a consequence of elevated CDK activity, which permitted inappropriate entry into mitosis. Thus, studies in fission yeast are likely to prove helpful in understanding the pathways that lead from replication stress and inappropriate mitosis to cell death in mammalian cells.","authors":"Marchetti MA, Weinberger M, Murakami Y, Burhans WC, Huberman JA","authors_abbrev":"Marchetti MA et al.","pubmed_publication_date":"01 Jan 2006","pubmed_entrez_date":"2005-12-24","publication_year":"2006","canto_session_key":"f5dc7dbed1ca7c42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-05-10 15:24:26","canto_approved_date":"2025-01-27 21:18:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-16 14:21:04","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":76,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_16371652_phaf.tsv"}],"genes":["SPCC550.13","SPAC664.07c","SPBC342.05","SPBC646.14c","SPBC216.05","SPAC1556.01c","SPCC1183.05c","SPAC2G11.12","SPAC9E9.08","SPAC4H3.05","SPAC14C4.13","SPAC13C5.07","SPBC685.09","SPCC18B5.11c","SPBC11B10.09","SPCC126.02c","SPCC1259.13","SPAC20G4.04c","SPAC1952.07","SPBC14C8.07c"],"gene_count":20,"ltp_gene_count":20,"approved_date":"2016-05-10"},{"uniquename":"PMID:15650330","title":"Differential regulation of three genes encoding glutathione S-transferases in Schizosaccharomyces pombe.","citation":"Mol Cells 2004 Dec 31;18(3):332-9","abstract":"Glutathione S-transferases (GSTs) are detoxifying enzymes that catalyze the conjugation of glutathione with a variety of reactive electrophilic compounds. Three GST genes were previously characterized in the fission yeast Schizosaccharomyces pombe. In this work, we examined the transcriptional regulation of these genes using individual GST-lacZ fusions and RT-PCR. Basal synthesis of beta-galactosidase from the GSTII-lacZ fusion was higher than from the GSTI-lacZ and GSTIII-lacZ fusion. Diethylmaleate (0.2 mM) greatly enhanced the synthesis of beta-galactosidase from the GSTII-lacZ fusion, but did not affect synthesis from the other two fusion genes. A switch to 0.3% glucose or 0.3% sucrose as sole carbon source enhanced expression from the GSTIII-lacZ fusion gene, while sodium nitroprusside (1.5 mM), tert-butylhydroquinone (0.2 mM), and L-buthionine-[S,R]-sulfoximine (0.01 mM) increased expression of the GSTII gene. The effects of these agents on GST mRNA levels were confirmed by measurements employing RT-PCR. Our results suggest that transcription of the three S. pombe GST genes is subjected to differential regulation under various stress conditions, and may be linked to their different physiological functions.","authors":"Kim HG, Kim BC, Park EH, Ahn K, Lim CJ","authors_abbrev":"Kim HG et al.","pubmed_publication_date":"31 Dec 2004","pubmed_entrez_date":"2005-01-15","publication_year":"2004","canto_session_key":"4390011118608f4c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-20 13:48:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-20 13:48:07","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC191.09c","SPCC965.07c","SPAC1783.07c","SPAC688.04c"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2014-11-20"},{"uniquename":"PMID:16252089","title":"Characterization of rec15, an early meiotic recombination gene in Schizosaccharomyces pombe.","citation":"Curr Genet 2005 Nov;48(5):323-33","abstract":"In S. pombe strains mutant for rec15 aberrant ascus morphology, reduced spore viability and severe reduction of meiotic recombination was detected. Genetic and cytological analysis identified frequent interruption of meiosis after the first division, and nondisjunction I, as the main segregation errors in the mutant. Chromosome segregation at meiosis I was not random in rec15, suggesting the presence of a backup system for correct segregation of achiasmate chromosomes. The analysis of meiotic progression in time-course experiments revealed that the major meiotic events, such as the onset of premeiotic DNA synthesis, of horse-tail nuclear movement, and of the first meiotic division occurred earlier in rec15 than in wild-type. The early onset of meiotic events is a novel observation for an early recombination mutant and implies a function of rec15 protein already at or before DNA synthesis.","authors":"Doll E, Molnar M, Hiraoka Y, Kohli J","authors_abbrev":"Doll E et al.","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-10-28","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28988770","title":"Structural Basis for a Safety-Belt Mechanism That Anchors Condensin to Chromosomes.","citation":"Cell 2017 Oct 19;171(3):588-600.e24","abstract":"Condensin protein complexes coordinate the formation of mitotic chromosomes and thereby ensure the successful segregation of replicated genomes. Insights into how condensin complexes bind to chromosomes and alter their topology are essential for understanding the molecular principles behind the large-scale chromatin rearrangements that take place during cell divisions. Here, we identify a direct DNA-binding site in the eukaryotic condensin complex, which is formed by its Ycg1 Cnd3  HEAT-repeat and Brn1 Cnd2  kleisin subunits. DNA co-crystal structures reveal a conserved, positively charged groove that accommodates the DNA double helix. A peptide loop of the kleisin subunit encircles the bound DNA and, like a safety belt, prevents its dissociation. Firm closure of the kleisin loop around DNA is essential for the association of condensin complexes with chromosomes and their DNA-stimulated ATPase activity. Our data suggest a sophisticated molecular basis for anchoring condensin complexes to chromosomes that enables the formation of large-sized chromatin loops.","doi":"10.1016/j.cell.2017.09.008","authors":"Kschonsak M, Merkel F, Bisht S, Metz J, Rybin V, Hassler M, Haering CH","authors_abbrev":"Kschonsak M et al.","pubmed_publication_date":"19 Oct 2017","pubmed_entrez_date":"2017-10-10","publication_year":"2017","canto_session_key":"21f10651018e42ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-09 07:23:37","canto_approved_date":"2023-12-30 18:16:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-09 07:23:30","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC306.03c","SPCC188.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-03-09","pdb_entries":[{"pdb_id":"5oqr","gene_chains":[{"gene_uniquename":"SPCC188.03","chain":"A/B","position":"1-823"},{"gene_uniquename":"SPCC306.03c","chain":"C/D","position":"416-544"}],"title":"Crystal structure of the S. pombe condensin Cnd3-Cnd2 subcomplex","entry_authors":"Kschonsak M,Hassler M,Haering CH","entry_authors_abbrev":"Kschonsak M et al.","reference_uniquename":"PMID:28988770","experimental_method":"X-ray","resolution":"2.61"}]},{"uniquename":"PMID:15338237","title":"Schizosaccharomyces pombe replication protein Cdc45/Sna41 requires Hsk1/Cdc7 and Rad4/Cut5 for chromatin binding.","citation":"Chromosoma 2004 Sep;113(3):145-56","abstract":"Cdc45 is a conserved protein required for firing of replication origins and processive DNA replication. We used an in situ chromatin-binding assay to determine factors required for fission yeast Cdc45p chromatin binding. Assembly of the pre-replicative complex is essential for Cdc45p chromatin binding, but pre-replicative complex assembly occurs independently of Cdc45p. Fission yeast Cdc45p associates with MCM proteins in asynchronously growing cells and cells arrested in S phase by hydroxyurea, but not in cells arrested at the G2/M transition. Both hsk1+ (the fission yeast CDC7 homologue) and rad4+/ cut5+ (the fission yeast DPB11 homologue) are required for Cdc45p chromatin binding. Cdc45p also remains chromatin-bound in mutants that fail to recover from replication arrest. In summary, Cdc45p chromatin binding requires an intact pre-replicative complex as well as signaling from both the Dbf4-dependent kinase and cyclin-dependent kinases.","authors":"Dolan WP, Sherman DA, Forsburg SL","authors_abbrev":"Dolan WP et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-09-01","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPBC211.04c","SPCC1682.02c","SPBC776.12c","SPCC16A11.17","SPBC25D12.03c","SPBC216.05","SPAC17D4.02"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:33483504","title":"Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex.","citation":"Nat Commun 2021 Jan 22;12(1):521","abstract":"The endoplasmic reticulum-mitochondria encounter structure (ERMES) complex creates contact sites between the endoplasmic reticulum and mitochondria, playing crucial roles in interorganelle communication, mitochondrial fission, mtDNA inheritance, lipid transfer, and autophagy. The mechanism regulating the number of ERMES foci within the cell remains unclear. Here, we demonstrate that the mitochondrial membrane protein Emr1 contributes to regulating the number of ERMES foci. We show that the absence of Emr1 significantly decreases the number of ERMES foci. Moreover, we find that Emr1 interacts with the ERMES core component Mdm12 and colocalizes with Mdm12 on mitochondria. Similar to ERMES mutant cells, cells lacking Emr1 display defective mitochondrial morphology and impaired mitochondrial segregation, which can be rescued by an artificial tether capable of linking the endoplasmic reticulum and mitochondria. We further demonstrate that the cytoplasmic region of Emr1 is required for regulating the number of ERMES foci. This work thus reveals a crucial regulatory protein necessary for ERMES functions and provides mechanistic insights into understanding the dynamic regulation of endoplasmic reticulum-mitochondria communication.","doi":"10.1038/s41467-020-20866-x","authors":"Rasul F, Zheng F, Dong F, He J, Liu L, Liu W, Cheema JY, Wei W, Fu C","authors_abbrev":"Rasul F et al.","pubmed_publication_date":"22 Jan 2021","pubmed_entrez_date":"2021-01-23","publication_year":"2021","canto_session_key":"e3f5a4777bcb5c84","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Wenfan","canto_first_approved_date":"2021-04-13 09:23:11","canto_approved_date":"2022-08-30 07:06:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-05 10:43:54","canto_added_date":"2021-04-05 10:19:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Wenfan","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.11c","SPAC8C9.19","SPBC28F2.06c","SPBC27B12.01c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2021-04-13"},{"uniquename":"PMID:3283148","title":"A temperature-sensitive mutation of the Schizosaccharomyces pombe gene nuc2+ that encodes a nuclear scaffold-like protein blocks spindle elongation in mitotic anaphase.","citation":"J Cell Biol 1988 Apr;106(4):1171-83","abstract":"A temperature-sensitive mutant nuc2-663 of the fission yeast Schizosaccharomyces pombe specifically blocks mitotic spindle elongation at restrictive temperature so that nuclei in arrested cells contain a short uniform spindle (approximately 3-micron long), which runs through a metaphase plate-like structure consisting of three condensed chromosomes. In the wild-type or in the mutant cells at permissive temperature, the spindle is fully extended approximately 15-micron long in anaphase. The nuc2' gene was cloned in a 2.4-kb genomic DNA fragment by transformation, and its complete nucleotide sequence was determined. Its coding region predicts a 665-residues internally repeating protein (76.250 mol wt). By immunoblots using anti-sera raised against lacZ-nuc2+ fused proteins, a polypeptide (designated p67; 67,000 mol wt) encoded by nuc2+ is detected in the wild-type S. pombe extracts; the amount of p67 is greatly increased when multi-copy or high-expression plasmids carrying the nuc2+ gene are introduced into the S. pombe cells. Cellular fractionation and Percoll gradient centrifugation combined with immunoblotting show that p67 cofractionates with nuclei and is enriched in resistant structure that is insoluble in 2 M NaCl, 25 mM lithium 3,5'-diiodosalicylate, and 1% Triton but is soluble in 8 M urea. In nuc2 mutant cells, however, soluble p76, perhaps an unprocessed precursor, accumulates in addition to insoluble p67. The role of nuc2+ gene may be to interconnect nuclear and cytoskeletal functions in chromosome separation.","authors":"Hirano T, Hiraoka Y, Yanagida M","authors_abbrev":"Hirano T et al.","pubmed_publication_date":"Apr 1988","pubmed_entrez_date":"1988-04-01","publication_year":"1988","canto_session_key":"c742ac749e3e621d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-03 17:56:49","canto_approved_date":"2026-01-29 12:17:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-18 13:40:55","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-01-03"},{"uniquename":"PMID:22279963","title":"Pap1p-dependent upregulation of thioredoxin 3 and thioredoxin reductase genes from the fission yeast under nitrosative stress.","citation":"Can J Microbiol 2012 Feb;58(2):206-11","abstract":"The thioredoxin system, consisting of thioredoxin, thioredoxin reductase, and NADPH, is involved in the response against a variety of stresses. The TRX3(+) and TrxR(+) genes encode thioredoxin 3 and thioredoxin reductase, respectively, in the fission yeast Schizosaccharomyces pombe . Their transcriptional regulations were studied using the lacZ fusion genes. Synthesis of β-galactosidase from the TRX3(+)-lacZ fusion gene was markedly enhanced by nitric-oxide-generating sodium nitroprusside in the Pap1p-positive cells but not in the Pap1p-negative cells. Similarly, synthesis of β-galactosidase from the TrxR(+)-lacZ fusion gene was upregulated by sodium nitroprusside in a Pap1p-dependent manner. Synthesis of β-galactosidase from the TRX3(+)-lacZ and TrxR(+)-lacZ fusion genes was also enhanced by S-nitrosoglutathione in the Pap1p-positive cells but not in the Pap1p-negative cells. In brief, the S. pombe genes encoding thioredoxin 3 and thioredoxin reductase are upregulated under nitrosative stress in a Pap1p-dependent manner.","doi":"10.1139/w11-125","authors":"Park MS, Kim HJ, Park AR, Ahn K, Lim HW, Lim CJ","authors_abbrev":"Park MS et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2012-01-28","publication_year":"2012","canto_session_key":"fc699487103de63a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-01 12:47:59","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-28 17:09:16","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3F6.03","SPBC577.08c","SPAC1783.07c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2014-11-28"},{"uniquename":"PMID:32909946","title":"Atg1 kinase in fission yeast is activated by Atg11-mediated dimerization and cis-autophosphorylation.","citation":"Elife 2020 Sep 10;9","abstract":"Autophagy is a proteolytic pathway that is conserved from yeasts to mammals. Atg1 kinase is essential for autophagy, but how its activity is controlled remains insufficiently understood. Here, we show that, in the fission yeast  Schizosaccharomyces pombe,  Atg1 kinase activity requires Atg11, the ortholog of mammalian FIP200/RB1CC1, but does not require Atg13, Atg17, or Atg101. Remarkably, a 62 amino acid region of Atg11 is sufficient for the autophagy function of Atg11 and for supporting the Atg1 kinase activity. This region harbors an Atg1-binding domain and a homodimerization domain. Dimerizing Atg1 is the main role of Atg11, as it can be bypassed by artificially dimerizing Atg1. In an Atg1 dimer, only one Atg1 molecule needs to be catalytically active, suggesting that Atg1 activation can be achieved through cis-autophosphorylation. We propose that mediating Atg1 oligomerization and activation may be a conserved function of Atg11/FIP200 family proteins and cis-autophosphorylation may be a general mechanism of Atg1 activation.","doi":"10.7554/eLife.58073","authors":"Pan ZQ, Shao GC, Liu XM, Chen Q, Dong MQ, Du LL","authors_abbrev":"Pan ZQ et al.","pubmed_publication_date":"10 Sep 2020","pubmed_entrez_date":"2020-09-10","publication_year":"2020","canto_session_key":"615730f8699178ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Zhao-Qian Pan","canto_first_approved_date":"2020-09-29 12:34:11","canto_approved_date":"2024-07-02 12:08:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-30 07:04:03","canto_added_date":"2020-09-13 00:15:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Zhao-Qian Pan","community_curator":true,"annotation_count":61,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC10F6.11c","SPAC4F10.07c","SPCC63.08c","SPAC7D4.04","SPAC25H1.03"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-09-29"},{"uniquename":"PMID:23254763","title":"Ght2⁺ is required for UDP-galactose synthesis from extracellular galactose by Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2013 Jun;97(11):4957-64","abstract":"Schizosaccharomyces pombe has eight hexose transporter genes, ght1 (+) to ght8 (+). Here we report that ght2 (+), which is highly expressed in the presence of glucose, is essential for UDP-galactose synthesis from extracellular galactose when cells grow on glucose. The galactosylation defect of a uge1Δ mutant defective in synthesis of UDP-galactose from glucose was suppressed in galactose-containing medium, but disruption of ght2 (+) in the uge1Δ mutant reversed suppression of the galactosylation defect. Expression of Saccharomyces cerevisiae GAL2 in uge1Δght2Δ cells suppressed the defective galactosylation phenotype in galactose-containing medium. These results indicate that galactose is transported from the medium to the cytosol in a Ght2-dependent manner, and is then converted into UDP-galactose.","doi":"10.1007/s00253-012-4637-4","authors":"Matsuzawa T, Hara F, Tanaka N, Tohda H, Takegawa K","authors_abbrev":"Matsuzawa T et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2012-12-21","publication_year":"2013","canto_session_key":"c52a25b43bc64269","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2020-02-18 12:47:08","canto_approved_date":"2020-02-18 12:47:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-07 01:11:37","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1235.14","SPBC1348.14c","SPBC4B4.08","SPCC548.07c","SPAC1F8.01","SPBC1683.08","SPBPB2B2.12c","SPCC1235.13","SPCC548.06c","SPBC365.14c","SPCC1795.03"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2020-02-18"},{"uniquename":"PMID:34805795","title":"The fission yeast FLCN/FNIP complex augments TORC1 repression or activation in response to amino acid (AA) availability.","citation":"iScience 2021 Nov 19;24(11):103338","abstract":"The target of Rapamycin complex1 (TORC1) senses and integrates several environmental signals, including amino acid (AA) availability, to regulate cell growth. Folliculin (FLCN) is a tumor suppressor (TS) protein in renal cell carcinoma, which paradoxically activates TORC1 in response to AA supplementation. Few tractable systems for modeling FLCN as a TS are available. Here, we characterize the FLCN-containing complex in  Schizosaccharomyces pombe  (called BFC) and show that BFC augments TORC1 repression and activation in response to AA starvation and supplementation, respectively. BFC co-immunoprecipitates V-ATPase, a TORC1 modulator, and regulates its activity in an AA-dependent manner. BFC genetic and proteomic networks identify the conserved peptide transmembrane transporter Ptr2 and the phosphoribosylformylglycinamidine synthase Ade3 as new AA-dependent regulators of TORC1. Overall, these data ascribe an additional repressive function to Folliculin in TORC1 regulation and reveal  S. pombe  as an excellent system for modeling the AA-dependent, FLCN-mediated repression of TORC1 in eukaryotes.","doi":"10.1016/j.isci.2021.103338","authors":"Calvo IA, Sharma S, Paulo JA, Gulka AOD, Boeszoermenyi A, Zhang J, Lombana JM, Palmieri CM, Laviolette LA, Arthanari H, Iliopoulos O, Gygi SP, Motamedi M","authors_abbrev":"Calvo IA et al.","pubmed_publication_date":"19 Nov 2021","pubmed_entrez_date":"2021-11-22","publication_year":"2021","canto_session_key":"0a4aae8859bbb8db","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mo Motamedi","canto_first_approved_date":"2022-01-18 17:59:34","canto_approved_date":"2025-02-13 16:18:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-12-21 20:01:01","canto_added_date":"2021-11-23 11:04:49","annotation_curators":[{"name":"Mo Motamedi","community_curator":true,"annotation_count":113,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9.10","SPAC15E1.04","SPAC869.11","SPAC23D3.12","SPBC1A4.02c","SPAC17G8.11c","SPAC19G12.08","SPBC36.07","SPAP7G5.06","SPAPB2B4.04c","SPBC16G5.05c","SPBC18E5.02c","SPBC19F5.04","SPBC29A3.01","SPCC790.02","SPCC1235.14","SPAC24B11.12c","SPAC1420.02c","SPAC23H4.10c","SPAC1006.05c","SPAC4D7.01c","SPBC1921.05","SPBC4.07c","SPBP4H10.11c","SPCC1739.10","SPBC8E4.01c","SPAC30C2.07","SPBC16A3.15c","SPCC330.08","SPAC11D3.15","SPBC24C6.08c","SPAC1635.01","SPAC328.07c","SPBC16D10.06","SPAC644.13c","SPAC3C7.08c","SPAC6C3.06c","SPBC13A2.04c","SPBC428.05c","SPCC1281.01","SPAC12G12.03","SPAC29A4.15","SPBC646.07c","SPBC21D10.09c","SPAC3A11.10c","SPBC405.04c","SPBC887.17","SPAP7G5.05","SPAC18G6.05c","SPAC767.01c","SPBC1539.03c","SPBC1539.09c","SPBPJ4664.04","SPBC1711.10c","SPBC146.14c","SPBC26H8.07c","SPAPB1A10.10c","SPCPB1C11.03","SPBC1683.01","SPAC1F7.07c","SPBC2G5.06c","SPAC29A4.20","SPBC354.14c","SPAC22A12.16","SPAC13G6.07c","SPBC26H8.01","SPAC13G6.11c","SPAC26H5.07c","SPAC3G9.06","SPCC548.06c","SPBC3F6.02c","SPCC31H12.07","SPAC24H6.13","SPBC359.03c","SPBC887.12","SPCC23B6.04c","SPAC3A12.14","SPAC4D7.09","SPAC6F12.10c","SPAP8A3.03","SPAC637.05c","SPAC3A11.12c","SPBC36.05c","SPAC22A12.06c","SPAC11H11.06","SPAC14C4.14","SPAC1565.07c","SPAPB8E5.03","SPBC4C3.07","SPCC663.01c","SPCC584.13","SPAC9G1.05","SPBC2A9.05c","SPCP1E11.06","SPACUNK4.16c","SPAC17A2.13c","SPAC19A8.04","SPCC970.03","SPAC16E8.07c","SPCC1620.08","SPBC1703.13c","SPBC4B4.08","SPBC839.16"],"gene_count":103,"ltp_gene_count":88,"approved_date":"2022-01-18"},{"uniquename":"PMID:651937","title":"Mutation in continuous cultures of Schizosaccharomyces pombe II. Effect of amino acid starvation on mutational response and DNA concentration.","citation":"Mutat Res 1978 May;50(2):175-80","abstract":"In agreement with the results obtained in Escherichia coli by other workers and our own previous data, the kinetics with which spontaneous mutations to resistance to the 12,13-epoxytrichothecene trichodermin accumulate in a lysine auxotroph of Schizosaccharomyces pombe are dependent upon the nutrilite used to limit the growth of the population. Under conditions of glucose-limitation mutation accumulation is proportional to generation time, while under lysine-limitation it becomes proportional to chronological time. In contrast to observations made in bacterial system, however, no significant change in the DNA content per cell is noted in slow growing cultures grown under amino acid starvation. These findings help to eliminate some of the theories put forward to explain the differential mutational responses observed under different growth limiting regimes.","authors":"McAthey P, Kilbey B","authors_abbrev":"McAthey P et al.","pubmed_publication_date":"May 1978","pubmed_entrez_date":"1978-05-01","publication_year":"1978","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5574428","title":"Influence of ethidium bromide on respiration in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1971;110(4):361-6","abstract":"","authors":"Schwab R, Sebald M, Kaudewitz F","authors_abbrev":"Schwab R et al.","pubmed_publication_date":"1971","pubmed_entrez_date":"1971-01-01","publication_year":"1971","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36226970","title":"Arginylation Regulates Cytoskeleton Organization and Cell Division and Affects Mitochondria in Fission Yeast.","citation":"Mol Cell Biol 2022 Nov 17;42(11):e0026122","abstract":"Protein arginylation mediated by arginyltransferase Ate1 is a posttranslational modification of emerging importance implicated in the regulation of mammalian embryogenesis, the cardiovascular system, tissue morphogenesis, cell migration, neurodegeneration, cancer, and aging.  Ate1  deletion results in embryonic lethality in mice but does not affect yeast viability, making yeast an ideal system to study the molecular pathways regulated by arginylation. Here, we conducted a global analysis of cytoskeleton-related arginylation-dependent phenotypes in Schizosaccharomyces pombe, a fission yeast species that shares many fundamental features of higher eukaryotic cells. Our studies revealed roles of Ate1 in cell division, cell polarization, organelle transport, and interphase cytoskeleton organization and dynamics. We also found a role of Ate1 in mitochondria morphology and maintenance. Furthermore, targeted mass spectrometry analysis of the total Sc. pombe arginylome identified a number of arginylated proteins, including those that play direct roles in these processes; lack of their arginylation may be responsible for  ate1 -knockout phenotypes. Our work outlines global biological processes potentially regulated by arginylation and paves the way to unraveling the functions of protein arginylation that are conserved at multiple levels of evolution and potentially constitute the primary role of this modification  in vivo .","doi":"10.1128/mcb.00261-22","authors":"Chen L, Kashina A","authors_abbrev":"Chen L et al.","pubmed_publication_date":"17 Nov 2022","pubmed_entrez_date":"2022-10-13","publication_year":"2022","canto_session_key":"5a416395667356e7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-10-15 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26982200","title":"HIV-1 Protease in the Fission Yeast Schizosaccharomyces pombe.","citation":"PLoS One 2016;11(3):e0151286","abstract":"HIV-1 protease (PR) is an essential viral enzyme. Its primary function is to proteolyze the viral Gag-Pol polyprotein for production of viral enzymes and structural proteins and for maturation of infectious viral particles. Increasing evidence suggests that PR cleaves host cellular proteins. However, the nature of PR-host cellular protein interactions is elusive. This study aimed to develop a fission yeast (Schizosaccharomyces pombe) model system and to examine the possible interaction of HIV-1 PR with cellular proteins and its potential impact on cell proliferation and viability.\nA fission yeast strain RE294 was created that carried a single integrated copy of the PR gene in its chromosome. The PR gene was expressed using an inducible nmt1 promoter so that PR-specific effects could be measured. HIV-1 PR from this system cleaved the same indigenous viral p6/MA protein substrate as it does in natural HIV-1 infections. HIV-1 PR expression in fission yeast cells prevented cell proliferation and induced cellular oxidative stress and changes in mitochondrial morphology that led to cell death. Both these PR activities can be prevented by a PR-specific enzymatic inhibitor, indinavir, suggesting that PR-mediated proteolytic activities and cytotoxic effects resulted from enzymatic activities of HIV-1 PR. Through genome-wide screening, a serine/threonine kinase, Hhp2, was identified that suppresses HIV-1 PR-induced protease cleavage and cell death in fission yeast and in mammalian cells, where it prevented PR-induced apoptosis and cleavage of caspase-3 and caspase-8.\nThis is the first report to show that HIV-1 protease is functional as an enzyme in fission yeast, and that it behaves in a similar manner as it does in HIV-1 infection. HIV-1 PR-induced cell death in fission yeast could potentially be used as an endpoint for mechanistic studies, and this system could be used for developing a high-throughput system for drug screenings.","doi":"10.1371/journal.pone.0151286","authors":"Benko Z, Elder RT, Li G, Liang D, Zhao RY","authors_abbrev":"Benko Z et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-03-17","publication_year":"2016","canto_session_key":"390060cdbd562862","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-13 12:48:47","canto_approved_date":"2018-03-13 12:48:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-03-13 12:48:40","canto_added_date":"2016-03-29 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-03-13"},{"uniquename":"PANTHER:PTHR12677","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:25441","SPBC1711.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21304269","title":"A homeodomain transcription factor regulates the DNA replication checkpoint in yeast.","citation":"Cell Cycle 2011 Feb 15;10(4):664-70","abstract":"Checkpoints monitor the successful completion of cell cycle processes, such as DNA replication, and also regulate the expression of cell cycle-dependent genes that are required for responses. In the model yeast Schizosaccharomyces pombe G 1/S phase-specific gene expression is regulated by the MBF (also known as DSC1) transcription factor complex and is also activated by the mammalian ATM/ATR-related Rad3 DNA replication checkpoint. Here, we show that the Yox1 homeodomain transcription factor acts to co-ordinate the expression of MBF-regulated genes during the cell division cycle. Moreover, our data suggests that Yox1 is inactivated by the Rad3 DNA replication checkpoint via phosphorylation by the conserved Cds1 checkpoint kinase. Collectively, our data has implications for understanding the mechanisms underlying the coordination of cell cycle processes in eukaryotes.","authors":"Purtill FS, Whitehall SK, Williams ES, McInerny CJ, Sharrocks AD, Morgan BA","authors_abbrev":"Purtill FS et al.","pubmed_publication_date":"15 Feb 2011","pubmed_entrez_date":"2011-02-10","publication_year":"2011","canto_session_key":"ebfa141e00e3a195","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC21B10.13c","SPBC216.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:8654972","title":"Isolation of an HSP12-homologous gene of Schizosaccharomyces pombe suppressing a temperature-sensitive mutant allele of cdc4.","citation":"Gene 1996 Jun 12;172(1):125-9","abstract":"Defects in the Schizosaccharomyces pombe (Sp) cell cycle-controlling genes prevent the cell cycle progression. Mutations in one of the late septation genes, cdc4, cause Sp cells to arrest at cytokinesis and result in an elongated cellular morphology. By functional complementation of one of the temperature-sensitive (ts) mutant alleles of cdc4, cdc4-31, with a Sp cDNA library, a novel gene, scf1, which suppresses the elongated ts phenotype of cdc4-31, was isolated. DNA sequence analysis of the cDNA revealed homology with a small heat-shock protein family, HSP12, of Saccharomyces cerevisiae (Sc). Expression of this gene is highly induced, both at 37 degrees C and in the stationary phase of cell growth. It is likely that scf1 is expressed in stress conditions such as heat-shock or nutritional limitation. The phenotypic suppression of cdc4-31 by a small HSP12 homolog, Scf1, suggests that the functional loss of cdc4, which is involved in formation of the F-actin contractile ring, can be prevented or repaired by one of the small HSP. This implies that an HSP might be involved in late cell plate formation or in stabilization of the Sp F-actin contractile ring structure.","authors":"Jang YJ, Park SK, Yoo HS","authors_abbrev":"Jang YJ et al.","pubmed_publication_date":"12 Jun 1996","pubmed_entrez_date":"1996-06-12","publication_year":"1996","canto_session_key":"bd24695e374cf6db","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-05-07 07:14:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-07 07:14:31","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP8A3.04c","SPAP8A3.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-05-07"},{"uniquename":"PMID:37250769","title":"DNA damage repair proteins across the Tree of Life.","citation":"iScience 2023 Jun 16;26(6):106778","abstract":"Genome maintenance is orchestrated by a highly regulated DNA damage response with specific DNA repair pathways. Here, we investigate the phylogenetic diversity in the recognition and repair of three well-established DNA lesions, primarily repaired by base excision repair (BER) and ribonucleotide excision repair (RER): (1) 8-oxoguanine, (2) abasic site, and (3) incorporated ribonucleotide in DNA in 11 species:  Escherichia coli, Bacillus subtilis, Halobacterium salinarum, Trypanosoma brucei, Tetrahymena thermophila, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Caenorhabditis elegans, Homo sapiens, Arabidopsis thaliana,  and  Zea mays.  Using quantitative mass spectrometry, we identified 337 binding proteins across these species. Of these proteins, 99 were previously characterized to be involved in DNA repair. Through orthology, network, and domain analysis, we linked 44 previously unconnected proteins to DNA repair. Our study presents a resource for future study of the crosstalk and evolutionary conservation of DNA damage repair across all domains of life.","doi":"10.1016/j.isci.2023.106778","authors":"Nischwitz E, Schoonenberg VAC, Fradera-Sola A, Dejung M, Vydzhak O, Levin M, Luke B, Butter F, Scheibe M","authors_abbrev":"Nischwitz E et al.","pubmed_publication_date":"16 Jun 2023","pubmed_entrez_date":"2023-05-30","publication_year":"2023","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2023-05-31 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2110481","title":"Phenylmethylsulfonyl fluoride protects L-lysine transport in Schizosaccharomyces pombe against inactivation by ammonium ions.","citation":"Biochim Biophys Acta 1990 Apr 30;1023(3):380-2","abstract":"Ammonium ions inactivate the basic amino acid transport system in Schizosaccharomyces pombe in an irreversible manner. The inactivation is accompanied by a 4-fold decrease of KT of L-lysine transport, leaving its Jmax unchanged; phenylmethylsulfonyl fluoride protects the system against inactivation. In contrast, two basic amino acid transport systems in a gap1 mutant of Saccharomyces cerevisiae are influenced by NH4+ ions in such a way that only the Jmax decreases while the KT of L-lysine transport is unchanged. Phenylmethylsulfonyl fluoride does not act here as a protective agent.","authors":"Horák J, Sychrová H, Kotyk A","authors_abbrev":"Horák J et al.","pubmed_publication_date":"30 Apr 1990","pubmed_entrez_date":"1990-04-30","publication_year":"1990","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16357443","title":"A role for fission yeast Rab GTPase Ypt7p in sporulation.","citation":"Cell Struct Funct 2005;30(2):43-9","abstract":"Ypt7p, a fission yeast (Schizosaccharomyces pombe) homologue of Rab7 GTPase, mediates fusion of endosomes to vacuoles and homotypic vacuole fusion. Here, we report that Ypt7p plays important roles in sporulation. Most ypt7Delta asci produced less than four spores, which were apparently immature and germinated at low frequency. Furthermore, ypt7Delta cells were defective in development of the forespore membranes. Vacuoles in sporulating cells were found to undergo extensive homotypic vacuole fusion to form a few large compartments occupying the entire cytoplasm of asci. This extensive vacuole fusion depended on Ypt7p.","authors":"Kashiwazaki J, Nakamura T, Iwaki T, Takegawa K, Shimoda C","authors_abbrev":"Kashiwazaki J et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-12-17","publication_year":"2005","canto_session_key":"68e0f42c57f9d011","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-09-16 14:19:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-28 14:26:01","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC825.03c","SPBC405.04c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-07-28"},{"uniquename":"PMID:26701883","title":"New scaling relation for information transfer in biological networks.","citation":"J R Soc Interface 2015 Dec 06;12(113):20150944","abstract":"We quantify characteristics of the informational architecture of two representative biological networks: the Boolean network model for the cell-cycle regulatory network of the fission yeast Schizosaccharomyces pombe (Davidich et al. 2008 PLoS ONE 3, e1672 (doi:10.1371/journal.pone.0001672)) and that of the budding yeast Saccharomyces cerevisiae (Li et al. 2004 Proc. Natl Acad. Sci. USA 101, 4781-4786 (doi:10.1073/pnas.0305937101)). We compare our results for these biological networks with the same analysis performed on ensembles of two different types of random networks: Erdös-Rényi and scale-free. We show that both biological networks share features in common that are not shared by either random network ensemble. In particular, the biological networks in our study process more information than the random networks on average. Both biological networks also exhibit a scaling relation in information transferred between nodes that distinguishes them from random, where the biological networks stand out as distinct even when compared with random networks that share important topological properties, such as degree distribution, with the biological network. We show that the most biologically distinct regime of this scaling relation is associated with a subset of control nodes that regulate the dynamics and function of each respective biological network. Information processing in biological networks is therefore interpreted as an emergent property of topology (causal structure) and dynamics (function). Our results demonstrate quantitatively how the informational architecture of biologically evolved networks can distinguish them from other classes of network architecture that do not share the same informational properties.","doi":"10.1098/rsif.2015.0944","authors":"Kim H, Davies P, Walker SI","authors_abbrev":"Kim H et al.","pubmed_publication_date":"06 Dec 2015","pubmed_entrez_date":"2015-12-25","publication_year":"2015","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2015-12-26 01:19:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34460892","title":"Transcriptome sequencing and screening of genes related to glucose availability in Schizosaccharomyces pombe by RNA-seq analysis.","citation":"Genet Mol Biol 2021;44(3):e20200245","abstract":"While calorie restriction is the most used experimental intervention to increase lifespan in numerous model organisms, increasing evidence suggests that excess glucose leads to decreased lifespan in various organisms. To fully understand the molecular basis of the pro-aging effect of glucose, it is still important to discover genetic interactions, gene expression patterns, and molecular responses depending on glucose availability. Here, we compared the gene expression profiles in Schizosaccharomyces pombe mid-log-phase cells grown in three different Synthetic Dextrose media with 3%, 5%, and 8% glucose, using the RNA sequencing method. Expression patterns of genes that function in carbohydrate metabolism were downregulated as expected, and these genes were downregulated in line with the increase in glucose content. Significant and consistent changes in the expression were observed such as genes that encoding retrotransposable elements, heat shock proteins, glutathione S-transferase, cell agglutination protein, and conserved fungal proteins. We group some genes that function together in the transcription process and mitotic regulation, which have recently been associated with glucose availability. Our results shed light on the relationship between excess glucose, diverse cellular processes, and aging.","doi":"10.1590/1678-4685-GMB-2020-0245","authors":"Tarhan Ç, Çakır Ö","authors_abbrev":"Tarhan Ç et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-08-30","publication_year":"2021","canto_session_key":"dff943277843288b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Cagatay TARHAN","canto_first_approved_date":"2021-09-28 17:55:39","canto_approved_date":"2021-09-28 18:29:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-22 10:43:28","canto_added_date":"2021-09-01 00:15:04","annotation_curators":[{"name":"Cagatay TARHAN","community_curator":true,"annotation_count":57,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.10","SPBP4H10.09","SPCC1223.03c","SPBC21C3.19","SPAC1071.04c","SPAC977.18","SPBC660.05","SPAC12G12.09","SPCC191.11","SPCC1902.02","SPAC13F5.03c","SPCC1020.01c","SPAC959.06c","SPAC13G7.02c","SPBC28E12.01c","SPBC359.04c","SPAP11E10.02c","SPBC29A3.03c","SPAPB24D3.10c","SPBC3E7.02c","SPBPB21E7.07","SPBPB2B2.12c","SPCC1235.18","SPAC869.02c","SPAC1687.20c","SPBC887.06c","SPCC576.19c","SPBPB2B2.10c","SPAPB15E9.03c","SPBC725.12","SPBPB21E7.04c","SPAC5H10.06c","SPCC794.01c","SPAC2F3.07c","SPBC685.02","SPCC1223.15c","SPAC4F8.08","SPCC61.02","SPAC26A3.13c","SPAC750.04c","SPAC823.06","SPBPB2B2.13","SPBP22H7.09c","SPCC548.07c","SPBPB2B2.05","SPCC965.07c","SPBPB2B2.11","SPAC589.02c","SPBC1604.20c","SPCC663.08c","SPCC970.12","SPCC63.03","SPCC1235.14","SPCP20C8.02c","SPBC1718.05","SPBPB2B2.18","SPBC23G7.09","SPAC959.11","SPBC16D10.08c"],"gene_count":59,"ltp_gene_count":57,"approved_date":"2021-09-28"},{"uniquename":"PMID:37731000","title":"Acetyl-methyllysine marks chromatin at active transcription start sites.","citation":"Nature 2023 Oct;622(7981):173-179","abstract":"Lysine residues in histones and other proteins can be modified by post-translational modifications that encode regulatory information 1 . Lysine acetylation and methylation are especially important for regulating chromatin and gene expression 2-4 . Pathways involving these post-translational modifications are targets for clinically approved therapeutics to treat human diseases. Lysine methylation and acetylation are generally assumed to be mutually exclusive at the same residue. Here we report cellular lysine residues that are both methylated and acetylated on the same side chain to form N ε -acetyl-N ε -methyllysine (Kacme). We show that Kacme is found on histone H4 (H4Kacme) across a range of species and across mammalian tissues. Kacme is associated with marks of active chromatin, increased transcriptional initiation and is regulated in response to biological signals. H4Kacme can be installed by enzymatic acetylation of monomethyllysine peptides and is resistant to deacetylation by some HDACs in vitro. Kacme can be bound by chromatin proteins that recognize modified lysine residues, as we demonstrate with the crystal structure of acetyllysine-binding protein BRD2 bound to a histone H4Kacme peptide. These results establish Kacme as a cellular post-translational modification with the potential to encode information distinct from methylation and acetylation alone and demonstrate that Kacme has all the hallmarks of a post-translational modification with fundamental importance to chromatin biology.","doi":"10.1038/s41586-023-06565-9","authors":"Lu-Culligan WJ, Connor LJ, Xie Y, Ekundayo BE, Rose BT, Machyna M, Pintado-Urbanc AP, Zimmer JT, Vock IW, Bhanu NV, King MC, Garcia BA, Bleichert F, Simon MD","authors_abbrev":"Lu-Culligan WJ et al.","pubmed_publication_date":"Oct 2023","pubmed_entrez_date":"2023-09-21","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1739.05"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:30465652","title":"Multi-protein bridging factor 1(Mbf1), Rps3 and Asc1 prevent stalled ribosomes from frameshifting.","citation":"Elife 2018 Nov 22;7","abstract":"Reading frame maintenance is critical for accurate translation. We show that the conserved eukaryotic/archaeal protein Mbf1 acts with ribosomal proteins Rps3/uS3 and eukaryotic Asc1/RACK1 to prevent frameshifting at inhibitory CGA-CGA codon pairs in the yeast  Saccharomyces cerevisiae . Mutations in  RPS3  that allow frameshifting implicate eukaryotic conserved residues near the mRNA entry site. Mbf1 and Rps3 cooperate to maintain the reading frame of stalled ribosomes, while Asc1 also mediates distinct events that result in recruitment of the ribosome quality control complex and mRNA decay. Frameshifting occurs through a +1 shift with a CGA codon in the P site and involves competition between codons entering the A site, implying that the wobble interaction of the P site codon destabilizes translation elongation. Thus, eukaryotes have evolved unique mechanisms involving both a universally conserved ribosome component and two eukaryotic-specific proteins to maintain the reading frame at ribosome stalls.","doi":"10.7554/eLife.39637","authors":"Wang J, Zhou J, Yang Q, Grayhack EJ","authors_abbrev":"Wang J et al.","pubmed_publication_date":"22 Nov 2018","pubmed_entrez_date":"2018-11-23","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16G5.14c","SPBC83.17"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:19712041","title":"Systematic mapping of genetic interaction networks.","citation":"Annu Rev Genet 2009;43:601-25","abstract":"Genetic interactions influencing a phenotype of interest can be identified systematically using libraries of genetic tools that perturb biological systems in a defined manner. Systematic screens conducted in the yeast Saccharomyces cerevisiae have identified thousands of genetic interactions and provided insight into the global structure of biological networks. Techniques enabling systematic genetic interaction mapping have been extended to other single-celled organisms, the bacteria Escherichia coli and the yeast Schizosaccharomyces pombe, opening the way to comparative investigations of interaction networks. Genetic interaction screens in Caenorhabditis elegans, Drosophila melanogaster, and mammalian models are helping to improve our understanding of metazoan-specific signaling pathways. Together, our emerging knowledge of the genetic wiring diagrams of eukaryotic and prokaryotic cells is providing a new understanding of the relationship between genotype and phenotype.","doi":"10.1146/annurev.genet.39.073003.114751","authors":"Dixon SJ, Costanzo M, Baryshnikova A, Andrews B, Boone C","authors_abbrev":"Dixon SJ et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-08-29","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21633354","title":"Condensin association with histone H2A shapes mitotic chromosomes.","citation":"Nature 2011 Jun 01;474(7352):477-83","abstract":"Chromosome structure is dynamically regulated during cell division, and this regulation is dependent, in part, on condensin. The localization of condensin at chromosome arms is crucial for chromosome partitioning during anaphase. Condensin is also enriched at kinetochores but its precise role and loading machinery remain unclear. Here we show that fission yeast (Schizosaccharomyces pombe) kinetochore proteins Pcs1 and Mde4--homologues of budding yeast (Saccharomyces cerevisiae) monopolin subunits and known to prevent merotelic kinetochore orientation--act as a condensin 'recruiter' at kinetochores, and that condensin itself may act to clamp microtubule binding sites during metaphase. In addition to the regional recruitment factors, overall condensin association with chromatin is governed by the chromosomal passenger kinase Aurora B. Aurora-B-dependent phosphorylation of condensin promotes its association with histone H2A and H2A.Z, which we identify as conserved chromatin 'receptors' of condensin. Condensin phosphorylation and its deposition onto chromosome arms reach a peak during anaphase, when Aurora B kinase relocates from centromeres to the spindle midzone, where the separating chromosome arms are positioned. Our results elucidate the molecular basis for the spatiotemporal regulation of mitotic chromosome architecture, which is crucial for chromosome partitioning.","doi":"10.1038/nature10179","authors":"Tada K, Susumu H, Sakuno T, Watanabe Y","authors_abbrev":"Tada K et al.","pubmed_publication_date":"01 Jun 2011","pubmed_entrez_date":"2011-06-03","publication_year":"2011","canto_session_key":"7d2c05ef7277f909","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-02-25 16:22:12","canto_approved_date":"2024-04-02 16:23:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-30 06:46:16","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":52,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC306.03c","SPAC19G12.06c","SPAC16A10.07c","SPBC336.07","SPAC11E3.03","SPBC1861.01c","SPBC11B10.10c","SPBC6B1.04","SPCC622.08c","SPBC776.13","SPBC146.03c","SPCC320.13c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2017-02-25"},{"uniquename":"PMID:28377506","title":"Heme deficiency sensitizes yeast cells to oxidative stress induced by hydroxyurea.","citation":"J Biol Chem 2017 Jun 02;292(22):9088-9103","abstract":"Hydroxyurea (HU) has a long history of clinical and scientific use as an antiviral, antibacterial, and antitumor agent. It inhibits ribonucleotide reductase and reversibly arrests cells in S phase. However, high concentrations or prolonged treatment with low doses of HU can cause cell lethality. Although the cytotoxicity of HU may significantly contribute to its therapeutic effects, the underlying mechanisms remain poorly understood. We have previously shown that HU can induce cytokinesis arrest in the  erg11-1  mutant of fission yeast, which has a partial defect in the biosynthesis of fungal membrane sterol ergosterol. Here, we report the identification of a new mutant in heme biosynthesis,  hem13-1 , that is hypersensitive to HU. We found that the HU hypersensitivity of the  hem13-1  mutant is caused by oxidative stress and not by replication stress or a defect in cellular response to replication stress. The mutation is hypomorphic and causes heme deficiency, which likely sensitizes the cells to the HU-induced oxidative stress. Because the heme biosynthesis pathway is highly conserved in eukaryotes, this finding, as we show in our separate report, may help to expand the therapeutic spectrum of HU to additional pathological conditions.","doi":"10.1074/jbc.M117.781211","authors":"Singh A, Xu YJ","authors_abbrev":"Singh A et al.","pubmed_publication_date":"02 Jun 2017","pubmed_entrez_date":"2017-04-06","publication_year":"2017","canto_session_key":"f3c7bd963b3b7da5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yongjie Xu","canto_first_approved_date":"2019-12-12 20:33:13","canto_approved_date":"2026-03-31 14:10:37","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-11-21 15:55:34","canto_added_date":"2017-04-07 00:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Yongjie Xu","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC222.11","SPAC4A8.03c","SPAC694.06c","SPCC4B3.05c","SPAC1F5.07c","SPCC18B5.11c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2019-12-12"},{"uniquename":"PMID:30394386","title":"Saccharomyces cerevisiae Metabolic Labeling with 4-thiouracil and the Quantification of Newly Synthesized mRNA As a Proxy for RNA Polymerase II Activity.","citation":"J Vis Exp 2018 Oct 22;(140)","abstract":"Global defects in RNA polymerase II transcription might be overlooked by transcriptomic studies analyzing steady-state RNA. Indeed, the global decrease in mRNA synthesis has been shown to be compensated by a simultaneous decrease in mRNA degradation to restore normal steady-state levels. Hence, the genome-wide quantification of mRNA synthesis, independently from mRNA decay, is the best direct reflection of RNA polymerase II transcriptional activity. Here, we discuss a method using non-perturbing metabolic labeling of nascent RNAs in Saccharomyces cerevisiae (S. cerevisiae). Specifically, the cells are cultured for 6 min with a uracil analog, 4-thiouracil, and the labeled newly transcribed RNAs are purified and quantified to determine the synthesis rates of all individual mRNA. Moreover, using labeled Schizosaccharomyces pombe cells as internal standard allows comparing mRNA synthesis in different S. cerevisiae strains. Using this protocol and fitting the data with a dynamic kinetic model, the corresponding mRNA decay rates can be determined.","doi":"10.3791/57982","authors":"Baptista T, Devys D","authors_abbrev":"Baptista T et al.","pubmed_publication_date":"22 Oct 2018","pubmed_entrez_date":"2018-11-06","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-11-07 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18045993","title":"RFCCtf18 and the Swi1-Swi3 complex function in separate and redundant pathways required for the stabilization of replication forks to facilitate sister chromatid cohesion in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2008 Feb;19(2):595-607","abstract":"Sister chromatid cohesion is established during S phase near the replication fork. However, how DNA replication is coordinated with chromosomal cohesion pathway is largely unknown. Here, we report studies of fission yeast Ctf18, a subunit of the RFC(Ctf18) replication factor C complex, and Chl1, a putative DNA helicase. We show that RFC(Ctf18) is essential in the absence of the Swi1-Swi3 replication fork protection complex required for the S phase stress response. Loss of Ctf18 leads to an increased sensitivity to S phase stressing agents, a decreased level of Cds1 kinase activity, and accumulation of DNA damage during S phase. Ctf18 associates with chromatin during S phase, and it is required for the proper resumption of replication after fork arrest. We also show that chl1Delta is synthetically lethal with ctf18Delta and that a dosage increase of chl1(+) rescues sensitivities of swi1Delta to S phase stressing agents, indicating that Chl1 is involved in the S phase stress response. Finally, we demonstrate that inactivation of Ctf18, Chl1, or Swi1-Swi3 leads to defective centromere cohesion, suggesting the role of these proteins in chromosome segregation. We propose that RFC(Ctf18) and the Swi1-Swi3 complex function in separate and redundant pathways essential for replication fork stabilization to facilitate sister chromatid cohesion in fission yeast.","authors":"Ansbach AB, Noguchi C, Klansek IW, Heidlebaugh M, Nakamura TM, Noguchi E","authors_abbrev":"Ansbach AB et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2007-11-30","publication_year":"2008","canto_session_key":"ec2b5001ede2dba2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-02-24 15:09:24","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-02-24 15:08:53","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_18045993_phaf.tsv"}],"genes":["SPBC216.06c","SPBC216.05","SPBC83.14c","SPCC338.17c","SPAC2G11.12","SPAC3G6.11","SPBC30D10.04","SPAC1687.03c","SPAC14C4.13","SPAC1142.03c","SPCC1259.13","SPBC902.02c","SPCC18B5.11c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2016-02-24"},{"uniquename":"PMID:16751704","title":"An alpha-amylase homologue, aah3, encodes a GPI-anchored membrane protein required for cell wall integrity and morphogenesis in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2006 Jun;70(6):1454-63","abstract":"Glycosylphosphatidylinositol (GPI)-anchored proteins are essential for normal cellular morphogenesis and have an additional role in mediating cross-linking of glycoproteins to cell wall glucan in yeast cells. Although many GPI-anchored proteins have been characterized in Saccharomyces cerevisiae, none have been reported for well-characterized GPI-anchored proteins in Schizosaccharomyces pombe to date. Among the putative GPI-anchored proteins in S. pombe, four alpha-amylase homologs (Aah1p-Aah4p) have putative signal sequences and C-terminal GPI anchor addition signals. Disruption of aah3(+) resulted in a morphological defect and hypersensitivity to cell wall-degrading enzymes. Biochemical analysis showed that Aah3p is an N-glycosylated, GPI-anchored membrane protein localized in the membrane and cell wall fractions. Conjugation and sporulation were not affected by the aah3(+) deletion, but the ascal wall of aah3Delta cells was easily lysed by hydrolases. Expression of aah3 alleles in which the conserved aspartic acid and glutamic acid residues required for hydrolase activity were replaced with alanine residues failed to rescue the morphological and ascal wall defects of aah3Delta cells. Taken together, these results indicate that Aah3p is a GPI-anchored protein and is required for cell and ascal wall integrity in S. pombe.","authors":"Morita T, Tanaka N, Hosomi A, Giga-Hama Y, Takegawa K","authors_abbrev":"Morita T et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-06-06","publication_year":"2006","canto_session_key":"1bf80bf0551f7784","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-01 08:07:35","canto_approved_date":"2022-08-30 06:58:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-01 08:07:27","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23D3.14c","SPCC757.12","SPCC63.02c","SPBC16A3.13"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-04-01"},{"uniquename":"PMID:16850188","title":"Cloning, characterization and regulation of a protein disulfide isomerase from the fission yeast Schizosaccharomyces pombe.","citation":"Mol Biol Rep 2006 Sep;33(3):187-96","abstract":"To elucidate the physiological roles and regulation of a protein disulfide isomerase (PDI) from the fission yeast Schizosaccharomyces pombe, the full-length PDI gene was ligated into the shuttle vector pRS316, resulting in pPDI10. The determined DNA sequence carries 1,636 bp and encodes the putative 359 amino acid sequence of PDI with a molecular mass of 39,490 Da. In the amino acid sequence, the S. pombe PDI appears to be very homologous to A. thaliana PDI. The S. pombe cells harboring pPDI10 showed increased PDI activity and accelerated growth, suggesting that the cloned PDI gene is functioning and involved in the yeast growth. The 460 bp upstream region of the PDI gene was fused into promoterless beta-galactosidase gene of the shuttle vector YEp367R to generate pYUPDI10. The synthesis of beta-galactosidase from the PDI-lacZ fusion gene was enhanced by oxidative stress, such as superoxide anion and hydrogen peroxide. It was also induced by some non-fermentable and fermentable carbon sources. Nitrogen starvation was able to enhance the synthesis of beta-galactosidase from the PDI-lacZ fusion gene. The enhancement by oxidative stress and fermentable carbon sources did not depend on the presence of Pap1. The PDI mRNA levels were increased in both Pap1-positive and Pap1-negative cells treated with glycerol. Taken together, the S. pombe PDI gene is involved in cellular growth and response to nutritional and oxidative stress.","authors":"Kim SJ, Choi YS, Kim HG, Park EH, Lim CJ","authors_abbrev":"Kim SJ et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-07-20","publication_year":"2006","canto_session_key":"8f3b89b9ffb6cf36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:35:38","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-06 11:15:05","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.14c","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-11-06"},{"uniquename":"PMID:12073089","title":"Characterization of Cu, Zn-superoxide dismutase-deficient mutant of fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 2002 May;41(2):82-8","abstract":"A Cu, Zn-superoxide dismutase gene ( sod1+) deletion mutant of fission yeast Schizosaccharomyces pombe was constructed and its properties were investigated. Superoxide dismutase activity was not detected in the mutant on activity staining of polyacrylamide gels. The mutant showed cysteine or methionine and lysine auxotrophy, slow growth and sensitivity to menadione. While expression of the apt1+ gene, induction of which depends on the Pap1 transcription factor, was induced at the same concentration of menadione in both the wild-type cell and the sod1 mutant, expression of the gpx1+ gene, induction of which depends on the Atf1 transcription factor, was induced at a lower concentration of menadione in the mutant compared with the wild-type control. Expression of the sod1+ gene was induced by oxidative stress and no induction was observed in pap1, prr1 and spc1 mutants.","authors":"Mutoh N, Nakagawa CW, Yamada K","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-06-20","publication_year":"2002","canto_session_key":"679551fd20beff97","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-08-04 10:36:37","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-08-04 10:36:30","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.14","SPBC32F12.03c","SPBC29B5.01","SPAC1783.07c","SPAC821.10c","SPAC24B11.06c"],"gene_count":6,"ltp_gene_count":1,"approved_date":"2015-08-04"},{"uniquename":"PMID:11864600","title":"Meiotic recombination remote from prominent DNA break sites in S. pombe.","citation":"Mol Cell 2002 Feb;9(2):253-63","abstract":"DNA breakage is intimately associated with meiotic recombination in the fission yeast Schizosaccharomyces pombe. Sites of prominent DNA breakage were found approximately 25 to approximately 200 kb apart in the genomic regions surveyed. We examined in detail a 501 kb region of chromosome I and found six sites, or tight clusters of sites, at which approximately 2%-11% of the DNA accumulated breaks in a rad50S mutant. In contrast to the discrete, widely spaced distribution of prominent break sites, recombination in this region was more uniformly distributed (0.7-1.6 cM/10 kb) whether the genetic interval tested contained no, one, or more such sites. We infer that although recombination depends upon DNA breakage, recombination often occurs remote from these sites (tens of kilobases away); we discuss mechanisms by which this may occur.","authors":"Young JA, Schreckhise RW, Steiner WW, Smith GR","authors_abbrev":"Young JA et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-02-28","publication_year":"2002","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.11","SPAC22F3.09c","SPAC22G7.06c","SPAC2G11.12"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:10409764","title":"Nup124p is a nuclear pore factor of Schizosaccharomyces pombe that is important for nuclear import and activity of retrotransposon Tf1.","citation":"Mol Cell Biol 1999 Aug;19(8):5768-84","abstract":"The long terminal repeat (LTR)-containing retrotransposon Tf1 propagates within the fission yeast Schizosaccharomyces pombe as the result of several mechanisms that are typical of both retrotransposons and retroviruses. To identify host factors that contribute to the transposition process, we mutagenized cultures of S. pombe and screened them for strains that were unable to support Tf1 transposition. One such strain contained a mutation in a gene we named nup124. The product of this gene contains 11 FXFG repeats and is a component of the nuclear pore complex. In addition to the reduced levels of Tf1 transposition, the nup124-1 allele caused a significant reduction in the nuclear localization of Tf1 Gag. Surprisingly, the mutation in nup124-1 did not cause any reduction in the growth rate, the nuclear localization of specific nuclear localization signal-containing proteins, or the cytoplasmic localization of poly(A) mRNA. A two-hybrid analysis and an in vitro precipitation assay both identified an interaction between Tf1 Gag and the N terminus of Nup124p. These results provide evidence for an unusual mechanism of nuclear import that relies on a direct interaction between a nuclear pore factor and Tf1 Gag.","authors":"Balasundaram D, Benedik MJ, Morphew M, Dang VD, Levin HL","authors_abbrev":"Balasundaram D et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-07-20","publication_year":"1999","canto_session_key":"fc322c6ce032c762","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-29 09:22:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-29 09:22:25","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-29"},{"uniquename":"PMID:23622681","title":"A 2D/3D image analysis system to track fluorescently labeled structures in rod-shaped cells: application to measure spindle pole asymmetry during mitosis.","citation":"Cell Div 2013;8:6","abstract":"The yeast Schizosaccharomyces pombe is frequently used as a model for studying the cell cycle. The cells are rod-shaped and divide by medial fission. The process of cell division, or cytokinesis, is controlled by a network of signaling proteins called the Septation Initiation Network (SIN); SIN proteins associate with the SPBs during nuclear division (mitosis). Some SIN proteins associate with both SPBs early in mitosis, and then display strongly asymmetric signal intensity at the SPBs in late mitosis, just before cytokinesis. This asymmetry is thought to be important for correct regulation of SIN signaling, and coordination of cytokinesis and mitosis. In order to study the dynamics of organelles or large protein complexes such as the spindle pole body (SPB), which have been labeled with a fluorescent protein tag in living cells, a number of the image analysis problems must be solved; the cell outline must be detected automatically, and the position and signal intensity associated with the structures of interest within the cell must be determined.\nWe present a new 2D and 3D image analysis system that permits versatile and robust analysis of motile, fluorescently labeled structures in rod-shaped cells. We have designed an image analysis system that we have implemented as a user-friendly software package allowing the fast and robust image-analysis of large numbers of rod-shaped cells. We have developed new robust algorithms, which we combined with existing methodologies to facilitate fast and accurate analysis. Our software permits the detection and segmentation of rod-shaped cells in either static or dynamic (i.e. time lapse) multi-channel images. It enables tracking of two structures (for example SPBs) in two different image channels. For 2D or 3D static images, the locations of the structures are identified, and then intensity values are extracted together with several quantitative parameters, such as length, width, cell orientation, background fluorescence and the distance between the structures of interest. Furthermore, two kinds of kymographs of the tracked structures can be established, one representing the migration with respect to their relative position, the other representing their individual trajectories inside the cell. This software package, called \"RodCellJ\", allowed us to analyze a large number of S. pombe cells to understand the rules that govern SIN protein asymmetry. (Continued on next page) (Continued from previous page).\n\"RodCellJ\" is freely available to the community as a package of several ImageJ plugins to simultaneously analyze the behavior of a large number of rod-shaped cells in an extensive manner. The integration of different image-processing techniques in a single package, as well as the development of novel algorithms does not only allow to speed up the analysis with respect to the usage of existing tools, but also accounts for higher accuracy. Its utility was demonstrated on both 2D and 3D static and dynamic images to study the septation initiation network of the yeast Schizosaccharomyces pombe. More generally, it can be used in any kind of biological context where fluorescent-protein labeled structures need to be analyzed in rod-shaped cells.\nRodCellJ is freely available under http://bigwww.epfl.ch/algorithms.html.","doi":"10.1186/1747-1028-8-6","authors":"Schmitter D, Wachowicz P, Sage D, Chasapi A, Xenarios I, Simanis, Unser M","authors_abbrev":"Schmitter D et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-04-30","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41910327","title":"mGem: Cut4/Apc1 and its prion form at the cross roads of cell cycle regulation, heterochromatin organization, RNAi, stress response, and evolution.","citation":"mBio 2026 Mar 30;:e0083725","abstract":"The anaphase-promoting complex/cyclosome (APC/C) complex plays a pivotal role in cell cycle progression in eukaryotes. APC/C-mediated polyubiquitination and subsequent degradation of regulatory factors ensure sister chromatid separation during mitosis and mitotic exit. Likewise, coordination between the chromodomain protein Swi6/HP1, histone methyltransferase Clr4/Suv39, and RNAi promotes heterochromatin assembly in  Schizosaccharomyces pombe . Interestingly, Cut4/Apc1 and Cut9 subunits of APC/C regulate RNAi and interact with Swi6/HP1 and Clr4/Suv39 to promote mutual recruitment at heterochromatin.  sng2-1 , a mutant of Cut4/Apc1, can assume a prion form, designated [SNG2], with defective heterochromatin silencing. As in prions, this defect is inherited in a non-Mendelian manner, accompanied by aggregation of Cut4. Paradoxically, along with greater chromosome instability and aneuploidy-phenotypes associated with cancer, the prion form displayed enhanced stress tolerance, thereby providing a trade-off between defects in chromosome integrity and survival under stress conditions. Thus, the prion form may confer evolutionary advantage.","doi":"10.1128/mbio.00837-25","authors":"Sharma S, Singh J","authors_abbrev":"Sharma S et al.","pubmed_publication_date":"30 Mar 2026","pubmed_entrez_date":"2026-03-30","publication_year":"2026","canto_session_key":"588feb394eb5f746","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-30 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18459978","title":"Schizosaccharomyces pombe positive cofactor 4 stimulates basal transcription from TATA-containing and TATA-less promoters through Mediator and transcription factor IIA.","citation":"FEBS J 2008 Jun;275(11):2873-83","abstract":"The positive cofactor 4 (PC4) protein has an important role in transcriptional activation, which has been proposed to be mediated by transcription factor IIA (TFIIA) and TATA-binding protein-associated factors. To test this hypothesis, we cloned the Schizosaccharomyces pombe PC4 gene and analysed the role of the PC4 protein in the stimulation of basal transcription driven by TATA-containing and TATA-less promoters. Sc. pombe PC4 was able to stimulate basal transcription from several TATA-containing promoters and from the Initiator sequences of the highly transcribed Sc. pombe nmt1 gene. Moreover, it was demonstrated that Sc. pombe PC4 stimulates formation of the transcription preinitiation complex. Activation of transcription by PC4 was dependent on the Mediator complex and TFIIA, but was independent of TATA-binding protein-associated factor. PC4 binds to double-stranded and single-stranded DNA and interacts with TATA-binding protein, TFIIB, TFIIA, Mediator, TFIIH and the transcriptional activator protein VP16.","doi":"10.1111/j.1742-4658.2008.06429.x","authors":"Contreras-Levicoy J, Urbina F, Maldonado E","authors_abbrev":"Contreras-Levicoy J et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-05-08","publication_year":"2008","canto_session_key":"ae0a54cf0c62977c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-09 16:31:25","canto_approved_date":"2024-06-09 16:31:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-09 16:31:17","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-06-09"},{"uniquename":"PMID:11493649","title":"Fission yeast mfr1 activates APC and coordinates meiotic nuclear division with sporulation.","citation":"J Cell Sci 2001 Jun;114(Pt 11):2135-43","abstract":"Meiosis is the developmental program by which sexually reproducing diploid organisms generate haploid gametes. In yeast, meiosis is followed by spore morphogenesis. These two events are normally coordinated in such a way that spore formation is dependent upon completion of the meiotic nuclear divisions. Here we describe a meiosis-specific protein, mfr1, that is involved in this coordination. mfr1 is an activator of the anaphase-promoting complex (APC), which is necessary for the rapid degradation of the cdc13 cyclin at the end of meiosis II, prior to the formation of spores. An mfr1 null mutant completes meiosis II but remains with high levels of cdc13 and cdc2 kinase activity and has considerably delayed spore formation. By analogy with the mitotic cell cycle, where proteolysis and inactivation of cdc2 kinase are necessary to trigger mitotic exit and cytokinesis, we propose that at the end of meiosis rapid and timely proteolysis of cyclins is required to switch on the differentiation program that eventually leads to the formation of haploid gametes.","authors":"Blanco MA, Pelloquin L, Moreno S","authors_abbrev":"Blanco MA et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-08-09","publication_year":"2001","canto_session_key":"d51e46afca090869","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-11 16:40:29","canto_approved_date":"2026-01-04 11:04:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-25 11:50:46","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPCC4E9.02","SPBC1198.12","SPAC19G12.01c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-10-11"},{"uniquename":"PMID:26519320","title":"Fission Yeast Cell Cycle Synchronization Methods.","citation":"Methods Mol Biol 2016;1369:293-308","abstract":"Fission yeast cells can be synchronized by cell cycle arrest and release or by size selection. Cell cycle arrest synchronization is based on the block and release of temperature-sensitive cell cycle mutants or treatment with drugs. The most widely used approaches are cdc10-129 for G1; hydroxyurea (HU) for early S-phase; cdc25-22 for G2, and nda3-KM311 for mitosis. Cells can also be synchronized by size selection using centrifugal elutriation or a lactose gradient. Here we describe the methods most commonly used to synchronize fission yeast cells.","doi":"10.1007/978-1-4939-3145-3_20","authors":"Tormos-Pérez M, Pérez-Hidalgo L, Moreno S","authors_abbrev":"Tormos-Pérez M et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-11-01","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-02 01:19:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33904404","title":"Protomer alignment modulates specificity of RNA substrate recognition by Ire1.","citation":"Elife 2021 Apr 27;10","abstract":"The unfolded protein response (UPR) maintains protein folding homeostasis in the endoplasmic reticulum (ER). In metazoan cells, the Ire1 branch of the UPR initiates two functional outputs-non-conventional mRNA splicing and selective mRNA decay (RIDD). By contrast, Ire1 orthologs from  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe  are specialized for only splicing or RIDD, respectively. Previously, we showed that the functional specialization lies in Ire1's RNase activity, which is either stringently splice-site specific or promiscuous (Li et al., 2018). Here, we developed an assay that reports on Ire1's RNase promiscuity. We found that conversion of two amino acids within the RNase domain of  S. cerevisiae  Ire1 to their  S. pombe  counterparts rendered it promiscuous. Using biochemical assays and computational modeling, we show that the mutations rewired a pair of salt bridges at Ire1 RNase domain's dimer interface, changing its protomer alignment. Thus, Ire1 protomer alignment affects its substrates specificity.","doi":"10.7554/eLife.67425","authors":"Li W, Crotty K, Garrido Ruiz D, Voorhies M, Rivera C, Sil A, Mullins RD, Jacobson MP, Peschek J, Walter P","authors_abbrev":"Li W et al.","pubmed_publication_date":"27 Apr 2021","pubmed_entrez_date":"2021-04-27","publication_year":"2021","canto_session_key":"1ce7ece55b87cb71","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-04-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC167.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8442387","title":"Yeasts have a four-fold variation in ribosomal DNA copy number.","citation":"Yeast 1993 Jan;9(1):53-8","abstract":"By employing pulsed-field gel electrophoresis we have determined the size of the rDNA cluster in wild-type yeast strains representing genera of Candida, Kluyveromyces, Pachysolen, Schizosaccharomyces and Torulaspora. Although the genome size of the examined species is similar (12.3-13.9 Mb), at least a four-fold variation has been observed between the lowest amount of rDNA repeats in P. tannophilus (28) and the highest in C. glabrata and S. poombe (> 115). In two species the rDNA cluster is represented by two loci, residing either in one (S. pombe) or two chromosomes (C. glabrata).","authors":"Maleszka R, Clark-Walker GD","authors_abbrev":"Maleszka R et al.","pubmed_publication_date":"Jan 1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28889911","title":"FPD: A comprehensive phosphorylation database in fungi.","citation":"Fungal Biol 2017 Oct;121(10):869-875","abstract":"Protein phosphorylation, one of the most classic post-translational modification, plays a critical role in diverse cellular processes including cell cycle, growth, and signal transduction pathways. However, the available information about phosphorylation in fungi is limited. Here, we provided a Fungi Phosphorylation Database (FPD) that comprises high-confidence in vivo phosphosites identified by MS-based proteomics in various fungal species. This comprehensive phosphorylation database contains 62 272 non-redundant phosphorylation sites in 11 222 proteins across eight organisms, including Aspergillus flavus, Aspergillus nidulans, Fusarium graminearum, Magnaporthe oryzae, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe, and Cryptococcus neoformans. A fungi-specific phosphothreonine motif and several conserved phosphorylation motifs were discovered by comparatively analysing the pattern of phosphorylation sites in plants, animals, and fungi.","doi":"10.1016/j.funbio.2017.06.004","authors":"Bai Y, Chen B, Li M, Zhou Y, Ren S, Xu Q, Chen M, Wang S","authors_abbrev":"Bai Y et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-09-12","publication_year":"2017","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2017-09-13 00:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15647272","title":"The fission yeast protein Ker1p is an ortholog of RNA polymerase I subunit A14 in Saccharomyces cerevisiae and is required for stable association of Rrn3p and RPA21 in RNA polymerase I.","citation":"J Biol Chem 2005 Mar 25;280(12):11467-74","abstract":"A heterodimer formed by the A14 and A43 subunits of RNA polymerase (pol) I in Saccharomyces cerevisiae is proposed to correspond to the Rpb4/Rpb7 and C17/C25 heterodimers in pol II and pol III, respectively, and to play a role(s) in the recruitment of pol I to the promoter. However, the question of whether the A14/A43 heterodimer is conserved in eukaryotes other than S. cerevisiae remains unanswered, although both Rpb4/Rpb7 and C17/C25 are conserved from yeast to human. To address this question, we have isolated a Schizosaccharomyces pombe gene named ker1+ using a yeast two-hybrid system, including rpa21+, which encodes an ortholog of A43, as bait. Although no homolog of A14 has previously been found in the S. pombe genome, functional characterization of Ker1p and alignment of Ker1p and A14 showed that Ker1p is an ortholog of A14. Disruption of ker1+ resulted in temperature-sensitive growth, and the temperature-sensitive deficit of ker1delta was suppressed by overexpression of either rpa21+ or rrn3+, which encodes the rDNA transcription factor Rrn3p, suggesting that Ker1p is involved in stabilizing the association of RPA21 and Rrn3p in pol I. We also found that Ker1p dissociated from pol I in post-log-phase cells, suggesting that Ker1p is involved in growth-dependent regulation of rDNA transcription.","authors":"Imazawa Y, Hisatake K, Mitsuzawa H, Matsumoto M, Tsukui T, Nakagawa K, Nakadai T, Shimada M, Ishihama A, Nogi Y","authors_abbrev":"Imazawa Y et al.","pubmed_publication_date":"25 Mar 2005","pubmed_entrez_date":"2005-01-14","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC3B9.07c","SPAC18G6.11c","SPBC1718.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10905343","title":"Characterisation of fission yeast alp11 mutants defines three functional domains within tubulin-folding cofactor B.","citation":"Mol Gen Genet 2000 Jun;263(5):752-60","abstract":"The proper folding of tubulins prior to their incorporation into microtubules requires a group of conserved proteins called cofactors A to E. In fission yeast, homologues of these cofactors (at least B, D and E) are necessary for the biogenesis of microtubules and for cell viability. Here we show that the temperature-sensitive alp11-924 mutant, which is defective in the cofactor B homologue, contains an opal nonsense mutation, which results in the production of a truncated Alp11B protein (Alp11(1-118). We isolated a tRNA(Trp) gene as a multicopy suppressor of this mutation, which rescues alp11-924 by read-through of the nonsense codon. The truncated Alp1-118 protein lacks the C-terminal half of Alp11B, consisting of a central coiled-coil region and the distal CLIP-170 domain found in a number of proteins involved in microtubule functions. Both of these domains are required for the maintenance of microtubule architecture in vivo. Detailed functional analyses lead us to propose that Alp11B comprises three functional domains: the N-terminal half executes the essential function, the central coiled-coil region is necessary for satisfactory maintenance of cellular alpha-tubulin levels, and the C-terminal CLIP-170 domain is required for efficient binding to alpha-tubulin.","authors":"Radcliffe PA, Toda T","authors_abbrev":"Radcliffe PA et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-07-25","publication_year":"2000","canto_session_key":"640f264024eab7f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2015-05-26 10:29:08","canto_approved_date":"2023-04-04 16:24:58","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2015-04-29 16:24:49","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Jacky Hayles","community_curator":false,"annotation_count":14,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.05c","SPBC26H8.07c","SPAC13D6.05"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2015-05-26"},{"uniquename":"PMID:8895572","title":"The role of proteolysis in cell cycle progression in Schizosaccharomyces pombe.","citation":"EMBO J 1996 Oct 01;15(19):5268-79","abstract":"A cell-free system derived from Xenopus eggs was used to identify the 'destruction box' of the Schizosaccharomyces pombe B-type cyclin, Cdc13, as residues 59-67: RHALDDVSN. Expression of indestructible Cdc13 from a regulated promoter in S.pombe blocked cells in anaphase and inhibited septation, showing that destruction of Cdc13 is necessary for exit from mitosis, but not for sister chromatid separation. In contrast, strong expression of a polypeptide comprising the N-terminal 70 residues of Cdc13, which acts as a competitive inhibitor of destruction box-mediated proteolysis, inhibited both sister chromatid separation and the destruction of Cdc13, whereas an equivalent construct with a mutated destruction box did not. Appropriately timed expression of this N-terminal fragment of Cdc13 overcame the G1 arrest seen in cdc10 mutant strains, suggesting that proteins required for the initiation of S phase are subject to destruction by the same proteolytic machinery as cyclin.","authors":"Yamano H, Gannon J, Hunt T","authors_abbrev":"Yamano H et al.","pubmed_publication_date":"01 Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC336.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:26088418","title":"Fission yeast telomere-binding protein Taz1 is a functional but not a structural counterpart of human TRF1 and TRF2.","citation":"Cell Res 2015 Jul;25(7):881-4","abstract":"","doi":"10.1038/cr.2015.76","authors":"Deng W, Wu J, Wang F, Kanoh J, Dehe PM, Inoue H, Chen J, Lei M","authors_abbrev":"Deng W et al.","pubmed_publication_date":"Jul 2015","pubmed_entrez_date":"2015-06-20","publication_year":"2015","canto_session_key":"410ec2f68d834d33","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-20 08:27:17","canto_approved_date":"2023-02-20 08:27:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-19 20:07:42","canto_added_date":"2015-06-21 00:20:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-20","pdb_entries":[{"pdb_id":"4zmk","gene_chains":[{"gene_uniquename":"SPAC16A10.07c","chain":"A","position":"408-478"}],"title":"Crystal structure of the dimerization domain of S. pombe Taz1","entry_authors":"Deng W,Wu J,Wang F,Lei M","entry_authors_abbrev":"Deng W et al.","reference_uniquename":"PMID:26088418","experimental_method":"X-ray","resolution":"1.5"},{"pdb_id":"4zmi","gene_chains":[{"gene_uniquename":"SPAC16A10.07c","chain":"A","position":"127-361"}],"title":"Crystal structure of the Helical domain of S. pombe Taz1","entry_authors":"Deng W,Wu J,Wang F,Lei M","entry_authors_abbrev":"Deng W et al.","reference_uniquename":"PMID:26088418","experimental_method":"X-ray","resolution":"2.3"}]},{"uniquename":"PMID:16085485","title":"Cell division: SIN, cytokinesis and ethanol dependency.","citation":"Curr Biol 2005 Aug 09;15(15):R605-7","abstract":"A novel mutant screen in fission yeast has identified the 'ethanol dependent' protein etd1p as a potential link between the septation initiation network (SIN), which initiates cytokinesis, and the actomyosin contractile ring that drives separation of the two daughter cells at the end of mitosis.","authors":"Krapp A, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"09 Aug 2005","pubmed_entrez_date":"2005-08-09","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22815068","title":"Schizosaccharomyces pombe reporter strains for relative quantitative assessment of heterochromatin silencing.","citation":"Yeast 2012 Aug;29(8):335-41","abstract":"The fission yeast Schizosaccharomyces pombe has been emerging as an important model organism for studying the formation and repression of heterochromatin. To enable simple and relative quantitative assessment of heterochromatin silencing, we have created bioluminescence-based reporter strains. A green-emitting click beetle luciferase (CBG68) gene was inserted within pericentromeric heterochromatin or at the silent mating-type locus via homologous recombination. In the same strains, a red-emitting click beetle luciferase (CBR) gene is expressed from the euchromatic leu1(+) locus and can be used as a reference in dual-colour assays. Our reporter strains are suitable for performing Chroma-Glo™ assays, which can be carried out directly in the culture medium without prior cell lysis and in a multiwell format. Our reporter system reliably reflects the state of chromatin and can be easily adapted for use in high-throughput screening approaches.","doi":"10.1002/yea.2913","authors":"Shimada Y, Bühler M","authors_abbrev":"Shimada Y et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-07-21","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2090428","title":"Regulation of fission yeast mating-type interconversion by chromosome imprinting.","citation":"Dev Suppl 1990;:3-8","abstract":"Mating types of the fission yeast Schizosaccharomyces pombe interchange nonrandomly in a cell lineage so that only one cell among four granddaughters of a cell ever switches, and the sister of the newly switched cell switches efficiently in consecutive cell divisions, thereby producing chains of recurrent switching. The programme of cellular differentiation is mediated by inheritance of parental DNA chains at the mating type locus (mat1) by progeny cells. This review summarizes recent results suggesting that two types of imprinting events at the mat1 locus are required to generate the specific pattern of switching in a cell lineage. One of those is a site- and strand- specific event that is required before the mat1 locus can be cleaved in vivo. The other is a double-stranded break at mat1 that is healed by gene conversion in the progeny cells resulting in switching the mat1 locus.","authors":"Klar AJ","authors_abbrev":"Klar AJ","pubmed_publication_date":"1990","pubmed_entrez_date":"1990-01-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16453724","title":"Isolation and characterization of Schizosaccharomyces pombe cutmutants that block nuclear division but not cytokinesis.","citation":"EMBO J 1986 Nov;5(11):2973-9","abstract":"By examining cytological phenotypes of 587 temperature-sensitive mutants of the fission yeast Schizosaccharomyces pombe, we obtained 18 mutants which cause cell division in the absence of nuclear division. By genetic analyses, these novel nuclear division arrest mutants can be classified into nine complementation groups (designated cut1 - cut9). The cytological phenotype of cut mutants is similar but not identical to that of DNA topoisomerase II mutants (top2). The cut1 gene was cloned by transformation and shown to complement cut2 as well as cut1, indicating a functional relationship between the two genes. The cut genes are required for nuclear division, but their mutant phenotypes differ from most of the previously identified mutants which block nuclear division and also the subsequent cytokinesis. Fluorescence microscopy indicates that the mitotic chromosomes formed in cut mutant cells are abnormal and fail to separate properly. We suggest that cut mutations, like top2, block mitotic chromosome formation and concomitantly nuclear division, but that cytokinesis proceeds independently of the defects in nuclear division, demonstrating uncoordinated mitotic pathways. A novel mutant nuc1 is also described which shows a cytological phenotype similar to the double mutant of DNA topoisomerases I and II but contains normal levels of both DNA topoisomerase activities.","authors":"Hirano T, Funahashi S, Uemura T, Yanagida M","authors_abbrev":"Hirano T et al.","pubmed_publication_date":"Nov 1986","pubmed_entrez_date":"1986-11-01","publication_year":"1986","canto_session_key":"c641c32144a9fceb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-19 14:17:22","canto_approved_date":"2022-04-02 13:20:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-05 15:32:58","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":40,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC56E4.04c","SPBC19C2.01","SPAC27E2.05","SPBC1A4.03c","SPBC14C8.01c","SPBC4C3.05c","SPBC106.09","SPAC25G10.07c","SPBC336.04","SPBC11B10.09","SPAC23C4.18c","SPBC146.03c","SPBC1703.14c","SPCC5E4.04","SPCC1739.11c","SPAC6F12.15c","SPCC18B5.03","SPAC24H6.05","SPBC1734.02c","SPAC1786.03","SPAC17C9.13c"],"gene_count":21,"ltp_gene_count":19,"approved_date":"2018-03-19"},{"uniquename":"PMID:30550856","title":"Ribosomal protein eL42 contributes to the catalytic activity of the yeast ribosome at the elongation step of translation.","citation":"Biochimie 2019 Mar;158:20-33","abstract":"The GGQ minidomain of the ribosomal protein eL42 was previously shown to contact the CCA-arm of P-site bound tRNA in human ribosome, indicating a possible involvement of the protein in the catalytic activity. Here, using Schizosaccharomyces pombe (S. pombe) cells, we demonstrate that the GGQ minidomain and neighboring region of eL42 is critical for the ribosomal function. Mutant eL42 proteins containing amino acid substitutions within or adjacent to the GGQ minidomain failed to complement the function of wild-type eL42, and expression of the mutant eL42 proteins led to severe growth defects. These results suggest that the mutations in eL42 interfere with the ribosomal function in vivo. Furthermore, we show that some of the mutations associated with the conserved GGQ region lead to reduced activities in the poly(Phe) synthesis and/or in the peptidyl transferase reaction with respect to puromycin, as compared with those of the wild-type ribosomes. A pK value of 6.95 was measured for the side chain of Lys-55/Arg-55, which is considerably less than that of a Lys or Arg residue. Altogether, our findings suggest that eL42 contributes to the 80S ribosome's peptidyl transferase activity by promoting the course of the elongation cycle.","doi":"10.1016/j.biochi.2018.12.005","authors":"Hountondji C, Créchet JB, Tanaka M, Suzuki M, Nakayama JI, Aguida B, Bulygin K, Cognet J, Karpova G, Baouz S","authors_abbrev":"Hountondji C et al.","pubmed_publication_date":"Mar 2019","pubmed_entrez_date":"2018-12-15","publication_year":"2019","canto_session_key":"b652960d04d0941b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-12-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24434583","title":"A Pil1-Sle1-Syj1-Tax4 functional pathway links eisosomes with PI(4,5)P2 regulation.","citation":"J Cell Sci 2014 Mar 15;127(Pt 6):1318-26","abstract":"Stable compartments of the plasma membrane promote a wide range of cellular functions. In yeast cells, cytosolic structures called eisosomes generate prominent cortical invaginations of unknown function. Through a series of genetic screens in fission yeast, we found that the eisosome proteins Pil1 and Sle1 function with the synaptojanin-like lipid phosphatase Syj1 and its ligand Tax4. This genetic pathway connects eisosome function with the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PI(4,5)P2] in cells. Defects in PI(4,5)P2 regulation led to eisosome defects, and we found that the core eisosome protein Pil1 can bind to and tubulate liposomes containing PI(4,5)P2. Mutations in components of the Pil1-Sle1-Syj1-Tax4 pathway suppress the growth and morphology defects of TORC2 mutants, indicating that eisosome-dependent regulation of PI(4,5)P2 feeds into signal transduction pathways. We propose that the geometry of membrane invaginations generates spatial and temporal signals for lipid-mediated signaling events in cells.","doi":"10.1242/jcs.143545","authors":"Kabeche R, Roguev A, Krogan NJ, Moseley JB","authors_abbrev":"Kabeche R et al.","pubmed_publication_date":"15 Mar 2014","pubmed_entrez_date":"2014-01-18","publication_year":"2014","canto_session_key":"0022e608d11dc3e0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29932902","title":"mRNA Deadenylation Is Coupled to Translation Rates by the Differential Activities of Ccr4-Not Nucleases.","citation":"Mol Cell 2018 Jun 21;70(6):1089-1100.e8","abstract":"Translation and decay of eukaryotic mRNAs is controlled by shortening of the poly(A) tail and release of the poly(A)-binding protein Pab1/PABP. The Ccr4-Not complex contains two exonucleases-Ccr4 and Caf1/Pop2-that mediate mRNA deadenylation. Here, using a fully reconstituted biochemical system with proteins from the fission yeast Schizosaccharomyces pombe, we show that Pab1 interacts with Ccr4-Not, stimulates deadenylation, and differentiates the roles of the nuclease enzymes. Surprisingly, Pab1 release relies on Ccr4 activity. In agreement with this, in vivo experiments in budding yeast show that Ccr4 is a general deadenylase that acts on all mRNAs. In contrast, Caf1 only trims poly(A) not bound by Pab1. As a consequence, Caf1 is a specialized deadenylase required for the selective deadenylation of transcripts with lower rates of translation elongation and reduced Pab1 occupancy. These findings reveal a coupling between the rates of translation and deadenylation that is dependent on Pab1 and Ccr4-Not.","doi":"10.1016/j.molcel.2018.05.033","authors":"Webster MW, Chen YH, Stowell JAW, Alhusaini N, Sweet T, Graveley BR, Coller J, Passmore LA","authors_abbrev":"Webster MW et al.","pubmed_publication_date":"21 Jun 2018","pubmed_entrez_date":"2018-06-23","publication_year":"2018","canto_session_key":"a308a12241b3cffe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lori Passmore","canto_first_approved_date":"2018-12-17 17:06:19","canto_approved_date":"2023-10-01 17:41:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-03 17:54:29","canto_added_date":"2018-06-24 00:15:04","annotation_curators":[{"name":"Lori Passmore","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29B12.06c","SPCC18.06c","SPAC57A7.04c","SPAC1B3.05","SPCC31H12.08c","SPAC16C9.04c","SPCC4G3.15c","SPAC20G8.06"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-12-17"},{"uniquename":"EMBL:AU007241","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007731","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4108061","title":"Mitosis in the fission yeast Schizosaccharomyces pombe: a comparative study with light and electron microscopy.","citation":"J Cell Sci 1971 Sep;9(2):475-507","abstract":"","authors":"McCully EK, Robinow CF","authors_abbrev":"McCully EK et al.","pubmed_publication_date":"Sep 1971","pubmed_entrez_date":"1971-09-01","publication_year":"1971","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42014854","title":"Chromosome fusion enhances dependency on Rif1 for entanglement resolution during meiosis in S. pombe.","citation":"Commun Biol 2026 Apr 22;","abstract":"Chromosome fusion represents a major form of karyotype evolution. However, it remains unclear how cells adapt to drastic changes in chromosomal organisation and overcome the topological challenges imposed by fusion to ensure accurate segregation, genome stability, and genome function. Here, we report that in the fission yeast Schizosaccharomyces pombe, nascently fused chromosomes exhibit elevated entanglements during meiosis due to the accumulation of recombination intermediates, which are eventually resolved in late anaphase I with high fidelity. Notably, loss of the conserved replication/repair factor Rif1 increases the frequency of these entanglements, revealing a meiotic role for Rif1 in promoting efficient resolution of recombination-derived DNA bridges, particularly in the context of chromosome fusion. Moreover, the delayed mid-region nuclear envelope breakdown observed in anaphase I appears to provide an extended time window and stable intranuclear environment for resolution, thereby ensuring faithful segregation of the fused chromosomes. Together, our findings uncover a heightened dependence of cells with altered karyotypes on DNA repair machinery and suggest that adaptive regulation of entanglement resolution safeguards genome integrity during karyotype evolution.","doi":"10.1038/s42003-026-10093-3","authors":"Zhou Y, Wei X, Zhang J, Gu X, Gong W, Zhou J, Li W, He X","authors_abbrev":"Zhou Y et al.","pubmed_publication_date":"22 Apr 2026","pubmed_entrez_date":"2026-04-21","publication_year":"2026","canto_session_key":"e9327b135b678f29","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:812699","title":"The effect of 8-hydroxyquinoline on enzyme synthesis in the fission yeast Schizosaccharomyces pombe.","citation":"Eur J Biochem 1975 Dec 15;60(2):487-93","abstract":"The effect of 8-hydroxyquinoline, a rapid inhibitor of RNA synthesis, was followed on the activity of a number of enzymes in cultures of the fission yeast Schizosaccharomyces pombe. Two types of effect were found. In the first the activity continued to rise for a period and then remained constant. This occurred with alkaline phosphatase, basal and derepressed acid phosphatase, hexokinase, and derepressed sucrase and maltase at low cell density. It is consistent with control being exercised by an unstable mRNA or by an unstable stimulator of translocation. In the second the activity increased above the control values for several hours. This occurred with basal sucrase and maltase, and suggests a stable mRNA and an unstable inhibitor of translation. The extent of 'superproduction' of sucrase varied with cell density and with growth medium and this may be due to differences in the degree of translational inhibition. The possiblilty of a stable mRNA has interesting implications for the control of enzyme synthesis through the cell cycle.","authors":"Creanor J, May JW, Mitchison JM","authors_abbrev":"Creanor J et al.","pubmed_publication_date":"15 Dec 1975","pubmed_entrez_date":"1975-12-15","publication_year":"1975","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19685316","title":"Analysis of Schizosaccharomyces pombe meiosis by nuclear spreading.","citation":"Methods Mol Biol 2009;558:15-36","abstract":"The fission yeast, Schizosaccharomyces pombe, much like the budding yeast, is a particularly well-suited model organism for genetic research. However, the miniscule size of both yeasts' nuclei has hindered their success as research models for cytologists. A solution to this problem is provided by the spreading of nuclei, which increases their volume and allows for a better spatial resolution of nuclear contents. Here we describe nuclear spreading in fission yeast. Spreading of meiotic nuclei is particularly helpful in exposing the linear elements (LinEs), which are the fission yeasts' rudimentary version of the synaptonemal complex. Although the LinEs' role is still not fully understood, they serve as important meiotic hallmarks and their presence and morphology can be used in characterizing meiotic mutants. We first describe methods to induce meiosis in liquid cell cultures, then outline a method to break down cell and nuclear membranes by detergent treatment to release chromatin on cytological slides, and finally provide a set of protocols for analyzing these nuclei by immunostaining and fluorescence in situ hybridization (FISH), and by electron microscopy.","doi":"10.1007/978-1-60761-103-5_2","authors":"Loidl J, Lorenz A","authors_abbrev":"Loidl J et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-08-18","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11686297","title":"Intracellular pH homeostasis during cell-cycle progression and growth state transition in Schizosaccharomyces pombe.","citation":"J Cell Sci 2001 Aug;114(Pt 16):2929-41","abstract":"Accurate measurement of intracellular pH in unperturbed cells is fraught with difficulty. Nevertheless, using a variety of methods, intracellular pH oscillations have been reported to play a regulatory role in the control of the cell cycle in several eukaryotic systems. Here, we examine pH homeostasis in Schizosaccharomyces pombe using a non-perturbing ratiometric pH sensitive GFP reporter. This method allows for accurate intracellular pH measurements in living, entirely undisturbed, logarithmically growing cells. In addition, the use of a flow cell allows internal pH to be monitored in real time during nutritional, or growth state transition. We can find no evidence for cell-cycle-related changes in intracellular pH. By contrast, all data are consistent with a very tight homeostatic regulation of intracellular pH near 7.3 at all points in the cell cycle. Interestingly, pH set point changes are associated with growth state. Spores, as well as vegetative cells starved of either nitrogen, or a carbon source, show a marked reduction in their internal pH compared with logarithmically growing vegetative cells. However, in both cases, homeostatic regulation is maintained.","authors":"Karagiannis J, Young PG","authors_abbrev":"Karagiannis J et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-11-01","publication_year":"2001","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30600397","title":"Recruitment, loading, and activation of the Smc5-Smc6 SUMO ligase.","citation":"Curr Genet 2019 Jun;65(3):669-676","abstract":"Duplication of the genome poses one of the most significant threats to genetic integrity, cellular fitness, and organismal health. Therefore, numerous mechanisms have evolved that maintain replication fork stability in the face of DNA damage and allow faithful genome duplication. The fission yeast BRCT-domain-containing protein Brc1, and its budding yeast orthologue Rtt107, has emerged as a \"hub\" factor that integrates multiple replication fork protection mechanisms. Notably, the cofactors and pathways through which Brc1, Rtt107, and their human orthologue (PTIP) act have appeared largely distinct. This either represents true evolutionary functional divergence, or perhaps an incomplete genetic and biochemical analysis of each protein. In this regard, we recently showed that like Rtt107, Brc1 supports key functions of the Smc5-Smc6 complex, including its recruitment into DNA repair foci, chromatin association, and SUMO ligase activity. Furthermore, fission yeast cells lacking the Nse5-Nse6 genome stability factor were found to exhibit defects in Smc5-Smc6 function, similar to but more severe than those in cells lacking Brc1. Here, we place these findings in context with the known functions of Brc1, Rtt107, and Smc5-Smc6, present data suggesting a role for acetylation in Smc5-Smc6 chromatin loading, and discuss wider implications for genome stability.","doi":"10.1007/s00294-018-0922-9","authors":"Oravcová M, Boddy MN","authors_abbrev":"Oravcová M et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-01-03","publication_year":"2019","canto_session_key":"dc6364e1fbce4916","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-01-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11E3.08c","SPBC582.05c","SPBC651.10","SPCC5E4.06","SPAC14C4.02c"],"gene_count":5,"ltp_gene_count":0},{"uniquename":"PMID:24911838","title":"Functional conservation of coenzyme Q biosynthetic genes among yeasts, plants, and humans.","citation":"PLoS One 2014;9(6):e99038","abstract":"Coenzyme Q (CoQ) is an essential factor for aerobic growth and oxidative phosphorylation in the electron transport system. The biosynthetic pathway for CoQ has been proposed mainly from biochemical and genetic analyses of Escherichia coli and Saccharomyces cerevisiae; however, the biosynthetic pathway in higher eukaryotes has been explored in only a limited number of studies. We previously reported the roles of several genes involved in CoQ synthesis in the fission yeast Schizosaccharomyces pombe. Here, we expand these findings by identifying ten genes (dps1, dlp1, ppt1, and coq3-9) that are required for CoQ synthesis. CoQ10-deficient S. pombe coq deletion strains were generated and characterized. All mutant fission yeast strains were sensitive to oxidative stress, produced a large amount of sulfide, required an antioxidant to grow on minimal medium, and did not survive at the stationary phase. To compare the biosynthetic pathway of CoQ in fission yeast with that in higher eukaryotes, the ability of CoQ biosynthetic genes from humans and plants (Arabidopsis thaliana) to functionally complement the S. pombe coq deletion strains was determined. With the exception of COQ9, expression of all other human and plant COQ genes recovered CoQ10 production by the fission yeast coq deletion strains, although the addition of a mitochondrial targeting sequence was required for human COQ3 and COQ7, as well as A. thaliana COQ6. In summary, this study describes the functional conservation of CoQ biosynthetic genes between yeasts, humans, and plants.","doi":"10.1371/journal.pone.0099038","authors":"Hayashi K, Ogiyama Y, Yokomi K, Nakagawa T, Kaino T, Kawamukai M","authors_abbrev":"Hayashi K et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-06-10","publication_year":"2014","canto_session_key":"80d942a640ec9e5a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-21 16:28:57","canto_approved_date":"2024-09-08 11:34:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-21 16:28:47","canto_added_date":"2014-06-10 10:58:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":113,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.12","SPBC2D10.18","SPCC4G3.04c","SPAC1687.12c","SPCC162.05","SPBPJ4664.01","SPAC19G12.12","SPAC56F8.04c","SPBC337.15c","SPAC19G12.11"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2016-10-21"},{"uniquename":"PMID:27851962","title":"Reconstitution of Targeted Deadenylation by the Ccr4-Not Complex and the YTH Domain Protein Mmi1.","citation":"Cell Rep 2016 Nov 15;17(8):1978-1989","abstract":"Ccr4-Not is a conserved protein complex that shortens the 3' poly(A) tails of eukaryotic mRNAs to regulate transcript stability and translation into proteins. RNA-binding proteins are thought to facilitate recruitment of Ccr4-Not to certain mRNAs, but lack of an in-vitro-reconstituted system has slowed progress in understanding the mechanistic details of this specificity. Here, we generate a fully recombinant Ccr4-Not complex that removes poly(A) tails from RNA substrates. The intact complex is more active than the exonucleases alone and has an intrinsic preference for certain RNAs. The RNA-binding protein Mmi1 is highly abundant in preparations of native Ccr4-Not. We demonstrate a high-affinity interaction between recombinant Ccr4-Not and Mmi1. Using in vitro assays, we show that Mmi1 accelerates deadenylation of target RNAs. Together, our results support a model whereby both RNA-binding proteins and the sequence context of mRNAs influence deadenylation rate to regulate gene expression.","doi":"10.1016/j.celrep.2016.10.066","authors":"Stowell JAW, Webster MW, Kögel A, Wolf J, Shelley KL, Passmore LA","authors_abbrev":"Stowell JAW et al.","pubmed_publication_date":"15 Nov 2016","pubmed_entrez_date":"2016-11-17","publication_year":"2016","canto_session_key":"6b6f6a7ce48fd8e7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-12-18 20:25:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-18 20:25:17","canto_added_date":"2016-12-01 22:29:21","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29B12.06c","SPAC20G8.06","SPCC18.06c","SPCC4G3.15c","SPAC1B3.05","SPAC16C9.04c","SPCC736.12c","SPCC31H12.08c","SPBC29A10.14"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-12-18"},{"uniquename":"PMID:28250213","title":"Large-Scale Purification of Small Ubiquitin-Like Modifier (SUMO)-Modified Proteins from  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Mar 01;2017(3):pdb.prot091603","abstract":"Covalent protein modification by sumoylation (i.e., addition of small ubiquitin-like modifiers [SUMOs]) regulates a broad spectrum of critical functions in eukaryotic cells; however, usually ≤1% of a given protein is modified as a result of the highly dynamic nature of sumoylation. As such, capturing and identifying sumoylated proteins are both important in biological studies and very challenging tasks. Here we report a tailored purification protocol that includes rapid and complete cell disruption, coupled to highly stringent isolation of sumoylated proteins. Proteins purified using this protocol are compatible with common downstream applications such as western and mass spectrometry analyses. This protocol will work equally well to study other key covalent modifiers such as ubiquitin and Ned8.","doi":"10.1101/pdb.prot091603","authors":"Nie M, Boddy MN","authors_abbrev":"Nie M et al.","pubmed_publication_date":"01 Mar 2017","pubmed_entrez_date":"2017-03-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-03-04 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27677791","title":"CAG Expansions Are Genetically Stable and Form Nontoxic Aggregates in Cells Lacking Endogenous Polyglutamine Proteins.","citation":"mBio 2016 Sep 27;7(5)","abstract":"Proteins containing polyglutamine (polyQ) regions are found in almost all eukaryotes, albeit with various frequencies. In humans, proteins such as huntingtin (Htt) with abnormally expanded polyQ regions cause neurodegenerative diseases such as Huntington's disease (HD). To study how the presence of endogenous polyQ aggregation modulates polyQ aggregation and toxicity, we expressed polyQ expanded Htt fragments (polyQ Htt) in Schizosaccharomyces pombe In stark contrast to other unicellular fungi, such as Saccharomyces cerevisiae, S. pombe is uniquely devoid of proteins with more than 10 Q repeats. We found that polyQ Htt forms aggregates within S. pombe cells only with exceedingly long polyQ expansions. Surprisingly, despite the presence of polyQ Htt aggregates in both the cytoplasm and nucleus, no significant growth defect was observed in S. pombe cells. Further, PCR analysis showed that the repetitive polyQ-encoding DNA region remained constant following transformation and after multiple divisions in S. pombe, in contrast to the genetic instability of polyQ DNA sequences in other organisms. These results demonstrate that cells with a low content of polyQ or other aggregation-prone proteins can show a striking resilience with respect to polyQ toxicity and that genetic instability of repetitive DNA sequences may have played an important role in the evolutionary emergence and exclusion of polyQ expansion proteins in different organisms.\nPolyglutamine (polyQ) proteins encoded by repetitive CAG DNA sequences serve a variety of normal biological functions. Yet some proteins with abnormally expanded polyQ regions cause neurodegeneration through unknown mechanisms. To study how distinct cellular environments modulate polyQ aggregation and toxicity, we expressed CAG-expanded huntingtin fragments in Schizosaccharomyces pombe In stark contrast to many other eukaryotes, S. pombe is uniquely devoid of proteins containing long polyQ tracts. Our results show that S. pombe cells, despite their low content of endogenous polyQ proteins, exhibit striking and unexpected resilience with respect to polyQ toxicity and that genetic instability of repetitive DNA sequences may have played an important role in the emergence and expansion of polyQ domains in eukaryotic evolution.","doi":"10.1128/mBio.01367-16","authors":"Zurawel AA, Kabeche R, DiGregorio SE, Deng L, Menon KM, Opalko H, Duennwald ML, Moseley JB, Supattapone S","authors_abbrev":"Zurawel AA et al.","pubmed_publication_date":"27 Sep 2016","pubmed_entrez_date":"2016-09-29","publication_year":"2016","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2016-10-01 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42112669","title":"Recombination shapes the diversification of the  wtf  meiotic drivers.","citation":"Elife 2026 May 11;13","abstract":"Meiotic drivers are selfish genetic elements that distort fair segregation. The  wtf  genes are poison-antidote meiotic drivers that are experiencing rapid diversification in fission yeasts. However, gene duplication alone is insufficient to drive the diversification of  wtf  genes, given the poison encoded by a newly duplicated  wtf  gene can be detoxified by the antidote encoded by the original  wtf  gene. Here, we analyze the evolution of  wtf  genes across 21 strains of  Schizosaccharomyces pombe . Knocking out each of 25  wtf  genes in  S. pombe  strain 972h- separately does not attenuate the yeast growth, indicating that the  wtf  genes might be largely neutral to their carriers in asexual life cycle. Interestingly,  wtf  genes underwent recurrent and intricate recombination. As proof of principle, we generate a novel meiotic driver through artificial recombination between  wtf  drivers, and its encoded poison cannot be detoxified by the antidotes encoded by their parental  wtf  genes but can be detoxified by its own antidote. Therefore, we propose that recombination can generate new meiotic drivers and thus shape the diversification of the  wtf  drivers.","doi":"10.7554/eLife.100638","authors":"Wang Y, Xu H, He Q, Wu Z, Gong Z, Han GZ","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"11 May 2026","pubmed_entrez_date":"2026-05-11","publication_year":"2026","canto_session_key":"a43f14eda4ee99be","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-05-11 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25454595","title":"Organellar mechanosensitive channels involved in hypo-osmoregulation in fission yeast.","citation":"Cell Calcium 2014 Dec;56(6):467-71","abstract":"MscS and MscL, bacterial mechanosensitive channels, play crucial roles in the hypo-osmotic shock response. However, only MscS has homologs in eukaryotes. These homologs are called MscS-like proteins or MSL proteins. MSL proteins have changed both structurally and functionally during evolution and are now localized not only to the membrane of the chloroplast, which is thought to be a descendant of an ancient, free-living bacterium, but also the cell membrane and the endoplasmic reticulum (ER) membrane, suggesting that the role of MSL proteins has diverged. In this brief review, we mainly focus on two MSL proteins in the fission yeast Schizosaccharomyces pombe that are localized in the ER membrane and protect cells from hypo-osmotic shock-induced death by regulating intracellular Ca(2+) concentrations. We also discuss Arabidopsis thaliana MSL proteins and other yeast ion channels in terms of osmoregulation in eukaryotes.","doi":"10.1016/j.ceca.2014.10.001","authors":"Nakayama Y, Iida H","authors_abbrev":"Nakayama Y et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-12-03","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-12-04 01:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6230352","title":"Isolation of the structural genes for the alpha and beta subunits of the mitochondrial ATPase from the fission yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1984 Mar 10;259(5):2840-4","abstract":"The structural genes for the two major subunits of the mitochondrial ATPase were isolated among genomic clones from the yeast Schizosaccharomyces pombe by transformation and complementation of mutants unable to grow on glycerol and lacking either the alpha or the beta subunits. The plasmid pMa1 containing a 2.3-kilobase genomic insert transformed the mutant A23-13 lacking a detectable alpha subunit. The transformant grew on glycerol and contained an alpha subunit of normal electrophoretic mobility. The plasmid pMa2 containing a 5.4-kilobase genomic insert transformed the mutant B59-1 lacking the beta subunit. The transformant grew on glycerol and contained a beta subunit of normal mobility. The structural gene for the beta ATPase subunit for the fission yeast S. pombe was localized within the pMa2 insert by hybridization to a probe containing the beta ATPase gene from the budding yeast Saccharomyces cerevisiae (Saltzgaber, J., Kunapuli, S., and Douglas, M. G. (1983) J. Biol. Chem. 258, 11465-11470). The mRNAs which hybridized to pMa1 and pMa2 were translated by a reticulocyte lysate into polypeptides of Mr = 59,000 and 54,000, respectively. These genes products reacted with an anti-F1-ATPase serum and therefore correspond most probably to precursors of the alpha and beta subunits.","authors":"Boutry M, Vassarotti A, Ghislain M, Douglas M, Goffeau A","authors_abbrev":"Boutry M et al.","pubmed_publication_date":"10 Mar 1984","pubmed_entrez_date":"1984-03-10","publication_year":"1984","canto_session_key":"85cf0f0a98b2a98d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-31 08:48:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-31 08:47:54","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-03-31"},{"uniquename":"PANTHER:PTHR31576","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.09c","HGNC:11533"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11243781","title":"Fission yeast nascent polypeptide-associated complex binds to four-way DNA junctions.","citation":"J Mol Biol 2001 Mar 02;306(4):703-16","abstract":"The four-way DNA junction (X-junction) is both a central intermediate of recombination reactions and, in some cases, a controlling element in transcription and the initiation of DNA replication. Many different proteins have been found to bind to X-junctions in a structure-specific manner. In some cases, this ability only reflects the proteins' general predilection for distorted DNAs but in others the interaction is highly specific and usually signifies that the X-junction is the real target for the protein in vivo. Here we identify the Schizosaccharomyces pombe (Sp) nascent polypeptide associated complex (NAC) as a potent binder of X-junction DNA. NAC is highly conserved in eukaryotes and has reported functions in transcription and the targeting of proteins within the cytosol. NAC is composed of alpha and beta subunits. Each SpNAC subunit has the capacity to bind X-junction DNA, but optimal binding depends on a heterodimer of subunits. Competition assays and binding comparisons using a range of different DNA substrates reveal that SpNAC is highly selective for the X-junction structure. By comparative gel electrophoresis we show that the X-junction is held in its open square conformation when bound by SpNAC. Junction binding is inhibited by concentrations of magnesium ions that are sufficient to \"stack\" the X-junction, suggesting that SpNAC recognises only the open junction structure. Finally, SpNAC can bind to X-junctions that are already bound by a tetramer of the Escherichia coli RuvA protein, indicating that it interacts with only one face of the junction. The possible biological significance of X-junction binding by SpNAC is discussed.","authors":"Whitby MC, Dixon J","authors_abbrev":"Whitby MC et al.","pubmed_publication_date":"02 Mar 2001","pubmed_entrez_date":"2001-03-13","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24506453","title":"The RNA-binding protein Spo5 promotes meiosis II by regulating cyclin Cdc13 in fission yeast.","citation":"Genes Cells 2014 Mar;19(3):225-38","abstract":"Meiosis comprises two consecutive nuclear divisions, meiosis I and II. Despite this unique progression through the cell cycle, little is known about the mechanisms controlling the sequential divisions. In this study, we carried out a genetic screen to identify factors that regulate the initiation of meiosis II in the fission yeast Schizosaccharomyces pombe. We identified mutants deficient in meiosis II progression and repeatedly isolated mutants defective in spo5, which encodes an RNA-binding protein. Using fluorescence microscopy to visualize YFP-tagged protein, we found that spo5 mutant cells precociously lost Cdc13, the major B-type cyclin in fission yeast, before meiosis II. Importantly, the defect in meiosis II was rescued by increasing CDK activity. In wild-type cells, cdc13 transcripts increased during meiosis II, but this increase in cdc13 expression was weaker in spo5 mutants. Thus, Spo5 is a novel regulator of meiosis II that controls the level of cdc13 expression and promotes de novo synthesis of Cdc13. We previously reported that inhibition of Cdc13 degradation is necessary to initiate meiosis II; together with the previous information, the current findings indicate that the dual control of Cdc13 by de novo synthesis and suppression of proteolysis ensures the progression of meiosis II.","doi":"10.1111/gtc.12133","authors":"Arata M, Sato M, Yamashita A, Yamamoto M","authors_abbrev":"Arata M et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-02-11","publication_year":"2014","canto_session_key":"5785ff817ea0cbc9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.03","SPCC18B5.03","SPBC11B10.09","SPBC29A10.02","SPAC5D6.08c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:3244367","title":"U2 small nuclear RNA is remarkably conserved between Schizosaccharomyces pombe and mammals.","citation":"Mol Cell Biol 1988 Dec;8(12):5575-80","abstract":"We report the molecular cloning and sequencing of the most abundant trimethylguanosine-capped small nuclear RNA from the fission yeast Schizosaccharomyces pombe, a highly conserved homolog of mammalian U2 small nuclear RNA. This RNA is 186 nucleotides in length, just 2 nucleotides shorter than its human counterpart; this is in contrast to Saccharomyces cerevisiae U2, which is 1,175 nucleotides long. Moreover, the secondary structure of Schizosaccharomyces pombe U2 is virtually identical to that of mammalian U2, including the 3' half of the RNA, which shows limited primary sequence identity. Northern (RNA) blot analysis revealed that the size of this RNA is conserved not only in fission yeasts but in many organisms, including other ascomycetes.","authors":"Brennwald P, Porter G, Wise JA","authors_abbrev":"Brennwald P et al.","pubmed_publication_date":"Dec 1988","pubmed_entrez_date":"1988-12-01","publication_year":"1988","canto_session_key":"911ee9ca1b28aa22","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-19 13:26:20","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-19 13:25:59","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.02"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-19"},{"uniquename":"PMID:34198697","title":"Specific Functional Features of the Cell Integrity MAP Kinase Pathway in the Dimorphic Fission Yeast  Schizosaccharomyces japonicus .","citation":"J Fungi (Basel) 2021 Jun 14;7(6)","abstract":"Mitogen activated protein kinase (MAPK) signaling pathways execute essential functions in eukaryotic organisms by transducing extracellular stimuli into adaptive cellular responses. In the fission yeast model  Schizosaccharomyces pombe  the cell integrity pathway (CIP) and its core effector, MAPK Pmk1, play a key role during regulation of cell integrity, cytokinesis, and ionic homeostasis.  Schizosaccharomyces japonicus , another fission yeast species, shows remarkable differences with respect to  S. pombe , including a robust yeast to hyphae dimorphism in response to environmental changes. We show that the CIP MAPK module architecture and its upstream regulators, PKC orthologs Pck1 and Pck2, are conserved in both fission yeast species. However, some of  S. pombe 's CIP-related functions, such as cytokinetic control and response to glucose availability, are regulated differently in  S. japonicus.  Moreover, Pck1 and Pck2 antagonistically regulate  S. japonicus  hyphal differentiation through fine-tuning of Pmk1 activity. Chimeric MAPK-swapping experiments revealed that  S. japonicus  Pmk1 is fully functional in  S. pombe , whereas  S. pombe  Pmk1 shows a limited ability to execute CIP functions and promote  S. japonicus  mycelial development. Our findings also suggest that a modified N-lobe domain secondary structure within  S. japonicus  Pmk1 has a major influence on the CIP signaling features of this evolutionarily diverged fission yeast.","doi":"10.3390/jof7060482","authors":"Gómez-Gil E, Franco A, Vázquez-Marín B, Prieto-Ruiz F, Pérez-Díaz A, Vicente-Soler J, Madrid M, Soto T, Cansado J","authors_abbrev":"Gómez-Gil E et al.","pubmed_publication_date":"14 Jun 2021","pubmed_entrez_date":"2021-07-02","publication_year":"2021","canto_session_key":"4b104f39c2d5ae0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elisa Gómez Gil","canto_first_approved_date":"2024-07-03 16:02:00","canto_approved_date":"2024-07-03 16:03:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-01 20:53:27","canto_added_date":"2021-07-04 00:15:05","annotation_curators":[{"name":"Elisa Gómez Gil","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.14c","SPBC12D12.04c","SPBC119.08"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2024-07-03"},{"uniquename":"PMID:1644306","title":"Cloning and regulation of Schizosaccharomyces pombe thi2, a gene involved in thiamine biosynthesis.","citation":"Gene 1992 Aug 01;117(1):141-3","abstract":"Biosyntheses of the pyrimidine and thiazole moieties of the thiamine molecule occur by separate pathways. In Schizosaccharomyces pombe, a gene, thi2, is responsible for thiazole synthesis [Schweingruber et al., Curr. Genet. 19 (1991) 249-254]. We have cloned a 3.1-kb genomic S. pombe fragment which can functionally complement a thi2 mutant. The fragment maps genetically at the thi2 site, indicating that it carries thi2. As shown by Northern hybridization analysis, the appearance of thi2 mRNA levels is repressed when cells are grown in the presence of thiamine and 5-(2-hydroxyethyl)-4-methylthiazole. The thi3 gene involved in the biosynthesis of the pyrimidine moiety, is also regulated by thiamine [Maundrell, J. Biol. Chem. 265 (1990) 10857-10864; Schweingruber et al., Curr. Genet. 19 (1991) 249-254]. We previously identified and analyzed four regulatory genes (tnr1, tnr2, tnr3, and thi1) that are responsible for the regulation of thi3 [Schweingruber et al., Genetics (1992) in press]. Mutants defective in these regulatory genes affect expression of thi2 in a similar way to thi3. This indicates that biosynthesis of the pyrimidine and thiazole moieties are under common genetic control in S. pombe.","authors":"Zurlinden A, Schweingruber ME","authors_abbrev":"Zurlinden A et al.","pubmed_publication_date":"01 Aug 1992","pubmed_entrez_date":"1992-08-01","publication_year":"1992","canto_session_key":"1b8ed217ce984ab5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-07 22:02:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-07 22:02:50","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.01","SPAC6F12.05c","SPAC1486.10"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-01-07"},{"uniquename":"EMBL:AU010822","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34524082","title":"SUV39 SET domains mediate crosstalk of heterochromatic histone marks.","citation":"Elife 2021 Sep 15;10","abstract":"The SUV39 class of methyltransferase enzymes deposits histone H3 lysine 9 di- and trimethylation (H3K9me2/3), the hallmark of constitutive heterochromatin. How these enzymes are regulated to mark specific genomic regions as heterochromatic is poorly understood. Clr4 is the sole H3K9me2/3 methyltransferase in the fission yeast  Schizosaccharomyces pombe,  and recent evidence suggests that ubiquitination of lysine 14 on histone H3 (H3K14ub) plays a key role in H3K9 methylation. However, the molecular mechanism of this regulation and its role in heterochromatin formation remain to be determined. Our structure-function approach shows that the H3K14ub substrate binds specifically and tightly to the catalytic domain of Clr4, and thereby stimulates the enzyme by over 250-fold. Mutations that disrupt this mechanism lead to a loss of H3K9me2/3 and abolish heterochromatin silencing similar to  clr4  deletion. Comparison with mammalian SET domain proteins suggests that the Clr4 SET domain harbors a conserved sensor for H3K14ub, which mediates licensing of heterochromatin formation.","doi":"10.7554/eLife.62682","authors":"Stirpe A, Guidotti N, Northall SJ, Kilic S, Hainard A, Vadas O, Fierz B, Schalch T","authors_abbrev":"Stirpe A et al.","pubmed_publication_date":"15 Sep 2021","pubmed_entrez_date":"2021-09-15","publication_year":"2021","canto_session_key":"b419f152633d75f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Thomas Schalch","canto_first_approved_date":"2021-11-08 14:49:44","canto_approved_date":"2025-04-18 08:51:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-11-04 09:52:31","canto_added_date":"2021-09-17 00:15:03","annotation_curators":[{"name":"Thomas Schalch","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC212.11","SPAC1834.04","SPCC11E10.08","SPBC1105.11c","SPBC428.08c","SPBC8D2.04"],"gene_count":6,"ltp_gene_count":1,"approved_date":"2021-11-08","pdb_entries":[{"pdb_id":"6z2a","gene_chains":[{"gene_uniquename":"SPBC428.08c","chain":"A/B","position":"196-489"}],"title":"Structure of Clr4 mutant - F256A/F310A/F427A bound to SAH","entry_authors":"Stirpe A,Schalch T","entry_authors_abbrev":"Stirpe A et al.","reference_uniquename":"PMID:34524082","experimental_method":"X-ray","resolution":"2.456"}]},{"uniquename":"PMID:41850284","title":"Arp2/3-dependent actin assembly shapes endosomes and promotes intracellular trafficking in fission yeast.","citation":"Curr Biol 2026 Mar 17;","abstract":"Endosomes serve as crucial sorting centers that streamline the distribution of cell surface proteins. The early endosome receives traffic from both the plasma membrane (PM) and the Golgi and orchestrates the redistribution of cargoes for recycling to the PM or through retrograde movement to the Golgi, and for degradation to late endosomes and lysosomes. 1  In animal cells and amoebas, Arp2/3-complex-mediated F-actin assembly plays critical roles in many aspects of endosome function, promoting both recycling and degradative trafficking routes. 2  Yeast models, which allowed dissection of the major membrane trafficking routes, 3  exhibit highly simplified endosomes, as shown in Saccharomyces cerevisiae, where the trans-Golgi network (TGN) functions as recycling endosome. 4  Furthermore, there is no reported role for Arp2/3 complex or F-actin in endomembrane remodeling in yeast cells, which lack Arp2/3 complex activators that function on animal endosomes. 5  ,  6  Here, we examine the role of the Arp2/3 complex in the shape and function of fission yeast Schizosaccharomyces pombe endosomes. Through live imaging and correlative light electron tomography, we describe endosomes as dynamic tubulo-cisternal compartments, whose morphology requires branched actin, as inhibition of the Arp2/3 complex leads to endosome rounding. Though branched actin primarily localizes to endocytic patches, we show localization of the Arp2/3 complex and F-actin at endosomes for short bursts of time. Remarkably, Arp2/3-dependent actin assembly is critical to allow retrograde trafficking from the endosome to the degradative vacuole. Thus, Arp2/3-complex-dependent actin assembly has a deeply conserved role in shaping and promoting the function of the endomembrane trafficking system.","doi":"10.1016/j.cub.2026.02.030","authors":"Melero A, Basante-Bedoya M, Muriel-Lopez O, Martin SG","authors_abbrev":"Melero A et al.","pubmed_publication_date":"17 Mar 2026","pubmed_entrez_date":"2026-03-18","publication_year":"2026","canto_session_key":"c0bca5a26b05a241","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2026-03-27 13:01:53","canto_approved_date":"2026-04-01 12:01:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-03-25 09:37:52","canto_added_date":"2026-03-20 00:25:06","annotation_curators":[{"name":"Sophie Martin","community_curator":true,"annotation_count":5,"orcid":"0000-0002-5317-2557","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11H11.06","SPAC630.03","SPAC30.01c","SPBC20F10.07","SPAC6G9.11","SPAC17G8.04c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2026-03-27"},{"uniquename":"EMBL:SPD220","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19198588","title":"A complex gene regulatory mechanism that operates at the nexus of multiple RNA processing decisions.","citation":"Nat Struct Mol Biol 2009 Mar;16(3):255-64","abstract":"Expression of crs1 pre-mRNA, encoding a meiotic cyclin, is blocked in actively growing fission yeast cells by a multifaceted mechanism. The most striking feature is that in vegetative cells, crs1 transcripts are continuously synthesized but are targeted for degradation rather than splicing and polyadenylation. Turnover of crs1 RNA requires the exosome, as do previously described nuclear surveillance and silencing mechanisms, but does not involve a noncanonical poly(A) polymerase. Instead, crs1 transcripts are targeted for destruction by a factor previously implicated in turnover of meiotic RNAs in growing cells. Like exosome mutants, mmi1 mutants splice and polyadenylate vegetative crs1 transcripts. Two regulatory elements are located at the 3' end of the crs1 gene, consistent with the increased accumulation of spliced RNA in polyadenylation factor mutants. This highly integrated regulatory strategy may ensure a rapid response to adverse conditions, thereby guaranteeing survival.","doi":"10.1038/nsmb.1556","authors":"McPheeters DS, Cremona N, Sunder S, Chen HM, Averbeck N, Leatherwood J, Wise JA","authors_abbrev":"McPheeters DS et al.","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2009-02-10","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4255493","title":"Induction synchrony in the fission yeast. Schizosaccharomyces pombe.","citation":"Exp Cell Res 1971 Aug;67(2):368-74","abstract":"","authors":"Mitchison JM, Creanor J","authors_abbrev":"Mitchison JM et al.","pubmed_publication_date":"Aug 1971","pubmed_entrez_date":"1971-08-01","publication_year":"1971","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5473904","title":"Segregational respiratory-deficient mutants of a \"petite negative\" yeast Schizosaccharomyces pombe 972h-.","citation":"J Bacteriol 1970 Oct;104(1):482-91","abstract":"No viable respiratory-deficient mutants of Schizosaccharomyces pombe 972h(-) could be obtained by acriflavine and ethidium bromide treatments. These mutagens induce 15 to 70% of microcolonies which, after a growth-lag of a few days, further develop into normal, respiratory-competent colonies. These results suggest that unstable petites were induced. Segregational respiratory-deficient mutants resistant to cobalt sulfate inhibition were isolated. Some of these strains are deficient in cytochrome a + a(3) and respire at low rates. The morphology of their mitochondrial membranes is modified: either the cristae are absent or they show aberrant concentric or tubular structures. Segregational mutants resistant to the respiratory inhibitors, 2,4-dinitrophenol or decamethylene diguanidine, were obtained. Neither mitochondrial structure nor function seems to be modified in these mutants. A segregational mutant resistant to benzimidazole inhibition does not grow on glycerol, although neither growth on glucose nor respiration appear to be affected.","authors":"Heslot H, Louis C, Goffeau A","authors_abbrev":"Heslot H et al.","pubmed_publication_date":"Oct 1970","pubmed_entrez_date":"1970-10-01","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26343758","title":"Mis16 Independently Recognizes Histone H4 and the CENP-ACnp1-Specific Chaperone Scm3sp.","citation":"J Mol Biol 2015 Oct 09;427(20):3230-3240","abstract":"CENP-A is a centromere-specific histone H3 variant that is required for kinetochore assembly and accurate chromosome segregation. For it to function properly, CENP-A must be specifically localized to centromeres. In fission yeast, Scm3sp and the Mis18 complex, composed of Mis16, Eic1, and Mis18, function as a CENP-A(Cnp1)-specific chaperone and a recruiting factor, respectively, and together ensure accurate delivery of CENP-A(Cnp1) to centromeres. Although how Scm3sp specifically recognizes CENP-A(Cnp1) has been revealed recently, the recruiting mechanism of CENP-A(Cnp1) via the Mis18 complex remains unknown. In this study, we have determined crystal structures of Schizosaccharomyces japonicus Mis16 alone and in complex with the helix 1 of histone H4 (H4α1). Crystal structures followed by mutant analysis and affinity pull-downs have revealed that Mis16 recognizes both H4α1 and Scm3sp independently within the CENP-A(Cnp1)/H4:Scm3sp complex. This observation suggests that Mis16 gains CENP-A(Cnp1) specificity by recognizing both Scm3sp and histone H4. Our studies provide insights into the molecular mechanisms underlying specific recruitment of CENP-A(Cnp1)/H4:Scm3sp into centromeres.","doi":"10.1016/j.jmb.2015.08.022","authors":"An S, Kim H, Cho US","authors_abbrev":"An S et al.","pubmed_publication_date":"09 Oct 2015","pubmed_entrez_date":"2015-09-08","publication_year":"2015","canto_session_key":"1955fa560c65ac30","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-09-09 00:19:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1834.03c","SPCC1672.10","SPAPB1A10.02"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:27714790","title":"TeloPCR-seq: a high-throughput sequencing approach for telomeres.","citation":"FEBS Lett 2016 Dec;590(23):4159-4170","abstract":"We have developed a high-throughput sequencing approach that enables us to determine terminal telomere sequences from tens of thousands of individual Schizosaccharomyces pombe telomeres. This method provides unprecedented coverage of telomeric sequence complexity in fission yeast. S. pombe telomeres are composed of modular degenerate repeats that can be explained by variation in usage of the TER1 RNA template during reverse transcription. Taking advantage of this deep sequencing approach, we find that 'like' repeat modules are highly correlated within individual telomeres. Moreover, repeat module preference varies with telomere length, suggesting that existing repeats promote the incorporation of like repeats and/or that specific conformations of the telomerase holoenzyme efficiently and/or processively add repeats of like nature. After the loss of telomerase activity, this sequencing and analysis pipeline defines a population of telomeres with altered sequence content. This approach will be adaptable to study telomeric repeats in other organisms and also to interrogate repetitive sequences throughout the genome that are inaccessible to other sequencing methods.","doi":"10.1002/1873-3468.12444","authors":"Bennett HW, Liu N, Hu Y, King MC","authors_abbrev":"Bennett HW et al.","pubmed_publication_date":"Dec 2016","pubmed_entrez_date":"2016-10-08","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-10-09 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33138913","title":"Atg43 tethers isolation membranes to mitochondria to promote starvation-induced mitophagy in fission yeast.","citation":"Elife 2020 Nov 03;9","abstract":"Degradation of mitochondria through mitophagy contributes to the maintenance of mitochondrial function. In this study, we identified that Atg43, a mitochondrial outer membrane protein, serves as a mitophagy receptor in the model organism  Schizosaccharomyces pombe  to promote the selective degradation of mitochondria. Atg43 contains an Atg8-family-interacting motif essential for mitophagy. Forced recruitment of Atg8 to mitochondria restores mitophagy in Atg43-deficient cells, suggesting that Atg43 tethers expanding isolation membranes to mitochondria. We found that the mitochondrial import factors, including the Mim1-Mim2 complex and Tom70, are crucial for mitophagy. Artificial mitochondrial loading of Atg43 bypasses the requirement of the import factors, suggesting that they contribute to mitophagy through Atg43. Atg43 not only maintains growth ability during starvation but also facilitates vegetative growth through its mitophagy-independent function. Thus, Atg43 is a useful model to study the mechanism and physiological roles, as well as the origin and evolution, of mitophagy in eukaryotes.","doi":"10.7554/eLife.61245","authors":"Fukuda T, Ebi Y, Saigusa T, Furukawa K, Yamashita SI, Inoue K, Kobayashi D, Yoshida Y, Kanki T","authors_abbrev":"Fukuda T et al.","pubmed_publication_date":"03 Nov 2020","pubmed_entrez_date":"2020-11-03","publication_year":"2020","canto_session_key":"3a3a0d9e76ed714d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomoyuki Fukuda","canto_first_approved_date":"2021-01-15 17:29:41","canto_approved_date":"2026-04-15 15:01:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-08 05:29:10","canto_added_date":"2020-11-05 01:15:05","annotation_curators":[{"name":"Tomoyuki Fukuda","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":60,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.07c","SPBC409.23","SPBC713.08","SPAC4A8.04","SPBC6B1.05c","SPAC14C4.01c","SPBP8B7.24c","SPAC6B12.12"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2021-01-15"},{"uniquename":"PMID:16094962","title":"Excision of pyrimidine dimers by several UV-sensitive mutants of S. pombe.","citation":"Mol Gen Genet 1975;136(1):1-8","abstract":"Nine radiation-sensitive mutants of S. pombe showing a variety of phenotypic characteristics were analysed for their ability to excise pyrimidine dimers after ultraviolet irradiation. From earlier studies using indirect parameters, it was expected that some would be excision-deficient. Data reported here show that all the mutants tested, like wild type cells, were able to remove a high percentage of pyrimidine dimers during post-irradiation incubation in several different holding media, but not in saline or phosphate buffer. These mutants included strains showing increased, as well as others which showed decreased, levels of UV-induced mutation frequency relative to that of the wild type at the same total dose.","authors":"Birnboim HC, Nasim A","authors_abbrev":"Birnboim HC et al.","pubmed_publication_date":"1975","pubmed_entrez_date":"1975-01-01","publication_year":"1975","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21983101","title":"Rpa43 and its partners in the yeast RNA polymerase I transcription complex.","citation":"FEBS Lett 2011 Nov 04;585(21):3355-9","abstract":"An Rpa43/Rpa14 stalk protrudes from RNA polymerase I (RNAPI), with homology to Rpb7/Rpb4 (RNAPII), Rpc25/Rpc17 (RNAPIII) and RpoE/RpoF (archaea). In fungi and vertebrates, Rpa43 contains hydrophilic domains forming about half of its size, but these domains lack in Schizosaccharomyces pombe and most other eukaryote lineages. In Saccharomyces cerevisiae, they can be lost with little or no growth effect, as shown by deletion mapping and by domain swapping with fission yeast, but genetically interact with rpa12Δ, rpa34Δ or rpa49Δ, lacking non-essential subunits important for transcript elongation. Two-hybrid data and other genetic evidence suggest that Rpa43 directly bind Spt5, an RNAPI elongation factor also acting in RNAPII-dependent transcription, and may also interact with the nucleosomal chaperone Spt6.","doi":"10.1016/j.febslet.2011.09.011","authors":"Beckouët F, Mariotte-Labarre S, Peyroche G, Nogi Y, Thuriaux P","authors_abbrev":"Beckouët F et al.","pubmed_publication_date":"04 Nov 2011","pubmed_entrez_date":"2011-10-11","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24858417","title":"Quality control of homologous recombination.","citation":"Cell Mol Life Sci 2014 Oct;71(19):3779-97","abstract":"Exogenous and endogenous genotoxic agents, such as ionizing radiation and numerous chemical agents, cause DNA double-strand breaks (DSBs), which are highly toxic and lead to genomic instability or tumorigenesis if not repaired accurately and efficiently. Cells have over evolutionary time developed certain repair mechanisms in response to DSBs to maintain genomic integrity. Major DSB repair mechanisms include non-homologous end joining and homologous recombination (HR). Using sister homologues as templates, HR is a high-fidelity repair pathway that can rejoin DSBs without introducing mutations. However, HR execution without appropriate guarding may lead to more severe gross genome rearrangements. Here we review current knowledge regarding the factors and mechanisms required for accomplishment of accurate HR.","doi":"10.1007/s00018-014-1649-5","authors":"Liu T, Huang J","authors_abbrev":"Liu T et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-05-27","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-11-12 01:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPO243276","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29601584","title":"2'-O-methylation of the mRNA cap protects RNAs from decapping and degradation by DXO.","citation":"PLoS One 2018;13(3):e0193804","abstract":"The 5' RNA cap structure (m7GpppRNA) is a key feature of eukaryotic mRNAs with important roles in stability, splicing, polyadenylation, mRNA export, and translation. Higher eukaryotes can further modify this minimal cap structure with the addition of a methyl group on the ribose 2'-O position of the first transcribed nucleotide (m7GpppNmpRNA) and sometimes on the adjoining nucleotide (m7GpppNmpNmpRNA). In higher eukaryotes, the DXO protein was previously shown to be responsible for both decapping and degradation of RNA transcripts harboring aberrant 5' ends such as pRNA, pppRNA, GpppRNA, and surprisingly, m7GpppRNA. It was proposed that the interaction of the cap binding complex with the methylated cap would prevent degradation of m7GpppRNAs by DXO. However, the critical role of the 2'-O-methylation found in higher eukaryotic cap structures was not previously addressed. In the present study, we demonstrate that DXO possesses both decapping and exoribonuclease activities toward incompletely capped RNAs, only sparing RNAs with a 2'-O-methylated cap structure. Fluorescence spectroscopy assays also revealed that the presence of the 2'-O-methylation on the cap structure drastically reduces the affinity of DXO for RNA. Moreover, immunofluorescence and structure-function assays also revealed that a nuclear localisation signal is located in the amino-terminus region of DXO. Overall, these results are consistent with a quality control mechanism in which DXO degrades incompletely capped RNAs.","doi":"10.1371/journal.pone.0193804","authors":"Picard-Jean F, Brand C, Tremblay-Létourneau M, Allaire A, Beaudoin MC, Boudreault S, Duval C, Rainville-Sirois J, Robert F, Pelletier J, Geiss BJ, Bisaillon M","authors_abbrev":"Picard-Jean F et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-03-31","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19D5.06c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:5857584","title":"Mutants of the yeast Schizosaccharomyces pombe requiring a high concentration of potassium.","citation":"Experientia 1964 Nov 15;20(11):638-9","abstract":"","authors":"Megnet R","authors_abbrev":"Megnet R","pubmed_publication_date":"15 Nov 1964","pubmed_entrez_date":"1964-11-15","publication_year":"1964","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26979837","title":"A simplified vector system for visualization of localized RNAs in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2016 Jul;80(7):1362-7","abstract":"RNA localization is an important event that is essential for the polarization and differentiation of a cell. Although several methods are currently used to detect localized RNAs, a simplified detection system has not yet been developed for Schizosaccharomyces pombe. In the present study, we describe a new vector system for the visualization of localized RNAs in S. pombe using a U1A-tag-GFP system. A pREP1-U1A-tag vector plasmid to express U1A-tagged RNA and a pREP2-U1AGFP plasmid to produce a U1A-GFP fusion protein were constructed for this system. Since the U1A-GFP protein binds U1A-tagged RNA, fluorescence is observed at the location of U1A-tagged RNA in cells expressing both of these. The nucleolar localization of U3 snoRNA was successfully detected using this system, and a novel RNA localized at the DNA region of the nucleus was found by screening localized RNAs. This system will accelerate the study of localized RNAs in S. pombe.","doi":"10.1080/09168451.2016.1158633","authors":"Takeuchi-Andoh T, Ohba S, Shinoda Y, Fuchita A, Hayashi S, Nishiyoshi E, Terouchi N, Tani T","authors_abbrev":"Takeuchi-Andoh T et al.","pubmed_publication_date":"Jul 2016","pubmed_entrez_date":"2016-03-17","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27903914","title":"Proteomic analysis of the human KEOPS complex identifies C14ORF142 as a core subunit homologous to yeast Gon7.","citation":"Nucleic Acids Res 2017 Jan 25;45(2):805-817","abstract":"The KEOPS/EKC complex is a tRNA modification complex involved in the biosynthesis of N 6 -threonylcarbamoyladenosine (t 6 A), a universally conserved tRNA modification found on ANN-codon recognizing tRNAs. In archaea and eukaryotes, KEOPS is composed of OSGEP/Kae1, PRPK/Bud32, TPRKB/Cgi121 and LAGE3/Pcc1. In fungi, KEOPS contains an additional subunit, Gon7, whose orthologs outside of fungi, if existent, remain unidentified. In addition to displaying defective t 6 A biosynthesis, Saccharomyces cerevisiae strains harboring KEOPS mutations are compromised for telomere homeostasis, growth and transcriptional co-activation. To identify a Gon7 ortholog in multicellular eukaryotes as well as to uncover KEOPS-interacting proteins that may link t 6 A biosynthesis to the diverse set of KEOPS mutant phenotypes, we conducted a proteomic analysis of human KEOPS. This work identified 152 protein interactors, one of which, C14ORF142, interacted strongly with all four KEOPS subunits, suggesting that it may be a core component of human KEOPS. Further characterization of C14ORF142 revealed that it shared a number of biophysical and biochemical features with fungal Gon7, suggesting that C14ORF142 is the human ortholog of Gon7. In addition, our proteomic analysis identified specific interactors for different KEOPS subcomplexes, hinting that individual KEOPS subunits may have additional functions outside of t 6 A biosynthesis.","doi":"10.1093/nar/gkw1181","authors":"Wan LC, Maisonneuve P, Szilard RK, Lambert JP, Ng TF, Manczyk N, Huang H, Laister R, Caudy AA, Gingras AC, Durocher D, Sicheri F","authors_abbrev":"Wan LC et al.","pubmed_publication_date":"25 Jan 2017","pubmed_entrez_date":"2016-12-02","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6B12.18","HGNC:20356"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22347452","title":"The SET domain protein, Set3p, promotes the reliable execution of cytokinesis in Schizosaccharomyces pombe.","citation":"PLoS One 2012;7(2):e31224","abstract":"In response to perturbation of the cell division machinery fission yeast cells activate regulatory networks that ensure the faithful completion of cytokinesis. For instance, when cells are treated with drugs that impede constriction of the actomyosin ring (low doses of Latrunculin A, for example) these networks ensure that cytokinesis is complete before progression into the subsequent mitosis. Here, we identify three previously uncharacterized genes, hif2, set3, and snt1, whose deletion results in hyper-sensitivity to LatA treatment and in increased rates of cytokinesis failure. Interestingly, these genes are orthologous to TBL1X, MLL5, and NCOR2, human genes that encode components of a histone deacetylase complex with a known role in cytokinesis. Through co-immunoprecipitation experiments, localization studies, and phenotypic analysis of gene deletion mutants, we provide evidence for an orthologous complex in fission yeast. Furthermore, in light of the putative role of the complex in chromatin modification, together with our results demonstrating an increase in Set3p levels upon Latrunculin A treatment, global gene expression profiles were generated. While this analysis demonstrated that the expression of cytokinesis genes was not significantly affected in set3Δ backgrounds, it did reveal defects in the ability of the mutant to regulate genes with roles in the cellular response to stress. Taken together, these findings support the existence of a conserved, multi-protein complex with a role in promoting the successful completion of cytokinesis.","doi":"10.1371/journal.pone.0031224","authors":"Rentas S, Saberianfar R, Grewal C, Kanippayoor R, Mishra M, McCollum D, Karagiannis J","authors_abbrev":"Rentas S et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-02-21","publication_year":"2012","canto_session_key":"f20d1a8914693c8e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-12 19:21:33","canto_approved_date":"2024-06-12 19:21:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 19:21:25","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1235.09","SPAC20G8.05c","SPAC1782.09c","SPAC2F3.15","SPAC22E12.19","SPAC22E12.11c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2024-06-12"},{"uniquename":"PMID:27155541","title":"Overview of fission yeast septation.","citation":"Cell Microbiol 2016 Sep;18(9):1201-7","abstract":"Cytokinesis is the final process of the vegetative cycle, which divides a cell into two independent daughter cells once mitosis is completed. In fungi, as in animal cells, cytokinesis requires the formation of a cleavage furrow originated by constriction of an actomyosin ring which is connected to the plasma membrane and causes its invagination. Additionally, because fungal cells have a polysaccharide cell wall outside the plasma membrane, cytokinesis requires the formation of a septum coincident with the membrane ingression. Fission yeast Schizosaccharomyces pombe is a unicellular, rod-shaped fungus that has become a popular model organism for the study of actomyosin ring formation and constriction during cell division. Here we review the current knowledge of the septation and separation processes in this fungus, as well as recent advances in understanding the functional interaction between the transmembrane enzymes that build the septum and the actomyosin ring proteins.","doi":"10.1111/cmi.12611","authors":"Pérez P, Cortés JC, Martín-García R, Ribas JC","authors_abbrev":"Pérez P et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-05-08","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-05-09 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38102143","title":"A single C-terminal residue controls SARS-CoV-2 spike trafficking and incorporation into VLPs.","citation":"Nat Commun 2023 Dec 15;14(1):8358","abstract":"The spike (S) protein of SARS-CoV-2 is delivered to the virion assembly site in the ER-Golgi Intermediate Compartment (ERGIC) from both the ER and cis-Golgi in infected cells. However, the relevance and modulatory mechanism of this bidirectional trafficking are unclear. Here, using structure-function analyses, we show that S incorporation into virus-like particles (VLP) and VLP fusogenicity are determined by coatomer-dependent S delivery from the cis-Golgi and restricted by S-coatomer dissociation. Although S mimicry of the host coatomer-binding dibasic motif ensures retrograde trafficking to the ERGIC, avoidance of the host-like C-terminal acidic residue is critical for S-coatomer dissociation and therefore incorporation into virions or export for cell-cell fusion. Because this C-terminal residue is the key determinant of SARS-CoV-2 assembly and fusogenicity, our work provides a framework for the export of S protein encoded in genetic vaccines for surface display and immune activation.","doi":"10.1038/s41467-023-44076-3","authors":"Dey D, Qing E, He Y, Chen Y, Jennings B, Cohn W, Singh S, Gakhar L, Schnicker NJ, Pierce BG, Whitelegge JP, Doray B, Orban J, Gallagher T, Hasan SS","authors_abbrev":"Dey D et al.","pubmed_publication_date":"15 Dec 2023","pubmed_entrez_date":"2023-12-15","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBPJ4664.04"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"8enz","gene_chains":[{"gene_uniquename":"SPBPJ4664.04","chain":"A/B/C","position":"1-327"}],"title":"Crystal structure of alpha-COPI-WD40 domain K15A mutant.","entry_authors":"Dey D,Hasan SS","entry_authors_abbrev":"Dey D et al.","reference_uniquename":"PMID:38102143","experimental_method":"X-ray","resolution":"1.65"},{"pdb_id":"8eny","gene_chains":[{"gene_uniquename":"SPBPJ4664.04","chain":"A/B/C","position":"1-327"}],"title":"Crystal structure of alpha-COPI-WD40 domain R13A mutant.","entry_authors":"Dey D,Hasan SS","entry_authors_abbrev":"Dey D et al.","reference_uniquename":"PMID:38102143","experimental_method":"X-ray","resolution":"1.9"},{"pdb_id":"8eo0","gene_chains":[{"gene_uniquename":"SPBPJ4664.04","chain":"A/B/C","position":"1-327"}],"title":"Crystal structure of alpha-COPI WD40 domain R300A mutant.","entry_authors":"Dey D,Hasan SS","entry_authors_abbrev":"Dey D et al.","reference_uniquename":"PMID:38102143","experimental_method":"X-ray","resolution":"1.8"}]},{"uniquename":"PMID:21098635","title":"Mid1p-dependent regulation of the M-G1 transcription wave in fission yeast.","citation":"J Cell Sci 2010 Dec 15;123(Pt 24):4366-73","abstract":"The control of gene expression at certain times during the mitotic cell division cycle is a common feature in eukaryotes. In fission yeast, at least five waves of gene expression have been described, with one transcribed at the M-G1 interval under the control of the PBF transcription factor complex. PBF consists of at least three transcription factors, two forkhead-like proteins Sep1p and Fkh2p, and a MADS box-like protein Mbx1p, and binds to PCB motifs found in the gene promoters. Mbx1p is under the direct control of the polo-like kinase Plo1p and the Cdc14p-like phosphatase Clp1p (Flp1p). Here, we show that M-G1 gene expression in fission yeast is also regulated by the anillin-like protein, Mid1p (Dmf1p). Mid1p binds in vivo to both Fkh2p and Sep1p, and to the promoter regions of M-G1 transcribed genes. Mid1p promoter binding is dependent on Fkh2p, Plo1p and Clp1p. The absence of mid1(+) in cells results in partial loss of M-G1 specific gene expression, suggesting that it has a negative role in controlling gene expression. This phenotype is exacerbated by also removing clp1(+), suggesting that Mid1p and Clp1p have overlapping functions in controlling transcription. As mid1(+) is itself expressed at M-G1, these observations offer a new mechanism whereby Mid1p contributes to controlling cell cycle-specific gene expression as part of a feedback loop.","doi":"10.1242/jcs.073049","authors":"Agarwal M, Papadopoulou K, Mayeux A, Vajrala V, Quintana DM, Paoletti A, McInerny CJ","authors_abbrev":"Agarwal M et al.","pubmed_publication_date":"15 Dec 2010","pubmed_entrez_date":"2010-11-25","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4C3.12","SPCC4B3.15","SPBC16G5.15c","SPAC1782.09c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:9572736","title":"Replication checkpoint enforced by kinases Cds1 and Chk1.","citation":"Science 1998 May 08;280(5365):909-12","abstract":"Cdc2, the kinase that induces mitosis, is regulated by checkpoints that couple mitosis to the completion of DNA replication and repair. The repair checkpoint kinase Chk1 regulates Cdc25, a phosphatase that activates Cdc2. Effectors of the replication checkpoint evoked by hydroxyurea (HU) are unknown. Treatment of fission yeast with HU stimulated the kinase Cds1, which appears to phosphorylate the kinase Wee1, an inhibitor of Cdc2. The protein kinase Cds1 was also required for a large HU-induced increase in the amount of Mik1, a second inhibitor of Cdc2. HU-induced arrest of cell division was abolished in cds1 chk1 cells. Thus, Cds1 and Chk1 appear to jointly enforce the replication checkpoint.","authors":"Boddy MN, Furnari B, Mondesert O, Russell P","authors_abbrev":"Boddy MN et al.","pubmed_publication_date":"08 May 1998","pubmed_entrez_date":"1998-05-23","publication_year":"1998","canto_session_key":"36d4085e11a5e17d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-11 15:55:41","canto_approved_date":"2024-04-11 15:55:41","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-04-11 15:55:31","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":28,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPAC1952.07","SPCC18B5.11c","SPBC216.05","SPBC660.14","SPCC1259.13","SPBC11B10.09","SPCC18B5.03","SPAC24H6.05"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2024-04-11"},{"uniquename":"PMID:23549175","title":"RNF8 links nucleosomal and cytoskeletal ubiquitylation of higher order protein structures.","citation":"Cell Cycle 2013 Apr 15;12(8):1161-2","abstract":"","doi":"10.4161/cc.24402","authors":"Chahwan R, Gravel S, Matsusaka T, Jackson SP","authors_abbrev":"Chahwan R et al.","pubmed_publication_date":"15 Apr 2013","pubmed_entrez_date":"2013-04-04","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:47:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G8.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:40147281","title":"Identification and characterization of aldo-keto reductase responsible for patulin degradation in Saccharomyces cerevisiae.","citation":"Food Chem 2025 Mar 03;478:143706","abstract":"Patulin (PAT) is a hazardous mycotoxin that contaminates fruits and their products, causing significant economic losses. An aldo-keto reductase from Saccharomyces cerevisiae (ScAKR) was expressed in Escherichia coli in this study. The purified ScAKR converted PAT to E-ascladiol with NADPH as a cofactor. The ScAKR exhibited a strong degradation activity on PAT and the optimal degradation conditions were pH 7 and 37 °C. Molecular docking and site-specific mutagenesis indicated that the amino acids in ScAKR interacting with PAT aldehyde affected the degradation effect, and the mutation of Trp298 showed the most significant effect on the degradation rate. Furthermore, ScAKR also showed a strong degradation effect on 3-keto-deoxynivalenol, a metabolite of another mycotoxin, deoxynivalenol (DON). The findings offer new insights on the detoxification mechanism of PAT by S. cerevisiae and for the development and application of bioenzymes with broad-spectrum mycotoxin degradation properties.","doi":"10.1016/j.foodchem.2025.143706","authors":"Yang C, Huang L, Hu C, Yao J, Zhou T, Li XZ, Seah SYK, Peng B","authors_abbrev":"Yang C et al.","pubmed_publication_date":"03 Mar 2025","pubmed_entrez_date":"2025-03-27","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10660053","title":"The alm1+ gene from Schizosaccharomyces pombe encodes a coiled-coil protein that associates with the medial region during mitosis.","citation":"Mol Gen Genet 2000 Jan;262(6):921-30","abstract":"We have isolated a cDNA that encodes a 142 kDa protein by immunoscreening of a Schizosaccharomyces pombe expression library with a new antibody, mAb8, that reveals spindle poles and equatorial ring-like structures in several organisms. This cDNA encodes a putative protein which we termed Alm (for abnormal long morphology). The protein is predicted to be a coiled-coil protein, containing a central alpha-helical domain flanked by non-helical terminal domains. Immunofluorescence analysis showed that Alm1 is localized in the medial region of the cell from anaphase to the end of cytokinesis. Cells carrying an alm1::ura4+ disruption are viable and exhibit an elongated morphology. Homozygous alm1::ura4+ diploids sporulated normally but the spores did not germinate. Spores that have inherited the disruption allele from a heterozygous alm1+/ alm1::ura4+ diploid germinated but generated smaller colonies. We propose that Alm1 participates in the structural organization of the medial region in S. pombe.","authors":"Jiménez M, Petit T, Gancedo C, Goday C","authors_abbrev":"Jiménez M et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-02-05","publication_year":"2000","canto_session_key":"ba38ca0a0e236a70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-06-18 17:10:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-18 17:10:29","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1486.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-18"},{"uniquename":"PMID:27260214","title":"Are all repeats created equal? Understanding DNA repeats at an individual level.","citation":"Curr Genet 2017 Feb;63(1):57-63","abstract":"Repetitive DNA sequences, comprising up to 50 % of the genome in all eukaryotes, play important roles in a wide range of cellular functions, such as transcriptional regulation, genome stability, and cellular differentiation. However, due to technical difficulties in differentiating their sequences, DNA repeats remain one of the most mysterious parts of eukaryotic genomes. Key questions, such as how repetitive entities behave at individual level and how the internal architecture of these repeats is organized, are still poorly understood. Recent advances from our group reveal unexpected position-dependent variation within tandem DNA repeats in fission yeast. Despite sharing identical DNA sequences, the peri-centromeric repeats are organized into diverse epigenetic states and chromatin structures. We demonstrate that this position-dependent variation requires key heterochromatin factors and condensin. Our works further suggest that the peri-centromeric repeats are organized into distinct higher order structures that ensure a proper positioning of CENP-A, the centromere-specific histone H3 variant, to centromeres. These most recent developments offer insights into the mechanisms underlying the position effect within tandem DNA arrays, and have broad implications in the field of epigenetics and chromatin biology.","doi":"10.1007/s00294-016-0619-x","authors":"Yang J, Li F","authors_abbrev":"Yang J et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-06-05","publication_year":"2017","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-06-06 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22313747","title":"A double mutant between fission yeast telomerase and RecQ helicase is sensitive to thiabendazole, an anti-microtubule drug.","citation":"Biosci Biotechnol Biochem 2012;76(2):264-9","abstract":"In the fission yeast Schizosaccharomyces pombe, deletion of trt1(+) causes gradual telomere shortening, while deletion of pot1(+) causes rapid telomere loss. The double mutant between pot1 and RecQ helicase rqh1 is synthetically lethal. We found that the trt1 rqh1 double mutant was not synthetically lethal. The chromosome end fragments in both the trt1Δ rqh1Δ and the trt1Δ rqh1-hd (helicase dead) double mutants did not enter a pulsed-field electrophoresis gel. Both the trt1Δ rqh1Δ and the trt1Δ rqh1-hd double mutants were sensitive to the anti-microtubule drug thiabendazole. Moreover, the trt1Δ rqh1-hd double mutant displayed RPA foci on the chromosome bridge at high frequency in M phase cells. These phenotypes are very similar to that of the pot1Δ rqh1-hd double mutant, in which recombination intermediates accumulate at the chromosme ends in the M phase. These results suggest that the entangled chromosome ends, most likely recombination intermediates, are present in the M phase in the trt1Δ rqh1-hd double mutant.","authors":"Ukimori S, Kawabata N, Shimada H, Imano R, Takahashi K, Yukawa M, Tsuchiya E, Ueno M","authors_abbrev":"Ukimori S et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-02-09","publication_year":"2012","canto_session_key":"5fff5e70e49d4274","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-16 14:38:55","canto_approved_date":"2021-11-15 18:03:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-05 11:57:34","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC1D4.12","SPAC2G11.12","SPBC29A3.14c","SPAC26H5.06"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2016-06-16"},{"uniquename":"PMID:38643032","title":"Expression of an endo-rhamnogalacturonase from Aspergillus aculeatus enhances release of Arabidopsis transparent mucilage.","citation":"J Biosci Bioeng 2024 Apr 19;","abstract":"Mucilage is a gelatinous and sticky hydrophilic polysaccharide released from epidermal cells of seed coat after the hydration of mature seeds and is composed primarily of unbranched rhamnogalacturonan I (RG-I). In this study, we produced a recombinant endo-RG-I hydrolase from Aspergillus aculeatus (AaRhgA) in the fission yeast Schizosaccharomyces pombe and examined its substrate preference for pyridylaminated (PA) RG-I with the various degrees of polymerization (DP). Recombinant AaRhgA requires PA-RG-I with a DP of 10 or higher for its hydrolase activity. We heterologously expressed the AarhgA gene under the strong constitutive promoter, cauliflower mosaic virus 35S promoter, in Arabidopsis thaliana. In a series of biochemical analyses of each mucilage fraction released from the water-imbibed seeds of the transgenic plants, we found the enhanced deposition of the transparent mucilage layer that existed in the peripheral regions of the adherent mucilage and was not stained with ruthenium red. This study demonstrated the feasibility of manipulating the mucilage organization by heterologous expression of the endo-RG-I hydrolase.","doi":"10.1016/j.jbiosc.2024.03.006","authors":"Ohashi T, Mabira Y, Mitsuyoshi Y, Kajiura H, Misaki R, Ishimizu T, Fujiyama K","authors_abbrev":"Ohashi T et al.","pubmed_publication_date":"19 Apr 2024","pubmed_entrez_date":"2024-04-20","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-04-21 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU014345","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22510556","title":"A new tool for an old problem: synchronizing fission yeast cells during meiosis using an ATP analog-sensitive protein kinase.","citation":"Cell Cycle 2012 May 01;11(9):1755-6","abstract":"","doi":"10.4161/cc.20314","authors":"Nosek J, Tomáska L","authors_abbrev":"Nosek J et al.","pubmed_publication_date":"01 May 2012","pubmed_entrez_date":"2012-04-19","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42144894","title":"On the other side of the membrane: A new role for a luminal protein in the cytoplasm.","citation":"FEBS J 2026 May 17;","abstract":"Proteins annotated as localizing inside membrane-bound organelles are accepted as residing there. Thus, encountering a mitochondrial cytochrome in the cytoplasm would be unexpected. Yet, a mitochondrial cytochrome does relocalize to the cytoplasm during apoptotic cell death. In fact, a growing list of annotated luminal proteins has demonstrable cytoplasmic functions. It is with this perspective of bi-compartmental proteins that I encourage you to read the new study from Zhu and Fu in this issue of The FEBS Journal. The authors investigate how stress inside the ER lumen influences cytoplasmic energy regulation and uncover a surprising mechanism in fission yeast.","doi":"10.1111/febs.70586","authors":"Snapp E","authors_abbrev":"Snapp E","pubmed_publication_date":"17 May 2026","pubmed_entrez_date":"2026-05-18","publication_year":"2026","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2026-05-18 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12888341","title":"Functional analysis of the novel C-terminal domains of S pombe transcription factor IIIA.","citation":"J Mol Biol 2003 Aug 08;331(2):321-30","abstract":"Transcription factor IIIA from S.pombe exhibits a novel structural organization compared to its homologues in other species. TFIIIA from S.cerevisiae or vertebrates contains a total of nine C(2)H(2) zinc-finger domains and a non-zinc finger region at its C terminus. In addition, the S.cerevisiae protein possesses an 81-amino acid spacer between zinc fingers eight and nine. In contrast, the S.pombe TFIIIA sequence includes ten potential zinc finger motifs, with a 53-amino acid spacer between fingers nine and ten. Zinc finger nine of the S.pombe protein deviates from the consensus for a C(2)H(2) zinc finger, however, in that it does not include an appropriately positioned second Zn(2+)-coordinating histidine. We demonstrate here, through analysis of mutated forms of the protein, that the non-canonical ninth zinc finger is functional in both DNA binding and transcription. In addition, we have shown that the spacer preceding finger ten and finger ten itself are essential for the transcriptional function of S.pombe TFIIIA, but neither is required for wild-type 5S rRNA gene-binding activity.","authors":"Schulman DB, Setzer DR","authors_abbrev":"Schulman DB et al.","pubmed_publication_date":"08 Aug 2003","pubmed_entrez_date":"2003-07-31","publication_year":"2003","canto_session_key":"bfc8cbcebd1237c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-03 07:07:15","canto_approved_date":"2024-03-29 09:42:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-01-02 04:21:19","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC144.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-01-03"},{"uniquename":"PMID:25926702","title":"Anniversary of the discovery/isolation of the yeast centromere by Clarke and Carbon.","citation":"Mol Biol Cell 2015 May 01;26(9):1575-7","abstract":"The first centromere was isolated 35 years ago by Louise Clarke and John Carbon from budding yeast. They embarked on their journey with rudimentary molecular tools (by today's standards) and little knowledge of the structure of a chromosome, much less the nature of a centromere. Their discovery opened up a new field, as centromeres have now been isolated from fungi and numerous plants and animals, including mammals. Budding yeast and several other fungi have small centromeres with short, well-defined sequences, known as point centromeres, whereas regional centromeres span several kilobases up to megabases and do not seem to have DNA sequence specificity. Centromeres are at the heart of artificial chromosomes, and we have seen the birth of synthetic centromeres in budding and fission yeast and mammals. The diversity in centromeres throughout phylogeny belie conserved functions that are only beginning to be understood.","doi":"10.1091/mbc.E14-11-1512","authors":"Bloom K","authors_abbrev":"Bloom K","pubmed_publication_date":"01 May 2015","pubmed_entrez_date":"2015-05-01","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-05-02 00:19:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20944394","title":"Vba2p, a vacuolar membrane protein involved in basic amino acid transport in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2010;74(10):2166-9","abstract":"A recent study filling the gap in the genome sequence in the left arm of chromosome 2 of Schizosaccharomyces pombe revealed a homolog of budding yeast Vba2p, a vacuolar transporter of basic amino acids. GFP-tagged Vba2p in fission yeast was localized to the vacuolar membrane. Upon disruption of vba2, the uptake of several amino acids, including lysine, histidine, and arginine, was impaired. A transient increase in lysine uptake under nitrogen starvation was lowered by this mutation. These findings suggest that Vba2p is involved in basic amino acid transport in S. pombe under diverse conditions.","authors":"Sugimoto N, Iwaki T, Chardwiriyapreecha S, Shimazu M, Sekito T, Takegawa K, Kakinuma Y","authors_abbrev":"Sugimoto N et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-10-15","publication_year":"2010","canto_session_key":"55b630d3d775188d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-16 13:42:20","canto_approved_date":"2024-07-02 13:10:37","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-10-16 08:11:32","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC460.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-03-16"},{"uniquename":"PMID:24982431","title":"Pom1 regulates the assembly of Cdr2-Mid1 cortical nodes for robust spatial control of cytokinesis.","citation":"J Cell Biol 2014 Jul 07;206(1):61-77","abstract":"Proper division plane positioning is essential to achieve faithful DNA segregation and to control daughter cell size, positioning, or fate within tissues. In Schizosaccharomyces pombe, division plane positioning is controlled positively by export of the division plane positioning factor Mid1/anillin from the nucleus and negatively by the Pom1/DYRK (dual-specificity tyrosine-regulated kinase) gradients emanating from cell tips. Pom1 restricts to the cell middle cortical cytokinetic ring precursor nodes organized by the SAD-like kinase Cdr2 and Mid1/anillin through an unknown mechanism. In this study, we show that Pom1 modulates Cdr2 association with membranes by phosphorylation of a basic region cooperating with the lipid-binding KA-1 domain. Pom1 also inhibits Cdr2 interaction with Mid1, reducing its clustering ability, possibly by down-regulation of Cdr2 kinase activity. We propose that the dual regulation exerted by Pom1 on Cdr2 prevents Cdr2 assembly into stable nodes in the cell tip region where Pom1 concentration is high, which ensures proper positioning of cytokinetic ring precursors at the cell geometrical center and robust and accurate division plane positioning.","doi":"10.1083/jcb.201311097","authors":"Rincon SA, Bhatia P, Bicho C, Guzman-Vendrell M, Fraisier V, Borek WE, Alves Fde L, Dingli F, Loew D, Rappsilber J, Sawin KE, Martin SG, Paoletti A","authors_abbrev":"Rincon SA et al.","pubmed_publication_date":"07 Jul 2014","pubmed_entrez_date":"2014-07-02","publication_year":"2014","canto_session_key":"73217d5f7d7f3454","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-02-26 11:03:57","canto_approved_date":"2026-06-09 08:13:22","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-02-09 15:02:17","canto_added_date":"2014-07-03 00:15:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPAC2F7.03c","SPCC4B3.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2026-02-26"},{"uniquename":"PMID:7706287","title":"A mutation in the Schizosaccharomyces pombe rae1 gene causes defects in poly(A)+ RNA export and in the cytoskeleton.","citation":"J Biol Chem 1995 Mar 31;270(13):7411-9","abstract":"A collection of fission yeast Schizosaccharomyces pombe conditional mutants was screened for defective nucleocytoplasmic transport of poly(A)+ RNA by fluorescence in situ hybridization. We identified a temperature-sensitive mutant that accumulated poly(A)+ RNA in the nucleus and have named it rae1-1, for ribonucleic acid export. All rae1-1 cells exhibit the defect in poly(A)+ RNA export within 30 min following a shift to the non-permissive temperature. In addition, in the rae1-1 mutant, actin and tubulin become disorganized, and cells undergo an irreversible cycle arrest. Results from experiments in which rae1-1 cells were arrested in various phases of the cell division cycle and then shifted to nonpermissive temperature suggest that cells are particularly vulnerable to loss of rae1 function during G2/M. However, the inability to export RNA from the nucleus to the cytoplasm was not limited to a particular phase of the cell division cycle. The rae1 gene was isolated by complementation and encodes a predicted protein of 352 amino acids with four beta-transducin/WD40 repeats.","authors":"Brown JA, Bharathi A, Ghosh A, Whalen W, Fitzgerald E, Dhar R","authors_abbrev":"Brown JA et al.","pubmed_publication_date":"31 Mar 1995","pubmed_entrez_date":"1995-03-31","publication_year":"1995","canto_session_key":"fa139ea3d6452102","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-22 09:46:06","canto_approved_date":"2026-01-30 15:52:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-20 10:51:28","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC16A3.15c","SPBC16A3.05c","SPBC800.05c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2015-04-22"},{"uniquename":"PMID:27734801","title":"Curvature-induced expulsion of actomyosin bundles during cytokinetic ring contraction.","citation":"Elife 2016 Oct 13;5","abstract":"Many eukaryotes assemble a ring-shaped actomyosin network that contracts to drive cytokinesis. Unlike actomyosin in sarcomeres, which cycles through contraction and relaxation, the cytokinetic ring disassembles during contraction through an unknown mechanism. Here we find in  Schizosaccharomyces japonicus  and  Schizosaccharomyces pombe  that, during actomyosin ring contraction, actin filaments associated with actomyosin rings are expelled as micron-scale bundles containing multiple actomyosin ring proteins. Using functional isolated actomyosin rings we show that expulsion of actin bundles does not require continuous presence of cytoplasm. Strikingly, mechanical compression of actomyosin rings results in expulsion of bundles predominantly at regions of high curvature. Our work unprecedentedly reveals that the increased curvature of the ring itself promotes its disassembly. It is likely that such a curvature-induced mechanism may operate in disassembly of other contractile networks.","doi":"10.7554/eLife.21383","authors":"Huang J, Chew TG, Gu Y, Palani S, Kamnev A, Martin DS, Carter NJ, Cross RA, Oliferenko S, Balasubramanian MK","authors_abbrev":"Huang J et al.","pubmed_publication_date":"13 Oct 2016","pubmed_entrez_date":"2016-10-14","publication_year":"2016","canto_session_key":"dcb7cd75c4e0c804","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-10-15 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33846633","title":"Structural basis of nucleosome transcription mediated by Chd1 and FACT.","citation":"Nat Struct Mol Biol 2021 Apr;28(4):382-387","abstract":"Efficient transcription of RNA polymerase II (Pol II) through nucleosomes requires the help of various factors. Here we show biochemically that Pol II transcription through a nucleosome is facilitated by the chromatin remodeler Chd1 and the histone chaperone FACT when the elongation factors Spt4/5 and TFIIS are present. We report cryo-EM structures of transcribing Saccharomyces cerevisiae Pol II-Spt4/5-nucleosome complexes with bound Chd1 or FACT. In the first structure, Pol II transcription exposes the proximal histone H2A-H2B dimer that is bound by Spt5. Pol II has also released the inhibitory DNA-binding region of Chd1 that is poised to pump DNA toward Pol II. In the second structure, Pol II has generated a partially unraveled nucleosome that binds FACT, which excludes Chd1 and Spt5. These results suggest that Pol II progression through a nucleosome activates Chd1, enables FACT binding and eventually triggers transfer of FACT together with histones to upstream DNA.","doi":"10.1038/s41594-021-00578-6","authors":"Farnung L, Ochmann M, Engeholm M, Cramer P","authors_abbrev":"Farnung L et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2021-04-13","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1783.05","SPBC609.05"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:24493214","title":"ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling.","citation":"EMBO J 2014 Mar 03;33(5):482-500","abstract":"The Mre11-Rad50 complex is highly conserved, yet the mechanisms by which Rad50 ATP-driven states regulate the sensing, processing and signaling of DNA double-strand breaks are largely unknown. Here we design structure-based mutations in Pyrococcus furiosus Rad50 to alter protein core plasticity and residues undergoing ATP-driven movements within the catalytic domains. With this strategy we identify Rad50 separation-of-function mutants that either promote or destabilize the ATP-bound state. Crystal structures, X-ray scattering, biochemical assays, and functional analyses of mutant PfRad50 complexes show that the ATP-induced 'closed' conformation promotes DNA end binding and end tethering, while hydrolysis-induced opening is essential for DNA resection. Reducing the stability of the ATP-bound state impairs DNA repair and Tel1 (ATM) checkpoint signaling in Schizosaccharomyces pombe, double-strand break resection in Saccharomyces cerevisiae, and ATM activation by human Mre11-Rad50-Nbs1 in vitro, supporting the generality of the P. furiosus Rad50 structure-based mutational analyses. These collective results suggest that ATP-dependent Rad50 conformations switch the Mre11-Rad50 complex between DNA tethering, ATM signaling, and 5' strand resection, revealing molecular mechanisms regulating responses to DNA double-strand breaks.","doi":"10.1002/embj.201386100","authors":"Deshpande RA, Williams GJ, Limbo O, Williams RS, Kuhnlein J, Lee JH, Classen S, Guenther G, Russell P, Tainer JA, Paull TT","authors_abbrev":"Deshpande RA et al.","pubmed_publication_date":"03 Mar 2014","pubmed_entrez_date":"2014-02-05","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC1556.01c","SPCC23B6.03c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:37230993","title":"The conserved RNA-binding protein Seb1 promotes cotranscriptional ribosomal RNA processing by controlling RNA polymerase I progression.","citation":"Nat Commun 2023 May 25;14(1):3013","abstract":"Transcription by RNA polymerase I (RNAPI) represents most of the transcriptional activity in eukaryotic cells and is associated with the production of mature ribosomal RNA (rRNA). As several rRNA maturation steps are coupled to RNAPI transcription, the rate of RNAPI elongation directly influences processing of nascent pre-rRNA, and changes in RNAPI transcription rate can result in alternative rRNA processing pathways in response to growth conditions and stress. However, factors and mechanisms that control RNAPI progression by influencing transcription elongation rate remain poorly understood. We show here that the conserved fission yeast RNA-binding protein Seb1 associates with the RNAPI transcription machinery and promotes RNAPI pausing states along the rDNA. The overall faster progression of RNAPI at the rDNA in Seb1-deficient cells impaired cotranscriptional pre-rRNA processing and the production of mature rRNAs. Given that Seb1 also influences pre-mRNA processing by modulating RNAPII progression, our findings unveil Seb1 as a pause-promoting factor for RNA polymerases I and II to control cotranscriptional RNA processing.","doi":"10.1038/s41467-023-38826-6","authors":"Duval M, Yague-Sanz C, Turowski TW, Petfalski E, Tollervey D, Bachand F","authors_abbrev":"Duval M et al.","pubmed_publication_date":"25 May 2023","pubmed_entrez_date":"2023-05-25","publication_year":"2023","canto_session_key":"99924527e7598939","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-05-27 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27037074","title":"Transformation of Schizosaccharomyces pombe: Electroporation Procedure.","citation":"Cold Spring Harb Protoc 2016 Apr 01;2016(4):pdb.prot090951","abstract":"Transformation ofSchizosaccharomyces pombewith DNA requires the conditioning of cells to promote DNA uptake followed by cell growth under conditions that select and maintain the plasmid or integration event. The three main methodologies are electroporation, treatment with lithium cations, and transformation of protoplasts. This protocol describes transformation by electroporation. It involves pretreatingS. pombecells with dithiothreitol (DTT), which increases the transformation efficiency once the electric pulse is applied.","doi":"10.1101/pdb.prot090951","authors":"Murray JM, Watson AT, Carr AM","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"01 Apr 2016","pubmed_entrez_date":"2016-04-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-04-04 00:15:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24873914","title":"Regulation of the unbalanced redox state in a Schizosaccharomyces pombe tert-butyl hydroperoxide-resistant mutant.","citation":"Acta Biol Hung 2014 Jun;65(2):218-26","abstract":"The one-gene mutation in the tert-butyl hydroperoxide-resistant mutant hyd1-190 of the fission yeast Schizosaccharomyces pombe led to a 4-fold increase in resistance to t-BuOOH and decreased specific concentrations of superoxide and total thiols in comparison with the parental strain hyd+. It suggested an unbalanced redox state of the cells, which induced continuously increased specific activities of glutathione peroxidase, glutathione reductase and glutathione S-transferase and decreased activities of the antioxidant enzymes superoxide dismutases and glucose-6-phosphate dehydrogenase to regulate the redox balance of the mutation-induced permanent, low-level but tolerable internal stress. These results may contribute to the understanding of internal, oxidative stress-related human diseases.","doi":"10.1556/ABiol.65.2014.2.9","authors":"Gazdag Z, Kálmán N, Blaskó A, Virág E, Belágyi J, Pesti M","authors_abbrev":"Gazdag Z et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-05-31","publication_year":"2014","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9325108","title":"A new Holliday junction resolving enzyme from Schizosaccharomyces pombe that is homologous to CCE1 from Saccharomyces cerevisiae.","citation":"J Mol Biol 1997 Oct 03;272(4):509-22","abstract":"The resolution of Holliday junctions is a critical stage in recombination. We describe the identification and initial biochemical characterisation of a new Holliday junction resolvase from Schizosaccharomyces pombe. Resolvase activity was initially detected in partially purified cell-free extracts of S. pombe. Resolution of X-junction DNA occurred by the introduction of symmetrical cuts in strands of the same polarity. All cuts occurred 3' of thymine nucleotides with a possible preference for cleavage one nucleotide 3' from the point of strand crossover. During the course of these studies, a potential S. pombe homologue of the Saccharomyces cerevisiae Cruciform Cutting Endonuclease I was identified in the database (SpCCE1). The gene was cloned by PCR, overexpressed in Escherichia coli and its product purified as a His-tagged fusion protein. Purified SpCCE1 binds to X-junctions in a structure-specific manner and resolves them to nicked linear duplex products that are repairable by DNA ligase. SpCCE1 cuts X-junctions in precisely the same way as the resolvase activity from partially purified extracts of S. pombe, indicating that they are probably the same. Finally, we show that SpCCE1 can function as a Holliday junction resolvase in vivo by its ability to complement a resolvase-deficient strain of E. coli.","authors":"Whitby MC, Dixon J","authors_abbrev":"Whitby MC et al.","pubmed_publication_date":"03 Oct 1997","pubmed_entrez_date":"1997-10-31","publication_year":"1997","canto_session_key":"563b3ea3f2426460","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-09-02 10:48:29","canto_approved_date":"2020-01-23 13:49:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-01 17:26:34","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-02"},{"uniquename":"PMID:26383111","title":"Differentiating the roles of microtubule-associated proteins at meiotic kinetochores during chromosome segregation.","citation":"Chromosoma 2016 Jun;125(2):309-20","abstract":"Meiosis is a specialised cell division process for generating gametes. In contrast to mitosis, meiosis involves recombination followed by two consecutive rounds of cell division, meiosis I and II. A vast field of research has been devoted to understanding the differences between mitotic and meiotic cell divisions from the viewpoint of chromosome behaviour. For faithful inheritance of paternal and maternal genetic information to offspring, two events are indispensable: meiotic recombination, which generates a physical link between homologous chromosomes, and reductional segregation, in which homologous chromosomes move towards opposite poles, thereby halving the ploidy. The cytoskeleton and its regulators play specialised roles in meiosis to accomplish these divisions. Recent studies have shown that microtubule-associated proteins (MAPs), including tumour overexpressed gene (TOG), play unique roles during meiosis. Furthermore, the conserved mitotic protein kinase Polo modulates MAP localisation in meiosis I. As Polo is a well-known regulator of reductional segregation in meiosis, the evidence suggests that Polo constitutes a plausible link between meiosis-specific MAP functions and reductional segregation. Here, we review the latest findings on how the localisation and regulation of MAPs in meiosis differ from those in mitosis, and we discuss conservation of the system between yeast and higher eukaryotes.","doi":"10.1007/s00412-015-0541-x","authors":"Kakui Y, Sato M","authors_abbrev":"Kakui Y et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2015-09-19","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-09-20 00:18:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36075094","title":"On the Mechanistic Basis of Killer Meiotic Drive in Fungi.","citation":"Annu Rev Microbiol 2022 Sep 08;76:305-323","abstract":"Spore killers are specific genetic elements in fungi that kill sexual spores that do not contain them. A range of studies in the last few years have provided the long-awaited first insights into the molecular mechanistic aspects of spore killing in different fungal models, including both yeast-forming and filamentous Ascomycota. Here we describe these recent advances, focusing on the  wtf  system in the fission yeast  Schizosaccharomyces pombe ; the  Sk  spore killers of  Neurospora  species; and two spore-killer systems in  Podospora anserina ,  Spok  and [Het-s]. The spore killers appear thus far mechanistically unrelated. They can involve large genomic rearrangements but most often rely on the action of just a single gene. Data gathered so far show that the protein domains involved in the killing and resistance processes differ among the systems and are not homologous. The emerging picture sketched by these studies is thus one of great mechanistic and evolutionary diversity of elements that cheat during meiosis and are thereby preferentially inherited over sexual generations.","doi":"10.1146/annurev-micro-041320-113730","authors":"Saupe SJ, Johannesson H","authors_abbrev":"Saupe SJ et al.","pubmed_publication_date":"08 Sep 2022","pubmed_entrez_date":"2022-09-08","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-09-10 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30911189","title":"Atg2 mediates direct lipid transfer between membranes for autophagosome formation.","citation":"Nat Struct Mol Biol 2019 Apr;26(4):281-288","abstract":"A key event in autophagy is autophagosome formation, whereby the newly synthesized isolation membrane (IM) expands to form a complete autophagosome using endomembrane-derived lipids. Atg2 physically links the edge of the expanding IM with the endoplasmic reticulum (ER), a role that is essential for autophagosome formation. However, the molecular function of Atg2 during ER-IM contact remains unclear, as does the mechanism of lipid delivery to the IM. Here we show that the conserved amino-terminal region of Schizosaccharomyces pombe Atg2 includes a lipid-transfer-protein-like hydrophobic cavity that accommodates phospholipid acyl chains. Atg2 bridges highly curved liposomes, thereby facilitating efficient phospholipid transfer in vitro, a function that is inhibited by mutations that impair autophagosome formation in vivo. These results suggest that Atg2 acts as a lipid-transfer protein that supplies phospholipids for autophagosome formation.","doi":"10.1038/s41594-019-0203-4","authors":"Osawa T, Kotani T, Kawaoka T, Hirata E, Suzuki K, Nakatogawa H, Ohsumi Y, Noda NN","authors_abbrev":"Osawa T et al.","pubmed_publication_date":"Apr 2019","pubmed_entrez_date":"2019-03-27","publication_year":"2019","canto_session_key":"857a5b25fc327d3c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-20 08:43:50","canto_approved_date":"2023-02-20 08:43:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-18 17:25:55","canto_added_date":"2019-03-28 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31E1.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-20","pdb_entries":[{"pdb_id":"6a9j","gene_chains":[{"gene_uniquename":"SPBC31E1.01c","chain":"A/A/B/B","position":"21-240"}],"title":"Crystal structure of the PE-bound N-terminal domain of Atg2","entry_authors":"Osawa T,Noda NN","entry_authors_abbrev":"Osawa T et al.","reference_uniquename":"PMID:30911189","experimental_method":"X-ray","resolution":"2.7"},{"pdb_id":"6a9e","gene_chains":[{"gene_uniquename":"SPBC31E1.01c","chain":"A/A/B/B","position":"21-240"}],"title":"Crystal structure of the N-terminal domain of Atg2","entry_authors":"Osawa T,Noda NN","entry_authors_abbrev":"Osawa T et al.","reference_uniquename":"PMID:30911189","experimental_method":"X-ray","resolution":"3.205"}]},{"uniquename":"PMID:9928955","title":"Interaction between the fission yeast nim1/cdr1 protein kinase and a dynamin-related protein.","citation":"FEBS Lett 1999 Jan 22;443(1):71-4","abstract":"The nim1/cdr1 protein kinase is required for an efficient adaptation of cell cycle parameters to changes in nutritional conditions. We have isolated msp1, a new fission yeast member of the dynamin-related large GTPase family, in a two-hybrid screen designed to identify proteins interacting with the nim1 kinase. Msp1 has been shown to be essential for the maintenance of mtDNA and hence for the inheritance of functional mitochondria. We present evidence indicating that niml and mspl proteins physically interact both in vitro and in vivo in fission yeast. These interactions occur through the amino-terminal catalytic domain of nim1 and the carboxy-terminal putative regulatory domain of mspl. These results provide new evidence for the existence of a connection between mitochondrial function and the cell cycle machinery.","authors":"Pelloquin L, Ducommun B, Belenguer P","authors_abbrev":"Pelloquin L et al.","pubmed_publication_date":"22 Jan 1999","pubmed_entrez_date":"1999-02-03","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1718.06","SPAC644.06c","SPCC18B5.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:18617043","title":"A protocol for isolation and visualization of yeast nuclei by scanning electron microscopy.","citation":"Methods Cell Biol 2008;88:367-87","abstract":"This article describes a protocol that details methods for the isolation of yeast nuclei from budding yeast (Saccharomyces cerevisiae) and fission yeast (Schizosaccharomyces pombe), immunogold labelling of proteins, and visualization by Field Emission Scanning Electron Microscopy (FESEM). This involves the removal of the yeast cell wall and isolation of the nucleus from within, followed by subsequent processing for high resolution microscopy. The nuclear isolation step is performed by enzymatic treatment of yeast cells to rupture the cell wall and generate spheroplasts (cells that have partially lost their cell wall and their characteristic shape), followed by isolation of nuclei by centrifugation. This protocol has been optimized for the visualization of the yeast nuclear envelope (NE), nuclear pore complexes (NPCs), and associated cytoskeletal structures. Samples, once processed for FESEM, can be stored under vacuum for weeks, allowing considerable time for image acquisition.","doi":"10.1016/S0091-679X(08)00419-6","authors":"Murray S, Kiseleva E","authors_abbrev":"Murray S et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-07-12","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1436080","title":"A new tropomyosin essential for cytokinesis in the fission yeast S. pombe.","citation":"Nature 1992 Nov 05;360(6399):84-7","abstract":"Mutations in the Schizosaccharomyces pombe cdc8 gene impair cytokinesis. Here we clone cdc8+ and find that it encodes a novel tropomyosin. Gene disruption results in lethal arrest of the cell cycle, but spore germination, cell growth, DNA replication and mitosis are all unaffected. Haploid cdc8 gene disruptants are rescued by expression of a fibroblast tropomyosin complementary DNA. Immunofluorescence microscopy of wild type and cdc8 gene disruptants indicates that cdc8 tropomyosin is present in two distinct cellular distributions: in dispersed patches, and during cytokinesis as a transient medial band. Collectively these results indicate that cdc8 tropomyosin has a specialized role which, we suggest, is to form part of the F-actin contractile ring at cytokinesis. These results establish the basis for further genetic studies of cytokinesis and of contractile protein function in S. pombe.","authors":"Balasubramanian MK, Helfman DM, Hemmingsen SM","authors_abbrev":"Balasubramanian MK et al.","pubmed_publication_date":"05 Nov 1992","pubmed_entrez_date":"1992-11-05","publication_year":"1992","canto_session_key":"82154f75e067e7cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-09-17 14:34:38","canto_approved_date":"2020-01-22 14:25:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-05 09:16:27","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-17"},{"uniquename":"PMID:23221635","title":"Implication of the SMN complex in the biogenesis and steady state level of the signal recognition particle.","citation":"Nucleic Acids Res 2013 Jan;41(2):1255-72","abstract":"Spinal muscular atrophy is a severe motor neuron disease caused by reduced levels of the ubiquitous Survival of MotoNeurons (SMN) protein. SMN is part of a complex that is essential for spliceosomal UsnRNP biogenesis. Signal recognition particle (SRP) is a ribonucleoprotein particle crucial for co-translational targeting of secretory and membrane proteins to the endoplasmic reticulum. SRP biogenesis is a nucleo-cytoplasmic multistep process in which the protein components, except SRP54, assemble with 7S RNA in the nucleolus. Then, SRP54 is incorporated after export of the pre-particle into the cytoplasm. The assembly factors necessary for SRP biogenesis remain to be identified. Here, we show that 7S RNA binds to purified SMN complexes in vitro and that SMN complexes associate with SRP in cellular extracts. We identified the RNA determinants required. Moreover, we report a specific reduction of 7S RNA levels in the spinal cord of SMN-deficient mice, and in a Schizosaccharomyces pombe strain carrying a temperature-degron allele of SMN. Additionally, microinjected antibodies directed against SMN or Gemin2 interfere with the association of SRP54 with 7S RNA in Xenopus laevis oocytes. Our data show that reduced levels of the SMN protein lead to defect in SRP steady-state level and describe the SMN complex as the first identified cellular factor required for SRP biogenesis.","doi":"10.1093/nar/gks1224","authors":"Piazzon N, Schlotter F, Lefebvre S, Dodré M, Méreau A, Soret J, Besse A, Barkats M, Bordonné R, Branlant C, Massenet S","authors_abbrev":"Piazzon N et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2012-12-11","publication_year":"2013","canto_session_key":"f0e36621b9f61ff1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-06-12 16:35:35","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-08-08 09:21:18","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"vw253@cam.ac.uk","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.02","SPNCRNA.98","SPAC2G11.08c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2013-08-08"},{"uniquename":"PMID:16916637","title":"Constraining G1-specific transcription to late G1 phase: the MBF-associated corepressor Nrm1 acts via negative feedback.","citation":"Mol Cell 2006 Aug;23(4):483-96","abstract":"G1-specific transcription in yeast depends upon SBF and MBF. We have identified Nrm1 (negative regulator of MBF targets 1), as a stable component of MBF. NRM1 (YNR009w), an MBF-regulated gene expressed during late G1 phase, associates with G1-specific promoters via MBF. Transcriptional repression upon exit from G1 phase requires both Nrm1 and MBF. Inactivation of Nrm1 results in prolonged expression of MBF-regulated transcripts and leads to hydroxyurea (HU) resistance and enhanced bypass of rad53Delta- and mec1Delta-associated lethality. Constitutive expression of a stabilized form of Nrm1 represses MBF targets and leads to HU sensitivity. The fission yeast homolog SpNrm1, encoded by the MBF target gene nrm1(+) (SPBC16A3.07c), binds to MBF target genes and acts as a corepressor. In both yeasts, MBF represses G1-specific transcription outside of G1 phase. A negative feedback loop involving Nrm1 bound to MBF leads to transcriptional repression as cells exit G1 phase.","authors":"de Bruin RA, Kalashnikova TI, Chahwan C, McDonald WH, Wohlschlegel J, Yates J, Russell P, Wittenberg C","authors_abbrev":"de Bruin RA et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-19","publication_year":"2006","canto_session_key":"11e42e4be40ab42d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-07-24 14:52:14","canto_approved_date":"2024-07-24 14:52:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-24 14:52:08","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.07c","SPBC336.12c","SPAC22F3.09c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2024-07-24"},{"uniquename":"PMID:26801560","title":"Ribosomal protein methyltransferases in the yeast Saccharomyces cerevisiae: Roles in ribosome biogenesis and translation.","citation":"Biochem Biophys Res Commun 2016 Feb 12;470(3):552-557","abstract":"A significant percentage of the methyltransferasome in Saccharomyces cerevisiae and higher eukaryotes is devoted to methylation of the translational machinery. Methylation of the RNA components of the translational machinery has been studied extensively and is important for structure stability, ribosome biogenesis, and translational fidelity. However, the functional effects of ribosomal protein methylation by their cognate methyltransferases are still largely unknown. Previous work has shown that the ribosomal protein Rpl3 methyltransferase, histidine protein methyltransferase 1 (Hpm1), is important for ribosome biogenesis and translation elongation fidelity. In this study, yeast strains deficient in each of the ten ribosomal protein methyltransferases in S. cerevisiae were examined for potential defects in ribosome biogenesis and translation. Like Hpm1-deficient cells, loss of four of the nine other ribosomal protein methyltransferases resulted in defects in ribosomal subunit synthesis. All of the mutant strains exhibited resistance to the ribosome inhibitors anisomycin and/or cycloheximide in plate assays, but not in liquid culture. Translational fidelity assays measuring stop codon readthrough, amino acid misincorporation, and programmed -1 ribosomal frameshifting, revealed that eight of the ten enzymes are important for translation elongation fidelity and the remaining two are necessary for translation termination efficiency. Altogether, these results demonstrate that ribosomal protein methyltransferases in S. cerevisiae play important roles in ribosome biogenesis and translation.","doi":"10.1016/j.bbrc.2016.01.107","authors":"Al-Hadid Q, White J, Clarke S","authors_abbrev":"Al-Hadid Q et al.","pubmed_publication_date":"12 Feb 2016","pubmed_entrez_date":"2016-01-24","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16C6.01c","SPAC1071.05"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:11501416","title":"Spontaneous and radical-induced plasma membrane lipid peroxidation in differently oxidant-sensitive yeast species and its suppression by antioxidants.","citation":"Folia Microbiol (Praha) 2000;45(6):509-14","abstract":"Formation of thiobarbituric acid-reactive substances (TBRS; nmol/mg lipids) indicative of lipid peroxidation was measured in whole cells and in isolated plasma membrane lipids from three yeast species differing in oxidant sensitivity (Schizosaccharomyces pombe, Saccharomyces cerevisiae and Rhodotorula glutinis) after exposure to the Fenton reagent, FeII, H2O2, tert-butyl hydroperoxide (TBHP) and azo compounds (AAPH, ACHN). In whole cells, spontaneous TBRS formation rose in the sequence S. pombe < S. cerevisiae < R. glutinis (1:approximately 5:approximately 7). Oxidants increased the TBRS production 13-18 fold in the sequence FeII approximately TBHP > AAPH approximately ACHN approximately Fe-Fenton > H2O2. This increase need not be solely due to increased lipid peroxidation. In isolated plasma membrane lipids from all three species, the spontaneous TBRS production referred to 1 mg lipids was 9-13-fold higher than in whole cells. In S. pombe lipids, only TBHP increased the TBRS production. In lipids from S. cerevisiae and R. glutinis, all added oxidants increased the spontaneous TBRS production 2-3 times in the sequence TBHP > ACHN > AAPH > FeII > Fe-Fenton > H2O2. Oxidant-induced TBRS production in both whole cells and isolated membrane lipids was partially suppressed by the lipid peroxidation inhibitors 2,6-di-tert-butyl-4-methylphenol (\"butylated hydroxytoluene\"; BHT) and the newly synthesized PYA12 compound. Both agents were more effective in isolated lipids than in whole cells and against OH.-producing than against ROO.- or RO.-producing oxidants. Yeast membrane lipids, which are generally poor in polyunsaturated fatty acids, are thus subject to perceptible lipid peroxidation.","authors":"Krasowska A, Lukaszewicz M, Oświecimska M, Witek S, Sigler K","authors_abbrev":"Krasowska A et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2001-08-15","publication_year":"2000","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41482935","title":"Overproduction of a nuclear export signal in fission yeast promotes nuclear expansion through microtubules.","citation":"FEBS Lett 2026 Jan 03;","abstract":"In eukaryotes, nuclear size scales with cell size, maintaining a constant nucleocytoplasmic volume ratio, known as the N/C ratio. Although nucleocytoplasmic transport plays a crucial role in nuclear size control, the underlying mechanisms remain elusive. Here, we investigated the impact of overexpression of a nuclear export signal (NES) fused with GFP (NES-GFP) in fission yeast on nuclear size. The overexpression of NES-GFP disrupts nuclear export, leading to the nuclear accumulation of cargo proteins and the formation of intranuclear microtubule bundles, thereby increasing the nuclear volume to cell volume (N/C) ratio dependent on nuclear import and microtubule nucleation. Enhanced formation of intranuclear microtubule bundles in cells overexpressing NES-GFP further accelerates nuclear expansion. We propose that membrane tension in the nucleus plays an important role in nuclear size control.","doi":"10.1002/1873-3468.70267","authors":"Fujimoto T, Mizunuma M, Kume K","authors_abbrev":"Fujimoto T et al.","pubmed_publication_date":"03 Jan 2026","pubmed_entrez_date":"2026-01-03","publication_year":"2026","canto_session_key":"c1e0bbbcdc2b6e0c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-01-04 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35354597","title":"Quantitative analysis of nuclear pore complex organization in  Schizosaccharomyces pombe .","citation":"Life Sci Alliance 2022 Jul;5(7)","abstract":"The number, distribution, and composition of nuclear pore complexes (NPCs) in the nuclear envelope varies between cell types and changes during cellular differentiation and in disease. To understand how NPC density and organization are controlled, we analyzed the NPC number and distribution in the fission yeast  Schizosaccharomyces pombe  using structured illumination microscopy. The small size of yeast nuclei, genetic features of fungi, and our robust image analysis pipeline allowed us to study NPCs in intact nuclei under multiple conditions. Our data revealed that NPC density is maintained across a wide range of nuclear sizes. Regions of reduced NPC density are observed over the nucleolus and surrounding the spindle pole body (SPB). Lem2-mediated tethering of the centromeres to the SPB is required to maintain NPC exclusion near SPBs. These findings provide a quantitative understanding of NPC number and distribution in  S. pombe  and show that interactions between the centromere and the nuclear envelope influences local NPC distribution.","doi":"10.26508/lsa.202201423","authors":"Varberg JM, Unruh JR, Bestul AJ, Khan AA, Jaspersen SL","authors_abbrev":"Varberg JM et al.","pubmed_publication_date":"Jul 2022","pubmed_entrez_date":"2022-03-31","publication_year":"2022","canto_session_key":"0e4eff4ea2905045","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-31 08:05:55","canto_approved_date":"2024-04-10 09:11:59","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-25 13:48:25","canto_added_date":"2022-04-02 00:15:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":27,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.04","SPCC1620.11","SPCC285.13c","SPAC14C4.05c","SPCC63.08c","SPBC3B8.10c","SPCC737.03c","SPBC13A2.02","SPAC24H6.05","SPBC17G9.04c","SPAC1486.04c","SPBC11B10.09","SPAC4F10.18","SPBC2G2.14","SPAC26A3.15c","SPBP8B7.24c","SPAC18G6.10","SPCC18B5.03"],"gene_count":18,"ltp_gene_count":17,"approved_date":"2024-03-31"},{"uniquename":"PMID:19221197","title":"The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria.","citation":"J Cell Biol 2009 Feb 23;184(4):583-96","abstract":"Prohibitin ring complexes in the mitochondrial inner membrane regulate cell proliferation as well as the dynamics and function of mitochondria. Although prohibitins are essential in higher eukaryotes, prohibitin-deficient yeast cells are viable and exhibit a reduced replicative life span. Here, we define the genetic interactome of prohibitins in yeast using synthetic genetic arrays, and identify 35 genetic interactors of prohibitins (GEP genes) required for cell survival in the absence of prohibitins. Proteins encoded by these genes include members of a conserved protein family, Ups1 and Gep1, which affect the processing of the dynamin-like GTPase Mgm1 and thereby modulate cristae morphogenesis. We show that Ups1 and Gep1 regulate the levels of cardiolipin and phosphatidylethanolamine in mitochondria in a lipid-specific but coordinated manner. Lipid profiling by mass spectrometry of GEP-deficient mitochondria reveals a critical role of cardiolipin and phosphatidylethanolamine for survival of prohibitin-deficient cells. We propose that prohibitins control inner membrane organization and integrity by acting as protein and lipid scaffolds.","doi":"10.1083/jcb.200810189","authors":"Osman C, Haag M, Potting C, Rodenfels J, Dip PV, Wieland FT, Brügger B, Westermann B, Langer T","authors_abbrev":"Osman C et al.","pubmed_publication_date":"23 Feb 2009","pubmed_entrez_date":"2009-02-18","publication_year":"2009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1782.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU009741","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12221110","title":"Role of fission yeast Tup1-like repressors and Prr1 transcription factor in response to salt stress.","citation":"Mol Biol Cell 2002 Sep;13(9):2977-89","abstract":"In Schizosaccharomyces pombe, the Sty1 mitogen-activated protein kinase and the Atf1 transcription factor control transcriptional induction in response to elevated salt concentrations. Herein, we demonstrate that two repressors, Tup11 and Tup12, and the Prr1 transcription factor also function in the response to salt shock. We find that deletion of both tup genes together results in hypersensitivity to elevated cation concentrations (K(+) and Ca(2+)) and we identify cta3(+), which encodes an intracellular cation transporter, as a novel stress gene whose expression is positively controlled by the Sty1 pathway and negatively regulated by Tup repressors. The expression of cta3(+) is maintained at low levels by the Tup repressors, and relief from repression requires the Sty1, Atf1, and Prr1. Prr1 is also required for KCl-mediated induction of several other Sty1-dependent genes such as gpx1(+) and ctt1(+). Surprisingly, the KCl-mediated induction of cta3(+) expression occurs independently of Sty1 in a tup11Delta tup12Delta mutant and so the Tup repressors link induction to the Sty1 pathway. We also report that in contrast to a number of other Sty1- and Atf1-dependent genes, the expression of cta3(+) is induced only by high salt concentrations. However, in the absence of the Tup repressors this specificity is lost and a range of stresses induces cta3(+) expression.","authors":"Greenall A, Hadcroft AP, Malakasi P, Jones N, Morgan BA, Hoffman CS, Whitehall SK","authors_abbrev":"Greenall A et al.","pubmed_publication_date":"Sep 2002","pubmed_entrez_date":"2002-09-11","publication_year":"2002","canto_session_key":"c6f4c320243a46a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-01-05 16:43:55","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-01-05 16:43:37","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":61,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC757.07c","SPBC32F12.03c","SPBC839.06","SPAC18B11.10","SPAC630.14c","SPAC21E11.03c","SPBC29B5.01","SPAC24B11.06c","SPAC8C9.14","SPBC215.05"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2016-01-05"},{"uniquename":"PMID:12083520","title":"The structural basis of riboflavin binding to Schizosaccharomyces pombe 6,7-dimethyl-8-ribityllumazine synthase.","citation":"J Mol Biol 2002 May 17;318(5):1317-29","abstract":"Riboflavin is an essential cofactor in all organisms. Its direct biosynthetic precursor, 6,7-dimethyl-8-ribityllumazine, is synthesised by the enzyme 6,7-dimethyl-8-ribityllumazine synthase. Recently, we have found that the enzyme from Schizosaccharomyces pombe binds riboflavin, the final product of the pathway with a relatively high affinity with a KD of 1.2 microM. Here, we report on the crystal structure of lumazine synthase from S. pombe with bound riboflavin and compare the binding mode with those of the substrate analogue inhibitor 5-nitro-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione and of the product analogue 6-carboxyethyl-7-oxo-8-ribityllumazine. In all complexes the pyrimidinedione moieties of each respective ligand bind in a very similar orientation. Binding of riboflavin additionally involves a stacking interaction of the dimethylbenzene moiety with the side-chain of His94, a highly conserved residue in all lumazine synthases. The enzyme from Bacillus subtilis showed a KD of at least 1 mM whereas the very homologous enzyme from Saccharomyces cerevisiae had a comparable KD of 3.9 microM. Structural comparison of the S. cerevisiae, the S. pombe, and the mutant enzymes suggests that fine tuning of affinity is achieved by influencing this stacking interaction.","authors":"Gerhardt S, Haase I, Steinbacher S, Kaiser JT, Cushman M, Bacher A, Huber R, Fischer M","authors_abbrev":"Gerhardt S et al.","pubmed_publication_date":"17 May 2002","pubmed_entrez_date":"2002-06-27","publication_year":"2002","canto_session_key":"95d3ffba5b299787","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-07 14:49:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-14 15:54:32","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-14","pdb_entries":[{"pdb_id":"1kz4","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Mutant enzyme W63Y Lumazine Synthase from S.pombe","entry_authors":"Gerhardt S,Haase I,Steinbacher S,Kaiser JT,Cushman M,Bacher A,Huber R,Fischer M","entry_authors_abbrev":"Gerhardt S et al.","reference_uniquename":"PMID:12083520","experimental_method":"X-ray","resolution":"3.1"},{"pdb_id":"1kz9","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Mutant Enzyme L119F Lumazine Synthase from S.pombe","entry_authors":"Gerhardt S,Haase I,Steinbacher S,Kaiser JT,Cushman M,Bacher A,Huber R,Fischer M","entry_authors_abbrev":"Gerhardt S et al.","reference_uniquename":"PMID:12083520","experimental_method":"X-ray","resolution":"3.1"},{"pdb_id":"1kz1","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Mutant enzyme W27G Lumazine Synthase from S.pombe","entry_authors":"Gerhardt S,Haase I,Steinbacher S,Kaiser JT,Cushman M,Bacher A,Huber R,Fischer M","entry_authors_abbrev":"Gerhardt S et al.","reference_uniquename":"PMID:12083520","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"1kz6","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Mutant enzyme W63Y/L119F Lumazine Synthase from S.pombe","entry_authors":"Gerhardt S,Haase I,Steinbacher S,Kaiser JT,Cushman M,Bacher A,Huber R,Fischer M","entry_authors_abbrev":"Gerhardt S et al.","reference_uniquename":"PMID:12083520","experimental_method":"X-ray","resolution":"2.7"},{"pdb_id":"1kyv","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Lumazine Synthase from S.pombe bound to riboflavin","entry_authors":"Gerhardt S,Haase I,Steinbacher S,Kaiser JT,Cushman M,Bacher A,Huber R,Fischer M","entry_authors_abbrev":"Gerhardt S et al.","reference_uniquename":"PMID:12083520","experimental_method":"X-ray","resolution":"2.4"},{"pdb_id":"1kyy","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Lumazine Synthase from S.pombe bound to nitropyrimidinedione","entry_authors":"Gerhardt S,Haase I,Steinbacher S,Kaiser JT,Cushman M,Bacher A,Huber R,Fischer M","entry_authors_abbrev":"Gerhardt S et al.","reference_uniquename":"PMID:12083520","experimental_method":"X-ray","resolution":"2.4"},{"pdb_id":"1kyx","gene_chains":[{"gene_uniquename":"SPBC409.13","chain":"A/B/C/D/E","position":"1-159"}],"title":"Lumazine Synthase from S.pombe bound to carboxyethyllumazine","entry_authors":"Gerhardt S,Haase I,Steinbacher S,Kaiser JT,Cushman M,Bacher A,Huber R,Fischer M","entry_authors_abbrev":"Gerhardt S et al.","reference_uniquename":"PMID:12083520","experimental_method":"X-ray","resolution":"2.6"}]},{"uniquename":"PMID:18245278","title":"Bot1p is required for mitochondrial translation, respiratory function, and normal cell morphology in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2008 Apr;7(4):619-29","abstract":"Maintenance of cell morphology is essential for normal cell function. For eukaryotic cells, a growing body of recent evidence highlights a close interdependence between mitochondrial function, the cytoskeleton, and cell cycle control mechanisms; however, the molecular details of this interconnection are still not completely understood. We have identified a novel protein, Bot1p, in the fission yeast Schizosaccharomyces pombe. The bot1 gene is essential for cell viability. bot1Delta mutant cells expressing lower levels of Bot1p display altered cell size and cell morphology and a disrupted actin cytoskeleton. Bot1p localizes to the mitochondria in live cells and cofractionates with purified mitochondrial ribosomes. Reduced levels of Bot1p lead to mitochondrial fragmentation, decreased mitochondrial protein translation, and a corresponding decrease in cell respiration. Overexpression of Bot1p results in cell cycle delay, with increased cell size and cell length and enhanced cell respiration rate. Our results show that Bot1p has a novel function in the control of cell respiration by acting on the mitochondrial protein synthesis machinery. Our observations also indicate that in fission yeast, alterations of mitochondrial function are linked to changes in cell cycle and cell morphology control mechanisms.","doi":"10.1128/EC.00048-07","authors":"Wiley DJ, Catanuto P, Fontanesi F, Rios C, Sanchez N, Barrientos A, Verde F","authors_abbrev":"Wiley DJ et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-02-05","publication_year":"2008","canto_session_key":"6eb1454735373927","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-23 15:47:29","canto_approved_date":"2022-07-27 21:21:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-18 11:12:11","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.16c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-23"},{"uniquename":"PMID:36526269","title":"Fission yeast cells mix parental mitochondria in a progressive manner during meiosis.","citation":"J Mol Cell Biol 2023 Apr 06;14(11)","abstract":"Mitochondria in many fungi are inherited uniparentally during meiosis. It has remained unclear whether parental mitochondria in the fission yeast Schizosaccharomyces pombe are inherited uniparentally or biparentally. Here, we assessed the mixing of parental mitochondria carefully by live-cell microscopy and developed an algorithm to determine the degree of mitochondrial mixing in a quantitative manner. We found that parental mitochondria in fission yeast cells were mixed progressively as meiosis progressed. Moreover, we established that mitochondrial fission and the size of the conjugation neck are the limiting factors in restricting the mixing of parental mitochondria. We further employed a combination of quantitative polymerase chain reaction, fluorescent live-cell microscopy, and transmission electron microscopy approaches to examine the mitochondrial inheritance of progeny cells derived from a cross between wild-type and Rho0 (mitochondrial DNA absent) cells. The results show that all progeny cells of the cross carry mitochondrial DNA. Hence, our data support the model in which parental mitochondria in the fission yeast S. pombe are inherited biparentally during meiosis.","doi":"10.1093/jmcb/mjac070","authors":"Wu D, Chu Y, Wei W, Liu L, Fu C","authors_abbrev":"Wu D et al.","pubmed_publication_date":"06 Apr 2023","pubmed_entrez_date":"2022-12-16","publication_year":"2023","canto_session_key":"ac7f9663d58fb5e7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-12-18 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15367656","title":"Swi1 and Swi3 are components of a replication fork protection complex in fission yeast.","citation":"Mol Cell Biol 2004 Oct;24(19):8342-55","abstract":"Swi1 is required for programmed pausing of replication forks near the mat1 locus in the fission yeast Schizosaccharomyces pombe. This fork pausing is required to initiate a recombination event that switches mating type. Swi1 is also needed for the replication checkpoint that arrests division in response to fork arrest. How Swi1 accomplishes these tasks is unknown. Here we report that Swi1 copurifies with a 181-amino-acid protein encoded by swi3(+). The Swi1-Swi3 complex is required for survival of fork arrest and for activation of the replication checkpoint kinase Cds1. Association of Swi1 and Swi3 with chromatin during DNA replication correlated with movement of the replication fork. swi1Delta and swi3Delta mutants accumulated Rad22 (Rad52 homolog) DNA repair foci during replication. These foci correlated with the Rad22-dependent appearance of Holliday junction (HJ)-like structures in cells lacking Mus81-Eme1 HJ resolvase. Rhp51 and Rhp54 homologous recombination proteins were not required for viability in swi1Delta or swi3Delta cells, indicating that the HJ-like structures arise from single-strand DNA gaps or rearranged forks instead of broken forks. We propose that Swi1 and Swi3 define a fork protection complex that coordinates leading- and lagging-strand synthesis and stabilizes stalled replication forks.","authors":"Noguchi E, Noguchi C, McDonald WH, Yates JR, Russell P","authors_abbrev":"Noguchi E et al.","pubmed_publication_date":"Oct 2004","pubmed_entrez_date":"2004-09-16","publication_year":"2004","canto_session_key":"ef57da759b1d97c2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2020-02-18 14:53:32","canto_approved_date":"2023-12-31 17:17:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-10 09:23:01","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":73,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.03c","SPBC25H2.13c","SPAC644.14c","SPAC30D11.10","SPCC1259.13","SPBC19C7.09c","SPBC336.04","SPBC3E7.08c","SPBC30D10.04","SPCC18B5.11c","SPCC4G3.05c","SPBC216.06c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2020-02-18"},{"uniquename":"EMBL:AB084839","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.27","SPNCRNA.28"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:2792737","title":"A mating-type-specific sterility gene map1 is required for transcription of a mating-type gene mat1-Pi in the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 1989 Jul 01;51(1):45-8","abstract":"Transcriptional activation of the mating-type gene mat1-Pi essential for meiosis in the fission yeast Schizosaccharomyces pombe was studied. A homozygous diploid harboring the mutation at the h+-specific sterility gene, map1, was arrested before premeiotic DNA synthesis in the nitrogen-free sporulation medium. Transcription of mat1-Pi was totally absent in the map1 mutant. The mei2 gene encoding a positive regulator for meiosis was normally transcribed in the map1 mutant, suggesting that the map1 function was specific to mat1-Pi.","authors":"Fujioka H, Shimoda C","authors_abbrev":"Fujioka H et al.","pubmed_publication_date":"01 Jul 1989","pubmed_entrez_date":"1989-07-01","publication_year":"1989","canto_session_key":"1cfea3361eac50c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-24 07:26:37","canto_approved_date":"2022-06-01 14:48:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-03-14 15:02:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMTR.01","SPMTR.02","SPAC11E3.06"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2014-06-24"},{"uniquename":"PMID:17037208","title":"[Continuous ethanol fermentation coupled with recycling of yeast flocs].","citation":"Sheng Wu Gong Cheng Xue Bao 2006 Sep;22(5):816-20","abstract":"A continuous ethanol fermentation system composed of three-stage tanks in series coupled with two sedimentation tanks was established. A self-flocculating yeast strain developed by protoplast fusion from Saccharomyces cerevisiae and Schizosaccharomyces pombe was applied. Two-stage enzymatic hydrolysate of corn powder containing 220g/L of reducing sugar, supplemented with 1.5g/L (NH4)2HPO4 and 2.5g/L KH2PO4, was used as the ethanol fermentation substrate and fed into the first fermentor at the dilution rate of 0.057h(-1). The yeast flocs separated by sedimentation were recycled into the first fermentor as two different models: activation-recycle and direct recycle. The quasi-steady states were obtained for both operation models after the fermentation systems experienced short periods of transitions. Activation process helped enhance the performance of ethanol fermentation at the high dilution rates. The broth containing more than 101g/L ethanol, 3.2g/L residual reducing sugar and 7.7g/L residual total sugar was produced. The ethanol productivity was calculated to be 5.77g/(L x h), which increased by more than 70% compared with that achieved in the same tank in series system without recycling of yeast cells.","authors":"Wang B, Ge XM, Li N, Bai FW","authors_abbrev":"Wang B et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-10-14","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41259369","title":"Hydroxyurea induces an oxidative stress response that triggers ER expansion and cytoplasmic protein aggregation.","citation":"PLoS Biol 2025 Nov 19;23(11):e3003493","abstract":"The endoplasmic reticulum (ER) lumen provides the proper redox environment for disulfide bond formation, which is essential for the correct folding of proteins entering the secretory pathway and forming membranes. However, the precise mechanisms by which disruptions in protein folding within the ER activate proteostatic mechanisms remain to be fully elucidated. In this study, we demonstrate that in Schizosaccharomyces pombe the antineoplastic agent hydroxyurea (HU) induces a transient perinuclear ER expansion, Bip1 accumulation, and the clustering of nuclear pore complexes in a specific region of the nuclear envelope. This striking phenotype is mimicked by diamide (DIA), a specific inducer of thiol stress, and can be prevented or rapidly reversed by dithiothreitol, a reducing agent, suggesting that ER expansion results from disulfide stress. Furthermore, HU or DIA treatments resulted in the accumulation of misfolded proteins in cytoplasmic foci containing Hsp104 disaggregase and Hsp70/Ssa1 chaperones. Our data show that HU impacts redox-dependent protein folding, impairs the secretory pathway, and activates specific proteostatic mechanisms in both the ER and the cytoplasm.","doi":"10.1371/journal.pbio.3003493","authors":"Sánchez-Molina A, Bernal M, Posligua-García JD, Pérez-Pulido AJ, de Cubas L, Hidalgo E, Valdivieso MH, Salas-Pino S, Daga RR","authors_abbrev":"Sánchez-Molina A et al.","pubmed_publication_date":"19 Nov 2025","pubmed_entrez_date":"2025-11-19","publication_year":"2025","canto_session_key":"7aff55d541c43802","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana Sánchez-Molina","canto_first_approved_date":"2026-02-26 09:47:21","canto_approved_date":"2026-02-26 09:47:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-02-06 10:57:16","canto_added_date":"2025-11-20 00:25:05","annotation_curators":[{"name":"Ana Sánchez-Molina","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":28,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.04","SPCC965.07c","SPAC167.01","SPBC3E7.02c","SPAC23A1.08c","SPAC1783.07c","SPCC1281.01","SPBP8B7.24c","SPBC3B9.16c","SPCC1840.02c","SPAC22F3.10c","SPBC1683.09c","SPCC830.08c","SPBC1198.05","SPBC1604.18c","SPBC609.04","SPAC2G11.06","SPAC13G7.02c","SPBC691.05c","SPBC16D10.08c","SPCC663.08c","SPAC14C4.05c","SPAC3F10.04","SPBC17A3.07","SPBC25D12.04","SPBPB2B2.06c","SPAC18G6.10","SPBC365.12c","SPCC1322.15","SPAC29B12.03","SPAC26A3.07c","SPBC31A8.01c","SPCC162.08c","SPCC576.08c","SPAC1F8.03c","SPCC736.04c","SPCC737.03c","SPBC18A7.01","SPAC19G12.10c","SPBC106.02c","SPCC550.14","SPAC24B11.11c","SPAC1F7.05","SPAC24H6.05","SPAC22A12.15c","SPAC926.04c","SPBC19G7.05c","SPBC1604.08c","SPAC1786.03","SPAC9E9.11","SPAC1F5.02"],"gene_count":51,"ltp_gene_count":27,"approved_date":"2026-02-26"},{"uniquename":"PMID:9495778","title":"Characterization of mutants devoid of neutral trehalase activity in the fission yeast Schizosaccharomyces pombe: partial protection from heat shock and high-salt stress.","citation":"J Bacteriol 1998 Mar;180(5):1342-5","abstract":"Exposure of cells of Schizosaccharomyces pombe to heat shock or osmotic upshift results in an increased level of neutral trehalase activity, which is responsible for hydrolysis of intracellular trehalose. We constructed S. pombe mutants lacking neutral trehalase activity by gene replacement at the newly defined ntp1+ locus. Analysis of these mutants revealed that a twofold increase in trehalose accumulation, enhanced acquired thermoresistance, and marked salt tolerance characterized their ability to grow in liquid and solid media. Analysis of the expression of the trehalase gene under heat shock and osmotic upshift revealed the transcriptional activation of ntp1+ in response to both stresses.","authors":"Cansado J, Soto T, Fernandez J, Vicente-Soler J, Gacto M","authors_abbrev":"Cansado J et al.","pubmed_publication_date":"Mar 1998","pubmed_entrez_date":"1998-03-12","publication_year":"1998","canto_session_key":"5929f42c9869ea6c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-09-07 13:36:11","canto_approved_date":"2019-10-29 13:42:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-09-05 12:27:37","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10","SPBC660.07","SPAC328.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-09-07"},{"uniquename":"PMID:11779789","title":"Counteracting regulation of chromatin remodeling at a fission yeast cAMP response element-related recombination hotspot by stress-activated protein kinase, cAMP-dependent kinase and meiosis regulators.","citation":"Genetics 2001 Dec;159(4):1467-78","abstract":"In fission yeast, an ATF/CREB-family transcription factor Atf1-Pcr1 plays important roles in the activation of early meiotic processes via the stress-activated protein kinase (SAPK) and the cAMP-dependent protein kinase (PKA) pathways. In addition, Atf1-Pcr1 binds to a cAMP responsive element (CRE)-like sequence at the site of the ade6-M26 mutation, which results in local enhancement of meiotic recombination and chromatin remodeling. Here we studied the roles of meiosis-inducing signal transduction pathways in M26 chromatin remodeling. Chromatin analysis revealed that persistent activation of PKA in meiosis inhibited M26 chromatin remodeling, suggesting that the PKA pathway represses M26 chromatin remodeling. The SAPK pathway activated M26 chromatin remodeling, since mutants lacking a component of this pathway, the Wis1 or Spc1/Sty1 kinases, had no M26 chromatin remodeling. M26 chromatin remodeling also required the meiosis regulators Mei2 and Mei3 but not the subsequently acting regulators Sme2 and Mei4, suggesting that induction of M26 chromatin remodeling needs meiosis-inducing signals before premeiotic DNA replication. Similar meiotic chromatin remodeling occurred meiotically around natural M26 heptamer sequences. These results demonstrate the coordinated action of genetic and physiological factors required to remodel chromatin in preparation for high levels of meiotic recombination and eukaryotic cellular differentiation.","authors":"Mizuno K, Hasemi T, Ubukata T, Yamada T, Lehmann E, Kohli J, Watanabe Y, Iino Y, Yamamoto M, Fox ME, Smith GR, Murofushi H, Shibata T, Ohta K","authors_abbrev":"Mizuno K et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2002-01-10","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5838699","title":"Autoradiographic analysis of regional cell wall growth of yeasts. Schizosaccharomyces pombe.","citation":"Exp Cell Res 1965 Sep;39(2):613-24","abstract":"","authors":"Johnson BF","authors_abbrev":"Johnson BF","pubmed_publication_date":"Sep 1965","pubmed_entrez_date":"1965-09-01","publication_year":"1965","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10545451","title":"spp42, identified as a classical suppressor of prp4-73, which encodes a kinase involved in pre-mRNA splicing in fission yeast, is a homologue of the splicing factor Prp8p.","citation":"Genetics 1999 Nov;153(3):1183-91","abstract":"We have identified two classical extragenic suppressors, spp41 and spp42, of the temperature sensitive (ts) allele prp4-73. The prp4(+) gene of Schizosaccharomyces pombe encodes a protein kinase. Mutations in both suppressor genes suppress the growth and the pre-mRNA splicing defect of prp4-73(ts) at the restrictive temperature (36 degrees ). spp41 and spp42 are synthetically lethal with each other in the presence of prp4-73(ts), indicating a functional relationship between spp41 and spp42. The suppressor genes were mapped on the left arm of chromosome I proximal to the his6 gene. Based on our mapping data we isolated spp42 by screening PCR fragments for functional complementation of the prp4-73(ts) mutant at the restrictive temperature. spp42 encodes a large protein (p275), which is the homologue of Prp8p. This protein has been shown in budding yeast and mammalian cells to be a bona fide pre-mRNA splicing factor. Taken together with other recent genetic and biochemical data, our results suggest that Prp4 kinase plays an important role in the formation of catalytic spliceosomes.","authors":"Schmidt H, Richert K, Drakas RA, Käufer NF","authors_abbrev":"Schmidt H et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-11-05","publication_year":"1999","canto_session_key":"5e8be86dbefad66c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-06-09 16:34:35","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-30 14:24:18","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.02c","SPAC4F8.12c","SPAC9.03c","SPCC777.14"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2014-07-30"},{"uniquename":"PMID:2900688","title":"Cyclin in fission yeast.","citation":"Cell 1988 Sep 09;54(6):738-40","abstract":"","authors":"","authors_abbrev":"","pubmed_publication_date":"09 Sep 1988","pubmed_entrez_date":"1988-09-09","publication_year":"1988","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32802966","title":"Phosphoregulation of tropomyosin-actin interaction revealed using a genetic code expansion strategy.","citation":"Wellcome Open Res 2020;5:161","abstract":"Tropomyosins are coiled-coil proteins that regulate the stability and / or function of actin cytoskeleton in muscle and non-muscle cells through direct binding of actin filaments. Recently, using the fission yeast, we discovered a new mechanism by which phosphorylation of serine 125 of tropomyosin (Cdc8), reduced its affinity for actin filaments thereby providing access for the actin severing protein Adf1/Cofilin to actin filaments causing instability of actin filaments. Here we use a genetic code expansion strategy to directly examine this conclusion. We produced in  Escherichia coli  Cdc8-tropomyosin bearing a phosphate group on Serine-125 (Cdc8  PS125 ), using an orthogonal tRNA-tRNA synthetase pair that directly incorporates phosphoserine into proteins in response to a UAG codon in the corresponding mRNA. We show using total internal reflection (TIRF) microscopy that, whereas  E.coli  produced Cdc8  PS125  does not bind actin filaments, Cdc8  PS125  incubated with lambda phosphatase binds actin filaments. This work directly demonstrates that a phosphate moiety present on serine 125 leads to decreased affinity of Cdc8-tropomyosin for actin filaments. We also extend the work to demonstrate the usefulness of the genetic code expansion approach in imaging actin cytoskeletal components.","doi":"10.12688/wellcomeopenres.16082.1","authors":"Palani S, Koester D, Balasubramanian MK","authors_abbrev":"Palani S et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-08-18","publication_year":"2020","canto_session_key":"1dad97f0dabd8938","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-08-19 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32543370","title":" Pyphe , a python toolbox for assessing microbial growth and cell viability in high-throughput colony screens.","citation":"Elife 2020 Jun 16;9","abstract":"Microbial fitness screens are a key technique in functional genomics. We present an all-in-one solution,  pyphe , for automating and improving data analysis pipelines associated with large-scale fitness screens, including image acquisition and quantification, data normalisation, and statistical analysis.  Pyphe  is versatile and processes fitness data from colony sizes, viability scores from phloxine B staining or colony growth curves, all obtained with inexpensive transilluminating flatbed scanners. We apply  pyphe  to show that the fitness information contained in late endpoint measurements of colony sizes is similar to maximum growth slopes from time series. We phenotype gene-deletion strains of fission yeast in 59,350 individual fitness assays in 70 conditions, revealing that colony size and viability provide complementary, independent information. Viability scores obtained from quantifying the redness of phloxine-stained colonies accurately reflect the fraction of live cells within colonies.  Pyphe  is user-friendly, open-source and fully documented, illustrated by applications to diverse fitness analysis scenarios.","doi":"10.7554/eLife.55160","authors":"Kamrad S, Rodríguez-López M, Cotobal C, Correia-Melo C, Ralser M, Bähler J","authors_abbrev":"Kamrad S et al.","pubmed_publication_date":"16 Jun 2020","pubmed_entrez_date":"2020-06-17","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-06-18 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31641022","title":"The cytosolic form of aspartate aminotransferase is required for full activation of TOR complex 1 in fission yeast.","citation":"J Biol Chem 2019 Nov 29;294(48):18244-18255","abstract":"The evolutionarily conserved TOR complex 1 (TORC1) activates cell growth and proliferation in response to nutritional signals. In the fission yeast  Schizosaccharomyces pombe , TORC1 is essential for vegetative growth, and its activity is regulated in response to nitrogen quantity and quality. Yet, how TORC1 senses nitrogen is poorly understood. Rapamycin, a specific TOR inhibitor, inhibits growth in  S. pombe  only under conditions in which the activity of TORC1 is compromised. In a genetic screen for rapamycin-sensitive mutations, we isolated  caa1-1 , a loss-of-function mutation of the cytosolic form of aspartate aminotransferase (Caa1). We demonstrate that loss of  caa1  +  partially mimics loss of TORC1 activity and that Caa1 is required for full TORC1 activity. Disruption of  caa1  +  resulted in aspartate auxotrophy, a finding that prompted us to assess the role of aspartate in TORC1 activation. We found that the amino acids glutamine, asparagine, arginine, aspartate, and serine activate TORC1 most efficiently following nitrogen starvation. The glutamine synthetase inhibitor l-methionine sulfoximine abolished the ability of asparagine, arginine, aspartate, or serine, but not that of glutamine, to induce TORC1 activity, consistent with a central role for glutamine in activating TORC1. Neither addition of aspartate nor addition of glutamine restored TORC1 activity in  caa1 -deleted cells or in cells carrying a Caa1 variant with a catalytic site substitution, suggesting that the catalytic activity of Caa1 is required for TORC1 activation. Taken together, our results reveal the contribution of the key metabolic enzyme Caa1 to TORC1 activity in  S. pombe .","doi":"10.1074/jbc.RA119.010101","authors":"Reidman S, Cohen A, Kupiec M, Weisman R","authors_abbrev":"Reidman S et al.","pubmed_publication_date":"29 Nov 2019","pubmed_entrez_date":"2019-10-24","publication_year":"2019","canto_session_key":"3fc0a58cd1accb51","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronit Weisman","canto_first_approved_date":"2019-12-19 14:06:05","canto_approved_date":"2019-12-19 14:07:36","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-28 14:03:17","canto_added_date":"2019-10-25 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ronit Weisman","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.07c","SPBC337.13c","SPAC10F6.13c","SPBC839.17c","SPBC30D10.10c","SPBC106.10","SPCC4G3.08","SPBC725.01"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2019-12-19"},{"uniquename":"PMID:26494834","title":"AnABlast: a new in silico strategy for the genome-wide search of novel genes and fossil regions.","citation":"DNA Res 2015 Dec;22(6):439-49","abstract":"Genome annotation, assisted by computer programs, is one of the great advances in modern biology. Nevertheless, the in silico identification of small and complex coding sequences is still challenging. We observed that amino acid sequences inferred from coding-but rarely from non-coding-DNA sequences accumulated alignments in low-stringency BLAST searches, suggesting that this alignments accumulation could be used to highlight coding regions in sequenced DNA. To investigate this possibility, we developed a computer program (AnABlast) that generates profiles of accumulated alignments in query amino acid sequences using a low-stringency BLAST strategy. To validate this approach, all six-frame translations of DNA sequences between every two annotated exons of the fission yeast genome were analysed with AnABlast. AnABlast-generated profiles identified three new copies of known genes, and four new genes supported by experimental evidence. New pseudogenes, ancestral carboxyl- and amino-terminal subtractions, complex gene rearrangements, and ancient fragments of mitDNA and of bacterial origin, were also inferred. Thus, this novel in silico approach provides a powerful tool to uncover new genes, as well as fossil-coding sequences, thus providing insight into the evolutionary history of annotated genomes.","doi":"10.1093/dnares/dsv025","authors":"Jimenez J, Duncan CD, Gallardo M, Mata J, Perez-Pulido AJ","authors_abbrev":"Jimenez J et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-10-24","publication_year":"2015","canto_session_key":"85a5accc68b69077","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-04-05 15:34:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-31 14:09:28","canto_added_date":"2015-10-25 00:19:22","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3B8.10","SPAC22F3.11c","SPAC29A4.23","SPAC11D3.20","SPAPB1A11.06"],"gene_count":5,"ltp_gene_count":0,"approved_date":"2016-03-31"},{"uniquename":"EMBL:SPD143","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22286754","title":"Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography.","citation":"Mol Cell Proteomics 2012 Mar;11(3):M111.014126","abstract":"Chemical cross-linking in combination with mass spectrometric analysis offers the potential to obtain low-resolution structural information from proteins and protein complexes. Identification of peptides connected by a cross-link provides direct evidence for the physical interaction of amino acid side chains, information that can be used for computational modeling purposes. Despite impressive advances that were made in recent years, the number of experimentally observed cross-links still falls below the number of possible contacts of cross-linkable side chains within the span of the cross-linker. Here, we propose two complementary experimental strategies to expand cross-linking data sets. First, enrichment of cross-linked peptides by size exclusion chromatography selects cross-linked peptides based on their higher molecular mass, thereby depleting the majority of unmodified peptides present in proteolytic digests of cross-linked samples. Second, we demonstrate that the use of proteases in addition to trypsin, such as Asp-N, can additionally boost the number of observable cross-linking sites. The benefits of both SEC enrichment and multiprotease digests are demonstrated on a set of model proteins and the improved workflow is applied to the characterization of the 20S proteasome from rabbit and Schizosaccharomyces pombe.","doi":"10.1074/mcp.M111.014126","authors":"Leitner A, Reischl R, Walzthoeni T, Herzog F, Bohn S, Förster F, Aebersold R","authors_abbrev":"Leitner A et al.","pubmed_publication_date":"Mar 2012","pubmed_entrez_date":"2012-01-31","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9655965","title":"[Regulatory proteins of type 1 protein phosphatase].","citation":"Tanpakushitsu Kakusan Koso 1998 Jun;43(8 Suppl):1072-82","abstract":"","authors":"Kotani H, Ito M, Ichikawa K, Nakano T","authors_abbrev":"Kotani H et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-07-10","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19707600","title":"SUMO chain formation is required for response to replication arrest in S. pombe.","citation":"PLoS One 2009 Aug 25;4(8):e6750","abstract":"SUMO is a ubiquitin-like protein that is post-translationally attached to one or more lysine residues on target proteins. Despite having only 18% sequence identity with ubiquitin, SUMO contains the conserved betabetaalphabetabetaalphabeta fold present in ubiquitin. However, SUMO differs from ubiquitin in having an extended N-terminus. In S. pombe the N-terminus of SUMO/Pmt3 is significantly longer than those of SUMO in S. cerevisiae, human and Drosophila. Here we investigate the role of this N-terminal region. We have used two dimensional gel electrophoresis to demonstrate that S. pombe SUMO/Pmt3 is phosphorylated, and that this occurs on serine residues at the extreme N-terminus of the protein. Mutation of these residues (in pmt3-1) results in a dramatic reduction in both the levels of high Mr SUMO-containing species and of total SUMO/Pmt3, indicating that phosphorylation of SUMO/Pmt3 is required for its stability. Despite the significant reduction in high Mr SUMO-containing species, pmt3-1 cells do not display an aberrant cell morphology or sensitivity to genotoxins or stress. Additionally, we demonstrate that two lysine residues in the N-terminus of S. pombe SUMO/Pmt3 (K14 and K30) can act as acceptor sites for SUMO chain formation in vitro. Inability to form SUMO chains results in aberrant cell and nuclear morphologies, including stretched and fragmented chromatin. SUMO chain mutants are sensitive to the DNA synthesis inhibitor, hydroxyurea (HU), but not to other genotoxins, such as UV, MMS or CPT. This implies a role for SUMO chains in the response to replication arrest in S. pombe.","doi":"10.1371/journal.pone.0006750","authors":"Skilton A, Ho JC, Mercer B, Outwin E, Watts FZ","authors_abbrev":"Skilton A et al.","pubmed_publication_date":"25 Aug 2009","pubmed_entrez_date":"2009-08-27","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10207106","title":"Isolation of a mammalian homologue of a fission yeast differentiation regulator.","citation":"Mol Cell Biol 1999 May;19(5):3829-41","abstract":"In the fission yeast Schizosaccharomyces pombe the nrd1(+) gene encoding an RNA binding protein negatively regulates the onset of differentiation. Its biological role is to block differentiation by repressing a subset of the Ste11-regulated genes essential for conjugation and meiosis until the cells reach a critical level of nutrient starvation. By using the phenotypic suppression of the S. pombe temperature-sensitive pat1 mutant that commits lethal haploid meiosis at the restrictive temperature, we have cloned ROD1, a functional homologue of nrd1(+), from rat and human cDNA libraries. Like nrd1(+), ROD1 encodes a protein with four repeats of typical RNA binding domains, though its amino acid homology to Nrd1 is limited. When expressed in the fission yeast, ROD1 behaves in a way that is functionally similar to nrd1(+), being able to repress Ste11-regulated genes and to inhibit conjugation upon overexpression. ROD1 is predominantly expressed in hematopoietic cells or organs of adult and embryonic rat. Like nrd1(+) for fission yeast differentiation, overexpressed ROD1 effectively blocks both 12-O-tetradecanoyl phorbol-13-acetate-induced megakaryocytic and sodium butyrate-induced erythroid differentiation of the K562 human leukemia cells without affecting their proliferative ability. These results suggest a role for ROD1 in differentiation control in mammalian cells. We discuss the possibility that a differentiation control system found in the fission yeast might well be conserved in more complex organisms, including mammals.","authors":"Yamamoto H, Tsukahara K, Kanaoka Y, Jinno S, Okayama H","authors_abbrev":"Yamamoto H et al.","pubmed_publication_date":"May 1999","pubmed_entrez_date":"1999-04-17","publication_year":"1999","canto_session_key":"afb87d52a744eda7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-07-02 13:45:06","canto_approved_date":"2020-02-14 15:30:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-02 13:44:59","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-02"},{"uniquename":"Pfam:PF14880","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC757.15","HGNC:28216"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8632802","title":"Cut2 proteolysis required for sister-chromatid seperation in fission yeast.","citation":"Nature 1996 May 30;381(6581):438-41","abstract":"Although mitotic cyclins are well-known substrates for ubiquitin-mediated proteolysis at the metaphase-anaphase transition, their degradation is not essential for separation of sister chromatids; several lines of evidence suggest that proteolysis of other protein(s) is required, however. Here we report the anaphase-specific proteolysis of the Schizosaccharomyces pombe Cut2 protein, which is essential for sister-chromatid separation. Cut2 is located in the nucleus, where it is concentrated along the short metaphase spindle. The rapid degradation of Cut2 at anaphase requires its amino-terminal region and the activity of Cut9 (ref. 14), a component of the 20S cyclosome/anaphase-promoting complex (APC), which is necessary for cyclin destruction. Expression of non-degradable Cut2 blocks sister-chromatid separation but not cell-cycle progression. This defect can be overcome by grafting the N terminus of cyclin B onto the truncated Cut2, demonstrating that the regulated proteolysis of Cut2 is essential for sister-chromatid separation.","authors":"Funabiki H, Yamano H, Kumada K, Nagao K, Hunt T, Yanagida M","authors_abbrev":"Funabiki H et al.","pubmed_publication_date":"30 May 1996","pubmed_entrez_date":"1996-05-30","publication_year":"1996","canto_session_key":"adfedf2c04f15ddc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-08-21 21:13:29","canto_approved_date":"2023-03-23 14:22:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-09 12:14:42","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC14C8.01c","SPAC6F12.15c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-08-21"},{"uniquename":"EMBL:SPC10849","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18310029","title":"Multiple functions of ergosterol in the fission yeast Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 2008 Mar;154(Pt 3):830-841","abstract":"Sterols are a major class of membrane lipids in eukaryotes. In Schizosaccharomyces pombe, sterol 24-C-methyltransferase (Erg6p), C-8 sterol isomerase (Erg2p), C-5 sterol desaturase (Erg31p, Erg32p), C-22 sterol desaturase (Erg5p) and C-24 (28) sterol reductase (Sts1p/Erg4p) have been predicted, but not yet determined, to catalyse a sequence of reactions from zymosterol to ergosterol. Disruption mutants of these genes were unable to synthesize ergosterol, and most were tolerant to the polyene drugs amphotericin B and nystatin. Disruption of erg31(+) or erg32(+) did not cause ergosterol deficiency or tolerance to polyene drugs, indicating that the two C-5 sterol desaturases have overlapping functions. GFP-tagged DRM (detergent-resistant membrane)-associated protein Pma1p localized to the plasma membrane in ergDelta mutants. DRM fractionation revealed that the association between Pma1-GFP and DRM was weakened in erg6Delta but not in other erg mutants. Several GFP-tagged plasma membrane proteins were tested, and an amino acid permease homologue, SPBC359.03c, was found to mislocalize to intracellular punctate structures in the ergDelta mutants. These results indicate that these proteins are responsible for ergosterol biosynthesis in fission yeast, similar to the situation in Saccharomyces cerevisiae. Furthermore, in fission yeast, ergosterol is important for plasma membrane structure and function and for localization of plasma membrane proteins.","doi":"10.1099/mic.0.2007/011155-0","authors":"Iwaki T, Iefuji H, Hiraga Y, Hosomi A, Morita T, Giga-Hama Y, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-03-04","publication_year":"2008","canto_session_key":"4a5ea46ea5b10383","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-12-14 22:36:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-17 18:20:01","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":79,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27B12.03c","SPAC1687.16c","SPBC359.03c","SPCC663.03","SPCC18B5.01c","SPBC16E9.05","SPAC20G4.07c","SPAC20G8.07c","SPAC19A8.04"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2015-12-17"},{"uniquename":"PMID:12857752","title":"Schizosaccharomyces pombe Ddb1 is functionally linked to the replication checkpoint pathway.","citation":"J Biol Chem 2003 Sep 26;278(39):37006-14","abstract":"Schizosaccharomyces pombe Ddb1 is homologous to the mammalian DDB1 protein, which has been implicated in damaged-DNA recognition and global genomic repair. However, a recent study suggested that the S. pombe Ddb1 is involved in cell division and chromosomal segregation. Here, we provide evidence that the S. pombe Ddb1 is functionally linked to the replication checkpoint control gene cds1. We show that the S. pombe strain lacking ddb1 has slow growth due to delayed replication progression. Flow cytometric analysis shows an extensive heterogeneity in DNA content. Furthermore, the Deltaddb1 strain is hypersensitive to UV irradiation in S phase and is unable to tolerate a prolonged replication block imposed by hydroxyurea. Interestingly, the Deltaddb1 strain exhibits a high level of the Cds1 kinase activity during passage through S phase. Moreover, mutation of the cds1 gene relieves the defects observed in Deltaddb1 strain. The results suggest that many of the defects observed in Deltaddb1 cells are linked to an aberrant activation of Cds1, and that Ddb1 is functionally linked to Cds1.","authors":"Bondar T, Mirkin EV, Ucker DS, Walden WE, Mirkin SM, Raychaudhuri P","authors_abbrev":"Bondar T et al.","pubmed_publication_date":"26 Sep 2003","pubmed_entrez_date":"2003-07-15","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19417105","title":"Structural insights into eRF3 and stop codon recognition by eRF1.","citation":"Genes Dev 2009 May 01;23(9):1106-18","abstract":"Eukaryotic translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act cooperatively to ensure efficient stop codon recognition and fast polypeptide release. The crystal structures of human and Schizosaccharomyces pombe full-length eRF1 in complex with eRF3 lacking the GTPase domain revealed details of the interaction between these two factors and marked conformational changes in eRF1 that occur upon binding to eRF3, leading eRF1 to resemble a tRNA molecule. Small-angle X-ray scattering analysis of the eRF1/eRF3/GTP complex suggested that eRF1's M domain contacts eRF3's GTPase domain. Consistently, mutation of Arg192, which is predicted to come in close contact with the switch regions of eRF3, revealed its important role for eRF1's stimulatory effect on eRF3's GTPase activity. An ATP molecule used as a crystallization additive was bound in eRF1's putative decoding area. Mutational analysis of the ATP-binding site shed light on the mechanism of stop codon recognition by eRF1.","doi":"10.1101/gad.1770109","authors":"Cheng Z, Saito K, Pisarev AV, Wada M, Pisareva VP, Pestova TV, Gajda M, Round A, Kong C, Lim M, Nakamura Y, Svergun DI, Ito K, Song H","authors_abbrev":"Cheng Z et al.","pubmed_publication_date":"01 May 2009","pubmed_entrez_date":"2009-05-07","publication_year":"2009","canto_session_key":"c29d60efe6a85457","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-05-28 16:44:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-30 13:33:39","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC584.04","SPAC1834.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-10-30","pdb_entries":[{"pdb_id":"3e20","gene_chains":[{"gene_uniquename":"SPCC584.04","chain":"A/D/E/J","position":"467-662"},{"gene_uniquename":"SPAC1834.01","chain":"B/C/H/K","position":"1-433"}],"title":"Crystal structure of S.pombe eRF1/eRF3 complex","entry_authors":"Cheng Z,Lim M,Kong C,Song H","entry_authors_abbrev":"Cheng Z et al.","reference_uniquename":"PMID:19417105","experimental_method":"X-ray","resolution":"3.5"}]},{"uniquename":"PMID:9769097","title":"Programmed frameshifting in the synthesis of mammalian antizyme is +1 in mammals, predominantly +1 in fission yeast, but -2 in budding yeast.","citation":"RNA 1998 Oct;4(10):1230-8","abstract":"The coding sequence for mammalian ornithine decarboxylase antizyme is in two different partially overlapping reading frames with no independent ribosome entry to the second ORF. Immediately before the stop codon of the first ORF, a proportion of ribosomes undergo a quadruplet translocation event to shift to the +1 reading frame of the second and main ORF. The proportion that frameshifts is dependent on the polyamine level and, because the product antizyme is a negative regulator of intracellular polyamine levels, the frameshifting acts to complete an autoregulatory circuit by sensing polyamine levels. An mRNA element just 5' of the shift site and a 3' pseudoknot are important for efficient frameshifting. Previous work has shown that a cassette with the mammalian shift site and associated signals directs efficient shifting in the budding yeast Saccharomyces cerevisiae at the same codon to the correct frame, but that the shift is -2 instead of +1. The product contains an extra amino acid corresponding to the shift site. The present work shows efficient frameshifting also occurs in the fission yeast, Schizosaccharomyces pombe. This frameshifting is 80% +1 and 20% -2. The response of S. pombe translation apparatus to the mammalian antizyme recoding signals is more similar to that of the mammalian system than to that of S. cerevisiae. S. pombe provides a good model system for genetic studies on the mechanism of at least this type of programmed mammalian frameshifting.","authors":"Ivanov IP, Gesteland RF, Matsufuji S, Atkins JF","authors_abbrev":"Ivanov IP et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-10-13","publication_year":"1998","canto_session_key":"2b1399dc4897acdf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2025-02-27 14:54:40","canto_approved_date":"2025-02-27 14:54:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-02-27 14:54:12","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC577.14c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2025-02-27"},{"uniquename":"PMID:10473641","title":"Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast.","citation":"Mol Biol Cell 1999 Sep;10(9):2987-3001","abstract":"We describe the isolation of fission yeast homologues of tubulin-folding cofactors B (Alp11) and E (Alp21), which are essential for cell viability and the maintenance of microtubules. Alp11(B) contains the glycine-rich motif (the CLIP-170 domain) involved in microtubular functions, whereas, unlike mammalian cofactor E, Alp21(E) does not. Both mammalian and yeast cofactor E, however, do contain leucine-rich repeats. Immunoprecipitation analysis shows that Alp11(B) interacts with both alpha-tubulin and Alp21(E), but not with the cofactor D homologue Alp1, whereas Alp21(E) also interacts with Alp1(D). The cellular amount of alpha-tubulin is decreased in both alp1 and alp11 mutants. Overproduction of Alp11(B) results in cell lethality and the disappearance of microtubules, which is rescued by co-overproduction of alpha-tubulin. Both full-length Alp11(B) and the C-terminal third containing the CLIP-170 domain localize in the cytoplasm, and this domain is required for efficient binding to alpha-tubulin. Deletion of alp11 is suppressed by multicopy plasmids containing either alp21(+) or alp1(+), whereas alp21 deletion is rescued by overexpression of alp1(+) but not alp11(+). Finally, the alp1 mutant is not complemented by either alp11(+) or alp21(+). The results suggest that cofactors operate in a linear pathway (Alp11(B)-Alp21(E)-Alp1(D)), each with distinct roles.","authors":"Radcliffe PA, Hirata D, Vardy L, Toda T","authors_abbrev":"Radcliffe PA et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-09-03","publication_year":"1999","canto_session_key":"63a35e2ffef1be6f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-23 18:21:51","canto_approved_date":"2026-04-12 07:28:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-26 16:17:18","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22H10.10","SPBC11C11.04c","SPAC13D6.05","SPBC800.05c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-01-23"},{"uniquename":"PMID:18535244","title":"Fission yeast Pot1-Tpp1 protects telomeres and regulates telomere length.","citation":"Science 2008 Jun 06;320(5881):1341-4","abstract":"Telomeres are specialized chromatin structures that protect chromosomal ends. Protection of telomeres 1 (Pot1) binds to the telomeric G-rich overhang, thereby protecting telomeres and regulating telomerase. Mammalian POT1 and TPP1 interact and constitute part of the six-protein shelterin complex. Here we report that Tpz1, the TPP1 homolog in fission yeast, forms a complex with Pot1. Tpz1 binds to Ccq1 and the previously undiscovered protein Poz1 (Pot1-associated in Schizosaccharomyces pombe), which protect telomeres redundantly and regulate telomerase in positive and negative manners, respectively. Thus, the Pot1-Tpz1 complex accomplishes its functions by recruiting effector molecules Ccq1 and Poz1. Moreover, Poz1 bridges Pot1-Tpz1 and Taz1-Rap1, thereby connecting the single-stranded and double-stranded telomeric DNA regions. Such molecular architectures are similar to those of mammalian shelterin, indicating that the overall DNA-protein architecture is conserved across evolution.","doi":"10.1126/science.1154819","authors":"Miyoshi T, Kanoh J, Saito M, Ishikawa F","authors_abbrev":"Miyoshi T et al.","pubmed_publication_date":"06 Jun 2008","pubmed_entrez_date":"2008-06-07","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06","SPAC6F6.16c","SPCC188.07","HGNC:25070","SPAC19G12.13c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:11907273","title":"The 14-kDa dynein light chain-family protein Dlc1 is required for regular oscillatory nuclear movement and efficient recombination during meiotic prophase in fission yeast.","citation":"Mol Biol Cell 2002 Mar;13(3):930-46","abstract":"A Schizosaccharomyces pombe spindle pole body (SPB) protein interacts in a two-hybrid system with Dlc1, which belongs to the 14-kDa Tctex-1 dynein light chain family. Green fluorescent protein-tagged Dlc1 accumulated at the SPB throughout the life cycle. During meiotic prophase, Dlc1 was present along astral microtubules and microtubule-anchoring sites on the cell cortex, reminiscent of the cytoplasmic dynein heavy chain Dhc1. In a dlc1-null mutant, Dhc1-dependent nuclear movement in meiotic prophase became irregular in its duration and direction. Dhc1 protein was displaced from the cortex anchors and the formation of microtubule bundle(s) that guide nuclear movement was impaired in the mutant. Meiotic recombination in the dlc1 mutant was reduced to levels similar to that in the dhc1 mutant. Dlc1 and Dhc1 also have roles in karyogamy and rDNA relocation during the sexual phase. Strains mutated in both the dlc1 and dhc1 loci displayed more severe defects in recombination, karyogamy, and sporulation than in either single mutant alone, suggesting that Dlc1 is involved in nuclear events that are independent of Dhc1. S. pombe contains a homolog of the 8-kDa dynein light chain, Dlc2. This class of dynein light chain, however, is not essential in either the vegetative or sexual phases.","authors":"Miki F, Okazaki K, Shimanuki M, Yamamoto A, Hiraoka Y, Niwa O","authors_abbrev":"Miki F et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-22","publication_year":"2002","canto_session_key":"53712c93077e090e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-20 16:14:54","canto_approved_date":"2026-01-01 20:09:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-28 13:39:41","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.07c","SPAC1805.08","SPAC3A11.05c","SPAC1093.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-03-20"},{"uniquename":"PMID:33277379","title":"Sequestration of the PKC ortholog Pck2 in stress granules as a feedback mechanism of MAPK signaling in fission yeast.","citation":"J Cell Sci 2021 Jan 26;134(2)","abstract":"Protein kinase C (PKC) signaling is a highly conserved signaling module that plays a central role in a myriad of physiological processes, ranging from cell proliferation to cell death, via various signaling pathways, including MAPK signaling. Stress granules (SGs) are non-membranous cytoplasmic foci that aggregate in cells exposed to environmental stresses. Here, we explored the role of SGs in PKC/MAPK signaling activation in fission yeast. High-heat stress (HHS) induced Pmk1 MAPK activation and Pck2 translocation from the cell tips into poly(A)-binding protein (Pabp)-positive SGs. Pck2 dispersal from the cell tips required Pck2 kinase activity, and constitutively active Pck2 exhibited increased translocation to SGs. Importantly, Pmk1 deletion impaired Pck2 recruitment to SGs, indicating that MAPK activation stimulates Pck2 SG translocation. Consistently, HHS-induced SGs delayed Pck2 relocalization at the cell tips, thereby blocking subsequent Pmk1 reactivation after recovery from HHS. HHS partitioned Pck2 into the Pabp-positive SG-containing fraction, which resulted in reduced Pck2 abundance and kinase activity in the soluble fraction. Taken together, these results indicate that MAPK-dependent Pck2 SG recruitment serves as a feedback mechanism to intercept PKC/MAPK activation induced by HHS, which might underlie PKC-related diseases.","doi":"10.1242/jcs.250191","authors":"Kanda Y, Satoh R, Takasaki T, Tomimoto N, Tsuchiya K, Tsai CA, Tanaka T, Kyomoto S, Hamada K, Fujiwara T, Sugiura R","authors_abbrev":"Kanda Y et al.","pubmed_publication_date":"26 Jan 2021","pubmed_entrez_date":"2020-12-05","publication_year":"2021","canto_session_key":"be13fa270a576ad2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-12-07 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37637271","title":"Isolation of mutant alleles of the U6 snRNA m  6  A methyltransferase Mtl16 and characterization of their genetic interactions with splicing mutants in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2023;2023","abstract":" Schizosaccharomyces pombe  Dim1 is a conserved essential component of the U4/U6.U5 tri-snRNP complex essential for pre-mRNA splicing. In a synthetic lethal screen with the temperature-sensitive  dim1-35  mutant, we isolated multiple alleles of non-essential  mtl16  that encodes the U6 snRNA m  6  A methyltransferase. Further genetic analysis revealed strong and specific negative genetic interactions between  mtl16  and a mutation in the Dim1 binding partner, Prp31, and between  dim1-35  and a mutation in the Prp31 binding partner, Prp6. Our work provides additional tools to study pre-mRNA splicing in  S. pombe  and biological confirmation of the importance of the Prp6-Prp31-Dim1-U6 snRNA interactions for pre-mRNA splicing.","doi":"10.17912/micropub.biology.000948","authors":"Willet AH, Ren L, Turner LA, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-08-28","publication_year":"2023","canto_session_key":"af542192349c135a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2023-09-01 15:11:44","canto_approved_date":"2024-04-04 08:20:24","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-09-01 13:06:47","canto_added_date":"2023-08-29 00:15:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":11,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.07","SPBC119.13c","SPAPJ698.03c","SPAC27D7.08c","SPCC16A11.05c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2023-09-01"},{"uniquename":"PMID:38881181","title":"Siderophore Biosynthesis and Transport Systems in Model and Pathogenic Fungi.","citation":"J Microbiol Biotechnol 2024 Jun 13;34(8):1-12","abstract":"Fungi employ diverse mechanisms for iron uptake to ensure proliferation and survival in ironlimited environments. Siderophores are secondary metabolite small molecules with a high affinity specifically for ferric iron; these molecules play an essential role in iron acquisition in fungi and significantly influence fungal physiology and virulence. Fungal siderophores, which are primarily hydroxamate types, are synthesized via non-ribosomal peptide synthetases (NRPS) or NRPSindependent pathways. Following synthesis, siderophores are excreted, chelate iron, and are transported into the cell by specific cell membrane transporters. In several human pathogenic fungi, siderophores are pivotal for virulence, as inhibition of their synthesis or transport significantly reduces disease in murine models of infection. This review briefly highlights siderophore biosynthesis and transport mechanisms in fungal pathogens as well the model fungi  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe.  Understanding siderophore biosynthesis and transport in pathogenic fungi provides valuable insights into fungal biology and illuminates potential therapeutic targets for combating fungal infections.","doi":"10.4014/jmb.2405.05020","authors":"Choi S, Kronstad JW, Jung WH","authors_abbrev":"Choi S et al.","pubmed_publication_date":"13 Jun 2024","pubmed_entrez_date":"2024-06-17","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-06-17 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19121815","title":"Roles of F-BAR/PCH proteins in the regulation of membrane dynamics and actin reorganization.","citation":"Int Rev Cell Mol Biol 2009;272:1-31","abstract":"The Pombe Cdc15 Homology (PCH) proteins have emerged in many species as important coordinators of signaling pathways that regulate actomyosin assembly and membrane dynamics. The hallmark of the PCH proteins is the presence of a Fes/CIP4 homology-Bin/Amphiphysin/Rvsp (F-BAR) domain; therefore they are commonly referred to as F-BAR proteins. The prototype F-BAR protein, Cdc15p of Schizosaccharomyces pombe, has a role in the formation of the contractile actomyosin ring during cytokinesis. Vertebrate F-BAR proteins have an established role in binding phospholipids and they participate in membrane deformations, for instance, during the internalization of transmembrane receptors. This way the F-BAR proteins will function as linkers between the actin polymerization apparatus and the machinery regulating membrane dynamics. Interestingly, some members of the F-BAR proteins are implicated in inflammatory or neurodegenerative disorders and the observations can be expected to have clinical implications for the treatment of the diseases.","doi":"10.1016/S1937-6448(08)01601-8","authors":"Aspenström P","authors_abbrev":"Aspenström P","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-01-06","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10574693","title":"Expression system for foreign genes using the fission yeast Schizosaccharomyces pombe.","citation":"Biotechnol Appl Biochem 1999 Dec;30(3):235-44","abstract":"Foreign-gene expression systems using mammalian cells, Escherichia coli, insect cells, yeast and other organisms as hosts have been developed. The demand for protein-production systems will be further increased in basic research, medical science and the biotechnological industry. Systems using the fission yeast Schizosaccharomyces pombe as a host have only recently received attention. The advantages of this yeast, which is more advanced evolutionarily than other types of yeast, the expression vectors available and examples of heterologous protein produced with this system, are reviewed here.","authors":"Giga-Hama Y, Kumagai H","authors_abbrev":"Giga-Hama Y et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-11-27","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10996305","title":"The S. pombe sep1 gene encodes a nuclear protein that is required for periodic expression of the cdc15 gene.","citation":"FEBS Lett 2000 Sep 15;481(2):105-8","abstract":"The Schizosaccharomyces pombe sep1 gene encodes a putative transcription factor that is required for cell separation. Among the genes required for septum formation and cytokinesis in fission yeast examined to date, the only one whose mRNA fluctuates significantly during the cell cycle is cdc15. In this study we have examined cdc15 mRNA levels in sep1 mutant and null backgrounds and have found that sep1p function is required for periodic accumulation of cdc15 mRNA. We have also localised sep1p and find that it is a nuclear protein, consistent with its proposed role as a transcription factor.","authors":"Zilahi E, Salimova E, Simanis V, Sipiczki M","authors_abbrev":"Zilahi E et al.","pubmed_publication_date":"15 Sep 2000","pubmed_entrez_date":"2000-09-21","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4C3.12"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:29654060","title":"RNAi drives nonreciprocal translocations at eroding chromosome ends to establish telomere-free linear chromosomes.","citation":"Genes Dev 2018 Apr 01;32(7-8):537-554","abstract":"The identification of telomerase-negative HAATI (heterochromatin amplification-mediated and telomerase-independent) cells, in which telomeres are superseded by nontelomeric heterochromatin tracts, challenged the idea that canonical telomeres are essential for chromosome linearity and raised crucial questions as to how such tracts translocate to eroding chromosome ends and confer end protection. Here we show that HAATI arises when telomere loss triggers a newly recognized illegitimate translocation pathway that requires RNAi factors. While RNAi is necessary for the translocation events that mobilize ribosomal DNA (rDNA) tracts to all chromosome ends (forming \"HAATI rDNA \" chromosomes), it is dispensable for HAATI rDNA  maintenance. Surprisingly, Dicer (Dcr1) plays a separate, RNAi-independent role in preventing formation of the rare HAATI subtype in which a different repetitive element (the subtelomeric element) replaces telomeres. Using genetics and fusions between shelterin components and rDNA-binding proteins, we mapped the mechanism by which rDNA loci engage crucial end protection factors-despite the absence of telomere repeats-and secure end protection. Sequence analysis of HAATI rDNA  genomes allowed us to propose RNA and DNA polymerase template-switching models for the mechanism of RNAi-triggered rDNA translocations. Collectively, our results reveal unforeseen roles for noncoding RNAs (ncRNAs) in assembling a telomere-free chromosome end protection device.","doi":"10.1101/gad.311712.118","authors":"Begnis M, Apte MS, Masuda H, Jain D, Wheeler DL, Cooper JP","authors_abbrev":"Begnis M et al.","pubmed_publication_date":"01 Apr 2018","pubmed_entrez_date":"2018-04-15","publication_year":"2018","canto_session_key":"16f247326c8b8f20","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-06-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPCC188.13c","SPCC736.11"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23060961","title":"Cdc42 regulation of polarized traffic in fission yeast.","citation":"Commun Integr Biol 2012 Jul 01;5(4):370-3","abstract":"Cdc42 is a key factor in the control of cell polarity and morphogenesis. Fission yeast Cdc42 regulates formin activation and actin cable assembly. Cdc42 is also required for exocyst function, contributing to polarized secretion. Additionally, Cdc42 participates in membrane trafficking, endosome recycling, and vacuole formation. We show here how Cdc42 is required for the correct transport/recycling to the plasma membrane of the glucan synthases Bgs1 and Bgs4, responsible of cell wall biosynthesis and polarized growth at the cell tips.","doi":"10.4161/cib.19977","authors":"Estravis M, Rincon S, Pérez P","authors_abbrev":"Estravis M et al.","pubmed_publication_date":"01 Jul 2012","pubmed_entrez_date":"2012-10-13","publication_year":"2012","canto_session_key":"a6812171921eb25c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pilar Perez","canto_first_approved_date":"2017-06-30 14:36:57","canto_approved_date":"2026-04-25 12:35:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-05 12:09:35","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pilar Perez","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPAC110.03"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2017-06-30"},{"uniquename":"EMBL:AB084816","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19431597","title":"Orientation of Schizosaccharomyces POMBE Nonliving Cells under Alternating Uniform and Nonuniform Electric Fields.","citation":"Biophys J 1985 Nov;48(5):721-6","abstract":"When nonliving cells of Schizosaccharomyces pombe were subjected to the action of alternating uniform and nonuniform electric fields, two types of orientation were produced. The first one, with its longest axis parallel to the field lines, is similar to that obtained with living cells. The second, perpendicular to the direction of the field, is produced for relatively high frequencies and low conductivities; this probably takes place when the conductivities of the external and internal media (cell cytoplasm) become equal. A mixed cell population is produced in a discrete interval of the parameters used. Our results provide direct evidence that cell alignment does not depend on the physiological state of the cells.","authors":"Iglesias FJ, López MC, Santamaría C, Domínguez A","authors_abbrev":"Iglesias FJ et al.","pubmed_publication_date":"Nov 1985","pubmed_entrez_date":"2009-05-12","publication_year":"1985","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30456391","title":"Phosphorylation of Arp2 is not essential for Arp2/3 complex activity in fission yeast.","citation":"Life Sci Alliance 2018 Oct;1(5):e201800202","abstract":"LeClaire et al presented evidence that phosphorylation of three sites on the Arp2 subunit activates the Arp2/3 complex to nucleate actin filaments. We mutated the homologous residues of Arp2 (Y198, T233, and T234) in the fission yeast genome to amino acids that preclude or mimic phosphorylation. Arp2/3 complex is essential for the viability of fission yeast, yet strains unable to phosphorylate these sites grew normally. Y198F/T233A/T234A Arp2 was only nonfunctional if GFP-tagged, as observed by LeClaire et al in  Drosophila  cells. Replacing both T233 and T234 with aspartic acid was lethal, suggesting that phosphorylation might be inhibitory. Nevertheless, blocking phosphorylation at these sites had the same effect as mimicking it: slowing assembly of endocytic actin patches. Mass spectrometry revealed phosphorylation at a fourth conserved Arp2 residue, Y218, but both blocking and mimicking phosphorylation of Y218 only slowed actin patch assembly slightly. Therefore, phosphorylation of Y198, T233, T234, and Y218 is not required for the activity of fission yeast Arp2/3 complex.","doi":"10.26508/lsa.201800202","authors":"Epstein AE, Espinoza-Sanchez S, Pollard TD","authors_abbrev":"Epstein AE et al.","pubmed_publication_date":"Oct 2018","pubmed_entrez_date":"2018-11-21","publication_year":"2018","canto_session_key":"8fd14f7705dad425","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-11-22 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23543032","title":"Replication of telomeres and the regulation of telomerase.","citation":"Cold Spring Harb Perspect Biol 2013 May 01;5(5):a010405","abstract":"Telomeres are the physical ends of eukaryotic chromosomes. They protect chromosome ends from DNA degradation, recombination, and DNA end fusions, and they are important for nuclear architecture. Telomeres provide a mechanism for their replication by semiconservative DNA replication and length maintenance by telomerase. Through telomerase repression and induced telomere shortening, telomeres provide the means to regulate cellular life span. In this review, we introduce the current knowledge on telomere composition and structure. We then discuss in depth the current understanding of how telomere components mediate their function during semiconservative DNA replication and how telomerase is regulated at the end of the chromosome. We focus our discussion on the telomeres from mammals and the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.","doi":"10.1101/cshperspect.a010405","authors":"Pfeiffer V, Lingner J","authors_abbrev":"Pfeiffer V et al.","pubmed_publication_date":"01 May 2013","pubmed_entrez_date":"2013-04-02","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20716958","title":"Regulation of yeast forkhead transcription factors and FoxM1 by cyclin-dependent and polo-like kinases.","citation":"Cell Cycle 2010 Aug 15;9(16):3233-42","abstract":"Members of the forkhead-box (Fox) family of transcription factors are present in many eukaryotes. More than 100 such proteins that share homology in the winged-helix DNA-binding domain have been identified in higher eukaryotes. This family of transcription factors is implicated in the regulation of a variety of cellular processes, including the cell cycle, apoptosis, DNA repair, stress resistance and metabolism. A subfamily of Fox proteins are required to activate expression of the genes encoding B-type cyclins, Cdc25 and Polo-like kinase (Plk) during the mitotic cell cycle and meiosis in organisms from yeast to mammals. These proteins are activators of cyclin-dependent kinase 1 (Cdk1). Cdk1 and Plk phosphorylate Fox and its associated proteins at different sites, resulting in activation or repression of Fox transcriptional activity, depending on the target genes. In addition to their documented transcriptional functions, Fox proteins are involved in the regulation of pre-mRNA processing, at least in yeast. In this review, we will focus on the role of Fox proteins in the fission yeast Schizosaccharomyces pombe and budding yeast Saccharomyces cerevisiae, in addition to the role of FoxM1 in mammals in the cell cycle and in pre-mRNA processing, as revealed in recent studies.","doi":"10.4161/cc.9.16.12599","authors":"Murakami H, Aiba H, Nakanishi M, Murakami-Tonami Y","authors_abbrev":"Murakami H et al.","pubmed_publication_date":"15 Aug 2010","pubmed_entrez_date":"2010-08-19","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7657644","title":"Ca2+ binding to calmodulin and its role in Schizosaccharomyces pombe as revealed by mutagenesis and NMR spectroscopy.","citation":"J Biol Chem 1995 Sep 01;270(35):20643-52","abstract":"As a first step toward identifying the important structural elements of calmodulin from Schizosaccharomyces pombe, we examined the ability of heterologous calmodulins and Ca(2+)-binding site mutant S. pombe calmodulins to replace the essential cam1+ gene. A cDNA encoding vertebrate calmodulin allows growth of S. pombe. However, calmodulin from Saccharomyces cerevisiae does not support growth even though the protein is produced at high levels. With one exception, all mutant S. pombe calmodulins with one or more intact Ca(2+)-binding sites allow growth at 21 degrees C. A mutant containing only an intact Ca(2+)-binding site 3 fails to support growth, as does S. pombe calmodulin with all four Ca(2+)-binding sites mutated. Several of the mutant proteins confer a temperature-sensitive phenotype. Analysis of the degree of temperature sensitivity allows the Ca(2+)-binding sites to be ranked by their ability to support fission yeast proliferation. Site 2 is more important than site 1, which is more important than site 4, which is more important than site 3. A visual colony color screen based on the fission yeast ade1+ gene was developed to perform these genetic analyses. To compare the Ca(2+)-binding properties of individual sites to their functional importance for viability, Ca2+ binding to calmodulin from S. pombe was studied by 1H NMR spectroscopy. NMR analysis indicates a Ca(2+)-binding profile that differs from those previously determined for vertebrate and S. cerevisiae calmodulins. Ca(2+)-binding site 3 has the highest relative affinity for Ca2+, while the affinities of sites 1, 2, and 4 are indistinguishable. A combination of an in vivo functional assay and an in vitro physical assay reveals that the relative affinity of a site for Ca2+ does not predict its functional importance.","authors":"Moser MJ, Lee SY, Klevit RE, Davis TN","authors_abbrev":"Moser MJ et al.","pubmed_publication_date":"01 Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_session_key":"8e9ae50d97ec7769","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-06-08 07:39:38","canto_approved_date":"2026-01-29 13:38:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-04 09:40:18","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":64,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-06-08"},{"uniquename":"PMID:2249257","title":"The structural gene coding for thiamin-repressible acid phosphatase in Schizosaccharomyces pombe.","citation":"Curr Genet 1990 Oct;18(3):269-72","abstract":"The pho4 gene of the fission yeast Schizosaccharomyces pombe is regulated by thiamin. The nucleotide sequence of this gene is given here and it is shown that it matches the amino acid sequence of thiamin-repressible acid phosphatase, corroborating genetic evidence that pho4 represents the structural gene of this enzyme. The gene codes for a protein of 463 amino acids in length and shows regions of strong similarity with the phosphate-repressible acid phosphatase of Schizosaccharomyces pombe. The enzyme has a cleavable signal sequence 18 amino acids long and carries nine potential N-glycosylation sites.","authors":"Yang JW, Schweingruber ME","authors_abbrev":"Yang JW et al.","pubmed_publication_date":"Oct 1990","pubmed_entrez_date":"1990-10-01","publication_year":"1990","canto_session_key":"40213c281e540075","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-07-10 17:36:56","canto_approved_date":"2022-10-26 19:23:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-10 13:40:31","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-07-10"},{"uniquename":"EMBL:AU012097","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24268782","title":"A peroxiredoxin promotes H2O2 signaling and oxidative stress resistance by oxidizing a thioredoxin family protein.","citation":"Cell Rep 2013 Dec 12;5(5):1425-35","abstract":"H2O2 can cause oxidative damage associated with age-related diseases such as diabetes and cancer but is also used to initiate diverse responses, including increased antioxidant gene expression. Despite significant interest, H2O2-signaling mechanisms remain poorly understood. Here, we present a mechanism for the propagation of an H2O2 signal that is vital for the adaptation of the model yeast, Schizosaccharomyces pombe, to oxidative stress. Peroxiredoxins are abundant peroxidases with conserved antiaging and anticancer activities. Remarkably, we find that the only essential function for the thioredoxin peroxidase activity of the Prx Tpx1(hPrx1/2) in resistance to H2O2 is to inhibit a conserved thioredoxin family protein Txl1(hTxnl1/TRP32). Thioredoxins regulate many enzymes and signaling proteins. Thus, our discovery that a Prx amplifies an H2O2 signal by driving the oxidation of a thioredoxin-like protein has important implications, both for Prx function in oxidative stress resistance and for responses to H2O2.","doi":"10.1016/j.celrep.2013.10.036","authors":"Brown JD, Day AM, Taylor SR, Tomalin LE, Morgan BA, Veal EA","authors_abbrev":"Brown JD et al.","pubmed_publication_date":"12 Dec 2013","pubmed_entrez_date":"2013-11-26","publication_year":"2013","canto_session_key":"45f5ecd620515505","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elizabeth Veal","canto_first_approved_date":"2018-08-09 07:01:29","canto_approved_date":"2022-06-13 15:41:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-06 10:41:48","canto_added_date":"2013-12-05 13:58:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Elizabeth Veal","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC7D4.07c","SPBC577.08c","SPCC965.07c","SPAC3C7.14c","SPBC106.02c","SPAC1783.07c","SPCC576.03c","SPBC3F6.03"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2018-08-09"},{"uniquename":"PMID:8846774","title":"Fission yeast rad17: a homologue of budding yeast RAD24 that shares regions of sequence similarity with DNA polymerase accessory proteins.","citation":"EMBO J 1995 Dec 01;14(23):5812-23","abstract":"Following DNA damage or a block to DNA synthesis, checkpoint pathways act to arrest mitosis and prevent the attempted segregation of damaged or unreplicated DNA. The rad17 locus of Schizosaccharomyces pombe is one of seven known radiation-sensitive (rad) loci which are absolutely required to prevent mitosis following DNA damage in fission yeast. Six of these (rad1, rad3, rad9, rad17, rad26 and hus1) are also required for the checkpoint which prevents mitosis from occurring before DNA replication is complete. We report here that the predicted rad17 gene product is a basic hydrophilic protein of 606 amino acids which contains five domains with sequence homology to replication factor C (RF-C)/activator 1 subunits. Western analysis and fusion with Green Fluorescent Protein indicate that the abundance and electrophoretic mobility of Rad17 is not significantly modified following a block to DNA synthesis or following DNA damage, and that Rad17 is localized in the nucleus. Rad17 function is not essential for growth, but is required for the function of the DNA structure-dependent checkpoints. Site-directed mutagenesis has been used to demonstrate the biological significance of the RF-C/activator 1-related domains. These studies have also defined an element of the radiation sensitivity caused by loss of Rad17 function which is not associated with the radiation-induced G2 arrest defect seen in the rad17.d null mutant cells.","authors":"Griffiths DJ, Barbet NC, McCready S, Lehmann AR, Carr AM","authors_abbrev":"Griffiths DJ et al.","pubmed_publication_date":"01 Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"088b3d745f525fe8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-04 21:16:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-06 15:45:01","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.13","SPAC14C4.13","SPAC9E9.08","SPBC3E7.08c","SPAC664.07c","SPCC1259.13","SPAC1952.07","SPAC23C4.18c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2014-03-06"},{"uniquename":"PMID:19056889","title":"Stepping into the ring: the SIN takes on contractile ring assembly.","citation":"Genes Dev 2008 Nov 15;22(22):3082-8","abstract":"The septation initiation network (SIN) regulates the timing of septum formation in Schizosaccharomyces pombe. However, whether and how the SIN functions in contractile ring formation has remained unclear. In this issue of Genes & Development, Hachet and Simanis (3205-3216) demonstrate that the SIN acts downstream from the Plo1 kinase to control a final step in contractile ring assembly. Furthermore, their careful analysis of contractile ring formation may help bridge two existing models of cytokinetic ring formation.","doi":"10.1101/gad.1748908","authors":"Roberts-Galbraith RH, Gould KL","authors_abbrev":"Roberts-Galbraith RH et al.","pubmed_publication_date":"15 Nov 2008","pubmed_entrez_date":"2008-12-06","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22370951","title":"Engineered high content of ricinoleic acid in fission yeast Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2012 Jul;95(1):179-87","abstract":"In an effort to produce ricinoleic acid (12-hydroxy-octadeca-cis-9-enoic acid: C18:1-OH) as a petrochemical replacement in a variety of industrial processes, we introduced Claviceps purpurea oleate ∆12-hydroxylase gene (CpFAH12) to Schizosaccharomyces pombe, putting it under the control of inducible nmt1 promoter. Since Fah12p is able to convert oleic acid to ricinoleic acid, we thought that S. pombe, in which around 75% of total fatty acid (FA) is oleic acid, would accordingly be an ideal microorganism for high production of ricinoleic acid. Unfortunately, at the normal growth temperature of 30 °C, S. pombe cells harboring CpFAH12 grew poorly when the CpFAH12 gene expression was induced, perhaps implicating ricinoleic acid as toxic in S. pombe. However, in line with a likely thermoinstability of Fah12p, there was almost no growth inhibition at 37 °C or, by contrast with 30 °C and lower temperatures, ricinoleic acid accumulation. Accordingly, various optimization steps led to a regime with preliminary growth at 37 °C followed by a 5-day incubation at 20 °C, and the level of ricinoleic acid reached 137.4 μg/ml of culture that corresponded to 52.6% of total FA.","doi":"10.1007/s00253-012-3959-6","authors":"Holic R, Yazawa H, Kumagai H, Uemura H","authors_abbrev":"Holic R et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-02-29","publication_year":"2012","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19737749","title":"Ectopic overproduction of a sporulation-specific transcription factor induces assembly of prespore-like membranous compartments in vegetative cells of fission yeast.","citation":"Genetics 2009 Nov;183(3):1195-9","abstract":"Mei4 is a key sporulation-specific transcription factor in fission yeast. Ectopic expression of Mei4 in vegetative cells caused formation of nucleated membranous compartments, which shared common features with normal forespore membranes, thereby perturbing nuclear division. These results suggest why expression of development-specific transcription factors must be strictly controlled.","doi":"10.1534/genetics.109.106906","authors":"Nakase Y, Hirata A, Shimoda C, Nakamura T","authors_abbrev":"Nakase Y et al.","pubmed_publication_date":"Nov 2009","pubmed_entrez_date":"2009-09-10","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21195161","title":"Cross-species Functionome analysis identifies proteins associated with DNA repair, translation and aerobic respiration as conserved modulators of UV-toxicity.","citation":"Genomics 2011 Mar;97(3):133-47","abstract":"Cellular responses to DNA damage can prevent mutations and death. In this study, we have used high throughput screens and developed a comparative genomic approach, termed Functionome mapping, to discover conserved responses to UVC-damage. Functionome mapping uses gene ontology (GO) information to link proteins with similar biological functions from different organisms, and we have used it to compare 303, 311 and 288 UVC-toxicity modulating proteins from Escherichia coli, Schizosaccharomyces pombe and Saccharomyces cerevisiae, respectively. We have demonstrated that all three organisms use DNA repair, translation and aerobic respiration associated processes to modulate the toxicity of UVC, with these last two categories highlighting the importance of ribosomal proteins and electron transport machinery. Our study has demonstrated that comparative genomic approaches can be used to identify conserved responses to damage, and suggest roles for translational machinery and components of energy metabolism in optimizing the DNA damage response.","doi":"10.1016/j.ygeno.2010.12.005","authors":"Rooney JP, Patil A, Joseph F, Endres L, Begley U, Zappala MR, Cunningham RP, Begley TJ","authors_abbrev":"Rooney JP et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-01-04","publication_year":"2011","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33827924","title":"Establishment of heterochromatin in domain-size-dependent bursts.","citation":"Proc Natl Acad Sci U S A 2021 Apr 13;118(15)","abstract":"Methylation of histone H3K9 is a hallmark of epigenetic silencing in eukaryotes. Nucleosome modifications often rely on positive feedback where enzymes are recruited by modified nucleosomes. A combination of local and global feedbacks has been proposed to account for some dynamic properties of heterochromatin, but the range at which the global feedbacks operate and the exact mode of heterochromatin propagation are not known. We investigated these questions in fission yeast. Guided by mathematical modeling, we incrementally increased the size of the mating-type region and profiled heterochromatin establishment over time. We observed exponential decays in the proportion of cells with active reporters, with rates that decreased with domain size. Establishment periods varied from a few generations in wild type to >200 generations in the longest region examined, and highly correlated silencing of two reporters located outside the nucleation center was observed. On a chromatin level, this indicates that individual regions are silenced in sudden bursts. Mathematical modeling accounts for these bursts if heterochromatic nucleosomes facilitate a deacetylation or methylation reaction at long range, in a distance-independent manner. A likely effector of three-dimensional interactions is the evolutionarily conserved Swi6 HP1  H3K9me reader, indicating the bursting behavior might be a general mode of heterochromatin propagation.","doi":"10.1073/pnas.2022887118","authors":"Nickels JF, Edwards AK, Charlton SJ, Mortensen AM, Hougaard SCL, Trusina A, Sneppen K, Thon G","authors_abbrev":"Nickels JF et al.","pubmed_publication_date":"13 Apr 2021","pubmed_entrez_date":"2021-04-08","publication_year":"2021","canto_session_key":"6ec4e75812d31fa0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-04-10 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25831549","title":"Epigenetics. Epigenetic inheritance uncoupled from sequence-specific recruitment.","citation":"Science 2015 Apr 03;348(6230):1258699","abstract":"Changes in histone posttranslational modifications are associated with epigenetic states that define distinct patterns of gene expression. It remains unclear whether epigenetic information can be transmitted through histone modifications independently of specific DNA sequence, DNA methylation, or RNA interference. Here we show that, in the fission yeast Schizosaccharomyces pombe, ectopically induced domains of histone H3 lysine 9 methylation (H3K9me), a conserved marker of heterochromatin, are inherited through several mitotic and meiotic cell divisions after removal of the sequence-specific initiator. The putative JmjC domain H3K9 demethylase, Epe1, and the chromodomain of the H3K9 methyltransferase, Clr4/Suv39h, play opposing roles in maintaining silent H3K9me domains. These results demonstrate how a direct \"read-write\" mechanism involving Clr4 propagates histone modifications and allows histones to act as carriers of epigenetic information.","doi":"10.1126/science.1258699","authors":"Ragunathan K, Jih G, Moazed D","authors_abbrev":"Ragunathan K et al.","pubmed_publication_date":"03 Apr 2015","pubmed_entrez_date":"2015-04-02","publication_year":"2015","canto_session_key":"e9c626e3d4661f4d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-06-28 12:32:59","canto_approved_date":"2025-09-01 09:29:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-26 15:41:26","canto_added_date":"2015-04-03 00:18:09","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":14,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPCC188.13c","SPCC622.16c","SPBC428.08c","SPCC736.11","SPBC16C6.10","SPBC16D10.07c","SPAC664.01c"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2024-06-28"},{"uniquename":"PMID:25352017","title":"Implementation of the CRISPR-Cas9 system in fission yeast.","citation":"Nat Commun 2014 Oct 29;5:5344","abstract":"Application of the CRISPR-Cas9 genome editing system in the model organism Schizosaccharomyces pombe has been hampered by the lack of constructs to express RNA of arbitrary sequence. Here we present expression constructs that use the promoter/leader RNA of K RNA (rrk1) and a ribozyme to produce the targeting guide RNA. Together with constitutive expression of Cas9, this system achieves selection-free specific mutagenesis with efficiencies approaching 100%. The rrk1 CRISPR-Cas9 method enables rapid and efficient genome manipulation and unlocks the CRISPR toolset for use in fission yeast.","doi":"10.1038/ncomms6344","authors":"Jacobs JZ, Ciccaglione KM, Tournier V, Zaratiegui M","authors_abbrev":"Jacobs JZ et al.","pubmed_publication_date":"29 Oct 2014","pubmed_entrez_date":"2014-10-30","publication_year":"2014","canto_session_key":"267b85c1b667dcb2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-22 17:28:15","canto_approved_date":"2019-06-11 11:52:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-22 17:27:17","canto_added_date":"2014-10-31 01:15:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-03-22"},{"uniquename":"PMID:38527022","title":"Recombinant cyclin B-Cdk1-Suc1 capable of multi-site mitotic phosphorylation in vitro.","citation":"PLoS One 2024;19(3):e0299003","abstract":"Cyclin-dependent kinase 1 (Cdk1) complexed with cyclin B phosphorylates multiple sites on hundreds of proteins during mitosis. However, it is not fully understood how multi-site mitotic phosphorylation by cyclin B-Cdk1 controls the structures and functions of individual substrates. Here we develop an easy-to-use protocol to express recombinant vertebrate cyclin B and Cdk1 in insect cells from a single baculovirus vector and to purify their complexes with excellent homogeneity. A series of in-vitro assays demonstrate that the recombinant cyclin B-Cdk1 can efficiently and specifically phosphorylate the SP and TP motifs in substrates. The addition of Suc1 (a Cks1 homolog in fission yeast) accelerates multi-site phosphorylation of an artificial substrate containing TP motifs. Importantly, we show that mitosis-specific multi-subunit and multi-site phosphorylation of the condensin I complex can be recapitulated in vitro using recombinant cyclin B-Cdk1-Suc1. The materials and protocols described here will pave the way for dissecting the biochemical basis of critical mitotic processes that accompany Cdk1-mediated large-scale phosphorylation.","doi":"10.1371/journal.pone.0299003","authors":"Shintomi K, Masahara-Negishi Y, Shima M, Tane S, Hirano T","authors_abbrev":"Shintomi K et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-03-25","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-03-26 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000079","title":"Representation of assembly or disassembly of a cell component as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the assembly or disassembly of a cellular component as a biological process. The underlying equivalence axiom templates are \"GO:0022607 and 'results_in_assembly_of' some C\" (assembly) and \"GO:0022411 and 'results_in_disassembly_of' some C\" (disassembly), where C is a cellular component.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39916665","title":"In quiescent G0 phase, Schizosaccharomyces pombe Mis4 ensures full nuclear separation during the subsequent M phase.","citation":"J Cell Sci 2025 Feb 07;","abstract":"Evolutionarily conserved Mis4 establishes cohesion between replicated sister chromatids in vegetatively proliferating cells. In the fission yeast, Schizosaccharomyces pombe, defects in Mis4 lead to premature separation of sister chromatids, resulting in fatal chromosome mis-segregation during mitosis. In humans, NIPBL, an ortholog of Mis4, is responsible for a multisystem disorder called Cornelia de Lange syndrome. We reported that Mis4 is also essential in non-proliferating quiescent cells. Whereas wild-type fission yeast cells can maintain high viability for long periods without cell division in the quiescent G0 phase, mis4-450 mutant cells cannot. Here, we show that Mis4 is not required for cells to enter G0 phase, but is essential for them to exit from it. When resuming mitosis after passage of G0, mis4 mutant cells segregated sister chromatid successfully, but failed to separate daughter nuclei completely and consequently formed dikaryon-like cells. These findings suggest a novel role for Mis4/NIPBL in quiescent cells, which is prerequisite for full nuclear separation upon resumed mitosis. As most human cells are in a quiescent state, this study may facilitate development of novel therapies for human diseases caused by Mis4/NIPBL deficiency.","doi":"10.1242/jcs.263747","authors":"Suma M, Arakawa O, Tahara Y, Sajiki K, Saitoh S, Yanagida M","authors_abbrev":"Suma M et al.","pubmed_publication_date":"07 Feb 2025","pubmed_entrez_date":"2025-02-07","publication_year":"2025","canto_session_key":"fa1ed8446f4571f5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Michiko Suma","canto_first_approved_date":"2025-03-14 16:52:19","canto_approved_date":"2026-01-29 14:37:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-06 06:59:26","canto_added_date":"2025-02-08 00:25:04","annotation_curators":[{"name":"Michiko Suma","community_curator":true,"annotation_count":10,"orcid":"0009-0009-7414-5775","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":10,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-03-14"},{"uniquename":"PMID:28771613","title":"Activation of Gcn2 in response to different stresses.","citation":"PLoS One 2017;12(8):e0182143","abstract":"All organisms have evolved pathways to respond to different forms of cellular stress. The Gcn2 kinase is best known as a regulator of translation initiation in response to starvation for amino acids. Work in budding yeast has showed that the molecular mechanism of GCN2 activation involves the binding of uncharged tRNAs, which results in a conformational change and GCN2 activation. This pathway requires GCN1, which ensures delivery of the uncharged tRNA onto GCN2. However, Gcn2 is activated by a number of other stresses which do not obviously involve accumulation of uncharged tRNAs, raising the question how Gcn2 is activated under these conditions. Here we investigate the requirement for ongoing translation and tRNA binding for Gcn2 activation after different stresses in fission yeast. We find that mutating the tRNA-binding site on Gcn2 or deleting Gcn1 abolishes Gcn2 activation under all the investigated conditions. These results suggest that tRNA binding to Gcn2 is required for Gcn2 activation not only in response to starvation but also after UV irradiation and oxidative stress.","doi":"10.1371/journal.pone.0182143","authors":"Anda S, Zach R, Grallert B","authors_abbrev":"Anda S et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-08-04","publication_year":"2017","canto_session_key":"554b67537d04311a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Beata Grallert","canto_first_approved_date":"2018-02-19 12:16:36","canto_approved_date":"2023-03-14 18:04:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-09 17:27:01","canto_added_date":"2017-08-06 00:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Beata Grallert","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.05c","SPAC3G9.09c","SPBC36B7.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-02-19"},{"uniquename":"PMID:33511417","title":"Repression of a large number of genes requires interplay between homologous recombination and HIRA.","citation":"Nucleic Acids Res 2021 Feb 26;49(4):1914-1934","abstract":"During homologous recombination, Dbl2 protein is required for localisation of Fbh1, an F-box helicase that efficiently dismantles Rad51-DNA filaments. RNA-seq analysis of dbl2Δ transcriptome showed that the dbl2 deletion results in upregulation of more than 500 loci in Schizosaccharomyces pombe. Compared with the loci with no change in expression, the misregulated loci in dbl2Δ are closer to long terminal and long tandem repeats. Furthermore, the misregulated loci overlap with antisense transcripts, retrotransposons, meiotic genes and genes located in subtelomeric regions. A comparison of the expression profiles revealed that Dbl2 represses the same type of genes as the HIRA histone chaperone complex. Although dbl2 deletion does not alleviate centromeric or telomeric silencing, it suppresses the silencing defect at the outer centromere caused by deletion of hip1 and slm9 genes encoding subunits of the HIRA complex. Moreover, our analyses revealed that cells lacking dbl2 show a slight increase of nucleosomes at transcription start sites and increased levels of methylated histone H3 (H3K9me2) at centromeres, subtelomeres, rDNA regions and long terminal repeats. Finally, we show that other proteins involved in homologous recombination, such as Fbh1, Rad51, Mus81 and Rad54, participate in the same gene repression pathway.","doi":"10.1093/nar/gkab027","authors":"Misova I, Pitelova A, Budis J, Gazdarica J, Sedlackova T, Jordakova A, Benko Z, Smondrkova M, Mayerova N, Pichlerova K, Strieskova L, Prevorovsky M, Gregan J, Cipak L, Szemes T, Polakova SB","authors_abbrev":"Misova I et al.","pubmed_publication_date":"26 Feb 2021","pubmed_entrez_date":"2021-01-29","publication_year":"2021","canto_session_key":"719521c232a83155","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silvia Polakova","canto_first_approved_date":"2021-02-24 16:03:21","canto_approved_date":"2026-01-26 16:21:24","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-02-12 16:51:55","canto_added_date":"2021-01-31 01:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Silvia Polakova","community_curator":true,"annotation_count":20,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31F10.13c","SPBC947.08c","SPBC31F10.14c","SPAC23H4.12","SPAC644.14c","SPCC4G3.05c","SPBC428.08c","SPBC36.05c","SPBC15D4.03","SPCC553.01c","SPCC188.13c","SPAC23C11.15"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2021-02-24"},{"uniquename":"PMID:26436827","title":"Rif1 binds to G quadruplexes and suppresses replication over long distances.","citation":"Nat Struct Mol Biol 2015 Nov;22(11):889-97","abstract":"Rif1 regulates replication timing and repair of double-strand DNA breaks. Using a chromatin immunoprecipitation-sequencing method, we identified 35 high-affinity Rif1-binding sites in fission yeast chromosomes. Binding sites tended to be located near dormant origins and to contain at least two copies of a conserved motif, CNWWGTGGGGG. Base substitution within these motifs resulted in complete loss of Rif1 binding and in activation of late-firing or dormant origins located up to 50 kb away. We show that Rif1-binding sites adopt G quadruplex-like structures in vitro, in a manner dependent on the conserved sequence and on other G tracts, and that purified Rif1 preferentially binds to this structure. These results suggest that Rif1 recognizes and binds G quadruplex-like structures at selected intergenic regions, thus generating local chromatin structures that may exert long-range suppressive effects on origin firing.","doi":"10.1038/nsmb.3102","authors":"Kanoh Y, Matsumoto S, Fukatsu R, Kakusho N, Kono N, Renard-Guillet C, Masuda K, Iida K, Nagasawa K, Shirahige K, Masai H","authors_abbrev":"Kanoh Y et al.","pubmed_publication_date":"Nov 2015","pubmed_entrez_date":"2015-10-06","publication_year":"2015","canto_session_key":"f9d56d5255d19a70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hisao Masai","canto_first_approved_date":"2016-07-18 09:08:31","canto_approved_date":"2022-09-29 15:30:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-05 09:42:27","canto_added_date":"2015-10-07 00:18:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Hisao Masai","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-07-18"},{"uniquename":"PMID:11027263","title":"Schizosaccharomyces pombe Hsk1p is a potential cds1p target required for genome integrity.","citation":"Mol Cell Biol 2000 Nov;20(21):7922-32","abstract":"The fission yeast Hsk1p kinase is an essential activator of DNA replication. Here we report the isolation and characterization of a novel mutant allele of the gene. Consistent with its role in the initiation of DNA synthesis, hsk1(ts) genetically interacts with several S-phase mutants. At the restrictive temperature, hsk1(ts) cells suffer abnormal S phase and loss of nuclear integrity and are sensitive to both DNA-damaging agents and replication arrest. Interestingly, hsk1(ts) mutants released to the restrictive temperature after early S-phase arrest in hydroxyurea (HU) are able to complete bulk DNA synthesis but they nevertheless undergo an abnormal mitosis. These findings indicate a second role for hsk1 subsequent to HU arrest. Consistent with a later S-phase role, hsk1(ts) is synthetically lethal with Deltarqh1 (RecQ helicase) or rad21ts (cohesin) mutants and suppressed by Deltacds1 (RAD53 kinase) mutants. We demonstrate that Hsk1p undergoes Cds1p-dependent phosphorylation in response to HU and that it is a direct substrate of purified Cds1p kinase in vitro. These results indicate that the Hsk1p kinase is a potential target of Cds1p regulation and that its activity is required after replication initiation for normal mitosis.","authors":"Snaith HA, Brown GW, Forsburg SL","authors_abbrev":"Snaith HA et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-10-12","publication_year":"2000","canto_session_key":"02e5918aa9716b93","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-11-06 16:34:34","canto_approved_date":"2023-04-08 18:19:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-06 16:51:08","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":48,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC211.04c","SPBC776.12c","SPBC4.04c","SPBC216.05","SPAC1B2.05","SPAC23C4.18c","SPCC550.13","SPCC18B5.11c","SPAC2G11.12","SPBC336.12c","SPAC24H6.05","SPCC338.17c","SPBC29A10.15","SPCC1259.13","SPBC1347.10","SPAC8F11.07c","SPCC16A11.17"],"gene_count":17,"ltp_gene_count":15,"approved_date":"2019-11-06"},{"uniquename":"PMID:21330786","title":"Sgo1 is required for co-segregation of sister chromatids during achiasmate meiosis I.","citation":"Cell Cycle 2011 Mar 15;10(6):951-5","abstract":"The reduction of chromosome number during meiosis is achieved by two successive rounds of chromosome segregation, called meiosis I and meiosis II. While meiosis II is similar to mitosis in that sister kinetochores are bi-oriented and segregate to opposite poles, recombined homologous chromosomes segregate during the first meiotic division. Formation of chiasmata, mono-orientation of sister kinetochores and protection of centromeric cohesion are three major features of meiosis I chromosomes which ensure the reductional nature of chromosome segregation. Here we show that sister chromatids frequently segregate to opposite poles during meiosis I in fission yeast cells that lack both chiasmata and the protector of centromeric cohesion Sgo1. Our data are consistent with the notion that sister kinetochores are frequently bi-oriented in the absence of chiasmata and that Sgo1 prevents equational segregation of sister chromatids during achiasmate meiosis I.","authors":"Dudas A, Ahmad S, Gregan J","authors_abbrev":"Dudas A et al.","pubmed_publication_date":"15 Mar 2011","pubmed_entrez_date":"2011-02-19","publication_year":"2011","canto_session_key":"86a4848cebfe178e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9560432","title":"Exogenous inositol and genes responsible for inositol transport are required for mating and sporulation in Shizosaccharomyces pombe.","citation":"Curr Genet 1998 Apr;33(4):255-61","abstract":"Fission yeast, Schizosaccharomyces pombe, is a natural inositol auxotroph. We show here that the amount of exogenous inositol added to the medium is critical for the control of its life cycle. Above growth-limiting concentrations inositol stimulates mating and sporulation in minimal medium. The effect of inositol is also observed on yeast-extract-medium plates. We selected a mutant, IM49, which mates and sporulates only poorly and show that it is defective in inositol transport. Its defect is in a gene (itr2) coding for a putative 12 membrane-spanning protein. The polypeptide contains the two sugar-transport motifs typical for hexose transporters and shows good homology to the two Saccharomyces cerevisiae inositol transporters. The itr2 gene is essential for cell growth and its mRNA level is repressed by glucose. Mutant IM49 is also complemented by a multicopy suppressor gene (itr1) which codes for a putative hexose transporter with unknown substrate specifity.","authors":"Niederberger C, Gräub R, Schweingruber AM, Fankhauser H, Rusu M, Poitelea M, Edenharter L, Schweingruber ME","authors_abbrev":"Niederberger C et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-05-26","publication_year":"1998","canto_session_key":"de924eb687e556b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-09-10 15:38:52","canto_approved_date":"2022-02-02 17:07:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-09 16:19:56","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.15","SPAC20G8.03","SPBC32C12.02"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2018-09-10"},{"uniquename":"PMID:25659377","title":"Evolutionary and functional analysis of the invariant SWIM domain in the conserved Shu2/SWS1 protein family from Saccharomyces cerevisiae to Homo sapiens.","citation":"Genetics 2015 Apr;199(4):1023-33","abstract":"The Saccharomyces cerevisiae Shu2 protein is an important regulator of Rad51, which promotes homologous recombination (HR). Shu2 functions in the Shu complex with Shu1 and the Rad51 paralogs Csm2 and Psy3. Shu2 belongs to the SWS1 protein family, which is characterized by its SWIM domain (CXC...Xn...CXH), a zinc-binding motif. In humans, SWS1 interacts with the Rad51 paralog SWSAP1. Using genetic and evolutionary analyses, we examined the role of the Shu complex in mitotic and meiotic processes across eukaryotic lineages. We provide evidence that the SWS1 protein family contains orthologous genes in early-branching eukaryote lineages (e.g., Giardia lamblia), as well as in multicellular eukaryotes including Caenorhabditis elegans and Drosophila melanogaster. Using sequence analysis, we expanded the SWIM domain to include an invariant alanine three residues after the terminal CXH motif (CXC…Xn…CXHXXA). We found that the SWIM domain is conserved in all eukaryotic orthologs, and accordingly, in vivo disruption of the invariant residues within the canonical SWIM domain inhibits DNA damage tolerance in yeast and protein-protein interactions in yeast and humans. Furthermore, using evolutionary analyses, we found that yeast and Drosophila Shu2 exhibit strong coevolutionary signatures with meiotic proteins, and in yeast, its disruption leads to decreased meiotic progeny. Together our data indicate that the SWS1 family is an ancient and highly conserved eukaryotic regulator of meiotic and mitotic HR.","doi":"10.1534/genetics.114.173518","authors":"Godin SK, Meslin C, Kabbinavar F, Bratton-Palmer DS, Hornack C, Mihalevic MJ, Yoshida K, Sullivan M, Clark NL, Bernstein KA","authors_abbrev":"Godin SK et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-02-10","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1696233","title":"Fluid-phase endocytosis in yeasts other than Saccharomyces cerevisiae.","citation":"FEMS Microbiol Lett 1990 May;57(1-2):7-11","abstract":"A FITC-dextran internalization assay with Saccharomyces cerevisiae as positive control was used to determine whether fluid-phase endocytosis is a general characteristic of yeasts. Schizosaccharomyces pombe, Pichia polymorpha, Kluyveromyces phaseolosporus, Yarrowia lipolytica and Candida albicans were clearly positive, whereas results obtained with Debaryomyces marama were inconclusive. In all cases internalized FITC-dextran was found to be localized in the vacuoles and the process was always time- and temperature-dependent. Lower eucaryotes, particularly yeasts, appear to have the ability to incorporate substances from the extracellular medium through fluid-phase endocytosis.","authors":"Fernandez N, Puente P, Leal F","authors_abbrev":"Fernandez N et al.","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21113595","title":"Advancing our understanding of functional genome organisation through studies in the fission yeast.","citation":"Curr Genet 2011 Feb;57(1):1-12","abstract":"Significant progress has been made in understanding the functional organisation of the cell nucleus. Still many questions remain to be answered about the relationship between the spatial organisation of the nucleus and the regulation of the genome function. There are many conflicting data in the field making it very difficult to merge published results on mammalian cells into one model on subnuclear chromatin organisation. The fission yeast, Schizosaccharomyces pombe, over the last decades has emerged as a valuable model organism in understanding basic biological mechanisms, especially the cell cycle and chromosome biology. In this review we describe and compare the nuclear organisation in mammalian and fission yeast cells. We believe that fission yeast is a good tool to resolve at least some of the contradictions and unanswered questions concerning functional nuclear architecture, since S. pombe has chromosomes structurally similar to that of human. S. pombe also has the advantage over higher eukaryotes in that the genome can easily be manipulated via homologous recombination making it possible to integrate the tools needed for visualisation of chromosomes using live-cell microscopy. Classical genetic experiments can be used to elucidate what factors are involved in a certain mechanism. The knowledge we have gained during the last few years indicates similarities between the genome organisation in fission yeast and mammalian cells. We therefore propose the use of fission yeast for further advancement of our understanding of functional nuclear organisation.","doi":"10.1007/s00294-010-0327-x","authors":"Olsson I, Bjerling P","authors_abbrev":"Olsson I et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2010-11-30","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32918581","title":"Golgi localization of glycosyltransferases requires Gpp74p in Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2020 Oct;104(20):8897-8909","abstract":"The majority of Golgi glycosyltransferases are type II membrane proteins with a small cytosolic tail at their N-terminus. Several mechanisms for localizing these glycosyltransferases to the Golgi have been proposed. In Saccharomyces cerevisiae, the phosphatidylinositol-4-phosphate-binding protein ScVps74p interacts with the cytosolic tail of a Golgi glycosyltransferase and contributes to its localization. In this study, we investigated whether a similar mechanism functions in the fission yeast Schizosaccharomyces pombe. First, we identified gpp74 +  (GPP34 domain-containing Vps74 homolog protein), a gene encoding the S. pombe homolog of S. cerevisiae Vps74p. Deletion of the gpp74 +  gene resulted in the missorting of three Golgi glycosyltransferases, SpOch1p, SpMnn9p, and SpOmh1p, to vacuoles, but not SpAnp1p, indicating Gpp74p is required for targeting some glycosyltransferases to the Golgi apparatus. Gpp74p with an N-terminal GFP-tag localized to both the Golgi apparatus and the cytosol. Golgi localization of Gpp74p was dependent on the phosphatidylinositol 4-kinase SpPik1p. Site-directed mutagenesis of hydrophobic and basic amino acids in the cytosolic tails of SpOch1p and SpMnn9p resulted in their missorting to vacuoles, indicating these cytosolic N-terminal residues are important for localization in the Golgi. Unexpectedly, no prominent alternations in protein glycosylation were observed in S. pombe gpp74Δ cells, probably due to the residual Golgi localization of some SpOch1p and SpMnn9p in these cells. Collectively, these results demonstrate that both Gpp74p-dependent and Gpp74p-independent mechanisms are responsible for the Golgi localization of glycosyltransferases to the Golgi in S. pombe. KEY POINTS: • Gpp74p is involved in the localization of glycosyltransferases to the Golgi. • The cytosolic tails of glycosyltransferases are important for Golgi localization. • Gpp74p localizes to the Golgi in a SpPik1p-dependent manner.","doi":"10.1007/s00253-020-10881-9","authors":"Ohashi T, Hegi S, Fukunaga T, Hosomi A, Takegawa K","authors_abbrev":"Ohashi T et al.","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-09-12","publication_year":"2020","canto_session_key":"b1a2216c215012e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2020-10-21 13:19:06","canto_approved_date":"2022-02-07 18:08:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-10-13 00:44:02","canto_added_date":"2020-09-15 00:15:04","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.05c","SPAC22E12.16c","SPBC16C6.06","SPBC19C7.12c","SPAC19G12.10c","SPAC5D6.13","SPBC1734.04","SPAC4F10.10c","SPCC1795.03"],"gene_count":9,"ltp_gene_count":4,"approved_date":"2020-10-21"},{"uniquename":"PMID:18984586","title":"Diffusion and directed movement: in vitro motile properties of fission yeast kinesin-14 Pkl1.","citation":"J Biol Chem 2008 Dec 26;283(52):36465-73","abstract":"Fission yeast Pkl1 is a kinesin-14A family member that is known to be localized at the cellular spindle and is capable of hydrolyzing ATP. However, its motility has not been detected. Here, we show that Pkl1 is a slow, minus end-directed microtubule motor with a maximum velocity of 33+/-9 nm/s. The Km,MT value of steady-state ATPase activity of Pkl1 was as low as 6.4+/-1.1 nM, which is 20-30 times smaller than that of kinesin-1 and another kinesin-14A family member, Ncd, indicating a high affinity of Pkl1 for microtubules. However, the duty ratio of 0.05 indicates that Pkl1 spends only a small fraction of the ATPase cycle strongly associated with a microtubule. By using total internal reflection fluorescence microscopy, we demonstrated that single molecules of Pkl1 were not highly processive but only exhibited biased one-dimensional diffusion along microtubules, whereas several molecules of Pkl1, probably fewer than 10 molecules, cooperatively moved along microtubules and substantially reduced the diffusive component in the movement. Our results suggest that Pkl1 molecules work in groups to move and generate forces in a cooperative manner for their mitotic functions.","doi":"10.1074/jbc.M803730200","authors":"Furuta K, Edamatsu M, Maeda Y, Toyoshima YY","authors_abbrev":"Furuta K et al.","pubmed_publication_date":"26 Dec 2008","pubmed_entrez_date":"2008-11-06","publication_year":"2008","canto_session_key":"3dc22cc8e22c9557","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-08 17:20:02","canto_approved_date":"2019-11-08 17:20:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-08 17:19:56","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A11.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-08"},{"uniquename":"EMBL:X78872","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8290359","title":"Cloning and characterisation of the Schizosaccharomyces pombe rad8 gene, a member of the SNF2 helicase family.","citation":"Nucleic Acids Res 1993 Dec 25;21(25):5964-71","abstract":"The Schizosaccharomyces pombe rad8 mutant is sensitive to both UV and gamma irradiation. We have cloned the rad8 gene by complementation of the UV sensitivity of a rad8.190 mutant strain. The gene comprises an open reading frame of 3.4 kb which does not contain any introns and is capable of encoding a 1133 amino acid protein of 129 kDa. Deletion of the gene indicates that it is not essential for cell viability. Recognisable motifs are present for a nuclear localisation signal, a RING finger and helicase domains. The predicted protein is a member of the SNF2 subfamily of proteins and shows particular homology to the Saccharomyces cerevisiae RAD5 protein. Double mutant analysis demonstrated that the rad8 mutant is not epistatic to mutants in the excision repair pathway (rad13) or checkpoint pathway (rad9). Analysis of radiation sensitivity though the cell cycle indicates that, unlike most other rad mutants, rad8 is most sensitive to irradiation during the G1/S period.","authors":"Doe CL, Murray JM, Shayeghi M, Hoskins M, Lehmann AR, Carr AM, Watts FZ","authors_abbrev":"Doe CL et al.","pubmed_publication_date":"25 Dec 1993","pubmed_entrez_date":"1993-12-25","publication_year":"1993","canto_session_key":"d8499d610fc61689","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-05-21 12:09:01","canto_approved_date":"2022-12-13 10:41:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-02 23:36:20","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.18c","SPBC3E7.08c","SPCC338.17c","SPAC13G6.01c","SPCC5E4.06","SPAC664.07c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2013-05-21"},{"uniquename":"PMID:12186627","title":"Interactions between two fission yeast serine/arginine-rich proteins and their modulation by phosphorylation.","citation":"Biochem J 2002 Dec 01;368(Pt 2):527-34","abstract":"The unexpected low number of genes in the human genome has triggered increasing attention to alternative pre-mRNA splicing, and serine/arginine-rich (SR) proteins have been correlated with the complex alternative splicing that is a characteristic of metazoans. SR proteins interact with RNA and splicing protein factors, and they also undergo reversible phosphorylation, thereby regulating constitutive and alternative splicing in mammals and Drosophila. However, it is not clear whether the features of SR proteins and alternative splicing are present in simple and genetically tractable organisms, such as yeasts. In the present study, we show that the SR-like proteins Srp1 and Srp2, found in the fission yeast Schizosaccharomyces pombe, interact with each other and the interaction is modulated by protein phosphorylation. By using Srp1 as bait in a yeast two-hybrid analysis, we specifically isolated Srp2 from a random screen. This Srp interaction was confirmed by a glutathione-S-transferase pull-down assay. We also found that the Srp1-Srp2 complex was phosphorylated at a reduced efficiency by a fission yeast SR-specific kinase, Dis1-suppression kinase (Dsk1). Conversely, Dsk1-mediated phosphorylation inhibited the formation of the Srp complex. These findings offer the first example in fission yeast for interactions between SR-related proteins and the modulation of the interactions by specific protein phosphorylation, suggesting that a mammalian-like SR protein function may exist in fission yeast.","authors":"Tang Z, Käufer NF, Lin RJ","authors_abbrev":"Tang Z et al.","pubmed_publication_date":"01 Dec 2002","pubmed_entrez_date":"2002-08-21","publication_year":"2002","canto_session_key":"6fa67f13900a2d46","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-23 17:34:34","canto_approved_date":"2023-12-24 11:08:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-23 17:33:58","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC530.14c","SPAC16.02c","SPBC11C11.08"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-03-23"},{"uniquename":"PMID:30072439","title":"The putative ceramide-conjugation protein Cwh43 regulates G0 quiescence, nutrient metabolism and lipid homeostasis in fission yeast.","citation":"J Cell Sci 2018 Aug 21;131(16)","abstract":"Cellular nutrient states control whether cells proliferate, or whether they enter or exit quiescence. Here, we report characterizations of fission yeast temperature-sensitive (ts) mutants of the evolutionarily conserved transmembrane protein Cwh43, and explore its relevance to utilization of glucose, nitrogen source and lipids. GFP-tagged Cwh43 localizes at ER associated with the nuclear envelope and the plasma membrane, as in budding yeast. We found that  cwh43  mutants failed to divide in low glucose and lost viability during quiescence under nitrogen starvation. In  cwh43  mutants, comprehensive metabolome analysis demonstrated dramatic changes in marker metabolites that altered under low glucose and/or nitrogen starvation, although  cwh43  cells apparently consumed glucose in the culture medium. Furthermore, we found that  cwh43  mutant cells had elevated levels of triacylglycerols (TGs) and coenzyme A, and that they accumulated lipid droplets. Notably, TG biosynthesis was required to maintain cell division in the  cwh43  mutant. Thus, Cwh43 affects utilization of glucose and nitrogen sources, as well as storage lipid metabolism. These results may fit a notion developed in budding yeast stating that Cwh43 conjugates ceramide to glycosylphosphatidylinositol (GPI)-anchored proteins and maintains integrity of membrane organization.","doi":"10.1242/jcs.217331","authors":"Nakazawa N, Teruya T, Sajiki K, Kumada K, Villar-Briones A, Arakawa O, Takada J, Saitoh S, Yanagida M","authors_abbrev":"Nakazawa N et al.","pubmed_publication_date":"21 Aug 2018","pubmed_entrez_date":"2018-08-04","publication_year":"2018","canto_session_key":"468fa2c5da611313","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Norihiko Nakazawa","canto_first_approved_date":"2019-07-12 06:15:15","canto_approved_date":"2026-01-31 15:35:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-27 21:44:37","canto_added_date":"2018-08-05 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":75,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Norihiko Nakazawa","community_curator":true,"annotation_count":31,"orcid":"0000-0001-8386-0812","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC548.06c","SPCC1235.14","SPBC776.14","SPCC5E4.04","SPBC14C8.01c","SPAC589.12","SPCC1235.15"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2019-07-12"},{"uniquename":"PMID:21607855","title":"Heterologous expression of GPCRs in fission yeast.","citation":"Methods Mol Biol 2011;746:113-31","abstract":"In this chapter, we describe methods to heterologously express G protein-coupled receptors (GPCRs) in the fission yeast Schizosaccharomyces (Sz.) pombe. GPCRs regulate a diverse range of biological processes in all eukaryotic cells, including plants, insects, humans, and yeast. The high degree of conservation between GPCRs from different organisms has facilitated the development of a large number of model systems to enable study of this pharmaceutically important family of cell-surface receptors. Of the many model systems available for investigating GPCRs, yeast have proven to be one of the more attractive. Yeasts' amenability to both genetic and biochemical manipulation, a reduced number of endogenous GPCRs and their relative low culturing costs has facilitated their use in many high-throughput drug screens. Given the high number of detailed methods relating to the expression of GPCRs within budding yeast, we have focused our attention on the use of fission yeast as a model system. We describe the methods used and provide examples from our own experiences of expressing a number of human GPCRs in Sz. pombe cells.","doi":"10.1007/978-1-61779-126-0_7","authors":"Davey J, Ladds G","authors_abbrev":"Davey J et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-05-25","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15537703","title":"The nuclear kinase Lsk1p positively regulates the septation initiation network and promotes the successful completion of cytokinesis in response to perturbation of the actomyosin ring in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2005 Jan;16(1):358-71","abstract":"Cytokinesis in fission yeast requires the function of an actomyosin-based contractile ring whose constriction is dependent on a signaling module termed the septation initiation network (SIN). In response to minor perturbation of the ring, the duration of SIN signaling is extended concurrently with a delay in nuclear cycle progression. These mechanisms require the conserved phosphatase Clp1p/Flp1p and facilitate the successful completion of cytokinesis, thereby increasing cellular viability. To isolate novel components of this cytokinesis monitoring system, we screened a genome-wide bank of protein kinase deletion mutants and identified Lsk1p, a nuclear-localized protein kinase. Similar to clp1Delta mutants, and in contrast to wild type, lsk1Delta cells are unable to maintain the integrity of the actomyosin ring upon treatment with low doses (0.3 microM) of latrunculin A. However, unlike clp1Delta mutants, lsk1Delta cells are competent to delay nuclear cycle progression after cytokinetic failure. In addition, lsk1Delta mutants suppress the lethal, multiseptate phenotype conferred by hyperactivation of the SIN, demonstrating that Lsk1p is a positive regulator of this module. In this report, we demonstrate that Lsk1p acts in parallel to Clp1p to promote actomyosin ring stability upon checkpoint activation. Our studies also establish that actomyosin ring maintenance and nuclear cycle delay in response to cytokinetic perturbation can be genetically resolved into independent pathways.","authors":"Karagiannis J, Bimbó A, Rajagopalan S, Liu J, Balasubramanian MK","authors_abbrev":"Karagiannis J et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-11-13","publication_year":"2005","canto_session_key":"28f15204b6b233af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-07 20:22:02","canto_approved_date":"2024-04-03 09:46:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-11 15:35:30","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC24C6.07","SPAC23C11.16","SPAC1782.09c","SPBC32H8.12c","SPCC613.04c","SPAC2F3.15","SPAC6F6.08c","SPAC9G1.09"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-10-07"},{"uniquename":"PMID:29180432","title":"Phosphorylation of CENP-C by Aurora B facilitates kinetochore attachment error correction in mitosis.","citation":"Proc Natl Acad Sci U S A 2017 Dec 12;114(50):E10667-E10676","abstract":"Kinetochores are superprotein complexes that orchestrate chromosome segregation via a dynamic interaction with spindle microtubules. A physical connection between CENP-C and the Mis12-Ndc80-Knl1 (KMN) protein network is an important pathway that is used to assemble kinetochores on CENP-A nucleosomes. Multiple outer kinetochore components are phosphorylated by Aurora B kinase to activate the spindle assembly checkpoint (SAC) and to ensure accurate chromosome segregation. However, it is unknown whether Aurora B can phosphorylate inner kinetochore components to facilitate proper mitotic chromosome segregation. Here, we reported the structure of the fission yeast  Schizosaccharomyces pombe  Mis12-Nnf1 complex and showed that N-terminal residues 26-50 in Cnp3 (the CENP-C homolog of  S. pombe ) are responsible for interacting with the Mis12 complex. Interestingly, Thr28 of Cnp3 is a substrate of Ark1 (the Aurora B homolog of  S. pombe ), and phosphorylation impairs the interaction between the Cnp3 and Mis12 complex. The expression of a phosphorylation-mimicking Cnp3 mutant results in defective chromosome segregation due to improper kinetochore assembly. These results establish a previously uncharacterized regulatory mechanism involved in CENP-C-Mis12-facilitated kinetochore attachment error correction to ensure accurate chromosome segregation during mitosis.","doi":"10.1073/pnas.1710506114","authors":"Zhou X, Zheng F, Wang C, Wu M, Zhang X, Wang Q, Yao X, Fu C, Zhang X, Zang J","authors_abbrev":"Zhou X et al.","pubmed_publication_date":"12 Dec 2017","pubmed_entrez_date":"2017-11-29","publication_year":"2017","canto_session_key":"a03f8c91ccf38c01","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-07 10:46:06","canto_approved_date":"2023-06-20 15:21:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-02 13:44:29","canto_added_date":"2017-11-30 01:15:15","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.13c","SPCC1020.02","SPBC409.09c","SPBC409.04c","SPAC29E6.04","SPBC1861.01c","SPBC11C11.03"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2019-01-07","pdb_entries":[{"pdb_id":"5wwl","gene_chains":[{"gene_uniquename":"SPAC29E6.04","chain":"N","position":"1-140"},{"gene_uniquename":"SPBC409.04c","chain":"M","position":"1-215"}],"title":"Crystal structure of the Schizogenesis pombe kinetochore Mis12C subcomplex","entry_authors":"Wang C,Zhou X,Wu M,Zhang X,Zang J","entry_authors_abbrev":"Wang C et al.","reference_uniquename":"PMID:29180432","experimental_method":"X-ray","resolution":"2.4"}]},{"uniquename":"PMID:29219228","title":"Structure and function of yeast and fungal Na +  /H +  antiporters.","citation":"IUBMB Life 2018 Jan;70(1):23-31","abstract":"Sodium proton antiporters (or sodium proton exchangers [NHEs]) are a critical family of membrane proteins that exchange sodium for protons across cell membranes. In yeast and plants, their primary function is to keep the sodium concentration low inside the cytoplasm. One class of NHE constitutively expressed in yeast is the plasma membrane Na +  /H +  antiporter, and another class is expressed on the endosomal/vacuolar membrane. At present, four bacterial plasma membrane antiporter structures are known and nuclear magnetic resonance structures are available for the membrane spanning transmembrane helices of mammalian and yeast NHEs. Additionally, a vast amount of mutational data are available on the role of individual amino acids and critical motifs involved in transport. We combine this information to obtain a more detailed picture of the yeast NHE plasma membrane protein and review mechanisms of transport, conserved motifs, unique residues important in function, and regulation of these proteins. The Na +  /H +  antiporter of Schizosaccharomyces pombe, SpNHE1, is an interesting model protein in an easy to study system and is representative of fungal Na +  /H +  antiporters. © IUBMB Life, 70(1):23-31, 2018.","doi":"10.1002/iub.1701","authors":"Dutta D, Fliegel L","authors_abbrev":"Dutta D et al.","pubmed_publication_date":"Jan 2018","pubmed_entrez_date":"2017-12-09","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-12-10 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30076928","title":"Point mutation A394E in the central intrinsic disordered region of Rna14 leads to chromosomal instability in fission yeast.","citation":"Int J Biol Macromol 2018 Nov;119:785-791","abstract":"Accurate chromosomal segregation is crucial for the maintenance of genomic integrity. Rna14 is a major component of the yeast pre-mRNA 3'-end processing factor, the cleavage factor IA complex, and is involved in cleavage and polyadenylation of mRNA in the nucleus. Rna14 is also essential for the maintenance of genomic integrity in fission yeast Schizosaccharomyces pombe. In the present study, we report that a non-homologous mutation, A394E that is present in the central intrinsic disordered region of Rna14 leads to chromosomal instability in fission yeast. This mutation was shown to disrupt chromosome segregation and 3'-end maturation, and also affects the pre-mRNA splicing in vivo at non-permissive temperatures. We observed that a significant part of Rna14 is intrinsically disordered, that includes the N- and C-terminal of Rna14, as well as the central region containing the HAT repeats and the mutation within amino acid residues 372-435. These regions are crucial for the function of Rna14 as they are involved in the interaction of Rna14 with other proteins.","doi":"10.1016/j.ijbiomac.2018.07.193","authors":"Sonkar A, Lyngdoh DL, Shukla R, Shukla H, Tripathi T, Ahmed S","authors_abbrev":"Sonkar A et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-08-05","publication_year":"2018","canto_session_key":"84cf2fbfe26627cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shakil Ahmed","canto_first_approved_date":"2020-09-28 15:08:54","canto_approved_date":"2020-09-28 15:08:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-09-26 09:23:07","canto_added_date":"2018-08-06 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Shakil Ahmed","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAC29E6.08","SPAC6F12.17","SPCC1259.13"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2020-09-28"},{"uniquename":"PMID:21686774","title":"A novel mitochondrial ATP8 gene mutation in a patient with apical hypertrophic cardiomyopathy and neuropathy.","citation":"BMJ Case Rep 2009;2009","abstract":"To identify the biochemical and molecular genetic defect in a 16-year-old patient presenting with apical hypertrophic cardiomyopathy and neuropathy suspected for a mitochondrial disorder.Measurement of the mitochondrial energy-generating system (MEGS) capacity in muscle and enzyme analysis in muscle and fibroblasts were performed. Relevant parts of the mitochondrial DNA were analysed by sequencing.A homoplasmic nonsense mutation m.8529G→A (p.Trp55X) was found in the mitochondrial ATP8 gene in the patient's fibroblasts and muscle tissue. Reduced complex V activity was measured in the patient's fibroblasts and muscle tissue, and was confirmed in cybrid clones containing patient-derived mitochondrial DNAWe describe the first pathogenic mutation in the mitochondrial ATP8 gene, resulting in an improper assembly and reduced activity of the complex V holoenzyme.","doi":"10.1136/bcr.07.2008.0504","authors":"Jonckheere AI, Hogeveen M, Nijtmans L, van den Brand M, Janssen A, Diepstra H, van den Brandt F, van den Heuvel B, Hol F, Hofste T, Kapusta L, Dillmann U, Shamdeen M, Smeitink J, Smeitink J, Rodenburg R","authors_abbrev":"Jonckheere AI et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2011-06-21","publication_year":"2009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPMIT.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24047983","title":"Measuring affinities of fission yeast spindle pole body proteins in live cells across the cell cycle.","citation":"Biophys J 2013 Sep 17;105(6):1324-35","abstract":"Characterizing protein-protein interactions is essential for understanding molecular mechanisms, although reproducing cellular conditions in vitro is challenging and some proteins are difficult to purify. We developed a method to measure binding to cellular structures using fission yeast cells as reaction vessels. We varied the concentrations of Sid2p and Mob1p (proteins of the septation initiation network) and measured their binding to spindle pole bodies (SPBs), the centrosome equivalent of yeast. From our measurements we infer that Sid2p and Mob1p both exist as monomeric, heterodimeric, and homodimeric species throughout the cell cycle. During interphase these species have widely different affinities for their common receptor Cdc11p on the SPB. The data support a model with a subset of Cdc11p binding the heterodimeric species with a Kd < 0.1 μM when Sid2p binds Mob1p-Cdc11p and Kd in the micromolar range when Mob1p binds Sid2p-Cdc11p. During mitosis an additional species presumed to be the phosphorylated Sid2p-Mob1p heterodimer binds SPBs with a lower affinity. Homodimers of Sid2p or Mob1p bind to the rest of Cdc11p at SPBs with lower affinity: Kds > 10 μM during interphase and somewhat stronger during mitosis. These measurements allowed us to account for the fluctuations in Sid2p binding to SPBs throughout the cell cycle.","doi":"10.1016/j.bpj.2013.08.017","authors":"McCormick CD, Akamatsu MS, Ti SC, Pollard TD","authors_abbrev":"McCormick CD et al.","pubmed_publication_date":"17 Sep 2013","pubmed_entrez_date":"2013-09-20","publication_year":"2013","canto_session_key":"67e6d603004e18cf","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.13c","SPAC24B11.11c","SPCC1739.11c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:2955197","title":"Fungal 1,3-beta-glucan synthase.","citation":"Methods Enzymol 1987;138:637-42","abstract":"","authors":"Cabib E, Kang MS","authors_abbrev":"Cabib E et al.","pubmed_publication_date":"1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32546512","title":"Inactivation of fission yeast Erh1 de-represses  pho1  expression: evidence that Erh1 is a negative regulator of  prt  lncRNA termination.","citation":"RNA 2020 Oct;26(10):1334-1344","abstract":"Fission yeast Erh1 exists in a complex with RNA-binding protein Mmi1. Deletion of  erh1  up-regulates the phosphate homeostasis gene  pho1 , which is normally repressed by transcription in  cis  of a 5' flanking  prt  lncRNA. Here we present evidence that de-repression of  pho1  by e rh1 Δ is achieved through precocious 3'-processing/termination of  prt  lncRNA synthesis, to wit: (i)  erh1 Δ does not affect the activity of the  prt  or  pho1  promoters per se; (ii) de-repression by  erh1 Δ depends on CPF (cleavage and polyadenylation factor) subunits Ctf1, Dis2, Ssu72, Swd22, and Ppn1 and on termination factor Rhn1; (iii) de-repression requires synthesis by the Asp1 IPP kinase of inositol 1-pyrophosphates (1-IPPs); (iv) de-repression is effaced by mutating Thr4 of the RNA polymerase II CTD to alanine; and (v)  erh1 Δ exerts an additive effect on  pho1  de-repression in combination with mutating CTD Ser7 to alanine and with deletion of the IPP pyrophosphatase Aps1. These findings point to Erh1 as an antagonist of lncRNA termination in the  prt-pho1  axis. In contrast, in  mmi1 Δ cells there is a reduction in  pho1  mRNA and increase in the formation of a  prt-pho1  read-through transcript, consistent with Mmi1 being an agonist of  prt  termination. We envision that Erh1 acts as a brake on Mmi1's ability to promote CPF-dependent termination during  prt  lncRNA synthesis. Consistent with this idea,  erh1 Δ de-repression of  pho1  was eliminated by mutating the Mmi1-binding sites in the  prt  lncRNA.","doi":"10.1261/rna.076463.120","authors":"Schwer B, Sanchez AM, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-06-18","publication_year":"2020","canto_session_key":"95ec493fb8fa90cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana Sanchez","canto_first_approved_date":"2022-10-26 11:51:05","canto_approved_date":"2024-04-02 13:40:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-21 16:37:56","canto_added_date":"2020-06-19 00:15:06","annotation_curators":[{"name":"Ana Sanchez","community_curator":true,"annotation_count":66,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPAC19G12.17","SPBC337.03","SPBC28F2.12","SPCC74.02c","SPAC824.04","SPBC3B9.11c","SPBC776.02c","SPAC13G6.14","SPCC736.12c","SPAC3G9.04","SPNCRNA.1712","SPCC1672.06c"],"gene_count":13,"ltp_gene_count":11,"approved_date":"2022-10-26"},{"uniquename":"PMID:23896534","title":"Regulation of cytotoxic, non-estrogenic, oxidative stress-induced processes of zearalenone in the fission yeast Schizosaccharomyces pombe.","citation":"Toxicon 2013 Oct;73:130-43","abstract":"This study investigates the non-estrogenic mode of zearalenone (ZEA) toxicity in a novel aspect via accumulation of reactive oxygen species (ROS) and the regulation of the activities of antioxidant enzymes in the Schizosaccharomyces pombe in acute toxicity tests. In comparison with the control, 500 μM ZEA treatment caused 66% decrease in the concentration of glutathione (GSH), which was a consequence, in the absence of ZEA-GSH interaction, of the GSH-consuming processes of the antioxidant system; this depletion of GSH initiated a 1.8- and 2.0-fold accumulation of the superoxide anion and hydrogen peroxide, but did not increase the concentration of the hydroxyl radical; ROS-induced adaptation processes via activation of the Pap1 transcription factor resulted in significantly increased activities of superoxide dismutases, catalase, glutathione reductase and glutathione S-transferase, and decreased activities of glutathione peroxidase and glucose-6-phosphate dehydrogenase. This treatment altered the sterol composition of the cells by inducing decreased concentrations of ergosterol, squalene and 24-methylene-24,25-hydrolanosterol, and also elevated the number of fragmented nuclei. Cells strived to correct the unbalanced redox state by regulation of the antioxidant system, but this was not enough to defend the cells from the disturbed sterol composition, the cell cycle arrest, and the fragmentation of nuclei.","doi":"10.1016/j.toxicon.2013.07.015","authors":"Mike N, Papp G, Certik M, Czibulya Z, Kunsági-Máté S, Ember I, Vágvölgyi C, Pesti M, Gazdag Z","authors_abbrev":"Mike N et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-07-31","publication_year":"2013","canto_session_key":"0e22a76c0124f124","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-03-20 15:22:23","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-03-20 15:22:09","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-03-20"},{"uniquename":"EMBL:AU009395","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36468882","title":"Structures of Fission Yeast Inositol Pyrophosphate Kinase Asp1 in Ligand-Free, Substrate-Bound, and Product-Bound States.","citation":"mBio 2022 Dec 20;13(6):e0308722","abstract":"Expression of the fission yeast Schizosaccharomyces pombe phosphate regulon is sensitive to the intracellular level of the inositol pyrophosphate signaling molecule 1,5-IP 8 . IP 8  dynamics are determined by Asp1, a bifunctional enzyme consisting of an N-terminal kinase domain and a C-terminal pyrophosphatase domain that catalyze IP 8  synthesis and catabolism, respectively. Here, we report structures of the Asp1 kinase domain, crystallized with two protomers in the asymmetric unit, one of which was complexed with ligands (ADPNP, ADP, or ATP; Mg 2+  or Mn 2+ ; IP 6 , 5-IP 7 , or 1,5-IP 8 ) and the other which was ligand-free. The ligand-free enzyme adopts an \"open\" conformation that allows ingress of substrates and egress of products. ADPNP, ADP, and ATP and associated metal ions occupy a deep phospho-donor pocket in the active site. IP 6  or 5-IP 7  engagement above the nucleotide favors adoption of a \"closed\" conformation, in which surface protein segments undergo movement and a disordered-to-ordered transition to form an inositol polyphosphate-binding site. In a structure mimetic of the kinase Michaelis complex, the anionic 5-IP 7  phosphates are encaged by an ensemble of nine cationic amino acids: Lys43, Arg223, Lys224, Lys260, Arg274, Arg285, Lys290, Arg293, and Lys341. Alanine mutagenesis of amino acids that contact the adenosine nucleoside of the ATP donor underscored the contributions of Asp258 interaction with the ribose 3'-OH and of Glu248 with adenine- N  6 . Changing Glu248 to Gln elicited a gain of function whereby the kinase became adept at using GTP as phosphate donor. Wild-type Asp1 kinase can utilize  N  6 -benzyl-ATP as phosphate donor.  IMPORTANCE  The inositol pyrophosphate signaling molecule 1,5-IP 8  modulates fission yeast phosphate homeostasis via its action as an agonist of RNA 3'-processing and transcription termination. Cellular IP 8  levels are determined by Asp1, a bifunctional enzyme composed of an N-terminal kinase and a C-terminal pyrophosphatase domain. Here, we present a series of crystal structures of the Asp1 kinase domain, in a ligand-free state and in complexes with nucleotides ADPNP, ADP, and ATP, divalent cations magnesium and manganese, and inositol polyphosphates IP 6 , 5-IP 7 , and 1,5-IP 8 . Substrate binding elicits a switch from open to closed conformations, entailing a disordered-to-ordered transition and a rearrangement or movement of two peptide segments that form a binding site for the phospho-acceptor. Our structures, along with structure-guided mutagenesis, fortify understanding of the mechanism and substrate specificity of Asp1 kinase, and they extend and complement structural and functional studies of the orthologous human kinase PPIP5K2.","doi":"10.1128/mbio.03087-22","authors":"Benjamin B, Goldgur Y, Jork N, Jessen HJ, Schwer B, Shuman S","authors_abbrev":"Benjamin B et al.","pubmed_publication_date":"20 Dec 2022","pubmed_entrez_date":"2022-12-05","publication_year":"2022","canto_session_key":"9a6b5c972816ede4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-07 16:26:59","canto_approved_date":"2024-01-08 16:35:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 16:29:36","canto_added_date":"2022-12-06 01:15:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-03-07","pdb_entries":[{"pdb_id":"8e1j","gene_chains":[{"gene_uniquename":"SPCC1672.06c","chain":"A/B","position":"31-364"}],"title":"Asp1 kinase in complex with 1,5-IP8","entry_authors":"Goldgur Y,Shuman S,Benjamin B","entry_authors_abbrev":"Goldgur Y et al.","reference_uniquename":"PMID:36468882","experimental_method":"X-ray","resolution":"1.6"},{"pdb_id":"8e1t","gene_chains":[{"gene_uniquename":"SPCC1672.06c","chain":"A/B","position":"31-364"}],"title":"Asp1 kinase in complex with ADPNP Mg IP7","entry_authors":"Goldgur Y,Shuman S,Benjamin B","entry_authors_abbrev":"Goldgur Y et al.","reference_uniquename":"PMID:36468882","experimental_method":"X-ray","resolution":"1.71"},{"pdb_id":"8e1v","gene_chains":[{"gene_uniquename":"SPCC1672.06c","chain":"A/B","position":"31-364"}],"title":"Asp1 kinase in complex with ADPNP Mg IP6","entry_authors":"Goldgur Y,Shuman S,Benjamin B","entry_authors_abbrev":"Goldgur Y et al.","reference_uniquename":"PMID:36468882","experimental_method":"X-ray","resolution":"1.9"},{"pdb_id":"8e1s","gene_chains":[{"gene_uniquename":"SPCC1672.06c","chain":"A/B","position":"31-364"}],"title":"Asp1 kinase in complex with ADPNP Mn IP6","entry_authors":"Goldgur Y,Shuman S,Benjamin B","entry_authors_abbrev":"Goldgur Y et al.","reference_uniquename":"PMID:36468882","experimental_method":"X-ray","resolution":"1.72"},{"pdb_id":"8e1h","gene_chains":[{"gene_uniquename":"SPCC1672.06c","chain":"A/B","position":"31-364"}],"title":"Asp1 kinase in complex with ADP Mg 5-IP7","entry_authors":"Goldgur Y,Shuman S,Benjamin B","entry_authors_abbrev":"Goldgur Y et al.","reference_uniquename":"PMID:36468882","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:19390147","title":"Structure of SRP14 from the Schizosaccharomyces pombe signal recognition particle.","citation":"Acta Crystallogr D Biol Crystallogr 2009 May;65(Pt 5):421-33","abstract":"The signal recognition particle (SRP) Alu domain has been implicated in translation elongation arrest in yeasts and mammals. Fission yeast SRP RNA is similar to that of mammals, but has a minimal Alu-domain RNA lacking two stem-loops. The mammalian Alu-domain proteins SRP9 and SRP14 bind their cognate Alu RNA as a heterodimer. However, in yeasts, notably Saccharomyces cerevisiae, SRP14 is thought to bind Alu RNA as a homodimer, the SRP9 protein being replaced by SRP21, the function of which is not yet clear. Structural characterization of the Schizosaccharomyces pombe Alu domain may thus help to identify the critical features required for elongation arrest. Here, the crystal structure of the SRP14 subunit of S. pombe SRP (SpSRP14) which crystallizes as a homodimer, is presented. Comparison of the SpSRP14 homodimer with the known structure of human SRP9/14 in complex with Alu RNA suggests that many of the protein-RNA contacts centred on the conserved U-turn motif are likely to be conserved in fission yeast. Initial attempts to solve the structure using traditional selenomethionine SAD labelling failed. However, two As atoms originating from the cacodylate buffer were found to make cysteine adducts and strongly contributed to the anomalous substructure. These adducts were highly radiation-sensitive and this property was exploited using the RIP (radiation-damage-induced phasing) method. The combination of SAD and RIP phases yielded an interpretable electron-density map. This example will be of general interest to crystallographers attempting de novo phasing from crystals grown in cacodylate buffer.","doi":"10.1107/S0907444909005484","authors":"Brooks MA, Ravelli RB, McCarthy AA, Strub K, Cusack S","authors_abbrev":"Brooks MA et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-04-25","publication_year":"2009","canto_session_key":"1cde2d9d360a0671","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-12 16:31:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-12 16:30:58","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19B12.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-12","pdb_entries":[{"pdb_id":"2w9j","gene_chains":[{"gene_uniquename":"SPAC19B12.09","chain":"A/B","position":"1-91"}],"title":"The crystal structure of SRP14 from the Schizosaccharomyces pombe signal recognition particle","entry_authors":"Brooks MA,Ravelli RBG,McCarthy AA,Strub K,Cusack S","entry_authors_abbrev":"Brooks MA et al.","reference_uniquename":"PMID:19390147","experimental_method":"X-ray","resolution":"2.6"}]},{"uniquename":"PMID:31591131","title":"F-BAR Cdc15 Promotes Cdc42 Activation During Cytokinesis and Cell Polarization in  Schizosaccharomyces pombe .","citation":"Genetics 2019 Dec;213(4):1341-1356","abstract":"Cdc42, a Rho-family GTPase, is a master regulator of cell polarity. Recently, it has been shown that Cdc42 also facilitates proper cytokinesis in the fission yeast  Schizosaccharomyces pombe  Cdc42 is activated by two partially redundant GEFs, Gef1 and Scd1. Although both GEFs activate Cdc42, their deletion mutants display distinct phenotypes, indicating that they are differentially regulated by an unknown mechanism. During cytokinesis, Gef1 localizes to the division site and activates Cdc42 to initiate ring constriction and septum ingression. Here, we report that the F-BAR protein Cdc15 promotes Gef1 localization to its functional sites. We show that  cdc15  promotes Gef1 association with cortical puncta at the incipient division site to activate Cdc42 during ring assembly. Moreover,  cdc15  phospho-mutants phenocopy the polarity phenotypes of  gef1  mutants. In a hypermorphic  cdc15  mutant, Gef1 localizes precociously to the division site and is readily detected at the cortical patches and the cell cortex. Correspondingly, the hypermorphic  cdc15  mutant shows increased bipolarity during interphase and precocious Cdc42 activation at the division site during cytokinesis. Finally, loss of  gef1  in hypermorphic  cdc15  mutants abrogates the increased bipolarity and precocious Cdc42 activation phenotype. We did not see any change in the localization of the other GEF Scd1 in a Cdc15-dependent manner. Our data indicate that Cdc15 facilitates Cdc42 activation at the division site during cytokinesis at the cell cortex to promote bipolarity and this is mediated by promoting Gef1 localization to these sites.","doi":"10.1534/genetics.119.302649","authors":"Hercyk BS, Das ME","authors_abbrev":"Hercyk BS et al.","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-10-09","publication_year":"2019","canto_session_key":"da2a15af785735e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maitreyi Das","canto_first_approved_date":"2019-10-18 14:31:04","canto_approved_date":"2023-10-08 11:54:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-16 19:25:33","canto_added_date":"2019-10-10 00:15:04","annotation_curators":[{"name":"Maitreyi Das","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.09","SPBC725.09c","SPAC24B11.11c","SPAC110.03","SPAC16E8.09","SPCC4B3.15","SPAC23C11.16","SPAC20G8.05c","SPAC1F5.04c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2019-10-18"},{"uniquename":"PMID:30955932","title":"Noisy Cell-Size-Correlated Expression of Cyclin B Drives Probabilistic Cell-Size Homeostasis in Fission Yeast.","citation":"Curr Biol 2019 Apr 22;29(8):1379-1386.e4","abstract":"How cells correct deviations from a mean cell size at mitosis remains uncertain. Classical cell-size homeostasis models are the sizer, timer, and adder [1]. Sizers postulate that cells divide at some threshold size; timers, that cells grow for a set time; and adders, that cells add a constant volume before division. Here, we show that a size-based probabilistic model of cell-size control at the G2/M transition (P(Div)) can generate realistic cell-size homeostasis in silico. In fission yeast cells, Cyclin B Cdc13  scales with size, and we propose that this increases the likelihood of mitotic entry, while molecular noise in its expression adds a probabilistic component to the model. Varying Cdc13 expression levels exogenously using a newly developed tetracycline inducible promoter shows that both the level and variability of its expression influence cell size at division. Our results demonstrate that as cells grow larger, their probability of dividing increases, and this is sufficient to generate cell-size homeostasis. Size-correlated Cdc13 expression forms part of the molecular circuitry of this system.","doi":"10.1016/j.cub.2019.03.011","authors":"Patterson JO, Rees P, Nurse P","authors_abbrev":"Patterson JO et al.","pubmed_publication_date":"22 Apr 2019","pubmed_entrez_date":"2019-04-09","publication_year":"2019","canto_session_key":"2ab60436ce72611d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-05-02 15:01:55","canto_approved_date":"2019-05-02 15:01:55","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-04-23 15:34:00","canto_added_date":"2019-04-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.03","SPAC24H6.05","SPBC11B10.09","SPCC18B5.03"],"gene_count":4,"ltp_gene_count":0,"approved_date":"2019-05-02"},{"uniquename":"EMBL:AB084853","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21B10.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9801299","title":"A Schizosaccharomyces pombe artificial chromosome large DNA cloning system.","citation":"Nucleic Acids Res 1998 Nov 15;26(22):5052-60","abstract":"The feasibility of using the fission yeast, Schizosaccharomyces pombe , as a host for the propagation of cloned large fragments of human DNA has been investigated. Two acentric vector arms were utilized; these carry autonomously replicating sequences ( ars elements), selectable markers ( ura4(+) or LEU2 ) and 250 bp of S. pombe terminal telomeric repeats. All cloning was performed between the unique sites in both vector arms for the restriction endonuclease Not I. Initially the system was tested by converting six previously characterized cosmids from human chromosome 11p13 into a form that could be propagated in S.pombe as linear episomal elements of 50-60 kb in length. In all transformants analysed these cosmids were maintained intact. To test if larger fragments of human DNA could also be propagated total human DNA was digested with Not I and size fractionated by pulsed field gel electrophoresis (PFGE). Fractions of 100-1000 kb were ligated to Not I-digested vector arms and transformed into S.pombe protoplasts in the presence of lipofectin. Prototrophic ura+leu+transformants were obtained which upon examination by PFGE were found to contain additional linear chromosomes migrating at between 100 and 500 kb with a copy number of 5-10 copies/cell. Hybridization analyses revealed that these additional bands contained human DNA. Fluorescent in situ hybridization (FISH) analyses of several independent clones indicated that the inserts were derived from single loci within the human genome. These analyses clearly demonstrate that it is possible to clone large fragments of heterologous DNA in fission yeast using this S.p ombe artificial chromosome system which we have called SPARC. This vector-host system will complement the various other systems for cloning large DNA fragments.","authors":"Young DJ, Nimmo ER, Allshire RC","authors_abbrev":"Young DJ et al.","pubmed_publication_date":"15 Nov 1998","pubmed_entrez_date":"1998-11-04","publication_year":"1998","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15988528","title":"The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae.","citation":"Nature 2005 Jun 30;435(7046):1257-61","abstract":"SCF-type E3 ubiquitin ligases are multi-protein complexes required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome. Cullins, together with the RING-finger protein Rbx1, form the catalytic core of the ligase, and recruit the substrate-recognition module. Cycles of covalent modification of cullins by the ubiquitin-like molecule Nedd8 (neddylation) and removal of Nedd8 by the COP9 signalosome (deneddylation) positively regulate E3 ligase activity. Here we report the identification and analysis of a widely conserved protein that is required for cullin neddylation in the nematode Caenorhabditis elegans and the yeast Saccharomyces cerevisiae. C. elegans DCN-1 and S. cerevisiae Dcn1p (defective in cullin neddylation) are characterized by a novel UBA-like ubiquitin-binding domain and a DUF298 domain of unknown function. Consistent with their requirements for neddylation, DCN-1 and Dcn1p directly bind Nedd8 and physically associate with cullins in both species. Moreover, overexpression of Dcn1p in yeast results in the accumulation of Nedd8-modified cullin Cdc53p. Both in vivo and in vitro experiments indicate that Dcn1p does not inhibit deneddylation of Cdc53p by the COP9 signalosome, but greatly increases the kinetics of the neddylation reaction.","authors":"Kurz T, Ozlü N, Rudolf F, O'Rourke SM, Luke B, Hofmann K, Hyman AA, Bowerman B, Peter M","authors_abbrev":"Kurz T et al.","pubmed_publication_date":"30 Jun 2005","pubmed_entrez_date":"2005-07-01","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"UniProtKB:Q6IUU5","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC30D10.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15182371","title":"Mediator is required for activated transcription in a Schizosaccharomyces pombe in vitro system.","citation":"Eur J Biochem 2004 Jun;271(12):2561-72","abstract":"RNA polymerase II (RNAPII) requires a set of general transcription factors - TFIIA, TFIIB, TFIID, TFIIE, TFIIF and TFIIH - to initiate transcription from a gene promoter in vitro. General transcription factors have been isolated from Saccharomyces cerevisiae, rat, human and Drosophila, and their corresponding cDNAs have been cloned. In this report, we describe a reconstituted in vitro transcription system that consists of the following preparations of factors from the yeast Schizosaccharomyces pombe: affinity-purified RNAPII, TFIIH, and recombinant TBP, TFIIB, TFIIE and TFIIF. We show that this system can support basal transcription from the adenovirus major late promoter when purified RNAPII is used and activated transcription when the RNAPII holoenzyme (RNAPII plus the Mediator proteins) is included in the reaction. In contrast, the TATA binding protein-associated factors had no effect on transcriptional activation in our Sc. pombe system. These results indicate that Sc. pombe uses the same set of general transcription factors as other eukaryotes and that the Mediator is involved in activated transcription.","authors":"Tamayo E, Bernal G, Teno U, Maldonado E","authors_abbrev":"Tamayo E et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-06-09","publication_year":"2004","canto_session_key":"98038c26b79df7dc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-06-21 08:40:50","canto_approved_date":"2024-03-25 12:52:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-20 19:21:50","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":48,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1682.07","SPAC17A5.06","SPBC31F10.04c","SPAC23G3.01","SPBC1198.13c","SPAC16E8.11c","SPAC29A4.07","SPBC21.04","SPAC16E8.16","SPAC1B3.12c","SPAC29E6.08","SPCC1450.05c","SPBC28F2.12","SPBC1A4.10c","SPBC13G1.13","SPAC458.07","SPACUNK4.06c","SPBC19F8.07","SPBC14F5.08","SPCC1672.08c","SPAC23C4.15","SPCC1620.09c","SPCC1442.10c","SPAC3A12.07"],"gene_count":24,"ltp_gene_count":24,"approved_date":"2023-06-21"},{"uniquename":"PMID:10077189","title":"Analysis of TFIIH subunit through isolation of the gene from Schizosaccharomyces pombe corresponding to that of Saccharomyces cerevisiae SSL1, reveals the presence of conserved structural motifs.","citation":"Yeast 1999 Feb;15(3):255-62","abstract":"We isolated a Schizosaccharomyces pombe (Sz. pombe) gene encoding the counterpart of the TFIIH subunit Homo sapiens (H. sapiens) p44 and Saccharomyces cerevisiae (S. cerevisiae) SSL1, and we named this gene product p47. Contrary to the case of SSL1, which is an essential gene of S. cerevisiae, p47 is not essential for the viability of Sz. pombe. The deduced amino acid sequence revealed that this TFIIH subunit is highly conserved during evolution. Comparison of the primary structures revealed differences in the predicted positions of introns in the Caenorhabditis elegans (C. elegans) gene encoding the p47 counterpart found during the genome project. A charged cluster in the N-terminal region is present in the two yeasts. Two putative zinc-binding motifs, an extended C2H2 zinc finger with a 'C8 motif' and a second putative zinc-binding motif common to the two TFIIH subunits, were also found, the former being completely conserved. The latter motif consists of five cysteine residues and is also present in hp44, SSL1 and another TFIIH subunit, human p34 (hp34). Since one zinc atom can bind to four ligands in zinc-binding motifs, the conservation of cysteine residues was given attention. This motif is completely conserved in p47 homologues derived from the four species. As one cysteine residue is not conserved among the homologues of hp34, the consensus of this motif is concluded to be Cys X2-Cys-X(10,12)-Cys-X2-Cys. This nucleotide sequence has been deposited in the GenBank Data Library under Accession Number AF017646.","authors":"Adachi N, Matsumoto M, Hasegawa S, Yamamoto T, Horikoshi M","authors_abbrev":"Adachi N et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-03-17","publication_year":"1999","canto_session_key":"cb68789bf4938e57","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-09-11 16:46:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 16:37:21","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1682.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-11"},{"uniquename":"PMID:33108274","title":"The  wtf4  meiotic driver utilizes controlled protein aggregation to generate selective cell death.","citation":"Elife 2020 Oct 27;9","abstract":"Meiotic drivers are parasitic loci that force their own transmission into greater than half of the offspring of a heterozygote. Many drivers have been identified, but their molecular mechanisms are largely unknown. The  wtf4  gene is a meiotic driver in  Schizosaccharomyces pombe  that uses a poison-antidote mechanism to selectively kill meiotic products (spores) that do not inherit  wtf4 . Here, we show that the Wtf4 proteins can function outside of gametogenesis and in a distantly related species,  Saccharomyces cerevisiae . The Wtf4 poison  protein forms dispersed, toxic aggregates. The Wtf4 antidote  can co-assemble with the Wtf4 poison  and promote its trafficking to vacuoles. We show that neutralization of the Wtf4 poison  requires both co-assembly with the Wtf4 antidote  and aggregate trafficking, as mutations that disrupt either of these processes result in cell death in the presence of the Wtf4 proteins. This work reveals that  wtf  parasites can exploit protein aggregate management pathways to selectively destroy spores.","doi":"10.7554/eLife.55694","authors":"Nuckolls NL, Mok AC, Lange JJ, Yi K, Kandola TS, Hunn AM, McCroskey S, Snyder JL, Bravo Núñez MA, McClain M, McKinney SA, Wood C, Halfmann R, Zanders SE","authors_abbrev":"Nuckolls NL et al.","pubmed_publication_date":"27 Oct 2020","pubmed_entrez_date":"2020-10-27","publication_year":"2020","canto_session_key":"1bc3fe03ff243df2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Zanders","canto_first_approved_date":"2021-05-04 13:25:02","canto_approved_date":"2025-09-03 10:56:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-27 16:37:40","canto_added_date":"2020-10-29 01:15:05","annotation_curators":[{"name":"Sarah Zanders","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC548.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-05-04"},{"uniquename":"PMID:16940176","title":"Molecular architecture of a eukaryotic DNA replication terminus-terminator protein complex.","citation":"Mol Cell Biol 2006 Nov;26(21):8061-74","abstract":"DNA replication forks pause at programmed fork barriers within nontranscribed regions of the ribosomal DNA (rDNA) genes of many eukaryotes to coordinate and regulate replication, transcription, and recombination. The mechanism of eukaryotic fork arrest remains unknown. In Schizosaccharomyces pombe, the promiscuous DNA binding protein Sap1 not only causes polar fork arrest at the rDNA fork barrier Ter1 but also regulates mat1 imprinting at SAS1 without fork pausing. Towards an understanding of eukaryotic fork arrest, we probed the interactions of Sap1 with Ter1 as contrasted with SAS1. The Sap1 dimer bound Ter1 with high affinity at one face of the DNA, contacting successive major grooves. The complex displayed translational symmetry. In contrast, Sap1 subunits approached SAS1 from opposite helical faces, forming a low-affinity complex with mirror image rotational symmetry. The alternate symmetries were reflected in distinct Sap1-induced helical distortions. Importantly, modulating protein-DNA interactions of the fork-proximal Sap1 subunit with the nonnatural binding site DR2 affected blocking efficiency without changes in binding affinity or binding mode but with alterations in Sap1-induced DNA distortion. The results reveal that Sap1-DNA affinity alone is insufficient to account for fork arrest and suggest that Sap1 binding-induced structural changes may result in formation of a competent fork-blocking complex.","authors":"Krings G, Bastia D","authors_abbrev":"Krings G et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-08-31","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18265095","title":"Preparation of yeast DNA.","citation":"Curr Protoc Mol Biol 2001 May;Chapter 13:Unit13.11","abstract":"Molecular studies in yeast often require the isolation of both plasmid and chromosomal yeast DNA. Plasmid DNA is used in the transformation of E. coli, whereas chromosomal DNA is used for Southern hybridization analysis, in vitro amplification by the polymerase chain reaction (PCR), or cloning of integrated plasmids. This unit presents two variations of the \"smash and grab\" protocol that produce suitable DNA for all these applications. These protocols work for both Saccharomyces cerevisiae and Schizosaccharomyces pombe.","doi":"10.1002/0471142727.mb1311s39","authors":"Hoffman CS","authors_abbrev":"Hoffman CS","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2008-02-12","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15302919","title":"Genetic and biochemical analyses of Pfh1 DNA helicase function in fission yeast.","citation":"Nucleic Acids Res 2004;32(14):4205-16","abstract":"The Schizosaccharomyces pombe pfh1+ gene (PIF1 homolog) encodes an essential enzyme that has both DNA helicase and ATPase activities and is implicated in lagging strand DNA processing. Mutations in the pfh1+ gene suppress a temperature-sensitive allele of cdc24+, which encodes a protein that functions with Schizosaccharomyces pombe Dna2 in Okazaki fragment processing. In this study, we describe the enzymatic properties of the Pfh1 helicase and the genetic interactions between pfh1 and cdc24, dna2, cdc27 or pol 3, all of which are involved in the Okazaki fragment metabolism. We show that a full-length Pfh1 fusion protein is active as a monomer. The helicase activity of Pfh1 displaced only short (<30 bp) duplex DNA regions efficiently in a highly distributive manner and was markedly stimulated by the presence of a replication-fork-like structure in the substrate. The temperature-sensitive phenotype of a dna2-C2 or a cdc24-M38 mutant was suppressed by pfh1-R20 (a cold-sensitive mutant allele of pfh1) and overexpression of wild-type pfh1+ abolished the ability of the pfh1 mutant alleles to suppress dna2-C2 and cdc24-M38. Purified Pfh1-R20 mutant protein displayed significantly reduced ATPase and helicase activities. These results indicate that the simultaneous loss-of-function mutations of pfh1+ and dna2+ (or cdc24+) are essential to restore the growth defect. Our genetic data indicate that the Pfh1 DNA helicase acts in concert with Cdc24 and Dna2 to process single-stranded DNA flaps generated in vivo by pol -mediated lagging strand displacement DNA synthesis.","authors":"Ryu GH, Tanaka H, Kim DH, Kim JH, Bae SH, Kwon YN, Rhee JS, MacNeill SA, Seo YS","authors_abbrev":"Ryu GH et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-08-11","publication_year":"2004","canto_session_key":"b4c0aef96ec456f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-09-19 12:37:58","canto_approved_date":"2021-06-16 14:25:55","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-19 12:37:38","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.04","SPBC16D10.04c","SPBC1734.02c","SPBC887.14c","SPAC8F11.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-09-19"},{"uniquename":"PMID:1515677","title":"A low copy number central sequence with strict symmetry and unusual chromatin structure in fission yeast centromere.","citation":"Mol Biol Cell 1992 Jul;3(7):819-35","abstract":"Fission yeast centromeres vary in size but are organized in a similar fashion. Each consists of two distinct domains, namely, the approximately 15-kilobase (kb) central region (cnt+imr), containing chromosome-specific low copy number sequences, and 20- to 100-kb outer surrounding sequences (otr) with highly repetitive motifs common to all centromeres. The central region consists of an inner asymmetric sequence flanked by inverted repeats that exhibit strict identity with each other. Nucleotide changes in the left repeat are always accompanied with the same changes in the right. The chromatin structure of the central region is unusual. A nucleosomal nuclease digestion pattern formed on unstable plasmids but not on stable chromosome. DNase I hypersensitive sites correlate with the location of tRNA genes in the central region. Autonomously replicating sequences are also present in the central region. The behavior of truncated minichromosomes suggested that the central region is essential, but not sufficient, to confer transmission stability. A portion of the outer repetitive region is also required. A larger outer region is necessary to ensure correct meiotic behavior. Fluorescence in situ hybridization identified individual cens. In the interphase, they cluster near the nuclear periphery. The central sequence (cnt+imr) may play a role in positioning individual chromosomes within the nucleus, whereas the outer regions (otr) may interact with each other to form the higher-order complex structure.","authors":"Takahashi K, Murakami S, Chikashige Y, Funabiki H, Niwa O, Yanagida M","authors_abbrev":"Takahashi K et al.","pubmed_publication_date":"Jul 1992","pubmed_entrez_date":"1992-07-01","publication_year":"1992","canto_session_key":"a449933b39c46f9e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-02 13:44:53","canto_approved_date":"2019-01-02 13:44:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 21:52:04","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-02"},{"uniquename":"PMID:26727711","title":"A nucleoporin that facilitates meiotic kinetochore reorganization.","citation":"Cell Cycle 2016;15(3):307-8","abstract":"","doi":"10.1080/15384101.2015.1125237","authors":"Yang HJ, Haraguchi T, Hiraoka Y","authors_abbrev":"Yang HJ et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-01-05","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-12-17 01:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16096637","title":"Fission yeast MO25 protein is localized at SPB and septum and is essential for cell morphogenesis.","citation":"EMBO J 2005 Sep 07;24(17):3012-25","abstract":"Cell morphogenesis is of fundamental significance in all eukaryotes for development, differentiation, and cell proliferation. In fission yeast, Drosophila Furry-like Mor2 plays an essential role in cell morphogenesis in concert with the NDR/Tricornered kinase Orb6. Mutations of these genes result in the loss of cell polarity. Here we show that the conserved proteins, MO25-like Pmo25, GC kinase Nak1, Mor2, and Orb6, constitute a morphogenesis network that is important for polarity control and cell separation. Intriguingly, Pmo25 was localized at the mitotic spindle pole bodies (SPBs) and then underwent translocation to the dividing medial region upon cytokinesis. Pmo25 formed a complex with Nak1 and was required for both the localization and kinase activity of Nak1. Pmo25 and Nak1 in turn were essential for Orb6 kinase activity. Further, the Pmo25 localization at the SPBs and the Nak1-Orb6 kinase activities during interphase were under the control of the Cdc7 and Sid1 kinases in the septation initiation network (SIN), suggesting a functional linkage between SIN and the network for cell morphogenesis/separation following cytokinesis.","authors":"Kanai M, Kume K, Miyahara K, Sakai K, Nakamura K, Leonhard K, Wiley DJ, Verde F, Toda T, Hirata D","authors_abbrev":"Kanai M et al.","pubmed_publication_date":"07 Sep 2005","pubmed_entrez_date":"2005-08-13","publication_year":"2005","canto_session_key":"c22f209fe76ffcd8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-06-28 12:27:22","canto_approved_date":"2026-01-30 15:36:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 13:27:18","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":57,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_16096637_phaf.tsv"}],"genes":["SPBC21.06c","SPAC6F6.08c","SPBP19A11.04c","SPAC1834.06c","SPBC17F3.02","SPBC336.12c","SPAC9G1.09","SPAC24H6.05","SPCC417.07c","SPAC821.12","SPBC19G7.05c","SPAC24B11.11c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2017-06-28"},{"uniquename":"PMID:10669867","title":"Sequence analysis of two cosmids from the right arm of the Schizosaccharomyces pombe chromosome II.","citation":"Yeast 2000 Mar 15;16(4):299-306","abstract":"We report the complete sequence of two cosmids, SPBC19C7 (34815 bp insert, Accession No. AL023859) and SPBC15D4 (33203 bp insert, Accession No. AL031349), localized on chromosome II of the S. pombe genome. Twelve open reading frames (ORFs) were identified in SPBC19C7 and 16 in SPBC5D4. Two known genes were found on each cosmid: cyr1 and uve1 on SPBC19C7, encoding adenylate cyclase and a UV-endonuclease, respectively, and gpt and pho2 on SPBC15D4, encoding an N-acetylglucosamine-1-phosphate transferase and a4-nitrophenylphosphatase, respectively. Five ORFs similar to known proteins were found on SPBC19C7, and six on SPBC15D4. They include putative genes for a ubiquitin protein ligase, a prolyl-tRNA synthetase, a tRNA splicing endonuclease, a voltage-gated chloride channel, a mannosyl transferase, a kinesin-like protein, a histone transcriptional regulator, an N-acetyltransferase, a cystathionine gamma-synthase and a TFIID subunit. Two ORF products of SPBC15D4 do not have clear homologues: one encodes a putative transcriptional regulator with a binuclear zinc domain and the other a protein with six transmembrane domains. Two ORFs from SPBC15D4 are similar to unknown ORFs, one from Saccharomyces cerevisiae and the other from Caenorhabditis elegans. Finally, two ORFs of SPBC19C7 and six of SPBC15D4 correspond to orphan genes. The frequent occurrence of introns and the short and degenerated intron-exon boundaries consensus sequences significantly complicated ORF predictions. Two potential ORF-free regions spanning several kb were predicted, and a clustering of ORFs transcribed in the same orientation was observed.","authors":"Lucas M, Lyne M, Lepingle A, Rochet M, Gaillardin C","authors_abbrev":"Lucas M et al.","pubmed_publication_date":"15 Mar 2000","pubmed_entrez_date":"2000-02-12","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18410286","title":"The beta-1,3-glucanosyltransferase gas4p is essential for ascospore wall maturation and spore viability in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2008 Jun;68(5):1283-99","abstract":"Meiosis is the developmental programme by which sexually reproducing diploid organisms generate haploid gametes. In yeast, meiosis is followed by spore morphogenesis. The formation of the Schizosaccharomyces pombe ascospore wall requires the co-ordinated activity of enzymes involved in the biosynthesis and modification of its components, such as glucans. During sporogenesis, the beta-1,3-glucan synthase bgs2p synthesizes linear beta-1,3-glucans, which remain unorganized and alkali-soluble until covalent linkages are set up between beta-1,3-glucans and other cell wall components. Several proteins belonging to the glycoside hydrolase family 72 (GH72) with beta-1,3-glucanosyltransferase activity have been described in other organisms, such as the Saccharomyces cerevisiae Gas1p or the Aspergillus fumigatus Gel1p. Here we describe the characterization of gas4(+), a new gene that encodes a protein of the GH72 family. Deletion of this gene does not lead to any apparent defect during vegetative growth, but homozygous gas4Delta diploids show a sporulation defect. Although meiosis occurs normally, ascospores are unable to mature or to germinate. The expression of gas4(+) is strongly induced during sporulation and a yellow fluorescent protein (YFP)-gas4p fusion protein localizes to the ascospore periphery during sporulation. We conclude that gas4p is required for ascospore maturation in S. pombe.","doi":"10.1111/j.1365-2958.2008.06233.x","authors":"de Medina-Redondo M, Arnáiz-Pita Y, Fontaine T, Del Rey F, Latgé JP, Vázquez de Aldana CR","authors_abbrev":"de Medina-Redondo M et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-16","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC342.03"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:9885154","title":"Fusion of a fission yeast.","citation":"Yeast 1998 Dec;14(16):1529-66","abstract":"","authors":"Davey J","authors_abbrev":"Davey J","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1999-01-13","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8590474","title":"Growth of a mutant defective in a putative phosphoinositide-specific phospholipase C of Schizosaccharomyces pombe is restored by low concentrations of phosphate and inositol.","citation":"Curr Genet 1995 Jul;28(2):199-203","abstract":"A mutant (plc1-1) of Schizosaccharomyces pombe unable to grow on a minimal medium containing high amounts of phosphate was selected. On yeast-extract agar its growth is temperature sensitive. Tests in liquid synthetic medium show that growth of the mutant is partially restored by lowering the phosphate and inositol concentrations in the growth medium. The growth defect is fully suppressed by a plasmid encoding a putative protein having the structural features of phosphoinositide-specific phospholipases C (PI-PLC). This protein, of 899 amino-acids, contains the characteristic X and Y domains found in all PI-PLCs of higher and lower eucaryotes and reveals, in addition, an EF-hand motif (putative Ca(2+)-binding site). Like the corresponding enzyme from Saccharomyces cerevisiae, the S. pombe PI-PLC is most similar to the delta form of PI-PLC isoenzymes. The cloned gene integrates at the plc1 site indicating that plc1 codes for a putative PI-PLC. Plc1 physically maps on the left arm of chromosome II between rad11 and mei3.","authors":"Fankhauser H, Schweingruber AM, Edenharter E, Schweingruber ME","authors_abbrev":"Fankhauser H et al.","pubmed_publication_date":"Jul 1995","pubmed_entrez_date":"1995-07-01","publication_year":"1995","canto_session_key":"bb591d5e45b99277","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-22 08:08:12","canto_approved_date":"2022-09-22 08:08:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-18 08:53:48","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F8.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-09-22"},{"uniquename":"PMID:31980821","title":"Nuclear envelope attachment of telomeres limits TERRA and telomeric rearrangements in quiescent fission yeast cells.","citation":"Nucleic Acids Res 2020 Apr 06;48(6):3029-3041","abstract":"Telomere anchoring to nuclear envelope (NE) is a key feature of nuclear genome architecture. Peripheral localization of telomeres is important for chromatin silencing, telomere replication and for the control of inappropriate recombination. Here, we report that fission yeast quiescent cells harbor predominantly a single telomeric cluster anchored to the NE. Telomere cluster association to the NE relies on Rap1-Bqt4 interaction, which is impacted by the length of telomeric sequences. In quiescent cells, reducing telomere length or deleting bqt4, both result in an increase in transcription of the telomeric repeat-containing RNA (TERRA). In the absence of Bqt4, telomere shortening leads to deep increase in TERRA level and the concomitant formation of subtelomeric rearrangements (STEEx) that accumulate massively in quiescent cells. Taken together, our data demonstrate that Rap1-Bqt4-dependent telomere association to NE preserves telomere integrity in post-mitotic cells, preventing telomeric transcription and recombination. This defines the nuclear periphery as an area where recombination is restricted, creating a safe zone for telomeres of post-mitotic cells.","doi":"10.1093/nar/gkaa043","authors":"Maestroni L, Reyes C, Vaurs M, Gachet Y, Tournier S, Géli V, Coulon S","authors_abbrev":"Maestroni L et al.","pubmed_publication_date":"06 Apr 2020","pubmed_entrez_date":"2020-01-26","publication_year":"2020","canto_session_key":"f0915212069f1a84","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Stéphane COULON","canto_first_approved_date":"2020-07-07 14:30:38","canto_approved_date":"2021-03-08 17:47:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-12 06:31:27","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"Stéphane COULON","community_curator":true,"annotation_count":6,"orcid":"0000-0001-8090-914X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.10","SPNCRNA.214","SPBC1778.02","SPAC12G12.13c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2020-07-07"},{"uniquename":"PMID:18525239","title":"Fission yeast-based screening to identify putative HDAC inhibitors using a telomeric reporter strain.","citation":"Mol Cells 2008 Jul 31;26(1):93-9","abstract":"Transcriptional silencing is regulated by promoter methylation and histone modifications such as methylation and acetylation. We constructed a Schizosaccaromyces pombe reporter strain, KCT120a, to identify modifiers of transcriptional silencing, by inserting the ura4(+) gene into a heterochromatic telomere region. Two compounds inhibited the activity of histone deacetylases, induced acetylation of histone H3 and caused apoptotic cell death in HeLa cells. Expression of gelsolin and p21(waf1/cip1) also increased, as it does in response to HDAC inhibitors such as TSA. Therefore, these compounds appear to be potent inhibitors of HDACs, and hence potential anti-cancer drugs. Our observations suggest that a yeast cell-based assay system for transcriptional silencing may be useful for identifying histone deacetylase inhibitors and other agents affecting chromatin remodeling.","authors":"Chung KS, Ahn J, Choi CH, Yim NH, Kang CM, Kim CH, Lee K, Park HM, Song KB, Won M","authors_abbrev":"Chung KS et al.","pubmed_publication_date":"31 Jul 2008","pubmed_entrez_date":"2008-06-06","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11950932","title":"The spindle pole body protein Cdc11p links Sid4p to the fission yeast septation initiation network.","citation":"Mol Biol Cell 2002 Apr;13(4):1203-14","abstract":"The Schizosaccharomyces pombe septation initiation network (SIN) signals the onset of cell division from the spindle pole body (SPB) and is regulated by the small GTPase Spg1p. The localization of SIN components including Spg1p to the SPB is required for cytokinesis and is dependent on Sid4p, a constitutive resident of SPBs. However, a direct interaction between Sid4p and other members of the SIN has not been detected. To understand how Sid4p is linked to other SIN components, we have begun to characterize an S. pombe homolog of the Saccharomyces cerevisiae SPB protein Nud1p. We have determined that this S. pombe Nud1p homolog corresponds to Cdc11p, a previously uncharacterized SIN element. We report that Cdc11p is present constitutively at SPBs and that its function appears to be required for the localization of all other SIN components to SPBs with the exception of Sid4p. The Cdc11p C terminus localizes the protein to SPBs in a Sid4p-dependent manner, and we demonstrate a direct Cdc11p-Sid4p interaction. The N-terminus of Cdc11p is required for Spg1p binding to SPBs. Our studies indicate that Cdc11p provides a physical link between Sid4p and the Spg1p signaling pathway.","authors":"Tomlin GC, Morrell JL, Gould KL","authors_abbrev":"Tomlin GC et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-16","publication_year":"2002","canto_session_key":"0b586801d9eddd09","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-12-15 12:42:12","canto_approved_date":"2023-12-20 10:18:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-06 05:09:26","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPAC1565.06c","SPAC6F6.08c","SPCC1739.11c","SPAC24B11.11c","SPBC21.06c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2023-12-15"},{"uniquename":"PMID:885876","title":"Properties of a mitochondrial suppressor mutation restoring oxidative phosphorylation in a nuclear mutant of the yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1977 Aug 25;252(16):5716-23","abstract":"","authors":"Labaille F, Colson AM, Petit L, Goffeau A","authors_abbrev":"Labaille F et al.","pubmed_publication_date":"25 Aug 1977","pubmed_entrez_date":"1977-08-25","publication_year":"1977","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4315977","title":"Phosphatidic acid and phosphatidylinositol metabolism in Schizosaccharomyces pombe.","citation":"Biochem J 1970 Apr;117(2):203-13","abstract":"The phospholipid composition of Schizosaccharomyces pombe was not markedly affected by changes in the phosphate concentration of the medium or phase of growth. The major fatty acids in the total lipid extract and purified phosphatidylinositol were palmitic acid and oleic acid. Phosphatidic acid was synthesized by acylation of l-3-glycerophosphate in Schiz. pombe and phosphatidate phosphohydrolase was present. Phosphatidylinositol synthesis from inositol occurred in the absence of CDP-diglyceride. Even with dialysed cell-free preparations, the inositol lipid was synthesized by an apparently energy-independent route, at rates greater than would be required during cell growth. Phosphatidylinositol appeared to be broken down by a phospholipase D. All the enzymes examined were particulate; similar activities were found in Saccharomyces cerevisiae.","authors":"White GL, Hawthorne JN","authors_abbrev":"White GL et al.","pubmed_publication_date":"Apr 1970","pubmed_entrez_date":"1970-04-01","publication_year":"1970","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10660979","title":"Recognition for fission yeast.","citation":"Trends Cell Biol 2000 Feb;10(2):81-2","abstract":"","authors":"Millar J","authors_abbrev":"Millar J","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-02-08","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4110142","title":"Isolation of temperature-sensitive mutants of Schizosaccharomyces pombe.","citation":"J Bacteriol 1972 Feb;109(2):484-91","abstract":"Seventy-one mutants of the yeast Schizosaccharomyces pombe that were able to grow on complete medium at 25 C but not at 37 C were isolated. Strains selected for further study showed: (i) single gene mutation and (ii) cell lengthening at the restrictive temperature. Preliminary characterization of 13 mutants is reported. Seven of them have a less pronounced synthesis of deoxyribonucleic acid at the restrictive temperature, and four of them seem to be affected in cell division.","authors":"Bonatti S, Simili M, Abbondandolo A","authors_abbrev":"Bonatti S et al.","pubmed_publication_date":"Feb 1972","pubmed_entrez_date":"1972-02-01","publication_year":"1972","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27737959","title":"Mutations in genes encoding condensin complex proteins cause microcephaly through decatenation failure at mitosis.","citation":"Genes Dev 2016 Oct 01;30(19):2158-2172","abstract":"Compaction of chromosomes is essential for accurate segregation of the genome during mitosis. In vertebrates, two condensin complexes ensure timely chromosome condensation, sister chromatid disentanglement, and maintenance of mitotic chromosome structure. Here, we report that biallelic mutations in NCAPD2, NCAPH, or NCAPD3, encoding subunits of these complexes, cause microcephaly. In addition, hypomorphic Ncaph2 mice have significantly reduced brain size, with frequent anaphase chromatin bridge formation observed in apical neural progenitors during neurogenesis. Such DNA bridges also arise in condensin-deficient patient cells, where they are the consequence of failed sister chromatid disentanglement during chromosome compaction. This results in chromosome segregation errors, leading to micronucleus formation and increased aneuploidy in daughter cells. These findings establish \"condensinopathies\" as microcephalic disorders, with decatenation failure as an additional disease mechanism for microcephaly, implicating mitotic chromosome condensation as a key process ensuring mammalian cerebral cortex size.","authors":"Martin CA, Murray JE, Carroll P, Leitch A, Mackenzie KJ, Halachev M, Fetit AE, Keith C, Bicknell LS, Fluteau A, Gautier P, Hall EA, Joss S, Soares G, Silva J, Bober MB, Duker A, Wise CA, Quigley AJ, Phadke SR, Deciphering Developmental Disorders Study, Wood AJ, Vagnarelli P, Jackson AP","authors_abbrev":"Martin CA et al.","pubmed_publication_date":"01 Oct 2016","pubmed_entrez_date":"2016-10-15","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC306.03c","SPBC776.13"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:24450973","title":"Pathogenesis and management of Wilson disease.","citation":"Hepatol Res 2014 Apr;44(4):395-402","abstract":"Hepatolenticular degeneration, commonly known as Wilson disease, is an autosomal recessive inherited disease of abnormal copper metabolism, characterized by the accumulation of copper in the body due to decreased biliary excretion of copper from hepatocytes. Wilson disease protein, ATP7B, functions in copper excretion into bile and in copper secretion to the bloodstream coupled with ceruloplasmin synthesis. Various kinds of mutations of ATP7B cause Wilson disease. Wilson disease is a rare genetic disease that can be treated pharmacologically. Recognition and prompt diagnosis are very important, because Wilson disease is fatal if left untreated. In this review, I summarize the pathogenesis and management of Wilson disease.","doi":"10.1111/hepr.12301","authors":"Harada M","authors_abbrev":"Harada M","pubmed_publication_date":"Apr 2014","pubmed_entrez_date":"2014-01-24","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:20:22","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11948160","title":"Identification of [2Fe-2S] clusters in microbial ferrochelatases.","citation":"J Bacteriol 2002 May;184(9):2460-4","abstract":"The terminal enzyme of heme biosynthesis, ferrochelatase (EC 4.99.1.1), catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme. Prior to the present work, [2Fe-2S] clusters have been identified and characterized in animal ferrochelatases but not in plant or prokaryotic ferrochelatases. Herein we present evidence that ferrochelatases from the bacteria Caulobacter crescentus and Mycobacterium tuberculosis possess [2Fe-2S] clusters. The enzyme from C. crescentus is a homodimeric, membrane-associated protein while the enzyme from M. tuberculosis is monomeric and soluble. The clusters of the C. crescentus and M. tuberculosis ferrochelatases are ligated by four cysteines but possess ligand spacings that are unlike those of any previously characterized [2Fe-2S] cluster-containing protein, including the ferrochelatase of the yeast Schizosaccharomyces pombe. Thus, the microbial ferrochelatases represent a new group of [2Fe-2S] cluster-containing proteins.","authors":"Dailey TA, Dailey HA","authors_abbrev":"Dailey TA et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-04-12","publication_year":"2002","canto_session_key":"a39d114fa4eca923","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-05-17 08:36:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-05-16 08:55:35","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-05-16"},{"uniquename":"PMID:2046669","title":"byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype.","citation":"Mol Cell Biol 1991 Jul;11(7):3554-63","abstract":"Schizosaccharomyces pombe contains a single gene, ras1, which is a homolog of the mammalian RAS genes. ras1 is required for conjugation, sporulation, and normal cell shape. ras1 has been previously identified as ste5. We report here a gene we call byr2 that can encode a predicted protein kinase and can partially suppress defects in ras1 mutants. ras1 mutant strains expressing high levels of byr2 can sporulate competently but are still defective in conjugation and abnormally round. byr2 mutants are viable and have normal shape but are absolutely defective in conjugation and sporulation. byr2 is probably identical to ste8. In many respects, byr2 resembles the byr1 gene, another suppressor of the ras1 mutation, which has been identified previously as ste1. Our data indicate that if ras1, byr2, and byr1 act along the same pathway, then the site of action for byr2 is between the sites for ras1 and byr1.","authors":"Wang Y, Xu HP, Riggs M, Rodgers L, Wigler M","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_session_key":"803cfb382ebb41c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-09 09:18:56","canto_approved_date":"2024-04-03 11:59:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 08:28:54","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC1D7.05","SPAC1D4.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-06-09"},{"uniquename":"PMID:18057023","title":"Regulation of gene expression during M-G1-phase in fission yeast through Plo1p and forkhead transcription factors.","citation":"J Cell Sci 2008 Jan 01;121(Pt 1):38-47","abstract":"In fission yeast the expression of several genes during M-G1 phase is controlled by binding of the PCB binding factor (PBF) transcription factor complex to Pombe cell cycle box (PCB) promoter motifs. Three components of PBF have been identified, including two forkhead-like proteins Sep1p and Fkh2p, and a MADS-box-like protein, Mbx1p. Here, we examine how PBF is controlled and reveal a role for the Polo kinase Plo1p. plo1(+) shows genetic interactions with sep1(+), fkh2(+) and mbx1(+), and overexpression of a kinase-domain mutant of plo1 abolishes M-G1-phase transcription. Plo1p binds to and directly phosphorylates Mbx1p, the first time a Polo kinase has been shown to phosphorylate a MADS box protein in any organism. Fkh2p and Sep1p interact in vivo and in vitro, and Fkh2p, Sep1p and Plo1p contact PCB promoters in vivo. However, strikingly, both Fkh2p and Plo1p bind to PCB promoters only when PCB-controlled genes are not expressed during S- and G2-phase, whereas by contrast Sep1p contacts PCBs coincident with M-G1-phase transcription. Thus, Plo1p, Fkh2p and Sep1p control M-G1-phase gene transcription through a combination of phosphorylation and cell-cycle-specific DNA binding to PCBs.","authors":"Papadopoulou K, Ng SS, Ohkura H, Geymonat M, Sedgwick SG, McInerny CJ","authors_abbrev":"Papadopoulou K et al.","pubmed_publication_date":"01 Jan 2008","pubmed_entrez_date":"2007-12-07","publication_year":"2008","canto_session_key":"e73fcd0460d8dc7f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-22 14:43:32","canto_approved_date":"2024-04-22 14:43:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-12 16:25:14","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":42,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPBC4.04c","SPAC19E9.02","SPBC16G5.15c","SPBC19G7.06","SPAC23C11.16","SPAC1B9.02c","SPCC4B3.15","SPAC20G8.05c","SPBC4C3.12","SPAC24B11.11c","SPAC1F7.05","SPAC3F10.15c"],"gene_count":13,"ltp_gene_count":5,"approved_date":"2024-04-22"},{"uniquename":"PMID:27466270","title":"Php4 Is a Key Player for Iron Economy in Meiotic and Sporulating Cells.","citation":"G3 (Bethesda) 2016 Oct 13;6(10):3077-3095","abstract":"Meiosis is essential for sexually reproducing organisms, including the fission yeast Schizosaccharomyces pombe In meiosis, chromosomes replicate once in a diploid precursor cell (zygote), and then segregate twice to generate four haploid meiotic products, named spores in yeast. In S. pombe, Php4 is responsible for the transcriptional repression capability of the heteromeric CCAAT-binding factor to negatively regulate genes encoding iron-using proteins under low-iron conditions. Here, we show that the CCAAT-regulatory subunit Php4 is required for normal progression of meiosis under iron-limiting conditions. Cells lacking Php4 exhibit a meiotic arrest at metaphase I. Microscopic analyses of cells expressing functional GFP-Php4 show that it colocalizes with chromosomal material at every stage of meiosis under low concentrations of iron. In contrast, GFP-Php4 fluorescence signal is lost when cells undergo meiosis under iron-replete conditions. Global gene expression analysis of meiotic cells using DNA microarrays identified 137 genes that are regulated in an iron- and Php4-dependent manner. Among them, 18 genes are expressed exclusively during meiosis and constitute new putative Php4 target genes, which include hry1 +  and mug14 +  Further analysis validates that Php4 is required for maximal and timely repression of hry1 +  and mug14 +  genes. Using a chromatin immunoprecipitation approach, we show that Php4 specifically associates with hry1 +  and mug14 +  promoters in vivo Taken together, the results reveal that in iron-starved meiotic cells, Php4 is essential for completion of the meiotic program since it participates in global gene expression reprogramming to optimize the use of limited available iron.","doi":"10.1534/g3.116.031898","authors":"Brault A, Rallis C, Normant V, Garant JM, Bähler J, Labbé S","authors_abbrev":"Brault A et al.","pubmed_publication_date":"13 Oct 2016","pubmed_entrez_date":"2016-07-29","publication_year":"2016","canto_session_key":"97b8c3d130989993","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-30 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15335873","title":"Mitotic regulation of protein phosphatases by the fission yeast sds22 protein.","citation":"Curr Biol 1993 Jan;3(1):13-26","abstract":"Cell cycle progression requires the activity of protein kinases and phosphatases at critical points in the cell cycle in all eukaryotes. We have previously reported that the dis2(+) and sds2(+) genes of fission yeast encode redundant catalytic subunits of a type 1-like protein phosphatase. The sds22(+) gene was shown to be essential for cell viability and to interact genetically with dis2(+) and sds21(+).\nHere we show by immunoprecipitation that the sds22 protein physically interacts with the dis2 and sds21 proteins, and that sds22-associated phosphatase activity has altered substrate specificity, The loss of sds22 function by a temperature sensitive mutation leads to cell cycle arrest at mid-mitosis, at which point cdc2-dependent histone Hl kinase activity is high while sds22-dependent H1 phosphatase activity is low. To examine the unusual properties of sds22 protein structure, we analyzed a collection of sds22 deletion and point mutants by a variety of functional criteria.\nWe propose that sds22 is a regulatory subunit of the dis2/sds21 phosphatase catalytic subunits and that sds22-bound phosphatase carries a key phosphatase activity essential for the progression from metaphase to anaphase. Mutational analysis indicates that dis2/sds21 interacts with the central repetitive domain of sds22, while the C-terminal and central regions of sds22 may be involved in subcellular targeting and the N-terminus is important for stability.","authors":"Stone EM, Yamano H, Kinoshita N, Yanagida M","authors_abbrev":"Stone EM et al.","pubmed_publication_date":"Jan 1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_session_key":"96a3c95dd4918678","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-09-18 15:51:51","canto_approved_date":"2024-03-28 18:06:50","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-01-15 15:25:25","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC31H12.05c","SPAC4A8.12c","SPBC11B10.09","SPBC776.02c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-09-18"},{"uniquename":"EMBL:AU010251","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1339382","title":"Meiotically induced rec7 and rec8 genes of Schizosaccharomyces pombe.","citation":"Genetics 1992 Sep;132(1):75-85","abstract":"The Schizosaccharomyces pombe rec7 and rec8 genes, which are required for meiotic intragenic recombination but not for mitotic recombination, have been cloned and their DNA sequences determined. Genetic and physical analyses demonstrated that the cloned fragments contained the rec genes rather than rec mutation suppressors. A 1.6-kb DNA fragment contained a functional rec7 gene, and a 2.1-kb fragment contained a functional rec8 gene. The nucleotide sequences of these fragments revealed open reading frames predicting 249 amino acids for the rec7 gene product and 393 amino acids for the rec8 gene product. Northern hybridization analysis showed that both rec gene mRNAs were detectable only at 2-3 hr after induction of meiosis. The absence of these mRNAs in mitosis and their disappearance at 4 hr and later in meiosis suggest that the rec7 and rec8 gene products may be involved primarily in the early steps of meiotic recombination in S. pombe.","authors":"Lin Y, Larson KL, Dorer R, Smith GR","authors_abbrev":"Lin Y et al.","pubmed_publication_date":"Sep 1992","pubmed_entrez_date":"1992-09-01","publication_year":"1992","canto_session_key":"a11e770cdc18b3f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"vw253@cam.ac.uk","canto_approved_date":"2014-07-29 14:09:50","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-08-12 15:38:08","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"vw253@cam.ac.uk","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPCC1753.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-08-12"},{"uniquename":"PMID:31690658","title":"Pat1 activates late steps in mRNA decay by multiple mechanisms.","citation":"Proc Natl Acad Sci U S A 2019 Nov 19;116(47):23512-23517","abstract":"Pat1 is a hub for mRNA metabolism, acting in pre-mRNA splicing, translation repression, and mRNA decay. A critical step in all 5'-3' mRNA decay pathways is removal of the 5' cap structure, which precedes and permits digestion of the RNA body by conserved exonucleases. During bulk 5'-3' decay, the Pat1/Lsm1-7 complex engages mRNA at the 3' end and promotes hydrolysis of the cap structure by Dcp1/Dcp2 at the 5' end through an unknown mechanism. We reconstitute Pat1 with 5' and 3' decay factors and show how it activates multiple steps in late mRNA decay. First, we find that Pat1 stabilizes binding of the Lsm1-7 complex to RNA using two conserved short-linear interaction motifs. Second, Pat1 directly activates decapping by binding elements in the disordered C-terminal extension of Dcp2, alleviating autoinhibition and promoting substrate binding. Our results uncover the molecular mechanism of how separate domains of Pat1 coordinate the assembly and activation of a decapping messenger ribonucleoprotein (mRNP) that promotes 5'-3' mRNA degradation.","doi":"10.1073/pnas.1905455116","authors":"Lobel JH, Tibble RW, Gross JD","authors_abbrev":"Lobel JH et al.","pubmed_publication_date":"19 Nov 2019","pubmed_entrez_date":"2019-11-07","publication_year":"2019","canto_session_key":"58fcf6dcb43d38f2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-04-22 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPAC19A8.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:11168400","title":"Intracellular contents and assembly states of all 12 subunits of the RNA polymerase II in the fission yeast Schizosaccharomyces pombe.","citation":"Eur J Biochem 2001 Feb;268(3):612-9","abstract":"The RNA polymerase II (Pol II) of the fission yeast Schizosaccharomyces pombe is composed of 12 different polypeptides, Rpb1 to Rpb12, of which five, Rpb5, Rpb6, Rpb8, Rpb10 and Rpb12, are shared among three forms of the RNA polymerase. To get an insight into the control of synthesis and assembly of individual subunits, we have measured the intracellular concentrations of all 12 subunits in S. pombe by quantitative immunoblotting. Results indicate that the levels are low for the three large subunits, Rpb1, Rpb2 and Rpb3, which are the homologues of beta', beta and alpha subunits, respectively, of prokaryotic RNA polymerase. On the other hand, the levels of small-sized subunits were between 2- to 15-fold higher than these three core subunits. The levels of the five common subunits shared among RNA polymerases I, II and III are about 10 times greater than those of the Pol II-specific core subunits. The assembly state of the Rpb proteins was analyzed by glycerol gradient centrifugation of S. pombe whole cell extracts. The three core subunits are mostly assembled in Pol II, but some of the small subunits were detected in the slowly sedimenting fractions, indicating that at least some of the excess Rpb proteins exist in unassembled forms. Based on the intracellular concentration of the least abundant Rpb3 subunit, the total number of Pol II in a growing S. pombe cell was estimated to be about 10,000 molecules. The intracellular distribution of some Pol II subunits was also analyzed by microscopic observation of the green fluorescent protein (GFP)-fused Rpb proteins. In agreement with the biochemical analysis, the GFP-Rpb1 and GFP-Rpb3 fusions were present in the nuclei but the GFP-Rpb4 was detected in the cytoplasm as well as the nuclei.","authors":"Kimura M, Sakurai H, Ishihama A","authors_abbrev":"Kimura M et al.","pubmed_publication_date":"Feb 2001","pubmed_entrez_date":"2001-02-13","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1442.10c","SPAC1B3.12c","SPBC14C8.12","SPAC3A12.07","SPACUNK4.06c","SPBC19C2.03","SPBC337.14","SPAC23C4.15","SPAPYUG7.04c","SPBC28F2.12","SPAC23G3.01"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:24853205","title":"A global non-coding RNA system modulates fission yeast protein levels in response to stress.","citation":"Nat Commun 2014 May 23;5:3947","abstract":"Non-coding RNAs (ncRNAs) are frequent and prevalent across the taxa. Although individual non-coding loci have been assigned a function, most are uncharacterized. Their global biological significance is unproven and remains controversial. Here we investigate the role played by ncRNAs in the stress response of Schizosaccharomyces pombe. We integrate global proteomics and RNA sequencing data to identify a systematic programme in which elevated antisense RNA arising both from ncRNAs and from 3'-overlapping convergent gene pairs is directly associated with substantial reductions in protein levels throughout the genome. We describe an extensive array of ncRNAs with trans associations that have the potential to influence multiple pathways. Deletion of one such locus reduces levels of atf1, a transcription factor downstream of the stress-activated mitogen-activated protein kinase (MAPK) pathway, and alters sensitivity to oxidative stress. These non-coding transcripts therefore regulate specific stress responses, adding unanticipated information-processing capacity to the MAPK signalling system.","doi":"10.1038/ncomms4947","authors":"Leong HS, Dawson K, Wirth C, Li Y, Connolly Y, Smith DL, Wilkinson CR, Miller CJ","authors_abbrev":"Leong HS et al.","pubmed_publication_date":"23 May 2014","pubmed_entrez_date":"2014-05-24","publication_year":"2014","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22696216","title":"Sequence determinants of a microtubule tip localization signal (MtLS).","citation":"J Biol Chem 2012 Aug 17;287(34):28227-42","abstract":"Microtubule plus-end-tracking proteins (+TIPs) specifically localize to the growing plus-ends of microtubules to regulate microtubule dynamics and functions. A large group of +TIPs contain a short linear motif, SXIP, which is essential for them to bind to end-binding proteins (EBs) and target microtubule ends. The SXIP sequence site thus acts as a widespread microtubule tip localization signal (MtLS). Here we have analyzed the sequence-function relationship of a canonical MtLS. Using synthetic peptide arrays on membrane supports, we identified the residue preferences at each amino acid position of the SXIP motif and its surrounding sequence with respect to EB binding. We further developed an assay based on fluorescence polarization to assess the mechanism of the EB-SXIP interaction and to correlate EB binding and microtubule tip tracking of MtLS sequences from different +TIPs. Finally, we investigated the role of phosphorylation in regulating the EB-SXIP interaction. Together, our results define the sequence determinants of a canonical MtLS and provide the experimental data for bioinformatics approaches to carry out genome-wide predictions of novel +TIPs in multiple organisms.","doi":"10.1074/jbc.M112.373928","authors":"Buey RM, Sen I, Kortt O, Mohan R, Gfeller D, Veprintsev D, Kretzschmar I, Scheuermann J, Neri D, Zoete V, Michielin O, de Pereda JM, Akhmanova A, Volkmer R, Steinmetz MO","authors_abbrev":"Buey RM et al.","pubmed_publication_date":"17 Aug 2012","pubmed_entrez_date":"2012-06-15","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7859557","title":"The spindle pole body of yeast.","citation":"Chromosoma 1994 Oct;103(6):369-80","abstract":"Microtubule organizing centers play an essential cellular role in nucleating microtubule assembly and establishing the microtubule array. The microtubule organizing center of yeast, the spindle pole body (SPB), shares many functions and properties with those other organisms. In recent years considerable new information has been generated concerning components associated with the SPB, and the mechanism by which it duplicates. This article reviews our current view of the cytology and molecular composition of the SPB of the budding yeast, Saccharomyces cerevisiae, and the fission yeast, Schizosaccharomyces pombe. Genetic studies in these organisms has revealed information about how the SPB duplicates and separates, and its roles during vegetative growth, mating and meiosis.","authors":"Snyder M","authors_abbrev":"Snyder M","pubmed_publication_date":"Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30093689","title":"A single N 1 -methyladenosine on the large ribosomal subunit rRNA impacts locally its structure and the translation of key metabolic enzymes.","citation":"Sci Rep 2018 Aug 09;8(1):11904","abstract":"The entire chemical modification repertoire of yeast ribosomal RNAs and the enzymes responsible for it have recently been identified. Nonetheless, in most cases the precise roles played by these chemical modifications in ribosome structure, function and regulation remain totally unclear. Previously, we demonstrated that yeast Rrp8 methylates m 1 A 645  of 25S rRNA in yeast. Here, using mung bean nuclease protection assays in combination with quantitative RP-HPLC and primer extension, we report that 25S/28S rRNA of S. pombe, C. albicans and humans also contain a single m 1 A methylation in the helix 25.1. We characterized nucleomethylin (NML) as a human homolog of yeast Rrp8 and demonstrate that NML catalyzes the m 1 A 1322  methylation of 28S rRNA in humans. Our in vivo structural probing of 25S rRNA, using both DMS and SHAPE, revealed that the loss of the Rrp8-catalyzed m 1 A modification alters the conformation of domain I of yeast 25S rRNA causing translation initiation defects detectable as halfmers formation, likely because of incompetent loading of 60S on the 43S-preinitiation complex. Quantitative proteomic analysis of the yeast Δrrp8 mutant strain using 2D-DIGE, revealed that loss of m 1 A 645  impacts production of specific set of proteins involved in carbohydrate metabolism, translation and ribosome synthesis. In mouse, NML has been characterized as a metabolic disease-associated gene linked to obesity. Our findings in yeast also point to a role of Rrp8 in primary metabolism. In conclusion, the m 1 A modification is crucial for maintaining an optimal 60S conformation, which in turn is important for regulating the production of key metabolic enzymes.","doi":"10.1038/s41598-018-30383-z","authors":"Sharma S, Hartmann JD, Watzinger P, Klepper A, Peifer C, Kötter P, Lafontaine DLJ, Entian KD","authors_abbrev":"Sharma S et al.","pubmed_publication_date":"09 Aug 2018","pubmed_entrez_date":"2018-08-11","publication_year":"2018","canto_session_key":"5598c8bdf6555b06","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-08-16 22:40:47","canto_approved_date":"2018-08-27 07:10:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-16 22:39:20","canto_added_date":"2018-08-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC56F8.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-08-16"},{"uniquename":"PMID:36435847","title":"Rad52's DNA annealing activity drives template switching associated with restarted DNA replication.","citation":"Nat Commun 2022 Nov 26;13(1):7293","abstract":"It is thought that many of the simple and complex genomic rearrangements associated with congenital diseases and cancers stem from mistakes made during the restart of collapsed replication forks by recombination enzymes. It is hypothesised that this recombination-mediated restart process transitions from a relatively accurate initiation phase to a less accurate elongation phase characterised by extensive template switching between homologous, homeologous and microhomologous DNA sequences. Using an experimental system in fission yeast, where fork collapse is triggered by a site-specific replication barrier, we show that ectopic recombination, associated with the initiation of recombination-dependent replication (RDR), is driven mainly by the Rad51 recombinase, whereas template switching, during the elongation phase of RDR, relies more on DNA annealing by Rad52. This finding provides both evidence and a mechanistic basis for the transition hypothesis.","doi":"10.1038/s41467-022-35060-4","authors":"Kishkevich A, Tamang S, Nguyen MO, Oehler J, Bulmaga E, Andreadis C, Morrow CA, Jalan M, Osman F, Whitby MC","authors_abbrev":"Kishkevich A et al.","pubmed_publication_date":"26 Nov 2022","pubmed_entrez_date":"2022-11-26","publication_year":"2022","canto_session_key":"0ee46fe792f5a85c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-11-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16777962","title":"Mechanism of action of a flavin-containing monooxygenase.","citation":"Proc Natl Acad Sci U S A 2006 Jun 27;103(26):9832-7","abstract":"Elimination of nonnutritional and insoluble compounds is a critical task for any living organism. Flavin-containing monooxygenases (FMOs) attach an oxygen atom to the insoluble nucleophilic compounds to increase solubility and thereby increase excretion. Here we analyze the functional mechanism of FMO from Schizosaccharomyces pombe using the crystal structures of the wild type and protein-cofactor and protein-substrate complexes. The structure of the wild-type FMO revealed that the prosthetic group FAD is an integral part of the protein. FMO needs NADPH as a cofactor in addition to the prosthetic group for its catalytic activity. Structures of the protein-cofactor and protein-substrate complexes provide insights into mechanism of action. We propose that FMOs exist in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, readying them to act on substrates. The 4alpha-hydroperoxyflavin form of the prosthetic group represents a transient intermediate of the monooxygenation process. The oxygenated and reduced forms of the prosthetic group help stabilize interactions with cofactor and substrate alternately to permit continuous enzyme turnover.","authors":"Eswaramoorthy S, Bonanno JB, Burley SK, Swaminathan S","authors_abbrev":"Eswaramoorthy S et al.","pubmed_publication_date":"27 Jun 2006","pubmed_entrez_date":"2006-06-17","publication_year":"2006","canto_session_key":"2be6f24e1afc37d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-20 15:54:16","canto_approved_date":"2023-02-20 15:54:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-20 15:49:13","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP16F5.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-20","pdb_entries":[{"pdb_id":"2gv8","gene_chains":[{"gene_uniquename":"SPBP16F5.08c","chain":"A/B","position":"1-447"}],"title":"Crystal structure of flavin-containing monooxygenase (FMO) from S.pombe and NADPH cofactor complex","entry_authors":"Eswaramoorthy S,Swaminathan S,Burley SK,New York SGX Research Center for Structural Genomics (NYSGXRC)","entry_authors_abbrev":"Eswaramoorthy S et al.","reference_uniquename":"PMID:16777962","experimental_method":"X-ray","resolution":"2.1"},{"pdb_id":"2gvc","gene_chains":[{"gene_uniquename":"SPBP16F5.08c","chain":"A/B/D/E","position":"1-447"}],"title":"Crystal structure of flavin-containing monooxygenase (FMO)from S.pombe and substrate (methimazole) complex","entry_authors":"Eswaramoorthy S,Swaminathan S,Burley SK,New York SGX Research Center for Structural Genomics (NYSGXRC)","entry_authors_abbrev":"Eswaramoorthy S et al.","reference_uniquename":"PMID:16777962","experimental_method":"X-ray","resolution":"2.22"},{"pdb_id":"1vqw","gene_chains":[{"gene_uniquename":"SPBP16F5.08c","chain":"A/B","position":"2-447"}],"title":"Crystal structure of a protein with similarity to flavin-containing monooxygenases and to mammalian dimethylalanine monooxygenases","entry_authors":"Eswaramoorthy S,Swaminathan S,Burley SK,New York SGX Research Center for Structural Genomics (NYSGXRC)","entry_authors_abbrev":"Eswaramoorthy S et al.","reference_uniquename":"PMID:16777962","experimental_method":"X-ray","resolution":"2.4"}]},{"uniquename":"PMID:24526119","title":"Cell-size control: complicated.","citation":"Cell Cycle 2014;13(5):693-4","abstract":"","doi":"10.4161/cc.28088","authors":"Zhu YH, Wu JQ","authors_abbrev":"Zhu YH et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-15","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7982971","title":"mik1+ encodes a tyrosine kinase that phosphorylates p34cdc2 on tyrosine 15.","citation":"J Biol Chem 1994 Dec 02;269(48):30530-7","abstract":"mik1+ and wee1+ function to regulate the tyrosine phosphorylation of p34cdc2 in Schizosaccharomyces pombe (Lundgren, K., Walworth, N., Booher, R., Dembski, M., Kirschner, M., and Beach, D. (1991) Cell 64, 1111-1122). wee1+ encodes a tyrosine kinase that directly phosphorylates p34cdc2 on tyrosine 15, resulting in the inactivation of the cyclin B/p34cdc2 complex. We have overproduced the mik1+ gene product in insect cells and in S. pombe in order to characterize it biochemically. Immunoprecipitates of Mik1 from both sources catalyzed the phosphorylation of p34cdc2 on tyrosine 15 whereas immunoprecipitates of a kinase-deficient mutant of Mik1 were negative in this assay. Mik1 overproduced in insect cells was partially purified by column chromatography, and column fractions were assayed for their ability to phosphorylate p34cdc2 on tyrosine 15. Two major peaks of Mik1 protein were detected by gel filtration chromatography. One peak eluted in the void volume, and a second peak eluted with an apparent molecular mass expected for monomeric Mik1 (approximately 68 kDa). The tyrosine 15 kinase activity co-eluted with the 68 kDa form of Mik1. These results indicate that mik1+ encodes a tyrosine kinase that directly phosphorylates p34cdc2 on tyrosine 15.","authors":"Lee MS, Enoch T, Piwnica-Worms H","authors_abbrev":"Lee MS et al.","pubmed_publication_date":"02 Dec 1994","pubmed_entrez_date":"1994-12-02","publication_year":"1994","canto_session_key":"14b50b1211e9a434","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-28 09:48:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-24 16:05:48","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.14","SPBC11B10.09","SPCC18B5.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-10-24"},{"uniquename":"PMID:21211724","title":"Chromodomain-mediated oligomerization of HP1 suggests a nucleosome-bridging mechanism for heterochromatin assembly.","citation":"Mol Cell 2011 Jan 07;41(1):67-81","abstract":"HP1 proteins are central to the assembly and spread of heterochromatin containing histone H3K9 methylation. The chromodomain (CD) of HP1 proteins specifically recognizes the methyl mark on H3 peptides, but the same extent of specificity is not observed within chromatin. The chromoshadow domain of HP1 proteins promotes homodimerization, but this alone cannot explain heterochromatin spread. Using the S. pombe HP1 protein, Swi6, we show that recognition of H3K9-methylated chromatin in vitro relies on an interface between two CDs. This interaction causes Swi6 to tetramerize on a nucleosome, generating two vacant CD sticky ends. On nucleosomal arrays, methyl mark recognition is highly sensitive to internucleosomal distance, suggesting that the CD sticky ends bridge nearby methylated nucleosomes. Strengthening the CD-CD interaction enhances silencing and heterochromatin spread in vivo. Our findings suggest that recognition of methylated nucleosomes and HP1 spread on chromatin are structurally coupled and imply that methylation and nucleosome arrangement synergistically regulate HP1 function.","doi":"10.1016/j.molcel.2010.12.016","authors":"Canzio D, Chang EY, Shankar S, Kuchenbecker KM, Simon MD, Madhani HD, Narlikar GJ, Al-Sady B","authors_abbrev":"Canzio D et al.","pubmed_publication_date":"07 Jan 2011","pubmed_entrez_date":"2011-01-08","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC8D2.04","SPAC1834.04","SPAC664.01c","SPBC1105.11c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:17266728","title":"Schizosaccharomyces pombe possesses two plasma membrane alkali metal cation/H antiporters differing in their substrate specificity.","citation":"FEMS Yeast Res 2007 Mar;7(2):188-95","abstract":"The Schizosaccharomyces pombe plasma membrane Na(+)/H(+) antiporter, SpSod2p, has been shown to belong to the subfamily of yeast Na(+)/H(+) antiporters that only recognize Na(+) and Li(+) as substrates. Nevertheless, most of the studied plasma membrane alkali metal cation/H(+) antiporters from other yeasts have broader substrate specificities, exporting K(+) and Rb(+) as well. Such antiporters probably play two roles in the physiology of cells: the elimination of surplus toxic cations, and the regulation of stable intracellular K(+) content, pH and cell volume. The systematic sequencing of the Sch. pombe genome revealed the presence of an as-yet uncharacterized homolog of the Spsod2 gene (designated Spsod22). Spsod22 and Spsod2 were expressed in Saccharomyces cerevisiae cells lacking their own alkali metal cation efflux systems, and the transport properties of both Sch. pombe antiporters were compared to those of the Sac. cerevisiae Nha1 antiporter expressed under the same conditions. Here we show that SpSod22p has broad substrate specificity upon heterologous expression in Sac. cerevisiae cells and contributes to cell tolerance to high external levels of K(+). Thus, the Sch. pombe genome encodes two plasma membrane alkali metal cation/H(+) antiporters that play different roles in the physiology of the yeast.","authors":"Papouskova K, Sychrova H","authors_abbrev":"Papouskova K et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-02-03","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7956080","title":"Coupling DNA replication to the cell cycle.","citation":"Cold Spring Harb Symp Quant Biol 1993;58:637-44","abstract":"","authors":"Kelly TJ, Nurse P, Forsburg SL","authors_abbrev":"Kelly TJ et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8292390","title":"A novel mutation involved in the mitotic checkpoint in the fission yeast Schizosaccharomyces pombe.","citation":"Jpn J Genet 1993 Aug;68(4):265-76","abstract":"The cps8 mutation which confers supersensitivity to a spindle poison, Isopropyl N-3-chlorophenyl carbamate (CIPC), in the fission yeast Schizosaccharomyces pombe was investigated. The cps8 mutant accumulated enlarged multinucleate cells in the stationary phase under normal growth conditions. The mutant was highly lethal at 36.5 degrees C in a fresh growth medium but not in a saline solution where the cell cycle ceases quickly. Lethality at high temperature was significantly suppressed by cdc1 or nda2 mutation which blocks nuclear division, but not by hydroxyurea treatment or cdc22 mutation which blocks DNA synthesis. A cdc10 cps8 double mutant remained lethal to high temperature, suggesting this double mutant to bypass the requirement for cdc10+ indispensable for the cell cycle start in a wild-type cell. After being transferred to a fresh medium at 36.5 degrees C, the multinucleate cells rapidly divided with aberrant nuclear segregation. Thus, cps8 mutation allows cells to undergo mitosis without DNA replication at the restrictive temperature. The cps8 gene was mapped on the left arm of chromosome II closely linked to but distinct from cdc2 locus.","authors":"Ishiguro J, Yamada N","authors_abbrev":"Ishiguro J et al.","pubmed_publication_date":"Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_session_key":"e92c2476d90dea83","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-03-12 17:12:26","canto_approved_date":"2026-01-29 12:04:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 17:12:19","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27E2.05","SPAC24H6.05","SPBC32H8.12c","SPBC16A3.15c","SPAC1F7.05","SPBC336.12c","SPCC18B5.03"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2015-03-12"},{"uniquename":"PMID:25143395","title":"Local and global analysis of endocytic patch dynamics in fission yeast using a new \"temporal superresolution\" realignment method.","citation":"Mol Biol Cell 2014 Nov 05;25(22):3501-14","abstract":"Quantitative microscopy is a valuable tool for inferring molecular mechanisms of cellular processes such as clathrin-mediated endocytosis, but, for quantitative microscopy to reach its potential, both data collection and analysis needed improvement. We introduce new tools to track and count endocytic patches in fission yeast to increase the quality of the data extracted from quantitative microscopy movies. We present a universal method to achieve \"temporal superresolution\" by aligning temporal data sets with higher temporal resolution than the measurement intervals. These methods allowed us to extract new information about endocytic actin patches in wild-type cells from measurements of the fluorescence of fimbrin-mEGFP. We show that the time course of actin assembly and disassembly varies <600 ms between patches. Actin polymerizes during vesicle formation, but we show that polymerization does not participate in vesicle movement other than to limit the complex diffusive motions of newly formed endocytic vesicles, which move faster as the surrounding actin meshwork decreases in size over time. Our methods also show that the number of patches in fission yeast is proportional to cell length and that the variability in the repartition of patches between the tips of interphase cells has been underestimated.","doi":"10.1091/mbc.E13-01-0004","authors":"Berro J, Pollard TD","authors_abbrev":"Berro J et al.","pubmed_publication_date":"05 Nov 2014","pubmed_entrez_date":"2014-08-22","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-08-23 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16678171","title":"Transcription regulation of the alpha-glucanase gene agn1 by cell separation transcription factor Ace2p in fission yeast.","citation":"FEBS Lett 2006 May 29;580(13):3099-106","abstract":"During the final stage of the cell division cycle in the fission yeast Schizosaccharomyces pombe, transcription factor Ace2p activates expression of genes involved in the separation of newly formed daughter cells, such as agn1+, which encodes the alpha-glucanase Agn1p. The agn1 promoter contains three copies of the nucleotide sequence motif CCAGCC, whose presence seems to correlate with Ace2p-mediated transcription activation. Here, we describe a simple plate-based assay utilizing as a reporter the secreted glucoamylase of Arxula adeninivorans to investigate the function of this motif. We show that not all three repeats, but only the two most proximal to the transcription start point, act as an upstream activating sequence (UAS). Finally, we demonstrate that this UAS is essential for agn1 promoter activity in vivo.","authors":"Dekker N, de Haan A, Hochstenbach F","authors_abbrev":"Dekker N et al.","pubmed_publication_date":"29 May 2006","pubmed_entrez_date":"2006-05-09","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.09","SPAC6G10.12c"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:26877082","title":"ER-PM Contacts Define Actomyosin Kinetics for Proper Contractile Ring Assembly.","citation":"Curr Biol 2016 Mar 07;26(5):647-53","abstract":"The cortical endoplasmic reticulum (ER), an elaborate network of tubules and cisternae [1], establishes contact sites with the plasma membrane (PM) through tethering machinery involving a set of conserved integral ER proteins [2]. The physiological consequences of forming ER-PM contacts are not fully understood. Here, we reveal a kinetic restriction role of ER-PM contacts over ring compaction process for proper actomyosin ring assembly in Schizosaccharomyces pombe. We show that fission yeast cells deficient in ER-PM contacts exhibit aberrant equatorial clustering of actin cables during ring assembly and are particularly susceptible to compromised actin filament crosslinking activity. Using quantitative image analyses and computer simulation, we demonstrate that ER-PM contacts function to modulate the distribution of ring components and to constrain their compaction kinetics. We propose that ER-PM contacts have evolved as important physical modulators to ensure robust ring assembly.","doi":"10.1016/j.cub.2015.12.070","authors":"Zhang D, Bidone TC, Vavylonis D","authors_abbrev":"Zhang D et al.","pubmed_publication_date":"07 Mar 2016","pubmed_entrez_date":"2016-02-16","publication_year":"2016","canto_session_key":"0431a5bb28c48745","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dan Zhang","canto_first_approved_date":"2017-04-17 20:26:19","canto_approved_date":"2026-04-22 15:36:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-30 16:00:23","canto_added_date":"2016-02-17 01:15:14","annotation_curators":[{"name":"Dan Zhang","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16G5.05c","SPAC17C9.12","SPAC15A10.08"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-04-17"},{"uniquename":"PMID:8375648","title":"Directionality of fission yeast mating-type interconversion is controlled by the location of the donor loci.","citation":"Genetics 1993 Aug;134(4):1045-54","abstract":"Cells of homothallic strains of Schizosaccharomyces pombe efficiently switch between two mating types called P and M. The phenotypic switches are due to conversion of the expressed mating-type locus (mat1) by two closely linked silent loci, mat2-P and mat3-M, that contain unexpressed information for the P and M mating types, respectively. In this process, switching-competent cells switch to the opposite mating type in 72-90% of the cell divisions. Hence, mat2-P is a preferred donor of information to mat1 in M cells, whereas mat3-M is a preferred donor in P cells. We investigated the reason for the donor preference by constructing a strain in which the genetic contents of the donor loci were swapped. We found that switching to the opposite mating type was very inefficient in that strain. This shows that the location of the silent cassettes in the chromosome, rather than their content, is the deciding factor for recognition of the donor for each cell type. We propose a model in which switching is achieved by regulating accessibility of the donor loci, perhaps by changing the chromatin structure in the mating-type region, thus promoting an intrachromosomal folding of mat2 or mat3 onto mat1 in a cell type-specific fashion. We also present evidence for the involvement of the Swi6 and Swi6-mod trans-acting factors in the donor-choice mechanism. We suggest that these factors participate in forming the proposed folded structure.","authors":"Thon G, Klar AJ","authors_abbrev":"Thon G et al.","pubmed_publication_date":"Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33658710","title":"Centromeres are dismantled by foundational meiotic proteins Spo11 and Rec8.","citation":"Nature 2021 Mar;591(7851):671-676","abstract":"Meiotic processes are potentially dangerous to genome stability and could be disastrous if activated in proliferative cells. Here we show that two key meiosis-defining proteins, the topoisomerase Spo11 (which forms double-strand breaks) and the meiotic cohesin Rec8, can dismantle centromeres. This dismantlement is normally observable only in mutant cells that lack the telomere bouquet, which provides a nuclear microdomain conducive to centromere reassembly 1 ; however, overexpression of Spo11 or Rec8 leads to levels of centromere dismantlement that cannot be countered by the bouquet. Specific nucleosome remodelling factors mediate centromere dismantlement by Spo11 and Rec8. Ectopic expression of either protein in proliferating cells leads to the loss of mitotic kinetochores in both fission yeast and human cells. Hence, while centromeric chromatin has been characterized as extraordinarily stable, Spo11 and Rec8 challenge this stability and may jeopardize kinetochores in cancers that express meiotic proteins.","doi":"10.1038/s41586-021-03279-8","authors":"Hou H, Kyriacou E, Thadani R, Klutstein M, Chapman JH, Cooper JP","authors_abbrev":"Hou H et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2021-03-04","publication_year":"2021","canto_session_key":"abe7e683503fbf57","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-03-05 11:42:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15936270","title":"Wsh3/Tea4 is a novel cell-end factor essential for bipolar distribution of Tea1 and protects cell polarity under environmental stress in S. pombe.","citation":"Curr Biol 2005 Jun 07;15(11):1006-15","abstract":"The fission yeast Schizosaccharomyces pombe has a cylindrical cell shape, for which growth is strictly limited to both ends, and serves as an excellent model system for genetic analysis of cell-polarity determination. Previous studies identified a cell-end marker protein, Tea1, that is transported by cytoplasmic microtubules to cell tips and recruits other cell-end factors, including the Dyrk-family Pom1 kinase. The deltatea1 mutant cells cannot grow in a bipolar fashion and show T-shaped morphology after heat shock.\nWe identified Wsh3/Tea4 as a novel protein that interacts with Win1 MAP kinase kinase kinase (MAPKKK) of the stress-activated MAP kinase cascade. Wsh3 forms a complex with Tea1 and is transported to cell tips by growing microtubules. The deltawsh3 mutant shows monopolar growth with abnormal Tea1 aggregate at the non-growing cell end; this abnormal aggregate fails to recruit Pom1 kinase. Consistent with the observed interaction between Win1 and Wsh3, cells lacking Wsh3 or Tea1 show more severe cell-polarity defects under osmolarity and heat-stress stimuli that are known to activate the stress MAPK cascade. Furthermore, mutants of the stress MAPK also exhibit cell-polarity defects when exposed to the same stress.\nWsh3/Tea4 is an essential component of the Tea1 cell-end complex. In addition to its role in bipolar growth during the normal cell cycle, the Wsh3-Tea1 complex, together with the stress-signaling MAPK cascade, contributes to cell-polarity maintenance under stress conditions.","authors":"Tatebe H, Shimada K, Uzawa S, Morigasaki S, Shiozaki K","authors_abbrev":"Tatebe H et al.","pubmed_publication_date":"07 Jun 2005","pubmed_entrez_date":"2005-06-07","publication_year":"2005","canto_session_key":"72405b0ba0db4d73","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-06-18 08:21:36","canto_approved_date":"2025-09-04 11:42:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-16 15:51:28","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPCC1223.06","SPBC1706.01","SPAC2F7.03c","SPAC24B11.06c","SPCC1739.11c","SPAC1006.09"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2020-06-18"},{"uniquename":"PMID:7660474","title":"Genetic nomenclature guide. Schizosaccharomyces pombe.","citation":"Trends Genet 1995 Mar;:9-10","abstract":"","authors":"Kohli J, Nurse P","authors_abbrev":"Kohli J et al.","pubmed_publication_date":"Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21307936","title":"Structural basis for the subunit assembly of the anaphase-promoting complex.","citation":"Nature 2011 Feb 10;470(7333):227-32","abstract":"The anaphase-promoting complex or cyclosome (APC/C) is an unusually large E3 ubiquitin ligase responsible for regulating defined cell cycle transitions. Information on how its 13 constituent proteins are assembled, and how they interact with co-activators, substrates and regulatory proteins is limited. Here, we describe a recombinant expression system that allows the reconstitution of holo APC/C and its sub-complexes that, when combined with electron microscopy, mass spectrometry and docking of crystallographic and homology-derived coordinates, provides a precise definition of the organization and structure of all essential APC/C subunits, resulting in a pseudo-atomic model for 70% of the APC/C. A lattice-like appearance of the APC/C is generated by multiple repeat motifs of most APC/C subunits. Three conserved tetratricopeptide repeat (TPR) subunits (Cdc16, Cdc23 and Cdc27) share related superhelical homo-dimeric architectures that assemble to generate a quasi-symmetrical structure. Our structure explains how this TPR sub-complex, together with additional scaffolding subunits (Apc1, Apc4 and Apc5), coordinate the juxtaposition of the catalytic and substrate recognition module (Apc2, Apc11 and Apc10 (also known as Doc1)), and TPR-phosphorylation sites, relative to co-activator, regulatory proteins and substrates.","doi":"10.1038/nature09756","authors":"Schreiber A, Stengel F, Zhang Z, Enchev RI, Kong EH, Morris EP, Robinson CV, da Fonseca PC, Barford D","authors_abbrev":"Schreiber A et al.","pubmed_publication_date":"10 Feb 2011","pubmed_entrez_date":"2011-02-11","publication_year":"2011","canto_session_key":"cf3005820af86b6a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-04 14:45:33","canto_approved_date":"2025-09-04 07:23:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-04 14:45:06","canto_added_date":"2015-10-23 16:58:23","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-04-04"},{"uniquename":"PMID:27884105","title":"Structural features of DNA that determine RNA polymerase II core promoter.","citation":"BMC Genomics 2016 Nov 25;17(1):973","abstract":"The general structure and action of all eukaryotic and archaeal RNA polymerases machinery have an astonishing similarity despite the diversity of core promoter sequences in different species. The goal of our work is to find common characteristics of DNA region that define it as a promoter for the RNA polymerase II (Pol II).\nThe profiles of a large number of physical and structural characteristics, averaged over representative sets of the Pol II minimal core promoters of the evolutionary divergent species from animals, plants and unicellular fungi were analysed. In addition to the characteristics defined at the base-pair steps, we, for the first time, use profiles of the ultrasonic cleavage and DNase I cleavage indexes, informative for internal properties of each complementary strand.\nDNA of the core promoters of metazoans and Schizosaccharomyces pombe has similar structural organization. Its mechanical and 3D structural characteristics have singular properties at the positions of TATA-box. The minor groove is broadened and conformational motion is decreased in that region. Special characteristics of conformational behavior are revealed in metazoans at the region, which connects the end of TATA-box and the transcription start site (TSS). The intensities of conformational motions in the complementary strands are periodically changed in opposite phases. They are noticeable, best of all, in mammals. Such conformational features are lacking in the core promoters of S. pombe. The profiles of Saccharomyces cerevisiae core promoters significantly differ: their singular region is shifted down thus pointing to the uniqueness of their structural organization. Obtained results may be useful in genetic engineering for artificial modulation of the promoter strength.","authors":"Il'icheva IA, Khodikov MV, Poptsova MS, Nechipurenko DY, Nechipurenko YD, Grokhovsky SL","authors_abbrev":"Il'icheva IA et al.","pubmed_publication_date":"25 Nov 2016","pubmed_entrez_date":"2016-11-26","publication_year":"2016","canto_session_key":"195b92fda1b69c9c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 18:04:53","canto_approved_date":"2019-01-31 18:04:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 17:58:56","canto_added_date":"2016-11-27 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"EMBL:SPSQUASYN","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21856351","title":"Uptake of various yeast genera by antigen-presenting cells and influence of subcellular antigen localization on the activation of ovalbumin-specific CD8 T lymphocytes.","citation":"Vaccine 2011 Oct 19;29(45):8165-73","abstract":"Yeasts of the genus Saccharomyces expressing recombinant antigens are currently evaluated as candidate T cell vaccines. Here, we compared the interaction kinetics between four biotechnologically relevant yeast genera (Saccharomyces cerevisiae, Schizosaccharomyces pombe, Kluyveromyces lactis and Pichia pastoris) and human dendritic cells as well as the involvement of Dectin-1 and mannose receptor in phagocytosis. Further, we analyzed the activation capacity of recombinant yeasts expressing ovalbumin (OVA) either intracellular, extracellular or surface-displayed by OVA-specific CD8 T lymphocytes. We found that the kinetic patterns of yeast uptake by phagocytic cells varied between the tested yeast genera and that both genus and subcellular OVA antigen localization influenced the strength of T cell activation. In particular, in S. cerevisiae, a secreted antigen was less effectively delivered than its cytosolic variant, whereas most efficient antigen delivery with P. pastoris was obtained by cell surface bound antigen. Our data indicate that protein secretion might not be an effective delivery pathway in yeast.","doi":"10.1016/j.vaccine.2011.07.141","authors":"Bazan SB, Geginat G, Breinig T, Schmitt MJ, Breinig F","authors_abbrev":"Bazan SB et al.","pubmed_publication_date":"19 Oct 2011","pubmed_entrez_date":"2011-08-23","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15870269","title":"Response of fission yeast to toxic cations involves cooperative action of the stress-activated protein kinase Spc1/Sty1 and the Hal4 protein kinase.","citation":"Mol Cell Biol 2005 May;25(10):3945-55","abstract":"Stress-activated protein kinases (SAPKs), members of a mitogen-activated protein kinase (MAPK) subfamily, are highly conserved among eukaryotes. Studies of yeasts demonstrated that SAPKs play pivotal roles in survival responses to high osmolarity, oxidative stress, and heat shock. Here we report a novel physiological role of the fission yeast Spc1 SAPK in cellular resistance to certain cations, such as Na(+), Li(+), and Ca(2+). Strains lacking Spc1 or its activator, Wis1 MAPK kinase, are hypersensitive to these cations. Spc1 positively regulates expression of sod2(+) encoding a Na(+)/H(+) antiporter through Atf1 and other transcription factors. In addition, we have identified a novel Spc1-interacting protein, Hal4, which is highly homologous to the budding yeast Sat4/Hal4 protein kinase. Like its budding yeast counterpart, the fission yeast Hal4 kinase is essential for cellular resistance to Na(+), Li(+), and Ca(2+). The hal4-null phenotype is complemented by overexpression of the Trk1 potassium transporter or increased K(+) in the growth medium, suggesting that Hal4 promotes K(+) uptake, which consequently increases cellular resistance to other cations. Interestingly, the Spc1-Hal4 interaction appears to be required for cellular resistance to Ca(2+) but not Na(+) and Li(+). We propose that Spc1 SAPK and Hal4 kinase cooperatively function to protect cells from the toxic cations.","authors":"Wang LY, Shimada K, Morishita M, Shiozaki K","authors_abbrev":"Wang LY et al.","pubmed_publication_date":"May 2005","pubmed_entrez_date":"2005-05-05","publication_year":"2005","canto_session_key":"09a2ea749be9cd03","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-22 16:00:29","canto_approved_date":"2023-02-14 21:15:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-22 16:00:19","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":55,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29A4.16","SPBC29B5.01","SPAC977.10","SPBC409.07c","SPAC3F10.02c","SPAC23A1.06c","SPCC1322.08","SPAC1639.02c","SPAC26F1.10c","SPAC24B11.06c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2017-09-22"},{"uniquename":"PMID:27876895","title":"Multiple crosstalk between TOR and the cell integrity MAPK signaling pathway in fission yeast.","citation":"Sci Rep 2016 Nov 23;6:37515","abstract":"In eukaryotic cells, the highly conserved Target of Rapamycin (TOR) and the Mitogen Activated Protein Kinase (MAPK) signaling pathways elicit adaptive responses to extra- and intracellular conditions by regulating essential cellular functions. However, the nature of the functional relationships between both pathways is not fully understood. In the fission yeast Schizosaccharomyces pombe the cell integrity MAPK pathway (CIP) regulates morphogenesis, cell wall structure and ionic homeostasis. We show that the Rab GTPase Ryh1, a TORC2 complex activator, cross-activates the CIP and its core member, the MAPK Pmk1, by two distinct mechanisms. The first one involves TORC2 and its downstream effector, Akt ortholog Gad8, which together with TORC1 target Psk1 increase protein levels of the PKC ortholog Pck2 during cell wall stress or glucose starvation. Also, Ryh1 activates Pmk1 in a TORC2-independent fashion by prompting plasma membrane trafficking and stabilization of upstream activators of the MAPK cascade, including PDK ortholog Ksg1 or Rho1 GEF Rgf1. Besides, stress-activated Pmk1 cross-inhibits Ryh1 signaling by decreasing the GTPase activation cycle, and this ensures cell growth during alterations in phosphoinositide metabolism. Our results reveal a highly intricate cross-regulatory relationship between both pathways that warrants adequate cell adaptation and survival in response to environmental changes.","doi":"10.1038/srep37515","authors":"Madrid M, Vázquez-Marín B, Franco A, Soto T, Vicente-Soler J, Gacto M, Cansado J","authors_abbrev":"Madrid M et al.","pubmed_publication_date":"23 Nov 2016","pubmed_entrez_date":"2016-11-24","publication_year":"2016","canto_session_key":"40259d467850f810","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-11-25 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4G3.08","SPAC4C5.02c","SPCC24B10.07","SPAC19G12.14","SPBC651.03c","SPBC216.07c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:24019917","title":"Relationships between cell cycle regulator gene copy numbers and protein expression levels in Schizosaccharomyces pombe.","citation":"PLoS One 2013;8(9):e73319","abstract":"We previously determined the copy number limits of overexpression for cell division cycle (cdc) regulatory genes in the fission yeast Schizosaccharomyces pombe using the \"genetic tug-of-war\" (gTOW) method. In this study, we measured the levels of tandem affinity purification (TAP)-tagged target proteins when their copy numbers are increased in gTOW. Twenty analyzed genes showed roughly linear correlations between increased protein levels and gene copy numbers, which suggested a general lack of compensation for gene dosage in S. pombe. Cdc16 and Sid2 protein levels but not their mRNA levels were much lower than that expected by their copy numbers, which suggested the existence of a post-transcriptional down regulation of these genes. The cyclin Cig1 protein level and its mRNA level were much higher than that expected by its copy numbers, which suggested a positive feedback mechanism for its expression. A higher Cdc10 protein level and its mRNA level, probably due to cloning its gene into a plasmid, indicated that Cdc10 regulation was more robust than that previously predicted.","doi":"10.1371/journal.pone.0073319","authors":"Chino A, Makanae K, Moriya H","authors_abbrev":"Chino A et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-09-11","publication_year":"2013","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16911510","title":"Heat shock-inducible expression vectors for use in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2006 Sep;6(6):883-7","abstract":"A new, heat shock-inducible expression system based on an endogenous hsp16+ promoter was developed for use in the fission yeast Schizosaccharomyces pombe. Analysis of GFP expression profiles indicated that a 1.2-kb segment of the hsp16+ promoter region was sufficient to drive expression of heterologous protein. The hsp16+ promoter was found to be activated not only by heat shock but also by other stresses including cadmium, ethanol, and oxidative stress. Two expression vectors, pHIL and pHIU, were constructed using the 1.2-kb hsp16+ promoter for inducible gene expression in Sch. pombe. This new expression system utilizes a simple induction protocol and promises to be a useful tool for analyzing gene expression in Sch. pombe.","authors":"Fujita Y, Tohda H, Giga-Hama Y, Takegawa K","authors_abbrev":"Fujita Y et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-08-17","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15546162","title":"pDUAL, a multipurpose, multicopy vector capable of chromosomal integration in fission yeast.","citation":"Yeast 2004 Nov;21(15):1289-305","abstract":"A novel series of plasmid vectors named pDUAL have been developed. These vectors enable one to introduce not only multicopies of genes with episomal maintenance but also a single copy with chromosomal integration into the fission yeast, Schizosaccharomyces pombe. The multicopy plasmids can be easily converted to fragments for chromosomal integration by digestion of the plasmids with a certain restriction endonuclease before transformation of the yeast cells. The resultant fragments, lacking the autonomously replicating sequence, are designed for targeting into the chromosomal leu1 locus by homologous recombination. Whether the transformants are the results of episomal maintenance of the plasmid or homologous gene targeting can be readily checked by their requirement for uracil or leucine, or by the PCR diagnostic analysis. Furthermore, we propose the use of pDUAL derivatives for PCR-based chromosomal tagging of a gene to introduce several tags into 5'-terminus of a gene, employing a set of primers. Using these all-in-one vectors, a suitable mode of expression of a cloned gene can be selected for individual analysis without any complicated subcloning processes.","authors":"Matsuyama A, Shirai A, Yashiroda Y, Kamata A, Horinouchi S, Yoshida M","authors_abbrev":"Matsuyama A et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-11-17","publication_year":"2004","canto_session_key":"86746c3b2bce0444","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-07-19 11:40:08","canto_approved_date":"2024-07-15 11:52:30","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-07-19 06:49:56","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC9B6.08","SPBC1A4.02c","SPBC800.05c","SPCC330.05c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2012-07-19"},{"uniquename":"EMBL:AU008601","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38442865","title":"The fission yeast NDR kinase Orb6 and its signalling pathway MOR regulate cytoplasmic microtubule organization during the cell cycle.","citation":"Open Biol 2024 Mar;14(3):230440","abstract":"Microtubule organization and reorganization during the cell cycle are achieved by regulation of the number, distribution and activity of microtubule-organizing centres (MTOCs). In fission yeast, the Mto1/2 complex determines the activity and distribution of cytoplasmic MTOCs. Upon mitosis, cytoplasmic microtubule nucleation ceases; inactivation of the Mto1/2 complex is triggered by Mto2 hyperphosphorylation. However, the protein kinase(s) that phosphorylates Mto2 remains elusive. Here we show that a conserved signalling network, called MOR (morphogenesis Orb6 network) in fission yeast, negatively regulates cytoplasmic MTOCs through Mto2 phosphorylation to ensure proper microtubule organization. Inactivation of Orb6 kinase, the most downstream MOR component, by attenuation of MOR signalling leads to reduced Mto2 phosphorylation, coincident with increased number of both Mto2 puncta and cytoplasmic microtubules. These defects cause the emergence of uncoordinated mitotic cells with cytoplasmic microtubules, resulting in reduced spindle assembly. Thus, the regulation of Mto2 by the MOR is crucial for cytoplasmic microtubule organization and contributes to reorganization of the microtubule cytoskeletons during the cell cycle.","doi":"10.1098/rsob.230440","authors":"Kume K, Nishikawa K, Furuyama R, Fujimoto T, Koyano T, Matsuyama M, Mizunuma M, Hirata D","authors_abbrev":"Kume K et al.","pubmed_publication_date":"Mar 2024","pubmed_entrez_date":"2024-03-05","publication_year":"2024","canto_session_key":"82e092beb9dd503e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kazunori Kume","canto_first_approved_date":"2024-06-26 08:55:22","canto_approved_date":"2024-09-24 09:22:47","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-06-18 15:34:08","canto_added_date":"2024-03-07 00:25:05","annotation_curators":[{"name":"Kazunori Kume","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":30,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17F3.02","SPBP19A11.04c","SPAPB1A10.09","SPCC1281.01","SPBC902.06","SPAC1834.06c","SPAC18G6.15","SPCC16C4.09","SPCC417.07c","SPAC821.12"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2024-06-26"},{"uniquename":"PMID:8358826","title":"Reorientation of the distal region in linkage group IIR of fission yeast.","citation":"Curr Genet 1993;24(1-2):179-80","abstract":"The genetic map of the fission yeast Schizosaccharomyces pombe has been revised in the distal region of chromosome arm IIR. The spo4 locus, hitherto considered the outermost marker, has been moved to an intermediate position. As a result, and in accordance with recent physical mapping data, the order of the entire distal subgroup of some 12 genetic markers is reversed relative to previously published gene maps.","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-07-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3576170","title":"Cell cycle genes of the fission yeast.","citation":"Sci Prog 1987;71(281 Pt 1):1-14","abstract":"","authors":"Lee MG, Nurse P","authors_abbrev":"Lee MG et al.","pubmed_publication_date":"1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19710424","title":"Pob1 participates in the Cdc42 regulation of fission yeast actin cytoskeleton.","citation":"Mol Biol Cell 2009 Oct;20(20):4390-9","abstract":"Rho GTPases regulate the actin cytoskeleton in all eukaryotes. Fission yeast Cdc42 is involved in actin cable assembly and formin For3 regulation. We isolated cdc42-879 as a thermosensitive strain with actin cable and For3 localization defects. In a multicopy suppressor screening, we identified pob1(+) as suppressor of cdc42-879 thermosensitivity. Pob1 overexpression also partially restores actin cables and localization of For3 in the mutant strain. Pob1 interacts with Cdc42 and this GTPase regulates Pob1 localization and/or stability. The C-terminal pleckstrin homology (PH) domain of Pob1 is required for Cdc42 binding. Pob1 also binds to For3 through its N-terminal sterile alpha motif (SAM) domain and contributes to the formin localization at the cell tips. The previously described pob1-664 mutant strain (Mol. Biol. Cell. 10, 2745-2757, 1999), which carries a mutation in the PH domain, as well as pob1 mutant strains in which Pob1 lacks the N-terminal region (pob1DeltaN) or the SAM domain (pob1DeltaSAM), have cytoskeletal defects similar to that of cdc42-879 cells. Expression of constitutively active For3DAD* partially restores actin organization in cdc42-879, pob1-664, pob1DeltaN, and pob1DeltaSAM. Therefore, we propose that Pob1 is required for For3 localization to the tips and facilitates Cdc42-mediated relief of For3 autoinhibition to stimulate actin cable formation.","authors":"Rincón SA, Ye Y, Villar-Tajadura MA, Santos B, Martin SG, Pérez P","authors_abbrev":"Rincón SA et al.","pubmed_publication_date":"Oct 2009","pubmed_entrez_date":"2009-08-28","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22H10.07","SPCC895.05","SPAC110.03","SPBC1289.04c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:21089642","title":"[Regulation of RNA-binding proteins by MAPK signaling].","citation":"Tanpakushitsu Kakusan Koso 2009 Dec;54(16 Suppl):2207-12","abstract":"","authors":"Satoh R, Takada H, Kita A, Sugiura R","authors_abbrev":"Satoh R et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2010-11-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12788946","title":"Homodimeric quaternary structure is required for the in vivo function and thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe RNA triphosphatases.","citation":"J Biol Chem 2003 Aug 15;278(33):30487-96","abstract":"Saccharomyces cerevisiae Cet1 and Schizosaccharomyces pombe Pct1 are the essential RNA triphosphatase components of the mRNA capping apparatus of budding and fission yeast, respectively. Cet1 and Pct1 share a baroque active site architecture and a homodimeric quaternary structure. The active site is located within a topologically closed hydrophilic beta-barrel (the triphosphate tunnel) that rests on a globular core domain (the pedestal) composed of elements from both protomers of the homodimer. Earlier studies of the effects of alanine cluster mutations at the crystallographic dimer interface of Cet1 suggested that homodimerization is important for triphosphatase function in vivo, albeit not for catalysis. Here, we studied the effects of 14 single-alanine mutations on Cet1 activity and thereby pinpointed Asp280 as a critical side chain required for dimer formation. We find that disruption of the dimer interface is lethal in vivo and renders Cet1 activity thermolabile at physiological temperatures in vitro. In addition, we identify individual residues within the pedestal domain (Ile470, Leu519, Ile520, Phe523, Leu524, and Ile530) that stabilize Cet1 in vivo and in vitro. In the case of Pct1, we show that dimerization depends on the peptide segment 41VPKIEMNFLN50 located immediately prior to the start of the Pct1 catalytic domain. Deletion of this peptide converts Pct1 into a catalytically active monomer that is defective in vivo in S. pombe and hypersensitive to thermal inactivation in vitro. Our findings suggest an explanation for the conservation of quaternary structure in fungal RNA triphosphatases, whereby the delicate tunnel architecture of the active site is stabilized by the homodimeric pedestal domain.","authors":"Hausmann S, Pei Y, Shuman S","authors_abbrev":"Hausmann S et al.","pubmed_publication_date":"15 Aug 2003","pubmed_entrez_date":"2003-06-06","publication_year":"2003","canto_session_key":"ce3349acca59ef69","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-19 17:06:43","canto_approved_date":"2021-09-27 16:38:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-22 15:17:08","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.09c","SPAC644.04"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-01-19"},{"uniquename":"PANTHER:PTHR13384","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20H4.08","SPBP4H10.16c","HGNC:24658"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:12628934","title":"Pathway utilization in response to a site-specific DNA double-strand break in fission yeast.","citation":"EMBO J 2003 Mar 17;22(6):1419-30","abstract":"We have examined the genetic requirements for efficient repair of a site-specific DNA double-strand break (DSB) in Schizosaccharomyces pombe. Tech nology was developed in which a unique DSB could be generated in a non-essential minichromosome, Ch(16), using the Saccharomyces cerevisiae HO-endonuclease and its target site, MATa. DSB repair in this context was predominantly through interchromosomal gene conversion. We found that the homologous recombination (HR) genes rhp51(+), rad22A(+), rad32(+) and the nucleotide excision repair gene rad16(+) were required for efficient interchromosomal gene conversion. Further, DSB-induced cell cycle delay and efficient HR required the DNA integrity checkpoint gene rad3(+). Rhp55 was required for interchromosomal gene conversion; however, an alternative DSB repair mechanism was used in an rhp55Delta background involving ku70(+) and rhp51(+). Surprisingly, DSB-induced minichromosome loss was significantly reduced in ku70Delta and lig4Delta non-homologous end joining (NHEJ) mutant backgrounds compared with wild type. Furthermore, roles for Ku70 and Lig4 were identified in suppressing DSB-induced chromosomal rearrangements associated with gene conversion. These findings are consistent with both competitive and cooperative interactions between components of the HR and NHEJ pathways.","authors":"Prudden J, Evans JS, Hussey SP, Deans B, O'Neill P, Thacker J, Humphrey T","authors_abbrev":"Prudden J et al.","pubmed_publication_date":"17 Mar 2003","pubmed_entrez_date":"2003-03-12","publication_year":"2003","canto_session_key":"acc7b3fc549e03fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-05-04 15:49:03","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-05-04 15:48:55","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPCC970.01","SPBC216.05","SPCC1183.05c","SPAC30D11.10","SPAC3C7.03c","SPCC126.02c","SPAC13C5.07"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-05-04"},{"uniquename":"PMID:16390871","title":"Activity of Cdc2 and its interaction with the cyclin Cdc13 depend on the molecular chaperone Cdc37 in Schizosaccharomyces pombe.","citation":"J Cell Sci 2006 Jan 15;119(Pt 2):292-302","abstract":"Cdc37 is a molecular chaperone whose clients are predominantly protein kinases, many of which are important in cell-cycle progression. Temperature-sensitive mutants of cdc37 in Schizosaccharomyces pombe are lethal at the restrictive temperature, arresting cell division within a single cell cycle. These mutant cells elongate during incubation at the restrictive temperature, consistent with a cell-cycle defect. The cell-cycle arrest arises from defective function of the mutant Cdc37 proteins rather than a reduction in Cdc37 protein levels. Around 80% of the arrested, elongated cells contain a single nucleus and replicated (2C) DNA content, indicating that these mutants arrest the cell cycle in G2 or mitosis (M). Cytological observations show that the majority of cells arrest in G2. In fission yeast, a G2 cell-cycle arrest can arise by inactivation of the cyclin-dependent kinase (Cdk) Cdc2 that regulates entry into mitosis. Studies of the cdc37 temperature-sensitive mutants show a genetic interaction with some cdc2 alleles and overexpression of cdc2 rescues the lethality of some cdc37 alleles at the restrictive temperature, suggesting that Cdc2 is a likely client for the Cdc37 molecular chaperone. In cdc37 temperature-sensitive mutants at the restrictive temperature, the level of Cdc2 protein remains constant but Cdc2 protein kinase activity is greatly reduced. Inactivation of Cdc2 appears to result from the inability to form complexes with its mitotic cyclin partner Cdc13. Further evidence for Cdc2 being a client of Cdc37 in S. pombe comes from the identification of genetic and biochemical interactions between these proteins.","authors":"Turnbull EL, Martin IV, Fantes PA","authors_abbrev":"Turnbull EL et al.","pubmed_publication_date":"15 Jan 2006","pubmed_entrez_date":"2006-01-05","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03","SPBC9B6.10"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:34918022","title":"The fission yeast bromodomain protein Bdf2 is required for the growth of cells with circular chromosomes.","citation":"Biosci Biotechnol Biochem 2022 Jan 24;86(2):224-230","abstract":"Circular chromosomes have frequently been observed in tumors of mesenchymal origin. In the fission yeast Schizosaccharomyces pombe, deletion of pot1+ results in rapid telomere loss, and the resulting survivors have circular chromosomes. Fission yeast has 2 bromodomain and extra-terminal (BET) proteins, Bdf1 and Bdf2; both are required for maintaining acetylated histones. Here, we found that bdf2, but not bdf1, was synthetically lethal with pot1. We also obtained a temperature-sensitive bdf2-ts mutant, which can grow at high temperatures but becomes camptothecin sensitive. This suggests that Bdf2 is defective at high temperatures. The cell cycle of the pot1 bdf2-ts mutant was delayed in the G2 and/or M phase at a semipermissive temperature. Furthermore, a temperature-sensitive mutant of mst1, which encodes histone acetyltransferase, showed a synthetic growth defect with a pot1 disruptant at a semipermissive temperature. Our results suggest that Bdf2 and Mst1 are required for the growth of cells with circular chromosomes.","doi":"10.1093/bbb/zbab215","authors":"Yasuda M, Habib AGK, Sugiura K, Shamim HM, Ueno M","authors_abbrev":"Yasuda M et al.","pubmed_publication_date":"24 Jan 2022","pubmed_entrez_date":"2021-12-17","publication_year":"2022","canto_session_key":"a643b3ec3dbdf557","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-21 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009902","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30726745","title":"Fission Yeast NDR/LATS Kinase Orb6 Regulates Exocytosis via Phosphorylation of the Exocyst Complex.","citation":"Cell Rep 2019 Feb 05;26(6):1654-1667.e7","abstract":"NDR/LATS kinases regulate multiple aspects of cell polarity and morphogenesis from yeast to mammals. Fission yeast NDR/LATS kinase Orb6 has been proposed to control cell polarity by regulating the Cdc42 guanine nucleotide exchange factor Gef1. Here, we show that Orb6 regulates polarity largely independently of Gef1 and that Orb6 positively regulates exocytosis. Through Orb6 inhibition in vivo and quantitative global phosphoproteomics, we identify Orb6 targets, including proteins involved in membrane trafficking. We confirm Sec3 and Sec5, conserved components of the exocyst complex, as substrates of Orb6 both in vivo and in vitro, and we show that Orb6 kinase activity is important for exocyst localization to cell tips and for exocyst activity during septum dissolution after cytokinesis. We further find that Orb6 phosphorylation of Sec3 contributes to exocyst function in concert with exocyst protein Exo70. We propose that Orb6 contributes to polarized growth by regulating membrane trafficking at multiple levels.","doi":"10.1016/j.celrep.2019.01.027","authors":"Tay YD, Leda M, Spanos C, Rappsilber J, Goryachev AB, Sawin KE","authors_abbrev":"Tay YD et al.","pubmed_publication_date":"05 Feb 2019","pubmed_entrez_date":"2019-02-07","publication_year":"2019","canto_session_key":"6d1f3a3caef131ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ye Dee Tay","canto_first_approved_date":"2019-08-18 18:14:03","canto_approved_date":"2026-04-16 06:18:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-31 13:21:18","canto_added_date":"2019-02-08 01:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie 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SPAC23G3.02c","SPAC22H12.03","SPBC691.04","SPAC2G11.05c","SPAC644.06c","SPBC215.15","SPAC1F3.07c","SPAC4A8.16c","SPAC9E9.14","SPBC16D10.09","SPAC139.06","SPCC1494.05c","SPCC330.07c","SPBC660.07","SPAC1783.06c","SPAC30C2.07","SPAC17C9.15c","SPBC1539.09c","SPAC17H9.07","SPBC1703.14c","SPCC794.07","SPCC285.16c","SPACUNK4.11c","SPCC594.01","SPBC30D10.18c","SPAC890.07c","SPBC1683.03c","SPAC30C2.04","SPBP8B7.03c","SPCC1682.02c","SPCC188.07","SPAC1F7.07c","SPAC1786.01c","SPAC27E2.03c","SPAC1093.06c","SPBC26H8.04c","SPAC23C4.13","SPAC9.12c","SPBP19A11.03c","SPAC17D4.02","SPAC17H9.06c","SPAC17C9.03","SPCC1795.12c","SPAC13G6.02c","SPBC4B4.07c","SPCC1442.08c","SPBC14C8.15","SPAC23D3.01","SPBC1683.10c","SPAPB2B4.07","SPAC2C4.12c","SPAC6G9.11","SPAC29A4.09","SPBC36B7.03","SPBC16H5.03c","SPBC428.10","SPAC26A3.14c","SPAC806.04c","SPCC1183.03c","SPAC23E2.01"],"gene_count":2521,"ltp_gene_count":5,"approved_date":"2019-08-18"},{"uniquename":"PMID:16891172","title":"Repair of topoisomerase I-mediated DNA damage.","citation":"Prog Nucleic Acid Res Mol Biol 2006;81:179-229","abstract":"Topoisomerase I (Top1) is an abundant and essential enzyme. Top1 is the selective target of camptothecins, which are effective anticancer agents. Top1-DNA cleavage complexes can also be trapped by various endogenous and exogenous DNA lesions including mismatches, abasic sites and carcinogenic adducts. Tyrosyl-DNA phosphodiesterase (Tdp1) is one of the repair enzymes for Top1-DNA covalent complexes. Tdp1 forms a multiprotein complex that includes poly(ADP) ribose polymerase (PARP). PARP-deficient cells are hypersensitive to camptothecins and functionally deficient for Tdp1. We will review recent developments in several pathways involved in the repair of Top1 cleavage complexes and the role of Chk1 and Chk2 checkpoint kinases in the cellular responses to Top1 inhibitors. The genes conferring camptothecin hypersensitivity are compiled for humans, budding yeast and fission yeast.","authors":"Pommier Y, Barcelo JM, Rao VA, Sordet O, Jobson AG, Thibaut L, Miao ZH, Seiler JA, Zhang H, Marchand C, Agama K, Nitiss JL, Redon C","authors_abbrev":"Pommier Y et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-08-08","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-11-23 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1464319","title":"Negative regulation of mitosis by two functionally overlapping PTPases in fission yeast.","citation":"EMBO J 1992 Dec;11(13):4943-52","abstract":"We have identified a third protein tyrosine phosphatase (PTPase) gene in fission yeast, pyp2, encoding an 85 kDa protein. Disruption of pyp2 has no impact on cell viability, but pyp2 is essential in strains lacking the 60 kDa pyp1 PTPase. The two pyp PTPases are approximately 42% identical in their C-terminal catalytic domains and share weak homology in their N-terminal regions. Both genes play a role in inhibiting the onset of mitosis. Disruption of either gene rescues the G2 arrest caused by mutation of the cdc25 mitotic inducer, though the effect of pyp1-disruption is more pronounced. Disruption of pyp1 advances mitosis, suppresses overexpression of the tyrosine kinase encoded by the wee1 mitotic inhibitor, and causes lethal mitotic catastrophe in cdc25 overproducer cells. Cells bearing inactive wee1 are unresponsive to disruption of pyp1. Overexpression of pyp1 or pyp2 delays the onset of mitosis by a wee1-dependent mechanism. These data reveal an unexpected second role for protein tyrosine phosphorylation in the mitotic control that acts by promoting the inhibitory wee1 pathway.","authors":"Millar JB, Russell P, Dixon JE, Guan KL","authors_abbrev":"Millar JB et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"65c76fa511461156","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-04 13:32:28","canto_approved_date":"2026-01-31 16:05:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-09 17:10:47","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.09","SPAC24H6.05","SPCC18B5.03","SPAC26F1.10c","SPAC19D5.01","SPAC644.06c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-08-04"},{"uniquename":"PMID:22682245","title":"The intra-S phase checkpoint targets Dna2 to prevent stalled replication forks from reversing.","citation":"Cell 2012 Jun 08;149(6):1221-32","abstract":"When replication forks stall at damaged bases or upon nucleotide depletion, the intra-S phase checkpoint ensures they are stabilized and can restart. In intra-S checkpoint-deficient budding yeast, stalling forks collapse, and ∼10% form pathogenic chicken foot structures, contributing to incomplete replication and cell death (Lopes et al., 2001; Sogo et al., 2002; Tercero and Diffley, 2001). Using fission yeast, we report that the Cds1(Chk2) effector kinase targets Dna2 on S220 to regulate, both in vivo and in vitro, Dna2 association with stalled replication forks in chromatin. We demonstrate that Dna2-S220 phosphorylation and the nuclease activity of Dna2 are required to prevent fork reversal. Consistent with this, Dna2 can efficiently cleave obligate precursors of fork regression-regressed leading or lagging strands-on model replication forks. We propose that Dna2 cleavage of regressed nascent strands prevents fork reversal and thus stabilizes stalled forks to maintain genome stability during replication stress.","doi":"10.1016/j.cell.2012.04.030","authors":"Hu J, Sun L, Shen F, Chen Y, Hua Y, Liu Y, Zhang M, Hu Y, Wang Q, Xu W, Sun F, Ji J, Murray JM, Carr AM, Kong D","authors_abbrev":"Hu J et al.","pubmed_publication_date":"08 Jun 2012","pubmed_entrez_date":"2012-06-12","publication_year":"2012","canto_session_key":"4aff66ed2ed54ace","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-06 15:26:59","canto_approved_date":"2025-09-04 06:38:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-21 10:46:07","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":43,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.21c","SPBC216.05","SPBC16D10.04c","SPBC685.09","SPCC18B5.11c","SPAC3H5.06c","SPAC17D4.02"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2015-07-06"},{"uniquename":"PMID:26265703","title":"The Spontaneous Mutation Rate in the Fission Yeast Schizosaccharomyces pombe.","citation":"Genetics 2015 Oct;201(2):737-44","abstract":"The rate at which new mutations arise in the genome is a key factor in the evolution and adaptation of species. Here we describe the rate and spectrum of spontaneous mutations for the fission yeast Schizosaccharomyces pombe, a key model organism with many similarities to higher eukaryotes. We undertook an ∼1700-generation mutation accumulation (MA) experiment with a haploid S. pombe, generating 422 single-base substitutions and 119 insertion-deletion mutations (indels) across the 96 replicates. This equates to a base-substitution mutation rate of 2.00 × 10(-10) mutations per site per generation, similar to that reported for the distantly related budding yeast Saccharomyces cerevisiae. However, these two yeast species differ dramatically in their spectrum of base substitutions, the types of indels (S. pombe is more prone to insertions), and the pattern of selection required to counteract a strong AT-biased mutation rate. Overall, our results indicate that GC-biased gene conversion does not play a major role in shaping the nucleotide composition of the S. pombe genome and suggest that the mechanisms of DNA maintenance may have diverged significantly between fission and budding yeasts. Unexpectedly, CpG sites appear to be excessively liable to mutation in both species despite the likely absence of DNA methylation.","doi":"10.1534/genetics.115.177329","authors":"Farlow A, Long H, Arnoux S, Sung W, Doak TG, Nordborg M, Lynch M","authors_abbrev":"Farlow A et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2015-08-13","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-08-14 00:19:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7764684","title":"Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae.","citation":"Biotechnology (N Y) 1994 Apr;12(4):381-4","abstract":"Overexpression of protein disulfide isomerase (PDI) from a single chromosomally integrated copy in Saccharomyces cerevisiae results in ten-fold higher levels of secretion of human platelet derived growth factor B homodimer, and a four-fold increase in secretion of Schizosaccharomyces pombe acid phosphatase. This result provides evidence that inefficient protein folding limits the secretion of some heterologous proteins, and that manipulation of the endoplasmic reticulum lumenal environment can help overcome this limitation.","authors":"Robinson AS, Hines V, Wittrup KD","authors_abbrev":"Robinson AS et al.","pubmed_publication_date":"Apr 1994","pubmed_entrez_date":"1994-04-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19596787","title":"A Cds1-mediated checkpoint protects the MBF activator Rep2 from ubiquitination by anaphase-promoting complex/cyclosome-Ste9 at S-phase arrest in fission yeast.","citation":"Mol Cell Biol 2009 Sep;29(18):4959-70","abstract":"Transcription of the MluI cell cycle box (MCB) motif-containing genes at G(1) phase is regulated by the MCB-binding factors (MBF) (also called DSC1) in Schizosaccharomyces pombe. Upon S-phase arrest, the MBF transcriptional activity is induced through the accumulation of the MBF activator Rep2. In this study, we show that the turnover of Rep2 is attributable to ubiquitin-mediated proteolysis. Levels of Rep2 oscillate during the cell cycle, with a peak at G(1) phase, coincident with the MBF activity. Furthermore, we show that Rep2 ubiquitination requires the function of the E3 ligase anaphase-promoting complex/cyclosome (APC/C). Ste9 can be phosphorylated by the checkpoint kinase Cds1 in vitro, and its inhibition/phosphorylation at S-phase arrest is dependent on the function of Cds1. Our data indicate that the Cds1-dependent stabilization of Rep2 is achieved through the inhibition/phosphorylation of APC/C-Ste9 at the onset of S-phase arrest. Stabilization of Rep2 is important for stimulating transcription of the MBF-dependent genes to ensure a sufficient supply of proteins essential for cell recovery from S-phase arrest. We propose that oscillation of Rep2 plays a role in regulation of periodic transcription of the MBF-dependent genes during cell cycle progression.","doi":"10.1128/MCB.00562-09","authors":"Chu Z, Eshaghi M, Poon SY, Liu J","authors_abbrev":"Chu Z et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-07-15","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25239486","title":"Schizosaccharomyces pombe: a novel transport vehicle of functional DNA and mRNA into mammalian antigen-presenting cells.","citation":"Vaccine 2014 Oct 21;32(46):6029-33","abstract":"Vaccine vehicles based on recombinant yeasts have become promising candidates for the induction of cellular immune responses. In this study, we investigated the capacity of the fission yeast Sz. pombe for the delivery of functional nucleic acids into murine and human antigen-presenting cells. We demonstrate that Sz. pombe cells effectively induce maturation of human dendritic cells (DC), an important prerequisite for T-cell activation. Further, recombinant fission yeast efficiently delivers functional DNA and mRNA into murine macrophages and human DC resulting in the expression of the model antigen eGFP in these cells. Thus, Sz. pombe suggests itself as a promising candidate for a novel live vaccine.","doi":"10.1016/j.vaccine.2014.09.011","authors":"Walch-Rückheim B, Schmitt MJ, Breinig F","authors_abbrev":"Walch-Rückheim B et al.","pubmed_publication_date":"21 Oct 2014","pubmed_entrez_date":"2014-09-21","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-09-24 00:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12242289","title":"The 14-3-3 proteins Rad24 and Rad25 negatively regulate Byr2 by affecting its localization in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2002 Oct;22(20):7105-19","abstract":"In Schizosaccharomyces pombe, rad24 and rad25 have been identified to be homologous to mammalian 14-3-3 genes and found to be involved in many cellular events, including checkpoint and meiosis. In the present study, we present evidences that Rad24 and Rad25 act as negative regulators of Byr2 (mitogen-activated protein kinase [MAPK] kinase kinase). Overexpression of rad24 or rad25 reduced mating and sporulation in homothallic wild-type cells. In contrast, the mating and sporulation efficiency of rad24- or rad25-null cells was higher than that of wild-type cells. Deletion of rad24 or rad25 increased sporulation efficiency in ras1-null diploid cells but not in byr2-, ste4-, byr1-, and spk1-null cells. Rad24 and Rad25 had no effect on the activity of constitutively active Byr1(S214DT218D). Rad24 and Rad25 bound to both the N-terminal and the C-terminal domains of Byr2 when these bacterially expressed proteins were examined. The formation of complexes in vivo between Byr2 and either Rad24 or Rad25 was also confirmed by immunocoprecipitation. Furthermore, we showed negative regulation of Byr2 by Rad25, by monitoring the mRNA level of mam2, which is regulated by both the Ras1/MAPK pathway and ste11, in various combinations of mutants. In addition, the cellular localization of Byr2 in living cells was observed by using fusion to green fluorescent protein. Byr2 was mainly localized in the cytoplasm during vegetative growth and then concentrated at the plasma membrane in response to nitrogen starvation. Deletion of rad24 or rad25 fastened the timing of Byr2 translocation. Our results are consistent with the hypothesis that one of the roles of 14-3-3 is to keep Byr2 in the cytoplasm and to affect the timing of Byr2 translocation in response to sexual developmental signal.","authors":"Ozoe F, Kurokawa R, Kobayashi Y, Jeong HT, Tanaka K, Sen K, Nakagawa T, Matsuda H, Kawamukai M","authors_abbrev":"Ozoe F et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-09-21","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPBC1D7.05","SPAC17H9.09c","SPAC17A2.13c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:4077736","title":"Leptomycins A and B, new antifungal antibiotics. III. Mode of action of leptomycin B on Schizosaccharomyces pombe.","citation":"J Antibiot (Tokyo) 1985 Nov;38(11):1573-80","abstract":"Mode of action of leptomycin B (LMB), a new antifungal antibiotic, was studied with Schizosaccharomyces pombe. A low concentration of LMB caused inhibition of cell division, producing elongated cells with morphologically altered nuclei and several cell plates, while it inhibited nucleic acid synthesis in intact cells at 100-fold higher concentration. Addition of LMB during G2 phase in synchronous culture blocked following events in cell cycle. Analysis of the effect of LMB on cdc mutants suggested the antibiotic inhibited some specific step, possibly in M phase just prior to nuclear division.","authors":"Hamamoto T, Uozumi T, Beppu T","authors_abbrev":"Hamamoto T et al.","pubmed_publication_date":"Nov 1985","pubmed_entrez_date":"1985-11-01","publication_year":"1985","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39918318","title":"Polysulfides promote protein disulfide bond formation in microorganisms growing under anaerobic conditions.","citation":"Appl Environ Microbiol 2025 Feb 07;:e0192624","abstract":"Polysulfides commonly occur in anaerobic, microbial active environments, where they play key roles in sulfur cycling and redox transformations. Anaerobic survival of microorganisms requires the formation of protein disulfide bond (DSB). The relationship between polysulfides and anaerobic DSB formation has not been studied so far. Herein, we discovered that polysulfides can efficiently mediate protein DSB formation of microorganisms under anaerobic conditions. We used polysulfides to treat proteins, including roGFP2, Trx1, and DsbA, under anaerobic conditions and found that all three proteins formed intramolecular DSB  in vitro . Under anaerobic conditions,  Escherichia coli  Δ dsbB  displayed reduced growth and decreased intracellular protein DSB levels, but polysulfide treatment restored both growth and DSB content. Similarly, polysulfide treatment of  E. coli  Δ dsbA  promoted periplasmic roGFP2 DSB formation and recovered growth under anaerobic conditions. Furthermore, treating  Schizosaccharomyces pombe  and  Cupriavidus pinatubonensis  JMP134 with polysulfides increased their intracellular protein DSB content. Collectively, these findings demonstrate that polysulfides can promote DSB formation independently of known enzymatic DSB-mediated systems and the presence of oxygen, thereby benefiting the survival of microorganisms in anaerobic habitats.IMPORTANCEHow polysulfides enhance the adaption of microorganisms to anaerobic environments remains unclear. Our study reveals that polysulfides efficiently facilitate protein DSB formation under anaerobic conditions. Polysulfides contain zero-valent sulfur atoms (S 0 ), which can be transferred to the thiol group of cysteine residue. This S 0  atom then accepts two electrons from two cysteine residues and is reduced to H 2 S, leaving the two cysteines linked by a disulfide bond. Anaerobic growth of microorganisms benefits from the formation of DSB. These findings pave the way for a deeper understanding of the intricate relationship between polysulfides and microorganisms in various environmental contexts.","doi":"10.1128/aem.01926-24","authors":"Xin Y, Wang Q, Yang J, Wu X, Xia Y, Xun L, Liu H","authors_abbrev":"Xin Y et al.","pubmed_publication_date":"07 Feb 2025","pubmed_entrez_date":"2025-02-07","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-02-08 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24727291","title":"A genome-wide screen for sporulation-defective mutants in Schizosaccharomyces pombe.","citation":"G3 (Bethesda) 2014 Apr 11;4(6):1173-82","abstract":"Yeast sporulation is a highly regulated developmental program by which diploid cells generate haploid gametes, termed spores. To better define the genetic pathways regulating sporulation, a systematic screen of the set of ~3300 nonessential Schizosaccharomyces pombe gene deletion mutants was performed to identify genes required for spore formation. A high-throughput genetic method was used to introduce each mutant into an h(90) background, and iodine staining was used to identify sporulation-defective mutants. The screen identified 34 genes whose deletion reduces sporulation, including 15 that are defective in forespore membrane morphogenesis. In S. pombe, the total number of sporulation-defective mutants is a significantly smaller fraction of coding genes than in S. cerevisiae, which reflects the different evolutionary histories and biology of the two yeasts.","doi":"10.1534/g3.114.011049","authors":"Ucisik-Akkaya E, Leatherwood JK, Neiman AM","authors_abbrev":"Ucisik-Akkaya E et al.","pubmed_publication_date":"11 Apr 2014","pubmed_entrez_date":"2014-04-15","publication_year":"2014","canto_session_key":"9aa63f21e3aaee68","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-17 08:41:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-17 08:40:55","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":61,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_24727291_phaf.tsv"}],"genes":["SPAC5D6.08c","SPBP4H10.05c","SPAC821.06","SPBC146.02","SPAC11H11.04","SPAC17A5.08","SPCC11E10.08","SPBC12C2.07c","SPBC32H8.11","SPAC6C3.06c","SPAP11E10.02c","SPBC215.03c","SPAC6G9.04","SPBC25B2.02c","SPBC119.04","SPBC30B4.01c","SPAC1F3.06c","SPAC23C11.08","SPBC29A10.02","SPBC1711.12","SPAPB17E12.04c","SPAC607.10","SPAC22H12.05c","SPAC27D7.03c","SPBP4H10.11c","SPAPB1E7.02c","SPAC17H9.19c","SPCC1739.04c","SPAC30C2.02","SPBC18E5.08","SPBC21C3.18","SPCC553.04","SPAP7G5.03","SPBC3B8.02","SPAC19G12.15c","SPAC1783.06c","SPBC16E9.09c"],"gene_count":37,"ltp_gene_count":7,"approved_date":"2014-10-17"},{"uniquename":"PMID:8535288","title":"Transformation of cadmium-binding complexes during cadmium sequestration in fission yeast.","citation":"Biochem Mol Biol Int 1995 Aug;36(6):1169-75","abstract":"Fission yeast responded to environmental cadmium by producing a family of small Cd-binding peptides, phytochelatins (PCn). A low molecular weight (LMW) complex essentially composed of PC2, and PC3 was produced and then disappeared gradually in 24 hrs after Cd treatment, which served as a transient form for a temporary but quick relief of Cd in the cytosoL It had been reported that the LMW complex was further transported into the vacuole by an ABC-type protein (HMT1), and a higher molecular weight (HMW) complex was formed in the vacuole. Results from gel filtration chromatography and HPLC analysis showed that the transformation of the LMW to the HMW complex was accompanied with a rearrangement of its PCn component. Besides, the molecular conformation of the HMW complex changed from a relaxed form in the early stage to a more condensed conformation during cell aging. And the transformation of the LMW into the HMW complex by the addition of sulfide in the test tube was demonstrated.","authors":"Wu JS, Sung HY, Juang RH","authors_abbrev":"Wu JS et al.","pubmed_publication_date":"Aug 1995","pubmed_entrez_date":"1995-08-01","publication_year":"1995","canto_triage_status":"Structure","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7559598","title":"Regulation of calcineurin gene expression in Schizosaccharomyces pombe. Dependence on the ste11 transcription factor.","citation":"J Biol Chem 1995 Oct 20;270(42):24794-9","abstract":"Calmodulin and its target enzymes are important regulators of numerous cellular processes, including reversible protein phosphorylation. The calmodulin-dependent protein phosphatase (calcineurin) has been suggested to play roles in activation of T cells and in the mating response of yeast. Recently, studies have shown it to be the target of immunosuppressant drugs such as cyclosporin and FK-506. In this study, we have cloned the gene for the catalytic subunit of calcineurin, CnA, from the yeast Schizosaccharomyces pombe. The gene (named ppb1+) has been mapped to chromosome II by analysis of the hybridization of a genomic DNA probe to an ordered library. The gene produces a single mRNA species of 2.5 kilobases, which varies during the cell cycle in exponentially growing cells. In addition, expression of ppb1+ mRA is induced by nitrogen starvation, a condition that favors mating in S. pombe. The ppb1+ gene promoter contains a cis-acting element for the ste11 transcription factor, and we have shown that induction of the ppb1+ mRNA during nitrogen starvation is dependent on the ste11 gene product. Together with earlier studies showing that disruption of the ppb1+ gene in S. pombe results in sterility (Yoshida, T., Toda, T., and Yanagida, M. (1994) J. Cell Sci., 107, 1725-1735), our studies suggest that the ppb1+ gene plays a role in the gene expression cascade that is essential for mating and sporulation in S. pombe.","authors":"Plochocka-Zulinska D, Rasmussen G, Rasmussen C","authors_abbrev":"Plochocka-Zulinska D et al.","pubmed_publication_date":"20 Oct 1995","pubmed_entrez_date":"1995-10-20","publication_year":"1995","canto_session_key":"133b9a4cefba1a78","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-08 09:53:32","canto_approved_date":"2023-04-20 11:25:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-08 09:53:27","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPBP4H10.04"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-11-08"},{"uniquename":"PMID:34761070","title":"A Rapid Induction Overexpression System for the Fission Yeast  Schizosaccharomyces pombe .","citation":"Bio Protoc 2021 Oct 20;11(20):e4198","abstract":"The fission yeast  Schizosaccharomyces pombe  is an excellent genetically tractable model organism used in the study of conserved eukaryotic cellular biology. One genetic tool in the assessment of gene function is the  in vivo  overexpression of proteins. Existing overexpression tools have limitations of induction kinetics, dynamic range, and/or system-wide changes due to the induction conditions or inducer. Here, I describe the methodology for the use of a plasmid-based long non-coding RNA (lncRNA)-regulated overexpression system that is induced by the addition of thiamine. This system, termed the pTIN-system ( t hiamine  in ducible), utilizes the fast repression kinetics of the thiamine-regulated  nmt1   +  promoter integrated with the lncRNA regulated  tgp1   +  promoter. The advantages of the pTIN-system are rapid induction kinetics of gene expression, broad dynamic range, and tunable expression.","authors":"Garg A","authors_abbrev":"Garg A","pubmed_publication_date":"20 Oct 2021","pubmed_entrez_date":"2021-11-11","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-11-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25981630","title":"Minimum network constraint on reverse engineering to develop biological regulatory networks.","citation":"J Theor Biol 2015 Sep 07;380:9-15","abstract":"Reconstructing the topological structure of biological regulatory networks from microarray expression data or data of protein expression profiles is one of major tasks in systems biology. In recent years, various mathematical methods have been developed to meet this task. Here, based on our previously reported reverse engineering method, we propose a new constraint, i.e., the minimum network constraint, to facilitate the reconstruction of biological networks. Three well studied regulatory networks (the budding yeast cell cycle network, the fission yeast cell cycle network, and the SOS network of Escherichia coli) were used as the test sets to verify the performance of this method. Numerical results show that the biological networks prefer to use the minimal networks to fulfill their functional tasks, making it possible to apply minimal network criteria in the network reconstruction process. Two scenarios were considered in the reconstruction process: generating data using different initial conditions; and generating data from knock out and over-expression experiments. In both cases, network structures are revealed faithfully in a few steps using our approach.","doi":"10.1016/j.jtbi.2015.05.005","authors":"Shao B, Wu J, Tian B, Ouyang Q","authors_abbrev":"Shao B et al.","pubmed_publication_date":"07 Sep 2015","pubmed_entrez_date":"2015-05-19","publication_year":"2015","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2015-05-21 00:19:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR14369","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:11478","SPAC8C9.10c","SPBC947.07"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:26404838","title":"Arrested replication forks guide retrotransposon integration.","citation":"Science 2015 Sep 25;349(6255):1549-53","abstract":"Long terminal repeat (LTR) retrotransposons are an abundant class of genomic parasites that replicate by insertion of new copies into the host genome. Fungal LTR retrotransposons prevent mutagenic insertions through diverse targeting mechanisms that avoid coding sequences, but conserved principles guiding their target site selection have not been established. Here, we show that insertion of the fission yeast LTR retrotransposon Tf1 is guided by the DNA binding protein Sap1 and that the efficiency and location of the targeting depend on the activity of Sap1 as a replication fork barrier. We propose that Sap1 and the fork arrest it causes guide insertion of Tf1 by tethering the integration complex to target sites.","doi":"10.1126/science.aaa3810","authors":"Jacobs JZ, Rosado-Lugo JD, Cranz-Mileva S, Ciccaglione KM, Tournier V, Zaratiegui M","authors_abbrev":"Jacobs JZ et al.","pubmed_publication_date":"25 Sep 2015","pubmed_entrez_date":"2015-09-26","publication_year":"2015","canto_session_key":"800a3d249c222a4d","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-09-27 00:18:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26689777","title":"Tor Signaling Regulates Transcription of Amino Acid Permeases through a GATA Transcription Factor Gaf1 in Fission Yeast.","citation":"PLoS One 2015;10(12):e0144677","abstract":"In the fission yeast, two Tor isoforms, Tor1 and Tor2, oppositely regulate gene expression of amino acid permeases. To elucidate the transcriptional machinery for these regulations, here we have employed the cap analysis of gene expression (CAGE), a method of analyzing expression profiles and identifying transcriptional start sites (TSSs). The loss of Tor1 decreased, and Tor2 inhibition by its temperature sensitive mutation increased, mRNA expression of isp5+, per1+, put4+ and SPBPB2B2.01. In contrast, the loss of Tor1 increased, and Tor2 inhibition decreased, the expression of cat1+. These changes were confirmed by semi-quantitative RT-PCR. These opposite effects by the loss of Tor1 and Tor2 inhibition appeared to occur evenly across multiple TSSs for the respective genes. The motif discovery analysis based on the CAGE results identified the GATA motifs as a potential cis-regulatory element for Tor-mediated regulation. In the luciferase reporter assay, the loss of Tor1 reduced, and Tor2 inhibition and nitrogen depletion increased, the activity of isp5+ promoter as well as that of a GATAAG reporter. One of the GATAAG motifs in isp5+ promoter was critical for its transcriptional activity, and a GATA transcription factor Gaf1 was critical for the activities of isp5+ promoter and the GATAAG reporter. Furthermore, Tor2 inhibition and nitrogen depletion induced nuclear localization of Gaf1 from the cytosol and its dephosphorylation. These results suggest that Tor2 inhibition, which is known to be induced by nitrogen depletion, promotes nuclear localization of Gaf1, thereby inducing isp5+ transcription through Gaf1 binding to the GATAAG motif in its promoter. Since Gaf1 was also critical for transcription of per1+ and put4+, Tor-Gaf1 signaling may coordinate transcription of multiple amino acid permeases according to nutrient availability.","doi":"10.1371/journal.pone.0144677","authors":"Ma Y, Ma N, Liu Q, Qi Y, Manabe R, Furuyashiki T","authors_abbrev":"Ma Y et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-12-23","publication_year":"2015","canto_session_key":"2043cdfaa8bfef7c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2026-01-19 09:28:41","canto_approved_date":"2026-06-09 08:25:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-11-16 13:22:45","canto_added_date":"2015-12-24 01:19:42","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":203,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.05c","SPBC543.04","SPBC216.07c","SPAPB1E7.12","SPCC1902.01","SPCC777.05","SPAC13G6.07c","SPBC337.13c","SPAC23H3.03c","SPAC869.11","SPAC1039.09"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2026-01-19"},{"uniquename":"PMID:9705352","title":"Purification of Hsk1, a minichromosome maintenance protein kinase from fission yeast.","citation":"J Biol Chem 1998 Aug 21;273(34):22083-90","abstract":"Members of the Cdc7 family of protein kinases are essential for the initiation of DNA replication in all eukaryotes, but their precise biochemical function is unclear. We have purified the fission yeast Cdc7 homologue Hsk1 approximately 30,000-fold, to near homogeneity. Purified Hsk1 has protein kinase activity on several substrates and is capable of autophosphorylation. Point mutations in highly conserved regions of Hsk1 inactivate the kinase in vitro and in vivo. Overproduction of two of the mutant hsk1 alleles blocks initiation of DNA replication and deranges the mitotic checkpoint, a phenotype consistent with a role for Hsk1 in the early stages of initiation. The purified Hsk1 kinase can be separated into two active forms, a Hsk1 monomer and a heterodimer consisting of Hsk1 complexed with a co-purifying polypeptide, Dfp1. Association with Dfp1 stimulates phosphorylation of exogenous substrates but has little effect on autokinase activity. We have identified Dfp1 as the fission yeast homologue of budding yeast Dbf4. Purified Hsk1 phosphorylates the Cdc19 (Mcm2) subunit of the six-member minichromosome maintenance protein complex purified from fission yeast. Since minichromosome maintenance proteins have been implicated in the initiation of DNA replication, the essential function of Hsk1 at the G1/S transition may be mediated by phosphorylation of Cdc19. Furthermore, the phosphorylation of critical substrates by Hsk1 kinase is likely regulated by association with a Dbf4-like co-factor.","authors":"Brown GW, Kelly TJ","authors_abbrev":"Brown GW et al.","pubmed_publication_date":"21 Aug 1998","pubmed_entrez_date":"1998-08-15","publication_year":"1998","canto_session_key":"f176723226a4e520","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-27 14:36:50","canto_approved_date":"2021-03-22 16:09:57","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-10-31 13:22:05","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25D12.03c","SPBC776.12c","SPCC16A11.17","SPCC1682.02c","SPCC550.13","SPAC1B2.05","SPBC4.04c","SPBC211.04c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-11-27"},{"uniquename":"PMID:28982178","title":"Filamentous invasive growth of mutants of the genes encoding ammonia-metabolizing enzymes in the fission yeast Schizosaccharomyces pombe.","citation":"PLoS One 2017;12(10):e0186028","abstract":"The fission yeast Schizosaccharomyces pombe undergoes a switch from yeast to filamentous invasive growth in response to certain environmental stimuli. Among them is ammonium limitation. Amt1, one of the three ammonium transporters in this yeast, is required for the ammonium limitation-induced morphological transition; however, the underlying molecular mechanism remains to be understood. Cells lacking Amt1 became capable of invasive growth upon increasing concentrations of ammonium in the medium, suggesting that the ammonium taken up into the cell or a metabolic intermediate in ammonium assimilation might serve as a signal for the ammonium limitation-induced morphological transition. To investigate the possible role of ammonium-metabolizing enzymes in the signaling process, deletion mutants were constructed for the gdh1, gdh2, gln1, and glt1 genes, which were demonstrated by enzyme assays to encode NADP-specific glutamate dehydrogenase, NAD-specific glutamate dehydrogenase, glutamine synthetase, and glutamate synthase, respectively. Growth tests on various nitrogen sources revealed that a gln1Δ mutant was a glutamine auxotroph and that a gdh1Δ mutant had a defect in growth on ammonium, particularly at high concentrations. The latter observation indicates that the NADP-specific glutamate dehydrogenase of S. pombe plays a major role in ammonium assimilation under high ammonium concentrations. Invasive growth assays showed that gdh1Δ and glt1Δ mutants underwent invasive growth to a lesser extent than did wild-type strains. Increasing the ammonium concentration in the medium suppressed the invasive growth defect of the glt1Δ mutant, but not the gdh1Δ mutant. These results suggest that the nitrogen status of the cell is important in the induction of filamentous invasive growth in S. pombe.","doi":"10.1371/journal.pone.0186028","authors":"Sasaki Y, Kojima A, Shibata Y, Mitsuzawa H","authors_abbrev":"Sasaki Y et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-10-06","publication_year":"2017","canto_session_key":"d272c70052e00b9c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroshi Mitsuzawa","canto_first_approved_date":"2018-03-09 16:05:51","canto_approved_date":"2025-06-29 07:11:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-28 01:58:19","canto_added_date":"2017-10-07 00:15:47","annotation_curators":[{"name":"Hiroshi Mitsuzawa","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H4.06","SPAPB1E7.07","SPCC622.12c","SPCC132.04c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-03-09"},{"uniquename":"PMID:27020743","title":"Local Pheromone Release from Dynamic Polarity Sites Underlies Cell-Cell Pairing during Yeast Mating.","citation":"Curr Biol 2016 Apr 25;26(8):1117-25","abstract":"Cell pairing is central for many processes, including immune defense, neuronal connection, hyphal fusion, and sexual reproduction. How does a cell orient toward a partner, especially when faced with multiple choices? Fission yeast Schizosaccharomyces pombe P and M cells, which respectively express P and M factor pheromones [1, 2], pair during the mating process induced by nitrogen starvation. Engagement of pheromone receptors Map3 and Mam2 [3, 4] with their cognate pheromone ligands leads to activation of the Gα protein Gpa1 to signal sexual differentiation [3, 5, 6]. Prior to cell pairing, the Cdc42 GTPase, a central regulator of cell polarization, forms dynamic zones of activity at the cell periphery at distinct locations over time [7]. Here we show that Cdc42-GTP polarization sites contain the M factor transporter Mam1, the general secretion machinery, which underlies P factor secretion, and Gpa1, suggesting that these are sub-cellular zones of pheromone secretion and signaling. Zone lifetimes scale with pheromone concentration. Computational simulations of pair formation through a fluctuating zone show that the combination of local pheromone release and sensing, short pheromone decay length, and pheromone-dependent zone stabilization leads to efficient pair formation. Consistently, pairing efficiency is reduced in the absence of the P factor protease. Similarly, zone stabilization at reduced pheromone levels, which occurs in the absence of the predicted GTPase-activating protein for Ras, leads to reduction in pairing efficiency. We propose that efficient cell pairing relies on fluctuating local signal emission and perception, which become locked into place through stimulation.","doi":"10.1016/j.cub.2016.02.064","authors":"Merlini L, Khalili B, Bendezú FO, Hurwitz D, Vincenzetti V, Vavylonis D, Martin SG","authors_abbrev":"Merlini L et al.","pubmed_publication_date":"25 Apr 2016","pubmed_entrez_date":"2016-03-30","publication_year":"2016","canto_session_key":"43bea869ed339006","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_approved_date":"2016-12-01 14:49:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-11-15 15:53:33","canto_added_date":"2016-03-31 00:15:22","annotation_curators":[{"name":"Sophie Martin","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25B2.02c","SPAC11H11.04","SPAC18G6.03","SPAC1296.03c","SPBC24C6.06","SPBC646.12c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-11-15"},{"uniquename":"PMID:37160462","title":"Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components.","citation":"Cell Mol Life Sci 2023 May 09;80(6):143","abstract":"In terms of its relative frequency, lysine is a common amino acid in the human proteome. However, by bioinformatics we find hundreds of proteins that contain long and evolutionarily conserved stretches completely devoid of lysine residues. These so-called lysine deserts show a high prevalence in intrinsically disordered proteins with known or predicted functions within the ubiquitin-proteasome system (UPS), including many E3 ubiquitin-protein ligases and UBL domain proteasome substrate shuttles, such as BAG6, RAD23A, UBQLN1 and UBQLN2. We show that introduction of lysine residues into the deserts leads to a striking increase in ubiquitylation of some of these proteins. In case of BAG6, we show that ubiquitylation is catalyzed by the E3 RNF126, while RAD23A is ubiquitylated by E6AP. Despite the elevated ubiquitylation, mutant RAD23A appears stable, but displays a partial loss of function phenotype in fission yeast. In case of UBQLN1 and BAG6, introducing lysine leads to a reduced abundance due to proteasomal degradation of the proteins. For UBQLN1 we show that arginine residues within the lysine depleted region are critical for its ability to form cytosolic speckles/inclusions. We propose that selective pressure to avoid lysine residues may be a common evolutionary mechanism to prevent unwarranted ubiquitylation and/or perhaps other lysine post-translational modifications. This may be particularly relevant for UPS components as they closely and frequently encounter the ubiquitylation machinery and are thus more susceptible to nonspecific ubiquitylation.","doi":"10.1007/s00018-023-04782-z","authors":"Kampmeyer C, Grønbæk-Thygesen M, Oelerich N, Tatham MH, Cagiada M, Lindorff-Larsen K, Boomsma W, Hofmann K, Hartmann-Petersen R","authors_abbrev":"Kampmeyer C et al.","pubmed_publication_date":"09 May 2023","pubmed_entrez_date":"2023-05-09","publication_year":"2023","canto_session_key":"b924eeaf3c11e580","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_first_approved_date":"2023-09-04 20:57:35","canto_approved_date":"2025-09-04 12:22:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-09-04 07:33:29","canto_added_date":"2023-05-11 00:15:04","annotation_curators":[{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-09-04"},{"uniquename":"PMID:17296299","title":"Pombe Cdc15 homology (PCH) proteins: coordinators of membrane-cytoskeletal interactions.","citation":"Trends Cell Biol 2007 Mar;17(3):145-56","abstract":"Cellular adhesion, motility, endocytosis, exocytosis and cytokinesis involve the coordinated reorganization of the cytoskeleton and of the plasma membrane. The 'Pombe Cdc15 homology' (PCH) family of adaptor proteins has recently been shown to coordinate the membrane and cytoskeletal dynamics involved in these processes by curving membranes, recruiting dynamin and controlling the architecture of the actin cytoskeleton. Mutations in PCH family members or proteins that interact with them are associated with autoinflammatory, neurological or neoplastic diseases. Here, we review the nature, actions and disease associations of the vertebrate PCH family members, highlighting their fundamental roles in the regulation of processes involving membrane-cytoskeletal interactions.","authors":"Chitu V, Stanley ER","authors_abbrev":"Chitu V et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-02-14","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24006488","title":"The DNA damage and the DNA replication checkpoints converge at the MBF transcription factor.","citation":"Mol Biol Cell 2013 Nov;24(21):3350-7","abstract":"In fission yeast cells, Cds1 is the effector kinase of the DNA replication checkpoint. We previously showed that when the DNA replication checkpoint is activated, the repressor Yox1 is phosphorylated and inactivated by Cds1, resulting in activation of MluI-binding factor (MBF)-dependent transcription. This is essential to reinitiate DNA synthesis and for correct G1-to-S transition. Here we show that Cdc10, which is an essential part of the MBF core, is the target of the DNA damage checkpoint. When fission yeast cells are treated with DNA-damaging agents, Chk1 is activated and phosphorylates Cdc10 at its carboxy-terminal domain. This modification is responsible for the repression of MBF-dependent transcription through induced release of MBF from chromatin. This inactivation of MBF is important for survival of cells challenged with DNA-damaging agents. Thus Yox1 and Cdc10 couple normal cell cycle regulation in unperturbed conditions and the DNA replication and DNA damage checkpoints into a single transcriptional complex.","doi":"10.1091/mbc.E13-05-0257","authors":"Ivanova T, Alves-Rodrigues I, Gómez-Escoda B, Dutta C, DeCaprio JA, Rhind N, Hidalgo E, Ayté J","authors_abbrev":"Ivanova T et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-09-06","publication_year":"2013","canto_session_key":"17bd4722f4e3d0a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jose Ayte","canto_first_approved_date":"2018-08-16 15:53:22","canto_approved_date":"2025-05-27 14:44:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-28 16:15:58","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":42,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jose Ayte","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC14C8.07c","SPBC725.16","SPCC18B5.11c","SPAC17H9.19c","SPAC1F7.05","SPBC216.05","SPCC1259.13","SPBC21B10.13c","SPBC16A3.07c","SPAC22F3.09c"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2018-08-16"},{"uniquename":"PMID:27574536","title":"Fission yeast septation.","citation":"Commun Integr Biol 2016;9(4):e1189045","abstract":"In animal cells cytokinesis relies on the contraction of an actomyosin ring that pulls the plasma membrane to create a cleavage furrow, whose ingression finally divides the mother cell into two daughter cells. Fungal cells are surrounded by a tough and flexible structure called cell wall, which is considered to be the functional equivalent of the extracellular matrix in animal cells. Therefore, in addition to cleavage furrow ingression, fungal cytokinesis also requires the centripetal formation of a septum wall structure that develops between the dividing cells, whose genesis must be strictly coordinated with both the actomyosin ring closure and plasma membrane ingression. Here we briefly review what is known about the septum structure and composition in the fission yeast Schizosaccharomyces pombe, the recent progress about the relationship between septum biosynthesis and actomyosin ring constriction, and the importance of the septum and ring in the steady progression of the cleavage furrow.","doi":"10.1080/19420889.2016.1189045","authors":"Cortés JC, Ramos M, Osumi M, Pérez P, Ribas JC","authors_abbrev":"Cortés JC et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-08-31","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-09-01 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36943461","title":"Zinc homeostasis in Schizosaccharomyces pombe.","citation":"Arch Microbiol 2023 Mar 21;205(4):126","abstract":"Most metal ions such as iron, calcium, zinc, or copper are essential for all eukaryotes. Organisms must maintain homeostasis of these metal ions because excess or deficiency of metal ions could cause damage to organisms. The steady state of many metal ions such as iron and copper has been well studied in detail. However, how to regulate zinc homeostasis in Schizosaccharomyces pombe is still confusing. In this review, we provide an overview of the molecular mechanisms that how S. pombe is able to maintain the balance of zinc levels in the changes of environment. In response to high levels of zinc, the transcription factor Loz1 represses the expression of several genes involved in the acquisition of zinc. Meanwhile, the CDF family proteins transport excess zinc to the secretory pathway. When zinc levels are limited, Loz1 was inactivated and could not inhibit the expression of zinc acquisition genes, and zinc stored in the secretory pathway is released for use by the cells. Besides, other factors that regulate zinc homeostasis are also discussed.","doi":"10.1007/s00203-023-03473-4","authors":"Yao R, Li R, Huang Y","authors_abbrev":"Yao R et al.","pubmed_publication_date":"21 Mar 2023","pubmed_entrez_date":"2023-03-21","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-03-22 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25B8.19c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU009880","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31015410","title":"Nuclear membrane protein Lem2 regulates nuclear size through membrane flow.","citation":"Nat Commun 2019 Apr 23;10(1):1871","abstract":"The size of the membrane-bound nucleus scales with cell size in a wide range of cell types but the mechanisms determining overall nuclear size remain largely unknown. Here we investigate the role of fission yeast inner nuclear membrane proteins in determining nuclear size, and propose that the Lap2-Emerin-Man1 domain protein Lem2 acts as a barrier to membrane flow between the nucleus and other parts of the cellular membrane system. Lem2 deletion increases membrane flow into and out of the nuclear envelope in response to changes in membrane synthesis and nucleocytoplasmic transport, altering nuclear size. The endoplasmic reticulum protein Lnp1 acts as a secondary barrier to membrane flow, functionally compensating for lack of Lem2. We propose that this is part of the mechanism that maintains nuclear size proportional to cellular membrane content and thus to cell size. Similar regulatory principles may apply to other organelles in the eukaryotic subcellular membrane network.","doi":"10.1038/s41467-019-09623-x","authors":"Kume K, Cantwell H, Burrell A, Nurse P","authors_abbrev":"Kume K et al.","pubmed_publication_date":"23 Apr 2019","pubmed_entrez_date":"2019-04-25","publication_year":"2019","canto_session_key":"7bbe318b26434db4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2019-06-20 14:15:41","canto_approved_date":"2025-07-02 06:08:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-11 13:37:35","canto_added_date":"2019-04-26 00:15:04","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":30,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A11.05c","SPCC1620.07c","SPBC16A3.05c","SPBC3B8.10c","SPAC18G6.10","SPCC737.03c","SPAC14C4.05c","SPBC12D12.01"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2019-06-20"},{"uniquename":"PMID:1769544","title":"The novel gene trs1 encodes an essential protein for the transition from mitotic cell cycle to resting state in Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 1991 Nov 01;68(1):1-5","abstract":"A novel gene trs1 in the fission yeast Schizosaccharomyces pombe has been genetically defined. The trs1 mutant showed several intriguing phenotypes. Cells were sensitive to starvation and rapidly lost viability in the stationary phase; cells in the stationary phase were sensitive to heat shock. Some heat-shock proteins were not induced and the heat-shock response in log-phase cells was defective. These mutant phenotypes strongly suggest a vital function of the trs1 gene product for transition from the G1 to G0 phase on starvation and for the normal heat-shock response.","authors":"Kitamura K, Shimoda C","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"01 Nov 1991","pubmed_entrez_date":"1991-11-01","publication_year":"1991","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:703759","title":"Synergistic interaction between UV and ionizing radiation in wild-type Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1978 Aug 04;164(1):31-7","abstract":"A synergistic effect of combined UV and gamma-ray exposure was observed for inactivation of wild-type Schizosaccharomyces pombe. A recombinational repair process, known to be important in restitution of damage induced by both radiations, appears to be involved; a radiation-sensitive mutant defective in this repair pathway showed essentially no synergistic interaction between UV and gamma-rays. Recovery from the synergistic effect of pre-exposure in wild-type cells did not display the expected fast gamma-recovery and slow UV-recovery kinetics previously observed for regain of resistance to further exposure to the same radiation. Rather, UV-irradiated cells recovered quickly from synergistic inactivation on subsequent gamma-exposure, while gamma-irradiated cells recovered UV-resistance slowly. Recovery from synergism thus appears to reflect the nature of the second, and not the initial, radiation.","authors":"Gentner NE, Werner MM","authors_abbrev":"Gentner NE et al.","pubmed_publication_date":"04 Aug 1978","pubmed_entrez_date":"1978-08-04","publication_year":"1978","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16264237","title":"Silencing in yeast: identification of clr4 targets.","citation":"Methods Mol Biol 2006;317:287-98","abstract":"Efficient handling of multiple reactions is a crucial prerequisite for productive RNA differential display (DD) analysis. To identify transcriptional targets of the histone H3 Lys9-specific methyltransferase Clr4, we applied a multiformat modification of DD to compare between clr4+ and clr4- transcriptomes of Schizosaccaromyces pombe. As a result, 14 differentially expressed bands were identified among 720 polymerase chain reaction (PCR) studied. The content of these bands was then analyzed by cloning, sequencing, and Northern analysis. In the final stage of verification, four Clr4 targets were isolated based on their expression in six Clr4 chromo and SET domain mutant strains. The step-by-step description of the multiformat DD provided below includes RNA purification, cDNA synthesis, 96-well PCR, electrophoretic separation of PCR products, isolation of DNA fragments from differentially expressed bands, and verification of candidate genes by Northern analysis.","authors":"Ivanov SV, Ivanova AV","authors_abbrev":"Ivanov SV et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2005-11-03","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17762864","title":"Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins.","citation":"EMBO J 2007 Sep 19;26(18):4102-12","abstract":"The function of small ubiquitin-like modifier (SUMO)-binding proteins is key to understanding how SUMOylation regulates cellular processes. We identified two related Schizosaccharomyces pombe proteins, Rfp1 and Rfp2, each having an N-terminal SUMO-interacting motif (SIM) and a C-terminal RING-finger domain. Genetic analysis shows that Rfp1 and Rfp2 have redundant functions; together, they are essential for cell growth and genome stability. Mammalian RNF4, an active ubiquitin E3 ligase, is an orthologue of Rfp1/Rfp2. Rfp1 and Rfp2 lack E3 activity but recruit Slx8, an active RING-finger ubiquitin ligase, through a RING-RING interaction, to form a functional E3. RNF4 complements the growth and genomic stability defects of rfp1rfp2, slx8, and rfp1rfp2slx8 mutant cells. Both the Rfp-Slx8 complex and RNF4 specifically ubiquitylate artificial SUMO-containing substrates in vitro in a SUMO binding-dependent manner. SUMOylated proteins accumulate in rfp1rfp2 double-null cells, suggesting that Rfp/Slx8 proteins may promote ubiquitin-dependent degradation of SUMOylated targets. Hence, we describe a family of SIM-containing RING-finger proteins that potentially regulates eukaryotic genome stability through linking SUMO-interaction with ubiquitin conjugation.","authors":"Sun H, Leverson JD, Hunter T","authors_abbrev":"Sun H et al.","pubmed_publication_date":"19 Sep 2007","pubmed_entrez_date":"2007-09-01","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC343.18","SPAC19A8.10","SPBC365.06","SPBC3D6.11c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:10079326","title":"Transient inhibition of histone deacetylase activity overcomes silencing in the mating-type region in fission yeast.","citation":"Curr Genet 1999 Mar;35(2):82-7","abstract":"We have investigated the effects of inhibition of histone de-acetylase activity on silencing at the silent mating-type loci in fission yeast. Treatment of exponentially growing cells with the histone deacetylase inhibitor, trichostatin A (TSA), resulted in derepression of a marker gene inserted 150 bp distal from the silent mat3-M locus. The natural targets for the silencing mechanism in this region were only partially derepressed and the activation appeared to be asymmetric, i.e. the mat2-P cassette remained silent at concentrations that clearly partially derepressed the mat3-M cassette. We further noted that treatment of wild-type h90 cells resulted in the generation of altered sporulation phenotypes, indicating that the treatment affected the expression of mating-type genes and/or mating-type switching. The results are discussed in the light of recent accumulated data regarding the role of deacetylation for silencing in other species.","authors":"Olsson TG, Silverstein RA, Ekwall K, Sunnerhagen P","authors_abbrev":"Olsson TG et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-03-18","publication_year":"1999","canto_session_key":"e4d2c2cf0fb3634e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-06-15 20:58:00","canto_approved_date":"2024-06-15 20:58:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-13 14:22:36","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G9.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2024-06-15"},{"uniquename":"PMID:21333630","title":"Sde2: a novel nuclear protein essential for telomeric silencing and genomic stability in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2011 Mar 18;406(3):444-8","abstract":"Telomeres, specialized domains assembled at the ends of linear chromosomes, are essential for genomic stability in eukaryotes. The formation and maintenance of telomeres are governed by numerous factors such as telomeric repeats, telomere-binding proteins, heterochromatin proteins, and telomerase. Here, we report Sde2, a novel nuclear protein essential for telomeric silencing and genomic stability in the fission yeast Schizosaccharomyces pombe. A deficiency in sde2 results in the derepression of the ura4(+) gene inserted near telomeric repeats, and the noncoding transcripts from telomeric regions accumulate in sde2Δ cells. The loss of Sde2 function compromises transcriptional silencing at telomeres, and this silencing defect is accompanied by increased levels of acetylated histone H3K14 and RNA polymerase II occupancy at telomeres as well as reduced recruitment of the SNF2 ATPase/histone deacetylase-containing complex SHREC to telomeres. Deletion of sde2 also leads to a higher frequency of mitotic minichromosome loss, and sde2Δ cells often form asci that contain spores in abnormal numbers, shapes, or both. In addition, sde2Δ cells are highly sensitive to several stresses, including high/low temperatures, bleomycin, which induces DNA damage, and thiabendazole, a microtubule-destabilizing agent. Furthermore, Sde2 genetically interacts with the telomere regulators Taz1, Pof3, and Ccq1. These findings demonstrate that Sde2 cooperates with other telomere regulators to maintain functional telomeres, thereby preventing genomic instability.","doi":"10.1016/j.bbrc.2011.02.068","authors":"Sugioka-Sugiyama R, Sugiyama T","authors_abbrev":"Sugioka-Sugiyama R et al.","pubmed_publication_date":"18 Mar 2011","pubmed_entrez_date":"2011-02-22","publication_year":"2011","canto_session_key":"75d712cebd4a2bd1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-01-08 15:49:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-10 16:25:37","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.18c","SPAC16A10.07c","SPCC188.07","SPCC338.16","SPBC800.03","SPBP35G2.10"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2014-09-10"},{"uniquename":"PMID:41056333","title":"PP6 phosphatase and Elongator contribute to kinesin 5-dependent spindle assembly by controlling microtubule regulators levels.","citation":"PLoS Genet 2025 Oct;21(10):e1011596","abstract":"Eukaryotic chromosome segregation relies on the assembly of a bipolar machinery based on microtubules (MTs), named the mitotic spindle. Formation of the mitotic spindle follows a force balance mechanism that ensures the proper capture and separation of sister chromatids. Many proteins have been involved in the establishment of this force balance, although kinesin 5 is well recognized as the major outward pushing force generator, since its inactivation results in monopolar, non-functional spindles. In order to find additional players in the force balance mechanism, we have performed a suppressor screen using a conditional allele of the fission yeast kinesin 5 ortholog Cut7. This screen identified that the lack of the PP6 phosphatase partially suppresses cut7 phenotypes, at least by defective translation of MT regulators, such as the minus end-directed kinesin Klp2, the MT stabilizer Alp7 and the MT bundler Ase1, impacting on the force balance mechanism. Additionally, our data show that the Elongator complex, a target activated by PP6 for efficient tRNA modification, also contributes to the force balance, albeit to a lesser extent. Importantly, this complex has recently been implicated in direct MT polymerization in metazoans, a role not shared by its fission yeast counterpart.","doi":"10.1371/journal.pgen.1011596","authors":"Marín L, Castro-Sangrador J, Hoya M, Tello S, Coll PM, Encinar Del Dedo J, Fernández-Álvarez A, Ribas JC, Tran PT, Rincon SA","authors_abbrev":"Marín L et al.","pubmed_publication_date":"Oct 2025","pubmed_entrez_date":"2025-10-07","publication_year":"2025","canto_session_key":"5e17f275b314e8fa","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-07 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24920274","title":"Meiotic long non-coding meiRNA accumulates as a dot at its genetic locus facilitated by Mmi1 and plays as a decoy to lure Mmi1.","citation":"Open Biol 2014 Jun;4(6):140022","abstract":"Long non-coding RNAs (lncRNAs) play key roles in the formation of nuclear bodies. In the fission yeast Schizosaccharomyces pombe, a lncRNA species termed meiRNA forms a nuclear dot structure at its own genetic locus, the sme2 locus, with its protein-binding partner Mei2. This dot structure, called Mei2 dot, promotes the progression of meiosis by suppressing Mmi1, a crucial factor involved in the selective elimination of meiosis-specific transcripts. The meiRNA itself is a target of Mmi1-mediated elimination and is supposed to function as a decoy to lure Mmi1. However, detailed mechanisms underlying the formation of Mei2 dot and inactivation of Mmi1 remain ambiguous. Here, we show that the localization of meiRNA, at its genetic locus sme2, depends on its association with Mmi1. We also demonstrate that one of the multiple Mmi1 foci in mitotic cells localizes to the sme2 locus. Furthermore, the overexpression of meiRNA promotes the accumulation of Mmi1 to the sme2 locus even in the absence of Mei2 and reduces the activity of Mmi1. These findings indicate that the retention of meiRNA at its genetic locus is facilitated by Mmi1, which then attracts scattered Mmi1 to inhibit its function.","doi":"10.1098/rsob.140022","authors":"Shichino Y, Yamashita A, Yamamoto M","authors_abbrev":"Shichino Y et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-06-13","publication_year":"2014","canto_session_key":"45395a087bd927e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-11-11 14:40:10","canto_approved_date":"2026-01-30 14:51:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-10-22 13:17:00","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":59,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPBC16E9.12c","SPCC736.12c","SPAC1006.03c","SPNCRNA.103","SPBC32H8.11","SPAC27D7.03c","SPBC646.04","SPAC27D7.13c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2020-11-11"},{"uniquename":"EMBL:AU009450","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.110"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7732725","title":"Characterization of Schizosaccharomyces pombe his1 and his5 cDNAs.","citation":"Yeast 1995 Feb;11(2):157-67","abstract":"We have isolated Schizosaccharomyces pombe cDNAs corresponding to the genes his1+ and his5+. The his1 cDNA was isolated by functional complementation of the His- phenotype in a his1-29 gcn3 Saccharomyces cerevisiae strain, while the his5 cDNA was isolated as a suppressor of the 3-amino-1,2, 4-triazole (3-AT) sensitivity in a gcn3 S. cerevisiae strain. his1 and his5 are each present in single copy in haploid S. pombe. As is the case with S. cerevisiae, we have found that the growth of wild-type strains of S. pombe is sensitive to 3-AT, an inhibitor of imidazoleglycerol-phosphate dehydratase. This enzyme is encoded by the HIS3 gene in S. cerevisiae and the his5+ gene in S. pombe. Treatment of S. pombe cells with 3-AT leads to a small increase in the level of the his5 transcript, but no effect is seen on the level of the his1 transcript. This is in contrast to larger increases in transcription of amino acid biosynthetic genes, regulated by the general amino acid control, seen previously in similarly treated cultures of S. cerevisiae. These results suggest that there are likely to be some differences in the regulation of amino acid biosynthesis between these two yeasts.","authors":"Erickson FL, Hannig EM","authors_abbrev":"Erickson FL et al.","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_session_key":"ffef0a4669e1a0fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-21 11:40:21","canto_approved_date":"2021-04-12 16:06:29","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-21 11:40:14","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.05c","SPBC21H7.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-10-21"},{"uniquename":"PMID:23168257","title":"Cellular strategies for regulating functional and nonfunctional protein aggregation.","citation":"Cell Rep 2012 Nov 29;2(5):1425-37","abstract":"Growing evidence suggests that aggregation-prone proteins are both harmful and functional for a cell. How do cellular systems balance the detrimental and beneficial effect of protein aggregation? We reveal that aggregation-prone proteins are subject to differential transcriptional, translational, and degradation control compared to nonaggregation-prone proteins, which leads to their decreased synthesis, low abundance, and high turnover. Genetic modulators that enhance the aggregation phenotype are enriched in genes that influence expression homeostasis. Moreover, genes encoding aggregation-prone proteins are more likely to be harmful when overexpressed. The trends are evolutionarily conserved and suggest a strategy whereby cellular mechanisms specifically modulate the availability of aggregation-prone proteins to (1) keep concentrations below the critical ones required for aggregation and (2) shift the equilibrium between the monomeric and oligomeric/aggregate form, as explained by Le Chatelier's principle. This strategy may prevent formation of undesirable aggregates and keep functional assemblies/aggregates under control.","doi":"10.1016/j.celrep.2012.09.036","authors":"Gsponer J, Babu MM","authors_abbrev":"Gsponer J et al.","pubmed_publication_date":"29 Nov 2012","pubmed_entrez_date":"2012-11-22","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17502269","title":"Electrically induced protein release from Schizosaccharomyces pombe cells in a hyperosmotic condition during and following a high electropulsation.","citation":"J Biosci Bioeng 2007 Apr;103(4):298-302","abstract":"A high-electric-field application of fission yeast cells under hyperosmotic conditions improved the electro-induced release of protein and cytoplasmic enzymes. A cell suspension was pulsed at 12.5 kV/cm for 10 ms in a batch system and immediately postincubated at 30 degrees C. The total protein release rate from cells increased in the hypertonic solutions of 1.5-2.5 M sorbitol to approximately threefold higher than those in the hypotonic and isotonic solutions of 0-0.5 M sorbitol. The protein release rate in 2.0 M sorbitol greatly increased up to 4.5 h and then gradually increased after 7.5 h. The maximum activities of cytoplasmic enzymes, such as alcohol dehydrogenase and 3-phosphoglycerate kinase, were obtained at 7.5 h after electropulsation in 2.0 M sorbitol, yielding approximately 90% of the enzyme activity levels found in spheroplast lysate. On the other hand, the release rates of protease in vacuoles and invertase in periplasmic space did not depend on osmotic solutions during electric pulse application.","authors":"Suga M, Goto A, Hatakeyama T","authors_abbrev":"Suga M et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-05-16","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ632010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.44"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU014071","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16816948","title":"Pol5p, a novel binding partner to Cdc10p in fission yeast involved in rRNA production.","citation":"Mol Genet Genomics 2006 Oct;276(4):391-401","abstract":"Cdc10p is a major component of the cell cycle transcription factor complex MBF that controls G1-S phase specific gene expression in the fission yeast Schizosaccharomyces pombe. Here, we describe the identification of a new binding partner to Cdc10p and Pol5p. Pol5p was discovered through a 2-hybrid screen, with the direct interaction confirmed by in vitro \"pull-down\" experiments with bacterially expressed proteins. Pol5p appears to have no role in cell cycle gene expression, but is instead required for rRNA production. Pol5p is an essential gene, expressed constitutively throughout both the mitotic and meiotic life cycles, and localises to the nucleus. Over-expressing Pol5p has no phenotype, but reducing levels of Pol5p inhibits rRNA production. Pol5p is shown to bind to rDNA promoter fragments. Potentially, we have identified a mechanism by which Cdc10p controls rDNA gene expression, therefore linking the cell cycle with cellular growth.","authors":"Nadeem FK, Blair D, McInerny CJ","authors_abbrev":"Nadeem FK et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-07-04","publication_year":"2006","canto_session_key":"34b5610ee8bc464d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-01-22 15:23:59","canto_approved_date":"2021-01-22 15:24:00","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-01-22 15:23:53","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC14C8.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-01-22"},{"uniquename":"PMID:29813053","title":"Specific detection of fission yeast primary septum reveals septum and cleavage furrow ingression during early anaphase independent of mitosis completion.","citation":"PLoS Genet 2018 May;14(5):e1007388","abstract":"It is widely accepted in eukaryotes that the cleavage furrow only initiates after mitosis completion. In fission yeast, cytokinesis requires the synthesis of a septum tightly coupled to cleavage furrow ingression. The current cytokinesis model establishes that simultaneous septation and furrow ingression only initiate after spindle breakage and mitosis exit. Thus, this model considers that although Cdk1 is inactivated at early-anaphase, septation onset requires the long elapsed time until mitosis completion and full activation of the Hippo-like SIN pathway. Here, we studied the precise timing of septation onset regarding mitosis by exploiting both the septum-specific detection with the fluorochrome calcofluor and the high-resolution electron microscopy during anaphase and telophase. Contrarily to the existing model, we found that both septum and cleavage furrow start to ingress at early anaphase B, long before spindle breakage, with a slow ingression rate during anaphase B, and greatly increasing after telophase onset. This shows that mitosis and cleavage furrow ingression are not concatenated but simultaneous events in fission yeast. We found that the timing of septation during early anaphase correlates with the cell size and is regulated by the corresponding levels of SIN Etd1 and Rho1. Cdk1 inactivation was directly required for timely septation in early anaphase. Strikingly the reduced SIN activity present after Cdk1 loss was enough to trigger septation by immediately inducing the medial recruitment of the SIN kinase complex Sid2-Mob1. On the other hand, septation onset did not depend on the SIN asymmetry establishment, which is considered a hallmark for SIN activation. These results recalibrate the timing of key cytokinetic events in fission yeast; and unveil a size-dependent control mechanism that synchronizes simultaneous nuclei separation with septum and cleavage furrow ingression to safeguard the proper chromosome segregation during cell division.","doi":"10.1371/journal.pgen.1007388","authors":"G Cortés JC, Ramos M, Konomi M, Barragán I, Moreno MB, Alcaide-Gavilán M, Moreno S, Osumi M, Pérez P, Ribas JC","authors_abbrev":"G Cortés JC et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-05-30","publication_year":"2018","canto_session_key":"6788fbad2542709a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juan Carlos García Cortés","canto_first_approved_date":"2019-03-05 17:02:29","canto_approved_date":"2024-04-04 09:13:12","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-02-01 17:40:54","canto_added_date":"2018-06-01 00:15:03","annotation_curators":[{"name":"Juan Carlos García Cortés","community_curator":true,"annotation_count":15,"orcid":"0000-0002-2395-6668","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPCC18B5.03","SPAC20G8.05c","SPBC11B10.09","SPAC24B11.11c","SPCC1739.11c","SPAC1006.08","SPAC1F7.04","SPBC336.12c","SPBC27B12.04c","SPAC24H6.05","SPBC582.03","SPAC4A8.05c","SPBC19G7.05c"],"gene_count":14,"ltp_gene_count":12,"approved_date":"2019-03-05"},{"uniquename":"PMID:15358101","title":"Phosphoinositide-dependent kinase-1 orthologues from five eukaryotes are activated by the hydrophobic motif in AGC kinases.","citation":"Biochem Biophys Res Commun 2004 Sep 03;321(4):823-7","abstract":"Phosphoinositide-dependent kinase-1 (PDK1) mediates activation of many AGC kinases by docking onto a phosphorylated hydrophobic motif located C-terminal of the catalytic domain in the AGC kinase. The interaction shifts PDK1 into a conformation with increased catalytic activity and leads to autophosphorylation of PDK1. We demonstrate here that addition of a hydrophobic motif peptide increases the catalytic activity of PDK1 orthologues from Homo sapiens, Aplysia californica, Arabidopsis thaliana, Schizosaccharomyces pombe (ksg1), and Saccharomyces cerevisiae (Pkh1 and Pkh2) 2- to 12-fold. Furthermore, the hydrophobic motif peptide increases autophosphorylation of PDK1 from Homo sapiens, S. pombe, and S. cerevisiae (Phk2). Our results suggest that PDK1 interaction and activation by the hydrophobic motif of AGC kinases is a central mechanism in PDK1 function, which is conserved during eukaryotic evolution.","authors":"Silber J, Antal TL, Gammeltoft S, Rasmussen TE","authors_abbrev":"Silber J et al.","pubmed_publication_date":"03 Sep 2004","pubmed_entrez_date":"2004-09-11","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18309270","title":"Genome-wide drug-induced haploinsufficient screening of fission yeast for identification of hydrazinocurcumin targets.","citation":"J Microbiol Biotechnol 2008 Feb;18(2):263-9","abstract":"Hydrazinocurcumin (HC), a synthetic derivative of curcumin, has been reported to inhibit angiogenesis via unknown mechanisms. Understanding the molecular mechanisms of the drug's action is important for the development of improved compounds with better pharmacological properties. A genomewide drug-induced haploinsufficiency screening of fission yeast gene deletion mutants has been applied to identify drug targets of HC. As a first step, the 50% inhibition concentration (IC50) of HC was determined to be 2.2 microM. The initial screening of 4,158 mutants in 384-well plates using robotics was performed at concentrations of 2, 3, and 4 microM. A second screening was performed to detect sensitivity to HC on the plates. The first screening revealed 178 candidates, and the second screening resulted in 13 candidates, following the elimination of 165 false positives. Final filtering of the condition-dependent haploinsufficient genes gave eight target genes. Analysis of the specific targets of HC has shown that they are related to septum formation and the general transcription processes, which may be related to histone acetyl transferase. The target mutants showed 65% growth inhibition in response to HC compared with wild-type controls, as shown by liquid culture assay.","authors":"Baek ST, Kim DU, Han S, Woo IS, Nam M, Kim L, Heo KS, Lee H, Hwang HR, Choi SJ, Won M, Lee M, Park SK, Lee S, Kwon HJ, Maeng PJ, Park HM, Park Y, Kim D, Hoe KL","authors_abbrev":"Baek ST et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2008-03-01","publication_year":"2008","canto_session_key":"9a1022fd353bacb9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-17 09:01:19","canto_approved_date":"2019-06-14 08:02:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-17 09:01:11","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.10","SPBC646.17c","SPBC215.09c","SPAC23G3.09","SPAC1834.05","SPAC1006.02","SPBP16F5.02","SPBC16A3.01"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2014-10-17"},{"uniquename":"PMID:19470480","title":"Ctp1 and Exonuclease 1, alternative nucleases regulated by the MRN complex, are required for efficient meiotic recombination.","citation":"Proc Natl Acad Sci U S A 2009 Jun 09;106(23):9356-61","abstract":"Double-strand breaks (DSBs) in DNA are lethal unless repaired. Faithful repair requires processing of the DSB ends and interaction with intact homologous DNA, which can produce genetic recombinants. To determine the role of nucleases in DSB end-processing and joint molecule resolution, we studied recombination at the site of a single DSB, generated by induction of the I-SceI endonuclease, during meiosis of fission yeast lacking Rec12 (Spo11 homolog) and, hence, other DSBs. We find that in the presence of the MRN (Rad32-Rad50-Nbs1) complex efficient recombination requires Ctp1, the ortholog of the nuclease Sae2, but not the nuclease activity of MRN. In the absence of MRN, exonuclease 1 (Exo1) becomes the major nuclease required for efficient recombination. Our data indicate that MRN enables access of Ctp1 to the DSB but blocks access of Exo1. In our assay, the Rad16-Swi10 nuclease, required for nucleotide excision-repair, is required for efficient recombination, presumably to remove heterologous DNA at the end of the I-SceI cut site. Another nuclease, the Mus81-Eme1 Holliday junction resolvase, is required to generate crossovers accompanying gene conversion at the I-SceI cut site. Additional, previously published evidence indicates that these 5 nucleases play similar roles in wild-type fission yeast meiotic recombination and in the repair of spontaneous and damage-induced mitotic DSBs. We propose that in wild-type meiosis MRN, in conjunction with Ctp1, removes the covalently attached Rec12 protein from the DNA end, which is then resected by Ctp1 and other activities to produce the single-stranded DNA necessary for further steps of DSB repair.","doi":"10.1073/pnas.0902793106","authors":"Farah JA, Cromie GA, Smith GR","authors_abbrev":"Farah JA et al.","pubmed_publication_date":"09 Jun 2009","pubmed_entrez_date":"2009-05-28","publication_year":"2009","canto_session_key":"bfaf9bdc389abc6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-02-21 17:20:56","canto_approved_date":"2020-07-09 15:53:14","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-02-21 17:20:44","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPCC338.08","SPBC29A10.05","SPAC13C5.07","SPCC970.01","SPCC4G3.05c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-02-21"},{"uniquename":"PMID:9514857","title":"Identification of Schizosaccharomyces pombe prenol as dolichol-16,17.","citation":"Biochem Biophys Res Commun 1998 Mar 17;244(2):546-50","abstract":"The identity of the prenol involved in N-linked glycosylation in the fission yeast Schizosaccharomyces pombe was unknown. In order to determine the identity of the prenol, S. pombe cells were incubated with a metabolic precursor of prenol, tritiated mevalonolactone. The cells incorporated only a modest amount of label, about 1000 dpm per million cells, into base-stable lipid and only 1% of that radioactivity was incorporated into prenol. We found by normal phase silica HPLC and more directly by the lack of reactivity with MnO2 that the labeled lipid was predominantly dolichol, not polyprenol. Reverse phase HPLC demonstrated that in S. pombe dolichol ranged between 14 and 18 isoprene units with dolichol-16,17 being the most abundant prenol. This dolichol is of an intermediate length, between the dolichol of S. cerevisiae and that of mammalian cells.","authors":"Quellhorst GJ, Piotrowski JS, Steffen SE, Krag SS","authors_abbrev":"Quellhorst GJ et al.","pubmed_publication_date":"17 Mar 1998","pubmed_entrez_date":"1998-03-26","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22093749","title":"Versatile use of Schizosaccharomyces pombe plasmids in Saccharomyces cerevisiae.","citation":"FEMS Yeast Res 2011 Dec;11(8):653-5","abstract":"The two model yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe appear to have diverged 1000 million years ago. Here, we describe that S. pombe vectors can be propagated efficiently in S. cerevisiae as pUR19 derivatives, and the pREP and pJR vector series carrying the S. cerevisiae LEU2 or the S. pombe ura4(+) selection marker are maintained in S. cerevisiae cells. In addition, genes transcribed from the S. pombe nmt1(+) promoter and derivatives are expressed in budding yeast. Thus, S. pombe vectors can be used as shuttle vectors in S. cerevisiae and S. pombe. Our finding greatly facilitates the testing for functional orthologs of protein families and simplifies the cloning of new S. pombe plasmids by using the highly efficient in vivo homologous recombination activity of S. cerevisiae.","doi":"10.1111/j.1567-1364.2011.00752.x","authors":"Jakopec V, Walla E, Fleig U","authors_abbrev":"Jakopec V et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-11-19","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9042863","title":"Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast.","citation":"Genes Dev 1997 Feb 15;11(4):504-11","abstract":"A common cellular response to DNA damage is cell cycle arrest. This checkpoint control has been the subject of intensive genetic investigation, but the biochemical mechanism that prevents mitosis following DNA damage is unknown. In Schizosaccharomyces pombe, as well as vertebrates, the timing of mitosis under normal circumstances is determined by the balance of kinases and phosphatases that regulate inhibitory phosphorylation of Cdc2. In S. pombe, the phosphorylation occurs on tyrosine-15. This method of mitotic control is also used in S. pombe to couple mitosis with completion of DNA replication, but the role of Cdc2 tyrosine phosphorylation in the Chk1 kinase-mediated DNA damage checkpoint has remained uncertain. We show that, in contrast to recent speculation, the G2 DNA damage checkpoint arrest in S. pombe depends on the inhibitory tyrosine phosphorylation of Cdc2 carried out by the Wee1 and Mik1 kinases. Furthermore, the rate of Cdc2 tyrosine dephosphorylation is reduced by irradiation. This result implicates regulation of Cdc2 tyrosine dephosphorylation, mainly carried out by the Cdc25 tyrosine phosphatase, as an important part of the mechanism by which the DNA damage checkpoint induces Cdc2 inhibition and G2 arrest.","authors":"Rhind N, Furnari B, Russell P","authors_abbrev":"Rhind N et al.","pubmed_publication_date":"15 Feb 1997","pubmed_entrez_date":"1997-02-15","publication_year":"1997","canto_session_key":"34790a1dd257be4f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2020-02-18 12:43:57","canto_approved_date":"2023-04-03 13:11:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-10 15:48:35","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.14","SPAC24H6.05","SPCC18B5.03","SPCC1259.13","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-02-18"},{"uniquename":"PMID:38427716","title":"The roles of Gti1/Pac2 family proteins in fungal growth, morphogenesis, stress response and pathogenicity.","citation":"Mol Plant Microbe Interact 2024 Mar 01;","abstract":"Gti1/Pac2 is a fungal specific transcription factor family with a stable and conserved N-terminal domains. Generally, there are two members in this family named as Gti1/Wor1/Rpy1/Mit1/Reg1/Ros1/Sge1 and Pac2, which are involving in fungal growth, development, stress response, spore production, pathogenicity and so on. The Gti1/Pac2 family proteins shared some conserved and distinct functions. For example, in Schizosaccharomyces pombe, Gti1 promotes the initiation of gluconate uptake during glucose starvation, while Pac2 controls the onset of sexual development in a pathway independent of the cAMP cascade. In recent two decades, more attention was focused on the Gti1 and its orthologs due to their significant effect on morphology switch and fungal virulence. By contrast, there are limited works on the functions of Pac2 which is required for stress responses and conidiation, but play minor roles in fungal virulence. In this review, we present an overview of our current understanding of the Gti1/Pac2 proteins that contribute to fungal development and/or pathogenicity and of the regulation mechanisms during infection related development. Understanding the working networks of the conserved Gti1/Pac2 transcription factors in fungal pathogenicity not only advances our knowledge of the highly elaborate infection process but may also lead to the development of novel strategies for the control of plant disease.","doi":"10.1094/MPMI-11-23-0198-CR","authors":"Luo Z, Xiong D, Tian C","authors_abbrev":"Luo Z et al.","pubmed_publication_date":"01 Mar 2024","pubmed_entrez_date":"2024-03-01","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-03-02 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3309892","title":"A single intronless action gene in the fission yeast Schizosaccharomyces pombe: nucleotide sequence and transcripts formed in homologous and heterologous yeast.","citation":"Nucleic Acids Res 1987 Sep 25;15(18):7369-79","abstract":"The actin gene of the fission yeast Schizosaccharomyces pombe has been isolated by using as a hybridization probe cloned actin DNA from the budding yeast Saccharomyces cerevisiae. In contrast to most actin genes studied from diverse eukaryotic species, the S. pombe gene is not interrupted by introns. The protein sequence deduced from the nucleotide sequence of the gene shows that the S. pombe actin is more closely related to the mammalian gamma-actin than to the actin of S. cerevisiae. Three transcripts of 1240, 1650 and 1850 nucleotides having the same 5' end but differing in the length of their 3' untranslated region are generated in the fission yeast. Only one messenger RNA of 1330 nucleotides is formed from the S. pombe actin gene in S. cerevisiae. Contrary to the observation made with other S. pombe genes transcribed in the budding yeast, the heterologous actin gene transcript is initiated 39 nucleotides upstream of the initiation start site used in the homologous yeast. The mRNA termination (or 3' processing) mechanism in the two ascomycetes also differs as the 3'end of the S. pombe actin gene transcript in S. cerevisiae does not coincide with either of the three 3'ends mapped in the fission yeast.","authors":"Mertins P, Gallwitz D","authors_abbrev":"Mertins P et al.","pubmed_publication_date":"25 Sep 1987","pubmed_entrez_date":"1987-09-25","publication_year":"1987","canto_session_key":"4bffd6cca3d587b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 17:41:02","canto_approved_date":"2019-01-31 17:41:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 17:40:54","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.12c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:12851470","title":"Does a GATA factor make the bed for centromeric nucleosomes?","citation":"Cell Cycle 2003;2(4):277-8","abstract":"CENP-A is an evolutionarily conserved, centromere-specific histone H3 variant. It remains a great mystery how CENP-A is correctly incorporated into the centromere, a restricted chromosomal region, despite the presence of an overwhelming amount of histone H3. We identified a cell cycle-regulated GATA factor, Ams2, as a component of the CENP-A localization pathway in fission yeast. Unexpectedly, this putative transcription factor, which belongs to a protein family containing members that remodel nucleosomes, appeared to bind to and function at the central region of the centromere. Although the centromere has in general been considered transcriptionally inactive, fission yeast's outer centromeric region has recently been shown to encode non-translated snRNAs that are involved in heterochromatin formation. Transcription factors such as Ams2 may directly transcribe some unidentified non-translated centromeric RNAs. Transcription and/or remodeling of the nucleosomes at the centromeres may be important for the precise incorporation of CENP-A in fission yeast.","authors":"Chen ES, Yanagida M, Takahashi K","authors_abbrev":"Chen ES et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-07-10","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12166068","title":"[Genome sequence of Schizosaccharomyces pombe].","citation":"Tanpakushitsu Kakusan Koso 2002 Jul;47(9):1215-20","abstract":"","authors":"Chikashige Y, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-08-09","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6350830","title":"Expression of cloned mitochondrial DNA from the petite negative yeast Schizosaccharomyces pombe in E. coli minicells.","citation":"Mol Gen Genet 1983;191(1):91-8","abstract":"The minicell producing Escherichia coli strain D24 (lysogenic for phage lambda cI857) was transformed with the recombinant plasmid pDG3 containing the entire mitochondrial (mt) genome of the fission yeast Schizosaccharomyces pombe (S. pombe) cloned in the single BamHI-site of the E. coli plasmid pBR322 (Del Giudice 1981). By DNA-RNA hybridization it could be shown that the total mtDNA sequence of the plasmid pDG3 was transcribed in the E. coli minicells. The cloned mtDNA also directed the synthesis of at least five novel polypeptides with molecular weights between 7,200 and 34,000. When the minicell producing E. coli strain P678-54 was transformed with the hybrid plasmid pDG3, considerable portions of the inserted mtDNA sequences were deleted. One of the resulting plasmids (pDG4), lacking about two-thirds of the mtDNA sequence, directed the synthesis of new polypeptides in the range of 7,000 to 17,500 daltons. Another derivative of pDG3, the plasmid pDG5, containing one-sixth of the mtDNA sequence, directed the synthesis of at least three novel polypeptides. The mt origin of novel polypeptides coded by the hybrid plasmid pDG3 was demonstrated by use of antisera raised against total mitochondrial proteins from S. pombe and antisera against subunits II and III of cytochrome c oxidase from Saccharomyces cerevisiae (S. cer.).","authors":"Del Giudice L, Wolf K, Manna F, Massardo DR","authors_abbrev":"Del Giudice L et al.","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-01-01","publication_year":"1983","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18154680","title":"Checkpoint effects and telomere amplification during DNA re-replication in fission yeast.","citation":"BMC Mol Biol 2007 Dec 21;8:119","abstract":"Although much is known about molecular mechanisms that prevent re-initiation of DNA replication on newly replicated DNA during a single cell cycle, knowledge is sparse regarding the regions that are most susceptible to re-replication when those mechanisms are bypassed and regarding the extents to which checkpoint pathways modulate re-replication. We used microarrays to learn more about these issues in wild-type and checkpoint-mutant cells of the fission yeast, Schizosaccharomyces pombe.\nWe found that over-expressing a non-phosphorylatable form of the replication-initiation protein, Cdc18 (known as Cdc6 in other eukaryotes), drove re-replication of DNA sequences genome-wide, rather than forcing high level amplification of just a few sequences. Moderate variations in extents of re-replication generated regions spanning hundreds of kilobases that were amplified (or not) approximately 2-fold more (or less) than average. However, these regions showed little correlation with replication origins used during S phase. The extents and locations of amplified regions in cells deleted for the checkpoint genes encoding Rad3 (ortholog of human ATR and budding yeast Mec1) and Cds1 (ortholog of human Chk2 and budding yeast Rad53) were similar to those in wild-type cells. Relatively minor but distinct effects, including increased re-replication of heterochromatic regions, were found specifically in cells lacking Rad3. These might be due to Cds1-independent roles for Rad3 in regulating re-replication and/or due to the fact that cells lacking Rad3 continued to divide during re-replication, unlike wild-type cells or cells lacking Cds1. In both wild-type and checkpoint-mutant cells, regions near telomeres were particularly susceptible to re-replication. Highly re-replicated telomere-proximal regions (50-100 kb) were, in each case, followed by some of the least re-replicated DNA in the genome.\nThe origins used, and the extent of replication fork progression, during re-replication are largely independent of the replication and DNA-damage checkpoint pathways mediated by Cds1 and Rad3. The fission yeast pattern of telomere-proximal amplification adjacent to a region of under-replication has also been seen in the distantly-related budding yeast, which suggests that subtelomeric sequences may be a promising place to look for DNA re-replication in other organisms.","authors":"Mickle KL, Oliva A, Huberman JA, Leatherwood J","authors_abbrev":"Mickle KL et al.","pubmed_publication_date":"21 Dec 2007","pubmed_entrez_date":"2007-12-25","publication_year":"2007","canto_session_key":"800e03555a772a5d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-08-07 10:39:04","canto_approved_date":"2019-08-07 10:39:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-08-07 10:36:15","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC14C8.07c","SPBC216.05"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2019-08-07"},{"uniquename":"PMID:16782736","title":"High-pressure freezing is a powerful tool for visualization of Schizosaccharomyces pombe cells: ultra-low temperature and low-voltage scanning electron microscopy and immunoelectron microscopy.","citation":"J Electron Microsc (Tokyo) 2006 Apr;55(2):75-88","abstract":"Yeast cells have a thick cell wall composed of an inner network of glucans and an outer layer of mannoproteins, which is difficult to penetrate with osmium tetroxide. We previously developed the sandwich technique to overcome this problem. Although the freeze-etching method allows the fracturing of cryofixed yeast cells, it has been difficult to fracture cryofixed yeast cells for examination by cryo-scanning electron microscopy (SEM). The development of an alternative method of cryofixation, namely, high-pressure freezing, began in the 1960s and is now available for the electron microscopic analysis of yeast. We show here that when high-pressure freezing is combined with ultra-low temperature and low-voltage SEM using the new cryo-system, the Gatan Alto 2500 Cryo Transfer System, fractured and coated yeast samples could be quickly prepared. These samples yielded a fine fracture plane and revealed the ultrastructure of both external and internal cell components. We used this method to analyze the process of septum formation, one of the final and most important events of mitosis, and cell separation. The images we obtained provide a three-dimensional view of these processes for the first time. We also showed that high-pressure freezing in combination with immunoelectron microscopy made it possible to preserve the antigenicity, in situ localization, and behavior of the cell wall component alpha-1,3-glucan and its synthase during septum formation in Schizosaccharomyces pombe.","authors":"Osumi M, Konomi M, Sugawara T, Takagi T, Baba M","authors_abbrev":"Osumi M et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-06-20","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20621843","title":"Processing of the dynamin Msp1p in S. pombe reveals an evolutionary switch between its orthologs Mgm1p in S. cerevisiae and OPA1 in mammals.","citation":"FEBS Lett 2010 Jul 16;584(14):3153-7","abstract":"Mitochondrial fusion depends on the evolutionary conserved dynamin, OPA1/Mgm1p/Msp1p, whose activity is controlled by proteolytic processing. Since processing diverges between Mgm1p (Saccharomyces cerevisiae) and OPA1 (mammals), we explored this process in another model, Msp1p in Schizosaccharomyces pombe. Generation of the short isoform of Msp1p neither results from the maturation of the long isoform nor correlates with mitochondrial ATP levels. Msp1p is processed by rhomboid and a protease of the matrix ATPase associated with various cellular activities (m-AAA) family. The former is involved in the generation of short Msp1p and the latter in the stability of long Msp1p. These results reveal that Msp1p processing may represent an evolutionary switch between Mgm1p and OPA1.","doi":"10.1016/j.febslet.2010.05.060","authors":"Leroy I, Khosrobakhsh F, Diot A, Daloyau M, Arnauné-Pelloquin L, Cavelier C, Emorine LJ, Belenguer P","authors_abbrev":"Leroy I et al.","pubmed_publication_date":"16 Jul 2010","pubmed_entrez_date":"2010-07-13","publication_year":"2010","canto_session_key":"a0ebde350da08790","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-20 08:32:41","canto_approved_date":"2026-04-08 12:46:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-20 08:32:31","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.13","SPBC530.10c","SPAC222.12c","SPBC1718.06","SPBC543.09","SPBC13E7.11","SPBP4H10.10","SPAC14C4.14"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2014-08-20"},{"uniquename":"PMID:12058375","title":"Primitive forms of meiosis: the possible evolution of meiosis.","citation":"Biocell 2002 Apr;26(1):1-13","abstract":"Meiosis is a basic process of most eukaryotes, as it forms with conjugation the basis of sexual reproduction. As sex seems to be present in the vast majority of eukaryotes, the origin of meiosis is presently unknown. Protists having optional or alternative sexual and asexual cycles seem to be the best targets for research on the evolution of meiosis. While the budding yeast Saccharomyces cerevisiae shows an elaborate and well-known meiotic process, the fission yeast Schizosaccharomyces pombe, has a much simpler meiosis, which may show some of the most primitive features of meiotic mechanisms. The present availability of whole genome sequences of many bacteria and some protists is revealing that eukaryotic sexual reproduction has recruited some prokaryotic processes for its own development. Some of these processes are analyzed and the basic role of chromosome linearity and telomere constitution in the development of meiosis is underlined.","authors":"Solari AJ","authors_abbrev":"Solari AJ","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-06-13","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22876190","title":"A positive feedback loop links opposing functions of P-TEFb/Cdk9 and histone H2B ubiquitylation to regulate transcript elongation in fission yeast.","citation":"PLoS Genet 2012;8(8):e1002822","abstract":"Transcript elongation by RNA polymerase II (RNAPII) is accompanied by conserved patterns of histone modification. Whereas histone modifications have established roles in transcription initiation, their functions during elongation are not understood. Mono-ubiquitylation of histone H2B (H2Bub1) plays a key role in coordinating co-transcriptional histone modification by promoting site-specific methylation of histone H3. H2Bub1 also regulates gene expression through an unidentified, methylation-independent mechanism. Here we reveal bidirectional communication between H2Bub1 and Cdk9, the ortholog of metazoan positive transcription elongation factor b (P-TEFb), in the fission yeast Schizosaccharomyces pombe. Chemical and classical genetic analyses indicate that lowering Cdk9 activity or preventing phosphorylation of its substrate, the transcription processivity factor Spt5, reduces H2Bub1 in vivo. Conversely, mutations in the H2Bub1 pathway impair Cdk9 recruitment to chromatin and decrease Spt5 phosphorylation. Moreover, an Spt5 phosphorylation-site mutation, combined with deletion of the histone H3 Lys4 methyltransferase Set1, phenocopies morphologic and growth defects due to H2Bub1 loss, suggesting independent, partially redundant roles for Cdk9 and Set1 downstream of H2Bub1. Surprisingly, mutation of the histone H2B ubiquitin-acceptor residue relaxes the Cdk9 activity requirement in vivo, and cdk9 mutations suppress cell-morphology defects in H2Bub1-deficient strains. Genome-wide analyses by chromatin immunoprecipitation also demonstrate opposing effects of Cdk9 and H2Bub1 on distribution of transcribing RNAPII. Therefore, whereas mutual dependence of H2Bub1 and Spt5 phosphorylation indicates positive feedback, mutual suppression by cdk9 and H2Bub1-pathway mutations suggests antagonistic functions that must be kept in balance to regulate elongation. Loss of H2Bub1 disrupts that balance and leads to deranged gene expression and aberrant cell morphologies, revealing a novel function of a conserved, co-transcriptional histone modification.","doi":"10.1371/journal.pgen.1002822","authors":"Sansó M, Lee KM, Viladevall L, Jacques PÉ, Pagé V, Nagy S, Racine A, St Amour CV, Zhang C, Shokat KM, Schwer B, Robert F, Fisher RP, Tanny JC","authors_abbrev":"Sansó M et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-10","publication_year":"2012","canto_session_key":"22719ff0a4d26bd1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19F8.07","SPCC622.09","SPBC32H8.10","SPAC23C4.19","SPAC2F3.15","SPCC306.04c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:17248796","title":"Influence of the mat1-M Allele on Meiotic Recombination in the Mating-Type Region of SCHIZOSACCHAROMYCES POMBE.","citation":"Genetics 1978 Feb;88(2):235-8","abstract":"Angehrn and Gutz (1968) have shown that homozygosity for the mat1-M allele in diploid strains of Schizosaccharomyces pombe increases mitotic recombination between his7 and mat2. In this paper, we report that meiotic recombination frequencies can vary from 3.4 to 16.1 percent between his7 and his2 and that this variation is due to the combination of alleles at the mat1 and mat2 loci.","authors":"Meade JH, Gutz H","authors_abbrev":"Meade JH et al.","pubmed_publication_date":"Feb 1978","pubmed_entrez_date":"1978-02-01","publication_year":"1978","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27250945","title":"Cell Cycle Synchronization of Schizosaccharomyces pombe by Lactose Gradient Centrifugation to Isolate Small Cells.","citation":"Cold Spring Harb Protoc 2016 Jun 01;2016(6)","abstract":"Size selection of small cells from an asynchronous Schizosaccharomyces pombe culture offers a simple way to generate cultures in which progression through the mitotic cell division cycle is synchronized throughout the population. Here, we describe how density centrifugation of cells from asynchronous cultures through lactose gradients selects small G2 cells to generate synchronized cultures as large as 500 mL. The ease and simplicity of this approach makes it an accessible and attractive method for generating synchronous cultures.","doi":"10.1101/pdb.prot091249","authors":"Hagan IM, Grallert A, Simanis V","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"01 Jun 2016","pubmed_entrez_date":"2016-06-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-06-04 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15897182","title":"Two distinct pathways responsible for the loading of CENP-A to centromeres in the fission yeast cell cycle.","citation":"Philos Trans R Soc Lond B Biol Sci 2005 Mar 29;360(1455):595-606; discussion 606-7","abstract":"CENP-A is a centromere-specific histone H3 variant that is- essential for faithful chromosome segregation in all eukaryotes thus far investigated. We genetically identified two factors, Ams2 and Mis6, each of which is required for the correct centromere localization of SpCENP-A (Cnp1), the fission yeast homologue of CENP-A. Ams2 is a cell-cycle-regulated GATA factor that localizes on the nuclear chromatin, including on centromeres, during the S phase. Ams2 may be responsible for the replication-coupled loading of SpCENP-A by facilitating nucleosomal formation during the S phase. Consistently, overproduction of histone H4, but not that of H3, suppressed the defect of SpCENP-A localization in Ams2-deficient cells. We demonstrated the existence of at least two distinct phases for SpCENP-A loading during the cell cycle: the S phase and the late-G2 phase. Ectopically induced SpCENP-A was efficiently loaded onto the centromeres in G2-arrested cells, indicating that SpCENP-A probably undergoes replication-uncoupled loading after the completion of S phase. This G2 loading pathway of SpCENP-A may require Mis6, a constitutive centromere-binding protein that is also implicated in the Mad2-dependent spindle attachment checkpoint response. Here, we discuss the functional relationship between the flexible loading mechanism of CENP-A and the plasticity of centromere chromatin formation in fission yeast.","authors":"Takahashi K, Takayama Y, Masuda F, Kobayashi Y, Saitoh S","authors_abbrev":"Takahashi K et al.","pubmed_publication_date":"29 Mar 2005","pubmed_entrez_date":"2005-05-18","publication_year":"2005","canto_session_key":"beb7ea66dfc7fba2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-01-24 11:01:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-22 12:39:19","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC290.04","SPBC1105.12","SPBC1105.17"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-01-22"},{"uniquename":"PMID:39332155","title":"3,3'-Diindolylmethane disrupts the endoplasmic reticulum and nuclear envelope in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2024 Sep 24;733:150724","abstract":"3,3'-Diindolylmethane is recognized for its anti-cancer activities in various pathways, though its mechanism remains to be fully elucidated. Previous studies have shown that 3,3'-Diindolylmethane disturbed the localization of Cut11, a nuclear pore complex subunit in Schizosaccharomyces pombe. This study further reveals that in Schizosaccharomyces pombe, 3,3'-Diindolylmethane also disrupts other components of nuclear envelope, causing GFP-NLS leakage, making it evident that 3,3'-Diindolylmethane disrupts the nuclear envelope. 3,3'-Diindolylmethane also disturbs the localization of GFP-ADEL and Ost4, which are endoplasmic reticulum lumen proteins and membrane proteins respectively, suggesting the function of 3,3'-Diindolylmethane on endoplasmic reticulum disturbance. The nuclear envelope repairment, normal nuclear envelope physical properties, and lipid metabolism homeostasis are crucial for cell survival in the presence of 3,3'-Diindolylmethane. These findings provide new insights into the understanding and development of 3,3'-Diindolylmethane as an anti-cancer agent.","doi":"10.1016/j.bbrc.2024.150724","authors":"Wang K, Seol H, Emami P, Nagai H, Ueno M","authors_abbrev":"Wang K et al.","pubmed_publication_date":"24 Sep 2024","pubmed_entrez_date":"2024-09-27","publication_year":"2024","canto_session_key":"b9c7a8434d45653c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-09-28 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11238401","title":"The git5 Gbeta and git11 Ggamma form an atypical Gbetagamma dimer acting in the fission yeast glucose/cAMP pathway.","citation":"Genetics 2001 Mar;157(3):1159-68","abstract":"Fission yeast adenylate cyclase, like mammalian adenylate cyclases, is regulated by a heterotrimeric G protein. The gpa2 Galpha and git5 Gbeta are both required for glucose-triggered cAMP signaling. The git5 Gbeta is a unique member of the Gbeta family in that it lacks an amino-terminal coiled-coil domain shown to be essential for mammalian Gbeta folding and interaction with Ggamma subunits. Using a git5 bait in a two-hybrid screen, we identified the git11 Ggamma gene. Co-immunoprecipitation studies confirm the composition of this Gbetagamma dimer. Cells deleted for git11 are defective in glucose repression of both fbp1 transcription and sexual development, resembling cells lacking either the gpa2 Galpha or the git5 Gbeta. Overexpression of the gpa2 Galpha partially suppresses loss of either the git5 Gbeta or the git11 Ggamma, while mutational activation of the Galpha fully suppresses loss of either Gbeta or Ggamma. Deletion of gpa2 (Galpha), git5 (Gbeta), or git11 (Ggamma) confer quantitatively distinct effects on fbp1 repression, indicating that the gpa2 Galpha subunit remains partially active in the absence of the Gbetagamma dimer and that the git5 Gbeta subunit remains partially active in the absence of the git11 Ggamma subunit. The addition of the CAAX box from the git11 Ggamma to the carboxy-terminus of the git5 Gbeta partially suppresses the loss of the Ggamma. Thus the Ggamma in this system is presumably required for localization of the Gbetagamma dimer but not for folding of the Gbeta subunit. In mammalian cells, the essential roles of the Gbeta amino-terminal coiled-coil domains and Ggamma partners in Gbeta folding may therefore reflect a mechanism used by cells that express multiple forms of both Gbeta and Ggamma subunits to regulate the composition and activity of its G proteins.","authors":"Landry S, Hoffman CS","authors_abbrev":"Landry S et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-03-10","publication_year":"2001","canto_session_key":"61e3a10a189ba939","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-29 16:13:00","canto_approved_date":"2026-04-08 08:18:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-29 14:12:42","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC215.04","SPBC19C7.03","SPBC32H8.07","SPAC23H3.13c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-03-29"},{"uniquename":"EMBL:SPD180","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1560765","title":"The two similarly expressed genes encoding U3 snRNA in Schizosaccharomyces pombe lack introns.","citation":"Mol Biol Evol 1992 Mar;9(2):297-308","abstract":"Both genes encoding U3 small nuclear RNA (snRNA) from the budding yeast Saccharomyces cerevisiae were recently shown to be interrupted by introns of the type removed by the pre-mRNA splicing machinery. We previously described one of the two U3 genes from the fission yeast Schizosaccharomyces pombe. In the present work, the second S. pombe U3 coding sequence was identified, and direct RNA sequence analysis was used to show that neither the U3A nor the U3B gene from this organism contains an intervening sequence. Our data also demonstrate that, as expected, the two RNAs exhibit great primary- and secondary-structure conservation. These similarities are not likely to be the result of a recent gene duplication or conversion event, because the DNA sequences flanking the U3A and U3B genes have diverged substantially. A notable exception is a 19-bp block, centered 36 nucleotides upstream from the transcriptional start site, in which the two loci match in 15 positions; this motif may represent an RNA polymerase II upstream regulatory element, because related sequences are found preceding fission yeast U1, U2, U4, and U5 snRNA genes. The significance of a short conserved sequence just downstream of the U3A and U3B genes is unknown, as it is not found 3' to other snRNA coding sequences in S. pombe. The 5' one-third of U3B RNA can be folded into a dual hairpin structure, as we previously proposed for Schizosaccharomyces pombe U3A and for other lower eukaryotic U3 homologues. Quantitation of fission yeast U3A and U3B indicates that, in contrast to snR17A and B in Saccharomyces cerevisiae, these RNAs accumulate to similar levels.","authors":"Selinger DA, Porter GL, Brennwald PJ, Wise JA","authors_abbrev":"Selinger DA et al.","pubmed_publication_date":"Mar 1992","pubmed_entrez_date":"1992-03-01","publication_year":"1992","canto_session_key":"be8cb1e334f904ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-19 16:52:23","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-19 16:51:56","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.03","SPSNRNA.07"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2014-06-19"},{"uniquename":"PMID:27188733","title":"The roles of SPBC409.08 and SPAC9.02c hypothetical genes in cell cycle and stress response, in Schizosaccharomyces pombe.","citation":"Cell Mol Biol (Noisy-le-grand) 2016 Apr 30;62(4):42-7","abstract":"Polyamine molecules are known to have important roles in the cell cycle control and fighting against stress in the cell. The mechanism and modification of polyamines are regulated by the cooperation of many proteins such as polyamine transporter proteins and polyamine acetyltransferases. In this study, our aim is to characterize two hypothetical Schizosaccharomyces pombe genes, SPBC409.08 and SPAC9.02c, which show sequence similarity to spermine family transporters and polyamine N-acetyltransferases, respectively. To this end, we generated deletion mutants of SPBC409.08 and SPAC9.02c genes using Bahler method and checked the cell cycle progression and stress responses of these mutants. Our results showed that SPBC409.08Δ cells showed some defects in the cell size, while SPAC9.02cΔ cells showed some sensitivity to UV irradiation. These data support their potential roles in the cell cycle and stress response. To our knowledge our results are the first experimental characterization of these genes.","authors":"Güngör I, Örs Gevrekci A","authors_abbrev":"Güngör I et al.","pubmed_publication_date":"30 Apr 2016","pubmed_entrez_date":"2016-05-19","publication_year":"2016","canto_session_key":"87f2700b47b2492e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-05 13:56:11","canto_approved_date":"2019-06-05 13:56:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-06-05 13:56:04","canto_added_date":"2016-05-19 00:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9.02c","SPBC409.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-06-05"},{"uniquename":"PMID:23085840","title":"Growth of transplastomic cells expressing D-amino acid oxidase in chloroplasts is tolerant to D-alanine and inhibited by D-valine.","citation":"Plant Physiol 2012 Dec;160(4):2219-26","abstract":"Dual-conditional positive/negative selection markers are versatile genetic tools for manipulating genomes. Plastid genomes are relatively small and conserved DNA molecules that can be manipulated precisely by homologous recombination. High-yield expression of recombinant products and maternal inheritance of plastid-encoded traits make plastids attractive sites for modification. Here, we describe the cloning and expression of a dao gene encoding D-amino acid oxidase from Schizosaccharomyces pombe in tobacco (Nicotiana tabacum) plastids. The results provide genetic evidence for the uptake of D-amino acids into plastids, which contain a target that is inhibited by D-alanine. Importantly, this nonantibiotic-based selection system allows the use of cheap and widely available D-amino acids, which are relatively nontoxic to animals and microbes, to either select against (D-valine) or for (D-alanine) cells containing transgenic plastids. Positive/negative selection with d-amino acids was effective in vitro and against transplastomic seedlings grown in soil. The dual functionality of dao is highly suited to the polyploid plastid compartment, where it can be used to provide tolerance against potential D-alanine-based herbicides, control the timing of recombination events such as marker excision, influence the segregation of transgenic plastid genomes, identify loci affecting dao function in mutant screens, and develop D-valine-based methods to manage the spread of transgenic plastids tagged with dao.","doi":"10.1104/pp.112.204107","authors":"Gisby MF, Mudd EA, Day A","authors_abbrev":"Gisby MF et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-10-23","publication_year":"2012","canto_session_key":"08e1fa02cea14b7d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-05-23 15:43:46","canto_approved_date":"2025-03-02 16:34:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-17 10:39:39","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1450.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-05-23"},{"uniquename":"PMID:29392410","title":"STEEx, a boundary between the world of quiescence and the vegetative cycle.","citation":"Curr Genet 2018 Aug;64(4):901-905","abstract":"Telomere maintenance mechanism is poorly studied in quiescence, a reversible non-proliferative state. We previously described in fission yeast a new mode of repair of telomeres named STEEx, that specifically operates in post-mitotic cells harboring eroded telomeres. This mechanism, promoted by transcription-induced telomeric recombination, prevents cells to exit properly from quiescence, suggesting that STEEx act as an anti-proliferative barrier. Here, we further showed that STEEx are genetically controlled by the Tel1 ATM - and Rad3 ATR - dependent DDR pathways. We discussed the possibility that STEEx represent a boundary between quiescence and vegetative cycle.","doi":"10.1007/s00294-018-0808-x","authors":"Maestroni L, Géli V, Coulon S","authors_abbrev":"Maestroni L et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-02-03","publication_year":"2018","canto_session_key":"5508511871f7de91","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-02-04 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21098718","title":"Important characteristics of sequence-specific recombination hotspots in Schizosaccharomyces pombe.","citation":"Genetics 2011 Feb;187(2):385-96","abstract":"In many organisms, meiotic recombination occurs preferentially at a limited number of sites in the genome known as hotspots. In the fission yeast Schizosaccharomyces pombe, simple sequence motifs determine the location of at least some, and possibly most or all, hotspots. Recently, we showed that a large number of different sequences can create hotspots. Among those sequences we identified some recurring motifs that fell into at least five distinct families, including the well-characterized CRE family of hotspots. Here we report the essential sequence for activity of two of the novel hotspots, the oligo-C and CCAAT hotspots, and identify associated trans-acting factors required for hotspot activity. The oligo-C hotspot requires a unique 8-bp sequence, CCCCGCAC, though hotspot activity is also significantly affected by adjacent nucleotides. The CCAAT hotspot requires a more complex and degenerate sequence, including the originally identified seven nucleotide CCAATCA sequence at its core. We identified transcription factors, the CCAAT-binding factor (CBF) and Rst2, which are required specifically for activity of the CCAAT hotspots and oligo-C hotspots, respectively. Each of these factors binds to its respective motifs in vitro. However, unlike CRE, the sequence required for hotspot activity is larger than the sequence required for binding, suggesting the involvement of additional factors.","doi":"10.1534/genetics.110.124636","authors":"Steiner WW, Davidow PA, Bagshaw AT","authors_abbrev":"Steiner WW et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2010-11-25","publication_year":"2011","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16496115","title":"Studies on inositol-mediated expression of MAL gene encoding maltase and phospholipid biosynthesis in Schizosaccharomyces pombe.","citation":"J Ind Microbiol Biotechnol 2006 Jun;33(6):417-22","abstract":"In this study, the effects of inositol addition on expression of the MAL gene encoding maltase and phosphatidylinositol (PI) biosynthesis in Schizosaccharomyces pombe (a naturally inositol-requiring strain) were examined. We found that specific maltase activity was at its maximum when the concentration of added inositol reached 6 microg ml(-1) in a synthetic medium containing 2.0% (w/v) glucose. When the concentration of added inositol was 1 microg ml(-1) in the medium, repression of MAL gene expression occurred at glucose concentration higher than 0.2% (w/v). However, when S. pombe was cultured in the synthetic medium containing 6 microg ml(-1), repression of maltase gene expression occurred only at initial glucose concentration above 1.0% (w/v). More mRNA encoding maltase was detected in the cells grown in the medium with 6 microg ml(-1) inositol than in those grown in the same medium with 1 microg ml(-1) inositol. These results demonstrate that higher inositol concentrations in the synthetic medium could derepress MAL gene expression in S. pombe. PI content of the yeast cells grown in the synthetic medium with 6 microg ml(-1) of inositol was higher than that of the yeast cells grown in the same medium with 1 microg ml(-1) of inositol. This means that PI may be involved in the derepression of MAL gene expression in S. pombe.","authors":"Yao S, Chi Z, He S","authors_abbrev":"Yao S et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-02-24","publication_year":"2006","canto_session_key":"262964f9a96d875c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-05-21 13:37:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-05-21 13:37:32","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1683.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-05-21"},{"uniquename":"PMID:6230353","title":"Independent loci for the structural genes of the yeast mitochondrial alpha and beta ATPase subunits.","citation":"J Biol Chem 1984 Mar 10;259(5):2845-9","abstract":"In the yeast Schizosaccharomyces pombe, the structural gene mutations A23-13 (alpha-) and B59-1 (beta-) which totally prevent the expression of either the alpha or the beta subunits of the mitochondrial ATPase, were shown by classical genetic mapping studies to be both located on chromosome I but genetically unlinked. It is concluded that the structural genes ATP1 and ATP2 for the alpha and beta subunits of the mitochondrial ATPase are not organized in a cluster. By both meiotic recombination frequency analysis and gene transfer studies, three single nuclear mutations affecting to different extents the electrophoretic mobility of the beta polypeptide were located on the chromosome I very close to the mutation B59-1 (beta-). Two mutations involved a defective ATPase activity and the inability to grow on glycerol (gly). One of these mutants E5-23 (beta\") exhibited a beta subunit of slightly reduced electrophoretic mobility. The other mutation F1-10 (beta) was associated with a beta subunit of normal electrophoretic mobility. The plasmid pMa2 (Boutry, M., Vassarotti, A., Ghislain, M., Douglas, M., Goffeau, A. (1984) J. Biol. Chem. 259, 2840-2844) containing the structural gene for the beta subunit complemented the mutants E5-23 (beta\") and F1-10 (beta) as well as B59-1 (beta-). These three mutations are therefore likely to affect the beta structural gene itself or a very contiguous gene contained in the 5.4-kilobase genomic insert of pMa2. The mutation F1-10 (beta) was mapped between E5-23 (beta\") and B59-1 (beta-) by analysis of the meiotic recombination frequencies. Another mutation F25-28-11 (beta') was responsible for an appreciable decrease of electrophoretic mobility of the beta subunit which, however, did not affect either the ATPase activity or the ability to grow on glycerol (GLY). This mutant transformed by pMa2 was able to express the structural gene for the wild type beta subunit and the resulting transformants synthesized and assembled both the beta and beta' subunits. It is concluded that the mutation F25-28-11 (beta') also affects the structural gene for the beta subunit and does not affect genes controlling the processing machinery.","authors":"Vassarotti A, Boutry M, Colson AM, Goffeau A","authors_abbrev":"Vassarotti A et al.","pubmed_publication_date":"10 Mar 1984","pubmed_entrez_date":"1984-03-10","publication_year":"1984","canto_session_key":"c97b2eb2fa87d8f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-05 17:04:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-04 13:09:07","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-09-04"},{"uniquename":"EMBL:AB084855","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.43"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11504566","title":"The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p.","citation":"BMC Biochem 2001;2:7","abstract":"The function of the fission yeast cullins Pcu1p and Pcu4p requires modification by the ubiquitin-related peptide Ned8p. A recent report by Lyapina et al. shows that the COP9/signalosome (CSN), a multifunctional eight subunit complex, regulates Ned8p modification of Pcu1p. Disruption of caa1/csn1, which encodes subunit 1 of the putative S. pombe CSN, results in accumulation of Pcu1p exclusively in the modified form. However, it remained unclear whether this reflects global control of all cullins by the entire CSN complex.\nWe demonstrate that multiple CSN subunits control Ned8p modification of Pcu3p, another fission yeast cullin, which, in complex with the RING domain protein Pip1p, forms a ubiquitin ligase that functions in cellular stress response. Pcu3p is modified by Ned8p on Lys 729 and accumulates exclusively in the neddylated form in cells lacking the CSN subunits 1, 3, 4, and 5. These CSN subunits co-elute with Pcu3p in gel filtration fractions corresponding to approximately 550 kDa and specifically bind both native and Ned8p-modified Pcu3p in vivo. While CSN does not influence the subcellular localization of Pcu3p, Pcu3p-associated in vitro ubiquitin ligase activity is stimulated in the absence of CSN.\nTaken together, our data suggest that CSN is a global regulator of Ned8p modification of multiple cullins and potentially other proteins involved in cellular regulation.","authors":"Zhou C, Seibert V, Geyer R, Rhee E, Lyapina S, Cope G, Deshaies RJ, Wolf DA","authors_abbrev":"Zhou C et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-08-16","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.03","SPAC22A12.03c","SPBC215.03c","SPBC12D12.08c","SPAC1687.13c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:36629411","title":"The Fission Yeast Mating-Type Switching Motto: \"One-for-Two\" and \"Two-for-One\".","citation":"Microbiol Mol Biol Rev 2023 Mar 21;87(1):e0000821","abstract":"Schizosaccharomyces pombe is an ascomycete fungus that divides by medial fission; it is thus commonly referred to as fission yeast, as opposed to the distantly related budding yeast Saccharomyces cerevisiae. The reproductive lifestyle of S. pombe relies on an efficient genetic sex determination system generating a 1:1 sex ratio and using alternating haploid/diploid phases in response to environmental conditions. In this review, we address how one haploid cell manages to generate two sister cells with opposite mating types, a prerequisite to conjugation and meiosis. This mating-type switching process depends on two highly efficient consecutive asymmetric cell divisions that rely on DNA replication, repair, and recombination as well as the structure and components of heterochromatin. We pay special attention to the intimate interplay between the genetic and epigenetic partners involved in this process to underscore the importance of basic research and its profound implication for a better understanding of chromatin biology.","doi":"10.1128/mmbr.00008-21","authors":"Arcangioli B, Gangloff S","authors_abbrev":"Arcangioli B et al.","pubmed_publication_date":"21 Mar 2023","pubmed_entrez_date":"2023-01-11","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-01-12 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12242222","title":"The Scw1 RNA-binding domain protein regulates septation and cell-wall structure in fission yeast.","citation":"Genetics 2002 Sep;162(1):45-58","abstract":"Loss of the nonessential RNA-binding domain protein, Scw1, increases resistance to cell-wall-degrading enzymes in fission yeast. Surprisingly, scw1 null mutations also suppress the lethality of mutations (cdc11-136, cdc7-24, cdc14-118, sid1-239, sid2-250, sid3-106, sid4-A1, and mob1-1) at all levels of the sid pathway. This pathway forms part of the septation initiation network (SIN), which regulates the onset of septum formation and ensures the proper coupling of mitosis to cytokinesis. In contrast, scw1(-) mutations do not suppress ts alleles of the rng genes, cdc12 or cdc15. These mutations also prevent the formation of a septum and in addition block assembly and/or function of the contractile acto-myosin ring. sid mutants exhibit a hyper-sensitivity to cell-wall-degrading enzymes that is suppressed by loss of Scw1. Furthermore, scw1(-)-mediated rescue of sid mutants is abolished in the presence of calcofluor white, a compound that interferes with cell-wall synthesis. These data suggest that Scw1 acts in opposition to the SIN as a negative regulator of cell-wall/septum deposition. Unlike components of the SIN, Scw1 is predominantly a cytoplasmic protein and is not localized to the spindle pole body.","authors":"Karagiannis J, Oulton R, Young PG","authors_abbrev":"Karagiannis J et al.","pubmed_publication_date":"Sep 2002","pubmed_entrez_date":"2002-09-21","publication_year":"2002","canto_session_key":"3e87e38190d31d91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-18 18:20:41","canto_approved_date":"2022-09-04 08:52:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-18 18:16:52","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.11c","SPBC244.01c","SPBC24C6.07","SPAC6F6.08c","SPAC9G1.09","SPBC21.06c","SPBC428.13c","SPAC24B11.11c","SPAC1565.06c","SPCC16C4.07"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2017-07-18"},{"uniquename":"PMID:18523008","title":"Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells.","citation":"Proc Natl Acad Sci U S A 2008 Jun 10;105(23):8014-9","abstract":"Two functions are proposed for the conserved family of UCS proteins: helping to fold myosin motor proteins and stimulating the motor function of folded myosins. We examined both functions in yeast. The fission yeast UCS protein (Rng3p) concentrates in nodes containing myosin-II (Myo2) and other proteins that condense into the cytokinetic contractile ring. Both the N-terminal (central) and C-terminal (UCS) domains of Rng3p can concentrate independently in contractile rings, but only full-length Rng3p supports contractile ring function in vivo. The presence of Rng3p in ATPase assays doubles the apparent affinity (K(ATPase)) of both native Myo2 and recombinant heads of Myo2 for actin filaments. Rng3p promotes gliding of actin filaments by full-length Myo2 molecules, but not Myo2 heads alone. Myo2 isolated from mutant strains defective for Rng3p function is soluble and supports actin filament gliding. In budding yeast the single UCS protein (She4p) acts on both myosin-I isoforms (Myo3p and Myo5p) and one of two myosin-V isoforms (Myo4p). Myo5p turns over approximately 10 times faster in she4Delta cells than wild-type cells, reducing the level of Myo5p in cells 10-fold and in cortical actin patches approximately 4-fold. Nevertheless, Myo5p isolated from she4Delta cells has wild-type ATPase and motility activities. Thus, a fraction of this yeast myosin can fold de novo in the absence of UCS proteins, but UCS proteins promote myosin stability and interactions with actin.","doi":"10.1073/pnas.0802874105","authors":"Lord M, Sladewski TE, Pollard TD","authors_abbrev":"Lord M et al.","pubmed_publication_date":"10 Jun 2008","pubmed_entrez_date":"2008-06-05","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22101932","title":"Tel1ATM and Rad3ATR kinases promote Ccq1-Est1 interaction to maintain telomeres in fission yeast.","citation":"Nat Struct Mol Biol 2011 Nov 20;18(12):1408-13","abstract":"The evolutionarily conserved shelterin complex has been shown to play both positive and negative roles in telomerase regulation in mammals and fission yeast. Although shelterin prevents the checkpoint kinases ATM and ATR from fully activating DNA damage responses at telomeres in mammalian cells, those kinases also promote telomere maintenance. In fission yeast, cells lacking both Tel1 (ATM ortholog) and Rad3 (ATR ortholog) fail to recruit telomerase to telomeres and survive by circularizing chromosomes. However, the critical telomere substrate(s) of Tel1(ATM) and Rad3(ATR) was unknown. Here we show that phosphorylation of the shelterin subunit Ccq1 on Thr93, redundantly mediated by Tel1(ATM) and/or Rad3(ATR), is essential for telomerase association with telomeres. In addition, we show that the telomerase subunit Est1 interacts directly with the phosphorylated Thr93 of Ccq1 to ensure telomere maintenance. The shelterin subunits Taz1, Rap1 and Poz1 (previously established inhibitors of telomerase) were also found to negatively regulate Ccq1 phosphorylation. These findings establish Tel1(ATM)/Rad3(ATR)-dependent Ccq1 Thr93 phosphorylation as a critical regulator of telomere maintenance in fission yeast.","doi":"10.1038/nsmb.2187","authors":"Moser BA, Chang YT, Kosti J, Nakamura TM","authors_abbrev":"Moser BA et al.","pubmed_publication_date":"20 Nov 2011","pubmed_entrez_date":"2011-11-22","publication_year":"2011","canto_session_key":"5bc2f7e622b6ae01","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.07","SPBC216.05","SPBC1778.02","SPCC23B6.03c","SPNCRNA.214","SPAC6F6.16c","SPBC2D10.13"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:7798319","title":"Bypassing anaphase by fission yeast cut9 mutation: requirement of cut9+ to initiate anaphase.","citation":"J Cell Biol 1994 Dec;127(6 Pt 1):1655-70","abstract":"A novel anaphase block phenotype was found in fission yeast temperature-sensitive cut9 mutants. Cells enter mitosis with chromosome condensation and short spindle formation, then block anaphase, but continue to progress into postanaphase events such as degradation of the spindle, reformation of the postanaphase cytoplasmic microtubule arrays, septation, and cytokinesis. The cut9 mutants are defective in the onset of anaphase and possibly in the restraint of postanaphase events until the completion of anaphase. The cut9+ gene encodes a 78-kD protein containing the 10 34-amino acid repeats, tetratricopeptide repeats (TPR), and similar to budding yeast Cdc16. It is essential for viability, and the mutation sites reside in the TPR. The three genes, namely, nuc2+, scn1+, and scn2+, genetically interact with cut9+. The nuc2+ and cut9+ genes share an essential function to initiate anaphase. The cold-sensitive scn1 and scn2 mutations, defective in late anaphase, can suppress the ts phenotype of cut9.","authors":"Samejima I, Yanagida M","authors_abbrev":"Samejima I et al.","pubmed_publication_date":"Dec 1994","pubmed_entrez_date":"1994-12-01","publication_year":"1994","canto_session_key":"720a7afb1d87000c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-07-16 11:53:15","canto_approved_date":"2024-03-28 17:47:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-05-15 10:58:45","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPATRNAALA.02","SPAC17C9.01c","SPATRNAALA.03","SPAC6F12.15c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-07-16"},{"uniquename":"PMID:24104454","title":"Functional role and analysis of cysteine residues of the salt tolerance protein Sod2.","citation":"Mol Cell Biochem 2014 Jan;386(1-2):85-98","abstract":"Sod2 is the major salt tolerance plasma membrane protein of Schizosaccharomyces pombe. It functions to remove excess intracellular sodium (or lithium) in exchange for protons. We investigated the role of cysteine residues and created a cysteine-free Sod2 protein. Each cysteine residue of the ten present was individually mutated to serine and the different proteins expressed and characterized in S. pombe. Western blotting revealed that all the individual mutant proteins were expressed. We examined the ability of the mutant proteins to confer salt tolerance to S. pombe with the endogenous Sod2 protein deleted. Only proteins with C26S and C374S mutations were partially reduced in their ability to confer salt tolerance. Additionally, they showed a change in conformation in comparison to the wild-type protein, indicated by differential sensitivity to trypsin. Deletion of all the cysteine residues of Sod2 resulted in a functional protein that was expressed in S. pombe at levels similar to the wild type and also conferred salt tolerance. The conformation of the cysteine-free Sod2 protein was not altered relative to the wild-type protein. We examined the accessibility of amino acids of the cysteineless protein present on putative extracellular loop 2. A cysteine placed at position Ala119 was accessible to externally applied [2-(trimethylammonium)ethyl] methane thiosulfonate bromide. The results demonstrate that cysteines in the Sod2 protein can be changed to serine residues resulting in an expressed, functional protein. The utility of the cysteine-free Sod2 protein for determination of topology and amino acid accessibility is demonstrated.","doi":"10.1007/s11010-013-1847-8","authors":"Ullah A, El-Magd RA, Fliegel L","authors_abbrev":"Ullah A et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2013-10-10","publication_year":"2014","canto_session_key":"8c750b6746d9f779","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 13:46:50","canto_approved_date":"2022-06-14 15:30:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-30 11:48:10","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-31"},{"uniquename":"PMID:556756","title":"Structure of mitochondria and vacuoles of Candida utilis and Schizosaccharomyces pombe studied by electron microscopy of serial thin sections and model building.","citation":"J Gen Microbiol 1977 Jan;98(1):147-53","abstract":"The structure of mitochondria and of vacuoles in Candida utilis and Schizosaccharomyces pombe has been studied by electron microscopy of serial thin sections and subsequent model building. The models of the two cells of C. utilis which were studied confirmed our earlier findings, made by high voltage electron microscopy of thick sections, that there is a single, branched and continuous mitochondrial network in the cell (Davison & Garland, 1975). A model of a S. pombe cell showed that the mitochondrial structure was far more continuous than expected from inspection of thin sections, there being but two large and two small mitochondria. The models demonstrated that the few large vacuoles in C. utilis were interconnected into a single cluster, whereas in S. pombe there were two separate complexes of interconnected vacuoles towards each pole of the cell.","authors":"Davison MT, Garland PB","authors_abbrev":"Davison MT et al.","pubmed_publication_date":"Jan 1977","pubmed_entrez_date":"1977-01-01","publication_year":"1977","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25691662","title":"Casein kinase 1γ ensures monopolar growth polarity under incomplete DNA replication downstream of Cds1 and calcineurin in fission yeast.","citation":"Mol Cell Biol 2015 May;35(9):1533-42","abstract":"Cell polarity is essential for various cellular functions during both proliferative and developmental stages, and it displays dynamic alterations in response to intracellular and extracellular cues. However, the molecular mechanisms underlying spatiotemporal control of polarity transition are poorly understood. Here, we show that fission yeast Cki3 (a casein kinase 1γ homolog) is a critical regulator to ensure persistent monopolar growth during S phase. Unlike the wild type, cki3 mutant cells undergo bipolar growth when S phase is blocked, a condition known to delay transition from monopolar to bipolar growth (termed NETO [new end takeoff]). Consistent with this role, Cki3 kinase activity is substantially increased, and cells lose their viability in the absence of Cki3 upon an S-phase block. Cki3 acts downstream of the checkpoint kinase Cds1/Chk2 and calcineurin, and the latter physically interacts with Cki3. Autophosphorylation in the C terminus is inhibitory toward Cki3 kinase activity, and calcineurin is responsible for its dephosphorylation. Cki3 localizes to the plasma membrane, and this localization requires the palmitoyltransferase complex Erf2-Erf4. Membrane localization is needed not only for proper NETO timing but also for Cki3 kinase activity. We propose that Cki3 acts as a critical inhibitor of cell polarity transition under S-phase arrest.","doi":"10.1128/MCB.01465-14","authors":"Koyano T, Konishi M, Martin SG, Ohya Y, Hirata D, Toda T, Kume K","authors_abbrev":"Koyano T et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-02-19","publication_year":"2015","canto_session_key":"8656ddc9240734bd","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-02-20 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1805.05","SPAC3H5.06c","SPBP4H10.04","SPAC3C7.12"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:38604460","title":"The Schizosaccharomyces pombe DEAD-box protein Mss116 is required for mitoribosome assembly and mitochondrial translation.","citation":"Mitochondrion 2024 Apr 09;76:101881","abstract":"DEAD-box helicases are important players in mitochondrial gene expression, which is necessary for mitochondrial respiration. In this study, we characterized Schizosaccharomyces pombe Mss116 (spMss116), a member of the family of DEAD-box RNA helicases. Deletion of spmss116 in a mitochondrial intron-containing background significantly reduced the levels of mitochondrial DNA (mtDNA)-encoded cox1 and cob1 mRNAs and impaired mitochondrial translation, leading to a severe respiratory defect and a loss of cell viability during stationary phase. Deletion of mitochondrial introns restored the levels of cox1 and cob1 mRNAs to wide-type (WT) levels but could not restore mitochondrial translation and respiration in Δspmss116 cells. Furthermore, deletion of spmss116 in both mitochondrial intron-containing and intronless backgrounds impaired mitoribosome assembly and destabilization of mitoribosomal proteins. Our findings suggest that defective mitochondrial translation caused by deletion of spmss116 is most likely due to impaired mitoribosome assembly.","doi":"10.1016/j.mito.2024.101881","authors":"Wang Y, Feng G, Huang Y","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"09 Apr 2024","pubmed_entrez_date":"2024-04-11","publication_year":"2024","canto_session_key":"0b47b3720f6a23d9","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-04-12 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26134317","title":"Epigenetic Regulation of Chromatin States in Schizosaccharomyces pombe.","citation":"Cold Spring Harb Perspect Biol 2015 Jul 01;7(7):a018770","abstract":"This article discusses the advances made in epigenetic research using the model organism fission yeast Schizosaccharomyces pombe. S. pombe has been used for epigenetic research since the discovery of position effect variegation (PEV). This is a phenomenon in which a transgene inserted within heterochromatin is variably expressed, but can be stably inherited in subsequent cell generations. PEV occurs at centromeres, telomeres, ribosomal DNA (rDNA) loci, and mating-type regions of S. pombe chromosomes. Heterochromatin assembly in these regions requires enzymes that modify histones and the RNA interference (RNAi) machinery. One of the key histone-modifying enzymes is the lysine methyltransferase Clr4, which methylates histone H3 on lysine 9 (H3K9), a classic hallmark of heterochromatin. The kinetochore is assembled on specialized chromatin in which histone H3 is replaced by the variant CENP-A. Studies in fission yeast have contributed to our understanding of the establishment and maintenance of CENP-A chromatin and the epigenetic activation and inactivation of centromeres.","doi":"10.1101/cshperspect.a018770","authors":"Allshire RC, Ekwall K","authors_abbrev":"Allshire RC et al.","pubmed_publication_date":"01 Jul 2015","pubmed_entrez_date":"2015-07-03","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-07-04 00:22:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37828292","title":"Experimental phasing opportunities for macromolecular crystallography at very long wavelengths.","citation":"Commun Chem 2023 Oct 12;6(1):219","abstract":"Despite recent advances in cryo-electron microscopy and artificial intelligence-based model predictions, a significant fraction of structure determinations by macromolecular crystallography still requires experimental phasing, usually by means of single-wavelength anomalous diffraction (SAD) techniques. Most synchrotron beamlines provide highly brilliant beams of X-rays of between 0.7 and 2 Å wavelength. Use of longer wavelengths to access the absorption edges of biologically important lighter atoms such as calcium, potassium, chlorine, sulfur and phosphorus for native-SAD phasing is attractive but technically highly challenging. The long-wavelength beamline I23 at Diamond Light Source overcomes these limitations and extends the accessible wavelength range to λ = 5.9 Å. Here we report 22 macromolecular structures solved in this extended wavelength range, using anomalous scattering from a range of elements which demonstrate the routine feasibility of lighter atom phasing. We suggest that, in light of its advantages, long-wavelength crystallography is a compelling option for experimental phasing.","doi":"10.1038/s42004-023-01014-0","authors":"El Omari K, Duman R, Mykhaylyk V, Orr CM, Latimer-Smith M, Winter G, Grama V, Qu F, Bountra K, Kwong HS, Romano M, Reis RI, Vogeley L, Vecchia L, Owen CD, Wittmann S, Renner M, Senda M, Matsugaki N, Kawano Y, Bowden TA, Moraes I, Grimes JM, Mancini EJ, Walsh MA, Guzzo CR, Owens RJ, Jones EY, Brown DG, Stuart DI, Beis K, Wagner A","authors_abbrev":"El Omari K et al.","pubmed_publication_date":"12 Oct 2023","pubmed_entrez_date":"2023-10-12","publication_year":"2023","canto_session_key":"9fd2306cbf163d07","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-11-11 12:02:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC222.09"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"8px5","gene_chains":[{"gene_uniquename":"SPAC222.09","chain":"A","position":"388-540"}],"title":"Structure of the RNA recognition motif (RRM) of Seb1 from S. pombe., solved at wavelength 2.75 A","entry_authors":"El Omari K,Duman R,Mykhaylyk V,Orr C,Wittmann S,Renner M,Grimes JM,Wagner A","entry_authors_abbrev":"El Omari K et al.","reference_uniquename":"PMID:37828292","experimental_method":"X-ray","resolution":"1.77"}]},{"uniquename":"PMID:32099016","title":"Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells.","citation":"Sci Rep 2020 Feb 25;10(1):3422","abstract":"Ribosome stalling triggers the ribosome-associated quality control (RQC) pathway, which targets collided ribosomes and leads to subunit dissociation, followed by proteasomal degradation of the nascent peptide. In yeast, RQC is triggered by Hel2-dependent ubiquitination of uS10, followed by subunit dissociation mediated by the RQC-trigger (RQT) complex. In mammals, ZNF598-dependent ubiquitination of collided ribosomes is required for RQC, and activating signal cointegrator 3 (ASCC3), a component of the ASCC complex, facilitates RQC. However, the roles of other components and associated factors of the ASCC complex remain unknown. Here, we demonstrate that the human RQC-trigger (hRQT) complex, an ortholog of the yeast RQT complex, plays crucial roles in RQC. The hRQT complex is composed of ASCC3, ASCC2, and TRIP4, which are orthologs of the RNA helicase Slh1(Rqt2), ubiquitin-binding protein Cue3(Rqt3), and zinc-finger type protein yKR023W(Rqt4), respectively. The ATPase activity of ASCC3 and the ubiquitin-binding activity of ASCC2 are crucial for triggering RQC. Given the proposed function of the RQT complex in yeast, we propose that the hRQT complex recognizes the ubiquitinated stalled ribosome and induces subunit dissociation to facilitate RQC.","doi":"10.1038/s41598-020-60241-w","authors":"Hashimoto S, Sugiyama T, Yamazaki R, Nobuta R, Inada T","authors_abbrev":"Hashimoto S et al.","pubmed_publication_date":"25 Feb 2020","pubmed_entrez_date":"2020-02-27","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1906.02c","SPAC1A6.01c","SPBC13G1.10c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:35348762","title":"Facultative heterochromatin formation in rDNA is essential for cell survival during nutritional starvation.","citation":"Nucleic Acids Res 2022 Apr 22;50(7):3727-3744","abstract":"During the cellular adaptation to nutrient starvation, cells temporarily decelerate translation processes including ribosomal biogenesis. However, the mechanisms repressing robust gene expression from the ribosomal gene cluster (rDNA) are unclear. Here, we demonstrate that fission yeast cells facing glucose starvation assemble facultative heterochromatin in rDNA leading to its transcriptional repression. Glucose starvation induces quick dissociation of the ATF/CREB-family protein Atf1 from rDNA, where in turn the histone chaperone FACT is recruited to promote H3K9 methylation and heterochromatinization. We also identify the histone acetyltransferase Gcn5 as a repressor of rDNA heterochromatinization in glucose-rich conditions, and this protein dissociates from rDNA upon glucose starvation. Facultative heterochromatin formation in rDNA requires histone deacetylases Clr3 and both the RNAi-dependent and -independent gene silencing pathways. This is essential in adaptation to starvation since mutants lacking heterochromatin formation in rDNA lead to untimely cell death during glucose starvation.","doi":"10.1093/nar/gkac175","authors":"Hirai H, Takemata N, Tamura M, Ohta K","authors_abbrev":"Hirai H et al.","pubmed_publication_date":"22 Apr 2022","pubmed_entrez_date":"2022-03-29","publication_year":"2022","canto_session_key":"bec47e43d1cbc2f7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-03-31 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25806539","title":"A cascade of iron-containing proteins governs the genetic iron starvation response to promote iron uptake and inhibit iron storage in fission yeast.","citation":"PLoS Genet 2015 Mar;11(3):e1005106","abstract":"Iron is an essential cofactor, but it is also toxic at high levels. In Schizosaccharomyces pombe, the sensor glutaredoxin Grx4 guides the activity of the repressors Php4 and Fep1 to mediate a complex transcriptional response to iron deprivation: activation of Php4 and inactivation of Fep1 leads to inhibition of iron usage/storage, and to promotion of iron import, respectively. However, the molecular events ruling the activity of this double-branched pathway remained elusive. We show here that Grx4 incorporates a glutathione-containing iron-sulfur cluster, alone or forming a heterodimer with the BolA-like protein Fra2. Our genetic study demonstrates that Grx4-Fra2, but not Fep1 nor Php4, participates not only in iron starvation signaling but also in iron-related aerobic metabolism. Iron-containing Grx4 binds and inactivates the Php4 repressor; upon iron deprivation, the cluster in Grx4 is probably disassembled, the proteins dissociate, and Php4 accumulates at the nucleus and represses iron consumption genes. Fep1 is also an iron-containing protein, and the tightly bound iron is required for transcriptional repression. Our data suggest that the cluster-containing Grx4-Fra2 heterodimer constitutively binds to Fep1, and upon iron deprivation the disassembly of the iron cluster between Grx4 and Fra2 promotes reverse metal transfer from Fep1 to Grx4-Fra2, and de-repression of iron-import genes. Our genetic and biochemical study demonstrates that the glutaredoxin Grx4 independently governs the Php4 and Fep1 repressors through metal transfer. Whereas iron loss from Grx4 seems to be sufficient to release Php4 and allow its nuclear accumulation, total or partial disassembly of the Grx4-Fra2 cluster actively participates in iron-containing Fep1 activation by sequestering its iron and decreasing its interaction with promoters.","doi":"10.1371/journal.pgen.1005106","authors":"Encinar del Dedo J, Gabrielli N, Carmona M, Ayté J, Hidalgo E","authors_abbrev":"Encinar del Dedo J et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-03-26","publication_year":"2015","canto_session_key":"4f30f3893b88315a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Javier Encinar","canto_first_approved_date":"2017-03-29 16:42:18","canto_approved_date":"2024-12-10 15:06:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-29 16:48:30","canto_added_date":"2015-03-27 01:15:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Javier Encinar","community_curator":true,"annotation_count":21,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23E2.01","SPAC23G3.03","SPCC645.03c","SPAC8C9.11","SPBC26H8.06","SPBC16E9.01c","SPAC22F3.10c","SPBC1683.10c","SPAC1F7.08","SPAC1F8.03c"],"gene_count":10,"ltp_gene_count":5,"approved_date":"2017-03-29"},{"uniquename":"PMID:15724441","title":"Identification of conserved polar residues important for salt tolerance by the Na+/H+ exchanger of Schizosaccharomyces pombe.","citation":"Mol Cell Biochem 2005 Jan;268(1-2):83-92","abstract":"The Na+/H+ exchanger is a ubiquitous protein that transports Na+ and H+ in opposite directions across cell membranes. In fission yeast, the Na+/H+ exchanger sod2 plays a major role in the removal of excess detrimental intracellular sodium. The effect of mutagenesis of conserved polar amino acids of sod2 was examined by expressing 10 different mutant forms of sod2 in sod2 deficient S. pombe and characterizing salt tolerance. Asp145, 266, 267, and Glu173 were critical for proper function of sod2. Asp241 had an intermediate effect on sod2 function while mutation of Asp178 did not impair sod2 function. Simultaneous mutation of the Asp266, 267 pair impaired sod2 function. Mutation of each individual residue demonstrated that both were critical for sod2 function. Conservative mutations (Asp to Glu) of Asp266 and 267 failed to restore sod2 function. The results suggest that acidic residues associated with transmembrane segments are important in function, possibly being important in binding and coordinating cations.","authors":"Fliegel L","authors_abbrev":"Fliegel L","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2005-02-24","publication_year":"2005","canto_session_key":"5fabf4733ea9413f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 13:49:05","canto_approved_date":"2023-09-08 06:44:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-30 18:04:39","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-31"},{"uniquename":"PMID:15545638","title":"A natural meiotic DNA break site in Schizosaccharomyces pombe is a hotspot of gene conversion, highly associated with crossing over.","citation":"Genetics 2005 Feb;169(2):595-605","abstract":"In Schizosaccharomyces pombe, meiosis-specific DNA breaks that initiate recombination are observed at prominent but widely separated sites. We investigated the relationship between breakage and recombination at one of these sites, the mbs1 locus on chromosome I. Breaks corresponding to 10% of chromatids were mapped to four clusters spread over a 2.1-kb region. Gene conversion of markers within the clusters occurred in 11% of tetrads (3% of meiotic chromatids), making mbs1 a conversion hotspot when compared to other fission yeast markers. Approximately 80% of these conversions were associated with crossing over of flanking markers, suggesting a strong bias in meiotic break repair toward the generation of crossovers. This bias was observed in conversion events at three other loci, ade6, ade7, and ura1. A total of 50-80% of all crossovers seen in a 90-kb region flanking mbs1 occurred in a 4.8-kb interval containing the break sites. Thus, mbs1 is also a hotspot of crossing over, with breakage at mbs1 generating most of the crossovers in the 90-kb interval. Neither Rec12 (Spo11 ortholog) nor I-SceI-induced breakage at mbs1 was significantly associated with crossing over in an apparently break-free interval >25 kb away. Possible mechanisms for generating crossovers in such break-free intervals are discussed.","authors":"Cromie GA, Rubio CA, Hyppa RW, Smith GR","authors_abbrev":"Cromie GA et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2004-11-17","publication_year":"2005","canto_session_key":"15e24ccc56c8ba6f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40668835","title":"α-glucan remodeling by GH13-domain enzymes shapes fungal cell wall architecture.","citation":"Proc Natl Acad Sci U S A 2025 Jul 22;122(29):e2505509122","abstract":"Cell walls are critical structures of fungi, bacteria, and plants, providing mechanical strength, maintaining shape, and protecting cells from environmental stress. In the fission yeast  Schizosaccharomyces pombe , the α-glucan synthase Ags1 produces α-1,3-glucan chains essential for cell wall integrity, but how these chains are further assembled into mature polymers is not understood. Here, we identify two conserved glycosylphosphatidylinositol-anchored α-amylase-like enzymes, Aah1 and Aah3, which act redundantly as key contributors to α-glucan network formation. Cells lacking both enzymes exhibit severe growth and morphological defects, including rounded shape, delayed division, and cell clumping. Using solid-state NMR spectroscopy of intact cells, we show that the double mutant cell walls have dramatically reduced α-1,3-glucan and galactomannan content, with a compensatory increase in β-glucans driven by the activation of the cell integrity pathway. These changes correlate with cell wall thickening, increased rigidity, and reduced polymer mobility and hydration. We also uncover in vivo polymorphic forms of α- and β-glucans, some of which are selectively lost or gained in the mutant cells. Our data suggest that Aah1 and Aah3 function as GH13-family transglycosylases that collaborate nonredundantly with the α-glucan synthase to build a properly organized α-glucan matrix. These findings highlight a previously unrecognized layer of complexity in fungal cell wall biosynthesis and point to GH13-family enzymes as potential antifungal targets given that related enzymes are found in many fungi.","doi":"10.1073/pnas.2505509122","authors":"Jacob A, Willet AH, Igarashi MG, El Hariri El Nokab M, Turner LA, Alsanad AKA, Wang T, Gould KL","authors_abbrev":"Jacob A et al.","pubmed_publication_date":"22 Jul 2025","pubmed_entrez_date":"2025-07-16","publication_year":"2025","canto_session_key":"6a6fd8723b8d49c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2025-08-26 13:05:20","canto_approved_date":"2026-02-16 16:31:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-08-18 14:50:21","canto_added_date":"2025-07-16 23:25:05","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":29,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPCC757.12","SPBC16A3.13","SPAC23D3.14c","SPCC1281.01","SPBC119.08","SPBC12D12.04c","SPAC25H1.09","SPCC1840.02c","SPCC63.02c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2025-08-26"},{"uniquename":"PMID:18759110","title":"Transcriptional regulators of seven yeast species: comparative genome analysis. Review.","citation":"Folia Microbiol (Praha) 2008;53(4):275-87","abstract":"The regulation of gene transcription allows yeast cells to respond properly to changing environmental conditions. Several protein complexes take part in this process. They involve RNA polymerase complexes, chromatin remodeling complexes, mediators, general transcription factors and specific transcriptional regulators. Using Saccharomyces cerevisiae as reference, the genomes of six species (Ashbya gossypii, Kluyveromyces lactis, K. waltii, Candida albicans, C. glabrata and Schizosaccharomyces pombe) that are human pathogens or important for the food industry were analyzed for their complement of genes encoding the homologous transcriptional regulators. The number of orthologs identified in a given species correlated with its phylogenetic distance from S. cerevisiae. Many duplicated genes encoding transcriptional regulators in S. cerevisiae and C. glabrata were reduced to one copy in species diverged before the ancestral whole genome duplication. Some transcriptional regulators appear to be specific for S. cerevisiae and probably reflect the physiological differences among species. Phylogenetic analysis and conserved gene order relationships indicate that a similar set of gene families involved in the control of multidrug resistance and oxidative stress response already existed in the common ancestor of the compared fungal species.","doi":"10.1007/s12223-008-0044-8","authors":"Drobná E, Bialková A, Subík J","authors_abbrev":"Drobná E et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-09-02","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11152613","title":"Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes.","citation":"J Mol Biol 2001 Jan 19;305(3):567-80","abstract":"We describe and validate a new membrane protein topology prediction method, TMHMM, based on a hidden Markov model. We present a detailed analysis of TMHMM's performance, and show that it correctly predicts 97-98 % of the transmembrane helices. Additionally, TMHMM can discriminate between soluble and membrane proteins with both specificity and sensitivity better than 99 %, although the accuracy drops when signal peptides are present. This high degree of accuracy allowed us to predict reliably integral membrane proteins in a large collection of genomes. Based on these predictions, we estimate that 20-30 % of all genes in most genomes encode membrane proteins, which is in agreement with previous estimates. We further discovered that proteins with N(in)-C(in) topologies are strongly preferred in all examined organisms, except Caenorhabditis elegans, where the large number of 7TM receptors increases the counts for N(out)-C(in) topologies. We discuss the possible relevance of this finding for our understanding of membrane protein assembly mechanisms. A TMHMM prediction service is available at http://www.cbs.dtu.dk/services/TMHMM/.","authors":"Krogh A, Larsson B, von Heijne G, Sonnhammer EL","authors_abbrev":"Krogh A et al.","pubmed_publication_date":"19 Jan 2001","pubmed_entrez_date":"2001-01-12","publication_year":"2001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1687.07","SPAC688.16","SPAC227.01c","SPAC1D4.08","SPAC24H6.01c","SPBPB2B2.02","SPAC17A2.14","SPAPB17E12.08","SPBC27B12.09c","SPBC216.05","SPBC3B8.04c","SPBPJ4664.05","SPBC1271.06c","SPBC29A3.01","SPAC29B12.14c","SPBC776.05","SPCC31H12.02c","SPAC26H5.13c","SPAC959.05c","SPBC1348.05","SPCC1183.11","SPBC13A2.04c","SPAC630.04c","SPBC21B10.09","SPAC1527.01","SPAC3F10.10c","SPAC5H10.11","SPAC23H4.07c","SPBC359.03c","SPBC365.12c","SPBP8B7.04","SPAC1A6.06c","SPCC584.12","SPCC965.11c","SPAC589.12","SPAC732.01","SPAC1687.17c","SPAP14E8.03","SPAC664.09","SPBC776.03","SPAC12B10.09","SPAC24C9.07c","SPBPB2B2.16c","SPAC14C4.10c","SPAC16E8.02","SPBC428.14","SPCC965.13","SPAC24B11.12c","SPAC2F3.08","SPAC25B8.07c","SPCC4B3.04c","SPBP4H10.03","SPBC19C7.05","SPBPB10D8.06c","SPAC23C4.13","SPAC9.10","SPBC530.10c","SPBC16D10.05","SPAPB1A10.07c","SPBC16A3.17c","SPCC63.02c","SPAC13G6.03","SPMIT.01","SPAC105.01c","SPBC839.11c","SPBPB10D8.01","SPCC126.09","SPBC1921.06c","SPAPB2B4.04c","SPBC16A3.12c","SPAC31G5.02","SPBP4H10.19c","SPAC1B3.15c","SPAC3A12.03c","SPBPB8B6.05c","SPAC607.09c","SPAC19B12.06c","SPAC2F3.07c","SPAC824.08","SPCC663.03","SPAC13G6.12c","SPAC1399.03","SPCC736.05","SPAC664.14","SPAC25H1.07","SPAC3A11.09","SPBC365.02c","SPAC1834.05","SPAC1F8.01","SPAC1851.02","SPACUNK4.07c","SPAC17D4.03c","SPBC12C2.09c","SPBCPT2R1.04c","SPCC663.14c","SPCC550.04c","SPAPB15E9.06","SPAC27E2.11c","SPAC17H9.08","SPBC3H7.02","SPCPB1C11.02","SPAC212.01c","SPAPB24D3.09c","SPCC548.03c","SPBC2F12.15c","SPCC70.10","SPBC1348.14c","SPBC1683.12","SPAC5H10.12c","SPCC338.18","SPAC6G10.09","SPBC2G5.01","SPAC4G9.14","SPBC27B12.12c","SPAC3C7.11c","SPBC2A9.08c","SPBC1271.09","SPBC19G7.19","SPBC8D2.09c","SPMIT.09","SPAC26H5.07c","SPAP27G11.02","SPAC23H4.13c","SPAC977.10","SPBC83.16c","SPBP8B7.30c","SPBC119.09c","SPAC2C4.09","SPAC23H3.12c","SPBC354.08c","SPAC823.07","SPCPJ732.03","SPCC11E10.05c","SPAC1782.12c","SPCC757.10","SPBC3E7.05c","SPCC1281.01","SPAC22E12.10c","SPAC26H5.05","SPBC1711.03","SPBC9B6.09c","SPBC21C3.06","SPAC24C9.16c","SPBPB8B6.04c","SPAC5D6.10c","SPAC977.06","SPAC630.11","SPBC1734.04","SPMIT.11","SPBC409.18","SPCC4G3.11","SPCP31B10.06","SPAC2F3.18c","SPAC20G4.07c","SPBC8E4.01c","SPBC27.05","SPAC1F7.03","SPBC3B9.04","SPCC1235.08c","SPAC212.04c","SPBPB2B2.19c","SPAC8F11.08c","SPMIT.10","SPAC688.12c","SPBC119.16c","SPBC26H8.03","SPBC1105.08","SPAC607.07c","SPAC23A1.05","SPBC2F12.17","SPAC167.01","SPBC405.03c","SPBC354.02c","SPAC1039.04","SPBC1198.06c","SPCC1235.11","SPAC5D6.07c","SPAC57A10.07","SPAC869.03c","SPBC19G7.05c","SPBC1711.09c","SPBC4F6.09","SPBC14F5.13c","SPBP26C9.03c","SPCC576.17c","SPBC25H2.14","SPBC17A3.01c","SPAC3G6.05","SPBC1773.08c","SPBPB8B6.06c","SPCC613.01","SPAC9.08c","SPBC19F8.06c","SPCC550.09","SPAC23H3.04","SPAC1786.03","SPBC1289.13c","SPCC970.11c","SPAC6F6.13c","SPBC11G11.01","SPAC644.13c","SPAC2C4.05","SPBC1685.16","SPAC14C4.11","SPAC1783.02c","SPAC56E4.06c","SPCC594.04c","SPBC354.04","SPBC21B10.11","SPAC27E2.07","SPAC6F6.01","SPAC1782.02c","SPCC1393.07c","SPBC1271.08c","SPAC144.18","SPAC16E8.07c","SPAC328.07c","SPBC660.17c","SPBC3E7.15c","SPCC569.05c","SPCC576.04","SPBC1347.04","SPCC1840.02c","SPCC330.20","SPBPB2B2.01","SPAC227.06","SPCC1235.14","SPAC7D4.15c","SPBC947.10","SPAC2E1P5.03","SPAC750.05c","SPBP23A10.02","SPAC23C11.14","SPBPB2B2.07c","SPBC106.07c","SPBC8D2.17","SPBC685.05","SPAC25B8.01","SPCC1795.10c","SPCC320.08","SPAC750.04c","SPBC16E9.03c","SPAC11H11.04","SPAC7D4.06c","SPAC1952.01","SPCC553.12c","SPAC57A7.09","SPBC1348.03","SPCC1322.14c","SPCC645.11c","SPAC1527.02","SPCC622.06c","SPBC1683.05","SPCC1450.07c","SPBC32F12.07c","SPAC4G9.19","SPBCPT2R1.01c","SPCC1020.01c","SPBC12D12.01","SPBC25H2.08c","SPAC750.06c","SPCC1235.17","SPCC1739.15","SPCC14G10.01","SPBC36.03c","SPBC11B10.07c","SPCC962.01","SPBC20F10.07","SPAC29E6.07","SPBC32H8.03","SPBC337.07c","SPAPB15E9.02c","SPBP19A11.02c","SPBC19F8.04c","SPBC3B9.10","SPAPB8E5.10","SPAC3H1.04c","SPBC12C2.13c","SPCPB1C11.03","SPBC887.17","SPBC16H5.09c","SPCC1235.06","SPBC1347.14c","SPAC30.04c","SPCC1795.12c","SPCC1682.01","SPAC144.10c","SPCPB1C11.01","SPAC1A6.10","SPAC12G12.12","SPCC1906.04","SPBC16E9.14c","SPAPB8E5.08","SPCC330.12c","SPAC1786.01c","SPBC609.04","SPAC17G8.08c","SPAC1639.02c","SPAC6C3.06c","SPAC2H10.04","SPBC16H5.14c","SPAC23D3.14c","SPBC1709.03","SPAC1039.01","SPBC19C2.09","SPBC3B8.07c","SPBC887.15c","SPAC6F12.07","SPAC9E9.17c","SPAC16A10.01","SPAC30D11.06c","SPAC1687.08","SPAC17A5.08","SPBC405.02c","SPAC5H10.13c","SPBC30B4.09","SPAC922.09","SPCC1235.16","SPBC19C2.15c","SPCC794.02","SPBC1604.15","SPAC17G6.07c","SPBC1348.01","SPCC16A11.06c","SPAC3H1.05","SPBC947.05c","SPAC186.01","SPACUNK4.08","SPBC16E9.20","SPCC1906.03","SPBC3E7.06c","SPAC8F11.06","SPBC776.14","SPCC1322.07c","SPCC1183.10","SPBC13A2.03","SPBC18A7.02c","SPCC1884.02","SPAC11D3.18c","SPBC1652.02","SPCC1450.06c","SPCC548.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N -Terminus Does Not Govern Protein Turnover of  Schizosaccharomyces pombe  CENP-A.","citation":"Int J Mol Sci 2020 Aug 26;21(17)","abstract":"Centromere integrity underlies an essential framework for precise chromosome segregation and epigenetic inheritance. Although centromeric DNA sequences vary among different organisms, all eukaryotic centromeres comprise a centromere-specific histone H3 variant, centromeric protein A (CENP-A), on which other centromeric proteins assemble into the kinetochore complex. This complex connects chromosomes to mitotic spindle microtubules to ensure accurate partitioning of the genome into daughter cells. Overexpression of CENP-A is associated with many cancers and is correlated with its mistargeting, forming extra-centromeric kinetochore structures. The mislocalization of CENP-A can be counteracted by proteolysis. The amino ( N )-terminal domain (NTD) of CENP-A has been implicated in this regulation and shown to be dependent on the proline residues within this domain in  Saccharomyces cerevisiae  CENP-A, Cse4. We recently identified a proline-rich GRANT motif in the NTD of  Schizosaccharomyces pombe  CENP-A (SpCENP-A) that regulates the centromeric targeting of CENP-A via binding to the CENP-A chaperone Sim3. Here, we investigated whether the NTD is required to confer SpCENP-A turnover (i.e., counter stability) using various truncation mutants of SpCENP-A. We show that sequential truncation of the NTD did not improve the stability of the protein, indicating that the NTD of SpCENP-A does not drive turnover of the protein. Instead, we reproduced previous observations that heterochromatin integrity is important for SpCENP-A stability, and showed that this occurs in an NTD-independent manner. Cells bearing the null mutant of the histone H3 lysine 9 methyltransferase Clr4 ( Δclr4 ), which have compromised constitutive heterochromatin integrity, showed reductions in the proportion of SpCENP-A in the chromatin-containing insoluble fraction of the cell extract, suggesting that heterochromatin may promote SpCENP-A chromatin incorporation. Thus, a disruption in heterochromatin may result in the delocalization of SpCENP-A from chromatin, thus exposing it to protein turnover. Taken together, we show that the NTD is not required to confer SpCENP-A protein turnover.","doi":"10.3390/ijms21176175","authors":"Tan HL, Zeng YB, Chen ES","authors_abbrev":"Tan HL et al.","pubmed_publication_date":"26 Aug 2020","pubmed_entrez_date":"2020-08-30","publication_year":"2020","canto_session_key":"3393d0ea05343004","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-08-31 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084822","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.1234"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24403109","title":"Multifaceted roles of Furry proteins in invertebrates and vertebrates.","citation":"J Biochem 2014 Mar;155(3):137-46","abstract":"Furry (Fry) is a large protein that is evolutionarily conserved from yeast to human. Fry and its orthologues in invertebrates (termed Tao3p in budding yeast, Mor2p in fission yeast, Sax-2 in nematode and Fry in fruit fly) genetically and physically interact with nuclear Dbf2-related (NDR) kinases (termed Cbk1p in budding yeast, Orb6p in fission yeast, Sax-1 in nematode and Trc in fruitfly), and function as activators or scaffolds of these kinases. Fry-NDR kinase signals are implicated in the control of polarized cell growth and morphogenesis in yeast, neurite outgrowth in nematode, and epidermal morphogenesis and dendritic tiling in fruit fly. Recent studies revealed that mammalian Fry is a microtubule-associated protein that is involved in the control of chromosome alignment, spindle organization and Polo-like kinase-1 activation in mitosis, and promotes microtubule acetylation in mitotic spindles via inhibiting the tubulin deacetylase Sirtuin 2. Here, we review current knowledge about the diverse cellular functions and regulation of Fry proteins in invertebrates and vertebrates.","doi":"10.1093/jb/mvu001","authors":"Nagai T, Mizuno K","authors_abbrev":"Nagai T et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-01-10","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB108422","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29414716","title":"Modeling the Dynamics of Cdc42 Oscillation in Fission Yeast.","citation":"Biophys J 2018 Feb 06;114(3):711-722","abstract":"Regulation of polarized cell growth is essential for many cellular processes, including spatial coordination of cell morphology changes during growth and division. We present a mathematical model of the core mechanism responsible for the regulation of polarized growth dynamics by the small GTPase Cdc42. The model is based on the competition of growth zones of Cdc42 localized at the cell tips for a common substrate (inactive Cdc42) that diffuses in the cytosol. We consider several potential ways of implementing negative feedback between Cd42 and its GEF in this model that would be consistent with the observed oscillations of Cdc42 in fission yeast. We analyze the bifurcations in this model as the cell length increases, and total amount of Cdc42 and GEF increase. Symmetric antiphase oscillations at two tips emerge via saddle-homoclinic bifurcations or Hopf bifurcations. We find that a stable oscillation and a stable steady state can coexist, which is consistent with the experimental finding that only 50% of bipolar cells oscillate. The mean amplitude and period can be tuned by parameters involved in the negative feedback. We link modifications in the parameters of the model to observed mutant phenotypes. Our model suggests that negative feedback is more likely to be acting through inhibition of GEF association rather than upregulation of GEF dissociation.","doi":"10.1016/j.bpj.2017.12.007","authors":"Xu B, Jilkine A","authors_abbrev":"Xu B et al.","pubmed_publication_date":"06 Feb 2018","pubmed_entrez_date":"2018-02-08","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-02-09 01:15:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29044765","title":"A novel inborn error of the coenzyme Q10 biosynthesis pathway: cerebellar ataxia and static encephalomyopathy due to COQ5 C-methyltransferase deficiency.","citation":"Hum Mutat 2018 Jan;39(1):69-79","abstract":"Primary coenzyme Q10 (CoQ 10  ; MIM# 607426) deficiencies are an emerging group of inherited mitochondrial disorders with heterogonous clinical phenotypes. Over a dozen genes are involved in the biosynthesis of CoQ 10  , and mutations in several of these are associated with human disease. However, mutations in COQ5 (MIM# 616359), catalyzing the only C-methylation in the CoQ 10  synthetic pathway, have not been implicated in human disease. Here, we report three female siblings of Iraqi-Jewish descent, who had varying degrees of cerebellar ataxia, encephalopathy, generalized tonic-clonic seizures, and cognitive disability. Whole-exome and subsequent whole-genome sequencing identified biallelic duplications in the COQ5 gene, leading to reduced levels of CoQ 10  in peripheral white blood cells of all affected individuals and reduced CoQ 10  levels in the only muscle tissue available from one affected proband. CoQ 10  supplementation led to clinical improvement and increased the concentrations of CoQ 10  in blood. This is the first report of primary CoQ 10  deficiency caused by loss of function of COQ5, with delineation of the clinical, laboratory, histological, and molecular features, and insights regarding targeted treatment with CoQ 10  supplementation.","doi":"10.1002/humu.23345","authors":"Malicdan MCV, Vilboux T, Ben-Zeev B, Guo J, Eliyahu A, Pode-Shakked B, Dori A, Kakani S, Chandrasekharappa SC, Ferreira CR, Shelestovich N, Marek-Yagel D, Pri-Chen H, Blatt I, Niederhuber JE, He L, Toro C, Taylor RW, Deeken J, Yardeni T, Wallace DC, Gahl WA, Anikster Y","authors_abbrev":"Malicdan MCV et al.","pubmed_publication_date":"Jan 2018","pubmed_entrez_date":"2017-10-19","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16A11.07","SPCC4G3.04c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:31932483","title":"A Redox-Sensitive Thiol in Wis1 Modulates the Fission Yeast Mitogen-Activated Protein Kinase Response to H 2 O 2  and Is the Target of a Small Molecule.","citation":"Mol Cell Biol 2020 Mar 16;40(7)","abstract":"Oxidation of a highly conserved cysteine (Cys) residue located in the kinase activation loop of mitogen-activated protein kinase kinases (MAPKK) inactivates mammalian MKK6. This residue is conserved in the fission yeast  Schizosaccharomyces pombe  MAPKK Wis1, which belongs to the H 2 O 2 -responsive MAPK Sty1 pathway. Here, we show that H 2 O 2  reversibly inactivates Wis1 through this residue (C458)  in vitro  We found that C458 is oxidized  in vivo  and that serine replacement of this residue significantly enhances Wis1 activation upon addition of H 2 O 2  The allosteric MAPKK inhibitor INR119, which binds in a pocket next to the activation loop and C458, prevented the inhibition of Wis1 by H 2 O 2  in vitro  and significantly increased Wis1 activation by low levels of H 2 O 2  in vivo  We propose that oxidation of C458 inhibits Wis1 and that INR119 cancels out this inhibitory effect by binding close to this residue. Kinase inhibition through the oxidation of a conserved Cys residue in MKK6 (C196) is thus conserved in the  S. pombe  MAPKK Wis1.","doi":"10.1128/MCB.00346-19","authors":"Sjölander JJ, Tarczykowska A, Picazo C, Cossio I, Redwan IN, Gao C, Solano C, Toledano MB, Grøtli M, Molin M, Sunnerhagen P","authors_abbrev":"Sjölander JJ et al.","pubmed_publication_date":"16 Mar 2020","pubmed_entrez_date":"2020-01-15","publication_year":"2020","canto_session_key":"4bd2526203a7cc33","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Per Sunnerhagen","canto_first_approved_date":"2020-10-09 13:15:28","canto_approved_date":"2020-10-13 12:51:37","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-10-07 13:57:04","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Per Sunnerhagen","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9G1.02","SPBC409.07c","SPBC106.02c","SPAC24B11.06c","SPAC1006.09"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2020-10-09"},{"uniquename":"PMID:11212351","title":"Myosin-V: head to tail.","citation":"Cell Mol Life Sci 1999 Oct 15;56(3-4):233-42","abstract":"The myosin-V family is the most extensively studied of the unconventional myosin families. Most organisms examined have at least one member of the myosin-V family: many have multiple members. The wide range of species in which myosin-V has been identified suggests that myosin-V is a fundamental component of organelle transport in all higher eukaryotes. Possible cargoes for myosin-V range from melanosomes and synaptic vesicles in mammals to vacuoles and messenger RNA in yeast. In this review, we discuss the current state of research on the cellular function of myosin-V as described by the actions of the head, neck and tail domains.","authors":"Provance DW, Mercer JA","authors_abbrev":"Provance DW et al.","pubmed_publication_date":"15 Oct 1999","pubmed_entrez_date":"2001-02-24","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22456336","title":"Chemical genetic induction of meiosis in Schizosaccharomyces pombe.","citation":"Cell Cycle 2012 Apr 15;11(8):1621-5","abstract":"In the fission yeast Schizosaccharomyces pombe, meiosis is inhibited by the protein kinase Pat1, which phosphorylates and inactivates Mei2, an RNA binding protein essential for the initiation of meiosis. When diploid cells are deprived of nutrients, they initiate a cascade of events leading to the inactivation of Pat1 and entry into meiosis. Strains carrying the temperature-sensitive pat1-114 allele are forced to enter into meiosis when shifted to the non-permissive temperature, independently of the ploidity of the cell. This system has been extensively used, since it is possible to achieve a highly synchronous meiosis, which is a must for any molecular or microscopic approach that aims to decipher the mechanisms governing meiosis. Here, we have designed a new system to obtain a similarly synchronous meiosis, but independently of temperature shifts. Thus, by introducing a mutation in the ATP pocket of Pat1, we have generated a protein kinase that, in the presence of small specific inhibitors, can be inactivated. This results in forced entry into meiosis without the need of a temperature shift, minimizing the introduction of heat shock or any other stress responses along the meiotic waves of transcription.","doi":"10.4161/cc.20051","authors":"Guerra-Moreno A, Alves-Rodrigues I, Hidalgo E, Ayté J","authors_abbrev":"Guerra-Moreno A et al.","pubmed_publication_date":"15 Apr 2012","pubmed_entrez_date":"2012-03-30","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1487050","title":"Action of diphtheria toxin on Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1992 Nov;20(4):728-30","abstract":"","authors":"Davey J","authors_abbrev":"Davey J","pubmed_publication_date":"Nov 1992","pubmed_entrez_date":"1992-11-01","publication_year":"1992","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39330407","title":"The Myosin-V Myo51 and Alpha-Actinin Ain1p Cooperate during Contractile Ring Assembly and Disassembly in Fission Yeast Cytokinesis.","citation":"J Fungi (Basel) 2024 Sep 12;10(9)","abstract":"Cytokinesis is driven in part by the constriction of a ring of actin filaments, myosin motors and other proteins. In fission yeast, three myosins contribute to cytokinesis including a Myosin-V Myo51. As Myosin-Vs typically carry cargo along actin filaments, the role of Myo51 in cytokinesis remains unclear. The previous work suggests that Myo51 may crosslink actin filaments. We hypothesized that if Myo51 crosslinks actin filaments, cells carrying double deletions of  ain1 , which encodes the crosslinker alpha-actinin, and  myo51  ( ∆ain1 ∆myo51  cells) will exhibit more severe cytokinesis phenotypes than cells with the single  ∆ain1  mutation. Contrary to our expectations, we found that the loss of Myo51 in  ∆ain1  cells partially rescued the severity of the node clumping phenotype measured in  ∆ain1  cells. Furthermore, we describe a normal process of contractile ring \"shedding\", the appearance of fragments of ring material extending away from the contractile ring along the ingressing septum that occurs in the second half of constriction. We measured that  ∆ain1 ∆myo51  cells exhibit premature and exaggerated shedding. Our work suggests that Myo51 is not a simple actin filament crosslinker. Instead, a role in effective node motion better recapitulates its function during ring assembly and disassembly.","doi":"10.3390/jof10090647","authors":"Tyree ZL, Bellingham-Johnstun K, Martinez-Baird J, Laplante C","authors_abbrev":"Tyree ZL et al.","pubmed_publication_date":"12 Sep 2024","pubmed_entrez_date":"2024-09-27","publication_year":"2024","canto_session_key":"a75022bdef0034ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Zoe Tyree","canto_first_approved_date":"2025-02-24 14:03:25","canto_approved_date":"2025-03-20 10:22:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-02-21 16:17:13","canto_added_date":"2024-09-27 23:25:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Zoe Tyree","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.08","SPBC2D10.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2025-02-24"},{"uniquename":"PMID:3981130","title":"A correlation between mode of growth and regional ultrastructure of the plasma membrane of Schizosaccharomyces pombe as revealed by freeze-fracturing before and after filipin treatment.","citation":"J Gen Microbiol 1985 Feb;131(2):309-16","abstract":"The ultrastructure of the plasma membrane of Schizosaccharomyces pombe was studied by freeze-fracture using invaginations of the plasma membrane as natural markers and filipin-induced deformations as artificial markers. In accord with the mode of growth of this organism, ultrastructural aspects of the plasma membrane were related to the following ring zones: the growing pole, adjacent regions, proximal regions, the new cell pole, and the middle in dividing cells. The growing pole and adjacent regions had no or only a few invaginations. Filipin induced numerous deformations in these regions. By contrast, the proximal regions of the plasma membrane had several invaginations and resisted filipin-induced deformation. Concomitantly with commitment to cytokinesis, both the invaginations and the resistance to filipin-induced deformation disappeared in the middle. The results presented here strongly suggest the existence of two states of the plasma membrane of S. pombe, a fact which correlates well with the mode of growth of this organism.","authors":"Takeo K","authors_abbrev":"Takeo K","pubmed_publication_date":"Feb 1985","pubmed_entrez_date":"1985-02-01","publication_year":"1985","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008214","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28825727","title":"Condensin-mediated remodeling of the mitotic chromatin landscape in fission yeast.","citation":"Nat Genet 2017 Oct;49(10):1553-1557","abstract":"The eukaryotic genome consists of DNA molecules far longer than the cells that contain them. They reach their greatest compaction during chromosome condensation in mitosis. This process is aided by condensin, a structural maintenance of chromosomes (SMC) family member. The spatial organization of mitotic chromosomes and how condensin shapes chromatin architecture are not yet fully understood. Here we use chromosome conformation capture (Hi-C) to study mitotic chromosome condensation in the fission yeast Schizosaccharomyces pombe. This showed that the interphase landscape characterized by small chromatin domains is replaced by fewer but larger domains in mitosis. Condensin achieves this by setting up longer-range, intrachromosomal DNA interactions, which compact and individualize chromosomes. At the same time, local chromatin contacts are constrained by condensin, with profound implications for local chromatin function during mitosis. Our results highlight condensin as a major determinant that changes the chromatin landscape as cells prepare their genomes for cell division.","doi":"10.1038/ng.3938","authors":"Kakui Y, Rabinowitz A, Barry DJ, Uhlmann F","authors_abbrev":"Kakui Y et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-08-22","publication_year":"2017","canto_session_key":"f0afc6fe7b0b439a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Frank Uhlmann","canto_first_approved_date":"2017-10-19 15:38:58","canto_approved_date":"2024-04-01 14:17:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-09 11:59:57","canto_added_date":"2017-08-23 00:15:15","annotation_curators":[{"name":"Frank Uhlmann","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.03","SPBP4H10.06c","SPCC320.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-10-19"},{"uniquename":"PMID:39965018","title":"Functional constraints of wtf killer meiotic drivers.","citation":"PLoS Genet 2025 Feb 18;21(2):e1011534","abstract":"Killer meiotic drivers are selfish DNA loci that sabotage the gametes that do not inherit them from a driver+/driver- heterozygote. These drivers often employ toxic proteins that target essential cellular functions to cause the destruction of driver- gametes. Identifying the mechanisms of drivers can expand our understanding of infertility and reveal novel insights about the cellular functions targeted by drivers. In this work, we explore the molecular mechanisms underlying the wtf family of killer meiotic drivers found in fission yeasts. Each wtf killer acts using a toxic Wtfpoison protein that can be neutralized by a corresponding Wtfantidote protein. The wtf genes are rapidly evolving and extremely diverse. Here we found that self-assembly of Wtfpoison proteins is broadly conserved and associated with toxicity across the gene family, despite minimal amino acid conservation. In addition, we found the toxicity of Wtfpoison assemblies can be modulated by protein tags designed to increase or decrease the extent of the Wtfpoison assembly, implicating assembly size in toxicity. We also identified a conserved, critical role for the specific co-assembly of the Wtfpoison and Wtfantidote proteins in promoting effective neutralization of Wtfpoison toxicity. Finally, we engineered wtf alleles that encode toxic Wtfpoison proteins that are not effectively neutralized by their corresponding Wtfantidote proteins. The possibility of such self-destructive alleles reveals functional constraints on wtf evolution and suggests similar alleles could be cryptic contributors to infertility in fission yeast populations. As rapidly evolving killer meiotic drivers are widespread in eukaryotes, analogous self-killing drive alleles could contribute to sporadic infertility in many lineages.","doi":"10.1371/journal.pgen.1011534","authors":"Nidamangala Srinivasa A, Campbell S, Venkatesan S, Nuckolls NL, Lange JJ, Halfmann R, Zanders SE","authors_abbrev":"Nidamangala Srinivasa A et al.","pubmed_publication_date":"18 Feb 2025","pubmed_entrez_date":"2025-02-18","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-02-19 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12186947","title":"A novel chk1-dependent G1/M checkpoint in fission yeast.","citation":"J Cell Sci 2002 Sep 15;115(Pt 18):3609-18","abstract":"Fission yeast cells with a temperature-sensitive Orp1 protein, a component of the origin recognition complex, cannot perform DNA replication at the restrictive temperature. Seventy percent of orp1-4 cells arrest with a 1C DNA content, whereas 30% proceed to mitosis ('cut'). The arrest depends upon the checkpoint Rad proteins and, surprisingly, the Chk1 protein, which is thought to act only from late S phase. The arrested cells maintain a 1C DNA content, as judged by flow cytometry, and the early origin ars3001 has not been initiated, as judged by 2D gel analysis. We show that in G1-arrested orp1-4 cells, Wee1 phosphorylates and inactivates Cdc2. Activation of Chk1 occurs earlier than Cdc2 phosphorylation, indicating a novel role for Chk1, namely to induce and/or maintain Cdc2 phosphorylation upon checkpoint activation in G1. We also show that commitment to cutting occurs already in early G1 phase.","authors":"Synnes M, Nilssen EA, Boye E, Grallert B","authors_abbrev":"Synnes M et al.","pubmed_publication_date":"15 Sep 2002","pubmed_entrez_date":"2002-08-21","publication_year":"2002","canto_session_key":"e0f7d8e22ba14953","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-31 16:44:44","canto_approved_date":"2023-01-12 18:11:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-06 13:34:42","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPBC29A10.15","SPAC9E9.08","SPBC11B10.09","SPBC14C8.07c","SPCC18B5.03","SPBC336.12c","SPBC660.14","SPCC1259.13","SPBC216.05","SPAC14C4.13","SPCC18B5.11c"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2017-01-31"},{"uniquename":"PMID:23956636","title":"Possible Roles of LAMMER Kinase Lkh1 in Fission Yeast by Comparative Proteome Analysis.","citation":"Mycobiology 2010 Jun;38(2):108-12","abstract":"To investigate the possible roles of LAMMER kinase homologue, Lkh1, in Schizosaccharomyces pombe, whole proteins were extracted from wild type and lkh1-deletion mutant cells and subjected to polyacrylamide gel electrophoresis. Differentially expressed proteins were identified by tandem mass spectrometry (MS/MS) and were compared with a protein database. In whole-cell extracts, 10 proteins were up-regulated and 9 proteins were down-regulated in the mutant. In extracellular preparations, 6 proteins were up-regulated in the lkh1 (+) null mutant and 4 proteins successfully identified: glycolipid anchored surface precursor, β-glucosidase (Psu1), cell surface protein, glucan 1,3-β-glucosidase (Bgl2), and exo-1,3 β-glucanase (Exg1). These results suggest that Lkh1 is involved in regulating cell wall assembly.","doi":"10.4489/MYCO.2010.38.2.108","authors":"Cho SJ, Kim YH, Park HM, Shin KS","authors_abbrev":"Cho SJ et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2013-08-20","publication_year":"2010","canto_session_key":"86a759e366cff322","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-09-23 14:15:56","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-09-19 13:24:43","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14F5.04c","SPAC26F1.06","SPBC21C3.08c","SPAC664.11","SPAC23H3.15c","SPAC1002.13c","SPAC9E9.09c","SPAC3C7.14c","SPAC4H3.10c","SPAC926.04c","SPBC19C2.07","SPCC1739.13","SPBC1815.01","SPAC26H5.08c","SPBPB21E7.01c","SPBC215.11c","SPCC576.03c","SPCC794.12c","SPBC29A10.08","SPAC1D4.11c","SPBC1105.05","SPBC1773.06c"],"gene_count":22,"ltp_gene_count":1,"approved_date":"2013-09-19"},{"uniquename":"PMID:10684947","title":"A rapid genetic screening system for identifying gene-specific suppression constructs for use in human cells.","citation":"Nucleic Acids Res 2000 Mar 15;28(6):E15","abstract":"We describe a rapid cell-based genetic screen using fission yeast for identifying efficient gene suppression constructs (GSCs) from large libraries (10(5)) for any target sequence for use in human cells. In this system, target sequences are fused to the 5' end of the lacZ reporter gene and expressed in yeast. Random fragment expression libraries derived from the target sequence are screened in the fusion gene-expressing strain using the lacZ gene-encoded colony color phenotype. We demonstrate the utility of this screening assay by identifying a range of different GSCs for the fission yeast ura4 gene and human c-myc and Chk1 sequences, including rare efficient suppressors. GSCs specific for c-myc were shown to regulate expression of both a c-myc-lacZ fusion gene and the endogenous c-myc gene in human cells.","authors":"Arndt GM, Patrikakis M, Atkins D","authors_abbrev":"Arndt GM et al.","pubmed_publication_date":"15 Mar 2000","pubmed_entrez_date":"2000-02-24","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1290464","title":"Role of alkaline metal ions in the H(+)-ATPase activity of various yeast species.","citation":"Biochem Int 1992 Dec;28(6):1089-96","abstract":"Saccharomyces cerevisiae, Schizosaccharomyces pombe, Endomyces magnussi, Lodderomyces elongisporus and Rhodotorula gracilis, yeast species ranging from a glycolytic type to a strictly aerobic one, were tested for the activity of their plasma membrane H(+)-ATPase and the effect of alkaline metal cations thereon. The ATP-hydrolyzing activity of membranes from glucose-activated cells ranged from 456 to 932 mumol inorganic phosphate released per min per 1 g membrane protein. The effect of 0.2 M Li+, Na+, K+, Rb+ and Cs+ never exceeded the statistical range of error. In contrast, acidification after glucose addition ranged from 0.15 (for R. gracilis) to 14.8 nmol H+ per min per mg dry weight (for S. cerevisiae) and it was markedly influenced by the presence of alkaline metal chlorides, the highest effect observed being a seven-fold increase by K+ in a S. cerevisiae suspension. The effects were additive to those observed without ions in solution and are ascribed to the operation of independent channels and/or exchange systems for H+ with a clear selectivity toward K+. The separate nature of the ion-triggered extracellular acidification is supported by a different ratio of titration to pH-derived acidity with and without K+.","authors":"Kotyk A, Dvoraková M, Georghiou G","authors_abbrev":"Kotyk A et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19883398","title":"The Kinesin motor protein Cut7 regulates biogenesis and function of Ago1-complexes.","citation":"Traffic 2010 Jan;11(1):25-36","abstract":"Argonaute proteins are the effectors of small RNA-dependent gene-silencing pathways. In the cytoplasm, they are incorporated into large mobile ribonucleoprotein (RNP) complexes that travel along microtubules. We used a genetic screen to identify the microtubule-associated motor that interacts with Ago1-containing RNPs. Here, we report that activity of the kinesin family member Cut7 is important for biogenesis and/or stability of Ago1-containing RNPs in the cytoplasm. Results from pulldown and coimmunoprecipitation assays indicate that Cut7 interacts with Ago1 as well as its two cognate binding proteins, Dcr1 and Rdp1. Loss of Cut7 activity was associated with increased levels of reverse centromeric transcripts, presumably because of a defect in post-transcriptional gene silencing. Overexpression of the Ago1-binding region of Cut7 resulted in loss of microscopic Ago1-containing RNPs. Together, these results suggest that microtubule motor proteins function in the biogenesis and function of gene-silencing machinery in the cytoplasm.","doi":"10.1111/j.1600-0854.2009.01000.x","authors":"Stoica C, Park J, Pare JM, Willows S, Hobman TC","authors_abbrev":"Stoica C et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-11-04","publication_year":"2010","canto_session_key":"92ca5253836f252e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-01-02 03:38:03","canto_approved_date":"2021-01-02 03:38:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-02 03:37:29","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25G10.07c","SPAC6F12.09","SPCC188.13c","SPCC736.11"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2021-01-02"},{"uniquename":"PMID:33064910","title":"Sulfur depletion induces autophagy through Ecl1 family genes in fission yeast.","citation":"Genes Cells 2020 Dec;25(12):825-830","abstract":"Autophagy is an intracellular degradation system widely conserved among various species. Autophagy is induced by the depletion of various nutrients, and this degradation mechanism is essential for adaptation to such conditions. In this study, we demonstrated that sulfur depletion induces autophagy in the fission yeast Schizosaccharomyces pombe. Based on the finding that autophagy induced by sulfur depletion was completely abolished in a mutant in which the ecl1, ecl2 and ecl3 genes were deleted (Δecls), we report that these three genes are essential for the induction of autophagy by sulfur depletion. Furthermore, autophagy-defective mutant cells exhibited poor growth and short lifespan (compared with wild-type cells) under the sulfur-depleted condition. These results indicated that the mechanism of autophagy is necessary for the appropriate adaptation to sulfur depletion.","doi":"10.1111/gtc.12815","authors":"Shimasaki T, Okamoto K, Ohtsuka H, Aiba H","authors_abbrev":"Shimasaki T et al.","pubmed_publication_date":"Dec 2020","pubmed_entrez_date":"2020-10-16","publication_year":"2020","canto_session_key":"52125a607a59b282","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2020-11-08 14:45:35","canto_approved_date":"2021-06-11 15:47:22","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-10-28 02:03:00","canto_added_date":"2020-10-20 00:15:06","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":9,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.16c","SPCC63.08c","SPAC19B12.08","SPBC8E4.12c","SPCC70.12c","SPCC16A11.08","SPBC3B9.06c","SPAC4F10.07c","SPBP8B7.24c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2020-11-08"},{"uniquename":"PMID:30341288","title":"Common mechanism of transcription termination at coding and noncoding RNA genes in fission yeast.","citation":"Nat Commun 2018 Oct 19;9(1):4364","abstract":"Termination of RNA polymerase II (RNAPII) transcription is a fundamental step of gene expression that is critical for determining the borders between genes. In budding yeast, termination at protein-coding genes is initiated by the cleavage/polyadenylation machinery, whereas termination of most noncoding RNA (ncRNA) genes occurs via the Nrd1-Nab3-Sen1 (NNS) pathway. Here, we find that NNS-like transcription termination is not conserved in fission yeast. Rather, genome-wide analyses show global recruitment of mRNA 3' end processing factors at the end of ncRNA genes, including snoRNAs and snRNAs, and that this recruitment coincides with high levels of Ser2 and Tyr1 phosphorylation on the RNAPII C-terminal domain. We also find that termination of mRNA and ncRNA transcription requires the conserved Ysh1/CPSF-73 and Dhp1/XRN2 nucleases, supporting widespread cleavage-dependent transcription termination in fission yeast. Our findings thus reveal that a common mode of transcription termination can produce functionally and structurally distinct types of polyadenylated and non-polyadenylated RNAs.","doi":"10.1038/s41467-018-06546-x","authors":"Larochelle M, Robert MA, Hébert JN, Liu X, Matteau D, Rodrigue S, Tian B, Jacques PÉ, Bachand F","authors_abbrev":"Larochelle M et al.","pubmed_publication_date":"19 Oct 2018","pubmed_entrez_date":"2018-10-21","publication_year":"2018","canto_session_key":"b9a971923a3e9e07","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-10-22 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38679759","title":"Heterochromatin repeat organization at an individual level: Rex1BD and the 14-3-3 protein coordinate to shape the epigenetic landscape within heterochromatin repeats.","citation":"Bioessays 2024 Apr 28;:e2400030","abstract":"In eukaryotic cells, heterochromatin is typically composed of tandem DNA repeats and plays crucial roles in gene expression and genome stability. It has been reported that silencing at individual units within tandem heterochromatin repeats exhibits a position-dependent variation. However, how the heterochromatin is organized at an individual repeat level remains poorly understood. Using a novel genetic approach, our recent study identified a conserved protein Rex1BD required for position-dependent silencing within heterochromatin repeats. We further revealed that Rex1BD interacts with the 14-3-3 protein to regulate heterochromatin silencing by linking RNAi and HDAC pathways. In this review, we discuss how Rex1BD and the 14-3-3 protein coordinate to modulate heterochromatin organization at the individual repeat level, and comment on the biological significance of the position-dependent effect in heterochromatin repeats. We also identify the knowledge gaps that still need to be unveiled in the field.","doi":"10.1002/bies.202400030","authors":"Gao J, Li F","authors_abbrev":"Gao J et al.","pubmed_publication_date":"28 Apr 2024","pubmed_entrez_date":"2024-04-28","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-04-29 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013496","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15175657","title":"PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits.","citation":"EMBO J 2004 Jul 07;23(13):2641-50","abstract":"The mammalian protein arginine methyltransferase 3 (PRMT3) catalyzes the formation of asymmetric (type I) dimethylarginine in vitro. As yet, natural substrates and cellular pathways modulated by PRMT3 remain unknown. Here, we have identified an ortholog of PRMT3 in fission yeast. Tandem affinity purification of fission yeast PRMT3 coupled with mass spectrometric protein identification revealed that PRMT3 associates with components of the translational machinery. We identified the 40S ribosomal protein S2 as the first physiological substrate of PRMT3. In addition, a fraction of yeast and human PRMT3 cosedimented with free 40S ribosomal subunits, as determined by sucrose gradient velocity centrifugation. The activity of PRMT3 is not essential since prmt3-disrupted cells are viable. Interestingly, cells lacking PRMT3 showed an accumulation of free 60S ribosomal subunits resulting in an imbalance in the 40S:60S free subunits ratio; yet pre-rRNA processing appeared to occur normally. Our results identify PRMT3 as the first type I ribosomal protein arginine methyltransferase and suggest that it regulates ribosome biosynthesis at a stage beyond pre-rRNA processing.","authors":"Bachand F, Silver PA","authors_abbrev":"Bachand F et al.","pubmed_publication_date":"07 Jul 2004","pubmed_entrez_date":"2004-06-04","publication_year":"2004","canto_session_key":"ebbf99a628743442","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-22 09:51:24","canto_approved_date":"2025-09-03 14:54:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-22 09:51:16","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC839.15c","SPAC890.07c","SPCC576.08c","SPAC17G6.06","SPBC8D2.10c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-06-22"},{"uniquename":"PMID:9652094","title":"Mathematical model of the fission yeast cell cycle with checkpoint controls at the G1/S, G2/M and metaphase/anaphase transitions.","citation":"Biophys Chem 1998 May 05;72(1-2):185-200","abstract":"All events of the fission yeast cell cycle can be orchestrated by fluctuations of a single cyclin-dependent protein kinase, the Cdc13/Cdc2 heterodimer. The G1/S transition is controlled by interactions of Cdc13/Cdc2 and its stoichiometric inhibitor, Rum1. The G2/M transition is regulated by a kinase-phosphatase pair, Wee1 and Cdc25, which determine the phosphorylation state of the Tyr-15 residue of Cdc2. The meta/anaphase transition is controlled by interactions between Cdc13/Cdc2 and the anaphase promoting complex, which labels Cdc13 subunits for proteolysis. We construct a mathematical model of fission yeast growth and division that encompasses all three crucial checkpoint controls. By numerical simulations we show that the model is consistent with a broad selection of cell cycle mutants, and we predict the phenotypes of several multiple-mutant strains that have not yet been constructed.","authors":"Novak B, Csikasz-Nagy A, Gyorffy B, Chen K, Tyson JJ","authors_abbrev":"Novak B et al.","pubmed_publication_date":"05 May 1998","pubmed_entrez_date":"1998-07-04","publication_year":"1998","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012621","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.107"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16453723","title":"Involvement of ras in sexual differentiation but not in growth control in fission yeast.","citation":"EMBO J 1986 Nov;5(11):2963-71","abstract":"The function of the ras gene of Schizosaccharomyces pombe has been studied by constructing null and activated alleles of this gene. An activated allele (Val (12)) inhibits conjugation but has no effect on cell growth, entry into stationary phase or sporulation. The phenotype of Val (12) is distinct from that caused by elevating the intracellular level of cAMP. This supports the hypothesis that ras of fission yeast does not modulate adenylate cyclase in a manner analogous to S. cerevisiae RAS. Introduction of a human ras sequence into fission yeast cells containing a non-functional null allele of ras restored the sexual differentiation process thus indicating that the human sequence can complement S. pombe ras. Our data suggest that although ras genes are highly conserved across a considerable evolutionary divide, the cellular function of the ras gene product varies in different organisms.","authors":"Nadin-Davis SA, Nasim A, Beach D","authors_abbrev":"Nadin-Davis SA et al.","pubmed_publication_date":"Nov 1986","pubmed_entrez_date":"1986-11-01","publication_year":"1986","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11402029","title":"Bipartite binding of a kinase activator activates Cdc7-related kinase essential for S phase.","citation":"J Biol Chem 2001 Aug 17;276(33):31376-87","abstract":"Dfp1/Him1 protein of fission yeast, Schizosaccharomyces pombe, encodes the regulatory subunit for Hsk1 kinase, a homologue of budding yeast Cdc7 kinase essential for initiation and progression of the S phase of the cell cycle. This protein binds and activates Hsk1 kinase, which phosphorylates the MCM2 protein. Comparison of the amino acid sequences of the Cdc7 regulatory subunits from various eukaryotes revealed the presence of three small stretches of conserved amino acid sequences, namely Dbf4 motifs N, M, and C. We report here that the Dbf4 motif M, a unique proline-rich motif, and the Dbf4 motif C, a C(2)H(2)-type zinc finger motif, are essential for mitotic functions of Dfp1/Him1 protein as well as for full-level activation of Hsk1 kinase. In vitro, a small segment containing the Dbf4 motif M or C alone binds to and partially activates Hsk1. Co-expression of these two segments augments the extent of activation. Furthermore, a fused polypeptide containing only Dbf4 motifs M and C without any spacer can activate Hsk1 and is capable of rescuing the growth defect of him1 null cells. Insertion of a long stretch of amino acids between the motif M and motif C can be tolerated for mitotic functions. On the other hand, internal deletion of Dbf4 motif N, which has some similarity with the BRCA C-terminal domain motif, results in a defect in hydroxyurea-induced checkpoint responses and sensitivity to methyl methane sulfonate, yet mitotic functions and kinase activation are intact. In one-hybrid assays with budding yeast Dbf4, motif N mutants exhibit reduced interaction with a replication origin. Our observations suggest the molecular architecture of Cdc7.Dbf4-related kinase complexes at the origins, in which they are tethered to replication machinery through Dbf4 motif N and the catalytic subunits are activated through bipartite binding of Dbf4 motifs M and C of the regulatory subunits.","authors":"Ogino K, Takeda T, Matsui E, Iiyama H, Taniyama C, Arai K, Masai H","authors_abbrev":"Ogino K et al.","pubmed_publication_date":"17 Aug 2001","pubmed_entrez_date":"2001-06-13","publication_year":"2001","canto_session_key":"7f0cc1dde6a7ce20","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-10-09 13:43:02","canto_approved_date":"2022-02-24 10:56:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-09 13:42:56","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":123,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC550.13","SPBC4.04c","SPBC776.12c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-10-09"},{"uniquename":"EMBL:SPC02659","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14573465","title":"Fission yeast Tup1-like repressors repress chromatin remodeling at the fbp1+ promoter and the ade6-M26 recombination hotspot.","citation":"Genetics 2003 Oct;165(2):505-15","abstract":"Chromatin remodeling plays crucial roles in the regulation of gene expression and recombination. Transcription of the fission yeast fbp1(+) gene and recombination at the meiotic recombination hotspot ade6-M26 (M26) are both regulated by cAMP responsive element (CRE)-like sequences and the CREB/ATF-type transcription factor Atf1*Pcr1. The Tup11 and Tup12 proteins, the fission yeast counterparts of the Saccharomyces cerevisiae Tup1 corepressor, are involved in glucose repression of the fbp1(+) transcription. We have analyzed roles of the Tup1-like corepressors in chromatin regulation around the fbp1(+) promoter and the M26 hotspot. We found that the chromatin structure around two regulatory elements for fbp1(+) was remodeled under derepressed conditions in concert with the robust activation of fbp1(+) transcription. Strains with tup11delta tup12delta double deletions grown in repressed conditions exhibited the chromatin state associated with wild-type cells grown in derepressed conditions. Interestingly, deletion of rst2(+), encoding a transcription factor controlled by the cAMP-dependent kinase, alleviated the tup11delta tup12delta defects in chromatin regulation but not in transcription repression. The chromatin at the M26 site in mitotic cultures of a tup11delta tup12delta mutant resembled that of wild-type meiotic cells. These observations suggest that these fission yeast Tup1-like corepressors repress chromatin remodeling at CRE-related sequences and that Rst2 antagonizes this function.","authors":"Hirota K, Hoffman CS, Shibata T, Ohta K","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2003-10-24","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7809944","title":"A model for specification of the left-right axis in vertebrates.","citation":"Trends Genet 1994 Nov;10(11):392-6","abstract":"The mechanisms that underlie the formation of the left-right embryonic axis in vertebrates are not known. The programmed pattern of cell-type change in fission yeast results from the inheritance of specific chromatids of the parental chromosome. Here, I address how such a model may explain left-right specification of the viscera in mice. The model proposes that DNA replication produces different chromatids, and that these specific chromatids of both homologs are nonrandomly segregated to daughter cells to specify the left-right axis of the embryo. Such a model presents a simple explanation of the interesting phenotype of the newly discovered insertional mutation inv in mice, which causes reversal of the left-right axis, proposing that it is caused by a chromosomal inversion.","authors":"Klar AJ","authors_abbrev":"Klar AJ","pubmed_publication_date":"Nov 1994","pubmed_entrez_date":"1994-11-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009920","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011500","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24314397","title":"Inhibition of serine and proline racemases by substrate-product analogues.","citation":"Bioorg Med Chem Lett 2014 Jan 01;24(1):390-3","abstract":"d-Amino acids can play important roles as specific biosynthetic building blocks required by organisms or act as regulatory molecules. Consequently, amino acid racemases that catalyze the formation of d-amino acids are potential therapeutic targets. Serine racemase catalyzes the reversible formation of d-serine (a modulator of neurotransmission) from l-serine, while proline racemase (an essential enzymatic and mitogenic protein in trypanosomes) catalyzes the reversible conversion of l-proline to d-proline. We show the substrate-product analogue α-(hydroxymethyl)serine is a modest, linear mixed-type inhibitor of serine racemase from Schizosaccharomyces pombe (Ki=167±21mM, Ki'=661±81mM, cf. Km=19±2mM). The bicyclic substrate-product analogue of proline, 7-azabicyclo[2.2.1]heptan-7-ium-1-carboxylate is a weak inhibitor of proline racemase from Clostridium sticklandii, giving only 29% inhibition at 142.5mM. However, the more flexible bicyclic substrate-product analogue tetrahydro-1H-pyrrolizine-7a(5H)-carboxylate is a noncompetitive inhibitor of proline racemase from C. sticklandii (Ki=111±15mM, cf. Km=5.7±0.5mM). These results suggest that substrate-product analogue inhibitors of racemases may only be effective when the active site is capacious and/or plastic, or when the inhibitor is sufficiently flexible.","doi":"10.1016/j.bmcl.2013.10.061","authors":"Harty M, Nagar M, Atkinson L, Legay CM, Derksen DJ, Bearne SL","authors_abbrev":"Harty M et al.","pubmed_publication_date":"01 Jan 2014","pubmed_entrez_date":"2013-12-10","publication_year":"2014","canto_session_key":"0f86c034b975c3a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-06-26 18:01:31","canto_approved_date":"2020-01-21 09:16:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-06 12:11:46","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-26"},{"uniquename":"PMID:18502752","title":"Int6/eIF3e promotes general translation and Atf1 abundance to modulate Sty1 MAPK-dependent stress response in fission yeast.","citation":"J Biol Chem 2008 Aug 08;283(32):22063-75","abstract":"int-6 is one of the frequent integration sites for mouse mammary tumor viruses. Although its product is the e-subunit of translation initiation factor eIF3, other evidence indicates that it interacts with proteasomes or other proteins to regulate protein stability. Here we report that the fission yeast int6(+) is required for overcoming stress imposed by histidine starvation, using the drug 3-aminotriazole (3AT). Microarray and complementary Northern studies using wild-type, int6Delta or gcn2Delta mutants indicate that 3AT-treated wild-type yeast induces core environmental stress response (CESR) genes in addition to typical general amino acid control (GAAC) genes whose transcription depends on the eIF2 kinase, Gcn2. In agreement with this, Sty1 MAPK and its target transcription factor Atf1, which signal the CESR, are required for overcoming 3AT-induced starvation. We find that Int6 is required for maintaining the basal level of Atf1 and for rapid transcriptional activation of the CESR on 3AT-insult. Pulse labeling experiments indicate that int6Delta significantly slows down de novo protein synthesis. Moreover, Atf1 protein half-life was reduced in int6Delta cells. These effects would account for the compromised Atf1 activity on 3AT-induced stress. Thus, the robust protein synthesis promoted by intact eIF3 appears to be a part of the requisites for sound Sty1 MAPK-dependent signaling governed by the activity of the Atf1 transcription factor.","doi":"10.1074/jbc.M710017200","authors":"Udagawa T, Nemoto N, Wilkinson CR, Narashimhan J, Jiang L, Watt S, Zook A, Jones N, Wek RC, Bähler J, Asano K","authors_abbrev":"Udagawa T et al.","pubmed_publication_date":"08 Aug 2008","pubmed_entrez_date":"2008-05-27","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC36B7.09","SPAC222.07c","SPAC20G4.03c","SPBC646.09c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:15546915","title":"Schizosaccharomyces pombe Rgf3p is a specific Rho1 GEF that regulates cell wall beta-glucan biosynthesis through the GTPase Rho1p.","citation":"J Cell Sci 2004 Dec 01;117(Pt 25):6163-74","abstract":"Rho1p regulates cell integrity by controlling the actin cytoskeleton and cell-wall synthesis. Here, we describe the cloning and characterization of rgf3+, a member of the Rho family of guanine nucleotide exchange factors (Rho GEFs). The rgf3+ gene was cloned by complementation of a mutant (ehs2-1) hypersensitive to drugs that interfere with cell-wall biosynthesis. The rgf3+ gene was found to be essential for cell viability and depletion of Rgf3p afforded phenotypes similar to those obtained following depletion of Rho1p. However, the cell death caused by Rgf3p depletion could be rescued by the presence of 1.2 M sorbitol, whereas depletion of Rho1 was lethal under the same conditions. We show that Rgf3p is a specific Rho1-GEF. The hypersensitivity to drugs affecting the cell wall of the ehs2-1 mutant was suppressed by overexpression of rho1+ but not by any of the other GTPases of the Rho family. Rgf3p interacted with the GDP-bound form of Rho1p and promoted the GDP-GTP exchange. In addition, we show that overexpression of Rgf3p produces multiseptated cells and increases beta-1,3-glucan synthase activity and the amount of cell wall beta-1,3-glucan. Rgf3p localized to the septum and the mRNA level was regulated in a cell-cycle-dependent manner peaking during septation. Our results suggest that Rgf3p acts as a positive activator of Rho1p, probably activating the Rho functions that coordinate cell-wall biosynthesis to maintain cell integrity during septation.","authors":"Tajadura V, García B, García I, García P, Sánchez Y","authors_abbrev":"Tajadura V et al.","pubmed_publication_date":"01 Dec 2004","pubmed_entrez_date":"2004-11-18","publication_year":"2004","canto_session_key":"8702be0070bbe887","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-04-25 10:57:18","canto_approved_date":"2025-09-02 20:33:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-30 17:55:30","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.03","SPCC645.06c","SPAC19B12.03","SPCC18B5.03","SPAC24B11.11c","SPAC1F7.04"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2022-04-25"},{"uniquename":"PMID:20547592","title":"Vgl1, a multi-KH domain protein, is a novel component of the fission yeast stress granules required for cell survival under thermal stress.","citation":"Nucleic Acids Res 2010 Oct;38(19):6555-66","abstract":"Multiple KH-domain proteins, collectively known as vigilins, are evolutionarily highly conserved proteins that are present in eukaryotic organisms from yeast to metazoa. Proposed roles for vigilins include chromosome segregation, messenger RNA (mRNA) metabolism, translation and tRNA transport. As a step toward understanding its biological function, we have identified the fission yeast vigilin, designated Vgl1, and have investigated its role in cellular response to environmental stress. Unlike its counterpart in Saccharomyces cerevisiae, we found no indication that Vgl1 is required for the maintenance of cell ploidy in Schizosaccharomyces pombe. Instead, Vgl1 is required for cell survival under thermal stress, and vgl1Δ mutants lose their viability more rapidly than wild-type cells when incubated at high temperature. As for Scp160 in S. cerevisiae, Vgl1 bound polysomes accumulated at endoplasmic reticulum (ER) but in a microtubule-independent manner. Under thermal stress, Vgl1 is rapidly relocalized from the ER to cytoplasmic foci that are distinct from P-bodies but contain stress granule markers such as poly(A)-binding protein and components of the translation initiation factor eIF3. Together, these observations demonstrated in S. pombe the presence of RNA granules with similar composition as mammalian stress granules and identified Vgl1 as a novel component that required for cell survival under thermal stress.","doi":"10.1093/nar/gkq555","authors":"Wen WL, Stevenson AL, Wang CY, Chen HJ, Kearsey SE, Norbury CJ, Watt S, Bähler J, Wang SW","authors_abbrev":"Wen WL et al.","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2010-06-16","publication_year":"2010","canto_session_key":"9178dbaf766a122a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-11-01 12:29:34","canto_approved_date":"2023-09-26 07:34:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-27 12:38:44","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.04c","SPAC3G9.09c","SPAC20G4.03c","SPBC36B7.09","SPBC3B9.21","SPAC19A8.12","SPBC1718.01","SPAC25G10.08","SPCC550.14"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2016-11-01"},{"uniquename":"PMID:9635188","title":"Rng2p, a protein required for cytokinesis in fission yeast, is a component of the actomyosin ring and the spindle pole body.","citation":"Curr Biol 1998 May 21;8(11):611-21","abstract":"An actomyosin-based contractile ring plays a pivotal role in cytokinesis. Despite the identification of many components of the ring, the steps involved in its assembly are unknown. The fission yeast Schizosaccharomyces pombe is an attractive organism in which to study cytokinesis because its cell cycle has been well characterized; it divides by medial fission using an actomyosin ring; and a number of S. pombe mutants defective in actomyosin ring assembly have been isolated. Here, we have characterized one such mutant, rng2.\nTemperature-sensitive rng2 mutants accumulated F-actin cables in the medial region of the cell but failed to organize the cables into a ring. In rng2-null mutants, only a spot-like structure containing F-actin was detected. The rng2+ gene encodes a protein related to human IQGAP1, a protein that binds actin and calmodulin and is a potential effector for the Rho family of GTPases. Rng2p localized to the actomyosin ring and to the spindle pole body (SPB) of interphase and mitotic cells. Localization of Rng2p to the actomyosin ring but not the SPB required F-actin. Rng2p interacted with calmodulin, a component of the SPB and the actomyosin ring. The rng2 gene showed genetic interactions with three other actomyosin ring assembly mutants, cdc4, cdc12, and rng5.\nThe S. pombe IQGAP-related protein Rng2p is a component of the actomyosin ring and the SPB and is required for actomyosin ring construction following assembly of F-actin at the division site.","authors":"Eng K, Naqvi NI, Wong KC, Balasubramanian MK","authors_abbrev":"Eng K et al.","pubmed_publication_date":"21 May 1998","pubmed_entrez_date":"1998-06-23","publication_year":"1998","canto_session_key":"f982d832f0775175","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-01-05 16:24:34","canto_approved_date":"2025-05-19 08:23:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-05 16:24:29","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAC3A12.14","SPAP8A3.08","SPAC27F1.02c","SPAC4F8.13c","SPAC1F5.04c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-01-05"},{"uniquename":"EMBL:X55772","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21364888","title":"Interactions between the Nse3 and Nse4 components of the SMC5-6 complex identify evolutionarily conserved interactions between MAGE and EID Families.","citation":"PLoS One 2011 Feb 25;6(2):e17270","abstract":"The SMC5-6 protein complex is involved in the cellular response to DNA damage. It is composed of 6-8 polypeptides, of which Nse1, Nse3 and Nse4 form a tight sub-complex. MAGEG1, the mammalian ortholog of Nse3, is the founding member of the MAGE (melanoma-associated antigen) protein family and Nse4 is related to the EID (E1A-like inhibitor of differentiation) family of transcriptional repressors.\nUsing site-directed mutagenesis, protein-protein interaction analyses and molecular modelling, we have identified a conserved hydrophobic surface on the C-terminal domain of Nse3 that interacts with Nse4 and identified residues in its N-terminal domain that are essential for interaction with Nse1. We show that these interactions are conserved in the human orthologs. Furthermore, interaction of MAGEG1, the mammalian ortholog of Nse3, with NSE4b, one of the mammalian orthologs of Nse4, results in transcriptional co-activation of the nuclear receptor, steroidogenic factor 1 (SF1). In an examination of the evolutionary conservation of the Nse3-Nse4 interactions, we find that several MAGE proteins can interact with at least one of the NSE4/EID proteins.\nWe have found that, despite the evolutionary diversification of the MAGE family, the characteristic hydrophobic surface shared by all MAGE proteins from yeast to humans mediates its binding to NSE4/EID proteins. Our work provides new insights into the interactions, evolution and functions of the enigmatic MAGE proteins.","doi":"10.1371/journal.pone.0017270","authors":"Hudson JJ, Bednarova K, Kozakova L, Liao C, Guerineau M, Colnaghi R, Vidot S, Marek J, Bathula SR, Lehmann AR, Palecek J","authors_abbrev":"Hudson JJ et al.","pubmed_publication_date":"25 Feb 2011","pubmed_entrez_date":"2011-03-03","publication_year":"2011","canto_session_key":"07e197372b9f88a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-01-09 16:51:38","canto_approved_date":"2023-08-08 16:28:53","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2015-01-09 16:51:32","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":200,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_21364888_phaf.tsv"}],"genes":["SPCC645.04","SPCC550.05","SPBC20F10.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-01-09"},{"uniquename":"PMID:35097140","title":"Fission yeast Ase1 PRC1  is required for the G 2 -microtubule damage response.","citation":"Mol Biol Res Commun 2021 Dec;10(4):179-188","abstract":" Schizosaccharomyces pombe  delays entry into mitosis following G 2  microtubule damage. This pathway is dependent on Rad26 ATRIP , the regulatory subunit of the Rad26 ATRIP /Rad3 ATR  DNA damage response (DDR) complex. However, this G 2  microtubule damage response pathway acts independently of the G 2  DNA damage checkpoint pathway. To identify other proteins in this G 2  microtubule damage pathway, we previously screened a cDNA overexpression library for genes that rescued the sensitivity of  rad26Δ  cells to the microtubule poison thiabendazole. A partial cDNA fragment encoding only the C-terminal regulatory region of the microtubule bundling protein  Ase1   PRC1  was isolated. This fragment lacks the Ase1 PRC1  dimerization and microtubule binding domains and retains the conserved C-terminal unstructured regulatory region. Here, we report that  ase1Δ  cells fail to delay entry into mitosis following G 2  microtubule damage. Microscopy revealed that Rad26 ATRIP  foci localized alongside Ase1 PRC1  filaments, although we suggest that this is related to microtubule-dependent double strand break mobility that facilitates homologous recombination events. Indeed, we report that the DNA repair protein Rad52 co-localizes with Rad26 ATRIP  at these foci, and that localization of Rad26 ATRIP  to these foci depends on a Rad26 ATRIP  N-terminal region containing a checkpoint recruitment domain. To our knowledge, this is the first report implicating Ase1 PRC1  in regulation of the G 2 /M transition.","doi":"10.22099/mbrc.2021.41001.1650","authors":"Doss RM, Xhunga S, Klimczak D, Cameron M, Verlare J, Wolkow TD","authors_abbrev":"Doss RM et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2022-01-31","publication_year":"2021","canto_session_key":"cf439bd5d8536df8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-02-02 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10871270","title":"A homolog of mammalian antizyme is present in fission yeast Schizosaccharomyces pombe but not detected in budding yeast Saccharomyces cerevisiae.","citation":"Bioinformatics 2000 May;16(5):478-81","abstract":"The antizymes (AZ) are proteins that regulate cellular polyamine pools in metazoa. To search for remote homologs in single-celled eukaryotes, we used computer software based on hidden Markov models. The most divergent homolog detected was that of the fission yeast Schizosaccharomyces pombe. Sequence identities between S.POMBE: AZ and known AZs are as low as 18-22% in the most conserved C-terminal regions. The authenticity of the S.POMBE: AZ is validated by the presence of a conserved nucleotide sequence that, in metazoa, promotes a +1 programmed ribosomal frameshift required for AZ expression. However, no homolog was detected in the completed genome of the budding yeast Saccharomyces cerevisiae. Procedural details and supplementary information can be found at http://itsa.ucsf.edu/ approximately czhu/AZ.","authors":"Zhu C, Karplus K, Grate L, Coffino P","authors_abbrev":"Zhu C et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-06-28","publication_year":"2000","canto_session_key":"a2ba7a9f9f7b0ea0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-02 14:39:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-02 14:39:17","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC577.14c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-09-02"},{"uniquename":"PMID:26486472","title":"West syndrome caused by homozygous variant in the evolutionary conserved gene encoding the mitochondrial elongation factor GUF1.","citation":"Eur J Hum Genet 2016 Jul;24(7):1001-8","abstract":"West syndrome (WS), defined by the triad of infantile spasms, pathognomonic hypsarrhythmia and developmental regression, is a rare epileptic disease affecting about 1:3500 live births. To get better insights on the genetic of this pathology, we exome-sequenced the members of a consanguineous family affected with isolated WS. We identified a homozygous variant (c.1825G>T/p.(Ala609Ser)) in the GUF1 gene in the three affected siblings. GUF1 encodes a protein essential in conditions that counteract faithful protein synthesis: it is able to remobilize stuck ribosomes and transiently inhibit the elongation process to optimize protein synthesis. The variant identified in the WS family changes an alanine residue conserved in all eukaryotic organisms and positioned within the tRNA-binding moiety of this nuclear genome-encoded mitochondrial translational elongation factor. Yeast complementation assays show that the activity of GUF1(A609S) is modified in suboptimal environments. We suggest a new link between improper assembly of respiratory chain complexes and WS.","doi":"10.1038/ejhg.2015.227","authors":"Alfaiz AA, Müller V, Boutry-Kryza N, Ville D, Guex N, de Bellescize J, Rivier C, Labalme A, des Portes V, Edery P, Till M, Xenarios I, Sanlaville D, Herrmann JM, Lesca G, Reymond A","authors_abbrev":"Alfaiz AA et al.","pubmed_publication_date":"Jul 2016","pubmed_entrez_date":"2015-10-22","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B3.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26568486","title":"Co-Expression Network Models Suggest that Stress Increases Tolerance to Mutations.","citation":"Sci Rep 2015 Nov 16;5:16726","abstract":"Network models are a well established tool for studying the robustness of complex systems, including modelling the effect of loss of function mutations in protein interaction networks. Past work has concentrated on average damage caused by random node removal, with little attention to the shape of the damage distribution. In this work, we use fission yeast co-expression networks before and after exposure to stress to model the effect of stress on mutational robustness. We find that exposure to stress decreases the average damage from node removal, suggesting stress induces greater tolerance to loss of function mutations. The shape of the damage distribution is also changed upon stress, with a greater incidence of extreme damage after exposure to stress. We demonstrate that the change in shape of the damage distribution can have considerable functional consequences, highlighting the need to consider the damage distribution in addition to average behaviour.","doi":"10.1038/srep16726","authors":"Lehtinen S, Bähler J, Orengo C","authors_abbrev":"Lehtinen S et al.","pubmed_publication_date":"16 Nov 2015","pubmed_entrez_date":"2015-11-17","publication_year":"2015","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2015-11-18 01:19:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9928931","title":"The S/M checkpoint at 37 degrees C and the recovery of viability of the mutant poldeltats3 require the crb2+/rhp9+ gene in fission yeast.","citation":"Mol Gen Genet 1999 Jan;260(6):522-34","abstract":"We have isolated a mutant in fission yeast, in which mitosis is uncoupled from completion of DNA replication when DNA synthesis is impaired by a thermosensitive mutation in the gene encoding the catalytic subunit of DNA polymerase delta. By functional complementation, we cloned the wild-type gene and identified it as the recently cloned checkpoint gene crb2+/rhp9+. This gene has been implicated in the DNA damage checkpoint and acts in the Chk1 pathway. Unlike the deleted strain dcrb2, cells bearing the crb2-1 allele were not affected in the DNA repair checkpoint after UV or MMS treatment at 30 degrees C, but were defective in this checkpoint function when treated with MMS at 37 degrees C. We analysed the involvement of Crb2 in the S/M checkpoint by blocking DNA replication with hydroxyurea, by using S phase cdc mutants, or by overexpression of the mutant PCNA L68S. Both crb2 mutants were unable to maintain the S/M checkpoint at 37 degrees C. Furthermore, the crb2+ gene was required, together with the cds1+ gene, for the S/M checkpoint at 30 degrees C. Finally, both the crb2 deletion and the crb2-1 allele induced a rapid death phenotype in the poldeltats3 background at both 30 degrees C and 37 degrees C. The rapid death phenotype was independent of the checkpoint functions.","authors":"Grenon M, Tillit J, Piard K, Baldacci G, Francesconi S","authors_abbrev":"Grenon M et al.","pubmed_publication_date":"Jan 1999","pubmed_entrez_date":"1999-02-03","publication_year":"1999","canto_session_key":"af19fd77ce6d95dd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-22 15:13:40","canto_approved_date":"2021-01-05 15:33:50","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-04-22 15:13:35","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":52,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPAC24H6.05","SPCC1259.13","SPAC3H5.06c","SPAC20G8.01","SPBC336.04","SPBC1734.02c","SPBC336.12c","SPBC342.05","SPAC8F11.07c","SPBC16D10.09","SPCC18B5.11c","SPBC14C8.07c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2015-04-22"},{"uniquename":"PMID:10607632","title":"Yeast as a tool for apoptosis research.","citation":"Curr Opin Microbiol 1999 Dec;2(6):618-23","abstract":"Apoptosis is a unique cell suicide process that plays important roles in a wide variety of developmental and normal physiological processes in animal species, and causes diseases when inappropriately controlled. Although yeast do not possess the proteases ultimately responsible for the morphological events recognized as apoptosis, these simple unicellular eukaryotes can serve as a powerful tool for apoptosis researchers. Ectopic expression of several human and animal apoptosis proteins in either budding or fission yeast results in phenotypes that create opportunities for genetic screens. Recent exploitation of yeast as tools for studying human apoptosis-regulatory proteins has yielded novel insights into cell death mechanisms, suggesting strategies for identification of genes and drugs that modulate the functions of proteins involved in apoptosis control.","authors":"Matsuyama S, Nouraini S, Reed JC","authors_abbrev":"Matsuyama S et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-12-23","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9191268","title":"Identification of the transporter for the M-factor mating pheromone in fission yeast.","citation":"Biochem Soc Trans 1997 May;25(2):224S","abstract":"","authors":"Davey J, Christensen PU, Nielsen O","authors_abbrev":"Davey J et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"2b3b7ef23078576","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-03-29 13:35:55","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-02-24 14:04:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25B2.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-02-24"},{"uniquename":"EMBL:AU010092","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39477922","title":"Clr4 SUV39H1  ubiquitination and non-coding RNA mediate transcriptional silencing of heterochromatin via Swi6 phase separation.","citation":"Nat Commun 2024 Oct 30;15(1):9384","abstract":"Transcriptional silencing by RNAi paradoxically relies on transcription, but how the transition from transcription to silencing is achieved has remained unclear. The Cryptic Loci Regulator complex (CLRC) in Schizosaccharomyces pombe is a cullin-ring E3 ligase required for silencing that is recruited by RNAi. We found that the E2 ubiquitin conjugating enzyme Ubc4 interacts with CLRC and mono-ubiquitinates the histone H3K9 methyltransferase Clr4 SUV39H1 , promoting the transition from co-transcriptional gene silencing (H3K9me2) to transcriptional gene silencing (H3K9me3). Ubiquitination of Clr4 occurs in an intrinsically disordered region (Clr4 IDR ), which undergoes liquid droplet formation in vitro, along with Swi6 HP1  the effector of transcriptional gene silencing. Our data suggests that phase separation is exquisitely sensitive to non-coding RNA (ncRNA) which promotes self-association of Clr4, chromatin association, and di-, but not tri- methylation instead. Ubc4-CLRC also targets the transcriptional co-activator Bdf2 BRD4 , down-regulating centromeric transcription and small RNA (sRNA) production. The deubiquitinase Ubp3 counteracts both activities.","doi":"10.1038/s41467-024-53417-9","authors":"Kim HS, Roche B, Bhattacharjee S, Todeschini L, Chang AY, Hammell C, Verdel A, Martienssen RA","authors_abbrev":"Kim HS et al.","pubmed_publication_date":"30 Oct 2024","pubmed_entrez_date":"2024-10-31","publication_year":"2024","canto_session_key":"16e80a5ff73f73c2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-11-01 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26933253","title":"Growth and the Environment of Schizosaccharomyces pombe.","citation":"Cold Spring Harb Protoc 2016 Mar 01;2016(3):pdb.top079764","abstract":"Here, we summarize the composition and uses of Schizosaccharomyces pombe media and discuss key issues for consideration in the generation of S. pombe cultures. We discuss the concept of \"culture memory,\" in which the growth state and stress experienced by a strain during storage, propagation, and starter culture preparation can alter experimental outcomes at later stages. We also describe the triggers that are widely used to manipulate signaling through the environment sensing pathways.","doi":"10.1101/pdb.top079764","authors":"Petersen J, Russell P","authors_abbrev":"Petersen J et al.","pubmed_publication_date":"01 Mar 2016","pubmed_entrez_date":"2016-03-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-03-06 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7498728","title":"sck1, a high copy number suppressor of defects in the cAMP-dependent protein kinase pathway in fission yeast, encodes a protein homologous to the Saccharomyces cerevisiae SCH9 kinase.","citation":"Genetics 1995 Jun;140(2):457-67","abstract":"Schizosaccharomyces pombe regulates intracellular cAMP levels, and thus cAMP-dependent protein kinase (PKA) activity, in response to changes in nutrient conditions. Mutations in any of eight git genes inhibit glucose repression of fbp1 transcription, alter the cell morphology, and cause a reduction in the growth rate. The eight git genes encode components of an adenylate cyclase activation pathway, adenylate cyclase itself, and the catalytic subunit of PKA. Three of these genes have been identified in other studies as regulators of meiosis. Here we show that the sck1 gene, cloned as a high copy number suppressor of a mutation in git3, is able to suppress the defects conferred by a mutation in any of these git genes. Sequence analysis suggests that sck1 encodes a protein most closely related to the Saccharomyces cerevisiae SCH9 protein kinase that had previously been identified as a high copy number suppressor of mutations in S. cerevisiae that reduce or eliminate PKA activity. Disruption of the sck1 gene causes a significant delay in exit from stationary phase when combined with a disruption of the pka1 (git6) gene encoding the catalytic subunit of PKA. However, the sck1 disruption by itself has little or no effect upon fbp1 transcription, meiosis, or exit from stationary phase, and does not enhance the constitutive fbp1 transcription observed in a pka1 mutant. Therefore, sck1 appears to function in a redundant fashion to pka1, but to varying degrees, in the pathways regulated by pka1.","authors":"Jin M, Fujita M, Culley BM, Apolinario E, Yamamoto M, Maundrell K, Hoffman CS","authors_abbrev":"Jin M et al.","pubmed_publication_date":"Jun 1995","pubmed_entrez_date":"1995-06-01","publication_year":"1995","canto_session_key":"0985ee80b4323f76","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-11-01 09:37:20","canto_approved_date":"2021-02-08 09:18:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-24 14:37:56","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21C3.20c","SPBC36.12c","SPAC926.04c","SPAC1B9.02c","SPAC23H3.13c","SPBC32H8.07","SPBC19C7.03","SPCC1753.02c","SPBC106.10"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2013-11-01"},{"uniquename":"PMID:22461145","title":"Identification of an Hsp90 mutation that selectively disrupts cAMP/PKA signaling in Saccharomyces cerevisiae.","citation":"Curr Genet 2012 Jun;58(3):149-63","abstract":"The molecular chaperone Hsp90 cooperates with multiple cochaperone proteins as it promotes the folding and activation of diverse client proteins. Some cochaperones regulate the ATPase activity of Hsp90, while others appear to promote Hsp90 interaction with specific types of client proteins. Through its interaction with the adenylate cyclase Cyr1, the Sgt1 cochaperone modulates the activity of the cAMP pathway in Saccharomyces cerevisiae. A specific mutation in yeast Hsp90, hsc82-W296A, or a mutation in Sgt1, sgt1-K360E, resulted in altered transcription patterns genetically linked to the cAMP pathway. Hsp90 interacted with Cyr1 in vivo and the hsc82-W296A mutation resulted in reduced accumulation of Cyr1. Hsp90-Sgt1 interaction was altered by either the hsc82-W296A or sgt1-K360E mutation, suggesting defective Hsp90-Sgt1 cooperation leads to reduced Cyr1 activity. Microarray analysis of hsc82-W296A cells indicated that over 80 % of all transcriptional changes in this strain may be attributed to altered cAMP signaling. This suggests that a majority of the cellular defects observed in hsc82-W296A cells are due to altered interaction with one specific essential cochaperone, Sgt1 and one essential client, Cyr1. Together our results indicate that specific interaction of Hsp90 and Sgt1 with Cyr1 plays a key role in regulating gene expression, including genes involved in polarized morphogenesis.","doi":"10.1007/s00294-012-0373-7","authors":"Flom GA, Langner E, Johnson JL","authors_abbrev":"Flom GA et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2012-03-31","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.04c","SPBC36.12c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:23211746","title":"Initiation of DNA damage responses through XPG-related nucleases.","citation":"EMBO J 2013 Jan 23;32(2):290-302","abstract":"Lesion-specific enzymes repair different forms of DNA damage, yet all lesions elicit the same checkpoint response. The common intermediate required to mount a checkpoint response is thought to be single-stranded DNA (ssDNA), coated by replication protein A (RPA) and containing a primer-template junction. To identify factors important for initiating the checkpoint response, we screened for genes that, when overexpressed, could amplify a checkpoint signal to a weak allele of chk1 in fission yeast. We identified Ast1, a novel member of the XPG-related family of endo/exonucleases. Ast1 promotes checkpoint activation caused by the absence of the other XPG-related nucleases, Exo1 and Rad2, the homologue of Fen1. Each nuclease is recruited to DSBs, and promotes the formation of ssDNA for checkpoint activation and recombinational repair. For Rad2 and Exo1, this is independent of their S-phase role in Okazaki fragment processing. This XPG-related pathway is distinct from MRN-dependent responses, and each enzyme is critical for damage resistance in MRN mutants. Thus, multiple nucleases collaborate to initiate DNA damage responses, highlighting the importance of these responses to cellular fitness.","doi":"10.1038/emboj.2012.322","authors":"Kuntz K, O'Connell MJ","authors_abbrev":"Kuntz K et al.","pubmed_publication_date":"23 Jan 2013","pubmed_entrez_date":"2012-12-06","publication_year":"2013","canto_session_key":"472cd1acc285281c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-08-18 15:33:33","canto_approved_date":"2024-01-11 19:05:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-05 07:46:42","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":46,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC3G6.06c","SPBC660.13c","SPCC126.02c","SPBC1734.02c","SPAC30D11.10","SPBC29A10.05","SPCC1259.13","SPAC27E2.05","SPCC962.05","SPAC13C5.07"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2015-08-18"},{"uniquename":"PMID:8374168","title":"A functional homologue of the RNA1 gene product in Schizosaccharomyces pombe: purification, biochemical characterization, and identification of a leucine-rich repeat motif.","citation":"Mol Biol Cell 1993 Jun;4(6):569-81","abstract":"The RNA1 gene from Saccharomyces cerevisiae is defined by the temperature-sensitive rna1-1 mutation that interferes with the maturation and/or nucleocytoplasmic transport of RNA. We describe the purification of a 44-kDa protein from the evolutionary distant fission yeast Schizosaccharomyces pombe and the cloning and sequence analysis of the corresponding gene. Although this protein shares only 42% sequence identity with the RNA1 gene product, it represents a functional homologue because the expression of the S. pombe gene in S. cerevisiae complements the rna1-1 defect. Disruption in S. pombe of the gene encoding the 44-kDa protein, for which we propose the name S. pombe rna1p, reveals that it is essential for growth. Our analysis of purified S. pombe rna1p represents the first biochemical characterization of an RNA1 gene product and reveals that it is a monomeric protein of globular shape. Cell fractionation and immunofluorescence microscopy indicate that rna1p is a cytoplasmic protein possibly enriched in the nuclear periphery. We identify a sequence motif of 29 residues, which is rich in leucine and repeated eight times both in S. pombe and in S. cerevisiae rna1p. Similar leucine-rich repeats present in a series of other proteins, e.g., the mammalian ribonuclease/angiogenin inhibitor, adenylyl cyclase from S. cerevisiae, the toll protein from Drosophila melanogaster, and the sds22 protein phosphatase regulatory subunit from S. pombe, are thought to be involved in protein-protein interactions. Thus rna1p may act as a scaffold protein possibly interacting in the nuclear periphery with a protein ligand that could be associated with exported RNA.","authors":"Melchior F, Weber K, Gerke V","authors_abbrev":"Melchior F et al.","pubmed_publication_date":"Jun 1993","pubmed_entrez_date":"1993-06-01","publication_year":"1993","canto_session_key":"6ccd3d72e233f12b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-04-29 18:54:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 18:54:12","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-29"},{"uniquename":"PMID:21211723","title":"Asf1/HIRA facilitate global histone deacetylation and associate with HP1 to promote nucleosome occupancy at heterochromatic loci.","citation":"Mol Cell 2011 Jan 07;41(1):56-66","abstract":"Heterochromatin impacts various nuclear processes by providing a recruiting platform for diverse chromosomal proteins. In fission yeast, HP1 proteins Chp2 and Swi6, which bind to methylated histone H3 lysine 9, associate with SHREC (Snf2/HDAC repressor complex) and Clr6 histone deacetylases (HDACs) involved in heterochromatic silencing. However, heterochromatic silencing machinery is not fully defined. We describe a histone chaperone complex containing Asf1 and HIRA that spreads across silenced domains via its association with Swi6 to enforce transcriptional silencing. Asf1 functions in concert with a Clr6 HDAC complex to silence heterochromatic repeats, and it suppresses antisense transcription by promoting histone deacetylation. Furthermore, we demonstrate that Asf1 and SHREC facilitate nucleosome occupancy at heterochromatic regions but TFIIIC transcription factor binding sites within boundary elements are refractory to these factors. These analyses uncover a role for Asf1 in global histone deacetylation and suggest that HP1-associated histone chaperone promotes nucleosome occupancy to assemble repressive heterochromatin.","doi":"10.1016/j.molcel.2010.12.009","authors":"Yamane K, Mizuguchi T, Cui B, Zofall M, Noma K, Grewal SI","authors_abbrev":"Yamane K et al.","pubmed_publication_date":"07 Jan 2011","pubmed_entrez_date":"2011-01-08","publication_year":"2011","canto_session_key":"24f09f2166d1c063","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-30 15:42:25","canto_approved_date":"2025-12-03 12:09:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-17 15:04:04","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":40,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC83.03c","SPAC23H4.12","SPBC800.03","SPBC428.08c","SPAC664.01c","SPAC1834.03c","SPBP35G2.10","SPBC36.05c","SPBC31F10.14c","SPAC25H1.06","SPAC1834.04","SPBC16D10.09","SPBC31F10.13c","SPBC8D2.03c","SPBC29A10.03c","SPBC947.08c","SPAC26H5.03","SPBC8D2.04","SPCC663.05c","SPBC15D4.03"],"gene_count":20,"ltp_gene_count":20,"approved_date":"2024-01-30"},{"uniquename":"PMID:36901728","title":"Analysis of the Localization of  Schizosaccharomyces pombe  Glucan Synthases in the Presence of the Antifungal Agent Caspofungin.","citation":"Int J Mol Sci 2023 Feb 21;24(5)","abstract":"In recent years, invasive fungal infections have emerged as a common source of infections in immunosuppressed patients. All fungal cells are surrounded by a cell wall that is essential for cell integrity and survival. It prevents cell death and lysis resulting from high internal turgor pressure. Since the cell wall is not present in animal cells, it is an ideal target for selective invasive fungal infection treatments. The antifungal family known as echinocandins, which specifically inhibit the synthesis of the cell wall β(13)glucan, has been established as an alternative treatment for mycoses. To explore the mechanism of action of these antifungals, we analyzed the cell morphology and glucan synthases localization in  Schizosaccharomyces pombe  cells during the initial times of growth in the presence of the echinocandin drug caspofungin.  S. pombe  are rod-shaped cells that grow at the poles and divide by a central division septum. The cell wall and septum are formed by different glucans, which are synthesized by four essential glucan synthases: Bgs1, Bgs3, Bgs4, and Ags1. Thus,  S. pombe  is not only a perfect model for studying the synthesis of the fungal β(1-3)glucan, but also it is ideal for examining the mechanisms of action and resistance of cell wall antifungals. Herein, we examined the cells in a drug susceptibility test in the presence of either lethal or sublethal concentrations of caspofungin, finding that exposure to the drug for long periods at high concentrations (>10 µg/mL) induced cell growth arrest and the formation of rounded, swollen, and dead cells, whereas low concentrations (<10 µg/mL) permitted cell growth with a mild effect on cell morphology. Interestingly, short-term treatments with either high or low concentrations of the drug induced effects contrary to those observed in the susceptibility tests. Thus, low drug concentrations induced a cell death phenotype that was not observed at high drug concentrations, which caused transient fungistatic cell growth arrest. After 3 h, high concentrations of the drug caused the following: (i) a decrease in the GFP-Bgs1 fluorescence level; (ii) altered locations of Bgs3, Bgs4, and Ags1; and (iii) a simultaneous accumulation of cells with calcofluor-stained incomplete septa, which at longer times resulted in septation uncoupling from plasma membrane ingression. The incomplete septa revealed with calcofluor were found to be complete when observed via the membrane-associated GFP-Bgs or Ags1-GFP. Finally, we found that the accumulation of incomplete septa depended on Pmk1, the last kinase of the cell wall integrity pathway.","doi":"10.3390/ijms24054299","authors":"San-Quirico E, Curto MÁ, Gómez-Delgado L, Moreno MB, Pérez P, Ribas JC, Cortés JCG","authors_abbrev":"San-Quirico E et al.","pubmed_publication_date":"21 Feb 2023","pubmed_entrez_date":"2023-03-11","publication_year":"2023","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2023-03-12 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010493","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35970865","title":"The Mis6 inner kinetochore subcomplex maintains CENP-A nucleosomes against centromeric non-coding transcription during mitosis.","citation":"Commun Biol 2022 Aug 15;5(1):818","abstract":"Centromeres are established by nucleosomes containing the histone H3 variant CENP-A. CENP-A is recruited to centromeres by the Mis18-HJURP machinery. During mitosis, CENP-A recruitment ceases, implying the necessity of CENP-A maintenance at centromeres, although the exact underlying mechanism remains elusive. Herein, we show that the inner kinetochore protein Mis6 (CENP-I) and Mis15 (CENP-N) retain CENP-A during mitosis in fission yeast. Eliminating Mis6 or Mis15 during mitosis caused immediate loss of pre-existing CENP-A at centromeres. CENP-A loss occurred due to the transcriptional upregulation of non-coding RNAs at the central core region of centromeres, as confirmed by the observation RNA polymerase II inhibition preventing CENP-A loss from centromeres in the mis6 mutant. Thus, we concluded that the inner kinetochore complex containing Mis6-Mis15 blocks the indiscriminate transcription of non-coding RNAs at the core centromere, thereby retaining the epigenetic inheritance of CENP-A during mitosis.","doi":"10.1038/s42003-022-03786-y","authors":"Hirai H, Shogaki Y, Sato M","authors_abbrev":"Hirai H et al.","pubmed_publication_date":"15 Aug 2022","pubmed_entrez_date":"2022-08-15","publication_year":"2022","canto_session_key":"b10feb0836d1f5f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2022-10-06 11:47:46","canto_approved_date":"2025-09-03 10:49:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-10-05 08:57:41","canto_added_date":"2022-08-18 00:15:04","annotation_curators":[{"name":"Masamitsu Sato","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.20c","SPBP22H7.09c","SPAPB1A10.02","SPAC1F7.01c","SPAC27F1.04c","SPAC25A8.01c","SPBC27B12.02","SPBC1105.17","SPBC609.05","SPAC6F12.15c","SPBC28F2.12","SPBC409.04c"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2022-10-06"},{"uniquename":"PMID:17043891","title":"Oxidative stress in Schizosaccharomyces pombe: different H2O2 levels, different response pathways.","citation":"Mol Genet Genomics 2006 Dec;276(6):495-502","abstract":"Schizosaccharomyces pombe triggers different signalling pathways depending on the severity of the oxidative stress exerted, the main ones being the Pap1 and the Sty1 pathways. The Pap1 transcription factor is more sensitive to hydrogen peroxide (H(2)O(2)) than the MAP kinase Sty1 pathway, and is designed to induce adaptation, rather than survival, responses. The peroxiredoxin Tpx1 acts as a H(2)O(2) sensor and the upstream activator of the Pap1 pathway. Therefore, sensitivity to H(2)O(2) depends on this thioredoxin peroxidase. In order to achieve maximal activation of the MAP kinase pathway, the concentration of H(2)O(2) needs to be at least fivefold higher than that to fully activate Pap1. Tpx1 is a H(2)O(2) scavenger, thus its peroxidase activity is essential for aerobic growth. As described for other eukaryotic peroxiredoxins, high doses of H(2)O(2) temporarily inactivate Tpx1 and delay Pap1 activation, whereas the Sty1 pathway remains fully functional under these conditions. As part of the Sty1-dependent transcriptional response, the expression of Srx1 is induced and this reductase re-activates the over-oxidised Tpx1. Therefore, the antioxidant pathways of the fission yeast are perfectly designed so that the transcriptional programs triggered by the different signalling pathways never overlap.","authors":"Vivancos AP, Jara M, Zuin A, Sansó M, Hidalgo E","authors_abbrev":"Vivancos AP et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-10-18","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22558440","title":"Cuf2 is a novel meiosis-specific regulatory factor of meiosis maturation.","citation":"PLoS One 2012;7(4):e36338","abstract":"Meiosis is the specialized form of the cell cycle by which diploid cells produce the haploid gametes required for sexual reproduction. Initiation and progression through meiosis requires that the expression of the meiotic genes is precisely controlled so as to provide the correct gene products at the correct times. During meiosis, four temporal gene clusters are either induced or repressed by a cascade of transcription factors.\nIn this report a novel copper-fist-type regulator, Cuf2, is shown to be expressed exclusively during meiosis. The expression profile of the cuf2(+) mRNA revealed that it was induced during middle-phase meiosis. Both cuf2(+) mRNA and protein levels are unregulated by copper addition or starvation. The transcription of cuf2(+) required the presence of a functional mei4(+) gene encoding a key transcription factor that activates the expression of numerous middle meiotic genes. Microscopic analyses of cells expressing a functional Cuf2-GFP protein revealed that Cuf2 co-localized with both homologous chromosomes and sister chromatids during the meiotic divisions. Cells lacking Cuf2 showed an elevated and sustained expression of several of the middle meiotic genes that persisted even during late meiosis. Moreover, cells carrying disrupted cuf2Δ/cuf2Δ alleles displayed an abnormal morphology of the forespore membranes and a dramatic reduction of spore viability.\nCollectively, the results revealed that Cuf2 functions in the timely repression of the middle-phase genes during meiotic differentiation.","doi":"10.1371/journal.pone.0036338","authors":"Ioannoni R, Beaudoin J, Lopez-Maury L, Codlin S, Bahler J, Labbe S","authors_abbrev":"Ioannoni R et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-05-05","publication_year":"2012","canto_session_key":"2306fd737a53d0b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Raphael Ioannoni","canto_first_approved_date":"2017-03-17 13:06:01","canto_approved_date":"2025-12-03 12:22:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-03-25 16:15:54","canto_added_date":"2012-11-13 19:41:09","annotation_curators":[{"name":"Raphael Ioannoni","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC162.04c","SPBC32H8.11","SPAC1B2.03c","SPBC1348.01","SPAC1610.03c","SPCC825.03c","SPBC19C2.05","SPBC1347.03","SPCC584.02","SPCC1393.10"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2017-03-17"},{"uniquename":"PMID:8879048","title":"Purification of Sxa2, a carboxypeptidase involved in pheromone recovery in fission yeast.","citation":"Biochem Soc Trans 1996 Aug;24(3):504S","abstract":"","authors":"Ladds G, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_session_key":"af1b2fb92c778beb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-05 12:34:04","canto_approved_date":"2025-05-19 08:28:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-03-22 17:04:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1296.03c","SPCC1795.06"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-02-05"},{"uniquename":"EMBL:SPC06443","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42017229","title":"Temperature-specific regulation of the NDR kinase Orb6 by the MAPK Sty1 to promote heat stress resilience.","citation":"J Cell Sci 2026 Apr 15;139(8)","abstract":"The cellular response to environmental fluctuations, such as increased temperature, is crucial in promoting cell survival and plays an increasingly recognized role in cancer biology. Important cellular functions altered by heat stress are cell polarization and protein translation. Previous studies have shown that heat stress alters the dynamics of Cdc42, a key regulator of cell polarization in eukaryotes, and promotes ribonucleoprotein (RNP) granule formation, reprogramming protein translation. The biological mechanisms underlying these vast changes are only partially known. Here, we report that the conserved NDR kinase Orb6, a homolog of mammalian STK38, responds to heat stress and regulates heat stress resilience by modulating Cdc42 dynamics and promoting RNP granule assembly in Schizosaccharomyces pombe. Also, we discovered a finely tuned mechanism whereby stress-activated mitogen-activated protein kinase (MAPK) Sty1 negatively regulates Orb6 kinase and Orb6 C-terminal phosphorylation during heat stress. Orb6 inhibition by Sty1 increases the sensitivity of the cell to heat stress in a temperature-specific manner, fostering increased stress resilience and metabolic adaptation. These observations highlight the role of NDR kinase in the process of heat adaptation and thermotolerance during environmental cell exposure to elevated temperatures.","doi":"10.1242/jcs.264507","authors":"Doyle LP, Tams RN, Chen C, Nuñez I, Haller PR, Verde F","authors_abbrev":"Doyle LP et al.","pubmed_publication_date":"15 Apr 2026","pubmed_entrez_date":"2026-04-22","publication_year":"2026","canto_session_key":"b2085c6d6df436bb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.12","SPAC24B11.06c","SPCC16C4.09"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:31037469","title":"The molecular basis of monopolin recruitment to the kinetochore.","citation":"Chromosoma 2019 Sep;128(3):331-354","abstract":"The monopolin complex is a multifunctional molecular crosslinker, which in S. pombe binds and organises mitotic kinetochores to prevent aberrant kinetochore-microtubule interactions. In the budding yeast S. cerevisiae, whose kinetochores bind a single microtubule, the monopolin complex crosslinks and mono-orients sister kinetochores in meiosis I, enabling the biorientation and segregation of homologs. Here, we show that both the monopolin complex subunit Csm1 and its binding site on the kinetochore protein Dsn1 are broadly distributed throughout eukaryotes, suggesting a conserved role in kinetochore organisation and function. We find that budding yeast Csm1 binds two conserved motifs in Dsn1, one (termed Box 1) representing the ancestral, widely conserved monopolin binding motif and a second (termed Box 2-3) with a likely role in enforcing specificity of sister kinetochore crosslinking. We find that Box 1 and Box 2-3 bind the same conserved hydrophobic cavity on Csm1, suggesting competition or handoff between these motifs. Using structure-based mutants, we also find that both Box 1 and Box 2-3 are critical for monopolin function in meiosis. We identify two conserved serine residues in Box 2-3 that are phosphorylated in meiosis and whose mutation to aspartate stabilises Csm1-Dsn1 binding, suggesting that regulated phosphorylation of these residues may play a role in sister kinetochore crosslinking specificity. Overall, our results reveal the monopolin complex as a broadly conserved kinetochore organiser in eukaryotes, which budding yeast have co-opted to mediate sister kinetochore crosslinking through the addition of a second, regulatable monopolin binding interface.","doi":"10.1007/s00412-019-00700-0","authors":"Plowman R, Singh N, Tromer EC, Payan A, Duro E, Spanos C, Rappsilber J, Snel B, Kops GJPL, Corbett KD, Marston AL","authors_abbrev":"Plowman R et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-05-01","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11E3.03","SPBC409.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:37193545","title":"Fission yeast obeys a linear size law under nutrient titration.","citation":"MicroPubl Biol 2023;2023","abstract":"Steady-state cell size and geometry depend on growth conditions. Here, we use an experimental setup based on continuous culture and single-cell imaging to study how cell volume, length, width and surface-to-volume ratio vary across a range of growth conditions including nitrogen and carbon titration, the choice of nitrogen source, and translation inhibition. Overall, we find cell geometry is not fully determined by growth rate and depends on the specific mode of growth rate modulation. However, under nitrogen and carbon titrations, we observe that the cell volume and the growth rate follow the same linear scaling.","doi":"10.17912/micropub.biology.000833","authors":"Bertaux F, Kleijn IT, Marguerat S, Shahrezaei V","authors_abbrev":"Bertaux F et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-05-16","publication_year":"2023","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2023-05-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8497309","title":"Cell cycle. Sunburnt fission yeast.","citation":"Nature 1993 May 27;363(6427):302","abstract":"","authors":"Murray AW","authors_abbrev":"Murray AW","pubmed_publication_date":"27 May 1993","pubmed_entrez_date":"1993-05-27","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18257517","title":"Phosphoproteome analysis of fission yeast.","citation":"J Proteome Res 2008 Mar;7(3):1088-97","abstract":"Phosphorylation is a key regulator of many events in eukaryotic cells. The acquisition of large-scale phosphorylation data sets from model organisms can pinpoint conserved regulatory inputs and reveal kinase-substrate relationships. Here, we provide the first large-scale phosphorylation analysis of the fission yeast, Schizosaccharomyces pombe. Protein from thiabendazole-treated cells was separated by preparative SDS-PAGE and digested with trypsin. The resulting peptides were subjected to either IMAC or TiO2 phosphopeptide enrichment methods and then analyzed by LC-MS/MS using an LTQ-Orbitrap mass spectrometer. In total, 2887 distinct phosphorylation sites were identified from 1194 proteins with an estimated false-discovery rate of <0.5% at the peptide level. A comparison of the two different enrichment methods is presented, supporting the finding that they are complementary. Finally, phosphorylation sites were examined for phosphorylation-specific motifs and evolutionary conservation. These analyses revealed both motifs and specific phosphorylation events identified in S. pombe were conserved and predicted novel phosphorylation in mammals.","doi":"10.1021/pr7006335","authors":"Wilson-Grady JT, Villén J, Gygi SP","authors_abbrev":"Wilson-Grady JT et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-02-09","publication_year":"2008","canto_session_key":"640df135c586fdb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2015-02-16 10:50:40","canto_approved_date":"2024-10-17 06:01:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-17 18:04:47","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"file_curator_name":"Kim Rutherford","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Kim 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mass spectrometry-based analysis of the fission yeast proteome: the Schizosaccharomyces pombe PeptideAtlas.","citation":"Mol Cell Proteomics 2013 Jun;12(6):1741-51","abstract":"We report a high quality and system-wide proteome catalogue covering 71% (3,542 proteins) of the predicted genes of fission yeast, Schizosaccharomyces pombe, presenting the largest protein dataset to date for this important model organism. We obtained this high proteome and peptide (11.4 peptides/protein) coverage by a combination of extensive sample fractionation, high resolution Orbitrap mass spectrometry, and combined database searching using the iProphet software as part of the Trans-Proteomics Pipeline. All raw and processed data are made accessible in the S. pombe PeptideAtlas. The identified proteins showed no biases in functional properties and allowed global estimation of protein abundances. The high coverage of the PeptideAtlas allowed correlation with transcriptomic data in a system-wide manner indicating that post-transcriptional processes control the levels of at least half of all identified proteins. Interestingly, the correlation was not equally tight for all functional categories ranging from r(s) >0.80 for proteins involved in translation to r(s) <0.45 for signal transduction proteins. Moreover, many proteins involved in DNA damage repair could not be detected in the PeptideAtlas despite their high mRNA levels, strengthening the translation-on-demand hypothesis for members of this protein class. In summary, the extensive and publicly available S. pombe PeptideAtlas together with the generated proteotypic peptide spectral library will be a useful resource for future targeted, in-depth, and quantitative proteomic studies on this microorganism.","doi":"10.1074/mcp.M112.023754","authors":"Gunaratne J, Schmidt A, Quandt A, Neo SP, Saraç OS, Gracia T, Loguercio S, Ahrné E, Xia RL, Tan KH, Lössner C, Bähler J, Beyer A, Blackstock W, Aebersold R","authors_abbrev":"Gunaratne J et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-03-07","publication_year":"2013","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11179008","title":"Tissue-specific expression of a splicing mutation in the IKBKAP gene causes familial dysautonomia.","citation":"Am J Hum Genet 2001 Mar;68(3):598-605","abstract":"Familial dysautonomia (FD; also known as \"Riley-Day syndrome\"), an Ashkenazi Jewish disorder, is the best known and most frequent of a group of congenital sensory neuropathies and is characterized by widespread sensory and variable autonomic dysfunction. Previously, we had mapped the FD gene, DYS, to a 0.5-cM region on chromosome 9q31 and had shown that the ethnic bias is due to a founder effect, with >99.5% of disease alleles sharing a common ancestral haplotype. To investigate the molecular basis of FD, we sequenced the minimal candidate region and cloned and characterized its five genes. One of these, IKBKAP, harbors two mutations that can cause FD. The major haplotype mutation is located in the donor splice site of intron 20. This mutation can result in skipping of exon 20 in the mRNA of patients with FD, although they continue to express varying levels of wild-type message in a tissue-specific manner. RNA isolated from lymphoblasts of patients is primarily wild-type, whereas only the deleted message is seen in RNA isolated from brain. The mutation associated with the minor haplotype in four patients is a missense (R696P) mutation in exon 19, which is predicted to disrupt a potential phosphorylation site. Our findings indicate that almost all cases of FD are caused by an unusual splice defect that displays tissue-specific expression; and they also provide the basis for rapid carrier screening in the Ashkenazi Jewish population.","authors":"Slaugenhaupt SA, Blumenfeld A, Gill SP, Leyne M, Mull J, Cuajungco MP, Liebert CB, Chadwick B, Idelson M, Reznik L, Robbins C, Makalowska I, Brownstein M, Krappmann D, Scheidereit C, Maayan C, Axelrod FB, Gusella JF","authors_abbrev":"Slaugenhaupt SA et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-02-17","publication_year":"2001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC36.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26305931","title":"Telomerase RNA stem terminus element affects template boundary element function, telomere sequence, and shelterin binding.","citation":"Proc Natl Acad Sci U S A 2015 Sep 08;112(36):11312-7","abstract":"The stem terminus element (STE), which was discovered 13 y ago in human telomerase RNA, is required for telomerase activity, yet its mode of action is unknown. We report that the Schizosaccharomyces pombe telomerase RNA, TER1 (telomerase RNA 1), also contains a STE, which is essential for telomere maintenance. Cells expressing a partial loss-of-function TER1 STE allele maintained short stable telomeres by a recombination-independent mechanism. Remarkably, the mutant telomere sequence was different from that of wild-type cells. Generation of the altered sequence is explained by reverse transcription into the template boundary element, demonstrating that the STE helps maintain template boundary element function. The altered telomeres bound less Pot1 (protection of telomeres 1) and Taz1 (telomere-associated in Schizosaccharomyces pombe 1) in vivo. Thus, the S. pombe STE, although distant from the template, ensures proper telomere sequence, which in turn promotes proper assembly of the shelterin complex.","doi":"10.1073/pnas.1503157112","authors":"Webb CJ, Zakian VA","authors_abbrev":"Webb CJ et al.","pubmed_publication_date":"08 Sep 2015","pubmed_entrez_date":"2015-08-26","publication_year":"2015","canto_session_key":"18e97108cb413e18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Virginia Zakian","canto_first_approved_date":"2016-10-04 08:41:36","canto_approved_date":"2020-12-28 22:21:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-22 12:43:00","canto_added_date":"2015-08-27 00:18:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Virginia Zakian","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.214","SPAC16A10.07c","SPCC188.07","SPAC26H5.06","SPBC29A3.14c","SPBC2D10.13","SPAC644.14c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2016-10-04"},{"uniquename":"PMID:28733400","title":"Visualization of a Specific Genome Locus by the  lacO /LacI-GFP System.","citation":"Cold Spring Harb Protoc 2017 Oct 03;2017(10):pdb.prot091934","abstract":"Observing the dynamics of a specific chromosome locus in living cells can provide important information as to the molecular mechanisms underlying events such as chromosome segregation, homologous chromosome pairing, chromosome arrangement, and gene expression. The  lacO /LacI-GFP system provides a simple and useful method in which a chromosome locus is visualized by inserting  lacO  repeat arrays and then expressing an LacI-GFP fusion that specifically binds to the  lacO  sequence. This system has been adapted for use in  Schizosaccharomyces pombe  by expressing the LacI-GFP under a promoter of the  dis1  +  gene. Furthermore, a two-step integration method has been developed that ensures high-efficiency integration of  lacO  arrays to a desired target position.","doi":"10.1101/pdb.prot091934","authors":"Ding DQ, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"03 Oct 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29735656","title":"Suppressor mutation analysis combined with 3D modeling explains cohesin's capacity to hold and release DNA.","citation":"Proc Natl Acad Sci U S A 2018 May 22;115(21):E4833-E4842","abstract":"Cohesin is a fundamental protein complex that holds sister chromatids together. Separase protease cleaves a cohesin subunit Rad21/SCC1, causing the release of cohesin from DNA to allow chromosome segregation. To understand the functional organization of cohesin, we employed next-generation whole-genome sequencing and identified numerous extragenic suppressors that overcome either inactive separase/Cut1 or defective cohesin in the fission yeast  Schizosaccharomyces pombe  Unexpectedly, Cut1 is dispensable if suppressor mutations cause disorders of interfaces among essential cohesin subunits Psm1/SMC1, Psm3/SMC3, Rad21/SCC1, and Mis4/SCC2, the crystal structures of which suggest physical and functional impairment at the interfaces of Psm1/3 hinge, Psm1 head-Rad21, or Psm3 coiled coil-Rad21. Molecular-dynamics analysis indicates that the intermolecular β-sheets in the cohesin hinge of  cut1  suppressor mutants remain intact, but a large mobility change occurs at the coiled coil bound to the hinge. In contrast, suppressors of  rad21-K1  occur in either the head ATPase domains or the Psm3 coiled coil that interacts with Rad21. Suppressors of  mis4-G1326E  reside in the head of Psm3/1 or the intragenic domain of Mis4. These may restore the binding of cohesin to DNA. Evidence is provided that the head and hinge of SMC subunits are proximal, and that they coordinate to form arched coils that can hold or release DNA by altering the angles made by the arched coiled coils. By combining molecular modeling with suppressor sequence analysis, we propose a cohesin structure designated the \"hold-and-release\" model, which may be considered as an alternative to the prevailing \"ring\" model.","doi":"10.1073/pnas.1803564115","authors":"Xu X, Kanai R, Nakazawa N, Wang L, Toyoshima C, Yanagida M","authors_abbrev":"Xu X et al.","pubmed_publication_date":"22 May 2018","pubmed_entrez_date":"2018-05-09","publication_year":"2018","canto_session_key":"16ad711046a3f839","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xingya Xu","canto_first_approved_date":"2019-05-29 10:43:45","canto_approved_date":"2025-09-03 12:57:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-20 15:02:13","canto_added_date":"2018-05-09 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Xingya Xu","community_curator":true,"annotation_count":37,"orcid":"0000-0002-3728-2633","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC10F6.09c","SPCC5E4.04","SPBC29A10.04","SPAC31A2.05c","SPBC14C8.01c","SPCC338.17c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-05-29"},{"uniquename":"PMID:29804820","title":"Mis16 Switches Function from a Histone H4 Chaperone to a CENP-A Cnp1 -Specific Assembly Factor through Eic1 Interaction.","citation":"Structure 2018 Jul 03;26(7):960-971.e4","abstract":"The Mis18 complex, composed of Mis16, Eic1, and Mis18 in fission yeast, selectively deposits the centromere-specific histone H3 variant, CENP-A Cnp1 , at centromeres. How the intact Mis18 holo-complex oligomerizes and how Mis16, a well-known ubiquitous histone H4 chaperone, plays a centromere-specific role in the Mis18 holo-complex, remain unclear. Here, we report the stoichiometry of the intact Mis18 holo-complex as (Mis16) 2 :(Eic1) 2 :(Mis18) 4  using analytical ultracentrifugation. We further determine the crystal structure of Schizosaccharomyces pombe Mis16 in complex with the C-terminal portion of Eic1 (Eic1-CT). Notably, Mis16 accommodates Eic1-CT through the binding pocket normally occupied by histone H4, indicating that Eic1 and H4 compete for the same binding site, providing a mechanism for Mis16 to switch its binding partner from histone H4 to Eic1. Thus, our analyses not only determine the stoichiometry of the intact Mis18 holo-complex but also uncover the molecular mechanism by which Mis16 plays a centromere-specific role through Eic1 association.","doi":"10.1016/j.str.2018.04.012","authors":"An S, Koldewey P, Chik J, Subramanian L, Cho US","authors_abbrev":"An S et al.","pubmed_publication_date":"03 Jul 2018","pubmed_entrez_date":"2018-05-29","publication_year":"2018","canto_session_key":"f6960ee6a5709c02","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Uhn-Soo Cho","canto_first_approved_date":"2023-04-03 09:55:56","canto_approved_date":"2025-09-03 12:55:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-04-03 09:55:49","canto_added_date":"2018-05-31 00:15:03","annotation_curators":[{"name":"Uhn-Soo Cho","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27B12.02","SPBC1105.12","SPBC8D2.03c","SPCC1672.10","SPAC1834.03c","SPCC970.12"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2023-04-03","pdb_entries":[{"pdb_id":"5wjc","gene_chains":[{"gene_uniquename":"SPBC27B12.02","chain":"B","position":"1-112"},{"gene_uniquename":"SPCC1672.10","chain":"A","position":"1-430"}],"title":"Crystal structure of Schizosaccharomyces pombe Mis16 in complex with Eic1","entry_authors":"An S,Cho U-S,Koldewey P,Chik J,Subramanian L","entry_authors_abbrev":"An S et al.","reference_uniquename":"PMID:29804820","experimental_method":"X-ray","resolution":"2.298"}]},{"uniquename":"PMID:41806041","title":"Emw1/TTC27 is a chaperone required for folding of the eukaryotic elongation factor 2.","citation":"Cell Mol Life Sci 2026 Mar 10;","abstract":"","doi":"10.1007/s00018-026-06154-9","authors":"Yang M, Li R, Mikolajczak AI, Wright VA, Hassan M, Vaughan CK, Prescott TAK, Heritz JA, Mollapour M, Panaretou B","authors_abbrev":"Yang M et al.","pubmed_publication_date":"10 Mar 2026","pubmed_entrez_date":"2026-03-10","publication_year":"2026","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCP31B10.07","SPAC19B12.01","SPAC513.01c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:21450810","title":"Point mutations in the Rpb9-homologous domain of Rpc11 that impair transcription termination by RNA polymerase III.","citation":"Nucleic Acids Res 2011 Aug;39(14):6100-13","abstract":"RNA polymerase III recognizes and pauses at its terminator, an oligo(dT) tract in non-template DNA, terminates 3' oligo(rU) synthesis within this sequence, and releases the RNA. The pol III subunit Rpc11p (C11) mediates RNA 3'-5' cleavage in the catalytic center of pol III during pausing. The amino and carboxyl regions of C11 are homologous to domains of the pol II subunit Rpb9p, and the pol II elongation and RNA cleavage factor, TFIIS, respectively. We isolated C11 mutants from Schizosaccharomyces pombe that cause pol III to readthrough terminators in vivo. Mutant RNA confirmed the presence of terminator readthrough transcripts. A predominant mutation site, F32, resides in the C11 Rpb9-like domain. Another mutagenic approach confirmed the F32 mutation and also isolated I34 and Y30 mutants. Modeling Y30, F32 and I34 of C11 in available cryoEM pol III structures predicts a hydrophobic patch that may interface with C53/37. Another termination mutant, Rpc2-T455I, appears to reside internally, near the RNA-DNA hybrid. We show that the Rpb9 and TFIIS homologous mutants of C11 reflect distinct activities, that differentially affect terminator recognition and RNA 3' cleavage. We propose that these C11 domains integrate action at the upper jaw and center of pol III during termination.","doi":"10.1093/nar/gkr182","authors":"Iben JR, Mazeika JK, Hasson S, Rijal K, Arimbasseri AG, Russo AN, Maraia RJ","authors_abbrev":"Iben JR et al.","pubmed_publication_date":"Aug 2011","pubmed_entrez_date":"2011-04-01","publication_year":"2011","canto_session_key":"f73ec44b6db23cab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-04-21 16:40:52","canto_approved_date":"2020-04-21 16:40:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-03 15:59:07","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.05","SPAC4G9.08c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-04-21"},{"uniquename":"PMID:10931913","title":"Analysis of the splicing machinery in fission yeast: a comparison with budding yeast and mammals.","citation":"Nucleic Acids Res 2000 Aug 15;28(16):3003-10","abstract":"Based on genetic and bioinformatic analysis, 80 proteins from the newly sequenced Schizosaccharomyces pombe genome appear to be splicing factors. The fission yeast splicing factors were compared to those of Homo sapiens and Saccharomyces cerevisiae in order to determine the extent of conservation or divergence that has occurred over the billion years of evolution that separate these organisms. Our results indicate that many of the factors present in all three organisms have been well conserved throughout evolution. It is calculated that 38% of the fission yeast splicing factors are more similar to the human proteins than to the budding yeast proteins (>10% more similar or similar over a greater region). Many of the factors in this category are required for recognition of the 3' splice site. Ten fission yeast splicing factors, including putative regulatory factors, have human homologs, but no apparent budding yeast homologs based on sequence data alone. Many of the budding yeast factors that are absent in fission yeast are associated with the U1 and U4/U6.U5 snRNP. Collectively the data presented in this survey indicate that of the two yeasts, S.POMBE: contains a splicing machinery more closely reflecting the archetype of a spliceosome.","authors":"Käufer NF, Potashkin J","authors_abbrev":"Käufer NF et al.","pubmed_publication_date":"15 Aug 2000","pubmed_entrez_date":"2000-08-10","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22194353","title":"Intracellular trafficking and ubiquitination of the Schizosaccharomyces pombe amino acid permease Aat1p.","citation":"Microbiology (Reading) 2012 Mar;158(Pt 3):659-673","abstract":"In Schizosaccharomyces pombe, neither intracellular sorting nor ubiquitination of amino acid permeases is well understood. In the present study, we show that intracellular sorting of the amino acid permease Aat1p in S. pombe depends on the presence of a nitrogen source in the growth medium. Under nitrogen-sufficient conditions, Aat1p appeared to be stably localized at the Golgi apparatus. In contrast, under nitrogen-insufficient conditions, Aat1p was sorted to the plasma membrane. Over time, plasma membrane-localized Aat1p was internalized and sorted to the lumen of the vacuole, where it was degraded. Sorting of Aat1p to the vacuolar lumen was dependent on the ESCRT (endosomal sorting complex required for transport) complex, which is required for formation of the multivesicular body. S. pombe has three genes (pub1(+), pub2(+) and pub3(+)) that are homologous to the ubiquitin ligase RSP5. Under nitrogen-sufficient conditions, Aat1-GFP was missorted to the plasma membrane in pub1Δ cells and ubiquitinated Aat1p was not detected. These results suggest that Pub1p-mediated ubiquitination is required for retention of Aat1 at the Golgi under nitrogen-sufficient conditions. The Aat1p lysine mutant Aat1(K18, 26, 27) was completely missorted to the plasma membrane under nitrogen-rich conditions. Furthermore, Aat1(K4, 18R), Aat1(K4, 26, 27R) and Aat1(K18, 26, 27K) mutants were severely blocked in endocytosis. These results indicate that ubiquitination is an important determinant for localization and regulation of the Aat1p permease in S. pombe.","doi":"10.1099/mic.0.053389-0","authors":"Nakase M, Nakase Y, Chardwiriyapreecha S, Kakinuma Y, Matsumoto T, Takegawa K","authors_abbrev":"Nakase M et al.","pubmed_publication_date":"Mar 2012","pubmed_entrez_date":"2011-12-24","publication_year":"2012","canto_session_key":"a035b5a40395d9ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2017-09-16 14:12:00","canto_approved_date":"2022-07-01 08:18:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-09 03:01:35","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16E9.11c","SPAC19B12.10","SPBP16F5.07","SPBC359.03c","SPBC4B4.06","SPCP1E11.06","SPBC215.14c","SPBC25H2.16c","SPAP27G11.06c","SPAC1B3.07c","SPBC337.08c","SPBC947.02","SPAC11G7.02","SPAC1805.15c","SPAC1F3.05","SPAC9E9.14","SPAC19A8.05c"],"gene_count":17,"ltp_gene_count":9,"approved_date":"2017-09-16"},{"uniquename":"PMID:26917764","title":"The TopoVIB-Like protein family is required for meiotic DNA double-strand break formation.","citation":"Science 2016 Feb 26;351(6276):943-9","abstract":"Meiotic recombination is induced by the formation of DNA double-strand breaks (DSBs) catalyzed by SPO11, the ortholog of subunit A of TopoVI DNA topoisomerase (TopoVIA). TopoVI activity requires the interaction between A and B subunits. We identified a conserved family of plant and animal proteins [the TOPOVIB-Like (TOPOVIBL) family] that share strong structural similarity to the TopoVIB subunit of TopoVI DNA topoisomerase. We further characterize the meiotic recombination proteins Rec102 (Saccharomyces cerevisiae), Rec6 (Schizosaccharomyces pombe), and MEI-P22 (Drosophila melanogaster) as homologs to the transducer domain of TopoVIB. We demonstrate that the mouse TOPOVIBL protein interacts and forms a complex with SPO11 and is required for meiotic DSB formation. We conclude that meiotic DSBs are catalyzed by a complex involving SPO11 and TOPOVIBL.","doi":"10.1126/science.aad5309","authors":"Robert T, Nore A, Brun C, Maffre C, Crimi B, Bourbon HM, de Massy B","authors_abbrev":"Robert T et al.","pubmed_publication_date":"26 Feb 2016","pubmed_entrez_date":"2016-02-27","publication_year":"2016","canto_session_key":"8e034795a2a4a786","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-10-16 13:14:00","canto_approved_date":"2019-10-16 13:14:00","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-10-16 13:13:55","canto_added_date":"2016-02-28 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["YLR329W","SPBC21B10.12","HGNC:26197"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-10-16"},{"uniquename":"PMID:34244792","title":"RNAi and Ino80 complex control rate limiting translocation step that moves rDNA to eroding telomeres.","citation":"Nucleic Acids Res 2021 Aug 20;49(14):8161-8176","abstract":"The discovery of HAATIrDNA, a telomerase-negative survival mode in which canonical telomeres are replaced with ribosomal DNA (rDNA) repeats that acquire chromosome end-protection capability, raised crucial questions as to how rDNA tracts 'jump' to eroding chromosome ends. Here, we show that HAATIrDNA formation is initiated and limited by a single translocation that juxtaposes rDNA from Chromosome (Chr) III onto subtelomeric elements (STE) on Chr I or II; this rare reaction requires RNAi and the Ino80 nucleosome remodeling complex (Ino80C), thus defining an unforeseen relationship between these two machineries. The unique STE-rDNA junction created by this initial translocation is efficiently copied to the remaining STE chromosome ends, independently of RNAi or Ino80C. Intriguingly, both RNAi and Ino80C machineries contain a component that plays dual roles in HAATI subtype choice. Dcr1 of the RNAi pathway and Iec1 of Ino80C both promote HAATIrDNA formation as part of their respective canonical machineries, but both also inhibit formation of the exceedingly rare HAATISTE (where STE sequences mobilize throughout the genome and assume chromosome end protection capacity) in non-canonical, pathway-independent manners. This work provides a glimpse into a previously unrecognized crosstalk between RNAi and Ino80C in controlling unusual translocation reactions that establish telomere-free linear chromosome ends.","doi":"10.1093/nar/gkab586","authors":"Apte MS, Masuda H, Wheeler DL, Cooper JP","authors_abbrev":"Apte MS et al.","pubmed_publication_date":"20 Aug 2021","pubmed_entrez_date":"2021-07-10","publication_year":"2021","canto_session_key":"d7b52638e976e413","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-10-09 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30938578","title":"Hidden in plain sight: what remains to be discovered in the eukaryotic proteome?","citation":"Open Biol 2019 Feb 28;9(2):180241","abstract":"The first decade of genome sequencing stimulated an explosion in the characterization of unknown proteins. More recently, the pace of functional discovery has slowed, leaving around 20% of the proteins even in well-studied model organisms without informative descriptions of their biological roles. Remarkably, many uncharacterized proteins are conserved from yeasts to human, suggesting that they contribute to fundamental biological processes (BP). To fully understand biological systems in health and disease, we need to account for every part of the system. Unstudied proteins thus represent a collective blind spot that limits the progress of both basic and applied biosciences. We use a simple yet powerful metric based on Gene Ontology BP terms to define characterized and uncharacterized proteins for human, budding yeast and fission yeast. We then identify a set of conserved but unstudied proteins in S. pombe, and classify them based on a combination of orthogonal attributes determined by large-scale experimental and comparative methods. Finally, we explore possible reasons why these proteins remain neglected, and propose courses of action to raise their profile and thereby reap the benefits of completing the catalogue of proteins' biological roles.","doi":"10.1098/rsob.180241","authors":"Wood V, Lock A, Harris MA, Rutherford K, Bähler J, Oliver SG","authors_abbrev":"Wood V et al.","pubmed_publication_date":"28 Feb 2019","pubmed_entrez_date":"2019-04-03","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-04-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24947517","title":"The putative exchange factor Gef3p interacts with Rho3p GTPase and the septin ring during cytokinesis in fission yeast.","citation":"J Biol Chem 2014 Aug 08;289(32):21995-2007","abstract":"The small GTP-binding proteins of the Rho family and its regulatory proteins play a central role in cytokinetic actomyosin ring assembly and cytokinesis. Here we show that the fission yeast guanine nucleotide exchange factor Gef3p interacts with Rho3p at the division site. Gef3p contains a putative DH homology domain and a BAR/IMD-like domain. The protein localized to the division site late in mitosis, where it formed a ring that did not constrict with actomyosin ring (cytokinetic actomyosin ring) invagination; instead, it split into a double ring that resembled the septin ring. Gef3p co-localized with septins and Mid2p and required septins and Mid2p for its localization. Gef3p interacts physically with the GTP-bound form of Rho3p. Although Gef3p is not essential for cell separation, the simultaneous disruption of gef3(+) and Rho3p-interacting proteins, such as Sec8p, an exocyst component, Apm1p, a subunit of the clathrin adaptor complex or For3p, an actin-polymerizing protein, yielded cells with strong defects in septation and polarity respectively. Our results suggest that interactions between septins and Rho-GEFs provide a new targeting mechanism for GTPases in cytokinesis, in this case probably contributing to Rho3p function in vesicle tethering and vesicle trafficking in the later steps of cell separation.","doi":"10.1074/jbc.M114.548792","authors":"Muñoz S, Manjón E, Sánchez Y","authors_abbrev":"Muñoz S et al.","pubmed_publication_date":"08 Aug 2014","pubmed_entrez_date":"2014-06-21","publication_year":"2014","canto_session_key":"dee2cb4000771ecf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-04 07:32:47","canto_approved_date":"2021-06-18 16:08:22","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-08-22 14:36:00","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":46,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.16","SPCC970.09","SPAC16A10.04","SPAC23C4.08","SPCC895.05","SPAC110.03","SPCC1235.10c","SPBP16F5.07","SPCC825.03c","SPBC106.20","SPAPYUG7.03c","SPBC29A3.17","SPCC645.06c","SPAC16.01","SPAC4F10.11","SPAC24H6.09"],"gene_count":16,"ltp_gene_count":13,"approved_date":"2016-09-04"},{"uniquename":"PMID:4908558","title":"Activity and location of two enzyme fractions during the culture cycle of Schizosaccharomyces pombe.","citation":"Can J Microbiol 1970 Mar;16(3):187-91","abstract":"","authors":"Rock GD, Johnson BF","authors_abbrev":"Rock GD et al.","pubmed_publication_date":"Mar 1970","pubmed_entrez_date":"1970-03-01","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:64191","title":"[Transport functions of plasmic ATPase in Schizosaccharomyces pombe].","citation":"Arch Int Physiol Biochim 1976;84(3):618-9","abstract":"","authors":"Foury F, Boutry M, Goffeau A","authors_abbrev":"Foury F et al.","pubmed_publication_date":"1976","pubmed_entrez_date":"1976-01-01","publication_year":"1976","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11550467","title":"In vitro approaches for the study of microtubule nucleation at the fission yeast spindle pole body.","citation":"Methods Cell Biol 2001;67:167-77","abstract":"","authors":"Masuda H, Takada S, Shibata T, Cande WZ, Hiraoka Y","authors_abbrev":"Masuda H et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-09-12","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7521515","title":"Mutagenic and carcinogenic effects of waste oil of frying bean cake on Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Mutat Res 1994 Sep;322(3):161-7","abstract":"The present investigation was conducted to study the genotoxic effects of waste oil of frying bean cake (Taamiah oil) using Saccharomyces cerevisiae and Schizosaccharomyces pombe as test organisms. The results showed that the different concentrations of Taamiah oil exert different toxicity on yeast cells. the induced toxicity in both organisms was gradually increased with rising the concentration of Taamiah oil While, the differences between cellular survival and respiratory deficient mutants in treated and untreated samples were significant. Though Taamiah oil induced a concentration-dependent toxicity, it did not exert an induction of recombination. Thus, it seems likely that there was a cytotoxic effect and a weak effect on the induction of cytoplasmic petite mutations in yeast. The results suggest that Taamiah oil does not seem to induce lesions in DNA that are subject to excision repair. However, in Schizosaccharomyces pombe some point mutations seem to be induced in addition to toxicity. The conclusion is straight forward that waste oil of frying bean cake is mutagenic and may be carcinogenic in humans.","authors":"Zaied KA","authors_abbrev":"Zaied KA","pubmed_publication_date":"Sep 1994","pubmed_entrez_date":"1994-09-01","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10632879","title":"Proper ascospore maturation requires the chs1+ chitin synthase gene in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2000 Jan;35(1):79-89","abstract":"We have cloned chs1+, a Schizosaccharomyces pombe gene with similarity to class II chitin synthases, and have shown that it is responsible for chitin synthase activity present in cell extracts from this organism. Analysis of this activity reveals that it behaves like chitin synthases from other fungi, although with specific biochemical characteristics. Deletion or overexpression of this gene does not lead to any apparent defect during vegetative growth. In contrast, chs1+ expression increases significantly during sporulation, and this is accompanied by an increase in chitin synthase activity. In addition, spore formation is severely affected when both parental strains carry a chs1 deletion, as a result of a defect in the synthesis of the ascospore cell wall. Finally, we show that wild-type, but not chs1-/chs1-, ascospore cell walls bind wheatgerm agglutinin. Our results clearly suggest the existence of a relationship between chs1+, chitin synthesis and ascospore maturation in S. pombe.","authors":"Arellano M, Cartagena-Lirola H, Nasser Hajibagheri MA, Durán A, Henar Valdivieso M","authors_abbrev":"Arellano M et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-13","publication_year":"2000","canto_session_key":"b7a6f0807ab70d55","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-18 08:36:40","canto_approved_date":"2024-06-13 04:50:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-18 08:36:18","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G6.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-04-18"},{"uniquename":"EMBL:AJ632014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.48"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34849776","title":"An improved auxin-inducible degron system for fission yeast.","citation":"G3 (Bethesda) 2022 Jan 04;12(1)","abstract":"Conditional degron technologies, which allow a protein of interest to be degraded in an inducible manner, are important tools for biological research, and are especially useful for creating conditional loss-of-function mutants of essential genes. The auxin-inducible degron (AID) technology, which utilizes plant auxin signaling components to control protein degradation in nonplant species, is a widely used small-molecular-controlled degradation method in yeasts and animals. However, the currently available AID systems still have room for further optimization. Here, we have improved the AID system for the fission yeast Schizosaccharomyces pombe by optimizing all three components: the AID degron, the small-molecule inducer, and the inducer-responsive F-box protein. We chose a 36-amino-acid sequence of the Arabidopsis IAA17 protein as the degron and employed three tandem copies of it to enhance efficiency. To minimize undesirable side effects of the inducer, we adopted a bulky analog of auxin, 5-adamantyl-IAA, and paired it with the F-box protein OsTIR1 that harbors a mutation (F74A) at the auxin-binding pocket. 5-adamantyl-IAA, when utilized with OsTIR1-F74A, is effective at concentrations thousands of times lower than auxin used in combination with wild-type OsTIR1. We tested our improved AID system on 10 essential genes and achieved inducible lethality for all of them, including ones that could not be effectively inactivated using a previously published AID system. Our improved AID system should facilitate the construction of conditional loss-of-function mutants in fission yeast.","doi":"10.1093/g3journal/jkab393","authors":"Zhang XR, Zhao L, Suo F, Gao Y, Wu Q, Qi X, Du LL","authors_abbrev":"Zhang XR et al.","pubmed_publication_date":"04 Jan 2022","pubmed_entrez_date":"2021-12-01","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-12-03 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19119411","title":"Predicting cellular growth from gene expression signatures.","citation":"PLoS Comput Biol 2009 Jan;5(1):e1000257","abstract":"Maintaining balanced growth in a changing environment is a fundamental systems-level challenge for cellular physiology, particularly in microorganisms. While the complete set of regulatory and functional pathways supporting growth and cellular proliferation are not yet known, portions of them are well understood. In particular, cellular proliferation is governed by mechanisms that are highly conserved from unicellular to multicellular organisms, and the disruption of these processes in metazoans is a major factor in the development of cancer. In this paper, we develop statistical methodology to identify quantitative aspects of the regulatory mechanisms underlying cellular proliferation in Saccharomyces cerevisiae. We find that the expression levels of a small set of genes can be exploited to predict the instantaneous growth rate of any cellular culture with high accuracy. The predictions obtained in this fashion are robust to changing biological conditions, experimental methods, and technological platforms. The proposed model is also effective in predicting growth rates for the related yeast Saccharomyces bayanus and the highly diverged yeast Schizosaccharomyces pombe, suggesting that the underlying regulatory signature is conserved across a wide range of unicellular evolution. We investigate the biological significance of the gene expression signature that the predictions are based upon from multiple perspectives: by perturbing the regulatory network through the Ras/PKA pathway, observing strong upregulation of growth rate even in the absence of appropriate nutrients, and discovering putative transcription factor binding sites, observing enrichment in growth-correlated genes. More broadly, the proposed methodology enables biological insights about growth at an instantaneous time scale, inaccessible by direct experimental methods. Data and tools enabling others to apply our methods are available at http://function.princeton.edu/growthrate.","doi":"10.1371/journal.pcbi.1000257","authors":"Airoldi EM, Huttenhower C, Gresham D, Lu C, Caudy AA, Dunham MJ, Broach JR, Botstein D, Troyanskaya OG","authors_abbrev":"Airoldi EM et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2009-01-03","publication_year":"2009","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18629612","title":"Expression, purification, and reconstitution of the Na(+)/H (+) exchanger sod2 in Saccharomyces cerevisiae.","citation":"Mol Cell Biochem 2008 Dec;319(1-2):79-86","abstract":"Sod2, is a Na(+)/H(+) exchanger present on the cytoplasmic membrane of the fission yeast Schizosaccharomyces pombe. It expels toxic Na(+) from the cytosol. Sod2 was expressed in Saccharomyces cerevisiae with a C-terminal histidine tag under control of the GAL1 promoter. Western blots using anti-V5 antibodies identified the tagged protein. Solubilization of the protein was by n-dodecyl beta-D: -maltoside. Immobilized Ni-ion column affinity chromatography partially purified the protein at a yield of ~240 microg per liter of culture. Sod2 was present as a 40-kDa and an 80-kDa protein, however, it co-purified with a number of other proteins. Cross linking of sod2 with N,N'-(o-phenylene)dimaleimide showed that sod2 was present in association with a number of other proteins as a larger molecular weight complex. Partially purified sod2 protein was reconstituted in proteoliposomes and functionally active. Our results suggest that the sod2 protein associates with a number of other proteins and can be expressed in S. cerevisiae in active form.","doi":"10.1007/s11010-008-9879-1","authors":"Chen H, Fliegel L","authors_abbrev":"Chen H et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-07-17","publication_year":"2008","canto_session_key":"c6ca207c0a092f8e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-11-30 14:26:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-30 14:26:25","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-30"},{"uniquename":"PMID:10993721","title":"Periodic accumulation of cdc15 mRNA is not necessary for septation in Schizosaccharomyces pombe.","citation":"J Mol Biol 2000 Sep 29;302(4):751-9","abstract":"Analysis of Schizosaccharomyces pombe mutants that are defective in septum formation and cytokinesis has identified the product of the cdc15 gene as a key element in formation of a division septum. S. pombe cells lacking cdc15p function cannot assemble a functional medial ring, and do not make a division septum. cdc15 mRNA accumulates periodically during the cell cycle, peaking after entry into mitosis, and increased expression of the gene in G2-arrested cells can promote F-actin ring formation. Here, we have investigated the effects of mutations that block cell division upon the expression of cdc15 in synchronised cell populations, and analysed the expression of cdc15 when septum formation is induced by ectopic activation of the septation signalling network. We concluded the following: (i) the septation signalling network genes are not required for periodic accumulation of cdc15 mRNA; (ii) induction of septum formation in G2-arrested cells by activation of the septation signalling network does not result in accumulation of cdc15 mRNA, which is therefore not a prerequisite for septum formation; (iii) failure to turn off septum formation at the end of mitosis results in continued expression of cdc15; and (iv) periodic accumulation of cdc15 mRNA is mediated by a 97 bp region 5' to the mRNA start site.","authors":"Utzig S, Fankhauser C, Simanis V","authors_abbrev":"Utzig S et al.","pubmed_publication_date":"29 Sep 2000","pubmed_entrez_date":"2000-09-20","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14981505","title":"A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing.","citation":"Nat Struct Mol Biol 2004 Mar;11(3):275-83","abstract":"We report a novel chromatin-modulating factor, nuclear FK506-binding protein (FKBP). It is a member of the peptidyl prolyl cis-trans isomerase (PPIase) family, whose members were originally identified as enzymes that assist in the proper folding of polypeptides. The endogenous FKBP gene is required for the in vivo silencing of gene expression at the rDNA locus and FKBP has histone chaperone activity in vitro. Both of these properties depend on the N-terminal non-PPIase domain of the protein. The C-terminal PPIase domain is not essential for the histone chaperone activity in vitro, but it regulates rDNA silencing in vivo. Chromatin immunoprecipitation showed that nuclear FKBP associates with chromatin at rDNA loci in vivo. These in vivo and in vitro findings in nuclear FKBPs reveal a hitherto unsuspected link between PPIases and the alteration of chromatin structure.","authors":"Kuzuhara T, Horikoshi M","authors_abbrev":"Kuzuhara T et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-02-26","publication_year":"2004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1347.02"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:27558480","title":"A conserved role of the RSC chromatin remodeler in the establishment of nucleosome-depleted regions.","citation":"Curr Genet 2017 May;63(2):187-193","abstract":"The occupancy of nucleosomes governs access to the eukaryotic genomes and results from a combination of biophysical features and the effect of ATP-dependent remodelling complexes. Most promoter regions show a conserved pattern characterized by a nucleosome-depleted region (NDR) flanked by nucleosomal arrays. The conserved RSC remodeler was reported to be critical to establish NDR in vivo in budding yeast but other evidences suggested that this activity may not be conserved in fission yeast. By reanalysing and expanding previously published data, we propose that NDR formation requires, at least partially, RSC in both yeast species. We also discuss the most prominent biological role of RSC and the possibility that non-essential subunits do not define alternate versions of the complex.","doi":"10.1007/s00294-016-0642-y","authors":"Yague-Sanz C, Vázquez E, Sánchez M, Antequera F, Hermand D","authors_abbrev":"Yague-Sanz C et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2016-08-26","publication_year":"2017","canto_session_key":"de59b80d996a5080","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-08-27 00:15:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC10863","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19965387","title":"Phosphorylation of H2A by Bub1 prevents chromosomal instability through localizing shugoshin.","citation":"Science 2010 Jan 08;327(5962):172-7","abstract":"Bub1 is a multi-task protein kinase required for proper chromosome segregation in eukaryotes. Impairment of Bub1 in humans may lead to chromosomal instability (CIN) or tumorigenesis. Yet, the primary cellular substrate of Bub1 has remained elusive. Here, we show that Bub1 phosphorylates the conserved serine 121 of histone H2A in fission yeast Schizosaccharomyces pombe. The h2a-SA mutant, in which all cellular H2A-S121 is replaced by alanine, phenocopies the bub1 kinase-dead mutant (bub1-KD) in losing the centromeric localization of shugoshin proteins. Artificial tethering of shugoshin to centromeres largely restores the h2a-SA or bub1-KD-related CIN defects, a function that is evolutionally conserved. Thus, Bub1 kinase creates a mark for shugoshin localization and the correct partitioning of chromosomes.","doi":"10.1126/science.1180189","authors":"Kawashima SA, Yamagishi Y, Honda T, Ishiguro K, Watanabe Y","authors_abbrev":"Kawashima SA et al.","pubmed_publication_date":"08 Jan 2010","pubmed_entrez_date":"2009-12-08","publication_year":"2010","canto_session_key":"99f58cdf989ca814","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-30 17:22:35","canto_approved_date":"2026-04-20 17:36:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-30 17:22:25","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":88,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPCC1322.12c","SPCC622.08c","SPCC320.13c","SPBP35G2.03c","SPAC19G12.06c","SPCC188.02","SPBC29A10.14","SPAC15A10.15"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2018-03-30"},{"uniquename":"EMBL:AU012438","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28162934","title":"S. pombe Uba1-Ubc15 Structure Reveals a Novel Regulatory Mechanism of Ubiquitin E2 Activity.","citation":"Mol Cell 2017 Feb 16;65(4):699-714.e6","abstract":"Ubiquitin (Ub) E1 initiates the Ub conjugation cascade by activating and transferring Ub to tens of different E2s. How Ub E1 cooperates with E2s that differ substantially in their predicted E1-interacting residues is unknown. Here, we report the structure of S. pombe Uba1 in complex with Ubc15, a Ub E2 with intrinsically low E1-E2 Ub thioester transfer activity. The structure reveals a distinct Ubc15 binding mode that substantially alters the network of interactions at the E1-E2 interface compared to the only other available Ub E1-E2 structure. Structure-function analysis reveals that the intrinsically low activity of Ubc15 largely results from the presence of an acidic residue at its N-terminal region. Notably, Ub E2 N termini are serine/threonine rich in many other Ub E2s, leading us to hypothesize that phosphorylation of these sites may serve as a novel negative regulatory mechanism of Ub E2 activity, which we demonstrate biochemically and in cell-based assays.","doi":"10.1016/j.molcel.2017.01.008","authors":"Lv Z, Rickman KA, Yuan L, Williams K, Selvam SP, Woosley AN, Howe PH, Ogretmen B, Smogorzewska A, Olsen SK","authors_abbrev":"Lv Z et al.","pubmed_publication_date":"16 Feb 2017","pubmed_entrez_date":"2017-02-07","publication_year":"2017","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-08 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC10F6.05c","SPBC1105.09","SPAC18B11.07c","SPBC1604.21c","SPCC1259.15c","SPBC2D10.20","SPAC11E3.04c","SPAC1250.03","SPBC119.02","SPBC211.07c","SPBP16F5.04"],"gene_count":11,"ltp_gene_count":11,"pdb_entries":[{"pdb_id":"5knl","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A/D","position":"13-1012"},{"gene_uniquename":"SPBC1105.09","chain":"C/F","position":"1-167"}],"title":"Crystal structure of S. pombe ubiquitin E1 (Uba1) in complex with Ubc15 and ubiquitin","entry_authors":"Olsen SK,Lv Z,Yuan L,Williams K","entry_authors_abbrev":"Olsen SK et al.","reference_uniquename":"PMID:28162934","experimental_method":"X-ray","resolution":"2.5"}]},{"uniquename":"PMID:25253718","title":"csi2p modulates microtubule dynamics and organizes the bipolar spindle for chromosome segregation.","citation":"Mol Biol Cell 2014 Dec 01;25(24):3900-8","abstract":"Proper chromosome segregation is of paramount importance for proper genetic inheritance. Defects in chromosome segregation can lead to aneuploidy, which is a hallmark of cancer cells. Eukaryotic chromosome segregation is accomplished by the bipolar spindle. Additional mechanisms, such as the spindle assembly checkpoint and centromere positioning, further help to ensure complete segregation fidelity. Here we present the fission yeast csi2+. csi2p localizes to the spindle poles, where it regulates mitotic microtubule dynamics, bipolar spindle formation, and subsequent chromosome segregation. csi2 deletion (csi2Δ) results in abnormally long mitotic microtubules, high rate of transient monopolar spindles, and subsequent high rate of chromosome segregation defects. Because csi2Δ has multiple phenotypes, it enables estimates of the relative contribution of the different mechanisms to the overall chromosome segregation process. Centromere positioning, microtubule dynamics, and bipolar spindle formation can all contribute to chromosome segregation. However, the major determinant of chromosome segregation defects in fission yeast may be microtubule dynamic defects.","doi":"10.1091/mbc.E14-09-1370","authors":"Costa J, Fu C, Khare VM, Tran PT","authors_abbrev":"Costa J et al.","pubmed_publication_date":"01 Dec 2014","pubmed_entrez_date":"2014-09-26","publication_year":"2014","canto_session_key":"79d476e92beb688e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-06 22:32:27","canto_approved_date":"2022-11-08 17:52:34","canto_session_submitted_date":"2015-05-29 12:34:40","canto_added_date":"2014-09-27 00:16:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.01","SPAC4D7.07c","SPBC12D12.01","SPAC25G10.07c","SPBC2G2.14","SPBC20F10.06","SPAC23H3.08c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-02-06"},{"uniquename":"PMID:28682306","title":"Unique roles for histone H3K9me states in RNAi and heritable silencing of transcription.","citation":"Nature 2017 Jul 27;547(7664):463-467","abstract":"Heterochromatic DNA domains have important roles in the regulation of gene expression and maintenance of genome stability by silencing repetitive DNA elements and transposons. From fission yeast to mammals, heterochromatin assembly at DNA repeats involves the activity of small noncoding RNAs (sRNAs) associated with the RNA interference (RNAi) pathway. Typically, sRNAs, originating from long noncoding RNAs, guide Argonaute-containing effector complexes to complementary nascent RNAs to initiate histone H3 lysine 9 di- and trimethylation (H3K9me2 and H3K9me3, respectively) and the formation of heterochromatin. H3K9me is in turn required for the recruitment of RNAi to chromatin to promote the amplification of sRNA. Yet, how heterochromatin formation, which silences transcription, can proceed by a co-transcriptional mechanism that also promotes sRNA generation remains paradoxical. Here, using Clr4, the fission yeast Schizosaccharomyces pombe homologue of mammalian SUV39H H3K9 methyltransferases, we design active-site mutations that block H3K9me3, but allow H3K9me2 catalysis. We show that H3K9me2 defines a functionally distinct heterochromatin state that is sufficient for RNAi-dependent co-transcriptional gene silencing at pericentromeric DNA repeats. Unlike H3K9me3 domains, which are transcriptionally silent, H3K9me2 domains are transcriptionally active, contain modifications associated with euchromatic transcription, and couple RNAi-mediated transcript degradation to the establishment of H3K9me domains. The two H3K9me states recruit reader proteins with different efficiencies, explaining their different downstream silencing functions. Furthermore, the transition from H3K9me2 to H3K9me3 is required for RNAi-independent epigenetic inheritance of H3K9me domains. Our findings demonstrate that H3K9me2 and H3K9me3 define functionally distinct chromatin states and uncover a mechanism for the formation of transcriptionally permissive heterochromatin that is compatible with its broadly conserved role in sRNA-mediated genome defence.","doi":"10.1038/nature23267","authors":"Jih G, Iglesias N, Currie MA, Bhanu NV, Paulo JA, Gygi SP, Garcia BA, Moazed D","authors_abbrev":"Jih G et al.","pubmed_publication_date":"27 Jul 2017","pubmed_entrez_date":"2017-07-07","publication_year":"2017","canto_session_key":"85dd491c95da2708","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2026-01-19 09:36:08","canto_approved_date":"2026-01-19 09:36:08","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-10-23 15:43:51","canto_added_date":"2017-07-08 00:15:16","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":36,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.02c","SPAC664.01c","SPBC428.08c","SPCC736.11","SPBC16C6.10","SPBC800.03"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2026-01-19"},{"uniquename":"PMID:17092950","title":"Inhibitory activity of 1-farnesylpyridinium on the spatial control over the assembly of cell wall polysaccharides in Schizosaccharomyces pombe.","citation":"J Biochem 2006 Dec;140(6):851-9","abstract":"The modes of actions of 1-farnesylpyridinium (FPy) on yeast cell growth were investigated on the basis of its effects on cell cycle progression, morphogenesis and the related events for construction of cell wall architecture in Schizosacchromyces pombe. FPy predominantly inhibited the growth of the yeast cells after various cycles of cell division so that cells were arrested at the phase of separation into daughter cells accompanying morphological changes to swollen spherical cells at 24 h of incubation. FPy-treated cells were osmotically stable but were susceptible to the lytic action of (1, 3) beta-D-glucanases, and characterized by serious damages to the cell wall architecture as represented by a rough and irregular surface outlook. The isolated cell wall fraction gave a similar hexose composition with or without FPy treatment, suggesting that FPy did not inhibit the synthesis of each cell wall polysaccharide. FPy was permissive for the extracellular accumulation of amorphous cell wall materials and septum development in protoplasts, but absolutely interfered with the following morphogenetic process for construction of the rod-shaped cell wall architecture. Our results suggest the inhibitory activity of FPy on the spatial control over the assembly of cell wall polysaccharides.","authors":"Hamada M, Ohata I, Fujita K, Usuki Y, Ogita A, Ishiguro J, Tanaka T","authors_abbrev":"Hamada M et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-11-10","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8165291","title":"[Meiotic genes in fission yeast].","citation":"Tanpakushitsu Kakusan Koso 1994 Mar;39(4):458-66","abstract":"","authors":"Shimoda C","authors_abbrev":"Shimoda C","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3329975","title":"Genetic nomenclature and gene list of the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1987;11(8):575-89","abstract":"The nomenclature rules for the genetics of the fission yeast Schizosaccharomyces pombe have been fixed for the first time, after discussion among scientists working with this organism. Conventions are proposed for the naming of genes and alleles that are obtained by classical means or by reverse genetics. In addition a list has been compiled of 460 known genes of S. pombe. It includes genes defined both by classical mutation analysis and by molecular cloning. 270 genes have been assigned either to one of the three nuclear chromosomes or the mitochondrial genome.","authors":"Kohli J","authors_abbrev":"Kohli J","pubmed_publication_date":"1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25724335","title":"Essential function of Aco2, a fusion protein of aconitase and mitochondrial ribosomal protein bL21, in mitochondrial translation in fission yeast.","citation":"FEBS Lett 2015 Mar 24;589(7):822-8","abstract":"A possible interaction between aconitase and a mitochondrial ribosomal protein was suggested in a genome-wide interactome study. In fission yeast Schizosaccharomyces pombe, the aco2(+) gene encodes a fusion protein between aconitase and a putative mitochondrial ribosomal protein bL21 (Mrpl49). Two types of aco2(+) transcripts are generated via alternative poly (A) site selection, producing both a single aconitase domain protein and the fusion form. The bL21-fused Aco2 protein resides in mitochondria as well as in the cytosol and the nucleus. The viability defect of aco2 mutation is complemented not by the aconitase domain but by the bL21 domain, which enables mitochondrial translation.","doi":"10.1016/j.febslet.2015.02.015","authors":"Jung SJ, Seo Y, Lee KC, Lee D, Roe JH","authors_abbrev":"Jung SJ et al.","pubmed_publication_date":"24 Mar 2015","pubmed_entrez_date":"2015-03-01","publication_year":"2015","canto_session_key":"3ae02f9ef40a096c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-11-22 13:27:07","canto_approved_date":"2024-10-15 07:18:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-10-14 15:54:30","canto_added_date":"2015-03-02 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H8.03","SPAC24C9.06c","SPBP4H10.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-11-22"},{"uniquename":"PMID:26058898","title":"Telomere protein Rap1 is a charge resistant scaffolding protein in chromosomal bouquet formation.","citation":"BMC Biol 2015 Jun 10;13:37","abstract":"Chromosomes reorganize in early meiotic prophase to form the so-called telomere bouquet. In fission yeast, telomeres localize to the nuclear periphery via interaction of the telomeric protein Rap1 with the membrane protein Bqt4. During meiotic prophase, the meiotic proteins Bqt1-2 bind Rap1 and tether to the spindle pole body to form the bouquet. Although it is known that this polarized chromosomal arrangement plays a crucial role in meiotic progression, the molecular mechanisms of telomere bouquet regulation are poorly understood.\nHere, we detected high levels of Rap1 phospho-modification throughout meiotic prophase, and identified a maximum of 35 phosphorylation sites. Concomitant phosphomimetic mutation of the modification sites suggests that Rap1 hyper-phosphorylation does not directly regulate telomere bouquet formation or dissociation. Despite the negative charge conferred by its highly phosphorylated state, Rap1 maintains interactions with its binding partners. Interestingly, mutations that change the charge of negatively charged residues within the Bqt1-2 binding site of Rap1 abolished the affinity to the Bqt1-2 complex, suggesting that the intrinsic negative charge of Rap1 is crucial for telomere bouquet formation.\nWhereas Rap1 hyper-phosphorylation observed in meiotic prophase does not have an apparent role in bouquet formation, the intrinsic negative charge of Rap1 is important for forming interactions with its binding partners. Thus, Rap1 is able to retain bouquet formation under heavily phosphorylated status.","doi":"10.1186/s12915-015-0149-x","authors":"Amelina H, Subramaniam S, Moiseeva V, Armstrong CA, Pearson SR, Tomita K","authors_abbrev":"Amelina H et al.","pubmed_publication_date":"10 Jun 2015","pubmed_entrez_date":"2015-06-11","publication_year":"2015","canto_session_key":"825471d01f967516","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kazunori Tomita","canto_approved_date":"2015-08-20 10:29:38","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-08-17 09:49:25","canto_added_date":"2015-06-12 00:20:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":45,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kazunori Tomita","community_curator":true,"annotation_count":3,"orcid":"0000-0003-1096-6725","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.02","SPAC6G9.13c","SPBC19C7.10","SPAC19G12.13c","SPAC1002.06c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-08-17"},{"uniquename":"EMBL:SPD240","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12063243","title":"Distinct roles for glutathione S-transferases in the oxidative stress response in Schizosaccharomyces pombe.","citation":"J Biol Chem 2002 Sep 20;277(38):35523-31","abstract":"We have identified three genes, gst1(+), gst2(+), and gst3(+), encoding theta-class glutathione S-transferases (GSTs) in Schizosaccharomyces pombe. The gst1(+) and gst2(+) genes encode closely related proteins (79% identical). Our analysis suggests that Gst1, Gst2, and Gst3 all have GST activity with the substrate 1-chloro-2,4-dinitrobenzene and that Gst3 has glutathione peroxidase activity. Although Gst1 and Gst2 have no detectable peroxidase activity, all three gst genes are required for normal cellular resistance to peroxides. In contrast, each mutant is more resistant to diamide than wild-type cells. The gst1Delta, gst2Delta, and gst3Delta mutants are also more sensitive to fluconazole, suggesting that GSTs may be involved in anti-fungal drug detoxification. Both gst2(+) and gst3(+) mRNA levels increase in stationary phase, and all three gst genes are induced by hydrogen peroxide. Indeed, gst1(+), gst2(+), and gst3(+) are regulated by the stress-activated protein kinase Sty1. The Gst1 and Gst2 proteins are distributed throughout the cell and can form homodimers and Gst1-Gst2 heterodimers. In contrast, Gst3 is excluded from the nucleus and forms homodimers but not complexes with either Gst1 or Gst2. Collectively, our data suggest that GSTs have separate and overlapping roles in oxidative stress and drug responses in fission yeast.","authors":"Veal EA, Toone WM, Jones N, Morgan BA","authors_abbrev":"Veal EA et al.","pubmed_publication_date":"20 Sep 2002","pubmed_entrez_date":"2002-06-14","publication_year":"2002","canto_session_key":"9228d905707e8ee3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-02 17:25:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-26 08:27:48","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":39,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPCC191.09c","SPAC24B11.06c","SPAC688.04c","SPAC1783.07c","SPCC965.07c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-11-26"},{"uniquename":"PMID:23499261","title":"In vivo self-assembly of TMV-like particles in yeast and bacteria for nanotechnological applications.","citation":"J Virol Methods 2013 May;189(2):328-40","abstract":"Heterologous expression of tobacco mosaic virus coat protein and in vivo assembly of rod-shaped TMV-like particles encapsidating viral or host RNA were compared between Escherichia coli and Schizosaccharomyces pombe. TMV-like particles were produced in both hosts, irrespective of whether the TMV origin of assembly was present. The additional plasmid providing an OAS-containing RNA was able to alter the length distribution of the TMV-like particles. Plant and yeast-expressed CP behaved similarly upon isoelectric focusing, whereas CP expressed in bacteria migrated differently. After purification by buoyant density centrifugation, the encapsidated nucleic acids were determined to be of host origin as well as of viral origin. OAS-containing mRNA was packaged preferentially in yeast to some extent (8%). In consequence, the majority of TMV-like particles showed the same length distribution similar to those in the absence of OAS-containing mRNA, likely due to host RNA being primarily encapsidated. Notwithstanding this limitation for tailoring particle sizes, the heterologous expression system provides a new avenue to deliver versatile nucleoprotein scaffolds for a diversity of nanotechnological applications, without the need for an infectious virus. The results are discussed with reference to the competition of translation and packaging as well as to the selective decay of TMV RNA.","doi":"10.1016/j.jviromet.2013.02.017","authors":"Kadri A, Wege C, Jeske H","authors_abbrev":"Kadri A et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-03-19","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19543678","title":"Polycystic kidney disease channel and synaptotagmin homologues play roles in schizosaccharomyces pombe cell wall synthesis/repair and membrane protein trafficking.","citation":"J Membr Biol 2009 Jun;229(3):141-52","abstract":"Eukaryotic cells can sense a wide variety of environmental stresses, including changes in temperature, pH, osmolarity and nutrient availability. They respond to these changes through a variety of signal-transduction mechanisms, including activation of Ca(2+)-dependent signaling pathways. This research has discovered important implications in the function(s) of polycystic kidney disease (PKD) channels and the mechanisms through which they act in the control of cell growth and cell polarity in Schizosaccharomyces pombe by ion channel-mediated Ca(2+) signaling. Pkd2 was expressed maximally during the exponential growth phase. At the cell surface pkd2 was localized at the cell tip during the G(2) phase of the cell cycle, although following cell wall damage, the cell surface-expressed protein relocalized to the whole plasma membrane. Pkd2 depletion affected Golgi trafficking, resulting in a buildup of vesicles at the cell poles, and strongly affected plasma membrane protein delivery. Surface-localized pkd2 was present in the plasma membrane for a very short time and was rapidly internalized. Internalization was dependent on Ca(2+), enhanced by amphipaths and inhibited by gadolinium. The pkd2 protein was in a complex with a yeast synaptotagmin homologue and myosin V. Depletion of pkd2 severely affected the localization of glucan synthase. A role for pkd2 in a cell polarity and cell wall synthesis signaling complex with a synaptotagmin homologue, myosin V and glucan synthase is proposed.","doi":"10.1007/s00232-009-9180-6","authors":"Aydar E, Palmer CP","authors_abbrev":"Aydar E et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-06-23","publication_year":"2009","canto_session_key":"b595ffbb38089b55","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-05-17 12:57:39","canto_approved_date":"2019-05-17 12:57:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-16 12:45:11","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPYUK71.03c","SPCC1919.10c","SPBC1652.02","SPAC1F7.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-05-17"},{"uniquename":"PMID:26652183","title":"Coordination of DNA damage tolerance mechanisms with cell cycle progression in fission yeast.","citation":"Cell Cycle 2016;15(2):261-73","abstract":"DNA damage tolerance (DDT) mechanisms allow cells to synthesize a new DNA strand when the template is damaged. Many mutations resulting from DNA damage in eukaryotes are generated during DDT when cells use the mutagenic translesion polymerases, Rev1 and Polζ, rather than mechanisms with higher fidelity. The coordination among DDT mechanisms is not well understood. We used live-cell imaging to study the function of DDT mechanisms throughout the cell cycle of the fission yeast Schizosaccharomyces pombe. We report that checkpoint-dependent mitotic delay provides a cellular mechanism to ensure the completion of high fidelity DDT, largely by homology-directed repair (HDR). DDT by mutagenic polymerases is suppressed during the checkpoint delay by a mechanism dependent on Rad51 recombinase. When cells pass the G2/M checkpoint and can no longer delay mitosis, they completely lose the capacity for HDR and simultaneously exhibit a requirement for Rev1 and Polζ. Thus, DDT is coordinated with the checkpoint response so that the activity of mutagenic polymerases is confined to a vulnerable period of the cell cycle when checkpoint delay and HDR are not possible.","doi":"10.1080/15384101.2015.1121353","authors":"Callegari AJ, Kelly TJ","authors_abbrev":"Callegari AJ et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-12-15","publication_year":"2016","canto_session_key":"40950ae0da782908","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"a. john callegari","canto_first_approved_date":"2016-09-05 08:43:56","canto_approved_date":"2021-11-04 13:52:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-18 15:41:47","canto_added_date":"2015-12-16 01:19:29","annotation_curators":[{"name":"a. john callegari","community_curator":true,"annotation_count":26,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13C5.07","SPBC1347.01c","SPAC13G6.01c","SPBC16A3.11","SPBC1734.06","SPBC19C7.09c","SPBC649.03","SPAC688.10","SPAC644.14c","SPCC1259.13"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2016-09-05"},{"uniquename":"PMID:12399374","title":"The 2.1-kb inverted repeat DNA sequences flank the mat2,3 silent region in two species of Schizosaccharomyces and are involved in epigenetic silencing in Schizosaccharomyces pombe.","citation":"Genetics 2002 Oct;162(2):591-602","abstract":"The mat2,3 region of the fission yeast Schizosaccharomyces pombe exhibits a phenomenon of transcriptional silencing. This region is flanked by two identical DNA sequence elements, 2.1 kb in length, present in inverted orientation: IRL on the left and IRR on the right of the silent region. The repeats do not encode any ORF. The inverted repeat DNA region is also present in a newly identified related species, which we named S. kambucha. Interestingly, the left and right repeats share perfect identity within a species, but show approximately 2% bases interspecies variation. Deletion of IRL results in variegated expression of markers inserted in the silent region, while deletion of the IRR causes their derepression. When deletions of these repeats were genetically combined with mutations in different trans-acting genes previously shown to cause a partial defect in silencing, only mutations in clr1 and clr3 showed additive defects in silencing with the deletion of IRL. The rate of mat1 switching is also affected by deletion of repeats. The IRL or IRR deletion did not cause significant derepression of the mat2 or mat3 loci. These results implicate repeats for maintaining full repression of the mat2,3 region, for efficient mat1 switching, and further support the notion that multiple pathways cooperate to silence the mat2,3 domain.","authors":"Singh G, Klar AJ","authors_abbrev":"Singh G et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-10-26","publication_year":"2002","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31835586","title":"Greatwall-Endosulfine: A Molecular Switch that Regulates PP2A/B55 Protein Phosphatase Activity in Dividing and Quiescent Cells.","citation":"Int J Mol Sci 2019 Dec 10;20(24)","abstract":"During the cell cycle, hundreds of proteins become phosphorylated and dephosphorylated, indicating that protein kinases and protein phosphatases play a central role in its regulation. It has been widely recognized that oscillation in cyclin-dependent kinase (CDK) activity promotes DNA replication, during S-phase, and chromosome segregation, during mitosis. Each CDK substrate phosphorylation status is defined by the balance between CDKs and CDK-counteracting phosphatases. In fission yeast and animal cells, PP2A/B55 is the main protein phosphatase that counteracts CDK activity. PP2A/B55 plays a key role in mitotic entry and mitotic exit, and it is regulated by the Greatwall-Endosulfine (ENSA) molecular switch that inactivates PP2A/B55 at the onset of mitosis, allowing maximal CDK activity at metaphase. The Greatwall-ENSA-PP2A/B55 pathway is highly conserved from yeast to animal cells. In yeasts, Greatwall is negatively regulated by nutrients through TORC1 and S6 kinase, and couples cell growth, regulated by TORC1, to cell cycle progression, driven by CDK activity. In animal cells, Greatwall is phosphorylated and activated by Cdk1 at G2/M, generating a bistable molecular switch that results in full activation of Cdk1/CyclinB. Here we review the current knowledge of the Greatwall-ENSA-PP2A/B55 pathway and discuss its role in cell cycle progression and as an integrator of nutritional cues.","doi":"10.3390/ijms20246228","authors":"García-Blanco N, Vázquez-Bolado A, Moreno S","authors_abbrev":"García-Blanco N et al.","pubmed_publication_date":"10 Dec 2019","pubmed_entrez_date":"2019-12-15","publication_year":"2019","canto_session_key":"7324575552297784","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1597466","title":"Post-translational processing of Schizosaccharomyces pombe YPT proteins.","citation":"J Biol Chem 1992 Jun 05;267(16):11329-36","abstract":"ras proteins are post-translationally processed at their carboxyl-terminal CAAX motif by a triplet of modifications: prenylation of C with farnesyl, proteolytic trimming of AAX, and carboxyl-methylation. These modifications co-operate with palmitoylation of nearby sites or a polybasic region to target plasma membrane localization. The related YPT/rab proteins in contrast are localized to compartments of the endo-membrane system and may be involved in directing membrane traffic. These proteins end in XCC or CXC motifs. We have analyzed the processing of members of this subfamily form the fission yeast Schizosaccharomyces pombe. We find using in vitro translation in reticulocyte lysates that YPT1, -3, and -5 are prenylated with geranylgeranyl and that they incorporate label from [3H]mevalonic acid when expressed in transfected COS cells in vivo. Furthermore, prenylation was necessary for membrane binding in vivo. The CXC protein YPT5, but neither of the two XCC proteins YPT1 and YPT3, was carboxyl-methylated in S. pombe and in COS cells in vivo. However, YPT5 was not carboxyl-methylated in vitro in lysates which were able to methylate ras protein. YPT3 was detectably palmitoylated when expressed in COS cells, though at a much lower level than ras.","authors":"Newman CM, Giannakouros T, Hancock JF, Fawell EH, Armstrong J, Magee AI","authors_abbrev":"Newman CM et al.","pubmed_publication_date":"05 Jun 1992","pubmed_entrez_date":"1992-06-05","publication_year":"1992","canto_session_key":"d4d976e3056b1065","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-09 11:36:04","canto_approved_date":"2022-08-30 07:58:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-17 15:32:12","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.03","SPBC1703.10","SPAC6F6.15"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-02-09"},{"uniquename":"PMID:34458867","title":"Analysis of local protein accumulation kinetics by live-cell imaging in yeast systems.","citation":"STAR Protoc 2021 Sep 17;2(3):100733","abstract":"Microscopy-based analysis of protein accumulation at a given subcellular location in real time provides invaluable insights into the function of a protein in a specific process. Here, we describe a detailed protocol for determining protein accumulation kinetics at the division site in the budding yeast  Saccharomyces cerevisiae  and fission yeast  Schizosaccharomyces pombe . This protocol can be adapted for the analysis of any protein involved in any process as long as the protein is localized to a discrete region of the cell. For complete details on the use and execution of this protocol, please refer to Okada et al. (2021) and Okada et al. (2019).","doi":"10.1016/j.xpro.2021.100733","authors":"Okada H, MacTaggart B, Bi E","authors_abbrev":"Okada H et al.","pubmed_publication_date":"17 Sep 2021","pubmed_entrez_date":"2021-08-30","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-09-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3402730","title":"Genetic and physical analysis of the M26 recombination hotspot of Schizosaccharomyces pombe.","citation":"Genetics 1988 Jul;119(3):491-7","abstract":"The ade6-M26 mutation of Schizosaccharomyces pombe has previously been reported to stimulate ade6 intragenic meiotic recombination. We report here that the ade6-M26 mutation is a single G----T nucleotide change, that M26 stimulated recombination within ade6 but not at other distinct loci, and that M26 stimulated meiotic but not mitotic recombination. In addition, M26 stimulated recombination within ade6 when M26 is homozygous; this result demonstrates that a base-pair mismatch at the M26 site was not required for the stimulation. These results are consistent with the ade6-M26 mutation creating a meiotic recombination initiation site.","authors":"Ponticelli AS, Sena EP, Smith GR","authors_abbrev":"Ponticelli AS et al.","pubmed_publication_date":"Jul 1988","pubmed_entrez_date":"1988-07-01","publication_year":"1988","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009770","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10329185","title":"Influence of a replication enhancer on the hierarchy of origin efficiencies within a cluster of DNA replication origins.","citation":"J Mol Biol 1999 May 21;288(5):867-82","abstract":"DNA replication origins in animal cells sometimes occur in clusters. Often one of the multiple origins within these clusters fires more frequently than the others. The reason for this hierarchy remains unknown. Similar origin clusters occur in the fission yeast, Schizosaccharomyces pombe. One such cluster is located near the ura4 gene on chromosome III and contains three origins: ars3002, ars3003, and ars3004. In their natural chromosomal context (ars3003 is about 2.5 kb upstream of ars3002 and ars3004 is adjacent to ars3002 on the downstream side) their initiation frequencies display a striking hierarchy: ars3002 >> ars3003 >> ars3004. Here, we describe experiments that reveal a 400 bp replication enhancer within ars3004, adjacent to ars3002. The enhancer is essential for ars3004 origin function in a plasmid, but even with the enhancer ars3004 is an inefficient origin. The enhancer is not essential for ars3002 plasmid origin activity, but dramatically stimulates this activity, converting ars3002 from an inefficient plasmid origin to a very efficient one. It also stimulates the plasmid origin activity of ars3001 and ars3003 at all tested positions and orientations on both sides of each autonomously replicating sequence (ARS) element. If ars3002 is redefined to include the enhancer, then the relative activities of the three ARS elements as single origins within separate plasmids or as origins when all three ARS elements are present in a single plasmid is the same as the chromosomal hierarchy. Thus, this replication enhancer defines the relative activities of the three origins in the ura4 origin region. Similar enhancers may affect relative activities in the origin clusters of animal cells.","authors":"Kim SM, Huberman JA","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"21 May 1999","pubmed_entrez_date":"1999-05-18","publication_year":"1999","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11387218","title":"A role for DNA polymerase alpha in epigenetic control of transcriptional silencing in fission yeast.","citation":"EMBO J 2001 Jun 01;20(11):2857-66","abstract":"In the fission yeast Schizosaccharomyces pombe, transcriptional silencing at the mating-type region, centromeres and telomeres is epigenetically controlled, and results from the assembly of higher order chromatin structures. Chromatin proteins associated with these silenced loci are believed to serve as molecular bookmarks that help promote inheritance of the silenced state during cell division. Specifically, a chromodomain protein Swi6 is believed to be an important determinant of the epigenetic imprint. Here, we show that a mutation in DNA polymerase alpha (pol(alpha)) affects Swi6 localization at the mating-type region and causes a 45-fold increase in spontaneous transition from the silenced epigenetic state to the expressed state. We also demonstrate that pol(alpha) mutant cells are defective in Swi6 localization at centromeres and telomeres. Genetic analysis suggests that Polalpha and Swi6 are part of the same silencing pathway. Interestingly, we found that Swi6 directly binds to Pol(alpha) in vitro. Moreover, silencing-defective mutant Pol(alpha) displays reduced binding to Swi6 protein. This work indicates involvement of a DNA replication protein, Pol(alpha), in heterochromatin assembly and inheritance of epigenetic chromatin structures.","authors":"Nakayama Ji, Allshire RC, Klar AJ, Grewal SI","authors_abbrev":"Nakayama Ji et al.","pubmed_publication_date":"01 Jun 2001","pubmed_entrez_date":"2001-06-02","publication_year":"2001","canto_session_key":"5fe213e9b923b10e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-06-01 15:12:00","canto_approved_date":"2025-09-04 11:01:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-13 16:02:38","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c","SPAC664.01c","SPBC30D10.04","SPBC216.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-06-01"},{"uniquename":"PMID:10469572","title":"Movement of a cytokinesis factor cdc12p to the site of cell division.","citation":"Curr Biol 1999 Jul 29;9(15):849-52","abstract":"A key question in cytokinesis is how the plane of cell division is positioned within the cell. Although a number of cytokinesis factors involved in formation of the actomyosin contractile ring have been identified, little is known about how these factors are localized and assembled at the cell-division site. Cells of the fission yeast Schizosaccharomyces pombe divide using a medial actomyosin ring that assembles in early mitosis [1]. The S. pombe cdc12 gene encodes a formin, a member of a family of proteins that have functions in cytokinesis and cell polarity and that may bind Rho/Cdc42 GTPases, profilin and other actin-associated proteins [1] [2] [3] [4]. The cdc12 protein (cdc12p) is required specifically for medial-ring assembly during cytokinesis and is a component of this ring [2] [5]. In this study, cdc12p was found, during interphase, in a discrete, motile cytoplasmic spot that moved to the future site of cell division at the onset of mitosis. Three lines of evidence indicated that this cdc12p spot moved on both actin and microtubule networks: movement required either actin or microtubules; the spot was associated with actin and microtubule structures; and individual spots were seen to move along both microtubule and non-microtubule tracks. These findings demonstrate that a cytokinesis factor may travel on both microtubule and actin networks to the future site of cell division.","authors":"Chang F","authors_abbrev":"Chang F","pubmed_publication_date":"29 Jul 1999","pubmed_entrez_date":"1999-09-02","publication_year":"1999","canto_session_key":"cddfc909486fc517","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-02-22 21:52:24","canto_approved_date":"2019-02-22 21:52:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-02-22 21:52:16","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-02-22"},{"uniquename":"PMID:16408318","title":"Spsgt1, a new essential gene of Schizosaccharomyces pombe, is involved in carbohydrate metabolism.","citation":"Yeast 2006 Jan 15;23(1):35-53","abstract":"hSGT1 (human suppressor of Gcr two) was isolated as a suppressor gene of the gcr2 mutation. Since Gcr2p is a key regulatory factor of glycolytic gene expression in Saccharomyces cerevisiae, hSGT1 is a candidate for a novel human transcription factor involved in carbohydrate metabolism. SGT1 appears to be conserved from Schizosaccharomyces pombe to human but not present in S. cerevisiae. To further study its function, we cloned the hSgt1p orthologue of Sz. pombe (Spsgt1) from Sz. pombe genomic DNA. Overall identity and similarity between SpSgt1p and hSgt1p are 24% and 37%, respectively. Disruption of Spsgt1 showed that Spsgt1 is essential for growth and, using a construct which conditionally expresses sgt1, which with low level expression growth was severely affected on glucose but normal on non-fermentable carbon sources. DNA microarray analyses showed that the transcription of many genes involved in carbohydrate metabolism and amino acid metabolism were upregulated in the mutant, suggesting that SpSgt1p may be involved in the regulation of carbohydrate metabolism. Furthermore, a GFP fusion of SpSgt1p was localized to the nucleus, fitting with the possibility of SpSgt1p as a transcription factor.","authors":"Kainou T, Shinzato T, Sasaki K, Mitsui Y, Giga-Hama Y, Kumagai H, Uemura H","authors_abbrev":"Kainou T et al.","pubmed_publication_date":"15 Jan 2006","pubmed_entrez_date":"2006-01-13","publication_year":"2006","canto_session_key":"f1af739513d48754","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-28 14:13:58","canto_approved_date":"2021-10-04 15:13:22","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-10-04 15:13:12","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1002.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-01-28"},{"uniquename":"PMID:12242294","title":"The mal2p protein is an essential component of the fission yeast centromere.","citation":"Mol Cell Biol 2002 Oct;22(20):7168-83","abstract":"Precise segregation of chromosomes requires the activity of a specialized chromatin region, the centromere, that assembles the kinetochore complex to mediate the association with spindle microtubules. We show here that Mal2p, previously identified as a protein required for genome stability, is an essential component of the fission yeast centromere. Loss of functional Mal2p leads to extreme missegregation of chromosomes due to nondisjunction of sister chromatids and results in inviable cells. Mal2p associates specifically with the central region of the complex fission yeast centromere, where it is required for the specialized chromatin architecture as well as for transcriptional silencing of this region. Genetic evidence indicates that mal2(+) interacts with mis12(+), encoding another component of the inner centromere core complex. In addition, Mal2p is required for correct metaphase spindle length. Our data imply that the Mal2p protein is required to build up a functional fission yeast centromere.","authors":"Jin QW, Pidoux AL, Decker C, Allshire RC, Fleig U","authors_abbrev":"Jin QW et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-09-21","publication_year":"2002","canto_session_key":"c6538160af902d62","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-04-12 08:10:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-02 10:26:54","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.09","SPAC25B8.14","SPAC18G6.15","SPCC895.07","SPAC6F12.15c","SPBC20F10.06","SPBC106.01","SPBC409.04c","SPCC736.14"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2016-03-02"},{"uniquename":"EMBL:AB084863","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.51"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11683500","title":"Bob1, a Gim5/MM-1/Pfd5 homolog, interacts with the MAP kinase kinase Byr1 to regulate sexual differentiation in the fission yeast, Schizosaccharomyces pombe.","citation":"Differentiation 2001 Jun;67(4-5):98-106","abstract":"The MAPKK Byr1 is an essential component of a Ras-dependent MAPK module required for sexual differentiation in the fission yeast, Schizosaccharomyces pombe. Here we describe the genetic and molecular characterization of a highly conserved protein, Bob1, which was identified from a two-hybrid screen for Byr1-interacting proteins. Byrl and Bobl proteins coprecipitate from S. pombe cell lysates, and both proteins localize to the tips and septa of S. pombe cells. S. pombe bob1 null (bob1delta) mutants lack obvious growth defects but exhibit a significant mating deficiency, which can be suppressed by overexpression of Byrl. Overexpression of Bob1 also leads to inhibition of mating in S. pombe, and this defect is likewise suppressed by Byrl overexpression. Bob1 is highly homologous in structure to the mammalian MM-1/Pfd5 and budding yeast Gim5/Pfd5-Sc proteins, which have been implicated as regulators of actin and tubulins. Similar to budding yeast gim5/pfd5-Sc mutants, S. pombe bob1delta cells have cytoskeletal defects, as judged by hypersensitivity to cytoskeletal disrupting drugs. byr1delta mutants do not share this characteristic with bob1delta mutants, and byr1delta bob1delta mutants are not significantly more sensitive to cytoskeletal disrupting drugs than cells carrying only the bob1delta mutation. Taken together, our results suggest that Bob1 has Byr1-related function(s) required for proper mating response of S. pombe cells and Byrl-independent function(s) required for normal cytoskeletal control. We show that the human MM-1/Pfd5 protein can substitute for its counterpart in fission yeast, providing evidence that the functions of Bob1-related proteins have been highly conserved through evolution. Our results lead us to propose that Bob1-related proteins may play diverse roles in eukaryotic organisms.","authors":"Henkel J, Du H, Yang P, Qyang Y, Kansra S, Ko M, Kim HW, Marcus S","authors_abbrev":"Henkel J et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-10-31","publication_year":"2001","canto_session_key":"9a84ff9ab5f5d661","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-28 23:00:42","canto_approved_date":"2021-01-28 16:24:08","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-20 09:04:03","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.13","SPAC31G5.09c","SPBC215.02"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2018-04-28"},{"uniquename":"PMID:12653111","title":"Thiamin regulates agglutination and zygote formation in Schizosaccharomyces pombe.","citation":"Curr Genet 1990 Mar;17(3):191-4","abstract":"Nutritional conditions regulate mating of the fission yeast S. pombe. To investigate how nutritional signals are monitored by the cell and translated into appropriate mating behaviour, effects of unique and specific growth factors would be desirable. We show that thiamin can inhibit sexual agglutination and zygote formation in S. pombe. A concentration of 50 nM thiamin in the culture medium is required for full growth of a thiamin auxotrophic strain. At this concentration thiamin starts to inhibit mating of wild-type cells of opposite heterothallic mating type and at a 1 microM concentration zygote formation is inhibited by more than 95%. Growth conditions modulate the inhibitory effect of thiamin. Thiamin acts only for a restricted period of time and seems to inhibit commitment to zygote formation rather than the cell aggregation and fusion process itself. Pyrithiamin, a thiamin antagonist, inhibits growth as well as mating.","authors":"Schweingruber ME, Edenharter E","authors_abbrev":"Schweingruber ME et al.","pubmed_publication_date":"Mar 1990","pubmed_entrez_date":"1990-03-01","publication_year":"1990","canto_session_key":"7f4c3278d6ecc195","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-05-23 15:48:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-23 08:03:11","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1486.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-05-23"},{"uniquename":"PMID:16603158","title":"The fission yeast stress MAPK cascade regulates the pmp3+ gene that encodes a highly conserved plasma membrane protein.","citation":"FEBS Lett 2006 May 01;580(10):2409-13","abstract":"In eukaryotic organisms, stress-activated mitogen-activated protein kinases (MAPK) play crucial roles in transmitting environmental signals to regulate gene expression for cellular stress adaptation. Here we report that, in the fission yeast Schizosaccharomyces pombe, Spc1/Sty1 MAPK and the Atf1 transcription factor regulate the stress-induced expression of Pmp3, a ubiquitous small membrane protein implicated in the modulation of the plasma membrane potential. The pmp3 null mutant, as well as the spc1 and atf1 mutants, is hypersensitive to the cationic antibiotic hygromycin B. Transcriptional regulation of the Pmp3-like genes by the stress-activated MAPK may also be conserved in other eukaryotes, including plants.","authors":"Wang LY, Shiozaki K","authors_abbrev":"Wang LY et al.","pubmed_publication_date":"01 May 2006","pubmed_entrez_date":"2006-04-11","publication_year":"2006","canto_session_key":"0e871df11c506380","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-07-31 09:39:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-18 15:22:33","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC29B5.01","SPCC1183.09c","SPBC713.11c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-08-18"},{"uniquename":"PMID:36749320","title":"Multiple polarity kinases inhibit phase separation of F-BAR protein Cdc15 and antagonize cytokinetic ring assembly in fission yeast.","citation":"Elife 2023 Feb 07;12","abstract":"The F-BAR protein Cdc15 is essential for cytokinesis in  Schizosaccharomyces pombe  and plays a key role in attaching the cytokinetic ring (CR) to the plasma membrane (PM). Cdc15's abilities to bind to the membrane and oligomerize via its F-BAR domain are inhibited by phosphorylation of its intrinsically disordered region (IDR). Multiple cell polarity kinases regulate Cdc15 IDR phosphostate, and of these the DYRK kinase Pom1 phosphorylation sites on Cdc15 have been shown in vivo to prevent CR formation at cell tips. Here, we compared the ability of Pom1 to control Cdc15 phosphostate and cortical localization to that of other Cdc15 kinases: Kin1, Pck1, and Shk1. We identified distinct but overlapping cohorts of Cdc15 phosphorylation sites targeted by each kinase, and the number of sites correlated with each kinases' abilities to influence Cdc15 PM localization. Coarse-grained simulations predicted that cumulative IDR phosphorylation moves the IDRs of a dimer apart and toward the F-BAR tips. Further, simulations indicated that the overall negative charge of phosphorylation masks positively charged amino acids necessary for F-BAR oligomerization and membrane interaction. Finally, simulations suggested that dephosphorylated Cdc15 undergoes phase separation driven by IDR interactions. Indeed, dephosphorylated but not phosphorylated Cdc15 undergoes liquid-liquid phase separation to form droplets in vitro that recruit Cdc15 binding partners. In cells, Cdc15 phosphomutants also formed PM-bound condensates that recruit other CR components. Together, we propose that a threshold of Cdc15 phosphorylation by assorted kinases prevents Cdc15 condensation on the PM and antagonizes CR assembly.","doi":"10.7554/eLife.83062","authors":"Bhattacharjee R, Hall AR, Mangione MC, Igarashi MG, Roberts-Galbraith RH, Chen JS, Vavylonis D, Gould KL","authors_abbrev":"Bhattacharjee R et al.","pubmed_publication_date":"07 Feb 2023","pubmed_entrez_date":"2023-02-07","publication_year":"2023","canto_session_key":"0fa0811aad33bde1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2023-03-29 12:55:19","canto_approved_date":"2025-04-23 17:53:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-17 12:00:21","canto_added_date":"2023-02-08 01:15:06","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":43,"orcid":null,"file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":13,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC83.18c","SPBC4F6.06","SPBC19G7.05c","SPBC244.01c","SPAC2F7.03c","SPCC4B3.15","SPAC20G8.05c","SPAC1F5.04c","SPAC17G8.14c","SPBC1604.14c","SPAC926.03","SPBC4F6.12"],"gene_count":12,"ltp_gene_count":9,"approved_date":"2023-03-29"},{"uniquename":"PMID:23394940","title":"Flexible nanoassembly for sequestering non-native proteins.","citation":"Structure 2013 Feb 05;21(2):193-4","abstract":"A crystal structure of a yeast small heat shock protein reported by Hanazono and colleagues in this issue of Structure reveals the versatility of the α-crystallin domain dimer for building assemblies of different size and symmetry. The domains assemble into a vessel filled with hydrophobic sequence extensions enriched with phenylalanines.","doi":"10.1016/j.str.2013.01.009","authors":"Slingsby C, Clark AR","authors_abbrev":"Slingsby C et al.","pubmed_publication_date":"05 Feb 2013","pubmed_entrez_date":"2013-02-12","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-08-22 05:19:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16043634","title":"Cloning and characterization of the Schizosaccharomyces pombe homologs of the human protein Translin and the Translin-associated protein TRAX.","citation":"Nucleic Acids Res 2005;33(13):4128-39","abstract":"Translin is a human octameric protein that specifically binds the single-stranded microsatellite repeats d(GT)n and the corresponding transcripts (GU)n. It also binds, with lesser affinities, other single-stranded G-rich DNA and RNA sequences. TRAX is a human protein that bears a homology to Translin and interacts with it. Translin and TRAX have been proposed to be involved in DNA recombination, chromosomal translocation and mRNA transport and translation. Both proteins are highly conserved in eukaryotes, including the fission yeast Schizosaccharomyces pombe, which is amenable to genetic analysis. Here, we report the first study of the S.pombe Translin and TRAX homologs. We have deleted the genes encoding Translin and TRAX in S.pombe and found that the proliferation of the mutant cells was slightly stimulated, suggesting that these genes are not essential for the fission yeast. We have also shown that the S.pombe Translin and TRAX interact. Biochemical analysis of the S.pombe Translin, which was cloned and expressed in Escherichia coli, revealed that it is octameric and that it selectively binds d(GT)n and d(GTT)n microsatellite repeats. However, unlike the human protein, it has much higher affinities for the homologous RNA sequences (GU)n and (GUU)n. These data suggest that the S.pombe Translin is primarily involved in functions related to RNA metabolism.","authors":"Laufman O, Ben Yosef R, Adir N, Manor H","authors_abbrev":"Laufman O et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-07-27","publication_year":"2005","canto_session_key":"90ad8a21a33a782d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-26 16:14:16","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-02-26 16:13:21","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.09c","SPAC30.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-02-26"},{"uniquename":"PMID:39796344","title":"Development of a Wine Yeast Strain Capable of Malolactic Fermentation and Reducing the Ethyl Carbamate Content in Wine.","citation":"Foods 2024 Dec 27;14(1)","abstract":"In winemaking, malolactic fermentation (MLF), which converts L-malic acid to L-lactic acid, is often applied after the alcoholic fermentation stage to improve the sensory properties of the wine and its microbiological stability. MLF is usually performed by lactic acid bacteria, which, however, are sensitive to the conditions of alcoholic fermentation. Therefore, the development of wine yeast strains capable of both alcoholic fermentation and MLF is an important task. Using genome editing, we engineered a modified variant of the triploid wine yeast strain  Saccharomyces cerevisiae  I-328, in which the  CAR1  arginase gene was replaced by the malate permease gene from  Schizosaccharomyces pombe  and the malolactic enzyme gene from  Oenococcus oeni . Genome-wide transcriptional profiling confirmed the expression of the introduced genes and revealed a limited effect of the modification on global gene expression. Winemaking experiments show that genome editing did not affect fermentation activity and ethanol production, while use of the modified strain resulted in a tenfold reduction in malate content with simultaneous formation of lactate. The resulting wines had a softer and more harmonious taste compared to wine obtained using the parental strain. Inactivation of arginase, which forms urea and L-ornithine through the breakdown of arginine, also resulted in a twofold decrease in the content of urea and the carcinogenic ethyl carbamate in wine. Thus, the new strain with the replacement of the arginase gene with the MLF gene cassette is promising for use in winemaking.","doi":"10.3390/foods14010054","authors":"Vasyagin EA, Urakov VN, Shalamitskiy MY, Cherviak SN, Ivanova EV, Zagoruyko VI, Beletsky AV, Rakitin AL, Mardanova ES, Kushnirov VV, Ravin NV, Mardanov AV","authors_abbrev":"Vasyagin EA et al.","pubmed_publication_date":"27 Dec 2024","pubmed_entrez_date":"2025-01-11","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2025-01-12 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR18921","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC119.12","HGNC:12305"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:3153581","title":"Regulation of meiosis in Schizosaccharomyces pombe.","citation":"Microbiol Sci 1986 Aug;3(8):234-7","abstract":"Analysis of a new class of meiotic mutants isolated in the fission yeast Schizosaccharomyces pombe strongly indicates that the gene in which they are deficient codes for a factor whose physiological role is inhibition of initiation of meiosis. A negative control mechanism for meiosis is discussed.","authors":"Yamamoto M","authors_abbrev":"Yamamoto M","pubmed_publication_date":"Aug 1986","pubmed_entrez_date":"1986-08-01","publication_year":"1986","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23032265","title":"Dynamic nature of heterochromatin highlighted by a HP1Swi6-dependent gene silencing mechanism.","citation":"Cell Cycle 2012 Nov 01;11(21):3907-8","abstract":"","doi":"10.4161/cc.22234","authors":"Bühler M, Hiller S","authors_abbrev":"Bühler M et al.","pubmed_publication_date":"01 Nov 2012","pubmed_entrez_date":"2012-10-04","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26147350","title":"The Protein Level of Rev1, a TLS Polymerase in Fission Yeast, Is Strictly Regulated during the Cell Cycle and after DNA Damage.","citation":"PLoS One 2015;10(7):e0130000","abstract":"Translesion DNA synthesis provides an alternative DNA replication mechanism when template DNA is damaged. In fission yeast, Eso1 (polη), Kpa1/DinB (polκ), Rev1, and Polζ (a complex of Rev3 and Rev7) have been identified as translesion synthesis polymerases. The enzymatic characteristics and protein-protein interactions of these polymerases have been intensively characterized; however, how these proteins are regulated during the cell cycle remains unclear. Therefore, we examined the cell cycle oscillation of translesion polymerases. Interestingly, the protein levels of Rev1 peaked during G1 phase and then decreased dramatically at the entry of S phase; this regulation was dependent on the proteasome. Temperature-sensitive proteasome mutants, such as mts2-U31 and mts3-U32, stabilized Rev1 protein when the temperature was shifted to the restrictive condition. In addition, deletion of pop1 or pop2, subunits of SCF ubiquitin ligase complexes, upregulated Rev1 protein levels. Besides these effects during the cell cycle, we also observed upregulation of Rev1 protein upon DNA damage. This upregulation was abolished when rad3, a checkpoint protein, was deleted or when the Rev1 promoter was replaced with a constitutive promoter. From these results, we hypothesize that translesion DNA synthesis is strictly controlled through Rev1 protein levels in order to avoid unwanted mutagenesis.","doi":"10.1371/journal.pone.0130000","authors":"Uchiyama M, Terunuma J, Hanaoka F","authors_abbrev":"Uchiyama M et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-07-07","publication_year":"2015","canto_session_key":"90316fb4e00b13b5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-07-08 00:22:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12D12.09","SPBC1347.01c","SPAC4D7.03","SPBC16A3.11","SPBC1718.01"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:1833395","title":"The pma1 and pma2 H(+)-ATPases from Schizosaccharomyces pombe are functionally interchangeable.","citation":"J Biol Chem 1991 Sep 25;266(27):18276-9","abstract":"The pma2 gene of Schizosaccharomyces pombe codes for a polypeptide having a predicted Mr of 110,126 and which is 79% identical to the plasma membrane H(+)-ATPase encoded by the pma1 gene. The pma2 gene, unlike pma1, is weakly expressed and not essential to mitotic growth. By constructing yeast strains in which the chromosomal pma2 gene is under control of the adh promoter, it has been possible to identify the overproduced ATPase in plasma membrane via formation of a phosphoenzyme. In a pma1-1 mutant strain whose ATPase activity is insensitive to vanadate, the overexpressed pma2 gene restores vanadate sensitivity. It also rescues a pma1 null mutant from lethality. These results demonstrate that the two H(+)-ATPases are functionally interchangeable in vivo but differently expressed.","authors":"Ghislain M, Goffeau A","authors_abbrev":"Ghislain M et al.","pubmed_publication_date":"25 Sep 1991","pubmed_entrez_date":"1991-09-25","publication_year":"1991","canto_session_key":"0b858a6efa067b13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-26 21:59:35","canto_approved_date":"2026-02-24 20:12:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-08 16:30:53","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1020.01c","SPAC1071.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-02-26"},{"uniquename":"PMID:40640210","title":"HP1 loses its chromatin clustering and phase separation function across evolution.","citation":"Nat Commun 2025 Jul 10;16(1):6375","abstract":"Heterochromatin protein 1 (HP1) is a multifunctional chromatin-associated protein conserved from fission yeast to mammals. HP1 has been suggested to drive heterochromatin formation via phase separation. However, there is seemingly conflicting evidence about HP1 phase-separating in different systems or not. Here, we assess the phase separation behavior of HP1 from fission yeast, fruit fly and mouse in vitro and in mammalian cells side-by-side. We find that HP1 from fission yeast and fly can undergo liquid-liquid phase separation and induce heterochromatin coalescence in mouse cells, in stark contrast to HP1 from mouse. Induced heterochromatin coalescence has only mild effects on gene expression. We link the decreasing phase separation propensity of HP1 homologs to their decreasing intrinsic disorder and their increasing sensitivity to HP1 paralogs antagonizing phase separation. Our work elucidates the relationship between phase separation, nuclear organization and gene expression, and highlights the evolutionary dimension of protein phase separation control.","doi":"10.1038/s41467-025-61749-3","authors":"Bensaha S, Lewandowska D, Muzzopappa F, Hutin S, Tully MD, Anfossi M, Cammas FM, Normand C, Erdel F","authors_abbrev":"Bensaha S et al.","pubmed_publication_date":"10 Jul 2025","pubmed_entrez_date":"2025-07-10","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-11 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33121335","title":"A novel reticulophagy receptor, Epr1: a bridge between the phagophore protein Atg8 and ER transmembrane VAP proteins.","citation":"Autophagy 2021 Mar;17(3):597-598","abstract":"Reticulophagy, a type of selective autophagy that specifically targets and degrades parts of the endoplasmic reticulum (ER) network (sheets or tubules), plays a crucial role in the responses to ER stress. The selectivity of the ER cargo recognition relies on the unique reticulophagy receptors, which tether and deliver cargos to phagophores, the precursors to autophagosomes. Various integral membrane proteins have been well characterized as reticulophagy receptors, including Atg39, Atg40, RETREG1/FAM134B, SEC62, RTN3L, CCPG1, TEX264, and ATL3, in both yeast and mammals in the past five years. In a recent paper, Zhao et al. discovered in fission yeast a novel reticulophagy receptor, Epr1, which bridges the ER and phagophore by binding to Atg8 and VAPs, a mechanism different from the aforementioned reticulophagy receptors.","doi":"10.1080/15548627.2020.1837457","authors":"Yang Y, Klionsky DJ","authors_abbrev":"Yang Y et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2020-10-30","publication_year":"2021","canto_session_key":"1450f8d6c5f392db","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-11-01 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23349808","title":"Fission yeast Nod1 is a component of cortical nodes involved in cell size control and division site placement.","citation":"PLoS One 2013;8(1):e54142","abstract":"Most cells enter mitosis once they have reached a defined size. In the fission yeast Schizosaccharomyces pombe, mitotic entry is orchestrated by a geometry-sensing mechanism that involves the Cdk1/Cdc2-inhibiting Wee1 kinase. The factors upstream of Wee1 gather together in interphase to form a characteristic medial and cortical belt of nodes. Nodes are also considered to be precursors of the cytokinesis contractile actomyosin ring (CAR). Here we describe a new component of the interphase nodes and cytokinesis rings, which we named Nod1. Consistent with its role in cell size control at division, nod1Δ cells were elongated and epistatic with regulators of Wee1. Through biochemical and localisation studies, we placed Nod1 in a complex with the Rho-guanine nucleotide exchange factor Gef2. Nod1 and Gef2 mutually recruited each other in nodes and Nod1 also assembles Gef2 in rings. Like gef2Δ, nod1Δ cells showed a mild displacement of their division plane and this phenotype was severely exacerbated when the parallel Polo kinase pathway was also compromised. We conclude that Nod1 specifies the division site by localising Gef2 to the mitotic cell middle. Previous work showed that Gef2 in turn anchors factors that control the spatio-temporal recruitment of the actin nucleation machinery. It is believed that the actin filaments originated from the nodes pull nodes together into a single contractile ring. Surprisingly however, we found that node proteins could form pre-ring helical filaments in a cdc12-112 mutant in which nucleation of the actin ring is impaired. Furthermore, the deletion of either nod1 or gef2 created an un-expected situation where different ring components were recruited sequentially rather than simultaneously. At later stages of cytokinesis, these various rings appeared inter-fitted rather than merged. This study brings a new slant to the understanding of CAR assembly and function.","doi":"10.1371/journal.pone.0054142","authors":"Jourdain I, Brzezińska EA, Toda T","authors_abbrev":"Jourdain I et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-01-26","publication_year":"2013","canto_session_key":"eef07d879f4207d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Isabelle Jourdain","canto_first_approved_date":"2017-05-28 17:06:21","canto_approved_date":"2020-12-12 17:45:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-01 15:25:50","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":38,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Isabelle Jourdain","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.04c","SPAC31A2.16","SPAC23C11.16","SPAC12B10.10","SPBC1A4.05","SPCC4B3.15","SPAC2F7.03c","SPCC18B5.03","SPAC926.03","SPAC57A10.02","SPAC24H6.05","SPAC644.06c"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2017-05-28"},{"uniquename":"PMID:24127216","title":"The formins Cdc12 and For3 cooperate during contractile ring assembly in cytokinesis.","citation":"J Cell Biol 2013 Oct 14;203(1):101-14","abstract":"Both de novo-assembled actin filaments at the division site and existing filaments recruited by directional cortical transport contribute to contractile ring formation during cytokinesis. However, it is unknown which source is more important. Here, we show that fission yeast formin For3 is responsible for node condensation into clumps in the absence of formin Cdc12. For3 localization at the division site depended on the F-BAR protein Cdc15, and for3 deletion was synthetic lethal with mutations that cause defects in contractile ring formation. For3 became essential in cells expressing N-terminal truncations of Cdc12, which were more active in actin assembly but depended on actin filaments for localization to the division site. In tetrad fluorescence microscopy, double mutants of for3 deletion and cdc12 truncations were severely defective in contractile ring assembly and constriction, although cortical transport of actin filaments was normal. Together, these data indicate that different formins cooperate in cytokinesis and that de novo actin assembly at the division site is predominant for contractile ring formation.","doi":"10.1083/jcb.201305022","authors":"Coffman VC, Sees JA, Kovar DR, Wu JQ","authors_abbrev":"Coffman VC et al.","pubmed_publication_date":"14 Oct 2013","pubmed_entrez_date":"2013-10-16","publication_year":"2013","canto_session_key":"612939864abd598a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Valerie Coffman","canto_first_approved_date":"2015-10-08 15:21:25","canto_approved_date":"2024-04-04 08:02:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-11 21:38:34","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Coffman","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08","SPCC645.05c","SPAC20G8.05c","SPAC1F5.04c","SPCC895.05","SPAC926.03","SPCC4B3.15","SPAC630.03","SPAC4A8.15c","SPAC4F8.13c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-10-08"},{"uniquename":"PMID:12062100","title":"Cid13 is a cytoplasmic poly(A) polymerase that regulates ribonucleotide reductase mRNA.","citation":"Cell 2002 May 31;109(5):563-73","abstract":"Fission yeast Cid13 and budding yeast Trf4/5 are members of a newly identified nucleotidyltransferase family conserved from yeast to man. Trf4/5 are thought to be essential DNA polymerases. We report that Cid13 is a poly(A) polymerase. Unlike conventional poly(A) polymerases, which act in the nucleus and indiscriminately polyadenylate all mRNA, Cid13 is a cytoplasmic enzyme that specifically targets suc22 mRNA that encodes a subunit of ribonucleotide reductase (RNR). cid13 mutants have reduced dNTP pools and are sensitive to hydroxyurea, an RNR inhibitor. We propose that Cid13 defines a cytoplasmic form of poly(A) polymerase important for DNA replication and genome maintenance.","authors":"Saitoh S, Chabes A, McDonald WH, Thelander L, Yates JR, Russell P","authors_abbrev":"Saitoh S et al.","pubmed_publication_date":"31 May 2002","pubmed_entrez_date":"2002-06-14","publication_year":"2002","canto_session_key":"df782d43e0f73c73","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-09-24 10:22:12","canto_approved_date":"2023-03-15 08:43:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-24 10:22:01","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC1259.13","SPAC664.07c","SPBC21B10.03c","SPBC216.05","SPCC18B5.11c","SPAC13G7.02c","SPAC8E11.02c","SPAC9G1.05","SPAC1952.07","SPAC14C4.13","SPAC17A2.13c","SPAC821.04c","SPAC9E9.08","SPBC25D12.04","SPAC57A7.04c","SPAC926.04c"],"gene_count":17,"ltp_gene_count":17,"approved_date":"2021-09-24"},{"uniquename":"PMID:3116001","title":"Change in the rate of CO2 production in synchronous cultures of the fission yeast Schizosaccharomyces pombe: a periodic cell cycle event that persists after the DNA-division cycle has been blocked.","citation":"J Cell Sci 1986 Dec;86:191-206","abstract":"CO2 production has been followed by manometry in synchronous and asynchronous cultures of Schizosaccharomyces pombe prepared by elutriation from the same initial culture. The rate of production follows a linear pattern in synchronous cultures with a rate change once per cycle at the time of cell division. This pattern is most clearly shown in oscillations of the difference between values of the second differential (acceleration) for the synchronous and asynchronous cultures. The association between the rate change and the time of division is maintained during growth speeded up in rich medium and slowed down in poor medium and at lower temperature. It is also maintained after a shift-up in temperature. Results with wee mutants suggest that the association is with the S period rather than division itself. The rate and acceleration of CO2 production are approximately proportional to cell size (protein content) in asynchronous cultures. When synchronous cultures of the temperature-sensitive mutants cdc2.33 and cdc2.33 wee1.6 are shifted up to the restrictive temperature, the DNA-division cycle is blocked. The oscillatory pattern of CO2 production, however, continues for one to two cycles until the acceleration reaches a constant value, after which the oscillations are undetectable. This point is reached later in the double mutant and there is a phase difference in the oscillations compared to those in the single mutant. With both blocked mutants the 'free-running' oscillations are about 15% shorter than the normal cycle time. There are well-known examples of such oscillations in eggs but they are rare in growing systems.","authors":"Novak B, Mitchison JM","authors_abbrev":"Novak B et al.","pubmed_publication_date":"Dec 1986","pubmed_entrez_date":"1986-12-01","publication_year":"1986","canto_session_key":"2eb1bb260acf60e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-08-26 09:49:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-25 11:59:19","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC18B5.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-08-25"},{"uniquename":"PMID:3464952","title":"Analysis of centromeric DNA in the fission yeast Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1986 Nov;83(21):8253-7","abstract":"The Schizosaccharomyces pombe centromere-linked genes, LYS1 and CYH1 on chromosome I and TPS13 and RAN1 on chromosome II, have been isolated. The genetic order of these markers with respect to their centromeres was determined to establish relative directionality on the genetic and physical maps. Chromosome walking toward the centromeres reveals a group of repetitive sequences that occur only in the centromere regions of chromosomes I and II and at one other specific location in the S. pombe genome, presumably the centromere of chromosome III. The major class of large repeated sequence elements is 6.4 kilobases (kb) long (repeat K), portions of which occur at least twice on chromosome II and in several tandemly arranged intact copies at another centromeric location. Repeat K in turn contains groups of smaller repeats. Genetic recombination is strongly suppressed in the centromere II region, which contains at least 30 kb of repeated sequences. Centromeric DNA organization is much more complex in fission yeast than has been described in budding yeast (Saccharomyces cerevisiae), possibly because of the larger more condensed nature of the S. pombe chromosomes.","authors":"Clarke L, Amstutz H, Fishel B, Carbon J","authors_abbrev":"Clarke L et al.","pubmed_publication_date":"Nov 1986","pubmed_entrez_date":"1986-11-01","publication_year":"1986","canto_session_key":"07c572c62c49c3da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 14:47:46","canto_approved_date":"2019-01-07 14:47:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 14:47:40","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:41008638","title":"Inorganic Polyphosphate Modulates Chromosome Transmission Fidelity in the Fission Yeast  Schizosaccharomyces pombe .","citation":"Biomolecules 2025 Sep 18;15(9)","abstract":"Chromosome transmission fidelity is vital for organism fitness. Yet, extrinsic and intrinsic changes can affect this process, leading to aneuploidy, the loss/gain of chromosomes, which is a hallmark of cancer. Here, using a haploid fission yeast  Schizosaccharomyces pombe  strain with a segmental aneuploidy, we assayed genome stability under different temperatures and altered gene dosage. We find that  S. pombe  genome stability is temperature-dependent and is unexpectedly modulated by intracellular levels of inorganic polyphosphate polymers (polyP). The  vtc4 +   gene, encoding a subunit of the polyP-generating VTC complex, is present twice due to the segmental aneuploidy resulting in a gene-dosage-coupled increase in polyP. Using strains with different amounts of polyP, we find a direct negative correlation between polyP and chromosome segregation fidelity. PolyP modulates the function of the conserved CCAN kinetochore subcomplex, as the abnormal growth phenotype caused by the mutant CCAN protein Fta2-291 was rescued in the absence of polyP, while extra polyP had the opposite effect. Importantly, this appears to occur in part by modulation of the nucleolin Gar2. Gar2 is the functional homolog of the  Saccharomyces cerevisiae  Nsr1 protein, whose function is modulated by posttranslational polyP-mediated polyphosphorylation. Thus, polyP modulates genome stability, linking cellular metabolism to chromosome transmission fidelity.","doi":"10.3390/biom15091331","authors":"Bollé S, Koc E, Saiardi A, Juhran L, Walla E, Fleig U, Alcázar-Román A","authors_abbrev":"Bollé S et al.","pubmed_publication_date":"18 Sep 2025","pubmed_entrez_date":"2025-09-27","publication_year":"2025","canto_session_key":"c7ed486c940c7fb0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-27 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30422110","title":"Structural basis of tubulin recruitment and assembly by microtubule polymerases with tumor overexpressed gene (TOG) domain arrays.","citation":"Elife 2018 Nov 13;7","abstract":"XMAP215/Stu2/Alp14 proteins accelerate microtubule plus-end polymerization by recruiting tubulins via arrays of tumor overexpressed gene (TOG) domains, yet their mechanism remains unknown. Here, we describe the biochemical and structural basis for TOG arrays in recruiting and polymerizing tubulins. Alp14 binds four tubulins via dimeric TOG1-TOG2 subunits, in which each domain exhibits a distinct exchange rate for tubulin. X-ray structures revealed square-shaped assemblies composed of pseudo-dimeric TOG1-TOG2 subunits assembled head-to-tail, positioning four unpolymerized tubulins in a polarized wheel-like configuration. Crosslinking and electron microscopy show Alp14-tubulin forms square assemblies in solution, and inactivating their interfaces destabilize this organization without influencing tubulin binding. An X-ray structure determined using approach to modulate tubulin polymerization revealed an unfurled assembly, in which TOG1-TOG2 uniquely bind to two polymerized tubulins. Our findings suggest a new microtubule polymerase model in which TOG arrays recruit tubulins by forming square assemblies that then unfurl, facilitating their concerted polymerization into protofilaments.","doi":"10.7554/eLife.38922","authors":"Nithianantham S, Cook BD, Beans M, Guo F, Chang F, Al-Bassam J","authors_abbrev":"Nithianantham S et al.","pubmed_publication_date":"13 Nov 2018","pubmed_entrez_date":"2018-11-14","publication_year":"2018","canto_session_key":"13d185b487b72ba0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-11-15 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC895.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9636183","title":"Fission yeast orb6, a ser/thr protein kinase related to mammalian rho kinase and myotonic dystrophy kinase, is required for maintenance of cell polarity and coordinates cell morphogenesis with the cell cycle.","citation":"Proc Natl Acad Sci U S A 1998 Jun 23;95(13):7526-31","abstract":"The molecular mechanisms that coordinate cell morphogenesis with the cell cycle remain largely unknown. We have investigated this process in fission yeast where changes in polarized cell growth are coupled with cell cycle progression. The orb6 gene is required during interphase to maintain cell polarity and encodes a serine/threonine protein kinase, belonging to the myotonic dystrophy kinase/cot1/warts family. A decrease in Orb6 protein levels leads to loss of polarized cell shape and to mitotic advance, whereas an increase in Orb6 levels maintains polarized growth and delays mitosis by affecting the p34(cdc2) mitotic kinase. Thus the Orb6 protein kinase coordinates maintenance of cell polarity during interphase with the onset of mitosis. orb6 interacts genetically with orb2, which encodes the Pak1/Shk1 protein kinase, a component of the Ras1 and Cdc42-dependent signaling pathway. Our results suggest that Orb6 may act downstream of Pak1/Shk1, forming part of a pathway coordinating cell morphogenesis with progression through the cell cycle.","authors":"Verde F, Wiley DJ, Nurse P","authors_abbrev":"Verde F et al.","pubmed_publication_date":"23 Jun 1998","pubmed_entrez_date":"1998-06-24","publication_year":"1998","canto_session_key":"adf22222853d160f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-16 10:49:52","canto_approved_date":"2020-03-16 16:15:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-09 16:38:29","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.12","SPBC1604.14c","SPCC18B5.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-08-16"},{"uniquename":"PMID:19723888","title":"Inhibition of type I histone deacetylase increases resistance of checkpoint-deficient cells to genotoxic agents through mitotic delay.","citation":"Mol Cancer Ther 2009 Sep;8(9):2606-15","abstract":"Histone deacetylase (HDAC) inhibitors potently inhibit tumor growth and are currently being evaluated for their efficacy as chemosensitizers and radiosensitizers. This efficacy is likely to be limited by the fact that HDAC inhibitors also induce cell cycle arrest. Deletion of the class I HDAC Rpd3 has been shown to specifically suppress the sensitivity of Saccharomyces cerevisiae DNA damage checkpoint mutants to UV and hydroxyurea. We show that in the fission yeast Schizosaccharomyces pombe, inhibition of the homologous class I HDAC specifically suppresses the DNA damage sensitivity of checkpoint mutants. Importantly, the prototype HDAC inhibitor Trichostatin A also suppressed the sensitivity of DNA damage checkpoint but not of DNA repair mutants to UV and HU. TSA suppressed DNA damage activity independently of the mitogen-activated protein kinase-dependent and spindle checkpoint pathways. We show that TSA delays progression into mitosis and propose that this is the main mechanism for suppression of the DNA damage sensitivity of S. pombe checkpoint mutants, partially compensating for the loss of the G(2) checkpoint pathway. Our studies also show that the ability of HDAC inhibitors to suppress DNA damage sensitivity is not species specific. Class I HDACs are the major target of HDAC inhibitors and cancer cells are often defective in checkpoint activation. Effective use of these agents as chemosensitizers and radiosensitizers may require specific treatment schedules that circumvent their inhibition of cell cycle progression.","doi":"10.1158/1535-7163.MCT-09-0218","authors":"Alao JP, Olesch J, Sunnerhagen P","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-09-03","publication_year":"2009","canto_session_key":"335eb22b9fc8a7c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Per Sunnerhagen","canto_first_approved_date":"2013-07-15 11:12:50","canto_approved_date":"2021-06-22 14:21:01","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-06-28 12:59:03","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Per Sunnerhagen","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":42,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.07c","SPAC24B11.06c","SPAC1952.07","SPBC800.03","SPCC18B5.11c","SPCC1322.08","SPBC36.05c","SPCC18B5.03","SPBC11B10.09","SPCC1259.13","SPBC216.05","SPAC20G4.04c","SPBC20F10.06"],"gene_count":13,"ltp_gene_count":11,"approved_date":"2013-07-15"},{"uniquename":"PMID:5875030","title":"[Study on the synthesis of acetoin by Saccharomyces cerevisiae and Schizosaccharomyces pombe].","citation":"Arch Mikrobiol 1965 Dec 07;52(4):345-52","abstract":"","authors":"Dittrich HH, Eschenbruch R","authors_abbrev":"Dittrich HH et al.","pubmed_publication_date":"07 Dec 1965","pubmed_entrez_date":"1965-12-07","publication_year":"1965","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11087750","title":"Structure of Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe.","citation":"J Biol Chem 2001 Feb 23;276(8):5943-51","abstract":"The Schizosaccharomyces pombe Cdc4 protein is required for the formation and function of the contractile ring, presumably acting as a myosin light chain. By using NMR spectroscopy, we demonstrate that purified Cdc4p is a monomeric protein with two structurally independent domains, each exhibiting a fold reminiscent of the EF-hand class of calcium-binding proteins. Although Cdc4p has one potentially functional calcium-binding site, it does not bind calcium in vitro. Three variants of Cdc4p containing single point mutations responsible for temperature-sensitive arrest of the cell cycle at cytokinesis (Gly-19 to Glu, Gly-82 to Asp, and Gly-107 to Ser) were also characterized by NMR and circular dichroism spectroscopy. In each case, the amino acid substitution only leads to small perturbations in the conformation of the protein. Furthermore, thermal unfolding studies indicate that, like wild-type Cdc4p, the three mutant forms are all extremely stable, remaining completely folded at temperatures significantly above those causing failure of cytokinesis in intact cells. Therefore, the altered phenotype must arise directly from a disruption of the function of Cdc4p rather than indirectly through a disruption of its overall structure. Several mutant alleles of Cdc4p also show interallelic complementation in diploid cells. This phenomenon can be explained if Cdcp4 has more than one essential function or, alternatively, if two mutant proteins assemble to form a functional complex. Based on the structure of Cdc4p, possible models for interallelic complementation including interactions with partner proteins and the formation of a myosin complex with Cdc4p fulfilling the role of both an essential and regulatory light chain are proposed.","authors":"Slupsky CM, Desautels M, Huebert T, Zhao R, Hemmingsen SM, McIntosh LP","authors_abbrev":"Slupsky CM et al.","pubmed_publication_date":"23 Feb 2001","pubmed_entrez_date":"2000-11-23","publication_year":"2001","canto_session_key":"bdbe3a9490dcf6a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-04 14:22:30","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-09-04 14:22:17","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-04","pdb_entries":[{"pdb_id":"1ggw","gene_chains":[{"gene_uniquename":"SPAP8A3.08","chain":"A","position":"2-141"}],"title":"CDC4P FROM SCHIZOSACCHAROMYCES POMBE","entry_authors":"Slupsky CM,Hemmingsen SM,McIntosh LP","entry_authors_abbrev":"Slupsky CM et al.","reference_uniquename":"PMID:11087750","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:10982890","title":"Human RNA lariat debranching enzyme cDNA complements the phenotypes of Saccharomyces cerevisiae dbr1 and Schizosaccharomyces pombe dbr1 mutants.","citation":"Nucleic Acids Res 2000 Sep 15;28(18):3666-73","abstract":"The cDNA encoding the human RNA lariat debranching enzyme (hDBR1) was identified and cloned by searching the Expressed Sequence Tag (EST) database and screening a HeLa cDNA library, based on predicted amino acid sequence homologies with the Saccharomyces cerevisiae, Schizosaccharomyces pombe and Caenorhabditis elegans debranching enzymes. The hDBR1 cDNA expressed in Escherichia coli showed debranching activity in vitro and was also shown to be functional in an interspecies specific complementation experiment. hDBR1 cDNA in a S. cerevisiae expression vector complemented the intron accumulation phenotype of a S. cerevisiae dbr1 null mutant. Integration of the cDNA for hDBR1 into the ura4 locus of S. pombe also complemented both the intron accumulation and slow growth phenotypes of a S. pombe dbr1 null mutant strain. Comparison of the amino acid sequence of hDBR1 with the other DBR protein sequences showed several conserved regions, with 40, 44 and 43% identity to the S. cerevisiae, S. pombe and C. elegans debranching enzymes, respectively.","authors":"Kim JW, Kim HC, Kim GM, Yang JM, Boeke JD, Nam K","authors_abbrev":"Kim JW et al.","pubmed_publication_date":"15 Sep 2000","pubmed_entrez_date":"2000-09-13","publication_year":"2000","canto_session_key":"568a3b7940a857ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-07 17:31:57","canto_approved_date":"2019-11-07 17:31:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-07 17:31:52","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-07"},{"uniquename":"PMID:29813128","title":"The fission yeast SPB component Dms1 is required to initiate forespore membrane formation and maintain meiotic SPB components.","citation":"PLoS One 2018;13(5):e0197879","abstract":"The spindle pole body (SPB) plays a central role in spore plasma membrane formation in addition to its recognized role in microtubule organization. During meiosis, a biomembrane called the forespore membrane (FSM) is newly formed at the SPB. Although several SPB proteins essential for the initiation of FSM formation (meiotic SPB components) have been identified, the molecular mechanism is still unknown. Here, we report the isolation and functional characterization of Dms1 as a component of the SPB. We show that FSM formation does not initiate in dms1Δ cells. Dms1 protein is constitutively expressed throughout the life cycle and localizes to the SPB and the nuclear envelope. The predicted Dms1 protein has a transmembrane domain, which is required for correct localization at the SPB. Dms1 is essential for the proper localization of three meiotic SPB components, Spo15, Spo2, and Spo13, but these components do not affect localization of Dms1. Collectively, these results suggest that Dms1 anchors these meiotic SPB components to the SPB, thereby facilitating the initiation of FSM formation.","doi":"10.1371/journal.pone.0197879","authors":"Niimi T, Nakamura T","authors_abbrev":"Niimi T et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-05-30","publication_year":"2018","canto_session_key":"23d6ce7d8178a0ee","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-06-01 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18368927","title":"The spindle checkpoint: how do cells delay anaphase onset?","citation":"SEB Exp Biol Ser 2008;59:243-56","abstract":"Several models have been suggested above, describing possible modes of spindle checkpoint action: 1. Cdc20 sequestration (by Mad2-Cdc20 and/or MCC). 2. Stable MCC-APC/C association. 3. Cdc20 turnover (in budding yeast). 4. Cdc20-APC/C modification (by Mps1, Bub1, MAPK, Aurora B or BubR1 kinases). Several of these mechanisms could affect APC/C activity by modifying, competing for, and/or blocking the binding site(s) for its substrates. Alternatively, they could reduce the processivity of ubiquitination of substrates, or prevent the release of substrates and thereby reduce substrate turnover. Indeed, the processivity of ubiquitination can determine the order of destruction of APC/C substrates (Rape et al., 2006). Most substrates require multiple APC/C binding events in order to build polyubiquitin chains, and only polyubiquitinated substrates are recognised by the 26S proteasome for destruction. Thus, if the processivity of ubiquitination or the turnover of APC/C substrates were impaired in mitosis, the degradation of securin and cyclin would no longer take place, which would result in mitotic arrest. Our results have highlighted the importance of Mad3 as an anaphase inhibitor, and suggest that it usually acts in concert with Mad2 to efficiently inhibit Cdc20-APC/C. Further experiments are necessary to fully understand their mechanism of action, and this will require a wide range of approaches including dynamic studies of the 'flux' of Mad2 and BubR1 through signalling scaffolds, further structural insights, the identification of important phosphorylation sites on both the checkpoint proteins and Cdc20-APC/C, and an in vitro reconstitution of MCC inhibition of the APC/C. We look forward to seeing the complex regulation of mitotic progression being described over the coming years.","authors":"Sczaniecka MM, Hardwick KG","authors_abbrev":"Sczaniecka MM et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-03-29","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10801329","title":"Ultraviolet damage endonuclease (Uve1p): a structure and strand-specific DNA endonuclease.","citation":"Biochemistry 2000 May 16;39(19):5788-96","abstract":"Schizosaccharomyces pombe ultraviolet damage endonuclease (UVDE or Uve1p) performs the initial step in an alternative excision repair pathway for UV-induced DNA damage. This DNA repair pathway was originally thought to be specific for UV damage. However, the broad substrate specificity of Uve1p suggests a more general role for this enzyme. Uve1p recognizes UV-induced bipyrimidine photoadducts and other non-UV-induced DNA adducts. Biochemical and genetic analysis also suggests that Uve1p may be involved in orchestrating mismatch repair in vivo. This study demonstrates that Uve1p recognizes and cleaves heteroduplex DNA with small unpaired loops but does not recognize loops six to eight nucleotides in length. In addition, the enzyme does not recognize DNA with palindromic insertions that could form base-paired hairpin structures. The cleavage efficiency of Uve1p depends on the distance of a mismatch from the DNA terminus, suggesting that the 3' terminus may contribute to the strand discrimination signal for Uve1p. These biochemical activities are discussed in the context of the role of Uve1p in DNA repair.","authors":"Kaur B, Doetsch PW","authors_abbrev":"Kaur B et al.","pubmed_publication_date":"16 May 2000","pubmed_entrez_date":"2000-05-10","publication_year":"2000","canto_session_key":"8e7f14a45fdb3d89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-01 08:57:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-01 08:48:30","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-01"},{"uniquename":"PMID:8807800","title":"Autocrine response of Schizosaccharomyces pombe haploid cells to mating pheromones.","citation":"FEMS Microbiol Lett 1996 Sep 15;143(1):41-5","abstract":"The mating response of the fission yeast Schizosaccharomyces pombe is mediated by mating pheromones, M-factor and P-factor, produced by h- and h+ cells, respectively. When the M-factor receptor (Map3) was ectopically expressed in h- cells lacking the P-factor receptor (Mam2), they acquired mating competence in response to M-factor which they secreted. The autocrine response to P-factor in h- cells was so weak that mating competence was not acquired, although expression of the pheromone-responsive gene matl-Pm was detected. These observations support the notion that the intensity of cellular response to mating phermones is different between h- and h+ cells, although downstream pathways of the pheromone receptors are shared by the two mating types.","authors":"Kitamura K, Nakamura T, Miki F, Shimoda C","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"15 Sep 1996","pubmed_entrez_date":"1996-09-15","publication_year":"1996","canto_session_key":"7f7a3d91c943972f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-26 14:39:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-08 03:41:06","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.10c","SPAC11H11.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-01-08"},{"uniquename":"PMID:11030343","title":"Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control.","citation":"Mol Cell 2000 Sep;6(3):637-48","abstract":"Cdc6/Cdc18 is a conserved and essential component of prereplication complexes. The 2.0 A crystal structure of an archaeal Cdc6 ortholog, in conjunction with a mutational analysis of the homologous Cdc18 protein from Schizosaccharomyces pombe, reveals novel aspects of Cdc6/Cdc18 function. Two domains of Cdc6 form an AAA+-type nucleotide binding fold that is observed bound to Mg.ADP. A third domain adopts a winged-helix fold similar to known DNA binding modules. Sequence comparisons show that the winged-helix domain is conserved in Orc1, and mutagenesis data demonstrate that this region of Cdc6/Cdc18 is required for function in vivo. Additional mutational analyses suggest that nucleotide binding and/or hydrolysis by Cdc6/Cdc18 is required not only for progression through S phase, but also for maintenance of checkpoint control during S phase.","authors":"Liu J, Smith CL, DeRyckere D, DeAngelis K, Martin GS, Berger JM","authors_abbrev":"Liu J et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-10-13","publication_year":"2000","canto_session_key":"6e9c92a7382e9127","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-03 15:55:48","canto_approved_date":"2023-09-11 08:05:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-09 11:26:29","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":79,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_11030343_phaf.tsv"}],"genes":["SPBC14C8.07c","SPAC1952.07","SPAC20G4.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-07-03"},{"uniquename":"PMID:9136929","title":"The Mcs4 response regulator coordinately controls the stress-activated Wak1-Wis1-Sty1 MAP kinase pathway and fission yeast cell cycle.","citation":"Genes Dev 1997 Apr 15;11(8):1008-22","abstract":"The fission yeast Sty1 MAP kinase is required for cell cycle control, initiation of sexual differentiation, and protection against cellular stress. Like the mammalian JNK/SAPK and p38/CSBP1 MAP kinases, Sty1 is activated by a range of environmental insults including osmotic stress, hydrogen peroxide, menadione, heat shock, and the protein synthesis inhibitor anisomycin. We have identified an upstream regulator that mediates activation of the Sty1 MAP kinase by multiple environmental stresses as the product of the mitotic catastrophe suppressor, mcs4. Mcs4 is structurally and functionally homologous to the budding yeast SSK1 response regulator, suggesting that the eukaryotic stress-activated MAP kinase pathway is controlled by a conserved two-component system. Mcs4 acts upstream of Wak1, a homolog of the SSK2 and SSK22 MEK kinases, which transmits the stress signal to the Wis1 MEK. We show that the Wis1 MEK is controlled by an additional pathway that is independent of both Mcs4 and the Wak1 MEK kinase. Furthermore, we demonstrate that Mcs4 is required for the correct timing of mitotic initiation by mechanisms both dependent and independent on Sty1, indicating that Mcs4 coordinately controls cell cycle progression with the cellular response to environmental stress.","authors":"Shieh JC, Wilkinson MG, Buck V, Morgan BA, Makino K, Millar JB","authors_abbrev":"Shieh JC et al.","pubmed_publication_date":"15 Apr 1997","pubmed_entrez_date":"1997-04-15","publication_year":"1997","canto_session_key":"ea7f33ab6887fe6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-08 07:49:52","canto_approved_date":"2026-02-04 11:30:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-12 15:06:50","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":60,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC409.07c","SPBC29B5.01","SPBC215.05","SPAC19D5.01","SPCC757.07c","SPCC18B5.03","SPAC24H6.05","SPAC9G1.02","SPAC24B11.06c","SPBC887.10"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2017-09-08"},{"uniquename":"PMID:25036832","title":"Anti-aging and anti-microbial effects of melleolide on various types of yeast.","citation":"Biosci Biotechnol Biochem 2014;78(3):455-7","abstract":"The chronological lifespan (CLS) of the budding yeast Saccharomyces cerevisiae is a model for the aging of post-mitotic cells in higher eukaryotes. In this study, we found that the sesquiterpene aryl ester melleolide expands the CLS of budding yeast. In contrast, melleolide compromised the CLS of the fission yeast Schizosaccharomyces pombe. This indicates that melleolide might have a potential anti-aging activity against some types of cell, and that it might be useful as a selective anti-fungal drug.","doi":"10.1080/09168451.2014.885826","authors":"Nakaya S, Kobori H, Sekiya A, Kawagishi H, Ushimaru T","authors_abbrev":"Nakaya S et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-07-19","publication_year":"2014","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2014-07-20 00:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27354705","title":"The S. pombe mRNA decapping complex recruits cofactors and an Edc1-like activator through a single dynamic surface.","citation":"RNA 2016 Sep;22(9):1360-72","abstract":"The removal of the 5' 7-methylguanosine mRNA cap structure (decapping) is a central step in the 5'-3' mRNA degradation pathway and is performed by the Dcp1:Dcp2 decapping complex. The activity of this complex is tightly regulated to prevent premature degradation of the transcript. Here, we establish that the aromatic groove of the EVH1 domain of Schizosaccharomyces pombe Dcp1 can interact with proline-rich sequences in the exonuclease Xrn1, the scaffolding protein Pat1, the helicase Dhh1, and the C-terminal disordered region of Dcp2. We show that this region of Dcp1 can also recruit a previously unidentified enhancer of decapping protein (Edc1) and solved the crystal structure of the complex. NMR relaxation dispersion experiments reveal that the Dcp1 binding site can adopt multiple conformations, thus providing the plasticity that is required to accommodate different ligands. We show that the activator Edc1 makes additional contacts with the regulatory domain of Dcp2 and that an activation motif in Edc1 increases the RNA affinity of Dcp1:Dcp2. Our data support a model where Edc1 stabilizes the RNA in the active site, which results in enhanced decapping rates. In summary, we show that multiple decapping factors, including the Dcp2 C-terminal region, compete with Edc1 for Dcp1 binding. Our data thus reveal a network of interactions that can fine-tune the catalytic activity of the decapping complex.","doi":"10.1261/rna.057315.116","authors":"Wurm JP, Overbeck J, Sprangers R","authors_abbrev":"Wurm JP et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-06-30","publication_year":"2016","canto_session_key":"970e7dfb32a1c6d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-06-09 06:34:18","canto_approved_date":"2023-06-09 06:34:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-08 13:54:35","canto_added_date":"2016-07-01 00:15:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.09c","YGL222C","HGNC:23158","SPBC3B9.21","SPBC776.09","SPAC19A8.12","SPBC19C2.05","HGNC:17278","YER035W","SPAC17A5.14"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2023-06-09","pdb_entries":[{"pdb_id":"5jp4","gene_chains":[{"gene_uniquename":"SPAC18G6.09c","chain":"B","position":"156-181"},{"gene_uniquename":"SPBC3B9.21","chain":"A","position":"1-127"}],"title":"Crystal structure of S. pombe Dcp1 in complex with the decapping enhancer EDC","entry_authors":"Wurm JP,Sprangers R","entry_authors_abbrev":"Wurm JP et al.","reference_uniquename":"PMID:27354705","experimental_method":"X-ray","resolution":"2.043"}]},{"uniquename":"PMID:12596864","title":"His-to-Asp phosphorelay circuitry for regulation of sexual development in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2002 Dec;66(12):2663-72","abstract":"The fission yeast Schizosaccharomyces pombe has three histidine kinases (Phk1/Mak2, Phk2/Mak3, and Phk3/Mak1), and two response regulators (Mcs4 and Prr1). The results of recent extensive studies on the S. pombe His-to-Asp phosphorelay circuitry suggested that it is involved in oxidative stress responses through the transcriptional regulation of several scavenger genes for toxic free radicals. The functions of these histidine kinases have not yet been fully characterized. Here we characterize a homothallic (h90) mutant lacking the genes for all the histidine kinases, with special reference to sexual development. Homothallic phk1/2/3delta cells underwent mating precociously in a nitrogen-deficient medium. Surprisingly, the mutant cells underwent mating even in a nitrogen-sufficient medium, under which conditions wild-type cells did so rarely if at all. Under anaerobic (or microaerobic) growth conditions, wild-type cells did not undergo sexual development even in a nitrogen-deficient medium, but the homothallic phk1/2/3delta cells mated efficiently. Oxidative reagents such as H2O2 induced sexual development in wild-type cells grown anaerobically. On the basis of these results, we propose the novel view that the S. pombe His-to-Asp phosphorelay, initiated by the Phk histidine kinases, is crucial for regulation of sexual development. This Phk-mediated signaling pathway is linked to the well-documented canonical pathway for induction of the sexual development, in that both converge at the initiation of meiosis through activation of ste11+, mam2+, and mei2+ transcription.","authors":"Nakamichi N, Yamada H, Aoyama K, Ohmiya R, Aiba H, Mizuno T","authors_abbrev":"Nakamichi N et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2003-02-25","publication_year":"2002","canto_session_key":"4e3227943350f291","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-08-04 14:50:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-15 17:27:30","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.14","SPCC74.06","SPAC1834.08","SPBC725.02","SPBC887.10","SPAC27E2.09"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-10-15"},{"uniquename":"PMID:32692737","title":"CRL4Cdt2 ubiquitin ligase regulates Dna2 and Rad16 (XPF) nucleases by targeting Pxd1 for degradation.","citation":"PLoS Genet 2020 Jul;16(7):e1008933","abstract":"Structure-specific endonucleases (SSEs) play key roles in DNA replication, recombination, and repair. SSEs must be tightly regulated to ensure genome stability but their regulatory mechanisms remain incompletely understood. Here, we show that in the fission yeast Schizosaccharomyces pombe, the activities of two SSEs, Dna2 and Rad16 (ortholog of human XPF), are temporally controlled during the cell cycle by the CRL4Cdt2 ubiquitin ligase. CRL4Cdt2 targets Pxd1, an inhibitor of Dna2 and an activator of Rad16, for degradation in S phase. The ubiquitination and degradation of Pxd1 is dependent on CRL4Cdt2, PCNA, and a PCNA-binding degron motif on Pxd1. CRL4Cdt2-mediated Pxd1 degradation prevents Pxd1 from interfering with the normal S-phase functions of Dna2. Moreover, Pxd1 degradation leads to a reduction of Rad16 nuclease activity in S phase, and restrains Rad16-mediated single-strand annealing, a hazardous pathway of repairing double-strand breaks. These results demonstrate a new role of the CRL4Cdt2 ubiquitin ligase in genome stability maintenance and shed new light on how SSE activities are regulated during the cell cycle.","doi":"10.1371/journal.pgen.1008933","authors":"Zhang JM, Zheng JX, Ding YH, Zhang XR, Suo F, Ren JY, Dong MQ, Du LL","authors_abbrev":"Zhang JM et al.","pubmed_publication_date":"Jul 2020","pubmed_entrez_date":"2020-07-22","publication_year":"2020","canto_session_key":"53e0b793e37b4408","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jia-Min Zhang","canto_first_approved_date":"2020-09-03 09:34:58","canto_approved_date":"2024-04-03 09:27:25","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-08-17 02:48:19","canto_added_date":"2020-07-23 00:15:05","annotation_curators":[{"name":"Jia-Min Zhang","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":35,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":7,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPAC17H9.19c","SPBC16D10.04c","SPCC970.01","SPAC29B12.03","SPBC887.14c","SPCC1322.02","SPAC17H9.10c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2020-09-03"},{"uniquename":"PMID:10427688","title":"Isolation and some properties of a novel killer toxin-like protein produced by Streptomyces sp. F-287.","citation":"Biosci Biotechnol Biochem 1999 Jun;63(6):1037-44","abstract":"A killer toxin-like protein was found in the culture supernatant of a strain isolated from soil. The strain was classified and designated as Streptomyces sp. F-287. The molecular weight of the purified killer toxin-like protein was estimated to be 9,500 by SDS-PAGE. The purified protein was heat stable (100 degrees C, 5 min), pH stable (pH 6.0-9.0, 60 degrees C, for 30 min), and had a relatively wide action spectra. The SKLP showed a cytocidal effect on both budding yeast, Saccharomyces cerevisiae W303 (IC50 = 15.6 micrograms/ml) and on fission yeast, Schizosaccharomyces pombe SP870 (IC50 = 20.0 micrograms/ml). The SKLP also caused morphological changes on some sensitive yeasts and filamentous fungi. These characteristics are apparently different from known killer toxins. These results suggest that this is a novel killer toxin-like protein from Streptomyces sp. strain F-287.","authors":"Hiraga K, Hayashi S, Kitazawa M, Oda K","authors_abbrev":"Hiraga K et al.","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-07-31","publication_year":"1999","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35111072","title":"Use of a Fission Yeast Platform to Identify and Characterize Small Molecule PDE Inhibitors.","citation":"Front Pharmacol 2021;12:833156","abstract":"Cyclic nucleotide phosphodiesterases (PDEs) have been proven to be targets for which highly selective and potent drugs can be developed. Mammalian genomes possess 21 genes whose products are pharmacologically grouped into 11 families; however related genes from pathogenic organisms display sufficient divergence from the mammalian homologs such that PDE inhibitors to these enzymes could be used to treat parasitic infections without acting on the related human PDEs. We have developed a platform for expressing cloned PDEs in the fission yeast  Schizosaccharomyces pombe , allowing for inexpensive, but robust screening for small molecule inhibitors that are cell permeable. Such compounds typically display the expected biological activity when tested in cell culture, including anti-inflammatory properties for PDE4 and PDE7 inhibitors. The genetic pliability of  S. pombe  also allows for molecular genetic screens to identify mutations in target PDE genes that confer some resistance to these inhibitors as a way of investigating the PDE-inhibitor interaction. This screening method is readily accessible to academic laboratories as it does not require the purification of large quantities of a target protein. This allows for the discovery and profiling of PDE inhibitors to treat inflammation or of inhibitors of targets such as pathogen PDEs for which there may not be a sufficient financial motivation for pharmaceutical companies to identify selective PDE inhibitors using more traditional  in vitro  enzyme-based screening methods.","doi":"10.3389/fphar.2021.833156","authors":"Hoffman CS","authors_abbrev":"Hoffman CS","pubmed_publication_date":"2021","pubmed_entrez_date":"2022-02-03","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-02-05 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19805578","title":"Genome-wide mapping of myosin protein-RNA networks suggests the existence of specialized protein production sites.","citation":"FASEB J 2010 Feb;24(2):479-84","abstract":"Motor proteins can organize posttranscriptional processes by transporting ribonucleoprotein complexes to specific locations. To investigate a possible role of myosin proteins in gene expression control, I have identified mRNAs associated with five myosin heavy chains in the fission yeast Schizosaccharomyces pombe, by purifying the proteins and identifying bound transcripts using DNA microarrays. Each myosin coimmunoprecipitated with 5-13 different mRNAs (approximately 0.1-0.2% of all genes), including those encoding four different myosin heavy chains. Moreover, one of the myosins (Myo1) interacted with mRNAs encoding components of the cortical actin cytoskeleton. These interactions were not observed in control immunoprecipitates. A myosin-specific chaperone (Rng3) that interacts cotranslationally with myosin mRNAs was essential for the association between myosin proteins and transcripts but not between Myo1 and other mRNAs. Finally, proteins encoded by the Myo1-associated mRNAs immunoprecipitated each other's transcripts, but not myosin mRNAs. These interactions suggest the existence of two distinct myosin-containing ribonucleoprotein complexes: those containing myosin mRNAs and those associated with Myo1. They are distinguished by their mRNA composition, requirement for the Rng3 chaperone and the presence of nonmyosin cytoskeletal proteins. I propose that these complexes represent specialized sites for the production of myosin proteins and the assembly of cytoskeletal components, respectively.","doi":"10.1096/fj.09-140335","authors":"Mata J","authors_abbrev":"Mata J","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2009-10-07","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1919.10c","SPAC4A8.05c","SPAC323.06c","SPBC2D10.14c","SPAC4F8.12c","SPBC146.13c","SPBC2G2.14","SPCC645.05c","SPAC4F8.13c","SPCC645.07","SPAC4F10.15c","SPAC13A11.03","SPAC10F6.08c"],"gene_count":13,"ltp_gene_count":13},{"uniquename":"PMID:17961508","title":"Inhibition of splicing and nuclear retention of pre-mRNA by spliceostatin A in fission yeast.","citation":"Biochem Biophys Res Commun 2007 Dec 21;364(3):573-7","abstract":"Nuclear retention of pre-mRNAs is tightly regulated by several security mechanisms that prevent pre-mRNA export into the cytoplasm. Recently, spliceostatin A, a methylated derivative of a potent antitumor microbial metabolite FR901464, was found to cause pre-mRNA accumulation and translation in mammalian cells. Here we report that spliceostatin A also inhibits splicing and nuclear retention of pre-mRNA in a fission yeast strain that lacks the multidrug resistance protein Pmd1. As observed in mammalian cells, spliceostatin A is bound to components of the SF3b complex in the spliceosome. Furthermore, overexpression of nup211, a homolog of Saccharomyces cerevisiae MLP1, suppresses translation of pre-mRNAs accumulated by spliceostatin A. These results suggest that the SF3b complex has a conserved role in pre-mRNA retention, which is independent of the Mlp1 function.","authors":"Lo CW, Kaida D, Nishimura S, Matsuyama A, Yashiroda Y, Taoka H, Ishigami K, Watanabe H, Nakajima H, Tani T, Horinouchi S, Yoshida M","authors_abbrev":"Lo CW et al.","pubmed_publication_date":"21 Dec 2007","pubmed_entrez_date":"2007-10-27","publication_year":"2007","canto_session_key":"ff37a04ae46f945b","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12963835","title":"Preventing DNA re-replication--divergent safeguards in yeast and metazoa.","citation":"Cell Cycle 2003;2(5):431-4","abstract":"Eukaryotes employ redundant mechanisms to limit the replication of genomic DNA to only once per cycle. These mechanisms prevent DNA re-replication by restricting the assembly of the pre-replication complex to the cell cycle stages of late mitosis and G1 phase so that the re-initiation of DNA replication cannot occur during S phase. Here we discuss the conserved yet divergent mechanisms of replication control employed in yeast and metazoan species, including a perspective on the newly uncovered role of the CUL-4 ubiquitin ligase as a central regulator of DNA replication in the nematode Caenorhabditis elegans.","authors":"Feng H, Kipreos ET","authors_abbrev":"Feng H et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-09-10","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC05879","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22291963","title":"Histone chaperone Asf1 plays an essential role in maintaining genomic stability in fission yeast.","citation":"PLoS One 2012;7(1):e30472","abstract":"The histone H3-H4 chaperone Asf1 is involved in chromatin assembly (or disassembly), histone exchange, regulation of transcription, and chromatin silencing in several organisms. To investigate the essential functions of Asf1 in Schizosaccharomyces pombe, asf1-ts mutants were constructed by random mutagenesis using PCR. One mutant (asf1-33(ts)) was mated with mutants in 77 different kinase genes to identify synthetic lethal combinations. The asf1-33 mutant required the DNA damage checkpoint factors Chk1 and Rad3 for its survival at the restrictive temperature. Chk1, but not Cds1, was phosphorylated in the asf1-33 mutant at the restrictive temperature, indicating that the DNA damage checkpoint was activated in the asf1-33 mutant. DNA damage occured in the asf1-33 mutant, with degradation of the chromosomal DNA observed through pulse-field gel electrophoresis and the formation of Rad22 foci. Sensitivity to micrococcal nuclease in the asf1-33 mutant was increased compared to the asf1(+) strain at the restrictive temperature, suggesting that asf1 mutations also caused a defect in overall chromatin structure. The Asf1-33 mutant protein was mislocalized and incapable of binding histones. Furthermore, histone H3 levels at the centromeric outer repeat region were decreased in the asf1-33 mutant and heterochromatin structure was impaired. Finally, sim3, which encodes a CenH3 histone chaperone, was identified as a strong suppressor of the asf1-33 mutant. Taken together, these results clearly indicate that Asf1 plays an essential role in maintaining genomic stability in S. pombe.","doi":"10.1371/journal.pone.0030472","authors":"Tanae K, Horiuchi T, Matsuo Y, Katayama S, Kawamukai M","authors_abbrev":"Tanae K et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-02-01","publication_year":"2012","canto_session_key":"b284d3aacd905379","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_first_approved_date":"2018-10-02 13:19:04","canto_approved_date":"2024-02-07 07:32:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-13 00:31:29","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.11c","SPAC2F3.15","SPBC11B10.09","SPBC530.14c","SPAC3C7.06c","SPBP35G2.05c","SPBC8D2.04","SPAC167.01","SPBC1778.10c","SPACUNK12.02c","SPAC15A10.13","SPBC16E9.13","SPAC22E12.14c","SPCC1259.13","SPAC1834.04","SPBC4F6.06","SPAC1006.09","SPAC1805.05","SPAC57A10.02","SPBC577.15c","SPAC22G7.08","SPBC216.05","SPCC663.05c","SPAC29A4.16","SPAC2C4.14c"],"gene_count":25,"ltp_gene_count":24,"approved_date":"2018-10-02"},{"uniquename":"PMID:30150414","title":"Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments.","citation":"Proc Natl Acad Sci U S A 2018 Sep 11;115(37):E8642-E8651","abstract":"We used fluorescence spectroscopy and EM to determine how binding of ATP, nucleation-promoting factors, actin monomers, and actin filaments changes the conformation of Arp2/3 complex during the process that nucleates an actin filament branch. We mutated subunits of  Schizosaccharomyces pombe  Arp2/3 complex for labeling with fluorescent dyes at either the C termini of Arp2 and Arp3 or ArpC1 and ArpC3. We measured Förster resonance energy transfer (FRET) efficiency (ET eff ) between the dyes in the presence of the various ligands. We also computed class averages from electron micrographs of negatively stained specimens. ATP binding made small conformational changes of the nucleotide-binding cleft of the Arp2 subunit. WASp-VCA, WASp-CA, and WASp-actin-VCA changed the ET eff  between the dyes on the Arp2 and Arp3 subunits much more than between dyes on ArpC1 and ArpC3. Ensemble FRET detected an additional structural change that brought ArpC1 and ArpC3 closer together when Arp2/3 complex bound actin filaments. VCA binding to Arp2/3 complex causes a conformational change that favors binding to the side of an actin filament, which allows further changes required to nucleate a daughter filament.","doi":"10.1073/pnas.1717594115","authors":"Espinoza-Sanchez S, Metskas LA, Chou SZ, Rhoades E, Pollard TD","authors_abbrev":"Espinoza-Sanchez S et al.","pubmed_publication_date":"11 Sep 2018","pubmed_entrez_date":"2018-08-29","publication_year":"2018","canto_session_key":"53e1b0748269e391","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-08-30 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14C8.06","SPBC1778.08c","SPAC630.03","SPAC11H11.06"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:2197066","title":"Controls of cell proliferation in yeast and animals.","citation":"Ciba Found Symp 1990;150:168-77; discussion 177-83","abstract":"Genetic studies using fission yeast (Schizosaccharomyces pombe) have identified a gene, cdc2, whose product (p34cdc2) is a protein kinase required for traversal of both the G1 and G2 cell cycle control points. Genetic complementation has been used to demonstrate that p34cdc2 homologues are functionally and structurally conserved in distantly related eukaryotes, and p34cdc2-related proteins are components of both maturation-promoting factor (MPF) and the M phase (growth-associated) histone H1 kinase. The p34cdc2 homologues of multicellular eukaryotes undergo potentially regulatory phosphorylation changes through the cell cycle. Phosphorylation on serine during late G1 is accompanied by a significant increase in p34cdc2 kinase activity which, by analogy with fission yeast, may betray a function related to control over entry into S phase. Phosphorylation on threonine and tyrosine in G2 precedes dephosphorylation of these residues during kinase hyperactivation and entry into mitosis. In addition, long-term control of expression of mammalian p34cdc2 homologues is likely to be exerted at the transcriptional level. These observations provide the framework of a universal model for the control of eukaryotic cell proliferation, in which the p34cdc2 protein kinase integrates multiple cues to signal the initiation of S phase and, subsequently, mitosis.","authors":"Norbury C, Nurse P","authors_abbrev":"Norbury C et al.","pubmed_publication_date":"1990","pubmed_entrez_date":"1990-01-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19903940","title":"Nutrition-minded cell cycle.","citation":"Sci Signal 2009 Nov 10;2(96):pe74","abstract":"For decades, the fission yeast Schizosaccharomyces pombe has been used as an excellent model with which to explore how cellular growth is coordinated with the division cycle, a yet-unanswered question in biology. New studies in this organism show that TOR (target of rapamycin) kinase and stress-responsive MAPK (mitogen-activated protein kinase) form a signaling pathway that readjusts the timing of mitotic onset in response to poor nutrient conditions. Nutritional environment appears to be translated into graded activity of the protein kinases that influence the activation of Cdc2, a cyclin-dependent kinase driving cell-cycle progression.","doi":"10.1126/scisignal.296pe74","authors":"Shiozaki K","authors_abbrev":"Shiozaki K","pubmed_publication_date":"10 Nov 2009","pubmed_entrez_date":"2009-11-12","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9055078","title":"Epigenetic inheritance of transcriptional silencing and switching competence in fission yeast.","citation":"Genetics 1997 Mar;145(3):685-96","abstract":"Epigenetic events allow the inheritance of phenotypic changes that are not caused by an alteration in DNA sequence. Here we characterize an epigenetic phenomenon occurring in the mating-type region of fission yeast. Cells of fission yeast switch between the P and M mating-type by interconverting their expressed mating-type cassette between two allelic forms, mat1-P and mat1-M. The switch results from gene conversions of mat1 by two silent cassettes, mat2-P and mat3-M, which are linked to each other and to mat1. GREWAL and KLAR observed that the ability to both switch mat1 and repress transcription near mat2-P and mat3-M was maintained epigenetically in a strain with an 8-kb deletion between mat2 and mat3. Using a strain very similar to theirs, we determined that interconversions between the switching- and silencing-proficient state and the switching and silencing-deficient state occurred less frequently than once per 1000 cell divisions. Although transcriptional silencing was alleviated by the 8-kb deletion, it was not abolished. We performed a mutant search and obtained a class of trans-acting mutations that displayed a strong cumulative effect with the 8-kb deletion. These mutations allow to assess the extent to which silencing is affected by the deletion and provide new insights on the redundancy of the silencing mechanism.","authors":"Thon G, Friis T","authors_abbrev":"Thon G et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_session_key":"e2652e0c0cecb1f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-06-12 18:20:41","canto_approved_date":"2024-06-12 18:20:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 14:19:28","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29B12.08","SPAC664.01c","SPBC1711.02"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2024-06-12"},{"uniquename":"PMID:34158470","title":"Inhibition of MRN activity by a telomere protein motif.","citation":"Nat Commun 2021 Jun 22;12(1):3856","abstract":"The MRN complex (MRX in Saccharomyces cerevisiae, made of Mre11, Rad50 and Nbs1/Xrs2) initiates double-stranded DNA break repair and activates the Tel1/ATM kinase in the DNA damage response. Telomeres counter both outcomes at chromosome ends, partly by keeping MRN-ATM in check. We show that MRX is disabled by telomeric protein Rif2 through an N-terminal motif (MIN, MRN/X-inhibitory motif). MIN executes suppression of Tel1, DNA end-resection and non-homologous end joining by binding the Rad50 N-terminal region. Our data suggest that MIN promotes a transition within MRX that is not conductive for endonuclease activity, DNA-end tethering or Tel1 kinase activation, highlighting an Achilles' heel in MRN, which we propose is also exploited by the RIF2 paralog ORC4 (Origin Recognition Complex 4) in Kluyveromyces lactis and the Schizosaccharomyces pombe telomeric factor Taz1, which is evolutionarily unrelated to Orc4/Rif2. This raises the possibility that analogous mechanisms might be deployed in other eukaryotes as well.","doi":"10.1038/s41467-021-24047-2","authors":"Khayat F, Cannavo E, Alshmery M, Foster WR, Chahwan C, Maddalena M, Smith C, Oliver AW, Watson AT, Carr AM, Cejka P, Bianchi A","authors_abbrev":"Khayat F et al.","pubmed_publication_date":"22 Jun 2021","pubmed_entrez_date":"2021-06-23","publication_year":"2021","canto_session_key":"03d2723ea379f156","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.07c","SPAC1556.01c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9858584","title":"Genetic evidence for Pak1 autoinhibition and its release by Cdc42.","citation":"Mol Cell Biol 1999 Jan;19(1):602-11","abstract":"Pak1 protein kinase of Schizosaccharomyces pombe, a member of the p21-GTPase-activated protein kinase (PAK) family, participates in signaling pathways including sexual differentiation and morphogenesis. The regulatory domain of PAK proteins is thought to inhibit the kinase catalytic domain, as truncation of this region renders kinases more active. Here we report the detection in the two-hybrid system of the interaction between Pak1 regulatory domain and the kinase catalytic domain. Pak1 catalytic domain binds to the same highly conserved region on the regulatory domain that binds Cdc42, a GTPase protein capable of activating Pak1. Two-hybrid, mutant, and genetic analyses indicated that this intramolecular interaction rendered the kinase in a closed and inactive configuration. We show that Cdc42 can induce an open configuration of Pak1. We propose that Cdc42 interaction disrupts the intramolecular interactions of Pak1, thereby releasing the kinase from autoinhibition.","authors":"Tu H, Wigler M","authors_abbrev":"Tu H et al.","pubmed_publication_date":"Jan 1999","pubmed_entrez_date":"1998-12-22","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03","SPBC1604.14c","SPBC1D7.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10805724","title":"Three yeast proteins related to the human candidate tumor suppressor p33(ING1) are associated with histone acetyltransferase activities.","citation":"Mol Cell Biol 2000 Jun;20(11):3807-16","abstract":"Three Saccharomyces cerevisiae proteins (Yng1/YOR064c, Yng2/YHR090c, and Pho23) and two Schizosaccharomyces pombe proteins (Png1/CAA15917 and Png2/CAA21250) share significant sequence identity with the human candidate tumor suppressor p33(ING1) in their C-terminal regions. The homologous regions contain PHD finger domains which have been implicated in chromatin-mediated transcriptional regulation. We show that GFP-Yng2, like human Ing1, is localized in the nucleus. Deletion of YNG2 results in several phenotypes, including an abnormal multibudded morphology, an inability to utilize nonfermentable carbon sources, heat shock sensitivity, slow growth, temperature sensitivity, and sensitivity to caffeine. These phenotypes are suppressed by expression of either human Ing1 or S. pombe Png1, suggesting that the yeast and human proteins are functionally conserved. Yng1- and Pho23-deficient cells also share some of these phenotypes. We demonstrated by yeast two-hybrid and coimmunoprecipitation tests that Yng2 interacts with Tra1, a component of histone acetyltransferase (HAT) complexes. We further demonstrated by coimmunoprecipitation that HA-Yng1, HA-Yng2, HA-Pho23, and HA-Ing1 are associated with HAT activities in yeast. Genetic and biochemical evidence indicate that the Yng2-associated HAT is Esa1, suggesting that Yng2 is a component of the NuA4 HAT complex. These studies suggest that the yeast Ing1-related proteins are involved in chromatin remodeling. They further suggest that these functions may be conserved in mammals and provide a possible mechanism for the human Ing1 candidate tumor suppressor.","authors":"Loewith R, Meijer M, Lees-Miller SP, Riabowol K, Young D","authors_abbrev":"Loewith R et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-05-11","publication_year":"2000","canto_session_key":"4d7eee8e1d716c2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-07 17:20:56","canto_approved_date":"2019-11-07 17:20:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-07 17:20:49","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1709.11c","SPAC3G9.08"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2019-11-07"},{"uniquename":"PMID:15805465","title":"Replication checkpoint kinase Cds1 regulates Mus81 to preserve genome integrity during replication stress.","citation":"Genes Dev 2005 Apr 15;19(8):919-32","abstract":"The replication checkpoint kinase Cds1 preserves genome integrity by stabilizing stalled replication forks. Cds1 targets substrates through its FHA domain. The Cds1 FHA domain interacts with Mus81, a subunit of the Mus81-Eme1 structure-specific endonuclease. We report here that Mus81 and Rhp51 are required for generating deletion mutations in fission yeast replication mutants that experience replication stress. A mutation in the Mus81 FHA-binding motif eliminates its Cds1-binding and Cds1-dependent phosphorylation. Furthermore, this mutation exacerbates the deletion mutator phenotype of a replication mutant, and induces a hyper-recombination phenotype in hydroxyurea-treated cells. In unperturbed cells, Mus81 associates with chromatin throughout S phase. In replication mutants grown at semipermissive temperature, Mus81 undergoes minor Cds1-dependent phosphorylation, remains chromatin-associated, generates deletion mutations, and maintains cell growth. Upon S-phase arrest by acute hydroxyurea treatment, Mus81 is not required for cell viability but is essential for recovery from replication fork collapse. Moreover, Mus81 undergoes extensive Cds1-dependent phosphorylation and dissociates from chromatin in hydroxyurea-arrested cells, thereby preventing it from cleaving stalled replication forks that could lead to fork breakage and chromosomal rearrangement. These results provide novel insights into how Cds1 regulates Mus81 accordingly when cells experience different replication stress to preserve genome integrity.","authors":"Kai M, Boddy MN, Russell P, Wang TS","authors_abbrev":"Kai M et al.","pubmed_publication_date":"15 Apr 2005","pubmed_entrez_date":"2005-04-05","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC4G3.05c","SPAPB1E7.06c","SPAC3H5.06c","SPAC644.14c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:10930468","title":"Analysis of mid1p, a protein required for placement of the cell division site, reveals a link between the nucleus and the cell surface in fission yeast.","citation":"Mol Biol Cell 2000 Aug;11(8):2757-73","abstract":"mid1 is required for the proper placement of the contractile actin ring for cytokinesis at a medial site overlying the nucleus. Here we find that mid1 protein (mid1p) shuttles between the nucleus and a cortical medial broad band during interphase and early mitosis. The position of this broad band, which overlies the nucleus, is linked to nuclear position even in cells with displaced or multiple nuclei. We identified and created mutations in an NLS and in two crm1-dependent NES sequences in mid1p. NES mutations caused mid1p accumulation in the nucleus and loss of function. An NLS mutations greatly reduced nuclear localization but did not perturb cytoplasmic localization or function. mid1p localization to the medial broad band was also not dependent on mid1p PH domain or microtubule and actin cytoskeletons. Overexpression of mid1p produced ectopic cell growth at this band during interphase and abnormal karmellae-like nuclear membrane structures. In plo1-1, mid1p formed a medial broad band but did not incorporate into a tight ring, suggesting that polo kinase plo1p is required for activation of mid1p function. Thus, the mid1p broad band defines a compartment at the medial cell surface, whose localization is linked to the position of the nucleus, and whose function may be to position the plane of cell division.","authors":"Paoletti A, Chang F","authors_abbrev":"Paoletti A et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2000-08-10","publication_year":"2000","canto_session_key":"977c41e138dc2e0d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-05 14:42:14","canto_approved_date":"2025-09-03 12:15:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-02 06:58:57","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPAC1805.17","SPAC23C11.16"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-03-05"},{"uniquename":"PMID:9762918","title":"The Pzh1 protein phosphatase and the Spm1 protein kinase are involved in the regulation of the plasma membrane H+-ATPase in fission yeast.","citation":"FEBS Lett 1998 Sep 18;435(2-3):241-4","abstract":"We have previously shown that the mutation of the Schizosaccharomyces pombe PPZ-like protein phosphatase encoded by the gene pzh1+ results in increased tolerance to sodium and in hypersensitivity to potassium ions. A similar phenotype has also been reported for deletants in the spm1/pmk1 gene, encoding a mitogen-activated protein (MAP) kinase. We have found that the sodium tolerance phenotype of pzh1 deletants is stronger than that of spm1 mutants, and both effects are additive. Therefore, most probably both gene products mediate different pathways on sodium tolerance. In our hands, mutation of the kinase does not alter the tolerance to potassium, but it yields cells more tolerant to magnesium ions. While in budding yeast the mutations are synthetically lethal, fission yeast cells lacking both the phosphatase and the kinase genes are viable. Interestingly, their ability to export H+ to the medium is greatly impaired (although not that of pzh1 or spm1 single mutants). We have observed that, although the amount of the H+-ATPase in the plasma membrane is not altered, the activity of the enzyme is lower than normal and cannot be induced by glucose. These observations suggest that the activity of the H+-ATPase in fission yeast might be regulated by phospho-dephosphorylation mechanisms that might involve the pzh1+ and spm1+ gene products.","authors":"Balcells L, Martín R, Ruiz MC, Gómez N, Ramos J, Ariño J","authors_abbrev":"Balcells L et al.","pubmed_publication_date":"18 Sep 1998","pubmed_entrez_date":"1998-10-08","publication_year":"1998","canto_session_key":"8950c84dfdf2cad2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-04-11 08:24:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-04-11 08:24:35","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.08","SPBC119.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-04-11"},{"uniquename":"PMID:34967420","title":"Genetic screen for suppression of transcriptional interference reveals fission yeast 14-3-3 protein Rad24 as an antagonist of precocious Pol2 transcription termination.","citation":"Nucleic Acids Res 2022 Jan 25;50(2):803-819","abstract":"Expression of fission yeast Pho1 acid phosphatase is repressed under phosphate-replete conditions by transcription of an upstream prt lncRNA that interferes with the pho1 mRNA promoter. lncRNA control of pho1 mRNA synthesis is influenced by inositol pyrophosphate (IPP) kinase Asp1, deletion of which results in pho1 hyper-repression. A forward genetic screen for ADS (Asp1 Deletion Suppressor) mutations identified the 14-3-3 protein Rad24 as a governor of phosphate homeostasis. Production of full-length interfering prt lncRNA was squelched in rad24Δ cells, concomitant with increased production of pho1 mRNA and increased Pho1 activity, while shorter precociously terminated non-interfering prt transcripts persisted. Epistasis analysis showed that pho1 de-repression by rad24Δ depends on: (i) 3'-processing and transcription termination factors CPF, Pin1, and Rhn1; and (ii) Threonine-4 of the Pol2 CTD. Combining rad24Δ with the IPP pyrophosphatase-dead asp1-H397A allele caused a severe synthetic growth defect that was ameliorated by loss-of-function mutations in CPF, Pin1, and Rhn1, and by CTD phospho-site mutations T4A and Y1F. Rad24 function in repressing pho1 was effaced by mutation of its phosphate-binding pocket. Our findings instate a new role for a 14-3-3 protein as an antagonist of precocious RNA 3'-processing/termination.","doi":"10.1093/nar/gkab1263","authors":"Garg A, Shuman S, Schwer B","authors_abbrev":"Garg A et al.","pubmed_publication_date":"25 Jan 2022","pubmed_entrez_date":"2021-12-30","publication_year":"2022","canto_session_key":"af39cc71da933c2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Angad Garg","canto_first_approved_date":"2022-10-26 13:56:57","canto_approved_date":"2023-09-16 13:31:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-10-20 17:53:04","canto_added_date":"2022-01-01 01:15:04","annotation_curators":[{"name":"Angad Garg","community_curator":true,"annotation_count":84,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1183.12","SPBC428.03c","SPAC8E11.02c","SPAC513.03","SPCC1795.06","SPBC28F2.12","SPAC27D7.03c","SPBC21D10.06c","SPAC13G6.14","SPAC19G12.17","SPAC824.04","SPBC337.03","SPCC1672.06c","SPAC1F7.07c","SPAC3F10.10c","SPBC359.06","SPBP4G3.02","SPAC1D4.06c","SPBP8B7.17c","SPBC8E4.12c","SPAC29A4.12c","SPBC4F6.09","SPBC1271.09","SPAC1F7.08","SPBC947.05c","SPBC3B9.11c","SPAC11E3.06","SPNCRNA.1712","SPAC3G9.04","SPCC16C4.03","SPAC6F12.05c","SPCC74.02c","SPBC776.02c","SPBC106.02c","SPAC343.12","SPCC188.12"],"gene_count":36,"ltp_gene_count":17,"approved_date":"2022-10-26"},{"uniquename":"PMID:33202882","title":"The Fission Yeast RNA-Binding Protein Meu5 Is Involved in Outer Forespore Membrane Breakdown during Spore Formation.","citation":"J Fungi (Basel) 2020 Nov 13;6(4)","abstract":"In  Schizosaccharomyces pombe , the spore wall confers strong resistance against external stress. During meiosis II, the double-layered intracellular forespore membrane (FSM) forms de novo and encapsulates the nucleus. Eventually, the inner FSM layer becomes the plasma membrane of the spore, while the outer layer breaks down. However, the molecular mechanism and biological significance of this membrane breakdown remain unknown. Here, by genetic investigation of an  S. pombe  mutant (E22) with normal prespore formation but abnormal spores, we showed that Meu5, an RNA-binding protein known to bind to and stabilize more than 80 transcripts, is involved in this process. We confirmed that the E22 mutant does not produce Meu5 protein, while overexpression of  meu5 +   in E22 restores the sporulation defect. Furthermore, electron microscopy revealed that the outer membrane of the FSM persisted in  meu5 ∆ spores. Investigation of the target genes of  meu5  +  showed that a mutant of  cyc1  +  encoding cytochrome  c  also showed a severe defect in outer FSM breakdown. Lastly, we determined that outer FSM breakdown occurs coincident with or after formation of the outermost Isp3 layer of the spore wall. Collectively, our data provide novel insights into the molecular mechanism of spore formation.","doi":"10.3390/jof6040284","authors":"Zhang B, Teraguchi E, Imada K, Tahara YO, Nakamura S, Miyata M, Kagiwada S, Nakamura T","authors_abbrev":"Zhang B et al.","pubmed_publication_date":"13 Nov 2020","pubmed_entrez_date":"2020-11-18","publication_year":"2020","canto_session_key":"7ac74c1d6b6f1521","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Bowen Zhang","canto_first_approved_date":"2021-01-21 16:10:44","canto_approved_date":"2021-01-21 16:10:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-01-12 06:25:49","canto_added_date":"2020-11-21 01:15:04","annotation_curators":[{"name":"Bowen Zhang","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1610.03c","SPCC191.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-01-21"},{"uniquename":"PMID:10438147","title":"DNA-induced conformational change of Gaf1, a novel GATA factor in Schizosaccharomyces pombe.","citation":"Biochem Cell Biol 1999;77(2):127-32","abstract":"A novel GATA factor in Schizosaccharomyces pombe, Gaf1, containing one zinc-finger motif was studied for conformational change that was induced by DNA-binding. Gaf1 was shown to bind to the upstream activation sequence of a gene in Saccharomyces cerevisiae containing GATA element by gel mobility shift assay. Circular dichroism spectra of Gaf1 indicated an increase of alpha-helix content of Gaf1 occurred upon binding to the upstream activation sequence. These results suggest that the binding of Gaf1 to the GATA element is required for the conformational change that may precede transactivation of the target gene(s).","authors":"Won M, Hoe KL, Cho YS, Song KB, Yoo HS","authors_abbrev":"Won M et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-08-07","publication_year":"1999","canto_session_key":"ae55f5308b1fdb21","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-07-31 14:47:00","canto_approved_date":"2022-02-02 14:07:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-24 07:17:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1902.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:41550769","title":"The MO25 protein Pmo25 functions in contractile ring stability and Sid2 localization during cytokinesis.","citation":"iScience 2026 Jan 16;29(1):114287","abstract":"Mouse protein-25 (MO25) family proteins are crucial in development and morphogenesis from plants to humans. The fission yeast MO25 protein Pmo25 is essential for cell polarity and division. However, how Pmo25 regulates cytokinesis remains largely unknown. Here, we found that the actomyosin contractile ring and septum formation were defective during cytokinesis in  pmo25  mutants. Pmo25 physically and genetically interacted with the myosin-II light chain Cdc4, which is essential for the contractile-ring assembly and function. Additionally,  pmo25  mutations had synthetic genetic interactions with all other tested mutations in contractile-ring proteins. Moreover, Pmo25 colocalized with the NDR kinase Sid2 and participated in its recruitment to the division plane. Furthermore, Pmo25 directly bound the Munc13/UNC-13 protein Ync13 and modulated the secretion of glucanase Eng1 to the division site for daughter-cell separation. Our data provide insight into how Pmo25 regulates cytokinesis and suggest that the conserved MO25 proteins can link various steps of cytokinesis.","doi":"10.1016/j.isci.2025.114287","authors":"Ye Y, Zhang S, Gregory JR, Osmani AH, Goodyear EG, Singh D, Wu JQ","authors_abbrev":"Ye Y et al.","pubmed_publication_date":"16 Jan 2026","pubmed_entrez_date":"2026-01-19","publication_year":"2026","canto_session_key":"bb5160fcda8eb4c3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-01-20 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18044988","title":"Mutation of RNA Pol III subunit rpc2/polr3b Leads to Deficiency of Subunit Rpc11 and disrupts zebrafish digestive development.","citation":"PLoS Biol 2007 Nov;5(11):e312","abstract":"The role of RNA polymerase III (Pol III) in developing vertebrates has not been examined. Here, we identify a causative mutation of the second largest Pol III subunit, polr3b, that disrupts digestive organ development in zebrafish slim jim (slj) mutants. The slj mutation is a splice-site substitution that causes deletion of a conserved tract of 41 amino acids in the Polr3b protein. Structural considerations predict that the slj Pol3rb deletion might impair its interaction with Polr3k, the ortholog of an essential yeast Pol III subunit, Rpc11, which promotes RNA cleavage and Pol III recycling. We engineered Schizosaccharomyces pombe to carry an Rpc2 deletion comparable to the slj mutation and found that the Pol III recovered from this rpc2-delta yeast had markedly reduced levels of Rpc11p. Remarkably, overexpression of cDNA encoding the zebrafish rpc11 ortholog, polr3k, rescued the exocrine defects in slj mutants, indicating that the slj phenotype is due to deficiency of Rpc11. These data show that functional interactions between Pol III subunits have been conserved during eukaryotic evolution and support the utility of zebrafish as a model vertebrate for analysis of Pol III function.","authors":"Yee NS, Gong W, Huang Y, Lorent K, Dolan AC, Maraia RJ, Pack M","authors_abbrev":"Yee NS et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-11-30","publication_year":"2007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22A12.05","SPAC4G9.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:24815688","title":"Does a shift to limited glucose activate checkpoint control in fission yeast?","citation":"FEBS Lett 2014 Aug 01;588(15):2373-8","abstract":"Here we review cell cycle control in the fission yeast, Schizosaccharomyces pombe, in response to an abrupt reduction of glucose concentration in culture media. S. pombe arrests cell cycle progression when transferred from media containing 2.0% glucose to media containing 0.1%. After a delay, S. pombe resumes cell division at a surprisingly fast rate, comparable to that observed in 2% glucose. We found that a number of genes, including zinc-finger transcription factor Scr1, CaMKK-like protein kinase Ssp1, and glucose transporter Ght5, enable rapid cell division in low glucose. In this article, we examine whether cell cycle checkpoint-like control operates during the delay and after resumption of cell division in limited-glucose. Using microarray analysis and genetic screening, we identified several candidate genes that may be involved in controlling this low-glucose adaptation.","doi":"10.1016/j.febslet.2014.04.047","authors":"Saitoh S, Yanagida M","authors_abbrev":"Saitoh S et al.","pubmed_publication_date":"01 Aug 2014","pubmed_entrez_date":"2014-05-13","publication_year":"2014","canto_session_key":"b5db93caaa51792d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shigeaki Saitoh","canto_approved_date":"2015-08-20 18:12:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-30 07:48:22","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Shigeaki Saitoh","community_curator":true,"annotation_count":6,"orcid":"0000-0001-5408-296X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPBC725.02","SPBC800.09","SPAPB1E7.02c","SPAC9E9.08","SPCC18B5.03"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-08-30"},{"uniquename":"PMID:23673619","title":"Spatial segregation of polarity factors into distinct cortical clusters is required for cell polarity control.","citation":"Nat Commun 2013;4:1834","abstract":"Cell polarity is regulated by evolutionarily conserved polarity factors whose precise higher-order organization at the cell cortex is largely unknown. Here we image frontally the cortex of live fission yeast cells using time-lapse and super-resolution microscopy. Interestingly, we find that polarity factors are organized in discrete cortical clusters resolvable to ~50-100 nm in size, which can form and become cortically enriched by oligomerization. We show that forced co-localization of the polarity factors Tea1 and Tea3 results in polarity defects, suggesting that the maintenance of both factors in distinct clusters is required for polarity. However, during mitosis, their co-localization increases, and Tea3 helps to retain the cortical localization of the Tea1 growth landmark in preparation for growth reactivation following mitosis. Thus, regulated spatial segregation of polarity factor clusters provides a means to spatio-temporally control cell polarity at the cell cortex. We observe similar clusters in Saccharomyces cerevisiae and Caenorhabditis elegans cells, indicating this could be a universal regulatory feature.","doi":"10.1038/ncomms2813","authors":"Dodgson J, Chessel A, Yamamoto M, Vaggi F, Cox S, Rosten E, Albrecht D, Geymonat M, Csikasz-Nagy A, Sato M, Carazo-Salas RE","authors_abbrev":"Dodgson J et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-05-16","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1223.06","SPBC1706.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU013296","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35108037","title":"Fission yeast paxillin contains two Cdc15 binding motifs for robust recruitment to the cytokinetic ring.","citation":"Mol Biol Cell 2022 Apr 01;33(4):br4","abstract":"The F-BAR protein Cdc15 mediates attachment of the cytokinetic ring (CR) to the plasma membrane and is essential for cytokinesis in  Schizosaccharomyces pombe.  While its N-terminal F-BAR domain is responsible for oligomerization and membrane binding, its C-terminal SH3 domain binds other partners at a distance from the membrane. We previously demonstrated that the essential cytokinetic formin Cdc12, through an N-terminal motif, directly binds the cytosolic face of the F-BAR domain. Here, we show that paxillin-like Pxl1, which is important for CR stability, contains a motif highly related to that in formin Cdc12, and also binds the Cdc15 F-BAR domain directly. Interestingly, Pxl1 has a second site for binding the Cdc15 SH3 domain. To understand the importance of these two Pxl1-Cdc15 interactions, we mapped and disrupted both. Disrupting the Pxl1-Cdc15 F-BAR domain interaction reduced Pxl1 levels in the CR, whereas disrupting Pxl1's interaction with the Cdc15 SH3 domain, did not. Unexpectedly, abolishing Pxl1-Cdc15 interaction greatly reduced but did not eliminate CR Pxl1 and did not significantly affect cytokinesis. These data point to another mechanism of Pxl1 CR recruitment and show that very little CR Pxl1 is sufficient for its cytokinetic function.","doi":"10.1091/mbc.E21-11-0560","authors":"Snider CE, Bhattacharjee R, Igarashi MG, Gould KL","authors_abbrev":"Snider CE et al.","pubmed_publication_date":"01 Apr 2022","pubmed_entrez_date":"2022-02-02","publication_year":"2022","canto_session_key":"3bfc9f7d307c2e12","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chloe Snider","canto_first_approved_date":"2022-02-15 17:22:50","canto_approved_date":"2023-03-14 18:03:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-02-15 20:46:42","canto_added_date":"2022-02-04 01:15:04","annotation_curators":[{"name":"Chloe Snider","community_curator":true,"annotation_count":70,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.03","SPCC645.05c","SPBP4H10.04","SPAC1F5.04c","SPAC20G8.05c","SPAC1782.09c","SPBC19G7.05c","SPBC4F6.12","SPAP8A3.08","SPAC4F8.13c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2022-02-15"},{"uniquename":"PMID:26645666","title":"Nitric oxide signaling and its role in oxidative stress response in Schizosaccharomyces pombe.","citation":"Nitric Oxide 2016 Jan 30;52:29-40","abstract":"In the fission yeast Schizosaccharomyces pombe, we found that the putative NO dioxygenase SPAC869.02c (named Yhb1) and the S-nitrosoglutathione reductase Fmd2 cooperatively reduced intracellular NO levels as NO-detoxification enzymes. Although both mRNA and protein levels were increased with exogenous NO, their expression patterns were different during growth phases. While treatment with an NO synthase inhibitor in the log phase abrogated both NO production and Yhb1 expression, induction of Fmd2 in the stationary phase was correlated with elevated mitochondrial respiratory chain (MRC) activity, confirmed by the fact that inhibition of MRC complex III led to a decrease in Fmd2 and NO levels. Moreover, NO was localized in the mitochondria in the stationary phase, suggesting that there are two distinctive types of NO signaling in S. pombe. For mitochondria, pretreatment with an NO donor rescued cell growth by repressing generation of reactive oxygen species (ROS) under oxidative stress. DNA microarray analysis revealed that exogenous NO contributes to tolerance to hydrogen peroxide (H2O2) by (i) inhibition of Fe(3+) to Fe(2+) conversion, (ii) upregulation of the H2O2-detoxifying enzymes, and (iii) downregulation of the MRC genes, suggesting that NO plays a pivotal role in the negative feedback system to regulate ROS levels in S. pombe.","doi":"10.1016/j.niox.2015.11.001","authors":"Astuti RI, Watanabe D, Takagi H","authors_abbrev":"Astuti RI et al.","pubmed_publication_date":"30 Jan 2016","pubmed_entrez_date":"2015-12-10","publication_year":"2016","canto_session_key":"81b6cf4212a4f077","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-02 10:00:43","canto_approved_date":"2018-03-02 10:00:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-03-02 10:00:31","canto_added_date":"2015-12-11 01:19:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC869.02c","SPCC13B11.04c","SPBC1198.01","SPBC1539.07c","SPAC1782.07"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2018-03-02"},{"uniquename":"PMID:21300781","title":"Psm3 acetylation on conserved lysine residues is dispensable for viability in fission yeast but contributes to Eso1-mediated sister chromatid cohesion by antagonizing Wpl1.","citation":"Mol Cell Biol 2011 Apr;31(8):1771-86","abstract":"In budding yeast and humans, cohesion establishment during S phase requires the acetyltransferase Eco1/Esco1-2, which acetylates the cohesin subunit Smc3 on two conserved lysine residues. Whether Smc3 is the sole Eco1/Esco1-2 effector and how Smc3 acetylation promotes cohesion are unknown. In fission yeast (Schizosaccharomyces pombe), as in humans, cohesin binding to G(1) chromosomes is dynamic and the unloading reaction is stimulated by Wpl1 (human ortholog, Wapl). During S phase, a subpopulation of cohesin becomes stably bound to chromatin in an Eso1 (fission yeast Eco1/Esco1-2)-dependent manner. Cohesin stabilization occurs unevenly along chromosomes. Cohesin remains largely labile at the rDNA repeats but binds mostly in the stable mode to pericentromere regions. This pattern is largely unchanged in eso1Δ wpl1Δ cells, and cohesion is unaffected, indicating that the main Eso1 role is counteracting Wpl1. A mutant of Psm3 (fission yeast Smc3) that mimics its acetylated state renders cohesin less sensitive to Wpl1-dependent unloading and partially bypasses the Eso1 requirement but cannot generate the stable mode of cohesin binding in the absence of Eso1. Conversely, nonacetylatable Psm3 reduces the stable cohesin fraction and affects cohesion in a Wpl1-dependent manner, but cells are viable. We propose that Psm3 acetylation contributes to Eso1 counteracting of Wpl1 to secure stable cohesin interaction with postreplicative chromosomes but that it is not the sole molecular event by which this occurs.","doi":"10.1128/MCB.01284-10","authors":"Feytout A, Vaur S, Genier S, Vazquez S, Javerzat JP","authors_abbrev":"Feytout A et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2011-02-09","publication_year":"2011","canto_session_key":"d445419299dddade","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jean-Paul Javerzat ","canto_first_approved_date":"2017-11-01 11:57:43","canto_approved_date":"2025-09-03 18:58:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-24 12:23:42","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":84,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jean-Paul Javerzat ","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAC110.02","SPAC10F6.09c","SPAC31A2.05c","SPBC16A3.11","SPBC428.17c","SPAC664.01c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-11-01"},{"uniquename":"PMID:25252312","title":"[Ash2, a subunit of histone H3K4 methyltransferase complex, is involved in the sporulation in Schizosaccharomyces pombe].","citation":"Yi Chuan 2014 Sep;36(9):943-51","abstract":"Schizosaccharomyces pombe undergoes meiosis instead of mitosis under conditions of nitrogen starvation and pheromone signalling, which results in conjugation and sporulation. During this progress, the pheromone-responsive MAPK(Mitogen-activated protein kinases) pathway plays an important role in regulating the conjuation and the transcriptional activation of genes required for meiosis. Spk1, a key component of MAPK pathway, activates Ste11 through protein phosphorylation and then induced the transcriptions of several genes requied for meiosis, including mei2(+), mam2(+) and map3(+). Methylation of histone H3K4 is involved in several important biological processes, including transcriptional activation and chromatin remodeling. However, its role in the sporualtion of fission yeast is poorly understood. Ash2 is a subunit of COMPASS, a conserved H3K4 methyltransferase complex. Sequence alignment analysis revealed that Ash2 in pombe shares two conserved domain with other homologues. Ash2 is localized in nucleus and contributes to methylation of H3K4. Deletion of ash2(+) resulted in a delay of sporulation and a substantial drop of sporulation efficiency. ChIP and qPCR analysis showed that deletion of ash2(+) caused a reduction of H3K4me2 level in the coding region of spk1(+), as well as a reduction of its mRNA level. Although the mRNA level of ste11(+) kept unchanged, the levels of Ste11-targetted genes, such as mei2(+), mam2(+) and map3(+), all reduced in ash2Δ cells. The results suggest that Ash2 regulates MAPK pathway and sporulation through H3K4 methylation. This might provide a new clue to elucidate the link between meiosis and epigenetic regulation.","doi":"10.3724/SP.J.1005.2014.0943","authors":"Wang W, Zhou H, Yu Y, Lv H","authors_abbrev":"Wang W et al.","pubmed_publication_date":"Sep 2014","pubmed_entrez_date":"2014-09-25","publication_year":"2014","canto_session_key":"6d1e8a0bc513a2f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-04 14:46:28","canto_approved_date":"2021-09-25 15:36:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-04 14:46:20","canto_added_date":"2014-09-26 00:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.10c","SPAC27D7.03c","SPCC306.04c","SPAC31G5.09c","SPBC13G1.08c","SPAC11H11.04"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2014-12-04"},{"uniquename":"PMID:12409464","title":"The fission yeast pfh1(+) gene encodes an essential 5' to 3' DNA helicase required for the completion of S-phase.","citation":"Nucleic Acids Res 2002 Nov 01;30(21):4728-39","abstract":"The Cdc24 protein plays an essential role in chromosomal DNA replication in the fission yeast Schizosaccharomyces pombe, most likely via its direct interaction with Dna2, a conserved endonuclease-helicase protein required for Okazaki fragment processing. To gain insights into Cdc24 function, we isolated cold-sensitive chromosomal suppressors of the temperature-sensitive cdc24-M38 allele. One of the complementation groups of such suppressors defined a novel gene, pfh1(+), encoding an 805 amino acid nuclear protein highly homologous to the Saccharomyces cerevisiae Pif1p and Rrm3p DNA helicase family proteins. The purified Pfh1 protein displayed single-stranded DNA-dependent ATPase activity as well as 5' to 3' DNA helicase activity in vitro. Reverse genetic analysis in S.pombe showed that helicase activity was essential for the function of the Pfh1 protein in vivo. Schizosaccharomyces pombe cells carrying the cold-sensitive pfh1-R20 allele underwent cell cycle arrest in late S/G2-phase of the cell cycle when shifted to the restrictive temperature. This arrest was dependent upon the presence of a functional late S/G2 DNA damage checkpoint, suggesting that Pfh1 is required for the completion of DNA replication. Furthermore, at their permissive temperature pfh1-R20 cells were highly sensitive to the DNA-alkylating agent methyl methanesulphonate, implying a further role for Pfh1 in the repair of DNA damage.","authors":"Tanaka H, Ryu GH, Seo YS, Tanaka K, Okayama H, MacNeill SA, Yuasa Y","authors_abbrev":"Tanaka H et al.","pubmed_publication_date":"01 Nov 2002","pubmed_entrez_date":"2002-11-01","publication_year":"2002","canto_session_key":"6eca82cdfddd5b82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-08-13 13:47:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-19 13:03:18","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8F11.07c","SPBC887.14c","SPAC1952.07"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-09-19"},{"uniquename":"PMID:11139492","title":"Crossing over is rarely associated with mitotic intragenic recombination in Schizosaccharomyces pombe.","citation":"Genetics 2001 Jan;157(1):63-77","abstract":"Chromosomal rearrangements can result from crossing over during ectopic homologous recombination between dispersed repetitive DNA. We have previously shown that meiotic ectopic recombination between artificially dispersed ade6 heteroalleles in the fission yeast Schizosaccharomyces pombe frequently results in chromosomal rearrangements. The same recombination substrates have been studied in mitotic recombination. Ectopic recombination rates in haploids were approximately 1-4 x 10(-6) recombinants per cell generation, similar to allelic recombination rates in diploids. In contrast, ectopic recombination rates in heterozygous diploids were 2.5-70 times lower than allelic recombination or ectopic recombination in haploids. These results suggest that diploid-specific factors inhibit ectopic recombination. Very few crossovers occurred in ade6 mitotic recombination, either allelic or ectopic. Allelic intragenic recombination was associated with 2% crossing over, and ectopic recombination between multiple different pairing partners showed 1-7% crossing over. These results contrast sharply with the 35-65% crossovers associated with meiotic ade6 recombination and suggest either differential control of resolution of recombination intermediates or alternative pathways of recombination in mitosis and meiosis.","authors":"Virgin JB, Bailey JP, Hasteh F, Neville J, Cole A, Tromp G","authors_abbrev":"Virgin JB et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-01-05","publication_year":"2001","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23481256","title":"Rules for the recognition of dilysine retrieval motifs by coatomer.","citation":"EMBO J 2013 Apr 03;32(7):926-37","abstract":"Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α-COP and β'-COP subunits and packaged into COPI-coated vesicles for Golgi-to-ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α-COP and β'-COP bound to a series of naturally occurring retrieval motifs-encompassing KKxx, KxKxx and non-canonical RKxx and viral KxHxx sequences. Binding experiments show that α-COP and β'-COP have generally the same specificity for KKxx and KxKxx, but only β'-COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side-chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C-terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non-lysine residues.","doi":"10.1038/emboj.2013.41","authors":"Ma W, Goldberg J","authors_abbrev":"Ma W et al.","pubmed_publication_date":"03 Apr 2013","pubmed_entrez_date":"2013-03-14","publication_year":"2013","canto_session_key":"052d674b68351b66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-12-15 12:48:45","canto_approved_date":"2026-01-07 13:26:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-14 20:36:04","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-12-15","pdb_entries":[{"pdb_id":"4j8b","gene_chains":[{"gene_uniquename":"SPBPJ4664.04","chain":"A","position":"1-327"}],"title":"Crystal structure of alpha-COP/Emp47p complex","entry_authors":"Ma W,Goldberg J","entry_authors_abbrev":"Ma W et al.","reference_uniquename":"PMID:23481256","experimental_method":"X-ray","resolution":"1.878"},{"pdb_id":"4j8g","gene_chains":[{"gene_uniquename":"SPBPJ4664.04","chain":"A/B","position":"1-327"}],"title":"Crystal structure of alpha-COP/E19 complex","entry_authors":"Ma W,Goldberg J","entry_authors_abbrev":"Ma W et al.","reference_uniquename":"PMID:23481256","experimental_method":"X-ray","resolution":"1.895"},{"pdb_id":"4j87","gene_chains":[{"gene_uniquename":"SPBPJ4664.04","chain":"A","position":"1-327"}],"title":"Crystal structure of alpha-COP","entry_authors":"Ma W,Goldberg J","entry_authors_abbrev":"Ma W et al.","reference_uniquename":"PMID:23481256","experimental_method":"X-ray","resolution":"1.67"}]},{"uniquename":"PMID:17360675","title":"Point mutations in TOR confer Rheb-independent growth in fission yeast and nutrient-independent mammalian TOR signaling in mammalian cells.","citation":"Proc Natl Acad Sci U S A 2007 Feb 27;104(9):3514-9","abstract":"Rheb is a unique member of the Ras superfamily GTP-binding proteins. We as well as others previously have shown that Rheb is a critical component of the TSC/TOR signaling pathway. In fission yeast, Rheb is encoded by the rhb1 gene. Rhb1p is essential for growth and directly interacts with Tor2p. In this article, we report identification of 22 single amino acid changes in the Tor2 protein that enable growth in the absence of Rhb1p. These mutants also exhibit decreased mating efficiency. Interestingly, the mutations are located in the C-terminal half of the Tor2 protein, clustering mainly within the FAT and kinase domains. We noted some differences in the effect of a mutation in the FAT domain (L1310P) and in the kinase domain (E2221K) on growth and mating. Although the Tor2p mutations bypass Rhb1p's requirement for growth, they are incapable of suppressing Rhb1p's requirement for resistance to stress and toxic amino acids, pointing to multiple functions of Rhb1p. In mammalian systems, we find that mammalian target of rapamycin (mTOR) carrying analogous mutations (L1460P or E2419K), although sensitive to rapamycin, exhibits constitutive activation even when the cells are starved for nutrients. These mutations do not show significant difference in their ability to form complexes with Raptor, Rictor, or mLST8. Furthermore, we present evidence that mutant mTOR can complex with wild-type mTOR and that this heterodimer is active in nutrient-starved cells.","authors":"Urano J, Sato T, Matsuo T, Otsubo Y, Yamamoto M, Tamanoi F","authors_abbrev":"Urano J et al.","pubmed_publication_date":"27 Feb 2007","pubmed_entrez_date":"2007-03-16","publication_year":"2007","canto_session_key":"b8af2bfd2bb974e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-05-03 13:02:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-27 14:14:45","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":40,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.16c","SPBC216.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-01-27"},{"uniquename":"PMID:2630562","title":"The first transition point of the mutant cdc2.33 in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1989 Dec;94 ( Pt 4):657-62","abstract":"We show that the first of the two transition points of cdc2.33, a mutant of Schizosaccharomyces pombe, exists in exponential phase cells. Using flow cytometry and a double-block experiment, we have measured the position of this transition point both in the single mutant and in the double mutant cdc2.33 wee1.6. In the single mutant, this point is in early G1. In the double mutant, however, this point is only delayed slightly, if at all, despite much larger delays in the S period and in the transition point of cdc10, another 'start' mutant. There is therefore a significant dissociation in the timing of what are thought to be two start events, and the first one appears not to be subject to a size control and to be associated with the completion of mitosis rather than the G1/S boundary.","authors":"Novak B, Mitchison JM","authors_abbrev":"Novak B et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013778","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR14677","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1271.05c","HGNC:28073","HGNC:25206","HGNC:25858"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9398669","title":"A WD repeat protein controls the cell cycle and differentiation by negatively regulating Cdc2/B-type cyclin complexes.","citation":"Mol Biol Cell 1997 Dec;8(12):2475-86","abstract":"In the fission yeast Schizosaccharomyces pombe, p34(cdc2) plays a central role controlling the cell cycle. We recently isolated a new gene named srw1(+), capable of encoding a WD repeat protein, as a multicopy suppressor of hyperactivated p34(cdc2). Cells lacking srw1(+) are sterile and defective in cell cycle controls. When starved for nitrogen source, they fail to effectively arrest in G1 and die of accelerated mitotic catastrophe if regulation of p34(cdc2)/Cdc13 by inhibitory tyrosine phosphorylation is compromised by partial inactivation of Wee1 kinase. Fertility is restored to the disruptant by deletion of Cig2 B-type cyclin or slight inactivation of p34(cdc2). srw1(+) shares functional similarity with rum1(+), having abilities to induce endoreplication and restore fertility to rum1 disruptants. In the srw1 disruptant, Cdc13 fails to be degraded when cells are starved for nitrogen. We conclude that Srw1 controls differentiation and cell cycling at least by negatively regulating Cig2- and Cdc13-associated p34(cdc2) and that one of its roles is to down-regulate the level of the mitotic cyclin particularly in nitrogen-poor environments.","authors":"Yamaguchi S, Murakami H, Okayama H","authors_abbrev":"Yamaguchi S et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1997-12-17","publication_year":"1997","canto_session_key":"9ef4b740616f8870","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-04-25 19:02:19","canto_approved_date":"2025-09-04 11:32:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-03 17:45:56","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC144.13c","SPBC11B10.09","SPAC1952.07","SPAC664.07c","SPAPB2B4.03","SPCC1259.13","SPAC821.08c","SPBC660.14","SPBC32F12.09","SPCC18B5.03","SPBC582.03"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2017-04-25"},{"uniquename":"PMID:20498706","title":"Tip1/CLIP-170 protein is required for correct chromosome poleward movement in fission yeast.","citation":"PLoS One 2010 May 13;5(5):e10634","abstract":"The plus-end microtubule binding proteins (+TIPs) play an important role in the regulation of microtubule stability and cell polarity during interphase. In S. pombe, the CLIP-170 like protein Tip1, together with the kinesin Tea2, moves along the microtubules towards their plus ends. Tip1 also requires the EB1 homolog Mal3 to localize to the microtubule tips. Given the requirement for Tip1 for microtubule stability, we have investigated its role during spindle morphogenesis and chromosome movement. Loss of Tip1 affects metaphase plate formation and leads to the activation of the spindle assembly checkpoint. In the absence of Tip1 we also observed the appearance of lagging chromosomes, which do not influence the normal rate of spindle elongation. Our results suggest that S. pombe Tip1/CLIP170 is directly or indirectly required for correct chromosome poleward movement independently of Mal3/EB1.","doi":"10.1371/journal.pone.0010634","authors":"Goldstone S, Reyes C, Gay G, Courthéoux T, Dubarry M, Tournier S, Gachet Y","authors_abbrev":"Goldstone S et al.","pubmed_publication_date":"13 May 2010","pubmed_entrez_date":"2010-05-26","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.12","SPAC6F6.08c","SPBC20F10.06","SPAC18G6.15","SPBC1604.20c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:9547260","title":"Cloning and characterization of a human DEAH-box RNA helicase, a functional homolog of fission yeast Cdc28/Prp8.","citation":"Nucleic Acids Res 1998 May 01;26(9):2063-8","abstract":"During the splicing process, spliceosomal snRNAs undergo numerous conformational rearrangements that appear to be catalyzed by proteins belonging to the DEAD/H-box superfamily of RNA helicases. We have cloned a new RNA helicase gene, designated DBP2 (DEAH-boxprotein), homologous to the Schizosaccaromyces pombe cdc28(+)/prp8(+) gene involved in pre-mRNA splicing and cell cycle progression. The full-length DBP2 contains 3400 nucleotides and codes for a protein of 1041 amino acids with a calculated mol. wt of 119 037 Da. Transfection experiments demonstrated that the GFP-DBP2 gene product, transiently expressed in HeLa cells, was localized in the nucleus. The DBP2 gene was mapped by FISH to the MHC region on human chromosome 6p21.3, a region where many malignant, genetic and autoimmune disease genes are linked. Because the expression of DBP2 gene in S.pombe prp8 mutant cells partially rescued the temperature-sensitive phenotype, we conclude that DBP2 is a functional human homolog of the fission yeast Cdc28/Prp8 protein.","authors":"Imamura O, Saiki K, Tani T, Ohshima Y, Sugawara M, Furuichi Y","authors_abbrev":"Imamura O et al.","pubmed_publication_date":"01 May 1998","pubmed_entrez_date":"1998-06-20","publication_year":"1998","canto_session_key":"0a44a215ad5ff0ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 16:29:58","canto_session_submitted_date":"2012-03-03 16:29:38","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.01"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:14735354","title":"Characterization of Schizosaccharomyces pombe mutants defective in vacuolar acidification and protein sorting.","citation":"Mol Genet Genomics 2004 Mar;271(2):197-207","abstract":"The vacuolar H+-ATPases (V-ATPases) are ATP-dependent proton pumps responsible for acidification of intracellular compartments in eukaryotic cells. To investigate the functional roles of the V-ATPase in Schizosaccharomyces pombe, the gene vma1 encoding subunit A or vma3 encoding subunit c was disrupted. Both deletion mutants lost the capacity for vacuolar acidification in vivo, and showed sensitivity to neutral pH or high concentrations of divalent cations including Ca2+. The delivery of FM4-64 to the vacuolar membrane and accumulation of Lucifer Yellow CH were strongly inhibited in the vma1 and vma3 mutants. Moreover, deletion of the S. pombe vma1+ or vma3+ gene resulted in pleiotropic phenotypes consistent with lack of vacuolar acidification, including the missorting of vacuolar carboxypeptidase Y, abnormal vacuole morphology, and mating defects. These findings suggest that V-ATPase is essential for endocytosis, ion and pH homeostasis, and for intracellular targeting of vacuolar proteins and vacuolar biogenesis in S. pombe.","authors":"Iwaki T, Goa T, Tanaka N, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-01-22","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B3.14","SPAC343.05"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:30181366","title":"Dysfunction of Prohibitin 2 Results in Reduced Susceptibility to Multiple Antifungal Drugs via Activation of the Oxidative Stress-Responsive Transcription Factor Pap1 in Fission Yeast.","citation":"Antimicrob Agents Chemother 2018 Nov;62(11)","abstract":"The fight against resistance to antifungal drugs requires a better understanding of the underlying cellular mechanisms. In order to gain insight into the mechanisms leading to antifungal drug resistance, we performed a genetic screen on a model organism,  Schizosaccharomyces pombe , to identify genes whose overexpression caused resistance to antifungal drugs, including clotrimazole and terbinafine. We identified the  phb2  +  gene, encoding a highly conserved mitochondrial protein, prohibitin (Phb2), as a novel determinant of reduced susceptibility to multiple antifungal drugs. Unexpectedly, deletion of the  phb2  +  gene also exhibited antifungal drug resistance. Overexpression of the  phb2  +  gene failed to cause drug resistance when the  pap1  +  gene, encoding an oxidative stress-responsive transcription factor, was deleted. Furthermore,  pap1 +   mRNA expression was significantly increased when the  phb2  +  gene was overexpressed or deleted. Importantly, either overexpression or deletion of the  phb2  +  gene stimulated the synthesis of NO and reactive oxygen species (ROS), as measured by the cell-permeant fluorescent NO probe DAF-FM DA (4-amino-5-methylamino-2',7'-difluorofluorescein diacetate) and the ROS probe DCFH-DA (2',7'-dichlorodihydrofluorescein diacetate), respectively. Taken together, these results suggest that Phb2 dysfunction results in reduced susceptibility to multiple antifungal drugs by increasing NO and ROS synthesis due to dysfunctional mitochondria, thereby activating the transcription factor Pap1 in fission yeast.","doi":"10.1128/AAC.00860-18","authors":"Liu Q, Yao F, Jiang G, Xu M, Chen S, Zhou L, Sakamoto N, Kuno T, Fang Y","authors_abbrev":"Liu Q et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-09-06","publication_year":"2018","canto_session_key":"405497aa07bd389b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yue Fang","canto_first_approved_date":"2019-08-13 14:08:46","canto_approved_date":"2019-08-13 14:08:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-08-07 05:03:59","canto_added_date":"2018-09-07 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":39,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Yue Fang","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC1782.06c","SPCC1322.16"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-08-13"},{"uniquename":"PMID:21447816","title":"Temporal and spatial regulation of targeting aurora B to the inner centromere.","citation":"Cold Spring Harb Symp Quant Biol 2010;75:419-23","abstract":"Successful partitioning of chromosomes in mitosis relies on the bipolar attachment of sister chromatids at metaphase. For this biorientation, the chromosomal passenger complex (CPC), composed of catalytic kinase Aurora B and regulatory components (INCENP, Survivin, and Borealin), must be localized at the center of paired kinetochores, the site called the inner centromere. It is largely unknown what defines the inner centromere and how the CPC is targeted to this site. Recent studies point out that the shugoshin protein (SGO), originally identified as a cohesin protector, also acts as a conserved centromeric adapter of the CPC. Phosphorylation of the CPC by Cdk1 promotes direct binding with shugoshin, thus explaining how the CPC is targeted to the centromere in a timely manner at prometaphase during the cell cycle. Moreover, the phosphorylation of histone H3 threonine 3 (H3-pT3) mediated by Haspin cooperates with Bub1-mediated H2A-S121 phosphorylation in targeting the CPC to the inner centromere. H3-pT3 promotes nucleosome binding of Survivin, whereas H2A-pS121 facilitates the binding of shugoshin. Haspin colocalizes with cohesin by associating with Pds5, a cohesin-binding protein, and Bub1 localizes at kinetochores. Thus, the inner centromere is defined by the spatial intersection of two histone marks mediated by cohesin- and kinetochore-associated kinases.","doi":"10.1101/sqb.2010.75.035","authors":"Watanabe Y","authors_abbrev":"Watanabe Y","pubmed_publication_date":"2010","pubmed_entrez_date":"2011-03-31","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8939675","title":"S-phase and DNA-damage checkpoints: a tale of two yeasts.","citation":"Curr Opin Cell Biol 1996 Dec;8(6):781-7","abstract":"Many genes required for the S-phase and DNA-damage checkpoints have been identified in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. This year many checkpoint genes have been sequenced, providing new information about the mechanism of checkpoint control. Several of these genes are conserved between the two yeasts but others are species-specific.","authors":"Stewart E, Enoch T","authors_abbrev":"Stewart E et al.","pubmed_publication_date":"Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16270032","title":"INSIG: a broadly conserved transmembrane chaperone for sterol-sensing domain proteins.","citation":"EMBO J 2005 Nov 16;24(22):3917-26","abstract":"INSIGs are proteins that underlie sterol regulation of the mammalian proteins SCAP (SREBP cleavage activating protein) and HMG-CoA reductase (HMGR). The INSIGs perform distinct tasks in the regulation of these effectors: they promote ER retention of SCAP, but ubiquitin-mediated degradation of HMGR. Two questions that arise from the discovery and study of INSIGs are: how do they perform these distinct tasks, and how general are the actions of INSIGs in biology? We now show that the yeast INSIG homologs NSG1 and NSG2 function to control the stability of yeast Hmg2p, the HMGR isozyme that undergoes regulated ubiquitination. Yeast Nsgs inhibit degradation of Hmg2p in a highly specific manner, by directly interacting with the sterol-sensing domain (SSD)-containing transmembrane region. Nsg1p functions naturally to limit degradation of Hmg2p when both proteins are at native levels, indicating a long-standing functional interplay between these two classes of proteins. One way to unify the known, disparate actions of INSIGs is to view them as known adaptations of a chaperone dedicated to SSD-containing client proteins.","authors":"Flury I, Garza R, Shearer A, Rosen J, Cronin S, Hampton RY","authors_abbrev":"Flury I et al.","pubmed_publication_date":"16 Nov 2005","pubmed_entrez_date":"2005-11-05","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC162.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AB016047","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7551732","title":"Physiological characterization of a cadmium-resistant mutant in the fission yeast Schizosaccharomyces pombe.","citation":"Microbiol Res 1995 Sep;150(3):233-7","abstract":"After treatment of the wild-type strain 975 h+ with N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) mutants able to grow on YEP-medium containing 15 mM CdCl2 were isolated. Mutant R17 showed a specific resistance to Cd, but no increased tolerance to Pb(NO3)2, CuSO4 or ZnCl2. No higher content of Cd-binding phytochelatins could be detected, but the mutant accumulated lower levels of Cd than the corresponding wild-type. No change, however, was observed in the accumulation of Cu. Under the influence of Cd, the respiratory activity of mutant R 17 is reduced less than in the wild-type. The mechanism of resistance could be an increased secretion or a decreased uptake of Cd.","authors":"Wunderlich C, Zhao Q, Zimmermann M, Wolf K","authors_abbrev":"Wunderlich C et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB089499","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25580577","title":"Tetrameric Ctp1 coordinates DNA binding and DNA bridging in DNA double-strand-break repair.","citation":"Nat Struct Mol Biol 2015 Feb;22(2):158-66","abstract":"Ctp1 (also known as CtIP or Sae2) collaborates with Mre11-Rad50-Nbs1 to initiate repair of DNA double-strand breaks (DSBs), but its functions remain enigmatic. We report that tetrameric Schizosaccharomyces pombe Ctp1 contains multivalent DNA-binding and DNA-bridging activities. Through structural and biophysical analyses of the Ctp1 tetramer, we define the salient features of Ctp1 architecture: an N-terminal interlocking tetrameric helical dimer-of-dimers (THDD) domain and a central intrinsically disordered region (IDR) linked to C-terminal 'RHR' DNA-interaction motifs. The THDD, IDR and RHR are required for Ctp1 DNA-bridging activity in vitro, and both the THDD and RHR are required for efficient DSB repair in S. pombe. Our results establish non-nucleolytic roles of Ctp1 in binding and coordination of DSB-repair intermediates and suggest that ablation of human CtIP DNA binding by truncating mutations underlie the CtIP-linked Seckel and Jawad syndromes.","doi":"10.1038/nsmb.2945","authors":"Andres SN, Appel CD, Westmoreland JW, Williams JS, Nguyen Y, Robertson PD, Resnick MA, Williams RS","authors_abbrev":"Andres SN et al.","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2015-01-13","publication_year":"2015","canto_session_key":"48be31dcce9039d3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-04-20 13:51:50","canto_approved_date":"2021-10-01 20:46:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-04 12:55:34","canto_added_date":"2015-01-14 01:15:58","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC543.03c","SPBC29A10.05","SPCC338.08"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-04-20","pdb_entries":[{"pdb_id":"4x01","gene_chains":[{"gene_uniquename":"SPCC338.08","chain":"A/B/C/D/E/F/G/H","position":"5-60"}],"title":"S. pombe Ctp1 tetramerization domain","entry_authors":"Andres SN,Williams RS","entry_authors_abbrev":"Andres SN et al.","reference_uniquename":"PMID:25580577","experimental_method":"X-ray","resolution":"2.201"}]},{"uniquename":"PMID:17426133","title":"The checkpoint clamp, Rad9-Rad1-Hus1 complex, preferentially stimulates the activity of apurinic/apyrimidinic endonuclease 1 and DNA polymerase beta in long patch base excision repair.","citation":"Nucleic Acids Res 2007;35(8):2596-608","abstract":"Growing evidence suggests that the Rad9-Rad1-Hus1 complex (the 9-1-1 complex), besides its functions in DNA damage sensing and signaling pathways, plays also a direct role in various DNA repair processes. Recent studies have demonstrated that the 9-1-1 complex physically and functionally interacts with several components of the base excision repair (BER) machinery namely DNA polymerase beta (Pol beta), flap endonuclease 1 (Fen 1), DNA ligase I (Lig I) and the MutY homologue of Schizosaccharomyces pombe. In this work, we found for the first time that the 9-1-1 complex interacts in vitro and in vivo with the apurinic/apyrimidinic endonuclease 1 (APE 1), an early component of BER, and can stimulate its AP-endonuclease activity. Moreover, we show that the 9-1-1 complex possesses a stimulatory effect on long patch base excision repair (LP-BER) reconstituted in vitro. The enhancement of LP-BER activity is due to the specific stimulation of the two early components of the repair machinery, namely APE 1 and Pol beta, suggesting a hierarchy of interactions between the 9-1-1 complex and the BER proteins acting in the repairosome. Overall, our results indicate that the 9-1-1 complex is directly involved in LP-BER, thus providing a possible link between DNA damage checkpoints and BER.","authors":"Gembka A, Toueille M, Smirnova E, Poltz R, Ferrari E, Villani G, Hübscher U","authors_abbrev":"Gembka A et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-04-12","publication_year":"2007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1921.05","SPAC664.07c","SPAC20G4.04c","SPAC1952.07"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:37463585","title":"The fission yeast cell size control system integrates pathways measuring cell surface area, volume, and time.","citation":"Curr Biol 2023 Aug 21;33(16):3312-3324.e7","abstract":"Eukaryotic cells tightly control their size, but the relevant aspect of size is unknown in most cases. Fission yeast divide at a threshold cell surface area (SA) due, in part, to the protein kinase Cdr2. We find that fission yeast cells only divide by SA under a size threshold. Mutants that divide at a larger size shift to volume-based divisions. Diploid cells divide at a larger size than haploid cells do, but they maintain SA-based divisions, and this indicates that the size threshold for changing from surface-area-based to volume-based control is set by ploidy. Within this size control system, we found that the mitotic activator Cdc25 accumulates like a volume-based sizer molecule, whereas the mitotic cyclin Cdc13 accumulates in the nucleus as a timer. We propose an integrated model for cell size control based on multiple signaling pathways that report on distinct aspects of cell size and growth, including cell SA (Cdr2), cell volume (Cdc25), and time (Cdc13). Combined modeling and experiments show how this system can generate both sizer- and adder-like properties.","doi":"10.1016/j.cub.2023.06.054","authors":"Miller KE, Vargas-Garcia C, Singh A, Moseley JB","authors_abbrev":"Miller KE et al.","pubmed_publication_date":"21 Aug 2023","pubmed_entrez_date":"2023-07-18","publication_year":"2023","canto_session_key":"509050b0fadf3da1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-07-20 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.03","SPAC24H6.05","SPAC57A10.02"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"EMBL:AU013904","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12733640","title":"RNA interference is required for normal centromere function in fission yeast.","citation":"Chromosome Res 2003;11(2):137-46","abstract":"In plants, animals and fungi, active centromeres are associated with arrays of repetitive DNA sequences. The outer repeats at fission yeast (Schizosaccharomyces pombe) centromeres are heterochromatic and are required for the assembly of an active centromere. Components of the RNA interference (RNAi) machinery process transcripts derived from these repeats and mediate the formation of silent chromatin. A subfragment of the repeat (dg) is known to induce silencing of marker genes at euchromatic sites and is required for centromere formation. We show that the RNAi components, Argonaute (Ago1), Dicer (Dcr1) and RNA-dependent RNA polymerase (Rdp1), are required to maintain silencing, lysine 9 methylation of histone H3 and association of Swi6 via this dg ectopic silencer. Deletion of Ago1, Dcr1 or Rdp1 disrupts chromosome segregation leading to a high incidence of lagging chromosomes on late anaphase spindles and sensitivity to a microtubule poison. Analysis of dg transcription indicates that csp mutants, previously shown to abrogate centromere silencing and chromosome segregation, are also defective in the regulation of non-coding centromeric RNAs. In addition, histone H3 lysine 9 methylation at, and recruitment of Swi6 and cohesin to, centromeric repeats is disrupted in these mutants. Thus the formation of silent chromatin on dg repeats and the development of a fully functional centromere is dependent on RNAi.","authors":"Volpe T, Schramke V, Hamilton GL, White SA, Teng G, Martienssen RA, Allshire RC","authors_abbrev":"Volpe T et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-05-08","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009518","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR10957","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YPL161C","SPCC1494.03","HGNC:9859"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15645504","title":"Pro-oxidant action of phloxine B on fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2005 Jan 30;22(2):91-7","abstract":"A Schizosaccharomyces pombe mutant deficient in Cu,Zn-superoxide dismutase (sod1 mutant) was hypersensitive to phloxine B, which is used as a food-colouring agent and also to distinguish diploid strains of Sz. pombe from haploid strains, under illumination with light. The pro-oxidant nature of phloxine B was confirmed biochemically. The carbonyl content of proteins (which represents protein oxidation) increased, and the reduced form of glutathione was transiently decreased by phloxine B treatment under illumination with light. When cells were treated with phloxine B under light, carbonyl content of proteins in the sod1 mutant was greater than that in the wild-type and amount of glutathione was much decreased in the sod1 mutant compared with the wild-type. Genes induced by oxidative stress were induced by phloxine B under illumination with light and some were induced by phloxine B without light.","authors":"Mutoh N, Kawabata M, Nakagawa CW, Kitajima S","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"30 Jan 2005","pubmed_entrez_date":"2005-01-13","publication_year":"2005","canto_session_key":"e5f825600d6309c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-22 08:09:54","canto_approved_date":"2022-09-22 08:09:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-18 18:40:30","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC757.07c","SPAC23A1.03","SPAC821.10c","SPBC32F12.03c"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2022-09-22"},{"uniquename":"PMID:17212653","title":"Participation of XPB/Ptr8p, a component of TFIIH, in nucleocytoplasmic transport of mRNA in fission yeast.","citation":"Genes Cells 2007 Jan;12(1):35-47","abstract":"To identify novel factors involved in nuclear mRNA export in Schizosaccharomyces pombe, we isolated and characterized the ptr8(+) gene, mutation of which causes nuclear accumulation of poly (A)(+) RNA. The ptr8(+) gene encodes an S. pombe homologue of human XPB, a component of TFIIH involved in nucleotide excision repair (NER) and transcription. A temperature-sensitive mutant of ptr8(+) (ptr8-1) was highly sensitive to UV irradiation, as are human XPB cells. Northern blot analysis demonstrated that the amount of total poly (A)(+) mRNAs does not decrease significantly at the nonpermissive temperature in ptr8-1 cells, whereas a pulse-labeling assay using (35)S-methionine showed that protein synthesis decreases rapidly after incubation of cells at the nonpermissive temperature, suggesting that ptr8-1 cells have a defect in nuclear mRNA export. In Saccharomyces cerevisiae, a mutation in the SSL2 gene encoding a homologue of Ptr8p also causes a block of mRNA export at the nonpermissive temperature. In addition, expression of human XPB in ptr8-1 cells rescued the ts phenotype and the mRNA export defects, suggesting that human XPB may also play a role in mRNA export. Furthermore, we revealed a functional interaction between Ptr8p and Tho2p, a component of the TREX complex involved in mRNA export. These results suggest that XPB/Ptr8p plays roles not only in NER and transcription, but also plays a conserved role in mRNA export.","authors":"Mizuki F, Namiki T, Sato H, Furukawa H, Matsusaka T, Ohshima Y, Ishibashi R, Andoh T, Tani T","authors_abbrev":"Mizuki F et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2007-01-11","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1D4.14","SPAC17A5.06"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:10667200","title":"Trichostatin and leptomycin. Inhibition of histone deacetylation and signal-dependent nuclear export.","citation":"Ann N Y Acad Sci 1999;886:23-36","abstract":"Trichostatin A (TSA), an inhibitor of the eukaryotic cell cycle and an inducer of morphological reversion of transformed cells, inhibits histone deacetylase (HDAC) at nanomolar concentrations. Recently, trapoxin, oxamflatin, and FR901228, antitumor agents structurally unrelated to TSA, were found to be potent HDAC inhibitors. These inhibitors activate expression of p21Waf1 and 16INK4A in a p53-independent manner. Changes in the expression of these cell cycle regulators by an increase in histone acetylation may be responsible for cell cycle arrest and antitumor activity by HDAC inhibitors. The target molecule of leptomycin B (LMB), a potent antitumor agent, was genetically and biochemically identified as CRM1, a protein reported as being required for chromosome structure control. We showed that CRM1 was a receptor for the nuclear export signal (NES) and that LMB inhibited nuclear export of proteins. Using LMB, we identified a novel NES in fission yeast transcription factor Pap1, the function of which is abolished by oxidative stress in a manner conserved in eukaryotes.","authors":"Yoshida M, Horinouchi S","authors_abbrev":"Yoshida M et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"2000-02-10","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36045211","title":"Detecting Cell Cycle Stage and Progression in Fission Yeast, Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2022;2579:235-246","abstract":"We have previously described methods to synchronize cultures of fission yeast, Schizosaccharomyces pombe. In this chapter, we provide methods to detect cell cycle stage in cells and populations of S. pombe. These protocols used fixed samples. First, we describe sample preparation for flow cytometry of bulk DNA content. This technique allows users to monitor progression of DNA replication and detect any perturbation during the synthesis (S) phase of the cell cycle. Second, we describe methods to stain nuclei and septa of fixed yeast cells, and monitor proportions of cell cycle stages within cultures. Together, these methods provide the ability to compare cell cycle progression or delay between cultures, making use of the powerful molecular genetics tool that is S. pombe.","doi":"10.1007/978-1-0716-2736-5_18","authors":"Kianfard Z, Cheung K, Rappaport D, Magalage SP, Sabatinos SA","authors_abbrev":"Kianfard Z et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-08-31","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-09-03 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33782714","title":"Wake-up alarm: virtual time-lapse gene expression landscape illuminates mechanisms underlying dormancy breaking of germinating spores.","citation":"Curr Genet 2021 Aug;67(4):519-534","abstract":"Dormancy breaking is a common physiological phenomenon that is shared by eukaryotes. Germination of spores in fungi is one of the most representative cases of dormancy breaking. Understanding the mechanisms of spore germination is therefore fundamental to basic studies on the control of cell proliferation and differentiation, as well as agricultural applications and medical investigation of fungal pathogenesis. In fission yeast, spores are generated as a consequence of sexual differentiation under nutrient starvation, remaining dormant until further nourishment, but little is known about how dormant spores germinate in response to environmental change. In a breakthrough, methods for single-cell-based gene expression profiling have recently been introduced. Several mRNA expression profiles were assembled from single spore cells during dormancy or germination. Single-cell RNA-seq profiles were aligned sequentially according to their similarities. The alignment of transcriptomes visualised how gene expression varies over time upon dormancy breaking. In this review, we revisit knowledge from previous studies on germination, select candidate genes that may be involved in germination, and query their expression from the temporal transcriptomic dataset so that studies on S. pombe germination can be extended further.","doi":"10.1007/s00294-021-01177-0","authors":"Tsuyuzaki H, Ujiie R, Sato M","authors_abbrev":"Tsuyuzaki H et al.","pubmed_publication_date":"Aug 2021","pubmed_entrez_date":"2021-03-30","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-04-01 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3077931","title":"Stem cells: a problem in asymmetry.","citation":"J Cell Sci Suppl 1988;10:1-9","abstract":"The special property of stem cells is that their development is asymmetric. They give rise both to cells that are identical to themselves and to cells that are different. The mechanism that provides this asymmetry may be intrinsic or extrinsic. Such mechanisms are considered within the context of other systems where asymmetric development occurs. The specification of mating types in yeast provides a clear example of a stem cell system generated intrinsically. In fission yeast it appears that the asymmetry is due to chromosomal differences: this is the only known mechanism for intrinsic asymmetry. While there is good evidence for intrinsic asymmetry in both plants and invertebrates--particularly the nematode--the mechanism is not known. In insects and vertebrates there is no well established example of intrinsic asymmetry if one excludes asymmetric cytoplasmic localization during cleavage of the egg. Asymmetry is thus due to environmental influences. Stem cell systems are usually well structured and the cell's behaviour seems to be position-dependent. This is well established for the stem cells of hydra. By contrast it is claimed that the mammalian haemopoietic system is generated by an intrinsic, asymmetric, probabilistic mechanism--the validity of this view is questioned.","authors":"Wolpert L","authors_abbrev":"Wolpert L","pubmed_publication_date":"1988","pubmed_entrez_date":"1988-01-01","publication_year":"1988","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084836","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.24"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34147496","title":"Regulation of inorganic polyphosphate is required for proper vacuolar proteolysis in fission yeast.","citation":"J Biol Chem 2021 Jul;297(1):100891","abstract":"Regulation of cellular proliferation and quiescence is a central issue in biology that has been studied using model unicellular eukaryotes, such as the fission yeast Schizosaccharomyces pombe. We previously reported that the ubiquitin/proteasome pathway and autophagy are essential to maintain quiescence induced by nitrogen deprivation in S. pombe; however, specific ubiquitin ligases that maintain quiescence are not fully understood. Here we investigated the SPX-RING-type ubiquitin ligase Pqr1, identified as required for quiescence in a genetic screen. Pqr1 is found to be crucial for vacuolar proteolysis, the final step of autophagy, through proper regulation of phosphate and its polymer polyphosphate. Pqr1 restricts phosphate uptake into the cell through ubiquitination and subsequent degradation of phosphate transporters on plasma membranes. We hypothesized that Pqr1 may act as the central regulator for phosphate control in S. pombe, through the function of the SPX domain involved in phosphate sensing. Deletion of pqr1 +  resulted in hyperaccumulation of intracellular phosphate and polyphosphate and in improper autophagy-dependent proteolysis under conditions of nitrogen starvation. Polyphosphate hyperaccumulation in pqr1 + -deficient cells was mediated by the polyphosphate synthase VTC complex in vacuoles. Simultaneous deletion of VTC complex subunits rescued Pqr1 mutant phenotypes, including defects in proteolysis and loss of viability during quiescence. We conclude that excess polyphosphate may interfere with proteolysis in vacuoles by mechanisms that as yet remain unknown. The present results demonstrate a connection between polyphosphate metabolism and vacuolar functions for proper autophagy-dependent proteolysis, and we propose that polyphosphate homeostasis contributes to maintenance of cellular viability during quiescence.","doi":"10.1016/j.jbc.2021.100891","authors":"Sawada N, Ueno S, Takeda K","authors_abbrev":"Sawada N et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-06-20","publication_year":"2021","canto_session_key":"8f9a11dd49d50293","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kojiro Takeda","canto_first_approved_date":"2021-07-06 16:28:12","canto_approved_date":"2025-12-21 16:45:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-07-16 10:43:07","canto_added_date":"2021-06-23 00:15:04","annotation_curators":[{"name":"Kojiro Takeda","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.05c","SPCC1322.14c","SPCC2H8.02","SPBC4B4.10c","SPBC8E4.01c","SPBC1683.01","SPAC23D3.12","SPAC4F10.07c","SPAC6B12.07c","SPBC3B9.06c","SPBP8B7.24c","SPBC3B8.04c","SPAC14C4.11","SPAC19G12.10c"],"gene_count":14,"ltp_gene_count":10,"approved_date":"2021-07-06"},{"uniquename":"PMID:28777780","title":"Coupling TOR to the Cell Cycle by the Greatwall-Endosulfine-PP2A-B55 Pathway.","citation":"Biomolecules 2017 Aug 04;7(3)","abstract":"Cell growth and division are two processes tightly coupled in proliferating cells. While Target of Rapamycin (TOR) is the master regulator of growth, the cell cycle is dictated by the activity of the cyclin-dependent kinases (CDKs). A long-standing question in cell biology is how these processes may be connected. Recent work has highlighted that regulating the phosphatases that revert CDK phosphorylations is as important as regulating the CDKs for cell cycle progression. At mitosis, maintaining a low level of protein phosphatase 2A (PP2A)-B55 activity is essential for CDK substrates to achieve the correct level of phosphorylation. The conserved Greatwall-Endosulfine pathway has been shown to be required for PP2A-B55 inhibition at mitosis in yeasts and multicellular organisms. Interestingly, in yeasts, the Greatwall-Endosulfine pathway is negatively regulated by TOR Complex 1 (TORC1). Moreover, Greatwall-Endosulfine activation upon TORC1 inhibition has been shown to regulate the progression of the cell cycle at different points: the G1 phase in budding yeast, the G2/M transition and the differentiation response in fission yeast, and the entry into quiescence in both budding and fission yeasts. In this review, we discuss the recent findings on how the Greatwall-Endosulfine pathway may provide a connection between cell growth and the cell cycle machinery.","doi":"10.3390/biom7030059","authors":"Pérez-Hidalgo L, Moreno S","authors_abbrev":"Pérez-Hidalgo L et al.","pubmed_publication_date":"04 Aug 2017","pubmed_entrez_date":"2017-08-05","publication_year":"2017","canto_session_key":"ade4bbd6d86365e4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-08-06 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30282034","title":"Elongation/Termination Factor Exchange Mediated by PP1 Phosphatase Orchestrates Transcription Termination.","citation":"Cell Rep 2018 Oct 02;25(1):259-269.e5","abstract":"Termination of RNA polymerase II (Pol II) transcription is a key step that is important for 3' end formation of functional mRNA, mRNA release, and Pol II recycling. Even so, the underlying termination mechanism is not yet understood. Here, we demonstrate that the conserved and essential termination factor Seb1 is found on Pol II near the end of the RNA exit channel and the Rpb4/7 stalk. Furthermore, the Seb1 interaction surface with Pol II largely overlaps with that of the elongation factor Spt5. Notably, Seb1 co-transcriptional recruitment is dependent on Spt5 dephosphorylation by the conserved PP1 phosphatase Dis2, which also dephosphorylates threonine 4 within the Pol II heptad repeated C-terminal domain. We propose that Dis2 orchestrates the transition from elongation to termination phase during the transcription cycle by mediating elongation to termination factor exchange and dephosphorylation of Pol II C-terminal domain.","doi":"10.1016/j.celrep.2018.09.007","authors":"Kecman T, Kuś K, Heo DH, Duckett K, Birot A, Liberatori S, Mohammed S, Geis-Asteggiante L, Robinson CV, Vasiljeva L","authors_abbrev":"Kecman T et al.","pubmed_publication_date":"02 Oct 2018","pubmed_entrez_date":"2018-10-04","publication_year":"2018","canto_session_key":"acd89b47e1b47f21","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tea Kecman","canto_first_approved_date":"2020-12-01 14:13:13","canto_approved_date":"2024-02-28 16:23:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-22 14:22:42","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tea Kecman","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC31H12.05c","SPAC23G3.01","SPAC23C4.19","SPACUNK4.06c","SPAC23C4.15","SPBC28F2.12","SPCC1442.10c","SPAC222.09","SPBC776.02c","SPBC19C2.03","SPBC337.14"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2020-12-01"},{"uniquename":"PMID:40825586","title":"Fission yeast Rad54 prevents intergenerational buildup of Rad51 aggregates in proliferating cells.","citation":"Life Sci Alliance 2025 Nov;8(11)","abstract":"Homologous recombination is central to the maintenance of genome stability. Using fission yeast, we found that mutation of the  rad54  gene leads to robust Rad51 accumulation in vegetatively growing cells. By developing a protocol to track Rad51 in live yeast cells, we traced the origin and fate of Rad51 aggregates formed in  rad54  mutants. Our observations strongly suggest that DNA breaks arising in late S phase act as the primary initiators of Rad51 accumulation. Rad51 initially appears as foci during late S phase, which continue to enlarge throughout the G2 phase. These Rad51 accumulations frequently persist into M phase and are distributed along with chromosomes into daughter cells. The inherited Rad51 mass in daughter cells continues to grow, forming robust Rad51 aggregates that are often associated with cell cycle arrest. Thus, the primary role of Rad54 in vegetative fission yeast cells is to facilitate the repair of DNA breaks arising in late S phase. The intergenerational accumulation of Rad51 aggregates in  rad54  mutants reveals a novel mechanism through which defective homologous recombination drives genome instability.","doi":"10.26508/lsa.202503252","authors":"Taniguchi G, May AI, Iwasaki H, Tsubouchi H","authors_abbrev":"Taniguchi G et al.","pubmed_publication_date":"Nov 2025","pubmed_entrez_date":"2025-08-18","publication_year":"2025","canto_session_key":"15929e21dd969776","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-08-20 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8074660","title":"Molecular cloning and sequence analysis of two novel fission yeast casein kinase-1 isoforms.","citation":"Biochem Biophys Res Commun 1994 Aug 30;203(1):231-6","abstract":"The cDNAs for two casein kinase-1 homologs, hhp1 and hhp2, have been isolated from Schizosaccharomyces pombe and characterized. Their corresponding genes reside on chromosomes II and I, respectively, and encode approximately 42-46 kDa proteins that are related structurally to the HRR25 gene product of budding yeast. On the basis of multiple sequence alignment, the CK1 family appears to consist of three main branches. We predict that the branch containing the hhp genes encodes nuclear kinases involved in the regulation of DNA metabolism.","authors":"Kearney PH, Ebert M, Kuret J","authors_abbrev":"Kearney PH et al.","pubmed_publication_date":"30 Aug 1994","pubmed_entrez_date":"1994-08-30","publication_year":"1994","canto_session_key":"87754e1bfa311bdf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 22:03:15","canto_approved_date":"2018-12-22 22:03:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 22:03:08","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:11027266","title":"Evidence for splice site pairing via intron definition in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2000 Nov;20(21):7955-70","abstract":"Schizosaccharomyces pombe pre-mRNAs are generally multi-intronic and share certain features with pre-mRNAs from Drosophila melanogaster, in which initial splice site pairing can occur via either exon or intron definition. Here, we present three lines of evidence suggesting that, despite these similarities, fission yeast splicing is most likely restricted to intron definition. First, mutating either or both splice sites flanking an internal exon in the S. pombe cdc2 gene produced almost exclusively intron retention, in contrast to the exon skipping observed in vertebrates. Second, we were unable to induce skipping of the internal microexon in fission yeast cgs2, whereas the default splicing pathway excludes extremely small exons in mammals. Because nearly quantitative removal of the downstream intron in cgs2 could be achieved by expanding the microexon, we propose that its retention is due to steric occlusion. Third, several cryptic 5' junctions in the second intron of fission yeast cdc2 are located within the intron, in contrast to their generally exonic locations in metazoa. The effects of expanding and contracting this intron are as predicted by intron definition; in fact, even highly deviant 5' junctions can compete effectively with the standard 5' splice site if they are closer to the 3' splicing signals. Taken together, our data suggest that pairing of splice sites in S. pombe most likely occurs exclusively across introns in a manner that favors excision of the smallest segment possible.","authors":"Romfo CM, Alvarez CJ, van Heeckeren WJ, Webb CJ, Wise JA","authors_abbrev":"Romfo CM et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-10-12","publication_year":"2000","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17612531","title":"RNA-binding protein Csx1 is phosphorylated by LAMMER kinase, Lkh1, in response to oxidative stress in Schizosaccharomyces pombe.","citation":"FEBS Lett 2007 Jul 24;581(18):3473-8","abstract":"Recent studies have shown that global gene expression during oxidative stress in Schizosaccharomyces pombe is regulated by stress-induced activation and binding of Csx1 to atf1(+) mRNA. However, the kinase responsible for the activation of Csx1 has not been identified. Here, we describe, for the first time, that Csx1 is phosphorylated by S. pombe LAMMER kinase, Lkh1, under oxidative conditions and that the stress-activated binding of the Csx1 to the atf1(+) mRNA was also affected by Lkh1 and Spc1. These data indicate that concerted actions of Spc1 and Lkh1 are required for the activation of Csx1 during oxidative condition in the fission yeast S. pombe.","authors":"Kang WH, Park YD, Hwang JS, Park HM","authors_abbrev":"Kang WH et al.","pubmed_publication_date":"24 Jul 2007","pubmed_entrez_date":"2007-07-07","publication_year":"2007","canto_session_key":"91e29bfaa0076845","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-08 02:56:11","canto_approved_date":"2020-11-16 18:35:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-14 16:47:34","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC17A2.09c","SPAC1D4.11c","SPAC24B11.06c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-12-08"},{"uniquename":"PMID:15236961","title":"The Schizosaccharomyces pombe open promoter bubble: mammalian-like arrangement and properties.","citation":"J Mol Biol 2004 Jul 23;340(5):981-9","abstract":"The fission yeast Schizosaccharomyces pombe is often used as a genetic system to model processes that apply to higher cells. Here S.pombe was used to study promoter DNA opening and transcription initiation by RNA polymerase II. The melted region within the adh promoter is about 20 bp in size and has the start site near its center. This arrangement is similar to that at the AdML promoter but different from that in Saccharomyces cerevisiae. Although expression of human TFIIB shifts the start site to the nearby human position, it does not change the location of the bubble. The start site shift is directed by the C terminus of human TFIIB, in contrast to expectations from S.cerevisiae. The creation of the bubble requires the ATPase motifs of XPB. Overall, the data show that promoter melting and initiation in fission yeast is much more similar to humans than to budding yeast.","authors":"Choi WS, Lin YC, Gralla JD","authors_abbrev":"Choi WS et al.","pubmed_publication_date":"23 Jul 2004","pubmed_entrez_date":"2004-07-09","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11463848","title":"The elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELL-induced leukemogenesis.","citation":"Mol Cell Biol 2001 Aug;21(16):5678-87","abstract":"The MLL-ELL chimeric gene is the product of the (11;19)(q23p13.1) translocation associated with de novo and therapy-related acute myeloid leukemias (AML). ELL is an RNA polymerase II elongation factor that interacts with the recently identified EAF1 (ELL associated factor 1) protein. EAF1 contains a limited region of homology with the transcriptional activation domains of three other genes fused to MLL in leukemias, AF4, LAF4, and AF5q31. Using an in vitro transformation assay of retrovirally transduced myeloid progenitors, we conducted a structure-function analysis of MLL-ELL. Whereas the elongation domain of ELL was dispensable, the EAF1 interaction domain of ELL was critical to the immortalizing properties of MLL-ELL in vitro. To confirm these results in vivo, we transplanted mice with bone marrow transduced with MLL fused to the minimal EAF1 interaction domain of ELL. These mice all developed AML, with a longer latency than mice transplanted with the wild-type MLL-ELL fusion. Based on these results, we generated a heterologous MLL-EAF1 fusion gene and analyzed its transforming potential. Strikingly, we found that MLL-EAF1 immortalized myeloid progenitors in the same manner as that of MLL-ELL. Furthermore, transplantation of bone marrow transduced with MLL-EAF1 induced AML with a shorter latency than mice transplanted with the MLL-ELL fusion. Taken together, these results indicate that the leukemic activity of MLL-ELL requires the EAF1 interaction domain of ELL, suggesting that the recruitment by MLL of a transactivation domain similar to that in EAF1 or the AF4/LAF4/AF5q31 family may be a critical common feature of multiple 11q23 translocations. In addition, these studies support a critical role for MLL partner genes and their protein-protein interactions in 11q23 leukemogenesis.","authors":"Luo RT, Lavau C, Du C, Simone F, Polak PE, Kawamata S, Thirman MJ","authors_abbrev":"Luo RT et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-07-21","publication_year":"2001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP23A10.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR22741","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15A10.16","HGNC:25428","HGNC:29506"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:39547223","title":"STK19 drives transcription-coupled repair by stimulating repair complex stability, RNA Pol II ubiquitylation, and TFIIH recruitment.","citation":"Mol Cell 2024 Dec 19;84(24):4740-4757.e12","abstract":"Transcription-coupled nucleotide excision repair (TC-NER) efficiently eliminates DNA damage that impedes gene transcription by RNA polymerase II (RNA Pol II). TC-NER is initiated by the recognition of lesion-stalled RNA Pol II by CSB, which recruits the CRL4 CSA  ubiquitin ligase and UVSSA. RNA Pol II ubiquitylation at RPB1-K1268 by CRL4 CSA  serves as a critical TC-NER checkpoint, governing RNA Pol II stability and initiating DNA damage excision by TFIIH recruitment. However, the precise regulatory mechanisms of CRL4 CSA  activity and TFIIH recruitment remain elusive. Here, we reveal human serine/threonine-protein kinase 19 (STK19) as a TC-NER factor, which is essential for correct DNA damage removal and subsequent transcription restart. Cryogenic electron microscopy (cryo-EM) studies demonstrate that STK19 is an integral part of the RNA Pol II-TC-NER complex, bridging CSA, UVSSA, RNA Pol II, and downstream DNA. STK19 stimulates TC-NER complex stability and CRL4 CSA  activity, resulting in efficient RNA Pol II ubiquitylation and correct UVSSA and TFIIH binding. These findings underscore the crucial role of STK19 as a core TC-NER component.","doi":"10.1016/j.molcel.2024.10.030","authors":"Ramadhin AR, Lee SH, Zhou D, Salmazo A, Gonzalo-Hansen C, van Sluis M, Blom CMA, Janssens RC, Raams A, Dekkers D, Bezstarosti K, Slade D, Vermeulen W, Pines A, Demmers JAA, Bernecky C, Sixma TK, Marteijn JA","authors_abbrev":"Ramadhin AR et al.","pubmed_publication_date":"19 Dec 2024","pubmed_entrez_date":"2024-11-15","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1834.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:39316607","title":"The conserved protein adaptors CALM/AP180 and FCHo1/2 cooperatively recruit Eps15 to promote the initiation of clathrin-mediated endocytosis in yeast.","citation":"PLoS Biol 2024 Sep 24;22(9):e3002833","abstract":"Clathrin-mediated endocytosis (CME) is a critical trafficking process that begins when an elaborate endocytic protein network is established at the plasma membrane. Interaction of early endocytic proteins with anionic phospholipids and/or cargo has been suggested to trigger CME initiation. However, the exact mechanism by which CME sites are initiated has not been fully elucidated. In the budding yeast Saccharomyces cerevisiae, higher levels of anionic phospholipids and cargo molecules exist in the newly formed daughter cell compared to the levels in the mother cell during polarized growth. Taking advantage of this asymmetry, we quantitatively compared CME proteins in S. cerevisiae mother versus daughter cells, observing differences in the dynamics and composition of key endocytic proteins. Our results show that CME site initiation occurs preferentially on regions of the plasma membrane with a relatively higher density of endocytic cargo and/or acidic phospholipids. Furthermore, our combined live cell-imaging and yeast genetics analysis provided evidence for a molecular mechanism in which CME sites are initiated when Yap1801 and Yap1802 (yeast CALM/AP180) and Syp1 (yeast FCHo1/2) coordinate with anionic phospholipids and cargo molecules to trigger Ede1 (yeast Eps15)-centric CME initiation complex assembly at the plasma membrane.","doi":"10.1371/journal.pbio.3002833","authors":"Sun Y, Yeam A, Kuo J, Iwamoto Y, Hu G, Drubin DG","authors_abbrev":"Sun Y et al.","pubmed_publication_date":"24 Sep 2024","pubmed_entrez_date":"2024-09-24","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4C3.06","SPBC800.10c","SPBC19F8.03c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:11854406","title":"Fission yeast Rad26 is a regulatory subunit of the Rad3 checkpoint kinase.","citation":"Mol Biol Cell 2002 Feb;13(2):480-92","abstract":"Fission yeast Rad3 is a member of a family of phosphoinositide 3-kinase -related kinases required for the maintenance of genomic stability in all eukaryotic cells. In fission yeast, Rad3 regulates the cell cycle arrest and recovery activities associated with the G2/M checkpoint. We have developed an assay that directly measures Rad3 kinase activity in cells expressing physiological levels of the protein. Using the assay, we demonstrate directly that Rad3 kinase activity is stimulated by checkpoint signals. Of the five other G2/M checkpoint proteins (Hus1, Rad1, Rad9, Rad17, and Rad26), only Rad26 was required for Rad3 kinase activity. Because Rad26 has previously been shown to interact constitutively with Rad3, our results demonstrate that Rad26 is a regulatory subunit, and Rad3 is the catalytic subunit, of the Rad3/Rad26 kinase complex. Analysis of Rad26/Rad3 kinase activation in rad26.T12, a mutant that is proficient for cell cycle arrest, but defective in recovery, suggests that these two responses to checkpoint signals require quantitatively different levels of kinase activity from the Rad3/Rad26 complex.","authors":"Wolkow TD, Enoch T","authors_abbrev":"Wolkow TD et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-02-21","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18368919","title":"The G2/M transition in eukaryotes.","citation":"SEB Exp Biol Ser 2008;59:81-98","abstract":"","authors":"Francis D","authors_abbrev":"Francis D","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-03-29","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10921876","title":"APC(ste9/srw1) promotes degradation of mitotic cyclins in G(1) and is inhibited by cdc2 phosphorylation.","citation":"EMBO J 2000 Aug 01;19(15):3945-55","abstract":"Fission yeast ste9/srw1 is a WD-repeat protein highly homologous to budding yeast Hct1/Cdh1 and Drosophila Fizzy-related that are involved in activating APC/C (anaphase-promoting complex/cyclosome). We show that APC(ste9/srw1) specifically promotes the degradation of mitotic cyclins cdc13 and cig1 but not the S-phase cyclin cig2. APC(ste9/srw1) is not necessary for the proteolysis of cdc13 and cig1 that occurs at the metaphase-anaphase transition but it is absolutely required for their degradation in G(1). Therefore, we propose that the main role of APC(ste9/srw1) is to promote degradation of mitotic cyclins when cells need to delay or arrest the cell cycle in G(1). We also show that ste9/srw1 is negatively regulated by cdc2-dependent protein phosphorylation. In G(1), when cdc2-cyclin kinase activity is low, unphosphorylated ste9/srw1 interacts with APC/C. In the rest of the cell cycle, phosphorylation of ste9/srw1 by cdc2-cyclin complexes both triggers proteolysis of ste9/srw1 and causes its dissociation from the APC/C. This mechanism provides a molecular switch to prevent inactivation of cdc2 in G(2) and early mitosis and to allow its inactivation in G(1).","authors":"Blanco MA, Sánchez-Díaz A, de Prada JM, Moreno S","authors_abbrev":"Blanco MA et al.","pubmed_publication_date":"01 Aug 2000","pubmed_entrez_date":"2000-08-02","publication_year":"2000","canto_session_key":"47e7d9844090c3e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-04-27 12:30:47","canto_approved_date":"2023-05-10 06:25:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-12 22:46:43","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4E9.02","SPAPB2B4.03","SPAC144.13c","SPAC6F12.15c","SPBC582.03","SPBC32F12.09","SPBC11B10.09"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2017-04-27"},{"uniquename":"PMID:6179956","title":"Dependency relations between events in mitosis in Schizosaccharomyces pombe.","citation":"J Cell Sci 1982 Jun;55:383-402","abstract":"","authors":"Fantes PA","authors_abbrev":"Fantes PA","pubmed_publication_date":"Jun 1982","pubmed_entrez_date":"1982-06-01","publication_year":"1982","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16800891","title":"A general method for the unbiased improvement of solution NMR structures by the use of related X-ray data, the AUREMOL-ISIC algorithm.","citation":"BMC Struct Biol 2006 Jun 26;6:14","abstract":"Rapid and accurate three-dimensional structure determination of biological macromolecules is mandatory to keep up with the vast progress made in the identification of primary sequence information. During the last few years the amount of data deposited in the protein data bank has substantially increased providing additional information for novel structure determination projects. The key question is how to combine the available database information with the experimental data of the current project ensuring that only relevant information is used and a correct structural bias is produced. For this purpose a novel fully automated algorithm based on Bayesian reasoning has been developed. It allows the combination of structural information from different sources in a consistent way to obtain high quality structures with a limited set of experimental data. The new ISIC (Intelligent Structural Information Combination) algorithm is part of the larger AUREMOL software package.\nOur new approach was successfully tested on the improvement of the solution NMR structures of the Ras-binding domain of Byr2 from Schizosaccharomyces pombe, the Ras-binding domain of RalGDS from human calculated from a limited set of NMR data, and the immunoglobulin binding domain from protein G from Streptococcus by their corresponding X-ray structures. In all test cases clearly improved structures were obtained. The largest danger in using data from other sources is a possible bias towards the added structure. In the worst case instead of a refined target structure the structure from the additional source is essentially reproduced. We could clearly show that the ISIC algorithm treats these difficulties properly.\nIn summary, we present a novel fully automated method to combine strongly coupled knowledge from different sources. The combination with validation tools such as the calculation of NMR R-factors strengthens the impact of the method considerably since the improvement of the structures can be assessed quantitatively. The ISIC method can be applied to a large number of similar problems where the quality of the obtained three-dimensional structures is limited by the available experimental data like the improvement of large NMR structures calculated from sparse experimental data or the refinement of low resolution X-ray structures. Also structures may be refined using other available structural information such as homology models.","authors":"Brunner K, Gronwald W, Trenner JM, Neidig KP, Kalbitzer HR","authors_abbrev":"Brunner K et al.","pubmed_publication_date":"26 Jun 2006","pubmed_entrez_date":"2006-06-28","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26935949","title":"Phosphorylation of the amino-terminus of the AGC kinase Gad8 prevents its interaction with TORC2.","citation":"Open Biol 2016 Mar;6(3)","abstract":"Cell proliferation, metabolism, migration and survival are coordinated through the tight control of two target of rapamycin (TOR) kinase complexes: TORC1 and TORC2. Here, we show that a novel phosphorylation of fission yeast Gad8 (AGC kinase) on the evolutionarily conserved threonine 6 (Thr6) prevents the physical association between Gad8 and TORC2. Accordingly, this block to protein interactions by Gad8 Thr6 phosphorylation decreases TORC2-controlled activation of Gad8. Likewise, phosphorylation of Gad8 Thr6, possibly by PKC, prevents the association of Gad8 with TORC2 thereby increasing TORC2 activity, because it reduces Gad8-mediated feedback inhibition of TORC2. Consistently, the introduction of a Gad8 T6D mutant, that mimics phosphorylation, increased TORC2 activity. Increased PKC(Pck2) expression prevented Gad8-TORC2 binding and so reduced the TORC2-mediated phosphorylation of Gad8 serine 546 that activates Gad8. Interestingly, independent of the Ser546 phosphorylation status, Gad8 Thr6 phosphorylation is important for remodelling the actin cytoskeleton and survival upon potassium ion and heat stresses. In contrast, Ser546 phosphorylation is required for the control of G1 arrest, mating, cell length at division and vascular size. Finally, these findings reveal a novel mode of TORC2 activation that is essential for cell survival following stress.","doi":"10.1098/rsob.150189","authors":"Du W, Forte GM, Smith D, Petersen J","authors_abbrev":"Du W et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2016-03-04","publication_year":"2016","canto_session_key":"7c26737aca79678a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-03-06 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.07","SPAPYUG7.02c","SPBC30D10.10c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:11115118","title":"Identification of proteases with shared functions to the proprotein processing protease Krp1 in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Microbiol 2000 Nov;38(4):839-53","abstract":"Many secretory proteins are synthesized as inactive proproteins that undergo proteolytic activation as they travel through the eukaryotic secretory pathway. The best characterized family of processing enzymes are the prohormone convertases or kexins, and these are responsible for the processing of a wide variety of prohormones and other precursors. Recent work has identified other proteases that appear to be involved in proprotein processing, but characterization of these enzymes is at an early stage. Krp1 is the only kexin identified in the fission yeast Schizosaccharomyces pombe, in which it is essential for cell viability. We have used a genetic screen to identify four proteases with specificities that overlap Krp1. Two are serine proteases, one is a zinc metalloprotease (glycoprotease) and one is an aspartyl protease that belongs to the recently described yapsin family of processing enzymes. All four proteases support the growth of a yeast strain lacking Krp1, and each is able to process the P-factor precursor, the only substrate currently known to be processed by Krp1.","authors":"Ladds G, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-12-15","publication_year":"2000","canto_session_key":"fa909d739f78709c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-01-13 14:47:28","canto_approved_date":"2019-06-07 12:49:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-10-02 10:48:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.04","SPAC22E12.09c","SPAC1006.01","SPCC1795.09","SPCC1259.10"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-01-13"},{"uniquename":"PMID:8896453","title":"Dis3, implicated in mitotic control, binds directly to Ran and enhances the GEF activity of RCC1.","citation":"EMBO J 1996 Oct 15;15(20):5595-605","abstract":"Using the two-hybrid method, we isolated a Saccharomyces cerevisiae cDNA encoding a protein homologous to Schizosaccharomyces pombe protein Dis3sp, using as bait, human GTPase Ran. The DIS3 gene is essential for viability and complements S.pombe mutant dis3-54 which is defective in mitosis. Although Dis3sc has no homology to RanBP1, it bound directly to Ran and the S.cerevisiae Ran homologue Cnr1, but not to the S.cerevisiae RCC1 homologue Srm1. Upon binding to Ran with a 1:1 molar ratio, Dis3sc enhanced a nucleotide-releasing activity of RCC1 on Ran. In the presence of Dis3sc, the K(m) of RCC1 on Ran decreased by half, while the kcat was unchanged. In vivo, Dis3sp was present as oligomers of M(r) 670-200 kDa as previously reported, and the 200 kDa oligomer of Dis3sp was found to include Spi1 and Pim1, the S.pombe homologues of Ran and RCC1, respectively. Although the biological function of the heterotrimeric oligomer consisting of Dis3, Spi1 and Pim1 is unknown, our results indicate that Dis3 is a component of the RCC1-Ran pathway.","authors":"Noguchi E, Hayashi N, Azuma Y, Seki T, Nakamura M, Nakashima N, Yanagida M, He X, Mueller U, Sazer S, Nishimoto T","authors_abbrev":"Noguchi E et al.","pubmed_publication_date":"15 Oct 1996","pubmed_entrez_date":"1996-10-15","publication_year":"1996","canto_session_key":"8a9a38b3856bff34","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-11-22 13:14:58","canto_approved_date":"2017-11-22 13:14:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-22 13:14:50","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC557.03c","SPBC1289.03c","SPBC26H8.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-11-22"},{"uniquename":"PMID:20935472","title":"Laser microsurgery provides evidence for merotelic kinetochore attachments in fission yeast cells lacking Pcs1 or Clr4.","citation":"Cell Cycle 2010 Oct 01;9(19):3997-4004","abstract":"In order to segregate chromosomes properly, the cell must prevent merotelic kinetochore attachment, an error that occurs when a single kinetochore is attached to microtubules emanating from both spindle poles. Merotelic kinetochore orientation represents a major mechanism of aneuploidy in mitotic mammalian cells and it is the primary mechanism of chromosome instability in cancer cells. Fission yeast mutants defective in putative microtubule-site clamp Pcs1/Mde4 or Clr4/Swi6-dependent centromeric heterochromatin display high frequencies of lagging chromosomes during anaphase. Here, we developed an assay based on laser microsurgery to show that the stretched morphology of lagging kinetochores in pcs1Δ and clr4Δ mutant cells is due to merotelic attachment. We further show that Mde4 is regulated by Cdc2 and that Cdc2 activity prevents precocious localization of Mde4 to the metaphase spindle. Finally, we show that Pcs1/Mde4 complex shares similar features with the conserved kinetochore complex Spc24/Spc25 suggesting that these two complexes may occupy a similar functional niche.","authors":"Rumpf C, Cipak L, Schleiffer A, Pidoux A, Mechtler K, Tolić-Nørrelykke IM, Gregan J","authors_abbrev":"Rumpf C et al.","pubmed_publication_date":"01 Oct 2010","pubmed_entrez_date":"2010-10-12","publication_year":"2010","canto_session_key":"f7e6c33889ea1fa0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-05-24 13:16:35","canto_approved_date":"2021-05-01 07:19:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-12 12:55:47","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC428.08c","SPBC6B1.04","SPAC11E3.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-05-24"},{"uniquename":"PMID:27479698","title":"Sensitive and Quantitative Three-Color Protein Imaging in Fission Yeast Using Spectrally Diverse, Recoded Fluorescent Proteins with Experimentally-Characterized In Vivo Maturation Kinetics.","citation":"PLoS One 2016;11(8):e0159292","abstract":"Schizosaccharomyces pombe is an outstanding model organism for cell biological investigations, yet the range of useful and well-characterized fluorescent proteins (XFPs) is limited. We generated and characterized three recoded fluorescent proteins for 3-color analysis in S.pombe, Super-folder GFP, monomeric Kusabira Orange 2 and E2Crimson. Upon optimization and expression in S. pombe, the three proteins enabled sensitive simultaneous 3-color detection capability. Furthermore, we describe a strategy that combines a pulse-chase approach and mathematical modeling to quantify the maturation kinetics of these proteins in vivo. We observed maturation kinetics in S. pombe that are expected from those described for these proteins in vitro and/or in other cell types, but also unpredicted behaviors. Our studies provide a kinetically-characterized, integrated three-color XFP toolbox for S. pombe.","doi":"10.1371/journal.pone.0159292","authors":"Al-Sady B, Greenstein RA, El-Samad HJ, Braun S, Madhani HD","authors_abbrev":"Al-Sady B et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-08-02","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-08-03 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34375584","title":"A composite DNA element that functions as a maintainer required for epigenetic inheritance of heterochromatin.","citation":"Mol Cell 2021 Oct 07;81(19):3979-3991.e4","abstract":"Epigenetic inheritance of heterochromatin requires DNA-sequence-independent propagation mechanisms, coupling to RNAi, or input from DNA sequence, but how DNA contributes to inheritance is not understood. Here, we identify a DNA element (termed \"maintainer\") that is sufficient for epigenetic inheritance of pre-existing histone H3 lysine 9 methylation (H3K9me) and heterochromatin in Schizosaccharomyces pombe but cannot establish de novo gene silencing in wild-type cells. This maintainer is a composite DNA element with binding sites for the Atf1/Pcr1 and Deb1 transcription factors and the origin recognition complex (ORC), located within a 130-bp region, and can be converted to a silencer in cells with lower rates of H3K9me turnover, suggesting that it participates in recruiting the H3K9 methyltransferase Clr4/Suv39h. These results suggest that, in the absence of RNAi, histone H3K9me is only heritable when it can collaborate with maintainer-associated DNA-binding proteins that help recruit the enzyme responsible for its epigenetic deposition.","doi":"10.1016/j.molcel.2021.07.017","authors":"Wang X, Paulo JA, Li X, Zhou H, Yu J, Gygi SP, Moazed D","authors_abbrev":"Wang X et al.","pubmed_publication_date":"07 Oct 2021","pubmed_entrez_date":"2021-08-10","publication_year":"2021","canto_session_key":"64f28fc935d7b022","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-08-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC21E11.03c","SPAC1B1.01","SPBC428.08c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:21408210","title":"SUMO-targeted ubiquitin ligase, Rad60, and Nse2 SUMO ligase suppress spontaneous Top1-mediated DNA damage and genome instability.","citation":"PLoS Genet 2011 Mar;7(3):e1001320","abstract":"Through as yet undefined proteins and pathways, the SUMO-targeted ubiquitin ligase (STUbL) suppresses genomic instability by ubiquitinating SUMO conjugated proteins and driving their proteasomal destruction. Here, we identify a critical function for fission yeast STUbL in suppressing spontaneous and chemically induced topoisomerase I (Top1)-mediated DNA damage. Strikingly, cells with reduced STUbL activity are dependent on tyrosyl-DNA phosphodiesterase 1 (Tdp1). This is notable, as cells lacking Tdp1 are largely aphenotypic in the vegetative cell cycle due to the existence of alternative pathways for the removal of covalent Top1-DNA adducts (Top1cc). We further identify Rad60, a SUMO mimetic and STUbL-interacting protein, and the SUMO E3 ligase Nse2 as critical Top1cc repair factors in cells lacking Tdp1. Detection of Top1ccs using chromatin immunoprecipitation and quantitative PCR shows that they are elevated in cells lacking Tdp1 and STUbL, Rad60, or Nse2 SUMO ligase activity. These unrepaired Top1ccs are shown to cause DNA damage, hyper-recombination, and checkpoint-mediated cell cycle arrest. We further determine that Tdp1 and the nucleotide excision repair endonuclease Rad16-Swi10 initiate the major Top1cc repair pathways of fission yeast. Tdp1-based repair is the predominant activity outside S phase, likely acting on transcription-coupled Top1cc. Epistasis analyses suggest that STUbL, Rad60, and Nse2 facilitate the Rad16-Swi10 pathway, parallel to Tdp1. Collectively, these results reveal a unified role for STUbL, Rad60, and Nse2 in protecting genome stability against spontaneous Top1-mediated DNA damage.","doi":"10.1371/journal.pgen.1001320","authors":"Heideker J, Prudden J, Perry JJ, Tainer JA, Boddy MN","authors_abbrev":"Heideker J et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-03-17","publication_year":"2011","canto_session_key":"fe945f3484811d26","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPCP31B10.05","SPBC3D6.11c","SPBC1703.14c","SPBC1921.02","SPAC13C5.07","SPBC4F6.15c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:10443431","title":"In vitro excision repair assay in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 1999;113:327-35","abstract":"","authors":"Salles B, Calsou P","authors_abbrev":"Salles B et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-08-12","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15371339","title":"Two modes of DNA double-strand break repair are reciprocally regulated through the fission yeast cell cycle.","citation":"Genes Dev 2004 Sep 15;18(18):2249-54","abstract":"Several considerations suggest that levels of the two major modes of double-strand break (DSB) repair, homologous recombination (HR), and nonhomologous end joining (NHEJ), are regulated through the cell cycle. However, this idea has not been explicitly tested. In the absence of the telomere-binding protein Taz1, fission yeast undergo lethal telomere fusions via NHEJ. These fusions occur only during periods of nitrogen starvation and fail to accumulate during logarithmic growth, when the majority of cells are in G2. We show that G1 arrest is the specific nitrogen starvation-induced event that promotes NHEJ between taz1(-) telomeres. Furthermore, the general levels of NHEJ and HR are reciprocally regulated through the cell cycle, so that NHEJ is 10-fold higher in early G1 than in other cell cycle stages; the reverse is true for HR. Whereas NHEJ is known to be dispensable for survival of DSBs in cycling cells, we find that it is critical for repair and survival of DSBs arising during G1.","authors":"Ferreira MG, Cooper JP","authors_abbrev":"Ferreira MG et al.","pubmed_publication_date":"15 Sep 2004","pubmed_entrez_date":"2004-09-17","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42275214","title":"Protection and deprotection of the Rec8 cohesin complex during meiosis.","citation":"Cell Rep 2026 Jun 11;45(6):117541","abstract":"During meiosis I, the cohesin Rec8 is cleaved by separase along the chromosome arms but is protected at the centromere by shugoshin (Sgo1); during meiosis II, it is not protected. In fission yeast, another meiotic regulator, meikin (Moa1), supports the protective function of Sgo1 primarily by phosphorylating Rec8 at S450. Here we show that both meiosis I-specific proteins, Sgo1 and Moa1, are degraded during anaphase I by the APC/C-Slp1 pathway. To explore the possibility of ectopic protection during meiosis II, we expressed non-degradable forms of Moa1 and Sgo1 during meiosis. Our analyses revealed that stabilization of the Sgo1 protein and phosphorylation of Rec8 at S449 and S450 are necessary and sufficient for the protection of Rec8 cohesin during meiosis II. Furthermore, our results suggest that the phosphorylation-dependent interaction between Rec8 and Sgo1 during meiosis is prominent at mono-oriented kinetochores but not at bi-oriented kinetochores.","doi":"10.1016/j.celrep.2026.117541","authors":"Liu Y, Zhang K, Bai Z, Sun L, Hou H, Watanabe Y","authors_abbrev":"Liu Y et al.","pubmed_publication_date":"11 Jun 2026","pubmed_entrez_date":"2026-06-11","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-11 23:25:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14501122","title":"Expression, purification, crystallization and preliminary crystallographic analysis of the calponin-homology domain of Rng2.","citation":"Acta Crystallogr D Biol Crystallogr 2003 Oct;59(Pt 10):1809-12","abstract":"Rng2 is a multidomain protein component of the actiomyosin ring and the spindle pole body necessary for cytokinesis in Schizosaccharomyces pombe. The calponin-homology domain of Rng2 from S. pombe has been overexpressed, purified and crystallized. The crystals belong to space group P2(1). Br- and Hg-derivative data sets were measured to 2.21 A using synchrotron radiation from crystals that were partially fixed with glutaraldehyde. Electron-density maps have been obtained from two-wavelength MAD on the Br derivative and SAD on the Hg derivative.","authors":"Wang CH, Walsh M, Balasubramanian MK, Dokland T","authors_abbrev":"Wang CH et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2003-09-23","publication_year":"2003","canto_session_key":"b18515799185f9f2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-01 07:47:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-30 08:46:48","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F8.13c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-04-30"},{"uniquename":"PMID:34114004","title":"Identification of sur2 mutation affecting the lifespan of fission yeast.","citation":"FEMS Microbiol Lett 2021 Jun 24;368(12)","abstract":"Yeast is a suitable model system to analyze the mechanism of lifespan. In this study, to identify novel factors involved in chronological lifespan, we isolated a mutant with a long chronological lifespan and found a missense mutation in the sur2+ gene, which encodes a homolog of Saccharomyces cerevisiae sphingolipid C4-hydroxylase in fission yeast. Characterization of the mutant revealed that loss of sur2 function resulted in an extended chronological lifespan. The effect of caloric restriction, a well-known signal for extending lifespan, is thought to be dependent on the sur2+ gene.","doi":"10.1093/femsle/fnab070","authors":"Kurauchi T, Matsui K, Shimasaki T, Ohtsuka H, Tsubouchi S, Ihara K, Tani M, Aiba H","authors_abbrev":"Kurauchi T et al.","pubmed_publication_date":"24 Jun 2021","pubmed_entrez_date":"2021-06-11","publication_year":"2021","canto_session_key":"383268b909ae2915","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_first_approved_date":"2021-06-17 14:57:46","canto_approved_date":"2021-06-17 14:57:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-06-17 01:19:00","canto_added_date":"2021-06-13 00:15:03","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":6,"orcid":"0000-0002-7775-0446","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10","SPBC887.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-06-17"},{"uniquename":"PMID:8121805","title":"Replacement of the Saccharomyces cerevisiae RPR1 gene with heterologous RNase P RNA genes.","citation":"Nucleic Acids Res 1994 Jan 25;22(2):200-7","abstract":"Phylogenetic studies of yeast nuclear RNase P RNA genes have shown a striking conservation of secondary structure for the Saccharomyces and Schizosaccharomyces RNase P RNAs, yet much of the primary sequence and many substructures vary among the RNAs examined. To investigate which sequences and structural features can be varied and still allow function in a heterologous organism, RNase P genes from several yeast species were tested for the ability to substitute for the Saccharomyces cerevisiae RNA. The RNase P genes from Saccharomyces carlsbergensis and Saccharomyces kluyveri could act as the sole source of RNase P RNA within S. cerevisiae cells, whereas the genes from Saccharomyces globosus and Schizosaccharomyces pombe could not. Although heterologous RNase P RNAs were synthesized by the cells in all cases, the RNAs that complemented tended to be processed from longer precursor transcripts into mature-sized RNase P RNA, while the RNAs that did not complement tended to accumulate as the longer precursor form. The results identified sequences and structures in the RNA that are not essential for interaction with species-specific proteins, processing or localization, and suggested other positions that may be candidates for such processes.","authors":"Pagán-Ramos E, Tranguch AJ, Kindelberger DW, Engelke DR","authors_abbrev":"Pagán-Ramos E et al.","pubmed_publication_date":"25 Jan 1994","pubmed_entrez_date":"1994-01-25","publication_year":"1994","canto_session_key":"943cdbab645ee2f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-15 11:14:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-15 11:14:14","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.128"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-15"},{"uniquename":"PMID:22356826","title":"Iterative orthology prediction uncovers new mitochondrial proteins and identifies C12orf62 as the human ortholog of COX14, a protein involved in the assembly of cytochrome c oxidase.","citation":"Genome Biol 2012 Feb 22;13(2):R12","abstract":"Orthology is a central tenet of comparative genomics and ortholog identification is instrumental to protein function prediction. Major advances have been made to determine orthology relations among a set of homologous proteins. However, they depend on the comparison of individual sequences and do not take into account divergent orthologs.\nWe have developed an iterative orthology prediction method, Ortho-Profile, that uses reciprocal best hits at the level of sequence profiles to infer orthology. It increases ortholog detection by 20% compared to sequence-to-sequence comparisons. Ortho-Profile predicts 598 human orthologs of mitochondrial proteins from Saccharomyces cerevisiae and Schizosaccharomyces pombe with 94% accuracy. Of these, 181 were not known to localize to mitochondria in mammals. Among the predictions of the Ortho-Profile method are 11 human cytochrome c oxidase (COX) assembly proteins that are implicated in mitochondrial function and disease. Their co-expression patterns, experimentally verified subcellular localization, and co-purification with human COX-associated proteins support these predictions. For the human gene C12orf62, the ortholog of S. cerevisiae COX14, we specifically confirm its role in negative regulation of the translation of cytochrome c oxidase.\nDivergent homologs can often only be detected by comparing sequence profiles and profile-based hidden Markov models. The Ortho-Profile method takes advantage of these techniques in the quest for orthologs.","doi":"10.1186/gb-2012-13-2-r12","authors":"Szklarczyk R, Wanschers BF, Cuypers TD, Esseling JJ, Riemersma M, van den Brand MA, Gloerich J, Lasonder E, van den Heuvel LP, Nijtmans LG, Huynen MA","authors_abbrev":"Szklarczyk R et al.","pubmed_publication_date":"22 Feb 2012","pubmed_entrez_date":"2012-02-24","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15611619","title":"A transcriptional pathway for cell separation in fission yeast.","citation":"Cell Cycle 2005 Jan;4(1):39-41","abstract":"Numerous genes are transcriptionally activated and repressed in a cell cycle-dependent manner. We have recently reported the global gene expression program during the cell cycle in fission yeast (S. pombe). Among the periodically expressed fission yeast genes, a large proportion shows peak transcript levels during mitosis. Many of these genes are regulated by a transcriptional cascade involving two transcription factors: the forkhead protein Sep1p which activates the zinc finger protein Ace2p. A main function of the Sep1p-Ace2p transcriptional pathway is to trigger the separation of daughter cells after cytokinesis. Absence of Sep1p, Ace2p, or some of their target genes leads to a hyphal-like growth pattern with chains of connected cells. Yeast cells probably evolved from filamentous fungi. It is possible that the Sep1p-Ace2p pathway contributed to the emergence of proliferation through single cells, and that this regulatory pathway can still be modulated to adjust growth modes depending on environmental conditions. Here, various properties of the Sep1p-Ace2p transcriptional pathway and mechanisms for cell separation are discussed in the context of recent findings.","authors":"Bähler J","authors_abbrev":"Bähler J","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-12-22","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15798214","title":"A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation.","citation":"Mol Cell Biol 2005 Apr;25(8):3305-16","abstract":"Histone methylation and the enzymes that mediate it are important regulators of chromatin structure and gene transcription. In particular, the histone H3 lysine 36 (K36) methyltransferase Set2 has recently been shown to associate with the phosphorylated C-terminal domain (CTD) of RNA polymerase II (RNAPII), implying that this enzyme has an important role in the transcription elongation process. Here we show that a novel domain in the C terminus of Set2 is responsible for interaction between Set2 and RNAPII. This domain, termed the Set2 Rpb1 interacting (SRI) domain, is encompassed by amino acid residues 619 to 718 in Set2 and is found to occur in a number of putative Set2 homologs from Schizosaccharomyces pombe to humans. Unexpectedly, BIACORE analysis reveals that the SRI domain binds specifically, and with high affinity, to CTD repeats that are doubly modified (serine 2 and serine 5 phosphorylated), indicating that Set2 association across the body of genes requires a specific pattern of phosphorylated RNAPII. Deletion of the SRI domain not only abolishes Set2-RNAPII interaction but also abolishes K36 methylation in vivo, indicating that this interaction is required for establishing K36 methylation on chromatin. Using 6-azauracil (6AU) as an indicator of transcription elongation defects, we found that deletion of the SRI domain conferred a strong resistance to this compound, which was identical to that observed with set2 deletion mutants. Furthermore, yeast strains carrying set2 alleles that are catalytically inactive or yeast strains bearing point mutations at K36 were also found to be resistant to 6AU. These data suggest that it is the methylation by Set2 that affects transcription elongation. In agreement with this, we have determined that deletion of SET2, its SRI domain, or amino acid substitutions at K36 result in an alteration of RNAPII occupancy levels over transcribing genes. Taken together, these data indicate K36 methylation, established by the SRI domain-mediated association of Set2 with RNAPII, plays an important role in the transcription elongation process.","authors":"Kizer KO, Phatnani HP, Shibata Y, Hall H, Greenleaf AL, Strahl BD","authors_abbrev":"Kizer KO et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-03-31","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23G3.01","SPBC28F2.12","SPAC29B12.02c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:22137473","title":"Shaping fission yeast cells by rerouting actin-based transport on microtubules.","citation":"Curr Biol 2011 Dec 20;21(24):2064-9","abstract":"Kinesins and myosins transport cargos to specific locations along microtubules and actin filaments, respectively. The relative contribution of the two transport systems for cell polarization varies extensively in different cell types, with some cells relying exclusively on actin-based transport while others mainly use microtubules. Using fission yeast, we asked whether one transport system can substitute for the other. In this organism, microtubules and actin cables both contribute to polarized growth by transporting cargos to cell poles, but with distinct roles: microtubules transport landmarks to label cell poles for growth and actin assembly but do not directly contribute to the growth process [1]. Actin cables serve as tracks for myosin V delivery of growth vesicles to cell poles [2-4]. We engineered a chimera between the motor domain of the kinesin 7 Tea2 and the globular tail of the myosin V Myo52, which we show transports Ypt3, a myosin cargo receptor, to cell poles along microtubules. Remarkably, this chimera restores polarized growth and viability to cells lacking actin cables. It also bypasses the normal microtubule-dependent marking of cell poles for polarized growth, but not for other functions. Thus, a synthetic motor protein successfully redirects cargos along a distinct cytoskeletal route.","doi":"10.1016/j.cub.2011.10.033","authors":"Lo Presti L, Martin SG","authors_abbrev":"Lo Presti L et al.","pubmed_publication_date":"20 Dec 2011","pubmed_entrez_date":"2011-12-06","publication_year":"2011","canto_session_key":"098d04fd85e6672d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-01-22 14:49:46","canto_approved_date":"2024-04-02 12:02:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-01-22 14:49:34","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.14c","SPCC1919.10c","SPBC106.20","SPCC1223.06","SPBC1706.01","SPCC895.05","SPAC18G6.15","SPBC1604.20c","SPAC18G6.03"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2020-01-22"},{"uniquename":"EMBL:AB084827","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.15"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21098516","title":"Structural analysis of α1,3-linked galactose-containing oligosaccharides in Schizosaccharomyces pombe mutants harboring single and multiple α-galactosyltransferase genes disruptions.","citation":"Glycobiology 2011 Mar;21(3):340-51","abstract":"In the fission yeast Schizosaccharomyces pombe, galactose (Gal) residues are transferred to N- and O-linked oligosaccharides of glycoproteins by galactosyltransferases in the lumen of the Golgi apparatus. In S. pombe, the major in vitro α1,2-galactosyltransferase activity has been purified, the gma12(+) gene has been cloned, and three α-galactosyltransferase genes (gmh1(+)-gmh3(+)) have also been partially characterized. In this study, we found three additional uncharacterized genes with homology to gmh1(+) (gmh4(+)-gmh6(+)) in the fission yeast genome sequence. All possible single disruption mutants and the septuple disruption strain were constructed and characterized. The electrophoretic mobility of acid phosphatase prepared from gma12Δ, gmh2Δ, gmh3Δ and gmh6Δ mutants was higher than that from wild type, indicating that Gma12p, Gmh2p, Gmh3p and Gmh6p are required for the galactosylation of N-linked oligosaccharides. High-performance liquid chromatography (HPLC) analysis of pyridylaminated O-linked oligosaccharides from each single mutant showed that Gma12p, Gmh2p and Gmh6p are involved in galactosylation of O-linked oligosaccharides. The septuple mutant exhibited similar drug and temperature sensitivity as a gms1Δ mutant that is incapable of galactosylation. Oligosaccharide structural analysis based on HPLC and methylation analysis revealed that the septuple mutant still contained oligosaccharides consisting of α1,3-linked Gal residues, indicating that an unknown α1,3-galactosyltransferase activity was still present in the septuple mutant.","doi":"10.1093/glycob/cwq167","authors":"Ohashi T, Nakakita S, Sumiyoshi W, Yamada N, Ikeda Y, Tanaka N, Takegawa K","authors_abbrev":"Ohashi T et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2010-11-25","publication_year":"2011","canto_session_key":"a9159ec6909bd6c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2017-11-08 14:27:44","canto_approved_date":"2024-07-17 07:15:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-09 09:44:27","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.17","SPAC5H10.11","SPBC1289.13c","SPCC1795.03","SPAC637.06","SPCC736.04c","SPAC22E12.06c","SPAC5H10.13c","SPAC1006.05c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2017-11-08"},{"uniquename":"PMID:35082773","title":"Phosphoinositide-Dependent Protein Kinases Regulate Cell Cycle Progression Through the SAD Kinase Cdr2 in Fission Yeast.","citation":"Front Microbiol 2021;12:807148","abstract":"Aberration in the control of cell cycle contributes to the development and progression of many diseases including cancers. Ksg1 is a  Schizosaccharomyces pombe  fission yeast homolog of mammalian phosphoinositide-dependent protein kinase 1 (PDK1) which is regarded as a signaling hub for human tumorigenesis. A previous study reported that Ksg1 plays an important role in cell cycle progression, however, the underlying mechanism remains elusive. Our genomic library screen for novel elements involved in Ksg1 function identified two serine/threonine kinases, namely SAD family kinase Cdr2 and another PDK1 homolog Ppk21, as multicopy suppressors of the thermosensitive phenotype of  ksg1-208  mutant. We found that overexpression of Ppk21 or Cdr2 recovered the defective cell cycle transition of  ksg1-208  mutant. In addition,  ksg1-208  Δ ppk21  cells showed more marked defects in cell cycle transition than each single mutant. Moreover, overexpression of Ppk21 failed to recover the thermosensitive phenotype of the  ksg1-208  mutant when Cdr2 was lacking. Notably, the  ksg1-208  mutation resulted in abnormal subcellular localization and decreased abundance of Cdr2, and Ppk21 deletion exacerbated the decreased abundance of Cdr2 in the  ksg1-208  mutant. Intriguingly, expression of a mitotic inducer Cdc25 was significantly decreased in  ksg1-208 , Δ ppk21 , or Δ cdr2  cells, and overexpression of Ppk21 or Cdr2 partially recovered the decreased protein level of Cdc25 in the  ksg1-208  mutant. Altogether, our findings indicated that Cdr2 is a novel downstream effector of PDK1 homologs Ksg1 and Ppk21, both of which cooperatively participate in regulating cell cycle progression, and Cdc25 is involved in this process in fission yeast.","doi":"10.3389/fmicb.2021.807148","authors":"Liu K, Liu Q, Sun Y, Fan J, Zhang Y, Sakamoto N, Kuno T, Fang Y","authors_abbrev":"Liu K et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2022-01-27","publication_year":"2021","canto_session_key":"f5cf2ad5297d65c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yue Fang","canto_first_approved_date":"2022-04-14 18:04:52","canto_approved_date":"2022-04-21 08:10:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-04-11 20:46:20","canto_added_date":"2022-01-29 01:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yue Fang","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC1778.10c","SPCC576.15c","SPAC57A10.02"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2022-04-14"},{"uniquename":"PMID:19682301","title":"A large complex mediated by Moc1, Moc2 and Cpc2 regulates sexual differentiation in fission yeast.","citation":"FEBS J 2009 Sep;276(18):5076-93","abstract":"Sexual differentiation in Schizosaccharomyces pombe is triggered by nutrient starvation and is downregulated by cAMP. Screening programs have identified the moc1/sds23, moc2/ded1, moc3 and moc4/zfs1 genes as inducers of sexual differentiation, even in the presence of elevated levels of cAMP. To investigate possible interactions among Moc1, Moc2, Moc3 and Moc4 proteins, we first screened for individual Moc-interacting proteins using the yeast two-hybrid system and verified the interactions with other Moc proteins. Using this screening process, Cpc2 and Rpl32-2 were highlighted as factors involved in interactions with multiple Moc proteins. Cpc2 interacted with Moc1, Moc2 and Moc3, whereas the ribosomal protein Rpl32-2 interacted with all Moc proteins in the two-hybrid system. Physical interactions of Cpc2 with Moc1, Moc2 and Rpl32-2, and of Rpl32-2 with Moc2 were confirmed by coimmunoprecipitation. In addition, using Blue Native/PAGE, we revealed that each Moc protein exists as a large complex. Overexpression of Moc1, Moc2, Moc3, Moc4 and Rpl32-2 resulted in the efficient induction of a key transcription factor Ste11, suggesting that all proteins tested are positive regulators of Ste11. Considering that Moc2/Ded1 is a general translation factor and that Cpc2 associates with many ribosomal proteins, including Rpl32-2, it is possible that a large Moc-mediated complex, detected in this study, may act as a translational regulator involved in the control of sexual differentiation in S. pombe through the induction of Ste11.","doi":"10.1111/j.1742-4658.2009.07204.x","authors":"Paul SK, Oowatari Y, Kawamukai M","authors_abbrev":"Paul SK et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-08-18","publication_year":"2009","canto_session_key":"a9b16aacd2d4635","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-24 11:05:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-02-16 22:25:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC74.05","SPAC1002.13c","SPAC6F6.07c","SPCC16A11.14","SPAC1834.05","SPBC577.02","SPBC1718.07c","SPBC11C11.07","SPAC13G7.08c","SPCC1795.11","SPAPB1A10.11c","SPAC3A12.10","SPBC646.13","SPAC3H5.12c","SPAC1F8.07c","SPBC23G7.15c","SPAC513.01c","SPCC16C4.13c","SPCC576.09","SPAC664.04c","SPAC22H12.04c","SPAC227.18","SPCC74.02c","SPAC17H9.05","SPBC32F12.11","SPAC6B12.15","SPBC776.01","SPCC188.06c","SPCC576.03c","SPAC821.07c","SPAC821.10c","SPBC29A3.04","SPAC323.02c","SPBC19C2.07","SPAC20H4.10","SPAC3C7.14c","SPBC32C12.02","SPAC3H5.10","SPAC3H5.05c","SPBC1815.01","SPCC1442.10c","SPCC794.09c"],"gene_count":42,"ltp_gene_count":4,"approved_date":"2012-02-16"},{"uniquename":"PMID:2397448","title":"Pattern of end growth of the fission yeast Schizosaccharomyces pombe.","citation":"Can J Microbiol 1990 Jun;36(6):390-4","abstract":"The patterns of end growth of individual cells of Schizosaccharomyces pombe, wild-type cells (strain 972 h-), cells exposed to 8 mM hydroxyurea, and cdc mutants (cdc11-123 and cdc2-33), were investigated by time-lapse photomicrography. It was reconfirmed that there are three patterns of end growth: cells growing at the old end, at the new end, and at both ends from the beginning of the cell cycle. Cells that initiated growth at the old (new) end increased their growth rate at the new (old) end and became constant in their growth rate at the old (new) end when cells had their growth rate higher than a critical value: 0.08, 0.09, 0.08, and 0.11 microns/min in wild-type cells, cells exposed to hydroxyurea, cdc11-123 cells, and cdc2-33 cells, respectively. The critical value is proportional to the doubling time in length.","authors":"Miyata H, Miyata M, Johnson BF","authors_abbrev":"Miyata H et al.","pubmed_publication_date":"Jun 1990","pubmed_entrez_date":"1990-06-01","publication_year":"1990","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11694585","title":"Interactions among a fimbrin, a capping protein, and an actin-depolymerizing factor in organization of the fission yeast actin cytoskeleton.","citation":"Mol Biol Cell 2001 Nov;12(11):3515-26","abstract":"We report studies of the fission yeast fimbrin-like protein Fim1, which contains two EF-hand domains and two actin-binding domains (ABD1 and ABD2). Fim1 is a component of both F-actin patches and the F-actin ring, but not of F-actin cables. Fim1 cross-links F-actin in vitro, but a Fim1 protein lacking either EF-hand domains (Fim1A12) or both the EF-hand domains and ABD1 (Fim1A2) has no actin cross-linking activity. Overexpression of Fim1 induced the formation of F-actin patches throughout the cell cortex, whereas the F-actin patches disappear in cells overexpressing Fim1A12 or Fim1A2. Thus, the actin cross-linking activity of Fim1 is probably important for the formation of F-actin patches. The overexpression of Fim1 also excluded the actin-depolymerizing factor Adf1 from the F-actin patches and inhibited the turnover of actin in these structures. Thus, Fim1 may function in stabilizing the F-actin patches. We also isolated the gene encoding Acp1, a subunit of the heterodimeric F-actin capping protein. fim1 acp1 double null cells showed more severe defects in the organization of the actin cytoskeleton than those seen in each single mutant. Thus, Fim1 and Acp1 may function in a similar manner in the organization of the actin cytoskeleton. Finally, genetic studies suggested that Fim1 may function in cytokinesis in cooperation with Cdc15 (PSTPIP) and Rng2 (IQGAP), respectively.","authors":"Nakano K, Satoh K, Morimatsu A, Ohnuma M, Mabuchi I","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2001-11-06","publication_year":"2001","canto_session_key":"d7f404ebd5804111","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-06-30 13:52:19","canto_approved_date":"2026-04-21 18:22:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-04-17 16:57:38","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":71,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.13c","SPBC1778.06c","SPAC12B10.07","SPAC20G4.06c","SPBC26H8.07c","SPBC24C6.07","SPAC4A8.15c","SPBC32H8.12c","SPAC20G8.05c","SPAP8A3.08","SPAC27F1.02c","SPCC1739.11c","SPBC21.06c","SPAC1F5.04c"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2017-06-30"},{"uniquename":"PMID:22343349","title":"Protein phosphatase CaPpz1 is involved in cation homeostasis, cell wall integrity and virulence of Candida albicans.","citation":"Microbiology (Reading) 2012 May;158(Pt 5):1258-1267","abstract":"The opportunistic pathogen Candida albicans has a single protein phosphatase Z (PPZ) candidate gene termed CaPPZ1, which shows significant allele variability. We demonstrate here that bacterially expressed CaPpz1 protein exhibits phosphatase activity which can be inhibited by recombinant Hal3, a known inhibitor of Saccharomyces cerevisiae Ppz1. Site-directed mutagenesis experiments based on natural polymorphisms allowed the identification of three amino acid residues that affect enzyme activity or stability. The expression of CaPPZ1 in ppz1 S. cerevisiae and pzh1 Schizosaccharomyces pombe cells partially rescued the salt and caffeine phenotypes of the deletion mutants. CaPpz1 also complemented the slt2 S. cerevisiae mutant, which is crippled in the mitogen-activated protein (MAP) kinase that mediates the cell wall integrity signalling pathway. Collectively, our results suggest that the orthologous PPZ enzymes have similar but not identical functions in different fungi. The deletion of the CaPPZ1 gene in C. albicans resulted in a mutant that was sensitive to salts such as LiCl and KCl, to caffeine, and to agents that affect cell wall biogenesis such as Calcofluor White and Congo red, but was tolerant to spermine and hygromycin B. Reintegration of the CaPPZ1 gene into the deletion mutant alleviated all of the mutant phenotypes tested. Thus CaPpz1 is involved in cation homeostasis, cell wall integrity and the regulation of the membrane potential of C. albicans. In addition, the germ tube growth rate, and virulence in the BALB/c mouse model, were reduced in the null mutant, suggesting a novel function for CaPpz1 in the yeast to hypha transition that may have medical relevance.","doi":"10.1099/mic.0.057075-0","authors":"Ádám C, Erdei É, Casado C, Kovács L, González A, Majoros L, Petrényi K, Bagossi P, Farkas I, Molnar M, Pócsi I, Ariño J, Dombrádi V","authors_abbrev":"Ádám C et al.","pubmed_publication_date":"May 2012","pubmed_entrez_date":"2012-02-21","publication_year":"2012","canto_session_key":"5faec493a92279d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-03-28 13:43:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-03-28 13:32:20","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-03-28"},{"uniquename":"PMID:23420873","title":"Conserved and divergent features of kinetochores and spindle microtubule ends from five species.","citation":"J Cell Biol 2013 Feb 18;200(4):459-74","abstract":"Interfaces between spindle microtubules and kinetochores were examined in diverse species by electron tomography and image analysis. Overall structures were conserved in a mammal, an alga, a nematode, and two kinds of yeasts; all lacked dense outer plates, and most kinetochore microtubule ends flared into curved protofilaments that were connected to chromatin by slender fibrils. Analyses of curvature on >8,500 protofilaments showed that all classes of spindle microtubules displayed some flaring protofilaments, including those growing in the anaphase interzone. Curved protofilaments on anaphase kinetochore microtubules were no more flared than their metaphase counterparts, but they were longer. Flaring protofilaments in budding yeasts were linked by fibrils to densities that resembled nucleosomes; these are probably the yeast kinetochores. Analogous densities in fission yeast were larger and less well-defined, but both yeasts showed ring- or partial ring-shaped structures girding their kinetochore microtubules. Flaring protofilaments linked to chromatin are well placed to exert force on chromosomes, assuring stable attachment and reliable anaphase segregation.","doi":"10.1083/jcb.201209154","authors":"McIntosh JR, O'Toole E, Zhudenkov K, Morphew M, Schwartz C, Ataullakhanov FI, Grishchuk EL","authors_abbrev":"McIntosh JR et al.","pubmed_publication_date":"18 Feb 2013","pubmed_entrez_date":"2013-02-20","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16051163","title":"Cytoskeleton: microtubules born on the run.","citation":"Curr Biol 2005 Jul 26;15(14):R551-4","abstract":"The organization of microtubules into large arrays determines cell morphology and structure. Recent work in the fission yeast describes a novel mechanism for microtubule self-organization in the absence of centrosomes; this mechanism may function in a variety of cell types found in diverse organisms.","authors":"Becker BE, Cassimeris L","authors_abbrev":"Becker BE et al.","pubmed_publication_date":"26 Jul 2005","pubmed_entrez_date":"2005-07-30","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10581266","title":"The identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeasts.","citation":"Genetics 1999 Dec;153(4):1561-72","abstract":"The Wee1 kinase inhibits entry into mitosis by phosphorylation of the Cdc2 kinase. Searching for multicopy suppressors that abolish this inhibition in the fission yeast, we have identified a novel gene, here named wos2, encoding a protein with significant homology to human p23, an Hsp90-associated cochaperone. The deletion mutant has a modest phenotype, being heat-shock sensitive. Using antibodies raised against bacterially produced protein, we determined that Wos2 is very abundant, ubiquitously distributed in the yeast cell, and its expression dropped drastically as cells entered into early stationary phase, indicating that its function is associated with cell proliferation. In proliferating cells, the amount of Wos2 protein was not subjected to cell cycle regulation. However, in vitro assays demonstrated that this Hsp90 cochaperone is potentially regulated by phosphorylation. In addition to suppressing Wee1 activity, overproduction of Wos2 displayed synthetic lethality with Cdc2 mutant proteins, indicating that this Hsp90 cochaperone functionally interacts with Cdc2. The level of Cdc2 protein and its associated H1 kinase activity under synthetic lethal conditions suggested a regulatory role for this Wos2-Cdc2 interaction. Hsp90 complexes are required for CDK regulation; the synergy found between the excess of Wos2 and a deficiency in Hsp90 activity suggests that Wos2 could specifically interfere with the Hsp90-dependent regulation of Cdc2. In vitro analysis indicated that the above genetic interactions could take place by physical association of Wos2 with the single CDK complex of the fission yeast. Expression of the budding yeast p23 protein (encoded by the SBA1 gene) in the fission yeast indicated that Wos2 and Sba1 are functionally exchangeable and therefore that properties described here for Wos2 could be of wide significance in understanding the biological function of cochaperone p23 in eukaryotic cells.","authors":"Muñoz MJ, Bejarano ER, Daga RR, Jimenez J","authors_abbrev":"Muñoz MJ et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-12-03","publication_year":"1999","canto_session_key":"20c200984ffb7421","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-07 17:14:42","canto_approved_date":"2019-06-07 17:14:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-06-07 17:14:35","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPCC18B5.03","SPBC11B10.09","SPAC9E9.13","SPAC926.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-06-07"},{"uniquename":"PMID:24256269","title":"Switching the centromeres on and off: epigenetic chromatin alterations provide plasticity in centromere activity stabilizing aberrant dicentric chromosomes.","citation":"Biochem Soc Trans 2013 Dec;41(6):1648-53","abstract":"The kinetochore, which forms on a specific chromosomal locus called the centromere, mediates interactions between the chromosome and the spindle during mitosis and meiosis. Abnormal chromosome rearrangements and/or neocentromere formation can cause the presence of multiple centromeres on a single chromosome, which results in chromosome breakage or cell cycle arrest. Analyses of artificial dicentric chromosomes suggested that the activity of the centromere is regulated epigenetically; on some stably maintained dicentric chromosomes, one of the centromeres no longer functions as a platform for kinetochore formation, although the DNA sequence remains intact. Such epigenetic centromere inactivation occurs in cells of various eukaryotes harbouring 'regional centromeres', such as those of maize, fission yeast and humans, suggesting that the position of the active centromere is determined by epigenetic markers on a chromosome rather than the nucleotide sequence. Our recent findings in fission yeast revealed that epigenetic centromere inactivation consists of two steps: disassembly of the kinetochore initiates inactivation and subsequent heterochromatinization prevents revival of the inactivated centromere. Kinetochore disassembly followed by heterochromatinization is also observed in normal senescent human cells. Thus epigenetic centromere inactivation may not only stabilize abnormally generated dicentric chromosomes, but also be part of an intrinsic mechanism regulating cell proliferation.","doi":"10.1042/BST20130136","authors":"Sato H, Saitoh S","authors_abbrev":"Sato H et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006816","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8110200","title":"The amino acid sequence of the small monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe.","citation":"Biochem J 1994 Feb 01;297 ( Pt 3)(Pt 3):603-8","abstract":"The amino acid sequence of the monomeric 2,3-bisphosphoglycerate (BPG)-dependent phosphoglycerate mutase (PGAM) from the fission yeast Schizosaccharomyces pombe has been determined. Amino acid sequencing of proteolytic fragments of the enzyme showed the S. pombe mutase to be similar in sequence to the tetrameric enzyme of baker's yeast (Saccharomyces cerevisiae). An S. pombe cDNA library was screened using a PCR fragment generated from two oligonucleotides complementary to sequences encoding the regions at the two active-site histidine residues. The 0.63 kb cDNA encoded an open reading frame of 210 amino acids. This sequence agreed completely with sequences of peptides derived from the purified protein. The amino acid sequence of S. pombe PGAM is 43% identical with that of S. cerevisiae PGAM and shows an equally high degree of identity with BPG-dependent PGAMs from other sources. However, the sequence of the S. pombe enzyme differs from other BPG-dependent enzymes in three important ways: (i) it does not contain the alanine- and lysine-rich sequence of amino acids at the C-terminus which have been proposed to constitute a flexible tail involved in catalysis; (ii) the sequence spanning residues 122-146 (S. cerevisiae PGAM numbering) is not present in the S. pombe PGAM sequence; in the S. cerevisiae PGAM crystal structure this stretch of sequence has been shown to occur as an extended loop, part of which is involved in inter-subunit interactions; (iii) the amino acid sequence in the region of a second S. cerevisiae inter-subunit contact (residues 74-78) shows radical mutations in the S. pombe enzyme.","authors":"Nairn J, Price NC, Fothergill-Gilmore LA, Walker GE, Fothergill JE, Dunbar B","authors_abbrev":"Nairn J et al.","pubmed_publication_date":"01 Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_session_key":"db05aed8c3bd2392","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 21:50:02","canto_approved_date":"2018-12-22 21:50:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 20:27:48","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:8631292","title":"A new stress protein: synthesis of Schizosaccharomyces pombe UDP--Glc:glycoprotein glucosyltransferase mRNA is induced by stress conditions but the enzyme is not essential for cell viability.","citation":"EMBO J 1996 Feb 15;15(4):705-13","abstract":"We have identified and begun the characterization of the gene encoding UDP-Glc:glycoprotein glucosyltransferase in Schizosaccharomyces pombe. This gene, here designated gpt1, codes for a polypeptide having a signal peptide of 18 amino acids followed by 1429 amino acids with no transmembrane domain, as expected for a soluble protein of the endoplasmic reticulum (ER). The C-terminal tetrapeptide PDEL most probably corresponds to a novel ER retention signal in this fission yeast. Synthesis of the corresponding mRNA was induced 2- to 9-fold by conditions known to affect glycoprotein folding in the ER (e.g. heat shock, culture in the presence of a Ca2+ionophore, 2-mercaptoethanol or inhibitors of protein N-glycosylation such as tunicamycin or 2-deoxyglucose). This is the first evidence obtained in vivo that supports the proposed involvement of the enzyme in the quality control of glycoprotein folding in the ER. Thus far, the said involvement was inferred solely from the ability of the enzyme to glucosylate misfolded but not native glycoproteins in cell-free assays. The gpt1 gene was disrupted and gpt1- cells were found to be viable. Moreover, no significant differences in the growth rate patterns at 18, 28 or 39 degrees C or in cell morphology between gpt1+ and gpt1- cells were observed, although they differed slightly in size.","authors":"Fernandez F, Jannatipour M, Hellman U, Rokeach LA, Parodi AJ","authors_abbrev":"Fernandez F et al.","pubmed_publication_date":"15 Feb 1996","pubmed_entrez_date":"1996-02-15","publication_year":"1996","canto_session_key":"690091d99f2a514b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-31 12:18:48","canto_approved_date":"2024-12-31 12:11:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-28 14:56:00","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-03-31"},{"uniquename":"PMID:9472012","title":"The Cdk inhibitors p25rum1 and p40SIC1 are functional homologues that play similar roles in the regulation of the cell cycle in fission and budding yeast.","citation":"J Cell Sci 1998 Mar;111 ( Pt 6):843-51","abstract":"p25rum1 and p40SIC1 are specific inhibitors of p34(cdc2/CDC28) kinase complexes with B-type cyclins that play a central role in the regulation of the G1 phase of the cell cycle. We show here that low levels of expression of SIC1 in Schizosaccharomyces pombe rescues all the phenotypes of cells lacking the rum1+ gene. In addition, high level expression of SIC1 in S. pombe induces extra rounds of DNA replication without mitosis, a phenotype very similar to the overexpression of rum1+. Transient expression of rum1+ in S. cerevisiae restores the G1 arrest phenotype of cdc4 sic1Delta double mutants. Overproduction of rum1+ in Saccharomyces cerevisiae causes a cell cycle block in G1 with a phenotype similar to inactivation of all the Clb cyclins. Finally, we have mapped the cyclin interacting domain and Cdk inhibitory domain to a region of about 80 amino acids in p25rum1 that has significant homology to the C-terminal domain of p40SIC1. All these observations suggest that fission yeast p25rum1 and budding yeast p40SIC1 define a family of Cdk inhibitors that specifically down regulate cyclin B/Cdk1 during the G1 phase of the cell cycle.","authors":"Sánchez-Díaz A, González I, Arellano M, Moreno S","authors_abbrev":"Sánchez-Díaz A et al.","pubmed_publication_date":"Mar 1998","pubmed_entrez_date":"1998-05-12","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC32F12.09"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:33038513","title":"Growth media selection alters the proteome profiles of three model microorganisms.","citation":"J Proteomics 2021 Jan 16;231:104006","abstract":"The selection of growth media is a very important consideration of any cell-based proteomics experiment. Alterations thereof may result in differences in basal proteomes simply due to disparities in the metabolite composition of the media. We investigate the effect of growth media on the proteomes of three microorganisms, specifically E. coli, S. cerevisiae, and S. pombe, using tandem mass tag (TMT)-based quantitative proteomics. We compared the protein abundance profiles of these microorganisms propagated in two distinct growth media that are commonly used for the respective organism. Our sample preparation strategy included SP3 bead-assisted protein isolation and digestion. In addition, we assembled a replicate set of samples in which we altered the proteolytic digestion from sequential treatment with LysC and trypsin to only LysC. Despite differences in peptides identified and a drop in quantified proteins, the results were similar between the two datasets for all three microorganisms. Approximately 10% of the proteins of each respective microorganism were significantly altered in each dataset. As expected, gene ontology analysis revealed that the majority of differentially expressed proteins are implicated in metabolism. These data emphasize further the importance and the potential consequences of growth media selection. SIGNIFICANCE: Various microorganisms are used as model systems throughout in biological studies, including proteomics-based investigations. The growth conditions of these organisms are of utmost importance, of which one major consideration is the choice of growth media. We hypothesize that growth media selection has a considerable impact on the baseline proteome of a given microorganism. To test this hypothesis, we used tandem mass tag (TMT)-based quantitative multiplexed proteomics to profile the proteomes of E. coli, S. cerevisiae, and S. pombe each grown in two different, yet common, growth media for the respective species. Our data show that approximately 10% of the proteins of each respective microorganism were significantly altered and that many of the differentially expressed proteins are implicated in metabolism. We provide several datasets which are potentially valuable for growth media selection with respect to downstream biochemical analysis.","doi":"10.1016/j.jprot.2020.104006","authors":"Navarrete-Perea J, Gygi SP, Paulo JA","authors_abbrev":"Navarrete-Perea J et al.","pubmed_publication_date":"16 Jan 2021","pubmed_entrez_date":"2020-10-10","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-10-12 00:16:23","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30967422","title":"Negative Regulation of the Mis17-Mis6 Centromere Complex by mRNA Decay Pathway and EKC/KEOPS Complex in  Schizosaccharomyces pombe .","citation":"G3 (Bethesda) 2019 Jun 05;9(6):1815-1823","abstract":"The mitotic kinetochore forms at the centromere for proper chromosome segregation. Deposition of the centromere-specific histone H3 variant, spCENP-A/Cnp1, is vital for the formation of centromere-specific chromatin and the Mis17-Mis6 complex of the fission yeast  Schizosaccharomyces pombe  is required for this deposition. Here we identified extragenic suppressors for a Mis17-Mis6 complex temperature-sensitive (ts) mutant,  mis17-S353P , using whole-genome sequencing. The large and small daughter nuclei phenotype observed in  mis17-S353P  was greatly rescued by these suppressors. Suppressor mutations in two ribonuclease genes involved in the mRNA decay pathway,  exo2  and  pan2 , may affect Mis17 protein level, as  mis17  mutant protein level was recovered in  mis17-S353P exo2  double mutant cells. Suppressor mutations in EKC/KEOPS complex genes may not regulate Mis17 protein level, but restored centromeric localization of spCENP-A/Cnp1, Mis6 and Mis15 in  mis17-S353P  Therefore, the EKC/KEOPS complex may inhibit Mis17-Mis6 complex formation or centromeric localization. Mutational analysis in protein structure indicated that suppressor mutations in the EKC/KEOPS complex may interfere with its kinase activity or complex formation. Our results suggest that the mRNA decay pathway and the EKC/KEOPS complex negatively regulate Mis17-Mis6 complex-mediated centromere formation by distinct and unexpected mechanisms.","doi":"10.1534/g3.119.400227","authors":"Xu X, Nakazawa N, Wang L, Arakawa O, Yanagida M","authors_abbrev":"Xu X et al.","pubmed_publication_date":"05 Jun 2019","pubmed_entrez_date":"2019-04-11","publication_year":"2019","canto_session_key":"ac98af394a19cfe7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xingya Xu","canto_first_approved_date":"2019-05-19 17:01:47","canto_approved_date":"2022-09-16 13:18:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-17 20:49:18","canto_added_date":"2019-04-12 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Xingya Xu","community_curator":true,"annotation_count":7,"orcid":"0000-0002-3728-2633","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22G7.04","SPBC1105.17","SPCC895.03c","SPBP22H7.09c","SPBC21.01","SPAC6B12.18","SPBC16D10.03","SPAC17A5.14","SPAC1687.20c","SPAP27G11.07c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2019-05-19"},{"uniquename":"PMID:40205688","title":"Conserved Phosphorylation of the Myosin1e TH1 Domain Impacts Membrane Association and Function in Yeast and Worms.","citation":"Cytoskeleton (Hoboken) 2025 Apr 09;","abstract":"Cells have an intrinsic ability to rapidly respond to environmental change to regulate cell cycle progression and membrane organisation, thereby affecting cell growth and division. The actin cytoskeleton is a highly dynamic complex of proteins that can rapidly reorganise to change the growth pattern of a cell. Class I myosins are monomeric actin-associated motor proteins that play key roles in diverse cellular functions such as tension sensing and membrane reorganisation, as well as promoting actin polymer nucleation at sites of cell growth. We have analysed the localisation and function of both C. elegans class 1 myosins, HUM-1 (Myo1e) and HUM-5 (Myo1d). Both motors are non-essential. While HUM-1 is expressed in diverse cells and tissues, HUM-5 localises exclusively to a subset of cells in the nervous system. While animals lacking hum-1 displayed a reduced maximal brood size and a delay in embryo release, deleting both hum-1 and hum-5 together shortened C. elegans lifespan. Moreover, we identified that phosphorylation of a conserved serine residue within the Myo1e TH1 domain had an impact on the localisation and function of the motor protein in both C. elegans and the fission yeast, S. pombe, indicating this modification modulates the ability of Myo1e/HUM-1 to interact with phospholipids at the plasma membrane. We conclude that TH1 domain phosphorylation plays a key role in regulating the cellular distribution and function of Myo1e motors across all eukaryotes.","doi":"10.1002/cm.22026","authors":"Brooker HR, Baker K, Ezcurra M, Laissue PP, Wang L, Geeves MA, Tullet JM, Mulvihill DP","authors_abbrev":"Brooker HR et al.","pubmed_publication_date":"09 Apr 2025","pubmed_entrez_date":"2025-04-10","publication_year":"2025","canto_session_key":"f5a6f3a9cacc9a50","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-04-10 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC146.13c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11238405","title":"Transcriptional regulators of the Schizosaccharomyces pombe fbp1 gene include two redundant Tup1p-like corepressors and the CCAAT binding factor activation complex.","citation":"Genetics 2001 Mar;157(3):1205-15","abstract":"The Schizosaccharomyces pombe fbp1 gene, which encodes fructose-1,6-bis-phosphatase, is transcriptionally repressed by glucose through the activation of the cAMP-dependent protein kinase A (PKA) and transcriptionally activated by glucose starvation through the activation of a mitogen-activated protein kinase (MAPK). To identify transcriptional regulators acting downstream from or in parallel to PKA, we screened an adh-driven cDNA plasmid library for genes that increase fbp1 transcription in a strain with elevated PKA activity. Two such clones express amino-terminally truncated forms of the S. pombe tup12 protein that resembles the Saccharomyces cerevisiae Tup1p global corepressor. These clones appear to act as dominant negative alleles. Deletion of both tup12 and the closely related tup11 gene causes a 100-fold increase in fbp1-lacZ expression, indicating that tup11 and tup12 are redundant negative regulators of fbp1 transcription. In strains lacking tup11 and tup12, the atf1-pcr1 transcriptional activator continues to play a central role in fbp1-lacZ expression; however, spc1 MAPK phosphorylation of atf1 is no longer essential for its activation. We discuss possible models for the role of tup11- and tup12-mediated repression with respect to signaling from the MAPK and PKA pathways. A third clone identified in our screen expresses the php5 protein subunit of the CCAAT-binding factor (CBF). Deletion of php5 reduces fbp1 expression under both repressed and derepressed conditions. The CBF appears to act in parallel to atf1-pcr1, although it is unclear whether or not CBF activity is regulated by PKA.","authors":"Janoo RT, Neely LA, Braun BR, Whitehall SK, Hoffman CS","authors_abbrev":"Janoo RT et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-03-10","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8C9.03","SPBC1198.14c","SPBC29B5.01","SPAC18B11.10","SPBC409.07c","SPBC725.11c","SPAC21E11.03c","SPBC1D7.02c","SPBC106.10","SPAC630.14c","SPBC3B8.02"],"gene_count":11,"ltp_gene_count":10},{"uniquename":"PMID:26292216","title":"Functional equivalence of an evolutionarily conserved RNA binding module.","citation":"J Biol Chem 2015 Oct 02;290(40):24413-23","abstract":"Members of the tristetraprolin (TTP) family of proteins participate in the regulation of mRNA turnover after initially binding to AU-rich elements in target mRNAs. Related proteins from most groups of eukaryotes contain a conserved tandem zinc finger (TZF) domain consisting of two closely spaced, similar CCCH zinc fingers that form the primary RNA binding domain. There is considerable sequence variation within the TZF domains from different family members within a single organism and from different organisms, raising questions about sequence-specific effects on RNA binding and decay promotion. We hypothesized that TZF domains from evolutionarily distant species are functionally interchangeable. The single family member expressed in the fission yeast Schizosaccharomyces pombe, Zfs1, promotes the turnover of several dozen transcripts, some of which are involved in cell-cell interactions. Using knockin techniques, we replaced the TZF domain of S. pombe Zfs1 with the equivalent domains from human TTP and the single family member proteins expressed in the silkworm Bombyx mori, the pathogenic yeast Candida guilliermondii, and the plant Chromolaena odorata. We found that the TZF domains from these widely disparate species could completely substitute for the native S. pombe TZF domain, as determined by measurement of target transcript levels and the flocculation phenotype characteristic of Zfs1 deletion. Recombinant TZF domain peptides from several of these species bound to an AU-rich RNA oligonucleotide with comparably high affinity. We conclude that the TZF domains from TTP family members in these evolutionarily widely divergent species are functionally interchangeable in mRNA binding and decay.","doi":"10.1074/jbc.M115.673012","authors":"Wells ML, Hicks SN, Perera L, Blackshear PJ","authors_abbrev":"Wells ML et al.","pubmed_publication_date":"02 Oct 2015","pubmed_entrez_date":"2015-08-21","publication_year":"2015","canto_session_key":"084b345f1a30bfaa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-10-12 22:41:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-12 22:41:33","canto_added_date":"2015-08-22 00:18:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1718.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-10-12"},{"uniquename":"PMID:41258116","title":"TORC2 inactivation promotes heterochromatin formation in rDNA and prolongs viability of quiescent fission yeast cells.","citation":"Commun Biol 2025 Nov 19;8(1):1606","abstract":"A large amount of the energy produced by glucose is consumed in the biogenesis of ribosomes, the cellular machinery for protein synthesis. Recent studies suggest that a low-calorie diet and the suppression of ribosome biogenesis can extend lifespan. However, the molecular mechanisms underlying these phenomena remain elusive. Here, we demonstrate that TORC2 (TOR complex 2) promotes ribosomal RNA (rRNA) transcription by facilitating the association of Paf1C (RNA polymerase II-associated factor 1 complex) with the rDNA region. Under glucose starvation, inactivation of the TORC2-Gad8 pathway leads to the dissociation of Paf1C from rDNA, thereby promoting heterochromatin formation and transcriptional repression. This mechanism is distinct from TORC1-mediated gene regulation of rDNA. Additionally, simultaneous inactivation of the redundant TORC1 and TORC2 pathways in nutrient-rich conditions leads to robust rDNA heterochromatin formation and rRNA transcriptional suppression, which is associated with prolonged viability of quiescent cells. This extension of viability is attenuated by the disruption of the H3K9 methyltransferase Clr4. These results suggest that robust heterochromatin formation in the rDNA region may support sustained survival of quiescent cells.","doi":"10.1038/s42003-025-08953-5","authors":"Hirai H, Ohta K","authors_abbrev":"Hirai H et al.","pubmed_publication_date":"19 Nov 2025","pubmed_entrez_date":"2025-11-19","publication_year":"2025","canto_session_key":"b9d7851c29d8038c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hayato Hirai","canto_first_approved_date":"2026-02-26 09:37:53","canto_approved_date":"2026-02-26 09:37:53","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-12-25 10:52:55","canto_added_date":"2025-11-20 00:25:05","annotation_curators":[{"name":"Hayato Hirai","community_curator":true,"annotation_count":29,"orcid":"0000-0001-9811-429X","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":10,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.10c","SPBC12C2.02c","SPBC216.07c","SPBC428.08c","SPCC24B10.07","SPAPYUG7.02c","SPBC29B5.01","SPBC21B10.05c","SPAC1952.05","SPAC664.01c","SPBC13E7.08c"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2026-02-26"},{"uniquename":"PMID:26057830","title":"Circular RNA biogenesis can proceed through an exon-containing lariat precursor.","citation":"Elife 2015 Jun 09;4:e07540","abstract":"Pervasive expression of circular RNA is a recently discovered feature of eukaryotic gene expression programs, yet its function remains largely unknown. The presumed biogenesis of these RNAs involves a non-canonical 'backsplicing' event. Recent studies in mammalian cell culture posit that backsplicing is facilitated by inverted repeats flanking the circularized exon(s). Although such sequence elements are common in mammals, they are rare in lower eukaryotes, making current models insufficient to describe circularization. Through systematic splice site mutagenesis and the identification of splicing intermediates, we show that circular RNA in Schizosaccharomyces pombe is generated through an exon-containing lariat precursor. Furthermore, we have performed high-throughput and comprehensive mutagenesis of a circle-forming exon, which enabled us to discover a systematic effect of exon length on RNA circularization. Our results uncover a mechanism for circular RNA biogenesis that may account for circularization in genes that lack noticeable flanking intronic secondary structure.","doi":"10.7554/eLife.07540","authors":"Barrett SP, Wang PL, Salzman J","authors_abbrev":"Barrett SP et al.","pubmed_publication_date":"09 Jun 2015","pubmed_entrez_date":"2015-06-10","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-06-11 00:20:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12896976","title":"Schizosaccharomyces pombe cells lacking the Ran-binding protein Hba1 show a multidrug resistance phenotype due to constitutive nuclear accumulation of Pap1.","citation":"J Biol Chem 2003 Oct 17;278(42):40565-72","abstract":"In Schizosaccharomyces pombe, the transcription factor Pap1, and the mitogen-activated protein kinase Sty1 are excluded from the nucleus in a Crm1-dependent manner under non-stressed conditions. Upon oxidant treatment, both Sty1 and Pap1 concentrate into the nucleus, due to an enhanced import or an impaired export. Hba1, a protein that when overexpressed confers brefeldin A resistance, contains a Ran binding domain. The purpose of this project was to understand at the molecular level the role of Hba1 in the S. pombe oxidative stress response. Fluorescent and confocal microscopy studies demonstrate that Hba1 is located at the nucleoplasm and not at the nuclear envelope. We also demonstrate that either multiple copies or deletion of the hba1 gene induces nuclear accumulation of Pap1 and Sty1. We propose that Hba1 assists Crm1 to export some nuclear export signal-containing proteins. Pap1 nuclear accumulation is sufficient for constitutive activation of its specific antioxidant response. On the contrary, constitutive nuclear localization of Sty1 in the Deltahba1 strain does not trigger the Sty1-specific, Atf1-dependent antioxidant response in the absence of stress. We conclude that the increased multidrug resistance of strains lacking or overexpressing Hba1 is due to the accumulation of Pap1 in the nucleus under non-stressed conditions.","authors":"Castillo EA, Vivancos AP, Jones N, Ayte J, Hidalgo E","authors_abbrev":"Castillo EA et al.","pubmed_publication_date":"17 Oct 2003","pubmed_entrez_date":"2003-08-05","publication_year":"2003","canto_session_key":"2898cdc2a698835a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 20:36:20","canto_approved_date":"2020-05-26 16:16:58","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-08-22 13:29:34","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.13c","SPAC1783.07c","SPBC29B5.01","SPAC1805.17","SPAC24B11.06c","SPAC3C7.14c","SPBC32F12.03c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2019-01-30"},{"uniquename":"PMID:8590799","title":"The N-terminus of fission yeast DNA polymerase alpha contains a basic pentapeptide that acts in vivo as a nuclear localization signal.","citation":"Mol Biol Cell 1995 Dec;6(12):1697-705","abstract":"The N-terminal sequence of the catalytic subunit of fission yeast DNA polymerase alpha (pol alpha) contains two putative nuclear localization signals (NLS). To check the functionality of these signals in vivo, the N-terminal sequence was experimentally divided into three amino acid blocks, two of which contain a distinct presumptive NLS. Each block was deleted, either individually or in combination with one of the two others. The deleted gene products were expressed in fission yeast, and assayed by indirect immunofluorescence for their aptitude to localize to the cell nucleus. Block II, which contains the putative NLS pentapeptide 97RKRKK, was both necessary and sufficient to promote nuclear import of pol alpha, as well as of a pyruvate kinase fusion protein. Precise excision of the NLS pentapeptide from block II inhibited the nuclear import of pol alpha, thus confirming the role of this sequence as the functional NLS of the fission yeast enzyme.","authors":"Bouvier D, Baldacci G","authors_abbrev":"Bouvier D et al.","pubmed_publication_date":"Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"b441e982b7d11e0f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-07-22 13:30:11","canto_approved_date":"2021-11-10 16:38:28","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-22 13:29:58","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-07-22"},{"uniquename":"PMID:20231361","title":"Separable functions of the fission yeast Spt5 carboxyl-terminal domain (CTD) in capping enzyme binding and transcription elongation overlap with those of the RNA polymerase II CTD.","citation":"Mol Cell Biol 2010 May;30(10):2353-64","abstract":"An interaction network connecting mRNA capping enzymes, the RNA polymerase II (Pol II) carboxyl-terminal domain (CTD), elongation factor Spt5, and the Cdk7 and Cdk9 protein kinases is thought to comprise a transcription elongation checkpoint. A crux of this network is Spt5, which regulates early transcription elongation and has an imputed role in pre-mRNA processing via its physical association with capping enzymes. Schizosaccharomyces pombe Spt5 has a distinctive CTD composed of tandem nonapeptide repeats of the consensus sequence (1)TPAWNSGSK(9). The Spt5 CTD binds the capping enzymes and is a substrate for threonine phosphorylation by the Cdk9 kinase. Here we report that deletion of the S. pombe Spt5 CTD results in slow growth and aberrant cell morphology. The severity of the spt5-DeltaCTD phenotype is exacerbated by truncation of the Pol II CTD and ameliorated by overexpression of the capping enzymes RNA triphosphatase and RNA guanylyltransferase. These results suggest that the Spt5 and Pol II CTDs play functionally overlapping roles in capping enzyme recruitment. We probed structure-activity relations of the Spt5 CTD by alanine scanning of the consensus nonapeptide. The T1A change abolished CTD phosphorylation by Cdk9 but did not affect CTD binding to the capping enzymes. The T1A and P2A mutations elicited cold-sensitive (cs) and temperature-sensitive (ts) growth defects and conferred sensitivity to growth inhibition by 6-azauracil that was exacerbated by partial truncations of the Pol II CTD. The T1A phenotypes were rescued by a phosphomimetic T1E change but not by capping enzyme overexpression. These results imply a positive role for Spt5 CTD phosphorylation in Pol Il transcription elongation in fission yeast, distinct from its capping enzyme interactions. Viability of yeast cells bearing both Spt5 CTD T1A and Pol II CTD S2A mutations heralds that the Cdk9 kinase has an essential target other than Spt5 and Pol II CTD-Ser2.","doi":"10.1128/MCB.00116-10","authors":"Schneider S, Pei Y, Shuman S, Schwer B","authors_abbrev":"Schneider S et al.","pubmed_publication_date":"May 2010","pubmed_entrez_date":"2010-03-17","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPAC23C4.19","SPBC2F12.08c","SPAC644.04"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:17072890","title":"Homologous chromosome pairing in Schizosaccharomyces pombe.","citation":"Yeast 2006 Oct 15;23(13):977-89","abstract":"Homologous chromosome pairing is a central feature of meiosis I, contributing to the correct segregation of chromosomes during meiosis. The fission yeast, Schizosaccharomyces pombe, has been widely used to study meiotic chromosome dynamics, partly because studies in this yeast are simplified due to the lack of post-pairing synaptic structures. Chromosome pairing in Sz. pombe occurs differentially throughout the genome. Telomeres cluster at the spindle pole body (SPB) at the onset of meiosis, imposing a spatial restriction on pairing events. Subsequently, centromeres dissociate from the SPB and pair in a recombination- and heterochromatin (Swi6)-independent fashion. Pairing of telomere distal regions occurs during meiotic prophase, concomitant with a dynamic association/dissociation of homologous regions, with interhomologue associations becoming increasingly stable. The stabilization of paired regions is enhanced by factors required for the initiation of meiotic recombination, suggesting that recombination stabilizes paired regions. However, substantial pairing is initiated in the absence of recombination; this is dependent upon another factor, the conserved Meu13 protein, demonstrating that recombination is not required for initial pairing interactions. During meiotic prophase Sz. pombe exhibits a pronounced dynein-dependent nuclear oscillation, which drives the pairing of centromeric and interstitial regions. Dynein is also required for the significant levels of achiasmate reductional segregation observed in Sz. pombe, possibly implicating the centromere-associated pairing with achiasmate homologue segregation. Whilst Sz. pombe does not form discernable synaptic structures continuously along the meiotic chromosomes, it does form proteinacious, meiosis-specific, linear structures (linear elements). However, the role, if any, of these structures in mediating homologue pairing is unknown.","authors":"Wells JL, Pryce DW, McFarlane RJ","authors_abbrev":"Wells JL et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22240020","title":"Characterization of the ptr5+ gene involved in nuclear mRNA export in fission yeast.","citation":"Biochem Biophys Res Commun 2012 Feb 03;418(1):62-6","abstract":"To analyze the mechanisms of mRNA export from the nucleus to the cytoplasm, we have isolated eleven mutants, ptr [poly(A)(+) RNA transport] 1 to 11, which accumulate poly(A)(+) RNA in the nucleus at a nonpermissive temperature in Schizosaccharomyces pombe. Of those, the ptr5-1 mutant shows dots- or a ring-like accumulation of poly(A)(+) RNA at the nuclear periphery after shifting to the nonpermissive temperature. We cloned the ptr5(+) gene and found that it encodes a component of the nuclear pore complex (NPC), nucleoporin 85 (Nup85). The ptr5-1 mutant shows no defects in protein transport, suggesting the specific involvement of Ptr5p/Nup85p in nuclear mRNA export in S. pombe. We identified Seh1p, a nucleoporin interacting with Nup85p, an mRNA-binding protein Mlo3p, and Sac3p, a component of the TREX-2 complex involved in coupling of nuclear mRNA export with transcription, as multi-copy suppressors for the ptr5-1 mutation. In addition, we found that the ptr5-1 mutation is synthetically lethal with a mutation of the mRNA export factor Rae1p, and that the double mutant exaggerates defective nuclear mRNA export, suggesting that Ptr5p/Nup85p is involved in nuclear mRNA export through Rae1p. Interestingly, the ptr5-1 mutation also showed synthetic effects with several prp pre-mRNA splicing mutations, suggesting a functional linkage between the NPCs and the splicing apparatus in the yeast nucleus.","doi":"10.1016/j.bbrc.2011.12.128","authors":"Watanabe N, Ikeda T, Mizuki F, Tani T","authors_abbrev":"Watanabe N et al.","pubmed_publication_date":"03 Feb 2012","pubmed_entrez_date":"2012-01-14","publication_year":"2012","canto_session_key":"2385d15c265b7f6a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-05-25 09:05:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-04-25 05:55:51","canto_added_date":"2012-02-17 18:08:23","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.05c","SPAC27F1.09c","SPBC146.07","SPAC3A12.11c","SPBC17G9.04c","SPBC19C2.01","SPAC15F9.02","SPCC576.05","SPBC1D7.04","SPAC29E6.02","SPBC6B1.07"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2012-04-25"},{"uniquename":"PMID:18429817","title":"Bood POZ containing gene type 2 is a human counterpart of yeast Btb3p and promotes the degradation of terminal deoxynucleotidyltransferase.","citation":"Genes Cells 2008 May;13(5):439-57","abstract":"Bood POZ containing gene type 2 (BPOZ-2) is involved in the growth suppressive effect of the phosphatase and tensin homologue (PTEN). We showed that BPOZ-2 is a human counterpart of yeast Btb3p, which is a putative adaptor for Pcu3p-based ubiquitin ligase. BPOZ-2 bound to E3 ligase CUL3 in vitro and in vivo. BPOZ-2 itself was ubiquitinated through the CUL3-based E3 ligase mainly within the nucleus and degraded by the 26S proteasome. Although BPOZ-2 was mainly expressed within the cytoplasm, it accumulated within the nucleus in the presence of the specific 26S proteasome inhibitor MG132. BPOZ-2 may be recruited to the nucleus from the cytoplasm. Terminal deoxynucleotidyltransferase (TdT) was detected as a BPOZ-2-binding protein using a yeast two-hybrid system by screening a human thymus cDNA library. TdT, BPOZ-2, and CUL3 formed a ternary complex in vivo. TdT was ubiquitinated only within the nucleus and degraded by the 26S proteasome. The ubiqutination or degradation of TdT was markedly promoted by co-expression of BPOZ-2 and CUL3 or BPOZ-2 in 293T cells, respectively.","doi":"10.1111/j.1365-2443.2008.01179.x","authors":"Maezawa S, Hayano T, Koiwai K, Fukushima R, Kouda K, Kubota T, Koiwai O","authors_abbrev":"Maezawa S et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-04-24","publication_year":"2008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:18275","SPAC13D6.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12805221","title":"Schizosaccharomyces pombe AGC family kinase Gad8p forms a conserved signaling module with TOR and PDK1-like kinases.","citation":"EMBO J 2003 Jun 16;22(12):3073-83","abstract":"The TOR protein is a phosphoinositide kinase-related kinase widely conserved among eukaryotes. Fission yeast tor1 encodes an ortholog of TOR, which is required for sexual development and growth under stressed conditions. We isolated gad8, which encodes a Ser/Thr kinase of the AGC family, as a high-copy suppressor of the sterility of a tor1 mutant. Disruption of gad8 caused phenotypes similar to those of tor1 disruption. Gad8p was less phosphorylated and its kinase activity was undetectable in tor1Delta cells. Three amino acid residues corresponding to conserved phosphorylation sites in the AGC family kinases, namely Thr387 in the activation loop, Ser527 in the turn motif and Ser546 in the hydrophobic motif, were important for the kinase activity of Gad8p. Tor1p was responsible for the phosphorylation of Ser527 and Ser546, whereas Ksg1p, a PDK1-like kinase, appeared to phosphorylate Thr387 directly. Altogether, Tor1p, Ksg1p and Gad8p appear to constitute a signaling module for sexual development and growth under stressed conditions in fission yeast, which resembles the mTOR-PDK1-S6K1 system in mammals and may represent a basic signaling module ubiquitous in eukaryotes.","authors":"Matsuo T, Kubo Y, Watanabe Y, Yamamoto M","authors_abbrev":"Matsuo T et al.","pubmed_publication_date":"16 Jun 2003","pubmed_entrez_date":"2003-06-14","publication_year":"2003","canto_session_key":"9a10046246e64418","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 16:30:14","canto_approved_date":"2026-04-11 20:22:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-18 18:12:10","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":51,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC24B10.07","SPCC576.15c","SPBC30D10.10c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-10-31"},{"uniquename":"PMID:11907263","title":"Distinct regulatory proteins control the graded transcriptional response to increasing H(2)O(2) levels in fission yeast Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2002 Mar;13(3):805-16","abstract":"The signaling pathways that sense adverse stimuli and communicate with the nucleus to initiate appropriate changes in gene expression are central to the cellular stress response. Herein, we have characterized the role of the Sty1 (Spc1) stress-activated mitogen-activated protein kinase pathway, and the Pap1 and Atf1 transcription factors, in regulating the response to H(2)O(2) in the fission yeast Schizosaccharomyces pombe. We find that H(2)O(2) activates the Sty1 pathway in a dose-dependent manner via at least two sensing mechanisms. At relatively low levels of H(2)O(2), a two component-signaling pathway, which feeds into either of the two stress-activated mitogen-activated protein kinase kinase kinases Wak1 or Win1, regulates Sty1 phosphorylation. In contrast, at high levels of H(2)O(2), Sty1 activation is controlled predominantly by a two-component independent mechanism and requires the function of both Wak1 and Win1. Individual transcription factors were also found to function within a limited range of H(2)O(2) concentrations. Pap1 activates target genes primarily in response to low levels of H(2)O(2), whereas Atf1 primarily controls the transcriptional response to high concentrations of H(2)O(2). Our results demonstrate that S. pombe uses a combination of stress-responsive regulatory proteins to gauge and effect the appropriate transcriptional response to increasing concentrations of H(2)O(2).","authors":"Quinn J, Findlay VJ, Dawson K, Millar JB, Jones N, Morgan BA, Toone WM","authors_abbrev":"Quinn J et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-22","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPBC29B5.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:38889144","title":"Cytoplasmic fluidization contributes to breaking spore dormancy in fission yeast.","citation":"Proc Natl Acad Sci U S A 2024 Jun 25;121(26):e2405553121","abstract":"The cytoplasm is a complex, crowded environment that influences myriad cellular processes including protein folding and metabolic reactions. Recent studies have suggested that changes in the biophysical properties of the cytoplasm play a key role in cellular homeostasis and adaptation. However, it still remains unclear how cells control their cytoplasmic properties in response to environmental cues. Here, we used fission yeast spores as a model system of dormant cells to elucidate the mechanisms underlying regulation of the cytoplasmic properties. By tracking fluorescent tracer particles, we found that particle mobility decreased in spores compared to vegetative cells and rapidly increased at the onset of dormancy breaking upon glucose addition. This cytoplasmic fluidization depended on glucose-sensing via the cyclic adenosine monophosphate-protein kinase A pathway. PKA activation led to trehalose degradation through trehalase Ntp1, thereby increasing particle mobility as the amount of trehalose decreased. In contrast, the rapid cytoplasmic fluidization did not require de novo protein synthesis, cytoskeletal dynamics, or cell volume increase. Furthermore, the measurement of diffusion coefficients with tracer particles of different sizes suggests that the spore cytoplasm impedes the movement of larger protein complexes (40 to 150 nm) such as ribosomes, while allowing free diffusion of smaller molecules (~3 nm) such as second messengers and signaling proteins. Our experiments have thus uncovered a series of signaling events that enable cells to quickly fluidize the cytoplasm at the onset of dormancy breaking.","doi":"10.1073/pnas.2405553121","authors":"Sakai K, Kondo Y, Goto Y, Aoki K","authors_abbrev":"Sakai K et al.","pubmed_publication_date":"25 Jun 2024","pubmed_entrez_date":"2024-06-18","publication_year":"2024","canto_session_key":"c5b0c32f69a1468d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kazuhiro Aoki","canto_first_approved_date":"2024-10-16 11:55:09","canto_approved_date":"2024-10-16 11:55:11","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-09-28 06:36:09","canto_added_date":"2024-06-18 23:25:05","annotation_curators":[{"name":"Kazuhiro Aoki","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":6,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPBC106.10","SPBC660.07","SPAC23H3.13c","SPCC1753.02c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2024-10-16"},{"uniquename":"EMBL:AU008776","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19427212","title":"Spatial control of cytokinesis by Cdr2 kinase and Mid1/anillin nuclear export.","citation":"Curr Biol 2009 Jun 09;19(11):961-6","abstract":"Maintaining genome integrity and cellular function requires proper positioning of the cell division plane. In most eukaryotes, cytokinesis relies on a contractile actomyosin ring positioned by intrinsic spatial signals that are poorly defined at the molecular level. Fission yeast cells assemble a medial contractile ring in response to positive spatial cues from the nucleus at the cell center and negative spatial cues from the cell tips. These signals control the localization of the anillin-like protein Mid1, which defines the position of the division plane at the medial cortex, where it recruits contractile-ring components at mitosis onset. Here we show that Cdr2 kinase anchors Mid1 at the medial cortex during interphase through association with the Mid1 N terminus. This association underlies the negative regulation of Mid1 distribution by cell tips. We also demonstrate that the positive signaling from the nucleus is based on Mid1 nuclear export, which links division-plane position to nuclear position during early mitosis. After nuclear displacement, Mid1 nuclear export is dominant over Cdr2-dependent positioning of Mid1. We conclude that Cdr2- and nuclear export-dependent positioning of Mid1 constitute two overlapping mechanisms that relay cell polarity and nuclear positional information to ensure proper division-plane specification.","doi":"10.1016/j.cub.2009.04.024","authors":"Almonacid M, Moseley JB, Janvore J, Mayeux A, Fraisier V, Nurse P, Paoletti A","authors_abbrev":"Almonacid M et al.","pubmed_publication_date":"09 Jun 2009","pubmed_entrez_date":"2009-05-12","publication_year":"2009","canto_session_key":"889ae07851beec32","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-23 09:57:45","canto_approved_date":"2024-06-26 16:23:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-12 14:57:30","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":24,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPAC57A10.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-04-23"},{"uniquename":"PMID:17412958","title":"A conserved family of enzymes that phosphorylate inositol hexakisphosphate.","citation":"Science 2007 Apr 06;316(5821):106-9","abstract":"Inositol pyrophosphates are a diverse group of high-energy signaling molecules whose cellular roles remain an active area of study. We report a previously uncharacterized class of inositol pyrophosphate synthase and find it is identical to yeast Vip1 and Asp1 proteins, regulators of actin-related protein-2/3 (ARP 2/3) complexes. Vip1 and Asp1 acted as enzymes that encode inositol hexakisphosphate (IP6) and inositol heptakisphosphate (IP7) kinase activities. Alterations in kinase activity led to defects in cell growth, morphology, and interactions with ARP complex members. The functionality of Asp1 and Vip1 may provide cells with increased signaling capacity through metabolism of IP6.","authors":"Mulugu S, Bai W, Fridy PC, Bastidas RJ, Otto JC, Dollins DE, Haystead TA, Ribeiro AA, York JD","authors_abbrev":"Mulugu S et al.","pubmed_publication_date":"06 Apr 2007","pubmed_entrez_date":"2007-04-07","publication_year":"2007","canto_session_key":"88a0961bc71fcefc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-21 13:05:17","canto_approved_date":"2024-08-21 13:05:17","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-21 13:05:11","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":15,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.06c","SPAC630.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-08-21"},{"uniquename":"PMID:26305173","title":"When two is not enough: a CtIP tetramer is required for DNA repair by Homologous Recombination.","citation":"Nucleus 2015;6(5):344-8","abstract":"Homologous recombination (HR) is central to the repair of double-strand DNA breaks that occur in S/G2 phases of the cell cycle. HR relies on the CtIP protein (Ctp1 in fission yeast, Sae2 in budding yeast) for resection of DNA ends, a key step in generating the 3'-DNA overhangs that are required for the HR strand-exchange reaction. Although much has been learned about the biological importance of CtIP in DNA repair, our mechanistic insight into its molecular functions remains incomplete. It has been recently discovered that CtIP and Ctp1 share a conserved tetrameric architecture that is mediated by their N-terminal domains and is critical for their function in HR. The specific arrangement of protein chains in the CtIP/Ctp1 tetramer indicates that an ability to bridge DNA ends might be an important feature of CtIP/Ctp1 function, establishing an intriguing similarity with the known ability of the MRE11-RAD50-NBS1 complex to link DNA ends. Although the exact mechanism of action remains to be elucidated, the remarkable evolutionary conservation of CtIP/Ctp1 tetramerisation clearly points to its crucial role in HR.","doi":"10.1080/19491034.2015.1086050","authors":"Forment JV, Jackson SP, Pellegrini L","authors_abbrev":"Forment JV et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-08-26","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-08-27 00:18:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR28139","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YBL029C-A","SPBPB2B2.18"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7773391","title":"A temperature-compensated ultradian clock ticks in Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 1995 Apr;141 ( Pt 4):883-90","abstract":"An ultradian oscillation is described for Schizosaccharomyces pombe which meets the criteria for a cellular clock, i.e. timekeeping device. The rhythm can be induced by transfer from circadian conditions (stationary phase or very slow growth) to ultradian conditions (rapid growth). It can also be synchronized by ultradian temperature cycles of 6 degrees C difference. Released to constant temperature, the rhythm persists for 20 h without damping. The period of the free-running rhythm is temperature-compensated and in no experiment did period length fall outside the narrow range between 40 and 44 min. The parameter observed is the septum index, i.e. the percentage of cells occupying the last stage of the cell cycle in wild-type cells before final division. The results suggest control of the cell division processes by the ultradian clock.","authors":"Kippert F, Lloyd D","authors_abbrev":"Kippert F et al.","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11513961","title":"Characterization and regulation of glutathione S-transferase gene from Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2001 Aug 30;1520(2):179-85","abstract":"A glutathione S-transferase (GST) gene has been cloned from Schizosaccharomyces pombe for the first time. The nucleotide sequence determined was found to contain 2030 base pairs including an open reading frame of 229 amino acids that would encode a protein of a molecular mass of 27017 Da. The cloned GST gene was expressed and was found to function in S. pombe, Saccharomyces cerevisiae, and Escherichia coli. The plasmid pGT207 encoding the S. pombe GST gene appeared to be able to accelerate the growth of a wild type S. pombe culture. In a culture of S. pombe containing plasmid pGT207, the growth was inhibited less by mercuric chloride than in a culture with vector alone. The 1088 bp region upstream from the GST gene as well as the region encoding the N-terminal 14 amino acids was transferred into the promoterless beta-galactosidase gene of plasmid YEp357R to yield the fusion plasmid pYSH2000. beta-Galactosidase synthesis was induced by cadmium chloride, mercuric chloride, hydrogen peroxide, and menadione. It was also induced by high temperature. These results suggest that the cloned S. pombe GST gene is involved in the oxidative stress response.","authors":"Kim HG, Park KN, Cho YW, Park EH, Fuchs JA, Lim CJ","authors_abbrev":"Kim HG et al.","pubmed_publication_date":"30 Aug 2001","pubmed_entrez_date":"2001-08-22","publication_year":"2001","canto_session_key":"6e59492bc6f8a8f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:54:35","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 14:47:33","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC191.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-05"},{"uniquename":"PMID:9135147","title":"Spm1, a stress-activated MAP kinase that regulates morphogenesis in S.pombe.","citation":"EMBO J 1997 Mar 17;16(6):1318-31","abstract":"A gene encoding a novel MAP kinase family member, Spm1, was isolated from the fission yeast Schizosaccharomyces pombe. Overproduction of Spm1 inhibits proliferation. Disruption of the spm1+ gene interferes with cell separation and morphogenesis. Under conditions of nutrient limitation, hypertonic stress or elevated temperature, spm1 delta cells grow as short branched filaments in which the cell walls and septa are thickened, suggesting defects in polarized growth and cell wall remodeling. At high osmolarity, spm1 delta cells fail to form colonies. The Spm1 protein is tyrosine phosphorylated and activated in response to osmotic and heat stress, consistent with a role for Spm1 in adaptation to these conditions. Two other S.pombe MAP kinases are known, Spk1, required for sexual differentiation and sporulation, and Spc1/Sty1/Phh1, which is activated in hypertonic conditions. However, the distinctive features of the spm1 delta mutant phenotype and direct biochemical assays suggest that Spm1 does not lie on other known MAP kinase pathways. Our results demonstrate the existence of a new MAP kinase pathway that regulates cell wall remodeling and cytokinesis in response to environmental stresses.","authors":"Zaitsevskaya-Carter T, Cooper JA","authors_abbrev":"Zaitsevskaya-Carter T et al.","pubmed_publication_date":"17 Mar 1997","pubmed_entrez_date":"1997-03-17","publication_year":"1997","canto_session_key":"67ba83cbaba024a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-28 15:43:24","canto_approved_date":"2020-01-17 12:15:41","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-08-14 14:31:35","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.08","SPBC409.07c","SPAC31G5.09c","SPAC1D4.13","SPBC12D12.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-10-28"},{"uniquename":"PMID:10506761","title":"RHO GTPases in the control of cell morphology, cell polarity, and actin localization in fission yeast.","citation":"Microsc Res Tech 1999 Oct 01;47(1):51-60","abstract":"The fission yeast Schizosaccharomyces pombe undergoes morphogenetic changes during both vegetative and sexual cell cycles that require asymmetric cell growth and actin cytoskeleton reorganisations. Different complex signal transduction pathways participate in S. pombe morphogenesis. The Rho family of GTPases are present in all eukaryotic cells, from yeast to mammals, and their role as key regulators in the signalling pathways that control actin organisation and morphogenetic processes is well known. In this review, we will briefly summarize the role of the Rho GTPases in the establishment and maintenance of cell polarity and growth of S. pombe. As in other fungi, S. pombe morphogenesis is closely related to cell wall biosynthesis, and Rho GTPases are critical modulators of this process. They provide the coordinated regulation of cell wall biosynthetic enzymes and actin organisation required to maintain cell integrity and polarised growth.","authors":"Arellano M, Coll PM, Pérez P","authors_abbrev":"Arellano M et al.","pubmed_publication_date":"01 Oct 1999","pubmed_entrez_date":"1999-10-03","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21757403","title":"Schizosaccharomyces pombe Pep12p is required for vacuolar protein transport and vacuolar homotypic fusion.","citation":"J Biosci Bioeng 2011 Oct;112(4):309-14","abstract":"In eukaryotic cells, SNARE proteins are essential for intracellular vesicle trafficking. Several SNARE proteins are required for vacuolar protein transport and vacuolar biogenesis in Saccharomyces cerevisiae. Previously we demonstrated that one of the fission yeast SNARE proteins, Pep12p, is not required for vacuolar fusion process in Schizosaccharomyces pombe. We have re-examined the function of S. pombe Pep12p using the newly created pep12(+) deletion strain. Deletion of the fission yeast pep12(+) gene results in pleiotropic phenotypes consistent with the absence of normal vacuoles, including missorting of vacuolar carboxypeptidase Y-and various ion- and drug-sensitivities. GFP-Pep12 fusion protein is mostly localized at the vacuolar membrane and the prevacuolar compartment. The S. pombe pep12Δ mutation phenocopies that of vps33Δ, suggesting that both Pep12p and Vps33p act at the same membrane fusion step in S. pombe, and both mutations cause vacuolar deficiency.","doi":"10.1016/j.jbiosc.2011.06.009","authors":"Hosomi A, Nakase M, Takegawa K","authors_abbrev":"Hosomi A et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-07-16","publication_year":"2011","canto_session_key":"f6417d0fe2233b57","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-07-16 14:25:18","canto_approved_date":"2026-05-29 11:56:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-22 11:01:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC458.05","SPAC19G12.10c","SPBC31E1.04","SPBC1703.15c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2014-07-16"},{"uniquename":"EMBL:AU009778","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7991582","title":"Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases.","citation":"Proc Natl Acad Sci U S A 1994 Dec 06;91(25):12046-50","abstract":"Formation of the 5' cap structure of eukaryotic mRNAs occurs via transfer of GMP from GTP to the 5' terminus of the primary transcript. RNA guanylyltransferase, the enzyme that catalyzes this reaction, has been isolated from many viral and cellular sources. Though differing in molecular weight and subunit structure, the various guanylyltransferases employ a common catalytic mechanism involving a covalent enzyme-(Lys-GMP) intermediate. Saccharomyces cerevisiae CEG1 is the sole example of a cellular capping enzyme gene. In this report, we describe the identification and characterization of the PCE1 gene encoding the capping enzyme from Schizosaccharomyces pombe. PCE1 was isolated from a cDNA library by functional complementation in Sa. cerevisiae. Induced expression of PCE1 in bacteria and in yeast confirmed that the 47-kDa Sc. pombe protein was enzymatically active. The amino acid sequence of PCE1 is 38% identical (152 of 402 residues) to the 52-kDa capping enzyme from Sa. cerevisiae. Comparison of the two cellular capping enzymes with guanylyltransferases encoded by DNA viruses revealed local sequence similarity at the enzyme's active site and at four additional collinear motifs. Mutational analysis of yeast CEG1 demonstrated that four of the five conserved motifs are essential for capping enzyme function in vivo. Remarkably, the same motifs are conserved in the polynucleotide ligase family of enzymes that employ an enzyme-(Lys-AMP) intermediate. These findings illuminate a shared structural basis for covalent catalysis in nucleotidyl transfer and suggest a common evolutionary origin for capping enzymes and ligases.","authors":"Shuman S, Liu Y, Schwer B","authors_abbrev":"Shuman S et al.","pubmed_publication_date":"06 Dec 1994","pubmed_entrez_date":"1994-12-06","publication_year":"1994","canto_session_key":"66d4b91126b26c13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-09-09 10:25:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-08 17:11:49","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-09-08"},{"uniquename":"PMID:8441660","title":"Cloning and sequence determination of the Schizosaccharomyces pombe rpb2 gene encoding the subunit 2 of RNA polymerase II.","citation":"Nucleic Acids Res 1993 Feb 11;21(3):469-73","abstract":"The gene, rpb2, encoding the second largest subunit, subunit 2, of RNA polymerase II has been cloned from Schizosaccharomyces pombe using the corresponding gene, RPB2, of Saccharomyces cerevisiae as a probe for cross-hybridization. We have determined the complete nucleotide sequence of rpb2, and parts of the PCR-amplified rpb2 cDNA. The predicted coding sequence of a polypeptide of 1210 amino acid residues with a calculated molecular weight of 138 kilodaltons was interrupted by a short intron. The overall amino acid sequence homology of the S. pombe subunit 2 is 68, 62 and 62% with the corresponding protein from S. cerevisiae, D. melanogaster and H. sapiens, respectively. Southern analysis of the genomic DNA digested with various restriction enzymes showed that rpb2 was present as a single copy in the S. pombe genome. Northern analysis showed that the transcript of rpb2 was about 4 kb in length.","authors":"Kawagishi M, Yamagishi M, Ishihama A","authors_abbrev":"Kawagishi M et al.","pubmed_publication_date":"11 Feb 1993","pubmed_entrez_date":"1993-02-11","publication_year":"1993","canto_session_key":"16ab20d5c9c0195f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 14:16:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 14:16:49","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23G3.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:10588642","title":"Nuclear localization of Schizosaccharomyces pombe Mcm2/Cdc19p requires MCM complex assembly.","citation":"Mol Biol Cell 1999 Dec;10(12):4043-57","abstract":"The minichromosome maintenance (MCM) proteins MCM2-MCM7 are conserved eukaryotic replication factors that assemble in a heterohexameric complex. In fission yeast, these proteins are nuclear throughout the cell cycle. In studying the mechanism that regulates assembly of the MCM complex, we analyzed the cis and trans elements required for nuclear localization of a single subunit, Mcm2p. Mutation of any single mcm gene leads to redistribution of wild-type MCM subunits to the cytoplasm, and this redistribution depends on an active nuclear export system. We identified the nuclear localization signal sequences of Mcm2p and showed that these are required for nuclear targeting of other MCM subunits. In turn, Mcm2p must associate with other MCM proteins for its proper localization; nuclear localization of MCM proteins thus requires assembly of MCM proteins in a complex. We suggest that coupling complex assembly to nuclear targeting and retention ensures that only intact heterohexameric MCM complexes remain nuclear.","authors":"Pasion SG, Forsburg SL","authors_abbrev":"Pasion SG et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-12-10","publication_year":"1999","canto_session_key":"062614007433f668","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-11 10:45:08","canto_approved_date":"2022-08-03 09:31:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-05 15:30:25","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":61,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1682.02c","SPBC29A10.15","SPCC16A11.17","SPBC4.04c","SPAC1F7.05","SPAC1805.17","SPAC3H5.06c","SPAC20G8.01","SPBC211.04c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2015-06-11"},{"uniquename":"EMBL:AU012391","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26412298","title":"A Degenerate Cohort of Yeast Membrane Trafficking DUBs Mediates Cell Polarity and Survival.","citation":"Mol Cell Proteomics 2015 Dec;14(12):3132-41","abstract":"Deubiquitinating enzymes (DUBs), cysteine or metallo- proteases that cleave ubiquitin chains or protein conjugates, are present in nearly every cellular compartment, with overlapping protein domain structure, localization, and functions. We discovered a cohort of DUBs that are involved in membrane trafficking (ubp4, ubp5, ubp9, ubp15, and sst2) and found that loss of all five of these DUBs but not loss of any combination of four, significantly impacted cell viability in the fission yeast Schizosaccharomyces pombe (1). Here, we delineate the collective and individual functions and activities of these five conserved DUBs using comparative proteomics, biochemistry, and microscopy. We find these five DUBs are degenerate rather than redundant at the levels of cell morphology, substrate selectivity, ubiquitin chain specificity, and cell viability under stress. These studies reveal the complexity of interplay among these enzymes, providing a foundation for understanding DUB biology and providing another example of how cells utilize degeneracy to improve survival.","doi":"10.1074/mcp.M115.050039","authors":"Beckley JR, Chen JS, Yang Y, Peng J, Gould KL","authors_abbrev":"Beckley JR et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-09-29","publication_year":"2015","canto_session_key":"7881e95072db6f1d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Janel beckley","canto_first_approved_date":"2017-12-15 14:40:00","canto_approved_date":"2025-09-04 09:36:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-11 20:04:48","canto_added_date":"2015-09-30 00:18:55","annotation_curators":[{"name":"Janel beckley","community_curator":true,"annotation_count":493,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":70,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1085,"orcid":"0000-0003-4148-4606","file_type":"protein_modification","file_name":"PMID_26412298_modifications.tsv"}],"genes":["SPAC1565.08","SPAC31G5.03","SPBC119.10","SPAC1071.07c","SPBC336.15","SPAC17G6.16c","SPCC1827.03c","SPBC11B10.07c","SPBC119.05c","SPBC1711.08","SPAC890.08","SPAC9E9.04","SPBC14F5.04c","SPAC977.14c","SPCC4G3.17","SPBC21H7.02","SPCC18.16c","SPBC12C2.04","SPAC1834.03c","SPAC4A8.11c","SPBP16F5.03c","SPCC162.08c","SPAC823.03","SPAC1952.03","SPAC4F10.02","SPBC3H7.13","SPCC663.03","SPAC19B12.10","SPAC2C4.15c","SPAC17G8.11c","SPAC31A2.12","SPCC132.02","SPBC839.17c","SPAC3H8.02","SPBC646.09c","SPBC16E9.05","SPAC13G6.02c","SPCC13B11.01","SPAC16E8.13","SPBC106.03","SPAC13G7.08c","SPAC3H1.07","SPBC577.08c","SPCC24B10.09","SPAC9E9.11","SPBC1289.05c","SPAC22H10.05c","SPAC821.03c","SPAC8C9.15c","SPBC24C6.04","SPBC32F12.03c","SPCC1281.06c","SPBC4C3.07","SPBC887.04c","SPAC637.13c","SPBC13A2.04c","SPCC1672.11c","SPAC1F3.06c","SPBP22H7.08","SPCC23B6.01c","SPAC24C9.08","SPAC14C4.04","SPBC336.10c","SPBC16H5.07c","SPAC959.07","SPCC74.03c","SPBC28F2.03","SPAC644.13c","SPACUNK4.16c","SPAP27G11.13c","SPCC757.09c","SPAC29B12.11c","SPAC31G5.05c","SPBC36.05c","SPAC1071.12c","SPCC1322.14c","SPBC31A8.01c","SPAC1A6.01c","SPBC1271.04c","SPAC6F6.07c","SPBC26H8.07c","SPAC3H1.05","SPAC4G9.16c","SPBC1703.13c","SPAC17G6.05c","SPAC7D4.07c","SPAC3A11.10c","SPBC1539.09c","SPAC9.10","SPBC337.08c","SPCC794.12c","SPBC1289.04c","SPAC1002.02","SPCC24B10.21","SPBC119.02","SPCC4B3.03c","SPBC18E5.01","SPAC6B12.15","SPBC29A3.12","SPAC19G12.05","SPAC23G3.11","SPAC24B11.07c","SPBC1105.02c","SPBC19C2.07","SPBC83.17","SPCC18.18c","SPBC3H7.15","SPBC1347.06c","SPBC16A3.02c","SPBC16D10.08c","SPBC32F12.10","SPBC839.06","SPAC3H8.06","SPCC1682.14","SPCC584.15c","SPAC631.02","SPCC1450.04","SPBC8D2.18c","SPBC2D10.10c","SPBC1734.08","SPAC227.15","SPAC1002.03c","SPBC23G7.12c","SPBC685.07c","SPBC4F6.09","SPAC1805.05","SPAC1F7.03","SPAPB1E7.08c","SPCC622.14","SPCC663.09c","SPCP1E11.04c","SPBC18E5.06","SPAC3A11.12c","SPAC1F7.08","SPCC14G10.04","SPBC15C4.06c","SPCC736.15","SPAC1006.07","SPCC569.01c","SPAC16C9.04c","SPAC22G7.06c","SPAC1805.06c","SPBC31E1.02c","SPCPB16A4.05c","SPBC26H8.01","SPCC737.09c","SPAC1142.06","SPAC25G10.08","SPBC1198.05","SPCC188.08c","SPBC649.02","SPAC688.07c","SPAC664.04c","SPBC359.03c","SPBC56F2.02","SPAC1F7.05","SPAC11G7.02","SPAPYUK71.03c","SPCP20C8.01c","SPAC8F11.10c","SPAC3A12.10","SPBC582.07c","SPBC106.06","SPAC30C2.04","SPBP26C9.03c","SPBPJ4664.04","SPCC364.07","SPBC354.14c","SPAC3C7.11c","SPAC15A10.02","SPBC460.02c","SPBC1773.10c","SPAC3G9.09c","SPAC1556.07","SPAC637.05c","SPBC354.05c","SPBC30D10.18c","SPBC839.13c","SPBC1105.12","SPCC16A11.10c","SPCC576.08c","SPBC16D10.09","SPAC23A1.06c","SPAC19A8.10","SPBC17G9.11c","SPAC12G12.11c","SPAC29A4.04c","SPBC17G9.06c","SPAC25B8.12c","SPAC24H6.04","SPBC25D12.03c","SPCC622.08c","SPAC22H10.12c","SPBC2A9.02","SPAC328.03","SPBC8E4.01c","SPAP11E10.01","SPCC1739.13","SPCC1235.14","SPCC18B5.11c","SPAC637.10c","SPAC23D3.12","SPCC1672.02c","SPBC17A3.07","SPBC11C11.09c","SPAC23D3.11","SPBC530.07c","SPAC1250.05","SPAC26F1.06","SPBC2F12.07c","SPBC19F8.03c","SPBC839.04","SPBC23E6.09","SPAC1142.02c","SPBC32F12.11","SPBC776.11","SPAC30D11.12","SPAC3F10.16c","SPAC29B12.04","SPAC6F12.12","SPAC17G6.09","SPBC17D11.01","SPAC22F8.05","SPBC25H2.16c","SPBC365.01","SPBC16D10.01c","SPAC57A7.10c","SPAC24C9.06c","SPBC1685.13","SPAC4G9.08c","SPAC3H5.09c","SPCC1322.09","SPAC24B11.12c","SPCC132.04c","SPBC1921.05","SPBC25H2.12c","SPCC16A11.16c","SPAC26A3.07c","SPAC521.05","SPAC9E9.09c","SPAC22F8.06","SPAC29A4.16","SPBC19C2.11c","SPBC21D10.05c","SPAC26F1.03","SPAC16E8.11c","SPBC3H7.02","SPCC18.03","SPAC6B12.12","SPCC364.06","SPCC553.10","SPAC17G8.10c","SPBC30D10.07c","SPAC22F8.08","SPAC18G6.14c","SPCC338.07c","SPBC146.07","SPCC330.14c","SPCC338.14","SPAC15F9.02","SPBC19C7.05","SPCC364.03","SPAC1805.13","SPAC6F12.03c","SPBC409.06","SPCC191.02c","SPAC1782.11","SPAC9G1.05","SPAPB2B4.07","SPBC1709.02c","SPAC2F3.06c","SPBC3E7.07c","SPAC1F7.13c","SPBP8B7.18c","SPAC1834.11c","SPCC1827.06c","SPBC1198.08","SPAC6G10.02c","SPCC4B3.15","SPCC1840.07c","SPBC409.05","SPBC18H10.13","SPAPB8E5.02c","SPCC1020.06c","SPBC17G9.04c","SPBC577.10","SPCC320.08","SPAC23H4.06","SPBC18H10.08c","SPAC9E9.15","SPAC222.10c","SPBC16H5.02","SPCC548.06c","SPCC16C4.09","SPAC1A6.04c","SPBP8B7.19","SPAC26A3.11","SPBC354.13","SPAC22A12.11","SPAC6F12.06","SPAC26A3.16","SPBC31F10.06c","SPCC4G3.15c","SPBC28F2.04c","SPCC4G3.12c","SPAC11E3.15","SPAC3C7.14c","SPBC16C6.06","SPCC330.05c","SPAC20G4.06c","SPAC959.08","SPAC1F3.05","SPBC3B9.10","SPAC57A10.12c","SPAC664.05","SPBC1604.05","SPBC146.09c","SPBC1773.07c","SPBC4C3.05c","SPAC31G5.17c","SPBC1921.01c","SPCC1672.07","SPBC1711.16","SPAC1F7.09c","SPCC965.13","SPBC244.01c","SPBC17G9.10","SPAC29A4.15","SPAC6F6.15","SPAC56F8.05c","SPAC1834.04","SPBC9B6.08","SPCC31H12.07","SPBC21D10.12","SPAC5D6.01","SPAC637.04","SPBC119.01","SPAC20H4.03c","SPAC1565.06c"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fission yeast meiosis-specific Dmc1 recombinase mediates formation and branch migration of Holliday junctions by preferentially promoting strand exchange in a direction opposite to that of Rad51.","citation":"Genes Dev 2011 Mar 01;25(5):516-27","abstract":"Homologous recombination proceeds via the formation of several intermediates including Holliday junctions (HJs), which are important for creating crossover products. DNA strand exchange is a core reaction that produces these intermediates that is directly catalyzed by RecA family recombinases, of which there are two types in eukaryotes: universal Rad51 and meiosis-specific Dmc1. We demonstrated previously that Rad51 promotes four-strand exchange, mimicking the formation and branch migration of HJs. Here we show that Dmc1 from fission yeast has a similar activity, which requires ATP hydrolysis and is independent of an absolute requirement for the Swi5-Sfr1 complex. These features are critically different from three-strand exchange mediated by Dmc1, but similar to those of four-strand exchange mediated by Rad51, suggesting that strand exchange reactions between duplex-duplex and single-duplex DNAs are mechanistically different. Interestingly, despite similarities in protein structure and in reaction features, the preferential polarities of Dmc1 and Rad51 strand exchange are different (Dmc1 promotes exchange in the 5'-to-3' direction and Rad51 promotes exchange in the 3'-to-5' direction relative to the ssDNA region of the DNA substrate). The significance of the Dmc1 polarity is discussed within the context of the necessity for crossover production.","doi":"10.1101/gad.1997511","authors":"Murayama Y, Tsutsui Y, Iwasaki H","authors_abbrev":"Murayama Y et al.","pubmed_publication_date":"01 Mar 2011","pubmed_entrez_date":"2011-03-03","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28143796","title":"Clr4 specificity and catalytic activity beyond H3K9 methylation.","citation":"Biochimie 2017 Apr;135:83-88","abstract":"In fission yeast, the catalytic activity of the protein lysine methyltransferase (PKMT) Clr4, the sole homolog of the mammalian SUV39H1 and SUV39H2 enzymes, majorly contributes to the formation of heterochromatin. The enzyme introduces histone 3 lysine 9 (H3K9) di- and tri-methylation, a central heterochromatic histone modification, and later it was also found to methylate the Mlo3 protein, which has a role in heterochromatin formation as well. Herein, we have investigated the substrate specificity of Clr4 using custom made mutational scanning peptide arrays. Our data show, that Clr4 recognizes an RK core motif, showing high preference for R8. In addition, it exhibits specific contacts at the S10, T11, G12 and G13 positions of the H3 peptide recognizing an R-K-SKRT-TCS-G sequence. Based on the specificity profile and in vitro methyltransferase assay targeted searches, 11 putative methylation sites in S. pombe proteins were identified from reported Clr4 interacting proteins including Mlo3. Peptide methylation was observed on Mlo3 and 7 novel target sites with strongest methylation signals on Spbc28F2.11 (HMG box-containing protein) at lysine 292 and Hrp3 (Chromodomain ATP-dep DNA helicase) at lysine 89. These data suggest that Clr4 has additional methylation substrates and it will be important to study the biological function of these novel methylation events. Furthermore, the specificity profile of Clr4 has been used to develop a quantitative method to compare and cluster specificity profiles of PKMTs. It shows that the specificity profile of Clr4 is most similar to that of the SUV39H2 enzyme, one of its human homologs. This approach will be helpful in the comparison of the recognition profiles of other families of PKMTs as well.","doi":"10.1016/j.biochi.2017.01.013","authors":"Kusevic D, Kudithipudi S, Iglesias N, Moazed D, Jeltsch A","authors_abbrev":"Kusevic D et al.","pubmed_publication_date":"Apr 2017","pubmed_entrez_date":"2017-02-02","publication_year":"2017","canto_session_key":"226a912f6492e25c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-03 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6G10.07","SPBC1D7.04","SPBC428.08c","SPAC1834.04","SPAC664.01c","SPBC28F2.11","SPAC3G6.01","SPAC1687.10"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:30796050","title":"Ssu72 phosphatase is a conserved telomere replication terminator.","citation":"EMBO J 2019 Apr 01;38(7)","abstract":"Telomeres, the protective ends of eukaryotic chromosomes, are replicated through concerted actions of conventional DNA polymerases and elongated by telomerase, but the regulation of this process is not fully understood. Telomere replication requires (Ctc1/Cdc13)-Stn1-Ten1, a telomeric ssDNA-binding complex homologous to RPA Here, we show that the evolutionarily conserved phosphatase Ssu72 is responsible for terminating the cycle of telomere replication in fission yeast. Ssu72 controls the recruitment of Stn1 to telomeres by regulating Stn1 phosphorylation at Ser74, a residue located within its conserved OB-fold domain. Consequently,  ssu72∆  mutants are defective in telomere replication and exhibit long 3'-ssDNA overhangs, indicative of defective lagging-strand DNA synthesis. We also show that hSSU72 regulates telomerase activation in human cells by controlling recruitment of hSTN1 to telomeres. These results reveal a previously unknown yet conserved role for the phosphatase SSU72, whereby this enzyme controls telomere homeostasis by activating lagging-strand DNA synthesis, thus terminating the cycle of telomere replication.","doi":"10.15252/embj.2018100476","authors":"Escandell JM, Carvalho ES, Gallo-Fernandez M, Reis CC, Matmati S, Luís IM, Abreu IA, Coulon S, Ferreira MG","authors_abbrev":"Escandell JM et al.","pubmed_publication_date":"01 Apr 2019","pubmed_entrez_date":"2019-02-24","publication_year":"2019","canto_session_key":"6c6733a743354788","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-04-30 13:51:52","canto_approved_date":"2022-09-26 17:22:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-27 10:28:27","canto_added_date":"2019-02-25 01:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":44,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c","SPBC1778.02","SPBC17D1.06","SPAC16A10.07c","SPBC29A3.14c","SPAC644.14c","SPBC17D11.06","SPBC409.12c","SPCC188.07","SPCC1393.14","SPAC30D11.10","SPBC216.05","SPBC660.13c","SPAC926.09c","SPAC6B12.10c","SPCC1259.13","SPBC2F12.04","SPAC3G9.04","SPAC6F6.17","SPAC6F6.16c","SPBC11B10.09"],"gene_count":21,"ltp_gene_count":13,"approved_date":"2019-04-30"},{"uniquename":"PMID:34359522","title":"In Vitro Activity of Selected Phenolic Compounds against Planktonic and Biofilm Cells of Food-Contaminating Yeasts.","citation":"Foods 2021 Jul 17;10(7)","abstract":"Phenolic compounds are natural substances that can be obtained from plants. Many of them are potent growth inhibitors of foodborne pathogenic microorganisms, however, phenolic activities against spoilage yeasts are rarely studied. In this study, planktonic and biofilm growth, and the adhesion capacity of  Pichia anomala ,  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe  and  Debaryomyces hansenii  spoilage yeasts were investigated in the presence of hydroxybenzoic acid, hydroxycinnamic acid, stilbene, flavonoid and phenolic aldehyde compounds. The results showed significant anti-yeast properties for many phenolics. Among the tested molecules, cinnamic acid and vanillin exhibited the highest antimicrobial activity with minimum inhibitory concentration (MIC) values from 500 µg/mL to 2 mg/mL. Quercetin, (-)-epicatechin, resveratrol, 4-hydroxybenzaldehyde,  p -coumaric acid and ferulic acid were also efficient growth inhibitors for certain yeasts with a MIC of 2 mg/mL. The  D. hansenii ,  P. anomala  and  S. pombe  biofilms were the most sensitive to the phenolics, while the  S. cerevisiae  biofilm was quite resistant against the activity of the compounds. Fluorescence microscopy revealed disrupted biofilm matrix on glass surfaces in the presence of certain phenolics. Highest antiadhesion activity was registered for cinnamic acid with inhibition effects between 48% and 91%. The active phenolics can be natural interventions against food-contaminating yeasts in future preservative developments.","doi":"10.3390/foods10071652","authors":"Kimani BG, Kerekes EB, Szebenyi C, Krisch J, Vágvölgyi C, Papp T, Takó M","authors_abbrev":"Kimani BG et al.","pubmed_publication_date":"17 Jul 2021","pubmed_entrez_date":"2021-08-07","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-08-09 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30809004","title":"Bub1 kinase- and H2A phosphorylation-independent regulation of Shugoshin proteins under glucose-restricted conditions.","citation":"Sci Rep 2019 Feb 26;9(1):2826","abstract":"Shugoshin family proteins are involved in various aspects of chromatin regulations, such as chromosome segregation, chromatin structure, and gene expression. In growing yeast and mammalian cells, C-terminal phosphorylation of histone H2A by Bub1 kinase is essential for the localization of Shugoshin proteins to chromatin. Here, we show that in stationary-phase cells, Bub1-mediated H2A phosphorylation is not necessary for chromatin localization of the Shugoshin paralog Sgo2 in Schizosaccharomyces pombe, or for Sgo2-dependent suppression of gene expression in subtelomeric regions. The conserved C-terminal basic domain of Sgo2, which directly binds with phosphorylated H2A, is also dispensable for the localization of Sgo2 to chromatin at stationary phase. Instead, we found that the conserved N-terminal coiled-coil domain and the uncharacterized medial region of Sgo2 are required for Bub1-independent localization of Sgo2. Moreover, Set2-mediated H3K36 methylation was important for the regulation. Intriguingly, the chromatin localization of Sgo2 in the absence of Bub1 was also observed when cells were grown in low-glucose medium. These findings suggest a novel mechanism between nutrient availability and regulation of chromatin by Shugoshin proteins.","doi":"10.1038/s41598-019-39479-6","authors":"Kobayashi Y, Kawashima SA","authors_abbrev":"Kobayashi Y et al.","pubmed_publication_date":"26 Feb 2019","pubmed_entrez_date":"2019-02-28","publication_year":"2019","canto_session_key":"e5421f5df609cde8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-03-01 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36271106","title":"Structure of the pre-mRNA leakage 39-kDa protein reveals a single domain of integrated zf-C3HC and Rsm1 modules.","citation":"Sci Rep 2022 Oct 21;12(1):17691","abstract":"In Saccharomyces cerevisiae, the pre-mRNA leakage 39-kDa protein (ScPml39) was reported to retain unspliced pre-mRNA prior to export through nuclear pore complexes (NPCs). Pml39 homologs outside the Saccharomycetaceae family are currently unknown, and mechanistic insight into Pml39 function is lacking. Here we determined the crystal structure of ScPml39 at 2.5 Å resolution to facilitate the discovery of orthologs beyond Saccharomycetaceae, e.g. in Schizosaccharomyces pombe or human. The crystal structure revealed integrated zf-C3HC and Rsm1 modules, which are tightly associated through a hydrophobic interface to form a single domain. Both zf-C3HC and Rsm1 modules belong to the Zn-containing BIR (Baculovirus IAP repeat)-like super family, with key residues of the canonical BIR domain being conserved. Features unique to the Pml39 modules refer to the spacing between the Zn-coordinating residues, giving rise to a substantially tilted helix αC in the zf-C3HC and Rsm1 modules, and an extra helix αAB' in the Rsm1 module. Conservation of key residues responsible for its distinct features identifies S. pombe Rsm1 and Homo sapiens NIPA/ZC3HC1 as structural orthologs of ScPml39. Based on the recent functional characterization of NIPA/ZC3HC1 as a scaffold protein that stabilizes the nuclear basket of the NPC, our data suggest an analogous function of ScPml39 in S. cerevisiae.","doi":"10.1038/s41598-022-22183-3","authors":"Hashimoto H, Ramirez DH, Lautier O, Pawlak N, Blobel G, Palancade B, Debler EW","authors_abbrev":"Hashimoto H et al.","pubmed_publication_date":"21 Oct 2022","pubmed_entrez_date":"2022-10-21","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1753.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24990387","title":"Optimization of the analogue-sensitive Cdc2/Cdk1 mutant by in vivo selection eliminates physiological limitations to its use in cell cycle analysis.","citation":"Open Biol 2014 Jul;4(7)","abstract":"Analogue-sensitive (as) mutants of kinases are widely used to selectively inhibit a single kinase with few off-target effects. The analogue-sensitive mutant cdc2-as of fission yeast (Schizosaccharomyces pombe) is a powerful tool to study the cell cycle, but the strain displays meiotic defects, and is sensitive to high and low temperature even in the absence of ATP-analogue inhibitors. This has limited the use of the strain for use in these settings. Here, we used in vivo selection for intragenic suppressor mutations of cdc2-as that restore full function in the absence of ATP-analogues. The cdc2-asM17 underwent meiosis and produced viable spores to a similar degree to the wild-type strain. The suppressor mutation also rescued the sensitivity of the cdc2-as strain to high and low temperature, genotoxins and an anti-microtubule drug. We have used cdc2-asM17 to show that Cdc2 activity is required to maintain the activity of the spindle assembly checkpoint. Furthermore, we also demonstrate that maintenance of the Shugoshin Sgo1 at meiotic centromeres does not require Cdc2 activity, whereas localization of the kinase aurora does. The modified cdc2-asM17 allele can be thus used to analyse many aspects of cell-cycle-related events in fission yeast.","doi":"10.1098/rsob.140063","authors":"Aoi Y, Kawashima SA, Simanis V, Yamamoto M, Sato M","authors_abbrev":"Aoi Y et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-07-04","publication_year":"2014","canto_session_key":"339ce5a9b3baae8a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-07-07 00:15:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18613106","title":"Carbon and energy balances in cell-recycle cultures of Schizosaccharomyces pombe.","citation":"Biotechnol Bioeng 1993 Sep 05;42(6):729-36","abstract":"A strain of the fission yeast Schizosaccharomyces pombe was aerobically grown in a cell-recycle fermentor under various operating conditions, i.e., different bleeding rates and various separate feed rates of glucose and basal medium. Carbon and energy balances were analyzed during steady-state culture regimes, allowing growth yields and maintenance coefficients to be determined under glucose-limited and glucose-excess environments. Special attention was given to the metabolic shift from purely oxidative to respirofermentative glucose catabolism resulting from a change in the growth-limiting factor. No maintenance requirements for the carbon source and for energy were observed during glucose-limited culture regimes and oxidative catabolism. Under glucose excess and respirofermentative metabolism, the m(G) coefficient was shown to be growth-linked, whereas the enhancement of the apparent m(e) coefficient observed for increased residual glucose concentrations could be assigned to a decline in the ATP yield.","authors":"Uribelarrea JL, De Queiroz H, Goma G, Pareilleux A","authors_abbrev":"Uribelarrea JL et al.","pubmed_publication_date":"05 Sep 1993","pubmed_entrez_date":"1993-09-05","publication_year":"1993","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28844968","title":"Aging and immortality in unicellular species.","citation":"Mech Ageing Dev 2017 Oct;167:5-15","abstract":"It has been historically thought that in conditions that permit growth, most unicellular species do not to age. This was particularly thought to be the case for symmetrically dividing species, as such species lack a clear distinction between the soma and the germline. Despite this, studies of the symmetrically dividing species Escherichia coli and Schizosaccharomyces pombe have recently started to challenge this notion. They indicate that E. coli and S. pombe do age, but only when subjected to environmental stress. If true, this suggests that aging may be widespread among microbial species in general, and that studying aging in microbes may inform other long-standing questions in aging. This review examines the recent evidence for and against replicative aging in symmetrically dividing unicellular organisms, the mechanisms that underlie aging, why aging evolved in these species, and how microbial aging fits into the context of other questions in aging.","doi":"10.1016/j.mad.2017.08.006","authors":"Florea M","authors_abbrev":"Florea M","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-08-29","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-08-30 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39477503","title":"A DUF3844 domain-containing protein is required for vacuolar protein sorting in Schizosaccharomyces pombe.","citation":"J Gen Appl Microbiol 2024 Oct 31;","abstract":"Protein trafficking to vacuoles in plants and fungi, and to lysosomes in animals, is essential for the maintenance of cellular homeostasis. In Saccharomyces cerevisiae, the vacuolar protein sorting (VPS) pathway has been well studied by using vacuolar carboxypeptidase Y (CPY) as a model, and many VPS genes have been identified. By contrast, the vacuolar protein trafficking pathway in Schizosaccharomyces pombe remains poorly understood. In this study, we identified a novel VPS gene (SPBC1709.03) in S. pombe that is broadly conserved in fungi, but not in S. cerevisiae. Owing to its DUF3844 domain of unknown function, the gene was named vps3844. Disruption mutants of vps3844 had defects in both CPY sorting and incorporation of FM4-64 dye into the vacuolar membrane. Partial deletion analysis of the Vps3844 protein revealed that, within the DUF3844 domain, the region comprising amino acids 354 to 380 is important for protein trafficking to the vacuole. Our findings represent the first report of a VPS gene involved in vacuolar transport that is conserved in fungi, particularly S. pombe, but lacks representation in S. cerevisiae.","doi":"10.2323/jgam.2024.10.001","authors":"Inagawa T, Ohkubo K, Watanabe M, Morita T, Higuchi Y, Maekawa H, Takegawa K","authors_abbrev":"Inagawa T et al.","pubmed_publication_date":"31 Oct 2024","pubmed_entrez_date":"2024-10-30","publication_year":"2024","canto_session_key":"52dd09ea98dec059","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2024-11-08 15:59:58","canto_approved_date":"2026-04-22 05:06:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-07 07:06:34","canto_added_date":"2024-11-01 00:25:04","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.04","SPAC1006.01","SPBC1709.03"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2024-11-08"},{"uniquename":"PMID:11939799","title":"Characterization of an iron-sulfur cluster assembly protein (ISU1) from Schizosaccharomyces pombe.","citation":"Biochemistry 2002 Apr 16;41(15):5024-32","abstract":"Genetic studies of bacteria and eukaryotes have led to identification of several gene products that are involved in the biosynthesis of protein-bound iron-sulfur clusters. One of these proteins, ISU, is homologous to the N-terminus of bacterial NifU. The mature forms of His-tagged wild-type and D37A Schizosaccharomyces pombe ISU1 were cloned and overexpressed as inclusion bodies in Escherichia coli. The recombinant D37A protein was purified under denaturing conditions and subsequently reconstituted in vitro. By use of a 5-fold excess of iron and sulfide the reconstituted product was found to be red-brown in color, forming a homodimer of 17 kDa per subunit with approximately two iron atoms per monomer determined by protein and iron quantitation. UV-vis absorption and Mössbauer spectroscopies (delta = 0.29 +/- 0.05 mm/s; DeltaE(Q) = 0.59 +/- 0.05 mm/s) were used to characterize D37A ISU1 and show the presence of [2Fe-2S](2+) clusters in each subunit. Formation of the holo form of wild-type ISU1 was significantly less efficient using the same reconstitution conditions and is consistent with prior observations that the D37A substitution can stabilize protein-bound clusters. Relative to the human homologue, the yeast ISU is significantly less soluble at ambient temperatures. In both cases the native ISU1 is more sensitive to proton-mediated degradation relative to the D37A derivative. The lability of this family of proteins relative to [2Fe-2S] bearing ferredoxins most likely is of functional relevance for cluster transfer chemistry. Mössbauer parameters obtained for wild-type ISU1 (delta = 0.31 +/- 0.05 mm/s; DeltaE(Q) = 0.64 +/- 0.05 mm/s) were similar to those obtained for the D37A derivative. Cluster transfer from ISU1 to apo Fd is demonstrated: the first example of transfer from an ISU-type protein. A lower limit for k(2) of 80 M(-1) min(-1) was established for WT cluster transfer and a value of 18 M(-1) min(-1) for the D37A derivative. Finally, we have demonstrated through cross-linking studies that ferredoxin, an electron-transport protein, forms a complex with ISU1 in both apo and holo states. Cross-linking of holo ISU1 with holo Fd is consistent with a role for redox chemistry in cluster assembly and may mimic the intramolecular complex already defined in NifU.","authors":"Wu G, Mansy SS, Wu Sp SP, Surerus KK, Foster MW, Cowan JA","authors_abbrev":"Wu G et al.","pubmed_publication_date":"16 Apr 2002","pubmed_entrez_date":"2002-04-10","publication_year":"2002","canto_session_key":"32806b589efc50fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-04 09:23:34","canto_approved_date":"2023-05-17 10:30:56","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2012-11-22 23:17:32","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.10c","SPAC227.13c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-10-04"},{"uniquename":"PMID:32161768","title":"The euchromatic histone mark H3K36me3 preserves heterochromatin through sequestration of an acetyltransferase complex in fission yeast.","citation":"Microb Cell 2020 Jan 03;7(3):80-92","abstract":"Maintaining the identity of chromatin states requires mechanisms that ensure their structural integrity through the concerted actions of histone modifiers, readers, and erasers. Histone H3K9me and H3K27me are hallmarks of repressed heterochromatin, whereas H3K4me and H3K36me are associated with actively transcribed euchromatin. Paradoxically, several studies have reported that loss of Set2, the methyltransferase responsible for H3K36me, causes de-repression of heterochromatin. Here we show that unconstrained activity of the acetyltransferase complex Mst2C, which antagonizes heterochromatin, is the main cause of the silencing defects observed in Set2-deficient cells. As previously shown, Mst2C is sequestered to actively transcribed chromatin via binding to H3K36me3 that is recognized by the PWWP domain protein Pdp3. We demonstrate that combining deletions of  set2    +   and  pdp3    +   results in an epistatic silencing phenotype. In contrast, deleting  mst2    +   , or other members of Mst2C, fully restores silencing in Set2-deficient cells. Suppression of the silencing defect in  set2 Δ cells is specific for pericentromeres and subtelomeres, which are marked by H3K9me, but is not seen for loci that lack genuine heterochromatin. Mst2 is known to acetylate histone H3K14 redundantly with the HAT Gnc5. Further, it is involved in the acetylation of the non-histone substrate and E3 ubiquitin ligase Brl1, resulting in increased H2B-K119 ubiquitylation at euchromatin. However, we reveal that none of these mechanisms are responsible for the Set2-dependent silencing pathway, implying that Mst2 targets another, unknown substrate critical for heterochromatin silencing. Our findings demonstrate that maintenance of chromatin states requires spatial constraint of opposing chromatin activities.","doi":"10.15698/mic2020.03.711","authors":"Georgescu PR, Capella M, Fischer-Burkart S, Braun S","authors_abbrev":"Georgescu PR et al.","pubmed_publication_date":"03 Jan 2020","pubmed_entrez_date":"2020-03-13","publication_year":"2020","canto_session_key":"e15fa7319d76d648","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-03-14 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16202243","title":"The gene encoding gamma-glutamyl transpeptidase II in the fission yeast is regulated by oxidative and metabolic stress.","citation":"J Biochem Mol Biol 2005 Sep 30;38(5):609-18","abstract":"gamma-Glutamyl transpeptidase (GGT, EC 2.3.2.2.) catalyzes the transfer of the gamma-glutamyl moiety from gamma-glutamylcontaining compounds, notably glutathione (GSH), to acceptor amino acids and peptides. A second gene (GGTII) encoding GGT was previously isolated and characterized from the fission yeast Schizosaccharomyces pombe. In the present work, the GGTII-lacZ fusion gene was constructed and used to study the transcriptional regulation of the S. pombe GGTII gene. The synthesis of beta-galactosidase from the GGTII-lacZ fusion gene was significantly enhanced by NO-generating SNP and hydrogen peroxide in the wildtype yeast cells. The GGTII mRNA level was increased in the wild-type S. pombe cells treated with SNP. However, the induction by SNP was abolished in the Pap1-negative S. pombe cells, implying that the induction by SNP of GGTII is mediated by Pap1. Fermentable carbon sources, such as glucose (at low concentrations), lactose and sucrose, as a sole carbon source, enhanced the synthesis of beta-galactosidase from the GGTII-lacZ fusion gene in wildtype KP1 cells but not in Pap1-negative cells. Glycerol, a non-fermentable carbon source, was also able to induce the synthesis of beta-galactosidase from the fusion gene, but other non-fermentable carbon sources such as acetate and ethanol were not. Transcriptional induction of the GGTII gene by fermentable carbon sources was also confirmed by increased GGTII mRNA levels in the yeast cells grown with them. Nitrogen starvation was also able to induce the synthesis of beta-galactosidase from the GGTII-lacZ fusiongene in a Pap1-dependent manner. On the basis of the results, it is concluded that the S. pombe GGTII gene is regulated by oxidative and metabolic stress.","authors":"Kang HJ, Kim BC, Park EH, Ahn K, Lim CJ","authors_abbrev":"Kang HJ et al.","pubmed_publication_date":"30 Sep 2005","pubmed_entrez_date":"2005-10-06","publication_year":"2005","canto_session_key":"3f84c3643996d6f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-08 08:53:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-08 08:53:42","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC56E4.06c","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-08-08"},{"uniquename":"PMID:17086156","title":"[Cell cycle control and CDC28/Cdc2 homologue and related gene cloning of Cryptococcus neoformans].","citation":"Nihon Ishinkin Gakkai Zasshi 2006;47(4):257-62","abstract":"In Cryptococcus neoformans the DNA content of cells having tiny buds varied rather widely, depending on growth phases and strains used. Typically, buds of C. neoformans emerged soon after initiation of DNA synthesis in the early exponential phase. However, bud emergence was delayed to G2 during transition to the stationary phase, and in the early stationary phase budding scarcely occurred, although roughly half of the cells completed DNA synthesis. The timing of budding in C. neoformans was shifted to later cell cycle points with progression of the growth phase of the culture. Similarly, a deficit in oxygen was demonstrated to delay the timing of budding, prolong the G2 phase and cause accumulation of cells after DNA synthesis, but before commitment to budding. The C. neoformans homologue of the main cell cycle control gene CDC28/Cdc2 was isolated using degenerate RT-PCR. The full-length coding region was then amplified using primers to target the regions around the start and stop codons. The gene was called CnCdk1 and was found to have high homologies to S. cerevisiae CDC28 and S. pombe cdc2. To determine its function, its ability to rescue S. cerevisiae cdc28-temperature sensitive mutants was tested. S. cerevisiae cdc28-4 and cdc28-1N strains transformed with the pYES2-CnCdk1 construct exhibited growth at the restrictive temperature. Results of the sequence analysis and the ability of CnCdk1 to complement the S. cerevisiae cdc28-ts mutations support its assumed role as the CDC28/cdc2 homologue in C. neoformans.","authors":"Takeo K, Virtudazo E, Ohkusu M, Kawamoto S, Ito-Kuwa S, Aoki S","authors_abbrev":"Takeo K et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-11-07","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8375778","title":"Effect of hydrogen peroxide on sugar transport in Schizosaccharomyces pombe. Absence of membrane lipid peroxidation.","citation":"Folia Microbiol (Praha) 1993;38(2):135-40","abstract":"Stationary unaerated cells of S. pombe containing endogenous substrates but not energized by any exogenous ones take up 2-deoxy-D-glucose, 6-deoxy-D-glucose, D-xylose and D-arabinose actively over diffusion equilibrium. The active uptake is inhibited by 20-100 mmol/L H2O2 which causes an increase in KT but has no effect on Jmax. This \"competitive inhibition\" indicates that H2O2 affects directly the sugar binding sites of the transporters. The ATP-binding site of the plasma membrane H(+)-ATPase is also affected by 100 mmol/L H2O2; the KT decreases 7-fold, Jmax about 2.5-fold. These effects are not likely to be mediated by membrane lipid peroxidation which appears to be lacking in S. pombe, and this lack may be one of the reasons for the high resistance of this yeast to H2O2. Because of this S. pombe represents a suitable system for studying direct effects of oxidants on membrane proteins.","authors":"Janda S, Gille G, Sigler K, Höfer M","authors_abbrev":"Janda S et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16107732","title":"The fission yeast Crb2/Chk1 pathway coordinates the DNA damage and spindle checkpoint in response to replication stress induced by topoisomerase I inhibitor.","citation":"Mol Cell Biol 2005 Sep;25(17):7889-99","abstract":"Living organisms experience constant threats that challenge their genome stability. The DNA damage checkpoint pathway coordinates cell cycle progression with DNA repair when DNA is damaged, thus ensuring faithful transmission of the genome. The spindle assembly checkpoint inhibits chromosome segregation until all chromosomes are properly attached to the spindle, ensuring accurate partition of the genetic material. Both the DNA damage and spindle checkpoint pathways participate in genome integrity. However, no clear connection between these two pathways has been described. Here, we analyze mutants in the BRCT domains of fission yeast Crb2, which mediates Chk1 activation, and provide evidence for a novel function of the Chk1 pathway. When the Crb2 mutants experience damaged replication forks upon inhibition of the religation activity of topoisomerase I, the Chk1 DNA damage pathway induces sustained activation of the spindle checkpoint, which in turn delays metaphase-to-anaphase transition in a Mad2-dependent fashion. This new pathway enhances cell survival and genome stability when cells undergo replicative stress in the absence of a proficient G(2)/M DNA damage checkpoint.","authors":"Collura A, Blaisonneau J, Baldacci G, Francesconi S","authors_abbrev":"Collura A et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-08-19","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009289","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36478272","title":"Translation-complex profiling of fission yeast cells reveals dynamic rearrangements of scanning ribosomal subunits upon nutritional stress.","citation":"Nucleic Acids Res 2022 Dec 09;50(22):13011-13025","abstract":"Control of mRNA translation is key for stress responses. Translation initiation is usually rate-limiting and, in eukaryotes, involves mRNA scanning by the small ribosomal subunit. Despite its importance, many aspects of translation in vivo have not been explored fully, especially at the transcriptome-wide level. A recent method termed translation-complex profiling (TCP-seq) allows transcriptome-wide views of scanning ribosomal subunits. We applied TCP-seq to nutritional stress in the fission yeast Schizosaccharomyces pombe. At initiation sites, we observed multiple complexes resembling those of mammals, and consistent with queuing of scanning subunits. In 5' UTRs, small subunit accumulations were common and may reflect impediments to scanning. A key mediator of stress responses in S. pombe is the Fil1 transcription factor, which is regulated translationally by a poorly-understood mechanism involving upstream Open Reading Frames (uORFs). TCP-seq data of fil1 shows that stress allows scanning subunits to by-pass specific uORFs and reach the fil1 coding sequence. The integration of these observations with reporter assays revealed that fil1 translational control is mediated by a combination of scanning reinitiation-repressive and permissive uORFs, and establishes fil1 as a model for uORF-mediated translational control. Altogether, our transcriptome-wide study reveals general and gene-specific features of translation in a model eukaryote.","doi":"10.1093/nar/gkac1140","authors":"Duncan CDS, Mata J","authors_abbrev":"Duncan CDS et al.","pubmed_publication_date":"09 Dec 2022","pubmed_entrez_date":"2022-12-08","publication_year":"2022","canto_session_key":"45773f69ce740bfc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2025-05-22 08:28:56","canto_approved_date":"2025-05-22 08:28:57","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-05-22 08:28:39","canto_added_date":"2022-12-09 01:15:06","annotation_curators":[],"file_curator_name":"Pascal Carme","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":458,"orcid":"0009-0003-9059-1333","file_type":"qualitative_gene_expression","file_name":"PMID_36478272_Duncan_qualitative_expression.txt"}],"genes":["SPCC285.11","SPBC211.07c","SPAC13G7.02c","SPAC2F3.16","SPAC644.15","SPAPB24D3.07c","SPBC1706.03","SPCC132.04c","SPAC29B12.10c","SPBPB2B2.10c","SPCC1393.10","SPBPB10D8.01","SPCC306.08c","SPBC16A3.02c","SPAC23H4.06","SPBC839.05c","SPCC18.11c","SPAC458.07","SPBC1347.02","SPAC19B12.08","SPAC3G6.13c","SPAC9.09","SPAC17C9.14","SPAC1F8.03c","SPAC22A12.04c","SPCC777.09c","SPBC405.02c","SPAC664.05","SPBPB2B2.19c","SPAC1296.05c","SPAC343.12","SPAC4H3.03c","SPAC24H6.10c","SPAC3H5.07","SPBC1677.03c","SPAC7D4.06c","SPCC4B3.02c","SPAC1805.12c","SPAC14C4.09","SPBC530.07c","SPCC965.04c","SPAC9.04","SPBC1271.07c","SPAC750.05c","SPCC613.05c","SPBC119.10","SPBC577.02","SPBC24C6.09c","SPBC16A3.17c","SPAC26F1.06","SPAC24C9.08","SPBC19F5.04","SPBP4G3.02","SPAC10F6.03c","SPBC646.14c","SPAC26F1.03","SPAC24C9.06c","SPBC17G9.03c","SPBC106.18","SPAC5D6.01","SPAC3A11.10c","SPAC4G9.10","SPAC1F7.13c","SPCC330.14c","SPBC1815.01","SPAC23A1.10","SPCC1739.06c","SPBC14F5.04c","SPAC806.03c","SPAC9E9.13","SPBC776.03","SPCC1322.08","SPCC970.05","SPCC757.07c","SPCP1E11.09c","SPBC215.05","SPBP16F5.04","SPAC22H12.04c","SPAC23D3.10c","SPAC10F6.12c","SPBC25B2.06c","SPAC11D3.17","SPBC19G7.19","SPCC1840.05c","SPAC2E12.03c","SPBC1921.01c","SPAC1071.08","SPCC74.05","SPBC30D10.18c","SPAC1F8.06","SPAC3G9.13c","SPAC19E9.03","SPBC660.05","SPCC1739.13","SPBC4F6.09","SPCC1442.09","SPBC56F2.06","SPAC13G7.13c","SPCC70.12c","SPBC1685.09","SPBC839.15c","SPBC25H2.05","SPCC962.04","SPAC637.03","SPCC11E10.07c","SPBC685.07c","SPCC24B10.08c","SPAC13D6.02c","SPAC821.11","SPCC645.03c","SPCC1322.13","SPAC869.11","SPCC1259.09c","SPAC4A8.16c","SPCC70.10","SPCC1020.10","SPBC2G2.03c","SPAC22A12.16","SPBC725.17c","SPAC1952.09c","SPBC1105.07c","SPAC21E11.03c","SPBPB21E7.04c","SPAC2F3.08","SPAC2F7.13c","SPBC13A2.04c","SPAC694.05c","SPBC83.13","SPBC16G5.14c","SPAP7G5.06","SPBC19C7.07c","SPBPB21E7.07","SPBC1778.01c","SPAC167.06c","SPCPB16A4.07","SPCC320.05","SPBC1709.05","SPAC977.11","SPAC17A5.03","SPBC21B10.03c","SPAC1F12.02c","SPAC25B8.13c","SPAC19D5.07","SPCC285.05","SPBC56F2.09c","SPBC23G7.13c","SPBC947.04","SPAC19A8.14","SPCC622.18","SPCC364.07","SPAC31G5.04","SPCC1672.03c","SPBP4H10.15","SPAC22F8.05","SPAC167.08","SPAC6F12.03c","SPCC1393.08","SPAC27D7.09c","SPBC1683.06c","SPBC24C6.10c","SPAC13G6.02c","SPAC11D3.09","SPCC4G3.03","SPBC646.09c","SPBC83.17","SPBC3B9.01","SPAC15E1.02c","SPAC16C9.01c","SPBC839.08c","SPCC757.11c","SPBC2D10.10c","SPCC417.08","SPAC5D6.12","SPAP7G5.04c","SPCC1753.04","SPAC3A12.18","SPAC222.08c","SPAC23A1.03","SPBP8B7.06","SPAPJ698.02c","SPBPB2B2.13","SPAC977.12","SPAC57A7.05","SPAC1687.14c","SPCP31B10.07","SPBC19G7.03c","SPBC11B10.03","SPAC11D3.08c","SPBC1709.02c","SPAC3C7.13c","SPCC1223.02","SPAC1071.07c","SPAC688.02c","SPBC4F6.04","SPBC428.11","SPCC794.09c","SPAC1002.09c","SPCC364.03","SPCC1827.03c","SPAC4D7.02c","SPAC6F6.07c","SPAC15E1.03","SPAC26F1.04c","SPCC31H12.06","SPCC1450.13c","SPBC2G2.01c","SPACUNK4.17","SPAC19A8.15","SPCC1259.03","SPAC144.11","SPCC736.02","SPBC2F12.04","SPAC869.05c","SPAC15A10.01","SPCC24B10.15","SPAC3F10.18c","SPAC513.01c","SPAC17C9.02c","SPAC29A4.17c","SPAP8A3.07c","SPAC11D3.18c","SPAPB1A10.08","SPCC16C4.19","SPAC29B12.04","SPBC651.09c","SPCC1827.06c","SPAC16E8.16","SPBC1105.02c","SPBC36B7.09","SPBC119.03","SPAC227.18","SPBC11C11.06c","SPAC890.08","SPCC297.04c","SPAC25G10.06","SPAC20H4.08","SPBC83.02c","SPBC887.01","SPAC24C9.12c","SPBC1347.13c","SPBC17G9.11c","SPBC83.09c","SPAC11E3.15","SPBC365.03c","SPAC57A7.12","SPAC1687.06c","SPAC11G7.04","SPBC19C7.04c","SPAC27E2.03c","SPBC16D10.11c","SPBC3D6.15","SPCC645.14c","SPAC56E4.03","SPCC1235.02","SPAC1805.11c","SPAC23H3.15c","SPBC1683.09c","SPAC1039.02","SPBC11B10.02c","SPAC21E11.04","SPCC1183.08c","SPBC17G9.10","SPBC365.12c","SPAC30D11.12","SPBC21C3.19","SPBC25B2.03","SPCC576.09","SPBC1685.10","SPBC1734.11","SPAC31G5.17c","SPBC23G7.15c","SPCC1682.13","SPCC550.06c","SPBC1703.07","SPBC25H2.04c","SPBC1703.08c","SPCC576.08c","SPAC17C9.11c","SPAC19B12.04","SPBC83.12","SPAC25G10.08","SPAC1B3.03c","SPBC18H10.13","SPAC1F7.10","SPBC409.04c","SPBC27.08c","SPBC2G5.06c","SPAC23D3.04c","SPBC1773.17c","SPAC22H10.05c","SPBC30D10.13c","SPAC4F10.11","SPCC1672.05c","SPBC32H8.03","SPAPYUG7.03c","SPAC1B3.16c","SPAC22A12.15c","SPAC23A1.12c","SPBC1711.08","SPCC126.10","SPCC330.03c","SPBC56F2.12","SPBC1711.13","SPAC11D3.02c","SPAP27G11.13c","SPBC1683.03c","SPCC965.11c","SPAC1F12.07","SPBC649.02","SPCC126.11c","SPBC428.02c","SPAC1805.16c","SPBC1198.05","SPAPB8E5.06c","SPAC144.09c","SPBC1A4.02c","SPAC6G10.08","SPBC428.10","SPCC24B10.05","SPBC418.01c","SPBC3B9.19","SPBC18H10.14","SPAPB1A10.05","SPBC409.10","SPCC417.05c","SPAC1039.09","SPAC664.04c","SPAC607.03c","SPCC63.14","SPBC1289.06c","SPBC28E12.04","SPCC320.11c","SPCP1E11.05c","SPBC2F12.11c","SPBP4H10.14c","SPCC1450.04","SPBC4.06","SPCC191.11","SPCC1223.09","SPAC17G6.03","SPAC57A10.07","SPAP7G5.02c","SPAC17G8.06c","SPCC830.07c","SPAC9E9.11","SPBP35G2.07","SPAC22E12.03c","SPBC582.08","SPBC2G2.05","SPAC15F9.03c","SPBC3E7.16c","SPBC1683.12","SPBC8E4.01c","SPAC3H5.12c","SPAC31G5.03","SPAC6G9.09c","SPAC1F5.05c","SPAC589.10c","SPBC725.01","SPAC139.02c","SPBC839.07","SPBC428.05c","SPBC11C11.09c","SPBC29B5.02c","SPBC27.06c","SPBC15D4.15","SPAC5H10.10","SPAC13A11.05","SPAC10F6.13c","SPCC1620.06c","SPAC9E9.03","SPCC794.07","SPAP8A3.04c","SPCP31B10.08c","SPAC4F10.14c","SPBP16F5.08c","SPAC11E3.14","SPAC644.09","SPAC13D1.01c","SPBC9B6.02c","SPAC637.07","SPBC409.11","SPAC8F11.09c","SPBC2F12.14c","SPBC3H7.02","SPAC9G1.03c","SPBPB8B6.06c","SPBC839.11c","SPBC215.08c","SPAC4F10.20","SPBC16D10.08c","SPBPB8B6.05c","SPBP8B7.28c","SPBC725.03","SPBC3B8.03","SPCC663.04","SPBC16C6.11","SPBC1348.02","SPCC1840.03","SPBC405.01","SPCC330.06c","SPAC26F1.13c","SPBC17D11.08","SPBC660.06","SPCC18.14c","SPBC18H10.12c","SPBC1271.08c","SPAC1002.12c","SPBC1105.14","SPBPB2B2.05","SPCC306.05c","SPAC869.10c","SPAC16.02c","SPAC22A12.05","SPAC4G8.02c","SPAC13G6.07c","SPAC6C3.04","SPAC3G9.03","SPAC15E1.08","SPBC19G7.16","SPCC285.15c","SPBP35G2.09","SPAC227.17c","SPCC1235.11","SPAC3G6.05","SPCC330.05c","SPCPB16A4.03c","SPAC6F12.10c","SPCC1753.02c","SPBC839.06","SPBC337.06c","SPAC926.04c","SPAC3H5.05c","SPBC30B4.09"],"gene_count":434,"ltp_gene_count":0,"approved_date":"2025-05-22"},{"uniquename":"PMID:940546","title":"The genetic instabilities of the mating type locus in fission yeast.","citation":"Mol Gen Genet 1976 Jun 15;145(3):281-6","abstract":"Certain genetic instabilities of the \"mating type locus\" in the yeast Schizosaccharomyces pombe are interpreted in terms of transposition: Homothallic strains are characterized by two adjacent mating type genes (mat1-mat2+) with sexually complementary functions. One of these genes (mat2+) is able to duplicate itself, and the duplicated copy maps at the position of mat1-. The former function of mat1-is lost (owing to insertion), and only becomes reactivated when the inserted sequence (mat1+) is again excised. Analyses of analogous instabilities expressed by the partially defective mutation mat2+ -B102 have substantiated this transposition scheme. Homothallism is acribed to alternate and mutually exclusive activation of mat1- or mat2+ genes.","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"15 Jun 1976","pubmed_entrez_date":"1976-06-15","publication_year":"1976","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28827290","title":"Kinetochore Components Required for Centromeric Chromatin Assembly Are Impacted by Msc1 in  Schizosaccharomyces pombe .","citation":"Genetics 2017 Oct;207(2):559-569","abstract":"Eukaryotic chromosome segregation requires a protein complex known as the kinetochore that mediates attachment between mitotic spindle microtubules and centromere-specific nucleosomes composed of the widely conserved histone variant CENP-A. Mutations in kinetochore proteins of the fission yeast  Schizosaccharomyces pombe  lead to chromosome missegregation such that daughter cells emerge from mitosis with unequal DNA content. We find that multiple copies of Msc1-a fission yeast homolog of the KDM5 family of proteins-suppresses the temperature-sensitive growth defect of several kinetochore mutants, including  mis16  and  mis18 , as well as  mis6 ,  mis15 , and  mis17 , components of the Constitutive Centromere Associated Network (CCAN). On the other hand, deletion of  msc1  exacerbates both the growth defect and chromosome missegregation phenotype of each of these mutants. The C-terminal PHD domains of Msc1, previously shown to associate with a histone deacetylase activity, are necessary for Msc1 function when kinetochore mutants are compromised. We also demonstrate that, in the absence of Msc1, the frequency of localization to the kinetochore of Mis16 and Mis15 is altered from wild-type cells. As we show here for  msc1 , others have shown that elevating  cnp1  levels acts similarly to promote survival of the CCAN mutants. The rescue of  mis15  and  mis17  by  cnp1  is, however, independent of  msc1  Thus, Msc1 appears to contribute to the chromatin environment at the centromere: the absence of Msc1 sensitizes cells to perturbations in kinetochore function, while elevating Msc1 overcomes loss of function of critical components of the kinetochore and centromere.","doi":"10.1534/genetics.117.300183","authors":"Gao C, Langbein L, Kamal F, George AA, Walworth NC","authors_abbrev":"Gao C et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-08-23","publication_year":"2017","canto_session_key":"b9792083a95e2fee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Anuja George","canto_first_approved_date":"2017-10-10 21:24:57","canto_approved_date":"2023-10-05 15:26:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-22 18:28:15","canto_added_date":"2017-08-24 00:15:16","annotation_curators":[{"name":"Anuja George","community_curator":true,"annotation_count":8,"orcid":"0000-0003-2643-6307","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC343.11c","SPAC1687.20c","SPBP22H7.09c","SPBC21.01","SPCC970.12","SPCC1672.10","SPBC1105.17"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-10-10"},{"uniquename":"PMID:38677290","title":"Structural and functional insights into yeast Tbf1 as an atypical telomeric repeat-binding factor.","citation":"Structure 2024 Apr 17;","abstract":"Telomeric repeat-binding factor 1 (Tbf1) has a similar architecture as the TRF family of telomeric proteins and plays important roles in both telomere homeostasis and ribosome regulation. However, the molecular basis of why Tbf1 has such different functions compared to other TRFs remains unclear. Here, we present the crystal structures of the TRF homology (TRFH) and Myb-L domains from Schizosaccharomyces pombe Tbf1 (spTbf1). TRFH-mediated homodimerization is essential for spTbf1 stability. Importantly, spTbf1 TRFH  lacks the conserved docking motif for interactions with telomeric proteins, explaining why spTbf1 does not participate in the assembly of the shelterin complex. Finally, structural and biochemical analyses demonstrate that TRFH and Myb-L domains as well as the loop region of spTbf1 coordinate to recognize S. pombe telomeric double-stranded DNA. Overall, our findings provide structural and functional insights into how fungi Tbf1 acts as an atypical telomeric repeat-binding factor, which helps to understand the evolution of TRFH-containing telomeric proteins.","doi":"10.1016/j.str.2024.04.002","authors":"Wu Z, Gu X, Zha L, Yang Q, Zhou Y, Zeng Z","authors_abbrev":"Wu Z et al.","pubmed_publication_date":"17 Apr 2024","pubmed_entrez_date":"2024-04-27","publication_year":"2024","canto_session_key":"29db59cac09c4779","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-12-30 10:06:44","canto_approved_date":"2025-09-02 20:27:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-13 16:24:11","canto_added_date":"2024-04-28 23:25:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-12-30","pdb_entries":[{"pdb_id":"8ynu","gene_chains":[{"gene_uniquename":"SPBC19G7.13","chain":"A/B","position":"407-485"}],"title":"Crystal structure of the myb domain of S.pombe Tbf1 in the P222 space group","entry_authors":"Zhou YZ,Wu ZF","entry_authors_abbrev":"Zhou YZ et al.","reference_uniquename":"PMID:38677290","experimental_method":"X-ray","resolution":"1.76"}]},{"uniquename":"PMID:38228139","title":"Live-cell imaging defines a threshold in CDK activity at the G2/M transition.","citation":"Dev Cell 2024 Jan 08;","abstract":"Cyclin-dependent kinase (CDK) determines the temporal ordering of the cell cycle phases. However, despite significant progress in studying regulators of CDK and phosphorylation patterns of CDK substrates at the population level, it remains elusive how CDK regulators coordinately affect CDK activity at the single-cell level and how CDK controls the temporal order of cell cycle events. Here, we elucidate the dynamics of CDK activity in fission yeast and mammalian cells by developing a CDK activity biosensor, Eevee-spCDK. We find that although CDK activity does not necessarily correlate with cyclin levels, it converges to the same level around mitotic onset in several mutant backgrounds, including pom1Δ cells and wee1 or cdc25 overexpressing cells. These data provide direct evidence that cells enter the M phase when CDK activity reaches a high threshold, consistent with the quantitative model of cell cycle progression in fission yeast.","doi":"10.1016/j.devcel.2023.12.014","authors":"Sugiyama H, Goto Y, Kondo Y, Coudreuse D, Aoki K","authors_abbrev":"Sugiyama H et al.","pubmed_publication_date":"08 Jan 2024","pubmed_entrez_date":"2024-01-16","publication_year":"2024","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2024-01-18 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC2F7.03c","SPCC18B5.03"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:11739790","title":"Two related kinesins, klp5+ and klp6+, foster microtubule disassembly and are required for meiosis in fission yeast.","citation":"Mol Biol Cell 2001 Dec;12(12):3919-32","abstract":"The kinesin superfamily of microtubule motor proteins is important in many cellular processes, including mitosis and meiosis, vesicle transport, and the establishment and maintenance of cell polarity. We have characterized two related kinesins in fission yeast, klp5+ and klp6+,, that are amino-terminal motors of the KIP3 subfamily. Analysis of null mutants demonstrates that neither klp5+ nor klp6+, individually or together, is essential for vegetative growth, although these mutants have altered microtubule behavior. klp5Delta and klp6Delta are resistant to high concentrations of the microtubule poison thiabendazole and have abnormally long cytoplasmic microtubules that can curl around the ends of the cell. This phenotype is greatly enhanced in the cell cycle mutant cdc25-22, leading to a bent, asymmetric cell morphology as cells elongate during cell cycle arrest. Klp5p-GFP and Klp6p-GFP both localize to cytoplasmic microtubules throughout the cell cycle and to spindles in mitosis, but their localizations are not interdependent. During the meiotic phase of the life cycle, both of these kinesins are essential. Spore viability is low in homozygous crosses of either null mutant. Heterozygous crosses of klp5Delta with klp6Delta have an intermediate viability, suggesting cooperation between these proteins in meiosis.","authors":"West RR, Malmstrom T, Troxell CL, McIntosh JR","authors_abbrev":"West RR et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-12-12","publication_year":"2001","canto_session_key":"8d41506ec01aec5b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-06-20 08:41:15","canto_approved_date":"2022-10-05 16:26:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-02 21:48:49","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":39,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPBC2F12.13","SPBC1685.15c","SPCC18B5.03","SPBC336.12c","SPAC24H6.05"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-06-20"},{"uniquename":"PMID:11739791","title":"Dynamic behavior of microtubules during dynein-dependent nuclear migrations of meiotic prophase in fission yeast.","citation":"Mol Biol Cell 2001 Dec;12(12):3933-46","abstract":"During meiotic prophase in fission yeast, the nucleus migrates back and forth between the two ends of the cell, led by the spindle pole body (SPB). This nuclear oscillation is dependent on astral microtubules radiating from the SPB and a microtubule motor, cytoplasmic dynein. Here we have examined the dynamic behavior of astral microtubules labeled with the green fluorescent protein during meiotic prophase with the use of optical sectioning microscopy. During nuclear migrations, the SPB mostly follows the microtubules that extend toward the cell cortex. SPB migrations start when these microtubules interact with the cortex and stop when they disappear, suggesting that these microtubules drive nuclear migrations. The microtubules that are followed by the SPB often slide along the cortex and are shortened by disassembly at their ends proximal to the cortex. In dynein-mutant cells, where nuclear oscillations are absent, the SPB never migrates by following microtubules, and microtubule assembly/disassembly dynamics is significantly altered. Based on these observations, together with the frequent accumulation of dynein at a cortical site where the directing microtubules interact, we propose a model in which dynein drives nuclear oscillation by mediating cortical microtubule interactions and regulating the dynamics of microtubule disassembly at the cortex.","authors":"Yamamoto A, Tsutsumi C, Kojima H, Oiwa K, Hiraoka Y","authors_abbrev":"Yamamoto A et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-12-12","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19556509","title":"Synthetic heterochromatin bypasses RNAi and centromeric repeats to establish functional centromeres.","citation":"Science 2009 Jun 26;324(5935):1716-9","abstract":"In the central domain of fission yeast centromeres, the kinetochore is assembled on CENP-A(Cnp1) nucleosomes. Normally, small interfering RNAs generated from flanking outer repeat transcripts direct histone H3 lysine 9 methyltransferase Clr4 to homologous loci to form heterochromatin. Outer repeats, RNA interference (RNAi), and centromeric heterochromatin are required to establish CENP-A(Cnp1) chromatin. We demonstrated that tethering Clr4 via DNA-binding sites at euchromatic loci induces heterochromatin assembly, with or without active RNAi. This synthetic heterochromatin completely substitutes for outer repeats on plasmid-based minichromosomes, promoting de novo CENP-A(Cnp1) and kinetochore assembly, to allow their mitotic segregation, even with RNAi inactive. Thus, the role of outer repeats in centromere establishment is simply the provision of RNAi substrates to direct heterochromatin formation; H3K9 methylation-dependent heterochromatin is alone sufficient to form functional centromeres.","doi":"10.1126/science.1172026","authors":"Kagansky A, Folco HD, Almeida R, Pidoux AL, Boukaba A, Simmer F, Urano T, Hamilton GL, Allshire RC","authors_abbrev":"Kagansky A et al.","pubmed_publication_date":"26 Jun 2009","pubmed_entrez_date":"2009-06-27","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41743984","title":"Evolutionary persistence and divergence of the  tdk  killer meiotic driver family.","citation":"bioRxiv 2025 Dec 29;","abstract":"Killer meiotic drivers (KMDs) are selfish genetic elements that achieve super-Mendelian inheritance by selectively eliminating gametes lacking the driver. Although predicted to arise recurrently, KMDs are generally considered evolutionarily ephemeral-going extinct after fixation or host suppression. The identification of  tdk1  , a single-gene KMD in the fission yeast  Schizosaccharomyces pombe  , provides a model for studying KMD evolution. Here, we identify two divergent  tdk1  homologs (  tdk210  and  tdk203  ) from  S. cryophilus  , a fission yeast species that diverged ∼100 million years ago from  S. pombe  , as active KMDs. These three KMDs all act via post-germination killing, disrupting chromosome segregation in noncarrier progeny. Notably, they also exhibit striking functional divergences:  tdk1  ,  tdk210  , and  tdk203  are mutually incompatible (showing no cross-resistance), and the latter two act independently of Bdf1/Bdf2-host chromatin proteins required for  tdk1  killing. Phylogenetic analyses of the dozens of  tdk  family genes in  Schizosaccharomyces  support long-term persistence and rapid evolutionary dynamics of this gene family. Remarkably, homologs in distantly related fungal phyla display genomic and structural similarities to  Schizosaccharomyces tdk  genes, suggesting a deeply rooted origin of this KMD family in fungi. Our findings reveal that a single KMD family can undergo repeated functional innovation-generating mutually incompatible variants and rewiring host dependencies-while maintaining a conserved killing mode over deep evolutionary time.","doi":"10.64898/2025.12.28.696746","authors":"Zhang FY, Jia GS, Ren JY, Suo F, Du TY, Zhang WC, Li W, Wang QM, Du LL, Hua Y","authors_abbrev":"Zhang FY et al.","pubmed_publication_date":"29 Dec 2025","pubmed_entrez_date":"2026-02-26","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-02-27 00:25:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8543576","title":"Malfolded cytochrome P-450(M1) localized in unusual membrane structures of the endoplasmic reticulum in cultured animal cells.","citation":"J Biochem 1995 Aug;118(2):397-404","abstract":"A conserved region containing three to five proline residues is present just behind the signal-anchor sequence in the amino terminal portion of most microsomal cytochrome P-450s. We have shown that the proline residues are crucial for correct folding in Schizosaccharomyces pombe cells by using mutants of P-450(M1) in which one to three of the proline residues were changed to alanine. To examine the effects of the mutations on the intracellular localization of P-450s, they were expressed in COS-7 cells. They were found to be localized only in the perinuclear loci as patched structures like the Golgi apparatus, while the wild-type P-450(M1) is localized in the reticular structures which are typical for the ER membrane. However, treatment of the cells with Brefeldin A had no effect on the patched structures. Upon co-expression with another ER membrane protein, CD4D, which possesses a double lysine motif, the expressed CD4D was localized not only in the patched structures as the mutated P-450(M1)s, but also in the reticular structures of ER. When the cells were homogenized and then fractionated, the mutated P-450(M1) was recovered mainly in the low-speed precipitate and in the fractions of much higher density than the normal ER membrane. On electron microscopic observation, unusual membranous bodies were observed near the nucleus only when the mutated P-450(M1) was expressed.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Ishihara N, Yamashina S, Sakaguchi M, Mihara K, Omura T","authors_abbrev":"Ishihara N et al.","pubmed_publication_date":"Aug 1995","pubmed_entrez_date":"1995-08-01","publication_year":"1995","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18665130","title":"Mapping the strand-specific transcriptome of fission yeast.","citation":"Nat Genet 2008 Aug;40(8):935-6","abstract":"","doi":"10.1038/ng0808-935","authors":"Gingeras TR","authors_abbrev":"Gingeras TR","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-07-31","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21246752","title":"Dividing the spoils of growth and the cell cycle: The fission yeast as a model for the study of cytokinesis.","citation":"Cytoskeleton (Hoboken) 2011 Feb;68(2):69-88","abstract":"Cytokinesis is the final stage of the cell cycle, and ensures completion of both genome segregation and organelle distribution to the daughter cells. Cytokinesis requires the cell to solve a spatial problem (to divide in the correct place, orthogonally to the plane of chromosome segregation) and a temporal problem (to coordinate cytokinesis with mitosis). Defects in the spatiotemporal control of cytokinesis may cause cell death, or increase the risk of tumor formation [Fujiwara et al., 2005 (Fujiwara T, Bandi M, Nitta M, Ivanova EV, Bronson RT, Pellman D. 2005. Cytokinesis failure generating tetraploids promotes tumorigenesis in p53-null cells. Nature 437:1043–1047); reviewed by Ganem et al., 2007 (Ganem NJ, Storchova Z, Pellman D. 2007. Tetraploidy, aneuploidy and cancer. Curr Opin Genet Dev 17:157–162.)]. Asymmetric cytokinesis, which permits the generation of two daughter cells that differ in their shape, size and properties, is important both during development, and for cellular homeostasis in multicellular organisms [reviewed by Li, 2007 (Li R. 2007. Cytokinesis in development and disease: variations on a common theme. Cell Mol Life Sci 64:3044–3058)]. The principal focus of this review will be the mechanisms of cytokinesis in the mitotic cycle of the yeast Schizosaccharomyces pombe. This simple model has contributed significantly to our understanding of how the cell cycle is regulated, and serves as an excellent model for studying aspects of cytokinesis. Here we will discuss the state of our knowledge of how the contractile ring is assembled and disassembled, how it contracts, and what we know of the regulatory mechanisms that control these events and assure their coordination with chromosome segregation.","doi":"10.1002/cm.20500","authors":"Goyal A, Takaine M, Simanis V, Nakano K","authors_abbrev":"Goyal A et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2011-01-20","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008420","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17688408","title":"Schizosaccharomyces pombe Rad4/Cut5 protein modification and chromatin binding changes in DNA damage.","citation":"DNA Cell Biol 2007 Aug;26(8):565-75","abstract":"The Schizosaccharomyces pombe Rad4/Cut5 protein is essential for DNA replication and checkpoint control. We have analyzed the behavior of the protein during unperturbed DNA replication, in different replication and checkpoint mutant backgrounds and in response to DNA-damaging agents. In an unperturbed cell cycle, Rad4 is chromatin bound and the mobility of the protein is not altered. Rad4 protein level and thus chromatin binding are dependent on a functional DNA polymerase epsilon. In response to replication arrest and DNA damage, the protein is modified in a Rad3-dependent manner. These data indicate that Rad4 undergoes diverse forms of regulation that are distinct in both DNA replication and checkpoint response.","authors":"Siam R, Gómez EB, Forsburg SL","authors_abbrev":"Siam R et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-08-11","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2909894","title":"The gene for the U6 small nuclear RNA in fission yeast has an intron.","citation":"Nature 1989 Jan 05;337(6202):87-90","abstract":"The small nuclear RNAs (snRNAs) are a class of metabolically stable small RNAs present in the nuclei of eukaryotic cells. In mammalian cells, there are six major molecular species (U1 to U6 snRNA), which are complexed with proteins, forming small nuclear ribonucleoprotein particles, snRNPs. Of these, the U1, U2, U4, U5, U6 snRNPs are thought to participate in pre-mRNA splicing as part of the spliceosome. Here, we describe the characterization of the gene coding for the Schizosaccharomyces pombe U6 snRNA. Unexpectedly, the Schiz. pombe U6 RNA gene was found to contain an intron-like sequence of 50 base pairs. Northern blot analysis and RNA sequencing revealed that this intron-like sequence is precisely removed from the transcript. The mature U6 RNA of Schiz. pombe has 77% sequence homology with the mammalian U6 RNA. In Schiz. pombe, it is possible that U6 RNA is not only involved in pre-mRNA splicing, but is also a splicing substrate. This is the first report of an intron in a snRNA gene.","authors":"Tani T, Ohshima Y","authors_abbrev":"Tani T et al.","pubmed_publication_date":"05 Jan 1989","pubmed_entrez_date":"1989-01-05","publication_year":"1989","canto_session_key":"e18edf945f0c6cb5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-19 15:38:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-19 15:37:57","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-19"},{"uniquename":"PMID:23615440","title":"The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.","citation":"Mol Biol Cell 2013 Jun;24(12):1830-41","abstract":"The mitochondrial Hsp70 chaperone Ssq1 plays a dedicated role in the maturation of iron-sulfur (Fe/S) proteins, an essential process of mitochondria. Similar to its bacterial orthologue HscA, Ssq1 binds to the scaffold protein Isu1, thereby facilitating dissociation of the newly synthesized Fe/S cluster on Isu1 and its transfer to target apoproteins. Here we use in vivo and in vitro approaches to show that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from that of Isu1. Grx5 binding does not stimulate the ATPase activity of Ssq1 and is most pronounced for the ADP-bound form of Ssq1, which interacts with Isu1 most tightly. The vicinity of Isu1 and Grx5 on the Hsp70 chaperone facilitates rapid Fe/S cluster transfer from Isu1 to Grx5. Grx5 and its bound Fe/S cluster are required for maturation of all cellular Fe/S proteins, regardless of the type of bound Fe/S cofactor and subcellular localization. Hence Grx5 functions as a late-acting component of the core Fe/S cluster (ISC) assembly machinery linking the Fe/S cluster synthesis reaction on Isu1 with late assembly steps involving Fe/S cluster targeting to dedicated apoproteins.","doi":"10.1091/mbc.E12-09-0644","authors":"Uzarska MA, Dutkiewicz R, Freibert SA, Lill R, Mühlenhoff U","authors_abbrev":"Uzarska MA et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-04-26","publication_year":"2013","canto_session_key":"c5ebbd5f12e181cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-03-27 06:52:41","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-07-07 07:15:25","canto_added_date":"2017-07-07 06:57:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB2B4.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-07"},{"uniquename":"PMID:18178164","title":"Redox control and oxidative stress in yeast cells.","citation":"Biochim Biophys Acta 2008 Nov;1780(11):1217-35","abstract":"Protein structure and function can be altered by reactive oxygen species produced either by cell metabolism or by external oxidants. Although catalases, superoxide dismutases and peroxidases contribute to maintaining non-toxic levels of reactive oxygen species, modification of amino acid side chains occurs. In particular, oxidative modification of sulphydryl groups in proteins can be a two-faceted process: it could lead to impairment of protein function or, depending on the redox state of cysteine residues, may activate specific pathways involved in regulating key cell functions. In yeast cells, the thioredoxin and glutaredoxin systems participate in such redox regulation in different cell compartments, and interplay exists between both systems. In this context, glutaredoxins with monothiol activity initially characterised in Saccharomyces cerevisiae may display specific regulatory functions at the mitochondria and nuclei. Furthermore, their structural conservation in other organisms point to a conserved important role in metal homeostasis also in higher eukaryotes. Control of gene expression in response to oxidative stress is mediated by several transcription factors, among which Yap1 has a predominant role in S. cerevisiae (Pap1 in Schizosaccharomyces pombe and Cap1 in Candida albicans). In combination with Gpx3 peroxidase and Ybp1 protein, the activity of Yap1 is itself controlled depending on the redox state of some of its cysteine residues, which determines the nucleocytoplasmic location of the Yap1 molecules.","doi":"10.1016/j.bbagen.2007.12.004","authors":"Herrero E, Ros J, Bellí G, Cabiscol E","authors_abbrev":"Herrero E et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-01-08","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013547","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12093738","title":"G(1)/S CDK is inhibited to restrain mitotic onset when DNA replication is blocked in fission yeast.","citation":"EMBO J 2002 Jul 01;21(13):3370-6","abstract":"Cyclin-dependent kinase (CDK) Tyr15 phosphorylation plays a major role in regulating G(2)/M CDKs, but the role of this phosphorylation in regulating G(1)/S CDKs is less clear. We have studied the regulation and function of Cdc2-Tyr15 phosphorylation in the fission yeast Schizosaccharomyces pombe G(1)/S CDK Cig2/Cdc2. This complex is subject to high level Cdc2-Tyr15 phosphorylation inhibiting its kinase activity in hydroxyurea-treated cells blocked in S-phase. We show that this Tyr15 phosphorylation is required to maintain efficient mitotic checkpoint arrest, because Cig2 accumulates during the block and this accumulation can advance mitotic onset. This mitotic induction operates, at least in part, through activation of the normal G(2)/M CDK complex Cdc13/Cdc2. Thus, Tyr15 phosphorylation of G(1)/S CDK complexes is important in the checkpoint control blocking mitotic onset when DNA replication is inhibited.","authors":"Zarzov P, Decottignies A, Baldacci G, Nurse P","authors_abbrev":"Zarzov P et al.","pubmed_publication_date":"01 Jul 2002","pubmed_entrez_date":"2002-07-03","publication_year":"2002","canto_session_key":"aba22b8a34948b96","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-11-15 14:57:49","canto_approved_date":"2026-06-26 08:20:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-11-13 16:01:28","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":22,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB2B4.03","SPCC18B5.03","SPBC582.03","SPBC660.14","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-11-15"},{"uniquename":"PMID:23845962","title":"De novo transcript sequence reconstruction from RNA-seq using the Trinity platform for reference generation and analysis.","citation":"Nat Protoc 2013 Aug;8(8):1494-512","abstract":"De novo assembly of RNA-seq data enables researchers to study transcriptomes without the need for a genome sequence; this approach can be usefully applied, for instance, in research on 'non-model organisms' of ecological and evolutionary importance, cancer samples or the microbiome. In this protocol we describe the use of the Trinity platform for de novo transcriptome assembly from RNA-seq data in non-model organisms. We also present Trinity-supported companion utilities for downstream applications, including RSEM for transcript abundance estimation, R/Bioconductor packages for identifying differentially expressed transcripts across samples and approaches to identify protein-coding genes. In the procedure, we provide a workflow for genome-independent transcriptome analysis leveraging the Trinity platform. The software, documentation and demonstrations are freely available from http://trinityrnaseq.sourceforge.net. The run time of this protocol is highly dependent on the size and complexity of data to be analyzed. The example data set analyzed in the procedure detailed herein can be processed in less than 5 h.","doi":"10.1038/nprot.2013.084","authors":"Haas BJ, Papanicolaou A, Yassour M, Grabherr M, Blood PD, Bowden J, Couger MB, Eccles D, Li B, Lieber M, MacManes MD, Ott M, Orvis J, Pochet N, Strozzi F, Weeks N, Westerman R, William T, Dewey CN, Henschel R, LeDuc RD, Friedman N, Regev A","authors_abbrev":"Haas BJ et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-07-13","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:37:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24205865","title":"Aging and cell death in the other yeasts, Schizosaccharomyces pombe and Candida albicans.","citation":"FEMS Yeast Res 2014 Feb;14(1):119-35","abstract":"How do cells age and die? For the past 20 years, the budding yeast, Saccharomyces cerevisiae, has been used as a model organism to uncover the genes that regulate lifespan and cell death. More recently, investigators have begun to interrogate the other yeasts, the fission yeast, Schizosaccharomyces pombe, and the human fungal pathogen, Candida albicans, to determine if similar longevity and cell death pathways exist in these organisms. After summarizing the longevity and cell death phenotypes in S. cerevisiae, this mini-review surveys the progress made in the study of both aging and programed cell death (PCD) in the yeast models, with a focus on the biology of S. pombe and C. albicans. Particular emphasis is placed on the similarities and differences between the two types of aging, replicative aging, and chronological aging, and between the three types of cell death, intrinsic apoptosis, autophagic cell death, and regulated necrosis, found in these yeasts. The development of the additional microbial models for aging and PCD in the other yeasts may help further elucidate the mechanisms of longevity and cell death regulation in eukaryotes.","doi":"10.1111/1567-1364.12113","authors":"Lin SJ, Austriaco N","authors_abbrev":"Lin SJ et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-11-12","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012138","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28373489","title":"Preparation of Total RNA from Fission Yeast.","citation":"Cold Spring Harb Protoc 2017 Apr 03;2017(4):pdb.prot091629","abstract":"Treatment with hot phenol breaks open fission yeast cells and begins to strip away bound proteins from RNA. Deproteinization is completed by multiple extractions with chloroform/isoamyl alcohol and separation of the aqueous and organic phases using MaXtract gel, an inert material that acts as a physical barrier between the phases. The final step is concentration of the RNA by ethanol precipitation. The protocol can be used to prepare RNA from several cultures grown in parallel, but it is important not to process too many samples at once because delays can be detrimental to RNA quality. A reasonable number of samples to process at once would be three to four for microarray or RNA sequencing analyses and six for preliminary investigations of mutants implicated in RNA metabolism.","doi":"10.1101/pdb.prot091629","authors":"Bähler J, Wise JA","authors_abbrev":"Bähler J et al.","pubmed_publication_date":"03 Apr 2017","pubmed_entrez_date":"2017-04-05","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-04-06 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19734666","title":"A simple and specific procedure to permeabilize the plasma membrane of Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2009 Sep;73(9):2090-5","abstract":"Cu(2+)-treatment is a useful technique in selectively permeabilizing the fungal plasma membrane. We describe herein a practical application with Schizosaccharomyces pombe. Incubation of cells with 0.5 mM CuCl(2) at 30 degrees C for 20 min induced efficient leakage of cytosolic constituents. The kinetic characteristics of the calcium and amino acid flux from Cu(2+)-treated S. pombe cells suggested that the Cu(2+) treatment permeabilized the plasma membrane without loss of vacuolar function. As a further application of the method, the amino acid contents of Cu(2+)-treated and untreated cells were also determined. The amino acid pool of Cu(2+)-treated wild-type cells was enriched in basic amino acids but not in acidic amino acids, as is characteristic of the vacuolar amino acid pool of fungi, including Saccharomyces cerevisiae and Neurosporra crassa. The amino acid pool of the S. pombe V-ATPase mutant vma1Delta was also successfully determined. We conclude that the vacuolar amino acid pool of S. pombe can be measured using Cu(2+)-treated cells. The method is simple, inexpensive, and rapid relative to the isolation of vacuolar vesicles, making it useful in estimating vacuolar pools and transport across the vacuolar membrane.","authors":"Chardwiriyapreecha S, Hondo K, Inada H, Chahomchuen T, Sekito T, Iwaki T, Kakinuma Y","authors_abbrev":"Chardwiriyapreecha S et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-09-08","publication_year":"2009","canto_session_key":"35b5b191ed2039f2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-01 13:45:29","canto_approved_date":"2025-04-09 06:41:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-26 11:00:25","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC343.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-01"},{"uniquename":"PMID:3443299","title":"The RNA components of Schizosaccharomyces pombe RNase P are essential for cell viability.","citation":"Gene 1987;60(2-3):157-61","abstract":"The fission yeast Schizosaccharomyces pombe contains in the haploid genome one copy of the gene (designated rrkl) for the RNA components of RNase P. Gene disruption in diploid cells of one copy of rrkl resulted in a moderate reduction of the level of cellular RNase P activity. Haploidization by meiosis demonstrated that rrkl is required for cell growth. Thus, the RNA components of S. pombe RNase P are essential in vivo. This is similar to the situation in Escherichia coli.","authors":"Cherayil B, Krupp G, Schuchert P, Char S, Söll D","authors_abbrev":"Cherayil B et al.","pubmed_publication_date":"1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_session_key":"94cf820b62c19f47","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 15:45:13","canto_approved_date":"2020-07-13 14:13:59","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-20 13:47:57","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.128"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-17"},{"uniquename":"PMID:8635736","title":"Differential expression of the rhp51+ gene, a recA and RAD51 homolog from the fission yeast Schizosaccharomyces pombe.","citation":"Gene 1996 Feb 22;169(1):125-30","abstract":"The rhp51+ gene encodes three transcripts of 1.9, 1.6 and 1.3 kb which have at least six polyadenylation sites. Primer-extension analysis revealed that two transcription start points (tsp) at - 166 and - 136 were responsible for the DNA damage inducibility of this gene. Northern blot analyses showed that the three transcripts were expressed differentially in response to a variety of DNA damage. During the mitotic cell cycle, only the largest transcript exhibited periodic expression, reaching the maximal level in front of the cdc22+ transcript which peaks at the G1/S boundary. Unexpectedly, the steady-state levels of the three transcripts were differentially regulated during the growth cycle. The largest and smallest transcripts accumulated in large quantity at the diauxic shift and during the entry into stationary phase, respectively. To localize the regions responsible for the differential expression of rhp51+, we constructed rhp51::ura4 and ura4::rhp51 hybrid genes, and analyzed their expression patterns in response to methyl methanesulfonate (MMS)-induced DNA damage. The results showed that the promoter region and 5' half of rhp51+ are sufficient to confer damage-responsiveness while the 3' end of the gene alone can direct the formation of multiple, discrete 3' ends of the transcripts. From these results, we conclude that this novel one gene-multiple product system is possible through the cooperation of both the promoter and 3' terminal regions.","authors":"Jang YK, Jin YH, Myung K, Seong RH, Hong SH, Park SD","authors_abbrev":"Jang YK et al.","pubmed_publication_date":"22 Feb 1996","pubmed_entrez_date":"1996-02-22","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4018034","title":"Cloning, sequencing and transcriptional control of the Schizosaccharomyces pombe cdc10 'start' gene.","citation":"EMBO J 1985 Feb;4(2):457-63","abstract":"The cdc10 'start' gene from the fission yeast Schizosaccharomyces pombe has been cloned by rescue of mutant function. It is present as a single copy in the haploid genome. Hybridisation of the gene to Northern blots has identified a low abundance 2.7-kb polyadenylated RNA. Study of RNA extracted from cells both entering stationary phase and undergoing synchronous cell divisions suggests that commitment to the cell cycle is not controlled by regulation of cdc10 transcript level. DNA sequence analysis of the gene has identified an open reading frame capable of encoding a protein of mol. wt. 85 400. The putative cdc10 gene product shows no significant primary structure similarity with products of other fission and budding yeast cell cycle genes, or with other protein sequences in several databases.","authors":"Aves SJ, Durkacz BW, Carr A, Nurse P","authors_abbrev":"Aves SJ et al.","pubmed_publication_date":"Feb 1985","pubmed_entrez_date":"1985-02-01","publication_year":"1985","canto_session_key":"3476287ff34d635d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-10-14 15:17:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-09-30 11:32:13","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.12c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-09-30"},{"uniquename":"PMID:21676862","title":"Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex.","citation":"Proc Natl Acad Sci U S A 2011 Aug 16;108(33):E463-71","abstract":"Actin-related protein (Arp) 2/3 complex mediates the formation of actin filament branches during endocytosis and at the leading edge of motile cells. The pathway of branch formation is ambiguous owing to uncertainty regarding the stoichiometry and location of VCA binding sites on Arp2/3 complex. Isothermal titration calorimetry showed that the CA motif from the C terminus of fission yeast WASP (Wsp1p) bound to fission yeast and bovine Arp2/3 complex with a stoichiometry of 2 to 1 and very different affinities for the two sites (K(d)s of 0.13 and 1.6 μM for fission yeast Arp2/3 complex). Equilibrium binding, kinetic, and cross-linking experiments showed that (i) CA at high-affinity site 1 inhibited Arp2/3 complex binding to actin filaments, (ii) low-affinity site 2 had a higher affinity for CA when Arp2/3 complex was bound to actin filaments, and (iii) Arp2/3 complex had a much higher affinity for free CA than VCA cross-linked to an actin monomer. Crystal structures showed the C terminus of CA bound to the low-affinity site 2 on Arp3 of bovine Arp2/3 complex. The C helix is likely to bind to the barbed end groove of Arp3 in a position for VCA to deliver the first actin subunit to the daughter filament.","doi":"10.1073/pnas.1100125108","authors":"Ti SC, Jurgenson CT, Nolen BJ, Pollard TD","authors_abbrev":"Ti SC et al.","pubmed_publication_date":"16 Aug 2011","pubmed_entrez_date":"2011-06-17","publication_year":"2011","canto_session_key":"5564a30a271f4dce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-18 18:35:54","canto_approved_date":"2022-08-26 07:25:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-17 10:35:02","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11H11.06","SPAC630.03","SPAC4F10.15c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-10-18"},{"uniquename":"PMID:17524442","title":"Expression and characterization of a novel reverse transcriptase of the LTR retrotransposon Tf1.","citation":"Virology 2007 Sep 30;366(2):263-76","abstract":"The LTR retrotransposon of Schizosacharomyces pombe, Tf1, has several distinctive properties that can be related to the unique properties of its reverse transcriptase (RT). Consequently, we expressed, purified and studied the recombinant Tf1 RT. This monomeric protein possesses all activities typical to RTs: DNA and RNA-dependent DNA polymerase as well as an inherent ribonuclease H. The DNA polymerase activity shows preference to Mn(+)(2) or Mg(+)(2), depending on the substrate used, whereas the ribonuclease H strongly prefers Mn(+)(2). The most outstanding feature of Tf1 RT is its capacity to add non-templated nucleotides to the 3'-ends of the nascent DNA. This is mainly apparent in the presence of Mn(+)(2), as is the noticeable low fidelity of DNA synthesis. In all, Tf1 RT has a marked infidelity in synthesizing DNA at template ends, a phenomenon that can explain, as discussed herein, some of the features of Tf1 replication in the host cells.","authors":"Kirshenboim N, Hayouka Z, Friedler A, Hizi A","authors_abbrev":"Kirshenboim N et al.","pubmed_publication_date":"30 Sep 2007","pubmed_entrez_date":"2007-05-26","publication_year":"2007","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC00293","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38058589","title":"3D models of fungal chromosomes to enhance visual integration of omics data.","citation":"NAR Genom Bioinform 2023 Dec;5(4):lqad104","abstract":"The functions of eukaryotic chromosomes and their spatial architecture in the nucleus are reciprocally dependent. Hi-C experiments are routinely used to study chromosome 3D organization by probing chromatin interactions. Standard representation of the data has relied on contact maps that show the frequency of interactions between parts of the genome. In parallel, it has become easier to build 3D models of the entire genome based on the same Hi-C data, and thus benefit from the methodology and visualization tools developed for structural biology. 3D modeling of entire genomes leverages the understanding of their spatial organization. However, this opportunity for original and insightful modeling is underexploited. In this paper, we show how seeing the spatial organization of chromosomes can bring new perspectives to omics data integration. We assembled state-of-the-art tools into a workflow that goes from Hi-C raw data to fully annotated 3D models and we re-analysed public omics datasets available for three fungal species. Besides the well-described properties of the spatial organization of their chromosomes (Rabl conformation, hypercoiling and chromosome territories), our results highlighted (i) in  Saccharomyces cerevisiae , the backbones of the cohesin anchor regions, which were aligned all along the chromosomes, (ii) in  Schizosaccharomyces pombe , the oscillations of the coiling of chromosome arms throughout the cell cycle and (iii) in  Neurospora crassa , the massive relocalization of histone marks in mutants of heterochromatin regulators. 3D modeling of the chromosomes brings new opportunities for visual integration of omics data. This holistic perspective supports intuition and lays the foundation for building new concepts.","doi":"10.1093/nargab/lqad104","authors":"Poinsignon T, Gallopin M, Grognet P, Malagnac F, Lelandais G, Poulain P","authors_abbrev":"Poinsignon T et al.","pubmed_publication_date":"Dec 2023","pubmed_entrez_date":"2023-12-07","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-12-08 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17121544","title":"Fission yeast Tor2 links nitrogen signals to cell proliferation and acts downstream of the Rheb GTPase.","citation":"Genes Cells 2006 Dec;11(12):1367-79","abstract":"The target of rapamycin (Tor) plays a pivotal role in cell growth and metabolism. Yeast contains two related proteins, Tor1 and Tor2. In fission yeast, Tor1 is dispensable for normal growth but is involved in amino acid uptake and cell survival under various stress conditions. In contrast, Tor2 is essential for cell proliferation; however, its physiological function remains unknown. Here we characterize the roles of fission yeast Tor2 by creating temperature sensitive (tor2(ts)) mutants. Remarkably, we have found that tor2(ts) mimics nitrogen starvation responses, because the mutant displays a number of phenotypes that are normally induced only on nitrogen deprivation. These include G1 cell-cycle arrest with a small cell size, induction of autophagy and commitment to sexual differentiation. By contrast, tor1Deltator2(ts) double mutant cells show distinct phenotypes, as the cells cease division with normal cell size in the absence of G1 arrest. Tor2 physically interacts with the conserved Rhb1/GTPase. Intriguingly, over-expression of rhb1(+) or deletion of Rhb1-GAP-encoding tsc2(+) is capable of rescuing stress-sensitive phenotypes of the tor1 mutant, implying that Tor1 and Tor2 also share functions in cell survival under adverse environment. We propose that Tor1 and Tor2 are involved in both corroborative and independent roles in nutrient sensing and stress response pathways.","authors":"Uritani M, Hidaka H, Hotta Y, Ueno M, Ushimaru T, Toda T","authors_abbrev":"Uritani M et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-11-24","publication_year":"2006","canto_session_key":"5776ed0daa755f60","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-05-24 13:15:29","canto_approved_date":"2026-01-31 15:26:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-24 13:13:51","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.16c","SPAC4A8.04","SPBC30D10.10c","SPBC216.07c","SPAC630.13c","SPAC22F3.13"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2021-05-24"},{"uniquename":"PMID:8521500","title":"p25rum1 orders S phase and mitosis by acting as an inhibitor of the p34cdc2 mitotic kinase.","citation":"Cell 1995 Dec 15;83(6):1001-9","abstract":"p25rum1 from the fission yeast S. pombe is shown to act as a specific in vitro inhibitor of the p34cdc2/p56cdc13 mitotic kinase. It is also shown that early G1 cells contain p25rum1, which associates with and inhibits the mitotic kinase, and maintains p56cdc13 mitotic B cyclin at a low level, ensuring that these cells do not undergo a premature lethal entry into mitosis. A high level of p25rum1 in G2 cells inhibits the p34cdc2/p56cdc13 kinase that removes the block preventing a further S phase and leads to repeated rounds of DNA replication. Thus, the cyclin-dependent kinase inhibitor p25rum1, acting on the p34cdc2 mitotic kinase, plays an important role in ensuring the correct sequence of S phase and mitosis during the cell cycle.","authors":"Correa-Bordes J, Nurse P","authors_abbrev":"Correa-Bordes J et al.","pubmed_publication_date":"15 Dec 1995","pubmed_entrez_date":"1995-12-15","publication_year":"1995","canto_session_key":"93c624d8e120755e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-06-19 04:55:57","canto_approved_date":"2025-07-02 06:26:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-03-19 11:22:18","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":20,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC18B5.03","SPCC4E9.02","SPAC24H6.05","SPBC336.12c","SPBC25H2.13c","SPBC660.14","SPBC32F12.09","SPAPB2B4.03","SPBC582.03"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2018-06-19"},{"uniquename":"PMID:17591689","title":"Microtubules offset growth site from the cell centre in fission yeast.","citation":"J Cell Sci 2007 Jul 01;120(Pt 13):2205-13","abstract":"The design principles that underlie cellular morphogenetic mechanisms are central to understanding the generation of cell form. We have investigated the constraints governing the formation and positioning of new growth zones in the fission yeast cell and have shown that establishment of a new axis of polarity is independent of microtubules and that in the absence of microtubules a new growth zone is activated near the nucleus in the middle of the cell. Activation of a new growth zone can occur at any stage of the cell cycle as long as the nucleus is a sufficient distance away from previously growing ends. The positioning of growth zones is regulated by the polarity marker Tea1 delivered by microtubules; cells with short microtubules locate the growth zone near the region where the microtubules terminate. We propose a model for the activation of new growth zones comprising a long-range laterally inhibitory component and a self-activating positive local component that is delivered to cell ends by Tea1 and the microtubules. The principle of this symmetry-breaking design may also apply to the morphogenesis of other cells.","authors":"Castagnetti S, Novák B, Nurse P","authors_abbrev":"Castagnetti S et al.","pubmed_publication_date":"01 Jul 2007","pubmed_entrez_date":"2007-06-27","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28470426","title":"The yeasts phosphorelay systems: a comparative view.","citation":"World J Microbiol Biotechnol 2017 Jun;33(6):111","abstract":"Cells contain signal transduction pathways that mediate communication between the extracellular environment and the cell interior. These pathways control transcriptional programs and posttranscriptional processes that modify cell metabolism in order to maintain homeostasis. One type of these signal transduction systems are the so-called Two Component Systems (TCS), which conduct the transfer of phosphate groups between specific and conserved histidine and aspartate residues present in at least two proteins; the first protein is a sensor kinase which autophosphorylates a histidine residue in response to a stimulus, this phosphate is then transferred to an aspartic residue located in a response regulator protein. There are classical and hybrid TCS, whose difference consists in the number of proteins and functional domains involved in the phosphorelay. The TCS are widespread in bacteria where the sensor and its response regulator are mostly specific for a given stimulus. In eukaryotic organisms such as fungi, slime molds, and plants, TCS are present as hybrid multistep phosphorelays, with a variety of arrangements (Stock et al. in Annu Rev Biochem 69:183-215, 2000; Wuichet et al. in Curr Opin Microbiol 292:1039-1050, 2010). In these multistep phosphorelay systems, several phosphotransfer events take place between different histidine and aspartate residues localized in specific domains present in more than two proteins (Thomason and Kay, in J Cell Sci 113:3141-3150, 2000; Robinson et al. in Nat Struct Biol 7:626-633, 2000). This review presents a brief and succinct description of the Two-component systems of model yeasts, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida albicans, Cryptococcus neoformans and Kluyveromyces lactis. We have focused on the comparison of domain organization and functions of each component present in these phosphorelay systems.","doi":"10.1007/s11274-017-2272-z","authors":"Salas-Delgado G, Ongay-Larios L, Kawasaki-Watanabe L, López-Villaseñor I, Coria R","authors_abbrev":"Salas-Delgado G et al.","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2017-05-05","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-05-06 00:15:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11709168","title":"The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast.","citation":"Structure 2001 Nov;9(11):1043-50","abstract":"The small GTP binding protein Ras has important roles in cellular growth and differentiation. Mutant Ras is permanently active and contributes to cancer development. In its activated form, Ras interacts with effector proteins, frequently initiating a kinase cascade. In the lower eukaryotic Schizosaccharomyces pombe, Byr2 kinase represents a Ras target that in terms of signal-transduction hierarchy can be considered a homolog of mammalian Raf-kinase. The activation mechanism of protein kinases by Ras is not understood, and there is no detailed structural information about Ras binding domains (RBDs) in nonmammalian organisms.\nThe crystal structure of the Ras-Byr2RBD complex at 3 A resolution shows a complex architecture similar to that observed in mammalian homologous systems, with an interprotein beta sheet stabilized by predominantly polar interactions between the interacting components. The C-terminal half of the Ras switch I region contains most of the contact anchors, while on the Byr2 side, a number of residues from topologically distinct regions are involved in complex stabilization. A C-terminal helical segment, which is not present in the known mammalian homologous systems and which is part of the auto-inhibitory region, has an additional binding site outside the switch I region.\nThe structure of the Ras-Byr2 complex confirms the Ras binding module as a communication element mediating Ras-effector interactions; the Ras-Byr2 complex is also conserved in a lower eukaryotic system like yeast, which is in contrast to other small GTPase families. The extra helical segment might be involved in kinase activation.","authors":"Scheffzek K, Grünewald P, Wohlgemuth S, Kabsch W, Tu H, Wigler M, Wittinghofer A, Herrmann C","authors_abbrev":"Scheffzek K et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2001-11-16","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1D7.05"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"1k8r","gene_chains":[{"gene_uniquename":"SPBC1D7.05","chain":"B","position":"71-180"}],"title":"Crystal structure of Ras-Bry2RBD complex","entry_authors":"Scheffzek K,Gruenewald P,Wohlgemuth S,Kabsch W,Tu H,Wigler M,Wittinghofer A,Herrmann C","entry_authors_abbrev":"Scheffzek K et al.","reference_uniquename":"PMID:11709168","experimental_method":"X-ray","resolution":"3.0"}]},{"uniquename":"PMID:16049679","title":"Mpg1, a fission yeast protein required for proper septum structure, is involved in cell cycle progression through cell-size checkpoint.","citation":"Mol Genet Genomics 2005 Sep;274(2):155-67","abstract":"Using a yeast two-hybrid screen we isolated a gene from Schizosaccharomyces pombe which corresponds to the previously uncharacterized ORF SPCC1906.01. We have designated this gene as mpg1, based on the putative function of its product as a mannose-1-phosphatase guanyltransferase. Mpg1 shows strong similarity to other GDP-mannose-1-phosphate guanyltransferases involved in the maintenance of cell wall integrity and/or glycosylation. This homology, together with the protein's localization pattern demonstrated in this work, strongly suggests that Mpg1 is involved in cell wall and septum synthesis. Moreover, cells lacking Mpg1 present a defect in glycosylation, are more sensitive to Lyticase, and show an aberrant septum structure from the start of its deposition, indicating that the Mpg1 function is necessary for the correct assembly of the septum. Interestingly, lack of Mpg1 clearly affects cell cycle progression: mpg1 null mutants arrest as septated and bi-nucleated 4C cells, without an actomyosin ring. Wee1 is required for the G2/M arrest induced in the absence of Mpg1, since the blockade is circumvented when Wee1 is inactivated. Wee1 is part of a cell-size checkpoint that prevents entry into mitosis before cells reach a critical size. The results presented in this work demonstrate that the G2/M arrest induced in the absence of Mpg1 is mediated by this cell size checkpoint, since oversized mutant cells enter mitosis. The mpg1 loss-of-function mutant, therefore, provides a good model in which to study how cells coordinate cell growth and cell division.","authors":"Donoso I, Muñoz-Centeno MC, Sànchez-Durán MA, Flores A, Daga RR, Guevara CM, Bejarano ER","authors_abbrev":"Donoso I et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-07-29","publication_year":"2005","canto_session_key":"eb090de8a5e6eecf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-05-05 13:31:44","canto_approved_date":"2020-12-30 21:21:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-03 16:01:38","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPCC191.11","SPCC1906.01","SPAC1782.09c"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2017-05-05"},{"uniquename":"PMID:8568444","title":"Ultrahigh-resolution low-voltage SEM reveals ultrastructure of the glucan network formation from fission yeast protoplast.","citation":"J Electron Microsc (Tokyo) 1995 Aug;44(4):198-206","abstract":"The refined field emission SEM, S-900 LV which gives better resolution especially at low voltages below 5 kV was developed for ultrahigh resolution scanning electron microscopy. A visualization test at x 300,000 was made using a gold-evaporated magnetic tape, and the resolution was found to be about 1 nm at 2.5 kV. The ultrastructure of the cell wall, especially the reverting glucan network, from the protoplast of Schizosaccharomyces pombe was studied using this improved ultrahigh-resolution low-voltage SEM (UHR-LVSEM). The results with uncoated reverting protoplasts observed with this microscope revealed that the network was originally formed as secreted particles scattered on the protoplast surface and these were subsequently stretched to microfibrils about 2 nm thick. The microfibrils were twisted around each other and joined together so that they developed into 8-nm-thick fibrils, forming a ribbon-shaped network of glucans about 16-nm-thick which covered the entire protoplast surface. The UHR-LVSEM images of reverting protoplasts treated with glucanase confirmed that the particles scattered on the protoplast surface in the initial stage of regeneration were glucan in nature.","authors":"Osumi M, Yamada N, Yaguchi H, Kobori H, Nagatani T, Sato M","authors_abbrev":"Osumi M et al.","pubmed_publication_date":"Aug 1995","pubmed_entrez_date":"1995-08-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30996236","title":"Functional Analysis of Conserved Transmembrane Charged Residues and a Yeast Specific Extracellular Loop of the Plasma Membrane Na + /H +  Antiporter of Schizosaccharomyces pombe.","citation":"Sci Rep 2019 Apr 17;9(1):6191","abstract":"The Na + /H +  exchanger of the plasma membrane of S. pombe (SpNHE1) removes excess intracellular sodium in exchange for an extracellular proton. We examined the functional role of acidic amino acids of a yeast specific periplasmic extracellular loop 6 (EL6) and of Glu 74  and Arg 77  of transmembrane segment 3. Glu 74  and Arg 77  are conserved in yeast species while Glu 74  is conserved throughout various phyla. The mutation E74A caused a minor effect, while mutation R77A had a larger effect on the ability of SpNHE1 to confer salt tolerance. Mutation of both residues to Ala or Glu also eliminated the ability to confer salt tolerance. Arg 341  and Arg 342  were also necessary for SpNHE1 transport in S. pombe. Deletion of 3 out of 4 acidic residues (Asp 389 , Glu 390 , Glu 392 , Glu 397 ) of EL6 did not greatly affect SpNHE1 function while deletion of all did. Replacement of EL6 with a segment from the plant Na + /H +  exchanger SOS1 also did not affect function. We suggest that EL6 forms part of a cation coordination sphere, attracting cations for transport but that the region is not highly specific for the location of acidic charges. Overall, we identified a number of polar amino acids important in SpNHE1 function.","doi":"10.1038/s41598-019-42658-0","authors":"Dutta D, Ullah A, Bibi S, Fliegel L","authors_abbrev":"Dutta D et al.","pubmed_publication_date":"17 Apr 2019","pubmed_entrez_date":"2019-04-19","publication_year":"2019","canto_session_key":"0a79c8dca3733456","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-05-16 09:28:03","canto_approved_date":"2022-09-21 17:08:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-01 20:21:35","canto_added_date":"2019-04-20 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-05-16"},{"uniquename":"PMID:19664555","title":"Prevention of bacterial contamination using acetate-tolerant Schizosaccharomyces pombe during bioethanol production from molasses.","citation":"J Biosci Bioeng 2009 Sep;108(3):216-9","abstract":"Bacterial contamination causes yield reduction during ethanol production from molasses. To prevent contamination, construction of a fermentation system using acetate-tolerant yeast under an acetate-containing condition was attempted. Schizosaccharomyces pombe was screened as an acetate-tolerant strain. Bacterial contamination was significantly prevented by the combined use of Sc. pombe and acetate.","doi":"10.1016/j.jbiosc.2009.03.022","authors":"Saithong P, Nakamura T, Shima J","authors_abbrev":"Saithong P et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-08-12","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2566512","title":"New expression vectors for the fission yeast Schizosaccharomyces pombe.","citation":"FEBS Lett 1989 May 08;248(1-2):105-10","abstract":"A general expression vector (pMB332) for the fission yeast Schizosaccharomyces pombe was constructed. The heterologous gene expression is driven by the S. pombe alcohol dehydrogenase (adh) promoter. Transcription termination signals were isolated from the S. pombe actin gene. The vectors carry the Saccharomyces cerevisiae Ura3 gene, which complements the S. pombe ura4 mutation. The plasmid stability is conferred by the S. pombe ars and stb elements isolated from pFL120 [(1983) Cell 32, 371-377]. An 'ATG' vector (pMB340) was created, which allows the expression of protein fragments fused to a translational start codon downstream of the adh promoter. The function of this vector system is shown by the production of the human blood coagulation protein factor XIIIa.","authors":"Bröker M, Bäuml O","authors_abbrev":"Bröker M et al.","pubmed_publication_date":"08 May 1989","pubmed_entrez_date":"1989-05-08","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28367989","title":"The conserved protein Seb1 drives transcription termination by binding RNA polymerase II and nascent RNA.","citation":"Nat Commun 2017 Apr 03;8:14861","abstract":"Termination of RNA polymerase II (Pol II) transcription is an important step in the transcription cycle, which involves the dislodgement of polymerase from DNA, leading to release of a functional transcript. Recent studies have identified the key players required for this process and showed that a common feature of these proteins is a conserved domain that interacts with the phosphorylated C-terminus of Pol II (CTD-interacting domain, CID). However, the mechanism by which transcription termination is achieved is not understood. Using genome-wide methods, here we show that the fission yeast CID-protein Seb1 is essential for termination of protein-coding and non-coding genes through interaction with S2-phosphorylated Pol II and nascent RNA. Furthermore, we present the crystal structures of the Seb1 CTD- and RNA-binding modules. Unexpectedly, the latter reveals an intertwined two-domain arrangement of a canonical RRM and second domain. These results provide important insights into the mechanism underlying eukaryotic transcription termination.","doi":"10.1038/ncomms14861","authors":"Wittmann S, Renner M, Watts BR, Adams O, Huseyin M, Baejen C, El Omari K, Kilchert C, Heo DH, Kecman T, Cramer P, Grimes JM, Vasiljeva L","authors_abbrev":"Wittmann S et al.","pubmed_publication_date":"03 Apr 2017","pubmed_entrez_date":"2017-04-04","publication_year":"2017","canto_session_key":"66c9ead399a6a1ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sina Wittmann","canto_first_approved_date":"2018-02-09 12:53:12","canto_approved_date":"2024-02-26 18:43:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-21 12:42:57","canto_added_date":"2017-04-05 00:15:12","annotation_curators":[{"name":"Sina Wittmann","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC227.08c","SPAC6F12.17","SPAC26A3.12c","SPAC12G12.14c","SPAC57A7.04c","SPAC1071.01c","SPBC28F2.12","SPAC1F7.07c","SPBC1709.15c","SPBC337.03","SPAC222.09","SPAC4G9.04c","SPBC1709.08","SPAC17G6.16c"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2018-02-09","pdb_entries":[{"pdb_id":"5mdu","gene_chains":[{"gene_uniquename":"SPAC222.09","chain":"A","position":"388-540"}],"title":"Structure of the RNA recognition motif (RRM) of Seb1 from S. pombe.","entry_authors":"Wittmann S,Renner M,El Omari K,Adams O,Vasiljeva L,Grimes J","entry_authors_abbrev":"Wittmann S et al.","reference_uniquename":"PMID:28367989","experimental_method":"X-ray","resolution":"1.02"},{"pdb_id":"5mdt","gene_chains":[{"gene_uniquename":"SPAC222.09","chain":"A","position":"1-152"}],"title":"Structure of the CTD-interacting domain (CID) of Seb1 from S. pombe.","entry_authors":"Wittmann S,Renner M,Vasiljeva L,Grimes J","entry_authors_abbrev":"Wittmann S et al.","reference_uniquename":"PMID:28367989","experimental_method":"X-ray","resolution":"1.62"}]},{"uniquename":"PMID:17381328","title":"Studies on the mechanism of RNAi-dependent heterochromatin assembly.","citation":"Cold Spring Harb Symp Quant Biol 2006;71:461-71","abstract":"Assembly of heterochromatin at centromeric DNA regions in the fission yeast Schizosaccharomyces pombe involves an intimate interplay between chromatin modifying complexes and components of the RNAi pathway. The RNA-induced transcriptional silencing (RITS) complex, containing Chp1, Ago1, Tas3, and centromeric siRNAs, localizes to centromeric DNA repeats and is required for the assembly and maintenance of heterochromatin. RITS brings together two types of molecular recognition modules: a chromodomain protein, which binds to lysine 9 methylated histone H3 (H3K9), and Argonaute, which binds to specific sequences by siRNA-directed base-pairing interactions. The RNA-directed RNA polymerase complex (RDRC), composed of Rdp1, the Hrr1 helicase, and the Cid12 Poly(A) polymerase family member, synthesizes double-stranded RNA and creates the substrate for Dicer to generate siRNAs. RDRC physically associates with RITS, and both complexes localize to noncoding centromeric RNAs and centromeric DNA repeats, suggesting that recognition of nascent RNA transcripts may be involved in localization of these complexes to specific chromosome regions. In support of this possibility, tethering of the RITS complex to the transcript of the normally euchromatic ura4 (+) gene results in siRNA generation and RNAi- and heterochromatin-dependent silencing of the ura4 (+) gene. Finally, silencing of a subset of endogenous and transgene promoters within heterochromatic DNA domains occurs by RNAi-dependent degradation of nascent transcripts by a mechanism that we have termed co-transcriptional gene silencing (CTGS).","authors":"Moazed D, Bühler M, Buker SM, Colmenares SU, Gerace EL, Gerber SA, Hong EJ, Motamedi MR, Verdel A, Villén J, Gygi SP","authors_abbrev":"Moazed D et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-03-27","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20013338","title":"Overexpression of protein disulfide isomerases enhances secretion of recombinant human transferrin in Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2010 Apr;86(4):1135-43","abstract":"Although the fission yeast Schizosaccharomyces pombe has been used for high-level heterologous protein production, the productivity of secreted human serum transferrin (hTF) has been low, presumably, because the protein harbors twenty disulfide bonds and two N-glycosylation sites. In the present study, we found that overexpression of endogenous putative protein disulfide isomerase (PDI) improved productivity. Whole genome sequence analysis of S. pombe revealed five putative PDI genes and overexpression of two of them, SPAC17H9.14c and SPBC3D6.13c (SpPdi2p or SpPdi3p, respectively), significantly improved the productivity of secreted hTF. GFP-fused SpPdi2p and SpPdi3p were found to localize to the endoplasmic reticulum. Co-overexpression of SpPdi2p or SpPdi3p with hTF coupled with modifications to the growth medium reported in our previous study were able to increase the level of secreted hTF approximately 30-fold relative to conventional conditions.","doi":"10.1007/s00253-009-2393-x","authors":"Mukaiyama H, Tohda H, Takegawa K","authors_abbrev":"Mukaiyama H et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2009-12-17","publication_year":"2010","canto_session_key":"b7b90222a52ec909","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-05-20 09:14:50","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-04-04 14:51:24","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.13c","SPAC17H9.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-04-04"},{"uniquename":"PMID:7432372","title":"The use of organic solvents in mutagenicity testing.","citation":"Mutat Res 1980 Oct;79(2):141-50","abstract":"13 organic substances (dimethylsulfoxide, methanol, ethanol, n-propyl alcohol, sec-butyl alcohol, tert-butyl alcohol, dl-sec-amyl alcohol, ethylene glycol, ethylene glycol monomethyl ether, 1,4-diethylene dioxide, acetone, methyl acetate and formamide) were considered from the standpoint of their use as solvents for water-insoluble chemicals to be tested for mutagenicity. First, the effect of these solvents on cell survival was studied in the yeast Schizosaccharomyces pombe and in V79 Chinese hamster cells. 8 solvents showing relatively low toxicity on either cell system (dimethylsulfoxide, ethanol, ethylene glycol, ethylene glycol monomethyl ether, 1,4-diethylene dioxide, acetone, methyl acetate and formamide) were tested for their effect on aminopyrine demethylase. 4 solvents (ethanol, 1,4-diethylene dioxide, methyl acetate and formamide) showed a more or less pronounced adverse effect on the microsomal enzymic activity. The remaining 4 and methanol (whose effect on aminopyrine demethylase was not testable) were assayed for mutagenicity in S. pombe. They all gave negative results both with and without the post-mitochondrial fraction from mouse liver.","authors":"Abbondandolo A, Bonatti S, Corsi C, Corti G, Fiorio R, Leporini C, Mazzaccaro A, Nieri R, Barale R, Loprieno N","authors_abbrev":"Abbondandolo A et al.","pubmed_publication_date":"Oct 1980","pubmed_entrez_date":"1980-10-01","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU014399","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007304","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28116355","title":"Physical determinants of bipolar mitotic spindle assembly and stability in fission yeast.","citation":"Sci Adv 2017 Jan;3(1):e1601603","abstract":"Mitotic spindles use an elegant bipolar architecture to segregate duplicated chromosomes with high fidelity. Bipolar spindles form from a monopolar initial condition; this is the most fundamental construction problem that the spindle must solve. Microtubules, motors, and cross-linkers are important for bipolarity, but the mechanisms necessary and sufficient for spindle assembly remain unknown. We describe a physical model that exhibits de novo bipolar spindle formation. We began with physical properties of fission-yeast spindle pole body size and microtubule number, kinesin-5 motors, kinesin-14 motors, and passive cross-linkers. Our model results agree quantitatively with our experiments in fission yeast, thereby establishing a minimal system with which to interrogate collective self-assembly. By varying the features of our model, we identify a set of functions essential for the generation and stability of spindle bipolarity. When kinesin-5 motors are present, their bidirectionality is essential, but spindles can form in the presence of passive cross-linkers alone. We also identify characteristic failed states of spindle assembly-the persistent monopole, X spindle, separated asters, and short spindle, which are avoided by the creation and maintenance of antiparallel microtubule overlaps. Our model can guide the identification of new, multifaceted strategies to induce mitotic catastrophes; these would constitute novel strategies for cancer chemotherapy.","doi":"10.1126/sciadv.1601603","authors":"Blackwell R, Edelmaier C, Sweezy-Schindler O, Lamson A, Gergely ZR, O'Toole E, Crapo A, Hough LE, McIntosh JR, Glaser MA, Betterton MD","authors_abbrev":"Blackwell R et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2017-01-25","publication_year":"2017","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2017-01-26 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4225287","title":"The effect of fluorouracil and fluorodeoxyuridine on the genetic recombination in Schizosaccharomyces pombe.","citation":"Experientia 1966 Mar 15;22(3):151-2","abstract":"","authors":"Megnet R","authors_abbrev":"Megnet R","pubmed_publication_date":"15 Mar 1966","pubmed_entrez_date":"1966-03-15","publication_year":"1966","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11726502","title":"Fission yeast Rad50 stimulates sister chromatid recombination and links cohesion with repair.","citation":"EMBO J 2001 Dec 03;20(23):6660-71","abstract":"To study the role of Rad50 in the DNA damage response, we cloned and deleted the Schizosaccharomyces pombe RAD50 homologue. The deletion is sensitive to a range of DNA-damaging agents and shows dynamic epistatic interactions with other recombination-repair genes. We show that Rad50 is necessary for recombinational repair of the DNA lesion at the mating-type locus and that rad50Delta shows slow DNA replication. We also find that Rad50 is not required for slowing down S phase in response to hydroxy urea or methyl methanesulfonate (MMS) treatment. Interestingly, in rad50Delta cells, the recombination frequency between two homologous chromosomes is increased at the expense of sister chromatid recombination. We propose that Rad50, an SMC-like protein, promotes the use of the sister chromatid as the template for homologous recombinational repair. In support of this, we found that Rad50 functions in the same pathway for the repair of MMS-induced damage as Rad21, the homologue of the Saccharomyces cerevisiae Scc1 cohesin protein. We speculate that Rad50 interacts with the cohesin complex during S phase to assist repair and possibly re-initiation of replication after replication fork collapse.","authors":"Hartsuiker E, Vaessen E, Carr AM, Kohli J","authors_abbrev":"Hartsuiker E et al.","pubmed_publication_date":"03 Dec 2001","pubmed_entrez_date":"2001-12-01","publication_year":"2001","canto_session_key":"22e0aeba5f85fb0e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-21 12:59:12","canto_approved_date":"2020-07-08 17:30:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-20 16:35:07","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13C5.07","SPAC3C7.03c","SPAC30D11.10","SPAC3G6.06c","SPCC338.17c","SPAC644.14c","SPAC1556.01c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-04-21"},{"uniquename":"PMID:40278099","title":"Regulation of Yeast Cytokinesis by Calcium.","citation":"J Fungi (Basel) 2025 Apr 02;11(4)","abstract":"The role of calcium, an essential secondary messenger, in cell division remains an outstanding question in cell biology despite several significant findings over the past few decades. Among them is the landmark discovery of intracellular calcium waves during cytokinesis, the last stage of cell division, in fish cells. Nevertheless, subsequent studies have been largely unable to determine the underlying molecular mechanism of these cytokinetic transients. At the center of this stalemate stands two challenging questions, how these calcium transients rise and what they do during cytokinesis. Yeast, despite its proven prowess as a model organism to study cell cycle, has not drawn much interest in addressing these questions. However, the recent discovery of cytokinetic calcium spikes in the fission yeast  Schizosaccharomyces pombe  has provided novel insights into how calcium regulates cytokinesis. In this review, I will primarily focus on our current understanding of the molecular mechanism of cytokinetic calcium transients in yeast cells. First, I will briefly recount the discovery of cytokinetic calcium transients in animal cells. This will be followed by an introduction to the intracellular calcium homeostasis. Next, I will discuss yeast cytokinetic calcium spikes, the ion channel Pkd2 that promotes these spikes, and the potential molecular targets of these spikes. I will also compare the calcium regulation of cytokinesis between yeast and animal cells. I will conclude by presenting a few critical questions in our continued quest to understand how calcium regulates cytokinesis.","doi":"10.3390/jof11040278","authors":"Chen Q","authors_abbrev":"Chen Q","pubmed_publication_date":"02 Apr 2025","pubmed_entrez_date":"2025-04-25","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-04-25 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9755189","title":"The Schizosaccharomyces pombe cho1+ gene encodes a phospholipid methyltransferase.","citation":"Genetics 1998 Oct;150(2):553-62","abstract":"The isolation of mutants of Schizosaccharomyces pombe defective in the synthesis of phosphatidylcholine via the methylation of phosphatidylethanolamine is reported. These mutants are choline auxotrophs and fall into two unlinked complementation groups, cho1 and cho2. We also report the analysis of the cho1+ gene, the first structural gene encoding a phospholipid biosynthetic enzyme from S. pombe to be cloned and characterized. The cho1+ gene disruption mutant (cho1Delta) is viable if choline is supplied and resembles the cho1 mutants isolated after mutagenesis. Sequence analysis of the cho1+ gene indicates that it encodes a protein closely related to phospholipid methyltransferases from Saccharomyces cerevisiae and rat. Phospholipid methyltransferases encoded by a rat liver cDNA and the S. cerevisiae OPI3 gene are both able to complement the choline auxotrophy of the S. pombe cho1 mutants. These results suggest that both the structure and function of the phospholipid N-methyltransferases are broadly conserved among eukaryotic organisms.","authors":"Kanipes MI, Hill JE, Henry SA","authors_abbrev":"Kanipes MI et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-10-02","publication_year":"1998","canto_session_key":"1c6c7baa73344225","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-17 09:06:32","canto_approved_date":"2024-08-07 15:10:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-17 09:06:26","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.03","SPBC337.16"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-04-17"},{"uniquename":"PMID:22094427","title":"Genetic approaches to aging in budding and fission yeasts: new connections and new opportunities.","citation":"Subcell Biochem 2012;57:291-314","abstract":"Yeasts are powerful model systems to examine the evolutionarily conserved aspects of eukaryotic aging because they maintain many of the same core cellular signaling pathways and essential organelles as human cells. We constructed a strain of the budding yeast Saccharomyces cerevisiae that could monitor the distribution of proteins involved in heterochromatic silencing and aging, and isolated mutants that alter this distribution. The largest class of such mutants cause defects in mitochondrial function, and appear to cause changes in nuclear silencing separate from the well-known Rtg2p-dependent pathway that alters nuclear transcription in response to the loss of the mitochondrial genome. Mutants that inactivate the ATP2 gene, which encodes the ATPase subunit of the mitochondrial F(1)F(0)-ATPase, were isolated twice in our screen and identify a lifespan extending pathway in a gene that is conserved in both prokaryotes and eukaryotes. The budding yeast S. cerevisiae S. cerevisiae has been used with great success to identify other lifespan-extending pathways in screens using surrogate phenotypes such as stress resistance or silencing to identify random mutants, or in high throughput screens that utilize the deletion strain set resource. However, the direct selection of long-lived mutants from a pool of random mutants is more challenging. We have established a new chronological aging assay for the evolutionarily distant fission yeast Schizosaccharomyces pombe that recapitulates aspects of aging conserved in all eukaryotes. We have constructed a novel S. pombe S. pombe DNA insertion mutant bank, and used it to show that we can directly select for a long-lived mutant. The use of both the budding and fission yeast systems should continue to facilitate the identification and validation of lifespan extending pathways that are conserved in humans.","doi":"10.1007/978-94-007-2561-4_13","authors":"Chen BR, Runge KW","authors_abbrev":"Chen BR et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2011-11-19","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1336448","title":"Protein phosphatases and cell division cycle control.","citation":"Ciba Found Symp 1992;170:130-40; discussion 140-6","abstract":"Fission yeast has at least ten protein phosphatase genes that appear to play distinct roles in cell cycle control. Because of functional overlap, a clear lethal phenotype can be obtained only after multiple genetic alterations. Cells that have lost the protein phosphatase 1 (PP1)-like dis2/sds21 phosphatase activities prematurely enter mitosis and remain in a defective mitotic state with high H1 kinase activity and without sister chromatid disjunction. The same phenotype can be obtained in the presence of hydroxyurea. Overexpression of PP1-like phosphatase, on the other hand, delays the entry into mitosis. Cells that have lost PP2A-like ppa2 phosphatase activity also prematurely enter mitosis with a reduction in cell size. This semi-wee phenotype is enhanced in delta ppa2 mutants treated with the phosphatase inhibitor, okadaic acid. Genetic interactions between ppa2 and mitotic regulators suggest that ppa1/ppa2 phosphatase may directly or indirectly inhibit p34cdc2/cyclin kinase. Thus both PP1- and PP2A-like phosphatases in fission yeast may negatively regulate entry into mitosis. The major property of the dis2/sds21 mutant which is distinct from those of the ppa2/ppa1 mutant is its failure to inactivate the p34cdc2/cyclin complex after entry into mitosis. A novel phosphatase regulator encoded by sds22+ binds to dis2 phosphatase and controls the substrate specificity which appears to become essential in the progression from metaphase to anaphase.","authors":"Yanagida M, Kinoshita N, Stone EM, Yamano H","authors_abbrev":"Yanagida M et al.","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14663827","title":"Role of Tea1p, Tea3p and Pom1p in the determination of cell ends in Schizosaccharomyces pombe.","citation":"Yeast 2003 Dec;20(16):1349-58","abstract":"Schizosaccharomyces pombe cells are rod-shaped and grow along a single axis from their two ends. Microtubules extend from the cell centre terminating at the cell ends. The ERM(ezrin/radixin/moesin)-like proteins Tea1p and Tea3p, and the Dyrk-like kinase Pom1p are cell end markers involved in the regulation of growth and microtubular dynamics at the cell ends. We have analysed the relative contribution of these three proteins to the determination of cell ends as sites both for cell growth and for microtubular termination. Pom1Delta, in combination with Tea1Delta or Tea3Delta, has the greatest difficulty in relocalizing actin to the cell ends following actin depolymerization and generates the most defective growth pattern. Tea1Delta, in combination with Pom1Delta or Tea3Delta, displays the highest number of microtubules bending round the cell ends. Tea1DeltaPom1Delta, which has the most defective growth pattern and microtubules, also displays the highest number of branched cells. We show that Tea1p, Tea3p and Pom1p all contribute, to different extents, to the determination of cell ends, as sites for both cell growth and microtubular termination. We also show that the fission yeast cell relies on both the positioning of landmarks and a properly organized microtubule cytoskeleton to direct cell growth.","authors":"Niccoli T, Arellano M, Nurse P","authors_abbrev":"Niccoli T et al.","pubmed_publication_date":"Dec 2003","pubmed_entrez_date":"2003-12-10","publication_year":"2003","canto_session_key":"f2155bc676f8eae1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-10-17 13:04:22","canto_approved_date":"2023-11-10 18:47:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-15 15:20:43","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G10.02c","SPAC2F7.03c","SPCC1223.06"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-10-17"},{"uniquename":"PMID:22912829","title":"Response to arsenate treatment in Schizosaccharomyces pombe and the role of its arsenate reductase activity.","citation":"PLoS One 2012;7(8):e43208","abstract":"Arsenic toxicity has been studied for a long time due to its effects in humans. Although epidemiological studies have demonstrated multiple effects in human physiology, there are many open questions about the cellular targets and the mechanisms of response to arsenic. Using the fission yeast Schizosaccharomyces pombe as model system, we have been able to demonstrate a strong activation of the MAPK Spc1/Sty1 in response to arsenate. This activation is dependent on Wis1 activation and Pyp2 phosphatase inactivation. Using arsenic speciation analysis we have also demonstrated the previously unknown capacity of S. pombe cells to reduce As (V) to As (III). Genetic analysis of several fission yeast mutants point towards the cell cycle phosphatase Cdc25 as a possible candidate to carry out this arsenate reductase activity. We propose that arsenate reduction and intracellular accumulation of arsenite are the key mechanisms of arsenate tolerance in fission yeast.","doi":"10.1371/journal.pone.0043208","authors":"Salgado A, López-Serrano Oliver A, Matia-González AM, Sotelo J, Zarco-Fernández S, Muñoz-Olivas R, Cámara C, Rodríguez-Gabriel MA","authors_abbrev":"Salgado A et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-23","publication_year":"2012","canto_session_key":"3dc249fb7bbb074a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-01 15:43:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 22:26:05","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9G1.02","SPAC24B11.06c","SPBC11B10.09","SPAC1006.09","SPBC409.07c","SPAC26F1.10c","SPAC19D5.01","SPBC887.10","SPAC24H6.05"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2014-06-30"},{"uniquename":"PMID:9077438","title":"Molecular assembly of RNA polymerase II from the fission yeast Schizosaccharomyces pombe: subunit-subunit contact network involving Rpb5.","citation":"Genes Cells 1996 Sep;1(9):843-54","abstract":"Eukaryotic RNA polymerase II is composed of more than 10 polypeptide chains. The minimum and essential subunits for RNA synthesis have not yet been identified. Toward this ultimate goal, we analysed the topological arrangement of the putative subunits. Here we report a subunit-subunit contact network involving subunit 5 of the fission yeast Schizosaccharomyces pombe RNA polymerase II.\nThe rpb5+ gene encoding subunit 5 of RNA polymerase II was cloned from the fission yeast Schizosaccharomyces pombe. The polypeptide predicted from DNA sequence of the rpb5+ gene consists of 210 amino acids with a calculated molecular weight of 23914. The homology of the amino acid sequence is 55% and 43% with Saccharomyces cerevisiae RPB5 and human hRPB25, respectively. Far-Western blot analysis of S. pombe RNA polymerase II using 32P-labelled recombinant Rpb5 fused to glutathione S-transferase (GST) as a probe, indicated that Rpb5 binds strongly to membrane-immobilized Rpb1, Rpb2 and Rpb3 and weakly to Rpb5 and a 15-kDa subunit (Rpb8 or Rpb11). In agreement with this result, the 32P-labelled Rpb3 probe showed a strong binding signal against Rpb5 in addition to Rpb1 and Rpb2. The existence of Rpb5-Rpb3 contact was supported by detection of complexes formed between these two proteins synthesized in vitro using protein-immobilized beads.\nRpb3 and Rpb5, the putative subunits of RNA polymerase II, associate each other to form binary complexes. These two subunits also bind to the two large subunits, Rpb1 and Rpb2, independently.","authors":"Miyao T, Yasui K, Sakurai H, Yamagishi M, Ishihama A","authors_abbrev":"Miyao T et al.","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_session_key":"a68731e606c7d316","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-12 06:29:32","canto_approved_date":"2023-12-11 08:31:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 06:29:24","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1442.10c","SPAC23G3.01","SPAC23C4.15","SPBC28F2.12"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-06-12"},{"uniquename":"PMID:18591258","title":"A yeast exosome cofactor, Mpp6, functions in RNA surveillance and in the degradation of noncoding RNA transcripts.","citation":"Mol Cell Biol 2008 Sep;28(17):5446-57","abstract":"A genome-wide screen for synthetic lethal (SL) interactions with loss of the nuclear exosome cofactors Rrp47/Lrp1 or Air1 identified 3'-->5' exonucleases, the THO complex required for mRNP assembly, and Ynr024w (Mpp6). SL interactions with mpp6Delta were confirmed for rrp47Delta and nuclear exosome component Rrp6. The results of bioinformatic analyses revealed homology between Mpp6 and a human exosome cofactor, underlining the high conservation of the RNA surveillance system. Mpp6 is an RNA binding protein that physically associates with the exosome and was localized throughout the nucleus. The results of functional analyses demonstrated roles for Mpp6 in the surveillance of both pre-rRNA and pre-mRNAs and in the degradation of \"cryptic\" noncoding RNAs (ncRNAs) derived from intergenic regions and the ribosomal DNA spacer heterochromatin. Strikingly, these ncRNAs are also targeted by other exosome cofactors, including Rrp47, the TRAMP complex (which includes Air1), and the Nrd1/Nab3 complex, and are degraded by both Rrp6 and the core exosome. Heterochromatic transcripts and other ncRNAs are characterized by very rapid degradation, and we predict that functional redundancy is an important feature of ncRNA metabolism.","doi":"10.1128/MCB.00463-08","authors":"Milligan L, Decourty L, Saveanu C, Rappsilber J, Ceulemans H, Jacquier A, Tollervey D","authors_abbrev":"Milligan L et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-07-02","publication_year":"2008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YNR024W","SPACUNK4.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9559555","title":"Nucleotide sequence of the Schizosaccharomyces pombe lys1+ gene and similarities of the lys1+ protein to peptide antibiotic synthetases.","citation":"Yeast 1998 Mar 30;14(5):479-84","abstract":"The 4.2 kbp lys1+ gene of Schizosaccharomyces pombe encoding the large subunit of alpha-aminoadipate reductase (EC1.2.1.31), an enzyme specific to lysine synthesis in higher fungi, was completely sequenced at the nucleotide level from pLYS1H. The S. pombe lys1+ gene product consists of 1415 amino acid residues and has a putative molecular weight of 155.8 kDa. The encoded protein converts alpha-aminoadipic acid to alpha-aminoadipate-delta-semialdehyde by an ATP-mediated adenylation. Analysis of the sequence showed that the putative protein encoded by lys1+ shares strong homology with the peptide antibiotic synthetases which also use in adenylation step.","authors":"Bhattacherjee V, Bhattacharjee JK","authors_abbrev":"Bhattacherjee V et al.","pubmed_publication_date":"30 Mar 1998","pubmed_entrez_date":"1998-04-29","publication_year":"1998","canto_session_key":"7c378db0fa1db19e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-10-28 16:33:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-28 16:33:11","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP7G5.04c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-10-28"},{"uniquename":"PMID:16464860","title":"Methylglyoxal as a signal initiator for activation of the stress-activated protein kinase cascade in the fission yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 2006 Apr 07;281(14):9086-92","abstract":"Methylglyoxal (MG) is a typical 2-oxoaldehyde derived from glycolysis. We have recently found that MG activates transcription factors such as Yap1 and Msn2, and triggers a Hog1 mitogen-activated protein kinase cascade in Saccharomyces cerevisiae. Regarding the activation of Hog1 by MG, we found that Sln1, an osmosensor possessing histidine kinase activity, functions as a sensor of MG (Maeta, K., Izawa, S., and Inoue, Y. (2005) J. Biol. Chem. 280, 253-260). To gain further insight into the role of MG as a signal initiator, here we analyze the response of Schizosaccharomyces pombe to extracellular MG. Spc1, a stress-activated protein kinase (SAPK), was phosphorylated following the treatment with MG. No phosphorylation was observed in a wis1Delta mutant. The His-to-Asp phosphorelay system consisting of three histidine kinases (Phk1, Phk2, and Phk3), a phosphorelay protein (Spy1), and a response regulator (Mcs4) exists upstream of the Spc1-SAPK pathway. The phosphorylation of Spc1 following MG treatment was observed in phk1Deltaphk2Deltaphk3Delta and spy1Delta cells, but not in mcs4Delta cells. These results suggest that S. pombe has an alternative module(s) that directs the MG signal to the SAPK pathway via Mcs4. Additionally, we found that the transcription factor Pap1 is concentrated in the nucleus in response to MG, independent of the Spc1-SAPK pathway.","authors":"Takatsume Y, Izawa S, Inoue Y","authors_abbrev":"Takatsume Y et al.","pubmed_publication_date":"07 Apr 2006","pubmed_entrez_date":"2006-02-09","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11711540","title":"The Ded1 DEAD box helicase interacts with Chk1 and Cdc2.","citation":"J Biol Chem 2002 Jan 25;277(4):2637-43","abstract":"Ded1 is a fission yeast DEAD box protein involved in translation. We isolated Ded1 in a screen for multi-copy suppressors of a cold-sensitive, loss-of-function mutant of the cyclin-dependent kinase Cdc2. The checkpoint protein kinase Chk1, required for cell cycle arrest in response to DNA damage, was also isolated in this screen. Ded1 interacts with Chk1 in a two-hybrid screen, and this physical interaction can be recapitulated in Schizosaccharomyces pombe. The Ded1 polypeptide is modified in response to heat shock and depletion of carbon source. These two stressors appear to cause different modifications. Thus, the Ded1 protein appears to respond to particular types of cellular stress and may influence the activity of Cdc2 as a result.","authors":"Liu HY, Nefsky BS, Walworth NC","authors_abbrev":"Liu HY et al.","pubmed_publication_date":"25 Jan 2002","pubmed_entrez_date":"2001-11-17","publication_year":"2002","canto_session_key":"7240ad7f25f52209","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-07-29 14:48:58","canto_approved_date":"2022-02-25 05:41:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-29 14:48:51","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.14","SPCC18B5.03","SPCC1259.13","SPBC11B10.09","SPCC1795.11","SPBC582.03"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-07-29"},{"uniquename":"PMID:10503004","title":"[Fission yeast mutants defective in sisiter chromatid separation].","citation":"Tanpakushitsu Kakusan Koso 1999 Sep;44(12 Suppl):1703-10","abstract":"","authors":"Nakaseko Y, Yanagida M","authors_abbrev":"Nakaseko Y et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-09-30","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29386379","title":"Resolving single-actin filaments within the contractile ring of fission yeast.","citation":"Proc Natl Acad Sci U S A 2018 Feb 13;115(7):1403-1405","abstract":"","doi":"10.1073/pnas.1722624115","authors":"Laplante C","authors_abbrev":"Laplante C","pubmed_publication_date":"13 Feb 2018","pubmed_entrez_date":"2018-02-02","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-02-03 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:732808","title":"Characterisation of ribosomes from drug resistant strains of Schizosaccharomyces pombe in a poly U directed cell free protein synthesising system.","citation":"Mol Gen Genet 1978 Nov 29;167(2):217-25","abstract":"Mutants of Schizosaccharomyces pombe were isolated as resistant either to trichodermin or to anisomycin. Growth tests showed that the majority of mutants isolated were cross resistant to both drugs and also to cycloheximide. A limited genetic analysis showed that mutants at least four loci, tri3, tri4, ani1 and ani2, had this phenotype as was also the case for mutants at three cycloheximide resistant loci, cyh2, cyh3 and cyh4 reported previously (Ibrahim and Coddington, 1976). Allelism tests showed that the tri3, ani2 and cyh4 strains were allelic. A mutant at another trichodermin resistant locus, tri5, was cross resistant to anisomycin but sensitive to cycloheximide. Ribosomes from wild type and selected strains were analysed in a poly U directed cell free protein synthesising system. Three strains, cyh1-C7, ani1-F1 and tri-N15 (probably a tri5 allele) possessed ribosomes which were more resistant than the wild type to the drugs used in their isolation. In each case the site of the resistance was in the 60S subunit. Ribosomes from the cyh2, cyh3 and cyh4 strains were as sensitive to cycloheximide as those from wild type.","authors":"Berry CH, Ibrahim MA, Coddington A","authors_abbrev":"Berry CH et al.","pubmed_publication_date":"29 Nov 1978","pubmed_entrez_date":"1978-11-29","publication_year":"1978","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15755919","title":"Hsp90 protein in fission yeast Swo1p and UCS protein Rng3p facilitate myosin II assembly and function.","citation":"Eukaryot Cell 2005 Mar;4(3):567-76","abstract":"The F-actin-based molecular motor myosin II is involved in a variety of cellular processes such as muscle contraction, cell motility, and cytokinesis. In recent years, a family of myosin II-specific cochaperones of the UCS family has been identified from work with yeasts, fungi, worms, and humans. Biochemical analyses have shown that a complex of Hsp90 and the Caenorhabditis elegans UCS domain protein UNC-45 prevent myosin head aggregation, thereby allowing it to assume a proper structure. Here we demonstrate that a temperature-sensitive mutant of the fission yeast Hsp90 (Swo1p), swo1-w1, is defective in actomyosin ring assembly at the restrictive temperature. Two alleles of swo1, swo1-w1 and swo1-26, showed synthetic lethality with a specific mutant allele of the fission yeast type II myosin head, myo2-E1, but not with two other mutant alleles of myo2 or with mutations affecting 14 other genes important for cytokinesis. swo1-w1 also showed a strong genetic interaction with rng3-65, a gene encoding a mutation in the fission yeast UCS domain protein Rng3p, which has previously been shown to be important for myosin II assembly. A similar deleterious effect was found when myo2-E1, swo1-w1, and rng3-65 were pharmacologically treated with geldanamycin to partially inhibit Hsp90 function. Interestingly, Swo1p-green fluorescent protein is detected at the improperly assembled actomyosin rings in myo2-E1 but not in a wild-type strain. Yeast two-hybrid and coimmunoprecipitation analyses verified interactions between Rng3p and the myosin head domain as well as interactions between Rng3p and Swo1p. Our analyses of Myo2p, Swo1p, and the UCS domain protein Rng3p establish that Swo1p and Rng3p collaborate in vivo to modulate myosin II function.","authors":"Mishra M, D'souza VM, Chang KC, Huang Y, Balasubramanian MK","authors_abbrev":"Mishra M et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-03-10","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.04c","SPCC613.04c","SPCC645.05c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:16814252","title":"The Rad9 protein enhances survival and promotes DNA repair following exposure to ionizing radiation.","citation":"Biochem Biophys Res Commun 2006 Aug 18;347(1):232-7","abstract":"Following DNA damage cells initiate cell cycle checkpoints to allow time to repair sustained lesions. Rad9, Rad1, and Hus1 proteins form a toroidal complex, termed the 9-1-1 complex, that is involved in checkpoint signaling. 9-1-1 shares high structural similarity to the DNA replication protein proliferating cell nuclear antigen (PCNA) and 9-1-1 has been shown in vitro to stimulate steps of the repair process known as long patch base excision repair. Using a system that allows conditional repression of the Rad9 protein in human cell culture, we show that Rad9, and by extension, the 9-1-1 complex, enhances cell survival, is required for efficient exit from G2-phase arrest, and stimulates the repair of damaged DNA following ionizing radiation. These data provide in vivo evidence that the human 9-1-1 complex participates in DNA repair in addition to its previously described role in DNA damage sensing.","authors":"Brandt PD, Helt CE, Keng PC, Bambara RA","authors_abbrev":"Brandt PD et al.","pubmed_publication_date":"18 Aug 2006","pubmed_entrez_date":"2006-07-04","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11513869","title":"mik1(+) G1-S transcription regulates mitotic entry in fission yeast.","citation":"FEBS Lett 2001 Aug 17;503(2-3):131-4","abstract":"In the fission yeast Schizosaccharomyces pombe Mik1p, in combination with Wee1p, is an important inhibitor of mitosis through direct phosphorylation of Cdc2p. Here we present the observation that mik1(+) is transcribed during G1- and S-phase in normally dividing cells. mik1(+) transcription is regulated by the MCB-DSC1 system, which controls expression of other genes at the G1-S interval. mik1(+) is shown to be an important target of MCB-DSC1 as it is epistatic for the mitotic delay phenotype displayed in cdc10-C4 cells, which are mutated in a component of DSC1. The mitotic delay in cdc10-C4 cells is bypassed by cdc2-1w, suggesting that mik1(+) acts directly on cdc2(+), with no checkpoint function involved. Thus, mik1(+) represents a new type of MCB-DSC1 regulated gene in fission yeast, whose gene product is exclusively expressed during G1- and S-phase to prevent premature mitosis during this cell cycle stage.","authors":"Ng SS, Anderson M, White S, McInerny CJ","authors_abbrev":"Ng SS et al.","pubmed_publication_date":"17 Aug 2001","pubmed_entrez_date":"2001-08-22","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC11B10.09","SPBC660.14"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:7941744","title":"Chemical synthesis of the M-factor mating pheromone from Schizosaccharomyces pombe.","citation":"Yeast 1994 May;10(5):595-601","abstract":"Conjugation in the fission yeast Schizosaccharomyces pombe is controlled by the reciprocal action of mating pheromones. We recently showed that M-factor, the pheromone released by cells of the cellular mating type Minus, is a nonapeptide in which the C-terminal cysteine residue is carboxyl-methylated and S-alkylated, probably with a farnesyl residue (Davey, 1992): Tyr-Thr-Pro-Lys-Val-Pro-Tyr-Met-Cys(S-farnesyl)- OCH3. Here we describe the chemical synthesis of this modified peptide and show that it exhibits all of the properties of the native pheromone. These results confirm the structure of the M-factor while the production of relatively large amounts of pure pheromone will be invaluable for studying the mating response in this yeast.","authors":"Wang SH, Xue CB, Nielsen O, Davey J, Naider F","authors_abbrev":"Wang SH et al.","pubmed_publication_date":"May 1994","pubmed_entrez_date":"1994-05-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34343465","title":"Cosegregation of asymmetric features during cell division.","citation":"Open Biol 2021 Aug;11(8):210116","abstract":"Cellular asymmetry plays a major role in the ageing and evolution of multicellular organisms. However, it remains unknown how the cell distinguishes 'old' from 'new' and whether asymmetry is an attribute of highly specialized cells or a feature inherent in all cells. Here, we investigate the segregation of three asymmetric features: old and new DNA, the spindle pole body (SPB, the centrosome analogue) and the old and new cell ends, using a simple unicellular eukaryote,  Schizosaccharomyces pombe . To our knowledge, this is the first study exploring three asymmetric features in the same cells. We show that of the three chromosomes of  S. pombe , chromosome I containing the new parental strand, preferentially segregated to the cells inheriting the old cell end. Furthermore, the new SPB also preferentially segregated to the cells inheriting the old end. Our results suggest that the ability to distinguish 'old' from 'new' and to segregate DNA asymmetrically are inherent features even in simple unicellular eukaryotes.","doi":"10.1098/rsob.210116","authors":"Anda S, Boye E, Schink KO, Grallert B","authors_abbrev":"Anda S et al.","pubmed_publication_date":"Aug 2021","pubmed_entrez_date":"2021-08-03","publication_year":"2021","canto_session_key":"6adaec221020f319","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-08-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12135745","title":"Cmk2, a novel serine/threonine kinase in fission yeast.","citation":"FEBS Lett 2002 Jul 31;524(1-3):79-86","abstract":"The cmk2 gene of Schizosaccharomyces pombe encodes a 504 amino acid protein kinase with sequence homology with the calmodulin-dependent protein kinase family. The cmk2(+) gene is not essential for cell viability but overexpression of cmk2(+) blocks the cell cycle at G2 phase and this inhibition is cdc2-dependent. The Cmk2 is a cytoplasmic protein expressed in a cell cycle-dependent manner, peaking at the G1/S boundary. Overexpression of Cmk2 suppresses fission yeast DNA replication checkpoint defects but not DNA damage checkpoint defects, suggesting that the G2 cell cycle arrest mediated by high levels of Cmk2 provides sufficient time to correct DNA replication alterations.","authors":"Alemany V, Sanchez-Piris M, Bachs O, Aligue R","authors_abbrev":"Alemany V et al.","pubmed_publication_date":"31 Jul 2002","pubmed_entrez_date":"2002-07-24","publication_year":"2002","canto_session_key":"091362c584b40ce2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-04 15:27:52","canto_approved_date":"2022-11-25 20:53:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-18 10:03:47","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC1952.07","SPBC11B10.09","SPAC23A1.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-08-04"},{"uniquename":"PMID:18160711","title":"Recombination-based telomere maintenance is dependent on Tel1-MRN and Rap1 and inhibited by telomerase, Taz1, and Ku in fission yeast.","citation":"Mol Cell Biol 2008 Mar;28(5):1443-55","abstract":"Fission yeast cells survive loss of the telomerase catalytic subunit Trt1 (TERT) through recombination-based telomere maintenance or through chromosome circularization. Although trt1Delta survivors with linear chromosomes can be obtained, they often spontaneously circularize their chromosomes. Therefore, it was difficult to establish genetic requirements for telomerase-independent telomere maintenance. In contrast, when the telomere-binding protein Taz1 is also deleted, taz1Delta trt1Delta cells are able to stably maintain telomeres. Thus, taz1Delta trt1Delta cells can serve as a valuable tool in understanding the regulation of telomerase-independent telomere maintenance. In this study, we show that the checkpoint kinase Tel1 (ATM) and the DNA repair complex Rad32-Rad50-Nbs1 (MRN) are required for telomere maintenance in taz1Delta trt1Delta cells. Surprisingly, Rap1 is also essential for telomere maintenance in taz1Delta trt1Delta cells, even though recruitment of Rap1 to telomeres depends on Taz1. Expression of catalytically inactive Trt1 can efficiently inhibit recombination-based telomere maintenance, but the inhibition requires both Est1 and Ku70. While Est1 is essential for recruitment of Trt1 to telomeres, Ku70 is dispensable. Thus, we conclude that Taz1, TERT-Est1, and Ku70-Ku80 prevent telomere recombination, whereas MRN-Tel1 and Rap1 promote recombination-based telomere maintenance. Evolutionarily conserved proteins in higher eukaryotic cells might similarly contribute to telomere recombination.","authors":"Subramanian L, Moser BA, Nakamura TM","authors_abbrev":"Subramanian L et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2007-12-28","publication_year":"2008","canto_session_key":"89f6dc6bc010963b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-29 15:05:12","canto_approved_date":"2022-05-18 12:19:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-05 10:13:30","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":50,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.02c","SPBC1778.02","SPBC216.05","SPAC30D11.10","SPAC16A10.07c","SPBC29A3.14c","SPAC1556.01c","SPBC2D10.13","SPAC13C5.07","SPCC23B6.03c","SPBC6B1.09c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2016-06-29"},{"uniquename":"PMID:18364227","title":"Cytokinesis: catch and drag.","citation":"Curr Biol 2008 Mar 25;18(6):R247-50","abstract":"Recent studies of actomyosin-ring assembly in fission yeast have suggested that an intricate web of membrane-bound nodes containing myosin and the actin nucleator formin is pulled together into a tight ring through a 'search-and-capture' mechanism.","doi":"10.1016/j.cub.2008.01.029","authors":"Mishra M, Oliferenko S","authors_abbrev":"Mishra M et al.","pubmed_publication_date":"25 Mar 2008","pubmed_entrez_date":"2008-03-28","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9078365","title":"The regulatory subunits of fission yeast protein phosphatase 2A (PP2A) affect cell morphogenesis, cell wall synthesis and cytokinesis.","citation":"Genes Cells 1996 Jan;1(1):29-45","abstract":"Protein phosphatase 2A (PP2A) holoenzymes have a trimeric structure, consisting of a catalytic subunit C and two regulatory subunits A (PR65) and B (PR55). In fission yeast the C subunits, being 80% identical to their mammalian counterparts, are essential for viability and negatively regulate the entry into mitosis. Genetic analyses in budding yeast and Drosophila show that the regulatory subunits are implicated in chromosome segregation, cell morphogenesis and/or cytokinesis.\nWe isolated fission yeast genes paa1+ and pab1+ encoding the regulatory subunits PR65 and PR55, respectively. Gene disruption showed that the paa1+ gene was essential for viability while pab1+ was not required at 26-33 degrees C. Microtubule and actin distributions were anomalous in gene disrupted delta paa1 cells which were incapable of forming a polarized cell shape. Gene disrupted delta pab1 cells were pear- or round-shaped, and lost the polar distributions of actin and microtubules. In addition, delta pab1 cells were defective in cell wall synthesis and sporulation at permissive temperatures. At restrictive temperatures, delta pab1 cells showed an osmoremedial temperature-sensitive phenotype and delayed in cytokinesis. However, chromosome segregation was normal.\nFission yeast PP2A regulatory subunit plays a critical role in cell morphogenesis, probably through regulation of the cytoskeletal network and cell wall synthesis.","authors":"Kinoshita K, Nemoto T, Nabeshima K, Kondoh H, Niwa H, Yanagida M","authors_abbrev":"Kinoshita K et al.","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"91d681458c26c2f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 13:24:08","canto_approved_date":"2024-06-28 11:07:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-10-11 15:20:57","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":27,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC227.07c","SPBC16H5.07c","SPAP8A3.09c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-09-17"},{"uniquename":"EMBL:AU009530","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008744","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7338524","title":"Cadmium-binding peptide induced in fission yeast, Schizosaccharomyces pombe.","citation":"J Biochem 1981 Nov;90(5):1561-4","abstract":"When S. pombe is cultured in a medium containing a high concentration of CdCl2 (1 mM), it grows for over 20 h accumulating Cd2+ in the cells. Simultaneously, Cd-binding peptides (Cd-BP1 and -BP2) are synthesized, and accumulated depending on the time after addition of Cd2+ to the culture medium. Apparent molecular weights of Cd-BP1 and -BP2 are 4,000 and 1,800, respectively. Both Cd-BPs are composed of common unit peptides, confirmed by chemical and physicochemical analyses.","authors":"Murasugi A, Wada C, Hayashi Y","authors_abbrev":"Murasugi A et al.","pubmed_publication_date":"Nov 1981","pubmed_entrez_date":"1981-11-01","publication_year":"1981","canto_session_key":"b006cfdf62673d81","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-17 16:08:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-17 16:08:08","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-01-17"},{"uniquename":"PMID:35128479","title":"Tandem affinity purification protocol for isolation of protein complexes from  Schizosaccharomyces pombe .","citation":"STAR Protoc 2022 Mar 18;3(1):101137","abstract":"Many cellular processes require the activities of complex molecular machines composed of several protein subunits. Insights into these systems can be gained by isolation of protein complexes followed by  in vitro  analyses determining the identity, posttranslational modifications, and interactions among proteins. Here, we present a protocol for tandem affinity purification (TAP) of protein complexes from the fission yeast  Schizosaccharomyces pombe . The protocol employs cells expressing C-terminally TAP-tagged proteins and is suitable for the analysis of purified proteins by mass spectrometry. For complete information on the use and execution of this protocol, please refer to Cipakova et al. (2019).","doi":"10.1016/j.xpro.2022.101137","authors":"Cipak L, Selicky T, Jurcik J, Cipakova I, Osadska M, Lukacova V, Barath P, Gregan J","authors_abbrev":"Cipak L et al.","pubmed_publication_date":"18 Mar 2022","pubmed_entrez_date":"2022-02-07","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-02-09 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8575018","title":"Two novel genes involved in the sexual development of Schizosaccharomyces pombe.","citation":"Curr Genet 1995 Oct;28(5):447-53","abstract":"We isolated two sterile mutants of Schizosaccharomyces pombe. One of them was mapped close to ste13 (8 cM). Since it turned out to be allelic with the hitherto unmapped ral2, its linkage with ste13 localizes ral2 on the right arm of chromosome II. The other mutant defines a novel class-I ste gene, ste15, closely linked to ste7 (4 cM) on chromosome I. ste15 is conjugation-specific and acts upstream of pat1 and ras1. During its genetic analysis, a phenotypic suppression of ste12-N9 was observed which was caused by mutations in the unlinked gene ssw1.","authors":"Molnar M, Sipiczki M","authors_abbrev":"Molnar M et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_session_key":"b79aef8fb079adc7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-24 14:34:09","canto_approved_date":"2022-04-13 10:07:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-24 14:34:02","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.09","SPBC21.05c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-10-24"},{"uniquename":"PMID:3329047","title":"Induction of yeast DNA ligase genes in exponential and stationary phase cultures in response to DNA damaging agents.","citation":"Curr Genet 1986;11(2):107-12","abstract":"UV-irradiation of stationary phase cells of Saccharomyces cerevisiae and Schizosaccharomyces pombe leads to a 9-fold and 90-fold increase in transcript levels from the respective DNA ligase genes CDC9 and CDC17, whereas exponential cells show only 3-fold and 2-fold increases. Induction of CDC9 after MMS treatment and gamma-irradiation was also observed by using a CDC9-lacZ translational fusion and assaying for beta-galactosidase. Surprisingly, irradiation of S. cerevisiae induces only a 50% increase in DNA ligase itself, probably reflecting the extremely high in vivo stability of the enzyme. The UV-induction of ligase may be part of a \"fail-safe\" mechanism which, together with the enzyme stability, ensures adequate supplies of this essential enzyme.","authors":"Johnson AL, Barker DG, Johnston LH","authors_abbrev":"Johnson AL et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_session_key":"3e3a72e72a40b881","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-30 11:11:41","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-30 11:11:29","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G8.01"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-09-30"},{"uniquename":"PMID:22622085","title":"Insights from a new tool for meiotic induction in fission yeast.","citation":"Cell Cycle 2012 Jun 01;11(11):2050","abstract":"","doi":"10.4161/cc.20537","authors":"Wu PY","authors_abbrev":"Wu PY","pubmed_publication_date":"01 Jun 2012","pubmed_entrez_date":"2012-05-25","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7929079","title":"Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance.","citation":"J Biol Chem 1994 Sep 30;269(39):24229-36","abstract":"The fungal metabolite brefeldin A (BFA) causes the inhibition of protein secretion and the disruption of the structure and function of the Golgi complex in mammalian cells. Here we show that BFA has identical effects in the fission yeast Schizosaccharomyces pombe which normally contains a Golgi complex of stacked cisternae similar to the Golgi complexes in animal cells. After treatment with BFA, secretion was inhibited, Golgi complexes disappeared, and there was an accumulation of endoplasmic reticulum. These results indicate that the effects of BFA in fungi are very similar to those in mammalian cells and provide direct evidence for an effect of BFA on Golgi morphology in fungi. Five spontaneous BFA-resistant mutants were isolated. Genetic analysis showed that the mutations conferring BFA resistance were dominant and in two separate linkage groups. One of the BFA-resistant mutations was found to be allelic to crm1, a gene affecting chromatin structure. All BFA-resistant mutants overexpressed a 20-kDa protein, and the corresponding gene obr1 was isolated and sequenced. However, obr1 overexpression was not sufficient to confer BFA resistance. Plasmids capable of conferring BFA resistance to wild type cells were isolated from libraries constructed from the two BFA-resistant mutants. These plasmids contain six different genes capable of conferring resistance when present in high copy. One of these genes encoded the transcription factor pap1, a homolog of the mammalian AP1 protein. The overexpression of pap1 probably confers BFA resistance indirectly by inducing expression of one or more other proteins. The isolation of several genes conferring BFA resistance suggests several mechanisms are involved.","authors":"Turi TG, Webster P, Rose JK","authors_abbrev":"Turi TG et al.","pubmed_publication_date":"30 Sep 1994","pubmed_entrez_date":"1994-09-30","publication_year":"1994","canto_session_key":"c8e3ef000434cbb6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-28 17:20:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-28 17:20:07","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC1805.17","SPAC3C7.14c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2013-10-28"},{"uniquename":"PMID:31048178","title":"Modeling of yeast thermal resistance and optimization of the pasteurization treatment applied to soft drinks.","citation":"Int J Food Microbiol 2019 Jul 16;301:1-8","abstract":"Yeast are usually responsible for spoilage of soft drinks and fruit beverages, because of the particular characteristics of these products (low pH, high C/N ratio). The microbial stability is guaranteed by thermal treatments. However, excessive heat treatments can affect food sensorial quality. In this work the thermal resistance of different yeasts strains (seven belonging to the species Saccharomyces cerevisiae and six belonging to the species Kluyveromyces marxianus, Zygosaccharomyces bisporus, Z. mellis, Z. rouxii, Schizosaccharomyces pombe and Saccharomycodes ludwigii) was assessed in a model system. The results showed non-linear death curves and a high variability also within the same species. The most resistant strain, belonging to the species S. cerevisiae, was chosen for further experiments in orange juice based industrial beverages: first, death curves were performed; then, the probability of beverage spoilage in relation to process parameters (initial inoculum, temperature, treatment time) was evaluated using a logistic regression model. Finally, a cross-validation was performed to investigate the predictive capability of the fitted model. Pasteurization in the soft drink industry is commonly applied according to parameters defined several decades ago, which does not consider the successive findings concerning microbial physiology and stress response, the process improvement and the more recent tools provided by predictive microbiology. In this perspective, this study can fill a gap in the literature on this subject, going to be a basis for optimizing thermal processes. In fact, the data obtained indicated an interesting possibility for food industry to better modulated (and even reduce) thermal treatments, with the aim to guarantee microbial stability while reducing thermal damage and energy costs.","doi":"10.1016/j.ijfoodmicro.2019.04.006","authors":"Montanari C, Tabanelli G, Zamagna I, Barbieri F, Gardini A, Ponzetto M, Redaelli E, Gardini F","authors_abbrev":"Montanari C et al.","pubmed_publication_date":"16 Jul 2019","pubmed_entrez_date":"2019-05-04","publication_year":"2019","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2019-05-04 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"TreeFam:TF314636","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC18E5.05c","HGNC:30617"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8273144","title":"Finishing the cell cycle: control of mitosis and cytokinesis in fission yeast.","citation":"Trends Genet 1993 Oct;9(10):333-5","abstract":"","authors":"Chang F, Nurse P","authors_abbrev":"Chang F et al.","pubmed_publication_date":"Oct 1993","pubmed_entrez_date":"1993-10-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8904333","title":"Malolactic fermentation by engineered Saccharomyces cerevisiae as compared with engineered Schizosaccharomyces pombe.","citation":"Yeast 1996 Mar 15;12(3):215-25","abstract":"The ability of yeast strains to perform both alcoholic and malolactic fermentation in winemaking was studied with a view to achieving a better control of malolactic fermentation in enology. The malolactic gene of Lactococcus lactis (mleS) was expressed in Saccharomyces cerevisiae and Schizosaccharomyces pombe. The heterologous protein is expressed at a high level in cell extracts of a S. cerevisiae strain expressing the gene mleS under the control of the alcohol dehydrogenase (ADH1) promoter on a multicopy plasmid. Malolactic enzyme specific activity is three times higher than in L. lactis extracts. Saccharomyces cerevisiae expressing the malolactic enzyme produces significant amounts of L-lactate during fermentation on glucose-rich medium in the presence of malic acid. Isotopic filiation was used to demonstrate that 75% of the L-lactate produced originates from endogenous L-malate and 25% from exogenous L-malate. Moreover, although a small amount of exogenous L-malate was degraded by S. cerevisiae transformed or not by mleS, all the exogenous degraded L-malate was converted into L-lactate via a malolactic reaction in the recombinant strain, providing evidence for very efficient competition of malolactic enzyme with the endogenous malic acid pathways. These results indicate that the sole limiting step for S. cerevisiae in achieving malolactic fermentation is in malate transport. This was confirmed using a different model, S. pombe, which efficiently degrades L-malate. Total malolactic fermentation was obtained in this strain, with most of the L-malate converted into L-lactate and CO2. Moreover, L-malate was used preferentially by the malolactic enzyme in this strain also.","authors":"Ansanay V, Dequin S, Camarasa C, Schaeffer V, Grivet JP, Blondin B, Salmon JM, Barre P","authors_abbrev":"Ansanay V et al.","pubmed_publication_date":"15 Mar 1996","pubmed_entrez_date":"1996-03-15","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17998404","title":"The size-wise nucleus: nuclear volume control in eukaryotes.","citation":"J Cell Biol 2007 Nov 19;179(4):583-4","abstract":"Eukaryotic cells have an \"awareness\" of their volume and organellar volumes, and maintain a nuclear size that is proportional to the total cell size. New studies in budding and fission yeast have examined the relationship between cell and nuclear volumes. It was found that the size of the nucleus remains proportional to cell size in a wide range of genetic backgrounds and growth conditions that alter cell volume and DNA content. Moreover, in multinucleated fission yeast cells, Neumann and Nurse (see p. 593 of this issue) found that the sizes of individual nuclei are controlled by the relative amount of cytoplasm surrounding each nucleus. These results highlight a role of the cytoplasm in nuclear size control.","authors":"Huber MD, Gerace L","authors_abbrev":"Huber MD et al.","pubmed_publication_date":"19 Nov 2007","pubmed_entrez_date":"2007-11-14","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14507429","title":"Uncoupling of the glucose growth defect and the deregulation of glycolysis in Saccharomyces cerevisiae Tps1 mutants expressing trehalose-6-phosphate-insensitive hexokinase from Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2003 Sep 30;1606(1-3):83-93","abstract":"In the yeast Saccharomyces cerevisiae inactivation of trehalose-6-phosphate (Tre6P) synthase (Tps1) encoded by the TPS1 gene causes a specific growth defect in the presence of glucose in the medium. The growth inhibition is associated with deregulation of the initial part of glycolysis. Sugar phosphates, especially fructose-1,6-bisphosphate (Fru1,6bisP), hyperaccumulate while the levels of ATP, Pi and downstream metabolites are rapidly depleted. This was suggested to be due to the absence of Tre6P inhibition on hexokinase. Here we show that overexpression of Tre6P (as well as glucose-6-phosphate (Glu6P))-insensitive hexokinase from Schizosaccharomyces pombe in a wild-type strain does not affect growth on glucose but still transiently enhances initial sugar phosphate accumulation. We have in addition replaced the three endogenous glucose kinases of S. cerevisiae by the Tre6P-insensitive hexokinase from S. pombe. High hexokinase activity was measured in cell extracts and growth on glucose was somewhat reduced compared to an S. cerevisiae wild-type strain but expression of the Tre6P-insensitive S. pombe hexokinase never caused the typical tps1Delta phenotype. Moreover, deletion of TPS1 in this strain expressing only the Tre6P-insensitive S. pombe hexokinase still resulted in a severe drop in growth capacity on glucose as well as sensitivity to millimolar glucose levels in the presence of excess galactose. In this case, poor growth on glucose was associated with reduced rather than enhanced glucose influx into glycolysis. Initial glucose transport was not affected. Apparently, deletion of TPS1 causes reduced activity of the S. pombe hexokinase in vivo. Our results show that Tre6P inhibition of hexokinase is not the major mechanism by which Tps1 controls the influx of glucose into glycolysis or the capacity to grow on glucose. In addition, they show that a Tre6P-insensitive hexokinase can still be controlled by Tps1 in vivo.","authors":"Bonini BM, Van Dijck P, Thevelein JM","authors_abbrev":"Bonini BM et al.","pubmed_publication_date":"30 Sep 2003","pubmed_entrez_date":"2003-09-26","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1834684","title":"Conserved structural motifs in cyclins identified by sequence analysis.","citation":"J Cell Sci 1991 Jul;99 ( Pt 3):669-74","abstract":"Cyclins, as regulatory subunits of the ubiquitous p34cdc2 protein kinase, act as key controlling elements of the eukaryotic cell cycle. We have examined published sequences of A- and B-type cyclins for both amino acid and secondary structure homologies. In particular, we sought regions of homology outside the recognised area of sequence conservation known as the \"cyclin box', as well as conserved features predicted to lie at the protein surface. Our analysis demonstrates the existence of a number of islands of homology outside the cyclin box, and indicates candidate residues for phosphorylation. One of these, a motif containing the amino acids SPXXXE/D is also present in fission yeast p13suc1, another protein known to interact with p34cdc2. This motif may define a possible p34cdc2 binding or phosphorylation site. A database search revealed that the CDC25 and SCD25 genes of the budding yeast Saccharomyces cerevisiae also contain some of the newly identified motifs, perhaps indicating a common regulatory or degradation pathway.","authors":"Nugent JH, Alfa CE, Young T, Hyams JS","authors_abbrev":"Nugent JH et al.","pubmed_publication_date":"Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_session_key":"c839fb2a597cde76","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-09 15:38:24","canto_approved_date":"2019-01-09 15:38:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-09 15:38:17","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-09"},{"uniquename":"PMID:29925630","title":"A transcription factor primes the condensin pump.","citation":"J Cell Biol 2018 Jul 02;217(7):2233-2234","abstract":"Chromosome condensation is regulated by the condensin complex but whether this process is subject to transcriptional control is poorly understood. In this issue, Schiklenk et al. (2018.  J. Cell Biol.  https://doi.org/10.1083/jcb.201711097) reveal that the transcription factor Zas1 mediates timely chromosome condensation and promotes transcription of several genes in  Saccharomyces pombe , including the condensin subunit Cnd1.","doi":"10.1083/jcb.201806043","authors":"Gerton JL","authors_abbrev":"Gerton JL","pubmed_publication_date":"02 Jul 2018","pubmed_entrez_date":"2018-06-22","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-06-23 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24609083","title":"Circular RNA is expressed across the eukaryotic tree of life.","citation":"PLoS One 2014;9(6):e90859","abstract":"An unexpectedly large fraction of genes in metazoans (human, mouse, zebrafish, worm, fruit fly) express high levels of circularized RNAs containing canonical exons. Here we report that circular RNA isoforms are found in diverse species whose most recent common ancestor existed more than one billion years ago: fungi (Schizosaccharomyces pombe and Saccharomyces cerevisiae), a plant (Arabidopsis thaliana), and protists (Plasmodium falciparum and Dictyostelium discoideum). For all species studied to date, including those in this report, only a small fraction of the theoretically possible circular RNA isoforms from a given gene are actually observed. Unlike metazoans, Arabidopsis, D. discoideum, P. falciparum, S. cerevisiae, and S. pombe have very short introns (∼ 100 nucleotides or shorter), yet they still produce circular RNAs. A minority of genes in S. pombe and P. falciparum have documented examples of canonical alternative splicing, making it unlikely that all circular RNAs are by-products of alternative splicing or 'piggyback' on signals used in alternative RNA processing. In S. pombe, the relative abundance of circular to linear transcript isoforms changed in a gene-specific pattern during nitrogen starvation. Circular RNA may be an ancient, conserved feature of eukaryotic gene expression programs.","doi":"10.1371/journal.pone.0090859","authors":"Wang PL, Bao Y, Yee MC, Barrett SP, Hogan GJ, Olsen MN, Dinneny JR, Brown PO, Salzman J","authors_abbrev":"Wang PL et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-03-11","publication_year":"2014","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36052670","title":"Actin turnover protects the cytokinetic contractile ring from structural instability.","citation":"J Cell Sci 2023 Mar 01;136(5)","abstract":"In common with other actomyosin contractile cellular machineries, actin turnover is required for normal function of the cytokinetic contractile ring. Cofilin is an actin-binding protein contributing to turnover by severing actin filaments, required for cytokinesis by many organisms. In fission yeast cofilin mutants, contractile rings suffer bridging instabilities in which segments of the ring peel away from the plasma membrane, forming straight bridges whose ends remain attached to the membrane. The origin of bridging instability is unclear. Here, we used molecularly explicit simulations of contractile rings to examine the role of cofilin. Simulations reproduced the experimentally observed cycles of bridging and reassembly during constriction, and the occurrence of bridging in ring segments with low density of the myosin II protein Myo2. The lack of cofilin severing produced ∼2-fold longer filaments and, consequently, ∼2-fold higher ring tensions. Simulations identified bridging as originating in the boosted ring tension, which increased centripetal forces that detached actin from Myo2, which was anchoring actin to the membrane. Thus, cofilin serves a critical role in cytokinesis by providing protection from bridging, the principal structural threat to contractile rings.","doi":"10.1242/jcs.259969","authors":"McDargh Z, Zhu T, Zhu H, O'Shaughnessy B","authors_abbrev":"McDargh Z et al.","pubmed_publication_date":"01 Mar 2023","pubmed_entrez_date":"2022-09-02","publication_year":"2023","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-09-04 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9804990","title":"Cloning and characterization of two genes encoding dihydroxyacetone kinase from Schizosaccharomyces pombe IFO 0354.","citation":"Biochim Biophys Acta 1998 Nov 08;1442(2-3):361-8","abstract":"We report the cloning and characterization of two genes encoding dihydroxyacetone kinase (EC 2.7.1.29), SpDAK1 and SpDAK2, from Schizosaccharomyces pombe IFO 0354. The open reading frames of both genes encode 591 amino acids and have Mrs of 62158 and 62170, respectively. Both predicted amino acid sequences exhibited a high identity to each other (99.8%) and relatively high identities (30% to 76%) to other putative dihydroxyacetone kinase gene products. A Western blot analysis showed that these enzymes are induced by glycerol and repressed by glucose. A genomic Southern blot analysis indicated the presence of SpDAK1 and the absence of SpDAK2 in a standard laboratory strain, S. pombe 972h-.","authors":"Kimura T, Takahashi M, Yoshihara K, Furuichi T, Suzuki K, Imai K, Karita S, Sakka K, Ohmiya K","authors_abbrev":"Kimura T et al.","pubmed_publication_date":"08 Nov 1998","pubmed_entrez_date":"1998-11-07","publication_year":"1998","canto_session_key":"b313f75129a151a6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-04-14 09:48:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-14 09:48:24","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC977.16c","SPAC22A12.11"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2015-04-14"},{"uniquename":"PMID:16467469","title":"Copper induces cytoplasmic retention of fission yeast transcription factor cuf1.","citation":"Eukaryot Cell 2006 Feb;5(2):277-92","abstract":"Copper homeostasis within the cell is established and preserved by different mechanisms. Changes in gene expression constitute a way of maintaining this homeostasis. In Schizosaccharomyces pombe, the Cuf1 transcription factor is critical for the activation of copper transport gene expression under conditions of copper starvation. However, in the presence of elevated intracellular levels of copper, the mechanism of Cuf1 inactivation to turn off gene expression remains unclear. In this study, we provide evidence that inactivation of copper transport gene expression by Cuf1 is achieved through a copper-dependent, cytosolic retention of Cuf1. We identify a minimal nuclear localization sequence (NLS) between amino acids 11 to 53 within the Cuf1 N terminus. Deletion of this region and specific mutation of the Lys13, Arg16, Arg19, Lys24, Arg28, Lys45, Arg47, Arg50, and Arg53 residues to alanine within this putative NLS is sufficient to abrogate nuclear targeting of Cuf1. Under conditions of copper starvation, Cuf1 resides in the nucleus. However, in the presence of excess copper as well as silver ions, Cuf1 is sequestered in the cytoplasm, a process which requires the putative copper binding motif, 328Cys-X-Cys-X3-Cys-X-Cys-X2-Cys-X2-His342 (designated C-rich), within the C-terminal region of Cuf1. Deletion of this region and mutation of the Cys residues within the C-rich motif result in constitutive nuclear localization of Cuf1. By coexpressing the Cuf1 N terminus with its C terminus in trans and by using a two-hybrid assay, we show that these domains physically interact with each other in a copper-dependent manner. We propose a model wherein copper induces conformational changes in Cuf1 that promote a physical interaction between the Cuf1 N terminus and the C-rich motif in the C terminus that masks the NLS. Cuf1 is thereby sequestered in the cytosol under conditions of copper excess, thereby extinguishing copper transport gene expression.","authors":"Beaudoin J, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-02-10","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31A2.11c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:8978690","title":"The Schizosaccharomyces pombe rad3 checkpoint gene.","citation":"EMBO J 1996 Dec 02;15(23):6641-51","abstract":"The rad3 gene of Schizosaccharomyces pombe is required for checkpoint pathways that respond to DNA damage and replication blocks. We report the complete rad3 gene sequence and show that rad3 is the homologue of Saccharomyces cerevisiae ESR1 (MEC1/SAD3) and Drosophila melanogaster mei-41 checkpoint genes. This establishes Rad3/Mec1 as the only conserved protein which is required for all the DNA structure checkpoints in both yeast model systems. Rad3 is an inessential member of the 'lipid kinase' subclass of kinases which includes the ATM protein defective in ataxia telangiectasia patients. Mutational analysis indicates that the kinase domain is required for Rad3 function, and immunoprecipitation of overexpressed Rad3 demonstrates an associated protein kinase activity. The previous observation that rad3 mutations can be rescued by a truncated clone lacking the kinase domain may be due to intragenic complementation. Consistent with this, biochemical data suggest that Rad3 exists in a complex containing multiple copies of Rad3. We have identified a novel human gene (ATR) whose product is closely related to Rad3/Esr1p/Mei-41. ATR can functionally complement esr1-1 radiation sensitivity in S. cerevisiae. Together, the structural conservation and functional complementation suggest strongly that the mechanisms underlying the DNA structure checkpoints are conserved throughout evolution.","authors":"Bentley NJ, Holtzman DA, Flaggs G, Keegan KS, DeMaggio A, Ford JC, Hoekstra M, Carr AM","authors_abbrev":"Bentley NJ et al.","pubmed_publication_date":"02 Dec 1996","pubmed_entrez_date":"1996-12-02","publication_year":"1996","canto_session_key":"c3b1db70e7d5847e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-06-01 14:38:43","canto_approved_date":"2022-03-17 18:20:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-01 14:38:35","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-01"},{"uniquename":"PMID:11861765","title":"Fission yeast Pds5 is required for accurate chromosome segregation and for survival after DNA damage or metaphase arrest.","citation":"J Cell Sci 2002 Feb 01;115(Pt 3):587-98","abstract":"Sister chromatid cohesion, which is established during the S phase of the eukaryotic cell cycle and persists until the onset of anaphase, is essential for the maintenance of genomic integrity. Cohesion requires the multi-protein complex cohesin, as well as a number of accessory proteins including Pds5/BIMD/Spo76. In the budding yeast Saccharomyces cerevisiae Pds5 is an essential protein that localises to chromosomes in a cohesin-dependent manner. Here we describe the characterisation in the fission yeast Schizosaccharomyces pombe of pds5(+), a novel, non-essential orthologue of S. cerevisiae PDS5. The S. pombe Pds5 protein was localised to punctate nuclear foci in a manner that was dependent on the Rad21 cohesin component. This, together with additional genetic evidence, points towards an involvement of S. pombe Pds5 in sister chromatid cohesion. S. pombe pds5 mutants were hypersensitive to DNA damage and to mitotic metaphase delay, but this sensitivity was apparently not due to precocious loss of sister chromatid cohesion. These cells also suffered increased spontaneous chromosome loss and meiotic defects and their viability was dependent on the spindle checkpoint protein Bub1. Thus, while S. pombe Pds5 has an important cohesin-related role, this differs significantly from that of the equivalent budding yeast protein.","authors":"Wang SW, Read RL, Norbury CJ","authors_abbrev":"Wang SW et al.","pubmed_publication_date":"01 Feb 2002","pubmed_entrez_date":"2002-02-28","publication_year":"2002","canto_session_key":"067e21ef8aa97ffd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-07-06 07:07:38","canto_approved_date":"2023-01-25 18:40:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-26 12:51:25","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":32,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPBC26H8.07c","SPCC338.17c","SPAC110.02","SPCC1322.12c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-07-06"},{"uniquename":"EMBL:SPD256","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9717240","title":"Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe.","citation":"Yeast 1998 Jul;14(10):943-51","abstract":"We describe a straightforward PCR-based approach to the deletion, tagging, and overexpression of genes in their normal chromosomal locations in the fission yeast Schizosaccharomyces pombe. Using this approach and the S. pombe ura4+ gene as a marker, nine genes were deleted with efficiencies of homologous integration ranging from 6 to 63%. We also constructed a series of plasmids containing the kanMX6 module, which allows selection of G418-resistant cells and thus provides a new heterologous marker for use in S. pombe. The modular nature of these constructs allows a small number of PCR primers to be used for a wide variety of gene manipulations, including deletion, overexpression (using the regulatable nmt1 promoter), C- or N-terminal protein tagging (with HA, Myc, GST, or GFP), and partial C- or N-terminal deletions with or without tagging. Nine genes were manipulated using these kanMX6 constructs as templates for PCR. The PCR primers included 60 to 80 bp of flanking sequences homologous to target sequences in the genome. Transformants were screened for homologous integration by PCR. In most cases, the efficiency of homologous integration was > or = 50%, and the lowest efficiency encountered was 17%. The methodology and constructs described here should greatly facilitate analysis of gene function in S. pombe.","authors":"Bähler J, Wu JQ, Longtine MS, Shah NG, McKenzie A, Steever AB, Wach A, Philippsen P, Pringle JR","authors_abbrev":"Bähler J et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-08-26","publication_year":"1998","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41826490","title":"Parallel but distinct adaptive routes in the budding and fission yeasts after 10,000 generations of experimental evolution.","citation":"Nat Ecol Evol 2026 Mar 13;","abstract":"Experimental evolution has been a useful tool for investigating long-term temporal evolutionary dynamics and molecular mechanisms underlying adaptation. However, extracting fundamental principles and predictive features of evolutionary outcomes from these datasets remains challenging. Here we sought to circumvent these challenges by comparing distant yeast species that share several evolutionary features but differ in evolutionary history and genome architecture, that is Saccharomyces cerevisiae and Schizosaccharomyces pombe. We evolved ten populations of the fission yeast for 10,000 generations in the same conditions as a pre-existing budding yeast dataset, allowing us to observe repeatable evolutionary outcomes within species but diverse molecular targets of adaptation across species. The most frequent route of adaptation was through changes in carbon flux metabolism, which was previously unseen in S. cerevisiae evolved populations, but similar evolutionary paths have been observed in wild populations. This suggests that parallelism is pervasive and that mechanisms of adaptation can be shared among closely related or distant species. Despite similar gene content and identical environments, recurrent adaptation across S. pombe populations involved different genes than in S. cerevisiae and was detectable mostly at the transcriptomic level. This indicates that trans-regulatory effects and contingency may contribute to differences in evolutionary outcomes between these species.","doi":"10.1038/s41559-026-03017-1","authors":"N'Guessan A, Wang V, Bakerlee CW, Belousova J, Brenna GY, Dillingham ME, Gopalakrishnan S, Goyal J, Gupta M, Holmes CM, Humphrey PT, Jagdish T, Jerison ER, Johnson MS, Kosheleva K, Lawrence KR, Min J, Moulana A, Pai SV, Phillips AM, Piper JC, Purkanti R, Rego-Costa A, Ruiz-Bedoya T, Trivellin C, McDonald MJ, Desai MM, Nguyen Ba AN","authors_abbrev":"N'Guessan A et al.","pubmed_publication_date":"13 Mar 2026","pubmed_entrez_date":"2026-03-14","publication_year":"2026","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2026-03-15 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9457874","title":"Std1, a gene involved in glucose transport in Schizosaccharomyces pombe.","citation":"J Bacteriol 1998 Feb;180(3):674-9","abstract":"A wild-type strain, Sp972 h-, of Schizosaccharomyces pombe was mutagenized with ethylmethanesulfonate (EMS), and 2-deoxyglucose (2-DOG)-resistant mutants were isolated. Out of 300 independent 2-DOG-resistant mutants, 2 failed to grow on glucose and fructose (mutants 3/8 and 3/23); however, their hexokinase activity was normal. They have been characterized as defective in their sugar transport properties, and the mutations have been designated as std1-8 and std1-23 (sugar transport defective). The mutations are allelic and segregate as part of a single gene when the mutants carrying them are crossed to a wild-type strain. We confirmed the transport deficiency of these mutants by [14C]glucose uptake. They also fail to grow on other monosaccharides, such as fructose, mannose, and xylulose, as well as disaccharides, such as sucrose and maltose, unlike the wild-type strain. Lack of growth of the glucose transport-deficient mutants on maltose revealed the extracellular breakdown of maltose in S. pombe, unlike in Saccharomyces cerevisiae. Both of the mutants are unable to grow on low concentrations of glucose (10 to 20 mM), while one of them, 3/23, grows on high concentrations (50 to 100 mM) as if altered in its affinity for glucose. This mutant (3/23) shows a lag period of 12 to 18 h when grown on high concentrations of glucose. The lag disappears when the culture is transferred from the log phase of its growth on high concentrations. These mutants complement phenotypically similar sugar transport mutants (YGS4 and YGS5) reported earlier by Milbradt and Hoefer (Microbiology 140:2617-2623, 1994), and the clone complementing YGS4 and YGS5 was identified as the only glucose transporter in fission yeast having 12 transmembrane domains. These mutants also demonstrate two other defects: lack of induction and repression of shunt pathway enzymes and defective mating.","authors":"Mehta SV, Patil VB, Velmurugan S, Lobo Z, Maitra PK","authors_abbrev":"Mehta SV et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-02-11","publication_year":"1998","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7969124","title":"The Srp54 GTPase is essential for protein export in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1994 Dec;14(12):7839-54","abstract":"Signal recognition particle (SRP) is a cytoplasmic ribonucleoprotein required for targeting a subset of presecretory proteins to the endoplasmic reticulum (ER) membrane. Here we report the results of a series of experiments to define the function of the Schizosaccharomyces pombe homolog of the 54-kDa subunit of mammalian SRP. One-step gene disruption reveals that the Srp54 protein, like SRP RNA, is essential for viability in S. pombe. Precursor to the secretory protein acid phosphatase accumulates in cells in which Srp54 synthesis has been repressed under the control of a regulated promoter, indicating that S. pombe SRP functions in protein targeting. In common with other Srp54 homologs, the S. pombe protein has a modular structure consisting of an amino-terminal G (GTPase) domain and a carboxyl-terminal M (methionine-rich) domain. We have analyzed the effects of 17 site-specific mutations designed to alter the function of each of the four GTPase consensus motifs individually. Several alleles, including some with relatively conservative amino acid substitutions, confer lethal or conditional phenotypes, indicating that GTP binding and hydrolysis are critical to the in vivo role of the protein. Two mutations (R to L at position 194 [R194L] and R194H) which were designed, by analogy to oncogenic mutations in rats, to dramatically decrease the catalytic rate and one (T248N) predicted to alter nucleotide binding specificity produce proteins that are unable to support growth at 18 degrees C. Consistent with its design, the R194L mutant hydrolyzes GTP at a reduced rate relative to wild-type Srp54 in enzymatic assays on immunoprecipitated proteins. In strains that also contain wild-type srp54, this mutant protein, as well as others designed to be locked in a GTP-bound conformation, exhibits temperature-dependent dominant inhibitory effects on growth, while a mutant predicted to be GDP locked does not interfere with the function of the wild-type protein. These results form the basis of a simple model for the role of GTP hydrolysis by Srp54 during the SRP cycle.","authors":"Althoff SM, Stevens SW, Wise JA","authors_abbrev":"Althoff SM et al.","pubmed_publication_date":"Dec 1994","pubmed_entrez_date":"1994-12-01","publication_year":"1994","canto_session_key":"1c5c00db9eb607a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-08-18 14:21:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-16 13:36:59","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_7969124_phaf.tsv"}],"genes":["SPBP4G3.02","SPCC188.06c","SPAC22A12.15c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2014-06-16"},{"uniquename":"PMID:2004705","title":"Genetic and molecular analysis of cdr1/nim1 in Schizosaccharomyces pombe.","citation":"Genetics 1991 Feb;127(2):309-18","abstract":"The cdr1 gene in Schizosaccharomyces pombe was identified as a mutation affecting the nutritional responsiveness of the mitotic size control. cdr1 alleles have been further analyzed for genetic interactions with elements of the mitotic control pathway and cloned by plasmid rescue of a conditional lethal cdr1-76 cdc25-22 double mutant. These analyses show that the cdr1 gene is allelic to nim1, a gene identified as a high copy number plasmid suppressor of the mitotic control gene, cdc25. The gene structure for cdr1 differs from the described nim1 gene in the carboxyl-terminal portion of the gene. The published nim1 sequence encoded a product of predicted Mr 45,000, and included 356 amino acids from the amino-terminal region of the gene and 14 amino acids from a noncontiguous carboxyl-terminal fragment. The cdr1 sequence includes an additional 237 amino acids of the contiguous fragment and encodes a product of predicted Mr 67,000. The sequence shows a high level of identity with protein kinases over the amino-terminal catalytic domain, and limited identity with yeast protein kinases SNF1, KIN2 and KIN1 over part of the carboxyl-terminal domain. The effect of overexpression of the full length gene has been examined in various genetic backgrounds. These data show that the full length gene product is required to give a normal cell cycle response to nitrogen starvation. A detailed examination of the genetic interaction of cdr1 mutants with various mutants of mitotic control genes (cdc2, cdc25, wee1, cdc13) demonstrated strong interactions with cdc25, some cdc2 alleles, and with cdc13-117. Overall, the results are interpretable within the framework of the existing model of cdr1/nim1 action in mitotic control, i.e., cdr1 functions upstream of wee1 to relieve mitotic inhibition.","authors":"Feilotter H, Nurse P, Young PG","authors_abbrev":"Feilotter H et al.","pubmed_publication_date":"Feb 1991","pubmed_entrez_date":"1991-02-01","publication_year":"1991","canto_session_key":"60b1b7b58e039c57","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-05-12 12:25:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-11 15:39:59","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC582.03","SPAC644.06c","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-05-11"},{"uniquename":"PMID:6343850","title":"Testing of chemicals for mutagenic activity with Schizosaccharomyces pombe.","citation":"Mutat Res 1983 Jun;115(2):215-23","abstract":"Two genetic end-points are used for testing mutagens in Schizosaccharomyces pombe: forward mutations of the loci which encode steps early in the adenine synthetic pathway and reversion of certain selected mutants. 54 chemicals have been tested for at least one of the genetic end-points. The relevant literature has been reviewed through 1979.","authors":"Loprieno N, Barale R, Von Halle ES, von Borstel RC","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"Jun 1983","pubmed_entrez_date":"1983-06-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35716431","title":"Rrp1, Rrp2 and Uls1 - Yeast SWI2/SNF2 DNA dependent translocases in genome stability maintenance.","citation":"DNA Repair (Amst) 2022 Aug;116:103356","abstract":"Multiple eukaryotic SWI2/SNF2 DNA translocases safeguard genome integrity, mostly by remodelling nucleosomes, but also by fine-tuning mechanisms of DNA repair, such as homologous recombination. Among this large family there is a unique class of Rad5/16-like enzymes, including Saccharomyces cerevisiae Uls1 and its Schizosaccharomyces pombe orthologues Rrp1 and Rrp2, that have both translocase and E3 ubiquitin ligase activities, and are often directed towards their substrates by SUMOylation. Here we summarize recent advances in understanding how different activities of these yeast proteins jointly contribute to their important roles in replication stress response particularly at centromeres and telomeres. This extends the possible range of functions performed by this class of SNF2 enzymes in human cells involving both their translocase and ubiquitin ligase activities and related to SUMOylation pathways within the nucleus.","doi":"10.1016/j.dnarep.2022.103356","authors":"Kramarz K, Dziadkowiec D","authors_abbrev":"Kramarz K et al.","pubmed_publication_date":"Aug 2022","pubmed_entrez_date":"2022-06-18","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-06-23 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16009555","title":"Some assembly required: yeast septins provide the instruction manual.","citation":"Trends Cell Biol 2005 Aug;15(8):414-24","abstract":"Septins are a family of conserved proteins that form hetero-oligomeric complexes that assemble into filaments. The filaments can be organized into linear arrays, coils, rings and gauzes. They serve as membrane-associated scaffolds and as barriers to demarcate local compartments, especially for the establishment of the septation site for cytokinesis. Studies in budding and fission yeast have revealed many of the protein-protein interactions that govern the formation of multi-septin complexes. GTP binding and phosphorylation direct the polymerization of filaments that is required for septin-collar assembly in budding yeast, whereas a homolog of anillin instructs timely formation of the ring of septin filaments at the medial cortex in fission yeast. These insights should aid understanding of the organization and function of the diverse septin structures in animal cells.","authors":"Versele M, Thorner J","authors_abbrev":"Versele M et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-07-13","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009800","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17188431","title":"Identification and biochemical analysis of a mitochondrial endonuclease of Podospora anserina related to curved-DNA binding proteins.","citation":"Biochim Biophys Acta 2007 Apr;1770(4):527-42","abstract":"We purified and characterized previously from Podospora anserina mitochondria an endonuclease, active on single-stranded, double-stranded and flap DNA, with RNAse H activity, named P49 according to the major 49 kDa band observed on SDS-PAGE. Edman sequencing allowed us to identify the corresponding gene called nuc49. Here we report the properties of the (His)-tagged NUC49 protein expressed in E. coli. We show that this protein does exhibit an endonuclease activity on plasmid DNA, circular recessed and flap M13 substrate with short protruding single strand. However, in contrast to the mt endonuclease purified fraction it does not present RNase H activity and does not cleave linear flap substrate. The activity differences between the protein expressed in E. coli and the mitochondrial endonuclease fraction previously described are discussed. NUC49 presents a strong homology with the S. pombe CDB4 curved DNA binding protein which belongs to a large family including the human cell cycle protein PA2G4 and is able to bind curved DNA. The results constitute the first description of a mitochondrial endonuclease activity associated to this family of proliferation associated homologous proteins. The function of this endonuclease either in recombination, repair or mt DNA rearrangements remains to be determined.","authors":"Laquel-Robert P, Sellem CH, Sainsard-Chanet A, Castroviejo M","authors_abbrev":"Laquel-Robert P et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2006-12-26","publication_year":"2007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23H4.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32124033","title":"Mutation in histone deacetylase clr6 promotes the survival of S. pombe cds1 null mutant in response to hydroxyurea.","citation":"Mol Genet Genomics 2020 May;295(3):695-703","abstract":"Fission yeast Cds1 is responsible for the replication checkpoint activation and helps to protect replication fork collapse in response to hydroxyurea (HU). Here, we investigated the role of histone deacetylase in response to replication fork arrest and observed that in the presence of HU, the survival of cds1Δ cells was improved when the cells were simultaneously treated with histone deacetylase inhibitors. Furthermore, a mutation in the histone deacetylase gene, clr6, also suppresses the growth defect of cds1Δ cells in response to HU indicating a suppressive role of clr6-1 mutation in cds1 deletion background upon HU treatment. Interestingly, in response to HU, phosphorylation of Chk1 kinase and the number of Rad52YFP foci was reduced in cds1Δ clr6-1 double mutant as compared to cds1Δ single mutant indicating a decrease in the level of DNA damage in response to HU. Accordingly, the single-cell gel electrophoresis assay revealed a drastic reduction in the tail length of cds1Δ clr6-1 double mutant as compared to cds1Δ cells in the presence of HU suggesting the suppression of chromosomal defects in the double mutant. Taken together, we proposed that there could be transient suppression of fork collapse in cds1Δ clr6-1 double mutant upon HU treatment due to the delay in mitotic progression that leads to the facilitation of cell growth.","doi":"10.1007/s00438-020-01655-z","authors":"Khan S, Ahamad N, Panigrahi L, Walworth N, Ahmed S","authors_abbrev":"Khan S et al.","pubmed_publication_date":"May 2020","pubmed_entrez_date":"2020-03-04","publication_year":"2020","canto_session_key":"593d8098fd17ef85","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-03-05 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC36.05c","SPCC18B5.11c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:37080282","title":"Gene regulatory networks with binary weights.","citation":"Biosystems 2023 May;227-228:104902","abstract":"An evolutionary computation framework to learn binary threshold networks is presented. Inspired by the recent trend of binary neural networks, where weights and activation thresholds are represented using 1 and -1 such that they can be stored in 1-bit instead of full precision, we explore this approach for gene regulatory network modeling. We test our method by inferring binary threshold networks of two regulatory network models: Quorum sensing systems in bacterium Paraburkholderia phytofirmans PsJN and the fission yeast cell-cycle. We considered differential evolution and particle swarm optimization for the simulations. Results for weights having only 1 and -1 values, and different activation thresholds are presented. Full binary threshold networks were found with minimum error (2 bits), whereas when the binary restriction is relaxed for the activation thresholds, networks with 0 bit error were found.","doi":"10.1016/j.biosystems.2023.104902","authors":"Ruz GA, Goles E","authors_abbrev":"Ruz GA et al.","pubmed_publication_date":"May 2023","pubmed_entrez_date":"2023-04-20","publication_year":"2023","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2023-04-22 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10960485","title":"Biochemical and functional characterization of inositol 1,3,4,5, 6-pentakisphosphate 2-kinases.","citation":"J Biol Chem 2000 Nov 24;275(47):36575-83","abstract":"Synthesis of inositol 1,2,3,4,5,6-hexakisphosphate (IP(6)), also known as phytate, is integral to cellular function in all eukaryotes. Production of IP(6) predominately occurs through phosphorylation of inositol 1,3,4,5,6-pentakisphosphate (IP(5)) by a 2-kinase. Recent cloning of the gene encoding this kinase from Saccharomyces cerevisiae, designated scIpk1, has identified a cellular role for IP(6) production in the regulation of mRNA export from the nucleus. In this report, we characterize the biochemical and functional parameters of recombinant scIpk1. Purified recombinant scIpk1 kinase activity is highly selective for IP(5) substrate and exhibits apparent K(m) values of 644 nm and 62.8 microm for IP(5) and ATP, respectively. The observed apparent catalytic efficiency (k(cat)/K(m)) of scIpk1 is 31,610 s(-)(1) m(-)(1). A sequence similarity search was used to identify an IP(5) 2-kinase from the fission yeast Schizosaccharomyces pombe. Recombinant spIpk1 has similar substrate selectivity and catalytic efficiency to its budding yeast counterpart, despite sharing only 24% sequence identity. Cells lacking sc-IPK1 are deficient in IP(6) production and exhibit lethality in combination with a gle1 mutant allele. Both of these phenotypes are complemented by expression of the spIPK1 gene in the sc-ipk1 cells. Analysis of several inactive mutants and multiple sequence alignment of scIpk1, spIpk1, and a putative Candida albicans Ipk1 have identified residues involved in catalysis. This includes two conserved motifs: E(i/l/m)KPKWL(t/y) and LXMTLRDV(t/g)(l/c)(f/y)I. Our data suggest that the mechanism for IP(6) production is conserved across species.","authors":"Ives EB, Nichols J, Wente SR, York JD","authors_abbrev":"Ives EB et al.","pubmed_publication_date":"24 Nov 2000","pubmed_entrez_date":"2000-08-29","publication_year":"2000","canto_session_key":"87af6376c69d68cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-05-25 11:17:54","canto_approved_date":"2024-05-25 11:17:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-25 11:17:37","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4B3.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-05-25"},{"uniquename":"EMBL:AU010632","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12719471","title":"Sim4: a novel fission yeast kinetochore protein required for centromeric silencing and chromosome segregation.","citation":"J Cell Biol 2003 Apr 28;161(2):295-307","abstract":"Fission yeast centromeres are composed of two domains: the central core and the outer repeats. Although both regions are required for full centromere function, the central core has a distinct chromatin structure and is likely to underlie the kinetochore itself, as it is associated with centromere-specific proteins. Genes placed within either region are transcriptionally silenced, reflecting the formation of a functional kinetochore complex and flanking centromeric heterochromatin. Here, transcriptional silencing was exploited to identify components involved in central core silencing and kinetochore assembly or structure. The resulting sim (silencing in the middle of the centromere) mutants display severe chromosome segregation defects. sim2+ encodes a known kinetochore protein, the centromere-specific histone H3 variant Cnp1CENP-A. sim4+ encodes a novel essential coiled-coil protein, which is specifically associated with the central core region and is required for the unusual chromatin structure of this region. Sim4 coimmunoprecipitates with the central core component Mis6 and, like Mis6, affects Cnp1CENP-A association with the central domain. Functional Mis6 is required for Sim4 localization at the kinetochore. Our analyses illustrate the fundamental link between silencing, chromatin structure, and kinetochore function, and establish defective silencing as a powerful approach for identifying proteins required to build a functional kinetochore.","authors":"Pidoux AL, Richardson W, Allshire RC","authors_abbrev":"Pidoux AL et al.","pubmed_publication_date":"28 Apr 2003","pubmed_entrez_date":"2003-04-30","publication_year":"2003","canto_session_key":"77d6af7bf719b589","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-01-31 17:02:32","canto_approved_date":"2026-01-29 13:49:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-21 12:54:16","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.04c","SPBC577.15c","SPAC23H3.08c","SPBC20F10.06","SPAC1687.20c","SPBC1105.17","SPBC18E5.03c","SPAPB1A10.02","SPBC26H8.07c","SPCC11E10.08","SPCC1322.12c","SPAC25B8.14"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2015-01-31"},{"uniquename":"PMID:22681890","title":"Hierarchical modularity and the evolution of genetic interactomes across species.","citation":"Mol Cell 2012 Jun 08;46(5):691-704","abstract":"To date, cross-species comparisons of genetic interactomes have been restricted to small or functionally related gene sets, limiting our ability to infer evolutionary trends. To facilitate a more comprehensive analysis, we constructed a genome-scale epistasis map (E-MAP) for the fission yeast Schizosaccharomyces pombe, providing phenotypic signatures for ~60% of the nonessential genome. Using these signatures, we generated a catalog of 297 functional modules, and we assigned function to 144 previously uncharacterized genes, including mRNA splicing and DNA damage checkpoint factors. Comparison with an integrated genetic interactome from the budding yeast Saccharomyces cerevisiae revealed a hierarchical model for the evolution of genetic interactions, with conservation highest within protein complexes, lower within biological processes, and lowest between distinct biological processes. Despite the large evolutionary distance and extensive rewiring of individual interactions, both networks retain conserved features and display similar levels of functional crosstalk between biological processes, suggesting general design principles of genetic interactomes.","doi":"10.1016/j.molcel.2012.05.028","authors":"Ryan CJ, Roguev A, Patrick K, Xu J, Jahari H, Tong Z, Beltrao P, Shales M, Qu H, Collins SR, Kliegman JI, Jiang L, Kuo D, Tosti E, Kim HS, Edelmann W, Keogh MC, Greene D, Tang C, Cunningham P, Shokat KM, Cagney G, Svensson JP, Guthrie C, Espenshade PJ, Ideker T, Krogan NJ","authors_abbrev":"Ryan CJ et al.","pubmed_publication_date":"08 Jun 2012","pubmed_entrez_date":"2012-06-12","publication_year":"2012","canto_session_key":"7c5a980860f3b18c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"vw253@cam.ac.uk","canto_first_approved_date":"2016-02-17 11:57:03","canto_approved_date":"2024-02-18 07:17:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-23 16:47:07","canto_added_date":"2012-10-19 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and characterization of the Schizosaccharomyces pombe gene encoding transcript elongation factor TFIIS.","citation":"Yeast 1996 Mar 15;12(3):227-36","abstract":"A gene designated tfs1 has been isolated from Schizosaccharomyces pombe based on its similarity to genes encoding transcription elongation factor TFIIS. The nucleotide sequence of the tfs1 gene predicts a polypeptide with similarity to mammalian. Drosophila and Saccharomyces cerevisiae TFIIS. A haploid Sz. pombe strain with tfs1 deleted from the genome is viable. Thus, tfs1 is not essential for viability. However, deletion of tfs1 results in slow growth and increased sensitivity to the drug 6-azauracil, a phenotype similar to that of a S. cerevisiae strain deleted for the gene encoding TFIIS. The DNA sequence of tfs1 has been deposited in GenBank under Accession Number U20526.","authors":"Williams LA, Kane CM","authors_abbrev":"Williams LA et al.","pubmed_publication_date":"15 Mar 1996","pubmed_entrez_date":"1996-03-15","publication_year":"1996","canto_session_key":"3e715341ef8deda7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-05-06 07:57:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-05 21:15:58","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20H4.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-05"},{"uniquename":"PMID:7501024","title":"Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast.","citation":"Nature 1995 Dec 14;378(6558):739-43","abstract":"In fission yeast the onset of mitosis is brought about by Cdc2/Cdc13 kinase, which is inhibited by the Wee1/Mik1 tyrosine kinases and activated by Cdc25 tyrosine phosphatase. This control network integrates many signals, including those that monitor DNA replication, DNA damage and cell size. We report here that a fission yeast MAP kinase pathway links the cell-cycle G2/M control with changes in the extracellular environment that affect cell physiology. Fission yeast spc1- mutants have a G2 delay that is greatly exacerbated by growth in high osmolarity media and nutrient limitation. A lethal interaction of spc1 and cdc25 mutations shows that Spc1 promotes the onset of mitosis. Spc1 is a MAP kinase homologue that is activated by Wis1 kinase in response to osmotic stress and nutrient limitation. Spc1 is inactivated by Pyp1, a phosphatase previously identified as a mitotic inhibitor. Pyp1 dephosphorylates only tyrosine-173 of Spc1, unlike the dual-specificity phosphatases that have been shown to regulate other MAP kinases.","authors":"Shiozaki K, Russell P","authors_abbrev":"Shiozaki K et al.","pubmed_publication_date":"14 Dec 1995","pubmed_entrez_date":"1995-12-14","publication_year":"1995","canto_session_key":"dbb1e62e1d85e3b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 16:38:36","canto_approved_date":"2025-06-12 05:51:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-20 15:35:03","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC19D5.01","SPBC11B10.09","SPCC18B5.03","SPAC24B11.06c","SPAC26F1.10c","SPBC409.07c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-10-31"},{"uniquename":"PMID:25195688","title":"Functional analysis of putative phosphoenolpyruvate transporters localized to the Golgi apparatus in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2014 Nov;14(7):1101-9","abstract":"The cell surface of Schizosaccharomyces pombe is negatively charged due to the presence of pyruvylated oligosaccharides, which is important for cell-cell recognition. However, the mechanism of pyruvate supply to oligosaccharides is not clearly understood. Here, we analyzed three putative phosphoenolpyruvate (PEP) transporter genes (pet1(+) , pet2(+) , and pet3(+) ) in S. pombe, identified by sequence homology search against the Arabidopsis thaliana PEP transporter AtPPT1. Schizosaccharomyces pombe strain carrying a disruption in pet1(+) (pet1Δ) or in pet2(+) (pet2Δ), but not the strain carrying a disruption in pet3(+) (pet3Δ), showed reduced pyruvate level on the cell surface. This reduction in pyruvate level was restored to the control level by expressing green fluorescent protein (GFP)-tagged Pet1p and Pet2p in respective disruptants. Fluorescence microscope studies revealed that GFP-tagged Pet1p and Pet2p were localized to the Golgi apparatus. Although expression of neither AtPPT1 nor AtPPT2 suppressed the pet1Δ phenotype, that of chimeric constructs, where the N-terminal regions of AtPPT1 and AtPPT2 were replaced by the N-terminal region of Pet1p, partially suppressed the pet1Δ phenotype. Furthermore, the reduction in cell surface negative charge in pet1Δ cells was restored by incubating these cells with recombinant Pvg1p and PEP. Thus, Pet1p and Pet2p are likely involved in transporting PEP from the cytoplasm into the Golgi.","doi":"10.1111/1567-1364.12207","authors":"Yoritsune K, Higuchi Y, Matsuzawa T, Takegawa K","authors_abbrev":"Yoritsune K et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-09-09","publication_year":"2014","canto_session_key":"b7a6635419d42c62","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-12-16 13:21:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-16 19:07:02","canto_added_date":"2014-09-11 00:15:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC83.11","SPAC22F8.04","SPAC8F11.10c","SPAC22E12.01"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-11-16"},{"uniquename":"PMID:20967229","title":"Checkpoint-dependent and -independent roles of Swi3 in replication fork recovery and sister chromatid cohesion in fission yeast.","citation":"PLoS One 2010 Oct 12;5(10):e13379","abstract":"Multiple genome maintenance processes are coordinated at the replication fork to preserve genomic integrity. How eukaryotic cells accomplish such a coordination is unknown. Swi1 and Swi3 form the replication fork protection complex and are involved in various processes including stabilization of replication forks, activation of the Cds1 checkpoint kinase and establishment of sister chromatid cohesion in fission yeast. However, the mechanisms by which the Swi1-Swi3 complex achieves and coordinates these tasks are not well understood. Here, we describe the identification of separation-of-function mutants of Swi3, aimed at dissecting the molecular pathways that require Swi1-Swi3. Unlike swi3 deletion mutants, the separation-of-function mutants were not sensitive to agents that stall replication forks. However, they were highly sensitive to camptothecin that induces replication fork breakage. In addition, these mutants were defective in replication fork regeneration and sister chromatid cohesion. Interestingly, unlike swi3-deleted cell, the separation-of-functions mutants were proficient in the activation of the replication checkpoint, but their fork regeneration defects were more severe than those of checkpoint mutants including cds1Δ, chk1Δ and rad3Δ. These results suggest that, while Swi3 mediates full activation of the replication checkpoint in response to stalled replication forks, Swi3 activates a checkpoint-independent pathway to facilitate recovery of collapsed replication forks and the establishment of sister chromatid cohesion. Thus, our separation-of-function alleles provide new insight into understanding the multiple roles of Swi1-Swi3 in fork protection during DNA replication, and into understanding how replication forks are maintained in response to different genotoxic agents.","doi":"10.1371/journal.pone.0013379","authors":"Rapp JB, Noguchi C, Das MM, Wong LK, Ansbach AB, Holmes AM, Arcangioli B, Noguchi E","authors_abbrev":"Rapp JB et al.","pubmed_publication_date":"12 Oct 2010","pubmed_entrez_date":"2010-10-23","publication_year":"2010","canto_session_key":"06af275a3781aeeb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-11-19 09:53:02","canto_approved_date":"2025-11-19 09:53:02","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-11-15 20:29:59","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":154,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC902.02c","SPBC216.06c","SPBC30D10.04","SPBC216.05","SPCC1259.13","SPCC18B5.11c","SPAC9E9.08"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2025-11-19"},{"uniquename":"PMID:28461655","title":"4-Thiouridine Labeling to Analyze mRNA Turnover in  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 May 01;2017(5)","abstract":"Traditionally, the half-lives of mRNAs were measured after inhibition of transcription to allow decay of the preexisting population. The protocol presented here is a more recently developed strategy in which mRNA turnover is analyzed by measuring the decline in levels of newly synthesized RNA labeled with 4-thiouridine (4sU) during a brief pulse. After RNA extraction, the 4sU is biotinylated and the labeled species are purified using streptavidin beads. DNA microarrays can then be used to compare this population with total RNA, allowing half-lives to be calculated.","doi":"10.1101/pdb.prot091645","authors":"Mata J, Wise JA","authors_abbrev":"Mata J et al.","pubmed_publication_date":"01 May 2017","pubmed_entrez_date":"2017-05-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-05-05 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8771785","title":"Arabidopsis profilins are functionally similar to yeast profilins: identification of a vascular bundle-specific profilin and a pollen-specific profilin.","citation":"Plant J 1996 Aug;10(2):269-79","abstract":"Four members of the Arabidopsis profilin (pfn) multigene family have been cloned, sequenced and analyzed. By RNA gel blot analysis it has been shown that these four genes fall into two groups: one group (pfn1 and pfn2) is expressed in all organs of the plant and the other group (pfn3 and pfn4) in floral tissues only. Based on amino acid sequence alignment Arabidopsis profilins can be divided into the same two groups: PFN1 and PFN2 are 89% identical and PFN3 and PFN4 are 91% identical. Between these two groups they are 71-75% identical. The Arabidopsis profilins bind poly-L-proline and can complement both the Saccharomyces cerevisiae profilin deletion mutant and the Schizosaccharomyces pombe cdc3-124/profilin mutation, showing that the plant profilins are functionally similar to yeast profilins despite the low amino acid sequence homology. Analysis of pfn promoter-GUS fusion genes in transgenic Arabidopsis shows that pfn2 is specifically expressed in the vascular bundles of roots, hypocotyls, cotyledons, leaves, sepals, petals, stamen filaments and stalks of developing seeds, whereas expression of pfn4 is restricted to mature and germinating pollen grains.","authors":"Christensen HE, Ramachandran S, Tan CT, Surana U, Dong CH, Chua NH","authors_abbrev":"Christensen HE et al.","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_session_key":"e2a958b4fbd0f3de","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:59:56","canto_session_submitted_date":"2012-03-03 15:59:42","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4A8.15c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:11529427","title":"Mechanism and control of meiotic recombination initiation.","citation":"Curr Top Dev Biol 2001;52:1-53","abstract":"Homologous recombination is essential during meiosis in most sexually reproducing organisms. In budding yeast, and most likely in other organisms as well, meiotic recombination proceeds via the formation and repair of DNA double-strand breaks (DSBs). These breaks appear to be formed by the Spo11 protein, with assistance from a large number of other gene products, by a topoisomerase-like transesterase mechanism. Recent studies in fission yeast, multicellular fungi, flies, worms, plants, and mammals indicate that the role of Spo11 in meiotic recombination initiation is highly conserved. This chapter reviews the properties of Spo11 and the other gene products required for meiotic DSB formation in a number of organisms and discusses ways in which recombination initiation is coordinated with other events occurring in the meiotic cell.","authors":"Keeney S","authors_abbrev":"Keeney S","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-09-01","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17315266","title":"Role of the alpha-glucanase Agn2p in ascus-wall endolysis following sporulation in fission yeast.","citation":"Yeast 2007 Apr;24(4):279-88","abstract":"During sporulation in the ascomyceteous fungus Schizosaccharomyces pombe, diploid cells undergo differentiation into asci containing four haploid ascospores, which are highly resistant to environmental stresses. Although the morphogenetic processes involved in ascospore formation have been studied extensively, little is known about the molecular mechanism that ensures the release of mature ascospores from the ascus, allowing their dispersal into the environment. Recently, we identified Agn2p as the paralogue of the characterized endo-(1,3)-alpha-glucanase Agn1p, and observed that asci deleted for agn2 are defective in ascospore dispersal. Here, we focus on the cellular and biochemical functions of Agn2p. By placing agn2 under the control of an inducible promoter, we show that expression of agn2 is required for the efficient release of ascospores from their asci. Furthermore, we characterize the enzyme activity of purified recombinant Agn2p and show that Agn2p, like Agn1p, is an endo-(1,3)-alpha-glucanase that produces predominantly (1,3)-alpha-glucan pentasaccharides. Finally, we demonstrate that exogenous addition of purified Agn2p liberated the ascospores from asci deleted for agn2. We propose that Agn2p participates in the endolysis of the ascus wall by hydrolysing its (1,3)-alpha-glucan, thereby assisting in the release of ascospores.","authors":"Dekker N, van Rijssel J, Distel B, Hochstenbach F","authors_abbrev":"Dekker N et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-02-23","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC646.06c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:20418666","title":"In quiescence of fission yeast, autophagy and the proteasome collaborate for mitochondrial maintenance and longevity.","citation":"Autophagy 2010 May;6(4):564-5","abstract":"Regulation of proliferation and quiescence in response to intra- or extracellular environmental signals are important for medicine and basic biology. Quiescence is relevant to tumorigenesis and tissue regeneration, and the maintenance of post-mitotic cells is important with regard to a number of senescence-related diseases such as neurodegeneration. We employ fission yeast, Schizosaccharomyces pombe, as a model to study quiescence and longevity as this lower eukaryote has a long chronological life span (over months) in quiescence that is induced by nitrogen starvation. We recently reported that autophagy and the proteasome cooperate in proper mitochondrial maintenance in the quiescent phase. Such cooperativity is not found in proliferating cells. In quiescence, the proteasome is required for normal mitochondrial functions; inactivation of the proteasome results in a large accumulation of reactive oxygen species (ROS), diminished mitochondrial function, and the elevation of proteins and compounds having anti-oxidant activities. Autophagy contributes to preventing the lethal accumulation of ROS by degrading mitochondria, the primary source of ROS. Our results indicate that the degradation of mitochondria by autophagy during proteasome dysfunction is a defense mechanism of quiescent cells against the accumulation of ROS.","doi":"10.4161/auto.6.4.11948","authors":"Takeda K, Yanagida M","authors_abbrev":"Takeda K et al.","pubmed_publication_date":"May 2010","pubmed_entrez_date":"2010-04-27","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9326493","title":"Substrate structure requirements of the Pac1 ribonuclease from Schizosaccharmyces pombe.","citation":"RNA 1997 Oct;3(10):1182-93","abstract":"The Pac1 ribonuclease of Schizosaccharomyces pombe is a member of the RNase III family of double-strand-specific ribonucleases. To examine RNA structural features required for efficient cleavage by the Pac1 RNase, we tested a variety of double-stranded and hairpin RNAs as substrates for the enzyme. The Pac1 RNase required substrates that have a minimal helix length of about 20 base pairs. The enzyme cut both strands of the helix at sites separated by two base pairs. However, Pac1 was also able to make a single-stranded cleavage within an internal bulge of an authentic Escherichia coli substrate at the same site chosen by RNase III. Pac1 efficiently degraded the structurally complex adenovirus VA RNA(I), but was inactive against the short HIV-1 TAR RNA hairpin. These results indicate that the Pac1 RNase prefers straight, perfect helices, but it can tolerate internal bulges that do not distort the helix severely. Like its homologue from Saccharomyces cerevisiae, the Pac1 RNase cleaved at two in vivo RNA processing sites in a hairpin structure in the 3' external transcribed spacer of the S. pombe pre-rRNA, suggesting a role for the enzyme in rRNA maturation.","authors":"Rotondo G, Huang JY, Frendewey D","authors_abbrev":"Rotondo G et al.","pubmed_publication_date":"Oct 1997","pubmed_entrez_date":"1997-11-05","publication_year":"1997","canto_session_key":"a30f8ddc63621c16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-30 13:31:13","canto_approved_date":"2023-03-02 08:11:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-17 17:51:45","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-03-30"},{"uniquename":"PMID:41786738","title":"An H3K14ub-H3K9me3 feedback circuit governs heterochromatin spreading and inheritance in fission yeast.","citation":"Nat Commun 2026 Mar 05;","abstract":"Heterochromatin is a bistable chromatin state essential for genome stability and gene regulation. Its spreading and inheritance have long been explained by a \"read-write\" cycle in which histone methyltransferases bind pre-existing tri-methylation of histone H3 lysine 9 (H3K9me3) and propagate this mark to neighboring nucleosomes. However, the weak affinity and limited catalytic stimulation provided by H3K9me3 alone challenge this model. The fission yeast H3K9 methyltransferase Clr4 functions within the CLRC complex, which also catalyzes histone H3 lysine 14 ubiquitination (H3K14ub). Here we show that H3K14ub and H3K9me3 form a feedback loop: H3K14ub strongly stimulates Clr4 activity on nucleosomes, while both H3K14ub and H3K9me3 stabilize CLRC binding to chromatin. Even subtle perturbations that disrupt this feedback, such as mutating one of the three H3 genes to prevent ubiquitination or methylation, or impairing Clr3-mediated H3K14 deacetylation, compromises heterochromatin spreading and inheritance. Conversely, counteracting activities, such as H3K14 acetylation by Mst2 and H3K9 demethylation by Epe1, synergistically constrains heterochromatin expansion. Thus, rather than relying solely on the weak H3K9me3 \"read-write\" cycle, heterochromatin is maintained through an integrated circuit of ubiquitination, deacetylation, and methylation, which governs spreading and inheritance.","doi":"10.1038/s41467-026-70276-8","authors":"Toda T, Zang J, Qi H, Fang Y, Jiang P, Shan CM, Wong J, Jia S","authors_abbrev":"Toda T et al.","pubmed_publication_date":"05 Mar 2026","pubmed_entrez_date":"2026-03-05","publication_year":"2026","canto_session_key":"f745b70966c55b35","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Songtao Jia","canto_first_approved_date":"2026-05-22 06:11:33","canto_approved_date":"2026-05-22 06:11:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-04-08 23:51:01","canto_added_date":"2026-03-08 00:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":75,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Songtao Jia","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.04","SPBC428.08c","SPBC1105.11c","SPCC11E10.08","SPAC694.06c","SPAC17G8.13c","SPBC8D2.04","SPBC4.04c","SPCC622.16c","SPCC613.12c","SPCC970.07c","SPBC800.03"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2026-05-22"},{"uniquename":"PMID:16251353","title":"DNA replication origins fire stochastically in fission yeast.","citation":"Mol Biol Cell 2006 Jan;17(1):308-16","abstract":"DNA replication initiates at discrete origins along eukaryotic chromosomes. However, in most organisms, origin firing is not efficient; a specific origin will fire in some but not all cell cycles. This observation raises the question of how individual origins are selected to fire and whether origin firing is globally coordinated to ensure an even distribution of replication initiation across the genome. We have addressed these questions by determining the location of firing origins on individual fission yeast DNA molecules using DNA combing. We show that the firing of replication origins is stochastic, leading to a random distribution of replication initiation. Furthermore, origin firing is independent between cell cycles; there is no epigenetic mechanism causing an origin that fires in one cell cycle to preferentially fire in the next. Thus, the fission yeast strategy for the initiation of replication is different from models of eukaryotic replication that propose coordinated origin firing.","authors":"Patel PK, Arcangioli B, Baker SP, Bensimon A, Rhind N","authors_abbrev":"Patel PK et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2005-10-28","publication_year":"2006","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20970334","title":"Nuclear compartmentalization is abolished during fission yeast meiosis.","citation":"Curr Biol 2010 Nov 09;20(21):1913-8","abstract":"In eukaryotic cells, the nuclear envelope partitions the nucleus from the cytoplasm. The fission yeast Schizosaccharomyces pombe undergoes closed mitosis in which the nuclear envelope persists rather than being broken down, as in higher eukaryotic cells. It is therefore assumed that nucleocytoplasmic transport continues during the cell cycle. Here we show that nuclear transport is, in fact, abolished specifically during anaphase of the second meiotic nuclear division. During that time, both nucleoplasmic and cytoplasmic proteins disperse throughout the cell, reminiscent of the open mitosis of higher eukaryotes, but the architecture of the S. pombe nuclear envelope itself persists. This functional alteration of the nucleocytoplasmic barrier is likely induced by spore wall formation, because ectopic induction of sporulation signaling leads to premature dispersion of nucleoplasmic proteins. A photobleaching assay demonstrated that nuclear envelope permeability increases abruptly at the onset of anaphase of the second meiotic division. The permeability was not altered when sporulation was inhibited by blocking the trafficking of forespore-membrane vesicles from the endoplasmic reticulum to the Golgi. The evidence indicates that yeast gametogenesis produces vesicle transport-mediated forespore membranes by inducing nuclear envelope permeabilization.","doi":"10.1016/j.cub.2010.09.004","authors":"Arai K, Sato M, Tanaka K, Yamamoto M","authors_abbrev":"Arai K et al.","pubmed_publication_date":"09 Nov 2010","pubmed_entrez_date":"2010-10-26","publication_year":"2010","canto_session_key":"6a45801fc3d039ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2025-04-17 09:07:18","canto_approved_date":"2025-04-17 09:07:18","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-17 09:07:02","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2025-04-17"},{"uniquename":"EMBL:AU014496","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009551","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.94"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28733408","title":"DNA Double-Strand Break Repair Assay.","citation":"Cold Spring Harb Protoc 2018 Apr 02;2018(4)","abstract":"DNA double-strand breaks (DSBs), arising during normal DNA metabolism or following exposure to mutagenic agents such as ionizing radiation can lead to chromosomal rearrangements and genome instability, and are potentially lethal if unrepaired. Therefore, understanding the mechanisms of DSB repair and misrepair, and identifying the factors involved in these processes is of biological as well as medical interest. Here we describe a DSB assay in  Schizosaccharomyces pombe  that can be used to identify and quantify different repair, misrepair, and failed repair events resulting from a site-specific DSB within the context of a nonessential minichromosome, Ch 16  This assay can be used to determine the contribution of most genes or genetic backgrounds to DSB repair and genome stability, and can also provide mechanistic insights into their function.","doi":"10.1101/pdb.prot092031","authors":"Pai CC, Blaikley E, Humphrey TC","authors_abbrev":"Pai CC et al.","pubmed_publication_date":"02 Apr 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25701403","title":"Two fission yeast high mobility group box proteins in the maintenance of genomic integrity following doxorubicin insult.","citation":"Gene 2015 May 10;562(1):70-5","abstract":"Drug resistance is a challenge in chemotherapy, and, to date, there has been little resolution as to how it is induced. We previously isolated a host of doxorubicin resistance (DXR) genes in fission yeast and here we investigate the regulation of this resistance through two high mobility group (HMG) motif-containing DXR proteins, Nht1 and Hap2. The concurrent deletion of nht1 and hap2 did not confer cumulative sensitivity to doxorubicin, indicating that these factors cooperate closely in similar epistatic groups. We show that doxorubicin treatment resulted in the subcellular reorganization of Rhp54, a homologous recombination-dependent DNA damage repair protein. The disruption of either nht1 or hap2 attenuated Rhp54-foci formation, suggesting that these factors modulate the repair of doxorubicin-induced DNA lesions via the recruitment of homologous recombination machinery. Epistatic analyses further confirmed that Nht1 and Hap2 act in similar functional groups with complexes related to DSB repair but act synergistically with factors that regulate transcription and chromosome segregation. Overall, this work shows the molecular crosstalk coordinated by HMG proteins in conferring doxorubicin resistance in fission yeast.","doi":"10.1016/j.gene.2015.02.041","authors":"Tang MY, Guo H, Nguyen TT, Low LS, Jackson RA, Yamada T, Chen ES","authors_abbrev":"Tang MY et al.","pubmed_publication_date":"10 May 2015","pubmed_entrez_date":"2015-02-22","publication_year":"2015","canto_session_key":"b8f50aefb8466a56","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-01 08:02:07","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-01 08:01:58","canto_added_date":"2015-02-25 01:15:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16C4.20c","SPBC1105.10","SPBC16A3.07c","SPAC17G8.07","SPAC630.14c","SPAC144.02","SPAC10F6.08c","SPAC1952.05","SPAC2F7.07c","SPAC23D3.09","SPAC1805.07c","SPAC15A10.03c","SPBC21B10.13c","SPAC3C7.03c","SPBC28F2.10c","SPCC23B6.05c"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2015-04-01"},{"uniquename":"PMID:29069466","title":"MGA repository: a curated data resource for ChIP-seq and other genome annotated data.","citation":"Nucleic Acids Res 2018 Jan 04;46(D1):D175-D180","abstract":"The Mass Genome Annotation (MGA) repository is a resource designed to store published next generation sequencing data and other genome annotation data (such as gene start sites, SNPs, etc.) in a completely standardised format. Each sample has undergone local processing in order the meet the strict MGA format requirements. The original data source, the reformatting procedure and the biological characteristics of the samples are described in an accompanying documentation file manually edited by data curators. 10 model organisms are currently represented: Homo sapiens, Mus musculus, Danio rerio, Drosophila melanogaster, Apis mellifera, Caenorhabditis elegans, Arabidopsis thaliana, Zea mays, Saccharomyces cerevisiae and Schizosaccharomyces pombe. As of today, the resource contains over 24 000 samples. In conjunction with other tools developed by our group (the ChIP-Seq and SSA servers), it allows users to carry out a great variety of analysis task with MGA samples, such as making aggregation plots and heat maps for selected genomic regions, finding peak regions, generating custom tracks for visualizing genomic features in a UCSC genome browser window, or downloading chromatin data in a table format suitable for local processing with more advanced statistical analysis software such as R. Home page: http://ccg.vital-it.ch/mga/.","doi":"10.1093/nar/gkx995","authors":"Dréos R, Ambrosini G, Groux R, Périer RC, Bucher P","authors_abbrev":"Dréos R et al.","pubmed_publication_date":"04 Jan 2018","pubmed_entrez_date":"2017-10-26","publication_year":"2018","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2017-10-28 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30355770","title":"RNA polymerase II CTD interactome with 3' processing and termination factors in fission yeast and its impact on phosphate homeostasis.","citation":"Proc Natl Acad Sci U S A 2018 Nov 06;115(45):E10652-E10661","abstract":"The carboxy-terminal domain (CTD) code encrypted within the Y 1 S 2 P 3 T 4 S 5 P 6 S 7  heptad repeats of RNA polymerase II (Pol2) is deeply rooted in eukaryal biology. Key steps to deciphering the code are identifying the events in gene expression that are governed by individual \"letters\" and then defining a vocabulary of multiletter \"words\" and their meaning. Thr4 and Ser7 exert opposite effects on the fission yeast  pho1  gene, expression of which is repressed under phosphate-replete conditions by transcription of an upstream flanking long noncoding RNA (lncRNA). Here we attribute the derepression of  pho1  by a CTD -S7A  mutation to precocious termination of lncRNA synthesis, an effect that is erased by mutations of cleavage-polyadenylation factor (CPF) subunits Ctf1, Ssu72, Ppn1, Swd22, and Dis2 and termination factor Rhn1. By contrast, a CTD -T4A  mutation hyperrepresses  pho1 , as do CPF subunit and Rhn1 mutations, implying that  T4A  reduces lncRNA termination. Moreover, CTD -T4A  is synthetically lethal with  ppn1 ∆ and  swd22 ∆, signifying that Thr4 and the Ppn1•Swd22 module play important, functionally redundant roles in promoting Pol2 termination. We find that Ppn1 and Swd22 become essential for viability when the CTD array is curtailed and that  S7A  overcomes the need for Ppn1•Swd22 in the short CTD context. Mutational synergies highlight redundant essential functions of ( i ) Ppn1•Swd22 and Rhn1, ( ii ) Ppn1•Swd22 and Ctf1, and ( iii ) Ssu72 and Dis2 phosphatases. CTD alleles  Y1F ,  S2A , and  T4A  have overlapping synthetic lethalities with  ppn1 ∆ and  swd22 ∆, suggesting that Tyr1-Ser2-Thr4 form a three-letter CTD word that abets termination, with Rhn1 being a likely \"reader\" of this word.","doi":"10.1073/pnas.1810711115","authors":"Sanchez AM, Shuman S, Schwer B","authors_abbrev":"Sanchez AM et al.","pubmed_publication_date":"06 Nov 2018","pubmed_entrez_date":"2018-10-26","publication_year":"2018","canto_session_key":"ab5171b90f5cef1d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-04-18 15:19:51","canto_approved_date":"2024-04-05 07:45:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-04-13 17:30:09","canto_added_date":"2018-10-27 00:15:05","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":36,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.03","SPBC776.02c","SPAC824.04","SPBC32H8.10","SPAC3G9.04","SPBC3B9.11c","SPBP4G3.02","SPAC1D4.06c","SPNCRNA.1712","SPBC28F2.12","SPCC74.02c","SPBC8E4.01c"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2023-04-18"},{"uniquename":"PMID:11532929","title":"Expression of Cdc18/Cdc6 and Cdt1 during G2 phase induces initiation of DNA replication.","citation":"EMBO J 2001 Sep 03;20(17):4648-56","abstract":"Cdc18/Cdc6 and Cdt1 are essential initiation factors for DNA replication. In this paper we show that expression of Cdc18 in fission yeast G2 cells is sufficient to override the controls that ensure one S phase per cell cycle. Cdc18 expression in G2 induces DNA synthesis by re-firing replication origins and recruiting the MCM Cdc21 to chromatin in the presence of low levels of Cdt1. However, when Cdt1 is expressed together with Cdc18 in G2, cells undergo very rapid, uncontrolled DNA synthesis, accumulating DNA contents of 64C or more. Our data suggest that Cdt1 may potentiate re-replication by inducing origins to fire more persistently, possibly by stabilizing Cdc18 on chromatin. In addition, low level expression of a mutant form of Cdc18 that cannot be phosphorylated by cyclin-dependent kinases is not sufficient to induce replication in G2, but does so only when co-expressed with Cdt1. Thus, regulation of both Cdc18 and Cdt1 in G2 plays a crucial role in preventing the re-initiation of DNA synthesis until the next cell cycle.","authors":"Yanow SK, Lygerou Z, Nurse P","authors_abbrev":"Yanow SK et al.","pubmed_publication_date":"03 Sep 2001","pubmed_entrez_date":"2001-09-05","publication_year":"2001","canto_session_key":"489d3679b1f959f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-05-07 15:54:49","canto_approved_date":"2024-06-27 13:44:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-05-07 15:54:43","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPBC14C8.07c","SPAC24H6.05","SPBC428.18"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-05-07"},{"uniquename":"PMID:27298342","title":"Identification of S-phase DNA damage-response targets in fission yeast reveals conservation of damage-response networks.","citation":"Proc Natl Acad Sci U S A 2016 Jun 28;113(26):E3676-85","abstract":"The cellular response to DNA damage during S-phase regulates a complicated network of processes, including cell-cycle progression, gene expression, DNA replication kinetics, and DNA repair. In fission yeast, this S-phase DNA damage response (DDR) is coordinated by two protein kinases: Rad3, the ortholog of mammalian ATR, and Cds1, the ortholog of mammalian Chk2. Although several critical downstream targets of Rad3 and Cds1 have been identified, most of their presumed targets are unknown, including the targets responsible for regulating replication kinetics and coordinating replication and repair. To characterize targets of the S-phase DDR, we identified proteins phosphorylated in response to methyl methanesulfonate (MMS)-induced S-phase DNA damage in wild-type, rad3∆, and cds1∆ cells by proteome-wide mass spectrometry. We found a broad range of S-phase-specific DDR targets involved in gene expression, stress response, regulation of mitosis and cytokinesis, and DNA replication and repair. These targets are highly enriched for proteins required for viability in response to MMS, indicating their biological significance. Furthermore, the regulation of these proteins is similar in fission and budding yeast, across 300 My of evolution, demonstrating a deep conservation of S-phase DDR targets and suggesting that these targets may be critical for maintaining genome stability in response to S-phase DNA damage across eukaryotes.","doi":"10.1073/pnas.1525620113","authors":"Willis NA, Zhou C, Elia AE, Murray JM, Carr AM, Elledge SJ, Rhind N","authors_abbrev":"Willis NA et al.","pubmed_publication_date":"28 Jun 2016","pubmed_entrez_date":"2016-06-15","publication_year":"2016","canto_session_key":"df3225a93491efe9","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-06-16 00:15:15","annotation_curators":[],"file_curator_name":"Nick Rhind","file_curator_role":"community","annotation_file_curators":[{"name":"Nick Rhind","community_curator":true,"annotation_count":1287,"orcid":"0000-0003-1758-7736","file_type":"protein_modification","file_name":"PMID_27298342_modifications.tsv"}],"genes":["SPCC285.13c","SPBC2F12.04","SPBC23G7.08c","SPBC1734.15","SPAPJ698.02c","SPAC25G10.09c","SPAC806.06c","SPBC16G5.05c","SPCC338.17c","SPAC10F6.08c","SPBC1198.11c","SPCC18.03","SPBC13E7.03c","SPBC16D10.07c","SPBC646.08c","SPBC16H5.02","SPCC1906.02c","SPAC12G12.04","SPAC144.17c","SPAC30.01c","SPCC1235.09","SPAC9.13c","SPAP8A3.07c","SPBC31F10.13c","SPAC1071.10c","SPBC23E6.07c","SPAC24H6.13","SPAC1399.03","SPAC23H3.15c","SPBC17D1.05","SPBC1773.11c","SPCC16C4.07","SPBC19C7.11","SPAC23C11.16","SPAC521.04c","SPBC6B1.10","SPAC24B11.10c","SPBC3H7.13","SPBC28F2.07","SPAC222.14c","SPBC13E7.08c","SPBC660.11","SPBP4H10.13","SPCC1223.06","SPCC1020.12c","SPAC29B12.04","SPBC6B1.07","SPBC4F6.12","SPAC29A4.10","SPBC609.01","SPCC1393.10","SPAC1B3.05","SPAC23H3.09c","SPBC887.12","SPAC30D11.10","SPCC162.12","SPAC23G3.06","SPAC29B12.07","SPCC417.05c","SPAC31G5.15","SPBC17F3.02","SPCC663.01c","SPBC11C11.06c","SPAC1687.09","SPAC1805.05","SPBC23E6.09","SPBC16H5.03c","SPBC17G9.08c","SPCC63.08c","SPBC947.01","SPBC11B10.05c","SPAC27F1.08","SPBC1815.01","SPAC328.03","SPAC17G6.09","SPBC16G5.15c","SPCC1827.02c","SPBC3F6.04c","SPBC2G5.04c","SPAC25B8.05","SPBC530.15c","SPBC1861.09","SPCC1020.05","SPBC1271.09","SPCC1281.02c","SPCC1739.10","SPBC530.04","SPAC27D7.02c","SPBC25B2.03","SPBC216.05","SPCC757.07c","SPAC6G9.15c","SPAC3G9.05","SPAC8C9.15c","SPCC1183.06","SPAC3G9.12","SPBC16D10.04c","SPBC336.06c","SPBC887.10","SPBC215.06c","SPBC18H10.04c","SPAC29B12.10c","SPAC56F8.03","SPBC365.13c","SPAC589.10c","SPCC1739.11c","SPAC6G9.14","SPBP35G2.14","SPAPJ696.02","SPAC26A3.05","SPBC1198.13c","SPBC2D10.04","SPBC28E12.05","SPAC1F8.07c","SPBC902.04","SPBC3E7.05c","SPAC20H4.03c","SPBC365.11","SPCC320.08","SPBC409.05","SPAC6B12.11","SPAC6B12.09","SPCC162.01c","SPBC354.05c","SPAC57A10.10c","SPAC139.01c","SPBC1604.12","SPCC1902.01","SPCC364.06","SPAC688.07c","SPBC20F10.07","SPAC22F8.05","SPAC26F1.13c","SPBC25H2.05","SPBC1685.14c","SPBC31F10.07","SPCC1795.11","SPAC6G9.06c","SPBC12C2.10c","SPBC19G7.15","SPBC36.11","SPAC140.02","SPBC83.09c","SPBC1709.11c","SPAC644.16","SPBC30B4.03c","SPBC902.02c","SPAC1006.03c","SPCC23B6.04c","SPAC869.05c","SPBC19C2.07","SPBC1703.14c","SPCP1E11.04c","SPCC1840.02c","SPCC1259.07","SPAC110.01","SPAC1142.01","SPAC17G8.12","SPAC17A5.12","SPBC1734.01c","SPCC1672.02c","SPBC21C3.11","SPAC1F3.09","SPAC1006.09","SPAC17A5.13","SPAC9.11","SPBC1826.01c","SPBC354.13","SPBC887.01","SPAC644.06c","SPBC32F12.06","SPAC2C4.15c","SPAC2F3.14c","SPAC22H10.11c","SPBC530.14c","SPCC63.14","SPCC18.02","SPAC27F1.06c","SPAC926.06c","SPAC1952.13","SPBC23G7.04c","SPBC27B12.06","SPBC1711.07","SPBC1604.14c","SPAC22F8.09","SPAC23A1.17","SPAC3A12.11c","SPCC306.09c","SPBC887.14c","SPBC557.04","SPAC926.04c","SPBC12D12.04c","SPAC637.05c","SPBP8B7.19","SPAC1071.07c","SPCC364.07","SPAC977.14c","SPCP1E11.09c","SPBC1734.06","SPAC16C9.07","SPAC637.04","SPBC1709.02c","SPBC1A4.05","SPAC22G7.10","SPCC1827.06c","SPAC4G8.05","SPCP1E11.02","SPAC4H3.10c","SPCC736.15","SPAC13G7.13c","SPBC16A3.07c","SPBC1709.15c","SPCC16A11.17","SPBC29B5.03c","SPBP35G2.08c","SPBC16D10.06","SPBC1D7.02c","SPAC57A7.12","SPAC10F6.16","SPAC1002.10c","SPBC1706.01","SPBC3E7.06c","SPCC4B3.15","SPCC132.04c","SPAC32A11.04c","SPAC1F5.05c","SPBC106.04","SPBC36.01c","SPCC1183.07","SPCC285.16c","SPAC167.05","SPBC365.06","SPCC320.05","SPBC1711.05","SPAC17C9.03","SPBC146.03c","SPAC11E3.11c","SPAC7D4.02c","SPAC15A10.13","SPAC29B12.02c","SPAC23D3.04c","SPAC1F3.01","SPBC14C8.16c","SPAC1952.12c","SPBC21B10.07","SPAC22G7.06c","SPAC3H5.10","SPCC1442.09","SPBC2F12.05c","SPAC1687.20c","SPAC19G12.14","SPBC16E9.16c","SPBC342.05","SPAC19A8.11c","SPAC3F10.06c","SPBC25D12.04","SPBC29A10.05","SPAC664.01c","SPAC1142.04","SPAC24H6.06","SPAC1327.01c","SPBC839.17c","SPCC23B6.01c","SPAC4F10.13c","SPBC1271.10c","SPCC777.14","SPBC19F5.04","SPBC106.14c","SPBC12C2.03c","SPAC13G7.08c","SPCC4F11.02","SPAC14C4.11","SPCC10H11.01","SPAC24B11.11c","SPAC1805.01c","SPAC31A2.05c","SPCC970.08","SPAC9E9.05","SPCP31B10.06","SPAC24B11.06c","SPAC7D4.12c","SPBC409.07c","SPBC4C3.12","SPAC1783.05","SPAP8A3.04c","SPAC1952.17c","SPAC458.02c","SPBC11C11.01","SPAC17A2.09c","SPBC146.09c","SPAC22F8.11","SPAC1782.09c","SPAC19A8.15","SPAC23C4.02","SPBC428.10","SPAC664.03","SPBC725.04","SPBC6B1.05c","SPAC6F12.14","SPAC1783.07c","SPCC18B5.11c","SPCC1450.11c","SPBP22H7.07","SPAC3H8.02","SPBC1921.07c","SPBC839.10","SPBC216.07c","SPAC1142.08","SPCC1739.01","SPBC25D12.02c","SPCC584.05","SPAC29E6.02","SPCC70.08c","SPAC1A6.07","SPBC216.01c","SPAC3H8.06","SPCC31H12.03c","SPCC584.04","SPBC4F6.06","SPBC18E5.07","SPBP8B7.14c","SPBC25D12.05","SPCC1795.08c","SPBC83.05","SPBC1347.02","SPBC16E9.13","SPBP8B7.20c","SPAC6B12.05c","SPCC16C4.13c","SPBC3E7.15c","SPAC1687.05","SPAC3C7.11c","SPAC227.15","SPBC1778.02","SPCC622.08c","SPBC119.09c","SPBC16C6.11","SPCC1235.14","SPBC1685.13","SPAC343.09","SPAC2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mutated in poikiloderma with neutropenia protein 1, is a conserved 3'-to-5' RNA exonuclease processing U6 small nuclear RNA.","citation":"Cell Rep 2012 Oct 25;2(4):855-65","abstract":"Clericuzio-type poikiloderma with neutropenia (PN) is a rare genodermatosis associated with mutations in the C16orf57 gene, which codes for the uncharacterized protein hMpn1. We show here that, in both fission yeasts and humans, Mpn1 processes the spliceosomal U6 small nuclear RNA (snRNA) posttranscriptionally. In Mpn1-deficient cells, U6 molecules carry 3' end polyuridine tails that are longer than those in normal cells and lack a terminal 2',3' cyclic phosphate group. In mpn1Δ yeast cells, U6 snRNA and U4/U6 di-small nuclear RNA protein complex levels are diminished, leading to precursor messenger RNA splicing defects, which are reverted by expression of either yeast or human Mpn1 and by overexpression of U6. Recombinant hMpn1 is a 3'-to-5' RNA exonuclease that removes uridines from U6 3' ends, generating terminal 2',3' cyclic phosphates in vitro. Finally, U6 degradation rates increase in mpn1Δ yeasts and in lymphoblasts established from individuals affected by PN. Our data indicate that Mpn1 promotes U6 stability through 3' end posttranscriptional processing and implicate altered U6 metabolism as a potential mechanism for PN pathogenesis.","doi":"10.1016/j.celrep.2012.08.031","authors":"Shchepachev V, Wischnewski H, Missiaglia E, Soneson C, Azzalin CM","authors_abbrev":"Shchepachev V et al.","pubmed_publication_date":"25 Oct 2012","pubmed_entrez_date":"2012-10-02","publication_year":"2012","canto_session_key":"6206e69fb2754a89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-04 10:26:42","canto_approved_date":"2024-12-30 15:50:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-26 10:27:45","canto_added_date":"2015-08-25 12:52:15","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.214","SPAC23C11.10","SPBC660.16","SPBP8B7.16c","SPSNRNA.06"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2015-11-04"},{"uniquename":"EMBL:AU009525","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25023750","title":"Functional significance of nuclear export and mRNA binding of meiotic regulator Spo5 in fission yeast.","citation":"BMC Microbiol 2014 Jul 15;14:188","abstract":"Meiotic cells undergo two rounds of nuclear division and generate gametes. Previous studies have indicated that a number of transcription factors modulate the transcriptome in successive waves during meiosis and spore formation in fission yeast. However, the mechanisms underlying the post-transcriptional regulation in meiosis are not fully understood. The fission yeast spo5+ gene encodes a meiosis-specific RNA-binding protein, which is required for the progression of meiosis II and spore formation. However, the target RNA molecules of Spo5 are yet to be identified. Characterization of meiosis-specific RNA-binding proteins will provide insight into how post-transcriptional regulation influence gene expression during sexual differentiation.\nTo assess the functional significance of RNA-recognition motifs (RRMs) of Spo5, we constructed a series of new spo5 truncated mutants and previously reported spo5 missense mutants. In addition, we isolated novel spo5 missense mutants. The phenotypic characteristics of these mutants indicated that the RRMs are essential for both the localization and function of the protein. Interestingly, Spo5 is exported from the nucleus to the cytoplasm via the Rae1-dependent mRNA export pathway, but is unlikely to be involved in global mRNA export. Furthermore, cytoplasmic localization of Spo5 is important for its function, which suggests the involvement of Spo5 in post-transcriptional regulation. We identified pcr1+ mRNA as one of the critical targets of Spo5. The pcr1+ gene encodes an activating transcription factor/cAMP response element binding (ATF/CREB) transcription factor family. Among the four family members, namely Pcr1, Atf1, Atf21, and Atf31, only the mRNA encoding Pcr1 binds to Spo5.\nSpo5 is exported from the nucleus with mRNAs via the Rae1-dependent pathway. RRMs are necessary for this process and also for the function of Spo5 after the nuclear export. Spo5 appears to influence the activity of pcr1+ mRNA, and the mechanism of how Spo5 stimulates the mRNA to promote the progression of meiosis II and spore formation remains an intriguing question for future research.","doi":"10.1186/1471-2180-14-188","authors":"Togashi N, Yamashita A, Sato M, Yamamoto M","authors_abbrev":"Togashi N et al.","pubmed_publication_date":"15 Jul 2014","pubmed_entrez_date":"2014-07-16","publication_year":"2014","canto_session_key":"7fb1e9d8090945d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-07-17 00:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC21E11.03c","SPBC29A10.02"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU013582","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15576943","title":"Assaying cell cycle checkpoints: activity of the protein kinase Chk1.","citation":"Methods Mol Biol 2005;296:345-54","abstract":"Eukaryotic cells regulate progression through the cell cycle in response to DNA damage. Cell cycle checkpoints are the signal transduction pathways that couple the detection of DNA damage to the proteins that control transitions in the cell cycle. The protein kinase Chk1, originally discovered in fission yeast, but conserved in humans, is essential for preventing mitotic entry in the presence of DNA damage or blocks to DNA replication that cannot be reconciled. Chk1 is phosphorylated in response to DNA damage. Phosphorylation depends on the activity of conserved components of the checkpoint pathway including Rad3, a member of the ATM/ATR family of kinases. Phosphorylation leads to activation of Chk1 kinase activity. In this chapter, we describe an assay for monitoring the activity of Chk1 isolated.","authors":"Palermo C, Walworth NC","authors_abbrev":"Palermo C et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2004-12-04","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14560953","title":"The fission yeast TOR proteins and the rapamycin response: an unexpected tale.","citation":"Curr Top Microbiol Immunol 2004;279:85-95","abstract":"The TOR proteins are known as key regulators of cell growth in response to nutritional and mitogenic signals and as targets for the immunosuppressive and anti-cancerous drug rapamycin. The fission yeast Schizosaccharomyces pombe has two TOR homologues, tor1+ and tor2+. Despite their structural similarity, these genes have distinct functions: tor1+ is required under starvation, extreme temperatures, and osmotic or oxidative stress conditions, whereas tor2+ is required under normal growth conditions. Surprisingly, rapamycin does not seem to inhibit the S. pombe TOR-related functions. Rapamycin specifically inhibits sexual development in S. pombe, and this seems to stem from direct inhibition of the S. pombe FKBP12 homologue. Why S. pombe cells are resistant to rapamycin during the growth phase is as yet unclear and awaits further analysis of the TOR-dependent signaling pathways.","authors":"Weisman R","authors_abbrev":"Weisman R","pubmed_publication_date":"2004","pubmed_entrez_date":"2003-10-17","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5640702","title":"Morphometric analysis of yeast cells. II. Cell size of Schizosaccharomyces pombe during the growth cycle.","citation":"Exp Cell Res 1968 Jan;49(1):59-68","abstract":"","authors":"Johnson BF","authors_abbrev":"Johnson BF","pubmed_publication_date":"Jan 1968","pubmed_entrez_date":"1968-01-01","publication_year":"1968","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22531001","title":"Genome-wide identification and characterization of replication origins by deep sequencing.","citation":"Genome Biol 2012 Apr 24;13(4):R27","abstract":"DNA replication initiates at distinct origins in eukaryotic genomes, but the genomic features that define these sites are not well understood.\nWe have taken a combined experimental and bioinformatic approach to identify and characterize origins of replication in three distantly related fission yeasts: Schizosaccharomyces pombe, Schizosaccharomyces octosporus and Schizosaccharomyces japonicus. Using single-molecule deep sequencing to construct amplification-free high-resolution replication profiles, we located origins and identified sequence motifs that predict origin function. We then mapped nucleosome occupancy by deep sequencing of mononucleosomal DNA from the corresponding species, finding that origins tend to occupy nucleosome-depleted regions.\nThe sequences that specify origins are evolutionarily plastic, with low complexity nucleosome-excluding sequences functioning in S. pombe and S. octosporus, and binding sites for trans-acting nucleosome-excluding proteins functioning in S. japonicus. Furthermore, chromosome-scale variation in replication timing is conserved independently of origin location and via a mechanism distinct from known heterochromatic effects on origin function. These results are consistent with a model in which origins are simply the nucleosome-depleted regions of the genome with the highest affinity for the origin recognition complex. This approach provides a general strategy for understanding the mechanisms that define DNA replication origins in eukaryotes.","doi":"10.1186/gb-2012-13-4-r27","authors":"Xu J, Yanagisawa Y, Tsankov AM, Hart C, Aoki K, Kommajosyula N, Steinmann KE, Bochicchio J, Russ C, Regev A, Rando OJ, Nusbaum C, Niki H, Milos P, Weng Z, Rhind N","authors_abbrev":"Xu J et al.","pubmed_publication_date":"24 Apr 2012","pubmed_entrez_date":"2012-04-26","publication_year":"2012","canto_session_key":"1f206f98668cbef8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-02-14 11:28:11","canto_approved_date":"2020-02-14 11:28:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-14 11:27:36","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2020-02-14"},{"uniquename":"PMID:16051179","title":"Role of fission yeast myosin I in organization of sterol-rich membrane domains.","citation":"Curr Biol 2005 Jul 26;15(14):1331-6","abstract":"Specialized membrane domains containing lipid rafts are thought to be important for membrane processes such as signaling and trafficking. An unconventional type I myosin has been shown to reside in lipid rafts and function to target a disaccharidase to rafts in brush borders of intestinal mammalian cells. In the fission yeast Schizosaccharomyces pombe, distinct sterol-rich membrane domains are formed at the cell division site and sites of polarized cell growth at cell tips. Here, we show that the sole S. pombe myosin I, myo1p, is required for proper organization of these membrane domains. myo1 mutants lacking the TH1 domain exhibit a uniform distribution of sterol-rich membranes all over the plasma membrane throughout the cell cycle. These effects are independent of endocytosis because myo1 mutants exhibit no endocytic defects. Conversely, overexpression of myo1p induces ectopic sterol-rich membrane domains. Myo1p localizes to nonmotile foci that cluster in sterol-rich plasma membrane domains and fractionates with detergent-resistant membranes. Because the myo1p TH1 domain may bind directly to acidic phospholipids, these findings suggest a model for how type I myosin contributes to the organization of specialized membrane domains.","authors":"Takeda T, Chang F","authors_abbrev":"Takeda T et al.","pubmed_publication_date":"26 Jul 2005","pubmed_entrez_date":"2005-07-30","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29930079","title":"A novel live-cell imaging system reveals a reversible hydrostatic pressure impact on cell-cycle progression.","citation":"J Cell Sci 2018 Aug 06;131(15)","abstract":"Life is dependent upon the ability of a cell to rapidly respond to changes in the environment. Small perturbations in local environments change the ability of molecules to interact and, hence, communicate. Hydrostatic pressure provides a rapid non-invasive, fully reversible method for modulating affinities between molecules both  in vivo  and  in vitro  We have developed a simple fluorescence imaging chamber that allows intracellular protein dynamics and molecular events to be followed at pressures <200 bar in living cells. By using yeast, we investigated the impact of hydrostatic pressure upon cell growth and cell-cycle progression. While 100 bar has no effect upon viability, it induces a delay in chromosome segregation, resulting in the accumulation of long undivided cells that are also bent, consistent with disruption of the cytoskeletons. This delay is independent of stress signalling and induces synchronisation of cell-cycle progression. Equivalent effects were observed in  Candida albicans , with pressure inducing a reversible cell-cycle delay and hyphal growth. We present a simple novel non-invasive fluorescence microscopy-based approach to transiently impact molecular dynamics in order to visualise, dissect and study signalling pathways and cellular processes in living cells.","doi":"10.1242/jcs.212167","authors":"Brooker HR, Gyamfi IA, Wieckowska A, Brooks NJ, Mulvihill DP, Geeves MA","authors_abbrev":"Brooker HR et al.","pubmed_publication_date":"06 Aug 2018","pubmed_entrez_date":"2018-06-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-06-24 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8443413","title":"Cell cycle expression of two replicative DNA polymerases alpha and delta from Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1993 Feb;4(2):145-57","abstract":"We have investigated the expression of two Schizosaccharomyces pombe replicative DNA polymerases alpha and delta during the cell cycle. The pol alpha+ and pol delta+ genes encoding DNA polymerases alpha and delta were isolated from S. pombe. Both pol alpha+ and pol delta+ genes are single copy genes in haploid cells and are essential for cell viability. In contrast to Saccharomyces cerevisiae homologs, the steady-state transcripts of both S. pombe pol alpha+ and pol delta+ genes were present throughout the cell cycle. Sequence analysis of the pol alpha+ and pol delta+ genes did not reveal the Mlu I motifs in their upstream sequences that are involved in cell cycle-dependent transcription of S. cerevisiae DNA synthesis genes as well as the S. pombe cdc22+ gene at the G1/S boundary. However, five near-match Mlu I motifs were found in the upstream region of the pol alpha+ gene. S. pombe DNA polymerases alpha and delta proteins were also expressed constantly throughout the cell cycle. In addition, the enzymatic activity of the S. pombe DNA polymerase alpha measured by in vitro assay was detected at all stages of the cell cycle. Thus, these S. pombe replicative DNA polymerases, like that of S. pombe cdc17+ gene, are expressed throughout the cell cycle at the transcriptional and protein level. These results indicate that S. pombe has at least two regulatory modes for the expression of genes involved in DNA replication and DNA precursor synthesis.","authors":"Park H, Francesconi S, Wang TS","authors_abbrev":"Park H et al.","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_session_key":"09f828b671f1e7ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-18 17:01:53","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-18 17:01:43","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.04","SPAC3H5.06c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2014-09-18"},{"uniquename":"PMID:24992933","title":"TORC2-a new player in genome stability.","citation":"EMBO Mol Med 2014 Aug;6(8):995-1002","abstract":"The inhibition of the central growth regulatory kinase TOR, which participates in two complexes, TORC1 and TORC2, has been a focus of metabolic and cancer studies for many years. Most studies have dealt with TORC1, the canonical target of rapamycin, and the role of this complex in autophagy, protein synthesis, and cell growth control. Recent work on TORC2 in budding and fission yeast species points to a conserved role of this lesser-known TOR complex in the survival of DNA damage. In budding yeast, TORC2 controls lipid biosynthesis and actin cytoskeleton through downstream AGC kinases, which are now, surprisingly, implicated in the survival of oxidative DNA damage. Preliminary data from mTORC2 modulation in cancer cells suggest that an extension to human chemotherapy is worth exploring.","doi":"10.15252/emmm.201403959","authors":"Weisman R, Cohen A, Gasser SM","authors_abbrev":"Weisman R et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-07-05","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-07-07 00:15:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10648098","title":"Nickel transport systems in microorganisms.","citation":"Arch Microbiol 2000 Jan;173(1):1-9","abstract":"The transition metal Ni is an essential cofactor for a number of enzymatic reactions in both prokaryotes and eukaryotes. Molecular analyses have revealed the existence of two major types of high-affinity Ni2+ transporters in bacteria. The Nik system of Escherichia coli is a member of the ABC transporter family and provides Ni2+ ion for the anaerobic biosynthesis of hydrogenases. The periplasmic binding protein of the transporter, NikA, is likely to play a dual role. It acts as the primary binder in the uptake process and is also involved in negative chemotaxis to escape Ni overload. Expression of the nik operon is controlled by the Ni-responsive repressor NikR, which shows functional similarity to the ferric ion uptake regulator Fur. The second type of Ni2+ transporter is represented by HoxN of Ralstonia eutropha, the prototype of a novel family of transition metal permeases. Members of this family have been identified in gram-negative and gram-positive bacteria and recently also in a fission yeast. They transport Ni2+ with very high affinity, but differ with regard to specificity. Site-directed mutagenesis experiments have identified residues that are essential for transport. Besides these uptake systems, different types of metal export systems, which prevent microorganisms from the toxic effects of Ni2+ at elevated intracellular concentrations, have also been described.","authors":"Eitinger T, Mandrand-Berthelot MA","authors_abbrev":"Eitinger T et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-27","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33266419","title":"Mechanistic Insights into the Allosteric Regulation of the Clr4 Protein Lysine Methyltransferase by Autoinhibition and Automethylation.","citation":"Int J Mol Sci 2020 Nov 22;21(22)","abstract":"Clr4 is a histone H3 lysine 9 methyltransferase in  Schizosaccharomyces pombe  that is essential for heterochromatin formation. Previous biochemical and structural studies have shown that Clr4 is in an autoinhibited state in which an autoregulatory loop (ARL) blocks the active site. Automethylation of lysine residues in the ARL relieves autoinhibition. To investigate the mechanism of Clr4 regulation by autoinhibition and automethylation, we exchanged residues in the ARL by site-directed mutagenesis leading to stimulation or inhibition of automethylation and corresponding changes in Clr4 catalytic activity. Furthermore, we demonstrate that Clr4 prefers monomethylated (H3K9me1) over unmodified (H3K9me0) histone peptide substrates, similar to related human enzymes and, accordingly, H3K9me1 is more efficient in overcoming autoinhibition. Due to enzyme activation by automethylation, we observed a sigmoidal dependence of Clr4 activity on the AdoMet concentration, with stimulation at high AdoMet levels. In contrast, an automethylation-deficient mutant showed a hyperbolic Michaelis-Menten type relationship. These data suggest that automethylation of the ARL could act as a sensor for AdoMet levels in cells and regulate the generation and maintenance of heterochromatin accordingly. This process could connect epigenome modifications with the metabolic state of cells. As other human protein lysine methyltransferases (for example, PRC2) also use automethylation/autoinhibition mechanisms, our results may provide a model to describe their regulation as well.","doi":"10.3390/ijms21228832","authors":"Khella MS, Bröhm A, Weirich S, Jeltsch A","authors_abbrev":"Khella MS et al.","pubmed_publication_date":"22 Nov 2020","pubmed_entrez_date":"2020-12-03","publication_year":"2020","canto_session_key":"68686c2a5f088c4c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-12-05 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9864354","title":"Fission yeast bub1 is a mitotic centromere protein essential for the spindle checkpoint and the preservation of correct ploidy through mitosis.","citation":"J Cell Biol 1998 Dec 28;143(7):1775-87","abstract":"The spindle checkpoint ensures proper chromosome segregation by delaying anaphase until all chromosomes are correctly attached to the mitotic spindle. We investigated the role of the fission yeast bub1 gene in spindle checkpoint function and in unperturbed mitoses. We find that bub1(+) is essential for the fission yeast spindle checkpoint response to spindle damage and to defects in centromere function. Activation of the checkpoint results in the recruitment of Bub1 to centromeres and a delay in the completion of mitosis. We show that Bub1 also has a crucial role in normal, unperturbed mitoses. Loss of bub1 function causes chromosomes to lag on the anaphase spindle and an increased frequency of chromosome loss. Such genomic instability is even more dramatic in Deltabub1 diploids, leading to massive chromosome missegregation events and loss of the diploid state, demonstrating that bub1(+ )function is essential to maintain correct ploidy through mitosis. As in larger eukaryotes, Bub1 is recruited to kinetochores during the early stages of mitosis. However, unlike its vertebrate counterpart, a pool of Bub1 remains centromere-associated at metaphase and even until telophase. We discuss the possibility of a role for the Bub1 kinase after the metaphase-anaphase transition.","authors":"Bernard P, Hardwick K, Javerzat JP","authors_abbrev":"Bernard P et al.","pubmed_publication_date":"28 Dec 1998","pubmed_entrez_date":"1998-12-29","publication_year":"1998","canto_session_key":"8b51c7a94991f857","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-05 07:58:02","canto_approved_date":"2019-11-05 08:47:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-30 16:29:50","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPCC1322.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-11-05"},{"uniquename":"PMID:21970592","title":"QD-antibody conjugates via carbodiimide-mediated coupling: a detailed study of the variables involved and a possible new mechanism for the coupling reaction under basic aqueous conditions.","citation":"Langmuir 2011 Nov 15;27(22):13888-96","abstract":"A detailed study into the optimization of carbodiimide-mediated coupling of antibodies (Ab) and quantum dots (QD) for use in cellular imaging has been undertaken. This involved the grafting of commercially available carboxyl-modified QDs (Evident Technologies \"Lake Placid Blue\" Evitag and eBioscience's eflour nanocrystals) with anti-Cdc8 Abs to produce conjugates with specific affinity for fission yeast tropomyosin Cdc8 protein. The water-soluble carbodiimide 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) was used to activate the QDs prior to their incubation with antibody, and a range of QD-carboxyl/EDC/Ab mole ratios were used in the experiments in attempts to optimize fluorescence and bioaffinity of the conjugate products (EDC to QD-carboxyl-600 nmol/15 pmol to 0.12 nmol/15 pmol and QD to Ab 120 pmol/24 pmol to 120 pmol/1.2 pmol). It was observed that a specific \"optimum\" ratio of the three reactants was required to produce the most fluorescent and biologically active product and that it was generated at alkaline pH 10.8. Increasing the ratio of Ab to QD produced conjugate which was less fluorescent while reducing the ratio of EDC to QD in the activation step led to increased fluorescence of product. Conjugates were tested for their possession of antibody by measurement of their absorption at OD(280 nm) and for their fluorescence by assay λ(max(em)) at 495 nm. A quantitative assay of the bioactivity of the conjugates was developed whereby a standardized amount of Cdc8 antigen was spotted onto nylon membranes and reacted with products from conjugation reactions in a sandwich-type colormetric assay The \"best\" conjugate was used in intracellular imaging of yeast Cdc8 protein and produced brighter, higher definition images of fixed yeast cell actin structure than a fluorescein-Ab conjugate routinely produced in our laboratory. The QD-Ab conjugate was also significantly more resistant to photobleaching than the fluorescein-Ab conjugate. Results from other experiments involving EDC, the water-soluble carbodiimide 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulphonate (CMC), and EDC.HCl have suggested a new reaction mechanism for EDC coupling under basic aqueous conditions. In summary, a robust understanding of commercial QD-COOH surface chemistry and the variables involved in the materials' efficient conjugation with a bioligand using carbidiimide has been obtained along with an optimized approach for Ab-QD conjugate production. A novel assay has been developed for bioassay of QD-Ab conjugates and a new mechanism for EDC coupling under basic aqueous conditions is proposed.","doi":"10.1021/la203273p","authors":"East DA, Mulvihill DP, Todd M, Bruce IJ","authors_abbrev":"East DA et al.","pubmed_publication_date":"15 Nov 2011","pubmed_entrez_date":"2011-10-06","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12606573","title":"Function of Cdc2p-dependent Bub1p phosphorylation and Bub1p kinase activity in the mitotic and meiotic spindle checkpoint.","citation":"EMBO J 2003 Mar 03;22(5):1075-87","abstract":"Cdc2p is a cyclin-dependent kinase (CDK) essential for both mitotic and meiotic cell cycle progression in fission yeast. We have found that the spindle checkpoint kinase Bub1p becomes phosphorylated by Cdc2p during spindle damage in mitotic cells. Cdc2p directly phosphorylates Bub1p in vitro at the CDK consensus sites. A Bub1p mutant that cannot be phosphorylated by Cdc2p is checkpoint defective, indicating that Cdc2p-dependent Bub1p phosphorylation is required to activate the checkpoint after spindle damage. The kinase activity of Bub1p is required, but is not sufficient, for complete spindle checkpoint function. The role of Bub1p in maintaining centromeric localization of Rec8p during meiosis I is entirely dependent upon its kinase activity, suggesting that Bub1p kinase activity is essential for establishing proper kinetochore function. Finally, we show that there is a Bub1p-dependent meiotic checkpoint, which is activated in recombination mutants.","authors":"Yamaguchi S, Decottignies A, Nurse P","authors_abbrev":"Yamaguchi S et al.","pubmed_publication_date":"03 Mar 2003","pubmed_entrez_date":"2003-02-28","publication_year":"2003","canto_session_key":"a07f7b8bc158c1e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-09-29 10:16:56","canto_approved_date":"2025-09-03 14:00:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-22 14:47:23","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPBC20F10.06","SPBC11B10.09","SPCC1753.03c","SPCC1322.12c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2021-09-29"},{"uniquename":"PMID:37849458","title":"Peptide Variant Detection by a Living Yeast Biosensor via an Epitope-Selective Protease.","citation":"Biodes Res 2023;5:0003","abstract":"We previously demonstrated that we could hijack the fungal pheromone signaling pathway to provide a living yeast biosensor where peptide biomarkers were recognized by G-protein-coupled receptors and engineered to transcribe a readout. Here, we demonstrated that the protease could be reintroduced to the biosensor to provide a simple mechanism for distinguishing single-amino-acid changes in peptide ligands that, otherwise, would likely be difficult to detect using binding-based assays. We characterized the dose-response curves for five fungal pheromone G-protein-coupled receptors, peptides, and proteases -Saccharomyces cerevisiae ,  Candida albicans ,  Schizosaccharomyces pombe ,  Schizosaccharomyces octosporus , and  Schizosaccharomyces japonicus . Alanine scanning was carried out for the most selective of these- S. cerevisiae  and  C. albicans -with and without the protease. Two peptide variants were discovered, which showed diminished cleavage by the protease (CaPep2A and CaPep2A13A). Those peptides were then distinguished by utilizing the biosensor strains with and without the protease, which selectively cleaved and altered the apparent concentration of peptide required for half-maximal activation for 2 peptides-CaPep and CaPep13A, respectively-by more than one order of magnitude. These results support the hypothesis that the living yeast biosensor with a sequence-specific protease can translate single-amino-acid changes into more than one order of magnitude apparent shift in the concentration of peptide required for half-maximal activation. With further engineering by computational modeling and directed evolution, the biosensor could likely distinguish a wide variety of peptide sequences beyond the alanine scanning carried out here. In the future, we envision incorporating proteases into our living yeast biosensor for use as a point of care diagnostic, a scalable communication language, and other applications.","doi":"10.34133/bdr.0003","authors":"Crnković T, Bokor BJ, Lockwood ME, Cornish VW","authors_abbrev":"Crnković T et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-10-18","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-10-18 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7772375","title":"A practical method for fission yeast transformation by electroporation.","citation":"Jpn J Genet 1995 Feb;70(1):1-6","abstract":"High-voltage shock within a very short duration under the proper conditions causes cells to incorporate exogenous macromolecules. This technique, electroporation, has been widely used in recent years to transform many organisms. We determined optimum conditions for fission yeast transformation using this method. Of nineteen combinations of electric field strength and pulse time examined, 1.75 kV/0.2 cm, 4 msec pulse was found to provide approximately 4.0 x 10(5) transformants per micrograms of DNA. Other factors responsible for the transformation efficiency in fission yeast are also discussed.","authors":"Ishiguro J, Kobayashi W","authors_abbrev":"Ishiguro J et al.","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11016957","title":"Lineage-specific loss and divergence of functionally linked genes in eukaryotes.","citation":"Proc Natl Acad Sci U S A 2000 Oct 10;97(21):11319-24","abstract":"By comparing 4,344 protein sequences from fission yeast Schizosaccharomyces pombe with all available eukaryotic sequences, we identified those genes that are conserved in S. pombe and nonfungal eukaryotes but are missing or highly diverged in the baker's yeast Saccharomyces cerevisiae. Since the radiation from the common ancestor with S. pombe, S. cerevisiae appears to have lost about 300 genes, and about 300 more genes have diverged by far beyond expectation. The most notable feature of the set of genes lost in S. cerevisiae is the coelimination of functionally connected groups of proteins, such as the signalosome and the spliceosome components. We predict similar coelimination of the components of the posttranscriptional gene-silencing system that includes the recently identified RNA-dependent RNA polymerase. Because one of the functions of posttranscriptional silencing appears to be \"taming\" of retrotransposons, the loss of this system in yeast could have triggered massive retrotransposition, resulting in elimination of introns and subsequent loss of spliceosome components that become dispensable. As the genome database grows, systematic analysis of coordinated gene loss may become a general approach for predicting new components of functional systems or even defining previously unknown functional complexes.","authors":"Aravind L, Watanabe H, Lipman DJ, Koonin EV","authors_abbrev":"Aravind L et al.","pubmed_publication_date":"10 Oct 2000","pubmed_entrez_date":"2000-10-04","publication_year":"2000","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21193357","title":"Schizosaccharomyces pombe encodes a mutated AP endonuclease 1.","citation":"DNA Repair (Amst) 2011 Mar 07;10(3):296-305","abstract":"Mutagenic and cytotoxic apurinic/apyrimidinic (AP) sites are among the most frequent lesions in DNA. Repair of AP sites is initiated by AP endonucleases and most organisms possess two or more of these enzymes. Saccharomyces cerevisiae has AP endonuclease 1 (Apn1) as the major enzymatic activity with AP endonuclease 2 (Apn2) being an important backup. Schizosaccharomyces pombe also encodes two potential AP endonucleases, and Apn2 has been found to be the main repair activity, while Apn1 has no, or only a limited role in AP site repair. Here we have identified a new 5' exon (exon 1) in the apn1 gene and show that the inactivity of S. pombe Apn1 is due to a nonsense mutation in the fifth codon of this new exon. Reversion of this mutation restored the AP endonuclease activity of S. pombe Apn1. Interestingly, the apn1 nonsense mutation was only found in laboratory strains derived from L972 h(-) and not in unrelated isolates of S. pombe. Since all S. pombe laboratory strains originate from L972 h(-), it appears that all experiments involving S. pombe have been conducted in an apn1(-) mutant strain with a corresponding DNA repair deficiency. These observations have implications both for future research in S. pombe and for the interpretation of previously conducted epistatis analysis.","doi":"10.1016/j.dnarep.2010.11.014","authors":"Laerdahl JK, Korvald H, Nilsen L, Dahl-Michelsen K, Rognes T, Bjørås M, Alseth I","authors_abbrev":"Laerdahl JK et al.","pubmed_publication_date":"07 Mar 2011","pubmed_entrez_date":"2011-01-04","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.17"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:16751097","title":"A role for TFIIIC transcription factor complex in genome organization.","citation":"Cell 2006 Jun 02;125(5):859-72","abstract":"Eukaryotic genome complexity necessitates boundary and insulator elements to partition genomic content into distinct domains. We show that inverted repeat (IR) boundary elements flanking the fission yeast mating-type heterochromatin domain contain B-box sequences, which prevent heterochromatin from spreading into neighboring euchromatic regions by recruiting transcription factor TFIIIC complex without RNA polymerase III (Pol III). Genome-wide analysis reveals TFIIIC with Pol III at all tRNA genes, many of which cluster at pericentromeric heterochromatin domain boundaries. However, a single tRNA(phe) gene with modest TFIIIC enrichment is insufficient to serve as boundary and requires RNAi-associated element to restrain heterochromatin spreading. Remarkably, we found TFIIIC localization without Pol III at many sites located between divergent promoters. These sites appear to act as chromosome-organizing clamps by tethering distant loci to the nuclear periphery, at which TFIIIC is concentrated into several distinct bodies. Our analyses uncover a general genome organization mechanism involving conserved TFIIIC complex.","authors":"Noma K, Cam HP, Maraia RJ, Grewal SI","authors_abbrev":"Noma K et al.","pubmed_publication_date":"02 Jun 2006","pubmed_entrez_date":"2006-06-06","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.07","SPBC21H7.05","SPCC16C4.14c","SPAC6F12.11c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:31122217","title":"Pivoting of microtubules driven by minus-end-directed motors leads to spindle assembly.","citation":"BMC Biol 2019 May 23;17(1):42","abstract":"At the beginning of mitosis, the cell forms a spindle made of microtubules and associated proteins to segregate chromosomes. An important part of spindle architecture is a set of antiparallel microtubule bundles connecting the spindle poles. A key question is how microtubules extending at arbitrary angles form an antiparallel interpolar bundle.\nHere, we show in fission yeast that microtubules meet at an oblique angle and subsequently rotate into antiparallel alignment. Our live-cell imaging approach provides a direct observation of interpolar bundle formation. By combining experiments with theory, we show that microtubules from each pole search for those from the opposite pole by performing random angular movement. Upon contact, two microtubules slide sideways along each other in a directed manner towards the antiparallel configuration. We introduce the contour length of microtubules as a measure of activity of motors that drive microtubule sliding, which we used together with observation of Cut7/kinesin-5 motors and our theory to reveal the minus-end-directed motility of this motor in vivo.\nRandom rotational motion helps microtubules from the opposite poles to find each other and subsequent accumulation of motors allows them to generate forces that drive interpolar bundle formation.","doi":"10.1186/s12915-019-0656-2","authors":"Winters L, Ban I, Prelogović M, Kalinina I, Pavin N, Tolić IM","authors_abbrev":"Winters L et al.","pubmed_publication_date":"23 May 2019","pubmed_entrez_date":"2019-05-25","publication_year":"2019","canto_session_key":"c7afc1150604bd08","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-05-29 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30230460","title":"[The TOR SAGA to the rescue of starved yeast cells].","citation":"Med Sci (Paris) 2018;34(8-9):645-648","abstract":"","doi":"10.1051/medsci/20183408005","authors":"Laboucarié T, Helmlinger D","authors_abbrev":"Laboucarié T et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-09-20","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25957277","title":"Intrinsic Toxicity of Unchecked Heterochromatin Spread Is Suppressed by Redundant Chromatin Boundary Functions in Schizosacchromyces pombe.","citation":"G3 (Bethesda) 2015 May 08;5(7):1453-61","abstract":"Effective boundary mechanisms halt the spread of repressive histone methylation. In the fission yeast Schizosacchromyces pombe, two factors/elements required for boundary function have been described, the jmjC protein Epe1 and binding sites for the RNA polymerase III transcription factor TFIIIC. Perplexingly, individual mutation of Epe1 or TFIIIC sites produces only mild boundary defects, and no other boundary factors have been identified. To approach these issues, we developed a synthetic reporter gene tool that uses a tethered Clr4 histone H3K9 methyltransferase and monitors the ability of a DNA element to block heterochromatin spread. The inverted repeat (IR) that flanks the mat2/3 silent mating-type cassette region demonstrates strong boundary activity compared to sequences that flank pericentromeric heterochromatic repeats. Rather than acting in the same inhibitory pathway, Epe1 and TFIIIC sites mediate boundary function of the IR via the two parallel and largely redundant pathways. We also use the system to demonstrate that HP1/Swi6 promotes boundary activity in addition to promoting silencing and acts in the same pathway as Epe1. Inhibition of heterochromatin spread at the endogenous IR element also requires either Epe1 or TFIIIC sites. Strikingly, mutation of both mechanisms results in growth inhibition that is associated with the spread of heterochromatin over many kilobases to the nearest essential gene and the near-complete silencing of several intervening euchromatic genes. The growth defect is reversed by deletion of clr4+, indicating that the redundant boundary mechanisms protect cells from intrinsic toxicity caused by the spread of heterochromatin.","doi":"10.1534/g3.115.018663","authors":"Garcia JF, Al-Sady B, Madhani HD","authors_abbrev":"Garcia JF et al.","pubmed_publication_date":"08 May 2015","pubmed_entrez_date":"2015-05-10","publication_year":"2015","canto_session_key":"01ffe8e938bbe70d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-05-11 00:19:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.16c","SPBC428.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12672592","title":"Differential malic acid degradation by selected strains of Saccharomyces during alcoholic fermentation.","citation":"Int J Food Microbiol 2003 May 25;83(1):49-61","abstract":"To produce a high-quality wine, it is important to obtain a fine balance between the various chemical constituents, especially between the sugar and acid content. The latter is more difficult to achieve in wines that have high acidity due to excess malic acid, since wine yeast in general cannot effectively degrade malic acid during alcoholic fermentation. An indigenous Saccharomyces paradoxus strain RO88 was able to degrade 38% of the malic acid in Chardonnay must and produced a wine of good quality. In comparison, Schizosaccharomyces pombe strain F effectively removed 90% of the malic acid, but did not produce a good-quality wine. Although commercially promoted as a malic-acid-degrading wine yeast strain, only 18% of the malic acid was degraded by Saccharomyces cerevisiae Lalvin strain 71B. Preliminary studies on the transcriptional regulation of the malic enzyme gene from three Saccharomyces strains, i.e. S. paradoxus RO88, S. cerevisiae 71B and Saccharomyces bayanus EC1118, were undertaken to elucidate the differences in their ability to degrade malic acid. Expression of the malic enzyme gene from S. paradoxus RO88 and S. cerevisiae 71B increased towards the end of fermentation once glucose was depleted, whereas no increase in transcription was observed for S. bayanus EC1118 which was also unable to effectively degrade malic acid.","authors":"Redzepovic S, Orlic S, Majdak A, Kozina B, Volschenk H, Viljoen-Bloom M","authors_abbrev":"Redzepovic S et al.","pubmed_publication_date":"25 May 2003","pubmed_entrez_date":"2003-04-04","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21494755","title":"Biotechnological production of 20-alpha-dihydrodydrogesterone at pilot scale.","citation":"Appl Biochem Biotechnol 2011 Sep;165(1):190-203","abstract":"The human sex hormone progesterone plays an essential and complex role in a number of physiological processes. Progesterone deficiency is associated with menstrual disorders and infertility as well as premature birth and abortion. For progesterone replacement therapy, the synthetic progestogen dydrogesterone is commonly used. In the body, this drug is metabolized to 20α-dihydrodydrogesterone (20α-DHD), which also shows extensive pharmacological effects and hence could act as a therapeutic agent itself. In this study, we describe an efficient biotechnological production procedure for 20α-DHD that employs the stereo- and regioselective reduction of dydrogesterone in a whole-cell biotransformation process based on recombinant fission yeast cells expressing the human enzyme AKR1C1 (20α-hydroxysteroid dehydrogenase, 20α-HSD). In a fed-batch fermentation at pilot scale (70 L) with a genetically improved production strain and under optimized reaction conditions, an average 20α-DHD production rate of 190 μM day(-1) was determined for a total biotransformation time of 136 h. Combined with an effective and reliable downstream processing, a continuous production rate of 12.3 ± 1.4 g 20α-DHD per week and fermenter was achieved. We thus established an AKR-dependent whole-cell biotransformation process that can also be used for the production of other AKR1C1 substrates (as exemplarily shown by the production of 20α-dihydroprogesterone in gram scale) and is in principle suited for the production of further human AKR metabolites at industrial scale.","doi":"10.1007/s12010-011-9243-x","authors":"Naumann JM, Zöllner A, Drăgan CA, Messinger J, Adam J, Bureik M","authors_abbrev":"Naumann JM et al.","pubmed_publication_date":"Sep 2011","pubmed_entrez_date":"2011-04-16","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35854527","title":"Energetic constraints on filament-mediated cell polarization.","citation":"Phys Rev E 2022 Jun;105(6-1):064406","abstract":"Cell polarization underlies many cellular processes, such as differentiation, migration, and budding. Many living cells, such as budding yeast and fission yeast, use cytoskeletal structures to actively transport proteins to one location on the membrane and create a high-density spot of membrane-bound proteins. Yet, the thermodynamic constraints on filament-based cell polarization remain unknown. We show by mathematical modeling that cell polarization requires detailed balance to be broken, and we quantify the free-energy cost of maintaining a polarized state of the cell. Our study reveals that detailed balance cannot only be broken via the active transport of proteins along filaments but also via a chemical modification cycle, allowing detailed balance to be broken by the shuttling of proteins between the filament, membrane, and cytosol. Our model thus shows that cell polarization can be established via two distinct driving mechanisms, one based on active transport and one based on nonequilibrium binding. Furthermore, the model predicts that the driven binding process dissipates orders of magnitude less free energy than the transport-based process to create the same membrane spot. Active transport along filaments may be sufficient to create a polarized distribution of membrane-bound proteins, but an additional chemical modification cycle of the proteins themselves is more efficient and less sensitive to the physical exclusion of proteins on the transporting filaments, providing insight in the design principles of the Pom1/Tea1/Tea4 system in fission yeast and the Cdc42 system in budding yeast.","doi":"10.1103/PhysRevE.105.064406","authors":"Wierenga H, Wolde PRT","authors_abbrev":"Wierenga H et al.","pubmed_publication_date":"Jun 2022","pubmed_entrez_date":"2022-07-20","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-07-23 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12952871","title":"Retrotransposons and their recognition of pol II promoters: a comprehensive survey of the transposable elements from the complete genome sequence of Schizosaccharomyces pombe.","citation":"Genome Res 2003 Sep;13(9):1984-97","abstract":"The complete DNA sequence of the genome of Schizosaccharomyces pombe provides the opportunity to investigate the entire complement of transposable elements (TEs), their association with specific sequences, their chromosomal distribution, and their evolution. Using homology-based sequence identification, we found that the sequenced strain of S. pombe contained only one family of full-length transposons. This family, Tf2, consisted of 13 full-length copies of a long terminal repeat (LTR) retrotransposon. We found that LTR-LTR recombination of previously existing transposons had resulted in extensive populations of solo LTRs. These included 35 solo LTRs of Tf2, as well as 139 solo LTRs from other Tf families. Phylogenetic analysis of solo Tf LTRs reveals that Tf1 and Tf2 were the most recently active elements within the genome. The solo LTRs also served as footprints for previous insertion events by the Tf retrotransposons. Analysis of 186 genomic insertion events revealed a close association with RNA polymerase II promoters. These insertions clustered in the promoter-proximal regions of genes, upstream of protein coding regions by 100 to 400 nucleotides. The association of Tf insertions with pol II promoters was very similar to the preference previously observed for Tf1 integration. We found that the recently active Tf elements were absent from centromeres and pericentromeric regions of the genome containing tandem tRNA gene clusters. In addition, our analysis revealed that chromosome III has twice the density of insertion events compared to the other two chromosomes. Finally we describe a novel repetitive sequence, wtf, which was also preferentially located on chromosome III, and was often located near solo LTRs of Tf elements.","authors":"Bowen NJ, Jordan IK, Epstein JA, Wood V, Levin HL","authors_abbrev":"Bowen NJ et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-09-04","publication_year":"2003","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1289.17","SPCC548.02c","SPBC1706.02c","SPCC663.02","SPCC663.17","SPAC13D1.01c","SPAC27E2.08","SPCC1739.15","SPAPB15E9.03c","SPCC306.10","SPCC548.03c","SPCC1494.11c","SPCC1450.08c","SPAC26A3.13c","SPCC576.16c","SPCC1906.04","SPBC9B6.02c","SPCC1183.10","SPAC9.04","SPCC285.06c","SPBC1E8.04","SPCC794.02","SPCC1919.06c","SPCC830.02","SPCC1906.03","SPAC2E12.05","SPCC970.11c","SPAC2E1P3.03c","SPCC622.21","SPCC1281.08","SPCC1620.02","SPAC19D5.09c","SPCC285.07c","SPCC736.05","SPCC162.04c","SPAC167.08","SPCC1020.14"],"gene_count":37,"ltp_gene_count":0},{"uniquename":"PMID:1905818","title":"Isolation and characterization of a gene encoding a G-protein alpha subunit from Schizosaccharomyces pombe: involvement in mating and sporulation pathways.","citation":"Proc Natl Acad Sci U S A 1991 Jul 01;88(13):5877-81","abstract":"The gpal gene of Schizosaccharomyces pombe, which encodes a protein homologous with the alpha subunits of mammalian guanine nucleotide-binding proteins (G proteins), was isolated by cross-hybridization using rat Gi1 alpha and Gx alpha cDNA. The deduced amino acid sequence was about 37% identical with rat Gi1 alpha and Gx alpha proteins and contained three conserved motifs commonly found in all GTP-binding proteins. Disruption of gpa1 was not lethal but conferred sterility and sporulation deficiency on Sch. pombe cells. Thus, the gene is essential for the sexual development and is probably coupled to mating-factor receptors. In contrast to Saccharomyces cerevisiae GPA1, which plays a negative role in mating-factor signal transduction, Sch. pombe gpa1+ apparently has a positive function. A gpa1 transcript of 2.2 kilobases was detected in vegetatively growing cells. A 1.6-kilobase gpa1 transcript appeared in addition to the 2.2-kilobase transcript when cells were derepressed for mating or meiosis.","authors":"Obara T, Nakafuku M, Yamamoto M, Kaziro Y","authors_abbrev":"Obara T et al.","pubmed_publication_date":"01 Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_session_key":"e81eaddcfa17ed1c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-14 21:22:12","canto_approved_date":"2026-04-10 19:48:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-10 13:26:16","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC24C6.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-14"},{"uniquename":"PMID:16348060","title":"Relationships among Cell Size, Membrane Permeability, and Preservative Resistance in Yeast Species.","citation":"Appl Environ Microbiol 1989 Nov;55(11):2995-9","abstract":"The rate of uptake of propanoic acid and the cell dimensions were measured for 23 yeasts differing in their resistance to weak-acid-type preservatives. Relationships between reciprocal uptake rate, reciprocal permeability, cell volume, cell area, volume/area, and the MICs of benzoic acid and propanoic acid for the yeasts were tested by correlation analysis on pairs of parameters. The MIC of methylparaben, which is not a weak-acid-type preservative, was included. The most significant relationships found were between both reciprocal uptake rate and reciprocal permeability and the MICs of propanoic and benzoic acids Cell volume, area, and volume/area were each individually correlated with propanoic and benzoic acid MICs, but less strongly. In multiple regression analyses, inclusion of terms for volume, area, or volume/area did not markedly increase the significance. The MIC of methylparaben was unrelated to the uptake and permeability parameters, but did show a correlation with cell volume/area. Schizosaccharomyces pombe was anomalous in having very low permeability. Exclusion of these outlying data revealed particularly strong relationships (P < 0.001) between both reciprocal uptake rate and reciprocal permeability and the benzoic acid MIC. MICs for Zygosaccharomyces bailii isolates were substantially higher than for the other species, and therefore Z. baillii isolates had a large influence on the regressions. However, the relationships observed remained significant even after removal of the Z. bailii data. In showing a correlation between the rate at which propanoic acid enters yeast cells and the ability of the cells to tolerate this and other weak-acid-type preservatives, but not methylparaben, the results suggest that the resistance mechanism, in which preservative is continuously removed from the cell, is a common and major determinant of the preservative tolerance of yeast species.","authors":"Warth AD","authors_abbrev":"Warth AD","pubmed_publication_date":"Nov 1989","pubmed_entrez_date":"1989-11-01","publication_year":"1989","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010565","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1314161","title":"Complementation of the cs dis2-11 cell cycle mutant of Schizosaccharomyces pombe by a protein phosphatase from Arabidopsis thaliana.","citation":"EMBO J 1992 Apr;11(4):1327-33","abstract":"The activities of type I protein phosphatases play a central role in eukaryotic cell cycle control. Here, we report the cloning and characterization from the flowering plant Arabidopsis thaliana of a cDNA clone named PP1-At which is highly homologous to protein phosphatase 1. The deduced amino acid sequence of PP1-At shows that the PP1-At protein is 318 amino acid residues long and has a molecular weight of 35,298 Da. The PP1-At protein has strong similarity to all other known protein phosphatase type 1 catalytic subunits. Approximately 62% of the amino acids are identical to type 1 protein phosphatases of rabbit, mouse, Saccharomyces cerevisiae and Schizosaccharomyces pombe. RNA blot analysis revealed a single mRNA species of approximately the same size as the cDNA isolated. The PP1-At-encoded mRNA of 1.3 kb is abundant in most vegetative Arabidopsis tissues, with the lowest level of expression in leaves. When transferred to the fission yeast S.pombe, the PP1-At-encoded protein can rescue a semidominant mutant, cold sensitive (cs) dis2-11, which under nonpermissive conditions is unable to complete chromosome disjunction.","authors":"Nitschke K, Fleig U, Schell J, Palme K","authors_abbrev":"Nitschke K et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"d2ea3c4fc4a0899d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-04-12 14:44:18","canto_session_submitted_date":"2012-03-03 11:46:20","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:672899","title":"Orientation of \"plus\" genes at the mating-typing locus in homothallic fission yeast.","citation":"Mol Gen Genet 1978 May 31;161(3):305-9","abstract":"Results of four crosses are presented which indicate that, in Schizosaccharomyces pombe the plus segment of the mating-typing locus is regulated from a central position, in between of the plus and the minus segment. This conclusion is based on the mapping of a plus-restraining entity r, which is revealed by recombination in certain crosses, or by mutation to unstabe negative strains. To this end, a meiosis-defective mating-type mutation was used as a marker for the plus segment, by taking advantage of its suppressibility by a nonsense suppressor. This suppressibility was substanitated by an additional cross.","authors":"Egal R","authors_abbrev":"Egal R","pubmed_publication_date":"31 May 1978","pubmed_entrez_date":"1978-05-31","publication_year":"1978","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10087920","title":"PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization.","citation":"Trends Biochem Sci 1999 Jan;24(1):34-6","abstract":"","authors":"Nakai K, Horton P","authors_abbrev":"Nakai K et al.","pubmed_publication_date":"Jan 1999","pubmed_entrez_date":"1999-03-24","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:10:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12833058","title":"Recasting meiotic cohesion.","citation":"Nat Cell Biol 2003 Jul;5(7):591","abstract":"","authors":"McDonald D","authors_abbrev":"McDonald D","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-07-02","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8223497","title":"Novel gene expression mechanism in a fission yeast retroelement: Tf1 proteins are derived from a single primary translation product.","citation":"EMBO J 1993 Dec;12(12):4885-95","abstract":"In sharp contrast to the single ORF of the Schizosaccharomyces pombe retrotransposon Tf1, retroviruses and most retrotransposons employ two different ORFs to separately encode the Gag and Pol proteins. The different ORFs are thought to allow for overexpression of the Gag protein relative to Pol protein presumed necessary for the assembly of functional retrovirus particles and virus-like particles (VLPs). The results of in vivo experiments designed to detect the transposition of Tf1 show that Tf1 is indeed active and can insert itself into the host genome via a true retrotransposition process. Thus, a paradox emerged between the lack of any obvious means of overexpressing Tf1 Gag protein and the demonstrated functionality of the element. Epitope tagging experiments described here confirm that the Tf1 large ORF is intact and that there is no translational or transcriptional mechanism used to overexpress the Tf1 Gag protein. In addition, we used sucrose gradients and antisera specific for Tf1 capsid (CA) and integrase (IN) to show that the Tf1 proteins do assemble into uniform populations of macromolecular particles that also cosediment with Tf1 reverse transcription products. This evidence suggests that Tf1 proteins form VLPs without using the previously described mechanisms that retroviruses and retrotransposons require to overexpress Gag proteins.","authors":"Levin HL, Weaver DC, Boeke JD","authors_abbrev":"Levin HL et al.","pubmed_publication_date":"Dec 1993","pubmed_entrez_date":"1993-12-01","publication_year":"1993","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33109728","title":"High-Throughput Identification of Nuclear Envelope Protein Interactions in  Schizosaccharomyces pombe  Using an Arrayed Membrane Yeast-Two Hybrid Library.","citation":"G3 (Bethesda) 2020 Dec 03;10(12):4649-4663","abstract":"The nuclear envelope (NE) contains a specialized set of integral membrane proteins that maintain nuclear shape and integrity and influence chromatin organization and gene expression. Advances in proteomics techniques and studies in model organisms have identified hundreds of proteins that localize to the NE. However, the function of many of these proteins at the NE remains unclear, in part due to a lack of understanding of the interactions that these proteins participate in at the NE membrane. To assist in the characterization of NE transmembrane protein interactions we developed an arrayed library of integral and peripheral membrane proteins from the fission yeast  Schizosaccharomyces pombe  for high-throughput screening using the split-ubiquitin based membrane yeast two -hybrid system. We used this approach to characterize protein interactions for three conserved proteins that localize to the inner nuclear membrane: Cut11/Ndc1, Lem2 and Ima1/Samp1/Net5. Additionally, we determined how the interaction network for Cut11 is altered in canonical temperature-sensitive  cut11-ts  mutants. This library and screening approach is readily applicable to characterizing the interactomes of integral membrane proteins localizing to various subcellular compartments.","doi":"10.1534/g3.120.401880","authors":"Varberg JM, Gardner JM, McCroskey S, Saravanan S, Bradford WD, Jaspersen SL","authors_abbrev":"Varberg JM et al.","pubmed_publication_date":"03 Dec 2020","pubmed_entrez_date":"2020-10-28","publication_year":"2020","canto_session_key":"e9763156a337dd76","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-06-27 15:31:44","canto_approved_date":"2022-07-14 09:12:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-06-27 15:31:37","canto_added_date":"2020-10-30 01:15:05","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":15,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.10","SPBC36B7.03","SPCC1235.16","SPAC1687.17c","SPAPJ695.01c","SPAC15A10.01","SPAC6G10.04c","SPAC18B11.08c","SPBC354.02c","SPAC7D4.09c","SPAC2E1P5.03","SPBC19C7.11","SPBPB2B2.01","SPCC794.06","SPBC19C7.10","SPAPYUK71.03c","SPBC530.09c","SPAC4F10.18","SPBC3H7.01","SPAC29B12.14c","SPAC212.12","SPAC23A1.05","SPBC1778.08c","SPBC409.20c","SPCC970.03","SPBC31F10.06c","SPBC3H7.02","SPAC7D4.14c","SPAC23A1.02c","SPAC24C9.08","SPAPB8E5.04c","SPBC56F2.10c","SPAC2E1P3.02c","SPBC776.03","SPBC776.14","SPBC354.04","SPCC1235.06","SPAC926.07c","SPCC1281.03c","SPCC74.04","SPBC887.16","SPCC825.03c","SPBC1289.13c","SPAC2C4.05","SPBC1604.08c","SPBC713.08","SPAC1039.09","SPBC887.17","SPAC1002.16c","SPBC3B9.21","SPAC22E12.06c","SPAC869.10c","SPBC3B8.04c","SPAC13A11.02c","SPAC824.08","SPBC25H2.06c","SPCC830.08c","SPBC3H7.09","SPBC12D12.08c","SPBC16G5.05c","SPBC11B10.01","SPCC1020.05","SPAC24B11.08c","SPCC16C4.01","SPAC4F10.10c","SPCC1682.06","SPAC9E9.04","SPAC1782.12c","SPBC1734.09","SPAC31A2.13c","SPBC21C3.17c","SPBC337.05c","SPAC20H4.02","SPBC646.05c","SPBPB2B2.16c","SPAC3A11.04","SPCC16A11.06c","SPAC750.07c","SPCC553.05c","SPBC354.09c","SPCC622.04","SPBC776.05","SPCC777.07","SPAC6F12.04","SPAC10F6.05c","SPBC36.01c","SPBC29A10.16c","SPAC12B10.02c","SPBC18A7.01","SPCC757.05c","SPCC1235.08c","SPAC1039.04","SPCC1739.04c","SPAC14C4.11","SPAC23C11.11","SPAC17C9.12","SPBPB10D8.01","SPCC338.18","SPAC7D4.12c","SPCC576.07","SPAC6F12.08c","SPBC887.15c","SPBC16H5.04","SPAC13C5.01c","SPAC22F8.06","SPCC16A11.04","SPAC23C4.13","SPAC3H8.06","SPCC1827.07c","SPAC2F3.08","SPAC15E1.02c","SPAC19G12.15c","SPAC27E2.11c","SPAC14C4.07","SPBC16C6.07c","SPCC553.06","SPAC637.06","SPBC17A3.05c","SPBC4.01","SPAC1A6.09c","SPAC56E4.06c","SPAC227.10","SPBC530.16","SPAC1B3.07c","SPAC1782.02c","SPCC4B3.02c","SPAC688.16","SPCC737.05","SPAPB1E7.09","SPAC1039.01","SPAC56E4.05","SPAC823.05c","SPBC20F10.07","SPAC3F10.02c","SPBC1271.10c","SPCC306.11","SPBC31A8.01c","SPBC16E9.14c","SPAP8A3.08","SPCC1235.15","SPAC589.04","SPBC1539.04","SPAC22F8.02c","SPBC14F5.13c","SPBC23G7.13c","SPAC1399.01c","SPAC977.06","SPBC839.11c","SPBC1D7.01","SPBC8D2.17","SPCC191.04c","SPCC63.12c","SPAC18G6.10","SPBC3E7.06c","SPCC16A11.10c","SPBC713.12","SPAC22A12.15c","SPBC1271.08c","SPCC1682.11c","SPBC1718.05","SPAC22F8.04","SPAC23H4.18c","SPBC725.10","SPCC622.01c","SPBC4B4.08","SPCC663.02","SPBC30B4.09","SPBC1271.06c","SPAC56F8.07","SPBC1348.05","SPBC646.16","SPBC365.08c","SPAC2E1P5.02c","SPAC4G9.14","SPAC17A2.14","SPAC5H10.12c","SPCC757.10","SPAC17G6.07c","SPAC3A11.10c","SPBC1677.02","SPAC2F3.07c","SPBC106.16","SPCC645.11c","SPAC630.11","SPAC4D7.11","SPBC119.16c","SPBC21B10.04c","SPBC36B7.07","SPAC7D4.15c","SPCC330.12c","SPBC887.12","SPBC21B10.11","SPCC417.10","SPCC320.05","SPBC28F2.08c","SPAC1805.08","SPAC4F8.01","SPCC1281.06c","SPAC1687.07","SPBC29B5.02c","SPBC1921.06c","SPBC29A10.07","SPAC4G9.13c","SPCC895.04c","SPBC839.06","SPBC16G5.18","SPBC3E7.15c","SPAC1786.03","SPAC227.06","SPBC25H2.14","SPAC2F3.18c","SPAC1687.02","SPAC922.09","SPAC1B3.14","SPBC902.03","SPBC365.02c","SPBC2A9.08c","SPAC664.09","SPAC17A2.02c","SPCC1450.15","SPCC4G3.11","SPAC1002.02","SPCC61.04c","SPCC794.03","SPAC19A8.09","SPAC664.14","SPBC23G7.16","SPAC1527.02","SPAC4C5.03","SPAC521.04c","SPAC823.07","SPAC977.01","SPBC119.09c","SPAC688.12c","SPAC1B3.16c","SPBC12D12.01","SPBC2G2.03c","SPAC3G6.05","SPAC750.02c","SPAC14C4.10c","SPBC27B12.12c","SPAC926.03","SPBC29A10.01","SPAC343.21","SPBC530.12c","SPBC660.17c","SPBC887.22","SPCC1235.13","SPCC4B3.13","SPCC790.03","SPCC794.04c","SPACUNK4.08","SPAC23C11.01","SPBC21B10.07","SPBC3B9.10","SPBC12C2.13c","SPAC4G8.10","SPAC1952.13","SPAC9.08c","SPCC1672.11c","SPCC1442.06","SPCC63.02c","SPCPB1C11.01","SPCC417.15","SPAC19G12.08","SPBC21B10.06c","SPCC1393.10","SPBC3B8.07c","SPCC622.02","SPAC21E11.08","SPCC736.04c","SPAC23A1.15c","SPAC1071.04c","SPAPB17E12.07c","SPBC4B4.06","SPBC409.21","SPBC359.03c","SPAC20G8.03","SPBC18H10.18c","SPAC2E1P5.04c","SPAC20G4.07c","SPBC3D6.05","SPAPB24D3.02c","SPAC10F6.12c","SPAC977.17","SPBC1348.03","SPBC23G7.06c","SPBC428.14","SPAC31G5.02","SPAC22E12.01","SPCC1322.14c","SPBC11B10.07c","SPCC1795.03","SPCC1795.12c","SPBC337.16","SPCC70.04c","SPCP1E11.05c","SPCP31B10.04","SPAC1399.03","SPAC1851.03","SPCC330.07c","SPAC25H1.07","SPAP14E8.05c","SPAC4D7.07c","SPBC713.11c","SPAC19E9.01c","SPBC19G7.19","SPAC3F10.10c","SPAC2F3.02","SPAC1786.01c","SPAC1006.05c","SPAC8F11.10c","SPAC9E9.14","SPBC16H5.09c","SPAC5H10.11","SPAC1A6.06c","SPBC19C7.05","SPBC2G5.04c","SPAC3H1.06c","SPAC1834.05","SPBC30D10.09c","SPBC31E1.02c","SPAC17G8.08c","SPAC1071.10c","SPAC1952.01","SPAC959.06c","SPBC1685.03","SPAC1142.05","SPBC32F12.01c","SPBC32H8.03","SPBC337.09","SPBC405.02c","SPBC543.05c","SPBC577.10","SPBC947.06c","SPCC1183.09c","SPBC3B8.06","SPAC57A10.07","SPCC970.06","SPAC17H9.14c","SPBC543.08","SPAC1486.02c","SPAC630.04c","SPCC1682.16","SPCC306.05c","SPBC19C2.15c","SPCC737.03c","SPBC3D6.13c","SPAC977.04","SPAC30D11.11","SPBC342.01c","SPBC215.15","SPAC17G6.09","SPCC1020.11c","SPCC1795.10c","SPAC22A12.13","SPAC3A12.03c","SPBC13G1.12","SPBC19F8.06c","SPBC1E8.03c","SPAC23H3.11c","SPCC63.10c","SPAC222.14c","SPAC1D4.08","SPBC409.05","SPCC1450.06c","SPAC13G7.05","SPCC1884.02","SPAPB24D3.10c","SPCC594.07c","SPBC16C6.09","SPAPB8E5.03","SPAC1687.08","SPBC12C2.09c","SPCC1620.05","SPCC330.20"],"gene_count":376,"ltp_gene_count":3,"approved_date":"2022-06-27"},{"uniquename":"PMID:34849791","title":"Perturbation of kinetochore function using GFP-binding protein in fission yeast.","citation":"G3 (Bethesda) 2021 Oct 19;11(11)","abstract":"Using genetic mutations to study protein functions in vivo is a central paradigm of modern biology. Single-domain camelid antibodies generated against GFP have been engineered as nanobodies or GFP-binding proteins (GBPs) that can bind GFP as well as some GFP variants with high affinity and selectivity. In this study, we have used GBP-mCherry fusion protein as a tool to perturb the natural functions of a few kinetochore proteins in the fission yeast Schizosaccharomyces pombe. We found that cells simultaneously expressing GBP-mCherry and the GFP-tagged inner kinetochore protein Cnp1 are sensitive to high temperature and microtubule drug thiabendazole (TBZ). In addition, kinetochore-targeted GBP-mCherry by a few major kinetochore proteins with GFP tags causes defects in faithful chromosome segregation. Thus, this setting compromises the functions of kinetochores and renders cells to behave like conditional mutants. Our study highlights the potential of using GBP as a general tool to perturb the function of some GFP-tagged proteins in vivo with the objective of understanding their functional relevance to certain physiological processes, not only in yeasts, but also potentially in other model systems.","doi":"10.1093/g3journal/jkab290","authors":"Deng DJ, Xia QC, Jia GS, Suo F, Chen JL, Sun L, Wang JQ, Wang SM, Du LL, Wang Y, Jin QW","authors_abbrev":"Deng DJ et al.","pubmed_publication_date":"19 Oct 2021","pubmed_entrez_date":"2021-12-01","publication_year":"2021","canto_session_key":"216f4dec12ef6153","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dajie Deng","canto_first_approved_date":"2022-04-10 17:06:43","canto_approved_date":"2023-03-23 13:26:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-04-07 11:29:31","canto_added_date":"2021-12-03 01:15:04","annotation_curators":[{"name":"Dajie Deng","community_curator":true,"annotation_count":144,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.05c","SPCC338.17c","SPAC1687.20c","SPCC1020.02","SPBC11C11.03","SPBC409.04c","SPBC1105.17","SPBC1861.01c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2022-04-10"},{"uniquename":"PMID:24506481","title":"FTY720 stimulated ROS generation and the Sty1/Atf1 signaling pathway in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Cells 2014 Apr;19(4):325-37","abstract":"Fingolimod hydrochloride (FTY720) is the first-in-class immune modulator known as sphingosine 1-phosphate (S1P) receptor agonists. FTY720 has also been reported to exert a variety of physiological functions such as antitumor effect, angiogenesis inhibition, and Ca2+ mobilization. Here, we show that FTY720 treatment induced reactive oxygen species (ROS) accumulation, and investigated the effect of FTY720 on the stress-activated MAP kinase Spc1/Sty1, a functional homologue of p38 MAPK, using a Renilla luciferase reporter construct fused to the CRE, which gives an accurate measure of the transcriptional activity of Atf1 and thus serves as a faithful readout of the Spc1/Sty1 MAPK signaling in response to oxidative stresses. FTY720 stimulated the CRE responses in a concentration-dependent manner, which was markedly reduced by deletion of the components of the Spc1/Sty1 MAPK pathway. The blockade of ROS production by NAC (N-acetyl-L-cysteine) significantly reversed the FTY720-induced ROS accumulation, subsequent activation of the Spc1/Sty1 MAPK pathway, and inhibition of cell proliferation. Cells lacking the components of the Spc1/Sty1 MAPK exhibited higher sensitivity to FTY720 and higher ROS levels upon FTY720 treatment than in wild-type cells. Thus, our results demonstrate the usefulness of fission yeast for elucidating the FTY720-mediated signaling pathways involving ROS.","doi":"10.1111/gtc.12134","authors":"Hagihara K, Mizukura A, Kitai Y, Yao M, Ishida K, Kita A, Kunoh T, Masuko T, Matzno S, Chiba K, Sugiura R","authors_abbrev":"Hagihara K et al.","pubmed_publication_date":"Apr 2014","pubmed_entrez_date":"2014-02-11","publication_year":"2014","canto_session_key":"3b2db8fb5912d221","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25869666","title":"Microtubule minus end motors kinesin-14 and dynein drive nuclear congression in parallel pathways.","citation":"J Cell Biol 2015 Apr 13;209(1):47-58","abstract":"Microtubules (MTs) and associated motors play a central role in nuclear migration, which is crucial for diverse biological functions including cell division, polarity, and sexual reproduction. In this paper, we report a dual mechanism underlying nuclear congression during fission yeast karyogamy upon mating of haploid cells. Using microfluidic chambers for long-term imaging, we captured the precise timing of nuclear congression and identified two minus end-directed motors operating in parallel in this process. Kinesin-14 Klp2 associated with MTs may cross-link and slide antiparallel MTs emanating from the two nuclei, whereas dynein accumulating at spindle pole bodies (SPBs) may pull MTs nucleated from the opposite SPB. Klp2-dependent nuclear congression proceeds at constant speed, whereas dynein accumulation results in an increase of nuclear velocity over time. Surprisingly, the light intermediate chain Dli1, but not dynactin, is required for this previously unknown function of dynein. We conclude that efficient nuclear congression depends on the cooperation of two minus end-directed motors.","doi":"10.1083/jcb.201409087","authors":"Scheffler K, Minnes R, Fraisier V, Paoletti A, Tran PT","authors_abbrev":"Scheffler K et al.","pubmed_publication_date":"13 Apr 2015","pubmed_entrez_date":"2015-04-15","publication_year":"2015","canto_session_key":"682763c91da26aea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-07-14 08:30:37","canto_approved_date":"2025-09-03 16:39:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-07-14 08:30:28","canto_added_date":"2015-04-16 00:19:04","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":20,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.10","SPAC1093.06c","SPBC646.17c","SPBC1604.20c","SPAC458.04c","SPAC18G6.15","SPAC27D7.13c","SPAC3A11.14c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2022-07-14"},{"uniquename":"PMID:17072881","title":"How to get the most from fission yeast genome data: a report from the 2006 European Fission Yeast Meeting computing workshop.","citation":"Yeast 2006 Oct 15;23(13):905-12","abstract":"A fission yeast computing workshop 'How to get the most from the fission yeast genome data' was run as a satellite to the European Fission Yeast Meeting. The broad aims of the workshop were to provide fission yeast bench biologists with a set of tools and protocols to query the fission yeast genome data in specific ways, in order to extract biologically meaningful information of interest, which can be tailored to the needs of individual research projects. A description of the workshop content is provided and a selection of the tools presented are reviewed.","authors":"Wood V","authors_abbrev":"Wood V","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30988468","title":"Unbiased screen of RNA tailing activities reveals a poly(UG) polymerase.","citation":"Nat Methods 2019 May;16(5):437-445","abstract":"Ribonucleotidyl transferases (rNTases) add untemplated ribonucleotides to diverse RNAs. We have developed TRAID-seq, a screening strategy in Saccharomyces cerevisiae to identify sequences added to a reporter RNA at single-nucleotide resolution by overexpressed candidate enzymes from different organisms. The rNTase activities of 22 previously unexplored enzymes were determined. In addition to poly(A)- and poly(U)-adding enzymes, we identified a cytidine-adding enzyme that is likely to be part of a two-enzyme system that adds CCA to tRNAs in a eukaryote; a nucleotidyl transferase that adds nucleotides to RNA without apparent nucleotide preference; and a poly(UG) polymerase, Caenorhabditis elegans MUT-2, that adds alternating uridine and guanosine nucleotides to form poly(UG) tails. MUT-2 is known to be required for certain forms of RNA silencing, and mutants of the enzyme that result in defective silencing did not add poly(UG) tails in our assay. We propose that MUT-2 poly(UG) polymerase activity is required to promote genome integrity and RNA silencing.","doi":"10.1038/s41592-019-0370-6","authors":"Preston MA, Porter DF, Chen F, Buter N, Lapointe CP, Keles S, Kimble J, Wickens M","authors_abbrev":"Preston MA et al.","pubmed_publication_date":"May 2019","pubmed_entrez_date":"2019-04-17","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1093.04c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"EMBL:SPD236","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23399914","title":"Increased expression of BIN1 mediates Alzheimer genetic risk by modulating tau pathology.","citation":"Mol Psychiatry 2013 Nov;18(11):1225-34","abstract":"Genome-wide association studies (GWAS) have identified a region upstream the BIN1 gene as the most important genetic susceptibility locus in Alzheimer's disease (AD) after APOE. We report that BIN1 transcript levels were increased in AD brains and identified a novel 3 bp insertion allele ∼28 kb upstream of BIN1, which increased (i) transcriptional activity in vitro, (ii) BIN1 expression levels in human brain and (iii) AD risk in three independent case-control cohorts (Meta-analysed Odds ratio of 1.20 (1.14-1.26) (P=3.8 × 10(-11))). Interestingly, decreased expression of the Drosophila BIN1 ortholog Amph suppressed Tau-mediated neurotoxicity in three different assays. Accordingly, Tau and BIN1 colocalized and interacted in human neuroblastoma cells and in mouse brain. Finally, the 3 bp insertion was associated with Tau but not Amyloid loads in AD brains. We propose that BIN1 mediates AD risk by modulating Tau pathology.","doi":"10.1038/mp.2013.1","authors":"Chapuis J, Hansmannel F, Gistelinck M, Mounier A, Van Cauwenberghe C, Kolen KV, Geller F, Sottejeau Y, Harold D, Dourlen P, Grenier-Boley B, Kamatani Y, Delepine B, Demiautte F, Zelenika D, Zommer N, Hamdane M, Bellenguez C, Dartigues JF, Hauw JJ, Letronne F, Ayral AM, Sleegers K, Schellens A, Broeck LV, Engelborghs S, De Deyn PP, Vandenberghe R, O'Donovan M, Owen M, Epelbaum J, Mercken M, Karran E, Bantscheff M, Drewes G, Joberty G, Campion D, Octave JN, Berr C, Lathrop M, Callaerts P, Mann D, Williams J, Buée L, Dewachter I, Van Broeckhoven C, Amouyel P, Moechars D, Dermaut B, Lambert JC, GERAD consortium","authors_abbrev":"Chapuis J et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-02-13","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16C6.06","SPBC21D10.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:19602414","title":"Cell-cycle control: don't supersize me.","citation":"Curr Biol 2009 Jul 14;19(13):R517-9","abstract":"Cells often grow to a certain cell size before entering mitosis and dividing. Two recent articles suggest that fission yeast cells sense their own size through the action of an intracellular gradient emanating from cell tips and a sensor at the cell middle.","doi":"10.1016/j.cub.2009.05.044","authors":"Pan KZ, Chang F","authors_abbrev":"Pan KZ et al.","pubmed_publication_date":"14 Jul 2009","pubmed_entrez_date":"2009-07-16","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19686339","title":"The epigenetic calnexin-independent state is induced in response to environmental changes.","citation":"FEMS Yeast Res 2009 Dec;9(8):1250-9","abstract":"Yeasts have evolved numerous responsive pathways to survive in fluctuating and stressful environments. The endoplasmic reticulum (ER) is sensitive to adverse conditions, which are detected by response pathways to ensure correct protein folding. Calnexin is an ER transmembrane chaperone acting in both quality control of folding and response to persistent stress. Calnexin is a key protein required for viability in certain organisms such as mammals and the fission yeast Schizosaccharomyces pombe. Nevertheless, S. pombe calnexin-independent (Cin) cells were obtained after transient expression of a particular calnexin mutant. The Cin state is dominant, is stably propagated by an epigenetic mechanism and segregates in a non-Mendelian fashion to the meiotic progeny. The nucleolar protein Cif1p was identified as an inducer of the Cin state in a previous genetic screen. Here, we report the identification of novel inducers isolated in an overexpression genetic screen: pyruvate kinase (Pyk1p) and phosphoglycerate kinase (Pgk1p). Addition of pyruvate, the end product of pyruvate kinase and glycolysis, also induced calnexin independence in a dose-dependent manner. Remarkably, growth in respiration media or cold temperatures induced the appearance of Cin cells at high frequencies. Taken together, our results indicate that the Cin state can be triggered by extracellular changes, suggesting that this state represents an epigenetic adaptative response to environmental modifications.","doi":"10.1111/j.1567-1364.2009.00554.x","authors":"Guérin R, Turcotte C, Leroux A, Rokeach LA","authors_abbrev":"Guérin R et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-08-19","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9391101","title":"Transcription factor Mts1/Mts2 (Atf1/Pcr1, Gad7/Pcr1) activates the M26 meiotic recombination hotspot in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1997 Dec 09;94(25):13765-70","abstract":"Homologous recombination hotspots increase the frequency of recombination in nearby DNA. The M26 hotspot in the ade6 gene of Schizosaccharomyces pombe is a meiotic hotspot with a discrete, cis-acting nucleotide sequence (5'-ATGACGT-3') defined by extensive mutagenesis. A heterodimeric M26 DNA binding protein, composed of subunits Mts1 and Mts2, has been identified and purified 40,000-fold. Cloning, disruption, and genetic analyses of the mts genes demonstrate that the Mts1/Mts2 heterodimer is essential for hotspot activity. This provides direct evidence that a specific trans-acting factor, binding to a cis-acting site with a unique nucleotide sequence, is required to activate this meiotic hotspot. Intriguingly, the Mts1/Mts2 protein subunits are identical to the recently described transcription factors Atf1 (Gad7) and Pcr1, which are required for a variety of stress responses. However, we report differential dependence on the Mts proteins for hotspot activation and stress response, suggesting that these proteins are multifunctional and have distinct activities. Furthermore, ade6 mRNA levels are equivalent in hotspot and nonhotspot meioses and do not change in mts mutants, indicating that hotspot activation is not a consequence of elevated transcription levels. These findings suggest an intimate but separable link between the regulation of transcription and meiotic recombination. Other studies have recently shown that the Mts1/Mts2 protein and M26 sites are involved in meiotic recombination elsewhere in the S. pombe genome, suggesting that these factors help regulate the timing and distribution of homologous recombination.","authors":"Kon N, Krawchuk MD, Warren BG, Smith GR, Wahls WP","authors_abbrev":"Kon N et al.","pubmed_publication_date":"09 Dec 1997","pubmed_entrez_date":"1998-02-12","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:1376421","title":"Antimutagenicity in yeast.","citation":"Mutat Res 1992 Jun;267(2):193-200","abstract":"In recent years there has been increasing interest in antimutagenesis, and studies have been done using both prokaryotic and eukaryotic systems. In eukaryotic systems the first studies were performed with different strains of Schizosaccharomyces pombe. In particular, caffeine and L-methionine were investigated. Different strains of Saccharomyces cerevisiae were employed in studies of a wide variety of compounds, including acridine, saccharin, salts, tumor promoters and co-carcinogens. Strain D7 was widely employed and antimutagenic activity of spermine, chlorophyllin, cobaltous chloride and fermented milk is reported.","authors":"Bronzetti G, Della Croce C, Galli A","authors_abbrev":"Bronzetti G et al.","pubmed_publication_date":"Jun 1992","pubmed_entrez_date":"1992-06-01","publication_year":"1992","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41199776","title":"Model systems informing mechanisms and drug discovery: a review of  POLG -related disease models.","citation":"Wellcome Open Res 2023;8:33","abstract":"CRD42021234883.","doi":"10.12688/wellcomeopenres.18637.2","authors":"Meyrick J, Stefanetti RJ, Errington L, McFarland R, Gorman GS, Lax NZ","authors_abbrev":"Meyrick J et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2025-11-07","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-11-08 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4007065","title":"Indirect suppression of the wee1 mutant phenotype in Schizosaccharomyces pombe.","citation":"Exp Cell Res 1985 Jun;158(2):533-43","abstract":"For S. pombe cells mutations in the wee1 regulatory gene have been shown previously to allow cells to be smaller than normal at cell division, to endow the cell with a significantly long G1 cell cycle interval, and to alter the timing in the cell cycle of certain mutationally-defined cell cycle steps in G2. We show here that situations which lengthen S phase in proliferating wee1 mutant cells 'suppress' to varying degrees these wee1-mediated cell cycle alterations. Conditions chosen to protract S phase were use of cdc22.M45 mutant cells at semipermissive temperatures, and the presence of sub-arresting concentrations of the S phase inhibitors hydroxyurea or deoxyadenosine. Proliferation in the presence of each of these inhibitors was shown directly to result in protracted S phase. Residual cell division measurements were used to measure the cell cycle timing of G1 and G2 cell-cycle steps. The indirect suppression of the wee1 phenotype shown here can be understood in terms of the proposed role of the wee1+ gene product in coordinating cell division with cellular growth.","authors":"Singer RA, Johnston GC","authors_abbrev":"Singer RA et al.","pubmed_publication_date":"Jun 1985","pubmed_entrez_date":"1985-06-01","publication_year":"1985","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30989357","title":"Functional interaction between Cdc42 and the stress MAPK signaling pathway during the regulation of fission yeast polarized growth.","citation":"Int Microbiol 2020 Jan;23(1):31-41","abstract":"Cell polarization can be defined as the generation and maintenance of directional cellular organization. The spatial distribution and protein or lipid composition of the cell are not symmetric but organized in specialized domains which allow cells to grow and acquire a certain shape that is closely linked to their physiological function. The establishment and maintenance of polarized growth requires the coordination of diverse processes including cytoskeletal dynamics, membrane trafficking, and signaling cascade regulation. Some of the major players involved in the selection and maintenance of sites for polarized growth are Rho GTPases, which recognize the polarization site and transmit the signal to regulatory proteins of the cytoskeleton. Additionally, cytoskeletal organization, polarized secretion, and endocytosis are controlled by signaling pathways including those mediated by mitogen-activated protein kinases (MAPKs). Rho GTPases and the MAPK signaling pathways are strongly conserved from yeast to mammals, suggesting that the basic mechanisms of polarized growth have been maintained throughout evolution. For this reason, the study of how polarized growth is established and regulated in simple organisms such as the fission yeast Schizosaccharomyces pombe has contributed to broaden our knowledge about these processes in multicellular organisms. We review here the function of the Cdc42 GTPase and the stress activated MAPK (SAPK) signaling pathways during fission yeast polarized growth, and discuss the relevance of the crosstalk between both pathways.","doi":"10.1007/s10123-019-00072-6","authors":"Pérez P, Soto T, Gómez-Gil E, Cansado J","authors_abbrev":"Pérez P et al.","pubmed_publication_date":"Jan 2020","pubmed_entrez_date":"2019-04-17","publication_year":"2020","canto_session_key":"6dcce3679f584d84","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-04-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03","SPAC24B11.06c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:32451862","title":"Myosins in Cytokinesis.","citation":"Adv Exp Med Biol 2020;1239:233-244","abstract":"Nearly five decades of research have established myosin as the main motor responsible for cytokinesis in organisms on the branch of the phylogenetic tree that includes amoebas, fungi and animals. This research has grown to be more mechanistic over the past decade, so we now have computer simulations of physically reasonable models that explain how myosins contribute to the assembly and constriction of contractile rings that pinch dividing cells into two daughter cells. Isoforms of myosin-II, from the same family as muscle myosins, are the main myosins for cytokinesis, but other myosins contribute to cytokinesis in fission yeast. Progress has been made on how animal cells use Rho-GTPases to control the accumulation and activity of myosin-II at the site of cleavage, but the regulatory mechanisms are less clear in other systems.","doi":"10.1007/978-3-030-38062-5_11","authors":"Pollard TD","authors_abbrev":"Pollard TD","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-05-27","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-05-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14623292","title":"LAMMER kinase homolog, Lkh1, is involved in oxidative-stress response of fission yeast.","citation":"Biochem Biophys Res Commun 2003 Nov 28;311(4):1078-83","abstract":"Previously, we reported that the LAMMER kinase homolog, Lkh1, is a negative regulator of filamentous growth and asexual flocculation in the fission yeast, Schizosaccharomyces pombe. Here, we report that the lkh1(+) null mutant is sensitive to oxidative stress because of a reduction in the expression of genes for antioxidant enzymes such as catalase (ctt1(+)) and Cu,Zn-superoxide dismutase (sod1(+)). Furthermore, the lkh1(+) null mutant shows increased levels of intracellular peroxides under conditions of oxidative stress compared with wild-type cells. Interestingly, expression of the gene for the transcription factor Atf1 is reduced in the lkh1(+) null mutant under oxidative stress, whereas expression of the transcription factor Pap1 is not. We report the novel finding that Lkh1 is involved in the oxidative-stress response of the fission yeast, S. pombe, and regulates the expression of antioxidant enzymes via the transcription factor Atf1.","authors":"Park YD, Kang WH, Yang WS, Shin KS, Sook Bae K, Park HM","authors_abbrev":"Park YD et al.","pubmed_publication_date":"28 Nov 2003","pubmed_entrez_date":"2003-11-19","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1D4.11c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:9809416","title":"Mutation of Gly-444 inactivates the S. pombe malic enzyme.","citation":"FEMS Microbiol Lett 1998 Oct 15;167(2):157-62","abstract":"A mutant malic enzyme gene, mae2-, was cloned from a strain of Schizosaccharomyces pombe that displayed almost no malic enzyme activity. Sequence analysis revealed only one codon-altering mutation, a guanine to adenine at nucleotide 1331, changing the glycine residue at position 444 to an aspartate residue. Gly-444 is located in Region H, previously identified as one of eight highly conserved regions in malic enzymes. We found that Gly-444 is absolutely conserved in 27 malic enzymes from various prokaryotic and eukaryotic sources, as well as in three bacterial malolactic enzymes investigated. The evolutionary conservation of Gly-444 suggests that this residue is important for enzymatic function.","authors":"Viljoen M, van der Merwe M, Subden RE, van Vuuren HJ","authors_abbrev":"Viljoen M et al.","pubmed_publication_date":"15 Oct 1998","pubmed_entrez_date":"1998-11-11","publication_year":"1998","canto_session_key":"d596748cb15fc691","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-04 12:56:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 12:02:05","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC794.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:15114530","title":"AICA-ribosiduria: a novel, neurologically devastating inborn error of purine biosynthesis caused by mutation of ATIC.","citation":"Am J Hum Genet 2004 Jun;74(6):1276-81","abstract":"In a female infant with dysmorphic features, severe neurological defects, and congenital blindness, a positive urinary Bratton-Marshall test led to identification of a massive excretion of 5-amino-4-imidazolecarboxamide (AICA)-riboside, the dephosphorylated counterpart of AICAR (also termed \"ZMP\"), an intermediate of de novo purine biosynthesis. ZMP and its di- and triphosphate accumulated in the patient's erythrocytes. Incubation of her fibroblasts with AICA-riboside led to accumulation of AICAR, not observed in control cells, suggesting impairment of the final steps of purine biosynthesis, catalyzed by the bifunctional enzyme AICAR transformylase/IMP cyclohydrolase (ATIC). AICAR transformylase was profoundly deficient, whereas the IMP cyclohydrolase level was 40% of normal. Sequencing of ATIC showed a K426R change in the transformylase region in one allele and a frameshift in the other. Recombinant protein carrying mutation K426R completely lacks AICAR transformylase activity.","authors":"Marie S, Heron B, Bitoun P, Timmerman T, Van Den Berghe G, Vincent MF","authors_abbrev":"Marie S et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-04-29","publication_year":"2004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCPB16A4.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32285141","title":"Phase separation drives pairing of homologous chromosomes.","citation":"Curr Genet 2020 Oct;66(5):881-887","abstract":"Pairing of homologous chromosomes is crucial for ensuring accurate segregation of chromosomes during meiosis. Molecular mechanisms of homologous chromosome pairing in meiosis have been extensively studied in the fission yeast Schizosaccharomyces pombe. In this organism, meiosis-specific noncoding RNA transcribed from specific genes accumulates at the respective gene loci, and chromosome-associated RNA-protein complexes mediate meiotic pairing of homologous loci through phase separation. Pairing of homologous chromosomes also occurs in somatic diploid cells in certain situations. For example, somatic pairing of homologous chromosomes occurs during the early embryogenesis in diptera, and relies on the transcription-associated chromatin architecture. Earlier models also suggest that transcription factories along the chromosome mediate pairing of homologous chromosomes in plants. These studies suggest that RNA bodies formed on chromosomes mediate the pairing of homologous chromosomes. This review summarizes lessons from S. pombe to provide general insights into mechanisms of homologous chromosome pairing mediated by phase separation of chromosome-associated RNA-protein complexes.","doi":"10.1007/s00294-020-01077-9","authors":"Hiraoka Y","authors_abbrev":"Hiraoka Y","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-04-15","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-04-16 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24450652","title":"Cdc42 regulates polarized growth and cell integrity in fission yeast.","citation":"Biochem Soc Trans 2014 Feb;42(1):201-5","abstract":"Polarized cell growth requires a well-orchestrated number of events, namely selection of growth site, organization of cytoskeleton elements and delivery of new material to the growth region. The small Rho GTPase Cdc42 has emerged as a major organizer of polarized growth through its participation in many of these events. In the present short review, we focus on the regulation of Cdc42 activity and localization as well as how it controls downstream events necessary for polarized cell growth in Schizosaccharomyces pombe. Owing to the high level of similarity of the polarity pathways, analogies between fission yeast and other model systems can be useful to decipher how cells can actively define their shape by polarized growth.","doi":"10.1042/BST20130155","authors":"Rincón SA, Estravís M, Pérez P","authors_abbrev":"Rincón SA et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2014-01-24","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24486717","title":"Proteome compression via protein domain compositions.","citation":"Methods 2014 Jun 01;67(3):380-5","abstract":"In this paper, we study domain compositions of proteins via compression of whole proteins in an organism for the sake of obtaining the entropy that the individual contains. We suppose that a protein is a multiset of domains. Since gene duplication and fusion have occurred through evolutionary processes, the same domains and the same compositions of domains appear in multiple proteins, which enables us to compress a proteome by using references to proteins for duplicated and fused proteins. Such a network with references to at most two proteins is modeled as a directed hypergraph. We propose a heuristic approach by combining the Edmonds algorithm and an integer linear programming, and apply our procedure to 14 proteomes of Dictyostelium discoideum, Escherichia coli, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Caenorhabditis elegans, Drosophila melanogaster, Arabidopsis thaliana, Oryza sativa, Danio rerio, Xenopus laevis, Gallus gallus, Mus musculus, Pan troglodytes, and Homo sapiens. The compressed size using both of duplication and fusion was smaller than that using only duplication, which suggests the importance of fusion events in evolution of a proteome.","doi":"10.1016/j.ymeth.2014.01.012","authors":"Hayashida M, Ruan P, Akutsu T","authors_abbrev":"Hayashida M et al.","pubmed_publication_date":"01 Jun 2014","pubmed_entrez_date":"2014-02-04","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25307058","title":"Cohesin-dependent globules and heterochromatin shape 3D genome architecture in S. pombe.","citation":"Nature 2014 Dec 18;516(7531):432-435","abstract":"Eukaryotic genomes are folded into three-dimensional structures, such as self-associating topological domains, the borders of which are enriched in cohesin and CCCTC-binding factor (CTCF) required for long-range interactions. How local chromatin interactions govern higher-order folding of chromatin fibres and the function of cohesin in this process remain poorly understood. Here we perform genome-wide chromatin conformation capture (Hi-C) analysis to explore the high-resolution organization of the Schizosaccharomyces pombe genome, which despite its small size exhibits fundamental features found in other eukaryotes. Our analyses of wild-type and mutant strains reveal key elements of chromosome architecture and genome organization. On chromosome arms, small regions of chromatin locally interact to form 'globules'. This feature requires a function of cohesin distinct from its role in sister chromatid cohesion. Cohesin is enriched at globule boundaries and its loss causes disruption of local globule structures and global chromosome territories. By contrast, heterochromatin, which loads cohesin at specific sites including pericentromeric and subtelomeric domains, is dispensable for globule formation but nevertheless affects genome organization. We show that heterochromatin mediates chromatin fibre compaction at centromeres and promotes prominent inter-arm interactions within centromere-proximal regions, providing structural constraints crucial for proper genome organization. Loss of heterochromatin relaxes constraints on chromosomes, causing an increase in intra- and inter-chromosomal interactions. Together, our analyses uncover fundamental genome folding principles that drive higher-order chromosome organization crucial for coordinating nuclear functions.","doi":"10.1038/nature13833","authors":"Mizuguchi T, Fudenberg G, Mehta S, Belton JM, Taneja N, Folco HD, FitzGerald P, Dekker J, Mirny L, Barrowman J, Grewal SIS","authors_abbrev":"Mizuguchi T et al.","pubmed_publication_date":"18 Dec 2014","pubmed_entrez_date":"2014-10-14","publication_year":"2014","canto_session_key":"39d640cef006b15d","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-10-15 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16912194","title":"Cross-talk between nucleotide excision and homologous recombination DNA repair pathways in the mechanism of action of antitumor trabectedin.","citation":"Cancer Res 2006 Aug 15;66(16):8155-62","abstract":"Trabectedin (Yondelis) is a potent antitumor drug that has the unique characteristic of killing cells by poisoning the DNA nucleotide excision repair (NER) machinery. The basis for the NER-dependent toxicity has not yet been elucidated but it has been proposed as the major determinant for the drug's cytotoxicity. To study the in vivo mode of action of trabectedin and to explore the role of NER in its cytotoxicity, we used the fission yeast Schizosaccharomyces pombe as a model system. Treatment of S. pombe wild-type cells with trabectedin led to cell cycle delay and activation of the DNA damage checkpoint, indicating that the drug causes DNA damage in vivo. DNA damage induced by the drug is mostly caused by the NER protein, Rad13 (the fission yeast orthologue to human XPG), and is mainly repaired by homologous recombination. By constructing different rad13 mutants, we show that the DNA damage induced by trabectedin depends on a 46-amino acid region of Rad13 that is homologous to a DNA-binding region of human nuclease FEN-1. More specifically, an arginine residue in Rad13 (Arg961), conserved in FEN1 (Arg314), was found to be crucial for the drug's cytotoxicity. These results lead us to propose a model for the action of trabectedin in eukaryotic cells in which the formation of a Rad13/DNA-trabectedin ternary complex, stabilized by Arg961, results in cell death.","authors":"Herrero AB, Martín-Castellanos C, Marco E, Gago F, Moreno S","authors_abbrev":"Herrero AB et al.","pubmed_publication_date":"15 Aug 2006","pubmed_entrez_date":"2006-08-17","publication_year":"2006","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPBC3E7.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:28049779","title":"Cryoelectron Microscopy of Fission Yeast.","citation":"Cold Spring Harb Protoc 2017 Jan 03;2017(1)","abstract":"Fission yeast cells can be prepared for electron microscopy (EM) in the frozen-hydrated state. This eliminates the requirement for dehydration and heavy metal staining when preparing samples for EM. As with room temperature imaging, however, the yeast must be sectioned to make them thin enough for transmission of the electron beam. Cutting sections of vitreous ice with a microtome is challenging. An alternative method that uses a focused ion beam to make a thin sample by milling away much of the sample at liquid nitrogen temperatures is under development but is not yet available for routine use. Imaging frozen-hydrated samples by EM is also a challenge. The technique involves battling low image contrast, high sensitivity to the electron beam, and mechanical distortions produced during the sectioning process. When used successfully, however, the method holds promise of providing excellent molecular detail without the disruption characteristic of dehydration or isolating a structure from its cellular environment. Cryo-EM of tilted views can be used to examine small structures and macromolecular complexes in their native cellular environment. If a structure exists in multiple copies, or has a repeating unit, it can be investigated at higher resolution using subvolume averaging. This protocol focuses on the preparation of cells for cryo-EM.","doi":"10.1101/pdb.prot091330","authors":"Morphew MK, Giddings TH, McIntosh JR","authors_abbrev":"Morphew MK et al.","pubmed_publication_date":"03 Jan 2017","pubmed_entrez_date":"2017-01-05","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-01-06 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28388826","title":"Sulfur restriction extends fission yeast chronological lifespan through Ecl1 family genes by downregulation of ribosome.","citation":"Mol Microbiol 2017 Jul;105(1):84-97","abstract":"Nutritional restrictions such as calorie restrictions are known to increase the lifespan of various organisms. Here, we found that a restriction of sulfur extended the chronological lifespan (CLS) of the fission yeast Schizosaccharomyces pombe. The restriction decreased cellular size, RNA content, and ribosomal proteins and increased sporulation rate. These responses depended on Ecl1 family genes, the overexpression of which results in the extension of CLS. We also showed that the Zip1 transcription factor results in the sulfur restriction-dependent expression of the ecl1 +  gene. We demonstrated that a decrease in ribosomal activity results in the extension of CLS. Based on these observations, we propose that sulfur restriction extends CLS through Ecl1 family genes in a ribosomal activity-dependent manner.","doi":"10.1111/mmi.13686","authors":"Ohtsuka H, Takinami M, Shimasaki T, Hibi T, Murakami H, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Jul 2017","pubmed_entrez_date":"2017-04-08","publication_year":"2017","canto_session_key":"1534156512e84afb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-10-24 07:35:38","canto_approved_date":"2023-05-06 08:14:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-03 07:15:49","canto_added_date":"2017-04-09 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8E4.12c","SPBC32C12.02","SPBP35G2.16c","SPAC27D7.03c","SPAC25G10.03","SPAC22E12.14c","SPBC106.10","SPBC2F12.09c","SPCC576.11","SPCC70.12c","SPAPB1E7.12","SPCC16C4.13c","SPAPJ698.02c","SPAC15E1.03"],"gene_count":14,"ltp_gene_count":10,"approved_date":"2019-10-24"},{"uniquename":"PMID:27257059","title":"Ribosome recycling defects modify the balance between the synthesis and assembly of specific subunits of the oxidative phosphorylation complexes in yeast mitochondria.","citation":"Nucleic Acids Res 2016 Jul 08;44(12):5785-97","abstract":"Mitochondria have their own translation machinery that produces key subunits of the OXPHOS complexes. This machinery relies on the coordinated action of nuclear-encoded factors of bacterial origin that are well conserved between humans and yeast. In humans, mutations in these factors can cause diseases; in yeast, mutations abolishing mitochondrial translation destabilize the mitochondrial DNA. We show that when the mitochondrial genome contains no introns, the loss of the yeast factors Mif3 and Rrf1 involved in ribosome recycling neither blocks translation nor destabilizes mitochondrial DNA. Rather, the absence of these factors increases the synthesis of the mitochondrially-encoded subunits Cox1, Cytb and Atp9, while strongly impairing the assembly of OXPHOS complexes IV and V. We further show that in the absence of Rrf1, the COX1 specific translation activator Mss51 accumulates in low molecular weight forms, thought to be the source of the translationally-active form, explaining the increased synthesis of Cox1. We propose that Rrf1 takes part in the coordination between translation and OXPHOS assembly in yeast mitochondria. These interactions between general and specific translation factors might reveal an evolutionary adaptation of the bacterial translation machinery to the set of integral membrane proteins that are translated within mitochondria.","doi":"10.1093/nar/gkw490","authors":"Ostojić J, Panozzo C, Bourand-Plantefol A, Herbert CJ, Dujardin G, Bonnefoy N","authors_abbrev":"Ostojić J et al.","pubmed_publication_date":"08 Jul 2016","pubmed_entrez_date":"2016-06-04","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.11","SPAC25B8.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:SPD233","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21233285","title":"Spatiotemporal regulations of Wee1 at the G2/M transition.","citation":"Mol Biol Cell 2011 Mar 01;22(5):555-69","abstract":"Wee1 is a protein kinase that negatively regulates mitotic entry in G2 phase by suppressing cyclin B-Cdc2 activity, but its spatiotemporal regulations remain to be elucidated. We observe the dynamic behavior of Wee1 in Schizosaccharomyces pombe cells and manipulate its localization and kinase activity to study its function. At late G2, nuclear Wee1 efficiently suppresses cyclin B-Cdc2 around the spindle pole body (SPB). During the G2/M transition when cyclin B-Cdc2 is highly enriched at the SPB, Wee1 temporally accumulates at the nuclear face of the SPB in a cyclin B-Cdc2-dependent manner and locally suppresses both cyclin B-Cdc2 activity and spindle assembly to counteract a Polo kinase-dependent positive feedback loop. Then Wee1 disappears from the SPB during spindle assembly. We propose that regulation of Wee1 localization around the SPB during the G2/M transition is important for proper mitotic entry and progression.","doi":"10.1091/mbc.E10-07-0644","authors":"Masuda H, Fong CS, Ohtsuki C, Haraguchi T, Hiraoka Y","authors_abbrev":"Masuda H et al.","pubmed_publication_date":"01 Mar 2011","pubmed_entrez_date":"2011-01-15","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6G9.06c","SPCC18B5.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9753750","title":"Use of gap repair in fission yeast to obtain novel alleles of specific genes.","citation":"Nucleic Acids Res 1998 Oct 15;26(20):4783-4","abstract":"We have adapted a method for making libraries of mutations in any specific gene for use in the fission yeast Schizosaccharomyces pombe . This elegant and simple method consists of PCR amplification of the gene of interest, followed by co-transformation of fission yeast with the PCR fragment and a linearized plasmid vector prepared such that the ends of the vector share DNA sequence with the ends of the PCR fragment. Homologous recombination between the vector and the PCR fragment occurs at a high frequency and results in a collection of yeast transformants, most harboring a mutated allele of the original gene within the vector of choice. This library can then be screened or selected for phenotypes of interest.","authors":"Kostrub CF, Lei EP, Enoch T","authors_abbrev":"Kostrub CF et al.","pubmed_publication_date":"15 Oct 1998","pubmed_entrez_date":"1998-10-01","publication_year":"1998","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9467896","title":"Analysis of fission yeast DNA structure checkpoints.","citation":"Microbiology (Reading) 1998 Jan;144 ( Pt 1):5-11","abstract":"","doi":"10.1099/00221287-144-1-5","authors":"Carr AM","authors_abbrev":"Carr AM","pubmed_publication_date":"Jan 1998","pubmed_entrez_date":"1998-02-19","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18820293","title":"Nuclear export competence of pre-40S subunits in fission yeast requires the ribosomal protein Rps2.","citation":"Nucleic Acids Res 2008 Nov;36(19):6132-42","abstract":"Ribosome biogenesis is an evolutionarily conserved pathway that requires ribosomal and nonribosomal proteins. Here, we investigated the role of the ribosomal protein S2 (Rps2) in fission yeast ribosome synthesis. As for many budding yeast ribosomal proteins, Rps2 was essential for cell viability in fission yeast and the genetic depletion of Rps2 caused a complete inhibition of 40S ribosomal subunit production. The pattern of pre-rRNA processing upon depletion of Rps2 revealed a reduction of 27SA(2) pre-rRNAs and the concomitant production of 21S rRNA precursors, consistent with a role for Rps2 in efficient cleavage at site A(2) within the 32S pre-rRNA. Importantly, kinetics of pre-rRNA accumulation as determined by rRNA pulse-chases assays indicated that a small fraction of 35S precursors matured into 20S-containing particles, suggesting that most 40S precursors were rapidly degraded in the absence of Rps2. Analysis of steady-state RNA levels revealed that some pre-40S particles were produced in Rps2-depleted cells, but that these precursors were retained in the nucleolus. Our findings suggest a role for Rps2 in a mechanism that monitors pre-40S export competence.","doi":"10.1093/nar/gkn625","authors":"Perreault A, Bellemer C, Bachand F","authors_abbrev":"Perreault A et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-09-30","publication_year":"2008","canto_session_key":"8044eed53ee25b01","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC285.15c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:17677001","title":"Plasticity of fission yeast CENP-A chromatin driven by relative levels of histone H3 and H4.","citation":"PLoS Genet 2007 Jul;3(7):e121","abstract":"The histone H3 variant CENP-A assembles into chromatin exclusively at centromeres. The process of CENP-A chromatin assembly is epigenetically regulated. Fission yeast centromeres are composed of a central kinetochore domain on which CENP-A chromatin is assembled, and this is flanked by heterochromatin. Marker genes are silenced when placed within kinetochore or heterochromatin domains. It is not known if fission yeast CENP-A(Cnp1) chromatin is confined to specific sequences or whether histone H3 is actively excluded. Here, we show that fission yeast CENP-A(Cnp1) can assemble on noncentromeric DNA when it is inserted within the central kinetochore domain, suggesting that in fission yeast CENP-A(Cnp1) chromatin assembly is driven by the context of a sequence rather than the underlying DNA sequence itself. Silencing in the central domain is correlated with the amount of CENP-A(Cnp1) associated with the marker gene and is also affected by the relative level of histone H3. Our analyses indicate that kinetochore integrity is dependent on maintaining the normal ratio of H3 and H4. Excess H3 competes with CENP-A(Cnp1) for assembly into central domain chromatin, resulting in less CENP-A(Cnp1) and other kinetochore proteins at centromeres causing defective kinetochore function, which is manifest as aberrant mitotic chromosome segregation. Alterations in the levels of H3 relative to H4 and CENP-A(Cnp1) influence the extent of DNA at centromeres that is packaged in CENP-A(Cnp1) chromatin and the composition of this chromatin. Thus, CENP-A(Cnp1) chromatin assembly in fission yeast exhibits plasticity with respect to the underlying sequences and is sensitive to the levels of CENP-A(Cnp1) and other core histones.","authors":"Castillo AG, Mellone BG, Partridge JF, Richardson W, Hamilton GL, Allshire RC, Pidoux AL","authors_abbrev":"Castillo AG et al.","pubmed_publication_date":"Jul 2007","pubmed_entrez_date":"2007-08-07","publication_year":"2007","canto_session_key":"c06e8b663aa9d810","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-04-23 10:09:24","canto_approved_date":"2020-04-23 10:09:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-31 16:36:02","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.17","SPBC8D2.03c","SPBC8D2.04","SPBC1105.11c","SPAC1834.03c","SPAC1834.04"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2020-04-23"},{"uniquename":"PMID:31468675","title":"H3K14 ubiquitylation promotes H3K9 methylation for heterochromatin assembly.","citation":"EMBO Rep 2019 Oct 04;20(10):e48111","abstract":"The methylation of histone H3 at lysine 9 (H3K9me), performed by the methyltransferase Clr4/SUV39H, is a key event in heterochromatin assembly. In fission yeast, Clr4, together with the ubiquitin E3 ligase Cul4, forms the Clr4 methyltransferase complex (CLRC), whose physiological targets and biological role are currently unclear. Here, we show that CLRC-dependent H3 ubiquitylation regulates Clr4's methyltransferase activity. Affinity-purified CLRC ubiquitylates histone H3, and mass spectrometric and mutation analyses reveal that H3 lysine 14 (H3K14) is the preferred target of the complex. Chromatin immunoprecipitation analysis shows that H3K14 ubiquitylation (H3K14ub) is closely associated with H3K9me-enriched chromatin. Notably, the CLRC-mediated H3 ubiquitylation promotes H3K9me by Clr4, suggesting that H3 ubiquitylation is intimately linked to the establishment and/or maintenance of H3K9me. These findings demonstrate a cross-talk mechanism between histone ubiquitylation and methylation that is involved in heterochromatin assembly.","doi":"10.15252/embr.201948111","authors":"Oya E, Nakagawa R, Yoshimura Y, Tanaka M, Nishibuchi G, Machida S, Shirai A, Ekwall K, Kurumizaka H, Tagami H, Nakayama JI","authors_abbrev":"Oya E et al.","pubmed_publication_date":"04 Oct 2019","pubmed_entrez_date":"2019-08-31","publication_year":"2019","canto_session_key":"a09af17a2956146d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-ichi Nakayama","canto_first_approved_date":"2019-10-03 16:00:35","canto_approved_date":"2025-09-03 11:52:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-09-25 02:53:51","canto_added_date":"2019-09-01 00:15:04","annotation_curators":[{"name":"Jun-ichi Nakayama","community_curator":true,"annotation_count":5,"orcid":"0000-0002-5597-8239","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.04","SPBC8D2.04","SPBC428.08c","SPAC3A11.08","SPCC11E10.08","SPBC1105.11c","SPAC23H4.18c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2019-10-03"},{"uniquename":"PMID:16813561","title":"Identification of a novel NADH-specific aldo-keto reductase using sequence and structural homologies.","citation":"Biochem J 2006 Nov 15;400(1):105-14","abstract":"The AKRs (aldo-keto reductases) are a superfamily of enzymes which mainly rely on NADPH to reversibly reduce various carbonyl-containing compounds to the corresponding alcohols. A small number have been found with dual NADPH/NADH specificity, usually preferring NADPH, but none are exclusive for NADH. Crystal structures of the dual-specificity enzyme xylose reductase (AKR2B5) indicate that NAD+ is bound via a key interaction with a glutamate that is able to change conformations to accommodate the 2'-phosphate of NADP+. Sequence comparisons suggest that analogous glutamate or aspartate residues may function in other AKRs to allow NADH utilization. Based on this, nine putative enzymes with potential NADH specificity were identified and seven genes were successfully expressed and purified from Drosophila melanogaster, Escherichia coli, Schizosaccharomyces pombe, Sulfolobus solfataricus, Sinorhizobium meliloti and Thermotoga maritima. Each was assayed for co-substrate dependence with conventional AKR substrates. Three were exclusive for NADPH (AKR2E3, AKR3F2 and AKR3F3), two were dual-specific (AKR3C2 and AKR3F1) and one was specific for NADH (AKR11B2), the first such activity in an AKR. Fluorescence measurements of the seventh protein indicated that it bound both NADPH and NADH but had no activity. Mutation of the aspartate into an alanine residue or a more mobile glutamate in the NADH-specific E. coli protein converted it into an enzyme with dual specificity. These results show that the presence of this carboxylate is an indication of NADH dependence. This should allow improved prediction of co-substrate specificity and provide a basis for engineering enzymes with altered co-substrate utilization for this class of enzymes.","authors":"Di Luccio E, Elling RA, Wilson DK","authors_abbrev":"Di Luccio E et al.","pubmed_publication_date":"15 Nov 2006","pubmed_entrez_date":"2006-07-04","publication_year":"2006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.09"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:30718845","title":"Single-cell imaging and RNA sequencing reveal patterns of gene expression heterogeneity during fission yeast growth and adaptation.","citation":"Nat Microbiol 2019 Mar;4(3):480-491","abstract":"Phenotypic cell-to-cell variability is a fundamental determinant of microbial fitness that contributes to stress adaptation and drug resistance. Gene expression heterogeneity underpins this variability but is challenging to study genome-wide. Here we examine the transcriptomes of >2,000 single fission yeast cells exposed to various environmental conditions by combining imaging, single-cell RNA sequencing and Bayesian true count recovery. We identify sets of highly variable genes during rapid proliferation in constant culture conditions. By integrating single-cell RNA sequencing and cell-size data, we provide insights into genes that are regulated during cell growth and division, including genes whose expression does not scale with cell size. We further analyse the heterogeneity of gene expression during adaptive and acute responses to changing environments. Entry into the stationary phase is preceded by a gradual, synchronized adaptation in gene regulation that is followed by highly variable gene expression when growth decreases. Conversely, sudden and acute heat shock leads to a stronger, coordinated response and adaptation across cells. This analysis reveals that the magnitude of global gene expression heterogeneity is regulated in response to different physiological conditions within populations of a unicellular eukaryote.","doi":"10.1038/s41564-018-0330-4","authors":"Saint M, Bertaux F, Tang W, Sun XM, Game L, Köferle A, Bähler J, Shahrezaei V, Marguerat S","authors_abbrev":"Saint M et al.","pubmed_publication_date":"Mar 2019","pubmed_entrez_date":"2019-02-06","publication_year":"2019","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-02-07 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38168868","title":"A novel cell biological tool to explain mechanics and dynamics in fission yeast.","citation":"J Basic Microbiol 2024 Jan 02;","abstract":"The Rho guanosine triphosphatase hydrolase enzyme (GTPase) is required for the control of the actin cytoskeleton, but its activation in vivo condition is unknown. The study's goal was to find a new synthetic nanobody V H  H (P-36 tagged with mNeonGreen) that interacts strongly with the Rho GTPase. We present the first novel synthetic nanobody, V H  H (P-36 tagged with mNeonGreen), tested in fission yeast cells and found to have a particular interaction with Rho1GTPase. Plasmids were constructed by using of certain enzymes to digest the pDUAL-pef1a vector plasmid to produce a protein that was encoded by cloned genes. A varied V H  H library was created synthetically, then transformed into yeast cells, and positive clones were chosen using chemical agents. To investigate protein interactions and cellular reactions, several studies were carried out, such as live cell imaging, growth curve analysis, coimmunoprecipitation, structural analysis, and cell therapies. Prism and RStudio were used for the statistical analysis. The presence of V H  H (P-36) has no effect on the growth pattern making it an appropriate model for studying cytokinesis in vivo. According to a computational biological study, its affinity to interact with Rho1GTPase with all the complementarity-determining region (CDR) regions found on V H  H (P-36) is extremely strong. We were able to track its subcellular target by localization using a fluorescent confocal microscope, ensuring the maintenance of cell polarity and morphology. Spheroplast analysis revealed a circular-shaped cell with an even distribution of Rho1 tagged V H  H (P-36), indicating that the interaction occurs near the plasma membrane. The introduction of latrunculin-A (Lat-A) disrupted Rho GTPase localization, demonstrating the control over actin production, and the cell did not show evidence of mitotic phase commencement while Lat-A was present. Finally, this important biological tool can aid in our understanding of the mechanics and dynamics of cytokinesis in relation to Rho1GTPase.","doi":"10.1002/jobm.202300605","authors":"Rasheed MA, Mohy-Ud-Din R, Anwar T, Faiz M","authors_abbrev":"Rasheed MA et al.","pubmed_publication_date":"02 Jan 2024","pubmed_entrez_date":"2024-01-03","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-01-05 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26173815","title":"Genome-wide screen of fission yeast mutants for sensitivity to 6-azauracil, an inhibitor of transcriptional elongation.","citation":"Yeast 2015 Oct;32(10):643-55","abstract":"6-Azauracil (6 AU) inhibits enzymes in nucleoside synthesis and depletes the intracellular GTP/UTP pool. Mutations in transcriptional elongation machinery, as well as mutations in a variety of other pathways, exaggerate the growth defect of cells in the presence of 6 AU. Thus, identification of mutations that render cells sensitive to 6 AU will benefit study on the basis of 6 AU-sensitive phenotype. Here we performed a genome-wide screen of a fission yeast deletion library. Of 3235 single-gene deletions, 66 mutants displayed at least 50% drop of fitness in the presence of 6 AU and 60 mutants were reported for the first time; five deletions showed synthetic decrease of fitness when combined with deletion of set3(+) , which encodes a transcriptional regulator. Genes conferring tolerance to 6 AU were enriched in various processes, especially in chromosome segregation. Accordingly, genes encoding subunits of CLRC complex and spindle pole body were over-represented. Mutants were subjected to an in vivo transcript length-dependent reporter assay to assess the potential roles of deleted genes in transcriptional elongation. As with the deletions known to affect elongation, nab2Δ, nxt1Δ, rhp18Δ, SPAC24C9.08Δ, clr3Δ and ncs1Δset3Δ mutants exhibited defects in expressing long transcripts. New 6 AU-sensitive mutants identified here will help to elucidate the mechanism of action of 6 AU in the cells. Meanwhile, our study revealed novel genes potentially involved in transcriptional elongation and provided valuable targets for transcription study.","doi":"10.1002/yea.3085","authors":"Zhou H, Liu Q, Shi T, Yu Y, Lu H","authors_abbrev":"Zhou H et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2015-07-16","publication_year":"2015","canto_session_key":"54d139db4219114e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-07-27 11:11:16","canto_approved_date":"2022-02-07 19:51:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-27 11:11:06","canto_added_date":"2015-07-17 00:20:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":66,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_26173815_phaf.tsv"}],"genes":["SPAC20H4.03c","SPAC20G4.04c","SPAC24C9.08","SPAC20G8.08c","SPAC22F8.11","SPBC19F5.01c","SPAC959.04c","SPCC970.07c","SPCC4E9.01c","SPAC1142.08","SPCC126.11c","SPCC16C4.10","SPBC27.02c","SPAC9G1.08c","SPAC23C4.03","SPBC428.08c","SPBC354.10","SPCC576.01c","SPBC30B4.03c","SPBPB2B2.11","SPAC139.01c","SPAC6F12.06","SPAC17H9.03c","SPAC18B11.02c","SPBC1734.06","SPAC17H9.10c","SPBC1709.11c","SPBC23E6.10c","SPAC3G9.01","SPAC16A10.05c","SPAC22E12.11c","SPAC27E2.02","SPAPB1A10.10c","SPAC30D11.05","SPBC32H8.06","SPBC428.17c","SPBC36B7.02","SPACUNK4.11c","SPBC19G7.04","SPBC800.03","SPCC16C4.11","SPCC1919.13c","SPAC18G6.02c","SPAC1F5.05c","SPAC144.06","SPAC688.10","SPAC1705.02","SPAC4F10.20","SPBC1734.07c","SPAC8C9.09c","SPCC24B10.12","SPAC3G9.15c","SPAC30.02c","SPAC18B11.04","SPAC29B12.08","SPCC11E10.08","SPBC32H8.03","SPAC664.01c","SPBC30D10.04","SPAC23H3.13c","SPAC14C4.06c","SPCC584.11c","SPCPJ732.02c","SPAC1687.15","SPBC1683.06c","SPBC1711.14","SPAC20H4.09","SPAC630.13c","SPAPB1A10.03","SPCC364.06","SPCC16A11.16c","SPBC16C6.04"],"gene_count":72,"ltp_gene_count":15,"approved_date":"2015-07-27"},{"uniquename":"PMID:31601154","title":" gas1  mutation extends chronological lifespan via Pmk1 and Sty1 MAPKs in  Schizosaccharomyces pombe .","citation":"Biosci Biotechnol Biochem 2020 Feb;84(2):330-337","abstract":"In the longevity research by using yeasts, chronological lifespan is defined as the survival time after entry into stationary phase. Previously, screening for long lived mutants of  Schizosaccharomyces pombe  was performed to identify the novel factors involved in longevity. From this screening, one long lived mutant called as No.36 was obtained. In this study, we identified the mutation caused in  gas1  + , which encodes glucanosyltransferase ( gas1-287  mutation) is responsible for the longevity of No.36 mutant. Through the analysis of this mutant, we found that cell wall perturbing agent micafungin also extends chronological lifespan in fission yeast. This lifespan extension depended on both Pmk1 and Sty1 MAP kinases, and longevity caused by the  gas1-287  mutation also depended on these kinases. In summary, we propose that the  gas1-287  mutation causes longevity as the similar mechanism as cell wall stress depending on Pmk1 and Sty1 MAPK pathways.","doi":"10.1080/09168451.2019.1676695","authors":"Imai Y, Shimasaki T, Enokimura C, Ohtsuka H, Tsubouchi S, Ihara K, Aiba H","authors_abbrev":"Imai Y et al.","pubmed_publication_date":"Feb 2020","pubmed_entrez_date":"2019-10-12","publication_year":"2020","canto_session_key":"a5f9b2e25384cb10","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2019-12-10 18:19:08","canto_approved_date":"2019-12-10 18:19:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-23 16:14:51","canto_added_date":"2019-10-13 00:15:04","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":1,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.08","SPAC19B12.02c","SPAC24B11.06c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-12-10"},{"uniquename":"PMID:9614195","title":"Functional domains of rep2, a transcriptional activator subunit for Res2-Cdc10, controlling the cell cycle \"start\".","citation":"Mol Biol Cell 1998 Jun;9(6):1577-88","abstract":"In the fission yeast Schizosaccharomyces pombe, passage from G1 to S-phase requires the execution of the transcriptional factor complex that consists of the Cdc10 and Res1/2 molecules. This complex activates the MluI cell cycle box cis-element contained in genes essential for S-phase onset and progression. The rep2(+) gene, isolated as a multicopy suppressor of a temperature-sensitive cdc10 mutant, has been postulated to encode a putative transcriptional activator subunit for the Res2-Cdc10 complex. To identify the rep2(+) function and molecularly define its domain organization, we reconstituted the Res2-Cdc10 complex-dependent transcriptional activation in Saccharomyces cerevisiae. Reconstitution experiments, deletion analyses using one and two hybrid systems, and in vivo Res2 coimmunoprecipitation assays show that the Res2-Cdc10 complex itself can recognize but cannot activate MluI cell cycle box without Rep2, and that consistent with its postulated function, Rep2 contains 45-amino acid Res2 binding and 22-amino acid transcriptional activation domains in the middle and C terminus of the molecule, respectively. The functional essentiality of these domains is also demonstrated by their requirement for rescue of the cold-sensitive rep2 deletion mutant of fission yeast.","authors":"Tahara S, Tanaka K, Yuasa Y, Okayama H","authors_abbrev":"Tahara S et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-06-17","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2F12.11c","SPBC725.16","SPAC22F3.09c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:21547948","title":"A fast and inexpensive method for random spore analysis in Schizosaccharomyces pombe.","citation":"Yeast 2011 Jul;28(7):527-33","abstract":"Random spore analysis is a fundamental tool of yeast genetics for determining gene linkage and the generation of recombinant progeny by genetic crosses. Experimentally it involves treatment of a mating mix with enzymes, such as zymolyase or lyticase, that selectively lyse the cell wall of vegetative cells rather than the spores. Here, we describe a method whereby the relative refractory nature of the spores to treatment with elevated temperature and repeated freeze-thawing facilitates random spore analysis at low cost in fission yeast Schizosaccharomyces pombe. Because of similar properties of spores in budding yeast, this method should prove to be useful for random spore analysis in both budding and fission yeasts.","doi":"10.1002/yea.1855","authors":"Khare AK, Singh B, Singh J","authors_abbrev":"Khare AK et al.","pubmed_publication_date":"Jul 2011","pubmed_entrez_date":"2011-05-07","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26806637","title":"Molecular control of fission yeast cytokinesis.","citation":"Semin Cell Dev Biol 2016 May;53:28-38","abstract":"Cytokinesis gives rise to two independent daughter cells at the end of the cell division cycle. The fission yeast Schizosaccharomyces pombe has emerged as one of the most powerful systems to understand how cytokinesis is controlled molecularly. Like in most eukaryotes, fission yeast cytokinesis depends on an acto-myosin based contractile ring that assembles at the division site under the control of spatial cues that integrate information on cell geometry and the position of the mitotic apparatus. Cytokinetic events are also tightly coordinated with nuclear division by the cell cycle machinery. These spatial and temporal regulations ensure an equal cleavage of the cytoplasm and an accurate segregation of the genetic material in daughter cells. Although this model system has specificities, the basic mechanisms of contractile ring assembly and function deciphered in fission yeast are highly valuable to understand how cytokinesis is controlled in other organisms that rely on a contractile ring for cell division.","doi":"10.1016/j.semcdb.2016.01.007","authors":"Rincon SA, Paoletti A","authors_abbrev":"Rincon SA et al.","pubmed_publication_date":"May 2016","pubmed_entrez_date":"2016-01-26","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-01-27 01:15:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21247896","title":"The dynamics and mechanism of SUMO chain deconjugation by SUMO-specific proteases.","citation":"J Biol Chem 2011 Mar 25;286(12):10238-47","abstract":"SUMOylation of proteins is a cyclic process that requires both conjugation and deconjugation of SUMO moieties. Besides modification by a single SUMO, SUMO chains have also been observed, yet the dynamics of SUMO conjugation/deconjugation remain poorly understood. Using a non-deconjugatable form of SUMO we demonstrate the underappreciated existence of SUMO chains in vivo, we highlight the importance of SUMO deconjugation, and we demonstrate the highly dynamic nature of the SUMO system. We show that SUMO-specific proteases (SENPs) play a crucial role in the dynamics of SUMO chains in vivo by constant deconjugation. Preventing deSUMOylation in Schizosaccharomyces pombe results in slow growth and a sensitivity to replication stress, highlighting the biological requirement for deSUMOylation dynamics. Furthermore, we present the mechanism of SUMO chain deconjugation by SENPs, which occurs via a stochastic mechanism, resulting in cleavage anywhere within a chain. Our results offer mechanistic insights into the workings of deSUMOylating proteases and highlight their importance in the homeostasis of (poly)SUMO-modified substrates.","doi":"10.1074/jbc.M110.205153","authors":"Békés M, Prudden J, Srikumar T, Raught B, Boddy MN, Salvesen GS","authors_abbrev":"Békés M et al.","pubmed_publication_date":"25 Mar 2011","pubmed_entrez_date":"2011-01-21","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9080773","title":"The FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair.","citation":"Bioessays 1997 Mar;19(3):233-40","abstract":"Unlike the most well-characterized prokaryotic polymerase, E. coli DNA pol l, none of the eukaryotic polymerases have their own 5' to 3' exonuclease domain for nick translation and Okazaki fragment processing. In eukaryotes, FEN-1 is an endo- and exonuclease that carries out this function independently of the polymerase molecules. Only seven nucleases have been cloned from multicellular eukaryotic cells. Among these, FEN-1 is intriguing because it has complex structural preferences; specifically, it cleaves at branched DNA structures. The cloning of FEN-1 permitted establishment of the first eukaryotic nuclease family, predicting that S. cerevisiae RAD2 (S. pombe Rad13) and its mammalian homolog, XPG, would have similar structural specificity. The FEN-1 nuclease family includes several similar enzymes encoded by bacteriophages. The crystal structures of two enzymes in the FEN-1 nuclease family have been solved and they provide a structural basis for the interesting steric requirements of FEN-1 substrates. Because of their unique structural specificities, FEN-1 and its family members have important roles in DNA replication, repair and, potentially, recombination. Recently, FEN-1 was found to specifically associate with PCNA, explaining some aspects of FEN-1 function during DNA replication and potentially in DNA repair.","authors":"Lieber MR","authors_abbrev":"Lieber MR","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9774280","title":"Two modes of survival of fission yeast without telomerase.","citation":"Science 1998 Oct 16;282(5388):493-6","abstract":"Deletion of the telomerase catalytic subunit gene trt1+ in Schizosaccharomyces pombe results in death for the majority of cells, but a subpopulation survives. Here it is shown that most survivors have circularized all of their chromosomes, whereas a smaller number maintain their telomeres presumably through recombination. When the telomeric DNA-binding gene taz1+ is also deleted, trt1- taz1- survivors use the recombinational mode more frequently. Moreover, the massive elongation of telomeres in taz1- cells is absent in the double mutant. Thus, Taz1p appears to regulate telomeric recombination as well as telomerase activity in fission yeast.","authors":"Nakamura TM, Cooper JP, Cech TR","authors_abbrev":"Nakamura TM et al.","pubmed_publication_date":"16 Oct 1998","pubmed_entrez_date":"1998-10-17","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.07c","SPBC29A3.14c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:23093943","title":"Cytokinesis-based constraints on polarized cell growth in fission yeast.","citation":"PLoS Genet 2012;8(10):e1003004","abstract":"The rod-shaped fission yeast Schizosaccharomyces pombe, which undergoes cycles of monopolar-to-bipolar tip growth, is an attractive organism for studying cell-cycle regulation of polarity establishment. While previous research has described factors mediating this process from interphase cell tips, we found that division site signaling also impacts the re-establishment of bipolar cell growth in the ensuing cell cycle. Complete loss or targeted disruption of the non-essential cytokinesis protein Fic1 at the division site, but not at interphase cell tips, resulted in many cells failing to grow at new ends created by cell division. This appeared due to faulty disassembly and abnormal persistence of the cell division machinery at new ends of fic1Δ cells. Moreover, additional mutants defective in the final stages of cytokinesis exhibited analogous growth polarity defects, supporting that robust completion of cell division contributes to new end-growth competency. To test this model, we genetically manipulated S. pombe cells to undergo new end take-off immediately after cell division. Intriguingly, such cells elongated constitutively at new ends unless cytokinesis was perturbed. Thus, cell division imposes constraints that partially override positive controls on growth. We posit that such constraints facilitate invasive fungal growth, as cytokinesis mutants displaying bipolar growth defects formed numerous pseudohyphae. Collectively, these data highlight a role for previous cell cycles in defining a cell's capacity to polarize at specific sites, and they additionally provide insight into how a unicellular yeast can transition into a quasi-multicellular state.","doi":"10.1371/journal.pgen.1003004","authors":"Bohnert KA, Gould KL","authors_abbrev":"Bohnert KA et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-10-25","publication_year":"2012","canto_session_key":"60eea6892c654dff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-04-02 08:53:32","canto_approved_date":"2025-12-19 13:59:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-26 15:20:57","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":43,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPYUG7.03c","SPAC9G1.11c","SPAC4F10.11","SPAC821.09","SPCC895.05","SPCC1223.06","SPAC4F10.15c","SPBC19G7.05c","SPAC20G8.05c","SPBC11C11.02","SPBC83.18c","SPAC23C4.02","SPAC19B12.10","SPBC21.06c","SPBC1706.01","SPAC14C4.09","SPCC645.07","SPAC9E9.14","SPAC9G1.06c","SPBC3F6.05","SPCC1672.06c"],"gene_count":21,"ltp_gene_count":18,"approved_date":"2021-04-02"},{"uniquename":"PMID:9559549","title":"Identification and analysis of homologues of Saccharomyces cerevisiae Spt3 suggest conserved functional domains.","citation":"Yeast 1998 Mar 30;14(5):409-17","abstract":"Spt3 of Saccharomyces cerevisiae is a factor required for normal transcription from particular RNA polymerase II-dependent promoters. As a step towards analysing Spt3 structure-function relationships, we have identified and studied Spt3 homologues from three other yeasts: Kluyveromyces lactis, Clavispora opuntiae and Schizosaccharomyces pombe. Alignment of their predicted amino acid sequences shows an overall identity of 30% between all four homologues and suggests that three conserved domains are present in Spt3. When tested for function in S. cerevisiae, K. lactis SPT3 was shown to fully complement and S. pombe SPT3 to partially complement an spt3 delta mutation. These data demonstrate that Spt3 is functionally conserved among distantly related yeasts.","authors":"Madison JM, Winston F","authors_abbrev":"Madison JM et al.","pubmed_publication_date":"30 Mar 1998","pubmed_entrez_date":"1998-04-29","publication_year":"1998","canto_session_key":"105d5a2707e2b51b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-04-12 14:35:14","canto_session_submitted_date":"2012-03-03 16:32:54","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC61.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-03-03"},{"uniquename":"PMID:4695223","title":"The effect of liquid holding in Schizosaccharomyces pombe strains after gamma and ultraviolet irradiation.","citation":"Radiat Res 1973 Feb;53(2):216-25","abstract":"","authors":"Shahin MM, Gentner NE, Nasim A","authors_abbrev":"Shahin MM et al.","pubmed_publication_date":"Feb 1973","pubmed_entrez_date":"1973-02-01","publication_year":"1973","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12526748","title":"A new role for the transcriptional corepressor SIN3; regulation of centromeres.","citation":"Curr Biol 2003 Jan 08;13(1):68-72","abstract":"Centromeres play a vital role in maintaining the genomic stability of eukaryotes by coordinating the equal distribution of chromosomes to daughter cells during mitosis and meiosis. Fission yeast (S. pombe) centromeres consist of a 4-9 kb central core region and 30-100 kb of flanking inner (imr/B) and outer (otr/K) repeats. These sequences direct a laminar kinetochore structure similar to that of human centromeres. Centromeric heterochromatin is generally underacetylated. We have previously shown that inhibition of histone deacetylases (HDACs) caused hyperacetylation of centromeres and defective chromosome segregation. SIN3 is a HDAC corepressor that has the ability to mediate HDAC targeting in the repression of promoters. In this study, we have characterized S. pombe sin three corepressors (Pst1p and Pst2p) to investigate whether SIN3-HDAC is required in the regulation of centromeres. We show that only pst1-1 and not pst2Delta cells displayed anaphase defects and thiabendazole sensitivity. pst1-1 cells showed reduced centromeric silencing, increased histone acetylation in centromeric chromatin, and defective centromeric sister chromatid cohesion. The HDAC Clr6p and Pst1p coimmunoprecipitated, and Pst1p colocalized with centromeres, particularly in binucleate cells. These data are consistent with a model in which Pst1p-Clr6p temporally associate with centromeres to carry out the initial deacetylation necessary for subsequent steps in heterochromatin formation.","authors":"Silverstein RA, Richardson W, Levin H, Allshire R, Ekwall K","authors_abbrev":"Silverstein RA et al.","pubmed_publication_date":"08 Jan 2003","pubmed_entrez_date":"2003-01-16","publication_year":"2003","canto_session_key":"dea291f22cf98fe2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-04-08 14:39:08","canto_approved_date":"2025-09-04 11:04:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-25 10:39:14","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPBC36.05c","SPAC664.01c","SPBC12C2.10c","SPAC23C11.15"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-04-08"},{"uniquename":"PMID:14575697","title":"Identification of a SNARE protein required for vacuolar protein transport in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2003 Nov 07;311(1):77-82","abstract":"Intracellular vesicle trafficking is mediated by a set of SNARE proteins in eukaryotic cells. Several SNARE proteins are required for vacuolar protein transport and vacuolar biogenesis in Saccharomyces cerevisiae. A search of the Schizosaccharomyces pombe genome database revealed a total of 17 SNARE-related genes. Although no homologs of Vam3p, Nyv1p, and Vam7p have been found in S. pombe, we identified one SNARE-like protein that is homologous to S. cerevisiae Pep12p. However, the disruptants transport vacuolar hydrolase CPY (SpCPY) to the vacuole normally, suggesting that the Pep12 homolog is not required for vacuolar protein transport in S. pombe cells. To identify the SNARE protein(s) involved in Golgi-to-vacuole protein transport, we have deleted four SNARE homolog genes in S. pombe. SpCPY was significantly missorted to the cell surface on deletion of one of the SNARE proteins, Fsv1p (SPAC6F12.03c), with no apparent S. cerevisiae ortholog. In addition, sporulation, endocytosis, and in vivo vacuolar fusion appear to be normal in fsv1Delta cells. These results showed that Fsv1p is mainly involved in vesicle-mediated protein transport between the Golgi and vacuole in S. pombe cells.","authors":"Takegawa K, Hosomi A, Iwaki T, Fujita Y, Morita T, Tanaka N","authors_abbrev":"Takegawa K et al.","pubmed_publication_date":"07 Nov 2003","pubmed_entrez_date":"2003-10-25","publication_year":"2003","canto_session_key":"1c2a91bb312f9e9e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-21 17:15:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-21 17:15:37","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.10c","SPAC6F12.03c","SPAC458.05","SPAC4G8.10","SPAC823.05c","SPBC31E1.04","SPBC36B7.07"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2015-04-21"},{"uniquename":"PMID:17502373","title":"Fission yeast Rnf4 homologs are required for DNA repair.","citation":"J Biol Chem 2007 Jul 13;282(28):20388-94","abstract":"We describe two RING finger proteins in the fission yeast Schizosaccharomyces pombe, Rfp1 and Rfp2. We show that these proteins function redundantly in DNA repair. Rfp1 was isolated as a Chk1-interacting protein in a two-hybrid screen and has high amino acid sequence similarity to Rfp2. Deletion of either gene does not cause a phenotype, but a double deletion (rfp1Deltarfp2Delta) showed poor viability and defects in cell cycle progression. These cells are also sensitive to DNA-damaging agents, although they maintained normal checkpoint signaling to Chk1. Rfp1 and Rfp2 are most closely related to human Rnf4, and we showed that Rnf4 can substitute functionally for Rfp1 and/or Rfp2. The double mutants also showed significantly increased levels of protein SUMOylation, and we identified an S. pombe Ulp2/Smt4 homolog that, when overexpressed, reduced SUMO levels and suppressed the DNA damage sensitivity of rfp1Delta rfp2Delta cells.","authors":"Kosoy A, Calonge TM, Outwin EA, O'Connell MJ","authors_abbrev":"Kosoy A et al.","pubmed_publication_date":"13 Jul 2007","pubmed_entrez_date":"2007-05-16","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19A8.10","SPAC8E11.02c","SPCC1450.11c","SPAC19A8.12","SPCC1919.15","SPCC1259.13","SPCC1795.11","SPCC613.03","SPAC343.18"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:19633696","title":"HAT-HDAC interplay modulates global histone H3K14 acetylation in gene-coding regions during stress.","citation":"EMBO Rep 2009 Sep;10(9):1009-14","abstract":"Histone acetylation and deacetylation are important for gene regulation. The histone acetyltransferase, Gcn5, is an activator of transcriptional initiation that is recruited to gene promoters. Here, we map genome-wide Gcn5 occupancy and histone H3K14ac at high resolution. Gcn5 is predominantly localized to coding regions of highly transcribed genes, where it collaborates antagonistically with the class-II histone deacetylase, Clr3, to modulate H3K14ac levels and transcriptional elongation. An interplay between Gcn5 and Clr3 is crucial for the regulation of many stress-response genes. Our findings suggest a new role for Gcn5 during transcriptional elongation, in addition to its known role in transcriptional initiation.","doi":"10.1038/embor.2009.127","authors":"Johnsson A, Durand-Dubief M, Xue-Franzén Y, Rönnerblad M, Ekwall K, Wright A","authors_abbrev":"Johnsson A et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-07-28","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G9.07c","SPAC1952.05","SPBC800.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:9519900","title":"Yeast myosin II: a new subclass of unconventional conventional myosins?","citation":"Cell Motil Cytoskeleton 1998;39(3):195-200","abstract":"Myosin II is the founder member of a large and structurally diverse clan of actin-based motor proteins. The native myosin II molecule is a hexamer consisting of two heavy chains, two essential light chains (ELC), and two regulatory light chains (RLC). For convenience, the myosin IIs are often subdivided into four subclasses: vertebrate skeletal and cardiac muscle myosin II form one subclass, vertebrate smooth muscle and nonmuscle myosin II a second, invertebrate muscle a third, and protozoan myosin II a fourth [Sellers and Goodson, 1995]. Different mechanisms of regulation may exist between myosins within a single subclass yet all myosin IIs share a common three-domain structure; the N-terminus of the heavy chain forms two globular heads that contain the ATP- and actin-binding sites and the alpha-helical neck region that is stabilised by the binding of the two classes of light chains, whilst the C-terminus forms an extended coiled-coil tail that can consist of anywhere between 700 and 1,200 amino acids. In nonmuscle cells, myosin II has at least two well-defined functions, cell locomotion and cytokinesis. Yeast cells do not locomote, and their mechanism of cytokinesis involves the deposition of a cross-wall or septum. However, in the fission yeast, Schizosaccharomyces pombe, deposition of the septum is anticipated by the appearance of a contractile actomyosin ring [Marks and Hyams, 1985; May et al., 1997; Kitayama et al., 1997] and actin is also present at the bud neck during cytokinesis in the budding yeast, Saccharomyces cerevisiae [Kilmartin and Adams, 1984]. Here we report a phylogenetic analysis of the N-terminal head domains of the myosin IIs from both yeasts, a structural analysis of the tail domains of these proteins and we speculate as to the nature of the light chains that regulate their function. On the basis of these findings, we propose that the yeast myosin IIs constitute a divergent fifth class of \"unconventional\" conventional myosins.","authors":"May KM, Win TZ, Hyams JS","authors_abbrev":"May KM et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-03-31","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000091","title":"Representation of cell migration as biological processes in the Gene Ontology","abstract":"We have created a standard template for classes describing the cell migration process for a cell type as a biological process. The underlying equivalence axiom template is \"'cell migration' and 'alters_location_of' some C\", where C is a native cell (CL:0000004).","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22500803","title":"EBs recognize a nucleotide-dependent structural cap at growing microtubule ends.","citation":"Cell 2012 Apr 13;149(2):371-82","abstract":"Growing microtubule ends serve as transient binding platforms for essential proteins that regulate microtubule dynamics and their interactions with cellular substructures. End-binding proteins (EBs) autonomously recognize an extended region at growing microtubule ends with unknown structural characteristics and then recruit other factors to the dynamic end structure. Using cryo-electron microscopy, subnanometer single-particle reconstruction, and fluorescence imaging, we present a pseudoatomic model of how the calponin homology (CH) domain of the fission yeast EB Mal3 binds to the end regions of growing microtubules. The Mal3 CH domain bridges protofilaments except at the microtubule seam. By binding close to the exchangeable GTP-binding site, the CH domain is ideally positioned to sense the microtubule's nucleotide state. The same microtubule-end region is also a stabilizing structural cap protecting the microtubule from depolymerization. This insight supports a common structural link between two important biological phenomena, microtubule dynamic instability and end tracking.","doi":"10.1016/j.cell.2012.02.049","authors":"Maurer SP, Fourniol FJ, Bohner G, Moores CA, Surrey T","authors_abbrev":"Maurer SP et al.","pubmed_publication_date":"13 Apr 2012","pubmed_entrez_date":"2012-04-17","publication_year":"2012","canto_session_key":"4ae00e4a028f2c80","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-19 13:41:46","canto_approved_date":"2019-11-19 13:41:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-19 13:41:38","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPAC18G6.15","SPBC16A3.15c","SPBC800.05c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-11-19","pdb_entries":[{"pdb_id":"4abo","gene_chains":[{"gene_uniquename":"SPAC18G6.15","chain":"I","position":"2-142"}],"title":"Mal3 CH domain homology model and mammalian tubulin (2XRP) docked into the 8.6-Angstrom cryo-EM map of Mal3-GTPgammaS-microtubules","entry_authors":"Maurer SP,Fourniol FJ,Bohner G,Moores CA,Surrey T","entry_authors_abbrev":"Maurer SP et al.","reference_uniquename":"PMID:22500803","experimental_method":"EM","resolution":"8.6"}]},{"uniquename":"PMID:23358415","title":"γH2A-binding protein Brc1 affects centromere function in fission yeast.","citation":"Mol Cell Biol 2013 Apr;33(7):1410-6","abstract":"The coordinated replication and transcription of pericentromeric repeats enable RNA interference (RNAi)-mediated transmission of pericentromeric heterochromatin in fission yeast, which is essential for the proper function of centromeres. Rad3/ATR kinase phosphorylates histone H2A on serine-128/-129 to create γH2A in pericentromeric heterochromatin during S phase, which recruits Brc1 through its breast cancer gene 1 protein (BRCA1) C-terminal (BRCT) domains. Brc1 prevents the collapse of stalled replication forks; however, it is unknown whether this activity influences centromere function. Here, we show that Brc1 localizes in pericentromeric heterochromatin during S phase, where it enhances Clr4/Suv39-mediated H3 lysine-9 dimethylation (H3K9me2) and gene silencing. Loss of Brc1 increases sensitivity to the microtubule-destabilizing drug thiabendazole (TBZ) and increases chromosome missegregation in the presence of TBZ. Brc1 retains significant function even when it cannot bind γH2A. However, elimination of the serine-121 site on histone H2A, a target of Bub1 spindle assembly checkpoint kinase, sensitizes γH2A-deficient and brc1Δ cells to replication stress and microtubule destabilization. Collective results suggest that Brc1-mediated stabilization of stalled replication forks is necessary for fully efficient transmission of pericentromeric heterochromatin, which is required for accurate chromosome segregation during mitosis.","doi":"10.1128/MCB.01654-12","authors":"Lee SY, Rozenzhak S, Russell P","authors_abbrev":"Lee SY et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2013-01-30","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.05c","SPAC664.01c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:10967139","title":"The genomic structure of c14orf1 is conserved across eukarya.","citation":"Mamm Genome 2000 Sep;11(9):786-8","abstract":"We have recently cloned the gene C14orf1, which is strongly expressed in normal testis and in several cancer cell lines and tumors. This gene maps to 14q24.3 and is interrupted by four introns. Two of them are also represented in the open reading frame of Schizosaccharomyces pombe in the same phase. In Arabidopsis taliana only the first of the two introns was found, in the same phase as the corresponding ones in S. pombe and human. Disruption of the ortholog in Saccharomyces cerevisiae (Yer044c) led to a severe growth defect, and C14orf1 failed to complement mutant yeast when put under the control of the natural Yer044c promoter. Further studies are needed to understand the causes underlying the high degree of conservation of the C14orf1 genomic structure.","authors":"Ottolenghi C, Daizadeh I, Ju A, Kossida S, Renault G, Jacquet M, Fellous A, Gilbert W, Veitia R","authors_abbrev":"Ottolenghi C et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-09-01","publication_year":"2000","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20852022","title":"Characterization of glycoside hydrolase family 5 proteins in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2010 Nov;9(11):1650-60","abstract":"In yeast, enzymes with β-glucanase activity are thought to be necessary in morphogenetic events that require controlled hydrolysis of the cell wall. Comparison of the sequence of the Saccharomyces cerevisiae exo-β(1,3)-glucanase Exg1 with the Schizosaccharomyces pombe genome allowed the identification of three genes that were named exg1(+) (locus SPBC1105.05), exg2(+) (SPAC12B10.11), and exg3(+) (SPBC2D10.05). The three proteins have different localizations: Exg1 is secreted to the periplasmic space, Exg2 is a membrane protein, and Exg3 is a cytoplasmic protein. Characterization of the biochemical activity of the proteins indicated that Exg1 and Exg3 are active only against β(1,6)-glucans while no activity was detected for Exg2. Interestingly, Exg1 cleaves the glucans with an endohydrolytic mode of action. exg1(+) showed periodic expression during the cell cycle, with a maximum coinciding with the septation process, and its expression was dependent on the transcription factor Sep1. The Exg1 protein localizes to the septum region in a pattern that was different from that of the endo-β(1,3)-glucanase Eng1. Overexpression of Exg2 resulted in an increase in cell wall material at the poles and in the septum, but the putative catalytic activity of the protein was not required for this effect.","doi":"10.1128/EC.00187-10","authors":"Dueñas-Santero E, Martín-Cuadrado AB, Fontaine T, Latgé JP, del Rey F, Vázquez de Aldana C","authors_abbrev":"Dueñas-Santero E et al.","pubmed_publication_date":"Nov 2010","pubmed_entrez_date":"2010-09-21","publication_year":"2010","canto_session_key":"a0941171b84a6b67","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-07 12:45:13","canto_approved_date":"2025-12-31 11:38:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-07 12:44:49","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4C3.12","SPBC1105.05","SPAC6G10.12c","SPBC2D10.05","SPAC12B10.11","SPAC821.09"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-09-07"},{"uniquename":"PMID:12972644","title":"Mitochondrial positioning in fission yeast is driven by association with dynamic microtubules and mitotic spindle poles.","citation":"Proc Natl Acad Sci U S A 2003 Sep 30;100(20):11424-8","abstract":"Microtubules mediate mitochondrial distribution in the yeast Schizosaccharomyces pombe and many higher eukaryotic cells. In higher eukaryotes, kinesin motor proteins have been shown to transport mitochondria along microtubules, but the nature of the mitochondria-microtubule interactions in S. pombe has not been explored. By time lapse, total internal reflection fluorescence microscopy, or spinning-disk confocal microscopy, mitochondria appeared to be both tethered to ends and bound laterally along the sides of microtubules. Mitochondrial tubules extended and retracted when attached to the tips of elongating or shortening microtubules, respectively, but translocation along established microtubules was never observed. Mitochondria that were not associated with microtubules were largely immobile until they were \"captured\" by a growing microtubule. In mitotic cells, a portion of the mitochondria was tethered to the spindle-pole bodies and moved to the cellular ends during spindle elongation. This association may be important for organelle inheritance during cell division. Thus, in contrast to kinesin-mediated transport used by higher eukaryotes, mitochondrial motility and distribution in fission yeast are driven largely by microtubule polymerization and the elongation of the mitotic spindle.","authors":"Yaffe MP, Stuurman N, Vale RD","authors_abbrev":"Yaffe MP et al.","pubmed_publication_date":"30 Sep 2003","pubmed_entrez_date":"2003-09-16","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34436628","title":"Variables Influencing Differences in Sequence Conservation in the Fission Yeast Schizosaccharomyces pombe.","citation":"J Mol Evol 2021 Dec;89(9-10):601-610","abstract":"Which variables determine the constraints on gene sequence evolution is one of the most central questions in molecular evolution. In the fission yeast Schizosaccharomyces pombe, an important model organism, the variables influencing the rate of sequence evolution have yet to be determined. Previous studies in other single celled organisms have generally found gene expression levels to be most significant, with numerous other variables such as gene length and functional importance identified as having a smaller impact. Using publicly available data, we used partial least squares regression, principal components regression, and partial correlations to determine the variables most strongly associated with sequence evolution constraints. We identify centrality in the protein-protein interactions network, amino acid composition, and cellular location as the most important determinants of sequence conservation. However, each factor only explains a small amount of variance, and there are numerous variables having a significant or heterogeneous influence. Our models explain more than half of the variance in dN, raising the possibility that future refined models could quantify the role of stochastics in evolutionary rate variation.","doi":"10.1007/s00239-021-10028-y","authors":"Harnqvist SE, Grace CA, Jeffares DC","authors_abbrev":"Harnqvist SE et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-08-26","publication_year":"2021","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-08-28 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37615341","title":" Schizosaccharomyces pombe  Rtf2 is important for replication fork barrier activity of  RTS1  via splicing of  Rtf1 .","citation":"Elife 2023 Aug 24;12","abstract":"Arrested replication forks, when restarted by homologous recombination, result in error-prone DNA syntheses and non-allelic homologous recombination. Fission yeast  RTS1  is a model fork barrier used to probe mechanisms of recombination-dependent restart.  RTS1  barrier activity is entirely dependent on the DNA binding protein Rtf1 and partially dependent on a second protein, Rtf2. Human RTF2 was recently implicated in fork restart, leading us to examine fission yeast Rtf2's role in more detail. In agreement with previous studies, we observe reduced barrier activity upon  rtf2  deletion. However, we identified Rtf2 to be physically associated with mRNA processing and splicing factors and  rtf2  deletion to cause increased intron retention. One of the most affected introns resided in the  rtf1  transcript. Using an intronless  rtf1,  we observed no reduction in RFB activity in the absence of Rtf2. Thus, Rtf2 is essential for correct  rtf1  splicing to allow optimal  RTS1  barrier activity.","doi":"10.7554/eLife.78554","authors":"Budden AM, Eravci M, Watson AT, Campillo-Funollet E, Oliver AW, Naiman K, Carr AM","authors_abbrev":"Budden AM et al.","pubmed_publication_date":"24 Aug 2023","pubmed_entrez_date":"2023-08-24","publication_year":"2023","canto_session_key":"63c808bbf4024255","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tony Carr","canto_first_approved_date":"2024-04-18 09:50:29","canto_approved_date":"2024-04-18 09:50:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-09 10:05:07","canto_added_date":"2023-08-25 00:15:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":145,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Tony Carr","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC222.09","SPAC9.03c","SPAC24B11.11c","SPBC1711.05","SPBC2F12.04","SPBC1711.17","SPBC646.10c","SPBC211.02c","SPCP31B10.05","SPAC3H8.07c","SPAC167.03c","SPAC3A12.11c","SPAC644.12","SPAC26H5.04","SPBC18H10.15","SPBC36.05c","SPAC630.14c","SPAC20G8.09c","SPAC2G11.14","SPBC839.10","SPCC1620.09c","SPBC1711.07","SPBC1734.01c","SPAC22G7.09c","SPBC25H2.12c","SPBC13E7.01","SPAC4A8.09c","SPAC19A8.15","SPAC23D3.07","SPCC663.01c","SPAC806.02c","SPAC57A10.10c","SPBC13G1.08c","SPBC1604.21c","SPBC1539.10","SPAC20G8.01","SPAC1783.05","SPCC736.12c","SPAC1D4.04","SPBC1289.11","SPCC1739.14","SPBC409.09c","SPBC4B4.09","SPAC16.02c","SPAC23G3.06","SPBC13E7.02","SPCC191.02c","SPCC1672.02c","SPCC1906.02c","SPAC17A5.06","SPAC5H10.10","SPCC188.11","SPBC887.03c","SPCC1442.09","SPAC6F6.03c","SPAC3G9.09c","SPAC9E9.09c","SPCC613.06","SPAC23H4.06","SPBC119.01","SPBC428.02c","SPAC24H6.07","SPAC631.01c","SPAC821.06","SPBC17G9.04c","SPAC22F8.10c","SPAC13A11.02c","SPAC23C11.15","SPAC1071.09c","SPAC24C9.11","SPAC644.16","SPBC1709.15c","SPBC19C7.06","SPCC1739.13","SPCC320.10","SPAC4D7.10c","SPAC1805.17","SPBC11B10.10c","SPBC31F10.11c","SPAPB24D3.08c","SPBC3F6.04c","SPAC22F8.07c","SPCC364.02c","SPBC609.05","SPAC144.04c","SPAC22G7.05","SPAC21E11.05c","SPCC18B5.07c","SPBC19G7.15","SPAC5H10.03","SPCC970.10c","SPBC337.05c","SPBC800.06","SPBC409.17c","SPAC16.04","SPBC1347.03","SPAC23C4.19","SPAC1805.12c","SPAC227.08c","SPAC56F8.08","SPBC13E7.08c","SPBC3B9.01","SPBC215.03c","SPCP1E11.10","SPBC25D12.04","SPAC56E4.04c","SPBC216.06c","SPAC26A3.15c","SPAC664.03","SPBC12C2.10c","SPAC1D4.09c","SPCC1620.11","SPBC8D2.06","SPAC4A8.08c","SPCP25A2.03","SPAC17G6.10","SPAC1B3.09c","SPAC926.08c","SPBC19C2.01","SPAC57A7.06","SPAC29A4.08c","SPBC15D4.15","SPBC3E7.10","SPAC30D11.04c","SPBC1604.08c","SPBC21H7.07c","SPBC16D10.07c","SPBC800.08","SPAC10F6.02c","SPBC337.06c","SPCC737.06c","SPBC1A4.02c","SPBC1A4.08c"],"gene_count":133,"ltp_gene_count":132,"approved_date":"2024-04-18"},{"uniquename":"PMID:12102630","title":"Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: role of redox chemistry and a conserved aspartate.","citation":"Biochemistry 2002 Jul 16;41(28):8876-85","abstract":"ISU-type proteins mediate cluster transfer to apo protein targets. Rate constants have been determined for cluster transfer from ISU to apo Fd for both Homo sapiens and Schizosaccharomyces pombe proteins, and cross reactions have also been examined. Substitution of a key aspartate residue of ISU is found to decrease the rate of cluster transfer by at least an order of magnitude (for wild-type Hs ISU cluster transfer to Hs apo Fd, k(2) approximately 540 M(-1) min(-1), relative 56 M(-1) min(-1) for D37A ISU). This change in rate constant does not reflect any change in binding affinity of the ISU and Fd proteins. The pH dependencies of cluster transfer rates are similar for WT and D37A ISU, arguing against a role for Asp37 as a catalytic base, although evidence for general base catalysis mediating deprotonation of Cys from the apo target is supported by an observed pK(a) of 6.9 determined from the pH profiles for both WT and D37A ISU. Such a pK(a) value is at the lower limit for Cys and is common for solvent-accessible Cys thiols. The temperature dependence of the rate constant defining the cluster transfer reaction for wild type versus the aspartate derivative is distinct. Thermal activation parameters (DeltaH and DeltaS) are consistent with a solvent-accessible ISU-bound cluster, with desolvation as a principle barrier to cluster transfer. Experiments to determine the dependence of reaction rate constants on viscosity indicate cluster transfer to be rate-limiting. Fully oxidized cluster appears to be the natural state for transfer to target proteins. Reduced Fd does not readily reduce ISU-bound [2Fe-2S](2+) and does not promote cluster transfer to an apo Fd target.","authors":"Wu SP, Wu G, Surerus KK, Cowan JA","authors_abbrev":"Wu SP et al.","pubmed_publication_date":"16 Jul 2002","pubmed_entrez_date":"2002-07-10","publication_year":"2002","canto_session_key":"413f9c27bbcf0d46","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-04 09:50:00","canto_approved_date":"2023-05-15 17:19:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-19 10:33:35","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.10c","SPAC227.13c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-10-04"},{"uniquename":"PMID:19055762","title":"Module evolution and substrate specificity of fungal nonribosomal peptide synthetases involved in siderophore biosynthesis.","citation":"BMC Evol Biol 2008 Dec 03;8:328","abstract":"Most filamentous ascomycete fungi produce high affinity iron chelators called siderophores, biosynthesized nonribosomally by multimodular adenylating enzymes called nonribosomal peptide synthetases (NRPSs). While genes encoding the majority of NRPSs are intermittently distributed across the fungal kingdom, those encoding ferrichrome synthetase NRPSs, responsible for biosynthesis of ferrichrome siderophores, are conserved, which offers an opportunity to trace their evolution and the genesis of their multimodular domain architecture. Furthermore, since the chemistry of many ferrichromes is known, the biochemical and structural 'rules' guiding NRPS substrate choice can be addressed using protein structural modeling and evolutionary approaches.\nA search of forty-nine complete fungal genome sequences revealed that, with the exception of Schizosaccharomyces pombe, none of the yeast, chytrid, or zygomycete genomes contained a candidate ferrichrome synthetase. In contrast, all filamentous ascomycetes queried contained at least one, while presence and numbers in basidiomycetes varied. Genes encoding ferrichrome synthetases were monophyletic when analyzed with other NRPSs. Phylogenetic analyses provided support for an ancestral duplication event resulting in two main lineages. They also supported the proposed hypothesis that ferrichrome synthetases derive from an ancestral hexamodular gene, likely created by tandem duplication of complete NRPS modules. Recurrent losses of individual domains or complete modules from this ancestral gene best explain the diversity of extant domain architectures observed. Key residues and regions in the adenylation domain pocket involved in substrate choice and for binding the amino and carboxy termini of the substrate were identified.\nIron-chelating ferrichrome synthetases appear restricted to fission yeast, filamentous ascomycetes, and basidiomycetes and fall into two main lineages. Phylogenetic analyses suggest that loss of domains or modules led to evolution of iterative biosynthetic mechanisms that allow flexibility in biosynthesis of the ferrichrome product. The 10 amino acid NRPS code, proposed earlier, failed when we tried to infer substrate preference. Instead, our analyses point to several regions of the binding pocket important in substrate choice and suggest that two positions of the code are involved in substrate anchoring, not substrate choice.","doi":"10.1186/1471-2148-8-328","authors":"Bushley KE, Ripoll DR, Turgeon BG","authors_abbrev":"Bushley KE et al.","pubmed_publication_date":"03 Dec 2008","pubmed_entrez_date":"2008-12-06","publication_year":"2008","canto_session_key":"41d41c3d9a8d754f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-23 18:34:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-23 09:36:24","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-23"},{"uniquename":"PMID:27444384","title":"The iron uptake repressor Fep1 in the fission yeast binds Fe-S cluster through conserved cysteines.","citation":"Biochem Biophys Res Commun 2016 Sep 09;478(1):187-192","abstract":"Iron homeostasis is tightly regulated since iron is an essential but toxic element in the cell. The GATA-type transcription factor Fep1 and its orthologs contribute to iron homeostasis in many fungi by repressing genes for iron uptake when intracellular iron is high. Even though the function and interaction partners of Fep1 have been elucidated extensively In Schizosaccharomyces pombe, the mechanism behind iron-sensing by Fep1 remains elusive. It has been reported that Fep1 interacts with Fe-S-containing monothiol glutaredoxin Grx4 and Grx4-Fra2 complex. In this study, we demonstrate that Fep1 also binds iron, in the form of Fe-S cluster. Spectroscopic and biochemical analyses of as isolated and reconstituted Fep1 suggest that the dimeric Fep1 binds Fe-S clusters. The mutation study revealed that the cluster-binding depended on the conserved cysteines located between the two zinc fingers in the DNA binding domain. EPR analyses revealed [Fe-S]-specific peaks indicative of mixed presence of [2Fe-2S], [3Fe-4S], or [4Fe-4S]. The finding that Fep1 is an Fe-S protein fits nicely with the model that the Fe-S-trafficking Grx4 senses intracellular iron environment and modulates the activity of Fep1.","doi":"10.1016/j.bbrc.2016.07.070","authors":"Kim HJ, Lee KL, Kim KD, Roe JH","authors_abbrev":"Kim HJ et al.","pubmed_publication_date":"09 Sep 2016","pubmed_entrez_date":"2016-07-23","publication_year":"2016","canto_session_key":"a0f6f6a0c5ab5507","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jung-Hye Roe","canto_first_approved_date":"2016-08-08 10:30:28","canto_approved_date":"2022-02-01 17:11:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-04 01:30:55","canto_added_date":"2016-07-26 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jung-Hye Roe","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23E2.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-08-08"},{"uniquename":"PMID:19516334","title":"Flipping of alkylated DNA damage bridges base and nucleotide excision repair.","citation":"Nature 2009 Jun 11;459(7248):808-13","abstract":"Alkyltransferase-like proteins (ATLs) share functional motifs with the cancer chemotherapy target O(6)-alkylguanine-DNA alkyltransferase (AGT) and paradoxically protect cells from the biological effects of DNA alkylation damage, despite lacking the reactive cysteine and alkyltransferase activity of AGT. Here we determine Schizosaccharomyces pombe ATL structures without and with damaged DNA containing the endogenous lesion O(6)-methylguanine or cigarette-smoke-derived O(6)-4-(3-pyridyl)-4-oxobutylguanine. These results reveal non-enzymatic DNA nucleotide flipping plus increased DNA distortion and binding pocket size compared to AGT. Our analysis of lesion-binding site conservation identifies new ATLs in sea anemone and ancestral archaea, indicating that ATL interactions are ancestral to present-day repair pathways in all domains of life. Genetic connections to mammalian XPG (also known as ERCC5) and ERCC1 in S. pombe homologues Rad13 and Swi10 and biochemical interactions with Escherichia coli UvrA and UvrC combined with structural results reveal that ATLs sculpt alkylated DNA to create a genetic and structural intersection of base damage processing with nucleotide excision repair.","doi":"10.1038/nature08076","authors":"Tubbs JL, Latypov V, Kanugula S, Butt A, Melikishvili M, Kraehenbuehl R, Fleck O, Marriott A, Watson AJ, Verbeek B, McGown G, Thorncroft M, Santibanez-Koref MF, Millington C, Arvai AS, Kroeger MD, Peterson LA, Williams DM, Fried MG, Margison GP, Pegg AE, Tainer JA","authors_abbrev":"Tubbs JL et al.","pubmed_publication_date":"11 Jun 2009","pubmed_entrez_date":"2009-06-12","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1250.04c","SPBC3E7.08c","SPBC649.03","SPAC3G6.06c"],"gene_count":4,"ltp_gene_count":4,"pdb_entries":[{"pdb_id":"3gx4","gene_chains":[{"gene_uniquename":"SPAC1250.04c","chain":"X","position":"1-108"}],"title":"Crystal Structure Analysis of S. Pombe ATL in complex with DNA","entry_authors":"Tubbs JL,Arvai AS,Tainer JA","entry_authors_abbrev":"Tubbs JL et al.","reference_uniquename":"PMID:19516334","experimental_method":"X-ray","resolution":"2.7"},{"pdb_id":"3gva","gene_chains":[{"gene_uniquename":"SPAC1250.04c","chain":"A/B","position":"1-108"}],"title":"Crystal Structure Analysis of S. Pombe ATL","entry_authors":"Tubbs JL,Arvai AS,Tainer JA","entry_authors_abbrev":"Tubbs JL et al.","reference_uniquename":"PMID:19516334","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"3gyh","gene_chains":[{"gene_uniquename":"SPAC1250.04c","chain":"X","position":"1-108"}],"title":"Crystal Structure Analysis of S. Pombe ATL in complex with damaged DNA containing POB","entry_authors":"Tubbs JL,Arvai AS,Tainer JA,Shin DS","entry_authors_abbrev":"Tubbs JL et al.","reference_uniquename":"PMID:19516334","experimental_method":"X-ray","resolution":"2.8"}]},{"uniquename":"EMBL:K00771","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPRRNA.41"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8621569","title":"Characterization of a nuclear protein conferring brefeldin A resistance in Schizosaccharomyces pombe.","citation":"J Biol Chem 1996 Apr 12;271(15):9166-71","abstract":"The fungal metabolite brefeldin A disrupts protein secretion and causes the redistribution of the Golgi complex to the endoplasmic reticulum. Previously we isolated six genes that, when present in multiple copies, confer brefeldin A resistance to wild type Schizosaccharomyces pombe. Here we describe the characterization of one of these genes, hba1. This gene encodes an essential protein that shares homology with the mammalian protein RanBP1 and the protein encoded by the Saccharomyces cerevisiae gene YRB1 and contains a peptide motif present in several proteins found within the nuclear pore complex. The protein encoded by hba1 is localized to the nucleus, and it was determined that this protein is phosphorylated in vivo. The characterization of hba1 thus demonstrates a novel mechanism of drug resistance in S. pombe.","authors":"Turi TG, Mueller UW, Sazer S, Rose JK","authors_abbrev":"Turi TG et al.","pubmed_publication_date":"12 Apr 1996","pubmed_entrez_date":"1996-04-12","publication_year":"1996","canto_session_key":"10092d733e710515","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-07-31 14:53:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 14:53:42","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:2164794","title":"A versatile microtiter assay for the universal cdc2 cell cycle regulator.","citation":"Anal Biochem 1990 May 15;187(1):94-7","abstract":"A microassay for p34cdc2 based on the high affinity association between cdc2 and Schizosaccharomyces pombe p13suc1 has been developed. p13 purified from Escherichia coli was immobilized on microtiter plates and cellular lysate was incubated in the wells to allow the binding of cdc2 and its associated proteins. p34cdc2 was assayed either as a histone kinase or by immunological methods. The method was optimized for S. pombe cell extracts but can also be applied to other organisms such as Xenopus oocytes or HeLa cells. This rapid assay allows the specific determination of p34cdc2 histone H1 kinase activity in a very large number of samples.","authors":"Ducommun B, Beach D","authors_abbrev":"Ducommun B et al.","pubmed_publication_date":"15 May 1990","pubmed_entrez_date":"1990-05-15","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24173340","title":"Multiple drug resistance in the fission yeast Schizosaccharomyces pombe: Correlation between drug and amino acid uptake and membrane ATPase activities.","citation":"Curr Genet 1983 Jul;7(4):299-307","abstract":"Cyh3 and cyh4, multiple drug resistant strains of Schizosaccharomyces pombe, show a much reduced uptake of trichodermin, chloramphenicol, cycloheximide, L-lysine, glycine, L-threonine, L-glutamine, L-arginine and L-glutamic acid when compared to wild type. The plasma membrane and mitochondrial ATPase activities of these mutants are also greatly reduced. Since the uptake of such compounds is likely to be driven by a proton electrochemical gradient set up by the membrane ATPase it is suggested that the primary effect of these mutations is at the level of the membrane ATPase. Another drug resistant strain, cyh1, which is resistant only to high levels of cycloheximide, shows increased uptake of trichodermin, L-lysine, glycine, L-threonine, L-glutamine when compared to wild type. The plasma membrane and mitochondrial ATPases of cyh1 are considerably greater than those of wild type. It has been shown previously that cyh1 possesses an altered 60S ribosonal subunit protein when compared to wild type and this makes it resistant to cycloheximide. There is no obvious explanation as to how this change could lead to the alterations in drug and amino acid uptake and in ATPase activities observed.","doi":"10.1007/BF00376075","authors":"Johnston PA, Coddington A","authors_abbrev":"Johnston PA et al.","pubmed_publication_date":"Jul 1983","pubmed_entrez_date":"2013-11-01","publication_year":"1983","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39540318","title":"Pck2 association with the plasma membrane and efficient response of the cell integrity pathway require regulation of PI4P homeostasis by exomer.","citation":"Open Biol 2024 Nov;14(11):240101","abstract":"Exomer is a protein complex that facilitates trafficking between the Golgi and the plasma membrane (PM).  Schizosaccharomyces pombe  exomer is composed of Cfr1 and Bch1, and we have found that full activation of the cell integrity pathway (CIP) in response to osmotic stress requires exomer. In the wild-type, the CIP activators Rgf1 (Rho1 GEF) and Pck2 (PKC homologue) and the MEK kinase Mkh1 localize in the PM, internalize after osmotic shock and re-localize after adaptation. This re-localization is inefficient in exomer mutants. Overexpression of the PM-associated 1-phosphatidylinositol 4-kinase  stt4+ , and deletion of the  nem1+  phosphatase suppress the defects in Pck2 dynamics in exomer mutants, but not their defect in CIP activation, demonstrating that exomer regulates CIP in additional ways. Exomer mutants accumulate PI4P in the TGN, and increasing the expression of the Golgi-associated 1-phosphatidylinositol 4-kinase  pik1+  suppresses their defect in Pck2 dynamics. These findings suggest that efficient PI4P transport from the Golgi to the PM requires exomer. Mutants lacking clathrin adaptors are defective in CIP activation, but not in Pck2 dynamics or in PI4P accumulation in the Golgi. Hence, traffic from the Golgi regulates CIP activation, and exomer participates in this regulation through an exclusive mechanism.","doi":"10.1098/rsob.240101","authors":"Moscoso-Romero E, Moro S, Duque A, Yanguas F, Valdivieso MH","authors_abbrev":"Moscoso-Romero E et al.","pubmed_publication_date":"Nov 2024","pubmed_entrez_date":"2024-11-14","publication_year":"2024","canto_session_key":"42317f42f3d8dfcb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Henar Valdivieso","canto_first_approved_date":"2025-03-03 10:05:08","canto_approved_date":"2025-03-03 10:05:08","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-02-11 09:19:50","canto_added_date":"2024-11-15 00:25:06","annotation_curators":[{"name":"Henar Valdivieso","community_curator":true,"annotation_count":64,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":35,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.14","SPAC6G9.12","SPAC11G7.01","SPCC794.11c","SPAC24B11.06c","SPBC25H2.16c","SPBP4H10.04","SPBC30B4.01c","SPAC1F3.02c","SPAC16.01","SPBC3B8.10c","SPCC645.07","SPBC12D12.04c","SPBP16F5.07","SPBC1685.01","SPBC30D10.10c","SPBC31F10.16","SPAC22E12.16c","SPBC543.07","SPBC119.08","SPBC577.06c","SPAC1F3.05"],"gene_count":22,"ltp_gene_count":18,"approved_date":"2025-03-03"},{"uniquename":"PMID:8321236","title":"The fission yeast ferric reductase gene frp1+ is required for ferric iron uptake and encodes a protein that is homologous to the gp91-phox subunit of the human NADPH phagocyte oxidoreductase.","citation":"Mol Cell Biol 1993 Jul;13(7):4342-50","abstract":"We have identified a cell surface ferric reductase activity in the fission yeast Schizosaccharomyces pombe. A mutant strain deficient in this activity was also deficient in ferric iron uptake, while ferrous iron uptake was not impaired. Therefore, reduction is a required step in cellular ferric iron acquisition. We have cloned frp1+, the wild-type allele of the mutant gene. frp1+ mRNA levels were repressed by iron addition to the growth medium. Fusion of 138 nucleotides of frp1+ promoter sequences to a reporter gene, the bacterial chloramphenicol acetyltransferase gene, conferred iron-dependent regulation upon the latter when introduced into S. pombe. The predicted amino acid sequence of the frp1+ gene exhibits hydrophobic regions compatible with transmembrane domains. It shows similarity to the Saccharomyces cerevisiae FRE1 gene product and the gp91-phox protein, a component of the human NADPH phagocyte oxidoreductase that is deficient in X-linked chronic granulomatous disease.","authors":"Roman DG, Dancis A, Anderson GJ, Klausner RD","authors_abbrev":"Roman DG et al.","pubmed_publication_date":"Jul 1993","pubmed_entrez_date":"1993-07-01","publication_year":"1993","canto_session_key":"169dc6a662075c56","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-01-24 12:11:23","canto_approved_date":"2025-02-21 16:00:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-09 08:36:42","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1683.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-24"},{"uniquename":"PMID:8521469","title":"p65cdc18 plays a major role controlling the initiation of DNA replication in fission yeast.","citation":"Cell 1995 Nov 03;83(3):397-405","abstract":"A key problem in the cell cycle is understanding what brings about the initiation of DNA replication and how this is linked with global cell cycle controls. The fission yeast gene cdc18 is required for DNA replication and is transcriptionally activated by the cdc10/res1/res2 control acting at START in late G1. We show here that overexpressing cdc18 is able to bring about repeated rounds of DNA synthesis in the absence of mitosis and of continuing protein synthesis. The level of the cdc18-encoded protein p65cdc18 is periodic in the cell cycle, peaking at the G1 to S phase transition, and p65cdc18 is located in the nucleus when cdc18 is overexpressed. We propose that p65cdc18 acts at the initiation of DNA replication and plays a major role in controlling the onset of S phase.","authors":"Nishitani H, Nurse P","authors_abbrev":"Nishitani H et al.","pubmed_publication_date":"03 Nov 1995","pubmed_entrez_date":"1995-11-03","publication_year":"1995","canto_session_key":"e8ac2521a0651d1d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-29 15:34:55","canto_approved_date":"2025-06-09 18:07:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-24 16:04:21","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPAC24H6.05","SPBC336.12c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-04-29"},{"uniquename":"PMID:34580178","title":"ATAD2 controls chromatin-bound HIRA turnover.","citation":"Life Sci Alliance 2021 Dec;4(12)","abstract":"Taking advantage of the evolutionary conserved nature of ATAD2, we report here a series of parallel functional studies in human, mouse, and  Schizosaccharomyces pombe  to investigate ATAD2's conserved functions. In  S. pombe , the deletion of  ATAD2  ortholog,  abo1 , leads to a dramatic decrease in cell growth, with the appearance of suppressor clones recovering normal growth. The identification of the corresponding suppressor mutations revealed a strong genetic interaction between Abo1 and the histone chaperone HIRA. In human cancer cell lines and in mouse embryonic stem cells, we observed that the KO of  ATAD2  leads to an accumulation of HIRA. A ChIP-seq mapping of nucleosome-bound HIRA and FACT in  Atad2  KO mouse ES cells demonstrated that both chaperones are trapped on nucleosomes at the transcription start sites of active genes, resulting in the abnormal presence of a chaperone-bound nucleosome on the TSS-associated nucleosome-free regions. Overall, these data highlight an important layer of regulation of chromatin dynamics ensuring the turnover of histone-bound chaperones.","doi":"10.26508/lsa.202101151","authors":"Wang T, Perazza D, Boussouar F, Cattaneo M, Bougdour A, Chuffart F, Barral S, Vargas A, Liakopoulou A, Puthier D, Bargier L, Morozumi Y, Jamshidikia M, Garcia-Saez I, Petosa C, Rousseaux S, Verdel A, Khochbin S","authors_abbrev":"Wang T et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-09-28","publication_year":"2021","canto_session_key":"add2e9acc505616a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-04-10 09:58:53","canto_approved_date":"2023-07-19 14:45:48","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-04-10 09:58:46","canto_added_date":"2021-09-30 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.03c","SPBC31F10.14c","SPBC15D4.03","SPAC31G5.19","SPBC29A10.03c","SPBC8D2.04","SPBC8D2.03c","SPAC1834.04"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2023-04-10"},{"uniquename":"PMID:17690098","title":"Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity.","citation":"J Biol Chem 2007 Sep 28;282(39):28587-28596","abstract":"In budding yeast, acetylation of histone H3 lysine 56 (H3-K56) is catalyzed by the Rtt109-Vps75 histone acetyltransferase (HAT) complex, with Rtt109 being the catalytic subunit, and histone chaperone Asf1 is required for this modification. Cells lacking Rtt109 are susceptible to perturbations in DNA replication. However, how Asf1 regulates acetylation of H3-K56 and how loss of H3-K56 acetylation affects DNA replication are unclear. We show that at low concentrations the Rtt109-Vps75 HAT complex acetylates H3-K56 in vitro when H3/H4 is complexed with Asf1, but not H3/H4 tetramers, recapitulating the in vivo requirement of Asf1 for H3-K56 acetylation using recombinant proteins. Moreover, the Rtt109-Vps75 complex interacts with Asf1-H3/H4 but not Asf1. In vivo, the Rtt109-Asf1 interaction is also dependent on the ability of Asf1 to bind H3/H4. Furthermore, the Rtt109 homolog in Schizosaccharomyces pombe (SpRtt109) also displayed an Asf1-dependent H3-K56 HAT activity in vitro. These results indicate that Asf1 regulates H3-K56 acetylation by presenting histones H3 and H4 to Rtt109-Vps575 for acetylation, and this mechanism is likely to be conserved. Finally, we have shown that cells lacking Rtt109 or expressing H3-K56 mutants exhibited significant reduction in the association of three proteins with stalled DNA replication forks and hyper-recombination of replication forks stalled at replication fork barriers of the ribosomal DNA locus compared with wild-type cells. Taken together, these studies provide novel insight into the role of Asf1 in the regulation of H3-K56 acetylation and the function of this modification in DNA replication.","doi":"10.1074/jbc.M702496200","authors":"Han J, Zhou H, Li Z, Xu RM, Zhang Z","authors_abbrev":"Han J et al.","pubmed_publication_date":"28 Sep 2007","pubmed_entrez_date":"2007-08-11","publication_year":"2007","canto_session_key":"a2b5048e60f2a789","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-08 10:07:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-08 10:06:59","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC342.06c","SPCC663.05c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-10-08"},{"uniquename":"PMID:1563350","title":"DNA repair mutants defining G2 checkpoint pathways in Schizosaccharomyces pombe.","citation":"EMBO J 1992 Apr;11(4):1343-50","abstract":"We have tested mutants corresponding to 20 DNA repair genes of the fission yeast Schizosaccharomyces pombe for their ability to arrest in G2 after DNA damage. Of the mutants tested, four are profoundly defective in this damage dependent G2 arrest. In addition, these four mutants are highly sensitive to a transient inhibition of DNA synthesis by hydroxyurea. This suggests that the pathway responsible for the recognition of DNA damage and the subsequent mitotic arrest, shares many functions with the mechanism that controls the dependency of mitosis on the completion of S phase. The phenotype of these checkpoint rad mutants in wee mutant backgrounds indicate that the G2 arrest response is mediated either through, or in parallel with, the activity of the cdc2 gene product.","authors":"al-Khodairy F, Carr AM","authors_abbrev":"al-Khodairy F et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34118432","title":"Sec14 family of lipid transfer proteins in yeasts.","citation":"Biochim Biophys Acta Mol Cell Biol Lipids 2021 Oct;1866(10):158990","abstract":"The hydrophobicity of lipids prevents their free movement across the cytoplasm. To achieve highly heterogeneous and precisely regulated lipid distribution in different cellular membranes, lipids are transported by lipid transfer proteins (LTPs) in addition to their transport by vesicles. Sec14 family is one of the most extensively studied groups of LTPs. Here we provide an overview of Sec14 family of LTPs in the most studied yeast Saccharomyces cerevisiae as well as in other selected non-Saccharomyces yeasts-Schizosaccharomyces pombe, Kluyveromyces lactis, Candida albicans, Candida glabrata, Cryptococcus neoformans, and Yarrowia lipolytica. Discussed are specificities of Sec14-domain LTPs in various yeasts, their mode of action, subcellular localization, and physiological function. In addition, quite few Sec14 family LTPs are target of antifungal drugs, serve as modifiers of drug resistance or influence virulence of pathologic yeasts. Thus, they represent an important object of study from the perspective of human health.","doi":"10.1016/j.bbalip.2021.158990","authors":"Holič R, Šťastný D, Griač P","authors_abbrev":"Holič R et al.","pubmed_publication_date":"Oct 2021","pubmed_entrez_date":"2021-06-12","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-06-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8552193","title":"Role for a Xenopus Orc2-related protein in controlling DNA replication.","citation":"Nature 1996 Jan 25;379(6563):357-60","abstract":"The six-subunit origin recognition complex (ORC) is essential for the initiation of DNA replication at specific origins in the budding yeast Saccharomyces cerevisiae. An important issue is whether DNA replication in higher eukaryotes, in which the characteristics of replication origins are poorly defined, occurs by an ORC-dependent mechanism. We have identified a Xenopus laevis Orc2-related protein (XORC2) by its ability to rescue a mitotic-catastrophe mutant of the fission yeast Schizosaccharomyces pombe. We show that immunodepletion of XORC2 from Xenopus egg extracts abolishes the replication of chromosomal DNA but not elongation synthesis on a single-stranded DNA template. Indirect immunofluorescence indicates that XORC2 binds to chromatin well before the commencement of DNA synthesis, and even under conditions that prevent the association of replication licensing factor(s) with the DNA. These findings suggest that Orc2 plays an important role at an early step of chromosomal replication in animal cells.","authors":"Carpenter PB, Mueller PR, Dunphy WG","authors_abbrev":"Carpenter PB et al.","pubmed_publication_date":"25 Jan 1996","pubmed_entrez_date":"1996-01-25","publication_year":"1996","canto_session_key":"968dd4b03241d795","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:37:56","canto_session_submitted_date":"2012-03-03 15:37:42","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:8367276","title":"Domains of p85cdc10 required for function of the fission yeast DSC-1 factor.","citation":"Nucleic Acids Res 1993 Aug 11;21(16):3615-21","abstract":"p85cdc10 is a component of the S.pombe DSC-1 complex, which is thought to mediate periodic transcription of genes in late G1. In order to understand the role of p85cdc10 in the function of this complex, we have analysed which domains of p85cdc10 are required for biological activity and the formation of a stable DSC-1 complex in vitro, both in cdc10 temperature sensitive and null backgrounds. No DSC-1 activity is found in the absence of p85cdc10 and the activity of the complex is reduced or absent in all cdc10ts mutants tested. Full biological activity and rescue of a cdc10::ura4+ null allele requires the N-terminal domain, the cdc10/SWI6 repeats and the helical C-terminal region. In the absence of p85cdc10, both the C-terminal and cdc10/SWI6 repeat domains are required for DSC-1 activity in vitro. In a cdc10ts background, rescue of DSC-1 activity and complementation of mutants, requires only expression of the C-terminal domain, though the presence of the cdc10/SWI6 motifs enhances its activity. The N-terminal domain, alone, or in combination with the cdc10/SWI6 motifs, does not have biological activity, and does not restore DSC-1 activity. We conclude that both the C-terminal domain of p85cdc10 is critical for formation of the DSC-1 complex and that the cdc10/SWI6 motifs also play a role, perhaps by stabilizing the complex. Our data also suggest that the S.pombe DSC-1 complex contains more than one molecule of p85cdc10.","authors":"Reymond A, Simanis V","authors_abbrev":"Reymond A et al.","pubmed_publication_date":"11 Aug 1993","pubmed_entrez_date":"1993-08-11","publication_year":"1993","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15585577","title":"Interaction of 14-3-3 protein with Chk1 affects localization and checkpoint function.","citation":"J Cell Sci 2005 Jan 01;118(Pt 1):39-50","abstract":"The protein kinase Chk1 is required for proper arrest of the cell cycle in response to DNA damage. We have previously shown in Schizosaccharomyces pombe, that upon DNA damage, phosphorylation of Chk1 correlates with checkpoint activation and that phosphorylated Chk1 is capable of interacting with the 14-3-3 proteins, Rad24 and Rad25. The interaction between Rad24 and Chk1 is stimulated tenfold after exposure to DNA damaging agents and we postulate that it is an important event in the DNA damage checkpoint response pathway in fission yeast. We identified a stretch of leucine residues as the domain in Chk1 that mediates the interaction with 14-3-3 proteins. Substitution of leucine residues with alanine disrupts the interaction with Rad24 and also prevents Chk1 from becoming phosphorylated in response to DNA damaging agents. Cells expressing the mutants are sensitive to UV radiation. In this study, we also show that Chk1 accumulates in the nucleus in response to DNA damage and this behavior is dependent on Rad24. Interestingly, the 14-3-3 binding domain mutants also fail to localize to the nucleus prompting a search for localization sequences within Chk1. Our investigations have identified the presence of both functional nuclear import and nuclear export sequences encoded in S. pombe Chk1 that, in conjunction with 14-3-3 proteins, may play a prominent role in regulating Chk1 localization and function.","authors":"Dunaway S, Liu HY, Walworth NC","authors_abbrev":"Dunaway S et al.","pubmed_publication_date":"01 Jan 2005","pubmed_entrez_date":"2004-12-09","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPCC1259.13","SPAC20G8.01"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:28619713","title":"Molecular model of fission yeast centrosome assembly determined by superresolution imaging.","citation":"J Cell Biol 2017 Aug 07;216(8):2409-2424","abstract":"Microtubule-organizing centers (MTOCs), known as centrosomes in animals and spindle pole bodies (SPBs) in fungi, are important for the faithful distribution of chromosomes between daughter cells during mitosis as well as for other cellular functions. The cytoplasmic duplication cycle and regulation of the  Schizosaccharomyces pombe  SPB is analogous to centrosomes, making it an ideal model to study MTOC assembly. Here, we use superresolution structured illumination microscopy with single-particle averaging to localize 14  S. pombe  SPB components and regulators, determining both the relationship of proteins to each other within the SPB and how each protein is assembled into a new structure during SPB duplication. These data enabled us to build the first comprehensive molecular model of the  S. pombe  SPB, resulting in structural and functional insights not ascertained through investigations of individual subunits, including functional similarities between Ppc89 and the budding yeast SPB scaffold Spc42, distribution of Sad1 to a ring-like structure and multiple modes of Mto1 recruitment.","doi":"10.1083/jcb.201701041","authors":"Bestul AJ, Yu Z, Unruh JR, Jaspersen SL","authors_abbrev":"Bestul AJ et al.","pubmed_publication_date":"07 Aug 2017","pubmed_entrez_date":"2017-06-17","publication_year":"2017","canto_session_key":"e28e479729269ce9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Andrew Bestul","canto_first_approved_date":"2018-01-18 16:12:24","canto_approved_date":"2022-08-31 11:41:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-16 23:40:11","canto_added_date":"2017-06-19 00:15:14","annotation_curators":[{"name":"Andrew Bestul","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.14","SPBC649.05","SPBC428.20c","SPCC1739.11c","SPBC244.01c","SPAC4H3.11c","SPCC417.07c","SPAC9G1.15c","SPBC32F12.04","SPBC8D2.05c","SPBC365.15","SPBC12D12.01","SPAC6G9.06c","SPCC1682.04","SPBC947.12"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2018-01-18"},{"uniquename":"PMID:23966468","title":"Cooperation between Rho-GEF Gef2 and its binding partner Nod1 in the regulation of fission yeast cytokinesis.","citation":"Mol Biol Cell 2013 Oct;24(20):3187-204","abstract":"Cytokinesis is the last step of the cell-division cycle, which requires precise spatial and temporal regulation to ensure genetic stability. Rho guanine nucleotide exchange factors (Rho GEFs) and Rho GTPases are among the key regulators of cytokinesis. We previously found that putative Rho-GEF Gef2 coordinates with Polo kinase Plo1 to control the medial cortical localization of anillin-like protein Mid1 in fission yeast. Here we show that an adaptor protein, Nod1, colocalizes with Gef2 in the contractile ring and its precursor cortical nodes. Like gef2, nod1 has strong genetic interactions with various cytokinesis mutants involved in division-site positioning, suggesting a role of Nod1 in early cytokinesis. We find that Nod1 and Gef2 interact through the C-termini, which is important for their localization. The contractile-ring localization of Nod1 and Gef2 also depends on the interaction between Nod1 and the F-BAR protein Cdc15, where the Nod1/Gef2 complex plays a role in contractile-ring maintenance and affects the septation initiation network. Moreover, Gef2 binds to purified GTPases Rho1, Rho4, and Rho5 in vitro. Taken together, our data indicate that Nod1 and Gef2 function cooperatively in a protein complex to regulate fission yeast cytokinesis.","doi":"10.1091/mbc.E13-06-0301","authors":"Zhu YH, Ye Y, Wu Z, Wu JQ","authors_abbrev":"Zhu YH et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-08-23","publication_year":"2013","canto_session_key":"3c2cf7f390975961","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jian-Qiu Wu","canto_first_approved_date":"2016-10-09 21:38:04","canto_approved_date":"2026-02-14 10:17:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-30 14:07:39","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[{"name":"Jian-Qiu Wu","community_curator":true,"annotation_count":33,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":49,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":"quantitative_gene_expression","file_name":"PMID_23966468_Zhu_protein_quantitative_expression.txt"}],"genes":["SPAC16A10.04","SPAC1F7.04","SPAP8A3.08","SPAC20G8.05c","SPAC12B10.10","SPAC24B11.11c","SPAC20H4.11c","SPAC23C11.16","SPBC21.06c","SPAC4F8.13c","SPAC31A2.16","SPCC1739.11c","SPCC4B3.15"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2016-10-09"},{"uniquename":"PMID:10786374","title":"[Mechanism of arsenic compound resistance in prokaryotes and eukaryotes].","citation":"Postepy Biochem 1999;45(4):304-12","abstract":"","authors":"Wysocki R, Bobrowicz P, Ułaszewski S","authors_abbrev":"Wysocki R et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"2000-04-29","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9182666","title":"Fission yeast dim1(+) encodes a functionally conserved polypeptide essential for mitosis.","citation":"J Cell Biol 1997 Jun 16;137(6):1337-54","abstract":"In a screen for second site mutations capable of reducing the restrictive temperature of the fission yeast mutant cdc2-D217N, we have isolated a novel temperature-sensitive mutant, dim1-35. When shifted to restrictive temperature, dim1-35 mutant cells arrest before entry into mitosis or proceed through mitosis in the absence of nuclear division, demonstrating an uncoupling of proper DNA segregation from other cell cycle events. Deletion of dim1 from the Schizosaccharomyces pombe genome produces a lethal G2 arrest phenotype. Lethality is rescued by overexpression of the mouse dim1 homolog, mdim1. Likewise, deletion of the Saccharomyces cerevisiae dim1 homolog, CDH1, is lethal. Both mdim1 and dim1(+) are capable of rescuing lethality in the cdh1::HIS3 mutant. Although dim1-35 displays no striking genetic interactions with various other G2/M or mitotic mutants, dim1-35 cells incubated at restrictive temperature arrest with low histone H1 kinase activity. Morevoer, dim1-35 displays sensitivity to the microtubule destabilizing drug, thiabendazole (TBZ). We conclude that Dim1p plays a fundamental, evolutionarily conserved role as a protein essential for entry into mitosis as well as for chromosome segregation during mitosis. Based on TBZ sensitivity and failed chromosome segregation in dim1-35, we further speculate that Dim1p may play a role in mitotic spindle formation and/or function.","authors":"Berry LD, Gould KL","authors_abbrev":"Berry LD et al.","pubmed_publication_date":"16 Jun 1997","pubmed_entrez_date":"1997-06-16","publication_year":"1997","canto_session_key":"8dfa0891a4a7ec3f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-03-07 15:50:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-06 17:36:58","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.05c","SPAC24H6.05","SPCC1739.11c","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-05-06"},{"uniquename":"PMID:10440376","title":"Cohesin Rec8 is required for reductional chromosome segregation at meiosis.","citation":"Nature 1999 Jul 29;400(6743):461-4","abstract":"When cells exit from mitotic cell division, their sister chromatids lose cohesion and separate to opposite poles of the dividing cell, resulting in equational chromosome segregation. In contrast, the reductional segregation of the first stage of meiotic cell division (meiosis I) requires that sister chromatids remain associated through their centromeres and move together to the same pole. Centromeric cohesion is lost as cells exit from meiosis II and sister chromatids can then separate. The fission yeast cohesin protein Rec8 is specific to and required for meiosis. Here we show that Rec8 appears in the centromeres and adjacent chromosome arms during the pre-meiotic S phase. Centromeric Rec8 persists throughout meiosis I and disappears at anaphase of meiosis II. When the rec8 gene is deleted, sister chromatids separate at meiosis I, resulting in equational rather than reductional chromosome segregation. We propose that the persistence of Rec8 at centromeres during meiosis I maintains sister-chromatid cohesion, and that its presence in the centromere-adjacent regions orients the kinetochores so that sister chromatids move to the same pole. This results in the reductional pattern of chromosome segregation necessary to reduce a diploid zygote to haploid gametes.","authors":"Watanabe Y, Nurse P","authors_abbrev":"Watanabe Y et al.","pubmed_publication_date":"29 Jul 1999","pubmed_entrez_date":"1999-08-10","publication_year":"1999","canto_session_key":"363d7c14c0239ceb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-09 16:42:44","canto_approved_date":"2023-09-12 09:34:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-30 13:05:34","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPCC338.17c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-09"},{"uniquename":"Pfam:PF01803","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:6533","SPBC30B4.03c","HGNC:6532"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11564871","title":"Widespread use of TATA elements in the core promoters for RNA polymerases III, II, and I in fission yeast.","citation":"Mol Cell Biol 2001 Oct;21(20):6870-81","abstract":"In addition to directing transcription initiation, core promoters integrate input from distal regulatory elements. Except for rare exceptions, it has been generally found that eukaryotic tRNA and rRNA genes do not contain TATA promoter elements and instead use protein-protein interactions to bring the TATA-binding protein (TBP), to the core promoter. Genomewide analysis revealed TATA elements in the core promoters of tRNA and 5S rRNA (Pol III), U1 to U5 snRNA (Pol II), and 37S rRNA (Pol I) genes in Schizosaccharomyces pombe. Using tRNA-dependent suppression and other in vivo assays, as well as in vitro transcription, we demonstrated an obligatory requirement for upstream TATA elements for tRNA and 5S rRNA expression in S. pombe. The Pol III initiation factor Brf is found in complexes with TFIIIC and Pol III in S. pombe, while TBP is not, consistent with independent recruitment of TBP by TATA. Template commitment assays are consistent with this and confirm that the mechanisms of transcription complex assembly and initiation by Pol III in S. pombe differ substantially from those in other model organisms. The results were extended to large-rRNA synthesis, as mutation of the TATA element in the Pol I promoter also abolishes rRNA expression in fission yeast. A survey of other organisms' genomes reveals that a substantial number of eukaryotes may use widespread TATAs for transcription. These results indicate the presence of TATA-unified transcription systems in contemporary eukaryotes and provide insight into the residual need for TBP by all three Pols in other eukaryotes despite a lack of TATA elements in their promoters.","authors":"Hamada M, Huang Y, Lowe TM, Maraia RJ","authors_abbrev":"Hamada M et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-09-21","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1368589","title":"FAB-MS/MS spectrometry in determining the primary structure of gamma-glutamyl-containing peptides.","citation":"Agric Biol Chem 1990 Jul;54(7):1651-60","abstract":"Positive fast atom bombardment tandem mass spectrometry (FAB-MS/MS) was applied for peptide sequencing, particularly for determining the gamma glutamyl linkage involved in metal-binding peptides such as Cadystin (gamma EC)3G = Cadystin A and Cadystin (gamma EC)2G = Cadystin B (MW 771 and 539, respectively). The fragmentation patterns between the natural gamma glutamyl peptide and the synthetic alpha glutamyl one were clearly distinguishable. FAB-MS/MS was proved to be a good method for determining these peptides, since it needed no chemical degradation and only a small amount of the peptide was needed for determination.","authors":"Isobe M, Uyakul D, Liu KL, Goto T","authors_abbrev":"Isobe M et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15702347","title":"The N-terminal region of the Schizosaccharomyces pombe RecQ helicase, Rqh1p, physically interacts with Topoisomerase III and is required for Rqh1p function.","citation":"Mol Genet Genomics 2005 Mar;273(1):102-14","abstract":"The Schizosaccharomyces pombe rqh1+ gene encodes a member of the RecQ DNA helicase family. Members of this protein family are essential for the maintenance of genetic integrity. Thus, mutations in the genes encoding the human RecQ homologues Blm, Wrn and RecQ4 cause Bloom syndrome, Werner syndrome and Rothmund-Thomson syndrome, respectively-diseases which result from genome instability. S. pombe cells that lack a functional rqh1+ gene show reduced viability and display defective chromosome segregation, particularly after UV irradiation or S-phase arrest. In this study we used an rqh1+ deletion series to show that the N-terminal portion of Rqh1 is essential for Rqh1 function. Moreover, the conserved Helicase and RNaseD C-terminal (HRDC) domain of Rqh1 also plays a role in allowing cells to tolerate exposure to DNA damaging agents and the S-phase inhibitor hydroxyurea (HU). We also demonstrate that Topoisomerase III (Top3) binds to a site within the first 322 N-terminal amino acids of Rqh1 and that this binding correlates with Rqh1 function. Genetic analysis of rqh1- top3delta mutants reveals that, in the presence of functional or partially functional Rqh1 protein, Top3 is required to maintain genome integrity and cell viability.","authors":"Ahmad F, Stewart E","authors_abbrev":"Ahmad F et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-02-11","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1703.14c","SPAC2G11.12","SPBC16G5.12c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10397759","title":"Effects of genome position and the DNA damage checkpoint on the structure and frequency of sod2 gene amplification in fission yeast.","citation":"Mol Biol Cell 1999 Jul;10(7):2199-208","abstract":"The Schizosaccharomyces pombe sod2 gene, located near the telomere on the long arm of chromosome I, encodes a Na+ (or Li+)/H+ antiporter. Amplification of sod2 has previously been shown to confer resistance to LiCl. We analyzed 20 independent LiCl-resistant strains and found that the only observed mechanism of resistance is amplification of sod2. The amplicons are linear, extrachromosomal elements either 225 or 180 kb long, containing both sod2 and telomere sequences. To determine whether proximity to a telomere is necessary for sod2 amplification, a strain was constructed in which the gene was moved to the middle of the same chromosomal arm. Selection of LiCl-resistant strains in this genetic background also yielded amplifications of sod2, but in this case the amplified DNA was exclusively chromosomal. Thus, proximity to a telomere is not a prerequisite for gene amplification in S. pombe but does affect the mechanism. Relative to wild-type cells, mutants with defects in the DNA damage aspect of the rad checkpoint control pathway had an increased frequency of sod2 amplification, whereas mutants defective in the S-phase completion checkpoint did not. Two models for generating the amplified DNA are presented.","authors":"Patterson TE, Albrecht EB, Nurse P, Sazer S, Stark GR","authors_abbrev":"Patterson TE et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-09","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR21456","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:31419","SPCC1494.08c","HGNC:27637"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19799177","title":"Genetic analysis of meiotic recombination in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2009;557:65-76","abstract":"The fission yeast Schizosaccharomyces pombe is well-suited for studying meiotic recombination. Methods are described here for culturing S. pombe and for genetic assays ofintragenic recombination (gene conversion), intergenic recombination (crossing-over), and spore viability. Both random spore and tetrad analyses are described.","doi":"10.1007/978-1-59745-527-5_6","authors":"Smith GR","authors_abbrev":"Smith GR","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-10-06","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20082307","title":"A versatile selection system for folding competent proteins using genetic complementation in a eukaryotic host.","citation":"Protein Sci 2010 Mar;19(3):579-92","abstract":"Recombinant expression of native or modified eukaryotic proteins is pivotal for structural and functional studies and for industrial and pharmaceutical production of proteins. However, it is often impeded by the lack of proper folding. Here, we present a stringent and broadly applicable eukaryotic in vivo selection system for folded proteins. It is based on genetic complementation of the Schizosaccharomyces pombe growth marker gene invertase fused C-terminally to a protein library. The fusion proteins are directed to the secretion system, utilizing the ability of the eukaryotic protein quality-control systems to retain misfolded proteins in the ER and redirect them for cytosolic degradation, thereby only allowing folded proteins to reach the cell surface. Accordingly, the folding potential of the tested protein determines the ability of autotrophic colony growth. This system was successfully demonstrated using a complex insertion mutant library of TNF-alpha, from which different folding competent mutant proteins were uncovered.","doi":"10.1002/pro.337","authors":"Lyngsø C, Kjaerulff S, Müller S, Bratt T, Mortensen UH, Dal Degan F","authors_abbrev":"Lyngsø C et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2010-01-19","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26187949","title":"Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation.","citation":"Biol Open 2015 Jul 17;4(8):1040-51","abstract":"Tropomyosin is a coiled-coil protein that binds and regulates actin filaments. The tropomyosin gene in Schizosaccharomyces pombe, cdc8, is required for formation of actin cables, contractile rings, and polar localization of actin patches. The roles of conserved residues were investigated in gene replacement mutants. The work validates an evolution-based approach to identify tropomyosin functions in living cells and sites of potential interactions with other proteins. A cdc8 mutant with near-normal actin affinity affects patch polarization and vacuole fusion, possibly by affecting Myo52p, a class V myosin, function. The presence of labile residual cell attachments suggests a delay in completion of cell division and redistribution of cell patches following cytokinesis. Another mutant with a mild phenotype is synthetic negative with GFP-fimbrin, inferring involvement of the mutated tropomyosin sites in interaction between the two proteins. Proteins that assemble in the contractile ring region before actin do so in a mutant cdc8 strain that cannot assemble condensed actin rings, yet some cells can divide. Of general significance, LifeAct-GFP negatively affects the actin cytoskeleton, indicating caution in its use as a biomarker for actin filaments.","doi":"10.1242/bio.012609","authors":"Cranz-Mileva S, MacTaggart B, Russell J, Hitchcock-DeGregori SE","authors_abbrev":"Cranz-Mileva S et al.","pubmed_publication_date":"17 Jul 2015","pubmed_entrez_date":"2015-07-19","publication_year":"2015","canto_session_key":"02594045398fd2f8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-07-20 00:20:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPBC1778.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12109161","title":"Regularities and irregularities in the cell cycle of the fission yeast, Schizosaccharomyces pombe (a review).","citation":"Acta Microbiol Immunol Hung 2002;49(2-3):289-304","abstract":"In an exponentially growing wild-type fission yeast culture a size control mechanism ensures that mitosis is executed only if the cells have reached a critical size. However, there is some scattering both in cell length at birth (BL) and in cycle time (CT). By computational simulations we show here that this scattering cannot be explained solely by asymmetric cell division, therefore we assume that nuclear division is a stochastic, asymmetric process as well. We introduce an appropriate stochastic variable into a mathematical model and prove that this assumption is suitable to describe the CT vs. BL graph in a wild-type fission yeast population. In a double mutant of fission yeast (namely wee1-50 cdc25 delta) this CT vs. BL plot is even more curious: cycle time splits into three different values resulting in three clusters in this coordinate system. We show here that it is possible to describe these quantized cycles by choosing the appropriate values of the key parameters of mitotic entry and exit and even more the clustered behavior may be simulated by applying a further stochastic parameter.","authors":"Sveiczer A, Novák B","authors_abbrev":"Sveiczer A et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-07-12","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17173334","title":"In Schizosaccharomyces pombe the 14-3-3 protein Rad24p is involved in negative control of pho1 gene expression.","citation":"Yeast 2007 Feb;24(2):121-7","abstract":"Expression of Schizosaccharomyces pombe pho1-encoded acid phosphatase is transcriptionally regulated by adenine and phosphate. Four genes, anr1-3 and anr5, encode negative regulators of pho1 expression. Apart from being designated as loci, the anr genes have not been further characterized. In this study we provide evidence that a strain carrying the deletion of rad24, a 14-3-3 protein-encoding gene, exhibits an anr mutant like the phenotype (higher phosphatase activity, higher transcript levels of pho1, lower sensitivity to adenine of pho1 expression) and that rad24 is closely linked, probably allelic, to anr5. By sequencing the two exons of the rad24 gene in a strain carrying the mutant allele anr5-13, we found a T/A-to-C/G transition in the 225th codon of its ORF, causing a leucine-to-serine substitution in a highly conserved region of all proteins of the 14-3-3 family. anr2 and anr3 are not allelic to rad24. The mutant alleles of anr2 and anr3 are recessive to their wild-type alleles and do not belong to the same epistasis group as rad24.","authors":"Voicu PM, Petrescu-Danila E, Poitelea M, Watson AT, Rusu M","authors_abbrev":"Voicu PM et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2006-12-19","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15897177","title":"Shugoshin protects cohesin complexes at centromeres.","citation":"Philos Trans R Soc Lond B Biol Sci 2005 Mar 29;360(1455):515-21, discussion 521","abstract":"The different regulation of sister chromatid cohesion at centromeres and along chromosome arms is obvious during meiosis, because centromeric cohesion, but not arm cohesion, persists throughout anaphase of the first division. A protein required to protect centromeric cohesin Rec8 from separase cleavage has been identified and named shugoshin (or Sgo1) after shugoshin (\"guardian spirit\" in Japanese). It has become apparent that shugoshin shows marginal homology with Drosophila Mei-S332 and several uncharacterized proteins in other eukaryotic organisms. Because Mei-S332 is a protein previously shown to be required for centromeric cohesion in meiosis, it is now established that shugoshin represents a conserved protein family defined as a centromeric protector of Rec8 cohesin complexes in meiosis. The regional difference of sister chromatid cohesion is also observed during mitosis in vertebrates; the cohesion is much more robust at the centromere at metaphase, where it antagonizes the pulling force of spindle microtubules that attach the kinetochores from opposite poles. The human shugoshin homologue (hSgo1) is required to protect the centromeric localization of the mitotic cohesin, Scc1, until metaphase. Bub1 plays a crucial role in the localization of shugoshin to centromeres in both fission yeast and humans.","authors":"Watanabe Y, Kitajima TS","authors_abbrev":"Watanabe Y et al.","pubmed_publication_date":"29 Mar 2005","pubmed_entrez_date":"2005-05-18","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4362740","title":"The development of cytochromes during the cell cycle of a glucose-repressed fission yeast, Schizosaccharomyces pombe 972h-.","citation":"Biochem J 1974 Feb;138(2):201-10","abstract":"1. Spectrophotometric analysis of intact cells of Schizosaccharomyces pombe, harvested from exponentially growing cultures during the phase of glucose repression, revealed the presence of cytochromes a+a(3), c and at least two species of cytochrome b. 2. An absorption maximum at 554nm at 77 degrees K, previously attributed to cytochrome c(1), has been identified as a b-type cytochrome. 3. CO-difference spectra reveal the presence of cytochromes P-420 and P-450 in addition to cytochrome a(3). 4. The cell cycle was analysed by separation of cells into classes representing successive stages in the cell cycle by isopycnic zonal centrifugation. 5. Cytochromes c(548), b(554) and b(560) each exhibited a single broad maximum of synthesis during the cell cycle. 6. Amounts of cytochromes a+a(3) and b(563) (tentatively identified as cytochrome b(T) by its reaction on pulsing anaerobic cell suspensions with O(2)) oscillated in phase, and showed two maxima during the cycle; the second maximum of cytochromes a+a(3) was coincident with a maximum of activity of enzymically active cytochrome c oxidase. 7. The amount of cytochrome P-420 decreased during the first three-quarters of the cell-cycle, whereas that of cytochrome P-450 increased during this period. 8. The discrepancy between spectrophotometric and enzymic assay of cytochrome c oxidase, the changing ratio of cytochrome a(3)/cytochrome a and the relationship between changes in cellular content of cytochromes and previous observations on respiratory oscillations during the cell cycle are discussed.","authors":"Poole RK, Lloyd D, Chance B","authors_abbrev":"Poole RK et al.","pubmed_publication_date":"Feb 1974","pubmed_entrez_date":"1974-02-01","publication_year":"1974","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25361577","title":"Asymmetric inheritance of cytoophidia in Schizosaccharomyces pombe.","citation":"Biol Open 2014 Oct 31;3(11):1092-7","abstract":"A general view is that Schizosaccharomyces pombe undergoes symmetric cell division with two daughter cells inheriting equal shares of the content from the mother cell. Here we show that CTP synthase, a metabolic enzyme responsible for the de novo synthesis of the nucleotide CTP, can form filamentous cytoophidia in the cytoplasm and nucleus of S. pombe cells. Surprisingly, we observe that both cytoplasmic and nuclear cytoophidia are asymmetrically inherited during cell division. Our time-lapse studies suggest that cytoophidia are dynamic. Once the mother cell divides, the cytoplasmic and nuclear cytoophidia independently partition into one of the two daughter cells. Although the two daughter cells differ from one another morphologically, they possess similar chances of inheriting the cytoplasmic cytoophidium from the mother cell, suggesting that the partition of cytoophidium is a stochastic process. Our findings on asymmetric inheritance of cytoophidia in S. pombe offer an exciting opportunity to study the inheritance of metabolic enzymes in a well-studied model system.","doi":"10.1242/bio.20149613","authors":"Zhang J, Hulme L, Liu JL","authors_abbrev":"Zhang J et al.","pubmed_publication_date":"31 Oct 2014","pubmed_entrez_date":"2014-11-02","publication_year":"2014","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-11-03 01:15:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11283354","title":"Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly.","citation":"Science 2001 Apr 06;292(5514):110-3","abstract":"The assembly of higher order chromatin structures has been linked to the covalent modifications of histone tails. We provide in vivo evidence that lysine 9 of histone H3 (H3 Lys9) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions in fission yeast. Both the conserved chromo- and SET domains of Clr4 are required for H3 Lys9 methylation in vivo. Localization of Swi6, a homolog of Drosophila HP1, to heterochomatic regions is dependent on H3 Lys9 methylation. Moreover, an H3-specific deacetylase Clr3 and a beta-propeller domain protein Rik1 are required for H3 Lys9 methylation by Clr4 and Swi6 localization. These data define a conserved pathway wherein sequential histone modifications establish a \"histone code\" essential for the epigenetic inheritance of heterochromatin assembly.","authors":"Nakayama J, Rice JC, Strahl BD, Allis CD, Grewal SI","authors_abbrev":"Nakayama J et al.","pubmed_publication_date":"06 Apr 2001","pubmed_entrez_date":"2001-04-03","publication_year":"2001","canto_session_key":"6dd31d982c2e470c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-03-05 19:33:18","canto_approved_date":"2024-03-04 14:52:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-03-05 19:33:10","canto_added_date":"2012-02-24 05:51:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":57,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.08","SPBC428.08c","SPBC800.03","SPAC664.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-03-05"},{"uniquename":"PMID:1883373","title":"Electrophoretic separation of S. pombe chromosomes in polyacrylamide solutions using a constant field.","citation":"Biochem Biophys Res Commun 1991 Aug 30;179(1):482-6","abstract":"Previous electrophoretic separations of megabase (Mb) sized DNA have been achieved in pulsed electric fields, using agarose gel as a matrix. The present study demonstrates separations of Mb sized DNA due to a retardation of migration in proportion to the concentration of uncrosslinked polyacrylamide of 5 x 10(6) molecular weight, using a constant electric field. Potentially, the method should be applicable to large DNA in general, greatly reducing the instrumental complexity of such separations and rendering them compatible with capillary electrophoresis apparatus.","authors":"Guszczynski T, Chrambach A","authors_abbrev":"Guszczynski T et al.","pubmed_publication_date":"30 Aug 1991","pubmed_entrez_date":"1991-08-30","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11160377","title":"A novel gene conserved from yeast to humans is involved in sterol biosynthesis.","citation":"J Lipid Res 2001 Jan;42(1):150-4","abstract":"The ERG28 gene was originally identified by microarray expression profiling as possibly involved in the Saccharomyces cerevisiae sterol pathway. Microarray analyses suggested that the transcription pattern of ERG28 closely followed that of genes involved in sterol synthesis. ERG28 was also found in Schizosaccharomyces pombe and Arabidopsis as well as humans, and in the latter was shown to be highly expressed in adult testis tissue. All four proteins contain potential transmembrane domain(s). Gas chromatography-mass spectrometry analysis of an ERG28-deleted S. cerevisiae strain (which is slow growing but not auxotrophic for ergosterol) indicates a lesion in sterol C-4 demethylation. Sterol profiles indicate accumulation of 3-keto and carboxylic acid sterol intermediates, which are involved in removing the two C-4 methyl groups from the sterol A ring. Similar intermediates have previously been demonstrated to accumulate in erg26 (sterol dehydrogenase/decarboxylase) and erg27 (3-ketoreductase) mutants in yeast. We speculate that the role of the Erg28 protein (Erg28p) may be either to tether Erg26p and Erg27p to the endoplasmic reticulum or to facilitate interaction between these proteins.-Gachotte, D., J. Eckstein, R. Barbuch, T. Hughes, C. Roberts, and M. Bard. A novel gene conserved from yeast to humans is involved in sterol biosynthesis. J. Lipid Res. 2001. 42: 150;-154.","authors":"Gachotte D, Eckstein J, Barbuch R, Hughes T, Roberts C, Bard M","authors_abbrev":"Gachotte D et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-02-13","publication_year":"2001","canto_session_key":"96b99e4781c56d89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-12-05 15:33:54","canto_approved_date":"2017-12-05 15:33:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-22 12:31:23","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC337.09"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2017-12-05"},{"uniquename":"PMID:8845581","title":"Cyclins, cyclin-dependent kinases and cdk inhibitors: implications in cell cycle control and cancer.","citation":"Crit Rev Eukaryot Gene Expr 1995;5(2):127-56","abstract":"A significant portion of cell scientific literature published is dedicated to describing the cloning, the link to cancer, or the characterization of proteins involved in the progression of the cell cycle. With this abundance of information, the cascading pathways of molecular events that occur in the cell cycle are proving to be exceedingly complicated. Originally, the sole regulator of the fission yeast cells division cycle, cdc2, was thought to also regulate mammalian cell cycles in the same manner. However, mammalian cdc2 has now been joined by seven well-characterized relatives acting at distinct points in the cell cycle. These kinases are activated by larger proteins called cyclins, named with respect to their cyclical expression and degradation. Therefore, the catalytic subunits of these complexes are named cyclin-dependent kinases (cdks). In the event that the cell must stop normal cycling behavior, a number of cdk inhibitors, which have only begun to be characterized, function in inhibiting the kinase ability of cdks, among other nonproliferative acts. The external environment manipulates cellular proliferation and differentiation by stimulating or inhibiting certain signal transduction pathways. However, each component of the cell cycle machinery, as they are the final executors in cell division, has the potential to elicit or to contribute to a neoplastic phenotype. This review focuses on the characterization of each member of the cell cycle protein family and also addresses the potential role each plays in cancer.","authors":"MacLachlan TK, Sang N, Giordano A","authors_abbrev":"MacLachlan TK et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15805194","title":"A checkpoint control linking meiotic S phase and recombination initiation in fission yeast.","citation":"Proc Natl Acad Sci U S A 2005 Apr 19;102(16):5797-801","abstract":"During meiosis, high levels of recombination initiated by DNA double-strand breaks (DSBs) occur only after DNA replication. However, how DSB formation is coupled to DNA replication is unknown. We examined several DNA replication proteins for a role in this coupling in Schizosaccharomyces pombe, and we show that ribonucleotide reductase, the rate-limiting enzyme of deoxyribonucleotide synthesis and the target of the DNA synthesis inhibitor hydroxyurea (HU) is indirectly required for DSB formation linked to DNA replication. However, in cells in which the function of the DNA-replication-checkpoint proteins Rad1p, Rad3p, Rad9p, Rad17p, Rad26p, Hus1p, or Cds1p was compromised, DSB formation occurred at similar frequencies in the absence or presence of HU. The DSBs in the HU-treated mutant cells occurred at normal sites and were associated with recombination. In addition, Cdc2p is apparently not involved in this process. We propose that the sequence of meiotic S phase and initiation of recombination is coordinated by DNA-replication-checkpoint proteins.","authors":"Tonami Y, Murakami H, Shirahige K, Nakanishi M","authors_abbrev":"Tonami Y et al.","pubmed_publication_date":"19 Apr 2005","pubmed_entrez_date":"2005-04-05","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12455412","title":"1,3-beta-Glucan synthase: a useful target for antifungal drugs.","citation":"Curr Drug Targets Infect Disord 2001 Aug;1(2):159-69","abstract":"1,3-beta-glucan synthase, a multisubunit enzyme, is responsible for fungal cell wall construction, division septum deposition, and ascospore wall assembly. The catalytic subunit of this enzyme complex, an integral membrane protein, has been identified both in model yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, and in pathogenic fungi such as Candida, Aspergillus, Cryptococcus and Pneumocystis species. The catalytic activity of the 1,3-beta-glucan synthase is regulated by a small GTPase of the Ras superfamily, the Rho-GTPase, and protein kinase C (Pkc)-like signaling molecules. It has been shown that the plasma membrane localization of this enzyme is essential for its activity. Interestingly, inhibition of 1,3-beta-glucan synthase activity by anti-fungal drugs of the lipopeptide type triggers a cell cycle feedback mechanism leading to cell cycle arrest. Recent progress in studies of molecular mechanisms of the temporal and spatial regulation of 1,3-beta-glucan synthase is presented. The implication of the cell cycle checkpoint that is activated by the anti-fungal drugs is also discussed.","authors":"Liu J, Balasubramanian MK","authors_abbrev":"Liu J et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2002-11-29","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11516644","title":"Role of bud6p and tea1p in the interaction between actin and microtubules for the establishment of cell polarity in fission yeast.","citation":"Curr Biol 2001 Jun 05;11(11):836-45","abstract":"In many cell types, microtubules are thought to direct the spatial distribution of F-actin in cell polarity. Schizosaccharomyces pombe cells exhibit a regulated program of polarized cell growth: after cell division, they grow first in a monopolar manner at the old end, and in G2 phase, initiate growth at the previous cell division site (the new end). The role of microtubule ends in cell polarity is highlighted by the finding that the cell polarity factor, tea1p, is present on microtubule plus ends and cell tips [1].\nHere, we characterize S. pombe bud6p/fat1p, a homolog of S. cerevisiae Bud6/Aip3. bud6Delta mutant cells have a specific defect in the efficient initiation of growth at the new end and like tea1Delta cells, form T-shaped cells in a cdc11 background. Bud6-GFP localizes to both cell tips and the cytokinesis ring. Maintenance of cell tip localization is dependent upon actin but not microtubules. Bud6-GFP localization is tea1p dependent, and tea1p localization is not bud6p dependent. tea1Delta and bud6Delta cells generally grow in a monopolar manner but exhibit different growth patterns. tea1(Delta)bud6Delta mutants resemble tea1Delta mutants. Tea1p and bud6p coimmunoprecipitate and comigrate in large complexes.\nOur studies show that tea1p (a microtubule end-associated factor) and bud6p (an actin-associated factor) function in a common pathway, with bud6p downstream of tea1p. To our knowledge, bud6p is the first protein shown to interact physically with tea1p. These studies delineate a pathway for how microtubule plus ends function to polarize the actin cytoskeleton through actin-associated polarity factors.","authors":"Glynn JM, Lustig RJ, Berlin A, Chang F","authors_abbrev":"Glynn JM et al.","pubmed_publication_date":"05 Jun 2001","pubmed_entrez_date":"2001-08-23","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15A10.16","SPCC1223.06"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:20946853","title":"Two-component signaling to the stress MAP kinase cascade in fission yeast.","citation":"Methods Enzymol 2010;471:279-89","abstract":"In the fission yeast Schizosaccharomyces pombe, the Mak2/3 sensor histidine kinases (HKs), the Mpr1 histidine-containing phosphotransfer (HPt) protein, and the Mcs4 response regulator (RR) constitute a multistep phosphorelay, which is connected to a stress-activated mitogen-activated protein kinase (MAPK) cascade. This hybrid signaling pathway senses H2O2 and transmits the stress signal by sequential phosphorylation of the component proteins, whose physical interactions play crucial roles to attain eventual activation of Spc1 MAPK. This chapter describes methodological details of the copurification assays in S. pombe cell lysate to detect the physical interactions between the Mpr1 HPt and Mcs4 RR proteins and between Mcs4 and the MAPK kinase kinases (MAPKKKs) of the Spc1 cascade. Unexpectedly, we found that the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) encoded by tdh1+ is involved in the H2O2 signaling process, and its association with Mcs4 and MAPKKKs in cell lysate is also detectable by copurification assays. In response to H2O2, the catalytic cysteine residue of Tdh1 GAPDH is subjected to S-thiolation, of which detection protocol is described as well.","doi":"10.1016/S0076-6879(10)71015-6","authors":"Morigasaki S, Shiozaki K","authors_abbrev":"Morigasaki S et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-10-16","publication_year":"2010","canto_session_key":"7391bcf18f0b16a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-08-04 10:38:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-08-04 10:38:46","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.11","SPAC9G1.02","SPBC725.02","SPBC887.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-08-04"},{"uniquename":"PMID:31371524","title":"Subunit interactions and arrangements in the fission yeast Mis16-Mis18-Mis19 complex.","citation":"Life Sci Alliance 2019 Aug;2(4)","abstract":"Centromeric chromatin in fission yeast is distinguished by the presence of nucleosomes containing the histone H3 variant Cnp1 CENP-A  Cell cycle-specific deposition of Cnp1 requires the Mis16-Mis18-Mis19 complex, which is thought to direct recruitment of Scm3-chaperoned Cnp1/histone H4 dimers to DNA. Here, we present the structure of the essential Mis18 partner protein Mis19 and describe its interaction with Mis16, revealing a bipartite-binding site. We provide data on the stoichiometry and overall architecture of the complex and provide detailed insights into the Mis18-Mis19 interface.","doi":"10.26508/lsa.201900408","authors":"Korntner-Vetter M, Lefèvre S, Hu XW, George R, Singleton MR","authors_abbrev":"Korntner-Vetter M et al.","pubmed_publication_date":"Aug 2019","pubmed_entrez_date":"2019-08-03","publication_year":"2019","canto_session_key":"02fb3179843288fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-29 16:36:33","canto_approved_date":"2019-10-29 16:36:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-29 16:36:27","canto_added_date":"2019-08-04 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.03c","SPCC970.12","SPBC1105.12","SPBC27B12.02","SPCC1672.10","SPAC1834.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-10-29","pdb_entries":[{"pdb_id":"6s29","gene_chains":[{"gene_uniquename":"SPBC27B12.02","chain":"B/D","position":"52-112"},{"gene_uniquename":"SPCC1672.10","chain":"A/C","position":"2-430"}],"title":"Structure of fission yeast Mis16-Mis19 complex","entry_authors":"Lefevre S,Korntner-Vetter M,Singleton MR","entry_authors_abbrev":"Lefevre S et al.","reference_uniquename":"PMID:31371524","experimental_method":"X-ray","resolution":"1.988"},{"pdb_id":"6s1l","gene_chains":[{"gene_uniquename":"SPCC1672.10","chain":"A","position":"2-430"}],"title":"Structure of fission yeast Mis16","entry_authors":"Lefevre S,Korntner-Vetter M,Singleton MR","entry_authors_abbrev":"Lefevre S et al.","reference_uniquename":"PMID:31371524","experimental_method":"X-ray","resolution":"1.94"},{"pdb_id":"6s1r","gene_chains":[{"gene_uniquename":"SPCC1672.10","chain":"A","position":"2-430"},{"gene_uniquename":"SPBC8D2.03c","chain":"B","position":"14-44"}],"title":"Structure of fission yeast Mis16 bound to histone H4","entry_authors":"Lefevre S,Korntner-Vetter M,Singleton MR","entry_authors_abbrev":"Lefevre S et al.","reference_uniquename":"PMID:31371524","experimental_method":"X-ray","resolution":"1.8"}]},{"uniquename":"PMID:17264117","title":"Caf1 regulates translocation of ribonucleotide reductase by releasing nucleoplasmic Spd1-Suc22 assembly.","citation":"Nucleic Acids Res 2007;35(4):1187-97","abstract":"Appropriate supply of deoxyribonucleotides by the ribonucleotide reductase (RNR) complex is essential for DNA replication and repair. One recent model for the RNR activation in Schizosaccharomyces pombe is translocation of the regulatory subunit Suc22 from the nucleoplasm to the cytoplasm. The RNR inhibitory protein Spd1, which retains Suc22 in the nucleoplasm, is rapidly degraded upon DNA-replication stress, resulting in release of Suc22 to form the active RNR complex in the cytoplasm. Here, we show that Caf1, a component of the Ccr4-Not complex, is responsible for resistance of the replication stress and control of the Suc22 translocation. Caf1 is required not only for the stress-induced translocation of Suc22 from nucleoplasm to cytoplasm but also for the degradation of nucleoplasmic Spd1. DNA-replication stress appears to allow Caf1 to interact with Suc22, resulting in release of the nucleoplasmic Spd1-Suc22 assembly. Taken together, these results suggest a novel function of Caf1 as a key regulator in the stress-induced RNR activation.","authors":"Takahashi S, Kontani K, Araki Y, Katada T","authors_abbrev":"Takahashi S et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-02-01","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC9E9.08","SPCC18.06c","SPBC25D12.04"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:15548596","title":"Analysis of mutant phenotypes and splicing defects demonstrates functional collaboration between the large and small subunits of the essential splicing factor U2AF in vivo.","citation":"Mol Biol Cell 2005 Feb;16(2):584-96","abstract":"The heterodimeric splicing factor U2AF plays an important role in 3' splice site selection, but the division of labor between the two subunits in vivo remains unclear. In vitro assays led to the proposal that the human large subunit recognizes 3' splice sites with extensive polypyrimidine tracts independently of the small subunit. We report in vivo analysis demonstrating that all five domains of spU2AFLG are essential for viability; a partial deletion of the linker region, which forms the small subunit interface, produces a severe growth defect and an aberrant morphology. A small subunit zinc-binding domain mutant confers a similar phenotype, suggesting that the heterodimer functions as a unit during splicing in Schizosaccharomyces pombe. As this is not predicted by the model for metazoan 3' splice site recognition, we sought introns for which the spU2AFLG and spU2AFSM make distinct contributions by analyzing diverse splicing events in strains harboring mutations in each partner. Requirements for the two subunits are generally parallel and, moreover, do not correlate with the length or strength of the 3' pyrimidine tract. These and other studies performed in fission yeast support a model for 3' splice site recognition in which the two subunits of U2AF functionally collaborate in vivo.","authors":"Webb CJ, Lakhe-Reddy S, Romfo CM, Wise JA","authors_abbrev":"Webb CJ et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2004-11-19","publication_year":"2005","canto_session_key":"e81392bd8d0bb821","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-23 15:10:06","canto_approved_date":"2026-02-16 16:37:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-11 15:04:45","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":58,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPBC146.07","SPAC664.07c","SPCC1919.01","SPAC9E9.08","SPCC16A11.08","SPBP22H7.07","SPAC17A5.16","SPAC17G8.14c","SPBC1703.14c","SPAC8F11.03","SPCC18B5.06","SPAC20G4.01","SPAP8A3.06","SPAC6F6.15","SPAC11E3.09","SPBC557.03c","SPAC20G8.01","SPBC11B10.09","SPBP16F5.02","SPCC1259.13"],"gene_count":21,"ltp_gene_count":2,"approved_date":"2015-07-23"},{"uniquename":"PMID:17496123","title":"The Schizosaccharomyces pombe Cdc7 protein kinase required for septum formation is a client protein of Cdc37.","citation":"Eukaryot Cell 2007 Jul;6(7):1089-96","abstract":"Cdc37 is an essential molecular chaperone found in fungi and metazoa whose main specificity is for certain protein kinases. Cdc37 can act as an Hsp90 cochaperone or alone; in yeasts, the interaction with Hsp90 is weak and appears not to be essential for Cdc37 function. Numerous genetic interactions between Cdc37 and likely client proteins have been observed in yeasts, but biochemical confirmation has been reported in only a few cases. We and others have generated and characterized temperature-sensitive cdc37 alleles in S. pombe and have used them to investigate the cellular roles of Cdc37: previous work has shown that mitotic Cdc2 is a major client. In this paper, we describe a screen for mutations synthetically lethal with a cdc37ts mutant with the aim of identifying genes encoding further client proteins of Cdc37. Ten such strains were isolated, and genomic libraries were screened for rescuing plasmids. In one case, a truncated cdc7 gene was identified. Further experiments showed that the mutation in this strain was indeed in cdc7. Cdc7 is a protein kinase required for septum initiation, and we show that its kinase activity is greatly reduced when Cdc37 function is impaired. Cdc7 normally locates to the spindle pole body during mitosis, and this appears to be unaffected in the cdc37ts mutant. Other evidence suggests that, in addition to mitosis and septum initiation, Cdc37 may also be required for septum cleavage.","authors":"Liang J, Fantes P","authors_abbrev":"Liang J et al.","pubmed_publication_date":"Jul 2007","pubmed_entrez_date":"2007-05-15","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21.06c","SPBC9B6.10"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12944481","title":"Molecular characterization of the Schizosaccharomyces pombe nbs1+ gene involved in DNA repair and telomere maintenance.","citation":"Mol Cell Biol 2003 Sep;23(18):6553-63","abstract":"The human MRN complex is a multisubunit nuclease that is composed of Mre11, Rad50, and Nbs1 and is involved in homologous recombination and DNA damage checkpoints. Mutations of the MRN genes cause genetic disorders such as Nijmegen breakage syndrome. Here we identified a Schizosaccharomyces pombe nbs1(+) homologue by screening for mutants with mutations that caused methyl methanesulfonate (MMS) sensitivity and were synthetically lethal with the rad2Delta mutation. Nbs1 physically interacts with the C-terminal half of Rad32, the Schizosaccharomyces pombe Mre11 homologue, in a yeast two-hybrid assay. nbs1 mutants showed sensitivities to gamma-rays, UV, MMS, and hydroxyurea and displayed telomere shortening similar to the characteristics of rad32 and rad50 mutants. nbs1, rad32, and rad50 mutant cells were elongated and exhibited abnormal nuclear morphology. These findings indicate that S. pombe Nbs1 forms a complex with Rad32-Rad50 and is required for homologous recombination repair, telomere length regulation, and the maintenance of chromatin structure. Amino acid sequence features and some characteristics of the DNA repair function suggest that the S. pombe Rad32-Rad50-Nbs1 complex has functional similarity to the corresponding MRN complexes of higher eukaryotes. Therefore, S. pombe Nbs1 will provide an additional model system for studying the molecular function of the MRN complex associated with genetic diseases.","authors":"Ueno M, Nakazaki T, Akamatsu Y, Watanabe K, Tomita K, Lindsay HD, Shinagawa H, Iwasaki H","authors_abbrev":"Ueno M et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-08-29","publication_year":"2003","canto_session_key":"35666363d66653ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-27 13:39:44","canto_approved_date":"2023-01-18 09:22:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-13 21:12:11","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.06c","SPAC13C5.07","SPAC644.14c","SPAC16A10.07c","SPBC216.05","SPBC6B1.09c","SPAC1556.01c","SPAC20H4.07"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2015-04-27"},{"uniquename":"PMID:36825780","title":"Myosin II regulatory light chain phosphorylation and formin availability modulate cytokinesis upon changes in carbohydrate metabolism.","citation":"Elife 2023 Feb 24;12","abstract":"Cytokinesis, the separation of daughter cells at the end of mitosis, relies in animal cells on a contractile actomyosin ring (CAR) composed of actin and class II myosins, whose activity is strongly influenced by regulatory light chain (RLC) phosphorylation. However, in simple eukaryotes such as the fission yeast  Schizosaccharomyces pombe , RLC phosphorylation appears dispensable for regulating CAR dynamics. We found that redundant phosphorylation at Ser35 of the  S. pombe  RLC homolog Rlc1 by the p21-activated kinases Pak1 and Pak2, modulates myosin II Myo2 activity and becomes essential for cytokinesis and cell growth during respiration. Previously, we showed that the stress-activated protein kinase pathway (SAPK) MAPK Sty1 controls fission yeast CAR integrity by downregulating formin For3 levels (Gómez-Gil et al., 2020). Here, we report that the reduced availability of formin For3-nucleated actin filaments for the CAR is the main reason for the required control of myosin II contractile activity by RLC phosphorylation during respiration-induced oxidative stress. Thus, the restoration of For3 levels by antioxidants overrides the control of myosin II function regulated by RLC phosphorylation, allowing cytokinesis and cell proliferation during respiration. Therefore, fine-tuned interplay between myosin II function through Rlc1 phosphorylation and environmentally controlled actin filament availability is critical for a successful cytokinesis in response to a switch to a respiratory carbohydrate metabolism.","doi":"10.7554/eLife.83285","authors":"Prieto-Ruiz F, Gómez-Gil E, Martín-García R, Pérez-Díaz AJ, Vicente-Soler J, Franco A, Soto T, Pérez P, Madrid M, Cansado J","authors_abbrev":"Prieto-Ruiz F et al.","pubmed_publication_date":"24 Feb 2023","pubmed_entrez_date":"2023-02-24","publication_year":"2023","canto_session_key":"f4b2a6b2ca02dd13","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-02-25 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20007600","title":"The N-terminus of Prp1 (Prp6/U5-102 K) is essential for spliceosome activation in vivo.","citation":"Nucleic Acids Res 2010 Mar;38(5):1610-22","abstract":"The spliceosomal protein Prp1 (Prp6/U5-102 K) is necessary for the integrity of pre-catalytic spliceosomal complexes. We have identified a novel regulatory function for Prp1. Expression of mutations in the N-terminus of Prp1 leads to the accumulation of pre-catalytic spliceosomal complexes containing the five snRNAs U1, U2, U5 and U4/U6 and pre-mRNAs. The mutations in the N-terminus, which prevent splicing to occur, include in vitro and in vivo identified phosphorylation sites of Prp4 kinase. These sites are highly conserved in the human ortholog U5-102 K. The results presented here demonstrate that structural integrity of the N-terminus is required to mediate a splicing event, but is not necessary for the assembly of spliceosomes.","doi":"10.1093/nar/gkp1155","authors":"Lützelberger M, Bottner CA, Schwelnus W, Zock-Emmenthal S, Razanau A, Käufer NF","authors_abbrev":"Lützelberger M et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2009-12-17","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC6B1.07","SPBC1685.10","SPBC776.01","SPCC777.14","SPBC119.13c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:9529887","title":"Molecular genetics of mating recognition in basidiomycete fungi.","citation":"Microbiol Mol Biol Rev 1998 Mar;62(1):55-70","abstract":"The recognition of compatible mating partners in the basidiomycete fungi requires the coordinated activities of two gene complexes defined as the mating-type genes. One complex encodes members of the homeobox family of transcription factors, which heterodimerize on mating to generate an active transcription regulator. The other complex encodes peptide pheromones and 7-transmembrane receptors that permit intercellular signalling. Remarkably, a single species may have many thousands of cross-compatible mating types because the mating-type genes are multiallelic. Different alleles of both sets of genes are necessary for mating compatibility, and they trigger the initial stages of sexual development--the formation of a specialized filamentous mycelium termed the dikaryon, in which the haploid nuclei remain closely associated in each cell but do not fuse. Three species have been taken as models to describe the molecular structure and organization of the mating-type loci and the genes sequestered within them: the pathogenic smut fungus Ustilago maydis and the mushrooms Coprinus cinereus and Schizophyllum commune. Topics addressed in this review are the roles of the mating-type gene products in regulating sexual development, the molecular basis for multiple mating types, and the molecular interactions that permit different allelic products of the mating type genes to be discriminated. Attention is drawn to the remarkable conservation in the mechanisms that regulate sexual development in basidiomycetes and unicellular ascomycete yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe, a theme which is developed in the general conclusion to include the filamentous ascomycetes Neurospora crassa and Podospora anserina.","authors":"Casselton LA, Olesnicky NS","authors_abbrev":"Casselton LA et al.","pubmed_publication_date":"Mar 1998","pubmed_entrez_date":"1998-04-08","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8668157","title":"Schizosaccharomyces pombe map1+ encodes a MADS-box-family protein required for cell-type-specific gene expression.","citation":"Mol Cell Biol 1996 Jul;16(7):3420-8","abstract":"We cloned the Schizosaccharomyces pombe map1 gene by virtue of its ability to stimulate transcription of the sxa2 gene, which encodes a carboxypeptidase expressed specifically in h- cells in response to mating-pheromone signaling. The cloned gene had a coding capacity of 398 amino acids split by two introns, and the deduced product was a protein of the MADS box family. This gene was most similar to Saccharomyces cerevisiae MCM1, which regulates cell-type-specific gene expression in budding yeast cells. Disruption of the S. pombe gene did not affect vegetative cell growth but conferred sterility. It blocked the mating ability of h+ cells completely and that of h- cells partially. Genetic and sequencing analysis indicated that the cloned gene is map1], which was originally defined by a mutation that caused h+-speciftic sterility. Northern (RNA) blot analysis showed that the function of map1 is absolutely essential for the expression of h+-specific genes and is required for the full activation of h--specific gene expression. Overexpression of map1 resulted in enhanced transcription of cell-type-specilic genes, but the range of genes affected by Map1 was restricted by the mating type of the cell. Results of yeast two-hybrid analysis suggested that Map1 may physically interact with Mat1-Pc, the product of the h(+)-specific mating-type gene mat1-Pc. On the basis of these observations, we speculate that Map1 may be a transcriptional regulator of cell-type-specific genes similar to S. cerevisiae MCM1, whose activity is modulated by the oil and alpha2 mating-type gene products.","authors":"Yabana N, Yamamoto M","authors_abbrev":"Yabana N et al.","pubmed_publication_date":"Jul 1996","pubmed_entrez_date":"1996-07-01","publication_year":"1996","canto_session_key":"bf6ebbd7a7fa9fb9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-12 06:40:16","canto_approved_date":"2026-02-02 10:23:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-12 08:56:54","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP11E10.02c","SPAC1296.03c","SPAC3F10.10c","SPAC11E3.06","SPBC21D10.06c","SPMTR.01","SPBC32C12.02","SPAC11H11.04","SPAC31G5.09c","SPCC1795.06"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2018-10-12"},{"uniquename":"PMID:2020549","title":"Budding yeast CAN1 gene as a selection marker in fission yeast.","citation":"Nucleic Acids Res 1991 Mar 11;19(5):1150","abstract":"","authors":"Ekwall K, Ruusala T","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"11 Mar 1991","pubmed_entrez_date":"1991-03-11","publication_year":"1991","canto_session_key":"1ff0297254ee616d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-07-25 11:10:41","canto_approved_date":"2022-07-14 21:52:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-16 12:20:09","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18H10.20c","SPBC18H10.16"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2012-07-25"},{"uniquename":"PMID:17287513","title":"Primed vesicles can be distinguished from docked vesicles by analyzing their mobility.","citation":"J Neurosci 2007 Feb 07;27(6):1386-95","abstract":"Neurotransmitters are released from nerve terminals and neuroendocrine cells by calcium-dependent exocytosis of vesicles. Before fusion, vesicles are docked to the plasma membrane and rendered release competent through a process called priming. Electrophysiological methods such as membrane capacitance measurements and carbon fiber amperometry accurately measure the fusion step of exocytosis with high time resolution but provide only indirect information about priming and docking. Total internal reflection fluorescence microscopy (TIRFM) enables the real-time visualization of vesicles, near the plasma membrane, as they undergo changes from one molecular state to the other. We devised a new method to analyze the mobility of vesicles, which not only allowed us to classify the movement of vesicles in three different categories but also to monitor dynamic changes in the mobility of vesicles over time. We selectively enhanced priming by treating bovine chromaffin cells with phorbol myristate acetate (PMA) or by overexpressing Munc13-1 (mammalian Unc) and analyzed the mobility of large dense-core vesicles. We demonstrate that nearly immobile vesicles represent primed vesicles because the pool of vesicles displaying this type of mobility was significantly increased after PMA treatment and Munc13-1 overexpression and decreased during tetanus toxin expression. Moreover, we showed that the movement of docked but unprimed vesicles is restricted to a confined region of approximately 220 nm diameter. Finally, a small third population of undocked vesicles showed a directed and probably active type of mobility. For the first time, we can thus distinguish the molecular state of vesicles in TIRFM by their mobility.","authors":"Nofal S, Becherer U, Hof D, Matti U, Rettig J","authors_abbrev":"Nofal S et al.","pubmed_publication_date":"07 Feb 2007","pubmed_entrez_date":"2007-02-09","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-12-08 09:49:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24167631","title":"Klf1, a C2H2 zinc finger-transcription factor, is required for cell wall maintenance during long-term quiescence in differentiated G0 phase.","citation":"PLoS One 2013;8(10):e78545","abstract":"Fission yeast, Schizoaccharomyces pombe, is a model for studying cellular quiescence. Shifting to a medium that lacks a nitrogen-source induces proliferative cells to enter long-term G0 quiescence. Klf1 is a Krüppel-like transcription factor with a 7-amino acid Cys2His2-type zinc finger motif. The deletion mutant, ∆klf1, normally divides in vegetative medium, but proliferation is not restored after long-term G0 quiescence. Cell biologic, transcriptomic, and metabolomic analyses revealed a unique phenotype of the ∆klf1 mutant in quiescence. Mutant cells had diminished transcripts related to signaling molecules for switching to differentiation; however, proliferative metabolites for cell-wall assembly and antioxidants had significantly increased. Further, the size of ∆klf1 cells increased markedly during quiescence due to the aberrant accumulation of Calcofluor-positive, chitin-like materials beneath the cell wall. After 4 weeks of quiescence, reversible proliferation ability was lost, but metabolism was maintained. Klf1 thus plays a role in G0 phase longevity by enhancing the differentiation signal and suppressing metabolism for growth. If Klf1 is lost, S. pombe fails to maintain a constant cell size and normal cell morphology during quiescence.","doi":"10.1371/journal.pone.0078545","authors":"Shimanuki M, Uehara L, Pluskal T, Yoshida T, Kokubu A, Kawasaki Y, Yanagida M","authors_abbrev":"Shimanuki M et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-10-30","publication_year":"2013","canto_session_key":"6c783779bf55e958","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomas Pluskal","canto_first_approved_date":"2015-04-14 11:57:59","canto_approved_date":"2020-01-17 20:36:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-18 14:48:37","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tomas Pluskal","community_curator":true,"annotation_count":28,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.09c","SPCC162.10","SPAC343.04c","SPAC1039.05c","SPCC1393.10","SPAC22F3.12c","SPBC2G2.17c","SPAC11H11.04","SPAPJ691.02","SPAC869.09","SPBPB21E7.01c","SPAC11D3.01c","SPBC1198.04c","SPCC74.04","SPCC1442.01","SPBPB21E7.07","SPCC70.08c"],"gene_count":17,"ltp_gene_count":4,"approved_date":"2015-04-14"},{"uniquename":"PMID:9635190","title":"Cut1 is loaded onto the spindle by binding to Cut2 and promotes anaphase spindle movement upon Cut2 proteolysis.","citation":"Curr Biol 1998 May 21;8(11):633-41","abstract":"The Cut1 and Cut2 proteins of the fission yeast Schizosaccharomyces pombe form a complex and are required for the separation of sister chromatids during anaphase. Polyubiquitinated Cut2 degrades at the onset of anaphase and this degradation, like that of mitotic cyclin, is dependent on the anaphase-promoting complex/cyclosome. Expression of Cut2 that cannot be degraded blocks sister chromatid separation and anaphase spindle elongation. Here, we have investigated the role of the Cut1-Cut2 interaction in sister chromatid separation.\nThe carboxyl terminus of Cut2 interacts with the amino terminus of Cut1, and temperature-sensitive Cut2 mutants expressed Cut2 proteins that contain substitutions in the carboxyl terminus and fail to interact with Cut1, resulting in aberrant anaphase. Localization of Cut1 alters dramatically during the cell cycle. Cut1 is retained in the cytoplasm during interphase and moves to the mitotic spindle pole bodies and the spindle upon entry into prophase, when spindles are formed. The association between Cut2 and Cut1 is needed for the localization of Cut1 to the spindles, as Cut1 remains unbound to the spindle if complex formation is impaired. Cut2 degrades during anaphase, but Cut1 remains bound to the anaphase spindle. This association with the anaphase spindle requires the conserved carboxyl terminus of Cut1.\nComplex formation between Cut1 and Cut2 is needed for the onset of normal anaphase. Cut2 is required for loading Cut1 onto the spindle at prophase and Cut2 proteolysis is needed for the active participation of Cut1 in sister chromatid separation.","authors":"Kumada K, Nakamura T, Nagao K, Funabiki H, Nakagawa T, Yanagida M","authors_abbrev":"Kumada K et al.","pubmed_publication_date":"21 May 1998","pubmed_entrez_date":"1998-06-23","publication_year":"1998","canto_session_key":"25aefd25e9ecb150","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-09-28 14:33:24","canto_approved_date":"2024-05-02 07:40:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-06 10:03:02","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.04","SPBC14C8.01c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-09-28"},{"uniquename":"PMID:8995275","title":"An oxidase-permease-based iron transport system in Schizosaccharomyces pombe and its expression in Saccharomyces cerevisiae.","citation":"J Biol Chem 1997 Jan 03;272(1):401-5","abstract":"Genetic studies have demonstrated that high affinity ferrous transport in Saccharomyces cerevisiae requires an oxidase (Fet3p) and a permease (Ftr1p). Using an iron-independent galactose-based expression system, we show that expression of these two genes can mediate high affinity ferrous iron transport, indicating that these two genes are not only necessary, but sufficient for high affinity iron transport. Schizosaccharomyces pombe also employ an oxidase-permease system for high affinity iron transport. The S. pombe genes, fio1+ (ferrous iron oxidase) and fip1+ (ferriferous permease), share significant similarity to FET3 and FTR1 from S. cerevisiae. Both fio1+ and fip1+ are transcriptionally regulated by iron need, and disruption of fio1+ results in a loss of high affinity iron transport. Expression of fio1+ alone in an S. cerevisiae fet3 disruption strain does not result in high affinity iron transport. This result indicates that the S. pombe ferroxidase, while functionally homologous to the S. cerevisiae ferroxidase, does not have enough similarity to interact with the S. cerevisiae permease. Simultaneous expression of both S. pombe genes, fio1+ and fip1+, in S. cerevisiae can reconstitute high affinity iron transport. These results demonstrate that the oxidase and permease are all that is required to reconstitute high affinity iron transport and suggest that such transport systems are found in other eukaryotes.","authors":"Askwith C, Kaplan J","authors_abbrev":"Askwith C et al.","pubmed_publication_date":"03 Jan 1997","pubmed_entrez_date":"1997-01-03","publication_year":"1997","canto_session_key":"3a2dde8117141243","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-02-02 04:19:12","canto_approved_date":"2024-04-12 06:45:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-11-08 16:58:43","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.08","SPAC1F7.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-02-02"},{"uniquename":"PMID:29423856","title":"High-Frequency Lithium Acetate Transformation of Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2018;1721:167-177","abstract":"The introduction of ectopic DNA, such as plasmids, into yeast cells has for decades been a critical protocol for the study of this eukaryotic model system. We describe here an efficient transformation procedure for use in the fission yeast Schizosaccharomyces pombe. This method relies on chemical agents (lithium acetate, and polyethylene glycol) and temperature stresses, which ultimately facilitate transfer of the genetic material through the cell wall and plasma membrane without significant impact on the transferred DNA or the recipient cell. Using this protocol, we consistently see transformation efficiencies between 1.0 × 10 3  and 1.0 × 10 4  transformants per microgram of the plasmid with 10 8  S. pombe cells. The principal benefits and advantages of this method are its simplicity, efficiency, and relative speed of completion.","doi":"10.1007/978-1-4939-7546-4_15","authors":"Rai SK, Atwood-Moore A, Levin HL","authors_abbrev":"Rai SK et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20211173","title":"Chd1 remodelers maintain open chromatin and regulate the epigenetics of differentiation.","citation":"Exp Cell Res 2010 May 01;316(8):1316-23","abstract":"Eukaryotic DNA is packaged around octamers of histone proteins into nucleosomes, the basic unit of chromatin. In addition to enabling meters of DNA to fit within the confines of a nucleus, the structure of chromatin has functional implications for cell identity. Covalent chemical modifications to the DNA and to histones, histone variants, ATP-dependent chromatin remodelers, small noncoding RNAs and the level of chromatin compaction all contribute to chromosomal structure and to the activity or silencing of genes. These chromatin-level alterations are defined as epigenetic when they are heritable from mother to daughter cell. The great diversity of epigenomes that can arise from a single genome permits a single, totipotent cell to generate the hundreds of distinct cell types found in humans. Two recent studies in mouse and in fly have highlighted the importance of Chd1 chromatin remodelers for maintaining an open, active chromatin state. Based on evidence from fission yeast as a model system, we speculate that Chd1 remodelers are involved in the disassembly of nucleosomes at promoter regions, thus promoting active transcription and open chromatin. It is likely that these nucleosomes are specifically marked for disassembly by the histone variant H2A.Z.","doi":"10.1016/j.yexcr.2010.02.029","authors":"Persson J, Ekwall K","authors_abbrev":"Persson J et al.","pubmed_publication_date":"01 May 2010","pubmed_entrez_date":"2010-03-10","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12153042","title":"Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe.","citation":"J Biomol NMR 2002 Jun;23(2):155-6","abstract":"","authors":"Odaert B, Landrieu I, Dijkstra K, Schuurman-Wolters G, Casteels P, Wieruszeski JM, Scheek R, Lippens G","authors_abbrev":"Odaert B et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-08-03","publication_year":"2002","canto_session_key":"9b4984827175f550","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 10:03:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-20 10:03:02","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1734.14c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:15866025","title":"Bub1 and the multilayered inhibition of Cdc20-APC/C in mitosis.","citation":"Trends Cell Biol 2005 May;15(5):231-3","abstract":"To ensure the accuracy of chromosome segregation in mitosis, the spindle checkpoint blocks the activity of the anaphase-promoting complex APC/C until all chromosomes are properly bi-orientated on the metaphase spindle. How the checkpoint machinery actually inhibits the APC/C is still unclear. A new paper by Tang and coworkers helps further our understanding of this complex and fundamental process.","authors":"Vanoosthuyse V, Hardwick KG","authors_abbrev":"Vanoosthuyse V et al.","pubmed_publication_date":"May 2005","pubmed_entrez_date":"2005-05-04","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21200030","title":"Correlated fluorescence and 3D electron microscopy with high sensitivity and spatial precision.","citation":"J Cell Biol 2011 Jan 10;192(1):111-9","abstract":"Correlative electron and fluorescence microscopy has the potential to elucidate the ultrastructural details of dynamic and rare cellular events, but has been limited by low precision and sensitivity. Here we present a method for direct mapping of signals originating from ∼20 fluorescent protein molecules to 3D electron tomograms with a precision of less than 100 nm. We demonstrate that this method can be used to identify individual HIV particles bound to mammalian cell surfaces. We also apply the method to image microtubule end structures bound to mal3p in fission yeast, and demonstrate that growing microtubule plus-ends are flared in vivo. We localize Rvs167 to endocytic sites in budding yeast, and show that scission takes place halfway through a 10-s time period during which amphiphysins are bound to the vesicle neck. This new technique opens the door for direct correlation of fluorescence and electron microscopy to visualize cellular processes at the ultrastructural scale.","doi":"10.1083/jcb.201009037","authors":"Kukulski W, Schorb M, Welsch S, Picco A, Kaksonen M, Briggs JA","authors_abbrev":"Kukulski W et al.","pubmed_publication_date":"10 Jan 2011","pubmed_entrez_date":"2011-01-05","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16754953","title":"Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p.","citation":"J Cell Biol 2006 Jun 05;173(5):651-8","abstract":"Mgm1p is a conserved dynamin-related GTPase required for fusion, morphology, inheritance, and the genome maintenance of mitochondria in Saccharomyces cerevisiae. Mgm1p undergoes unconventional processing to produce two functional isoforms by alternative topogenesis. Alternative topogenesis involves bifurcate sorting in the inner membrane and intramembrane proteolysis by the rhomboid protease Pcp1p. Here, we identify Ups1p, a novel mitochondrial protein required for the unique processing of Mgm1p and for normal mitochondrial shape. Our results demonstrate that Ups1p regulates the sorting of Mgm1p in the inner membrane. Consistent with its function, Ups1p is peripherally associated with the inner membrane in the intermembrane space. Moreover, the human homologue of Ups1p, PRELI, can fully replace Ups1p in yeast cells. Together, our findings provide a conserved mechanism for the alternative topogenesis of Mgm1p and control of mitochondrial morphology.","authors":"Sesaki H, Dunn CD, Iijima M, Shepard KA, Yaffe MP, Machamer CE, Jensen RE","authors_abbrev":"Sesaki H et al.","pubmed_publication_date":"05 Jun 2006","pubmed_entrez_date":"2006-06-07","publication_year":"2006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D82575","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15791413","title":"Comparison of Dam tagging and chromatin immunoprecipitation as tools for the identification of the binding sites for S. pombe CENP-C.","citation":"Chromosome Res 2005;13(1):73-83","abstract":"We have established the identity of the Schizosaccharomyces pombe homologue of vertebrate CENP-C and Saccharomyces cerevisiae MIF2p and have used it to compare Dam tagging and chromatin immunoprecipitation (ChiP)as tools for the mapping of protein binding sites on DNA. ChiP shows that S. pombe CENP-C binds to the central core and inner repeats of the S. pombe centromere. It binds weakly, however, to the outer repeats. The binding pattern is thus similar to that of S. pombe CENP-A. Dam-tagged S. pombe CENP-C, however, methylates the entire centromere and 5 kb of flanking DNA. This comparison suggests that Dam tagging is less precise as a tool for mapping DNA binding sites than ChiP. We have also used the Dam tagging technique to address the question of whether there is any CENP-C binding to the ribosomal DNA in S. pombe and find none.","authors":"Holland S, Ioannou D, Haines S, Brown WR","authors_abbrev":"Holland S et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-03-26","publication_year":"2005","canto_session_key":"d3effd4d831c58d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1861.01c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:27180904","title":"Sterol-Rich Membrane Domains Define Fission Yeast Cell Polarity.","citation":"Cell 2016 May 19;165(5):1182-1196","abstract":"Cell polarization is crucial for the functioning of all organisms. The cytoskeleton is central to the process but its role in symmetry breaking is poorly understood. We study cell polarization when fission yeast cells exit starvation. We show that the basis of polarity generation is de novo sterol biosynthesis, cell surface delivery of sterols, and their recruitment to the cell poles. This involves four phases occurring independent of the polarity factor cdc42p. Initially, multiple, randomly distributed sterol-rich membrane (SRM) domains form at the plasma membrane, independent of the cytoskeleton and cell growth. These domains provide platforms on which the growth and polarity machinery assembles. SRM domains are then polarized by the microtubule-dependent polarity factor tea1p, which prepares for monopolar growth initiation and later switching to bipolar growth. SRM polarization requires F-actin but not the F-actin organizing polarity factors for3p and bud6p. We conclude that SRMs are key to cell polarization.","doi":"10.1016/j.cell.2016.04.037","authors":"Makushok T, Alves P, Huisman SM, Kijowski AR, Brunner D","authors_abbrev":"Makushok T et al.","pubmed_publication_date":"19 May 2016","pubmed_entrez_date":"2016-05-17","publication_year":"2016","canto_session_key":"b2f0190c9fa67e22","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-05-19 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1223.06","SPBC146.13c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:22633491","title":"Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery.","citation":"Mol Cell 2012 May 25;46(4):542-8","abstract":"N-linked glycosylation is an important posttranslational modification in all eukaryotes, but little is known about the N-glycoproteomes in nonmammalian systems. Here, we measure N-glycoproteomes of the major model organisms Arabidopsis thaliana, Schizosaccharomyces pombe, Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, and Danio rerio, representatively spanning the eukaryotic domain of life. The number of detected N-glycosylation sites varied between 425 in fission yeast, 516 in budding yeast, 1,794 in worm, 2,186 in plant, 2,229 in fly, and 2,254 in zebrafish. We find that all eukaryotic N-glycoproteomes have invariant characteristics including sequence recognition patterns, structural constraints, and subcellular localization. However, a surprisingly large percentage of the N-glycoproteome evolved after the phylogenetic divergences between plants, fungi, nematodes, insects, and vertebrates. Many N-glycosylated proteins coevolved with the rise of extracellular processes that are specific within corresponding phylogenetic groups and essential for organismal development, body growth, and organ formation.","doi":"10.1016/j.molcel.2012.04.031","authors":"Zielinska DF, Gnad F, Schropp K, Wiśniewski JR, Mann M","authors_abbrev":"Zielinska DF et al.","pubmed_publication_date":"25 May 2012","pubmed_entrez_date":"2012-05-29","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":425,"orcid":"0000-0003-4148-4606","file_type":"protein_modification","file_name":"PMID_22633491_modifications.tsv"}],"genes":["SPAPB1E7.04c","SPAC27D7.11c","SPBC1921.06c","SPBC21D10.11c","SPAC17G6.03","SPAC4G8.13c","SPBC19C2.09","SPCC1840.07c","SPAC3C7.11c","SPAC977.09c","SPAPB24D3.03","SPAC1B3.05","SPBC4F6.09","SPAC664.09","SPBC839.08c","SPBPJ4664.06","SPBC21C3.12c","SPBC21C3.17c","SPBC1105.05","SPCC162.09c","SPAC26H5.05","SPCC11E10.02c","SPAC1D4.04","SPBC776.03","SPBC27B12.06","SPBC36.11","SPBC651.06","SPBP4G3.02","SPAC27D7.09c","SPAC23A1.04c","SPAC4G8.12c","SPBC3D6.02","SPAC2G11.07c","SPBC29A10.01","SPBC3E7.08c","SPCC24B10.21","SPAC22E12.06c","SPBC646.05c","SPBC947.01","SPBC24C6.06","SPAC167.01","SPAC29E6.10c","SPCC1739.13","SPAC1486.05","SPAC630.12","SPAC1039.02","SPBC2G5.05","SPBC28F2.09","SPAC17A2.05","SPAC637.06","SPAC57A10.02","SPCC1450.14c","SPBC21B10.07","SPAC11G7.02","SPCC757.05c","SPBC16D10.05","SPBC13G1.11","SPBC947.04","SPBC16H5.09c","SPCC11E10.05c","SPAC19A8.04","SPAC26A3.01","SPBC3B8.06","SPBC543.10","SPAC23C11.11","SPAC4A8.04","SPBC1815.01","SPAC1705.03c","SPAC9E9.09c","SPBC19G7.10c","SPBC27B12.11c","SPAC1006.01","SPBC15D4.07c","SPCC1259.02c","SPAC3F10.11c","SPBC27.06c","SPAC25H1.07","SPBC32H8.08c","SPBC16G5.09","SPAC13F5.05","SPAC1834.05","SPBC354.05c","SPBC947.10","SPBC15C4.06c","SPBC1683.09c","SPAC1F7.08","SPAC3A11.10c","SPAC32A11.03c","SPAC5H10.13c","SPBC29A10.07","SPBC3B9.15c","SPBC36B7.03","SPAC23C4.16c","SPBC18H10.18c","SPAC56F8.11","SPBC337.07c","SPBC11B10.07c","SPBC1703.10","SPAC11E3.13c","SPAC2E1P5.01c","SPAC23A1.02c","SPCC18.01c","SPCC569.06","SPAC7D4.14c","SPBP35G2.14","SPAC24B11.08c","SPBC36.02c","SPBC23G7.16","SPAC1071.11","SPAC23H3.15c","SPAC20G8.07c","SPAC23H4.14","SPCC306.06c","SPCC757.12","SPBC21H7.03c","SPAC167.09","SPAC167.05","SPBC1709.05","SPBC13E7.02","SPCC4G3.13c","SPAC19G12.16c","SPCC63.14","SPCC777.12c","SPCC1322.14c","SPAC227.11c","SPAC6G9.14","SPAP14E8.03","SPBC1685.03","SPCC1919.02","SPBC28F2.08c","SPAC22A12.15c","SPAC4D7.07c","SPBC1709.03","SPAC31A2.13c","SPAC13G6.03","SPBC1105.02c","SPAC13G7.04c","SPAC22H12.05c","SPAC8F11.10c","SPAC17C9.03","SPAC977.05c","SPBC16A3.18","SPAP8A3.03","SPBC29A10.08","SPBC776.14","SPAC31G5.02","SPAC12B10.16c","SPBC20F10.07","SPAC1B3.10c","SPBC530.09c","SPBC14F5.13c","SPAC1A6.03c","SPBPB2B2.06c","SPAC23C4.05c","SPAC1142.05","SPAC1A6.07","SPAC630.08c","SPAC22E12.16c","SPCC553.11c","SPBC15C4.04c","SPBC1198.06c","SPAC17D4.03c","SPBC1347.04","SPBC4F6.06","SPCC1840.02c","SPBC19C7.12c","SPCC1795.11","SPAPB1E7.09","SPAC56E4.06c","SPCC1919.12c","SPBC428.03c","SPBC16C6.09","SPBC530.12c","SPAC4G8.10","SPAC17C9.08","SPACUNK4.08","SPAC11E3.11c","SPCC645.07","SPAC21E11.08","SPAC23A1.10","SPAC3A12.17c","SPCC306.11","SPAC1F5.06","SPAC19D5.02c","SPAC17C9.12","SPBC16C6.06","SPAC821.09","SPBC1198.07c","SPAC19B12.02c","SPAC1002.03c","SPAC27E2.07","SPBP4H10.19c","SPAC1F8.03c","SPAC29B12.10c","SPBC27B12.03c","SPBCPT2R1.08c","SPBC713.07c","SPAC23C4.13","SPBC215.14c","SPAPB8E5.04c","SPBC16C6.07c","SPCC1281.01","SPBC119.10","SPBC1711.12","SPAC24C9.08","SPBC354.09c","SPBC1604.05","SPAC22A12.07c","SPAC16C9.06c","SPAC1A6.04c","SPAC4F10.14c","SPAC27F1.07","SPAC824.02","SPAC1782.11","SPCC594.01","SPAC22E12.02","SPAPJ760.02c","SPAC25B8.04c","SPAPB2C8.01","SPBC3B9.10","SPCC338.15","SPAC26H5.08c","SPAC824.09c","SPAC343.14c","SPAC1610.04","SPAC6F6.06c","SPBC3E7.09","SPBC16A3.17c","SPBC3H7.15","SPBC4F6.16c","SPBC839.16","SPAC1639.01c","SPBC216.02","SPBC12D12.01","SPAC1F5.02","SPBC14C8.19","SPAC30D11.01c","SPAC17G6.11c","SPBC28F2.11","SPBC725.05c","SPCC4F11.04c","SPBC83.10","SPCC63.02c","SPAC2G11.09","SPBC146.10","SPAC17G8.11c","SPAC3G9.08","SPAC1786.02","SPAC23G3.06","SPCC285.05","SPBC725.08"],"gene_count":251,"ltp_gene_count":0},{"uniquename":"PMID:30448942","title":"Building the contractile ring from the ground up: a lesson in perseverance and scientific creativity.","citation":"Biophys Rev 2018 Dec;10(6):1491-1497","abstract":"This contribution to the Festschrift for Professor Thomas (Tom) D. Pollard focuses on his work on the elucidation of the protein organization within the cytokinetic nodes, protein assemblies, precursors to the contractile ring. In particular, this work highlights recent discoveries in the molecular organization of the proteins that make the contractile machine in fission yeast using advanced microscopy techniques. One of the main aspects of Tom's research philosophy that marked my career as one of his trainees is his embrace of interdisciplinary approaches to research. The cost of interdisciplinary research is to be willing to step out of our technical comfort zone to learn a new set of tools. The payoff of interdisciplinary research is the expansion our realm of possibilities by bringing new creative tools and ideas to push our research program forward. The rewarding outcomes of this work under Tom's mentorship were the molecular model of the cytokinetic node and the development of new techniques to unravel the structure of multi-protein complexes in live cells. Together, these findings open a new set of questions about the mechanism of cytokinesis and provide creative tools to address them.","doi":"10.1007/s12551-018-0482-8","authors":"Laplante C","authors_abbrev":"Laplante C","pubmed_publication_date":"Dec 2018","pubmed_entrez_date":"2018-11-19","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-20 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15316103","title":"Meiotic chromosome segregation mutants identified by insertional mutagenesis of fission yeast Schizosaccharomyces pombe; tandem-repeat, single-site integrations.","citation":"Nucleic Acids Res 2004;32(14):4400-10","abstract":"Identification of genes required for segregation of chromosomes in meiosis (scm) is difficult because in most organisms high-fidelity chromosome segregation is essential to produce viable meiotic products. The biology of fission yeast Schizosaccharomyces pombe facilitates identification of such genes. Insertional mutagenesis was achieved by electroporation of linear ura4+ DNA into cells harboring a ura4 deletion. Approximately 1000 stable transformants were screened individually for the production of elevated frequencies of aneuploid spore colonies. Twenty-two candidates were subjected to a secondary screen for cytological defects. Five mutants exhibited significant levels of aberrant meiotic chromosome segregation, but were proficient for mating and completion of meiosis. Each mutant's phenotype cosegregated with its respective ura4+ transgene. The mutations were recessive and defined five complementation groups, revealing five distinct genes (scm1, scm2, scm3, scm4 and scm5). Southern blotting revealed single-site integration in each transformant, indicating that insertional mutagenesis is useful for generating single-locus scm mutations linked to a selectable marker. The transgene insertion points were refractory to analysis by inverse-PCR. Molecular and real-time PCR analyses revealed the presence of multiple, truncated copies of ura4+ at each integration site. Thus, electroporation-mediated insertional mutagenesis in S.pombe is preceded by exonucleolytic processing and concatomerization of the transforming DNA.","authors":"Davidson MK, Young NP, Glick GG, Wahls WP","authors_abbrev":"Davidson MK et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-08-19","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18976909","title":"Genotype-phenotype correlations in ACTA1 mutations that cause congenital myopathies.","citation":"Neuromuscul Disord 2009 Jan;19(1):6-16","abstract":"Mutations in the skeletal muscle actin gene, ACTA1 are responsible for up to 20% of congenital myopathies with a variety of pathologies that includes nemaline myopathy, intranuclear rod myopathy, actin myopathy and congenital fibre type disproportion. In their review of 2003, Sparrow et al. considered how these actin mutations might affect muscle function at the molecular level and thus cause the disease. Since then several laboratories have taken up the challenge of investigating genotype-phenotype relationships experimentally. The objective of this review is to assess the current state of our understanding of the molecular mechanisms of skeletal myopathies and the prospects for future therapies based on this knowledge. Thirty congenital myopathy-causing ACTA1 mutations have been studied using a range of biochemical and in vitro approaches. They showed diverse molecular defects, and there is no obvious pattern seen in mutations resulting in the same histopathology.","doi":"10.1016/j.nmd.2008.09.005","authors":"Feng JJ, Marston S","authors_abbrev":"Feng JJ et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2008-11-04","publication_year":"2009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1883874","title":"sar1, a gene from Schizosaccharomyces pombe encoding a protein that regulates ras1.","citation":"Cell Regul 1991 Jun;2(6):453-65","abstract":"Proper ras1 function is required for normal sexual function in the yeast Schizosaccharomyces pombe. We have found a gene in S. pombe, sar1, that encodes a product capable of regulating ras1 function. sar1 is a member of an expanding family of RAS GTPase-activating proteins (GAPs) that includes mammalian GAP, the yeast Saccharomyces cerevisiae IRA proteins, and the product of the human neurofibromatosis locus, NF1 sar1, like these other proteins, can complement the loss of IRA function in S. cerevisiae. Computer analysis shows that the highest degree of sequence conservation is restricted to a very small number of diagnostic residues represented by the motif Phe-Leu-Arg-X-X-X-Pro-Ala-X-X-X-Pro. We find no evidence that sar1 is required for the effector function of ras1.","authors":"Wang Y, Boguski M, Riggs M, Rodgers L, Wigler M","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"Jun 1991","pubmed_entrez_date":"1991-06-01","publication_year":"1991","canto_session_key":"e42f9397f3987b2a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-04-18 15:40:20","canto_approved_date":"2026-04-08 10:55:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-01 14:27:40","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC646.12c","SPBC24C6.06","SPCC1442.01"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-04-18"},{"uniquename":"PMID:18613214","title":"Low-copy episomal vector pFY20 and high-saturation coverage genomic libraries for the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2008 Sep;25(9):643-50","abstract":"In fission yeast, as in many organisms, episomally replicating plasmid DNA molecules can be used for a wide variety of applications. However, replicating plasmids described previously are each propagated at a high copy number per cell. Plasmid fission yeast twenty (pFY20) contains the ura4(+) gene for positive and negative selection, an origin of replication (ars1) and a stability element (stb). Although this plasmid does not have a centromere, it is propagated with a copy number of about two plasmids per haploid genome equivalent and it is transmitted with relatively high fidelity in mitosis and meiosis. This low-copy vector is useful for screens and mutational studies where overexpression (e.g. from high copy plasmids) is undesirable. We therefore constructed multiple partial-digest, size-fractionated, fission yeast genomic DNA libraries in pFY20 and in the cloning vector pBluescript KS(+). These libraries have sufficient complexity (average of 2100 genome equivalents each) for saturation screening by complementation, plasmid shuffle or hybridization.","doi":"10.1002/yea.1605","authors":"Wahls WP, Davidson MK","authors_abbrev":"Wahls WP et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-07-10","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31562247","title":"Glucose starvation induces mitochondrial fragmentation depending on the dynamin GTPase Dnm1/Drp1 in fission yeast.","citation":"J Biol Chem 2019 Nov 22;294(47):17725-17734","abstract":"Mitochondria undergo morphological and dynamic changes in response to environmental stresses. Few studies have focused on addressing mitochondrial remodeling under stress. Using the fission yeast  Schizosaccharomyces pombe  as a model organism, here we investigated mitochondrial remodeling under glucose starvation. We employed live-cell microscopy to monitor mitochondrial morphology and dynamics of cells in profusion chambers under glucose starvation. Our results revealed that mitochondria fragment within minutes after glucose starvation and that the dynamin GTPase Dnm1 is required for promoting mitochondrial fragmentation. Moreover, we found that glucose starvation enhances Dnm1 localization to mitochondria and increases the frequency of mitochondrial fission but decreases PKA activity. We further demonstrate that low PKA activity enhances glucose starvation-induced mitochondrial fragmentation, whereas high PKA activity confers resistance to glucose starvation-induced mitochondrial fragmentation. Moreover, we observed that AMP-activated protein kinase is not involved in regulating mitochondrial fragmentation under glucose starvation. Of note, glucose starvation-induced mitochondrial fragmentation was associated with enhanced reactive oxygen species production. Our work provides detailed mechanistic insights into mitochondrial remodeling in response to glucose starvation.","doi":"10.1074/jbc.RA119.010185","authors":"Zheng F, Jia B, Dong F, Liu L, Rasul F, He J, Fu C","authors_abbrev":"Zheng F et al.","pubmed_publication_date":"22 Nov 2019","pubmed_entrez_date":"2019-09-29","publication_year":"2019","canto_session_key":"90e7f1df3e7c70af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-19 15:08:20","canto_approved_date":"2023-12-28 10:23:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-10 05:45:57","canto_added_date":"2019-09-30 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1919.03c","SPAC1556.08c","SPBC106.10","SPBC12C2.08","SPBC19C7.03","SPAC8C9.03","SPCC74.03c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2021-01-19"},{"uniquename":"PMID:38041816","title":"Unraveling the mechanisms and evolution of a two-domain module in IQGAP proteins for controlling eukaryotic cytokinesis.","citation":"Cell Rep 2023 Nov 30;42(12):113510","abstract":"The IQGAP family of proteins plays a crucial role in cytokinesis across diverse organisms, but the underlying mechanisms are not fully understood. In this study, we demonstrate that IQGAPs in budding yeast, fission yeast, and human cells use a two-domain module to regulate their localization as well as the assembly and disassembly of the actomyosin ring during cytokinesis. Strikingly, the calponin homology domains (CHDs) in these IQGAPs bind to distinct cellular F-actin structures with varying specificity, whereas the non-conserved domains immediately downstream of the CHDs in these IQGAPs all target the division site, but differ in timing, localization strength, and binding partners. We also demonstrate that human IQGAP3 acts in parallel to septins and myosin-IIs to mediate the role of anillin in cytokinesis. Collectively, our findings highlight the two-domain mechanism by which IQGAPs regulate cytokinesis in distantly related organisms as well as their evolutionary conservation and divergence.","doi":"10.1016/j.celrep.2023.113510","authors":"Wang K, Okada H, Wloka C, Bi E","authors_abbrev":"Wang K et al.","pubmed_publication_date":"30 Nov 2023","pubmed_entrez_date":"2023-12-02","publication_year":"2023","canto_session_key":"dfbcec2a0269ec27","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-07-01 20:36:24","canto_approved_date":"2024-11-28 17:06:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-01 20:33:17","canto_added_date":"2023-12-03 00:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-07-01"},{"uniquename":"PMID:13480293","title":"The growth of single cells. I. Schizosaccharomyces pombe.","citation":"Exp Cell Res 1957 Oct;13(2):244-62","abstract":"","authors":"MITCHISON JM","authors_abbrev":"MITCHISON JM","pubmed_publication_date":"Oct 1957","pubmed_entrez_date":"1957-10-01","publication_year":"1957","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37410615","title":"Heterologous expression of α-1,3-glucanase Agn1p from Schizosaccharomyces pombe, and efficient production of nigero-oligosaccharides by enzymatic hydrolysis from solubilized α-1,3;1,6-glucan.","citation":"Biosci Biotechnol Biochem 2023 Sep 21;87(10):1219-1228","abstract":"The glycoside hydrolase family 71 α-1,3-glucanase (Agn1p) of Schizosaccharomyces pombe was expressed in Escherichia coli Rosetta-gami B (DE3). Agn1p (0.5 nmol/mL) hydrolyzed insoluble α-1,3-glucan (1%), and about 3.3 mm reducing sugars were released after 1440 min of reaction. The analysis of reaction products by high-performance liquid chromatography revealed that pentasaccharides accumulated in the reaction mixture as the main products, along with a small amount of mono-, di-, tri-, tetra-, and hexasaccharides. Soluble glucan was prepared from insoluble α-1,3;1,6-glucan by alkaline and sonication treatment to improve the hydrolytic efficiency. As a result, this solubilized α-1,3;1,6-glucan maintained a solubilized state for at least 6 h. Agn1p (0.5 nmol/mL) hydrolyzed the solubilized α-1,3;1,6-glucan (1%), and about 8.2 mm reducing sugars were released after 240 min of reaction. Moreover, Agn1p released about 12.3 mm reducing sugars from 2% of the solubilized α-1,3;1,6-glucan.","doi":"10.1093/bbb/zbad094","authors":"Horaguchi Y, Takahashi M, Takamatsu K, Konno H, Makabe K, Yano S","authors_abbrev":"Horaguchi Y et al.","pubmed_publication_date":"21 Sep 2023","pubmed_entrez_date":"2023-07-06","publication_year":"2023","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2023-07-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37252866","title":"SpindlesTracker: An Automatic and Low-Cost Labeled Workflow for Spindle Analysis.","citation":"IEEE J Biomed Health Inform 2023 Aug;27(8):4098-4109","abstract":"Quantitative analysis of spindle dynamics in mitosis through fluorescence microscopy requires tracking spindle elongation in noisy image sequences. Deterministic methods, which use typical microtubule detection and tracking methods, perform poorly in the sophisticated background of spindles. In addition, the expensive data labeling cost also limits the application of machine learning in this field. Here we present a fully automatic and low-cost labeled workflow that efficiently analyzes the dynamic spindle mechanism of time-lapse images, called SpindlesTracker. In this workflow, we design a network named YOLOX-SP which can accurately detect the location and endpoint of each spindle under box-level data supervision. We then optimize the algorithm SORT and MCP for spindle's tracking and skeletonization. As there was no publicly available dataset, we annotated a S.pombe dataset that was entirely acquired from the real world for both training and evaluation. Extensive experiments demonstrate that SpindlesTracker achieves excellent performance in all aspects, while reducing label costs by 60%. Specifically, it achieves 84.1% mAP in spindle detection and over 90% accuracy in endpoint detection. Furthermore, the improved algorithm enhances tracking accuracy by 1.3% and tracking precision by 6.5%. Statistical results also indicate that the mean error of spindle length is within 1 μm. In summary, SpindlesTracker holds significant implications for the study of mitotic dynamic mechanisms and can be readily extended to the analysis of other filamentous objects. The code and the dataset are both released on GitHub.","doi":"10.1109/JBHI.2023.3281454","authors":"Li Z, Jian Y, Hu J, Zhang C, Meng X, Liu J","authors_abbrev":"Li Z et al.","pubmed_publication_date":"Aug 2023","pubmed_entrez_date":"2023-05-30","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-05-31 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21030438","title":"Mapping of long-range associations throughout the fission yeast genome reveals global genome organization linked to transcriptional regulation.","citation":"Nucleic Acids Res 2010 Dec;38(22):8164-77","abstract":"We have comprehensively mapped long-range associations between chromosomal regions throughout the fission yeast genome using the latest genomics approach that combines next generation sequencing and chromosome conformation capture (3C). Our relatively simple approach, referred to as enrichment of ligation products (ELP), involves digestion of the 3C sample with a 4 bp cutter and self-ligation, achieving a resolution of 20 kb. It recaptures previously characterized genome organizations and also identifies new and important interactions. We have modeled the 3D structure of the entire fission yeast genome and have explored the functional relationships between the global genome organization and transcriptional regulation. We find significant associations among highly transcribed genes. Moreover, we demonstrate that genes co-regulated during the cell cycle tend to associate with one another when activated. Remarkably, functionally defined genes derived from particular gene ontology groups tend to associate in a statistically significant manner. Those significantly associating genes frequently contain the same DNA motifs at their promoter regions, suggesting that potential transcription factors binding to these motifs are involved in defining the associations among those genes. Our study suggests the presence of a global genome organization in fission yeast that is functionally similar to the recently proposed mammalian transcription factory.","doi":"10.1093/nar/gkq955","authors":"Tanizawa H, Iwasaki O, Tanaka A, Capizzi JR, Wickramasinghe P, Lee M, Fu Z, Noma K","authors_abbrev":"Tanizawa H et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-10-30","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29954949","title":"The  S. pombe  mitochondrial transcriptome.","citation":"RNA 2018 Sep;24(9):1241-1254","abstract":"Mitochondrial gene expression is largely controlled through post-transcriptional processes including mitochondrial RNA (mt-RNA) processing, modification, decay, and quality control. Defective mitochondrial gene expression results in mitochondrial oxidative phosphorylation (OXPHOS) deficiency and has been implicated in human disease. To fully understand mitochondrial transcription and RNA processing, we performed RNA-seq analyses of mt-RNAs from the fission yeast  Schizosaccharomyces pombe  RNA-seq analyses show that the abundance of mt-RNAs vary greatly. Analysis of data also reveals mt-RNA processing sites including an unusual RNA cleavage event by mitochondrial tRNA (mt-tRNA) 5'-end processing enzyme RNase P. Additionally, this analysis reveals previously unknown mitochondrial transcripts including the  rnpB -derived fragment, mitochondrial small RNAs (mitosRNAs) such as mt-tRNA-derived fragments (mt-tRFs) and mt-tRNA halves, and mt-tRNAs marked with 3'-CCACCA/CCACC in  S. pombe  Finally, RNA-seq reveals that inactivation of  trz2  encoding  S. pombe  mitochondrial tRNA 3'-end processing enzyme globally impairs mt-tRNA 3'-end processing, inhibits mt-mRNA 5'-end processing, and causes accumulation of unprocessed transcripts, demonstrating the feasibility of using RNA-seq to examine the protein known or predicted to be involved in mt-RNA processing in  S. pombe  Our work uncovers the complexity of a fungal mitochondrial transcriptome and provides a framework for future studies of mitochondrial gene expression using  S. pombe  as a model system.","doi":"10.1261/rna.064477.117","authors":"Shang J, Yang Y, Wu L, Zou M, Huang Y","authors_abbrev":"Shang J et al.","pubmed_publication_date":"Sep 2018","pubmed_entrez_date":"2018-06-30","publication_year":"2018","canto_session_key":"975af9a2f2803efe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2018-08-09 13:55:41","canto_approved_date":"2022-08-29 16:29:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-22 12:54:11","canto_added_date":"2018-07-01 00:15:03","annotation_curators":[{"name":"Ying Huang","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMITTRNAALA.01","SPMITTRNAGLU.01","SPMITNCRNA.01","SPRRNA.01","SPRRNA.02","SPBC3D6.03c"],"gene_count":6,"ltp_gene_count":1,"approved_date":"2018-08-09"},{"uniquename":"EMBL:AU013839","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35908934","title":"Euchromatin factors HULC and Set1C affect heterochromatin organization and mating-type switching in fission yeast Schizosaccharomyces pombe.","citation":"Genes Genet Syst 2022 Oct 18;97(3):123-138","abstract":"Mating-type (P or M) of fission yeast Schizosaccharomyces pombe is determined by the transcriptionally active mat1 cassette and is switched by gene conversion using a donor, either mat2 or mat3, located in an adjacent heterochromatin region (mating-type switching; MTS). In the switching process, heterochromatic donors of genetic information are selected based on the P or M cell type and on the action of two recombination enhancers, SRE2 promoting the use of mat2-P and SRE3 promoting the use of mat3-M, leading to replacement of the content of the expressed mat1 cassette. Recently, we found that the histone H3K4 methyltransferase complex Set1C participates in donor selection, raising the question of how a complex best known for its effects in euchromatin controls recombination in heterochromatin. Here, we report that the histone H2BK119 ubiquitin ligase complex HULC functions with Set1C in MTS, as mutants in the shf1, brl1, brl2 and rad6 genes showed defects similar to Set1C mutants and belonged to the same epistasis group as set1Δ. Moreover, using H3K4R and H2BK119R histone mutants and a Set1-Y897A catalytic mutant, we found that ubiquitylation of histone H2BK119 by HULC and methylation of histone H3K4 by Set1C are functionally coupled in MTS. Cell-type biases in MTS in these mutants suggested that HULC and Set1C inhibit the use of the SRE3 recombination enhancer in M cells, thus favoring SRE2 and mat2-P. Consistent with this, imbalanced switching in the mutants was traced to compromised association of the directionality factor Swi6 with the recombination enhancers in M cells. Based on their known effects at other chromosomal locations, we speculate that HULC and Set1C control nucleosome mobility and strand invasion near the SRE elements. In addition, we uncovered distinct effects of HULC and Set1C on histone H3K9 methylation and gene silencing, consistent with additional functions in the heterochromatic domain.","doi":"10.1266/ggs.22-00012","authors":"Esquivel-Chávez A, Maki T, Tsubouchi H, Handa T, Kimura H, Haber JE, Thon G, Iwasaki H","authors_abbrev":"Esquivel-Chávez A et al.","pubmed_publication_date":"18 Oct 2022","pubmed_entrez_date":"2022-07-31","publication_year":"2022","canto_session_key":"ed9270b453b0c024","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroshi Iwasaki","canto_first_approved_date":"2025-04-01 07:50:43","canto_approved_date":"2025-04-01 07:50:43","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-03-27 23:08:33","canto_added_date":"2022-08-03 00:15:03","annotation_curators":[{"name":"Hiroshi Iwasaki","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":35,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.03","SPCC188.13c","SPAC21E11.03c","SPCC1919.15","SPCC970.10c","SPCC306.04c","SPAC18B11.07c","SPBC13E7.08c","SPAC22F8.12c","SPAC664.01c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2025-04-01"},{"uniquename":"PMID:9560431","title":"S. pombe sck2+, a second homologue of S. cerevisiae SCH9 in fission yeast, encodes a putative protein kinase closely related to PKA in function.","citation":"Curr Genet 1998 Apr;33(4):248-54","abstract":"The Schizosaccharomyces pombe sck2 gene, originally identified as SPAC22E12.14c in the genome-sequencing project, encodes a putative protein kinase highly similar to Saccharomyces cerevisiae Sch9p and S. pombe Sck1p, both of which can suppress loss of cAMP-dependent protein kinase (PKA) if over-produced. Over-expression of sck2 suppressed typical phenotypes of PKA-defective cells, including ectopic mating, slow growth and short cell morphology. Wild-type cells over-expressing sck2 behaved like the PKA-hyperactive mutant. Disruption of sck2 caused no obvious phenotype, but it intensified de-repression for sexual development when combined with the disruption of sck1. The pka1 sck1 sck2 triple disruptant could grow but only very slowly. Whereas disruption of sck1 enhanced the inefficiency of Deltapka1 spores in germination, disruption of sck2 did not. These results suggest that the molecular function of Sck2p largely overlaps with that of Sck1p, but also that they differ somewhat either quantitatively or qualitatively.","authors":"Fujita M, Yamamoto M","authors_abbrev":"Fujita M et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-05-26","publication_year":"1998","canto_session_key":"d423aed4be8e9264","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-03-08 10:32:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-18 09:13:10","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B9.02c","SPAC22E12.14c","SPBC106.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-09-18"},{"uniquename":"PMID:29298360","title":"Chromosome passenger complex is required for the survival of cells with ring chromosomes in fission yeast.","citation":"PLoS One 2018;13(1):e0190523","abstract":"Ring chromosomes are circular chromosomal abnormalities that have been reported in association with some genetic disorders and cancers. In Schizosaccharomyces pombe, lack of function of protection of telomere 1 (Pot1) or telomerase catalytic subunit (Trt1) results in survivors with circular chromosomes. Hitherto, it is poorly understood how cells with circular chromosomes survive and how circular chromosomes are maintained. Fission yeast Cut17/Bir1, Ark1, Pic1, and Nbl1 is a conserved chromosome passenger complex (CPC) functioning mainly throughout mitosis. Here, using a temperature-sensitive mutant of CPC subunits, we determined that CPC is synthetically lethal in combination with either Pot1 or Trt1. The pot1Δ pic1-T269 double mutant, which has circular chromosomes, showed a high percentage of chromosome mis-segregation and DNA damage foci at 33°C. We furthermore found that neither Shugoshin Sgo2 nor heterochromatin protein Swi6, which contribute to the centromeric localization of CPC, were required for the survival in the absence of Pot1. Both the pot1Δ sgo2Δ and pot1Δ swi6Δ double mutants displayed a high percentage of DNA damage foci, but a low percentage of chromosome mis-segregation, suggesting the link between the high percentage of chromosome mis-segregation and the lethality of the CPC pot1Δ double mutant. Our results suggest that CPC is required for the survival of cells with circular chromosomes and sheds light on the possible roles of CPC in the maintenance of circular chromosomes.","doi":"10.1371/journal.pone.0190523","authors":"Habib AGK, Sugiura K, Ueno M","authors_abbrev":"Habib AGK et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-01-04","publication_year":"2018","canto_session_key":"0e18c17a62e466d0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-01-05 01:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06","SPCC962.02c","SPAC15A10.15","SPBC336.15","SPAC664.01c","SPBC29A3.14c","SPCC320.13c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:12383793","title":"Regulating the actin cytoskeleton during vesicular transport.","citation":"Curr Opin Cell Biol 2002 Aug;14(4):428-33","abstract":"Although the actin cytoskeleton is widely believed to play an important role in intracellular protein transport, this role is poorly understood. Recently, progress has been made toward identifying specific actin-binding proteins and signaling molecules involved in regulating actin structures that function in the secretory pathway. Studies on coat protomer I (COPI)-mediated transport at the Golgi apparatus and on clathrin-mediated endocytosis have been particularly informative in identifying such mechanisms. Important similarities between actin regulation at the Golgi and at the plasma membrane have been uncovered. The studies reveal that ADP-ribosylation factor and vesicle coat proteins are able to act through the Rho-family GTP-binding proteins, Cdc42 and Rac, and several specific actin-binding proteins to direct actin assembly through the Arp2/3 complex. Efficient function of the secretory pathway is likely to require precise temporal regulation among transport-vesicle assembly, vesicle scission, and the targeting machinery. It is proposed that numerous actin regulatory mechanisms and the connections between actin signaling and vesicle-coat formation are employed to provide such temporal regulation.","authors":"Stamnes M","authors_abbrev":"Stamnes M","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-10-18","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16164595","title":"A novel pathway determining multidrug sensitivity in Schizosaccharomyces pombe.","citation":"Genes Cells 2005 Oct;10(10):941-51","abstract":"In this study, we show that a mutation isolated during a screen for determinants of chemosensitivity in S. pombe results in loss of function of a previously uncharacterized protein kinase now named Hal4. Hal4 shares sequence homology to Hal4 and Hal5 in S. cerevisiae, and previous evidence indicates that these kinases positively regulate the major potassium transporter Trk1,2 and thereby maintain the plasma membrane potential. Disruption of this ion homeostasis pathway results in a hyperpolarized membrane and a concomitant increased sensitivity to cations. We demonstrate that a mutation in hal4+ results in hyperpolarization of the plasma membrane. In addition to the original selection agent, the hal4-1 mutant is sensitive to a variety of chemotherapeutic agents and stress-inducing compounds. Furthermore, this wider chemosensitive phenotype is also displayed by corresponding mutants in S. cerevisiae, and in a trk1deltatrk2delta double deletion mutant in S. pombe. We propose that this pathway and its role in regulating the plasma membrane potential may act as a pleiotropic determinant of sensitivity to chemotherapeutic agents.","authors":"Thornton G, Wilkinson CR, Toone WM, Jones N","authors_abbrev":"Thornton G et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-09-17","publication_year":"2005","canto_session_key":"46ec3002e49856a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-09-22 15:59:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-09-22 15:59:17","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":57,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1639.02c","SPAC3F10.02c","SPAC29A4.16"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-09-22"},{"uniquename":"PMID:31745560","title":"Pol5 is required for recycling of small subunit biogenesis factors and for formation of the peptide exit tunnel of the large ribosomal subunit.","citation":"Nucleic Acids Res 2020 Jan 10;48(1):405-420","abstract":"More than 200 assembly factors (AFs) are required for the production of ribosomes in yeast. The stepwise association and dissociation of these AFs with the pre-ribosomal subunits occurs in a hierarchical manner to ensure correct maturation of the pre-rRNAs and assembly of the ribosomal proteins. Although decades of research have provided a wealth of insights into the functions of many AFs, others remain poorly characterized. Pol5 was initially classified with B-type DNA polymerases, however, several lines of evidence indicate the involvement of this protein in ribosome assembly. Here, we show that depletion of Pol5 affects the processing of pre-rRNAs destined for the both the large and small subunits. Furthermore, we identify binding sites for Pol5 in the 5' external transcribed spacer and within domain III of the 25S rRNA sequence. Consistent with this, we reveal that Pol5 is required for recruitment of ribosomal proteins that form the polypeptide exit tunnel in the LSU and that depletion of Pol5 impairs the release of 5' ETS fragments from early pre-40S particles. The dual functions of Pol5 in 60S assembly and recycling of pre-40S AFs suggest that this factor could contribute to ensuring the stoichiometric production of ribosomal subunits.","doi":"10.1093/nar/gkz1079","authors":"Braun CM, Hackert P, Schmid CE, Bohnsack MT, Bohnsack KE, Perez-Fernandez J","authors_abbrev":"Braun CM et al.","pubmed_publication_date":"10 Jan 2020","pubmed_entrez_date":"2019-11-21","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14C8.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11744736","title":"Selective inhibition of MAPKK Wis1 in the stress-activated MAPK cascade of Schizosaccharomyces pombe by novel berberine derivatives.","citation":"J Biol Chem 2002 Apr 05;277(14):12388-95","abstract":"Intracellular molecular targets of novel berberine derivatives, HWY 289 and HWY 336, were identified by a screen of a variety of mutants in fission yeast Schizosaccharomyces pombe. HWY 289 and HWY 336 completely inhibited the proliferation of wild type as well as various mutant fission yeast cells (minimal inhibitory concentrations were 29.52 microm for HWY 289 and 11.83 microm for HWY 336), but did not affect the proliferation of Wis1 mitogen-activated protein kinase kinase (MAPKK) deletion mutants. In addition, HWY 289 with an IC(50) value of 7.3 microm or HWY 336 with IC(50) of 5.7 microm specifically inhibited in vitro kinase activities of purified Wis1, whereas either compound did not affect the activities of other kinases in the mitogen-activated protein kinase (MAPK) cascades of fission yeast. These genetic and biochemical results demonstrate the high degree of specificity of HWY 289 and HWY 336 to MAPKK Wis1 and suggest that the cytotoxicity of these compounds is not simply due to the inhibition of Wis1 kinase activity. High salt wash experiments have shown that strong noncovalent binding occurs between Wis1 and either HWY 289 or HWY 336. The preincubation of Wis1 kinase with ATP did not affect the inhibition of Wis1 by HWY 289 and HWY 336, but when Wis1 was preincubated with MBP, a protein substrate, Wis1 kinase activity was no longer inhibited. These observations demonstrate that HWY 289/HWY 336 do inhibit Wis1 kinase, not by binding to the ATP-binding site but by disturbing the binding of substrate to the kinase. Target validation of the complex of HWY 289/HWY 336 and Wis1 kinase will provide important clues for the mechanism of specific cytotoxicity of these compounds in S. pombe. On a broader aspect, it would create an initiative to further modify and develop compounds that selectively inhibit kinases and cause cytotoxicity in various MAPK cascades including those of mammals.","authors":"Jang MJ, Jwa M, Kim JH, Song K","authors_abbrev":"Jang MJ et al.","pubmed_publication_date":"05 Apr 2002","pubmed_entrez_date":"2001-12-18","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16397764","title":"Evaluation of image processing programs for accurate measurement of budding and fission yeast morphology.","citation":"Curr Genet 2006 Apr;49(4):237-47","abstract":"To study the cellular functions of gene products, various yeast morphological mutants have been investigated. To describe yeast morphology objectively, we have developed image processing programs for budding and fission yeast. The programs, named CalMorph for budding yeast and F-CalMorph for fission yeast, directly process microscopic images and generate quantitative data about yeast cell shape, nuclear shape and location, and actin distribution. Using CalMorph, we can easily and quickly obtain various quantitative data reproducibly. To study the utility and reliability of CalMorph, we evaluated its data in three ways: (1) The programs extracted three-dimensional bud information from two-dimensional digital images with a low error rate (<1%). (2) The absolute values of the diameters of manufactured fluorescent beads calculated with CalMorph were very close to those given in the manufacturer's data sheet. (3) The programs generated reproducible data consistent with that obtained by hand. Based on these results, we determined that CalMorph could monitor yeast morphological changes accompanied by the progression of the cell cycle. We discuss the potential of the CalMorph series as a novel tool for the analysis of yeast cell morphology.","authors":"Suzuki G, Sawai H, Ohtani M, Nogami S, Sano-Kumagai F, Saka A, Yukawa M, Saito TL, Sese J, Hirata D, Morishita S, Ohya Y","authors_abbrev":"Suzuki G et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-01-07","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009389","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9716495","title":"Isolation and characterization of a processive DNA helicase from the fission yeast Schizosaccharomyces pombe that translocates in a 5'-to-3' direction.","citation":"Biochem J 1998 Sep 01;334 ( Pt 2)(Pt 2):377-86","abstract":"We report here the isolation and characterization of a novel DNA helicase from extracts of the fission yeast Schizosaccharomyces pombe. The enzyme, called DNA helicase II, also contains an intrinsic DNA-dependent ATPase activity. Both the helicase and ATPase activities co-purified with a 63 kDa polypeptide on an SDS/polyacrylamide gel. The protein has a sedimentation coefficient of 4.8 S and a Stokes radius of 36 A (3.6 nm); from these data the native molecular mass was calculated to be 65 kDa. The enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. Unwinding reactions carried out in the presence of increasing enzyme showed a sigmoidal curve, suggesting either co-operative interactions between monomers or multimerization of DNA helicase II in the presence of single-stranded DNA and/or ATP. This enzyme favoured adenosine nucleotides (ATP and dATP) as its energy source, but utilized to limited extents GTP, CTP, dGTP and dCTP. Non-hydrolysable ATP analogues did not support helicase activity. Kinetic analyses showed that the unwinding reaction was rapid, being complete after 50-100 s of incubation. Addition of unlabelled substrates to the helicase reaction after preincubation of the enzyme with substrate did not significantly diminish unwinding. The ATPase activity of DNA helicase II increased proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continued to increase up to the longest time tested (3 h), whereas it ceased to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time was not affected by DNA species used. These data indicate that the enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive.","authors":"Lee C, Seo YS","authors_abbrev":"Lee C et al.","pubmed_publication_date":"01 Sep 1998","pubmed_entrez_date":"1998-08-26","publication_year":"1998","canto_session_key":"10c49151c9ba3e55","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-06-12 07:44:05","canto_approved_date":"2018-06-12 07:44:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 07:44:00","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC70.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2018-06-12"},{"uniquename":"PMID:28223353","title":"Sap1 is a replication-initiation factor essential for the assembly of pre-replicative complex in the fission yeast  Schizosaccharomyces pombe .","citation":"J Biol Chem 2017 Apr 14;292(15):6056-6075","abstract":"A central step in the initiation of chromosomal DNA replication in eukaryotes is the assembly of pre-replicative complex (pre-RC) at late M and early G 1  phase of the cell cycles. Since 1973, four proteins or protein complexes, including cell division control protein 6 (Cdc6)/Cdc18, minichromosome maintenance protein complex, origin recognition complex (ORC), and Cdt1, are known components of the pre-RC. Previously, we reported that a non-ORC protein binds to the essential element Δ9 of the  Schizosaccharomyces pombe  DNA-replication origin ARS3001. In this study, we identified that the non-ORC protein is Sap1. Like ORC, Sap1 binds to DNA origins during cell growth cycles. But unlike ORC, which binds to asymmetric AT-rich sequences through its nine AT-hook motifs, Sap1 preferentially binds to a DNA sequence of 5'-(A/T)   n   (C/G)(A/T) 9-10 (G/C)(A/T)   n   -3' ( n  ≥ 1). We also found that Sap1 and ORC physically interact. We further demonstrated that Sap1 is required for the assembly of the pre-RC because of its essential role in recruiting Cdc18 to DNA origins. Thus, we conclude that Sap1 is a replication-initiation factor that directly participates in the assembly of the pre-RC. DNA-replication origins in fission yeast are defined by possessing two essential elements with one bound by ORC and the other by Sap1.","doi":"10.1074/jbc.M116.767806","authors":"Guan L, He P, Yang F, Zhang Y, Hu Y, Ding J, Hua Y, Zhang Y, Ye Q, Hu J, Wang T, Jin C, Kong D","authors_abbrev":"Guan L et al.","pubmed_publication_date":"14 Apr 2017","pubmed_entrez_date":"2017-02-23","publication_year":"2017","canto_session_key":"46c22e1bcb30ae0a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-24 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1672.02c","SPBC14C8.07c"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"5jdk","gene_chains":[{"gene_uniquename":"SPCC1672.02c","chain":"A","position":"1-135"}],"title":"Crystal structure of the DNA binding domain of Sap1 in fission yeast S.pombe","entry_authors":"He P,Wang T","entry_authors_abbrev":"He P et al.","reference_uniquename":"PMID:28223353","experimental_method":"X-ray","resolution":"0.998"},{"pdb_id":"5b7j","gene_chains":[{"gene_uniquename":"SPCC1672.02c","chain":"A","position":"25-135"}],"title":"Structure model of Sap1-DNA complex","entry_authors":"Jin C,Hu Y,Ding J,Zhang Y","entry_authors_abbrev":"Jin C et al.","reference_uniquename":"PMID:28223353","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:18809570","title":"Balance between distinct HP1 family proteins controls heterochromatin assembly in fission yeast.","citation":"Mol Cell Biol 2008 Dec;28(23):6973-88","abstract":"Heterochromatin protein 1 (HP1) is a conserved chromosomal protein with important roles in chromatin packaging and gene silencing. In fission yeast, two HP1 family proteins, Swi6 and Chp2, are involved in transcriptional silencing at heterochromatic regions, but how they function and whether they act cooperatively or differentially in heterochromatin assembly remain elusive. Here, we show that both Swi6 and Chp2 are required for the assembly of fully repressive heterochromatin, in which they play distinct, nonoverlapping roles. Swi6 is expressed abundantly and plays a dose-dependent role in forming a repressive structure through its self-association property. In contrast, Chp2, expressed at a lower level, does not show a simple dose-dependent repressive activity. However, it contributes to the recruitment of chromatin-modulating factors Clr3 and Epe1 and possesses a novel ability to bind the chromatin-enriched nuclear subfraction that is closely linked with its silencing function. Finally, we demonstrate that a proper balance between Swi6 and Chp2 is critical for heterochromatin assembly. Our findings provide novel insight into the distinct and cooperative functions of multiple HP1 family proteins in the formation of higher-order chromatin structure.","doi":"10.1128/MCB.00791-08","authors":"Sadaie M, Kawaguchi R, Ohtani Y, Arisaka F, Tanaka K, Shirahige K, Nakayama J","authors_abbrev":"Sadaie M et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-09-24","publication_year":"2008","canto_session_key":"699531ab309cc4ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-07 16:27:44","canto_approved_date":"2024-05-17 11:36:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-02 09:06:52","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":59,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPBC800.03","SPBC428.08c","SPBC16C6.10","SPCC622.16c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2024-05-07"},{"uniquename":"PMID:3214489","title":"Peptide elongation factor 1 from yeasts: purification and biochemical characterization of peptide elongation factors 1 alpha and 1 beta (gamma) from Saccharomyces carlsbergensis and Schizosaccharomyces pombe.","citation":"J Biochem 1988 Mar;103(3):508-21","abstract":"Cytoplasmic elongation factor 1 alpha (EF-1 alpha) [corrected] was purified to homogeneity in high yield from the two different yeasts Saccharomyces carlsbergensis (S. carls.) and Schizosaccharomyces pombe (S. pombe). The purification was easily achieved by CM-Sephadex column chromatography of the breakthrough fractions from DEAE-Sephadex chromatography of cell-free extracts. The basic proteins have a molecular weight of 47,000 for the S. carls. factor and of 49,000 for the S. pombe factor. While the purified yeast EF-1 alpha s function analogously to other eukaryotic factors and the E. coli EF-Tu in Phe-tRNA binding and polyphenylalanine synthesis, the yeast factor unusually hydrolyzed GTP on yeast ribosomes upon addition of Phe-tRNA in the absence of poly(U) as mRNA. This novelty is probably owing to the yeast ribosomes, which are assumed to lack elongation factor 3-equivalent component(s). Trypsin and chymotrypsin selectively cleaved the two yeast factors to generate resistant fragments with the same molecular weight of 43,000 (by trypsin) and of 44,000 (by chymotrypsin), respectively. Those cleavage sites were characteristically protected by the presence of several ligands bound to EF-1 alpha such as GDP, GTP, and aminoacyl-tRNA. Based on the sequence analysis of the fragments generated by the two proteases, the partial amino acid sequence of the S. carls. EF-1 alpha was deduced to be in accordance with the N-terminal region covering positions (1) to 94 and two Lys residues at the C-terminal end of the predicted total sequence of the Saccharomyces cerevisiae (S. cerev.) factor derived from DNA analysis, except for a few N-terminal residues, confirming the predicted S. cerev. sequence at the protein level. EF-1 beta and EF-1 beta gamma were isolated and highly purified as biologically active entities from the two yeasts. EF-1 beta s from the two yeasts have the same molecular weight of 27,000, whereas component gamma of the S. carls. EF-1 beta gamma showed a higher molecular weight (47,000) than that of the S. pombe factor (40,000). It was also shown that a stoichiometric complex was formed between EF-1 alpha and EF-1 beta gamma from S. pombe. Furthermore, a considerable amount of Phe-tRNA binding activity was distributed in the EF-1H (probably EF-1 alpha beta gamma) fraction from freshly prepared cell-free extracts of yeast.","authors":"Miyazaki M, Uritani M, Fujimura K, Yamakatsu H, Kageyama T, Takahashi K","authors_abbrev":"Miyazaki M et al.","pubmed_publication_date":"Mar 1988","pubmed_entrez_date":"1988-03-01","publication_year":"1988","canto_session_key":"382d70dc36fdd8a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-09-24 15:30:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 15:30:13","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23A1.10","SPCC794.09c","SPBC839.15c","SPAC29A4.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2013-09-24"},{"uniquename":"PMID:39358553","title":"Ageing-associated long non-coding RNA extends lifespan and reduces translation in non-dividing cells.","citation":"EMBO Rep 2024 Oct 02;","abstract":"Genomes produce widespread long non-coding RNAs (lncRNAs) of largely unknown functions. We characterize aal1 (ageing-associated lncRNA), which is induced in quiescent fission yeast cells. Deletion of aal1 shortens the chronological lifespan of non-dividing cells, while ectopic overexpression prolongs their lifespan, indicating that aal1 acts in trans. Overexpression of aal1 represses ribosomal-protein gene expression and inhibits cell growth, and aal1 genetically interacts with coding genes functioning in protein translation. The aal1 lncRNA localizes to the cytoplasm and associates with ribosomes. Notably, aal1 overexpression decreases the cellular ribosome content and inhibits protein translation. The aal1 lncRNA binds to the rpl1901 mRNA, encoding a ribosomal protein. The rpl1901 levels are reduced ~2-fold by aal1, which is sufficient to extend lifespan. Remarkably, the expression of the aal1 lncRNA in Drosophila boosts fly lifespan. We propose that aal1 reduces the ribosome content by decreasing Rpl1901 levels, thus attenuating the translational capacity and promoting longevity. Although aal1 is not conserved, its effect in flies suggests that animals feature related mechanisms that modulate ageing, based on the conserved translational machinery.","doi":"10.1038/s44319-024-00265-9","authors":"Anver S, Sumit AF, Sun XM, Hatimy A, Thalassinos K, Marguerat S, Alic N, Bähler J","authors_abbrev":"Anver S et al.","pubmed_publication_date":"02 Oct 2024","pubmed_entrez_date":"2024-10-02","publication_year":"2024","canto_session_key":"8cfa36fcddaa98fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jurg Bahler","canto_first_approved_date":"2024-11-13 09:28:25","canto_approved_date":"2025-03-03 16:32:53","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-10-27 11:54:19","canto_added_date":"2024-10-03 23:25:04","annotation_curators":[{"name":"Jurg Bahler","community_curator":true,"annotation_count":6,"orcid":"0000-0003-4036-1532","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":88,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1020.06c","SPAC1F7.13c","SPBC8D2.18c","SPAC12G12.13c","SPBC11C11.07","SPAC1006.07","SPBC18H10.13","SPBC337.08c","SPAC9G1.03c","SPAC637.03","SPBC56F2.12","SPAC1556.02c","SPCC1450.13c","SPAC11E3.15","SPAC3A11.07","SPAC1F3.01","SPAC23C11.06c","SPAC589.10c","SPBC16H5.02","SPBC1703.13c","SPAC13G6.02c","SPAC22H12.04c","SPAC26F1.06","SPBC31A8.01c","SPCC13B11.01","SPCP31B10.07","SPAC6C3.04","SPAC17A5.14","SPBC800.14c","SPAC1071.10c","SPBC839.04","SPAC144.11","SPNCRNA.1530","SPAC1783.08c","SPBC56F2.02","SPAC24C9.12c","SPCC576.08c","SPBC26H8.10","SPAC3H5.05c","SPAC11G7.04","SPAC926.04c","SPBC14F5.05c","SPCC1259.01c","SPAC31G5.03","SPAC6G10.11c","SPAC9E9.09c","SPAPB17E12.13","SPBC1539.04","SPCC188.13c","SPAC3G9.11c","SPAC4H3.10c","SPBC1711.13","SPAC140.01","SPBC215.05","SPBC19C2.07","SPCC1682.01","SPCC576.11","SPAC750.08c","SPAC824.07","SPCC794.12c","SPAC6B12.15","SPBC16E9.12c","SPBC16D10.11c","SPAC227.18","SPBC16D10.08c","SPBC660.16","SPCC330.06c","SPBC16G5.14c","SPAC1805.12c","SPBC12C2.04","SPBC2F12.07c","SPAC4A8.15c","SPCC1393.12","SPBC428.02c","SPBC32H8.12c","SPAC6F12.09","SPBC1289.03c","SPCC736.11"],"gene_count":78,"ltp_gene_count":78,"approved_date":"2024-11-13"},{"uniquename":"PMID:18931302","title":"Significant conservation of synthetic lethal genetic interaction networks between distantly related eukaryotes.","citation":"Proc Natl Acad Sci U S A 2008 Oct 28;105(43):16653-8","abstract":"Synthetic lethal genetic interaction networks define genes that work together to control essential functions and have been studied extensively in Saccharomyces cerevisiae using the synthetic genetic array (SGA) analysis technique (ScSGA). The extent to which synthetic lethal or other genetic interaction networks are conserved between species remains uncertain. To address this question, we compared literature-curated and experimentally derived genetic interaction networks for two distantly related yeasts, Schizosaccharomyces pombe and S. cerevisiae. We find that 23% of interactions in a novel, high-quality S. pombe literature-curated network are conserved in the existing S. cerevisiae network. Next, we developed a method, called S. pombe SGA analysis (SpSGA), enabling rapid, high-throughput isolation of genetic interactions in this species. Direct comparison by SpSGA and ScSGA of approximately 220 genes involved in DNA replication, the DNA damage response, chromatin remodeling, intracellular transport, and other processes revealed that approximately 29% of genetic interactions are common to both species, with the remainder exhibiting unique, species-specific patterns of genetic connectivity. We define a conserved yeast network (CYN) composed of 106 genes and 144 interactions and suggest that this network may help understand the shared biology of diverse eukaryotic species.","doi":"10.1073/pnas.0806261105","authors":"Dixon SJ, Fedyshyn Y, Koh JL, Prasad TS, Chahwan C, Chua G, Toufighi K, Baryshnikova A, Hayles J, Hoe KL, Kim DU, Park HO, Myers CL, Pandey A, Durocher D, Andrews BJ, Boone C","authors_abbrev":"Dixon SJ et al.","pubmed_publication_date":"28 Oct 2008","pubmed_entrez_date":"2008-10-22","publication_year":"2008","canto_session_key":"8fb2a52d2c99b03e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-23 17:42:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-23 17:21:00","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC328.01c","SPCC1223.06","SPAC25G10.02","SPAC1805.15c","SPAC11E3.08c","SPAC637.06","SPCC306.04c","SPBC19G7.01c","SPAC24H6.13","SPBC30D10.04","SPAC664.01c","SPAC1687.13c","SPCC24B10.13","SPBC2G5.03","SPBC1703.14c","SPBC1604.20c","SPBC887.10","SPBC1685.15c","SPBC16D10.07c","SPAC3H8.07c","SPAC694.06c","SPBC106.01","SPAC19D5.01","SPAC16C9.06c","SPCC11E10.03","SPBC1861.03","SPBP8B7.21","SPCC11E10.08","SPAC4H3.05","SPCC576.13","SPBC342.05","SPAC1834.07","SPAC20H4.07","SPBC16E9.11c","SPAC1142.08","SPCC285.16c","SPAC13G6.01c","SPAC1F3.02c","SPAC17G6.17","SPAC3G6.06c","SPBC530.01","SPAPB1A10.09","SPBC336.14c","SPAC631.01c","SPAC24H6.03","SPBC23G7.04c","SPCC1259.13","SPAC1F5.09c","SPAC4C5.02c","SPCC895.05","SPAC12B10.15c","SPBC1778.02","SPBC31E1.02c","SPAC27D7.13c","SPAC144.14","SPBC887.04c","SPCC338.16","SPBC2G2.02","SPBC31F10.13c","SPCC18B5.11c","SPBC20F10.06","SPAC29E6.01","SPBC15D4.06","SPAC19E9.02","SPAC29A4.20","SPBC28F2.10c","SPBC215.02","SPBC216.05","SPAC17G8.10c","SPBC29A10.05","SPAC3G9.05","SPAC3A11.13","SPBC3H7.14","SPBC713.11c","SPBC800.03","SPBC28F2.11","SPAC17H9.10c","SPCC126.04c","SPAC1805.07c","SPCC594.05c","SPBC13E7.08c","SPCP31B10.05","SPBC119.12","SPBC1734.06","SPAC1687.05","SPAC19A8.10","SPCC1827.08c","SPBC3H7.06c","SPAC1002.03c","SPAC926.07c","SPAC6F6.02c","SPAC2F7.04","SPAC16A10.05c","SPAC12B10.12c","SPBC336.03","SPAC6B12.02c","SPAC3H1.05","SPAC2G11.05c","SPBC1703.06","SPAPJ696.01c","SPAC12B10.07","SPBC337.03","SPAC8F11.03","SPAC26F1.10c","SPCC1840.04","SPBC342.01c","SPBC336.01","SPAC17A2.13c","SPBC725.09c","SPAC1952.12c","SPBC1347.08c","SPAC3G9.07c","SPAC20G4.04c","SPAC14C4.13","SPBC15D4.03","SPAC343.18","SPAC18G6.15","SPBC36.07","SPBC11B10.10c","SPBC365.06","SPBC1709.11c","SPAC1B3.03c","SPAC23G3.12c","SPCC188.13c","SPAC15A10.16","SPAC1D4.03c","SPAC9E9.08","SPBC649.03","SPBC651.10","SPAC31A2.15c","SPBC1105.14","SPAPYUG7.04c","SPCC4F11.04c","SPAC11E3.01c","SPAC1F5.08c","SPAC17H9.03c","SPBC4F6.15c","SPAC23C11.04c","SPBC337.16","SPBC1734.15","SPBC25H2.03","SPAC13G7.03","SPCC132.02","SPCC23B6.03c","SPAC823.05c","SPBP35G2.13c","SPAC521.02","SPAC227.10","SPAC227.05","SPBC3D6.04c","SPAC23C4.02","SPBC13G1.08c","SPAC22F3.09c","SPAC1782.09c","SPCC4B3.12","SPBC543.03c","SPAC664.07c","SPAC3C7.09","SPBC27.02c","SPCC1223.04c","SPAC30C2.02","SPAC3G6.11","SPBC19C7.10","SPCC16C4.11","SPAC6G10.02c","SPBC3E7.08c","SPAC17A2.06c","SPAC6B12.05c","SPAC17C9.05c","SPBC215.03c","SPBC902.02c","SPAC11E3.09","SPAC9G1.06c"],"gene_count":173,"ltp_gene_count":0,"approved_date":"2016-02-23"},{"uniquename":"PMID:28334931","title":"Rgf1p (Rho1p GEF) is required for double-strand break repair in fission yeast.","citation":"Nucleic Acids Res 2017 May 19;45(9):5269-5284","abstract":"Rho GTPases are conserved molecules that control cytoskeletal dynamics. These functions are expedited by Rho GEFs that stimulate the release of GDP to enable GTP binding, thereby allowing Rho proteins to initiate intracellular signaling. How Rho GEFs and Rho GTPases protect cells from DNA damage is unknown. Here, we explore the extreme sensitivity of a deletion mutation in the Rho1p exchange factor Rgf1p to the DNA break/inducing antibiotic phleomycin (Phl). The Rgf1p mutant cells are defective in reentry into the cell cycle following the induction of severe DNA damage. This phenotype correlates with the inability of rgf1Δ cells to efficiently repair fragmented chromosomes after Phl treatment. Consistent with this observation Rad11p (ssDNA binding protein, RPA), Rad52p, Rad54p and Rad51p, which facilitate strand invasion in the process of homology-directed repair (HDR), are permanently stacked in Phl-induced foci in rgf1Δ cells. These phenotypes are phenocopied by genetic inhibition of Rho1p. Our data provide evidence that Rgf1p/Rho1p activity positively controls a repair function that confers resistance against the anti-cancer drug Phl.","doi":"10.1093/nar/gkx176","authors":"Manjón E, Edreira T, Muñoz S, Sánchez Y","authors_abbrev":"Manjón E et al.","pubmed_publication_date":"19 May 2017","pubmed_entrez_date":"2017-03-24","publication_year":"2017","canto_session_key":"8d28a15d2b3f9ddc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-25 01:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.13c","SPAC30D11.10","SPAC15A10.03c","SPCC645.07","SPAC644.14c","SPCC1183.05c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:15341766","title":"SIN and the art of splitting the fission yeast cell.","citation":"Curr Biol 2004 Sep 07;14(17):R722-30","abstract":"The septation initiation network (SIN) triggers the onset of cytokinesis in the fission yeast Schizosaccharomyces pombe by promoting contraction of the medially placed F-actin ring. SIN signaling is regulated by the polo-like kinase plo1p and by cdc2p, the initiator of mitosis, and its activation is co-ordinated with other events in mitosis to ensure that cytokinesis does not begin until chromosomes have been separated. Though the SIN controls the contractile ring, the signal originates from the poles of the mitotic spindle. Recent studies suggest that the spindle pole body may act as a dynamic assembly site for active SIN signaling complexes. In the budding yeast Saccharomyces cerevisiae the counterpart of the SIN, called the MEN, mediates both mitotic exit and cytokinesis, in part through regulating activation of the phosphoprotein phosphatase Cdc14p. Flp1p, the S. pombe ortholog of Cdc14p, is not essential for mitotic exit, but may contribute to an orderly mitosis-G1 transition by regulating the destruction of the mitotic inducer cdc25p.","authors":"Krapp A, Gulli MP, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"07 Sep 2004","pubmed_entrez_date":"2004-09-03","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21182284","title":"Survey of the phosphorylation status of the Schizosaccharomyces pombe deubiquitinating enzyme (DUB) family.","citation":"J Proteome Res 2011 Mar 04;10(3):1208-15","abstract":"Ubiquitination plays a role in virtually every cellular signaling pathway ranging from cell cycle control to DNA damage response to endocytosis and gene regulation. The bulk of our knowledge of the ubiquitination system is centered on modification of specific substrate proteins and the enzymatic cascade of ubiquitination. Our understanding of the regulation of the reversal of these modifications (deubiquitination) lags significantly behind. We recently reported a multifaceted study of the fission yeast Schizosaccharomyces pombe DUBs including characterization of their binding partners, in vitro enzymatic activity and subcellular localization. (1) Over half of the 20 fission yeast DUBs have a stable protein partner and some of those partners regulate the localization and/or activity of their cognate DUB. As a next step in understanding how DUBs might otherwise be regulated, we investigated the phosphostatus of the entire fission yeast DUB family using LC-MS/MS, and here we discuss the possible implications of phosphoregulation.","doi":"10.1021/pr100985s","authors":"McLean JR, Kouranti I, Gould KL","authors_abbrev":"McLean JR et al.","pubmed_publication_date":"04 Mar 2011","pubmed_entrez_date":"2010-12-25","publication_year":"2011","canto_session_key":"767451d8f8ef6abe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Janel McLean","canto_approved_date":"2014-07-28 12:55:09","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-21 16:16:36","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Janel McLean","community_curator":true,"annotation_count":116,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC713.02c","SPBP8B7.21","SPBC17D11.07c","SPAC17A5.16","SPBC342.04","SPBC6B1.06c","SPBP19A11.03c","SPBC1703.12","SPBC18H10.08c","SPAC31A2.14","SPAC6G9.08","SPAC23G3.08c","SPAC12B10.03","SPCC1494.05c","SPBP8B7.11","SPCC188.08c","SPAC3F10.13","SPAC31G5.13","SPAC19B12.10","SPAC328.06","SPAC7D4.02c"],"gene_count":21,"ltp_gene_count":21,"approved_date":"2014-07-21"},{"uniquename":"PMID:9642054","title":"Two large subunits of the fission yeast RNA polymerase II provide platforms for the assembly of small subunits.","citation":"J Mol Biol 1998 Jun 19;279(4):703-12","abstract":"The subunit-subunit contact network was analyzed for the Schizosaccharomyces pombe RNA polymerase II consisting of ten putative subunits. Previously we carried out far-Western blot analysis of bimolecular interaction with radio-labeled subunit 3 and 5 probes. Here we extended the analysis using another six small-sized subunits as probes. Taking the results together the subunit-subunit interaction was observed for a total 18 (or 19) combinations. All eight small-sized subunits exhibited binding activities to two large subunits, Rpb1 and Rpb2. In addition, bimolecular interaction was observed for the combinations of Rpb3-Rpb5, Rpb3-Rpb11 (and Rpb5-Rpb8/11). The subunit-subunit contact within the assembled RNA polymerase was then analyzed by protein-protein cross-linking using five species of bifunctional cross-linkers with different length and specificity. Cross-linking was observed for a total of 19 combinations, including five combinations between small subunits, Rpb3-Rpb10, Rpb3-Rpb11, Rpb5-Rpb6, Rpb6-Rpb7 and Rpb6-Rpb8. The results altogether indicate that two large subunits Rpb1 and Rpb2 provide the platform for assembly of small subunits and also small subunits interact with each other for limited combinations. Direct contact of the two large subunits, Rpb1 and Rpb2, was also demonstrated by cross-linking.","authors":"Ishiguro A, Kimura M, Yasui K, Iwata A, Ueda S, Ishihama A","authors_abbrev":"Ishiguro A et al.","pubmed_publication_date":"19 Jun 1998","pubmed_entrez_date":"1998-06-27","publication_year":"1998","canto_session_key":"c39fb6fd2b416713","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-12 08:17:16","canto_approved_date":"2023-12-10 10:39:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 08:17:09","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPAC23C4.15","SPAC3A12.07","SPAC1B3.12c","SPCC1442.10c","SPBC14C8.12","SPCC1020.04c","SPAC23G3.01","SPACUNK4.06c","SPBC19C2.03"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2018-06-12"},{"uniquename":"PMID:28148851","title":"Preparation of Protein Extracts from Schizosaccharomyces pombe Using Trichloroacetic Acid Precipitation.","citation":"Cold Spring Harb Protoc 2017 Feb 01;2017(2)","abstract":"Schizosaccharomyces pombe is an attractive model organism with which to study core principles of conserved molecular cell biology processes. The ability to monitor protein behavior following separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) underpins much of this activity. Here we describe a robust protocol for the preparation of protein samples for analysis by SDS-PAGE.","doi":"10.1101/pdb.prot091579","authors":"Grallert A, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"01 Feb 2017","pubmed_entrez_date":"2017-02-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-02-04 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41354344","title":"The mitotic functions of a fission yeast CK1 enzyme are regulated by Cdk1-dependent and auto-phosphorylation.","citation":"J Biol Chem 2025 Dec 05;:111007","abstract":"CK1 enzymes are conserved regulators of diverse cellular processes. In Schizosaccharomyces pombe, the CK1 orthologs of CK1δ and CK1ε, Hhp1 and Hhp2, are required for a mitotic checkpoint that delays cytokinesis when the mitotic spindle is disrupted. Here, we show that Hhp2, but not Hhp1, undergoes transient hyperphosphorylation during mitosis. Hhp2 autophosphorylates at four residues and is phosphorylated by the cyclin-dependent kinase Cdk1 at three additional sites. Functionally, these phosphorylation events inhibit Hhp2 catalytic activity, as phospho-ablating mutants exhibited enhanced in vitro kinase activity. In vivo, a mutant combining all seven sites (hhp2-7A) behaved as a gain-of-function mutant in the mitotic checkpoint and also had the unexpected phenotype of accelerating mitosis and cytokinesis in unperturbed conditions. Further genetic analyses indicated that Hhp2 likely promotes mitotic progression in parallel with the Polo-like kinase, Plo1. These findings establish that mitotic phosphorylation of Hhp2 serves as a negative regulatory mechanism that silences checkpoint activity and modulates cell cycle timing. Because mitotic phosphorylation of human CK1δ has been observed, our results suggest that Cdk1-mediated inhibition of CK1 enzymes is a conserved mechanism coupling the core cell cycle control machinery to CK1-dependent signaling pathways.","doi":"10.1016/j.jbc.2025.111007","authors":"Akizuki K, Cullati SN, Johnson AE, Chen JS, Willet AH, Gould KL","authors_abbrev":"Akizuki K et al.","pubmed_publication_date":"05 Dec 2025","pubmed_entrez_date":"2025-12-07","publication_year":"2025","canto_session_key":"b1e5b33f093ba019","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2026-02-24 18:53:20","canto_approved_date":"2026-03-06 13:04:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-02-23 19:45:58","canto_added_date":"2025-12-09 00:25:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":19,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC23C11.16","SPBC26H8.07c","SPBC3H7.15","SPAC23C4.12"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2026-02-24"},{"uniquename":"PMID:26776736","title":"Nutritional Control of Cell Size by the Greatwall-Endosulfine-PP2A·B55 Pathway.","citation":"Curr Biol 2016 Feb 08;26(3):319-30","abstract":"Proliferating cells adjust their cell size depending on the nutritional environment. Cells are large in rich media and small in poor media. This physiological response has been demonstrated in both unicellular and multicellular organisms. Here we show that the greatwall-endosulfine (Ppk18-Igo1 in fission yeast) pathway couples the nutritional environment to the cell-cycle machinery by regulating the activity of PP2A·B55. In the presence of nutrients, greatwall (Ppk18) protein kinase is inhibited by TORC1 and PP2A·B55 is active. High levels of PP2A·B55 prevent the activation of mitotic Cdk1·Cyclin B, and cells increase in size in G2 before they undergo mitosis. When nutrients are limiting, TORC1 activity falls off, and the activation of greatwall (Ppk18) leads to the phosphorylation of endosulfine (Igo1) and inhibition of PP2A·B55, which in turn allows full activation of Cdk1·CyclinB and entry into mitosis with a smaller cell size. Given the conservation of this pathway, it is reasonable to assume that this mechanism operates in higher eukaryotes, as well.","doi":"10.1016/j.cub.2015.12.035","authors":"Chica N, Rozalén AE, Pérez-Hidalgo L, Rubio A, Novak B, Moreno S","authors_abbrev":"Chica N et al.","pubmed_publication_date":"08 Feb 2016","pubmed_entrez_date":"2016-01-19","publication_year":"2016","canto_session_key":"5beca4251520f38b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-29 16:05:19","canto_approved_date":"2025-09-04 06:30:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-30 17:09:11","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":63,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.06c","SPAC227.07c","SPAPB1E7.12","SPBC16H5.07c","SPAC24B11.06c","SPCC18B5.03","SPAPB18E9.02c","SPAC1B9.02c","SPAC22E12.14c","SPAC2F7.03c","SPAC823.15","SPBC216.07c","SPAC24H6.05","SPAC644.06c","SPAC19D5.01","SPCC1450.11c","SPCC4G3.08","SPAC10F6.16","HGNC:19042"],"gene_count":18,"ltp_gene_count":15,"approved_date":"2018-03-29"},{"uniquename":"PMID:8598285","title":"Rum1 and Cdc18 link inhibition of cyclin-dependent kinase to the initiation of DNA replication in Schizosaccharomyces pombe.","citation":"Genes Dev 1996 Mar 01;10(5):541-52","abstract":"Eukaryotic cells have evolved regulatory mechanisms to ensure the strict alternation of DNA replication and mitosis. Recent work has suggested that the mitotic form of cyclin-dependent kinase (Cdc2/cyclin B) has a role in preventing re-replication of the genome before mitosis, but the relevant targets of this inhibition are unknown. In this report we present evidence that the mitotic cyclin-dependent kinase affects DNA replication by inhibiting the accumulation and function of Cdc18, a critical regulator of S-phase entry. We found that the ruml+ gene efficiently suppresses the lethality of a conditional cdc18 mutant. Conversely, deletion of ruml+ increases the severity of the cdc18 mutant phenotype, resulting in inappropriate cell division and a rapid loss of viability. Biochemical experiments indicate that Ruml potently inhibits Cdc2 phosphorylation of histone H1 or a Cdc18 fusion protein by directly interacting with the Cdc2/cyclin B complex. Overexpression of Ruml under conditions that promote re-replication of the genome induces a striking accumulation of Cdc18 protein by a largely post-transcriptional mechanism. Overexpression of SIC1, an unrelated cyclin-dependent kinase inhibitor from budding yeast, causes a similar accumulation of Cdc18 and also leads to re-replication. Our data link a potent inhibitor of Cdc2 kinase to a key protein required for the initiation of DNA replication and strongly suggest that inhibition of Cdc18 by cyclin-dependent kinases has an important role in ensuring that the genome is duplicated precisely once each cell cycle.","authors":"Jallepalli PV, Kelly TJ","authors_abbrev":"Jallepalli PV et al.","pubmed_publication_date":"01 Mar 1996","pubmed_entrez_date":"1996-03-01","publication_year":"1996","canto_session_key":"ff086b28d1132e67","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-05-09 07:04:42","canto_approved_date":"2022-08-31 15:23:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-28 14:04:52","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.09","SPBC582.03","SPBC14C8.07c","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-05-09"},{"uniquename":"PMID:23604080","title":"HDAC-mediated suppression of histone turnover promotes epigenetic stability of heterochromatin.","citation":"Nat Struct Mol Biol 2013 May;20(5):547-54","abstract":"Heterochromatin causes epigenetic repression that can be transmitted through multiple cell divisions. However, the mechanisms underlying silencing and stability of heterochromatin are not fully understood. We show that heterochromatin differs from euchromatin in histone turnover and identify histone deacetylase (HDAC) Clr3 as a factor required for inhibiting histone turnover across heterochromatin domains in Schizosaccharomyces pombe. Loss of RNA-interference factors, Clr4 methyltransferase or HP1 proteins involved in HDAC localization causes increased histone turnover across pericentromeric domains. Clr3 also affects histone turnover at the silent mating-type region, where it can be recruited by alternative mechanisms acting in parallel to H3K9me-HP1. Notably, the JmjC-domain protein Epe1 promotes histone exchange, and loss of Epe1 suppresses both histone turnover and defects in heterochromatic silencing. Our results suggest that heterochromatic-silencing factors preclude histone turnover to promote silencing and inheritance of repressive chromatin.","doi":"10.1038/nsmb.2565","authors":"Aygün O, Mehta S, Grewal SI","authors_abbrev":"Aygün O et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-04-23","publication_year":"2013","canto_session_key":"6ebaf94fe498e8cc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.16c","SPCC736.11","SPBC16C6.10","SPAC664.01c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:15928091","title":"Dynamic positioning of the fission yeast cell division plane.","citation":"Proc Natl Acad Sci U S A 2005 Jun 07;102(23):8228-32","abstract":"A key question in cytokinesis is how the cell division plane is positioned. Whereas microtubules of the mitotic apparatus specify the division site in animal cells, we show here that the nucleus plays this role in the fission yeast Schizosaccharomyces pombe. By centrifuging cells to move the nucleus, we find that the nucleus (or a nuclear-associated structure) actively influences the position of contractile ring assembly during early mitosis. Displacement of the nucleus during this induction period can lead to formation of multiple rings. The nucleus signals its position in a microtubule-independent manner by emitting the protein mid1p. Furthermore, movement of ring fragments together minimizes formation of multiple division sites. These dynamic mechanisms of ring positioning provide a robust coordination of nuclear and cell division.","authors":"Daga RR, Chang F","authors_abbrev":"Daga RR et al.","pubmed_publication_date":"07 Jun 2005","pubmed_entrez_date":"2005-06-02","publication_year":"2005","canto_session_key":"5c0a56e1a090e57a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-19 14:03:49","canto_approved_date":"2022-09-19 14:03:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-19 14:03:42","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-09-19"},{"uniquename":"PMID:15507118","title":"An interactive gene network for securin-separase, condensin, cohesin, Dis1/Mtc1 and histones constructed by mass transformation.","citation":"Genes Cells 2004 Nov;9(11):1069-82","abstract":"The small genome of fission yeast Schizosaccharomyces pombe contains 4824 predicted genes and gene disruption suggests that approximately 850 are essential for viability. To obtain information on interactions among genes required for chromosome segregation, an approach called Strategy B was taken using mass transformation of the 1015 temperature-sensitive (ts) mutants that were made by random mutagenesis and transformed by plasmids carrying the genes for securin, separase, condensin, cohesin, kinetochore microtubule-binding proteins Dis1/Mtc1 or histones. Mutant strains whose phenotypes were either suppressed or inhibited by plasmids were selected. Each plasmid interacted positively or negatively with the average 14 strains. Identification of the mutant gene products by cloning revealed many hitherto unknown interactions. The interactive networks of segregation therefore may consist of genes with a variety of functions. For example, separase/Cut1 interacts with Cdc48/p97/VCP, which stabilizes securin and separase. Surprisingly, S. pombe cdc48 mutants displayed the mitotic phenotype highly similar to separase/cut1 mutants. This approach also provides a novel way of mutant isolation, resulting in two histone H2B strains and a cohesion mutant with a new phenotype.","authors":"Yuasa T, Hayashi T, Ikai N, Katayama T, Aoki K, Obara T, Toyoda Y, Maruyama T, Kitagawa D, Takahashi K, Nagao K, Nakaseko Y, Yanagida M","authors_abbrev":"Yuasa T et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-28","publication_year":"2004","canto_session_key":"6fa5a621a1388c10","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-05-04 08:24:42","canto_approved_date":"2025-09-04 09:56:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-07 16:37:15","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.07c","SPAC3H5.06c","SPBC12C2.02c","SPBC146.01","SPCC895.07","SPBC12C2.06","SPBC19G7.05c","SPAC1B2.05","SPAC24H6.12c","SPAC17A2.09c","SPAC17A2.13c","SPBC31E1.05","SPCC962.02c","SPBC106.09","SPBP4H10.06c","SPBC14C8.01c","SPBC211.04c","SPAC8E11.02c","SPBC1105.12","SPBC23G7.05","SPBC19G7.16","SPAC31A2.05c","SPCC736.14","SPBC646.13","SPBC16G5.12c","SPBC646.14c","SPBC14C8.07c","SPAC22H10.10","SPCC285.09c","SPBC1105.11c","SPBC21B10.05c","SPBC1A4.01","SPAC17C9.13c","SPAC23C11.12","SPAC6B12.10c","SPAC959.09c","SPBC409.05","SPAC1565.08","SPAC4F10.10c","SPCC5E4.04","SPBC4.04c","SPAC6F12.14","SPAC3G9.14","SPCC338.17c","SPBC146.03c","SPBC1709.05","SPAC19G12.01c","SPAC1F7.01c","SPBC29A10.04","SPAC17H9.20","SPAC6F12.15c"],"gene_count":51,"ltp_gene_count":51,"approved_date":"2018-05-04"},{"uniquename":"PMID:5312020","title":"The growth of Schizosaccharomyces pombe in media of high osmotic pressure.","citation":"Antonie Van Leeuwenhoek 1969 Jun;35:Suppl:H25-6","abstract":"","authors":"Duffus JH, Mitchell CJ","authors_abbrev":"Duffus JH et al.","pubmed_publication_date":"Jun 1969","pubmed_entrez_date":"1969-06-01","publication_year":"1969","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34890395","title":"3,3'-Diindolylmethane induces apoptosis and autophagy in fission yeast.","citation":"PLoS One 2021;16(12):e0255758","abstract":"3,3'-Diindolylmethane (DIM) is a compound derived from the digestion of indole-3-carbinol, found in the broccoli family. It induces apoptosis and autophagy in some types of human cancer. DIM extends lifespan in the fission yeast Schizosaccharomyces pombe. The mechanisms by which DIM induces apoptosis and autophagy in humans and expands lifespan in fission yeasts are not fully understood. Here, we show that DIM induces apoptosis and autophagy in log-phase cells, which is dose-dependent in fission yeast. A high concentration of DIM disrupted the nuclear envelope (NE) structure and induced chromosome condensation at an early time point. In contrast, a low concentration of DIM induced autophagy but did not disrupt NE structure. The mutant defective in autophagy was more sensitive to a low concentration of DIM, demonstrating that the autophagic pathway contributes to the survival of cells against DIM. Moreover, our results showed that the lem2 mutant is more sensitive to DIM. NE in the lem2 mutant was disrupted even at the low concentration of DIM. Our results demonstrate that the autophagic pathway and NE integrity are important to maintain viability in the presence of a low concentration of DIM. The mechanism of apoptosis and autophagy induction by DIM might be conserved in fission yeast and humans. Further studies will contribute to the understanding of the mechanism of apoptosis and autophagy by DIM in fission yeast and humans.","doi":"10.1371/journal.pone.0255758","authors":"Emami P, Ueno M","authors_abbrev":"Emami P et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-12-10","publication_year":"2021","canto_session_key":"282bad47ac13d105","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24449894","title":"CRL4-like Clr4 complex in Schizosaccharomyces pombe depends on an exposed surface of Dos1 for heterochromatin silencing.","citation":"Proc Natl Acad Sci U S A 2014 Feb 04;111(5):1795-800","abstract":"Repressive histone H3 lysine 9 methylation (H3K9me) and its recognition by HP1 proteins are necessary for pericentromeric heterochromatin formation. In Schizosaccharomyces pombe, H3K9me deposition depends on the RNAi pathway. Cryptic loci regulator 4 (Clr4), the only known H3K9 methyltransferase in this organism, is a subunit of the Clr4 methyltransferase complex (CLRC), whose composition is reminiscent of a CRL4 type cullin-RING ubiquitin ligase (CRL) including its cullin Cul4, the RING-box protein Pip1, the DNA damage binding protein 1 homolog Rik1, and the DCAF-like protein delocalization of Swi6 1 (Dos1). Dos2 and Stc1 have been proposed to be part of the complex but do not bear similarity to canonical ubiquitin ligase components. CLRC is an active E3 ligase in vitro, and this activity is necessary for heterochromatin assembly in vivo. The similarity between CLRC and the CRLs suggests that the WD repeat protein Dos1 will act to mediate target recognition and substrate specificity for CLRC. Here, we present a pairwise interaction screen that confirms a CRL4-like subunit arrangement and further identifies Dos2 as a central component of the complex and recruiter of Stc1. We determined the crystal structure of the Dos1 WD repeat domain, revealing an eight-bladed β-propeller fold. Functional mapping of the putative target-binding surface of Dos1 identifies key residues required for heterochromatic silencing, consistent with Dos1's role as the specificity factor for the E3 ubiquitin ligase.","doi":"10.1073/pnas.1313096111","authors":"Kuscu C, Zaratiegui M, Kim HS, Wah DA, Martienssen RA, Schalch T, Joshua-Tor L","authors_abbrev":"Kuscu C et al.","pubmed_publication_date":"04 Feb 2014","pubmed_entrez_date":"2014-01-23","publication_year":"2014","canto_session_key":"db2776491fc257ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2026-04-20 14:02:29","canto_approved_date":"2026-04-20 14:02:29","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-04-20 14:02:23","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":53,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.07c","SPCC11E10.08","SPAC3A11.08","SPCC613.12c","SPBC428.08c","SPAC23H4.18c","SPBP8B7.28c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2026-04-20","pdb_entries":[{"pdb_id":"4o9d","gene_chains":[{"gene_uniquename":"SPCC613.12c","chain":"A/B","position":"213-638"}],"title":"Structure of Dos1 propeller","entry_authors":"Kuscu C,Schalch T,Joshua-Tor L","entry_authors_abbrev":"Kuscu C et al.","reference_uniquename":"PMID:24449894","experimental_method":"X-ray","resolution":"2.0"}]},{"uniquename":"PMID:39527197","title":"Mapping Active RNA Polymerases in Proliferating and Quiescent Fission Yeast Cells Using Precision Run-On Sequencing.","citation":"Methods Mol Biol 2025;2862:121-139","abstract":"The development of next-generation sequencing (NGS) approaches to investigate the functioning of RNA polymerases has led to groundbreaking advances in the field of transcriptional regulation. One powerful method, Precision nuclear Run-On sequencing (PRO-seq), maps the locations of RNA polymerase active sites genome-wide at high resolution. PRO-seq provides a snapshot of strand-specific transcriptional activity and does not rely on immunoprecipitation of the polymerase of interest. Notably, this technique has been utilized to investigate the control of the RNA polymerase II transcription cycle in a variety of model systems. However, the initially published PRO-seq method required significant amounts of starting sample and was technically challenging, both of which were deterrents for its broader use. Recently, an improved and simplified version called qPRO-seq that reduced the length of the experiment and the quantity of necessary input sample was developed for human and Drosophila cell lines. Here we provide an updated, step-by-step protocol in which we have validated and optimized qPRO-seq for the fission yeast Schizosaccharomyces pombe. Importantly, we have implemented this method for assessing RNA polymerase activity in nutrient-limiting conditions, for both proliferating and nitrogen-depleted quiescent cells.","doi":"10.1007/978-1-0716-4168-2_9","authors":"Vázquez-Bolado A, Wu PJ","authors_abbrev":"Vázquez-Bolado A et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4291962","title":"Mutants partially deficient in alcohol dehydrogenase in Schizosaccharomyces pombe.","citation":"Arch Biochem Biophys 1967 Jul;121(1):194-201","abstract":"","authors":"Megnet R","authors_abbrev":"Megnet R","pubmed_publication_date":"Jul 1967","pubmed_entrez_date":"1967-07-01","publication_year":"1967","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30931102","title":"Oxidative stress-mediated apoptotic cell death induced by camphor in  sod1 -deficient  Schizosaccharomyces pombe .","citation":"Toxicol Res (Camb) 2019 Mar 01;8(2):216-226","abstract":"Camphor is one of the monoterpenes widely used in cosmetics, pharmaceutics and the food industry. In this study, we aimed to assess the oxidative, cytotoxic and apoptotic effects of camphor on the fission yeast ( Schizosaccharomyces pombe ), which is a promising unicellular model organism in mechanistic toxicology and cell biology. Since Sod1 is the main radical scavenger in the cell, we used  sod1  mutants to understand whether camphor-induced ROS accumulation caused higher cytotoxicity and apoptosis. Camphor exposure (0-2000 mg L -1 ) caused significant cytotoxicity in yeast, particularly in  sod1 Δ cells. DCFDA (2,7-dichlorodihydrofluorescein diacetate) fluorescence and NBT ( p -nitro-blue tetrazolium chloride) reduction increased (at least 2.5-3-fold in  sod1 Δ cells) in correlation with camphor concentrations (800-1200 mg L -1 ), showing higher ROS levels and oxidative stress. Moreover, cells, stained with acridine orange/ethidium bromide, showed an apoptotic morphology with nuclear fragmentation and condensation. DAPI (4',6-diamidino-2-phenylindole) staining was used to validate the apoptotic nuclear morphology. Dramatically increased mitochondrial impairment, which was higher in  sod1 Δ cells than in wild type cells, was shown by rhodamine 123 staining. In conclusion, camphor-induced excessive ROS production, which could not be prevented significantly in  sod1  mutants, caused a dramatic increase in mortality rates due to intrinsic apoptosis revealed by mitochondrial impairment and apoptotic nuclear morphology. The potential effects of camphor on apoptotic cell death and the underlying mechanisms were clarified in the unicellular eukaryotic model,  S. pombe .","doi":"10.1039/c8tx00279g","authors":"Agus HH, Sengoz CO, Yilmaz S","authors_abbrev":"Agus HH et al.","pubmed_publication_date":"01 Mar 2019","pubmed_entrez_date":"2019-04-02","publication_year":"2019","canto_session_key":"f59add46c7c1ea16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-21 12:48:40","canto_approved_date":"2019-11-21 12:48:41","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-12 13:38:51","canto_added_date":"2019-04-03 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-21"},{"uniquename":"PMID:23172863","title":"An empirical Bayes approach for analysis of diverse periodic trends in time-course gene expression data.","citation":"Bioinformatics 2013 Jan 15;29(2):182-8","abstract":"There is a substantial body of works in the biology literature that seeks to characterize the cyclic behavior of genes during cell division. Gene expression microarrays made it possible to measure the expression profiles of thousands of genes simultaneously in time-course experiments to assess changes in the expression levels of genes over time. In this context, the commonly used procedures for testing include the permutation test by de Lichtenberg et al. and the Fisher's G-test, both of which are designed to evaluate periodicity against noise. However, it is possible that a gene of interest may have expression that is neither cyclic nor just noise. Thus, there is a need for a new test for periodicity that can identify cyclic patterns against not only noise but also other non-cyclic patterns such as linear, quadratic or higher order polynomial patterns.\nTo address this weakness, we have introduced an empirical Bayes approach to test for periodicity and compare its performance in terms of sensitivity and specificity with that of the permutation test and Fisher's G-test through extensive simulations and by application to a set of time-course experiments on the Schizosaccharomyces pombe cell-cycle gene expression. We use 'conserved' and 'cycling' genes by Lu et al. to assess the sensitivity and CESR genes by Chenet al. to assess the specificity of our new empirical Bayes method.\nThe SAS Macro for our empirical Bayes test for periodicity is included in the supplementary materials along with a sample run of the MACRO program.\nmkocak1@uthsc.edu\nSupplementary data are available at Bioinformatics online.","doi":"10.1093/bioinformatics/bts672","authors":"Kocak M, George EO, Pyne S, Pounds S","authors_abbrev":"Kocak M et al.","pubmed_publication_date":"15 Jan 2013","pubmed_entrez_date":"2012-11-23","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37279920","title":"A dual, catalytic role for the fission yeast Ccr4-Not complex in gene silencing and heterochromatin spreading.","citation":"Genetics 2023 Aug 09;224(4)","abstract":"Heterochromatic gene silencing relies on combinatorial control by specific histone modifications, the occurrence of transcription, and/or RNA degradation. Once nucleated, heterochromatin propagates within defined chromosomal regions and is maintained throughout cell divisions to warrant proper genome expression and integrity. In the fission yeast Schizosaccharomyces pombe, the Ccr4-Not complex partakes in gene silencing, but its relative contribution to distinct heterochromatin domains and its role in nucleation versus spreading have remained elusive. Here, we unveil major functions for Ccr4-Not in silencing and heterochromatin spreading at the mating type locus and subtelomeres. Mutations of the catalytic subunits Caf1 or Mot2, involved in RNA deadenylation and protein ubiquitinylation, respectively, result in impaired propagation of H3K9me3 and massive accumulation of nucleation-distal heterochromatic transcripts. Both silencing and spreading defects are suppressed upon disruption of the heterochromatin antagonizing factor Epe1. Overall, our results position the Ccr4-Not complex as a critical, dual regulator of heterochromatic gene silencing and spreading.","doi":"10.1093/genetics/iyad108","authors":"Challal D, Menant A, Goksal C, Leroy E, Al-Sady B, Rougemaille M","authors_abbrev":"Challal D et al.","pubmed_publication_date":"09 Aug 2023","pubmed_entrez_date":"2023-06-06","publication_year":"2023","canto_session_key":"62ab4a718bc5d4d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mathieu Rougemaille","canto_first_approved_date":"2023-06-15 11:58:21","canto_approved_date":"2023-06-15 11:58:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-08 16:07:51","canto_added_date":"2023-06-08 00:15:04","annotation_curators":[{"name":"Mathieu Rougemaille","community_curator":true,"annotation_count":90,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.16c","SPAC1B3.05","SPBC28F2.12","SPAC16C9.04c","SPCC18.06c","SPAC18G6.02c","SPCC4G3.15c","SPCC31H12.08c","SPAC29B12.06c"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2023-06-15"},{"uniquename":"PMID:27662899","title":"Nucleosomal signatures impose nucleosome positioning in coding and noncoding sequences in the genome.","citation":"Genome Res 2016 Nov;26(11):1532-1543","abstract":"In the yeast genome, a large proportion of nucleosomes occupy well-defined and stable positions. While the contribution of chromatin remodelers and DNA binding proteins to maintain this organization is well established, the relevance of the DNA sequence to nucleosome positioning in the genome remains controversial. Through quantitative analysis of nucleosome positioning, we show that sequence changes distort the nucleosomal pattern at the level of individual nucleosomes in three species of Schizosaccharomyces and in Saccharomyces cerevisiae This effect is equally detected in transcribed and nontranscribed regions, suggesting the existence of sequence elements that contribute to positioning. To identify such elements, we incorporated information from nucleosomal signatures into artificial synthetic DNA molecules and found that they generated regular nucleosomal arrays indistinguishable from those of endogenous sequences. Strikingly, this information is species-specific and can be combined with coding information through the use of synonymous codons such that genes from one species can be engineered to adopt the nucleosomal organization of another. These findings open the possibility of designing coding and noncoding DNA molecules capable of directing their own nucleosomal organization.","authors":"González S, García A, Vázquez E, Serrano R, Sánchez M, Quintales L, Antequera F","authors_abbrev":"González S et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-09-25","publication_year":"2016","canto_session_key":"5c4990b96d3002cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-11-13 12:08:31","canto_approved_date":"2018-11-13 12:08:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-11-13 12:08:09","canto_added_date":"2018-11-13 12:06:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-11-13"},{"uniquename":"EMBL:AU007697","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9187764","title":"Cassette for the generation of sequential gene disruptions in the yeast Schizosaccharomyces pombe.","citation":"Biotechniques 1997 Jun;22(6):1134-9","abstract":"The ability to conveniently construct gene disruptions is an important methodology for genetic analysis of the fission yeast Schizosaccharomyces pombe. Because of the limited number of selectable markers available for generating gene disruptions in fission yeast, the construction of strains that contain multiple gene disruptions can be quite difficult. This becomes a particular problem when episomal plasmids carrying selectable markers are also required within the same strains. To alleviate these difficulties, we have constructed a hisG-ura(4+)-hisG cassette that can be used repeatedly for constructing gene disruptions in S. pombe. This cassette allows the recycling of the ura4+ marker, thereby permitting the disruption of an indefinite number of genes sequentially within the same strain and/or for subsequently introducing a ura(4+)-marked plasmid.","authors":"McNabb DS, Pak SM, Guarente L","authors_abbrev":"McNabb DS et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:U59434","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34382912","title":"Anillin/Mid1p interacts with the ESCRT-associated protein Vps4p and mitotic kinases to regulate cytokinesis in fission yeast.","citation":"Cell Cycle 2021 Sep;20(18):1845-1860","abstract":"Cytokinesis is the final stage of the cell cycle which separates cellular constituents to produce two daughter cells. Using the fission yeast  Schizosaccharomyces pombe  we have investigated the role of various classes of proteins involved in this process. Central to these is anillin/Mid1p which forms a ring-like structure at the cell equator that predicts the site of cell separation through septation in fission yeast. Here we demonstrate a direct physical interaction between Mid1p and the endosomal sorting complex required for transport (ESCRT)-associated protein Vps4p, a genetic interaction of the  mid1  and  vps4  genes essential for cell viability, and a requirement of Vps4p for the correct cellular localization of Mid1p. Furthermore, we show that Mid1p is phosphorylated by aurora kinase, a genetic interaction of the  mid1  and the aurora kinase  ark1  genes is essential for cell viability, and that Ark1p is also required for the correct cellular localization of Mid1p. We mapped the sites of phosphorylation of Mid1p by human aurora A and the polo kinase Plk1 and assessed their importance in fission yeast by mutational analysis. Such analysis revealed serine residues S332, S523 and S531 to be required for Mid1p function and its interaction with Vps4p, Ark1p and Plo1p. Combined these data suggest a physical interaction between Mid1p and Vps4p important for cytokinesis, and identify phosphorylation of Mid1p by aurora and polo kinases as being significant for this process.","doi":"10.1080/15384101.2021.1962637","authors":"Rezig IM, Yaduma WG, Gould GW, McInerny CJ","authors_abbrev":"Rezig IM et al.","pubmed_publication_date":"Sep 2021","pubmed_entrez_date":"2021-08-12","publication_year":"2021","canto_session_key":"c33d429f18cfda43","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chris McInerny","canto_first_approved_date":"2021-09-05 16:06:47","canto_approved_date":"2021-09-05 16:06:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-08-27 13:46:04","canto_added_date":"2021-08-14 00:15:04","annotation_curators":[{"name":"Chris McInerny","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.06","SPCC4B3.15","SPCC320.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2021-09-05"},{"uniquename":"PMID:7300901","title":"In vivo decoding rules in Schizosaccharomyces pombe are at variance with in vitro data.","citation":"Nature 1981 Nov 12;294(5837):187-8","abstract":"","authors":"Munz P, Leupold U, Agris P, Kohli J","authors_abbrev":"Munz P et al.","pubmed_publication_date":"12 Nov 1981","pubmed_entrez_date":"1981-11-12","publication_year":"1981","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7812044","title":"The centromeric K-type repeat and the central core are together sufficient to establish a functional Schizosaccharomyces pombe centromere.","citation":"Mol Biol Cell 1994 Jul;5(7):747-61","abstract":"The DNA requirements for centromere function in fission yeast have been investigated using a minichromosome assay system. Critical elements of Schizosaccharomyces pombe centromeric DNA are portions of the centromeric central core and sequences within a 2.1-kilobase segment found on all three chromosomes as part of the K-type (K/K\"/dg) centromeric repeat. The S. pombe centromeric central core contains DNA sequences that appear functionally redundant, and the inverted repeat motif that flanks the central core in all native fission yeast centromeres is not essential for centromere function in circular minichromosomes. Tandem copies of centromeric repeat K\", in conjunction with the central core, exert an additive effect on centromere function, increasing minichromosome mitotic stability with each additional copy. Centromeric repeats B and L, however, and parts of the central core and its core-associated repeat are dispensable and cannot substitute for K-type sequences. Several specific protein binding sites have been identified within the centromeric K-type repeat, consistent with a recently proposed model for centromere/kinetochore function in S. pombe.","authors":"Baum M, Ngan VK, Clarke L","authors_abbrev":"Baum M et al.","pubmed_publication_date":"Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_session_key":"0aad7064d9d54547","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 19:05:41","canto_approved_date":"2018-12-22 19:05:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 19:05:37","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:10503538","title":"Isolation and characterization of temperature-sensitive mutations in the gene (rpb3) for subunit 3 of RNA polymerase II in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1999 Aug;262(1):73-84","abstract":"Subunit 3 (Rpb3) of eukaryotic RNA polymerase II is a homologue of the alpha subunit of prokaryotic RNA polymerase, which plays a key role in subunit assembly of this complex enzyme by providing the contact surfaces for both beta and beta' subunits. Previously we demonstrated that the Schizosaccharomyces pombe Rpb3 protein forms a core subassembly together with Rpb2 (the beta homologue) and Rpb11 (the second alpha homologue) subunits, as in the case of the prokaryotic alpha2beta complex. In order to obtain further insight into the physiological role(s) of Rpb3, we subjected the S. pombe rpb3 gene to mutagenesis. A total of nine temperature-sensitive (Ts) and three cold-sensitive (Cs) S. pombe mutants have been isolated, each (with the exception of one double mutant) carrying a single mutation in the rpb3 gene in one of the four regions (A D) that are conserved between the homologues of eukaryotic subunit 3. The three Cs mutations were all located in region A, in agreement with the central role of the corresponding region in the assembly of prokaryotic RNA polymerase; the Ts mutations, in contrast, were found in all four regions. Growth of the Ts mutants was reduced to various extents at non-permissive temperatures. Since the metabolic stability of most Ts mutant Rpb3 proteins was markedly reduced at non-permissive temperature, we predict that these mutant Rpb3 proteins are defective in polymerase assembly or the mutant RNA polymerases containing mutant Rpb3 subunits are unstable. In accordance with this prediction, the Ts phenotype of all the mutants was suppressed to varying extents by overexpression of Rpb11, the pairing partner of Rpb3 in the core subassembly. We conclude that the majority of rpb3 mutations affect the assembly of Rpb3, even though their effects on subunit assembly vary depending on the location of the mutation considered.","authors":"Mitobe J, Mitsuzawa H, Yasui K, Ishihama A","authors_abbrev":"Mitobe J et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-09-30","publication_year":"1999","canto_session_key":"a7d1fe2ced263484","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-29 08:38:26","canto_approved_date":"2019-01-29 08:38:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-19 16:38:41","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.15","SPAC23G3.01","SPAC3A12.07","SPCC1020.04c","SPCC1442.10c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-01-29"},{"uniquename":"PMID:17194216","title":"Connectivity in the yeast cell cycle transcription network: inferences from neural networks.","citation":"PLoS Comput Biol 2006 Dec 22;2(12):e169","abstract":"A current challenge is to develop computational approaches to infer gene network regulatory relationships based on multiple types of large-scale functional genomic data. We find that single-layer feed-forward artificial neural network (ANN) models can effectively discover gene network structure by integrating global in vivo protein:DNA interaction data (ChIP/Array) with genome-wide microarray RNA data. We test this on the yeast cell cycle transcription network, which is composed of several hundred genes with phase-specific RNA outputs. These ANNs were robust to noise in data and to a variety of perturbations. They reliably identified and ranked 10 of 12 known major cell cycle factors at the top of a set of 204, based on a sum-of-squared weights metric. Comparative analysis of motif occurrences among multiple yeast species independently confirmed relationships inferred from ANN weights analysis. ANN models can capitalize on properties of biological gene networks that other kinds of models do not. ANNs naturally take advantage of patterns of absence, as well as presence, of factor binding associated with specific expression output; they are easily subjected to in silico \"mutation\" to uncover biological redundancies; and they can use the full range of factor binding values. A prominent feature of cell cycle ANNs suggested an analogous property might exist in the biological network. This postulated that \"network-local discrimination\" occurs when regulatory connections (here between MBF and target genes) are explicitly disfavored in one network module (G2), relative to others and to the class of genes outside the mitotic network. If correct, this predicts that MBF motifs will be significantly depleted from the discriminated class and that the discrimination will persist through evolution. Analysis of distantly related Schizosaccharomyces pombe confirmed this, suggesting that network-local discrimination is real and complements well-known enrichment of MBF sites in G1 class genes.","authors":"Hart CE, Mjolsness E, Wold BJ","authors_abbrev":"Hart CE et al.","pubmed_publication_date":"22 Dec 2006","pubmed_entrez_date":"2006-12-30","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6325178","title":"Rearrangements of the transposable mating-type cassettes of fission yeast.","citation":"EMBO J 1984 Mar;3(3):603-10","abstract":"The fission yeast, Schizosaccharomyces pombe, switches mating type every few cell divisions. Switching is controlled by the genes of the mating-type locus, which consists of three components, mat1, mat2-P and mat3-M, each separated by approximately 15 kb. Copy transposition of P (Plus) or M (Minus) information from mat2-P or mat3-M into the expression locus mat1 mediates cell type switching. The mating-type locus undergoes events at high frequency (10(-2)-10(-6)) which stabilize one or other mating type. These events are shown to be rearrangements which result in either deletion or insertion of DNA between cassettes.","authors":"Beach DH, Klar AJ","authors_abbrev":"Beach DH et al.","pubmed_publication_date":"Mar 1984","pubmed_entrez_date":"1984-03-01","publication_year":"1984","canto_session_key":"320a8f69a31884c8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-12-08 22:35:23","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-08 22:35:14","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-12-08"},{"uniquename":"PMID:35704207","title":"DNA:RNA Immunoprecipitation from S. pombe Cells for qPCR and Genome-Wide Sequencing.","citation":"Methods Mol Biol 2022;2528:411-428","abstract":"By temporarily distorting the DNA double helix, the moving RNA polymerases can lead to the formation of non-B DNA structures. One of the most abundant and largest non-B DNA structures in the genome is the R-loop, a three-stranded structure forming when the nascent RNA hybridizes with its DNA template, thereby extruding the non-template DNA strand. Growing evidence suggests that at least a subset of R-loops could induce transcription stress and genome instability, although the direct, primary consequences of R-loop formation on the surrounding chromatin are still unclear.To understand the direct impact of R-loops on transcription and genome stability, accurate and quantitative mapping of R-loops is essential. R-loop mapping is commonly achieved using the antibody-based DNA:RNA Immunoprecipitation (DRIP) strategy. While it is reasonably straightforward to obtain robust DRIP enrichments from human cells, this has proved harder in yeast, where DRIP signals are often relatively weak, with a poor signal-to-noise ratio. Although it is unclear whether such weak signals stem from a technical or a biological reality, they make the accurate quantification of DRIP signals all the more important, especially when deep sequencing is used to monitor and quantify the distribution of R-loops genome-wide. Here we propose a DRIP protocol that has been optimized for the mapping and the quantification of R-loops in Schizosaccharomyces pombe but that can also be used in Saccharomyces cerevisiae. As a result, this protocol can be used to generate calibrated DRIP-seq data, where genomic DNA extracted from S. cerevisiae serves as spike-in reference.","doi":"10.1007/978-1-0716-2477-7_27","authors":"Vachez L, Teste C, Vanoosthuyse V","authors_abbrev":"Vachez L et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-06-15","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-06-17 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34010011","title":"Heh2/Man1 may be an evolutionarily conserved sensor of NPC assembly state.","citation":"Mol Biol Cell 2021 Jul 15;32(15):1359-1373","abstract":"Integral membrane proteins of the Lap2-emerin-MAN1 (LEM) family have emerged as important components of the inner nuclear membrane (INM) required for the functional and physical integrity of the nuclear envelope. However, like many INM proteins, there is limited understanding of the biochemical interaction networks that enable LEM protein function. Here, we show that Heh2/Man1 can interact with major scaffold components of the nuclear pore complex (NPC), specifically the inner ring complex (IRC), in evolutionarily distant yeasts. Although an N-terminal domain is required for Heh2 targeting to the INM, we demonstrate that more stable interactions with the NPC are mediated by a C-terminal winged helix (WH) domain, thus decoupling INM targeting and NPC binding. Inhibiting Heh2's interactions with the NPC by deletion of the Heh2 WH domain leads to NPC clustering. Interestingly, Heh2's association with NPCs can also be disrupted by knocking out several outer ring nucleoporins. Thus, Heh2's interaction with NPCs depends on the structural integrity of both major NPC scaffold complexes. We propose a model in which Heh2 acts as a sensor of NPC assembly state, which may be important for NPC quality control mechanisms and the segregation of NPCs during cell division.","doi":"10.1091/mbc.E20-09-0584","authors":"Borah S, Thaller DJ, Hakhverdyan Z, Rodriguez EC, Isenhour AW, Rout MP, King MC, Lusk CP","authors_abbrev":"Borah S et al.","pubmed_publication_date":"15 Jul 2021","pubmed_entrez_date":"2021-05-19","publication_year":"2021","canto_session_key":"de6d5e34a87aea0b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-25 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC890.06","SPCC1739.14","SPCC290.03c","SPAC1486.05","SPAC14C4.05c","SPAC26A3.15c","SPAP27G11.10c","SPBC29A10.07","SPCC1620.11"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:25849502","title":"Crystallization and preliminary X-ray characterization of the eukaryotic replication terminator Reb1-Ter DNA complex.","citation":"Acta Crystallogr F Struct Biol Commun 2015 Apr;71(Pt 4):414-8","abstract":"The Reb1 protein from Schizosaccharomyces pombe is a member of a family of proteins that control programmed replication termination and/or transcription termination in eukaryotic cells. These events occur at naturally occurring replication fork barriers (RFBs), where Reb1 binds to termination (Ter) DNA sites and coordinates the polar arrest of replication forks and transcription approaching in opposite directions. The Reb1 DNA-binding and replication-termination domain was expressed in Escherichia coli, purified and crystallized in complex with a 26-mer DNA Ter site. Batch crystallization under oil was required to produce crystals of good quality for data collection. Crystals grew in space group P2₁, with unit-cell parameters a = 68.9, b = 162.9, c = 71.1 Å, β = 94.7°. The crystals diffracted to a resolution of 3.0 Å. The crystals were mosaic and required two or three cycles of annealing. This study is the first to yield structural information about this important family of proteins and will provide insights into the mechanism of replication and transcription termination.","doi":"10.1107/S2053230X15004112","authors":"Jaiswal R, Singh SK, Bastia D, Escalante CR","authors_abbrev":"Jaiswal R et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-04-08","publication_year":"2015","canto_session_key":"86d936836a1e0ccc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-10-07 18:20:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-04 10:16:32","canto_added_date":"2015-04-09 00:18:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-04-04"},{"uniquename":"PMID:10835372","title":"Partial suppression of the fission yeast rqh1(-) phenotype by expression of a bacterial Holliday junction resolvase.","citation":"EMBO J 2000 Jun 01;19(11):2751-62","abstract":"A key stage during homologous recombination is the processing of the Holliday junction, which determines the outcome of the recombination reaction. To dissect the pathways of Holliday junction processing in a eukaryote, we have targeted an Escherichia coli Holliday junction resolvase to the nuclei of fission yeast recombination-deficient mutants and analysed their phenotypes. The resolvase partially complements the UV and hydroxyurea hypersensitivity and associated aberrant mitoses of an rqh1(-) mutant. Rqh1 is a member of the RecQ subfamily of DNA helicases that control recombination particularly during S-phase. Significantly, overexpression of the resolvase in wild-type cells partly mimics the loss of viability, hyper-recombination and 'cut' phenotype of an rqh1(-) mutant. These results indicate that Holliday junctions form in wild-type cells that are normally removed in a non-recombinogenic way, possibly by Rqh1 catalysing their reverse branch migration. We propose that in the absence of Rqh1, replication fork arrest results in the accumulation of Holliday junctions, which can either impede sister chromatid segregation or lead to the formation of recombinants through Holliday junction resolution.","authors":"Doe CL, Dixon J, Osman F, Whitby MC","authors_abbrev":"Doe CL et al.","pubmed_publication_date":"01 Jun 2000","pubmed_entrez_date":"2000-06-03","publication_year":"2000","canto_session_key":"5c375f308f62eac7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-09 11:18:25","canto_approved_date":"2023-11-28 14:10:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-09 11:18:19","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-09"},{"uniquename":"PMID:17541414","title":"Anchoring microtubules at the spindle poles.","citation":"Nat Cell Biol 2007 Jun;9(6):619-21","abstract":"","authors":"Paoletti A, Tran PT","authors_abbrev":"Paoletti A et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-06-02","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27667686","title":"Potent, Reversible, and Specific Chemical Inhibitors of Eukaryotic Ribosome Biogenesis.","citation":"Cell 2016 Oct 06;167(2):512-524.e14","abstract":"All cellular proteins are synthesized by ribosomes, whose biogenesis in eukaryotes is a complex multi-step process completed within minutes. Several chemical inhibitors of ribosome function are available and used as tools or drugs. By contrast, we lack potent validated chemical probes to analyze the dynamics of eukaryotic ribosome assembly. Here, we combine chemical and genetic approaches to discover ribozinoindoles (or Rbins), potent and reversible triazinoindole-based inhibitors of eukaryotic ribosome biogenesis. Analyses of Rbin sensitivity and resistance conferring mutations in fission yeast, along with biochemical assays with recombinant proteins, provide evidence that Rbins' physiological target is Midasin, an essential ∼540-kDa AAA+ (ATPases associated with diverse cellular activities) protein. Using Rbins to acutely inhibit or activate Midasin function, in parallel experiments with inhibitor-sensitive or inhibitor-resistant cells, we uncover Midasin's role in assembling Nsa1 particles, nucleolar precursors of the 60S subunit. Together, our findings demonstrate that Rbins are powerful probes for eukaryotic ribosome assembly.","doi":"10.1016/j.cell.2016.08.070","authors":"Kawashima SA, Chen Z, Aoi Y, Patgiri A, Kobayashi Y, Nurse P, Kapoor TM","authors_abbrev":"Kawashima SA et al.","pubmed_publication_date":"06 Oct 2016","pubmed_entrez_date":"2016-09-27","publication_year":"2016","canto_session_key":"cdefbdb00205d394","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Zhen Chen","canto_first_approved_date":"2018-12-03 14:26:04","canto_approved_date":"2026-01-08 09:55:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-11-20 19:31:06","canto_added_date":"2016-09-28 00:15:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":51,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Zhen Chen","community_curator":true,"annotation_count":1,"orcid":"0000-0003-1723-0251","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19F5.05c","SPCC737.08","SPAC890.04c","SPCC18.05c","SPBC83.15","SPBC16E9.10c","SPCC4G3.18"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-12-03"},{"uniquename":"PMID:22365419","title":"The Schizosaccharomyces pombe AlkB homolog Abh1 exhibits AP lyase activity but no demethylase activity.","citation":"DNA Repair (Amst) 2012 May 01;11(5):453-62","abstract":"2-Oxoglutarate (2OG) and iron (Fe(II)) dependent dioxygenases catalyze a wide range of biological oxidations, including hydroxylation and demethylation of proteins and nucleic acids. AlkB from Escherichia coli directly reverses certain methyl lesions in DNA, and defines a subfamily of 2OG/Fe(II) dioxygenases that has so far been shown to be involved in both nucleic acid repair and modification. The human genome encodes nine AlkB homologs and the function of most of these is still unknown. The fission yeast Schizosaccharomyces pombe has two AlkB homologs and here we have addressed the function of one of these, Abh1, which appears not to possess a classical AlkB-like repair activity. No enzymatic activity was found toward methylated DNA or etheno adducts, nor was the yeast abh1- mutant sensitive toward alkylating agents. Interestingly, heterologous expression of E. coli AlkB protected the fission yeast cells from alkylation induced cytotoxicity, suggesting that S. pombe lacks systems for efficient repair of lesions that are AlkB substrates. Further, we show that Abh1 possesses an unexpected DNA incision activity at apurinic/apyrimidinic (AP) sites. This AP lyase activity did not depend on 2OG and Fe(II) and was not repressed by dioxygenase inhibitors. Survival and complementation analyses failed to reveal any biological role for AP lyase cleavage by Abh1. It appears that in vitro AP lyase activity can be detected for a number of enzymes belonging to structurally and functionally unrelated families, but the in vivo significance of such activities may be questionable.","doi":"10.1016/j.dnarep.2012.01.014","authors":"Korvald H, Falnes PØ, Laerdahl JK, Bjørås M, Alseth I","authors_abbrev":"Korvald H et al.","pubmed_publication_date":"01 May 2012","pubmed_entrez_date":"2012-02-28","publication_year":"2012","canto_session_key":"b1789c18fe3b02f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-10-13 13:53:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-13 13:52:10","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC13G1.04c","SPAPB24D3.04c","SPCC970.01","SPAC3C7.03c"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2015-10-13"},{"uniquename":"PMID:38285941","title":"Specialized replication of heterochromatin domains ensures self-templated chromatin assembly and epigenetic inheritance.","citation":"Proc Natl Acad Sci U S A 2024 Feb 06;121(6):e2315596121","abstract":"Heterochromatin, defined by histone H3 lysine 9 methylation (H3K9me), spreads across large domains and can be epigenetically inherited in a self-propagating manner. Heterochromatin propagation depends upon a read-write mechanism, where the Clr4/Suv39h methyltransferase binds to preexisting trimethylated H3K9 (H3K9me3) and further deposits H3K9me. How the parental methylated histone template is preserved during DNA replication is not well understood. Here, we demonstrate using  Schizosaccharomyces pombe  that heterochromatic regions are specialized replication domains demarcated by their surrounding boundary elements. DNA replication throughout these domains is distinguished by an abundance of replisome components and is coordinated by Swi6/HP1. Although mutations in the replicative helicase subunit Mcm2 that affect histone binding impede the maintenance of a heterochromatin domain at an artificially targeted ectopic site, they have only a modest impact on heterochromatin propagation via the read-write mechanism at an endogenous site. Instead, our findings suggest a crucial role for the replication factor Mcl1 in retaining parental histones and promoting heterochromatin propagation via a mechanism involving the histone chaperone FACT. Engagement of FACT with heterochromatin requires boundary elements, which position the heterochromatic domain at the nuclear peripheral subdomain enriched for heterochromatin factors. Our findings highlight the importance of replisome components and boundary elements in creating a specialized environment for the retention of parental methylated histones, which facilitates epigenetic inheritance of heterochromatin.","doi":"10.1073/pnas.2315596121","authors":"Nathanailidou P, Dhakshnamoorthy J, Xiao H, Zofall M, Holla S, O'Neill M, Andresson T, Wheeler D, Grewal SIS","authors_abbrev":"Nathanailidou P et al.","pubmed_publication_date":"06 Feb 2024","pubmed_entrez_date":"2024-01-29","publication_year":"2024","canto_session_key":"fdfc9c73a3820302","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Patroula Nathanailidou","canto_first_approved_date":"2024-04-08 17:10:56","canto_approved_date":"2024-05-14 14:44:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-07 23:12:43","canto_added_date":"2024-01-31 00:25:05","annotation_curators":[{"name":"Patroula Nathanailidou","community_curator":true,"annotation_count":30,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC613.12c","SPBP8B7.19","SPBC4.07c","SPBC609.05","SPCC338.16","SPBC4.04c","SPCC576.10c","SPBC428.08c","SPCC1682.10","SPAC664.01c","SPAC607.05","SPAC3A11.12c","SPCC736.11","SPBC582.07c","SPBC800.03","SPBC16G5.01","SPBP19A11.03c","SPBC17D11.07c","SPAC694.06c","SPBC1A4.03c","SPAPB1E7.02c","SPBP35G2.10","SPAC31G5.13","SPBC660.13c","SPBC119.01","SPAC23G3.11","SPCC1753.01c","SPAC227.16c","SPAC17G6.12","SPAC25A8.01c","SPBC16C6.07c","SPAC1420.03","SPBC409.05"],"gene_count":33,"ltp_gene_count":31,"approved_date":"2024-04-08"},{"uniquename":"PMID:10757751","title":"Isolation and characterization of par1(+) and par2(+): two Schizosaccharomyces pombe genes encoding B' subunits of protein phosphatase 2A.","citation":"Genetics 2000 Mar;154(3):1025-38","abstract":"Protein phosphatase 2A (PP2A) is one of the major serine/threonine phosphatases found in eukaryotic cells. We cloned two genes, par1(+) and par2(+), encoding distinct B' subunits of PP2A in fission yeast. They share 52% identity at the amino acid sequence level. Neither gene is essential but together they are required for normal septum positioning and cytokinesis, for growth at both high and low temperature, and for growth under a number of stressful conditions. Immunofluorescence microscopy revealed that Par2p has a cell-cycle-related localization pattern, being localized at cell ends during interphase and forming a medial ring in cells that are undergoing septation and cytokinesis. Our analyses also indicate that Par1p is more abundant than Par2p in the cell. Cross-organism studies showed that both par1(+) and par2(+) could complement the rts1Delta allele in Saccharomyces cerevisiae, albeit to different extents, in spite of the fact that neither contains a serine/threonine-rich N-terminal domain like that found in the S. cerevisiae homolog Rts1p. Thus, while Schizosaccharomyces pombe is more similar to higher eukaryotes with respect to its complement of B'-encoding genes, the function of those proteins is conserved relative to that of Rts1p.","authors":"Jiang W, Hallberg RL","authors_abbrev":"Jiang W et al.","pubmed_publication_date":"Mar 2000","pubmed_entrez_date":"2000-04-11","publication_year":"2000","canto_session_key":"64b3e898f595aee5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-09 16:48:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-19 17:07:35","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":37,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.02","SPAC6F12.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-01-19"},{"uniquename":"PMID:21518960","title":"Mrc1 marks early-firing origins and coordinates timing and efficiency of initiation in fission yeast.","citation":"Mol Cell Biol 2011 Jun;31(12):2380-91","abstract":"How early- and late-firing origins are selected on eukaryotic chromosomes is largely unknown. Here, we show that Mrc1, a conserved factor required for stabilization of stalled replication forks, selectively binds to the early-firing origins in a manner independent of Cdc45 and Hsk1 kinase in the fission yeast Schizosaccharomyces pombe. In mrc1Δ cells (and in swi1Δ cells to some extent), efficiency of firing is stimulated, and its timing is advanced selectively at those origins that are normally bound by Mrc1. In contrast, the late or inefficient origins which are not bound by Mrc1 are not activated in mrc1Δ cells. The enhanced firing and precocious Cdc45 loading at Mrc1-bound early-firing origins are not observed in a checkpoint mutant of mrc1, suggesting that non-checkpoint function is involved in maintaining the normal program of early-firing origins. We propose that prefiring binding of Mrc1 is an important marker of early-firing origins which are precociously activated by the absence of this protein.","doi":"10.1128/MCB.01239-10","authors":"Hayano M, Kanoh Y, Matsumoto S, Masai H","authors_abbrev":"Hayano M et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-04-27","publication_year":"2011","canto_session_key":"f54393989e565d1a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-03-30 13:23:36","canto_approved_date":"2024-12-11 16:19:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-08 15:56:40","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17D4.02","SPBC11B10.09","SPCC18B5.11c","SPCC16A11.17","SPAC694.06c","SPBC776.12c","SPBC216.06c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2016-03-30"},{"uniquename":"PMID:24564655","title":"Mechanisms of the 14-3-3 protein function: regulation of protein function through conformational modulation.","citation":"Physiol Res 2014;63(Suppl 1):S155-64","abstract":"Many aspects of protein function regulation require specific protein-protein interactions to carry out the exact biochemical and cellular functions. The highly conserved members of the 14-3-3 protein family mediate such interactions and through binding to hundreds of other proteins provide multitude of regulatory functions, thus playing key roles in many cellular processes. The 14-3-3 protein binding can affect the function of the target protein in many ways including the modulation of its enzyme activity, its subcellular localization, its structure and stability, or its molecular interactions. In this minireview, we focus on mechanisms of the 14-3-3 protein-dependent regulation of three important 14-3-3 binding partners: yeast neutral trehalase Nth1, regulator of G-protein signaling 3 (RGS3), and phosducin.","authors":"Obsilova V, Kopecka M, Kosek D, Kacirova M, Kylarova S, Rezabkova L, Obsil T","authors_abbrev":"Obsilova V et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-26","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-10-22 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30626735","title":"Ctp1 protein-DNA filaments promote DNA bridging and DNA double-strand break repair.","citation":"J Biol Chem 2019 Mar 01;294(9):3312-3320","abstract":"The Ctp1 protein in  Schizosaccharomyces pombe  is essential for DNA double-strand break (DSB) repair by homologous recombination. Fission yeast Ctp1 and its budding yeast (Sae2) and human (CtIP) homologs control Mre11-Rad50-Nbs1 nuclease complex activity and harbor DNA-binding and -bridging activities. However, the molecular basis for Ctp1-DNA transactions remains undefined. Here, we report atomic force microscopy (AFM) imaging of  S. pombe  Ctp1-DNA complexes revealing that Ctp1 polymerizes on dsDNA molecules and forms synaptic filaments that bridge two dsDNA strands. We observed that Ctp1 DNA filaments are typified by an average filament length of ∼180 bp of dsDNA and a Ctp1 tetramer footprint of ∼15 bp. Biochemical results characterizing Ctp1 variants with impaired DNA-binding or -bridging properties were consistent with Ctp1-mediated DNA bridging requiring the intact and correctly folded Ctp1 tetramer. Furthermore, mutations altering Ctp1 oligomerization and DNA bridging  in vitro  conferred cell sensitivity to DSB-producing agents. Together, these results support an important role for Ctp1-regulated DNA strand coordination required for DNA DSB repair in  S. pombe .","doi":"10.1074/jbc.RA118.006759","authors":"Andres SN, Li ZM, Erie DA, Williams RS","authors_abbrev":"Andres SN et al.","pubmed_publication_date":"01 Mar 2019","pubmed_entrez_date":"2019-01-11","publication_year":"2019","canto_session_key":"699def6a055fb333","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sara Andres","canto_first_approved_date":"2020-05-05 14:39:25","canto_approved_date":"2021-10-19 10:34:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-04-23 21:54:00","canto_added_date":"2019-01-12 01:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sara Andres","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-05-05"},{"uniquename":"PMID:9428524","title":"Transient inhibition of histone deacetylation alters the structural and functional imprint at fission yeast centromeres.","citation":"Cell 1997 Dec 26;91(7):1021-32","abstract":"Histone acetylation may act to mark and maintain transcriptionally active or inactive chromosomal domains through the cell cycle and in different lineages. A novel role for histone acetylation in centromere regulation has been identified. Exposure of fission yeast cells to TSA, a specific inhibitor of histone deacetylase, interferes with repression of marker genes in centromeric heterochromatin, causes chromosome loss, and disrupts the localization of Swi6p, a component of centromeric heterochromatin. Transient TSA treatment induces a heritable hyperacetylated state in centromeric chromatin that is propagated in lineages in the absence of drug. This state is linked in cis to the treated centromere locus and correlates with inheritance of functionally defective centromeres and persistent chromosome segregation problems. Thus, assembly of fully functional centromeres is partly imprinted in the underacetylated or transcriptionally silent state of centromeric chromatin.","authors":"Ekwall K, Olsson T, Turner BM, Cranston G, Allshire RC","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"26 Dec 1997","pubmed_entrez_date":"1998-01-15","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:231973","title":"The reaction of cytochrome oxidase with oxygen in the fission yeast Schizosaccharomyces pombe 972h-. Studies at subzero temperatures and measurement of apparent oxygen affinity.","citation":"Biochem J 1979 Dec 15;184(3):555-63","abstract":"1. Cytochrome alpha 3 in whole-cell suspensions of the fission yeast Schizosaccharomyces pombe reacted in the reduced form with CO to give a photodissociable CO complex with absorption maxima at 429, 543 and 591 nm in CO-liganded reduced-minus-reduced difference spectra. 2. Other CO-bound haemoproteins, cytochromes P-420 and P-450, were not photodissociated under the conditions employed. 3. Measurements of the rates of reassociation of CO with cytochrome alpha 3 after flash photolysis over the temperature range from -101 to -109 degrees C gave a value for Eact. of 28.6 kJ/mol. 4. Between -94 and -106 degrees C, O2 reacted with cytochrome oxidase in intact cells to give an oxygenated intermediate (compound A). 5. At -70 degrees C compound A was converted into a second spectrally distinct intermediate (compound B). 6. Electron transport, indicated by the oxidation of cytochromes alpha + alpha 3 and cytochrome c, did not occur until the temperature was raised to -50 degrees C. 7. At room temperature cytochfome oxidase was oxidized to 50% of its steady-state concentration by 0.35 microM-O2.","authors":"Poole RK, Lloyd D, Chance B","authors_abbrev":"Poole RK et al.","pubmed_publication_date":"15 Dec 1979","pubmed_entrez_date":"1979-12-15","publication_year":"1979","canto_session_key":"20a6226c4391b4b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-26 15:31:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-26 15:31:08","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-26"},{"uniquename":"EMBL:AU007561","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29082230","title":"Yeast for virus research.","citation":"Microb Cell 2017 Sep 18;4(10):311-330","abstract":"Budding yeast ( Saccharomyces cerevisiae ) and fission yeast ( Schizosaccharomyces pombe ) are two popular model organisms for virus research. They are natural hosts for viruses as they carry their own indigenous viruses. Both yeasts have been used for studies of plant, animal and human viruses. Many positive sense (+) RNA viruses and some DNA viruses replicate with various levels in yeasts, thus allowing study of those viral activities during viral life cycle. Yeasts are single cell eukaryotic organisms. Hence, many of the fundamental cellular functions such as cell cycle regulation or programed cell death are highly conserved from yeasts to higher eukaryotes. Therefore, they are particularly suited to study the impact of those viral activities on related cellular activities during virus-host interactions. Yeasts present many unique advantages in virus research over high eukaryotes. Yeast cells are easy to maintain in the laboratory with relative short doubling time. They are non-biohazardous, genetically amendable with small genomes that permit genome-wide analysis of virologic and cellular functions. In this review, similarities and differences of these two yeasts are described. Studies of virologic activities such as viral translation, viral replication and genome-wide study of virus-cell interactions in yeasts are highlighted. Impacts of viral proteins on basic cellular functions such as cell cycle regulation and programed cell death are discussed. Potential applications of using yeasts as hosts to carry out functional analysis of small viral genome and to develop high throughput drug screening platform for the discovery of antiviral drugs are presented.","doi":"10.15698/mic2017.10.592","authors":"Zhao RY","authors_abbrev":"Zhao RY","pubmed_publication_date":"18 Sep 2017","pubmed_entrez_date":"2017-10-31","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-11-02 01:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPAJ2731","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14502989","title":"The COP9 signalosome: regulating plant development through the control of proteolysis.","citation":"Annu Rev Plant Biol 2003;54:165-82","abstract":"The COP9 signalosome (CSN) is a multiprotein complex that was initially identified in plants as a repressor of photomorphogenesis. It is now known to play major roles in several other developmental pathways, from auxin response to flower development. Furthermore, the COP9 signalosome shares homologies with the lid sibcomplex of the proteasome and is evolutionarily conserved from fission yeast to humans. It is important for the proper development of virtually all higher eukaryotes. In recent years, significant progress has been made in unraveling the molecular, cellular, and physiological mode of action of the COP9 signalosome. This review discusses our current understanding of the COP9 signalosome function with particular emphasis on its recently defined role in modulating a wide variety of cellular processes by regulating specific protein degradation events.","authors":"Serino G, Deng XW","authors_abbrev":"Serino G et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-09-25","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15475954","title":"RITS acts in cis to promote RNA interference-mediated transcriptional and post-transcriptional silencing.","citation":"Nat Genet 2004 Nov;36(11):1174-80","abstract":"RNA interference is a conserved mechanism by which double-stranded RNA is processed into short interfering RNAs (siRNAs) that can trigger both post-transcriptional and transcriptional gene silencing. In fission yeast, the RNA-induced initiation of transcriptional gene silencing (RITS) complex contains Dicer-generated siRNAs and is required for heterochromatic silencing. Here we show that RITS components, including Argonaute protein, bind to all known heterochromatic loci. At the mating-type region, RITS is recruited to the centromere-homologous repeat cenH in a Dicer-dependent manner, whereas the spreading of RITS across the entire 20-kb silenced domain, as well as its subsequent maintenance, requires heterochromatin machinery including Swi6 and occurs even in the absence of Dicer. Furthermore, our analyses suggest that RNA interference machinery operates in cis as a stable component of heterochromatic domains with RITS tethered to silenced loci by methylation of histone H3 at Lys9. This tethering promotes the processing of transcripts and generation of additional siRNAs for heterochromatin maintenance.","authors":"Noma K, Sugiyama T, Cam H, Verdel A, Zofall M, Jia S, Moazed D, Grewal SI","authors_abbrev":"Noma K et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-12","publication_year":"2004","canto_session_key":"6d702a6f1957248f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-06-18 15:13:21","canto_approved_date":"2024-06-18 15:13:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-06-15 21:01:24","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":79,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.11","SPAC6F12.09","SPCC188.13c","SPBC428.08c","SPBC83.03c","SPAC21E11.03c","SPAC18G6.02c","SPAC664.01c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2024-06-18"},{"uniquename":"PMID:27613427","title":"Stress sensitivity of a fission yeast strain lacking histidine kinases is rescued by the ectopic expression of Chk1 from Candida albicans.","citation":"Curr Genet 2017 May;63(2):343-357","abstract":"The development of new drugs against the pathogenic yeast Candida albicans is compelling and the evolution of relevant bioassays is important to achieve this goal. Promising drug targets are proteins that lack human counterparts which are true for the His-to-Asp phosphorelay signal transduction systems, important for stress sensing in bacteria, fungi, and plants. In the pathogenic yeast, Candida albicans, the CaChk1 histidine kinase is a trigger of the pathway that leads to a switch from yeast to hyphal growth necessary for invasion. Intriguingly, the model yeast Schizosaccharomyces pombe has a similar phosphorelay system, with three histidine kinases named Mak1, Mak2, and Mak3, which are important for the prevention of aberrant mating and sporulation on rich media. This study uncovered distinct functions for the three histidine kinases; Mak1 alone or Mak2 and Mak3 together were sufficient for the repression of the meiotic cycle when nutrients were available. Moreover, strains lacking histidine kinase genes were sensitive to various types of stress conditions in an auxotrophic strain background, while the stress sensitivity was lost in prototrophic strains. Finally, the stress sensitivity of a S. pombe strain that lacks endogenous histidine kinases could be complemented by the ectopic expression of the CaChk1 histidine kinase from C. albicans. This finding opens up for the possibility to perform a drug screen with a biological read-out in S. pombe to find inhibitors of CaChk1.","doi":"10.1007/s00294-016-0644-9","authors":"Maksimov V, Wäneskog M, Rodriguez A, Bjerling P","authors_abbrev":"Maksimov V et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2016-09-11","publication_year":"2017","canto_session_key":"5c744b7dd350f431","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pernilla Bjerling","canto_first_approved_date":"2017-08-10 10:32:50","canto_approved_date":"2025-09-03 15:21:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-04 11:32:55","canto_added_date":"2016-09-12 00:15:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pernilla Bjerling","community_curator":true,"annotation_count":45,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27E2.09","SPCC74.06","SPAC1834.08","SPCC330.05c","SPCC1322.13","SPBC1A4.02c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-08-10"},{"uniquename":"PMID:29779879","title":"The XMAP215 Ortholog Alp14 Promotes Microtubule Nucleation in Fission Yeast.","citation":"Curr Biol 2018 Jun 04;28(11):1681-1691.e4","abstract":"The organization and number of microtubules (MTs) in a cell depend on the proper regulation of MT nucleation. Currently, the mechanism of nucleation is the most poorly understood aspect of MT dynamics. XMAP215/chTOG/Alp14/Stu2 proteins are MT polymerases that stimulate MT polymerization at MT plus ends by binding and releasing tubulin dimers. Although these proteins also localize to MT organizing centers and have nucleating activity in vitro, it is not yet clear whether these proteins participate in MT nucleation in vivo. Here, we demonstrate that in the fission yeast Schizosaccharomyces pombe, the XMAP215 ortholog Alp14 is critical for efficient MT nucleation in vivo. In multiple assays, loss of Alp14 function led to reduced nucleation rate and numbers of interphase MT bundles. Conversely, activation of Alp14 led to increased nucleation frequency. Alp14 associated with Mto1 and γ-tubulin complex components, and artificially targeting Alp14 to the γ-tubulin ring complexes (γ-TuRCs) stimulated nucleation. In imaging individual nucleation events, we found that Alp14 transiently associated with a γ-tubulin particle shortly before the appearance of a new MT. The transforming acidic coiled-coil (TACC) ortholog Alp7 mediated the localization of Alp14 at nucleation sites but not plus ends, and was required for efficient nucleation but not for MT polymerization. Our findings provide the strongest evidence to date that Alp14 serves as a critical MT nucleation factor in vivo. We suggest a model in which Alp14 associates with the γ-tubulin complex in an Alp7-dependent manner to facilitate the assembly or stabilization of the nascent MT.","doi":"10.1016/j.cub.2018.04.008","authors":"Flor-Parra I, Iglesias-Romero AB, Chang F","authors_abbrev":"Flor-Parra I et al.","pubmed_publication_date":"04 Jun 2018","pubmed_entrez_date":"2018-05-22","publication_year":"2018","canto_session_key":"bdd935d25d2c0b9d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-05-23 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC365.15","SPCC895.07","SPCC417.07c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:22098069","title":"Identification of a galactose-specific flocculin essential for non-sexual flocculation and filamentous growth in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2011 Dec;82(6):1531-44","abstract":"Although various mutant strains of the fission yeast Schizosaccharomyces pombe exhibit non-sexual flocculation, little is known about the mechanistic basis for this phenomenon, nor have genes encoding the implicated flocculin been identified. In the budding yeast Saccharomyces cerevisiae, the transcription factor Flo8 controls expression of some of the genes involved in non-sexual flocculation. We have found that overexpression of S. cerevisiae FLO8 induced non-sexual flocculation in S. pombe. This non-sexual flocculation was Ca(2+) -dependent, and was inhibited by addition of galactose, but not by mannose, glucose or sucrose. In the FLO8-overexpressing strain, a gene designated gsf2(+) (galactose-specific flocculation) was specifically induced. The gsf2(+) gene was also highly expressed in lkh1Δ, tup12Δ and gsf1 mutants, all of which exhibited non-sexual flocculation dependent on gsf2(+) . We show that the N-terminal region of Gsf2 recognizes galactose in mediating cell-cell interaction. Disruption of gsf2(+) also abolished the adhesion phenotype and invasive growth of the wild-type strain cultured in low ammonium medium. The newly identified flocculin Gsf2 in fission yeast was not only required for non-sexual flocculation but was also required for adhesion and filamentous growth through recognition of galactose residues on cell surface glycoconjugates.","doi":"10.1111/j.1365-2958.2011.07908.x","authors":"Matsuzawa T, Morita T, Tanaka N, Tohda H, Takegawa K","authors_abbrev":"Matsuzawa T et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-11-22","publication_year":"2011","canto_session_key":"c381c274e0743264","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-04-28 17:20:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-17 11:17:03","canto_added_date":"2012-02-17 18:45:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.11c","SPAC630.14c","SPCC1742.01","SPAC8F11.10c","SPCC1795.03","SPBC1D7.02c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2012-09-17"},{"uniquename":"PMID:21516229","title":"Mapping Post-translational Modifications of Histones H2A, H2B and H4 in Schizosaccharomyces pombe.","citation":"Int J Mass Spectrom 2011 Mar 30;301(1-3):159-165","abstract":"Core histones are known to carry a variety of post-translational modifications (PTMs), including acetylation, phosphorylation, methylation and ubiquitination, which play important roles in the epigenetic control of gene expression. The nature and biological functions of these PTMs in histones from plants, animals and budding yeast have been extensively investigated. In contrast, the corresponding studies for fission yeast were mainly focused on histone H3. In the present study, we applied LC-nano-ESI-MS/MS, coupled with multiple protease digestion, to identify PTMs in histones H2A, H2B and H4 from Schizosaccharomyces pombe (S. pombe), the typical model organism of fission yeast. Various protease digestions provided high sequence coverage for PTM mapping, and accurate mass measurement of fragment ions allowed for unambiguous differentiation of acetylation from tri-methylation. Many modification sites conserved in other organisms were identified in S. pombe. In addition, some unique modification sites, including N-terminal acetylation in H2A and H2B as well as K123 acetylation in H2A.β, were observed. Our results provide a comprehensive picture of the PTMs of histones H2A, H2B and H4 in S. pombe, which serves as a foundation for future investigations on the regulation and functions of histone modifications in this important model organism.","authors":"Xiong L, Wang Y","authors_abbrev":"Xiong L et al.","pubmed_publication_date":"30 Mar 2011","pubmed_entrez_date":"2011-04-26","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24766403","title":"Mudi, a web tool for identifying mutations by bioinformatics analysis of whole-genome sequence.","citation":"Genes Cells 2014 Jun;19(6):517-27","abstract":"In forward genetics, identification of mutations is a time-consuming and laborious process. Modern whole-genome sequencing, coupled with bioinformatics analysis, has enabled fast and cost-effective mutation identification. However, for many experimental researchers, bioinformatics analysis is still a difficult aspect of whole-genome sequencing. To address this issue, we developed a browser-accessible and easy-to-use bioinformatics tool called Mutation discovery (Mudi; http://naoii.nig.ac.jp/mudi_top.html), which enables 'one-click' identification of causative mutations from whole-genome sequence data. In this study, we optimized Mudi for pooled-linkage analysis aimed at identifying mutants in yeast model systems. After raw sequencing data are uploaded, Mudi performs sequential analysis, including mapping, detection of variant alleles, filtering and removal of background polymorphisms, prioritization, and annotation. In an example study of suppressor mutants of ptr1-1 in the fission yeast Schizosaccharomyces pombe, pooled-linkage analysis with Mudi identified mip1(+) , a component of Target of Rapamycin Complex 1 (TORC1), as a novel component involved in RNA interference (RNAi)-related cell-cycle control. The accessibility of Mudi will accelerate systematic mutation analysis in forward genetics.","doi":"10.1111/gtc.12151","authors":"Iida N, Yamao F, Nakamura Y, Iida T","authors_abbrev":"Iida N et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-04-29","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A7.11","SPCC736.11","SPAC19D5.04"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:19335451","title":"Intracellular nanosurgery and cell enucleation using a picosecond laser.","citation":"J Microsc 2009 Apr;234(1):1-8","abstract":"Living cells are highly organized in space and time, which makes spatially and temporally confined manipulations an indispensable tool in cell biology. Laser-based nanosurgery is an elegant method that allows precise ablation of intracellular structures. Here, we show cutting of fluorescently labelled microtubules and mitotic spindles in fission yeast, performed with a picosecond laser coupled to a confocal microscope. Diverse effects from photo-bleaching to partial and complete breakage are obtained by varying the exposure time, while simultaneously imaging the structures of interest. Using this system we developed an efficient technique to generate enucleated cells without perturbing the distribution of other organelles. This enucleation method can be used to study the cytoskeleton in a nucleus-free environment, as well as the role of the nucleus in cell growth and a variety of cellular functions.","doi":"10.1111/j.1365-2818.2009.03142.x","authors":"Raabe I, Vogel SK, Peychl J, Tolić-Nørrelykke IM","authors_abbrev":"Raabe I et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-04-02","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10214922","title":"DNA structure checkpoint pathways in Schizosaccharomyces pombe.","citation":"Biochimie 1999;81(1-2):173-81","abstract":"The response to DNA damage includes a delay to progression through the cell cycle to aid DNA repair. Incorrectly replicated chromosomes (replication checkpoint) or DNA damage (DNA damage checkpoint) delay the onset of mitosis. These checkpoint pathways detect DNA perturbations and generate a signal. The signal is amplified and transmitted to the cell cycle machinery. Since the checkpoint pathways are essential for genome stability, the related proteins which are found in all eukaryotes (from yeast to mammals) are expected to have similar functions to the yeast progenitors. This review article focuses on the function of checkpoint proteins in the model system Schizosaccharomyces pombe. Checkpoint controls in Saccharomyces cerevisiae and mammalian cells are mentioned briefly to underscore common or diverse features.","authors":"Caspari T, Carr AM","authors_abbrev":"Caspari T et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-04-24","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10471700","title":"Meiotic chromosome dynamics dependent upon the rec8(+), rec10(+) and rec11(+) genes of the fission yeast Schizosaccharomyces pombe.","citation":"Genetics 1999 Sep;153(1):57-68","abstract":"During meiosis homologous chromosomes replicate once, pair, experience recombination, and undergo two rounds of segregation to produce haploid meiotic products. The rec8(+), rec10(+), and rec11(+) genes of the fission yeast Schizosaccharomyces pombe exhibit similar specificities for meiotic recombination and rec8(+) is required for sister chromatid cohesion and homolog pairing. We applied cytological and genetic approaches to identify potential genetic interactions and to gauge the fidelity of meiotic chromosome segregation in the mutants. The rec8(+) gene was epistatic to rec10(+) and to rec11(+), but there was no clear epistatic relationship between rec10(+) and rec11(+). Reciprocal (crossover) recombination in the central regions of all three chromosomes was compromised in the rec mutants, but recombination near the telomeres was nearly normal. Each of the mutants also exhibited a high rate of aberrant segregation for all three chromosomes. The rec8 mutations affected mainly meiosis I segregation. Remarkably, the rec10 and rec11 mutations, which compromised recombination during meiosis I, affected mainly meiosis II segregation. We propose that these genes encode regulators or components of a \"meiotic chromatid cohesion\" pathway involved in establishing, maintaining, and appropriately releasing meiotic interactions between chromosomes. A model of synergistic interactions between sister chromatid cohesion and crossover position suggests how crossovers and cohesion help ensure the proper segregation of chromosomes in each of the meiotic divisions.","authors":"Krawchuk MD, DeVeaux LC, Wahls WP","authors_abbrev":"Krawchuk MD et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-09-03","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10388806","title":"Rereplication phenomenon in fission yeast requires MCM proteins and other S phase genes.","citation":"Genetics 1999 Jul;152(3):839-51","abstract":"The fission yeast Schizosaccharomyces pombe can be induced to perform multiple rounds of DNA replication without intervening mitoses by manipulating the activity of the cyclin-dependent kinase p34(cdc2). We have examined the role in this abnormal rereplication of a large panel of genes known to be involved in normal S phase. The genes analyzed can be grouped into four classes: (1) those that have no effect on rereplication, (2) others that delay DNA accumulation, (3) several that allow a gradual increase in DNA content but not in genome equivalents, and finally, (4) mutations that completely block rereplication. The rereplication induced by overexpression of the CDK inhibitor Rum1p or depletion of the Cdc13p cyclin is essentially the same and requires the activity of two minor B-type cyclins, cig1(+) and cig2(+). In particular, the level, composition, and localization of the MCM protein complex does not alter during rereplication. Thus rereplication in fission yeast mimics the DNA synthesis of normal S phase, and the inability to rereplicate provides an excellent assay for novel S-phase mutants.","authors":"Snaith HA, Forsburg SL","authors_abbrev":"Snaith HA et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-02","publication_year":"1999","canto_session_key":"a64fc9a5b004423d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-01-19 13:09:16","canto_approved_date":"2021-12-13 18:03:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-08-24 15:37:29","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":61,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPBC4.04c","SPAC23C4.18c","SPBC336.12c","SPAPB2B4.03","SPCC16A11.17","SPAC8F11.07c","SPAC27E2.05","SPAC1B2.05","SPBC14C8.07c","SPBC32F12.09","SPBC29A10.15","SPAC20G8.01","SPAC3H5.06c","SPBC211.04c","SPBC1347.10","SPCC4E9.02","SPBC336.04","SPBC582.03"],"gene_count":19,"ltp_gene_count":17,"approved_date":"2016-01-19"},{"uniquename":"PMID:7615134","title":"Antifungal activity of Aplysianin E, a cytotoxic protein of sea hare (Aplysia kurodai) eggs.","citation":"Dev Comp Immunol 1995;19(1):13-9","abstract":"We observed for the first time that antifungal activity was exhibited by Aplysianin E (AKE), an antineoplastic and antibacterial glycoprotein purified from the eggs of Aplysia kurodai. AKE completely suppressed growth of the yeast form fungi, Saccharomyces cerevisiae A 5 8 1 A, Schizosaccharomyces pombe JY 1 and Candida albicans ATCC 36232 at a concentration of over 16 micrograms/mL. The colony-forming abilities of the fungi were also significantly decreased after contact with AKE. These results indicate that AKE has an antifungal property and that its mode of action is fungicidal.","authors":"Iijima R, Kisugi J, Yamazaki M","authors_abbrev":"Iijima R et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20462492","title":"The Prp19 WD40 domain contains a conserved protein interaction region essential for its function.","citation":"Structure 2010 May 12;18(5):584-93","abstract":"Prp19 is a member of the WD40 repeat family of E3 ubiquitin ligases and a conserved eukaryotic RNA splicing factor essential for activation and stabilization of the spliceosome. To understand the role of the WD40 repeat domain of Prp19 we have determined its structure using X-ray crystallography. The domain has a distorted seven bladed WD40 architecture with significant asymmetry due to irregular packing of blades one and seven into the core of the WD40 domain. Structure-based mutagenesis identified a highly conserved surface centered around blade five that is required for the physical interaction between Prp19 and Cwc2, another essential splicing factor. This region is found to be required for Prp19 function and yeast viability. Experiments in vitro and in vivo demonstrate that two molecules of Cwc2 bind to the Prp19 tetramer. These coupled structural and functional studies provide a model for the functional architecture of Prp19.","doi":"10.1016/j.str.2010.02.015","authors":"Vander Kooi CW, Ren L, Xu P, Ohi MD, Gould KL, Chazin WJ","authors_abbrev":"Vander Kooi CW et al.","pubmed_publication_date":"12 May 2010","pubmed_entrez_date":"2010-05-14","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:19:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.12","SPAC29A4.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:18793196","title":"The spindle pole body plays a key role in controlling mitotic commitment in the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 2008 Oct;36(Pt 5):1097-101","abstract":"Commitment to mitosis is regulated by a conserved protein kinase complex called MPF (mitosis-promoting factor). MPF activation triggers a positive-feedback loop that further promotes the activity of its activating phosphatase Cdc25 and is assumed to down-regulate the MPF-inhibitory kinase Wee1. Four protein kinases contribute to this amplification loop: MPF itself, Polo kinase, MAPK (mitogen-activated protein kinase) and Greatwall kinase. The fission yeast SPB (spindle pole body) component Cut12 plays a critical role in modulating mitotic commitment. In this review, I discuss the relationship between Cut12 and the fission yeast Polo kinase Plo1 in mitotic control. These results indicate that commitment to mitosis is co-ordinated by control networks on the spindle pole. I then describe how the Cut12/Plo1 control network links growth control signalling from TOR (target of rapamycin) and MAPK networks to the activation of MPF to regulate the timing of cell division.","doi":"10.1042/BST0361097","authors":"Hagan IM","authors_abbrev":"Hagan IM","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-09-17","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28636937","title":"The Conserved RNA Binding Cyclophilin, Rct1, Regulates Small RNA Biogenesis and Splicing Independent of Heterochromatin Assembly.","citation":"Cell Rep 2017 Jun 20;19(12):2477-2489","abstract":"RNAi factors and their catalytic activities are essential for heterochromatin assembly in S. pombe. This has led to the idea that siRNAs can promote H3K9 methylation by recruiting the cryptic loci regulator complex (CLRC), also known as recombination in K complex (RIKC), to the nucleation site. The conserved RNA-binding protein Rct1 (AtCyp59/SIG-7) interacts with splicing factors and RNA polymerase II. Here we show that Rct1 promotes processing of pericentromeric transcripts into siRNAs via the RNA recognition motif. Surprisingly, loss of siRNA in rct1 mutants has no effect on H3K9 di- or tri-methylation, resembling other splicing mutants, suggesting that post-transcriptional gene silencing per se is not required to maintain heterochromatin. Splicing of the Argonaute gene is also defective in rct1 mutants and contributes to loss of silencing but not to loss of siRNA. Our results suggest that Rct1 guides transcripts to the RNAi machinery by promoting splicing of elongating non-coding transcripts.","doi":"10.1016/j.celrep.2017.05.086","authors":"Chang AY, Castel SE, Ernst E, Kim HS, Martienssen RA","authors_abbrev":"Chang AY et al.","pubmed_publication_date":"20 Jun 2017","pubmed_entrez_date":"2017-06-22","publication_year":"2017","canto_session_key":"67a8c4d1671a4f88","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-06-23 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F3.01","SPBC800.03","SPBC17G9.05","SPBC1D7.04","SPCC736.11"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:1769560","title":"A constitutive, heat shock-activated neutral trehalase occurs in Schizosaccharomyces pombe in addition to the sporulation-specific acid trehalase.","citation":"FEMS Microbiol Lett 1991 Nov 01;68(1):85-90","abstract":"Trehalase was studied in Schizosaccharomyces pombe cells growing vegetatively on minimal medium and in sporulating cultures. Acid trehalase activity, measured at pH 4.2, was absent in vegetative cells and occurred only in asci, indicating that this activity represented the sporulation-specific trehalase reported previously. In contrast, neutral trehalase, measured at pH 6.0, was constitutively present in vegetative cells during the exponential and stationary growth phase as well as in asci. In vegetative cells, neutral trehalase did not sediment with cell walls, suggesting a cytoplasmic localization. Its activity increased ten-fold when growing cells were subjected to heat treatment of 2 h. Neutral trehalase from heat-treated cells had a pH optimum of 6.0 and was almost completely inhibited by 3 mM ZnCl2. Acid trehalase activity could be measured in intact asci, indicating that it is localized in the ascus cell walls, while neutral trehalase was not detectable in intact asci and appeared to be present primarily in the walls of ascospores and in the ascus epiplasm.","authors":"De Virgilio C, Müller J, Boller T, Wiemken A","authors_abbrev":"De Virgilio C et al.","pubmed_publication_date":"01 Nov 1991","pubmed_entrez_date":"1991-11-01","publication_year":"1991","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38099423","title":"Engineering heterothallic strains in fission yeast.","citation":"Yeast 2023 Dec 15;","abstract":"In poor nitrogen conditions, fission yeast cells mate, undergo meiosis and form spores that are resistant to deleterious environments. Natural isolates of Schizosaccharomyces pombe are homothallic. This allows them to naturally switch between the two h- and h+ mating types with a high frequency, thereby ensuring the presence of both mating partners in a population of cells. However, alteration of the mating type locus can abolish mating type switching or reduce it to a very low frequency. Such heterothallic strains have been isolated and are common in research laboratories due to the simplicity of their use for Mendelian genetics. In addition to the standard laboratory strains, a large collection of natural S. pombe isolates is now available, representing a powerful resource for investigating the genetic diversity and biology of fission yeast. However, most of these strains are homothallic, and only tedious or mutagenic strategies have been described to obtain heterothallic cells from a homothallic parent. Here, we describe a simple approach to generate heterothallic strains. It takes advantage of an alteration of the mating type locus that was previously identified in a mating type switching-deficient strain and the CRISPR-Cas9 editing tool, allowing for a one-step engineering of heterothallic cells with high efficiency.","doi":"10.1002/yea.3914","authors":"García-Ruano D, Hsu I, Leray B, Billard B, Liti G, Coudreuse D","authors_abbrev":"García-Ruano D et al.","pubmed_publication_date":"15 Dec 2023","pubmed_entrez_date":"2023-12-15","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-12-16 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22375062","title":"Plo1 phosphorylates Dam1 to promote chromosome bi-orientation in fission yeast.","citation":"J Cell Sci 2012 Apr 01;125(Pt 7):1645-51","abstract":"The fungal-specific heterodecameric outer kinetochore DASH complex facilitates the interaction of kinetochores with spindle microtubules. In budding yeast, where kinetochores bind a single microtubule, the DASH complex is essential, and phosphorylation of Dam1 by the Aurora kinase homologue, Ipl1, causes detachment of kinetochores from spindle microtubules. We demonstrate that in the distantly related fission yeast, where the DASH complex is not essential for viability and kinetochores bind multiple microtubules, Dam1 is instead phosphorylated on serine 143 by the Polo kinase homologue, Plo1, during prometaphase and metaphase. This phosphorylation site is conserved in most fungal Dam1 proteins, including budding yeast Dam1. We show that Dam1 phosphorylation by Plo1 is dispensable for DASH assembly and chromosome retrieval but instead aids tension-dependent chromosome bi-orientation.","doi":"10.1242/jcs.096826","authors":"Buttrick GJ, Lancaster TC, Meadows JC, Millar JB","authors_abbrev":"Buttrick GJ et al.","pubmed_publication_date":"01 Apr 2012","pubmed_entrez_date":"2012-03-01","publication_year":"2012","canto_session_key":"caf685fa8d7a836f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-11 16:49:30","canto_approved_date":"2022-02-02 17:51:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-10 11:54:36","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":48,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPAC19E9.02","SPCC1795.01c","SPBC32F12.08c","SPBC2F12.13","SPAC14C4.16","SPCC1223.15c","SPBC776.02c","SPBC26H8.07c","SPBC16H5.07c","SPBC3B9.22c","SPCC1322.12c","SPAC1805.07c","SPBC106.01","SPCC417.02","SPAC589.08c","SPAC8C9.17c","SPBC20F10.06","SPAC16A10.05c","SPAC1782.09c","SPCC320.13c","SPBC27.02c"],"gene_count":22,"ltp_gene_count":17,"approved_date":"2017-01-11"},{"uniquename":"PMID:28976798","title":"Conserved and unique features of the fission yeast core Atg1 complex.","citation":"Autophagy 2017;13(12):2018-2027","abstract":"Although the human ULK complex mediates phagophore initiation similar to the budding yeast Saccharomyces cerevisiae Atg1 complex, this complex contains ATG101 but not Atg29 and Atg31. Here, we analyzed the fission yeast Schizosaccharomyces pombe Atg1 complex, which has a subunit composition that resembles the human ULK complex. Our pairwise coprecipitation experiments showed that while the interactions between Atg1, Atg13, and Atg17 are conserved, Atg101 does not bind Atg17. Instead, Atg101 interacts with the HORMA domain of Atg13 and this enhances the stability of both proteins. We also found that S. pombe Atg17, the putative scaffold subunit, adopts a rod-shaped structure with no discernible curvature. Interestingly, S. pombe Atg17 binds S. cerevisiae Atg13, Atg29, and Atg31 in vitro, but it cannot complement the function of S. cerevisiae Atg17 in vivo. Furthermore, S. pombe Atg101 cannot substitute for the function of S. cerevisiae Atg29 and Atg31 in vivo. Collectively, our work generates new insights into the subunit organization and structural properties of an Atg101-containing Atg1/ULK complex.","doi":"10.1080/15548627.2017.1382782","authors":"Nanji T, Liu X, Chew LH, Li FK, Biswas M, Yu ZQ, Lu S, Dong MQ, Du LL, Klionsky DJ, Yip CK","authors_abbrev":"Nanji T et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-10-05","publication_year":"2017","canto_session_key":"8d0ac74703887de6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Calvin Yip","canto_first_approved_date":"2017-12-19 19:19:22","canto_approved_date":"2018-03-23 15:29:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-12-18 23:24:12","canto_added_date":"2017-10-06 00:15:14","annotation_curators":[{"name":"Calvin Yip","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC10F6.11c","SPAC25H1.03","SPCC63.08c","SPAC4F10.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-12-19"},{"uniquename":"PMID:29549582","title":"The conserved histone variant H2A.Z illuminates meiotic recombination initiation.","citation":"Curr Genet 2018 Oct;64(5):1015-1019","abstract":"Meiotic recombination ensures faithful chromosome segregation and confers genetic diversity to gametes, and thus, is a key DNA-templated reaction not only for sexual reproduction, but also evolution. This recombination is initiated by programmed DNA double strand breaks (DSBs), which are mainly formed at recombination hotspots. As meiotic DSB formation requires multiple proteins, it is regulated by chromatin structure. In particular, DSB occurs in a higher-order chromatin architecture termed \"axis-loop\", in which many loops protrude from proteinaceous axis. Previous studies have suggested that assembly of this structure is dependent on chromatin binding of cohesin, which in turn recruits proteins implicated in DSB formation. However, roles of chromatin in meiotic DSB formation are not fully characterized. This review article summarizes our recent report showing that the conserved histone H2A variant H2A.Z promotes meiotic DSB formation in fission yeast. Through a series of experiments, we found that, in H2A.Z-lacking mutants, multiple proteins involved in DSB formation, but not cohesin subunits, are less associated with chromatin. Strikingly, nuclei were more compact in the absence of H2A.Z. These observations led us to propose that fission yeast H2A.Z promotes meiotic DSB formation partly through modulating chromosome architecture to enhance interaction between DSB-related proteins and cohesin-loaded chromatin. In addition, biological implications of our findings are discussed, and their relevance to DSB formation in other species as well as to other DNA-related events are also provided.","doi":"10.1007/s00294-018-0825-9","authors":"Yamada S, Kugou K, Ding DQ, Fujita Y, Hiraoka Y, Murakami H, Ohta K, Yamada T","authors_abbrev":"Yamada S et al.","pubmed_publication_date":"Oct 2018","pubmed_entrez_date":"2018-03-18","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-03-21 01:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23874965","title":"Distal and proximal actions of peptide pheromone M-factor control different conjugation steps in fission yeast.","citation":"PLoS One 2013;8(7):e69491","abstract":"Mating pheromone signaling is essential for conjugation between haploid cells of P-type (P-cells) and haploid cells of M-type (M-cells) in Schizosaccharomyces pombe. A peptide pheromone, M-factor, produced by M-cells is recognized by the receptor of P-cells. An M-factor-less mutant, in which the M-factor-encoding genes are deleted, is completely sterile. In liquid culture, sexual agglutination was not observed in the mutant, but it could be recovered by adding exogenous synthetic M-factor, which stimulated expression of the P-type-specific cell adhesion protein, Map4. Exogenous M-factor, however, failed to recover the cell fusion defect in the M-factor-less mutant. When M-factor-less cells were added to a mixture of wild-type P- and M-cells, marked cell aggregates were formed. Notably, M-factor-less mutant cells were also incorporated in these aggregates. In this mixed culture, P-cells conjugated preferentially with M-cells secreting M-factor, and rarely with M-factor-less M-cells. The kinetics of mating parameters in liquid culture revealed that polarized growth commenced from the contact region of opposite mating-type cells. Taken together, these findings indicate that M-factor at a low concentration induces adhesin expression, leading to initial cell-cell adhesion in a type of \"distal pheromone action\", but M-factor that is secreted directly in the proximity of the adhered P-cells may be necessary for cell fusion in a type of \"proximal pheromone action\".","doi":"10.1371/journal.pone.0069491","authors":"Seike T, Nakamura T, Shimoda C","authors_abbrev":"Seike T et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-23","publication_year":"2013","canto_session_key":"d2faca3e7a62644a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22559741","title":"A conserved histone deacetylase with a role in the regulation of cytokinesis in Schizosaccharomyces pombe.","citation":"Cell Div 2012 May 04;7(1):13","abstract":"In Schizosaccharomyces pombe the SET domain protein, Set3p - together with its interacting partners, Snt1p, and Hif2p - form a complex that aids in preventing cell division failure upon mild cytokinetic stress. Intriguingly, the human orthologs of these proteins (MLL5, NCOR2, and TBL1X) are also important for the faithful completion of cytokinesis in tissue culture cells. Since MLL5, NCOR2, and TBL1X form a complex with the histone deacetylase, HDAC3, we sought to determine if an orthologous counterpart played a regulatory role in fission yeast cytokinesis.\nIn this report we identify the hos2 gene as the fission yeast HDAC3 ortholog. We show that Hos2p physically interacts with Set3p, Snt1p, and Hif2p, and that hos2∆ mutants are indeed compromised in their ability to reliably complete cell division in the presence of mild cytokinetic stresses. Furthermore, we demonstrate that over-expression of hos2 causes severe morphological and cytokinetic defects. Lastly, through recombinase mediated cassette exchange, we show that expression of human HDAC3 complements the cytokinetic defects exhibited by hos2∆ cells.\nThese data support a model in which Hos2p functions as an essential component of the Set3p-Snt1p-Hif2p complex with respect to the regulation of cytokinesis. The ability of human HDAC3 to complement the cytokinesis defects associated with the deletion of the hos2 gene suggests that further analysis of this system could provide insight into the role of HDAC3 in both the regulation of cell division, as well as other biological processes influenced by HDAC3 deacetylation.","doi":"10.1186/1747-1028-7-13","authors":"Grewal C, Hickmott J, Rentas S, Karagiannis J","authors_abbrev":"Grewal C et al.","pubmed_publication_date":"04 May 2012","pubmed_entrez_date":"2012-05-08","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G9.07c","SPAC1782.09c","SPAC22E12.19","SPCC16C4.01","SPAC20G8.05c","SPCC1235.09","SPAC22E12.11c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:6082328","title":"Cellular growth rates of the fission yeast. Schizosaccharomyces pombe, and variable sensitivity to 2-deoxyglucose.","citation":"Exp Cell Res 1967 Dec;48(3):618-20","abstract":"","authors":"Johnson BF, Rupert CM","authors_abbrev":"Johnson BF et al.","pubmed_publication_date":"Dec 1967","pubmed_entrez_date":"1967-12-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9872989","title":"Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex.","citation":"J Biol Chem 1999 Jan 08;274(2):567-70","abstract":"DNA damage activates cell cycle checkpoints in yeast and human cells. In the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe checkpoint-deficient mutants have been characterized, and the corresponding genes have been cloned. Searches for human homologs of S. pombe rad1, rad9, and hus1 genes identified the potential human homologs hRad1, hRad9, and hHus1; however, little is known about the roles of these proteins in human cells. The present studies demonstrate that hRad1 and hHus1 associate in a complex that interacts with a highly modified form of hRad9, but hHus1 and hRad1 do not associate with hRad17. In addition to being a key participant in complex formation, hRad9 is phosphorylated in response to DNA damage. Together, these results suggest that hRad9, hRad1, and hHus1 are central components of a DNA damage-responsive protein complex in human cells.","authors":"Volkmer E, Karnitz LM","authors_abbrev":"Volkmer E et al.","pubmed_publication_date":"08 Jan 1999","pubmed_entrez_date":"1999-01-05","publication_year":"1999","canto_session_key":"4a66d253b038fc5f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-07 17:08:03","canto_approved_date":"2019-11-07 17:08:03","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-07 17:07:56","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-11-07"},{"uniquename":"EMBL:SPTRX2","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24165938","title":"Extracellular cell wall β(1,3)glucan is required to couple septation to actomyosin ring contraction.","citation":"J Cell Biol 2013 Oct 28;203(2):265-82","abstract":"Cytokinesis has been extensively studied in different models, but the role of the extracellular cell wall is less understood. Here we studied this process in fission yeast. The essential protein Bgs4 synthesizes the main cell wall β(1,3)glucan. We show that Bgs4-derived β(1,3)glucan is required for correct and stable actomyosin ring positioning in the cell middle, before the start of septum formation and anchorage to the cell wall. Consequently, β(1,3)glucan loss generated ring sliding, oblique positioned rings and septa, misdirected septum synthesis indicative of relaxed rings, and uncoupling between a fast ring and membrane ingression and slow septum synthesis, suggesting that cytokinesis can progress with defective septum pushing and/or ring pulling forces. Moreover, Bgs4-derived β(1,3)glucan is essential for secondary septum formation and correct primary septum completion. Therefore, our results show that extracellular β(1,3)glucan is required for cytokinesis to connect the cell wall with the plasma membrane and for contractile ring function, as proposed for the equivalent extracellular matrix in animal cells.","doi":"10.1083/jcb.201304132","authors":"Muñoz J, Cortés JC, Sipiczki M, Ramos M, Clemente-Ramos JA, Moreno MB, Martins IM, Pérez P, Ribas JC","authors_abbrev":"Muñoz J et al.","pubmed_publication_date":"28 Oct 2013","pubmed_entrez_date":"2013-10-30","publication_year":"2013","canto_session_key":"aa2040ae8297ad5b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juan Carlos Ribas","canto_first_approved_date":"2018-03-16 13:51:22","canto_approved_date":"2022-03-28 16:41:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-04 09:48:09","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Juan Carlos Ribas","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.02c","SPBC19G7.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-16"},{"uniquename":"PMID:42270273","title":"Interaction between Zygosaccharomyces bailii and Schizosaccharomyces pombe enhances acetic acid reduction in Baijiu fermentation.","citation":"Food Res Int 2026 Sep 01;239:119566","abstract":"Acetic acid is a crucial organic acid in the production of sauce-flavored Baijiu, influencing microbial succession during fermentation. Nevertheless, excessive concentrations of acetic acid can inhibit the growth and metabolism of microorganisms. Consequently, elucidating the microbial interactions under acidic stress is vital. Our study demonstrates that industrial-scale fortification with a defined four-strain yeast consortium significantly reduces acetic acid by 21.9% at the end of heap fermentation and improves starch utilization efficiency and ethanol yield. By employing a cell-contact-free dual-chamber system, this study reveals a synergistic effect on acetic acid reduction during the co-cultivation of Z. bailii and S. pombe. Comparative transcriptomics shows pronounced gene enrichment in the glyoxylate cycle of Z. bailii. The residual acetic acid content was 48.5% higher in the co-cultures involving an MLS1 gene deletion strain of Z. bailii with S. pombe compared to co-cultures with the wild-type Z. bailii, suggesting that the synergistic reduction in acetic acid is likely mediated through upregulation of the MLS1 gene in Z. bailii. This study elucidates the mechanism by which yeast interactions drive acetic acid reduction, offering potential guidance for optimizing acetic acid utilization.","doi":"10.1016/j.foodres.2026.119566","authors":"Yuan S, Yun Y, Liu Z, Xing S, Du J, Liu Q, He M, Guo J, Lin L, Zhang C","authors_abbrev":"Yuan S et al.","pubmed_publication_date":"01 Sep 2026","pubmed_entrez_date":"2026-06-10","publication_year":"2026","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2026-06-11 23:25:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27730285","title":"Big data mining powers fungal research: recent advances in fission yeast systems biology approaches.","citation":"Curr Genet 2017 Jun;63(3):427-433","abstract":"Biology research has entered into big data era. Systems biology approaches therefore become the powerful tools to obtain the whole landscape of how cell separate, grow, and resist the stresses. Fission yeast Schizosaccharomyces pombe is wonderful unicellular eukaryote model, especially studying its division and metabolism can facilitate to understanding the molecular mechanism of cancer and discovering anticancer agents. In this perspective, we discuss the recent advanced fission yeast systems biology tools, mainly focus on metabolomics profiling and metabolic modeling, protein-protein interactome and genetic interaction network, DNA sequencing and applications, and high-throughput phenotypic screening. We therefore hope this review can be useful for interested fungal researchers as well as bioformaticians.","doi":"10.1007/s00294-016-0657-4","authors":"Wang Z","authors_abbrev":"Wang Z","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2016-10-13","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-10-14 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30928696","title":"Distinct Roles of Myosin-II Isoforms in Cytokinesis under Normal and Stressed Conditions.","citation":"iScience 2019 Apr 26;14:69-87","abstract":"To address the question of why more than one myosin-II isoform is expressed in a single cell to drive cytokinesis, we analyzed the roles of the myosin-II isoforms, Myo2 and Myp2, of the fission yeast Schizosaccharomyces pombe, in cytokinesis under normal and stressed conditions. We found that Myp2 controls the disassembly, stability, and constriction initiation of the Myo2 ring in response to high-salt stress. A C-terminal coiled-coil domain of Myp2 is required for its immobility and contractility during cytokinesis, and when fused to the tail of the dynamic Myo2, renders the chimera the low-turnover property. We also found, by following distinct processes in real time at the single-cell level, that Myo2 and Myp2 are differentially required but collectively essential for guiding extracellular matrix remodeling during cytokinesis. These results suggest that the dynamic and immobile myosin-II isoforms are evolved to carry out cytokinesis with robustness under different growth conditions.","doi":"10.1016/j.isci.2019.03.014","authors":"Okada H, Wloka C, Wu JQ, Bi E","authors_abbrev":"Okada H et al.","pubmed_publication_date":"26 Apr 2019","pubmed_entrez_date":"2019-04-01","publication_year":"2019","canto_session_key":"f7e61f1bbab2a27b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Okada, Hiroki","canto_first_approved_date":"2019-05-02 15:30:41","canto_approved_date":"2024-03-29 12:48:58","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-04-17 18:25:12","canto_added_date":"2019-04-02 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Okada, Hiroki","community_curator":true,"annotation_count":42,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08","SPBC19G7.05c","SPBC2D10.14c","SPAC4A8.05c","SPCC645.05c","SPCC1739.11c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2019-05-02"},{"uniquename":"PMID:14576344","title":"Cytoplasmic dynein in fungi: insights from nuclear migration.","citation":"J Cell Sci 2003 Nov 15;116(Pt 22):4501-12","abstract":"Cytoplasmic dynein is a microtubule motor that mediates various biological processes, including nuclear migration and organelle transport, by moving on microtubules while associated with various cellular structures. The association of dynein with cellular structures and the activation of its motility are crucial steps in dynein-dependent processes. However, the mechanisms involved remain largely unknown. In fungi, dynein is required for nuclear migration. In budding yeast, nuclear migration is driven by the interaction of astral microtubules with the cell cortex; the interaction is mediated by dynein that is probably associated with the cortex. Recent studies suggest that budding yeast dynein is first recruited to microtubules, then delivered to the cortex by microtubules and finally activated by association with the cortex. Nuclear migration in many other fungi is probably driven by a similar mechanism. Recruitment of dynein to microtubules and its subsequent activation upon association with cellular structures are perhaps common to many dynein-dependent eukaryotic processes, including organelle transport.","authors":"Yamamoto A, Hiraoka Y","authors_abbrev":"Yamamoto A et al.","pubmed_publication_date":"15 Nov 2003","pubmed_entrez_date":"2003-10-25","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:11:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12840006","title":"Xenopus origin recognition complex (ORC) initiates DNA replication preferentially at sequences targeted by Schizosaccharomyces pombe ORC.","citation":"EMBO J 2003 Jul 01;22(13):3441-50","abstract":"Budding yeast (Saccharomyces cerevisiae) origin recognition complex (ORC) requires ATP to bind specific DNA sequences, whereas fission yeast (Schizosaccharomyces pombe) ORC binds to specific, asymmetric A:T-rich sites within replication origins, independently of ATP, and frog (Xenopus laevis) ORC seems to bind DNA non-specifically. Here we show that despite these differences, ORCs are functionally conserved. Firstly, SpOrc1, SpOrc4 and SpOrc5, like those from other eukaryotes, bound ATP and exhibited ATPase activity, suggesting that ATP is required for pre-replication complex (pre-RC) assembly rather than origin specificity. Secondly, SpOrc4, which is solely responsible for binding SpORC to DNA, inhibited up to 70% of XlORC-dependent DNA replication in Xenopus egg extract by preventing XlORC from binding to chromatin and assembling pre-RCs. Chromatin-bound SpOrc4 was located at AT-rich sequences. XlORC in egg extract bound preferentially to asymmetric A:T-sequences in either bare DNA or in sperm chromatin, and it recruited XlCdc6 and XlMcm proteins to these sequences. These results reveal that XlORC initiates DNA replication preferentially at the same or similar sites to those targeted in S.pombe.","authors":"Kong D, Coleman TR, DePamphilis ML","authors_abbrev":"Kong D et al.","pubmed_publication_date":"01 Jul 2003","pubmed_entrez_date":"2003-07-04","publication_year":"2003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC685.09","SPBC29A10.15","SPBP23A10.13"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:20826957","title":"Complex regulation of sister kinetochore orientation in meiosis-I.","citation":"J Biosci 2010 Sep;35(3):485-95","abstract":"Kinetochores mediate chromosome movement during cell division by interacting with the spindle microtubules. Sexual reproduction necessitates the daunting task of reducing ploidy (number of chromosome sets) in the gametes, which depends upon the specialized properties of meiosis. Kinetochores have a central role in the reduction process. In this review, we discuss the complexity of this role of kinetochores in meiosis-I.","authors":"Bardhan A","authors_abbrev":"Bardhan A","pubmed_publication_date":"Sep 2010","pubmed_entrez_date":"2010-09-10","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16754851","title":"Compartmentalized signaling of Ras in fission yeast.","citation":"Proc Natl Acad Sci U S A 2006 Jun 13;103(24):9045-50","abstract":"Compartment-specific Ras signaling is an emerging paradigm that may explain the multiplex outputs from a single GTPase. The fission yeast, Schizosaccharomyces pombe, affords a simple system in which to study Ras signaling because it has a single Ras protein, Ras1, that regulates two distinct pathways: one that controls mating through a Byr2-mitogen-activated protein kinase cascade and one that signals through Scd1-Cdc42 to maintain elongated cell morphology. We generated Ras1 mutants that are restricted to either the endomembrane or the plasma membrane. Protein binding studies showed that each could interact with the effectors of both pathways. However, when examined in ras1 null cells, endomembrane-restricted Ras1 supported morphology but not mating, and, conversely, plasma membrane-restricted Ras1 supported mating but did not signal to Scd1-Cdc42. These observations provide a striking demonstration of compartment-specific Ras signaling and indicate that spatial specificity in the Ras pathway is evolutionarily conserved.","authors":"Onken B, Wiener H, Philips MR, Chang EC","authors_abbrev":"Onken B et al.","pubmed_publication_date":"13 Jun 2006","pubmed_entrez_date":"2006-06-07","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC1D7.05","SPAC16E8.09"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:1657709","title":"Schizosaccharomyces pombe ste11+ encodes a transcription factor with an HMG motif that is a critical regulator of sexual development.","citation":"Genes Dev 1991 Nov;5(11):1990-9","abstract":"Schizosaccharomyces pombe ste11 encodes a member of the family of HMG-box proteins. Its transcript is induced in response to nitrogen starvation and a concomitant decrease of the intracellular cAMP level. Expression of ste11 is essential for induction of sexual development, and its ectopic expression stimulates uncontrolled mating and sporulation. Ste11 protein regulates positively transcription of the following genes required for sexual development: the mating type genes, matP and matM, and the mei2 gene, which is essential for commitment to meiosis. Ste11 protein synthesized in vitro binds specifically to a DNA fragment carrying a 10-base motif TTCTTTGTTY that is an essential cis-acting element for the induction of mei2 and is commonly seen in the upstream regions of the genes inducible by nitrogen starvation. These observations strongly suggest that Ste11 serves as a key transcription factor for sexual development.","authors":"Sugimoto A, Iino Y, Maeda T, Watanabe Y, Yamamoto M","authors_abbrev":"Sugimoto A et al.","pubmed_publication_date":"Nov 1991","pubmed_entrez_date":"1991-11-01","publication_year":"1991","canto_session_key":"5943de801ceb71fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-28 23:11:25","canto_approved_date":"2026-04-08 07:17:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-03-08 12:25:03","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.17c","SPMTR.02","SPBC23G7.09","SPAC27D7.03c","SPBC19C7.03","SPBC32C12.02","SPMTR.01"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2018-04-28"},{"uniquename":"PMID:17160654","title":"Monitoring dynamic systems with multiparameter fluorescence imaging.","citation":"Anal Bioanal Chem 2007 Jan;387(1):71-82","abstract":"A new general strategy based on the use of multiparameter fluorescence detection (MFD) to register and quantitatively analyse fluorescence images is introduced. Multiparameter fluorescence imaging (MFDi) uses pulsed excitation, time-correlated single-photon counting and a special pixel clock to simultaneously monitor the changes in the eight-dimensional fluorescence information (fundamental anisotropy, fluorescence lifetime, fluorescence intensity, time, excitation spectrum, fluorescence spectrum, fluorescence quantum yield, distance between fluorophores) in real time. The three spatial coordinates are also stored. The most statistically efficient techniques known from single-molecule spectroscopy are used to estimate fluorescence parameters of interest for all pixels, not just for the regions of interest. Their statistical significance is judged from a stack of two-dimensional histograms. In this way, specific pixels can be selected for subsequent pixel-based subensemble analysis in order to improve the statistical accuracy of the parameters estimated. MFDi avoids the need for sequential measurements, because the registered data allow one to perform many analysis techniques, such as fluorescence-intensity distribution analysis (FIDA) and fluorescence correlation spectroscopy (FCS), in an off-line mode. The limitations of FCS for counting molecules and monitoring dynamics are discussed. To demonstrate the ability of our technique, we analysed two systems: (i) interactions of the fluorescent dye Rhodamine 110 inside and outside of a glutathione sepharose bead, and (ii) microtubule dynamics in live yeast cells of Schizosaccharomyces pombe using a fusion protein of Green Fluorescent Protein (GFP) with Minichromosome Altered Loss Protein 3 (Mal3), which is involved in the dynamic cycle of polymerising and depolymerising microtubules.","authors":"Kudryavtsev V, Felekyan S, Woźniak AK, König M, Sandhagen C, Kühnemuth R, Seidel CA, Oesterhelt F","authors_abbrev":"Kudryavtsev V et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2006-12-13","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007212","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.133"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20404084","title":"Transcriptional activation of the general amino acid permease gene per1 by the histone deacetylase Clr6 Is regulated by Oca2 kinase.","citation":"Mol Cell Biol 2010 Jul;30(13):3396-410","abstract":"Expression of nitrogen metabolism genes is regulated by the quality of the nitrogen supply. Here, we describe a mechanism for the transcriptional regulation of the general amino acid permease gene per1 in Schizosaccharomyces pombe. We show that when ammonia is used as the nitrogen source, low levels of per1 are transcribed and histones in the coding and surrounding regions of per1 are acetylated. In the presence of proline, per1 transcription is upregulated and initiates from a more upstream site, generating 5'-extended mRNAs. Concomitantly, histones at per1 are deacetylated in a Clr6-dependent manner, suggesting a positive role for Clr6 in transcriptional regulation of per1. Upstream initiation and histone deactylation of per1 are constitutive in cells lacking the serine/threonine kinase oca2, indicating that Oca2 is a repressor of per1. Oca2 interacts with a protein homologous to the Saccharomyces cerevisiae transcriptional activator Cha4 and with Ago1. Loss of Cha4 or Ago1 causes aberrant induction of per1 under noninducing conditions, suggesting that these proteins are also involved in per1 regulation and hence in nitrogen utilization.","doi":"10.1128/MCB.00971-09","authors":"Kaufmann I, White E, Azad A, Marguerat S, Bähler J, Proudfoot NJ","authors_abbrev":"Kaufmann I et al.","pubmed_publication_date":"Jul 2010","pubmed_entrez_date":"2010-04-21","publication_year":"2010","canto_session_key":"f14ac3e4832ef0fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-09-28 08:03:57","canto_approved_date":"2025-12-06 04:50:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-09-23 17:50:15","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":44,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC36.05c","SPAP7G5.06","SPAC22G7.08","SPCC736.11","SPAC29A4.18","SPCC1020.10","SPAC869.10c","SPBC1683.13c","SPAC139.06"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2025-09-28"},{"uniquename":"PMID:8834792","title":"Isolation of the Schizosaccharomyces pombe RAD54 homologue, rhp54+, a gene involved in the repair of radiation damage and replication fidelity.","citation":"J Cell Sci 1996 Jan;109 ( Pt 1):73-81","abstract":"The RAD54 gene of Saccharomyces cerevisiae encodes a putative helicase, which is involved in the recombinational repair of DNA damage. The RAD54 homologue of the fission yeast Schizosaccharomyces pombe, rhp54+, was isolated by using the RAD54 gene as a heterologous probe. The gene is predicted to encode a protein of 852 amino acids. The overall homology between the mutual proteins of the two species is 67% with 51% identical amino acids and 16% similar amino acids. A rhp54 deletion mutant is very sensitive to both ionizing radiation and UV. Fluorescence microscopy of the rhp54 mutant cells revealed that a large portion of the cells are elongated and occasionally contain aberrant nuclei. In addition, FACS analysis showed an increased DNA content in comparison with wild-type cells. Through a minichromosome-loss assay it was shown that the rhp54 deletion mutant has a very high level of chromosome loss. Furthermore, the rhp54 mutation in either a rad17 or a cdc2.3w mutant background (where the S-phase/mitosis checkpoint is absent) shows a significant reduction in viability. It is hypothesized that the rhp54+ gene is involved in the recombinational repair of UV and X-ray damage and plays a role in the processing of replication-specific lesions.","authors":"Muris DF, Vreeken K, Carr AM, Murray JM, Smit C, Lohman PH, Pastink A","authors_abbrev":"Muris DF et al.","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"10d3f62a451aabc9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-05-13 09:57:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-13 09:57:50","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.13","SPAC644.14c","SPCC1259.13","SPAC15A10.03c","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-05-13"},{"uniquename":"EMBL:AU011532","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013705","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8041894","title":"The molecular basis for cell cycle delays following ionizing radiation: a review.","citation":"Radiother Oncol 1994 Apr;31(1):1-13","abstract":"Exposure of a wide variety of cells to ionizing (X- or gamma-) irradiation results in a division delay which may have several components including a G1 block, a G2 arrest or an S phase delay. The G1 arrest is absent in many cell lines, and the S phase delay is typically seen following relatively high doses (> 5 Gy). In contrast, the G2 arrest is seen in virtually all eukaryotic cells and occurs following high and low doses, even under 1 Gy. The mechanism underlying the G2 arrest may involve suppression of cyclin B1 mRNA and/or protein in some cell lines and tyrosine phosphorylation of p34cdc2 in others. Similar mechanisms are likely to be operative in the G2 arrest induced by various chemotherapeutic agents including nitrogen mustard and etoposide. The upstream signal transduction pathways involved in the G2 arrest following ionizing radiation remain obscure in mammalian cells; however, in the budding yeast the rad9 gene and in the fission yeast the chk1/rad27 gene are involved. There is evidence indicating that shortening of the G2 arrest results in decreased survival which has led to the hypothesis that during this block, cells repair damaged DNA following exposure to genotoxic agents. In cell lines examined to date, wildtype p53 is required for the G1 arrest following ionizing radiation. The gadd45 gene may also have a role in this arrest. Elimination of the G1 arrest leads to no change in survival following radiation in some cell lines and increased radioresistance in others. It has been suggested that this induction of radioresistance in certain cell lines is due to loss of the ability to undergo apoptosis. Relatively little is known about the mechanism underlying the S phase delay. This delay is due to a depression in the rate of DNA synthesis and has both a slow and a fast component. In some cells the S phase delay can be abolished by staurosporine, suggesting involvement of a protein kinase. Understanding the molecular mechanisms behind these delays may lead to improvement in the efficacy of radiotherapy and/or chemotherapy if they can be exploited to decrease repair or increase apoptosis following exposure to those agents.","authors":"Maity A, McKenna WG, Muschel RJ","authors_abbrev":"Maity A et al.","pubmed_publication_date":"Apr 1994","pubmed_entrez_date":"1994-04-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20110347","title":"Tropomyosin and myosin-II cellular levels promote actomyosin ring assembly in fission yeast.","citation":"Mol Biol Cell 2010 Mar 15;21(6):989-1000","abstract":"Myosin-II (Myo2p) and tropomyosin are essential for contractile ring formation and cytokinesis in fission yeast. Here we used a combination of in vivo and in vitro approaches to understand how these proteins function at contractile rings. We find that ring assembly is delayed in Myo2p motor and tropomyosin mutants, but occurs prematurely in cells engineered to express two copies of myo2. Thus, the timing of ring assembly responds to changes in Myo2p cellular levels and motor activity, and the emergence of tropomyosin-bound actin filaments. Doubling Myo2p levels suppresses defects in ring assembly associated with a tropomyosin mutant, suggesting a role for tropomyosin in maximizing Myo2p function. Correspondingly, tropomyosin increases Myo2p actin affinity and ATPase activity and promotes Myo2p-driven actin filament gliding in motility assays. Tropomyosin achieves this by favoring the strong actin-bound state of Myo2p. This mode of regulation reflects a role for tropomyosin in specifying and stabilizing actomyosin interactions, which facilitates contractile ring assembly in the fission yeast system.","authors":"Stark BC, Sladewski TE, Pollard LW, Lord M","authors_abbrev":"Stark BC et al.","pubmed_publication_date":"15 Mar 2010","pubmed_entrez_date":"2010-01-30","publication_year":"2010","canto_session_key":"0bcdd20806ae5fa2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-15 15:42:56","canto_approved_date":"2022-09-17 19:12:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-15 15:42:51","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":39,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAC27F1.02c","SPAC4A8.05c","SPAC926.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-08-15"},{"uniquename":"PMID:8488304","title":"[Genome mapping of Schizosaccharomyces pombe].","citation":"Tanpakushitsu Kakusan Koso 1993 Feb;38(3):677-84","abstract":"","authors":"Mizukami T, Garkavtsev I, Beach D, Marr T, Niwa O, Yanagida M","authors_abbrev":"Mizukami T et al.","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10816558","title":"The survival motor neuron protein of Schizosacharomyces pombe. Conservation of survival motor neuron interaction domains in divergent organisms.","citation":"J Biol Chem 2000 Aug 04;275(31):23841-6","abstract":"Spinal muscular atrophy is a common often lethal neurodegenerative disease resulting from deletions or mutations in the survival motor neuron gene (SMN). SMN is ubiquitously expressed in metazoan cells and plays a role in small nuclear ribonucleoprotein assembly and pre-mRNA splicing. Here we characterize the Schizosacharomyces pombe orthologue of SMN (yeast SMN (ySMN)). We report that the ySMN protein is essential for viability and localizes in both the cytoplasm and the nucleus. Like human SMN, we show that ySMN can oligomerize. Remarkably, ySMN interacts directly with human SMN and Sm proteins. The highly conserved carboxyl-terminal domain of ySMN is necessary for the evolutionarily conserved interactions of SMN and required for cell viability. We also demonstrate that the conserved amino-terminal region of ySMN is not required for SMN and Sm binding but is critical for the housekeeping function of SMN.","authors":"Paushkin S, Charroux B, Abel L, Perkinson RA, Pellizzoni L, Dreyfuss G","authors_abbrev":"Paushkin S et al.","pubmed_publication_date":"04 Aug 2000","pubmed_entrez_date":"2000-05-19","publication_year":"2000","canto_session_key":"da0fce46ad28a5f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-07-23 13:55:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-25 10:48:21","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-25"},{"uniquename":"PMID:18758733","title":"The fission yeast homologue of Glel is essential for growth and involved in mRNA export.","citation":"J Microbiol 2008 Aug;46(4):422-8","abstract":"We have isolated Glel homologue (named as spglel) as a partial multicopy suppressor of the synthetic lethality of rael-167 elfl-21 in fission yeast Schizosaccharomyces pombe. The spglel is also able to complement partially temperature-sensitive phenotype of rael-167 only at a lower restrictive temperature. The spglel gene contains one intron and encodes a 480 amino-acid protein with predicted molecular weight of 56.2 kDa. We showed that spglel gene is essential for vegetative growth and functional Glel-GFP protein is localized mainly in NPC. The accumulation of poly(A)(+) RNA in the nucleus is exhibited when expression of spglel is repressed or over-expressed. These results suggest that the spGle1 protein is also involved in mRNA export in fission yeast.","doi":"10.1007/s12275-008-0177-0","authors":"Moon D, Bae JA, Cho HJ, Yoon JH","authors_abbrev":"Moon D et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-09-02","publication_year":"2008","canto_session_key":"afd6568b8a2d599f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-10 17:12:36","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-08 16:20:12","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1921.03c","SPAC3C7.08c","SPBC16A3.05c","SPBC31E1.05"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-12-08"},{"uniquename":"PMID:20081200","title":"Mapping of interaction sites of the Schizosaccharomyces pombe protein Translin with nucleic acids and proteins: a combined molecular genetics and bioinformatics study.","citation":"Nucleic Acids Res 2010 May;38(9):2975-89","abstract":"Translin is a single-stranded RNA- and DNA-binding protein, which has been highly conserved in eukaryotes, from man to Schizosaccharomyces pombe. TRAX is a Translin paralog associated with Translin, which has coevolved with it. We generated structural models of the S. pombe Translin (spTranslin), based on the solved 3D structure of the human ortholog. Using several bioinformatics computation tools, we identified in the equatorial part of the protein a putative nucleic acids interaction surface, which includes many polar and positively charged residues, mostly arginines, surrounding a shallow cavity. Experimental verification of the bioinformatics predictions was obtained by assays of nucleic acids binding to amino acid substitution variants made in this region. Bioinformatics combined with yeast two-hybrid assays and proteomic analyses of deletion variants, also identified at the top of the spTranslin structure a region required for interaction with spTRAX, and for spTranslin dimerization. In addition, bioinformatics predicted the presence of a second protein-protein interaction site at the bottom of the spTranslin structure. Similar nucleic acid and protein interaction sites were also predicted for the human Translin. Thus, our results appear to generally apply to the Translin family of proteins, and are expected to contribute to a further elucidation of their functions.","doi":"10.1093/nar/gkp1230","authors":"Eliahoo E, Ben Yosef R, Pérez-Cano L, Fernández-Recio J, Glaser F, Manor H","authors_abbrev":"Eliahoo E et al.","pubmed_publication_date":"May 2010","pubmed_entrez_date":"2010-01-19","publication_year":"2010","canto_session_key":"729e6559539b7379","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-28 13:58:38","canto_approved_date":"2022-02-03 09:04:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-19 17:11:35","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.09c","SPAC30.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-04-28"},{"uniquename":"PMID:26308057","title":"Spatiotemporal Regulation of Nuclear Transport Machinery and Microtubule Organization.","citation":"Cells 2015 Aug 21;4(3):406-26","abstract":"Spindle microtubules capture and segregate chromosomes and, therefore, their assembly is an essential event in mitosis. To carry out their mission, many key players for microtubule formation need to be strictly orchestrated. Particularly, proteins that assemble the spindle need to be translocated at appropriate sites during mitosis. A small GTPase (hydrolase enzyme of guanosine triphosphate), Ran, controls this translocation. Ran plays many roles in many cellular events: nucleocytoplasmic shuttling through the nuclear envelope, assembly of the mitotic spindle, and reorganization of the nuclear envelope at the mitotic exit. Although these events are seemingly distinct, recent studies demonstrate that the mechanisms underlying these phenomena are substantially the same as explained by molecular interplay of the master regulator Ran, the transport factor importin, and its cargo proteins. Our review focuses on how the transport machinery regulates mitotic progression of cells. We summarize translocation mechanisms governed by Ran and its regulatory proteins, and particularly focus on Ran-GTP targets in fission yeast that promote spindle formation. We also discuss the coordination of the spatial and temporal regulation of proteins from the viewpoint of transport machinery. We propose that the transport machinery is an essential key that couples the spatial and temporal events in cells.","doi":"10.3390/cells4030406","authors":"Okada N, Sato M","authors_abbrev":"Okada N et al.","pubmed_publication_date":"21 Aug 2015","pubmed_entrez_date":"2015-08-27","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-08-28 00:18:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18252721","title":"Fission yeast MAP kinase Sty1 is recruited to stress-induced genes.","citation":"J Biol Chem 2008 Apr 11;283(15):9945-56","abstract":"The stress-induced expression of many fission yeast genes is dependent upon the Sty1 mitogen-activated protein kinase (MAPK) and Atf1 transcription factor. Atf1 is phosphorylated by Sty1 yet this phosphorylation is not required for stress-induced gene expression, suggesting another mechanism exists whereby Sty1 activates transcription. Here we show that Sty1 associates with Atf1-dependent genes and is recruited to both their promoters and coding regions. This occurs in response to various stress conditions coincident with the kinetics of the activation of Sty1. Association with promoters is not a consequence of increased nuclear accumulation of Sty1 nor does it require the phosphorylation of Atf1. However, recruitment is completely abolished in a mutant lacking Sty1 kinase activity. Both Atf1 and its binding partner Pcr1 are required for association of Sty1 with Atf1-dependent promoters, suggesting that this heterodimer must be intact for optimal recruitment of the MAPK. However, many Atf1-dependent genes are still expressed in a pcr1Delta mutant but with significantly delayed kinetics, thus providing an explanation for the relatively mild stress sensitivity displayed by pcr1Delta. Consistent with this delay, Sty1 and Atf1 cannot be detected at these promoters in this condition, suggesting that their association with chromatin is weak or transient in the absence of Pcr1.","doi":"10.1074/jbc.M710428200","authors":"Reiter W, Watt S, Dawson K, Lawrence CL, Bähler J, Jones N, Wilkinson CR","authors_abbrev":"Reiter W et al.","pubmed_publication_date":"11 Apr 2008","pubmed_entrez_date":"2008-02-07","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC21E11.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21642955","title":"Tra1 has specific regulatory roles, rather than global functions, within the SAGA co-activator complex.","citation":"EMBO J 2011 Jun 03;30(14):2843-52","abstract":"The SAGA complex is a conserved, multifunctional co-activator that has broad roles in eukaryotic transcription. Previous studies suggested that Tra1, the largest SAGA component, is required either for SAGA assembly or for SAGA recruitment by DNA-bound transcriptional activators. In contrast to Saccharomyces cerevisiae and mouse, a tra1Δ mutant is viable in Schizosaccharomyces pombe, allowing us to test these issues in vivo. We find that, in a tra1Δ mutant, SAGA assembles and is recruited to some, but not all, promoters. Consistent with these findings, Tra1 regulates the expression of only a subset of SAGA-dependent genes. We previously reported that the SAGA subunits Gcn5 and Spt8 have opposing regulatory roles during S. pombe sexual differentiation. We show here that, like Gcn5, Tra1 represses this pathway, although by a distinct mechanism. Thus, our study reveals that Tra1 has specific regulatory roles, rather than global functions, within SAGA.","doi":"10.1038/emboj.2011.181","authors":"Helmlinger D, Marguerat S, Villén J, Swaney DL, Gygi SP, Bähler J, Winston F","authors_abbrev":"Helmlinger D et al.","pubmed_publication_date":"03 Jun 2011","pubmed_entrez_date":"2011-06-07","publication_year":"2011","canto_session_key":"45dd89cc4951b51a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dominique Helmlinger","canto_first_approved_date":"2017-03-17 13:17:01","canto_approved_date":"2026-02-07 06:36:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-27 09:04:27","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[{"name":"Dominique Helmlinger","community_curator":true,"annotation_count":112,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.02","SPBC32C12.02","SPAC4D7.10c","SPBC21H7.02","SPBC14C8.17c","SPAC13A11.04c","SPAC1F5.11c","SPBC6B1.12c","SPAC27D7.03c","SPBC21D10.10","SPBP23A10.08","SPCC126.04c","SPAC1952.05","SPBP16F5.03c","SPBC25H2.11c","SPCC622.13c","SPAC637.12c","SPAC57A10.14","SPCC16C4.18c","SPAC9G1.13c","SPCC24B10.08c","SPBC16A3.19","SPAC12G12.05c","SPCC1795.08c","SPCC61.02","SPAC6F6.09","SPBC83.08","SPBC28F2.10c","SPCC830.05c","SPAC17G8.07","SPBC887.18c","SPAC3G9.08","SPBC1604.17c","SPAPB8E5.09","SPAC458.03","SPBC1921.07c","SPBC106.04","SPAC1006.02","SPCC5E4.03c"],"gene_count":39,"ltp_gene_count":37,"approved_date":"2017-03-17"},{"uniquename":"PMID:17208257","title":"Schizosaccharomyces pombe Rad22A and Rad22B have similar biochemical properties and form multimeric structures.","citation":"Mutat Res 2007 Feb 03;615(1-2):143-52","abstract":"The Saccharomyces cerevisiae Rad52 protein has a crucial role in the repair of DNA double-strand breaks by homologous recombination. In vitro, Rad52 displays DNA binding and strand annealing activities and promotes Rad51-mediated strand exchange. Schizosaccharomyces pombe has two Rad52 homologues, Rad22A and Rad22B. Whereas rad22A deficient strains exhibit severe defects in repair and recombination, rad22B mutants have a much less severe phenotype. To better understand the role of Rad22A and Rad22B in double-strand break repair, both proteins were purified to near homogeneity. Using gel retardation and filter binding assays, binding of Rad22A and Rad22B to short single-stranded DNAs was demonstrated. Binding of Rad22A to double-stranded oligonucleotides or linearized plasmid molecules containing blunt ends or short single-stranded overhangs could not be detected. Rad22B also does not bind efficiently to short duplex oligonucleotides but binds readily to DNA fragments containing 3'-overhangs. Rad22A as well as Rad22B efficiently promote annealing of complementary single-stranded DNAs. In the presence of Rad22A annealing of complementary DNAs is almost 90%. Whereas in reactions containing Rad22B the maximum level of annealing is 60%, most likely due to inhibition of the reaction by duplex DNA. Gel-filtration experiments and electron microscopic analyses indicate self-association of Rad22A and Rad22B and the formation of multimeric structures as has been observed for Rad52 in yeast and man.","authors":"de Vries FA, Zonneveld JB, de Groot AJ, Koning RI, van Zeeland AA, Pastink A","authors_abbrev":"de Vries FA et al.","pubmed_publication_date":"03 Feb 2007","pubmed_entrez_date":"2007-01-09","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC26H8.10","SPAC30D11.10","SPBC119.14"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:29529046","title":"Zinc transporters belonging to the Cation Diffusion Facilitator (CDF) family have complementary roles in transporting zinc out of the cytosol.","citation":"PLoS Genet 2018 Mar;14(3):e1007262","abstract":"Zinc is an essential trace element that is required for the function of a large number of proteins. As these zinc-binding proteins are found within the cytosol and organelles, all eukaryotes require mechanisms to ensure that zinc is delivered to organelles, even under conditions of zinc deficiency. Although many zinc transporters belonging to the Cation Diffusion Facilitator (CDF) families have well characterized roles in transporting zinc into the lumens of intracellular compartments, relatively little is known about the mechanisms that maintain organelle zinc homeostasis. The fission yeast Schizosaccharomyces pombe is a useful model system to study organelle zinc homeostasis as it expresses three CDF family members that transport zinc out of the cytosol into intracellular compartments: Zhf1, Cis4, and Zrg17. Zhf1 transports zinc into the endoplasmic reticulum, and Cis4 and Zrg17 form a heterodimeric complex that transports zinc into the cis-Golgi. Here we have used the high and low affinity ZapCY zinc-responsive FRET sensors to examine cytosolic zinc levels in yeast mutants that lack each of these CDF proteins. We find that deletion of cis4 or zrg17 leads to higher levels of zinc accumulating in the cytosol under conditions of zinc deficiency, whereas deletion of zhf1 results in zinc accumulating in the cytosol when zinc is not limiting. We also show that the expression of cis4, zrg17, and zhf1 is independent of cellular zinc status. Taken together our results suggest that the Cis4/Zrg17 complex is necessary for zinc transport out of the cytosol under conditions of zinc-deficiency, while Zhf1 plays the dominant role in removing zinc from the cytosol when labile zinc is present. We propose that the properties and/or activities of individual CDF family members are fine-tuned to enable cells to control the flux of zinc out of the cytosol over a broad range of environmental zinc stress.","doi":"10.1371/journal.pgen.1007262","authors":"Choi S, Hu YM, Corkins ME, Palmer AE, Bird AJ","authors_abbrev":"Choi S et al.","pubmed_publication_date":"Mar 2018","pubmed_entrez_date":"2018-03-13","publication_year":"2018","canto_session_key":"2ffb56fc6f8cf07d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Amanda Bird","canto_first_approved_date":"2019-02-10 09:02:25","canto_approved_date":"2026-01-19 10:17:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-04 20:04:24","canto_added_date":"2018-03-14 01:15:04","annotation_curators":[{"name":"Amanda Bird","community_curator":true,"annotation_count":18,"orcid":"0000-0002-1846-7050","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17D4.03c","SPBC16D10.06","SPAC25B8.19c","SPAC23C11.14","SPBC16E9.14c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-02-10"},{"uniquename":"PANTHER:PTHR15502","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC31F10.14c","HGNC:24187"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1396551","title":"Heavy metal tolerance in the fission yeast requires an ATP-binding cassette-type vacuolar membrane transporter.","citation":"EMBO J 1992 Oct;11(10):3491-9","abstract":"In response to heavy metal stress, plants and certain fungi, such as the fission yeast Schizosaccharomyces pombe, synthesize small metal-binding peptides known as phytochelatins. We have identified a cadmium sensitive S. pombe mutant deficient in the accumulation of a sulfide-containing phytochelatin-cadmium complex, and have isolated the gene, designated hmt1, that complements this mutant. The deduced protein sequence of the hmt1 gene product shares sequence identity with the family of ABC (ATP-binding cassette)-type transport proteins which includes the mammalian P-glycoproteins and CFTR, suggesting that the encoded product is an integral membrane protein. Analysis of fractionated fission yeast cell components indicates that the HMT1 polypeptide is associated with the vacuolar membrane. Additionally, fission yeast strains harboring an hmt1-expressing multicopy plasmid exhibit enhanced metal tolerance along with a higher intracellular level of cadmium, implying a relationship between HMT1 mediated transport and compartmentalization of heavy metals. This suggests that tissue-specific overproduction of a functional hmt1 product in transgenic plants might be a means to alter the tissue localization of these elements, such as for sequestering heavy metals away from consumable parts of crop plants.","authors":"Ortiz DF, Kreppel L, Speiser DM, Scheel G, McDonald G, Ow DW","authors_abbrev":"Ortiz DF et al.","pubmed_publication_date":"Oct 1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_session_key":"e4bf4f71cadcf254","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-21 13:14:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-02-16 22:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-02-16"},{"uniquename":"PMID:7961415","title":"Cloning, nucleotide sequence, and regulation of Schizosaccharomyces pombe thi4, a thiamine biosynthetic gene.","citation":"J Bacteriol 1994 Nov;176(21):6631-5","abstract":"thi4 mutants of Schizosaccharomyces pombe exhibit defective thiamine biosynthesis, and thi4 mutations define a gene which is believed to be involved in the phosphorylation of 4-amino-5-hydroxymethyl-2-methylpyrimidine or 5-(2-hydroxyethyl)-4-methylthiazole and/or in the coupling of the two phosphorylated precursors to thiamine monophosphate (A. M. Schweingruber, J. Dlugonski, E. Edenharter, and M. E. Schweingruber, Curr. Genet. 19:249-254, 1991). The thi4 gene was cloned by functional complementation of a thi4 mutant and physically mapped on the left arm of chromosome I close to the genetic marker gln1. The thi4-carrying DNA fragment shows an open reading frame encoding a protein of 518 amino acids and a calculated molecular mass of 55.6 kDa. The appearance of thi4 mRNA is strongly repressed by thiamine and to a lesser extent by 5-(2-hydroxyethyl)-4-methylthiazole. thi4 mRNA production is under the control of the thi1 gene-encoded transcription factor and of the negative regulators encoded by genes tnr1, tnr2, and tnr3. thi4 is expressed and regulated in manners similar to those of other S. pombe genes involved in thiamine metabolism, including thi2, thi3, and pho4.","authors":"Zurlinden A, Schweingruber ME","authors_abbrev":"Zurlinden A et al.","pubmed_publication_date":"Nov 1994","pubmed_entrez_date":"1994-11-01","publication_year":"1994","canto_session_key":"c547e80e90d0f369","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-08 08:51:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-08 08:51:23","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPAC6F12.05c","SPAC1486.10","SPAC23H4.10c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2014-08-08"},{"uniquename":"PMID:30659798","title":"Cryo-EM Structure (4.5-Å) of Yeast Kinesin-5-Microtubule Complex Reveals a Distinct Binding Footprint and Mechanism of Drug Resistance.","citation":"J Mol Biol 2019 Feb 15;431(4):864-872","abstract":"Kinesin-5s are microtubule-dependent motors that drive spindle pole separation during mitosis. We used cryo-electron microscopy to determine the 4.5-Å resolution structure of the motor domain of the fission yeast kinesin-5 Cut7 bound to fission yeast microtubules and explored the topology of the motor-microtubule interface and the susceptibility of the complex to drug binding. Despite their non-canonical architecture and mechanochemistry, Schizosaccharomyces pombe microtubules were stabilized by epothilone at the taxane binding pocket. The overall Cut7 footprint on the S. pombe microtubule surface is altered compared to mammalian tubulin microtubules because of their different polymer architectures. However, the core motor-microtubule interaction is tightly conserved, reflected in similar Cut7 ATPase activities on each microtubule type. AMPPNP-bound Cut7 adopts a kinesin-conserved ATP-like conformation including cover neck bundle formation. However, the Cut7 ATPase is not blocked by a mammalian-specific kinesin-5 inhibitor, consistent with the non-conserved sequence and structure of its loop5 insertion.","doi":"10.1016/j.jmb.2019.01.011","authors":"von Loeffelholz O, Peña A, Drummond DR, Cross R, Moores CA","authors_abbrev":"von Loeffelholz O et al.","pubmed_publication_date":"15 Feb 2019","pubmed_entrez_date":"2019-01-20","publication_year":"2019","canto_session_key":"3bdb6bca18decfc1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-02-04 16:26:28","canto_approved_date":"2019-02-06 08:03:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-04 09:58:33","canto_added_date":"2019-01-21 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.05c","SPBC26H8.07c","SPAC25G10.07c","SPBC16A3.15c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-02-04","pdb_entries":[{"pdb_id":"6s8m","gene_chains":[{"gene_uniquename":"SPBC16A3.15c","chain":"A","position":"1-455"},{"gene_uniquename":"SPBC26H8.07c","chain":"B","position":"1-448"},{"gene_uniquename":"SPAC25G10.07c","chain":"K","position":"1-432"}],"title":"S. pombe microtubule decorated with Cut7 motor domain in the AMPPNP state","entry_authors":"Moores CA,von Loeffelholz O","entry_authors_abbrev":"Moores CA et al.","reference_uniquename":"PMID:30659798","experimental_method":"EM","resolution":"4.5"}]},{"uniquename":"PMID:23535663","title":"CAND1 controls in vivo dynamics of the cullin 1-RING ubiquitin ligase repertoire.","citation":"Nat Commun 2013;4:1642","abstract":"The combinatorial architecture of cullin 1-RING ubiquitin ligases, in which multiple F-box containing substrate receptors compete for access to CUL1, poses special challenges to assembling cullin 1-RING ubiquitin ligase complexes through high affinity protein interactions while maintaining the flexibility to dynamically sample the entire F-box containing substrate receptor repertoire. Here, using highly quantitative mass spectrometry, we demonstrate that this problem is addressed by CAND1, a factor that controls the dynamics of the global cullin 1-RING ubiquitin ligase network by promoting the assembly of newly synthesized F-box containing substrate receptors with CUL1-RBX1 core complexes. Our studies of in vivo cullin 1-RING ubiquitin ligase dynamics and in vitro biochemical findings showing that CAND1 can displace F-box containing substrate receptors from Cul1p suggest that CAND1 functions in a cycle that serves to exchange F-box containing substrate receptors on CUL1 cores. We propose that this cycle assures comprehensive sampling of the entire F-box containing substrate receptor repertoire in order to maintain the cullin 1-RING ubiquitin ligase landscape, a function that we show to be critical for substrate degradation and normal physiology.","doi":"10.1038/ncomms2636","authors":"Wu S, Zhu W, Nhan T, Toth JI, Petroski MD, Wolf DA","authors_abbrev":"Wu S et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-03-29","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-11-01 02:19:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1718.01","SPAC57A10.05c","SPAPB17E12.04c","SPAC1687.13c","SPAC23H4.18c","SPAC17G6.12","SPBC3H7.06c","SPBC1703.06","SPCC1827.08c","SPAC4D7.03","SPAC13D6.01","SPBC215.03c","SPBC409.05","SPAC29E6.01","SPAC6F6.02c","SPAC22A12.03c"],"gene_count":16,"ltp_gene_count":16},{"uniquename":"PMID:27105116","title":"SHREC Silences Heterochromatin via Distinct Remodeling and Deacetylation Modules.","citation":"Mol Cell 2016 Apr 21;62(2):207-221","abstract":"Nucleosome remodeling and deacetylation (NuRD) complexes are co-transcriptional regulators implicated in differentiation, development, and diseases. Methyl-CpG binding domain (MBD) proteins play an essential role in recruitment of NuRD complexes to their target sites in chromatin. The related SHREC complex in fission yeast drives transcriptional gene silencing in heterochromatin through cooperation with HP1 proteins. How remodeler and histone deacetylase (HDAC) cooperate within NuRD complexes remains unresolved. We determined that in SHREC the two modules occupy distant sites on the scaffold protein Clr1 and that repressive activity of SHREC can be modulated by the expression level of the HDAC-associated Clr1 domain alone. Moreover, the crystal structure of Clr2 reveals an MBD-like domain mediating recruitment of the HDAC module to heterochromatin. Thus, SHREC bi-functionality is organized in two separate modules with separate recruitment mechanisms, which work together to elicit transcriptional silencing at heterochromatic loci.","doi":"10.1016/j.molcel.2016.03.016","authors":"Job G, Brugger C, Xu T, Lowe BR, Pfister Y, Qu C, Shanker S, Baños Sanz JI, Partridge JF, Schalch T","authors_abbrev":"Job G et al.","pubmed_publication_date":"21 Apr 2016","pubmed_entrez_date":"2016-04-23","publication_year":"2016","canto_session_key":"271aac2916b6baf0","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-04-24 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B3.17","SPBC800.03","SPBP35G2.10","SPBC2D10.17"],"gene_count":4,"ltp_gene_count":4,"pdb_entries":[{"pdb_id":"5ikf","gene_chains":[{"gene_uniquename":"SPBC2D10.17","chain":"B","position":"357-500"},{"gene_uniquename":"SPBP35G2.10","chain":"A","position":"1156-1417"}],"title":"Crystal structure of the C-terminal domain of the Mit1 nucleosome remodeler in complex with Clr1","entry_authors":"Brugger C,Schalch T","entry_authors_abbrev":"Brugger C et al.","reference_uniquename":"PMID:27105116","experimental_method":"X-ray","resolution":"2.8"},{"pdb_id":"5ikk","gene_chains":[{"gene_uniquename":"SPBC800.03","chain":"A","position":"31-687"}],"title":"Structure of the histone deacetylase Clr3","entry_authors":"Brugger C,Schalch T","entry_authors_abbrev":"Brugger C et al.","reference_uniquename":"PMID:27105116","experimental_method":"X-ray","resolution":"2.4"},{"pdb_id":"5ikj","gene_chains":[{"gene_uniquename":"SPAC1B3.17","chain":"A","position":"1-537"},{"gene_uniquename":"SPBC2D10.17","chain":"B","position":"1151-1238"}],"title":"Structure of Clr2 bound to the Clr1 C-terminus","entry_authors":"Pfister Y,Schalch T","entry_authors_abbrev":"Pfister Y et al.","reference_uniquename":"PMID:27105116","experimental_method":"X-ray","resolution":"2.3"}]},{"uniquename":"PMID:14668484","title":"Global gene expression responses of fission yeast to ionizing radiation.","citation":"Mol Biol Cell 2004 Feb;15(2):851-60","abstract":"A coordinated transcriptional response to DNA-damaging agents is required to maintain genome stability. We have examined the global gene expression responses of the fission yeast Schizosaccharomyces pombe to ionizing radiation (IR) by using DNA microarrays. We identified approximately 200 genes whose transcript levels were significantly altered at least twofold in response to 500 Gy of gamma IR in a temporally defined manner. The majority of induced genes were core environmental stress response genes, whereas the remaining genes define a transcriptional response to DNA damage in fission yeast. Surprisingly, few DNA repair and checkpoint genes were transcriptionally modulated in response to IR. We define a role for the stress-activated mitogen-activated protein kinase Sty1/Spc1 and the DNA damage checkpoint kinase Rad3 in regulating core environmental stress response genes and IR-specific response genes, both independently and in concert. These findings suggest a complex network of regulatory pathways coordinate gene expression responses to IR in eukaryotes.","authors":"Watson A, Mata J, Bähler J, Carr A, Humphrey T","authors_abbrev":"Watson A et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2003-12-12","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC216.05","SPCC1259.13"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:36110330","title":"Viscoelastic Relaxation of the Nuclear Envelope Does Not Cause the Collapse of the Spindle After Ablation in  S. pombe .","citation":"J Undergrad Rep Phys 2021;31(1)","abstract":"A large molecular machine called the mitotic spindle is responsible for accurate chromosome segregation in eukaryotic cells. The spindle consists of protein filaments known as microtubules and microtubule-associated proteins such as motors and crosslinkers, which help impart its organization. In the case of the fission yeast  S. pombe , these form a single bundle inside the nucleus. During spindle elongation, sliding by motor proteins provides an internal source of extensile forces, which are resisted by the compressive forces of the nuclear envelope. To probe the sources of this force balance, we cut the spindle using focused laser light at various stages of spindle elongation. We find that the spindle pole bodies collapse toward each other post-ablation. While this basic behavior has been previously observed, many questions remain about the timing, mechanics, and molecular requirements of this phenomenon. Here, we quantify the time scale of the relaxation and probe its underlying mechanism. We demonstrate that viscoelastic relaxation of the nuclear envelope cannot explain this phenomenon and provide evidence of active forces as the underlying mechanism.","doi":"10.1063/10.0006352","authors":"Zareiesfandabadi P, Elting MW","authors_abbrev":"Zareiesfandabadi P et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2022-09-16","publication_year":"2021","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2022-09-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37783794","title":"An ESCRT grommet cooperates with a diffusion barrier to maintain nuclear integrity.","citation":"Nat Cell Biol 2023 Oct;25(10):1465-1477","abstract":"The molecular mechanisms by which the endosomal sorting complexes required for transport (ESCRT) proteins contribute to the integrity of the nuclear envelope (NE) barrier are not fully defined. We leveraged the single NE hole generated by mitotic extrusion of the Schizosaccharomyces pombe spindle pole body to reveal two modes of ESCRT function executed by distinct complements of ESCRT-III proteins, both dependent on CHMP7/Cmp7. A grommet-like function is required to restrict the NE hole in anaphase B, whereas replacement of Cmp7 by a sealing module ultimately closes the NE in interphase. Without Cmp7, nucleocytoplasmic compartmentalization remains intact despite NE discontinuities of up to 540 nm, suggesting mechanisms to limit diffusion through these holes. We implicate spindle pole body proteins as key components of a diffusion barrier acting with Cmp7 in anaphase B. Thus, NE remodelling mechanisms cooperate with proteinaceous diffusion barriers beyond nuclear pore complexes to maintain the nuclear compartment.","doi":"10.1038/s41556-023-01235-4","authors":"Ader NR, Chen L, Surovtsev IV, Chadwick WL, Rodriguez EC, King MC, Lusk CP","authors_abbrev":"Ader NR et al.","pubmed_publication_date":"Oct 2023","pubmed_entrez_date":"2023-10-02","publication_year":"2023","canto_session_key":"48d935f12b87d5c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nicholas Ader","canto_first_approved_date":"2023-10-11 08:15:02","canto_approved_date":"2026-01-29 17:11:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-07 09:06:04","canto_added_date":"2023-10-03 23:25:04","annotation_curators":[{"name":"Nicholas Ader","community_curator":true,"annotation_count":73,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":22,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4H3.11c","SPBC1604.18c","SPAC1786.03","SPAC23C11.16","SPBC244.01c","SPBC947.12","SPAC18G6.10","SPAC3A12.14","SPCC1442.17c","SPBC428.20c","SPBC365.15","SPCC1739.11c","SPBC902.06","SPAC9E9.14","SPAC14C4.05c","SPCC895.07","SPCC417.07c","SPBC13G1.12","SPAC8F11.06","SPAC9G1.15c","SPBC32F12.04","SPBC12D12.01","SPAC4F8.01","SPAC6G9.06c","SPBC649.05","SPAC1142.07c"],"gene_count":26,"ltp_gene_count":26,"approved_date":"2023-10-11"},{"uniquename":"GO_REF:0000094","title":"Representation of metazoan development as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the development of a metazoan structure as a biological process. The underlying equivalence axiom template is \"'anatomical structure development' and 'results in development of' some E\", where E is a anatomical entity (UBERON:0001062).","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25872245","title":"Addition of citral controls ROS and reduces toxicity in 5-fluorouracil treated Schizosaccharomyces pombe cells.","citation":"Indian J Exp Biol 2015 Mar;53(3):152-7","abstract":"In systemic therapy, chemotherapeutic drugs, often, cause considerable side effects; and combination of natural compounds lessen the extent of such effects. In the present study, combined effect of citral and 5-fluorouracil was studied in Schizosaccharomyces pombe cells. The antagonistic combination index found was at 0.01 and 0.025 mM of citral with 40 μg or higher concentration of 5-fluorouracil. The combined treatment was so effective that higher number of cells underwent apoptosis compared to individual treatment of 5-fluorouracil. Citral controlled ROS levels and increased survival of normal cells. Several differentially expressed proteins observed in the citral treatment could further help understanding its mechanism of action.","authors":"Patel PB, Thakkar VR","authors_abbrev":"Patel PB et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-04-16","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-04-18 00:19:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38105947","title":"The Greatwall-Endosulfine-PP2A/B55 pathway controls entry into quiescence by promoting translation of Elongator-tuneable transcripts.","citation":"Res Sq 2023 Dec 05;","abstract":"Quiescent cells require a continuous supply of proteins to maintain protein homeostasis. In fission yeast, entry into quiescence is triggered by nitrogen stress, leading to the inactivation of TORC1 and the activation of TORC2. Here, we report that the Greatwall-Endosulfine-PPA/B55 pathway connects the downregulation of TORC1 with the upregulation of TORC2, resulting in the activation of Elongator-dependent tRNA modifications essential for sustaining the translation programme during entry into quiescence. This process promotes U34 and A37 tRNA modifications at the anticodon stem loop, enhancing translation efficiency and fidelity of mRNAs enriched for AAA versus AAG lysine codons. Notably, some of these mRNAs encode inhibitors of TORC1, activators of TORC2, tRNA modifiers, and proteins necessary for telomeric and subtelomeric functions. Therefore, we propose a novel mechanism by which cells respond to nitrogen stress at the level of translation, involving a coordinated interplay between the tRNA epitranscriptome and biased codon usage.","doi":"10.21203/rs.3.rs-3616701/v1","authors":"Moreno S, Del Dedo JE, Segundo RL, Vázquez-Bolado A, Sun J, García-Blanco N, Suárez MB, García P, Tricquet P, Chen JS, Dedon P, Gould K, Hidalgo E, Hermand D","authors_abbrev":"Moreno S et al.","pubmed_publication_date":"05 Dec 2023","pubmed_entrez_date":"2023-12-18","publication_year":"2023","canto_session_key":"437a6cbc1ebe0935","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-12-19 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19362535","title":"High-affinity binding of Chp1 chromodomain to K9 methylated histone H3 is required to establish centromeric heterochromatin.","citation":"Mol Cell 2009 Apr 10;34(1):36-46","abstract":"In fission yeast, assembly of centromeric heterochromatin requires the RITS complex, which consists of Ago1, Tas3, Chp1, and siRNAs derived from centromeric repeats. Recruitment of RITS to centromeres has been proposed to depend on siRNA-dependent targeting of Ago1 to centromeric sequences. Previously, we demonstrated that methylated lysine 9 of histone H3 (H3K9me) acts upstream of siRNAs during heterochromatin establishment. Our crystal structure of Chp1's chromodomain in complex with a trimethylated lysine 9 H3 peptide reveals extensive sites of contact that contribute to Chp1's high-affinity binding. We found that this high-affinity binding is critical for the efficient establishment of centromeric heterochromatin, but preassembled heterochromatin can be maintained when Chp1's affinity for H3K9me is greatly reduced.","doi":"10.1016/j.molcel.2009.02.024","authors":"Schalch T, Job G, Noffsinger VJ, Shanker S, Kuscu C, Joshua-Tor L, Partridge JF","authors_abbrev":"Schalch T et al.","pubmed_publication_date":"10 Apr 2009","pubmed_entrez_date":"2009-04-14","publication_year":"2009","canto_session_key":"6e7137c59c7c4231","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-13 17:46:03","canto_approved_date":"2025-04-16 09:41:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-03 11:16:12","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":86,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.04","SPAC18G6.02c","SPAC664.01c","SPAC1834.04","SPCC736.11","SPBC83.03c","SPBC428.08c","SPBC1105.11c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2024-02-13","pdb_entries":[{"pdb_id":"3g7l","gene_chains":[{"gene_uniquename":"SPBC8D2.04","chain":"P","position":"2-17"},{"gene_uniquename":"SPAC18G6.02c","chain":"A","position":"15-75"}],"title":"Chromodomain of Chp1 in complex with Histone H3K9me3 peptide","entry_authors":"Schalch T,Joshua-Tor L","entry_authors_abbrev":"Schalch T et al.","reference_uniquename":"PMID:19362535","experimental_method":"X-ray","resolution":"2.2"}]},{"uniquename":"GO_REF:0000095","title":"Literature reference not indexed by PubMed","abstract":"This article is not referenced in PubMed. Please see contributing data resource for details.","authors":"Mouse Genome Informatics scientific curators and FlyBase","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15003443","title":"A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"J Mol Biol 2004 Mar 19;337(2):243-53","abstract":"The fungal transamidase complex that executes glycosylphosphatidylinositol (GPI) lipid anchoring of precursor proteins has overlapping but distinct sequence specificity compared with the animal system. Therefore, a taxon-specific prediction tool for the recognition of the C-terminal signal in fungal sequences is necessary. We have collected a learning set of fungal precursor protein sequences from the literature and fungal proteomes. Although the general four segment scheme of the recognition signal is maintained also in fungal precursors, there are taxon specificities in details. A fungal big-Pi predictor has been developed for the assessment of query sequence concordance with fungi-specific recognition signal requirements. The sensitivity of this predictor is close to 90%. The rate of false positive prediction is in the range of 0.1%. The fungal big-Pi tool successfully predicts the Gas1 mutation series described by C. Nuoffer and co-workers, and recognizes that the human PLAP C terminus is not a target for the fungal transamidase complex. Lists of potentially GPI lipid anchored proteins for five fungal proteomes have been generated and the hits have been functionally classified. The fungal big-Pi prediction WWW server as well as precursor lists are available at","authors":"Eisenhaber B, Schneider G, Wildpaner M, Eisenhaber F","authors_abbrev":"Eisenhaber B et al.","pubmed_publication_date":"19 Mar 2004","pubmed_entrez_date":"2004-03-09","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2178979","title":"Adenylyl cyclase activity of the fission yeast Schizosaccharomyces pombe is not regulated by guanyl nucleotides.","citation":"FEBS Lett 1990 Feb 26;261(2):413-8","abstract":"The adenylyl cyclase activity of the fission yeast Schizosaccharomyces pombe is localized to the plasma membrane of the cell. The enzyme utilizes Mn2+/ATP as substrate and free Mn2+ ions as an effector. Unlike the baker yeast Saccharomyces cerevisiae, S. pombe adenylyl cyclase does not utilize Mg2+/ATP as substrate and the activity is not stimulated by guanyl nucleotides. The optimal pH for the S. pombe adenylyl cyclase activity is 6.0. The activity dependence on ATP is cooperative with a Hill coefficient of 1.68 +/- 0.14.","authors":"Engelberg D, Poradosu E, Simchen G, Levitzki A","authors_abbrev":"Engelberg D et al.","pubmed_publication_date":"26 Feb 1990","pubmed_entrez_date":"1990-02-26","publication_year":"1990","canto_session_key":"a7bba768d717f074","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-27 11:55:01","canto_approved_date":"2020-01-23 13:24:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-27 11:54:54","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-27"},{"uniquename":"PMID:23950735","title":"Global analysis of fission yeast mating genes reveals new autophagy factors.","citation":"PLoS Genet 2013;9(8):e1003715","abstract":"Macroautophagy (autophagy) is crucial for cell survival during starvation and plays important roles in animal development and human diseases. Molecular understanding of autophagy has mainly come from the budding yeast Saccharomyces cerevisiae, and it remains unclear to what extent the mechanisms are the same in other organisms. Here, through screening the mating phenotype of a genome-wide deletion collection of the fission yeast Schizosaccharomyces pombe, we obtained a comprehensive catalog of autophagy genes in this highly tractable organism, including genes encoding three heretofore unidentified core Atg proteins, Atg10, Atg14, and Atg16, and two novel factors, Ctl1 and Fsc1. We systematically examined the subcellular localization of fission yeast autophagy factors for the first time and characterized the phenotypes of their mutants, thereby uncovering both similarities and differences between the two yeasts. Unlike budding yeast, all three Atg18/WIPI proteins in fission yeast are essential for autophagy, and we found that they play different roles, with Atg18a uniquely required for the targeting of the Atg12-Atg5·Atg16 complex. Our investigation of the two novel factors revealed unforeseen autophagy mechanisms. The choline transporter-like protein Ctl1 interacts with Atg9 and is required for autophagosome formation. The fasciclin domain protein Fsc1 localizes to the vacuole membrane and is required for autophagosome-vacuole fusion but not other vacuolar fusion events. Our study sheds new light on the evolutionary diversity of the autophagy machinery and establishes the fission yeast as a useful model for dissecting the mechanisms of autophagy.","doi":"10.1371/journal.pgen.1003715","authors":"Sun LL, Li M, Suo F, Liu XM, Shen EZ, Yang B, Dong MQ, He WZ, Du LL","authors_abbrev":"Sun LL et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-08-17","publication_year":"2013","canto_session_key":"7e33223e7aa2a9d8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Li-Lin Du","canto_first_approved_date":"2016-07-27 16:19:03","canto_approved_date":"2019-05-02 21:58:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-02-12 21:42:15","canto_added_date":"2013-08-21 16:57:16","annotation_curators":[{"name":"Li-Lin Du","community_curator":false,"annotation_count":65,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Li-Lin Du","file_curator_role":"community","annotation_file_curators":[{"name":"Li-Lin Du","community_curator":true,"annotation_count":228,"orcid":null,"file_type":"PHAF","file_name":"PMID_23950735_phaf.tsv"}],"genes":["SPAC4D7.10c","SPCC297.03","SPAC644.07","SPAC23H3.03c","SPAC926.03","SPAC664.03","YLR360W","SPCC1223.12c","SPAC6C3.04","SPAC25A8.02","SPBC3B8.02","SPBC16H5.13","SPCC31H12.08c","SPAC589.07c","SPBC17G9.10","SPBC31F10.14c","SPAC1610.02c","SPBC15D4.10c","SPAC222.12c","SPAC688.11","SPBC19C2.14","SPBC1215.01","SPBC14C8.17c","SPBC1D7.05","SPAC31A2.02","SPBC2D10.13","SPBC119.06","SPBC1D7.04","SPAC22F8.12c","SPBC29A3.14c","SPCC417.09c","SPAC824.04","SPAC1783.05","SPAC13C5.07","SPBC12D12.07c","SPBC17G9.02c","SPBC19G7.09","SPAC23E2.03c","SPAC8C9.03","SPAC10F6.11c","SPAC23C11.15","SPCC553.08c","SPBC29A3.18","SPCC1795.06","SPBC3H7.09","SPAC1F5.10","SPCC11E10.04","SPCC1840.03","SPCC4G3.04c","SPAC3G6.02","SPCC188.02","SPBC405.05","SPBC4F6.08c","SPBC26H8.05c","SPBC30B4.03c","SPAC19B12.08","SPBC4F6.06","SPBC18H10.11c","SPBC106.07c","SPAC1851.03","SPAP27G11.14c","SPCC162.05","SPBC691.04","SPBC4B4.07c","SPAC13C5.02","SPCC18.06c","SPCC188.07","SPAC31A2.11c","SPCC1682.01","SPBC215.03c","SPAC8C9.06c","SPCC74.02c","SPAC2E1P3.05c","SPAC1F7.01c","SPBC15D4.06","SPCC645.07","SPAC25H1.03","SPCC663.12","SPAC824.02","SPAC4A8.04","SPCC4B3.08","SPCC63.02c","SPCC613.10","SPBC530.01","SPCC757.04","SPAC22H10.07","SPCC613.12c","SPAC31G5.09c","SPAC16C9.05","SPAC823.10c","HGNC:12640","SPBC3B9.06c","SPAC4F10.07c","SPAC1556.08c","SPAC323.01c","SPBC4F6.10","SPBC713.08","SPBC4B4.10c","SPBC1604.02c","SPAC24H6.03","SPAPJ696.01c","SPAC6F6.09","SPBC3H7.12","SPBC776.04","SPBC31F10.10c","SPAC227.04","SPCC16C4.11","SPBC146.12","SPCC1672.04c","SPAC3A12.12","SPBC336.13c","SPAC227.17c","SPAC27E2.11c","SPBC2G2.07c","SPAC17H9.09c","SPBC16A3.07c","SPBC337.15c","SPBC6B1.05c","SPBC646.13","SPAC6B12.15","SPCC1235.09","SPBC4C3.12","SPAC1071.11","SPAC144.02","SPBC28E12.04","SPCC63.08c","SPAC22H12.05c","SPBC19C7.02","SPBC3E7.15c","SPBC1289.06c","SPBC31E1.01c","SPCC1442.01","SPBC146.13c","SPAC637.07","SPAC222.04c","SPBC30D10.13c","SPBC365.10","SPBC17A3.05c","SPBC21.05c","SPCC830.06","SPAC22H10.09","SPBC16A3.03c","SPCPJ732.01","SPAC4D7.03","SPBC106.04","SPAC1B3.17","SPBC1198.11c","SPAC458.06","SPBC887.13c","SPAC22F8.11","SPBC428.02c","SPCC1753.05","SPAC1687.12c","SPBP8B7.24c","SPBC12C2.02c","SPAC1006.03c","SPAC1B2.04","SPAC8C9.19","SPCC1840.09","SPBC3E7.04c","SPBC27B12.08","SPBC1105.10","SPBC25H2.11c","SPBC19G7.16","SPAC227.01c","SPBC428.08c","SPAC19G12.11","SPBP35G2.07","SPBC15D4.07c","SPBC16A3.18","SPAC14C4.14","SPAC20G8.10c","SPAC2F7.07c","SPBC27.06c","SPAC1D4.13","SPBC947.02","SPBC800.07c","SPAC6B12.12","SPBC365.14c","SPCC622.16c","SPAC4G8.13c","SPBC21B10.13c","SPAC2F7.17","SPBC1709.09","SPBC18H10.19","SPBC1604.20c","YMR159C","SPCC1682.11c","SPAC4G8.11c","SPBC29A3.10c","SPAC7D4.04","SPAC4F10.20","SPAC823.16c","SPBPJ4664.01","SPBC1718.03","SPAC23C4.16c","SPAC3C7.12","SPAC4F8.03","SPCC16A11.07","SPBC1604.08c","SPBC23E6.08","SPAC23C11.10","SPAC17G8.05","SPAC17A2.06c","SPBC31F10.15c","SPAPB2B4.03","SPBC16H5.06","SPAC1565.04c","SPCC1739.07","SPAC323.05c","SPAC1783.06c","SPBC24C6.06","SPBP4H10.04","SPBC2D10.18","SPAC17G6.08"],"gene_count":212,"ltp_gene_count":23,"approved_date":"2016-07-27"},{"uniquename":"PMID:14657251","title":"Meiosis-specific failure of cell cycle progression in fission yeast by mutation of a conserved beta-tubulin residue.","citation":"Mol Biol Cell 2004 Mar;15(3):1160-71","abstract":"The microtubule cytoskeleton is involved in regulation of cell morphology, differentiation, and cell cycle progression. Precisely controlled dynamic properties are required for these microtubule functions. To better understand how tubulin's dynamics are embedded in its primary sequence, we investigated in vivo the consequences of altering a single, highly conserved residue in beta-tubulin that lies at the interface between two structural domains. The residue differs between the cold-adapted Antarctic fish and temperate animals in a manner that suggests a role in microtubule stability. Fungi, like the Antarctic fish, have a phenylalanine in this position, whereas essentially all other animals have tyrosine. We mutated the corresponding residue in fission yeast to tyrosine. Temperature effects were subtle, but time-lapse microscopy of microtubule dynamics revealed reduced depolymerization rates and increased stability. Mitotic exit signaled by breakdown of the mitotic spindle was delayed. In meiosis, microtubules displayed prolonged contact to the cell cortex during horsetail movement, followed by completion of meiosis I but frequent asymmetric failure of meiosis II spindle formation. Our results indicate that depolymerization dynamics modulated through interdomain motion may be important for regulating a subset of plus-end microtubule complexes in Schizosaccharomyces pombe.","authors":"Paluh JL, Killilea AN, Detrich HW, Downing KH","authors_abbrev":"Paluh JL et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2003-12-06","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9230688","title":"A telomerase mutant defective in sister chromatid separation at mitosis.","citation":"Bioessays 1997 Jul;19(7):557-9","abstract":"The telomere is a functional domain of the chromosome, located at the extreme ends, and is essential for normal chromosome stability. Chromosomes lacking telomeres are inherited improperly, and mutations in the telomeric repeat sequences are thought to lead to senescence and possibly to cancer. The molecular mechanisms maintaining chromosomes by telomeres, however, have been unclear. Results recently reported by Kirk et al, offer an insight into new telomerase function. They have identified a novel telomerase mutation that blocks sister chromatid separation in mitosis.","authors":"Nakaseko Y, Yanagida M","authors_abbrev":"Nakaseko Y et al.","pubmed_publication_date":"Jul 1997","pubmed_entrez_date":"1997-07-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR11362","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2F12.10","HGNC:14033"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29192673","title":"TRFH domain: at the root of telomere protein evolution?","citation":"Cell Res 2018 Jan;28(1):7-8","abstract":"Two articles in Cell Research focus on the structure-function relationships in the shelterin complex that binds to telomeres and is essential for their stability and functions. These studies concerning both mammalian and Schizosaccharomyces pombe proteins reveal unexpected structural conservation of a motif called TRFH (Telomeric Repeat Factors Homology) domain between several subunits in these complexes, providing a rationale for further dissection of the role of telomeres in chromosome stability, aging and cancer, and encouraging us to revisit the evolution of telomere proteins.","doi":"10.1038/cr.2017.152","authors":"Giraud-Panis MJ, Ye J, Gilson E","authors_abbrev":"Giraud-Panis MJ et al.","pubmed_publication_date":"Jan 2018","pubmed_entrez_date":"2017-12-02","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-12-03 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11509236","title":"Myosin V-mediated vacuole distribution and fusion in fission yeast.","citation":"Curr Biol 2001 Jul 24;11(14):1124-7","abstract":"The class V myosins are actin-based motors that move a variety of cellular cargoes [1]. In budding yeast, their activity includes the relocation of a portion of the vacuole from the mother cell to the bud [2, 3]. Fission yeast cells contain numerous (approximately 80) small vacuoles. When S. pombe cells are placed in water, vacuoles fuse in response to osmotic stress [4]. Fission yeast possess two type V myosin genes, myo51(+) and myo52(+) [5]. In a myo51Delta strain, vacuoles were distributed throughout the cell, and mean vacuole diameter was identical to that seen in wild-type cells. When myo51Delta and wild-type cells were placed in water, vacuoles enlarged by fusion. In myo52Delta cells, by contrast, vacuoles were smaller and mostly clustered around the nucleus, and fusion in water was largely inhibited. When cells containing GFP-Myo52 were placed in water, Myo52 was seen to redistribute from the cell poles to the surface of the fusing vacuoles. Vacuole fusion in fission yeast was inhibited by the microtubule drug thiabendazole (TBZ) but not by the actin inhibitor latrunculin B. This is the first demonstration of the involvement of a type V myosin, possibly via an interaction with microtubules, in homotypic membrane fusion.","authors":"Mulvihill DP, Pollard PJ, Win TZ, Hyams JS","authors_abbrev":"Mulvihill DP et al.","pubmed_publication_date":"24 Jul 2001","pubmed_entrez_date":"2001-08-18","publication_year":"2001","canto_session_key":"77b8b1e0a2875e4f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-15 20:55:12","canto_approved_date":"2024-06-15 20:55:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 12:49:24","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.14c","SPCC1919.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-06-15"},{"uniquename":"PMID:26325630","title":"One step closer to understanding mammalian macroautophagy initiation: Interplay of 2 HORMA architectures in the ULK1 complex.","citation":"Autophagy 2015 Nov 02;11(11):1953-1955","abstract":"ULK1 and ATG13 assemble with RB1CC1/FIP200 and ATG101 to form a macroautophagy (hereafter autophagy) induction (ULK1) complex in higher eukaryotes. The yeast counterpart, the Atg1 complex, is comprised of Atg1 and Atg13 (ULK1 and ATG13 homologs), Atg17 (a proposed functional homolog of RB1CC1), and either the Atg101 subunit (in Schizosaccharomyces pombe) or the Atg29-Atg31 heterodimer (in Saccharomyces cerevisiae). With mutual exclusivity of, and no detectable homology between, the Atg29-Atg31 dimer and Atg101, knowledge about the roles of these proteins in autophagy induction is an important piece in the puzzle of understanding the molecular mechanism of autophagy initiation. A recent study reporting the structure of the S. pombe homolog Atg101 bound to the Atg13 HORMA  domain is a notable contribution to this knowledge (see the punctum in this issue of the journal).","authors":"Popelka H, Klionsky DJ","authors_abbrev":"Popelka H et al.","pubmed_publication_date":"02 Nov 2015","pubmed_entrez_date":"2015-09-02","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-09-03 00:22:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16627999","title":"The fission yeast APC activator Ste9 is regulated by mRNA decay.","citation":"Cell Cycle 2006 Apr;5(8):865-8","abstract":"Fission yeast Ste9/Srw1 is a family member of the Fizzy-related APC activators that promote the ubiquitination and degradation of mitotic cyclins and other substrates at the end of mitosis and G1. These proteins are highly regulated during the cell cycle at the level of gene transcription and protein phosphorylation in order to guarantee the correct order of events during the cell cycle. Here we propose mRNA decay as a novel mechanism that regulates ste9+ gene expression during the cell cycle. We have characterized the elements in the 3'UTR of the ste9 mRNA responsible for this mechanism. Moreover, we demonstrate that the instability of ste9 mRNA is important for downregulating Ste9 levels in G2, allowing appropriate cyclin B accumulation to promote timely entry into mitosis.","authors":"Alvarez B, Blanco MA, Moreno S","authors_abbrev":"Alvarez B et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-04-22","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12894167","title":"Targeted movement of cell end factors in fission yeast.","citation":"Nat Cell Biol 2003 Sep;5(9):812-8","abstract":"Kinesins are microtubule-based motor proteins that transport cargo to specific locations within the cell. However, the mechanisms by which cargoes are directed to specific cellular locations have remained elusive. Here, we investigated the in vivo movement of the Schizosaccharomyces pombe kinesin Tea2 to establish how it is targeted to microtubule tips and cell ends. Tea2 is loaded onto microtubules in the middle of the cell, in close proximity to the nucleus, and then travels using its intrinsic motor activity primarily at the tips of polymerizing microtubules. The microtubule-associated protein Mal3, an EB1 homologue, is required for loading and/or processivity of Tea2 and this function can be substituted by human EB1. In addition, the cell-end marker Tea1 is required to anchor Tea2 to cell ends. Movement of Tea1 and the CLIP170 homologue Tip1 to cell ends is abolished in Tea2 rigor (ATPase) mutants. We propose that microtubule-based transport from the vicinity of the nucleus to cell ends can be precisely regulated, with Mal3 required for loading/processivity, Tea2 for movement and Tea1 for cell-end anchoring.","authors":"Browning H, Hackney DD, Nurse P","authors_abbrev":"Browning H et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-08-02","publication_year":"2003","canto_session_key":"edfddf218bf755ae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-02-11 11:34:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-01 20:26:42","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.20c","SPAC18G6.15","SPCC1223.06","SPAC3C7.12"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2016-11-01"},{"uniquename":"PMID:7836423","title":"Protein kinase Byr2 is a target of Ras1 in the fission yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1995 Feb 03;270(5):1979-82","abstract":"Conservation of the structure and function of Ras proteins has been observed in a variety of eukaryotic organisms. However, the nature of their downstream effectors appears to be quite divergent; adenylyl cyclase and a protein kinase Raf-1, which do not share any structural homology with each other, are effectors of Ras in the budding yeast and in higher organisms, respectively. We show here that a protein kinase Byr2, which has been known to act downstream of Ras1 in a mating pheromone signal transduction system of Schizosaccharomyces pombe, binds directly to Ras proteins in a GTP-dependent manner. The region of Byr2 responsible for the Ras binding was mapped by a gene deletion analysis to its N-terminal segment of 206 amino acid residues, which does not possess any significant homology with the other effectors of Ras. The affinity of the Byr2 N terminus for Saccharomyces cerevisiae Ras2 was determined by measuring its activity to competitively inhibit Ras-dependent adenylyl cyclase activity and found to be comparable with those of yeast adenylyl cyclase and human Raf-1, with a dissociation constant (Kd) of about 1 nM. Furthermore, Byr2 inhibited a Ras GTPase-activating activity of Ira2, a S. cerevisiae homologue of neurofibromin. These results indicate that Byr2 is an immediate downstream target of Ras1 in S. pombe.","authors":"Masuda T, Kariya K, Shinkai M, Okada T, Kataoka T","authors_abbrev":"Masuda T et al.","pubmed_publication_date":"03 Feb 1995","pubmed_entrez_date":"1995-02-03","publication_year":"1995","canto_session_key":"401175fa48a0f4a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-11-02 11:18:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-29 10:36:59","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC1D7.05"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2013-10-29"},{"uniquename":"PMID:24963140","title":"Genome rearrangements and pervasive meiotic drive cause hybrid infertility in fission yeast.","citation":"Elife 2014 Jun 24;3:e02630","abstract":"Hybrid sterility is one of the earliest postzygotic isolating mechanisms to evolve between two recently diverged species. Here we identify causes underlying hybrid infertility of two recently diverged fission yeast species Schizosaccharomyces pombe and S. kambucha, which mate to form viable hybrid diploids that efficiently complete meiosis, but generate few viable gametes. We find that chromosomal rearrangements and related recombination defects are major but not sole causes of hybrid infertility. At least three distinct meiotic drive alleles, one on each S. kambucha chromosome, independently contribute to hybrid infertility by causing nonrandom spore death. Two of these driving loci are linked by a chromosomal translocation and thus constitute a novel type of paired meiotic drive complex. Our study reveals how quickly multiple barriers to fertility can arise. In addition, it provides further support for models in which genetic conflicts, such as those caused by meiotic drive alleles, can drive speciation.DOI: http://dx.doi.org/10.7554/eLife.02630.001.","doi":"10.7554/eLife.02630","authors":"Zanders SE, Eickbush MT, Yu JS, Kang JW, Fowler KR, Smith GR, Malik HS","authors_abbrev":"Zanders SE et al.","pubmed_publication_date":"24 Jun 2014","pubmed_entrez_date":"2014-06-26","publication_year":"2014","canto_session_key":"21c4c41f4af7f470","canto_annotation_status":"APPROVED","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_first_approved_date":"2020-01-07 16:01:49","canto_approved_date":"2020-01-07 16:01:49","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-01-07 15:59:21","canto_added_date":"2014-06-26 17:50:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2020-01-07"},{"uniquename":"PMID:27587357","title":"The conundrum of UDP-Glc entrance into the yeast ER lumen.","citation":"Glycobiology 2017 Jan;27(1):64-79","abstract":"UDP-Glc entrance into the endoplasmic reticulum (ER) of eukaryotic cells is a key step in the quality control of glycoprotein folding, a mechanism requiring transfer of a Glc residue from the nucleotide sugar (NS) to glycoprotein folding intermediates by the UDP-Glc:glycoprotein glucosyltransferase (UGGT). According to a bioinformatics search there are only eight genes in the Schizosaccharomyces pombe genome belonging to the three Pfam families to which all known nucleotide-sugar transporters (NSTs) of the secretory pathway belong. The protein products of two of them (hut1 +  and yea4 + ) localize to the ER, those of genes gms1 + , vrg4 + , pet1 + , pet2 +  and pet3 +  to the Golgi, whereas that of gms2 +  has an unknown location. Here we demonstrate that (1) Δhut1 and Δgpt1 (UGGT null) mutants share several phenotypic features; (2) Δhut1 mutants show a 50% reduction in UDP-Glc transport into ER-derived membranes; (3) in vivo UDP-Glc ER entrance occurred in Δhut1Δyea4Δgms2 mutants and in cells in which Δhut1 disruption was combined with that of each of four of the genes encoding Golgi-located proteins. Therefore, disruption of all genes whose products localize to the ER or have an unknown location did not obliterate UDP-Glc ER entrance. We conclude that the hut1 +  gene product is involved in UDP-Glc entrance into the ER, but that at least another as yet unknown NST displaying an unconventional sequence operates in the yeast secretory pathway. This conclusion agrees with our previous results showing that UDP-Glc entrance into the yeast ER does not follow the classical NST antiport mechanism.","doi":"10.1093/glycob/cww092","authors":"Bredeston LM, Marino-Buslje C, Mattera VS, Buzzi LI, Parodi AJ, D'Alessio C","authors_abbrev":"Bredeston LM et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2016-09-03","publication_year":"2017","canto_session_key":"38ddd4fc7a5de776","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Cecilia D'Alessio","canto_first_approved_date":"2017-10-30 14:16:50","canto_approved_date":"2025-10-07 06:53:22","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-10-20 18:30:37","canto_added_date":"2016-09-04 00:15:11","annotation_curators":[{"name":"Cecilia D'Alessio","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.01","SPAC12G12.12","SPBC342.01c","SPAC144.18","SPAC22F8.04","SPBC83.11","SPCC1795.03","SPBPJ4664.06","SPBC56F2.10c","SPBC839.11c","SPBC1734.09"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2017-10-30"},{"uniquename":"PMID:19750564","title":"MPR1 as a novel selection marker in Saccharomyces cerevisiae.","citation":"Yeast 2009 Nov;26(11):587-93","abstract":"L-Azetidine-2-carboxylic acid (AZC) is a toxic four-membered ring analogue of L-proline that is transported into cells by proline transporters. AZC and L-proline in the cells are competitively incorporated into nascent proteins. When AZC is present in a minimum medium, misfolded proteins are synthesized in the cells, thereby inhibiting cell growth. The MPR1 gene has been isolated from the budding yeast Saccharomyces cerevisiae Sigma1278b as a multicopy suppressor of AZC-induced growth inhibition. MPR1 encodes a novel acetyltransferase that detoxifies AZC via N-acetylation. Since MPR1 is absent in the laboratory strain of S. cerevisiae S288C, it could be a positive selection marker that confers AZC resistance in the S288C background strains. To examine the usefulness of MPR1, we constructed some plasmid vectors that harboured MPR1 under the control of various promoters and introduced them into the S288C-derived strains. The expression of MPR1 conferred AZC resistance that was largely dependent on the expression level of MPR1. In an additional experiment, the galactose-inducible MPR1 and ppr1(+), the fission yeast Schizosaccharomyces pombe homologue of MPR1, were used for gene disruption by homologous recombination, and here AZC-resistant colonies were also successfully selected. We concluded that our MPR1-AZC system provides a powerful tool for yeast transformation.","doi":"10.1002/yea.1708","authors":"Ogawa-Mitsuhashi K, Sagane K, Kuromitsu J, Takagi H, Tsukahara K","authors_abbrev":"Ogawa-Mitsuhashi K et al.","pubmed_publication_date":"Nov 2009","pubmed_entrez_date":"2009-09-15","publication_year":"2009","canto_session_key":"0aa2289de82202ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-30 23:02:41","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 23:02:34","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC21E11.04"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-30"},{"uniquename":"PMID:23628481","title":"A proteome-wide visual screen identifies fission yeast proteins localizing to DNA double-strand breaks.","citation":"DNA Repair (Amst) 2013 Jun 01;12(6):433-43","abstract":"DNA double-strand breaks (DSBs) are a major threat to genome integrity. Proteins involved in DNA damage checkpoint signaling and DSB repair often relocalize and concentrate at DSBs. Here, we used an ORFeome library of the fission yeast Schizosaccharomyces pombe to systematically identify proteins targeted to DSBs. We found 51 proteins that, when expressed from a strong exogenous promoter on the ORFeome plasmids, were able to form a distinct nuclear focus at an HO endonuclease-induced DSB. The majority of these proteins have known connections to DNA damage response, but few have been visualized at a specific DSB before. Among the screen hits, 37 can be detected at DSBs when expressed from native promoters. We classified them according to the focus emergence timing of the endogenously tagged proteins. Eight of these 37 proteins are yet unnamed. We named these eight proteins DNA-break-localizing proteins (Dbls) and performed preliminary functional analysis on two of them, Dbl1 (SPCC2H8.05c) and Dbl2 (SPCC553.01c). We found that Dbl1 and Dbl2 contribute to the normal DSB targeting of checkpoint protein Rad26 (homolog of human ATRIP) and DNA repair helicase Fml1 (homolog of human FANCM), respectively. As the first proteome-wide inventory of DSB-localizing proteins, our screen result will be a useful resource for understanding the mechanisms of eukaryotic DSB response.","doi":"10.1016/j.dnarep.2013.04.001","authors":"Yu Y, Ren JY, Zhang JM, Suo F, Fang XF, Wu F, Du LL","authors_abbrev":"Yu Y et al.","pubmed_publication_date":"01 Jun 2013","pubmed_entrez_date":"2013-05-01","publication_year":"2013","canto_session_key":"86b26767a12a86ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li-Lin Du","canto_first_approved_date":"2013-09-19 15:21:19","canto_approved_date":"2022-04-03 07:47:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-21 16:36:33","canto_added_date":"2013-05-23 11:27:13","annotation_curators":[{"name":"Li-Lin Du","community_curator":true,"annotation_count":37,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8F11.03","SPAC9.05","SPBC28F2.07","SPAC1952.07","SPAC1687.05","SPCC23B6.05c","SPBC16G5.12c","SPAC9E9.08","SPAC15A10.03c","SPAC23C4.18c","SPCC2H8.05c","SPAC13G6.01c","SPBC16A3.11","SPBC342.05","SPBC660.13c","SPBC29A10.10c","SPAC3H5.06c","SPCC553.01c","SPCC1259.13","SPBC14C8.09c","SPBC16C6.04","SPBC4F6.15c","SPAC19A8.10","SPAC20H4.07","SPBC16D10.04c","SPBC1347.01c","SPBC1347.10","SPBC651.12c","SPBC409.16c","SPCC1753.01c","SPAC30D11.10","SPAC20G4.04c","SPBC582.05c","SPAC3G6.11","SPAC8F11.07c","SPCC548.05c","SPAC3C7.03c","SPBC887.14c","SPAC328.02"],"gene_count":39,"ltp_gene_count":37,"approved_date":"2013-09-19"},{"uniquename":"PMID:16823372","title":"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.","citation":"Nat Biotechnol 2006 Jul;24(7):841-7","abstract":"Cloning of the entire set of an organism's protein-coding open reading frames (ORFs), or 'ORFeome', is a means of connecting the genome to downstream 'omics' applications. Here we report a proteome-scale study of the fission yeast Schizosaccharomyces pombe based on cloning of the ORFeome. Taking advantage of a recombination-based cloning system, we obtained 4,910 ORFs in a form that is readily usable in various analyses. First, we evaluated ORF prediction in the fission yeast genome project by expressing each ORF tagged at the 3' terminus. Next, we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein. Furthermore, using leptomycin B, an inhibitor of the nuclear export protein Crm1, we identified 285 proteins whose localization is regulated by Crm1.","authors":"Matsuyama A, Arai R, Yashiroda Y, Shirai A, Kamata A, Sekido S, Kobayashi Y, Hashimoto A, Hamamoto M, Hiraoka Y, Horinouchi S, Yoshida M","authors_abbrev":"Matsuyama A et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-07-11","publication_year":"2006","canto_session_key":"e442ede7e2d1dbdb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2012-11-13 13:18:08","canto_approved_date":"2024-09-11 11:36:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-13 13:17:39","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori 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of a Mitochondrial DNA Polymerase Affecting Cardiotoxicity of Sunitinib Using a Genome-Wide Screening on S. pombe Deletion Library.","citation":"Toxicol Sci 2016 Jan;149(1):4-14","abstract":"Drug toxicity is a key issue for drug R&D, a fundamental challenge of which is to screen for the targets genome-wide. The anticancer tyrosine kinase inhibitor sunitinib is known to induce cardiotoxicity. Here, to understand the molecular insights of cardiotoxicity by sunitinib at the genome level, we used a genome-wide drug target screening technology (GPScreen) that measures drug-induced haploinsufficiency (DIH) in the fission yeast Schizosaccharomyces pombe genome-wide deletion library and found a mitochondrial DNA polymerase (POG1). In the results, sunitinib induced more severe cytotoxicity and mitochondrial damage in POG1-deleted heterozygous mutants compared to wild type (WT) of S. pombe. Furthermore, knockdown of the human ortholog POLG of S. pombe POG1 in human cells significantly increased the cytotoxicity of sunitinib. Notably, sunitinib dramatically decreased the levels of POLG mRNAs and proteins, of which downregulation was already known to induce mitochondrial damage of cardiomyocytes, causing cardiotoxicity. These results indicate that POLG might play a crucial role in mitochondrial damage as a gene of which expressional pathway is targeted by sunitinib for cardiotoxicity, and that genome-wide drug target screening with GPScreen can be applied to drug toxicity target discovery to understand the molecular insights regarding drug toxicity.","doi":"10.1093/toxsci/kfv210","authors":"Kim DM, Kim H, Yeon JH, Lee JH, Park HO","authors_abbrev":"Kim DM et al.","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2015-09-20","publication_year":"2016","canto_session_key":"48e19f4911beba5f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-23 14:06:36","canto_approved_date":"2019-06-14 08:29:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-23 14:06:29","canto_added_date":"2015-09-21 00:18:56","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC24B10.22"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-23"},{"uniquename":"PMID:39717400","title":"Enhancing wine fermentation through concurrent utilization of  Lachancea thermotolerans  and lactic acid bacteria ( Oenococcus oeni  and  Lactiplantibacillus plantarum ) or  Schizosaccharomyces pombe .","citation":"Food Chem X 2024 Dec 30;24:102054","abstract":"Most commercially available red wines undergo alcoholic fermentation by  Saccharomyces  yeasts, followed by a second fermentation with the lactic acid bacteria  Oenococcus oeni  once the initial process is complete. However, this traditional approach can encounter complications in specific scenarios. These situations pose risks such as stalled alcoholic fermentation or the growth of undesirable bacteria while the process remains incomplete, leaving residual sugars in the wine. To address these challenges and the issue of low acidity prevalent in warmer viticultural regions, several novel alternatives are available. The alternatives involve the combined use of  Lachancea thermotolerans  to increase the acidity of the musts, lactic acid bacteria ( Oenococcus oeni  and  Lactiplantibacillus plantarum ) to ensure malic acid stability during early alcoholic fermentation stages, and  Saccharomyces cerevisiae  to properly complete alcoholic fermentation. The study showed variations in the final chemical parameters of wines based on the microorganisms used.","doi":"10.1016/j.fochx.2024.102054","authors":"Vicente J, Wang L, Brezina S, Fritsch S, Navascués E, Santos A, Calderón F, Tesfaye W, Marquina D, Rauhut D, Benito S","authors_abbrev":"Vicente J et al.","pubmed_publication_date":"30 Dec 2024","pubmed_entrez_date":"2024-12-24","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-12-25 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12631727","title":"The fission yeast spo14+ gene encoding a functional homologue of budding yeast Sec12 is required for the development of forespore membranes.","citation":"Mol Biol Cell 2003 Mar;14(3):1109-24","abstract":"The Schizosaccharomyces pombe spo14-B221 mutant was originally isolated as a sporulation-deficient mutant. However, the spo14(+) gene is essential for cell viability and growth. spo14(+) is identical to the previously characterized stl1(+) gene encoding a putative homologue of Saccharomyces cerevisiae Sec12, which is essential for protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus. In the spo14 mutant cells, ER-like membranes were accumulated beneath the plasma membrane and the ER/Golgi shuttling protein Rer1 remained in the ER. Sec12 is a guanine nucleotide exchange factor for the Sar1 GTPase. Overproduction of psr1(+) coding for an S. pombe Sar1 homologue suppressed both the sporulation defect of spo14-B221 and cold-sensitive growth of newly isolated spo14-6 and spo14-7 mutants. These results indicate that Spo14 is involved in early steps of the protein secretory pathway. The spo14-B221 allele carries a single nucleotide change in the branch point consensus of the fifth intron, which reduces the abundance of the spo14 mRNA. During meiosis II, the forespore membrane was initiated near spindle pole bodies; however, subsequent extension of the membrane was arrested before its closure into a sac. We conclude that Spo14 is responsible for the assembly of the forespore membrane by supplying membrane vesicles.","authors":"Nakamura-Kubo M, Nakamura T, Hirata A, Shimoda C","authors_abbrev":"Nakamura-Kubo M et al.","pubmed_publication_date":"Mar 2003","pubmed_entrez_date":"2003-03-13","publication_year":"2003","canto_session_key":"bcc4dde202655d0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-30 10:25:00","canto_approved_date":"2026-03-30 14:32:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-30 10:24:53","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.05c","SPBC31F10.06c","SPBC3H7.01"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-10-30"},{"uniquename":"PMID:4309177","title":"Regulation of the biosynthesis of purine nucleotides in Schizosaccharomyces pombe. II. Kinetic studies of IMP dehydrogenase.","citation":"Biochim Biophys Acta 1969;185(2):310-5","abstract":"","authors":"Pourquie J","authors_abbrev":"Pourquie J","pubmed_publication_date":"1969","pubmed_entrez_date":"1969-01-01","publication_year":"1969","canto_session_key":"8a0da786fa9e1aed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-09-25 13:42:56","canto_approved_date":"2020-01-17 18:58:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-25 13:14:34","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-25"},{"uniquename":"PMID:23732911","title":"A stress-activated, p38 mitogen-activated protein kinase-ATF/CREB pathway regulates posttranscriptional, sequence-dependent decay of target RNAs.","citation":"Mol Cell Biol 2013 Aug;33(15):3026-35","abstract":"Broadly conserved, mitogen-activated/stress-activated protein kinases (MAPK/SAPK) of the p38 family regulate multiple cellular processes. They transduce signals via dimeric, basic leucine zipper (bZIP) transcription factors of the ATF/CREB family (such as Atf2, Fos, and Jun) to regulate the transcription of target genes. We report additional mechanisms for gene regulation by such pathways exerted through RNA stability controls. The Spc1 (Sty1/Phh1) kinase-regulated Atf1-Pcr1 (Mts1-Mts2) heterodimer of the fission yeast Schizosaccharomyces pombe controls the stress-induced, posttranscriptional stability and decay of sets of target RNAs. Whole transcriptome RNA sequencing data revealed that decay is associated nonrandomly with transcripts that contain an M26 sequence motif. Moreover, the ablation of an M26 sequence motif in a target mRNA is sufficient to block its stress-induced loss. Conversely, engineered M26 motifs can render a stable mRNA into one that is targeted for decay. This stress-activated RNA decay (SARD) provides a mechanism for reducing the expression of target genes without shutting off transcription itself. Thus, a single p38-ATF/CREB signal transduction pathway can coordinately induce (promote transcription and RNA stability) and repress (promote RNA decay) transcript levels for distinct sets of genes, as is required for developmental decisions in response to stress and other stimuli.","doi":"10.1128/MCB.00349-13","authors":"Gao J, Wagnon JL, Protacio RM, Glazko GV, Beggs M, Raj V, Davidson MK, Wahls WP","authors_abbrev":"Gao J et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-06-05","publication_year":"2013","canto_session_key":"316d428e67c14527","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16566825","title":"The time-profile of cell growth in fission yeast: model selection criteria favoring bilinear models over exponential ones.","citation":"Theor Biol Med Model 2006 Mar 27;3:16","abstract":"There is considerable controversy concerning the exact growth profile of size parameters during the cell cycle. Linear, exponential and bilinear models are commonly considered, and the same model may not apply for all species. Selection of the most adequate model to describe a given data-set requires the use of quantitative model selection criteria, such as the partial (sequential) F-test, the Akaike information criterion and the Schwarz Bayesian information criterion, which are suitable for comparing differently parameterized models in terms of the quality and robustness of the fit but have not yet been used in cell growth-profile studies.\nLength increase data from representative individual fission yeast (Schizosaccharomyces pombe) cells measured on time-lapse films have been reanalyzed using these model selection criteria. To fit the data, an extended version of a recently introduced linearized biexponential (LinBiExp) model was developed, which makes possible a smooth, continuously differentiable transition between two linear segments and, hence, allows fully parametrized bilinear fittings. Despite relatively small differences, essentially all the quantitative selection criteria considered here indicated that the bilinear model was somewhat more adequate than the exponential model for fitting these fission yeast data.\nA general quantitative framework was introduced to judge the adequacy of bilinear versus exponential models in the description of growth time-profiles. For single cell growth, because of the relatively limited data-range, the statistical evidence is not strong enough to favor one model clearly over the other and to settle the bilinear versus exponential dispute. Nevertheless, for the present individual cell growth data for fission yeast, the bilinear model seems more adequate according to all metrics, especially in the case of wee1Delta cells.","authors":"Buchwald P, Sveiczer A","authors_abbrev":"Buchwald P et al.","pubmed_publication_date":"27 Mar 2006","pubmed_entrez_date":"2006-03-29","publication_year":"2006","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15530381","title":"DNA replication: stalling a fork for imprinting and switching.","citation":"Curr Biol 2004 Nov 09;14(21):R915-7","abstract":"Mating-type switching in fission yeast has long been known to be directed by a DNA 'imprint'. This imprint has now been firmly characterized as a protected site-specific and strand-specific nick. New work also links the widely conserved Swi1-Swi3 complex to the protection of stalled replication forks in general.","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"09 Nov 2004","pubmed_entrez_date":"2004-11-09","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20056877","title":"Molecular biology. Directing the centromere guardian.","citation":"Science 2010 Jan 08;327(5962):150-1","abstract":"","doi":"10.1126/science.1184770","authors":"Javerzat JP","authors_abbrev":"Javerzat JP","pubmed_publication_date":"08 Jan 2010","pubmed_entrez_date":"2010-01-09","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11741546","title":"Human Mus81-associated endonuclease cleaves Holliday junctions in vitro.","citation":"Mol Cell 2001 Nov;8(5):1117-27","abstract":"Mus81, a protein with homology to the XPF subunit of the ERCC1-XPF endonuclease, is important for replicational stress tolerance in both budding and fission yeast. Human Mus81 has associated endonuclease activity against structure-specific oligonucleotide substrates, including synthetic Holliday junctions. Mus81-associated endonuclease resolves Holliday junctions into linear duplexes by cutting across the junction exclusively on strands of like polarity. In addition, Mus81 protein abundance increases in cells following exposure to agents that block DNA replication. Taken together, these findings suggest a role for Mus81 in resolving Holliday junctions that arise when DNA replication is blocked by damage or by nucleotide depletion. Mus81 is not related by sequence to previously characterized Holliday junction resolving enzymes, and it has distinct enzymatic properties that suggest it uses a novel enzymatic strategy to cleave Holliday junctions.","authors":"Chen XB, Melchionna R, Denis CM, Gaillard PHL, Blasina A, Van de Weyer I, Boddy MN, Russell P, Vialard J, McGowan CH","authors_abbrev":"Chen XB et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2001-12-14","publication_year":"2001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4G3.05c","SPAPB1E7.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:26804917","title":"Spatiotemporal Control of Forkhead Binding to DNA Regulates the Meiotic Gene Expression Program.","citation":"Cell Rep 2016 Feb 02;14(4):885-895","abstract":"Meiosis is a differentiated program of the cell cycle that is characterized by high levels of recombination followed by two nuclear divisions. In fission yeast, the genetic program during meiosis is regulated at multiple levels, including transcription, mRNA stabilization, and splicing. Mei4 is a forkhead transcription factor that controls the expression of mid-meiotic genes. Here, we describe that Fkh2, another forkhead transcription factor that is essential for mitotic cell-cycle progression, also plays a pivotal role in the control of meiosis. Fkh2 binding preexists in most Mei4-dependent genes, inhibiting their expression. During meiosis, Fkh2 is phosphorylated in a CDK/Cig2-dependent manner, decreasing its affinity for DNA, which creates a window of opportunity for Mei4 binding to its target genes. We propose that Fkh2 serves as a placeholder until the later appearance of Mei4 with a higher affinity for DNA that induces the expression of a subset of meiotic genes.","doi":"10.1016/j.celrep.2015.12.074","authors":"Alves-Rodrigues I, Ferreira PG, Moldón A, Vivancos AP, Hidalgo E, Guigó R, Ayté J","authors_abbrev":"Alves-Rodrigues I et al.","pubmed_publication_date":"02 Feb 2016","pubmed_entrez_date":"2016-01-26","publication_year":"2016","canto_session_key":"883442658ddcd9a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jose Ayte","canto_first_approved_date":"2017-12-29 20:40:32","canto_approved_date":"2025-09-03 17:46:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-15 11:24:52","canto_added_date":"2016-01-27 01:15:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jose Ayte","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.11","SPBC11B10.09","SPBC16G5.15c","SPAPB2B4.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-12-29"},{"uniquename":"PMID:23977061","title":"Regulation of cell wall synthesis by the clathrin light chain is essential for viability in Schizosaccharomyces pombe.","citation":"PLoS One 2013;8(8):e71510","abstract":"The regulation of cell wall synthesis by the clathrin light chain has been addressed. Schizosaccharomyces pombe clc1Δ mutant was inviable in the absence of osmotic stabilization; when grown in sorbitol-supplemented medium clc1Δ cells grew slowly, formed aggregates, and had strong defects in morphology. Additionally, clc1Δ cells exhibited an altered cell wall composition. A mutant that allowed modulating the amount of Clc1p was created to analyze in more detail the dependence of cell wall synthesis on clathrin. A 40% reduction in the amount of Clc1p did not affect acid phosphatase secretion and bulk lipid internalization. Under these conditions, β(1,3)glucan synthase activity and cell wall synthesis were reduced. Also, the delivery of glucan synthases to the cell surface, and the secretion of the Eng1p glucanase were defective. These results suggest that the defects in the cell wall observed in the conditional mutant were due to a defective secretion of enzymes involved in the synthesis/remodelling of this structure, rather than to their endocytosis. Our results show that a reduction in the amount of clathrin that has minor effects on general vesicle trafficking has a strong impact on cell wall synthesis, and suggest that this is the reason for the lethality of clc1Δ cells in the absence of osmotic stabilization.","doi":"10.1371/journal.pone.0071510","authors":"de León N, Sharifmoghadam MR, Hoya M, Curto MÁ, Doncel C, Valdivieso MH","authors_abbrev":"de León N et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-08-27","publication_year":"2013","canto_session_key":"f85ac1dcd8ab8c25","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-26 10:48:03","canto_approved_date":"2026-03-29 08:23:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-28 16:39:24","canto_added_date":"2013-09-20 13:54:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC9B6.08","SPCC1840.02c","SPAC821.09","SPAC26A3.05","SPAC19B12.03","SPBC19G7.05c"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2016-10-26"},{"uniquename":"PMID:37787465","title":"Glucose to lactate shift reprograms CDK-dependent mitotic decisions and its communication with MAPK Sty1 in Schizosaccharomyces pombe.","citation":"Biol Open 2023 Oct 15;12(10)","abstract":"Cell cycle regulation in response to biochemical cues is a fundamental event associated with many diseases. The regulation of such responses in complex metabolic environments is poorly understood. This study reveals unknown aspects of the metabolic regulation of cell division in Schizosaccharomyces pombe. We show that changing the carbon source from glucose to lactic acid alters the functions of the cyclin-dependent kinase (CDK) Cdc2 and mitogen-activated protein kinase (MAPK) Sty1, leading to unanticipated outcomes in the behavior and fate of such cells. Functional communication of Cdc2 with Sty1 is known to be an integral part of the cellular response to aberrant Cdc2 activity in S. pombe. Our results show that cross-talk between Cdc2 and Sty1, and the consequent Sty1-dependent regulation of Cdc2 activity, appears to be compromised and the relationship between Cdc2 activity and mitotic timing is also reversed in the presence of lactate. We also show that the biochemical status of cells under these conditions is an important determinant of the altered molecular functions mentioned above as well as the altered behavior of these cells.","doi":"10.1242/bio.060145","authors":"Sarkar P, Misra S, Ghosal A, Mukherjee S, Ghosh A, Sundaram G","authors_abbrev":"Sarkar P et al.","pubmed_publication_date":"15 Oct 2023","pubmed_entrez_date":"2023-10-03","publication_year":"2023","canto_session_key":"9d56e0cfc18f0d09","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Geetanjali Sundaram","canto_first_approved_date":"2024-05-09 07:13:49","canto_approved_date":"2024-05-24 16:33:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-04-25 17:25:19","canto_added_date":"2023-10-03 23:25:04","annotation_curators":[{"name":"Geetanjali Sundaram","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":22,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPAC24H6.05","SPBC11B10.09","SPBC409.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-05-09"},{"uniquename":"PMID:11907277","title":"The localization of the integral membrane protein Cps1p to the cell division site is dependent on the actomyosin ring and the septation-inducing network in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2002 Mar;13(3):989-1000","abstract":"Schizosaccharomyces pombe cells divide by medial fission through the use of an actomyosin-based contractile ring. Constriction of the actomyosin ring is accompanied by the centripetal addition of new membranes and cell wall material. In this article, we characterize the mechanism responsible for the localization of Cps1p, a septum-synthesizing 1,3-beta-glucan synthase, to the division site during cytokinesis. We show that Cps1p is an integral membrane protein that localizes to the cell division site late in anaphase. Neither F-actin nor microtubules are essential for the initial assembly of Cps1p to the medial division site. F-actin, but not microtubules, is however important for the eventual incorporation of Cps1p into the actomyosin ring. Assembly of Cps1p into the cell division ring is also dependent on the septation-inducing network (SIN) proteins that regulate division septum formation after assembly of the actomyosin ring. Fluorescence-recovery after-photobleaching experiments reveal that Cps1p does not diffuse appreciably within the plasma membrane and is retained at the division site by a mechanism that does not depend on an intact F-actin cytoskeleton. We conclude that the actomyosin ring serves as a spatial cue for Cps1p localization, whereas the maintenance of Cps1p at the division site occurs by a novel F-actin- and microtubule-independent mechanism. Furthermore, we propose that the SIN proteins ensure localization of Cps1p at the appropriate point in the cell cycle.","authors":"Liu J, Tang X, Wang H, Oliferenko S, Balasubramanian MK","authors_abbrev":"Liu J et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-22","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29694900","title":"Importin α and vNEBD Control Meiotic Spindle Disassembly in Fission Yeast.","citation":"Cell Rep 2018 Apr 24;23(4):933-941","abstract":"In metazoans, the nuclear envelope (NE) breakdown (NEBD) occurs during \"open\" mitosis and meiosis. In the fission yeast Schizosaccharomyces pombe, the mitosis and the first meiotic division (MI) are \"closed,\" during which the NE is maintained. Intriguingly, during the second meiotic division (MII), the NE is also maintained, but nuclear and cytoplasmic molecules are mixed similarly to open mitosis, a phenomenon of unknown biological significance called \"virtual\" NEBD (vNEBD). Here, we show that importin-α-dependent nucleocytoplasmic transport regulates spindle disassembly late in anaphase B at MI, as previously reported for mitosis. At MII, however, spindle dissolution is triggered by vNEBD early in anaphase B, a mechanism that short-circuits the nucleocytoplasmic transport system. We demonstrate that the sequential action of these two spindle disassembly systems regulates the spatiotemporal order and ploidy of the meiotic products.","doi":"10.1016/j.celrep.2018.03.073","authors":"Flor-Parra I, Iglesias-Romero AB, Salas-Pino S, Lucena R, Jimenez J, Daga RR","authors_abbrev":"Flor-Parra I et al.","pubmed_publication_date":"24 Apr 2018","pubmed_entrez_date":"2018-04-26","publication_year":"2018","canto_session_key":"e66906b54c5398a2","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-04-27 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1604.08c","SPBC29A10.02"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:20452294","title":"Ubiquitin-PCNA fusion as a mimic for mono-ubiquitinated PCNA in Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2010 Jul 01;9(7):777-84","abstract":"Translesion synthesis is a major mechanism with which eukaryotic cells deal with DNA damage during replication. Mono-ubiquitinated PCNA is a key regulator of this process. We have investigated whether a ubiquitin-PCNA fusion can mimic ubiquitinated PCNA, by transforming plasmids expressing this fusion protein into different mutants of Schizosaccharomyces pombe. We show that the fusion protein is able to form PCNA trimers and that it can reduce the UV sensitivity and increase translesion synthesis in mutants in which PCNA cannot be ubiquitinated (pcn1-K164R and rhp18), but not of the rad8 mutant in which PCNA can be mono-ubiquitinated but not poly-ubiquitinated. We conclude that the fusion protein is a mimic of mono-ubiquitinated PCNA but it cannot be poly-ubiquitinated. Expression of the fusion protein at levels similar to that of endogenous unmodified protein has little effect on the spontaneous mutation rate of S. pombe. Replacement of the pcn1 locus with PCNA N-terminally tagged with different epitopes resulted in lethality, probably because the tagged proteins were expressed at substantially reduced levels.","doi":"10.1016/j.dnarep.2010.03.015","authors":"Ramasubramanyan S, Coulon S, Fuchs RP, Lehmann AR, Green CM","authors_abbrev":"Ramasubramanyan S et al.","pubmed_publication_date":"01 Jul 2010","pubmed_entrez_date":"2010-05-11","publication_year":"2010","canto_session_key":"7145919e461c7ff3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-05 15:11:34","canto_approved_date":"2025-09-03 14:05:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-05 15:11:24","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPBC19C7.09c","SPBC1703.04","SPAC13G6.01c","SPBC1734.06","SPBC337.08c","SPBC4F6.15c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2016-04-05"},{"uniquename":"PMID:16117676","title":"RNA interference and epigenetic control of heterochromatin assembly in fission yeast.","citation":"Cold Spring Harb Symp Quant Biol 2004;69:419-27","abstract":"","authors":"Cam H, Grewal SI","authors_abbrev":"Cam H et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2005-08-25","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18923422","title":"Rad51 suppresses gross chromosomal rearrangement at centromere in Schizosaccharomyces pombe.","citation":"EMBO J 2008 Nov 19;27(22):3036-46","abstract":"Centromere that plays a pivotal role in chromosome segregation is composed of repetitive elements in many eukaryotes. Although chromosomal regions containing repeats are the hotspots of rearrangements, little is known about the stability of centromere repeats. Here, by using a minichromosome that has a complete set of centromere sequences, we have developed a fission yeast system to detect gross chromosomal rearrangements (GCRs) that occur spontaneously. Southern and comprehensive genome hybridization analyses of rearranged chromosomes show two types of GCRs: translocation between homologous chromosomes and formation of isochromosomes in which a chromosome arm is replaced by a copy of the other. Remarkably, all the examined isochromosomes contain the breakpoint in centromere repeats, showing that isochromosomes are produced by centromere rearrangement. Mutations in the Rad3 checkpoint kinase increase both types of GCRs. In contrast, the deletion of Rad51 recombinase preferentially elevates isochromosome formation. Chromatin immunoprecipitation analysis shows that Rad51 localizes at centromere around S phase. These data suggest that Rad51 suppresses rearrangements of centromere repeats that result in isochromosome formation.","doi":"10.1038/emboj.2008.215","authors":"Nakamura K, Okamoto A, Katou Y, Yadani C, Shitanda T, Kaweeteerawat C, Takahashi TS, Itoh T, Shirahige K, Masukata H, Nakagawa T","authors_abbrev":"Nakamura K et al.","pubmed_publication_date":"19 Nov 2008","pubmed_entrez_date":"2008-10-17","publication_year":"2008","canto_session_key":"a46da3af971de4e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-01-08 16:56:30","canto_approved_date":"2020-09-28 15:49:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-12-12 16:36:35","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPBC216.05","SPBC428.08c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-01-08"},{"uniquename":"PMID:33591272","title":"Mitochondrial copper and phosphate transporter specificity was defined early in the evolution of eukaryotes.","citation":"Elife 2021 Feb 16;10","abstract":"The mitochondrial carrier family protein SLC25A3 transports both copper and phosphate in mammals, yet in  Saccharomyces cerevisiae  the transport of these substrates is partitioned across two paralogs: PIC2 and MIR1. To understand the ancestral state of copper and phosphate transport in mitochondria, we explored the evolutionary relationships of PIC2 and MIR1 orthologs across the eukaryotic tree of life. Phylogenetic analyses revealed that PIC2-like and MIR1-like orthologs are present in all major eukaryotic supergroups, indicating an ancient gene duplication created these paralogs. To link this phylogenetic signal to protein function, we used structural modeling and site-directed mutagenesis to identify residues involved in copper and phosphate transport. Based on these analyses, we generated an L175A variant of mouse SLC25A3 that retains the ability to transport copper but not phosphate. This work highlights the utility of using an evolutionary framework to uncover amino acids involved in substrate recognition by mitochondrial carrier family proteins.","doi":"10.7554/eLife.64690","authors":"Zhu X, Boulet A, Buckley KM, Phillips CB, Gammon MG, Oldfather LE, Moore SA, Leary SC, Cobine PA","authors_abbrev":"Zhu X et al.","pubmed_publication_date":"16 Feb 2021","pubmed_entrez_date":"2021-02-16","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1703.13c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37120429","title":"Nucleotide exchange is sufficient for Hsp90 functions in vivo.","citation":"Nat Commun 2023 Apr 29;14(1):2489","abstract":"Hsp90 is an essential eukaryotic chaperone that regulates the activity of many client proteins. Current models of Hsp90 function, which include many conformational rearrangements, specify a requirement of ATP hydrolysis. Here we confirm earlier findings that the Hsp82-E33A mutant, which binds ATP but does not hydrolyze it, supports viability of S. cerevisiae, although it displays conditional phenotypes. We find binding of ATP to Hsp82-E33A induces the conformational dynamics needed for Hsp90 function. Hsp90 orthologs with the analogous EA mutation from several eukaryotic species, including humans and disease organisms, support viability of both S. cerevisiae and Sz. pombe. We identify second-site suppressors of EA that rescue its conditional defects and allow EA versions of all Hsp90 orthologs tested to support nearly normal growth of both organisms, without restoring ATP hydrolysis. Thus, the requirement of ATP for Hsp90 to maintain viability of evolutionarily distant eukaryotic organisms does not appear to depend on energy from ATP hydrolysis. Our findings support earlier suggestions that exchange of ATP for ADP is critical for Hsp90 function. ATP hydrolysis is not necessary for this exchange but provides an important control point in the cycle responsive to regulation by co-chaperones.","doi":"10.1038/s41467-023-38230-0","authors":"Reidy M, Garzillo K, Masison DC","authors_abbrev":"Reidy M et al.","pubmed_publication_date":"29 Apr 2023","pubmed_entrez_date":"2023-04-29","publication_year":"2023","canto_session_key":"d2ab88a6fe77fa6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-05-11 10:38:15","canto_approved_date":"2023-05-11 10:38:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-05-11 10:37:47","canto_added_date":"2023-05-01 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-05-11"},{"uniquename":"PMID:31588841","title":"Impact of cadmium and nickel on ion homeostasis in the yeast  Schizosaccharomyces pombe .","citation":"J Environ Sci Health B 2020;55(2):166-173","abstract":"Toxicity of heavy metals to living organisms is a worldwide research topic. Although, much has been discovered about cadmium and nickel impact on biological systems, a lot still remains unclear. We used inductively coupled plasma - optical emission spectroscopy to address the question of the effect of two different heavy metals nickel, and cadmium on intracellular ion balance. Increase or decrease of the content of several essential cations including Ca 2+ , Na + , K + , Mg 2+ , Cu 2+ , Fe 3+  in the yeast  Schizosaccharomyces pombe  was determined. Our results revealed that the cell exposure to high nickel and cadmium concentrations led to significant elevation of Ca 2+ , Na + , Mg 2+ , Cu 2+ , Fe 3+  levels in the yeast cell, while the content of K +  decreased. Correlation analyses showing in the presence of nickel and cadmium strong positive correlation among each tested element (Ca 2+ , Na + , Cu 2+ , Mg 2+  and Fe 3+ ) except for K + , demonstrate the significant impact of heavy metal treatment to ion homeostasis of the cell. Our data indicate that acute nickel and cadmium contamination leads to substantial ionome misbalance in yeast.","doi":"10.1080/03601234.2019.1673613","authors":"Pozgajova M, Navratilova A, Arvay J, Duranova H, Trakovicka A","authors_abbrev":"Pozgajova M et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2019-10-08","publication_year":"2020","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-10-09 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18577206","title":"Evidence of recent interkingdom horizontal gene transfer between bacteria and Candida parapsilosis.","citation":"BMC Evol Biol 2008 Jun 24;8:181","abstract":"To date very few incidences of interdomain gene transfer into fungi have been identified. Here, we used the emerging genome sequences of Candida albicans WO-1, Candida tropicalis, Candida parapsilosis, Clavispora lusitaniae, Pichia guilliermondii, and Lodderomyces elongisporus to identify recent interdomain HGT events. We refer to these as CTG species because they translate the CTG codon as serine rather than leucine, and share a recent common ancestor.\nPhylogenetic and syntenic information infer that two C. parapsilosis genes originate from bacterial sources. One encodes a putative proline racemase (PR). Phylogenetic analysis also infers that there were independent transfers of bacterial PR enzymes into members of the Pezizomycotina, and protists. The second HGT gene in C. parapsilosis belongs to the phenazine F (PhzF) superfamily. Most CTG species also contain a fungal PhzF homolog. Our phylogeny suggests that the CTG homolog originated from an ancient HGT event, from a member of the proteobacteria. An analysis of synteny suggests that C. parapsilosis has lost the endogenous fungal form of PhzF, and subsequently reacquired it from a proteobacterial source. There is evidence that Schizosaccharomyces pombe and Basidiomycotina also obtained a PhzF homolog through HGT.\nOur search revealed two instances of well-supported HGT from bacteria into the CTG clade, both specific to C. parapsilosis. Therefore, while recent interkingdom gene transfer has taken place in the CTG lineage, its occurrence is rare. However, our analysis will not detect ancient gene transfers, and we may have underestimated the global extent of HGT into CTG species.","doi":"10.1186/1471-2148-8-181","authors":"Fitzpatrick DA, Logue ME, Butler G","authors_abbrev":"Fitzpatrick DA et al.","pubmed_publication_date":"24 Jun 2008","pubmed_entrez_date":"2008-06-26","publication_year":"2008","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37078207","title":"Ceramide synthase homolog Tlc4 maintains nuclear envelope integrity via its Golgi translocation.","citation":"J Cell Sci 2023 May 15;136(10)","abstract":"Maintaining the integrity of the nuclear envelope (NE) is essential for preventing genomic DNA damage. Recent studies have shown that enzymes that catalyze lipid synthesis are involved in NE maintenance, but the underlying mechanism remains unclear. Here, we found that the ceramide synthase (CerS) homolog in the fission yeast Schizosaccharomyces pombe Tlc4 (SPAC17A2.02c) suppressed NE defects in cells lacking the NE proteins Lem2 and Bqt4. Tlc4 possesses a TRAM/LAG1/CLN8 domain that is conserved in CerS proteins and functions through its non-catalytic activity. Tlc4 was localized at the NE and endoplasmic reticulum, similar to CerS proteins, and also showed unique additional localization at the cis- and medial-Golgi cisternae. Growth and mutation analyses revealed that Golgi localization of Tlc4 was tightly linked to its activity of suppressing the defects in the double-deletion mutant of Lem2 and Bqt4. Our results suggest that Lem2 and Bqt4 control the translocation of Tlc4 from the NE to the Golgi, which is necessary for maintaining NE integrity.","doi":"10.1242/jcs.260923","authors":"Hirano Y, Ohno Y, Kubota Y, Fukagawa T, Kihara A, Haraguchi T, Hiraoka Y","authors_abbrev":"Hirano Y et al.","pubmed_publication_date":"15 May 2023","pubmed_entrez_date":"2023-04-20","publication_year":"2023","canto_session_key":"67fe379d8498baea","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-04-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.10","SPAC17A2.02c","SPAC18G6.10"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:41790804","title":"Genetic and environmental determinants of multicellular-like phenotypes in fission yeast.","citation":"Genetics 2026 Mar 06;","abstract":"Multicellular fungi have repeatedly given rise to primarily unicellular yeast species. Some of these, including the fission yeast Schizosaccharomyces pombe, can revert to multicellular-like phenotypes (MLPs). As MLP formation remains understudied in fission yeast compared to budding yeast, we aimed to narrow this gap. We developed high-throughput assays for two MLPs: flocculation and surface adhesion, which correlated in minimal media, suggesting a common mechanism. Using a library of 57 natural S. pombe isolates, we found that MLP formation varied widely across different nutrient and drug conditions. In a segregant S. pombe library generated by crossing an adhesive natural isolate with the standard laboratory strain, MLP formation correlated with expression levels of the transcription factor gene mbx2 and several flocculin genes. Quantitative trait locus (QTL) mapping of MLP formation located a frameshift mutation in the srb11 gene encoding cyclin C, a part of the Cdk8 kinase module (CKM) of the Mediator complex. Deletion of either srb11 or srb10 (encoding the Cdk8 kinase) resulted in MLP formation through upregulation of mbx2. Screening a library of 3721 gene-deletion strains uncovered 31 additional genes involved in surface adhesion, including 15 genes not previously associated with MLPs in fission or budding yeast. Notably, deletion of srb11, unlike deletions of the 31 hits, did not compromise cell growth, which might explain its natural occurrence as a QTL for MLP formation. Our findings provide a comprehensive genetic survey of MLP formation in fission yeast and a functional description of a causal variant that drives MLP formation in nature.","doi":"10.1093/genetics/iyag064","authors":"Kӧvér B, Cohen CE, Seres L, Raut S, Ralser M, Heineike BM, Bähler J","authors_abbrev":"Kӧvér B et al.","pubmed_publication_date":"06 Mar 2026","pubmed_entrez_date":"2026-03-06","publication_year":"2026","canto_session_key":"2f9d7ad652aa4f16","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-07 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25704380","title":"Characterization of the non-sexual flocculation of fission yeast cells that results from the deletion of ribosomal protein L32.","citation":"Yeast 2015 May;32(5):439-49","abstract":"We recently reported that deleting either of the two paralogous rpl32 genes resulted in non-sexual flocculation in fission yeast. This study represents the first report that these non-sexually flocculating fission yeast cells exhibit a thicker cell wall, an increased wall protein content with smeared glycosylated wall proteins, and increased cell wall polysaccharide content and adhesin-binding sugar residues (i.e. glucose, mannose and galactose). These changes reflect the wall features of flocculating cells that mediate recognition and connections between cells. Furthermore, this study demonstrates that this non-sexual flocculation is an adhesin-mediated process: (a) the transcription levels of several members of the Mam3/Map4 family of adhesins (i.e. PFL3, PFL7 and PFL6) and a Flo11-like adhesin protein are upregulated in rpl32-1Δ and rpl32-2Δ cells; (b) this non-sexual flocculation of rpl32-1Δ and rpl32-2Δ cells was eliminated by heating or enzyme digestion; (c) this non-sexual flocculation of rpl32-1Δ and rpl32-2Δ cells was enhanced by Ca(2+) and some other divalent metal ions, which stabilize the active conformation of adhesins; and (d) this non-sexual flocculation of rpl32-1Δ and rpl32-2Δ cells was competitively inhibited by glucose, galactose or mannose rather than only by galactose, as reported previously. Although different adhesin genes are selectively expressed under particular physiological or environmental conditions, the functions of these adhesins are the same and are interchangeable.","doi":"10.1002/yea.3070","authors":"Liu Z, Li R, Dong Q, Bian L, Li X, Yuan S","authors_abbrev":"Liu Z et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-02-24","publication_year":"2015","canto_session_key":"59b837f171477832","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-02-25 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15359428","title":"Robustness of metabolic map reconstruction.","citation":"J Bioinform Comput Biol 2004 Sep;2(3):589-93","abstract":"With the ever increasing amount of genomic data available, the interest for generating biochemical pathways has grown tremendously. So far, mainly complete genomes have been used to reconstruct the biochemical pathways and their associated interactions. However, a large number of low coverage genomes, as well as other sources of partial genomic data, are currently available for many organisms. In order to be able to use incomplete data for metabolic reconstruction, the inherent properties of this procedure need to be investigated. In this short note, we describe the robustness and predictive power of metabolic reconstructions using partial information from Schizosaccharomyces pombe. We also discuss the implications of the results on reference genome projects as well as other large-scale sequencing data.","authors":"Ahren DG, Ouzounis CA","authors_abbrev":"Ahren DG et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-09-11","publication_year":"2004","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19740752","title":"Mal3 masks catastrophe events in Schizosaccharomyces pombe microtubules by inhibiting shrinkage and promoting rescue.","citation":"J Biol Chem 2009 Oct 23;284(43):29246-50","abstract":"Schizosaccharomyces pombe Mal3 is a member of the EB family of proteins, which are proposed to be core elements in a tip-tracking network that regulates microtubule dynamics in cells. How Mal3 itself influences microtubule dynamics is unclear. We tested the effects of full-length recombinant Mal3 on dynamic microtubules assembled in vitro from purified S. pombe tubulin, using dark field video microscopy to avoid fluorescent tagging and data-averaging techniques to improve spatiotemporal resolution. We find that catastrophe occurs stochastically as a fast (<2.2 s) transition from constant speed growth to constant speed shrinkage with a constant probability that is independent of the Mal3 concentration. This implies that Mal3 neither stabilizes nor destabilizes microtubule tips. Mal3 does, however, stabilize the main part of the microtubule lattice, inhibiting shrinkage and increasing the frequency of rescues, consistent with recent models in which Mal3 on the lattice forms stabilizing lateral links between neighboring protofilaments. At high concentrations, Mal3 can entirely block shrinkage and induce very rapid rescue, making catastrophes impossible to detect, which may account for the apparent suppression of catastrophe by Mal3 and other EBs in vivo. Overall, we find that Mal3 stabilizes microtubules not by preventing catastrophe at the microtubule tip but by inhibiting lattice depolymerization and enhancing rescue. We argue that this implies that Mal3 binds microtubules in different modes at the tip and on the lattice.","doi":"10.1074/jbc.C109.052159","authors":"Katsuki M, Drummond DR, Osei M, Cross RA","authors_abbrev":"Katsuki M et al.","pubmed_publication_date":"23 Oct 2009","pubmed_entrez_date":"2009-09-11","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19252122","title":"Iron activates in vivo DNA binding of Schizosaccharomyces pombe transcription factor Fep1 through its amino-terminal region.","citation":"Eukaryot Cell 2009 Apr;8(4):649-64","abstract":"In Schizosaccharomyces pombe, the iron sensor Fep1 mediates the transcriptional repression of iron transport genes in response to high concentrations of iron. On the other hand, fep1(+) expression is downregulated under conditions of iron starvation by the CCAAT-binding factor Php4. In this study, we created a fep1Delta php4Delta double mutant strain where expression of fep1(+) was disengaged from its iron limitation-dependent repression by Php4 to examine the effects of iron on constitutively expressed functional fep1(+)-GFP and TAP-fep1(+) alleles and their gene products. In these cells, Fep1-green fluorescent protein was invariably localized in the nucleus under both iron-limiting and iron-replete conditions. Using chromatin immunoprecipitation assays, we found that Fep1 is associated with iron-responsive promoters in vivo. Chromatin binding was iron dependent, with a loss of binding observed in the presence of low iron. Functional dissection of the protein revealed that the N-terminal 241-residue segment that includes two consensus Cys(2)/Cys(2)-type zinc finger motifs and a Cys-rich region is required for optimal promoter occupancy by Fep1. Within this segment, a minimal module encompassing amino acids 60 to 241 is sufficient for iron-dependent chromatin binding. Using yeast one-hybrid analysis, we showed that the replacement of the repression domain of Fep1 by fusing the activation domain of VP16 to the chromatin-binding fragment of amino acids 1 to 241 of Fep1 converts the protein from an iron-dependent repressor into an iron-dependent transcriptional activator. Thus, the repression function of Fep1 can be replaced with that of a transcriptional activation function without the loss of its iron-dependent DNA-binding activity.","doi":"10.1128/EC.00001-09","authors":"Jbel M, Mercier A, Pelletier B, Beaudoin J, Labbé S","authors_abbrev":"Jbel M et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-03-03","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12651004","title":"Identification and characterisation of Schizosaccharomyces pombe cyclophilin 3, a cyclosporin A insensitive orthologue of human USA-CyP.","citation":"J Chromatogr B Analyt Technol Biomed Life Sci 2003 Mar 25;786(1-2):81-91","abstract":"We have identified nine cyclophilins encoded in the genome of the fission yeast Schizosaccharomyces pombe (Sp). Cyclophilin 3 is an orthologue of hUSA-CyP, which is associated with Prp4/Prp3 in the [U4/U6.U5] snRNP complex and Prp18, both of which are components of the pre-mRNA splicing machinery. PPIase assays have shown SpCyp3 and hUSA-CyP to have comparable activity and substrate specificity, but SpCyp3 has a reduced sensitivity to CsA correlating with a difference in the catalytic site. Prp3, Prp4 and Prp18 proteins exist in S. pombe and nuclear localisation of SpCyp3 has been shown, indicating conservation of function between hUSA-CyP and SpCyp3.","authors":"Pemberton TJ, Rulten SL, Kay JE","authors_abbrev":"Pemberton TJ et al.","pubmed_publication_date":"25 Mar 2003","pubmed_entrez_date":"2003-03-26","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1709.04c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:30381185","title":"Chemical composition of bilberry wine fermented with non-Saccharomyces yeasts (Torulaspora delbrueckii and Schizosaccharomyces pombe) and Saccharomyces cerevisiae in pure, sequential and mixed fermentations.","citation":"Food Chem 2018 Nov 15;266:262-274","abstract":"This study evaluated the effects of fermentation with pure cultures of Torulaspora delbrueckii (TD291 and TD70526) and Schizosaccharomyces pombe (SP3796 and SP70572), as well as in sequential and mixed inoculations with Saccharomyces cerevisiae, on the chemical composition of bilberry wine. In comparison to the bilberry wines produced by pure and sequential fermentations, mixed cultures produced bilberry wines with more ethanol, higher pH values, higher percentages of red and yellow shade, but less glycerol and acetaldehyde. Higher values of color intensity and bluish parameter were found in products of pure fermentations with non-Saccharomyces yeasts. Compared to S. cerevisiae, T. delbrueckii contributed to the reduction of ethanol and acetic acid while increasing the content of succinic acid, lactic acid and higher alcohols; S. pombe consumed malic acid almost completely and produced more glycerol, acetaldehyde and/or pyruvic acid. Fermentation with SP70572 had the highest amounts of anthocyanins and hydroxycinnamic acids derivatives.","doi":"10.1016/j.foodchem.2018.06.003","authors":"Liu S, Laaksonen O, Kortesniemi M, Kalpio M, Yang B","authors_abbrev":"Liu S et al.","pubmed_publication_date":"15 Nov 2018","pubmed_entrez_date":"2018-11-02","publication_year":"2018","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2018-11-03 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23589458","title":"Insight into actin organization and function in cytokinesis from analysis of fission yeast mutants.","citation":"Genetics 2013 Jun;194(2):435-46","abstract":"Actin is a key cytoskeletal protein with multiple roles in cellular processes such as polarized growth, cytokinesis, endocytosis, and cell migration. Actin is present in all eukaryotes as highly dynamic filamentous structures, such as linear cables and branched filaments. Detailed investigation of the molecular role of actin in various processes has been hampered due to the multifunctionality of the protein and the lack of alleles defective in specific processes. The actin cytoskeleton of the fission yeast, Schizosaccharomyces pombe, has been extensively characterized and contains structures analogous to those in other cell types. In this study, primarily with the view to uncover actin function in cytokinesis, we generated a large bank of fission yeast actin mutants that affect the organization of distinct actin structures and/or discrete physiological functions of actin. Our screen identified 17 mutants with specific defects in cytokinesis. Some of these cytokinesis mutants helped in dissecting the function of specific actin structures during ring assembly. Further genetic analysis of some of these actin mutants revealed multiple genetic interactions with mutants previously known to affect the actomyosin ring assembly. We also characterize a mutant allele of actin that is suppressed upon overexpression of Cdc8p-tropomyosin, underscoring the utility of this mutant bank. Another 22 mutant alleles, defective in polarized growth and/or other functions of actin obtained from this screen, are also described in this article. This mutant bank should be a valuable resource to study the physiological and biochemical functions of actin.","doi":"10.1534/genetics.113.149716","authors":"Subramanian D, Huang J, Sevugan M, Robinson RC, Balasubramanian MK, Tang X","authors_abbrev":"Subramanian D et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-04-17","publication_year":"2013","canto_session_key":"15c83a99a76b5872","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC27F1.02c","SPAC4A8.15c","SPAP8A3.08","SPAC1F5.04c","SPCC645.05c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:18354085","title":"Diminishing HDACs by drugs or mutations promotes normal or abnormal sister chromatid separation by affecting APC/C and adherin.","citation":"J Cell Sci 2008 Apr 01;121(Pt 7):1107-18","abstract":"Histone acetyltransferases (HATs) and histone deacetylases (HDACs) play important roles in cell regulation, including cell cycle progression, although their precise role in mitotic progression remains elusive. To address this issue, the effects of HDAC inhibition were examined upon a variety of mitotic mutants of the fission yeast Schizosaccharomyces pombe, which contains three HDACs that are sensitive to trichostatin A (TSA) and are similar to human HDACs. Here it is shown that HDACs are implicated in sister chromatid cohesion and separation. A mutant of the cohesin loader Mis4 (adherin) was hypersensitive to TSA and synthetically lethal with HDAC deletion mutations. TSA treatment of mis4 mutant cells decreased chromatin-bound cohesins in the chromosome arm region. By contrast, HDAC inhibitors and clr6 HDAC mutations rescued temperature sensitive (ts) phenotypes of the mutants of the ubiquitin ligase complex anaphase-promoting complex/cyclosome (APC/C), which display metaphase arrest. This suppression coincided with facilitated complex formation of APC/C. Moreover, our mass spectrometry analysis showed that an APC/C subunit, Cut23/APC8, is acetylated. HATs and HDACs might directly target adherin and APC/C to ensure proper chromosome segregation, and anti-tumour effects of HDAC inhibitors could be attributed to this deregulation.","doi":"10.1242/jcs.024224","authors":"Kimata Y, Matsuyama A, Nagao K, Furuya K, Obuse C, Yoshida M, Yanagida M","authors_abbrev":"Kimata Y et al.","pubmed_publication_date":"01 Apr 2008","pubmed_entrez_date":"2008-03-21","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC106.09","SPBC20F10.06","SPAC6F12.14","SPAC17C9.01c","SPBC36.05c","SPBC800.03","SPAC6F12.15c","SPBC1A4.01","SPAC3G9.07c","SPBC106.10","SPBP23A10.04","SPAC31A2.05c"],"gene_count":12,"ltp_gene_count":12},{"uniquename":"PMID:20094054","title":"Understanding cytokinesis: lessons from fission yeast.","citation":"Nat Rev Mol Cell Biol 2010 Feb;11(2):149-55","abstract":"For decades after the discovery that a contractile ring made of actin filaments and myosin II produces the force to constrict the cleavage furrow of animal cells, the complexity of cytokinesis has slowed progress in understanding the mechanism. Mechanistic insights, however, have been obtained by genetic, biochemical, microscopic and mathematical modelling approaches in the fission yeast Schizosaccharomyces pombe. Many features that have been identified in fission yeast are probably shared with animal cells, as both inherited many cytokinesis genes from their common ancestor about one billion years ago.","doi":"10.1038/nrm2834","authors":"Pollard TD, Wu JQ","authors_abbrev":"Pollard TD et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2010-01-23","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12112238","title":"Two non-complementing genes encoding enzymatically active methylenetetrahydrofolate reductases control methionine requirement in fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2002 Jul;19(10):841-8","abstract":"By transforming two methionine auxotrophic mutants from fission yeast Schizosaccharomyces pombe with a wild-type gene library, we defined two genes, met9 and met11, which both encode a methylenetetrahydrofolate reductase. The genes cannot complement each other. We detected single transcripts for both. In vitro measurements of enzymatic activities showed that the met11-encoded enzyme was responsible for only 15-20% of the total methylenetetrahydrofolate reductase activity. A strain in which gene met9 was disrupted required significantly more methionine for full growth and efficient mating and sporulation than the strain disrupted for gene met11. The in vitro and in vivo data thus indicated that met9 was the major expressed gene. Our results are in accordance with the assumption that the two methylenetetrahydrofolate reductases generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine, and suggest that expression of the two genes is an important parameter in the control of methionine biosynthesis.","authors":"Naula N, Walther C, Baumann D, Schweingruber ME","authors_abbrev":"Naula N et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-07-12","publication_year":"2002","canto_session_key":"ce75498c19ea15fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-26 08:35:37","canto_approved_date":"2025-01-22 20:09:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 10:08:56","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC343.10","SPAC56F8.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-09-26"},{"uniquename":"PMID:29769606","title":"Malonylation of histone H2A at lysine 119 inhibits Bub1-dependent H2A phosphorylation and chromosomal localization of shugoshin proteins.","citation":"Sci Rep 2018 May 16;8(1):7671","abstract":"Post-translational modifications of histones, such as acetylation and phosphorylation, are highly conserved in eukaryotes and their combination enables precise regulation of many cellular functions. Recent studies using mass spectrometry have revealed various non-acetyl acylations in histones, including malonylation and succinylation, which change the positive charge of lysine into a negative one. However, the molecular function of histone malonylation or succinylation is poorly understood. Here, we discovered the functions of malonylation in histone H2A at lysine 119 (H2A-K119) in chromosome segregation during mitosis and meiosis. Analyses of H2A-K119 mutants in Saccharomyces cerevisiae and Schizosaccharomyces pombe showed that anionic mutations, specifically to aspartate (K119D) and glutamate (K119E), showed mis-segregation of the chromosomes and sensitivity to microtubule-destabilizing reagents in mitosis and meiosis. We found that the chromosomal localization of shugoshin proteins, which depends on Bub1-catalyzed phosphorylation of H2A at serine 121 (H2A-S121), was significantly reduced in the H2A-K119D and the H2A-K119E mutants. Biochemical analyses using K119-unmodified or -malonylated H2A-C-tail peptides showed that H2A-K119 malonylation inhibited the interaction between Bub1 and H2A, leading to a decrease in Bub1-dependent H2A-S121 phosphorylation. Our results indicate a novel crosstalk between lysine malonylation and serine/threonine phosphorylation, which may be important for fine-tuning chromatin functions such as chromosome segregation.","doi":"10.1038/s41598-018-26114-z","authors":"Ishiguro T, Tanabe K, Kobayashi Y, Mizumoto S, Kanai M, Kawashima SA","authors_abbrev":"Ishiguro T et al.","pubmed_publication_date":"16 May 2018","pubmed_entrez_date":"2018-05-18","publication_year":"2018","canto_session_key":"f83f9b9d22696ff4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-04-24 16:30:57","canto_approved_date":"2024-10-09 11:07:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-24 16:01:06","canto_added_date":"2018-05-19 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.06c","SPBP35G2.03c","SPCC622.08c","SPAC15A10.15","SPCC1322.12c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2024-04-24"},{"uniquename":"PMID:26537787","title":"Targeting of SUMO substrates to a Cdc48-Ufd1-Npl4 segregase and STUbL pathway in fission yeast.","citation":"Nat Commun 2015 Nov 05;6:8827","abstract":"In eukaryotes, the conjugation of proteins to the small ubiquitin-like modifier (SUMO) regulates numerous cellular functions. A proportion of SUMO conjugates are targeted for degradation by SUMO-targeted ubiquitin ligases (STUbLs) and it has been proposed that the ubiquitin-selective chaperone Cdc48/p97-Ufd1-Npl4 facilitates this process. However, the extent to which the two pathways overlap, and how substrates are selected, remains unknown. Here we address these questions in fission yeast through proteome-wide analyses of SUMO modification sites. We identify over a thousand sumoylated lysines in a total of 468 proteins and quantify changes occurring in the SUMO modification status when the STUbL or Ufd1 pathways are compromised by mutations. The data suggest the coordinated processing of several classes of SUMO conjugates, many dynamically associated with centromeres or telomeres. They provide new insights into subnuclear organization and chromosome biology, and, altogether, constitute an extensive resource for the molecular characterization of SUMO function and dynamics.","doi":"10.1038/ncomms9827","authors":"Køhler JB, Tammsalu T, Jørgensen MM, Steen N, Hay RT, Thon G","authors_abbrev":"Køhler JB et al.","pubmed_publication_date":"05 Nov 2015","pubmed_entrez_date":"2015-11-06","publication_year":"2015","canto_session_key":"95d820b9de46239c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-11-06 15:46:09","canto_approved_date":"2026-01-31 14:05:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-06 15:45:59","canto_added_date":"2015-11-07 01:19:15","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1113,"orcid":"0000-0003-4148-4606","file_type":"protein_modification","file_name":"PMID_26537787_modifications.tsv"}],"genes":["SPAC16A10.07c","SPAC20G8.09c","SPAC27F1.04c","SPBC19C2.09","SPAC630.14c","SPBC30D10.17c","SPCC1235.05c","SPAC7D4.14c","SPAC25B8.14","SPBC776.13","SPCC338.17c","SPBC1347.11","SPAC8C9.04","SPACUNK4.17","SPBC2G2.04c","SPCC188.07","SPAC17H9.16","SPAC19G12.06c","SPAC6F6.16c","SPBC2F12.04","SPBC1773.02c","SPBC2A9.07c","SPAC23H3.14","SPAC3A12.05c","SPBC27.02c","SPBC13E7.08c","SPAC6B12.02c","SPAC22G7.05","SPBC1289.07c","SPBC32F12.04","SPBC4B4.03","SPCC338.08","SPAC26H5.06","SPAC22G7.10","SPAC57A7.06","SPAC9E9.10c","SPBC11G11.03","SPBC12D12.01","SPBC14F5.04c","SPBC1A4.07c","SPBC336.07","SPBC25D12.05","SPAC644.04","SPAC644.05c","SPBC1711.06","SPAC7D4.07c","SPBC16H5.03c","SPBC800.06","SPBC28F2.11","SPAC959.03c","SPBP8B7.19","SPBC25H2.05","SPBC428.08c","SPBC16E9.10c","SPCC1020.06c","SPCC1682.03c","SPAC23C11.15","SPBP22H7.02c","SPCC613.05c","SPAC22H12.04c","SPAC3H1.12c","SPAC29A4.04c","SPAC589.10c","SPAC11H11.01","SPBP23A10.07","SPBC1778.02","SPAC22E12.17c","SPBC1709.18","SPAC589.08c","SPCP25A2.03","SPAC1783.04c","SPBC3B8.09","SPBC651.01c","SPAPB8E5.02c","SPBC24C6.04","SPAC17A2.01","SPAPB1A10.02","SPAC3G6.04","SPBC18H10.12c","SPAC1B3.03c","SPAC2E1P3.01","SPAC6G10.06","SPCC645.04","SPAC890.04c","SPBC19G7.09","SPBC25H2.11c","SPAC17A2.08c","SPCC16A11.11","SPAC22E12.03c","SPCPB16A4.05c","SPAC27F1.02c","SPAC9E9.11","SPBC1709.08","SPBC19C2.07","SPCC285.17","SPBC17G9.03c","SPBC146.09c","SPBC19C7.10","SPCC1281.06c","SPBC30B4.03c","SPBC409.10","SPCC1322.12c","SPAC15E1.04","SPBC1289.10c","SPBC16D10.06","SPCC736.08","SPAC25B8.10","SPBC947.08c","SPAC25G10.07c","SPAC22A12.15c","SPBC2G2.14","SPAC3C7.14c","SPBC16A3.19","SPAC8C9.08","SPAC1B9.03c","SPBC3D6.12","SPAC821.03c","SPCC1753.05","SPAC2G11.15c","SPAC2E1P3.04","SPAC25B8.12c","SPAC22H10.11c","SPAC1142.07c","SPBC3E7.02c","SPAC3H5.07","SPAC644.12","SPAC6F6.07c","SPCC306.07c","SPBC26H8.09c","SPAC328.10c","SPBC16C6.08c","SPAC212.11","SPAC29E6.08","SPAC11G7.04","SPAC22F3.13","SPAP8A3.04c","SPAC4H3.10c","SPAC1071.08","SPBP35G2.10","SPAC823.14","SPCC1450.02","SPBC1A4.03c","SPAC1565.08","SPCC777.09c","SPAC32A11.03c","SPAC926.04c","SPCC24B10.19c","SPBC557.03c","SPAC3A12.10","SPAC3F10.17","SPBC28F2.12","SPAC19G12.13c","SPCC1739.13","SPBC839.13c","SPAC9.09","SPAC823.12","SPCC330.13","SPAC1783.05","SPCC285.13c","SPAC821.07c","SPAC15A10.15","SPAC31G5.03","SPBP4H10.13","SPBC19G7.13","SPAC26F1.07","SPAC9E9.09c","SPBCPT2R1.08c","SPAC23E2.01","SPCC18.12c","SPAPYUG7.03c","SPAC6G10.11c","SPCC1450.03","SPBC16A3.02c","SPACUNK4.14","SPBC23E6.07c","SPBC20F10.01","SPAC821.10c","SPAC4D7.10c","SPAC24C9.04","SPAC1F8.07c","SPAC23G3.09","SPAC25G10.03","SPAC631.02","SPAC26H5.10c","SPBC15D4.14","SPAC29B12.04","SPBC1347.02","SPBC27.04","SPBC8D2.04","SPAC222.06","SPAC17G6.16c","SPCC1450.04","SPBC13E7.01","SPAC23H4.18c","SPCC188.03","SPBC1685.08","SPAC22H12.02","SPAC694.06c","SPBC1289.03c","SPAC2E1P5.05","SPAC1783.07c","SPAC16A10.06c","SPBP8B7.09c","SPAC15F9.02","SPCC364.03","SPCC1672.02c","SPAC18B11.10","SPAC6B12.18","SPBC28F2.10c","SPAC26A3.04","SPAC105.03c","SPAC30D11.13","SPCC962.02c","SPCC965.07c","SPBC646.10c","SPAC23C11.02c","SPBC3B9.01","SPAC11E3.01c","SPCC16C4.13c","SPAPB1E7.07","SPCC1672.07","SPBC1734.02c","SPBC839.05c","SPAC3H5.12c","SPAC9E9.13","SPBP8B7.06","SPAC10F6.08c","SPAC31G5.05c","SPBC4F6.12","SPBC16D10.11c","SPCC338.12","SPBC11G11.05","SPAC31A2.11c","SPBC146.03c","SPCC18.07","SPBC3B9.06c","SPBC1703.02","SPAC15E1.06","SPBC337.08c","SPBP23A10.13","SPCC285.03","SPAPJ760.02c","SPCC622.08c","SPAC5H10.10","SPAC1565.07c","SPBC1289.16c","SPBC1198.04c","SPAC458.02c","SPAC8C9.03","SPBC23E6.09","SPBC31F10.14c","SPAC23C11.03","SPAC1071.06","SPAC343.11c","SPBC365.06","SPAC16E8.08","SPBC1A4.02c","SPCP31B10.07","SPBC8D2.06","SPAC18G6.10","SPAC1093.04c","SPAC24C9.03","SPAC3A11.02","SPBC6B1.04","SPCC594.01","SPBC15C4.03","SPAC4C5.04","SPAC5D6.02c","SPBC27B12.11c","SPBC887.04c","SPBP23A10.08","SPCC1620.09c","SPCC18B5.07c","SPAC1486.04c","SPAC13G6.02c","SPAC19G12.10c","SPBC31F10.04c","SPAC17G6.10","SPAC12G12.05c","SPBC1685.10","SPCC23B6.04c","SPCC1259.01c","SPBC365.15","SPAC14C4.02c","SPBC23E6.02","SPBC3B8.06","SPBC336.10c","SPAC22A12.04c","SPBC776.09","SPCC794.09c","SPAC6F12.17","SPAC6G10.12c","SPBC1711.05","SPAC1610.01","SPBC1539.10","SPCC1919.14c","SPBC215.12","SPBC646.14c","SPAC5D6.01","SPBC21.01","SPAC24C9.12c","SPAC2G11.12","SPBC646.09c","SPCC576.03c","SPAC1687.05","SPAC144.11","SPCC63.13","SPCC830.03","SPBC11C11.09c","SPAC18B11.06","SPAC19A8.01c","SPBC2D10.17","SPBC428.10","SPCC16C4.14c","SPCC5E4.07","SPAC25G10.08","SPBC2G5.05","SPCC5E4.06","SPAC17C9.05c","SPBC8D2.18c","SPAC23G3.10c","SPBP8B7.10c","SPBC36.05c","SPBC29B5.01","SPAC1F7.05","SPCC162.08c","SPCC31H12.08c","SPCC1919.09","SPAC227.02c","SPAC17G8.03c","SPBC17G9.08c","SPAC2F3.03c","SPBC83.08","SPBC1652.01","SPCC1620.12c","SPBC1198.11c","SPCC622.16c","SPBC18E5.11c","SPBC4C3.05c","SPAC2G11.07c","SPAC1142.08","SPBC19C2.03","SPCC13B11.01","SPBC31F10.13c","SPAC2G11.14","SPBC28F2.04c","SPAC20G8.08c","SPCC576.11","SPBC4F6.13c","SPCC622.09","SPBC12C2.06","SPCC24B10.21","SPAC23A1.11","SPCC31H12.04c","SPBC56F2.02","SPBC660.16","SPBC1861.04c","SPBC106.14c","SPBC11C11.03","SPBC119.15","SPAC29A4.02c","SPBC887.18c","SPCC306.04c","SPCC1494.10","SPAC57A10.10c","SPAC664.05","SPBC16A3.08c","SPAC26F1.06","SPAC1783.08c","SPAC23A1.10","SPAC23H4.11c","SPAC1071.01c","SPAC3H1.13","SPAC9G1.13c","SPCC1259.03","SPBC1198.13c","SPAC17G8.02","SPBC1709.15c","SPAC57A10.09c","SPBP8B7.03c","SPCC5E4.05c","SPAC890.08","SPBC1773.07c","SPAC664.01c","SPCC613.12c","SPBC21C3.08c","SPAC10F6.06","SPBC1105.11c","SPBC14C8.14c","SPCC63.14","SPBC19G7.16","SPAC30D11.08c","SPBC25D12.02c","SPCC126.02c","SPBC16A3.09c","SPCC1393.08","SPAC13G7.02c","SPBC146.01","SPAC22E12.19","SPBC3F6.04c","SPAC2E12.02","SPAC3G6.01","SPAC3C7.11c","SPBC14F5.08","SPBC4F6.04","SPBC2G2.05","SPBC26H8.01","SPCC4G3.18","SPBC1685.02c","SPBC3E7.08c","SPBC12C2.10c","SPAC1250.01","SPAC8C9.10c","SPBC1861.01c","SPAC23G3.06","SPBC3D6.11c","SPCC285.16c","SPBC32H8.12c","SPAC17H9.06c","SPBC13E7.10c","SPAC29B12.01","SPCC24B10.11c","SPAC10F6.09c","SPBC1734.15","SPAC17H9.04c","SPBC365.10","SPAC23H4.12","SPAC6G9.06c","SPAC57A7.12","SPBC839.15c","SPBC14F5.12c","SPCC126.04c","SPBC1685.04","SPAC23C4.02","SPBC646.15c","SPCC1393.04","SPCC306.03c","SPCC1223.02","SPBC119.02","SPAC17G6.14c","SPAC31G5.19","SPBC776.11","SPAC1805.12c","SPBC8D2.03c","SPCC74.05","SPBC409.09c","SPBC1861.02","SPBC17G9.02c","SPBC106.18","SPAC15A10.04c","SPAC140.02","SPAC20H4.01","SPBC1703.14c","SPAC9E9.15","SPCC24B10.08c","SPAC30D11.07","SPAC1486.05","SPCC1259.07","SPCC330.01c","SPBC3E7.12c","SPBC83.15","SPBC21C3.01c","SPBC1826.01c","SPBC1815.01","SPAC824.07","SPAC26H5.05","SPCC962.04","SPBC1709.05","SPBC215.05","SPAC4F10.09c","SPAC6F6.17","SPAC12B10.10","SPAC15A10.02","SPBP16F5.08c","SPAC1420.03","SPBC354.05c","SPBC32F12.11","SPBC354.12","SPCC24B10.09","SPBC6B1.10","SPCC1442.04c","SPAC30C2.08","SPBC29A3.04","SPCP1E11.07c","SPCP1E11.09c","SPAC16E8.06c","SPBC29A10.04","SPCC1020.02","SPCC5E4.03c","SPBP4H10.06c","SPAC17G6.13"],"gene_count":491,"ltp_gene_count":3,"approved_date":"2020-11-06"},{"uniquename":"PMID:26968627","title":"Prp8 retinitis pigmentosa mutants cause defects in the transition between the catalytic steps of splicing.","citation":"RNA 2016 May;22(5):793-809","abstract":"Pre-mRNA splicing must occur with high fidelity and efficiency for proper gene expression. The spliceosome uses DExD/H box helicases to promote on-pathway interactions while simultaneously minimizing errors. Prp8 and Snu114, an EF2-like GTPase, regulate the activity of the Brr2 helicase, promoting RNA unwinding by Brr2 at appropriate points in the splicing cycle and repressing it at others. Mutations linked to retinitis pigmentosa (RP), a disease that causes blindness in humans, map to the Brr2 regulatory region of Prp8. Previous in vitro studies of homologous mutations in Saccharomyces cerevisiaes how that Prp8-RP mutants cause defects in spliceosome activation. Here we show that a subset of RP mutations in Prp8 also causes defects in the transition between the first and second catalytic steps of splicing. Though Prp8-RP mutants do not cause defects in splicing fidelity, they result in an overall decrease in splicing efficiency. Furthermore, genetic analyses link Snu114 GTP/GDP occupancy to Prp8-dependent regulation of Brr2. Our results implicate the transition between the first and second catalytic steps as a critical place in the splicing cycle where Prp8-RP mutants influence splicing efficiency. The location of the Prp8-RP mutants, at the \"hinge\" that links the Prp8 Jab1-MPN regulatory \"tail\" to the globular portion of the domain, suggests that these Prp8-RP mutants inhibit regulated movement of the Prp8 Jab1/MPN domain into the Brr2 RNA binding channel to transiently inhibit Brr2. Therefore, in Prp8-linked RP, disease likely results not only from defects in spliceosome assembly and activation, but also because of defects in splicing catalysis.","doi":"10.1261/rna.055459.115","authors":"Mayerle M, Guthrie C","authors_abbrev":"Mayerle M et al.","pubmed_publication_date":"May 2016","pubmed_entrez_date":"2016-03-13","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19584544","title":"Identification of sam4 as a rad24 allele in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2009 Jul;73(7):1591-8","abstract":"Fission yeast requires nutritional starvation to switch the mitotic cell cycle to sexual differentiation, but sam mutants, of which we had isolated nine alleles, mate without the starvation condition. These mutants are useful for understanding the mechanism underlying the way cells sense nutritional starvation and change the cell cycle. To identify the sam allele, we first sought phenotypes other than the original sam phenotype. We found that all nine sam mutants were sensitive to 1 M KCl, that sam2, sam3, sam4 and sam9 were sensitive to 0.1 M CaCl(2), and that only the sam4 mutant was sensitive to 150 J/m(2) UV. This peculiar phenotype of sam4 suggested to us that sam4 might be an allele of rad24, which encodes a 14-3-3 protein. In fact, the Rad24 protein disappeared in sam4 and the rad24 mRNA was not transcribed in sam4. In addition, the mutation that changed Gln to a stop codon was found in the rad24 locus of sam4. Hence we concluded that sam4 is an allele of rad24. We also found that over-expression of rad24 or rad25 (a paralog of rad24) has a suppressive effect on sam1, and that sam1 was not an allele of rad24 nor rad25. Thus 14-3-3 proteins are deeply involved in the switching of the mitotic cell cycle to the sexual differentiation of fission yeast.","authors":"Oowatari Y, Toma K, Ozoe F, Kawamukai M","authors_abbrev":"Oowatari Y et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-07-09","publication_year":"2009","canto_session_key":"0606c7fce02ac897","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-08-05 14:50:19","canto_approved_date":"2026-01-01 21:25:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-01 17:45:24","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPBC106.10","SPAC17A2.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-08-05"},{"uniquename":"PMID:15862318","title":"cda1+, encoding chitin deacetylase is required for proper spore formation in Schizosaccharomyces pombe.","citation":"FEBS Lett 2005 May 09;579(12):2737-43","abstract":"In Schizosaccharomyces pombe, a major role of chitin is to build up a complete spore. Here, we analyzed the cda1(+) gene (SPAC19G12.03), which encodes a protein homologous to chitin deacetylases, to know whether it is required for spore formation in S. pombe. The homothallic Deltacda1 strain constructed by homologous recombination was found to form a little amount of abnormal spores that contained one, two, or three asci, similar to (but not as strong as) the phenotype observed in a deletion mutant of chs1 encoding chitin synthase 1. This phenotype is reversed by expression of S. cerevisiae chitin deacetylase CDA1 or CDA2, suggesting that cda1 encodes a chitin deacetylase. To support the role of Cda1 in sporulation, the timing of expression of cda1(+) mRNA increased during sporulation process. We also found that the Cda1 protein self-associated when its binding was tested both by two-hybrid system and immunoprecipitation. Thus, these data indicated that cda1(+) is required for proper spore formation in S. pombe.","authors":"Matsuo Y, Tanaka K, Matsuda H, Kawamukai M","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"09 May 2005","pubmed_entrez_date":"2005-05-03","publication_year":"2005","canto_session_key":"2e6a22df8110d36d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-29 16:00:53","canto_approved_date":"2024-06-13 04:56:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-18 10:33:21","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.03","SPAC13G6.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-29"},{"uniquename":"EMBL:AU011243","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28554046","title":"Non-invasive, electro-orientation-based viability assay using optically transparent electrodes for individual fission yeast cells.","citation":"Biosens Bioelectron 2017 Nov 15;97:53-58","abstract":"A non-invasive assay of cylindrical yeast cell viability based on electro-orientation (EO) in an alternating electric field was developed, in which cell viability can be determined by each cell's EO direction without the need for reagents. A cell suspension of a few microliters was sandwiched between a pair of optically transparent indium-tin-oxide (ITO) plate electrodes. Observation under a light microscope enabled easy identification of EO based on cell shape, e.g., cells were standing upright and appeared perfectly circular when oriented parallel to the electric field direction (standing position), and they were lying flat and had an elongated shape when oriented perpendicular to the field (lain-down position). The alternative EO positions of living or dead cells were dependent on the applied frequency: opposite EO positions were obtained by applying an AC voltage of 1.5V at 10MHz; at which point, only living cells rapidly attained a standing position, whereas dead cells were lain-down within 10s. All the cell's EO positions agreed well with a viability assay by florescence staining. Therefore, at the single-cell level and fluorescently label-free, it was possible to simply and accurately determine whether individual cells were alive or dead based on their shape.","doi":"10.1016/j.bios.2017.05.034","authors":"Suga M, Kunimoto A, Shinohara H","authors_abbrev":"Suga M et al.","pubmed_publication_date":"15 Nov 2017","pubmed_entrez_date":"2017-05-30","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-05-31 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41285957","title":"Phosphatase specificity influences phosphorylation timing of CDK substrates during the cell cycle.","citation":"Nat Commun 2025 Nov 24;","abstract":"Cell cycle events are ordered by cyclin-dependent kinases (CDKs), which phosphorylate hundreds of substrates. Multiple phosphatases oppose these CDK substrates, yet their collective role in regulating phosphorylation timing in vivo remains unclear. Here, we show that four phosphatases (PP2A-B55, PP2A-B56, CDC14, and PP1) each target distinct subsets of CDK substrate sites in vivo in fission yeast, influencing when phosphorylation occurs during G2 and mitosis. On average, sites dephosphorylated by CDC14 and PP2A-B56 are phosphorylated earlier during G2, followed by sites dephosphorylated by PP1 and PP2A-B55. This suggests that these phosphatases set different phosphorylation thresholds at the G2/M transition. Consistent with this, depleting PP2A-B55 or CDC14 accelerates mitotic onset, likely by advancing phosphorylation of their respective CDK substrates, suggesting these phosphorylation thresholds are important for regulating mitotic onset. Our findings establish in vivo phosphatase substrate specificity as a key factor regulating the timing of CDK substrate phosphorylation throughout the cell cycle.","doi":"10.1038/s41467-025-66547-5","authors":"Zeisner TU, Auchynnikava T, Roberts EL, Nurse P","authors_abbrev":"Zeisner TU et al.","pubmed_publication_date":"24 Nov 2025","pubmed_entrez_date":"2025-11-25","publication_year":"2025","canto_session_key":"83617c395b1b8e7f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-11-26 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1196141","title":"Synchronization of the fission yeast Schizosaccharomyces pombe using heat shocks.","citation":"Methods Cell Biol 1975;12:373-80","abstract":"","authors":"Kramhoft B, Zeuthen E","authors_abbrev":"Kramhoft B et al.","pubmed_publication_date":"1975","pubmed_entrez_date":"1975-01-01","publication_year":"1975","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18256290","title":"Schizosaccharomyces pombe Pxl1 is a paxillin homologue that modulates Rho1 activity and participates in cytokinesis.","citation":"Mol Biol Cell 2008 Apr;19(4):1727-38","abstract":"Schizosaccharomyces pombe Rho GTPases regulate actin cytoskeleton organization and cell integrity. We studied the fission yeast gene SPBC4F6.12 based on its ability to suppress the thermosensitivity of cdc42-1625 mutant strain. This gene, named pxl1(+), encodes a protein with three LIM domains that is similar to paxillin. Pxl1 does not interact with Cdc42 but it interacts with Rho1, and it negatively regulates this GTPase. Fission yeast Pxl1 forms a contractile ring in the cell division region and deletion of pxl1(+) causes a delay in cell-cell separation, suggesting that it has a function in cytokinesis. Pxl1 N-terminal region is required and sufficient for its localization to the medial ring, whereas the LIM domains are necessary for its function. Pxl1 localization requires actin polymerization and the actomyosin ring, but it is independent of the septation initiation network (SIN) function. Moreover, Pxl1 colocalizes and interacts with Myo2, and Cdc15, suggesting that it is part of the actomyosin ring. Here, we show that in cells lacking Pxl1, the myosin ring is not correctly assembled and that actomyosin ring contraction is delayed. Together, these data suggest that Pxl1 modulates Rho1 GTPase signaling and plays a role in the formation and contraction of the actomyosin ring during cytokinesis.","authors":"Pinar M, Coll PM, Rincón SA, Pérez P","authors_abbrev":"Pinar M et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_session_key":"ad37ffc7d6aa5f2a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-02-28 15:37:27","canto_approved_date":"2026-01-31 16:02:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-06 14:02:51","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":80,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.06c","SPAC110.03","SPAC4A8.05c","SPAC14C4.09","SPCC1840.02c","SPCC4B3.15","SPAC1F7.04","SPCC645.05c","SPAC20G8.05c","SPAC1F5.04c","SPAC821.09","SPAC24H6.09","SPAPYUG7.03c","SPAC6F6.08c","SPCC1739.11c","SPBC17F3.01c","SPAC4F10.11","SPAP8A3.08","SPBC19G7.05c","SPCC970.09","SPBC16A3.01","SPBC4F6.12","SPAC4F8.13c","SPAC926.03","SPAC16E8.09","SPAC1851.04c"],"gene_count":26,"ltp_gene_count":21,"approved_date":"2018-02-28"},{"uniquename":"PMID:38007544","title":"Gene duplication and deletion caused by over-replication at a fork barrier.","citation":"Nat Commun 2023 Nov 25;14(1):7730","abstract":"Replication fork stalling can provoke fork reversal to form a four-way DNA junction. This remodelling of the replication fork can facilitate repair, aid bypass of DNA lesions, and enable replication restart, but may also pose a risk of over-replication during fork convergence. We show that replication fork stalling at a site-specific barrier in fission yeast can induce gene duplication-deletion rearrangements that are independent of replication restart-associated template switching and Rad51-dependent multi-invasion. Instead, they resemble targeted gene replacements (TGRs), requiring the DNA annealing activity of Rad52, the 3'-flap nuclease Rad16-Swi10, and mismatch repair protein Msh2. We propose that excess DNA, generated during the merging of a canonical fork with a reversed fork, can be liberated by a nuclease and integrated at an ectopic site via a TGR-like mechanism. This highlights how over-replication at replication termination sites can threaten genome stability in eukaryotes.","doi":"10.1038/s41467-023-43494-7","authors":"Oehler J, Morrow CA, Whitby MC","authors_abbrev":"Oehler J et al.","pubmed_publication_date":"25 Nov 2023","pubmed_entrez_date":"2023-11-25","publication_year":"2023","canto_session_key":"0a2e7f13952dc6b7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-11-27 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7248858","title":"Production of protoplasts in different yeasts by mutanase.","citation":"Can J Microbiol 1981 May;27(5):550-3","abstract":"Mutanase (Mutanase Novo) affects the high frequency production of protoplasts in the following strains of yeast: Saccharomyces cerevisiae, Schizosaccharomyces pombe, Kluyveromyces lactis, Trichosporon pullulans, and Schwanniomyces alluvius. Regeneration frequencies varied with the strain used and ranged between 10 and 18%. This enzyme preparation appears to be a very useful means of obtaining protoplasts from a wide variety of yeasts currently being used for experimental purposes.","authors":"Stephen ER, Nasim A","authors_abbrev":"Stephen ER et al.","pubmed_publication_date":"May 1981","pubmed_entrez_date":"1981-05-01","publication_year":"1981","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12032093","title":"The meiotic recombination checkpoint is regulated by checkpoint rad+ genes in fission yeast.","citation":"EMBO J 2002 Jun 03;21(11):2807-18","abstract":"During the course of meiotic prophase, intrinsic double-strand breaks (DSBs) must be repaired before the cell can engage in meiotic nuclear division. Here we investigate the mechanism that controls the meiotic progression in Schizosaccharomyces pombe that have accumulated excess meiotic DSBs. A meiotic recombination-defective mutant, meu13Delta, shows a delay in meiotic progression. This delay is dependent on rec12+, namely on DSB formation. Pulsed-field gel electrophoresis analysis revealed that meiotic DSB repair in meu13Delta was retarded. We also found that the delay in entering nuclear division was dependent on the checkpoint rad+, cds1+ and mek1+ (the meiotic paralog of Cds1/Chk2). This implies that these genes are involved in a checkpoint that provides time to repair DSBs. Consistently, the induction of an excess of extrinsic DSBs by ionizing radiation delayed meiotic progression in a rad17(+)-dependent manner. dmc1Delta also shows meiotic delay, however, this delay is independent of rec12+ and checkpoint rad+. We propose that checkpoint monitoring of the status of meiotic DSB repair exists in fission yeast and that defects other than DSB accumulation can cause delays in meiotic progression.","authors":"Shimada M, Nabeshima K, Tougan T, Nojima H","authors_abbrev":"Shimada M et al.","pubmed_publication_date":"03 Jun 2002","pubmed_entrez_date":"2002-05-29","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.03","SPAC14C4.13","SPAC222.15","SPAC8E11.03c","SPBC216.05","SPCC18B5.11c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:6296690","title":"Evolutionary divergence of the mRNA transcription initiation mechanism in yeast.","citation":"Nature 1983 Jan 13;301(5896):167-9","abstract":"The promoters of eukaryotic genes are being increasingly defined through the identification of consensus DNA sequences, by mutational analysis, and by in vitro and in vivo studies of transcription. Whereas the TATA sequence (Goldberg-Hogness box) has been largely conserved among protein encoding genes (transcribed by RNA polymerase II) of eukaryotes, there is some evidence that other structural and functional determinants of mRNA transcription are not conserved between species. I report there an in vivo comparative analysis of the transcription initiation systems of the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharmyces pombe (which can both be transformed by identical plasmids). I have found no instance in which a gene is transcribed in the same fashion in both yeasts. Instead, I have found that the in vivo transcription starting points for many different yeast genes are determined by the cell in which it is transcribed rather than its gene structure alone. The evidence also suggests that the divergence of the transcription initiation system may partly involve the mechanism or structure which determines the distance from the TATA consensus sequence to the site of transcription initiation.","authors":"Russell PR","authors_abbrev":"Russell PR","pubmed_publication_date":"13 Jan 1983","pubmed_entrez_date":"1983-01-13","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26942680","title":"Licensing of Centromeric Chromatin Assembly through the Mis18α-Mis18β Heterotetramer.","citation":"Mol Cell 2016 Mar 03;61(5):774-787","abstract":"Centromeres are specialized chromatin domains specified by the centromere-specific CENP-A nucleosome. The stable inheritance of vertebrate centromeres is an epigenetic process requiring deposition of new CENP-A nucleosomes by HJURP. We show HJURP is recruited to centromeres through a direct interaction between the HJURP centromere targeting domain and the Mis18α-β C-terminal coiled-coil domains. We demonstrate Mis18α and Mis18β form a heterotetramer through their C-terminal coiled-coil domains. Mis18α-β heterotetramer formation is required for Mis18BP1 binding and centromere recognition. S. pombe contains a single Mis18 isoform that forms a homotetramer, showing tetrameric Mis18 is conserved from fission yeast to humans. HJURP binding disrupts the Mis18α-β heterotetramer and removes Mis18α from centromeres. We propose stable binding of Mis18 to centromeres in telophase licenses them for CENP-A deposition. Binding of HJURP deposits CENP-A at centromeres and facilitates the removal of Mis18, restricting CENP-A deposition to a single event per cell cycle.","doi":"10.1016/j.molcel.2016.02.014","authors":"Nardi IK, Zasadzińska E, Stellfox ME, Knippler CM, Foltz DR","authors_abbrev":"Nardi IK et al.","pubmed_publication_date":"03 Mar 2016","pubmed_entrez_date":"2016-03-05","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC970.12"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:20028739","title":"Splicing factor Spf30 assists exosome-mediated gene silencing in fission yeast.","citation":"Mol Cell Biol 2010 Mar;30(5):1145-57","abstract":"Heterochromatin assembly in fission yeast relies on the processing of cognate noncoding RNAs by both the RNA interference and the exosome degradation pathways. Recent evidence indicates that splicing factors facilitate the cotranscriptional processing of centromeric transcripts into small interfering RNAs (siRNAs). In contrast, how the exosome contributes to heterochromatin assembly and whether it also relies upon splicing factors were unknown. We provide here evidence that fission yeast Spf30 is a splicing factor involved in the exosome pathway of heterochromatin silencing. Spf30 and Dis3, the main exosome RNase, colocalize at centromeric heterochromatin and euchromatic genes. At the centromeres, Dis3 helps recruiting Spf30, whose deficiency phenocopies the dis3-54 mutant: heterochromatin is impaired, as evidenced by reduced silencing and the accumulation of polyadenylated centromeric transcripts, but the production of siRNAs appears to be unaffected. Consistent with a direct role, Spf30 binds centromeric transcripts and locates at the centromeres in an RNA-dependent manner. We propose that Spf30, bound to nascent centromeric transcripts, perhaps with other splicing factors, assists their processing by the exosome. Splicing factor intercession may thus be a common feature of gene silencing pathways.","doi":"10.1128/MCB.01317-09","authors":"Bernard P, Drogat J, Dheur S, Genier S, Javerzat JP","authors_abbrev":"Bernard P et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2009-12-24","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1281.02c","SPBC6B1.07","SPAC664.01c","SPBC20F10.06","SPBC26H8.10"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"EMBL:SPC01712","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9108274","title":"A wat1 mutant of fission yeast is defective in cell morphology.","citation":"Mol Gen Genet 1997 Mar 26;254(2):127-38","abstract":"The organization of the actin cytoskeleton plays an integral role in cell morphogenesis of all eukaryotes. We have isolated a temperature-sensitive mutant in Schizosaccharomyces pombe, wat1-1, in which acting patches are delocalized, resulting in an elliptically shaped cell phenotype. Molecular cloning and DNA sequencing of wat1+ showed that the gene encodes a 314 residue protein containing WD-40 repeats. Cells lacking wat1+ are slow growing but viable at 25 degrees C and temperature-sensitive for growth above 33 degrees C. At restrictive temperature, wat1-d strains are phenotypically indistinguishable from wat1-1. When combined with a deletion for the wat1+ gene, cdc mutants failed to elongate at restrictive temperature and exhibited alterations in actin patch localization. This analysis suggests that wat1+ is required directly or indirectly for polarized cell growth in S. pombe. Wat1p and a functional, epitope-tagged, version of Wat1p can be overproduced without inducing alterations in cell morphology.","authors":"Kemp JT, Balasubramanian MK, Gould KL","authors_abbrev":"Kemp JT et al.","pubmed_publication_date":"26 Mar 1997","pubmed_entrez_date":"1997-03-26","publication_year":"1997","canto_session_key":"201b62bab67ac941","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-11-07 11:20:08","canto_approved_date":"2023-04-12 17:22:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-03 12:53:14","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21B10.05c","SPAC4A8.15c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-11-07"},{"uniquename":"PMID:15632061","title":"Global effects on gene expression in fission yeast by silencing and RNA interference machineries.","citation":"Mol Cell Biol 2005 Jan;25(2):590-601","abstract":"Histone modifications influence gene expression in complex ways. The RNA interference (RNAi) machinery can repress transcription by recruiting histone-modifying enzymes to chromatin, although it is not clear whether this is a general mechanism for gene silencing or whether it requires repeated sequences such as long terminal repeats (LTRs). We analyzed the global effects of the Clr3 and Clr6 histone deacetylases, the Clr4 methyltransferase, the zinc finger protein Clr1, and the RNAi proteins Dicer, RdRP, and Argonaute on the transcriptome of Schizosaccharomyces pombe (fission yeast). The clr mutants derepressed similar subsets of genes, many of which also became transcriptionally activated in cells that were exposed to environmental stresses such as nitrogen starvation. Many genes that were repressed by the Clr proteins clustered in extended regions close to the telomeres. Surprisingly few genes were repressed by both the silencing and RNAi machineries, with transcripts from centromeric repeats and Tf2 retrotransposons being notable exceptions. We found no correlation between repression by RNAi and proximity to LTRs, and the wtf family of repeated sequences seems to be repressed by histone deacetylation independent of RNAi. Our data indicate that the RNAi and Clr proteins show only a limited functional overlap and that the Clr proteins play more global roles in gene silencing.","authors":"Hansen KR, Burns G, Mata J, Volpe TA, Martienssen RA, Bähler J, Thon G","authors_abbrev":"Hansen KR et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2005-01-06","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC800.03","SPCC736.11","SPCC188.13c","SPBC36.05c","SPAC6F12.09","SPBC428.08c","SPBC2D10.17"],"gene_count":7,"ltp_gene_count":2},{"uniquename":"PMID:10953879","title":"Meiotic double-strand breaks in Schizosaccharomyces pombe.","citation":"Curr Genet 2000 Jul;38(1):33-8","abstract":"Meiotic DNA double-strand breaks (DSBs) are associated with recombination hot spots in the yeast Saccharomyces cerevisiae and are believed to initiate the process of recombination. Until now, meiosis-induced breaks have not been shown to occur regularly in other organisms. Here we show, by pulsed-field gel electrophoresis of DNA, that meiotic DSBs occur transiently in all three chromosomes of the fission yeast Schizosaccharomyces pombe. In a repair defective mutant, carrying a mutation in the RecA homolog gene rhp51, meiotic DSBs accumulate. In contrast to expectation from the genetic map of S. pombe, however, many chromosomal DNA molecules remain unbroken during meiosis.","authors":"Zenvirth D, Simchen G","authors_abbrev":"Zenvirth D et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-08-23","publication_year":"2000","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1524835","title":"Isolation and characterization of mutants supersensitive to the spindle poison, isopropyl N-3-chlorophenyl carbamate (CIPC) in the fission yeast Schizosaccharomyces pombe.","citation":"Jpn J Genet 1992 Apr;67(2):97-109","abstract":"Mutants supersensitive to the spindle poison, Isopropyl N-3-chlorophenyl carbamate (CIPC) of the fission yeast Schizosaccharomyces pombe were isolated and characterized genetically. Fourteen different recessive loci were assigned for the mutation (donated as cps1 to cps14) and two, cps1 and cps3, were mapped precisely on the chromosomes. Nine mutant strains were also supersensitive to phenothiazine derivatives, inhibitors of calcium-binding protein calmodulin. Four of nine strains were incapable of growing in the presence of 10 microM calcium ionophore A23187, at which the drug had no effect on cell growth in other strains. Fluorescence microscopy using the DAPI and Calcofluor staining methods showed two strains out of four to be defective in normal cell division; most stationary-phase cells of the cps6 mutant were seen to be bi- or tetra-nucleate, being partitioned with one or three septa, respectively. In the other mutant (cps8), enlarged cells were unequally partitioned with multisepta, and each compartment contained several daughter nuclei. The septa appeared aberrant in position within the cell, and situated diagonally but not vertically along the long cell axis.","authors":"Ishiguro J, Uhara Y","authors_abbrev":"Ishiguro J et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"588296c78358a92c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-08-14 15:08:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-03-11 11:52:35","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A11.02","SPBC19G7.05c","SPBC32H8.12c","SPBP19A11.04c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-03-11"},{"uniquename":"PMID:8165288","title":"[Signal transduction systems in fission yeast].","citation":"Tanpakushitsu Kakusan Koso 1994 Mar;39(4):429-38","abstract":"","authors":"Isshiki T, Tanaka K, Yamamoto M","authors_abbrev":"Isshiki T et al.","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011723","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013737","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20086243","title":"Nitrogen depletion in the fission yeast Schizosaccharomyces pombe causes nucleosome loss in both promoters and coding regions of activated genes.","citation":"Genome Res 2010 Mar;20(3):361-71","abstract":"Gene transcription is associated with local changes in chromatin, both in nucleosome positions and in chemical modifications of the histones. Chromatin dynamics has mostly been studied on a single-gene basis. Those genome-wide studies that have been made primarily investigated steady-state transcription. However, three studies of genome-wide changes in chromatin during the transcriptional response to heat shock in the budding yeast Saccharomyces cerevisiae revealed nucleosome eviction in promoter regions but only minor effects in coding regions. Here, we describe the short-term response to nitrogen starvation in the fission yeast Schizosaccharomyces pombe. Nitrogen depletion leads to a fast induction of a large number of genes in S. pombe and is thus suitable for genome-wide studies of chromatin dynamics during gene regulation. After 20 min of nitrogen removal, 118 transcripts were up-regulated. The distribution of regulated genes throughout the genome was not random; many up-regulated genes were found in clusters, while large parts of the genome were devoid of up-regulated genes. Surprisingly, this up-regulation was associated with nucleosome eviction of equal magnitudes in the promoters and in the coding regions. The nucleosome loss was not limited to induction by nitrogen depletion but also occurred during cadmium treatment. Furthermore, the lower nucleosome density persisted for at least 60 min after induction. Two highly induced genes, urg1(+) and urg2(+), displayed a substantial nucleosome loss, with only 20% of the nucleosomes being left in the coding region. We conclude that nucleosome loss during transcriptional activation is not necessarily limited to promoter regions.","doi":"10.1101/gr.098558.109","authors":"Kristell C, Orzechowski Westholm J, Olsson I, Ronne H, Komorowski J, Bjerling P","authors_abbrev":"Kristell C et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2010-01-21","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28481910","title":"PCNA ubiquitylation ensures timely completion of unperturbed DNA replication in fission yeast.","citation":"PLoS Genet 2017 May;13(5):e1006789","abstract":"PCNA ubiquitylation on lysine 164 is required for DNA damage tolerance. In many organisms PCNA is also ubiquitylated in unchallenged S phase but the significance of this has not been established. Using Schizosaccharomyces pombe, we demonstrate that lysine 164 ubiquitylation of PCNA contributes to efficient DNA replication in the absence of DNA damage. Loss of PCNA ubiquitylation manifests most strongly at late replicating regions and increases the frequency of replication gaps. We show that PCNA ubiquitylation increases the proportion of chromatin associated PCNA and the co-immunoprecipitation of Polymerase δ with PCNA during unperturbed replication and propose that ubiquitylation acts to prolong the chromatin association of these replication proteins to allow the efficient completion of Okazaki fragment synthesis by mediating gap filling.","doi":"10.1371/journal.pgen.1006789","authors":"Daigaku Y, Etheridge TJ, Nakazawa Y, Nakayama M, Watson AT, Miyabe I, Ogi T, Osborne MA, Carr AM","authors_abbrev":"Daigaku Y et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2017-05-09","publication_year":"2017","canto_session_key":"76a3cc41b9c66144","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tony Carr","canto_approved_date":"2017-06-01 16:57:42","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-05-15 09:20:52","canto_added_date":"2017-05-11 00:15:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tony Carr","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPAC30D11.10","SPCC16A11.17","SPAC11E3.04c","SPBC1734.06","SPAC1687.05","SPBC25H2.13c","SPBC336.04","SPAC20G8.01"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-05-15"},{"uniquename":"PMID:11017199","title":"Structural basis for the diversity of DNA recognition by bZIP transcription factors.","citation":"Nat Struct Biol 2000 Oct;7(10):889-93","abstract":"The basic region leucine zipper (bZIP) proteins form one of the largest families of transcription factors in eukaryotic cells. Despite relatively high homology between the amino acid sequences of the bZIP motifs, these proteins recognize diverse DNA sequences. Here we report the 2.0 A resolution crystal structure of the bZIP motif of one such transcription factor, PAP1, a fission yeast AP-1-like transcription factor that binds DNA containing the novel consensus sequence TTACGTAA. The structure reveals how the Pap1-specific residues of the bZIP basic region recognize the target sequence and shows that the side chain of the invariant Asn in the bZIP motif adopts an alternative conformation in Pap1. This conformation, which is stabilized by a Pap1-specific residue and its associated water molecule, recognizes a different base in the target sequence from that in other bZIP subfamilies.","authors":"Fujii Y, Shimizu T, Toda T, Yanagida M, Hakoshima T","authors_abbrev":"Fujii Y et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-10-04","publication_year":"2000","canto_session_key":"a0c8d1e63698e9f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-02-14 16:43:20","canto_approved_date":"2025-09-04 09:37:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-14 16:43:13","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-02-14","pdb_entries":[{"pdb_id":"1gd2","gene_chains":[{"gene_uniquename":"SPAC1783.07c","chain":"E/F/G/H/I/J","position":"71-140"}],"title":"CRYSTAL STRUCTURE OF BZIP TRANSCRIPTION FACTOR PAP1 BOUND TO DNA","entry_authors":"Fujii Y,Shimizu T,Toda T,Yanagida M,Hakoshima T","entry_authors_abbrev":"Fujii Y et al.","reference_uniquename":"PMID:11017199","experimental_method":"X-ray","resolution":"2.0"}]},{"uniquename":"PMID:24938783","title":"Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes.","citation":"Proc Natl Acad Sci U S A 2014 Jul 01;111(26):9455-60","abstract":"The study of proteins and protein complexes using chemical cross-linking followed by the MS identification of the cross-linked peptides has found increasingly widespread use in recent years. Thus far, such analyses have used almost exclusively homobifunctional, amine-reactive cross-linking reagents. Here we report the development and application of an orthogonal cross-linking chemistry specific for carboxyl groups. Chemical cross-linking of acidic residues is achieved using homobifunctional dihydrazides as cross-linking reagents and a coupling chemistry at neutral pH that is compatible with the structural integrity of most protein complexes. In addition to cross-links formed through insertion of the dihydrazides with different spacer lengths, zero-length cross-link products are also obtained, thereby providing additional structural information. We demonstrate the application of the reaction and the MS identification of the resulting cross-linked peptides for the chaperonin TRiC/CCT and the 26S proteasome. The results indicate that the targeting of acidic residues for cross-linking provides distance restraints that are complementary and orthogonal to those obtained from lysine cross-linking, thereby expanding the yield of structural information that can be obtained from cross-linking studies and used in hybrid modeling approaches.","doi":"10.1073/pnas.1320298111","authors":"Leitner A, Joachimiak LA, Unverdorben P, Walzthoeni T, Frydman J, Förster F, Aebersold R","authors_abbrev":"Leitner A et al.","pubmed_publication_date":"01 Jul 2014","pubmed_entrez_date":"2014-06-19","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP19A11.03c","SPBC23G7.12c","SPCC1682.16","SPAC4A8.13c","SPCC1682.10","SPCC1795.04c","SPCC63.12c","SPBC16C6.07c","SPAC23G3.11","SPCC576.10c","SPAC6G10.04c","SPBC16G5.01","SPAC31A2.04c","SPAC3A11.12c","SPAC23D3.07","SPCC1442.06","SPBC577.10","SPBC17D11.07c","SPAC13C5.01c","SPAC323.02c","SPBC4.07c","SPBC582.07c","SPAC31G5.13","SPAC22F8.06","SPBC106.16","SPAC607.05"],"gene_count":26,"ltp_gene_count":26},{"uniquename":"PMID:2005906","title":"Identification of DNA regions required for mitotic and meiotic functions within the centromere of Schizosaccharomyces pombe chromosome I.","citation":"Mol Cell Biol 1991 Apr;11(4):2206-15","abstract":"We have determined the structural organization and functional roles of centromere-specific DNA sequence repeats in cen1, the centromere region from chromosome I of the fission yeast Schizosaccharomyces pombe. cen1 is composed of various classes of repeated sequences designated K', K\"(dgl), L, and B', arranged in a 34-kb inverted repeat surrounding a 4- to 5-kb nonhomologous central core. Artificial chromosomes containing various portions of the cen1 region were constructed and assayed for mitotic and meiotic centromere function in S. pombe. Deleting K' and L from the distal portion of one arm of the inverted repeat had no effect on mitotic centromere function but resulted in greatly increased precocious sister chromatid separation in the first meiotic division. A centromere completely lacking K' and L, but containing the central core, one copy of B' and K\" in one arm, and approximately 2.5 kb of the core-proximal portion of B' in the other arm, was also fully functional mitotically but again did not maintain sister chromatid attachment in meiosis I. However, deletion of K\" from this minichromosome resulted in complete loss of centromere function. Thus, one copy of at least a portion of the K\" (dgl) repeat is absolutely required but is not sufficient for S. pombe centromere function. The long centromeric inverted-repeat region must be relatively intact to maintain sister chromatid attachment in meiosis I.","authors":"Hahnenberger KM, Carbon J, Clarke L","authors_abbrev":"Hahnenberger KM et al.","pubmed_publication_date":"Apr 1991","pubmed_entrez_date":"1991-04-01","publication_year":"1991","canto_session_key":"e2ab9eac007adba1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 17:32:43","canto_approved_date":"2019-01-31 17:32:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 17:32:36","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:5340600","title":"Fractionation and composition of ribonucleic acids from Schizosaccharomyces pombe.","citation":"Can J Biochem 1967 Jun;45(6):973-8","abstract":"","authors":"Katona E","authors_abbrev":"Katona E","pubmed_publication_date":"Jun 1967","pubmed_entrez_date":"1967-06-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39727334","title":"Interaction mapping between nucleoporins in the fission yeast Schizosaccharomyces pombe using mass-spectrometry.","citation":"J Biochem 2024 Dec 27;","abstract":"Nuclear pore complexes (NPCs) act as gateways across the nuclear envelope for molecular transport between the nucleus and the cytoplasm in eukaryotes. NPCs consist of several subcomplexes formed by multiple copies of approximately 30 different proteins known as nucleoporins (Nups). In the fission yeast Schizosaccharomyces pombe, the NPC structure is unique, particularly in its outer ring subcomplexes, where the cytoplasmic and nucleoplasmic outer rings are composed of distinct sets of proteins. However, it remains unclear how this unique outer ring structure in S. pombe is supported by interactions between subcomplexes or individual Nups. In this study, we investigated protein-protein interactions between S. pombe Nups using mass spectrometry and identified Nups that interact with each subcomplex or a specific Nup. The cytoplasmic outer ring Nups bind to both the cytoplasmic filament Nups and the inner ring Nups, while the nucleoplasmic outer ring Nups bind to the nuclear basket Nups in addition to the inner ring Nups. Among the inner ring Nups, Nup155 interacts with most of the cytoplasmic and nucleoplasmic outer ring Nups, suggesting that Nup155 may serve as a hub supporting the uniquely asymmetric outer ring structure of the S. pombe NPC.","doi":"10.1093/jb/mvae095","authors":"Asakawa H, Nagao K, Fukagawa T, Obuse C, Hiraoka Y, Haraguchi T","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"27 Dec 2024","pubmed_entrez_date":"2024-12-27","publication_year":"2024","canto_session_key":"e2b13b68b301e118","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-12-28 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC890.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28357272","title":"A central role for TOR signalling in a yeast model for juvenile CLN3 disease.","citation":"Microb Cell 2015 Nov 11;2(12):466-480","abstract":"Yeasts provide an excellent genetically tractable eukaryotic system for investigating the function of genes in their biological context, and are especially relevant for those conserved genes that cause disease. We study the role of  btn1 , the orthologue of a human gene that underlies an early onset neurodegenerative disease (juvenile CLN3 disease, neuronal ceroid lipofuscinosis (NCLs) or Batten disease) in the fission yeast  Schizosaccharomyces pombe . A global screen for genetic interactions with  btn1  highlighted a conserved key signalling hub in which multiple components functionally relate to this conserved disease gene. This signalling hub includes two major mitogen-activated protein kinase (MAPK) cascades, and centers on the Tor kinase complexes TORC1 and TORC2. We confirmed that yeast cells modelling CLN3 disease exhibit features consistent with dysfunction in the TORC pathways, and showed that modulating TORC function leads to a comprehensive rescue of defects in this yeast disease model. The same pathways may be novel targets in the development of therapies for the NCLs and related diseases.","doi":"10.15698/mic2015.12.241","authors":"Bond ME, Brown R, Rallis C, Bähler J, Mole SE","authors_abbrev":"Bond ME et al.","pubmed_publication_date":"11 Nov 2015","pubmed_entrez_date":"2017-03-31","publication_year":"2015","canto_session_key":"d62104ba26ebd4b7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-04-02 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.14c","SPAP14E8.04","SPCC285.15c","SPAC9G1.07","SPAC9G1.10c","SPBC56F2.03","SPCC11E10.06c","SPCC622.12c","SPBC1271.15c","SPAC11G7.01","SPCC584.13","SPCC31H12.02c","SPAP27G11.14c","SPAC631.01c","SPAC13F5.01c","SPAC17H9.12c","SPBC21C3.20c","SPCC24B10.10c","SPAC31G5.17c","SPAC20H4.05c","SPCC24B10.14c","SPAC1A6.04c","SPCC16A11.07","SPCC63.06","SPCC825.04c","SPBC337.09","SPCC1223.06","SPCC584.15c","SPCC553.03","SPCC1672.06c","SPCC330.07c","SPCC18B5.03","SPAC17C9.14","SPCC1393.10","SPAC9G1.06c","SPCC1322.08","SPBC27B12.10c","SPCC1223.12c","SPCC550.15c","SPAC140.03","SPAC17G6.17","SPAP27G11.02","SPCC550.08","SPAC9G1.12","SPAC9G1.04","SPCC1020.07","SPCC613.02","SPCC126.15c","SPAP11E10.01","SPCC132.04c","SPCC1235.05c","SPBC32F12.11","SPCC645.13","SPAC17H9.03c","SPBC16D10.11c","SPCC1235.13","SPBC1198.08","SPAC19B12.11c","SPAP8A3.07c","SPCC622.17","SPCC1281.07c","SPCC895.09c","SPCC663.03","SPAC13D6.02c","SPAC20H4.10","SPAC23C11.14","SPBC651.09c","SPAC24H6.03","SPAC26H5.05","SPBC530.05","SPCC4B3.02c","SPAC57A10.12c","SPCC24B10.22","SPBC18H10.13","SPAC1B3.16c","SPAC22H10.04","SPCC4G3.04c","SPCC132.02","SPBC32H8.07","SPAC20H4.06c","SPCC1753.05","SPBC16G5.15c","SPCC1795.10c","SPCC24B10.02c","SPAC1071.08","SPAC13G6.09","SPBC543.03c","SPAC30.02c","SPCC622.16c","SPAPB1A10.12c","SPCC1393.13","SPAC20H4.04","SPCC736.09c","SPAC732.02c","SPAC1002.07c","SPAC20H4.03c","SPCC162.12","SPAC30C2.07","SPBC28E12.04","SPCC1020.10","SPCPB16A4.05c","SPCC18.17c","SPCC4B3.07","SPAC22A12.04c","SPBC409.07c","SPAC13D6.01","SPBC21B10.13c","SPCC1259.08","SPCC24B10.16c","SPAC32A11.02c","SPAC13G6.02c","SPAC30.03c","SPBC609.05","SPAC3C7.06c","SPAC1006.03c","SPAC343.16","SPCC188.08c","SPCC16A11.16c","SPAPB1A10.14","SPCC320.14","SPCC584.16c","SPCC1906.02c","SPAC6B12.02c","SPCC794.09c","SPAC607.06c","SPAC22H10.11c","SPCC777.13","SPCC613.06","SPAC18G6.01c","SPCC1753.02c","SPAC5H10.06c","SPCC1322.02","SPAC1782.11","SPCC622.14","SPAC3A12.10","SPCC1322.07c","SPCC1450.02","SPBP8B7.10c","SPBC2G2.03c","SPAC1F12.07","SPBC660.07","SPAC31G5.11","SPCC970.05","SPAC11E3.08c","SPCC645.12c","SPAC17H9.14c","SPBC8D2.18c","SPBC1718.03","SPAC13F5.03c","SPBC1734.12c","SPCC16C4.14c","SPAC8F11.02c","SPCC24B10.07","SPBC428.06c","SPCP31B10.07","SPCC23B6.03c","SPCC16A11.04","SPCC330.14c","SPAC3C7.09","SPCC1259.11c","SPAC3C7.12","SPCC1259.09c","SPAC664.02c","SPCC16A11.01","SPAPB1A10.05","SPCC736.13","SPAC6G10.06","SPCC16A11.08","SPAC1250.04c","SPBC13G1.10c","SPAC13F5.05","SPAC25H1.07","SPAC9G1.02","SPBC2G5.06c","SPAC18G6.05c","SPCC777.15","SPBC8D2.17","SPCC1902.01","SPCC1281.04","SPBC106.10","SPBC1703.12","SPCC1322.16","SPCC1322.06","SPBC2F12.09c","SPCC622.19","SPAC959.06c","SPBC1685.01","SPBC16E9.12c","SPBP4H10.13","SPCC306.07c","SPBC20F10.05","SPAC637.10c","SPAC24B11.13","SPAC3H1.13","SPAC6G10.08","SPCC18B5.06","SPAC1851.03","SPAC23C11.07","SPCC1795.09","SPCC74.02c","SPCC4B3.12","SPAC23C11.01","SPAC3C7.07c","SPBC26H8.03","SPCC1753.03c","SPAC18G6.13","SPAC3H8.05c","SPAC56F8.09","SPCC4B3.11c","SPBC26H8.05c","SPAC1142.08","SPAC328.10c","SPAC17A5.16","SPAC1B3.01c","SPCC1020.11c","SPAC20G4.04c","SPAC926.03","SPAC20G4.07c","SPCC794.11c","SPCC4B3.13","SPCPB16A4.04c","SPAC9G1.11c","SPAC1783.01","SPAC521.05","SPAC4G9.15","SPCC736.04c","SPAP7G5.05","SPBC3D6.04c","SPAC3H1.06c","SPCC645.07","SPBC19F8.08","SPAC3H8.07c","SPAC6C3.07","SPAC3C7.02c","SPAC17G8.13c","SPCC24B10.15","SPCC1259.10","SPBC2G5.02c","SPBC15C4.01c","SPAC20H4.11c","SPBC30D10.10c","SPCC895.07","SPAC1F7.04","SPCC550.01c","SPCC1223.01","SPAC343.19","SPAC23C11.06c","SPAC19A8.04","SPCC11E10.03","SPAC1527.02","SPAC607.07c","SPAC15A10.06","SPBC1652.02","SPCC584.03c","SPAC8C9.07","SPCC63.14","SPCC330.02","SPCC320.03","SPCC1322.03","SPCC1322.15","SPBC1709.11c","SPCC11E10.05c","SPAC664.01c","SPAC4G9.14","SPAC17A5.07c","SPCP25A2.02c","SPAC222.08c","SPAC13G7.02c","SPAC18G6.10","SPAC3C7.01c","SPAC18G6.02c","SPCC338.16","SPBP35G2.08c","SPAC17H9.04c","SPBC8D2.12c","SPAC1851.02","SPCC285.17","SPBC29A3.02c","SPCC24B10.13","SPAC3C7.04","SPAC17A5.18c","SPAC1071.04c","SPBC18H10.07","SPCPB16A4.06c","SPCC330.06c","SPBC27B12.11c","SPAC1B2.04","SPCC31H12.06","SPBC119.12","SPAC25G10.06","SPCC338.04","SPBC3B9.13c","SPAC3C7.13c","SPCC622.01c","SPAC23C11.13c","SPCC645.08c","SPCC622.15c","SPBC2D10.17","SPCC777.03c","SPAC9G1.05","SPAC1782.05","SPCC16A11.03c","SPAC20H4.09","SPCC1259.03","SPCC11E10.09c","SPCC63.03","SPBC19G7.17","SPAC890.05","SPCC2H8.05c","SPCC1322.14c","SPAC13F5.04c","SPBC16H5.08c","SPBC215.02","SPCC61.03","SPCC16C4.04","SPCC757.12","SPAC18G6.12c","SPAC6F12.09","SPCC188.02","SPAC6C3.04","SPAC1486.01","SPBC30D10.16","SPBC337.04","SPAC144.11","SPAC3H1.12c","SPAC32A11.03c","SPBPB7E8.02","SPCC18B5.11c","SPAC323.05c","SPAC631.02","SPBC1711.03","SPCC188.12","SPAC589.05c","SPBC6B1.06c","SPAC4G9.06c","SPBC428.16c","SPCPB16A4.02c","SPBC17A3.06","SPCC23B6.05c","SPCC306.11","SPAC6F12.06","SPCC757.07c","SPBC30D10.18c","SPCC338.02","SPAC23E2.01","SPAC3C7.05c","SPAC1B3.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binding of Nro1 to the prolyl hydroxylase Ofd1 regulates SREBP degradation in yeast.","citation":"EMBO J 2009 Jan 21;28(2):135-43","abstract":"Sre1, the fission yeast sterol regulatory element-binding protein, is an ER membrane-bound transcription factor that controls adaptation to low oxygen growth. Under low oxygen, Sre1 is proteolytically cleaved and the N-terminal transcription factor domain (Sre1N) is released from the membrane and enters the nucleus to activate hypoxic gene expression. Ofd1, a prolyl 4-hydroxylase-like 2-oxoglutarate dioxygenase, controls the oxygen-dependent stability of Sre1N. In the presence of oxygen, Ofd1 accelerates the degradation of Sre1N, but under low oxygen Ofd1 is inhibited and Sre1N accumulates. To identify the regulators of Sre1N, we performed a plasmid-based screen for genes that increased Sre1N transcriptional activity. Here, we identify Nro1 (SPCC4B3.07) as a positive regulator of Sre1N stability and a direct inhibitor of Ofd1. In the absence of oxygen, Nro1 binds to the Ofd1 C-terminal degradation domain and inhibits Sre1N degradation. In the presence of oxygen, Nro1 binding to Ofd1 is disrupted, leading to rapid degradation of Sre1N. We conclude that the Ofd1 dioxygenase domain functions as an oxygen sensor that regulates binding of Nro1 to Ofd1 to control oxygen-dependent Sre1N stability.","doi":"10.1038/emboj.2008.271","authors":"Lee CY, Stewart EV, Hughes BT, Espenshade PJ","authors_abbrev":"Lee CY et al.","pubmed_publication_date":"21 Jan 2009","pubmed_entrez_date":"2009-01-23","publication_year":"2009","canto_session_key":"c3ea2fabd9d13197","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2012-06-22 20:39:33","canto_approved_date":"2021-10-06 15:56:05","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-06-13 12:41:12","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.08c","SPCC4B3.07","SPBC19C2.09"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2012-06-22"},{"uniquename":"PMID:27984744","title":"Survival in Quiescence Requires the Euchromatic Deployment of Clr4/SUV39H by Argonaute-Associated Small RNAs.","citation":"Mol Cell 2016 Dec 15;64(6):1088-1101","abstract":"Quiescence (G0) is a ubiquitous stress response through which cells enter reversible dormancy, acquiring distinct properties including reduced metabolism, resistance to stress, and long life. G0 entry involves dramatic changes to chromatin and transcription of cells, but the mechanisms coordinating these processes remain poorly understood. Using the fission yeast, here, we track G0-associated chromatin and transcriptional changes temporally and show that as cells enter G0, their survival and global gene expression programs become increasingly dependent on Clr4/SUV39H, the sole histone H3 lysine 9 (H3K9) methyltransferase, and RNAi proteins. Notably, G0 entry results in RNAi-dependent H3K9 methylation of several euchromatic pockets, prior to which Argonaute1-associated small RNAs from these regions emerge. Overall, our data reveal another function for constitutive heterochromatin proteins (the establishment of the global G0 transcriptional program) and suggest that stress-induced alterations in Argonaute-associated sRNAs can target the deployment of transcriptional regulatory proteins to specific sequences.","doi":"10.1016/j.molcel.2016.11.020","authors":"Joh RI, Khanduja JS, Calvo IA, Mistry M, Palmieri CM, Savol AJ, Ho Sui SJ, Sadreyev RI, Aryee MJ, Motamedi M","authors_abbrev":"Joh RI et al.","pubmed_publication_date":"15 Dec 2016","pubmed_entrez_date":"2016-12-17","publication_year":"2016","canto_session_key":"f44eccf92770b920","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-07-14 16:46:47","canto_approved_date":"2023-01-03 16:49:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-07-14 16:46:11","canto_added_date":"2016-12-18 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network analysis in Schizosaccharomyces pombe reveals three distinct consequences of the common 1-kb deletion causing juvenile CLN3 disease.","citation":"Sci Rep 2021 Mar 18;11(1):6332","abstract":"Juvenile CLN3 disease is a recessively inherited paediatric neurodegenerative disorder, with most patients homozygous for a 1-kb intragenic deletion in CLN3. The btn1 gene is the Schizosaccharomyces pombe orthologue of CLN3. Here, we have extended the use of synthetic genetic array (SGA) analyses to delineate functional signatures for two different disease-causing mutations in addition to complete deletion of btn1. We show that genetic-interaction signatures can differ for mutations in the same gene, which helps to dissect their distinct functional effects. The mutation equivalent to the minor transcript arising from the 1-kb deletion (btn1 102-208del ) shows a distinct interaction pattern. Taken together, our results imply that the minor 1-kb deletion transcript has three consequences for CLN3: to both lose and retain some inherent functions and to acquire abnormal characteristics. This has particular implications for the therapeutic development of juvenile CLN3 disease. In addition, this proof of concept could be applied to conserved genes for other mendelian disorders or any gene of interest, aiding in the dissection of their functional domains, unpacking the global consequences of disease pathogenesis, and clarifying genotype-phenotype correlations. In doing so, this detail will enhance the goals of personalised medicine to improve treatment outcomes and reduce adverse events.","doi":"10.1038/s41598-021-85471-4","authors":"Minnis CJ, Townsend S, Petschnigg J, Tinelli E, Bähler J, Russell C, Mole SE","authors_abbrev":"Minnis CJ et al.","pubmed_publication_date":"18 Mar 2021","pubmed_entrez_date":"2021-03-19","publication_year":"2021","canto_session_key":"f64287df5709efb8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-03-21 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22140232","title":"Snf1-like protein kinase Ssp2 regulates glucose derepression in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2012 Feb;11(2):159-67","abstract":"The function of two fission yeast genes, SPCC74.03c/ssp2(+) and SPAC23H4.02/ppk9(+), encoding an Snf1-like protein kinase were investigated. Deletion of ssp2(+) caused a partial defect in glucose derepression of inv1(+), fbp1(+), and gld1(+) and in assimilation of sucrose and glycerol, while a mutation in ppk9(+) had no apparent effect. Scr1, a transcription factor involved in glucose repression, localized to the nucleus under glucose-rich conditions and to the cytoplasm during glucose starvation in wild-type cells. In contrast, in the ssp2Δ mutant, Scr1 localized to the nucleus in cells grown in glucose-rich medium as well as in glucose-starved cells. Immunoblot analysis showed that Ssp2 is required for the phosphorylation of Scr1 upon glucose deprivation. Mutation of five putative Ssp2 recognition sites in Scr1 prevented glucose derepression of invertase in glucose-starved cells. These results indicate that Ssp2 regulates phosphorylation and subcellular localization of Scr1 in response to glucose.","doi":"10.1128/EC.05268-11","authors":"Matsuzawa T, Fujita Y, Tohda H, Takegawa K","authors_abbrev":"Matsuzawa T et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-12-06","publication_year":"2012","canto_session_key":"118900a57ae7a3da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-28 16:43:37","canto_approved_date":"2026-03-17 07:56:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-28 16:41:00","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":53,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1D7.02c","SPAC23H4.02","SPCC74.03c","SPAC1556.08c","SPCC191.11","SPAC13F5.03c","SPBC1198.14c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2018-02-28"},{"uniquename":"PMID:17016471","title":"Repression of ergosterol level during oxidative stress by fission yeast F-box protein Pof14 independently of SCF.","citation":"EMBO J 2006 Oct 04;25(19):4547-56","abstract":"We describe a new member of the F-box family, Pof14, which forms a canonical, F-box dependent SCF (Skp1, Cullin, F-box protein) ubiquitin ligase complex. The Pof14 protein has intrinsic instability that is abolished by inactivation of its Skp1 interaction motif (the F-box), Skp1 or the proteasome, indicating that Pof14 stability is controlled by an autocatalytic mechanism. Pof14 interacts with the squalene synthase Erg9, a key enzyme in ergosterol metabolism, in a membrane-bound complex that does not contain the core SCF components. pof14 transcription is induced by hydrogen peroxide and requires the Pap1 transcription factor and the Sty1 MAP kinase. Pof14 binds to and decreases Erg9 activity in vitro and a pof14 deletion strain quickly loses viability in the presence of hydrogen peroxide due to its inability to repress ergosterol synthesis. A pof14 mutant lacking the F-box and an skp1-3 ts mutant behave as wild type in the presence of oxidant showing that Pof14 function is independent of SCF. This indicates that modulation of ergosterol level plays a key role in adaptation to oxidative stress.","authors":"Tafforeau L, Le Blastier S, Bamps S, Dewez M, Vandenhaute J, Hermand D","authors_abbrev":"Tafforeau L et al.","pubmed_publication_date":"04 Oct 2006","pubmed_entrez_date":"2006-10-04","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21.05c","SPBC1703.06","SPAC9.02c","SPCC1682.02c","SPBC776.18c","SPCC11E10.07c","SPAC13D6.01","SPCC1827.08c","SPBP4H10.11c","SPBC17D11.05","SPBC14F5.04c","SPAC16E8.18","SPAC26F1.06","SPBC409.05","SPAC1705.03c","SPBC17D1.01","SPBC646.05c","SPAC1783.07c","SPAC17G6.12","SPAC3A12.18","SPCC18.04","SPAC890.02c","SPAC4D7.03","SPAC56F8.05c"],"gene_count":24,"ltp_gene_count":5},{"uniquename":"PMID:1475195","title":"The protein sequence and some intron positions are conserved between the switching gene swi10 of Schizosaccharomyces pombe and the human excision repair gene ERCC1.","citation":"Nucleic Acids Res 1992 Dec 11;20(23):6347-53","abstract":"The switching gene swi10+ has a function in mating-type switching as well as in the repair of radiation damages. We have cloned the genomic swi10+ gene by functional complementation of the switching defect of the swi10-154 mutant. The swi10+ gene is not essential for viability. The DNA sequence revealed an open reading frame of 759 nucleotides interrupted by three introns of 127, 52 and 60 bp, respectively. The positions of intron I as well as of intron III of swi10 are evolutionary conserved in comparison to the introns III and IV of the human ERCC1 gene. The analysis of cDNA clones isolated by PCR amplification confirmed the structure of the swi10 gene. The putative Swi10 protein has homologies to the human and mouse ERCC1 protein, to Rad10 of Saccharomyces cerevisiae and to parts of UvrA and UvrC of E. coli. All these proteins are essential components for excision repair of damaged DNA. The Swi10 protein contains a putative DNA binding domain previously found in other proteins. Northern blot experiments and the analyses of cDNA clones indicate that intron I of the swi10 gene is not efficiently spliced.","authors":"Rödel C, Kirchhoff S, Schmidt H","authors_abbrev":"Rödel C et al.","pubmed_publication_date":"11 Dec 1992","pubmed_entrez_date":"1992-12-11","publication_year":"1992","canto_session_key":"3448b2e04419517c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-01-19 14:59:52","canto_approved_date":"2021-04-15 16:33:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-12-03 17:07:13","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.15c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-19"},{"uniquename":"PMID:15082762","title":"A novel protein with similarities to Rb binding protein 2 compensates for loss of Chk1 function and affects histone modification in fission yeast.","citation":"Mol Cell Biol 2004 May;24(9):3660-9","abstract":"The conserved protein kinase Chk1 mediates cell cycle progression and consequently the ability of cells to survive when exposed to DNA damaging agents. Cells deficient in Chk1 are hypersensitive to such agents and enter mitosis in the presence of damaged DNA, whereas checkpoint-proficient cells delay mitotic entry to permit time for DNA repair. In a search for proteins that can improve the survival of Chk1-deficient cells exposed to DNA damage, we identified fission yeast Msc1, which is homologous to a mammalian protein that binds to the tumor suppressor Rb (RBP2). Msc1 and RBP2 each possess three PHD fingers, domains commonly found in proteins that influence the structure of chromatin. Msc1 is chromatin associated and coprecipitates a histone deacetylase activity, a property that requires the PHD fingers. Cells lacking Msc1 have a dramatically altered histone acetylation pattern, exhibit a 20-fold increase in global acetylation of histone H3 tails, and are readily killed by trichostatin A, an inhibitor of histone deacetylases. We postulate that Msc1 plays an important role in regulating chromatin structure and that this function modulates the cellular response to DNA damage.","authors":"Ahmed S, Palermo C, Wan S, Walworth NC","authors_abbrev":"Ahmed S et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-04-15","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC343.11c","SPAC20G8.01"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU011048","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31243991","title":"The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation.","citation":"Biochemistry 2019 Jul 09;58(27):3031-3041","abstract":"Division of fungal and animal cells depends on scaffold proteins called anillins. Cytokinesis by the fission yeast Schizosaccharomyces pombe is compromised by the loss of anillin Mid1p (Mid1, UniProtKB P78953 ), because cytokinesis organizing centers, called nodes, are misplaced and fail to acquire myosin-II, so they assemble slowly into abnormal contractile rings. The C-terminal half of Mid1p consists of lipid binding C2 and PH domains, but the N-terminal half (Mid1p-N452) performs most of the functions of the full-length protein. Little is known about the structure of the N-terminal half of Mid1p, so we investigated its physical properties using structure prediction tools, spectroscopic techniques, and hydrodynamic measurements. The data indicate that Mid1p-N452 is intrinsically disordered but moderately compact. Recombinant Mid1p-N452 purified from insect cells was phosphorylated, which weakens its tendency to aggregate. Purified Mid1p-N452 demixes into liquid droplets at concentrations far below its concentration in nodes. These physical properties are appropriate for scaffolding other proteins in nodes.","doi":"10.1021/acs.biochem.9b00217","authors":"Chatterjee M, Pollard TD","authors_abbrev":"Chatterjee M et al.","pubmed_publication_date":"09 Jul 2019","pubmed_entrez_date":"2019-06-28","publication_year":"2019","canto_session_key":"5aaa3b29566066e1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-06-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12127488","title":"Functional characterization of 4'-phosphopantetheinyl transferase genes of bacterial and fungal origin by complementation of Saccharomyces cerevisiae lys5.","citation":"FEMS Microbiol Lett 2002 Jul 16;213(1):51-7","abstract":"Lysine biosynthesis in yeast requires the posttranslational conversion of the alpha-aminoadipate semialdehyde reductase Lys2 by the 4'-phosphopantetheinyl transferase (PPTase) Lys5 from the inactive apo-form into the catalytically active holo-form. In this reaction, the peptidyl carrier domain of Lys2 is modified at a conserved serine residue side chain with the 4'-phosphopantetheine moiety derived from coenzyme A. We have deleted the lys5 gene in Saccharomyces cerevisiae to investigate the substrate specificity of various heterologous PPTase genes of bacterial and fungal origin by testing their ability to complement lys5 in trans. Genes encoding PPTases Sfp and Gsp from Bacillus spp., which are involved in non-ribosomal peptide antibiotic synthesis, complemented the lys5 deletion, whereas ydcB of Bacillus subtilis, which encodes the acyl carrier protein synthase involved in fatty acid synthesis, could not. Two yet uncharacterized fungal genes, q10474 of Schizosaccharomyces pombe, meanwhile annotated as the putative lys7 gene, and npgA of Aspergillus nidulans, also complemented the lys5 deletion and have thus been functionally characterized as PPTases. The complementation system described also provides the basis for a simple method of functional characterization of PPTase candidate genes and their cloning from chromosomal DNA or cDNA libraries of diverse origin.","authors":"Mootz HD, Schörgendorfer K, Marahiel MA","authors_abbrev":"Mootz HD et al.","pubmed_publication_date":"16 Jul 2002","pubmed_entrez_date":"2002-07-20","publication_year":"2002","canto_session_key":"34f72c176b7505ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-26 11:18:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 16:04:59","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-06"},{"uniquename":"PMID:7803852","title":"Physical mapping of origins of replication in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1994 Aug;5(8):839-49","abstract":"We isolated four fragments from the Schizosaccharomyces pombe genome that mediate autonomous replication. A two-dimensional gel analysis revealed that in each case initiation could be mapped to within the S. pombe sequences. In three of the fragments, initiation could be mapped to one discrete location. In the fourth fragment, subcloning and two-dimensional gel analysis suggested that two discrete origins of replication were located within 3 kb of each other. When in proximity, usually only one of these origins fired, suggesting origin interference. Two-dimensional gel analysis of the four origin fragments at their genomic locations demonstrated that each is used in the chromosomes, but in only a subset of cells or cell divisions. The S. pombe genome appears to contain many discrete origins, not all of which fire in any given cell and some of which are closely spaced. Not I/Sfi I mapping of the five origins from this and a previous study indicates that they are randomly distributed throughout the genome and appear to be representative of chromosomal origins of replication in this organism. We compare the features of S. pombe replication origins with those of S. cerevisiae and animal cells.","authors":"Wohlgemuth JG, Bulboaca GH, Moghadam M, Caddle MS, Calos MP","authors_abbrev":"Wohlgemuth JG et al.","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012826","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28840243","title":"DNA Sequences in Centromere Formation and Function.","citation":"Prog Mol Subcell Biol 2017;56:305-336","abstract":"Faithful chromosome segregation during cell division depends on the centromere, a complex DNA/protein structure that links chromosomes to spindle microtubules. This chromosomal domain has to be marked throughout cell division and its chromosomal localization preserved across cell generations. From fission yeast to human, centromeres are established on a series of repetitive DNA sequences and on specialized centromeric chromatin. This chromatin is enriched with the histone H3 variant, named CENP-A, that was demonstrated to be the epigenetic mark that maintains centromere identity and function indefinitely. Although centromere identity is thought to be exclusively epigenetic, the presence of specific DNA sequences in the majority of eukaryotes and of the centromeric protein CENP-B that binds to these sequences, suggests the existence of a genetic component as well. In this review, we will highlight the importance of centromeric sequences for centromere formation and function, and discuss the centromere DNA sequence/CENP-B paradox.","doi":"10.1007/978-3-319-58592-5_13","authors":"Dumont M, Fachinetti D","authors_abbrev":"Dumont M et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-08-26","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-08-27 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19147354","title":"Establishing new sites of polarization by microtubules.","citation":"Curr Biol 2009 Jan 27;19(2):83-94","abstract":"Microtubules (MTs) participate in the spatial regulation of actin-based processes such as cytokinesis and cell polarization. The fission yeast Schizosaccharomyces pombe is a rod-shaped cell that exhibits polarized cell growth at cell tips. MT plus ends contact and shrink from the cell tips and contribute to polarity regulation.\nHere, we investigate the effects of changing cell shape on MTs and cell-polarization machinery. We physically bend fission yeast cells by forcing them into microfabricated femtoliter chambers. In these bent cells, MTs maintain a straight axis and contact and shrink from cortical sites at the sides of cells. At these ectopic sites, polarity factors such as bud6p, for3p (formin), and cdc42p are recruited and assemble actin cables in a MT-dependent manner. MT contact at the cortex induces the appearance of a bud6p dot within seconds. The accumulation of polarity factors leads to cell growth at these sites, when the MT-associated polarity factor tea1p is absent. This process is dependent on MTs, mal3p (EB1), moe1p (an EB1-binding protein), and for3p but, surprisingly, is independent of the tea1p-tea4p pathway.\nThese studies provide a direct demonstration for how MTs induce actin assembly at specific locations on the cell cortex and begin to identify a new pathway involved in this process. MT interactions with the cortex may be regulated by cortical-attachment sites. These findings highlight the crosstalk between cell shape, polarity mechanisms, and MTs responsible for cell morphogenesis.","doi":"10.1016/j.cub.2008.12.008","authors":"Minc N, Bratman SV, Basu R, Chang F","authors_abbrev":"Minc N et al.","pubmed_publication_date":"27 Jan 2009","pubmed_entrez_date":"2009-01-17","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26016543","title":"Combine Use of Selected Schizosaccharomyces pombe and Lachancea thermotolerans Yeast Strains as an Alternative to the Traditional Malolactic Fermentation in Red Wine Production.","citation":"Molecules 2015 May 26;20(6):9510-23","abstract":"Most red wines commercialized in the market use the malolactic fermentation process in order to ensure stability from a microbiological point of view. In this second fermentation, malic acid is converted into L-lactic acid under controlled setups. However this process is not free from possible collateral effects that on some occasions produce off-flavors, wine quality loss and human health problems. In warm viticulture regions such as the south of Spain, the risk of suffering a deviation during the malolactic fermentation process increases due to the high must pH. This contributes to produce wines with high volatile acidity and biogenic amine values. This manuscript develops a new red wine making methodology that consists of combining the use of two non-Saccharomyces yeast strains as an alternative to the traditional malolactic fermentation. In this method, malic acid is totally consumed by Schizosaccharomyces pombe, thus achieving the microbiological stabilization objective, while Lachancea thermotolerans produces lactic acid in order not to reduce and even increase the acidity of wines produced from low acidity musts. This technique reduces the risks inherent to the malolactic fermentation process when performed in warm regions.The result is more fruity wines that contain less acetic acid and biogenic amines than the traditional controls that have undergone the classical malolactic fermentation.","doi":"10.3390/molecules20069510","authors":"Benito Á, Calderón F, Palomero F, Benito S","authors_abbrev":"Benito Á et al.","pubmed_publication_date":"26 May 2015","pubmed_entrez_date":"2015-05-29","publication_year":"2015","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2015-05-30 00:19:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9701287","title":"The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast.","citation":"RNA 1998 Aug;4(8):958-72","abstract":"Translation termination in eukaryotes requires a codon-specific (class-I) release factor, eRF1, and a GTP/GDP-dependent (class-II) release factor, eRF3. The model of \"molecular mimicry between release factors and tRNA\" predicts that eRF1 mimics tRNA to read the stop codon and that eRF3 mimics elongation factor EF-Tu to bring eRF1 to the A site of the ribosome for termination of protein synthesis. In this study, we set up three systems, in vitro affinity binding, a yeast two-hybrid system, and in vitro competition assay, to determine the eRF3-binding site of eRF1 using the fission yeast Schizosaccharomyces pombe proteins and creating systematic deletions in eRF1. The in vitro affinity binding experiments demonstrated that the predicted tRNA-mimicry truncation of eRF1 (Sup45) forms a stable complex with eRF3 (Sup35). All three test systems revealed that the most critical binding site is located at the C-terminal region of eRF1, which is conserved among eukaryotic eRF1s and rich in acidic amino acids. To our surprise, however, the C-terminal deletion eRF1 seems to be sufficient for cell viability in spite of the severe defect in eRF3 binding when expressed in a temperature-sensitive sup45 mutant of the budding yeast, Saccharomyces cerevisiae. These results cannot be accounted for by the simple \"eRF3-EF-Tu mimicry\" model, but may provide new insight into the eRF3 function for translation termination in eukaryotes.","authors":"Ito K, Ebihara K, Nakamura Y","authors_abbrev":"Ito K et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-08-13","publication_year":"1998","canto_session_key":"6f0b1b999efe2190","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-09 16:25:10","canto_approved_date":"2019-01-09 16:25:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-09 16:25:02","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC584.04","SPAC1834.01","SPCC18B5.06"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-01-09"},{"uniquename":"PMID:18723894","title":"Rtf1-mediated eukaryotic site-specific replication termination.","citation":"Genetics 2008 Sep;180(1):27-39","abstract":"The molecular mechanisms mediating eukaryotic replication termination and pausing remain largely unknown. Here we present the molecular characterization of Rtf1 that mediates site-specific replication termination at the polar Schizosaccharomyces pombe barrier RTS1. We show that Rtf1 possesses two chimeric myb/SANT domains: one is able to interact with the repeated motifs encoded by the RTS1 element as well as the elements enhancer region, while the other shows only a weak DNA binding activity. In addition we show that the C-terminal tail of Rtf1 mediates self-interaction, and deletion of this tail has a dominant phenotype. Finally, we identify a point mutation in Rtf1 domain I that converts the RTS1 element into a replication barrier of the opposite polarity. Together our data establish that multiple protein DNA and protein-protein interactions between Rtf1 molecules and both the repeated motifs and the enhancer region of RTS1 are required for site-specific termination at the RTS1 element.","doi":"10.1534/genetics.108.089243","authors":"Eydmann T, Sommariva E, Inagawa T, Mian S, Klar AJ, Dalgaard JZ","authors_abbrev":"Eydmann T et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-08-30","publication_year":"2008","canto_session_key":"36fa256918417316","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-12 14:33:41","canto_approved_date":"2026-02-09 11:06:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-12 14:33:30","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F8.07c","SPBC216.06c","SPBC30D10.04"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-04-12"},{"uniquename":"PMID:14566325","title":"Genome-wide distribution of DNA replication origins at A+T-rich islands in Schizosaccharomyces pombe.","citation":"EMBO Rep 2003 Nov;4(11):1048-53","abstract":"Genome-wide analysis of replication dynamics requires the previous identification of DNA replication origins (ORIs). However, variability among the ORIs makes it difficult to predict their distribution across the genome on the basis of their sequence. We report here that ORIs in Schizosaccharomyces pombe coincide with discrete chromosomal A+T-rich islands of up to 1 kb long that are characterized by a distinctive A+T content that clearly differentiates them from the rest of the genome. Genome-wide analysis has enabled us to identify 384 of these regions, which predicts the position of most ORIs in the genome, as shown by functional replication analyses. A+T-rich islands occur at the mating locus, centromeres and subtelomeric regions at a density that is approximately fourfold higher than elsewhere in the genome, which suggests a link between the origin recognition complex (ORC) and transcriptional silencing in these regions. The absence of consensus elements in A+T-rich islands implies that different sequences can target the ORC to different ORIs.","authors":"Segurado M, de Luis A, Antequera F","authors_abbrev":"Segurado M et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-10-21","publication_year":"2003","canto_session_key":"1187e25113be8a13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-08-16 11:19:20","canto_approved_date":"2019-08-16 11:19:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-08-16 11:19:09","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-08-16"},{"uniquename":"EMBL:SP29892","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41996447","title":"Constitutively active RAS prolongs Cdc42 signalling, while MAPK signalling is attenuated during fission yeast mating.","citation":"PLoS Genet 2026 Apr 17;22(4):e1012117","abstract":"The small GTPase RAS is a signalling hub activating multiple pathways, which may respond differently to a constitutively active RAS mutation. We explored this issue in fission yeast, where RAS-mediated pheromone signalling (PS) activates two downstream pathways: the MAPKSpk1 and Cdc42 pathways. We observed that the yeast RAS mutation ras1.G17V, an equivalent of the mammalian ras.G12V oncogenic mutation, causes prolonged Cdc42 activation, whereas MAPKSpk1 activation was transient and attenuated. To explain this observation, we generated a PS framework by conducting genetic epistasis analysis of PS mutants and biochemical analysis of two Ras1 effectors, Cdc42-GEFScd1 and MAPKKKByr2, each of which triggers activation of the Cdc42 and MAPKSpk1 pathways, respectively. Cdc42-GEFScd1 and MAPKKKByr2 directly interacted with Ras1 in vitro in a competitive manner, and overexpression of the Ras binding domain of either Cdc42-GEFScd1 or MAPKKKByr2 in cells inhibited both downstream pathways, confirming that Ras1 signalling branches into the MAPKSpk1 and Cdc42 pathways. In conjunction with the genetic epistasis analysis, we developed the PS framework-based mathematical model to test which network structures can explain the transient MAPKSpk1 activation profile. Incorporating a negative-feedback circuit acting on pheromone production or sensing enabled the model to quantitatively reproduce MAPKSpk1 dynamics in the wild type and 20 additional PS mutants. The predicted PS negative-feedback was experimentally confirmed by deleting Sxa2, the carboxypeptidase that degrades one of the mating pheromones, which led to hyperactivation of both MAPKSpk1 and Cdc42. Our study provides a holistic understanding of the fission yeast pheromone signalling network, explaining how RAS signalling propagates differently through two downstream pathways. Our PS mathematical model may serve as a valuable reference framework for analysing other RAS signalling systems.","doi":"10.1371/journal.pgen.1012117","authors":"Kelsall EJ, Kimura A, Vértesy Á, Straatman KR, Tariq M, Gadea R, Parmar C, Schreiber G, Randhawa S, Ida TY, Dominguez C, Klipp E, Tanaka K","authors_abbrev":"Kelsall EJ et al.","pubmed_publication_date":"17 Apr 2026","pubmed_entrez_date":"2026-04-17","publication_year":"2026","canto_session_key":"4c4aca3efd55545a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-17 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1238264","title":"Parametric analysis of volume distributions of Schizosaccharomyces pombe and other cells.","citation":"Exp Cell Res 1975 Sep;94(2):267-76","abstract":"","authors":"James TW, Hemond P, Czer G, Bohman R","authors_abbrev":"James TW et al.","pubmed_publication_date":"Sep 1975","pubmed_entrez_date":"1975-09-01","publication_year":"1975","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12456004","title":"Schizosaccharomyces pombe Git7p, a member of the Saccharomyces cerevisiae Sgtlp family, is required for glucose and cyclic AMP signaling, cell wall integrity, and septation.","citation":"Eukaryot Cell 2002 Aug;1(4):558-67","abstract":"The Schizosaccharomyces pombe fbp1 gene, encoding fructose-1,6-bisphosphatase, is transcriptionally repressed by glucose. Mutations that confer constitutive fbp1 transcription identify git (glucose-insensitive transcription) genes that encode components of a cyclic AMP (cAMP) signaling pathway required for adenylate cyclase activation. Four of these genes encode the three subunits of a heterotrimeric G protein (gpa2, git5, and git11) and a G protein-coupled receptor (git3). Three additional genes, git1, git7, and git10, act in parallel to or downstream from the G protein genes. Here, we describe the cloning and characterization of the git7 gene. The Git7p protein is a member of the Saccharomyces cerevisiae Sgtlp protein family. In budding yeast, Sgtlp associates with Skplp and plays an essential role in kinetochore assembly, while in Arabidopsis, a pair of SGT1 proteins have been found to be involved in plant disease resistance through an interaction with RAR1. Like S. cerevisiae Sgtlp, Git7p is essential, but this requirement appears to be due to roles in septation and cell wall integrity, which are unrelated to cAMP signaling, as S. pombe cells lacking either adenylate cyclase or protein kinase A are viable. In addition, git7 mutants are sensitive to the microtubule-destabilizing drug benomyl, although they do not display a chromosome stability defect. Two alleles of git7 that are functional for cell growth and septation but defective for glucose-triggered cAMP signaling encode proteins that are altered in the highly conserved carboxy terminus. The S. cerevisiae and human SGT1 genes both suppress git7-93 but not git7-235 for glucose repression of fbp1 transcription and benomyl sensitivity. This allele-specific suppression indicates that the Git7p/Sgtlp proteins may act as multimers, such that Git7-93p but not Git7-235p can deliver the orthologous proteins to species-specific targets. Our studies suggest that members of the Git7p/Sgt1p protein family may play a conserved role in the regulation of adenylate cyclase activation in S. pombe, S. cerevisiae, and humans.","authors":"Schadick K, Fourcade HM, Boumenot P, Seitz JJ, Morrell JL, Chang L, Gould KL, Partridge JF, Allshire RC, Kitagawa K, Hieter P, Hoffman CS","authors_abbrev":"Schadick K et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-11-29","publication_year":"2002","canto_session_key":"a09d826a70b1a2d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-26 14:51:35","canto_approved_date":"2024-04-09 10:00:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-26 14:51:26","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.12c","SPBC409.05","SPBC19C7.03","SPBC29A3.02c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-07-26"},{"uniquename":"PMID:34250083","title":"Barcode sequencing and a high-throughput assay for chronological lifespan uncover ageing-associated genes in fission yeast.","citation":"Microb Cell 2021 Jul 05;8(7):146-160","abstract":"Ageing-related processes are largely conserved, with simple organisms remaining the main platform to discover and dissect new ageing-associated genes. Yeasts provide potent model systems to study cellular ageing owing their amenability to systematic functional assays under controlled conditions. Even with yeast cells, however, ageing assays can be laborious and resource-intensive. Here we present improved experimental and computational methods to study chronological lifespan in  Schizosaccharomyces pombe . We decoded the barcodes for 3206 mutants of the latest gene-deletion library, enabling the parallel profiling of ~700 additional mutants compared to previous screens. We then applied a refined method of barcode sequencing (Bar-seq), addressing technical and statistical issues raised by persisting DNA in dead cells and sampling bottlenecks in aged cultures, to screen for mutants showing altered lifespan during stationary phase. This screen identified 341 long-lived mutants and 1246 short-lived mutants which point to many previously unknown ageing-associated genes, including 46 conserved but entirely uncharacterized genes. The ageing-associated genes showed coherent enrichments in processes also associated with human ageing, particularly with respect to ageing in non-proliferative brain cells. We also developed an automated colony-forming unit assay to facilitate medium- to high-throughput chronological-lifespan studies by saving time and resources compared to the traditional assay. Results from the Bar-seq screen showed good agreement with this new assay. This study provides an effective methodological platform and identifies many new ageing-associated genes as a framework for analysing cellular ageing in yeast and beyond.","doi":"10.15698/mic2021.07.754","authors":"Romila CA, Townsend S, Malecki M, Kamrad S, Rodríguez-López M, Hillson O, Cotobal C, Ralser M, Bähler J","authors_abbrev":"Romila CA et al.","pubmed_publication_date":"05 Jul 2021","pubmed_entrez_date":"2021-07-12","publication_year":"2021","canto_session_key":"fb815dc7d9f5a139","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jurg Bahler","canto_first_approved_date":"2021-08-18 12:45:56","canto_approved_date":"2022-06-14 14:26:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-08-18 12:15:12","canto_added_date":"2021-07-14 00:15:04","annotation_curators":[{"name":"Jurg Bahler","community_curator":true,"annotation_count":7,"orcid":"0000-0003-4036-1532","file_type":null,"file_name":null}],"file_curator_name":"Jurg Bahler","file_curator_role":"community","annotation_file_curators":[{"name":"Jurg 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regulation of the Adh1 antisense transcript in fission yeast.","citation":"J Biol Chem 2013 Jan 11;288(2):759-69","abstract":"In yeast, Adh1 (alcohol dehydrogenase 1) is an abundant zinc-binding protein that is required for the conversion of acetaldehyde to ethanol. Through transcriptome profiling of the Schizosaccharomyces pombe genome, we identified a natural antisense transcript at the adh1 locus that is induced in response to zinc limitation. This antisense transcript (adh1AS) shows a reciprocal expression pattern to that of the adh1 mRNA partner. In this study, we show that increased expression of the adh1AS transcript in zinc-limited cells is necessary for the repression of adh1 gene expression and that the increased level of the adh1AS transcript in zinc-limited cells is a result of two mechanisms. At the transcriptional level, the adh1AS transcript is expressed at a high level in zinc-limited cells. In addition to this transcriptional control, adh1AS transcripts preferentially accumulate in zinc-limited cells when the adh1AS transcript is expressed from a constitutive promoter. This secondary mechanism requires the simultaneous expression of adh1. Our studies reveal how multiple mechanisms can synergistically control the ratio of sense to antisense transcripts and highlight a novel mechanism by which adh1 gene expression can be controlled by cellular zinc availability.","doi":"10.1074/jbc.M112.406165","authors":"Ehrensberger KM, Mason C, Corkins ME, Anderson C, Dutrow N, Cairns BR, Dalley B, Milash B, Bird AJ","authors_abbrev":"Ehrensberger KM et al.","pubmed_publication_date":"11 Jan 2013","pubmed_entrez_date":"2012-12-11","publication_year":"2013","canto_session_key":"e040dc62fa860ce5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-17 07:15:28","canto_approved_date":"2023-03-17 07:15:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-16 13:54:23","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC13B11.02c","SPCC13B11.01","SPNCRNA.1710"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2023-03-17"},{"uniquename":"PMID:19563126","title":"Incorporation of thymidine analogs for studying replication kinetics in fission yeast.","citation":"Methods Mol Biol 2009;521:509-15","abstract":"Labeling DNA during in vivo replication by the incorporation of exogenous thymidine and thymidine analogs has been a mainstay of DNA replication and repair studies for decades. Unfortunately, thymidine labeling does not work in fungi, because they lack the thymidine salvage pathway required for uptake of exogenous thymidine. This obstacle to thymidine labeling has been overcome in yeast by engineering a minimal thymidine salvage pathway consisting of a nucleoside transporter to allow uptake of exogenous thymidine from the medium and a thymidine kinase to phosphorylate the thymidine into thymidine monophosphate, which can be used by the cell. This chapter describes the labeling of fission yeast, Schizosaccharomyces pombe, with the thymidine analog BrdU in order to identify sites and determine kinetics of DNA replication.","doi":"10.1007/978-1-60327-815-7_29","authors":"Rhind N","authors_abbrev":"Rhind N","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15165244","title":"Activation of the redox sensor Pap1 by hydrogen peroxide requires modulation of the intracellular oxidant concentration.","citation":"Mol Microbiol 2004 Jun;52(5):1427-35","abstract":"The transcription factor Pap1 and the MAP kinase Sty1 are key regulators of hydrogen peroxide-induced responses in Schizosaccharomyces pombe. Pap1 can be activated quickly at low, but not high, hydrogen peroxide concentrations. The MAP kinase Sty1 has been reported to participate in Pap1 activation by the oxidant. Here, we provide biochemical and genetic evidence for the in vivo formation of a hydrogen peroxide-induced disulphide bond in Pap1, which precedes the rapid and reversible nuclear accumulation of the transcription factor. We show that activation of the Sty1 cascade before the oxidative insult, or overexpression of the Sty1-regulated genes ctt1 (encoding catalase) or gpx1 (encoding glutathione peroxidase), can accelerate Pap1 entry even at high doses of hydrogen peroxide. In fact, the lack of Sty1 impedes Pap1 nuclear localization, but only at high doses of the oxidant. We propose that, whereas low doses of hydrogen peroxide lead directly to Pap1 oxidation-activation, high concentrations of the oxidant initially activate the Sty1 pathway, with the consequent increase in scavenging enzymes, which in turn helps to decompose the excess of hydrogen peroxide and achieve an appropriate concentration for the subsequent activation of Pap1. Our results also suggest that activation of Sty1 at high doses of hydrogen peroxide may also be required to trigger other antioxidant activities such as those reverting the overoxidation of cysteine residues at the Pap1 pathway.","authors":"Vivancos AP, Castillo EA, Jones N, Ayté J, Hidalgo E","authors_abbrev":"Vivancos AP et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-05-29","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:26895050","title":"Qualitative and Quantitative Assays of Transposition and Homologous Recombination of the Retrotransposon Tf1 in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2016;1400:117-30","abstract":"Transposition and homologous recombination assays are valuable genetic tools to measure the production and integration of cDNA from the long terminal repeat (LTR) retrotransposon Tf1 in the fission yeast (Schizosaccharomyces pombe). Here we describe two genetic assays, one that measures the transposition activity of Tf1 by monitoring the mobility of a drug resistance marked Tf1 element expressed from a multi-copy plasmid and another assay that measures homologous recombination between Tf1 cDNA and the expression plasmid. While the transposition assay measures insertion of full-length Tf1 cDNA mediated by the transposon integrase, the homologous recombination assay measures levels of cDNA present in the nucleus and is independent of integrase activity. Combined, these assays can be used to systematically screen large collections of strains to identify mutations that specifically inhibit the integration step in the retroelement life cycle. Such mutations can be identified because they reduce transposition activity but nevertheless have wild-type frequencies of homologous recombination. Qualitative assays of yeast patches on agar plates detect large defects in integration and recombination, while the quantitative approach provides a precise method of determining integration and recombination frequencies.","doi":"10.1007/978-1-4939-3372-3_8","authors":"Sangesland M, Atwood-Moore A, Rai SK, Levin HL","authors_abbrev":"Sangesland M et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-02-20","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-02-21 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21138961","title":"A novel function of the mitochondrial transcription factor Mtf1 in fission yeast; Mtf1 regulates the nuclear transcription of srk1.","citation":"Nucleic Acids Res 2011 Apr;39(7):2690-700","abstract":"In eukaryotic cells, Mtf1 and its homologues function as mitochondrial transcription factors for the mitochondrial RNA polymerase in the mitochondrion. Here we show that in fission yeast Mtf1 exerts a non-mitochondrial function as a nuclear factor that regulates transcription of srk1, which is a kinase involved in the stress response and cell cycle progression. We first found Mtf1 expression in the nucleus. A ChIP-chip approach identified srk1 as a putative Mtf1 target gene. Over expression of Mtf1 induced transcription of the srk1 gene and Mtf1 deletion led to a reduction in transcription of the srk1 gene in vivo. Mtf1 overexpression causes cell elongation in a srk1 dependent manner. Mtf1 overexpression can cause cytoplasmic accumulation of Cdc25. We also provide biochemical evidence that Mtf1 binds to the upstream sequence of srk1. This is the first evidence that a mitochondrial transcription factor Mtf1 can regulate a nuclear gene. Mtf1 may also have a role in cell cycle progression.","doi":"10.1093/nar/gkq1179","authors":"Sun W, Wang Z, Jiang H, Zhang J, Bähler J, Chen D, Murchie AI","authors_abbrev":"Sun W et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2010-12-09","publication_year":"2011","canto_session_key":"2b8416d0ae06ec6f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-11-07 16:08:22","canto_approved_date":"2022-01-28 14:53:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-20 12:16:23","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1002.08c","SPAC24H6.05","SPCC1322.08","SPAC26H5.12"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2017-11-07"},{"uniquename":"PMID:37905308","title":"Insights into the identification and evolutionary conservation of key genes in the transcriptional circuits of meiosis initiation and commitment in budding yeast.","citation":"FEBS Open Bio 2023 Dec;13(12):2290-2305","abstract":"Initiation of meiosis in budding yeast does not commit the cells for meiosis. Thus, two distinct signaling cascades may differentially regulate meiosis initiation and commitment in budding yeast. To distinguish between the role of these signaling cascades, we reconstructed protein-protein interaction networks and gene regulatory networks with upregulated genes in meiosis initiation and commitment. Analyzing the integrated networks, we identified four master regulators (MRs) [Ume6p, Msn2p, Met31p, Ino2p], three transcription factors (TFs), and 279 target genes (TGs) unique for meiosis initiation, and three MRs [Ndt80p, Aro80p, Rds2p], 11 TFs, and 948 TGs unique for meiosis commitment. Functional enrichment analysis of these distinct members from the transcriptional cascades for meiosis initiation and commitment revealed that nutritional cues rewire gene expression for initiating meiosis and chromosomal recombination commits cells to meiosis. As meiotic chromosomal recombination is highly conserved in eukaryotes, we compared the evolutionary rate of unique members in the transcriptional cascade of two meiotic phases of Saccharomyces cerevisiae with members of the phylum Ascomycota, revealing that the transcriptional cascade governing chromosomal recombination during meiosis commitment has experienced greater purifying selection pressure (P value = 0.0013, 0.0382, 0.0448, 0.0369, 0.02967, 0.04937, 0.03046, 0.03357 and < 0.00001 for Ashbya gossypii, Yarrowia lipolytica, Debaryomyces hansenii, Aspergillus fumigatus, Neurospora crassa, Kluyveromyces lactis, Schizosaccharomyces pombe, Schizosaccharomyces cryophilus, and Schizosaccharomyces octosporus, respectively). This study demarcates crucial players driving meiosis initiation and commitment and demonstrates their differential rate of evolution in budding yeast.","doi":"10.1002/2211-5463.13728","authors":"Das D, Chaudhary AA, Ali MAM, Alawam AS, Sarkar H, Podder S","authors_abbrev":"Das D et al.","pubmed_publication_date":"Dec 2023","pubmed_entrez_date":"2023-10-31","publication_year":"2023","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2023-11-01 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27183912","title":"Translin and Trax differentially regulate telomere-associated transcript homeostasis.","citation":"Oncotarget 2016 Jun 07;7(23):33809-20","abstract":"Translin and Trax proteins are highly conserved nucleic acid binding proteins that have been implicated in RNA regulation in a range of biological processes including tRNA processing, RNA interference, microRNA degradation during oncogenesis, spermatogenesis and neuronal regulation. Here, we explore the function of this paralogue pair of proteins in the fission yeast. Using transcript analysis we demonstrate a reciprocal mechanism for control of telomere-associated transcripts. Mutation of tfx1+ (Trax) elevates transcript levels from silenced sub-telomeric regions of the genome, but not other silenced regions, such as the peri-centromeric heterochromatin. In the case of some sub-telomeric transcripts, but not all, this elevation is dependent on the Trax paralogue, Tsn1 (Translin). In a reciprocal fashion, Tsn1 (Translin) serves to repress levels of transcripts (TERRAs) from the telomeric repeats, whereas Tfx1 serves to maintain these elevated levels. This reveals a novel mechanism for the regulation of telomeric transcripts. We extend this to demonstrate that human Translin and Trax also control telomere-associated transcript levels in human cells in a telomere-specific fashion.","doi":"10.18632/oncotarget.9278","authors":"Gomez-Escobar N, Almobadel N, Alzahrani O, Feichtinger J, Planells-Palop V, Alshehri Z, Thallinger GG, Wakeman JA, McFarlane RJ","authors_abbrev":"Gomez-Escobar N et al.","pubmed_publication_date":"07 Jun 2016","pubmed_entrez_date":"2016-05-18","publication_year":"2016","canto_session_key":"5c38a2b4c0c5cd0e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-08-25 10:28:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-08-09 10:02:29","canto_added_date":"2016-05-19 00:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC212.11","SPBCPT2R1.08c","SPCC736.11","SPCC736.09c","SPAC16A10.07c","SPAC30.03c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2016-08-09"},{"uniquename":"PMID:13710048","title":"Distribution of x-ray- and nitrous acid-induced mutations in the genetic fine structure of the ad7 locus of Schizosaccharomyces pombe.","citation":"Nature 1961 Sep 09;191:1125-6","abstract":"","authors":"GUTZ H","authors_abbrev":"GUTZ H","pubmed_publication_date":"09 Sep 1961","pubmed_entrez_date":"1961-09-09","publication_year":"1961","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14723709","title":"Pmr1, a P-type ATPase, and Pdt1, an Nramp homologue, cooperatively regulate cell morphogenesis in fission yeast: the importance of Mn2+ homeostasis.","citation":"Genes Cells 2004 Jan;9(1):71-82","abstract":"Schizosaccharomyces pombe pmr1+ gene is homologous to Saccharomyces cerevisiae PMR1 gene, which encodes the P-type Ca2+/Mn2+-ATPase. Addition of Mn2+, as well as Ca2+, to the medium induced pmr1+ gene expression in a calcineurin-dependent manner. The pmr1 knockout (Deltapmr1) cells exhibited hypersensitivity to EGTA. A screen for high gene dosage-suppressors of the EGTA-hypersensitive phenotype of Deltapmr1 led to the identification of pdt1+ gene, which encodes an Nramp-related metal transporter. The Deltapmr1 cells showed round cell morphology. Although Deltapdt1 cells appeared normal in the regular medium, it showed round cell morphology similar to that of the Deltapmr1 cells when Mn2+ was removed from the medium. The removal of Mn2+ also exacerbated the round morphology of the Deltapmr1 cells. The Deltapmr1Deltapdt1 double mutants grew very slowly and showed extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppressed the morphological defects, while both Mn2+ and Ca2+ markedly improved the slow growth of the double mutants. These results suggest that Pmr1 and Pdt1 cooperatively regulate cell morphogenesis through the control of Mn2+ homeostasis, and that calcineurin functions as a Mn2+ sensor as well as a Mn2+ homeostasis regulator.","authors":"Maeda T, Sugiura R, Kita A, Saito M, Deng L, He Y, Yabin L, Fujita Y, Takegawa K, Shuntoh H, Kuno T","authors_abbrev":"Maeda T et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2004-01-16","publication_year":"2004","canto_session_key":"17cfc08007a52526","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-01-22 19:34:01","canto_approved_date":"2020-01-22 19:34:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2020-01-22 19:33:35","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31E1.02c","SPBP4H10.04","SPAPB2B4.04c","SPAC4G8.13c","SPAC27F1.08","SPAC19G12.10c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2020-01-22"},{"uniquename":"PMID:3042386","title":"A gene which encodes a predicted protein kinase can restore some functions of the ras gene in fission yeast.","citation":"EMBO J 1988 Apr;7(4):985-93","abstract":"The ras1- mutation of the fission yeast Schizosaccharomyces pombe interferes with sexual differentiation by preventing conjugation and causing inefficient sporulation. From a gene library, we have isolated a gene, byr1+, which when in high copy number restores efficient sporulation to ras1- strains. byr1+ encodes a putative 340-amino acid protein product, the sequence of which strongly suggests that it functions as a protein kinase. Gene disruption experiments show that loss of byr1+ function does not interfere with mitotic growth but it completely prevents both conjugation and sporulation. byr1 is thus another important gene in the sexual differentiation pathway and we believe that at least part of ras1 function is to act directly or indirectly through byr1 to modulate protein phosphorylation.","authors":"Nadin-Davis SA, Nasim A","authors_abbrev":"Nadin-Davis SA et al.","pubmed_publication_date":"Apr 1988","pubmed_entrez_date":"1988-04-01","publication_year":"1988","canto_session_key":"a64b97197e845b5b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-18 15:39:24","canto_approved_date":"2023-09-13 05:55:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-25 15:55:37","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPAC1D4.13"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-04-18"},{"uniquename":"PMID:8660701","title":"A single mouse glutathione synthetase gene encodes six mRNAs with different 5' ends.","citation":"Arch Biochem Biophys 1996 Jul 15;331(2):215-24","abstract":"To understand more about the role of glutathione (GSH) in metabolism, we have cloned both cDNA and genomic sequences for mouse glutathione synthetase (GSH syn), the enzyme that catalyzes the last step in the synthesis of glutathione. The mouse cDNA contains an open reading frame (ORF) of 474 aa and shares 64 and 95% deduced amino acid sequence identity with Xenopus cDNA and rat cDNA, respectively. The cDNA complements Schizosaccaromyces pombe strains deficient in GSH syn. The gene is a single-copy gene spanning approximately 30 kb and is composed of at least 15 exons. Steady-state RNA levels and enzyme activity levels are highest in kidney, about 3-fold lower in liver, and 8- to 10-fold lower in lung and brain. We have identified six different GSH syn RNAs: three, termed types A1, A2, and A3, have different 5' ends that localize to different sites in the gene, but appear to encode the same protein (474 aa). Types B, C1, and C2 all have unique 5' ends and type-specific ORFs, which are shorter than that for types A1, A2, and A3. In liver only type A1 GSH syn RNA is detectable, while in kidney 90% of GSH syn RNA is type A1 and types B and C account for about 10%.","authors":"Shi ZZ, Carter BZ, Habib GM, He X, Sazer S, Lebovitz RM, Lieberman MW","authors_abbrev":"Shi ZZ et al.","pubmed_publication_date":"15 Jul 1996","pubmed_entrez_date":"1996-07-15","publication_year":"1996","canto_session_key":"6d5463d84b0ca1f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:51:53","canto_session_submitted_date":"2012-03-03 15:51:31","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3F10.04"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:14648198","title":"DSC1-MCB regulation of meiotic transcription in Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2004 Feb;271(1):60-71","abstract":"Meiosis is initiated from the G1 phase of the mitotic cell cycle, and consists of pre-meiotic S-phase followed by two successive nuclear divisions. Here we show that control of gene expression during pre-meiotic S-phase in the fission yeast Schizosaccharomyces pombe is mediated by a DNA synthesis control-like transcription factor complex (DSC1), which acts upon M lu1 cell cycle box (MCB) promoter motifs. Several genes, including rec8+, rec11+, cdc18+, and cdc22+, which contain MCB motifs in their promoter regions, are found to be co-ordinately regulated during pre-meiotic S-phase. Both synthetic and native MCB motifs are shown to confer meiotic-specific transcription on a heterologous reporter gene. A DSC1-like transcription factor complex that binds to MCB motifs was also identified in meiotic cells. The effect of mutating and over-expressing individual components of DSC1 (cdc10+, res1+, res2+, rep1+ and rep2+) on the transcription of cdc22+, rec8+ and rec11+ during meiosis was examined. We found that cdc10+, res2+, rep1+ and rep2+ are required for correct meiotic transcription, while res1+ is not required for this process. This work demonstrates a role for MCB motifs and a DSC1-like transcription factor complex in controlling transcription during meiosis in fission yeast, and suggests a mechanism for how this specific expression occurs.","authors":"Cunliffe L, White S, McInerny CJ","authors_abbrev":"Cunliffe L et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2003-12-03","publication_year":"2004","canto_session_key":"83f34adf3500526f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-08-07 14:59:30","canto_approved_date":"2024-06-26 10:36:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-07 14:59:14","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":55,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPAC144.13c","SPBC2D10.06","SPBC32F12.02","SPBC1711.14","SPBC119.04","SPAC22F3.09c","SPBC21B10.12","SPCC1442.01","SPBC14C8.07c","SPBC336.12c","SPAC25G10.04c","SPAC17A5.11","SPBC660.14","SPAPB2B4.03","SPCC4E9.01c","SPBC32H8.11","SPBC29A10.14","SPBC2F12.11c","SPBC428.18","SPCC1753.03c","SPBC25D12.04","SPBC725.16"],"gene_count":23,"ltp_gene_count":5,"approved_date":"2019-08-07"},{"uniquename":"PMID:35157728","title":"TOR complex 2 contributes to regulation of gene expression via inhibiting Gcn5 recruitment to subtelomeric and DNA replication stress genes.","citation":"PLoS Genet 2022 Feb;18(2):e1010061","abstract":"The fission yeast TOR complex 2 (TORC2) is required for gene silencing at subtelomeric regions and for the induction of gene transcription in response to DNA replication stress. Thus, TORC2 affects transcription regulation both negatively and positively. Whether these two TORC2-dependent functions share a common molecular mechanism is currently unknown. Here, we show that Gad8 physically interacts with proteins that regulate transcription, including subunits of the Spt-Ada-Gcn5-acetyltransferase (SAGA) complex and the BET bromodomain protein Bdf2. We demonstrate that in the absence of TORC2, Gcn5, the histone acetyltransferase subunit of SAGA, accumulates at subtelomeric genes and at non-induced promoters of DNA replication genes. Remarkably, the loss of Gcn5 in TORC2 mutant cells restores gene silencing as well as transcriptional induction in response to DNA replication stress. Loss of Bdf2 alleviates excess of Gcn5 binding in TORC2 mutant cells and also rescues the aberrant regulation of transcription in these cells. Furthermore, the loss of either SAGA or Bdf2 suppresses the sensitivity of TORC2 mutant cells to a variety of stresses, including DNA replication, DNA damage, temperature and nutrient stresses. We suggest a role of TORC2 in transcriptional regulation that is critical for gene silencing and gene induction in response to stress and involves the binding of Gcn5 to the chromatin.","doi":"10.1371/journal.pgen.1010061","authors":"Cohen A, Pataki E, Kupiec M, Weisman R","authors_abbrev":"Cohen A et al.","pubmed_publication_date":"Feb 2022","pubmed_entrez_date":"2022-02-14","publication_year":"2022","canto_session_key":"258f4a60a582c915","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronit Weisman","canto_first_approved_date":"2022-03-10 17:18:18","canto_approved_date":"2023-10-13 08:21:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-01 13:46:06","canto_added_date":"2022-02-16 01:15:04","annotation_curators":[{"name":"Ronit Weisman","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1450.02","SPBC609.05","SPAC637.12c","SPBP8B7.19","SPBC14C8.07c","SPCC61.02","SPAC17G8.13c","SPAC1952.05","SPBC13E7.08c","SPAC631.02","SPCC5E4.03c","SPAC1F7.05","SPAC2F7.04","SPAC186.05c","SPCC24B10.07","SPBC25H2.11c","SPAC664.03","SPAC186.06","SPAC13A11.04c","SPAC29B12.02c","SPBC30D10.10c","SPAC3A12.05c","SPAC186.04c"],"gene_count":23,"ltp_gene_count":18,"approved_date":"2022-03-10"},{"uniquename":"PMID:17072883","title":"Gene Ontology annotation status of the fission yeast genome: preliminary coverage approaches 100%.","citation":"Yeast 2006 Oct 15;23(13):913-9","abstract":"In this review, we present an overview of the Gene Ontology (GO) structure and describe how the GO is implemented for Sz. pombe and made available via Sz. pombe GeneDB (http://www.genedb.org/genedb/pombe/). We give a detailed progress report of Sz. pombe GO annotation, providing the current status of both manual and automatic annotations. Fission yeast has at least one GO annotation for 98.3% of its genes (excluding annotations to 'unknown' terms), greater than the current percentage coverage for any other organism. Approximately 65% (3225 gene products) have at least one annotation to each of the three ontologies (biological process, cellular component and molecular function). Approximately 30% (1443 gene products) have GO terms derived directly from small-scale experiments in fission yeast, supporting the validity of fission yeast as a model eukaryote and a reference organism.","authors":"Aslett M, Wood V","authors_abbrev":"Aslett M et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31235592","title":"Systematic mapping of cell wall mechanics in the regulation of cell morphogenesis.","citation":"Proc Natl Acad Sci U S A 2019 Jul 09;116(28):13833-13838","abstract":"Walled cells of plants, fungi, and bacteria come with a large range of shapes and sizes, which are ultimately dictated by the mechanics of their cell wall. This stiff and thin polymeric layer encases the plasma membrane and protects the cells mechanically by opposing large turgor pressure derived mechanical stresses. To date, however, we still lack a quantitative understanding for how local and/or global mechanical properties of the wall support cell morphogenesis. Here, we combine subresolution imaging and laser-mediated wall relaxation to quantitate subcellular values of wall thickness (h) and bulk elastic moduli (Y) in large populations of live mutant cells and in conditions affecting cell diameter in the rod-shaped model fission yeast. We find that lateral wall stiffness, defined by the surface modulus, σ = hY, robustly scales with cell diameter. This scaling is valid across tens of mutants spanning various functions-within the population of individual isogenic strains, along single misshaped cells, and even across the fission yeasts clade. Dynamic modulations of cell diameter by chemical and/or mechanical means suggest that the cell wall can rapidly adapt its surface mechanics, rendering stretched wall portions stiffer than unstretched ones. Size-dependent wall stiffening constrains diameter definition and limits size variations; it may also provide an efficient means to keep elastic strains in the wall below failure strains, potentially promoting cell survival. This quantitative set of data impacts our current understanding of the mechanics of cell walls and its contribution to morphogenesis.","doi":"10.1073/pnas.1820455116","authors":"Davì V, Chevalier L, Guo H, Tanimoto H, Barrett K, Couturier E, Boudaoud A, Minc N","authors_abbrev":"Davì V et al.","pubmed_publication_date":"09 Jul 2019","pubmed_entrez_date":"2019-06-26","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-06-28 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21454125","title":"Acetate-glycerol cometabolism: cultivating Schizosaccharomyces pombe on a non-fermentable carbon source in a defined minimal medium.","citation":"J Biosci Bioeng 2011 Jul;112(1):20-5","abstract":"The growth of the fission yeast Schizosaccharomyces pombe on glucose and glycerol was monitored on-line in shake flasks and microtiter plates. The Edinburgh Minimal Medium 2 was improved by doubling its concentrations, improving its buffer and increasing its sulphur and iron concentrations additionally. By growing S. pombe on mixed carbon sources, it was shown that glycerol and glucose complement one another. Several tests were performed to establish the cultivation of S. pombe with non-fermentable glycerol as the main carbon source in minimal medium. Interestingly, a synergistic effect of glycerol and acetate was discovered which can significantly improve the growth of the fission yeast on glycerol. S. pombe showed optimal respiration activity, growth, and product formation by co-utilizing 20g/L glycerol and 2.5g/L sodium acetate.","doi":"10.1016/j.jbiosc.2011.02.014","authors":"Klement T, Dankmeyer L, Hommes R, van Solingen P, Büchs J","authors_abbrev":"Klement T et al.","pubmed_publication_date":"Jul 2011","pubmed_entrez_date":"2011-04-02","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20970342","title":"Virtual breakdown of the nuclear envelope in fission yeast meiosis.","citation":"Curr Biol 2010 Nov 09;20(21):1919-25","abstract":"Asymmetric localization of Ran regulators (RanGAP1 and RanGEF/RCC1) produces a gradient of RanGTP across the nuclear envelope. In higher eukaryotes, the nuclear envelope breaks down as the cell enters mitosis (designated \"open\" mitosis). This nuclear envelope breakdown (NEBD) leads to collapse of the RanGTP gradient and the diffusion of nuclear and cytoplasmic macromolecules in the cell, resulting in irreversible progression of the cell cycle. On the other hand, in many fungi, chromosome segregation takes place without NEBD (designated \"closed\" mitosis). Here we report that in the fission yeast Schizosaccharomyces pombe, despite the nuclear envelope and the nuclear pore complex remaining intact throughout both the meiotic and mitotic cell cycles, nuclear proteins diffuse into the cytoplasm transiently for a few minutes at the onset of anaphase of meiosis II. We also found that nuclear protein diffusion into the cytoplasm occurred coincidently with nuclear localization of Rna1, an S. pombe RanGAP1 homolog that is usually localized in the cytoplasm. These results suggest that nuclear localization of RanGAP1 and depression of RanGTP activity in the nucleus may be mechanistically tied to meiosis-specific diffusion of nuclear proteins into the cytoplasm. This nucleocytoplasmic shuffling of RanGAP1 and nuclear proteins represents virtual breakdown of the nuclear envelope.","doi":"10.1016/j.cub.2010.09.070","authors":"Asakawa H, Kojidani T, Mori C, Osakada H, Sato M, Ding DQ, Hiraoka Y, Haraguchi T","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"09 Nov 2010","pubmed_entrez_date":"2010-10-26","publication_year":"2010","canto_session_key":"011e491e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 17:21:30","canto_approved_date":"2025-03-28 11:16:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-25 22:06:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":86,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.05c","SPAC1002.02","SPCC18B5.07c","SPAC1786.03","SPBC21C3.18","SPAC30D11.04c","SPAC22E12.07","SPCC285.13c","SPBP35G2.06c","SPAC26A3.15c","SPBC13A2.02","SPAC15F9.02","SPBC31E1.05","SPAC4F10.18","SPBC19G7.15","SPCC290.03c","SPBC29A10.07","SPBC3B9.16c","SPAP27G11.10c","SPBC1703.14c","SPAC644.12","SPAC1486.05","SPBC11B10.09","SPBC17G9.04c","SPAC22G7.09c","SPCC1620.11","SPCC162.08c","SPBC29A10.02","SPBC428.01c","SPCC962.06c","SPBC557.03c","SPCC1739.14","SPAC23D3.06c","SPBC29A10.06c","SPBC646.04","SPAC1805.04","SPAC19E9.01c","SPAC890.06","SPAC16E8.01"],"gene_count":39,"ltp_gene_count":36,"approved_date":"2019-01-30"},{"uniquename":"PMID:11790314","title":"Cell polarity: following formin function.","citation":"Curr Biol 2002 Jan 08;12(1):R6-8","abstract":"Mutation of a novel fission yeast formin, for3p, leads to marked changes in both the actin and microtubule cytoskeleton, as well as a surprising asymmetric pattern of cell growth. At the same time, new work in budding yeast implicates formins directly in actin filament assembly.","authors":"Sawin KE","authors_abbrev":"Sawin KE","pubmed_publication_date":"08 Jan 2002","pubmed_entrez_date":"2002-01-16","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8921873","title":"Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase.","citation":"Gene 1996 Oct 24;177(1-2):237-41","abstract":"Synthesis of the ceramide portion of sphingolipids in animals has been hypothesized to be tightly regulated thereby controlling the rate of de novo sphingolipid formation. Regulation is predicted to occur at the first and committed biosynthetic step catalyzed by serine palmitoyltransferase (SPT, EC 2.3.1.50). This hypothesis remains unproven because SPT has been refractory to purification and subsequent characterization. To begin to test this hypothesis we have used a genetic strategy to isolate LCB2 homologs from the yeasts Kluyveromyces lactis and Schizosaccharomyces pombe and a cDNA homolog from humans and mice. Identity is supported by overall amino acid sequence similarity between the predicted proteins and the known Saccharomyces cerevisiae Lcb2 protein. In addition, a motif of 56 residues from the human protein functionally substituted for the corresponding region of the S. cerevisiae Lcb2 protein. The 56 residue motif was found to be unique to Lcb2 proteins. Likewise, the base sequence encoding it is unique to the human genome. Finally, a peptide sequence in the motif is known to be part of the catalytic domain of all members of the aminolevulinate synthase superfamily of proteins of which Lcb2 is a member. These data argue that this motif is part of the catalytic domain of SPT and is a signature of Lcb2 proteins. The mammalian LCB2 cDNAs provide valuable reagents for studying the Lcb2 subunit of SPT and for studying how ceramide synthesis is regulated.","authors":"Nagiec MM, Lester RL, Dickson RC","authors_abbrev":"Nagiec MM et al.","pubmed_publication_date":"24 Oct 1996","pubmed_entrez_date":"1996-10-24","publication_year":"1996","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24098959","title":"Cell-cycle regulated transcription associates with DNA replication timing in yeast and human.","citation":"Genome Biol 2013;14(10):R111","abstract":"Eukaryotic DNA replication follows a specific temporal program, with some genomic regions consistently replicating earlier than others, yet what determines this program is largely unknown. Highly transcribed regions have been observed to replicate in early S-phase in all plant and animal species studied to date, but this relationship is thought to be absent from both budding yeast and fission yeast. No association between cell-cycle regulated transcription and replication timing has been reported for any species.\nHere I show that in budding yeast, fission yeast, and human, the genes most highly transcribed during S-phase replicate early, whereas those repressed in S-phase replicate late. Transcription during other cell-cycle phases shows either the opposite correlation with replication timing, or no relation. The relationship is strongest near late-firing origins of replication, which is not consistent with a previously proposed model—that replication timing may affect transcription—and instead suggests a potential mechanism involving the recruitment of limiting replication initiation factors during S-phase.\nThese results suggest that S-phase transcription may be an important determinant of DNA replication timing across eukaryotes, which may explain the well-established association between transcription and replication timing.","authors":"Fraser HB","authors_abbrev":"Fraser HB","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-10-09","publication_year":"2013","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2013-11-01 02:19:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11895483","title":"Phosphatidylinositol 3-phosphate 5-kinase is required for the cellular response to nutritional starvation and mating pheromone signals in Schizosaccharomyces pombe.","citation":"Genes Cells 2002 Feb;7(2):199-215","abstract":"Phosphatidylinositol (3,5) bisphosphate, which is converted from phosphatidylinositol 3-phosphate by phosphatidylinositol 3-phosphate 5-kinase, is implicated in vacuolar functions and the sorting of cell surface proteins within endosomes in the endocytic pathway of budding yeast. A homologous protein, SpFab1p, has been found in the fission yeast Schizosaccharomyces pombe, but its role is not known.\nHere we report that SpFab1p is encoded by ste12+ known as a fertility gene in S. pombe. The ste12 mutant grew normally under stress-free conditions, but was highly vacuolated and swelled at high temperatures and under starvation conditions. In nitrogen-free medium, ste12 cells were arrested in G1 phase, but partially defective in the expression of genes responsible for mating and meiosis. The ste12 mutant was defective both in the production of, and in the response to, mating pheromones. The amount of the pheromone receptor protein Map3p, was substantially decreased in ste12 cells. Map3p was transported to the cell surface, then internalized and eventually transported to the vacuolar lumen, even in the ste12 mutant.\nThe results indicate that phosphatidylinositol(3,5)bisphosphate is essential for cellular responses to various stresses and for the mating pheromone signalling under starvation conditions.","authors":"Morishita M, Morimoto F, Kitamura K, Koga T, Fukui Y, Maekawa H, Yamashita I, Shimoda C","authors_abbrev":"Morishita M et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-03-16","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3E7.01"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:29906447","title":"Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human Nuclear RNA Exosome-MTR4 Complex.","citation":"Cell 2018 Jun 14;173(7):1663-1677.e21","abstract":"The ribonucleolytic RNA exosome interacts with RNA helicases to degrade RNA. To understand how the 3' to 5' Mtr4 helicase engages RNA and the nuclear exosome, we reconstituted 14-subunit Mtr4-containing RNA exosomes from Saccharomyces cerevisiae, Schizosaccharomyces pombe, and human and show that they unwind structured substrates to promote degradation. We loaded a human exosome with an optimized DNA-RNA chimera that stalls MTR4 during unwinding and determined its structure to an overall resolution of 3.45 Å by cryoelectron microscopy (cryo-EM). The structure reveals an RNA-engaged helicase atop the non-catalytic core, with RNA captured within the central channel and DIS3 exoribonuclease active site. MPP6 tethers MTR4 to the exosome through contacts to the RecA domains of MTR4. EXOSC10 remains bound to the core, but its catalytic module and cofactor C1D are displaced by RNA-engaged MTR4. Competition for the exosome core may ensure that RNA is committed to degradation by DIS3 when engaged by MTR4.","doi":"10.1016/j.cell.2018.05.041","authors":"Weick EM, Puno MR, Januszyk K, Zinder JC, DiMattia MA, Lima CD","authors_abbrev":"Weick EM et al.","pubmed_publication_date":"14 Jun 2018","pubmed_entrez_date":"2018-06-16","publication_year":"2018","canto_session_key":"7c75b3c731da0362","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-01 22:44:03","canto_approved_date":"2019-01-01 22:44:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-01 22:43:53","canto_added_date":"2018-06-17 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17D1.03c","SPBC26H8.10","SPAC1006.03c","SPAC22A12.12c","SPBC16G5.10","SPAC3G9.10c","SPAC6F12.16c","SPCC757.08","SPAP8A3.05","SPACUNK4.11c","SPAC1F3.01","SPBC115.01c","SPCC1739.07","SPBC211.08c","SPCC1840.11","SPAC2F7.14c"],"gene_count":16,"ltp_gene_count":13,"approved_date":"2019-01-01"},{"uniquename":"PMID:15173185","title":"Five genes involved in biosynthesis of the pyruvylated Galbeta1,3-epitope in Schizosaccharomyces pombe N-linked glycans.","citation":"J Biol Chem 2004 Aug 20;279(34):35644-55","abstract":"The N-linked galactomannans of Schizosaccharomyces pombe have pyruvylated Galbeta1,3-(PvGal) caps on a portion of the Galalpha1,2-residues in their outer chains (Gemmill, T. R., and Trimble, R. B. (1998) Glycobiology 8, 1087-1095). PvGal biosynthesis was investigated by ethyl methanesulfonate mutagenesis of S. pombe, followed by the isolation of cells devoid of negatively charged N-glycans by Q-Sepharose exclusion and failure to bind human serum amyloid P component, which acts as a lectin for terminal PvGal residues. Mutant glycans were characterized by lectin binding, saccharide composition, exoglycosidase sensitivity, and NMR spectroscopy. Restoration of the cell surface negative charge by complementation with an S. pombe genomic library led to the identification of five genes involved in PvGal biosynthesis, which we designated pvg1-pvg5. Pvg1p may be a pyruvyltransferase, since NMR of pvg1(-) mutant N-glycans revealed the absence of only the pyruvyl moiety. Pvg2p-Pvg5p are crucial for attachment of the Galbeta1,3-residue that becomes pyruvylated. Pvg3p is predicted to be a member of the beta1,3-galactosyltransferase family, and Pvg3p-green fluorescent protein labeling was consistent with Golgi localization. Predicted Pvg1p and Pvg3p functions imply that Galbeta1,3-is added to the galactomannans and is then pyruvylated in situ, rather than by an en bloc addition of PvGalbeta1,3-caps to the outer chain. Pvg4p-green fluorescent protein targeted to the nucleus, and its sequence contains a MADS-box DNA-binding and dimerization domain; however, it does not appear to solely control transcription of the other identified genes. Pvg2p and/or Pvg5p may contribute to an enzyme complex. Whereas a functional role for the PvGal epitope in S. pombe remains unclear, it is nonessential for either cell growth or mating under laboratory conditions.","authors":"Andreishcheva EN, Kunkel JP, Gemmill TR, Trimble RB","authors_abbrev":"Andreishcheva EN et al.","pubmed_publication_date":"20 Aug 2004","pubmed_entrez_date":"2004-06-03","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27E2.07","SPAC8F11.10c","SPBC1921.06c","SPAC22F8.02c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:19194512","title":"A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast.","citation":"PLoS One 2009;4(2):e4376","abstract":"A mutated allele of the essential gene TAH18 was previously identified in our laboratory in a genetic screen for new proteins interacting with the DNA polymerase delta in yeast [1]. The present work shows that Tah18 plays a role in response to oxidative stress. After exposure to lethal doses of H(2)O(2), GFP-Tah18 relocalizes to the mitochondria and controls mitochondria integrity and cell death. Dre2, an essential Fe/S cluster protein and homologue of human anti-apoptotic Ciapin1, was identified as a molecular partner of Tah18 in the absence of stress. Moreover, Ciapin1 is able to replace yeast Dre2 in vivo and physically interacts with Tah18. Our results are in favour of an oxidative stress-induced cell death in yeast that involves mitochondria and is controlled by the newly identified Dre2-Tah18 complex.","doi":"10.1371/journal.pone.0004376","authors":"Vernis L, Facca C, Delagoutte E, Soler N, Chanet R, Guiard B, Faye G, Baldacci G","authors_abbrev":"Vernis L et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-02-06","publication_year":"2009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1296.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8910298","title":"Intrinsic fluorescence properties and structural analysis of p13(suc1) from Schizosaccharomyces pombe.","citation":"J Biol Chem 1996 Nov 01;271(44):27249-58","abstract":"p13(suc1) acts in the fission yeast cell division cycle as a component of p34(cdc2). In the present work, structural information contained in the intrinsic fluorescence of p13(suc1) has been extracted by steady-state and time-resolved fluorescence techniques. In its native form, the steady-state emission spectrum of p13(suc1) is centered at 336 nm. Upon denaturation by guanidine HCl (4.0 M), the emission spectrum is shifted to 355-360 nm and the fluorescence intensity decreases 70%. The same changes are not obtained with p13(suc1) at 56 degrees C or after incubation at 100 degrees C, and the protein appears to be substantially temperature-stable. The fluorescence decay of p13(suc1) is best described by three discrete lifetimes of 0.6 ns (tau1), 2.9 ns (tau2), and 6.1 ns (tau3), with amplitudes that are dependent on the native or unfolded state of the protein. Under native conditions, the two predominant decay-associated spectra, DAS-tau2 (lambdamax = 332 nm) and DAS-tau3 (lambdamax = 340 nm), derive from two different excitation DAS. Moreover distinct quenching mechanisms and collisional accessibilities (kq(tau2)>>kq(tau3)) are resolved for each lifetime. An interpretation in terms of specific tryptophan residue (or protein conformer)-lifetime assignments is presented. The decay of the fluorescence anisotropy of native p13(suc1) is best described by a double exponential decay. The longer correlation time recovered (9 ns </= phi2 </= 15ns) can be associated with the rotational motion of the protein as a whole and a Stokes radius of 21.2 A has been calculated for p13(suc1). Anisotropy measurements obtained as a function of temperature indicate that, in solution, the protein exists exclusively as a prolate monomer. In 1 mM zinc, changes of the anisotropy decay parameters are compatible with subunits oligomerization.","authors":"Neyroz P, Menna C, Polverini E, Masotti L","authors_abbrev":"Neyroz P et al.","pubmed_publication_date":"01 Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_session_key":"f5ac732fc1788b88","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-10-29 11:33:36","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-29 11:30:39","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1734.14c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-10-29"},{"uniquename":"PMID:9740803","title":"Mutations in fission yeast Cut15, an importin alpha homolog, lead to mitotic progression without chromosome condensation.","citation":"Curr Biol 1998 Sep 10;8(18):1031-4","abstract":"Chromosome condensation is a major mitotic event. Fission yeast mutations in topoisomerase II and condensin subunits produce the characteristic 'cut' phenotypes, in which the septum bisects the nuclear material in the absence of normal condensation and sister chromatid separation. We show here that the same condensation defect is produced in cut15 temperature-sensitive mutants at the restrictive temperature (36 degrees C). The gene product of cut15+ is, surprisingly, very similar to importin alpha, which binds proteins containing a nuclear localization signal (NLS) and forms the heterodimer with importin beta that mediates translocation through the nuclear pore complex. We show that in a nuclear import assay, purified Cut15 protein behaved identically to mammalian importin alpha but mutant Cut15 did not. Mutant Cut15 failed to bind an NLS-containing protein in vitro but could still bind importin beta. Unexpectedly, however, NLS proteins were imported into the nucleus in cut15 mutants. Cut15 is thus essential for mitotic chromosome condensation, but its role in nuclear import might be dispensable. Green fluorescent protein (GFP)-tagged Cut15 was enriched within the nucleus specifically during prometaphase-metaphase, so the interaction of Cut15 with nuclear NLS proteins during mitosis might be important for condensation.","authors":"Matsusaka T, Imamoto N, Yoneda Y, Yanagida M","authors_abbrev":"Matsusaka T et al.","pubmed_publication_date":"10 Sep 1998","pubmed_entrez_date":"1998-09-19","publication_year":"1998","canto_session_key":"4e4fa8722ccab385","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-08-29 10:17:18","canto_approved_date":"2026-05-27 16:18:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-29 10:17:10","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.03c","SPCC962.03c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-08-29"},{"uniquename":"EMBL:AB084832","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.1649"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35830853","title":"Establishment of centromere identity is dependent on nuclear spatial organization.","citation":"Curr Biol 2022 Jul 25;32(14):3121-3136.e6","abstract":"The establishment of centromere-specific CENP-A chromatin is influenced by epigenetic and genetic processes. Central domain sequences from fission yeast centromeres are preferred substrates for CENP-A Cnp1  incorporation, but their use is context dependent, requiring adjacent heterochromatin. CENP-A Cnp1  overexpression bypasses heterochromatin dependency, suggesting that heterochromatin ensures exposure to conditions or locations permissive for CENP-A Cnp1  assembly. Centromeres cluster around spindle-pole bodies (SPBs). We show that heterochromatin-bearing minichromosomes localize close to SPBs, consistent with this location promoting CENP-A Cnp1  incorporation. We demonstrate that heterochromatin-independent de novo CENP-A Cnp1  chromatin assembly occurs when central domain DNA is placed near, but not far from, endogenous centromeres or neocentromeres. Moreover, direct tethering of central domain DNA at SPBs permits CENP-A Cnp1  assembly, suggesting that the nuclear compartment surrounding SPBs is permissive for CENP-A Cnp1  incorporation because target sequences are exposed to high levels of CENP-A Cnp1  and associated assembly factors. Thus, nuclear spatial organization is a key epigenetic factor that influences centromere identity.","doi":"10.1016/j.cub.2022.06.048","authors":"Wu W, McHugh T, Kelly DA, Pidoux AL, Allshire RC","authors_abbrev":"Wu W et al.","pubmed_publication_date":"25 Jul 2022","pubmed_entrez_date":"2022-07-13","publication_year":"2022","canto_session_key":"b8fe2ce4be785d1b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-07-15 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24398522","title":"Lineage-specific expansions of TET/JBP genes and a new class of DNA transposons shape fungal genomic and epigenetic landscapes.","citation":"Proc Natl Acad Sci U S A 2014 Feb 04;111(5):1676-83","abstract":"TET/JBP dioxygenases oxidize methylpyrimidines in nucleic acids and are implicated in generation of epigenetic marks and potential intermediates for DNA demethylation. We show that TET/JBP genes are lineage-specifically expanded in all major clades of basidiomycete fungi, with the majority of copies predicted to encode catalytically active proteins. This pattern differs starkly from the situation in most other organisms that possess just a single or a few copies of the TET/JBP family. In most basidiomycetes, TET/JBP genes are frequently linked to a unique class of transposons, KDZ (Kyakuja, Dileera, and Zisupton) and appear to have dispersed across chromosomes along with them. Several of these elements typically encode additional proteins, including a divergent version of the HMG domain. Analysis of their transposases shows that they contain a previously uncharacterized version of the RNase H fold with multiple distinctive Zn-chelating motifs and a unique insert, which are predicted to play roles in structural stabilization and target sequence recognition, respectively. We reconstruct the complex evolutionary history of TET/JBPs and associated transposons as involving multiple rounds of expansion with concomitant lineage sorting and loss, along with several capture events of TET/JBP genes by different transposon clades. On a few occasions, these TET/JBP genes were also laterally transferred to certain Ascomycota, Glomeromycota, Viridiplantae, and Amoebozoa. One such is an inactive version, calnexin-independence factor 1 (Cif1), from Schizosaccharomyces pombe, which has been implicated in inducing an epigenetically transmitted prion state. We argue that this unique transposon-TET/JBP association is likely to play important roles in speciation during evolution and epigenetic regulation.","doi":"10.1073/pnas.1321818111","authors":"Iyer LM, Zhang D, de Souza RF, Pukkila PJ, Rao A, Aravind L","authors_abbrev":"Iyer LM et al.","pubmed_publication_date":"04 Feb 2014","pubmed_entrez_date":"2014-01-09","publication_year":"2014","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40879988","title":"An In Vivo Yeast-Based Activity Assay for the PPIP5K Family.","citation":"Methods Mol Biol 2025;2972:205-219","abstract":"The highly conserved eukaryotic PPIP5K family of bifunctional enzymes regulate cellular levels of 1,5-InsP8, a high-energy molecule involved in a multitude of biological processes. Members of this family contain two opposing activities: an N-terminus ATP-grasp kinase domain synthesizing 1,5-InsP8 and a C-terminus pyrophosphatase domain degrading 1,5-InsP8. While biochemical characterization of members of this family is vital, we present a complementary, simple, and very fast in vivo assay in the fission yeast Schizosaccharomyces pombe, for the functional assessment of kinase and pyrophosphatase activities of PPIP5K family members of any species.","doi":"10.1007/978-1-0716-4799-8_15","authors":"Alcázar-Román AR, Fleig U","authors_abbrev":"Alcázar-Román AR et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-08-29","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-08-29 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1672.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10835385","title":"Loss of Rhb1, a Rheb-related GTPase in fission yeast, causes growth arrest with a terminal phenotype similar to that caused by nitrogen starvation.","citation":"Genetics 2000 Jun;155(2):611-22","abstract":"The Rheb GTPase is most similar in primary sequence to the Ras, Rap, R-Ras, and Ral GTPases, which regulate cell growth and differentiation in many cell types. A likely fission yeast homologue of mammalian Rheb, which we designated Rhb1, was identified by genome sequencing. Our investigation of rhb1 showed that rhb1(-) cells arrested cell growth and division with a terminal phenotype similar to that of nitrogen-starved cells. In particular, cells depleted of Rhb1 arrested as small, round cells with 1N DNA content, arrested more quickly in low-nitrogen medium, and induced expression of fnx1 and mei2 mRNA, two mRNAs that were normally induced by nitrogen starvation. Since mammalian Rheb binds and may regulate Raf-1, a Ras effector, we tested for functional overlap between Ras1 and Rhb1 in fission yeast. This analysis showed that Ras1 overexpression did not suppress rhb1(-) mutant phenotypes, Rhb1 overexpression did not suppress ras1(-) mutant phenotypes, and ras1(-) rhb1(-) double mutants had phenotypes equal to the sum of the corresponding single-mutant phenotypes. Hence, there is no evidence for overlapping functions between Ras1 and Rhb1. On the basis of this study, we hypothesize that Rhb1 negatively regulates entry into stationary phase when extracellular nitrogen levels are adequate for growth. If this hypothesis is correct, then Rhb1 and Ras1 regulate alternative responses to limiting nutrients.","authors":"Mach KE, Furge KA, Albright CF","authors_abbrev":"Mach KE et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-06-03","publication_year":"2000","canto_session_key":"e040917969e21e31","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-01-22 14:41:43","canto_approved_date":"2022-01-03 19:38:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-22 14:41:37","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPAC17H9.09c","SPAC8C9.03","SPAC27D7.03c","SPBC12C2.13c","SPBC428.16c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2021-01-22"},{"uniquename":"PMID:14623327","title":"But1 and But2 proteins bind to Uba3, a catalytic subunit of E1 for neddylation, in fission yeast.","citation":"Biochem Biophys Res Commun 2003 Nov 21;311(3):691-5","abstract":"NEDD8/Rub1 is the most homologous protein to ubiquitin among the ubiquitin-like proteins, and it is covalently linked to target proteins via the C-terminal glycine residue in a manner analogous to ubiquitylation. However, the mechanism(s) involved in the regulation of the NEDD8 ligation pathway remains elusive. Using the two-hybrid system, we isolated novel genes from the Schizosaccharomyces pombe cDNA library whose products bind to Uba3, which is a catalytic protein for E1-like activity of the NEDD8 pathway. We designated these genes but1(+) and but2(+) (for proteins that bind to Uba three). But1 is a nuclear protein and its overexpression caused cell elongation, which is a common phenotype of the NEDD8 pathway defective mutant in S. pombe. Furthermore, overexpression of but1(+) in ned8-temperature sensitive mutant had a deleterious effect even under permissive temperatures. Our results suggest that But1 may have an inhibitory role in the NEDD8 pathway.","authors":"Yashiroda H, Tanaka K","authors_abbrev":"Yashiroda H et al.","pubmed_publication_date":"21 Nov 2003","pubmed_entrez_date":"2003-11-19","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.12c","SPAC27D7.12c","SPBC12D12.08c","SPBC3D6.02"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"EMBL:AB084819","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24107707","title":"Spt6: two fundamentally distinct functions in the regulation of histone modification.","citation":"Epigenetics 2013 Dec;8(12):1249-53","abstract":"As posttranslational modifications of histones H3 and H4 determine the state of chromatin in cis, these histones should remain attached to template DNA during transcription in order to maintain the state of chromatin. RNA polymerase II itself can transcribe the nucleosome template without changing nucleosome positioning. However, it was uncertain whether Spt6, a highly conserved polymerase-associated histone chaperone, prevents \"preexisting\" histone molecules from being dissociated from template DNA during transcription. We recently showed that Spt6 prevents transcription-coupled loss of posttranslationally modified histone H3. Taking previous studies into account, we would like to propose here that Spt6 has two fundamentally distinct functions in the regulation of histone modification: one is to act as a platform for histone modifiers and the other is to act as a molecular liaison between histone molecules and template DNA to prevent cotranscriptional dissociation of preexisting histones in order to maintain locus-specific modifications.","doi":"10.4161/epi.26487","authors":"Kato H, Okazaki K, Urano T","authors_abbrev":"Kato H et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-10-11","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1809348","title":"Cell cycle regulation in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Annu Rev Cell Biol 1991;7:227-56","abstract":"","authors":"Forsburg SL, Nurse P","authors_abbrev":"Forsburg SL et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34974803","title":"Rrp14 controls rRNA transcription via facilitating the translocation of Pol5 into the nucleolus.","citation":"Cell Cycle 2022 Mar;21(5):489-500","abstract":"Rrp14 is a conserved protein that plays an important role in rRNA processing and ribosomal biogenesis. In  Schizosaccharomyces pombe , the  rrp14  gene is split into  SPAC8C9.10 c  ( rrp14 ) and  SPBC947.07  ( rrp1402 ). Although the  SPAC8C9.10 c  gene is not essential for  S. pombe  survival, deletion of the gene causes the yeast cells to grow sick and to exhibit decreased rRNA transcription. We identified a novel Pol5 protein that physically interacts with the Rrp14 protein. Taking advantage of the Pil1 co-tethering assay, we found that Rrp14 facilitates the nucleolus translocation of Pol5, and the 7-RINAWN-12 motif of the Rrp14 protein is responsible for the interaction between Pol5 and Rrp14. Since deletion of the 7-RINAWN-12 motif affects rRNA transcription, we thus propose that Rrp14 affects rRNA transcription by facilitating the nucleolus translocation of Pol5.","doi":"10.1080/15384101.2021.2023303","authors":"Lin Z, Liu H, Chen H, Cao H, Liu X, Zhu H, Zhao L, Chen Z","authors_abbrev":"Lin Z et al.","pubmed_publication_date":"Mar 2022","pubmed_entrez_date":"2022-01-03","publication_year":"2022","canto_session_key":"ee2849e956dcece5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-01-05 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8C9.10c","SPBC14C8.14c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8590806","title":"Separation of phenotypes in mutant alleles of the Schizosaccharomyces pombe cell-cycle checkpoint gene rad1+.","citation":"Mol Biol Cell 1995 Dec;6(12):1793-805","abstract":"The Schizosaccharomyces pombe rad1+ gene is involved in the G2 DNA damage cell-cycle checkpoint and in coupling mitosis to completed DNA replication. It is also required for viability when the cdc17 (DNA ligase) or wee1 proteins are inactivated. We have introduced mutations into the coding regions of rad1+ by site-directed mutagenesis. The effects of these mutations on the DNA damage and DNA replication checkpoints have been analyzed, as well as their associated phenotypes in a cdc17-K42 or a wee1-50 background. For all alleles, the resistance to radiation or hydroxyurea correlates well with the degree of functioning of checkpoint pathways activated by these treatments. One mutation, rad1-S3, completely abolishes the DNA replication checkpoint while partially retaining the DNA damage checkpoint. As single mutants, the rad1-S1, rad1-S2, rad1-S5, and rad1-S6 alleles have a wild-type phenotype with respect to radiation sensitivity and checkpoint functions; however, like the rad1 null allele, the rad1-S1 and rad1-S2 alleles exhibit synthetic lethality at the restrictive temperature with the cdc17-K42 or the wee1-50 mutation. The rad1-S5 and rad1-S6 alleles allow growth at higher temperatures in a cdc17-K42 or wee1-50 background than does wild-type rad1+, and thus behave like \"superalleles.\" In most cases both chromosomal and multi-copy episomal mutant alleles have been investigated, and the agreement between these two states is very good. We provide evidence that the functions of rad1 can be dissociated into three groups by specific mutations. Models for the action of these rad1 alleles are discussed. In addition, a putative negative regulatory domain of rad1 is identified.","authors":"Kanter-Smoler G, Knudsen KE, Jimenez G, Sunnerhagen P, Subramani S","authors_abbrev":"Kanter-Smoler G et al.","pubmed_publication_date":"Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC1952.07","SPAC20G8.01"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:39527210","title":"Genome-Wide Profiling of Histone Modifications in Fission Yeast Using CUT&Tag.","citation":"Methods Mol Biol 2025;2862:309-320","abstract":"Eukaryotic DNA is organized in the nucleus in the form of chromatin. Nucleosomes, the fundamental unit of chromatin, are subject to many posttranslational modifications (PTMs) as well as compositional variations through incorporation of histone variants. These alterations play important roles in regulation of genome structure and activity. Genome-wide profiling of these regulatory features is essential for understanding of genome function. Chromatin immunoprecipitation coupled with next-generation sequencing (ChIP-Seq) is a widely used method to assay genome-wide localization in fission yeast but suffers from the requirement for a large amount of input chromatin, antibodies, and a cumbersome experimental pipeline. New methods such as Cleavage Under Targets and Tagmentation (CUT&Tag), which combine the specificity of targeted cleavage and adapter insertion with the sensitivity of next-generation sequencing, enable identification and characterization of various epigenetic marks affording low input requirement as well as more streamlined protocols. However, these approaches have not been adapted for use in fission yeast, Schizosaccharomyces pombe. Here, we describe an adapted CUT&Tag protocol for epigenomic profiling in fission yeast using the heterochromatin-associated histone H3K9 methylation PTM for benchmarking.","doi":"10.1007/978-1-0716-4168-2_22","authors":"Torres-Garcia S, Huang Y, Dewornu FS, Tong P, Yeboah R, Allshire R, Shukla M","authors_abbrev":"Torres-Garcia S et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPO250428","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12808043","title":"The fission yeast meiotic regulator Mei2p forms a dot structure in the horse-tail nucleus in association with the sme2 locus on chromosome II.","citation":"Mol Biol Cell 2003 Jun;14(6):2461-9","abstract":"Fission yeast Mei2p is an RNA-binding protein essential for induction of both premeiotic DNA synthesis and first meiotic division. Mei2p forms a dot structure at an apparently fixed position in the horse-tail nucleus during meiotic prophase. This dot formation requires a meiosis-specific RNA species, meiRNA, which is indispensable for meiosis I, and the emergence of the dot is an indicator of the ability of the cell to perform meiosis I. Herein, we have sought the identity of this dot. Analyses using chromosome segregation in haploid meiosis, reciprocal translocation of chromosomes, and gene translocation have led us to conclude that the Mei2p dot is in association with the sme2 gene on the short arm of chromosome II, which encodes meiRNA. Transcripts of sme2, rather than the DNA sequence of the gene, seem to be the determinant of the localization of the Mei2p dot. However, evidence suggests that the dot may not be a simple reflection of the attachment of Mei2p to meiRNA undergoing transcription. We speculate that the Mei2p dot is a specialized structure, either to foster the assembly of Mei2p and meiRNA or to perform some unidentified function indispensable for meiosis I.","authors":"Shimada T, Yamashita A, Yamamoto M","authors_abbrev":"Shimada T et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-06-17","publication_year":"2003","canto_session_key":"a882e140c77212d8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-01-30 15:37:56","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-01-23 14:35:22","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-01-23"},{"uniquename":"PMID:12177320","title":"Morphogenetic checkpoint in fission yeast? No!","citation":"Microbiology (Reading) 2002 Aug;148(Pt 8):2271-2272","abstract":"","doi":"10.1099/00221287-148-8-2271","authors":"Rupeš I, Young PG","authors_abbrev":"Rupeš I et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-08-15","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29162650","title":"Steric hindrance in the upper 50 kDa domain of the motor Myo2p leads to cytokinesis defects in fission yeast.","citation":"J Cell Sci 2018 Jan 04;131(1)","abstract":"Cytokinesis in many eukaryotes requires a contractile actomyosin ring that is placed at the division site. In fission yeast, which is an attractive organism for the study of cytokinesis, actomyosin ring assembly and contraction requires the myosin II heavy chain Myo2p. Although  myo2 -E1, a temperature-sensitive mutant defective in the upper 50 kDa domain of Myo2p, has been studied extensively, the molecular basis of the cytokinesis defect is not understood. Here, we isolate  myo2 -E1-Sup2, an intragenic suppressor that contains the original mutation in  myo2 -E1 (G345R) and a second mutation in the upper 50 kDa domain (Y297C). Unlike  myo2 -E1-Sup1, a previously characterized  myo2 -E1 suppressor,  myo2 -E1-Sup2 reverses actomyosin ring contraction defects  in vitro  and  in vivo  Structural analysis of available myosin motor domain conformations suggests that a steric clash in  myo2 -E1, which is caused by the replacement of a glycine with a bulky arginine, is relieved in  myo2 -E1-Sup2 by mutation of a tyrosine to a smaller cysteine. Our work provides insight into the function of the upper 50 kDa domain of Myo2p, informs a molecular basis for the cytokinesis defect in  myo2 -E1, and may be relevant to the understanding of certain cardiomyopathies.","doi":"10.1242/jcs.205625","authors":"Palani S, Srinivasan R, Zambon P, Kamnev A, Gayathri P, Balasubramanian MK","authors_abbrev":"Palani S et al.","pubmed_publication_date":"04 Jan 2018","pubmed_entrez_date":"2017-11-23","publication_year":"2018","canto_session_key":"311b0d304d277383","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-11-24 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4A8.05c","SPCC645.05c","SPAC1782.09c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:30458148","title":"Sexual Reproduction: Preventing Re-fertilization in Fission Yeast.","citation":"Curr Biol 2018 Nov 19;28(22):R1300-R1303","abstract":"During sexual reproduction, two haploid cells fuse to produce a diploid cell called a zygote. A new study describes how fission yeast prevents a zygote from being formed by the fusion of more than two cells.","doi":"10.1016/j.cub.2018.09.048","authors":"Huraiova B, Pozgajova M, Gregan J","authors_abbrev":"Huraiova B et al.","pubmed_publication_date":"19 Nov 2018","pubmed_entrez_date":"2018-11-21","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-22 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19818717","title":"The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries.","citation":"Mol Cell 2009 Oct 09;36(1):141-52","abstract":"eIF3 promotes translation initiation, but relatively little is known about its full range of activities in the cell. Here, we employed affinity purification and highly sensitive LC-MS/MS to decipher the fission yeast eIF3 interactome, which was found to contain 230 proteins. eIF3 assembles into a large supercomplex, the translasome, which contains elongation factors, tRNA synthetases, 40S and 60S ribosomal proteins, chaperones, and the proteasome. eIF3 also associates with ribosome biogenesis factors and the importins-beta Kap123p and Sal3p. Our genetic data indicated that the binding to both importins-beta is essential for cell growth, and photobleaching experiments revealed a critical role for Sal3p in the nuclear import of one of the translasome constituents, the proteasome. Our data reveal the breadth of the eIF3 interactome and suggest that factors involved in translation initiation, ribosome biogenesis, translation elongation, quality control, and transport are physically linked to facilitate efficient protein synthesis.","doi":"10.1016/j.molcel.2009.09.026","authors":"Sha Z, Brill LM, Cabrera R, Kleifeld O, Scheliga JS, Glickman MH, Chang EC, Wolf DA","authors_abbrev":"Sha Z et al.","pubmed_publication_date":"09 Oct 2009","pubmed_entrez_date":"2009-10-13","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14F5.03c","SPAC3A12.13c","SPAC1751.03","SPBP19A11.03c","SPBC646.09c","SPCC1840.03"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:41731326","title":"Harnessing the Power of SMART Single-Molecule Display for Enzyme Evolution: A Focus on Oxidase.","citation":"ACS Synth Biol 2026 Feb 23;","abstract":"For a rapid and cost-effective evolution of tailor-made enzymes, we established a high-throughput  in vitro  selection platform named SMART (Single-Molecule Assay on Ribonucleic acid by Translated product), integrating mRNA display, next-generation sequencing, and bioinformatics. SMART represents a versatile system where a module termed an auxiliary unit allows enzyme-specific selection under various experimental conditions. Here, we report on the establishment of SMART for oxidases using a model enzyme,  Schizosaccharomyces pombe  d-amino acid oxidase (SpDAAO), and ascorbate peroxidase 2 as the auxiliary enzyme to detect hydrogen peroxide produced by the oxidase, and mediate biotinylation of active single-molecule display complexes. As a proof-of-concept, a library including site-saturation mutagenesis at the catalytic residue Y232 of SpDAAO was subjected to a single SMART selection round, yielding enrichment of the active enzyme variant. The results demonstrate the utility of SMART as a fast, robust, and efficient platform with the potential of customization for other enzyme chemistries through appropriate modifications of the auxiliary unit. Using SMART, desired enzyme variants can be selected in just a few hours by a single person without the need for costly equipment or any bias or limitations.","doi":"10.1021/acssynbio.5c00968","authors":"Munaweera K, Odake N, Halim HP, Ikeda K, Zhu B, Camagna M, Ito T, Kitaguchi T, Nemoto N, Nakano H, Damnjanović J","authors_abbrev":"Munaweera K et al.","pubmed_publication_date":"23 Feb 2026","pubmed_entrez_date":"2026-02-23","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-02-25 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10757807","title":"Cid1, a fission yeast protein required for S-M checkpoint control when DNA polymerase delta or epsilon is inactivated.","citation":"Mol Cell Biol 2000 May;20(9):3234-44","abstract":"The S-M checkpoint is an intracellular signaling pathway that ensures that mitosis is not initiated in cells undergoing DNA replication. We identified cid1, a novel fission yeast gene, through its ability when overexpressed to confer specific resistance to a combination of hydroxyurea, which inhibits DNA replication, and caffeine, which overrides the S-M checkpoint. Cid1 overexpression also partially suppressed the hydroxyurea sensitivity characteristic of DNA polymerase delta mutants and mutants defective in the \"checkpoint Rad\" pathway. Cid1 is a member of a family of putative nucleotidyltransferases including budding yeast Trf4 and Trf5, and mutation of amino acid residues predicted to be essential for this activity resulted in loss of Cid1 function in vivo. Two additional Cid1-like proteins play similar but nonredundant checkpoint-signaling roles in fission yeast. Cells lacking Cid1 were found to be viable but specifically sensitive to the combination of hydroxyurea and caffeine and to be S-M checkpoint defective in the absence of Cds1. Genetic data suggest that Cid1 acts in association with Crb2/Rhp9 and through the checkpoint-signaling kinase Chk1 to inhibit unscheduled mitosis specifically when DNA polymerase delta or epsilon is inhibited.","authors":"Wang SW, Toda T, MacCallum R, Harris AL, Norbury C","authors_abbrev":"Wang SW et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-04-11","publication_year":"2000","canto_session_key":"e5b469b55d5c3cba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-05-07 14:50:09","canto_approved_date":"2020-11-20 16:32:03","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-05-07 14:50:03","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":46,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPAC19D5.03","SPBC25H2.13c","SPBC342.05","SPCC663.12","SPAC2G11.12","SPCC18B5.11c","SPBC1734.02c","SPAC664.07c","SPCC1259.13","SPAC14C4.13","SPBC216.05","SPBC1685.06","SPBC336.04","SPAC27E2.05"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2015-05-07"},{"uniquename":"PMID:19106646","title":"Cascade transcription of mRNA-type long non-coding RNAs (mlonRNAs) and local chromatin remodeling.","citation":"Epigenetics 2009 Jan;4(1):5-7","abstract":"Eukaryotic transcriptome analyses have revealed the presence of a huge number of mRNA-type non-coding RNAs (ncRNAs). Expression of them is often developmentally regulated, but little is known about their function. We have recently demonstrated that cascade of RNA polymerase II (RNAPII)-mediated transcription initiation of such mRNA-type long ncRNAs (mlonRNA) results in stepwise disruption of local chromatin structure at the fission yeast Schizosaccharomyces pombe fbp1(+) locus during transcriptional activation upon glucose derepression. Similar transition of RNA transcripts coupled with local chromatin alteration is observed meiotically in the fission yeast recombination hotspot ade6-M26. Here, we hypothesize that RNAPII transcription of mlonRNAs disrupts chromatin array. This idea may provide a new clue to understand why so many species of ncRNAs are expressed in eukaryotic cells.","authors":"Hirota K, Ohta K","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2008-12-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28404620","title":"Accumulation of RNA on chromatin disrupts heterochromatic silencing.","citation":"Genome Res 2017 Jul;27(7):1174-1183","abstract":"Long noncoding RNAs (lncRNAs) play a conserved role in regulating gene expression, chromatin dynamics, and cell differentiation. They serve as a platform for RNA interference (RNAi)-mediated heterochromatin formation or DNA methylation in many eukaryotic organisms. We found in  Schizosaccharomyces pombe  that heterochromatin is lost at transcribed regions in the absence of RNA degradation. We show that heterochromatic RNAs are retained on chromatin, form DNA:RNA hybrids, and need to be degraded by the Ccr4-Not complex or RNAi to maintain heterochromatic silencing. The Ccr4-Not complex is localized to chromatin independently of H3K9me and degrades chromatin-associated transcripts, which is required for transcriptional silencing. Overexpression of heterochromatic RNA, but not euchromatic RNA, leads to chromatin localization and loss of silencing of a distant  ade6  reporter in wild-type cells. Our results demonstrate that chromatin-bound RNAs disrupt heterochromatin organization and need to be degraded in a process of heterochromatin formation.","doi":"10.1101/gr.216986.116","authors":"Brönner C, Salvi L, Zocco M, Ugolini I, Halic M","authors_abbrev":"Brönner C et al.","pubmed_publication_date":"Jul 2017","pubmed_entrez_date":"2017-04-14","publication_year":"2017","canto_session_key":"f02a15cea2c40c03","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mario Halic","canto_first_approved_date":"2018-11-22 17:34:13","canto_approved_date":"2024-08-07 15:02:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-11-15 16:59:45","canto_added_date":"2017-04-15 00:15:21","annotation_curators":[{"name":"Mario Halic","community_curator":true,"annotation_count":36,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c","SPAC16C9.04c","SPAC20G4.01","SPBCPT2R1.08c","SPAC212.11","SPAC16A10.07c","SPCC31H12.08c","SPAC1F3.01","SPBC1D7.04","SPCC4G3.15c","SPCC736.11","SPAC17A5.14","SPAC29B12.06c","SPCC18.06c"],"gene_count":14,"ltp_gene_count":12,"approved_date":"2018-11-22"},{"uniquename":"PMID:27304859","title":"Dbl2 Regulates Rad51 and DNA Joint Molecule Metabolism to Ensure Proper Meiotic Chromosome Segregation.","citation":"PLoS Genet 2016 Jun;12(6):e1006102","abstract":"To identify new proteins required for faithful meiotic chromosome segregation, we screened a Schizosaccharomyces pombe deletion mutant library and found that deletion of the dbl2 gene led to missegregation of chromosomes during meiosis. Analyses of both live and fixed cells showed that dbl2Δ mutant cells frequently failed to segregate homologous chromosomes to opposite poles during meiosis I. Removing Rec12 (Spo11 homolog) to eliminate meiotic DNA double-strand breaks (DSBs) suppressed the segregation defect in dbl2Δ cells, indicating that Dbl2 acts after the initiation of meiotic recombination. Analyses of DSBs and Holliday junctions revealed no significant defect in their formation or processing in dbl2Δ mutant cells, although some Rec12-dependent DNA joint molecules persisted late in meiosis. Failure to segregate chromosomes in the absence of Dbl2 correlated with persistent Rad51 foci, and deletion of rad51 or genes encoding Rad51 mediators also suppressed the segregation defect of dbl2Δ. Formation of foci of Fbh1, an F-box helicase that efficiently dismantles Rad51-DNA filaments, was impaired in dbl2Δ cells. Our results suggest that Dbl2 is a novel regulator of Fbh1 and thereby Rad51-dependent DSB repair required for proper meiotic chromosome segregation and viable sex cell formation. The wide conservation of these proteins suggests that our results apply to many species.","doi":"10.1371/journal.pgen.1006102","authors":"Polakova S, Molnarova L, Hyppa RW, Benko Z, Misova I, Schleiffer A, Smith GR, Gregan J","authors_abbrev":"Polakova S et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-06-16","publication_year":"2016","canto_session_key":"e7d045397ea469f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silvia Polakova","canto_first_approved_date":"2018-03-02 14:27:19","canto_approved_date":"2024-04-26 16:43:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-02 10:24:35","canto_added_date":"2016-06-17 00:15:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":59,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Silvia Polakova","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPCC553.01c","SPAC20H4.07","SPBC28F2.07","SPAC20H4.04","SPAC15A10.03c","SPAC30D11.10","SPAC22F3.03c","SPBC336.01","SPAC9.05","SPAC644.14c","SPAPB1E7.06c","SPAC17A5.11","SPAC3C7.03c","SPAC8E11.03c"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2018-03-02"},{"uniquename":"PMID:26465752","title":"Fission Yeast Exo1 and Rqh1-Dna2 Redundantly Contribute to Resection of Uncapped Telomeres.","citation":"PLoS One 2015;10(10):e0140456","abstract":"The uncapping of telomeres induces a DNA damage response. In Schizosaccharomyces pombe, deletion of pot1+ causes telomere uncapping and rapid telomere resection, resulting in chromosome fusion. Using the nmt-pot1-aid strain, we previously reported that Pot1 shut-off causes telomere loss and chromosome fusion in S. pombe. However, the factors responsible for the resection of uncapped telomeres remain unknown. In this study, we investigated these factors and found that concomitant deletion of rqh1+ and exo1+ alleviated the loss of telomeres following Pot1 shut-off, suggesting that Rqh1 and Exo1 are redundantly involved in the resection of uncapped telomeres. We also investigated the role of Rqh1 helicase activity and found it to be essential for the resection of uncapped telomeres. Moreover, we found that Dna2 and Exo1 function redundantly in the resection of uncapped telomeres. Taken together, these results suggest that Exo1 and Rqh1-Dna2 redundantly contribute to the resection of uncapped telomeres. Therefore, our results demonstrate that nmt-pot1-aid is an important model strain to study the role of helicases and nucleases in the resection of uncapped telomeres and to improve our understanding of DNA double-strand break repair.","doi":"10.1371/journal.pone.0140456","authors":"Nanbu T, Nguyễn LC, Habib AG, Hirata N, Ukimori S, Tanaka D, Masuda K, Takahashi K, Yukawa M, Tsuchiya E, Ueno M","authors_abbrev":"Nanbu T et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-10-15","publication_year":"2015","canto_session_key":"77d127b9b5a32549","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-10-17 00:19:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.05","SPAC2G11.12","SPBC16D10.04c","SPAC26H5.06"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:21855006","title":"Chromosome segregation: monopolin attracts condensin.","citation":"Curr Biol 2011 Aug 23;21(16):R634-6","abstract":"To segregate chromosomes properly, the cell must prevent merotely, an error that occurs when a single kinetochore is attached to microtubules emanating from both spindle poles. Recent evidence suggests that cooperation between Pcs1/Mde4 and condensin complexes plays an important role in preventing merotely.","doi":"10.1016/j.cub.2011.06.059","authors":"Dudas A, Polakova S, Gregan J","authors_abbrev":"Dudas A et al.","pubmed_publication_date":"23 Aug 2011","pubmed_entrez_date":"2011-08-23","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33493431","title":"A novel motif of Rad51 serves as an interaction hub for recombination auxiliary factors.","citation":"Elife 2021 Jan 25;10","abstract":"Homologous recombination (HR) is essential for maintaining genome stability. Although Rad51 is the key protein that drives HR, multiple auxiliary factors interact with Rad51 to potentiate its activity. Here, we present an interdisciplinary characterization of the interactions between Rad51 and these factors. Through structural analysis, we identified an evolutionarily conserved acidic patch of Rad51. The neutralization of this patch completely abolished recombinational DNA repair due to defects in the recruitment of Rad51 to DNA damage sites. This acidic patch was found to be important for the interaction with Rad55-Rad57 and essential for the interaction with Rad52. Furthermore, biochemical reconstitutions demonstrated that neutralization of this acidic patch also impaired the interaction with Rad54, indicating that a single motif is important for the interaction with multiple auxiliary factors. We propose that this patch is a fundamental motif that facilitates interactions with auxiliary factors and is therefore essential for recombinational DNA repair.","doi":"10.7554/eLife.64131","authors":"Afshar N, Argunhan B, Palihati M, Taniguchi G, Tsubouchi H, Iwasaki H","authors_abbrev":"Afshar N et al.","pubmed_publication_date":"25 Jan 2021","pubmed_entrez_date":"2021-01-25","publication_year":"2021","canto_session_key":"60793151324a1ef2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-01-27 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15942936","title":"New drug-resistant cassettes for gene disruption and epitope tagging in Schizosaccharomyces pombe.","citation":"Yeast 2005 May;22(7):583-91","abstract":"We describe new heterologous modules for PCR-based gene targeting in the fission yeast Schizosaccharomyces pombe. Two bacterial genes, hph and nat, which display dominant drug-resistance phenotypes, are used as new selectable markers in these modules. Both genes have been used successfully in the budding yeast Saccharomyces cerevisiae, in which hph confers resistance to hygromycin B, while nat confers nourseothricin resistance (Goldstein and McCusker, 1999). Vector modules for gene disruption and C-terminal tagging with 3HA, 13Myc and GFP(S65T) are constructed using previously constructed pFA6a-MX6-derived plasmids (Bähler et al., 1998; Wach et al., 1997). In combination with the existing systems that are based upon the G418-resistance gene (kan), triple gene deletions or tags could be constructed. In addition a vector for one-step integration of a monomeric RFP (mRFP) to the C-terminus of proteins of interest is developed. Finally, oligonucleotides that allow a simple marker switch from kan to hph or nat, and vice versa, are described. The new constructs developed here should facilitate post-genomic molecular analysis of protein functions in fission yeast.","authors":"Sato M, Dhut S, Toda T","authors_abbrev":"Sato M et al.","pubmed_publication_date":"May 2005","pubmed_entrez_date":"2005-06-09","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8943031","title":"A human homolog of the Schizosaccharomyces pombe rad9+ checkpoint control gene.","citation":"Proc Natl Acad Sci U S A 1996 Nov 26;93(24):13890-5","abstract":"The product of the Schizosaccharomyces pombe rad9+ gene is required for cell cycle arrest at the G2 checkpoints in response to incompletely replicated or damaged DNA. We have identified a human cDNA from an infant brain library that is a structural homolog of S. pombe rad9+, by searching the dBest data base for sequences similar to the fission yeast gene. The human gene encodes a 391-amino acid long, 42,520-Da protein that is approximately 25% identical and 52% similar to the yeast protein. The human and yeast gene products demonstrate partial conservation of function, as the human cDNA can rescue to different degrees the sensitivity of S. pombe rad9::ura4+ cells to the DNA synthesis inhibitor hydroxyurea and gamma rays, as well as the associated checkpoint controls. These results suggest an underlying conservation of the molecular mechanisms of S and G2 checkpoint control pathways in most if not all eukaryotes. Fluorescence in situ hybridization using a fragment of the corresponding human genome as a probe, in conjunction with PCR reactions employing DNA from human X rodent somatic cell hybrids, has localized the gene to human chromosome 11q13.1-13.2. This region contains a number of tumor suppressor loci, and based on the biology of checkpoint control genes, HRAD9 should be considered a strong candidate for one of them.","authors":"Lieberman HB, Hopkins KM, Nass M, Demetrick D, Davey S","authors_abbrev":"Lieberman HB et al.","pubmed_publication_date":"26 Nov 1996","pubmed_entrez_date":"1996-11-26","publication_year":"1996","canto_session_key":"46aba34c4871094d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-17 11:40:57","canto_approved_date":"2018-03-17 11:40:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-03-17 11:40:48","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-03-17"},{"uniquename":"PMID:12854975","title":"Whole-genome microarrays of fission yeast: characteristics, accuracy, reproducibility, and processing of array data.","citation":"BMC Genomics 2003 Jul 10;4(1):27","abstract":"The genome of the fission yeast Schizosaccharomyces pombe has recently been sequenced, setting the stage for the post-genomic era of this increasingly popular model organism. We have built fission yeast microarrays, optimised protocols to improve array performance, and carried out experiments to assess various characteristics of microarrays.\nWe designed PCR primers to amplify specific probes (180-500 bp) for all known and predicted fission yeast genes, which are printed in duplicate onto separate regions of glass slides together with control elements (approximately 13,000 spots/slide). Fluorescence signal intensities depended on the size and intragenic position of the array elements, whereas the signal ratios were largely independent of element properties. Only the coding strand is covalently linked to the slides, and our array elements can discriminate transcriptional direction. The microarrays can distinguish sequences with up to 70% identity, above which cross-hybridisation contributes to the signal intensity. We tested the accuracy of signal ratios and measured the reproducibility of array data caused by biological and technical factors. Because the technical variability is lower, it is best to use samples prepared from independent biological experiments to obtain repeated measurements with swapping of fluorochromes to prevent dye bias. We also developed a script that discards unreliable data and performs a normalization to correct spatial artefacts.\nThis paper provides data for several microarray properties that are rarely measured. The results define critical parameters for microarray design and experiments and provide a framework to optimise and interpret array data. Our arrays give reproducible and accurate expression ratios with high sensitivity. The scripts for primer design and initial data processing as well as primer sequences and detailed protocols are available from our website.","authors":"Lyne R, Burns G, Mata J, Penkett CJ, Rustici G, Chen D, Langford C, Vetrie D, Bähler J","authors_abbrev":"Lyne R et al.","pubmed_publication_date":"10 Jul 2003","pubmed_entrez_date":"2003-07-12","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084880","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.68"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8557036","title":"Schizosaccharomyces pombe Mop1-Mcs2 is related to mammalian CAK.","citation":"EMBO J 1995 Dec 15;14(24):6164-72","abstract":"The cyclin-dependent kinase (CDK)-activating kinase, CAK, from mammals and amphibians consists of MO15/CDK7 and cyclin H, a complex which has been identified also as a RNA polymerase II C-terminal domain (CTD) kinase. While the Schizosaccharomyces pombe cdc2 gene product also requires an activating phosphorylation, the enzyme responsible has not been identified. We have isolated an essential S.pombe gene, mop1, whose product is closely related to MO15 and to Saccharomyces cerevisiae Kin28. The functional similarity of Mop1 and MO15 is reflected in the ability of MO15 to rescue a mop1 null allele. This suggests that Mop1 would be a CDK, and indeed Mop1 associates with a previously characterized cyclin H-related cyclin Mcs2 of S.pombe. Also, Mop1 and Mcs2 can associate with the heterologous partners human cyclin H and MO15, respectively. Moreover, the rescue of a temperature-sensitive mcs2 strain by expression of mop1+ demonstrates a genetic interaction between mop1 and mcs2. In a functional assay, immunoprecipitated Mop1-Mcs2 acts both as an RNA polymerase II CTD kinase and as a CAK. The CAK activity of Mop1-Mcs2 distinguishes it from the related CDK-cyclin pair Kin28-Ccl1 from S.cerevisiae, and supports the notion that Mop1-Mcs2 may represent a homolog of MO15-cyclin H in S.pombe with apparent dual roles as a RNA polymerase CTD kinase and as a CAK.","authors":"Damagnez V, Mäkelä TP, Cottarel G","authors_abbrev":"Damagnez V et al.","pubmed_publication_date":"15 Dec 1995","pubmed_entrez_date":"1995-12-15","publication_year":"1995","canto_session_key":"e96bae1f0363904c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-03 14:09:38","canto_approved_date":"2025-09-03 10:37:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-03 17:02:16","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBP16F5.02","SPBC19F8.07"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-06-03"},{"uniquename":"PMID:8546451","title":"Phylogenesis of fission yeasts. Contradictions surrounding the origin of a century old genus.","citation":"Antonie Van Leeuwenhoek 1995 Aug;68(2):119-49","abstract":"The phylogenesis of fungi is controversial due to their simple morphology and poor fossilization. Traditional classification supported by morphological studies and physiological traits placed the fission yeasts in one group with ascomycetous yeasts. The rRNA sequence comparisons, however, revealed an enormous evolutionary gap between Saccharomyces and Schizosaccharomyces. As shown in this review, the protein sequences also show a large gap which is almost as large as that separating Schizosaccharomyces from higher animals. Since the two yeasts share features (both cytological and molecular) in common which are also characteristic of ascomycetous fungi, their separation must have taken place later than the sequence differences may suggest. Possible reasons for the paradox are discussed. The sequence data also suggest a slower evolutionary rate in the Schizosaccharomyces lineage than in the Saccharomyces branch. In the fission yeast lineage two ramifications can be supposed. First S. japonicus (Hasegawaea japonica) branched off, then S. octosporus (Octosporomyces octosporus) separated from S. pombe.","authors":"Sipiczki M","authors_abbrev":"Sipiczki M","pubmed_publication_date":"Aug 1995","pubmed_entrez_date":"1995-08-01","publication_year":"1995","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25007214","title":"Contributions of transcription and mRNA decay to gene expression dynamics of fission yeast in response to oxidative stress.","citation":"RNA Biol 2014;11(6):702-14","abstract":"The cooperation of transcriptional and post-transcriptional levels of control to shape gene regulation is only partially understood. Here we show that a combination of two simple and non-invasive genomic techniques, coupled with kinetic mathematical modeling, afford insight into the intricate dynamics of RNA regulation in response to oxidative stress in the fission yeast Schizosaccharomyces pombe. This study reveals a dominant role of transcriptional regulation in response to stress, but also points to the first minutes after stress induction as a critical time when the coordinated control of mRNA turnover can support the control of transcription for rapid gene regulation. In addition, we uncover specialized gene expression strategies associated with distinct functional gene groups, such as simultaneous transcriptional repression and mRNA destabilization for genes encoding ribosomal proteins, delayed mRNA destabilization with varying contribution of transcription for ribosome biogenesis genes, dominant roles of mRNA stabilization for genes functioning in protein degradation, and adjustment of both transcription and mRNA turnover during the adaptation to stress. We also show that genes regulated independently of the bZIP transcription factor Atf1p are predominantly controlled by mRNA turnover, and identify putative cis-regulatory sequences that are associated with different gene expression strategies during the stress response. This study highlights the intricate and multi-faceted interplay between transcription and RNA turnover during the dynamic regulatory response to stress.","authors":"Marguerat S, Lawler K, Brazma A, Bähler J","authors_abbrev":"Marguerat S et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-07-10","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-07-11 00:15:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19026544","title":"Physical mechanisms redirecting cell polarity and cell shape in fission yeast.","citation":"Curr Biol 2008 Nov 25;18(22):1748-53","abstract":"The cylindrical rod shape of the fission yeast Schizosaccharomyces pombe is organized and maintained by interactions between the microtubule, cell membrane, and actin cytoskeleton [1]. Mutations affecting any components in this pathway lead to bent, branched, or round cells [2]. In this context, the cytoskeleton controls cell polarity and thus dictates cell shape. Here, we use soft-lithography techniques to construct microfluidic channels to control cell shape. We show that when wild-type rod-shaped cells are physically forced to grow in a bent fashion, they will reorganize their cytoskeleton and redirect cell polarity to make new ectopic cell tips. Moreover, when bent or round mutant cells are physically forced to conform to the wild-type rod-shape, they will reverse their mutational phenotypes by reorganizing their cytoskeleton to maintain proper wild-type-like localization of microtubules, cell-membrane proteins, and actin. Our study provides direct evidence that the cytoskeleton controls cell polarity and cell shape and demonstrates that cell shape also controls the organization of the cytoskeleton in a feedback loop. We present a model of the feedback loop to explain how fission yeast maintain a rod shape and how perturbation of specific parameters of the loop can lead to different cell shapes.","doi":"10.1016/j.cub.2008.09.047","authors":"Terenna CR, Makushok T, Velve-Casquillas G, Baigl D, Chen Y, Bornens M, Paoletti A, Piel M, Tran PT","authors_abbrev":"Terenna CR et al.","pubmed_publication_date":"25 Nov 2008","pubmed_entrez_date":"2008-11-26","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18388861","title":"Mus81 is essential for sister chromatid recombination at broken replication forks.","citation":"EMBO J 2008 May 07;27(9):1378-87","abstract":"Recombination is essential for the recovery of stalled/collapsed replication forks and therefore for the maintenance of genomic stability. The situation becomes critical when the replication fork collides with an unrepaired single-strand break and converts it into a one-ended double-strand break. We show in fission yeast that a unique broken replication fork requires the homologous recombination (HR) enzymes for cell viability. Two structure-specific heterodimeric endonucleases participate in two different resolution pathways. Mus81/Eme1 is essential when the sister chromatid is used for repair; conversely, Swi9/Swi10 is essential when an ectopic sequence is used for repair. Consequently, the utilization of these two HR modes of resolution mainly relies on the ratio of unique and repeated sequences present in various eukaryotic genomes. We also provide molecular evidence for sister recombination intermediates. These findings demonstrate that Mus81/Eme1 is the dedicated endonuclease that resolves sister chromatid recombination intermediates during the repair of broken replication forks.","doi":"10.1038/emboj.2008.65","authors":"Roseaulin L, Yamada Y, Tsutsui Y, Russell P, Iwasaki H, Arcangioli B","authors_abbrev":"Roseaulin L et al.","pubmed_publication_date":"07 May 2008","pubmed_entrez_date":"2008-04-05","publication_year":"2008","canto_session_key":"4f106c6e34491953","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-12 14:12:30","canto_approved_date":"2024-07-12 14:12:30","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-12 14:10:50","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":55,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.03","SPAC1556.01c","SPBC887.14c","SPAC15A10.03c","SPAC13C5.07","SPBC19G7.01c","SPBC4F6.15c","SPAC644.14c","SPAC20H4.07","SPAC30D11.10","SPCC4G3.05c","SPBC29A10.05"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2024-07-12"},{"uniquename":"PMID:37463013","title":"Phosphorylation of Schizosaccharomyces pombe Dss1 mediates direct binding to the ubiquitin-ligase Dma1 in vitro.","citation":"Protein Sci 2023 Sep;32(9):e4733","abstract":"Intrinsically disordered proteins (IDPs) are often multifunctional and frequently posttranslationally modified. Deleted in split hand/split foot 1 (Dss1-Sem1 in budding yeast) is a highly multifunctional IDP associated with a range of protein complexes. However, it remains unknown if the different functions relate to different modified states. In this work, we show that Schizosaccharomyces pombe Dss1 is a substrate for casein kinase 2 in vitro, and we identify three phosphorylated threonines in its linker region separating two known disordered ubiquitin-binding motifs. Phosphorylations of the threonines had no effect on ubiquitin-binding but caused a slight destabilization of the C-terminal α-helix and mediated a direct interaction with the forkhead-associated (FHA) domain of the RING-FHA E3-ubiquitin ligase defective in mitosis 1 (Dma1). The phosphorylation sites are not conserved and are absent in human Dss1. Sequence analyses revealed that the Txx(E/D) motif, which is important for phosphorylation and Dma1 binding, is not linked to certain branches of the evolutionary tree. Instead, we find that the motif appears randomly, supporting the mechanism of ex nihilo evolution of novel motifs. In support of this, other threonine-based motifs, although frequent, are nonconserved in the linker, pointing to additional functions connected to this region. We suggest that Dss1 acts as an adaptor protein that docks to Dma1 via the phosphorylated FHA-binding motifs, while the C-terminal α-helix is free to bind mitotic septins, thereby stabilizing the complex. The presence of Txx(D/E) motifs in the disordered regions of certain septin subunits may be of further relevance to the formation and stabilization of these complexes.","doi":"10.1002/pro.4733","authors":"Jacobsen NL, Bloch M, Millard PS, Ruidiaz SF, Elsborg JD, Boomsma W, Hendus-Altenburger R, Hartmann-Petersen R, Kragelund BB","authors_abbrev":"Jacobsen NL et al.","pubmed_publication_date":"Sep 2023","pubmed_entrez_date":"2023-07-18","publication_year":"2023","canto_session_key":"14402f99832a6dc1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-07-19 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1347.06c","SPAC3G6.02","SPAC17G8.10c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:24787148","title":"Insights into the mechanism of deubiquitination by JAMM deubiquitinases from cocrystal structures of the enzyme with the substrate and product.","citation":"Biochemistry 2014 May 20;53(19):3199-217","abstract":"AMSH, a conserved zinc metallo deubiquitinase, controls downregulation and degradation of cell-surface receptors mediated by the endosomal sorting complexes required for transport (ESCRT) machinery. It displays high specificity toward the Lys63-linked polyubiquitin chain, which is used as a signal for ESCRT-mediated endosomal-lysosomal sorting of receptors. Herein, we report the crystal structures of the catalytic domain of AMSH orthologue Sst2 from fission yeast, its ubiquitin (product)-bound form, and its Lys63-linked diubiquitin (substrate)-bound form at 1.45, 1.7, and 2.3 Å, respectively. The structures reveal that the P-side product fragment maintains nearly all the contacts with the enzyme as seen with the P portion (distal ubiquitin) of the Lys63-linked diubiquitin substrate, with additional coordination of the Gly76 carboxylate group of the product with the active-site Zn(2+). One of the product-bound structures described herein is the result of an attempt to cocrystallize the diubiquitin substrate bound to an active site mutant presumed to render the enzyme inactive, instead yielding a cocrystal structure of the enzyme bound to the P-side ubiquitin fragment of the substrate (distal ubiquitin). This fragment was generated in situ from the residual activity of the mutant enzyme. In this structure, the catalytic water is seen placed between the active-site Zn(2+) and the carboxylate group of Gly76 of ubiquitin, providing what appears to be a snapshot of the active site when the product is about to depart. Comparison of this structure with that of the substrate-bound form suggests the importance of dynamics of a flexible flap near the active site in catalysis. The crystal structure of the Thr319Ile mutant of the catalytic domain of Sst2 provides insight into structural basis of microcephaly capillary malformation syndrome. Isothermal titration calorimetry yields a dissociation constant (KD) of 10.2 ± 0.6 μM for the binding of ubiquitin to the enzyme, a value comparable to the KM of the enzyme catalyzing hydrolysis of the Lys63-linked diubiquitin substrate (~20 μM). These results, together with the previously reported observation that the intracellular concentration of free ubiquitin (~20 μM) exceeds that of Lys63-linked polyubiquitin chains, imply that the free, cytosolic form of the enzyme remains inhibited by being tightly bound to free ubiquitin. We propose that when AMSH associates with endosomes, inhibition would be relieved because of ubiquitin binding domains present on its endosomal binding partners that would shift the balance toward better recognition of polyubiquitin chains via the avidity effect.","doi":"10.1021/bi5003162","authors":"Shrestha RK, Ronau JA, Davies CW, Guenette RG, Strieter ER, Paul LN, Das C","authors_abbrev":"Shrestha RK et al.","pubmed_publication_date":"20 May 2014","pubmed_entrez_date":"2014-05-03","publication_year":"2014","canto_session_key":"31eee06cfedda976","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-04-08 18:10:34","canto_approved_date":"2022-06-07 09:33:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-08 18:10:25","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.08c","SPAC19B12.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-04-08","pdb_entries":[{"pdb_id":"4jxe","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A/B","position":"245-435"}],"title":"Crystal structure of Schizosaccharomyces pombe sst2 catalytic domain","entry_authors":"Shrestha RK,Das C","entry_authors_abbrev":"Shrestha RK et al.","reference_uniquename":"PMID:24787148","experimental_method":"X-ray","resolution":"1.451"},{"pdb_id":"4ms7","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A/B","position":"245-435"}],"title":"Crystal structure of Schizosaccharomyces pombe sst2 catalytic domain","entry_authors":"Shrestha RK,Ronau JA,Das C","entry_authors_abbrev":"Shrestha RK et al.","reference_uniquename":"PMID:24787148","experimental_method":"X-ray","resolution":"1.673"},{"pdb_id":"4msm","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A/C","position":"245-435"}],"title":"Crystal structure of Schizosaccharomyces pombe AMSH-like protease sst2 E286A mutant bound to ubiquitin","entry_authors":"Shrestha RK,Ronau JA,Das C","entry_authors_abbrev":"Shrestha RK et al.","reference_uniquename":"PMID:24787148","experimental_method":"X-ray","resolution":"1.74"},{"pdb_id":"4msj","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A/B/C","position":"245-435"}],"title":"Crystal structure of S. pombe AMSH-like protease SST2 catalytic domain from P212121 space group","entry_authors":"Shrestha RK,Ronau JA,Das C","entry_authors_abbrev":"Shrestha RK et al.","reference_uniquename":"PMID:24787148","experimental_method":"X-ray","resolution":"1.8"},{"pdb_id":"4msq","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A/C","position":"245-435"}],"title":"Crystal structure of Schizosaccharomyces pombe AMSH-like protease sst2 catalytic domain bound to ubiquitin","entry_authors":"Shrestha RK,Ronau JA,Das C","entry_authors_abbrev":"Shrestha RK et al.","reference_uniquename":"PMID:24787148","experimental_method":"X-ray","resolution":"1.952"},{"pdb_id":"4nql","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A","position":"221-435"}],"title":"The crystal structure of the DUB domain of AMSH orthologue, Sst2 from S. pombe, in complex with lysine 63-linked diubiquitin","entry_authors":"Ronau JA,Shrestha RK,Das C","entry_authors_abbrev":"Ronau JA et al.","reference_uniquename":"PMID:24787148","experimental_method":"X-ray","resolution":"2.3"},{"pdb_id":"4k1r","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A/C","position":"245-435"}],"title":"Crystal structure of Schizosaccharomyces pombe sst2 catalytic domain and Ubiquitin","entry_authors":"Shrestha RK,Das C","entry_authors_abbrev":"Shrestha RK et al.","reference_uniquename":"PMID:24787148","experimental_method":"X-ray","resolution":"1.632"},{"pdb_id":"4pqt","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A","position":"245-435"}],"title":"Insights into the mechanism of deubiquitination by JAMM deubiquitinases from co-crystal structures of enzyme with substrate and product","entry_authors":"Shrestha RK,Ronau JA,Das C","entry_authors_abbrev":"Shrestha RK et al.","reference_uniquename":"PMID:24787148","experimental_method":"X-ray","resolution":"2.05"},{"pdb_id":"4msd","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A/B","position":"245-435"}],"title":"Crystal structure of Schizosaccharomyces pombe AMSH-like protein SST2 T319I mutant","entry_authors":"Shrestha RK,Ronau JA,Das C","entry_authors_abbrev":"Shrestha RK et al.","reference_uniquename":"PMID:24787148","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:25665008","title":"The genomic and phenotypic diversity of Schizosaccharomyces pombe.","citation":"Nat Genet 2015 Mar;47(3):235-41","abstract":"Natural variation within species reveals aspects of genome evolution and function. The fission yeast Schizosaccharomyces pombe is an important model for eukaryotic biology, but researchers typically use one standard laboratory strain. To extend the usefulness of this model, we surveyed the genomic and phenotypic variation in 161 natural isolates. We sequenced the genomes of all strains, finding moderate genetic diversity (π = 3 × 10(-3) substitutions/site) and weak global population structure. We estimate that dispersal of S. pombe began during human antiquity (∼340 BCE), and ancestors of these strains reached the Americas at ∼1623 CE. We quantified 74 traits, finding substantial heritable phenotypic diversity. We conducted 223 genome-wide association studies, with 89 traits showing at least one association. The most significant variant for each trait explained 22% of the phenotypic variance on average, with indels having larger effects than SNPs. This analysis represents a rich resource to examine genotype-phenotype relationships in a tractable model.","doi":"10.1038/ng.3215","authors":"Jeffares DC, Rallis C, Rieux A, Speed D, Převorovský M, Mourier T, Marsellach FX, Iqbal Z, Lau W, Cheng TM, Pracana R, Mülleder M, Lawson JL, Chessel A, Bala S, Hellenthal G, O'Fallon B, Keane T, Simpson JT, Bischof L, Tomiczek B, Bitton DA, Sideri T, Codlin S, Hellberg JE, van Trigt L, Jeffery L, Li JJ, Atkinson S, Thodberg M, Febrer M, McLay K, Drou N, Brown W, Hayles J, Carazo Salas RE, Ralser M, Maniatis N, Balding DJ, Balloux F, Durbin R, Bähler J","authors_abbrev":"Jeffares DC et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-02-10","publication_year":"2015","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2015-02-12 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11260263","title":"Identification and functional analysis of the gene for type I myosin in fission yeast.","citation":"Genes Cells 2001 Mar;6(3):187-99","abstract":"Type I myosin is highly conserved among eukaryotes, and apparently plays important roles in a number of cellular processes. In the budding yeast, two myosin I species have been identified and their role in F-actin assembly has been inferred.\nWe cloned the fission yeast myo1 gene, which apparently encoded a myosin I protein. Disruption of myo1 was not lethal, but it caused growth retardation at high and low temperatures, sensitivity to a high concentration of KCl, and aberrance in cell morphology associated with an abnormal distribution of F-actin patches. An abnormal deposition of cell wall materials was also seen. Homothallic myo1Delta cells could mate, but heterothallic myo1Delta cells were poor in conjugation. Myo1p was necessary for the encapsulation of spores. The tail domain of Myo1p was pivotal for its function. Calmodulin could bind to Myo1p through the IQ domain at the neck.\nMyo1p appears to control the redistribution of F-actin patches during the cell cycle. Loss of Myo1p function is likely to slow down the actin assembly/disassembly process, which results in a failure of the actin cycle to catch up with other events in both the mitotic and meiotic cell cycles, including extension of the conjugation tubes.","authors":"Toya M, Motegi F, Nakano K, Mabuchi I, Yamamoto M","authors_abbrev":"Toya M et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-03-22","publication_year":"2001","canto_session_key":"d30173fb3bf67d59","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-01-11 17:15:03","canto_approved_date":"2026-01-25 10:21:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-09 10:44:47","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.13c","SPAC3A12.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-01-11"},{"uniquename":"PMID:18292091","title":"Global analysis of gel mobility of proteins and its use in target identification.","citation":"J Biol Chem 2008 Apr 18;283(16):10745-52","abstract":"SDS-PAGE is a basic method that has long been used for separation of proteins according to their molecular sizes. Despite its simplicity, it provides information on characteristics of proteins beyond their molecular masses because gel mobility of proteins often reflects their physicochemical properties and post-translational modifications. Here we report on a global analysis of gel mobility of the proteome, which we term the \"mobilitome,\" covering 93.4% of the fission yeast proteome. To our surprise, more than 40% of proteins did not migrate to their calculated positions. Statistical analyses revealed that the discrepancy was largely dependent on the hydrophobicity of proteins. This experimental data set, with a high coverage rate of real mobility, made it feasible to identify proteins detected on the gel without using any specialized techniques. This approach enabled us to detect previously unknown post-translational modifications of a protein; for example, we revealed that eIF5A is novel substrate of a Sir2-related deacetylase Hst2. Furthermore, we concomitantly identified twelve acetylated and eight methylated proteins using specific anti-acetylated and anti-methylated lysine antibodies, most of which had not been known to be subject to the modifications. Thus, we propose the general usefulness of the mobilitome and electrophoresis-based methodology for the identification and characterization of proteins detected on the gel.","doi":"10.1074/jbc.M709211200","authors":"Shirai A, Matsuyama A, Yashiroda Y, Hashimoto A, Kawamura Y, Arai R, Komatsu Y, Horinouchi S, Yoshida M","authors_abbrev":"Shirai A et al.","pubmed_publication_date":"18 Apr 2008","pubmed_entrez_date":"2008-02-23","publication_year":"2008","canto_session_key":"282e5f4bcad2eb5f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-07-17 20:25:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 17:07:40","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26H5.10c","SPAC3G9.03","SPCC794.09c","SPBC1709.13c","SPBC8D2.04","SPCC1322.11","SPAC1834.04","SPCC31H12.04c","SPBC336.10c","SPCC132.02","SPCC16C4.13c","SPCC1739.05"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2015-03-12"},{"uniquename":"PMID:41879517","title":"Crystal structures of Fsc1, a novel autophagy factor that mediates autophagosome-vacuole fusion in fission yeast.","citation":"Acta Crystallogr D Struct Biol 2026 Apr 01;82(Pt 4):358-369","abstract":"Fsc1 is a recently identified autophagy factor in the fission yeast Schizosaccharomyces pombe that is implicated in the autophagosome-vacuole fusion step during the final stages of autophagy. Despite its critical role, the structural basis of Fsc1 function has remained unknown. Here, we report the first crystal structures of the luminal domain of Fsc1, revealing an elongated, modular architecture composed of five tandem fasciclin (FAS1) domains. Each domain adopts a hallmark β-sandwich fold, and the overall assembly forms a continuous scaffold featuring a conserved surface groove within the FAS1-4 domain. Structural and biochemical analyses demonstrate that Fsc1 forms a homodimer in solution through a shared interface observed in two independent crystal forms, supporting a biologically relevant but potentially low-affinity association. Comparative sequence and structural analyses reveal significant homology between Fsc1 and human fasciclin proteins, including TGFBI and periostin, suggesting similar structural principles underlying their functions. Together, these findings provide the first structural insights into Fsc1 and establish a structural framework for understanding how its modular architecture and context-dependent dimerization may facilitate late-stage membrane fusion during autophagy.","doi":"10.1107/S205979832600197X","authors":"Azuka C, Liu J, Jin X","authors_abbrev":"Azuka C et al.","pubmed_publication_date":"01 Apr 2026","pubmed_entrez_date":"2026-03-25","publication_year":"2026","canto_session_key":"23f209f34455e2d3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2026-04-20 11:53:14","canto_approved_date":"2026-04-20 11:53:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-04-20 11:52:56","canto_added_date":"2026-03-26 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22H12.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2026-04-20","pdb_entries":[{"pdb_id":"9o0b","gene_chains":[{"gene_uniquename":"SPAC22H12.05c","chain":"A","position":"22-670"}],"title":"X-ray Crystal Structure of Fission Yeast Fsc1 protein in P43212","entry_authors":"Azuka CD,Jin X","entry_authors_abbrev":"Azuka CD et al.","reference_uniquename":"PMID:41879517","experimental_method":"X-ray","resolution":"2.504"},{"pdb_id":"9nu9","gene_chains":[{"gene_uniquename":"SPAC22H12.05c","chain":"A","position":"22-670"}],"title":"X-ray Crystal Structure of Fission Yeast Fsc1 protein in C2 Symmetry","entry_authors":"Azuka CD,Jin X","entry_authors_abbrev":"Azuka CD et al.","reference_uniquename":"PMID:41879517","experimental_method":"X-ray","resolution":"2.45"}]},{"uniquename":"PMID:14762117","title":"A novel RING-finger-like protein Ini1 is essential for cell cycle progression in fission yeast.","citation":"J Cell Sci 2004 Feb 29;117(Pt 6):967-74","abstract":"We have cloned a fission yeast (Schizosaccharomyces pombe) homologue of Ini, a novel RING-finger-like protein recently identified in rat that interacts with the connexin43 (cx43) promoter and might be important for the response of the cx43 gene to estrogen. S. pombe cells deleted for ini1(+) fail to form colonies and arrest with an elongated cell phenotype, indicating a cell cycle block. Cell cycle arrest is dependent on expression of Wee1, but not Rad3, suggesting that it occurs independently of the DNA damage checkpoint control. Analysis of mRNA intermediates in cells depleted for Ini1 demonstrates that Ini1 is required for pre-mRNA splicing. We observe an accumulation of pre-mRNA for six of seven genes analysed, suggesting that Ini1 is required for general splicing activity. Interestingly, loss of Ini1 results in cell death that is partially suppressed by elimination of the Wee1 kinase. Therefore, Wee1 might promote cell death in the absence of Ini1.","authors":"Oltra E, Verde F, Werner R, D'Urso G","authors_abbrev":"Oltra E et al.","pubmed_publication_date":"29 Feb 2004","pubmed_entrez_date":"2004-02-06","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC23H3.02c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11909862","title":"The unique centromeric chromatin structure of Schizosaccharomyces pombe is maintained during meiosis.","citation":"J Biol Chem 2002 May 31;277(22):19817-22","abstract":"In meiosis I sister centromeres are unified in their polarity on the spindle, and this unique behavior is known to require the function of meiosis-specific factors that set some intrinsic property of the centromeres. The fission yeast, Schizosaccharomyces pombe, possesses complex centromeres consisting of repetitive DNA elements, making it an excellent model in which to study the behavior of complex centromeres. In mitosis, during which sister centromeres mediate chromosome segregation by establishing bipolar chromosome attachments to the spindle, the central core of the S. pombe centromere chromatin has a unique irregular nucleosome pattern. Deletion of repeats flanking this core structure have no effect on mitotic chromosome segregation, but have profound effects during meiosis. While this demonstrates that the outer repeats are critical for normal meiotic sister centromere behavior, exactly how they function and how monopolarity is established remains unclear. In this study we provide the first analysis of the chromatin structure of a complex centromere during meiosis. We show that the nature and extent of the unique central core chromatin structure is maintained with no measurable expansion. This demonstrates that monopolarity of sister centromeres, and subsequent reversion to bipolarity, does not involve a global change to the centromeric chromatin structure.","authors":"Smirnova JB, McFarlane RJ","authors_abbrev":"Smirnova JB et al.","pubmed_publication_date":"31 May 2002","pubmed_entrez_date":"2002-03-23","publication_year":"2002","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11005017","title":"The microtubule organizing centers of Schizosaccharomyces pombe.","citation":"Curr Top Dev Biol 2000;49:133-59","abstract":"","authors":"Hagan IM, Petersen J","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-09-27","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23480475","title":"The secretory pathway: exploring yeast diversity.","citation":"FEMS Microbiol Rev 2013 Nov;37(6):872-914","abstract":"Protein secretion is an essential process for living organisms. In eukaryotes, this encompasses numerous steps mediated by several hundred cellular proteins. The core functions of translocation through the endoplasmic reticulum membrane, primary glycosylation, folding and quality control, and vesicle-mediated secretion are similar from yeasts to higher eukaryotes. However, recent research has revealed significant functional differences between yeasts and mammalian cells, and even among diverse yeast species. This review provides a current overview of the canonical protein secretion pathway in the model yeast Saccharomyces cerevisiae, highlighting differences to mammalian cells as well as currently unresolved questions, and provides a genomic comparison of the S. cerevisiae pathway to seven other yeast species where secretion has been investigated due to their attraction as protein production platforms, or for their relevance as pathogens. The analysis of Candida albicans, Candida glabrata, Kluyveromyces lactis, Pichia pastoris, Hansenula polymorpha, Yarrowia lipolytica, and Schizosaccharomyces pombe reveals that many - but not all - secretion steps are more redundant in S. cerevisiae due to duplicated genes, while some processes are even absent in this model yeast. Recent research obviates that even where homologous genes are present, small differences in protein sequence and/or differences in the regulation of gene expression may lead to quite different protein secretion phenotypes.","doi":"10.1111/1574-6976.12020","authors":"Delic M, Valli M, Graf AB, Pfeffer M, Mattanovich D, Gasser B","authors_abbrev":"Delic M et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-03-14","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37182814","title":"Development of an efficient insecticide substrate and inhibitor screening system of insect P450s using fission yeast.","citation":"Insect Biochem Mol Biol 2023 Jun;157:103958","abstract":"Metabolic resistance is one of the most frequent mechanisms of insecticide resistance, characterized by an increased expression of several important enzymes and transporters, especially cytochrome P450s (CYPs). Due to the large number of P450s in pests, determining the precise relationship between these enzymes and the insecticide substrates is a challenge. Herein, we developed a luminescence-based screening system for efficient identification of insecticide substrates and insect P450 inhibitors. We recombinantly expressed Bemisia tabaci CYP6CM1vQ (Bt CYP6CM1vQ) in the fission yeast Schizosaccharomyces pombe and subsequently permeabilized the yeast cells to convert them into \"enzyme bags\". We exploited these enzyme bags to screen the activity of twelve luciferin substrates and identified Luciferin-FEE as the optimal competing probe that was further used to characterize the metabolism of eight candidate commercial insecticides. Among them, Bt CYP6CM1vQ exhibited notable activity against pymetrozine and imidacloprid. Their binding modes were predicted by homology modeling and molecular docking, revealing the mechanisms of the metabolism. We also tested the inhibitory effect of eight known P450 inhibitors using our system and identified letrozole and 1-benzylimidazole as showing significant activity against Bt CYP6CM1vQ, with IC 50  values of 23.74 μM and 1.30 μM, respectively. Their potential to be developed as an insecticide synergist was further proven by an in vitro toxicity assay using imidacloprid-resistant Bemisia tabaci. Overall, our luciferin-based enzyme bag method is capable of providing a robust and efficient screening of insect P450 substrates and, more importantly, inhibitors to overcome the resistance.","doi":"10.1016/j.ibmb.2023.103958","authors":"Li X, Lin L, Li Z, Hadiatullah H, Sharma S, Du H, Yang X, Chen W, You S, Bureik M, Yuchi Z","authors_abbrev":"Li X et al.","pubmed_publication_date":"Jun 2023","pubmed_entrez_date":"2023-05-14","publication_year":"2023","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2023-05-16 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012571","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16111942","title":"Hrs1p/Mcp6p on the meiotic SPB organizes astral microtubule arrays for oscillatory nuclear movement.","citation":"Curr Biol 2005 Aug 23;15(16):1479-86","abstract":"Microtubules and the motor protein dynein play pivotal roles in the movement and positioning of the nucleus and cytoplasmic organelles in a cell. In fission yeast, oscillatory movement of the nucleus termed horsetail nuclear movement (HNM) has been observed during meiotic prophase. HNM is led by an astral microtubule array emanating from the spindle pole body (SPB), a centrosome-equivalent organelle in yeasts, aided by the dynein-dynactin complex, and is proposed to facilitate the alignment of homologous chromosomes necessary for efficient meiotic recombination. Here we show that a meiosis-specific SPB component Hrs1p (also known as Mcp6p) is a key molecule to remodel microtubules into the horsetail-astral array (HAA). Deletion of Hrs1p impaired HAA formation, leading to compromised HNM. Ectopic expression of Hrs1p during the mitotic cell cycle resulted in the formation of a HAA-like astral microtubule array, which drove an oscillatory nuclear movement in interphase cells. Hrs1p interacted with components of the gamma-tubulin ring complex (gamma-TuRC) as well as with a meiotic SPB component. We propose that Hrs1p facilitates formation of the HAA, responsible for the vigorous HNM, by stabilizing connection between the SPB and minus ends of microtubules.","authors":"Tanaka K, Kohda T, Yamashita A, Nonaka N, Yamamoto M","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"23 Aug 2005","pubmed_entrez_date":"2005-08-23","publication_year":"2005","canto_session_key":"0c03bd2b6873d1cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-08 10:22:29","canto_approved_date":"2025-09-03 20:13:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-26 20:44:50","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC417.07c","SPBC582.06c","SPAC3A11.05c","SPBC365.15"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2020-11-08"},{"uniquename":"PMID:39094570","title":"A replisome-associated histone H3-H4 chaperone required for epigenetic inheritance.","citation":"Cell 2024 Sep 05;187(18):5010-5028.e24","abstract":"Faithful transfer of parental histones to newly replicated daughter DNA strands is critical for inheritance of epigenetic states. Although replication proteins that facilitate parental histone transfer have been identified, how intact histone H3-H4 tetramers travel from the front to the back of the replication fork remains unknown. Here, we use AlphaFold-Multimer structural predictions combined with biochemical and genetic approaches to identify the Mrc1/CLASPIN subunit of the replisome as a histone chaperone. Mrc1 contains a conserved histone-binding domain that forms a brace around the H3-H4 tetramer mimicking nucleosomal DNA and H2A-H2B histones, is required for heterochromatin inheritance, and promotes parental histone recycling during replication. We further identify binding sites for the FACT histone chaperone in Swi1/TIMELESS and DNA polymerase α that are required for heterochromatin inheritance. We propose that Mrc1, in concert with FACT acting as a mobile co-chaperone, coordinates the distribution of parental histones to newly replicated DNA.","doi":"10.1016/j.cell.2024.07.006","authors":"Yu J, Zhang Y, Fang Y, Paulo JA, Yaghoubi D, Hua X, Shipkovenska G, Toda T, Zhang Z, Gygi SP, Jia S, Li Q, Moazed D","authors_abbrev":"Yu J et al.","pubmed_publication_date":"05 Sep 2024","pubmed_entrez_date":"2024-08-02","publication_year":"2024","canto_session_key":"b8574c3af47f089c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juntao Yu","canto_first_approved_date":"2025-09-29 09:45:09","canto_approved_date":"2026-02-16 16:32:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-08-27 18:47:43","canto_added_date":"2024-10-01 11:27:54","annotation_curators":[{"name":"Juntao Yu","community_curator":true,"annotation_count":52,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":55,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.03c","SPBC725.13c","SPAC1B2.05","SPAC6B12.10c","SPAC25A8.01c","SPAC227.16c","SPBP8B7.14c","SPCC16C4.22","SPAPB1E7.02c","SPBC30D10.04","SPBC3D6.09","SPAC57A10.09c","SPAC26H5.03","SPBC609.05","SPAC25H1.06","SPBC25D12.03c","SPCC23B6.05c","SPAC17D4.02","SPBC211.04c","SPBP23A10.09","SPBP4H10.21c","SPBC25H2.13c","SPBC1347.10","SPAC1834.03c","SPAC1834.04","SPCC1682.02c","SPBC1105.12","SPBC8D2.04","SPBC776.18c","SPBC902.02c","SPCC553.09c","SPBC4.04c","SPCC736.11","SPBC8D2.03c","SPAC694.06c","SPCC18B5.11c","SPBP8B7.19","SPAC3H5.06c","SPBC1105.11c","SPCC338.16","SPBC216.06c","SPBC1703.14c","SPBC17D11.06","SPCC16A11.17"],"gene_count":44,"ltp_gene_count":26,"approved_date":"2025-09-29"},{"uniquename":"PMID:12774177","title":"The involvement of ATP sulfurylase in Se(VI) and Cr(VI) reduction processes in the fission yeast Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2003 Nov;63(1):89-95","abstract":"The response of Schizosaccharomyces pombe towards the oxyanions selenate [Se(VI)] and dichromate [Cr(VI)] was investigated in order to establish the involvement of the yeast ATP sulfurylase in their reduction. An ATP sulfurylase-defective/selenate-resistant mutant of S. pombe (B-579 Se(R) -2) and an ATP sulfurylase-active/selenate-sensitive strain of S. pombe (B-579 Se(S)) were included in this study. The inhibitory effect of Se(VI) and Cr(VI) oxyanions on growth and bioaccumulation was measured. The sensitive strain showed natural sensitivity to selenate while the resistant mutant tolerated a 100-fold higher concentration of selenate. These results indicate that selenate toxicity to microorganisms is connected with the reduction of selenate to selenite. Both strains showed similar sensitivity to Cr(VI) and in this study there was no evidence that ATP sulfurylase participates in the reduction process of Cr(VI).","authors":"Raspor P, Fujs S, Banszky L, Maraz A, Batic M","authors_abbrev":"Raspor P et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-05-30","publication_year":"2003","canto_session_key":"d66cfa71d757ea73","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-21 00:03:23","canto_approved_date":"2022-05-11 17:04:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-21 00:03:15","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-01-21"},{"uniquename":"PMID:27128920","title":"Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones.","citation":"Sensors (Basel) 2016 Apr 27;16(5)","abstract":"Detection and quantification of small peptides, such as yeast pheromones, are often challenging. We developed a highly sensitive and robust affinity-assay for the quantification of the α-factor pheromone of Saccharomyces cerevisiae based on recombinant hydrophobins. These small, amphipathic proteins self-assemble into highly stable monolayers at hydrophilic-hydrophobic interfaces. Upon functionalization of solid supports with a combination of hydrophobins either lacking or exposing the α-factor, pheromone-specific antibodies were bound to the surface. Increasing concentrations of the pheromone competitively detached the antibodies, thus allowing for quantification of the pheromone. By adjusting the percentage of pheromone-exposing hydrophobins, the sensitivity of the assay could be precisely predefined. The assay proved to be highly robust against changes in sample matrix composition. Due to the high stability of hydrophobin layers, the functionalized surfaces could be repeatedly used without affecting the sensitivity. Furthermore, by using an inverse setup, the sensitivity was increased by three orders of magnitude, yielding a novel kind of biosensor for the yeast pheromone with the lowest limit of detection reported so far. This assay was applied to study the pheromone secretion of diverse yeast strains including a whole-cell biosensor strain of Schizosaccharomyces pombe modulating α-factor secretion in response to an environmental signal.","doi":"10.3390/s16050602","authors":"Hennig S, Rödel G, Ostermann K","authors_abbrev":"Hennig S et al.","pubmed_publication_date":"27 Apr 2016","pubmed_entrez_date":"2016-04-30","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-05-01 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17322209","title":"Fingerprinting fission yeast: polymorphic markers for molecular genetic analysis of Schizosaccharomyces pombe strains.","citation":"Microbiology (Reading) 2007 Mar;153(Pt 3):887-97","abstract":"The fission yeast Schizosaccharomyces pombe is widely used as a model eukaryote for cell and molecular studies but little is known of natural genetic variation in this species. In order to obtain informative molecular markers, imperfect tandem repeats, identified through bioinformatic methods, were tested for length polymorphism in six wild-type strains of Sch. pombe isolated from different substrates and geographical locations in Africa, America, Asia and Europe. Of 26 loci tested, 21 were multi-allelic, consistent with tandem repeat copy number variation. Eleven of these polymorphic tandem repeats are in regions encoding intracellular proteins. Most of the protein-coding repeats are not sited within structured domains but have non-regular predicted structure; one has a repeat unit length corresponding to integer turns of a predicted amphipathic alpha-helix secondary structure, suggesting that this repeat may be tolerated because copy number mutations change alpha-helix length but not orientation within the protein structure. In contrast to the differences observed between natural isolates of Sch. pombe, genetic strains were found to be essentially isogenic: only two polymorphic loci were detected out of 26 minisatellites and five microsatellites tested in 16 strains, including a hypervariable microsatellite in the med15 gene. The polymorphic tandem repeat markers identified in this study will prove useful for DNA fingerprinting and molecular analysis of natural genetic variation in Sch. pombe isolates.","authors":"Patch AM, Aves SJ","authors_abbrev":"Patch AM et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-02-27","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9254727","title":"Integrated map of the Schizosaccharomyces pombe genome.","citation":"Chromosoma 1997 Sep;106(4):254-65","abstract":"A restriction map of the entire Schizosaccharomyces pombe genome was constructed using two restriction enzymes (BamHI and PstI) that recognize 6 bp. The restriction map contains 420 minimally overlapping clones (miniset) and has 22 gaps. We located 126 genes, marker fragments of DNA (NotI and SfiI linking clones), and 36 transposable elements by hybridization to unique restriction fragments.","authors":"Garkavtsev I, Mizukami T","authors_abbrev":"Garkavtsev I et al.","pubmed_publication_date":"Sep 1997","pubmed_entrez_date":"1997-08-20","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21840412","title":"Expression and functional characterisation of TNC, a high-affinity nickel transporter from Neurospora crassa.","citation":"Fungal Genet Biol 2011 Nov;48(11):1020-6","abstract":"Our previous in silico studies identified a high-affinity nickel transporter, TNC, from the metal transportome of Neurospora crassa. A knockout mutant of the tnc gene in N. crassa failed to transport nickel, showed phenotypic growth defects and diminished urease activity under physiological levels of nickel. Transport assays conducted in wild type and knockout mutant strains showed that TNC transports nickel with high affinity but exhibits selectivity for other transition metal ions like cobalt. Heterologous complementation of Schizosaccharomyces pombe nickel uptake mutant by TNC further substantiates its nickel transport function. Transcriptional analysis of the nickel transporter encoding gene, tnc in N. crassa by qRT-PCR showed its constitutive expression in various phases of its life cycle. However, levels of the corresponding protein TNC were down-regulated only by increasing the nickel, but not cobalt concentration in the media. Immunolocalisation data suggested that TNC is distributed in the plasma membrane of N. crassa. Thus, the present study establishes TNC as a functional plasma membrane nickel transporter necessary for physiological acquisition of nickel in the multicellular fungi N. crassa.","doi":"10.1016/j.fgb.2011.07.006","authors":"Tiwari A, Korripally P, Adhikarla H, Patnala K, Pamarthi MM, Bhanoori M","authors_abbrev":"Tiwari A et al.","pubmed_publication_date":"Nov 2011","pubmed_entrez_date":"2011-08-16","publication_year":"2011","canto_session_key":"69f3d35ee479961c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-02 13:33:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-02 13:33:18","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1884.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-02"},{"uniquename":"PMID:17761528","title":"Stress-activated protein kinase-mediated down-regulation of the cell integrity pathway mitogen-activated protein kinase Pmk1p by protein phosphatases.","citation":"Mol Biol Cell 2007 Nov;18(11):4405-19","abstract":"Fission yeast mitogen-activated protein kinase (MAPK) Pmk1p is involved in morphogenesis, cytokinesis, and ion homeostasis as part of the cell integrity pathway, and it becomes activated under multiple stresses, including hyper- or hypotonic conditions, glucose deprivation, cell wall-damaging compounds, and oxidative stress. The only protein phosphatase known to dephosphorylate and inactivate Pmk1p is Pmp1p. We show here that the stress-activated protein kinase (SAPK) pathway and its main effector, Sty1p MAPK, are essential for proper deactivation of Pmk1p under hypertonic stress in a process regulated by Atf1p transcription factor. We demonstrate that tyrosine phosphatases Pyp1p and Pyp2p, and serine/threonine phosphatase Ptc1p, that negatively regulate Sty1p activity and whose expression is dependent on Sty1p-Atf1p function, are involved in Pmk1p dephosphorylation under osmostress. Pyp1p and Ptc1p, in addition to Pmp1p, also control the basal level of MAPK Pmk1p activity in growing cells and associate with, and dephosphorylate Pmk1p both in vitro and in vivo. Our results with Ptc1p provide the first biochemical evidence for a PP2C-type phosphatase acting on more than one MAPK in yeast cells. Importantly, the SAPK-dependent down-regulation of Pmk1p through Pyp1p, Pyp2p, and Ptc1p was not complete, and Pyp1p and Ptc1p phosphatases are able to negatively regulate MAPK Pmk1p activity by an alternative regulatory mechanism. Our data also indicate that Pmk1p phosphorylation oscillates as a function of the cell cycle, peaking at cell separation during cytokinesis, and that Pmp1p phosphatase plays a main role in regulating this process.","authors":"Madrid M, Núñez A, Soto T, Vicente-Soler J, Gacto M, Cansado J","authors_abbrev":"Madrid M et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-09-01","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23028377","title":"Factors that promote H3 chromatin integrity during transcription prevent promiscuous deposition of CENP-A(Cnp1) in fission yeast.","citation":"PLoS Genet 2012 Sep;8(9):e1002985","abstract":"Specialized chromatin containing CENP-A nucleosomes instead of H3 nucleosomes is found at all centromeres. However, the mechanisms that specify the locations at which CENP-A chromatin is assembled remain elusive in organisms with regional, epigenetically regulated centromeres. It is known that normal centromeric DNA is transcribed in several systems including the fission yeast, Schizosaccharomyces pombe. Here, we show that factors which preserve stable histone H3 chromatin during transcription also play a role in preventing promiscuous CENP-A(Cnp1) deposition in fission yeast. Mutations in the histone chaperone FACT impair the maintenance of H3 chromatin on transcribed regions and promote widespread CENP-A(Cnp1) incorporation at non-centromeric sites. FACT has little or no effect on CENP-A(Cnp1) assembly at endogenous centromeres where CENP-A(Cnp1) is normally assembled. In contrast, Clr6 complex II (Clr6-CII; equivalent to Rpd3S) histone deacetylase function has a more subtle impact on the stability of transcribed H3 chromatin and acts to prevent the ectopic accumulation of CENP-A(Cnp1) at specific loci, including subtelomeric regions, where CENP-A(Cnp1) is preferentially assembled. Moreover, defective Clr6-CII function allows the de novo assembly of CENP-A(Cnp1) chromatin on centromeric DNA, bypassing the normal requirement for heterochromatin. Thus, our analyses show that alterations in the process of chromatin assembly during transcription can destabilize H3 nucleosomes and thereby allow CENP-A(Cnp1) to assemble in its place. We propose that normal centromeres provide a specific chromatin context that limits reassembly of H3 chromatin during transcription and thereby promotes the establishment of CENP-A(Cnp1) chromatin and associated kinetochores. These findings have important implications for genetic and epigenetic processes involved in centromere specification.","doi":"10.1371/journal.pgen.1002985","authors":"Choi ES, Strålfors A, Catania S, Castillo AG, Svensson JP, Pidoux AL, Ekwall K, Allshire RC","authors_abbrev":"Choi ES et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-10-03","publication_year":"2012","canto_session_key":"11f8c49a46c7964f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-27 14:21:59","canto_approved_date":"2026-01-30 13:05:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-27 14:21:51","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":39,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.10c","SPAPB1A10.02","SPBC19C7.11","SPAC1F7.01c","SPBP8B7.19","SPBC409.04c","SPBC36.05c","SPBC609.05","SPBC1105.17","SPAC26H5.06","SPAC1687.20c","SPAC23H4.12","SPAC13F5.01c","SPBC577.15c","SPAC16C9.05","SPCC970.12","SPAC23C11.15","SPBC428.08c","SPBC1861.01c"],"gene_count":19,"ltp_gene_count":10,"approved_date":"2016-01-27"},{"uniquename":"PMID:17072892","title":"Cytoplasmic microtubule organization in fission yeast.","citation":"Yeast 2006 Oct 15;23(13):1001-14","abstract":"During the cell cycle of the fission yeast Schizosaccharomyces pombe, striking changes in the organization of the cytoplasmic microtubule cytoskeleton take place. These may serve as a model for understanding the different modes of microtubule organization that are often characteristic of differentiated higher eukaryotic cells. In the last few years, considerable progress has been made in our understanding of the organization and behaviour of fission yeast cytoplasmic microtubules, not only in the identification of the genes and proteins involved but also in the physiological analysis of function using fluorescently-tagged proteins in vivo. In this review we discuss the state of our knowledge in three areas: microtubule nucleation, regulation of microtubule dynamics and the organization and polarity of microtubule bundles. Advances in these areas provide a solid framework for a more detailed understanding of cytoplasmic microtubule organization.","authors":"Sawin KE, Tran PT","authors_abbrev":"Sawin KE et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11750761","title":"Dielectric spectroscopy of Schizosaccharomyces pombe using electrorotation and electroorientation.","citation":"Biochim Biophys Acta 2001 Dec 05;1568(2):135-46","abstract":"Two complementary AC electrokinetic techniques electrorotation (ER) and electroorientation (EO) enabled the dielectric characterization of the rod-shaped fission yeast Schizosaccharomyces pombe. The use of microstructured electrodes allowed both ER and EO measurements to be performed over wide ranges of field frequency and medium conductivity. Due to their layered structure, living S. pombe cells exhibited up to three well resolved peaks in their ER spectra and also two distinct orientations, i.e., parallel or perpendicular to the imposed linear field. Heat treatment and enzymatic protoplast isolation led to dramatic changes in the electrokinetic behavior of fission yeast. Application of the theoretical models linking the ER and EO spectra yielded the dielectric parameters of the major structural units of S. pombe cells (cell wall, plasma membrane and cytosol). The dielectric characterization of yeasts has an enormous impact in biotechnology and biomedicine, because electric field pulse techniques (electrofusion and electropermeabilization) are widely used for production of transgenic yeast strains of economic importance. The present study also showed that combined ER and EO measurements can be employed as a powerful diagnostic tool for analyzing changes in yeast structure and physiology upon exposure to various stress conditions.","authors":"Kriegmaier M, Zimmermann M, Wolf K, Zimmermann U, Sukhorukov VL","authors_abbrev":"Kriegmaier M et al.","pubmed_publication_date":"05 Dec 2001","pubmed_entrez_date":"2001-12-26","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12697170","title":"Synthesis and antimicrobial evaluation of farnesyl diphosphate mimetics.","citation":"Bioorg Chem 2003 Feb;31(1):80-97","abstract":"The synthesis and first antimicrobial evaluation of farnesyl diphosphate mimetics are described. Several analogues (10, 12, 13, and 20) are inhibitors of Candida albicans, Shizosaccharomyces pombe, and Saccharomyces cerevisiae. The activities of analogues 10, 12, and 13, which contain a omega-phenyl moiety and a diphosphate isostere, are not attributable to inhibition of sterol biosynthesis via squalene synthase. Two geranyl phenylsulphones (14 and 15) are potent inhibitors of Escherichia coli. Analogue 15 exhibits potent activity towards Salmonella typhimurium and Pseudomonas aeruginosa (MIC-2 microg/mL) and represents the first type of semi-synthetic terpenoid allylic sulphone active against these bacteria.","authors":"Fairlamb IJ, Dickinson JM, O'Connor R, Cohen LH, van Thiel CF","authors_abbrev":"Fairlamb IJ et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-04-17","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2145281","title":"Calcium homeostasis and transport are affected by disruption of cta3, a novel gene encoding Ca2(+)-ATPase in Schizosaccharomyces pombe.","citation":"J Biol Chem 1990 Oct 25;265(30):18400-7","abstract":"A new P-type ATPase gene, cta3, has been identified in Schizosaccharomyces pombe. The deduced amino acid sequence presents a 45% identity with the Saccharomyces cerevisiae putative Ca2(+)-ATPase encoded by the PMR2 gene. The cta3 protein contains 7 out of the 8 amino acid residues involved in high affinity Ca2+ binding in the sarcoplasmic reticulum Ca2(+)-ATPase from muscles. It also contains a region similar to the phospholamban-binding domain that characterizes this Ca2+ pump. A null mutation of cta3 leads to higher levels of cytosolic free Ca2+ and to lower amounts of sequestered and bound Ca2+. Cellular Ca2+ efflux and rates of uptake into intracellular compartments are reduced by the loss of cta3 function. The sequence analysis and the physiological results strongly support the conclusion that the cta3 gene encodes a Ca2(+)-ATPase, probably located in intracellular membranes.","authors":"Ghislain M, Goffeau A, Halachmi D, Eilam Y","authors_abbrev":"Ghislain M et al.","pubmed_publication_date":"25 Oct 1990","pubmed_entrez_date":"1990-10-25","publication_year":"1990","canto_session_key":"b3dd7eb4e7f637de","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-02-08 19:19:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 18:45:35","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC839.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-08"},{"uniquename":"PMID:29167439","title":"Eroded telomeres are rearranged in quiescent fission yeast cells through duplications of subtelomeric sequences.","citation":"Nat Commun 2017 Nov 22;8(1):1684","abstract":"While the mechanisms of telomere maintenance has been investigated in dividing cells, little is known about the stability of telomeres in quiescent cells and how dysfunctional telomeres are processed in non-proliferating cells. Here we examine the stability of telomeres in quiescent cells using fission yeast. While wild type telomeres are stable in quiescence, we observe that eroded telomeres were highly rearranged during quiescence in telomerase minus cells. These rearrangements depend on homologous recombination (HR) and correspond to duplications of subtelomeric regions. HR is initiated at newly identified subtelomeric homologous repeated sequences (HRS). We further show that TERRA (Telomeric Repeat-containing RNA) is increased in post-mitotic cells with short telomeres and correlates with telomere rearrangements. Finally, we demonstrate that rearranged telomeres prevent cells to exit properly from quiescence. Taken together, we describe in fission yeast a mode of telomere repair mechanism specific to post-mitotic cells that is likely promoted by transcription.","doi":"10.1038/s41467-017-01894-6","authors":"Maestroni L, Audry J, Matmati S, Arcangioli B, Géli V, Coulon S","authors_abbrev":"Maestroni L et al.","pubmed_publication_date":"22 Nov 2017","pubmed_entrez_date":"2017-11-24","publication_year":"2017","canto_session_key":"f1c2dba49bdde890","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-05-16 18:56:11","canto_approved_date":"2025-09-03 13:23:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-18 09:34:45","canto_added_date":"2017-11-25 01:15:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPCC338.08","SPBC29A10.05","SPNCRNA.214","SPAC13C5.07","SPAC644.14c","SPBC428.08c","SPBP35G2.10","SPBC336.06c"],"gene_count":9,"ltp_gene_count":5,"approved_date":"2018-05-16"},{"uniquename":"PMID:16990132","title":"Monopolar attachment of sister kinetochores at meiosis I requires casein kinase 1.","citation":"Cell 2006 Sep 22;126(6):1049-64","abstract":"In meiosis, a single round of DNA replication is followed by two consecutive rounds of chromosome segregation, called meiosis I and II. Disjunction of maternal from paternal centromeres during meiosis I depends on the attachment of sister kinetochores to microtubules emanating from the same pole. In budding yeast, monopolar attachment requires recruitment to kinetochores of the monopolin complex. How monopolin promotes monopolar attachment was unclear, as its subunits are poorly conserved and lack similarities to proteins with known functions. We show here that the monopolin subunit Mam1 binds tightly to Hrr25, a highly conserved casein kinase 1 delta/epsilon (CK1delta/epsilon), and recruits it to meiosis I centromeres. Hrr25 kinase activity and Mam1 binding are both essential for monopolar attachment. Since CK1delta/epsilon activity is important for accurate chromosome segregation during meiosis I also in fission yeast, phosphorylation of kinetochore proteins by CK1delta/epsilon might be an evolutionary conserved process required for monopolar attachment.","authors":"Petronczki M, Matos J, Mori S, Gregan J, Bogdanova A, Schwickart M, Mechtler K, Shirahige K, Zachariae W, Nasmyth K","authors_abbrev":"Petronczki M et al.","pubmed_publication_date":"22 Sep 2006","pubmed_entrez_date":"2006-09-23","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.12","SPBC3H7.15"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:32499400","title":"Nutrient-dependent control of RNA polymerase II elongation rate regulates specific gene expression programs by alternative polyadenylation.","citation":"Genes Dev 2020 Jul 01;34(13-14):883-897","abstract":"Transcription by RNA polymerase II (RNAPII) is a dynamic process with frequent variations in the elongation rate. However, the physiological relevance of variations in RNAPII elongation kinetics has remained unclear. Here we show in yeast that a RNAPII mutant that reduces the transcription elongation rate causes widespread changes in alternative polyadenylation (APA). We unveil two mechanisms by which APA affects gene expression in the slow mutant: 3' UTR shortening and gene derepression by premature transcription termination of upstream interfering noncoding RNAs. Strikingly, the genes affected by these mechanisms are enriched for functions involved in phosphate uptake and purine synthesis, processes essential for maintenance of the intracellular nucleotide pool. As nucleotide concentration regulates transcription elongation, our findings argue that RNAPII is a sensor of nucleotide availability and that genes important for nucleotide pool maintenance have adopted regulatory mechanisms responsive to reduced rates of transcription elongation.","doi":"10.1101/gad.337212.120","authors":"Yague-Sanz C, Vanrobaeys Y, Fernandez R, Duval M, Larochelle M, Beaudoin J, Berro J, Labbé S, Jacques PÉ, Bachand F","authors_abbrev":"Yague-Sanz C et al.","pubmed_publication_date":"01 Jul 2020","pubmed_entrez_date":"2020-06-06","publication_year":"2020","canto_session_key":"63cd6d753b3b6617","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Carlo Yague-Sanz","canto_first_approved_date":"2020-06-24 09:39:31","canto_approved_date":"2024-04-04 10:21:49","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-06-14 20:32:37","canto_added_date":"2020-06-12 15:53:49","annotation_curators":[{"name":"Carlo Yague-Sanz","community_curator":true,"annotation_count":6,"orcid":"0000-0002-9941-9703","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8E4.01c","SPAC6F12.17","SPBC1271.09","SPBP4G3.02","SPNCRNA.1698","SPBC106.05c","SPAC222.09","SPBC27B12.11c","SPBC28F2.12"],"gene_count":9,"ltp_gene_count":2,"approved_date":"2020-06-24"},{"uniquename":"PMID:31584934","title":"Histone deposition promotes recombination-dependent replication at arrested forks.","citation":"PLoS Genet 2019 Oct;15(10):e1008441","abstract":"Replication stress poses a serious threat to genome stability. Recombination-Dependent-Replication (RDR) promotes DNA synthesis resumption from arrested forks. Despite the identification of chromatin restoration pathways after DNA repair, crosstalk coupling RDR and chromatin assembly is largely unexplored. The fission yeast Chromatin Assembly Factor-1, CAF-1, is known to promote RDR. Here, we addressed the contribution of histone deposition to RDR. We expressed a mutated histone, H3-H113D, to genetically alter replication-dependent chromatin assembly by destabilizing (H3-H4)2 tetramer. We established that DNA synthesis-dependent histone deposition, by CAF-1 and Asf1, promotes RDR by preventing Rqh1-mediated disassembly of joint-molecules. The recombination factor Rad52 promotes CAF-1 binding to sites of recombination-dependent DNA synthesis, indicating that histone deposition occurs downstream Rad52. Histone deposition and Rqh1 activity act synergistically to promote cell resistance to camptothecin, a topoisomerase I inhibitor that induces replication stress. Moreover, histone deposition favors non conservative recombination events occurring spontaneously in the absence of Rqh1, indicating that the stabilization of joint-molecules by histone deposition also occurs independently of Rqh1 activity. These results indicate that histone deposition plays an active role in promoting RDR, a benefit counterbalanced by stabilizing at-risk joint-molecules for genome stability.","doi":"10.1371/journal.pgen.1008441","authors":"Hardy J, Dai D, Ait Saada A, Teixeira-Silva A, Dupoiron L, Mojallali F, Fréon K, Ochsenbein F, Hartmann B, Lambert S","authors_abbrev":"Hardy J et al.","pubmed_publication_date":"Oct 2019","pubmed_entrez_date":"2019-10-05","publication_year":"2019","canto_session_key":"0de8787e35f61acb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Lambert","canto_first_approved_date":"2019-11-28 10:48:12","canto_approved_date":"2025-09-03 13:41:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-17 17:16:48","canto_added_date":"2019-10-06 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Sarah Lambert","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.04","SPBC31F10.13c","SPAC2G11.12","SPAC1834.04","SPBC1105.11c","SPBC29A10.03c","SPBC342.06c","SPCC663.05c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2019-11-28"},{"uniquename":"PMID:41565562","title":"Metabolic pathway of the rare sugar 5-keto-d-fructose in the oleaginous yeast Lipomycesstarkeyi.","citation":"J Biosci Bioeng 2026 Jan 20;","abstract":"Acetic acid bacteria convert environmental sugars and alcohols into acetic acid and various sugars through oxidative fermentation, resulting in the accumulation of these compounds at high concentrations in the culture medium. One such product is the rare sugar 5-keto-d-fructose (5-KF). In Gluconobacter species, 5-KF is transported into the cell and reduced to fructose in a single step by 5-ketofructose reductase, allowing entry into glycolysis. However, it remains unclear whether eukaryotic microorganisms can metabolize 5-KF or which genes are involved in this process. In this study, we investigated the ability of various yeasts to utilize 5-KF and identified genes involved in its metabolism. The model yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe were unable to grow on 5-KF, whereas the oleaginous yeast Lipomyces starkeyi efficiently metabolized this sugar. RNA-seq analysis of L. starkeyi grown on 5-KF revealed genes specifically upregulated in response to 5-KF. Based on gene annotation and expression profiles, a putative metabolic pathway was proposed. Gene knockout analyses showed that mutants deficient in specific steps of the pathway grew on downstream intermediates but failed to grow on upstream substrates, indicating loss of the corresponding enzymatic functions. These results suggest that L. starkeyi metabolizes 5-KF via a multistep pathway, 5-KF → l-sorbose → d-sorbitol → d-fructose. This study provides the first evidence of a 5-KF metabolic pathway in yeast, distinct from the single-step conversion to fructose observed in Gluconobacter species.","doi":"10.1016/j.jbiosc.2025.12.009","authors":"Noyori Y, Sato R, Takeshita K, Mori K, Tashiro K, Higuchi Y, Maekawa H, Takaku H, Takegawa K","authors_abbrev":"Noyori Y et al.","pubmed_publication_date":"20 Jan 2026","pubmed_entrez_date":"2026-01-21","publication_year":"2026","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2026-01-23 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10080187","title":"Involvement of nucleotide-excision repair in msh2 pms1-independent mismatch repair.","citation":"Nat Genet 1999 Mar;21(3):314-7","abstract":"Nucleotide-excision repair (NER) and mismatch repair (MMR) are prominent examples of highly conserved DNA repair systems which recognize and replace damaged and/or mispaired nucleotides in DNA. In humans, inheritable defects in components of the NER system are associated with severe diseases such as xeroderma pigmentosum (XP) and Cockayne syndrome (CS), whereas inactivation of MMR is accompanied by predisposition to certain types of cancer. In Schizosaccharomyces pombe, the msh2- and pms1-dependent long-patch MMR system efficiently corrects small insertion/deletion loops and all base-base mismatches, except C/C. Up to 70% of C/C mismatches generated in recombination intermediates, and to a lesser extent also other base-base mismatches, are thought to undergo correction by a minor, short-patch excision repair system. We identify here the NER genes rhpl4, swi10 and rad16 as components of this repair pathway and show that they act independently of msh2 and pms1.","authors":"Fleck O, Lehmann E, Schär P, Kohli J","authors_abbrev":"Fleck O et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-03-18","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC649.03","SPAC19G12.02c","SPBC4F6.15c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:21360732","title":"Marker reconstitution mutagenesis: a simple and efficient reverse genetic approach.","citation":"Yeast 2011 Mar;28(3):205-12","abstract":"A novel reverse genetic approach termed 'marker reconstitution mutagenesis' was designed to generate mutational allelic series in genes of interest. This approach consists of two simple steps which utilize two selective markers. First, using one selective marker, a partial fragment of another selective marker gene is inserted adjacently to a gene of interest by homologous recombination. Second, random mutations are introduced precisely into the gene of interest, together with the reconstitution of the latter selective marker by homologous recombination. This approach was successfully tested for several genes in the fission yeast Schizosaccharomyces pombe. It circumvents the problems encountered with other methods and should be adaptable to any organism that incorporates exogenous DNA by homologous recombination.","doi":"10.1002/yea.1831","authors":"Tang X, Huang J, Padmanabhan A, Bakka K, Bao Y, Tan BY, Cande WZ, Balasubramanian MK","authors_abbrev":"Tang X et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-03-02","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008067","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36095128","title":"Splicing of branchpoint-distant exons is promoted by Cactin, Tls1 and the ubiquitin-fold-activated Sde2.","citation":"Nucleic Acids Res 2022 Sep 23;50(17):10000-10014","abstract":"Intron diversity facilitates regulated gene expression and alternative splicing. Spliceosomes excise introns after recognizing their splicing signals: the 5'-splice site (5'ss), branchpoint (BP) and 3'-splice site (3'ss). The latter two signals are recognized by U2 small nuclear ribonucleoprotein (snRNP) and its accessory factors (U2AFs), but longer spacings between them result in weaker splicing. Here, we show that excision of introns with a BP-distant 3'ss (e.g. rap1 intron 2) requires the ubiquitin-fold-activated splicing regulator Sde2 in Schizosaccharomyces pombe. By monitoring splicing-specific ura4 reporters in a collection of S. pombe mutants, Cay1 and Tls1 were identified as additional regulators of this process. The role of Sde2, Cay1 and Tls1 was further confirmed by increasing BP-3'ss spacings in a canonical tho5 intron. We also examined BP-distant exons spliced independently of these factors and observed that RNA secondary structures possibly bridged the gap between the two signals. These proteins may guide the 3'ss towards the spliceosome's catalytic centre by folding the RNA between the BP and 3'ss. Orthologues of Sde2, Cay1 and Tls1, although missing in the intron-poor Saccharomyces cerevisiae, are present in intron-rich eukaryotes, including humans. This type of intron-specific pre-mRNA splicing appears to have evolved for regulated gene expression and alternative splicing of key heterochromatin factors.","doi":"10.1093/nar/gkac769","authors":"Anil AT, Choudhary K, Pandian R, Gupta P, Thakran P, Singh A, Sharma M, Mishra SK","authors_abbrev":"Anil AT et al.","pubmed_publication_date":"23 Sep 2022","pubmed_entrez_date":"2022-09-12","publication_year":"2022","canto_session_key":"d21f630f6100c4d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shravan Mishra","canto_first_approved_date":"2023-09-01 17:38:36","canto_approved_date":"2026-02-16 16:38:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-08-29 05:22:51","canto_added_date":"2022-09-15 00:15:04","annotation_curators":[{"name":"Shravan Mishra","community_curator":true,"annotation_count":36,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC663.11","SPAC1D4.01","SPAC17A5.16","SPBC6B1.10","SPAC3H5.04","SPCC1235.09","SPBC646.02","SPBC713.05","SPAC11E3.09","SPAC30D11.09","SPAC31G5.18c","SPBC582.04c","SPCC188.08c","SPBC1539.07c","SPBC800.02","SPAC57A10.03","SPBC32F12.05c","SPBC3B9.08c","SPBC428.06c","SPBC1778.02","SPBC2F12.12c","SPAC23C11.15","SPBC713.02c","SPAC3A12.14","SPCC825.05c","SPCC16A11.08","SPAC13C5.02","SPCC594.07c","SPAC1610.01","SPBC16H5.05c","SPAC1296.04"],"gene_count":31,"ltp_gene_count":18,"approved_date":"2023-09-01"},{"uniquename":"PMID:9372449","title":"Onset of gluconate-H+ symport in Schizosaccharomyces pombe is regulated by the kinases Wis1 and Pka1, and requires the gti1+ gene product.","citation":"J Cell Sci 1997 Oct;110 ( Pt 20):2599-608","abstract":"In the fission yeast Schizosaccharomyces pombe, glucose represses onset of gluconate-H+ symport and inhibits transiently the activity of the symport protein. Wild-type cells harvested from high glucose medium take up gluconate very slowly and the rate of uptake is increased 150-fold in response to glucose starvation. Here it is shown that an intact cAMP cascade is necessary to prevent premature onset in the presence of high glucose concentrations. Cells which have lost either adenylate cyclase (Cyr1) or cAMP-dependent protein kinase (Pka1) transport gluconate up to 60-fold faster than wild-type cells when harvested from high glucose medium. Moreover, inactivation of the stress-sensing Wis1-Sty1 MAP kinase pathway, by loss of Wis1 MAP kinase kinase, diminishes 10-fold the onset of gluconate uptake in response to starvation. A mutant was identified showing a comparable phenotype. By complementation, the gti1+ (gluconate transport inducer 1) gene has been isolated. Disruption of gti1 reduces starvation-induced onset by a similar factor to that observed in wis1 delta cells. Cells over-expressing gti1+ induce gluconate uptake much faster resulting in a threefold higher uptake rate, although gti1+ does not code for the gluconate transport protein. In contrast to the repression of onset, transient downregulation of the gluconate symporter is independent of Pka1 activity and requires ongoing glucose influx. Addition of glucose to starved cyr1 delta cells reduces uptake 9-fold, whereas starved pka1 delta cells, which are able to synthesise cAMP, respond with a 60-fold decrease in transport.","authors":"Caspari T","authors_abbrev":"Caspari T","pubmed_publication_date":"Oct 1997","pubmed_entrez_date":"1998-02-12","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC409.07c","SPBC19C7.03","SPAC1751.01c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23201273","title":"Nonspecific recognition is achieved in Pot1pC through the use of multiple binding modes.","citation":"Structure 2013 Jan 08;21(1):121-132","abstract":"Pot1 is the protein responsible for binding to and protecting the 3' single-stranded DNA (ssDNA) overhang at most eukaryotic telomeres. Here, we present the crystal structure of one of the two oligonucleotide/oligosaccharide-binding folds (Pot1pC) that make up the ssDNA-binding domain in S. pombe Pot1. Comparison with the homologous human domain reveals unexpected structural divergence in the mode of ligand binding that explains the differing ligand requirements between species. Despite the presence of apparently base-specific hydrogen bonds, Pot1pC is able to bind a wide range of ssDNA sequences with thermodynamic equivalence. To address how Pot1pC binds ssDNA with little to no specificity, multiple structures of Pot1pC bound to noncognate ssDNA ligands were solved. These structures reveal that this promiscuity is implemented through new binding modes that thermodynamically compensate for base-substitutions through alternate stacking interactions and new H-bonding networks.","doi":"10.1016/j.str.2012.10.015","authors":"Dickey TH, McKercher MA, Wuttke DS","authors_abbrev":"Dickey TH et al.","pubmed_publication_date":"08 Jan 2013","pubmed_entrez_date":"2012-12-04","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"4him","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"198-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GGATACGGT)","entry_authors":"Dickey TH,Wuttke DS","entry_authors_abbrev":"Dickey TH et al.","reference_uniquename":"PMID:23201273","experimental_method":"X-ray","resolution":"1.75"},{"pdb_id":"4hid","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"198-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GCTTACGGT)","entry_authors":"Dickey TH,Wuttke DS","entry_authors_abbrev":"Dickey TH et al.","reference_uniquename":"PMID:23201273","experimental_method":"X-ray","resolution":"1.822"},{"pdb_id":"4hj5","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"198-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GGTTTCGGT)","entry_authors":"Dickey TH,Wuttke DS","entry_authors_abbrev":"Dickey TH et al.","reference_uniquename":"PMID:23201273","experimental_method":"X-ray","resolution":"2.04"},{"pdb_id":"4hj9","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"198-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (CGGTTACGGT)","entry_authors":"Dickey TH,Wuttke DS","entry_authors_abbrev":"Dickey TH et al.","reference_uniquename":"PMID:23201273","experimental_method":"X-ray","resolution":"1.85"},{"pdb_id":"4hio","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"198-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GGTAACGGT)","entry_authors":"Dickey TH,McKercher MA,Wuttke DS","entry_authors_abbrev":"Dickey TH et al.","reference_uniquename":"PMID:23201273","experimental_method":"X-ray","resolution":"1.753"},{"pdb_id":"4hik","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"198-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GGTTACGGT)","entry_authors":"Dickey TH,Wuttke DS","entry_authors_abbrev":"Dickey TH et al.","reference_uniquename":"PMID:23201273","experimental_method":"X-ray","resolution":"1.636"},{"pdb_id":"4hja","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"198-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (ACGGTTACGGT)","entry_authors":"Dickey TH,Wuttke DS","entry_authors_abbrev":"Dickey TH et al.","reference_uniquename":"PMID:23201273","experimental_method":"X-ray","resolution":"2.1"},{"pdb_id":"4hj7","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"198-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GGTTAGGGT)","entry_authors":"Dickey TH,Wuttke DS","entry_authors_abbrev":"Dickey TH et al.","reference_uniquename":"PMID:23201273","experimental_method":"X-ray","resolution":"1.783"},{"pdb_id":"4hj8","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"198-339"}],"title":"Crystal Structure of Schizosaccharomyces pombe Pot1pC bound to ssDNA (GGTTACGCT)","entry_authors":"Dickey TH,Wuttke DS","entry_authors_abbrev":"Dickey TH et al.","reference_uniquename":"PMID:23201273","experimental_method":"X-ray","resolution":"2.043"}]},{"uniquename":"PMID:16849325","title":"Degradation of the amyloid beta-protein by the novel mitochondrial peptidasome, PreP.","citation":"J Biol Chem 2006 Sep 29;281(39):29096-104","abstract":"Recently we have identified the novel mitochondrial peptidase responsible for degrading presequences and other short unstructured peptides in mitochondria, the presequence peptidase, which we named PreP peptidasome. In the present study we have identified and characterized the human PreP homologue, hPreP, in brain mitochondria, and we show its capacity to degrade the amyloid beta-protein (Abeta). PreP belongs to the pitrilysin oligopeptidase family M16C containing an inverted zinc-binding motif. We show that hPreP is localized to the mitochondrial matrix. In situ immuno-inactivation studies in human brain mitochondria using anti-hPreP antibodies showed complete inhibition of proteolytic activity against Abeta. We have cloned, overexpressed, and purified recombinant hPreP and its mutant with catalytic base Glu(78) in the inverted zinc-binding motif replaced by Gln. In vitro studies using recombinant hPreP and liquid chromatography nanospray tandem mass spectrometry revealed novel cleavage specificities against Abeta-(1-42), Abeta-(1-40), and Abeta Arctic, a protein that causes increased protofibril formation an early onset familial variant of Alzheimer disease. In contrast to insulin degrading enzyme, which is a functional analogue of hPreP, hPreP does not degrade insulin but does degrade insulin B-chain. Molecular modeling of hPreP based on the crystal structure at 2.1 A resolution of AtPreP allowed us to identify Cys(90) and Cys(527) that form disulfide bridges under oxidized conditions and might be involved in redox regulation of the enzyme. Degradation of the mitochondrial Abeta by hPreP may potentially be of importance in the pathology of Alzheimer disease.","authors":"Falkevall A, Alikhani N, Bhushan S, Pavlov PF, Busch K, Johnson KA, Eneqvist T, Tjernberg L, Ankarcrona M, Glaser E","authors_abbrev":"Falkevall A et al.","pubmed_publication_date":"29 Sep 2006","pubmed_entrez_date":"2006-07-20","publication_year":"2006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3H1.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AF027822","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31132130","title":"Schizosaccharomyces osmophilus sp. nov., an osmophilic fission yeast occurring in bee bread of different solitary bee species.","citation":"FEMS Yeast Res 2019 Jun 01;19(4)","abstract":"Eight yeast strains that asexually reproduce by cell fission were isolated from bee bread of different solitary bees in Germany. DNA sequence analysis revealed that the strains shared the same sequence in the D1/D2 domain of the nuclear large subunit (LSU) rRNA gene with a strain that was previously isolated from a fig snack from Spain. The closest related type strain was that of Schizosaccharomyces octosporus, which showed 98.2% sequence similarity (11 substitutions) with the new strains. By clone sequence analysis of the internal transcribed spacer (ITS) region (ITS1, 5.8S rDNA, and ITS2) a total of nine different copy types were identified. The new strains differed from S. octosporus by approximately 31% in the ITS region. Sequence analysis of the RNAse P gene further supported the description of a new species. The strains isolated during this study show some phenotypic characteristics that separate them from the closest related species, S. octosporus and S. cryophilus. Since all strains showed true osmophily the name of the new species is S. osmophilus (holotype: CBS 15793T; isotype: CLIB 3267 T = NCAIM Y.02225 T, MycoBank no.: MB829586).","doi":"10.1093/femsyr/foz038","authors":"Brysch-Herzberg M, Tobias A, Seidel M, Wittmann R, Wohlmann E, Fischer R, Dlauchy D, Peter G","authors_abbrev":"Brysch-Herzberg M et al.","pubmed_publication_date":"01 Jun 2019","pubmed_entrez_date":"2019-05-28","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.10"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:12746851","title":"Chromate tolerance caused by reduced hydroxyl radical production and decreased glutathione reductase activity in Schizosaccharomyces pombe.","citation":"J Basic Microbiol 2003;43(2):96-103","abstract":"The stable Cr(VI)-tolerant chr1-66T mutant of Schizosaccharomyces pombe, which carries one simple gene mutation responsible for Cr(VI) tolerance, accumulated and reduced the chromate anion (CrO(4)(2-)) significantly more slowly than did its parental strain 6chr(+). The mutant chr1-66T proved to be sensitive to oxidative stressors such as H(2)O(2), menadione, tert-butyl hydroperoxide and Cd(2+). Both the Cr(VI) tolerance and the oxidative stress sensitivity were attributed to a decreased specific glutathione reductase activity. These effects were also enhanced with a decrease in the specific mitochondrial Mn-SOD activity.","authors":"Gazdag Z, Pócsi I, Belágyi J, Emri T, Blaskó A, Takács K, Pesti M","authors_abbrev":"Gazdag Z et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-05-15","publication_year":"2003","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17851138","title":"Turning off the G2 DNA damage checkpoint.","citation":"DNA Repair (Amst) 2008 Feb 01;7(2):136-40","abstract":"In response to DNA damage, cells activate checkpoints to delay cell cycle progression and allow time for completion of DNA repair before commitment to S-phase or mitosis. During G2, many proteins collaborate to activate Chk1, an effector protein kinase that ensures the mitotic cyclin-dependent kinase remains in an inactive state. This checkpoint is ancient in origin and highly conserved from fission yeast to humans. Work from many groups has led to a detailed description of the spatiotemporal control of signaling events leading to Chk1 activation. However, to survive DNA damage in G2, the checkpoint must be inactivated to allow resumption of cell cycling and entry into mitosis. Though only beginning to be understood, here we review current data regarding checkpoint termination signals acting on Chk1 and its' upstream regulators.","authors":"Calonge TM, O'Connell MJ","authors_abbrev":"Calonge TM et al.","pubmed_publication_date":"01 Feb 2008","pubmed_entrez_date":"2007-09-14","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18478529","title":"Heterochromatin tells CENP-A where to go.","citation":"Bioessays 2008 Jun;30(6):526-9","abstract":"The centromere is the region of the chromosome where the kinetochore forms. Kinetochores are the attachment sites for spindle microtubules that separate duplicated chromosomes in mitosis and meiosis. Kinetochore formation depends on a special chromatin structure containing the histone H3 variant CENP-A. The epigenetic mechanisms that maintain CENP-A chromatin throughout the cell cycle have been studied extensively but little is known about the mechanism that targets CENP-A to naked centromeric DNA templates. In a recent report published in Science, such de novo centromere assembly of CENP-A is shown to be dependent on heterochromatin and the RNA interference pathway.","doi":"10.1002/bies.20763","authors":"Durand-Dubief M, Ekwall K","authors_abbrev":"Durand-Dubief M et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-05-15","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9552388","title":"The family of polo-like kinases.","citation":"Prog Cell Cycle Res 1996;2:107-14","abstract":"Here we discuss members of a new family of serine/threonine protein kinases with a likely role in cell cycle control. These kinases are referred to as polo-like kinases, after the prototypic founding member of the family, the polo gene product of Drosophila melanogaster. The polo kinase was originally identified in mutants that display abnormal mitotic spindle organization. Subsequently, potential homologues of Drosophila polo have been identified in yeasts (Cdc5p in Saccharomyces cerevisiae; plo1+ in Schizosaccharmoyces pombe) and in mammals (polo-like kinase 1; Plk1). Genetic and biochemical studies suggest that polo, Cdc5p and plo1+ may be required for mitotic spindle organization and, possibly, for cytokinesis. Likewise, the patterns of expression, activity and subcellular localization of Plk1 strongly suggest that this mammalian kinase functions also during mitosis, possibly in spindle assembly and function. In addition to Plk1, however, more distantly related members of the polo-like kinase family have been identified in mammalian cells, and the available data are consistent with the idea that some of these may act earlier in the cell cycle, possibly during G1. If this hypothesis is correct, different members of the polo-like kinase family would act at several points during the cell cycle, reminiscent of the behaviour of Cdk/cyclin complexes.","authors":"Golsteyn RM, Lane HA, Mundt KE, Arnaud L, Nigg EA","authors_abbrev":"Golsteyn RM et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1272272","title":"Genetic effects of potassium dichromate in Schizosaccharomyces pombe.","citation":"Mutat Res 1976 Apr;38(2):147-50","abstract":"","authors":"Bonatti S, Meini M, Abbondandolo A","authors_abbrev":"Bonatti S et al.","pubmed_publication_date":"Apr 1976","pubmed_entrez_date":"1976-04-01","publication_year":"1976","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11921163","title":"Take five: a myosin class act in fission yeast.","citation":"Cell Motil Cytoskeleton 2002 Feb;51(2):53-6","abstract":"","authors":"Win TZ, Mulvihill DP, Hyams JS","authors_abbrev":"Win TZ et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-03-29","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000072","title":"Representation of chemical homeostasis and cellular chemical homeostasisl as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the homeostasis and cellular homeostasis for a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom templates are \"GO:0048878 and 'regulates level of' some X\" (homeostasis) and \"GO:0055082 and 'regulates level of' some X\" (cellular homeostasis), where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27687092","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-10-04 00:20:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ617312","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.17"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35923846","title":"Uncoupling of Mitosis and Cytokinesis Upon a Prolonged Arrest in Metaphase Is Influenced by Protein Phosphatases and Mitotic Transcription in Fission Yeast.","citation":"Front Cell Dev Biol 2022;10:876810","abstract":"Depletion of the Anaphase-Promoting Complex/Cyclosome (APC/C) activator Cdc20 arrests cells in metaphase with high levels of the mitotic cyclin (Cyclin B) and the Separase inhibitor Securin. In mammalian cells this arrest has been exploited for the treatment of cancer with drugs that engage the spindle assembly checkpoint and, recently, with chemical inhibitors of the APC/C. While most cells arrested in mitosis for prolonged periods undergo apoptosis, others skip cytokinesis and enter G1 with unsegregated chromosomes. This process, known as mitotic slippage, generates aneuploidy and increases genomic instability in the cancer cell. Here, we analyze the behavior of fission yeast cells arrested in mitosis through the transcriptional silencing of the Cdc20 homolog  slp1 . While depletion of  slp1  readily halts cells in metaphase, this arrest is only transient and a majority of cells eventually undergo cytokinesis and show steady mitotic dephosphorylation. Notably, this occurs in the absence of Cyclin B (Cdc13) degradation. We investigate the involvement of phosphatase activity in these events and demonstrate that PP2A-B55 Pab1  is required to prevent septation and, during the arrest, its CDK-mediated inhibition facilitates the induction of cytokinesis. In contrast, deletion of PP2A-B56 Par1  completely abrogates septation. We show that this effect is partly due to this mutant entering mitosis with reduced CDK activity. Interestingly, both PP2A-B55 Pab1  and PP2A-B56 Par1 , as well as Clp1 (the homolog of the budding yeast mitotic phosphatase Cdc14) are required for the dephosphorylation of mitotic substrates during the escape. Finally, we show that the mitotic transcriptional wave controlled by the RFX transcription factor Sak1 facilitates the induction of cytokinesis and also requires the activity of PP2A-B56 Par1  in a mechanism independent of CDK.","doi":"10.3389/fcell.2022.876810","authors":"Chica N, Portantier M, Nyquist-Andersen M, Espada-Burriel S, Lopez-Aviles S","authors_abbrev":"Chica N et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-08-04","publication_year":"2022","canto_session_key":"265f46acc6c2cb72","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-08-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25745419","title":"Recent advances in the genome-wide study of DNA replication origins in yeast.","citation":"Front Microbiol 2015;6:117","abstract":"DNA replication, one of the central events in the cell cycle, is the basis of biological inheritance. In order to be duplicated, a DNA double helix must be opened at defined sites, which are called DNA replication origins (ORIs). Unlike in bacteria, where replication initiates from a single replication origin, multiple origins are utilized in the eukaryotic genomes. Among them, the ORIs in budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe have been best characterized. In recent years, advances in DNA microarray and next-generation sequencing technologies have increased the number of yeast species involved in ORIs research dramatically. The ORIs in some non-conventional yeast species such as Kluyveromyces lactis and Pichia pastoris have also been genome-widely identified. Relevant databases of replication origins in yeast were constructed, then the comparative genomic analysis can be carried out. Here, we review several experimental approaches that have been used to map replication origins in yeast and some of the available web resources related to yeast ORIs. We also discuss the sequence characteristics and chromosome structures of ORIs in the four yeast species, which can be utilized to improve yeast replication origins prediction.","doi":"10.3389/fmicb.2015.00117","authors":"Peng C, Luo H, Zhang X, Gao F","authors_abbrev":"Peng C et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-07","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-03-08 01:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19898524","title":"Protection and replication of telomeres in fission yeast.","citation":"Biochem Cell Biol 2009 Oct;87(5):747-58","abstract":"Telomeres, the natural ends of linear chromosomes, must be protected and completely replicated to guarantee genomic stability in eukaryotic cells. However, the protected state of telomeres is not compatible with recruitment of telomerase, an enzyme responsible for extending telomeric G-rich repeats during S-phase; thus, telomeres must undergo switches from a protected state to an accessible state during the cell cycle. In this minireview, we will summarize recent advances in our understanding of proteins involved in the protection and replication of telomeres, and the way these factors are dynamically recruited to telomeres during the cell cycle. We will focus mainly on recent results from fission yeast Schizosaccharomyces pombe, and compare them with results from budding yeast Saccharomyces cerevisiae and mammalian cell studies. In addition, a model for the way in which fission yeast cells replicate telomeres will be presented.","doi":"10.1139/O09-037","authors":"Moser BA, Nakamura TM","authors_abbrev":"Moser BA et al.","pubmed_publication_date":"Oct 2009","pubmed_entrez_date":"2009-11-10","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26941334","title":"Unique spatiotemporal activation pattern of Cdc42 by Gef1 and Scd1 promotes different events during cytokinesis.","citation":"Mol Biol Cell 2016 Apr 15;27(8):1235-45","abstract":"The Rho-family GTPase Cdc42 regulates cell polarity and localizes to the cell division site. Cdc42 is activated by guanine nucleotide exchange factors (GEFs). We report that Cdc42 promotes cytokinesis via a unique spatiotemporal activation pattern due to the distinct action of its GEFs, Gef1 and Scd1, in fission yeast. Before cytokinetic ring constriction, Cdc42 activation, is Gef1 dependent, and after ring constriction, it is Scd1 dependent. Gef1 localizes to the actomyosin ring immediately after ring assembly and promotes timely onset of ring constriction. Gef1 is required for proper actin organization during cytokinesis, distribution of type V myosin Myo52 to the division site, and timely recruitment of septum protein Bgs1. In contrast, Scd1 localizes to the broader region of ingressing membrane during cytokinetic furrowing. Scd1 promotes normal septum formation, andscd1Δcells display aberrant septa with reduced Bgs1 localization. Thus we define unique roles of the GEFs Gef1 and Scd1 in the regulation of distinct events during cytokinesis. Gef1 localizes first to the cytokinetic ring and promotes timely constriction, whereas Scd1 localizes later to the ingressing membrane and promotes septum formation. Our findings are consistent with reports that complexity in GTPase signaling patterns enables exquisite precision over the control of cellular processes.","doi":"10.1091/mbc.E15-10-0700","authors":"Wei B, Hercyk BS, Mattson N, Mohammadi A, Rich J, DeBruyne E, Clark MM, Das M","authors_abbrev":"Wei B et al.","pubmed_publication_date":"15 Apr 2016","pubmed_entrez_date":"2016-03-05","publication_year":"2016","canto_session_key":"e02ca2efe2171cda","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maitreyi Das","canto_first_approved_date":"2017-06-14 12:40:49","canto_approved_date":"2021-11-24 20:14:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-03 15:14:23","canto_added_date":"2016-03-06 01:15:14","annotation_curators":[{"name":"Maitreyi Das","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":41,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.03","SPAC1F5.04c","SPAC20G8.05c","SPCC645.05c","SPAC24H6.09","SPAC4F8.13c","SPCC1840.02c","SPAC16E8.09","SPAC110.03","SPBC19G7.05c","SPCC895.05","SPCC1919.10c"],"gene_count":12,"ltp_gene_count":4,"approved_date":"2017-06-14"},{"uniquename":"PMID:11461899","title":"Isolation of a novel gene from Schizosaccharomyces pombe: stm1+ encoding a seven-transmembrane loop protein that may couple with the heterotrimeric Galpha 2 protein, Gpa2.","citation":"J Biol Chem 2001 Oct 26;276(43):40190-201","abstract":"A putative seven transmembrane protein gene, stm1(+), which is required for proper recognition of nitrogen starvation signals, was isolated as a multicopy suppressor of a ras1 synthetic lethal mutant in Schizosaccharomyces pombe. Under nitrogen-deficient conditions, transcription of the stm1 gene was induced; deletion of stm1 was associated with early entry into G(1) arrest. Under nutritionally sufficient conditions, overexpression of Stm1 inhibited vegetative cell growth, resulted in decreased intracellular cAMP levels, increased the expression of the meiosis-specific genes ste11, mei2, and mam2, and facilitated sexual development in homothallic cells. However inhibition of vegetative cell growth and reduction of cAMP levels were not observed in a deletion mutant of the heterotrimeric G protein Galpha2 gene, gpa2, that is responsible for regulating intracellular cAMP levels, a key factor in determining the sexual development in S. pombe. Stm1 protein was shown to interact with Gpa2 through its C-terminal transmembrane domains 5-7. Mutation at Lys(199) in the C-terminal domain (stm1(K199A)) abolished the Stm1 overexpression effect on lowering cAMP levels. Induction of ste11, a meiosis-specific gene transcription factor, by Stm1 overexpression was enhanced in gpa2-deleted cells but was absent in a deletion mutant of sty1, a key protein kinase that links mitotic control with environmental signals and induces stress-responsive genes. Moreover, deletion of both stm1 and ras1 caused delayed entry into G(1) arrest in S. pombe when the cells were grown in a nitrogen-deficient medium. Thus we consider that the stm1 gene can function through Gpa2-dependent and/or -independent pathways and may play a role in providing the prerequisite state for entering the pheromone-dependent differentiation cycle in which heterotrimeric Galpha1 protein, Gpa1, and Ras1 play major roles. Stm1 could function as a sentinel molecule sensing the nutritional state of the cells, stopping the proliferative cell cycle, and preparing the cell to enter meiosis under nutritionally deficient conditions.","authors":"Chung KS, Won M, Lee SB, Jang YJ, Hoe KL, Kim DU, Lee JW, Kim KW, Yoo HS","authors_abbrev":"Chung KS et al.","pubmed_publication_date":"26 Oct 2001","pubmed_entrez_date":"2001-07-20","publication_year":"2001","canto_session_key":"4c58cb4b9203cd31","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-07 14:28:28","canto_approved_date":"2021-10-21 17:44:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-02 23:22:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11H11.04","SPCC285.09c","SPBC24C6.06","SPAC24B11.06c","SPAC17H9.09c","SPAC23H3.13c","SPAC17C9.10"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-03-07"},{"uniquename":"PMID:16502473","title":"Nonribosomal peptide synthesis in Schizosaccharomyces pombe and the architectures of ferrichrome-type siderophore synthetases in fungi.","citation":"Chembiochem 2006 Apr;7(4):612-22","abstract":"A nonribosomal peptide synthetase (NRPS) in Schizosaccharomyces pombe, which possesses an unusual structure incorporating three adenylation domains, six thiolation domains and six condensation domains, has been shown to produce the cyclohexapeptide siderophore ferrichrome. One of the adenylation domains is truncated and contains a distorted key motif. Substrate-binding specificities of the remaining two domains were assigned by molecular modelling to glycine and to N-acetyl-N-hydroxy-L-ornithine. Hexapeptide siderophore synthetase genes of Magnaporthe grisea and Fusarium graminearum were both identified and analyzed with respect to substrate-binding sites, and the predicted product ferricrocin was identified in each. A comparative analysis of these synthetase systems, including those of the basidiomycete Ustilago maydis, the homobasidiomycete Omphalotus olearius and the ascomycetes Aspergillus nidulans, Aspergillus fumigatus, Fusarium graminearum, Cochliobolus heterostrophus, Neurospora crassa and Aureobasidium pullulans, revealed divergent domain compositions with respect to their number and positioning, although all produce similar products by iterative processes. A phylogenetic analysis of both NRPSs and associated L-N5-ornithine monooxygenases revealed that ferrichrome-type siderophore biosynthesis has coevolved in fungi with varying in trans interactions of NRPS domains.","authors":"Schwecke T, Göttling K, Durek P, Dueñas I, Käufer NF, Zock-Emmenthal S, Staub E, Neuhof T, Dieckmann R, von Döhren H","authors_abbrev":"Schwecke T et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-02-28","publication_year":"2006","canto_session_key":"dad3b136d74916c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-01 14:43:27","canto_approved_date":"2025-09-29 17:12:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-01 14:38:54","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23G3.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-01"},{"uniquename":"PMID:876029","title":"Extrachromosomal inheritance in Schizosaccharomyces pombe. III. Isolation and characterization of paromomycin-resistant mutants.","citation":"Mol Gen Genet 1977 Apr 29;152(3):319-24","abstract":"In the antimycin--resistant mutant anar-8 of the fission yeast Schizosaccharomyces pombe (Sch.p.) spontaneous mutants were isolated showing high resistance to the aminoglycoside antibiotic paromomycin. All mutants were resistant to the structurally related antibiotic neomycin. Tetrad analysis, mitotic segregation analysis, and mitotic haploidization revealed extrachromosomal, very likely mitochondrial inheritance. In contrast to the rapid segregation of mitochondrial markers in zygotic clones of Saccharomyces cerevisiae (S.c.) the heteroplasmic state of diploids proved to persist for at least 50 generations after zygote formation. Stationary cultures of the paromomycin-resistant mutants parr-106 and parr-112 contain up to 6% respiratory-deficient mutants, but no reversion to paromomycin-sensitivity was observed among 1700-1800 colonies tested. The ability of mutant anar-8 to produce spontaneously respiratory-deficient mutants could be separated from the antimycin-resistant phenotype of anar-8.","authors":"Del Giudice L, Wolf K, Seitz G, Burger G, Lang B, Kaudewitz F","authors_abbrev":"Del Giudice L et al.","pubmed_publication_date":"29 Apr 1977","pubmed_entrez_date":"1977-04-29","publication_year":"1977","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17472966","title":"Role of the synthase domain of Ags1p in cell wall alpha-glucan biosynthesis in fission yeast.","citation":"J Biol Chem 2007 Jun 29;282(26):18969-79","abstract":"The cell wall is important for maintenance of the structural integrity and morphology of fungal cells. Besides beta-glucan and chitin, alpha-glucan is a major polysaccharide in the cell wall of many fungi. In the fission yeast Schizosaccharomyces pombe, cell wall alpha-glucan is an essential component, consisting mainly of (1,3)-alpha-glucan with approximately 10% (1,4)-linked alpha-glucose residues. The multidomain protein Ags1p is required for alpha-glucan biosynthesis and is conserved among cell wall alpha-glucan-containing fungi. One of its domains shares amino acid sequence motifs with (1,4)-alpha-glucan synthases such as bacterial glycogen synthases and plant starch synthases. Whether Ags1p is involved in the synthesis of the (1,4)-alpha-glucan constituent of cell wall alpha-glucan had remained unclear. Here, we show that overexpression of Ags1p in S. pombe cells results in accumulation of (1,4)-alpha-glucan. To determine whether the synthase domain of Ags1p is responsible for this activity, we overexpressed Ags1p-E1526A, which carries a mutation in a putative catalytic residue of the synthase domain, but observed no accumulation of (1,4)-alpha-glucan. Compared with wild-type Ags1p, this mutant Ags1p showed a markedly reduced ability to complement the cell lysis phenotype of the temperature-sensitive ags1-1 mutant. Therefore, we conclude that, in S. pombe, the production of (1,4)-alpha-glucan by the synthase domain of Ags1p is important for the biosynthesis of cell wall alpha-glucan.","authors":"Vos A, Dekker N, Distel B, Leunissen JA, Hochstenbach F","authors_abbrev":"Vos A et al.","pubmed_publication_date":"29 Jun 2007","pubmed_entrez_date":"2007-05-03","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1281.01"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:12509234","title":"Inactivation of homologous recombination suppresses defects in topoisomerase III-deficient mutants.","citation":"DNA Repair (Amst) 2002 Jun 21;1(6):463-82","abstract":"The Saccharomyces cerevisiae TOP3 gene encodes the type IA topoisomerase (Top3p) that is highly conserved in evolution. Deletion of TOP3 leads to a reduction in cell viability, hyper-recombination between repetitive DNA sequences, and abnormalities in both cell cycle progression and responses to DNA damaging agents. Deletion of SGS1, encoding the sole RecQ family helicase in S. cerevisiae, strongly suppresses the phenotypic effects of loss of TOP3 function. Here, we show that many of the adverse phenotypic effects of TOP3 deletion can also be partially alleviated by disruption of homologous recombination (HR) functions. This genetic interaction is seen both in strains deleted for TOP3 and in wild-type strains over-expressing a dominant-negative Top3p mutant form that confers a top3-like phenotype. Moreover, we show that this genetic interaction is conserved in the distantly-related fission yeast, Schizosaccharomyces pombe. Our results implicate topoisomerase III enzymes in recombination repair events required for cellular protection against DNA damaging agents and DNA replication inhibitors.","authors":"Oakley TJ, Goodwin A, Chakraverty RK, Hickson ID","authors_abbrev":"Oakley TJ et al.","pubmed_publication_date":"21 Jun 2002","pubmed_entrez_date":"2003-01-02","publication_year":"2002","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPBC16G5.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:1735122","title":"Gene database for the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1992 Jan;21(1):1-11","abstract":"As an aid to the fission yeast genome project, we describe a database for Schizosaccharomyces pombe consisting of both genetic and physical information. As presented, it is therefore both an updated gene list of all the nuclear genes of the fission yeast, and provides an estimate of the physical distance between two mapped genes. Additionally, a field indicates whether the sequence of the gene is available. Currently, sequence information is available for 135 of the 501 known genes.","authors":"Lennon GG, Lehrach H","authors_abbrev":"Lennon GG et al.","pubmed_publication_date":"Jan 1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30373637","title":"Chromatin-mediated regulators of meiotic recombination revealed by proteomics of a recombination hotspot.","citation":"Epigenetics Chromatin 2018 Oct 29;11(1):64","abstract":"Meiotic recombination hotspots control the frequency and distribution of Spo11 (Rec12)-initiated recombination in the genome. Recombination occurs within and is regulated in part by chromatin structure, but relatively few of the many chromatin remodeling factors and histone posttranslational modifications (PTMs) have been interrogated for a role in the process.\nWe developed a chromatin affinity purification and mass spectrometry-based approach to identify proteins and histone PTMs that regulate recombination hotspots. Small (4.2 kbp) minichromosomes (MiniCs) bearing the fission yeast ade6-M26 hotspot or a basal recombination control were purified approximately 100,000-fold under native conditions from meiosis; then, associated proteins and histone PTMs were identified by mass spectrometry. Proteins and PTMs enriched at the hotspot included known regulators (Atf1, Pcr1, Mst2, Snf22, H3K14ac), validating the approach. The abundance of individual histones varied dynamically during meiotic progression in hotspot versus basal control MiniCs, as did a subset of 34 different histone PTMs, implicating these as potential regulators. Measurements of basal and hotspot recombination in null mutants confirmed that additional, hotspot-enriched proteins are bona fide regulators of hotspot activation within the genome. These chromatin-mediated regulators include histone H2A-H2B and H3-H4 chaperones (Nap1, Hip1/Hir1), subunits of the Ino80 complex (Arp5, Arp8), a DNA helicase/E3 ubiquitin ligase (Rrp2), components of a Swi2/Snf2 family remodeling complex (Swr1, Swc2), and a nucleosome evictor (Fft3/Fun30).\nOverall, our findings indicate that a remarkably diverse collection of chromatin remodeling factors and histone PTMs participate in designating where meiotic recombination occurs in the genome, and they provide new insight into molecular mechanisms of the process.","doi":"10.1186/s13072-018-0233-x","authors":"Storey AJ, Wang HP, Protacio RU, Davidson MK, Tackett AJ, Wahls WP","authors_abbrev":"Storey AJ et al.","pubmed_publication_date":"29 Oct 2018","pubmed_entrez_date":"2018-10-31","publication_year":"2018","canto_session_key":"23b11c4c25c0af07","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Wayne Wahls","canto_first_approved_date":"2020-02-19 16:31:41","canto_approved_date":"2020-02-19 16:31:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-02-06 21:43:19","canto_added_date":"2018-11-01 01:15:04","annotation_curators":[{"name":"Wayne Wahls","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31F10.13c","SPBC365.10","SPBC23E6.02","SPCC364.06","SPAC664.02c","SPAC25A8.01c","SPBP35G2.13c","SPAC11E3.01c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2020-02-19"},{"uniquename":"PMID:11094289","title":"Role for trehalase during germination of spores in the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 2000 Dec 01;193(1):117-21","abstract":"Spores from Schizosaccharomyces pombe contain neutral and acid trehalases. When spores from strains disrupted for ntp1(+), which encodes neutral trehalase, were induced to germinate, the onset of the process was markedly delayed as compared to wild-type spores. Further outgrowth was also reduced. Dormant spores lacking neutral trehalase contained twice the amount of trehalose present in wild-type spores and mobilised the intracellular pool of trehalose at a slower rate during germination. Inhibition by phloridzin of the sporulation-specific acid trehalase in ntp1-disrupted spores arrested germination completely while prompting no effect on wild-type spores. These results suggest that the two trehalase enzymes may support the utilisation of trehalose during germination but neutral trehalase is required for a more rapid and efficient process.","authors":"Beltran FF, Castillo R, Vicente-Soler J, Cansado J, Gacto M","authors_abbrev":"Beltran FF et al.","pubmed_publication_date":"01 Dec 2000","pubmed_entrez_date":"2000-11-30","publication_year":"2000","canto_session_key":"737c54a01a088432","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-09-20 13:37:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 09:48:40","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-20"},{"uniquename":"PMID:7689163","title":"Cellular recovery, DNA repair and mutagenesis--a tale of two yeasts.","citation":"Mutat Res 1993 Sep;289(1):55-60","abstract":"In studies related to recovery and repair mechanisms following DNA damage, one problem that has been frequently addressed concerns the effects of DNA repair on both spontaneous and induced mutagenesis. Among the eukaryotic organisms which served as unique and valuable systems for investigating this problem are the two yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe. With the basic genetics well worked out in both, these yeasts have provided the experimental tools for comparative analysis of mechanisms of DNA repair which show a great deal of diversity between the two unicellular eukaryotes. Since the present issue focuses on the contributions of R.H. Haynes to the area of DNA repair and mutagenesis, we have chosen to discuss those specific aspects of our studies which are directly or indirectly related to or influenced by his research in this field. These include: (i) liquid holding recovery, (ii) production of two strand mutations and the concept of heteroduplex repair, and (iii) understanding of pathways of repair through construction of supersensitive mutants in yeast.","authors":"Nasim A, Hannan MA","authors_abbrev":"Nasim A et al.","pubmed_publication_date":"Sep 1993","pubmed_entrez_date":"1993-09-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21992435","title":"Nuclear roles and regulation of chromatin structure by the stress-dependent MAP kinase Sty1 of Schizosaccharomyces pombe.","citation":"Mol Microbiol 2011 Nov;82(3):542-54","abstract":"Microorganisms are invariably exposed to abrupt changes in their environment, and consequently display robust, high plasticity gene programmes to respond to stresses. In fission yeast, the Sty1 pathway is activated in response to diverse stress conditions, such as osmotic and oxidative stress, heat shock or nitrogen deprivation. The MAP kinase Sty1 and its substrate, the transcription factor Atf1, regulate diverse processes mainly at the nucleus. For instance, Sty1, Atf1 and its heterodimeric partner Pcr1 participate in promoting recombination at some hot spots, and in the assembly of heterochromatin at the mating locus. Their main role, however, is to engage a wide gene expression programme aimed to allow cellular survival by decreasing and repairing the damage exerted. Once Sty1 and Atf1 are activated by stress, they are recruited to promoters of up to 5-10% of the coding genes and regulate their transcription. Even though there is no simple, global relationship establishing RNA polymerase II occupancy, nucleosome architecture and transcriptional activity in eukaryotes, we discuss within this review the current knowledge and future perspectives of how activation of Sty1 and Atf1 affect chromatin architecture of a large fraction of the Schizosaccharomyces pombe genome to trigger the cellular response to environmental stress.","doi":"10.1111/j.1365-2958.2011.07851.x","authors":"Sansó M, Vargas-Pérez I, García P, Ayté J, Hidalgo E","authors_abbrev":"Sansó M et al.","pubmed_publication_date":"Nov 2011","pubmed_entrez_date":"2011-10-14","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25799503","title":"Comparative 3D genome structure analysis of the fission and the budding yeast.","citation":"PLoS One 2015;10(3):e0119672","abstract":"We studied the 3D structural organization of the fission yeast genome, which emerges from the tethering of heterochromatic regions in otherwise randomly configured chromosomes represented as flexible polymer chains in an nuclear environment. This model is sufficient to explain in a statistical manner many experimentally determined distinctive features of the fission yeast genome, including chromatin interaction patterns from Hi-C experiments and the co-locations of functionally related and co-expressed genes, such as genes expressed by Pol-III. Our findings demonstrate that some previously described structure-function correlations can be explained as a consequence of random chromatin collisions driven by a few geometric constraints (mainly due to centromere-SPB and telomere-NE tethering) combined with the specific gene locations in the chromosome sequence. We also performed a comparative analysis between the fission and budding yeast genome structures, for which we previously detected a similar organizing principle. However, due to the different chromosome sizes and numbers, substantial differences are observed in the 3D structural genome organization between the two species, most notably in the nuclear locations of orthologous genes, and the extent of nuclear territories for genes and chromosomes. However, despite those differences, remarkably, functional similarities are maintained, which is evident when comparing spatial clustering of functionally related genes in both yeasts. Functionally related genes show a similar spatial clustering behavior in both yeasts, even though their nuclear locations are largely different between the yeast species.","doi":"10.1371/journal.pone.0119672","authors":"Gong K, Tjong H, Zhou XJ, Alber F","authors_abbrev":"Gong K et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-24","publication_year":"2015","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2015-03-25 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11997110","title":"A second stress-inducible glutathione S-transferase gene from Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2002 Apr 12;1574(3):399-402","abstract":"A second glutathione S-transferase gene (GST II) was isolated from the chromosomal DNA of the fission yeast Schizosaccharomyces pombe. The nucleotide sequence determined contains 1908 bp including an open reading frame of 230 amino acids that would encode a protein of a molecular mass of 26843.4 Da. The amino acid sequence of the putative GST II is very homologous with that of the previously isolated GST gene (GST I) located in the same chromosome III of S. pombe. The cloned GST II gene produces the functional GST in S. pombe, and it gives much higher GST in the stationary phase than in the exponential phase. Regulation of the GST II gene was studied using the GST II-lacZ fusion. The synthesis of beta-galactosidase from the fusion plasmid is greatly enhanced by the treatments with oxidative stresses such as menadione and mercuric chloride. It is also induced by o-dinitrobenzene, one of the GST substrates. NO-generating S-nitroso-N-acetylpenicillamine has a weak induction effect on the expression of GST II gene. These results indicate that the S. pombe GST II gene is involved in the oxidative stress response and detoxification. However, physiological meaning on the existence of the two similar GST genes in S. pombe remains unknown yet.","authors":"Cho YW, Park EH, Fuchs JA, Lim CJ","authors_abbrev":"Cho YW et al.","pubmed_publication_date":"12 Apr 2002","pubmed_entrez_date":"2002-05-09","publication_year":"2002","canto_session_key":"1a3a61ac4022e976","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:54:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 14:49:26","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC965.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-05"},{"uniquename":"PMID:21118717","title":"Use of a Schizosaccharomyces pombe PKA-repressible reporter to study cGMP metabolising phosphodiesterases.","citation":"Cell Signal 2011 Mar;23(3):594-601","abstract":"The Schizosaccharomyces pombe fbp1 gene is transcriptionally repressed by protein kinase A (PKA) that is activated by extracellular glucose via a cAMP-signaling pathway. We previously used an fbp1-ura4 reporter that places uracil biosynthesis under the control of the glucose-sensing pathway to identify mutations in genes of the cAMP pathway. More recently, this reporter has been used in high throughput screens for small molecule inhibitors of heterologously-expressed cyclic nucleotide phosphodiesterases (PDEs) that hydrolyse cAMP to 5' AMP. Here we show that strains lacking the adenylyl cyclase gene respond to either exogenous cAMP or cGMP to activate PKA, thus regulating fbp1-ura4 expression and other PKA-regulated processes such as conjugation and the nuclear export of an Rst2-GFP fusion protein. Expression of cGMP-specific PDEs or ones that hydrolyse both cAMP and cGMP increases the amount of exogenous cGMP required to activate PKA in order to repress fbp1-ura4 expression, creating conditions that allow detection of inhibitors of these PDEs. As proof of this concept, we screened a collection of compounds previously identified as inhibitors of cAMP-specific PDE4 or PDE7 enzymes for their ability to inhibit the mammalian cGMP-specific PDE5A enzyme. We identified compound BC76, which inhibits PDE5A in an in vitro enzyme assay with an IC(50) of 232nM. Further yeast-based assays show that BC76 inhibits PDE1, PDE4, PDE5, PDE8, PDE10 and PDE11, thus demonstrating the utility of this system for detecting and characterising inhibitors of either cAMP- or cGMP-metabolising PDEs.","doi":"10.1016/j.cellsig.2010.11.013","authors":"Demirbas D, Ceyhan O, Wyman AR, Ivey FD, Allain C, Wang L, Sharuk MN, Francis SH, Hoffman CS","authors_abbrev":"Demirbas D et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2010-12-02","publication_year":"2011","canto_session_key":"0d638c12aef4db07","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Charlie Hoffman","canto_first_approved_date":"2018-06-10 19:44:45","canto_approved_date":"2023-04-20 11:49:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-02 11:30:57","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Charlie Hoffman","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.02","SPBC19C7.03","SPCC285.09c","SPAC8C9.03"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-06-10"},{"uniquename":"PMID:9450932","title":"S-phase-specific activation of Cds1 kinase defines a subpathway of the checkpoint response in Schizosaccharomyces pombe.","citation":"Genes Dev 1998 Feb 01;12(3):382-95","abstract":"Checkpoints that respond to DNA structure changes were originally defined by the inability of yeast mutants to prevent mitosis following DNA damage or S-phase arrest. Genetic analysis has subsequently identified subpathways of the DNA structure checkpoints, including the reversible arrest of DNA synthesis. Here, we show that the Cds1 kinase is required to slow S phase in the presence of DNA-damaging agents. Cds1 is phosphorylated and activated by S-phase arrest and activated by DNA damage during S phase, but not during G1 or G2. Activation of Cds1 during S phase is dependent on all six checkpoint Rad proteins, and Cds1 interacts both genetically and physically with Rad26. Unlike its Saccharomyces cerevisiae counterpart Rad53, Cds1 is not required for the mitotic arrest checkpoints and, thus, defines an S-phase specific subpathway of the checkpoint response. We propose a model for the DNA structure checkpoints that offers a new perspective on the function of the DNA structure checkpoint proteins. This model suggests that an intrinsic mechanism linking S phase and mitosis may function independently of the known checkpoint proteins.","authors":"Lindsay HD, Griffiths DJ, Edwards RJ, Christensen PU, Murray JM, Osman F, Walworth N, Carr AM","authors_abbrev":"Lindsay HD et al.","pubmed_publication_date":"01 Feb 1998","pubmed_entrez_date":"1998-02-28","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC9E9.08"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:2078550","title":"Centromere structure and function in budding and fission yeasts.","citation":"New Biol 1990 Jan;2(1):10-9","abstract":"Functional centromeric DNAs have now been isolated and characterized from both budding (Saccharomyces cerevisiae) and fission (Schizosaccharomyces pombe) yeasts. Artificial chromosomes containing these centromere DNA sequences segregate faithfully in both mitotic and meiotic cell divisions, but only in the parent organism. Structure-function analyses have revealed surprising fundamental differences between these two centromere classes. In the budding yeast centromeres, a 125-bp consensus DNA sequence contains all the information needed in cis to provide proper chromosome segregation. In contrast, the fission yeast centromeres each contain a long run (40 to 100 kb) of untranscribed repetitive DNA sequences arranged into a large inverted repeat, most of which is required for full centromere function. The fission yeast centromere-kinetochore appears to be a highly relevant experimental model for analysis of the mechanism of chromosome segregation in higher eukaryotes, in which the centromere regions often contain megabases of transcriptionally silent repetitive DNA sequences of unknown function.","authors":"Carbon J, Clarke L","authors_abbrev":"Carbon J et al.","pubmed_publication_date":"Jan 1990","pubmed_entrez_date":"1990-01-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9658174","title":"Multiple domains of fission yeast Cdc19p (MCM2) are required for its association with the core MCM complex.","citation":"Mol Biol Cell 1998 Jul;9(7):1833-45","abstract":"The members of the MCM protein family are essential eukaryotic DNA replication factors that form a six-member protein complex. In this study, we use antibodies to four MCM proteins to investigate the structure of and requirements for the formation of fission yeast MCM complexes in vivo, with particular regard to Cdc19p (MCM2). Gel filtration analysis shows that the MCM protein complexes are unstable and can be broken down to subcomplexes. Using coimmunoprecipitation, we find that Mis5p (MCM6) and Cdc21p (MCM4) are tightly associated with one another in a core complex with which Cdc19p loosely associates. Assembly of Cdc19p with the core depends upon Cdc21p. Interestingly, there is no obvious change in Cdc19p-containing MCM complexes through the cell cycle. Using a panel of Cdc19p mutants, we find that multiple domains of Cdc19p are required for MCM binding. These studies indicate that MCM complexes in fission yeast have distinct substructures, which may be relevant for function.","authors":"Sherman DA, Pasion SG, Forsburg SL","authors_abbrev":"Sherman DA et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-07-11","publication_year":"1998","canto_session_key":"073951bf43ce4011","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-08-07 08:52:42","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-26 18:30:33","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":86,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPBC4.04c","SPBC211.04c","SPCC16A11.17"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2013-02-26"},{"uniquename":"PMID:25416816","title":"Multiple layers of regulation influence cell integrity control by the PKC ortholog Pck2 in fission yeast.","citation":"J Cell Sci 2015 Jan 15;128(2):266-80","abstract":"The fission yeast protein kinase C (PKC) ortholog Pck2 controls cell wall synthesis and is a major upstream activator of the cell integrity pathway (CIP) and its core component, the MAP kinase Pmk1 (also known as Spm1), in response to environmental stimuli. We show that in vivo phosphorylation of Pck2 at the conserved T842 activation loop during growth and in response to different stresses is mediated by the phosphoinositide-dependent kinase (PDK) ortholog Ksg1 and an autophosphorylation mechanism. However, T842 phosphorylation is not essential for Pmk1 activation, and putative phosphorylation at T846 might play an additional role in Pck2 catalytic activation and downstream signaling. These events, together with turn motif autophosphorylation at T984 and binding to small GTPases Rho1 and/or Rho2, stabilize Pck2 and render it competent to exert its biological functions. Remarkably, the target of rapamycin complex 2 (TORC2) does not participate in the catalytic activation of Pck2, but instead contributes to de novo Pck2 synthesis, which is essential to activate the CIP in response to cell wall damage or glucose exhaustion. These results unveil a novel mechanism whereby TOR regulates PKC function at a translational level, and they add a new regulatory layer to MAPK signaling cascades.","doi":"10.1242/jcs.158295","authors":"Madrid M, Jiménez R, Sánchez-Mir L, Soto T, Franco A, Vicente-Soler J, Gacto M, Pérez P, Cansado J","authors_abbrev":"Madrid M et al.","pubmed_publication_date":"15 Jan 2015","pubmed_entrez_date":"2014-11-23","publication_year":"2015","canto_session_key":"27e00ac6f1e1dbac","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-11-26 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G8.14c","SPCC576.15c","SPBC12D12.04c","SPBC30D10.10c","SPBC119.08"],"gene_count":5,"ltp_gene_count":4},{"uniquename":"PMID:8488276","title":"[Fission yeast cDNA project].","citation":"Tanpakushitsu Kakusan Koso 1993 Feb;38(3):429-33","abstract":"","authors":"Okayama H","authors_abbrev":"Okayama H","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11577719","title":"Production of pyridoxal phosphate by a mutant strain of Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2001 Aug;65(8):1789-95","abstract":"Conditions for extracellular production of vitamin B6 compounds (B6), especially pyridoxal 5'-phosphate (PLP) by Schizosaccharomyces pombe leul strain were examined. The productivity was dependent on concentration of L-leucine in the culture medium: 30 mg/l gave the highest concentrations of total B6 and PLP. The viable cells harvested at different growth phases showed different productivity: middle and late exponential phase cells showed the highest productivity of total B6 and PLP, respectively. D-Glucose (1%, w/v) among other sugars gave the best productivity. Supplementation of air and ammonium sulfate significantly increased extracellular production of PLP. Superoxide anion producers, menadione and plumbagin, and H202 increased the productivity of PLP. Cycloheximide inhibited the increase of PLP by the oxidative stress and, in contrast, increased pyridoxine.","authors":"Chumnantana R, Hirose K, Baba H, Yagi T","authors_abbrev":"Chumnantana R et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-10-02","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39746995","title":"DSIF factor Spt5 coordinates transcription, maturation and exoribonucleolysis of RNA polymerase II transcripts.","citation":"Nat Commun 2025 Jan 02;16(1):10","abstract":"Precursor messenger RNA (pre-mRNA) is processed into its functional form during RNA polymerase II (Pol II) transcription. Although functional coupling between transcription and pre-mRNA processing is established, the underlying mechanisms are not fully understood. We show that the key transcription termination factor, RNA exonuclease Xrn2 engages with Pol II forming a stable complex. Xrn2 activity is stimulated by Spt5 to ensure efficient degradation of nascent RNA leading to Pol II dislodgement from DNA. Our results support a model where Xrn2 first forms a stable complex with the elongating Pol II to achieve its full activity in degrading nascent RNA revising the current 'torpedo' model of termination, which posits that RNA degradation precedes Xrn2 engagement with Pol II. Spt5 is also a key factor that attenuates the expression of non-coding transcripts, coordinates pre-mRNA splicing and 3'-end processing. Our findings indicate that engagement with the transcribing Pol II is an essential regulatory step modulating the activity of RNA enzymes such as Xrn2, thus advancing our understanding of how RNA maturation is controlled during transcription.","doi":"10.1038/s41467-024-55063-7","authors":"Kuś K, Carrique L, Kecman T, Fournier M, Hassanein SS, Aydin E, Kilchert C, Grimes JM, Vasiljeva L","authors_abbrev":"Kuś K et al.","pubmed_publication_date":"02 Jan 2025","pubmed_entrez_date":"2025-01-02","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1020.04c","SPAC3A12.07","SPAPYUG7.04c","SPBC19C2.03","SPAC23C4.15","SPBC14C8.12","SPAC23C4.19","SPCC1442.10c","SPAC1B3.12c","SPACUNK4.06c","SPBC28F2.12","SPAC26A3.12c","SPAC23G3.01"],"gene_count":13,"ltp_gene_count":13,"pdb_entries":[{"pdb_id":"8qsz","gene_chains":[{"gene_uniquename":"SPAC1B3.12c","chain":"J","position":"1-71"},{"gene_uniquename":"SPAC23C4.19","chain":"Y","position":"1-990"},{"gene_uniquename":"SPACUNK4.06c","chain":"G","position":"1-172"},{"gene_uniquename":"SPAPYUG7.04c","chain":"I","position":"1-113"},{"gene_uniquename":"SPBC28F2.12","chain":"A","position":"1-1752"},{"gene_uniquename":"SPCC1020.04c","chain":"F","position":"1-142"},{"gene_uniquename":"SPCC1442.10c","chain":"C","position":"1-297"},{"gene_uniquename":"SPAC26A3.12c","chain":"X","position":"1-893"},{"gene_uniquename":"SPBC19C2.03","chain":"L","position":"1-63"},{"gene_uniquename":"SPAC3A12.07","chain":"K","position":"1-123"},{"gene_uniquename":"SPAC23G3.01","chain":"B","position":"1-1210"},{"gene_uniquename":"SPAC23C4.15","chain":"E","position":"1-210"},{"gene_uniquename":"SPBC14C8.12","chain":"H","position":"1-125"}],"title":"Structure of s. pombe RNA polymerase II in complex with DSIF and Rat1/Rai1","entry_authors":"Carrique L,Kus K,Vasiljeva L,Grimes JM","entry_authors_abbrev":"Carrique L et al.","reference_uniquename":"PMID:39746995","experimental_method":"EM","resolution":"2.67"}]},{"uniquename":"EMBL:AJ251856","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12196391","title":"Telomere binding of checkpoint sensor and DNA repair proteins contributes to maintenance of functional fission yeast telomeres.","citation":"Genetics 2002 Aug;161(4):1437-52","abstract":"Telomeres, the ends of linear chromosomes, are DNA double-strand ends that do not trigger a cell cycle arrest and yet require checkpoint and DNA repair proteins for maintenance. Genetic and biochemical studies in the fission yeast Schizosaccharomyces pombe were undertaken to understand how checkpoint and DNA repair proteins contribute to telomere maintenance. On the basis of telomere lengths of mutant combinations of various checkpoint-related proteins (Rad1, Rad3, Rad9, Rad17, Rad26, Hus1, Crb2, Chk1, Cds1), Tel1, a telomere-binding protein (Taz1), and DNA repair proteins (Ku70, Rad32), we conclude that Rad3/Rad26 and Tel1/Rad32 represent two pathways required to maintain telomeres and prevent chromosome circularization. Rad1/Rad9/Hus1/Rad17 and Ku70 are two additional epistasis groups, which act in the Rad3/Rad26 pathway. However, Rad3/Rad26 must have additional target(s), as cells lacking Tel1/Rad32, Rad1/Rad9/Hus1/Rad17, and Ku70 groups did not circularize chromosomes. Cells lacking Rad3/Rad26 and Tel1/Rad32 senesced faster than a telomerase trt1Delta mutant, suggesting that these pathways may contribute to telomere protection. Deletion of taz1 did not suppress chromosome circularization in cells lacking Rad3/Rad26 and Tel1/Rad32, also suggesting that two pathways protect telomeres. Chromatin immunoprecipitation analyses found that Rad3, Rad1, Rad9, Hus1, Rad17, Rad32, and Ku70 associate with telomeres. Thus, checkpoint sensor and DNA repair proteins contribute to telomere maintenance and protection through their association with telomeres.","authors":"Nakamura TM, Moser BA, Russell P","authors_abbrev":"Nakamura TM et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-08-28","publication_year":"2002","canto_session_key":"1533fbdc3a541b0f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-05-04 15:46:16","canto_approved_date":"2020-04-02 11:34:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-04 15:46:11","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":131,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.02c","SPAC9E9.08","SPAC1952.07","SPAC13C5.07","SPAC16A10.07c","SPCC23B6.03c","SPBC216.05","SPCC18B5.11c","SPCC1259.13","SPAC20G4.04c","SPAC14C4.13","SPBC342.05","SPAC664.07c","SPBC29A3.14c","SPAC1556.01c"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2016-05-04"},{"uniquename":"PMID:20040574","title":"The human Holliday junction resolvase GEN1 rescues the meiotic phenotype of a Schizosaccharomyces pombe mus81 mutant.","citation":"Nucleic Acids Res 2010 Apr;38(6):1866-73","abstract":"A key step in meiotic recombination involves the nucleolytic resolution of Holliday junctions to generate crossovers. Although the enzyme that performs this function in human cells is presently unknown, recent studies led to the identification of the XPG-family endonuclease GEN1 that promotes Holliday junction resolution in vitro, suggesting that it may perform a related function in vivo. Here, we show that ectopic expression of GEN1 in fission yeast mus81Delta strains results in Holliday junction resolution and crossover formation during meiosis.","doi":"10.1093/nar/gkp1179","authors":"Lorenz A, West SC, Whitby MC","authors_abbrev":"Lorenz A et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2009-12-31","publication_year":"2010","canto_session_key":"9e37370725226d2f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-16 17:39:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-16 17:38:58","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.05c","SPAC2G11.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-10-16"},{"uniquename":"PMID:8742356","title":"Purification and characterization of urease from schizosaccharomyces pombe.","citation":"Can J Microbiol 1996 Feb;42(2):132-40","abstract":"The urease from the ascomycetous fission yeast Schizosaccharomyces pombe was purified about 4000-fold (34% yield) to homogeneity by acetone precipitation, ammonium sulfate precipitation, DEAE-Sepharose ion-exchange column chromatography, and if required, Mono-Q ion-exchange fast protein liquid chromatography. The enzyme was intracellular and only one species of urease was detected by nondenaturing polyacrylamide gel electrophoresis (PAGE). The native enzyme had a M(r) of 212 kDa (Sepharose CL6B-200 gel filtration) and a single subunit was detected with a M(r) of 102 kDa (PAGE with sodium dodecyl sulfate). The subunit stoichiometry was not specifically determined, but the molecular mass estimations indicate that the undissociated enzyme may be a dimer of identical subunits. The specific activity was 700-800 micromols urea.min-1.mg protein-1, the optimum pH for activity was 8.0, and the Km for urea was 1.03 mM. The sequence of the amino terminus was Met-Gln-Pro-Arg-Glu-Leu-His-Lys-Leu-Thr-Leu-His-Gln-Leu-Gly-Ser-Leu-Ala and the sequence of two tryptic peptides of the enzyme were Phe-Ile-Glu-Thr-Asn-Glu-Lys and Leu-Tyr-Ala-Pro-Glu-Asn-Ser-Pro-Gly-Phe-Val-Glu-Val-Leu-Glu-Gly-Glu-Ile- Glu- Leu-Leu-Pro-Asn-Leu-Pro. The N-terminal sequence and physical and kinetic properties indicated that S. pombe urease was more like the plant enzymes than the bacterial ureases.","authors":"Lubbers MW, Rodriguez SB, Honey NK, Thornton RJ","authors_abbrev":"Lubbers MW et al.","pubmed_publication_date":"Feb 1996","pubmed_entrez_date":"1996-02-01","publication_year":"1996","canto_session_key":"08572856fa356dce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-07-31 16:24:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 16:24:00","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:32848252","title":"Closed mitosis requires local disassembly of the nuclear envelope.","citation":"Nature 2020 Sep;585(7823):119-123","abstract":"At the end of mitosis, eukaryotic cells must segregate the two copies of their replicated genome into two new nuclear compartments 1 . They do this either by first dismantling and later reassembling the nuclear envelope in an 'open mitosis' or by reshaping an intact nucleus and then dividing it into two in a 'closed mitosis' 2,3 . Mitosis has been studied in a wide variety of eukaryotes for more than a century 4 , but how the double membrane of the nuclear envelope is split into two at the end of a closed mitosis without compromising the impermeability of the nuclear compartment remains unknown 5 . Here, using the fission yeast Schizosaccharomyces pombe (a classical model for closed mitosis 5 ), genetics, live-cell imaging and electron tomography, we show that nuclear fission is achieved via local disassembly of nuclear pores within the narrow bridge that links segregating daughter nuclei. In doing so, we identify the protein Les1, which is localized to the inner nuclear envelope and restricts the process of local nuclear envelope breakdown to the bridge midzone to prevent the leakage of material from daughter nuclei. The mechanism of local nuclear envelope breakdown in a closed mitosis therefore closely mirrors nuclear envelope breakdown in open mitosis 3 , revealing an unexpectedly high conservation of nuclear remodelling mechanisms across diverse eukaryotes.","doi":"10.1038/s41586-020-2648-3","authors":"Dey G, Culley S, Curran S, Schmidt U, Henriques R, Kukulski W, Baum B","authors_abbrev":"Dey G et al.","pubmed_publication_date":"Sep 2020","pubmed_entrez_date":"2020-08-28","publication_year":"2020","canto_session_key":"21d843433d804639","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Gautam Dey","canto_first_approved_date":"2020-09-14 08:25:02","canto_approved_date":"2025-09-03 11:01:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-05 11:56:22","canto_added_date":"2020-08-29 00:15:06","annotation_curators":[{"name":"Gautam Dey","community_curator":true,"annotation_count":20,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.18c","SPAC1486.04c","SPBC3B9.16c","SPCC285.13c","SPBC800.05c","SPACUNK4.07c","SPBC19G7.15","SPCC162.08c","SPAC1002.02","SPAC4F10.18","SPBC365.12c","SPAC23C4.05c","SPBC3B8.10c","SPBC1604.08c","SPAC18G6.10","SPAC19E9.01c","SPCC320.13c","SPAC20G8.05c","SPBC13A2.02","SPAC1786.03"],"gene_count":20,"ltp_gene_count":10,"approved_date":"2020-09-14"},{"uniquename":"PMID:32175559","title":"Natural extract and its fractions isolated from the marine bacterium Pseudoalteromonas flavipulchra STILL-33 have antioxidant and antiaging activities in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2020 May 01;20(3)","abstract":"Investigations into the potential for pharmacological inhibition of the aging process and the onset of age-related disease are increasingly garnering attention. Here, we analyzed the antiaging properties of natural compounds derived from several marine bacteria in vitro and in vivo using the fission yeast Schizosaccharomyces pombe. The Pseudoalteromonas flavipulchra STILL-33 extract exhibited high antioxidant and antiglycation activities in vitro. We then characterized two antioxidant active fractions isolated from this extract. In addition, we showed that the P. flavipulchra STILL-33 extract or either of its two active fractions (Fractions 1 and 2) could extend the longevity of fission yeast. Moreover, the particular extract and two active fractions were found to induce mitochondrial activity and to delay the G1 phase of the fission yeast cell cycle, perhaps by improving the aging process. The P. flavipulchra STILL-33 extract and Fraction 1 also increased the expression of the catalase-encoding ctt1+ gene and thereby decreased the reactive oxygen species level. Structural analysis showed that Fraction 1 was dominated by l-arginine and ipriflavone, and we showed indeed that the two corresponding commercial products increase the fission yeast lifespan. As for Fraction 2 was identified as the putative structure of butamben. Together, these results should facilitate the discovery of additional antiaging compounds from P. flavipulchra and ultimately the development of novel antiaging compounds for pharmaceutical use.","doi":"10.1093/femsyr/foaa014","authors":"Prastya ME, Astuti RI, Batubara I, Takagi H, Wahyudi AT","authors_abbrev":"Prastya ME et al.","pubmed_publication_date":"01 May 2020","pubmed_entrez_date":"2020-03-17","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-03-18 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30321395","title":"PomBase 2018: user-driven reimplementation of the fission yeast database provides rapid and intuitive access to diverse, interconnected information.","citation":"Nucleic Acids Res 2019 Jan 08;47(D1):D821-D827","abstract":"PomBase (www.pombase.org), the model organism database for the fission yeast Schizosaccharomyces pombe, has undergone a complete redevelopment, resulting in a more fully integrated, better-performing service. The new infrastructure supports daily data updates as well as fast, efficient querying and smoother navigation within and between pages. New pages for publications and genotypes provide routes to all data curated from a single source and to all phenotypes associated with a specific genotype, respectively. For ontology-based annotations, improved displays balance comprehensive data coverage with ease of use. The default view now uses ontology structure to provide a concise, non-redundant summary that can be expanded to reveal underlying details and metadata. The phenotype annotation display also offers filtering options to allow users to focus on specific areas of interest. An instance of the JBrowse genome browser has been integrated, facilitating loading of and intuitive access to, genome-scale datasets. Taken together, the new data and pages, along with improvements in annotation display and querying, allow users to probe connections among different types of data to form a comprehensive view of fission yeast biology. The new PomBase implementation also provides a rich set of modular, reusable tools that can be deployed to create new, or enhance existing, organism-specific databases.","doi":"10.1093/nar/gky961","authors":"Lock A, Rutherford K, Harris MA, Hayles J, Oliver SG, Bähler J, Wood V","authors_abbrev":"Lock A et al.","pubmed_publication_date":"08 Jan 2019","pubmed_entrez_date":"2018-10-16","publication_year":"2019","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2018-10-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22160596","title":"Altered nuclear tRNA metabolism in La-deleted Schizosaccharomyces pombe is accompanied by a nutritional stress response involving Atf1p and Pcr1p that is suppressible by Xpo-t/Los1p.","citation":"Mol Biol Cell 2012 Feb;23(3):480-91","abstract":"Deletion of the sla1(+) gene, which encodes a homologue of the human RNA-binding protein La in Schizosaccharomyces pombe, causes irregularities in tRNA processing, with altered distribution of pre-tRNA intermediates. We show, using mRNA profiling, that cells lacking sla1(+) have increased mRNAs from amino acid metabolism (AAM) genes and, furthermore, exhibit slow growth in Edinburgh minimal medium. A subset of these AAM genes is under control of the AP-1-like, stress-responsive transcription factors Atf1p and Pcr1p. Although S. pombe growth is resistant to rapamycin, sla1-Δ cells are sensitive, consistent with deficiency of leucine uptake, hypersensitivity to NH4, and genetic links to the target of rapamycin (TOR) pathway. Considering that perturbed intranuclear pre-tRNA metabolism and apparent deficiency in tRNA nuclear export in sla1-Δ cells may trigger the AAM response, we show that modest overexpression of S. pombe los1(+) (also known as Xpo-t), encoding the nuclear exportin for tRNA, suppresses the reduction in pre-tRNA levels, AAM gene up-regulation, and slow growth of sla1-Δ cells. The conclusion that emerges is that sla1(+) regulates AAM mRNA production in S. pombe through its effects on nuclear tRNA processing and probably nuclear export. Finally, the results are discussed in the context of stress response programs in Saccharomyces cerevisiae.","doi":"10.1091/mbc.E11-08-0732","authors":"Cherkasova V, Maury LL, Bacikova D, Pridham K, Bähler J, Maraia RJ","authors_abbrev":"Cherkasova V et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-12-14","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP8B7.09c","SPAC22F3.13","SPAC21E11.03c","SPAC57A10.10c","SPBC30D10.10c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:10371208","title":"Schizosaccharomyces pombe UDP-galactose transporter: identification of its functional form through cDNA cloning and expression in mammalian cells.","citation":"FEBS Lett 1999 May 28;451(3):295-8","abstract":"The Schizosaccharomyces pombe UDP-galactose transporter cDNA (SpUGT cDNA), encoding the product of the gms1+ gene which consists of two exon sequences separated by a 173-bp intron, was cloned by RT-PCR. Its product, a hydrophobic protein of 353 amino acid residues resembling its human counterpart, was expressed in the Golgi membranes of UDP-galactose transporter-deficient Lec8 cells, and complemented the genetic defect of the mutant cells. This indicated that SpUGT cDNA encodes the functional S. pombe UDP-galactose transporter. The product of an ORF found in the second exon, which was previously assumed to be the S. pombe UDP-galactose transporter, thus represents an inactive, truncated form of the SpUGT protein.","authors":"Segawa H, Ishida N, Takegawa K, Kawakita M","authors_abbrev":"Segawa H et al.","pubmed_publication_date":"28 May 1999","pubmed_entrez_date":"1999-06-17","publication_year":"1999","canto_session_key":"068fc9fb01950f72","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-07 13:38:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-07 13:38:29","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1795.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-07"},{"uniquename":"PMID:12073326","title":"Yeast genomic expression studies using DNA microarrays.","citation":"Methods Enzymol 2002;350:393-414","abstract":"The exploration and characterization of yeast genomic expression programs is providing a wealth of information about yeast biology, as well as other organisms. The intriguing biology of yeast species invites characterization of genomic expression patterns to illuminate the details of cellular physiology. In addition to its value as an interesting organism, yeast maintains its role as an excellent model in which to characterize genomic expression programs. Microarray studies are quickly spreading to plant, animal, and microbial organisms that remain in the early stages of characterization. The extensive knowledge of yeast biology, as well as the relative ease with which yeast studies can be performed and controlled, facilitates interpretation of the genomic expression data. Importantly, existing information about yeast biology, including functional annotations for each gene, is captured and efficiently presented in databases such as the Saccharomyces Genome Database (SGD), the Munich Information Center Yeast Genome Database (MIPS), the Yeast and Pombe Protein Databases (YPD and PPD, respectively), and others. A number of databases also allow the exploration of published genomic expression studies, including the \"Expression Connection\" at SGD and the Microarray Global Viewer (yMGV) organized by Marc et al. Consulting these databases to retrieve known details about gene function and regulation vastly facilitates interpretation of the genomic expression data, allowing biological hypotheses to be formulated and tested. These hypotheses can be applied to other organisms that may execute genomic expression programs similar to those seen in yeast. Furthermore, as more genomic expression studies in multiple organisms emerge, large-scale data comparisons can be conducted, within and across organisms. Incorporating the results of yeast studies into such comparisons is certain to increase our understanding about the function, regulation, and evolution of genomic expression programs.","authors":"Gasch AP","authors_abbrev":"Gasch AP","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-06-21","publication_year":"2002","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36882296","title":"Duf89 abets lncRNA control of fission yeast phosphate homeostasis via its antagonism of precocious lncRNA transcription termination.","citation":"RNA 2023 Jun;29(6):808-825","abstract":"Fission yeast phosphate homeostasis gene  pho1  is actively repressed during growth in phosphate-rich medium by transcription in  cis  of a long noncoding (lnc) RNA from the 5' flanking  prt(nc-pho1)  gene. Pho1 expression is: (i) derepressed by genetic maneuvers that favor precocious lncRNA 3'-processing and termination, in response to DSR and PAS signals in  prt ; and (ii) hyperrepressed in genetic backgrounds that dampen 3'-processing/termination efficiency. Governors of 3'-processing/termination include the RNA polymerase CTD code, the CPF (cleavage and polyadenylation factor) complex, termination factors Seb1 and Rhn1, and the inositol pyrophosphate signaling molecule 1,5-IP 8  Here, we present genetic and biochemical evidence that fission yeast Duf89, a metal-dependent phosphatase/pyrophosphatase, is an antagonist of precocious 3'-processing/termination. We show that derepression of  pho1  in  duf89 Δ cells correlates with squelching the production of full-length  prt  lncRNA and is erased or attenuated by: (i) DSR/PAS mutations in  prt ; (ii) loss-of-function mutations in components of the 3'-processing and termination machinery; (iii) elimination of the CTD Thr4-PO 4  mark; (iv) interdicting CTD prolyl isomerization by Pin1; (v) inactivating the Asp1 kinase that synthesizes IP 8 ; and (vi) loss of the putative IP 8  sensor Spx1. The findings that  duf89 Δ is synthetically lethal with  pho1 -derepressive mutations  CTD-S7A  and  aps1 Δ-and that this lethality is rescued by  CTD-T4A , CPF/Rhn1/Pin1 mutations, and  spx1 Δ-implicate Duf89 more broadly as a collaborator in cotranscriptional regulation of essential fission yeast genes. The  duf89-D252A  mutation, which abolishes Duf89 phosphohydrolase activity, phenocopied  duf89   + , signifying that  duf89 Δ phenotypes are a consequence of Duf89 protein absence, not absence of Duf89 catalysis.","doi":"10.1261/rna.079595.123","authors":"Sanchez AM, Garg A, Schwer B, Shuman S","authors_abbrev":"Sanchez AM et al.","pubmed_publication_date":"Jun 2023","pubmed_entrez_date":"2023-03-07","publication_year":"2023","canto_session_key":"59bf3609c95bb937","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2023-04-18 16:18:34","canto_approved_date":"2023-10-05 17:00:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-04-11 17:01:53","canto_added_date":"2023-03-09 01:15:04","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":138,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":9,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC74.02c","SPCC70.08c","SPBC2G2.04c","SPBC36.03c","SPBC21C3.19","SPBC19C2.04c","SPAC26H5.09c","SPAC1F7.07c","SPAC15E1.02c","SPAC13G7.02c","SPAC21E11.04","SPBC3B9.11c","SPBC17A3.03c","SPCC364.06","SPBC1289.16c","SPCC1884.01","SPACUNK4.17","SPAC13G6.14","SPBC8E4.01c","SPCC16C4.03","SPCC330.21","SPBC1271.09","SPAC637.03","SPAC11D3.19","SPBPB21E7.01c","SPBC28F2.12","SPBC25B2.08","SPCC1672.06c","SPBC337.03","SPBC8E4.12c","SPBPB2B2.06c","SPAP8A3.04c","SPBC776.02c","SPBP4G3.02","SPBC23G7.13c","SPNCRNA.1712","SPBC4F6.09","SPAC3G9.04","SPAC26F1.05","SPBC947.04","SPBC216.02","SPBC26H8.11c","SPAC24C9.15c","SPCC1393.13","SPCC1235.14","SPBC1271.08c","SPBC106.02c","SPBPB21E7.07","SPAC6B12.07c","SPAC824.04","SPBC1271.07c","SPAC8E11.02c","SPCC70.12c"],"gene_count":53,"ltp_gene_count":15,"approved_date":"2023-04-18"},{"uniquename":"PMID:207525","title":"Cytochrome c from Schizosaccharomyces pombe. 2. Amino-acid sequence.","citation":"Eur J Biochem 1978 May 16;86(2):407-16","abstract":"The amino acid sequence of Schizosaccharomyces pombe cytochrome c has been established by automatic degradation of the protein and by manual degradation of fragments obtained by cyanogen bromide cleavage and chymotryptic digestion. The chymotryptic peptides were aligned by homology with other known cytochrome c sequences. The protein is 108 residues long, with a four-residue amino-terminal tail. It has only one methionine residue and differs from other fungal cytochromes c in lacking the one-residue deletion at the C-terminal end. After a cyanogen bromide step, an unexpected cleavage of the peptide chain before a cysteine residue was observed. This is ascribed to formation of a dehydroalanyl residue during an incomplete S-carboxymethylation of the apoprotein, and subsequent cleavage under acidic conditions. Experimental evidence is presented in favour of the proposed mechanisms.","authors":"Simon-Becam AM, Claisse M, Lederer F","authors_abbrev":"Simon-Becam AM et al.","pubmed_publication_date":"16 May 1978","pubmed_entrez_date":"1978-05-16","publication_year":"1978","canto_session_key":"c4091e6ccf8b96c5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-21 10:13:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-21 10:12:40","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC191.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-11-21"},{"uniquename":"PMID:25210736","title":"Dynamics of cell shape inheritance in fission yeast.","citation":"PLoS One 2014;9(9):e106959","abstract":"Every cell has a characteristic shape key to its fate and function. That shape is not only the product of genetic design and of the physical and biochemical environment, but it is also subject to inheritance. However, the nature and contribution of cell shape inheritance to morphogenetic control is mostly ignored. Here, we investigate morphogenetic inheritance in the cylindrically-shaped fission yeast Schizosaccharomyces pombe. Focusing on sixteen different 'curved' mutants--a class of mutants which often fail to grow axially straight--we quantitatively characterize their dynamics of cell shape inheritance throughout generations. We show that mutants of similar machineries display similar dynamics of cell shape inheritance, and exploit this feature to show that persistent axial cell growth in S. pombe is secured by multiple, separable molecular pathways. Finally, we find that one of those pathways corresponds to the swc2-swr1-vps71 SWR1/SRCAP chromatin remodelling complex, which acts additively to the known mal3-tip1-mto1-mto2 microtubule and tea1-tea2-tea4-pom1 polarity machineries.","doi":"10.1371/journal.pone.0106959","authors":"Abenza JF, Chessel A, Raynaud WG, Carazo-Salas RE","authors_abbrev":"Abenza JF et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-09-12","publication_year":"2014","canto_session_key":"08c96f6f44e500f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-03-26 20:15:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-22 17:31:50","canto_added_date":"2014-09-13 00:16:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":60,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_25210736_phaf.tsv"}],"genes":["SPBC1706.01","SPAC11E3.01c","SPCC895.07","SPBC1604.20c","SPBC691.04","SPBC29A3.05","SPAC2F7.03c","SPCC1223.05c","SPBC27.06c","SPCC417.07c","SPAC18G6.15","SPCC553.08c","SPBP35G2.13c","SPCC1223.06","SPAC3C7.12","SPBC902.06"],"gene_count":16,"ltp_gene_count":7,"approved_date":"2015-12-22"},{"uniquename":"PMID:9708997","title":"Expression, purification, and characterization of ultraviolet DNA endonuclease from Schizosaccharomyces pombe.","citation":"Biochemistry 1998 Aug 18;37(33):11599-604","abstract":"Ultraviolet damage endonuclease (UVDE) is a 68.7 kDa DNA repair enzyme of Schizosaccharomyces pombe that recognizes cyclobutane pyrimidine dimers (CPDs) and 6-4 photoproducts (6-4 PPs). UVDE is thought to initiate the first step in an alternative excision repair pathway for removal of UV light-induced DNA damage. We have overexpressed Delta228-UVDE, an active truncated form of UVDE, and have purified this protein to apparent homogeneity. We have characterized purified Delta228-UVDE with respect to its physical properties, divalent cation requirements, and kinetic parameters on oligodeoxynucleotide substrates containing a single CPD. DNA strand cleavage analysis indicates that both full-length UVDE and Delta228-UVDE incise the CPD-containing strand immediately 5' to the lesion. These results provide further insight into the UVDE-mediated alternative excision repair pathway.","authors":"Kaur B, Avery AM, Doetsch PW","authors_abbrev":"Kaur B et al.","pubmed_publication_date":"18 Aug 1998","pubmed_entrez_date":"1998-08-26","publication_year":"1998","canto_session_key":"2d0049560e58d2a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-03-06 15:03:43","canto_approved_date":"2025-03-11 11:55:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-18 11:21:21","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-03-06"},{"uniquename":"PMID:9857040","title":"Substrate specificity of the SpCCE1 holliday junction resolvase of Schizosaccharomyces pombe.","citation":"J Biol Chem 1998 Dec 25;273(52):35063-73","abstract":"SpCCE1 from Schizosaccharomyces pombe is an endonuclease that resolves Holliday junctions in vitro. SpCCE1 also binds and cleaves a range of other DNAs (Y-junction; flap; and flayed, nicked, and partial duplexes) with varying efficiency. Cleavage sites are always 3' of thymine nucleotides positioned at or close to the branch point or strand interruption. SpCCE1's favored substrate is the X-junction. Up to two dimers of SpCCE1 can bind concurrently to the same X-junction at its crossover point. From mixing experiments of SpCCE1 and the Escherichia coli RuvA protein, we show that each dimer of SpCCE1 binds to a different face of the X-junction and that both are seemingly competent for strand cleavage. We propose that this provides a mechanism whereby SpCCE1 can scrutinize all four junction strands simultaneously for cleavable thymine nucleotides. SpCCE1 appears to resolve X-junctions by a nick and counter-nick mechanism. Therefore, to ensure a high probability of bilateral strand cleavage, SpCCE1 has a relatively long lifetime on X-junctions. This mechanism has the drawback of limiting dissociation from noncleavable junctions. We discuss why this might not be a problem in vivo.","authors":"Whitby MC, Dixon J","authors_abbrev":"Whitby MC et al.","pubmed_publication_date":"25 Dec 1998","pubmed_entrez_date":"1998-12-18","publication_year":"1998","canto_session_key":"9197a3d2cbe7051e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-09-02 10:48:08","canto_approved_date":"2025-05-19 08:15:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-02 10:48:02","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-02"},{"uniquename":"EMBL:AU014341","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14560029","title":"Swi1 prevents replication fork collapse and controls checkpoint kinase Cds1.","citation":"Mol Cell Biol 2003 Nov;23(21):7861-74","abstract":"The replication checkpoint is a dedicated sensor-response system activated by impeded replication forks. It stabilizes stalled forks and arrests division, thereby preserving genome integrity and promoting cell survival. In budding yeast, Tof1 is thought to act as a specific mediator of the replication checkpoint signal that activates the effector kinase Rad53. Here we report studies of fission yeast Swi1, a Tof1-related protein required for a programmed fork-pausing event necessary for mating type switching. Our studies have shown that Swi1 is vital for proficient activation of the Rad53-like checkpoint kinase Cds1. Together they are required to prevent fork collapse in the ribosomal DNA repeats, and they also prevent irreversible fork arrest at a newly identified hydroxyurea pause site. Swi1 also has Cds1-independent functions. Rad22 DNA repair foci form during S phase in swi1 mutants and to a lesser extent in cds1 mutants, indicative of fork collapse. Mus81, a DNA endonuclease required for recovery from collapsed forks, is vital in swi1 but not cds1 mutants. Swi1 is recruited to chromatin during S phase. We propose that Swi1 stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors.","authors":"Noguchi E, Noguchi C, Du LL, Russell P","authors_abbrev":"Noguchi E et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-10-16","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.06c","SPBC342.05","SPCC1259.13","SPCC18B5.11c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:11942608","title":"Contractile ring formation in Xenopus egg and fission yeast.","citation":"Cell Struct Funct 2001 Dec;26(6):545-54","abstract":"How actin filaments (F-actin) and myosin II (myosin) assemble to form the contractile ring was investigated with fission yeast and Xenopus egg. In fission yeast cells, an aster-like structure composed of F-actin cables is formed at the medial cortex of the cell during prophase to metaphase, and a single F-actin cable(s) extends from this structure, which seems to be a structural basis of the contractile ring. In early mitosis, myosin localizes as dots in the medial cortex independently of F-actin. Then they fuse with each other and are packed into a thin contractile ring. At the growing ends of the cleavage furrow of Xenopus eggs, F-actin at first assembles to form patches. Next they fuse with each other to form short F-actin bundles. The short bundles then form long bundles. Myosin seems to be transported by the cortical movement to the growing end and assembles there as spots earlier than F-actin. Actin polymerization into the patches is likely to occur after accumulation of myosin. The myosin spots and the F-actin patches are simultaneously reorganized to form the contractile ring bundles. The idea that a Ca signal triggers cleavage furrow formation was tested with Xenopus eggs during the first cleavage. We could not detect any Ca signals such as a Ca wave, Ca puffs or even Ca blips at the growing end of the cleavage furrow. Furthermore, cleavages are not affected by Ca-chelators injected into the eggs at concentrations sufficient to suppress the Ca waves. Thus we conclude that formation of the contractile ring is not induced by a Ca signal at the growing end of the cleavage furrow.","authors":"Noguchi T, Arai R, Motegi F, Nakano K, Mabuchi I","authors_abbrev":"Noguchi T et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2002-04-11","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27385337","title":"Roles of the novel coiled-coil protein Rng10 in septum formation during fission yeast cytokinesis.","citation":"Mol Biol Cell 2016 Aug 15;27(16):2528-41","abstract":"Rho GAPs are important regulators of Rho GTPases, which are involved in various steps of cytokinesis and other processes. However, regulation of Rho-GAP cellular localization and function is not fully understood. Here we report the characterization of a novel coiled-coil protein Rng10 and its relationship with the Rho-GAP Rga7 in fission yeast. Both rng10Δ and rga7Δ result in defective septum and cell lysis during cytokinesis. Rng10 and Rga7 colocalize on the plasma membrane at the cell tips during interphase and at the division site during cell division. Rng10 physically interacts with Rga7 in affinity purification and coimmunoprecipitation. Of interest, Rga7 localization is nearly abolished without Rng10. Moreover, Rng10 and Rga7 work together to regulate the accumulation and dynamics of glucan synthases for successful septum formation in cytokinesis. Our results show that cellular localization and function of the Rho-GAP Rga7 are regulated by a novel protein, Rng10, during cytokinesis in fission yeast.","doi":"10.1091/mbc.E16-03-0156","authors":"Liu Y, Lee IJ, Sun M, Lower CA, Runge KW, Ma J, Wu JQ","authors_abbrev":"Liu Y et al.","pubmed_publication_date":"15 Aug 2016","pubmed_entrez_date":"2016-07-08","publication_year":"2016","canto_session_key":"613296d2e91f5cb0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jian-Qiu Wu","canto_first_approved_date":"2018-01-17 05:55:40","canto_approved_date":"2021-04-06 17:19:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-09 19:42:57","canto_added_date":"2016-07-09 00:15:20","annotation_curators":[{"name":"Jian-Qiu Wu","community_curator":true,"annotation_count":56,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":51,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1281.01","SPBC19G7.05c","SPCC1840.02c","SPAC688.07c","SPAC4A8.05c","SPBC4F6.12","SPAC13A11.01c","SPAC1F7.04","SPBC106.20","SPCC4B3.15","SPCC645.05c","SPBC19G7.08c","SPBC21.06c","SPAC16.01","SPBC23G7.08c","SPBC11C11.02","SPAC4F10.11"],"gene_count":17,"ltp_gene_count":15,"approved_date":"2018-01-17"},{"uniquename":"PMID:27250944","title":"Cell Cycle Synchronization of Schizosaccharomyces pombe by Centrifugal Elutriation of Small Cells.","citation":"Cold Spring Harb Protoc 2016 Jun 01;2016(6)","abstract":"Division of Schizosaccharomyces pombe by medial fission produces identically sized daughter cells that grow by tip extension until their own division is prompted by reaching the same critical size for division as the parental cell. The fidelity of this size control in the absence of perturbation means that cells of the same size are at the same point in the cell cycle. Size selection of small cells from an asynchronous culture by centrifugal elutriation permits generation of synchronous cultures large enough for biochemical analysis. The changes observed in the synchronized cell cycle progression of such cultures are representative of those that accompany cell cycle progression of individual cells. Here, we describe how size selection with the Beckman Coulter JE-5.0 rotor can be used to generate synchronized cultures. Because of the continuous passage of medium through the rotor throughout the procedure, elutriation is considered to have less impact on the integrity of the cell cycle than other approaches. Two protocols are presented here: The first generates a 2-L culture ideal for detailed biochemical analysis, whereas the second allows rapid generation and simultaneous analysis of three smaller (200-mL) cultures.","doi":"10.1101/pdb.prot091231","authors":"Hagan IM, Grallert A, Simanis V","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"01 Jun 2016","pubmed_entrez_date":"2016-06-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-06-04 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17674143","title":"Molecular mechanisms underlying the mitosis-meiosis decision.","citation":"Chromosome Res 2007;15(5):523-37","abstract":"Most eukaryotic cells possess genetic potential to perform meiosis, but the vast majority of them never initiate it. The entry to meiosis is strictly regulated by developmental and environmental conditions, which vary significantly from species to species. Molecular mechanisms underlying the mitosis-meiosis decision are unclear in most organisms, except for a few model systems including fission yeast Schizosaccharomyces pombe. Nutrient limitation is a cue to the entry into meiosis in this microbe. Signals from nutrients converge on the activity of Mei2 protein, which plays pivotal roles in both induction and progression of meiosis. Here we outline the current knowledge of how a set of environmental stimuli eventually activates Mei2, and discuss how Mei2 governs the meiotic program molecularly, especially focusing on a recent finding that Mei2 antagonizes selective elimination of meiotic messenger RNAs.","authors":"Harigaya Y, Yamamoto M","authors_abbrev":"Harigaya Y et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-08-04","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27825301","title":"Analysis of the association between codon optimality and mRNA stability in Schizosaccharomyces pombe.","citation":"BMC Genomics 2016 Nov 08;17(1):895","abstract":"Recent experiments have shown that codon optimality is a major determinant of mRNA stability in Saccharomyces cerevisiae and that this phenomenon may be conserved in Escherichia coli and some metazoans, although work in Neurospora crassa is not consistent with this model.\nWe examined the association between codon optimality and mRNA stability in the fission yeast Schizosaccharomyces pombe. Our analysis revealed the following points. First, we observe a genome-wide association between codon optimality and mRNA stability also in S. pombe, suggesting evolutionary conservation of the phenomenon. Second, in both S. pombe and S. cerevisiae, mRNA synthesis rates are also correlated at the genome-wide analysis with codon optimality, suggesting that the long-appreciated association between codon optimality and mRNA abundance is due to regulation of both mRNA synthesis and degradation. However, when we examined correlation of codon optimality and either mRNA half-lives or synthesis rates controlling for mRNA abundance, codon optimality was still positively correlated with mRNA half-lives in S. cerevisiae, but the association was no longer significant for mRNA half-lives in S. pombe or for synthesis rates in either organism. This illustrates how only the pairwise analysis of multiple correlating variables may limit these types of analyses. Finally, in S. pombe, codon optimality is associated with known DNA/RNA sequence motifs that are associated with mRNA production/stability, suggesting these two features have been under similar selective pressures for optimal gene expression.\nConsistent with the emerging body of studies, this study suggests that the association between codon optimality and mRNA stability may be a broadly conserved phenomenon. It also suggests that the association can be explained at least in part by independent adaptations of codon optimality and other transcript features for elevated expression during evolution.","authors":"Harigaya Y, Parker R","authors_abbrev":"Harigaya Y et al.","pubmed_publication_date":"08 Nov 2016","pubmed_entrez_date":"2016-11-10","publication_year":"2016","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2016-11-10 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19116660","title":"Model of For3p-mediated actin cable assembly in fission yeast.","citation":"PLoS One 2008;3(12):e4078","abstract":"Formin For3p nucleates actin cables at the tips of fission yeast cells for polarized cell growth. The results of prior experiments have suggested a possible mechanism for actin cable assembly that involves association of For3p near cell tips, For3p-mediated actin polymerization, retrograde flow of actin cables toward the cell center, For3p dissociation from cell tips, and cable disassembly. We used analytical and computational modeling to test the validity and implications of the proposed coupled For3p/actin mechanism. We compared the model to prior experiments quantitatively and generated predictions for the expected behavior of the actin cable system upon changes of parameter values. We found that the model generates stable steady states with realistic values of rate constants and actin and For3p concentrations. Comparison of our results to previous experiments monitoring the FRAP of For3p-3GFP and the response of actin cables to treatments with actin depolymerizing drugs provided further support for the model. We identified the set of parameter values that produces results in agreement with experimental observations. We discuss future experiments that will help test the model's predictions and eliminate other possible mechanisms. The results of the model suggest that flow of actin cables may establish actin and For3p concentration gradients in the cytoplasm that could be important in global cell patterning.","doi":"10.1371/journal.pone.0004078","authors":"Wang H, Vavylonis D","authors_abbrev":"Wang H et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2009-01-01","publication_year":"2008","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10723568","title":"Mutagenesis and gene cloning in Schizosaccharomyces pombe using nonhomologous plasmid integration and rescue.","citation":"Biotechniques 2000 Mar;28(3):532-6, 538, 540","abstract":"Genes are commonly cloned in yeasts and bacteria by plasmid complementation, where the introduction of the gene of interest into a host strain carrying a recessive mutation in that gene suppresses the host's mutant phenotype. However, a lack of low copy cloning vectors in the fission yeast Schizosaccharomyces pombe can complicate this approach especially when overexpression of one gene may suppress a defect in another gene or when overexpression of the desired gene is detrimental, if not lethal, to the cell. We describe here a method of identifying mutations in S. pombe that allows for the rapid and direct cloning of the defective gene. This involves the nonhomologous integration of a marked plasmid into the yeast genome and its subsequent rescue into Escherichia coli, so that DNA at the site of insertion is incorporated into the recovered plasmid. As two of three insertions obtained in this study occurred outside of the affected gene's open reading frame, this method should be applicable to cloning both essential genes and nonessential genes.","authors":"Hoffman CS, Welton R","authors_abbrev":"Hoffman CS et al.","pubmed_publication_date":"Mar 2000","pubmed_entrez_date":"2000-03-21","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28497998","title":"Transcriptional reprogramming in cellular quiescence.","citation":"RNA Biol 2017 Jul 03;14(7):843-853","abstract":"Most cells in nature are not actively dividing, yet are able to return to the cell cycle given the appropriate environmental signals. There is now ample evidence that quiescent G0 cells are not shut-down but still metabolically and transcriptionally active. Quiescent cells must maintain a basal transcriptional capacity to maintain transcripts and proteins necessary for survival. This implies a tight control over RNA polymerases: RNA pol II for mRNA transcription during G0, but especially RNA pol I and RNA pol III to maintain an appropriate level of structural RNAs, raising the possibility that specific transcriptional control mechanisms evolved in quiescent cells. In accordance with this, we recently discovered that RNA interference is necessary to control RNA polymerase I transcription during G0. While this mini-review focuses on yeast model organisms (Saccharomyces cerevisiae and Schizosaccharomyces pombe), parallels are drawn to other eukaryotes and mammalian systems, in particular stem cells.","doi":"10.1080/15476286.2017.1327510","authors":"Roche B, Arcangioli B, Martienssen R","authors_abbrev":"Roche B et al.","pubmed_publication_date":"03 Jul 2017","pubmed_entrez_date":"2017-05-13","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-05-14 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15466421","title":"A screen for Schizosaccharomyces pombe mutants defective in rereplication identifies new alleles of rad4+, cut9+ and psf2+.","citation":"Genetics 2005 Jan;169(1):77-89","abstract":"Fission yeast mutants defective in DNA replication have widely varying morphological phenotypes. We designed a screen for temperature-sensitive mutants defective in the process of replication regardless of morphology by isolating strains unable to rereplicate their DNA in the absence of cyclin B (Cdc13). Of the 42 rereplication-defective mutants analyzed, we were able to clone complementing plasmids for 10. This screen identified new alleles of the APC subunit cut9(+), the initiation/checkpoint factor rad4(+)/cut5(+), and the first mutant allele of psf2(+), a subunit of the novel GINS replication complex. Other genes identified are likely to play general roles in gene expression and protein localization.","authors":"Gómez EB, Angeles VT, Forsburg SL","authors_abbrev":"Gómez EB et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-10-07","publication_year":"2005","canto_session_key":"023210fa935d9ad0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-09-20 15:09:55","canto_approved_date":"2024-11-14 09:43:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-23 16:28:21","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.18c","SPBC582.03","SPAC12G12.14c","SPCC1259.13","SPAC6F12.15c","SPBC725.13c","SPBC216.05","SPAC13C5.02"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2014-09-20"},{"uniquename":"PMID:10525840","title":"Cloning of Schizosaccharomyces pombe bio2 by heterologous complementation of a Saccharomyces cerevisiae mutant.","citation":"Curr Microbiol 1999 Dec;39(6):348-0350","abstract":"A Saccharomyces cerevisiae mutant affected in the last step of the biotin biosynthesis pathway was isolated by using a transposon mutagenesis method. The gene BIO2, encoding a biotin synthase, is shown to be interrupted in this mutant. Heterologous complementation experiment allowed the cloning and the characterization of a novel bio gene: bio2, encoding biotin synthase from Schizosaccharomyces pombe.","authors":"Phalip V, Lemoine Y, Jeltsch JM","authors_abbrev":"Phalip V et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-10-20","publication_year":"1999","canto_session_key":"24b60bdead7d16b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-01 10:11:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-30 11:29:19","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1235.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-30"},{"uniquename":"PMID:23087902","title":"Lipid raft involvement in yeast cell growth and death.","citation":"Front Oncol 2012;2:140","abstract":"The notion that cellular membranes contain distinct microdomains, acting as scaffolds for signal transduction processes, has gained considerable momentum. In particular, a class of such domains that is rich in sphingolipids and cholesterol, termed as lipid rafts, is thought to compartmentalize the plasma membrane, and to have important roles in survival and cell death signaling in mammalian cells. Likewise, yeast lipid rafts are membrane domains enriched in sphingolipids and ergosterol, the yeast counterpart of mammalian cholesterol. Sterol-rich membrane domains have been identified in several fungal species, including the budding yeast Saccharomyces cerevisiae, the fission yeast Schizosaccharomyces pombe as well as the pathogens Candida albicans and Cryptococcus neoformans. Yeast rafts have been mainly involved in membrane trafficking, but increasing evidence implicates rafts in a wide range of additional cellular processes. Yeast lipid rafts house biologically important proteins involved in the proper function of yeast, such as proteins that control Na(+), K(+), and pH homeostasis, which influence many cellular processes, including cell growth and death. Membrane raft constituents affect drug susceptibility, and drugs interacting with sterols alter raft composition and membrane integrity, leading to yeast cell death. Because of the genetic tractability of yeast, analysis of yeast rafts could be an excellent model to approach unanswered questions of mammalian raft biology, and to understand the role of lipid rafts in the regulation of cell death and survival in human cells. A better insight in raft biology might lead to envisage new raft-mediated approaches to the treatment of human diseases where regulation of cell death and survival is critical, such as cancer and neurodegenerative diseases.","doi":"10.3389/fonc.2012.00140","authors":"Mollinedo F","authors_abbrev":"Mollinedo F","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-10-23","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013227","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15632064","title":"Mutations in the RNA polymerase III subunit Rpc11p that decrease RNA 3' cleavage activity increase 3'-terminal oligo(U) length and La-dependent tRNA processing.","citation":"Mol Cell Biol 2005 Jan;25(2):621-36","abstract":"Termination by RNA polymerase III (Pol III) produces RNAs whose 3' oligo(U) termini are bound by La protein, a chaperone that protects RNAs from 3' exonucleases and promotes their maturation. Multiple reports indicate that yeasts use La-dependent and -independent pathways for tRNA maturation, with defective pre-tRNAs being most sensitive to decay and most dependent on La for maturation and function. The Rpc11p subunit of Pol III shows homology with the zinc ribbon of TFIIS and is known to mediate RNA 3' cleavage and to be important for termination. We used a La-dependent opal suppressor, tRNASerUGAM, which suppresses ade6-704 and the accumulation of red pigment, to screen Schizosaccaromyces pombe for rpc11 mutants that increase tRNA-mediated suppression. Analyses of two zinc ribbon mutants indicate that they are deficient in Pol III RNA 3' cleavage activity and produce pre-tRNASerUGAM transcripts with elongated 3'-oligo(U) tracts that are better substrates for La. A substantial fraction of pre-tRNASerUGAM contains too few 3' Us for efficient La binding and appears to decay in wild-type cells but has elongated oligo(U) tracts and matures along the La-dependent pathway in the mutants. The data indicate that Rpc11p limits RNA 3'-U length and that this significantly restricts pre-tRNAs to a La-independent pathway of maturation in fission yeast.","authors":"Huang Y, Intine RV, Mozlin A, Hasson S, Maraia RJ","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2005-01-06","publication_year":"2005","canto_session_key":"9f89b5e1df7ace40","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-04-16 16:48:55","canto_approved_date":"2025-09-04 11:13:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-02 15:26:14","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.10c","SPAC22A12.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-04-16"},{"uniquename":"PMID:11333015","title":"Activation of a cryptic 5' splice site by U1 snRNA.","citation":"RNA 2001 Mar;7(3):342-50","abstract":"In the course of analyzing 5' splice site mutations in the second intron of Schizosaccharomyces pombe cdc2, we identified a cryptic 5' junction containing a nonconsensus nucleotide at position +2. An even more unusual feature of this cryptic 5' junction was its pattern of activation. By analyzing the profile of splicing products for an extensive series of cdc2 mutants in the presence and absence of compensatory U1 alleles, we have obtained evidence that the natural 5' splice site participates in activation of the cryptic 5' splice site, and that it does so via base pairing to U1 snRNA. Furthermore, the results of follow-up experiments strongly suggest that base pairing between U1 snRNA and the cryptic 5' junction itself plays a dominant role in its activation. Most remarkably, a mutant U1 can activate the cryptic 5' splice site even in the presence of a wild-type sequence at the natural 5' junction, providing unambiguous evidence that this snRNA redirects splicing via base pairing. Although previous work has demonstrated that U5 and U6 snRNAs can activate cryptic 5' splice sites through base pairing interactions, this is the first example in which U1 snRNA has been implicated in the final selection of a cryptic 5' junction.","authors":"Alvarez CJ, Wise JA","authors_abbrev":"Alvarez CJ et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-05-03","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12654244","title":"Chromosomal cohesin forms a ring.","citation":"Cell 2003 Mar 21;112(6):765-77","abstract":"The cohesin complex is essential for sister chromatid cohesion during mitosis. Its Smc1 and Smc3 subunits are rod-shaped molecules with globular ABC-like ATPases at one end and dimerization domains at the other connected by long coiled coils. Smc1 and Smc3 associate to form V-shaped heterodimers. Their ATPase heads are thought to be bridged by a third subunit, Scc1, creating a huge triangular ring that could trap sister DNA molecules. We address here whether cohesin forms such rings in vivo. Proteolytic cleavage of Scc1 by separase at the onset of anaphase triggers its dissociation from chromosomes. We show that N- and C-terminal Scc1 cleavage fragments remain connected due to their association with different heads of a single Smc1/Smc3 heterodimer. Cleavage of the Smc3 coiled coil is sufficient to trigger cohesin release from chromosomes and loss of sister cohesion, consistent with a topological association with chromatin.","authors":"Gruber S, Haering CH, Nasmyth K","authors_abbrev":"Gruber S et al.","pubmed_publication_date":"21 Mar 2003","pubmed_entrez_date":"2003-03-26","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2021084","title":"Evaluation of phylogenetic relationships among fission yeast by nDNA/nDNA reassociation and conventional taxonomic criteria.","citation":"Yeast 1991 Jan;7(1):73-8","abstract":"The genus Schizosaccharomyces comprises a small, somewhat heterogeneous group of yeast species which have in common a unique mode of vegetative reproduction by cross-wall formation without constriction as well as a certain degree of osmophilia, most strains having been isolated from habitats of high sugar concentration. This study evaluated inter- and intraspecific relationships utilizing nDNA/nDNA optical reassociation and by the analysis of physiological profiles of several strains of each species. Results demonstrate that the genus should be divided into three species: Schiz. japonicus, Schiz. octosporus and Schiz. pombe.","authors":"Vaughan Martini A","authors_abbrev":"Vaughan Martini A","pubmed_publication_date":"Jan 1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:EF165542","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.53"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AB084825","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30294483","title":"LAMMER Kinase Lkh1 Is an Upstream Regulator of Prk1-Mediated Non-Sexual Flocculation in Fission Yeast.","citation":"Mycobiology 2018;46(3):236-241","abstract":"The cation-dependent galactose-specific flocculation activity of the  Schizosaccharomyces pombe  null mutant of  lkh1   + , the gene encoding LAMMER kinase homolog, has previously been reported by our group. Here, we show that disruption of  prk1   + , another flocculation associated regulatory kinase encoding gene, also resulted in cation-dependent galactose-specific flocculation. Deletion of  prk1  increased the flocculation phenotype of the  lkh1   +  null mutant and its overexpression reversed the flocculation of cells caused by  lkh1  deletion. Transcript levels of  prk1   +  were also decreased by  lkh1   +  deletion. Cumulatively, these results indicate that Lkh1 is one of the negative regulators acting upstream of Prk1, regulating non-sexual flocculation in fission yeast.","doi":"10.1080/12298093.2018.1513115","authors":"Park YD, Kwon SJ, Bae KS, Park HM","authors_abbrev":"Park YD et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-10-09","publication_year":"2018","canto_session_key":"0708da5a693db6d9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-10-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1D4.11c","SPAC23H4.17c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:31131414","title":"Casein kinase 2 regulates telomere protein complex formation through Rap1 phosphorylation.","citation":"Nucleic Acids Res 2019 Jul 26;47(13):6871-6884","abstract":"Telomeres located at the ends of linear chromosomes play important roles in the maintenance of life. Rap1, a component of the shelterin telomere protein complex, interacts with multiple proteins to perform various functions; further, formation of shelterin requires Rap1 binding to other components such as Taz1 and Poz1, and telomere tethering to the nuclear envelope (NE) involves interactions between Rap1 and Bqt4, a nuclear membrane protein. Although Rap1 is a hub for telomere protein complexes, the regulatory mechanisms of its interactions with partner proteins are not fully understood. Here, we show that Rap1 is phosphorylated by casein kinase 2 (CK2) at multiple sites, which promotes interactions with Bqt4 and Poz1. Among the multiple CK2-mediated phosphorylation sites of Rap1, phosphorylation at Ser496 was found to be crucial for both Rap1-Bqt4 and Rap1-Poz1 interactions. These mechanisms mediate proper telomere tethering to the NE and the formation of the silenced chromatin structure at chromosome ends.","doi":"10.1093/nar/gkz458","authors":"Inoue H, Horiguchi M, Ono K, Kanoh J","authors_abbrev":"Inoue H et al.","pubmed_publication_date":"26 Jul 2019","pubmed_entrez_date":"2019-05-28","publication_year":"2019","canto_session_key":"1695e0f67f5e2639","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junko Kanoh","canto_first_approved_date":"2020-03-28 09:25:53","canto_approved_date":"2023-05-03 15:50:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-19 15:33:35","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Junko Kanoh","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.13c","SPBC19C7.10","SPAC23C11.11","SPCC188.07","SPAC30D11.10","SPAC6F6.16c","SPBCPT2R1.08c","SPAC1851.03","SPAC6G9.13c","SPAC664.01c","SPAC16A10.07c","SPBC1778.02","SPAC26H5.06","SPAC1002.06c"],"gene_count":14,"ltp_gene_count":4,"approved_date":"2020-03-28"},{"uniquename":"PMID:1628648","title":"Spectral characteristics of cadmium-containing phytochelatin complexes isolated from Schizosaccharomyces pombe.","citation":"Eur J Biochem 1992 Jul 01;207(1):201-5","abstract":"Phytochelatins, heavy-metal-containing peptides with structures (gamma EC)nG, where n = 2-8, have been isolated from higher plants and the fission yeast Schizosaccharomyces pombe. The present work describes the isolation and characterization of several naturally occurring mixed complexes of these peptides from S. pombe exposed to 1 mM CdCl2. A lower-molecular-mass fraction from Sephadex G-50 chromatography yielded three distinct species on further fractionation. HPLC chromatography revealed the presence of peptides with n = 1-4 in varying amounts in these three complexes, referred to as complexes I, II and III. Stoichiometries are proposed for these complexes, based on [Cd], [SH], [S2-] and the amino acid content. Ultraviolet absorption and magnetic circular dichroism spectra of complexes II and III are similar, whereas the CD spectra of these two complexes are strikingly different. Compared to both complexes II and III, the CD bands of complex I are relatively weak. Ultraviolet absorption, CD and magnetic circular dichroism spectra provide a basis for the discussion of structural differences in these complexes.","authors":"Plocke DJ, Kägi JH","authors_abbrev":"Plocke DJ et al.","pubmed_publication_date":"01 Jul 1992","pubmed_entrez_date":"1992-07-01","publication_year":"1992","canto_session_key":"4717c81b3d8d20ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-17 16:30:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-17 16:30:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-01-17"},{"uniquename":"PMID:27189367","title":"Yeast peroxisomes: structure, functions and biotechnological opportunities.","citation":"FEMS Yeast Res 2016 Jun;16(4)","abstract":"Peroxisomes are ubiquitous organelles found in most eukaryotic cells. In yeasts, peroxisomes play important roles in cell metabolism, especially in different catabolic processes including fatty acid β-oxidation, the glyoxylic shunt and methanol metabolism, as well as some biosynthetic processes. In addition, peroxisomes are the compartment in which oxidases and catalase are localized. New peroxisomes mainly arise by fission of pre-existing ones, although they can also be formed from the endoplasmic reticulum (ER). Peroxisomes consist of matrix-soluble proteins and membrane proteins known as peroxins. A total of 34 PEX peroxin genes and proteins have been identified to date. and their functions have been elucidated. Protein import into peroxisomes depends on peroxins and requires specific signals in the structure of transported proteins: PTS1, PTS2 and mPTS. The mechanisms of metabolite penetration into peroxisomes are still poorly understood. Peroxisome number and the volume occupied by these organelles are tightly regulated. Methanol, fatty acids and methylamine act as efficient peroxisome proliferators, whereas glucose and ethanol induce peroxisome autophagic degradation (pexophagy). To date, 42 Atg proteins involved in pexophagy are known. Catabolism and alcoholic fermentation of the major pentose sugar, xylose, depend on peroxisomal enzymes. Overexpression of peroxisomal transketolase and transaldolase activates xylose fermentation. Peroxisomes could be useful as target organelles for overexpression of foreign toxic proteins.","doi":"10.1093/femsyr/fow038","authors":"Sibirny AA","authors_abbrev":"Sibirny AA","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-05-19","publication_year":"2016","canto_session_key":"135d90e465fbed63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-06-29 14:59:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-06-29 14:58:56","canto_added_date":"2016-06-29 14:58:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2016-06-29"},{"uniquename":"PMID:7949418","title":"Fission yeast morphogenesis--posing the problems.","citation":"Mol Biol Cell 1994 Jun;5(6):613-6","abstract":"","authors":"Nurse P","authors_abbrev":"Nurse P","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9660817","title":"Cloning and characterization of shk2, a gene encoding a novel p21-activated protein kinase from fission yeast.","citation":"J Biol Chem 1998 Jul 17;273(29):18481-9","abstract":"We describe the characterization of a novel gene, shk2, encoding a second p21(cdc42/rac)-activated protein kinase (PAK) homolog in fission yeast. Like other known PAKs, Shk2 binds to Cdc42 in vivo and in vitro. While overexpression of either shk2 or cdc42 alone does not impair growth of wild type fission yeast cells, cooverexpression of the two genes is toxic and leads to highly aberrant cell morphology, providing evidence for functional interaction between Cdc42 and Shk2 proteins in vivo. Fission yeast shk2 null mutants are viable and exhibit no obvious phenotypic defects. Overexpression of shk2 restores viability and normal morphology but not full mating competence to fission yeast cells carrying a shk1 null mutation. Additional genetic data suggest that Shk2, like Cdc42 and Shk1, participates in Ras-dependent morphological control and mating response pathways in fission yeast. We also show that overexpression of byr2, a gene encoding a Ste11/MAPK kinase kinase homolog, suppresses the mating defect of cells partially defective for Shk1 function, providing evidence of a link between PAKs and mitogen-activated protein kinase signaling in fission yeast. Taken together, our results suggest that Shk2 is partially overlapping in function with Shk1, with Shk1 being the dominant protein in function.","authors":"Yang P, Kansra S, Pimental RA, Gilbreth M, Marcus S","authors_abbrev":"Yang P et al.","pubmed_publication_date":"17 Jul 1998","pubmed_entrez_date":"1998-07-11","publication_year":"1998","canto_session_key":"b9761ecd7fdd2a70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-05-11 14:00:05","canto_approved_date":"2018-05-11 14:00:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-05-11 13:59:56","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.03","SPAC1556.08c","SPBC1D7.05","SPBC1604.14c","SPAC22H10.07","SPAC1F5.09c","SPAC16E8.09","SPBC16H5.11c","SPAC1D4.13","SPAC31G5.09c","SPAC17H9.09c"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2018-05-11"},{"uniquename":"PMID:28981863","title":"Subtelomeres constitute a safeguard for gene expression and chromosome homeostasis.","citation":"Nucleic Acids Res 2017 Oct 13;45(18):10333-10349","abstract":"The subtelomere, a telomere-adjacent chromosomal domain, contains species-specific homologous DNA sequences, in addition to various genes. However, the functions of subtelomeres, particularly subtelomeric homologous (SH) sequences, remain elusive. Here, we report the first comprehensive analyses of the cellular functions of SH sequences in the fission yeast, Schizosaccharomyces pombe. Complete removal of SH sequences from the genome revealed that they are dispensable for mitosis, meiosis and telomere length control. However, when telomeres are lost, SH sequences prevent deleterious inter-chromosomal end fusion by facilitating intra-chromosomal circularization. Surprisingly, SH-deleted cells sometimes survive telomere loss through inter-chromosomal end fusions via homologous loci such as LTRs, accompanied by centromere inactivation of either chromosome. Moreover, SH sequences function as a buffer region against the spreading of subtelomeric heterochromatin into the neighboring gene-rich regions. Furthermore, we found a nucleosome-free region at the subtelomeric border, which may be a second barrier that blocks heterochromatin spreading into the subtelomere-adjacent euchromatin. Thus, our results demonstrate multiple defense functions of subtelomeres in chromosome homeostasis and gene expression.","doi":"10.1093/nar/gkx780","authors":"Tashiro S, Nishihara Y, Kugou K, Ohta K, Kanoh J","authors_abbrev":"Tashiro S et al.","pubmed_publication_date":"13 Oct 2017","pubmed_entrez_date":"2017-10-06","publication_year":"2017","canto_session_key":"c8a8914f57060ece","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junko Kanoh","canto_first_approved_date":"2020-02-17 15:53:18","canto_approved_date":"2020-02-17 15:53:18","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-02-08 16:41:21","canto_added_date":"2017-10-07 00:15:47","annotation_curators":[{"name":"Junko Kanoh","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPAC977.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-02-17"},{"uniquename":"PMID:2561424","title":"Gene products required for chromosome separation.","citation":"J Cell Sci Suppl 1989;12:213-29","abstract":"Gene products required for mitotic chromosome separation in the fission yeast Schizosaccharomyces pombe are described. They have been identified by two distinct strategies of mutant isolation, followed by gene cloning and immunochemical characterization of gene products. The roles of four representative genes, namely nda3+, nuc2+, top2+ and dis2+, encoding beta-tubulin, a nuclear scaffold-like protein, DNA topoisomerase II and type-1 protein phosphatase, respectively, are discussed in regard to the mechanisms and control of chromosome separation.","authors":"Yanagida M","authors_abbrev":"Yanagida M","pubmed_publication_date":"1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_session_key":"daf633509d7fad2c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-10-17 15:19:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-17 15:19:42","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC776.02c","SPAC17C9.01c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2016-10-17"},{"uniquename":"EMBL:AJ251852","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9358188","title":"Isolation of nuclei for chromatin analysis in fission yeast.","citation":"Nucleic Acids Res 1997 Nov 15;25(22):4700-1","abstract":"The methods available for analysis of the chromatin of Schizosaccharomyces pombe are time consuming (>8 h) and/or result in some degradation of the chromatin. Here we report an optimised method for the preparation of spheroplasts and the isolation of nuclei which takes <25 min and is suitable for analysis of chromatin structure by micrococcal nuclease, restriction endonuclease or by immunoprecipitation.","authors":"Mason JA, Mellor J","authors_abbrev":"Mason JA et al.","pubmed_publication_date":"15 Nov 1997","pubmed_entrez_date":"1998-02-12","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9405296","title":"Genes that cause aberrant cell morphology by overexpression in fission yeast: a role of a small GTP-binding protein Rho2 in cell morphogenesis.","citation":"J Cell Sci 1998 Jan;111 ( Pt 2):149-59","abstract":"To identify the genes involved in cell morphogenesis in Schizosaccharomyces pombe, we screened for the genes that cause aberrant cell morphology by overexpression. The isolated genes were classified on the basis of morphology conferred. One of the genes causing a rounded morphology was identified as the rho2+ gene encoding a small GTP-binding protein. The overexpression of rho2+ resulted in a randomized distribution of cortical F-actin and formation of a thick cell wall. Analyses using cdc mutants suggested that the overexpression of rho2+ prevents the establishment of growth polarity in G1. The rho2+ gene was not essential, but among cells deleted for rho2+, those with an irregular shape were observed. The disruptant also showed a defect in cell wall integrity. An HA-Rho2 expressed in the cell was suggested to be present as a membrane-bound form by a cell fractionation experiment. A GFP-Rho2 was localized at the growing end(s) of the cell and the septation site. The localization of GFP-Rho2 during interphase was partially dependent on sts5+. These results indicate that Rho2 is involved in cell morphogenesis, control of cell wall integrity, control of growth polarity, and maintenance of growth direction. Analysis of functional overlapping between Rho2 and Rho1 revealed that their functions are distinct from each other, with partial overlapping.","authors":"Hirata D, Nakano K, Fukui M, Takenaka H, Miyakawa T, Mabuchi I","authors_abbrev":"Hirata D et al.","pubmed_publication_date":"Jan 1998","pubmed_entrez_date":"1998-03-21","publication_year":"1998","canto_session_key":"9a6d1a60bd8f2c4f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-07 18:27:42","canto_approved_date":"2023-03-15 17:36:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-07 18:27:32","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":39,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPBC336.12c","SPAC16.01","SPCC1223.06","SPCC16C4.09","SPAC1F7.04","SPAC24H6.05","SPBC12D12.04c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-06-07"},{"uniquename":"PMID:32875947","title":"Term Matrix: a novel Gene Ontology annotation quality control system based on ontology term co-annotation patterns.","citation":"Open Biol 2020 Sep;10(9):200149","abstract":"Biological processes are accomplished by the coordinated action of gene products. Gene products often participate in multiple processes, and can therefore be annotated to multiple Gene Ontology (GO) terms. Nevertheless, processes that are functionally, temporally and/or spatially distant may have few gene products in common, and co-annotation to unrelated processes probably reflects errors in literature curation, ontology structure or automated annotation pipelines. We have developed an annotation quality control workflow that uses rules based on mutually exclusive processes to detect annotation errors, based on and validated by case studies including the three we present here: fission yeast protein-coding gene annotations over time; annotations for cohesin complex subunits in human and model species; and annotations using a selected set of GO biological process terms in human and five model species. For each case study, we reviewed available GO annotations, identified pairs of biological processes which are unlikely to be correctly co-annotated to the same gene products (e.g. amino acid metabolism and cytokinesis), and traced erroneous annotations to their sources. To date we have generated 107 quality control rules, and corrected 289 manual annotations in eukaryotes and over 52 700 automatically propagated annotations across all taxa.","doi":"10.1098/rsob.200149","authors":"Wood V, Carbon S, Harris MA, Lock A, Engel SR, Hill DP, Van Auken K, Attrill H, Feuermann M, Gaudet P, Lovering RC, Poux S, Rutherford KM, Mungall CJ","authors_abbrev":"Wood V et al.","pubmed_publication_date":"Sep 2020","pubmed_entrez_date":"2020-09-03","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-09-04 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:692424","title":"Preparation of protoplasts of Schizosaccharomyces pombe.","citation":"Methods Cell Biol 1978;20:101-5","abstract":"","authors":"Schwencke J, Nagy M","authors_abbrev":"Schwencke J et al.","pubmed_publication_date":"1978","pubmed_entrez_date":"1978-01-01","publication_year":"1978","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29987032","title":"Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes.","citation":"Proc Natl Acad Sci U S A 2018 Jul 24;115(30):E7063-E7072","abstract":"The lack of attachment of lipoic acid to its cognate enzyme proteins results in devastating human metabolic disorders. These mitochondrial disorders are evident soon after birth and generally result in early death. The mutations causing specific defects in lipoyl assembly map in three genes,  LIAS ,  LIPT1 , and  LIPT2  Although physiological roles have been proposed for the encoded proteins, only the LIPT1 protein had been studied at the enzyme level. LIPT1 was reported to catalyze only the second partial reaction of the classical lipoate ligase mechanism. We report that the physiologically relevant LIPT1 enzyme activity is transfer of lipoyl moieties from the H protein of the glycine cleavage system to the E2 subunits of the 2-oxoacid dehydrogenases required for respiration (e.g., pyruvate dehydrogenase) and amino acid degradation. We also report that LIPT2 encodes an octanoyl transferase that initiates lipoyl group assembly. The human pathway is now biochemically defined.","doi":"10.1073/pnas.1805862115","authors":"Cao X, Zhu L, Song X, Hu Z, Cronan JE","authors_abbrev":"Cao X et al.","pubmed_publication_date":"24 Jul 2018","pubmed_entrez_date":"2018-07-11","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28808035","title":"Fission yeast myosin Myo2 is down-regulated in actin affinity by light chain phosphorylation.","citation":"Proc Natl Acad Sci U S A 2017 Aug 29;114(35):E7236-E7244","abstract":"Studies in fission yeast  Schizosaccharomyces pombe  have provided the basis for the most advanced models of the dynamics of the cytokinetic contractile ring. Myo2, a class-II myosin, is the major source of tension in the contractile ring, but how Myo2 is anchored and regulated to produce force is poorly understood. To enable more detailed biochemical/biophysical studies, Myo2 was expressed in the baculovirus/ Sf 9 insect cell system with its two native light chains, Rlc1 and Cdc4. Milligram yields of soluble, unphosphorylated Myo2 were obtained that exhibited high actin-activated ATPase activity and in vitro actin filament motility. The fission yeast specific chaperone Rng3 was thus not required for expression or activity. In contrast to nonmuscle myosins from animal cells that require phosphorylation of the regulatory light chain for activation, phosphorylation of Rlc1 markedly reduced the affinity of Myo2 for actin. Another unusual feature of Myo2 was that, unlike class-II myosins, which generally form bipolar filamentous structures, Myo2 showed no inclination to self-assemble at approximately physiological salt concentrations, as analyzed by sedimentation velocity ultracentrifugation. This lack of assembly supports the hypothesis that clusters of Myo2 depend on interactions at the cell cortex in structural units called nodes for force production during cytokinesis.","doi":"10.1073/pnas.1703161114","authors":"Pollard LW, Bookwalter CS, Tang Q, Krementsova EB, Trybus KM, Lowey S","authors_abbrev":"Pollard LW et al.","pubmed_publication_date":"29 Aug 2017","pubmed_entrez_date":"2017-08-16","publication_year":"2017","canto_session_key":"c9e3c1f326d228f9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-08-17 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.03","SPBC32H8.12c","SPCC645.05c","SPCC613.04c","SPBC1604.14c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:22905165","title":"The integrity of the cytokinesis machinery under stress conditions requires the glucan synthase Bgs1p and its regulator Cfh3p.","citation":"PLoS One 2012;7(8):e42726","abstract":"In yeast, cytokinesis requires coordination between nuclear division, acto-myosin ring contraction, and septum synthesis. We studied the role of the Schizosaccharomyces pombe Bgs1p and Cfh3p proteins during cytokinesis under stress conditions. Cfh3p formed a ring in the septal area that contracted during mitosis; Cfh3p colocalized and co-immunoprecipitated with Cdc15p, showing that Cfh3p interacted with the contractile acto-myosin ring. In a wild-type strain, a significant number of contractile rings collapsed under stress conditions and this number increased dramatically in the cfh3Δ, bgs1cps1-191, and cfh3Δ bgs1/cps1-191. Our results show that after osmotic shock Cfh3p is essential for the stability of the (1,3) glucan synthase Bgs1p in the septal area, but not at the cell poles. Finally, cells adapted to stress; they repaired their contractile rings and re-localized Bgs1p to the cell surface some time after osmotic shock. A detailed analysis of the cytokinesis machinery in the presence of KCl revealed that the actomyosin ring collapsed before Bgs1p was internalized, and that it was repaired before Bgs1p re-localized to the cell surface. In the cfh3Δ, bgs1/cps1-191, and cfh3Δ bgs1/cps1-191 mutants, which have reduced glucan synthesis, the damage produced to the ring had stronger consequences, suggesting that an intact primary septum contributes to ring stability. The results show that the contractile actomyosin ring is very sensitive to stress, and that cells have efficient mechanisms to remedy the damage produced in this structure.","doi":"10.1371/journal.pone.0042726","authors":"Sharifmoghadam MR, Curto MÁ, Hoya M, de León N, Martin-Garcia R, Doncel C, Valdivieso MH","authors_abbrev":"Sharifmoghadam MR et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-21","publication_year":"2012","canto_session_key":"e1a1f6eb2da24846","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Henar Valdivieso","canto_first_approved_date":"2020-02-27 14:52:19","canto_approved_date":"2024-04-03 16:29:05","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-02-21 12:21:12","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Henar Valdivieso","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.09","SPBC1709.01","SPBC11C11.02","SPBC19G7.05c","SPBC1289.01c","SPBC32H8.12c","SPAP8A3.08","SPBC16A3.01","SPCC1739.11c","SPAC6F6.08c","SPAC20G8.05c"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2020-02-27"},{"uniquename":"PMID:17605132","title":"Comparative genomics of the environmental stress response in ascomycete fungi.","citation":"Yeast 2007 Nov;24(11):961-76","abstract":"Unicellular fungi thrive in diverse niches around the world, and many of these niches present unique and stressful challenges that must be contended with by their inhabitants. Numerous studies have investigated the genomic expression responses to environmental stress in 'model' ascomycete fungi, including Saccharomyces cerevisiae, Candida albicans and Schizosaccharomyces pombe. This review presents a comparative-genomics perspective on the environmental stress response, a common response to diverse stresses. Implications for the role of this response, based on its presence or absence in fungi from disparate ecological niches, are discussed.","authors":"Gasch AP","authors_abbrev":"Gasch AP","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-07-03","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29936183","title":"Linear Regression Links Transcriptomic Data and Cellular Raman Spectra.","citation":"Cell Syst 2018 Jul 25;7(1):104-117.e4","abstract":"Raman microscopy is an imaging technique that has been applied to assess molecular compositions of living cells to characterize cell types and states. However, owing to the diverse molecular species in cells and challenges of assigning peaks to specific molecules, it has not been clear how to interpret cellular Raman spectra. Here, we provide firm evidence that cellular Raman spectra and transcriptomic profiles of Schizosaccharomyces pombe and Escherichia coli can be computationally connected and thus interpreted. We find that the dimensions of high-dimensional Raman spectra and transcriptomes measured by RNA sequencing can be reduced and connected linearly through a shared low-dimensional subspace. Accordingly, we were able to predict global gene expression profiles by applying the calculated transformation matrix to Raman spectra, and vice versa. Highly expressed non-coding RNAs contributed to the Raman-transcriptome linear correspondence more significantly than mRNAs in S. pombe. This demonstration of correspondence between cellular Raman spectra and transcriptomes is a promising step toward establishing spectroscopic live-cell omics studies.","doi":"10.1016/j.cels.2018.05.015","authors":"Kobayashi-Kirschvink KJ, Nakaoka H, Oda A, Kamei KF, Nosho K, Fukushima H, Kanesaki Y, Yajima S, Masaki H, Ohta K, Wakamoto Y","authors_abbrev":"Kobayashi-Kirschvink KJ et al.","pubmed_publication_date":"25 Jul 2018","pubmed_entrez_date":"2018-06-25","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-06-26 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41323438","title":"Long multiply marked DNA repair template reveals lengths and fidelity of genome editing tracts in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2025;2025","abstract":"To test the ability of a fission yeast CRISPR-Cas9 system (  SpEDIT  ) to carry out genome editing over distance, we constructed a 1,935 bp-long, dsDNA repair template that contained 45 base pair substitutions (SNPs), relative to the wild-type target locus  ade6  . Template-directed repair was efficient in the vicinity of the recombination-initiating dsDNA break, but the efficiency fell rapidly with distance (median editing tract length of 163 bp). The regularly distributed markers also revealed evidence for heteroduplex DNA at the ends of repair tracks and, unexpectedly, that DNA ends of the repair template participate in many (~18%) of the genome editing events.","doi":"10.17912/micropub.biology.001917","authors":"Protacio RU, Ali NA, Chevireddy A, Wahls WP","authors_abbrev":"Protacio RU et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-12-01","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-12-02 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10806422","title":"Multiple pathways regulating fission yeast mitosis upon environmental stresses.","citation":"Yeast 2000 May;16(7):597-609","abstract":"Environmental signals, such as nutrient availability and physiological stresses, modulate the cell cycle and cell size of the fission yeast Schizosaccharomyces pombe. However, little is known about how these signals are transmitted to the central cell cycle regulator, Cdc2, the cyclin-dependent kinase that induces mitosis. We show here genetic evidence that medium alkalization stimulates mitosis and consequently reduces cell size, either through the Nim1-Wee1 cascade, which regulates the inhibitory phosphorylation of Cdc2 at Tyr(15), or through the Cdc2-activating phosphatase, Cdc25. Alkaline stress stimulates phosphorylation of Nim1, accumulation of Cdc25 and dephosphorylation of Cdc2 at Tyr(15). We also show that osmostress stimulates mitosis through two independent pathways: one stimulates accumulation of Cdc25, and another dephosphorylation of Cdc2 at Tyr(15). However, our analysis demonstrates that these environmental stresses can stimulate mitosis independently of dephosphorylation of Cdc2 at Tyr(15). The S. pombe MAP kinase, Spc1, was required for the steady-state level of Cdc25 in the normal cell cycle and for its accumulation in response to alkaline stress and nutritional starvation.","authors":"Kishimoto N, Yamashita I","authors_abbrev":"Kishimoto N et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-05-12","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12565827","title":"Fission yeast synaptobrevin is involved in cytokinesis and cell elongation.","citation":"Biochem Biophys Res Commun 2003 Feb 14;301(3):641-5","abstract":"Synaptobrevin is a vesicle-associated membrane protein playing an essential role in regulated vesicle transport. In this study, we characterized Syb1, synaptobrevin of Schizosaccharomyces pombe. Syb1 was located on various sizes of vesicle-like structures in the cytoplasm and enriched in the medial region and cell ends. Transport of Syb1 to the medial region was mainly dependent on F-actin and Myo52/Myo4. Syb1 is essential for cell viability and most of the syb1-null cells showed a round or short cylindrical form. These results suggest that Syb1 is involved in membrane trafficking of cytokinesis and cell elongation.","authors":"Edamatsu M, Toyoshima YY","authors_abbrev":"Edamatsu M et al.","pubmed_publication_date":"14 Feb 2003","pubmed_entrez_date":"2003-02-05","publication_year":"2003","canto_session_key":"191a34a7eb84c981","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-30 15:38:22","canto_approved_date":"2020-12-30 15:38:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-30 15:38:14","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-12-30"},{"uniquename":"PMID:21971174","title":"Abundance of prereplicative complexes (Pre-RCs) facilitates recombinational repair under replication stress in fission yeast.","citation":"J Biol Chem 2011 Dec 02;286(48):41701-41710","abstract":"Mcm2-7 complexes are loaded onto chromatin with the aid of Cdt1 and Cdc18/Cdc6 and form prereplicative complexes (pre-RCs) at multiple sites on each chromosome. Pre-RCs are essential for DNA replication and surviving replication stress. However, the mechanism by which pre-RCs contribute to surviving replication stress is largely unknown. Here, we isolated the fission yeast mcm6-S1 mutant that was hypersensitive to methyl methanesulfonate (MMS) and camptothecin (CPT), both of which cause forks to collapse. The mcm6-S1 mutation impaired the interaction with Cdt1 and decreased the binding of minichromosome maintenance (MCM) proteins to replication origins. Overexpression of Cdt1 restored MCM binding and suppressed the sensitivity to MMS and CPT, suggesting that the Cdt1-Mcm6 interaction is important for the assembly of pre-RCs and the repair of collapsed forks. MMS-induced Chk1 phosphorylation and Rad22/Rad52 focus formation occurred normally, whereas cells containing Rhp54/Rad54 foci, which are involved in DNA strand exchange and dissociation of the joint molecules, were increased. Remarkably, G(1) phase extension through deletion of an S phase cyclin, Cig2, as well as Cdt1 overexpression restored pre-RC assembly and suppressed Rhp54 accumulation. A cdc18 mutation also caused hypersensitivity to MMS and CPT and accumulation of Rhp54 foci. These data suggest that an abundance of pre-RCs facilitates a late step in the recombinational repair of collapsed forks in the following S phase.","doi":"10.1074/jbc.M111.285619","authors":"Maki K, Inoue T, Onaka A, Hashizume H, Somete N, Kobayashi Y, Murakami S, Shigaki C, Takahashi TS, Masukata H, Nakagawa T","authors_abbrev":"Maki K et al.","pubmed_publication_date":"02 Dec 2011","pubmed_entrez_date":"2011-10-06","publication_year":"2011","canto_session_key":"41faea428ef0af7e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-08-21 12:49:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-06-27 10:15:47","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB2B4.03","SPCC1259.13","SPBC428.18","SPBC211.04c","SPBC14C8.07c","SPCC16A11.17","SPCC18B5.11c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2012-06-27"},{"uniquename":"PMID:29322557","title":"Veni, vidi, vici: the success of wtf meiotic drivers in fission yeast.","citation":"Yeast 2018 Jul;35(7):447-453","abstract":"Meiotic drivers are selfish DNA loci that can bias their own transmission into gametes. Owing to their transmission advantages, meiotic drivers can spread in populations even if the drivers or linked variants decrease organismal fitness. Meiotic drive was first formally described in the 1950s and is thought to be a powerful force shaping eukaryotic genomes. Classic genetic analyses have detected the action of meiotic drivers in plants, filamentous fungi, insects and vertebrates. Several of these drive systems have limited experimental tractability and relatively little is known about the molecular mechanisms of meiotic drive. Recently, however, meiotic drivers were discovered in a yeast species. The Schizosaccharomyces pombe wtf gene family contains several active meiotic drive genes. This review summarizes what is known about the wtf family and highlights its potential as a highly tractable experimental model for molecular and evolutionary characterization of meiotic drive.","doi":"10.1002/yea.3305","authors":"López Hernández JF, Zanders SE","authors_abbrev":"López Hernández JF et al.","pubmed_publication_date":"Jul 2018","pubmed_entrez_date":"2018-01-12","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-01-14 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31801797","title":"A toolbox of stable integration vectors in the fission yeast  Schizosaccharomyces pombe .","citation":"J Cell Sci 2020 Jan 08;133(1)","abstract":" Schizosaccharomyces pombe  is a widely used model organism to study many aspects of eukaryotic cell physiology. Its popularity as an experimental system partially stems from the ease of genetic manipulations, where the innate homology-targeted repair is exploited to precisely edit the genome. While vectors to incorporate exogenous sequences into the chromosomes are available, most are poorly characterized. Here, we show that commonly used fission yeast vectors, which upon integration produce repetitive genomic regions, give rise to unstable genomic loci. We overcome this problem by designing a new series of stable integration vectors (SIVs) that target four different prototrophy genes. SIVs produce non-repetitive, stable genomic loci and integrate predominantly as single copy. Additionally, we develop a set of complementary auxotrophic alleles that preclude false-positive integration events. We expand the vector series to include antibiotic resistance markers, promoters, fluorescent tags and terminators, and build a highly modular toolbox to introduce heterologous sequences. Finally, as proof of concept, we generate a large set of ready-to-use, fluorescent probes to mark organelles and cellular processes with a wide range of applications in fission yeast research.This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.240754","authors":"Vještica A, Marek M, Nkosi PJ, Merlini L, Liu G, Bérard M, Billault-Chaumartin I, Martin SG","authors_abbrev":"Vještica A et al.","pubmed_publication_date":"08 Jan 2020","pubmed_entrez_date":"2019-12-06","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-01-06 15:42:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12769820","title":"A simple dependence between protein evolution rate and the number of protein-protein interactions.","citation":"BMC Evol Biol 2003 May 23;3:11","abstract":"It has been shown for an evolutionarily distant genomic comparison that the number of protein-protein interactions a protein has correlates negatively with their rates of evolution. However, the generality of this observation has recently been challenged. Here we examine the problem using protein-protein interaction data from the yeast Saccharomyces cerevisiae and genome sequences from two other yeast species.\nIn contrast to a previous study that used an incomplete set of protein-protein interactions, we observed a highly significant correlation between number of interactions and evolutionary distance to either Candida albicans or Schizosaccharomyces pombe. This study differs from the previous one in that it includes all known protein interactions from S. cerevisiae, and a larger set of protein evolutionary rates. In both evolutionary comparisons, a simple monotonic relationship was found across the entire range of the number of protein-protein interactions. In agreement with our earlier findings, this relationship cannot be explained by the fact that proteins with many interactions tend to be important to yeast. The generality of these correlations in other kingdoms of life unfortunately cannot be addressed at this time, due to the incompleteness of protein-protein interaction data from organisms other than S. cerevisiae.\nProtein-protein interactions tend to slow the rate at which proteins evolve. This may be due to structural constraints that must be met to maintain interactions, but more work is needed to definitively establish the mechanism(s) behind the correlations we have observed.","authors":"Fraser HB, Wall DP, Hirsh AE","authors_abbrev":"Fraser HB et al.","pubmed_publication_date":"23 May 2003","pubmed_entrez_date":"2003-05-29","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AY225216","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18B11.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:41184513","title":"Phosphorylation-dependent tuning of mRNA deadenylation rates.","citation":"Nat Struct Mol Biol 2025 Nov 03;","abstract":"Shortening of messenger RNA poly(A) tails by the Ccr4-Not complex initiates mRNA decay and is a major determinant of gene regulation. RNA adaptors modulate the specificity of deadenylation by binding to Ccr4-Not through their intrinsically disordered regions (IDRs). However, the determinants of specificity and their regulation are largely unclear. Here we use nuclear magnetic resonance spectroscopy, biochemical reconstitution and structural modeling to show that dispersed segments within the IDR of the fission yeast Puf3 RNA adaptor interact with Ccr4-Not, consistent with multivalency. Binding can be modulated by phosphorylation, altering the deadenylation rate in a continuously tunable manner. Regulation of deadenylation through multivalency and phosphorylation likely occurs in evolutionarily divergent IDRs from additional RNA adaptors, including human Pumilio and Tristetraprolin. Overall, our in vitro data suggest that mRNA decay can be regulated not only as a bistable on-off switch but also by a graded mechanism, rationalizing how post-transcriptional gene expression can be fine-tuned.","doi":"10.1038/s41594-025-01688-1","authors":"Stowell JAW, Yu CWH, Chen ZA, DeBell LK, Lee G, Morgan T, Sinn L, Agnello S, O'Reilly FJ, Rappsilber J, Freund SMV, Passmore LA","authors_abbrev":"Stowell JAW et al.","pubmed_publication_date":"03 Nov 2025","pubmed_entrez_date":"2025-11-03","publication_year":"2025","canto_session_key":"2a2e8a9bcebbb64a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lori Passmore","canto_first_approved_date":"2026-02-26 11:11:33","canto_approved_date":"2026-05-14 20:17:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-02-07 14:50:24","canto_added_date":"2025-11-05 00:25:04","annotation_curators":[{"name":"Lori Passmore","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16C9.04c","SPCC31H12.08c","SPAC20G8.06","SPCC18.06c","SPBC1778.10c","SPAC1B9.02c","SPCC4G3.15c","SPCC576.15c","SPAC1B3.05","SPAC57A7.04c","SPAC29B12.06c","SPAC1687.22c"],"gene_count":12,"ltp_gene_count":7,"approved_date":"2026-02-26"},{"uniquename":"PMID:14704433","title":"RNAi-mediated targeting of heterochromatin by the RITS complex.","citation":"Science 2004 Jan 30;303(5658):672-6","abstract":"RNA interference (RNAi) is a widespread silencing mechanism that acts at both the posttranscriptional and transcriptional levels. Here, we describe the purification of an RNAi effector complex termed RITS (RNA-induced initiation of transcriptional gene silencing) that is required for heterochromatin assembly in fission yeast. The RITS complex contains Ago1 (the fission yeast Argonaute homolog), Chp1 (a heterochromatin-associated chromodomain protein), and Tas3 (a novel protein). In addition, the complex contains small RNAs that require the Dicer ribonuclease for their production. These small RNAs are homologous to centromeric repeats and are required for the localization of RITS to heterochromatic domains. The results suggest a mechanism for the role of the RNAi machinery and small RNAs in targeting of heterochromatin complexes and epigenetic gene silencing at specific chromosomal loci.","authors":"Verdel A, Jia S, Gerber S, Sugiyama T, Gygi S, Grewal SI, Moazed D","authors_abbrev":"Verdel A et al.","pubmed_publication_date":"30 Jan 2004","pubmed_entrez_date":"2004-01-06","publication_year":"2004","canto_session_key":"b1769602f49f8e69","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-01-20 08:59:53","canto_approved_date":"2024-06-07 15:58:15","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-01-18 17:17:43","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.11","SPAC18G6.02c","SPAC6F12.09","SPBC16C6.10","SPBC83.03c","SPBC16D10.07c","SPCC188.13c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2024-01-20"},{"uniquename":"PMID:4447905","title":"Morphine analysis of yeast cells. III. Size distribution of 2-deoxyglucose-induced lysing Schizosaccharomyces pombe cells and their sites of lysis.","citation":"Can J Genet Cytol 1974 Sep;16(3):593-8","abstract":"","authors":"Johnson BF, Lu C, Brandwein S","authors_abbrev":"Johnson BF et al.","pubmed_publication_date":"Sep 1974","pubmed_entrez_date":"1974-09-01","publication_year":"1974","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20081370","title":"The role of specific HAT-HDAC interactions in transcriptional elongation.","citation":"Cell Cycle 2010 Feb 01;9(3):467-71","abstract":"We previously reported genome-wide evidence that the Gcn5 histone acetyltransferase (HAT) is located in the transcribed region of highly expressed genes and that it plays an important role in transcriptional elongation in the fission yeast, Schizosaccharomyces pombe (EMBO Reports 2009; 10:1009-14). Furthermore, the specific interplay between Gcn5 and the Clr3 histone deacetylase (HDAC) controls the acetylation levels of lysine-14 in histone H3 in the same class of highly expressed genes. Mutants of histone H3 that cannot be acetylated at residue 14 show similar stress phenotypes to those observed for mutants lacking Gcn5. In this Extra View article we review these findings in relation to related literature and extend important aspects of the original study. Notably, Gcn5 and Gcn5-dependent acetylation of histone H3K14 tend to be more enriched in the upstream regions of genes that require Gcn5 for correct expression compared to genes that are independent of Gcn5. This suggests a critical role of Gcn5 in the transcriptional initiation of these genes. Gcn5 is however most highly enriched in the transcribed regions of these gene sets but there is no difference between Gcn5-dependent and Gcn5-independent gene sets. Thus we suggest that Gcn5 plays an important but redundant role in the transcriptional elongation of these genes. The Sir2 HDAC has a similar genomic localization and enzymatic activity to Clr3. We studied gcn5Deltasir2Delta double mutants that do not show a suppressed phenotype in relation to gcn5Delta single mutants, compared to gcn5Deltaclr3Delta mutants that do, in order to better understand the specificity of the interplay between Gcn5 and Clr3. In some classes of non-highly expressed genes the clr3Delta mutant tends to restore levels of histone H3K14 acetylation in the double mutant strain more effectively than sir2Delta.","authors":"Johnsson AE, Wright AP","authors_abbrev":"Johnsson AE et al.","pubmed_publication_date":"01 Feb 2010","pubmed_entrez_date":"2010-01-19","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15923187","title":"Phosphatidylinositol-4-phosphate 5-kinase regulates fission yeast cell integrity through a phospholipase C-mediated protein kinase C-independent pathway.","citation":"J Biol Chem 2005 Jul 29;280(30):27561-8","abstract":"Fission yeast its3-1 mutant is an allele of the essential gene its3+ that encodes a phosphatidylinositol-4-phosphate 5-kinase (PIP5K) that produces phosphatidylinositol 4,5-bisphosphate. We found that the its3-1 mutant is sensitive to micafungin, a (1,3)-beta-D-glucan synthase inhibitor, suggesting a cell wall integrity defect. Consistently, its3-1 mutation caused synthetic lethality with a (1,3)-beta-D-glucan synthase mutant, bgs1-i2, and its3-1 mutant cells showed aberrant localization of green fluorescent protein-Bgs1. Similar aberrant localization of green fluorescent protein-tagged Rgf1, a putative phosphatidylinositol 4,5-bisphosphate-binding guanine nucleotide exchange factor for Rho protein, in its3-1 mutants was observed, suggesting a defective Rgf1/Rho pathway. To unravel the molecular mechanism(s), putative downstream components of PIP5K signaling were analyzed. Unexpectedly, overexpression of phospholipase C (Plc1), but not that of protein kinase C (PKC; Pck1 and Pck2), suppressed the phenotypes of the its3-1 mutant. These findings indicate that PKCs are not involved in the suppression, and further analysis revealed that PKCs are not downstream of Plc1 in fission yeast. Also, the enzymatic activity of Plc1 is essential for the suppression of the phenotypes and for the viability of the its3-1 mutant. These findings suggest that Its3 PIP5K regulates cell integrity through a Plc1-mediated PKC-independent pathway, in addition to the Rho/PKC pathway.","authors":"Deng L, Sugiura R, Ohta K, Tada K, Suzuki M, Hirata M, Nakamura S, Shuntoh H, Kuno T","authors_abbrev":"Deng L et al.","pubmed_publication_date":"29 Jul 2005","pubmed_entrez_date":"2005-06-01","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.14","SPAC17G8.14c","SPAC22F8.11","SPBC19G7.05c","SPBC12D12.04c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:41637053","title":"Construction of a reference genome for Starmerella batistae and annotation of Starmerella species reveal an unexpected evolutionary relationship with Schizosaccharomyces pombe and suggest an alternative enzymatic route for sophorolipid production.","citation":"FEMS Yeast Res 2026 Feb 04;","abstract":"The Starmerella clade is known for displaying osmotolerant and acidophilic traits from their association with bees. Several species in this genus can produce sophorolipids, which are commercially produced as biosurfactants. Here, we isolated a yeast contaminant from the laboratory environment, identified as Starmerella batistae, able to thrive at low pH and relative high temperatures. We sequenced and conducted a de novo genome assembly in three chromosomes and a mitochondrial genome for S. batistae (ca. 9.3 Mb). Based on this reference genome we functionally annotated 29 Starmerella species, using the publicly available sequences. Phylogenetic analysis across different yeast clades revealed a close relationship between Starmerella and Schizosaccharomyces yeasts. Fifteen genes were uniquely shared between Sz. pombe and S. batistae, of which twelve were involved in cell morphology, reflecting the fact that S. batistae cells are elongated rather than round. We found that all the Starmerella sophorolipid-producing strains shared a close common ancestor. One-to-one orthologs of S. bombicola sophorolipid pathway were only found in S. kuoi (full pathway, but inverted), and in S. powellii and S. floricola (partial pathway). These findings support the notion that alternative pathways for the production of sophorolipids have evolved in different Starmerella lineages.","doi":"10.1093/femsyr/foag008","authors":"Timouma S, Hanak A, Cisneros LNB, Donaldson I, Valle F, Delneri D","authors_abbrev":"Timouma S et al.","pubmed_publication_date":"04 Feb 2026","pubmed_entrez_date":"2026-02-04","publication_year":"2026","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2026-02-05 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11294220","title":"Molecular biology. The histone modification circus.","citation":"Science 2001 Apr 06;292(5514):64-5","abstract":"","authors":"Berger SL","authors_abbrev":"Berger SL","pubmed_publication_date":"06 Apr 2001","pubmed_entrez_date":"2001-04-11","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33050127","title":"The Impact of Chitosan on the Chemical Composition of Wines Fermented with  Schizosaccharomyces   pombe  and  Saccharomyces cerevisiae .","citation":"Foods 2020 Oct 09;9(10)","abstract":"This study investigates the influence of the antimicrobial agent chitosan on a selected  Schizosaccharomyces pombe  strain during the alcoholic fermentation of ultra-pasteurized grape juice with a high concentration of malic acid. It also studies a selected  Saccharomyces cerevisiae  strain as a control. The study examines several parameters relating to wine quality, including volatile and non-volatile compounds. The principal aim of the study is to test the influence of chitosan on the final chemical composition of the wine during alcoholic fermentation, and to compare the two studied fermentative yeasts between them. The results show that chitosan influences the final concentration of acetic acid, ethanol, glycerol, acetaldehyde, pyruvic acid, α-ketoglutarate, higher alcohols, acetate esters, ethyl esters, and fatty acids, depending on the yeast species.","doi":"10.3390/foods9101423","authors":"Scansani S, Rauhut D, Brezina S, Semmler H, Benito S","authors_abbrev":"Scansani S et al.","pubmed_publication_date":"09 Oct 2020","pubmed_entrez_date":"2020-10-14","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-10-20 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7654712","title":"Purification and characterization of the low molecular weight protein tyrosine phosphatase, Stp1, from the fission yeast Schizosaccharomyces pombe.","citation":"Biochemistry 1995 Aug 22;34(33):10560-8","abstract":"Genetic screening in fission yeast has identified a gene named stp1+ that rescues cdc25-22 [Mondesert et al. (1994) J. Biol. Chem. 269, 27996-27999]. This gene encodes a 17.4 kDa protein that is 42% identical to members of the low molecular weight protein tyrosine phosphatases (low M(r)PTPases) previously known to exist only in mammalian species. A simple and efficient purification procedure was developed to obtain the homogeneous recombinant yeast low M(r)PTPase, Stp1, in large quantities suitable for kinetic and structural studies. Authentic Stp1 was produced as judged by amino terminal protein sequencing and electrospray ionization mass spectrometry analyses. Stp1 was shown to possess intrinsic phosphatase activity toward both aryl phosphates (such as phosphotyrosine) and alkyl phosphates (such as phosphoserine). Stp1 also dephosphorylated phosphotyrosyl peptide/protein substrates. The yeast enzyme was 6-fold slower than the mammalian enzymes, which made it amenable to pre-steady-state stopped-flow spectroscopic kinetic analysis at 30 degrees C and pH 6.0. Burst kinetics was observed with Stp1 using p-nitrophenyl phosphate as a substrate, suggesting that the rate-limiting step corresponds to the decomposition of the phosphoenzyme intermediate. Interestingly, the bovine heart low M(r)PTPase was capable of removing phosphate groups from both phosphotyrosyl and phosphoseryl/threonyl protein substrates with comparable efficiencies. The low M(r)PTPases, like the Cdc25 family of phosphatases, may represent a new group of dual specificity phosphatases which may be involved in cell cycle control.","authors":"Zhang ZY, Zhou G, Denu JM, Wu L, Tang X, Mondesert O, Russell P, Butch E, Guan KL","authors_abbrev":"Zhang ZY et al.","pubmed_publication_date":"22 Aug 1995","pubmed_entrez_date":"1995-08-22","publication_year":"1995","canto_session_key":"baf208a0d2de2a0f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-29 12:55:35","canto_approved_date":"2026-01-27 12:46:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-21 14:08:34","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-29"},{"uniquename":"PMID:10648611","title":"Characterization of Schizosaccharomyces pombe Hus1: a PCNA-related protein that associates with Rad1 and Rad9.","citation":"Mol Cell Biol 2000 Feb;20(4):1254-62","abstract":"Hus1 is one of six checkpoint Rad proteins required for all Schizosaccharomyces pombe DNA integrity checkpoints. MYC-tagged Hus1 reveals four discrete forms. The main form, Hus1-B, participates in a protein complex with Rad9 and Rad1, consistent with reports that Rad1-Hus1 immunoprecipitation is dependent on the rad9(+) locus. A small proportion of Hus1-B is intrinsically phosphorylated in undamaged cells and more becomes phosphorylated after irradiation. Hus1-B phosphorylation is not increased in cells blocked in early S phase with hydroxyurea unless exposure is prolonged. The Rad1-Rad9-Hus1-B complex is readily detectable, but upon cofractionation of soluble extracts, the majority of each protein is not present in this complex. Indirect immunofluorescence demonstrates that Hus1 is nuclear and that this localization depends on Rad17. We show that Rad17 defines a distinct protein complex in soluble extracts that is separate from Rad1, Rad9, and Hus1. However, two-hybrid interaction, in vitro association and in vivo overexpression experiments suggest a transient interaction between Rad1 and Rad17.","authors":"Caspari T, Dahlen M, Kanter-Smoler G, Lindsay HD, Hofmann K, Papadimitriou K, Sunnerhagen P, Carr AM","authors_abbrev":"Caspari T et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-01-29","publication_year":"2000","canto_session_key":"9f192daa7cdd3cc7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-03-04 11:09:28","canto_approved_date":"2021-01-05 16:48:42","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-02-04 17:20:10","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC342.05","SPBC216.05","SPAC14C4.13","SPAC20G4.04c","SPAC9E9.08","SPAC664.07c","SPAC1952.07"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-03-04"},{"uniquename":"PMID:1551414","title":"Protein prenylation in Schizosaccharomyces pombe.","citation":"FEBS Lett 1992 Feb 03;297(1-2):103-6","abstract":"S. pombe is shown to be a powerful system for studies concerning attachment of polyisoprenoid moieties to proteins, due to its ability to take up exogenous mevalonic acid efficiently. The fission yeast can take up about 5% of the exogenously added mevalonic acid and incorporate approximately 10% of this into protein. By contrast, the uptake obtained with the budding yeast S. cerevisiae is less than 0.5%. HPLC analysis of total S. pombe protein-bound isoprenoids revealed that approximately 55% of the counts co-migrated with the geranylgeraniol standard, while approximately 45% of the counts co-migrated with farnesol. We could not detect any effects of mevinolin or other HMG-CoA reductase inhibitors in S. pombe.","authors":"Giannakouros T, Armstrong J, Magee AI","authors_abbrev":"Giannakouros T et al.","pubmed_publication_date":"03 Feb 1992","pubmed_entrez_date":"1992-02-03","publication_year":"1992","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22771823","title":"Schizosaccharomyces pombe Hat1 (Kat1) is associated with Mis16 and is required for telomeric silencing.","citation":"Eukaryot Cell 2012 Sep;11(9):1095-103","abstract":"The Hat1 histone acetyltransferase has been implicated in the acetylation of histone H4 during chromatin assembly. In this study, we have characterized the Hat1 complex from the fission yeast Schizosaccharomyces pombe and have examined its role in telomeric silencing. Hat1 is found associated with the RbAp46 homologue Mis16, an essential protein. The Hat1 complex acetylates lysines 5 and 12 of histone H4, the sites that are acetylated in newly synthesized H4 in a wide range of eukaryotes. Deletion of hat1 in S. pombe is itself sufficient to cause the loss of silencing at telomeres. This is in contrast to results obtained with an S. cerevisiae hat1Δ strain, which must also carry mutations of specific acetylatable lysines in the H3 tail domain for loss of telomeric silencing to occur. Notably, deletion of hat1 from S. pombe resulted in an increase of acetylation of histone H4 in subtelomeric chromatin, concomitant with derepression of this region. A similar loss of telomeric silencing was also observed after growing cells in the presence of the deacetylase inhibitor trichostatin A. However, deleting hat1 did not cause loss of silencing at centromeres or the silent mating type locus. These results point to a direct link between Hat1, H4 acetylation, and the establishment of repressed telomeric chromatin in fission yeast.","doi":"10.1128/EC.00123-12","authors":"Tong K, Keller T, Hoffman CS, Annunziato AT","authors_abbrev":"Tong K et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-07-10","publication_year":"2012","canto_session_key":"ab9f54dfaf87407a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-15 09:27:01","canto_approved_date":"2021-08-31 17:16:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-15 09:26:55","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.12","SPAC139.06","SPAC1834.03c","SPBC8D2.03c","SPCC1672.10"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-03-15"},{"uniquename":"PMID:1547958","title":"HPV16 E7 phosphorylation in fission yeast: characterization and biological effects.","citation":"Gene 1992 Feb 01;111(1):93-8","abstract":"Human papillomavirus type 16 E7 protein (HPV-16 E7), synthesised in Schizosaccharomyces pombe, is both phosphorylated and targeted to the nucleus [Tommasino et al., Gene 93 (1990) 265-270] as is E7 protein synthesized in primate cells. Further analysis of E7 expression in fission yeast indicates that: (i) E7 protein synthesised in S. pombe is phosphorylated only on the Ser residues which are part of a casein kinase II consensus site, as it has been shown to be the cause in human cells, and is tightly associated with the nuclear matrix; (ii) synthesis of wild type, phosphorylated E7 is responsible for a significant increase in S. pombe doubling time; and (iii) E7 phosphorylation is not required for the tight association of the protein with the nuclear matrix, but E7 mutants, in which one (Ser31) or both phosphorylated serines (Ser31 and Ser32) have been substituted, lack any effect on cell-cycle duration.","authors":"Tommasino M, Contorni M, Cavalieri F","authors_abbrev":"Tommasino M et al.","pubmed_publication_date":"01 Feb 1992","pubmed_entrez_date":"1992-02-01","publication_year":"1992","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9228070","title":"A DNA helicase from Schizosaccharomyces pombe stimulated by single-stranded DNA-binding protein at low ATP concentration.","citation":"J Biol Chem 1997 Jul 25;272(30):18910-9","abstract":"A DNA helicase named DNA helicase I was isolated from cell-free extracts of the fission yeast Schizosaccharomyces pombe. Both DNA helicase and single-stranded DNA-dependent ATPase activities copurified with a polypeptide of 95 kDa on an SDS-polyacrylamide gel. The helicase possessed a sedimentation coefficient of 6.0 S and a Stokes radius of 44.8 A determined by glycerol gradient centrifugation and gel filtration analysis, respectively. From these data the native molecular mass was calculated to be 110 kDa, indicating that the active enzyme is a monomer. The DNA-unwinding and ATP hydrolysis activities associated with DNA helicase I have been examined. One notable property of the enzyme was its relatively high rate of ATP turnover (35-50 molecules of ATP hydrolyzed/s/enzyme molecule) that may contribute to its inefficient unwinding activity at low concentrations of ATP (<0.2 mM). Addition of an ATP-regenerating system to the reaction mixture restored the DNA-unwinding activity of the enzyme. S. pombe single-stranded DNA-binding protein (SpSSB, also called SpRPA) stimulated the DNA helicase activity significantly at low levels of ATP (0.025-0.2 mM) even in the absence of an ATP-regenerating system. In contrast, SpRPA had no effect on ATP hydrolysis at any ATP concentration examined. These observations suggest that the stimulation of DNA unwinding by SpRPA is not simply a result of suppression of nonproductive ATP hydrolysis. Rather, the role of SpRPA is to lower the Km for ATP in the unwinding reaction, allowing the helicase to function efficiently at low ATP concentrations.","authors":"Park JS, Choi E, Lee SH, Lee C, Seo YS","authors_abbrev":"Park JS et al.","pubmed_publication_date":"25 Jul 1997","pubmed_entrez_date":"1997-07-25","publication_year":"1997","canto_session_key":"934f73b23470f4c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-11-24 16:51:03","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-24 16:50:59","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-24"},{"uniquename":"PMID:12183637","title":"Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1.","citation":"Science 2002 Oct 18;298(5593):608-11","abstract":"COP9 signalosome (CSN) cleaves the ubiquitin-like protein Nedd8 from the Cul1 subunit of SCF ubiquitin ligases. The Jab1/MPN domain metalloenzyme (JAMM) motif in the Jab1/Csn5 subunit was found to underlie CSN's Nedd8 isopeptidase activity. JAMM is found in proteins from archaea, bacteria, and eukaryotes, including the Rpn11 subunit of the 26S proteasome. Metal chelators and point mutations within JAMM abolished CSN-dependent cleavage of Nedd8 from Cul1, yet had little effect on CSN complex assembly. Optimal SCF activity in yeast and both viability and proper photoreceptor cell (R cell) development in Drosophila melanogaster required an intact Csn5 JAMM domain. We propose that JAMM isopeptidases play important roles in a variety of physiological pathways.","authors":"Cope GA, Suh GS, Aravind L, Schwarz SE, Zipursky SL, Koonin EV, Deshaies RJ","authors_abbrev":"Cope GA et al.","pubmed_publication_date":"18 Oct 2002","pubmed_entrez_date":"2002-08-17","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:11:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC215.03c","SPAC17G6.12","SPAC1687.13c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:9691032","title":"The Schizosaccharomyces pombe S-phase checkpoint differentiates between different types of DNA damage.","citation":"Genetics 1998 Aug;149(4):1729-37","abstract":"We have identified an S-phase DNA damage checkpoint in Schizosaccharomyces pombe. This checkpoint is dependent on Rad3, the S. pombe homolog of the mammalian ATM/ATR checkpoint proteins, and Cds1. Cds1 had previously been believed to be involved only in the replication checkpoint. The requirement of Cds1 in the DNA damage checkpoint suggests that Cds1 may be a general target of S-phase checkpoints. Unlike other checkpoints, the S. pombe S-phase DNA damage checkpoint discriminates between different types of damage. UV-irradiation, which causes base modification that can be repaired during G1 and S-phase, invokes the checkpoint, while gamma-irradiation, which causes double-stranded breaks that cannot be repaired by a haploid cell if induced before replication, does not invoke the checkpoint. Because the same genes are required to respond to UV- and gamma-irradiation during G2, this discrimination may represent an active suppression of the gamma response during S-phase.","authors":"Rhind N, Russell P","authors_abbrev":"Rhind N et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-08-05","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23613904","title":"Mechanisms of intron loss and gain in the fission yeast Schizosaccharomyces.","citation":"PLoS One 2013;8(4):e61683","abstract":"The fission yeast, Schizosaccharomyces pombe, is an important model species with a low intron density. Previous studies showed extensive intron losses during its evolution. To test the models of intron loss and gain in fission yeasts, we conducted a comparative genomic analysis in four Schizosaccharomyces species. Both intronization and de-intronization were observed, although both were at a low frequency. A de-intronization event was caused by a degenerative mutation in the branch site. Four cases of imprecise intron losses were identified, indicating that genomic deletion is not a negligible mechanism of intron loss. Most intron losses were precise deletions of introns, and were significantly biased to the 3' sides of genes. Adjacent introns tended to be lost simultaneously. These observations indicated that the main force shaping the exon-intron structures of fission yeasts was precise intron losses mediated by reverse transcriptase. We found two cases of intron gains caused by tandem genomic duplication, but failed to identify the mechanisms for the majority of the intron gain events observed. In addition, we found that intron-lost and intron-gained genes had certain similar features, such as similar Gene Ontology categories and expression levels.","doi":"10.1371/journal.pone.0061683","authors":"Zhu T, Niu DK","authors_abbrev":"Zhu T et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-04-25","publication_year":"2013","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11448769","title":"Fission yeast Clp1p phosphatase regulates G2/M transition and coordination of cytokinesis with cell cycle progression.","citation":"Curr Biol 2001 Jun 26;11(12):931-40","abstract":"In Saccharomyces cerevisiae the mitotic-exit network (MEN) functions in anaphase to promote the release of the Cdc14p phosphatase from the nucleolus. This release causes mitotic exit via inactivation of the cyclin-dependent kinase (Cdk). Cdc14p-like proteins are highly conserved; however, it is unclear if these proteins regulate mitotic exit as in S. cerevisiae. In Schizosaccharomyces pombe a signaling pathway homologous to the MEN and termed the septation initiation network (SIN) is required not for mitotic exit, but for initiation of cytokinesis and for a cytokinesis checkpoint that inhibits further cell cycle progression until cytokinesis is complete.\nWe have identified the S. pombe Cdc14p homolog, Clp1p, and show that it is not required for mitotic exit but rather functions together with the SIN in coordinating cytokinesis with the nuclear-division cycle. As cells enter mitosis, Clp1p relocalizes from the nucleolus to the spindle and site of cell division. Clp1p exit from the nucleolus does not depend on the SIN, but the SIN is required for keeping Clp1p out of the nucleolus until completion of cytokinesis. Clp1p, in turn, may promote the activation of the SIN by antagonizing Cdk activity until cytokinesis is complete and thus ensuring that cytokinesis is completed prior to the initiation of the next cell cycle. In addition to its roles in anaphase, Clp1p regulates the G2/M transition since cells deleted for clp1 enter mitosis precociously and cells overexpressing Clp1p delay mitotic entry. Unlike Cdc14p, Clp1p appears to antagonize Cdk activity by preventing dephosphorylation of Cdc2p on tyrosine.\nS. pombe Clp1p affects cell cycle progression in a markedly different manner than its S. cerevisiae homolog, Cdc14p. This finding raises the possibility that related phosphatases in animal cells will prove to have important roles in coordinating the onset of cytokinesis with the events of mitosis.","authors":"Trautmann S, Wolfe BA, Jorgensen P, Tyers M, Gould KL, McCollum D","authors_abbrev":"Trautmann S et al.","pubmed_publication_date":"26 Jun 2001","pubmed_entrez_date":"2001-07-13","publication_year":"2001","canto_session_key":"bd4f213d7cad1349","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-04-29 16:40:39","canto_approved_date":"2025-12-15 22:17:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-22 16:45:50","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPAC4A8.15c","SPAC1782.09c","SPAC1F5.04c","SPBC11B10.09","SPAC9G1.09","SPAC1565.06c","SPAC24B11.11c","SPBC19G7.05c"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2017-04-29"},{"uniquename":"PMID:38499131","title":"The deletion of ppr2 interferes iron sensing and leads to oxidative stress response in Schizosaccharomyces pombe.","citation":"Mitochondrion 2024 Mar 16;:101875","abstract":"Pentatricopeptide repeat proteins are involved in mitochondrial both transcriptional and posttranscriptional regulation. Schizosaccharomyces pombe Ppr2 is a general mitochondrial translation factor that plays a critical role in the synthesis of all mitochondrial DNA-encoded oxidative phosphorylation subunits, which are essential for mitochondrial respiration. Our previous analysis showed that ppr2 deletion resulted in increased expression of iron uptake genes and caused ferroptosis-like cell death in S. pombe. In the present work, we showed that deletion of ppr2 reduced viability on glycerol- and galactose-containing media.Php4 is a transcription repressor that regulates iron homeostasis in fission yeast. We found that in the ppr2 deletion strain, Php4 was constitutively active and accumulated in the nucleus in the stationary phase. We also found that deletion of ppr2 decreased the ferroptosis-related protein Gpx1 in the mitochondria. Overexpression of Gpx1 improves the viability of Δppr2 cells. We showed that the deletion of ppr2 increased the production of ROS, downregulated heme synthesis and iron-sulfur cluster proteins, and induced stress proteins. Finally, we observed the nuclear accumulation of Pap1-GFP and Sty1-GFP, suggesting that Sty1 and Pap1 in response to cellular stress in the ppr2 deletion strain. These results suggest thatppr2 deletion may cause mitochondrial dysfunction, which is likely to lead to iron-sensing defect and iron starvation response, resulting in perturbation of iron homeostasis and increased hydroxyl radical production. The increased hydroxyl radical production triggers cellular responses in theppr2 deletion strain.","doi":"10.1016/j.mito.2024.101875","authors":"Liu Z, Jin T, Qin B, Li R, Shang J, Huang Y","authors_abbrev":"Liu Z et al.","pubmed_publication_date":"16 Mar 2024","pubmed_entrez_date":"2024-03-18","publication_year":"2024","canto_session_key":"c6f8a329b174d4e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying  Luo","canto_first_approved_date":"2024-12-12 19:43:56","canto_approved_date":"2024-12-30 21:16:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-06 14:01:00","canto_added_date":"2024-03-20 00:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying  Luo","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18H10.11c","SPCC965.07c","SPBC1105.14","SPAC1783.07c","SPBC32F12.03c","SPAC1486.01","SPAC140.01","SPAC24B11.06c","SPBC16E9.01c","SPAC22H10.13","SPCC320.09"],"gene_count":11,"ltp_gene_count":2,"approved_date":"2024-12-12"},{"uniquename":"PMID:35781263","title":"Characterization of hexose transporter genes in the views of the chronological life span and glucose uptake in fission yeast.","citation":"J Gen Appl Microbiol 2023 Mar 06;68(6):270-277","abstract":"Fission yeast, Schizosaccharomyces pombe, possesses eight hexose transporters, Ght1~8. In order to clarify the role of each hexose transporter on glucose uptake, a glucose uptake assay system was established and the actual glucose uptake activity of each hexose transporter-deletion mutant was measured. Under normal growth condition containing 2% glucose, ∆ght5 and ∆ght2 mutants showed large and small decrease in glucose uptake activity, respectively. On the other hand, the other deletion mutants did not show any decrease in glucose uptake activity indicating that, in the presence of Ght5 and Ght2, the other hexose transporters do not play a significant role in glucose uptake. To understand the relevance between glucose uptake and lifespan regulation, we measured the chronological lifespan of each hexose transporter deletion mutant, and found that only ∆ght5 mutant showed a significant lifespan extension. Based on these results we showed that Ght5 is mainly involved in the glucose uptake in Schizosaccharomyces pombe, and suggested that the ∆ght5 mutant has prolonged lifespan due to physiological changes similar to calorie restriction.","doi":"10.2323/jgam.2022.05.006","authors":"Maruyama T, Hayashi K, Matsui K, Maekawa Y, Shimasaki T, Ohtsuka H, Shigeaki S, Aiba H","authors_abbrev":"Maruyama T et al.","pubmed_publication_date":"06 Mar 2023","pubmed_entrez_date":"2022-07-05","publication_year":"2023","canto_session_key":"6990ce523b5ad1e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_first_approved_date":"2022-09-27 16:10:40","canto_approved_date":"2025-09-24 07:32:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-27 11:52:11","canto_added_date":"2022-07-07 00:15:04","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":3,"orcid":"0000-0002-7775-0446","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1235.14","SPAC1F8.01","SPCC548.06c","SPBC1683.08","SPBC1348.14c","SPBC4B4.08","SPCC1235.13","SPCC548.07c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2022-09-27"},{"uniquename":"PMID:9472078","title":"Isolation and characterization of the aureobasidin A-resistant gene, aur1R, on Schizosaccharomyces pombe: roles of Aur1p+ in cell morphogenesis.","citation":"Curr Genet 1998 Jan;33(1):38-45","abstract":"To study the mechanism of action of the antibiotic aureobasidin A (AbA) on yeasts, we isolated a dominant mutant of Schizosaccharomyces pombe which gave high resistance to AbA. From a genomic library of the mutant, an aur1R mutant gene conferring AbA resistance was isolated. One amino-acid mutation, a substitution of glycine with cysteine at residue 240, was responsible for the acquisition of AbA resistance. The wild-type aur1+ gene was essential for viability, and its over-expression enhanced significant resistance to AbA. The predicted protein of S. pombe aur1R was highly homologous in primary structure and hydropathy profile with that of Saccharomyces cerevisiae AUR1R isolated as an AbA-resistance gene. To analyze a role in cell growth of S. pombe aur1+, temperature-sensitive mutants (aur1ts) were obtained by random mutagenesis procedures using a modified PCR. The aur1ts mutation caused a defect in cell elongation at the non-permissive temperature and finally led to cell death. These results suggest that Aur1p was a target of the antibiotic AbA and was required in the cell elongation of cell-end tips and in the viability of S. pombe.","authors":"Hashida-Okado T, Yasumoto R, Endo M, Takesako K, Kato I","authors_abbrev":"Hashida-Okado T et al.","pubmed_publication_date":"Jan 1998","pubmed_entrez_date":"1998-04-04","publication_year":"1998","canto_session_key":"74cf5c6bbcf50d38","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-06-30 10:48:13","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-26 09:16:52","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H8.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-26"},{"uniquename":"PMID:25106872","title":"Quantification of DNA-associated proteins inside eukaryotic cells using single-molecule localization microscopy.","citation":"Nucleic Acids Res 2014 Oct 29;42(19):e146","abstract":"Development of single-molecule localization microscopy techniques has allowed nanometre scale localization accuracy inside cells, permitting the resolution of ultra-fine cell structure and the elucidation of crucial molecular mechanisms. Application of these methodologies to understanding processes underlying DNA replication and repair has been limited to defined in vitro biochemical analysis and prokaryotic cells. In order to expand these techniques to eukaryotic systems, we have further developed a photo-activated localization microscopy-based method to directly visualize DNA-associated proteins in unfixed eukaryotic cells. We demonstrate that motion blurring of fluorescence due to protein diffusivity can be used to selectively image the DNA-bound population of proteins. We designed and tested a simple methodology and show that it can be used to detect changes in DNA binding of a replicative helicase subunit, Mcm4, and the replication sliding clamp, PCNA, between different stages of the cell cycle and between distinct genetic backgrounds.","doi":"10.1093/nar/gku726","authors":"Etheridge TJ, Boulineau RL, Herbert A, Watson AT, Daigaku Y, Tucker J, George S, Jönsson P, Palayret M, Lando D, Laue E, Osborne MA, Klenerman D, Lee SF, Carr AM","authors_abbrev":"Etheridge TJ et al.","pubmed_publication_date":"29 Oct 2014","pubmed_entrez_date":"2014-08-10","publication_year":"2014","canto_session_key":"a15df87245a922db","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-12 01:15:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31538680","title":"The fission yeast FHIT homolog affects checkpoint control of proliferation and is regulated by mitochondrial electron transport.","citation":"Cell Biol Int 2020 Feb;44(2):412-423","abstract":"Genetic analysis has strongly implicated human FHIT (Fragile Histidine Triad) as a tumor suppressor gene, being mutated in a large proportion of early-stage cancers. The functions of the FHIT protein have, however, remained elusive. Here, we investigated aph1 +  , the fission yeast homolog of FHIT, for functions related to checkpoint control and oxidative metabolism. In sublethal concentrations of DNA damaging agents, aph1Δ mutants grew with a substantially shorter lag phase. In aph1Δ mutants carrying a hypomorphic allele of cds1 (the fission yeast homolog of Chk2), in addition, increased chromosome fragmentation and missegregation were found. We also found that under hypoxia or impaired electron transport function, the Aph1 protein level was strongly depressed. Previously, FHIT has been linked to regulation of the human 9-1-1 checkpoint complex constituted by Hus1, Rad1, and Rad9. In Schizosaccharomyces pombe, the levels of all three 9-1-1 proteins are all downregulated by hypoxia in similarity with Aph1. Moreover, deletion of the aph1 +  gene reduced the Rad1 protein level, indicating a direct relationship between these two proteins. We conclude that the fission yeast FHIT homolog has a role in modulating DNA damage checkpoint function, possibly through an effect on the 9-1-1 complex, and that this effect may be critical under conditions of limiting oxidative metabolism and reoxygenation.","doi":"10.1002/cbin.11241","authors":"Sjölander JJ, Sunnerhagen P","authors_abbrev":"Sjölander JJ et al.","pubmed_publication_date":"Feb 2020","pubmed_entrez_date":"2019-09-21","publication_year":"2020","canto_session_key":"c5c033ad2e33e885","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Per Sunnerhagen","canto_first_approved_date":"2019-10-16 10:12:46","canto_approved_date":"2024-04-02 11:39:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-17 17:14:11","canto_added_date":"2019-09-22 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Per Sunnerhagen","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c","SPAC1952.07","SPCC18B5.11c","SPCC1259.13","SPAC20G4.04c","SPCC4G3.02"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2019-10-16"},{"uniquename":"PMID:29191370","title":"LINC complexes and nuclear positioning.","citation":"Semin Cell Dev Biol 2018 Oct;82:67-76","abstract":"One of the characteristics of eukaryotic cells is their structural plasticity associated with the ability to carry out a broad range of complex functions, both autonomously and as components of tissues and organs. Major cellular rearrangements can be observed in various systems from meiosis in fission yeast, through dermal differentiation in nematodes, to muscle and neuronal development in vertebrates. Each of these processes involves oftentimes dramatic relocation of the nucleus within the cell. During the last decade it has become apparent that the nuclear periphery represents a nexus of cytoskeletal interactions that are involved not only in nuclear movement but also in the distribution and dissemination of mechanical forces throughout the cell. Nucleocytoskeletal coupling is mediated in large part by SUN- and KASH-domain proteins of the nuclear membranes, that together assemble to form LINC (Linker of the Nucleoskeleton and Cytoskeleton) complexes. In this review we will describe how the LINC complex repertoire contributes to nuclear positioning and chromosome dynamics in a variety of cellular contexts.","doi":"10.1016/j.semcdb.2017.11.008","authors":"Lee YL, Burke B","authors_abbrev":"Lee YL et al.","pubmed_publication_date":"Oct 2018","pubmed_entrez_date":"2017-12-02","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-12-03 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19075108","title":"Assembly of normal actomyosin rings in the absence of Mid1p and cortical nodes in fission yeast.","citation":"J Cell Biol 2008 Dec 15;183(6):979-88","abstract":"Cytokinesis in many eukaryotes depends on the function of an actomyosin contractile ring. The mechanisms regulating assembly and positioning of this ring are not fully understood. The fission yeast Schizosaccharomyces pombe divides using an actomyosin ring and is an attractive organism for the study of cytokinesis. Recent studies in S. pombe (Wu, J.Q., V. Sirotkin, D.R. Kovar, M. Lord, C.C. Beltzner, J.R. Kuhn, and T.D. Pollard. 2006. J. Cell Biol. 174:391-402; Vavylonis, D., J.Q. Wu, S. Hao, B. O'Shaughnessy, and T.D. Pollard. 2008. Science. 319:97-100) have suggested that the assembly of the actomyosin ring is initiated from a series of cortical nodes containing several components of this ring. These studies have proposed that actomyosin interactions bring together the cortical nodes to form a compacted ring structure. In this study, we test this model in cells that are unable to assemble cortical nodes. Although the cortical nodes play a role in the timing of ring assembly, we find that they are dispensable for the assembly of orthogonal actomyosin rings. Thus, a mechanism that is independent of cortical nodes is sufficient for the assembly of normal actomyosin rings.","doi":"10.1083/jcb.200806151","authors":"Huang Y, Yan H, Balasubramanian MK","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"15 Dec 2008","pubmed_entrez_date":"2008-12-17","publication_year":"2008","canto_session_key":"a765c0082a3d7619","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-29 08:01:14","canto_approved_date":"2024-06-26 17:02:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-23 09:39:58","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":20,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPCC4B3.15","SPBC19G7.05c","SPAC926.03","SPAC6F6.08c","SPAC20G8.05c","SPAC1F5.04c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2024-04-29"},{"uniquename":"PMID:10082789","title":"Expression of the ADP/ATP carrier encoding genes in aerobic yeasts; phenotype of an ADP/ATP carrier deletion mutant of Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1999 Mar 09;1410(3):229-36","abstract":"The expression of a key mitochondrial membrane component, the ADP/ATP carrier, was investigated in two aerobic yeast species, Kluyveromyces lactis and Schizosaccharomyces pombe. Although the two species differ very much in their respiratory capacity, the expression of the carrier in both yeast species was decreased under partially anaerobic conditions and was induced by nonfermentable carbon sources. The single ADP/ATP carrier encoding gene was deleted in S. pombe. The null mutant exhibits impaired growth properties, especially when cultivated at reduced oxygen tension, and is unable to grow on a nonfermentable carbon source. Our results suggest that the inability of K. lactis and S. pombe to grow under anaerobic conditions can be related in part to the absence of a functional ADP/ATP carrier due to repression of the corresponding gene expression.","authors":"Trézéguet V, Zeman I, David C, Lauquin GJ, Kolarov J","authors_abbrev":"Trézéguet V et al.","pubmed_publication_date":"09 Mar 1999","pubmed_entrez_date":"1999-03-20","publication_year":"1999","canto_session_key":"b95de8f0b05adc82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-08 09:49:07","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-01 22:16:28","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC530.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-01"},{"uniquename":"PMID:34736160","title":"The local integration preference of the Tf1 retrotransposon in Schizosaccharomyces pombe.","citation":"Virology 2022 Jan 02;565:52-57","abstract":"Transposons are mobile DNAs that can move to different locations in host genomes. The integration site selection of transposons is critical for both themselves and host cells. Studies on the integration of retrotransposons and retroviruses have focused more on the global preference than on the local preference. The local preferences of retrotransposons are usually weak and of large diversity. Here, we analyzed hundreds of thousands of independent integration events of the Tf1 retrotransposon in Schizosaccharomyces pombe. The consensus sequence at the Tf1 integration sites shows a palindromic pattern, which can be divided into four sections, each of them contains one or more CGnTA units with a period of 10 base pairs, indicating interaction with subunits of the integrase oligomer in the pre-integration complex. Moreover, the analysis on the nucleosome occupancy flanking Tf1 target sites shows that Tf1 integration favors regions with one entire nucleosome depletion.","doi":"10.1016/j.virol.2021.10.008","authors":"Cui Y, Guo Y","authors_abbrev":"Cui Y et al.","pubmed_publication_date":"02 Jan 2022","pubmed_entrez_date":"2021-11-04","publication_year":"2022","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2021-11-06 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28455011","title":"Use of Schizosaccharomyces pombe and Torulaspora delbrueckii strains in mixed and sequential fermentations to improve red wine sensory quality.","citation":"Food Res Int 2015 Oct;76(Pt 3):325-333","abstract":"One of the main opportunities in the use of non-Saccharomyces yeasts is its great intraspecific variability in relation to the synthesis of secondary products of fermentation. Thus, mixed or sequential fermentation with non-Saccharomyces can increase the synthesis of certain metabolites that are important for colour stability, such as acetaldehyde and pyruvic acid (vitisin precursors) or vinylphenols (vinylphenolic pyranoanthocyanin precursors). Furthermore, the selection and use of non-Saccharomyces yeast strains with good yields in the production of certain volatile compounds (ethyl lactate, 2,3-butanediol, 2-phenylethyl acetate), with limited formation of higher alcohols, is a way to improve the aromatic profile of red wine. The main aim of this work was to evaluate the influence of sequential and mixed fermentations with Schizosaccharomyces pombe and Torulaspora delbrueckii strains on red wine's sensory quality. Anthocyanins and aromatic profiles, as well as glycerol and organic acid content, were analysed in the red wines obtained. Results show that, in general, mixed fermentations can promote an increment in polyols synthesis, while sequential fermentations can enhance the herbaceous aroma. Moreover, the use of T. delbrueckii in mixed fermentations allowed an increase to the fruity character of red wine. The use of S. pombe in sequential fermentations increased the stability of the colouring matter by favouring vitisins and vinylphenolic pyranoanthocyanin formation.","doi":"10.1016/j.foodres.2015.06.030","authors":"Loira I, Morata A, Comuzzo P, Callejo MJ, González C, Calderón F, Suárez-Lepe JA","authors_abbrev":"Loira I et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2017-04-30","publication_year":"2015","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2017-05-02 00:15:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010030","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17932486","title":"Aurora controls sister kinetochore mono-orientation and homolog bi-orientation in meiosis-I.","citation":"EMBO J 2007 Oct 31;26(21):4475-86","abstract":"Aurora-B kinases are important regulators of mitotic chromosome segregation, where they are required for the faithful bi-orientation of sister chromatids. In contrast to mitosis, sister chromatids have to be oriented toward the same spindle pole in meiosis-I, while homologous chromosomes are bi-oriented. We find that the fission yeast Aurora kinase Ark1 is required for the faithful bi-orientation of sister chromatids in mitosis and of homologous chromosomes in meiosis-I. Unexpectedly, Ark1 is also necessary for the faithful mono-orientation of sister chromatids in meiosis-I, even though the canonical mono-orientation pathway, which depends on Moa1 and Rec8, seems intact. Our data suggest that Ark1 prevents unified sister kinetochores during metaphase-I from merotelic attachment to both spindle poles and thus from being torn apart during anaphase-I, revealing a novel mechanism promoting monopolar attachment. Furthermore, our results provide an explanation for the previously enigmatic observation that fission yeast Shugoshin Sgo2, which assists in loading Aurora to centromeres, and its regulator Bub1 are required for the mono-orientation of sister chromatids in meiosis-I.","authors":"Hauf S, Biswas A, Langegger M, Kawashima SA, Tsukahara T, Watanabe Y","authors_abbrev":"Hauf S et al.","pubmed_publication_date":"31 Oct 2007","pubmed_entrez_date":"2007-10-13","publication_year":"2007","canto_session_key":"e15de5eadc4ac81c","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17714654","title":"Mitosis: ran scales the alps of spindle formation.","citation":"Curr Biol 2007 Aug 21;17(16):R643-5","abstract":"Alp7/TACC has been identified as an important target for Ran GTPase in spindle formation in fission yeast. This discovery underlines a general role for Ran in orchestrating mitosis in all eukaryotes.","authors":"Clarke PR, Sazer S","authors_abbrev":"Clarke PR et al.","pubmed_publication_date":"21 Aug 2007","pubmed_entrez_date":"2007-08-24","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20692117","title":"In vitro assay of the interaction between Rnc1 protein and Pmp1 mRNA by affinity capillary electrophoresis with a carboxylated capillary.","citation":"J Pharm Biomed Anal 2010 Dec 15;53(5):1332-7","abstract":"The interaction between Rnc1, an RNA interactive protein, and a Pmp1 mRNA was investigated by affinity capillary electrophoresis (ACE). Prior to the ACE experiments, the column performances of three capillaries (an untreated fused silica capillary, a polybrene-polyacrylic acid (PB-PAA) double layer coating capillary, and a carboxylated capillary with a covalent modification) were studied with model proteins including ribonuclease B (RNase B) and bovine serum albumin (BSA). Using an untreated fused silica and a PB-PAA double layer coating capillaries, both of the protein peaks were broad and tailing. However, using a carboxylated capillary, the protein peaks were sharp and symmetric, and migration times were repeatable (RSD<0.4%). Further, the proteins in human serum also gave sharp peaks and its repeatability was kept at a high level by pre-treatment of a capillary inner wall with 1M sodium chloride solution before each run. An Rnc1 protein was analyzed by ACE with background electrolytes containing various concentrations of Pmp1 sense mRNA using a carboxylated capillary. Increase in the concentration of the mRNA was found to delay the migration time of the protein. But the migration time of the protein was kept constant with increasing Pmp1 anti-sense mRNA instead of Pmp1 sense mRNA. A straight line (r=0.987) was obtained by plotting 1/(migration time shift) versus 1/(Pmp1 sense mRNA concentration) and the association constant of Rnc1 protein with Pmp1 sense mRNA could be estimated to be 4.15x10(6)M(-1). These results suggest that the association constants of proteins with mRNAs as ligands were easily determined by the proposed method.","doi":"10.1016/j.jpba.2010.07.009","authors":"Taga A, Satoh R, Ishiwata S, Kodama S, Sato A, Suzuki K, Sugiura R","authors_abbrev":"Taga A et al.","pubmed_publication_date":"15 Dec 2010","pubmed_entrez_date":"2010-08-10","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC757.09c","SPBC1685.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:34302476","title":"The RGG domain in the C-terminus of the DEAD box helicases Dbp2 and Ded1 is necessary for G-quadruplex destabilization.","citation":"Nucleic Acids Res 2021 Aug 20;49(14):8339-8354","abstract":"The identification of G-quadruplex (G4) binding proteins and insights into their mechanism of action are important for understanding the regulatory functions of G4 structures. Here, we performed an unbiased affinity-purification assay coupled with mass spectrometry and identified 30 putative G4 binding proteins from the fission yeast Schizosaccharomyces pombe. Gene ontology analysis of the molecular functions enriched in this pull-down assay included mRNA binding, RNA helicase activity, and translation regulator activity. We focused this study on three of the identified proteins that possessed putative arginine-glycine-glycine (RGG) domains, namely the Stm1 homolog Oga1 and the DEAD box RNA helicases Dbp2 and Ded1. We found that Oga1, Dbp2, and Ded1 bound to both DNA and RNA G4s in vitro. Both Dbp2 and Ded1 bound to G4 structures through the RGG domain located in the C-terminal region of the helicases, and point mutations in this domain weakened the G4 binding properties of the helicases. Dbp2 and Ded1 destabilized less thermostable G4 RNA and DNA structures, and this ability was independent of ATP but dependent on the RGG domain. Our study provides the first evidence that the RGG motifs in DEAD box helicases are necessary for both G4 binding and G4 destabilization.","doi":"10.1093/nar/gkab620","authors":"Yan KK, Obi I, Sabouri N","authors_abbrev":"Yan KK et al.","pubmed_publication_date":"20 Aug 2021","pubmed_entrez_date":"2021-07-24","publication_year":"2021","canto_session_key":"689a38d72e4c0146","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-07-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12898395","title":"Learning from yeasts: intracellular sensing of stress conditions.","citation":"Int Microbiol 2003 Sep;6(3):211-9","abstract":"One intriguing challenge in modern biology is to understand how cells respond to, and distinguish between different stressing stimuli. Evidence accumulated in recent years indicates that a network of signaling pathways extends from the plasma membrane to the very core of the cell nucleus to transduce environmental changes into a graded transcriptional response. Although many steps still remain unclear, studies on the stress-activated protein kinase (SAPK) pathways and related mechanisms provide insight into the biochemistry that regulates signal transmission and leads to outcomes such as cell adaptation and differentiation. This review focuses on selected topics of current interest related to the sensing of stress signals in cells of the fission yeast Schizosaccharomyces pombe. Because signaling pathways appear to be evolutionarily well conserved, yeasts may be useful models to learn how higher eukaryotes sense and respond to stresses at the cellular level.","authors":"Gacto M, Soto T, Vicente-Soler J, Villa TG, Cansado J","authors_abbrev":"Gacto M et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-08-05","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22160913","title":"Heterologous gene expression by chromosomal integration in fission yeast.","citation":"Methods Mol Biol 2012;824:433-50","abstract":"Thanks to the convenience and flexibility of the multicopy plasmid-based approach for heterologous gene expression, this technique has long been used for biological studies, especially in prokaryotes and lower eukaryotes. For better understanding of biological mechanisms, however, there are increasing demands on the experimental technologies enabling fine-tuned expression of introduced heterologous genes or serving conditions that are closer to the physiological conditions. For this purpose, the use of direct tagging of a chromosomal gene has been gradually increasing, although the use conditions of this approach are relatively limited compared to plasmid-based methods. Expression of a cloned gene using chromosomal integration has a property intermediate between multicopy plasmid-based method and direct tagging of an endogenous gene. Here, we describe the principle and methods of introduction of a cloned gene into the targeting loci of the chromosome in fission yeast.","doi":"10.1007/978-1-61779-433-9_23","authors":"Matsuyama A, Yoshida M","authors_abbrev":"Matsuyama A et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2011-12-14","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25468341","title":"Dynamic network morphology and tension buildup in a 3D model of cytokinetic ring assembly.","citation":"Biophys J 2014 Dec 02;107(11):2618-28","abstract":"During fission yeast cytokinesis, actin filaments nucleated by cortical formin Cdc12 are captured by myosin motors bound to a band of cortical nodes and bundled by cross-linking proteins. The myosin motors exert forces on the actin filaments, resulting in a net pulling of the nodes into a contractile ring, while cross-linking interactions help align actin filaments and nodes into a single bundle. We used these mechanisms in a three-dimensional computational model of contractile ring assembly, with semiflexible actin filaments growing from formins at cortical nodes, capturing of filaments by neighboring nodes, and cross-linking among filaments through attractive interactions. The model was used to predict profiles of actin filament density at the cell cortex, morphologies of condensing node-filament networks, and regimes of cortical tension by varying the node pulling force and strength of cross-linking among actin filaments. Results show that cross-linking interactions can lead to confinement of actin filaments at the simulated cortical boundary. We show that the ring-formation region in parameter space lies close to regions leading to clumps, meshworks or double rings, and stars/cables. Since boundaries between regions are not sharp, transient structures that resemble clumps, stars, and meshworks can appear in the process of ring assembly. These results are consistent with prior experiments with mutations in actin-filament turnover regulators, myosin motor activity, and changes in the concentration of cross-linkers that alter the morphology of the condensing network. Transient star shapes appear in some simulations, and these morphologies offer an explanation for star structures observed in prior experimental images. Finally, we quantify tension along actin filaments and forces on nodes during ring assembly and show that the mechanisms describing ring assembly can also drive ring constriction once the ring is formed.","doi":"10.1016/j.bpj.2014.10.034","authors":"Bidone TC, Tang H, Vavylonis D","authors_abbrev":"Bidone TC et al.","pubmed_publication_date":"02 Dec 2014","pubmed_entrez_date":"2014-12-04","publication_year":"2014","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2014-12-05 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF266750","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10672936","title":"Cloning, nucleotide sequence and expression of thioltransferase (glutaredoxin) cDNA from Schizosaccharomyces pombe.","citation":"Mol Cells 1999 Dec 31;9(6):668-72","abstract":"Thioltransferase (TTase), also known as glutaredoxin (Grx), is an enzyme that catalyzes the reduction of a variety of disulfide compounds, including protein disulfides, in the presence of reduced glutathione. TTase acts as a cofactor for various enzymes such as ribonucleotide reductase. We previously purified a TTase from Schizosaccharomyces pombe and its molecular size was determined. In the present study, a cDNA coding TTase was isolated from a cDNA library of Schizosaccharomyces pombe by colony hybridization, which was constructed in a plasmid vector pGAD GH, and its corresponding insert was confirmed by Southern hybridization. The nucleotide sequence of the 375 bp long cDNA clone reveals an open reading frame, which encodes a protein of 101 amino acids. The coding region of the original clone was transferred after the lac promoter of pUC13 vector for expression in E. coli, and simultaneously, a suitable Shine-Dalgarno (SD) sequence was added in front of the coding region by PCR. The two primers used for PCR also separately contained BamHI and HindIII restriction sites. The E. coli strain (A434) harboring the pUC13 derivative pKU10 showed a 17.3-fold increase in TTase activity compared to the strain with only the vector plasmid.","authors":"Kim HG, Cho YW, Park EH, Park SS, Ahn KS, Lim CJ","authors_abbrev":"Kim HG et al.","pubmed_publication_date":"31 Dec 1999","pubmed_entrez_date":"2000-02-15","publication_year":"1999","canto_session_key":"fedb189054811ca2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-19 10:12:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 09:25:19","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F10.20"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-05"},{"uniquename":"PMID:8532516","title":"Positive and negative roles for cdc10 in cell cycle gene expression.","citation":"Nucleic Acids Res 1995 Dec 11;23(23):4761-8","abstract":"In this paper we describe properties of the cdc10-C4 mutant of the fission yeast Schizosaccharomyces pombe. The cdc10+ gene encodes a component of the DSC1Sp/MBF transcription complex, which is required for cell-cycle regulated expression at G1-S of several genes via cis-acting MCB (MIuI cell cycle box) elements. At permissive temperatures cdc10-C4 causes expression of MCB-regulated genes through the whole cell cycle, which in asynchronously dividing cells is manifested in overall higher expression levels. This overexpression phenotype is cold sensitive: in cdc10-C4 cells, MCB genes are expressed offprogressively higher levels at lower temperatures. In heterozygous cdc10-C4/cdc10+ diploid strains, MCB-regulated genes are not overexpressed, suggesting that loss, rather than alteration, of function of the cdc10-C4 gene product is the reason for unregulated target gene expression. Consistent with this, the cdc10-C4 mutant allele is known to encode a truncated protein. We have also overexpressed the region of the cdc10 protein absent in cdc10-C4 under the control of an inducible promoter. This induces a G1 delay, and additionally causes a reduction of the overexpression of MCB genes in cdc10-C4 strains. These results suggest that DSC1Sp/MBF represses, as well as activates, MCB gene expression during the cell cycle.","authors":"McInerny CJ, Kersey PJ, Creanor J, Fantes PA","authors_abbrev":"McInerny CJ et al.","pubmed_publication_date":"11 Dec 1995","pubmed_entrez_date":"1995-12-11","publication_year":"1995","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:607151","title":"Characterisation of the ribosomal proteins from Schizosaccharomyces pombe by two-dimensional polyacrylamide gel electrophoresis: demonstration that a cycloheximide resistant strain, cyh1, has an altered 60S ribosomal protein.","citation":"Mol Gen Genet 1977 Dec 14;158(1):93-100","abstract":"","authors":"Coddington A, Fluri R","authors_abbrev":"Coddington A et al.","pubmed_publication_date":"14 Dec 1977","pubmed_entrez_date":"1977-12-14","publication_year":"1977","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23219921","title":"The type-2 N-end rule peptide recognition activity of Ubr11 ubiquitin ligase is required for the expression of peptide transporters.","citation":"FEBS Lett 2013 Jan 16;587(2):214-9","abstract":"The Ubr1-like canonical N-recognins, widely conserved ubiquitin ligases in eukaryotes, play a role in the N-end rule pathway-mediated degradation of substrates harboring basic (type-1) or bulky hydrophobic (type-2) amino acids at the N-terminus. In this study, the roles of conserved domains were studied in the Schizosaccharomyces pombe Ubr11 protein. Mutations in the UBR box and the autoinhibitory domain blocked degradation of both type-1 and type-2 substrates, expression of peptide transporter genes, and the uptake of oligopeptides. An N-domain mutant was normal for the type-1-related function, but nevertheless failed to express peptide transporters. These data suggest the importance of the type-2-related activity of Ubr11 for its in vivo function.","doi":"10.1016/j.febslet.2012.11.028","authors":"Kitamura K, Fujiwara H","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"16 Jan 2013","pubmed_entrez_date":"2012-12-11","publication_year":"2013","canto_session_key":"216267cfd237d459","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9950674","title":"Liz1p, a novel fission yeast membrane protein, is required for normal cell division when ribonucleotide reductase is inhibited.","citation":"Mol Biol Cell 1999 Feb;10(2):245-57","abstract":"Ribonucleotide reductase activity is required for generating deoxyribonucleotides for DNA replication. Schizosaccharomyces pombe cells lacking ribonucleotide reductase activity arrest during S phase of the cell cycle. In a screen for hydroxyurea-sensitive mutants in S. pombe, we have identified a gene, liz1(+), which when mutated reveals an additional, previously undescribed role for ribonucleotide reductase activity during mitosis. Inactivation of ribonucleotide reductase, by either hydroxyurea or a cdc22-M45 mutation, causes liz1(-) cells in G2 to undergo an aberrant mitosis, resulting in chromosome missegregation and late mitotic arrest. liz1(+) encodes a 514-amino acid protein with strong similarity to a family of transmembrane transporters, and localizes to the plasma membrane of the cell. These results reveal an unexpected G2/M function of ribonucleotide reductase and establish that defects in a transmembrane protein can affect cell cycle progression.","authors":"Moynihan EB, Enoch T","authors_abbrev":"Moynihan EB et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-02-09","publication_year":"1999","canto_session_key":"33ab85af0ca986c2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-17 19:55:16","canto_approved_date":"2021-01-06 17:33:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-06-12 10:09:27","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPBC2G2.01c","SPCC18B5.03","SPBC18H10.20c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-06-17"},{"uniquename":"PMID:10446227","title":"Characterization of the rhp7(+) and rhp16(+) genes in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1999 Sep 01;27(17):3410-6","abstract":"The global genome repair (GGR) subpathway of nucleotide excision repair (NER) is capable of removing lesions throughout the genome. In Saccharomyces cerevisiae the RAD7 and RAD16 genes are essential for GGR. Here we identify rhp7 (+), the RAD7 homolog in Schizosaccharomyces pombe. Surprisingly, rhp7 (+)and the previously cloned rhp16 (+)are located very close together and are transcribed in opposite directions. Upon UV irradiation both genes are induced, reaching a maximum level after 45-60 min. These observations suggest that the genes are co-regulated. Schizo-saccharomyces pombe rhp7 or rhp16 deficient cells are, in contrast to S.cerevisiae rad7 and rad16 mutants, not sensitive to UV irradiation. In S.pombe an alternative repair mechanism, UV damage repair (UVDR), is capable of efficiently removing photolesions from DNA. In the absence of this UVDR pathway both rhp7 and rhp16 deficient cells display an enhanced UV sensitivity. Epistatic analyses show that rhp7 (+)and rhp16 (+)are only involved in NER. Repair analyses at nucleotide resolution demonstrate that both Rhp7 and Rhp16, probably acting in a complex, are essential for GGR in S.pombe.","authors":"Lombaerts M, Peltola PH, Visse R, den Dulk H, Brandsma JA, Brouwer J","authors_abbrev":"Lombaerts M et al.","pubmed_publication_date":"01 Sep 1999","pubmed_entrez_date":"1999-08-14","publication_year":"1999","canto_session_key":"5ff8a765c2b2c7e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-13 15:56:19","canto_approved_date":"2025-02-27 06:59:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-13 15:56:12","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.02","SPBC3E7.08c","SPBC19C7.09c","SPCC330.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-04-13"},{"uniquename":"PMID:22928710","title":"Comparative chemogenomics to examine the mechanism of action of dna-targeted platinum-acridine anticancer agents.","citation":"ACS Chem Biol 2012 Nov 16;7(11):1892-901","abstract":"Platinum-based drugs have been used to successfully treat diverse cancers for several decades. Cisplatin, the original compound of this class, cross-links DNA, resulting in cell cycle arrest and cell death via apoptosis. Cisplatin is effective against several tumor types, yet it exhibits toxic side effects and tumors often develop resistance. To mitigate these liabilities while maintaining potency, we generated a library of non-classical platinum-acridine hybrid agents and assessed their mechanisms of action using a validated genome-wide screening approach in Saccharomyces cerevisiae and in the distantly related yeast Schizosaccharomyces pombe. Chemogenomic profiles from both S. cerevisiae and S. pombe demonstrate that several of the platinum-acridines damage DNA differently than cisplatin based on their requirement for distinct modules of DNA repair.","doi":"10.1021/cb300320d","authors":"Cheung-Ong K, Song KT, Ma Z, Shabtai D, Lee AY, Gallo D, Heisler LE, Brown GW, Bierbach U, Giaever G, Nislow C","authors_abbrev":"Cheung-Ong K et al.","pubmed_publication_date":"16 Nov 2012","pubmed_entrez_date":"2012-08-30","publication_year":"2012","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19400965","title":"Regulation of chk1.","citation":"Cell Div 2009 Apr 29;4:8","abstract":"Chk1 is a serine/threonine protein kinase that is the effector of the G2 DNA damage checkpoint. Chk1 homologs have a highly conserved N-terminal kinase domain, and a less conserved C-terminal regulatory domain of ~200 residues. In response to a variety of genomic lesions, a number of proteins collaborate to activate Chk1, which in turn ensures that the mitotic cyclin-dependent kinase Cdc2 remains in an inactive state until DNA repair is completed. Chk1 activation requires the phosphorylation of residues in the C-terminal domain, and this is catalyzed by the ATR protein kinase. How phosphorylation of the C-terminal regulatory domain activates the N-terminal kinase domain has not been elucidated, though some studies have suggested that this phosphorylation relieves an inhibitory intramolecular interaction between the N- and C-termini. However, recent studies in the fission yeast Schizosaccharomyces pombe have revealed that there is more to Chk1 regulation than this auto-inhibition model, and we review these findings and their implication to the biology of this genome integrity determinant.","doi":"10.1186/1747-1028-4-8","authors":"Tapia-Alveal C, Calonge TM, O'Connell MJ","authors_abbrev":"Tapia-Alveal C et al.","pubmed_publication_date":"29 Apr 2009","pubmed_entrez_date":"2009-04-30","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40042941","title":"PP2A-B56 regulates Mid1 protein levels for proper cytokinesis in fission yeast.","citation":"Mol Biol Cell 2025 Mar 05;:mbcE24080382","abstract":"Protein phosphorylation regulates many steps in the cell division process including cytokinesis. In fission yeast cells, the anillin-like protein Mid1 sets the cell division plane and is regulated by phosphorylation. Multiple protein kinases act on Mid1, but no protein phosphatases have been shown to regulate Mid1. Here, we discovered that the conserved protein phosphatase PP2A-B56 is required for proper cytokinesis by promoting Mid1 protein levels. We find that  par1∆  cells lacking the primary B56 subunit divide asymmetrically due to the assembly of misplaced cytokinetic rings that slide towards cell tips. These  par1∆  mutants have reduced whole-cell levels of Mid1 protein, leading to reduced Mid1 at the cytokinetic ring. Restoring proper Mid1 expression suppresses  par1∆  cytokinesis defects. This work identifies a new PP2A-B56 pathway regulating cytokinesis through Mid1, with implications for control of cytokinesis in other organisms.","doi":"10.1091/mbc.E24-08-0382","authors":"Chrupcala ML, Moseley JB","authors_abbrev":"Chrupcala ML et al.","pubmed_publication_date":"05 Mar 2025","pubmed_entrez_date":"2025-03-05","publication_year":"2025","canto_session_key":"9b854fc50b3860b8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-03-06 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4938688","title":"The initiation of cell wall synthesis in parasynchronous cultures of Schizosaccharomyces pombe.","citation":"Arch Mikrobiol 1971;78(3):205-13","abstract":"","authors":"Marchant R","authors_abbrev":"Marchant R","pubmed_publication_date":"1971","pubmed_entrez_date":"1971-01-01","publication_year":"1971","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17006448","title":"Co-evolution of transcriptional and post-translational cell-cycle regulation.","citation":"Nature 2006 Oct 05;443(7111):594-7","abstract":"DNA microarray studies have shown that hundreds of genes are transcribed periodically during the mitotic cell cycle of humans, budding yeast, fission yeast and the plant Arabidopsis thaliana. Here we show that despite the fact the protein complexes involved in this process are largely the same among all eukaryotes, their regulation has evolved considerably. Our comparative analysis of several large-scale data sets reveals that although the regulated subunits of each protein complex are expressed just before its time of action, the identity of the periodically expressed proteins differs significantly between organisms. Moreover, we show that these changes in transcriptional regulation have co-evolved with post-translational control independently in several lineages; loss or gain of cell-cycle-regulated transcription of specific genes is often mirrored by changes in phosphorylation of the proteins that they encode. Our results indicate that many different solutions have evolved for assembling the same molecular machines at the right time during the cell cycle, involving both transcriptional and post-translational layers that jointly control the dynamics of biological systems.","authors":"Jensen LJ, Jensen TS, de Lichtenberg U, Brunak S, Bork P","authors_abbrev":"Jensen LJ et al.","pubmed_publication_date":"05 Oct 2006","pubmed_entrez_date":"2006-09-29","publication_year":"2006","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32277274","title":"Conserved roles of chromatin remodellers in cohesin loading onto chromatin.","citation":"Curr Genet 2020 Oct;66(5):951-956","abstract":"Cohesin is a conserved, ring-shaped protein complex that topologically entraps DNA. This ability makes this member of the structural maintenance of chromosomes (SMC) complex family a central hub of chromosome dynamics regulation. Besides its essential role in sister chromatid cohesion, cohesin shapes the interphase chromatin domain architecture and plays important roles in transcriptional regulation and DNA repair. Cohesin is loaded onto chromosomes at centromeres, at the promoters of highly expressed genes, as well as at DNA replication forks and sites of DNA damage. However, the features that determine these binding sites are still incompletely understood. We recently described a role of the budding yeast RSC chromatin remodeler in cohesin loading onto chromosomes. RSC has a dual function, both as a physical chromatin receptor of the Scc2/Scc4 cohesin loader complex, as well as by providing a nucleosome-free template for cohesin loading. Here, we show that the role of RSC in sister chromatid cohesion is conserved in fission yeast. We discuss what is known about the broader conservation of the contribution of chromatin remodelers to cohesin loading onto chromatin.","doi":"10.1007/s00294-020-01075-x","authors":"Muñoz S, Passarelli F, Uhlmann F","authors_abbrev":"Muñoz S et al.","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-04-12","publication_year":"2020","canto_session_key":"876a4a699dfe65d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sofía Muñoz","canto_first_approved_date":"2020-05-06 13:14:50","canto_approved_date":"2022-09-21 11:52:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-27 18:47:34","canto_added_date":"2020-04-13 00:15:04","annotation_curators":[{"name":"Sofía Muñoz","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPCC1620.14c","SPAC1687.18c","SPAC11E3.01c","SPBP35G2.10","SPAC1250.01","SPAC3G6.01","SPAC1783.05"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2020-05-06"},{"uniquename":"PMID:22084384","title":"A quantitative model for cyclin-dependent kinase control of the cell cycle: revisited.","citation":"Philos Trans R Soc Lond B Biol Sci 2011 Dec 27;366(1584):3572-83","abstract":"The eukaryotic cell division cycle encompasses an ordered series of events. Chromosomal DNA is replicated during S phase of the cell cycle before being distributed to daughter cells in mitosis. Both S phase and mitosis in turn consist of an intricately ordered sequence of molecular events. How cell cycle ordering is achieved, to promote healthy cell proliferation and avert insults on genomic integrity, has been a theme of Paul Nurse's research. To explain a key aspect of cell cycle ordering, sequential S phase and mitosis, Stern & Nurse proposed 'A quantitative model for cdc2 control of S phase and mitosis in fission yeast'. In this model, S phase and mitosis are ordered by their dependence on increasing levels of cyclin-dependent kinase (Cdk) activity. Alternative mechanisms for ordering have been proposed that rely on checkpoint controls or on sequential waves of cyclins with distinct substrate specificities. Here, we review these ideas in the light of experimental evidence that has meanwhile accumulated. Quantitative Cdk control emerges as the basis for cell cycle ordering, fine-tuned by cyclin specificity and checkpoints. We propose a molecular explanation for quantitative Cdk control, based on thresholds imposed by Cdk-counteracting phosphatases, and discuss its implications.","doi":"10.1098/rstb.2011.0082","authors":"Uhlmann F, Bouchoux C, López-Avilés S","authors_abbrev":"Uhlmann F et al.","pubmed_publication_date":"27 Dec 2011","pubmed_entrez_date":"2011-11-16","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-11-23 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25691663","title":"Fission yeast Cdk7 controls gene expression through both its CAK and C-terminal domain kinase activities.","citation":"Mol Cell Biol 2015 May;35(9):1480-90","abstract":"Cyclin-dependent kinase (Cdk) activation and RNA polymerase II transcription are linked by the Cdk7 kinase, which phosphorylates Cdks as a trimeric Cdk-activating kinase (CAK) complex, and serine 5 within the polymerase II (Pol II) C-terminal domain (CTD) as transcription factor TFIIH-bound CAK. However, the physiological importance of integrating these processes is not understood. Besides the Cdk7 ortholog Mcs6, fission yeast possesses a second CAK, Csk1. The two enzymes have been proposed to act redundantly to activate Cdc2. Using an improved analogue-sensitive Mcs6-as kinase, we show that Csk1 is not a relevant CAK for Cdc2. Further analyses revealed that Csk1 lacks a 20-amino-acid sequence required for its budding yeast counterpart, Cak1, to bind Cdc2. Transcriptome profiling of the Mcs6-as mutant in the presence or absence of the budding yeast Cak1 kinase, in order to uncouple the CTD kinase and CAK activities of Mcs6, revealed an unanticipated role of the CAK branch in the transcriptional control of the cluster of genes implicated in ribosome biogenesis and cell growth. The analysis of a Cdc2 CAK site mutant confirmed these data. Our data show that the Cdk7 kinase modulates transcription through its well-described RNA Pol II CTD kinase activity and also through the Cdc2-activating kinase activity.","doi":"10.1128/MCB.00024-15","authors":"Devos M, Mommaerts E, Migeot V, van Bakel H, Hermand D","authors_abbrev":"Devos M et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-02-19","publication_year":"2015","canto_session_key":"3f9467bb487b3966","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-02-20 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19F8.07","SPBC11B10.09","SPBC28F2.12","SPBC32H8.10"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:17556368","title":"The Birt-Hogg-Dube and tuberous sclerosis complex homologs have opposing roles in amino acid homeostasis in Schizosaccharomyces pombe.","citation":"J Biol Chem 2007 Aug 24;282(34):24583-90","abstract":"Birt-Hogg-Dube (BHD) is a tumor suppressor gene disorder characterized by skin hamartomas, cystic lung disease, and renal cell carcinoma. The fact that hamartomas, lung cysts, and renal cell carcinoma can also occur in tuberous sclerosis complex (TSC) suggests that the BHD and TSC proteins may function within a common pathway. To evaluate this hypothesis, we deleted the BHD homolog in Schizosaccharomyces pombe. Expression profiling revealed that six permease and transporter genes, known to be down-regulated in Deltatsc1 and Deltatsc2, were up-regulated in Deltabhd, and levels of specific intracellular amino acids known to be low in Deltatsc1 and Deltatsc2 were elevated in Deltabhd. This \"opposite\" profile was unexpected, given the overlapping clinical phenotypes. The TSC1/2 proteins inhibit Rheb in mammals, and Tsc1/Tsc2 inhibit Rhb1 in S. pombe. Expression of a hypomorphic allele of rhb1(+) dramatically increased permease expression levels in Deltabhd but not in wild-type yeast. Loss of Bhd sensitized yeast to rapamycin-induced increases in permease expression levels, and rapamycin induced lethality in Deltabhd yeast expressing the hypomorphic Rhb1 allele. In S. pombe, it is known that Rhb1 binds Tor2, and Tor2 inhibition leads to up-regulation of permeases including those that are regulated by Bhd. Our data, therefore, suggest that Bhd activates Tor2. If the mammalian BHD protein, folliculin, similarly activates mammalian target of rapamycin, it will be of great interest to determine how mammalian target of rapamycin inhibition in BHD patients and mammalian target of rapamycin activation in TSC patients lead to overlapping clinical phenotypes.","authors":"van Slegtenhorst M, Khabibullin D, Hartman TR, Nicolas E, Kruger WD, Henske EP","authors_abbrev":"van Slegtenhorst M et al.","pubmed_publication_date":"24 Aug 2007","pubmed_entrez_date":"2007-06-09","publication_year":"2007","canto_session_key":"51ab1cf2ef51756d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-11-07 22:41:50","canto_approved_date":"2019-05-02 22:32:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-03 11:41:35","canto_added_date":"2012-02-17 18:26:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":42,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP7G5.06","SPAC869.10c","SPAC11D3.18c","SPAC1039.10","SPAC630.13c","SPBC13A2.04c","SPBC354.12","SPAC5H10.01","SPBC24C6.08c","SPAC1039.09","SPAC11D3.14c","SPBC428.16c","SPAC22F3.13","SPBC29B5.02c","SPBC216.07c"],"gene_count":15,"ltp_gene_count":4,"approved_date":"2016-11-07"},{"uniquename":"PMID:34830325","title":"Evolution of the Early Spliceosomal Complex-From Constitutive to Regulated Splicing.","citation":"Int J Mol Sci 2021 Nov 18;22(22)","abstract":"Pre-mRNA splicing is a major process in the regulated expression of genes in eukaryotes, and alternative splicing is used to generate different proteins from the same coding gene. Splicing is a catalytic process that removes introns and ligates exons to create the RNA sequence that codifies the final protein. While this is achieved in an autocatalytic process in ancestral group II introns in prokaryotes, the spliceosome has evolved during eukaryogenesis to assist in this process and to finally provide the opportunity for intron-specific splicing. In the early stage of splicing, the RNA 5' and 3' splice sites must be brought within proximity to correctly assemble the active spliceosome and perform the excision and ligation reactions. The assembly of this first complex, termed E-complex, is currently the least understood process. We focused in this review on the formation of the E-complex and compared its composition and function in three different organisms. We highlight the common ancestral mechanisms in  S. cerevisiae ,  S. pombe , and mammals and conclude with a unifying model for intron definition in constitutive and regulated co-transcriptional splicing.","doi":"10.3390/ijms222212444","authors":"Borao S, Ayté J, Hümmer S","authors_abbrev":"Borao S et al.","pubmed_publication_date":"18 Nov 2021","pubmed_entrez_date":"2021-11-27","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-11-29 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC146.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28106789","title":"Centromere Stability: The Replication Connection.","citation":"Genes (Basel) 2017 Jan 18;8(1)","abstract":"The fission yeast centromere, which is similar to metazoan centromeres, contains highly repetitive pericentromere sequences that are assembled into heterochromatin. This is required for the recruitment of cohesin and proper chromosome segregation. Surprisingly, the pericentromere replicates early in the S phase. Loss of heterochromatin causes this domain to become very sensitive to replication fork defects, leading to gross chromosome rearrangements. This review examines the interplay between components of DNA replication, heterochromatin assembly, and cohesin dynamics that ensures maintenance of genome stability and proper chromosome segregation.","doi":"10.3390/genes8010037","authors":"Forsburg SL, Shen KF","authors_abbrev":"Forsburg SL et al.","pubmed_publication_date":"18 Jan 2017","pubmed_entrez_date":"2017-01-21","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-01-22 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12963824","title":"Polo kinase--meiotic cell cycle coordinator.","citation":"Cell Cycle 2003;2(5):400-2","abstract":"","authors":"Lee BH, Amon A","authors_abbrev":"Lee BH et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-09-10","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU014126","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34100714","title":"Variations of intracellular density during the cell cycle arise from tip-growth regulation in fission yeast.","citation":"Elife 2021 Jun 08;10","abstract":"Intracellular density impacts the physical nature of the cytoplasm and can globally affect cellular processes, yet density regulation remains poorly understood. Here, using a new quantitative phase imaging method, we determined that dry-mass density in fission yeast is maintained in a narrow distribution and exhibits homeostatic behavior. However, density varied during the cell cycle, decreasing during G2, increasing in mitosis and cytokinesis, and dropping rapidly at cell birth. These density variations were explained by a constant rate of biomass synthesis, coupled to slowdown of volume growth during cell division and rapid expansion post-cytokinesis. Arrest at specific cell-cycle stages exacerbated density changes. Spatially heterogeneous patterns of density suggested links between density regulation, tip growth, and intracellular osmotic pressure. Our results demonstrate that systematic density variations during the cell cycle are predominantly due to modulation of volume expansion, and reveal functional consequences of density gradients and cell-cycle arrests.","doi":"10.7554/eLife.64901","authors":"Odermatt PD, Miettinen TP, Lemière J, Kang JH, Bostan E, Manalis SR, Huang KC, Chang F","authors_abbrev":"Odermatt PD et al.","pubmed_publication_date":"08 Jun 2021","pubmed_entrez_date":"2021-06-08","publication_year":"2021","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2021-06-10 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12718868","title":"Tome-1, wee1, and the onset of mitosis: coupled destruction for timely entry.","citation":"Mol Cell 2003 Apr;11(4):845-6","abstract":"In a recent issue of Cell, Ayad et al. (2003) report the identification of a novel F box protein Tome-1, which mediates the destruction of mitosis-inhibitory kinase wee1 via E3 ligase SCF. Tome-1 itself is targeted for degradation by APC in G1. This synergy of destructive action by APC and SCF has important implications for timely entry into mitosis.","authors":"Lim HH, Surana U","authors_abbrev":"Lim HH et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-04-30","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9490640","title":"A NIMA homologue promotes chromatin condensation in fission yeast.","citation":"J Cell Sci 1998 Apr;111 ( Pt 7):967-76","abstract":"Entry into mitosis requires p34(cdc2), which activates downstream mitotic events through phosphorylation of key target proteins. In Aspergillus nidulans, the NIMA protein kinase has been identified as a potential downstream target and plays a role in regulating chromatin condensation at mitosis. nimA- mutants arrest in a state that physically resembles interphase even though p34(cdc2) is fully active. Despite evidence for the existence of NIMA-like activities in a variety of cell types, the only bona fide NIMA homologue that has been identified is the nim-1 gene of Neurospora crassa. We report here the isolation of a fission yeast NIMA homologue, and have designated this gene fin1 and the 83 kDa predicted protein p83(fin1). Overexpression of fin1 promotes premature chromatin condensation from any point in the cell cycle independently of p34(cdc2) function. Like NIMA, p83(fin1) levels fluctuate through the cell cycle, peaking in mitosis and levels are greatly elevated by removal of C-terminal PEST sequences. Deletion of fin1 results in viable but elongated cells, indicative of a cell cycle delay. Genetic analysis has placed this delay in G2 but, unlike in nimA mutants of Aspergillus, p34(cdc2) activation appears to be delayed. Interaction of fin1 mutants with other strains defective in chromatin organisation also support the hypothesis of p83(fin1) playing a role in this process at the onset of mitosis. These data indicate that NIMA-related kinases may be a general feature of the cell cycle and chromatin organisation at mitosis.","authors":"Krien MJ, Bugg SJ, Palatsides M, Asouline G, Morimyo M, O'Connell MJ","authors_abbrev":"Krien MJ et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-05-20","publication_year":"1998","canto_session_key":"dff77e8a4cbbee1b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-04 09:03:14","canto_approved_date":"2022-02-02 14:50:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-29 08:18:53","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC336.12c","SPBC557.03c","SPBC11B10.09","SPBC1A4.03c","SPAC19E9.02"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-06-04"},{"uniquename":"PMID:15966770","title":"The cell cycle-regulated genes of Schizosaccharomyces pombe.","citation":"PLoS Biol 2005 Jul;3(7):e225","abstract":"Many genes are regulated as an innate part of the eukaryotic cell cycle, and a complex transcriptional network helps enable the cyclic behavior of dividing cells. This transcriptional network has been studied in Saccharomyces cerevisiae (budding yeast) and elsewhere. To provide more perspective on these regulatory mechanisms, we have used microarrays to measure gene expression through the cell cycle of Schizosaccharomyces pombe (fission yeast). The 750 genes with the most significant oscillations were identified and analyzed. There were two broad waves of cell cycle transcription, one in early/mid G2 phase, and the other near the G2/M transition. The early/mid G2 wave included many genes involved in ribosome biogenesis, possibly explaining the cell cycle oscillation in protein synthesis in S. pombe. The G2/M wave included at least three distinctly regulated clusters of genes: one large cluster including mitosis, mitotic exit, and cell separation functions, one small cluster dedicated to DNA replication, and another small cluster dedicated to cytokinesis and division. S. pombe cell cycle genes have relatively long, complex promoters containing groups of multiple DNA sequence motifs, often of two, three, or more different kinds. Many of the genes, transcription factors, and regulatory mechanisms are conserved between S. pombe and S. cerevisiae. Finally, we found preliminary evidence for a nearly genome-wide oscillation in gene expression: 2,000 or more genes undergo slight oscillations in expression as a function of the cell cycle, although whether this is adaptive, or incidental to other events in the cell, such as chromatin condensation, we do not know.","authors":"Oliva A, Rosebrock A, Ferrezuelo F, Pyne S, Chen H, Skiena S, Futcher B, Leatherwood J","authors_abbrev":"Oliva A et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-06-22","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27255861","title":"Genetic evidence for involvement of membrane trafficking in the action of 5-fluorouracil.","citation":"Fungal Genet Biol 2016 Aug;93:17-24","abstract":"To identify novel genes that mediate cellular sensitivity and resistance to 5-fluorouracil (5-FU), we performed a genome-wide genetic screening to identify altered susceptibility to 5-FU by Schizosaccharomyces pombe haploid nonessential gene deletion library containing 3004 deletion mutants. We identified 50 hypersensitive and 12 resistant mutants to this drug. Mutants sensitive or resistant to 5-FU were classified into various categories based on their putative functions. The largest group of the genes whose disruption renders cells altered susceptibility to 5-FU is involved in nucleic acid metabolism, but to our surprise, the second largest group is involved in membrane trafficking. In addition, several other membrane traffic mutants examined including gdi1-i11, ypt3-i5, Δryh1, Δric1, and Δaps1 exhibited hypersensitivity to 5-FU. Furthermore, we found that 5-FU in low concentration that generally do not affect cell growth altered the localization of Syb1, a secretory vesicle SNARE synaptobrevin which is cycled between the plasma membrane and the endocytic pathway. Notably, 5-FU at such low concentration also significantly inhibited the secretion of acid phosphatase. Altogether, our findings revealed the first evidence that 5-FU influences membrane trafficking as the potential underlying mechanism of the drug action.","doi":"10.1016/j.fgb.2016.05.007","authors":"Hu L, Yao F, Ma Y, Liu Q, Chen S, Hayafuji T, Kuno T, Fang Y","authors_abbrev":"Hu L et al.","pubmed_publication_date":"Aug 2016","pubmed_entrez_date":"2016-06-04","publication_year":"2016","canto_session_key":"b54c7e22c6dd02a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-08-09 08:54:29","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-08-08 14:44:27","canto_added_date":"2016-06-05 00:15:16","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":70,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_27255861_phaf.tsv"}],"genes":["SPAC16.04","SPBC609.03","SPAC14C4.16","SPBC16C6.05","SPAC9G1.07","SPBC2G2.15c","SPBP16F5.07","SPBC9B6.07","SPAC4C5.02c","SPAC3F10.16c","SPAC16A10.05c","SPACUNK4.12c","SPCP1E11.06","SPBC2D10.16","SPCC777.13","SPAPJ696.01c","SPAC1B3.01c","SPAC12G12.13c","SPAC9G1.03c","SPCC24B10.08c","SPCC1223.11","SPAC6G9.15c","SPAC1071.02","SPBC30B4.06c","SPBC215.03c","SPBC354.09c","SPBC776.04","SPCC162.11c","SPAC644.14c","SPBC19C7.02","SPAC18G6.03","SPAC1851.04c","SPAPB17E12.04c","SPAC1006.03c","SPBC609.02","SPAC23C11.04c","SPBP8B7.22","SPAC57A10.14","SPAC227.15","SPBC1718.03","SPCC11E10.04","SPAC19G12.02c","SPBC32F12.08c","SPBC19G7.04","SPAC18G6.13","SPCC1223.15c","SPCPJ732.01","SPAC4G9.13c","SPAC1F5.05c","SPAC222.05c","SPBC1861.05","SPAC30D11.07","SPBC800.04c","SPAC1B3.04c","SPAC15E1.06","SPBC36B7.08c","SPCC31H12.05c","SPCP1E11.05c","SPCC126.03","SPBC4F6.08c","SPAC13G6.14","SPAP27G11.16","SPAC22H10.12c","SPBC947.02","SPAC328.04","SPBC2G5.03","SPAC20H4.07"],"gene_count":67,"ltp_gene_count":0,"approved_date":"2016-08-08"},{"uniquename":"PMID:12560082","title":"Ubiquitin binding proteins protect ubiquitin conjugates from disassembly.","citation":"FEBS Lett 2003 Jan 30;535(1-3):77-81","abstract":"As a step in their turnover proteins in eukaryotic cells are coupled to a small protein, ubiquitin, before they are recognised by 26S proteasomes and degraded. However, cells also contain many deubiquitinating enzymes, which can rescue proteins by cleaving off the ubiquitin chains. Here we report that three ubiquitin binding proteins, Rhp23, Dph1 and Pus1, from fission yeast can protect multiubiquitin conjugates against deubiquitination. This protection depends on the ubiquitin binding domains and may promote degradation of ubiquitinated proteins.","authors":"Hartmann-Petersen R, Hendil KB, Gordon C","authors_abbrev":"Hartmann-Petersen R et al.","pubmed_publication_date":"30 Jan 2003","pubmed_entrez_date":"2003-02-01","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D89163","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19029820","title":"The fission yeast meiotic checkpoint kinase Mek1 regulates nuclear localization of Cdc25 by phosphorylation.","citation":"Cell Cycle 2008 Dec;7(23):3720-30","abstract":"In eukaryotic cells, fidelity in transmission of genetic information during cell division is ensured by the action of cell cycle checkpoints. Checkpoints are surveillance mechanisms that arrest or delay cell cycle progression when critical cellular processes are defective or when the genome is damaged. During meiosis, the so-called meiotic recombination checkpoint blocks entry into meiosis I until recombination has been completed, thus avoiding aberrant chromosome segregation and the formation of aneuploid gametes. One of the key components of the meiotic recombination checkpoint is the meiosis-specific Mek1 kinase, which belongs to the family of Rad53/Cds1/Chk2 checkpoint kinases containing forkhead-associated domains. In fission yeast, several lines of evidence suggest that Mek1 targets the critical cell cycle regulator Cdc25 to delay meiotic cell cycle progression. Here, we investigate in more detail the molecular mechanism of action of the fission yeast Mek1 protein. We demonstrate that Mek1 acts independently of Cds1 to phosphorylate Cdc25, and this phosphorylation is required to trigger cell cycle arrest. Using ectopic overexpression of mek1(+) as a tool to induce in vivo activation of Mek1, we find that Mek1 promotes cytoplasmic accumulation of Cdc25 and results in prolonged phosphorylation of Cdc2 at tyrosine 15. We propose that at least one of the mechanisms contributing to the cell cycle delay when the meiotic recombination checkpoint is activated in fission yeast is the nuclear exclusion of the Cdc25 phosphatase by Mek1-dependent phosphorylation.","authors":"Pérez-Hidalgo L, Moreno S, San-Segundo PA","authors_abbrev":"Pérez-Hidalgo L et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-11-26","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35765188","title":"Sporulation: A response to starvation in the fission yeast Schizosaccharomyces pombe.","citation":"Microbiologyopen 2022 Jun;11(3):e1303","abstract":"The fission yeast Schizosaccharomyces pombe employs two main strategies to adapt to the environment and survive when starved for nutrients. The strategies employ sporulation via sexual differentiation and extension of the chronological lifespan. When a cell is exposed to nutrient starvation in the presence of a cell of the opposite sex, the cells undergo fusion through conjugation and sporulation through meiosis. S. pombe spores are highly resistant to diverse stresses and may survive for a very long time. In this minireview, among the various sexual differentiation processes induced by starvation, we focused on and summarized the findings of the molecular mechanisms of spore formation in fission yeast. Furthermore, comparative measurements of the chronological lifespan of stationary phase cells and G 0  cells and the survival period of spore cells revealed that the spore cells survived for a long period, indicating the presence of an effective mechanism for survival. Currently, many molecules involved in sporulation and their functions are being discovered; however, our understanding of these is not complete. Further understanding of spores may not only deepen our comprehension of sexual differentiation but may also provide hints for sustaining life.","doi":"10.1002/mbo3.1303","authors":"Ohtsuka H, Imada K, Shimasaki T, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Jun 2022","pubmed_entrez_date":"2022-06-29","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-07-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37507029","title":"Binding of human Cdc123 to eIF2γ.","citation":"J Struct Biol 2023 Sep;215(3):108006","abstract":"Eukaryotic initiation factor 2 (eIF2) plays a key role in protein synthesis and in its regulation. The assembly of this heterotrimeric factor is facilitated by Cdc123, a member of the ATP grasp family that binds the γ subunit of eIF2. Notably, some mutations related to MEHMO syndrome, an X-linked intellectual disability, affect Cdc123-mediated eIF2 assembly. The mechanism of action of Cdc123 is unclear and structural information for the human protein is awaited. Here, the crystallographic structure of human Cdc123 (Hs-Cdc123) bound to domain 3 of human eIF2γ (Hs-eIF2γD3) was determined. The structure shows that the domain 3 of eIF2γ is bound to domain 1 of Cdc123. In addition, the long C-terminal region of Hs-Cdc123 provides a link between the ATP and Hs-eIF2γD3 binding sites. A thermal shift assay shows that ATP is tightly bound to Cdc123 whereas the affinity of ADP is much smaller. Yeast cell viability experiments, western blot analysis and two-hybrid assays show that ATP is important for the function of Hs-Cdc123 in eIF2 assembly. These data and recent findings allow us to propose a refined model to explain the mechanism of action of Cdc123 in eIF2 assembly.","doi":"10.1016/j.jsb.2023.108006","authors":"Cardenal Peralta C, Vandroux P, Neumann-Arnold L, Panvert M, Fagart J, Seufert W, Mechulam Y, Schmitt E","authors_abbrev":"Cardenal Peralta C et al.","pubmed_publication_date":"Sep 2023","pubmed_entrez_date":"2023-07-28","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP27G11.03"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:39247787","title":"Characterization of a valproic acid-sensitive mutant allele of the Golgi GDP-mannose transmembrane transporter Vrg4 in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2024;2024","abstract":"Valproic acid (VPA) is a widely used drug for epilepsy. However, precise molecular mechanisms relevant to VPA's side effects remain elusive. This study identifies a VPA-sensitive mutant strain (  vas21  ) in fission yeast with a missense mutation (T256I) in the nucleotide sugar-binding motif of the GDP-mannose transporter Vrg4 . This mutation impairs protein glycosylation, as evidenced by altered acid phosphatase mobility. We also found that Vrg4 overexpression deteriorates cell growth. Our results highlight the role of Vrg4 in glycosylation and implicate impaired glycosylation as a potential mechanism underlying VPA sensitivity. The new allele of  vrg4  will be useful in glycobiology and pharmacology.","doi":"10.17912/micropub.biology.001287","authors":"Takasaki T, Yamada M, Ikeda H, Fang Y, Sugiura R","authors_abbrev":"Takasaki T et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-09-09","publication_year":"2024","canto_session_key":"71fdf475a21ae784","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-09-09 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38272226","title":"E3 ubiquitin ligase Hul6 modulates iron-dependent metabolism by regulating Php4 stability.","citation":"J Biol Chem 2024 Jan 23;:105670","abstract":"Schizosaccharomyces pombe Php4 is the regulatory subunit of the CCAAT-binding complexes and plays an important role in the regulation of iron homeostasis and iron-dependent metabolism. Here we show that Php4 undergoes ubiquitin-dependent degradation in the late logarithmic and stationary phases. The degradation and ubiquitination of Php4 could be attenuated by deletion of hul6, a gene encoding a putative HECT-type E3 ubiquitin ligase. The expression levels of Hul6 and Php4 are oppositely regulated during cell growth. Hul6 interacts with the C-terminal region of Php4. Two lysine residues (K217 and K274) located in the C-terminal region of Php4 are required for its polyubiquitination. Increasing the levels of Php4 by deletion of hul6 or overexpression of php4 decreased expression of Php4 target proteins involved in iron-dependent metabolic pathways such as the tricarboxylic cycle (TCA cycle) and mitochondrial oxidative phosphorylation (OXPHOS), thus causing increased sensitivity to high-iron and reductions in succinate dehydrogenase (SDH) and mitochondrial complex II activities. Hul6 is located primarily in the mitochondrial outer membrane and most likely targets cytosolic Php4 for ubiquitination and degradation. Taken together, our data suggest that Hul6 regulates iron-dependent metabolism through degradation of Php4 under normal growth conditions. Our results also suggest that Hul6 promotes iron-dependent metabolism to help the cell to adapt to a nutrient-starved growth phase.","doi":"10.1016/j.jbc.2024.105670","authors":"Yao R, Li R, Wu X, Jin T, Luo Y, Li R, Huang Y","authors_abbrev":"Yao R et al.","pubmed_publication_date":"23 Jan 2024","pubmed_entrez_date":"2024-01-25","publication_year":"2024","canto_session_key":"48a191da3163b589","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying  Luo","canto_first_approved_date":"2024-12-12 09:46:14","canto_approved_date":"2025-12-20 13:18:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-06 23:53:05","canto_added_date":"2024-01-27 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":47,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying  Luo","community_curator":true,"annotation_count":38,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.10c","SPBC106.19","SPCC1235.02","SPAC1296.02","SPBC16E9.01c","SPBP23A10.16","SPCC737.02c","SPBC1683.10c","SPAC12B10.01c","SPBC4.07c"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2024-12-12"},{"uniquename":"PMID:40502003","title":"Impacts of stress and aging on spore health in  Schizosaccharomyces pombe .","citation":"bioRxiv 2025 May 30;","abstract":"","doi":"10.1101/2025.05.29.656811","authors":"Nuckolls NL, Eickbush MT, Lange JJ, Wood CJ, Nowotarski SH, Zanders SE","authors_abbrev":"Nuckolls NL et al.","pubmed_publication_date":"30 May 2025","pubmed_entrez_date":"2025-06-12","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-06-12 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8586271","title":"Cloning and sequencing of a gene encoding pyruvate kinase from Schizosaccharomyces pombe; implications for quaternary structure and regulation of the enzyme.","citation":"FEMS Microbiol Lett 1995 Dec 15;134(2-3):221-6","abstract":"A cDNA encoding pyruvate kinase from Schizosaccharomyces pombe has been isolated from a lambda ZAPII library. This cDNA was sequenced and found to contain an open reading frame of 1524 nucleotides, giving a predicted protein subunit M, of 55470. The sequence shows a high degree of identity with other pyruvate kinase sequences, with residues implicated in the binding of substrate and metal ion co-factors conserved. However, there are significant differences in the putative subunit interface and effector binding regions which may account for the unusual quaternary structure and regulatory properties of the S. pombe enzyme.","authors":"Nairn J, Smith S, Allison PJ, Rigden D, Fothergill-Gilmore LA, Price NC","authors_abbrev":"Nairn J et al.","pubmed_publication_date":"15 Dec 1995","pubmed_entrez_date":"1995-12-15","publication_year":"1995","canto_session_key":"266fff5de0065a16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 14:33:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 14:33:23","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4H3.10c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-07-31"},{"uniquename":"PMID:30257894","title":" mmi1  and  rep2  mRNAs are novel RNA targets of the Mei2 RNA-binding protein during early meiosis in  Schizosaccharomyces pombe .","citation":"Open Biol 2018 Sep 26;8(9)","abstract":"The RNA-binding protein Mei2 is crucial for meiosis in  Schizosaccharomyces pombe.  In  mei2  mutants, pre-meiotic S-phase is blocked, along with meiosis. Mei2 binds a long non-coding RNA (lncRNA) called meiRNA, which is a 'sponge RNA' for the meiotic inhibitor protein Mmi1. The interaction between Mei2, meiRNA and Mmi1 protein is essential for meiosis. But  mei2  mutants have stronger and different phenotypes than meiRNA mutants, since  mei2Δ  arrests before pre-meiotic S, while the meiRNA mutant arrests after pre-meiotic S but before meiosis. This suggests Mei2 may bind additional RNAs. To identify novel RNA targets of Mei2, which might explain how Mei2 regulates pre-meiotic S, we used RNA immunoprecipitation and cross-linking immunoprecipitation. In addition to meiRNA, we found the mRNAs for  mmi1  (which encodes Mmi1) and for the S-phase transcription factor  rep2  There were also three other RNAs of uncertain relevance. We suggest that at meiotic initiation, Mei2 may sequester  rep2  mRNA to help allow pre-meiotic S, and then may bind both meiRNA and  mmi1  mRNA to inactivate Mmi1 at two levels, the protein level (as previously known), and also the mRNA level, allowing meiosis. We call Mei2-meiRNA a 'double sponge' (i.e. binding both an mRNA and its encoded protein).","doi":"10.1098/rsob.180110","authors":"Mukherjee K, Futcher B, Leatherwood J","authors_abbrev":"Mukherjee K et al.","pubmed_publication_date":"26 Sep 2018","pubmed_entrez_date":"2018-09-28","publication_year":"2018","canto_session_key":"ecab76d5fbef2334","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-09-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.12c","SPAC27D7.03c","SPBC2F12.11c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:29985129","title":"Engineering ER-stress dependent non-conventional mRNA splicing.","citation":"Elife 2018 Jul 09;7","abstract":"The endoplasmic reticulum (ER) protein folding capacity is balanced with the protein folding burden to prevent accumulation of un- or misfolded proteins. The ER membrane-resident kinase/RNase Ire1 maintains ER protein homeostasis through two fundamentally distinct processes. First, Ire1 can initiate a transcriptional response through a non-conventional mRNA splicing reaction to increase the ER folding capacity. Second, Ire1 can decrease the ER folding burden through selective mRNA decay. In  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe,  the two Ire1 functions have been evolutionarily separated. Here, we show that the respective Ire1 orthologs have become specialized for their functional outputs by divergence of their RNase specificities. In addition, RNA structural features separate the splicing substrates from the decay substrates. Using these insights, we engineered an  S. pombe  Ire1 cleavage substrate into a splicing substrate, which confers  S. pombe  with both Ire1 functional outputs.","doi":"10.7554/eLife.35388","authors":"Li W, Okreglak V, Peschek J, Kimmig P, Zubradt M, Weissman JS, Walter P","authors_abbrev":"Li W et al.","pubmed_publication_date":"09 Jul 2018","pubmed_entrez_date":"2018-07-10","publication_year":"2018","canto_session_key":"9c2c0911ee4799b5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-07-11 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4602005","title":"[Malate dehydrogenase in Schizosaccharomyces pombe].","citation":"Pathol Microbiol (Basel) 1974;40(3):145-6","abstract":"","authors":"Flury U, Fiechter A","authors_abbrev":"Flury U et al.","pubmed_publication_date":"1974","pubmed_entrez_date":"1974-01-01","publication_year":"1974","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10852821","title":"Fission yeast Rng3p: an UCS-domain protein that mediates myosin II assembly during cytokinesis.","citation":"J Cell Sci 2000 Jul;113 ( Pt 13):2421-32","abstract":"Cell division in many eukaryotes, including the fission yeast Schizosaccharomyces pombe, utilizes a contractile actomyosin ring. In S. pombe, the actomyosin ring is assembled at the medial cortex upon entry into mitosis and constricts at the end of anaphase to guide the centripetal deposition of the septum. Despite identification of several structural components essential for actomyosin ring assembly, the interdependencies between these gene-products in the process of ring assembly are unknown. This study investigates the role of Rng3p, a member of the UCS-domain containing protein family (Unc-45p, Cro1p, She4p), in actomyosin ring assembly. Null mutants in rng3 resemble deletion mutants in the type II myosin heavy chain (myo2) and rng3(ts) mutants show strong negative interactions with the myo2-E1 mutant, suggesting that Rng3p is involved in modulating aspects of type II myosin function. Interestingly, a green fluorescent protein (GFP) tagged Rng3p fusion is detected at the division site in the myo2-E1 mutant, but not in other myo2-alleles, wild-type cells or in 18 other cytokinesis mutants. Assembly and maintenance of Rng3p at the division site in the myo2-E1 mutant requires F-actin. Rng3p is also required for the proper assembly of Myo2p and F-actin into a functional actomyosin ring but is not necessary for their accumulation at the division site. We conclude that Rng3p is a novel component of the F-actin cytoskeleton essential for a late step in actomyosin ring assembly and that it might monitor some aspect of type II myosin assembly during actomyosin ring construction.","authors":"Wong KC, Naqvi NI, Iino Y, Yamamoto M, Balasubramanian MK","authors_abbrev":"Wong KC et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-06-15","publication_year":"2000","canto_session_key":"2677a08d5a4fb5c7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-31 11:36:36","canto_approved_date":"2023-11-11 16:01:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-30 17:42:33","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPCC613.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-10-31"},{"uniquename":"PMID:29101277","title":"Application of a  Schizosaccharomyces pombe  Edc1-fused Dcp1-Dcp2 decapping enzyme for transcription start site mapping.","citation":"RNA 2018 Feb;24(2):251-257","abstract":"Changes in the 5' leader of an mRNA can have profound effects on its translational efficiency with little effect on abundance. Sequencing-based methods to accurately map the 5' leader by identifying the first transcribed nucleotide rely on enzymatic removal of the 5' eukaryotic cap structure by tobacco acid pyrophosphatase (TAP). However, commercial TAP production has been problematic and has now been discontinued. RppH, a bacterial enzyme that can also cleave the 5' cap, and Cap-Clip, a plant-derived enzyme, have been marketed as TAP replacements. We have engineered a  Schizosaccharomyces pombe  Edc1-fused Dcp1-Dcp2 decapping enzyme that functions as a superior TAP replacement. It can be purified from  E. coli  overexpression in high yields using standard biochemical methods. This constitutively active enzyme is four orders of magnitude more catalytically efficient than RppH at 5' cap removal, compares favorably to Cap-Clip, and the 5' monophosphorylated RNA product is suitable for standard RNA cloning methods. This engineered enzyme is a better replacement for TAP treatment than the current marketed use of RppH and can be produced cost-effectively in a general laboratory setting, unlike Cap-Clip.","doi":"10.1261/rna.062737.117","authors":"Paquette DR, Mugridge JS, Weinberg DE, Gross JD","authors_abbrev":"Paquette DR et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2017-11-05","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-11-06 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19A8.12"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18195021","title":"A conserved SET domain methyltransferase, Set11, modifies ribosomal protein Rpl12 in fission yeast.","citation":"J Biol Chem 2008 Mar 14;283(11):7185-95","abstract":"SET domain-containing methyltransferases post-translationally modify a variety of cellular proteins, such as histones, cytochrome c, ribulose-bisphosphate carboxylase/oxygenase, and ribosomal proteins. In the fission yeast Schizosaccharomyces pombe, at least 13 SET domain-containing proteins have been identified in the genome, four of which are involved in transcriptional regulation through their modification of histone tails. However, the roles played by the other SET domain proteins in cellular processes and their physiological substrates remain unresolved. We show here that S. pombe Set11, a SET domain-containing protein encoded by SPCC1223.04c, specifically modifies Rpl12 (ribosomal protein L12). Recombinant Set11 prepared from Escherichia coli had catalytic activity and methylated a 17-kDa polypeptide in cellular extracts of set11 mutant cells. The methylated protein was isolated by two-dimensional gel electrophoresis or by reverse-phase chromatography and was identified as Rpl12 by mass spectrometry. In vitro methylation experiments using wild-type and mutant Rpl12 proteins verified that Set11 modified recombinant Rpl12 and suggested that its potential target site was lysine 3. The methylation site modified by Set11 was also confirmed by mass spectrometric analysis, which also revealed other unique methylation sites of Rpl12. Finally, we found that Set11 predominantly localized to the nucleolus and that the overproduction of Set11 caused a severe growth defect. These results suggest that Rpl12 methylation occurs during the ribosomal assembly processes and that control of the Set11 expression level is important for its cellular function.","doi":"10.1074/jbc.M709429200","authors":"Sadaie M, Shinmyozu K, Nakayama J","authors_abbrev":"Sadaie M et al.","pubmed_publication_date":"14 Mar 2008","pubmed_entrez_date":"2008-01-16","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC31H12.04c","SPCC16C4.13c","SPCC1223.04c"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:1291234","title":"Expression of the catalytic subunits of pol alpha and pol delta from fission yeast Schizosaccharomyces pombe.","citation":"Chromosoma 1992;102(1 Suppl):S128-32","abstract":"This paper reports on expression and posttranslational modifications of the catalytic subunits of pol alpha and pol delta from fission yeast Schizosaccharomyces pombe. Okadaic acid treatment of S. pombe spheroplasts in amounts known to inhibit phosphatases 1 and 2A resulted in decreased proteolysis of both pol alpha and pol delta. Computer analysis of pol alpha and pol delta sequences confirmed the presence of consensus motifs for protein phosphorylation. Indirect immunofluorescence microscopy of S. pombe cells showed nuclear location of both proteins in wild type cells. However, whereas cells transformed with a vector expressing pol alpha produced a clear increase of the nuclear signal, no increase was detectable in cells transformed with pol delta. This observation suggests the existence of a mechanism limiting the cell concentration of pol delta in the cell. Constitutive expression of S. pombe pol delta in E. coli was possible only with vectors containing truncated forms of its gene, indicating a toxic effect of pol delta on E. coli growth.","authors":"Pignède G, Moussy G, Bouvier D, Tillit J, de Recondo AM, Baldacci G","authors_abbrev":"Pignède G et al.","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_session_key":"38165802a1dc7bd5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"vw253@cam.ac.uk","canto_approved_date":"2013-08-13 09:58:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-12 14:51:41","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"vw253@cam.ac.uk","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.04","SPAC3H5.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-08-12"},{"uniquename":"PMID:17072891","title":"The Cid1 family of non-canonical poly(A) polymerases.","citation":"Yeast 2006 Oct 15;23(13):991-1000","abstract":"Polyadenylation is an essential processing step for most eukaryotic mRNAs. In the nucleus, poly(A) polymerase adds poly(A) tails to mRNA 3' ends, contributing to their export, stability and translatability. Recently, a novel class of non-canonical poly(A) polymerases was discovered in yeast, worms and vertebrates. Different members of the Cid1 family, named after its founding member in the fission yeast Schizosaccharomyces pombe, are localized in the nucleus and the cytoplasm and are thought to target specific RNAs for polyadenylation. Polyadenylation of a target RNA by a Cid1-like poly(A) polymerase can lead to its degradation or stabilization, depending on the enzyme involved. Cid1-like proteins have important roles in diverse biological processes, including RNA surveillance pathways, DNA integrity checkpoint responses and RNAi-dependent heterochromatin formation.","authors":"Stevenson AL, Norbury CJ","authors_abbrev":"Stevenson AL et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36574952","title":"Application of the fission yeast Schizosaccharomyces pombe in human nutrition.","citation":"FEMS Yeast Res 2023 Jan 04;23","abstract":"Fission yeast Schizosaccharomyces pombe (S. pombe) is renowned as a powerful genetic model for deciphering cellular and molecular biological phenomena, including cell division, chromosomal events, stress responses, and human carcinogenesis. Traditionally, Africans use S. pombe to ferment the beer called 'Pombe', which continues to be consumed in many parts of Africa. Although not as widely utilized as the baker's yeast Saccharomyces cerevisiae, S. pombe has secured several niches in the food industry for human nutrition because of its unique metabolism. This review will explore three specific facets of human nutrition where S. pombe has made a significant impact: namely, in wine fermentation, animal husbandry and neutraceutical supplementation coenzyme Q10 production. Discussions focus on the current gaps in these areas, and the potential research advances useful for addressing future challenges. Overall, gaining a better understanding of S. pombe metabolism will strengthen production in these areas and potentially spearhead novel future applications.","doi":"10.1093/femsyr/foac064","authors":"Chen ES","authors_abbrev":"Chen ES","pubmed_publication_date":"04 Jan 2023","pubmed_entrez_date":"2022-12-27","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-12-29 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22658721","title":"Atl1 regulates choice between global genome and transcription-coupled repair of O(6)-alkylguanines.","citation":"Mol Cell 2012 Jul 13;47(1):50-60","abstract":"Nucleotide excision repair (NER) has long been known to remove DNA lesions induced by chemical carcinogens, and the molecular mechanism has been partially elucidated. Here we demonstrate that in Schizosaccharomyces pombe a DNA recognition protein, alkyltransferase-like 1 (Atl1), can play a pivotal role in selecting a specific NER pathway, depending on the nature of the DNA modification. The relative ease of dissociation of Atl1 from DNA containing small O(6)-alkylguanines allows accurate completion of global genome repair (GGR), whereas strong Atl1 binding to bulky O(6)-alkylguanines blocks GGR, stalls the transcription machinery, and diverts the damage to transcription-coupled repair. Our findings redraw the initial stages of the NER process in those organisms that express an alkyltransferase-like gene and raise the question of whether or not O(6)-alkylguanine lesions that are poor substrates for the alkyltransferase proteins in higher eukaryotes might, by analogy, signal such lesions for repair by NER.","doi":"10.1016/j.molcel.2012.04.028","authors":"Latypov VF, Tubbs JL, Watson AJ, Marriott AS, McGown G, Thorncroft M, Wilkinson OJ, Senthong P, Butt A, Arvai AS, Millington CL, Povey AC, Williams DM, Santibanez-Koref MF, Tainer JA, Margison GP","authors_abbrev":"Latypov VF et al.","pubmed_publication_date":"13 Jul 2012","pubmed_entrez_date":"2012-06-05","publication_year":"2012","canto_session_key":"9869aba8a5a2370a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-01 15:58:46","canto_approved_date":"2023-03-01 16:04:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-01 15:58:40","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC649.03","SPAC1250.04c","SPCP25A2.02c","SPBC4F6.15c","SPAC1556.01c","SPBC2D10.12","SPCC330.02"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2023-03-01","pdb_entries":[{"pdb_id":"4enn","gene_chains":[{"gene_uniquename":"SPAC1250.04c","chain":"A/B","position":"1-108"}],"title":"Crystal structure of S. pombe Atl1 in complex with damaged DNA containing O6-carboxymethylguanine","entry_authors":"Tubbs JL,Arvai AS,Tainer JA","entry_authors_abbrev":"Tubbs JL et al.","reference_uniquename":"PMID:22658721","experimental_method":"X-ray","resolution":"2.8448"},{"pdb_id":"4enk","gene_chains":[{"gene_uniquename":"SPAC1250.04c","chain":"A","position":"1-108"}],"title":"Crystal structure of S. pombe Atl1 in complex with damaged DNA containing O6-propylguanine","entry_authors":"Tubbs JL,Arvai AS,Tainer JA","entry_authors_abbrev":"Tubbs JL et al.","reference_uniquename":"PMID:22658721","experimental_method":"X-ray","resolution":"3.0445"},{"pdb_id":"4enm","gene_chains":[{"gene_uniquename":"SPAC1250.04c","chain":"A","position":"1-108"}],"title":"Crystal structure of S. pombe Atl1 in complex with damaged DNA containing O6-benzylguanine","entry_authors":"Tubbs JL,Arvai AS,Tainer JA","entry_authors_abbrev":"Tubbs JL et al.","reference_uniquename":"PMID:22658721","experimental_method":"X-ray","resolution":"2.8402"},{"pdb_id":"4enj","gene_chains":[{"gene_uniquename":"SPAC1250.04c","chain":"A","position":"1-108"}],"title":"Crystal structure of S. pombe Atl1 in complex with damaged DNA containing O6-hydroxyethylguanine","entry_authors":"Tubbs JL,Arvai AS,Tainer JA","entry_authors_abbrev":"Tubbs JL et al.","reference_uniquename":"PMID:22658721","experimental_method":"X-ray","resolution":"3.0989"}]},{"uniquename":"PMID:18062187","title":"Alterations in mitochondrial morphology of Schizosaccharomyces pombe induced by cell-death promoting agents.","citation":"Folia Microbiol (Praha) 2007;52(4):381-90","abstract":"The effect of the yeast cell-death inducing agents, Bax and acetic acid, on mitochondrial structure of Schizosaccharomyces pombe was studied. Comparison of mitochondrial structures in cells grown on different substrates and visualized with different probes revealed variations in their morphology. Cells grown on respiratory C sources as well as in the presence of antimycin A exhibited punctuated mitochondria when visualized with mitochondrially targeted green fluorescent protein, while they still appeared as tubular structures when stained with DiOC6(3). Both expression of Bax and acetic acid treatment induced fragmentation and aggregation of mitochondrial network, which could be prevented by coexpression of Bcl-XL. Aberrant mitochondrial morphology generated by either Bax or acetic acid was not accompanied with the loss of mitochondrial genome (mtDNA), indicating that alterations of mitochondrial morphology following death stimuli follow different mechanisms than those involved in mitochondrial inheritance mutants.","authors":"Pevala V, Kolarov J, Polcic P","authors_abbrev":"Pevala V et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-12-08","publication_year":"2007","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10335407","title":"[Structural-functional characteristics of the Schizosaccharomyces pombe rpb8+ gene, coding the subunit of RNA polymerase I-III, specific only for eukaryotes].","citation":"Bioorg Khim 1998 Feb;24(2):119-25","abstract":"A full-length cDNA of the rpb8+ gene encoding a common subunit Rpb8 of nuclear RNA polymerases I-III only specific for Eucarya was isolated from an expression library of the fission yeast Schizosaccharomyces pombe. The primary structure of the corresponding fragment of the Sz. pombe genome was also established. The rpb8+ gene contains two short introns, 59 and 48 bp long. Only short segments of homology were found upon comparing the Rpb8 subunit homologs from various eukaryotic species, and substantial differences exist between the corresponding proteins of unicellular and multicellular organisms. Subunit Rpb8 of Sz. pombe proved to be the smallest one among the known related proteins: it lacks the 21-aa fragment corresponding to amino acids residues 68-88 of the central part of the homologous subunit ABC14.5 of Saccharomyces cerevisiae. Accordingly, subunit Rpb8 of the fission yeast was not capable of substituting in vivo subunit ABC14.5 in nuclear RNA polymerases of the baker's yeast.","authors":"Shpakovskiĭ GV, Proshkin SA, Kaiushin AL, Korosteleva MD, Lebedenko EN","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1999-05-21","publication_year":"1998","canto_session_key":"8b5c376c89944200","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-06-12 09:27:00","canto_approved_date":"2018-06-12 09:27:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 09:26:52","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14C8.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-12"},{"uniquename":"PMID:11238999","title":"The dhp1(+) gene, encoding a putative nuclear 5'-->3' exoribonuclease, is required for proper chromosome segregation in fission yeast.","citation":"Nucleic Acids Res 2001 Mar 15;29(6):1326-33","abstract":"The Schizosaccharomyces pombe dhp1(+) gene is an ortholog of the Saccharomyces cerevisiae RAT1 gene, which encodes a nuclear 5'-->3' exoribonuclease, and is essential for cell viability. To clarify the cellular functions of the nuclear 5'-->3' exoribonuclease, we isolated and characterized a temperature-sensitive mutant of dhp1 (dhp1-1 mutant). The dhp1-1 mutant showed nuclear accumulation of poly(A)(+) RNA at the restrictive temperature, as was already reported for the rat1 mutant. Interestingly, the dhp1-1 mutant exhibited aberrant chromosome segregation at the restrictive temperature. The dhp1-1 cells frequently contained condensed chromosomes, most of whose sister chromatids failed to separate during mitosis despite normal mitotic spindle elongation. Finally, chromosomes were displaced or unequally segregated. As similar mitotic defects were also observed in Dhp1p-depleted cells, we concluded that dhp1(+) is required for proper chromosome segregation as well as for poly(A)(+) RNA metabolism in fission yeast. Furthermore, we isolated a multicopy suppressor of the dhp1-1 mutant, referred to as din1(+). We found that the gene product of dhp1-1 was unstable at high temperatures, but that reduced levels of Dhp1-1p could be suppressed by overexpressing Din1p at the restrictive temperature. Thus, Din1p may physically interact with Dhp1p and stabilize Dhp1p and/or restore its activity.","authors":"Shobuike T, Tatebayashi K, Tani T, Sugano S, Ikeda H","authors_abbrev":"Shobuike T et al.","pubmed_publication_date":"15 Mar 2001","pubmed_entrez_date":"2001-03-10","publication_year":"2001","canto_session_key":"57d5e228edb68d77","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-07 15:57:32","canto_approved_date":"2021-11-23 13:03:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-11-23 13:01:42","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.12c","SPAC19D5.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-03-07"},{"uniquename":"PMID:15157892","title":"Cell wall analysis.","citation":"Methods 2004 Jul;33(3):245-51","abstract":"The cell wall is a rigid structure essential for survival of the fungal cell. Because of its absence in mammalian cells, the cell wall is an attractive target for antifungal agents. Thus, for different reasons, it is important to know how the cell wall is synthesized and how different molecules regulate that synthesis. The Schizosaccharomyces pombe cell wall is mainly formed by glucose polysaccharides and some galactomannoproteins. Here, we describe a fast and reliable method to analyze changes in S. pombe cell wall composition by using specific enzymatic degradation and chemical treatment of purified cell walls. This approach provides a powerful means to analyze changes in (1,3)beta-glucan and (1,3)alpha-glucan, two main polysaccharides present in fungal cell walls. Analysis of cell wall polymers will be useful to search for new antifungal drugs that may inhibit cell wall biosynthesis and/or alter cell wall structure.","authors":"Pérez P, Ribas JC","authors_abbrev":"Pérez P et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4154968","title":"The enzymes of ammonia assimilation in Schizosaccharomyces spp. and in Saccharomycodes ludwigii.","citation":"J Gen Microbiol 1974 Nov;85(1):169-72","abstract":"","authors":"Johnson B, Brown CM","authors_abbrev":"Johnson B et al.","pubmed_publication_date":"Nov 1974","pubmed_entrez_date":"1974-11-01","publication_year":"1974","canto_session_key":"c9eb9105f66cbab8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-07-04 17:39:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-04 17:39:18","canto_added_date":"2016-09-04 13:34:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-04"},{"uniquename":"PMID:28455357","title":"Fission yeast neddylation ligase Dcn1 facilitates cohesin cleavage and chromosome segregation at anaphase.","citation":"Biol Open 2017 Jun 15;6(6):844-849","abstract":"Post-translational protein modification such as phosphorylation and ubiquitination are critical during mitosis to ensure proper timing and progression of chromosome segregation. It has been recently recognized that another type of protein modification - neddylation - may also regulate mitosis and chromosome segregation. The conserved protein DCN1 (defective cullin neddylation 1) has been shown, when knocked-down by RNAi, to result in multinucleated cells and/or blockage of cell proliferation. However, how DCN1 functions in mitosis and chromosome segregation is not known. We report here the fission yeast  dcn1 +   and its role in mitosis and chromosome segregation. Dcn1-GFP localizes to the nucleus throughout the cell cycle.  dcn1- deletion ( dcn1Δ ) leads to chromosome and kinetochore lagging at anaphase, resulting from delayed and attenuated cohesin cleavage and sister chromatids separation. These results put Dcn1 upstream of the anaphase promoting complex/cyclosome (APC/C) pathway. We propose a mechanism for Dcn1 function at mitosis.","doi":"10.1242/bio.021238","authors":"Lin L, Chen L, Tran PT","authors_abbrev":"Lin L et al.","pubmed_publication_date":"15 Jun 2017","pubmed_entrez_date":"2017-04-30","publication_year":"2017","canto_session_key":"7aaeec987eb96837","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-25 16:38:32","canto_approved_date":"2017-10-25 16:38:32","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-10-25 16:38:24","canto_added_date":"2017-05-01 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPBC839.03c","SPCC338.17c","SPAC1687.20c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2017-10-25"},{"uniquename":"PMID:15120077","title":"The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes.","citation":"Curr Biol 2004 May 04;14(9):824-8","abstract":"Valosin-containing protein, VCP/p97 or Cdc48, is a eukaryotic ATPase involved in membrane fusion, protein transport, and protein degradation. We describe two proteins, Ubx2 and Ubx3, which interact with Cdc48 in fission yeast. Ubx3 is the ortholog of p47/Shp1, a previously described Cdc48 cofactor involved in membrane fusion, whereas Ubx2 is a novel protein. Cdc48 binds the UBX domains present in both Ubx2 and Ubx3, indicating that this domain is a general Cdc48-interacting module. Ubx2 and Ubx3 also interact with ubiquitin chains. Disruption of the ubx3(+)-gene causes both temperature and canavanine sensitivity and stabilizes some ubiquitin-protein conjugates including the CDK inhibitor Rum1, but not a model substrate of the ER-degradation pathway. Moreover the ubx3 null displays synthetic lethality with a pus1 null mutant, a multiubiquitin binding subunit of the 26S proteasome. In contrast, the ubx2 null mutant did not display any obvious protein-degradation phenotype. In conclusion Ubx3/p47 is not, as previously thought, only important for membrane fusion; it's also important for the specific degradation of a subset of cell proteins. Our genetic analyses revealed that Ubx3/p47 functionally parallels a substrate receptor of the 26S proteasome, Pus1/Rpn10, indicating that the Cdc48-Ubx3 complex is involved in delivering substrates to the 26S proteasome.","authors":"Hartmann-Petersen R, Wallace M, Hofmann K, Koch G, Johnsen AH, Hendil KB, Gordon C","authors_abbrev":"Hartmann-Petersen R et al.","pubmed_publication_date":"04 May 2004","pubmed_entrez_date":"2004-05-04","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC337.08c","SPAC343.09","SPAC2C4.15c","SPAC1565.08","SPAC637.10c"],"gene_count":5,"ltp_gene_count":4},{"uniquename":"PMID:","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1795.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15689489","title":"Ase1p organizes antiparallel microtubule arrays during interphase and mitosis in fission yeast.","citation":"Mol Biol Cell 2005 Apr;16(4):1756-68","abstract":"Proper microtubule organization is essential for cellular processes such as organelle positioning during interphase and spindle formation during mitosis. The fission yeast Schizosaccharomyces pombe presents a good model for understanding microtubule organization. We identify fission yeast ase1p, a member of the conserved ASE1/PRC1/MAP65 family of microtubule bundling proteins, which functions in organizing the spindle midzone during mitosis. Using fluorescence live cell imaging, we show that ase1p localizes to sites of microtubule overlaps associated with microtubule organizing centers at both interphase and mitosis. ase1Delta mutants fail to form overlapping antiparallel microtubule bundles, leading to interphase nuclear positioning defects, and premature mitotic spindle collapse. FRAP analysis revealed that interphase ase1p at overlapping microtubule minus ends is highly dynamic. In contrast, mitotic ase1p at microtubule plus ends at the spindle midzone is more stable. We propose that ase1p functions to organize microtubules into overlapping antiparallel bundles both in interphase and mitosis and that ase1p may be differentially regulated through the cell cycle.","authors":"Loïodice I, Staub J, Setty TG, Nguyen NP, Paoletti A, Tran PT","authors_abbrev":"Loïodice I et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-02-04","publication_year":"2005","canto_session_key":"02e7585390af07ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-07-14 08:05:40","canto_approved_date":"2022-07-14 08:05:40","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-06-28 14:58:44","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":15,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-07-14"},{"uniquename":"PMID:12052869","title":"Two ras pathways in fission yeast are differentially regulated by two ras guanine nucleotide exchange factors.","citation":"Mol Cell Biol 2002 Jul;22(13):4598-606","abstract":"How a given Ras prreotein coordinates multiple signaling inputs and outputs is a fundamental issue of signaling specificity. Schizosaccharomyces pombe contains one Ras, Ras1, that has two distinct outputs. Ras1 activates Scd1, a presumptive guanine nucleotide exchange factor (GEF) for Cdc42, to control morphogenesis and chromosome segregation, and Byr2, a component of a mitogen-activated protein kinase cascade, to control mating. So far there is only one established Ras1 GEF, Ste6. Paradoxically, ste6 null (ste6 Delta) mutants are sterile but normal in cell morphology. This suggests that Ste6 specifically activates the Ras1-Byr2 pathway and that there is another GEF capable of activating the Scd1 pathway. We thereby characterized a potential GEF, Efc25. Genetic data place Efc25 upstream of the Ras1-Scd1, but not the Ras1-Byr2, pathway. Like ras1 Delta and scd1 Delta, efc25 Delta is synthetically lethal with a deletion in tea1, a critical element for cell polarity control. Using truncated proteins, we showed that the C-terminal GEF domain of Efc25 is essential for function and regulated by the N terminus. We conclude that Efc25 acts as a Ras1 GEF specific for the Scd1 pathway. While ste6 expression is induced during mating, efc25 expression is constitutive. Moreover, Efc25 overexpression renders cells hyperelongated and sterile; the latter can be rescued by activated Ras1. This suggests that Efc25 can recruit Ras1 to selectively activate Scd1 at the expense of Byr2. Reciprocally, Ste6 overexpression can block Scd1 activation. We propose that external signals can partly segregate two Ras1 pathways by modulating GEF expression and that GEFs can influence how Ras is coupled to specific effectors.","authors":"Papadaki P, Pizon V, Onken B, Chang EC","authors_abbrev":"Papadaki P et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-06-08","publication_year":"2002","canto_session_key":"4194e25ff0b7c9a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-29 13:37:38","canto_approved_date":"2023-12-27 20:29:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-29 13:37:16","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1D7.05","SPCC1223.06","SPAC16E8.09","SPAC637.07","SPAC17H9.09c","SPCC1442.01","SPBC336.03"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-04-29"},{"uniquename":"PMID:3518949","title":"Schizosaccharomyces pombe and Saccharomyces cerevisiae: a look at yeasts divided.","citation":"Cell 1986 Jun 20;45(6):781-2","abstract":"","authors":"Russell P, Nurse P","authors_abbrev":"Russell P et al.","pubmed_publication_date":"20 Jun 1986","pubmed_entrez_date":"1986-06-20","publication_year":"1986","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR16027","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25B8.08","HGNC:22226","HGNC:24716"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8723351","title":"Large, complex modular structure of a fission yeast DNA replication origin.","citation":"Curr Biol 1996 Apr 01;6(4):467-73","abstract":"In the budding yeast, Saccharomyces cerevisiae, each DNA replication origin is associated with an autonomously replicating sequence (ARS) element. Each element contains several modules, including an essential close match to the 11 base-pair (bp) ARS consensus sequence (ACS) and two or three short (< 20 bp) stimulatory motifs, within a stretch of approximately 150 bp or less. To determine whether a similar origin structure exists in the evolutionarily distant fission yeast, Schizosaccharomyces pombe, we used deletion and linker substitution scanning to identify the sequences important for the function of ars3002, a chromosomal replication origin.\nWe detected two large (30-55 bp) essential regions and several additional stimulatory sequences within a 600 bp stretch of a restriction fragment containing ars3002. The two essential regions are similar to each other, and sequences similar to them are found in all known S. pombe ARS elements, suggesting that one or both of them may represent the S. pombe equivalent of the S. cerevisiae ACS.\nLike S. cerevisiae origins, the S. pombe origin, ars3002, possesses a modular structure, but the number and size of modules is greater for ars3002, and ars3002 is larger than S. cerevisiae origins. These observations suggest that origin function in S. pombe requires more protein-DNA interactions than in S. cerevisiae.","authors":"Dubey DD, Kim SM, Todorov IT, Huberman JA","authors_abbrev":"Dubey DD et al.","pubmed_publication_date":"01 Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9153313","title":"Isolation and characterization of the Schizosaccharomyces pombe rhp9 gene: a gene required for the DNA damage checkpoint but not the replication checkpoint.","citation":"Nucleic Acids Res 1997 Jun 01;25(11):2138-46","abstract":"Checkpoint controls exist in eukaryotic cells to ensure that cells do not enter mitosis in the presence of DNA damage or unreplicated chromosomes. In Schizosaccharomyces pombe many of the checkpoint genes analysed to date are required for both the DNA damage and the replication checkpoints, an exception being chk1 . We report here on the characterization of nine new methylmethane sulphonate (MMS)-sensitive S.pombe mutants, one of which is defective in the DNA damage checkpoint but not the replication checkpoint. We have cloned and sequenced the corresponding gene. The predicted protein is most similar to the Saccharomyces cerevisiae Rad9 protein, having 46% similarity and 26% identity. The S.pombe protein, which we have named Rhp9 (Rad9 homologue in S. pombe) on the basis of structural and phenotypic similarity, also contains motifs present in BRCA1 and 53BP1. Deletion of the gene is not lethal and results in a DNA damage checkpoint defect. Epistasis analysis with other S.pombe checkpoint mutants indicates that rhp9 acts in a process involving the checkpoint rad genes and that the rhp9 mutant is phenotypically very similar to chk1.","authors":"Willson J, Wilson S, Warr N, Watts FZ","authors_abbrev":"Willson J et al.","pubmed_publication_date":"01 Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"35ddc02d3b26fd99","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-08-28 13:47:32","canto_approved_date":"2026-03-11 16:06:05","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-08-28 14:08:49","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.01","SPBC336.12c","SPAC3G6.06c","SPAC20G4.04c","SPCC1259.13","SPCC5E4.04","SPAC9E9.08","SPBC216.05","SPBC342.05","SPAC1F7.05","SPBC3E7.08c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2019-08-28"},{"uniquename":"PMID:16990277","title":"Fission yeast homologs of human histone H3 lysine 4 demethylase regulate a common set of genes with diverse functions.","citation":"J Biol Chem 2006 Nov 24;281(47):35983-8","abstract":"Schizosaccharomyces pombe contains two proteins, SWIRM1 and SWIRM2, with close homology to human histone H3 lysine 4 demethylase. Both proteins contain the amino oxidase catalytic domain and a recently described DNA interaction SWIRM domain. Here we describe the biochemical isolation and the functional characterization of SWIRM1 and SWIRM2. Our results indicate that while SWIRM2 is an essential gene, cells lacking SWIRM1 are viable. We found that SWIRM1 and SWIRM2 are stably associated in a multiprotein complex, but intriguingly, unlike their human counterpart, S. pombe SWIRM complex contains neither a histone deacetylase nor any detectable demethylase activity. Genome-wide chromatin immunoprecipitation unexpectedly showed the absence of both SWIRM proteins from heterochromatic domains. Instead, consistent with biochemical analyses, SWIRM1 and SWIRM2 co-localize to a common set of target gene promoters whose functions are implicated in diverse processes including mitochondrial metabolism and transcriptional regulation. Importantly, we show that SWIRM1 is not only required for optimum transcription of its target genes but also display a global role in regulation of antisense transcription.","authors":"Nicolas E, Lee MG, Hakimi MA, Cam HP, Grewal SI, Shiekhattar R","authors_abbrev":"Nicolas E et al.","pubmed_publication_date":"24 Nov 2006","pubmed_entrez_date":"2006-09-23","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1783.05","SPAC23E2.02","SPAC30D11.08c","SPCC4G3.07c","SPBC23E6.01c","SPBC146.09c","SPAC926.04c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:17762865","title":"SUMO-targeted ubiquitin ligases in genome stability.","citation":"EMBO J 2007 Sep 19;26(18):4089-101","abstract":"We identify the SUMO-Targeted Ubiquitin Ligase (STUbL) family of proteins and propose that STUbLs selectively ubiquitinate sumoylated proteins and proteins that contain SUMO-like domains (SLDs). STUbL recruitment to sumoylated/SLD proteins is mediated by tandem SUMO interaction motifs (SIMs) within the STUbLs N-terminus. STUbL-mediated ubiquitination maintains sumoylation pathway homeostasis by promoting target protein desumoylation and/or degradation. Thus, STUbLs establish a novel mode of communication between the sumoylation and ubiquitination pathways. STUbLs are evolutionarily conserved and include: Schizosaccharomyces pombe Slx8-Rfp (founding member), Homo sapiens RNF4, Dictyostelium discoideum MIP1 and Saccharomyces cerevisiae Slx5-Slx8. Cells lacking Slx8-Rfp accumulate sumoylated proteins, display genomic instability, and are hypersensitive to genotoxic stress. These phenotypes are suppressed by deletion of the major SUMO ligase Pli1, demonstrating the specificity of STUbLs as regulators of sumoylated proteins. Notably, human RNF4 expression restores SUMO pathway homeostasis in fission yeast lacking Slx8-Rfp, underscoring the evolutionary functional conservation of STUbLs. The DNA repair factor Rad60 and its human homolog NIP45, which contain SLDs, are candidate STUbL targets. Consistently, Rad60 and Slx8-Rfp mutants have similar DNA repair defects.","authors":"Prudden J, Pebernard S, Raffa G, Slavin DA, Perry JJ, Tainer JA, McGowan CH, Boddy MN","authors_abbrev":"Prudden J et al.","pubmed_publication_date":"19 Sep 2007","pubmed_entrez_date":"2007-09-01","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPBC651.10","SPAC3C7.03c","SPAPB1E7.06c","SPBC1921.02","SPBC365.06","SPAC11E3.08c","SPAC19A8.10","SPCC1919.15","SPAC644.14c","SPBC3D6.11c","SPAC343.18","SPAC1687.05","SPCC970.10c"],"gene_count":14,"ltp_gene_count":14},{"uniquename":"PMID:20719273","title":"Microtubule-dependent spatial organization of mitochondria in fission yeast.","citation":"Methods Cell Biol 2010;97:203-21","abstract":"The microtubule cytoskeleton has an important role in the control of mitochondrial distribution in higher eukaryotes. In humans, defects in axonal mitochondrial transport are linked to neurodegenerative diseases. This chapter highlights fission yeast Schizosaccharomyces pombe as a powerful genetic model system for the study of microtubule-dependent mitochondrial movement, dynamics and inheritance.","doi":"10.1016/S0091-679X(10)97012-X","authors":"Das M, Chiron S, Verde F","authors_abbrev":"Das M et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-08-20","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29993099","title":"Biological Significance of Hetero-Scaffolds Based Gold(III) Complexes.","citation":"Acta Chim Slov 2018 Jun;65(2):333-343","abstract":"Synthesized ligands and complexes, [Au(Ln)Cl2]Cl, have been characterized by various techniques such as elemental analysis, LC-MS, FT-IR, UV-Vis, 1H and 13C NMR spectroscopy, conductance measurement and magnetic moments measurement. The experimental results show that complexes exhibit higher antibacterial activity against Gram(+ve) and Gram(-ve) microorganisms than free ligands. The in vitro cytotoxicity and cellular level cytotoxicity suggest that Au(III) complexes show better activity than corresponding ligands. The DNA interaction study has been evaluated using absorption titration. The experimental evidence indicates (Kb = 1.08-3.44 • 105 M-1) that all the complexes have been bind to HS-DNA by intercalation mode. To further verify the nature of interaction viscosity measurement and molecular modeling have been carried out which suggest the intercalation binding between complex and DNA. The Schizosaccharomyces pombe cell DNA cleavage has been performed using agarose gel and their photographic images of complexes show smearing of DNA due to DNA cleavage from the nucleus.","doi":"10.17344/acsi.2017.4018","authors":"Kanthecha DN, Raval DB, Thakkar VR, Patel MN","authors_abbrev":"Kanthecha DN et al.","pubmed_publication_date":"Jun 2018","pubmed_entrez_date":"2018-07-12","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-07-13 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32840792","title":"The Analysis of Recombination-Dependent Processing of Blocked Replication Forks by Bidimensional Gel Electrophoresis.","citation":"Methods Mol Biol 2021;2153:365-381","abstract":"The perturbation of the DNA replication process is a threat to genome stability and is an underlying cause of cancer development and numerous human diseases. It has become central to understanding how stressed replication forks are processed to avoid their conversion into fragile and pathological DNA structures. The engineering of replication fork barriers (RFBs) to conditionally induce the arrest of a single replisome at a defined locus has made a tremendous impact in our understanding of replication fork processing. Applying the bidimensional gel electrophoresis (2DGE) technique to those site-specific RFBs allows the visualization of replication intermediates formed in response to replication fork arrest to investigate the mechanisms ensuring replication fork integrity. Here, we describe the 2DGE technique applied to the site-specific RTS1-RFB in Schizosaccharomyces pombe and explain how this approach allows the detection of arrested forks undergoing nascent strands resection.","doi":"10.1007/978-1-0716-0644-5_25","authors":"Kramarz K, Saada AA, Lambert SAE","authors_abbrev":"Kramarz K et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2020-08-26","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-08-27 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20563653","title":"Protective roles and Pap1-dependent regulation of the Schizosaccharomyces pombe spy1 gene under nitrosative and nutritional stresses.","citation":"Mol Biol Rep 2011 Feb;38(2):1129-36","abstract":"This work aimed to assess novel protective roles and regulation of Spy1, a histidine-containing phosphotransfer (HPt) protein, in the fission yeast Schizosaccharomyces pombe. The structural gene encoding Spy1 was cloned into the shuttle vector pRS316 to generate the recombinant plasmid pYFSpy1. The spy1(+) mRNA level was notably increased in S. pombe cells harboring the plasmid pYFSpy1. The S. pombe cells harboring pYFSpy1 exhibited higher survival than the vector control cells on the minimal media plates with nitric oxide (NO)-generating sodium nitroprusside (SNP) or without nitrogen source. In the liquid minimal media, they also showed higher viability under nitrosative stress or nitrogen-starved condition. The intracellular reactive oxygen species (ROS) level appeared to be lower in the fission yeast cells harboring pYFSpy1 than in the control yeast cells. Overexpression of the spy1(+) gene showed scavenging effect on NO generated from SNP. Synthesis of β-galactosidase from the spy1(+)-lacZ fusion gene was significantly enhanced by SNP and nitrogen starvation in the Pap1-positive but not in the Pap1-negative cells. The spy1(+) mRNA level in S. pombe was also elevated by SNP and nitrogen starvation in the Pap1-positive but not in the Pap1-negative cells. In summary, Spy1 plays protective roles against nitrosative and nutritional stress in the fission yeast and is transcriptionally up-regulated by nitrosative and nutritional stresses in a Pap1-dependent manner.","doi":"10.1007/s11033-010-0210-3","authors":"Kang MH, Jung HJ, Hyun DH, Park EH, Lim CJ","authors_abbrev":"Kang MH et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2010-06-22","publication_year":"2011","canto_session_key":"c8b732420cf87ff9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-01 14:07:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-01 14:07:35","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPBC725.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-12-01"},{"uniquename":"PMID:15157894","title":"Assaying the DNA damage checkpoint in fission yeast.","citation":"Methods 2004 Jul;33(3):260-3","abstract":"Cell cycle checkpoints exist to ensure the proper maintenance and stable inheritance of genomic information. The pathways that insure the faithful execution of these checkpoints are well conserved throughout evolution. In the fission yeast, Schizosaccharomyces pombe, a major cell cycle checkpoint exists that responds to the presence of damaged DNA and prevents this damage from being propagated to future generations. Fission yeast is an ideal system to investigate these pathways because there exist specific techniques that allow one to assay the fidelity of this DNA damage checkpoint pathway.","authors":"Dunaway S, Walworth NC","authors_abbrev":"Dunaway S et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9852154","title":"Role of polo kinase and Mid1p in determining the site of cell division in fission yeast.","citation":"J Cell Biol 1998 Dec 14;143(6):1603-16","abstract":"The fission yeast Schizosaccharomyces pombe divides symmetrically using a medial F-actin- based contractile ring to produce equal-sized daughter cells. Mutants defective in two previously described genes, mid1 and pom1, frequently divide asymmetrically. Here we present the identification of three new temperature-sensitive mutants defective in localization of the division plane. All three mutants have mutations in the polo kinase gene, plo1, and show defects very similar to those of mid1 mutants in both the placement and organization of the medial ring. In both cases, ring formation is frequently initiated near the cell poles, indicating that Mid1p and Plo1p function in recruiting medial ring components to the cell center. It has been reported previously that during mitosis Mid1p becomes hyperphosphorylated and relocates from the nucleus to a medial ring. Here we show that Mid1p first forms a diffuse cortical band during spindle formation and then coalesces into a ring before anaphase. Plo1p is required for Mid1p to exit the nucleus and form a ring, and Pom1p is required for proper placement of the Mid1p ring. Upon overexpression of Plo1p, Mid1p exits the nucleus prematurely and displays a reduced mobility on gels similar to that of the hyperphosphorylated form observed previously in mitotic cells. Genetic and two-hybrid analyses suggest that Plo1p and Mid1p act in a common pathway distinct from that involving Pom1p. Plo1p localizes to the spindle pole bodies and spindles of mitotic cells and also to the medial ring at the time of its formation. Taken together, the data indicate that Plo1p plays a role in the positioning of division sites by regulating Mid1p. Given its previously known functions in mitosis and the timing of cytokinesis, Plo1p is thus implicated as a key molecule in the spatial and temporal coordination of cytokinesis with mitosis.","authors":"Bähler J, Steever AB, Wheatley S, Wang Yl, Pringle JR, Gould KL, McCollum D","authors_abbrev":"Bähler J et al.","pubmed_publication_date":"14 Dec 1998","pubmed_entrez_date":"1998-12-16","publication_year":"1998","canto_session_key":"67631dafe77debd1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 16:12:11","canto_approved_date":"2023-05-04 12:41:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-28 15:47:42","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":51,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPAC24H6.05","SPAC2F7.03c","SPCC4B3.15"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2019-01-30"},{"uniquename":"PMID:5436084","title":"Colcemid sensitivity of fission yeast and the isolation of colcemid-resistant mutants.","citation":"Science 1970 Apr 24;168(3930):485-7","abstract":"Cell division of the fission yeast, Schizosaccharomyces pombe, is reversibly inhibited by the antimitotic agent Colcemid (N-deacetyl-N-methylcolchicine) in nutrient medium. Cell growth continiues until all cells become nonseparating cell doublets in a V configuration. Mutants have been isolated capable of uninhibited growth in the presence of concentrations of Colcemid mycostatic for the parent strain.","authors":"Lederberg S, Stetten G","authors_abbrev":"Lederberg S et al.","pubmed_publication_date":"24 Apr 1970","pubmed_entrez_date":"1970-04-24","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17276920","title":"Filament formation of the Escherichia coli actin-related protein, MreB, in fission yeast.","citation":"Curr Biol 2007 Feb 06;17(3):266-72","abstract":"Proteins structurally related to eukaryotic actins have recently been identified in several prokaryotic organisms. These actin-like proteins (MreB and ParM) and the deviant Walker A ATPase (SopA) play a key role in DNA segregation and assemble into polymers in vitro and in vivo. MreB also plays a role in cellular morphogenesis. Whereas the dynamic properties of eukaryotic actins have been extensively characterized, those of bacterial actins are only beginning to emerge. We have established the fission yeast Schizosaccharomyces pombe as a cellular model for the functional analysis of the Escherichia coli actin-related protein MreB. We show that MreB organizes into linear bundles that grow in a symmetrically bidirectional manner at 0.46 +/- 0.03 microm/min, with new monomers and/or oligomers being added along the entire length of the bundle. Organization of linear arrays was dependent on the ATPase activity of MreB, and their alignment along the cellular long axis was achieved by sliding along the cortex of the cylindrical part of the cell. The cell ends appeared to provide a physical barrier for bundle elongation. These experiments provide new insights into the mechanism of assembly and organization of the bacterial actin cytoskeleton.","authors":"Srinivasan R, Mishra M, Murata-Hori M, Balasubramanian MK","authors_abbrev":"Srinivasan R et al.","pubmed_publication_date":"06 Feb 2007","pubmed_entrez_date":"2007-02-06","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22215813","title":"Schizosaccharomyces pombe Ccq1 and TER1 bind the 14-3-3-like domain of Est1, which promotes and stabilizes telomerase-telomere association.","citation":"Genes Dev 2012 Jan 01;26(1):82-91","abstract":"The telomerase protein Est1 exists in multiple organisms, including Schizosaccharomyces pombe, humans, and Saccharomyces cerevisiae, but its function has only been closely examined in S. cerevisiae, where it is a recruiter/activator of telomerase. Here, we demonstrate that S. pombe Est1 was required for the telomere association of the telomerase holoenzyme, suggesting that it too has a recruitment role. Its association with telomeres was dependent on Trt1, the catalytic subunit, and Ccq1, a telomeric protein. Surprisingly, Est1 telomere binding was only partially dependent on TER1, the telomerase RNA, even though Est1 bound nucleotides 415-507 of TER1. A ter1-Δ415-507 strain had short telomeres and very low Est1 and Trt1 telomere association in late S phase but did not senesce. An unbiased search for mutations that reduced Est1-TER1 interaction identified mutations only in the Est1 14-3-3-like domain, a phosphoserine-binding motif, the first example of a 14-3-3-like domain with RNA-binding activity. These mutations also reduced Est1-Ccq1 binding. One such mutant prevented Est1 telomere association and caused telomere loss and slow senescence, similar to ccq1Δ. We propose that the Est1-Ccq1 interaction is critical for telomerase recruitment, while the Est1-TER1 interaction acts downstream from Ccq1-mediated recruitment to stabilize the holoenzyme at the telomere.","doi":"10.1101/gad.181826.111","authors":"Webb CJ, Zakian VA","authors_abbrev":"Webb CJ et al.","pubmed_publication_date":"01 Jan 2012","pubmed_entrez_date":"2012-01-05","publication_year":"2012","canto_session_key":"3abc67253af5c842","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPNCRNA.214","SPBC2D10.13","SPCC188.07"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:9560394","title":"Isolation and characterization of fission yeast sns mutants defective at the mitosis-to-interphase transition.","citation":"Genetics 1998 Apr;148(4):1799-811","abstract":"pim1-d1ts was previously identified in a visual screen for fission yeast mutants unable to complete the mitosis-to-interphase transition. pim1+ encodes the guanine nucleotide exchange factor (GEF) for the spi1 GTPase. Perturbations of this GTPase system by either mutation or overproduction of its regulatory proteins cause cells to arrest with postmitotic condensed chromosomes, an unreplicated genome, and a wide medial septum. The septation phenotype of pim1-d1ts was used as the basis for a more extensive screen for this novel class of sns (septated, not in S-phase) mutants. Seventeen mutants representing 14 complementation groups were isolated. Three strains, sns-A3, sns-A5, and sns-A6, representing two different alleles, are mutated in the pim1+ gene. Of the 13 non-pim1ts sns complementation groups, 11 showed genetic interactions with the spi1 GTPase system. The genes mutated in 10 sns strains were synthetically lethal with pim1-d1, and six sns strains were hypersensitive to overexpression of one or more of the known components of the spil GTPase system. Epistasis analysis places the action of the genes mutated in nine of these strains downstream of pim1+ and the action of one gene upstream of pim1+. Three strains, sns-A2, sns-B1, and sns-B9, showed genetic interaction with the spil GTPase system in every test performed. sns-B1 and sns-B9 are likely to identify downstream targets, whereas sns-A2 is likely to identify upstream regulators of the spi1 GTPase system that are required for the mitosis-to-interphase transition.","authors":"Matynia A, Mueller U, Ong N, Demeter J, Granger AL, Hinata K, Sazer S","authors_abbrev":"Matynia A et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-04-30","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC557.03c","SPBC1289.03c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:2719527","title":"Circadian control of heat tolerance in stationary phase cultures of Schizosaccharomyces pombe.","citation":"Arch Microbiol 1989;151(2):177-9","abstract":"The capacity of stationary phase cultures of Schizosaccharomyces pombe to survive a heat treatment at 55 degrees C is controlled by a circadian rhythm. In a synchronizing light-dark-cycle this rhythm shows a stable phase relationship to the onset of light. In continuous darkness it persists for several cycles without marked damping. The free-running period of about 27 h at 30 degrees C is only slightly longer at 20 degrees C, hence temperature-compensated. These results indicate that S. pombe is a suitable experimental organism for further research into both heat tolerance and circadian rhythms.","authors":"Kippert F","authors_abbrev":"Kippert F","pubmed_publication_date":"1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19685318","title":"Live-cell fluorescence imaging of meiotic chromosome dynamics in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2009;558:53-64","abstract":"The fission yeast Schizosaccharomyces pombe has provided a useful experimental system to study nuclear structures during meiosis. Unlike many higher animals in which meiosis takes place only in specialized tissues deep inside their bodies, S. pombe is a unicellular eukaryote and its meiosis can be induced simply by depleting nitrogen sources from the culture medium. The entire process of meiosis is completed within several hours, and thus can be followed in individual living cells. These features provide ease of microscopic observation. A more trivial merit is its rod-like cell shape, which aids microscopic observation, as the long axis of cells is kept in the microscope image plane. Here we describe methods for induction of meiosis and fluorescence microscopy observation in living cells of S. pombe.","doi":"10.1007/978-1-60761-103-5_4","authors":"Asakawa H, Hiraoka Y","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-08-18","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4741142","title":"Removal of pyrimidine dimers in cells of Schizosaccharomyces pombe mutated in different repair pathways.","citation":"Biochim Biophys Acta 1973 Jul 27;312(4):617-25","abstract":"","authors":"Fabre F, Moustacchi E","authors_abbrev":"Fabre F et al.","pubmed_publication_date":"27 Jul 1973","pubmed_entrez_date":"1973-07-27","publication_year":"1973","canto_session_key":"acd3be0be0f1a9b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-20 15:37:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-20 15:37:05","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-05-20"},{"uniquename":"PMID:9873063","title":"Regulation of phosphatidylinositol 4-phosphate 5-kinase from Schizosaccharomyces pombe by casein kinase I.","citation":"J Biol Chem 1999 Jan 08;274(2):1147-55","abstract":"Phosphatidylinositol ()P 5-kinase (PtdIns(4)P 5-kinase) catalyzes the last step in the synthesis of phosphatidylinositol 4, 5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is a precursor of diacylglycerol and inositol 1,4,5-trisphosphate and is also involved in regulation of actin cytoskeleton remodeling and membrane traffic. To satisfy such varied demands in several aspects of cell physiology, synthesis of PtdIns(4,5)P2 must be stringently regulated. In this paper we describe extraction, purification, and characterization of PtdIns(4)P 5-kinase from the plasma membranes of Schizosaccharomyces pombe. We also provide evidence that PtdIns(4)P 5-kinase is phosphorylated and inactivated by Cki1, the S. pombe homolog of casein kinase I. Phosphorylation by Cki1 in vitro decreases the activity of PtdIns(4)P 5-kinase. In addition, and most importantly, overexpression of Cki1 in S. pombe results in a reduced synthesis of PtdIns(4,5)P2 and in a lower activity of PtdIns(4)P 5-kinase associated with the plasma membrane. These results suggest that PtdIns(4)P 5-kinase is a target of Cki1 in S. pombe and that Cki1 is involved in regulation of PtdIns(4, 5)P2 synthesis by phosphorylating and inactivating PtdIns(4)P 5-kinase.","authors":"Vancurova I, Choi JH, Lin H, Kuret J, Vancura A","authors_abbrev":"Vancurova I et al.","pubmed_publication_date":"08 Jan 1999","pubmed_entrez_date":"1999-01-05","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC19G12.14","SPBC1347.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AB084857","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.45"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8500466","title":"Progress in developing improved programs for pulsed field agarose gel electrophoresis of DNA.","citation":"Electrophoresis 1993 Apr;14(4):344-8","abstract":"Details are described here for using a rotating gel to perform pulsed field agarose gel electrophoresis (PFGE) with programmable control of the following variables: magnitude of the electrical field, polarity of the electrical field, temperature of the gel and position of the rotating disk upon which the agarose gel rests. By use of this procedure for programmable control, modes of PFGE have been explored that have the following characteristics: (i) resolution by DNA length is completely lost for DNA shorter than a critical length that increases as the pulse times increase, and (ii) resolution by DNA length is enhanced for longer DNAs that are shorter than a second critical length. This window of resolution can be moved to the position of the 2-6 Mb chromosomes of Schizosaccharomyces pombe.","authors":"Arshad MF, Dunn FJ, Vega R, Valvano JW, Serwer P","authors_abbrev":"Arshad MF et al.","pubmed_publication_date":"Apr 1993","pubmed_entrez_date":"1993-04-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24301766","title":"Effects of glucose sensing/signaling on oxidative stress response in glucose repression mutants of Schizosaccharomyces pombe.","citation":"Genet Mol Res 2013 Oct 25;12(4):5046-56","abstract":"The resistant to glucose repression mutants of Schizosaccharomyces pombe (ird5, ird13, and ird14) have a high tolerance to oxidative stress induced by H2O2. In all ird mutants, the increased expression level of the fbp1 gene can be interpreted as a lack of glucose repression in these mutants. To investigate the mechanisms of the oxidative stress response in ird mutants, we analyzed the transcription of stress response-related genes, sod1, ctt1, atf1, pap1, and sty1, under stressed and non-stressed conditions. We then analyzed the phosphorylation state of the Sty1-MAP kinase in ird mutants. Our findings support the concept of an adaptive response to oxidative stress in these mutants. In addition, these results imply that either glucose signaling mechanisms leading to glucose repression and glucose utilization as an energy source are regulated apart from each other or, like Saccharomyces cerevisiae, S. pombe might have additional glucose detection systems.","doi":"10.4238/2013.October.25.3","authors":"Palabiyik B, Jafari Ghods F, Onay Ucar E","authors_abbrev":"Palabiyik B et al.","pubmed_publication_date":"25 Oct 2013","pubmed_entrez_date":"2013-12-05","publication_year":"2013","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8791414","title":"Nuclear tyrosine kinases: from Abl to WEE1.","citation":"Curr Opin Cell Biol 1996 Apr;8(2):174-81","abstract":"The notion of a critical role for protein tyrosine kinases in the nucleus is supported by recent findings linking these proteins with components of the cell cycle and with the transcription machinery. Several of these tyrosine kinases localize to both nuclear and cytoplasmic compartments of the cell, and may coordinate signal transduction events in the cytoplasm with specific changes in the nucleus. Among these proteins are Abl, Rak, Fes and Fer. The past year has brought significant progress both towards the elucidation of the pathways that lead to activation of the Abl tyrosine kinase and towards the identification of novel Abl targets. Recent advances have also been made in understanding the regulation of the nucleus-specific human WEE1 tyrosine kinase. Nuclear tyrosine kinases may participate in the regulation of multiple cellular processes including transcription, DNA repair and the cell cycle.","authors":"Pendergast AM","authors_abbrev":"Pendergast AM","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11737264","title":"Characterization of GTPase-activating proteins for the function of the Rho-family small GTPases in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Cells 2001 Dec;6(12):1031-42","abstract":"The small GTPase Rho1 has been shown to regulate the organization of the actin cytoskeleton and formation of the cell wall in the fission yeast Schizosaccharomyces pombe. Activity of Rho1 must be precisely regulated in vivo, since both increases and decreases in its activity affect cell growth and shape. Thus, it is important to clarify the mechanism by which the activity of Rho1 is regulated in vivo.\nSeven genes encoding putative GAPs, GTPase-activating proteins, for the function of the Rho-family proteins were isolated from S. pombe. After disruption of these genes, rga1+ was found to play important roles in cell growth and morphogenesis. In rga1 null cells, delocalized F-actin patches and extraordinary thickening of the cell wall and the septum were observed. On the other hand, over-expression of Rga1 produced shrunken or dumpy cells. The phenotype of the rga1 null cells or the Rga1-over-expressing cells was similar to that of cells containing abnormally high or low Rho1 activity, respectively. Moreover, direct association of Rga1 with Rho1 was shown. Rga1 was localized to the cell ends and septum where Rho1 is known to function.\nIn S. pombe, Rga1 is involved in the F-actin patch localization, cell morphogenesis, regulation of septation, and cell wall synthesis, probably functioning as a GAP for the function of Rho1.","authors":"Nakano K, Mutoh T, Mabuchi I","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-12-12","publication_year":"2001","canto_session_key":"13c6c57e6425bca9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-07-09 13:33:26","canto_approved_date":"2023-01-18 09:27:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-07-09 13:33:18","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":60,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC354.13","SPBC17F3.01c","SPBC3F6.05","SPBC28E12.03","SPAC1F7.04","SPAC26A3.09c","SPAC17G8.14c","SPAC29A4.11","SPBC23G7.08c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2020-07-09"},{"uniquename":"PMID:34066375","title":"The Mitochondria-to-Cytosol H 2 O 2  Gradient Is Caused by Peroxiredoxin-Dependent Cytosolic Scavenging.","citation":"Antioxidants (Basel) 2021 May 06;10(5)","abstract":"Fluorescent protein-based reporters used to measure intracellular H 2 O 2  were developed to overcome the limitations of small permeable dyes. The two major families of genetically encoded redox reporters are the reduction-oxidation sensitive green fluorescent protein (roGFP)-based proteins fused to peroxiredoxins and HyPer and derivatives. We have used the most sensitive probes of each family, roGFP2-Tpx1.C169S and HyPer7, to monitor steady-state and fluctuating levels of peroxides in fission yeast. While both are able to monitor the nanomolar fluctuations of intracellular H 2 O 2 , the former is two-five times more sensitive than HyPer7, and roGFP2-Tpx1.C169S is partially oxidized in the cytosol of wild-type cells while HyPer7 is fully reduced. We have successfully expressed HyPer7 in the mitochondrial matrix, and it is ~40% oxidized, suggesting higher steady-state levels of peroxides, in the low micromolar range, than in the cytosol. Cytosolic HyPer7 can detect negligible H 2 O 2  in the cytosol from mitochondrial origin unless the main H 2 O 2  scavenger, the cytosolic peroxiredoxin Tpx1, is absent, while mitochondrial HyPer7 is oxidized to the same extent in wild-type and  ∆tpx1  cells. We conclude that there is a bidirectional flux of H 2 O 2  across the matrix and the cytosol, but Tpx1 rapidly and efficiently scavenges mitochondrial-generated peroxides and stops their steady-state cytosolic levels rising.","doi":"10.3390/antiox10050731","authors":"de Cubas L, Pak VV, Belousov VV, Ayté J, Hidalgo E","authors_abbrev":"de Cubas L et al.","pubmed_publication_date":"06 May 2021","pubmed_entrez_date":"2021-06-02","publication_year":"2021","canto_session_key":"29f9da4b580ba2f3","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25330395","title":"Tpz1-Ccq1 and Tpz1-Poz1 interactions within fission yeast shelterin modulate Ccq1 Thr93 phosphorylation and telomerase recruitment.","citation":"PLoS Genet 2014 Oct;10(10):e1004708","abstract":"In both fission yeast and humans, the shelterin complex plays central roles in regulation of telomerase recruitment, protection of telomeres against DNA damage response factors, and formation of heterochromatin at telomeres. While shelterin is essential for limiting activation of the DNA damage checkpoint kinases ATR and ATM at telomeres, these kinases are required for stable maintenance of telomeres. In fission yeast, Rad3ATR and Tel1ATM kinases are redundantly required for telomerase recruitment, since Rad3ATR/Tel1ATM-dependent phosphorylation of the shelterin subunit Ccq1 at Thr93 promotes interaction between Ccq1 and the telomerase subunit Est1. However, it remained unclear how protein-protein interactions within the shelterin complex (consisting of Taz1, Rap1, Poz1, Tpz1, Pot1 and Ccq1) contribute to the regulation of Ccq1 Thr93 phosphorylation and telomerase recruitment. In this study, we identify domains and amino acid residues that are critical for mediating Tpz1-Ccq1 and Tpz1-Poz1 interaction within the fission yeast shelterin complex. Using separation of function Tpz1 mutants that maintain Tpz1-Pot1 interaction but specifically disrupt either Tpz1-Ccq1 or Tpz1-Poz1 interaction, we then establish that Tpz1-Ccq1 interaction promotes Ccq1 Thr93 phosphorylation, telomerase recruitment, checkpoint inhibition and telomeric heterochromatin formation. Furthermore, we demonstrate that Tpz1-Poz1 interaction promotes telomere association of Poz1, and loss of Poz1 from telomeres leads to increases in Ccq1 Thr93 phosphorylation and telomerase recruitment, and telomeric heterochromatin formation defect. In addition, our studies establish that Tpz1-Poz1 and Tpz1-Ccq1 interactions redundantly fulfill the essential telomere protection function of the shelterin complex, since simultaneous loss of both interactions caused immediate loss of cell viability for the majority of cells and generation of survivors with circular chromosomes. Based on these findings, we suggest that the negative regulatory function of Tpz1-Poz1 interaction works upstream of Rad3ATR kinase, while Tpz1-Ccq1 interaction works downstream of Rad3ATR kinase to facilitate Ccq1 Thr93 phosphorylation and telomerase recruitment.","doi":"10.1371/journal.pgen.1004708","authors":"Harland JL, Chang YT, Moser BA, Nakamura TM","authors_abbrev":"Harland JL et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-10-21","publication_year":"2014","canto_session_key":"e1f04adb6bf32089","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Toru Nakamura","canto_first_approved_date":"2017-11-14 23:13:14","canto_approved_date":"2022-08-31 19:02:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-31 10:08:33","canto_added_date":"2014-10-22 00:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":45,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Toru Nakamura","community_curator":true,"annotation_count":7,"orcid":"0000-0001-5752-0814","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPAC6F6.16c","SPCC1259.13","SPAC26H5.06","SPCC188.07","SPAC19G12.13c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2017-11-14"},{"uniquename":"PMID:12007415","title":"Importance of a myosin II-containing progenitor for actomyosin ring assembly in fission yeast.","citation":"Curr Biol 2002 Apr 30;12(9):724-9","abstract":"An actomyosin-based contractile ring provides the forces necessary for cell cleavage in several organisms [1-3]. Myosin II is an essential component of the actomyosin ring and has also been detected as a \"spot\" in interphase Schizosaccharomyces pombe cells [4-5]. It is currently unknown if this myosin II-containing spot is important for cytokinesis. In this study, we characterize this myosin II-containing spot using a combination of genetic and cell biological analyses. Whereas myosin II at the actomyosin ring undergoes rapid turnover, myosin II at the spot does not. Maintenance of the myosin II-containing spot is independent of F-actin function. Interestingly, maintenance of this myosin II spot in interphase requires the function of Rng3p, a UCS domain-containing protein, the Caenorhabditis elegans homolog of which has recently been shown to be a cochaperone for myosin II assembly [6]. Disassembly of the spot in interphase prevents actomyosin ring formation in the subsequent mitosis, implying that the spot might represent a progenitor that is important for assembly of the actomyosin ring. Given that mitosis represents a short period of the fission yeast cell cycle, organization of this progenitor structure in interphase might ensure proper assembly of the actomyosin ring and successful cell division.","authors":"Wong KC, D'souza VM, Naqvi NI, Motegi F, Mabuchi I, Balasubramanian MK","authors_abbrev":"Wong KC et al.","pubmed_publication_date":"30 Apr 2002","pubmed_entrez_date":"2002-05-15","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4854003","title":"Radiation-induced mutation rate and DNA content in Schizosaccharomyces pombe.","citation":"Mutat Res 1974 Aug;24(2):211-2","abstract":"","authors":"Nasim A","authors_abbrev":"Nasim A","pubmed_publication_date":"Aug 1974","pubmed_entrez_date":"1974-08-01","publication_year":"1974","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7772606","title":"A cDNA of Schizosaccharomyces pombe encoding a homologue of DnaJ-like protein.","citation":"Biochim Biophys Acta 1995 May 17;1262(1):87-90","abstract":"A Schizosaccharomyces pombe homologue, Psi, was cloned from Schizosaccharomyces pombe cDNA library. Deduced amino acid sequence of the cDNA has 55% sequence homology with the Saccharomyces cerevisiae Sis1 protein and contains the structural features of a family of DnaJ proteins. This homology suggests Psi protein may be implicated in the initiation of translation as like Sis1 function of Saccharomyces cerevisiae.","authors":"Park SK, Chon SK, Yoo HS","authors_abbrev":"Park SK et al.","pubmed_publication_date":"17 May 1995","pubmed_entrez_date":"1995-05-17","publication_year":"1995","canto_session_key":"be8c9e0988aa52b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 19:07:03","canto_approved_date":"2018-12-22 19:07:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 19:06:56","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:22184248","title":"Centromere-tethered Mps1 pombe homolog (Mph1) kinase is a sufficient marker for recruitment of the spindle checkpoint protein Bub1, but not Mad1.","citation":"Proc Natl Acad Sci U S A 2012 Jan 03;109(1):209-14","abstract":"The spindle checkpoint delays the onset of anaphase until all of the chromosomes properly achieve bipolar attachment to the spindle. It has been shown that unattached kinetochores are the site that emits a signal for activation of the checkpoint. Although the components of the checkpoint such as Bub1, Mad1 and Mad2 selectively accumulate at unattached kinetochores, the answer to how they recognize unattached kinetochores has remained elusive. Mps1 pombe homolog (Mph1) kinase has been shown to function upstream of most of the components of the checkpoint and thus it is thought to recognize unattached kinetochores by itself and recruit other components. In this study we have expressed a fusion protein of Mph1 and Ndc80 (a kinetochore protein of the outer plate) and shown that the fusion protein arrests cell cycle progression in a spindle-checkpoint\\x{2013}dependent manner in fission yeast. When expression of Mad2 is turned off, the cells grow normally with Mph1 constitutively localized at centromeres/kinetochores. Under this condition, Bub1 can be found with Mph1 throughout the cell cycle, indicating that localization of Mph1 at centromeres/kinetochores is sufficient to recruit Bub1. In contrast, Mad1 is found to transiently localize at kinetochores, which are presumably unattached to the spindle, but soon it dissociates from kinetochores. We propose that Mph1 is a sufficient marker for recruitment of Bub1. Mad1, in contrast, requires an additional condition/component for stable association with kinetochores.","doi":"10.1073/pnas.1114647109","authors":"Ito D, Saito Y, Matsumoto T","authors_abbrev":"Ito D et al.","pubmed_publication_date":"03 Jan 2012","pubmed_entrez_date":"2011-12-21","publication_year":"2012","canto_session_key":"10e451ad98a96256","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-07-27 11:48:08","canto_approved_date":"2024-11-29 07:40:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-12-07 20:23:53","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.01","SPBC3D6.04c","SPBC20F10.06","SPCC1322.12c","SPBC11C11.03","SPAC23H3.08c","SPCC1795.01c","SPAC821.08c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2019-07-27"},{"uniquename":"EMBL:AU014421","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9837990","title":"Interaction of the resolving enzyme YDC2 with the four-way DNA junction.","citation":"Nucleic Acids Res 1998 Dec 15;26(24):5609-16","abstract":"Holliday junctions (four-way DNA junctions), formed during homologous recombination, are bound and resolved by junction-specific endonucleases to yield recombinant duplex DNA products. The junction-resolving enzymes are a structurally diverse class of proteins that nevertheless have many properties in common; in particular a high structure specificity for binding and metal-dependent, (frequently) sequence-specific cleavage activity. In Saccharomyces cerevisiae, the enzyme CCE1 is necessary for the resolution of recombining mitochondrial genomes, and in Schizosaccharomyces pombe the homologous protein YDC2 is thought to have a similar function. We have generated an inactive mutant of YDC2, D226N, that retains structure-specific junction binding and have analysed the interaction of this protein with the four-way DNA junction. YDC2 binds the four-way junction in two specific complexes (I and II), unfolding the stacked X-structure into a conformation where the arms extend to the four corners of a square. This structure is reminiscent of that of the free junction in the absence of metal ions and of the structures imposed on the Holliday junction by CCE1 and RuvA. DNase I probing reveals footprints specific for complexes I and II which extend from the junction centre on all four arms. No protection is observed with the small, hydrophobic probe DMS.","authors":"White MF, Lilley DM","authors_abbrev":"White MF et al.","pubmed_publication_date":"15 Dec 1998","pubmed_entrez_date":"1998-12-05","publication_year":"1998","canto_session_key":"e71863fe9b8c14c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-09-23 16:04:48","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-23 16:04:41","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-23"},{"uniquename":"PMID:24992972","title":"3D-printed microfluidic microdissector for high-throughput studies of cellular aging.","citation":"Anal Chem 2014 Aug 05;86(15):7406-12","abstract":"Due to their short lifespan, rapid division, and ease of genetic manipulation, yeasts are popular model organisms for studying aging in actively dividing cells. To study replicative aging over many cell divisions, individual cells must be continuously separated from their progeny via a laborious manual microdissection procedure. Microfluidics-based soft-lithography devices have recently been used to automate microdissection of the budding yeast Saccharomyces cerevisiae. However, little is known about replicative aging in Schizosaccharomyces pombe, a rod-shaped yeast that divides by binary fission and shares many conserved biological functions with higher eukaryotes. In this report, we develop a versatile multiphoton lithography method that enables rapid fabrication of three-dimensional master structures for polydimethylsiloxane (PDMS)-based microfluidics. We exploit the rapid prototyping capabilities of multiphoton lithography to create and characterize a cell-capture device that is capable of high-resolution microscopic observation of hundreds of individual S. pombe cells. By continuously removing the progeny cells, we demonstrate that cell growth and protein aggregation can be tracked in individual cells for over ~100 h. Thus, the fission yeast lifespan microdissector (FYLM) provides a powerful on-chip microdissection platform that will enable high-throughput studies of aging in rod-shaped cells.","doi":"10.1021/ac500893a","authors":"Spivey EC, Xhemalce B, Shear JB, Finkelstein IJ","authors_abbrev":"Spivey EC et al.","pubmed_publication_date":"05 Aug 2014","pubmed_entrez_date":"2014-07-05","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-07-07 00:15:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21914852","title":"Evolutionary divergence of intrinsic and trans-regulated nucleosome positioning sequences reveals plastic rules for chromatin organization.","citation":"Genome Res 2011 Nov;21(11):1851-62","abstract":"The packaging of eukaryotic genomes into nuclesomes plays critical roles in chromatin organization and gene regulation. Studies in Saccharomyces cerevisiae indicate that nucleosome occupancy is partially encoded by intrinsic antinucleosomal DNA sequences, such as poly(A) sequences, as well as by binding sites for trans-acting factors that can evict nucleosomes, such as Reb1 and the Rsc3/30 complex. Here, we use genome-wide nucleosome occupancy maps in 13 Ascomycota fungi to discover large-scale evolutionary reprogramming of both intrinsic and trans determinants of chromatin structure. We find that poly(G)s act as intrinsic antinucleosomal sequences, comparable to the known function of poly(A)s, but that the abundance of poly(G)s has diverged greatly between species, obscuring their antinucleosomal effect in low-poly(G) species such as S. cerevisiae. We also develop a computational method that uses nucleosome occupancy maps for discovering trans-acting general regulatory factor (GRF) binding sites. Our approach reveals that the specific sequences bound by GRFs have diverged substantially across evolution, corresponding to a number of major evolutionary transitions in the repertoire of GRFs. We experimentally validate a proposed evolutionary transition from Cbf1 as a major GRF in pre-whole-genome duplication (WGD) yeasts to Reb1 in post-WGD yeasts. We further show that the mating type switch-activating protein Sap1 is a GRF in S. pombe, demonstrating the general applicability of our approach. Our results reveal that the underlying mechanisms that determine in vivo chromatin organization have diverged and that comparative genomics can help discover new determinants of chromatin organization.","doi":"10.1101/gr.122267.111","authors":"Tsankov A, Yanagisawa Y, Rhind N, Regev A, Rando OJ","authors_abbrev":"Tsankov A et al.","pubmed_publication_date":"Nov 2011","pubmed_entrez_date":"2011-09-15","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26034658","title":"The ClpS-like N-domain is essential for the functioning of Ubr11, an N-recognin in Schizosaccharomyces pombe.","citation":"Springerplus 2014;3:257","abstract":"Several Ubr ubiquitin ligases recognize the N-terminal amino acid of substrate proteins and promote their degradation via the Arg/N-end rule pathway. The primary destabilizing N-terminal amino acids in yeast are classified into type 1 (Arg, Lys, and His) and type 2 (Phe, Trp, Tyr, Leu, Ile, and Met-Ф) residues. The type 1 and type 2 residues bind to the UBR box and the ClpS/N-domain, respectively, in canonical Ubr ubiquitin ligases that act as N-recognins. In this study, the requirement for type 1 and type 2 amino acid recognition by Schizosaccharomyces pombe Ubr11 was examined in vivo. Consistent with the results of previous studies, the ubr11∆ null mutant was found to be defective in oligopeptide uptake and resistant to ergosterol synthesis inhibitors. Furthermore, the ubr11∆ mutant was also less sensitive to some protein synthesis inhibitors. A ubr11 ClpS/N-domain mutant, which retained ubiquitin ligase activity but could not recognize type 2 amino acids, phenocopied all known defects of the ubr11∆ mutant. However, the recognition of type 1 residues by Ubr11 was not required for its functioning, and no severe physiological abnormalities were observed in a ubr11 mutant defective in the recognition of type 1 residues. These results reinforce the fundamental importance of the ClpS/N-domain for the functioning of the N-recognin, Ubr11.","doi":"10.1186/2193-1801-3-257","authors":"Kitamura K","authors_abbrev":"Kitamura K","pubmed_publication_date":"2014","pubmed_entrez_date":"2015-06-03","publication_year":"2014","canto_session_key":"8d370598c22e8a0a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-06-09 00:28:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25587012","title":"Comparative genomics suggests primary homothallism of Pneumocystis species.","citation":"mBio 2015 Jan 13;6(1)","abstract":"Pneumocystis species are fungal parasites of mammal lungs showing host specificity. Pneumocystis jirovecii colonizes humans and causes severe pneumonia in immunosuppressed individuals. In the absence of in vitro cultures, the life cycle of these fungi remains poorly known. Sexual reproduction probably occurs, but the system of this process and the mating type (MAT) genes involved are not characterized. In the present study, we used comparative genomics to investigate the issue in P. jirovecii and Pneumocystis carinii, the species infecting rats, as well as in their relative Taphrina deformans. We searched sex-related genes using 103 sequences from the relative Schizosaccharomyces pombe as queries. Genes homologous to several sex-related role categories were identified in all species investigated, further supporting sexuality in these organisms. Extensive in silico searches identified only three putative MAT genes in each species investigated (matMc, matMi, and matPi). In P. jirovecii, these genes clustered on the same contig, proving their contiguity in the genome. This organization seems compatible neither with heterothallism, because two different MAT loci on separate DNA molecules would have been detected, nor with secondary homothallism, because the latter involves generally more MAT genes. Consistently, we did not detect cis-acting sequences for mating type switching in secondary homothallism, and PCR revealed identical MAT genes in P. jirovecii isolates from six patients. A strong synteny of the genomic region surrounding the putative MAT genes exists between the two Pneumocystis species. Our results suggest the hypothesis that primary homothallism is the system of reproduction of Pneumocystis species and T. deformans.\nSexual reproduction among fungi can involve a single partner (homothallism) or two compatible partners (heterothallism). We investigated the issue in three pathogenic fungal relatives: Pneumocystis jirovecii, which causes severe pneumonia in immunocompromised humans; Pneumocystis carinii, which infects rats; and the plant pathogen Taphrina deformans. The nature, the number, and the organization within the genome of the genes involved in sexual reproduction were determined. The three species appeared to harbor a single genomic region gathering only three genes involved in sexual differentiation, an organization which is compatible with sexual reproduction involving a single partner. These findings illuminate the strategy adopted by fungal pathogens to infect their hosts.","doi":"10.1128/mBio.02250-14","authors":"Almeida JM, Cissé OH, Fonseca Á, Pagni M, Hauser PM","authors_abbrev":"Almeida JM et al.","pubmed_publication_date":"13 Jan 2015","pubmed_entrez_date":"2015-01-15","publication_year":"2015","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2015-01-16 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9224658","title":"Molecular genetic elucidation of the tripartite structure of the Schizosaccharomyces pombe 72 kDa TFIID subunit which contains a WD40 structural motif.","citation":"Genes Cells 1997 Apr;2(4):245-54","abstract":"The multisubunit general transcription factor termed TFIID is comprised of the TATA box DNA binding protein TBP and several TBP-associated factors termed TAFs. Current arguments regarding the mechanisms of regulation of transcription contend that TFIID makes multiple specific protein-protein interactions with numerous protein factors, and that these interactions are important for the regulation of transcriptional initiation. TAFs contain a variety of potential structural motifs and it has been speculated that these motifs participate directly in TAF function. However, to date the physiological significance of these putative structural motifs has not been systematically analysed in vivo.\nThe essential gene encoding the Schizosaccharomyces pombe 72 kDa TFIID subunit is termed taf72+, which contains WD40 repeats, was cloned and sequenced. A comparison of the primary structure of this gene with its Drosophila and S. cerevisiae counterparts suggests the presence of regions that might play a role in TFIID function, due to the fact that significant portions of the sequences are highly conserved. Complementation analyses of a series of deletion mutants of this gene revealed that the most evolutionarily conserved regions of taf72+, including the WD40 repeats, are in fact indispensable for the viability.\nThe 72 kDa subunit of S. pombe TFIID, which contains putative WD40 repeats, consists of three distinct functional domains separated by intervening regions. The functional significance of the WD40 repeats is demonstrated by this in vivo study.","authors":"Yamamoto T, Poon D, Weil PA, Horikoshi M","authors_abbrev":"Yamamoto T et al.","pubmed_publication_date":"Apr 1997","pubmed_entrez_date":"1997-04-01","publication_year":"1997","canto_session_key":"24e1cb4e93273c16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-09-11 13:24:57","canto_approved_date":"2022-02-01 18:03:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 13:24:50","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-11"},{"uniquename":"PMID:7923372","title":"Cooperative interaction of S. pombe proteins required for mating and morphogenesis.","citation":"Cell 1994 Oct 07;79(1):131-41","abstract":"We isolated two S. pombe genes, scd1 and scd2, that are required for normal morphology and mating. scd1 and scd2 are homologous to CDC24 and BEM1, respectively, of S. cerevisiae. Epistasis analyses indicate that scd2 and ras1 converge upon scd1, which, in turn, interacts with cdc42sp, a RHO-like GTPase. Studies with the yeast two-hybrid system indicate that scd2 forms complexes with both scd1 and cdc42sp. Furthermore, biochemical studies indicate that the interaction between scd1 and scd2 is direct. The yeast two-hybrid data further suggest that scd1, scd2, cdc42sp, and ras1, in its GTP-bound state, act cooperatively to form a protein complex.","authors":"Chang EC, Barr M, Wang Y, Jung V, Xu HP, Wigler MH","authors_abbrev":"Chang EC et al.","pubmed_publication_date":"07 Oct 1994","pubmed_entrez_date":"1994-10-07","publication_year":"1994","canto_session_key":"7537db502e936856","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-15 16:31:51","canto_approved_date":"2026-02-19 15:49:37","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2022-05-25 13:40:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16E8.09","SPAC11H11.04","SPAC22H10.07","SPAC110.03","SPAC1D4.13","SPBC1D7.05","SPAC17H9.09c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2018-06-15"},{"uniquename":"PMID:40015273","title":"A comprehensive Schizosaccharomyces pombe atlas of physical transcription factor interactions with proteins and chromatin.","citation":"Mol Cell 2025 Feb 19;","abstract":"Transcription factors (TFs) are key regulators of gene expression, yet many of their targets and modes of action remain unknown. In Schizosaccharomyces pombe, one-third of TFs are solely homology predicted, with few experimentally validated. We created a comprehensive library of 89 endogenously tagged S. pombe TFs, mapping their protein and chromatin interactions using immunoprecipitation-mass spectrometry and chromatin immunoprecipitation sequencing. Our study identified protein interactors for half the TFs, with over a quarter potentially forming stable complexes. We discovered DNA-binding sites for most TFs across 2,027 unique genomic regions, revealing motifs for 38 TFs and uncovering a complex network of extensive TF cross- and autoregulation. Characterization of the largest TF family revealed conserved DNA sequence preferences but diverse binding patterns and identified a repressive heterodimer, Ntu1/Ntu2, linked to perinuclear gene localization. Our TFexplorer webtool makes all data interactively accessible, offering insights into TF interactions and regulatory mechanisms with broad biological relevance.","doi":"10.1016/j.molcel.2025.01.032","authors":"Skribbe M, Soneson C, Stadler MB, Schwaiger M, Suma Sreechakram VN, Iesmantavicius V, Hess D, Moreno EPF, Braun S, Seebacher J, Smallwood SA, Bühler M","authors_abbrev":"Skribbe M et al.","pubmed_publication_date":"19 Feb 2025","pubmed_entrez_date":"2025-02-27","publication_year":"2025","canto_session_key":"a701986324b116dd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Merle Skribbe","canto_first_approved_date":"2025-03-19 15:35:25","canto_approved_date":"2025-03-27 18:30:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-13 11:22:21","canto_added_date":"2025-03-01 00:25:05","annotation_curators":[{"name":"Merle Skribbe","community_curator":true,"annotation_count":42,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Kim Rutherford","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Kim 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Schizosaccharomyces pombe homologue of the chaperone calnexin is essential for viability.","citation":"J Biol Chem 1995 Mar 03;270(9):4845-53","abstract":"We have cloned a Schizosaccharomyces pombe gene, here designated cnx1, encoding the homologue of the endoplasmic reticulum molecular chaperone calnexin. Disruption of the cnx1 gene was lethal, demonstrating that it has an essential cellular function. Transcription of cnx1 mRNA is initiated at multiple sites, and it can be induced by various stress treatments that lead to the accumulation of unfolded and/or misfolded proteins in the endoplasmic reticulum. The encoded Cnx1p protein more closely resembles its plant and animal calnexin homologues than that of Saccharomyces cerevisiae. Cnx1p is acidic and migrates aberrantly on SDS-polyacrylamide gel electrophoresis, similar to its mammalian counterparts. Cnx1p contains the hallmark KPEDWD motifs that are found in all members of the calnexin/calreticulin family of proteins. Using an in vitro translation-processing system, we have shown that Cnx1p has the characteristic type I topology of calnexin proteins. Unlike its higher eukaryotic homologues, Cnx1p has a site for N-glycosylation that was modified in an in vitro translation-processing assay.","authors":"Jannatipour M, Rokeach LA","authors_abbrev":"Jannatipour M et al.","pubmed_publication_date":"03 Mar 1995","pubmed_entrez_date":"1995-03-03","publication_year":"1995","canto_session_key":"aa80b6544eead412","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 15:56:26","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-01-02 15:35:04","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-02"},{"uniquename":"PMID:18199689","title":"Distinct chromatin modulators regulate the formation of accessible and repressive chromatin at the fission yeast recombination hotspot ade6-M26.","citation":"Mol Biol Cell 2008 Mar;19(3):1162-73","abstract":"Histone acetyltransferases (HATs) and ATP-dependent chromatin remodeling factors (ADCRs) regulate transcription and recombination via alteration of local chromatin configuration. The ade6-M26 allele of Schizosaccharomyces pombe creates a meiotic recombination hotspot that requires a cAMP-responsive element (CRE)-like sequence M26, the Atf1/Pcr1 heterodimeric ATF/CREB transcription factor, the Gcn5 HAT, and the Snf22 SWI2/SNF2 family ADCR. Chromatin alteration occurs meiotically around M26, leading to the activation of meiotic recombination. We newly report the roles of other chromatin remodeling factors that function positively and negatively in chromatin alteration at M26: two CHD-1 family ADCRs (Hrp1 and Hrp3), a Spt-Ada-Gcn5 acetyltransferase component (Ada2), and a member of Moz-Ybf2/Sas3-Sas2-Tip60 family (Mst2). Ada2, Mst2, and Hrp3 are required for the full activation of chromatin changes around M26 and meiotic recombination. Acetylation of histone H3 around M26 is remarkably reduced in gcn5Delta, ada2Delta and snf22Delta, suggesting cooperative functions of these HAT complexes and Snf22. Conversely, Hrp1, another CHD-1 family ADCR, maintains repressive chromatin configuration at ade6-M26. Interestingly, transcriptional initiation site is shifted to a site around M26 from the original initiation sites, in couple with the histone acetylation and meiotic chromatin alteration induced around 3' region of M26, suggesting a collaboration between these chromatin modulators and the transcriptional machinery to form accessible chromatin. These HATs and ADCRs are also required for the regulation of transcription and chromatin structure around M26 in response to osmotic stress. Thus, we propose that multiple chromatin modulators regulate chromatin structure reversibly and participate in the regulation of both meiotic recombination and stress-induced transcription around CRE-like sequences.","authors":"Hirota K, Mizuno K, Shibata T, Ohta K","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-01-18","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.08c","SPAC3G6.01","SPAC1952.05","SPCC1620.14c","SPAC17G8.13c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:24493644","title":"lncRNA recruits RNAi and the exosome to dynamically regulate pho1 expression in response to phosphate levels in fission yeast.","citation":"Genes Dev 2014 Feb 01;28(3):231-44","abstract":"Numerous noncoding transcripts of unknown function have recently been identified. In this study, we report a novel mechanism that relies on transcription of noncoding RNA prt (pho1-repressing transcript) regulating expression of the pho1 gene. A product of this gene, Pho1, is a major secreted phosphatase needed for uptake of extracellular phosphate in fission yeast. prt is produced from the promoter located upstream of the pho1 gene in response to phosphate, and its transcription leads to deposition of RNAi-dependent H3K9me2 across the pho1 locus. In contrast, phosphate starvation leads to loss of H3K9me2 and pho1 induction. Strikingly, deletion of Clr4, a H3K9 methyltransferase, results in faster pho1 induction in response to phosphate starvation. We propose a new role for noncoding transcription in establishing transient heterochromatin to mediate an effective transcriptional response to environmental stimuli. RNAi recruitment to prt depends on the RNA-binding protein Mmi1. Importantly, we found that the exosome complex and Mmi1 are required for transcription termination and the subsequent degradation of prt but not pho1 mRNA. Moreover, in mitotic cells, transcription termination of meiotic RNAs also relies on this mechanism. We propose that exosome-dependent termination constitutes a specialized system that primes transcripts for degradation to ensure their efficient elimination.","doi":"10.1101/gad.230177.113","authors":"Shah S, Wittmann S, Kilchert C, Vasiljeva L","authors_abbrev":"Shah S et al.","pubmed_publication_date":"01 Feb 2014","pubmed_entrez_date":"2014-02-05","publication_year":"2014","canto_session_key":"ff703973c23246bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-01 09:42:58","canto_approved_date":"2024-04-02 14:43:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-19 19:08:34","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":37,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.103","SPAC26A3.12c","SPAC6F12.09","SPAC12G12.14c","SPBC26H8.10","SPBP4G3.02","SPBC16C6.10","SPBPB2B2.02","SPAC1F3.01","SPCC736.12c","SPCC736.11","SPNCRNA.1712","SPBC428.08c","SPCC188.13c","SPAC1006.03c","SPAC664.01c"],"gene_count":16,"ltp_gene_count":14,"approved_date":"2017-12-01"},{"uniquename":"PMID:19500986","title":"Mechanical forces of fission yeast growth.","citation":"Curr Biol 2009 Jul 14;19(13):1096-101","abstract":"Mechanical properties contribute to the control of cell size, morphogenesis, development, and lifestyle of fungal cells. Tip growth can be understood by a viscoplastic model, in which growth is derived by high internal turgor pressure and cell-wall elasticity. To understand how these properties regulate growth in the rod-shaped fission yeast Schizosaccaromyces pombe, we devised femtoliter cylindrical polydimethylsiloxane (PDMS) microchambers with varying elasticity as force sensors for single cells. By buckling cells in these chambers, we determine the elastic surface modulus of the cell wall to be 20.2 +/- 6.1 N.m(-1). By analyzing the growth of the cells as they push against the walls of the chamber, we derive force-velocity relationships and values for internal effective turgor pressure of 0.85 +/- 0.15 MPa and a growth-stalling force of 11 +/- 3 muN. The behavior of cells buckling under the force of their own growth provides an independent test of this model and parameters. Force generation is dependent on turgor pressure and a glycerol synthesis gene, gpd1(+) (glycerol-3-phosphate dehydrogenase), and is independent of actin cables. This study develops a quantitative framework for tip cell growth and characterizes mechanisms of force generation that contribute to fungal invasion into host tissues.","doi":"10.1016/j.cub.2009.05.031","authors":"Minc N, Boudaoud A, Chang F","authors_abbrev":"Minc N et al.","pubmed_publication_date":"14 Jul 2009","pubmed_entrez_date":"2009-06-09","publication_year":"2009","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1828291","title":"Identification of a G1-type cyclin puc1+ in the fission yeast Schizosaccharomyces pombe.","citation":"Nature 1991 May 16;351(6323):245-8","abstract":"In rapidly growing cells of the budding yeast Saccharomyces cerevisiae, the cell cycle is regulated chiefly at Start, just before the G1-S boundary, whereas in the fission yeast Schizosaccharomyces pombe, the cycle is predominantly regulated at G2-M. Both control points are present in both yeasts, and both require the p34cdc2 protein kinase. At G2-M, p34cdc2 kinase activity in S. pombe requires a B-type cyclin in a complex with p34cdc2; this complex is the same as MPF (maturation promoting factor). The p34cdc2 activity at the G1-S transition in S. cerevisiae may be regulated by a similar cyclin complex, using one of the products of a new class of cyclin genes (CLN1, CLN2 and WHI1 (DAF1/CLN3)). At least one is required for progression through the G1-S phase, and deletion of all three leads to G1 arrest. WHI1 was isolated as a dominant allele causing budding yeast cells to divide at a reduced size and was later independently identified as DAF1, a dominant allele of which rendered the cells refractory to the G1-arrest induced by the mating pheromone alpha-factor. The dominant alleles are truncations thought to yield proteins of increased stability, and the cells are accelerated through G1. Without WHI1 function, the cells are hypersensitive to alpha-factor, enlarged and delayed in G1. Heretofore, this G1-class of cyclins has not been identified in other organisms. We have isolated a G1-type cyclin gene called puc1+ from S. pombe, using a functional assay in S. cerevisiae. Expression of puc1+ in S. pombe indicates that it has a cyclin-like role in the fission yeast distinct from the role of the B-type mitotic cyclin.","authors":"Forsburg SL, Nurse P","authors_abbrev":"Forsburg SL et al.","pubmed_publication_date":"16 May 1991","pubmed_entrez_date":"1991-05-16","publication_year":"1991","canto_session_key":"426a7a471f3b855c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-09-12 16:12:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-01 15:10:46","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC19F5.01c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-01"},{"uniquename":"PMID:30635289","title":"Cell Cycle-Regulated Transcription of CENP-A by the MBF Complex Ensures Optimal Level of CENP-A for Centromere Formation.","citation":"Genetics 2019 Mar;211(3):861-875","abstract":"The centromere plays an essential role in chromosome segregation. In most eukaryotes, centromeres are epigenetically defined by the conserved histone H3 variant CENP-A. Proper centromere assembly is dependent upon the tight regulation of CENP-A level. Cell cycle regulation of CENP-A transcription appears to be a universal feature across eukaryotes, but the molecular mechanism underlying the temporal control of CENP-A transcription and how such regulation contributes to centromere function remains elusive. CENP-A in fission yeast has been shown to be transcribed before S phase. Using various synchronization methods, we confirmed that CENP-A transcription occurs at G1, leading to an almost twofold increase of the protein during S phase. Through a genetic screen, we identified the MBF (MluI box-binding factors) complex as a key regulator of temporal control of CENP-A transcription. The periodic transcription of CENP-A is lost in MBF mutants, resulting in CENP-A mislocalization and chromosome segregation defects. We identified the MCB (MluI cell cycle box) motif in the CENP-A promoter, and further showed that the MBF complex binds to the motif to restrict CENP-A transcription to G1. Mutations of the MCB motif cause constitutive CENP-A expression and deleterious effects on cell survival. Using promoters driving transcription to different cell cycle stages, we found that timing of CENP-A transcription is dispensable for its centromeric localization. Our data instead indicate that cell cycle-regulated CENP-A transcription is a key step to ensure that a proper amount of CENP-A is generated across generations. This study provides mechanistic insights into the regulation of cell cycle-dependent CENP-A transcription, as well as its importance on centromere function.","doi":"10.1534/genetics.118.301745","authors":"Aristizabal-Corrales D, Yang J, Li F","authors_abbrev":"Aristizabal-Corrales D et al.","pubmed_publication_date":"Mar 2019","pubmed_entrez_date":"2019-01-13","publication_year":"2019","canto_session_key":"5ecaf4c5a3d33afa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Fei Li","canto_first_approved_date":"2024-07-23 12:23:00","canto_approved_date":"2024-07-23 12:23:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-05 07:57:04","canto_added_date":"2019-01-14 01:15:04","annotation_curators":[{"name":"Fei Li","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.07c","SPAC22F3.09c","SPAC1834.04","SPBC14C8.07c","SPBC1105.17","SPBC21B10.13c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2024-07-23"},{"uniquename":"PMID:27101289","title":"Evolution of Telomeres in Schizosaccharomyces pombe and Its Possible Relationship to the Diversification of Telomere Binding Proteins.","citation":"PLoS One 2016;11(4):e0154225","abstract":"Telomeres of nuclear chromosomes are usually composed of an array of tandemly repeated sequences that are recognized by specific Myb domain containing DNA-binding proteins (telomere-binding proteins, TBPs). Whereas in many eukaryotes the length and sequence of the telomeric repeat is relatively conserved, telomeric sequences in various yeasts are highly variable. Schizosaccharomyces pombe provides an excellent model for investigation of co-evolution of telomeres and TBPs. First, telomeric repeats of S. pombe differ from the canonical mammalian type TTAGGG sequence. Second, S. pombe telomeres exhibit a high degree of intratelomeric heterogeneity. Third, S. pombe contains all types of known TBPs (Rap1p [a version unable to bind DNA], Tay1p/Teb1p, and Taz1p) that are employed by various yeast species to protect their telomeres. With the aim of reconstructing evolutionary paths leading to a separation of roles between Teb1p and Taz1p, we performed a comparative analysis of the DNA-binding properties of both proteins using combined qualitative and quantitative biochemical approaches. Visualization of DNA-protein complexes by electron microscopy revealed qualitative differences of binding of Teb1p and Taz1p to mammalian type and fission yeast telomeres. Fluorescence anisotropy analysis quantified the binding affinity of Teb1p and Taz1p to three different DNA substrates. Additionally, we carried out electrophoretic mobility shift assays using mammalian type telomeres and native substrates (telomeric repeats, histone-box sequences) as well as their mutated versions. We observed relative DNA sequence binding flexibility of Taz1p and higher binding stringency of Teb1p when both proteins were compared directly to each other. These properties may have driven replacement of Teb1p by Taz1p as the TBP in fission yeast.","doi":"10.1371/journal.pone.0154225","authors":"Sepsiova R, Necasova I, Willcox S, Prochazkova K, Gorilak P, Nosek J, Hofr C, Griffith JD, Tomaska L","authors_abbrev":"Sepsiova R et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-04-22","publication_year":"2016","canto_session_key":"157f44cabecf9aac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-11-24 00:24:39","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-08-01 13:38:48","canto_added_date":"2016-04-23 00:15:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.07c","SPAC13G7.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-08-01"},{"uniquename":"PMID:24334290","title":"Variant non ketotic hyperglycinemia is caused by mutations in LIAS, BOLA3 and the novel gene GLRX5.","citation":"Brain 2014 Feb;137(Pt 2):366-79","abstract":"Patients with nonketotic hyperglycinemia and deficient glycine cleavage enzyme activity, but without mutations in AMT, GLDC or GCSH, the genes encoding its constituent proteins, constitute a clinical group which we call 'variant nonketotic hyperglycinemia'. We hypothesize that in some patients the aetiology involves genetic mutations that result in a deficiency of the cofactor lipoate, and sequenced genes involved in lipoate synthesis and iron-sulphur cluster biogenesis. Of 11 individuals identified with variant nonketotic hyperglycinemia, we were able to determine the genetic aetiology in eight patients and delineate the clinical and biochemical phenotypes. Mutations were identified in the genes for lipoate synthase (LIAS), BolA type 3 (BOLA3), and a novel gene glutaredoxin 5 (GLRX5). Patients with GLRX5-associated variant nonketotic hyperglycinemia had normal development with childhood-onset spastic paraplegia, spinal lesion, and optic atrophy. Clinical features of BOLA3-associated variant nonketotic hyperglycinemia include severe neurodegeneration after a period of normal development. Additional features include leukodystrophy, cardiomyopathy and optic atrophy. Patients with lipoate synthase-deficient variant nonketotic hyperglycinemia varied in severity from mild static encephalopathy to Leigh disease and cortical involvement. All patients had high serum and borderline elevated cerebrospinal fluid glycine and cerebrospinal fluid:plasma glycine ratio, and deficient glycine cleavage enzyme activity. They had low pyruvate dehydrogenase enzyme activity but most did not have lactic acidosis. Patients were deficient in lipoylation of mitochondrial proteins. There were minimal and inconsistent changes in cellular iron handling, and respiratory chain activity was unaffected. Identified mutations were phylogenetically conserved, and transfection with native genes corrected the biochemical deficiency proving pathogenicity. Treatments of cells with lipoate and with mitochondrially-targeted lipoate were unsuccessful at correcting the deficiency. The recognition of variant nonketotic hyperglycinemia is important for physicians evaluating patients with abnormalities in glycine as this will affect the genetic causation and genetic counselling, and provide prognostic information on the expected phenotypic course.","doi":"10.1093/brain/awt328","authors":"Baker PR, Friederich MW, Swanson MA, Shaikh T, Bhattacharya K, Scharer GH, Aicher J, Creadon-Swindell G, Geiger E, MacLean KN, Lee WT, Deshpande C, Freckmann ML, Shih LY, Wasserstein M, Rasmussen MB, Lund AM, Procopis P, Cameron JM, Robinson BH, Brown GK, Brown RM, Compton AG, Dieckmann CL, Collard R, Coughlin CR, Spector E, Wempe MF, Van Hove JL","authors_abbrev":"Baker PR et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-12-17","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4B3.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19399178","title":"Efficient second strand cleavage during Holliday junction resolution by RuvC requires both increased junction flexibility and an exposed 5' phosphate.","citation":"PLoS One 2009;4(4):e5347","abstract":"Holliday junction (HJ) resolution is a critical step during homologous recombination. In Escherichia coli this job is performed by a member of the RNase H/Integrase superfamily called RuvC, whereas in Schizosaccharomyces pombe it has been attributed to the XPF family member Mus81-Eme1. HJ resolution is achieved through the sequential cleavage of two strands of like polarity at or close to the junction crossover point. RuvC functions as a dimer, whereas Mus81-Eme1 is thought to function as a dimer of heterodimers. However, in both cases the multimer contains two catalytic sites, which act independently and sequentially during the resolution reaction. To ensure that both strands are cleaved before the nuclease dissociates from the junction, the rate of second strand cleavage is greatly enhanced compared to that of the first. The enhancement of second strand cleavage has been attributed to the increased flexibility of the nicked HJ, which would facilitate rapid engagement of the second active site and scissile bond. Here we have investigated whether other properties of the nicked HJ are important for enhancing second strand cleavage.\nA comparison of the efficiency of cleavage of nicked HJs with and without a 5' phosphate at the nick site shows that a 5' phosphate is required for most of the enhancement of second strand cleavage by RuvC. In contrast Mus81-Eme1 cleaves nicked HJs with and without a 5' phosphate with equal efficiency, albeit there are differences in cleavage site selection.\nOur data show that efficient HJ resolution by RuvC depends on the 5' phosphate revealed by incision of the first strand. This is a hitherto unappreciated factor in promoting accelerated second strand cleavage. However, a 5' phosphate is not a universal requirement since efficient cleavage by Mus81-Eme1 appears to depend solely on the increased junction flexibility that is developed by the first incision.","doi":"10.1371/journal.pone.0005347","authors":"Osman F, Gaskell L, Whitby MC","authors_abbrev":"Osman F et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-04-29","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8141795","title":"Feedback controls and G2 checkpoints: fission yeast as a model system.","citation":"Bioessays 1993 Dec;15(12):775-82","abstract":"Dependency relationships within the cell cycle allow cells to arrest the cycle reversibly in response to agents or conditions that interfere with specific aspects of its normal progression. In addition, overlapping pathways exist which also arrest the cell cycle in response to DNA damage. Collectively, these control mechanisms have become known as checkpoints. Analysis of checkpoints is facilitated by the fact that dependency relationships within the cell cycle, such as the dependency of mitosis on the completion of DNA synthesis, and the DNA damage checkpoint can be separated genetically. In fission yeast, Schizosaccharomyces pombe, the dependency of mitosis on prior completion of DNA synthesis is mediated through tyrosine-15 phosphorylation of the ubiquitous mitotic regulator p34cdc2. In contrast, the arrest of mitosis caused by DNA damage acts through a separate mechanism that appears to be independent of tyrosine-15 phosphorylation. Despite these distinct interactions with the mitotic machinery, the majority of fission yeast mutants that are deficient in mitotic arrest after DNA damage are also unable to respond to inhibition of DNA synthesis. In this essay we survey the current knowledge concerning feedback controls and checkpoints within fission yeast and relate this to information derived from other systems.","authors":"Sheldrick KS, Carr AM","authors_abbrev":"Sheldrick KS et al.","pubmed_publication_date":"Dec 1993","pubmed_entrez_date":"1993-12-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26519310","title":"Isolation of Cytokinetic Actomyosin Rings from Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2016;1369:125-136","abstract":"Cytokinesis is the final stage of cell division, through which cellular constituents of mother cells are partitioned into two daughter cells resulting in the increase in cell number. In animal and fungal cells cytokinesis is mediated by an actomyosin contractile ring, which is attached to the overlying cell membrane. Contraction of this ring after chromosome segregation physically severs the mother cell into two daughters. Here we describe methods for the isolation and partial purification of the actomyosin ring from the fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae, which can serve as in vitro systems to facilitate biochemical and ultrastructural analysis of cytokinesis in these genetically tractable model systems.","doi":"10.1007/978-1-4939-3145-3_10","authors":"Huang J, Mishra M, Palani S, Chew TG, Balasubramanian MK","authors_abbrev":"Huang J et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-11-01","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-02 01:19:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19672306","title":"Genome-wide screen of genes required for caffeine tolerance in fission yeast.","citation":"PLoS One 2009 Aug 12;4(8):e6619","abstract":"An excess of caffeine is cytotoxic to all eukaryotic cell types. We aim to study how cells become tolerant to a toxic dose of this drug, and the relationship between caffeine and oxidative stress pathways.\nWe searched for Schizosaccharomyces pombe mutants with inhibited growth on caffeine-containing plates. We screened a collection of 2,700 haploid mutant cells, of which 98 were sensitive to caffeine. The genes mutated in these sensitive clones were involved in a number of cellular roles including the H(2)O(2)-induced Pap1 and Sty1 stress pathways, the integrity and calcineurin pathways, cell morphology and chromatin remodeling. We have investigated the role of the oxidative stress pathways in sensing and promoting survival to caffeine. The Pap1 and the Sty1 pathways are both required for normal tolerance to caffeine, but only the Sty1 pathway is activated by the drug. Cells lacking Pap1 are sensitive to caffeine due to the decreased expression of the efflux pump Hba2. Indeed, ?hba2 cells are sensitive to caffeine, and constitutive activation of the Pap1 pathway enhances resistance to caffeine in an Hba2-dependent manner.\nWith our caffeine-sensitive, genome-wide screen of an S. pombe deletion collection, we have demonstrated the importance of some oxidative stress pathway components on wild-type tolerance to the drug.","doi":"10.1371/journal.pone.0006619","authors":"Calvo IA, Gabrielli N, Iglesias-Baena I, García-Santamarina S, Hoe KL, Kim DU, Sansó M, Zuin A, Pérez P, Ayté J, Hidalgo E","authors_abbrev":"Calvo IA et al.","pubmed_publication_date":"12 Aug 2009","pubmed_entrez_date":"2009-08-13","publication_year":"2009","canto_session_key":"be5479891992fa57","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-09-14 13:14:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-12-19 10:29:40","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":173,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_19672306_phaf.tsv"}],"genes":["SPBC3H7.12","SPAC56F8.04c","SPBC651.11c","SPAC637.07","SPBC29B5.01","SPAC7D4.07c","SPCC18.06c","SPBC119.05c","SPAC144.02","SPAC17G8.14c","SPAC25A8.01c","SPAC31A2.13c","SPBC1685.01","SPBC216.05","SPAC1F3.02c","SPAC23G3.03","SPAC513.03","SPBC215.03c","SPCC16A11.07","SPCC18B5.01c","SPAC644.14c","SPAC19G12.15c","SPBC119.08","SPAC1142.07c","SPBC3F6.03","SPBC543.07","SPAC11H11.01","SPAC24B11.06c","SPAC1805.07c","SPCC306.06c","SPAC16.01","SPCC338.16","SPBC354.05c","SPBC428.04","SPAC17C9.13c","SPCC594.04c","SPAC19A8.04","SPBC1778.03c","SPAC13G6.14","SPCC23B6.05c","SPCC830.06","SPCC74.09","SPBC15D4.15","SPAC21E11.03c","SPAC20G8.04c","SPAC8C9.17c","SPAC15A10.03c","SPAC1834.08","SPCC757.09c","SPBC2G2.13c","SPCC4B3.02c","SPAC1F5.09c","SPBC409.07c","SPBP8B7.22","SPAC1834.05","SPBC106.02c","SPAC29A4.20","SPBC27.02c","SPAC23D3.09","SPBC3B9.09","SPAC1782.05","SPAC1783.07c","SPAC4C5.02c","SPBC4F6.06","SPBC146.13c","SPCC613.01","SPAC26F1.10c","SPAC23G3.02c","SPAC664.02c","SPCC188.02","SPAC824.02","SPBC24C6.05","SPBC12D12.07c","SPAC4G8.13c","SPAC4F8.01","SPAC3G9.04","SPAC4A8.06c","SPBC336.15","SPBC887.10","SPBC106.10","SPAC26F1.04c","SPBC21B10.03c","SPBC609.04","SPBC4B4.06","SPCC31H12.08c"],"gene_count":85,"ltp_gene_count":6,"approved_date":"2013-12-19"},{"uniquename":"PMID:19720063","title":"The Med8 mediator subunit interacts with the Rpb4 subunit of RNA polymerase II and Ace2 transcriptional activator in Schizosaccharomyces pombe.","citation":"FEBS Lett 2009 Oct 06;583(19):3115-20","abstract":"Several proteins are involved in separation of cells following division. However, their mutual interactions leading to cell separation is complex and not well understood. To explore the protein network that regulates this process at the transcriptional level in Schizosaccharomyces pombe, we have investigated the role of three proteins Med8, Rpb4 and Ace2. Using genetic and biochemical approaches we demonstrate that Ace2 binds Med8, which in turn interacts with Rpb4. We have delineated regions of Med8 and Rpb4 involved in their binding. We show that Med8 carboxyl-terminal region is necessary for its interaction with Rpb4 and can partially complement the sep15-598 mutant. Our results suggest that Med8 mediator subunit is involved in transmitting regulatory information from Ace2 to RNA polymerase II via Rpb4.","doi":"10.1016/j.febslet.2009.08.036","authors":"Mehta S, Miklos I, Sipiczki M, Sengupta S, Sharma N","authors_abbrev":"Mehta S et al.","pubmed_publication_date":"06 Oct 2009","pubmed_entrez_date":"2009-09-02","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21.04","SPAC6G10.12c","SPBC337.14"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:499806","title":"Allelism of methionine-sensitive mutants of Schizosaccharomyces pombe to loci involved in adenine biosynthesis.","citation":"Genet Res 1979 Jun;33(3):261-8","abstract":"","authors":"Strauss A","authors_abbrev":"Strauss A","pubmed_publication_date":"Jun 1979","pubmed_entrez_date":"1979-06-01","publication_year":"1979","canto_session_key":"a75082ad0a8ac32d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-06-30 19:17:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-30 19:17:21","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13","SPBC14F5.09c","SPAC6F12.10c","SPCC569.08c","SPBC409.10","SPAC4D7.08c","SPBC2G2.08","SPBC405.01","SPCPB16A4.03c","SPAC144.03"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2016-06-30"},{"uniquename":"EMBL:AU012439","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33788833","title":"Analysis of the SNARE Stx8 recycling reveals that the retromer-sorting motif has undergone evolutionary divergence.","citation":"PLoS Genet 2021 Mar;17(3):e1009463","abstract":"Fsv1/Stx8 is a Schizosaccharomyces pombe protein similar to mammalian syntaxin 8. stx8Δ cells are sensitive to salts, and the prevacuolar endosome (PVE) is altered in stx8Δ cells. These defects depend on the SNARE domain, data that confirm the conserved function of syntaxin8 and Stx8 in vesicle fusion at the PVE. Stx8 localizes at the trans-Golgi network (TGN) and the prevacuolar endosome (PVE), and its recycling depends on the retromer component Vps35, and on the sorting nexins Vps5, Vps17, and Snx3. Several experimental approaches demonstrate that Stx8 is a cargo of the Snx3-retromer. Using extensive truncation and alanine scanning mutagenesis, we identified the Stx8 sorting signal. This signal is an IEMeaM sequence that is located in an unstructured protein region, must be distant from the transmembrane (TM) helix, and where the 133I, 134E, 135M, and 138M residues are all essential for recycling. This sorting motif is different from those described for most retromer cargoes, which include aromatic residues, and resembles the sorting motif of mammalian polycystin-2 (PC2). Comparison of Stx8 and PC2 motifs leads to an IEMxx(I/M) consensus. Computer-assisted screening for this and for a loose Ψ(E/D)ΨXXΨ motif (where Ψ is a hydrophobic residue with large aliphatic chain) shows that syntaxin 8 and PC2 homologues from other organisms bear variation of this motif. The phylogeny of the Stx8 sorting motifs from the Schizosaccharomyces species shows that their divergence is similar to that of the genus, showing that they have undergone evolutionary divergence. A preliminary analysis of the motifs in syntaxin 8 and PC2 sequences from various organisms suggests that they might have also undergone evolutionary divergence, what suggests that the presence of almost-identical motifs in Stx8 and PC2 might be a case of convergent evolution.","doi":"10.1371/journal.pgen.1009463","authors":"Yanguas F, Valdivieso MH","authors_abbrev":"Yanguas F et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2021-03-31","publication_year":"2021","canto_session_key":"685768d63e59f072","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Henar Valdivieso","canto_first_approved_date":"2021-04-20 12:22:28","canto_approved_date":"2022-09-08 08:36:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-20 10:12:14","canto_added_date":"2021-04-02 00:15:08","annotation_curators":[{"name":"Henar Valdivieso","community_curator":true,"annotation_count":29,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":59,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19A8.05c","SPBC887.06c","SPBC31E1.04","SPBC13G1.11","SPAC6F12.03c","SPAC1006.01","SPCC594.06c","SPAC30.01c","SPAC24C9.08","SPAPJ696.01c","SPCC777.13","SPBC651.11c","SPBC3B9.10","SPAC6F6.12","SPCPJ732.01","SPBC16C6.06","SPAC4A8.04"],"gene_count":17,"ltp_gene_count":13,"approved_date":"2021-04-20"},{"uniquename":"PMID:26900649","title":"The hairpin region of Ndc80 is important for the kinetochore recruitment of Mph1/MPS1 in fission yeast.","citation":"Cell Cycle 2016;15(5):740-7","abstract":"The establishment of proper kinetochore-microtubule attachments facilitates faithful chromosome segregation. Incorrect attachments activate the spindle assembly checkpoint (SAC), which blocks anaphase onset via recruitment of a cohort of SAC components (Mph1/MPS1, Mad1, Mad2, Mad3/BubR1, Bub1 and Bub3) to kinetochores. KNL1, a component of the outer kinetochore KMN network (KNL1/Mis12 complex/Ndc80 complex), acts as a platform for Bub1 and Bub3 localization upon its phosphorylation by Mph1/MPS1. The Ndc80 protein, a major microtubule-binding site, is critical for MPS1 localization to the kinetochores in mammalian cells. Here we characterized the newly isolated mutant ndc80-AK01 in fission yeast, which contains a single point mutation within the hairpin region. This hairpin connects the preceding calponin-homology domain with the coiled-coil region. ndc80-AK01 was hypersensitive to microtubule depolymerizing reagents with no apparent growth defects without drugs. Subsequent analyses indicated that ndc80-AK01 is defective in SAC signaling, as mutant cells proceeded into lethal cell division in the absence of microtubules. Under mitotic arrest conditions, all SAC components (Ark1/Aurora B, Mph1, Bub1, Bub3, Mad3, Mad2 and Mad1) did not localize to the kinetochore. Further genetic analyses indicated that the Ndc80 hairpin region might act as a platform for the kinetochore recruitment of Mph1, which is one of the most upstream SAC components in the hierarchy. Intriguingly, artificial tethering of Mph1 to the kinetochore fully restored checkpoint signaling in ndc80-AK01 cells, further substantiating the notion that Ndc80 is a kinetochore platform for Mph1. The hairpin region of Ndc80, therefore, plays a critical role in kinetochore recruitment of Mph1.","doi":"10.1080/15384101.2016.1148842","authors":"Chmielewska AE, Tang NH, Toda T","authors_abbrev":"Chmielewska AE et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-02-23","publication_year":"2016","canto_session_key":"dd06290a49093559","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-02-01 17:39:28","canto_approved_date":"2022-09-25 06:39:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-28 22:31:39","canto_added_date":"2016-02-25 01:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPBC11C11.03","SPCC188.04c","SPBC409.04c","SPAC23H3.08c","SPBC3D6.04c","SPAC25G10.07c","SPCC320.13c","SPBC20F10.06","SPCC1322.12c","SPCC1795.01c","SPBC106.01","SPAC27F1.04c"],"gene_count":13,"ltp_gene_count":3,"approved_date":"2019-02-01"},{"uniquename":"PMID:9729469","title":"Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants.","citation":"Biochem J 1998 Sep 15;334 ( Pt 3)(Pt 3):609-16","abstract":"Glycosylphosphatidylinositol (GPI) represents an important anchoring molecule for cell surface proteins. The first step in its synthesis is the transfer of N-acetylglucosamine (GlcNAc) from UDP to phosphatidylinositol (PI). The products of three mammalian genes, PIG-A, PIG-C and PIG-H, have previously been shown to be involved in the putative enzymic complex. Here we report the cloning of human and mouse cDNAs encoding a fourth participant in the GlcNAc transfer reaction which are homologues of the Saccharomyces cerevisiae and Schizosaccharomyces pombe Gpi1 proteins. To provide evidence for their function, these proteins were expressed in GPI1-disrupted yeast strains. In Sacch. cerevisiae, where GPI1 disruption results in a temperature-sensitive phenotype and abolishes in vitro GlcNAc-PI synthesis, restoration of growth could be demonstrated in a temperature-dependent manner. In addition, in vitro GlcNAc-PI synthetic activity was again detectable. In Schiz. pombe, gpi1+ disruption is lethal. Using random spore analysis, we were able to show that the mammalian GPI1 homologues can rescue haploids harbouring the lethal gpi1+::his7+ allele. Our data demonstrate that the genes identified are indeed involved in the first step of GPI biosynthesis, and allow conclusions about a specific function for Gpi1p in stabilizing the enzymic complex. The finding that, despite a low degree of identity, the mammalian Gpi1 proteins are able to participate in the yeast GlcNAc-PI synthetic machinery as heterologous components further demonstrates that GPI biosynthesis has been highly conserved throughout evolution.","authors":"Tiede A, Schubert J, Nischan C, Jensen I, Westfall B, Taron CH, Orlean P, Schmidt RE","authors_abbrev":"Tiede A et al.","pubmed_publication_date":"15 Sep 1998","pubmed_entrez_date":"1998-09-08","publication_year":"1998","canto_session_key":"0e6b37edeafca702","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 17:03:32","canto_session_submitted_date":"2012-03-03 17:03:17","canto_added_date":"2012-02-24 05:53:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC30D10.11"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:23916750","title":"Iron uptake and regulation in Schizosaccharomyces pombe.","citation":"Curr Opin Microbiol 2013 Dec;16(6):669-76","abstract":"Schizosaccharomyces pombe is a useful model system for understanding many aspects of eukaryotic cell growth. Studies of S. pombe have identified novel genes that function in the regulation of iron homeostasis. In response to high levels of iron, Fep1 represses the expression of several genes involved in the acquisition of iron. When iron levels are limited, optimization of cellular iron utilization is coordinated by Php4, which represses genes encoding iron-using proteins. Results from studies in yeast have shed new light on the role of monothiol glutaredoxins (Grxs) in iron homeostasis. In S. pombe, the Grx4 protein serves as an inhibitory partner for Fep1 in response to iron deficiency, whereas it is required for the inhibition of Php4 under iron-replete conditions.","doi":"10.1016/j.mib.2013.07.007","authors":"Labbé S, Khan MG, Jacques JF","authors_abbrev":"Labbé S et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-08-07","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16083045","title":"[Chemical genomics by post-genomic approaches using Schizosaccharomyces pombe].","citation":"Tanpakushitsu Kakusan Koso 2005 Aug;50(9):1070-7","abstract":"","authors":"Nishimura S, Matsuyama A, Yoshida M","authors_abbrev":"Nishimura S et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-08-09","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1989884","title":"S. pombe pac1+, whose overexpression inhibits sexual development, encodes a ribonuclease III-like RNase.","citation":"EMBO J 1991 Jan;10(1):221-6","abstract":"The Schizosaccharomyces pombe pac1 gene is a multicopy suppressor of the pat1 temperature-sensitive mutation, which directs uncontrolled meiosis at the restrictive temperature. Overexpression of the pac1 gene had no apparent effect on vegetative growth but inhibited mating and sporulation in wild type S. pombe cells. In such cells, expression of certain genes required for mating or meiosis was inhibited. The pac1 gene is essential for vegetative cell growth. The deduced pac1 gene product has 363 amino acids. Its C-terminal 230 residues revealed 25% amino acid identity with ribonuclease III, an enzyme that digests double-stranded RNA and is involved in processing ribosomal RNA precursors and certain mRNAs in Escherichia coli. The pac1 gene product could degrade double-stranded RNA in vitro. These observations establish the presence of a RNase III homolog in eukaryotic cells. The pac1 gene product probably inhibits mating and meiosis by degrading a specific mRNA(s) required for sexual development. It is likely that mRNA processing is involved in the regulation of sexual development in fission yeast.","authors":"Iino Y, Sugimoto A, Yamamoto M","authors_abbrev":"Iino Y et al.","pubmed_publication_date":"Jan 1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_session_key":"864b5a9a8777fb8f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-07 12:20:49","canto_approved_date":"2021-04-16 13:24:23","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-22 17:16:49","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.11c","SPBC19C2.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-02-07"},{"uniquename":"EMBL:AB084830","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.928"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:41840227","title":"A gradient green-beard gene in fission yeast.","citation":"EMBO Rep 2026 Apr;27(8):1904-1917","abstract":"The social behaviors of microbes provide unique opportunities for testing social evolution theories. How can altruistic behaviors arise by natural selection is a central challenge in biology. Green-beard effect has been proposed as a basic mechanism for the evolution of altruistic behaviors. Yet, green-beard genes are generally thought to be rare. Here, we find that the Schizosaccharomyces pombe gsf2 gene mediates flocculation-like aggregation, and flocculation is triggered by acid stresses. gsf2-expressing cells preferentially adhere to each other. The expression of gsf2 is costly, but gsf2-expressing cells preferentially adhere to each other and protect each other from external stress. Gsf2 is highly variable in natural populations, likely contributing to different flocculation intensity. These findings suggest that gsf2 is a gradient green-beard gene that drives the altruism among gsf2 carriers. Moreover, we find that gsf2 is a new gene that originated very recently. Our results provide insights into the origin and evolution of green-beard genes.","doi":"10.1038/s44319-026-00748-x","authors":"Wu Z, Han GZ","authors_abbrev":"Wu Z et al.","pubmed_publication_date":"Apr 2026","pubmed_entrez_date":"2026-03-17","publication_year":"2026","canto_session_key":"56c612f96b0ebafb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-18 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010312","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38194460","title":"Elf1 promotes Rad26's interaction with lesion-arrested Pol II for transcription-coupled repair.","citation":"Proc Natl Acad Sci U S A 2024 Jan 16;121(3):e2314245121","abstract":"Transcription-coupled nucleotide excision repair (TC-NER) is a highly conserved DNA repair pathway that removes bulky lesions in the transcribed genome. Cockayne syndrome B protein (CSB), or its yeast ortholog Rad26, has been known for decades to play important roles in the lesion-recognition steps of TC-NER. Another conserved protein ELOF1, or its yeast ortholog Elf1, was recently identified as a core transcription-coupled repair factor. How Rad26 distinguishes between RNA polymerase II (Pol II) stalled at a DNA lesion or other obstacles and what role Elf1 plays in this process remains unknown. Here, we present cryo-EM structures of Pol II-Rad26 complexes stalled at different obstacles that show that Rad26 uses a common mechanism to recognize a stalled Pol II, with additional interactions when Pol II is arrested at a lesion. A cryo-EM structure of lesion-arrested Pol II-Rad26 bound to Elf1 revealed that Elf1 induces further interactions between Rad26 and a lesion-arrested Pol II. Biochemical and genetic data support the importance of the interplay between Elf1 and Rad26 in TC-NER initiation. Together, our results provide important mechanistic insights into how two conserved transcription-coupled repair factors, Rad26/CSB and Elf1/ELOF1, work together at the initial lesion recognition steps of transcription-coupled repair.","doi":"10.1073/pnas.2314245121","authors":"Sarsam RD, Xu J, Lahiri I, Gong W, Li Q, Oh J, Zhou Z, Hou P, Chong J, Hao N, Li S, Wang D, Leschziner AE","authors_abbrev":"Sarsam RD et al.","pubmed_publication_date":"16 Jan 2024","pubmed_entrez_date":"2024-01-09","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B3.02c","SPAC3C7.08c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:14585996","title":"Replication checkpoint protein Mrc1 is regulated by Rad3 and Tel1 in fission yeast.","citation":"Mol Cell Biol 2003 Nov;23(22):8395-403","abstract":"Fission yeast Mrc1 (mediator of replication checkpoint 1) is an adaptor checkpoint protein required for Rad3-dependent activation of the checkpoint kinase Cds1 in response to arrest of replication forks. Here we report studies on the regulation of Mrc1 by phosphorylation. Replication arrest induced by hydroxyurea (HU) induces Mrc1 phosphorylation that is detected by a change in Mrc1 electrophoretic mobility. Phosphorylation is maintained in cds1Delta, rad3Delta, and tel1Delta single mutants but eliminated in a rad3Delta tel1Delta double mutant. Mrc1 has two clusters of S/TQ motifs that are potential Rad3/Tel1 phosphorylation sites. Mutation of six S/TQ motifs in these two clusters strongly impairs Mrc1 phosphorylation. Two motifs located at S604 and T645 are vital for HU resistance. The T645A mutation strongly impairs a Cds1-Mrc1 yeast two-hybrid interaction that is dependent on a functional forkhead-associated (FHA) domain in Cds1, indicating that phosphorylation of T645 mediates Mrc1's association with Cds1. Consistent with this model, the T645 region of Mrc1 effectively substitutes for the T11 region of Cds1 that is thought to be phosphorylated by Rad3 and to mediate FHA-dependent oligomerization of Cds1. The S/TQ cluster that includes S604 is needed for Mrc1's increased association with chromatin in replication-arrested cells. These data indicate that Rad3 and Tel1 regulate Mrc1 through differential phosphorylation to control Cds1.","authors":"Zhao H, Tanaka K, Nogochi E, Nogochi C, Russell P","authors_abbrev":"Zhao H et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-10-31","publication_year":"2003","canto_session_key":"ed5a1aa8c1ecb938","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-03-21 16:53:30","canto_approved_date":"2021-10-19 15:00:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-03-21 16:53:25","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":44,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC694.06c","SPBC216.05","SPCC23B6.03c","SPCC1259.13","SPCC18B5.11c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-03-21"},{"uniquename":"PMID:9571240","title":"Fission yeast Ste9, a homolog of Hct1/Cdh1 and Fizzy-related, is a novel negative regulator of cell cycle progression during G1-phase.","citation":"Mol Biol Cell 1998 May;9(5):1065-80","abstract":"When proliferating fission yeast cells are exposed to nitrogen starvation, they initiate conjugation and differentiate into ascospores. Cell cycle arrest in the G1-phase is one of the prerequisites for cell differentiation, because conjugation occurs only in the pre-Start G1-phase. The role of ste9(+) in the cell cycle progression was investigated. Ste9 is a WD-repeat protein that is highly homologous to Hct1/Cdh1 and Fizzy-related. The ste9 mutants were sterile because they were defective in cell cycle arrest in the G1-phase upon starvation. Sterility was partially suppressed by the mutation in cig2 that encoded the major G1/S cyclin. Although cells lacking Ste9 function grow normally, the ste9 mutation was synthetically lethal with the wee1 mutation. In the double mutants of ste9 cdc10(ts), cells arrested in G1-phase at the restrictive temperature, but the level of mitotic cyclin (Cdc13) did not decrease. In these cells, abortive mitosis occurred from the pre-Start G1-phase. Overexpression of Ste9 decreased the Cdc13 protein level and the H1-histone kinase activity. In these cells, mitosis was inhibited and an extra round of DNA replication occurred. Ste9 regulates G1 progression possibly by controlling the amount of the mitotic cyclin in the G1-phase.","authors":"Kitamura K, Maekawa H, Shimoda C","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"May 1998","pubmed_entrez_date":"1998-05-22","publication_year":"1998","canto_session_key":"7dda0b52c4bd8bfa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-03-05 19:31:22","canto_approved_date":"2026-01-31 19:37:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-03-05 19:31:16","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC582.03","SPAC144.13c","SPBC660.14","SPBC11B10.09","SPBC32F12.09","SPAPB2B4.03","SPCC18B5.03"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2019-03-05"},{"uniquename":"EMBL:AB036343","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34473702","title":"Chromosomal Mcm2-7 distribution and the genome replication program in species from yeast to humans.","citation":"PLoS Genet 2021 Sep;17(9):e1009714","abstract":"The spatio-temporal program of genome replication across eukaryotes is thought to be driven both by the uneven loading of pre-replication complexes (pre-RCs) across the genome at the onset of S-phase, and by differences in the timing of activation of these complexes during S phase. To determine the degree to which distribution of pre-RC loading alone could account for chromosomal replication patterns, we mapped the binding sites of the Mcm2-7 helicase complex (MCM) in budding yeast, fission yeast, mouse and humans. We observed similar individual MCM double-hexamer (DH) footprints across the species, but notable differences in their distribution: Footprints in budding yeast were more sharply focused compared to the other three organisms, consistent with the relative sequence specificity of replication origins in S. cerevisiae. Nonetheless, with some clear exceptions, most notably the inactive X-chromosome, much of the fluctuation in replication timing along the chromosomes in all four organisms reflected uneven chromosomal distribution of pre-replication complexes.","doi":"10.1371/journal.pgen.1009714","authors":"Foss EJ, Sripathy S, Gatbonton-Schwager T, Kwak H, Thiesen AH, Lao U, Bedalov A","authors_abbrev":"Foss EJ et al.","pubmed_publication_date":"Sep 2021","pubmed_entrez_date":"2021-09-02","publication_year":"2021","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2021-09-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10373582","title":"The role of Schizosaccharomyces pombe Rad32, the Mre11 homologue, and other DNA damage response proteins in non-homologous end joining and telomere length maintenance.","citation":"Nucleic Acids Res 1999 Jul 01;27(13):2655-61","abstract":"The Schizosaccharomyces pombe homologue of Mre11, Rad32, is required for repair of UV- and ionising radiation-induced DNA damage and meiotic recombination. In this study we have investigated the role of Rad32 and other DNA damage response proteins in non-homologous end joining (NHEJ) and telomere length maintenance in S.pombe. We show that NHEJ in S.pombe occurs by an error-prone mechanism, in contrast to the accurate repair observed in Saccharomyces cerevisiae. Deletion of the rad32 gene results in a modest reduction in NHEJ activity and the remaining repair events that occur are accurate. Mutations in two of the phosphoesterase motifs in Rad32 have no effect on the efficiency or accuracy of end joining, suggesting that the role of Rad32 protein may be to recruit another nuclease(s) for processing during the end joining reaction. We also analysed NHEJ in other DNA damage response mutants and showed that the checkpoint mutant rad3-d and two recombination mutants defective in rhp51 and rhp54 (homologues of S.cerevisiae RAD51 and RAD54, respectively) are not affected. However disruption of rad22, rqh1 and rhp9 / crb2 (homologues of the S.cerevisiae RAD52, SGS1 and RAD9 genes) resulted in increased NHEJ activity. Telomere lengths in the rad32, rhp9 and rqh1 null alleles were reduced to varying extents intermediate between the lengths observed in wild-type and rad3 null cells.","authors":"Wilson S, Warr N, Taylor DL, Watts FZ","authors_abbrev":"Wilson S et al.","pubmed_publication_date":"01 Jul 1999","pubmed_entrez_date":"1999-06-22","publication_year":"1999","canto_session_key":"0ffa8093b9b4d8e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-13 15:44:10","canto_approved_date":"2024-04-08 16:57:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-15 11:56:43","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPAC2G11.12","SPBC216.05","SPAC644.14c","SPAC13C5.07","SPAC15A10.03c","SPBC342.05"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-04-13"},{"uniquename":"PMID:30668560","title":"Asymmetric diversification of mating pheromones in fission yeast.","citation":"PLoS Biol 2019 Jan;17(1):e3000101","abstract":"In fungi, mating between partners depends on the molecular recognition of two peptidyl mating pheromones by their respective receptors. The fission yeast Schizosaccharomyces pombe (Sp) has two mating types, Plus (P) and Minus (M). The mating pheromones P-factor and M-factor, secreted by P and M cells, are recognized by the receptors mating type auxiliary minus 2 (Mam2) and mating type auxiliary plus 3 (Map3), respectively. Our recent study demonstrated that a few mutations in both M-factor and Map3 can trigger reproductive isolation in S. pombe. Here, we explored the mechanism underlying reproductive isolation through genetic changes of pheromones/receptors in nature. We investigated the diversity of genes encoding the pheromones and their receptor in 150 wild S. pombe strains. Whereas the amino acid sequences of M-factor and Map3 were completely conserved, those of P-factor and Mam2 were very diverse. In addition, the P-factor gene contained varying numbers of tandem repeats of P-factor (4-8 repeats). By exploring the recognition specificity of pheromones between S. pombe and its close relative Schizosaccharomyces octosporus (So), we found that So-M-factor did not have an effect on S. pombe P cells, but So-P-factor had a partial effect on S. pombe M cells. Thus, recognition of M-factor seems to be stringent, whereas that of P-factor is relatively relaxed. We speculate that asymmetric diversification of the two pheromones might be facilitated by the distinctly different specificities of the two receptors. Our findings suggest that M-factor communication plays an important role in defining the species, whereas P-factor communication is able to undergo a certain degree of flexible adaptation-perhaps as a first step toward prezygotic isolation in S. pombe.","doi":"10.1371/journal.pbio.3000101","authors":"Seike T, Shimoda C, Niki H","authors_abbrev":"Seike T et al.","pubmed_publication_date":"Jan 2019","pubmed_entrez_date":"2019-01-23","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-01-24 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18082611","title":"Structural organization of the anaphase-promoting complex bound to the mitotic activator Slp1.","citation":"Mol Cell 2007 Dec 14;28(5):871-85","abstract":"The anaphase-promoting complex/cyclosome (APC/C) is a conserved multisubunit E3 ubiquitin (Ub) ligase required to signal the degradation of key cell-cycle regulators. Using single particle cryo-electron microscopy (cryo-EM), we have determined a three-dimensional (3D) structure of the core APC/C from Schizosaccharomyces pombe bound to the APC/C activator Slp1/Cdc20. At the 27 A resolution of our density map, the APC/C is a triangular-shaped structure, approximately 19x17x15 nm in size, with a deep internal cavity and a prominent horn-like protrusion emanating from a lip of the cavity. Using antibody labeling and mutant analysis, we have localized 12 of 13 core APC/C components, as well as the position of the activator Slp1, enabling us to propose a structural model of APC/C organization. Comparison of the APC/C with another multiprotein E3 ligase, the SCF complex, uncovers remarkable structural similarities.","authors":"Ohi MD, Feoktistova A, Ren L, Yip C, Cheng Y, Chen JS, Yoon HJ, Wall JS, Huang Z, Penczek PA, Gould KL, Walz T","authors_abbrev":"Ohi MD et al.","pubmed_publication_date":"14 Dec 2007","pubmed_entrez_date":"2007-12-18","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1795.01c","SPAC959.09c","SPBC83.04","SPAC19G12.01c","SPBP23A10.04","SPAC27D7.05c","SPBC106.09","SPBC28E12.01c","SPAC343.03","SPAC23C11.12","SPAC6F12.14","SPBC11C11.04c","SPBC1A4.01","SPBC20F10.06","SPAC17C9.01c","SPAC6F12.15c"],"gene_count":16,"ltp_gene_count":16},{"uniquename":"PMID:26305038","title":"New cassettes for single-step drug resistance and prototrophic marker switching in fission yeast.","citation":"Yeast 2015 Dec;32(12):703-10","abstract":"Construction of multiply mutated strains for genetic interaction analysis and of strains carrying different epitope tags at multiple open reading frames for testing protein localization, abundance and protein-protein interactions is hampered by the availability of a sufficient number of different selectable markers. Moreover, strains with single gene deletions or tags often already exist in strain collections; for historical reasons these will mostly carry the ura4(+) gene or the G418-resistance kanMX as marker. Because it is rather cumbersome to produce multiply deleted or tagged strains using the same marker, or to completely reconstruct a particular strain with a different marker, single-step exchange protocols of markers are a time-saving alternative. In recent years, dominant drug resistance markers (DDRMs) against clonNAT, hygromycin B and bleomycin have been adapted and successfully used in Schizosaccharomyces pombe. The corresponding DDRM cassettes, natMX, hphMX and bleMX, carry the TEF promotor and terminator sequences from Ashbya gossypii as kanMX; this provides flanking homologies to enable single-step marker swapping by homologous gene targeting. To expand this very useful toolset for single-step marker exchange, I constructed MX cassettes containing the nutritional markers arg3(+), his3(+), leu1(+) and ura4(+). Furthermore, a set of constructs was created to enable single-step exchange of ura4(+) to kanMX6, natMX4 and hphMX4. The functionality of the cassettes is demonstrated by successful single-step marker swapping at several loci. These constructs allow straightforward and rapid remarking of existing ura4(+) - and MX-deleted and -tagged strains.","doi":"10.1002/yea.3097","authors":"Lorenz A","authors_abbrev":"Lorenz A","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-08-26","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-08-27 00:18:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39786922","title":"The fission yeast SUMO-targeted ubiquitin ligase Slx8 functionally associates with clustered centromeres and the silent mating-type region at the nuclear periphery.","citation":"Biol Open 2024 Dec 15;13(12)","abstract":"The SUMO-targeted ubiquitin ligase (STUbL) family is involved in multiple cellular processes via a wide range of mechanisms to maintain genome stability. One of the evolutionarily conserved functions of STUbL is to promote changes in the nuclear positioning of DNA lesions, targeting them to the nuclear periphery. In Schizossacharomyces pombe, the STUbL Slx8 is a regulator of SUMOylated proteins and promotes replication stress tolerance by counteracting the toxicity of SUMO conjugates. In order to study the dynamic dialectic between ubiquitinylation and SUMOylation in the nuclear space of the S. pombe genome, we analyzed Slx8 localization. Unexpectedly, we did not detect replication stress-induced Slx8 foci. However, we discovered that Slx8 forms a single nuclear focus, enriched at the nuclear periphery, which marks both clustered centromeres at the spindle pole body and the silent mating-type region. The formation of this single Slx8 focus requires the E3 SUMO ligase Pli1, poly-SUMOylation and the histone methyl transferase Clr4 that is responsible for the heterochromatin histone mark H3-K9 methylation. Finally, we established that Slx8 promotes centromere clustering and gene silencing at heterochromatin domains. Altogether, our data highlight evolutionarily conserved and functional relationships between STUbL and heterochromatin domains to promote gene silencing and nuclear organization.","doi":"10.1242/bio.061746","authors":"Chakraborty S, Strachan J, Schirmeisen K, Besse L, Mercier E, Fréon K, Zhang H, Zhao N, Bayne EH, Lambert SAE","authors_abbrev":"Chakraborty S et al.","pubmed_publication_date":"15 Dec 2024","pubmed_entrez_date":"2025-01-09","publication_year":"2024","canto_session_key":"609a96b3831b9b45","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Lambert","canto_first_approved_date":"2025-02-03 15:54:47","canto_approved_date":"2025-03-03 16:38:18","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-01-31 10:53:07","canto_added_date":"2025-01-10 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":10,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Sarah Lambert","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.11c","SPBC428.08c","SPBC365.06","SPAC1687.05","SPAC1687.20c","SPCC188.13c","SPBC2G2.14","SPBC1105.17","SPAC16A10.06c","SPBC244.01c"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2025-02-03"},{"uniquename":"PMID:14554191","title":"K+ fluxes in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2003 Oct;4(1):1-6","abstract":"All living cells accumulate high concentrations of K+ in order to keep themselves alive. To this end they have developed a great diversity of transporters. The internal level of K+ is the result of the net balance between the activities of the K+ influx and the K+ efflux transporters. Potassium fluxes have been extensively studied and characterized in Saccharomyces cerevisiae. However, this is not the case in the fission yeast and, in addition, the information available indicates that both yeasts present substantial and interesting differences. In this paper we have reviewed and summarized the information on K+ fluxes in Schizosaccharomyces pombe. We have included some unpublished results recently obtained in our laboratory and, in particular, we have highlighted the significant differences found between the well-known yeast S. cerevisiae and the fission yeast Sch. pombe.","authors":"Calero F, Ramos J","authors_abbrev":"Calero F et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2003-10-14","publication_year":"2003","canto_session_key":"f8e918c2c86e9c33","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-03-28 15:03:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-03-28 15:03:38","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A7.08"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2017-03-28"},{"uniquename":"PMID:26608234","title":"Loss of the Mediator subunit Med20 affects transcription of tRNA and other non-coding RNA genes in fission yeast.","citation":"Biochim Biophys Acta 2016 Feb;1859(2):339-47","abstract":"Mediator is a co-regulator of RNA polymerase II (Pol II), transducing signals from regulatory elements and transcription factors to the general transcription machinery at the promoter. We here demonstrate that Med20 influences ribosomal protein expression in fission yeast. In addition, loss of Med20 leads to an accumulation of aberrant, readthrough tRNA transcripts. These transcripts are polyadenylated and targeted for degradation by the exosome. Similarly, other non-coding RNA molecules, such as snRNA, snoRNA and rRNA, are also enriched in the polyadenylate preparations in the absence of Med20. We suggest that fission yeast Mediator takes part in a regulatory pathway that affects Pol III-dependent transcripts.","doi":"10.1016/j.bbagrm.2015.11.007","authors":"Carlsten JO, Zhu X, López MD, Samuelsson T, Gustafsson CM","authors_abbrev":"Carlsten JO et al.","pubmed_publication_date":"Feb 2016","pubmed_entrez_date":"2015-11-27","publication_year":"2016","canto_session_key":"32641fbc31abea07","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-11-28 01:19:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10436027","title":"Plo1 kinase recruitment to the spindle pole body and its role in cell division in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1999 Aug;10(8):2771-85","abstract":"Polo kinases execute multiple roles during cell division. The fission yeast polo related kinase Plo1 is required to assemble the mitotic spindle, the prophase actin ring that predicts the site for cytokinesis and for septation after the completion of mitosis (Ohkura et al., 1995; Bahler et al., 1998). We show that Plo1 associates with the mitotic but not interphase spindle pole body (SPB). SPB association of Plo1 is the earliest fission yeast mitotic event recorded to date. SPB association is strong from mitotic commitment to early anaphase B, after which the Plo1 signal becomes very weak and finally disappears upon spindle breakdown. SPB association of Plo1 requires mitosis-promoting factor (MPF) activity, whereas its disassociation requires the activity of the anaphase-promoting complex. The stf1.1 mutation bypasses the usual requirement for the MPF activator Cdc25 (Hudson et al., 1990). Significantly, Plo1 associates inappropriately with the interphase SPB of stf1.1 cells. These data are consistent with the emerging theme from many systems that polo kinases participate in the regulation of MPF to determine the timing of commitment to mitosis and may indicate that pole association is a key aspect of Plo1 function. Plo1 does not associate with the SPB when septation is inappropriately driven by deregulation of the Spg1 pathway and remains SPB associated if septation occurs in the presence of a spindle. Thus, neither Plo1 recruitment to nor its departure from the SPB are required for septation; however, overexpression of plo1+ activates the Spg1 pathway and causes transient Cdc7 recruitment to the SPB and multiple rounds of septation.","authors":"Mulvihill DP, Petersen J, Ohkura H, Glover DM, Hagan IM","authors_abbrev":"Mulvihill DP et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-08-06","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C11.16"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:30463883","title":"Suppressor Analysis Uncovers That MAPs and Microtubule Dynamics Balance with the Cut7/Kinesin-5 Motor for Mitotic Spindle Assembly in  Schizosaccharomyces pombe .","citation":"G3 (Bethesda) 2019 Jan 09;9(1):269-280","abstract":"The Kinesin-5 motor Cut7 in  Schizosaccharomyces pombe  plays essential roles in spindle pole separation, leading to the assembly of bipolar spindle. In many organisms, simultaneous inactivation of Kinesin-14s neutralizes Kinesin-5 deficiency. To uncover the molecular network that counteracts Kinesin-5, we have conducted a genetic screening for suppressors that rescue the  cut7-22  temperature sensitive mutation, and identified 10 loci. Next generation sequencing analysis reveals that causative mutations are mapped in genes encoding α-, β-tubulins and the microtubule plus-end tracking protein Mal3/EB1, in addition to the components of the Pkl1/Kinesin-14 complex. Moreover, the deletion of various genes required for microtubule nucleation/polymerization also suppresses the  cut7  mutant. Intriguingly, Klp2/Kinesin-14 levels on the spindles are significantly increased in  cut7  mutants, whereas these increases are negated by suppressors, which may explain the suppression by these mutations/deletions. Consistent with this notion, mild overproduction of Klp2 in these double mutant cells confers temperature sensitivity. Surprisingly, treatment with a microtubule-destabilizing drug not only suppresses  cut7  temperature sensitivity but also rescues the lethality resulting from the deletion of  cut7 , though a single  klp2  deletion  per se  cannot compensate for the loss of Cut7. We propose that microtubule assembly and/or dynamics antagonize Cut7 functions, and that the orchestration between these two factors is crucial for bipolar spindle assembly.","doi":"10.1534/g3.118.200896","authors":"Yukawa M, Yamada Y, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"09 Jan 2019","pubmed_entrez_date":"2018-11-23","publication_year":"2019","canto_session_key":"1e872f4e7dc98480","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masashi Yukawa","canto_first_approved_date":"2019-06-04 14:33:25","canto_approved_date":"2026-01-30 14:04:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-18 07:03:15","canto_added_date":"2018-11-24 01:15:04","annotation_curators":[{"name":"Masashi Yukawa","community_curator":true,"annotation_count":29,"orcid":"0000-0002-1723-890X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC895.07","SPAC3A11.14c","SPBC13E7.06","SPAC890.02c","SPAC664.10","SPCC4G3.19","SPBC26H8.07c","SPBC32H8.09","SPCC736.14","SPAC25G10.07c","SPAC18G6.15","SPBC800.05c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2019-06-04"},{"uniquename":"PMID:36468849","title":"Pheromone Response and Mating Behavior in Fission Yeast.","citation":"Microbiol Mol Biol Rev 2022 Dec 21;86(4):e0013022","abstract":"Most ascomycete fungi, including the fission yeast Schizosaccharomyces pombe, secrete two peptidyl mating pheromones: C-terminally modified and unmodified peptides. S. pombe has two mating types, plus and minus, which secrete two different pheromones, P-factor (unmodified) and M-factor (modified), respectively. These pheromones are specifically recognized by receptors on the cell surface of cells of opposite mating types, which trigger a pheromone response. Recognition between pheromones and their corresponding receptors is important for mate discrimination; therefore, genetic changes in pheromone or receptor genes affect mate recognition and cause reproductive isolation that limits gene flow between populations. Such genetic variation in recognition via the pheromone/receptor system may drive speciation. Our recent studies reported that two pheromone receptors in S. pombe might have different stringencies in pheromone recognition. In this review, we focus on the molecular mechanism of pheromone response and mating behavior, emphasizing pheromone diversification and its impact on reproductive isolation in S. pombe and closely related fission yeast species. We speculate that the \"asymmetric\" system might allow flexible adaptation to pheromone mutational changes while maintaining stringent recognition of mating partners. The loss of pheromone activity results in the extinction of an organism's lineage. Therefore, genetic changes in pheromones and their receptors may occur gradually and/or coincidently before speciation. Our findings suggest that the M-factor plays an important role in partner discrimination, whereas P-factor communication allows flexible adaptation to create variations in S. pombe. Our inferences provide new insights into the evolutionary mechanisms underlying pheromone diversification.","doi":"10.1128/mmbr.00130-22","authors":"Seike T, Niki H","authors_abbrev":"Seike T et al.","pubmed_publication_date":"21 Dec 2022","pubmed_entrez_date":"2022-12-05","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-12-06 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11102532","title":"Schizosaccharomyces pombe rho2p GTPase regulates cell wall alpha-glucan biosynthesis through the protein kinase pck2p.","citation":"Mol Biol Cell 2000 Dec;11(12):4393-401","abstract":"Schizosaccharomyces pombe rho1(+) and rho2(+) genes are involved in the control of cell morphogenesis, cell integrity, and polarization of the actin cytoskeleton. Although both GTPases interact with each of the two S. pombe protein kinase C homologues, Pck1p and Pck2p, their functions are distinct from each other. It is known that Rho1p regulates (1,3)beta-D-glucan synthesis both directly and through Pck2p. In this paper, we have investigated Rho2p signaling and show that pck2 delta and rho2 delta strains display similar defects with regard to cell wall integrity, indicating that they might be in the same signaling pathway. We also show that Rho2 GTPase regulates the synthesis of alpha-D-glucan, the other main structural polymer of the S. pombe cell wall, primarily through Pck2p. Although overexpression of rho2(+) in wild-type or pck1 delta cells is lethal and causes morphological alterations, actin depolarization, and an increase in alpha-D-glucan biosynthesis, all of these effects are suppressed in a pck2 delta strain. In addition, genetic interactions suggest that Rho2p and Pck2p are important for the regulation of Mok1p, the major (1-3)alpha-D-glucan synthase. Thus, a rho2 delta mutation, like pck2 delta, is synthetically lethal with mok1-664, and the mutant partially fails to localize Mok1p to the growing areas. Moreover, overexpression of mok1(+) in rho2 delta cells causes a lethal phenotype that is completely different from that of mok1(+) overexpression in wild-type cells, and the increase in alpha-glucan is considerably lower. Taken together, all of these results indicate the presence of a signaling pathway regulating alpha-glucan biosynthesis in which the Rho2p GTPase activates Pck2p, and this kinase in turn controls Mok1p.","authors":"Calonge TM, Nakano K, Arellano M, Arai R, Katayama S, Toda T, Mabuchi I, Perez P","authors_abbrev":"Calonge TM et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-12-05","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12D12.04c","SPAC16.01","SPAC17G8.14c","SPAC1F7.04"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PB_REF:0000004","title":"Allele Synonyms","abstract":"PomBase curators record synonyms for alleles encountered in the literature, personal communications, or other resources.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32825021","title":"Novel Links between TORC1 and Traditional Non-Coding RNA, tRNA.","citation":"Genes (Basel) 2020 Aug 19;11(9)","abstract":"Target of rapamycin (TOR) is a serine/threonine kinase that modulates cell growth and metabolism in response to environmental changes. Transfer RNA (tRNA) is an abundant and ubiquitous small non-coding RNA that is essential in the translation of mRNAs. Beyond its canonical role, it has been revealed that tRNAs have more diverse functions. TOR complex 1 (TORC1), which is one of the two TOR complexes, regulates tRNA synthesis by controlling RNA polymerase III. In addition to tRNA synthesis regulation, recent studies have revealed hidden connections between TORC1 and tRNA, which are both essential players in eukaryotic cellular activities. Here, we review the accumulating findings on the regulatory links between TORC1 and tRNA-particularly those links in the budding yeast  Saccharomyces cerevisiae  and the fission yeast  Schizosaccharomyces pombe .","doi":"10.3390/genes11090956","authors":"Otsubo Y, Kamada Y, Yamashita A","authors_abbrev":"Otsubo Y et al.","pubmed_publication_date":"19 Aug 2020","pubmed_entrez_date":"2020-08-23","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-08-24 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9090845","title":"Schizosaccharomyces pombe gene GHT1 is highly homologous to other prokaryotic, yeast and higher eukaryotic genes coding for monosaccharide transporters.","citation":"Folia Microbiol (Praha) 1996;41(1):109-14","abstract":"","authors":"Näschen T, Lichtenberg-Fraté HC, Ludwig S, Höfer M","authors_abbrev":"Näschen T et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"101c373cfac5b3ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-10-28 16:13:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-28 16:13:25","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC548.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-10-28"},{"uniquename":"PMID:16495343","title":"Comparative structural biology of the genome: nano-scale imaging of single nucleus from different kingdoms reveals the common physicochemical property of chromatin with a 40 nm structural unit.","citation":"J Electron Microsc (Tokyo) 2006 Jan;55(1):31-40","abstract":"Genome function is closely linked to the higher-order chromatin structures. To reveal a structural basis for the interphase chromatin organization, the 'on-substrate' lysis procedure was applied to nuclei isolated from human HeLa cells, chicken erythrocyte cells and yeast Schizosaccharomyces pombe, which possessed different intrinsic properties of the genomes such as histone composition and inter-nucleosomal distance. The isolated nuclei on a coverslip were successively treated with a detergent and a high-salt solution to extract the nuclear membrane and the nucleoplasm, and therefore, atomic force microscopy (AFM) visualized the structural changes in response to the lysis procedure. After the nucleoplasm was extracted, AFM clarified that chromatin fibers, approximately 40 nm in width, were partially released out of the nuclei and that the other chromatin still remaining in the nuclei was composed of granular structures with diameter of 80-100 nm. Thus, these results suggest that the approximately 40 nm fiber would be a stable structural unit and fold the 80-100 nm granules into a one-step higher unit. A common mechanism could be implied regardless of the intrinsic properties of the eukaryotic genomes.","authors":"Kobori T, Kodama M, Hizume K, Yoshimura SH, Ohtani T, Takeyasu K","authors_abbrev":"Kobori T et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2006-02-24","publication_year":"2006","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18387370","title":"Dolichol-phosphate mannose synthase: structure, function and regulation.","citation":"Biochim Biophys Acta 2008 Jun;1780(6):861-8","abstract":"Glycosylation is the major modification of proteins, and alters their structures, functions and localizations. Glycosylation of secretory and surface proteins takes place in the endoplasmic reticulum and Golgi apparatus in eukaryotic cells and is classified into four modification pathways, namely N- and O-linked glycosylations, glycosylphosphatidylinositol (GPI)-anchor and C-mannosylation. These modifications are accomplished by sequential addition of single monosaccharides (O-linked glycosylation and C-mannosylation) or en bloc transfer of lipid-linked oligosaccharides (N-linked glycosylation and GPI) onto the proteins. The glycosyltransferases involved in these glycosylations are categorized into two classes based on the type of sugar donor, namely nucleotide-sugars and dolichol-phosphate-sugars, in which the sugar moiety is mannose or glucose. The sugar transfer from dolichol-phosphate-sugars occurs exclusively on the luminal side of the endoplasmic reticulum and is utilized in all four glycosylation pathways. In this review, we focus on the biosynthesis of dolichol-phosphate-mannose, and particularly on the mammalian enzyme complex involved in the reaction.","doi":"10.1016/j.bbagen.2008.03.005","authors":"Maeda Y, Kinoshita T","authors_abbrev":"Maeda Y et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-05","publication_year":"2008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21B10.11","SPBC1677.02"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:42260140","title":"GPATCH11 ortholog Sap34 regulates pre-mRNA splicing by interacting with early spliceosomal complexes in Schizosaccharomyces pombe.","citation":"Sci Rep 2026 Jun 08;","abstract":"Pre-mRNA splicing is an essential step in gene expression regulation. It is mediated by the spliceosome, a large ribonucleoprotein complex that undergoes dynamic structural and compositional rearrangements during each splicing cycle. Although the mechanisms of splicing and the roles of main spliceosomal components are well defined, the identities and functions of transiently associated spliceosomal proteins remain incompletely understood. Here, we investigated the molecular function of the poorly characterized G-patch domain-containing protein SPAC6F6.19 (herein Sap34, for spliceosome-associated protein of 34 kDa) in Schizosaccharomyces pombe, an ortholog of human GPATCH11. Using affinity purification and a yeast two-hybrid assay, we analyzed its interactome and identified its interaction partners. In addition, long-read sequencing was employed to assess Sap34-dependent changes in splicing efficiency. We found that Sap34 forms a complex with components of the U2 small nuclear ribonucleoprotein (snRNP) and the U4/U6 × U5 tri-snRNP, which are required for early spliceosome assembly and activation. Furthermore, we defined the interaction specificity of Sap34 with splicing proteins, demonstrating the importance of its C-terminal region for binding to Sap61 and Ini1, and of its G-patch domain for interaction with ATP-dependent RNA helicase Prp43, suggesting that G-patch domain of Sap34 may contribute to the regulation of Prp43 activity in early spliceosomes. Notably, we showed that deletion of sap34 leads to a global reduction in splicing efficiency, predominantly associated with increased intron retention. Together, these findings identify Sap34 as a previously unrecognized and important G-patch domain-containing protein regulating the early steps of pre-mRNA splicing in fission yeast.","doi":"10.1038/s41598-026-57150-9","authors":"Cipakova I, Karika LO, Hronska L, Selicky T, Iaparov B, Karhanek M, Kohutova L, Barath P, Cipak L","authors_abbrev":"Cipakova I et al.","pubmed_publication_date":"08 Jun 2026","pubmed_entrez_date":"2026-06-08","publication_year":"2026","canto_session_key":"326f91ca730e948a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-09 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.19"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21091378","title":"Txl1 and Txc1 are co-factors of the 26S proteasome in fission yeast.","citation":"Antioxid Redox Signal 2011 May 01;14(9):1601-8","abstract":"The 26S proteasome is a large proteolytic particle present in the cytosol and nucleus of eukaryotic cells. Most intracellular proteins, including those affected by oxidative damage, are degraded by the proteasome. The human thioredoxin, Txnl1, is known to associate with the 26S proteasome and thereby equips proteasomes with redox capabilities. Here, we characterize the fission yeast orthologue of Txnl1, called Txl1. Txl1 associates with the 26S proteasome via its C-terminal domain. This domain is also found in the uncharacterized protein, Txc1, which was also found to interact with 26S proteasomes. A txl1 null mutant, but not a txc1 null, displayed a synthetic growth defect with cut8, encoding a protein that tethers the proteasome to the nuclear membrane. Txc1 is present throughout the cytoplasm and nucleus, whereas Txl1 co-localizes with 26S proteasomes in both wild-type cells and in cut8 mutants, indicating that Txl1 is tightly associated with 26S proteasomes, while Txc1 might be only transiently bound to the complex. Finally, we show that Txl1 is an active thioredoxin. Accordingly, Txl1 was able to reduce and mediate the degradation of an oxidized model proteasome substrate in vitro. Thus, Txl1 and Txc1 are proteasome co-factors connected with oxidative stress.","doi":"10.1089/ars.2010.3329","authors":"Andersen KM, Jensen C, Kriegenburg F, Lauridsen AM, Gordon C, Hartmann-Petersen R","authors_abbrev":"Andersen KM et al.","pubmed_publication_date":"01 May 2011","pubmed_entrez_date":"2010-11-25","publication_year":"2011","canto_session_key":"8a0da77ab1315722","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-11 13:15:26","canto_approved_date":"2026-01-25 04:54:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-28 14:19:37","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC7D4.07c","SPBP19A11.03c","SPBP35G2.02","SPBC16G5.01","SPAC17C9.13c","SPBC577.08c","SPAC31G5.13"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-08-11"},{"uniquename":"PMID:9651580","title":"The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks.","citation":"Mol Cell 1998 Jun;1(7):969-79","abstract":"MRE11 and RAD50 are known to be required for nonhomologous joining of DNA ends in vivo. We have investigated the enzymatic activities of the purified proteins and found that Mre11 by itself has 3' to 5' exonuclease activity that is increased when Mre11 is in a complex with Rad50. Mre11 also exhibits endonuclease activity, as shown by the asymmetric opening of DNA hairpin loops. In conjunction with a DNA ligase, Mre11 promotes the joining of noncomplementary ends in vitro by utilizing short homologies near the ends of the DNA fragments. Sequence identities of 1-5 base pairs are present at all of these junctions, and their diversity is consistent with the products of nonhomologous end-joining observed in vivo.","authors":"Paull TT, Gellert M","authors_abbrev":"Paull TT et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-07-04","publication_year":"1998","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13C5.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24177739","title":"Two tightly linked silent cassettes in the mating-type region of Schizosaccharomyces pombe.","citation":"Curr Genet 1984 Apr;8(3):199-203","abstract":"Genetic evidence is presented for the presence of two silent cassettes mat2-P and mat3- M, which both map to the right of the expressible site mat1 of the mating-type region in Schizosaccharomyces pombe. During a switch of mating type, the resident cassette at mat1 is replaced by a copy of opposite mating-type information from one of the silent loci. Usually the switch becomes effective in one of two daughter cells, thus allowing for efficient sister-cell conjugation. In swi mutants, mating-type switching can be observed as early as for the first division after spore germination, albeit at a lower frequency. Genetically the two silent cassettes are linked so tightly that no crossovers were observed between mat2 and mat3 at a resolution of 10(-3) cM.","doi":"10.1007/BF00417816","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"Apr 1984","pubmed_entrez_date":"2013-11-02","publication_year":"1984","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33536395","title":"The fission yeast gmn2 +  gene encodes an ERD1 homologue of Saccharomyces cerevisiae required for protein glycosylation and retention of luminal endoplasmic reticulum proteins.","citation":"J Gen Appl Microbiol 2021 Jun 03;67(2):67-76","abstract":"The gmn2 mutant of Schizosaccharomyces pombe has previously been shown to exhibit defects in protein glycosylation of N-linked oligosaccharides (Ballou, L. and Ballou, CE., Proc. Natl. Acad. Sci. USA, 92, 2790-2794 (1995)). Like most glycosylation-defective mutants, the S. pombe gmn2 mutant was found to be sensitive to hygromycin B, an aminoglycoside antibiotic. As a result of complementation analysis, the gmn2 +  gene was found to be a single open reading frame that encodes a polypeptide of 373 amino acids consisting of multiple membrane-spanning regions. The Gmn2 protein shares sequence similarity with Kluyveromyces lactis and Saccharomyces cerevisiae Erd1 proteins, which are required for retention of luminal endoplasmic reticulum (ER) proteins. Although disruption of the gmn2 +  gene is not lethal, the secreted glycoprotein showed a significant glycosylation defect with destabilization of the glycosyltransferase responsible for N-glycan elongation. It was also shown that a significant amount of BiP was missorted to the cell surface according to ADEL receptor destabilization. Fluorescent microscopy revealed that the functional Gmn2-EGFP fusion protein is mainly localized in the Golgi membrane. These results indicate that the Gmn2 protein is required for protein glycosylation and for retention of ER-resident proteins in S. pombe cells.","doi":"10.2323/jgam.2020.07.002","authors":"Tanaka N, Kagami A, Hirai K, Suzuki S, Matsuura S, Fukunaga T, Tabuchi M, Takegawa K","authors_abbrev":"Tanaka N et al.","pubmed_publication_date":"03 Jun 2021","pubmed_entrez_date":"2021-02-04","publication_year":"2021","canto_session_key":"99dde499b1f33c52","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-06-15 09:25:38","canto_approved_date":"2023-06-19 14:18:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-09 00:29:08","canto_added_date":"2021-02-06 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP8B7.22","SPAC22A12.15c","SPAC1006.05c","SPCC191.11","SPAC227.01c"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2021-06-15"},{"uniquename":"PMID:24885407","title":"A formal concept analysis approach to consensus clustering of multi-experiment expression data.","citation":"BMC Bioinformatics 2014 May 19;15:151","abstract":"Presently, with the increasing number and complexity of available gene expression datasets, the combination of data from multiple microarray studies addressing a similar biological question is gaining importance. The analysis and integration of multiple datasets are expected to yield more reliable and robust results since they are based on a larger number of samples and the effects of the individual study-specific biases are diminished. This is supported by recent studies suggesting that important biological signals are often preserved or enhanced by multiple experiments. An approach to combining data from different experiments is the aggregation of their clusterings into a consensus or representative clustering solution which increases the confidence in the common features of all the datasets and reveals the important differences among them.\nWe propose a novel generic consensus clustering technique that applies Formal Concept Analysis (FCA) approach for the consolidation and analysis of clustering solutions derived from several microarray datasets. These datasets are initially divided into groups of related experiments with respect to a predefined criterion. Subsequently, a consensus clustering algorithm is applied to each group resulting in a clustering solution per group.These solutions are pooled together and further analysed by employing FCA which allows extracting valuable insights from the data and generating a gene partition over all the experiments. In order to validate the FCA-enhanced approach two consensus clustering algorithms are adapted to incorporate the FCA analysis. Their performance is evaluated on gene expression data from multi-experiment study examining the global cell-cycle control of fission yeast. The FCA results derived from both methods demonstrate that, although both algorithms optimize different clustering characteristics, FCA is able to overcome and diminish these differences and preserve some relevant biological signals.\nThe proposed FCA-enhanced consensus clustering technique is a general approach to the combination of clustering algorithms with FCA for deriving clustering solutions from multiple gene expression matrices. The experimental results presented herein demonstrate that it is a robust data integration technique able to produce good quality clustering solution that is representative for the whole set of expression matrices.","doi":"10.1186/1471-2105-15-151","authors":"Hristoskova A, Boeva V, Tsiporkova E","authors_abbrev":"Hristoskova A et al.","pubmed_publication_date":"19 May 2014","pubmed_entrez_date":"2014-06-03","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2698266","title":"Use of electron microscopy to characterize the surfaces of flocculent and nonflocculent yeast cells.","citation":"Can J Microbiol 1989 Dec;35(12):1081-6","abstract":"The surfaces of flocculent and nonflocculent yeast cells have been examined by electron microscopy. Nonextractive preparative procedures for scanning electron microscopy allow comparison in which sharp or softened images of surface details (scars, etc.) are the criteria for relative abundance of flocculum material. Asexually flocculent budding-yeast cells cannot be distinguished from nonflocculent budding-yeast cells in scanning electron micrographs because the scar details of both are well resolved, being hard and sharp. On the other hand, flocculent fission-yeast cells are readily distinguished from nonflocculent cells because fission scars are mostly soft or obscured on flocculent cells, but sharp on nonflocculent cells. Sexually and asexually flocculent fission-yeast cells cannot be distinguished from one another as both are heavily clad in \"mucilaginous\" or \"hairy\" coverings. Examination of lightly extracted and heavily extracted flocculent fission-yeast cells by transmission electron microscopy provides micrographs consistent with the scanning electron micrographs.","authors":"Johnson BF, Sowden LC, Walker T, Yoo BY, Calleja GB","authors_abbrev":"Johnson BF et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ010685","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10373577","title":"Srp2, an SR protein family member of fission yeast: in vivo characterization of its modular domains.","citation":"Nucleic Acids Res 1999 Jul 01;27(13):2618-26","abstract":"We isolated srp2, a gene encoding a protein composed of two RNA binding domains (RBDs) at the N-terminus followed by an arginine-rich region that is flanked by two short SR (serine/arginine) elements. The RBDs contain the signatures RDADDA and SWQDLKD found in RBD1 and RBD2 of all typical metazoan SR proteins. srp2 is essential for growth. We have analyzed in vivo the role of the modular domains of Srp2 by testing specific mutations in a conditional strain for complementation. We found that RBD2 is essential for function and determines the specificity of RBD1 in Srp2. Replacement of the first RBD with RBD1 of Srp1 of fission yeast does not change this specificity. The two SR elements in the C-terminus of Srp2 are also essential for function in vivo. Cellular distribution analysis with green fluorescence protein fused to portions of Srp2 revealed that the SR elements are necessary to target Srp2 to the nucleus. Furthermore, overexpression of modular domains of Srp2 and Srp1 show different effects on pre-mRNA splicing activity of the tfIId gene. Taken together, these findings are consistent with the notion that the RBDs of these proteins may be involved in pre-mRNA recognition.","authors":"Lützelberger M, Gross T, Käufer NF","authors_abbrev":"Lützelberger M et al.","pubmed_publication_date":"01 Jul 1999","pubmed_entrez_date":"1999-06-22","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11C11.08","SPAC16.02c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:32449465","title":"Synthesis of oligodeoxyribonucleotides containing a tricyclic thio analogue of  O  6 -methylguanine and their recognition by MGMT and Atl1.","citation":"Nucleosides Nucleotides Nucleic Acids 2020;39(8):1108-1121","abstract":"Promutagenic  O  6 -alkylguanine adducts in DNA are repaired in humans by  O  6 -methylguanine-DNA-methyltransferase (MGMT) in an irreversible reaction. Here we describe the synthesis of a phosphoramidite that allows the preparation of oligodeoxyribonucleotides (ODNs) containing a novel tricyclic thio analogue of  O  6 -methylguanine in which the third ring bridges the 6-thio group and C7 of a 7-deazapurine. These ODNs are very poor substrates for MGMT and poorly recognised by the alkyltransferase-like protein, Atl1. Examination of the active sites of both MGMT and Atl1 suggest large steric clashes hindering binding of the analogue. Such analogues, if mutagenic, are likely to be highly toxic.","doi":"10.1080/15257770.2020.1764971","authors":"Abdu K, Aiertza MK, Wilkinson OJ, Senthong P, Craggs TD, Povey AC, Margison GP, Williams DM","authors_abbrev":"Abdu K et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-05-26","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-01-13 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013116","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20444100","title":"Hyperosmosis enhances radiation and hydroxyurea resistance of Schizosaccharomyces pombe checkpoint mutants through the spindle checkpoint and delayed cytokinesis.","citation":"Mol Microbiol 2010 Jul 01;77(1):143-57","abstract":"The DNA damage and stress response pathways interact to regulate cellular responses to genotoxins and environmental stresses. How these pathways interact in Schizosaccharomyces pombe is not well understood. We demonstrate that osmotic stress suppresses the DNA damage sensitivity of checkpoint mutants, and that this occurs through three distinct cell cycle delays. A delay in G2/M is dependent on Srk1. Progression through mitosis is halted by the Mad2-dependent spindle checkpoint. Finally, cytokinesis is impaired by modulating Cdc25 expression. These three delays, imposed by osmotic stress, together compensate for the loss of checkpoint signalling.","doi":"10.1111/j.1365-2958.2010.07193.x","authors":"Alao JP, Huis In 't Veld PJ, Buhse F, Sunnerhagen P","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"01 Jul 2010","pubmed_entrez_date":"2010-05-07","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPAC23A1.06c","SPAC24B11.06c","SPBC11B10.09","SPAC24H6.05","SPAC1952.07","SPCC1322.08"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:10572255","title":"Molecular cloning and characterization of the gene HXK1 encoding the hexokinase from Yarrowia lipolytica.","citation":"Yeast 1999 Nov;15(15):1573-84","abstract":"We have cloned the gene HXK1 from the dimorphic yeast Yarrowia lipolytica that encodes the unique hexokinase of this yeast. The gene has an intron located 39 base pairs after the A of the first ATG. The putative protein contains a sequence of 40 amino acids which is absent from other known hexokinase sequences. Y. lipolytica strains devoid of hexokinase grew in glucose slower than wild-type. This growth was due to the existence of a glucokinase. The hexokinase from Y. lipolytica substituted effectively for hexokinase II from S. cerevisiae in catabolite repression of invertase. The hexokinases from Schizosaccharomyces pombe or Kluyveromyces lactis were much less effective in this role. The K(m) for glucose and fructose of hexokinase was 0.38 mM and 3.56 mM, respectively. The K(m) of glucokinase for glucose was 0.17 mM. While the hexokinase was strongly inhibited by trehalose-6-phosphate (K(i)=3.6 microM), glucokinase was not affected by this compound.","authors":"Petit T, Gancedo C","authors_abbrev":"Petit T et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-11-26","publication_year":"1999","canto_session_key":"7f9fcda6607c6064","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-30 23:51:46","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 23:51:39","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F8.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-30"},{"uniquename":"PMID:7548844","title":"DNA structure checkpoints in fission yeast.","citation":"Semin Cell Biol 1995 Apr;6(2):65-72","abstract":"A DNA structure checkpoint can be defined as any checkpoint which responds to changes in the structure of the DNA either through the cell cycle, or in response to outside events such as DNA damage. Genetic analysis of DNA structure checkpoints in fission yeast has identified several distinct pathways responding to different circumstances. Three checkpoints have been identified which inhibit the onset of mitosis. (1) A radiation checkpoint which prevents mitosis after DNA damage. (2) A checkpoint linking S phase and mitosis (the S-M checkpoint) that prevents mitosis when DNA synthesis is incomplete. (3) A checkpoint linking G1 to mitosis (the G1-M checkpoint) that prevents the onset of mitosis in cells which are arrested in the G1 period of the cycle. A large number of genetic loci that are required for these checkpoints have been identified through mutant analysis, and the involvement of the relevant genes with the individual checkpoint pathways has been investigated. The largest class of checkpoint genes, known as the 'checkpoint rad' genes, are required for all the DNA structure checkpoints and the evidence suggests that they may also be involved in regulating DNA synthesis following precursor deprivation (hydroxyurea treatment) or when the replication fork encounters DNA damage. In this review, the available genetic and physiological evidence has been interpreted to suggest a close association between the 'checkpoint rad' class of gene products and the DNA-protein complexes that regulate and perform DNA synthesis. Biochemical evidence will be required in order to prove or disprove this hypothesis.","authors":"Carr AM","authors_abbrev":"Carr AM","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1500441","title":"Vertebrate p34cdc2 phosphorylation site mutants: effects upon cell cycle progression in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1992 May;102 ( Pt 1):43-53","abstract":"We have used the fission yeast Schizosaccharomyces pombe to analyse the effects of in vitro mutagenesis of the four known phosphorylation sites in the chicken p34(cdc2) protein, Thr 14, Tyr 15, Thr 161 and Ser 277, upon cell cycle progression. We have studied both the effect of overexpression of mutant proteins in a cdc2+ background and assayed their ability to rescue null and temperature-sensitive alleles of cdc2. Mutations of Thr 14 and Tyr 15 within the ATP binding domain of p34(cdc2) that mimic constitutive phosphorylation cause dominant negative cell cycle arrest when overexpressed. In contrast, some substitutions that simulate permanent dephosphorylation of the corresponding sites advance dephosphorylation of the corresponding sites advance mitosis. These data confirm the model that p34(cdc2) function is negatively regulated by phosphorylation of residues in the ATP binding site. Mutagenesis of the conserved residue Thr 161 functionally inactivates p34(cdc2), and our data suggest that both phosphorylation and dephosphorylation events at Thr 161 are required for progression through the cell cycle. Mutations at the fourth site of phosphorylation. Ser 277, lead to cold-sensitive cell cycle arrest, in minimal but not rich growth medium, suggesting that this site is involved in monitoring the nutritional status of the cell.","authors":"Krek W, Marks J, Schmitz N, Nigg EA, Simanis V","authors_abbrev":"Krek W et al.","pubmed_publication_date":"May 1992","pubmed_entrez_date":"1992-05-01","publication_year":"1992","canto_session_key":"93d6e373bf272647","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-10 21:32:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-09 12:05:37","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-09-09"},{"uniquename":"PMID:21850271","title":"Genome-wide screening for genes associated with FK506 sensitivity in fission yeast.","citation":"PLoS One 2011;6(8):e23422","abstract":"We have been studying calcineurin signal transduction pathway in fission yeast Schizosaccharomyces pombe (S. pombe) by developing a genetic screen for mutants that show hypersensitivity to the immunosuppressive calcineurin inhibitor FK506 (tacrolimus). In the present study, to identify nonessential genes that are functionally related to the calcineurin signaling pathway, we performed a genome-wide screen of 3004 haploid deletion strains and confirmed 72 deletion strains to be FK506 sensitive. These 72 genes are classified into nine functional groups to include membrane trafficking (16 genes), signal transduction (10 genes), ubiquitination (8 genes), chromatin remodeling (6 genes), cytokinesis (4 genes), ribosomal protein (3 genes), RNA binding protein (3 genes), and a variety of other known functions (17 genes) or still unknown functions (5 genes) in the biological system. In our previous screening of FK506-sensitive mutants we isolated several membrane-trafficking mutants showing defective cell wall integrity. Here, we further examined the vacuolar fusion, the v-SNARE synaptobrevin Syb1 localization, and the sensitivity to the β-glucan synthase inhibitor micafungin in these 72 FK506-sensitive strains. Results showed that 25 deletion strains exhibited abnormal vacuole fusion, 19 deletion strains exhibited Syb1 mislocalization, and 14 deletion strains exhibited both abnormal vacuole fusion and Syb1 mislocalization, while 42 deletion strains showed both normal vacuole fusion and Syb1 localization. Likewise, 16 deletion strains showed sensitivity to micafungin. Altogether, our present study indicates that calcineurin mediates a plethora of physiological processes in fission yeast, and that calcineurin is extensively involved in cross-talk between signaling pathways.","doi":"10.1371/journal.pone.0023422","authors":"Ma Y, Jiang W, Liu Q, Ryuko S, Kuno T","authors_abbrev":"Ma Y et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-08-19","publication_year":"2011","canto_session_key":"edc7facc0f6fbc66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-24 13:11:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-24 13:10:54","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":131,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_21850271_phaf.tsv"}],"genes":["SPBC106.07c","SPAC11G7.06c","SPBC409.07c","SPAC17A5.14","SPAC3F10.05c","SPBC83.18c","SPCC613.03","SPBC1773.01","SPCC4B3.08","SPBC23G7.08c","SPCP1E11.06","SPBC146.13c","SPAC1782.09c","SPAC2C4.05","SPBC29A10.16c","SPBC16C6.02c","SPBC215.03c","SPAC3C7.06c","SPAC3F10.16c","SPAC959.08","SPBC365.14c","SPCC576.13","SPAC2G11.03c","SPAC30D11.13","SPAC1527.02","SPBP4G3.02","SPAC16E8.01","SPAC513.03","SPAC30D11.05","SPCC188.02","SPCC594.02c","SPCC74.09","SPBC29A3.05","SPAC19B12.10","SPAC15A10.08","SPBC31F10.10c","SPAC23H3.06","SPBC1709.09","SPBPB10D8.04c","SPBC21C3.02c","SPAC17A5.08","SPBC12C2.02c","SPAC23H3.03c","SPAPB17E12.04c","SPAC26H5.05","SPBC1685.01","SPAC4G8.10","SPAC1851.03","SPBC11B10.10c","SPAC8F11.02c","SPBC800.03","SPCP1E11.04c","SPAC31G5.18c","SPBC25H2.16c","SPAC6B12.07c","SPBC14C8.17c","SPBC14F5.13c","SPCC736.07c","SPAC16E8.05c","SPAC9G1.04","SPAC688.11","SPAC9G1.03c","SPAC22E12.11c","SPAPB1E7.02c","SPAC8E11.02c","SPBP16F5.07","SPAC17G8.05","SPBC3H7.09","SPCC757.09c","SPAC6G9.11","SPAC4C5.02c","SPCC550.14","SPBC16H5.06","SPBC530.01","SPBC19C7.02"],"gene_count":75,"ltp_gene_count":0,"approved_date":"2014-07-24"},{"uniquename":"PMID:21444718","title":"DNA repair and global sumoylation are regulated by distinct Ubc9 noncovalent complexes.","citation":"Mol Cell Biol 2011 Jun;31(11):2299-310","abstract":"Global sumoylation, SUMO chain formation, and genome stabilization are all outputs generated by a limited repertoire of enzymes. Mechanisms driving selectivity for each of these processes are largely uncharacterized. Here, through crystallographic analyses we show that the SUMO E2 Ubc9 forms a noncovalent complex with a SUMO-like domain of Rad60 (SLD2). Ubc9:SLD2 and Ubc9:SUMO noncovalent complexes are structurally analogous, suggesting that differential recruitment of Ubc9 by SUMO or Rad60 provides a novel means for such selectivity. Indeed, deconvoluting Ubc9 function by disrupting either the Ubc9:SLD2 or Ubc9:SUMO noncovalent complex reveals distinct roles in facilitating sumoylation. Ubc9:SLD2 acts in the Nse2 SUMO E3 ligase-dependent pathway for DNA repair, whereas Ubc9:SUMO instead promotes global sumoylation and chain formation, via the Pli1 E3 SUMO ligase. Moreover, this Pli1-dependent SUMO chain formation causes the genome instability phenotypes of SUMO-targeted ubiquitin ligase (STUbL) mutants. Overall, we determine that, unexpectedly, Ubc9 noncovalent partner choice dictates the role of sumoylation in distinct cellular pathways.","doi":"10.1128/MCB.05188-11","authors":"Prudden J, Perry JJ, Nie M, Vashisht AA, Arvai AS, Hitomi C, Guenther G, Wohlschlegel JA, Tainer JA, Boddy MN","authors_abbrev":"Prudden J et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-03-30","publication_year":"2011","canto_session_key":"684efd3d317a735a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-06-22 21:43:46","canto_approved_date":"2025-06-22 21:43:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-30 17:40:15","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":32,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.05c","SPAC1687.05","SPAC644.14c","SPAC17A5.07c","SPBC1921.02","SPBC1703.14c","SPBC3D6.11c","SPAC30D11.13","SPAC16A10.06c","SPBC365.06"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2025-06-22","pdb_entries":[{"pdb_id":"3rcz","gene_chains":[{"gene_uniquename":"SPAC30D11.13","chain":"B","position":"2-157"},{"gene_uniquename":"SPBC1921.02","chain":"A","position":"332-406"}],"title":"Rad60 SLD2 Ubc9 Complex","entry_authors":"Perry JJP,Arvai AS,Tainer JA","entry_authors_abbrev":"Perry JJP et al.","reference_uniquename":"PMID:21444718","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:35164835","title":"An updated view on the centrosome as a cell cycle regulator.","citation":"Cell Div 2022 Feb 14;17(1):1","abstract":"The centrosome is a multifunctional organelle that is known primarily for its microtubule organising function. Centrosomal defects caused by changes in centrosomal structure or number have been associated with human diseases ranging from congenital defects to cancer. We are only beginning to appreciate how the non-microtubule organising roles of the centrosome are related to these clinical conditions. In this review, we will discuss the historical evidence that led to the proposal that the centrosome participates in cell cycle regulation. We then summarize the body of work that describes the involvement of the mammalian centrosome in triggering cell cycle progression and checkpoint signalling. Then we will highlight work from the fission yeast model organism, revealing the molecular details that explain how the spindle pole body (SPB, the yeast functional equivalent of the centrosome), participates in these cell cycle transitions. Importantly, we will discuss some of the emerging questions from recent discoveries related to the role of the centrosome as a cell cycle regulator.","doi":"10.1186/s13008-022-00077-0","authors":"Lin M, Xie SS, Chan KY","authors_abbrev":"Lin M et al.","pubmed_publication_date":"14 Feb 2022","pubmed_entrez_date":"2022-02-15","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-02-17 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16887026","title":"Walker-Warburg syndrome.","citation":"Orphanet J Rare Dis 2006 Aug 03;1:29","abstract":"Walker-Warburg Syndrome (WWS) is a rare form of autosomal recessive congenital muscular dystrophy associated with brain and eye abnormalities. WWS has a worldwide distribution. The overall incidence is unknown but a survey in North-eastern Italy has reported an incidence rate of 1.2 per 100,000 live births. It is the most severe form of congenital muscular dystrophy with most children dying before the age of three years. WWS presents at birth with generalized hypotonia, muscle weakness, developmental delay with mental retardation and occasional seizures. It is associated with type II cobblestone lissencephaly, hydrocephalus, cerebellar malformations, eye abnormalities and congenital muscular dystrophy characterized by hypoglycosylation of alpha-dystroglycan. Several genes have been implicated in the etiology of WWS, and others are as yet unknown. Several mutations were found in the Protein O-Mannosyltransferase 1 and 2 (POMT1 and POMT2) genes, and one mutation was found in each of the fukutin and fukutin-related protein (FKRP) genes. Laboratory investigations usually show elevated creatine kinase, myopathic/dystrophic muscle pathology and altered alpha-dystroglycan. Antenatal diagnosis is possible in families with known mutations. Prenatal ultrasound may be helpful for diagnosis in families where the molecular defect is unknown. No specific treatment is available. Management is only supportive and preventive.","authors":"Vajsar J, Schachter H","authors_abbrev":"Vajsar J et al.","pubmed_publication_date":"03 Aug 2006","pubmed_entrez_date":"2006-08-05","publication_year":"2006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16C6.09","SPAC22A12.07c","SPAPB1E7.09"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:19531029","title":"Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms.","citation":"Biotechnol Appl Biochem 2009 Jun 22;53(Pt 4):217-26","abstract":"CoQ (coenzyme Q), an isoprenylated benzoquinone, is a well-known component of the electron-transfer system in eukaryotes. The main role of CoQ is to transfer electrons from NADH dehydrogenase and succinate dehydrogenase to CoQ:cytochrome c reductase in the respiratory chain. However, recent evidence indicates that an involvement in respiration is not the only role of CoQ. The second apparent role of CoQ is its anti-oxidation property, and other novel roles for CoQ, such as in disulfide-bond formation, sulfide oxidation and pyrimidine metabolism, have been reported. CoQ10, having ten isoprene units in the isoprenoid side chain, has been used as a medicine and is now commercially popular as a food supplement. Two yeast species, namely the budding yeast Saccharomyces cerevisiae, which produces CoQ6, and the fission yeast Schizosaccharomyces pombe, which produces CoQ10, are the main subjects of the present minireview because they have greatly contributed to our basic knowledge of CoQ biosynthesis among eukaryotes. The biosynthetic pathway that converts p-hydroxybenzoate into CoQ consists of eight steps in yeasts. The five enzymes involved in the biosynthetic pathway have been identified in both yeasts, yet the functions of three proteins were still not known. Analyses of the biosynthetic pathway in yeasts also contribute to the understanding of human genetic diseases related to CoQ deficiency. In the present minireview I focus on the biochemical and commercial aspects of CoQ in yeasts and in other organisms for comparison.","doi":"10.1042/BA20090035","authors":"Kawamukai M","authors_abbrev":"Kawamukai M","pubmed_publication_date":"22 Jun 2009","pubmed_entrez_date":"2009-06-18","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23209828","title":"Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1 transcription factor.","citation":"PLoS One 2012;7(11):e50796","abstract":"Here we report the result of a genetic screen for mutants resistant to the microtubule poison methyl benzimidazol-2-yl carbamate (MBC) that were also temperature sensitive for growth. In total the isolated mutants were distributed in ten complementation groups. Cloning experiments revealed that most of the mutants were in essential genes encoding various 26S proteasome subunits. We found that the proteasome mutants are multi-drug resistant due to stabilization of the stress-activated transcription factor Pap1. We show that the ubiquitylation and ultimately the degradation of Pap1 depend on the Rhp6/Ubc2 E2 ubiquitin conjugating enzyme and the Ubr1 E3 ubiquitin-protein ligase. Accordingly, mutants lacking Rhp6 or Ubr1 display drug-resistant phenotypes.","doi":"10.1371/journal.pone.0050796","authors":"Penney M, Samejima I, Wilkinson CR, McInerny CJ, Mathiassen SG, Wallace M, Toda T, Hartmann-Petersen R, Gordon C","authors_abbrev":"Penney M et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-12-05","publication_year":"2012","canto_session_key":"84dcea5bf4f580d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_first_approved_date":"2016-11-29 19:31:21","canto_approved_date":"2026-02-01 09:20:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-28 08:44:43","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":55,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.02","SPBC577.10","SPBC4C3.10c","SPBP19A11.03c","SPBC337.08c","SPAC3C7.14c","SPBC4.07c","SPAC18B11.07c","SPAC1783.07c","SPAC1805.17","SPBC106.16","SPAC607.05","SPAC23D3.07","SPAC31G5.13","SPBC16G5.01"],"gene_count":15,"ltp_gene_count":14,"approved_date":"2016-11-29"},{"uniquename":"EMBL:AJ632003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.38"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:6945472","title":"Synthesis of mitochondrial DNA during the cell cycle of the petite negative yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1981;182(2):252-4","abstract":"Synthesis of mitochondrial DNA (mitDNA) and nuclear DNA (nucDNA) during growth of synchronously dividing cultures of Schizosaccharomyces pombe (S. pombe) was followed by pulse labelling with radioactive adenine and determination of its rate of incorporation into total protoplast DNA and into the DNA of DNase-treated mitochondria at different stages of the cell cycle. It could be demonstrated that both mitDNA and nucDNA were synthesised discontinuously and at different points in the cell cycle.","authors":"Del Giudice L, Wolf K, Manna F, Pagliuca N","authors_abbrev":"Del Giudice L et al.","pubmed_publication_date":"1981","pubmed_entrez_date":"1981-01-01","publication_year":"1981","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31242058","title":"Actin assembly produces sufficient forces for endocytosis in yeast.","citation":"Mol Biol Cell 2019 Jul 22;30(16):2014-2024","abstract":"We formulated a spatially resolved model to estimate forces exerted by a polymerizing actin meshwork on an invagination of the plasma membrane during endocytosis in yeast cells. The model, which approximates the actin meshwork as a visco-active gel exerting forces on a rigid spherocylinder representing the endocytic invagination, is tightly constrained by experimental data. Simulations of the model produce forces that can overcome resistance of turgor pressure in yeast cells. Strong forces emerge due to the high density of polymerized actin in the vicinity of the invagination and because of entanglement of the meshwork due to its dendritic structure and cross-linking. The model predicts forces orthogonal to the invagination that are consistent with formation of a flask shape, which would diminish the net force due to turgor pressure. Simulations of the model with either two rings of nucleation-promoting factors (NPFs) as in fission yeast or a single ring of NPFs as in budding yeast produce enough force to elongate the invagination against the turgor pressure.","doi":"10.1091/mbc.E19-01-0059","authors":"Nickaeen M, Berro J, Pollard TD, Slepchenko BM","authors_abbrev":"Nickaeen M et al.","pubmed_publication_date":"22 Jul 2019","pubmed_entrez_date":"2019-06-27","publication_year":"2019","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2019-06-28 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28872942","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-09-08 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28302794","title":"DNA sequence-dependent epigenetic inheritance of gene silencing and histone H3K9 methylation.","citation":"Science 2017 Apr 07;356(6333):88-91","abstract":"Epigenetic inheritance mechanisms play fundamental roles in maintaining cellular memory of gene expression states. In fission yeast, histone H3 lysine 9 (H3K9) is methylated (H3K9me) at heterochromatic domains. These domains can be epigenetically inherited when  epe1 +   , encoding an enzyme that promotes H3K9 demethylation, is deleted. How native epigenetic states are stably maintained in  epe1 +   cells remains unknown. Here, we developed a system to examine the role of DNA sequence and genomic context in propagation of a cis-heritable H3K9me-dependent silenced state. We show that in  epe1 +   cells, in addition to sequence-independent mechanisms that propagate H3K9me, epigenetic inheritance of silencing requires binding sites for sequence-dependent activating transcription factor (ATF)-adenosine 3',5'-monophosphate (cAMP) response element-binding protein (CREB) family transcription factors within their native chromosomal context. Thus, specific DNA sequences contribute to cis inheritance of H3K9me and silent epigenetic states.","doi":"10.1126/science.aaj2114","authors":"Wang X, Moazed D","authors_abbrev":"Wang X et al.","pubmed_publication_date":"07 Apr 2017","pubmed_entrez_date":"2017-03-18","publication_year":"2017","canto_session_key":"271401e5b6db10aa","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-21 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9190794","title":"[The first member of a novel family of eukaryotic transcription factors detected by the heterospecific complementation].","citation":"Bioorg Khim 1997 Mar;23(3):234-7","abstract":"The cDNA of a previously uncharacterized gene fet5 (factor of eukaryotic transcription, clone no. 5) of the fission yeast Schizosaccharomyces pombe was cloned by the heterospecific complementation of a conditional mutant of Saccharomyces cerevisiae defective in the function of the RNA polymerases I-III common subunit ABC10 beta. The gene encodes a new factor of eukaryotic transcription, Fet5, the first member of a superfamily of proteins for which the area of functioning is determined. The Fet5-superfamily consists of three distinct families of proteins highly evolutionarily conserved and widely spread among eukaryotes. Features of the Fet5 amino acid sequence suggest that it belongs to ATP/GTP-binding proteins.","authors":"Shpakovskiĭ GV, Lebedenko EN","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_session_key":"49e2fabe10c86ddc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-06 08:02:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-05 21:41:52","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B3.12c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-05-05"},{"uniquename":"EMBL:AU007774","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8860233","title":"Forces acting on the fission yeast anaphase spindle.","citation":"Cell Motil Cytoskeleton 1996;34(1):69-75","abstract":"The fission yeast mitotic spindle consists of three sets of microtubules: one that extends between the chromosomes and the spindle pole bodies (SPBs); one that extends between the two SPBs forming a region of overlap; and a third, the so-called astral microtubules, that associates laterally with the cytoplasmic face of the SPBs, during anaphase B. The major bundles of the latter can exist with equal probability in two configurations which we have termed parallel and convergent. Mitosis in fission yeast is characterised by an extended anaphase B during which the spindle elongates from 2 mu m (the diameter of the interphase nucleus) to about 14 mu m, spanning the entire length of the cell. Anaphase B spindles viewed by indirect immunofluorescence microscopy frequently appeared bowed but only when the astral microtubules were in the convergent orientation. To investigate the possible significance of this observation, we have examined the situation in the abnormally long spindles that are formed in cells in which cell length has been extended either by overexpression of the weel + gene or by inactivation of the cdc25 + gene. The spindles in these strains were often considerably longer (up to 30 mu m) than in wild type cells but, unlike the latter, did not extend the entire length of the cell. Bowed spindles were again observed but only when the astral microtubules were convergent. We discuss these findings in the context of the astral microtubules either exerting a pulling force on the poles of the anaphase B spindle, or counteracting a pushing force generated by sliding of anti-parallel pole to pole microtubules of the mitotic spindle, or both of the above.","authors":"Hagan IM, Hyams JS","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"37651048e44cc918","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-02-05 15:08:44","canto_approved_date":"2019-02-05 15:09:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-05 15:09:18","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPCC18B5.03"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2019-02-05"},{"uniquename":"PMID:28533364","title":"Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.","citation":"Proc Natl Acad Sci U S A 2017 Jun 06;114(23):6034-6039","abstract":"Crystal structures of enzymes are indispensable to understanding their mechanisms on a molecular level. It, however, remains challenging to determine which structures are adopted in solution, especially for dynamic complexes. Here, we study the bilobed decapping enzyme Dcp2 that removes the 5' cap structure from eukaryotic mRNA and thereby efficiently terminates gene expression. The numerous Dcp2 structures can be grouped into six states where the domain orientation between the catalytic and regulatory domains significantly differs. Despite this wealth of structural information it is not possible to correlate these states with the catalytic cycle or the activity of the enzyme. Using methyl transverse relaxation-optimized NMR spectroscopy, we demonstrate that only three of the six domain orientations are present in solution, where Dcp2 adopts an open, a closed, or a catalytically active state. We show how mRNA substrate and the activator proteins Dcp1 and Edc1 influence the dynamic equilibria between these states and how this modulates catalytic activity. Importantly, the active state of the complex is only stably formed in the presence of both activators and the mRNA substrate or the m7GDP decapping product, which we rationalize based on a crystal structure of the Dcp1:Dcp2:Edc1:m7GDP complex. Interestingly, we find that the activating mechanisms in Dcp2 also result in a shift of the substrate specificity from bacterial to eukaryotic mRNA.","doi":"10.1073/pnas.1704496114","authors":"Wurm JP, Holdermann I, Overbeck JH, Mayer PHO, Sprangers R","authors_abbrev":"Wurm JP et al.","pubmed_publication_date":"06 Jun 2017","pubmed_entrez_date":"2017-05-24","publication_year":"2017","canto_session_key":"0927ffeae1602f26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-24 07:50:42","canto_approved_date":"2023-05-23 15:20:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-23 17:52:08","canto_added_date":"2018-05-25 00:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.09c","SPBC3B9.21","SPAC19A8.12"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-02-24","pdb_entries":[{"pdb_id":"5n2v","gene_chains":[{"gene_uniquename":"SPAC19A8.12","chain":"B/E","position":"1-243"},{"gene_uniquename":"SPAC18G6.09c","chain":"C/F","position":"155-180"},{"gene_uniquename":"SPBC3B9.21","chain":"A/D","position":"1-127"}],"title":"Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme","entry_authors":"Holdermann I,Sprangers R","entry_authors_abbrev":"Holdermann I et al.","reference_uniquename":"PMID:28533364","experimental_method":"X-ray","resolution":"3.1"}]},{"uniquename":"PMID:18072251","title":"The effect of superoxide dismutase deficiency on zinc toxicity in Schizosaccharomyces pombe.","citation":"J Basic Microbiol 2007 Dec;47(6):506-12","abstract":"Zinc is a metal which is a cofactor in many enzymes and a structural element in zinc finger motifs those are important in relation between DNA and regulator proteins. Little is known about uptake, distribution, toxicity and detoxification of zinc ions in cells. In this study, zinc toxicity and detoxification levels have been compared in wild type and Cu/Zn superoxide dismutase mutant (sod1Delta) cells of the fission yeast Schizosaccharomyces pombe. We evaluated the toxic levels of zinc, total zinc content, lipid peroxidation levels and catalase activities for both strains which were grown in medium containing different concentrations of zinc. sod1Delta mutant showed important growth retardation and has higher lipid peroxidation and catalase activities than wild type. Cu/Zn superoxide dismutase (SOD1) activity of wild type cells was markedly increased when they were treated with elevated levels of zinc. SOD1 mRNA level also significantly increased when the cells treated with higher concentrations of zinc. These results indicate that the mutant cells were more sensitive to zinc stress and seemed to have more oxidative intracellular environment than wild type cells. Our results support the idea that superoxide dismutase is an important factor for zinc detoxification in eukaryotes.","authors":"Tarhan C, Pekmez M, Karaer S, Arda N, Sarikaya AT","authors_abbrev":"Tarhan C et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-12-12","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.10c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:28733415","title":"Introduction to Fission Yeast as a Model System.","citation":"Cold Spring Harb Protoc 2018 May 01;2018(5)","abstract":"Here, we briefly outline the history of fission yeast, its life cycle, and aspects of its biology that make it a useful model organism for studying problems of eukaryotic molecular and cell biology.","doi":"10.1101/pdb.top079749","authors":"Hayles J, Nurse P","authors_abbrev":"Hayles J et al.","pubmed_publication_date":"01 May 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9450073","title":"A holliday junction endonuclease from fission yeast.","citation":"Biochem Soc Trans 1997 Nov;25(4):S645","abstract":"","authors":"White MF, Lilley DM","authors_abbrev":"White MF et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-02-05","publication_year":"1997","canto_session_key":"431b540e4db3bc64","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-01 15:00:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-01 15:00:26","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25G10.02"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-09-01"},{"uniquename":"PMID:23982516","title":"A winged helix domain in human MUS81 binds DNA and modulates the endonuclease activity of MUS81 complexes.","citation":"Nucleic Acids Res 2013 Nov;41(21):9741-52","abstract":"The MUS81-EME1 endonuclease maintains metazoan genomic integrity by cleaving branched DNA structures that arise during the resolution of recombination intermediates. In humans, MUS81 also forms a poorly characterized complex with EME2. Here, we identify and determine the structure of a winged helix (WH) domain from human MUS81, which binds DNA. WH domain mutations greatly reduce binding of the isolated domain to DNA and impact on incision activity of MUS81-EME1/EME2 complexes. Deletion of the WH domain reduces the endonuclease activity of both MUS81-EME1 and MUS81-EME2 complexes, and incisions made by MUS81-EME2 are made closer to the junction on substrates containing a downstream duplex, such as fork structures and nicked Holliday junctions. WH domain mutation or deletion in Schizosaccharomyces pombe phenocopies the DNA-damage sensitivity of strains deleted for mus81. Our results indicate an important role for the WH domain in both yeast and human MUS81 complexes.","doi":"10.1093/nar/gkt760","authors":"Fadden AJ, Schalbetter S, Bowles M, Harris R, Lally J, Carr AM, McDonald NQ","authors_abbrev":"Fadden AJ et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-08-29","publication_year":"2013","canto_session_key":"f370ebcf743b59da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-12-09 12:40:02","canto_approved_date":"2023-08-10 13:37:23","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2013-11-27 11:18:25","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":41,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1E7.06c","SPCC4G3.05c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2013-12-09"},{"uniquename":"PMID:42030144","title":"Gene loss, repression, amplification, and horizontal acquisition shape galactose/melibiose metabolism in fission yeast.","citation":"Proc Natl Acad Sci U S A 2026 Apr 28;123(17):e2532532123","abstract":"Natural variation in metabolism is a key driver of microbial adaptation. While galactose utilization is well studied in budding yeasts, it remains poorly understood in the fission yeast  Schizosaccharomyces pombe . Here, we reveal extensive natural variation in galactose utilization across  S. pombe  isolates-from complete deficiency (Gal - ) to exceptionally fast growth (Gal F ). Gal -  strains fall into two classes: one with deletions of the  gal  gene cluster (via three distinct mechanisms) and another with intact but repressed  gal  genes. In contrast, Gal F  is driven by an amplified gene cluster absent from the reference genome-the  gal - mel  cluster (GMC)-which also confers melibiose utilization (Mel + ). Mel +  is exclusively linked to the GMC, except in one strain harboring a standalone melibiase gene. Phylogenetic analyses indicate that horizontal gene transfer may underlie these adaptive traits. Together, our work demonstrates how diverse mechanisms-gene loss, repression, amplification, and horizontal acquisition-shape metabolic diversity and ecological specialization in fission yeast.","doi":"10.1073/pnas.2532532123","authors":"Du XM, Suo F, Du LL","authors_abbrev":"Du XM et al.","pubmed_publication_date":"28 Apr 2026","pubmed_entrez_date":"2026-04-24","publication_year":"2026","canto_session_key":"95ea4c91fb334b85","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-05-14 03:26:51","canto_added_date":"2026-04-24 23:25:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25103800","title":"Quantum dot-antibody conjugates via carbodiimide-mediated coupling for cellular imaging.","citation":"Methods Mol Biol 2014;1199:67-83","abstract":"This chapter describes the processes of antibody (Ab) production, purification, conjugation to quantum dots (QDs), and the use of the conjugates produced in intracellular imaging of cell components and structures. Specifically, information is provided on the conjugation of carboxyl surface-terminated QDs to Abs via a one-step reaction using the water-soluble carbodiimide, 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC). The chapter details the process of conjugate optimization in terms of its final fluorescence and biological activity. The method described should guarantee the production of QD-Ab conjugates, which outperform classic organic fluorophore-Ab conjugates in terms of both image definition produced and the longevity of the imaging agent.","doi":"10.1007/978-1-4939-1280-3_5","authors":"East DA, Todd M, Bruce IJ","authors_abbrev":"East DA et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-08-09","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-04-01 00:18:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10870100","title":"Cryopreservation of competent intact yeast cells for efficient electroporation.","citation":"Yeast 2000 Jul;16(10):889-96","abstract":"We have developed a simple method for cryopreserving Schizosaccharomyces pombe and Saccharomyces cerevisiae competent intact cells that permits high transformation efficiency and long-term storage for electroporation. Transformation efficiency is significantly decreased if intact cells are frozen in common permeating cryoprotectants such as glycerol or dimethyl sulphoxide. On the other hand, we found that a high transformation efficiency could be maintained if the cells were frozen in a non-permeating cryoprotectant such as sorbitol. The optimum concentration of sorbitol was found in a hypertonic solution of around 2 M. It was also very important to use S. pombe cells grown in minimal medium and S. cerevisiae cells grown in nutrient medium in the exponential growth phase. A slow freezing rate of 10 degrees C/min and a rapid thawing rate of 200 degrees C/min resulted in the highest transformation efficiency. We also found it necessary to wash the thawed cells with 1.0 M of non-electrolyte sorbitol, since the intracellular electrolytes had leaked as a result of cryoinjury. The frozen competent cells stored at -80 degrees C could be used for more than 9 months without any loss of transformation efficiency. This cryopreservation method for electroporation is simple and useful for routine transformations of intact cells. Frozen competent cells offer the advantages of long-term storage with high efficiency and freedom from the preparation of fresh competent cells for each transformation.","authors":"Suga M, Isobe M, Hatakeyama T","authors_abbrev":"Suga M et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-06-28","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22869600","title":"Seg1 controls eisosome assembly and shape.","citation":"J Cell Biol 2012 Aug 06;198(3):405-20","abstract":"Eisosomes are stable domains at the plasma membrane of the budding yeast Saccharomyces cerevisiae and have been proposed to function in endocytosis. Eisosomes are composed of two main cytoplasmic proteins, Pil1 and Lsp1, that form a scaffold around furrow-like plasma membrane invaginations. We show here that the poorly characterized eisosome protein Seg1/Ymr086w is important for eisosome biogenesis and architecture. Seg1 was required for efficient incorporation of Pil1 into eisosomes and the generation of normal plasma membrane furrows. Seg1 preceded Pil1 during eisosome formation and established a platform for the assembly of other eisosome components. This platform was further shaped and stabilized upon the arrival of Pil1 and Lsp1. Moreover, Seg1 abundance controlled the shape of eisosomes by determining their length. Similarly, the Schizosaccharomyces pombe Seg1-like protein Sle1 was necessary to generate the filamentous eisosomes present in fission yeast. The function of Seg1 in the stepwise biogenesis of eisosomes reveals striking architectural similarities between eisosomes in yeast and caveolae in mammals.","doi":"10.1083/jcb.201202097","authors":"Moreira KE, Schuck S, Schrul B, Fröhlich F, Moseley JB, Walther TC, Walter P","authors_abbrev":"Moreira KE et al.","pubmed_publication_date":"06 Aug 2012","pubmed_entrez_date":"2012-08-08","publication_year":"2012","canto_session_key":"086fa578860a41d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-13 11:48:17","canto_approved_date":"2024-03-28 12:09:53","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-11-30 16:52:10","canto_added_date":"2012-11-14 11:27:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.15","SPAC1A6.07","YMR086W"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-12-13"},{"uniquename":"PMID:11056821","title":"Use of high specific activity StarFire oligonucleotide probes to visualize low-abundance pre-mRNA splicing intermediates in S. pombe.","citation":"Biotechniques 2000 Oct;29(4):892-7","abstract":"An oligonucleotide labeling system was developed that can produce radiolabeled hybridization probes with tenfold or more higher specific activity than is obtained by traditional 5'-end-labeling with polynucleotide kinase. Yet the system is as rapid and simple as kinase labeling. The reaction uses the Klenow fragment of E. coli DNA polymerase to add alpha-32P-dA residues to the 3'-end of an oligonucleotide in a primer-extension reaction. Unlike other methods of radioactive tailing (e.g., terminal transferase), a single species is produced of both known length and known specific activity. The reaction is efficient, and over 90% of probe molecules are routinely labeled. Using this method of labeling, an oligonucleotide was shown to be tenfold more sensitive in detecting target DNA sequences in a dot blot hybridization assay, compared to the same oligonucleotide labeled using polynucleotide kinase. Northern blots of Schizosaccharomyces pombe RNA were probed with an oligonucleotide specific for intron 1 of the tf2d gene, a TATA-box binding transcription factor. Kinase-labeled tf2d probe detected only unspliced RNA, while the same oligonucleotide labeled using the new method detected both unspliced tf2d RNA and rare pre-mRNA splicing intermediates.","authors":"Behlke MA, Dames SA, McDonald WH, Gould KL, Devor EJ, Walder JA","authors_abbrev":"Behlke MA et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-11-01","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11384993","title":"Interaction between the noncatalytic region of Sid1p kinase and Cdc14p is required for full catalytic activity and localization of Sid1p.","citation":"J Biol Chem 2001 Jul 27;276(30):28185-9","abstract":"Sid1p is a group II p21-activated kinase/germinal center kinase family member that is part of a signaling network required for cytokinesis in fission yeast. Germinal center kinases are characterized by well conserved amino-terminal catalytic domains followed by less conserved carboxyl termini. The carboxyl termini among group I germinal center kinases are moderately conserved and thought to be regulatory regions. Little is known about the carboxyl termini of group II family members. Sid1p has been shown to bind the novel protein Cdc14p; however, the functional significance of this interaction is unknown. Here we report that the carboxyl terminus of Sid1p is an essential regulatory region. Our results indicate that this region contains the binding domain for Cdc14p, and this association is required for full Sid1p catalytic activity as well as intracellular localization. Furthermore, overexpression of the carboxyl terminus of Sid1p alone compromises the signaling of cytokinesis. We conclude that Cdc14p positively regulates the Sid1p kinase by binding the noncatalytic carboxyl-terminal region of the protein.","authors":"Guertin DA, McCollum D","authors_abbrev":"Guertin DA et al.","pubmed_publication_date":"27 Jul 2001","pubmed_entrez_date":"2001-06-01","publication_year":"2001","canto_session_key":"0cc7abf864eaa55c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-08 11:44:25","canto_approved_date":"2022-02-05 09:39:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-30 15:13:00","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9G1.09","SPBC24C6.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-01-08"},{"uniquename":"PMID:9090853","title":"Glucose transport in Schizosaccharomyces pombe.","citation":"Folia Microbiol (Praha) 1996;41(1):128","abstract":"","authors":"Völker B, Pinnel S, Martin HJ, Fuhrmann GF","authors_abbrev":"Völker B et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35452455","title":"Regulation of Mus81-Eme1 structure-specific endonuclease by Eme1 SUMO-binding and Rad3ATR kinase is essential in the absence of Rqh1BLM helicase.","citation":"PLoS Genet 2022 Apr;18(4):e1010165","abstract":"The Mus81-Eme1 structure-specific endonuclease is crucial for the processing of DNA recombination and late replication intermediates. In fission yeast, stimulation of Mus81-Eme1 in response to DNA damage at the G2/M transition relies on Cdc2CDK1 and DNA damage checkpoint-dependent phosphorylation of Eme1 and is critical for chromosome stability in absence of the Rqh1BLM helicase. Here we identify Rad3ATR checkpoint kinase consensus phosphorylation sites and two SUMO interacting motifs (SIM) within a short N-terminal domain of Eme1 that is required for cell survival in absence of Rqh1BLM. We show that direct phosphorylation of Eme1 by Rad3ATR is essential for catalytic stimulation of Mus81-Eme1. Chk1-mediated phosphorylation also contributes to the stimulation of Mus81-Eme1 when combined with phosphorylation of Eme1 by Rad3ATR. Both Rad3ATR- and Chk1-mediated phosphorylation of Eme1 as well as the SIMs are critical for cell fitness in absence of Rqh1BLM and abrogating bimodal phosphorylation of Eme1 along with mutating the SIMs is incompatible with rqh1Δ cell viability. Our findings unravel an elaborate regulatory network that relies on the poorly structured N-terminal domain of Eme1 and which is essential for the vital functions Mus81-Eme1 fulfills in absence of Rqh1BLM.","doi":"10.1371/journal.pgen.1010165","authors":"Giaccherini C, Scaglione S, Coulon S, Dehé PM, Gaillard PL","authors_abbrev":"Giaccherini C et al.","pubmed_publication_date":"Apr 2022","pubmed_entrez_date":"2022-04-22","publication_year":"2022","canto_session_key":"da41078c5584e5e2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-04-24 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11719547","title":"Dis1/TOG universal microtubule adaptors - one MAP for all?","citation":"J Cell Sci 2001 Nov;114(Pt 21):3805-12","abstract":"Microtubules play central roles in various cellular processes in eukaryotes. The dynamics and organisation of interphase microtubules and mitotic spindles are dramatically altered during the cell cycle and development. However, the molecular mechanisms underlying this dynamic behaviour remain to be understood. In recent years, a novel family of microtubule-associated proteins (MAPs), the Dis1/TOG family, has emerged as a versatile regulator of microtubule function. These MAPs are highly conserved in eukaryotes from yeasts and plants to humans. The localisation and function of these MAPs are not determined simply by their intrinsic microtubule-binding activity. Instead this family executes its diverse roles by interacting with other regulatory molecules, including microtubule motors and centrosomal proteins. The modular structure of these MAPs may allow them to interact with multiple proteins and thereby be involved in a wide variety of microtubule and spindle functions.","authors":"Ohkura H, Garcia MA, Toda T","authors_abbrev":"Ohkura H et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2001-11-24","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23337086","title":"Purification and characterization of the fission yeast telomere clustering factors, Bqt1 and Bqt2.","citation":"Protein Expr Purif 2013 Apr;88(2):207-13","abstract":"During meiosis, chromosomes adopt a bouquet arrangement, which is widely conserved among eukaryotes. This arrangement is assumed to play an important role in the normal progression of meiosis, by mediating the proper pairing of homologous chromosomes. In Schizosaccharomyces pombe, the complex of Bqt1 and Bqt2 plays a key role in telomere clustering and the subsequent bouquet arrangement of chromosomes during early meiotic prophase. Bqt1 and Bqt2 are part of a multi-protein complex that mediates the attachment of the telomere to the nuclear membrane. However, the structural details of the complex are needed to clarify the mechanism of telomere clustering. To enable biophysical studies of Bqt1 and Bqt2, we established a purification procedure for the Schizosaccharomyces japonicus Bqt1-Bqt2 complex, which is closely related to the S. pombe Bqt1-Bqt2 complex. A co-expression vector, in which one of the expressed subunits is fused to a removable SUMO tag, yielded high amounts of the proteins in the soluble fraction. The solubility of the Bqt1-Bqt2 complex after the removal of the SUMO tag was maintained by including CHAPS, a nondenaturing, zwitterionic detergent, in the purification buffers. These procedures enabled us to rapidly purify the stable Bqt1-Bqt2 complex. The co-purified Bqt1 and Bqt2 proteins formed a stable heterodimer, consistent with results from in vivo studies showing the requirement of both proteins for the bouquet arrangement. The expression and purification procedures established here will facilitate further biophysical studies of the Bqt1-Bqt2 complex.","doi":"10.1016/j.pep.2013.01.006","authors":"Ichikawa Y, Kagawa W, Saito K, Chikashige Y, Haraguchi T, Hiraoka Y, Kurumizaka H","authors_abbrev":"Ichikawa Y et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2013-01-23","publication_year":"2013","canto_session_key":"1ccb4c88c40908cb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-04-24 13:39:37","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-24 13:39:25","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1002.06c","SPAC6G9.13c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2015-04-24"},{"uniquename":"PMID:35664572","title":"Biomodulation of Physicochemical Parameters, Aromas, and Sensory Profile of Craft Beers by Using Non- Saccharomyces  Yeasts.","citation":"ACS Omega 2022 May 31;7(21):17822-17840","abstract":"Beer is an alcoholic beverage produced by the metabolism of yeasts and made from water, malt, and hops. In recent years, the interest in craft beers has increased considerably due to the demand for new beverages and the consumer's willingness to pay higher prices. This article explores the sensorial changes produced in craft beers by using different  Saccharomyces  and non- Saccharomyces  yeasts with several instrumental and sensory analyses performed. After a primary fermentation process with  Saccharomyces cerevisiae  or  Lachancea thermotolerans , it was observed that green beer brewed with  L. thermotolerans  had a lower pH (3.41) due to the significant production of l-lactic acid (3.98 g/L) compared to that brewed with  S. cerevisiae.  Following, the bottle conditioning was carried out with a culture of  S. cerevisiae ,  L. thermotolerans ,  Hanseniaspora vineae , or  Schizosaccharomyces pombe . Of note is the increased production of aromatic esters, including 2-phenylethyl acetate in the  H. vineae  conditioning, which is associated with a high aromatic quality, as well as ethyl lactate in all samples, whose main fermentation was carried out with  L. thermotolerans . Although this research is at an early stage, future complementary studies may shed more light on this topic.","doi":"10.1021/acsomega.2c01035","authors":"Peces-Pérez R, Vaquero C, Callejo MJ, Morata A","authors_abbrev":"Peces-Pérez R et al.","pubmed_publication_date":"31 May 2022","pubmed_entrez_date":"2022-06-06","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-06-08 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:141274","title":"Mitochondrial adenosine triphosphatase of the fission yeast Schizosaccharomyces pombe 972h-. Changes in inhibitor sensitivities during the cell cycle indicate similarities and differences in binding sites.","citation":"Biochem J 1977 Mar 15;162(3):581-90","abstract":"1. We used 11 different inhibitors of energy conservation as inhibitors of ATPase (adenosine triphosphatase) in extracts of Schizosaccharomyces pombe obtained from cells at different stages of the cell cycle. 2. All the inhibitors showed cell-cycle-dependent variations in their I50 values (microng of inhibitor/mg of protein giving 50% inhibition of inhibitor-sensitive ATPase at pH 8.6). 3. From the sensitivity profiles through the cell cycle it was concluded that: (a) oligomycin, venturicidin, triethyltin sulphate and dibutylchloromethyltin chloride all act at closely associated site(s); (b) NN'-dicyclohexylcarbodi-imide and leucinostatin both act at a similar site, which is, however, distinct from that at which other inhibitors of the membrane factor (Fo) act. 4. The variations in I50 values for efrapeptin closely followed changes in specific activity of ATPase, as would be expected for an inhibitor acting at catalytic sites; these fluctuations were different from those for aurovertin, Dio-9, 4-chloro-7-nitrobenzofurazan, quercetin and spegazzinine, all of which show different sensitivity profiles from one another. 5. Anomalous stepwise inhibitor-titration curves were obtained for spegazzinine, NN'-dicyclohexylcarbodiimide, dibutylchloromethyltin chloride and leucinostatin. 6. Possible explanations are proposed for the discontinuous expression of inhibitor-binding sites during the cell cycle.","authors":"Lloyd D, Edwards SW","authors_abbrev":"Lloyd D et al.","pubmed_publication_date":"15 Mar 1977","pubmed_entrez_date":"1977-03-15","publication_year":"1977","canto_session_key":"44c6adc86a3d1962","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-24 10:53:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-24 10:53:25","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-24"},{"uniquename":"PMID:9254700","title":"Sce3, a suppressor of the Schizosaccharomyces pombe septation mutant cdc11, encodes a putative RNA-binding protein.","citation":"Nucleic Acids Res 1997 Sep 01;25(17):3433-9","abstract":"In the fission yeast Schizosaccharomyces pombe, the cdc11 gene is required for the initiation of septum formation at the end of mitosis. The sce3 gene was cloned as a multi-copy suppressor of the heat-sensitive mutant cdc11-136. When over-expressed, it rescues all mutants of cdc11 and also a heat-sensitive allele of cdc14, but not the cdc14 null mutant. Deletion shows that sce3 is not essential for cell proliferation. It encodes a putative RNA-binding protein which shows homology to human eIF4B. Immunolocalisation indicates that Sce3p is located predominantly in the cytoplasm. Elevated expression of sce3 increases the steady-state level of cdc14 mRNA. Possible mechanisms of its action are discussed.","authors":"Schmidt S, Hofmann K, Simanis V","authors_abbrev":"Schmidt S et al.","pubmed_publication_date":"01 Sep 1997","pubmed_entrez_date":"1997-09-01","publication_year":"1997","canto_session_key":"ec374095afbe6160","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-10 16:32:18","canto_approved_date":"2026-01-31 13:39:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-10 16:32:09","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC24C6.07","SPBC18H10.04c","SPCC1739.11c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-12-10"},{"uniquename":"PMID:16005090","title":"Hybridization monitor: a method for identifying differences between complex genomes.","citation":"J Microbiol Methods 2006 Mar;64(3):305-15","abstract":"We have developed a method to identify and amplify differential fragments between two complex genomes. This technique, named hybridization-monitored genome differential analysis (HMDA), incorporates a monitor system into a PCR-based solid subtraction hybridization that tracks the entire hybridization process. This is achieved by monitoring the subtraction progress using PCR analysis of the conserved sequence of 18S rDNA in the tester sample after each round of subtraction. Homologous fragments can then be eliminated when bound to the driver DNA immobilized on a solid membrane. The hybridization continues until the conserved DNA sequence of 18S rDNA can no longer be detected, and most of the unbound DNA fragments left in the liquid were mainly the tester-specific fragments, thus greatly decreasing the complexity of DNA template of PCR amplification, increasing the amplification efficiency of differences accordingly, and ensuring high positive efficiency and coverage across the tester genome. We have applied the technique in a comparison between the genomes of Saccharomyces cerevisiae and Schizosaccharomyces pombe, which are two completely sequenced organisms. Results indicated that 95% of the subtracted clones have been confirmed to be different to the driver analyzed using the BLASTN homology alignment. With this technique, 240-fold enrichment of differences is obtained, and the coverage of the difference is up to 79%. These results indicate that HMDA can efficiently identify sequences that differ between two complex genomes.","authors":"Yueqing C, Zhengbo H, Zhongkang W, Youping Y, Guoxiong P, Yuxian X","authors_abbrev":"Yueqing C et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2005-07-12","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2336389","title":"Schizosaccharomyces U6 genes have a sequence within their introns that matches the B box consensus of tRNA internal promoters.","citation":"Nucleic Acids Res 1990 Apr 25;18(8):2025-32","abstract":"The gene for the U6 small nuclear RNA (snRNA) in the fission yeast Schizosaccharomyces pombe is interrupted by an intron whose structure is similar to those found in messenger RNA precursors (pre-mRNAs) (1). This is the only known example of a split snRNA gene from any organism--animal, plant, or yeast. To address the uniqueness of the S. pombe U6 gene, we have investigated the structures of the U6 genes from five Schizosaccharomyces strains and three other fungi. A fragment of the U6 coding sequence was amplified from the genomic DNA of each strain by the polymerase chain reaction (PCR). The sizes of the PCR products indicated that all of the fission yeast strains possess intron-containing U6 genes; whereas, the U6 genes from the other fungi appeared to be uninterrupted. The sequences of the Schizosaccharomyces U6 gene fragments revealed that each had an intron of approximately 50 base pairs in precisely the same position. In addition to the splice sites and putative branch point regions, a sequence immediately upstream of the branch point consensus was found to be conserved in all of the Schizosaccharomyces U6 genes. This sequence matches the consensus for the B box of eukaryotic tRNA promoters. These results raise the interesting possibility that synthesis of U6 RNA in fission yeast might involve the use of internal promoter elements similar to those found in other genes transcribed by RNA polymerase III.","authors":"Frendewey D, Barta I, Gillespie M, Potashkin J","authors_abbrev":"Frendewey D et al.","pubmed_publication_date":"25 Apr 1990","pubmed_entrez_date":"1990-04-25","publication_year":"1990","canto_session_key":"a2c7c54a40cf4efb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-01-16 17:23:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-01-16 17:23:02","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-01-16"},{"uniquename":"PMID:9372444","title":"A zinc finger protein required for stationary phase viability in fission yeast.","citation":"J Cell Sci 1997 Oct;110 ( Pt 20):2557-66","abstract":"Yeast cells exit the cell cycle and enter a metabolically inert stationary phase when starved for nutrients essential for normal proliferation. We have cloned a novel gene named rsv1+ (required for stationary phase viability) that is essential for fission yeast cell viability in a stationary phase induced by glucose starvation. rsv1+ encodes a 47 kDa protein with two zinc finger motifs that are partially homologous with Aspergillus nidulans CreA, Saccharomyces cerevisiae Mig1 and mammalian EGR-1/NGFI-A. Cells deleted for rsv1+ are unable to survive glucose starvation. Transcription of rsv1+ is negatively regulated by the cAMP pathway and induced by glucose starvation. Cells with the constitutively activated cAMP pathway are known to lose viability when grown to confluence or when starved for glucose. These cells are poor in rsv1+ induction and their viability loss is largely suppressed by ectopic expression of rsv1+. Thus, poor induction of rsv1+ is at least partially responsible for the viability loss. Analysis also showed that cells need to receive starvation signals before entry into the stationary phase in order to maintain viability in a glucose-poor environment.","authors":"Hao Z, Furunobu A, Nagata A, Okayama H","authors_abbrev":"Hao Z et al.","pubmed_publication_date":"Oct 1997","pubmed_entrez_date":"1998-02-12","publication_year":"1997","canto_session_key":"68a66dbed12dda86","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-09 11:39:14","canto_approved_date":"2018-06-09 11:39:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-06-09 11:39:06","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.09","SPBC19C7.03","SPBC106.10","SPBC19C2.05","SPBC409.07c","SPCC285.09c","SPBC1198.14c","SPAC8C9.03"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2018-06-09"},{"uniquename":"PMID:19546237","title":"TOR complex 2 controls gene silencing, telomere length maintenance, and survival under DNA-damaging conditions.","citation":"Mol Cell Biol 2009 Aug;29(16):4584-94","abstract":"The Target Of Rapamycin (TOR) kinase belongs to the highly conserved eukaryotic family of phosphatidylinositol-3-kinase-related kinases (PIKKs). TOR proteins are found at the core of two distinct evolutionarily conserved complexes, TORC1 and TORC2. Disruption of TORC1 or TORC2 results in characteristically dissimilar phenotypes. TORC1 is a major cell growth regulator, while the cellular roles of TORC2 are not well understood. In the fission yeast Schizosaccharomyces pombe, Tor1 is a component of the TORC2 complex, which is particularly required during starvation and various stress conditions. Our genome-wide gene expression analysis of Deltator1 mutants indicates an extensive similarity with chromatin structure mutants. Consistently, TORC2 regulates several chromatin-mediated functions, including gene silencing, telomere length maintenance, and tolerance to DNA damage. These novel cellular roles of TORC2 are rapamycin insensitive. Cells lacking Tor1 are highly sensitive to the DNA-damaging drugs hydroxyurea (HU) and methyl methanesulfonate, similar to mutants of the checkpoint kinase Rad3 (ATR). Unlike Rad3, Tor1 is not required for the cell cycle arrest in the presence of damaged DNA. Instead, Tor1 becomes essential for dephosphorylation and reactivation of the cyclin-dependent kinase Cdc2, thus allowing reentry into mitosis following recovery from DNA replication arrest. Taken together, our data highlight critical roles for TORC2 in chromatin metabolism and in promoting mitotic entry, most notably after recovery from DNA-damaging conditions. These data place TOR proteins in line with other PIKK members, such as ATM and ATR, as guardians of genome stability.","doi":"10.1128/MCB.01879-08","authors":"Schonbrun M, Laor D, López-Maury L, Bähler J, Kupiec M, Weisman R","authors_abbrev":"Schonbrun M et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-06-24","publication_year":"2009","canto_session_key":"ab2c8f1287892790","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-04-29 20:52:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-18 09:29:04","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":61,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPCC1259.13","SPAC694.06c","SPAC14C4.13","SPBC11B10.09","SPBC12C2.02c","SPBC36.05c","SPCC18B5.03","SPAC57A10.02","SPAPYUG7.02c","SPCC23B6.03c","SPCC24B10.07","SPBC216.07c","SPCC18B5.11c","SPAC24B11.06c","SPAC24H6.05","SPBC30D10.10c"],"gene_count":17,"ltp_gene_count":16,"approved_date":"2016-01-18"},{"uniquename":"PMID:29167352","title":"Two spatially distinct kinesin-14 proteins, Pkl1 and Klp2, generate collaborative inward forces against kinesin-5 Cut7 in  S. pombe .","citation":"J Cell Sci 2018 Jan 04;131(1)","abstract":"Kinesin motors play central roles in bipolar spindle assembly. In many eukaryotes, spindle pole separation is driven by kinesin-5, which generates outward force. This outward force is balanced by antagonistic inward force elicited by kinesin-14 and/or dynein. In fission yeast, two kinesin-14 proteins, Pkl1 and Klp2, play an opposing role against the kinesin-5 motor protein Cut7. However, how the two kinesin-14 proteins coordinate individual activities remains elusive. Here, we show that although deletion of either  pkl1  or  klp2  rescues temperature-sensitive  cut7  mutants, deletion of only  pkl1  can bypass the lethality caused by  cut7  deletion. Pkl1 is tethered to the spindle pole body, whereas Klp2 is localized along the spindle microtubule. Forced targeting of Klp2 to the spindle pole body, however, compensates for Pkl1 functions, indicating that cellular localizations, rather than individual motor specificities, differentiate between the two kinesin-14 proteins. Interestingly, human kinesin-14 (KIFC1 or HSET) can replace either Pkl1 or Klp2. Moreover, overproduction of HSET induces monopolar spindles, reminiscent of the phenotype of Cut7 inactivation. Taken together, this study has uncovered the biological mechanism whereby two different Kinesin-14 motor proteins exert their antagonistic roles against kinesin-5 in a spatially distinct manner.","doi":"10.1242/jcs.210740","authors":"Yukawa M, Yamada Y, Yamauchi T, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"04 Jan 2018","pubmed_entrez_date":"2017-11-24","publication_year":"2018","canto_session_key":"8f6a751681cb343e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2018-06-12 16:44:10","canto_approved_date":"2025-09-04 12:17:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-11 11:49:10","canto_added_date":"2017-11-25 01:15:31","annotation_curators":[{"name":"Takashi Toda","community_curator":true,"annotation_count":40,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c","SPAC664.10","SPAC3A11.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-06-12"},{"uniquename":"PMID:31456006","title":"Leucine depletion extends the lifespans of leucine-auxotrophic fission yeast by inducing Ecl1 family genes via the transcription factor Fil1.","citation":"Mol Genet Genomics 2019 Dec;294(6):1499-1509","abstract":"Many studies show that lifespans of various model organisms can be extended by limiting the quantities of nutrients that are necessary for proliferation. In Schizosaccharomyces pombe, the Ecl1 family genes have been associated with lifespan control and are necessary for cell responses to nutrient depletion, but their functions and mechanisms of action remain uncharacterized. Herein, we show that leucine depletion extends the chronological lifespan (CLS) of leucine-auxotrophic cells. Furthermore, depletion of leucine extended CLS and caused cell miniaturization and cell cycle arrest at the G1 phase, and all of these processes depended on Ecl1 family genes. Although depletion of leucine raises the expression of ecl1 +  by about 100-fold in leucine-auxotrophic cells, these conditions did not affect ecl1 +  expression in leucine-auxotrophic fil1 mutants that were isolated in deletion set screens using 79 mutants disrupting a transcription factor. Fil1 is a GATA-type zinc finger transcription factor that reportedly binds directly to the upstream regions of ecl1 +  and ecl2 + . Accordingly, we suggest that Ecl1 family genes are induced in response to environmental stresses, such as oxidative stress and heat stress, or by nutritional depletion of nitrogen or sulfur sources or the amino acid leucine. We also propose that these genes play important roles in the maintenance of cell survival until conditions that favor proliferation are restored.","doi":"10.1007/s00438-019-01592-6","authors":"Ohtsuka H, Kato T, Sato T, Shimasaki T, Kojima T, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-08-29","publication_year":"2019","canto_session_key":"c537e5db1ce48af2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2019-10-31 14:12:12","canto_approved_date":"2024-06-28 09:07:28","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-10-03 07:12:02","canto_added_date":"2019-08-30 00:15:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":1,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8E4.12c","SPBC30D10.10c","SPCC70.12c","SPCC1393.08","SPBC216.07c","SPBP35G2.16c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2019-10-31"},{"uniquename":"PMID:7956060","title":"The mechanism of fission yeast mating-type interconversion: evidence for two types of epigenetically inherited chromosomal imprinted events.","citation":"Cold Spring Harb Symp Quant Biol 1993;58:457-65","abstract":"Mating types of the fission yeast S. pombe interchange such that only one cell among four granddaughters of a cell ever switches, and the sister of the newly switched cell switches efficiently in consecutive cell divisions, thereby producing chains of recurrent switching. The developmental program is known to be mediated through specific parental chromosomal DNA-strand inheritance at the mating-type locus (mat1). A heritable DNA strand- and sequence-specific imprinting event was previously postulated to be required to cleave the chromosome at mat1 to initiate recombination required for switching. The pedigree analysis presented here demonstrates that swi1, swi3, and swi7 genes are required for the DNA cleavage step directly, and not for the imprinting function, since mutations in these genes reduce the efficiency of initial (i.e., switching of one in four granddaughters) and recurrent switching equally. However, when the mat1 gene sequence is placed adjacent to the indigenous mat1 locus, apparently it is imprinted inefficiently, since recurrent switches of the inserted locus occur nearly five times more often than the initial switches. This \"runaway switching\" is the first evidence formally demonstrating both the existence of and the requirement for an imprinted mat1 DNA, making it cleavable and consequently swichable. Second, the double-stranded break constitutes another imprinted event as it is evidenced to be inherited from the parental cell.","authors":"Klar AJ, Bonaduce MJ","authors_abbrev":"Klar AJ et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14504473","title":"Interdependence of the contractile ring and spindle midzone in cleavage plane maintenance.","citation":"Cell Cycle 2003;2(6):553-4","abstract":"How segregation of the chromosomes is coordinated with the ensuing cell cleavage to complete the cell cycle is not well understood. A recent study of cytokinesis in fission yeast by Pardo and Nurse suggests that the contractile ring is required for assembly of the post-mitotic microtubule array (PAA). In turn, the PAA is required to maintain the contractile ring at the cleavage plane, as well as to keep the nuclei separated at the poles of the cleaving cell. These functions may be particularly important for a cell cycle checkpoint ensuring that if cytokinesis is delayed, septation will occur between the two daughter nuclei.","authors":"Finger FP","authors_abbrev":"Finger FP","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-09-25","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11313455","title":"Fission yeast Rad17 associates with chromatin in response to aberrant genomic structures.","citation":"Mol Cell Biol 2001 May;21(10):3289-301","abstract":"Fission yeast checkpoint protein Rad17 is required for the DNA integrity checkpoint responses. A fraction of Rad17 is chromatin bound independent of the other checkpoint proteins throughout the cell cycle. Here we show that in response to DNA damage induced by either methyl methanesulfonate treatment or ionizing radiation, increased levels of Rad17 bind to chromatin. Following S-phase stall induced by hydroxyurea or a cdc22 mutation, the chromatin-bound Rad17 progressively dissociates from the chromatin. After S-phase arrest by hydroxyurea in cds1Delta or rad3Delta cells or by replication mutants, Rad17 remains chromatin bound. Rad17 is able to complex in vivo with an Rfc small subunit, Rfc2, but not with Rfc1. Furthermore, cells with rfc1Delta are checkpoint proficient, suggesting that Rfc1 does not have a role in checkpoint function. A checkpoint-defective mutant protein, Rad17(K118E), which has similar nuclear localization to that of the wild type, is unable to bind ATP and has reduced ability in chromatin binding. Mutant Rad17(K118E) protein also has reduced ability to complex with Rfc2, suggesting that Lys(118) of Rad17 plays a role in Rad17-Rfc small-subunit complex formation and chromatin association. However, in the rad17.K118E mutant cells, Cds1 can be activated by hydroxyurea. Together, these results suggest that Rad17 binds to chromatin in response to an aberrant genomic structure generated from DNA damage, replication mutant arrest, or hydroxyurea arrest in the absence of Cds1. Rad17 is not required to bind chromatin when genomic structures are protected by hydroxyurea-activated Cds1. The possible checkpoint events induced by chromatin-bound Rad17 are discussed.","authors":"Kai M, Tanaka H, Wang TS","authors_abbrev":"Kai M et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-04-21","publication_year":"2001","canto_session_key":"102974a067180de1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-02-18 16:36:25","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-02-18 16:36:16","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.13","SPBC23E6.07c","SPAC3H5.06c","SPAC1F7.05","SPCC18B5.11c","SPBC25H2.13c","SPAC23D3.02","SPBC216.05"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-02-18"},{"uniquename":"PMID:23609796","title":"Set them free: F-box protein exchange by Cand1.","citation":"Cell Res 2013 Jul;23(7):870-1","abstract":"Cand1 (Cullin-associated and neddylation-dissociated protein 1) has long been known as a regulator of SCF ubiquitin ligases, but details remained puzzling due to conflicting results from in vitro and in vivo experiments. Three recent reports, one in Cell and two in Nature Communications, propose Cand1 as a protein exchange factor with interesting mechanism that reconciles Cand1 genetics and biochemistry.","doi":"10.1038/cr.2013.55","authors":"Flick K, Kaiser P","authors_abbrev":"Flick K et al.","pubmed_publication_date":"Jul 2013","pubmed_entrez_date":"2013-04-24","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:47:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32090388","title":"Iron deficiency leads to repression of a non-canonical methionine salvage pathway in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2020 Jul;114(1):46-65","abstract":"The methionine salvage pathway (MSP) regenerates methionine from 5'-methylthioadenosine (MTA). Aerobic MSP consists of six enzymatic steps. The mug14 +  and adi1 +  genes that are involved in the third and fifth steps of the pathway are repressed when Schizosaccharomyces pombe undergoes a transition from high- to low-iron conditions. Results consistently show that methionine auxotrophic cells (met6Δ) require iron for growth in the presence of MTA as the sole source of methionine. Inactivation of the iron-using protein Adi1 leads to defects in the utilization of MTA. In the case of the third step of the pathway, co-expression of two distinct proteins, Mta3 and Mde1, is required. These proteins are interdependent to rescue MTA-dependent growth deficit of met6Δ cells. Coimmunoprecipitation experiments showed that Mta3 is a binding partner of Mde1. Meiotic met6Δ cells co-expressing mta3 +  and mde1 +  or mta3 +  and mug14 +  produce comparable levels of spores in the presence of MTA, revealing that Mde1 and Mug14 share a common function when co-expressed with Mta3 in sporulating cells. In sum, our findings unveil several novel features of MSP, especially with respect to its regulation by iron and the discovery of a non-canonical third enzymatic step in the fission yeast.","doi":"10.1111/mmi.14495","authors":"Brault A, Labbé S","authors_abbrev":"Brault A et al.","pubmed_publication_date":"Jul 2020","pubmed_entrez_date":"2020-02-25","publication_year":"2020","canto_session_key":"f5a3229db1e2f5d8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-26 01:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27766670","title":"Spatial organization of the Schizosaccharomyces pombe genome within the nucleus.","citation":"Yeast 2017 Feb;34(2):55-66","abstract":"The fission yeast Schizosaccharomyces pombe is a useful experimental system for studying the organization of chromosomes within the cell nucleus. S. pombe has a small genome that is organized into three chromosomes. The small size of the genome and the small number of chromosomes are advantageous for cytological and genome-wide studies of chromosomes; however, the small size of the nucleus impedes microscopic observations owing to limits in spatial resolution during imaging. Recent advances in microscopy, such as super-resolution microscopy, have greatly expanded the use of S. pombe as a model organism in a wide range of studies. In addition, biochemical studies, such as chromatin immunoprecipitation and chromosome conformation capture, have provided complementary approaches. Here, we review the spatial organization of the S. pombe genome as determined by a combination of cytological and biochemical studies. Copyright © 2016 John Wiley & Sons, Ltd.","doi":"10.1002/yea.3217","authors":"Matsuda A, Asakawa H, Haraguchi T, Hiraoka Y","authors_abbrev":"Matsuda A et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-10-22","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-10-23 00:15:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8573795","title":"RACH2, a novel human gene that complements a fission yeast cell cycle checkpoint mutation.","citation":"Mol Biol Cell 1995 Oct;6(10):1411-21","abstract":"We have identified a novel human gene by virtue of its ability to complement the rad1-1 checkpoint mutant of Schizosaccharomyces pombe. This gene, called RACH2, rescues the temperature-sensitive lethality of a rad1-1 wee1-50 double mutant of S. pombe. Expression of RACH2 in S. pombe rad1-1 strains partially restores UV resistance to the rad1-1 mutant strain. Expression of RACH2 in a rad1-1 cdc25-22 double mutant partially restores the dose-dependent delay in mitotic entry after irradiation that is lost in rad1-1 checkpoint-deficient mutants. Overexpression of RACH2 in human tissue culture cells induces apoptosis.","authors":"Davey S, Beach D","authors_abbrev":"Davey S et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_session_key":"b3e61b5ad72db303","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:55:41","canto_session_submitted_date":"2012-03-03 15:45:48","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.07","SPAC24H6.05","SPCC18B5.03"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"EMBL:SPD227","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41020759","title":"LLP1 is a pyrophosphatase involved in homeostasis/quality control of dolichol-linked oligosaccharide.","citation":"J Cell Biol 2025 Nov 03;224(11)","abstract":"Dolichol-linked oligosaccharide (DLO) is the precursor for asparagine (N)-linked protein glycosylation. DLO synthesis can be impaired by genetic and environmental factors, leading to the accumulation of various immature DLO intermediates that are subsequently cleaved into phosphorylated oligosaccharides (POSs). Despite the fact that its activity has been known since the 1970s, the identity of the enzyme has not been clarified. Here, we identified a Saccharomyces cerevisiae gene encoding a DLO-pyrophosphatase (Llp1), which converts DLO to POSs. Intriguingly, LLP1 mRNA was translated through a programmed +1 translational frameshifting. LLP1 orthologs encode members of VanZ family proteins, which are found in various bacteria and fungi. Llp1 and its substrate DLO are likely to be localized in the Golgi, and when LLP1 was knocked out, abnormal DLO modified by Golgi mannosyltransferases accumulated, which is consistent with a role in DLO homeostasis/quality control. This study provides insights into how the cellular levels and quality of DLOs are maintained in eukaryotes.","doi":"10.1083/jcb.202501239","authors":"Li ST, Kamada K, Honda A, Seino J, Matsuda T, Suzuki T, Dohmae N, Shichino Y, Iwasaki S, Noda Y, Costanzo M, Boone C, Suzuki T","authors_abbrev":"Li ST et al.","pubmed_publication_date":"03 Nov 2025","pubmed_entrez_date":"2025-09-29","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11E3.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20826461","title":"The role of Schizosaccharomyces pombe dma1 in spore formation during meiosis.","citation":"J Cell Sci 2010 Oct 01;123(Pt 19):3284-93","abstract":"Meiosis is a specialised form of the cell cycle that gives rise to haploid gametes. In Schizosaccharomyces pombe, the products of meiosis are four spores, which are formed by encapsulation of the four meiosis II nuclei within the cytoplasm of the zygote produced by fusion of the mating cells. The S. pombe spindle pole body is remodelled during meiosis II and membrane vesicles are then recruited there to form the forespore membrane, which encapsulates the haploid nucleus to form a prespore. Spore wall material is then deposited, giving rise to the mature spore. The septation initiation network is required to coordinate cytokinesis and mitosis in the vegetative cycle and for spore formation in the meiotic cycle. We have investigated the role of the SIN regulator dma1p in meiosis; we find that although both meiotic divisions occur in the absence of dma1p, asci frequently contain fewer than four spores, which are larger than in wild-type meiosis. Our data indicate that dma1p acts in parallel to the leading-edge proteins and septins to assure proper formation for the forespore membrane. Dma1p also contributes to the temporal regulation of the abundance of the meiosis-specific SIN component mug27p.","doi":"10.1242/jcs.069112","authors":"Krapp A, Del Rosario EC, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"01 Oct 2010","pubmed_entrez_date":"2010-09-10","publication_year":"2010","canto_session_key":"db89111ac3a96189","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-23 11:00:25","canto_approved_date":"2020-05-09 07:02:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-19 12:27:32","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPCC1739.11c","SPAC607.10","SPBC1198.12","SPBC1347.03","SPAC9G1.09","SPAC17G8.10c","SPAC1F3.06c","SPAC24C9.15c","SPCC417.06c","SPAC23C11.16"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2019-11-23"},{"uniquename":"PMID:12419251","title":"Stable association of mitotic cyclin B/Cdc2 to replication origins prevents endoreduplication.","citation":"Cell 2002 Nov 01;111(3):419-31","abstract":"We show that in fission yeast the mitotic B type cyclin Cdc13/Cdc2 kinase associates with replication origins in vivo. This association is dependent on the origin recognition complex (ORC), is established as chromosomes are replicated, and is maintained during G2 and early mitosis. Cells expressing an orp2 (ORC2) allele that reduces binding of Cdc13 to replication origins are acutely prone to chromosomal reduplication. In synchronized endoreduplicating cells, following Cdc13 ablation, replication origins are coordinately licensed prior to each successive round of S phase with the same periodicity as in a normal cell cycle. Thus, ORC bound mitotic Cyclin B/Cdc2 kinase imposes the dependency of S phase on an intervening mitosis but not the temporal licensing of replication origins between each S phase.","authors":"Wuarin J, Buck V, Nurse P, Millar JB","authors_abbrev":"Wuarin J et al.","pubmed_publication_date":"01 Nov 2002","pubmed_entrez_date":"2002-11-07","publication_year":"2002","canto_session_key":"30da765280e4ffe0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-03-26 09:36:27","canto_approved_date":"2026-06-26 08:20:03","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-10-22 15:32:09","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC29A10.15","SPBC14C8.07c","SPBC685.09","SPCC16A11.17","SPBC4.04c","SPBC11B10.09","SPBC428.18","SPAPB2B4.03"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2018-03-26"},{"uniquename":"PMID:2120045","title":"Drosophila cdc2 homologs: a functional homolog is coexpressed with a cognate variant.","citation":"EMBO J 1990 Nov;9(11):3573-81","abstract":"Using probes obtained by PCR amplification, we have cloned Drosophila cDNAs encoding structural homologs of the p34cdc2 cell cycle kinase. Southern blot experiments and in situ hybridization to polytene chromosomes demonstrated that the isolated cDNAs, were derived from two distinct genes, Dm cdc2 (31E) and Dm cdc2c (92F). Northern blot and in situ hybridization experiments revealed that these two genes are coexpressed during embryogenesis and that expression is correlated with cell proliferation. However, despite the similarity in structure and expression, the two gene products differed in functional assays in yeasts. Expression of Dm cdc2 in Schizosaccharomyces pombe and Saccharomyces cerevisiae rescued cell cycle arrest caused by mutations in cdc2+ and CDC28, the genes encoding the p34cdc2 kinase homologs of these yeasts. In contrast, the Dm cdc2c gene product did not restore cell cycle progression. Thus, in addition to the identification of a functional homolog in Drosophila, our results indicate the presence of a closely related cognate of the p34cdc2 cell cycle kinase.","authors":"Lehner CF, O'Farrell PH","authors_abbrev":"Lehner CF et al.","pubmed_publication_date":"Nov 1990","pubmed_entrez_date":"1990-11-01","publication_year":"1990","canto_session_key":"9905a9e3a93f769a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 13:14:16","canto_session_submitted_date":"2012-03-03 13:13:58","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:19385717","title":"Self-organization of dynein motors generates meiotic nuclear oscillations.","citation":"PLoS Biol 2009 Apr 21;7(4):e1000087","abstract":"Meiotic nuclear oscillations in the fission yeast Schizosaccharomyces pombe are crucial for proper chromosome pairing and recombination. We report a mechanism of these oscillations on the basis of collective behavior of dynein motors linking the cell cortex and dynamic microtubules that extend from the spindle pole body in opposite directions. By combining quantitative live cell imaging and laser ablation with a theoretical description, we show that dynein dynamically redistributes in the cell in response to load forces, resulting in more dynein attached to the leading than to the trailing microtubules. The redistribution of motors introduces an asymmetry of motor forces pulling in opposite directions, leading to the generation of oscillations. Our work provides the first direct in vivo observation of self-organized dynamic dynein distributions, which, owing to the intrinsic motor properties, generate regular large-scale movements in the cell.","doi":"10.1371/journal.pbio.1000087","authors":"Vogel SK, Pavin N, Maghelli N, Jülicher F, Tolić-Nørrelykke IM","authors_abbrev":"Vogel SK et al.","pubmed_publication_date":"21 Apr 2009","pubmed_entrez_date":"2009-04-24","publication_year":"2009","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1093.06c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:30658998","title":"A yeast-based screening assay identifies repurposed drugs that suppress mitochondrial fusion and mtDNA maintenance defects.","citation":"Dis Model Mech 2019 Feb 07;12(2)","abstract":"Mitochondria continually move, fuse and divide, and these dynamics are essential for the proper function of the organelles. Indeed, the dynamic balance of fusion and fission of mitochondria determines their morphology and allows their immediate adaptation to energetic needs as well as preserving their integrity. As a consequence, mitochondrial fusion and fission dynamics and the proteins that control these processes, which are conserved from yeast to human, are essential, and their disturbances are associated with severe human disorders, including neurodegenerative diseases. For example, mutations in  OPA1 , which encodes a conserved factor essential for mitochondrial fusion, lead to optic atrophy 1, a neurodegeneration that affects the optic nerve, eventually leading to blindness. Here, by screening a collection of ∼1600 repurposed drugs on a fission yeast model, we identified five compounds able to efficiently prevent the lethality associated with the loss of Msp1p, the fission yeast ortholog of OPA1. One compound, hexestrol, was able to rescue both the mitochondrial fragmentation and mitochondrial DNA (mtDNA) depletion induced by the loss of Msp1p, whereas the second, clomifene, only suppressed the mtDNA defect. Yeast has already been successfully used to identify candidate drugs to treat inherited mitochondrial diseases; this work may therefore provide useful leads for the treatment of optic atrophies such as optic atrophy 1 or Leber hereditary optic neuropathy.","doi":"10.1242/dmm.036558","authors":"Delerue T, Tribouillard-Tanvier D, Daloyau M, Khosrobakhsh F, Emorine LJ, Friocourt G, Belenguer P, Blondel M, Arnauné-Pelloquin L","authors_abbrev":"Delerue T et al.","pubmed_publication_date":"07 Feb 2019","pubmed_entrez_date":"2019-01-20","publication_year":"2019","canto_session_key":"60b7b54f3794075a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-06-12 17:22:30","canto_approved_date":"2024-04-05 07:34:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-04 14:55:40","canto_added_date":"2019-01-21 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1706.03","SPBC12C2.08","SPBC1718.06"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2019-06-12"},{"uniquename":"PMID:11086011","title":"The fission yeast ran GTPase is required for microtubule integrity.","citation":"J Cell Biol 2000 Nov 27;151(5):1101-11","abstract":"The microtubule cytoskeleton plays a pivotal role in cytoplasmic organization, cell division, and the correct transmission of genetic information. In a screen designed to identify fission yeast genes required for chromosome segregation, we identified a strain that carries a point mutation in the SpRan GTPase. Ran is an evolutionarily conserved eukaryotic GTPase that directly participates in nucleocytoplasmic transport and whose loss affects many biological processes. Recently a transport-independent effect of Ran on spindle formation in vitro was demonstrated, but the in vivo relevance of these findings was unclear. Here, we report the characterization of a Schizosaccharomyces pombe Ran GTPase partial loss of function mutant in which nucleocytoplasmic protein transport is normal, but the microtubule cytoskeleton is defective, resulting in chromosome missegregation and abnormal cell shape. These abnormalities are exacerbated by microtubule destabilizing drugs, by loss of the spindle checkpoint protein Mph1p, and by mutations in the spindle pole body component Cut11p, indicating that SpRan influences microtubule integrity. As the SpRan mutant phenotype can be partially suppressed by the presence of extra Mal3p, we suggest that SpRan plays a role in microtubule stability.","authors":"Fleig U, Salus SS, Karig I, Sazer S","authors_abbrev":"Fleig U et al.","pubmed_publication_date":"27 Nov 2000","pubmed_entrez_date":"2000-11-22","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1289.03c","SPBC1773.07c","SPAC1786.03","SPBC557.03c","SPAC18G6.15"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:16679453","title":"A novel DNA damage recognition protein in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2006;34(8):2347-54","abstract":"Toxic and mutagenic O6-alkylguanine adducts in DNA are repaired by O6-alkylguanine-DNA alkyltransferases (MGMT) by transfer of the alkyl group to a cysteine residue in the active site. Comparisons in silico of prokaryotes and lower eukaryotes reveal the presence of a group of proteins [alkyltransferase-like (ATL) proteins] showing amino acid sequence similarity to MGMT, but where the cysteine at the putative active site is replaced by tryptophan. To examine whether ATL proteins play a role in the biological effects of alkylating agents, we inactivated the gene, referred to as atl1+, in Schizosaccharomyces pombe, an organism that does not possess a functional MGMT homologue. The mutants are substantially more susceptible to the toxic effects of the methylating agents, N-methyl-N-nitrosourea, N-methyl-N'nitro-N-nitrosoguanidine and methyl methanesulfonate and longer chain alkylating agents including N-ethyl-N-nitrosourea, ethyl methanesulfonate, N-propyl-N-nitrosourea and N-butyl-N-nitrosourea. Purified Atl1 protein does not transfer methyl groups from O6-methylguanine in [3H]-methylated DNA but reversibly inhibits methyl transfer by human MGMT. Atl1 binds to short single-stranded oligonucleotides containing O6-methyl, -benzyl, -4-bromothenyl or -hydroxyethyl-guanine but does not remove the alkyl group or base and does not cleave the oligonucleotide in the region of the lesion. This suggests that Atl1 acts by binding to O6-alkylguanine lesions and signalling them for processing by other DNA repair pathways. This is the first report describing an activity that protects S.pombe against the toxic effects of O6-alkylguanine adducts and the biological function of a family of proteins that is widely found in prokaryotes and lower eukaryotes.","authors":"Pearson SJ, Wharton S, Watson AJ, Begum G, Butt A, Glynn N, Williams DM, Shibata T, Santibáñez-Koref MF, Margison GP","authors_abbrev":"Pearson SJ et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-05-09","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1250.04c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"EMBL:AU012274","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24782769","title":"Heme in pathophysiology: a matter of scavenging, metabolism and trafficking across cell membranes.","citation":"Front Pharmacol 2014;5:61","abstract":"Heme (iron-protoporphyrin IX) is an essential co-factor involved in multiple biological processes: oxygen transport and storage, electron transfer, drug and steroid metabolism, signal transduction, and micro RNA processing. However, excess free-heme is highly toxic due to its ability to promote oxidative stress and lipid peroxidation, thus leading to membrane injury and, ultimately, apoptosis. Thus, heme metabolism needs to be finely regulated. Intracellular heme amount is controlled at multiple levels: synthesis, utilization by hemoproteins, degradation and both intracellular and intercellular trafficking. This review focuses on recent findings highlighting the importance of controlling intracellular heme levels to counteract heme-induced oxidative stress. The contributions of heme scavenging from the extracellular environment, heme synthesis and incorporation into hemoproteins, heme catabolism and heme transport in maintaining adequate intracellular heme content are discussed. Particular attention is put on the recently described mechanisms of heme trafficking through the plasma membrane mediated by specific heme importers and exporters. Finally, the involvement of genes orchestrating heme metabolism in several pathological conditions is illustrated and new therapeutic approaches aimed at controlling heme metabolism are discussed.","doi":"10.3389/fphar.2014.00061","authors":"Chiabrando D, Vinchi F, Fiorito V, Mercurio S, Tolosano E","authors_abbrev":"Chiabrando D et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-05-01","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.13","SPAC1805.06c","SPAC222.11","SPCC4B3.05c","SPAC1F5.07c","SPAC31G5.08","SPCC320.09"],"gene_count":7,"ltp_gene_count":0},{"uniquename":"PMID:14963046","title":"Conserved nuclear export sequences in Schizosaccharomyces pombe Mex67 and human TAP function in mRNA export by direct nuclear pore interactions.","citation":"J Biol Chem 2004 Apr 23;279(17):17434-42","abstract":"Mex67, the homolog of human TAP, is not an essential mRNA export factor in Schizosaccharomyces pombe. Here we show that S. pombe encodes a homolog of the TAP cofactor that we have also named p15, whose function in mRNA export is not essential. We have identified and characterized two distinct nuclear export activities, nuclear export signal (NES) I and NES II, within the region of amino acids 434-509 of Mex67. These residues map within the known NTF2-like fold of TAP (amino acids 371-551). We show that the homologs of these two NESs are present and are functionally conserved in TAP. The NES I, NES II, and NES I + II of TAP and Mex67 directly bind with -phenylalanine-glycine (-FG)-containing sequences of S. pombe Nup159 and Nup98 but not with human p62. Mutants of NES I or NES II of Mex67/TAP that do not bind -FG Nup159 and Nup98 in vitro are unable to mediate nuclear export of a heterologous protein in S. pombe and in HeLa cells. Fused with the RNA recognition motifs (RRMs) of Crp79 and green fluorescent protein (GFP) (RRM-NES-GFP), the NES I and NES II of Mex67 or TAP can suppress the mRNA export defect of the Deltap15 rae1-167 synthetic lethal S. pombe strain, suggesting that the NESs can function in the absence of p15. These novel nuclear export sequences may provide additional routes for delivering Mex67/TAP to the nuclear pore complex.","authors":"Thakurta AG, Gopal G, Yoon JH, Saha T, Dhar R","authors_abbrev":"Thakurta AG et al.","pubmed_publication_date":"23 Apr 2004","pubmed_entrez_date":"2004-02-14","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23D3.06c","SPAPB1A10.03","SPBC1921.03c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:1762905","title":"Cloning and characterization of the rad4 gene of Schizosaccharomyces pombe; a gene showing short regions of sequence similarity to the human XRCC1 gene.","citation":"Nucleic Acids Res 1991 Dec 25;19(24):6737-41","abstract":"The rad4.116 mutant of the fission yeast Schizosaccharomyces pombe is temperature-sensitive for growth, as well as being sensitive to the killing actions of both ultraviolet light and ionizing radiation. We have cloned the rad4 gene by complementation of the temperature sensitive phenotype of the rad4.116 mutant with a S. pombe gene bank. The rad4 gene fully complemented the UV sensitivity of the rad4.116 mutant. The gene is predicted to encode a protein of 579 amino acids with a basic tail, a possible zinc finger and a nuclear location signal. The amino terminal part of the predicted rad4 ORF contains two short regions of similarity to the C-terminal part of the human XRCC1 gene. Codon usage suggests that the gene is very poorly expressed, and this was confirmed by RNA studies. Gene disruption showed that the rad4 gene was essential for the mitotic growth of S. pombe.","authors":"Fenech M, Carr AM, Murray J, Watts FZ, Lehmann AR","authors_abbrev":"Fenech M et al.","pubmed_publication_date":"25 Dec 1991","pubmed_entrez_date":"1991-12-25","publication_year":"1991","canto_session_key":"b80afd512b04f28a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-01-28 17:29:57","canto_approved_date":"2019-06-06 11:47:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-24 17:35:33","canto_added_date":"2012-02-24 05:55:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.18c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-28"},{"uniquename":"PMID:41739635","title":"Fission yeast cells use distinct cell size control mechanisms to regulate cell geometry in response to osmotic, oxidative, or low glucose conditions.","citation":"Mol Biol Cell 2026 Feb 25;:mbcE26020064","abstract":"Cells maintain an appropriate size to function, yet the mechanisms that enable size adaptation to environmental stress remain poorly understood. Fission yeast cells enter mitosis and divide at a threshold size when cyclin-dependent kinase (Cdk1) is activated through size- and time-dependent scaling of its regulators: Cdr2 kinase with cell surface area, Cdc25 phosphatase with cell volume, and mitotic cyclin Cdc13 with time. This integrated size control network is characterized in nutrient-rich conditions, but under stress it remains unclear which size parameters cells monitor, and which size- or time-sensing pathways mediate cell size changes. Using high-throughput image analysis, we quantified the geometry of dividing cells under osmotic, oxidative, and low glucose conditions. Wild-type cells increased their surface area-to-volume (SA:Vol) ratio in low glucose but decreased it under osmotic or oxidative stress, revealing distinct stress-specific geometric responses. Genetic perturbations of size- and time-sensing pathways revealed that Cdc25 is required for volume-based expansion in oxidative and osmotic stress, Cdr2 promotes surface area-based expansion in low glucose, and Cdc13 contributes to geometry changes under low glucose and osmotic stress. Although disrupting individual pathways altered normal geometric responses, cells remained viable, suggesting that a modular size control system enables flexible geometric responses to changing environments.","doi":"10.1091/mbc.E26-02-0064","authors":"Cabral EJ, Andres P, Argandona G, Duggan P, Kuran BM, Miller KE","authors_abbrev":"Cabral EJ et al.","pubmed_publication_date":"25 Feb 2026","pubmed_entrez_date":"2026-02-25","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-02-26 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17334405","title":"'Arc' escorts siRNAs in heterochromatin assembly.","citation":"Nat Struct Mol Biol 2007 Mar;14(3):178-9","abstract":"","authors":"Ekwall K","authors_abbrev":"Ekwall K","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-03-06","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17112379","title":"The CENP-B homolog, Abp1, interacts with the initiation protein Cdc23 (MCM10) and is required for efficient DNA replication in fission yeast.","citation":"Cell Div 2006 Nov 17;1:27","abstract":"Abp1, and the closely related Cbh1 and Cbh2 are homologous to the human centromere-binding protein CENP-B that has been implicated in the assembly of centromeric heterochromatin. Fission yeast cells lacking Abp1 show an increase in mini-chromosome instability suggesting that Abp1 is important for chromosome segregation and/or DNA synthesis. Here we show that Abp1 interacts with the DNA replication protein Cdc23 (MCM10) in a two-hybrid assay, and that the Deltaabp1 mutant displays a synthetic phenotype with a cdc23 temperature-sensitive mutant. Moreover, genetic interactions were also observed between abp1+ and four additional DNA replication initiation genes cdc18+, cdc21+, orc1+, and orc2+. Interestingly, we find that S phase is delayed in cells deleted for abp1+ when released from a G1 block. However, no delay is observed when cells are released from an early S phase arrest induced by hydroxyurea suggesting that Abp1 functions prior to, or coincident with, the initiation of DNA replication.","authors":"Locovei AM, Spiga MG, Tanaka K, Murakami Y, D'Urso G","authors_abbrev":"Locovei AM et al.","pubmed_publication_date":"17 Nov 2006","pubmed_entrez_date":"2006-11-23","publication_year":"2006","canto_session_key":"736ae506059f399d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-08-09 16:43:37","canto_approved_date":"2021-06-10 14:55:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-06-30 15:37:36","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":54,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.10c","SPBC1347.10","SPBC685.09","SPAC20G8.01","SPBC336.04","SPBC1105.04c","SPAC23C4.18c","SPBC1734.02c","SPBC14C8.07c","SPCC16A11.17","SPBC336.12c","SPAC27E2.05","SPAC17D4.02","SPBC14F5.12c","SPBC25H2.13c","SPBC29A10.15"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2018-08-09"},{"uniquename":"PMID:24789708","title":"Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A assembly.","citation":"Open Biol 2014 Apr 30;4(4):140043","abstract":"CENP-A chromatin forms the foundation for kinetochore assembly. Replication-independent incorporation of CENP-A at centromeres depends on its chaperone HJURP(Scm3), and Mis18 in vertebrates and fission yeast. The recruitment of Mis18 and HJURP(Scm3) to centromeres is cell cycle regulated. Vertebrate Mis18 associates with Mis18BP1(KNL2), which is critical for the recruitment of Mis18 and HJURP(Scm3). We identify two novel fission yeast Mis18-interacting proteins (Eic1 and Eic2), components of the Mis18 complex. Eic1 is essential to maintain Cnp1(CENP-A) at centromeres and is crucial for kinetochore integrity; Eic2 is dispensable. Eic1 also associates with Fta7(CENP-Q/Okp1), Cnl2(Nkp2) and Mal2(CENP-O/Mcm21), components of the constitutive CCAN/Mis6/Ctf19 complex. No Mis18BP1(KNL2) orthologue has been identified in fission yeast, consequently it remains unknown how the key Cnp1(CENP-A) loading factor Mis18 is recruited. Our findings suggest that Eic1 serves a function analogous to that of Mis18BP1(KNL2), thus representing the functional counterpart of Mis18BP1(KNL2) in fission yeast that connects with a module within the CCAN/Mis6/Ctf19 complex to allow the temporally regulated recruitment of the Mis18/Scm3(HJURP) Cnp1(CENP-A) loading factors. The novel interactions identified between CENP-A loading factors and the CCAN/Mis6/Ctf19 complex are likely to also contribute to CENP-A maintenance in other organisms.","doi":"10.1098/rsob.140043","authors":"Subramanian L, Toda NR, Rappsilber J, Allshire RC","authors_abbrev":"Subramanian L et al.","pubmed_publication_date":"30 Apr 2014","pubmed_entrez_date":"2014-05-03","publication_year":"2014","canto_session_key":"3a6306e205e3005a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1A10.02","SPBC27B12.02","SPAC23H4.11c","SPBC776.16","SPCC970.12","SPCC1672.10","SPAC25B8.14","SPAC139.06","SPAC1687.20c","SPBC1105.17","SPCC1235.07"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:12366830","title":"A nuclear protein in Schizosaccharomyces pombe with homology to the human tumour suppressor Fhit has decapping activity.","citation":"Mol Microbiol 2002 Oct;46(1):49-62","abstract":"A number of eukaryotic proteins are already known to orchestrate key steps of mRNA metabolism and translation via interactions with the 5' m7GpppN cap. We have characterized a new type of histidine triad (HIT) motif protein (Nhm1) that co-purifies with the cap-binding complex eIF4F of Schizosaccharomyces pombe. Nhm1 is an RNA-binding protein that binds to m7GTP-Sepharose, albeit with lower specificity and affinity for methylated GTP than is typical for the cap-binding protein known as eukaryotic initiation factor 4E. Sequence searches have revealed that proteins with strong sequence similarity over all regions of the new protein exist in a wide range of eukaryotes, yet none has been characterized up to now. However, other proteins that share specific motifs with Nhm1 include the human Fhit tumour suppressor protein and the diadenosine 5', 5\"'-P1, P4-tetraphosphate asymmetrical hydrolase of S. pombe. Our experimental work also reveals that Nhm1 inhibits translation in a cell-free extract prepared from S. pombe, and that it is therefore a putative translational modulator. On the other hand, purified Nhm1 manifests mRNA decapping activity, yet is physically distinct from the Saccharomyces cerevisiae decapping enzyme Dcp1. Moreover, fluorescence and immunofluorescence microscopy show that Nhm1 is predominantly, although not exclusively, nuclear. We conclude that Nhm1 has evolved as a special branch of the HIT motif superfamily that has the potential to influence both the metabolism and the translation of mRNA, and that its presence in S. pombe suggests the utilization of a novel decapping pathway.","authors":"Salehi Z, Geffers L, Vilela C, Birkenhäger R, Ptushkina M, Berthelot K, Ferro M, Gaskell S, Hagan I, Stapley B, McCarthy JE","authors_abbrev":"Salehi Z et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-10-09","publication_year":"2002","canto_session_key":"806270c955486a11","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-03 08:02:51","canto_approved_date":"2019-01-03 08:02:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-03 08:02:43","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:29812","SPBP4H10.20"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-01-03"},{"uniquename":"PMID:22105743","title":"Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe.","citation":"Proteins 2012 Feb;80(2):661-6","abstract":"Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the α-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we describe the first crystal structures of a fungal HICDH, including structures of an apoenzyme and a binary complex with a glycine tri-peptide. The structures illustrate the homology of HICDH with other β-hydroxyacid oxidative decarboxylases and reveal key differences with the active site of Thermus thermophilus HICDH that provide insights into the differences in substrate specificity of these enzymes.","doi":"10.1002/prot.23231","authors":"Bulfer SL, Hendershot JM, Trievel RC","authors_abbrev":"Bulfer SL et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-11-23","publication_year":"2012","canto_session_key":"255abbdad6ba296e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-09-12 20:26:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-12 20:26:03","canto_added_date":"2012-02-17 18:31:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31G5.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-09-12","pdb_entries":[{"pdb_id":"3ty3","gene_chains":[{"gene_uniquename":"SPAC31G5.04","chain":"A/B","position":"1-362"}],"title":"Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe bound to glycyl-glycyl-glycine","entry_authors":"Bulfer SL,Hendershot JM,Trievel RC","entry_authors_abbrev":"Bulfer SL et al.","reference_uniquename":"PMID:22105743","experimental_method":"X-ray","resolution":"1.85"},{"pdb_id":"3ty4","gene_chains":[{"gene_uniquename":"SPAC31G5.04","chain":"A/B","position":"1-362"}],"title":"Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe","entry_authors":"Bulfer SL,Hendershot JM,Trievel RC","entry_authors_abbrev":"Bulfer SL et al.","reference_uniquename":"PMID:22105743","experimental_method":"X-ray","resolution":"1.55"}]},{"uniquename":"PMID:16176584","title":"GeneSeer: a sage for gene names and genomic resources.","citation":"BMC Genomics 2005 Sep 21;6:134","abstract":"Independent identification of genes in different organisms and assays has led to a multitude of names for each gene. This balkanization makes it difficult to use gene names to locate genomic resources, homologs in other species and relevant publications.\nWe solve the naming problem by collecting data from a variety of sources and building a name-translation database. We have also built a table of homologs across several model organisms: H. sapiens, M. musculus, R. norvegicus, D. melanogaster, C. elegans, S. cerevisiae, S. pombe and A. thaliana. This allows GeneSeer to draw phylogenetic trees and identify the closest homologs. This, in turn, allows the use of names from one species to identify homologous genes in another species. A website http://geneseer.cshl.org/ is connected to the database to allow user-friendly access to our tools and external genomic resources using familiar gene names.\nGeneSeer allows access to gene information through common names and can map sequences to names. GeneSeer also allows identification of homologs and paralogs for a given gene. A variety of genomic data such as sequences, SNPs, splice variants, expression patterns and others can be accessed through the GeneSeer interface. It is freely available over the web http://geneseer.cshl.org/ and can be incorporated in other tools through an http-based software interface described on the website. It is currently used as the search engine in the RNAi codex resource, which is a portal for short hairpin RNA (shRNA) gene-silencing constructs.","authors":"Olson AJ, Tully T, Sachidanandam R","authors_abbrev":"Olson AJ et al.","pubmed_publication_date":"21 Sep 2005","pubmed_entrez_date":"2005-09-24","publication_year":"2005","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19893618","title":"Roles for the conserved spc105p/kre28p complex in kinetochore-microtubule binding and the spindle assembly checkpoint.","citation":"PLoS One 2009 Oct 28;4(10):e7640","abstract":"Kinetochores attach sister chromatids to microtubules of the mitotic spindle and orchestrate chromosome disjunction at anaphase. Although S. cerevisiae has the simplest known kinetochores, they nonetheless contain approximately 70 subunits that assemble on centromeric DNA in a hierarchical manner. Developing an accurate picture of the DNA-binding, linker and microtubule-binding layers of kinetochores, including the functions of individual proteins in these layers, is a key challenge in the field of yeast chromosome segregation. Moreover, comparison of orthologous proteins in yeast and humans promises to extend insight obtained from the study of simple fungal kinetochores to complex animal cell kinetochores.\nWe show that S. cerevisiae Spc105p forms a heterotrimeric complex with Kre28p, the likely orthologue of the metazoan kinetochore protein Zwint-1. Through systematic analysis of interdependencies among kinetochore complexes, focused on Spc105p/Kre28p, we develop a comprehensive picture of the assembly hierarchy of budding yeast kinetochores. We find Spc105p/Kre28p to comprise the third linker complex that, along with the Ndc80 and MIND linker complexes, is responsible for bridging between centromeric heterochromatin and kinetochore MAPs and motors. Like the Ndc80 complex, Spc105p/Kre28p is also essential for kinetochore binding by components of the spindle assembly checkpoint. Moreover, these functions are conserved in human cells.\nSpc105p/Kre28p is the last of the core linker complexes to be analyzed in yeast and we show it to be required for kinetochore binding by a discrete subset of kMAPs (Bim1p, Bik1p, Slk19p) and motors (Cin8p, Kar3p), all of which are nonessential. Strikingly, dissociation of these proteins from kinetochores prevents bipolar attachment, even though the Ndc80 and DASH complexes, the two best-studied kMAPs, are still present. The failure of Spc105 deficient kinetochores to bind correctly to spindle microtubules and to recruit checkpoint proteins in yeast and human cells explains the observed severity of missegregation phenotypes.","doi":"10.1371/journal.pone.0007640","authors":"Pagliuca C, Draviam VM, Marco E, Sorger PK, De Wulf P","authors_abbrev":"Pagliuca C et al.","pubmed_publication_date":"28 Oct 2009","pubmed_entrez_date":"2009-11-07","publication_year":"2009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB17E12.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38574974","title":"Quantifying redox transcription factor dynamics as a tool to investigate redox signalling.","citation":"Free Radic Biol Med 2024 Apr 02;218:16-25","abstract":"A critical feature of the cellular antioxidant response is the induction of gene expression by redox-sensitive transcription factors. In many cells, activating these transcription factors is a dynamic process involving multiple redox steps, but it is unclear how these dynamics should be measured. Here, we show how the dynamic profile of the Schizosaccharomyces pombe Pap1 transcription factor is quantifiable by three parameters: signal amplitude, signal time and signal duration. In response to increasing hydrogen peroxide concentrations, the Pap1 amplitude decreased while the signal time and duration showed saturable increases. In co-response plots, these parameters showed a complex, non-linear relationship to the mRNA levels of four Pap1-regulated genes. We also demonstrate that hydrogen peroxide and tert-butyl hydroperoxide trigger quantifiably distinct Pap1 activation profiles and transcriptional responses. Based on these findings, we propose that different oxidants and oxidant concentrations modulate the Pap1 dynamic profile, leading to specific transcriptional responses. We further show how the effect of combination and pre-exposure stresses on Pap1 activation dynamics can be quantified using this approach. This method is therefore a valuable addition to the redox signalling toolbox that may illuminate the role of dynamics in determining appropriate responses to oxidative stress.","doi":"10.1016/j.freeradbiomed.2024.04.004","authors":"Lind DJ, Naidoo KC, Tomalin LE, Rohwer JM, Veal EA, Pillay CS","authors_abbrev":"Lind DJ et al.","pubmed_publication_date":"02 Apr 2024","pubmed_entrez_date":"2024-04-04","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-04-05 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24186549","title":"Sterile mutants of Schizosaccharomyces pombe: Analysis by somatic hybridization.","citation":"Curr Genet 1982 Dec;6(3):223-7","abstract":"Sixteen sterile mutants of Schizosaccharomyces pombe, isolated from homothallic h (90)strains, were examined. It was found that they are blocked either in copulation and meiosis or in copulation alone.Protoplasts of the sterile strains were fused with protoplasts of h(+N), h(-S) or h (90)strains. In these somatic crosses, eight of the sterile strains yielded hybrids which were able to form azygotic asci. Tetrad analyses revealed that seven of these sterile strains contain a single mutation; the mutations represent at least five sterility genes (ste2, ste3, ste4, ste5, ste6). One sterile strain contains two unlinked mutations which do not represent sterility genes, but genes the interaction of which results in a sterile phenotype.","doi":"10.1007/BF00390342","authors":"Girgsdies O","authors_abbrev":"Girgsdies O","pubmed_publication_date":"Dec 1982","pubmed_entrez_date":"2013-11-05","publication_year":"1982","canto_session_key":"cf155cf5e2b5456e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-18 10:03:41","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-18 10:03:35","canto_added_date":"2014-02-16 06:09:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-09-18"},{"uniquename":"EMBL:AJ223844","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.23"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20434336","title":"The cortical ER network limits the permissive zone for actomyosin ring assembly.","citation":"Curr Biol 2010 Jun 08;20(11):1029-34","abstract":"Precise positioning of the cellular division plane is important for accurate segregation of genetic material and determination of daughter cell fates. Here we report a surprising connection between division site positioning and the organization of the cortical endoplasmic reticulum (ER). The cortical ER is an interconnected network of flat cisternae and highly curved tubules sharing a continuous lumen. Stabilization of high curvature by reticulon and DP1 family proteins contributes to formation of tubules. We show that in the fission yeast Schizosaccharomyces pombe, the ER network is maintained by a set of three membrane proteins: reticulon/Rtn1p, DP1/Yop1p, and a newly identified evolutionarily conserved protein, Tts1p. Cells lacking the ER domain sustained by these proteins exhibit severe defects in division plane positioning as a result of abnormal dispersion of a key regulator of division site selection, Mid1p, along the cell cortex. This triggers delocalized assembly of actomyosin cables and compromises their compaction into a single medially positioned ring. We propose that the cortical ER network restricts the lateral motion of Mid1p and hence generates a permissive zone for actomyosin ring assembly precisely at the cell equator.","doi":"10.1016/j.cub.2010.04.017","authors":"Zhang D, Vjestica A, Oliferenko S","authors_abbrev":"Zhang D et al.","pubmed_publication_date":"08 Jun 2010","pubmed_entrez_date":"2010-05-04","publication_year":"2010","canto_session_key":"c166fc9a9dd60e8d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-08 18:48:38","canto_approved_date":"2025-03-04 14:48:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-24 14:16:21","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":38,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1786.03","SPBC1539.04","SPCC4B3.15","SPAC1F5.04c","SPCC830.08c","SPAC926.03","SPBC32H8.12c","SPBC31A8.01c","SPAC2F7.03c"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2018-03-08"},{"uniquename":"PMID:37069604","title":"DeepEdit: single-molecule detection and phasing of A-to-I RNA editing events using nanopore direct RNA sequencing.","citation":"Genome Biol 2023 Apr 17;24(1):75","abstract":"Single-molecule detection and phasing of A-to-I RNA editing events remain an unresolved problem. Long-read and PCR-free nanopore native RNA sequencing offers a great opportunity for direct RNA editing detection. Here, we develop a neural network model, DeepEdit, that not only recognizes A-to-I editing events in single reads of Oxford Nanopore direct RNA sequencing, but also resolves the phasing of RNA editing events on transcripts. We illustrate the robustness of DeepEdit by applying it to Schizosaccharomyces pombe and Homo sapiens transcriptome data. We anticipate DeepEdit to be a powerful tool for the study of RNA editing from a new perspective.","doi":"10.1186/s13059-023-02921-0","authors":"Chen L, Ou L, Jing X, Kong Y, Xie B, Zhang N, Shi H, Qin H, Li X, Hao P","authors_abbrev":"Chen L et al.","pubmed_publication_date":"17 Apr 2023","pubmed_entrez_date":"2023-04-18","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-04-19 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34673780","title":"Restarted replication forks are error-prone and cause CAG repeat expansions and contractions.","citation":"PLoS Genet 2021 Oct;17(10):e1009863","abstract":"Disease-associated trinucleotide repeats form secondary DNA structures that interfere with replication and repair. Replication has been implicated as a mechanism that can cause repeat expansions and contractions. However, because structure-forming repeats are also replication barriers, it has been unclear whether the instability occurs due to slippage during normal replication progression through the repeat, slippage or misalignment at a replication stall caused by the repeat, or during subsequent replication of the repeat by a restarted fork that has altered properties. In this study, we have specifically addressed the fidelity of a restarted fork as it replicates through a CAG/CTG repeat tract and its effect on repeat instability. To do this, we used a well-characterized site-specific replication fork barrier (RFB) system in fission yeast that creates an inducible and highly efficient stall that is known to restart by recombination-dependent replication (RDR), in combination with long CAG repeat tracts inserted at various distances and orientations with respect to the RFB. We find that replication by the restarted fork exhibits low fidelity through repeat sequences placed 2-7 kb from the RFB, exhibiting elevated levels of Rad52- and Rad8ScRad5/HsHLTF-dependent instability. CAG expansions and contractions are not elevated to the same degree when the tract is just in front or behind the barrier, suggesting that the long-traveling Polδ-Polδ restarted fork, rather than fork reversal or initial D-loop synthesis through the repeat during stalling and restart, is the greatest source of repeat instability. The switch in replication direction that occurs due to replication from a converging fork while the stalled fork is held at the barrier is also a significant contributor to the repeat instability profile. Our results shed light on a long-standing question of how fork stalling and RDR contribute to expansions and contractions of structure-forming trinucleotide repeats, and reveal that tolerance to replication stress by fork restart comes at the cost of increased instability of repetitive sequences.","doi":"10.1371/journal.pgen.1009863","authors":"Gold MA, Whalen JM, Freon K, Hong Z, Iraqui I, Lambert SAE, Freudenreich CH","authors_abbrev":"Gold MA et al.","pubmed_publication_date":"Oct 2021","pubmed_entrez_date":"2021-10-21","publication_year":"2021","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2021-10-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8830765","title":"Septins may form a ubiquitous family of cytoskeletal filaments.","citation":"J Cell Biol 1996 Sep;134(6):1345-8","abstract":"","authors":"Cooper JA, Kiehart DP","authors_abbrev":"Cooper JA et al.","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10766248","title":"The Cdt1 protein is required to license DNA for replication in fission yeast.","citation":"Nature 2000 Apr 06;404(6778):625-8","abstract":"To maintain genome stability in eukaryotic cells, DNA is licensed for replication only after the cell has completed mitosis, ensuring that DNA synthesis (S phase) occurs once every cell cycle. This licensing control is thought to require the protein Cdc6 (Cdc18 in fission yeast) as a mediator for association of minichromosome maintenance (MCM) proteins with chromatin. The control is overridden in fission yeast by overexpressing Cdc18 (ref. 11) which leads to continued DNA synthesis in the absence of mitosis. Other factors acting in this control have been postulated and we have used a re-replication assay to identify Cdt1 (ref. 14) as one such factor. Cdt1 cooperates with Cdc18 to promote DNA replication, interacts with Cdc18, is located in the nucleus, and its concentration peaks as cells finish mitosis and proceed to S phase. Both Cdc18 and Cdt1 are required to load the MCM protein Cdc21 onto chromatin at the end of mitosis and this is necessary to initiate DNA replication. Genes related to Cdt1 have been found in Metazoa and plants (A. Whitaker, I. Roysman and T. Orr-Weaver, personal communication), suggesting that the cooperation of Cdc6/Cdc18 with Cdt1 to load MCM proteins onto chromatin may be a generally conserved feature of DNA licensing in eukaryotes.","authors":"Nishitani H, Lygerou Z, Nishimoto T, Nurse P","authors_abbrev":"Nishitani H et al.","pubmed_publication_date":"06 Apr 2000","pubmed_entrez_date":"2000-04-15","publication_year":"2000","canto_session_key":"86f3e1c248376b23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-02-03 13:48:30","canto_approved_date":"2022-09-08 10:39:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-07 15:32:08","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.18","SPBC14C8.07c","SPCC16A11.17"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-02-03"},{"uniquename":"PMID:26219431","title":"Structure of Ctk3, a subunit of the RNA polymerase II CTD kinase complex, reveals a noncanonical CTD-interacting domain fold.","citation":"Proteins 2015 Oct;83(10):1849-58","abstract":"CTDK-I is a yeast kinase complex that phosphorylates the C-terminal repeat domain (CTD) of RNA polymerase II (Pol II) to promote transcription elongation. CTDK-I contains the cyclin-dependent kinase Ctk1 (homologous to human CDK9/CDK12), the cyclin Ctk2 (human cyclin K), and the yeast-specific subunit Ctk3, which is required for CTDK-I stability and activity. Here we predict that Ctk3 consists of a N-terminal CTD-interacting domain (CID) and a C-terminal three-helix bundle domain. We determine the X-ray crystal structure of the N-terminal domain of the Ctk3 homologue Lsg1 from the fission yeast Schizosaccharomyces pombe at 2.0 Å resolution. The structure reveals eight helices arranged into a right-handed superhelical fold that resembles the CID domain present in transcription termination factors Pcf11, Nrd1, and Rtt103. Ctk3 however shows different surface properties and no binding to CTD peptides. Together with the known structure of Ctk1 and Ctk2 homologues, our results lead to a molecular framework for analyzing the structure and function of the CTDK-I complex.","doi":"10.1002/prot.24869","authors":"Mühlbacher W, Mayer A, Sun M, Remmert M, Cheung AC, Niesser J, Soeding J, Cramer P","authors_abbrev":"Mühlbacher W et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2015-07-30","publication_year":"2015","canto_session_key":"97e7933453e996d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-02-07 12:15:04","canto_approved_date":"2024-02-26 18:45:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-05 16:51:47","canto_added_date":"2015-07-31 00:19:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.08","SPAC4G9.04c","SPAC23H4.17c","SPBC28F2.12"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-02-07","pdb_entries":[{"pdb_id":"5ce7","gene_chains":[{"gene_uniquename":"SPCC4B3.08","chain":"A","position":"1-140"}],"title":"Structure of a non-canonical CID of Ctk3","entry_authors":"Muehlbacher W,Mayer A,Sun M,Remmert M,Cheung AC,Niesser J,Soeding J,Cramer P","entry_authors_abbrev":"Muehlbacher W et al.","reference_uniquename":"PMID:26219431","experimental_method":"X-ray","resolution":"2.0"}]},{"uniquename":"PMID:28159842","title":"Direct Visualization of RNA-DNA Primer Removal from Okazaki Fragments Provides Support for Flap Cleavage and Exonucleolytic Pathways in Eukaryotic Cells.","citation":"J Biol Chem 2017 Mar 24;292(12):4777-4788","abstract":"During DNA replication in eukaryotic cells, short single-stranded DNA segments known as Okazaki fragments are first synthesized on the lagging strand. The Okazaki fragments originate from ∼35-nucleotide-long RNA-DNA primers. After Okazaki fragment synthesis, these primers must be removed to allow fragment joining into a continuous lagging strand. To date, the models of enzymatic machinery that removes the RNA-DNA primers have come almost exclusively from biochemical reconstitution studies and some genetic interaction assays, and there is little direct evidence to confirm these models. One obstacle to elucidating Okazaki fragment processing has been the lack of methods that can directly examine primer removal  in vivo  In this study, we developed an electron microscopy assay that can visualize nucleotide flap structures on DNA replication forks in fission yeast ( Schizosaccharomyces pombe ). With this assay, we first demonstrated the generation of flap structures during Okazaki fragment processing  in vivo  The mean and median lengths of the flaps in wild-type cells were ∼51 and ∼41 nucleotides, respectively. We also used yeast mutants to investigate the impact of deleting key DNA replication nucleases on these flap structures. Our results provided direct  in vivo  evidence for a previously proposed flap cleavage pathway and the critical function of Dna2 and Fen1 in cleaving these flaps. In addition, we found evidence for another previously proposed exonucleolytic pathway involving RNA-DNA primer digestion by exonucleases RNase H2 and Exo1. Taken together, our observations suggest a dual mechanism for Okazaki fragment maturation in lagging strand synthesis and establish a new strategy for interrogation of this fascinating process.","doi":"10.1074/jbc.M116.758599","authors":"Liu B, Hu J, Wang J, Kong D","authors_abbrev":"Liu B et al.","pubmed_publication_date":"24 Mar 2017","pubmed_entrez_date":"2017-02-05","publication_year":"2017","canto_session_key":"0f82c11901edc80e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-07 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.05","SPBC16D10.04c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:18815595","title":"Promoter-driven splicing regulation in fission yeast.","citation":"Nature 2008 Oct 16;455(7215):997-1000","abstract":"The meiotic cell cycle is modified from the mitotic cell cycle by having a pre-meiotic S phase that leads to high levels of recombination, two rounds of nuclear division with no intervening DNA synthesis and a reductional pattern of chromosome segregation. Rem1 is a cyclin that is only expressed during meiosis in the fission yeast Schizosaccharomyces pombe. Cells in which rem1 has been deleted show decreased intragenic meiotic recombination and a delay at the onset of meiosis I (ref. 1). When ectopically expressed in mitotically growing cells, Rem1 induces a G1 arrest followed by severe mitotic catastrophes. Here we show that rem1 expression is regulated at the level of both transcription and splicing, encoding two proteins with different functions depending on the intron retention. We have determined that the regulation of rem1 splicing is not dependent on any transcribed region of the gene. Furthermore, when the rem1 promoter is fused to other intron-containing genes, the chimaeras show a meiotic-specific regulation of splicing, exactly the same as endogenous rem1. This regulation is dependent on two transcription factors of the forkhead family, Mei4 (ref. 2) and Fkh2 (ref. 3). Whereas Mei4 induces both transcription and splicing of rem1, Fkh2 is responsible for the intron retention of the transcript during vegetative growth and the pre-meiotic S phase.","doi":"10.1038/nature07325","authors":"Moldón A, Malapeira J, Gabrielli N, Gogol M, Gómez-Escoda B, Ivanova T, Seidel C, Ayté J","authors_abbrev":"Moldón A et al.","pubmed_publication_date":"16 Oct 2008","pubmed_entrez_date":"2008-09-26","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC10H11.01","SPAC644.12","SPBC32H8.11"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:19015259","title":"Structural and biochemical studies of TIGAR (TP53-induced glycolysis and apoptosis regulator).","citation":"J Biol Chem 2009 Jan 16;284(3):1748-54","abstract":"Activation of the p53 tumor suppressor by cellular stress leads to variable responses ranging from growth inhibition to apoptosis. TIGAR is a novel p53-inducible gene that inhibits glycolysis by reducing cellular levels of fructose-2,6-bisphosphate, an activator of glycolysis and inhibitor of gluconeogenesis. Here we describe structural and biochemical studies of TIGAR from Danio rerio. The overall structure forms a histidine phosphatase fold with a phosphate molecule coordinated to the catalytic histidine residue and a second phosphate molecule in a position not observed in other phosphatases. The recombinant human and zebra fish enzymes hydrolyze fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate but not fructose 6-phosphate in vitro. The TIGAR active site is open and positively charged, consistent with its enzymatic function as bisphosphatase. The closest related structures are the bacterial broad specificity phosphatase PhoE and the fructose-2,6-bisphosphatase domain of the bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. The structural comparison shows that TIGAR combines an accessible active site as observed in PhoE with a charged substrate-binding pocket as seen in the fructose-2,6-bisphosphatase domain of the bifunctional enzyme.","doi":"10.1074/jbc.M807821200","authors":"Li H, Jogl G","authors_abbrev":"Li H et al.","pubmed_publication_date":"16 Jan 2009","pubmed_entrez_date":"2008-11-19","publication_year":"2009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1687.21"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38126234","title":"Shaping the chromatin landscape at rRNA and tRNA genes, an emerging new role for RNA polymerase II transcription?","citation":"Yeast 2023 Dec 21;","abstract":"Eukaryotic genes must be condensed into chromatin while remaining accessible to the transcriptional machinery to support gene expression. Among the three eukaryotic RNA polymerases (RNAP), RNAPII is unique, partly because of the C-terminal domain (CTD) of its largest subunit, Rpb1. Rpb1 CTD can be extensively modified during the transcription cycle, allowing for the co-transcriptional recruitment of specific interacting proteins. These include chromatin remodeling factors that control the opening or closing of chromatin. How the CTD-less RNAPI and RNAPIII deal with chromatin at rRNA and tRNA genes is less understood. Here, we review recent advances in our understanding of how the chromatin at tRNA genes and rRNA genes can be remodeled in response to environmental cues in yeast, with a particular focus on the role of local RNAPII transcription in recruiting chromatin remodelers at these loci. In fission yeast, RNAPII transcription at tRNA genes is important to re-establish a chromatin environment permissive to tRNA transcription, which supports growth from stationary phase. In contrast, local RNAPII transcription at rRNA genes correlates with the closing of the chromatin in starvation in budding and fission yeast, suggesting a role in establishing silent chromatin. These opposite roles might support a general model where RNAPII transcription recruits chromatin remodelers to tRNA and rRNA genes to promote the closing and reopening of chromatin in response to the environment.","doi":"10.1002/yea.3921","authors":"Yague-Sanz C","authors_abbrev":"Yague-Sanz C","pubmed_publication_date":"21 Dec 2023","pubmed_entrez_date":"2023-12-21","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-12-22 00:25:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1658625","title":"A functional 125-kDa core polypeptide of fission yeast DNA topoisomerase II.","citation":"Mol Cell Biol 1991 Dec;11(12):6093-102","abstract":"We purified fission yeast DNA topoisomerase II (topo II) to apparent homogeneity. It consists of a single 165-kDa polypeptide in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and, upon treatment with a bifunctional reagent, doubles its molecular weight. Limited proteolysis of intact topo II by papain produces a 125-kDa core, which lacks the N-terminal 75 and the C-terminal approximately 260 amino acids but still contains regions similar to those of bacterial or phage T4 topo II subunits. The core retains relaxing and unknotting activities. Further digestion inactivates the core, cleaving it at the middle of the GyrB-like domain and at the beginning of the GyrA-like domain. Therefore, papain appears to cleave spatially distinct subdomains of topo II. We made top2 mutant genes deleted of the C-terminal 286 or N-terminal 74 amino acids, which can substitute for the wild-type top2+ gene in mitosis and meiosis. However, a mutant containing deletions of both termini cannot rescue the top2 null mutant, despite the fact that the product is enzymatically active. Therefore, the top2 product of the doubly truncated gene may not fulfill all of the in vivo requirements for top2+ function.","authors":"Shiozaki K, Yanagida M","authors_abbrev":"Shiozaki K et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"6f1818d4183cd160","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-01-03 17:10:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-03-24 10:44:01","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-03-24"},{"uniquename":"PMID:26519306","title":"Imaging Septum Formation by Fluorescence Microscopy.","citation":"Methods Mol Biol 2016;1369:73-85","abstract":"Fungal cleavage furrow formation during cytokinesis relays in the coordinated contraction of an actomyosin-based ring and the centripetal synthesis of both new plasma membrane and a special wall structure named division septum. Through transmission electron microscopy, the septum exhibits a three-layered structure with a central primary septum, flanked at both sides by the secondary septum. In contrast to the chitinous primary septum present in most of fungi, the fission yeast Schizosaccharomyces pombe does not contain chitin, instead it divides through the formation of a linear β(1,3)glucan-rich primary septum, which has been shown to be specifically stained by the fluorochrome Calcofluor white. Recent findings in S. pombe have revealed the importance of septum synthesis for the steady contraction of the ring during cytokinesis. Therefore, to study the molecular mechanisms that connect the extracellular septum wall with the other components of the cytokinetic machinery located in the plasma membrane and cytoplasm, new experimental approaches are needed. Here we describe the methods developed to image the septum structure by fluorescence microscopy, with a special focus in the analysis of septum progression by the use of time-lapse microscopy.","doi":"10.1007/978-1-4939-3145-3_6","authors":"Ribas JC, Cortés JC","authors_abbrev":"Ribas JC et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-11-01","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-02 01:19:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24323433","title":"A Lallzyme MMX-based rapid method for fission yeast protoplast preparation.","citation":"Yeast 2014 Feb;31(2):61-6","abstract":"Fungal cells including yeasts are surrounded by cell wall that counteracts turgor pressure and prevents cell lysis. Many yeast experiments, including genetic manipulation of sterile strains, morphogenesis studies, nucleic acid isolation and many others, require mechanical breakage or enzymatic removal of the cell wall. Some of these experiments require the generation of live cells lacking cell walls, called protoplasts, that can be maintained in osmostabilized medium. Enzymatic digestion of cell wall proteoglycans is a commonly used method of protoplast preparation. Currently existing protocols for fission yeast cell wall digestion are time consuming and not very efficient. We developed a new rapid method for fission yeast protoplast preparation that relies on digesting cell walls with Lallzyme MMX commercial enzyme mix, which produces protoplasts from all cells in less than 10 min. We demonstrate that these protoplasts can be utilized in three commonly used fission yeast protocols. Thus, we provide the fission yeast community with a robust and efficient plasmid extraction method, a new protocol for diploid generation and an assay for protoplast recovery that should be useful for studies of morphogenesis. Our method is potentially applicable to other yeasts and fungi.","doi":"10.1002/yea.2994","authors":"Flor-Parra I, Zhurinsky J, Bernal M, Gallardo P, Daga RR","authors_abbrev":"Flor-Parra I et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-12-11","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4118452","title":"Colcemid sensitivity of fission yeast. II. Sensitivity of stages of the cell cycle.","citation":"J Cell Biol 1973 Jan;56(1):259-62","abstract":"","authors":"Stetten G, Lederberg S","authors_abbrev":"Stetten G et al.","pubmed_publication_date":"Jan 1973","pubmed_entrez_date":"1973-01-01","publication_year":"1973","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27811944","title":"Complex structure of the fission yeast SREBP-SCAP binding domains reveals an oligomeric organization.","citation":"Cell Res 2016 Nov;26(11):1197-1211","abstract":"Sterol regulatory element-binding protein (SREBP) transcription factors are master regulators of cellular lipid homeostasis in mammals and oxygen-responsive regulators of hypoxic adaptation in fungi. SREBP C-terminus binds to the WD40 domain of SREBP cleavage-activating protein (SCAP), which confers sterol regulation by controlling the ER-to-Golgi transport of the SREBP-SCAP complex and access to the activating proteases in the Golgi. Here, we biochemically and structurally show that the carboxyl terminal domains (CTD) of Sre1 and Scp1, the fission yeast SREBP and SCAP, form a functional 4:4 oligomer and Sre1-CTD forms a dimer of dimers. The crystal structure of Sre1-CTD at 3.5 Å and cryo-EM structure of the complex at 5.4 Å together with in vitro biochemical evidence elucidate three distinct regions in Sre1-CTD required for Scp1 binding, Sre1-CTD dimerization and tetrameric formation. Finally, these structurally identified domains are validated in a cellular context, demonstrating that the proper 4:4 oligomeric complex formation is required for Sre1 activation.","doi":"10.1038/cr.2016.123","authors":"Gong X, Qian H, Shao W, Li J, Wu J, Liu JJ, Li W, Wang HW, Espenshade P, Yan N","authors_abbrev":"Gong X et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-11-05","publication_year":"2016","canto_session_key":"3cb710700bc0a9b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2018-02-02 16:57:44","canto_approved_date":"2022-02-24 13:20:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-19 21:29:41","canto_added_date":"2016-11-06 01:15:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Peter Espenshade","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.09","SPBC3B9.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-02-02","pdb_entries":[{"pdb_id":"5grs","gene_chains":[{"gene_uniquename":"SPBC3B9.15c","chain":"A/B/C/D/I/J/K/L","position":"986-1085"},{"gene_uniquename":"SPBC19C2.09","chain":"E/F/G/H","position":"628-896"}],"title":"Complex structure of the fission yeast SREBP-SCAP binding domains","entry_authors":"Gong X,Qian HW,Wu JP,Yan N","entry_authors_abbrev":"Gong X et al.","reference_uniquename":"PMID:27811944","experimental_method":"EM","resolution":"5.4"},{"pdb_id":"5gpd","gene_chains":[{"gene_uniquename":"SPBC19C2.09","chain":"A/B","position":"628-876"}],"title":"Crystal structure of the binding domain of SREBP from fission yeast","entry_authors":"Gong X,Qian HW,Wu JP,Yan N","entry_authors_abbrev":"Gong X et al.","reference_uniquename":"PMID:27811944","experimental_method":"X-ray","resolution":"3.501"}]},{"uniquename":"PMID:31630810","title":"Reassessment of the Basis of Cell Size Control Based on Analysis of Cell-to-Cell Variability.","citation":"Biophys J 2019 Nov 05;117(9):1728-1738","abstract":"Fundamental mechanisms governing cell size control and homeostasis are still poorly understood. The relationship between sizes at division and birth in single cells is used as a metric to categorize the basis of size homeostasis. Cells dividing at a fixed size regardless of birth size (sizer) are expected to show a division-birth slope of zero, whereas cells dividing after growing for a fixed size increment (adder) have an expected slope of +1. These two theoretical values are, however, rarely experimentally observed. For example, rod-shaped fission yeast Schizosaccharomyces pombe cells, which divide at a fixed surface area, exhibit a division-birth slope for cell lengths of 0.25 ± 0.02, significantly different from the expected sizer value of zero. Here, we investigate possible reasons for this discrepancy by developing a mathematical model of sizer control including the relevant sources of variation. Our results support pure sizer control and show that deviation from zero slope is exaggerated by measurement of an inappropriate geometrical quantity (e.g., length instead of area), combined with cell-to-cell radius variability. The model predicts that mutants with greater errors in size sensing or septum positioning paradoxically appear to behave as better sizers. Furthermore, accounting for cell width variability, we show that pure sizer control can in some circumstances reproduce the apparent adder behavior observed in Escherichia coli. These findings demonstrate that analysis of geometric variation can lead to new insights into cell size control.","doi":"10.1016/j.bpj.2019.09.031","authors":"Facchetti G, Knapp B, Chang F, Howard M","authors_abbrev":"Facchetti G et al.","pubmed_publication_date":"05 Nov 2019","pubmed_entrez_date":"2019-10-22","publication_year":"2019","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2019-10-23 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:X14196","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33137104","title":"The prefoldin complex stabilizes the von Hippel-Lindau protein against aggregation and degradation.","citation":"PLoS Genet 2020 Nov;16(11):e1009183","abstract":"Loss of von Hippel-Lindau protein pVHL function promotes VHL diseases, including sporadic and inherited clear cell Renal Cell Carcinoma (ccRCC). Mechanisms controlling pVHL function and regulation, including folding and stability, remain elusive. Here, we have identified the conserved cochaperone prefoldin complex in a screen for pVHL interactors. The prefoldin complex delivers non-native proteins to the chaperonin T-complex-protein-1-ring (TRiC) or Cytosolic Chaperonin containing TCP-1 (CCT) to assist folding of newly synthesized polypeptides. The pVHL-prefoldin interaction was confirmed in human cells and prefoldin knock-down reduced pVHL expression levels. Furthermore, when pVHL was expressed in Schizosaccharomyces pombe, all prefoldin mutants promoted its aggregation. We mapped the interaction of prefoldin with pVHL at the exon2-exon3 junction encoded region. Low levels of the PFDN3 prefoldin subunit were associated with poor survival in ccRCC patients harboring VHL mutations. Our results link the prefoldin complex with pVHL folding and this may impact VHL diseases progression.","doi":"10.1371/journal.pgen.1009183","authors":"Chesnel F, Couturier A, Alusse A, Gagné JP, Poirier GG, Jean D, Boisvert FM, Hascoet P, Paillard L, Arlot-Bonnemains Y, Le Goff X","authors_abbrev":"Chesnel F et al.","pubmed_publication_date":"Nov 2020","pubmed_entrez_date":"2020-11-02","publication_year":"2020","canto_session_key":"411b08353c057dbf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"LE GOFF Xavier","canto_first_approved_date":"2021-01-18 10:43:46","canto_approved_date":"2022-03-02 12:13:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-11 17:04:21","canto_added_date":"2020-11-04 01:15:05","annotation_curators":[{"name":"LE GOFF Xavier","community_curator":true,"annotation_count":33,"orcid":"0000-0002-5297-2421","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H8.07c","SPAC3A11.13","SPAC227.05","SPBC800.05c","SPAC6C3.08","SPAC227.10","SPBC1D7.01","SPBC215.02"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2021-01-18"},{"uniquename":"PMID:3029717","title":"Sequence and regulatory responses of a ribosomal protein gene from the fission yeast Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1987 Feb 25;15(4):1477-92","abstract":"We have determined the nucleotide sequence and mapped the 5' and 3' termini of a ribosomal protein gene. The gene is transcribed into a RNA molecule of about 770 nt and appears to initiate at multiple sites, as judged by SI nuclease analysis. Gene dosage experiments with a plasmid born gene leads to a proportional increase of the messenger RNA, but not to an overproduction of the protein, suggesting a posttranscriptional control mechanism. However, the heat shock response of this gene indicates that there is also a potential for transcriptional control. Comparison of the 5' flanking region of this gene with the ribosomal protein gene S 6 from Schizosaccharomyces pombe and with ribosomal protein genes from Saccharomyces cerevisiae revealed homologous sequences, which may be involved in the regulation of ribosomal protein genes.","authors":"Nischt R, Gross T, Gatermann K, Swida U, Käufer N","authors_abbrev":"Nischt R et al.","pubmed_publication_date":"25 Feb 1987","pubmed_entrez_date":"1987-02-25","publication_year":"1987","canto_session_key":"01c450fef84403b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-19 17:02:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-19 17:01:59","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2F12.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-05-19"},{"uniquename":"PMID:11739743","title":"Novel fission yeast Cdc7-Dbf4-like kinase complex required for the initiation and progression of meiotic second division.","citation":"Mol Cell Biol 2002 Jan;22(1):309-20","abstract":"Cdc7, a conserved serine/threonine protein kinase, controls initiation of DNA replication. A regulatory subunit, Dbf4, stimulates the kinase activity of Cdc7 and recruits it to the replication origins. Schizosaccharomyces pombe has a homologous kinase complex, composed of Hsk1 and Dfp1/Him1. Here, we report a novel protein kinase of S. pombe, Spo4, which shares common structural features with the Cdc7 kinases. In spite of the structural similarities, Spo4 is dispensable for mitotic growth and premeiotic DNA replication. Intriguingly, spo4 null mutants are defective in initiation and progression of the second meiotic division. Spindles for meiosis II are often fragmented. Spo4 kinase activity is markedly enhanced when the enzyme is associated with its regulatory subunit, Spo6, a Dbf4-like protein. Expression of Spo4 is specifically induced during meiosis. Spo4 is preferentially present in nuclei, but this nuclear localization does not require Spo6. These results suggest that Spo4 is a Cdc7 kinase whose primary role is in meiosis, not in DNA replication. This is the first report of an organism which has two Cdc7-related kinase complexes with different biological functions.","authors":"Nakamura T, Nakamura-Kubo M, Nakamura T, Shimoda C","authors_abbrev":"Nakamura T et al.","pubmed_publication_date":"Jan 2002","pubmed_entrez_date":"2001-12-12","publication_year":"2002","canto_session_key":"aa2d2ac23be4e963","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-01-04 22:37:07","canto_approved_date":"2026-01-04 22:37:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-01-04 22:36:10","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21C3.18","SPBC1778.04","SPBC32H8.11"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2026-01-04"},{"uniquename":"PMID:25795664","title":"Genetic Interaction Landscape Reveals Critical Requirements for Schizosaccharomyces pombe Brc1 in DNA Damage Response Mutants.","citation":"G3 (Bethesda) 2015 Mar 19;5(5):953-62","abstract":"Brc1, which was first identified as a high-copy, allele-specific suppressor of a mutation impairing the Smc5-Smc6 holocomplex in Schizosaccharomyces pombe, protects genome integrity during normal DNA replication and when cells are exposed to toxic compounds that stall or collapse replication forks. The C-terminal tandem BRCT (BRCA1 C-terminus) domain of fission yeast Brc1 docks with phosphorylated histone H2A (γH2A)-marked chromatin formed by ATR/Rad3 checkpoint kinase at arrested and damaged replication forks; however, how Brc1 functions in relation to other genome protection modules remains unclear. Here, an epistatic mini-array profile reveals critical requirements for Brc1 in mutants that are defective in multiple DNA damage response pathways, including checkpoint signaling by Rad3-Rad26/ATR-ATRIP kinase, DNA repair by Smc5-Smc6 holocomplex, replication fork stabilization by Mrc1/claspin and Swi1-Swi3/Timeless-Tipin, and control of ubiquitin-regulated proteolysis by the COP9 signalosome (CSN). Exogenous genotoxins enhance these negative genetic interactions. Rad52 and RPA foci are increased in CSN-defective cells, and loss of γH2A increases genotoxin sensitivity, indicating a critical role for the γH2A-Brc1 module in stabilizing replication forks in CSN-defective cells. A negative genetic interaction with the Nse6 subunit of Smc5-Smc6 holocomplex indicates that the DNA repair functions of Brc1 and Smc5-Smc6 holocomplex are at least partially independent. Rtt107, the Brc1 homolog in Saccharomyces cerevisiae, has a very different pattern of genetic interactions, indicating evolutionary divergence of functions and DNA damage responses.","doi":"10.1534/g3.115.017251","authors":"Sánchez A, Roguev A, Krogan NJ, Russell P","authors_abbrev":"Sánchez A et al.","pubmed_publication_date":"19 Mar 2015","pubmed_entrez_date":"2015-03-22","publication_year":"2015","canto_session_key":"d81e6d582d5b3b8f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Arancha Sanchez","canto_first_approved_date":"2016-10-21 14:51:41","canto_approved_date":"2025-09-03 16:52:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-26 10:49:53","canto_added_date":"2015-03-23 01:15:38","annotation_curators":[{"name":"Arancha Sanchez","community_curator":true,"annotation_count":40,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":155,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":79,"orcid":"0000-0003-4148-4606","file_type":"interaction","file_name":"PMID_25795664_scored_interactions.tab2.txt"}],"genes":["SPAC2G11.13","SPAC4H3.05","SPBC30D10.04","SPAC19G12.06c","SPBC32H8.07","SPAC19A8.04","SPBC3D6.10","SPBC365.06","SPCC548.04","SPAC4H3.06","SPAC8C9.12c","SPAC3G6.06c","SPAC17A2.11","SPAC20G4.04c","SPCC162.06c","SPBC725.10","SPBC27.05","SPCC2H8.05c","SPAC15A10.13","SPAC13A11.04c","SPCC23B6.05c","SPAC1A6.05c","SPBC215.03c","SPAC1635.01","SPBC20F10.05","SPCC1442.02","SPBC215.02","SPCC613.12c","SPAC23C11.04c","SPBC25H2.03","SPBC3H7.10","SPAC139.06","SPBC557.04","SPBC19G7.01c","SPAC13A11.01c","SPCC553.12c","SPAC167.01","SPBC2G2.13c","SPBC543.03c","SPAC23E2.01","SPAC664.07c","SPAC1142.01","SPBC1105.04c","SPBC582.05c","SPAC3F10.07c","SPBC342.05","SPCC1494.08c","SPAC17H9.10c","SPAC22E12.19","SPBP16F5.08c","SPBC1711.15c","SPACUNK4.11c","SPBC15D4.06","SPCC622.08c","SPBC651.05c","SPAC1687.13c","SPAC29B12.03","SPAC1952.07","SPAC23D3.09","SPAC9E9.08","SPBC1711.09c","SPAC1071.09c","SPCC736.08","SPCC61.02","SPCC1919.05","SPBC2G2.14","SPBC13G1.12","SPCC1183.09c","SPAC11E3.08c","SPCC306.04c","SPCC285.13c","SPBP16F5.05c","SPAC25H1.05","SPAC23A1.19c","SPBC1289.14","SPBC1718.07c","SPBC651.02","SPAC14C4.13","SPBC2D10.17","SPAC31G5.18c","SPBC28F2.10c","SPAC6B12.02c","SPAC1952.12c","SPCC737.09c"],"gene_count":84,"ltp_gene_count":21,"approved_date":"2016-10-21"},{"uniquename":"PMID:10233152","title":"Active nucleocytoplasmic shuttling required for function and regulation of stress-activated kinase Spc1/StyI in fission yeast.","citation":"Mol Biol Cell 1999 May;10(5):1395-407","abstract":"Transcriptional induction of many stress-response genes is dependent on stress-induced nuclear accumulation of stress-activated protein kinases (SAPKs). In the fission yeast Schizosaccharomyces pombe, nuclear accumulation of the SAPK Spc1 (also known as StyI) requires activating phosphorylation catalyzed by the SAPK kinase Wis1; however, it is unknown whether the localization of Spc1 is regulated by nuclear transport factors. Herein are reported studies that show that Spc1 localization is regulated by active transport mechanisms during osmotic stress. Nuclear import of Spc1 requires Pim1, a homologue of the guanine nucleotide exchange factor RCC1 that is essential for nucleocytoplasmic shuttling of proteins. Nuclear export of Spc1 is regulated by the export factor Crm1. An Spc1-Crm1 complex forms as Spc1 is exported from the nucleus. Wis1 and the tyrosine phosphatases Pyp1 and Pyp2 that inactivate Spc1 are excluded from the nucleus by a Crm1-independent mechanism; hence the nuclear import of Spc1 leads to transient isolation from its regulatory proteins. Thus, active nucleocytoplasmic shuttling is required for both the function and regulation of Spc1 during the osmotic shock response.","authors":"Gaits F, Russell P","authors_abbrev":"Gaits F et al.","pubmed_publication_date":"May 1999","pubmed_entrez_date":"1999-05-08","publication_year":"1999","canto_session_key":"93430f86eff5ae2f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-01 10:31:34","canto_approved_date":"2026-01-27 12:31:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-26 08:41:38","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC24B11.06c","SPAC26F1.10c","SPAC19D5.01","SPAC1805.17","SPBC557.03c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-02-01"},{"uniquename":"PMID:23462181","title":"Crosstalk between casein kinase II and Ste20-related kinase Nak1.","citation":"Cell Cycle 2013 Mar 15;12(6):884-8","abstract":"Although the sterile 20 (Ste20) serine/threonine protein kinase was originally identified as a component of the S. cerevisiae mating pathway, it has homologs in higher eukaryotes and is part of a larger family of Ste20-like kinases. Ste20-like kinases are involved in multiple cellular processes, such as cell growth, morphogenesis, apoptosis and immune response. Carrying out such a diverse array of biological functions requires numerous regulatory inputs and outputs in the form of protein-protein interactions and post-translational modifications. Hence, a thorough knowledge of Ste20-like kinase binding partners and phosphorylation sites will be essential for understanding the various roles of these kinases. Our recent study revealed that Schizosaccharomyces pombe Nak1 (a conserved member of the GC-kinase sub-family of Ste20-like kinases) is in a complex with the leucine-rich repeat-containing protein Sog2. Here, we show a novel and unexpected interaction between the Nak1-Sog2 kinase complex and Casein kinase 2 (Cka1, Ckb1 and Ckb2) using tandem-affinity purification followed by mass spectrometric analysis. In addition, we identify unique phosphosites on Nak1, Sog2 and the catalytic subunit of casein kinase 2, Cka1. Given the conserved nature of these kinases, we expect this work will shed light on the functions of these proteins both in yeast and higher eukaryotes.","doi":"10.4161/cc.24095","authors":"Cipak L, Gupta S, Rajovic I, Jin QW, Anrather D, Ammerer G, McCollum D, Gregan J","authors_abbrev":"Cipak L et al.","pubmed_publication_date":"15 Mar 2013","pubmed_entrez_date":"2013-03-07","publication_year":"2013","canto_session_key":"7f0d3ce30ca3af6f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lubos Cipak","canto_first_approved_date":"2019-12-13 15:06:43","canto_approved_date":"2022-04-27 14:51:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-11 14:58:33","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Lubos Cipak","community_curator":true,"annotation_count":42,"orcid":"0000-0001-7897-6001","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.11","SPBC887.09c","SPBC2G5.02c","SPAC1851.03","SPBC17F3.02"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-12-13"},{"uniquename":"PMID:2699733","title":"Regulation of the cell cycle timing of mitosis.","citation":"J Cell Sci Suppl 1989;12:1-8","abstract":"Considerable advances have been made recently in our understanding of how the cell cycle timing of mitosis is regulated. This has come about because links have been established between two independent areas of research, one based on a genetic approach using the fission yeast Schizosaccharomyces pombe and the second based on a biochemical approach using Xenopus and starfish oocytes. In this chapter we review work that has identified a number of the mitotic regulating genes in fission yeast and has established links with controls operative in multicellular eukaryotes.","authors":"Moreno S, Hayles J, Nurse P","authors_abbrev":"Moreno S et al.","pubmed_publication_date":"1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25547512","title":"Dissection of the PHO pathway in Schizosaccharomyces pombe using epistasis and the alternate repressor adenine.","citation":"Curr Genet 2015 May;61(2):175-83","abstract":"In Saccharomyces cerevisiae, intracellular phosphate levels are maintained by the PHO pathway, activation of which is assayed by increased phosphatase activity. The PHO pathway of Schizosaccharomyces pombe upregulates phosphatase activity (encoded by pho1 (+)) during low extracellular phosphate levels, but the underlying mechanism is poorly understood. We utilized an alternate repressor of pho1 (+) expression (adenine supplementation) along with epistasis analysis to develop a model of how S. pombe PHO pathway components interact. Analyzing Pho1 activity in S. pombe PHO pathway deletion mutants during adenine starvation, we observed most mutants with a phosphatase defect in phosphate starvation also had a defect in adenine starvation. Pho7, a transcription factor in the PHO pathway, is necessary for an adenine starvation-mediated increase in Pho1 activity. Comparing adenine starvation to phosphate starvation, there are differences in the degree to which individual mutants regulate the two responses. Through epistasis studies, we identified two positive regulatory arms and one repressive arm of the PHO pathway. PKA activation is a positive regulator of Pho1 activity under both environmental conditions and is critical for transducing adenine concentrations in the cell. The synthesis of IP7 also appears critical for the induction of Pho1 activity during adenine starvation, but IP7 is not critical during phosphate starvation, which differs from S. cerevisiae. Finally, Csk1 is critical for repression of pho1 (+) expression during phosphate starvation. We believe all of these regulatory arms converge to increase transcription of pho1 (+) and some of the regulation acts through pho7 (+).","doi":"10.1007/s00294-014-0466-6","authors":"Estill M, Kerwin-Iosue CL, Wykoff DD","authors_abbrev":"Estill M et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2014-12-31","publication_year":"2015","canto_session_key":"13d0d4d9d42e6f8f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dennis Wykoff","canto_approved_date":"2015-08-26 10:40:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-08-04 17:41:18","canto_added_date":"2015-01-01 01:15:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Dennis Wykoff","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.14","SPCC1672.06c","SPAC13G6.14","SPBC27B12.11c","SPBC8E4.01c","SPAC23H3.13c","SPBC3B9.11c","SPAC1D4.06c","SPAC4C5.02c","SPBP4G3.02","SPAC2F7.08c","SPCC757.10","SPBC106.10","SPAC17H9.04c","SPBC713.07c","SPAC1071.04c","SPAC4F10.04"],"gene_count":17,"ltp_gene_count":13,"approved_date":"2015-08-04"},{"uniquename":"PMID:12471453","title":"The Schizosaccharomyces pombe genes sep10 and sep11 encode putative general transcriptional regulators involved in multiple cellular processes.","citation":"Mol Genet Genomics 2002 Dec;268(4):553-62","abstract":"We have previously described the genetic analysis of eleven complementation groups ( sep6- sep16) defined by Schizosaccharomyces pombe mutants that are defective in cell separation and sexual differentiation. Here we report on the cloning and characterisation of two members of this set, sep10 and sep11. Sequencing of the full-length sep10 revealed a continuous ORF that encodes a conserved protein with possible functions in general transcriptional regulation. The coding region of sep11 is interrupted by introns and the putative s ep11 protein shows no sequence similarity with known proteins of other species. Disruption of each gene causes temperature sensitivity. Simultaneous disruption of both genes is lethal, demonstrating that sep10 and sep11 perform related, overlapping functions. Overexpression of aff1/ste11, a pivotal regulator of sexual development, suppresses the sterility of sep10 (-) cells, which suggests that sep10 is needed for the activity of aff1/ste11.","authors":"Szilagyi Z, Grallert A, Nemeth N, Sipiczki M","authors_abbrev":"Szilagyi Z et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2002-12-10","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC5D6.05","SPCP31B10.03c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23677513","title":"A role for Myh1 in DNA repair after treatment with strand-breaking and crosslinking chemotherapeutic agents.","citation":"Environ Mol Mutagen 2013 Jun;54(5):327-37","abstract":"The highly conserved DNA glycosylase MutY is implicated in repair of oxidative DNA damage, in particular in removing adenines misincorporated opposite 7,8-dihydro-8-oxoguanine (8-oxo-G). The MutY homologues (MutYH) physically associate with proteins implicated in replication, DNA repair, and checkpoint signaling, specifically with the DNA damage sensor complex 9-1-1 proteins. Here, we ask whether MutYH could have a broader function in sensing and repairing different types of DNA damage induced by conventional chemotherapeutics. Thus, we examined if deletion of the Schizosaccharomyces pombe MutY homologue, Myh1, alone or in combination with deletion of either component of the 9-1-1 sensor complex, influences survival after exposure to different classes of DNA damaging chemotherapeutics that do not act primarily by causing 8-oxoG lesions. We show that Myh1 contributes to survival on genotoxic stresses induced by the oxidizing, DNA double strand break-inducing, bleomycins, or the DNA crosslinking platinum compounds, particularly in a rad1 mutant background. Exposure of cells to cisplatin leads to a moderate overall accumulation of Myh1 protein. Interestingly, we found that DNA damage induced by phleomycin results in increased chromatin association of Myh1. Further, we demonstrate that Myh1 relocalizes to the nucleus after exposure to hydrogen peroxide or chemotherapeutics, most prominently seen after phleomycin treatment. These observations indicate a wider role of Myh1 in DNA repair and DNA damage-induced checkpoint activation than previously thought.","doi":"10.1002/em.21784","authors":"Jansson K, Alao JP, Viktorsson K, Warringer J, Lewensohn R, Sunnerhagen P","authors_abbrev":"Jansson K et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-05-17","publication_year":"2013","canto_session_key":"fdeaa8d994824f8c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Per Sunnerhagen","canto_approved_date":"2015-08-17 15:22:33","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-07-12 14:02:15","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Per Sunnerhagen","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c","SPAC26A3.02","SPAC20G4.04c","SPAC1952.07"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2013-07-12"},{"uniquename":"PMID:27023709","title":"Expression, purification, and crystallization of Schizosaccharomyces pombe eIF2B.","citation":"J Struct Funct Genomics 2016 Mar;17(1):33-8","abstract":"Tight control of protein synthesis is necessary for cells to respond and adapt to environmental changes rapidly. Eukaryotic translation initiation factor (eIF) 2B, the guanine nucleotide exchange factor for eIF2, is a key target of translation control at the initiation step. The nucleotide exchange activity of eIF2B is inhibited by the stress-induced phosphorylation of eIF2. As a result, the level of active GTP-bound eIF2 is lowered, and protein synthesis is attenuated. eIF2B is a large multi-subunit complex composed of five different subunits, and all five of the subunits are the gene products responsible for the neurodegenerative disease, leukoencephalopathy with vanishing white matter. However, the overall structure of eIF2B has remained unresolved, due to the difficulty in preparing a sufficient amount of the eIF2B complex. To overcome this problem, we established the recombinant expression and purification method for eIF2B from the fission yeast Schizosaccharomyces pombe. All five of the eIF2B subunits were co-expressed and reconstructed into the complex in Escherichia coli cells. The complex was successfully purified with a high yield. This recombinant eIF2B complex contains each subunit in an equimolar ratio, and the size exclusion chromatography analysis suggests it forms a heterodecamer, consistent with recent reports. This eIF2B increased protein synthesis in the reconstituted in vitro human translation system. In addition, disease-linked mutations led to subunit dissociation. Furthermore, we crystallized this functional recombinant eIF2B, and the crystals diffracted to 3.0 Å resolution.","doi":"10.1007/s10969-016-9203-3","authors":"Kashiwagi K, Shigeta T, Imataka H, Ito T, Yokoyama S","authors_abbrev":"Kashiwagi K et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2016-03-30","publication_year":"2016","canto_session_key":"ce612cb3c6fbd641","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-05-10 17:03:22","canto_approved_date":"2024-09-26 06:55:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-26 16:38:45","canto_added_date":"2016-03-31 00:15:22","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC343.14c","SPAC4D7.09","SPCC11E10.07c","SPAC21E11.06","SPAC8C9.15c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-05-10"},{"uniquename":"PMID:11523776","title":"Sna41goa1, a novel mutation causing G1/S arrest in fission yeast, is defective in a CDC45 homolog and interacts genetically with polalpha.","citation":"Mol Genet Genomics 2001 Aug;265(6):1039-49","abstract":"Proteins involved in the initiation of DNA replication play critical roles in the assembly and loading of replication complexes at replication origins. To gain further insight into the regulation of initiation, we screened in fission yeast for temperature-sensitive mutants which arrested at the G1/S boundary, and isolated nine mutants which arrested with a 1C DNA content at 36 degrees C. By linkage analysis, two complementation groups were identified which were not allelic to known G1 arrest mutations. One of the mutants isolated, sna41goul, arrested with a G1 DNA content and expressed a pleiomorphic phenotype, i.e., a mixture of cut and cdc phenotypes, at 36 degrees C. The point of arrest was identified as after START but before the hydroxyurea-induced block, by taking advantage of the mutant rad26.a14, which has a defect in an early S phase-specific checkpoint, and by performing reciprocal shift experiments. sna41 goal is allelic to sna41+, which is homologous to the CDC45 gene of budding yeast, and the mutation lies in a motif that is highly conserved in Cdc45-related proteins. The temperature sensitivity of the sna41goal mutant can be suppressed to some extent by ts mutations in polalpha. Our genetic results are consistent with a model in which Cdc45 plays crucial roles in the assembly of the replication apparatus at replication origins.","authors":"Uchiyama M, Arai K, Masai H","authors_abbrev":"Uchiyama M et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-08-29","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17D4.02","SPCC16A11.17","SPBC216.05","SPAC23C4.18c","SPAC1F7.05","SPBC4.04c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:30393157","title":"Overexpression of Schizosaccharomyces pombe tRNA 3'-end processing enzyme Trz2 leads to an increased cellular iron level and apoptotic cell death.","citation":"Fungal Genet Biol 2019 Jan;122:11-20","abstract":"The fission yeast Schizosaccharomyces pombe has two tRNase Z L  genes (trz1 and trz2) involved in nuclear and mitochondrial tRNA 3'-end processing, respectively. Overexpression of trz2 but not trz1 is toxic to cells. In the present work, we showed that trz2 overexpression led to apoptotic cell death, as revealed by DAPI and Annexin V-FITC staining. Overexpression of trz2 also caused a loss of mitochondrial membrane potential and an increased reactive oxygen species (ROS) formation. These effects required mitochondrial localization but not its catalytic activity. RNA sequencing (RNA-seq) analysis revealed increased expression levels of genes involved in iron uptake and/or iron homeostasis, suggesting an elevated level of intracellular iron in the trz2-overexpressing cells. Indeed, we showed that overexpressing trz2 increased the level of intracellular iron by ∼2-fold. We further showed that the iron chelator, bathophenanthroline disulfonic acid (BPS) nearly restored the viability of trz2-overexpression cells and reduced ROS levels in the cells. These results suggest that trz2 overexpression may cause mitochondrial dysfunction, which is likely to lead to perturbation of iron homeostasis, ROS accumulation and induction of apoptotic cell death in S. pombe.","doi":"10.1016/j.fgb.2018.10.003","authors":"Shang J, Wu L, Yang Y, Li Y, Liu Z, Huang Y","authors_abbrev":"Shang J et al.","pubmed_publication_date":"Jan 2019","pubmed_entrez_date":"2018-11-06","publication_year":"2019","canto_session_key":"7dcc48c984dda0bd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2018-12-14 18:29:18","canto_approved_date":"2021-04-29 16:01:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-11-15 06:53:19","canto_added_date":"2018-11-07 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":46,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC947.05c","SPAC328.03","SPCC1020.03","SPAC1F8.03c","SPAC977.16c","SPAC1F7.08","SPAC1F8.02c","SPCC61.01c","SPBC3D6.03c","SPACUNK4.16c","SPBC660.07","SPAC8C9.11","SPCC1223.03c","SPAC13F5.03c","SPAC8C9.12c","SPAC23G3.03","SPBC4F6.09","SPAC22A12.11","SPAC1F7.07c","SPBC1683.09c","SPCPB1C11.01"],"gene_count":21,"ltp_gene_count":1,"approved_date":"2018-12-14"},{"uniquename":"PMID:17254972","title":"Crosslinkers and motors organize dynamic microtubules to form stable bipolar arrays in fission yeast.","citation":"Cell 2007 Jan 26;128(2):357-68","abstract":"Microtubule (MT) nucleation not only occurs from centrosomes, but also in large part from dispersed nucleation sites. The subsequent sorting of short MTs into networks like the mitotic spindle requires molecular motors that laterally slide overlapping MTs and bundling proteins that statically connect MTs. How bundling proteins interfere with MT sliding is unclear. In bipolar MT bundles in fission yeast, we found that the bundler ase1p localized all along the length of antiparallel MTs, whereas the motor klp2p (kinesin-14) accumulated only at MT plus ends. Consequently, sliding forces could only overcome resistant bundling forces for short, newly nucleated MTs, which were transported to their correct position within bundles. Ase1p thus regulated sliding forces based on polarity and overlap length, and computer simulations showed these mechanisms to be sufficient to generate stable bipolar bundles. By combining motor and bundling proteins, cells can thus dynamically organize stable regions of overlap between cytoskeletal filaments.","authors":"Janson ME, Loughlin R, Loïodice I, Fu C, Brunner D, Nédélec FJ, Tran PT","authors_abbrev":"Janson ME et al.","pubmed_publication_date":"26 Jan 2007","pubmed_entrez_date":"2007-01-27","publication_year":"2007","canto_session_key":"a1838e0eb375536f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-29 17:01:10","canto_approved_date":"2024-05-01 02:20:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-29 17:01:01","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPAC664.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-10-29"},{"uniquename":"PMID:20065069","title":"The fission yeast Rad32(Mre11)-Rad50-Nbs1 complex acts both upstream and downstream of checkpoint signaling in the S-phase DNA damage checkpoint.","citation":"Genetics 2010 Apr;184(4):887-97","abstract":"The Mre11-Rad50-Nbs1 (MRN) heterotrimer plays various and complex roles in DNA damage repair and checkpoint signaling. Its role in activating Ataxia-Telangiectasia Mutated (ATM), the central checkpoint kinase in the metazoan double-strand break response, has been well studied. However, its function in the checkpoint independent of ATM activation, as well as functions that are completely checkpoint independent, are less well understood. In fission yeast, DNA damage checkpoint signaling requires Rad3, the homolog of the ATR (ATM and Rad3-related) kinase, not Tel1, the ATM homolog, allowing us to dissect MRN's ATM-independent S-phase DNA damage checkpoint roles from its role in ATM activation. We find that MRN is involved in Rad3 (ATR)-dependent checkpoint signaling in S phase, but not G2, suggesting that MRN is involved in ATR activation through its role in replication fork metabolism. In addition, we define a role for MRN in the S-phase DNA damage checkpoint-dependent slowing of replication that is independent of its role in checkpoint signaling. Genetic interactions between MRN and Rhp51, the fission yeast Rad51 homolog, lead us to suggest that MRN participates in checkpoint-dependent replication slowing through negative regulation of recombination.","doi":"10.1534/genetics.109.113019","authors":"Willis N, Rhind N","authors_abbrev":"Willis N et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-01-13","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.07","SPAC13C5.07","SPAC644.14c","SPBC6B1.09c","SPCC18B5.11c","SPBC216.06c","SPAC1556.01c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:18158900","title":"A NASP (N1/N2)-related protein, Sim3, binds CENP-A and is required for its deposition at fission yeast centromeres.","citation":"Mol Cell 2007 Dec 28;28(6):1029-44","abstract":"A defining feature of centromeres is the presence of the histone H3 variant CENP-A(Cnp1). It is not known how CENP-A(Cnp1) is specifically delivered to, and assembled into, centromeric chromatin. Through a screen for factors involved in kinetochore integrity in fission yeast, we identified Sim3. Sim3 is homologous to known histone binding proteins NASP(Human) and N1/N2(Xenopus) and aligns with Hif1(S. cerevisiae), defining the SHNi-TPR family. Sim3 is distributed throughout the nucleoplasm, yet it associates with CENP-A(Cnp1) and also binds H3. Cells defective in Sim3 function have reduced levels of CENP-A(Cnp1) at centromeres (and increased H3) and display chromosome segregation defects. Sim3 is required to allow newly synthesized CENP-A(Cnp1) to accumulate at centromeres in S and G2 phase-arrested cells in a replication-independent mechanism. We propose that one function of Sim3 is to act as an escort that hands off CENP-A(Cnp1) to chromatin assembly factors, allowing its incorporation into centromeric chromatin.","authors":"Dunleavy EM, Pidoux AL, Monet M, Bonilla C, Richardson W, Hamilton GL, Ekwall K, McLaughlin PJ, Allshire RC","authors_abbrev":"Dunleavy EM et al.","pubmed_publication_date":"28 Dec 2007","pubmed_entrez_date":"2007-12-27","publication_year":"2007","canto_session_key":"e98e46c39b053293","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-09 11:36:37","canto_approved_date":"2024-07-23 12:40:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-22 15:10:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC577.15c","SPBC1105.11c","SPBC1105.17","SPAC1834.04","SPBC8D2.04","YLL022C"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-02-09"},{"uniquename":"PMID:12972434","title":"Cpc2/RACK1 is a ribosome-associated protein that promotes efficient translation in Schizosaccharomyces pombe.","citation":"J Biol Chem 2003 Dec 05;278(49):49119-28","abstract":"Cpc2/RACK1 is a highly conserved WD domain protein found in all eucaryotes. Cpc2/RACK1 functions on mammalian signal transduction pathways most notably as an adaptor protein for the betaII protein kinase C isozyme. In single cell eucaryotes, Cpc2/RACK1 regulates growth, differentiation, and entry into G0 stationary phase. The exact biochemical function of Cpc2/RACK1 is unknown. Here, we provide evidence that Cpc2 is associated with the ribosome. Using immunoaffinity purification, we isolated ribosomal proteins in association with Cpc2/RACK1. Polysome and ribosomal subunit analysis using velocity gradient centrifugation of cell lysates demonstrated that Cpc2 co-sediments with the 40 S ribosomal subunit and with polysomes. Conditions known to disrupt ribosome structure alter sedimentation of the ribosome and of Cpc2/RACK1 coordinately. Loss of cpc2 does not dramatically alter the rate of cellular protein synthesis but causes a decrease in the steady state level of numerous proteins, some of which regulate methionine metabolism. Whereas real time PCR analysis demonstrated that transcriptional mechanisms are responsible for down-regulation of some of these proteins, one protein, ribosomal protein L25, is probably regulated at the level of translation.","authors":"Shor B, Calaycay J, Rushbrook J, McLeod M","authors_abbrev":"Shor B et al.","pubmed_publication_date":"05 Dec 2003","pubmed_entrez_date":"2003-09-16","publication_year":"2003","canto_session_key":"d6a49443005b8f21","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-02 11:41:25","canto_approved_date":"2025-09-03 14:01:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-21 20:35:01","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6B12.15","SPBC106.18","SPBC4F6.04"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2020-12-02"},{"uniquename":"PMID:38865179","title":"Transient PP2A SIP complex localization to mitotic SPBs for SIN inhibition is mediated solely by the Csc1 FHA domain.","citation":"Mol Biol Cell 2024 Jun 12;:mbcE24040196","abstract":"Many organisms utilize an actin- and myosin-based cytokinetic ring to help complete cytokinesis. In  Schizosaccharomyces pombe , the Septation Initiation Network (SIN) promotes proper CR function and stability. The SIN is a conserved and essential signaling network consisting of a GTPase and a cascade of kinases assembled at the spindle pole body (SPB). The PP2A SIN inhibitory phosphatase (SIP) complex related to the STRIPAK phosphatase complex is one inhibitor of SIN signaling. The SIP consists of Csc1, Csc2, Csc3, Csc4, Paa1, and the phosphatase subunit Ppa3. Here, we determine that the SIP is anchored at the SPB via the Csc1 FHA domain and that constitutive SPB localization of the SIP is lethal due to persistent SIN inhibition. Disrupting SIP docking at the SPB with a point mutation within the FHA domain or eliminating phosphatase activity by introducing a point mutation within Ppa3 resulted in intact SIP complexes without SIN inhibitory function. Lastly, we defined the unique features of Ppa3 that allow it, but not two other PP2A catalytic subunits, to incorporate into the SIP. Overall, we provide insight into how the SIP complex assembles, localizes, and functions to counteract the SIN with spatiotemporal precision during cytokinesis.","doi":"10.1091/mbc.E24-04-0196","authors":"Willet AH, Ren L, Turner LA, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"12 Jun 2024","pubmed_entrez_date":"2024-06-12","publication_year":"2024","canto_session_key":"45245ca07b498e71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2024-07-22 14:01:05","canto_approved_date":"2026-01-31 13:37:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-09 19:40:38","canto_added_date":"2024-06-12 23:25:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":22,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPAC22H10.04","SPBC3H7.13","SPBC27B12.04c","SPAC4H3.11c","SPAC9G1.09","SPAC2C4.10c","SPBC1773.01","SPBC21.06c","SPCC1739.11c","SPAC6F6.08c"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2024-07-22"},{"uniquename":"PMID:26365187","title":"Dissecting Fission Yeast Shelterin Interactions via MICro-MS Links Disruption of Shelterin Bridge to Tumorigenesis.","citation":"Cell Rep 2015 Sep 29;12(12):2169-80","abstract":"Shelterin, a six-member complex, protects telomeres from nucleolytic attack and regulates their elongation by telomerase. Here, we have developed a strategy, called MICro-MS (Mapping Interfaces via Crosslinking-Mass Spectrometry), that combines crosslinking-mass spectrometry and phylogenetic analysis to identify contact sites within the complex. This strategy allowed identification of separation-of-function mutants of fission yeast Ccq1, Poz1, and Pot1 that selectively disrupt their respective interactions with Tpz1. The various telomere dysregulation phenotypes observed in these mutants further emphasize the critical regulatory roles of Tpz1-centered shelterin interactions in telomere homeostasis. Furthermore, the conservation between fission yeast Tpz1-Pot1 and human TPP1-POT1 interactions led us to map a human melanoma-associated POT1 mutation (A532P) to the TPP1-POT1 interface. Diminished TPP1-POT1 interaction caused by hPOT1-A532P may enable unregulated telomere extension, which, in turn, helps cancer cells to achieve replicative immortality. Therefore, our study reveals a connection between shelterin connectivity and tumorigenicity.","doi":"10.1016/j.celrep.2015.08.043","authors":"Liu J, Yu C, Hu X, Kim JK, Bierma JC, Jun HI, Rychnovsky SD, Huang L, Qiao F","authors_abbrev":"Liu J et al.","pubmed_publication_date":"29 Sep 2015","pubmed_entrez_date":"2015-09-15","publication_year":"2015","canto_session_key":"f5d4afcf07aeed5b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Feng Qiao","canto_approved_date":"2016-08-03 13:11:16","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-21 23:10:53","canto_added_date":"2015-09-16 00:19:09","annotation_curators":[{"name":"Feng Qiao","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.13c","SPCC188.07","SPAC26H5.06","SPBC800.03","SPAC6F6.16c","SPBC29A3.14c","SPAC644.14c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-07-21"},{"uniquename":"PMID:14160283","title":"[SIMPLE DETERMINATION OF 1-MALIC ACID USING SCHIZOSACCHAROMYCES POMBE].","citation":"C R Hebd Seances Acad Sci 1964 Jun 01;258:5542-3","abstract":"","authors":"PEYNAUD E, LAFON-LAFOURCADE S","authors_abbrev":"PEYNAUD E et al.","pubmed_publication_date":"01 Jun 1964","pubmed_entrez_date":"1964-06-01","publication_year":"1964","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15449306","title":"Schizosaccharomyces pombe ER oxidoreductin-like proteins SpEro1a p and SpEro1b p.","citation":"Yeast 2004 Sep;21(12):1035-44","abstract":"Endoplasmic reticulum oxidoreductins (Ero proteins) are essential for oxidation of protein disulphide isomerase (Pdi), which introduces disulphide bonds in target proteins. Contrary to the situation in Saccharomyces cerevisiae, with a single Ero protein (Ero1p), the genomes of Schizosaccharomyces pombe and of humans encode two Ero-like proteins. Here we show that both Sz. pombe proteins (SpEro1a p and SpEro1b p) are N-glycosylated and firmly associated with membranes of the secretory pathway. Surprisingly, only expression of SpEro1b p completely restores growth of the temperature-sensitive S. cerevisiae ero1-1 mutant, whereas SpEro1a p only partially complements this mutation. Upon expression in S. cerevisiae wild-type cells, SpEro1b p leads to a significantly increased resistance to reductive stress by dithiothreitol, whereas SpEro1a p has only a marginal effect. These data suggest that SpEro1b p is a functional homologue of the S. cerevisiae Ero1p.","authors":"Kettner K, Blomberg A, Rödel G","authors_abbrev":"Kettner K et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-09-28","publication_year":"2004","canto_session_key":"a0734b28ff6e3a38","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-12 18:39:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-12 18:38:59","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.16c","SPCC1450.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-10-12"},{"uniquename":"PMID:24569997","title":"Characterization of Schizosaccharomyces pombe copper transporter proteins in meiotic and sporulating cells.","citation":"J Biol Chem 2014 Apr 04;289(14):10168-81","abstract":"Meiosis requires copper to undertake its program in which haploid gametes are produced from diploid precursor cells. In Schizosaccharomyces pombe, copper is transported by three members of the copper transporter (Ctr) family, namely Ctr4, Ctr5, and Ctr6. Although central for sexual differentiation, very little is known about the expression profile, cellular localization, and physiological contribution of the Ctr proteins during meiosis. Analysis of gene expression of ctr4(+) and ctr5(+) revealed that they are primarily expressed in early meiosis under low copper conditions. In the case of ctr6(+), its expression is broader, being detected throughout the entire meiotic process with an increase during middle- and late-phase meiosis. Whereas the expression of ctr4(+) and ctr5(+) is exclusively dependent on the presence of Cuf1, ctr6(+) gene expression relies on two distinct regulators, Cuf1 and Mei4. Ctr4 and Ctr5 proteins co-localize at the plasma membrane shortly after meiotic induction, whereas Ctr6 is located on the membrane of vacuoles. After meiotic divisions, Ctr4 and Ctr5 disappear from the cell surface, whereas Ctr6 undergoes an intracellular re-location to co-localize with the forespore membrane. Under copper-limiting conditions, disruption of ctr4(+) and ctr6(+) results in altered SOD1 activity, whereas these mutant cells exhibit substantially decreased levels of CAO activity mostly in early- and middle-phase meiosis. Collectively, these results emphasize the notion that Ctr proteins exhibit differential expression, localization, and contribution in delivering copper to SOD1 and Cao1 proteins during meiosis.","doi":"10.1074/jbc.M113.543678","authors":"Plante S, Ioannoni R, Beaudoin J, Labbé S","authors_abbrev":"Plante S et al.","pubmed_publication_date":"04 Apr 2014","pubmed_entrez_date":"2014-02-27","publication_year":"2014","canto_session_key":"7c6f6dac1e623770","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Samuel Plante","canto_first_approved_date":"2019-01-28 16:11:02","canto_approved_date":"2025-09-03 17:53:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-26 13:25:14","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Samuel Plante","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1142.05","SPCC1393.10","SPBC32H8.11","SPAC821.10c","SPAC2E1P3.04","SPAPB1A11.01","SPBC23G7.16","SPAC31A2.11c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2019-01-28"},{"uniquename":"PMID:25710177","title":"Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clients.","citation":"PLoS One 2015;10(2):e0117192","abstract":"The evolution of animals involved acquisition of an emergent gene repertoire for gastrulation. Whether loss of genes also co-evolved with this developmental reprogramming has not yet been addressed. Here, we identify twenty-four genetic functions that are retained in fungi and choanoflagellates but undetectable in animals. These lost genes encode: (i) sixteen distinct biosynthetic functions; (ii) the two ancestral eukaryotic ClpB disaggregases, Hsp78 and Hsp104, which function in the mitochondria and cytosol, respectively; and (iii) six other assorted functions. We present computational and experimental data that are consistent with a joint function for the differentially localized ClpB disaggregases, and with the possibility of a shared client/chaperone relationship between the mitochondrial Fe/S homoaconitase encoded by the lost LYS4 gene and the two ClpBs. Our analyses lead to the hypothesis that the evolution of gastrulation-based multicellularity in animals led to efficient extraction of nutrients from dietary sources, loss of natural selection for maintenance of energetically expensive biosynthetic pathways, and subsequent loss of their attendant ClpB chaperones.","doi":"10.1371/journal.pone.0117192","authors":"Erives AJ, Fassler JS","authors_abbrev":"Erives AJ et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-02-25","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.08c","SPBC4F6.17c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:35639793","title":"Elastic network modeling of cellular networks unveils sensor and effector genes that control information flow.","citation":"PLoS Comput Biol 2022 May;18(5):e1010181","abstract":"The high-level organization of the cell is embedded in indirect relationships that connect distinct cellular processes. Existing computational approaches for detecting indirect relationships between genes typically consist of propagating abstract information through network representations of the cell. However, the selection of genes to serve as the source of propagation is inherently biased by prior knowledge. Here, we sought to derive an unbiased view of the high-level organization of the cell by identifying the genes that propagate and receive information most effectively in the cell, and the indirect relationships between these genes. To this aim, we adapted a perturbation-response scanning strategy initially developed for identifying allosteric interactions within proteins. We deployed this strategy onto an elastic network model of the yeast genetic interaction profile similarity network. This network revealed a superior propensity for information propagation relative to simulated networks with similar topology. Perturbation-response scanning identified the major distributors and receivers of information in the network, named effector and sensor genes, respectively. Effectors formed dense clusters centrally integrated into the network, whereas sensors formed loosely connected antenna-shaped clusters and contained genes with previously characterized involvement in signal transduction. We propose that indirect relationships between effector and sensor clusters represent major paths of information flow between distinct cellular processes. Genetic similarity networks for fission yeast and human displayed similarly strong propensities for information propagation and clusters of effector and sensor genes, suggesting that the global architecture enabling indirect relationships is evolutionarily conserved across species. Our results demonstrate that elastic network modeling of cellular networks constitutes a promising strategy to probe the high-level organization and cooperativity in the cell.","doi":"10.1371/journal.pcbi.1010181","authors":"Acar O, Zhang S, Bahar I, Carvunis AR","authors_abbrev":"Acar O et al.","pubmed_publication_date":"May 2022","pubmed_entrez_date":"2022-05-31","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-06-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28934413","title":"Factors extending the chronological lifespan of yeast: Ecl1 family genes.","citation":"FEMS Yeast Res 2017 Nov 01;17(7)","abstract":"Ecl1 family genes are conserved among yeast, in which their overexpression extends chronological lifespan. Ecl1 family genes were first identified in the fission yeast Schizosaccharomyces pombe; at the time, they were considered noncoding RNA owing to their short coding sequence of fewer than 300 base pairs. Schizosaccharomyces pombe carries three Ecl1 family genes, ecl1+, ecl2+ and ecl3+, whereas Saccharomyces cerevisiae has one, ECL1. Their overexpression extends chronological lifespan, increases oxidative stress resistance and induces sexual development in fission yeast. A recent study indicated that Ecl1 family genes play a significant role in responding to environmental zinc or sulfur depletion. In this review, we focus on Ecl1 family genes in fission yeast and describe the relationship between nutritional depletion and cellular output, as the latter depends on Ecl1 family genes. Furthermore, we present the roles and functions of Ecl1 family genes characterized to date.","doi":"10.1093/femsyr/fox066","authors":"Ohtsuka H, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"01 Nov 2017","pubmed_entrez_date":"2017-09-22","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-09-23 00:15:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC70.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:3442824","title":"Genetic mapping of eleven spo genes essential for ascospore formation in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1986;10(6):443-7","abstract":"Sporulation-deficient mutants of the fission yeast Schizosaccharomyces pombe were isolated from a homothallic strain mutagenized with ethyl methanesulfonate. Complementation tests defined two new genetic loci (spo19 and spo20) essential for ascospore formation, in addition to the 18 known spo loci (Bresch et al. 1968). A novel mapping procedure using random spore analysis prior to tetrad analysis allowed us to map 11 spo genes. Four genes (spo3, spo15, spo19 and spo20) were mapped on chromosome I, 6 genes (spo2, spo4, spo5, spo6, spo14 and spo18) on chromosome III and 1 gene (spo13) on chromosome III. Although there was no noticeable clustering of spo genes on the chromosomes, three pairs of linked genes (spo15-spo20, spo3-spo19 and spo2-spo18) were found.","authors":"Kishida M, Shimoda C","authors_abbrev":"Kishida M et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_session_key":"b39e24367b203705","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-05-01 14:48:12","canto_approved_date":"2022-09-21 14:39:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-05 15:50:06","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16C6.14","SPBC1778.04","SPBC29A10.02","SPCC1183.12","SPAC607.10","SPAC1F3.06c","SPAC3H8.10","SPBC3H7.01","SPBC21C3.18"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2015-05-01"},{"uniquename":"EMBL:AU010033","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21773919","title":"Purification of tubulin from the fission yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2011;777:29-55","abstract":"The fission yeast Schizosaccharomyces pombe is an attractive source of tubulin for biochemical experiments as it contains few tubulin isoforms and is amenable to genetic manipulation. We describe the preparation of milligram quantities of highly purified native tubulin from S. pombe suitable for use in microtubule dynamics assays as well as structural and other biochemical studies. S. pombe cells are grown in bulk in a fermenter and then lysed using a bead mill. The soluble protein fraction is bound to anion-exchange chromatography resin by batch binding, packed in a -chromatography column and eluted by a salt gradient. The tubulin-containing fraction is ammonium sulphate precipitated to further concentrate and purify the protein. A round of high-resolution anion-exchange chromatography is carried out before a cycle of polymerisation and depolymerisation to select functional tubulin. Gel filtration is used to remove residual contaminants before a final desalting step. The purified tubulin is concentrated, and then frozen and stored in liquid nitrogen.","doi":"10.1007/978-1-61779-252-6_3","authors":"Drummond DR, Kain S, Newcombe A, Hoey C, Katsuki M, Cross RA","authors_abbrev":"Drummond DR et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-07-21","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34504165","title":"Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast.","citation":"Sci Rep 2021 Sep 09;11(1):17872","abstract":"Cell polarity and morphogenesis are regulated by the small GTPase Cdc42. Even though major advances have been done in the field during the last years, the molecular details leading to its activation in particular cellular contexts are not completely understood. In fission yeast, the β(1,3)-glucanase Eng2 is a \"moonlighting protein\" with a dual function, acting as a hydrolase during spore dehiscence, and as component of the endocytic machinery in vegetative cells. Here, we report that Eng2 plays a role in Cdc42 activation during polarized growth through its interaction with the scaffold protein Scd2, which brings Cdc42 together with its guanine nucleotide exchange factor (GEF) Scd1. eng2Δ mutant cells have defects in activation of the bipolar growth (NETO), remaining monopolar during all the cell cycle. In the absence of Eng2 the accumulation of Scd1 and Scd2 at the poles is reduced, the levels of Cdc42 activation decrease, and the Cdc42 oscillatory behavior, associated with bipolar growth in wild type cells, is altered. Furthermore, overexpression of Eng2 partially rescues the growth and polarity defects of a cdc42-L160S mutant. Altogether, our work unveils a new factor regulating the activity of Cdc42, which could potentially link the polarity and endocytic machineries.","doi":"10.1038/s41598-021-97311-6","authors":"García P, Coll PM, Del Rey F, Geli MI, Pérez P, Vázquez de Aldana CR, Encinar Del Dedo J","authors_abbrev":"García P et al.","pubmed_publication_date":"09 Sep 2021","pubmed_entrez_date":"2021-09-10","publication_year":"2021","canto_session_key":"141e7eb72b9a4c9b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-09-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23D3.10c","SPAC22H10.07"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:27683273","title":"Activation of Checkpoint Kinase Chk1 by Reactive Oxygen Species Resulting from Disruption of wat1/pop3 in Schizosaccharomyces pombe.","citation":"Genetics 2016 Dec;204(4):1397-1406","abstract":"DNA double-strand breaks are critical lesions that can lead to chromosomal aberrations and genomic instability. In response to DNA damage, Chk1, a serine/threonine kinase, is responsible for cell cycle arrest to prevent damaged cells from progressing through the cell cycle. Here, we report that the disruption of wat1, a WD repeat-containing protein, leads to the phosphorylation of Chk1. The double-deletion of chk1 and wat1 had a grave effect on the survival of fission yeast cells, and the spontaneous recombination rate was also high upon double-deletion of wat1 and chk1, as compared to the single-mutant. In the absence of wat1, the cells exhibited a high level of nuclear fragmentation that resulted in the accumulation of Rad22 yellow fluorescent protein foci. Furthermore, we show that wat1 is required for the regulation of the oxidative stress response. We observed elevated levels of reactive oxygen species (ROS) generation in wat1-null mutant that led to a high degree of propidium iodide staining at nonpermissive temperature. Based on the results presented here, we hypothesize that ROS production in wat1-null mutant cells generates DNA fragmentation that could trigger a checkpoint response and that, in the absence of checkpoint kinase Chk1, the cells exhibit severe growth defects leading to a synthetic lethal phenotype.","authors":"Ahamad N, Verma SK, Ahmed S","authors_abbrev":"Ahamad N et al.","pubmed_publication_date":"Dec 2016","pubmed_entrez_date":"2016-09-30","publication_year":"2016","canto_session_key":"94adbc82c6298e0e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-10-01 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21B10.05c","SPCC1259.13"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:SPC03900","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20526281","title":"Topoisomerase I regulates open chromatin and controls gene expression in vivo.","citation":"EMBO J 2010 Jul 07;29(13):2126-34","abstract":"DNA topoisomerases regulate the topological state of the DNA double helix and are key enzymes in the processes of DNA replication, transcription and genome stability. Using the fission yeast model Schizosaccharomyces pombe, we investigate genome wide how DNA topoisomerases I and II affect chromatin dynamics and gene expression in vivo. We show that topoisomerase I activity is directly required for efficient nucleosome disassembly at gene promoter regions. Lack of topoisomerase activity results in increased nucleosome occupancy, perturbed histone modifications and reduced transcription from these promoters. Strong correlative evidence suggests that topoisomerase I cooperates with the ATP-dependent chromatin remodeller Hrp1 in nucleosome disassembly. Our study links topoisomerase activity to the maintenance of open chromatin and regulating transcription in vivo.","doi":"10.1038/emboj.2010.109","authors":"Durand-Dubief M, Persson J, Norman U, Hartsuiker E, Ekwall K","authors_abbrev":"Durand-Dubief M et al.","pubmed_publication_date":"07 Jul 2010","pubmed_entrez_date":"2010-06-08","publication_year":"2010","canto_session_key":"52e4643f0c55be4b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12127990","title":"Hrp3, a chromodomain helicase/ATPase DNA binding protein, is required for heterochromatin silencing in fission yeast.","citation":"Biochem Biophys Res Commun 2002 Jul 26;295(4):970-4","abstract":"Hrp3, a paralog of Hrp1, is a novel member of the CHD1 (chromo-helicase/ATPase-DNA binding 1) protein family of Schizosaccharomyces pombe. Although it has been considered that CHD1 proteins are required for chromatin modifications in transcriptional regulations, little is known about their roles in vivo. In this study, we examined the effects of Hrp3 on heterochromatin silencing using several S. pombe reporter strains. The phenotypic analysis revealed that hrp3(+) is not an essential gene for cell viability. However, Hrp3 is required for transcriptional repression at silence loci of mat3. A chromatin immunoprecipitation assay showed that Hrp3 directly associates with mat3 chromatin. Thus, our results strongly suggest that Hrp3 is involved in heterochromatin silencing and plays a direct role as a chromatin remodeling factor at mat3 in vivo.","authors":"Jae Yoo E, Kyu Jang Y, Ae Lee M, Bjerling P, Bum Kim J, Ekwall K, Hyun Seong R, Dai Park S","authors_abbrev":"Jae Yoo E et al.","pubmed_publication_date":"26 Jul 2002","pubmed_entrez_date":"2002-07-20","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.01"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"EMBL:AY498547","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17933778","title":"Atomic force microscopy of DNA in solution and DNA modelling show that structural properties specify the eukaryotic replication initiation site.","citation":"Nucleic Acids Res 2007;35(20):6832-45","abstract":"The replication origins (ORIs) of Schizosaccharomyces pombe, like those in most eukaryotes, are long chromosomal regions localized within A+T-rich domains. Although there is no consensus sequence, the interacting proteins are strongly conserved, suggesting that DNA structure is important for ORI function. We used atomic force microscopy in solution and DNA modelling to study the structural properties of the Spars1 origin. We show that this segment is the least stable of the surrounding DNA (9 kb), and contains regions of intrinsically bent elements (strongly curved and inherently supercoiled DNAs). The pORC-binding site co-maps with a superhelical DNA region, where the spatial arrangement of adenine/thymine stretches may provide the binding substrate. The replication initiation site (RIP) is located within a strongly curved DNA region. On pORC unwinding, this site shifts towards the apex of the curvature, thus potentiating DNA melting there. Our model is entirely consistent with the sequence variability, large size and A+T-richness of ORIs, and also accounts for the multistep nature of the initiation process, the specificity of pORC-binding site(s), and the specific location of RIP. We show that the particular DNA features and dynamic properties identified in Spars1 are present in other eukaryotic origins.","authors":"Marilley M, Milani P, Thimonier J, Rocca-Serra J, Baldacci G","authors_abbrev":"Marilley M et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-10-16","publication_year":"2007","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22065639","title":"Cdk1 phosphorylation of the kinetochore protein Nsk1 prevents error-prone chromosome segregation.","citation":"J Cell Biol 2011 Nov 14;195(4):583-93","abstract":"Cdk1 controls many aspects of mitotic chromosome behavior and spindle microtubule (MT) dynamics to ensure accurate chromosome segregation. In this paper, we characterize a new kinetochore substrate of fission yeast Cdk1, Nsk1, which promotes proper kinetochore-MT (k-MT) interactions and chromosome movements in a phosphoregulated manner. Cdk1 phosphorylation of Nsk1 antagonizes Nsk1 kinetochore and spindle localization during early mitosis. A nonphosphorylatable Nsk1 mutant binds prematurely to kinetochores and spindle, cementing improper k-MT attachments and leading to high rates of lagging chromosomes that missegregate. Accordingly, cells lacking nsk1 exhibit synthetic growth defects with mutations that disturb MT dynamics and/or kinetochore structure, and lack of proper phosphoregulation leads to even more severe defects. Intriguingly, Nsk1 is stabilized by binding directly to the dynein light chain Dlc1 independently of the dynein motor, and Nsk1-Dlc1 forms chainlike structures in vitro. Our findings establish new roles for Cdk1 and the Nsk1-Dlc1 complex in regulating the k-MT interface and chromosome segregation.","doi":"10.1083/jcb.201105074","authors":"Chen JS, Lu LX, Ohi MD, Creamer KM, English C, Partridge JF, Ohi R, Gould KL","authors_abbrev":"Chen JS et al.","pubmed_publication_date":"14 Nov 2011","pubmed_entrez_date":"2011-11-09","publication_year":"2011","canto_session_key":"2725f4d76602a0b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2018-08-16 16:00:29","canto_approved_date":"2024-04-30 05:41:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-04 14:09:27","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.02c","SPAC3G9.01","SPAC1783.03","SPBC2F12.13","SPAC1805.08","SPAC1782.09c","SPBC11B10.09","SPCC320.13c","SPAC27F1.04c","SPAC890.02c","SPBC106.01","SPAC1687.20c","SPCC1020.02"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2018-08-16"},{"uniquename":"PMID:21965528","title":"Aurora promotes cell division during recovery from TOR-mediated cell cycle arrest by driving spindle pole body recruitment of Polo.","citation":"J Cell Sci 2011 Oct 15;124(Pt 20):3441-9","abstract":"The coordination of cell division and growth in response to changes in nutrient supply is mediated by TOR signalling. In fission yeast, increased nutrient provision transiently delays mitotic onset without affecting growth. The result is an increase in cell size at division. We find that this block to cell division relies upon TOR and MAPK signalling and that mitotic entry during recovery from this block is regulated by the Aurora kinase Ark1. We show that Ark1 phosphorylation of polo kinase Plo1 within the linker region between the kinase domain and polo boxes drives Plo1 onto the spindle poles where it promotes mitosis. Interestingly, the use of Ark1 to phosphorylate Plo1 and promote mitotic entry is dependent on the environment.","doi":"10.1242/jcs.083683","authors":"Hálová L, Petersen J","authors_abbrev":"Hálová L et al.","pubmed_publication_date":"15 Oct 2011","pubmed_entrez_date":"2011-10-04","publication_year":"2011","canto_session_key":"70f8ac4a3ff0e8c5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-22 17:06:51","canto_approved_date":"2026-06-02 16:46:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-27 14:16:38","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPAC23C11.16","SPCC320.13c","SPBC30D10.10c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-09-22"},{"uniquename":"PMID:31294478","title":"Senataxin homologue Sen1 is required for efficient termination of RNA polymerase III transcription.","citation":"EMBO J 2019 Aug 15;38(16):e101955","abstract":"R-loop disassembly by the human helicase Senataxin contributes to genome integrity and to proper transcription termination at a subset of RNA polymerase II genes. Whether Senataxin also contributes to transcription termination at other classes of genes has remained unclear. Here, we show that Sen1, one of two fission yeast homologues of Senataxin, promotes efficient termination of RNA polymerase III (RNAP3) transcription in vivo. In the absence of Sen1, RNAP3 accumulates downstream of RNAP3-transcribed genes and produces long exosome-sensitive 3'-extended transcripts. Importantly, neither of these defects was affected by the removal of R-loops. The finding that Sen1 acts as an ancillary factor for RNAP3 transcription termination in vivo challenges the pre-existing view that RNAP3 terminates transcription autonomously. We propose that Sen1 is a cofactor for transcription termination that has been co-opted by different RNA polymerases in the course of evolution.","doi":"10.15252/embj.2019101955","authors":"Rivosecchi J, Larochelle M, Teste C, Grenier F, Malapert A, Ricci EP, Bernard P, Bachand F, Vanoosthuyse V","authors_abbrev":"Rivosecchi J et al.","pubmed_publication_date":"15 Aug 2019","pubmed_entrez_date":"2019-07-12","publication_year":"2019","canto_session_key":"b843706c830e7b7d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"VANOOSTHUYSE","canto_first_approved_date":"2019-09-18 09:42:57","canto_approved_date":"2021-05-14 14:08:59","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-09-05 11:19:29","canto_added_date":"2019-07-13 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":45,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"VANOOSTHUYSE","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18.07","SPCTRNAASN.06","SPBC3B9.07c","SPAC1834.03c","SPBTRNAARG.05","SPAC22A12.01c","SPBC1289.07c","SPCTRNAMET.07","SPBC1815.01","SPCC794.09c","SPBC14F5.04c","SPSNRNA.06","SPBTRNATYR.04","SPAC1F8.07c","SPCC1739.13","SPCTRNASER.09","SPAC27E2.11c","SPRRNA.37","SPAC1071.10c","SPBC26H8.10","SPAC6G9.10c","SPAC4G9.08c","SPCC13B11.01","SPAC4G9.02","SPNCRNA.98","SPRRNA.05","SPRRNA.06","SPRRNA.20","SPATRNAPRO.02","SPBC29A10.10c","SPCC330.13","SPCTRNATHR.10","SPBC336.06c","SPBC19C2.07","SPAC1783.05","SPCTRNAARG.10","SPBC32F12.11","SPBC2G5.07c","SPAPB1E7.03","SPBC651.08c","SPBC839.12"],"gene_count":41,"ltp_gene_count":9,"approved_date":"2019-09-18"},{"uniquename":"PMID:8757394","title":"Novel alleles of cdc13 and cdc2 isolated as suppressors of mitotic catastrophe in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1996 Jul 26;251(6):635-46","abstract":"Cell cycle control in the fission yeast Schizosaccharomyces pombe involves interplay amongst a number of regulatory molecules, including the cdc2, cdc13, cdc25, wee1, and mik1 gene products. Cdc2, Cdc13, and Cdc25 act as positive regulators of cell cycle progression at the G2/M boundary, while Wee1 and Miky1 play a negative regulatory role. Here, we have screened for suppressors of the lethal premature entry into mitosis, termed mitotic catastrophe, which results from simultaneous loss of function of both Wee1 and Mik1. Through such a screen, we hoped to identify additional components of the cell cycle regulatory network, and/or G2/M-specific substrates of Cdc2. Although we did not identify such molecules, we isolated a number of alleles of both cdc2 and cdc13, including a novel wee allele of cdc2, cdc2-5w. Here, we characterize cdc2-5w and two alleles of cdc13, which have implications for the understanding of details of the interactions amongst Cdc2, Cdc13, and Wee1.","authors":"Berry LD, Gould KL","authors_abbrev":"Berry LD et al.","pubmed_publication_date":"26 Jul 1996","pubmed_entrez_date":"1996-07-26","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28876998","title":"Meiosis-specific localization of the exocytic Rab Ypt2 in fission yeast.","citation":"Small GTPases 2020 Mar;11(2):146-154","abstract":"Fission yeast Ypt2, an orthologue of the mammalian small GTPase Rab8, is responsible for post-Golgi membrane trafficking. During meiosis, Ypt2 localizes at the spindle pole body (SPB), where it regulates  de novo  biogenesis of the spore plasma membrane. Recruitment of Ypt2 to the SPB is dependent on its meiosis-specific GDP/GTP exchange factor (GEF), the SPB-resident protein Spo13. Here we have examined the SPB recruitment of Ypt2 by Spo13. The GEF activity of Spo13 was required, but not essential for recruitment. Furthermore, Ypt2 recruitment was regulated in a meiosis-specific manner and partially regulated by the nuclear Dbf2-related (NDR) kinase Sid2, indicating the existence of a novel regulatory mechanism for localization of Rab GTPases during meiosis.","doi":"10.1080/21541248.2017.1356425","authors":"Imada K, Nakamura T","authors_abbrev":"Imada K et al.","pubmed_publication_date":"Mar 2020","pubmed_entrez_date":"2017-09-07","publication_year":"2020","canto_session_key":"ba747e640ba07638","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-09-08 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPCC417.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:40057225","title":"Yeast Knowledge Graphs Database for Exploring Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"J Mol Biol 2025 Mar 06;:169072","abstract":"Biomedical literature contains an extensive wealth of information on gene and protein function across various biological processes and diseases. However, navigating this vast and often restricted-access data can be challenging, making it difficult to extract specific insights efficiently. In this study, we introduce a high-throughput pipeline that leverages OpenAI's Generative Pre-Trained Transformer Model (GPT) to automate the extraction and analysis of gene function information. We applied this approach to 84,427 publications on Saccharomyces cerevisiae and 6,452 publications on Schizosaccharomyces pombe, identifying 3,432,749 relationships for budding yeast and 421,198 relationships for S. pombe. This resulted in a comprehensive, searchable online Knowledge Graph database, available at yeast.connectome.tools and spombe.connectome.tools, which offers users extensive access to various interactions and pathways. Our analysis underscores the power of integrating artificial intelligence with bioinformatics, as demonstrated through key insights into important nodes like Hsp104 and Atg8 proteins. This work not only facilitates efficient data extraction in yeast research but also presents a scalable model for similar studies in other biological systems.","doi":"10.1016/j.jmb.2025.169072","authors":"Kumar MR, Arulprakasam KR, Kutevska AN, Mutwil M, Thibault G","authors_abbrev":"Kumar MR et al.","pubmed_publication_date":"06 Mar 2025","pubmed_entrez_date":"2025-03-08","publication_year":"2025","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2025-03-10 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41796983","title":"Engineering and Characterization of a Fluorescent Fission Yeast Arp2/3 Complex for Single Molecule Mechanistic Investigations.","citation":"Cytoskeleton (Hoboken) 2026 Mar 08;","abstract":"Arp2/3 complex is a seven-component protein complex that facilitates the assembly of branched actin filament networks by binding to pre-existing \"mother\" actin filaments and initiating the nucleation of new branched \"daughter\" filaments. Arp2/3 complex must be activated by a nucleation promoting factor such as the WASP/Scar protein family. The direct visualization of Arp2/3 complex during the branching pathway is critical to elucidate the underlying molecular mechanisms under diverse assembly conditions. Here we have successfully purified and fluorescently labeled a fission yeast Arp2/3 complex that is activated by different classes of fission yeast nucleation promoting factors. We visualized Arp2/3 complex actin filament binding and branch formation in two-color TIRF microscopy assays, revealing that a single complex of Arp2/3 complex nucleates a branched actin filament ~2 s after binding. We have therefore generated an important reagent that can help elucidate a clearer understanding of the pathway and regulation of Arp2/3 complex-mediated actin filament branch formation.","doi":"10.1002/cm.70120","authors":"Anderson CA, O'Connell ME, Homa KE, Suarez C, James ML, Baboolall KD, Zsolnay V, Sirotkin V, Kovar DR","authors_abbrev":"Anderson CA et al.","pubmed_publication_date":"08 Mar 2026","pubmed_entrez_date":"2026-03-09","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-10 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30228203","title":"From powerhouse to processing plant: conserved roles of mitochondrial outer membrane proteins in tRNA splicing.","citation":"Genes Dev 2018 Oct 01;32(19-20):1309-1314","abstract":"The mitochondrial cytoplasmic surface serves as a processing site for numerous RNAs from budding yeast to metazoans. We report that budding yeast mitochondrial outer membrane (MOM) proteins that are subunits of the translocase of the outer mitochondrial membrane (Tom70 and Tom 22) and sorting and assembly machinery (Sam37) are required for efficient pretransfer RNA (pre-tRNA) splicing. Defective pre-tRNA splicing in MOM mutants is due not to loss of respiratory metabolism but instead inefficient targeting/tethering of tRNA splicing endonuclease (SEN) subunits to mitochondria.  Schizosaccharomyces pombe  SEN subunits also localize to mitochondria, and Tom70 is required for this localization and pre-tRNA splicing. Thus, the role of MOM protein in targeting/tethering SEN subunits to mitochondria has been conserved for >500 million years.","doi":"10.1101/gad.316257.118","authors":"Wan Y, Hopper AK","authors_abbrev":"Wan Y et al.","pubmed_publication_date":"01 Oct 2018","pubmed_entrez_date":"2018-09-20","publication_year":"2018","canto_session_key":"56d74acb634ee730","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-04-02 10:13:39","canto_approved_date":"2025-07-03 10:46:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-02 10:00:24","canto_added_date":"2018-09-21 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC613.09","SPAPB17E12.07c","SPAC6B12.12","SPBC19C7.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2025-04-02"},{"uniquename":"PMID:27630265","title":"The exocytic Rabs Ypt3 and Ypt2 regulate the early step of biogenesis of the spore plasma membrane in fission yeast.","citation":"Mol Biol Cell 2016 Nov 01;27(21):3317-3328","abstract":"During fission yeast sporulation, a membrane compartment called the forespore membrane (FSM) is newly formed on the spindle pole body (SPB). The FSM expands by membrane vesicle fusion, encapsulates the daughter nucleus resulting from meiosis, and eventually matures into the plasma membrane of the spore. Although many of the genes involved in FSM formation have been identified, its molecular mechanism is not fully understood. Here a genetic screen for sporulation-deficient mutations identified Ypt3, a Rab-family small GTPase known to function in the exocytic pathway. The ypt3-ki8 mutant showed defects in both the initiation of FSM biogenesis and FSM expansion. We also show that a mutation in Ypt2, another Rab protein that may function in the same pathway as Ypt3, compromises the initiation of FSM formation. As meiosis proceeds, both GFP-Ypt3 and GFP-Ypt2 are observed at the SPB and then relocalize to the FSM. Their localizations at the SPB precede FSM formation and depend on the meiotic SPB component Spo13, a putative GDP/GTP exchange factor for Ypt2. Given that Spo13 is essential for initiating FSM formation, these results suggest that two exocytic Rabs, Ypt3 and Ypt2, regulate the initiation of FSM formation on the SPB in concert with Spo13.","authors":"Imada K, Nakamura T","authors_abbrev":"Imada K et al.","pubmed_publication_date":"01 Nov 2016","pubmed_entrez_date":"2016-09-16","publication_year":"2016","canto_session_key":"dd3170869113df7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Taro Nakamura","canto_first_approved_date":"2017-03-30 05:10:01","canto_approved_date":"2026-06-13 15:06:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-06 12:21:41","canto_added_date":"2016-09-17 00:15:11","annotation_curators":[{"name":"Taro Nakamura","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.03","SPCC1183.12","SPAC6G9.04","SPCC970.09","SPAC6G9.11","SPAC23C4.10","SPAC9E9.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-03-30"},{"uniquename":"PMID:6613166","title":"[Gene-enzyme relationships of the arom aggregate of Schizosaccharomyces pombe].","citation":"Z Allg Mikrobiol 1983;23(4):219-24","abstract":"The gene-enzyme relationships of the arom multienzyme complex of Schizosaccharomyces pombe that catalyzes steps two through six in the prechorismate polyaromatic amino acid biosynthetic pathway have been studied. The various mutants were subjected to biochemical analysis by direct enzymic assays. These studies have established that aro-3A, aro-3B, aro-3C, aro-3D, and aro-3E mutants lack, respectively, the enzymic activities 5-dehydroquinate synthase, 5-dehydroquinase, shekimate kinase, 3-enolpyruvylshikimate 5-phosphate synthase, and shikimate: NADP oxidoreductase. In S. pombe lack enzymic activities for the inducible quinate catabolic pathway. The functional significance of the arom aggregate is discussed.","authors":"Bode R","authors_abbrev":"Bode R","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-01-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25240800","title":"The RNA exosome promotes transcription termination of backtracked RNA polymerase II.","citation":"Nat Struct Mol Biol 2014 Oct;21(10):919-26","abstract":"The exosome is an RNA-decay complex that constantly monitors transcription and contributes to post-transcriptional turnover of faulty mRNAs. Yet how nuclear RNA surveillance by the exosome is coordinated with transcription is still unknown. Here we show that the RNA exosome of Schizosaccharomyces pombe can target the transcription machinery by terminating transcription events associated with paused and backtracked RNA polymerase II (RNAPII); this is contrary to the notion that the exosome acts exclusively on RNAs that have been released by RNAPII. Our data support a mechanism by which RNAPII backtracking provides a free RNA 3' end for the core exosome, which results in transcription termination with concomitant degradation of the associated transcript. These findings uncover a mechanism of cotranscriptional RNA surveillance whereby termination of transcription by the exosome prevents formation of aberrant readthrough RNAs and transcriptional interference at neighboring genes.","doi":"10.1038/nsmb.2893","authors":"Lemay JF, Larochelle M, Marguerat S, Atkinson S, Bähler J, Bachand F","authors_abbrev":"Lemay JF et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-09-22","publication_year":"2014","canto_session_key":"f2202f3e99350d80","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Marc Larochelle","canto_first_approved_date":"2018-04-04 16:10:40","canto_approved_date":"2024-04-03 16:15:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-04-03 14:09:08","canto_added_date":"2014-09-24 00:15:30","annotation_curators":[{"name":"Marc Larochelle","community_curator":true,"annotation_count":48,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.12c","SPAC20H4.03c","SPAC2F7.14c","SPAC17H9.02","SPSNORNA.32","SPBC26H8.10","SPAC1071.10c","SPCC1442.14c","SPCC1840.11","SPCC1739.07","SPSNORNA.35","SPBP35G2.08c","SPAC3G9.10c","SPAP8A3.04c","SPAC12G12.13c","SPAC6F12.16c"],"gene_count":16,"ltp_gene_count":8,"approved_date":"2018-04-04"},{"uniquename":"PMID:1549179","title":"The wee1 protein kinase is required for radiation-induced mitotic delay.","citation":"Nature 1992 Mar 26;356(6367):353-5","abstract":"Cellular feedback or 'checkpoint' mechanisms maintain the order of completion of essential, cell-cycle related functions. In the budding yeast, for example, the RAD9 gene product is required to delay progression into mitosis in response to DNA damage. Similarly, in fission yeast, the cdc25 and cdc2 gene products influence the ability of cells to delay mitosis in response to the inhibition of DNA synthesis. Because these two checkpoint controls regulate the same event, mitosis, we observed the effect of gamma-irradiation on cell cycle progression in fission yeast, to test whether the two controls require the same cell-cycle regulatory elements. We show that gamma-radiation-induced mitotic delay requires functional wee1 protein kinase but does not seem to involve the cdc25 pathway. Mitotic delay in response to DNA damage is thus distinct from the delay induced by inhibition of DNA synthesis, which involves cdc25 but is not dependent on wee1.","authors":"Rowley R, Hudson J, Young PG","authors_abbrev":"Rowley R et al.","pubmed_publication_date":"26 Mar 1992","pubmed_entrez_date":"1992-03-26","publication_year":"1992","canto_session_key":"e5a15cdcd4aa21c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-04 10:51:42","canto_approved_date":"2020-06-24 08:45:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-07 10:43:56","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPAC644.06c","SPBC660.14","SPAC24H6.05","SPCC18B5.03","SPBC1A4.02c","SPBC649.05","SPBC11B10.09"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2016-04-04"},{"uniquename":"PMID:7275933","title":"Isolation, properties, function, and regulation of endo-(1 leads to 3)-beta-glucanases in Schizosaccharomyces pombe.","citation":"J Bacteriol 1981 Sep;147(3):1085-94","abstract":"Cell-free extracts, membranous fractions, and cell wall preparations from Schizosaccharomyces pombe were examined for the presence of (1 --> 3)-beta-, (1 --> 3)-alpha-, and (1 --> 6)-beta-glucanase activities. The various glucanases were assayed in cells at different growth stages. Only (1 --> 3)-beta-glucanase activity was found, and this was associated with the cell wall fraction. Chromatographic fractionation of the crude enzyme revealed two endo-(1 --> 3)-beta-glucanases, designated as glucanase I and glucanase II. Glucanase I consisted of two subunits of molecular weights 78,500 and 82,000, and glucanase II was a single polypeptide of 75,000. Although both enzymes had similar substrate specificities and similar hydrolytic action on laminarin, glucanase II had much higher hydrolytic activity on isolated cell walls of S. pombe. On the basis of differential lytic activity on cell walls, glucanase II was shown to be present in conjugating cells and highest in sporulating cells. Glucanase II appeared to be specifically involved in conjugation and sporulation since vegetative cells and nonconjugating and nonsporulating cells did not contain this enzyme. The appearance of glucanase II in conjugating cells may be due to de novo enzyme synthesis since no activation could be demonstrated by combining extracts from vegetative and conjugating cells. Increased glucanase activity occurred when walls from conjugating cells were combined with walls from sporulating cells. Studies with trypsin and proteolytic inhibitors suggest that glucanase II exists as a zymogen in conjugating cells. A temperature-sensitive mutant of S. pombe was isolated which lysed at 37 degrees C. Glucanase activity was higher in vegetative cells held at 37 degrees C than cells held at 25 degrees C. Unlike the wild-type strain, this mutant contained glucanase II activity during vegetative growth and may be a regulatory mutant.","authors":"Reichelt BY, Fleet GH","authors_abbrev":"Reichelt BY et al.","pubmed_publication_date":"Sep 1981","pubmed_entrez_date":"1981-09-01","publication_year":"1981","canto_session_key":"29ca53761f769688","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-06-11 22:54:29","canto_approved_date":"2018-06-11 22:54:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-11 22:54:17","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23D3.10c","SPAC821.09"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2018-06-11"},{"uniquename":"EMBL:BK005597","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC12B10.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23530189","title":"The mitochondrial unfolded protein response activator ATFS-1 protects cells from inhibition of the mevalonate pathway.","citation":"Proc Natl Acad Sci U S A 2013 Apr 09;110(15):5981-6","abstract":"Statins are cholesterol-lowering drugs that inhibit 3-hydroxy-3-methyl-glutaryl-CoA (HMG-CoA) reductase, the rate-limiting enzyme in the synthesis of cholesterol via the mevalonate pathway. This pathway also produces coenzyme Q (a component of the respiratory chain), dolichols (important for protein glycosylation), and isoprenoids (lipid moieties responsible for the membrane association of small GTPases). We previously showed that the nematode Caenorhabditis elegans is useful to study the noncholesterol effects of statins because its mevalonate pathway lacks the sterol synthesis branch but retains all other branches. Here, from a screen of 150,000 mutagenized genomes, we isolated four C. elegans mutants resistant to statins by virtue of gain-of-function mutations within the first six amino acids of the protein ATFS-1, the key regulator of the mitochondrial unfolded protein response that includes activation of the chaperones HSP-6 and HSP-60. The atfs-1 gain-of-function mutants are also resistant to ibandronate, an inhibitor of an enzyme downstream of HMG-CoA reductase, and to gliotoxin, an inhibitor acting on a subbranch of the pathway important for protein prenylation, and showed improved mitochondrial function and protein prenylation in the presence of statins. Additionally, preinduction of the mitochondrial unfolded protein response in wild-type worms using ethidium bromide or paraquat triggered statin resistance, and similar observations were made in Schizosaccharomyces pombe and in a mammalian cell line. We conclude that statin resistance through maintenance of mitochondrial homeostasis is conserved across species, and that the cell-lethal effects of statins are caused primarily through impaired protein prenylation that results in mitochondria dysfunction.","doi":"10.1073/pnas.1218778110","authors":"Rauthan M, Ranji P, Aguilera Pradenas N, Pitot C, Pilon M","authors_abbrev":"Rauthan M et al.","pubmed_publication_date":"09 Apr 2013","pubmed_entrez_date":"2013-03-27","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16085490","title":"Distinct nuclear and cytoplasmic functions of the S. pombe Cdc14-like phosphatase Clp1p/Flp1p and a role for nuclear shuttling in its regulation.","citation":"Curr Biol 2005 Aug 09;15(15):1384-9","abstract":"Cdc14-like phosphatases regulate a variety of cell cycle events by dephosphorylating CDK sites. Their cell cycle-dependent changes in localization may be important to carry out distinct functions. Work in budding and fission yeast suggested that Cdc14-like phosphatases are inhibited by nucleolar sequestration. In S. cerevisiae, Cdc14p is released from the nucleolus by the FEAR network and Cdk1, whereas the S. pombe CDC14-like phosphatase Clp1p (also known as Flp1p) is released at mitotic entry by an unknown mechanism. The mitotic exit network (MEN) in S. cerevisiae and its homologous network, the septation initiation network (SIN), in S. pombe act through an unknown mechanism to keep the phosphatase out of the nucleolus in late mitosis. SIN-dependent cytoplasmic maintenance of Clp1p is thought to be essential for the cytokinesis checkpoint, which blocks further rounds of nuclear division until cytokinesis is completed. By targeting Clp1p to the nucleus or the cytoplasm, we demonstrate distinct functions for these pools of Clp1p in chromosome segregation and cytokinesis, respectively. Our results further suggest that the SIN does not keep Clp1p out of the nucleolus by regulating nucleolar affinity, as proposed for S. cerevisiae Cdc14p, but instead, Clp1p may be regulated by nuclear import/export.","authors":"Trautmann S, McCollum D","authors_abbrev":"Trautmann S et al.","pubmed_publication_date":"09 Aug 2005","pubmed_entrez_date":"2005-08-09","publication_year":"2005","canto_session_key":"5f6afd655a42fd4b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.14","SPAC1782.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:23442136","title":"Dynamics and stability: epigenetic conversions in position effect variegation.","citation":"Biochem Cell Biol 2013 Feb;91(1):6-13","abstract":"Position effect variegation (PEV) refers to quasi-stable patterns of gene expression that are observed at specific loci throughout the genomes of eukaryotes. The genes subjected to PEV can be completely silenced or fully active. Stochastic conversions between these 2 states are responsible for the variegated phenotypes. Positional variegation is used by human pathogens (Trypanosoma, Plasmodium, and Candida) to evade the immune system or adapt to the host environment. In the yeasts Saccharomyces cerevisiae and Saccharomyces pombe, telomeric PEV aids the adaptation to a changing environment. In metazoans, similar epigenetic conversions are likely to accompany cell differentiation and the setting of tissue-specific gene expression programs. Surprisingly, we know very little about the mechanisms of epigenetic conversions. In this article, earlier models on the nature of PEV are revisited and recent advances on the dynamic nature of chromatin are reviewed. The normal dynamic histone turnover during transcription and DNA replication and its perturbation at transcription and replication pause sites are discussed. It is proposed that such perturbations play key roles in epigenetic conversions and in PEV.","doi":"10.1139/bcb-2012-0048","authors":"Yankulov K","authors_abbrev":"Yankulov K","pubmed_publication_date":"Feb 2013","pubmed_entrez_date":"2013-02-28","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5413678","title":"Characterization of ICR-170-induced mutations in Schizosaccharomyces pombe.","citation":"Mutat Res 1970 Feb;9(2):199-212","abstract":"","authors":"Munz P, Leupold U","authors_abbrev":"Munz P et al.","pubmed_publication_date":"Feb 1970","pubmed_entrez_date":"1970-02-01","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14665462","title":"Sla1, a Schizosaccharomyces pombe homolog of the human La protein, induces ectopic meiosis when its C terminus is truncated.","citation":"Eukaryot Cell 2003 Dec;2(6):1274-87","abstract":"Sla1 is a Schizosaccharomyces pombe homolog of the human La protein. La proteins are known to be RNA-binding proteins that bear conserved RNA recognition motifs (La and RRMs), but their biological functions still have not been fully resolved. In this study, we show that the S. pombe La homolog (Sla1) is involved in regulating sexual development. Sla1 truncated in the C terminus (Sla1DeltaC) induced ectopic sporulation in the ras1Delta strain and several other sporulation-deficient mutants. The C terminus contains a nuclear localization signal. While full-length Sla1 localizes in the nucleus, Sla1DeltaC is found throughout the cell, suggesting the cytoplasmic localization of Sla1DeltaC is involved in its sporulation-inducing activity. Further deletion analysis of Sla1 indicated that a small region (35 amino acids) that includes a portion of RRM2 is sufficient to induce sporulation. The La motif (RRM1) is not involved in this activity. Strikingly, Sla1DeltaC induced haploid meiosis in a heterothallic strain, similar to the pat1-114 or mei2-SATA mutation. Sla1DeltaC induced sporulation in a mei3 disruptant but not in a mei2 disruptant, indicating that Sla1DeltaC requires Mei2 to induce haploid meiosis. Deletion of the chromosomal sla1 gene lowered the temperature sensitivity of the pat1-114 mutant. Two-hybrid analysis indicated that Pat1 interacts with Sla1DeltaC but not full-length Sla1. Thus, Sla1DeltaC may block Pat1 activity. This block would remove the inhibition on Mei2, which would then drive the cell into haploid meiosis. Finally, Sla1 was degraded prior to the start of meiosis when we monitored Sla1 in cells in which meiosis was synchronously induced. The ability of truncated Sla1 to induce ectopic meiosis represents a very novel function that has hitherto not been suspected for the La family of proteins.","authors":"Tanabe K, Ito N, Wakuri T, Ozoe F, Umeda M, Katayama S, Tanaka K, Matsuda H, Kawamukai M","authors_abbrev":"Tanabe K et al.","pubmed_publication_date":"Dec 2003","pubmed_entrez_date":"2003-12-11","publication_year":"2003","canto_session_key":"f45b0b374b31905c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-03 08:19:19","canto_approved_date":"2024-04-04 14:40:23","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-01-12 12:39:12","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPAC57A10.10c","SPAC31G5.09c","SPBC1D7.05","SPAC1D4.13","SPAC24B11.06c","SPBC119.04","SPAC57A10.11c","SPBC19C2.05"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2015-06-03"},{"uniquename":"PMID:9714741","title":"A Schizosaccharomyces pombe gene encoding a novel polypeptide with a predicted alpha-helical rod structure found in the myosin and intermediate-filament families of proteins.","citation":"Biochim Biophys Acta 1998 Jul 30;1399(1):67-72","abstract":"We have identified a Schizosaccharomyces pombe gene encoding a 461 amino acid polypeptide containing a predicted alpha-helical rod domain found in filamentous proteins. This gene, here designated noc1, is located immediately upstream from cnx1, the gene encoding the S. pombe homologue of mammalian calnexin, an endoplasmic reticulum chaperone [M. Jannatipour, L.A. Rokeach, J. Biol. Chem. 270 (1995) 4845-4853.]. Transcription of noc1 is divergent from that of cnx1. Northern blot analysis identified a single mRNA of approx. 2 kb whose expression was increased by heat shock and growth in the presence of beta-mercaptoethanol and 2-deoxyglucose.","authors":"Jannatipour M, Rokeach LA","authors_abbrev":"Jannatipour M et al.","pubmed_publication_date":"30 Jul 1998","pubmed_entrez_date":"1998-08-26","publication_year":"1998","canto_session_key":"576c2b46e288abd3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-29 21:29:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 21:05:16","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.12"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-04-29"},{"uniquename":"PMID:36981264","title":"Activity of Binary Combinations of Natural Phenolics and Synthetic Food Preservatives against Food Spoilage Yeasts.","citation":"Foods 2023 Mar 22;12(6)","abstract":"Natural compounds are a suitable alternative to synthetic food preservatives due to their natural origin and health-promoting properties. In the current study, phenolic-phenolic and phenolic-synthetic combinations were tested for their antibiofilm formation, anti-planktonic growth, and anti-adhesion properties against  Debaryomyces hansenii ,  Wickerhamomyces anomalus  (formerly  Pichia anomala ),  Schizosaccharomyces pombe , and  Saccharomyces cerevisiae . The phenolics were vanillin and cinnamic acid, while the synthetic preservatives were sodium benzoate, potassium sorbate, and sodium diacetate. The vanillin-cinnamic acid combination had synergistic effect in all the tested yeasts for the biofilm inhibition with a fractional inhibitory concentration index (FICI) of ≤0.19 for  W. anomalus , 0.25 for  S. pombe , 0.31 for  S .  cerevisiae , and 0.5 for  D. hansenii . Most of the phenolic-synthetic combinations had indifferent interaction regarding biofilm formation. The vanillin-cinnamic acid combination also had higher activity against spoilage yeasts adhesion on the abiotic surface and planktonic growth compared to the phenolic-synthetic combinations. For the phenolic-synthetic anti-planktonic activity, synergistic interaction was present in all the vanillin-synthetic combinations in  S. pombe , vanillin-sodium benzoate and vanillin-potassium sorbate in  S. cerevisiae , vanillin-sodium benzoate in  W. anomalus , and cinnamic acid-sodium diacetate in  S. pombe . These results suggest a novel antimicrobial strategy that may broaden the antimicrobial spectrum and reduce compound toxicity against food spoilage yeasts.","doi":"10.3390/foods12061338","authors":"Kimani BG, Takó M, Veres C, Krisch J, Papp T, Kerekes EB, Vágvölgyi C","authors_abbrev":"Kimani BG et al.","pubmed_publication_date":"22 Mar 2023","pubmed_entrez_date":"2023-03-29","publication_year":"2023","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2023-03-30 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17984966","title":"Transcription and RNAi in heterochromatic gene silencing.","citation":"Nat Struct Mol Biol 2007 Nov;14(11):1041-8","abstract":"Recent findings have challenged the longstanding belief that heterochromatin is an inert and transcriptionally inactive structure. Studies in organisms ranging from fission yeast to animals have found that noncoding RNAs transcribed from heterochromatic DNA repeats function in the assembly and function of heterochromatin. In this review, we discuss the roles of RNA and RNA turnover in mechanisms that mediate heterochromatin assembly and keep heterochromatic domains silent.","authors":"Bühler M, Moazed D","authors_abbrev":"Bühler M et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-11-07","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12653963","title":"The small GTPase Rho4 is involved in controlling cell morphology and septation in fission yeast.","citation":"Genes Cells 2003 Apr;8(4):357-70","abstract":"Rho family small GTPases have been shown to be involved in various cellular activities, including the organization of actin cytoskeleton in eukaryotic cells. There are six rho genes in the fission yeast Schizosaccharomyces pombe. Cdc42 is known to control the polarity of the cell. Rho1, Rho2 and Rho3 play important roles in controlling cell shape and septation. On the other hand, Rho4 and Rho5 have not yet been characterized. Here we report the function of rho4+ in fission yeast.\nGene disruption revealed that rho4+ is not essential for cell growth. However, rho4-null cells were abnormally elongated and had multiple septa of irregular shape at 37 degrees C. In these cells, F-actin patches were randomly localized all over the cell periphery, and cytoplasmic microtubules (MTs) were misoriented. On the other hand, the exogenous expression of a constitutively active Rho4-G23V or Rho4-Q74L in wild-type cells induced depolarization of F-actin patches and cytoplasmic MTs. Rho4 was localized to the cell periphery during interphase and septum during mitosis. Both the binding of GTP and isoprenylation of its C-terminus were necessary for the localization. Furthermore, the localization of Rho4 was likely to be controlled by Rho GAP and Rho GDI.\nRho4 may control cell morphogenesis and septation by regulating both the actin cytoskeleton and cytoplasmic MTs.","authors":"Nakano K, Mutoh T, Arai R, Mabuchi I","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-03-26","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.04","SPBC26H8.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:14008","title":"Study of the role of puring phosphoribosyltransferases in the uptake of adenine and guanine by Schizosaccharomyces pombe cells.","citation":"Eur J Biochem 1977 Feb 15;73(1):99-105","abstract":"1. In the yeast Schizosaccharomyces pombe 972h-, the uptake rate of both adenine and guanine is related to variations in the specific activity of the corresponding phosphoribosyltransferases during the growth of the culture. Furthermore, the mutant strains dap 1, devoid of adenine phosphoribosyltransferase activity, and pur 1, devoid of guanine phosphoribosyltransferase activity have a lowered uptake rate of adenine and guanine respectively, along with an increased apparent Km value for these purines in comparison to the wild-type 972h. 2. The uptake rate of the purines is strongly dependent on the pH of the uptake medium in 972h- as well as in the strains dap 1 and pur 1, the optimum being between pH4 and pH5. 3. A new method of extraction of 5-phosphoribosyl-1-pyrophosphate from the yeast has been devised. Important fluctuations of the P-Rib-P2 pool were measured in S. pombe at different stages of growth, the maximum taking place at the start of the exponential phase, whereas no variations in the specific activity of the P-Rib-P2 synthetase could be observed during the growth. The P-Rib-P2 intracellular content in the mutants devoid of purine phosphoribosyltransferases, namely pur 1, dap 1 and pur 1, dap 1, was increased up to 5-fold as compared to the wild-type strain. 4. The effect of intracellular concentrations of P-Rib-P2, a substrate for phosphoribosyltransferases, on the uptake rate of purines has been studied: addition of formycin to the growth medium lowered simultaneously the P-Rib-P2 intracellular content and the uptake of adenine and guanine. 5. Although our results demonstrate the activating effect of phosphoribosyltransferase activities on the uptake of adenine and guanine, they do not support the hypothesis of a 'group translocation' mechanism.","authors":"Housset P, Nagy M","authors_abbrev":"Housset P et al.","pubmed_publication_date":"15 Feb 1977","pubmed_entrez_date":"1977-02-15","publication_year":"1977","canto_session_key":"cc0a2203f689cfc8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-16 18:01:44","canto_approved_date":"2023-01-26 11:50:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-30 16:49:33","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.15","SPAC23C11.13c","SPBC405.01","SPAC23A1.03","SPBC1683.02","SPAC4H3.10c"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2014-12-16"},{"uniquename":"PMID:16880212","title":"SUMO-binding motifs mediate the Rad60-dependent response to replicative stress and self-association.","citation":"J Biol Chem 2006 Sep 22;281(38):27973-81","abstract":"In fission yeast, the replication checkpoint is enforced by the kinase Cds1 (human Chk2), which regulates both cell cycle progression and DNA repair factors to ensure that the genome is faithfully duplicated prior to mitosis. Cds1 contains a forkhead-associated domain that mediates its interaction with phosphorylated residues in target proteins. One target of Cds1 is the essential nuclear protein Rad60, which contains the unique structural feature of tandem SUMO homology domains at its C terminus. Hypomorphic mutants of Rad60 cause profound defects in DNA repair and replication stress tolerance. To explore the physiological significance of the Cds1-Rad60 interaction, we have examined the phosphorylation of Rad60 by Cds1 in vitro and the in vivo phosphorylation of Rad60 in response to replication blocks. We find that the N terminus but not the SUMO-like domain of Rad60 is phosphorylated in both conditions. Three important Rad60 phosphorylation sites were identified: Thr(72), Ser(32), and Ser(34). Rad60 Thr(72) mediates the Cds1-Rad60 interaction and is required for the Cds1-dependent phosphorylation of Rad60 in response to replication arrest. Phosphorylation of Rad60 Ser(32) and Ser(34) in a putative SUMO-binding motif is critical for the survival of replication stress. In addition, mutation of Rad60 Ser(32) and Ser(34) to alanine is lethal in cells deleted for the RecQ DNA helicase Rqh1. Finally, we find that Rad60 self-associates via its C-terminal SUMO-like domain and putative SUMO-binding motifs.","authors":"Raffa GD, Wohlschlegel J, Yates JR, Boddy MN","authors_abbrev":"Raffa GD et al.","pubmed_publication_date":"22 Sep 2006","pubmed_entrez_date":"2006-08-02","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1E7.06c","SPAC2G11.12","SPCC18B5.11c","SPBC1921.02"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"EMBL:SPC07120","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9771717","title":"Circular chromosome formation in a fission yeast mutant defective in two ATM homologues.","citation":"Nat Genet 1998 Oct;20(2):203-6","abstract":"Telomeres, found at chromosomal ends, are essential for stable maintenance of linear chromosomes in eukaryotes. The ATM family of genes, including budding yeast TEL1 (refs 1,2), fission yeast rad3+ (ref. 3) and human ATM (ref. 4), have been reported to be involved in telomere length regulation, although the significance of the telomere phenotypes observed with the mutated genes remains elusive. We have cloned tel1+, another fission yeast ATM homologue, and found that a tel1rad3 double mutant lost all telomeric DNA sequences. Thus, the ATM homologues are essential in telomere maintenance. The mutant grew poorly and formed irregular-shaped colonies, probably due to chromosome instability, however, during prolonged culture of the double mutant, cells forming normal round-shaped colonies arose at a relatively high frequency. All three chromosomes in these derivative cells were circular and lacked telomeric sequences. To our knowledge, this is the first report of eukaryotic cells whose chromosomes are all circular. Upon meiosis, these derivative cells produced few viable spores. Therefore, the exclusively circular genome lacking telomeric sequences is proficient for mitotic growth, but does not permit meiosis.","authors":"Naito T, Matsuura A, Ishikawa F","authors_abbrev":"Naito T et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-10-15","publication_year":"1998","canto_session_key":"40024707aa700ccb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-07 10:01:17","canto_approved_date":"2019-11-07 10:01:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-07 10:01:11","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC23B6.03c","SPBC216.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-11-07"},{"uniquename":"PMID:28345447","title":"Urea enhances cell lysis of Schizosaccharomyces pombe ura4 mutants.","citation":"Biosci Biotechnol Biochem 2017 Jul;81(7):1444-1451","abstract":"Cell lysis is induced in Schizosaccharomyces pombe ∆ura4 cells grown in YPD medium, which contains yeast extract, polypeptone, and glucose. To identify the medium components that induce cell lysis, we first tested various kinds of yeast extracts from different suppliers. Cell lysis of ∆ura4 cells on YE medium was observed when yeast extracts from OXOID, BD, Oriental, and Difco were used, but not when using yeast extract from Kyokuto. To determine which compounds induced cell lysis, we subjected yeast extract and polypeptone to GC-MS analysis. Ten kinds of compounds were detected in OXOID and BD yeast extracts, but not in Kyokuto yeast extract. Among them was urea, which was also present in polypeptone, and it clearly induced cell lysis. Deletion of the ure2 gene, which is responsible for utilizing urea, abolished the lytic effect of urea. The effect of urea was suppressed by deletion of pub1, and a similar phenotype was observed in the presence of polypeptone. Thus, urea is an inducer of cell lysis in S. pombe ∆ura4 cells.","doi":"10.1080/09168451.2017.1303360","authors":"Nishino K, Kushima M, Kaino T, Matsuo Y, Kawamukai M","authors_abbrev":"Nishino K et al.","pubmed_publication_date":"Jul 2017","pubmed_entrez_date":"2017-03-28","publication_year":"2017","canto_session_key":"ceb652bddd3380fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_approved_date":"2017-05-04 15:58:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-04-21 14:39:55","canto_added_date":"2017-03-29 00:15:13","annotation_curators":[{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22G7.06c","SPBC725.15","SPAC11G7.02","SPAC1399.03","SPAC1952.11c","SPAC16.03c","SPCC330.05c","SPAC57A10.12c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-04-21"},{"uniquename":"PMID:28357387","title":" S. pombe  placed on the prion map.","citation":"Microb Cell 2017 Feb 03;4(2):35-37","abstract":" Schizosaccharomyces pombe  has been used extensively as a model organism, however it is only recently that the first prion in this organism, a copper transporter protein encoded by  ctr4,  has been conclusively demonstrated. Prions are found in a wide range of organisms and have been implicated in a number of human neurodegenerative diseases. Research into the biology of prions has been carried out mainly in the budding yeast  Saccharomyces cerevisiae,  however there are many questions still to be addressed .  Now, with the identification of the Ctr4 prion in  S. pombe,  further work in the two yeasts and comparisons of prion biology in these organisms should lead to a greater understanding of prions and their role in disease.","doi":"10.15698/mic2017.02.555","authors":"Hayles J","authors_abbrev":"Hayles J","pubmed_publication_date":"03 Feb 2017","pubmed_entrez_date":"2017-03-31","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-04-01 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.08c","SPCC1393.10"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:15928972","title":"Second thoughts on septation by the fission yeast, Schizosaccharomyces pombe: pull vs. push mechanisms with an appendix--dimensional modelling of the flat and variable septa.","citation":"Antonie Van Leeuwenhoek 2005 Jul;88(1):1-12","abstract":"The correlation of contraction by an actomyosin band with the closing of the septum of dividing cells of the fission yeast, Schizosaccharomyces pombe, cannot suggest cause-and-effect because contraction would be apparent whether the membrane enveloping the centripetally closing septum were pulled or were pushed. Thus the common observation of contraction is not critical. Diagrams of published electron micrographs of dividing wild-type fission yeasts illustrate variable (tilted) septal images that are counterintuitive to a pull model. Circumference calculations based on those images suggest that some variable forms might be only 6% closed even though their two-dimensional profiles would be 50% closed, if they were not tilted. Development of multiseptate forms of cdc4-8 and cdc4-377 temperature sensitive mutants incubated at their restrictive temperature was followed. These multiseptate forms are shown to have functional (functional in terms of generating divided uninucleate cytoplasts) but grotesque septa which are formed in the absence of actomyosin bands. By contrast, the myosin of the plant phragmoplast is not properly oriented for contractility, and Dictyostelium (attached cells) and Saccharomyces (mutants) have been shown to divide in the absence of myosin II, just as S. pombe does (above). Hence contractility, the essence of a pull model for septum closure, would seem to be non-essential. Other, non-contractile mechanisms of myosin are emphasized, and a push model becomes a rational default hypothesis. The essence of push models is that their synthesis/assembly mechanisms are driving force sufficient for septum closure.","authors":"Johnson BF, Yoo BY, Calleja GB, Kozela CP","authors_abbrev":"Johnson BF et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-06-02","publication_year":"2005","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21095590","title":"DDK phosphorylates checkpoint clamp component Rad9 and promotes its release from damaged chromatin.","citation":"Mol Cell 2010 Nov 24;40(4):606-18","abstract":"When inappropriate DNA structures arise, they are sensed by DNA structure-dependent checkpoint pathways and subsequently repaired. Recruitment of checkpoint proteins to such structures precedes recruitment of proteins involved in DNA metabolism. Thus, checkpoints can regulate DNA metabolism. We show that fission yeast Rad9, a 9-1-1 heterotrimeric checkpoint-clamp component, is phosphorylated by Hsk1(Cdc7), the Schizosaccharomyces pombe Dbf4-dependent kinase (DDK) homolog, in response to replication-induced DNA damage. Phosphorylation of Rad9 disrupts its interaction with replication protein A (RPA) and is dependent on 9-1-1 chromatin loading, the Rad9-associated protein Rad4/Cut5(TopBP1), and prior phosphorylation by Rad3(ATR). rad9 mutants defective in DDK phosphorylation show wild-type checkpoint responses but abnormal DNA repair protein foci and decreased viability after replication stress. We propose that Rad9 phosphorylation by DDK releases Rad9 from DNA damage sites to facilitate DNA repair.","doi":"10.1016/j.molcel.2010.10.026","authors":"Furuya K, Miyabe I, Tsutsui Y, Paderi F, Kakusho N, Masai H, Niki H, Carr AM","authors_abbrev":"Furuya K et al.","pubmed_publication_date":"24 Nov 2010","pubmed_entrez_date":"2010-11-25","publication_year":"2010","canto_session_key":"3a1acc53ad7cd3a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-16 14:54:49","canto_approved_date":"2023-10-13 08:28:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-26 09:47:42","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC14C4.13","SPBC216.05","SPBC776.12c","SPBC4C3.05c","SPAC664.07c","SPAC1952.07","SPAC20G4.04c","SPBC342.05","SPBP23A10.07","SPAC23C4.18c","SPCC550.13"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2016-06-16"},{"uniquename":"PMID:31598751","title":"Unprogrammed epigenetic variation mediated by stochastic formation of ectopic heterochromatin.","citation":"Curr Genet 2020 Apr;66(2):319-325","abstract":"Changes in gene expression via chromatin-mediated mechanisms are important for reprogramming and differentiation, but uncontrolled changes can potentially lead to harmful or adaptive phenotypic alteration. Thus, diversification of the genome-wide chromatin state must be strictly limited, but the underlying mechanism of this regulation is largely unknown. In this review, we focused on distribution of heterochromatin, a tight chromatin structure that negatively regulates gene expression. Heterochromatin is characterized by methylation of histone H3 at lysine 9, and its formation and spreading are controlled by H3K9-specific methyltransferases and reversal factors such as histone demethylases. We summarize recent findings and discuss how variability in the heterochromatin distribution is controlled in the unicellular eukaryote fission yeast. In this context, we recently found that the anti-silencing factor Epe1 plays a key role in the formation of the individual-specific heterochromatin distribution. In conclusion, recent studies revealed that there are many potential heterochromatin formation sites in the fission yeast genome, and several proteins contribute to suppression of spreading and genome-wide dispersal of heterochromatin; knowledge from fission yeast studies may provide insights into the mechanisms regulating epigenetic diversification in multicellular eukaryotes.","doi":"10.1007/s00294-019-01031-4","authors":"Sorida M, Murakami Y","authors_abbrev":"Sorida M et al.","pubmed_publication_date":"Apr 2020","pubmed_entrez_date":"2019-10-11","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-10-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.16c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28318821","title":"SNF2 Family Protein Fft3 Suppresses Nucleosome Turnover to Promote Epigenetic Inheritance and Proper Replication.","citation":"Mol Cell 2017 Apr 06;66(1):50-62.e6","abstract":"Heterochromatin can be epigenetically inherited in cis, leading to stable gene silencing. However, the mechanisms underlying heterochromatin inheritance remain unclear. Here, we identify Fft3, a fission yeast homolog of the mammalian SMARCAD1 SNF2 chromatin remodeler, as a factor uniquely required for heterochromatin inheritance, rather than for de novo assembly. Importantly, we find that Fft3 suppresses turnover of histones at heterochromatic loci to facilitate epigenetic transmission of heterochromatin in cycling cells. Moreover, Fft3 also precludes nucleosome turnover at several euchromatic loci to prevent R-loop formation, ensuring proper replication progression. Our analyses show that overexpression of Clr4/Suv39h, which is also required for efficient replication through these loci, suppresses phenotypes associated with the loss of Fft3. This work uncovers a conserved factor critical for epigenetic inheritance of heterochromatin and describes a mechanism in which suppression of nucleosome turnover prevents formation of structural barriers that impede replication at fragile regions in the genome.","doi":"10.1016/j.molcel.2017.02.006","authors":"Taneja N, Zofall M, Balachandran V, Thillainadesan G, Sugiyama T, Wheeler D, Zhou M, Grewal SI","authors_abbrev":"Taneja N et al.","pubmed_publication_date":"06 Apr 2017","pubmed_entrez_date":"2017-03-21","publication_year":"2017","canto_session_key":"c9d47346a62d04c0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-22 01:15:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC25A8.01c","SPBC800.03","SPBC216.05","SPBC428.08c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:34310050","title":"Mitochondrial fusion and fission are required for proper mitochondrial function and cell proliferation in fission yeast.","citation":"FEBS J 2022 Jan;289(1):262-278","abstract":"Mitochondria form a branched tubular network in many types of cells, depending on a balance between mitochondrial fusion and fission. How mitochondrial fusion and fission are involved in regulating mitochondrial function and cell proliferation is not well understood. Here, we dissected the roles of mitochondrial fusion and fission in mitochondrial function and cell proliferation in fission yeast. We examined mitochondrial membrane potential by staining cells with DiOC 6  and assessed mitochondrial respiration by directly measuring oxygen consumption of cells with a dissolved oxygen respirometer. We found that defects in mitochondrial fission or fusion reduce mitochondrial membrane potential and compromise mitochondrial respiration while the absence of both mitochondrial fusion and fission restores wild type-like respiration, normal membrane potential, and tubular networks of mitochondria. Moreover, we found that the absence of either mitochondrial fission or fusion prolongs the cell cycle and that the absence of both mitochondrial fusion and fission significantly delays cell cycle progression after nitrogen replenishment. The prolonged/delayed cell cycle is likely due to the deregulation of Cdc2 activation. Hence, our work not only establishes an intimate link between mitochondrial morphology and function but also underscores the importance of mitochondrial dynamics in regulating the cell cycle.","doi":"10.1111/febs.16138","authors":"Dong F, Zhu M, Zheng F, Fu C","authors_abbrev":"Dong F et al.","pubmed_publication_date":"Jan 2022","pubmed_entrez_date":"2021-07-26","publication_year":"2022","canto_session_key":"e84318b6bdb0c4b6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-07-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12C2.08","SPBC1706.03"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:21151990","title":"The fission yeast XMAP215 homolog Dis1p is involved in microtubule bundle organization.","citation":"PLoS One 2010 Dec 02;5(12):e14201","abstract":"Microtubules are essential for a variety of fundamental cellular processes such as organelle positioning and control of cell shape. Schizosaccharomyces pombe is an ideal organism for studying the function and organization of microtubules into bundles in interphase cells. Using light microscopy and electron tomography we analyzed the bundle organization of interphase microtubules in S. pombe. We show that cells lacking ase1p and klp2p still contain microtubule bundles. In addition, we show that ase1p is the major determinant of inter-microtubule spacing in interphase bundles since ase1 deleted cells have an inter-microtubule spacing that differs from that observed in wild-type cells. We then identified dis1p, a XMAP215 homologue, as factor that promotes the stabilization of microtubule bundles. In wild-type cells dis1p partially co-localized with ase1p at regions of microtubule overlap. In cells deleted for ase1 and klp2, dis1p accumulated at the overlap regions of interphase microtubule bundles. In cells lacking all three proteins, both microtubule bundling and inter-microtubule spacing were further reduced, suggesting that Dis1p contributes to interphase microtubule bundling.","doi":"10.1371/journal.pone.0014201","authors":"Roque H, Ward JJ, Murrells L, Brunner D, Antony C","authors_abbrev":"Roque H et al.","pubmed_publication_date":"02 Dec 2010","pubmed_entrez_date":"2010-12-15","publication_year":"2010","canto_session_key":"81b27eb6010a93aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-20 14:09:11","canto_approved_date":"2019-11-20 14:09:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-08 16:33:15","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPAC664.10","SPCC736.14"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-11-20"},{"uniquename":"EMBL:AF027821","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36227631","title":"The  wtf  meiotic driver gene family has unexpectedly persisted for over 100 million years.","citation":"Elife 2022 Oct 13;11","abstract":"Meiotic drivers are selfish elements that bias their own transmission into more than half of the viable progeny produced by a driver+/driver- heterozygote. Meiotic drivers are thought to exist for relatively short evolutionary timespans because a driver gene or gene family is often found in a single species or in a group of very closely related species. Additionally, drivers are generally considered doomed to extinction when they spread to fixation or when suppressors arise. In this study, we examine the evolutionary history of the  wtf  meiotic drivers first discovered in the fission yeast  Schizosaccharomyces pombe . We identify homologous genes in three other fission yeast species,  S. octosporus ,  S. osmophilus , and  S. cryophilus , which are estimated to have diverged over 100 million years ago from the  S. pombe  lineage. Synteny evidence supports that  wtf  genes were present in the common ancestor of these four species. Moreover, the ancestral genes were likely drivers as  wtf  genes in  S. octosporus  cause meiotic drive. Our findings indicate that meiotic drive systems can be maintained for long evolutionary timespans.","doi":"10.7554/eLife.81149","authors":"De Carvalho M, Jia GS, Nidamangala Srinivasa A, Billmyre RB, Xu YH, Lange JJ, Sabbarini IM, Du LL, Zanders SE","authors_abbrev":"De Carvalho M et al.","pubmed_publication_date":"13 Oct 2022","pubmed_entrez_date":"2022-10-13","publication_year":"2022","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-10-15 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20625380","title":"A genome-wide screen for Schizosaccharomyces pombe deletion mutants that affect telomere length.","citation":"Cell Res 2010 Aug;20(8):963-5","abstract":"","doi":"10.1038/cr.2010.107","authors":"Liu NN, Han TX, Du LL, Zhou JQ","authors_abbrev":"Liu NN et al.","pubmed_publication_date":"Aug 2010","pubmed_entrez_date":"2010-07-14","publication_year":"2010","canto_session_key":"7c9a45500d002e2b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 09:41:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-20 09:39:00","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":167,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_20625380_phaf.tsv"}],"genes":["SPCC18B5.07c","SPAC1B3.11c","SPBC1271.05c","SPBC1718.03","SPAC926.06c","SPBC27B12.11c","SPAC6F6.13c","SPAC1687.13c","SPAC3C7.04","SPAC4C5.02c","SPCC553.01c","SPAC17A5.16","SPAC1952.06c","SPAC22G7.06c","SPAC1486.04c","SPBC29A3.10c","SPAC9G1.03c","SPAP27G11.15","SPCC74.06","SPCC757.02c","SPBP4G3.02","SPCC16C4.11","SPAC24H6.08","SPCC1739.15","SPAC1D4.09c","SPAC13A11.04c","SPBC28F2.07","SPAPB21F2.02","SPAC6F6.02c","SPAC8C9.10c","SPBC609.05","SPCC736.02","SPBC11C11.10","SPAC6G10.03c","SPAC2F3.15","SPBC32F12.03c","SPAC1D4.01","SPAC1805.01c","SPBC1D7.04","SPBC1703.14c","SPCC24B10.09","SPBC2D10.13","SPBC1861.03","SPAC27D7.05c","SPAC637.13c","SPAC17A2.06c","SPAC25B8.04c","SPBC685.07c","SPAC17A5.07c","SPBC2G5.02c","SPAPB24D3.08c","SPBC16G5.13","SPCC285.13c","SPAC15F9.01c","SPAC1556.03","SPAC30.04c","SPCC550.07","SPAC22E12.14c","SPAC1687.10","SPCC1672.03c","SPBC725.14","SPBC28F2.11","SPAC29B12.11c","SPAPB24D3.03","SPAC1687.07","SPAC19G12.13c","SPAC23A1.07","SPBC29A3.14c","SPBC1289.06c","SPAC4H3.02c","SPCC23B6.05c","SPAC20H4.02","SPAC823.05c","SPAC17C9.10","SPAC4D7.07c","SPBC887.17","SPBC1347.12","SPAC17H9.03c","SPAC17A2.10c","SPAC22A12.04c","SPBC839.05c","SPAC17G6.17","SPBC14C8.05c","SPAC3F10.16c","SPAC8E11.07c","SPAC3A12.13c","SPBC1D7.03","SPBC25B2.04c","SPBC543.03c","SPAC2F7.08c","SPAC1805.14","SPCC63.06","SPCC188.07","SPAC1782.01","SPBC19C7.01","SPCC417.11c","SPBC14F5.10c","SPAC9.02c","SPBC342.06c","SPBC2A9.03","SPBC1778.02","SPAC16A10.04","SPAC6F6.17","SPAC23C4.09c","SPCC364.04c","SPBC146.02","SPAC23H3.05c","SPAC5H10.07","SPBC365.07c","SPBP35G2.03c","SPBC26H8.03","SPBC1A4.05","SPAC1071.04c","SPCC18.17c","SPAC1687.09","SPAC3A12.12","SPAC22E12.18","SPAC23C11.15","SPAC22G7.08","SPCC613.11c","SPAC3A12.10","SPAC23D3.04c","SPAC6G9.13c","SPBC16C6.03c","SPAC25G10.02","SPCC622.08c","SPCC970.07c","SPBC1718.07c","SPBC19G7.16","SPAC824.04","SPBP8B7.11","SPAC1006.06","SPAC10F6.06","SPAC1805.04","SPBC29A10.01","SPAC23C4.03","SPBC18H10.05","SPBC1773.14","SPAC4G8.04","SPAC15E1.02c","SPAC25B8.15c","SPAC343.10","SPAC1F8.06","SPAC13G6.08","SPAC6C3.02c","SPAC24H6.03","SPBC12D12.07c","SPBC1703.11","SPCC622.14","SPBC21B10.13c","SPAC631.01c","SPAC688.10","SPBC365.06","SPBC115.02c","SPAC6C3.07","SPAC12B10.13","SPAC1782.05","SPAC343.12","SPBC3H7.11","SPAC1399.02","SPBC365.16","SPAC6B12.12","SPBC29A3.09c","SPAC4G9.16c","SPBC16D10.05","SPBC19G7.09","SPCC1235.11"],"gene_count":167,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:21376595","title":"IQGAP-related Rng2p organizes cortical nodes and ensures position of cell division in fission yeast.","citation":"Curr Biol 2011 Mar 22;21(6):467-72","abstract":"Correct positioning of the cell division machinery is crucial for genomic stability and cell fate determination. The fission yeast Schizosaccharomyces pombe, like animal cells, divides using an actomyosin ring and is an attractive model to study eukaryotic cytokinesis. In S. pombe, positioning of the actomyosin ring depends on the anillin-related protein Mid1p. Mid1p arrives first at the medial cortex and recruits actomyosin ring components to node-like structures, although how this is achieved is unknown. Here we show that the IQGAP-related protein Rng2p, an essential component of the actomyosin ring, is a key element downstream of Mid1p. Rng2p physically interacts with Mid1p and is required for the organization of other actomyosin ring components into cortical nodes. Failure of localization of Rng2p to the nodes prevents medial retention of Mid1p and leads to actomyosin ring assembly in a node-independent manner at nonmedial locations. We conclude that Mid1p recruits Rng2p to cortical nodes at the division site and that Rng2p, in turn, recruits other components of the actomyosin ring to cortical nodes, thereby ensuring correct placement of the division site.","doi":"10.1016/j.cub.2011.01.059","authors":"Padmanabhan A, Bakka K, Sevugan M, Naqvi NI, D'souza V, Tang X, Mishra M, Balasubramanian MK","authors_abbrev":"Padmanabhan A et al.","pubmed_publication_date":"22 Mar 2011","pubmed_entrez_date":"2011-03-08","publication_year":"2011","canto_session_key":"a206afb9651e2886","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-24 18:33:20","canto_approved_date":"2023-11-28 14:02:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-03-07 12:01:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08","SPAC20G8.05c","SPAC4F8.13c","SPAC926.03","SPCC4B3.15"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2015-02-24"},{"uniquename":"PMID:23260662","title":"Lsd1 and lsd2 control programmed replication fork pauses and imprinting in fission yeast.","citation":"Cell Rep 2012 Dec 27;2(6):1513-20","abstract":"In the fission yeast Schizosaccharomyces pombe, a chromosomal imprinting event controls the asymmetric pattern of mating-type switching. The orientation of DNA replication at the mating-type locus is instrumental in this process. However, the factors leading to imprinting are not fully identified and the mechanism is poorly understood. Here, we show that the replication fork pause at the mat1 locus (MPS1), essential for imprint formation, depends on the lysine-specific demethylase Lsd1. We demonstrate that either Lsd1 or Lsd2 amine oxidase activity is required for these processes, working upstream of the imprinting factors Swi1 and Swi3 (homologs of mammalian Timeless and Tipin, respectively). We also show that the Lsd1/2 complex controls the replication fork terminators, within the rDNA repeats. These findings reveal a role for the Lsd1/2 demethylases in controlling polar replication fork progression, imprint formation, and subsequent asymmetric cell divisions.","doi":"10.1016/j.celrep.2012.10.011","authors":"Holmes A, Roseaulin L, Schurra C, Waxin H, Lambert S, Zaratiegui M, Martienssen RA, Arcangioli B","authors_abbrev":"Holmes A et al.","pubmed_publication_date":"27 Dec 2012","pubmed_entrez_date":"2012-12-25","publication_year":"2012","canto_session_key":"87c7e4f7306c2d8c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-08-13 10:49:24","canto_approved_date":"2024-05-02 15:56:24","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-12-30 14:24:12","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":48,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23E2.02","SPBP8B7.07c","SPBC216.06c","SPCC4B3.12","SPCC306.04c","SPBC146.09c","SPBC428.08c","SPBP19A11.06"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-08-13"},{"uniquename":"PMID:8522343","title":"Precise epitope mapping of three monoclonal antibodies raised against tms1 protein of fission yeast.","citation":"Hybridoma 1995 Aug;14(4):329-33","abstract":"Recently we described the production of two monoclonal antibodies 10G2 and 10C4 of IgG3 subclass raised against the recombinant tms1 protein of fission yeast. Here we introduce a new monoclonal antibody 2E2 of IgG1 subclass and present the precise epitope mapping of these monoclonal antibodies using tms1 deletion mutants and synthetically produced oligopeptides spanning the tms1 protein by immunoblot analysis.","authors":"Schneider E, Fuchs A, Nastainczyk W, Montenarh M, Wagner P","authors_abbrev":"Schneider E et al.","pubmed_publication_date":"Aug 1995","pubmed_entrez_date":"1995-08-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1840886","title":"Controlling cell cycle progress in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Opin Genet Dev 1991 Oct;1(3):307-12","abstract":"The suitability of fission yeast as a model for understanding the eukaryotic cell cycle has been validated in five years of exciting developments. We review recent advances in understanding the nature of the controls that regulate progression through the cell cycle and the coordination of DNA replication and mitosis.","authors":"MacNeill SA, Warbrick E, Fantes PA","authors_abbrev":"MacNeill SA et al.","pubmed_publication_date":"Oct 1991","pubmed_entrez_date":"1991-10-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36820392","title":"Optimization of the CRISPR/Cas9 system using  adh1  promoter derivatives in fission yeast.","citation":"MicroPubl Biol 2023;2023","abstract":"The CRSIPR/Cas9 system has been applied to fission yeast, but there remain some rooms for improvement. Here we report that the weaker versions of the  adh1   +  promoter,  adh11  and  adh41  promoters, for the potentially cytotoxic Cas9 achieved highly efficient mutagenesis and gene deletion at the  ade6   +  locus. Employing a drug-selectable marker instead of conventional auxotrophic markers, our new vector system is compatible with a variety of experimental settings including prototrophic/auxotrophic strains and complete/minimal media.","doi":"10.17912/micropub.biology.000757","authors":"Saito M, Nakaoka H, Hayashi A, Takaku H, Yamazaki H","authors_abbrev":"Saito M et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-02-23","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-02-24 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16928959","title":"Real-time monitoring of calcineurin activity in living cells: evidence for two distinct Ca2+-dependent pathways in fission yeast.","citation":"Mol Biol Cell 2006 Nov;17(11):4790-800","abstract":"In fission yeast, calcineurin dephosphorylates and activates the Prz1 transcription factor. Here, we identified the calcineurin-dependent response element (CDRE) in the promoter region of prz1(+) gene and monitored the calcineurin activity in living cells using a destabilized luciferase reporter gene fused to three tandem repeats of CDRE. Elevated extracellular CaCl(2) caused an increase in calcineurin activity with an initial peak and then approached a sustained constant level in a concentration-dependent manner. In CaCl(2)-sensitive mutants such as Deltapmc1, the response was markedly enhanced, reflecting its high intracellular Ca(2+). Agents expected to induce Ca(2+) influx showed distinct patterns of the CDRE-reporter activity, suggesting different mechanisms of calcineurin activation. Knockout of yam8(+) or cch1(+) encoding putative subunits of a Ca(2+) channel abolished the activation of calcineurin upon exposure to various stimuli, including high extracellular NaCl and cell wall-damaging agents. However, knockout of yam8(+) or cch1(+) did not affect the activation of calcineurin upon stimulation by elevated extracellular Ca(2+). The Pck2 protein kinase C-Pmk1 mitogen-activate protein kinase pathway was required for the stimulation of calcineurin via Yam8/Cch1-mediated Ca(2+) influx, but it was not required for the stimulation by elevated extracellular Ca(2+), suggesting two distinct pathways for calcineurin activation.","authors":"Deng L, Sugiura R, Takeuchi M, Suzuki M, Ebina H, Takami T, Koike A, Iba S, Kuno T","authors_abbrev":"Deng L et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-08-25","publication_year":"2006","canto_session_key":"9618d1df6e9897a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-02-01 21:22:36","canto_approved_date":"2024-04-02 13:42:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-01-13 17:35:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.02c","SPAC6F6.01","SPAC1F5.08c","SPCC1795.02c","SPBC12D12.04c","SPBC31E1.02c","SPBC119.08","SPAC4G8.13c","SPAPB2B4.04c","SPBC543.07"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2020-02-01"},{"uniquename":"PMID:23335786","title":"Spontaneous telomere to telomere fusions occur in unperturbed fission yeast cells.","citation":"Nucleic Acids Res 2013 Mar 01;41(5):3056-67","abstract":"Telomeres protect eukaryotic chromosomes from illegitimate end-to-end fusions. When this function fails, dicentric chromosomes are formed, triggering breakage-fusion-bridge cycles and genome instability. How efficient is this protection mechanism in normal cells is not fully understood. We created a positive selection assay aimed at capturing chromosome-end fusions in Schizosaccharomyces pombe. We placed telomere sequences with a head to head arrangement in an intron of a selectable marker contained on a plasmid. By linearizing the plasmid between the telomere sequences, we generated a stable mini-chromosome that fails to express the reporter gene. Whenever the ends of the mini-chromosome join, the marker gene is reconstituted and fusions are captured by direct selection. Using telomerase mutants, we recovered several fusion events that lacked telomere sequences. The end-joining reaction involved specific homologous subtelomeric sequences capable of forming hairpins, suggestive of ssDNA stabilization prior to fusing. These events occurred via microhomology-mediated end-joining (MMEJ)/single-strand annealing (SSA) repair and also required MRN/Ctp1. Strikingly, we were able to capture spontaneous telomere-to-telomere fusions in unperturbed cells. Similar to disruption of the telomere regulator Taz1/TRF2, end-joining reactions occurred via non-homologous end-joining (NHEJ) repair. Thus, telomeres undergo fusions prior to becoming critically short, possibly through transient deprotection. These dysfunction events induce chromosome instability and may underlie early tumourigenesis.","doi":"10.1093/nar/gks1459","authors":"Almeida H, Godinho Ferreira M","authors_abbrev":"Almeida H et al.","pubmed_publication_date":"01 Mar 2013","pubmed_entrez_date":"2013-01-22","publication_year":"2013","canto_session_key":"7caec9d92d59a6be","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC6B1.09c","SPAC13C5.07","SPCC338.08","SPAC1556.01c","SPCC126.02c","SPCC1183.05c","SPBC29A3.14c","SPCC970.01","SPAC16A10.07c"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:9491802","title":"The small GTP-binding protein Rho1 is a multifunctional protein that regulates actin localization, cell polarity, and septum formation in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Cells 1997 Nov;2(11):679-94","abstract":"The small GTP-binding protein Rho has been shown to regulate the formation of the actin cytoskeleton in animal cells. We have previously isolated two rho genes, rho1+ and rho2+, from the fission yeast Schizosaccharomyces pombe in order to investigate the function of Rho using genetic techniques. In this paper, we report the cellular function of Rho1.\nWe found that Rho1 is essential for cell viability and cell polarity using gene disruption and by exogenous expression of botulinum C3 ADP-ribosyltransferase. In cells expressing either a constitutively active Rho1 or a dominant-negative Rho1, actin patches were delocalized. Both the cell wall and secondary septum were thick and stratified in cells expressing the constitutively active Rho1, while the cell wall of cells expressing the dominant-negative Rho1 seemed to be loosely organized. Furthermore, inactivation of Rho1 is apparently required for the separation of daughter cells. Cell fractionation studies suggested that Rho1 is predominantly membrane-bound. Moreover, we observed that Rho1 is localized to the cell periphery and to the septum.\nRho1 is involved in actin patch localization, the control of cell polarity, the regulation of septation, and cell wall synthesis.","authors":"Nakano K, Arai R, Mabuchi I","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-03-10","publication_year":"1997","canto_session_key":"fd98ac563a6f67cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-08-18 16:38:32","canto_approved_date":"2025-09-04 12:21:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-08-18 16:38:26","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-08-18"},{"uniquename":"PMID:37820734","title":"Establishment of dsDNA-dsDNA interactions by the condensin complex.","citation":"Mol Cell 2023 Nov 02;83(21):3787-3800.e9","abstract":"Condensin is a structural maintenance of chromosomes (SMC) complex family member thought to build mitotic chromosomes by DNA loop extrusion. However, condensin variants unable to extrude loops, yet proficient in chromosome formation, were recently described. Here, we explore how condensin might alternatively build chromosomes. Using bulk biochemical and single-molecule experiments with purified fission yeast condensin, we observe that individual condensins sequentially and topologically entrap two double-stranded DNAs (dsDNAs). Condensin loading transitions through a state requiring DNA bending, as proposed for the related cohesin complex. While cohesin then favors the capture of a second single-stranded DNA (ssDNA), second dsDNA capture emerges as a defining feature of condensin. We provide complementary in vivo evidence for DNA-DNA capture in the form of condensin-dependent chromatin contacts within, as well as between, chromosomes. Our results support a \"diffusion capture\" model in which condensin acts in mitotic chromosome formation by sequential dsDNA-dsDNA capture.","doi":"10.1016/j.molcel.2023.09.019","authors":"Tang M, Pobegalov G, Tanizawa H, Chen ZA, Rappsilber J, Molodtsov M, Noma KI, Uhlmann F","authors_abbrev":"Tang M et al.","pubmed_publication_date":"02 Nov 2023","pubmed_entrez_date":"2023-10-11","publication_year":"2023","canto_session_key":"40a3b7f45b30fa7f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tony Tang","canto_first_approved_date":"2024-01-03 15:55:33","canto_approved_date":"2024-02-02 15:50:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-14 00:18:31","canto_added_date":"2023-10-12 23:25:04","annotation_curators":[{"name":"Tony Tang","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.03c","SPBC776.13","SPBP4H10.06c","SPCC306.03c","SPCC188.03"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2024-01-03"},{"uniquename":"PMID:9191273","title":"The role of Sxa1 in pheromone recovery in Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1997 May;25(2):229S","abstract":"","authors":"Hughes M, Davey J","authors_abbrev":"Hughes M et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"3cd4cea969e25e08","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-07-05 13:33:12","canto_approved_date":"2025-05-28 11:05:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-05 23:22:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.01","SPAC1296.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-07-05"},{"uniquename":"PMID:22146713","title":"Function and structure studies of GH family 31 and 97 α-glycosidases.","citation":"Biosci Biotechnol Biochem 2011;75(12):2269-77","abstract":"A huge number of glycoside hydrolases are classified into the glycoside hydrolase family (GH family) based on their amino-acid sequence similarity. The glycoside hydrolases acting on α-glucosidic linkage are in GH family 4, 13, 15, 31, 63, 97, and 122. This review deals mainly with findings on GH family 31 and 97 enzymes. Research on two GH family 31 enzymes is described: clarification of the substrate recognition of Escherichia coli α-xylosidase, and glycosynthase derived from Schizosaccharomyces pombe α-glucosidase. GH family 97 is an aberrant GH family, containing inverting and retaining glycoside hydrolases. The inverting enzyme in GH family 97 displays significant similarity to retaining α-glycosidases, including GH family 97 retaining α-glycosidase, but the inverting enzyme has no catalytic nucleophile residue. It appears that a catalytic nucleophile has been eliminated during the molecular evolution in the same way as a man-made nucleophile mutant enzyme, which catalyzes the inverting reaction, as in glycosynthase and chemical rescue.","authors":"Okuyama M","authors_abbrev":"Okuyama M","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-12-08","publication_year":"2011","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28951277","title":"Efficient substrate screening and inhibitor testing of human CYP4Z1 using permeabilized recombinant fission yeast.","citation":"Biochem Pharmacol 2017 Dec 15;146:174-187","abstract":"We have established a protocol for the preparation of permeabilized fission yeast cells (enzyme bags) that recombinantly express human cytochrome P450 enzymes (CYPs). A direct comparison of CYP3A4 activity gave an eightfold higher space-time yield for enzyme bag-catalyzed biotransformation as compared to whole-cell biotransformation, even though the total number of cells employed was lower by a factor of 150. Biotransformation of the luminogenic substrate Luciferin-H using CYP2C9-containing enzyme bags proceeded efficiently and stably for 24h. CYP4Z1 is of interest because it is strongly overexpressed both in breast cancer cells and in breast cancer metastases; however, current knowledge about its catalytic properties is very limited. Screening of CYP4Z1-containing enzyme bags with 15 luminogenic substrates enabled us to identify two new hydroxylations and eleven ether cleavage reactions that are catalyzed by CYP4Z1. By far the best substrate found in this study was Luciferin benzyl ether (Luciferin-BE). On the basis of the recently published crystal structure of CYP4B1 we created a new homology model of CYP4Z1 and performed molecular docking experiments, which indicate that all active substrates show a highly similar binding geometry compared to the endogenous substrates. The model predicts that Ser113, Ser222, Asn381, and Ser383 are key hydrogen bonding residues. We also identified five new inhibitors of CYP4Z1: miconazole, econazole, aminobenzotriazole, tolazoline, and 1-benzylimidazole respectively, with the last compound being the most potent giving an IC 50  value of 180nM in our test system.","doi":"10.1016/j.bcp.2017.09.011","authors":"Yan Q, Machalz D, Zöllner A, Sorensen EJ, Wolber G, Bureik M","authors_abbrev":"Yan Q et al.","pubmed_publication_date":"15 Dec 2017","pubmed_entrez_date":"2017-09-28","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-09-29 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007844","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.134"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPC02442","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12784644","title":"Salt stress induces the expression of Schizosaccharomyces pombe och1+, which encodes an initiation-specific alpha-1,6-mannosyltransferase for N-linked outer chain synthesis of cell wall mannoproteins.","citation":"Biosci Biotechnol Biochem 2003 Apr;67(4):927-9","abstract":"The Schizosaccharomyces pombe Och1p is required for the initiation of outer chain elongation of N-linked oligosaccharides. In this report, we investigated the transcriptional control of the S. pombe och1+ gene and found that the expression of the och1+ gene was not regulated during the cell cycle, but was induced by NaCl and KCl through a transcription factor, Atf1p.","authors":"Yamamoto K, Okamoto M, Yoko-o T, Jigami Y","authors_abbrev":"Yamamoto K et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-06-06","publication_year":"2003","canto_session_key":"0b75c65eebff8b0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-08 10:17:38","canto_approved_date":"2019-11-08 10:17:38","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-08 10:17:33","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC8C9.14","SPAC1006.05c","SPBC215.05"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2019-11-08"},{"uniquename":"PMID:18980245","title":"Establishment of a transgenic yeast screening system for estrogenicity and identification of the anti-estrogenic activity of malachite green.","citation":"J Cell Biochem 2008 Dec 15;105(6):1399-409","abstract":"Endocrine disruptors refer to chemical compounds in the environment which interfere with the endocrine systems of organisms. Among them, environmental estrogens pose serious problems to aquatic organisms, in particular fish. It is therefore important and necessary to have a fast and low-cost system to screen the large number of different chemical compounds in the aquatic environment for their potential endocrine disrupting actions. In this study, a screening platform was developed to detect xenoestrogens in the aquatic environment using the fission yeast Schizosaccharomyces pombe, and applied for compound screening. The aim was to demonstrate any significant potential differences between the fish screening system and the human screening system. To this end, a yeast expression vector harboring a fish estrogen receptor alpha and a reporter vector containing the estrogen responsive element fused with the Escherichia coli LacZ gene were constructed. After transformation with these two vectors, the transformed yeast clones were confirmed by Western blotting and selected on the basis of the beta-galactosidase activity. In this transgenic yeast system, the natural estrogen (estradiol) and other known xenoestrogens such as diethylstilbestrol, bisphenol A, genistein and dichloro-diphenyl-trichloroethane exhibited dose-dependent activities. Using this system, more than 40 putative endocrine disruptors including phytoestrogens, pesticides, herbicides, industrial dyes and other industrial chemicals were screened. Ten of them were demonstrated to exhibit estrogenic actions. Industrial dyes such as malachite green (MG) that disrupt thyroid hormone synthesis are extensively used and are widely distributed in the aquatic environment. Using this system, MG did not show any estrogenic action, but was demonstrated to exhibit anti-estrogenic activity.","doi":"10.1002/jcb.21960","authors":"Jiao B, Yeung EK, Chan CB, Cheng CH","authors_abbrev":"Jiao B et al.","pubmed_publication_date":"15 Dec 2008","pubmed_entrez_date":"2008-11-05","publication_year":"2008","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12721304","title":"Identification and characterization of the human mus81-eme1 endonuclease.","citation":"J Biol Chem 2003 Jul 04;278(27):25172-8","abstract":"The faithful and complete replication of DNA is necessary for the maintenance of genome stability. It is known, however, that replication forks stall at lesions in the DNA template and need to be processed so that replication restart can occur. In fission yeast, the Mus81-Eme1 endonuclease complex (Mus81-Mms4 in Saccharomyces cerevisiae) has been implicated in the processing of aberrant replication intermediates. In this report, we identify the human homolog of the Schizosaccharomyces pombe EME1 gene and have purified the human Mus81-Eme1 heterodimer. We show that Mus81-Eme1 is an endonuclease that exhibits a high specificity for synthetic replication fork structures and 3'-flaps in vitro. The nuclease cleaves Holliday junctions inefficiently ( approximately 75-fold less than flap or fork structures), although cleavage can be increased 6-fold by the presence of homologous sequences previously shown to permit base pair \"breathing.\" We conclude that human Mus81-Eme1 is a flap/fork endonuclease that is likely to play a role in the processing of stalled replication fork intermediates.","authors":"Ciccia A, Constantinou A, West SC","authors_abbrev":"Ciccia A et al.","pubmed_publication_date":"04 Jul 2003","pubmed_entrez_date":"2003-05-02","publication_year":"2003","canto_session_key":"28bff6ae4eff2e87","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-10-24 20:10:58","canto_approved_date":"2019-10-24 20:10:58","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-10-24 20:10:52","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-10-24"},{"uniquename":"PMID:9531532","title":"The fission yeast SPB component Cut12 links bipolar spindle formation to mitotic control.","citation":"Genes Dev 1998 Apr 01;12(7):927-42","abstract":"During fission yeast mitosis, the duplicated spindle pole bodies (SPBs) nucleate microtubule arrays that interdigitate to form the mitotic spindle. cut12.1 mutants form a monopolar mitotic spindle, chromosome segregation fails, and the mutant undergoes a lethal cytokinesis. The cut12(+) gene encodes a novel 62-kD protein with two predicted coiled coil regions, and one consensus phosphorylation site for p34(cdc2) and two for MAP kinase. Cut12 is localized to the SPB throughout the cell cycle, predominantly around the inner face of the interphase SPB, adjacent to the nucleus. cut12(+) is allelic to stf1(+); stf1.1 is a gain-of-function mutation bypassing the requirement for the Cdc25 tyrosine phosphatase, which normally dephosphorylates and activates the p34(cdc2)/cyclin B kinase to promote the onset of mitosis. Expressing a cut12(+) cDNA carrying the stf1.1 mutation also suppressed cdc25.22. The spindle defect in cut12.1 is exacerbated by the cdc25.22 mutation, and stf1.1 cells formed defective spindles in a cdc25.22 background at high temperatures. We propose that Cut12 may be a regulator or substrate of the p34(cdc2) mitotic kinase.","authors":"Bridge AJ, Morphew M, Bartlett R, Hagan IM","authors_abbrev":"Bridge AJ et al.","pubmed_publication_date":"01 Apr 1998","pubmed_entrez_date":"1998-05-09","publication_year":"1998","canto_session_key":"abbc849e1c0c5544","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-03 10:37:56","canto_approved_date":"2026-01-31 14:19:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-03 10:37:49","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC649.05","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-01-03"},{"uniquename":"PMID:36200823","title":"The chromatin remodeler RSC prevents ectopic CENP-A propagation into pericentromeric heterochromatin at the chromatin boundary.","citation":"Nucleic Acids Res 2022 Oct 28;50(19):10914-10928","abstract":"Centromeres of most eukaryotes consist of two distinct chromatin domains: a kinetochore domain, identified by the histone H3 variant, CENP-A, and a heterochromatic domain. How these two domains are separated is unclear. Here, we show that, in Schizosaccharomyces pombe, mutation of the chromatin remodeler RSC induced CENP-ACnp1 misloading at pericentromeric heterochromatin, resulting in the mis-assembly of kinetochore proteins and a defect in chromosome segregation. We find that RSC functions at the kinetochore boundary to prevent CENP-ACnp1 from spreading into neighbouring heterochromatin, where deacetylated histones provide an ideal environment for the spread of CENP-ACnp1. In addition, we show that RSC decompacts the chromatin structure at this boundary, and propose that this RSC-directed chromatin decompaction prevents mis-propagation of CENP-ACnp1 into pericentromeric heterochromatin. Our study provides an insight into how the distribution of distinct chromatin domains is established and maintained.","doi":"10.1093/nar/gkac827","authors":"Tsunemine S, Nakagawa H, Suzuki Y, Murakami Y","authors_abbrev":"Tsunemine S et al.","pubmed_publication_date":"28 Oct 2022","pubmed_entrez_date":"2022-10-06","publication_year":"2022","canto_session_key":"4f955b5fd93e3ce0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Satoru Tsunemine","canto_first_approved_date":"2023-02-03 15:00:30","canto_approved_date":"2023-02-03 15:00:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-01-10 02:38:45","canto_added_date":"2022-10-08 00:15:04","annotation_curators":[{"name":"Satoru Tsunemine","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1861.01c","SPCC1620.14c","SPBC428.08c","SPAC1250.01","SPBC1105.17","SPBC12D12.01","SPAC1687.20c","SPBC1734.15","SPBC21.01","SPBC36B7.08c","SPBC577.15c","SPBC800.03","SPAC2F7.08c","SPBC32H8.12c","SPCC1672.10","SPCC970.12","SPBC336.07","SPCC16A11.14","SPBC18E5.03c","SPBC4B4.03","SPAPB1A10.02","SPBP22H7.09c"],"gene_count":22,"ltp_gene_count":7,"approved_date":"2023-02-03"},{"uniquename":"PMID:16769823","title":"Bqt2p is essential for initiating telomere clustering upon pheromone sensing in fission yeast.","citation":"J Cell Biol 2006 Jun 19;173(6):845-51","abstract":"The telomere bouquet, i.e., telomere clustering on the nuclear envelope (NE) during meiotic prophase, is thought to promote homologous chromosome pairing. Using a visual screen, we identified bqt2/im295, a mutant that disrupts telomere clustering in fission yeast. Bqt2p is required for linking telomeres to the meiotic spindle pole body (SPB) but not for attachment of telomeres or the SPB to the NE. Bqt2p is expressed upon pheromone sensing and colocalizes thereafter to Sad1p, an SPB protein. This localization only depends on Bqt1p, not on other identified proteins required for telomere clustering. Upon pheromone sensing, generation of Sad1p foci next to telomeres depends on Bqt2p. However, depletion of Bqt2p from the SPB is dispensable for dissolving the telomere bouquet at the end of meiotic prophase. Therefore, telomere bouquet formation requires Bqt2p as a linking component and is finely regulated during meiotic progression.","authors":"Tang X, Jin Y, Cande WZ","authors_abbrev":"Tang X et al.","pubmed_publication_date":"19 Jun 2006","pubmed_entrez_date":"2006-06-14","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2203537","title":"The fission yeast cut1+ gene regulates spindle pole body duplication and has homology to the budding yeast ESP1 gene.","citation":"Cell 1990 Sep 07;62(5):913-25","abstract":"Mutations in the fission yeast cut1+, cut2+, and cut10+ genes uncouple normally coordinated mitotic events and deregulate, rather than arrest, mitosis. DNA synthesis continues, making polyploid nuclei with several spindles. Multiple, aberrant spindle pole bodies (SPBs) are produced in cut1 mutant cells. The cut1+ and cut2+ genes are cloned by transformation. High gene dosage of cut1+ also complements cut2 and cut10 mutants. The cut2+ gene, however, complements only cut2. The 210 kd cut1+ gene product contains putative ATP binding and helical coil regions followed by a COOH-terminal domain homologous to the S. cerevisiae gene ESP1. Mutations in the ESP1 gene also result in many SPBs. The cut1+ product is shown by anti-cut1 antibody to be a rare component of the insoluble nuclear fraction. It may play a key role in coupling chromosome disjunction with other cell cycle events and is potentially a component, regulator, or motor for the SPB and/or kinetochores.","authors":"Uzawa S, Samejima I, Hirano T, Tanaka K, Yanagida M","authors_abbrev":"Uzawa S et al.","pubmed_publication_date":"07 Sep 1990","pubmed_entrez_date":"1990-09-07","publication_year":"1990","canto_session_key":"a285637adcbb8409","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-06 16:51:57","canto_approved_date":"2022-02-07 18:14:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-06 16:51:48","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.01c","SPAC6F12.15c","SPCC5E4.04","SPCC1739.11c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2016-09-06"},{"uniquename":"PMID:6215401","title":"Exchange of oxygen between phosphate and water catalyzed by the plasma membrane ATPase from the yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1982 Nov 10;257(21):12509-16","abstract":"The ATPase of the plasma membrane isolated from the yeast Schizosaccharomyces pombe catalyses a medium Pi in equilibrium H2O exchange in the presence of Mg2+ and in the absence of ATP and ADP. (formula, see text) The Pi in the E.Pi species tumbles in the active site so that each of its oxygens has an equal probability of exchange with water. The partition coefficient (Pc = k2/k2 + k-1) is 0.45. The total rate of oxygen exchange, Vex, representing the rate of incorporation of water oxygens occurring during hydrolysis of E--P into E.Pi (Vex = k-2[E--P]) is dependent on the [Pi] with an apparent Km of 177 mM, reflecting the very low affinity of the enzyme for Pi. The maximal exchange rate is 6.7 micrograms atoms of oxygen X min-1 X mg-1 of protein. The individual kinetic constants are evaluated: k2 = 3.4 X 10(3) min-1, k-2 = 5.50 X 10(5) min-1 and k-1 = 4.11 X 10(3) min-1. Under conditions of uncoupled transport, the hydrolysis of E--P is exergonic as [E.Pi]/[E--P] = k-2/k2 = 164. During hydrolysis of ATP, the rate of medium Pi in equilibrium H2O exchange activity as well as the extent of phosphorylation of the enzyme from Pi are markedly stimulated: 7.9 and 5.3 times, respectively, whereas the Pc is not modified. These data are most simply interpretated by the existence of two isomeric forms of the enzyme; one is specific for binding ATP and the other for binding Pi. The Pc for intermediate Pi in equilibrium H2O exchange, when the E--P species is formed from cleavage of [gamma-18O]ATP, is the same as for medium exchange, indicating that the same exchange pathway operates under both conditions. Varying the [ATP] had very little effect on the Pc, indicating little or no cooperativity between different catalytic sites under the conditions used in this study.","authors":"Amory A, Goffeau A, McIntosh DB, Boyer PD","authors_abbrev":"Amory A et al.","pubmed_publication_date":"10 Nov 1982","pubmed_entrez_date":"1982-11-10","publication_year":"1982","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8065367","title":"Identification of cut8+ and cek1+, a novel protein kinase gene, which complement a fission yeast mutation that blocks anaphase.","citation":"Mol Cell Biol 1994 Sep;14(9):6361-71","abstract":"The fission yeast Schizosaccharomyces pombe [corrected] temperature sensitivity cut8-563 mutation causes chromosome overcondensation and short spindle formation in the absence of sister chromatid separation. The cut8-563 mutation allows cytokinesis before the completion of anaphase, thus producing cells with a cut phenotype. The cut8+ gene product may be required for normal progression of anaphase. Diploidization occurs at the restrictive temperature, and 60 to 70% of the cells surviving after two generations are diploid. These phenotypes are reminiscent of those of budding yeast (Saccharomyces cerevisiae) ctf13 and ctf14 (ndc10) mutations. The cut8+ gene, isolated by complementation of the mutant, predicts a 262-amino-acid protein; the amino and carboxy domains are hydrophilic, while the central domain contains several hydrophobic stretches. It has a weak overall similarity to the budding yeast DBF8 gene product. DBF8 is an essential gene whose mutations result in delay in mitotic progression and chromosome instability. Anti-cut8 antibodies detect a 33-kDa polypeptide. Two multicopy suppressor genes for cut8-563 are identified. They are the cut1+ gene essential for nuclear division, and a new gene (designated cek1+) which encodes a novel protein kinase. The cek1+ gene product is unusually large (1,309 amino acids) and has a 112-amino-acid additional sequence in the kinase domain. The cek1+ gene is not an essential gene. Protein phosphorylation by cek1 may facilitate the progression of anaphase through direct or indirect interaction with the cut8 protein.","authors":"Samejima I, Yanagida M","authors_abbrev":"Samejima I et al.","pubmed_publication_date":"Sep 1994","pubmed_entrez_date":"1994-09-01","publication_year":"1994","canto_session_key":"0b84151023ead28b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-12 15:56:20","canto_approved_date":"2026-01-31 13:14:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-08 10:04:46","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1450.11c","SPCC5E4.04","SPAC17C9.13c","SPCC1739.11c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-01-12"},{"uniquename":"EMBL:AU006903","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5124486","title":"Further measurements of DNA synthesis and enzyme potential during cell cycle of fission yeast Schizosaccharomyces pombe.","citation":"Exp Cell Res 1971 Nov;69(1):244-7","abstract":"","authors":"Mitchison JM, Creanor J","authors_abbrev":"Mitchison JM et al.","pubmed_publication_date":"Nov 1971","pubmed_entrez_date":"1971-11-01","publication_year":"1971","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38790882","title":"Unconventional Yeasts Isolated from Chilean Honey: A Probiotic and Phenotypic Characterization.","citation":"Foods 2024 May 20;13(10)","abstract":"This study explores the potential probiotic properties of yeasts isolated from various Chilean honeys, focusing on Ulmo, Quillay, and Mountain honeys. Six yeast strains were identified, including  Zygosaccharomyces rouxii ,  Candida  sp.,  Schizosaccharomyces pombe ,  Rhodosporidiobolus ruineniae ,  Clavispora lusitaniae , and  Metschnikowia chrysoperlae . Phenotypic characterization involved assessing their fermentative performance, ethanol and hops resistance, and cross-resistance. Ethanol concentration emerged as a limiting factor in their fermentative performance. The probiotic potential of these yeasts was evaluated based on resistance to high temperatures, low pH, auto-aggregation capacity, survival in simulated  in vitro  digestion (INFOGEST method), and antimicrobial activity against pathogens like  Escherichia coli ,  Staphylococcus aureus , and  Salmonella enteritidis . Three yeasts,  Zygosaccharomyces rouxii ,  Schizosaccharomyces pombe , and  Metschnikowia chrysoperlae , exhibited potential probiotic characteristics by maintaining cell concentrations exceeding 10 6  CFU/mL after  in vitro  digestion. They demonstrated fermentative abilities and resistance to ethanol and hops, suggesting their potential as starter cultures in beer production. Despite revealing promising probiotic and technological aspects, further research is necessary to ascertain their viability in producing fermented foods. This study underscores the innovative potential of honey as a source for new probiotic microorganisms and highlights the need for comprehensive investigations into their practical applications in the food industry.","doi":"10.3390/foods13101582","authors":"Rodríguez Machado A, Caro CM, Hurtado-Murillo JJ, Gomes Lobo CJ, Zúñiga RN, Franco W","authors_abbrev":"Rodríguez Machado A et al.","pubmed_publication_date":"20 May 2024","pubmed_entrez_date":"2024-05-25","publication_year":"2024","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2024-05-25 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23907116","title":"Proteasome-dependent degradation of replisome components regulates faithful DNA replication.","citation":"Cell Cycle 2013 Aug 15;12(16):2564-9","abstract":"The replication machinery, or the replisome, collides with a variety of obstacles during the normal process of DNA replication. In addition to damaged template DNA, numerous chromosome regions are considered to be difficult to replicate owing to the presence of DNA secondary structures and DNA-binding proteins. Under these conditions, the replication fork stalls, generating replication stress. Stalled forks are prone to collapse, posing serious threats to genomic integrity. It is generally thought that the replication checkpoint functions to stabilize the replisome and replication fork structure upon replication stress. This is important in order to allow DNA replication to resume once the problem is solved. However, our recent studies demonstrated that some replisome components undergo proteasome-dependent degradation during DNA replication in the fission yeast Schizosaccharomyces pombe. Our investigation has revealed the involvement of the SCF(Pof3) (Skp1-Cullin/Cdc53-F-box) ubiquitin ligase in replisome regulation. We also demonstrated that forced accumulation of the replisome components leads to abnormal DNA replication upon replication stress. Here we review these findings and present additional data indicating the importance of replisome degradation for DNA replication. Our studies suggest that cells activate an alternative pathway to degrade replisome components in order to preserve genomic integrity.","doi":"10.4161/cc.25692","authors":"Roseaulin LC, Noguchi C, Noguchi E","authors_abbrev":"Roseaulin LC et al.","pubmed_publication_date":"15 Aug 2013","pubmed_entrez_date":"2013-08-03","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18574244","title":"A flexible template boundary element in the RNA subunit of fission yeast telomerase.","citation":"J Biol Chem 2008 Aug 29;283(35):24224-33","abstract":"Telomerase adds telomeric repeat sequences to chromosome ends using a short region of its RNA subunit as a template. Telomerase RNA subunits are phylogenetically highly divergent, and different strategies have evolved to demarcate the boundary of the template region. The recent identification of the gene encoding telomerase RNA in the fission yeast Schizosaccharomyces pombe (ter1+) has opened the door for structure-function analyses in a model that shares many features with the telomere maintenance machinery of higher eukaryotes. Here we describe a structural element in TER1 that defines the 5' boundary of the template. Disruption of a predicted long range base pairing interaction between template-adjacent nucleotides and a sequence further upstream resulted in reverse transcription beyond the template region and caused telomere shortening. Normal telomere length was restored by combining complementary nucleotide substitutions in both elements, showing that base pairing, not a specific sequence, limits reverse transcription beyond the template. The template boundary described here resembles that of budding yeasts and some mammalian telomerases. However, unlike any previously characterized boundary element, part of the paired region overlaps with the template itself, thus necessitating disruption of these interactions during most reverse transcription cycles. We show that changes in the paired region directly affect the length of individual telomeric repeat units. Our data further illustrate that marginal alignment of the telomeric 3' end with RNA sequences downstream of the template is responsible for primer slippage, causing incorporation of strings of guanosines at the start of a subset of repeats.","doi":"10.1074/jbc.M802043200","authors":"Box JA, Bunch JT, Zappulla DC, Glynn EF, Baumann P","authors_abbrev":"Box JA et al.","pubmed_publication_date":"29 Aug 2008","pubmed_entrez_date":"2008-06-25","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11927555","title":"The fission yeast NIMA kinase Fin1p is required for spindle function and nuclear envelope integrity.","citation":"EMBO J 2002 Apr 02;21(7):1713-22","abstract":"NIMA kinases appear to be the least functionally conserved mitotic regulators, being implicated in chromosome condensation in fungi and in spindle function in metazoans. We demonstrate here that the fission yeast NIMA homologue, Fin1p, can induce profound chromosome condensation in the absence of the condensin and topoisomerase II, indicating that Fin1p-induced condensation differs from mitotic condensation. Fin1p expression is transcriptionally and post-translationally cell cycle-regulated, with Fin1p kinase activity maximal from the metaphase-anaphase transition to G(1). Fin1p is localized to the spindle pole body and fin1Delta cells are hypersensitive to anti-microtubule drugs, synthetically lethal with a number of spindle mutants and require the spindle checkpoint for viability. Moreover, fin1Delta cells show unusual and extensive elaborations of the nuclear envelope. These data support a role for Fin1p in spindle function and nuclear envelope transactions at or after the metaphase-anaphase transition that may be generally applicable to other NIMA-family members.","authors":"Krien MJ, West RR, John UP, Koniaras K, McIntosh JR, O'Connell MJ","authors_abbrev":"Krien MJ et al.","pubmed_publication_date":"02 Apr 2002","pubmed_entrez_date":"2002-04-03","publication_year":"2002","canto_session_key":"7ac7ea383ba244b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-08 12:02:08","canto_approved_date":"2025-09-03 20:03:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-12 11:56:07","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.03c","SPAC1786.03","SPBC146.03c","SPCC338.17c","SPBC557.03c","SPBC649.05","SPAC19E9.02","SPBP4H10.06c","SPCC962.03c","SPCC1322.12c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2021-01-08"},{"uniquename":"PMID:7992504","title":"Codon usage table for Schizosaccharomyces pombe.","citation":"Yeast 1994 Aug;10(8):1045-7","abstract":"","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28718400","title":"Histone H3G34R mutation causes replication stress, homologous recombination defects and genomic instability in  S. pombe .","citation":"Elife 2017 Jul 18;6","abstract":"Recurrent somatic mutations of  H3F3A  in aggressive pediatric high-grade gliomas generate K27M or G34R/V mutant histone H3.3. H3.3-G34R/V mutants are common in tumors with mutations in p53 and ATRX, an H3.3-specific chromatin remodeler. To gain insight into the role of H3-G34R, we generated fission yeast that express only the mutant histone H3. H3-G34R specifically reduces H3K36 tri-methylation and H3K36 acetylation, and mutants show partial transcriptional overlap with  set2  deletions. H3-G34R mutants exhibit genomic instability and increased replication stress, including slowed replication fork restart, although DNA replication checkpoints are functional. H3-G34R mutants are defective for DNA damage repair by homologous recombination (HR), and have altered HR protein dynamics in both damaged and untreated cells. These data suggest H3-G34R slows resolution of HR-mediated repair and that unresolved replication intermediates impair chromosome segregation. This analysis of H3-G34R mutant fission yeast provides mechanistic insight into how G34R mutation may promote genomic instability in glioma.","doi":"10.7554/eLife.27406","authors":"Yadav RK, Jablonowski CM, Fernandez AG, Lowe BR, Henry RA, Finkelstein D, Barnum KJ, Pidoux AL, Kuo YM, Huang J, O'Connell MJ, Andrews AJ, Onar-Thomas A, Allshire RC, Partridge JF","authors_abbrev":"Yadav RK et al.","pubmed_publication_date":"18 Jul 2017","pubmed_entrez_date":"2017-07-19","publication_year":"2017","canto_session_key":"c30103543fc9385a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-07-21 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11E3.04c","SPAC29B12.02c","SPBC582.05c","SPCC5E4.06","SPBC29A10.15","SPBC1105.11c","SPCC126.02c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:25965521","title":"Ku stabilizes replication forks in the absence of Brc1.","citation":"PLoS One 2015;10(5):e0126598","abstract":"DNA replication errors are a major source of genome instability in all organisms. In the fission yeast Schizosaccharomyces pombe, the DNA damage response protein Brc1 binds phospho-histone H2A (γH2A)-marked chromatin during S-phase, but how Brc1 protects genome integrity remains unclear. Here we report that the non-homologous end-joining (NHEJ) protein Ku becomes critical for survival of replication stress in brc1∆ cells. Ku's protective activity in brc1∆ cells does not involve its canonical NHEJ function or its roles in protecting telomeres or shielding DNA ends from Exo1 exonuclease. In brc1∆ pku80∆ cells, nuclear foci of Rad52 homologous recombination (HR) protein increase and Mus81-Eme1 Holliday junction resolvase becomes critical, indicating increased replication fork instability. Ku's localization at a ribosomal DNA replication fork barrier associated with frequent replisome-transcriptosome collisions increases in brc1∆ cells and increased collisions correlate with an enhanced requirement for Brc1. These data indicate that Ku stabilizes replication forks in the absence of Brc1.","doi":"10.1371/journal.pone.0126598","authors":"Sánchez A, Russell P","authors_abbrev":"Sánchez A et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-05-13","publication_year":"2015","canto_session_key":"2415808f7b13c5d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Arancha Sanchez","canto_first_approved_date":"2016-08-26 10:11:30","canto_approved_date":"2025-09-03 19:39:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-06 19:27:35","canto_added_date":"2015-05-14 00:19:11","annotation_curators":[{"name":"Arancha Sanchez","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":73,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.08","SPBC543.03c","SPCC4G3.05c","SPBC582.05c","SPBC30D10.04","SPCC126.02c","SPBC29A10.05","SPCC1183.05c","SPBC216.06c","SPAC2G11.12"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2016-08-26"},{"uniquename":"PMID:14718525","title":"Tsc1+ and tsc2+ regulate arginine uptake and metabolism in Schizosaccharomyces pombe.","citation":"J Biol Chem 2004 Mar 26;279(13):12706-13","abstract":"Mutations in either TSC1 or TSC2 cause tuberous sclerosis complex, an autosomal dominant disorder characterized by seizures, mental retardation, and benign tumors of the skin, brain, heart, and kidneys. Homologs for the TSC1 and TSC2 genes have been identified in mouse, rat, Fugu, Drosophila, and in the yeast Schizosaccharomyces pombe. Here we show that S. pombe lacking tsc1+ or tsc2+ have similar phenotypes including decreased arginine uptake, decreased expression of three amino acid permeases, and low intracellular levels of four members of the arginine biosynthesis pathway. Recently, the small GTPase Rheb was identified as a target of the GTPase-activating domain of tuberin in mammalian cells and in Drosophila. We show that the defect in arginine uptake in cells lacking tsc2+ is rescued by the expression of a dominant negative form of rhb1+, the Rheb homolog in S. pombe, but not by expressing wild-type rhb1+. Expression of the tsc2+ gene with a patient-derived mutation within the GAP domain did not rescue the arginine uptake defect in tsc2+ mutant yeast. Taken together, these findings support a model in which arginine uptake is regulated through tsc1+, tsc2+, and rhb1+ in S. pombe and also suggest a role for the Tsc1 and Tsc2 proteins in amino acid biosynthesis and sensing.","authors":"van Slegtenhorst M, Carr E, Stoyanova R, Kruger WD, Henske EP","authors_abbrev":"van Slegtenhorst M et al.","pubmed_publication_date":"26 Mar 2004","pubmed_entrez_date":"2004-01-14","publication_year":"2004","canto_session_key":"d616690bf410cea4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-05-28 16:37:07","canto_approved_date":"2024-07-15 11:53:45","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-10-25 11:26:14","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":52,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC869.10c","SPBC1A4.02c","SPCC330.05c","SPBC428.16c","SPAC1039.09","SPAP7G5.06","SPBC29A3.02c","SPAC630.13c","SPAC22F3.13","SPCC1322.13"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2017-05-28"},{"uniquename":"PMID:17346842","title":"Yeast-based screening to identify modulators of G-protein signaling using uncontrolled cell division cycle by overexpression of Stm1.","citation":"J Biotechnol 2007 May 01;129(3):547-54","abstract":"Stm1, a G-protein coupled receptor, which senses nutritional state drives cells to stop the proliferative cell cycle and enter meiosis under nutritionally deficient conditions in Schizosaccharomyces pombe. It was shown that overexpression of Stm1 led growth inhibition and uncontrolled mitotic haploidization presumably by the premature initiation of mitosis. Sty1 and Gpa2 seem to play important roles for Stm1 to deliver starvation signal to induce downstream function. Based on the observation that conversion of diploid to haploid by overexpression of Stm1 can be easily detected as pink or red colonies in the media containing low adenine, HTS drug screening system to identify modulators of GPCR was established and tested using 413 compounds. Four very potent modulators of GPCR including Biochanin A, which possess strong inhibitory activity against uncontrolled cell division, were identified in this screening. This study provides the yeast-based platform that allows robust cellular assays to identify novel modulators of G-protein signaling and MAP kinase pathway.","authors":"Chung KS, Won M, Lee JJ, Ahn J, Hoe KL, Kim DU, Song KB, Yoo HS","authors_abbrev":"Chung KS et al.","pubmed_publication_date":"01 May 2007","pubmed_entrez_date":"2007-03-10","publication_year":"2007","canto_session_key":"1f1a8cf7c52d27d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-01-31 09:47:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-30 15:06:58","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPAC23H3.13c","SPAC24B11.06c","SPAC17C9.10"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2012-11-30"},{"uniquename":"PMID:3870979","title":"ran1+ controls the transition from mitotic division to meiosis in fission yeast.","citation":"Curr Genet 1985;10(4):297-311","abstract":"We have investigated the genetic and physiological control of meiosis in fission yeast. Nutritionally depleted h+/h- diploid cells become irreversibly commited to meiosis immediately prior to the initiation of premeiotic S phase. Premeiotic DNA synthesis requires matP+, matM+, mei2+ and mei3+ but not the mitotic cell cycle control gene, cdc2+. ran1+ is an essential gene, loss of which provokes sexual conjugation, premeiotic DNA synthesis, pseudo-meiosis and the sporulation of haploid cells. Our experiments suggest that sexual differentiation is achieved physiologically by the inhibition of ran1+ activity in a two-step process. In the first step, partial inhibition of ran1+ in starved haploid cells, leads to cell cycle arrest in G1 followed by sexual conjugation. In the second step, a pathway requiring the matP+, matM+ and mei3+ genes of the newly-formed zygote, further inhibits ran1+ and thereby commits the cell to meiosis. mei2+ is required for meiotic commitment after full inhibition of ran1+. ran1+ is normally essential for vegetative cell reproduction but is inessential in cells which have abnormally high levels of cAMP-dependent protein kinase. We propose that the ran1+ gene encodes a highly controlled protein kinase which shares key substrates with cAMP-dependent protein kinase.","authors":"Beach D, Rodgers L, Gould J","authors_abbrev":"Beach D et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_session_key":"cfa1ac27dc7acf6c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-10-08 17:15:31","canto_approved_date":"2024-06-28 11:01:59","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-07-18 16:33:52","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.11","SPBC11B10.09","SPBC19C2.05","SPBC119.04","SPAC27D7.03c","SPBC336.12c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-10-08"},{"uniquename":"PMID:26237280","title":"Regulation of Ace2-dependent genes requires components of the PBF complex in Schizosaccharomyces pombe.","citation":"Cell Cycle 2015;14(19):3124-37","abstract":"The division cycle of unicellular yeasts is completed with the activation of a cell separation program that results in the dissolution of the septum assembled during cytokinesis between the 2 daughter cells, allowing them to become independent entities. Expression of the eng1(+) and agn1(+) genes, encoding the hydrolytic enzymes responsible for septum degradation, is activated at the end of each cell cycle by the transcription factor Ace2. Periodic ace2(+) expression is regulated by the transcriptional complex PBF (PCB Binding Factor), composed of the forkhead-like proteins Sep1 and Fkh2 and the MADS box-like protein Mbx1. In this report, we show that Ace2-dependent genes contain several combinations of motifs for Ace2 and PBF binding in their promoters. Thus, Ace2, Fkh2 and Sep1 were found to bind in vivo to the eng1(+) promoter. Ace2 binding was coincident with maximum level of eng1(+) expression, whereas Fkh2 binding was maximal when mRNA levels were low, supporting the notion that they play opposing roles. In addition, we found that the expression of eng1(+) and agn1(+) was differentially affected by mutations in PBF components. Interestingly, agn1(+) was a major target of Mbx1, since its ectopic expression resulted in the suppression of Mbx1 deletion phenotypes. Our results reveal a complex regulation system through which the transcription factors Ace2, Fkh2, Sep1 and Mbx1 in combination control the expression of the genes involved in separation at the end of the cell division cycle.","doi":"10.1080/15384101.2015.1078035","authors":"Suárez MB, Alonso-Nuñez ML, del Rey F, McInerny CJ, Vázquez de Aldana CR","authors_abbrev":"Suárez MB et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-08-04","publication_year":"2015","canto_session_key":"69595171b25482f3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-05 00:19:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16G5.15c","SPBC19G7.06"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:14713954","title":"Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with intron RNA.","citation":"EMBO J 2004 Jan 28;23(2):376-85","abstract":"Communication between U1 and U2 snRNPs is critical during pre-spliceosome assembly; yet, direct connections have not been observed. To investigate this assembly step, we focused on Prp5, an RNA-dependent ATPase of the DExD/H family. We identified homologs of Saccharomyces cerevisiae Prp5 in humans (hPrp5) and Schizosaccharomyces pombe (SpPrp5), and investigated their interactions and function. Depletion and reconstitution of SpPrp5 from extracts demonstrate that ATP binding and hydrolysis by Prp5 are required for pre-spliceosome complex A formation. hPrp5 and SpPrp5 are each physically associated with both U1 and U2 snRNPs; Prp5 contains distinct U1- and U2-interacting domains that are required for pre-spliceosome assembly; and, we observe a Prp5-associated U1/U2 complex in S. pombe. Together, these data are consistent with Prp5 being a bridge between U1 and U2 snRNPs at the time of pre-spliceosome formation.","authors":"Xu YZ, Newnham CM, Kameoka S, Huang T, Konarska MM, Query CC","authors_abbrev":"Xu YZ et al.","pubmed_publication_date":"28 Jan 2004","pubmed_entrez_date":"2004-01-10","publication_year":"2004","canto_session_key":"7382bd45d9fc4175","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-15 15:26:40","canto_approved_date":"2021-06-16 14:26:08","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-15 15:26:34","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC10H11.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-15"},{"uniquename":"PMID:41759732","title":"The AAA-ATPase Yta4 inhibits the interaction between Ppa2 and Atg43 to promote Atg43 phosphorylation and mitophagy.","citation":"J Biol Chem 2026 Feb 25;:111326","abstract":"AAA-ATPase Yta4/Msp1/ATAD1 is a well-known quality control factor that clears mistargeted tail-anchored proteins and precursor proteins on mitochondria. However, whether Yta4 preserves mitochondrial homeostasis through alternate pathways remains unclear. Traditionally, mitophagy has been recognized as a crucial pathway for eliminating dysfunctional mitochondria, thereby ensuring the maintenance of mitochondrial homeostasis. In this study, we unveil a novel role for Yta4 in sustaining mitochondrial homeostasis by facilitating mitophagy in fission yeast. The absence of Yta4 delays the phosphorylation of the mitophagy receptor Atg43 and specifically inhibits mitophagy. Additionally, Atg43 phosphorylation sites Ser32, Ser35, and Ser36, which are crucial for mitophagy, were identified. We further found that the phosphatase Ppa2 plays a major role in Atg43 dephosphorylation and inhibits excessive mitophagy. Yta4 physically interacts with both Atg43 and Ppa2, and coordinates with Ppa2 to modulate Atg43 phosphorylation and mitophagy. Moreover, Yta4 and Ppa2 bind to the same cytosolic region of Atg43, and Yta4 inhibits the interaction between Atg43 and Ppa2. Collectively, our findings suggest that Yta4 promotes mitophagy by ensuring the effectiveness of Atg43 phosphorylation. Thus, our findings reveal the novel function of Yta4 in regulating mitophagy and expand the understanding of the molecular mechanisms underlying mitophagy in fission yeast.","doi":"10.1016/j.jbc.2026.111326","authors":"Liu K, He J, Wu Y, Zhao C, Yan S, Xiong F, Liu X, Yao X, Fu C","authors_abbrev":"Liu K et al.","pubmed_publication_date":"25 Feb 2026","pubmed_entrez_date":"2026-02-27","publication_year":"2026","canto_session_key":"36d48c38f3e5c7a5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-01 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12589679","title":"Role of the two type II myosins, Myo2 and Myp2, in cytokinetic actomyosin ring formation and function in fission yeast.","citation":"Cell Motil Cytoskeleton 2003 Mar;54(3):208-16","abstract":"The formation and contraction of a cytokinetic actomyosin ring (CAR) is essential for the execution of cytokinesis in fission yeast. Unlike most organisms in which its composition has been investigated, the fission yeast CAR contains two type II myosins encoded by the genes myo2(+) and myp2(+). myo2(+) is an essential gene whilst myp2(+) is dispensable under normal growth conditions. Myo2 is hence the major contractile protein of the CAR whilst Myp2 plays a more subtle and, as yet, incompletely documented role. Using a fission yeast strain in which the chromosomal copy of the myo2(+) gene is fused to the gene encoding green fluorescent protein (GFP), we analysed CAR formation and function in the presence and absence of Myp2. No change in the rate of CAR contraction was observed when Myp2 was absent although the CAR persisted longer in the contracted state and was occasionally observed to split into two discrete rings. This was also observed in myp2Delta cells following actin depolymerisation with latrunculin. CAR contraction in the absence of Myp2 was completely abolished in the presence of elevated levels of chloride ions. Thus, Myp2 appears to contribute to the stability of the CAR, in particular at a late stage of CAR contraction, and to be a component of the signalling pathway that regulates cytokinesis in response to elevated levels of chloride. To determine whether the presence of two type II myosins was a feature of cytokinesis in other fungi that divide by septation, we searched the genomes of two filamentous fungi, Aspergillus fumigatus and Neurospora crassa, for myosin genes. As in fission yeast, both A. fumigatus and N. crassa contained myosins of classes I, II, and V. Unlike fission yeast, both contained a single type II myosin gene that, on the basis of its tail structure, was more reminiscent of Myp2 than Myo2. The significance of these observations to our understanding of septum to formation and cleavage is discussed.","authors":"Mulvihill DP, Hyams JS","authors_abbrev":"Mulvihill DP et al.","pubmed_publication_date":"Mar 2003","pubmed_entrez_date":"2003-02-18","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36622644","title":"A force balance model for a cell size-dependent meiotic nuclear oscillation in fission yeast.","citation":"EMBO Rep 2023 Mar 06;24(3):e55770","abstract":"Fission yeast undergoes premeiotic nuclear oscillation, which is dependent on microtubules and is driven by cytoplasmic dynein. Although the molecular mechanisms have been analyzed, how a robust oscillation is generated despite the dynamic behaviors of microtubules has yet to be elucidated. Here, we show that the oscillation exhibits cell length-dependent frequency and requires a balance between microtubule and viscous drag forces, as well as proper microtubule dynamics. Comparison of the oscillations observed in living cells with a simulation model based on microtubule dynamic instability reveals that the period of oscillation correlates with cell length. Genetic alterations that reduce cargo size suggest that the nuclear movement depends on viscous drag forces. Deletion of a gene encoding Kinesin-8 inhibits microtubule catastrophe at the cell cortex and results in perturbation of oscillation, indicating that nuclear movement also depends on microtubule dynamic instability. Our findings link numerical parameters from the simulation model with cellular functions required for generating the oscillation and provide a basis for understanding the physical properties of microtubule-dependent nuclear movements.","doi":"10.15252/embr.202255770","authors":"Fujita I, Kimura A, Yamashita A","authors_abbrev":"Fujita I et al.","pubmed_publication_date":"06 Mar 2023","pubmed_entrez_date":"2023-01-09","publication_year":"2023","canto_session_key":"3d429976b2be1924","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-01-10 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8114734","title":"The rad16 gene of Schizosaccharomyces pombe: a homolog of the RAD1 gene of Saccharomyces cerevisiae.","citation":"Mol Cell Biol 1994 Mar;14(3):2029-40","abstract":"The rad10, rad16, rad20, and swi9 mutants of the fission yeast Schizosaccharomyces pombe, isolated by their radiation sensitivity or abnormal mating-type switching, have been shown previously to be allelic. We have cloned DNA correcting the UV sensitivity or mating-type switching phenotype of these mutants and shown that the correcting DNA is encompassed in a single open reading frame. The gene, which we will refer to as rad16, is approximately 3 kb in length, contains seven introns, and encodes a protein of 892 amino acids. It is not essential for viability of S. pombe. The predicted protein is the homolog of the Saccharomyces cerevisiae RAD1 protein, which is involved in an early step in excision-repair of UV damage from DNA. The approximately 30% sequence identity between the predicted proteins from the two yeasts is distributed throughout the protein. Two-hybrid experiments indicate a strong protein-protein interaction between the products of the rad16 and swi10 genes of S. pombe, which mirrors that reported for RAD1 and RAD10 in S. cerevisiae. We have identified the mutations in the four alleles of rad16. They mapped to the N-terminal (rad10), central (rad20), and C-terminal (rad16 and swi9) regions. The rad10 and rad20 mutations are in the splice donor sequences of introns 2 and 4, respectively. The plasmid correcting the UV sensitivity of the rad20 mutation was missing the sequence corresponding to the 335 N-terminal amino acids of the predicted protein. Neither smaller nor larger truncations were, however, able to correct its UV sensitivity.","authors":"Carr AM, Schmidt H, Kirchhoff S, Muriel WJ, Sheldrick KS, Griffiths DJ, Basmacioglu CN, Subramani S, Clegg M, Nasim A","authors_abbrev":"Carr AM et al.","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_session_key":"ba1b22d9edc02826","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-30 14:56:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-23 12:53:15","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.01","SPBC4F6.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-10-23"},{"uniquename":"PMID:33648190","title":"The deletion of Schizosaccharomyces pombe decreased the production of flavor-related metabolites during traditional Baijiu fermentation.","citation":"Food Res Int 2021 Feb;140:109872","abstract":"The microbiota in traditional solid-state fermentation is a complex microbiota that plays a key role in the production of feed, fuel, food and pharmaceutical products. The function of microbiota is an important factor dictating the quantity and quality of products. Core functional species play key metabolic roles in the microbiota, and their disappearance could result in the abnormal fermentation process. In this work, we combined Baijiu production and laboratory experiments to explore the keystone microbes and their metabolites. We found the deletion of core functional microbe resulted in the loss of multiple metabolites involved many alcohols and acids. In the traditional Baijiu production, the absence or appearance of Schizosaccharomyces pombe caused the content divergence in 227 flavor-related metabolites, especially in ethanol, butanol and pentanoic acid between abnormal and normal group (each content > 1 mg/kg and the content ratio of normal/abnormal group > 2). Schi. pombe increased the expression level of related genes involving alcohol dehydrogenase (ADH), acyl-CoA oxidase (ACOX) and trans-2-enoyl-CoA reductase (TER). Moreover, in the verification experiment of laboratory, the absence or appearance of Schizosaccharomyces pombe C-11 caused the content divergence in 136 flavor-related metabolites, especially in ethanol, butanol and pentanoic acid between Sp- and Sp+ group (each content > 1 mg/kg and the content ratio of Sp+/Sp- group > 2). Our results identified specific member that were essential for the function of fermentation microbiota. This study also suggests species deletions from fermentation microbiota and synthetic consortium could be a useful approach to illustrate relevant microbe-metabolites association and defining metabolic roles in the traditional solid-state fermentation.","doi":"10.1016/j.foodres.2020.109872","authors":"Du H, Song Z, Zhang M, Nie Y, Xu Y","authors_abbrev":"Du H et al.","pubmed_publication_date":"Feb 2021","pubmed_entrez_date":"2021-03-02","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-03-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18235227","title":"Fission yeast TOR complex 2 activates the AGC-family Gad8 kinase essential for stress resistance and cell cycle control.","citation":"Cell Cycle 2008 Feb 01;7(3):358-64","abstract":"Members of the mitogen-activated protein kinase (MAPK) subfamily responsive to environmental stress stimuli are known as SAPKs (stress-activated protein kinases), which are conserved from yeast to humans. In the fission yeast Schizosaccharomyces pombe, Spc1/Sty1 SAPK is activated by diverse forms of stress, such as osmostress, oxidative stress and heat shock, and induces gene expression through the Atf1 transcription factor. Sin1 (SAPK interacting protein 1) was originally isolated as a protein that interacts with Spc1, and its orthologs were also found in diverse eukaryotes. Here we report that Sin1 is not required for the stress gene expression regulated by Spc1 and Atf1, and that Sin1 is an essential component of TOR (target of rapamycin) complex 2 (TORC2). TORC2 is not essential for cell viability in S. pombe but plays important roles in cellular survival of stress conditions through phosphorylation and activation of an AGC-family protein kinase, Gad8. In addition, inactivation of Gad8 results in a synthetic growth defect with cdc25-22, a temperature-sensitive mutation of the Cdc25 phosphatase that activates Cdc2 kinase at G(2)/M. Gad8 also positively regulates expression of the CDK inhibitor gene rum1+, which is essential for cell cycle arrest in G(1) after nitrogen starvation. These results strongly suggest that the TORC2-Gad8 pathway has multiple physiological functions in cellular stress resistance and cell cycle progression at both G(1)/S and G(2)/M transitions.","authors":"Ikeda K, Morigasaki S, Tatebe H, Tamanoi F, Shiozaki K","authors_abbrev":"Ikeda K et al.","pubmed_publication_date":"01 Feb 2008","pubmed_entrez_date":"2008-02-01","publication_year":"2008","canto_session_key":"521475f7c063d784","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-05-30 22:48:36","canto_approved_date":"2021-06-14 06:58:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-05 16:45:53","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":50,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC24B11.06c","SPAC19D5.01","SPBC21B10.05c","SPBC32F12.09","SPCC24B10.07","SPAPYUG7.02c","SPAC1783.07c","SPBC215.05","SPBC16G5.15c","SPBC3F6.03","SPBC12C2.02c","SPAC24H6.05","SPBC30D10.10c"],"gene_count":14,"ltp_gene_count":9,"approved_date":"2016-05-30"},{"uniquename":"PMID:1655416","title":"Phosphorylation at Thr167 is required for Schizosaccharomyces pombe p34cdc2 function.","citation":"EMBO J 1991 Nov;10(11):3297-309","abstract":"Eukaryotic cell cycle progression requires the periodic activation and inactivation of a protein-serine/threonine kinase which in fission yeast is encoded by the cdc2+ gene. The activity of this gene product, p34cdc2, is controlled by numerous interactions with other proteins and by its phosphorylation state. In fission yeast, p34cdc2 is phosphorylated on two sites, one of which has been identified as Tyr15. Dephosphorylation of Tyr15 regulates the initiation of mitosis. To understand more completely the regulation of p34cdc2 kinase activity, we have identified the second site of phosphorylation as Thr167, a residue conserved amongst all p34cdc2 homologues. By analysing the phenotypes of cells expressing various position 167 mutations and performing in vitro experiments, we establish that Thr167 phosphorylation is required for p34cdc2 kinase activity at mitosis and is involved in the association of p34cdc2 with cyclin B. Dephosphorylation of Thr167 might also play a role in the exit from mitosis.","authors":"Gould KL, Moreno S, Owen DJ, Sazer S, Nurse P","authors_abbrev":"Gould KL et al.","pubmed_publication_date":"Nov 1991","pubmed_entrez_date":"1991-11-01","publication_year":"1991","canto_session_key":"29300b31506c9419","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-08-16 16:06:58","canto_approved_date":"2022-08-03 09:11:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-31 09:27:14","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-08-16"},{"uniquename":"EMBL:SPDMF1","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17028240","title":"Reciprocal nuclear shuttling of two antagonizing Zn finger proteins modulates Tup family corepressor function to repress chromatin remodeling.","citation":"Eukaryot Cell 2006 Dec;5(12):1980-9","abstract":"The Schizosaccharomyces pombe global corepressors Tup11 and Tup12, which are orthologs of Saccharomyces cerevisiae Tup1, are involved in glucose-dependent transcriptional repression and chromatin alteration of the fbp1+ gene. The fbp1+ promoter contains two regulatory elements, UAS1 and UAS2, one of which (UAS2) serves as a binding site for two antagonizing C2H2 Zn finger transcription factors, the Rst2 activator and the Scr1 repressor. In this study, we analyzed the role of Tup proteins and Scr1 in chromatin remodeling at fbp1+ during glucose repression. We found that Scr1, cooperating with Tup11 and Tup12, functions to maintain the chromatin of the fbp1+ promoter in a transcriptionally inactive state under glucose-rich conditions. Consistent with this notion, Scr1 is quickly exported from the nucleus to the cytoplasm at the initial stage of derepression, immediately after glucose starvation, at which time Rst2 is known to be imported into the nucleus. In addition, chromatin immunoprecipitation assays revealed a switching of Scr1 to Rst2 bound at UAS2 during glucose derepression. On the other hand, Tup11 and Tup12 persist in the nucleus and bind to the fbp1+ promoter under both derepressed and repressed conditions. These observations suggest that Tup1-like proteins recruited to the fbp1+ promoter are controlled by either of two antagonizing C2H2 Zn finger proteins. We propose that the actions of Tup11 and Tup12 are regulated by reciprocal nuclear shuttling of the two antagonizing Zn finger proteins in response to the extracellular glucose concentration. This notion provides new insights into the molecular mechanisms of the Tup family corepressors in gene regulation.","authors":"Hirota K, Hoffman CS, Ohta K","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-10-10","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.14c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:16252005","title":"Transactivation of Schizosaccharomyces pombe cdt2+ stimulates a Pcu4-Ddb1-CSN ubiquitin ligase.","citation":"EMBO J 2005 Nov 16;24(22):3940-51","abstract":"Cullin-4 forms a scaffold for multiple ubiquitin ligases. In Schizosaccharomyces pombe, the Cullin-4 homologue (Pcu4) physically associates with Ddb1 and the COP9 signalosome (CSN). One target of this complex is Spd1. Spd1 regulates ribonucleotide reductase (RNR) activity. Spd1 degradation during S phase, or following DNA damage of G2 cells, results in the nuclear export of the small RNR subunit. We demonstrate that Cdt2, an unstable WD40 protein, is a regulatory subunit of Pcu4-Ddb1-CSN ubiquitin ligase. cdt2 deletion stabilises Spd1 and prevents relocalisation of the small RNR subunit from the nucleus to the cytoplasm. cdt2+ is periodically transcribed by the Cdc10/DSC1 transcription factor during S phase and transiently transcribed following DNA damage of G2 cells, corresponding to Spd1 degradation profiles. Cdt2 co-precipitates with Spd1, and Cdt2 overexpression results in constitutive Spd1 degradation. We propose that Cdt2 incorporation into the Pcu4-Ddb1-CSN complex prompts Spd1 targeting and subsequent degradation and that Cdt2 is a WD40 repeat adaptor protein for Cullin-4-based ubiquitin ligase.","authors":"Liu C, Poitelea M, Watson A, Yoshida SH, Shimoda C, Holmberg C, Nielsen O, Carr AM","authors_abbrev":"Liu C et al.","pubmed_publication_date":"16 Nov 2005","pubmed_entrez_date":"2005-10-28","publication_year":"2005","canto_session_key":"5251feea6fc8d5fc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-01-02 13:08:15","canto_approved_date":"2021-12-21 07:56:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-12-20 12:54:08","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":51,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_16252005_phaf.tsv"}],"genes":["SPAC17H9.10c","SPAC22A12.03c","SPBC215.03c","SPBC16G5.01","SPBC25D12.04","SPBC25H2.12c","SPAC1687.13c","SPBC12D12.03","SPCC18B5.11c","SPBC216.05","SPBC12D12.08c","SPAC3A11.08","SPBC409.05","SPBC646.11","SPBC106.06","SPAC24H6.03","SPAC17H9.19c","SPCC1259.13","SPAPB17E12.04c","SPAC29B12.03"],"gene_count":20,"ltp_gene_count":19,"approved_date":"2018-01-02"},{"uniquename":"PMID:1807828","title":"The mating type in fission yeast is switched independently of its expression.","citation":"Curr Genet 1991 Nov;20(5):379-83","abstract":"The mating type of fission yeast is determined by the mat1 locus on chromosome II. The sequence content of this locus, and hence the mating type, is switched in a strictly regular pattern by transposition from one of two unexpressed mating type sequences. The expressed and the two silent sequences are located on the same chromosome. It is not understood how one of the two donor sequences is selected in this reaction. Here I test the possibility that the selection is governed by gene expression from the mat1 locus. Such a mechanism could favor transposition of a donor sequence of opposite mating type to the one present at mat1. Alternatively it could disfavor transposition of a synonymous sequence. The present data argue strongly against any type of participation of mat1 gene products in the choice of donor during the mating type switch. Alternative steering mechanisms are discussed.","authors":"Ruusala T","authors_abbrev":"Ruusala T","pubmed_publication_date":"Nov 1991","pubmed_entrez_date":"1991-11-01","publication_year":"1991","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23999616","title":"Swapping CENP-A at the centromere.","citation":"Nat Cell Biol 2013 Sep;15(9):1028-30","abstract":"Faithful genome segregation depends on the functions of the eukaryotic centromere, which is characterized by the histone variant CENP-A. Gene replacement in human cells and fission yeast has now been used to show how CENP-A biochemically encodes centromere identity, as well as reveal an unexpected role for CENP-B in centromere function.","doi":"10.1038/ncb2833","authors":"French BT, Straight AF","authors_abbrev":"French BT et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-09-04","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35752625","title":"Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1.","citation":"Nat Commun 2022 Jun 25;13(1):3650","abstract":"Neighbor of BRCA1 (Nbr1) is a conserved autophagy receptor that provides cargo selectivity to autophagy. The four-tryptophan (FW) domain is a signature domain of Nbr1, but its exact function remains unclear. Here, we show that Nbr1 from the filamentous fungus Chaetomium thermophilum uses its FW domain to bind the α-mannosidase Ams1, a cargo of selective autophagy in both budding yeast and fission yeast, and delivers Ams1 to the vacuole by conventional autophagy in heterologous fission yeast. The structure of the Ams1-FW complex was determined at 2.2 Å resolution by cryo-electron microscopy. The FW domain adopts an immunoglobulin-like β-sandwich structure and recognizes the quaternary structure of the Ams1 tetramer. Notably, the N-terminal di-glycine of Ams1 is specifically recognized by a conserved pocket of the FW domain. The FW domain becomes degenerated in fission yeast Nbr1, which binds Ams1 with a ZZ domain instead. Our findings illustrate the protein binding mode of the FW domain and reveal the versatility of Nbr1-mediated cargo recognition.","doi":"10.1038/s41467-022-31439-5","authors":"Zhang J, Wang YY, Pan ZQ, Li Y, Sui J, Du LL, Ye K","authors_abbrev":"Zhang J et al.","pubmed_publication_date":"25 Jun 2022","pubmed_entrez_date":"2022-06-25","publication_year":"2022","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2022-06-27 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33189720","title":"Stm1 is a vacuolar PQ-loop protein involved in the transport of basic amino acids in Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta Biomembr 2021 Feb 01;1863(2):183507","abstract":"The stm1 +  (SPAC17C9.10) gene of Schizosaccharomyces pombe is closely related to genes encoding vacuolar PQ-loop proteins, Ypq1, Ypq2, and Ypq3, of Saccharomyces cerevisiae. When stm1 +  fused with GFP was expressed in fission or budding yeast, Stm1-GFP localized at the vacuolar membrane. Isolated vacuolar membrane vesicles from S. cerevisiae cells overexpressing stm1 +  exhibited stm1 + -dependent arginine and lysine uptake activity. Exchange activity of arginine and histidine/arginine, as observed for Ypq2 of S. cerevisiae, was also detected in the vesicles expressing stm1 + . The expression levels of stm1 +  in S. pombe cells significantly affected the vacuolar contents of lysine, histidine, and arginine. These results suggest that Stm1 is a vacuolar PQ-loop protein involved in the transport of basic amino acids across the vacuolar membrane.","doi":"10.1016/j.bbamem.2020.183507","authors":"Kawano-Kawada M, Ueda T, Mori H, Ichimura H, Takegawa K, Sekito T","authors_abbrev":"Kawano-Kawada M et al.","pubmed_publication_date":"01 Feb 2021","pubmed_entrez_date":"2020-11-15","publication_year":"2021","canto_session_key":"9b69b88e5eb6d03d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-11-17 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17C9.10"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"EMBL:SPAB540","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32594847","title":"Proteomic analysis of meiosis and characterization of novel short open reading frames in the fission yeast  Schizosaccharomyces pombe .","citation":"Cell Cycle 2020 Jul;19(14):1777-1785","abstract":"Meiosis is the process by which haploid gametes are produced from diploid precursor cells. We used stable isotope labeling by amino acids in cell culture (SILAC) to characterize the meiotic proteome in the fission yeast  Schizosaccharomyces pombe . We compared relative levels of proteins extracted from cells harvested around meiosis I with those of meiosis II, and proteins from premeiotic S phase with the interval between meiotic divisions, when S phase is absent. Our proteome datasets revealed peptides corresponding to short open reading frames (sORFs) that have been previously identified by ribosome profiling as new translated regions. We verified expression of selected sORFs by Western blotting and analyzed the phenotype of deletion mutants. Our data provide a resource for studying meiosis that may help understand differences between meiosis I and meiosis II and how S phase is suppressed between the two meiotic divisions.","doi":"10.1080/15384101.2020.1779470","authors":"Huraiova B, Kanovits J, Polakova SB, Cipak L, Benko Z, Sevcovicova A, Anrather D, Ammerer G, Duncan CDS, Mata J, Gregan J","authors_abbrev":"Huraiova B et al.","pubmed_publication_date":"Jul 2020","pubmed_entrez_date":"2020-06-30","publication_year":"2020","canto_session_key":"35ce1fe63f12db9a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-09-29 18:26:10","canto_approved_date":"2020-09-29 18:26:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-29 18:26:02","canto_added_date":"2020-07-02 00:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC144.19"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-09-29"},{"uniquename":"PMID:7584421","title":"Genetic map construction with constraints.","citation":"Proc Int Conf Intell Syst Mol Biol 1994;2:78-86","abstract":"A pilot program, CME, is described for generating a physical genetic map from hybridization fingerprinting data. CME is implemented in the parallel constraint logic programming language ElipSys. The features of constraint logic programming are used to enable the integration of pre-existing mapping information (partial probe orders from cytogenetic maps and local physical maps) into the global map generation process, while parallelism enables the search space to be traversed more efficiently. CME was tested using data from chromosome 2 of Schizosaccharomyces pombe and was found able to generate maps as well as (and sometimes better than) a more traditional method. This paper illustrates the practical benefits of using a symbolic logic programming language and shows that the features of constraint handling and parallel execution bring the development of practical systems based on AI programming technologies nearer to being a reality.","authors":"Clark DA, Rawlings CJ, Doursenot S","authors_abbrev":"Clark DA et al.","pubmed_publication_date":"1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC02869","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12882583","title":"Functional over-expression of the Stm1 protein, a G-protein-coupled receptor, in Schizosaccharomyces pombe.","citation":"Biotechnol Lett 2003 Feb;25(3):267-72","abstract":"We report here the first functional over-expression of the Stm1 protein, a G-protein-coupled receptor with seven-trans-membrane spanning regions, in a homologous expression system without internal modification of the open reading frame of Stm1. The entire coding sequence, except for the termination codon followed by a C-terminal His6 tag, has been cloned into the pREP1 vector. The functionally active Stm1-His6 was over-expressed in Schizosaccharomyces pombe under the control of the nmt1 (no message in thiamine) promoter. The expression after induction was 120 times as much as that of control before induction and it gave approximately 500 ng protein/2 x 10(7) cells.","authors":"Chung KS, Kim DU, Ryoo SW, Kang EJ, Won M, Kim L, Jang YJ, Maeng PJ, Kim SC, Yoo HS, Hoe KL","authors_abbrev":"Chung KS et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-07-29","publication_year":"2003","canto_session_key":"1049db9c4e8922e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-06-27 12:21:24","canto_approved_date":"2019-12-10 16:54:52","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-02-22 15:31:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-06-27"},{"uniquename":"PMID:12972551","title":"Gef1p and Scd1p, the Two GDP-GTP exchange factors for Cdc42p, form a ring structure that shrinks during cytokinesis in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2003 Sep;14(9):3617-27","abstract":"Fission yeast Cdc42p, a small GTPase of the Rho family, is essential for cell proliferation and maintenance of the rod-like cell morphology. Scd1/Ral1p is a GDP-GTP exchange factor (GEF) for Cdc42p. This study and a parallel study by others establish that Gef1p is another GEF for Cdc42p. Deletions of gef1 and scd1 are synthetically lethal, generating round dead cells, and hence mimic the phenotype of cdc42 deletion. Gef1p is localized mainly to the cell division site. Scd1p is also there, but it is also detectable in other parts of the cell, including the nucleus, growing ends, and the tips of conjugation tubes. Gef1p and Scd1p form a ring structure at the cell division site, which shrinks during cytokinesis following the contraction of the actomyosin ring. Formation of the Gef1p/Scd1p ring apparently depends on the integrity of the actomyosin ring. In turn, recruitment of Cdc42p to the cell division site follows the shrinking Gef1p/Scd1p ring; the Cdc42p accumulates like a closing iris. These observations suggest that Gef1p and Scd1p may have a role in mediating between contraction of the actomyosin ring and formation of the septum, by recruiting active Cdc42p to the septation site.","authors":"Hirota K, Tanaka K, Ohta K, Yamamoto M","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-09-16","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.09","SPAC16E8.09","SPAC110.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:21402786","title":"Metabolic status rather than cell cycle signals control quiescence entry and exit.","citation":"J Cell Biol 2011 Mar 21;192(6):949-57","abstract":"Quiescence is defined as a temporary arrest of proliferation, yet it likely encompasses various cellular situations. Our knowledge about this widespread cellular state remains limited. In particular, little is known about the molecular determinants that orchestrate quiescence establishment and exit. Here we show that upon carbon source exhaustion, budding yeast can enter quiescence from all cell cycle phases. Moreover, using cellular structures that are candidate markers for quiescence, we found that the first steps of quiescence exit can be triggered independently of cell growth and proliferation by the sole addition of glucose in both Saccharomyces cerevisiae and Schizosaccharomyces pombe. Importantly, glucose needs to be internalized and catabolized all the way down to glycolysis to mobilize quiescent cell specific structures, but, strikingly, ATP replenishment is apparently not the key signal. Altogether, these findings strongly suggest that quiescence entry and exit primarily rely on cellular metabolic status and can be uncoupled from the cell cycle.","doi":"10.1083/jcb.201009028","authors":"Laporte D, Lebaudy A, Sahin A, Pinson B, Ceschin J, Daignan-Fornier B, Sagot I","authors_abbrev":"Laporte D et al.","pubmed_publication_date":"21 Mar 2011","pubmed_entrez_date":"2011-03-16","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39761853","title":"Regulation of sod1 mRNA and protein abundance by zinc in fission yeast is dependent on the CCR4-NOT complex.","citation":"J Biol Chem 2025 Jan 04;:108156","abstract":"Zinc is an essential micronutrient that serves as a cofactor in a wide variety of enzymes, including Cu-Zn Superoxide Dismutase 1 (Sod1). We have discovered in Schizosaccharomyces pombe that Sod1 mRNA and protein levels are regulated in response to cellular zinc availability. We demonstrate that lower levels of Sod1 mRNA and protein accumulate under low zinc conditions, and that this regulation does not require the sod1 promoter or known factors that regulate transcription of sod1 in response to zinc and other environmental stresses. Further analyses using yeast deletion strains and an inactive allele of Caf1 revealed that the reduced accumulation of sod1 mRNA and protein under low zinc conditions depends on the Caf1 and Ccr4 deadenylases of the CCR4-NOT complex. We also found that Caf1 and Ccr4 are both required for growth under zinc-limiting conditions. To gain additional mechanistic insight we used immunoblot analysis to map the regions required for the regulation of the Sod1 protein by zinc. We found that the sod1 ORF and 3'UTR are both necessary and sufficient for the zinc-dependent changes in Sod1 protein abundance. Collectively, our studies reveal a novel mechanism of altering mRNA and protein abundance in response to zinc status, which depends on the CCR4-NOT complex.","doi":"10.1016/j.jbc.2025.108156","authors":"Weeks AT, Bird AJ","authors_abbrev":"Weeks AT et al.","pubmed_publication_date":"04 Jan 2025","pubmed_entrez_date":"2025-01-06","publication_year":"2025","canto_session_key":"f580013c8f645e16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Amanda Bird","canto_first_approved_date":"2025-08-27 12:57:37","canto_approved_date":"2026-04-24 13:40:47","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-07-10 14:19:29","canto_added_date":"2025-01-08 00:25:05","annotation_curators":[{"name":"Amanda Bird","community_curator":true,"annotation_count":19,"orcid":"0000-0002-1846-7050","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":19,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18.06c","SPAC1783.07c","SPAC821.10c","SPBC29B5.01","SPCC31H12.08c","SPAC24B11.06c","SPAC25B8.19c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2025-08-27"},{"uniquename":"PMID:16314498","title":"Cooperative control of Crb2 by ATM family and Cdc2 kinases is essential for the DNA damage checkpoint in fission yeast.","citation":"Mol Cell Biol 2005 Dec;25(24):10721-30","abstract":"The cellular responses to double-stranded breaks (DSBs) typically involve the extensive accumulation of checkpoint proteins in chromatin surrounding the damaged DNA. One well-characterized example involves the checkpoint protein Crb2 in the fission yeast Schizosaccharomyces pombe. The accumulation of Crb2 at DSBs requires the C-terminal phosphorylation of histone H2A (known as gamma-H2A) by ATM family kinases in chromatin surrounding the break. It also requires the constitutive methylation of histone H4 on lysine-20 (K20). Interestingly, neither type of histone modification is essential for the Crb2-dependent checkpoint response. However, H4-K20 methylation is essential in a crb2-T215A strain that lacks a cyclin-dependent kinase phosphorylation site in Crb2. Here we explain this genetic interaction by describing a previously overlooked effect of the crb2-T215A mutation. We show that crb2-T215A cells are able to initiate but not sustain a checkpoint response. We also report that gamma-H2A is essential for the DNA damage checkpoint in crb2-T215A cells. Importantly, we show that inactivation of Cdc2 in gamma-H2A-defective cells impairs Crb2-dependent signaling to the checkpoint kinase Chk1. These findings demonstrate that full Crb2 activity requires phosphorylation of threonine-215 by Cdc2. This regulation of Crb2 is independent of the histone modifications that are required for the hyperaccumulation of Crb2 at DSBs.","authors":"Nakamura TM, Moser BA, Du LL, Russell P","authors_abbrev":"Nakamura TM et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-11-30","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC19G12.06c","SPBC342.05","SPCC622.08c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:40037704","title":"Mug20-Rec25-Rec27 binds DNA and enhances meiotic DNA break formation via phase-separated condensates.","citation":"Nucleic Acids Res 2025 Feb 27;53(5)","abstract":"During meiosis, programmed DNA double-strand breaks (DSBs) are formed at hotspots to initiate homologous recombination, which is vital for reassorting genetic material. In fission yeast, the linear element (LinE) proteins Mug20, Rec25, and Rec27 interdependently bind chromosomal hotspots with high specificity and are necessary for high-level DSB formation. However, their mechanistic role in regulating the meiotic DSB machinery remains unknown. Here, using purified Mug20-Rec25-Rec27 (MRR) complex and functional intracellular analyses, we reveal that the MRR-DNA nucleoprotein complex assembles phase-separated condensates that compact the DNA. Notably, MRR complex formation is a prerequisite for DNA binding and condensate assembly, with Rec27 playing a pivotal role in directly binding DNA. Consistent with this finding, failure to form MRR-DNA condensates results in defective intracellular meiotic DSB formation and recombination. Our results provide mechanistic insights into how LinEs enhance meiotic DSB formation and provide a paradigm for studies in other species.","doi":"10.1093/nar/gkaf123","authors":"Wang MF, Li MY, Yang YC, Chuang YC, Tsai CY, Binder MN, Ma L, Lin SW, Li HW, Smith GR, Chi P","authors_abbrev":"Wang MF et al.","pubmed_publication_date":"27 Feb 2025","pubmed_entrez_date":"2025-03-04","publication_year":"2025","canto_session_key":"beca1a9d41f7cf72","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-03-06 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7116208","title":"Sexual development in a homothallic fission yeast: synthesis of readiness proteins resolved by gel electrophoresis.","citation":"Can J Biochem 1982 Jun;60(6):693-704","abstract":"Sexual development of a homothallic strain of Schizosaccharomyces pombe was monitored by radiolabelling and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Of more than 60 bands detected by Coomassie brilliant blue and by autoradiography, about 30 bands synthesized during development were discrete enough for experimental analysis. About a dozen bands are preferentially vegetative, another dozen preferentially developmental. However, vegetative bands as a group are also synthesized during development. Their synthesis is relatively unaffected by low concentrations of cycloheximide or by chloramphenicol and is not temperature sensitive at 37 degrees C nor catabolite repressible. Only band 40 (ca. 40 000 daltons) seems to be exclusively vegetative. The synthesis of developmental bands 13, 18, 24, 30, and alpha, all of which first appear during late-log phase, is catabolite repressible. Developmental band 51 is also synthesized throughout the vegetative phase. The synthesis of bands 24, 30, 51, and alpha is temperature sensitive at 37 degrees C during the development, but that of band 18 is not. The synthesis of band 13 during development is not temperature sensitive, but its earlier synthesis during late-log phase is. The synthesis of all these six developmental bands is immediately inhibited by cycloheximide, but not by chloramphenicol. Their appearance as a group of radioactive bands is greatly diminished in cultures grown in cycloheximide, in chloramphenicol, or in ethidium bromide. Developmental bands 13, 18, 24, and 30 may be called readiness proteins. They first appear prior to the earliest morphological signs of sexual activity. Their developmental synthesis is inhibited by conditions that inhibit sexual development. Such inhibitory conditions include anaerobiosis, restrictive temperature, aging in stationary phase, the presence of inhibitors of cytoplasmic protein synthesis and of mitochondrial function, and catabolite repression. Readiness proteins may be regulating the switch from vegetative metabolism.","authors":"Calleja GB, Johnson BF, Walker T","authors_abbrev":"Calleja GB et al.","pubmed_publication_date":"Jun 1982","pubmed_entrez_date":"1982-06-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009885","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8891351","title":"Heat-shock treatment reduces in situ temperature in yeast at sub-lethal high temperature.","citation":"Cell Mol Biol (Noisy-le-grand) 1996 Sep;42(6):839-45","abstract":"Cells from the yeast Schizosaccharomyces pombe IFO-0342, once heat shocked and then treated with ultra-centrifugation showed a significant increase in tolerance compared to non heat-shocked control cells as estimated by colony forming unit (CFU). Fluorescence microscopical observation of these treated cells when stained with DAPI revealed that in non heat-shocked cells the chromatin regions were dislocated to one end due to the acceleration force of gravity. However, prior heat-shocked cells or 2.0 M glycerol suspended cells showed normal localization. From these results, it has been postulated that the interior part of the heat-shocked cells becomes viscous, and that in situ the temperature of the cell interior part might be reduced under semi-lethal high temperature.","authors":"Komatsu Y, Kodama O, Fujita K","authors_abbrev":"Komatsu Y et al.","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12359231","title":"Regulation and the role of Cu,Zn-containing superoxide dismutase in cell cycle progression of Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2002 Oct 04;297(4):854-62","abstract":"Regulation and the role of the sod1+ gene encoding CuZnSOD were investigated in fission yeast Schizosaccharomyces pombe. The amount of sod1+ mRNA decreased in the stationary phase, consistent with the decrease in enzyme activity. The transcript increased by treatment with oxidants such as H(2)O(2) and menadione (MD). Induction by H(2)O(2) was rapid and transient, being dependent on Wis1-Spc1-Atf1 pathway of signal transduction, whereas induction by MD was slow and sustained longer, being independent of Wis1 pathway. Wis1 and Spc1 also turned out to down-regulate sod1+ gene at the stationary phase. Tetrad analysis following sod1+ gene disruption revealed that the sod1Delta cells were not viable, even on rich media. Repression of the sod1+ gene expression by thiamine through nmt1 promoter resulted in the arrest of cell cycle progression following S phase, possibly between G(2) and cytokinesis. The current and previous observations that the viability of Schizosaccharomyces pombe cells, unlike Saccharomyces cerevisiae, critically depends on the action of oxidative defense enzymes in the cytosol, such as CuZnSOD and glutathione reductase, suggest that S. pombe can serve as a good model system to study the effect of oxidative stress on cell proliferation.","authors":"Lee J, Kwon ES, Kim DW, Cha J, Roe JH","authors_abbrev":"Lee J et al.","pubmed_publication_date":"04 Oct 2002","pubmed_entrez_date":"2002-10-03","publication_year":"2002","canto_session_key":"5388965f45db7c8b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:47:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-06 11:11:54","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.10c","SPAC24B11.06c","SPBC29B5.01","SPBC409.07c","SPAC1783.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-11-06"},{"uniquename":"PMID:10464333","title":"Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding.","citation":"J Biol Chem 1999 Sep 03;274(36):25899-905","abstract":"It has been proposed that in rat and murine tissues glucosidase II (GII) is formed by two subunits, GIIalpha and GIIbeta, respectively, responsible for the catalytic activity and the retention of the enzyme in the endoplasmic reticulum (ER). To test this proposal we disrupted genes (gls2alpha(+) and gls2beta(+)) encoding GIIalpha and GIIbeta homologs in Schizosaccharomyces pombe. Both mutant cells (gls2alpha and gls2beta) were completely devoid of GII activity in cell-free assays. Nevertheless, N-oligosaccharides formed in intact gls2alpha cells were identified as Glc(2)Man(9)GlcNAc(2) and Glc(2)Man(8)GlcNAc(2), whereas gls2beta cells formed, in addition, small amounts of Glc(1)Man(9)GlcNAc(2). It is suggested that this last compound was formed by GIIalpha transiently present in the ER. Monoglucosylated oligosaccharides facilitated glycoprotein folding in S. pombe as mutants, in which formation of monoglucosylated glycoproteins was completely (gls2alpha) or severely (gls2beta and UDP-Glc:glycoprotein:glucosyltransferase null) diminished, showed ER accumulation of misfolded glycoproteins when grown in the absence of exogenous stress as revealed by (a) induction of binding protein-encoding mRNA and (b) accumulation of glycoproteins bearing ER-specific oligosaccharides. Moreover, the same as in mammalian cell systems, formation of monoglucosylated oligosaccharides decreased the folding rate and increased the folding efficiency of glycoproteins as pulse-chase experiments revealed that carboxypeptidase Y arrived at a higher rate but in decreased amounts to the vacuoles of gls2alpha than to those of wild type cells.","authors":"D'Alessio C, Fernández F, Trombetta ES, Parodi AJ","authors_abbrev":"D'Alessio C et al.","pubmed_publication_date":"03 Sep 1999","pubmed_entrez_date":"1999-08-28","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24975289","title":"Exploring metabolic pathways in vivo by a combined approach of mixed stable isotope-labeled Raman microspectroscopy and multivariate curve resolution analysis.","citation":"Anal Chem 2014 Aug 05;86(15):7828-34","abstract":"Understanding cellular metabolism is a major challenge in current systems biology and has triggered extensive metabolomics research, which in most cases involves destructive analysis. However, the information obtainable only in a nondestructive manner will be required for accurately mapping the global structure of the organism's metabolic network at a given instant. Here we report that metabolic pathways can be explored in vivo by mixed stable isotope-labeled Raman microspectroscopy in conjunction with multivariate curve resolution analysis. As a model system, we studied ergosterol biosynthesis in single living fission yeast cells grown in mixtures of normal and (13)C-labeled glucose as the sole carbon source. The multivariate spectral data analysis of space-resolved Raman spectra revealed the intrinsic spectra and relative abundances of all isotopomers of ergosterol whose carbon atoms in the 5,7-diene moiety of the sterol skeleton are either partly or fully substituted with (13)C. Our approach is applicable to other metabolites and will earn a place in the toolbox of metabolomic analysis.","doi":"10.1021/ac501735c","authors":"Noothalapati H, Shigeto S","authors_abbrev":"Noothalapati H et al.","pubmed_publication_date":"05 Aug 2014","pubmed_entrez_date":"2014-07-01","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-07-02 00:15:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19491938","title":"A new way to initiate mRNA degradation.","citation":"Nat Struct Mol Biol 2009 Jun;16(6):613-4","abstract":"","doi":"10.1038/nsmb0609-613","authors":"Marzluff W","authors_abbrev":"Marzluff W","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-06-04","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26475597","title":"Succinate-CoA ligase deficiency due to mutations in SUCLA2 and SUCLG1: phenotype and genotype correlations in 71 patients.","citation":"J Inherit Metab Dis 2016 Mar;39(2):243-52","abstract":"The encephalomyopathic mtDNA depletion syndrome with methylmalonic aciduria is associated with deficiency of succinate-CoA ligase, caused by mutations in SUCLA2 or SUCLG1. We report here 25 new patients with succinate-CoA ligase deficiency, and review the clinical and molecular findings in these and 46 previously reported patients.\nOf the 71 patients, 50 had SUCLA2 mutations and 21 had SUCLG1 mutations. In the newly-reported 20 SUCLA2 patients we found 16 different mutations, of which nine were novel: two large gene deletions, a 1 bp duplication, two 1 bp deletions, a 3 bp insertion, a nonsense mutation and two missense mutations. In the newly-reported SUCLG1 patients, five missense mutations were identified, of which two were novel. The median onset of symptoms was two months for patients with SUCLA2 mutations and at birth for SUCLG1 patients. Median survival was 20 years for SUCLA2 and 20 months for SUCLG1. Notable clinical differences between the two groups were hepatopathy, found in 38% of SUCLG1 cases but not in SUCLA2 cases, and hypertrophic cardiomyopathy which was not reported in SUCLA2 patients, but documented in 14% of cases with SUCLG1 mutations. Long survival, to age 20 years or older, was reported in 12% of SUCLA2 and in 10% of SUCLG1 patients. The most frequent abnormality on neuroimaging was basal ganglia involvement, found in 69% of SUCLA2 and 80% of SUCLG1 patients. Analysis of respiratory chain enzyme activities in muscle generally showed a combined deficiency of complexes I and IV, but normal histological and biochemical findings in muscle did not preclude a diagnosis of succinate-CoA ligase deficiency. In five patients, the urinary excretion of methylmalonic acid was only marginally elevated, whereas elevated plasma methylmalonic acid was consistently found.\nTo our knowledge, this is the largest study of patients with SUCLA2 and SUCLG1 deficiency. The most important findings were a significantly longer survival in patients with SUCLA2 mutations compared to SUCLG1 mutations and a trend towards longer survival in patients with missense mutations compared to loss-of-function mutations. Hypertrophic cardiomyopathy and liver involvement was exclusively found in patients with SUCLG1 mutations, whereas epilepsy was much more frequent in patients with SUCLA2 mutations compared to patients with SUCLG1 mutations. The mutation analysis revealed a number of novel mutations, including a homozygous deletion of the entire SUCLA2 gene, and we found evidence of two founder mutations in the Scandinavian population, in addition to the known SUCLA2 founder mutation in the Faroe Islands.","doi":"10.1007/s10545-015-9894-9","authors":"Carrozzo R, Verrigni D, Rasmussen M, de Coo R, Amartino H, Bianchi M, Buhas D, Mesli S, Naess K, Born AP, Woldseth B, Prontera P, Batbayli M, Ravn K, Joensen F, Cordelli DM, Santorelli FM, Tulinius M, Darin N, Duno M, Jouvencel P, Burlina A, Stangoni G, Bertini E, Redonnet-Vernhet I, Wibrand F, Dionisi-Vici C, Uusimaa J, Vieira P, Osorio AN, McFarland R, Taylor RW, Holme E, Ostergaard E","authors_abbrev":"Carrozzo R et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2015-10-18","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1620.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7622565","title":"Schizosaccharomyces pombe cdc4+ gene encodes a novel EF-hand protein essential for cytokinesis.","citation":"J Cell Biol 1995 Aug;130(3):651-60","abstract":"Schizosaccharomyces pombe cells divide by medial fission. One class of cell division mutants (cdc), the late septation mutants, defines four genes: cdc3, cdc4, cdc8, and cdc12 (Nurse, P., P. Thuriaux, and K. Nasmyth. 1976. Mol. & Gen. Genet. 146:167-178). We have cloned and characterized the cdc4 gene and show that the predicted gene product. Cdc4p, is a 141-amino acid polypeptide that is similar in sequence to EF-hand proteins including myosin light chains, calmodulin, and troponin C. Two temperature-sensitive lethal alleles, cdc4-8 and cdc4-31, accumulate multiple nuclei and multiple improper F-actin rings and septa but fail to complete cytokinesis. Deletion of cdc4 also results in a lethal terminal phenotype characterized by multinucleate, elongated cells that fail to complete cytokinesis. Sequence comparisons suggest that Cdc4p may be a member of a new class of EF-hand proteins. Cdc4p localizes to a ringlike structure in the medial region of cells undergoing cytokinesis. Thus, Cdc4p appears to be an essential component of the F-actin contractile ring. We find that Cdc4 protein forms a complex with a 200-kD protein which can be cross-linked to UTP, a property common to myosin heavy chains. Together these results suggest that Cdc4p may be a novel myosin light chain.","authors":"McCollum D, Balasubramanian MK, Pelcher LE, Hemmingsen SM, Gould KL","authors_abbrev":"McCollum D et al.","pubmed_publication_date":"Aug 1995","pubmed_entrez_date":"1995-08-01","publication_year":"1995","canto_session_key":"3763e4e9332ec42e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-04 16:22:17","canto_approved_date":"2020-01-30 13:34:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-08-03 12:54:35","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-01-04"},{"uniquename":"PMID:31811152","title":"Chromosome-associated RNA-protein complexes promote pairing of homologous chromosomes during meiosis in Schizosaccharomyces pombe.","citation":"Nat Commun 2019 Dec 06;10(1):5598","abstract":"Pairing of homologous chromosomes in meiosis is essential for sexual reproduction. We have previously demonstrated that the fission yeast sme2 RNA, a meiosis-specific long noncoding RNA (lncRNA), accumulates at the sme2 chromosomal loci and mediates their robust pairing in meiosis. However, the mechanisms underlying lncRNA-mediated homologous pairing have remained elusive. In this study, we identify conserved RNA-binding proteins that are required for robust pairing of homologous chromosomes. These proteins accumulate mainly at the sme2 and two other chromosomal loci together with meiosis-specific lncRNAs transcribed from these loci. Remarkably, the chromosomal accumulation of these lncRNA-protein complexes is required for robust pairing. Moreover, the lncRNA-protein complexes exhibit phase separation properties, since 1,6-hexanediol treatment reversibly disassembled these complexes and disrupted the pairing of associated loci. We propose that lncRNA-protein complexes assembled at specific chromosomal loci mediate recognition and subsequent pairing of homologous chromosomes.","doi":"10.1038/s41467-019-13609-0","authors":"Ding DQ, Okamasa K, Katou Y, Oya E, Nakayama JI, Chikashige Y, Shirahige K, Haraguchi T, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"06 Dec 2019","pubmed_entrez_date":"2019-12-08","publication_year":"2019","canto_session_key":"6b5ad24ed09ee3d8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Da-Qiao Ding","canto_first_approved_date":"2020-05-05 19:01:24","canto_approved_date":"2023-03-17 23:15:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-09 03:39:37","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Da-Qiao Ding","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":40,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.11c","SPAC3H8.09c","SPAC222.09","SPAC27D7.03c","SPBC646.04","SPNCRNA.584","SPBC16E9.12c","SPNCRNA.130","SPAC29B12.06c","SPNCRNA.103","SPBC337.03","SPAC644.16","SPCC1919.05","SPAC4G9.04c","SPBC902.04"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2020-05-05"},{"uniquename":"PMID:8297389","title":"UV induction of excision repair enzymes detected in protein extracts from Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 1994 Jan 28;198(2):770-9","abstract":"Induction of genes and proteins after DNA damaging treatment is well documented in various biological systems. In order to monitor repair activity in Schizosacchromyces pombe, we adapted the biochemical assay that allowed specific quantification of excision repair in mammalian cells (Wood et al. 1988, Cell, 53, 97-106) to yeast-free extracts. Repair synthesis determined on UV-damaged plasmid DNA with S. pombe total protein extract relied on base excision repair and not nucleotide excision repair. Under conditions that allowed optimal repair activity, an enhanced repair synthesis was found with extract from yeast previously irradiated with UV light (254 nm). A 4-fold induction factor was obtained with 70 J/m2 irradiation dose after 40 min incubation post-irradiation. This base excision repair activity on UV photoproducts was transiently induced since it returned to the level of untreated yeast after about 2 hours post-irradiation.","authors":"Jaeg JP, Bouayadi K, Calsou P, Salles B","authors_abbrev":"Jaeg JP et al.","pubmed_publication_date":"28 Jan 1994","pubmed_entrez_date":"1994-01-28","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18923505","title":"Molecular biology: Bound to splice.","citation":"Nature 2008 Oct 16;455(7215):885-6","abstract":"","doi":"10.1038/455885a","authors":"Futcher B, Leatherwood JK","authors_abbrev":"Futcher B et al.","pubmed_publication_date":"16 Oct 2008","pubmed_entrez_date":"2008-10-17","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25724843","title":"Cancer-associated mutants of RNA helicase DDX3X are defective in RNA-stimulated ATP hydrolysis.","citation":"J Mol Biol 2015 May 08;427(9):1779-1796","abstract":"The DEAD-box RNA helicase DDX3X is frequently mutated in pediatric medulloblastoma. We dissect how these mutants affect DDX3X function with structural, biochemical, and genetic experiments. We identify an N-terminal extension (\"ATP-binding loop\", ABL) that is critical for the stimulation of ATP hydrolysis by RNA. We present crystal structures suggesting that the ABL interacts dynamically with ATP and confirming that the interaction occurs in solution by NMR chemical shift perturbation and isothermal titration calorimetry. DEAD-box helicases require interaction between two conserved RecA-like helicase domains, D1 and D2 for function. We use NMR chemical shift perturbation to show that DDX3X interacts specifically with double-stranded RNA through its D1 domain, with contact mediated by residues G302 and G325. Mutants of these residues, G302V and G325E, are associated with pediatric medulloblastoma. These mutants are defective in RNA-stimulated ATP hydrolysis. We show that DDX3X complements the growth defect in a ded1 temperature-sensitive strain of Schizosaccharomyces pombe, but the cancer-associated mutants G302V and G325E do not complement and exhibit protein expression defects. Taken together, our results suggest that impaired translation of important mRNA targets by mutant DDX3X represents a key step in the development of medulloblastoma.","doi":"10.1016/j.jmb.2015.02.015","authors":"Epling LB, Grace CR, Lowe BR, Partridge JF, Enemark EJ","authors_abbrev":"Epling LB et al.","pubmed_publication_date":"08 May 2015","pubmed_entrez_date":"2015-03-01","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1795.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU013992","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24493310","title":"Physiological aspects of conjugation in fission yeast.","citation":"Planta 1971 Mar;98(1):89-96","abstract":"Conjugation was studied in Schizosaccharomyces pombe using liquid media. Nitrogen, which was growth-limiting in a synthetic medium, had to be consumed completely before conjugation could start. Conjugation was preceded by sexual agglutination. Agglutinability was not constitutive in heterothallic strains. It only developed when cells of h (+) and h (-) mating type were grown in mixed culture for at least 2.5 hr before the start of conjugation.","doi":"10.1007/BF00387025","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"Mar 1971","pubmed_entrez_date":"2014-02-05","publication_year":"1971","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 06:09:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25807482","title":"Molecular biology: RNA interference hangs by a thread.","citation":"Nature 2015 Apr 09;520(7546):162-4","abstract":"","doi":"10.1038/nature14376","authors":"Zaratiegui M","authors_abbrev":"Zaratiegui M","pubmed_publication_date":"09 Apr 2015","pubmed_entrez_date":"2015-03-26","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-04-16 00:19:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22498309","title":"The evolution of metabolic enzymes in Plasmodium and trypanosomatids as compared to Saccharomyces and Schizosaccharomyces.","citation":"Mol Biochem Parasitol 2012 Jul;184(1):13-9","abstract":"Understanding how the biological connectivity of genes and gene products affects evolution is an important aspect of understanding evolution. Genes encoding enzymes are frequently used to carry out such analyses. Interestingly, studies have shown that connectivity in the metabolic networks in parasitic protists, including Plasmodium falciparum and Trypanosoma brucei, have been substantially altered as compared to free living eukaryotes, such as Saccharomyces cerevisiae. Herein, we have determined K(a) values, which are a measure of the non-synonymous substitution rate, and used them to examine the differences between the evolution of genes in T. brucei, P. falciparum, S. cerevisiae, and Schizosaccharomyces pombe. All four organisms share similar traits with respect to the evolution of genes encoding metabolic enzymes. First, genes encoding metabolic enzymes have lower K(a) values than genes encoding non-metabolic proteins. In addition, perturbations of the metabolic network appear to have limited affects on the genes encoding enzymes near the perturbation. In most cases, there is a negative relationship between connectivity in the metabolic network of the gene product and the K(a) value for the gene, i.e. examining how much constraint there is on gene evolution when it is connected to many other genes. In addition, we find that the K(a) values of orthologs encoding for metabolic enzymes in each organism are significantly correlated, indicating similar patterns of non-synonymous substitutions. In total, our results indicate that the evolution of genes encoding metabolic enzymes do not tend to be greatly affected by changes in the metabolic network.","doi":"10.1016/j.molbiopara.2012.03.007","authors":"Palenchar PM, Palenchar JB","authors_abbrev":"Palenchar PM et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-04-14","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12360293","title":"Astral microtubules monitor metaphase spindle alignment in fission yeast.","citation":"Nat Cell Biol 2002 Oct;4(10):816-20","abstract":"Segregating genetic material along the longest axis of the cell ensures that there is a sufficient distance between daughter chromosomes at the point of cytokinesis. Monitoring the orientation of the mitotic spindle can be subjected to cell cycle controls. In the fission yeast Schizosaccharomyces pombe, the existence of such a cell-cycle checkpoint has been proposed to delay the metaphase to anaphase transition when spindle poles are not properly oriented with respect to the actomyosin ring. Here we show, by using a fission yeast mutant compromised in its assembly of astral microtubules, that in the absence of astral microtubules short metaphase spindles are unable to orient themselves with respect to the long axis of the cell and are delayed in spindle elongation. This astral defect engages a spindle orientation checkpoint because deletion of the transcription factor Atf1, which is involved in maintaining this checkpoint, allows misaligned asterless metaphase spindles to elongate. We propose that astral microtubules are involved directly in monitoring orientation of the metaphase spindle and in controlling the timing of elongation in fission yeast.","authors":"Oliferenko S, Balasubramanian MK","authors_abbrev":"Oliferenko S et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-10-03","publication_year":"2002","canto_session_key":"6fae9a74671baaa1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-10-31 04:39:50","canto_approved_date":"2017-10-31 04:39:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-31 04:39:40","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC70.07c","SPAC890.02c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2017-10-31"},{"uniquename":"PMID:40124504","title":"Ltc1 localization by EMC regulates cell membrane fluidity to facilitate membrane protein biogenesis.","citation":"iScience 2025 Mar 21;28(3):112096","abstract":"The EMC complex, a highly conserved transmembrane chaperone in the endoplasmic reticulum (ER), has been associated in humans with sterol homeostasis and a myriad of different cellular activities, rendering the mechanism of EMC functionality enigmatic. Using fission yeast, we demonstrate that the EMC complex facilitates the biogenesis of the sterol transfer protein Lam6/Ltc1 at ER-plasma membrane and ER-mitochondria contact sites. Cells that lose EMC function sequester unfolded Lam6/Ltc1 and other proteins at the mitochondrial matrix, leading to surplus ergosterol, cold-sensitive growth, and mitochondrial dysfunctions. Remarkably, inhibition of ergosterol biosynthesis, but also fluidization of cell membranes to counteract their rigidizing effects, reduce the ER-unfolded protein response and rescue growth and mitochondrial defects in EMC-deficient cells. These results suggest that EMC-assisted biogenesis of Lam6/Ltc1 may provide, through ergosterol homeostasis, optimal membrane fluidity to facilitate biogenesis of other ER-membrane proteins.","doi":"10.1016/j.isci.2025.112096","authors":"Berraquero M, Tallada VA, Jimenez J","authors_abbrev":"Berraquero M et al.","pubmed_publication_date":"21 Mar 2025","pubmed_entrez_date":"2025-03-24","publication_year":"2025","canto_session_key":"2fff4fd823170b6c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juan Jimenez","canto_first_approved_date":"2025-04-19 17:27:00","canto_approved_date":"2025-04-27 12:36:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-11 10:38:05","canto_added_date":"2025-03-25 00:25:06","annotation_curators":[{"name":"Juan Jimenez","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC15C4.01c","SPBC1539.04","SPBC20F10.07","SPBC1711.03","SPAP4C9.02","SPBC19C2.11c","SPCC1020.11c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2025-04-19"},{"uniquename":"PMID:21892183","title":"Adaptive braking by Ase1 prevents overlapping microtubules from sliding completely apart.","citation":"Nat Cell Biol 2011 Sep 04;13(10):1259-64","abstract":"Short regions of overlap between ends of antiparallel microtubules are central elements within bipolar microtubule arrays. Although their formation requires motors, recent in vitro studies demonstrated that stable overlaps cannot be generated by molecular motors alone. Motors either slide microtubules along each other until complete separation or, in the presence of opposing motors, generate oscillatory movements. Here, we show that Ase1, a member of the conserved MAP65/PRC1 family of microtubule-bundling proteins, enables the formation of stable antiparallel overlaps through adaptive braking of Kinesin-14-driven microtubule-microtubule sliding. As overlapping microtubules start to slide apart, Ase1 molecules become compacted in the shrinking overlap and the sliding velocity gradually decreases in a dose-dependent manner. Compaction is driven by moving microtubule ends that act as barriers to Ase1 diffusion. Quantitative modelling showed that the molecular off-rate of Ase1 is sufficiently low to enable persistent overlap stabilization over tens of minutes. The finding of adaptive braking demonstrates that sliding can be slowed down locally to stabilize overlaps at the centre of bipolar arrays, whereas sliding proceeds elsewhere to enable network self-organization.","doi":"10.1038/ncb2323","authors":"Braun M, Lansky Z, Fink G, Ruhnow F, Diez S, Janson ME","authors_abbrev":"Braun M et al.","pubmed_publication_date":"04 Sep 2011","pubmed_entrez_date":"2011-09-06","publication_year":"2011","canto_session_key":"ddf4869fba46e0a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-23 13:19:09","canto_approved_date":"2024-06-26 10:21:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-08 16:16:55","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-23"},{"uniquename":"PMID:35773059","title":"Stress-induced cell depolarization through the MAP kinase-Cdc42 axis.","citation":"Trends Cell Biol 2023 Feb;33(2):124-137","abstract":"General stress responses, which sense environmental or endogenous signals, aim at promoting cell survival and fitness during adverse conditions. In eukaryotes, mitogen-activated protein (MAP) kinase-driven cascades trigger a shift in the cell's gene expression program as a cellular adaptation to stress. Here, we review another aspect of activated MAP kinase cascades reported in fission yeast: the transient inhibition of cell polarity in response to oxidative stress. The phosphorylation by a stress-activated MAP kinase of regulators of the GTPase cell division cycle 42 (Cdc42) causes a transient inhibition of polarized cell growth. The formation of growth sites depends on limiting and essential polarity components. We summarize here some processes in which inhibition of Cdc42 may be a general mechanism to regulate polarized growth also under physiological conditions.","doi":"10.1016/j.tcb.2022.06.004","authors":"Salat-Canela C, Pérez P, Ayté J, Hidalgo E","authors_abbrev":"Salat-Canela C et al.","pubmed_publication_date":"Feb 2023","pubmed_entrez_date":"2022-06-30","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-07-03 00:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26615217","title":"Bulk Segregant Analysis Reveals the Genetic Basis of a Natural Trait Variation in Fission Yeast.","citation":"Genome Biol Evol 2015 Nov 27;7(12):3496-510","abstract":"Although the fission yeast Schizosaccharomyces pombe is a well-established model organism, studies of natural trait variations in this species remain limited. To assess the feasibility of segregant-pool-based mapping of phenotype-causing genes in natural strains of fission yeast, we investigated the cause of a maltose utilization defect (Mal(-)) of the S. pombe strain CBS5557 (originally known as Schizosaccharomyces malidevorans). Analyzing the genome sequence of CBS5557 revealed 955 nonconservative missense substitutions, and 61 potential loss-of-function variants including 47 frameshift indels, 13 early stop codons, and 1 splice site mutation. As a side benefit, our analysis confirmed 146 sequence errors in the reference genome and improved annotations of 27 genes. We applied bulk segregant analysis to map the causal locus of the Mal(-) phenotype. Through sequencing the segregant pools derived from a cross between CBS5557 and the laboratory strain, we located the locus to within a 2.23-Mb chromosome I inversion found in most S. pombe isolates including CBS5557. To map genes within the inversion region that occupies 18% of the genome, we created a laboratory strain containing the same inversion. Analyzing segregants from a cross between CBS5557 and the inversion-containing laboratory strain narrowed down the locus to a 200-kb interval and led us to identify agl1, which suffers a 5-bp deletion in CBS5557, as the causal gene. Interestingly, loss of agl1 through a 34-kb deletion underlies the Mal(-) phenotype of another S. pombe strain CGMCC2.1628. This work adapts and validates the bulk segregant analysis method for uncovering trait-gene relationship in natural fission yeast strains.","doi":"10.1093/gbe/evv238","authors":"Hu W, Suo F, Du LL","authors_abbrev":"Hu W et al.","pubmed_publication_date":"27 Nov 2015","pubmed_entrez_date":"2015-11-29","publication_year":"2015","canto_session_key":"e3def4b016c7ad69","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-04-21 14:44:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-21 14:44:03","canto_added_date":"2015-11-30 01:19:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4F6.10","SPAC17G8.01c","SPAC1F8.07c","SPBC29A3.08","SPBC32F12.08c","SPBC13E7.01","SPAC1071.01c","SPBC16D10.10","SPBC23G7.06c","SPAC29E6.03c","SPAC29A4.03c","SPAC3A11.09","SPAC11D3.11c","SPAC3A11.06","SPCC1442.04c","SPAC22F3.11c","SPAC12B10.09","SPAC3A12.04c","SPAP27G11.10c","SPBC14C8.09c","SPAC823.04","SPBC29A3.06","SPBC1E8.03c","SPAC4D7.09","SPAC688.08","SPBC530.13","SPAC1486.05","SPAC29E6.04","SPBC16E9.16c","SPBC1A4.06c"],"gene_count":30,"ltp_gene_count":0,"approved_date":"2017-04-21"},{"uniquename":"PMID:39980688","title":"Fission yeast cells deficient in siderophore biosynthesis require Str2 for ferrichrome-dependent growth.","citation":"Front Microbiol 2025;16:1527727","abstract":"Ferrichrome (Fc) acquisition in  Schizosaccharomyces pombe  is mediated by the cell-surface siderophore-iron transporter Str1. Here, we report that Str2, a protein homologous to Str1, localizes to the vacuolar membrane. Like Str1, Str2 expression is transcriptionally regulated in response to changes in iron concentrations. Both the  str2 +   and  str1 +   genes are induced under low-iron conditions and are repressed by the iron-responsive GATA-type transcription factor Fep1 when iron is abundant. Under high-iron conditions, chromatin immunoprecipitation (ChIP) assays reveal that TAP-Fep1 occupies the  str2 +   and  str1 +   promoters. Isolated vacuoles from  str2Δ fep1Δ  cells expressing GFP-tagged Str2 exhibit iron accumulation in vacuoles upon exposure to exogenous holo-Fc.  sib1Δ sib2Δ  cells deficient in Fc biosynthesis and lacking the  str2 +   gene ( str2Δ ) are unable to grow in the presence of exogenous Fc as a sole source of iron. Further analysis identified that conserved amino acids Tyr 539  and Tyr 553  in the last predicted loop of Str2 are required for supporting Fc-dependent growth of a  sib1Δ sib2Δ  mutant strain. Collectively, these findings indicate that the vacuolar Str2 protein plays a role in the consumption of Fc as an iron source, while also revealing the involvement of the vacuole in iron release from exogenous Fc after its assimilation.","doi":"10.3389/fmicb.2025.1527727","authors":"Mbuya B, Plante S, Vahsen T, Brault A, Labbé S","authors_abbrev":"Mbuya B et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-02-21","publication_year":"2025","canto_session_key":"d5dd29de4ad6eb6a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-02-22 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12773391","title":"Condensin but not cohesin SMC heterodimer induces DNA reannealing through protein-protein assembly.","citation":"EMBO J 2003 Jun 02;22(11):2764-75","abstract":"Condensin and cohesin are chromosomal protein complexes required for chromosome condensation and sister chromatid cohesion, respectively. They commonly contain the SMC (structural maintenance of chromosomes) subunits consisting of a long coiled-coil with the terminal globular domains and the central hinge. Condensin and cohesin holo-complexes contain three and two non-SMC subunits, respectively. In this study, DNA interaction with cohesin and condensin complexes purified from fission yeast was investigated. The DNA reannealing activity is strong for condensin SMC heterodimer but weak for holo-condensin, whereas no annealing activity is found for cohesin heterodimer SMC and Rad21-bound heterotrimer complexes. One set of globular domains of the same condensin SMC is essential for the DNA reannealing activity. In addition, the coiled-coil and hinge region of another SMC are needed. Atomic force microscopy discloses the molecular events of DNA reannealing. SMC assembly that occurs on reannealing DNA seems to be a necessary intermediary step. SMC is eliminated from the completed double-stranded DNA. The ability of heterodimeric SMC to reanneal DNA may be regulated in vivo possibly through the non-SMC heterotrimeric complex.","authors":"Sakai A, Hizume K, Sutani T, Takeyasu K, Yanagida M","authors_abbrev":"Sakai A et al.","pubmed_publication_date":"02 Jun 2003","pubmed_entrez_date":"2003-05-30","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.04","SPAC10F6.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:SPC11281","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26882497","title":"Mps1Mph1 Kinase Phosphorylates Mad3 to Inhibit Cdc20Slp1-APC/C and Maintain Spindle Checkpoint Arrests.","citation":"PLoS Genet 2016 Feb;12(2):e1005834","abstract":"The spindle checkpoint is a mitotic surveillance system which ensures equal segregation of sister chromatids. It delays anaphase onset by inhibiting the action of the E3 ubiquitin ligase known as the anaphase promoting complex or cyclosome (APC/C). Mad3/BubR1 is a key component of the mitotic checkpoint complex (MCC) which binds and inhibits the APC/C early in mitosis. Mps1(Mph1) kinase is critical for checkpoint signalling and MCC-APC/C inhibition, yet few substrates have been identified. Here we identify Mad3 as a substrate of fission yeast Mps1(Mph1) kinase. We map and mutate phosphorylation sites in Mad3, producing mutants that are targeted to kinetochores and assembled into MCC, yet display reduced APC/C binding and are unable to maintain checkpoint arrests. We show biochemically that Mad3 phospho-mimics are potent APC/C inhibitors in vitro, demonstrating that Mad3p modification can directly influence Cdc20(Slp1)-APC/C activity. This genetic dissection of APC/C inhibition demonstrates that Mps1(Mph1) kinase-dependent modifications of Mad3 and Mad2 act in a concerted manner to maintain spindle checkpoint arrests.","doi":"10.1371/journal.pgen.1005834","authors":"Zich J, May K, Paraskevopoulos K, Sen O, Syred HM, van der Sar S, Patel H, Moresco JJ, Sarkeshik A, Yates JR, Rappsilber J, Hardwick KG","authors_abbrev":"Zich J et al.","pubmed_publication_date":"Feb 2016","pubmed_entrez_date":"2016-02-17","publication_year":"2016","canto_session_key":"25a5d9e72c9fc7ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-29 17:49:48","canto_approved_date":"2025-09-03 15:30:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-04 14:47:04","canto_added_date":"2016-02-19 01:15:23","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":62,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.20","SPBC20F10.06","SPCC1795.01c","SPBC14C8.01c","SPBC119.02","SPBC1604.21c","SPCC1259.15c","SPBC106.01","SPAC19G12.01c","SPAC821.08c","SPAC27F1.04c"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2018-11-29"},{"uniquename":"PMID:17049819","title":"Characterizing pathogenic processes in Batten disease: use of small eukaryotic model systems.","citation":"Biochim Biophys Acta 2006 Oct;1762(10):906-19","abstract":"The neuronal ceroid lipofuscinoses (NCLs) are neurodegenerative disorders. Nevertheless, small model organisms, including those lacking a nervous system, have proven invaluable in the study of mechanisms that underlie the disease and in studying the functions of the conserved proteins associated to each disease. From the single-celled yeast, Saccharomyces cerevisiae and Schizosaccharomyces pombe, to the worm, Caenorhabditis elegans and the fruitfly, Drosophila melanogaster, biochemical and, in particular, genetic studies on these organisms have provided insight into the NCLs.","authors":"Phillips SN, Muzaffar N, Codlin S, Korey CA, Taschner PE, de Voer G, Mole SE, Pearce DA","authors_abbrev":"Phillips SN et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-10-20","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12437782","title":"Distinct functions of S. pombe Rec12 (Spo11) protein and Rec12-dependent crossover recombination (chiasmata) in meiosis I; and a requirement for Rec12 in meiosis II.","citation":"Cell Chromosome 2002 Sep 19;1(1):1","abstract":"BACKGROUND: In most organisms proper reductional chromosome segregation during meiosis I is strongly correlated with the presence of crossover recombination structures (chiasmata); recombination deficient mutants lack crossovers and suffer meiosis I nondisjunction. We report that these functions are separable in the fission yeast Schizosaccharomyces pombe. RESULTS: Intron mapping and expression studies confirmed that Rec12 is a member of the Spo11/Top6A topoisomerase family required for the formation of meiotic dsDNA breaks and recombination. rec12-117, rec12-D15 (null), and rec12-Y98F (active site) mutants lacked most crossover recombination and chromosomes segregated abnormally to generate aneuploid meiotic products. Since S. pombe contains only three chromosome pairs, many of those aneuploid products were viable. The types of aberrant chromosome segregation were inferred from the inheritance patterns of centromere linked markers in diploid meiotic products. The rec12-117 and rec12-D15 mutants manifest segregation errors during both meiosis I and meiosis II. Remarkably, the rec12-Y98F (active site) mutant exhibited essentially normal meiosis I segregation patterns, but still exhibited meiosis II segregation errors. CONCLUSIONS: Rec12 is a 345 amino acid protein required for most crossover recombination and for chiasmatic segregation of chromosomes during meiosis I. Rec12 also participates in a backup distributive (achiasmatic) system of chromosome segregation during meiosis I. In addition, catalytically-active Rec12 mediates some signal that is required for faithful equational segregation of chromosomes during meiosis II.","authors":"Sharif WD, Glick GG, Davidson MK, Wahls WP","authors_abbrev":"Sharif WD et al.","pubmed_publication_date":"19 Sep 2002","pubmed_entrez_date":"2002-11-20","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.11"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:42033227","title":"How interdiction of inositol pyrophosphate catabolism perturbs the fission yeast response to phosphate starvation.","citation":"Nucleic Acids Res 2026 Apr 23;54(8)","abstract":"In fission yeast, inositol-1-pyrophosphates drive the synthesis of vacuolar inorganic polyphosphate (polyP), which serves as a phosphate reservoir during nutrient scarcity. Acute phosphate starvation of wild-type fission yeast cells triggers rapid depletion in tandem of inositol-1-pyrophosphates and polyP, and a gradual transition to G0 quiescence. Here, we report that HASX yeast cells, which lack the three pyrophosphatase enzymes that catabolize inositol pyrophosphates, mount an aberrant response to phosphate starvation associated with sustained elevation of inositol-1-pyrophosphates. This entails immediate cessation of growth; precocious onset of the phosphate starvation transcriptional program; persistently high vacuolar polyP levels; and rapid loss of polysomes, accumulation of 80S monosomes, and inefficient translation of starvation-induced pho1 mRNA. Two key findings are that: (i) the deviant phosphate starvation phenotype in HASX cells is effaced by deletion of vacuolar polyP polymerase Vtc4; and (ii) overdrive of Vtc4-catalyzed polyP synthesis by excess inositol-1-pyrophosphates rapidly exhausts the GTP pool in phosphate-starved HASX cells. GTP depletion, together with precocious repression of genes encoding translation factor GTPases, is the likely cause of the polysome decay. Our results provide new insights into how inositol pyrophosphate signaling and polyP dynamics influence the translation machinery, phosphate homeostasis, and the transcriptional response to nutrient stress.","doi":"10.1093/nar/gkag352","authors":"Babor J, Sanchez AM, Prucker I, Jessen HJ, Schwer B, Shuman S","authors_abbrev":"Babor J et al.","pubmed_publication_date":"23 Apr 2026","pubmed_entrez_date":"2026-04-25","publication_year":"2026","canto_session_key":"88e6b8ac6d4d8089","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-26 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011780","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14503856","title":"The thioltransferase (glutaredoxin) 1 gene of fission yeast is regulated by Atf1 and Pap1.","citation":"Mol Cells 2003 Aug 31;16(1):123-7","abstract":"We previously isolated a gene encoding thioltransferase (TTase1) from the fission yeast Schizosaccharomyces pombe. Using a TTase-lacZ fusion plasmid, carrying a 666 bp region upstream of the translation initiation point, we found that expression of TTase1 was enhanced by metal ions, diamide and NO-generating S-nitroso-N-acetylpenicillamine (SNAP). In the present work, we examined the regulation of TTase1 expression using a series of deletion mutants and identified a negatively acting sequence between bp -469 and -339. Atf1 is required for basal expression of TTase1, and Pap1 is required for its inducible expression by mercuric chloride, diamide and SNAP. The -469 approximately -339 bp region is also responsible for mediating the inducible expression.","authors":"Lim CJ, Cho YW, Hong SM, Lim HW, Park EH","authors_abbrev":"Lim CJ et al.","pubmed_publication_date":"31 Aug 2003","pubmed_entrez_date":"2003-09-25","publication_year":"2003","canto_session_key":"3bc4a5d3166ea425","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-04 14:43:27","canto_approved_date":"2022-02-01 10:35:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-04 14:43:17","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPBC409.07c","SPAC1783.07c","SPAC4F10.20"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-12-04"},{"uniquename":"PMID:29279306","title":"Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES.","citation":"J Cell Biol 2018 Mar 05;217(3):959-974","abstract":"The endoplasmic reticulum (ER)-mitochondrial encounter structure (ERMES) physically links the membranes of the ER and mitochondria in yeast. Although the ER and mitochondria cooperate to synthesize glycerophospholipids, whether ERMES directly facilitates the lipid exchange between the two organelles remains controversial. Here, we compared the x-ray structures of an ERMES subunit Mdm12 from  Kluyveromyces lactis  with that of Mdm12 from  Saccharomyces cerevisiae  and found that both Mdm12 proteins possess a hydrophobic pocket for phospholipid binding. However in vitro lipid transfer assays showed that Mdm12 alone or an Mmm1 (another ERMES subunit) fusion protein exhibited only a weak lipid transfer activity between liposomes. In contrast, Mdm12 in a complex with Mmm1 mediated efficient lipid transfer between liposomes. Mutations in Mmm1 or Mdm12 impaired the lipid transfer activities of the Mdm12-Mmm1 complex and furthermore caused defective phosphatidylserine transport from the ER to mitochondrial membranes via ERMES in vitro. Therefore, the Mmm1-Mdm12 complex functions as a minimal unit that mediates lipid transfer between membranes.","doi":"10.1083/jcb.201704119","authors":"Kawano S, Tamura Y, Kojima R, Bala S, Asai E, Michel AH, Kornmann B, Riezman I, Riezman H, Sakae Y, Okamoto Y, Endo T","authors_abbrev":"Kawano S et al.","pubmed_publication_date":"05 Mar 2018","pubmed_entrez_date":"2017-12-28","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.11c","SPBC28F2.06c","SPAP8A3.10","SPBC27B12.01c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:40894867","title":"Control of stress-activated Cdc42 dynamics by the MAP kinase Sty1-NDR kinase Orb6 regulatory axis.","citation":"iScience 2025 Sep 19;28(9):113298","abstract":"Cdc42 is a Rho-family GTPase that controls cell polarization from yeast to human cells. In fission yeast, under normal growth conditions, Cdc42-GTP oscillates between cell tips to promote polarized growth. However, when exposed to environmental stressors, Cdc42 adopts an \"exploratory\" pattern of Cdc42 activation along the cell membrane. This pattern also occurs when the NDR kinase Orb6 is downregulated. Here, we describe the molecular mechanism behind the emergence of exploratory Cdc42 dynamics and identify a substrate of Orb6 kinase, the Cdc42 GAP Rga3. Additionally, we show that MAP kinase Sty1, known for linking stress signals to the Cdc42 polarity module, negatively regulates Orb6 kinase. During nutritional stress, activation of Sty1 and inactivation of Orb6 are associated with chronological lifespan extension. Our findings reveal a mechanism controlling cell morphology during stress, with important implications for cell survival.","doi":"10.1016/j.isci.2025.113298","authors":"Doyle LP, Chen JS, Gould KL, McCollum D, Verde F","authors_abbrev":"Doyle LP et al.","pubmed_publication_date":"19 Sep 2025","pubmed_entrez_date":"2025-09-02","publication_year":"2025","canto_session_key":"21ac85d493f7e614","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-02 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18032583","title":"Cleavage of stalled forks by fission yeast Mus81/Eme1 in absence of DNA replication checkpoint.","citation":"Mol Biol Cell 2008 Feb;19(2):445-56","abstract":"During replication arrest, the DNA replication checkpoint plays a crucial role in the stabilization of the replisome at stalled forks, thus preventing the collapse of active forks and the formation of aberrant DNA structures. How this checkpoint acts to preserve the integrity of replication structures at stalled fork is poorly understood. In Schizosaccharomyces pombe, the DNA replication checkpoint kinase Cds1 negatively regulates the structure-specific endonuclease Mus81/Eme1 to preserve genomic integrity when replication is perturbed. Here, we report that, in response to hydroxyurea (HU) treatment, the replication checkpoint prevents S-phase-specific DNA breakage resulting from Mus81 nuclease activity. However, loss of Mus81 regulation by Cds1 is not sufficient to produce HU-induced DNA breaks. Our results suggest that unscheduled cleavage of stalled forks by Mus81 is permitted when the replisome is not stabilized by the replication checkpoint. We also show that HU-induced DNA breaks are partially dependent on the Rqh1 helicase, the fission yeast homologue of BLM, but are independent of its helicase activity. This suggests that efficient cleavage of stalled forks by Mus81 requires Rqh1. Finally, we identified an interplay between Mus81 activity at stalled forks and the Chk1-dependent DNA damage checkpoint during S-phase when replication forks have collapsed.","authors":"Froget B, Blaisonneau J, Lambert S, Baldacci G","authors_abbrev":"Froget B et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2007-11-23","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3311876","title":"A new type of fusion analysis applicable to many organisms: protein fusions to the URA3 gene of yeast.","citation":"Genetics 1987 Sep;117(1):5-12","abstract":"We have made constructs that join the promoter sequences and a portion of the coding region of the Saccharomyces cerevisiae HIS4 and GAL1 genes and the E. coli lacZ gene to the sixth codon of the S. cerevisiae URA3 gene (encodes orotidine-5'-phosphate (OMP) decarboxylase) to form three in frame protein fusions. In each case the fusion protein has OMP decarboxylase activity as assayed by complementation tests and this activity is properly regulated. A convenient cassette consisting of the URA3 segment plus some immediately proximal amino acids of HIS4C is available for making URA3 fusions to other proteins of interest. URA3 fusions offer several advantages over other systems for gene fusion analysis: the URA3 specified protein is small and cytosolic; genetic selections exist to identify mutants with either increased or decreased URA3 function in both yeast (S. cerevisiae and Schizosaccharomyces pombe) and bacteria (Escherichia coli and Salmonella typhimurium); and a sensitive OMP decarboxylase enzyme assay is available. Also, OMP decarboxylase activity is present in mammals, Drosophila and plants, so URA3 fusions may eventually be applicable in these other organisms as well.","authors":"Alani E, Kleckner N","authors_abbrev":"Alani E et al.","pubmed_publication_date":"Sep 1987","pubmed_entrez_date":"1987-09-01","publication_year":"1987","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20691155","title":"Phosphorylation of the protein kinase A catalytic subunit is induced by cyclic AMP deficiency and physiological stresses in the fission yeast, Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2010 Sep 03;399(4):665-9","abstract":"In the fission yeast, Schizosaccharomyces pombe, cyclic AMP (cAMP)-dependent protein kinase (PKA) is not essential for viability under normal culturing conditions, making this organism attractive for investigating mechanisms of PKA regulation. Here we show that S. pombe cells carrying a deletion in the adenylate cyclase gene, cyr1, express markedly higher levels of the PKA catalytic subunit, Pka1, than wild type cells. Significantly, in cyr1Delta cells, but not wild type cells, a substantial proportion of Pka1 protein is hyperphosphorylated. Pka1 hyperphosphorylation is strongly induced in cyr1Delta cells, and to varying degrees in wild type cells, by both glucose starvation and stationary phase stresses, which are associated with reduced cAMP-dependent PKA activity, and by KCl stress, the cellular adaptation to which is dependent on PKA activity. Interestingly, hyperphosphorylation of Pka1 was not detected in either cyr1(+) or cyr1Delta S. pombe strains carrying a deletion in the PKA regulatory subunit gene, cgs1, under any of the tested conditions. Our results demonstrate the existence of a cAMP-independent mechanism of PKA catalytic subunit phosphorylation, which we propose could serve as a mechanism for inducing or maintaining specific PKA functions under conditions in which its cAMP-dependent activity is downregulated.","doi":"10.1016/j.bbrc.2010.07.139","authors":"McInnis B, Mitchell J, Marcus S","authors_abbrev":"McInnis B et al.","pubmed_publication_date":"03 Sep 2010","pubmed_entrez_date":"2010-08-10","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8948095","title":"Mutational analysis of the gene for Schizosaccharomyces pombe RNase MRP RNA, mrp1, using plasmid shuffle by counterselection on canavanine.","citation":"Yeast 1996 Nov;12(14):1393-405","abstract":"Reverse genetics in fission yeast is hindered by the lack of a versatile established plasmid shuffle system. In order to screen efficiently and accurately through plasmid-borne mutations in the essential gene for the RNA component of RNase MRP, mrp1, we have developed a system for plasmid shuffling in fission yeast using counterselection on canavanine. The system takes advantage of the ability of the Saccharomyces cerevisiae CAN1 gene to complement a Schizosaccharomyces pombe can1-1 mutation. Two general use plasmids were constructed that allow directional cloning and initial selection for histidine before counterselection by canavanine. The strain constructed for plasmid shuffling carries auxotrophic markers for ade6, leul, ura4 and his3 along with the can1-1 mutation. Using this system we examined several partial deletions and point mutations in conserved nucleotides of Schizosaccharomyces pombe RNase MRP RNA for their ability to complement a chromosomal deletion of the mrp1 gene. The degree of background canavanine resistance as well as plasmid-plasmid recombination encountered in these experiments was sufficiently low to suggest that the system we have set up for counterselection by canavanine in fission yeast using multicopy plasmids will be widely useful.","authors":"Paluh JL, Clayton DA","authors_abbrev":"Paluh JL et al.","pubmed_publication_date":"Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_session_key":"8c45a7b8efd78a20","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-11 11:53:55","canto_approved_date":"2022-02-02 10:42:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-11 11:53:47","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.82"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-11"},{"uniquename":"GO_REF:0000070","title":"Representation of transmembrane transporter activity as molecular function in the Gene Ontology","abstract":"We have created a standard template for classes describing the transmembrane transporter activity a chemical entity (ChEBI) as molecular function. This includes variants for secondary active transmembrane transporter activity (GO:0015291), uptake transmembrane transporter activity (GO:0015563), and ATPase activity, coupled to transmembrane movement of substances (GO:0042626). The underlying equivalence axiom template is \"G and 'transports or maintains localization of' some X\",  where the genus G is either GO:0022857 (transmembrane transporter activity), GO:0015291, GO:0015563, or GO:0042626 depending on the variant. The variable X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16921379","title":"The Swi5-Sfr1 complex stimulates Rhp51/Rad51- and Dmc1-mediated DNA strand exchange in vitro.","citation":"Nat Struct Mol Biol 2006 Sep;13(9):823-30","abstract":"Nucleoprotein filaments made up of Rad51 or Dmc1 recombinases, the core structures of recombination, engage in ATP-dependent DNA-strand exchange. The ability of recombinases to form filaments is enhanced by recombination factors termed 'mediators'. Here, we show that the Schizosaccharomyces pombe Swi5-Sfr1 complex, a conserved eukaryotic protein complex, at substoichiometric concentrations stimulates strand exchange mediated by Rhp51 (the S. pombe Rad51 homolog) and Dmc1 on long DNA substrates. Reactions mediated by both recombinases are completely dependent on Swi5-Sfr1, replication protein A (RPA) and ATP, although RPA inhibits the reaction when it is incubated with single-stranded DNA (ssDNA) before the recombinase. The Swi5-Sfr1 complex overcomes, at least partly, the inhibitory effect of RPA, representing a novel class of mediator. Notably, the Swi5-Sfr1 complex preferentially stimulates the ssDNA-dependent ATPase activity of Rhp51, and it increases the amounts of Dmc1 bound to ssDNA.","authors":"Haruta N, Kurokawa Y, Murayama Y, Akamatsu Y, Unzai S, Tsutsui Y, Iwasaki H","authors_abbrev":"Haruta N et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-08-22","publication_year":"2006","canto_session_key":"4eb88108157577ae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-08-02 09:53:44","canto_approved_date":"2025-09-04 11:45:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-02 09:53:35","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.07","SPAC644.14c","SPAC8E11.03c","SPBC409.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-08-02"},{"uniquename":"PMID:34533984","title":"Cell patterning by secretion-induced plasma membrane flows.","citation":"Sci Adv 2021 Sep 17;7(38):eabg6718","abstract":"Cells self-organize using reaction-diffusion and fluid-flow principles. Whether bulk membrane flows contribute to cell patterning has not been established. Here, using mathematical modeling, optogenetics, and synthetic probes, we show that polarized exocytosis causes lateral membrane flows away from regions of membrane insertion. Plasma membrane–associated proteins with sufficiently low diffusion and/or detachment rates couple to the flows and deplete from areas of exocytosis. In rod-shaped fission yeast cells, zones of Cdc42 GTPase activity driving polarized exocytosis are limited by GTPase activating proteins (GAPs). We show that membrane flows pattern the GAP Rga4 distribution and that coupling of a synthetic GAP to membrane flows is sufficient to establish the rod shape. Thus, membrane flows induced by Cdc42-dependent exocytosis form a negative feedback restricting the zone of Cdc42 activity.","doi":"10.1126/sciadv.abg6718","authors":"Gerganova V, Lamas I, Rutkowski DM, Vještica A, Castro DG, Vincenzetti V, Vavylonis D, Martin SG","authors_abbrev":"Gerganova V et al.","pubmed_publication_date":"17 Sep 2021","pubmed_entrez_date":"2021-09-17","publication_year":"2021","canto_session_key":"993341fa136b2243","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-03-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9499374","title":"[Molecular cloning of rpb5+, rpb7+ and rpb11+ genes of the fission yeast Schizosaccharomyces pombe: completing primary structure of all indispensable subunits of its RNA polymerase II].","citation":"Bioorg Khim 1997 Dec;23(12):988-91","abstract":"","authors":"Shpakovskiĭ GV, Lebedenko EN","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1998-03-14","publication_year":"1997","canto_session_key":"36cb691db411000c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-29 21:28:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 20:43:35","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3A12.07","SPACUNK4.06c","SPAC23C4.15"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2014-04-29"},{"uniquename":"PMID:37952152","title":"Uncoupling the distinct functions of HP1 proteins during heterochromatin establishment and maintenance.","citation":"Cell Rep 2023 Nov 28;42(11):113428","abstract":"H3K9 methylation (H3K9me) marks transcriptionally silent genomic regions called heterochromatin. HP1 proteins are required to establish and maintain heterochromatin. HP1 proteins bind to H3K9me, recruit factors that promote heterochromatin formation, and oligomerize to form phase-separated condensates. We do not understand how these different HP1 properties are involved in establishing and maintaining transcriptional silencing. Here, we demonstrate that the S. pombe HP1 homolog, Swi6, can be completely bypassed to establish silencing at ectopic and endogenous loci when an H3K4 methyltransferase, Set1, and an H3K14 acetyltransferase, Mst2, are deleted. Deleting Set1 and Mst2 enhances Clr4 enzymatic activity, leading to higher H3K9me levels and spreading. In contrast, Swi6 and its capacity to oligomerize were indispensable during epigenetic maintenance. Our results demonstrate the role of HP1 proteins in regulating histone modification crosstalk during establishment and identify a genetically separable function in maintaining epigenetic memory.","doi":"10.1016/j.celrep.2023.113428","authors":"Seman M, Levashkevich A, Larkin A, Huang F, Ragunathan K","authors_abbrev":"Seman M et al.","pubmed_publication_date":"28 Nov 2023","pubmed_entrez_date":"2023-11-12","publication_year":"2023","canto_session_key":"a613f87cbba30ab3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-11-13 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16087707","title":"Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast.","citation":"J Cell Biol 2005 Aug 15;170(4):637-48","abstract":"Yeast actin patches are dynamic structures that form at the sites of cell growth and are thought to play a role in endocytosis. We used biochemical analysis and live cell imaging to investigate actin patch assembly in fission yeast Schizosaccharomyces pombe. Patch assembly proceeds via two parallel pathways: one dependent on WASp Wsp1p and verprolin Vrp1p converges with another dependent on class 1 myosin Myo1p to activate the actin-related protein 2/3 (Arp2/3) complex. Wsp1p activates Arp2/3 complex via a conventional mechanism, resulting in branched filaments. Myo1p is a weaker Arp2/3 complex activator that makes unstable branches and is enhanced by verprolin. During patch assembly in vivo, Wsp1p and Vrp1p arrive first independent of Myo1p. Arp2/3 complex associates with nascent activator patches over 6-9 s while remaining stationary. After reaching a maximum concentration, Arp2/3 complex patches move centripetally as activator proteins dissociate. Genetic dependencies of patch formation suggest that patch formation involves cross talk between Myo1p and Wsp1p/Vrp1p pathways.","authors":"Sirotkin V, Beltzner CC, Marchand JB, Pollard TD","authors_abbrev":"Sirotkin V et al.","pubmed_publication_date":"15 Aug 2005","pubmed_entrez_date":"2005-08-10","publication_year":"2005","canto_session_key":"36de390cd2e1923e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-01-11 16:34:29","canto_approved_date":"2026-04-06 15:02:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-11 16:34:21","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC13E7.09","SPAC4F10.15c","SPBC1778.08c","SPBC14C8.06","SPBC146.13c","SPAC17G8.04c","SPAC11H11.06","SPAC6F6.10c","SPAC6G9.07c","SPAC630.03"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2019-01-11"},{"uniquename":"PMID:1310980","title":"The yeast plasma membrane H(+)-ATPase. An essential change of conformation triggered by H+.","citation":"J Biol Chem 1992 Feb 25;267(6):3735-40","abstract":"The plasma membrane of Schizosaccharomyces pombe contains an H(+)-ATPase similar to the cation transport ATPases of other eukaryotic organisms. The fluorescence excitation and emission spectra of the purified H(+)-ATPase are characteristic of tryptophan residues. pH reduction from 7.5 to 5.7 produces a 4% decrease in fluorescence intensity, while a further reduction to pH 5.0 leads to an increase of fluorescence. A close correlation is observed between the pH dependence of the intrinsic fluorescence and the pH dependence of (i) ATPase activity, (ii) the fluorescence of Tb-formycin triphosphate bound to the active site, and (iii) inhibition by vanadate of ATPase activity. It is proposed that the effect of pH on intrinsic fluorescence reveals the existence of an H+ induced conformational change of the H(+)-ATPase similar to the E1----E2 transition of the other plasma membrane cation transport ATPases.","authors":"Blanpain JP, Ronjat M, Supply P, Dufour JP, Goffeau A, Dupont Y","authors_abbrev":"Blanpain JP et al.","pubmed_publication_date":"25 Feb 1992","pubmed_entrez_date":"1992-02-25","publication_year":"1992","canto_session_key":"7b933f0d2c28e1dd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-02-05 16:25:20","canto_approved_date":"2020-01-17 19:16:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-01 09:58:49","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-05"},{"uniquename":"PMID:9230309","title":"Mis6, a fission yeast inner centromere protein, acts during G1/S and forms specialized chromatin required for equal segregation.","citation":"Cell 1997 Jul 11;90(1):131-43","abstract":"Disorder in sister chromatid separation can lead to genome instability and cancer. A temperature-sensitive S. pombe mis6-302 frequently loses a minichromosome at 26 degrees C and abolishes equal segregation of regular chromosomes at 36 degrees C. The mis6+ gene is essential for viability, and its deletion results in missegregation identical to mis6-302. Mis6 acts before or at the onset of S phase, and mitotic missegregation defects are produced only after the passage of G1/S at 36 degrees C. Mis6 locates at the centromeres throughout the cell cycle. In the mutant, positioning of the centromeres becomes abnormal, and specialized chromatin in the inner centromeres, which give the smear micrococcal nuclease pattern in wild type, is disrupted. The ability to establish correct biorientation of sister centromeres in metaphase cells requires the Mis6-containing chromatin and originates during the passage of G1/S.","authors":"Saitoh S, Takahashi K, Yanagida M","authors_abbrev":"Saitoh S et al.","pubmed_publication_date":"11 Jul 1997","pubmed_entrez_date":"1997-07-11","publication_year":"1997","canto_session_key":"12185f18d361fa03","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-03-07 11:32:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-18 13:42:13","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.20c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-18"},{"uniquename":"PMID:25075304","title":"Yeast Augmented Network Analysis (YANA): a new systems approach to identify therapeutic targets for human genetic diseases.","citation":"F1000Res 2014;3:121","abstract":"Genetic interaction networks that underlie most human diseases are highly complex and poorly defined. Better-defined networks will allow identification of a greater number of therapeutic targets. Here we introduce our Yeast Augmented Network Analysis (YANA) approach and test it with the X-linked spinal muscular atrophy (SMA) disease gene UBA1. First, we express UBA1 and a mutant variant in fission yeast and use high-throughput methods to identify fission yeast genetic modifiers of UBA1. Second, we analyze available protein-protein interaction network databases in both fission yeast and human to construct UBA1 genetic networks. Third, from these networks we identified potential therapeutic targets for SMA. Finally, we validate one of these targets in a vertebrate (zebrafish) SMA model. This study demonstrates the power of combining synthetic and chemical genetics with a simple model system to identify human disease gene networks that can be exploited for treating human diseases.","doi":"10.12688/f1000research.4188.1","authors":"Wiley DJ, Juan I, Le H, Cai X, Baumbach L, Beattie C, D'Urso G","authors_abbrev":"Wiley DJ et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-07-31","publication_year":"2014","canto_session_key":"a581dee82a78cd90","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-08-01 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:X65868","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8371123","title":"Response of catalase activity and membrane fluidity of aerobically grown Schizosaccharomyces pombe and Saccharomyces cerevisiae to aeration and the presence of substrates.","citation":"J Gen Microbiol 1993 Jul;139(7):1627-34","abstract":"Intracellular catalase (EC 1.11.1.6) activity of permeabilized aerobically grown cells of Schizosaccharomyces pombe was insensitive to cell aeration and inhibition of protein synthesis, and was only mildly enhanced by the presence of glucose and ethanol via de novo protein synthesis. By contrast, the intracellular catalase activity of Saccharomyces cerevisiae, which, in freshly harvested cells, was two to three times lower than that in Sch. pombe, increased on aeration without substrates or with ethanol and was inhibited on aeration with glucose following cell permeabilization. The enhanced intracellular activity was due to de novo protein synthesis while the inhibitory effect of glucose, absent in Sch. pombe, was caused by one of the major glucose metabolites, succinate. The intact-cell catalase activity of both yeasts increased greatly during aeration. In Sacch. cerevisiae, this increase was again prevented by glucose. In parallel, export of catalase to the cell surface increased in both yeasts. This was especially conspicuous in Sch. pombe aerated in the presence of ethanol, and may represent a protective mechanism against the damaging effects of ethanol. The cell-surface-bound catalase activity was confirmed in isolated plasma membranes of both yeasts. The fluidity of the plasma membrane increased during aeration. This effect was further stimulated by the presence of glucose and to a lesser extent by ethanol. Both yeasts exhibited increased extracellular catalase activity during aeration which could not be caused entirely by cell lysis. In Sch. pombe this activity was strongly enhanced by the presence of ethanol.","authors":"Gille G, Sigler K, Höfer M","authors_abbrev":"Gille G et al.","pubmed_publication_date":"Jul 1993","pubmed_entrez_date":"1993-07-01","publication_year":"1993","canto_session_key":"75247310f2a58db1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-03-01 15:56:54","canto_approved_date":"2021-03-01 15:56:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-03-01 15:55:58","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC757.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2021-03-01"},{"uniquename":"PMID:19279143","title":"Role of the RNA-binding protein Nrd1 and Pmk1 mitogen-activated protein kinase in the regulation of myosin mRNA stability in fission yeast.","citation":"Mol Biol Cell 2009 May;20(9):2473-85","abstract":"Myosin II is an essential component of the actomyosin contractile ring and plays a crucial role in cytokinesis by generating the forces necessary for contraction of the actomyosin ring. Cdc4 is an essential myosin II light chain in fission yeast and is required for cytokinesis. In various eukaryotes, the phosphorylation of myosin is well documented as a primary means of activating myosin II, but little is known about the regulatory mechanisms of Cdc4. Here, we isolated Nrd1, an RNA-binding protein with RNA-recognition motifs, as a multicopy suppressor of cdc4 mutants. Notably, we demonstrated that Nrd1 binds and stabilizes Cdc4 mRNA, thereby suppressing the cytokinesis defects of the cdc4 mutants. Importantly, Pmk1 mitogen-activated protein kinase (MAPK) directly phosphorylates Nrd1, thereby negatively regulating the binding activity of Nrd1 to Cdc4 mRNA. Consistently, the inactivation of Pmk1 MAPK signaling, as well as Nrd1 overexpression, stabilized the Cdc4 mRNA level, thereby suppressing the cytokinesis defects associated with the cdc4 mutants. In addition, we demonstrated the cell cycle-dependent regulation of Pmk1/Nrd1 signaling. Together, our results indicate that Nrd1 plays a role in the regulation of Cdc4 mRNA stability; moreover, our study is the first to demonstrate the posttranscriptional regulation of myosin expression by MAPK signaling.","authors":"Satoh R, Morita T, Takada H, Kita A, Ishiwata S, Doi A, Hagihara K, Taga A, Matsumura Y, Tohda H, Sugiura R","authors_abbrev":"Satoh R et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-03-13","publication_year":"2009","canto_session_key":"61148469370725b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-01-10 15:13:24","canto_approved_date":"2026-01-30 15:17:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-01-07 09:40:42","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":62,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAC4A8.05c","SPBC543.07","SPAC926.03","SPAC2F7.11","SPBC19C2.05","SPBC119.08","SPAC24B11.06c","SPAC31G5.09c","SPCC613.04c","SPAP8A3.08"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2020-01-10"},{"uniquename":"PMID:15907173","title":"Expression and purification of the carboxyl terminus domain of Schizosaccharomyces pombe dicer in Escherichia coli.","citation":"Protein Pept Lett 2005 May;12(4):311-4","abstract":"The carboxyl terminus domain of Schizosaccharomyces pombe dicer (yDicerC) was expressed in Escherichia coli as an MBP-fusion protein (MBP-yDicerC). When the E. coli strain was cultured and induced at 25 degrees C, the MBP-yDicerC was partly expressed in the soluble fraction. It was then purified by two step affinity chromatography with amylose resin and Ni-NTA His Bind(R) resin. The purified MBP-yDicerC showed double-strand RNA digestion activity. siRNA-like products about 22-nt in length were generated.","authors":"Qian Z, Xuan B, Hong J, Hao Z, Wang L, Huang W","authors_abbrev":"Qian Z et al.","pubmed_publication_date":"May 2005","pubmed_entrez_date":"2005-05-24","publication_year":"2005","canto_session_key":"42ff5e517d74ae6c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-07-12 13:15:25","canto_session_submitted_date":"2012-04-26 16:25:41","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.13c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-04-26"},{"uniquename":"PMID:22806344","title":"Genome-wide screen reveals novel mechanisms for regulating cobalt uptake and detoxification in fission yeast.","citation":"Mol Genet Genomics 2012 Aug;287(8):651-62","abstract":"Cobalt is an essential micronutrient but is toxic when present in excess. To study cobalt homeostasis we performed a genome-wide screen for deletion strains that show sensitivity or resistance to CoCl(2). Among 54 cobalt-sensitive strains, 18 are supersensitive strains, which are involved in histidine biosynthetic process, ubiquitination, mitochondria function, membrane trafficking, transporter and a variety of other known functions or still unknown functions. Furthermore, we identified 56 cobalt-resistant deletion strains, which are mainly involved in mitochondria function, signal transduction, ubiquitination, and gene expression and chromatin remodeling. Notably, deletion of the zhf1(+) gene, encoding a zinc ion transporter, confers supersensitivity to cobalt and overexpression of the zhf1(+) gene confers marked tolerance to cobalt, indicating that Zhf1 play key roles in cobalt detoxification. Interestingly, all the histidine-auxotrophic mutants displayed cobalt sensitivity and deletion of cationic amino acid transporter Cat1, which was shown to be involved in histidine uptake, suppressed the CoCl(2)-sensitive growth defect of the his2 mutants, suggesting that CoCl(2) may be transported into the cell together with histidine via histidine transporters including Cat1. In addition, we obtained results suggesting that the E2 ubiquitin conjugating enzyme Rhp6 and Sty1 stress MAP kinase pathway are involved in the regulation of cobalt homeostasis. Altogether, our genome-wide study demonstrates for the first time the mechanisms of cobalt homeostasis, particularly its uptake and detoxification in fission yeast.","doi":"10.1007/s00438-012-0705-9","authors":"Ryuko S, Ma Y, Ma N, Sakaue M, Kuno T","authors_abbrev":"Ryuko S et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-07-19","publication_year":"2012","canto_session_key":"e461d6a93db62735","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-09-16 14:15:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-24 13:44:05","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":110,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_22806344_phaf.tsv"}],"genes":["SPBC2F12.12c","SPBC21D10.12","SPAC3G9.05","SPAC17C9.02c","SPAC23C11.14","SPBC577.11","SPAC31G5.19","SPAC56F8.12","SPCC4B3.03c","SPAC750.08c","SPAC22E12.14c","SPBC56F2.03","SPAC6B12.07c","SPBC947.10","SPBC365.14c","SPBC119.12","SPAC13G6.09","SPCC1442.02","SPBC11B10.02c","SPAC869.11","SPBC119.06","SPBC31F10.15c","SPCC1884.02","SPAC328.04","SPAPB17E12.08","SPAC3H1.11","SPAC328.09","SPCC24B10.08c","SPBC27.06c","SPCC1020.11c","SPAPB1E7.02c","SPAC6F6.01","SPBC21H7.07c","SPBC31F10.10c","SPAC823.10c","SPAC19G12.02c","SPCC965.13","SPAC17G8.13c","SPBC36B7.03","SPCC594.04c","SPCC4F11.04c","SPCC1235.09","SPAC664.14","SPBC15D4.10c","SPBC660.10","SPBC1683.10c","SPBC1604.02c","SPAC23C4.11","SPAC1783.07c","SPAC823.05c","SPAC14C4.14","SPBC18H10.02","SPAC23C11.08","SPAC23C11.02c","SPAC31A2.14","SPBC947.05c","SPBC887.10","SPAC3F10.09","SPBC29A3.13","SPAC4A8.03c","SPAC3A12.12","SPAC22F3.07c","SPCC613.12c","SPBC19C7.02","SPBC21D10.09c","SPAP8A3.04c","SPAC20H4.02","SPAC1F5.07c","SPAC644.14c","SPAC1006.09","SPAC30D11.07","SPAC3F10.04","SPCC1682.01","SPBC8D2.01","SPCC830.06","SPBC28F2.02","SPAC2F7.04","SPBC2G2.08","SPAC25G10.05c","SPBC3H7.03c","SPBC4F6.06","SPBP4H10.03","SPAC10F6.13c","SPAC3C7.06c","SPAC4D7.11","SPBC4F6.08c","SPAC26H5.05","SPAC1783.01","SPAC343.18","SPBC1718.07c","SPAC26A3.16","SPAC3H8.09c","SPBC691.03c","SPBC18H10.06c","SPBC776.04","SPBC29A3.02c","SPBP35G2.14","SPAC13G7.11","SPAC144.06","SPBC4C3.08","SPBC1711.13","SPBC887.04c","SPBC409.07c","SPAC6G10.11c","SPAC9G1.04","SPBC25B2.04c","SPBP4H10.19c","SPAC1486.02c","SPCC285.16c","SPAC19A8.10","SPAC25B8.01"],"gene_count":111,"ltp_gene_count":3,"approved_date":"2014-07-24"},{"uniquename":"PMID:36408846","title":"Differential phosphorylation of Clr4 SUV39H  by Cdk1 accompanies a histone H3 methylation switch that is essential for gametogenesis.","citation":"EMBO Rep 2023 Jan 09;24(1):e55928","abstract":"Methylation of histone H3 at lysine 9 (H3K9) is a hallmark of heterochromatin that plays crucial roles in gene silencing, genome stability, and chromosome segregation. In Schizosaccharomyces pombe, Clr4 mediates both di- and tri-methylation of H3K9. Although H3K9 methylation has been intensely studied in mitotic cells, its role during sexual differentiation remains unclear. Here, we map H3K9 methylation genome-wide during meiosis and show that constitutive heterochromatin temporarily loses H3K9me2 and becomes H3K9me3 when cells commit to meiosis. Cells lacking the ability to tri-methylate H3K9 exhibit meiotic chromosome segregation defects. Finally, the H3K9 methylation switch is accompanied by differential phosphorylation of Clr4 by the cyclin-dependent kinase Cdk1. Our results suggest that a conserved master regulator of the cell cycle controls the specificity of an H3K9 methyltransferase to prevent ectopic H3K9 methylation and to ensure faithful gametogenesis.","doi":"10.15252/embr.202255928","authors":"Kuzdere T, Flury V, Schalch T, Iesmantavicius V, Hess D, Bühler M","authors_abbrev":"Kuzdere T et al.","pubmed_publication_date":"09 Jan 2023","pubmed_entrez_date":"2022-11-21","publication_year":"2023","canto_session_key":"d77be516bab87443","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Marc Bühler","canto_first_approved_date":"2023-02-03 15:07:26","canto_approved_date":"2024-10-18 09:38:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-28 10:26:06","canto_added_date":"2022-11-23 01:15:05","annotation_curators":[{"name":"Marc Bühler","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPBC428.08c","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-02-03"},{"uniquename":"PMID:30244281","title":"Intricate regulation on epigenetic stability of the subtelomeric heterochromatin and the centromeric chromatin in fission yeast.","citation":"Curr Genet 2019 Apr;65(2):381-386","abstract":"In eukaryotes, the integrity of chromatin structure and organization is crucial to diverse key cellular processes from development to disease avoidance. To maintain the cell identity through mitotic cell generations, the genome (the genomic DNA sequence) as well as the epigenome (pertaining various forms of epigenetic information carriers, such as histone modifications, nucleosome positioning and the chromatin organization) is inherited with high fidelity. In comparison to the wealth of knowledge on genetic stability, we know much less on what may control the accuracy of epigenetic inheritance. In our recent work in the fission yeast Schizosaccharomyces pombe, by quantifying the epigenetic fidelity of CENP-A/Cnp1 or H3K9me2 nucleosome inheritance through cell divisions, we demonstrated that Ccp1, a homolog of histone chaperone Vps75 in budding yeast, participates in the modulation of centromeric nucleosomal epigenetic stability as well as proper heterochromatin organization. In this essay, we focus on discussing the uniquely high dynamicity of the subtelomeric heterochromatin regions and the complex mechanisms regulating epigenetic stability of centromeric chromatin.","doi":"10.1007/s00294-018-0886-9","authors":"Lu M, He X","authors_abbrev":"Lu M et al.","pubmed_publication_date":"Apr 2019","pubmed_entrez_date":"2018-09-24","publication_year":"2019","canto_session_key":"17eeab988c8528ba","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-09-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24374313","title":"Determinants of heterochromatic siRNA biogenesis and function.","citation":"Mol Cell 2014 Jan 23;53(2):262-76","abstract":"Endogenous small interfering RNAs (siRNAs) and other classes of small RNA provide the specificity signals for silencing of transposons and repeated DNA elements at the posttranscriptional and transcriptional levels. However, the determinants that define an siRNA-producing region or control the silencing function of siRNAs are poorly understood. Here we show that convergent antisense transcription and availability of the Dicer ribonuclease are the key determinants for primary siRNA generation. Surprisingly, Dicer makes dual contributions to heterochromatin formation, promoting histone H3 lysine 9 methylation independently of its catalytic activity, in addition to its well-known role in catalyzing siRNA generation. Furthermore, sequences in the 3' UTR of an mRNA-coding gene inhibit the ability of siRNAs to promote heterochromatin formation, providing another layer of control that prevents the silencing of protein-coding RNAs. Our results reveal distinct mechanisms that limit siRNA generation to centromeric DNA repeats and prevent spurious siRNA-mediated silencing at euchromatic loci.","doi":"10.1016/j.molcel.2013.11.014","authors":"Yu R, Jih G, Iglesias N, Moazed D","authors_abbrev":"Yu R et al.","pubmed_publication_date":"23 Jan 2014","pubmed_entrez_date":"2013-12-31","publication_year":"2014","canto_session_key":"164f3f8ea3cc788b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27545501","title":"Building on the Ccr4-Not architecture.","citation":"Bioessays 2016 Oct;38(10):997-1002","abstract":"In a recent issue of Nature Communications Ukleja and co-workers reported a cryo-EM 3D reconstruction of the Ccr4-Not complex from Schizosaccharomyces pombe with an immunolocalization of the different subunits. The newly gained architectural knowledge provides cues to apprehend the functional diversity of this major eukaryotic regulator. Indeed, in the cytoplasm alone, Ccr4-Not regulates translational repression, decapping and deadenylation, and the Not module additionally plays a positive role in translation. The spatial distribution of the subunits within the structure is compatible with a model proposing that the Ccr4-Not complex interacts with the 5' and 3' ends of target mRNAs, allowing different functional modules of the complex to act at different stages of the translation process, possibly within a circular constellation of the mRNA. This work opens new avenues, and reveals important gaps in our understanding regarding structure and mode of function of the Ccr4-Not complex that need to be addressed in the future.","doi":"10.1002/bies.201600051","authors":"Villanyi Z, Collart MA","authors_abbrev":"Villanyi Z et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-08-23","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-08-25 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9016341","title":"Role of determinants of cadmium sensitivity in the tolerance of Schizosaccharomyces pombe to cisplatin.","citation":"Mol Pharmacol 1997 Jan;51(1):12-8","abstract":"The genetic mechanisms underlying cisplatin (DDP) resistance in yeast were investigated by examining the cytotoxicity of DDP to Schizosaccharomyces pombe mutants that were either hypersensitive or resistant to Cd. Despite reports that have linked glutathione (GSH) to DDP resistance in human cancer cells, we found that a mutant of S. pombe that was hypersensitive to Cd by virtue of a 15-fold reduction in GSH level and lack of phytochelatin production was as tolerant as the wild-type strain to DDP. A mutant that harbored a mutation in hmt1, the gene encoding an ATP-binding cassette-type transporter for vacuolar sequestration of a phytochelatin/Cd complex, exhibited only mild hypersensitivity to DDP even though it was 100-fold more sensitive to Cd. Overexpression of hmt1 in wild-type or mutant cells conferred tolerance to Cd but failed to do the same for DDP. However, a strain that produced 6-fold more sulfide than wild-type cells was found to be 6-fold more resistant to DDP and twice as resistant to Cd; an association between DDP resistance and sulfide production was observed in three other strains that were examined, and overproduction of sulfide was accompanied by reduced platination of DNA. These results indicate that GSH and the GSH-derived phytochelatin peptides do not play critical roles in determining sensitivity to DDP in S. pombe but rather identify increased production of sulfide as a possible new mechanism of DDP resistance that may also be relevant to human cells.","authors":"Perego P, Vande Weghe J, Ow DW, Howell SB","authors_abbrev":"Perego P et al.","pubmed_publication_date":"Jan 1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_session_key":"d2c7801677e3387e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-10-26 11:16:06","canto_approved_date":"2022-02-02 11:47:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-01 17:47:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.09c","SPAC10F6.01c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-10-26"},{"uniquename":"PMID:22187461","title":"The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together.","citation":"Proc Natl Acad Sci U S A 2012 Jan 03;109(1):149-54","abstract":"Proteasomes execute the degradation of most cellular proteins. Although the 20S core particle (CP) has been studied in great detail, the structure of the 19S regulatory particle (RP), which prepares ubiquitylated substrates for degradation, has remained elusive. Here, we report the crystal structure of one of the RP subunits, Rpn6, and we describe its integration into the cryo-EM density map of the 26S holocomplex at 9.1 Å resolution. Rpn6 consists of an α-solenoid-like fold and a proteasome COP9/signalosome eIF3 (PCI) module in a right-handed suprahelical configuration. Highly conserved surface areas of Rpn6 interact with the conserved surfaces of the Pre8 (alpha2) and Rpt6 subunits from the alpha and ATPase rings, respectively. The structure suggests that Rpn6 has a pivotal role in stabilizing the otherwise weak interaction between the CP and the RP.","doi":"10.1073/pnas.1117648108","authors":"Pathare GR, Nagy I, Bohn S, Unverdorben P, Hubert A, Körner R, Nickell S, Lasker K, Sali A, Tamura T, Nishioka T, Förster F, Baumeister W, Bracher A","authors_abbrev":"Pathare GR et al.","pubmed_publication_date":"03 Jan 2012","pubmed_entrez_date":"2011-12-22","publication_year":"2012","canto_session_key":"e45f7be345d412be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-30 12:28:49","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-30 12:28:44","canto_added_date":"2016-09-21 00:19:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC23G7.12c","SPAC23G3.11","SPCC1442.06"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-09-30"},{"uniquename":"PMID:37590302","title":"The AAA-ATPase Yta4/ATAD1 interacts with the mitochondrial divisome to inhibit mitochondrial fission.","citation":"PLoS Biol 2023 Aug;21(8):e3002247","abstract":"Mitochondria are in a constant balance of fusion and fission. Excessive fission or deficient fusion leads to mitochondrial fragmentation, causing mitochondrial dysfunction and physiological disorders. How the cell prevents excessive fission of mitochondria is not well understood. Here, we report that the fission yeast AAA-ATPase Yta4, which is the homolog of budding yeast Msp1 responsible for clearing mistargeted tail-anchored (TA) proteins on mitochondria, plays a critical role in preventing excessive mitochondrial fission. The absence of Yta4 leads to mild mitochondrial fragmentation in a Dnm1-dependent manner but severe mitochondrial fragmentation upon induction of mitochondrial depolarization. Overexpression of Yta4 delocalizes the receptor proteins of Dnm1, i.e., Fis1 (a TA protein) and Mdv1 (the bridging protein between Fis1 and Dnm1), from mitochondria and reduces the localization of Dnm1 to mitochondria. The effect of Yta4 overexpression on Fis1 and Mdv1, but not Dnm1, depends on the ATPase and translocase activities of Yta4. Moreover, Yta4 interacts with Dnm1, Mdv1, and Fis1. In addition, Yta4 competes with Dnm1 for binding Mdv1 and decreases the affinity of Dnm1 for GTP and inhibits Dnm1 assembly in vitro. These findings suggest a model, in which Yta4 inhibits mitochondrial fission by inhibiting the function of the mitochondrial divisome composed of Fis1, Mdv1, and Dnm1. Therefore, the present work reveals an uncharacterized molecular mechanism underlying the inhibition of mitochondrial fission.","doi":"10.1371/journal.pbio.3002247","authors":"He J, Liu K, Wu Y, Zhao C, Yan S, Chen JH, Hu L, Wang D, Zheng F, Wei W, Xu C, Huang C, Liu X, Yao X, Ding L, Fang Z, Tang AH, Fu C","authors_abbrev":"He J et al.","pubmed_publication_date":"Aug 2023","pubmed_entrez_date":"2023-08-17","publication_year":"2023","canto_session_key":"054ab9697f2d7ae0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jiajia He","canto_first_approved_date":"2023-08-30 14:47:56","canto_approved_date":"2023-11-10 18:57:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-08-30 12:50:41","canto_added_date":"2023-08-18 00:15:04","annotation_curators":[{"name":"Jiajia He","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11G11.01","SPCC24B10.10c","SPAC664.15","SPBC12C2.08","SPAC140.01"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2023-08-30"},{"uniquename":"PMID:4211223","title":"Genes and isoenzymes controlling the first step in the aromatic amino acid biosynthesis in Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1974 Jun 18;350(2):319-27","abstract":"","authors":"Schweingruber ME, Wyssling HB","authors_abbrev":"Schweingruber ME et al.","pubmed_publication_date":"18 Jun 1974","pubmed_entrez_date":"1974-06-18","publication_year":"1974","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11180454","title":"The cyclic AMP/PKA signal pathway is required for initiation of spore germination in Schizosaccharomyces pombe.","citation":"Yeast 2001 Feb;18(3):207-17","abstract":"Spore germination, a transition from the quiescent G0 phase to the proliferation cycle, is triggered by glucose in Schizosaccharomyces pombe. The role of cAMP/protein kinase A (PKA) signalling in germination is investigated. Gene disruption of cyr1+, pka1+ and gpa2+ encoding adenylate cyclase, PKA and the alpha-subunit of a trimeric GTP-binding protein, respectively, reduced the colony-forming efficiency of spores in minimal medium. Isolated spores of these null mutants did not germinate in minimal medium for up to 12 h, at which time wild-type spores had completed germination and formed germ projections. In wild-type spores, cortical actin patches randomly distributed in the early stage of outgrowth and then localized to one side of spores before the formation of projections. In contrast, the mutant spores exhibited no actin patches, but the cell surface was predominantly stained, like ungerminated spores of wild-type. Flow fluorocytometric analysis of propidium iodide-stained spores revealed a distinct 1C DNA peak after germination was completed. The fluorescent profile of the mutant spores, however, did not change during 12 h incubation in the minimal medium. These observations indicate that spores harbouring either cyr1Delta, pka1Delta or gpa2Delta are hardly triggered to germination. When wild-type spores were exposed to glucose, the intracellular cAMP level transiently increased in a few minutes, but gpa2Delta spores did not respond to glucose. We conclude that S. pombe spores initiate germination in response to glucose through the cyclic AMP-PKA pathway.","authors":"Hatanaka M, Shimoda C","authors_abbrev":"Hatanaka M et al.","pubmed_publication_date":"Feb 2001","pubmed_entrez_date":"2001-02-17","publication_year":"2001","canto_session_key":"06326d4a1effbdd3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-07-15 10:54:36","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-15 10:54:30","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H3.13c","SPBC19C7.03","SPBC106.10","SPAC1B9.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-07-15"},{"uniquename":"PMID:34705258","title":"Non-mitochondrial aconitase regulates the expression of iron-uptake genes by controlling the RNA turnover process in fission yeast.","citation":"J Microbiol 2021 Dec;59(12):1075-1082","abstract":"Aconitase, a highly conserved protein across all domains of life, functions in converting citrate to isocitrate in the tricarboxylic acid cycle. Cytosolic aconitase is also known to act as an iron regulatory protein in mammals, binding to the RNA hairpin structures known as iron-responsive elements within the untranslated regions of specific RNAs. Aconitase-2 (Aco2) in fission yeast is a fusion protein consisting of an aconitase and a mitochondrial ribosomal protein, bL21, residing not only in mitochondria but also in cytosol and the nucleus. To investigate the role of Aco2 in the nucleus and cytoplasm of fission yeast, we analyzed the transcriptome of aco2ΔN mutant that is deleted of nuclear localization signal (NLS). RNA sequencing revealed that the aco2ΔN mutation caused increase in mRNAs encoding iron uptake transporters, such as Str1, Str3, and Shu1. The half-lives of mRNAs for these genes were found to be significantly longer in the aco2ΔN mutant than the wild-type strain, suggesting the role of Aco2 in mRNA turnover. The three conserved cysteines required for the catalytic activity of aconitase were not necessary for this role. The UV cross-linking RNA immunoprecipitation analysis revealed that Aco2 directly bound to the mRNAs of iron uptake transporters. Aco2-mediated degradation of iron-uptake mRNAs appears to utilize exoribonuclease pathway that involves Rrp6 as evidenced by genetic interactions. These results reveal a novel role of non-mitochondrial aconitase protein in the mRNA turnover in fission yeast to fine-tune iron homeostasis, independent of regulation by transcriptional repressor Fep1.","doi":"10.1007/s12275-021-1438-4","authors":"Cho SY, Jung SJ, Kim KD, Roe JH","authors_abbrev":"Cho SY et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-10-27","publication_year":"2021","canto_session_key":"6bfb6c024496e30a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-10-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000073","title":"Representation of import of a chemical as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the import of a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom template is \"GO:0006810 and 'imports' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12058392","title":"Viability and formation of conjugated dienes in plasma membrane lipids of Saccharomyces cerevisiae, Schizosaccharomyces pombe, Rhodotorula glutinis and Candida albicans exposed to hydrophilic, amphiphilic and hydrophobic pro-oxidants.","citation":"Folia Microbiol (Praha) 2002;47(2):145-51","abstract":"Effects of four lipid peroxidation-inducing pro-oxidants--amphiphilic tert-butyl hydroperoxide (TBHP), hydrophobic 1,1'-azobis(4-cyclohexanecarbonitrile) (ACHN), hydrophilic FeII and 2,2'-azobis(2-amidinopropane)dihydrochloride (AAPH)--on cell growth and on generation of peroxidation products in isolated plasma membrane lipids were determined in four yeast species (S. cerevisiae, S. pombe, R. glutinis and C. albicans) differing in their plasma membrane lipid composition. TBHP and ACHN inhibited cell growth most strongly, FeII and AAPH exerted inhibitory action for about 2 h, with subsequent cell growth resumption. S. cerevisiae strain SP4 was doped during growth with unsaturated linoleic (18:2) and linolenic (18:3) acids to change its resistance to lipid peroxidation. Its plasma membranes then contained some 30% of these acids as compared with some 1.3% of 18:2 acid found in undoped S. cerevisiae, while the content of (16:1) and (18:1) acids was lower than in undoped S. cerevisiae. The presence of linoleic and linolenic acids in S. cerevisiae cells lowered cell survival and increased the sensitivity to pro-oxidants. Peroxidation-generated conjugated dienes (CD) were measured in pure TBHP- and ACHN-exposed fatty acids used as standards. The CD level depended on the extent of unsaturation and the pro-oxidant used. The TBHP-induced CD production in a mixture of oleic acid and its ester was somewhat lower than in free acid and ester alone. In lipids isolated from the yeast plasma membranes, the CD production was time-dependent and decreased after a 5-15-min pro-oxidant exposure. ACHN was less active than TBHP. The most oxidizable were lipids from S. cerevisiae plasma membranes doped with linoleic and linolenic acids and from C. albicans with indigenous linolenic acid.","authors":"Krasowska A, Chmielewska L, Gapa D, Prescha A, Váchová L, Sigler K","authors_abbrev":"Krasowska A et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-06-13","publication_year":"2002","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15464854","title":"MAPping the eukaryotic tree of life: structure, function, and evolution of the MAP215/Dis1 family of microtubule-associated proteins.","citation":"Int Rev Cytol 2004;239:179-272","abstract":"The MAP215/Dis1 family of proteins is an evolutionarily ancient family of microtubule-associated proteins, with characterized members in all major kingdoms of eukaryotes, including fungi (Stu2 in S. cerevisiae, Dis1 and Alp14 in S. pombe), Dictyostelium (DdCP224), plants (Mor1 in A. thaliana and TMBP200 in N. tabaccum), and animals (Zyg9 in C. elegans, Msps in Drosophila, XMAP215 in Xenopus, and ch-TOG in humans). All MAP215/Dis1 proteins (with the exception of those in plants) localize to microtubule-organizing centers (MTOCs), including spindle pole bodies in yeast and centrosomes in animals, and all bind to microtubules in vitro and?or in vivo. Diverse roles in regulating microtubule assembly and organization have been proposed for individual family members, and a substantial body of evidence suggests that MAP215/Dis1-related proteins play critical roles in the assembly and function of the meiotic/mitotic spindles and/or cell division. An extensive search of public databases (including both EST and genome databases) identified partial sequences predicted to encode more than three dozen new members of the MAP215/Dis1 family, including putative MAP215/Dis1-related proteins in Giardia lamblia and four other protists, sixteen additional species of fungi, six plants, and twelve animals. The structure and function of MAP215/Dis1 proteins are discussed in relation to the evolution of this ancient family of microtubule-associated proteins.","authors":"Gard DL, Becker BE, Josh Romney S","authors_abbrev":"Gard DL et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-10-07","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC895.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22540024","title":"Fission yeast Lem2 and Man1 perform fundamental functions of the animal cell nuclear lamina.","citation":"Nucleus 2012;3(1):60-76","abstract":"In animal cells the nuclear lamina, which consists of lamins and lamin-associated proteins, serves several functions: it provides a structural scaffold for the nuclear envelope and tethers proteins and heterochromatin to the nuclear periphery. In yeast, proteins and large heterochromatic domains including telomeres are also peripherally localized, but there is no evidence that yeast have lamins or a fibrous nuclear envelope scaffold. Nonetheless, we found that the Lem2 and Man1 proteins of the fission yeast Schizosaccharomyces pombe, evolutionarily distant relatives of the Lap2/Emerin/Man1 (LEM) sub-family of animal cell lamin-associated proteins, perform fundamental functions of the animal cell lamina. These integral inner nuclear membrane localized proteins, with nuclear localized DNA binding Helix-Extension-Helix (HEH) domains, impact nuclear envelope structure and integrity, are essential for the enrichment of telomeres at the nuclear periphery and by means of their HEH domains anchor chromatin, most likely transcriptionally repressed heterochromatin, to the nuclear periphery. These data indicate that the core functions of the nuclear lamina are conserved between fungi and animal cells and can be performed in fission yeast, without lamins or other intermediate filament proteins.","doi":"10.4161/nucl.18824","authors":"Gonzalez Y, Saito A, Sazer S","authors_abbrev":"Gonzalez Y et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-04-28","publication_year":"2012","canto_session_key":"654d33ea7fb3acba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-02-06 16:16:19","canto_approved_date":"2021-09-01 09:49:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-17 13:24:34","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.10","SPBC557.03c","SPAC14C4.05c","SPAC26A3.15c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-02-06"},{"uniquename":"PMID:16042377","title":"Molecular-level investigation of the structure, transformation, and bioactivity of single living fission yeast cells by time- and space-resolved Raman spectroscopy.","citation":"Biochemistry 2005 Aug 02;44(30):10009-19","abstract":"The structure, transformation, and bioactivity of single living Schizosaccharomyces pombe cells at the molecular level have been studied in vivo by time- and space-resolved Raman spectroscopy. A time resolution of 100 s and a space resolution of 250 nm have been achieved with the use of a confocal Raman microspectrometer. The space-resolved Raman spectra of living S. pombe cells at different cell cycle stages were recorded in an effort to elucidate the molecular compositions of organelles, including nuclei, cytoplasm, mitochondria, and septa. The time- and space-resolved measurement of the central part of a dividing yeast cell showed continuous spectral evolution from that of the nucleus to those of the cytoplasm and mitochondria and finally to that of the septum, in accordance with the transformation during the cell cycle. A strong Raman band was observed at 1602 cm(-)(1) only when cells were under good nutrient conditions. The effect of a respiration inhibitor, KCN, on a living yeast cell was studied by measuring the Raman spectra of its mitochondria. A sudden disappearance of the 1602 cm(-)(1) band followed by the change in the shape and intensity of the phospholipid bands was observed, indicating a strong relationship between the cell activity and the intensity of this band. We therefore call this band \"the Raman spectroscopic signature of life\". The Raman mapping of a living yeast cell was also carried out. Not only the distributions of molecular species but also those of active mitochondria in the cell were successfully visualized in vivo.","authors":"Huang YS, Karashima T, Yamamoto M, Hamaguchi HO","authors_abbrev":"Huang YS et al.","pubmed_publication_date":"02 Aug 2005","pubmed_entrez_date":"2005-07-27","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009632","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26644575","title":"Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast.","citation":"Proc Natl Acad Sci U S A 2015 Dec 22;112(51):15648-53","abstract":"Dynamic cycling of N-Acetylglucosamine (GlcNAc) on serine and threonine residues (O-GlcNAcylation) is an essential process in all eukaryotic cells except yeast, including Saccharomyces cerevisiae and Schizosaccharomyces pombe. O-GlcNAcylation modulates signaling and cellular processes in an intricate interplay with protein phosphorylation and serves as a key sensor of nutrients by linking the hexosamine biosynthetic pathway to cellular signaling. A longstanding conundrum has been how yeast survives without O-GlcNAcylation in light of its similar phosphorylation signaling system. We previously developed a sensitive lectin enrichment and mass spectrometry workflow for identification of the human O-linked mannose (O-Man) glycoproteome and used this to identify a pleothora of O-Man glycoproteins in human cell lines including the large family of cadherins and protocadherins. Here, we applied the workflow to yeast with the aim to characterize the yeast O-Man glycoproteome, and in doing so, we discovered hitherto unknown O-Man glycosites on nuclear, cytoplasmic, and mitochondrial proteins in S. cerevisiae and S. pombe. Such O-Man glycoproteins were not found in our analysis of human cell lines. However, the type of yeast O-Man nucleocytoplasmic proteins and the localization of identified O-Man residues mirror that of the O-GlcNAc glycoproteome found in other eukaryotic cells, indicating that the two different types of O-glycosylations serve the same important biological functions. The discovery opens for exploration of the enzymatic machinery that is predicted to regulate the nucleocytoplasmic O-Man glycosylations. It is likely that manipulation of this type of O-Man glycosylation will have wide applications for yeast bioprocessing.","doi":"10.1073/pnas.1511743112","authors":"Halim A, Larsen IS, Neubert P, Joshi HJ, Petersen BL, Vakhrushev SY, Strahl S, Clausen H","authors_abbrev":"Halim A et al.","pubmed_publication_date":"22 Dec 2015","pubmed_entrez_date":"2015-12-09","publication_year":"2015","canto_session_key":"9471d468f49914e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-03 10:45:55","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-02-03 10:45:42","canto_added_date":"2015-12-10 01:19:36","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":87,"orcid":"0000-0003-4148-4606","file_type":"protein_modification","file_name":"PMID_26644575_modifications.tsv"}],"genes":["SPBC13G1.11","SPBC25H2.06c","SPCC584.04","SPAC1250.07","SPAC13F5.03c","SPBC660.16","SPAC4F10.14c","SPCC23B6.01c","SPBC11B10.05c","SPBC83.17","SPCC162.07","SPBC12C2.08","SPBC1815.01","SPAC10F6.03c","SPBC14F5.04c","SPCC1235.03","SPBC29A3.02c","SPAC29B12.12","SPCC1020.06c","SPAC1565.05","SPAC869.09","SPCC306.08c","SPAC4A8.08c","SPCC191.01","SPAPB8E5.06c","SPAC926.09c","SPCC126.06","SPBC216.07c","SPCC5E4.05c","SPBC29A10.07","SPAC29A4.15","SPBC354.10","SPAC10F6.16","SPAC1783.08c","SPBC20F10.07","SPBC56F2.06","SPAC1006.06","SPBC17G9.11c","SPAC2G11.12","SPAC24C9.02c","SPCC63.14","SPBC660.15","SPCC576.11","SPAC29A4.12c","SPBC2G2.03c","SPAC17A5.03","SPAC17C9.03","SPBC428.10","SPCC338.12","SPAC821.10c","SPAC16E8.01","SPAC31A2.07c","SPBC19C2.07","SPBC16A3.11","SPCC737.08","SPAC4G9.17c","SPAC343.16","SPAC29A4.04c","SPAC27D7.11c","SPCC1494.07","SPBC3E7.13c","SPCC16C4.09","SPCC794.09c","SPBC27.06c","SPCC965.04c","SPBC3D6.10","SPBC17D11.01","SPAC18G6.04c","SPAC688.04c","SPAC23C11.05","SPAC227.14","SPCC18.14c","SPBC660.09","SPBP8B7.26","SPBC365.12c","SPAC977.15","SPBC13G1.07","SPAC27D7.13c","SPAC1687.06c","SPBP8B7.10c","SPBP16F5.03c","SPAC15A10.16","SPBC21C3.11","SPCC14G10.04","SPAC10F6.06","SPAC22A12.09c","SPAC27D7.09c"],"gene_count":87,"ltp_gene_count":0,"approved_date":"2016-02-03"},{"uniquename":"PMID:25375137","title":"Systematic analysis of the role of RNA-binding proteins in the regulation of RNA stability.","citation":"PLoS Genet 2014 Nov;10(11):e1004684","abstract":"mRNA half-lives are transcript-specific and vary over a range of more than 100-fold in eukaryotic cells. mRNA stabilities can be regulated by sequence-specific RNA-binding proteins (RBPs), which bind to regulatory sequence elements and modulate the interaction of the mRNA with the cellular RNA degradation machinery. However, it is unclear if this kind of regulation is sufficient to explain the large range of mRNA stabilities. To address this question, we examined the transcriptome of 74 Schizosaccharomyces pombe strains carrying deletions in non-essential genes encoding predicted RBPs (86% of all such genes). We identified 25 strains that displayed changes in the levels of between 4 and 104 mRNAs. The putative targets of these RBPs formed biologically coherent groups, defining regulons involved in cell separation, ribosome biogenesis, meiotic progression, stress responses and mitochondrial function. Moreover, mRNAs in these groups were enriched in specific sequence motifs in their coding sequences and untranslated regions, suggesting that they are coregulated at the posttranscriptional level. We performed genome-wide RNA stability measurements for several RBP mutants, and confirmed that the altered mRNA levels were caused by changes in their stabilities. Although RBPs regulate the decay rates of multiple regulons, only 16% of all S. pombe mRNAs were affected in any of the 74 deletion strains. This suggests that other players or mechanisms are required to generate the observed range of RNA half-lives of a eukaryotic transcriptome.","doi":"10.1371/journal.pgen.1004684","authors":"Hasan A, Cotobal C, Duncan CD, Mata J","authors_abbrev":"Hasan A et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-11-07","publication_year":"2014","canto_session_key":"3233320f8849c7ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-02-25 09:43:52","canto_approved_date":"2026-03-03 21:54:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-05-21 03:49:41","canto_added_date":"2014-11-08 01:15:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Pascal Carme","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1263,"orcid":"0009-0003-9059-1333","file_type":"PHAF","file_name":"PMID_25375137_phaf.tsv"}],"genes":["SPBC725.04","SPAC26A3.06","SPAPJ691.03","SPAC17H9.04c","SPAC29B12.13","SPAC11D3.05","SPAC19G12.15c","SPAC27D7.09c","SPBC2G5.03","SPAC19G12.09","SPBC646.06c","SPBC2G5.07c","SPNCRNA.402","SPBC3E7.02c","SPAC26H5.08c","SPACUNK4.17","SPCC622.15c","SPCC16C4.07","SPBC146.08c","SPBC13A2.04c","SPBC56F2.06","SPNCRNA.111","SPBC16A3.13","SPBC557.05","SPBP4H10.08","SPBC1921.03c","SPBC31F10.12","SPAC22F3.12c","SPAC14C4.11","SPNCRNA.517","SPAC57A10.04","SPAC19B12.02c","SPBC9B6.07","SPBC947.07","SPCC736.15","SPAC13G7.02c","SPCC1739.04c","SPAC4G9.05","SPAPB24D3.06c","SPCC1620.13","SPBC365.11","SPCC1919.14c","SPACUNK4.16c","SPCC1322.10","SPAC5D6.05","SPAC30C2.02","SPAC26A3.17c","SPAC22E12.03c","SPNCRNA.243","SPBC16A3.18","SPCC1322.01","SPAC24C9.15c","SPAC10F6.05c","SPBC29A3.18","SPAC25G10.04c","SPCC70.08c","SPCC794.01c","SPAPB1E7.08c","SPBC1703.11","SPNCRNA.29","SPAC2G11.05c","SPBC21B10.09","SPAPB8E5.03","SPNCRNA.239","SPCC1840.06","SPAC19B12.11c","SPAC167.06c","SPAC664.06","SPCC16A11.07","SPCC23B6.03c","SPBC27B12.10c","SPBC11C11.01","SPCC191.03c","SPBC119.05c","SPBC1A4.07c","SPBC1683.08","SPBC660.06","SPCC576.02","SPBC106.12c","SPBC30B4.07c","SPBC1711.07","SPAC1F12.02c","SPBC16H5.12c","SPAC521.03","SPAC3H8.09c","SPNCRNA.525","SPAC110.01","SPAC1B3.17","SPCC16A11.01","SPAC1250.05","SPBC649.04","SPNCRNA.304","SPAC6B12.16","SPAC18B11.04","SPAC7D4.05","SPAC513.02","SPCC794.12c","SPAC56F8.16","SPAC343.06c","SPBC1685.11","SPAC1952.13","SPNCRNA.1032","SPAC9.10","SPBP23A10.04","SPAC31G5.11","SPNCRNA.28","SPCC4G3.17","SPNCRNA.928","SPAPB2B4.04c","SPAC1565.04c","SPAC6F6.06c","SPBC16H5.14c","SPAC1F5.07c","SPBP8B7.24c","SPBC215.14c","SPBPB21E7.09","SPCC1840.07c","SPCC1259.03","SPCC4F11.05","SPAC57A7.13","SPCC24B10.06","SPNCRNA.278","SPCC16C4.03","SPBC947.10","SPAC1F8.06","SPBP19A11.02c","SPBC244.02c","SPCC23B6.02c","SPCC645.08c","SPBC577.13","SPAC1B3.11c","SPBC1683.09c","SPBC359.03c","SPAC22H10.12c","SPCC364.07","SPAC17A5.10","SPCC1393.07c","SPAC1610.04","SPBC12C2.04","SPAC1D4.11c","SPAC227.06","SPNCRNA.21","SPNCRNA.62","SPCC338.18","SPAC16E8.16","SPCC1442.10c","SPAC637.03","SPBC800.06","SPAC1B3.16c","SPAC977.10","SPAC2E1P5.01c","SPAC13G6.15c","SPBC1198.07c","SPAC15A10.09c","SPAC2H10.01","SPBC409.15","SPNCRNA.448","SPCC1494.03","SPBC25H2.04c","SPCC1322.14c","SPCC1020.06c","SPBC2G2.13c","SPBPB2B2.13","SPCC1183.09c","SPCC736.13","SPAC688.04c","SPAC27F1.08","SPBC3B9.12","SPBC713.11c","SPCC364.01","SPBC20F10.06","SPNCRNA.253","SPBC26H8.01","SPBC3B9.01","SPBC1711.05","SPAC17A2.04c","SPBPB2B2.05","SPAC1834.11c","SPBC29A3.06","SPBC1289.16c","SPBPB21E7.04c","SPCC70.02c","SPCC70.09c","SPAC27D7.03c","SPBC8D2.09c","SPBC29A3.13","SPAC13A11.03","SPAC27D7.13c","SPAC4F8.06","SPBC21.07c","SPBP16F5.06","SPAC31G5.02","SPAC19A8.07c","SPBC1718.02","SPCC622.08c","SPBC725.03","SPAC20H4.05c","SPAC18G6.12c","SPAC9E9.09c","SPBC14F5.04c","SPBC4F6.06","SPNCRNA.184","SPCC4B3.13","SPAC31G5.09c","SPCC757.09c","SPAC17C9.08","SPCC1682.08c","SPBC14F5.11c","SPAC22F8.04","SPAC26A3.01","SPBC23G7.13c","SPCC1739.08c","SPAC17A2.09c","SPAC2F7.11","SPBC530.10c","SPCC1906.03","SPAC11D3.14c","SPCC338.12","SPBC24C6.06","SPBC428.10","SPBP8B7.05c","SPCC1020.12c","SPAC17H9.05","SPBC14F5.05c","SPAC1705.03c","SPNCRNA.9001","SPNCRNA.275","SPAC15A10.01","SPAC10F6.10","SPAC750.08c","SPAC23A1.03","SPCC126.11c","SPAC8C9.16c","SPBC216.02","SPNCRNA.123","SPBC530.02","SPCC645.13","SPAP7G5.04c","SPBC1347.01c","SPAC977.17","SPCC4E9.01c","SPBC1711.14","SPBC1703.05","SPAC10F6.01c","SPAC806.04c","SPBC14F5.08","SPAC1250.04c","SPAC869.10c","SPCC825.03c","SPCC569.08c","SPAC12G12.03","SPAC869.02c","SPCPB1C11.03","SPCC63.14","SPACUNK12.02c","SPCC63.02c","SPAC25B8.15c","SPAC1006.03c","SPAC22G7.06c","SPAC19G12.07c","SPAC16A10.01","SPBC15D4.02","SPAC23H3.09c","SPAC25H1.05","SPCC330.02","SPAPB1A10.12c","SPBC725.10","SPBC30B4.02c","SPAC17D4.02","SPAC1527.03","SPAC5H10.04","SPAC922.04","SPAC9.09","SPAC13G7.06","SPAC20G4.04c","SPCC1223.12c","SPAC25G10.01","SPCC550.08","SPBC646.17c","SPAC1610.03c","SPAC24H6.10c","SPBC902.04","SPAC27D7.08c","SPBC3B8.05","SPCC18.18c","SPBC32H8.11","SPNCRNA.04","SPCC417.11c","SPAC27D7.12c","SPAC1B3.01c","SPAC15E1.10","SPBC1734.12c","SPAC17G8.02","SPAC4C5.03","SPCC1450.10c","SPCC2H8.02","SPNCRNA.529","SPAC15A10.04c","SPBC1734.13","SPAC343.12","SPAC1F8.03c","SPBC16C6.08c","SPBC4B4.07c","SPAC57A10.03","SPAC22G7.03","SPCC1742.01","SPAC23A1.09","SPAC17G8.10c","SPAC26F1.06","SPBC1539.03c","SPCC11E10.03","SPAC1F8.01","SPBC106.03","SPAC19D5.05c","SPBP35G2.04c","SPAP8A3.04c","SPAC27D7.14c","SPAC5H10.01","SPCC4B3.14","SPAC11E3.13c","SPBC19F5.01c","SPCC790.03","SPCC1223.09","SPAC1006.01","SPCC965.06","SPBC19C2.05","SPAC17G6.11c","SPCC569.05c","SPAC23H4.09","SPAC2G11.13","SPAC17D4.01","SPBC2G2.05","SPCC1739.10","SPBC1683.04","SPCC737.04","SPBC16G5.13","SPBC25B2.08","SPAC11D3.13","SPAC1142.09","SPCC191.11","SPBC660.11","SPCC965.05c","SPNCRN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genome wide study in fission yeast reveals nine PPR proteins that regulate mitochondrial gene expression.","citation":"Nucleic Acids Res 2011 Oct;39(18):8029-41","abstract":"Pentatricopeptide repeat (PPR) proteins are particularly numerous in plant mitochondria and chloroplasts, where they are involved in different steps of RNA metabolism, probably due to the repeated 35 amino acid PPR motifs that are thought to mediate interactions with RNA. In non-photosynthetic eukaryotes only a handful of PPR proteins exist, for example the human LRPPRC, which is involved in a mitochondrial disease. We have conducted a systematic study of the PPR proteins in the fission yeast Schizosaccharomyces pombe and identified, in addition to the mitochondrial RNA polymerase, eight proteins all of which localized to the mitochondria, and showed some association with the membrane. The absence of all but one of these PPR proteins leads to a respiratory deficiency and modified patterns of steady state mt-mRNAs or newly synthesized mitochondrial proteins. Some cause a general defect, whereas others affect specific mitochondrial RNAs, either coding or non-coding: cox1, cox2, cox3, 15S rRNA, atp9 or atp6, sometimes leading to secondary defects. Interestingly, the two possible homologs of LRPPRC, ppr4 and ppr5, play opposite roles in the expression of the cox1 mt-mRNA, ppr4 being the first mRNA-specific translational activator identified in S. pombe, whereas ppr5 appears to be a general negative regulator of mitochondrial translation.","doi":"10.1093/nar/gkr511","authors":"Kühl I, Dujeancourt L, Gaisne M, Herbert CJ, Bonnefoy N","authors_abbrev":"Kühl I et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-07-06","publication_year":"2011","canto_session_key":"da671cd7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-12-12 16:48:57","canto_approved_date":"2019-01-18 16:36:07","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-12-12 16:48:46","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":95,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.03c","SPCC11E10.04","SPMIT.11","SPMIT.04","SPMIT.07","SPRRNA.02","SPBC19G7.07c","SPAC26H5.12","SPAC8C9.06c","SPMIT.10","SPRRNA.01","SPMIT.05","SPMIT.01","SPBC16G5.14c","SPBC1289.06c","SPMIT.09","SPBC1604.02c","SPAC1093.01","SPBC18H10.11c"],"gene_count":19,"ltp_gene_count":9,"approved_date":"2018-12-12"},{"uniquename":"PMID:8381667","title":"Isolation and characterization of diadenosine tetraphosphate (Ap4A) hydrolase from Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1993 Feb 13;1161(2-3):139-48","abstract":"An enzyme that catalyzes the asymmetric hydrolysis of Ap4A has been partially purified from the fission yeast, Schizosaccharomyces pombe. The crude supernatant fraction from log-phase cells was fractionated by (NH4)2SO4 precipitation followed by chromatography on DEAE-cellulose, Red A dye-ligand and QAE-Sepharose resins. Two peaks of Ap4A hydrolase activity, designated major and minor, were separated on the Red A dye-ligand resin. Both the major and minor Ap4A hydrolase have an apparent molecular mass of 49 kDa based on gel filtration chromatography. On a SDS polyacrylamide gel, a protein of 22 kDa exhibited Ap4A hydrolase activity. Both forms of the enzyme have a Km value in the range of 22 to 36 microM for Ap4A. Both forms of the enzyme asymmetrically hydrolyze Ap4A to AMP and ATP as determined by HPLC. Ap4A is the optimal substrate among several nucleotides and dinucleoside polyphosphates tested at 10 microM. A divalent metal cation is required for activity. Concentrations of Pi below 30 mM stimulate Ap4A hydrolase while higher concentrations inhibit the activity. Pi is not a substrate for this Ap4A-degradative enzyme. Fluoride, from 50 microM to 20 mM, has no significant effect on Ap4A hydrolase activity.","authors":"Robinson AK, de la Peña CE, Barnes LD","authors_abbrev":"Robinson AK et al.","pubmed_publication_date":"13 Feb 1993","pubmed_entrez_date":"1993-02-13","publication_year":"1993","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15789347","title":"Stress-induced changes in the Schizosaccharomyces pombe proteome using two-dimensional difference gel electrophoresis, mass spectrometry and a novel integrated robotics platform.","citation":"Proteomics 2005 Apr;5(6):1669-85","abstract":"Robotic and manual methods have been used to obtain identification of significantly changing proteins regulated when Schizosaccharomyces pombe is exposed to oxidative stress. Differently treated S. pombe cells were lysed, labelled with CyDye and analysed by two-dimensional difference gel electrophoresis. Gel images analysed off-line, using the DeCyder image analysis software [GE Healthcare, Amersham, UK] allowed selection of significantly regulated proteins. Proteins displaying differential expression were excised robotically for manual digestion and identified by matrix-assisted laser desorption/ionisation - mass spectrometry (MALDI-MS). Additionally the same set of proteins displaying differential expression were automatically cut and digested using a prototype robotic platform. Automated MALDI-MS, peak label assignment and database searching were utilised to identify as many proteins as possible. The results achieved by the robotic system were compared to manual methods. The identification of all significantly altered proteins provides an annotated peroxide stress-related proteome that can be used as a base resource against which other stress-induced proteomic changes can be compared.","authors":"Weeks ME, Sinclair J, Jacob RJ, Saxton MJ, Kirby S, Jones J, Waterfield MD, Cramer R, Timms JF","authors_abbrev":"Weeks ME et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-03-25","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2997624","title":"Fission yeast Schizosaccharomyces pombe correctly excises a mammalian RNA transcript intervening sequence.","citation":"Nature 1985 Nov 7;318(6041):78-80","abstract":"Study of heterologous gene expression in the budding yeast Saccharomyces cerevisiae has shown that this organism is incapable of correctly removing intervening sequences from transcripts of higher eukaryotic genes. This is probably due to the stringent requirement for the presence of a TACTAAC box close to the 3' end of the intervening sequence if splicing in S. cerevisiae is to occur. Comparison of the introns found in the fission yeast Schizosaccharomyces pombe has identified conserved sequences similar to those found in higher eukaryotes. Therefore, we have investigated whether Schiz. pombe is capable of accurately excising intervening sequences from the transcripts of higher eukarotic genes. We show here that both the 5' and 3' splice sites of the simian virus 40 (SV40) small-T antigen transcript are accurately utilized when cloned viral DNA is expressed in Schiz. pombe cells. These data suggest that Schiz. pombe may be a better model system than S. cerevisiae for the genetic study of RNA splicing and for expressing higher eukaryotic genes.","authors":"Käufer NF, Simanis V, Nurse P","authors_abbrev":"Käufer NF et al.","pubmed_publication_date":"7 Nov 1985","pubmed_entrez_date":"1985-11-07","publication_year":"1985","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17533155","title":"Properties of actin from the fission yeast Schizosaccharomyces pombe and interaction with fission yeast profilin.","citation":"J Biol Chem 2007 Jul 27;282(30):21683-94","abstract":"The fission yeast Schizosaccharomyces pombe serves as a model system for studying role of actin cytoskeleton, since it has simple actin cytoskeletons and is genetically tractable. In contrast, biochemical approaches using this organism are still developing; fission yeast actin has so far not been isolated in its native form and characterized, and therefore, biochemical assays of fission yeast actin-binding proteins (ABPs) or myosin have been performed using rabbit skeletal muscle actin that may interact with the fission yeast ABPs in a manner different from fission yeast actin. Here, we report a novel method for isolating functionally active actin from fission yeast cells. The highly purified fission yeast actin polymerized with kinetics somewhat different from those of muscle actin and forms filaments that are structurally indistinguishable from skeletal muscle actin filaments. The fission yeast actin was a significantly weaker activator of Mg(2+)-ATPase of HMM of skeletal muscle myosin than muscle actin. The fission yeast profilin Cdc3 suppressed polymerization of fission yeast actin more effectively than that of muscle actin and showed an affinity for fission yeast actin higher than for muscle actin. The establishment of purification of fission yeast actin will enable reconstruction of physiologically relevant interactions between the actin and fission yeast ABPs or myosins and contribute to clarification of function of actin cytoskeleton in various cellular activities.","authors":"Takaine M, Mabuchi I","authors_abbrev":"Takaine M et al.","pubmed_publication_date":"27 Jul 2007","pubmed_entrez_date":"2007-05-30","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38578833","title":"Protocol for studying topological DNA interactions by purified fission yeast condensin.","citation":"STAR Protoc 2024 Apr 03;5(2):102995","abstract":"To understand the transition from interphase chromatin into well-shaped chromosomes during cell divisions, we need to understand the biochemical activities of the contributing proteins. Here, we present a protocol to investigate how the ring-shaped condensin complex sequentially and topologically entraps two DNA substrates. We describe the steps to prepare purified Schizosaccharomyces pombe condensin, as well as bulk biochemical assays to monitor the first and second DNA capture reactions. This protocol may facilitate further investigations of these essential genome organizers. For complete details on the use and execution of this protocol, please refer to Tang et al. 1 .","doi":"10.1016/j.xpro.2024.102995","authors":"Tang M, Uhlmann F","authors_abbrev":"Tang M et al.","pubmed_publication_date":"03 Apr 2024","pubmed_entrez_date":"2024-04-05","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-04-05 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8846783","title":"Fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating.","citation":"EMBO J 1995 Dec 01;14(23):5908-19","abstract":"A STE20/p65pak homolog was isolated from fission yeast by PCR. The pak1+ gene encodes a 72 kDa protein containing a putative p21-binding domain near its amino-terminus and a serine/threonine kinase domain near its carboxyl-terminus. The Pak1 protein autophosphorylates on serine residues and preferentially binds to activated Cdc42p both in vitro and in vivo. This binding is mediated through the p21 binding domain on Pak1p and the effector domain on Cdc42p. Overexpression of an inactive mutant form of pak1 gives rise to cells with markedly abnormal shape with mislocalized actin staining. Pak1 overexpression does not, however, suppress lethality associated with cdc42-null cells or the morphologic defeat caused by overexpression of mutant cdc42 alleles. Gene disruption of pak1+ establishes that, like cdc42+, pak1+ function is required for cell viability. In budding yeast, pak1+ expression restores mating function to STE20-null cells and, in fission yeast, overexpression of an inactive form of Pak inhibits mating. These results indicate that the Pak1 protein is likely to be an effector for Cdc42p or a related GTPase, and suggest that Pak1p is involved in the maintenance of cell polarity and in mating.","authors":"Ottilie S, Miller PJ, Johnson DI, Creasy CL, Sells MA, Bagrodia S, Forsburg SL, Chernoff J","authors_abbrev":"Ottilie S et al.","pubmed_publication_date":"01 Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"5bd05902488c7543","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-31 14:49:03","canto_approved_date":"2022-01-01 17:41:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-30 15:29:44","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.02c","SPBC1604.14c","SPAC17H9.09c","SPBC32C12.02","SPAC110.03"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2017-07-31"},{"uniquename":"PMID:19664060","title":"Inactivating pentapeptide insertions in the fission yeast replication factor C subunit Rfc2 cluster near the ATP-binding site and arginine finger motif.","citation":"FEBS J 2009 Sep;276(17):4803-13","abstract":"Replication factor C (RFC) plays a key role in eukaryotic chromosome replication by acting as a loading factor for the essential sliding clamp and polymerase processivity factor, proliferating cell nuclear antigen (PCNA). RFC is a pentamer comprising a large subunit, Rfc1, and four small subunits, Rfc2-Rfc5. Each RFC subunit is a member of the AAA+ family of ATPase and ATPase-like proteins, and the loading of PCNA onto double-stranded DNA is an ATP-dependent process. Here, we describe the properties of a collection of 38 mutant forms of the Rfc2 protein generated by pentapeptide-scanning mutagenesis of the fission yeast rfc2 gene. Each insertion was tested for its ability to support growth in fission yeast rfc2Delta cells lacking endogenous Rfc2 protein and the location of each insertion was mapped onto the 3D structure of budding yeast Rfc2. This analysis revealed that the majority of the inactivating mutations mapped in or adjacent to ATP sites C and D in Rfc2 (arginine finger and P-loop, respectively) or to the five-stranded beta sheet at the heart of the Rfc2 protein. By contrast, nonlethal mutations map predominantly to loop regions or to the outer surface of the RFC complex, often in highly conserved regions of the protein. Possible explanations for the effects of the various insertions are discussed.","doi":"10.1111/j.1742-4658.2009.07181.x","authors":"Gray FC, Whitehead KA, MacNeill SA","authors_abbrev":"Gray FC et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-08-12","publication_year":"2009","canto_session_key":"f6a8cf21f01fa04c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2016-02-24 16:37:10","canto_approved_date":"2022-02-24 07:58:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-02-23 11:04:58","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":90,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_19664060_phaf.tsv"}],"genes":["SPAC23D3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-02-24"},{"uniquename":"PMID:28572211","title":"Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) Technology in Fission Yeast.","citation":"Cold Spring Harb Protoc 2017 Jun 01;2017(6):pdb.top079814","abstract":"Shotgun proteomics combined with stable isotope labeling by amino acids in cell culture (SILAC) is a powerful approach to quantify proteins and posttranslational modifications across the entire proteome. SILAC technology in  Schizosaccharomyces pombe  must cope with the \"arginine conversion problem,\" in which isotope-labeled arginine is converted to other amino acids. This can be circumvented by either using stable isotope-marked lysine only (as opposed to the more standard lysine/arginine double labeling) or using yeast genetics to create strains that only very inefficiently convert arginine. Both strategies have been used successfully in large-scale (phospho)proteomics projects in  S. pombe  Here we introduce methods for performing a typical SILAC-based experiment in fission yeast, including generation of SILAC-compatible strains, sample preparation, and measurement by mass spectrometry.","doi":"10.1101/pdb.top079814","authors":"Maček B, Carpy A, Koch A, Bicho CC, Borek WE, Hauf S, Sawin KE","authors_abbrev":"Maček B et al.","pubmed_publication_date":"01 Jun 2017","pubmed_entrez_date":"2017-06-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-06-04 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31065745","title":"TASks for subtelomeres: when nucleosome loss and genome instability are favored.","citation":"Curr Genet 2019 Oct;65(5):1153-1160","abstract":"Chromosome ends are protected from erosion and chromosomal fusions through telomeric repeats and the telomere-binding protein complex shelterin. Imperfect repetitive sequences, known as telomere-associated sequences (TAS), flank the telomeres, yet their function is not well understood. In this perspective, we discuss our recent findings demonstrating that the TAS, in Schizosaccharomyces pombe, are organized into a distinct chromatin domain that is marked by low nucleosome levels and is highly recombinogenic (van Emden et al. in EMBO Rep 20:e47181. https://doi.org/10.15252/embr.201847181 , 2019). Low nucleosome abundance at the TAS is independent of the chromosomal position, but is an intrinsic property of the DNA sequence itself. Critical nucleosome levels are maintained through two heterochromatin complexes recruited by the shelterin subunit Ccq1, which together control gene repression and nucleosome stability. Furthermore, Ccq1 inhibits TAS-facilitated recombination between subtelomeres, yet independently of nucleosome stability. In conclusion, the TAS present a unique chromatin environment causing nucleosome loss and genome instability, which are both counteracted by Ccq1 through independent mechanisms. Given the antagonistic behavior, we hypothesize that Ccq1 co-evolved with the appearance of TAS to regulate nucleosome dynamics and recombination-based telomere maintenance in the absence of telomerase.","doi":"10.1007/s00294-019-00986-8","authors":"van Emden TS, Braun S","authors_abbrev":"van Emden TS et al.","pubmed_publication_date":"Oct 2019","pubmed_entrez_date":"2019-05-09","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15537393","title":"A microbial TRP-like polycystic-kidney-disease-related ion channel gene.","citation":"Biochem J 2005 Apr 01;387(Pt 1):211-9","abstract":"Ion channel genes have been discovered in many microbial organisms. We have investigated a microbial TRP (transient receptor potential) ion channel gene which has most similarity to polycystic-kidney-disease-related ion channel genes. We have shown that this gene (pkd2) is essential for cellular viability, and is involved in cell growth and cell wall synthesis. Expression of this gene increases following damage to the cell wall. This fission yeast pkd2 gene, orthologues of which are found in all eukaryotic cells, appears to be a key signalling component in the regulation of cell shape and cell wall synthesis in yeast through an interaction with a Rho1-GTPase. A model for the mode of action of this Schizosaccharomyces pombe protein in a Ca2+ signalling pathway is hypothesized.","authors":"Palmer CP, Aydar E, Djamgoz MB","authors_abbrev":"Palmer CP et al.","pubmed_publication_date":"01 Apr 2005","pubmed_entrez_date":"2004-11-13","publication_year":"2005","canto_session_key":"6f48f05c223d7948","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-13 07:16:12","canto_approved_date":"2024-03-25 15:33:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-06 06:11:43","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.03","SPAC1F7.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-07-13"},{"uniquename":"PMID:31511300","title":"Diverse DNA Sequence Motifs Activate Meiotic Recombination Hotspots Through a Common Chromatin Remodeling Pathway.","citation":"Genetics 2019 Nov;213(3):789-803","abstract":"In meiosis, multiple different DNA sequence motifs help to position homologous recombination at hotspots in the genome. How do the seemingly disparate  cis -acting regulatory modules each promote locally the activity of the basal recombination machinery? We defined molecular mechanisms of action for five different hotspot-activating DNA motifs ( M26 ,  CCAAT ,  Oligo-C ,  4095 ,  4156 ) located independently at the same site within the  ade6  locus of the fission yeast  Schizosaccharomyces pombe  Each motif promoted meiotic recombination ( i.e. , is active) within this context, and this activity required the respective binding proteins (transcription factors Atf1, Pcr1, Php2, Php3, Php5, Rst2). High-resolution analyses of chromatin structure by nucleosome scanning assays revealed that each motif triggers the displacement of nucleosomes surrounding the hotspot motif in meiosis. This chromatin remodeling required the respective sequence-specific binding proteins, was constitutive for two motifs, and was enhanced meiotically for three others. Hotspot activity of each motif strongly required the ATP-dependent chromatin remodeling enzyme Snf22 (Snf2/Swi2), with lesser dependence on Gcn5, Mst2, and Hrp3. These findings support a model in which most meiotic recombination hotspots are positioned by the binding of transcription factors to their respective DNA sites. The functional redundancy of multiple, sequence-specific protein-DNA complexes converges upon shared chromatin remodeling pathways that help provide the basal recombination machinery (Spo11/Rec12 complex) access to its DNA substrates within chromatin.","doi":"10.1534/genetics.119.302679","authors":"Mukiza TO, Protacio RU, Davidson MK, Steiner WW, Wahls WP","authors_abbrev":"Mukiza TO et al.","pubmed_publication_date":"Nov 2019","pubmed_entrez_date":"2019-09-13","publication_year":"2019","canto_session_key":"f621d80f3fce5599","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-09-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21815629","title":"Schizosaccharomyces pombe protection of telomeres 1 utilizes alternate binding modes to accommodate different telomeric sequences.","citation":"Biochemistry 2011 Sep 06;50(35):7503-13","abstract":"The ends of eukaryotic chromosomes consist of long tracts of repetitive GT-rich DNA with variable sequence homogeneity between and within organisms. Telomeres terminate in a conserved 3'-ssDNA overhang that, regardless of sequence variability, is specifically and tightly bound by proteins of the telomere-end protection family. The high affinity ssDNA-binding activity of S. pombe Pot1 protein (SpPot1) is conferred by a DNA-binding domain consisting of two subdomains, Pot1pN and Pot1pC. Previous work has shown that Pot1pN binds a single repeat of the core telomere sequence (GGTTAC) with exquisite specificity, while Pot1pC binds an extended sequence of nine nucleotides (GGTTACGGT) with modest specificity requirements. We find that full-length SpPot1 binds the composite 15mer, (GGTTAC)(2)GGT, and a shorter two-repeat 12mer, (GGTTAC)(2), with equally high affinity (<3 pM), but with substantially different kinetic and thermodynamic properties. The binding mode of the SpPot1/15mer complex is more stable than that of the 12mer complex, with a 2-fold longer half-life and increased tolerance to nucleotide and amino acid substitutions. Our data suggest that SpPot1 protection of heterogeneous telomeres is mediated through 5'-sequence recognition and the use of alternate binding modes to maintain high affinity interaction with the G-strand, while simultaneously discriminating against the complementary strand.","doi":"10.1021/bi200826a","authors":"Altschuler SE, Dickey TH, Wuttke DS","authors_abbrev":"Altschuler SE et al.","pubmed_publication_date":"06 Sep 2011","pubmed_entrez_date":"2011-08-06","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8654750","title":"Characterisation of Sxa2, a protease involved in pheromone communication in fission yeast.","citation":"Biochem Soc Trans 1995 Nov;23(4):565S","abstract":"","authors":"Ladds G, Rasmussen M, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Nov 1995","pubmed_entrez_date":"1995-11-01","publication_year":"1995","canto_session_key":"aeb3d0063f6b810","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-01-06 16:15:45","canto_approved_date":"2022-08-30 07:38:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-14 04:16:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.06","SPAC1296.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-01-06"},{"uniquename":"PMID:2112088","title":"The ryh1 gene in the fission yeast Schizosaccharomyces pombe encoding a GTP-binding protein related to ras, rho and ypt: structure, expression and identification of its human homologue.","citation":"EMBO J 1990 Jun;9(6):1949-55","abstract":"A gene, ryh1, of the fission yeast Schizosaccharomyces pombe encoding a GTP-binding protein of 201 amino acids and belonging to the ras superfamily was isolated using the protein-coding region of the cloned Saccharomyces cerevisiae YPT1 gene as hybridization probe. The ryh1 gene is interrupted by three introns. ryh1 null mutants are viable but unable to grow at temperatures greater than 35.5 degrees C. Invertase of ryh1- cells is properly secreted but has a faster electrophoretic mobility compared to that of wild-type cells. The temperature-sensitive phenotype of ryh1 null mutants is complemented by the human rab6 cDNA expressed either under transcriptional control of the S.pombe adh or the SV40 early promoter.","authors":"Hengst L, Lehmeier T, Gallwitz D","authors_abbrev":"Hengst L et al.","pubmed_publication_date":"Jun 1990","pubmed_entrez_date":"1990-06-01","publication_year":"1990","canto_session_key":"048d5ba6ff81d687","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-03-20 15:23:47","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-07 09:37:44","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4C5.02c","SPCC191.11"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2013-02-07"},{"uniquename":"EMBL:SPD275","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR12048","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.09c","YDR060W","SPAC589.03c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:15350898","title":"Cdk5 deregulation in the pathogenesis of Alzheimer's disease.","citation":"Trends Mol Med 2004 Sep;10(9):452-8","abstract":"","authors":"Cruz JC, Tsai LH","authors_abbrev":"Cruz JC et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-09-08","publication_year":"2004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16C4.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23973085","title":"Imaging individual spindle microtubule dynamics in fission yeast.","citation":"Methods Cell Biol 2013;115:385-94","abstract":"Microtubules exhibit dynamic instability, stochastically switching between infrequent phases of growth and shrinkage. In the cell, microtubule dynamic instability is further modulated by microtubule-associated proteins and motors, which are specifically tuned to cell cycle stages. For example, mitotic microtubules are more dynamic than interphase microtubules. The different parameters of microtubule dynamics can be measured from length versus time data, which are generally obtained from time-lapse acquisition using the optical microscope. The typical maximum resolution of the optical microscope is ~λ/2 or ~300 nm. This scale represents a challenge for imaging fission yeast microtubule dynamics specifically during early mitosis, where the bipolar mitotic spindle contains many short dynamic microtubules of ~1-μm scale. Here, we present a novel method to image short fission yeast mitotic microtubules. The method uses the thermosensitive reversible kinesin-5 cut7.24(ts) to create monopolar spindles, where asters of individual mitotic microtubules are presented for imaging and subsequent analysis.","doi":"10.1016/B978-0-12-407757-7.00024-4","authors":"Costa J, Fu C, Syrovatkina V, Tran PT","authors_abbrev":"Costa J et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-08-27","publication_year":"2013","canto_session_key":"e089b44b0b7e4467","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-12 13:16:14","canto_approved_date":"2022-11-08 17:51:41","canto_session_submitted_date":"2016-10-12 13:16:08","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-12"},{"uniquename":"PMID:16254446","title":"Heterologous aquaporin (AQY2-1) expression strongly enhances freeze tolerance of Schizosaccharomyces pombe.","citation":"J Mol Microbiol Biotechnol 2005;9(1):52-6","abstract":"Aquaporin membrane proteins enable the transport of water across membranes in various organisms. In yeast their expression has been shown to correlate strongly with freeze tolerance. When we analyzed the freeze tolerance of Schizosaccharomyces pombe, an organism whose genome sequence has revealed no genes encoding a bona fide water channel, we found very low intrinsic freeze tolerance compared to other yeast species with aquaporin-encoding genes. Deletion of Spac977.17, which encodes a putative glycerol facilitator, resulted in no significant differences in freeze tolerance with its corresponding wild-type strain in all growth conditions tested. However, when we expressed the Saccharomyces cerevisiae aquaporin-encoding gene AQY2-1 in S. pombe cells, we found that the relatively low freeze tolerance of S. pombe could be significantly enhanced. Therefore, (i) the absence of a bona fide water channel in S. pombe might provide in part an explanation for its overall low freeze tolerance compared to other yeast species, and (ii) aquaporin overexpression might be a tool to improve cryopreservation of many other cell types as well, as has recently been shown for mouse oocytes and fish embryos.","authors":"Tanghe A, Kayingo G, Prior BA, Thevelein JM, Van Dijck P","authors_abbrev":"Tanghe A et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-10-29","publication_year":"2005","canto_session_key":"790a2d91cbd56490","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-09-02 06:26:25","canto_approved_date":"2025-09-02 06:26:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-09-01 17:25:55","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-09-02"},{"uniquename":"PMID:36093997","title":"The number of cytokinesis nodes in mitotic fission yeast scales with cell size.","citation":"Elife 2022 Sep 12;11","abstract":"Cytokinesis nodes are assemblies of stoichiometric ratios of proteins associated with the plasma membrane, which serve as precursors for the contractile ring during cytokinesis by fission yeast. The total number of nodes is uncertain, because of the limitations of the methods used previously. Here, we used the ~140 nm resolution of Airyscan super-resolution microscopy to measure the fluorescence intensity of small, single cytokinesis nodes marked with Blt1-mEGFP in live fission yeast cells early in mitosis. The ratio of the total Blt1-mEGFP fluorescence in the broad band of cytokinesis nodes to the average fluorescence of a single node gives about 190 single cytokinesis nodes in wild-type fission yeast cells early in mitosis. Most, but not all of these nodes condense into a contractile ring. The number of cytokinesis nodes scales with cell size in four strains tested, although large diameter  rga4Δ  mutant cells form somewhat fewer cytokinesis nodes than expected from the overall trend. The Pom1 kinase restricts cytokinesis nodes from the ends of cells, but the surface density of Pom1 on the plasma membrane around the equators of cells is similar with a wide range of node numbers, so Pom1 does not control cytokinesis node number. However, when the concentrations of either kinase Pom1 or kinase Cdr2 were varied with the  nmt1  promoter, the numbers of cytokinesis nodes increased above a baseline of about ~190 with the total cellular concentration of either kinase.","doi":"10.7554/eLife.76249","authors":"Sayyad WA, Pollard TD","authors_abbrev":"Sayyad WA et al.","pubmed_publication_date":"12 Sep 2022","pubmed_entrez_date":"2022-09-12","publication_year":"2022","canto_session_key":"7c58c424d8c85184","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-15 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27837315","title":"Cloning and characterization of decaprenyl diphosphate synthase from three different fungi.","citation":"Appl Microbiol Biotechnol 2017 Feb;101(4):1559-1571","abstract":"Coenzyme Q (CoQ) is composed of a benzoquinone moiety and an isoprenoid side chain of varying lengths. The length of the side chain is controlled by polyprenyl diphosphate synthase. In this study, dps1 genes encoding decaprenyl diphosphate synthase were cloned from three fungi: Bulleromyces albus, Saitoella complicata, and Rhodotorula minuta. The predicted Dps1 proteins contained seven conserved domains found in typical polyprenyl diphosphate synthases and were 528, 440, and 537 amino acids in length in B. albus, S. complicata, and R. minuta, respectively. Escherichia coli expressing the fungal dps1 genes produced CoQ 10  in addition to endogenous CoQ 8 . Two of the three fungal dps1 genes (from S. complicata and R. minuta) were able to replace the function of ispB in an E. coli mutant strain. In vitro enzymatic activities were also detected in recombinant strains. The three dps1 genes were able to complement a Schizosaccharomyces pombe dps1, dlp1 double mutant. Recombinant S. pombe produced mainly CoQ 10 , indicating that the introduced genes were independently functional and did not require dlp1. The cloning of dps1 genes from various fungi has the potential to enhance production of CoQ 10  in other organisms.","doi":"10.1007/s00253-016-7963-0","authors":"Moriyama D, Kaino T, Yajima K, Yanai R, Ikenaka Y, Hasegawa J, Washida M, Nanba H, Kawamukai M","authors_abbrev":"Moriyama D et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-11-13","publication_year":"2017","canto_session_key":"ec78aec4d193db1f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-11-16 14:42:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-11-16 14:42:22","canto_added_date":"2016-11-13 01:15:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.01","SPAC19G12.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-11-16"},{"uniquename":"PMID:11864908","title":"Pcp1p, an Spc110p-related calmodulin target at the centrosome of the fission yeast Schizosaccharomyces pombe.","citation":"Cell Growth Differ 2002 Feb;13(2):47-58","abstract":"In the budding yeast Saccharomyces cerevisiae, the calmodulin-binding protein Spc110p/Nuf1p facilitates mitotic spindle formation from the fungal centrosome or spindle pole body (SPB). The human Spc110p orthologue kendrin is a centrosomal, calmodulin-binding pericentrin isoform that is specifically overexpressed in carcinoma cells. Here we establish an evolutionary and functional link between Spc110p and kendrin through identification and analysis of similar calmodulin-binding proteins in the fission yeast Schizosaccharomyces pombe (Pcp1p, pole target of calmodulin in S. pombe) and the filamentous fungus Aspergillus nidulans. Like Spc110p and kendrin, Pcp1p and the A. nidulans protein contain predicted coiled-coil secondary structure and a COOH-terminal calmodulin-binding region. Green fluorescent protein fusions of Pcp1p localize to the SPB as analyzed by fluorescence and immunoelectron microscopy. Pcp1p overexpression causes chromosome missegregation, multiple mitotic spindle fragments, and multiple abnormal SPB-like structures, a phenotype remarkably similar to that of many human carcinoma lines, which exhibit chromosome and spindle defects, and supernumerary centrosomes.","authors":"Flory MR, Morphew M, Joseph JD, Means AR, Davis TN","authors_abbrev":"Flory MR et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-02-28","publication_year":"2002","canto_session_key":"c818973c0d0b2e39","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-21 14:33:04","canto_approved_date":"2020-02-20 21:19:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-16 11:57:58","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.06c","SPAC3A12.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-21"},{"uniquename":"PMID:26438724","title":"H3K9 methylation extends across natural boundaries of heterochromatin in the absence of an HP1 protein.","citation":"EMBO J 2015 Nov 12;34(22):2789-803","abstract":"Proteins of the conserved HP1 family are elementary components of heterochromatin and are generally assumed to play a central role in the creation of a rigid, densely packed heterochromatic network that is inaccessible to the transcription machinery. Here, we demonstrate that the fission yeast HP1 protein Swi6 exists as a single highly dynamic population that rapidly exchanges in cis and in trans between different heterochromatic regions. Binding to methylated H3K9 or to heterochromatic RNA decelerates Swi6 mobility. We further show that Swi6 is largely dispensable to the maintenance of heterochromatin domains. In the absence of Swi6, H3K9 methylation levels are maintained by a mechanism that depends on polymeric self-association properties of Tas3, a subunit of the RNA-induced transcriptional silencing complex. Our results disclose a surprising role for Swi6 dimerization in demarcating constitutive heterochromatin from neighboring euchromatin. Thus, rather than promoting maintenance and spreading of heterochromatin, Swi6 appears to limit these processes and appropriately confine heterochromatin.","doi":"10.15252/embj.201591320","authors":"Stunnenberg R, Kulasegaran-Shylini R, Keller C, Kirschmann MA, Gelman L, Bühler M","authors_abbrev":"Stunnenberg R et al.","pubmed_publication_date":"12 Nov 2015","pubmed_entrez_date":"2015-10-07","publication_year":"2015","canto_session_key":"190f5f719398b3d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Marc Buehler","canto_first_approved_date":"2018-02-13 11:26:24","canto_approved_date":"2025-09-03 16:16:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-01 13:19:46","canto_added_date":"2015-10-08 00:19:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Marc Buehler","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP4C9.02","SPBC16C6.10","SPBCPT2R1.08c","SPAC1556.01c","SPAC212.11","SPAC12G12.13c","SPAC664.01c","SPBC83.03c"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2018-02-13"},{"uniquename":"PMID:20708089","title":"Mechanisms controlling division-plane positioning.","citation":"Semin Cell Dev Biol 2010 Dec;21(9):874-80","abstract":"A critical and irreversible step in the cell division cycle is cytokinesis which physically separates the two daughter cells. This event is consequently subject to tight spatial and temporal regulation. This review focuses on the spatial regulatory mechanisms controlling the position of the division plane. Studies performed in prokaryotic and eukaryotic systems have revealed that various signal-emitting spatial cues - mitotic spindle, nucleus, nucleoid or cell tips - can favour or inhibit the assembly of the cytokinetic apparatus in their vicinity. Most often, several mechanisms operate in parallel to integrate spatial information and promote faithful genome segregation as well as proper cytoplasmic division. We primarily describe the spatial regulatory mechanisms operating in the fission yeast model system, where a detailed molecular understanding of cytokinesis has been achieved. In this system, spatial regulations target a major factor controlling the position of the division plane, the anillin-like protein Mid1. These mechanisms are then compared to spatial regulatory mechanisms prevailing in animal cells and rod-shaped bacteria.","doi":"10.1016/j.semcdb.2010.08.006","authors":"Almonacid M, Paoletti A","authors_abbrev":"Almonacid M et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-08-17","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15642092","title":"Global expression changes resulting from loss of telomeric DNA in fission yeast.","citation":"Genome Biol 2005;6(1):R1","abstract":"Schizosaccharomyces pombe cells lacking the catalytic subunit of telomerase (encoded by trt1+) lose telomeric DNA and enter crisis, but rare survivors arise with either circular or linear chromosomes. Survivors with linear chromosomes have normal growth rates and morphology, but those with circular chromosomes have growth defects and are enlarged. We report the global gene-expression response of S. pombe to loss of trt1+.\nSurvivors with linear chromosomes had expression profiles similar to cells with native telomeres, whereas survivors with circular chromosomes showed continued upregulation of core environmental stress response (CESR) genes. In addition, survivors with circular chromosomes had altered expression of 51 genes compared to survivors with linear chromosomes, providing an expression signature. S. pombe progressing through crisis displayed two waves of altered gene expression. One coincided with crisis and consisted of around 110 genes, 44% of which overlapped with the CESR. The second was synchronized with the emergence of survivors and consisted of a single class of open reading frames (ORFs) with homology both to RecQ helicases and to dh repeats at centromeres targeted for heterochromatin formation via an RNA interference (RNAi) mechanism. Accumulation of transcript from the ORF was found not only in trt1- cells, but also in dcr1- and ago1- RNAi mutants, suggesting that RNAi may control its expression.\nThese results demonstrate a correlation between a state of cellular stress, short telomeres and growth defects in cells with circular chromosomes. A putative new RecQ helicase was expressed as survivors emerged and appears to be transcriptionally regulated by RNAi, suggesting that this mechanism operates at telomeres.","authors":"Mandell JG, Bähler J, Volpe TA, Martienssen RA, Cech TR","authors_abbrev":"Mandell JG et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-01-12","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10376874","title":"C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids.","citation":"RNA 1999 Jun;5(6):739-50","abstract":"Translation termination in eukaryotes requires a stop codon-responsive (class-I) release factor, eRF1, and a guanine nucleotide-responsive (class-II) release factor, eRF3. Schizosaccharomyces pombe eRF3 has an N-terminal polypeptide similar in size to the prion-like domain of Saccharomyces cerevisiae eRF3 in addition to the EF-1alpha-like catalytic domain. By in vivo two-hybrid assay as well as by an in vitro pull-down analysis using purified proteins of S. pombe as well as of S. cerevisiae, eRF1 bound to the C-terminal one-third domain of eRF3, named eRF3C, but not to the N-terminal two-thirds, which was inconsistent with the previous report by Paushkin et al. (1997, Mol Cell Biol 17:2798-2805). The activity of S. pombe eRF3 in eRF1 binding was affected by Ala substitutions for the C-terminal residues conserved not only in eRF3s but also in elongation factors EF-Tu and EF-1alpha. These single mutational defects in the eRF1-eRF3 interaction became evident when either truncated protein eRF3C or C-terminally altered eRF1 proteins were used for the authentic protein, providing further support for the presence of a C-terminal interaction. Given that eRF3 is an EF-Tu/EF-1alpha homolog required for translation termination, the apparent dispensability of the N-terminal domain of eRF3 for binding to eRF1 is in contrast to importance, direct or indirect, in EF-Tu/EF-1alpha for binding to aminoacyl-tRNA, although both eRF3 and EF-Tu/EF-1alpha share some common amino acids for binding to eRF1 and aminoacyl-tRNA, respectively. These differences probably reflect the independence of eRF1 binding in relation to the G-domain function of eRF3 (i.e., probably uncoupled with GTP hydrolysis), whereas aminoacyl-tRNA binding depends on that of EF-Tu/EF-1alpha(i.e., coupled with GTP hydrolysis), which sheds some light on the mechanism of eRF3 function.","authors":"Ebihara K, Nakamura Y","authors_abbrev":"Ebihara K et al.","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-06-22","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC584.04","SPCC18B5.06"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:25948336","title":"Nile red fluorescence screening facilitating neutral lipid phenotype determination in budding yeast, Saccharomyces cerevisiae, and the fission yeast Schizosaccharomyces pombe.","citation":"Antonie Van Leeuwenhoek 2015 Jul;108(1):97-106","abstract":"Investigation of yeast neutral lipid accumulation is important for biotechnology and also for modelling aberrant lipid metabolism in human disease. The Nile red (NR) method has been extensively utilised to determine lipid phenotypes of yeast cells via microscopic means. NR assays have been used to differentiate lipid accumulation and relative amounts of lipid in oleaginous species but have not been thoroughly validated for phenotype determination arising from genetic modification. A modified NR assay, first described by Sitepu et al. (J Microbiol Methods 91:321-328, 2012), was able to detect neutral lipid changes in Saccharomyces cerevisiae deletion mutants with sensitivity similar to more advanced methodology. We have also be able to, for the first time, successfully apply the NR assay to the well characterised fission yeast Schizosaccharomyces pombe, an increasingly important organism in biotechnology. The described NR fluorescence assay is suitable for increased throughput and rapid screening of genetically modified strains in both the biotechnology industry and for modelling ectopic lipid production for a variety of human diseases. This ultimately negates the need for labour intensive and time consuming lipid analyses of samples that may not yield a desirable lipid phenotype, whilst genetic modifications impacting significantly on the cellular lipid phenotype can be further promoted for more in depth analyses.","doi":"10.1007/s10482-015-0467-6","authors":"Rostron KA, Rolph CE, Lawrence CL","authors_abbrev":"Rostron KA et al.","pubmed_publication_date":"Jul 2015","pubmed_entrez_date":"2015-05-08","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-05-09 00:19:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7025348","title":"Metabolic activation and mutagenicity of 4 vinylic monomers (vinyl chloride, styrene, acrylonitrile, butadiene).","citation":"Toxicol Eur Res 1981 May;3(3):131-40","abstract":"The mutagenic activity and the metabolism of four vinylic monomers; vinyl chloride, styrene, acrylonitrile and butadiene are reviewed. Those chemicals are converted by the mixed function oxidases system of the endoplasmic reticulum into reactive intermediates which can interact with macromolecules within the cell. In order to examine the mutagenic activity of these compounds and their metabolites, different mutagenicity testing systems have been used: tests with S. typhimurium, E. coli, Schizosaccharomyces pombe, Saccharomyces cerevisiae, V79 Chinese Hamster cells, CHO cells, Drosophila melanogaster as well as evaluations of chromosome aberrations.","authors":"Duverger M, Lambotte M, Malvoisin E, de Meester C, Poncelet F, Mercier M","authors_abbrev":"Duverger M et al.","pubmed_publication_date":"May 1981","pubmed_entrez_date":"1981-05-01","publication_year":"1981","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12595258","title":"Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold.","citation":"J Mol Biol 2003 Mar 07;326(5):1463-73","abstract":"The essential redox cofactors riboflavin monophosphate (FMN) and flavin adenine dinucleotide (FAD) are synthesised from their precursor, riboflavin, in sequential reactions by the metal-dependent riboflavin kinase and FAD synthetase. Here, we describe the 1.6A crystal structure of the Schizosaccharomyces pombe riboflavin kinase. The enzyme represents a novel family of phosphoryl transferring enzymes. It is a monomer comprising a central beta-barrel clasped on one side by two C-terminal helices that display an L-like shape. The opposite side of the beta-barrel serves as a platform for substrate binding as demonstrated by complexes with ADP and FMN. Formation of the ATP-binding site requires significant rearrangements in a short alpha-helix as compared to the substrate free form. The diphosphate moiety of ADP is covered by the glycine-rich flap I formed from parts of this alpha-helix. In contrast, no significant changes are observed upon binding of riboflavin. The ribityl side-chain might be covered by a rather flexible flap II. The unusual metal-binding site involves, in addition to the ADP phosphates, only the strictly conserved Thr45. This may explain the preference for zinc observed in vitro.","authors":"Bauer S, Kemter K, Bacher A, Huber R, Fischer M, Steinbacher S","authors_abbrev":"Bauer S et al.","pubmed_publication_date":"07 Mar 2003","pubmed_entrez_date":"2003-02-22","publication_year":"2003","canto_session_key":"aa109284eb32f450","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-19 09:16:24","canto_approved_date":"2025-03-06 17:00:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-11 12:13:09","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18.16c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-04-19","pdb_entries":[{"pdb_id":"1n08","gene_chains":[{"gene_uniquename":"SPCC18.16c","chain":"A/B","position":"1-163"}],"title":"Crystal Structure of Schizosaccharomyces pombe Riboflavin Kinase Reveals a Novel ATP and Riboflavin Binding Fold","entry_authors":"Bauer S,Kemter K,Bacher A,Huber R,Fischer M,Steinbacher S","entry_authors_abbrev":"Bauer S et al.","reference_uniquename":"PMID:12595258","experimental_method":"X-ray","resolution":"1.6"},{"pdb_id":"1n07","gene_chains":[{"gene_uniquename":"SPCC18.16c","chain":"A/B","position":"1-163"}],"title":"Crystal Structure of Schizosaccharomyces pombe Riboflavin Kinase Reveals a Novel ATP and Riboflavin Binding Fold","entry_authors":"Bauer S,Kemter K,Bacher A,Huber R,Fischer M,Steinbacher S","entry_authors_abbrev":"Bauer S et al.","reference_uniquename":"PMID:12595258","experimental_method":"X-ray","resolution":"2.45"},{"pdb_id":"1n06","gene_chains":[{"gene_uniquename":"SPCC18.16c","chain":"A/B","position":"1-163"}],"title":"Crystal Structure of Schizosaccharomyces pombe Riboflavin Kinase Reveals a Novel ATP and Riboflavin Binding Fold","entry_authors":"Bauer S,Kemter K,Bacher A,Huber R,Fischer M,Steinbacher S","entry_authors_abbrev":"Bauer S et al.","reference_uniquename":"PMID:12595258","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"1n05","gene_chains":[{"gene_uniquename":"SPCC18.16c","chain":"A","position":"1-163"}],"title":"Crystal Structure of Schizosaccharomyces pombe Riboflavin Kinase Reveals a Novel ATP and Riboflavin Binding Fold","entry_authors":"Bauer S,Kemter K,Bacher A,Huber R,Fischer M,Steinbacher S","entry_authors_abbrev":"Bauer S et al.","reference_uniquename":"PMID:12595258","experimental_method":"X-ray","resolution":"2.1"}]},{"uniquename":"PMID:22906049","title":"Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation.","citation":"Biochem J 2012 Nov 15;448(1):55-65","abstract":"The ubiquitin-proteasome system targets selected proteins for degradation by the 26S proteasome. Rpn12 is an essential component of the 19S regulatory particle and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. In the present paper we report the crystal structure of Rpn12, a proteasomal PCI-domain-containing protein. The structure helps to define a core structural motif for the PCI domain and identifies potential sites through which Rpn12 might form protein-protein interactions. We demonstrate that mutating residues at one of these sites impairs Rpn12 binding to Rpn10 in vitro and reduces Rpn10 incorporation into proteasomes in vivo.","doi":"10.1042/BJ20120542","authors":"Boehringer J, Riedinger C, Paraskevopoulos K, Johnson EO, Lowe ED, Khoudian C, Smith D, Noble ME, Gordon C, Endicott JA","authors_abbrev":"Boehringer J et al.","pubmed_publication_date":"15 Nov 2012","pubmed_entrez_date":"2012-08-22","publication_year":"2012","canto_session_key":"4036971a62022f41","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-09-09 13:57:13","canto_approved_date":"2022-02-01 18:06:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-05 18:46:22","canto_added_date":"2013-06-16 07:56:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16G5.01","SPAC637.10c","SPBP19A11.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-09-09","pdb_entries":[{"pdb_id":"4b0z","gene_chains":[{"gene_uniquename":"SPBC16G5.01","chain":"A/B","position":"1-224"}],"title":"Crystal structure of S. pombe Rpn12","entry_authors":"Boehringer J,Riedinger C,Paraskevopoulos K,Johnson EOD,Lowe ED,Khoudian C,Smith D,Noble MEM,Gordon C,Endicott JA","entry_authors_abbrev":"Boehringer J et al.","reference_uniquename":"PMID:22906049","experimental_method":"X-ray","resolution":"1.585"}]},{"uniquename":"PMID:40594858","title":"Dbl2 interacts with helicases and an endonuclease to maintain the integrity of repetitive regions.","citation":"Sci Rep 2025 Jul 01;15(1):21895","abstract":"Helicases and endonucleases play crucial roles in genome maintenance by unwinding or cleaving various forms of DNA and RNA structures in order to facilitate essential biological processes, such as DNA replication and recombination. Here, we identified fission yeast Dbl2 as a potential interactor of several complexes that exhibit either helicase or endonuclease activity, namely Fml1-MHF, SCF Fbh1 , Rqh1-Top3-Rmi1, and Mus81-Eme1. In vitro, Dbl2 binds to DNA, with a preference for branched molecules, such as D-loops, mobile Holliday junctions, and fork structures, making it a good candidate to play a central role in modulating the activity of helicases and endonucleases during replication and recombination repair. Previously, we showed that Dbl2 recruits Fbh1 to the ongoing homologous recombination sites, affecting the Rad51-nucleofilament. In this study, we determined that deleting dbl2 in an fbh1Δ background did not increase sensitivity to DNA-damaging agents or the frequency of Tf2 ectopic recombination. Therefore, Dbl2 and Fbh1 might be involved in the same molecular pathway, maintaining genome integrity by hindering ectopic recombination at repetitive elements.","doi":"10.1038/s41598-025-08626-7","authors":"Bakosova A, Cipak L, Mayerova N, Krol K, Benko Z, Pitelova A, Kolesar P, Piatrova D, Smondrkova M, Maresova A, Molnarova L, Cipakova I, Altmannova V, Bellova J, Barath P, Prevorovsky M, Palecek J, Krejci L, Gregan J, Skoneczna A, Polakova SB","authors_abbrev":"Bakosova A et al.","pubmed_publication_date":"01 Jul 2025","pubmed_entrez_date":"2025-07-02","publication_year":"2025","canto_session_key":"acb14f9badaa793d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silvia Polakova","canto_first_approved_date":"2026-05-22 05:53:09","canto_approved_date":"2026-06-26 07:06:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-03-22 08:46:35","canto_added_date":"2025-07-02 23:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":67,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Silvia Polakova","community_curator":true,"annotation_count":24,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1393.12","SPBC336.01","SPBC409.05","SPAC9.05","SPAC2G11.12","SPAPB1E7.06c","SPCC553.01c","SPBC543.03c","SPBC660.13c","SPBC11B10.10c","SPCC622.08c","SPCC126.02c","SPAC1834.04","SPAC26A3.03c","SPBC1105.11c","SPBC14C8.02","SPBC2D10.16","SPAC30D11.10","SPAC8E11.02c","SPCC576.12c","SPAC644.14c","SPAC1834.03c","SPCC622.09","SPBC21D10.12","SPCC364.06","SPCC4G3.05c"],"gene_count":26,"ltp_gene_count":26,"approved_date":"2026-05-22"},{"uniquename":"PMID:20799962","title":"A genetic screen for replication initiation defective (rid) mutants in Schizosaccharomyces pombe.","citation":"Cell Div 2010 Aug 27;5:20","abstract":"In fission yeast the intra-S phase and DNA damage checkpoints are activated in response to inhibition of DNA replication or DNA damage, respectively. The intra-S phase checkpoint responds to stalled replication forks leading to the activation of the Cds1 kinase that both delays cell cycle progression and stabilizes DNA replication forks. The DNA damage checkpoint, that operates during the G2 phase of the cell cycle delays mitotic progression through activation of the checkpoint kinase, Chk1. Delay of the cell cycle is believed to be essential to allow time for either replication restart (in S phase) or DNA damage repair (in G2). Previously, our laboratory showed that fission yeast cells deleted for the N-terminal half of DNA polymerase ε (Cdc20) are delayed in S phase, but surprisingly require Chk1 rather than Cds1 to maintain cell viability. Several additional DNA replication mutants were then tested for their dependency on Chk1 or Cds1 when grown under semi-permissive temperatures. We discovered that mutants defective in DNA replication initiation are sensitive only to loss of Chk1, whilst mutations that inhibit DNA replication elongation are sensitive to loss of both Cds1 and Chk1. To confirm that the Chk1-sensitive, Cds1-insensitive phenotype (rid phenotype) is specific to mutants defective in DNA replication initiation, we completed a genetic screen for cell cycle mutants that require Chk1, but not Cds1 to maintain cell viability when grown at semi-permissive temperatures. Our screen identified two mutants, rid1-1 and rid2-1, that are defective in Orc1 and Mcm4, respectively. Both mutants show defects in DNA replication initiation consistent with our hypothesis that the rid phenotype is replication initiation specific. In the case of Mcm4, the mutation has been mapped to a highly conserved region of the protein that appears to be required for DNA replication initiation, but not elongation. Therefore, we conclude that the cellular response to inhibition of DNA replication initiation is distinct from blocking DNA replication elongation, and this difference can be exploited to identify mutants specifically defective in DNA replication initiation.","doi":"10.1186/1747-1028-5-20","authors":"Locovei AM, Yin L, D'Urso G","authors_abbrev":"Locovei AM et al.","pubmed_publication_date":"27 Aug 2010","pubmed_entrez_date":"2010-08-31","publication_year":"2010","canto_session_key":"07bc527001c082d8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-11-26 17:36:26","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-11-26 17:36:22","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC16A11.17","SPAC694.06c","SPBC29A10.15","SPCC1259.13"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-11-26"},{"uniquename":"PMID:29695507","title":"A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding.","citation":"J Biol Chem 2018 Jun 15;293(24):9210-9222","abstract":"Mmi1 is an essential RNA-binding protein in the fission yeast  Schizosaccharomyces pombe  that eliminates meiotic transcripts during normal vegetative growth. Mmi1 contains a YTH domain that binds specific RNA sequences, targeting mRNAs for degradation. The YTH domain of Mmi1 uses a noncanonical RNA-binding surface that includes contacts outside the conserved fold. Here, we report that an N-terminal extension that is proximal to the YTH domain enhances RNA binding. Using X-ray crystallography, NMR, and biophysical methods, we show that this low-complexity region becomes more ordered upon RNA binding. This enhances the affinity of the interaction of the Mmi1 YTH domain with specific RNAs by reducing the dissociation rate of the Mmi1-RNA complex. We propose that the low-complexity region influences RNA binding indirectly by reducing dynamic motions of the RNA-binding groove and stabilizing a conformation of the YTH domain that binds to RNA with high affinity. Taken together, our work reveals how a low-complexity region proximal to a conserved folded domain can adopt an ordered structure to aid nucleic acid binding.","doi":"10.1074/jbc.RA118.002291","authors":"Stowell JAW, Wagstaff JL, Hill CH, Yu M, McLaughlin SH, Freund SMV, Passmore LA","authors_abbrev":"Stowell JAW et al.","pubmed_publication_date":"15 Jun 2018","pubmed_entrez_date":"2018-04-27","publication_year":"2018","canto_session_key":"d651aceebcf69794","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"James Stowell","canto_first_approved_date":"2018-06-05 15:44:32","canto_approved_date":"2018-06-05 15:44:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-05-14 17:13:01","canto_added_date":"2018-04-28 00:15:04","annotation_curators":[{"name":"James Stowell","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-05","pdb_entries":[{"pdb_id":"6fpx","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A/C/E","position":"299-488"}],"title":"Structure of S. pombe Mmi1 in complex with 11-mer RNA","entry_authors":"Stowell JAW,Hill CH,Yu M,Wagstaff JL,McLaughlin SH,Freund SMV,Passmore LA","entry_authors_abbrev":"Stowell JAW et al.","reference_uniquename":"PMID:29695507","experimental_method":"X-ray","resolution":"1.97"},{"pdb_id":"6fpp","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A/B","position":"327-488"}],"title":"Structure of S. pombe Mmi1","entry_authors":"Stowell JAW,Hill CH,Yu M,Wagstaff JL,McLaughlin SH,Freund SMV,Passmore LA","entry_authors_abbrev":"Stowell JAW et al.","reference_uniquename":"PMID:29695507","experimental_method":"X-ray","resolution":"1.93"},{"pdb_id":"6fpq","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A","position":"299-488"}],"title":"Structure of S. pombe Mmi1 in complex with 7-mer RNA","entry_authors":"Stowell JAW,Hill CH,Yu M,Wagstaff JL,McLaughlin SH,Freund SMV,Passmore LA","entry_authors_abbrev":"Stowell JAW et al.","reference_uniquename":"PMID:29695507","experimental_method":"X-ray","resolution":"1.42"}]},{"uniquename":"PMID:2044950","title":"mRNA-type introns in U6 small nuclear RNA genes: implications for the catalysis in pre-mRNA splicing.","citation":"Genes Dev 1991 Jun;5(6):1022-31","abstract":"U6 small nuclear RNA is one of the spliceosomal RNAs involved in pre-mRNA splicing. In the fission yeast Schizosaccharomyces pombe, the U6 RNA gene was found to have an intron similar to a nuclear pre-mRNA intron, and it was proposed that the U6 intron might be inserted erroneously during pre-mRNA splicing. Using the polymerase chain reaction, we analyzed the U6 RNA genes of 52 organisms. In addition to the five species of Schizosaccharomyces, we found that the yeast species Rhodotorula hasegawae and Rhodosporidium dacryoidum also have mRNA-type introns in their U6 genes; however, in all the other organisms tested, we found no intron within the region of the U6 gene examined. Four introns and one intron are present in the R. hasegawae and R. dacryoidum U6 genes, respectively; and these introns are located at sites differing from the location of the Schizosaccharomyces U6 intron. Most of the U6 introns locate within the conserved domain, which is strikingly similar in structure to the catalytic center of the negative strand of the satellite RNA of tobacco ring spot virus. The introns of the S. pombe and R. dacryoidum U6 genes are located immediately adjacent to the nucleotides that were shown to be essential for the second step of the splicing reaction. These results support the notion that U6 RNA has a catalytic role in pre-mRNA splicing and that U6 introns originated from insertion of an excised intron during pre-mRNA splicing.","authors":"Tani T, Ohshima Y","authors_abbrev":"Tani T et al.","pubmed_publication_date":"Jun 1991","pubmed_entrez_date":"1991-06-01","publication_year":"1991","canto_session_key":"a56fe9196e6e5d33","canto_annotation_status":"APPROVED","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_approved_date":"2014-06-20 13:13:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-20 13:13:20","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-20"},{"uniquename":"PMID:34706246","title":"Cross talk between the upstream exon-intron junction and Prp2 facilitates splicing of non-consensus introns.","citation":"Cell Rep 2021 Oct 26;37(4):109893","abstract":"Splicing of mRNA precursors is essential in the regulation of gene expression. U2AF65 recognizes the poly-pyrimidine tract and helps in the recognition of the branch point. Inactivation of fission yeast U2AF65 (Prp2) blocks splicing of most, but not all, pre-mRNAs, for reasons that are not understood. Here, we have determined genome-wide the splicing efficiency of fission yeast cells as they progress into synchronous meiosis in the presence or absence of functional Prp2. Our data indicate that in addition to the splicing elements at the 3' end of any intron, the nucleotides immediately upstream the intron will determine whether Prp2 is required or dispensable for splicing. By changing those nucleotides in any given intron, we regulate its Prp2 dependency. Our results suggest a model in which Prp2 is required for the coordinated recognition of both intronic ends, placing Prp2 as a key regulatory element in the determination of the exon-intron boundaries.","doi":"10.1016/j.celrep.2021.109893","authors":"Hümmer S, Borao S, Guerra-Moreno A, Cozzuto L, Hidalgo E, Ayté J","authors_abbrev":"Hümmer S et al.","pubmed_publication_date":"26 Oct 2021","pubmed_entrez_date":"2021-10-27","publication_year":"2021","canto_session_key":"bf8f7e547025faa5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sonia Borao","canto_first_approved_date":"2025-03-26 16:25:29","canto_approved_date":"2026-05-27 12:33:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-24 18:49:42","canto_added_date":"2021-10-29 00:15:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":9,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Sonia Borao","community_curator":true,"annotation_count":1,"orcid":"0000-0003-3775-2284","file_type":null,"file_name":null}],"file_curator_name":"Pascal Carme","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":229,"orcid":"0009-0003-9059-1333","file_type":"PHAF","file_name":"PMID_34706246_phaf.tsv"}],"genes":["SPBC16A3.09c","SPBC31E1.01c","SPCC1259.13","SPAC644.11c","SPAC4D7.14","SPAC22E12.17c","SPCC794.02","SPBC27B12.05","SPAC23H3.07c","SPBC16D10.02","SPBC337.03","SPBC25H2.03","SPBC15C4.02","SPAC227.11c","SPBC2G2.10c","SPBP23A10.17","SPCC830.10","SPAC222.07c","SPCC1620.05","SPAC15A10.10","SPCP1E11.03","SPCC1183.10","SPBC25H2.18","SPAC2F3.12c","SPACUNK12.02c","SPBC1604.17c","SPAC26H5.03","SPAC19G12.17","SPBC428.16c","SPAC3H1.13","SPCC1919.11","SPBC20F10.04c","SPAC1093.03","SPAC22A12.08c","SPBP23A10.04","SPAC16E8.02","SPBC29A10.11c","SPAC959.04c","SPCC1739.04c","SPAC1006.06","SPBC31F10.04c","SPAC328.08c","SPAC15E1.08","SPCC645.13","SPAC227.14","SPAC9.12c","SPAC9G1.05","SPBC9B6.07","SPCC1682.04","SPCP31B10.04","SPBP19A11.07c","SPAC2C4.10c","SPAC1D4.06c","SPBC1A4.06c","SPBC16H5.13","SPBC1604.07","SPAC22F3.05c","SPAC16E8.07c","SPAC22F3.15","SPAC17G8.04c","SPAC17C9.01c","SPACUNK4.14","SPCC1739.15","SPCC622.14","SPAC31G5.15","SPBC23G7.16","SPBP35G2.09","SPBC3B9.08c","SPAC22E12.16c","SPBC27B12.10c","SPBC409.18","SPAC12B10.13","SPCC16C4.04","SPAC8F11.07c","SPAC9G1.13c","SPBC776.04","SPSNRNA.01","SPBC582.04c","SPCC1235.09","SPAC31A2.16","SPBC11B10.09","SPAPB1A10.16","SPAC2F3.13c","SPAC13A11.04c","SPCC18.05c","SPCC1393.07c","SPAC19G12.01c","SPCC1259.12c","SPCC1235.15","SPBC19G7.14c","SPBC23E6.07c","SPBC887.04c","SPBC3B9.17","SPCC1672.12c","SPCC126.06","SPAC20H4.09","SPBC146.07","SPBC14C8.19","SPAC1687.02","SPBC19F8.01c","SPAC823.16c","SPAC17G8.14c","SPBC1347.07","SPAC1556.08c","SPAC1610.03c","SPBC9B6.04c","SPAC3A11.06","SPCC16C4.22","SPBC119.02","SPBC12D12.09","SPBC21D10.08c","SPBC947.11c","SPAC1952.13","SPBC646.03","SPBC19G7.04","SPBC16D10.10","SPBPJ4664.05","SPAC890.07c","SPAC3G9.13c","SPCC5E4.10c","SPAC15A10.13","SPBC119.14","SPAC1B3.05","SPAC4D7.05","SPAC1002.07c","SPCC330.02","SPAC22H10.02","SPCC14G10.04","SPCC18B5.06","SPBC29A3.14c","SPAC6F6.08c","SPBC776.07","SPCC1620.07c","SPCC1442.12","SPCC1020.13c","SPBC800.09","SPBC16E9.19","SPAC22F8.07c","SPAC1B1.04c","SPAC3H8.05c","SPAC30.03c","SPBP8B7.11","SPBC13G1.09","SPBC577.09","SPCC188.08c","SPAC9.05","SPAC959.09c","SPBC14F5.02","SPCC417.06c","SPBC577.02","SPAC23C4.12","SPAC1D4.04","SPAC23C4.17","SPAPB2B4.01c","SPCC188.03","SPAP27G11.12","SPBP8B7.10c","SPBC582.09","SPAC9.07c","SPBC1709.04c","SPBC2G2.11","SPSNRNA.06","SPBC17D11.08","SPAC4D7.04c","SPBC1861.03","SPBC660.14","SPCC1840.05c","SPAC13C5.02","SPBC839.10","SPBC651.02","SPBC428.07","SPCC1281.08","SPAC3A11.02","SPBC1778.04","SPCC5E4.03c","SPBC13G1.04c","SPBC365.10","SPAC24H6.01c","SPCC18B5.11c","SPCC16A11.10c","SPAC23D3.14c","SPCC126.02c","SPCC1620.02","SPBC20F10.06","SPAPB8E5.10","SPBC1773.09c","SPAC167.02","SPAC2G11.03c","SPAC22E12.08","SPBC405.04c","SPBC336.15","SPBC337.09","SPBC19C2.12","SPAPB18E9.01","SPBC1685.10","SPAC959.02","SPCC4B3.04c","SPBC1685.06","SPBC2G2.06c","SPBC8D2.02c","SPAC1142.07c","SPAC31A2.15c","SPAPB17E12.11","SPAC6G10.06","SPAC6F6.16c","SPBC19G7.18c","SPCC126.12","SPBC2A9.06c","SPAC926.07c","SPAC3C7.07c","SPAC22G7.04","SPBC1711.09c","SPAC3G9.17","SPBC12C2.05c","SPCC338.05c","SPBC1A4.08c","SPAC22F3.03c","SPBC887.06c","SPAC56F8.08","SPAC16E8.03","SPBC8D2.01","SPCC1183.05c","SPBC3E7.05c","SPAC1639.01c","SPAC22G7.09c","SPBC19G7.19","SPCC70.07c","SPAC19B12.10","SPAC16C9.02c","SPAC343.07","SPCC74.01","SPBC15D4.14","SPBC649.04"],"gene_count":233,"ltp_gene_count":4,"approved_date":"2025-03-26"},{"uniquename":"PMID:26451775","title":"Connectivity Homology Enables Inter-Species Network Models of Synthetic Lethality.","citation":"PLoS Comput Biol 2015 Oct;11(10):e1004506","abstract":"Synthetic lethality is a genetic interaction wherein two otherwise nonessential genes cause cellular inviability when knocked out simultaneously. Drugs can mimic genetic knock-out effects; therefore, our understanding of promiscuous drugs, polypharmacology-related adverse drug reactions, and multi-drug therapies, especially cancer combination therapy, may be informed by a deeper understanding of synthetic lethality. However, the colossal experimental burden in humans necessitates in silico methods to guide the identification of synthetic lethal pairs. Here, we present SINaTRA (Species-INdependent TRAnslation), a network-based methodology that discovers genome-wide synthetic lethality in translation between species. SINaTRA uses connectivity homology, defined as biological connectivity patterns that persist across species, to identify synthetic lethal pairs. Importantly, our approach does not rely on genetic homology or structural and functional similarity, and it significantly outperforms models utilizing these data. We validate SINaTRA by predicting synthetic lethality in S. pombe using S. cerevisiae data, then identify over one million putative human synthetic lethal pairs to guide experimental approaches. We highlight the translational applications of our algorithm for drug discovery by identifying clusters of genes significantly enriched for single- and multi-drug cancer therapies.","doi":"10.1371/journal.pcbi.1004506","authors":"Jacunski A, Dixon SJ, Tatonetti NP","authors_abbrev":"Jacunski A et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2015-10-10","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-10-11 00:18:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ577641","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.34"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:40163528","title":"The nuclear poly(A)-binding protein Pab2/PABPN1 promotes heterochromatin assembly through the formation of Pab2 nuclear condensates.","citation":"PLoS Genet 2025 Mar 31;21(3):e1011647","abstract":"The assembly of constitutive heterochromatin is a prerequisite for maintaining genome stability. However, the mechanism of heterochromatin formation has yet to be completely understood. Here, we demonstrate a crucial role of the nuclear poly(A)-binding protein (PABP) Pab2/PABPN1 in promoting constitutive heterochromatin formation in the fission yeast Schizosaccharomyces japonicus. Histone H3 Lys 9 di- and tri-methylation, hallmarks of heterochromatin, are significantly reduced at centromeres in the absence of Pab2. Pab2 forms nuclear condensates through its RNA-recognition motif (RRM) and the intrinsically disordered domain (IDR), both of which bind to centromeric non-coding RNAs. Intriguingly, two key heterochromatin factors, the histone H3 Lys9 methyltransferase Clr4 and the Mi2-type chromatin remodeler Mit1, associate with centromeres in a Pab2-dependent manner. Pab2 interacts with two putative RNA-binding proteins, the ZC3H3 ortholog Red5 and the RBM26·27 ortholog Rmn1, both essential for heterochromatin formation. Deletion of the Pab2 N-terminal region, which disrupts this interaction, largely abolishes Pab2 function, underscoring the importance of this complex. Pab2 also associates and colocalizes with Ppn1 (a PPP1R10 ortholog), a component of the cleavage and polyadenylation specificity factor (CPSF) complex, and ppn1 mutations disrupt constitutive heterochromatin. Notably, both Ppn1 and Rmn1 are able to interact with Clr4. Our findings reveal that Pab2 plays a pivotal role in heterochromatin assembly by forming nuclear condensates through its RRM/IDR, and Pab2 condensates facilitate the recruitment of Clr4 and Mit1 to centromeres, potentially through its binding proteins, Ppn1 and Rmn1. This study provides new insights into the mechanisms underlying heterochromatin formation and highlights the importance of RNA-binding proteins and phase separation in this process.","doi":"10.1371/journal.pgen.1011647","authors":"Liu Z, Song X, Thillainadesan G, Sugiyama T","authors_abbrev":"Liu Z et al.","pubmed_publication_date":"31 Mar 2025","pubmed_entrez_date":"2025-03-31","publication_year":"2025","canto_session_key":"06e3a4338a8adb5d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-04-01 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17486762","title":"[Dds20 operates in cds1-independent mechanism of tolerance to UV-induced DNA damage in Schizosaccharomyces pombe cells].","citation":"Genetika 2007 Mar;43(3):417-21","abstract":"Repair of DNA double-stranded breaks caused by ionizing radiation or cellular metabolization, homologous recombination, is an evolutionary conserved process controlled by RAD52 group genes. Genes of recombinational repair also play a leading role in the response to DNA damage caused by UV light. Cells with deletion in gene dds20 of recombinational repair were shown to manifest hypersensitivity to the action of UV light at lowered incubation temperature. Epistatic analysis revealed that dds20+ is not a member of the NER and UVER gene groups responsible for the repair of DNA damage induced by UV light. The Dds protein has functions in the Cds1-independent mechanism of UV damage tolerance of DNA.","authors":"Salakhova AF, Bashkirov VI, Khasanov FK","authors_abbrev":"Salakhova AF et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-05-10","publication_year":"2007","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20018864","title":"Neuronal calcium sensor-1 (Ncs1p) is up-regulated by calcineurin to promote Ca2+ tolerance in fission yeast.","citation":"J Biol Chem 2010 Feb 12;285(7):4405-14","abstract":"Neuronal calcium sensor (NCS) proteins regulate signal transduction and are highly conserved from yeast to humans. NCS homolog in fission yeast (Ncs1p) is essential for cell growth under extreme Ca(2+) conditions. Ncs1p expression increases approximately 100-fold when fission yeast grows in high extracellular Ca(2+) (>0.1 M). Here, we show that Ca(2+)-induced expression of Ncs1p is controlled at the level of transcription. Transcriptional reporter assays show that ncs1 promoter activity increased 30-fold when extracellular Ca(2+) was raised to 0.1 M and was highly Ca(2+)-specific. Ca(2+)-dependent transcription of ncs1 is abolished by the calcineurin inhibitor (FK506) and by knocking out the calcineurin target, prz1. Thus, Ca(2+)-induced expression of Ncs1p is linked to the calcineurin/prz1 stress response. The Ca(2+)-responsive ncs1 promoter region consists of 130 nucleotides directly upstream from the start codon and contains tandem repeats of the sequence, 5'-caact-3', that binds to Prz1p. The Ca(2+)-sensitive ncs1Delta phenotype is rescued by a yam8 null mutation, suggesting a possible interaction between Ncs1p and the Ca(2+) channel, Yam8p. Ca(2+) uptake and Ncs1p binding to yeast membranes are both decreased in yam8Delta, suggesting Ca(2+)-induced binding of Ncs1p to Yam8p results in channel closure. We propose that Ncs1p promotes Ca(2+) tolerance in fission yeast, in part by cytosolic Ca(2+) buffering and perhaps by negatively regulating the Yam8p Ca(2+) channel.","doi":"10.1074/jbc.M109.058594","authors":"Hamasaki-Katagiri N, Ames JB","authors_abbrev":"Hamasaki-Katagiri N et al.","pubmed_publication_date":"12 Feb 2010","pubmed_entrez_date":"2009-12-19","publication_year":"2010","canto_session_key":"eeccd430b89acffb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-05-25 16:42:26","canto_approved_date":"2024-04-03 16:09:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-23 09:09:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.04","SPAC1F5.08c","SPAC4G8.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-05-25"},{"uniquename":"EMBL:SPD125","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41201247","title":"Impacts of stress and aging on spore health in  Schizosaccharomyces pombe .","citation":"Microbiol Spectr 2025 Nov 07;:e0171025","abstract":"","doi":"10.1128/spectrum.01710-25","authors":"Nuckolls NL, Eickbush MT, Lange JJ, Wood CJ, Nowotarski SH, Zanders SE","authors_abbrev":"Nuckolls NL et al.","pubmed_publication_date":"07 Nov 2025","pubmed_entrez_date":"2025-11-07","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-11-08 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24265825","title":"Concerted action of the ubiquitin-fusion degradation protein 1 (Ufd1) and Sumo-targeted ubiquitin ligases (STUbLs) in the DNA-damage response.","citation":"PLoS One 2013;8(11):e80442","abstract":"In eukaryotes many players in the DNA-damage response (DDR) catalyze protein sumoylation or ubiquitylation. Emphasis has been placed on how these modifications orchestrate the sequential recruitment of repair factors to sites of DNA damage or stalled replication forks. Here, we shed light on a pathway in which sumoylated factors are eliminated through the coupled action of Sumo-targeted ubiquitin ligases (STUbLs) and the ubiquitin-fusion degradation protein 1 (Ufd1). Ufd1 is a subunit of the Cdc48-Ufd1-Npl4 complex implicated in the sorting of ubiquitylated substrates for degradation by the proteasome. We find that in fission yeast, Ufd1 interacts physically and functionally with the Sumo-targeted ubiquitin ligase (STUbL) Rfp1, homologous to human RNF4, and with the Sumo E3 ligase Pli1, homologous to human PIAS1. Deleting a C-terminal domain of Ufd1 that mediates the interaction of Ufd1 with Rfp1, Pli1, and Sumo (ufd1ΔCt(213-342) ) lead to an accumulation of high-molecular-weight Sumo conjugates and caused severe genomic instabilities. The spectrum of sensitivity of ufd1ΔCt(213-342) cells to genotoxins, the epistatic relationships of ufd1ΔCt(213-342) with mutations in DNA repair factors, and the localization of the repair factor Rad22 in ufd1ΔCt(213-342) cells point to ufd1ΔCt(213-342) cells accumulating aberrant structures during replication that require homologous recombination (HR) for their repair. We present evidence that HR is however often not successful in ufd1ΔCt(213-342) cells and we identify Rad22 as one of the high-molecular-weight conjugates accumulating in the ufd1ΔCt(213-342) mutant consistent with Rad22 being a STUbL/Ufd1 substrate. Suggesting a direct role of Ufd1 in the processing of Sumo-conjugates, Ufd1 formed nuclear foci colocalizing with Sumo during the DDR, and Sumo-conjugates accumulated in foci in the ufd1ΔCt(213-342) mutant. Broader functional relationships between Ufd1 and STUbLs conceivably affect numerous cellular processes beyond the DDR.","doi":"10.1371/journal.pone.0080442","authors":"Køhler JB, Jørgensen ML, Beinoraité G, Thorsen M, Thon G","authors_abbrev":"Køhler JB et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-11-23","publication_year":"2013","canto_session_key":"247abbf8bb674798","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPAC1687.05","SPAC644.14c","SPBC16A3.09c","SPBC1734.06","SPAC1565.08","SPAC19A8.10","SPBC3D6.11c","SPAC30D11.10","SPAC11E3.04c"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:17289569","title":"SHREC, an effector complex for heterochromatic transcriptional silencing.","citation":"Cell 2007 Feb 09;128(3):491-504","abstract":"Transcriptional gene silencing (TGS) is the mechanism generally thought by which heterochromatin effects silencing. However, recent discovery in fission yeast of a cis-acting posttranscriptional gene-silencing (cis-PTGS) pathway operated by the RNAi machinery at heterochromatin challenges the role of TGS in heterochromatic silencing. Here, we describe a multienzyme effector complex (termed SHREC) that mediates heterochromatic TGS in fission yeast. SHREC consists of a core quartet of proteins - Clr1, Clr2, Clr3, and Mit1 - which distribute throughout all major heterochromatin domains to effect TGS via distinct activities associated with the histone deacetylase Clr3 and the SNF2 chromatin-remodeling factor homolog Mit1. SHREC is also recruited to the telomeres by multiple independent mechanisms involving telomere binding protein Ccq1 cooperating with Taz1 and the RNAi machinery, and to euchromatic sites, via mechanism(s) distinct from its heterochromatin localization aided by Swi6/HP1. Our analyses suggest that SHREC regulates nucleosome positioning to assemble higher-order chromatin structures critical for heterochromatin functions.","authors":"Sugiyama T, Cam HP, Sugiyama R, Noma K, Zofall M, Kobayashi R, Grewal SI","authors_abbrev":"Sugiyama T et al.","pubmed_publication_date":"09 Feb 2007","pubmed_entrez_date":"2007-02-10","publication_year":"2007","canto_session_key":"5a010480a9612ae6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-03-24 08:31:58","canto_approved_date":"2026-02-15 11:45:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-12 19:37:39","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":88,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.17","SPBP35G2.10","SPAC16A10.07c","SPCC188.07","SPBC28F2.12","SPAC18G6.02c","SPBC800.03","SPCC736.11","SPAC1B3.17","SPAC664.01c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2020-03-24"},{"uniquename":"PMID:23986481","title":"Centromeric motion facilitates the mobility of interphase genomic regions in fission yeast.","citation":"J Cell Sci 2013 Nov 15;126(Pt 22):5271-83","abstract":"Dispersed genetic elements, such as retrotransposons and Pol-III-transcribed genes, including tRNA and 5S rRNA, cluster and associate with centromeres in fission yeast through the function of condensin. However, the dynamics of these condensin-mediated genomic associations remains unknown. We have examined the 3D motions of genomic loci including the centromere, telomere, rDNA repeat locus, and the loci carrying Pol-III-transcribed genes or long-terminal repeat (LTR) retrotransposons in live cells at as short as 1.5-second intervals. Treatment with carbendazim (CBZ), a microtubule-destabilizing agent, not only prevents centromeric motion, but also reduces the mobility of the other genomic loci during interphase. Further analyses demonstrate that condensin-mediated associations between centromeres and the genomic loci are clonal, infrequent and transient. However, when associated, centromeres and the genomic loci migrate together in a coordinated fashion. In addition, a condensin mutation that disrupts associations between centromeres and the genomic loci results in a concomitant decrease in the mobility of the loci. Our study suggests that highly mobile centromeres pulled by microtubules in cytoplasm serve as 'genome mobility elements' by facilitating physical relocations of associating genomic regions.","doi":"10.1242/jcs.133678","authors":"Kim KD, Tanizawa H, Iwasaki O, Corcoran CJ, Capizzi JR, Hayden JE, Noma K","authors_abbrev":"Kim KD et al.","pubmed_publication_date":"15 Nov 2013","pubmed_entrez_date":"2013-08-30","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:796682","title":"Anomalies in the selection of mutants of Schizosaccharomyces pombe resistant to 8-azaguanine.","citation":"Mol Gen Genet 1976 Dec 08;149(2):239-41","abstract":"Anomalies in selection render 8-azaguanine unsuitable as a selective agent for screening forward mutations in continuour cultures of Sch. pombe. This system may, however, provide tha basis for an enrichment method for the simultaneous isolation of mutants at two loci.","authors":"McAthey P","authors_abbrev":"McAthey P","pubmed_publication_date":"08 Dec 1976","pubmed_entrez_date":"1976-12-08","publication_year":"1976","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2185750","title":"The fission yeast, Schizosaccharomyces pombe.","citation":"Bioessays 1990 Apr;12(4):189-91","abstract":"","authors":"Mitchison JM","authors_abbrev":"Mitchison JM","pubmed_publication_date":"Apr 1990","pubmed_entrez_date":"1990-04-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35633597","title":"UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA polymerase II and are the human orthologues of yeast Def1.","citation":"DNA Repair (Amst) 2022 Jul;115:103343","abstract":"During transcription, RNA polymerase II (RNAPII) faces numerous obstacles, including DNA damage, which can lead to stalling or arrest. One mechanism to contend with this situation is ubiquitylation and degradation of the largest RNAPII subunit, RPB1 - the 'last resort' pathway. This conserved, multi-step pathway was first identified in yeast, and the functional human orthologues of all but one protein, RNAPII Degradation Factor 1 (Def1), have been discovered. Here we show that following UV-irradiation, human Ubiquitin-associated protein 2 (UBAP2) or its paralogue UBAP2-like (UBAP2L) are involved in the ubiquitylation and degradation of RNAPII through the recruitment of Elongin-Cul5 ubiquitin ligase. Together, our data indicate that UBAP2 and UBAP2L are the human orthologues of yeast Def1, and so identify the key missing proteins in the human last resort pathway.","doi":"10.1016/j.dnarep.2022.103343","authors":"Herlihy AE, Boeing S, Weems JC, Walker J, Dirac-Svejstrup AB, Lehner MH, Conaway RC, Conaway JW, Svejstrup JQ","authors_abbrev":"Herlihy AE et al.","pubmed_publication_date":"Jul 2022","pubmed_entrez_date":"2022-05-28","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:14185","HGNC:29877","SPBC354.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23093942","title":"Recovery of arrested replication forks by homologous recombination is error-prone.","citation":"PLoS Genet 2012;8(10):e1002976","abstract":"Homologous recombination is a universal mechanism that allows repair of DNA and provides support for DNA replication. Homologous recombination is therefore a major pathway that suppresses non-homology-mediated genome instability. Here, we report that recovery of impeded replication forks by homologous recombination is error-prone. Using a fork-arrest-based assay in fission yeast, we demonstrate that a single collapsed fork can cause mutations and large-scale genomic changes, including deletions and translocations. Fork-arrest-induced gross chromosomal rearrangements are mediated by inappropriate ectopic recombination events at the site of collapsed forks. Inverted repeats near the site of fork collapse stimulate large-scale genomic changes up to 1,500 times over spontaneous events. We also show that the high accuracy of DNA replication during S-phase is impaired by impediments to fork progression, since fork-arrest-induced mutation is due to erroneous DNA synthesis during recovery of replication forks. The mutations caused are small insertions/duplications between short tandem repeats (micro-homology) indicative of replication slippage. Our data establish that collapsed forks, but not stalled forks, recovered by homologous recombination are prone to replication slippage. The inaccuracy of DNA synthesis does not rely on PCNA ubiquitination or trans-lesion-synthesis DNA polymerases, and it is not counteracted by mismatch repair. We propose that deletions/insertions, mediated by micro-homology, leading to copy number variations during replication stress may arise by progression of error-prone replication forks restarted by homologous recombination.","doi":"10.1371/journal.pgen.1002976","authors":"Iraqui I, Chekkal Y, Jmari N, Pietrobon V, Fréon K, Costes A, Lambert SA","authors_abbrev":"Iraqui I et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-10-25","publication_year":"2012","canto_session_key":"40fd88a127db667a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Lambert","canto_first_approved_date":"2014-08-05 09:41:59","canto_approved_date":"2023-11-14 19:44:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-20 15:35:05","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sarah Lambert","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPAC30D11.10","SPAC644.14c","SPAC2G11.12"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-08-05"},{"uniquename":"PMID:9099890","title":"Comprehensive cloning of Schizosaccharomyces pombe genes encoding translation elongation factors.","citation":"Gene 1997 Mar 18;187(2):259-66","abstract":"In the course of the Schizosaccharomyces pombe cDNA project, we succeeded in cloning all the genes encoding translation elongation factors EF-1alpha, EF-1beta, EF-1gamma, EF-2 and EF-3. With the exception of the EF-1gamma gene, the nucleotide (nt) sequence of S. pombe elongation factors has not been previously reported. For EF-1alpha, we found three genes whose amino acid (aa) sequences are quite homologous each other (99.5%), but whose 3' untranslated regions (UTRs) are completely different. Southern blot indicated that those three EF-1alpha genes are located at different loci. Northern analysis indicated that one of three EF-1alpha genes was inducible with UV-irradiation, while the level of expression for another of three EF-1alpha genes was repressed by UV and heat-shock (HS) treatments. The aa sequence predicted from the nt sequence of the S. pombe EF-1beta cDNA clone covered almost all the coding sequence (CDS) of EF-1beta except the first methionine which has 55.4% identity with that of S. cerevisiae. We also identified two copies of S. pombe EF-2 genes. Their aa sequences deduced from nt sequences are identical (100%), but they have different 3' UTRs. The location of these two EF-2 genes in different loci was proved by Southern analysis. The S. pombe EF-3 cDNA clone encoded only a third of the CDS from the C-terminal and its deduced aa sequence has a 76% identity with those of other yeasts and fungi.","authors":"Mita K, Morimyo M, Ito K, Sugaya K, Ebihara K, Hongo E, Higashi T, Hirayama Y, Nakamura Y","authors_abbrev":"Mita K et al.","pubmed_publication_date":"18 Mar 1997","pubmed_entrez_date":"1997-03-18","publication_year":"1997","canto_session_key":"037e7452d6a9b565","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-10-27 14:30:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-27 14:30:09","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC513.01c","SPAC23A1.10","SPBC839.15c","SPCC794.09c"],"gene_count":4,"ltp_gene_count":0,"approved_date":"2014-10-27"},{"uniquename":"PMID:12478586","title":"Helicase activity is only partially required for Schizosaccharomyces pombe Rqh1p function.","citation":"Yeast 2002 Dec;19(16):1381-98","abstract":"The RecQ-related family of DNA helicases is required for the maintenance of genomic stability in organisms ranging from bacteria to humans. In humans, mutation of three RecQ-related helicases, BLM, WRN and RecQL4, cause the cancer-prone and premature ageing diseases of Bloom syndrome, Werner's syndrome and Rothmund-Thompson syndrome, respectively. In the fission yeast Schizosaccharomyces pombe, disruption of the rqh1(+) gene, which encodes the single Sz. pombe RecQ-related helicase, causes cells to display reduced viability and elevated levels of chromosome loss. After S-phase arrest or DNA damage, cells lacking rqh1(+) function display elevated levels of homologous recombination and defective chromosome segregation. Here we show that, like other RecQ family members, the Rqh1p protein displays 3' to 5' DNA helicase activity. Interestingly, however, unlike other RecQ family members, the helicase activity of Rqh1p is only partially required for its function in recovery from S-phase arrest or DNA damage. We also report that high cellular levels of Rqh1p result in lethal chromosome segregation defects, while more moderate levels of Rqh1p cause significantly elevated rates of chromosome loss. This suggests that careful regulation of RecQ-like protein levels in eukaryotic cells is vital for maintaining genome stability.","authors":"Ahmad F, Kaplan CD, Stewart E","authors_abbrev":"Ahmad F et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2002-12-13","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:9256449","title":"Identification of a new mammalian centrin gene, more closely related to Saccharomyces cerevisiae CDC31 gene.","citation":"Proc Natl Acad Sci U S A 1997 Aug 19;94(17):9141-6","abstract":"Among the numerous centrin isoforms identified by two-dimensional gel electrophoresis in human cells, an acidic and slow-migrating isoform is particularly enriched in a centrosome fraction. We report here that this isoform specifically reacts with antibodies raised against Saccharomyces cerevisiae Cdc31p and is present, as other centrin isoforms, in the distal lumen of centrioles. It is encoded by a new centrin gene, which we propose to name HsCEN3 (Homo sapiens centrin gene 3). This gene is more closely related to the yeast CDC31 gene, and shares less identity with algae centrin than HsCEN1 and HsCEN2. A murine CDC31-related gene was also found that shows 98% identity and 100% similarity with HsCEN3, demonstrating a higher interspecies conservation than the murine centrin gene MmCEN1 (Mus musculus centrin gene 1) with either HsCEN1, or HsCEN2. Finally, immunological data suggest that a CDC31-related gene could exist in amphibians and echinoderms as well. All together, our data suggest the existence of two divergent protein subfamilies in the current centrin family, which might be involved in distinct centrosome-associated functions. The possible implication of this new mammalian centrin gene in centrosome duplication is discussed.","authors":"Middendorp S, Paoletti A, Schiebel E, Bornens M","authors_abbrev":"Middendorp S et al.","pubmed_publication_date":"19 Aug 1997","pubmed_entrez_date":"1997-08-19","publication_year":"1997","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:1867","HGNC:1866","SPCC1682.04","HGNC:1868"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11702774","title":"New insights into development from mitosis of a unicellular yeast.","citation":"Dev Cell 2001 Aug;1(2):158-60","abstract":"Studies in the fission yeast Schizosaccharomyces pombe have uncovered a new spindle checkpoint.","authors":"Hagan IM, Jones N, Carr AM","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-11-13","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16408319","title":"A truncated derivative of nmt 1 promoter exhibits temperature-dependent induction of gene expression in Schizosaccharomyces pombe.","citation":"Yeast 2006 Jan 15;23(1):55-65","abstract":"Despite increasing exploitation of Schizosaccharomyces pombe as a model system there is a lack of convenient vectors for research and application. Expression with the commonly used promoter, nmt 1, requires a laborious regime involving the removal of repressor, thiamine, from a growing culture and further growth for 18 h to achieve maximum expression, thus underlining the need for more user-friendly promoters. We report here the isolation and characterization of a truncated derivative of the nmt 1 promoter having novel induction characteristics: it is induced by shift of growth temperature from 36 degrees C to 25 degrees C, achieving maximum expression within 3 h. Similar features of expression were observed with the reporter genes GFP and beta-galactosidase, a native gene, cdc 18, and a commercially important foreign therapeutic protein, streptokinase. The new promoter element offers additional advantages, such as lack of deleterious effect on cell viability and potential ability to express toxic proteins. These features make the new promoter a potentially better alternative to nmt 1, both as a research tool and for expression of commercially important proteins in Sz. pombe, and suggest the possibility of using similar approaches to design promoters with novel and useful properties.","authors":"Kumar R, Singh J","authors_abbrev":"Kumar R et al.","pubmed_publication_date":"15 Jan 2006","pubmed_entrez_date":"2006-01-13","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12398289","title":"Isolation and characterisation of nuclear mutants with enhanced mitochondrial mutability in the fission yeast Schizosaccharomyces pombe.","citation":"Microbiol Res 2002;157(3):197-200","abstract":"In this paper we report the isolation and preliminary characterisation of nuclear mutants with increased mitochondrial mutability in fission yeast. Screening of about 2000 clones after nitrosoguanidine mutagenesis led to the isolation of ten mutator mutants. For one of them (mut-1) we show that the mutation is chromosomally encoded. The activity of the mutator is restricted to the mitochondrial genome, since it increases the mutation rate to mitochondrially encoded drug resistance considerably, whereas the mutability of nuclear genes is not altered.","authors":"Massardo DR, Del Giudice L, Del Giudice A, Wolf K","authors_abbrev":"Massardo DR et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-10-26","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15474417","title":"EXO1-A multi-tasking eukaryotic nuclease.","citation":"DNA Repair (Amst) 2004 Dec 02;3(12):1549-59","abstract":"Exo1 was first isolated as a 5' --> 3' exonuclease activity induced during meiosis in fission yeast and since that time has been implicated in a multitude of eukaryotic DNA metabolic pathways that include DNA repair, recombination, replication, and telomere integrity. Involvement in multiple pathways affecting genomic stability makes EXO1 a logical target for mutation during oncogenesis. Here, we review studies in several experimental systems that shed light on the role of Exo1 in these DNA transaction pathways, particularly those that may relate to oncogenesis.","authors":"Tran PT, Erdeniz N, Symington LS, Liskay RM","authors_abbrev":"Tran PT et al.","pubmed_publication_date":"02 Dec 2004","pubmed_entrez_date":"2004-10-12","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AF017180","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12839619","title":"High dosage Rhp51 suppression of the MMS sensitivity of DNA structure checkpoint mutants reveals a relationship between Crb2 and Rhp51.","citation":"Genes Cells 2003 Jul;8(7):573-86","abstract":"In eukaryotic cells DNA structure checkpoints organize the cellular responses of DNA repair and transient cell cycle arrest and thereby ensure genomic stability. To investigate the exact role of crb2+ in the DNA damage checkpoint response, a genetic screen was carried out in order to identify suppressors of the conditional MMS sensitivity of a crb2-1 mutant. Here we report the isolation of rhp51+ as a multicopy suppressor.\nWe show that suppression is not specific for the checkpoint mutant while it is specific for the MMS treatment. Rescue by rhp51+ over-expression is not a consequence of increased recombination repair or checkpoint compensation and epistasis analysis confirms that crb2+ and rhp51+ function in different pathways. A tight linkage between the two pathways is nevertheless suggested by the complementary expression or modification of Crb2 and Rhp51 proteins. Crb2 protein stability is down-regulated when Rhp51 is over-expressed and up-regulated in the absence of Rhp51. The up-regulation of Crb2 is independent of the activation of DNA structure checkpoints. Conversely Rhp51 is more readily activated and differentially modified in the absence of Crb2 or other checkpoint proteins.\nWe conclude that fission yeast Crb2 and Rhp51 function in two parallel, tightly connected and coordinately regulated pathways.","authors":"Smeets MF, Francesconi S, Baldacci G","authors_abbrev":"Smeets MF et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-07-04","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC9E9.08","SPAC1952.07","SPAC664.07c","SPAC20G4.04c","SPCC1259.13","SPAC14C4.13","SPBC216.05","SPBC342.05","SPCC18B5.11c"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"DDBJ:LC043101","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1486.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9188094","title":"Mcs4 mitotic catastrophe suppressor regulates the fission yeast cell cycle through the Wik1-Wis1-Spc1 kinase cascade.","citation":"Mol Biol Cell 1997 Mar;8(3):409-19","abstract":"Spc1 in Schizosaccharomyces pombe is a member of the stress-activated protein kinase family, an evolutionary conserved subfamily of mitogen-activated protein kinases (MAPKs). Spc1 is activated by a MAPK kinase homologue, Wis1, and negatively regulated by Pyp1 and Pyp2 tyrosine phosphatases. Mutations in the spc1+ and wis1+ genes cause a G2 cell cycle delay that is exacerbated during stress. Herein, we describe two upstream regulators of the Wis1-Spc1 cascade. wik1+ (Wis1 kinase) was identified from its homology to budding yeast SSK2, which encodes a MAPKK kinase that regulates the HOG1 osmosensing pathway. Delta wik1 cells are impaired in stress-induced activation of Spc1 and show a G2 cell cycle delay and osmosensitive growth. Moreover, overproduction of a constitutively active form of Wik1 induces hyperactivation of Spc1 in wis1(+)-dependent manner, suggesting that Wik1 regulates Spc1 through activation of Wis1. A mutation of mcs4+ (mitotic catastrophe suppressor) was originally isolated as a suppressor of the mitotic catastrophe phenotype of a cdc2-3w wee1-50 double mutant. We have found that mcs4- cells are defective at activation of Spc1 in response to various forms of stress. Epistasis analysis has placed Mcs4-upstream of Wik1 in the Spc1 activation cascade. These results indicate that Mcs4 is part of a sensor system for multiple environmental signals that modulates the timing of entry into mitosis by regulating the Wik1-Wis1-Spc1 kinase cascade. Inactivation of the sensor system delays the onset of mitosis and rescues lethal premature mitosis in cdc2-3w wee1-50 cells.","authors":"Shiozaki K, Shiozaki M, Russell P","authors_abbrev":"Shiozaki K et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_session_key":"b5c7867e7494b87a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-02-23 14:37:52","canto_approved_date":"2021-09-27 15:08:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-23 14:38:38","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC18B5.03","SPAC24B11.06c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2021-02-23"},{"uniquename":"PMID:26293347","title":"Replication dynamics in fission and budding yeasts through DNA polymerase tracking.","citation":"Bioessays 2015 Oct;37(10):1067-73","abstract":"The dynamics of eukaryotic DNA polymerases has been difficult to establish because of the difficulty of tracking them along the chromosomes during DNA replication. Recent work has addressed this problem in the yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae through the engineering of replicative polymerases to render them prone to incorporating ribonucleotides at high rates. Their use as tracers of the passage of each polymerase has provided a picture of unprecedented resolution of the organization of replicons and replication origins in the two yeasts and has uncovered important differences between them. Additional studies have found an overlapping distribution of DNA polymorphisms and the junctions of Okazaki fragments along mononucleosomal DNA. This sequence instability is caused by the premature release of polymerase δ and the retention of non proof-read DNA tracts replicated by polymerase α. The possible implementation of these new experimental approaches in multicellular organisms opens the door to the analysis of replication dynamics under a broad range of genetic backgrounds and physiological or pathological conditions.","doi":"10.1002/bies.201500072","authors":"Vázquez E, Antequera F","authors_abbrev":"Vázquez E et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2015-08-22","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-08-23 00:18:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22003849","title":"RNA interference in mammalian DNA methylation.","citation":"Biochem Cell Biol 2012 Feb;90(1):70-7","abstract":"RNAi and Dicer-dependent siRNAs are required for constitutive heterochromatin formation in fission yeast and for establishing DNA methylation at repetitive elements in plants. In the mammalian male germ line, DICER1-independent piRNAs are required for the full establishment of DNA methylation of dispersed repetitive transposable elements. However, in other mammalian cell types, no clear picture has yet emerged of the role of RNAi in establishing heterochromatin and DNA methylation. In mouse embryonic stem cells, which remain viable on loss of DICER1 and ablation of RNAi, while no firm evidence has been obtained for defective heterochromatin formation, there are indications of defective DNA methylation. The latter has been attributed to an indirect effect of reduced DNA methyltransferase (DNMT) activity due to a loss of miRNA-mediated gene regulation. However, it is unclear whether the reductions in DNMT activity were sufficient to affect DNA methylation. We consider it equally likely that the defects in DNA methylation that can be observed in DICER1-deficient embryonic stem cells are the result of nonspecific effects related to RNAi loss aside from reduced DNMT activity.","doi":"10.1139/o11-050","authors":"Mann JR, Mattiske DM","authors_abbrev":"Mann JR et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-10-19","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18826944","title":"Di-methyl H4 lysine 20 targets the checkpoint protein Crb2 to sites of DNA damage.","citation":"J Biol Chem 2008 Nov 28;283(48):33168-74","abstract":"Histone lysine methylation is an important chromatin modification that can be catalyzed to a mono-, di-, or tri-methyl state. An ongoing challenge is to decipher how these different methyllysine histone marks can mediate distinct aspects of chromatin function. The fission yeast checkpoint protein Crb2 is rapidly targeted to sites of DNA damage after genomic insult, and this recruitment requires methylation of histone H4 lysine 20 (H4K20). Here we show that the tandem tudor domains of Crb2 preferentially bind the di-methylated H4K20 residue. Loss of this interaction by disrupting either the tudor-binding motif or the H4K20 methylating enzyme Set9/Kmt5 ablates Crb2 localization to double-strand breaks and impairs checkpoint function. Further we show that dimethylation, but not tri-methylation, of H4K20 is required for Crb2 localization, checkpoint function, and cell survival after DNA damage. These results argue that the di-methyl H4K20 modification serves as a binding target that directs Crb2 to sites of genomic lesions and defines an important genome integrity pathway mediated by a specific methyl-lysine histone mark.","doi":"10.1074/jbc.M806857200","authors":"Greeson NT, Sengupta R, Arida AR, Jenuwein T, Sanders SL","authors_abbrev":"Greeson NT et al.","pubmed_publication_date":"28 Nov 2008","pubmed_entrez_date":"2008-10-02","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1834.03c","SPBC342.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:15866870","title":"Functional characterization of the iron-regulatory transcription factor Fep1 from Schizosaccharomyces pombe.","citation":"J Biol Chem 2005 Jul 01;280(26):25146-61","abstract":"In response to excess iron, Schizosaccharomyces pombe cells repress transcription of genes encoding components involved in iron uptake through the Fep1 transcription factor. Fep1 mediates this control by interacting with the consensus sequence 5'-(A/T)GATAA-3', found in iron-dependent promoters. In this report, we show that Fep1 localizes to the nucleus under both iron-replete and iron-starved conditions. The Fep1 DNA binding domain (amino acids 1-241) contains two GATA-type zinc finger motifs. Although we determine that the Fep1 C-terminal zinc finger (ZF2) is essential for DNA binding, we show that the N-terminal zinc finger (ZF1) enhances DNA binding affinity approximately 5-fold. Between the two zinc finger motifs of Fep1 resides an invariant amino acid sequence, denoted the Cys-rich region (amino acids 68-94), in which four highly conserved Cys residues are found. Cells harboring mutant alleles in which two or more of the conserved Cys residues were substituted by alanine exhibited elevated fio1(+) mRNA levels. We determine that the dissociation constant for the resulting complex between each of the Cys mutants and the sequence 5'-(A/T)GATAA-3' reflects a much lower affinity that correlates with failure to repress fio1(+) gene expression. Deletion analysis identified two heptad repeats (amino acids 522-536) within the C-terminal region of Fep1 that are necessary and sufficient to mediate Fep1 dimerization. Moreover, mutations that impair dimerization also negatively affect transcriptional repression. Together these findings reveal several novel features of Fep1, a non-canonical GATA factor required for iron homeostasis.","authors":"Pelletier B, Trott A, Morano KA, Labbé S","authors_abbrev":"Pelletier B et al.","pubmed_publication_date":"01 Jul 2005","pubmed_entrez_date":"2005-05-04","publication_year":"2005","canto_session_key":"72b789a688713879","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-12 13:40:45","canto_approved_date":"2022-06-06 06:26:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-06-12 13:40:38","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23E2.01","SPAC18B11.10","SPAC1F7.08"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-06-12"},{"uniquename":"PMID:34086116","title":"Contribution of yeast models to virus research.","citation":"Appl Microbiol Biotechnol 2021 Jun;105(12):4855-4878","abstract":"Time and again, yeast has proven to be a vital model system to understand various crucial basic biology questions. Studies related to viruses are no exception to this. This simple eukaryotic organism is an invaluable model for studying fundamental cellular processes altered in the host cell due to viral infection or expression of viral proteins. Mechanisms of infection of several RNA and relatively few DNA viruses have been studied in yeast to date. Yeast is used for studying several aspects related to the replication of a virus, such as localization of viral proteins, interaction with host proteins, cellular effects on the host, etc. The development of novel techniques based on high-throughput analysis of libraries, availability of toolboxes for genetic manipulation, and a compact genome makes yeast a good choice for such studies. In this review, we provide an overview of the studies that have used yeast as a model system and have advanced our understanding of several important viruses. KEY POINTS: • Yeast, a simple eukaryote, is an important model organism for studies related to viruses. • Several aspects of both DNA and RNA viruses of plants and animals are investigated using the yeast model. • Apart from the insights obtained on virus biology, yeast is also extensively used for antiviral development.","doi":"10.1007/s00253-021-11331-w","authors":"Sahaya Glingston R, Yadav J, Rajpoot J, Joshi N, Nagotu S","authors_abbrev":"Sahaya Glingston R et al.","pubmed_publication_date":"Jun 2021","pubmed_entrez_date":"2021-06-04","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-06-06 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16841061","title":"New 'omics tools for fission yeast.","citation":"Nat Biotechnol 2006 Jul;24(7):789-90","abstract":"","authors":"Sazer S","authors_abbrev":"Sazer S","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-07-15","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPMYB","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ632005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.39"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11901107","title":"Fission yeast mutants affecting telomere clustering and meiosis-specific spindle pole body integrity.","citation":"Genetics 2002 Mar;160(3):861-76","abstract":"In meiotic prophase of many eukaryotic organisms, telomeres attach to the nuclear envelope and form a polarized configuration called the bouquet. Bouquet formation is hypothesized to facilitate homologous chromosome pairing. In fission yeast, bouquet formation and telomere clustering occurs in karyogamy and persists throughout the horsetail stage. Here we report the isolation and characterization of six mutants from our screen for meiotic mutants. These mutants show defective telomere clustering as demonstrated by mislocalization of Swi6::GFP, a heterochromatin-binding protein, and Taz1p::GFP, a telomere-specific protein. These mutants define four complementation groups and are named dot1 to dot4-defective organization of telomeres. dot3 and dot4 are allelic to mat1-Mm and mei4, respectively. Immunolocalization of Sad1, a protein associated with the spindle pole body (SPB), in dot mutants showed an elevated frequency of multiple Sad1-nuclei signals relative to wild type. Many of these Sad1 foci were colocalized with Taz1::GFP. Impaired SPB structure and function were further demonstrated by failure of spore wall formation in dot1, by multiple Pcp1::GFP signals (an SPB component) in dot2, and by abnormal microtubule organizations during meiosis in dot mutants. The coincidence of impaired SPB functions with defective telomere clustering suggests a link between the SPB and the telomere cluster.","authors":"Jin Y, Uzawa S, Cande WZ","authors_abbrev":"Jin Y et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-20","publication_year":"2002","canto_session_key":"8fa55d6ed8dab65f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-09 16:15:08","canto_approved_date":"2025-12-31 11:39:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-21 08:12:17","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.06c","SPBC651.05c","SPBC23G7.17c","SPBC32H8.11"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-03-09"},{"uniquename":"PMID:30397101","title":"mRNA decapping: finding the right structures.","citation":"Philos Trans R Soc Lond B Biol Sci 2018 Nov 05;373(1762)","abstract":"In eukaryotes, the elimination of the m 7 GpppN mRNA cap, a process known as decapping, is a critical, largely irreversible and highly regulated step of mRNA decay that withdraws the targeted mRNAs from the pool of translatable templates. The decapping reaction is catalysed by a multi-protein complex formed by the Dcp2 catalytic subunit and its Dcp1 cofactor, a holoenzyme that is poorly active on its own and needs several accessory proteins (Lsm1-7 complex, Pat1, Edc1-2, Edc3 and/or EDC4) to be fully efficient. Here, we discuss the several crystal structures of Dcp2 domains bound to various partners (proteins or small molecules) determined in the last couple of years that have considerably improved our current understanding of how Dcp2, assisted by its various activators, is recruited to its mRNA targets and adopts its active conformation upon substrate recognition. We also describe how, over the years, elegant integrative structural biology approaches combined to biochemistry and genetics led to the identification of the correct structure of the active Dcp1-Dcp2 holoenzyme among the many available conformations trapped by X-ray crystallography.This article is part of the theme issue '5' and 3' modifications controlling RNA degradation'.","doi":"10.1098/rstb.2018.0164","authors":"Charenton C, Graille M","authors_abbrev":"Charenton C et al.","pubmed_publication_date":"05 Nov 2018","pubmed_entrez_date":"2018-11-07","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-08-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15972456","title":"Brc1-mediated DNA repair and damage tolerance.","citation":"Genetics 2005 Oct;171(2):457-68","abstract":"The structural maintenance of chromosome (SMC) proteins are key elements in controlling chromosome dynamics. In eukaryotic cells, three essential SMC complexes have been defined: cohesin, condensin, and the Smc5/6 complex. The latter is essential for DNA damage responses; in its absence both repair and checkpoint responses fail. In fission yeast, the UV-C and ionizing radiation (IR) sensitivity of a specific hypomorphic allele encoding the Smc6 subunit, rad18-74 (renamed smc6-74), is suppressed by mild overexpression of a six-BRCT-domain protein, Brc1. Deletion of brc1 does not result in a hypersensitivity to UV-C or IR, and thus the function of Brc1 relative to the Smc5/6 complex has remained unclear. Here we show that brc1Delta cells are hypersensitive to a range of radiomimetic drugs that share the feature of creating lesions that are an impediment to the completion of DNA replication. Through a genetic analysis of brc1Delta epistasis and by defining genes required for Brc1 to suppress smc6-74, we find that Brc1 functions to promote recombination through a novel postreplication repair pathway and the structure-specific nucleases Slx1 and Mus81. Activation of this pathway through overproduction of Brc1 bypasses a repair defect in smc6-74, reestablishing resolution of lesions by recombination.","authors":"Sheedy DM, Dimitrova D, Rankin JK, Bass KL, Lee KM, Tapia-Alveal C, Harvey SH, Murray JM, O'Connell MJ","authors_abbrev":"Sheedy DM et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-06-24","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.11","SPBC582.05c","SPCC4G3.05c","SPBC1734.06","SPCC5E4.06","SPAC15A10.03c","SPAC2G11.12","SPAC664.07c","SPAC688.10","SPBC409.03","SPCC553.07c","SPAP27G11.15","SPAC20H4.07","SPAC14C4.13"],"gene_count":14,"ltp_gene_count":14},{"uniquename":"PMID:17677136","title":"Controllability analysis of networks.","citation":"Phys Rev E Stat Nonlin Soft Matter Phys 2007 May;75(5 Pt 2):056110","abstract":"The concept of controllability of linear systems from control theory is applied to networks inspired by biology. A node is in this context controllable if an external signal can be applied which can adjust the level (e.g., protein concentration) of the node in a finite time to an arbitrary value, regardless of the levels of the other nodes. The property of being downstream of the node to which the input is applied turns out to be a necessary but not a sufficient condition for being controllable. An interpretation of the controllability matrix, when applied to networks, is also given. Finally, two case studies are provided in order to better explain the concepts, as well as some results for a gene regulatory network of fission yeast.","authors":"Lombardi A, Hörnquist M","authors_abbrev":"Lombardi A et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-08-07","publication_year":"2007","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2115995","title":"Novel YPT1-related genes from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1990 Jul 25;18(14):4264","abstract":"","authors":"Fawell E, Hook S, Sweet D, Armstrong J","authors_abbrev":"Fawell E et al.","pubmed_publication_date":"25 Jul 1990","pubmed_entrez_date":"1990-07-25","publication_year":"1990","canto_session_key":"565cab88619a7411","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 14:19:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-28 14:19:11","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-01-28"},{"uniquename":"PMID:12689592","title":"Kinetochore recruitment of two nucleolar proteins is required for homolog segregation in meiosis I.","citation":"Dev Cell 2003 Apr;4(4):535-48","abstract":"Halving of the chromosome number during meiosis I depends on the segregation of maternal and paternal centromeres. This process relies on the attachment of sister centromeres to microtubules emanating from the same spindle pole. We describe here the identification of a protein complex, Csm1/Lrs4, that is essential for monoorientation of sister kinetochores in Saccharomyces cerevisiae. Both proteins are present in vegetative cells, where they reside in the nucleolus. Only shortly before meiosis I do they leave the nucleolus and form a \"monopolin\" complex with the meiosis-specific Mam1 protein, which binds to kinetochores. Surprisingly, Csm1's homolog in Schizosaccharomyces pombe, Pcs1, is essential for accurate chromosome segregation during mitosis and meiosis II. Csm1 and Pcs1 might clamp together microtubule binding sites on the same (Pcs1) or sister (Csm1) kinetochores.","authors":"Rabitsch KP, Petronczki M, Javerzat JP, Genier S, Chwalla B, Schleiffer A, Tanaka TU, Nasmyth K","authors_abbrev":"Rabitsch KP et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-04-12","publication_year":"2003","canto_session_key":"c955c8aac38b4df8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-04-23 15:23:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-12 17:20:28","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-12"},{"uniquename":"PMID:20850323","title":"A catalytic role for Mod5 in the formation of the Tea1 cell polarity landmark.","citation":"Curr Biol 2010 Oct 12;20(19):1752-7","abstract":"Many systems regulating cell polarity involve stable landmarks defined by internal cues. In the rod-shaped fission yeast Schizosaccharomyces pombe, microtubules regulate polarized vegetative growth via a landmark involving the protein Tea1. Tea1 is delivered to cell tips as packets of molecules associated with growing microtubule ends and anchored at the plasma membrane via a mechanism involving interaction with the membrane protein Mod5. Tea1 and Mod5 are highly concentrated in clusters at cell tips in a mutually dependent manner, but how the Tea1-Mod5 interaction contributes mechanistically to generating a stable landmark is not understood. Here, we use live-cell imaging, FRAP, and computational modeling to dissect dynamics of the Tea1-Mod5 interaction. Surprisingly, we find that Tea1 and Mod5 exhibit distinctly different turnover rates at cell tips. Our data and modeling suggest that rather than acting simply as a Tea1 receptor or as a molecular \"glue\" to retain Tea1, Mod5 functions catalytically to stimulate incorporation of Tea1 into a stable tip-associated cluster network. The model also suggests an emergent self-focusing property of the Tea1-Mod5 cluster network, which can increase the fidelity of polarized growth.","doi":"10.1016/j.cub.2010.08.035","authors":"Bicho CC, Kelly DA, Snaith HA, Goryachev AB, Sawin KE","authors_abbrev":"Bicho CC et al.","pubmed_publication_date":"12 Oct 2010","pubmed_entrez_date":"2010-09-21","publication_year":"2010","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPBC530.04","SPCC1223.06"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23644205","title":"N-alkylated 2,3,3-trimethylindolenines and 2-methylbenzothiazoles. Potential lead compounds in the fight against Saccharomyces cerevisiae infections.","citation":"Eur J Med Chem 2013 Jun;64:222-7","abstract":"The synthesis of a variety of N-alkylated 2,3,3-trimethylindolenines and 2-methylbenzothiazoles is reported herein. Their potential as antifungal agents is evaluated by preliminary screening against Saccharomyces cerevisiae (S. cerevisiae), Schizosaccharomyces pombe (S. pombe), and Candida albicans (C. albicans). Statistical analyses illustrate a strong relationship between chain length and growth inhibition for S. cerevisiae and S. pombe (p < 0.0001 in every case). Of particular interest is the activity of both sets of compounds against S. cerevisiae, as this is emerging as an opportunistic pathogen, especially in immunosuppressed and immunocompromised patients. Bioassays were set up to compare the efficacy of our range of N-alkylated compounds against classic antifungal agents; Amphotericin B and Thiabendazole.","doi":"10.1016/j.ejmech.2013.03.031","authors":"Tyler AR, Okoh AO, Lawrence CL, Jones VC, Moffatt C, Smith RB","authors_abbrev":"Tyler AR et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-05-07","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35812747","title":"Adaptive Control of the Meiotic Recombination Landscape by DNA Site-dependent Hotspots With Implications for Evolution.","citation":"Front Genet 2022;13:947572","abstract":"Meiosis is an essential component of the sexual life cycle in eukaryotes. The independent assortment of chromosomes in meiosis increases genetic diversity at the level of whole chromosomes and meiotic recombination increases genetic diversity within chromosomes. The resulting variability fuels evolution. Interestingly, global mapping of recombination in diverse taxa revealed dramatic changes in its frequency distribution between closely related species, subspecies, and even isolated populations of the same species. New insight into mechanisms for these evolutionarily rapid changes has come from analyses of environmentally induced plasticity of recombination in fission yeast. Many different DNA sites, and where identified their binding/activator proteins, control the positioning of recombination at hotspots. Each different class of hotspots functions as an independently controlled rheostat that modulates rates of recombination over a broad dynamic range in response to changing conditions. Together, this independent modulation can rapidly and dramatically alter the global frequency distribution of recombination. This process likely contributes substantially to (i.e., can largely explain) evolutionarily rapid, Prdm9-independent changes in the recombination landscape. Moreover, the precise control mechanisms allow cells to dynamically favor or disfavor newly arising combinations of linked alleles in response to changing extracellular and intracellular conditions, which has striking implications for the impacts of meiotic recombination on evolution.","doi":"10.3389/fgene.2022.947572","authors":"Protacio RU, Davidson MK, Wahls WP","authors_abbrev":"Protacio RU et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-07-11","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-07-13 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26292707","title":"Structure of a yeast spliceosome at 3.6-angstrom resolution.","citation":"Science 2015 Sep 11;349(6253):1182-91","abstract":"Splicing of precursor messenger RNA (pre-mRNA) in yeast is executed by the spliceosome, which consists of five small nuclear ribonucleoproteins (snRNPs), NTC (nineteen complex), NTC-related proteins (NTR), and a number of associated enzymes and cofactors. Here, we report the three-dimensional structure of a Schizosaccharomyces pombe spliceosome at 3.6-angstrom resolution, revealed by means of single-particle cryogenic electron microscopy. This spliceosome contains U2 and U5 snRNPs, NTC, NTR, U6 small nuclear RNA, and an RNA intron lariat. The atomic model includes 10,574 amino acids from 37 proteins and four RNA molecules, with a combined molecular mass of approximately 1.3 megadaltons. Spp42 (Prp8 in Saccharomyces cerevisiae), the key protein component of the U5 snRNP, forms a central scaffold and anchors the catalytic center. Both the morphology and the placement of protein components appear to have evolved to facilitate the dynamic process of pre-mRNA splicing. Our near-atomic-resolution structure of a central spliceosome provides a molecular framework for mechanistic understanding of pre-mRNA splicing.","doi":"10.1126/science.aac7629","authors":"Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y","authors_abbrev":"Yan C et al.","pubmed_publication_date":"11 Sep 2015","pubmed_entrez_date":"2015-08-22","publication_year":"2015","canto_session_key":"4ea2330bedd1d568","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-22 14:12:53","canto_approved_date":"2023-02-23 14:18:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-22 14:07:09","canto_added_date":"2015-08-23 00:18:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":44,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.07c","SPBC31F10.11c","SPAC29A4.08c","SPSNRNA.02","SPAC2F3.17c","SPBC30D10.06","SPBC28F2.04c","SPAC3A12.11c","SPBC337.06c","SPBC8D2.09c","SPAC30D11.09","SPBC24C6.11","SPBC215.12","SPBC3E7.14","SPBC4B4.05","SPAC26A3.08","SPAC644.12","SPBC1289.11","SPCC285.12","SPBP22H7.07","SPBC1861.08c","SPBC211.02c","SPBC6B1.10","SPAC2C4.03c","SPCC550.02c","SPSNRNA.05","SPBC9B6.05c","SPBC20F10.09","SPBC19C2.14","SPAC57A10.03","SPBC646.02","SPCC188.11","SPCC1620.01c","SPAC4F8.12c","SPCC1840.10","SPBC11G11.06c"],"gene_count":36,"ltp_gene_count":36,"approved_date":"2023-02-22","pdb_entries":[{"pdb_id":"3jb9","gene_chains":[{"gene_uniquename":"SPBP22H7.07","chain":"K","position":"149-473"},{"gene_uniquename":"SPAC29A4.08c","chain":"S/T/U/V","position":"1-488"},{"gene_uniquename":"SPAC2C4.03c","chain":"G/l","position":"1-115"},{"gene_uniquename":"SPAC4F8.12c","chain":"A","position":"1-2363"},{"gene_uniquename":"SPAC27D7.07c","chain":"F/f","position":"1-117"},{"gene_uniquename":"SPBC6B1.10","chain":"g","position":"1-558"},{"gene_uniquename":"SPBC3E7.14","chain":"I/n","position":"1-78"},{"gene_uniquename":"SPCC550.02c","chain":"a","position":"1-285"},{"gene_uniquename":"SPBC24C6.11","chain":"e","position":"1-146"},{"gene_uniquename":"SPBC4B4.05","chain":"J/o","position":"1-77"},{"gene_uniquename":"SPBC215.12","chain":"B","position":"1-984"},{"gene_uniquename":"SPBC646.02","chain":"X","position":"1-1284"},{"gene_uniquename":"SPBC1289.11","chain":"L","position":"1-340"},{"gene_uniquename":"SPAC644.12","chain":"W","position":"1-757"},{"gene_uniquename":"SPBC337.06c","chain":"h","position":"1-265"},{"gene_uniquename":"SPAC57A10.03","chain":"d","position":"1-155"},{"gene_uniquename":"SPAC3A12.11c","chain":"Y","position":"1-289"},{"gene_uniquename":"SPBC31F10.11c","chain":"R","position":"41-290"},{"gene_uniquename":"SPCC188.11","chain":"M","position":"1-557"},{"gene_uniquename":"SPAC30D11.09","chain":"c","position":"1-639"},{"gene_uniquename":"SPAC26A3.08","chain":"E/b","position":"1-147"},{"gene_uniquename":"SPBC8D2.09c","chain":"k","position":"1-111"},{"gene_uniquename":"SPBC211.02c","chain":"r","position":"498-653"},{"gene_uniquename":"SPBC28F2.04c","chain":"i","position":"1-187"},{"gene_uniquename":"SPBC1861.08c","chain":"j","position":"1-237"},{"gene_uniquename":"SPBC11G11.06c","chain":"H/m","position":"1-84"},{"gene_uniquename":"SPBC19C2.14","chain":"D/Z","position":"1-97"}],"title":"Cryo-EM structure of the yeast spliceosome at 3.6 angstrom resolution","entry_authors":"Yan C,Hang J,Wan R,Huang M,Wong C,Shi Y","entry_authors_abbrev":"Yan C et al.","reference_uniquename":"PMID:26292707","experimental_method":"EM","resolution":"3.6"}]},{"uniquename":"PMID:28965846","title":"FDXR Mutations Cause Sensorial Neuropathies and Expand the Spectrum of Mitochondrial Fe-S-Synthesis Diseases.","citation":"Am J Hum Genet 2017 Oct 05;101(4):630-637","abstract":"Hearing loss and visual impairment in childhood have mostly genetic origins, some of them being related to sensorial neuronal defects. Here, we report on eight subjects from four independent families affected by auditory neuropathy and optic atrophy. Whole-exome sequencing revealed biallelic mutations in FDXR in affected subjects of each family. FDXR encodes the mitochondrial ferredoxin reductase, the sole human ferredoxin reductase implicated in the biosynthesis of iron-sulfur clusters (ISCs) and in heme formation. ISC proteins are involved in enzymatic catalysis, gene expression, and DNA replication and repair. We observed deregulated iron homeostasis in FDXR mutant fibroblasts and indirect evidence of mitochondrial iron overload. Functional complementation in a yeast strain in which ARH1, the human FDXR ortholog, was deleted established the pathogenicity of these mutations. These data highlight the wide clinical heterogeneity of mitochondrial disorders related to ISC synthesis.","doi":"10.1016/j.ajhg.2017.09.007","authors":"Paul A, Drecourt A, Petit F, Deguine DD, Vasnier C, Oufadem M, Masson C, Bonnet C, Masmoudi S, Mosnier I, Mahieu L, Bouccara D, Kaplan J, Challe G, Domange C, Mochel F, Sterkers O, Gerber S, Nitschke P, Bole-Feysot C, Jonard L, Gherbi S, Mercati O, Ben Aissa I, Lyonnet S, Rötig A, Delahodde A, Marlin S","authors_abbrev":"Paul A et al.","pubmed_publication_date":"05 Oct 2017","pubmed_entrez_date":"2017-10-03","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3B8.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26345368","title":"A new phosphate-starvation response in fission yeast requires the endocytic function of myosin I.","citation":"J Cell Sci 2015 Oct 15;128(20):3707-13","abstract":"Endocytosis is essential for uptake of many substances into the cell, but how it links to nutritional signalling is poorly understood. Here, we show a new role for endocytosis in regulating the response to low phosphate in Schizosaccharomyces pombe. Loss of function of myosin I (Myo1), Sla2/End4 or Arp2, proteins involved in the early steps of endocytosis, led to increased proliferation in low-phosphate medium compared to controls. We show that once cells are deprived of phosphate they undergo a quiescence response that is dependent on the endocytic function of Myo1. Transcriptomic analysis revealed a wide perturbation of gene expression with induction of stress-regulated genes upon phosphate starvation in wild-type but not Δmyo1 cells. Thus, endocytosis plays a pivotal role in mediating the cellular response to nutrients, bridging the external environment and internal molecular functions of the cell.","doi":"10.1242/jcs.171314","authors":"Petrini E, Baillet V, Cridge J, Hogan CJ, Guillaume C, Ke H, Brandetti E, Walker S, Koohy H, Spivakov M, Varga-Weisz P","authors_abbrev":"Petrini E et al.","pubmed_publication_date":"15 Oct 2015","pubmed_entrez_date":"2015-09-09","publication_year":"2015","canto_session_key":"897ea00b9e24c756","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Edoardo Petrini","canto_first_approved_date":"2015-11-04 10:26:02","canto_approved_date":"2021-12-18 20:14:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-12 14:47:09","canto_added_date":"2015-09-10 00:19:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Edoardo Petrini","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.13c","SPBC405.04c","SPAC11H11.06","SPAC688.11","SPAC23D3.10c","SPBC119.05c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-11-04"},{"uniquename":"PMID:38815580","title":"RNA quality control factors nucleate Clr4/SUV39H and trigger constitutive heterochromatin assembly.","citation":"Cell 2024 May 21;","abstract":"In eukaryotes, the Suv39 family of proteins tri-methylate lysine 9 of histone H3 (H3K9me) to form constitutive heterochromatin. However, how Suv39 proteins are nucleated at heterochromatin is not fully described. In the fission yeast, current models posit that Argonaute1-associated small RNAs (sRNAs) nucleate the sole H3K9 methyltransferase, Clr4/SUV39H, to centromeres. Here, we show that in the absence of all sRNAs and H3K9me, the Mtl1 and Red1 core (MTREC)/PAXT complex nucleates Clr4/SUV39H at a heterochromatic long noncoding RNA (lncRNA) at which the two H3K9 deacetylases, Sir2 and Clr3, also accumulate by distinct mechanisms. Iterative cycles of H3K9 deacetylation and methylation spread Clr4/SUV39H from the nucleation center in an sRNA-independent manner, generating a basal H3K9me state. This is acted upon by the RNAi machinery to augment and amplify the Clr4/H3K9me signal at centromeres to establish heterochromatin. Overall, our data reveal that lncRNAs and RNA quality control factors can nucleate heterochromatin and function as epigenetic silencers in eukaryotes.","doi":"10.1016/j.cell.2024.04.042","authors":"Khanduja JS, Joh RI, Perez MM, Paulo JA, Palmieri CM, Zhang J, Gulka AOD, Haas W, Gygi SP, Motamedi M","authors_abbrev":"Khanduja JS et al.","pubmed_publication_date":"21 May 2024","pubmed_entrez_date":"2024-05-30","publication_year":"2024","canto_session_key":"6cb07f1af6a7ef7d","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_session_submitted_date":"2025-08-11 16:09:53","canto_added_date":"2024-05-31 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.07c","SPBC800.03","SPAC17H9.02","SPNCRNA.230"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:21072667","title":"hsf1 (+) extends chronological lifespan through Ecl1 family genes in fission yeast.","citation":"Mol Genet Genomics 2011 Jan;285(1):67-77","abstract":"The heat shock factor (HSF), a protein evolutionarily conserved from yeasts to human, regulates the expression of a set of proteins called heat shock proteins (HSPs), many of which function as molecular chaperones. In Saccharomyces cerevisiae, the HSF binds to the 5' upstream region of YGR146C and activates its transcription. YGR146C encodes a functional homolog of ecl1 (+), ecl2 (+), and ecl3 (+) of Schizosaccharomyces pombe. At present, these Ecl1 family genes, which are extenders of chronological lifespan, have been identified only in fungi groups. Based on ChIP analysis, we identified that Hsf1 binds to the upstream DNA region of ecl2 (+) after heat shock in S. pombe. In Caenorhabditis elegans, heat shock factor HSF-1 is known to regulate aging and required for the elongation of longevity by dietary restriction. We found that heat shock factor Hsf1 extends chronological lifespan of S. pombe when overexpressed. Moreover, we show that the extension of chronological lifespan by the overproduction of Hsf1 mainly depends on ecl2 (+) among Ecl1 family genes. From these results, we suggest that HSF is a conserved regulator of lifespan, at least in yeast and nematode, and Ecl1 family genes such as YGR146C and ecl2 (+) are the direct targets of Hsf1 and mediate lifespan extension by Hsf1.","doi":"10.1007/s00438-010-0588-6","authors":"Ohtsuka H, Azuma K, Murakami H, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-11-13","publication_year":"2011","canto_session_key":"f879af6f6b293ac8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-10 17:30:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-13 15:11:46","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8E4.12c","SPAC664.11","SPBP35G2.16c","SPAC2E12.02","SPCC70.12c","SPBC32C12.02"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2015-04-13"},{"uniquename":"PMID:10207182","title":"Novel Schizosaccharomyces pombe N-linked GalMan9GlcNAc isomers: role of the Golgi GMA12 galactosyltransferase in core glycan galactosylation.","citation":"Glycobiology 1999 May;9(5):497-505","abstract":"Schizosaccharomyces pombe synthesizes very large N-linked galactomannans, which are elongated from the Man9GlcNAc2 core that remains after the trimming of three Glc residues from the Glc3Man9GlcNAc2 originally transferred from dolichyl pyrophosphate to nascent proteins in the endoplasmic reticulum. Prior to elongation of the galactomannan outer chain, the Man9GlcNAc2 core is modified into a family of Hex10-15GlcNAc2 structures by the addition of both Gal and Man residues (Ziegler et al. (1994) J. Biol. Chem., 269, 12527-12535). To understand the pathway of Man9GlcNAc2 modification, the Hex10GlcNAc-sized pool was isolated by Bio-Gel P-4 gel filtration from the endo H-released N-glycans of S.pombe glycoproteins. This pool yielded four major fractions, a, b, c, and g, on preparative high pH, anion exchange chromatography, that represented 10, 29, 46, and 13% of the total Hex10GlcNAc present, respectively. Structures of the glycan isomers present in each fraction were determined by one- and two-dimensional 1H NMR spectroscopy techniques. Fraction a is principally (approximately 93%) a Man10GlcNAc with a new alpha1,2-linked Man cap on the upper-arm of Man9GlcNAc. Fraction b contained two isomers of GalMan9GlcNAc in which an alpha1,2-linked terminal Gal had been added either to the upper (b1, 30%) or middle-arm (b2, 70%) of Man9GlcNAc. The gma12 - alpha1,2-galactosyltransferase-negative S. pombe strain (Chappell et al. (1994) Mol. Biol. Cell., 5, 519-528) did not make fraction b implying that the gma12p galactosyltransferase is responsible for synthesis of both isomers b1 and b2. Isomer c is Man10GlcNAc in which a new branching alpha1, 6-linked Man had been added to the lower-arm alpha1,3-linked core residue as found earlier in Saccharomyces cerevisiae and Pichia pastoris. Fraction g had less than molar stoichiometry of both Gal and Glc. The major isomer (g1, 85%) is the Man9GlcNAc core with an alpha1,3-linked branching Gal on the penultimate 2-O-substituted Man of the lower arm. This residue is also found on a novel O-linked oligosaccharide recently described in S.pombe; Manalpha1,2(Galalpha1, 3)Manalpha1,2Mannitol (Gemmill and Trimble (1999) Glycobiology, 9, 507-515). The second isomer (g2, 15%) is the partially processed Glc2Man9GlcNAc intermediate. Defining these Hex10GlcNAc structures provides a starting point for understanding the enzymology of N-linked galactomannan core heterogeneity seen on S.pombe glycoproteins.","authors":"Ziegler FD, Cavanagh J, Lubowski C, Trimble RB","authors_abbrev":"Ziegler FD et al.","pubmed_publication_date":"May 1999","pubmed_entrez_date":"1999-04-20","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40254064","title":"Global analysis of protein and small-molecule substrates of ubiquitin-like proteins (UBLs).","citation":"Mol Cell Proteomics 2025 Apr 18;:100975","abstract":"Ubiquitin-like proteins (UBLs) constitute a family of evolutionarily conserved proteins that share similarities with ubiquitin in 3D structures and modification mechanisms. For most UBLs including Small-Ubiquitin-like Modifiers (SUMO), their modification sites on substrate proteins cannot be identified using the mass spectrometry-based method that has been successful for identifying ubiquitination sites, unless a UBL protein is mutated accordingly. To identify UBL modification sites without having to mutate UBL, we have developed a dedicated search engine pLink-UBL on the basis of pLink, a software tool for identification of cross-linked peptide pairs. pLink-UBL exhibited superior precision, sensitivity, and speed than \"make-do\" search engines such as MaxQuant, pFind, and pLink. For example, compared to MaxQuant, pLink-UBL increased the number of identified SUMOylation sites by 50 ∼ 300% from the same datasets. Additionally, we present a method for identifying small-molecule modifications of UBLs. This method involves antibody enrichment of a UBL C-terminal peptide following enrichment of a UBL protein, followed by LC-MS/MS analysis and a pFind 3 blind search to identify unexpected modifications. Using this method, we have discovered non-protein substrates of SUMO, of which spermidine is the major one for fission yeast SUMO Pmt3. Spermidine can be conjugated to the C-terminal carboxylate group of Pmt3 through its N 1  or also likely, N 8  amino group in the presence of SUMO E1, E2, and ATP. Pmt3-spermidine conjugation does not require E3 and can be reversed by SUMO isopeptidase Ulp1. SUMO-spermidine conjugation is present in mice and humans. Also, spermidine can be conjugated to ubiquitin in vitro by E1 and E2 in the presence of ATP. The above observations suggest that spermidine may be a common small molecule substrate of SUMO and possibly ubiquitin across eukaryotic species.","doi":"10.1016/j.mcpro.2025.100975","authors":"Shao GC, Chen ZL, Lu S, Wu QC, Sheng Y, Wang J, Ma Y, Sui JH, Chi H, Qi XB, He SM, Du LL, Dong MQ","authors_abbrev":"Shao GC et al.","pubmed_publication_date":"18 Apr 2025","pubmed_entrez_date":"2025-04-20","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-04-21 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27026703","title":"The Structure of the Complex between Yeast Frataxin and Ferrochelatase: CHARACTERIZATION AND PRE-STEADY STATE REACTION OF FERROUS IRON DELIVERY AND HEME SYNTHESIS.","citation":"J Biol Chem 2016 May 27;291(22):11887-98","abstract":"Frataxin is a mitochondrial iron-binding protein involved in iron storage, detoxification, and delivery for iron sulfur-cluster assembly and heme biosynthesis. The ability of frataxin from different organisms to populate multiple oligomeric states in the presence of metal ions, e.g. Fe(2+) and Co(2+), led to the suggestion that different oligomers contribute to the functions of frataxin. Here we report on the complex between yeast frataxin and ferrochelatase, the terminal enzyme of heme biosynthesis. Protein-protein docking and cross-linking in combination with mass spectroscopic analysis and single-particle reconstruction from negatively stained electron microscopic images were used to verify the Yfh1-ferrochelatase interactions. The model of the complex indicates that at the 2:1 Fe(2+)-to-protein ratio, when Yfh1 populates a trimeric state, there are two interaction interfaces between frataxin and the ferrochelatase dimer. Each interaction site involves one ferrochelatase monomer and one frataxin trimer, with conserved polar and charged amino acids of the two proteins positioned at hydrogen-bonding distances from each other. One of the subunits of the Yfh1 trimer interacts extensively with one subunit of the ferrochelatase dimer, contributing to the stability of the complex, whereas another trimer subunit is positioned for Fe(2+) delivery. Single-turnover stopped-flow kinetics experiments demonstrate that increased rates of heme production result from monomers, dimers, and trimers, indicating that these forms are most efficient in delivering Fe(2+) to ferrochelatase and sustaining porphyrin metalation. Furthermore, they support the proposal that frataxin-mediated delivery of this potentially toxic substrate overcomes formation of reactive oxygen species.","doi":"10.1074/jbc.M115.701128","authors":"Söderberg C, Gillam ME, Ahlgren EC, Hunter GA, Gakh O, Isaya G, Ferreira GC, Al-Karadaghi S","authors_abbrev":"Söderberg C et al.","pubmed_publication_date":"27 May 2016","pubmed_entrez_date":"2016-03-31","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1183.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37887293","title":"Thirty Years with ERH: An mRNA Splicing and Mitosis Factor Only or Rather a Novel Genome Integrity Protector?","citation":"Cells 2023 Oct 13;12(20)","abstract":"ERH is a 100 to about 110 aa nuclear protein with unique primary and three-dimensional structures that are very conserved from simple eukaryotes to humans, albeit some species have lost its gene, with most higher fungi being a noteworthy example. Initially, studies on  Drosophila melanogaster  implied its function in pyrimidine metabolism. Subsequently, research on  Xenopus laevis  suggested that it acts as a transcriptional repressor. Finally, studies in humans pointed to a role in pre-mRNA splicing and in mitosis but further research, also in  Caenorhabditis elegans  and  Schizosaccharomyces pombe,  demonstrated its much broader activity, namely involvement in the biogenesis of mRNA, and miRNA, piRNA and some other ncRNAs, and in repressive heterochromatin formation. ERH interacts with numerous, mostly taxon-specific proteins, like Mmi1 and Mei2 in  S. pombe , PID-3/PICS-1, TOST-1 and PID-1 in  C. elegans , and DGCR8, CIZ1, PDIP46/SKAR and SAFB1/2 in humans. There are, however, some common themes in this wide range of processes and partners, such as: (a) ERH homodimerizes to form a scaffold for several complexes involved in the metabolism of nucleic acids, (b) all these RNAs are RNA polymerase II transcripts, (c) pre-mRNAs, whose splicing depends on ERH, are enriched in transcripts of DNA damage response and DNA metabolism genes, and (d) heterochromatin is formed to silence unwanted transcription, e.g., from repetitive elements. Thus, it seems that ERH has been adopted for various pathways that serve to maintain genome integrity.","doi":"10.3390/cells12202449","authors":"Kozlowski P","authors_abbrev":"Kozlowski P","pubmed_publication_date":"13 Oct 2023","pubmed_entrez_date":"2023-10-27","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-10-27 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16849602","title":"Regulation of DNA replication machinery by Mrc1 in fission yeast.","citation":"Genetics 2006 Sep;174(1):155-65","abstract":"Faithful replication of chromosomes is crucial to genome integrity. In yeast, the ORC binds replication origins throughout the cell cycle. However, Cdc45 binds these before S-phase, and, during replication, it moves along the DNA with MCM helicase. When replication progression is inhibited, checkpoint regulation is believed to stabilize the replication fork; the detailed mechanism, however, remains unclear. To examine the relationship between replication initiation and elongation defects and the response to replication elongation block, we used fission yeast mutants of Orc1 and Cdc45--orp1-4 and sna41-928, respectively--at their respective semipermissive temperatures with regard to BrdU incorporation. Both orp1 and sna41 cells exhibited HU hypersensitivity in the absence of Chk1, a DNA damage checkpoint kinase, and were defective in full activation of Cds1, a replication checkpoint kinase, indicating that normal replication is required for Cds1 activation. Mrc1 is required to activate Cds1 and prevent the replication machinery from uncoupling from DNA synthesis. We observed that, while either the orp1 or the sna41 mutation partially suppressed HU sensitivity of cds1 cells, sna41 specifically suppressed that of mrc1 cells. Interestingly, sna41 alleviated the defect in recovery from HU arrest without increasing Cds1 activity. In addition to sna41, specific mutations of MCM suppressed the HU sensitivity of mrc1 cells. Thus, during elongation, Mrc1 may negatively regulate Cdc45 and MCM helicase to render stalled forks capable of resuming replication.","authors":"Nitani N, Nakamura K, Nakagawa C, Masukata H, Nakagawa T","authors_abbrev":"Nitani N et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-07-20","publication_year":"2006","canto_session_key":"fcc116682c80b4f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-01-20 11:06:52","canto_approved_date":"2021-12-15 21:39:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-21 13:33:32","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":33,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPCC1259.13","SPCC18B5.11c","SPAC17D4.02","SPBC4.04c","SPAC694.06c","SPCC18B5.03","SPBC29A10.15"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2016-01-20"},{"uniquename":"EMBL:AJ577640","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.33"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25417108","title":"Dicer promotes transcription termination at sites of replication stress to maintain genome stability.","citation":"Cell 2014 Oct 23;159(3):572-83","abstract":"Nuclear RNAi is an important regulator of transcription and epigenetic modification, but the underlying mechanisms remain elusive. Using a genome-wide approach in the fission yeast S. pombe, we have found that Dcr1, but not other components of the canonical RNAi pathway, promotes the release of Pol II from the 3? end of highly transcribed genes, and, surprisingly, from antisense transcription of rRNA and tRNA genes, which are normally transcribed by Pol I and Pol III. These Dcr1-terminated loci correspond to sites of replication stress and DNA damage, likely resulting from transcription-replication collisions. At the rDNA loci, release of Pol II facilitates DNA replication and prevents homologous recombination, which would otherwise lead to loss of rDNA repeats especially during meiosis. Our results reveal a novel role for Dcr1-mediated transcription termination in genome maintenance and may account for widespread regulation of genome stability by nuclear RNAi in higher eukaryotes.","doi":"10.1016/j.cell.2014.09.031","authors":"Castel SE, Ren J, Bhattacharjee S, Chang AY, Sánchez M, Valbuena A, Antequera F, Martienssen RA","authors_abbrev":"Castel SE et al.","pubmed_publication_date":"23 Oct 2014","pubmed_entrez_date":"2014-11-24","publication_year":"2014","canto_session_key":"3c804802186d667e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rob Martienssen","canto_first_approved_date":"2016-03-29 13:22:17","canto_approved_date":"2024-02-12 14:20:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-03 08:35:49","canto_added_date":"2014-11-26 01:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Rob Martienssen","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.09c","SPCC188.13c","SPCC736.11","SPBC342.05","SPBC887.14c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2016-03-29"},{"uniquename":"Pfam:PF15055","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:30536","SPAC1F7.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28199302","title":"Untimely expression of gametogenic genes in vegetative cells causes uniparental disomy.","citation":"Nature 2017 Mar 02;543(7643):126-130","abstract":"Uniparental disomy (UPD), in which an individual contains a pair of homologous chromosomes originating from only one parent, is a frequent phenomenon that is linked to congenital disorders and various cancers. UPD is thought to result mostly from pre- or post-zygotic chromosome missegregation. However, the factors that drive UPD remain unknown. Here we use the fission yeast Schizosaccharomyces pombe as a model to investigate UPD, and show that defects in the RNA interference (RNAi) machinery or in the YTH domain-containing RNA elimination factor Mmi1 cause high levels of UPD in vegetative diploid cells. This phenomenon is not due to defects in heterochromatin assembly at centromeres. Notably, in cells lacking RNAi components or Mmi1, UPD is associated with the untimely expression of gametogenic genes. Deletion of the upregulated gene encoding the meiotic cohesin Rec8 or the cyclin Crs1 suppresses UPD in both RNAi and mmi1 mutants. Moreover, overexpression of Rec8 is sufficient to trigger UPD in wild-type cells. Rec8 expressed in vegetative cells localizes to chromosomal arms and to the centromere core, where it is required for localization of the cohesin subunit Psc3. The centromeric localization of Rec8 and Psc3 promotes UPD by uniquely affecting chromosome segregation, causing a reductional segregation of one homologue. Together, these findings establish the untimely vegetative expression of gametogenic genes as a causative factor of UPD, and provide a solid foundation for understanding this phenomenon, which is linked to diverse human diseases.","doi":"10.1038/nature21372","authors":"Folco HD, Chalamcharla VR, Sugiyama T, Thillainadesan G, Zofall M, Balachandran V, Dhakshnamoorthy J, Mizuguchi T, Grewal SI","authors_abbrev":"Folco HD et al.","pubmed_publication_date":"02 Mar 2017","pubmed_entrez_date":"2017-02-16","publication_year":"2017","canto_session_key":"a6e39e4720b35ebf","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-17 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15A10.15","SPCC188.13c","SPAC17H9.20","SPCC736.12c","SPBC2G2.09c","SPBC29A10.14"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:27227887","title":"The Loss of Lam2 and Npr2-Npr3 Diminishes the Vacuolar Localization of Gtr1-Gtr2 and Disinhibits TORC1 Activity in Fission Yeast.","citation":"PLoS One 2016;11(5):e0156239","abstract":"In mammalian cells, mTORC1 activity is regulated by Rag GTPases. It is thought that the Ragulator complex and the GATOR (GAP activity towards Rags) complex regulate RagA/B as its GDP/GTP exchange factor (GEF) and GTPase-activating protein (GAP), respectively. However, the functions of components in these complexes remain elusive. Using fission yeast as a model organism, here we found that the loss of Lam2 (SPBC1778.05c), a homolog of a Ragulator component LAMTOR2, as well as the loss of Gtr1 or Gtr2 phenocopies the loss of Npr2 or Npr3, homologs of GATOR components Nprl2 or Nprl3, respectively. These phenotypes were rescued by TORC1 inhibition using pharmacological or genetic means, and the loss of Lam2, Gtr1, Gtr2, Npr2 or Npr3 disinhibited TORC1 activity under nitrogen depletion, as measured by Rps6 phosphorylation. Consistently, overexpression of GDP-locked Gtr1S20L or GTP-locked Gtr2Q60L, which suppress TORC1 activity in budding yeast, rescued the growth defect of Δgtr1 cells or Δgtr2 cells, respectively, and the loss of Lam2, Npr2 or Npr3 similarly diminished the vacuolar localization and the protein levels of Gtr1 and Gtr2. Furthermore, Lam2 physically interacted with Npr2 and Gtr1. These findings suggest that Lam2 and Npr2-Npr3 function together as a tether for GDP-bound Gtr1 to the vacuolar membrane, thereby suppressing TORC1 activity for multiple cellular functions.","doi":"10.1371/journal.pone.0156239","authors":"Ma N, Ma Y, Nakashima A, Kikkawa U, Furuyashiki T","authors_abbrev":"Ma N et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-05-27","publication_year":"2016","canto_session_key":"dd1b44baa214d190","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-11 16:23:50","canto_approved_date":"2022-02-07 18:03:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-11 16:23:41","canto_added_date":"2016-05-28 00:15:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":95,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.13c","SPBC216.07c","SPAC23H3.03c","SPBC543.04","SPCC1902.01","SPAC1039.09","SPAPB1E7.12","SPAC13G6.07c","SPCC757.07c","SPBC1778.05c","SPCC777.05"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2017-10-11"},{"uniquename":"PMID:25543282","title":"Profilin regulates F-actin network homeostasis by favoring formin over Arp2/3 complex.","citation":"Dev Cell 2015 Jan 12;32(1):43-53","abstract":"Fission yeast cells use Arp2/3 complex and formin to assemble diverse filamentous actin (F-actin) networks within a common cytoplasm for endocytosis, division, and polarization. Although these homeostatic F-actin networks are usually investigated separately, competition for a limited pool of actin monomers (G-actin) helps to regulate their size and density. However, the mechanism by which G-actin is correctly distributed between rival F-actin networks is not clear. Using a combination of cell biological approaches and in vitro reconstitution of competition between actin assembly factors, we found that the small G-actin binding protein profilin directly inhibits Arp2/3 complex-mediated actin assembly. Profilin is therefore required for formin to compete effectively with excess Arp2/3 complex for limited G-actin and to assemble F-actin for contractile ring formation in dividing cells.","doi":"10.1016/j.devcel.2014.10.027","authors":"Suarez C, Carroll RT, Burke TA, Christensen JR, Bestul AJ, Sees JA, James ML, Sirotkin V, Kovar DR","authors_abbrev":"Suarez C et al.","pubmed_publication_date":"12 Jan 2015","pubmed_entrez_date":"2014-12-29","publication_year":"2015","canto_session_key":"f3e180dfcfc5bea5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-12-31 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.03","SPAC4F10.15c","SPBC32H8.12c","SPAC11H11.06","SPAC4A8.15c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:24316442","title":"3D actin network centerline extraction with multiple active contours.","citation":"Med Image Anal 2014 Feb;18(2):272-84","abstract":"Fluorescence microscopy is frequently used to study two and three dimensional network structures formed by cytoskeletal polymer fibers such as actin filaments and actin cables. While these cytoskeletal structures are often dilute enough to allow imaging of individual filaments or bundles of them, quantitative analysis of these images is challenging. To facilitate quantitative, reproducible and objective analysis of the image data, we propose a semi-automated method to extract actin networks and retrieve their topology in 3D. Our method uses multiple Stretching Open Active Contours (SOACs) that are automatically initialized at image intensity ridges and then evolve along the centerlines of filaments in the network. SOACs can merge, stop at junctions, and reconfigure with others to allow smooth crossing at junctions of filaments. The proposed approach is generally applicable to images of curvilinear networks with low SNR. We demonstrate its potential by extracting the centerlines of synthetic meshwork images, actin networks in 2D Total Internal Reflection Fluorescence Microscopy images, and 3D actin cable meshworks of live fission yeast cells imaged by spinning disk confocal microscopy. Quantitative evaluation of the method using synthetic images shows that for images with SNR above 5.0, the average vertex error measured by the distance between our result and ground truth is 1 voxel, and the average Hausdorff distance is below 10 voxels.","doi":"10.1016/j.media.2013.10.015","authors":"Xu T, Vavylonis D, Huang X","authors_abbrev":"Xu T et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-12-10","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20708088","title":"Mechanisms of contractile-ring assembly in fission yeast and beyond.","citation":"Semin Cell Dev Biol 2010 Dec;21(9):892-8","abstract":"Most eukaryotes including fungi, amoebas, and animal cells assemble an actin/myosin-based contractile ring during cytokinesis. The majority of proteins implied in ring formation, maturation, and constriction are evolutionarily conserved, suggesting that common mechanisms exist among these divergent eukaryotes. Here, we review the recent advances in positioning and assembly of the actomyosin ring in the fission yeast Schizosaccharomyces pombe, the budding yeast Saccharomyces cerevisiae, and animal cells. In particular, major findings have been made recently in understanding ring formation in genetically tractable S. pombe, revealing a dynamic and robust search, capture, pull, and release mechanism.","doi":"10.1016/j.semcdb.2010.08.004","authors":"Laporte D, Zhao R, Wu JQ","authors_abbrev":"Laporte D et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-08-17","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37548402","title":"Cell-type specific regulator RBPMS switches alternative splicing via higher-order oligomerization and heterotypic interactions with other splicing regulators.","citation":"Nucleic Acids Res 2023 Oct 13;51(18):9961-9982","abstract":"Alternative pre-mRNA splicing decisions are regulated by RNA binding proteins (RBPs) that can activate or repress regulated splice sites. Repressive RBPs typically harness multivalent interactions to bind stably to target RNAs. Multivalency can be achieved by homomeric oligomerization and heteromeric interactions with other RBPs, often mediated by intrinsically disordered regions (IDRs), and by possessing multiple RNA binding domains. Cell-specific splicing decisions often involve the action of widely expressed RBPs, which are able to bind multivalently around target exons, but without effect in the absence of a cell-specific regulator. To address how cell-specific regulators can collaborate with constitutive RBPs in alternative splicing regulation, we used the smooth-muscle specific regulator RBPMS. Recombinant RBPMS is sufficient to confer smooth muscle cell specific alternative splicing of Tpm1 exon 3 in cell-free assays by preventing assembly of ATP-dependent splicing complexes. This activity depends upon a C-terminal IDR that facilitates dynamic higher-order self-assembly, cooperative binding to multivalent RNA and interactions with widely expressed splicing co-regulators, including MBNL1 and RBFOX2, allowing cooperative assembly of stable cell-specific regulatory complexes.","doi":"10.1093/nar/gkad652","authors":"Yang Y, Lee GC, Nakagaki-Silva E, Huang Y, Peacey M, Partridge R, Gooding C, Smith CWJ","authors_abbrev":"Yang Y et al.","pubmed_publication_date":"13 Oct 2023","pubmed_entrez_date":"2023-08-07","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC320.07c","SPCC16C4.07"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:15689498","title":"Ace2p controls the expression of genes required for cell separation in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2005 Apr;16(4):2003-17","abstract":"Schizosaccharomyces pombe cells divide by medial fission through contraction of an actomyosin ring and deposition of a multilayered division septum that must be cleaved to release the two daughter cells. Here we describe the identification of seven genes (adg1(+), adg2(+), adg3(+), cfh4(+), agn1(+), eng1(+), and mid2(+)) whose expression is induced by the transcription factor Ace2p. The expression of all of these genes varied during the cell cycle, maximum transcription being observed during septation. At least three of these proteins (Eng1p, Agn1p, and Cfh4p) localize to a ring-like structure that surrounds the septum region during cell separation. Deletion of the previously uncharacterized genes was not lethal to the cells, but produced defects or delays in cell separation to different extents. Electron microscopic observation of mutant cells indicated that the most severe defect is found in eng1Delta agn1Delta cells, lacking the Eng1p endo-beta-1,3-glucanase and the Agn1p endo-alpha-glucanase. The phenotype of this mutant closely resembled that of ace2Delta mutants, forming branched chains of cells. This suggests that these two proteins are the main activities required for cell separation to be completed.","authors":"Alonso-Nuñez ML, An H, Martín-Cuadrado AB, Mehta S, Petit C, Sipiczki M, del Rey F, Gould KL, de Aldana CR","authors_abbrev":"Alonso-Nuñez ML et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-02-04","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18.01c","SPAC19G12.16c","SPAPYUG7.03c","SPAC14C4.09","SPAC6G10.12c","SPBC3E7.12c","SPAPJ760.03c","SPAC821.09"],"gene_count":8,"ltp_gene_count":3},{"uniquename":"PMID:7254352","title":"Gene required in G1 for commitment to cell cycle and in G2 for control of mitosis in fission yeast.","citation":"Nature 1981 Aug 06;292(5823):558-60","abstract":"","authors":"Nurse P, Bissett Y","authors_abbrev":"Nurse P et al.","pubmed_publication_date":"06 Aug 1981","pubmed_entrez_date":"1981-08-06","publication_year":"1981","canto_session_key":"c2b25694958a17bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ryoko Mandeville","canto_first_approved_date":"2018-04-28 22:11:00","canto_approved_date":"2019-06-18 12:18:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-11 16:32:51","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[{"name":"Ryoko Mandeville","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-04-28"},{"uniquename":"PMID:15809031","title":"Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity.","citation":"Dev Cell 2005 Apr;8(4):479-91","abstract":"Microtubules regulate actin-based processes such as cell migration and cytokinesis, but molecular mechanisms are not understood. In the fission yeast Schizosaccharomyces pombe, microtubule plus ends regulate cell polarity in part by transporting the kelch repeat protein tea1p to cell ends. Here, we identify tea4p, a SH3 domain protein that binds directly to tea1p. Like tea1p, tea4p localizes to growing microtubule plus ends and to cortical sites at cell ends, and it is necessary for the establishment of bipolar growth. Tea4p binds directly to and recruits the formin for3p, which nucleates actin cable assembly. During \"new end take off\" (NETO), formation of a protein complex that includes tea1p, tea4p, and for3p is necessary and sufficient for the establishment of cell polarity and localized actin assembly at new cell ends. Our results suggest a molecular mechanism for how microtubule plus ends regulate the spatial distribution of actin assembly.","authors":"Martin SG, McDonald WH, Yates JR, Chang F","authors_abbrev":"Martin SG et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-04-06","publication_year":"2005","canto_session_key":"260a55b4758c2119","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-08-20 17:14:52","canto_approved_date":"2025-09-04 10:19:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-08-20 17:14:46","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":73,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC895.05","SPAC6G10.02c","SPCC1223.06","SPBC1706.01","SPAC3C7.12","SPBC530.04"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2020-08-20"},{"uniquename":"PMID:34948069","title":"Lipids and Trehalose Actively Cooperate in Heat Stress Management of  Schizosaccharomyces pombe .","citation":"Int J Mol Sci 2021 Dec 09;22(24)","abstract":"Homeostatic maintenance of the physicochemical properties of cellular membranes is essential for life. In yeast, trehalose accumulation and lipid remodeling enable rapid adaptation to perturbations, but their crosstalk was not investigated. Here we report about the first in-depth, mass spectrometry-based lipidomic analysis on heat-stressed  Schizosaccharomyces pombe  mutants which are unable to synthesize ( tps1Δ ) or degrade ( ntp1Δ ) trehalose. Our experiments provide data about the role of trehalose as a membrane protectant in heat stress. We show that under conditions of trehalose deficiency, heat stress induced a comprehensive, distinctively high-degree lipidome reshaping in which structural, signaling and storage lipids acted in concert. In the absence of trehalose, membrane lipid remodeling was more pronounced and increased with increasing stress dose. It could be characterized by decreasing unsaturation and increasing acyl chain length, and required de novo synthesis of stearic acid (18:0) and very long-chain fatty acids to serve membrane rigidification. In addition, we detected enhanced and sustained signaling lipid generation to ensure transient cell cycle arrest as well as more intense triglyceride synthesis to accommodate membrane lipid-derived oleic acid (18:1) and newly synthesized but unused fatty acids. We also demonstrate that these changes were able to partially substitute for the missing role of trehalose and conferred measurable stress tolerance to fission yeast cells.","doi":"10.3390/ijms222413272","authors":"Péter M, Gudmann P, Kóta Z, Török Z, Vígh L, Glatz A, Balogh G","authors_abbrev":"Péter M et al.","pubmed_publication_date":"09 Dec 2021","pubmed_entrez_date":"2021-12-24","publication_year":"2021","canto_session_key":"1c5400656dc56364","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2832071","title":"A new mutation for multiple drug resistance and modified plasma membrane ATPase activity in Schizosaccharomyces pombe.","citation":"Curr Genet 1986;10(5):359-64","abstract":"The mutant JV66 was selected from the wild type strain of S. pombe 972h- ade7-413 by its ability to grow on solid rich medium containing 200 micrograms Dio-9/ml. The single nuclear mutation, designated pma1 gives resistance towards diguanidines and several other positively charged compounds. The pma1 mutation also decreases plasma membrane ATPase activity and confers resistance of ATPase to vanadate. The pma1 locus is localized on chromosome I at 5.3 map units from cyh1-C7 and at about 20.7 map units from the centromere. This new mutation is genetically and phenotypically different from the mutation cyh3 and cyh4 previously described (Johnston and Coddington 1983).","authors":"Ulaszewski S, Coddington A, Goffeau A","authors_abbrev":"Ulaszewski S et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_session_key":"d5c757529d95fb29","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-11-29 15:29:12","canto_approved_date":"2021-06-16 14:33:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-09-24 16:14:36","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-11-29"},{"uniquename":"PMID:893552","title":"Linear increase in glycolytic activity through the cell cycle of schizosaccharomyces pombe.","citation":"J Cell Sci 1977 Apr;24:69-79","abstract":"The glycolytic activity of 3 different synchronous system in S. pombe was studied. Synchronous cultures were produced by a selection procedure, by cyclic heat treatment, or by cloning cells from an exponentially multiplying culture. In all experiments a complex medium with 3% glucose was used. The glycolytic activity was recorded with a gasometric method, the gradient diver. A single cell in exponential growth or a small number of synchronized cells were placed in ampulla divers in which the cells progressed undistrubed through a number of cycles. An ampulla diver is in principle a narrow pipette by which a single or a few cells are removed from the mother culture. It serves next as an axenic growth chamber and at the same time as a gasometer. The divers were placed in linear saline density gradients and the gaseous exchanges taking place in the divers resulted in migration of the divers. The migration rate is a measure of the glycolytic activity of the cells. Our results show that the glycolytic activity increases in a linear fashion between sucessive divisions. The rate of increase doubles at each division. This true in all 3 synchronous systems, and we take this as an indication that the cell cycles of heat-synchronized cells do not deviate seriously from the normal.","authors":"Hamburger K, Kramhoft B, Nissen SB, Zeuthen E","authors_abbrev":"Hamburger K et al.","pubmed_publication_date":"Apr 1977","pubmed_entrez_date":"1977-04-01","publication_year":"1977","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733399","title":"Synchronous Induction of Meiosis in the Fission Yeast  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Sep 01;2017(9):pdb.prot091777","abstract":"In fission yeast  Schizosaccharomyces pombe,  initiation of meiosis is repressed by Pat1 kinase. This protocol describes how ectopic inactivation of the temperature-sensitive Pat1-114 kinase in G 1 -arrested  h -   / h -   diploid cells carrying  mat1-Pc  induces a highly synchronized commitment to and execution of meiosis. Haploid or diploid  pat1 -114 mutants without  mat1-Pc  can also be used for convenience, although less synchrony may be attained compared with induction using true diploids. An essentially identical protocol can be used for induction via inhibition of genetically sensitized Pat1 kinase by ATP analogs.","doi":"10.1101/pdb.prot091777","authors":"Yamashita A, Sakuno T, Watanabe Y, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"01 Sep 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33374550","title":"The Important Contribution of Non- Saccharomyces  Yeasts to the Aroma Complexity of Wine: A Review.","citation":"Foods 2020 Dec 23;10(1)","abstract":"Non- Saccharomyces  yeast plays an important role in the initial stages of a wild ferment, as they are found in higher abundance in the vineyard than  Saccharomyces cerevisiae . As such, there has been a focus in recent years to isolate these yeast species and characterize their effect on wine fermentation and subsequent aroma. This effect on wine aroma is often species and strain dependent, as the enzymatic profile of each yeast will determine which aroma compounds are formed as secondary metabolites. Semi-fermentative yeast, such as  Hanseniaspora  spp.,  Candida  spp. and  Metschnikowia pulcherrima , are commonly in high abundance in fresh grape must and have diverse enzymatic profiles, however they show a weak tolerance to ethanol, limiting their impact to the initial stages of fermentation. Fully fermentative non- Saccharomyces  yeast, characterized by high ethanol tolerance, are often found at low abundance in fresh grape must, similar to  Saccharomyces cerevisiae . Their ability to influence the aroma profile of wine remains high, however, due to their presence into the final stages of fermentation. Some fermentative yeasts also have unique oenological properties, such as  Lanchancea thermotolerans  and  Schizosaccharomyces pombe , highlighting the potential of these yeast as inoculants for specific wine styles.","doi":"10.3390/foods10010013","authors":"Borren E, Tian B","authors_abbrev":"Borren E et al.","pubmed_publication_date":"23 Dec 2020","pubmed_entrez_date":"2020-12-30","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-01-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38526189","title":"Cdc48 and its co-factor Ufd1 extract CENP-A from centromeric chromatin and can induce chromosome elimination in the fission yeast Schizosaccharomyces pombe.","citation":"Biol Open 2024 Mar 25;","abstract":"CENP-A determines the identity of the centromere. Because the position and size of the centromere and its number per chromosome must be maintained, the distribution of CENP-A is strictly regulated. In this study, we have aimed to understand mechanisms to regulate the distribution of CENP-A (Cnp1SP) in fission yeast. A mutant of the ufd1+ gene (ufd1-73) encoding a cofactor of Cdc48 ATPase is sensitive to Cnp1 expressed at a high level and allows mislocalization of Cnp1. The level of Cnp1 in centromeric chromatin is increased in the ufd1-73 mutant even when Cnp1 is expressed at a normal level. A preexisting mutant of the cdc48+ gene (cdc48-353) phenocopies the ufd1-73 mutant. We have also shown that Cdc48 and Ufd1 proteins physically interact with centromeric chromatin. Finally, Cdc48 ATPase with Ufd1 artificially recruited to the centromere of a mini-chromosome (Ch16) induce a loss of Cnp1 from Ch16, leading to an increased rate of chromosome loss. It appears that Cdc48 ATPase, together with its cofactor Ufd1 remove excess Cnp1 from chromatin, likely in a direct manner. This mechanism may play a role in centromere disassembly, a process to eliminate Cnp1 to inactivate the kinetochore function during development, differentiation, and stress response.","doi":"10.1242/bio.060287","authors":"Nakase Y, Murakami H, Suma M, Nagano K, Wakuda A, Kitagawa T, Matsumoto T","authors_abbrev":"Nakase Y et al.","pubmed_publication_date":"25 Mar 2024","pubmed_entrez_date":"2024-03-25","publication_year":"2024","canto_session_key":"4ee746f747c10f22","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-26 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.08","SPBC1105.17","SPBC16A3.09c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:40883509","title":"Nrm1 is a bistable switch connecting cell cycle progression to transcriptional control.","citation":"EMBO Rep 2025 Aug 29;","abstract":"Entry into the cell cycle requires activation of G1 cyclin-dependent kinases (CDKs) and the G1/S transcriptional program. In fission yeast, the MBF complex is the main transcription factor driving early cell-cycle gene expression. MBF-dependent transcription is activated in metaphase and repressed at the end of S phase by a feedback loop involving the cyclin Cig2 and co-repressors Nrm1 and Yox1. While replicative stress inactivates Yox1 via phosphorylation, the mechanism that activates MBF during an unperturbed cell cycle remains unclear. Here, we identify Nrm1 as the key target of cell cycle regulation in a two-step control mechanism. First, CDK1 phosphorylates Nrm1 in metaphase, leading to its release-along with Yox1-from chromatin. Second, unphosphorylated Nrm1, generated either by dephosphorylation or de novo synthesis, is degraded during anaphase, preventing its re-association with MBF until the end of the next S phase. Together, these parallel pathways create a precisely timed window of MBF activation, ensuring proper cell cycle progression and preserving genomic stability.","doi":"10.1038/s44319-025-00566-7","authors":"Murciano-Julià G, Vega M, Pazo E, Pascual-Serra À, Alves-Rodrigues I, Bagudanch O, Anglada R, Bonet N, Aligué R, Moreno S, Oliva B, Hidalgo E, Ayté J","authors_abbrev":"Murciano-Julià G et al.","pubmed_publication_date":"29 Aug 2025","pubmed_entrez_date":"2025-08-29","publication_year":"2025","canto_session_key":"854d165c9678de56","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-08-30 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26108447","title":"Azoles activate Atf1-mediated transcription through MAP kinase pathway for antifungal effects in fission yeast.","citation":"Genes Cells 2015 Sep;20(9):695-705","abstract":"Azole antifungals directly inhibit enzymes for ergosterol biosynthesis, and this direct action is thought to underlie antifungal actions of these drugs. Recent studies showed that azoles alter expression of genes for various cellular functions. However, transcription factors regulated by azoles and their roles in antifungal actions remain poorly characterized. Using luciferase assay, we found that miconazole increased luciferase activity under the promoter containing the cAMP response element (CRE) motif. This azole-induced activation of CRE reporter was abolished in Atf1-deficient cells, suggesting that azoles induce Atf1 activation. As Atf1 is activated by stress-activated MAP kinase Sty1 upon various stressors, we examined its involvement. Azoles increased phosphorylation of Sty1 for its activation, and Sty1 deletion impaired azole-induced CRE reporter activation. In contrast, deletion of Pyp1, a tyrosine phosphatase which negatively regulates Sty1, increased CRE reporter activation. In addition, cells deficient in Atf1 and stress-activated MAP kinase pathway showed resistance to azoles, whereas cells lacking Pyp1 increased azole susceptibility, suggesting a critical role for azole-induced activation of MAP kinase-Atf1 pathway in antifungal actions of azoles. Collectively, these results suggest that azoles activate stress-activated MAP kinase pathway, thereby facilitating Atf1-mediated transcription for antifungal effects.","doi":"10.1111/gtc.12263","authors":"Hu L, Fang Y, Hayafuji T, Ma Y, Furuyashiki T","authors_abbrev":"Hu L et al.","pubmed_publication_date":"Sep 2015","pubmed_entrez_date":"2015-06-26","publication_year":"2015","canto_session_key":"da2ab48fecb84a55","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomoyuki Furuyashiki","canto_approved_date":"2016-07-18 08:59:58","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-07-01 02:40:14","canto_added_date":"2015-06-27 00:20:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Tomoyuki Furuyashiki","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.10","SPAC1006.09","SPAC9G1.02","SPAC24B11.06c","SPBC29B5.01","SPAC26F1.10c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-07-01"},{"uniquename":"PMID:23084836","title":"Epigenetic regulation of condensin-mediated genome organization during the cell cycle and upon DNA damage through histone H3 lysine 56 acetylation.","citation":"Mol Cell 2012 Nov 30;48(4):532-46","abstract":"Complex genome organizations participate in various nuclear processes including transcription, DNA replication, and repair. However, the mechanisms that generate and regulate these functional genome structures remain largely unknown. Here, we describe how the Ku heterodimer complex, which functions in nonhomologous end joining, mediates clustering of long terminal repeat retrotransposons at centromeres in fission yeast. We demonstrate that the CENP-B subunit, Abp1, functions as a recruiter of the Ku complex, which in turn loads the genome-organizing machinery condensin to retrotransposons. Intriguingly, histone H3 lysine 56 (H3K56) acetylation, which functions in DNA replication and repair, interferes with Ku localization at retrotransposons without disrupting Abp1 localization and, as a consequence, dissociates condensin from retrotransposons. This dissociation releases condensin-mediated genomic associations during S phase and upon DNA damage. ATR (ATM- and Rad3-related) kinase mediates the DNA damage response of condensin-mediated genome organization. Our study describes a function of H3K56 acetylation that neutralizes condensin-mediated genome organization.","doi":"10.1016/j.molcel.2012.09.011","authors":"Tanaka A, Tanizawa H, Sriswasdi S, Iwasaki O, Chatterjee AG, Speicher DW, Levin HL, Noguchi E, Noma K","authors_abbrev":"Tanaka A et al.","pubmed_publication_date":"30 Nov 2012","pubmed_entrez_date":"2012-10-23","publication_year":"2012","canto_session_key":"f895d3b39398c5aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-03-07 19:40:50","canto_approved_date":"2020-04-09 14:04:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-02-07 22:23:04","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.01","SPCC594.07c","SPAC1783.04c","SPBP4H10.06c","SPCC126.02c","SPBC146.03c","SPBC216.05","SPBC1778.02","SPAC16A10.07c","SPBC36.05c","SPBC342.06c","SPBC1105.04c","SPBC19C7.10","SPBC543.03c"],"gene_count":14,"ltp_gene_count":10,"approved_date":"2020-03-07"},{"uniquename":"PMID:13378072","title":"Remote hybridization of yeasts. II. Production of hybrids of Saccharomyces cerevisiae (race XII) and Schizosaccharomyces pombe by cell copulation.","citation":"Mikrobiologiia 1956;25(4):420-2","abstract":"","authors":"KOSIKOV KV","authors_abbrev":"KOSIKOV KV","pubmed_publication_date":"1956","pubmed_entrez_date":"1956-07-01","publication_year":"1956","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2558974","title":"A transcriptionally regulated expression vector for the fission yeast Schizosaccharomyces pombe.","citation":"Gene 1989 Dec 14;84(2):473-9","abstract":"An expression vector for the fission yeast Schizosaccharomyces pombe is described. The vector is designed to facilitate the construction of transcriptional fusions to the promoter of the S. pombe fructose bisphosphatase gene. Transcription from this promoter is regulated by glucose repression over a range of greater than 100-fold. The tight regulation by this promoter should allow for the maintenance of genes whose products are lethal to S. pombe and for the high level production of their protein or RNA products. Intermediate levels of expression can also be achieved by growth on different carbon sources.","authors":"Hoffman CS, Winston F","authors_abbrev":"Hoffman CS et al.","pubmed_publication_date":"14 Dec 1989","pubmed_entrez_date":"1989-12-14","publication_year":"1989","canto_session_key":"d9a59af610cff3eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-03-22 15:17:08","canto_session_submitted_date":"2012-02-16 22:47:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-02-16"},{"uniquename":"PMID:24100010","title":"Spt6 regulates intragenic and antisense transcription, nucleosome positioning, and histone modifications genome-wide in fission yeast.","citation":"Mol Cell Biol 2013 Dec;33(24):4779-92","abstract":"Spt6 is a highly conserved histone chaperone that interacts directly with both RNA polymerase II and histones to regulate gene expression. To gain a comprehensive understanding of the roles of Spt6, we performed genome-wide analyses of transcription, chromatin structure, and histone modifications in a Schizosaccharomyces pombe spt6 mutant. Our results demonstrate dramatic changes to transcription and chromatin structure in the mutant, including elevated antisense transcripts at >70% of all genes and general loss of the +1 nucleosome. Furthermore, Spt6 is required for marks associated with active transcription, including trimethylation of histone H3 on lysine 4, previously observed in humans but not Saccharomyces cerevisiae, and lysine 36. Taken together, our results indicate that Spt6 is critical for the accuracy of transcription and the integrity of chromatin, likely via its direct interactions with RNA polymerase II and histones.","doi":"10.1128/MCB.01068-13","authors":"DeGennaro CM, Alver BH, Marguerat S, Stepanova E, Davis CP, Bähler J, Park PJ, Winston F","authors_abbrev":"DeGennaro CM et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-10-09","publication_year":"2013","canto_session_key":"1ce42bbf54256dde","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Fred Winston","canto_first_approved_date":"2018-04-25 03:05:34","canto_approved_date":"2023-01-06 14:43:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-08-24 10:51:43","canto_added_date":"2013-11-01 02:19:02","annotation_curators":[{"name":"Fred Winston","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.03","SPAC27D7.14c","SPCC594.05c","SPAC23H3.05c","SPAC18B11.07c","SPAC1F7.01c","SPBC651.09c","SPBC17G9.02c"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2018-04-25"},{"uniquename":"PMID:33554116","title":" In silico  analysis of DNA re-replication across a complete genome reveals cell-to-cell heterogeneity and genome plasticity.","citation":"NAR Genom Bioinform 2021 Mar;3(1):lqaa112","abstract":"DNA replication is a complex and remarkably robust process: despite its inherent uncertainty, manifested through stochastic replication timing at a single-cell level, multiple control mechanisms ensure its accurate and timely completion across a population. Disruptions in these mechanisms lead to DNA re-replication, closely connected to genomic instability and oncogenesis. Here, we present a stochastic hybrid model of DNA re-replication that accurately portrays the interplay between discrete dynamics, continuous dynamics and uncertainty. Using experimental data on the fission yeast genome, model simulations show how different regions respond to re-replication and permit insight into the key mechanisms affecting re-replication dynamics. Simulated and experimental population-level profiles exhibit a good correlation along the genome, robust to model parameters, validating our approach. At a single-cell level, copy numbers of individual loci are affected by intrinsic properties of each locus,  in cis  effects from adjoining loci and  in trans  effects from distant loci.  In silico  analysis and single-cell imaging reveal that cell-to-cell heterogeneity is inherent in re-replication and can lead to genome plasticity and a plethora of genotypic variations.","doi":"10.1093/nargab/lqaa112","authors":"Rapsomaniki MA, Maxouri S, Nathanailidou P, Garrastacho MR, Giakoumakis NN, Taraviras S, Lygeros J, Lygerou Z","authors_abbrev":"Rapsomaniki MA et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2021-02-08","publication_year":"2021","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2021-02-10 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11886869","title":"A transporter in the endoplasmic reticulum of Schizosaccharomyces pombe cells mediates zinc storage and differentially affects transition metal tolerance.","citation":"J Biol Chem 2002 May 17;277(20):18215-21","abstract":"The cation diffusion facilitator (CDF) family represents a class of ubiquitous metal transporters. Inactivation of a CDF in Schizosaccharomyces pombe, Zhf, causes drastically different effects on the tolerance toward various metals. A deletion mutant is Zn(2+)/Co(2+)-hypersensitive yet displays significantly enhanced Cd(2+) and Ni(2+) tolerance. Accumulation of zinc, cobalt, and cadmium is reduced in mutant cells. Non-vacuolar zinc content, as measured by analytical electron microscopy, is lower in zhf(-) cells compared with wild-type cells in the presence of elevated Zn(2+) concentrations. The protective effect against cadmium toxicity is independent of the phytochelatin detoxification pathway. Phytochelatin synthase-deficient cells show extremely enhanced (about 200-fold) cadmium tolerance when zhf is disrupted. Immunogold labeling indicates endoplasmic reticulum (ER) localization of Zhf. Electron spectroscopic imaging shows that accumulation of zinc coincides with Zhf localization, demonstrating a major role of the ER for metal storage and the involvement of Zhf in cellular zinc homeostasis. Also, these observations indicate that Cd(2+) ions exert their toxic effects on cellular metabolism in the ER rather than in the cytosol.","authors":"Clemens S, Bloss T, Vess C, Neumann D, Nies DH, Zur Nieden U","authors_abbrev":"Clemens S et al.","pubmed_publication_date":"17 May 2002","pubmed_entrez_date":"2002-03-12","publication_year":"2002","canto_session_key":"7d86a078e24b65b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-02-04 19:36:08","canto_approved_date":"2025-09-03 14:53:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-27 11:07:24","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H1.10","SPAC23C11.14"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-02-04"},{"uniquename":"PMID:31644361","title":"A mechanism for how Cdr1/Nim1 kinase promotes mitotic entry by inhibiting Wee1.","citation":"Mol Biol Cell 2019 Dec 01;30(25):3015-3023","abstract":"To enter into mitosis, cells must shut off the cell cycle inhibitor Wee1. SAD family protein kinases regulate Wee1 signaling in yeast and humans. In  Schizosaccharomyces pombe , two SAD kinases (Cdr1/Nim1 and Cdr2) act as upstream inhibitors of Wee1. Previous studies found that  S. pombe  Cdr1/Nim1 directly phosphorylates and inhibits Wee1 in vitro, but different results were obtained for budding yeast and human SAD kinases. Without a full understanding of Cdr1 action on Wee1, it has been difficult to assess the in vivo relevance and conservation of this mechanism. Here, we show that both Cdr1 and Cdr2 promote Wee1 phosphorylation in cells, but only Cdr1 inhibits Wee1 kinase activity. Inhibition occurs when Cdr1 phosphorylates a cluster of serine residues linking α-helices G and H of the Wee1 kinase domain. This region is highly divergent among different Wee1 proteins, consistent with distinct regulatory mechanisms. A  wee(4A)  mutant that impairs phosphorylation by Cdr1 delays mitotic entry and causes elongated cells. By disrupting and retargeting Cdr1 localization, we show that Cdr1 inhibition of Wee1 occurs in cells at cortical nodes formed by Cdr2. On the basis of our results, we propose a two-step model for inhibition of Wee1 by Cdr1 and Cdr2 at nodes.","doi":"10.1091/mbc.E19-08-0430","authors":"Opalko HE, Nasa I, Kettenbach AN, Moseley JB","authors_abbrev":"Opalko HE et al.","pubmed_publication_date":"01 Dec 2019","pubmed_entrez_date":"2019-10-24","publication_year":"2019","canto_session_key":"020b7fc6a3fa0724","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"hannah opalko","canto_first_approved_date":"2020-02-19 18:04:29","canto_approved_date":"2025-09-03 11:45:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-07 18:24:58","canto_added_date":"2019-10-25 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"hannah opalko","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC644.06c","SPAC57A10.02","SPCC18B5.03","SPAC24H6.05"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-02-19"},{"uniquename":"PMID:41855172","title":"Distinct Cdc42 protein levels differentially regulate polarized growth and cell fusion in Schizosaccharomyces pombe.","citation":"PLoS Biol 2026 Mar;24(3):e3003712","abstract":"The conserved Cdc42 GTPase is a key driver of symmetry breaking and polarized growth, forming zones of activity that locally recruit effectors to organize the cytoskeleton and polarize secretion. Here, we show that Cdc42 also functions in cell-cell fusion during Schizosaccharomyces pombe sexual reproduction, but concentrates at the fusion site through mechanisms distinct from those proposed in Saccharomyces cerevisiae. Notably, the cdc42-mCherrySW allele, which is functional for cell polarization and has been used across organisms for dynamic studies, exhibits a strong fusion defect. These cells block fusion before cell wall digestion but after actin fusion focus formation, indicating that Cdc42 is required to translate the vesicle cluster into polarized cargo delivery. We trace the defect to instability of Cdc42-mCherrySW and demonstrate that mating and cell fusion require higher Cdc42 protein levels than mitotic polarized growth. Remarkably, by constructing an allelic series driving Cdc42 expression over a 5-fold range, we discover that mitotic polarized growth responds linearly to Cdc42 protein levels, whereas mating exhibits a sharp switch-like response. We further trace this all-or-none response to pheromone-induced polarized growth. Thus, polarized growth in response to intrinsic or extrinsic cues exhibits distinct requirements to Cdc42 protein levels.","doi":"10.1371/journal.pbio.3003712","authors":"Saha S, Sajeevan A, Merlini L, Vincenzetti V, Martin SG","authors_abbrev":"Saha S et al.","pubmed_publication_date":"Mar 2026","pubmed_entrez_date":"2026-03-19","publication_year":"2026","canto_session_key":"931627083b50568a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2026-05-22 10:13:25","canto_approved_date":"2026-05-29 18:47:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-04-01 09:39:32","canto_added_date":"2026-03-20 00:25:05","annotation_curators":[{"name":"Sophie Martin","community_curator":true,"annotation_count":67,"orcid":"0000-0002-5317-2557","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.03","SPAP7G5.03","SPAC1F5.09c","SPAC110.03","SPCC1235.10c","SPBC106.20","SPAC20G4.02c","SPCC1919.10c"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2026-05-22"},{"uniquename":"EMBL:AU013763","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23205155","title":"Mathematical modeling of fission yeast Schizosaccharomyces pombe cell cycle: exploring the role of multiple phosphatases.","citation":"Syst Synth Biol 2011 Dec;5(3-4):115-29","abstract":"Cell cycle is the central process that regulates growth and division in all eukaryotes. Based on the environmental condition sensed, the cell lies in a resting phase G0 or proceeds through the cyclic cell division process (G1→S→G2→M). These series of events and phase transitions are governed mainly by the highly conserved Cyclin dependent kinases (Cdks) and its positive and negative regulators. The cell cycle regulation of fission yeast Schizosaccharomyces pombe is modeled in this study. The study exploits a detailed molecular interaction map compiled based on the published model and experimental data. There are accumulating evidences about the prominent regulatory role of specific phosphatases in cell cycle regulations. The current study emphasizes the possible role of multiple phosphatases that governs the cell cycle regulation in fission yeast S. pombe. The ability of the model to reproduce the reported regulatory profile for the wild-type and various mutants was verified though simulations.\nThe online version of this article (doi:10.1007/s11693-011-9090-7) contains supplementary material, which is available to authorized users.","doi":"10.1007/s11693-011-9090-7","authors":"Anbumathi P, Bhartiya S, Venkatesh KV","authors_abbrev":"Anbumathi P et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2012-12-04","publication_year":"2011","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31391237","title":"The  S. pombe  adaptor protein Bbc1 regulates localization of Wsp1 and Vrp1 during endocytic actin patch assembly.","citation":"J Cell Sci 2019 Sep 11;132(17)","abstract":"Arp2/3 complex-nucleated branched actin networks provide the key force necessary for endocytosis. The Arp2/3 complex is activated by nucleation-promoting factors including the  Schizosaccharomyces pombe  Wiskott-Aldrich syndrome protein (Wsp1) and myosin-1 (Myo1). There are >40 known yeast endocytic proteins with distinct spatial and temporal localizations and functions; however, it is still unclear how these proteins work together to drive endocytosis. Here, we used quantitative live-cell imaging to determine the function of the uncharacterized  S. pombe  protein Bbc1. We discovered that Myo1 interacts with and recruits Bbc1 to sites of endocytosis. Bbc1 competes with the verprolin Vrp1 for localization to patches and association with Myo1, thus releasing Vrp1 and its binding partner Wsp1 from Myo1. Normally Myo1 remains at the base of the endocytic invagination and Vrp1-Wsp1 internalizes with the endocytic vesicle. However, in the absence of Bbc1, a portion of Vrp1-Wsp1 remains with Myo1 at the base of the invagination, and endocytic structures internalize twice as far. We propose that Bbc1 disrupts a transient interaction of Myo1 with Vrp1 and Wsp1 and thereby limits Arp2/3 complex-mediated nucleation of actin branches at the plasma membrane.This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.233502","authors":"MacQuarrie CD, Mangione MC, Carroll R, James M, Gould KL, Sirotkin V","authors_abbrev":"MacQuarrie CD et al.","pubmed_publication_date":"11 Sep 2019","pubmed_entrez_date":"2019-08-09","publication_year":"2019","canto_session_key":"ce21a1331b0f6dcc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-08-10 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC13E7.09","SPAC57A10.10c","SPAC23A1.17","SPBC146.13c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:36148799","title":"mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells.","citation":"J Cell Sci 2022 Sep 15;135(18)","abstract":"Tropomyosins are structurally conserved α-helical coiled-coil proteins that bind along the length of filamentous actin (F-actin) in fungi and animals. Tropomyosins play essential roles in the stability of actin filaments and in regulating myosin II contractility. Despite the crucial role of tropomyosin in actin cytoskeletal regulation, in vivo investigations of tropomyosin are limited, mainly due to the suboptimal live-cell imaging tools currently available. Here, we report on an mNeonGreen (mNG)-tagged tropomyosin, with native promoter and linker length configuration, that clearly reports tropomyosin dynamics in Schizosaccharomyces pombe (Cdc8), Schizosaccharomyces japonicus (Cdc8) and Saccharomyces cerevisiae (Tpm1 and Tpm2). We also describe a fluorescent probe to visualize mammalian tropomyosin (TPM2 isoform). Finally, we generated a camelid nanobody against S. pombe Cdc8, which mimics the localization of mNG-Cdc8 in vivo. Using these tools, we report the presence of tropomyosin in previously unappreciated patch-like structures in fission and budding yeasts, show flow of tropomyosin (F-actin) cables to the cytokinetic actomyosin ring and identify rearrangements of the actin cytoskeleton during mating. These powerful tools and strategies will aid better analyses of tropomyosin and F-actin cables in vivo.","doi":"10.1242/jcs.260288","authors":"Hatano T, Lim TC, Billault-Chaumartin I, Dhar A, Gu Y, Massam-Wu T, Scott W, Adishesha S, Chapa-Y-Lazo B, Springall L, Sivashanmugam L, Mishima M, Martin SG, Oliferenko S, Palani S, Balasubramanian MK","authors_abbrev":"Hatano T et al.","pubmed_publication_date":"15 Sep 2022","pubmed_entrez_date":"2022-09-23","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-09-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27797637","title":"Beyond Tethering and the LEM domain: MSCellaneous functions of the inner nuclear membrane Lem2.","citation":"Nucleus 2016 Nov;7(6):523-531","abstract":"The nuclear envelope plays a pivotal role in the functional organization of chromatin. Various inner nuclear membrane (INM) proteins associate with transcriptionally repressed chromatin, which is often found at the nuclear periphery. A prominent example is the conserved family of LEM (LAP2-Emerin-MAN1) domain proteins that interact with DNA-binding proteins and have been proposed to mediate tethering of chromatin to the nuclear membrane. We recently reported that the fission yeast protein Lem2, a homolog of metazoan LEM proteins, contributes to perinuclear localization and silencing of heterochromatin.  1  We demonstrate that binding and tethering of centromeric chromatin depends on the LEM domain of Lem2. Unexpectedly, this domain is dispensable for heterochromatin silencing, which is instead mediated by a different structural domain of Lem2, the MSC (MAN1-Src1 C-terminal) domain. Hence, silencing and tethering by Lem2 can be mechanistically separated. Notably, the MSC domain has multiple functions beyond heterochromatic silencing. Here we discuss the implications of these novel findings for the understanding of this conserved INM protein.","doi":"10.1080/19491034.2016.1252892","authors":"Braun S, Barrales RR","authors_abbrev":"Braun S et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-11-01","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-11-02 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24256300","title":"Clustered regulatory elements at nucleosome-depleted regions punctuate a constant nucleosomal landscape in Schizosaccharomyces pombe.","citation":"BMC Genomics 2013 Nov 21;14(1):813","abstract":"Nucleosomes facilitate the packaging of the eukaryotic genome and modulate the access of regulators to DNA. A detailed description of the nucleosomal organization under different transcriptional programmes is essential to understand their contribution to genomic regulation.\nTo visualize the dynamics of individual nucleosomes under different transcriptional programmes we have generated high-resolution nucleosomal maps in Schizosaccharomyces pombe. We show that 98.5% of the genome remains almost invariable during mitosis and meiosis while remodelling is limited to approximately 1100 nucleosomes in the promoters of a subset of meiotic genes. These inducible nucleosome-depleted regions (NDR) and also those constitutively present in the genome overlap precisely with clusters of binding sites for transcription factors (TF) specific for meiosis and for different functional classes of genes, respectively. Deletion of two TFs affects only a small fraction of all the NDRs to which they bind in vivo, indicating that TFs collectively contribute to NDR maintenance.\nOur results show that the nucleosomal profile in S. pombe is largely maintained under different physiological conditions and patterns of gene expression. This relatively constant landscape favours the concentration of regulators in constitutive and inducible NDRs. The combinatorial analysis of binding motifs in this discrete fraction of the genome will facilitate the definition of the transcriptional regulatory networks.","doi":"10.1186/1471-2164-14-813","authors":"Soriano I, Quintales L, Antequera F","authors_abbrev":"Soriano I et al.","pubmed_publication_date":"21 Nov 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_session_key":"5b88c1d2f4c48826","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-29 08:55:24","canto_approved_date":"2019-11-29 08:55:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-29 08:55:05","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-11-29"},{"uniquename":"PMID:34407404","title":"Two secured FACT recruitment mechanisms are essential for heterochromatin maintenance.","citation":"Cell Rep 2021 Aug 17;36(7):109540","abstract":"FACT (facilitate chromatin transcription) is involved in heterochromatic silencing, but its mechanisms and function remain unclear. We reveal that the Spt16 recruitment mechanism operates in two distinct ways in heterochromatin. First, Pob3 mediates Spt16 recruitment onto the heterochromatin through its Spt16 dimerization and tandem PH domains. Without Pob3, Spt16 recruitment is partially reduced, exhibiting a silencing defect and impaired H2A/H2B organization. Second, heterochromatin protein 1 (HP1)/Swi6 mediates Spt16 recruitment onto the heterochromatin by physical interaction of the Swi6 chromo-shadow domain (CSD) and Spt16 peptidase-like domains. Several CSD mutants are tested for Spt16 binding activity, and the charged loop connecting β1 and β2 is critical for Spt16 binding and heterochromatic silencing. Loss of these pathways causes a severe defect in H3K9 methylation and HP1/Swi6 localization in the pericentromeric region, exhibiting transcriptional silencing defects and disordered heterochromatin. Our findings suggest that FACT and HP1/Swi6 work intimately to regulate heterochromatin organization.","doi":"10.1016/j.celrep.2021.109540","authors":"Takahata S, Chida S, Ohnuma A, Ando M, Asanuma T, Murakami Y","authors_abbrev":"Takahata S et al.","pubmed_publication_date":"17 Aug 2021","pubmed_entrez_date":"2021-08-18","publication_year":"2021","canto_session_key":"4292b23863da2913","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-02-11 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c","SPBP8B7.19","SPAC57A10.09c","SPBC609.05"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:8769419","title":"Aberrant mitosis in fission yeast mutants defective in fatty acid synthetase and acetyl CoA carboxylase.","citation":"J Cell Biol 1996 Aug;134(4):949-61","abstract":"Two fission yeast temperature-sensitive mutants, cut6 and lsd1, show a defect in nuclear division. The daughter nuclei differ dramatically in size (the phenotype designated lsd, large and small daughter). Fluorescence in situ hybridization (FISH) revealed that sister chromatids were separated in the lsd cells, but appeared highly compact in one of the two daughter nuclei. EM showed asymmetric nuclear elongation followed by unequal separation of nonchromosomal nuclear structures in these mutant nuclei. The small nuclei lacked electron-dense nuclear materials and contained highly compacted chromatin. The cut6+ and lsd1+ genes are essential for viability and encode, respectively, acetyl CoA carboxylase and fatty acid synthetase, the key enzymes for fatty acid synthesis. Gene disruption of lsd1+ led to the lsd phenotype. Palmitate in medium fully suppressed the phenotypes of lsd1. Cerulenin, an inhibitor for fatty acid synthesis, produced the lsd phenotype in wild type. The drug caused cell inviability during mitosis but not during the G2-arrest induced by the cdc25 mutation. A reduced level of fatty acid thus led to impaired separation of non-chromosomal nuclear components. We propose that fatty acid is directly or indirectly required for separating the mother nucleus into two equal daughters.","authors":"Saitoh S, Takahashi K, Nabeshima K, Yamashita Y, Nakaseko Y, Hirata A, Yanagida M","authors_abbrev":"Saitoh S et al.","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_session_key":"b8f1a7f747cfebd1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 15:57:17","canto_approved_date":"2026-02-01 09:32:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-15 20:20:43","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.11c","SPAC56E4.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-17"},{"uniquename":"PMID:14534314","title":"Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent transcription in vitro.","citation":"J Biol Chem 2003 Dec 19;278(51):51301-6","abstract":"The fission yeast Schizosaccharomyces pombe has proved an important model system for cross-species comparative studies of many fundamental processes in the eukaryotic cell, such as cell cycle control and DNA replication. The RNA polymerase II transcription machinery is, however, still relatively poorly understood in S. pombe, partially due to the absence of a reconstituted in vitro transcription system. We have now purified S. pombe RNA polymerase II and its general initiation factors TFIIB, TFIIF, TFIIE, and TFIIH to near homogeneity. These factors enable RNA polymerase II to initiate transcription from the S. pombe alcohol dehydrogenase promoter (adh1p) when combined with Saccharomyces cerevisiae TATA-binding protein. We use our reconstituted system to examine effects of Mediator on basal transcription in vitro. S. pombe Mediator exists in two distinct forms, a free form, which contains the spSrb8, spTrap240, spSrb10, and spSrb11 subunits, and a smaller form, which lacks these four subunits and associates with RNA polymerase II to form a holoenzyme. We find that spSrb8/spTrap240/spSrb10/spSrb11 containing Mediator repress basal transcription, whereas Mediator lacking these subunits has a stimulatory effect on transcription. Our findings thus demonstrate that the spSrb8/spTrap240/spSrb10/spSrb11 subcomplex governs the ability of Mediator to stimulate or repress basal transcription in vitro.","authors":"Spahr H, Khorosjutina O, Baraznenok V, Linder T, Samuelsen CO, Hermand D, Mäkela TP, Holmberg S, Gustafsson CM","authors_abbrev":"Spahr H et al.","pubmed_publication_date":"19 Dec 2003","pubmed_entrez_date":"2003-10-10","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC776.18c","SPBP16F5.02","SPCC794.09c","SPBC32H8.12c","SPAC17A5.06","SPBC19F8.07","SPAC16E8.11c","SPBC30B4.07c","SPCC1682.07","SPBC13G1.13"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:5460194","title":"Antagonism by adenine in the nutrition of Schizosaccharomyces pombe mutants. Inhibition at the level of guanine uptake.","citation":"Biochim Biophys Acta 1970;209(2):269-77","abstract":"","authors":"Pourquie J","authors_abbrev":"Pourquie J","pubmed_publication_date":"1970","pubmed_entrez_date":"1970-01-01","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11968006","title":"Human papillomavirus-16 E7 protein inhibits the DNA interaction of the TATA binding transcription factor.","citation":"J Cell Biochem 2002;85(4):663-9","abstract":"Previous studies have shown that the HPV-16 E7 protein interacts with TBP. This interaction was found to take place through residues in the carboxy terminal half of E7, mutation of which resulted in weaker transforming activity. In addition, binding of E7 to TBP was found to be increased following protein kinase CK2 (casein kinase II) phosphorylation of E7, and mutation of this CK2 site also reduces E7's transforming activity. To date, however, there is no information on the effects of E7 upon TBP function. In order to address this we have performed a series of assays to investigate the effects of E7 upon the ability of human and S. pombe TBP to bind DNA. We show that HPV-16 E7 is indeed a potent inhibitor of TBP DNA binding activity. Further, this activity of E7 is increased following CK2 phosphorylation of E7, consistent with it having an increased affinity for TBP. Finally, a mutant E7 protein defective in its ability to bind TBP, has no effect upon TBP binding to DNA. These results demonstrate that one consequence of the E7-TBP interaction is abolition of TBP DNA binding activity, and may provide an explanation for the transcriptional inhibitory effects of E7.","authors":"Maldonado E, Cabrejos ME, Banks L, Allende JE","authors_abbrev":"Maldonado E et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-04-23","publication_year":"2002","canto_session_key":"20ad02c04a0ba957","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-27 15:55:50","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-07 13:54:46","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29E6.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-07"},{"uniquename":"PMID:28178334","title":"A novel mutual information-based Boolean network inference method from time-series gene expression data.","citation":"PLoS One 2017;12(2):e0171097","abstract":"Inferring a gene regulatory network from time-series gene expression data in systems biology is a challenging problem. Many methods have been suggested, most of which have a scalability limitation due to the combinatorial cost of searching a regulatory set of genes. In addition, they have focused on the accurate inference of a network structure only. Therefore, there is a pressing need to develop a network inference method to search regulatory genes efficiently and to predict the network dynamics accurately.\nIn this study, we employed a Boolean network model with a restricted update rule scheme to capture coarse-grained dynamics, and propose a novel mutual information-based Boolean network inference (MIBNI) method. Given time-series gene expression data as an input, the method first identifies a set of initial regulatory genes using mutual information-based feature selection, and then improves the dynamics prediction accuracy by iteratively swapping a pair of genes between sets of the selected regulatory genes and the other genes. Through extensive simulations with artificial datasets, MIBNI showed consistently better performance than six well-known existing methods, REVEAL, Best-Fit, RelNet, CST, CLR, and BIBN in terms of both structural and dynamics prediction accuracy. We further tested the proposed method with two real gene expression datasets for an Escherichia coli gene regulatory network and a fission yeast cell cycle network, and also observed better results using MIBNI compared to the six other methods.\nTaken together, MIBNI is a promising tool for predicting both the structure and the dynamics of a gene regulatory network.","doi":"10.1371/journal.pone.0171097","authors":"Barman S, Kwon YK","authors_abbrev":"Barman S et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-02-09","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-02-10 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009431","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19037096","title":"Kinesin-8 from fission yeast: a heterodimeric, plus-end-directed motor that can couple microtubule depolymerization to cargo movement.","citation":"Mol Biol Cell 2009 Feb;20(3):963-72","abstract":"Fission yeast expresses two kinesin-8s, previously identified and characterized as products of the klp5(+) and klp6(+) genes. These polypeptides colocalize throughout the vegetative cell cycle as they bind cytoplasmic microtubules during interphase, spindle microtubules, and/or kinetochores during early mitosis, and the interpolar spindle as it elongates in anaphase B. Here, we describe in vitro properties of these motor proteins and some truncated versions expressed in either bacteria or Sf9 cells. The motor-plus-neck domain of Klp6p formed soluble dimers that cross-linked microtubules and showed both microtubule-activated ATPase and plus-end-directed motor activities. Full-length Klp5p and Klp6p, coexpressed in Sf9 cells, formed soluble heterodimers with the same activities. The latter recombinant protein could also couple microbeads to the ends of shortening microtubules and use energy from tubulin depolymerization to pull a load in the minus end direction. These results, together with the spindle localizations of these proteins in vivo and their requirement for cell viability in the absence of the Dam1/DASH kinetochore complex, support the hypothesis that fission yeast kinesin-8 contributes both to chromosome congression to the metaphase plate and to the coupling of spindle microtubules to kinetochores during anaphase A.","authors":"Grissom PM, Fiedler T, Grishchuk EL, Nicastro D, West RR, McIntosh JR","authors_abbrev":"Grissom PM et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-11-28","publication_year":"2009","canto_session_key":"9e6658619f3b13c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-01 20:56:43","canto_approved_date":"2023-11-27 08:50:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-10 16:46:45","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.13","SPBC1685.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-01"},{"uniquename":"PMID:24256280","title":"Regulation of chromosome dynamics by Hsk1/Cdc7 kinase.","citation":"Biochem Soc Trans 2013 Dec;41(6):1712-9","abstract":"Hsk1 (homologue of Cdc7 kinase 1) of the fission yeast is a member of the conserved Cdc7 (cell division cycle 7) kinase family, and promotes initiation of chromosome replication by phosphorylating Mcm (minichromosome maintenance) subunits, essential components for the replicative helicase. Recent studies, however, indicate more diverse roles for Hsk1/Cdc7 in regulation of various chromosome dynamics, including initiation of meiotic recombination, meiotic chromosome segregation, DNA repair, replication checkpoints, centromeric heterochromatin formation and so forth. Hsk1/Cdc7, with its unique target specificity, can now be regarded as an important modulator of various chromosome transactions.","doi":"10.1042/BST20130217","authors":"Matsumoto S, Masai H","authors_abbrev":"Matsumoto S et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_session_key":"d93a1f2521dcaa55","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11136247","title":"Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex requires forked DNA structures.","citation":"Proc Natl Acad Sci U S A 2001 Jan 02;98(1):54-9","abstract":"The minichromosome maintenance (Mcm) proteins 2-7 are required for both the initiation and elongation steps of chromosomal DNA replication. Previous studies have shown that the Mcm complex consisting of the Mcm 4, 6, and 7 proteins contains 3' to 5' DNA helicase activity with limited processivity (displacing duplex DNA regions up to 30 nt). In this report, we show that the presence of both 5' and 3' single-stranded tails in DNA helicase substrates is essential for the processive helicase activity of the Mcm complex. The presence of both 5' and 3' tails facilitated the formation of double heterohexameric complexes of Mcm4/6/7 on substrate DNA, which appeared to be essential for the processive helicase activity. The double heterohexameric complex of Mcm4/6/7, in the presence of a single-strand DNA binding protein, is capable of unwinding duplex DNA region of about 600 bp in length. These results support the hypothesis that the Mcm4/6/7 complex can function as a replication helicase.","authors":"Lee JK, Hurwitz J","authors_abbrev":"Lee JK et al.","pubmed_publication_date":"02 Jan 2001","pubmed_entrez_date":"2001-01-03","publication_year":"2001","canto_session_key":"d326837365db1148","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2012-10-04 13:53:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-19 12:12:07","canto_added_date":"2012-09-05 15:32:56","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25D12.03c","SPBC211.04c","SPCC16A11.17"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-09-19"},{"uniquename":"PMID:9309214","title":"The spTRK gene encodes a potassium-specific transport protein TKHp in Schizosaccharomyces pombe.","citation":"J Membr Biol 1997 Sep 01;159(1):95-7","abstract":"","authors":"Bertl A","authors_abbrev":"Bertl A","pubmed_publication_date":"01 Sep 1997","pubmed_entrez_date":"1997-10-06","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR013887","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YDL073W","SPAC7D4.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21604055","title":"Biosorption of Ni (II) by Schizosaccharomyces pombe: kinetic and thermodynamic studies.","citation":"Bioprocess Biosyst Eng 2011 Oct;34(8):997-1005","abstract":"The potential of the dried yeast, wild-type Schizosaccharomyces pombe, to remove Ni(II) ion was investigated in batch mode under varying experimental conditions including pH, temperature, initial metal ion concentration and biosorbent dose. Optimum pH for biosorption was determined as 5.0. The highest equilibrium uptake of Ni(II) on S. pombe, q (e), was obtained at 25 °C as 33.8 mg g(-1). It decreased with increasing temperature within a range of 25-50 °C denoting an exothermic behaviour. Increasing initial Ni(II) concentration up to 400 mg L(-1) also elevated equilibrium uptake. No more adsorption took place beyond 400 mg L(-1). Equilibrium data fitted better to Langmuir model rather than Freundlich model. Sips, Redlich-Peterson, and Kahn isotherm equations modelled the investigated system with a performance not better than Langmuir. Kinetic model evaluations showed that Ni(II) biosorption process followed the pseudo-second order rate model while rate constants decreased with increasing temperature. Gibbs free energy changes (ΔG°) of the system at 25, 30, 35 and 50 °C were found as -1.47E + 4, -1.49E + 4, -1.51E + 4, and -1.58E + 4 J mol(-1), respectively. Enthalpy change (ΔH°) was determined as -2.57E + 3 J mol(-1) which also supports the observed exothermic behaviour of the biosorption process. Entropy change (ΔS°) had a positive value (40.75 J mol(-1) K(-1)) indicating an increase in randomness during biosorption process. Consequently, S. pombe was found to be a potential low-cost agent for Ni(II) in slightly acidic aqueous medium. In parallel, it has been assumed to act as a separating agent for Ni(II) recovery from its aqueous solution.","doi":"10.1007/s00449-011-0550-y","authors":"Durmaz-Sam S, Sayar NA, Topal-Sarikaya A, Sayar AA","authors_abbrev":"Durmaz-Sam S et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-05-24","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29352077","title":"Whole-Genome Sequencing of Suppressor DNA Mixtures Identifies Pathways That Compensate for Chromosome Segregation Defects in  Schizosaccharomyces pombe .","citation":"G3 (Bethesda) 2018 Mar 02;8(3):1031-1038","abstract":"Suppressor screening is a powerful method to identify genes that, when mutated, rescue the temperature sensitivity of the original mutation. Previously, however, identification of suppressor mutations has been technically difficult. Due to the small genome size of  Schizosaccharomyces pombe , we developed a spontaneous suppressor screening technique, followed by a cost-effective sequencing method. Genomic DNAs of 10 revertants that survived at the restrictive temperature of the original temperature sensitive (ts) mutant were mixed together as one sample before constructing a library for sequencing. Responsible suppressor mutations were identified bioinformatically based on allele frequency. Then, we isolated a large number of spontaneous extragenic suppressors for three ts mutants that exhibited defects in chromosome segregation at their restrictive temperature. Screening provided new insight into mechanisms of chromosome segregation: loss of Ufd2 E4 multi-ubiquitination activity suppresses defects of an AAA ATPase, Cdc48. Loss of Wpl1, a releaser of cohesin, compensates for the Eso1 mutation, which may destabilize sister chromatid cohesion. The segregation defect of a ts histone H2B mutant is rescued if it fails to be deubiquitinated by the SAGA complex, because H2B is stabilized by monoubiquitination.","doi":"10.1534/g3.118.200048","authors":"Xu X, Wang L, Yanagida M","authors_abbrev":"Xu X et al.","pubmed_publication_date":"02 Mar 2018","pubmed_entrez_date":"2018-01-21","publication_year":"2018","canto_session_key":"865ebc50ec806a07","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xingya Xu","canto_first_approved_date":"2019-05-26 16:07:42","canto_approved_date":"2023-09-21 09:44:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-17 20:26:53","canto_added_date":"2018-01-22 01:15:16","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Xingya Xu","community_curator":true,"annotation_count":8,"orcid":"0000-0002-3728-2633","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.18c","SPAC20H4.10","SPBC16A3.11","SPAC1952.05","SPAC13A11.04c","SPBC428.17c","SPCC622.09","SPAC57A10.14","SPBC6B1.12c","SPAC1565.08"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2019-05-26"},{"uniquename":"PMID:35584672","title":"The transcription factor Atf1 lowers the transition barrier for nucleosome-mediated establishment of heterochromatin.","citation":"Cell Rep 2022 May 17;39(7):110828","abstract":"Transcription factors can exert opposite effects depending on the chromosomal context. The fission yeast transcription factor Atf1 both activates numerous genes in response to stresses and mediates heterochromatic gene silencing in the mating-type region. Investigating this context dependency, we report here that the establishment of silent heterochromatin in the mating-type region occurs at a reduced rate in the absence of Atf1 binding. Quantitative modeling accounts for the observed establishment profiles by a combinatorial recruitment of histone-modifying enzymes: locally by Atf1 at two binding sites and over the whole region by dynamically appearing heterochromatic nucleosomes, a source of which is the RNAi-dependent cenH element. In the absence of Atf1 binding, the synergy is lost, resulting in a slow rate of heterochromatin formation. The system shows how DNA-binding proteins can influence local nucleosome states and thereby potentiate long-range positive feedback on histone-modification reactions to enable heterochromatin formation over large regions in a context-dependent manner.","doi":"10.1016/j.celrep.2022.110828","authors":"Nickels JF, Della-Rosa ME, Miguelez Goyeneche I, Charlton SJ, Sneppen K, Thon G","authors_abbrev":"Nickels JF et al.","pubmed_publication_date":"17 May 2022","pubmed_entrez_date":"2022-05-18","publication_year":"2022","canto_session_key":"761e54d503305159","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-05-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007984","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34830299","title":"DNA Repair in Haploid Context.","citation":"Int J Mol Sci 2021 Nov 17;22(22)","abstract":"DNA repair is a well-covered topic as alteration of genetic integrity underlies many pathological conditions and important transgenerational consequences. Surprisingly, the ploidy status is rarely considered although the presence of homologous chromosomes dramatically impacts the repair capacities of cells. This is especially important for the haploid gametes as they must transfer genetic information to the offspring. An understanding of the different mechanisms monitoring genetic integrity in this context is, therefore, essential as differences in repair pathways exist that differentiate the gamete's role in transgenerational inheritance. Hence, the oocyte must have the most reliable repair capacity while sperm, produced in large numbers and from many differentiation steps, are expected to carry de novo variations. This review describes the main DNA repair pathways with a special emphasis on ploidy. Differences between  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe  are especially useful to this aim as they can maintain a diploid and haploid life cycle respectively.","doi":"10.3390/ijms222212418","authors":"Mourrain L, Boissonneault G","authors_abbrev":"Mourrain L et al.","pubmed_publication_date":"17 Nov 2021","pubmed_entrez_date":"2021-11-27","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-11-29 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21098121","title":"Fission yeast Pot1 and RecQ helicase are required for efficient chromosome segregation.","citation":"Mol Cell Biol 2011 Feb;31(3):495-506","abstract":"Pot1 is a single-stranded telomere-binding protein that is conserved from fission yeast to mammals. Deletion of Schizosaccharomyces pombe pot1(+) causes immediate telomere loss. S. pombe Rqh1 is a homolog of the human RecQ helicase WRN, which plays essential roles in the maintenance of genomic stability. Here, we demonstrate that a pot1Δ rqh1-hd (helicase-dead) double mutant maintains telomeres that are dependent on Rad51-mediated homologous recombination. Interestingly, the pot1Δ rqh1-hd double mutant displays a \"cut\" (cell untimely torn) phenotype and is sensitive to the antimicrotubule drug thiabendazole (TBZ). Moreover, the chromosome ends of the double mutant do not enter the pulsed-field electrophoresis gel. These results suggest that the entangled chromosome ends in the pot1Δ rqh1-hd double mutant inhibit chromosome segregation, signifying that Pot1 and Rqh1 are required for efficient chromosome segregation. We also found that POT1 knockdown, WRN-deficient human cells are sensitive to the antimicrotubule drug vinblastine, implying that some of the functions of S. pombe Pot1 and Rqh1 may be conserved in their respective human counterparts POT1 and WRN.","doi":"10.1128/MCB.00613-10","authors":"Takahashi K, Imano R, Kibe T, Seimiya H, Muramatsu Y, Kawabata N, Tanaka G, Matsumoto Y, Hiromoto T, Koizumi Y, Nakazawa N, Yanagida M, Yukawa M, Tsuchiya E, Ueno M","authors_abbrev":"Takahashi K et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2010-11-25","publication_year":"2011","canto_session_key":"0a627529fc025c31","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-23 14:05:59","canto_approved_date":"2021-10-21 22:04:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-23 14:05:51","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26H5.06","SPAC2G11.12","SPAC644.14c","SPCC1259.13"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-10-23"},{"uniquename":"PMID:15120067","title":"Microtubule nucleation at non-spindle pole body microtubule-organizing centers requires fission yeast centrosomin-related protein mod20p.","citation":"Curr Biol 2004 May 04;14(9):763-75","abstract":"Many types of differentiated eukaryotic cells display microtubule distributions consistent with nucleation from noncentrosomal intracellular microtubule organizing centers (MTOCs), although such structures remain poorly characterized. In fission yeast, two types of MTOCs exist in addition to the spindle pole body, the yeast centrosome equivalent. These are the equatorial MTOC, which nucleates microtubules from the cell division site at the end of mitosis, and interphase MTOCs, which nucleate microtubules from multiple sites near the cell nucleus during interphase.\nFrom an insertional mutagenesis screen we identified a novel gene, mod20+, which is required for microtubule nucleation from non-spindle pole body MTOCs in fission yeast. Mod20p is not required for intranuclear mitotic spindle assembly, although it is required for cytoplasmic astral microtubule growth during mitosis. Mod20p localizes to MTOCs throughout the cell cycle and is also dynamically distributed along microtubules themselves. We find that mod20p is required for the localization of components of the gamma-tubulin complex to non-spindle pole body MTOCs and physically interacts with the gamma-tubulin complex in vivo. Database searches reveal a family of eukaryotic proteins distantly related to mod20p; these are found in organisms ranging from fungi to mammals and include Drosophila centrosomin.\nMod20p appears to act by recruiting components of the gamma-tubulin complex to non-spindle pole body MTOCs. The identification of mod20p-related proteins in higher eukaryotes suggests that this may represent a general mechanism for the organization of noncentrosomal MTOCs in eukaryotic cells.","authors":"Sawin KE, Lourenco PC, Snaith HA","authors_abbrev":"Sawin KE et al.","pubmed_publication_date":"04 May 2004","pubmed_entrez_date":"2004-05-04","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC365.15","SPCC417.07c","SPBC428.20c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10471699","title":"Centromere mapping functions for aneuploid meiotic products: Analysis of rec8, rec10 and rec11 mutants of the fission yeast Schizosaccharomyces pombe.","citation":"Genetics 1999 Sep;153(1):49-55","abstract":"Recent evidence suggests that the position of reciprocal recombination events (crossovers) is important for the segregation of homologous chromosomes during meiosis I and sister chromatids during meiosis II. We developed genetic mapping functions that permit the simultaneous analysis of centromere-proximal crossover recombination and the type of segregation error leading to aneuploidy. The mapping functions were tested in a study of the rec8, rec10, and rec11 mutants of fission yeast. In each mutant we monitored each of the three chromosome pairs. Between 38 and 100% of the chromosome segregation errors in the rec8 mutants were due to meiosis I nondisjunction of homologous chromosomes. The remaining segregation errors were likely the result of precocious separation of sister chromatids, a previously described defect in the rec8 mutants. Between 47 and 100% of segregation errors in the rec10 and rec11 mutants were due to nondisjunction of sister chromatids during meiosis II. In addition, centromere-proximal recombination was reduced as much as 14-fold or more on chromosomes that had experienced nondisjunction. These results demonstrate the utility of the new mapping functions and support models in which sister chromatid cohesion and crossover position are important determinants for proper chromosome segregation in each meiotic division.","authors":"Krawchuk MD, Wahls WP","authors_abbrev":"Krawchuk MD et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-09-03","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33023973","title":"Preventing Photomorbidity in Long-Term Multi-color Fluorescence Imaging of  Saccharomyces cerevisiae  and  S. pombe .","citation":"G3 (Bethesda) 2020 Dec 03;10(12):4373-4385","abstract":"Time-lapse imaging of live cells using multiple fluorescent reporters is an essential tool to study molecular processes in single cells. However, exposure to even moderate doses of visible excitation light can disturb cellular physiology and alter the quantitative behavior of the cells under study. Here, we set out to develop guidelines to avoid the confounding effects of excitation light in multi-color long-term imaging. We use widefield fluorescence microscopy to measure the effect of the administered excitation light on growth rate (here called photomorbidity) in yeast. We find that photomorbidity is determined by the cumulative light dose at each wavelength, but independent of the way excitation light is applied. Importantly, photomorbidity possesses a threshold light dose below which no effect is detectable (NOEL). We found, that the suitability of fluorescent proteins for live-cell imaging at the respective excitation light NOEL is equally determined by the cellular autofluorescence and the fluorescent protein brightness. Last, we show that photomorbidity of multiple wavelengths is additive and imaging conditions absent of photomorbidity can be predicted. Our findings enable researchers to find imaging conditions with minimal impact on physiology and can provide framework for how to approach photomorbidity in other organisms.","doi":"10.1534/g3.120.401465","authors":"Schmidt GW, Cuny AP, Rudolf F","authors_abbrev":"Schmidt GW et al.","pubmed_publication_date":"03 Dec 2020","pubmed_entrez_date":"2020-10-07","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-10-09 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17199038","title":"Priming of centromere for CENP-A recruitment by human hMis18alpha, hMis18beta, and M18BP1.","citation":"Dev Cell 2007 Jan;12(1):17-30","abstract":"The centromere is the chromosomal site that joins to microtubules during mitosis for proper segregation. Determining the location of a centromere-specific histone H3 called CENP-A at the centromere is vital for understanding centromere structure and function. Here, we report the identification of three human proteins essential for centromere/kinetochore structure and function, hMis18alpha, hMis18beta, and M18BP1, the complex of which is accumulated specifically at the telophase-G1 centromere. We provide evidence that such centromeric localization of hMis18 is essential for the subsequent recruitment of de novo-synthesized CENP-A. If any of the three is knocked down by RNAi, centromere recruitment of newly synthesized CENP-A is rapidly abolished, followed by defects such as misaligned chromosomes, anaphase missegregation, and interphase micronuclei. Tricostatin A, an inhibitor to histone deacetylase, suppresses the loss of CENP-A recruitment to centromeres in hMis18alpha RNAi cells. Telophase centromere chromatin may be primed or licensed by the hMis18 complex and RbAp46/48 to recruit CENP-A through regulating the acetylation status in the centromere.","authors":"Fujita Y, Hayashi T, Kiyomitsu T, Toyoda Y, Kokubu A, Obuse C, Yanagida M","authors_abbrev":"Fujita Y et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2007-01-03","publication_year":"2007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC970.12"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:28973473","title":"Transcription-induced supercoiling explains formation of self-interacting chromatin domains in S. pombe.","citation":"Nucleic Acids Res 2017 Sep 29;45(17):9850-9859","abstract":"The question of how self-interacting chromatin domains in interphase chromosomes are structured and generated dominates current discussions on eukaryotic chromosomes. Numerical simulations using standard polymer models have been helpful in testing the validity of various models of chromosome organization. Experimental contact maps can be compared with simulated contact maps and thus verify how good is the model. With increasing resolution of experimental contact maps, it became apparent though that active processes need to be introduced into models to recapitulate the experimental data. Since transcribing RNA polymerases are very strong molecular motors that induce axial rotation of transcribed DNA, we present here models that include such rotational motors. We also include into our models swivels and sites for intersegmental passages that account for action of DNA topoisomerases releasing torsional stress. Using these elements in our models, we show that transcription-induced supercoiling generated in the regions with divergent-transcription and supercoiling relaxation occurring between these regions are sufficient to explain formation of self-interacting chromatin domains in chromosomes of fission yeast (S. pombe).","doi":"10.1093/nar/gkx716","authors":"Benedetti F, Racko D, Dorier J, Burnier Y, Stasiak A","authors_abbrev":"Benedetti F et al.","pubmed_publication_date":"29 Sep 2017","pubmed_entrez_date":"2017-10-04","publication_year":"2017","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2017-10-05 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20537132","title":"Global fitness profiling of fission yeast deletion strains by barcode sequencing.","citation":"Genome Biol 2010;11(6):R60","abstract":"A genome-wide deletion library is a powerful tool for probing gene functions and one has recently become available for the fission yeast Schizosaccharomyces pombe. Here we use deep sequencing to accurately characterize the barcode sequences in the deletion library, thus enabling the quantitative measurement of the fitness of fission yeast deletion strains by barcode sequencing.","doi":"10.1186/gb-2010-11-6-r60","authors":"Han TX, Xu XY, Zhang MJ, Peng X, Du LL","authors_abbrev":"Han TX et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-06-12","publication_year":"2010","canto_session_key":"9a1ee9bbbbedad58","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-18 17:02:55","canto_approved_date":"2021-10-01 16:02:43","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-18 17:02:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":257,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_20537132_phaf.tsv"}],"genes":["SPAC24C9.05c","SPBC2G2.14","SPAC14C4.13","SPBC3D6.04c","SPAC8E11.02c","SPBC365.14c","SPBC23E6.08","SPBC1105.02c","SPAC16.01","SPCC1753.02c","SPCC18B5.11c","SPBC342.06c","SPAC2F7.10","SPCC1739.15","SPCC4F11.03c","SPBC1685.06","SPBC28F2.10c","SPAC19E9.02","SPCC825.03c","SPCC1393.05","SPCC1322.03","SPAC8C9.17c","SPAC17H9.10c","SPBC725.10","SPAC11G7.02","SPBC16E9.14c","SPAPB1A10.09","SPAC3A11.13","SPBC27B12.11c","SPBC119.08","SPAC25A8.01c","SPAC227.07c","SPBC1921.04c","SPAC30D11.04c","SPAC1F12.09","SPAC664.01c","SPAC19A8.04","SPCC1235.09","SPCC757.09c","SPBC2A9.08c","SPCC417.02","SPAC1093.01","SPBC1703.12","SPBC2G2.01c","SPBC17A3.10","SPAC23D3.09","SPAC1805.04","SPAC6G9.14","SPAC15E1.06","SPAC1556.03","SPBC660.11","SPCC550.12","SPBC30D10.04","SPAC343.12","SPAC23C11.04c","SPCC584.11c","SPBC1703.14c","SPAC11E3.08c","SPCC736.02","SPAC18G6.15","SPAC6B12.02c","SPBC8E4.05c","SPAC1071.04c","SPCC1393.08","SPAC18G6.02c","SPBC1734.06","SPAC3G6.06c","SPBC14C8.17c","SPAC2G11.06","SPBC2G2.10c","SPCC613.12c","SPCC126.15c","SPBC27.06c","SPAC56F8.02","SPCC4B3.08","SPAC227.18","SPAC19A8.11c","SPCC777.13","SPBC15C4.04c","SPBC8D2.03c","SPCC285.09c","SPCC1494.08c","SPCC306.04c","SPAC694.06c","SPCC4G3.11","SPBC947.08c","SPAC959.04c","SPBP8B7.28c","SPAC343.16","SPBC649.03","SPBC215.03c","SPAC31G5.04","SPCC1020.08","SPBC13G1.08c","SPBC409.15","SPAC140.03","SPAC4D7.07c","SPBC12C2.02c","SPCP31B10.05","SPAC20H4.07","SPAC3G6.11","SPAC30C2.02","SPBC365.11","SPBC1773.11c","SPAC9G1.05","SPAC806.05","SPAC17C9.02c","SPAC20G4.04c","SPAC23H3.13c","SPCC330.03c","SPCC4G3.14","SPAC1610.03c","SPBC2G2.13c","SPAC18G6.10","SPBC36.06c","SPAC4G9.13c","SPAC9G1.12","SPAC1A6.04c","SPBC1289.06c","SPAC3H5.08c","SPAC823.04","SPAC664.07c","SPCC1442.04c","SPBC31F10.13c","SPBC651.09c","SPCC11E10.08","SPBC354.03","SPCC663.12","SPCC1442.02","SPBC354.07c","SPBC1604.08c","SPBC8D2.17","SPAC24H6.03","SPAC1782.09c","SPBC1D7.04","SPBC2D10.13","SPBC2F12.11c","SPAC1F3.02c","SPCP1E11.05c","SPAC1399.02","SPBC543.07","SPBC725.09c","SPCC790.02","SPCC162.11c","SPAC824.05","SPBC1685.15c","SPBC428.08c","SPCC553.01c","SPBC18H10.19","SPCC23B6.05c","SPAC29B12.04","SPAC23H3.08c","SPBC20F10.05","SPCC594.05c","SPBC3B8.05","SPAC13G6.01c","SPCC553.08c","SPAC26H5.05","SPBC21C3.02c","SPAC1782.05","SPAC11E3.04c","SPAC823.05c","SPAC1952.07","SPAC17H9.11","SPAC1D4.03c","SPAC29B12.03","SPBC16G5.06","SPCC1739.10","SPBC27.02c","SPBC106.10","SPAPB1A11.01","SPBC428.06c","SPAP7G5.04c","SPBC19G7.09","SPBC800.05c","SPAC15A10.03c","SPCC162.10","SPBC29A3.14c","SPBC20F10.07","SPBP8B7.16c","SPAC2G11.13","SPBC27B12.06","SPBP4H10.04","SPAC1805.07c","SPCC895.07","SPBC776.04","SPAC6F6.01","SPAC31A2.15c","SPCC594.01","SPAC3H8.05c","SPAC16E8.13","SPAC1783.07c","SPAC19G12.08","SPBC342.05","SPBC800.08","SPCC338.08","SPAC1952.05","SPAC17C9.13c","SPBC13E7.03c","SPAC13G7.07","SPBC3E7.08c","SPAC959.07","SPBC3B8.03","SPAC30C2.07","SPCC736.08","SPCC1620.11","SPBC2D10.12","SPAC4A8.09c","SPCC1322.06","SPAC1F8.06","SPAC12B10.12c","SPBC3B9.11c","SPCC18.06c","SPAC9.02c"],"gene_count":214,"ltp_gene_count":2,"approved_date":"2015-02-18"},{"uniquename":"PMID:8635463","title":"Pub1 acts as an E6-AP-like protein ubiquitiin ligase in the degradation of cdc25.","citation":"EMBO J 1996 Mar 15;15(6):1301-12","abstract":"The level of the mitotic activating tyrosine phosphatase cdc25 is regulated by both transcriptional and post-transcriptional mechanisms in the fission yeast Schizosaccharomyces pombe. We have found that cdc25 is ubiquitinated and have cloned pub1, a gene which regulates this event. Pub1 contains a region highly homologous to the putative catalytic domain of the human protein ubiquitin ligase E6-AP. Disruption of pub1 elevates the level of cdc25 protein in vivo rendering cells relatively resistant to the cdc25-opposing tyrosine kinases wee1 and mik1. In addition, loss of wee1 activity in a pub1-disruption background results in a lethal premature entry into mitosis which can be rescued by loss of cdc25 function. A ubiquitin-thioester adduct of pub1 was isolated from fission yeast and disruption of pub1 dramatically reduced ubiquitination of cdc25 in vivo. These results suggest that pub1 directly ubiquitinates cdc25 in vivo.","authors":"Nefsky B, Beach D","authors_abbrev":"Nefsky B et al.","pubmed_publication_date":"15 Mar 1996","pubmed_entrez_date":"1996-03-15","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC24H6.05","SPAC11G7.02","SPCC18B5.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:35924983","title":"Genetic-interaction screens uncover novel biological roles and regulators of transcription factors in fission yeast.","citation":"G3 (Bethesda) 2022 Aug 25;12(9)","abstract":"In Schizosaccharomyces pombe, systematic analyses of single transcription factor deletion or overexpression strains have made substantial advances in determining the biological roles and target genes of transcription factors, yet these characteristics are still relatively unknown for over a quarter of them. Moreover, the comprehensive list of proteins that regulate transcription factors remains incomplete. To further characterize Schizosaccharomyces pombe transcription factors, we performed synthetic sick/lethality and synthetic dosage lethality screens by synthetic genetic array. Examination of 2,672 transcription factor double deletion strains revealed a sick/lethality interaction frequency of 1.72%. Phenotypic analysis of these sick/lethality strains revealed potential cell cycle roles for several poorly characterized transcription factors, including SPBC56F2.05, SPCC320.03, and SPAC3C7.04. In addition, we examined synthetic dosage lethality interactions between 14 transcription factors and a miniarray of 279 deletion strains, observing a synthetic dosage lethality frequency of 4.99%, which consisted of known and novel transcription factor regulators. The miniarray contained deletions of genes that encode primarily posttranslational-modifying enzymes to identify putative upstream regulators of the transcription factor query strains. We discovered that ubiquitin ligase Ubr1 and its E2/E3-interacting protein, Mub1, degrade the glucose-responsive transcriptional repressor Scr1. Loss of ubr1+ or mub1+ increased Scr1 protein expression, which resulted in enhanced repression of flocculation through Scr1. The synthetic dosage lethality screen also captured interactions between Scr1 and 2 of its known repressors, Sds23 and Amk2, each affecting flocculation through Scr1 by influencing its nuclear localization. Our study demonstrates that sick/lethality and synthetic dosage lethality screens can be effective in uncovering novel functions and regulators of Schizosaccharomyces pombe transcription factors.","doi":"10.1093/g3journal/jkac194","authors":"Chatfield-Reed K, Marno Jones K, Shah F, Chua G","authors_abbrev":"Chatfield-Reed K et al.","pubmed_publication_date":"25 Aug 2022","pubmed_entrez_date":"2022-08-04","publication_year":"2022","canto_session_key":"02289de0acddb1f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kurtis Marno Jones","canto_first_approved_date":"2023-07-31 08:03:25","canto_approved_date":"2024-03-30 08:09:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-12 17:49:52","canto_added_date":"2022-08-06 00:15:04","annotation_curators":[{"name":"Kurtis Marno Jones","community_curator":true,"annotation_count":98,"orcid":null,"file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":3,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.06","SPAC22F3.09c","SPBC31F10.10c","SPAC2F7.11","SPAC3F10.12c","SPAC4G8.13c","SPAC25B8.19c","SPAC1039.05c","SPAC3C7.04","SPBC19C7.02","SPCC1739.12","SPBC19G7.06","SPCC1223.11","SPCC1393.08","SPBP4H10.09","SPBC56F2.05c","SPCC584.02","SPAC18B11.07c","SPAC6G10.12c","SPAC31A2.11c","SPCC736.08","SPAC11E3.04c","SPBC32C12.03c","SPAC23H4.12","SPAC3H1.03","SPCC1020.10","SPAC25G10.03","SPAC139.06","SPAC23C11.08","SPAC17H9.19c","SPCC24B10.07","SPBC1105.14","SPAC1399.05c","SPBC4C3.12","SPBC646.13","SPAC139.03","SPAC19B12.07c","SPBC19G7.04","SPBC530.08","SPAC8C9.14","SPBC15D4.02","SPAC11E3.06","SPAC3H8.08c","SPCC1919.15","SPCC18B5.03","SPAC644.06c","SPBC23G7.09","SPBC21B10.13c","SPBC354.05c","SPAC23E2.01","SPCC306.04c","SPBC1D7.02c","SPAC22F8.12c","SPCC18B5.11c","SPCC1919.03c","SPBC2F12.09c","SPAC31G5.10","SPCC16C4.11","SPBC29A10.12","SPAC13A11.04c","SPAC16.05c","SPCC320.03","SPAC1783.07c","SPAC56F8.16","SPBC1921.07c","SPAC1F7.11c","SPBC1773.12","SPAP14E8.02","SPCC1223.13","SPBC28F2.08c"],"gene_count":70,"ltp_gene_count":62,"approved_date":"2023-07-31"},{"uniquename":"EMBL:AU013561","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17182615","title":"Regulation of Schizosaccharomyces pombe Atf1 protein levels by Sty1-mediated phosphorylation and heterodimerization with Pcr1.","citation":"J Biol Chem 2007 Feb 23;282(8):5160-70","abstract":"The Atf1 transcription factor plays a vital role in the ability of Schizosaccharomyces pombe cells to respond to various stress conditions. It regulates the expression of many genes in a stress-dependent manner, and its function is dependent upon the stress-activated MAPK, Sty1/Spc1. Moreover, Atf1 is directly phosphorylated by Sty1. Here we have investigated the role of such phosphorylation. Atf1 protein accumulates following stress, and this accumulation is lost in a strain defective in the Sty1 signaling pathway. In addition, accumulation of a mutant Atf1 protein that can no longer be phosphorylated is lost. Measurement of the half-life of Atf1 demonstrates that changes in Atf1 stability are responsible for this accumulation. Atf1 stability is also regulated by its heterodimeric partner, Pcr1. Similarly, Pcr1 levels are regulated by Atf1. Thus multiple pathways exist that ensure that Atf1 levels are appropriately regulated. Phosphorylation of Atf1 is important for cells to mount a robust response to H(2)O(2) stress, because the Atf1 phospho-mutant displays sensitivity to this stress, and induction of gene expression is lower than that observed in wild-type cells. Surprisingly, however, loss of Atf1 phosphorylation does not lead to the complete loss of stress-activated expression of Atf1 target genes. Accordingly, the Atf1 phospho-mutant does not display the same overall stress sensitivities as the atf1 deletion mutant. Taken together, these data suggest that Sty1 phosphorylation of Atf1 is not required for activation of Atf1 per se but rather for modulating its stability.","authors":"Lawrence CL, Maekawa H, Worthington JL, Reiter W, Wilkinson CR, Jones N","authors_abbrev":"Lawrence CL et al.","pubmed_publication_date":"23 Feb 2007","pubmed_entrez_date":"2006-12-22","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12953049","title":"DNA checkpoints in fission yeast.","citation":"J Cell Sci 2003 Oct 01;116(Pt 19):3847-8","abstract":"","authors":"Furuya K, Carr AM","authors_abbrev":"Furuya K et al.","pubmed_publication_date":"01 Oct 2003","pubmed_entrez_date":"2003-09-04","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28178520","title":"Identification of a Sgo2-Dependent but Mad2-Independent Pathway Controlling Anaphase Onset in Fission Yeast.","citation":"Cell Rep 2017 Feb 07;18(6):1422-1433","abstract":"The onset of anaphase is triggered by activation of the anaphase-promoting complex/cyclosome (APC/C) following silencing of the spindle assembly checkpoint (SAC). APC/C triggers ubiquitination of Securin and Cyclin B, which leads to loss of sister chromatid cohesion and inactivation of Cyclin B/Cdk1, respectively. This promotes relocalization of Aurora B kinase and other components of the chromosome passenger complex (CPC) from centromeres to the spindle midzone. In fission yeast, this is mediated by Clp1 phosphatase-dependent interaction of CPC with Klp9/MKLP2 (kinesin-6). When this interaction is disrupted, kinetochores bi-orient normally, but APC/C activation is delayed via a mechanism that requires Sgo2 and some (Bub1, Mph1/Mps1, and Mad3), but not all (Mad1 and Mad2), components of the SAC and the first, but not second, lysine, glutamic acid, glutamine (KEN) box in Mad3. These data indicate that interaction of CPC with Klp9 terminates a Sgo2-dependent, but Mad2-independent, APC/C-inhibitory pathway that is distinct from the canonical SAC.","doi":"10.1016/j.celrep.2017.01.032","authors":"Meadows JC, Lancaster TC, Buttrick GJ, Sochaj AM, Messin LJ, Del Mar Mora-Santos M, Hardwick KG, Millar JBA","authors_abbrev":"Meadows JC et al.","pubmed_publication_date":"07 Feb 2017","pubmed_entrez_date":"2017-02-09","publication_year":"2017","canto_session_key":"1823b4aa025cae13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"John C Meadows","canto_first_approved_date":"2018-08-13 10:26:10","canto_approved_date":"2023-05-03 15:53:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-13 10:23:34","canto_added_date":"2017-02-10 01:15:10","annotation_curators":[{"name":"John C Meadows","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":83,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.12","SPAC17G8.10c","SPAC18G6.15","SPAC821.08c","SPBC20F10.06","SPBC336.15","SPBC106.01","SPCC320.13c","SPCC1322.12c","SPBC3D6.04c","SPAC23H3.08c","SPAC1782.09c","SPCC1795.01c","SPAPB1A10.09","SPBC15D4.01c","SPAC3G9.12","SPBC11B10.09","SPBC582.03","SPAC15A10.15","SPCC962.02c"],"gene_count":20,"ltp_gene_count":16,"approved_date":"2018-08-13"},{"uniquename":"PMID:8514114","title":"Rapid, extensive and reversible vacuolation of Schizosaccharomyces pombe induced by amphotericin B.","citation":"FEMS Microbiol Lett 1993 Apr 15;108(3):265-9","abstract":"The fission yeast Schizosaccharomyces pombe has no large vacuoles under normal growth conditions, although budding yeasts usually have large central vacuoles. The minimum inhibitory concentration of amphotericin B to S. pombe was 0.5 microgram ml-1; treatment with 0.2 microgram ml-1 for 20 min induced rapid and extensive vacuolation in S. pombe exponential phase cells. Growth rate of the cells with 0.2 microgram ml-1 amphotericin B was much reduced for 6 h, showing extensive vacuolation. Vacuolation in itself was not fatal: on removal of the drug, most cells recovered gradually and eventually multiplied.","authors":"Takeo K, Yarita K, Yoshida S, Guan HQ, Nishimura K, Miyaji M","authors_abbrev":"Takeo K et al.","pubmed_publication_date":"15 Apr 1993","pubmed_entrez_date":"1993-04-15","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21670547","title":"Fission yeast homologs of human XPC and CSB, rhp41 and rhp26, are involved in transcription-coupled repair of methyl methanesulfonate-induced DNA damage.","citation":"Genes Genet Syst 2011;86(2):83-91","abstract":"Methyl methanesulfonate (MMS) methylates nitrogen atoms in purines, and predominantly produces 7-methylguanine and 3-methyladenine (3-meA). Previously, we showed that base excision repair (BER) and nucleotide excision repair (NER) synergistically function to repair MMS-induced DNA damage in the fission yeast Schizosaccharomyces pombe. Here, we studied the roles of NER components in repair of 3-meA and BER intermediates such as the AP site and single strand breaks. Mutants of rhp41 (XPC homolog) and rhp26 (CSB homolog) exhibited moderate sensitivity to MMS. Transcription of the fbp1 gene, which is induced by glucose starvation, was strongly inhibited by MMS damage in rhp41Δ and rhp26Δ strains but not in wild type and 3-meA DNA glycosylase-deficient cells. The results indicate that Rhp41p and Rhp26p are involved in transcription-coupled repair (TCR) of MMS-induced DNA damage. In the BER pathway of S. pombe, AP lyase activity of Nth1p mainly incises the AP site to generate a 3'-blocked end, which is in turn converted to 3'-OH by Apn2p. Deletion of rad16 or rhp26 in the nth1Δ strain greatly enhanced MMS sensitivity, suggesting that the AP site could also be corrected by TCR. Double mutant apn2Δ/rad16Δ exhibited hypersensitivity to MMS, implying that Rad16p provides a backup pathway for removal of the 3'-blocked end. Moreover, an rhp51Δ strain was extremely sensitive to MMS and double mutants of nth1Δ/rhp51Δ and apn2Δ/rhp51Δ increased the sensitivity, suggesting that homologous recombination is necessary for repair of three different types of lesions, 3-meA, AP sites and 3'-blocked ends.","authors":"Kanamitsu K, Ikeda S","authors_abbrev":"Kanamitsu K et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-06-15","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC12B10.12c","SPCP25A2.02c","SPCC970.01","SPAC30D11.07","SPAC644.14c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:15947136","title":"RNA polymerase II is required for RNAi-dependent heterochromatin assembly.","citation":"Science 2005 Jul 15;309(5733):467-9","abstract":"In Schizosaccharomyces pombe, the RNA interference (RNAi) machinery converts pericentromeric transcripts into small interfering RNAs (siRNAs) and is required for the assembly of pericentromeric heterochromatin. Here we describe a mutation in the second largest subunit of RNA polymerase II (RNAPII). Both wild-type and mutant RNAPII localized to the pericentromere. However, the mutation resulted in the loss of heterochromatic histone modifications and in the accumulation of pericentromeric transcripts, accompanied by the loss of siRNAs. This phenotype resembles mutants in RNAi and suggests that RNAPII couples pericentromeric transcription with siRNA processing and heterochromatin assembly.","authors":"Kato H, Goto DB, Martienssen RA, Urano T, Furukawa K, Murakami Y","authors_abbrev":"Kato H et al.","pubmed_publication_date":"15 Jul 2005","pubmed_entrez_date":"2005-06-11","publication_year":"2005","canto_session_key":"031cfd5b4b226346","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroaki Kato","canto_first_approved_date":"2016-02-09 10:12:03","canto_approved_date":"2026-01-26 11:40:05","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-06-27 18:40:58","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Hiroaki Kato","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c","SPAC23G3.01","SPBC1683.06c","SPBC428.08c","SPAC664.01c","SPBC3E7.02c"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2016-02-09"},{"uniquename":"PMID:38662722","title":"Chromodomain mutation in S. pombe Kat5/Mst1 affects centromere dynamics and DNA repair.","citation":"PLoS One 2024;19(4):e0300732","abstract":"KAT5 (S. pombe Mst1, human TIP60) is a MYST family histone acetyltransferase conserved from yeast to humans that is involved in multiple cellular activities. This family is characterized in part by containing a chromodomain, a motif associated with binding methylated histones. We show that a chromodomain mutation in the S. pombe Kat5, mst1-W66R, has defects in pericentromere silencing. mst1-W66R is sensitive to camptothecin (CPT) but only at an increased temperature of 36°C, although it is proficient for growth at this temperature. We also describe a de-silencing effect at the pericentromere by CPT that is independent of RNAi and methylation machinery. We also show that mst1-W66R disrupts recruitment of proteins to repair foci in response to camptothecin-induced DNA damage. Our data suggest a function of Mst1 chromodomain in centromere heterochromatin formation and a separate role in genome-wide damage repair in CPT.","doi":"10.1371/journal.pone.0300732","authors":"Li T, Petreaca RC, Forsburg SL","authors_abbrev":"Li T et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-04-25","publication_year":"2024","canto_session_key":"3c67057f2f646978","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-04-25 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19040720","title":"Chromatin Central: towards the comparative proteome by accurate mapping of the yeast proteomic environment.","citation":"Genome Biol 2008;9(11):R167","abstract":"Understanding the design logic of living systems requires the understanding and comparison of proteomes. Proteomes define the commonalities between organisms more precisely than genomic sequences. Because uncertainties remain regarding the accuracy of proteomic data, several issues need to be resolved before comparative proteomics can be fruitful.\nThe Saccharomyces cerevisiae proteome presents the highest quality proteomic data available. To evaluate the accuracy of these data, we intensively mapped a proteomic environment, termed 'Chromatin Central', which encompasses eight protein complexes, including the major histone acetyltransferases and deacetylases, interconnected by twelve proteomic hyperlinks. Using sequential tagging and a new method to eliminate background, we confirmed existing data but also uncovered new subunits and three new complexes, including ASTRA, which we suggest is a widely conserved aspect of telomeric maintenance, and two new variations of Rpd3 histone deacetylase complexes. We also examined the same environment in fission yeast and found a very similar architecture based on a scaffold of orthologues comprising about two-thirds of all proteins involved, whereas the remaining one-third is less constrained. Notably, most of the divergent hyperlinks were found to be due to gene duplications, hence providing a mechanism for the fixation of gene duplications in evolution.\nWe define several prerequisites for comparative proteomics and apply them to examine a proteomic environment in unprecedented detail. We suggest that high resolution mapping of proteomic environments will deliver the highest quality data for comparative proteomics.","doi":"10.1186/gb-2008-9-11-r167","authors":"Shevchenko A, Roguev A, Schaft D, Buchanan L, Habermann B, Sakalar C, Thomas H, Krogan NJ, Shevchenko A, Stewart AF","authors_abbrev":"Shevchenko A et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-12-02","publication_year":"2008","canto_session_key":"1dc316e1d9598252","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-09-11 16:05:47","canto_approved_date":"2024-03-04 12:45:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 08:27:21","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.06c","SPAC637.12c","SPAC25B8.02","SPCC1450.02","SPCC576.13","SPBC1734.16c","SPBP35G2.13c","SPAC222.04c","SPAC4H3.02c","SPBC83.08","SPAC1F5.11c","SPAC16C9.05","SPAC17G8.07","SPAC23H4.12","SPBC21D10.10","SPBC11B10.10c","SPAC23C11.15","SPBC12C2.10c","SPBC1A4.08c","SPCC1259.07","SPCC1235.09","SPAC3G9.07c","SPAC1420.02c","SPAC343.11c","SPBC36.05c","SPAC664.02c","SPAC2F7.07c","SPAC9G1.13c","SPAPB8E5.09","SPAC1D4.04","SPBC646.11","SPBC1685.08","SPAC22E12.11c","SPBC337.05c","SPBC29A3.05","SPCC1682.13","SPCC550.12","SPCC1259.04","SPBC25H2.12c","SPBC21C3.02c","SPAC23G3.04","SPBC365.10","SPAC29A4.18","SPCC830.05c","SPBP23A10.08","SPBC12D12.03","SPAC3G9.08","SPCC1795.08c","SPBC16A3.19","SPAC144.02","SPBC1709.11c","SPBC106.06","SPBC32H8.12c","SPAC29B12.01","SPAPB1E7.14","SPAC14C4.12c","SPAC22E12.19","SPAC11E3.01c"],"gene_count":58,"ltp_gene_count":57,"approved_date":"2014-09-11"},{"uniquename":"PMID:39461006","title":"Decreased mitochondrial translation confers 3,3'-Diindolylmethane resistance to Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2024 Oct 23;736:150864","abstract":"3,3'-Diindolylmethane (DIM), a compound derived from natural fruits and vegetables, is widely recognized for its anti-cancer activity. However, its action mechanisms remain ambiguous. In this study, to study the molecular mechanism of 3,3'-Diindolylmethane, we identified a novel mutation in the gene of mitochondrial translation elongation factor EF-Ts (tsf1 + ), a key factor in mitochondrial protein translation, that conferred DIM resistance to Schizosaccharomyces pombe. The tsf1Δ also conferred DIM resistance. Decreased mitochondrial translation was found to be responsible for conferring DIM resistance to Schizosaccharomyces pombe, as the cells gained DIM resistance after treatment with chloramphenicol, a specific mitochondrial translation inhibitor. Notably, tsf1Δ conferred DIM resistance in the absence of either autophagy-related protein, Atg7, or nuclear envelope protein, Lem2, two proteins that have been reported to be required for cell survival in the presence of DIM. Overall, this study revealed novel biological functions of DIM and highlighted its potential as an anti-cancer agent.","doi":"10.1016/j.bbrc.2024.150864","authors":"Wang K, Nagai H, Rajib SA, Satou Y, Ueno M","authors_abbrev":"Wang K et al.","pubmed_publication_date":"23 Oct 2024","pubmed_entrez_date":"2024-10-26","publication_year":"2024","canto_session_key":"6d3c1e1d0cc97af2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-10-28 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC800.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29331410","title":"Implementing CRISPR-Cas technologies in conventional and non-conventional yeasts: Current state and future prospects.","citation":"Biotechnol Adv 2018;36(3):641-665","abstract":"Within five years, the CRISPR-Cas system has emerged as the dominating tool for genome engineering, while also changing the speed and efficiency of metabolic engineering in conventional (Saccharomyces cerevisiae and Schizosaccharomyces pombe) and non-conventional (Yarrowia lipolytica, Pichia pastoris syn. Komagataella phaffii, Kluyveromyces lactis, Candida albicans and C. glabrata) yeasts. Especially in S. cerevisiae, an extensive toolbox of advanced CRISPR-related applications has been established, including crisprTFs and gene drives. The comparison of innovative CRISPR-Cas expression strategies in yeasts presented here may also serve as guideline to implement and refine CRISPR-Cas systems for highly efficient genome editing in other eukaryotic organisms.","doi":"10.1016/j.biotechadv.2018.01.006","authors":"Raschmanová H, Weninger A, Glieder A, Kovar K, Vogl T","authors_abbrev":"Raschmanová H et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-01-15","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-01-16 01:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20739936","title":"Phosphorylation of the CPC by Cdk1 promotes chromosome bi-orientation.","citation":"Nature 2010 Oct 07;467(7316):719-23","abstract":"Successful partition of replicated genomes at cell division requires chromosome attachment to opposite poles of mitotic spindle (bi-orientation). Any defects in this regulation bring about chromosomal instability, which may accelerate tumour progression in humans. To achieve chromosome bi-orientation at prometaphase, the chromosomal passenger complex (CPC), composed of catalytic kinase Aurora B and regulatory components (INCENP, Survivin and Borealin), must be localized to centromeres to phosphorylate kinetochore substrates. Although the CPC dynamically changes the subcellular localization, the regulation of centromere targeting is largely unknown. Here we isolated a fission yeast cyclin B mutant defective specifically in chromosome bi-orientation. Accordingly, we identified Cdk1 (also known as Cdc2)-cyclin-B-dependent phosphorylation of Survivin. Preventing Survivin phosphorylation impairs centromere CPC targeting as well as chromosome bi-orientation, whereas phosphomimetic Survivin suppresses the bi-orientation defect in the cyclin B mutant. Survivin phosphorylation promotes direct binding with shugoshin, which we now define as a conserved centromeric adaptor of the CPC. In human cells, the phosphorylation of Borealin has a comparable role. Thus, our study resolves the conserved mechanisms of CPC targeting to centromeres, highlighting a key role of Cdk1-cyclin B in chromosome bi-orientation.","doi":"10.1038/nature09390","authors":"Tsukahara T, Tanno Y, Watanabe Y","authors_abbrev":"Tsukahara T et al.","pubmed_publication_date":"07 Oct 2010","pubmed_entrez_date":"2010-08-27","publication_year":"2010","canto_session_key":"dd0b314b0bd84119","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2020-02-24 15:20:30","canto_approved_date":"2025-09-04 09:35:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-06 21:20:30","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC962.02c","SPBC11B10.09","SPBC582.03","SPAC15A10.15","SPCC188.02","SPBC336.15","SPBP35G2.03c","SPCC320.13c","SPBC725.12"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2020-02-24"},{"uniquename":"PMID:21714024","title":"Crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe RNA polymerase III.","citation":"Protein Sci 2011 Sep;20(9):1558-65","abstract":"Eukaryotic RNA polymerase III (Pol III) is a multisubunit enzyme responsible for transcribing tRNA, 5S rRNA, and several small RNAs. Of the 17 subunits in Pol III, the C17 (Rpc17) and C25 (Rpc25) subunits form a stable subcomplex that protrudes from the core polymerase. In this study, we determined the crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe. The subcomplex adopts an elongated shape, and each subunit has two domains. The two subunits in the subcomplex are tightly packed and extensively interact, with a contact area of 2080 Å(2) . The overall conformation of S. pombe C17/25 is considerably different from the previously reported structure of C17/25 from Saccharomyces cerevisiae, with respect to the position of the C17 HRDC domain, a helix bundle essential for cell viability. In contrast, the S. pombe C17/25 structure is quite similar to those of the Pol II and archaeal counterparts, Rpb4/7 and RpoE/F, respectively, despite the low sequence similarity. A phylogenetic comparison of the C17 subunits among eukaryotes revealed that they can be classified into three groups, according to the length of the interdomain linker. S. pombe C17, as well as Rpb4 and RpoF, belongs to the largest group, with the short linker. On the other hand, S. cerevisiae C17 belongs to the smallest group, with the long linker, which probably enables the subcomplex to assume the alternative conformation.","doi":"10.1002/pro.682","authors":"Ehara H, Sekine S, Yokoyama S","authors_abbrev":"Ehara H et al.","pubmed_publication_date":"Sep 2011","pubmed_entrez_date":"2011-06-30","publication_year":"2011","canto_session_key":"83b3944736594438","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-10 02:04:32","canto_approved_date":"2023-02-22 08:41:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-10 02:04:20","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1E7.10","SPBC2G5.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-12-10","pdb_entries":[{"pdb_id":"3ayh","gene_chains":[{"gene_uniquename":"SPBC2G5.07c","chain":"B","position":"1-203"},{"gene_uniquename":"SPAPB1E7.10","chain":"A","position":"1-129"}],"title":"Crystal structure of the C17/25 subcomplex from S. pombe RNA Polymerase III","entry_authors":"Ehara H,Sekine S,Yokoyama S","entry_authors_abbrev":"Ehara H et al.","reference_uniquename":"PMID:21714024","experimental_method":"X-ray","resolution":"2.193"}]},{"uniquename":"PMID:33322563","title":"Molecular Diversity via Tetrasubstituted Alkenes Containing a Barbiturate Motif: Synthesis and Biological Activity.","citation":"Molecules 2020 Dec 11;25(24)","abstract":"The synthesis of a molecularly diverse library of tetrasubstituted alkenes containing a barbiturate motif is described. Base-induced condensation of  N  1 -substituted pyrimidine-2,4,6(1 H ,3 H ,5 H )-triones with 5-(bis(methylthio)methylene)-2,2-dimethyl-1,3-dioxane-4,6-dione gave 3-substituted 5-(methylthio)-2 H -pyrano[2,3- d ]pyrimidine-2,4,7(1 H ,3 H )-triones ('pyranopyrimidinones'), regioselectively. A sequence of reactions involving ring-opening of the pyran moiety, displacement of the methylthio group with an amine, re-formation of the pyran ring, and after its final cleavage with an amine, gave tetrasubstituted alkenes (3-amino-3-(2,4,6-trioxotetrahydropyrimidin-5(2 H )-ylidene)propanamides) with a diversity of substituents. Cleavage of the pyranopyrimidinones with an aniline was facilitated in 2,2,2-trifluoroethanol under microwave irradiation. Compounds were tested against  Escherichia coli ,  Staphylococcus aureus , the yeast  Schizosaccharomyces pombe,  and the pathogenic fungus  Candida albicans . No compounds exhibited activity against  E. coli , whilst one compound was weakly active against  S. aureus . Three compounds were strongly active against  S. pombe , but none was active against  C. albicans .","doi":"10.3390/molecules25245868","authors":"Al-Sheikh A, Begum M, Zhang B, Lewis RA, Allenby NEE, Waddell PG, Golding BT","authors_abbrev":"Al-Sheikh A et al.","pubmed_publication_date":"11 Dec 2020","pubmed_entrez_date":"2020-12-16","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-12-18 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15014440","title":"Mechanism controlling perpendicular alignment of the spindle to the axis of cell division in fission yeast.","citation":"EMBO J 2004 Mar 24;23(6):1289-300","abstract":"In animal cells, the mitotic spindle is aligned perpendicular to the axis of cell division. This ensures that sister chromatids are separated to opposite sides of the cytokinetic actomyosin ring (CAR). We show that, in fission yeast, spindle rotation is dependent on the interaction of astral microtubules with the cortical actin cytoskeleton. Interaction initially occurs with a region surrounding the nucleus, which we term the astral microtubule interaction zone (AMIZ). Simultaneous contact of astral microtubules from both poles with the AMIZ directs spindle rotation and this requires both actin and two type V myosins, Myo51 and Myo52. Astral microtubules from one pole only then contact the CAR, which is located at the centre of the AMIZ. We demonstrate that the anillin homologue Mid1, which dictates correct placement of the CAR, is necessary to stabilise the mitotic spindle perpendicular to the axis of cell division. Finally, we show that the position of the mitotic spindle is monitored by a checkpoint that regulates the timing of sister chromatid separation.","authors":"Gachet Y, Tournier S, Millar JB, Hyams JS","authors_abbrev":"Gachet Y et al.","pubmed_publication_date":"24 Mar 2004","pubmed_entrez_date":"2004-03-12","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22683458","title":"Interacting factors and cellular localization of SR protein-specific kinase Dsk1.","citation":"Exp Cell Res 2012 Oct 01;318(16):2071-84","abstract":"Schizosaccharomyces pombe Dsk1 is an SR protein-specific kinase (SRPK), whose homologs have been identified in every eukaryotic organism examined. Although discovered as a mitotic regulator with protein kinase activity toward SR splicing factors, it remains largely unknown about what and how Dsk1 contributes to cell cycle and pre-mRNA splicing. In this study, we investigated the Dsk1 function by determining interacting factors and cellular localization of the kinase. Consistent with its reported functions, we found that pre-mRNA processing and cell cycle factors are prominent among the proteins co-purified with Dsk1. The identification of these factors led us to find Rsd1 as a novel Dsk1 substrate, as well as the involvement of Dsk1 in cellular distribution of poly(A)(+) RNA. In agreement with its role in nuclear events, we also found that Dsk1 is mainly localized in the nucleus during G(2) phase and at mitosis. Furthermore, we revealed the oscillation of Dsk1 protein in a cell cycle-dependent manner. This paper marks the first comprehensive analysis of in vivo Dsk1-associated proteins in fission yeast. Our results reflect the conserved role of SRPK family in eukaryotic organisms, and provide information about how Dsk1 functions in pre-mRNA processing and cell-division cycle.","doi":"10.1016/j.yexcr.2012.05.020","authors":"Tang Z, Luca M, Taggart-Murphy L, Portillio J, Chang C, Guven A, Lin RJ, Murray J, Carr A","authors_abbrev":"Tang Z et al.","pubmed_publication_date":"01 Oct 2012","pubmed_entrez_date":"2012-06-12","publication_year":"2012","canto_session_key":"0498b36c09de2c29","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-08-17 16:16:14","canto_approved_date":"2025-07-31 22:11:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-05 13:03:14","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC530.14c","SPAC19G12.07c","SPBC11C11.08","SPBC13E7.01","SPAC29A4.08c","SPBC146.07","SPCC1795.11","SPAC16.02c","SPAC1D4.11c","SPAC57A7.04c","SPBC646.02","SPCC663.05c","SPAC23C11.11"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2015-08-17"},{"uniquename":"PMID:26608589","title":"Time-lapse electrical impedance spectroscopy for monitoring the cell cycle of single immobilized S. pombe cells.","citation":"Sci Rep 2015 Nov 26;5:17180","abstract":"As a complement and alternative to optical methods, wide-band electrical impedance spectroscopy (EIS) enables multi-parameter, label-free and real-time detection of cellular and subcellular features. We report on a microfluidics-based system designed to reliably capture single rod-shaped Schizosaccharomyces pombe cells by applying suction through orifices in a channel wall. The system enables subsequent culturing of immobilized cells in an upright position, while dynamic changes in cell-cycle state and morphology were continuously monitored through EIS over a broad frequency range. Besides measuring cell growth, clear impedance signals for nuclear division have been obtained. The EIS system has been characterized with respect to sensitivity and detection limits. The spatial resolution in measuring cell length was 0.25 μm, which corresponds to approximately a 5-min interval of cell growth under standard conditions. The comprehensive impedance data sets were also used to determine the occurrence of nuclear division and cytokinesis. The obtained results have been validated through concurrent confocal imaging and plausibilized through comparison with finite-element modeling data. The possibility to monitor cellular and intracellular features of single S. pombe cells during the cell cycle at high spatiotemporal resolution renders the presented microfluidics-based EIS system a suitable tool for dynamic single-cell investigations.","doi":"10.1038/srep17180","authors":"Zhu Z, Frey O, Haandbaek N, Franke F, Rudolf F, Hierlemann A","authors_abbrev":"Zhu Z et al.","pubmed_publication_date":"26 Nov 2015","pubmed_entrez_date":"2015-11-27","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-28 01:19:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR19237","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:8044","HGNC:8043","SPCC613.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8675019","title":"Amiloride toxicity in the fission yeast Schizosaccharomyces pombe is released by thiamine and mutations in the thiamine-repressible gene car1.","citation":"Gene 1996 May 24;171(1):119-22","abstract":"Amiloride (Am) inhibits growth in the fission yeast Schizosaccharomyces pombe. We show that the toxic effect of this drug is relieved by low concentrations of thiamine (Th) and that the pyrimidine moiety of the Th molecule is responsible for growth inhibition release. A putative membrane protein encoded by the car1 gene is the target for Am action. It is responsible for Am sensitivity and is involved in the utilization of Th and its biosynthetic precursor, 4-amino-5-hydroxymethyl-2-methylpyrimidine. Its expression is repressed by Th and is under the genetic control of the genes, thi1, tnr1, tnr2 and tnr3, which have previously been shown to be responsible for the transcriptional control of genes involved in the biosynthesis and dephosphorylation of Th.","authors":"Niederberger C, Fankhauser H, Edenharter E, Schweingruber ME","authors_abbrev":"Niederberger C et al.","pubmed_publication_date":"24 May 1996","pubmed_entrez_date":"1996-05-24","publication_year":"1996","canto_session_key":"4b0970d0e5484486","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-05-13 13:59:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-07-10 21:07:28","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.02","SPAC17A2.01","SPAC6F12.05c","SPAC1486.10"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2012-07-10"},{"uniquename":"PMID:33420908","title":"Origin of translational control by eIF2α phosphorylation: insights from genome-wide translational profiling studies in fission yeast.","citation":"Curr Genet 2021 Jun;67(3):359-368","abstract":"During amino acid limitation, the protein kinase Gcn2 phosphorylates the α subunit of eIF2, thereby regulating mRNA translation. In yeast Saccharomyces cerevisiae and mammals, eIF2α phosphorylation regulates translation of related transcription factors Gcn4 and Atf4 through upstream open reading frames (uORFs) to activate transcription genome wide. However, mammals encode three more eIF2α kinases activated by distinct stimuli. Did the translational control system involving eIF2α phosphorylation evolve from so simple (as found in yeast S. cerevisiae) to complex (as found in humans)? Recent genome-wide translational profiling studies of amino acid starvation response in the fission yeast Schizosaccharomyces pombe provide an unexpected answer to this question.","doi":"10.1007/s00294-020-01149-w","authors":"Asano K","authors_abbrev":"Asano K","pubmed_publication_date":"Jun 2021","pubmed_entrez_date":"2021-01-09","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-01-11 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010143","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17698857","title":"Rescuing yeast mutants with human genes.","citation":"Brief Funct Genomic Proteomic 2007 Jun;6(2):104-11","abstract":"The fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae have, in addition to being extensively studied themselves, both been utilized for the last quarter century as experimental systems for the isolation of genes from other organisms. Mutations conferring growth defects in either of the two yeast strains have frequently been complemented by expression of cDNA libraries from heterologous species, often human. Many successful experiments have utilized available yeast mutations to allow successful complementation by a human gene, which can thus be deduced to have the same, or an overlapping function as the mutated yeast gene. However complementation in yeast has also been used with success to study two fields, apoptosis and steroid receptor signalling, which, at first glance, seem to be foreign to the yeast life cycle.","authors":"Osborn MJ, Miller JR","authors_abbrev":"Osborn MJ et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-08-19","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30814065","title":"Automated morphometry toolbox for analysis of microscopic model organisms using simple bright-field imaging.","citation":"Biol Open 2019 Mar 12;8(3)","abstract":"Model organisms with compact genomes, such as yeast and  C   aenorhabditis   elegans , are particularly useful for understanding organism growth and life/cell cycle. Organism morphology is a critical parameter to measure in monitoring growth and stage in the life cycle. However, manual measurements are both time consuming and potentially inaccurate, due to variations among users and user fatigue. In this paper we present an automated method to segment bright-field images of fission yeast, budding yeast, and  C. elegans  roundworm, reporting a wide range of morphometric parameters, such as length, width, eccentricity, and others. Comparisons between automated and manual methods on fission yeast reveal good correlation in size values, with the 95% confidence interval lying between -0.8 and +0.6 μm in cell length, similar to the 95% confidence interval between two manual users. In a head-to-head comparison with other published algorithms on multiple datasets, our method achieves more accurate and robust results with substantially less computation time. We demonstrate the method's versatility on several model organisms, and demonstrate its utility through automated analysis of changes in fission yeast growth due to single kinase deletions. The algorithm has additionally been implemented as a stand-alone executable program to aid dissemination to other researchers.","doi":"10.1242/bio.037788","authors":"Liu G, Dong F, Fu C, Smith ZJ","authors_abbrev":"Liu G et al.","pubmed_publication_date":"12 Mar 2019","pubmed_entrez_date":"2019-03-01","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-03-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28171765","title":"Myo2p is the major motor involved in actomyosin ring contraction in fission yeast.","citation":"Curr Biol 2017 Feb 06;27(3):R99-R100","abstract":"Cytokinesis in many eukaryotes requires an actomyosin-based contractile ring [1]. In fission yeast, cytokinesis involves the type II myosins Myo2p and Myp2p and the type V myosin Myo51p [2]. A recent study by Laplante et al.[3], using deletion mutants of myp2 and myo51 and the mis-sense mutant myo2-E1 [4], concluded that each myosin has distinct functions and proposed that Myp2p plays the dominant role in actomyosin ring contraction. Here we present evidence that Myo2p, not Myp2p, is likely to be the major motor driving actomyosin ring contractility. Since the previous work [3] was performed at 25°C, the permissive temperature for myo2-E1, we compared cytokinesis timings in myo2-E1 and myo2Δ at 25°C and found that myo2-E1 is only partially compromised at 25°C. Furthermore, we find that myp2Δ and myp2Δ myo51Δ double mutants contract actomyosin rings at ∼90% of the rate of wild-type cells at 30°C and 36°C, suggesting that Myp2p plays a minimal role in ring contraction at these temperatures. Finally, ring contraction in our myo2-E1 strain took longer at 25°C than previously reported [3]. Although faster-acting alleles of myo2 will be required to evaluate its contribution at 25°C, our work establishes that Myo2p is the major motor involved in ring contraction, under most, if not all, conditions.","doi":"10.1016/j.cub.2016.12.024","authors":"Zambon P, Palani S, Kamnev A, Balasubramanian MK","authors_abbrev":"Zambon P et al.","pubmed_publication_date":"06 Feb 2017","pubmed_entrez_date":"2017-02-08","publication_year":"2017","canto_session_key":"f52578868038203e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-10 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8590464","title":"Molecular properties of the lys1+ gene and the regulation of alpha-aminoadipate reductase in Schizosaccharomyces pombe.","citation":"Curr Genet 1995 Jul;28(2):131-7","abstract":"The alpha-aminoadipate pathway for the biosynthesis of lysine is unique to fungi. Molecular properties of the cloned lys1+ gene and the regulation of the encoded alpha-aminoadipate reductase (AAR) were investigated in the fission yeast Schizosaccharomyces pombe. A 5.2-kb HindIII-EcoRI fragment of S. pombe DNA, containing a functional lys1+ gene and a promoter, was subcloned to make the 10.7-kb plasmid pLYS1H. A nested 1.778-kb HindIII-EcoRI DNA fragment that complemented the lys1-131 mutant phenotype was sequenced from the plasmid pLYS1D, and shown to contain an open reading frame (ORF) of 470 amino acids, preceded by putative POLII promoter elements (TATA and CCAAT box elements, and two potential yeast GCN4-binding motifs) within 368 bp upstream of the start codon. This ORF shared with the corresponding region of the isofunctional AAR of Saccharomyces cerevisiae 49% amino-acid identity (62% similarity) overall, within which were smaller regions of marked sequence conservation. One such region coincided (95% identity) with a putative AMP-binding domain motif identified in the AAR of S. cerevisiae. In wild-type S. pombe, AAR activity from cells grown in lysine-supplemented minimal or YEPD media was less than the activity of cells grown in minimal medium. The AAR of S. pombe was more sensitive to feedback inhibition by lysine in vitro than the AAR of S. cerevisiae. These results show the effects of extensive evolutionary divergence on the structure and expression of a pivotal enzyme in the alpha-aminoadipate pathway. Presumably, delineated regions of strong sequence conservation correspond to discrete domains essential to AAR function.","authors":"Ford RA, Bhattacharjee JK","authors_abbrev":"Ford RA et al.","pubmed_publication_date":"Jul 1995","pubmed_entrez_date":"1995-07-01","publication_year":"1995","canto_session_key":"74e623dba5700603","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-01 15:40:56","canto_approved_date":"2026-03-09 16:00:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-23 07:42:54","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP7G5.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-02-01"},{"uniquename":"PMID:2544292","title":"Involvement of a type 1 protein phosphatase encoded by bws1+ in fission yeast mitotic control.","citation":"Cell 1989 Jun 16;57(6):1009-16","abstract":"Fission yeast cdc25+ and wee1+ interact genetically with cdc2+ in the regulation of cell division, respectively as a mitotic activator and inhibitor. cdc25+ is normally essential for mitosis, but this requirement is alleviated in a loss-of-function wee1 mutant background. A plasmid-borne sequence, other than wee1+, that causes a cdc25ts wee1- double mutant to revert to a temperature-sensitive cdc phenotype has been isolated. The gene carried by this plasmid is called bws1+ (for bypass of wee suppression). bws1+ also bypasses the ability of alleles of cdc2 that confer a wee phenotype (cdc2w) to suppress loss-of-function cdc25 mutants. The nucleotide sequence of bws1+ shows that the predicted protein shares 81% amino acid identity with the catalytic subunit of mammalian type 1 protein phosphatase. Thus a genetic screen that might have yielded a protein kinase (wee1+) uncovered a phosphatase that also appears to be involved in the pathway of mitotic control.","authors":"Booher R, Beach D","authors_abbrev":"Booher R et al.","pubmed_publication_date":"16 Jun 1989","pubmed_entrez_date":"1989-06-16","publication_year":"1989","canto_session_key":"77e60bd014f07c05","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-12 15:22:53","canto_approved_date":"2021-04-16 13:21:47","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-13 14:34:38","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC776.02c","SPAC24H6.05","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-06-12"},{"uniquename":"PMID:7900424","title":"Assessment of pheromone production and response in fission yeast by a halo test of induced sporulation.","citation":"Yeast 1994 Oct;10(10):1347-54","abstract":"We describe a rapid, sensitive and semi-quantitative plate assay for monitoring pheromone activity in the fission yeast Schizosaccharomyces pombe. It is based on the observation that meiosis requires stimulation by pheromone and exploits diploid strains that will only sporulate after addition of exogenous pheromone. The tester strains are heterozygous for mating type, are non-switching, and are mutated in one of the early subfunctions (either mat1-Mc or mat1-Pc), so that meiosis is only induced after exposure to exogenous pheromone (M-factor or P-factor, respectively). Pheromone activity is assessed as an iodine-positive halo of sporulation surrounding the pheromone source, and the width of the halo is related to the amount of pheromone being produced. The assay is sufficiently sensitive to monitor the low amount of M-factor produced by an M mam1 strain, and its sensitivity towards P-factor is greatly increased by using a hyper-sensitive tester strain lacking the Sxa2 protease that is believed to degrade this pheromone. We also demonstrate that the production of P-factor is very much stimulated by exposure of P cells to M-factor.","authors":"Egel R, Willer M, Kjaerulff S, Davey J, Nielsen O","authors_abbrev":"Egel R et al.","pubmed_publication_date":"Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_session_key":"66b209326b30f74b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-29 13:25:50","canto_approved_date":"2023-09-11 07:25:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-04-12 15:16:24","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.03","SPMTR.01","SPAC513.03","SPAPB8E5.05","SPAC17H9.09c","SPAC3F10.10c","SPBC25B2.02c","SPAC1296.03c","SPBC23G7.09"],"gene_count":9,"ltp_gene_count":5,"approved_date":"2016-03-29"},{"uniquename":"PMID:2035188","title":"Cryopreservation of competent Schizosaccharomyces pombe protoplasts.","citation":"Trends Genet 1991 Feb;7(2):40","abstract":"","authors":"Jimenez J","authors_abbrev":"Jimenez J","pubmed_publication_date":"Feb 1991","pubmed_entrez_date":"1991-02-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC00366","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11015724","title":"Schizosaccharomyces pombe gmd3(+)/alg11(+) is a functional homologue of Saccharomyces cerevisiae ALG11 which is involved in N-linked oligosaccharide synthesis.","citation":"Yeast 2000 Oct;16(14):1261-71","abstract":"The oligosaccharide of glycoproteins in the fission yeast Schizosaccharomyces pombe is unique in containing galactose. We isolated four mutants that had reduced amounts of galactose residues on their cell surface glycoproteins by fluorescence-activated cell sorter. The isolated four recessive mutants, gmd1 to gmd4, showed a defect in glycosylation of acid phosphatase, a cell surface glycoprotein. In gmd3 mutant cells, the amounts of both mannose and galactose residues were decreased on the cell surface galactomannoproteins, suggesting an underglycosylation of galactomannoproteins. The gmd3(+) gene encodes a protein that has significant similarity with Saccharomyces cerevisiae Alg11p and is likely to be involved in N-linked core oligosaccharide synthesis. ALG11 suppressed the gmd3 mutation, indicating that gmd3(+) gene is a functional homologue of the ALG11 gene. We therefore designated gmd3(+) as alg11(+).","authors":"Umeda K, Yoko-o T, Nakayama K, Suzuki T, Jigami Y","authors_abbrev":"Umeda K et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-10-04","publication_year":"2000","canto_session_key":"99162744a6084ce2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-02-19 16:39:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-13 15:03:16","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-13"},{"uniquename":"PMID:7166567","title":"Ascospore development in the fission yeasts Schizosaccharomyces pombe and S. japonicus.","citation":"J Cell Sci 1982 Aug;56:263-79","abstract":"The fine structure of ascospore formation in the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus var. japonicus was studied by serial thin-sectioning and electron microscopy. The morphogenetic events were almost the same in both species. Ascospore development was initiated by the formation of the forespore membrane on the cytoplasmic side of the differentiated nucleus-associated organelle (NAO) in the interval between meiosis I and II in S. pombe, or during the post-meiotic nuclear division in S. japonicus, and the process proceeded almost synchronously through the two or four nuclei in the ascus. The forespore membrane developed by fusion of the cytoplasmic vesicles and this was clearly demonstrated in S. japonicus where the behaviour of vesicles involved in the forespore membrane development could be traced as they were marked by the presence of electron-dense granules. The staining technique, by phosphotungustic acid--chromic acid (PTA-CA) after treatment with periodic acid, was used to attempt to elucidate the origin and the nature of the forespore membrane. The method specific to plasmalemma-type membranes stained both ascus and ascospore plasmalemmas; the forespore membrane was not stained at first but developed the same affinity for stain as the plasma membrane in the course of ascospore development. The results suggest that the forespore membrane did not come directly from the ascus plasma membrane, but from another membrane system such as the endoplasmic reticulum. Spore wall material was deposited in the space between the inner and outer leaflets of the forespore membrane.","authors":"Tanaka K, Hirata A","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"Aug 1982","pubmed_entrez_date":"1982-08-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD222","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1756736","title":"The wis1 protein kinase is a dosage-dependent regulator of mitosis in Schizosaccharomyces pombe.","citation":"EMBO J 1991 Dec;10(13):4291-9","abstract":"The wis1+ gene encodes a newly identified mitotic control element in Schizosaccharomyces pombe. It was isolated by virtue of its interaction with the mitotic control genes cdc25, wee1 and win1. The wis1+ gene potentially encodes a 66 kDa protein with homology to the serine/threonine family of protein kinases. wis1+ plays an important role in the regulation of entry into mitosis, as it shares with cdc25+ and nim1+/cdr1+ the property of inducing mitosis in a dosage-dependent manner. Increased levels of wis1+ expression cause mitotic initiation to occur at a reduced cell size. Loss of wis1+ function does not prevent vegetative growth and division, though wis1- cells show an elongated morphology, indicating that their entry into mitosis and cell division is delayed relative to wild type cells. wis1- cells undergo a rapid reduction of viability upon entry into stationary phase, suggesting a role for wis1+ in the integration of nutritional sensing with the control over entry into mitosis.","authors":"Warbrick E, Fantes PA","authors_abbrev":"Warbrick E et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"1cf6a37d7872772f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-08-21 11:08:49","canto_approved_date":"2019-06-14 13:16:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-02-26 10:00:30","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.09","SPAC823.15","SPCC18B5.03","SPAC24H6.05","SPBC409.07c","SPBC16H5.07c","SPBC11B10.09"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-08-21"},{"uniquename":"PMID:8978687","title":"The fission yeast dma1 gene is a component of the spindle assembly checkpoint, required to prevent septum formation and premature exit from mitosis if spindle function is compromised.","citation":"EMBO J 1996 Dec 02;15(23):6605-16","abstract":"Premature initiation of cytokinesis can lead to loss of chromosomes, and 'cutting' of the nucleus. Therefore, the proper spatial and temporal co-ordination of mitosis and cytokinesis is essential for maintaining the integrity of the genome. The fission yeast cdc16 gene is implicated both in the spindle assembly checkpoint and control of septum formation. To identify other proteins involved in these controls, we have isolated multicopy suppressors of the cdc16-116 mutation, and the characterization of one of these, dma1 (defective in mitotic arrest), is presented here. dma1 is not an essential gene, but in a dma1 null background (dma1-D1) the function of the spindle assembly checkpoint is compromised. If assembly of the spindle is prevented, dma1-D1 cells do not arrest, the activity of cdc2 kinase decays and cells form a division septum without completing a normal mitosis. dma1-D1 cells also show an increased rate of chromosome loss during exponential growth. Upon ectopic expression from an inducible promoter, dma1p delays progress through mitosis and inhibits septum formation, giving rise to elongated, multinucleate cells. We propose that dma1 is a component of the spindle assembly checkpoint, required to prevent septum formation and premature exit from mitosis if spindle function is impaired.","authors":"Murone M, Simanis V","authors_abbrev":"Murone M et al.","pubmed_publication_date":"02 Dec 1996","pubmed_entrez_date":"1996-12-02","publication_year":"1996","canto_session_key":"e70a1374f7a8719d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-02-28 10:43:25","canto_approved_date":"2021-06-18 15:50:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-10-06 20:58:03","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPAC17G8.10c","SPBC11B10.09","SPAC6F6.08c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-02-28"},{"uniquename":"PMID:909471","title":"[Relation of cell wall growth and conjugation to the cell division cycle in Schizosaccharomyces pombe].","citation":"Mikrobiologiia 1977;46(4):717-24","abstract":"The growth of the cell wall to Schizosaccharomyces pombe was studied by fluorescent microscopy and time-lapse microcinematography. The growth of individual cells was found to be bipolar and sharply asymmetrical. The two poles had different sequence of growth which depended on the functionation of the cell cycle. Findings concerning the growth of the poles were used for investigating the topography of the surface of zygotes. The formation of conjugation protuberances was not related to a certain pole and did not depend on its growth state. Some aspects of the cell cycle dependence of the cell wall growth and conjugation in Schizosaccharomyces pombe are discussed.","authors":"Shtreĭblova E","authors_abbrev":"Shtreĭblova E","pubmed_publication_date":"1977","pubmed_entrez_date":"1977-07-01","publication_year":"1977","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5855856","title":"A method for the selection of auxotrophic mutants of the yeast Schizosaccharomyces pombe.","citation":"Experientia 1964 Jun 15;20(6):320-1","abstract":"","authors":"Megnet R","authors_abbrev":"Megnet R","pubmed_publication_date":"15 Jun 1964","pubmed_entrez_date":"1964-06-15","publication_year":"1964","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14555473","title":"Fission yeast Sap1 protein is essential for chromosome stability.","citation":"Eukaryot Cell 2003 Oct;2(5):910-21","abstract":"Sap1 is a dimeric sequence-specific DNA binding-protein, initially identified for its role in mating-type switching of the fission yeast Schizosaccharomyces pombe. The protein is relatively abundant, around 10,000 dimers/cell, and is localized in the nucleus. sap1+ is essential for viability, and transient overexpression is accompanied by rapid cell death, without an apparent checkpoint response and independently of mating-type switching. Time lapse video microscopy of living cells revealed that the loss of viability is accompanied by abnormal mitosis and chromosome fragmentation. Overexpression of the C terminus of Sap1 induces minichromosome loss associated with the \"cut\" phenotype (uncoupling mitosis and cytokinesis). These phenotypes are favored when the C terminus of Sap1 is overexpressed during DNA replication. Fluorescence in situ hybridization experiments demonstrated that the cut phenotype is related to precocious centromere separation, a typical marker for loss of cohesion. We propose that Sap1 is an architectural chromatin-associated protein, required for chromosome organization.","authors":"de Lahondès R, Ribes V, Arcangioli B","authors_abbrev":"de Lahondès R et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2003-10-14","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23729666","title":"Structural requirements for sterol regulatory element-binding protein (SREBP) cleavage in fission yeast.","citation":"J Biol Chem 2013 Jul 12;288(28):20351-60","abstract":"Sterol regulatory element-binding proteins (SREBPs) are central regulators of cellular lipid synthesis and homeostasis. Mammalian SREBPs are proteolytically activated and liberated from the membrane by Golgi Site-1 and Site-2 proteases. Fission yeast SREBPs, Sre1 and Sre2, employ a different mechanism that genetically requires the Golgi Dsc E3 ligase complex for cleavage activation. Here, we established Sre2 as a model to define structural requirements for SREBP cleavage. We showed that Sre2 cleavage does not require the N-terminal basic helix-loop-helix zipper transcription factor domain, thus separating cleavage of Sre2 from its transcription factor function. From a mutagenesis screen of 94 C-terminal residues of Sre2, we isolated 15 residues required for cleavage and further identified a glycine-leucine sequence required for Sre2 cleavage. Importantly, the glycine-leucine sequence is located at a conserved distance before the first transmembrane segment of both Sre1 and Sre2 and cleavage occurs in between this sequence and the membrane. Bioinformatic analysis revealed a broad conservation of this novel glycine-leucine motif in SREBP homologs of ascomycete fungi, including the opportunistic human pathogen Aspergillus fumigatus where SREBP is required for virulence. Consistent with this, the sequence was also required for cleavage of the oxygen-responsive transcription factor Sre1 and adaptation to hypoxia, demonstrating functional conservation of this cleavage recognition motif. These cleavage mutants will aid identification of the fungal SREBP protease and facilitate functional dissection of the Dsc E3 ligase required for SREBP activation and fungal pathogenesis.","doi":"10.1074/jbc.M113.482224","authors":"Chong R, Espenshade PJ","authors_abbrev":"Chong R et al.","pubmed_publication_date":"12 Jul 2013","pubmed_entrez_date":"2013-06-05","publication_year":"2013","canto_session_key":"dc907bc500c1a07a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rocky Cheung","canto_first_approved_date":"2017-02-17 12:24:24","canto_approved_date":"2023-08-03 10:55:56","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2013-07-26 19:24:20","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Rocky Cheung","community_curator":true,"annotation_count":34,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20H4.02","SPBC119.02","SPBC354.05c","SPBC19C2.09","SPAC4D7.11","SPCC285.11","SPAC1486.02c","SPAC1565.08","SPBC947.10"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-02-17"},{"uniquename":"EMBL:AB084882","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.71"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30667359","title":"Factors affecting template switch recombination associated with restarted DNA replication.","citation":"Elife 2019 Jan 22;8","abstract":"Homologous recombination helps ensure the timely completion of genome duplication by restarting collapsed replication forks. However, this beneficial function is not without risk as replication restarted by homologous recombination is prone to template switching (TS) that can generate deleterious genome rearrangements associated with diseases such as cancer. Previously we established an assay for studying TS in  Schizosaccharomyces pombe  (Nguyen et al., 2015). Here, we show that TS is detected up to 75 kb downstream of a collapsed replication fork and can be triggered by head-on collision between the restarted fork and RNA Polymerase III transcription. The Pif1 DNA helicase, Pfh1, promotes efficient restart and also suppresses TS. A further three conserved helicases (Fbh1, Rqh1 and Srs2) strongly suppress TS, but there is no change in TS frequency in cells lacking Fml1 or Mus81. We discuss how these factors likely influence TS.","doi":"10.7554/eLife.41697","authors":"Jalan M, Oehler J, Morrow CA, Osman F, Whitby MC","authors_abbrev":"Jalan M et al.","pubmed_publication_date":"22 Jan 2019","pubmed_entrez_date":"2019-01-23","publication_year":"2019","canto_session_key":"772e462e74088043","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Matthew Whitby","canto_first_approved_date":"2019-08-01 16:59:52","canto_approved_date":"2024-03-28 17:49:43","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-07-11 13:25:59","canto_added_date":"2019-01-24 01:15:04","annotation_curators":[{"name":"Matthew Whitby","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.01","SPCC4G3.05c","SPAC2G11.12","SPAC4H3.05","SPAC25H1.06","SPAC26H5.03","SPBC887.14c","SPAC9.05"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2019-08-01"},{"uniquename":"PMID:6273154","title":"The cdc 22 mutation by Schizosaccharomyces pombe is a temperature-sensitive defect in nucleoside diphosphokinase.","citation":"Eur J Biochem 1981 Oct;119(2):341-5","abstract":"A number of temperature-sensitive cdc- mutants of Schizosaccharomyces pombe that are affected in DNA replication, were screened for the absence of deoxynucleoside triphosphate(s) when blocked at their restrictive temperature. The preliminary screening simply involved analysis of perchloric acid-soluble cell extracts by two-dimensional thin-layer chromatography on poly(ethyleneimine)-impregnated cellulose. One mutant strain, cdc 22-M45, was found which apparently lacked dTTP. Pulse-labelling of intracellular nucleotides revealed that not only did dTTP become depleted, but that dTDP accumulated when this mutant was blocked by a temperature shift-up, indicating a defective nucleoside diphosphokinase. Nucleoside diphosphokinase from cdc 22-M45 was less active than that from wild-type strain 972 when assayed at high temperatures. The nucleoside diphosphokinase of the mutant also has an altered Km for dTDP at both permissive (25 degrees C), and at the restrictive (36.8 degrees C) temperatures. At the restrictive temperature the Km for dTDP of the mutant enzyme is more than 11-times greater than that of the wild type. Characterisation of the biochemical basis of the defect in this cdc- mutant has shown that in S. pombe, despite its having an apparently complex system of genetic control over progression through S-phase, one factor at least is merely availability of a nucleoside triphosphate precursor to DNA synthesis.","authors":"Dickinson JR","authors_abbrev":"Dickinson JR","pubmed_publication_date":"Oct 1981","pubmed_entrez_date":"1981-10-01","publication_year":"1981","canto_session_key":"78331c9ee6d7b27a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-20 13:19:39","canto_approved_date":"2020-07-21 03:38:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-19 12:00:09","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-20"},{"uniquename":"PMID:16136186","title":"Directionality of F-actin cables changes during the fission yeast cell cycle.","citation":"Nat Cell Biol 2005 Sep;7(9):916-7","abstract":"Longitudinal F-actin cables are thought to be important for transporting materials for polarized cell growth in fission yeast. We show that most F-actin in the cables is oriented such that the barbed end faces the nearest cell tip during interphase; however, this directionality is reversed during mitosis. These orientations of F-actin ensure proper transport of materials to growing sites during these cell-cycle stages.","authors":"Kamasaki T, Arai R, Osumi M, Mabuchi I","authors_abbrev":"Kamasaki T et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-09-02","publication_year":"2005","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15052323","title":"Characterization and regulation of the gamma-glutamyl transpeptidase gene from the fission yeast Schizosaccharomyces pombe.","citation":"Can J Microbiol 2004 Jan;50(1):61-6","abstract":"The structural gene for the putative gamma-glutamyl transpeptidase (GGT) was isolated from the chromosomal DNA of the fission yeast Schizosaccharomyces pombe. The determined sequence contained 3324 bp and encoded the predicted 630 amino acid sequence of GGT, which resembles counterparts in Homo sapiens, Rattus norvegicus, Saccharomyces cerevisiae, and Escherichia coli. The S. pombe cells harboring the cloned GGT gene showed about twofold higher GGT activity in the exponential phase than the cells harboring the vector only, indicating that the cloned GGT gene was functional. To monitor the expression of the S. pombe GGT gene, we fused the fragment 1085 bp upstream of the cloned GGT gene into the promoterless beta-galactosidase gene of the shuttle vector YEp367R to generate the fusion plasmid pGT98. The synthesis of beta-galactosidase from the fusion plasmid in S. pombe cells was enhanced by treatments with NO-generating sodium nitroprusside (SN), L-buthionine-(S,R)-sulfoximine (BSO), and glycerol. The GGT mRNA level in the S. pombe cells was increased by SN and BSO. Involvement of Pap1 in the induction of the GGT gene by SN and BSO was observed.","authors":"Park HJ, Lim HW, Kim K, Kim IH, Park EH, Lim CJ","authors_abbrev":"Park HJ et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2004-03-31","publication_year":"2004","canto_session_key":"d461486b9fbbaa6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-05 14:45:04","canto_approved_date":"2026-01-19 15:45:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-10 15:01:57","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC664.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-07-05"},{"uniquename":"PMID:16133344","title":"Multiple genetic and biochemical interactions of Brr2, Prp8, Prp31, Prp1 and Prp4 kinase suggest a function in the control of the activation of spliceosomes in Schizosaccharomyces pombe.","citation":"Curr Genet 2005 Sep;48(3):151-61","abstract":"The spliceosomal component Prp1 (U5-102 kD) is found in Schizosaccharomyces pombe, a physiological substrate of Prp4 kinase. Here, we identify, spp41-1, a previously isolated extragenic suppressor of Prp4 kinase. The gene encodes an ATP-dependent RNA helicase homologous to the splicing factor Brr2 of Saccharomyces cerevisiae and U5-200 kD of mammalia. The suppressor allele, spp41-1, interacts genetically with alleles of prp1. We show that Prp1 and Brr2 are complexed in vivo with spliceosomal particles containing the five snRNAs U1, U2, U5, and base-paired U4/U6. Prp1 was found exclusively in small ribonucleoprotein particle (snRNP) complexes sedimenting in the range of 30S-60S, whereas Brr2 was also found sedimenting lower than 30S and free of snRNAs. Moreover, we find that the splicing factor Prp31 is complexed with Prp1 in the same spliceosomal particles containing the five snRNAs. These data indicate that in fission yeast spliceosomal particles larger than 30S exist, which can be considered as pre-catalytic spliceosomes. In addition, we show that S. pombe cells lacking Prp1 still contain these large pre-catalytic spliceosomal particles associated with Prp31. These data are consistent with the notion that in fission yeast phosphorylation of Prp1 by Prp4 kinase is involved in the activation of pre-catalytic spliceosomes.","authors":"Bottner CA, Schmidt H, Vogel S, Michele M, Käufer NF","authors_abbrev":"Bottner CA et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-09-01","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F8.12c","SPBC119.13c","SPAC9.03c","SPBC6B1.07"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:9170953","title":"[A mechanism of mRNA transport in fission yeast: nucleolar involvement and heat shock inhibition in mRNA transport].","citation":"Tanpakushitsu Kakusan Koso 1997 May;42(7 Suppl):1193-200","abstract":"","authors":"Tani T","authors_abbrev":"Tani T","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14663140","title":"Two different Swi5-containing protein complexes are involved in mating-type switching and recombination repair in fission yeast.","citation":"Proc Natl Acad Sci U S A 2003 Dec 23;100(26):15770-5","abstract":"Homologous recombination is an important biological process that occurs in all organisms and facilitates genome rearrangements and repair of DNA double-strand breaks. Eukaryotic Rad51 proteins (Rad51sp or Rhp51 in fission yeast) are functional and structural homologs of bacterial RecA protein, an evolutionarily conserved protein that plays a key role in homologous pairing and strand exchange between homologous DNA molecules in vitro. Here we show that the fission yeast swi5+ gene, which was originally identified as a gene required for normal mating-type switching, encodes a protein conserved among eukaryotes and is involved in a previously uncharacterized Rhp51 (Rad51sp)-dependent recombination repair pathway that does not require the Rhp55/57 (Rad55/57sp) function. Protein interactions with both Swi5 and Rhp51 were found to be mediated by a domain common to Swi2 and Sfr1 (Swi five-dependent recombination repair protein 1, a previously uncharacterized protein with sequence similarity to the C-terminal part of Swi2). Genetic epistasis analyses suggest that the Swi5-Sfr1-Rhp51 interactions function specifically in DNA recombination repair, whereas the Swi5-Swi2-Rhp51 interactions may function, together with chromodomain protein Swi6 (HP1 homolog), in mating-type switching.","authors":"Akamatsu Y, Dziadkowiec D, Ikeguchi M, Shinagawa H, Iwasaki H","authors_abbrev":"Akamatsu Y et al.","pubmed_publication_date":"23 Dec 2003","pubmed_entrez_date":"2003-12-10","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.07","SPBC409.03","SPAC1142.03c","SPAC644.14c","SPAC664.01c","SPAC20H4.07"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:19141478","title":"Fission yeast Ccq1 is telomerase recruiter and local checkpoint controller.","citation":"Genes Dev 2008 Dec 15;22(24):3461-74","abstract":"Telomeres recruit telomerase and differentiate chromosome ends from sites of DNA damage. Although the DNA damage checkpoint PI3-kinases ATM and ATR localize to telomeres and promote telomerase activation, activation of their downstream checkpoint pathway targets is inhibited. Here, we show that the fission yeast telomeric protein Ccq1 is required for telomerase recruitment and inhibition of ATR target activation at telomeres. The loss of Ccq1 results in progressive telomere shortening and persistent ATR-dependent activation of Chk1. Unlike the checkpoint activation that follows loss of telomerase, this checkpoint activation occurs prior to detectable levels of critically short telomeres. When ccq1Delta telomeres do become critically short, activated Chk1 promotes an unusual homologous recombination-based telomere maintenance process. We find that the previously reported meiotic segregation defects of cells lacking Ccq1 stem from its role in telomere maintenance rather than from a role in formation of the meiotic bouquet. These findings demonstrate the existence of a novel telomerase recruitment factor that also serves to suppress local checkpoint activation.","doi":"10.1101/gad.498608","authors":"Tomita K, Cooper JP","authors_abbrev":"Tomita K et al.","pubmed_publication_date":"15 Dec 2008","pubmed_entrez_date":"2009-01-15","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26519311","title":"Measurements of Myosin-II Motor Activity During Cytokinesis in Fission Yeast.","citation":"Methods Mol Biol 2016;1369:137-50","abstract":"Fission yeast myosin-II (Myo2p) represents the critical actin-based motor protein that drives actomyosin ring assembly and constriction during cytokinesis. We detail three different methods to measure Myo2p motor function. Actin-activated ATPases provide a readout of actomyosin ATPase motor activity in a bulk assay; actin filament motility assays reveal the speed and efficiency of myosin-driven actin filament gliding (when motors are anchored); myosin-bead motility assays reveal the speed and efficiency of myosin ensembles traveling along actin filaments (when actin is anchored). Collectively, these methods allow us to combine the standard in vivo approaches common to fission yeast with in vitro biochemical methods to learn more about the mechanistic action of myosin-II during cytokinesis.","doi":"10.1007/978-1-4939-3145-3_11","authors":"Tang Q, Pollard LW, Lord M","authors_abbrev":"Tang Q et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-11-01","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-02 01:19:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20036658","title":"Autophagy in the fission yeast Schizosaccharomyces pombe.","citation":"FEBS Lett 2010 Apr 02;584(7):1327-34","abstract":"Autophagy is a non-selective degradation process in eukaryotic cells. The genome sequence of the fission yeast Schizosaccharomyces pombe has revealed that many of the genes required for autophagy are common between the fission yeast and budding yeast, suggesting that the basic machinery of autophagy is conserved between these species. Autophagy in fission yeast is specifically induced by nitrogen starvation based on monitoring a GFP-Atg8p marker. Upon nitrogen starvation, fission yeast cells exit the vegetative cell cycle and initiate sexual differentiation to produce spores. Most of the nitrogen used for de novo protein synthesis during sporulation derives from the autophagic protein degradation system. This review focuses on the recent advances in the role of autophagy in fission yeast.","doi":"10.1016/j.febslet.2009.12.037","authors":"Mukaiyama H, Nakase M, Nakamura T, Kakinuma Y, Takegawa K","authors_abbrev":"Mukaiyama H et al.","pubmed_publication_date":"02 Apr 2010","pubmed_entrez_date":"2009-12-29","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41025246","title":"Metal ion homeostasis regulates condensin-dependent chromatin architecture and chromosome segregation in Schizosaccharomyces pombe.","citation":"J Microbiol 2025 Sep;63(9):e2505008","abstract":"Condensin plays a central role in mitotic chromosome organization and segregation by mediating long-range chromatin interactions. However, the extent to which cellular metabolic status influences condensin function remains unclear. To gain insights into the relationship of metal ion homeostasis and the function of condensin, we conducted genome-wide chromatin immunoprecipitation sequencing (ChIP-seq) using Schizosaccharomyces pombe under iron- or zine-deficient conditions. Under iron- or zinc-deficient conditions, ChIP-seq results revealed a selective reduction in condensin binding at high-affinity target loci, particularly genes regulated by Ace2 and Ams2, while cohesin binding remained largely unaffected. Hi-C analysis showed that iron depletion weakened chromatin interactions at these condensin targets and centromeres, without disrupting global genome architecture. DNA fluorescence in situ hybridization (FISH) confirmed that iron deficiency impaired long-range associations between centromeres and Ace2 target loci at the single-cell level. Notably, iron deficiency led to chromosome segregation defects during mitosis, suggesting that diminished condensin occupancy compromised genome stability. These changes occurred without significant alterations in condensin protein levels or global transcription, indicating a direct effect of metal ion availability on condensin activity. Collectively, our findings revealed a previously unrecognized regulatory axis in which cellular metal ion homeostasis modulated condensin-dependent chromatin organization and mitotic chromosome segregation, offering new insights into the integration of metabolic state with genome maintenance.","doi":"10.71150/jm.2505008","authors":"An SH, Kim KD","authors_abbrev":"An SH et al.","pubmed_publication_date":"Sep 2025","pubmed_entrez_date":"2025-09-30","publication_year":"2025","canto_session_key":"6d8297a34b28916a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-30 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18157152","title":"TER1, the RNA subunit of fission yeast telomerase.","citation":"Nat Struct Mol Biol 2008 Jan;15(1):26-33","abstract":"Telomerase is the ribonucleoprotein complex that adds telomeric repeats to the ends of chromosomes. Its protein subunit TERT is highly conserved among eukaryotes, whereas the RNA subunit varies greatly in size and sequence, hindering the identification of telomerase RNAs in some important model organisms. Here we report the identification and functional characterization of TER1, the telomerase RNA component from fission yeast Schizosaccharomyces pombe. Deletion of ter1+ caused progressive shortening of telomeres and cellular senescence followed by chromosome circularization. Interactions between Est1 and Trt1, the two known protein components of fission yeast telomerase, were dependent on TER1, supporting its role as a scaffold for the assembly of protein subunits. Using a series of template mutations, we show that translocation or dissociation site variability and template-primer slippage account for the sequence heterogeneity of fission yeast telomeres.","authors":"Leonardi J, Box JA, Bunch JT, Baumann P","authors_abbrev":"Leonardi J et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-12-25","publication_year":"2008","canto_session_key":"e92fbfc95586af82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-07-14 14:30:08","canto_approved_date":"2024-08-07 15:07:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-08 16:05:40","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPNCRNA.214","SPBC2D10.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-07-14"},{"uniquename":"PMID:35726599","title":"A CDK activity buffer ensures mitotic completion.","citation":"J Cell Sci 2022 Jun 15;135(12)","abstract":"The eukaryotic cell cycle is driven by the activity of cyclin-dependent kinases (CDKs). CDK activity rises over 50-fold during the cell cycle, from a low level in G1 to a high level in mitosis. However, it is not known whether the entire range of CDK activity is necessary for cell cycle progression, or whether cells can tolerate a reduction in CDK activity level. Here, in fission yeast, we show that sublethal CDK inhibition lengthens the time cells spend in mitosis but does not cause misordering of mitotic events. Maximum attainable CDK activity exceeds the amount necessary for mitosis, and thus forms a CDK activity buffer between sufficient and maximal possible CDK activities. This CDK activity buffer is needed for mitotic completion when CDK activity is compromised, and CDK inhibition only becomes lethal to cells when this buffer is exhausted. Finally, we explore what factors influence this CDK activity buffer, and find that it is influenced by CDK-counteracting phosphatases. Therefore, maximum attainable CDK activity is not necessary for mitosis but provides robustness to CDK activity reduction to ensure mitotic completion.","doi":"10.1242/jcs.259626","authors":"Basu S, Patterson JO, Zeisner TU, Nurse P","authors_abbrev":"Basu S et al.","pubmed_publication_date":"15 Jun 2022","pubmed_entrez_date":"2022-06-21","publication_year":"2022","canto_session_key":"6e1cda7882848261","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-06-23 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5410809","title":"[Study of mitotic conversions at level of ad-9 gene in Schizosaccharomyces pombe].","citation":"Mutat Res 1970 Jan;9(1):41-58","abstract":"","authors":"Adondi G, Heslot H","authors_abbrev":"Adondi G et al.","pubmed_publication_date":"Jan 1970","pubmed_entrez_date":"1970-01-01","publication_year":"1970","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25997339","title":"In vitro systems for the study of microtubule-based cell polarity in fission yeast.","citation":"Methods Cell Biol 2015;128:1-22","abstract":"Establishment of cell polarity is essential for processes such as growth and division. In fission yeast, as well as other species, polarity factors travel at the ends of microtubules to cortical sites where they associate with the membrane and subsequently maintain a polarized activity pattern despite their ability to diffuse in the membrane. In this chapter we present methods to establish an in vitro system that captures the essential features of this process. This bottom-up approach allows us to identify the minimal molecular requirements for microtubule-based cell polarity. We employ microfabrication techniques combined with surface functionalization to create rigid chambers with affinity for proteins, as well as microfluidic techniques to create and shape emulsion droplets with functionalized lipid boundaries. Preliminary results are shown demonstrating that a properly organized microtubule cytoskeleton can be confined to these confined spaces, and proteins traveling at the ends of growing microtubules can be delivered to their boundaries.","doi":"10.1016/bs.mcb.2015.02.008","authors":"Taberner N, Lof A, Roth S, Lamers D, Zeijlemaker H, Dogterom M","authors_abbrev":"Taberner N et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-05-23","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-05-24 00:19:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17694088","title":"Arabidopsis histone deacetylase 6: a green link to RNA silencing.","citation":"Oncogene 2007 Aug 13;26(37):5477-88","abstract":"Epigenetic reprogramming is at the base of cancer initiation and progression. Generally, genome-wide reduction in cytosine methylation contrasts with the hypermethylation of control regions of functionally well-established tumor suppressor genes and many other genes whose role in cancer biology is not yet clear. While insight into mechanisms that induce aberrant cytosine methylation in cancer cells is just beginning to emerge, the initiating signals for analogous promoter methylation in plants are well documented. In Arabidopsis, the silencing of promoters requires components of the RNA interference machinery and promoter double-stranded RNA (dsRNA) to induce a repressive chromatin state that is characterized by cytosine methylation and histone deacetylation catalysed by the RPD3-type histone deacetylase AtHDA6. Similar mechanisms have been shown to occur in fission yeast and mammals. This review focuses on the connections between cytosine methylation, dsRNA and AtHDA6-controlled histone deacetylation during promoter silencing in Arabidopsis and discusses potential mechanistic similarities of these silencing events in cancer and plant cells.","authors":"Aufsatz W, Stoiber T, Rakic B, Naumann K","authors_abbrev":"Aufsatz W et al.","pubmed_publication_date":"13 Aug 2007","pubmed_entrez_date":"2007-08-19","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32938716","title":"Assaying three-dimensional cellular architecture using X-ray tomographic and correlated imaging approaches.","citation":"J Biol Chem 2020 Nov 13;295(46):15782-15793","abstract":"Much of our understanding of the spatial organization of and interactions between cellular organelles and macromolecular complexes has been the result of imaging studies utilizing either light- or electron-based microscopic analyses. These classical approaches, while insightful, are nonetheless limited either by restrictions in resolution or by the sheer complexity of generating multidimensional data. Recent advances in the use and application of X-rays to acquire micro- and nanotomographic data sets offer an alternative methodology to visualize cellular architecture at the nanoscale. These new approaches allow for the subcellular analyses of unstained vitrified cells and three-dimensional localization of specific protein targets and have served as an essential tool in bridging light and electron correlative microscopy experiments. Here, we review the theory, instrumentation details, acquisition principles, and applications of both soft X-ray tomography and X-ray microscopy and how the use of these techniques offers a succinct means of analyzing three-dimensional cellular architecture. We discuss some of the recent work that has taken advantage of these approaches and detail how they have become integral in correlative microscopy workflows.","doi":"10.1074/jbc.REV120.009633","authors":"Bayguinov PO, Fisher MR, Fitzpatrick JAJ","authors_abbrev":"Bayguinov PO et al.","pubmed_publication_date":"13 Nov 2020","pubmed_entrez_date":"2020-09-17","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-09-19 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31418631","title":"Homeostasis in the Central Dogma of molecular biology: the importance of mRNA instability.","citation":"RNA Biol 2019 Dec;16(12):1659-1666","abstract":"Cell survival requires the control of biomolecule concentration, i.e. biomolecules should approach homeostasis. With information-carrying macromolecules, the particular concentration variation ranges depend on each type: DNA is not buffered, but mRNA and protein concentrations are homeostatically controlled, which leads to the ribostasis and proteostasis concepts. In recent years, we have studied the particular features of mRNA ribostasis and proteostasis in the model organism  S. cerevisiae . Here we extend this study by comparing published data from three other model organisms:  E. coli, S. pombe  and cultured human cells. We describe how mRNA ribostasis is less strict than proteostasis. A constant ratio appears between the average decay and dilution rates during cell growth for mRNA, but not for proteins. We postulate that this is due to a trade-off between the cost of synthesis and the response capacity. This compromise takes place at the transcription level, but is not possible at the translation level as the high stability of proteins,  versus  that of mRNAs, precludes it. We hypothesize that the middle-place role of mRNA in the  Central Dogma  of Molecular Biology and its chemical instability make it more suitable than proteins for the fast changes needed for gene regulation.","doi":"10.1080/15476286.2019.1655352","authors":"Pérez-Ortín JE, Tordera V, Chávez S","authors_abbrev":"Pérez-Ortín JE et al.","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-08-17","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-08-18 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8358831","title":"Polyploidy in the haplontic yeast Schizosaccharomyces pombe: construction and analysis of strains.","citation":"Curr Genet 1993;24(1-2):45-52","abstract":"The fission yeast Schizosaccharomyces pombe has a haplontic life cycle in which the diplophase is confined to the zygote. Through the use of one- and two-step protoplast fusions we show that the ploidy can be increased up to pentaploid. The polyploid fusion products are rather unstable and segregate cells of lower ploidies by gradual loss of chromosomes during mitotic divisions. The polyploid cells conjugate normally but are prone to arrest at various stages of meiosis (1-, 2- and 3-spored asci, binucleate spores) and/or produce inviable, most probably aneuploid, spores. Marker segregation in the complete tetrads indicates the multiple association of homologous chromosomes. In tetra- and penta-ploid meiosis, multispored (6- to 7-spored) asci are also produced, probably by postmeiotic division of the nuclei.","authors":"Molnar M, Sipiczki M","authors_abbrev":"Molnar M et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-07-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19804755","title":"Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair.","citation":"Cell 2009 Oct 02;139(1):87-99","abstract":"The Nijmegen breakage syndrome 1 (Nbs1) subunit of the Mre11-Rad50-Nbs1 (MRN) complex protects genome integrity by coordinating double-strand break (DSB) repair and checkpoint signaling through undefined interactions with ATM, MDC1, and Sae2/Ctp1/CtIP. Here, fission yeast and human Nbs1 structures defined by X-ray crystallography and small angle X-ray scattering (SAXS) reveal Nbs1 cardinal features: fused, extended, FHA-BRCT(1)-BRCT(2) domains flexibly linked to C-terminal Mre11- and ATM-binding motifs. Genetic, biochemical, and structural analyses of an Nbs1-Ctp1 complex show Nbs1 recruits phosphorylated Ctp1 to DSBs via binding of the Nbs1 FHA domain to a Ctp1 pThr-Asp motif. Nbs1 structures further identify an extensive FHA-BRCT interface, a bipartite MDC1-binding scaffold, an extended conformational switch, and the molecular consequences associated with cancer predisposing Nijmegen breakage syndrome mutations. Tethering of Ctp1 to a flexible Nbs1 arm suggests a mechanism for restricting DNA end processing and homologous recombination activities of Sae2/Ctp1/CtIP to the immediate vicinity of DSBs.","doi":"10.1016/j.cell.2009.07.033","authors":"Williams RS, Dodson GE, Limbo O, Yamada Y, Williams JS, Guenther G, Classen S, Glover JN, Iwasaki H, Russell P, Tainer JA","authors_abbrev":"Williams RS et al.","pubmed_publication_date":"02 Oct 2009","pubmed_entrez_date":"2009-10-07","publication_year":"2009","canto_session_key":"7622b54e59b561d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-11-21 19:08:47","canto_approved_date":"2022-07-21 15:46:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-14 16:52:44","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":80,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.09c","SPAC3G6.06c","SPAC13C5.07","SPCC338.08"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-11-21","pdb_entries":[{"pdb_id":"3hue","gene_chains":[{"gene_uniquename":"SPBC6B1.09c","chain":"A","position":"1-330"}],"title":"Structure of the S. pombe Nbs1 FHA-BRCT1-BRCT2 domains","entry_authors":"Williams RS,Guenther G,Tainer JA","entry_authors_abbrev":"Williams RS et al.","reference_uniquename":"PMID:19804755","experimental_method":"X-ray","resolution":"2.8"},{"pdb_id":"3huf","gene_chains":[{"gene_uniquename":"SPBC6B1.09c","chain":"A/B/C","position":"1-321"},{"gene_uniquename":"SPCC338.08","chain":"E","position":"72-84"}],"title":"Structure of the S. pombe Nbs1-Ctp1 complex","entry_authors":"Williams RS,Guenther G,Tainer JA","entry_authors_abbrev":"Williams RS et al.","reference_uniquename":"PMID:19804755","experimental_method":"X-ray","resolution":"2.15"}]},{"uniquename":"PMID:18723846","title":"Multiple mechanisms contribute to Schizosaccharomyces pombe origin recognition complex-DNA interactions.","citation":"J Biol Chem 2008 Oct 31;283(44):30216-24","abstract":"Eukaryotic DNA replication requires the assembly of multiprotein pre-replication complexes (pre-RCs) at chromosomal origins of DNA replication. Here we describe the interactions of highly purified Schizosaccharomyces pombe pre-RC components, SpORC, SpCdc18, and SpCdt1, with each other and with ars1 origin DNA. We show that SpORC binds DNA in at least two steps. The first step likely involves electrostatic interactions between the AT-hook motifs of SpOrc4 and AT tracts in ars1 DNA and results in the formation of a salt-sensitive complex. In the second step, the salt-sensitive complex is slowly converted to a salt-stable complex that involves additional interactions between SpORC and DNA. Binding of SpORC to ars1 DNA is facilitated by negative supercoiling and is accompanied by changes in DNA topology, suggesting that SpORC-DNA complexes contain underwound or negatively writhed DNA. Purified human origin recognition complex (ORC) induces similar topological changes in origin DNA, indicating that this property of ORC is conserved in eukaryotic evolution and plays an important role in ORC function. We also show that SpCdc18 and SpCdt1 form a binary complex that has greater affinity for DNA than either protein alone. In addition, both proteins contribute significantly to the stability of the initial SpORC-DNA complex and enhance the SpORC-dependent topology changes in origin DNA. Thus, the formation of stable protein-DNA complexes at S. pombe origins of replication involves binary interactions among all three proteins, as well as interactions of both SpORC and SpCdt1-SpCdc18 with origin DNA. These findings demonstrate that SpORC is not the sole determinant of origin recognition.","doi":"10.1074/jbc.M802649200","authors":"Houchens CR, Lu W, Chuang RY, Frattini MG, Fuller A, Simancek P, Kelly TJ","authors_abbrev":"Houchens CR et al.","pubmed_publication_date":"31 Oct 2008","pubmed_entrez_date":"2008-08-30","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2A9.12","SPBC685.09","SPAC3H1.01c","SPBP23A10.13","SPBC29A10.15","SPBC646.14c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:16428435","title":"Cyclin-dependent kinase 9 (Cdk9) of fission yeast is activated by the CDK-activating kinase Csk1, overlaps functionally with the TFIIH-associated kinase Mcs6, and associates with the mRNA cap methyltransferase Pcm1 in vivo.","citation":"Mol Cell Biol 2006 Feb;26(3):777-88","abstract":"Cyclin-dependent kinase 9 (Cdk9) of fission yeast is an essential ortholog of metazoan positive transcription elongation factor b (P-TEFb), which is proposed to coordinate capping and elongation of RNA polymerase II (Pol II) transcripts. Here we show that Cdk9 is activated to phosphorylate Pol II and the elongation factor Spt5 by Csk1, one of two fission yeast CDK-activating kinases (CAKs). Activation depends on Cdk9 T-loop residue Thr-212. The other CAK-Mcs6, the kinase component of transcription factor IIH (TFIIH)-cannot activate Cdk9. Consistent with the specificities of the two CAKs in vitro, the kinase activity of Cdk9 is reduced approximately 10-fold by csk1 deletion, and Cdk9 complexes from csk1Delta but not csk1+ cells can be activated by Csk1 in vitro. A cdk9(T212A) mutant is viable but phenocopies conditional growth defects of csk1Delta strains, indicating a role for Csk1-dependent activation of Cdk9 in vivo. A cdk9(T212A) mcs6(S165A) strain, in which neither Cdk9 nor Mcs6 can be activated by CAK, has a synthetic growth defect, implying functional overlap between the two CDKs, which have distinct but overlapping substrate specificities. Cdk9 forms complexes in vivo with the essential cyclin Pch1 and with Pcm1, the mRNA cap methyltransferase. The carboxyl-terminal region of Cdk9, through which it interacts with another capping enzyme, the RNA triphosphatase Pct1, is essential. Together, the data support a proposed model whereby Cdk9/Pch1-the third essential CDK-cyclin complex described in fission yeast-helps to target the capping apparatus to the transcriptional elongation complex.","authors":"Pei Y, Du H, Singer J, Stamour C, Granitto S, Shuman S, Fisher RP","authors_abbrev":"Pei Y et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-01-24","publication_year":"2006","canto_session_key":"992e706ca563bba4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-25 12:51:43","canto_approved_date":"2025-05-19 21:27:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-22 15:02:39","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":30,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.19","SPCC330.10","SPBC28F2.12","SPAC1D4.06c","SPBC32F12.06","SPAC644.04","SPBC32H8.10","SPBC19F8.07"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2024-03-25"},{"uniquename":"PMID:17637834","title":"Assembly of microtubules and actomyosin rings in the absence of nuclei and spindle pole bodies revealed by a novel genetic method.","citation":"PLoS One 2007 Jul 18;2(7):e618","abstract":"The nucleus and the centrosomes (spindle pole bodies; SPBs in yeast) are believed to play key roles in the organization of various cellular structures, such as the actomyosin ring and microtubules. The ability to generate cells lacking nuclei and centrosomes (SPBs) is key to the elucidation of the role of these structures in various cellular processes.\nHere we describe a genetic method, using the Schizosaccharomyces pombe cdc16-116 mutant, to reliably and efficiently generate fission yeast cells lacking nuclei and SPBs. We use this approach to show that the assembly of microtubules does not require nuclear associated microtubule organizing centers and SPBs. We also show that actomyosin rings can assemble albeit inefficiently in the absence of nuclei and SPBs.\nWe conclude that key cytoskeletal elements can be assembled in the absence of nuclei and SPBs. In addition, the approach we describe, taken together with physical approaches such as centrifugation, should facilitate the investigation of the role of the nucleus and SPBs in the assembly and inheritance of various cellular structures and organelles.","authors":"Huang Y, Tran PT, Oliferenko S, Balasubramanian MK","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"18 Jul 2007","pubmed_entrez_date":"2007-07-20","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22427686","title":"Characterization of Mid1 domains for targeting and scaffolding in fission yeast cytokinesis.","citation":"J Cell Sci 2012 Jun 15;125(Pt 12):2973-85","abstract":"Division-site selection and contractile-ring assembly are two crucial steps in cytokinesis. In fission yeast, the anillin-like Mid1 protein specifies the division site at the cell equator by assembling cortical nodes, the precursors of the contractile ring. Thus, Mid1 is essential for linking the positional cues for the cleavage site to contractile-ring formation. However, how Mid1 domains cooperate to regulate cytokinesis is poorly understood. Here we unravel the functions of different Mid1 domains (motifs) by a series of truncations. We report that the conserved PH domain stabilizes Mid1 in nodes by binding to lipids and is required for Mid1 cortical localization during interphase in the absence of Cdr2 kinase. Mid1 lacking an internal region that is approximately one third of the full-length protein has higher nuclear and cortical concentration and suppresses the division-site positioning defects in cells with a deletion of the dual-specificity tyrosine-regulated kinase Pom1. The N-terminus of Mid1 physically interacts with cytokinesis node proteins. When fused to cortical node protein Cdr2, Mid1(1-100) is sufficient to assemble cytokinesis nodes and the contractile ring. Collectively, our study recognizes domains regulating Mid1 cortical localization and reveals domains sufficient for contractile-ring assembly.","doi":"10.1242/jcs.102574","authors":"Lee IJ, Wu JQ","authors_abbrev":"Lee IJ et al.","pubmed_publication_date":"15 Jun 2012","pubmed_entrez_date":"2012-03-20","publication_year":"2012","canto_session_key":"a4941387dd36601f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-06 16:22:36","canto_approved_date":"2024-08-07 16:10:34","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-06 16:22:30","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":107,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAC31A2.16","SPCC4B3.15","SPAC4F8.13c","SPAC2F7.03c","SPAC57A10.02","SPAC926.03","SPAP8A3.08","SPAC20G8.05c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2024-08-06"},{"uniquename":"PMID:15545655","title":"Conserved locus-specific silencing functions of Schizosaccharomyces pombe sir2+.","citation":"Genetics 2005 Mar;169(3):1243-60","abstract":"In Schizosaccharomyces pombe, three genes, sir2(+), hst2(+), and hst4(+), encode members of the Sir2 family of conserved NAD(+)-dependent protein deacetylases. The S. pombe sir2(+) gene encodes a nuclear protein that is not essential for viability or for resistance to treatment with UV or a microtubule-destabilizing agent. However, sir2(+) is essential for full transcriptional silencing of centromeres, telomeres, and the cryptic mating-type loci. Chromatin immunoprecipitation results suggest that the Sir2 protein acts directly at these chromosomal regions. Enrichment of Sir2p at silenced regions does not require the HP1 homolog Swi6p; instead, Swi6-GFP localization to telomeres depends in part on Sir2p. The phenotype of sir2 swi6 double mutants supports a model whereby Sir2p functions prior to Swi6p at telomeres and the silent mating-type loci. However, Sir2p does not appear to be essential for the localization of Swi6p to centromeric foci. Cross-complementation experiments showed that the Saccharomyces cerevisiae SIR2 gene can function in place of S. pombe sir2(+), suggesting overlapping deacetylation substrates in both species. These results also suggest that, despite differences in most of the other molecules required, the two distantly related yeast species share a mechanism for targeting Sir2p homologs to silent chromatin.","authors":"Freeman-Cook LL, Gómez EB, Spedale EJ, Marlett J, Forsburg SL, Pillus L, Laurenson P","authors_abbrev":"Freeman-Cook LL et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2004-11-17","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.07c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:30991417","title":"Killer Meiotic Drive and Dynamic Evolution of the wtf Gene Family.","citation":"Mol Biol Evol 2019 Jun 01;36(6):1201-1214","abstract":"Natural selection works best when the two alleles in a diploid organism are transmitted to offspring at equal frequencies. Despite this, selfish loci known as meiotic drivers that bias their own transmission into gametes are found throughout eukaryotes. Drive is thought to be a powerful evolutionary force, but empirical evolutionary analyses of drive systems are limited by low numbers of identified meiotic drive genes. Here, we analyze the evolution of the wtf gene family of Schizosaccharomyces pombe that contains both killer meiotic drive genes and suppressors of drive. We completed assemblies of all wtf genes for two S. pombe isolates, as well as a subset of wtf genes from over 50 isolates. We find that wtf copy number can vary greatly between isolates and that amino acid substitutions, expansions and contractions of DNA sequence repeats, and nonallelic gene conversion between family members all contribute to dynamic wtf gene evolution. This work demonstrates the power of meiotic drive to foster rapid evolution and identifies a recombination mechanism through which transposons can indirectly mobilize meiotic drivers.","doi":"10.1093/molbev/msz052","authors":"Eickbush MT, Young JM, Zanders SE","authors_abbrev":"Eickbush MT et al.","pubmed_publication_date":"01 Jun 2019","pubmed_entrez_date":"2019-04-17","publication_year":"2019","canto_session_key":"9cfb203b56e8d5e3","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-04-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC548.03c","SPCC162.04c","SPCC1450.08c","SPCC285.06c","SPCC548.02c","SPCC285.07c","SPCC830.02","SPCC553.05c","SPCC306.10","SPCC1906.03","SPCC1620.02","SPCC1739.15","SPCC1919.06c","SPCC663.17","SPCC794.02","SPCC622.21","SPBC1706.02c","SPCC1281.08","SPCC736.05","SPCC663.02","SPCC1183.10","SPCC1906.04"],"gene_count":22,"ltp_gene_count":0},{"uniquename":"PMID:3520151","title":"Sloppy size control of the cell division cycle.","citation":"J Theor Biol 1986 Feb 21;118(4):405-26","abstract":"In an asynchronous, exponentially proliferating cell culture there is a great deal of variability among individual cells in size at birth, size at division and generation time (= age at division). To account for this variability we assume that individual cells grow according to some given growth law and that, after reaching a minimum size, they divide with a certain probability (per unit time) which increases with increasing cell size. This model is called sloppy size control because cell division is assumed to be a random process with size-dependent probability. We derive general equations for the distribution of cell size at division, the distribution of generation time, and the correlations between generation times of closely related cells. Our theoretical results are compared in detail with experimental results (obtained by Miyata and coworkers) for cell division in fission yeast, Schizosaccharomyces pombe. The agreement between theory and experiment is superior to that found for any other simple models of the coordination of cell growth and division.","authors":"Tyson JJ, Diekmann O","authors_abbrev":"Tyson JJ et al.","pubmed_publication_date":"21 Feb 1986","pubmed_entrez_date":"1986-02-21","publication_year":"1986","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25736293","title":"Dynactin and Num1 cooperate to establish the cortical anchoring of cytoplasmic dynein in S. pombe.","citation":"J Cell Sci 2015 Apr 15;128(8):1555-67","abstract":"Chromosome movement during meiosis is crucial for homologous pairing and meiotic recombination. During meiotic prophase in fission yeast, rapid nuclear migration is dependent on cytoplasmic dynein, which is anchored to the cell cortex and pulls microtubules, thereby driving nuclear migration. However, the precise mechanisms underlying dynein localization and activation remain unclear. Here, we identified three subunits of dynactin in fission yeast: Arp1, Mug5 and Jnm1 (also known as Mug1). These subunits transiently colocalized with dynein foci at the cell cortex and were essential for the cortical anchoring of dynein. Cortical factor Num1 (also known as Mcp5), which was also required for dynein anchoring, bound to dynein independently of dynactin. Whereas Num1 suppressed the sliding of dynein foci along the cortex, Arp1, Mug5 and Jnm1 were involved in the regulation of shrinkage and bundling of microtubules. From these data, we propose that dynein anchoring is established by cooperation of transient assembly of dynactin and function of Num1 at the cell cortex.","doi":"10.1242/jcs.163840","authors":"Fujita I, Yamashita A, Yamamoto M","authors_abbrev":"Fujita I et al.","pubmed_publication_date":"15 Apr 2015","pubmed_entrez_date":"2015-03-05","publication_year":"2015","canto_session_key":"a4cb97c63c8d6665","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-01-04 10:16:03","canto_approved_date":"2026-04-05 19:05:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-26 14:53:45","canto_added_date":"2015-03-06 01:15:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":68,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.03","SPBC1347.12","SPBC646.17c","SPAC14C4.08","SPAC27D7.13c","SPAC1805.08","SPBC216.02","SPAC1093.06c","SPAC458.04c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2018-01-04"},{"uniquename":"PMID:40873007","title":"PPA2 activates MTFP1-DNM1L fission signaling to govern mitochondrial proliferation and mitophagy.","citation":"Autophagy 2026 Jan;22(1):121-144","abstract":"The inorganic pyrophosphatase PPA2, a matrix-localized protein, maintains mitochondrial function. Here, we identified the role of PPA2 in activating mitochondrial fission signaling. We found that PPA2 overexpression promotes mitochondrial fission by upregulating the mitochondrial translocation of phosphorylated DNM1L S616. Moreover, PPA2 interacts with MTFP1, a mitochondrial inner membrane protein, to induce fission signaling; cells knocked down for MTFP1 and overexpressing PPA2 failed to induce DNM1L activation and subsequent mitochondrial fission. Furthermore, in physiological conditions, PPA2 directed mitochondrial fission at the midzone through MFF-DNM1L, leading to mitochondrial proliferation. Interestingly, during mitochondrial stress following CCCP treatment, PPA2 triggers peripheral fission through FIS1 and DNM1L to segregate parts of damaged mitochondria, which is essential for mitophagy. In addition, PPA2 utilized the C-terminal LC3-interacting region (LIR) of MTFP1 for mitophagy-mediated clearance of damaged mitochondria. In conclusion, PPA2 activates mitochondrial fission signaling through MTFP1-DNM1L and is essential in defining the site of mitochondrial fission, leading to mitochondrial proliferation or mitophagy for maintaining mitochondrial homeostasis. Abbreviations:  CCCP: carbonyl cyanide m-chlorophenyl hydrazone; Co-IP: co-immunoprecipitation; CQ: chloroquine; IMM: inner mitochondrial membrane; LIR: LC3-interacting region; MLS: mitochondrial localization signal; mtDNA: mitochondrial DNA; OMM: outer mitochondrial membrane; RT: room temperature.","doi":"10.1080/15548627.2025.2552900","authors":"Mishra SR, Mishra P, Mahapatra KK, Behera BP, Kendre G, Alotaibi MR, Pandey V, Patro BS, Klionsky DJ, Bhutia SK","authors_abbrev":"Mishra SR et al.","pubmed_publication_date":"Jan 2026","pubmed_entrez_date":"2025-08-28","publication_year":"2026","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16H5.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10855490","title":"Hanging on to your homolog: the roles of pairing, synapsis and recombination in the maintenance of homolog adhesion.","citation":"Chromosoma 2000;109(1-2):3-9","abstract":"Homologous chromosomes initially undergo weak alignments that bring homologous sequences into register during meiosis. These alignments can be facilitated by two types of mechanisms: interstitial homology searches and telomere-telomere alignments. As prophase (and chromatin compaction) proceeds, these initial pairings or alignments need to be stabilized. In at least some organisms, such as Saccharomyces cerevisiae and S. pombe, these pairings can apparently be maintained by the creation of recombination intermediates. In contrast, synapsis during zygotene may be able to facilitate and/or maintain chromosome pairing even in the absence of exchange in several higher organisms. It thus seems possible that the synaptonemal complex plays a role both in maintaining homolog adhesion during meiotic prophase and, more speculatively, in facilitating meiotic exchange.","authors":"Walker MY, Hawley RS","authors_abbrev":"Walker MY et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-06-16","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18223116","title":"Key function for the CCAAT-binding factor Php4 to regulate gene expression in response to iron deficiency in fission yeast.","citation":"Eukaryot Cell 2008 Mar;7(3):493-508","abstract":"The fission yeast Schizosaccharomyces pombe responds to the deprivation of iron by inducing the expression of the php4+ gene, which encodes a negative regulatory subunit of the heteromeric CCAAT-binding factor. Once formed, the Php2/3/4/5 transcription complex is required to inactivate a subset of genes encoding iron-using proteins. Here, we used a pan-S. pombe microarray to study the transcriptional response to iron starvation and identified 86 genes that exhibit php4+-dependent changes on a genome-wide scale. One of these genes encodes the iron-responsive transcriptional repressor Fep1, whose mRNA levels were decreased after treatment with the permeant iron chelator 2,2'-dipyridyl. In addition, several genes encoding the components of iron-dependent biochemical pathways, including the tricarboxylic acid cycle, mitochondrial respiration, amino acid biosynthesis, and oxidative stress defense, were downregulated in response to iron deficiency. Furthermore, Php4 repressed transcription when brought to a promoter using a yeast DNA-binding domain, and iron deprivation was required for this repression. On the other hand, Php4 was constitutively active when glutathione levels were depleted within the cell. Based on these and previous results, we propose that iron-dependent inactivation of Php4 is regulated at two distinct levels: first, at the transcriptional level by the iron-responsive GATA factor Fep1 and second, at the posttranscriptional level by a mechanism yet to be identified, which inhibits Php4-mediated repressive function when iron is abundant.","doi":"10.1128/EC.00446-07","authors":"Mercier A, Watt S, Bähler J, Labbé S","authors_abbrev":"Mercier A et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-01-29","publication_year":"2008","canto_session_key":"3dc265797d97f877","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-05-23 23:00:36","canto_approved_date":"2024-12-12 18:49:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-23 23:00:19","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.16","SPAC10F6.01c","SPAC1F7.08","SPCC330.12c","SPAC23C11.08","SPBC16E9.01c","SPAC22F3.10c","SPBC725.11c","SPCC757.07c","SPAPB1E7.07","SPCC645.03c","SPAC9E9.03","SPCC191.07","SPCC1235.02","SPAC20G8.04c","SPAC24B11.13","SPAC23E2.01","SPAC24C9.06c","SPBC3B8.02","SPAC13A11.02c","SPAC26F1.14c","SPBC29A3.18","SPAC140.01"],"gene_count":23,"ltp_gene_count":4,"approved_date":"2019-05-23"},{"uniquename":"PMID:28475874","title":"Unprotected Replication Forks Are Converted into Mitotic Sister Chromatid Bridges.","citation":"Mol Cell 2017 May 04;66(3):398-410.e4","abstract":"Replication stress and mitotic abnormalities are key features of cancer cells. Temporarily paused forks are stabilized by the intra-S phase checkpoint and protected by the association of Rad51, which prevents Mre11-dependent resection. However, if a fork becomes dysfunctional and cannot resume, this terminally arrested fork is rescued by a converging fork to avoid unreplicated parental DNA during mitosis. Alternatively, dysfunctional forks are restarted by homologous recombination. Using fission yeast, we report that Rad52 and the DNA binding activity of Rad51, but not its strand-exchange activity, act to protect terminally arrested forks from unrestrained Exo1-nucleolytic activity. In the absence of recombination proteins, large ssDNA gaps, up to 3 kb long, occur behind terminally arrested forks, preventing efficient fork merging and leading to mitotic sister chromatid bridging. Thus, Rad52 and Rad51 prevent temporarily and terminally arrested forks from degrading and, despite the availability of converging forks, converting to anaphase bridges causing aneuploidy and cell death.","doi":"10.1016/j.molcel.2017.04.002","authors":"Ait Saada A, Teixeira-Silva A, Iraqui I, Costes A, Hardy J, Paoletti G, Fréon K, Lambert SAE","authors_abbrev":"Ait Saada A et al.","pubmed_publication_date":"04 May 2017","pubmed_entrez_date":"2017-05-06","publication_year":"2017","canto_session_key":"92141eb3ba63c234","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Lambert","canto_first_approved_date":"2017-07-27 13:31:59","canto_approved_date":"2022-07-09 10:57:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-22 10:34:33","canto_added_date":"2017-05-08 00:15:15","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sarah Lambert","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPAC644.14c","SPBC29A10.05","SPAC1556.01c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-07-27"},{"uniquename":"PMID:12683916","title":"Mining meiosis and gametogenesis with DNA microarrays.","citation":"Reproduction 2003 Apr;125(4):447-56","abstract":"Gametogenesis is a key developmental process that involves complex transcriptional regulation of numerous genes including many that are conserved between unicellular eukaryotes and mammals. Recent expression-profiling experiments using microarrays have provided insight into the co-ordinated transcription of several hundred genes during mitotic growth and meiotic development in budding and fission yeast. Furthermore, microarray-based studies have identified numerous loci that are regulated during the cell cycle or expressed in a germ-cell specific manner in eukaryotic model systems like Caenorhabditis elegans, Mus musculus as well as Homo sapiens. The unprecedented amount of information produced by post-genome biology has spawned novel approaches to organizing biological knowledge using currently available information technology. This review outlines experiments that contribute to an emerging comprehensive picture of the molecular machinery governing sexual reproduction in eukaryotes.","authors":"Schlecht U, Primig M","authors_abbrev":"Schlecht U et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-04-10","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19211663","title":"A junction branch point adjacent to a DNA backbone nick directs substrate cleavage by Saccharomyces cerevisiae Mus81-Mms4.","citation":"Nucleic Acids Res 2009 Apr;37(6):2026-36","abstract":"The DNA structure-selective endonuclease Mus81-Mms4/Eme1 incises a number of nicked joint molecule substrates in vitro. 3'-flaps are an excellent in vitro substrate for Mus81-Mms4/Eme1. Mutants in MUS81 are synthetically lethal with mutations in the 5'-flap endonuclease FEN1/Rad27 in Saccharomyces cerevisiae and Schizosaccharomyces pombe. Considering the possibility for isoenergetic interconversion between 3'- and 5'- flaps, these data are consistent with the hypothesis that Mus81-Mms4/Eme1 acts on 3'-flaps in vivo. FEN1/Rad27 prefers dually flapped substrates and cleaves in a way that allows direct ligation of the resulting nick in the product duplex. Here we test the activity of Mus81-Mms4 on dually flapped substrates and find that in contrast to FEN1/Rad27, Mus81-Mms4 activity is impaired on such substrates, resulting in cleavage products that do not allow direct religation. We conclude that Mus81-Mms4, unlike FEN1/Rad27, does not prefer dually flapped substrates and is unlikely to function as a 3'-flapase counterpart to the 5'-flapase activity of FEN1/Rad27. We further find that joint molecule incision by Mus81-Mms4 occurs in a fashion determined by the branch point, regardless of the position of an upstream duplex end. These findings underscore the significance of a nick adjacent to a branch point for Mus81-Mms4 incision.","doi":"10.1093/nar/gkp038","authors":"Ehmsen KT, Heyer WD","authors_abbrev":"Ehmsen KT et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-02-13","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17502918","title":"A cyclin-dependent kinase that promotes cytokinesis through modulating phosphorylation of the carboxy terminal domain of the RNA Pol II Rpb1p sub-unit.","citation":"PLoS One 2007 May 09;2(5):e433","abstract":"In Schizosaccharomyces pombe, the nuclear-localized kinase, Lsk1p, promotes cytokinesis by positively regulating the Septation Initiation Network (SIN). Although a member of the cyclin-dependent kinase (CDK) family, neither a cyclin partner nor a physiological target has been identified. In this report we identify a cyclin, Lsc1p, that physically interacts and co-localizes with Lsk1p. Furthermore, lsk1Delta, lsc1Delta, as well as kinase-dead lsk1-K306R mutants, display highly similar cytokinesis defects. Lsk1p is related to CDKs that phosphorylate the carboxy-terminal domain (CTD) of the largest sub-unit of RNA polymerase II (Rpb1p). Interestingly, we find that Lsk1p and Lsc1p are required for phosphorylation of Ser-2 residues found in the heptad repeats of the CTD. To determine if Rpb1p could be a physiological target, we replaced the native rpb1 gene with a synthetic gene encoding a Rpb1p protein in which Ser-2 was substituted with the non-phosphorylatable amino-acid alanine in all heptads. Cells carrying this allele were similar to lsk1Delta mutants: They were viable, displayed genetic interactions with the SIN, and were unable to complete cytokinesis upon perturbation of the cell division machinery. We conclude that Ser-2 phosphorylation of the CTD heptads plays a novel physiological role in the regulation of cytokinesis.","authors":"Karagiannis J, Balasubramanian MK","authors_abbrev":"Karagiannis J et al.","pubmed_publication_date":"09 May 2007","pubmed_entrez_date":"2007-05-16","publication_year":"2007","canto_session_key":"5f111670d68adbbd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-23 15:08:51","canto_approved_date":"2023-08-10 14:24:29","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2015-11-23 15:08:43","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPAC19B12.05c","SPAC6F6.08c","SPBC530.13","SPBC24C6.07","SPAC1782.09c","SPAC2F3.15"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-11-23"},{"uniquename":"PMID:39519309","title":"Structural Features of DNA in tRNA Genes and Their Upstream Sequences.","citation":"Int J Mol Sci 2024 Nov 01;25(21)","abstract":"RNA polymerase III (Pol III) transcribes tRNA genes using type II promoters. The internal control regions contain a Box A and a Box B, which are recognized by TFIIIC. The 5'-flanking regions of tRNA genes clearly play a role in the regulation of transcription, but consensus sequences in it have been found only in some plants and  S. pombe ; although, the TATA binding protein (TBP) is a component of the TFIIIB complex in all eukaryotes. Archaea utilize an ortholog of the TBP. The goal of this work is the detection of the positions of intragenic and extragenic promoters of Pol III, which regulate the transcription of tRNA genes in eukaryotes and archaea. For this purpose, we analyzed textual and some structural, mechanical, and physicochemical properties of the DNA in the 5'-flanking regions of tRNA genes, as well as in 30 bp at the beginning of genes and 60 bp at the end of genes in organisms possessing the TBP or its analog (eukaryotes, archaea) and organisms not possessing the TBP (bacteria). Representative tRNA gene sets of 11 organisms were taken from the GtRNAdb database. We found that the consensuses of A- and B-boxes in organisms from all three domains are identical; although, they differ in the conservativism of some positions. Their location relative to the ends of tRNA genes is also identical. In contrast, the structural and mechanical properties of DNA in the 5'-flanking regions of tRNA genes differ not only between organisms from different domains, but also between organisms from the same domain. Well-expressed TBP binding positions are found only in  S. pombe  and  A. thaliana . We discuss possible reasons for the variability of the 5'-flanking regions of tRNA genes.","doi":"10.3390/ijms252111758","authors":"Savina EA, Shumilina TG, Porolo VA, Lebedev GS, Orlov YL, Anashkina AA, Il'icheva IA","authors_abbrev":"Savina EA et al.","pubmed_publication_date":"01 Nov 2024","pubmed_entrez_date":"2024-11-09","publication_year":"2024","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7957060","title":"Premature chromatin condensation upon accumulation of NIMA.","citation":"EMBO J 1994 Oct 17;13(20):4926-37","abstract":"The NIMA protein kinase of Aspergillus nidulans is required for the G2/M transition of the cell cycle. Mutants lacking NIMA arrest without morphological characteristics of mitosis, but they do contain an activated p37nimX kinase (the Aspergillus homologue of p34cdc2). To gain a better understanding of NIMA function we have investigated the effects of expressing various NIMA constructs in Aspergillus, fission yeast and human cells. Our experiments have shown that the instability of the NIMA protein requires sequences in the non-catalytic C-terminus of the protein. Removal of this domain results in a stable protein that, once accumulated, promotes a lethal premature condensation of chromatin without any other aspects of mitosis. Similar effects were also observed in fission yeast and human cells accumulating Aspergillus NIMA. This phenotype is independent of cell cycle progression and does not require p34cdc2 kinase activity. As gain of NIMA function by accumulation results in premature chromatin condensation, and loss of NIMA function results in an inability to enter mitosis, we propose that NIMA functions in G2 to promote the condensation of chromatin normally associated with entry into mitosis.","authors":"O'Connell MJ, Norbury C, Nurse P","authors_abbrev":"O'Connell MJ et al.","pubmed_publication_date":"17 Oct 1994","pubmed_entrez_date":"1994-10-17","publication_year":"1994","canto_session_key":"c8f6d94453228801","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-03-09 10:49:31","canto_approved_date":"2020-03-09 10:49:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-02 16:28:04","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC11B10.09","SPBC336.12c"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2020-03-09"},{"uniquename":"PMID:19111658","title":"HP1 proteins form distinct complexes and mediate heterochromatic gene silencing by nonoverlapping mechanisms.","citation":"Mol Cell 2008 Dec 26;32(6):778-90","abstract":"HP1 proteins are a highly conserved family of eukaryotic proteins that bind to methylated histone H3 lysine 9 (H3K9) and are required for heterochromatic gene silencing. In fission yeast, two HP1 homologs, Swi6 and Chp2, function in heterochromatic gene silencing, but their relative contribution to silencing remains unknown. Here we show that Swi6 and Chp2 exist in nonoverlapping complexes and make distinct contributions to silencing. Chp2 associates with the SHREC histone deacetylase complex (SHREC2), is required for histone H3 lysine 14 (H3K14) deacetylation, and mediates transcriptional repression by limiting RNA polymerase II access to heterochromatin. In contrast, Swi6 associates with a different set of nuclear proteins and with noncoding centromeric transcripts and is required for efficient RNAi-dependent processing of these transcripts. Our findings reveal an unexpected role for Swi6 in RNAi-mediated gene silencing and suggest that different HP1 proteins ensure full heterochromatic gene silencing through largely nonoverlapping inhibitory mechanisms.","doi":"10.1016/j.molcel.2008.10.026","authors":"Motamedi MR, Hong EJ, Li X, Gerber S, Denison C, Gygi S, Moazed D","authors_abbrev":"Motamedi MR et al.","pubmed_publication_date":"26 Dec 2008","pubmed_entrez_date":"2008-12-30","publication_year":"2008","canto_session_key":"31f83944ec9ea1a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-09-24 16:01:51","canto_approved_date":"2025-07-02 16:33:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-09-24 16:01:44","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":80,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":54,"orcid":"0000-0003-4148-4606","file_type":"interaction","file_name":"PMID_19111658_interactions.tab2.txt"}],"genes":["SPBC800.03","SPBC16C6.10","SPBC1A4.03c","SPBC660.13c","SPAC1250.01","SPCC1753.01c","SPAC4A8.15c","SPBC2D10.17","SPAC25A8.01c","SPAC9E9.10c","SPBC14F5.12c","SPCC1672.02c","SPAC18G6.02c","SPBP35G2.10","SPBC8D2.04","SPAC6F12.09","SPBP23A10.08","SPBC1105.11c","SPAC19G12.06c","SPBC83.08","SPCC417.07c","SPCC622.08c","SPCC622.09","SPAC23G3.10c","SPAC17G8.03c","SPCC188.07","SPAC3G6.01","SPAC4G9.08c","SPAPB8E5.09","SPAC1B3.17","SPBC4B4.03","SPAC664.01c","SPBC8D2.03c","SPAC1071.06","SPAC21E11.03c","SPAC31G5.19","SPBC29B5.01","SPBC365.10","SPBC28F2.12","SPAC1783.05","SPAC17G6.10","SPBC428.08c","SPBC1861.02","SPBC1734.15","SPCC1281.05","SPBC1105.04c","SPBP8B7.19","SPAC29B12.01","SPAC29E6.08","SPBC557.03c","SPBC609.05","SPAC1834.03c","SPAC1834.04","SPBC1105.12"],"gene_count":54,"ltp_gene_count":8,"approved_date":"2018-09-24"},{"uniquename":"PMID:7334057","title":"Sequential alterations in the nuclear chromatin region during mitosis of the fission yeast Schizosaccharomyces pombe: video fluorescence microscopy of synchronously growing wild-type and cold-sensitive cdc mutants by using a DNA-binding fluorescent probe.","citation":"J Cell Sci 1981 Dec;52:271-87","abstract":"Video-connected fluorescence microscopy was introduced to study the yeast nuclear chromatin region. It was defined as the nuclear area where a DNA-binding fluorescent probe 4',6-diamidino-2-phenylindole specifically bound and fluoresced. The 3-dimensional feature of the mitotic chromatin region was deduced by analysing the successive video images of a cell viewed at different angles. By investigating synchronous culture of the wild-type fission yeast Schizosaccharomyces pombe, we found sequential structural alterations in the chromatin region during mitosis. The steps found include the compaction of the chromatin region from the regular hemispherical form, the formation of a U-shaped intermediate and the rapid segregation into 2 daughter hemispherical forms. Six cs cdc mutants, apparently blocked in mitosis, were observed by fluorescence microscopy. Under the restrictive conditions their chromatin regions exhibited either hemispherical, compact, disk-like, U-shaped or partially segregated chromatin regions. Two mutants showed anomalous nuclear locations. The results of the temperature shift-up experiments of the highly reversible KM52 and KM108 strains supported the above scheme of sequential alterations in the chromatin region.","authors":"Toda T, Yamamoto M, Yanagida M","authors_abbrev":"Toda T et al.","pubmed_publication_date":"Dec 1981","pubmed_entrez_date":"1981-12-01","publication_year":"1981","canto_session_key":"1275ee66e3ff4666","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-03-27 14:50:30","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-03-12 15:36:00","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPBC16A3.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-03-12"},{"uniquename":"PMID:6211144","title":"Sequential utilization of mixed monosaccharides by yeasts.","citation":"Appl Environ Microbiol 1982 Apr;43(4):840-5","abstract":"Four yeasts (Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida utilus, and Rhodotorula toruloides) were tested for their ability to grow and consume D-glucose, D-xylose, D-xylulose, and D-xylitol. Sequential utilization of substrates was observed when D-glucose as mixed with D-xylulose as the carbon source. Catabolite inhibition was tentatively concluded to be responsible for this regulatory mechanism. D-Glucose was also found to inhibit the utilization of D-xylose and D-xylitol in C. utilus and R. toruloides. D-Xylose, D-xylitol, and D-xylulose were consumed simultaneously by R. toruloides and C. utilus.","authors":"Hsiao HY, Chiang LC, Ueng PP, Tsao GT","authors_abbrev":"Hsiao HY et al.","pubmed_publication_date":"Apr 1982","pubmed_entrez_date":"1982-04-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26631744","title":"Conserved factor Dhp1/Rat1/Xrn2 triggers premature transcription termination and nucleates heterochromatin to promote gene silencing.","citation":"Proc Natl Acad Sci U S A 2015 Dec 22;112(51):15548-55","abstract":"Cotranscriptional RNA processing and surveillance factors mediate heterochromatin formation in diverse eukaryotes. In fission yeast, RNAi machinery and RNA elimination factors including the Mtl1-Red1 core and the exosome are involved in facultative heterochromatin assembly; however, the exact mechanisms remain unclear. Here we show that RNA elimination factors cooperate with the conserved exoribonuclease Dhp1/Rat1/Xrn2, which couples pre-mRNA 3'-end processing to transcription termination, to promote premature termination and facultative heterochromatin formation at meiotic genes. We also find that Dhp1 is critical for RNAi-mediated heterochromatin assembly at retroelements and regulated gene loci and facilitates the formation of constitutive heterochromatin at centromeric and mating-type loci. Remarkably, our results reveal that Dhp1 interacts with the Clr4/Suv39h methyltransferase complex and acts directly to nucleate heterochromatin. Our work uncovers a previously unidentified role for 3'-end processing and transcription termination machinery in gene silencing through premature termination and suggests that noncanonical transcription termination by Dhp1 and RNA elimination factors is linked to heterochromatin assembly. These findings have important implications for understanding silencing mechanisms targeting genes and repeat elements in higher eukaryotes.","doi":"10.1073/pnas.1522127112","authors":"Chalamcharla VR, Folco HD, Dhakshnamoorthy J, Grewal SI","authors_abbrev":"Chalamcharla VR et al.","pubmed_publication_date":"22 Dec 2015","pubmed_entrez_date":"2015-12-04","publication_year":"2015","canto_session_key":"399e108c290a4129","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-12-05 01:19:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.12c","SPAC6F12.09","SPCC1739.03","SPAC17H9.02","SPBC16C6.10","SPAC20H4.03c","SPAC19D5.06c","SPAC1071.02","SPCC736.12c","SPBC83.03c","SPAC1F3.01","SPNCRNA.103","SPBC16E9.12c","SPCC970.07c","SPCC11E10.08","SPCC736.11","SPBC20F10.05"],"gene_count":17,"ltp_gene_count":7},{"uniquename":"PMID:30759238","title":"Role of Cdc23/Mcm10 in generating the ribonucleotide imprint at the mat1 locus in fission yeast.","citation":"Nucleic Acids Res 2019 Apr 23;47(7):3422-3433","abstract":"The developmental asymmetry of fission yeast daughter cells derives from inheriting 'older Watson' versus 'older Crick' DNA strand from the parental cell, strands that are complementary but not identical with each other. A novel DNA strand-specific 'imprint', installed during DNA replication at the mating-type locus (mat1), imparts competence for cell type inter-conversion to one of the two chromosome replicas. The catalytic subunit of DNA Polymerase α (Polα) has been implicated in the imprinting process. Based on its known biochemical function, Polα might install the mat1 imprint during lagging strand synthesis. The nature of the imprint is not clear: it is either a nick or a ribonucleotide insertion. Our investigations do not support a direct role of Polα in nicking through putative endonuclease domains but confirm its indirect role in installing an alkali-labile moiety as the imprint. While ruling out the role of the primase subunit of Polα holoenzyme, we find that mutations in the Polα-recruitment and putative primase homology domain in Mcm10/Cdc23 abrogate the ribonucleotide imprint formation. These results, while confirming the ribonucleotide nature of the imprint suggest the possibility of a direct role of Mcm10/Cdc23 in installing it in cooperation with Polα and Swi1.","doi":"10.1093/nar/gkz092","authors":"Singh B, Bisht KK, Upadhyay U, Kushwaha AC, Nanda JS, Srivastava S, Saini JK, Klar AJS, Singh J","authors_abbrev":"Singh B et al.","pubmed_publication_date":"23 Apr 2019","pubmed_entrez_date":"2019-02-14","publication_year":"2019","canto_session_key":"181d196fc3f2df51","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-06-26 08:57:24","canto_approved_date":"2025-02-11 16:09:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-25 18:38:06","canto_added_date":"2019-02-15 01:15:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":65,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC211.04c","SPBC4.04c","SPBC30D10.04","SPAC3H5.06c","SPAC6B12.10c","SPBC1347.10","SPAC1B2.05","SPBC216.06c","SPCC16A11.17","SPBC17D11.06"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2024-06-26"},{"uniquename":"PMID:15979505","title":"Golgi tethering factors.","citation":"Biochim Biophys Acta 2005 Jul 10;1744(3):325-39","abstract":"Transport of cargo to, through and from the Golgi complex is mediated by vesicular carriers and transient tubular connections. In this review, we describe vesicle tethering events with the understanding that similar events occur during transport via larger structures. Tethering factors can be generally divided into a group of coiled-coil proteins and a group of multi-subunit complexes. Current evidence suggests that these factors function in a variety of membrane-membrane tethering events at the Golgi complex, interact with SNARE molecules, and are regulated by small GTPases of the Rab and Arl families.","authors":"Lupashin V, Sztul E","authors_abbrev":"Lupashin V et al.","pubmed_publication_date":"10 Jul 2005","pubmed_entrez_date":"2005-06-28","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29E6.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34010645","title":"The histone H3K9M mutation synergizes with H3K14 ubiquitylation to selectively sequester histone H3K9 methyltransferase Clr4 at heterochromatin.","citation":"Cell Rep 2021 May 18;35(7):109137","abstract":"Oncogenic histone lysine-to-methionine mutations block the methylation of their corresponding lysine residues on wild-type histones. One attractive model is that these mutations sequester histone methyltransferases, but genome-wide studies show that mutant histones and histone methyltransferases often do not colocalize. Using chromatin immunoprecipitation sequencing (ChIP-seq), here, we show that, in fission yeast, even though H3K9M-containing nucleosomes are broadly distributed across the genome, the histone H3K9 methyltransferase Clr4 is mainly sequestered at pericentric repeats. This selective sequestration of Clr4 depends not only on H3K9M but also on H3K14 ubiquitylation (H3K14ub), a modification deposited by a Clr4-associated E3 ubiquitin ligase complex. In vitro, H3K14ub synergizes with H3K9M to interact with Clr4 and potentiates the inhibitory effects of H3K9M on Clr4 enzymatic activity. Moreover, binding kinetics show that H3K14ub overcomes the Clr4 aversion to H3K9M and reduces its dissociation. The selective sequestration model reconciles previous discrepancies and demonstrates the importance of protein-interaction kinetics in regulating biological processes.","doi":"10.1016/j.celrep.2021.109137","authors":"Shan CM, Kim JK, Wang J, Bao K, Sun Y, Chen H, Yue JX, Stirpe A, Zhang Z, Lu C, Schalch T, Liti G, Nagy PL, Tong L, Qiao F, Jia S","authors_abbrev":"Shan CM et al.","pubmed_publication_date":"18 May 2021","pubmed_entrez_date":"2021-05-19","publication_year":"2021","canto_session_key":"1d0fcf1209195c82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Songtao Jia","canto_first_approved_date":"2021-06-10 20:55:48","canto_approved_date":"2021-06-10 20:55:48","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-06-01 04:36:20","canto_added_date":"2021-05-21 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Songtao Jia","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.08","SPBC428.08c","SPAC1834.04","SPAC664.01c","SPAC18G6.02c","SPCC970.07c","SPCC613.12c","SPCC188.13c","SPCC736.11","SPBC1105.11c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2021-06-10"},{"uniquename":"PMID:10441448","title":"Some thoughts about microtubules and cell polarity in fission yeast.","citation":"Fungal Genet Biol 1999;27(2-3):224-30","abstract":"","authors":"Sawin KE","authors_abbrev":"Sawin KE","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-08-12","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17660548","title":"Schizosaccharomyces pombe switches mating type by the synthesis-dependent strand-annealing mechanism.","citation":"Genetics 2007 Sep;177(1):255-65","abstract":"Schizosaccharomyces pombe cells can switch between two mating types, plus (P) and minus (M). The change in cell type occurs due to a replication-coupled recombination event that transfers genetic information from one of the silent-donor loci, mat2P or mat3M, into the expressed mating-type determining mat1 locus. The mat1 locus can as a consequence contain DNA encoding either P or M information. A molecular mechanism, known as synthesis-dependent strand annealing, has been proposed for the underlying recombination event. A key feature of this model is that only one DNA strand of the donor locus provides the information that is copied into the mat1. Here we test the model by constructing strains that switch using two different mutant P cassettes introduced at the donor loci, mat2 and mat3. We show that in such strains wild-type P-cassette DNA is efficiently generated at mat1 through heteroduplex DNA formation and repair. The present data provide an in vivo genetic test of the proposed molecular recombination mechanism.","authors":"Yamada-Inagawa T, Klar AJ, Dalgaard JZ","authors_abbrev":"Yamada-Inagawa T et al.","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-07-31","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20970341","title":"A coordinated global control over cellular transcription.","citation":"Curr Biol 2010 Nov 23;20(22):2010-5","abstract":"Although much is known about the regulation of gene transcription in eukaryotes, it is not clear whether cells have global controls that determine overall rates of transcription. We have investigated the effects that the DNA-to-protein ratio has on both total transcription and the transcription of individual genes in the unicellular eukaryote fission yeast. Mutants altered in cell size and those blocked in cell-cycle progression were used to vary the DNA-to-protein ratio over a 5-fold range. We found that cells of sizes within 2-fold of the wild-type value regulated global transcription to maintain similar transcription rates per protein regardless of the cellular DNA content. These changes in total transcription correlated with coordinated changes in gene occupancy by RNA polymerase II. In cell-cycle-arrested mutants exceeding a certain size, total transcription rates plateaued as DNA became limiting for transcription at low DNA-to-protein ratios [1]. Unexpectedly, expression levels of individual genes remained tightly coordinated with each other over the entire range of cell sizes. We propose that there is a coordinated, global control that determines the rate of transcription of most genes and that this control plays a role in regulating growth rate of the cell.","doi":"10.1016/j.cub.2010.10.002","authors":"Zhurinsky J, Leonhard K, Watt S, Marguerat S, Bähler J, Nurse P","authors_abbrev":"Zhurinsky J et al.","pubmed_publication_date":"23 Nov 2010","pubmed_entrez_date":"2010-10-26","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37851576","title":"The LARP1 homolog Slr1p controls the stability and expression of proto-5'TOP mRNAs in fission yeast.","citation":"Cell Rep 2023 Oct 31;42(10):113226","abstract":"Messenger RNAs (mRNAs) in higher eukaryotes that encode proteins important for the assembly of the translational apparatus (e.g., ribosomal proteins) often harbor a pyrimidine-rich motif at the extreme 5' end known as a 5' terminal oligopyrimidine (5'TOP) sequence. Members of the La-related protein 1 (LARP1) family control 5'TOP expression through a conserved DM15 motif, but the mechanism is not well understood. 5'TOP motifs have not been described in many lower organisms, and fission yeast harbors a LARP1 homolog that also lacks a DM15 motif. In this work, we show that the fission yeast LARP1 homolog, Slr1p, controls the translation and stability of mRNAs encoding proteins analogous to 5'TOP mRNAs in higher eukaryotes, which we thus refer to as proto-5'TOPs. Our data suggest that the LARP1 DM15 motif and the mRNA 5'TOP motif may be features that were scaffolded over a more fundamental mechanism of LARP1-associated control of gene expression.","doi":"10.1016/j.celrep.2023.113226","authors":"Mansouri-Noori F, Pircher A, Bilodeau D, Siniavskaia L, Grigull J, Rissland OS, Bayfield MA","authors_abbrev":"Mansouri-Noori F et al.","pubmed_publication_date":"31 Oct 2023","pubmed_entrez_date":"2023-10-18","publication_year":"2023","canto_session_key":"76cfc5c875fdf959","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-10-18 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1527.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9552412","title":"The cdc18 protein initiates DNA replication in fission yeast.","citation":"Prog Cell Cycle Res 1997;3:135-42","abstract":"Recent work has demonstrated that cdc18p plays a crucial role in regulating the onset of S phase in fission yeast. cdc18p is a major product of START specific transcription and associates with ORC and MCM proteins which are required for the initiation of DNA replication. High expression of cdc18p induces continuing DNA synthesis and is thought to drive the assembly of initiation complexes. In addition to its role in bringing about DNA replication, cdc18p participates in the cell cycle checkpoint control linking S phase to START and mitosis. We propose that cdc18p is central to the molecular mechanism co-ordinating S phase and M phase in concert with changes in activity of the master cell cycle regulator, the cdc2 protein kinase.","authors":"Nishitani H, Nurse P","authors_abbrev":"Nishitani H et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24719968","title":"Switching genes in Schizosaccharomyces pombe.","citation":"Curr Genet 1985;9(5):325-31","abstract":"In homothallic (h 90) Schizosaccharomyces pombe strains mutants occur which exhibit reduced frequencies of mating-type switching. The colonies of such mutants show a mottled iodine reaction. The underlying mutations map either in a switching signal at matl or in switching (swi) genes which are not linked to the mating-type region. Forty-nine swi mutants were examined. They map in ten different swi genes, swil to swil 0. Seven swi genes were assigned to chromosomes I and II, respectively. - Two classes of swi genes can be distinguished: when plated, class I mutants yield only mottled colonies, whereas class II mutants yield mottled and iodine-negative colonies (most of the latter are h⁺).","authors":"Gutz H, Schmidt H","authors_abbrev":"Gutz H et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"2014-04-12","publication_year":"1985","canto_session_key":"bb830d1de0de2d50","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-18 10:54:16","canto_approved_date":"2022-12-12 17:27:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-18 10:54:09","canto_added_date":"2014-05-07 04:48:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8F11.03","SPBC19G7.01c","SPCC970.01","SPAC3H5.06c","SPBC30D10.04","SPAC664.01c","SPAC1142.03c","SPBC409.03","SPBC216.06c","SPBC4F6.15c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2014-06-18"},{"uniquename":"PMID:17483423","title":"Microhomology-mediated end joining in fission yeast is repressed by pku70 and relies on genes involved in homologous recombination.","citation":"Genetics 2007 Jul;176(3):1403-15","abstract":"Two DNA repair pathways are known to mediate DNA double-strand-break (DSB) repair: homologous recombination (HR) and nonhomologous end joining (NHEJ). In addition, a nonconservative backup pathway showing extensive nucleotide loss and relying on microhomologies at repair junctions was identified in NHEJ-deficient cells from a variety of organisms and found to be involved in chromosomal translocations. Here, an extrachromosomal assay was used to characterize this microhomology-mediated end-joining (MMEJ) mechanism in fission yeast. MMEJ was found to require at least five homologous nucleotides and its efficiency was decreased by the presence of nonhomologous nucleotides either within the overlapping sequences or at DSB ends. Exo1 exonuclease and Rad22, a Rad52 homolog, were required for repair, suggesting that MMEJ is related to the single-strand-annealing (SSA) pathway of HR. In addition, MMEJ-dependent repair of DSBs with discontinuous microhomologies was strictly dependent on Pol4, a PolX DNA polymerase. Although not strictly required, Msh2 and Pms1 mismatch repair proteins affected the pattern of MMEJ repair. Strikingly, Pku70 inhibited MMEJ and increased the minimal homology length required for efficient MMEJ. Overall, this study strongly suggests that MMEJ does not define a distinct DSB repair mechanism but reflects \"micro-SSA.\"","authors":"Decottignies A","authors_abbrev":"Decottignies A","pubmed_publication_date":"Jul 2007","pubmed_entrez_date":"2007-05-08","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27481777","title":"Identification of nuclear genes affecting 2-Deoxyglucose resistance in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2016 Sep;16(6)","abstract":"2-Deoxyglucose (2-DG) is a toxic glucose analog. To identify genes involved in 2-DG toxicity in Schizosaccharomyces pombe, we screened a wild-type overexpression library for genes which render cells 2-DG resistant. A gene we termed odr1, encoding an uncharacterized hydrolase, led to strong resistance and altered invertase expression when overexpressed. We speculate that Odr1 neutralizes the toxic form of 2-DG, similar to the Saccharomyces cerevisiae Dog1 and Dog2 phosphatases which dephosphorylate 2-DG-6-phosphate synthesized by hexokinase. In a complementary approach, we screened a haploid deletion library to identify 2-DG-resistant mutants. This screen identified the genes snf5, ypa1, pas1 and pho7 In liquid medium, deletions of these genes conferred 2-DG resistance preferentially under glucose-repressed conditions. The deletion mutants expressed invertase activity more constitutively than the control strain, indicating defects in the control of glucose repression. No S. cerevisiae orthologs of the pho7 gene is known, and no 2-DG resistance has been reported for any of the deletion mutants of the other genes identified here. Moreover, 2-DG leads to derepressed invertase activity in S. pombe, while in S. cerevisiae it becomes repressed. Taken together, these findings suggest that mechanisms involved in 2-DG resistance differ between budding and fission yeasts.","doi":"10.1093/femsyr/fow061","authors":"Vishwanatha A, Rallis C, Bevkal Subramanyaswamy S, D'Souza CJ, Bähler J, Schweingruber ME","authors_abbrev":"Vishwanatha A et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-08-03","publication_year":"2016","canto_session_key":"38c45e3ff2d98c4b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Akshay Vishwanatha","canto_approved_date":"2016-08-10 07:51:02","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-08-09 05:52:26","canto_added_date":"2016-08-03 07:53:35","annotation_curators":[{"name":"Akshay Vishwanatha","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC144.02","SPAC4F10.04","SPAC19E9.03","SPBC27B12.11c","SPAC13A11.05","SPAC637.07","SPBC18H10.19","SPBC215.10","SPCC1494.10","SPCC1259.07","SPAC2F7.08c","SPCC191.11","SPAC1639.02c","SPAC22F8.11"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2016-08-09"},{"uniquename":"PMID:34402513","title":"Phosphorylation in the intrinsically disordered region of F-BAR protein Imp2 regulates its contractile ring recruitment.","citation":"J Cell Sci 2021 Aug 15;134(16)","abstract":"The F-BAR protein Imp2 is an important contributor to cytokinesis in the fission yeast Schizosaccharomyces pombe. Because cell cycle-regulated phosphorylation of the central intrinsically disordered region (IDR) of the Imp2 paralog Cdc15 controls Cdc15 oligomerization state, localization and ability to bind protein partners, we investigated whether Imp2 is similarly phosphoregulated. We found that Imp2 is endogenously phosphorylated on 28 sites within its IDR, with the bulk of phosphorylation being constitutive. In vitro, the casein kinase 1 (CK1) isoforms Hhp1 and Hhp2 can phosphorylate 17 sites, and Cdk1 (also known as Cdc2) can phosphorylate the remaining 11 sites. Mutations that prevent Cdk1 phosphorylation result in precocious Imp2 recruitment to the cell division site, and mutations designed to mimic these phosphorylation events delay Imp2 accumulation at the contractile ring (CR). Mutations that eliminate CK1 phosphorylation sites allow CR sliding, and phosphomimetic substitutions at these sites reduce Imp2 protein levels and slow CR constriction. Thus, like Cdc15, the Imp2 IDR is phosphorylated at many sites by multiple kinases. In contrast to Cdc15, for which phosphorylation plays a major cell cycle regulatory role, Imp2 phosphorylation is primarily constitutive, with milder effects on localization and function. This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.258645","authors":"Willet AH, Igarashi MG, Chen JS, Bhattacharjee R, Ren L, Cullati SN, Elmore ZC, Roberts-Galbraith RH, Johnson AE, Beckley JR, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"15 Aug 2021","pubmed_entrez_date":"2021-08-17","publication_year":"2021","canto_session_key":"0f10611fa56323c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2021-07-28 14:13:18","canto_approved_date":"2023-06-23 15:26:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-07-27 15:24:09","canto_added_date":"2021-08-18 09:10:28","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":105,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16C4.07","SPAC6G9.14","SPAC20G8.05c","SPBC11C11.02","SPBC27.04","SPCC794.11c","SPBC16A3.18","SPAC323.07c","SPBC18H10.04c","SPBC26H8.07c","SPAC17C9.03","SPCC645.05c","SPAC8C9.15c","SPAC23C4.12","SPBC19G7.05c","SPAC24B11.11c","SPBC3H7.15","SPAC23A1.17","SPBC16H5.08c","SPBC11B10.09","SPBC8D2.20c","SPCC1795.11","SPAC13G7.04c","SPBC18H10.03","SPAC4A8.05c"],"gene_count":25,"ltp_gene_count":8,"approved_date":"2021-07-28"},{"uniquename":"PMID:8631305","title":"B-type cyclins regulate G1 progression in fission yeast in opposition to the p25rum1 cdk inhibitor.","citation":"EMBO J 1996 Feb 15;15(4):839-49","abstract":"The onset of S phase in fission yeast is regulated at Start, the point of commitment to the mitotic cell cycle. The p34cdc2 kinase is essential for G1 progression past Start, but until now its regulation has been poorly understood. Here we show that the cig2/cyc17 B-type cyclin has an important role in G1 progression, and demonstrate that p34cdc2 kinase activity is periodically associated with cig2 in G1. Cells lacking cig2 are defective in G1 progression, and this is particularly clear in small cells that must regulate Start with respect to cell size. We also find that the cig1 B-type cyclin can promote G1 progression. Whilst p25rum1 can inhibit cig2/cdc2 activity in vitro, and may transiently inhibit this complex in vivo, cig1 is regulated independently of p25rum1. Since cig1/cdc2 kinase activity peaks in mitotic cells, and decreases after mitosis with similar kinetics to cdc13-associated kinase activity, we suggest that cig2 is likely to be the principal fission yeast G1 cyclin. cig2 protein levels accumulate in G1 cells, and we propose that p25rum1 may transiently inhibit cig2-associated p34cdc2 activity until the critical cell size required for Start is reached.","authors":"Martin-Castellanos C, Labib K, Moreno S","authors_abbrev":"Martin-Castellanos C et al.","pubmed_publication_date":"15 Feb 1996","pubmed_entrez_date":"1996-02-15","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19308707","title":"RAD50, an SMC family member with multiple roles in DNA break repair: how does ATP affect function?","citation":"Chromosome Res 2009;17(2):277-88","abstract":"The protein complex including Mre11, Rad50, and Nbs1 (MRN) functions in DNA double-strand break repair to recognize and process DNA ends as well as signal for cell cycle arrest. Amino acid sequence similarity and overall architecture make Rad50 a member of the structural maintenance of chromosome (SMC) protein family. Like SMC proteins, Rad50 function depends on ATP binding and hydrolysis. All current evidence indicates that ATP binding and hydrolysis cause architectural rearrangements in SMC protein complexes that are important for their functions in organizing DNA. In the case of the MRN complex, the functional significance of ATP binding and hydrolysis are not yet defined. Here we review the data on the ATP-dependent activities of MRN and their possible mechanistic significance. We present some speculation on the role of ATP for function of the MRN complex based on the similarities and differences in the molecular architecture of the Rad50-containing complexes and the SMC complexes condensin and cohesin.","doi":"10.1007/s10577-008-9018-6","authors":"Kinoshita E, van der Linden E, Sanchez H, Wyman C","authors_abbrev":"Kinoshita E et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-03-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8657565","title":"The small subunit of the splicing factor U2AF is conserved in fission yeast.","citation":"Nucleic Acids Res 1996 May 15;24(10):1849-54","abstract":"The human splicing factor U2 auxiliary factor (hsU2AF) is comprised of two interacting subunits of 65 and 35 kDa. Previously we identified the Schizosaccharomyces pombe homolog, spU2AF59, of the human large subunit. We have screened a fission yeast cDNA library in search of proteins that interact with spU2AF59 using the yeast two-hybrid system and have identified a homolog of the hsU2AF35 subunit. The S. pombe U2AF small subunit is a single copy gene that encodes a protein which shares 55% amino acid identity and 17% similarity with the human small subunit. Unlike the human protein, the yeast protein lacks an arginine/serine-rich region. The predicted molecular mass of the spU2AF small subunit is 23 kDa. The region of spU2AF59 that interacts with spU2AF23 is similar to the region in which the human small and large subunits interact.","authors":"Wentz-Hunter K, Potashkin J","authors_abbrev":"Wentz-Hunter K et al.","pubmed_publication_date":"15 May 1996","pubmed_entrez_date":"1996-05-15","publication_year":"1996","canto_session_key":"5648bdc10209d555","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-22 10:04:53","canto_approved_date":"2022-02-24 12:00:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-30 16:13:33","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.07","SPAP8A3.06"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-04-22"},{"uniquename":"PMID:2668944","title":"Adenylate cyclases in yeast: a comparison of the genes from Schizosaccharomyces pombe and Saccharomyces cerevisiae.","citation":"Proc Natl Acad Sci U S A 1989 Aug;86(15):5693-7","abstract":"A Schizosaccharomyces pombe gene encoding adenylate cyclase has been cloned by cross-hybridization with the Saccharomyces cerevisiae adenylate cyclase gene. The protein encoded consists of 1692 amino acids and has adenylate cyclase activity that cannot be activated by the Sa. cerevisiae RAS2 protein. Sc. pombe cyclase has a high degree of homology (approximately 60%) with the catalytic domain of Sa. cerevisiae cyclase precisely mapped by a gene-deletion analysis. A 25-40% identity is observed throughout the middle segments of approximately 1000 residues of both cyclases, large parts of which are composed of repetitions of a 23-amino acid motif similar to those found in human glycoproteins, Drosophila chaoptin, and Toll gene product. However, a segment corresponding to the NH2-terminal 620 residues of Sa. cerevisiae cyclase appears lost from Sc. pombe cyclase, and the COOH-terminal 140 residues are not well conserved between the two yeast species. Deletions involving the COOH-terminal residues of Sa. cerevisiae cyclase cause loss of activation by the RAS2 protein. These results suggest that Sc. pombe cyclase may have lost the ability to interact with RAS proteins by the loss of a regulatory site.","authors":"Yamawaki-Kataoka Y, Tamaoki T, Choe HR, Tanaka H, Kataoka T","authors_abbrev":"Yamawaki-Kataoka Y et al.","pubmed_publication_date":"Aug 1989","pubmed_entrez_date":"1989-08-01","publication_year":"1989","canto_session_key":"3ab49d477832bab2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-30 13:44:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-30 13:43:46","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-09-30"},{"uniquename":"PMID:16280550","title":"Secrets of a double agent: CDK7 in cell-cycle control and transcription.","citation":"J Cell Sci 2005 Nov 15;118(Pt 22):5171-80","abstract":"In metazoans, cyclin-dependent kinase 7 (CDK7) has essential roles in both the cell-division cycle and transcription, as a CDK-activating kinase (CAK) and as a component of the general transcription factor TFIIH, respectively. Controversy over its double duty has been resolved, but questions remain. First, how does CDK7 achieve the dual substrate specificity necessary to perform both roles? Second, is there a deeper connection implied by the dichotomy of CDK7 function, for example similar mechanisms controlling cell division and gene expression, and/or actual coordination of the two processes? Enzymological studies have revealed solutions to the unusual substrate recognition problem, and there is evidence that the distinct functions of CDK7 can be regulated independently. Finally, despite divergence in their wiring, the CAK-CDK networks of budding yeast, fission yeast and metazoans all link transcriptional regulation with operation of the cell-cycle machinery. This connection might help to ensure that mRNAs encoding effectors of cell division are expressed at the right time in the cycle.","authors":"Fisher RP","authors_abbrev":"Fisher RP","pubmed_publication_date":"15 Nov 2005","pubmed_entrez_date":"2005-11-11","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20802492","title":"Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis.","citation":"Nat Chem Biol 2010 Oct;6(10):758-65","abstract":"Cytosolic and nuclear iron-sulfur (Fe-S) proteins play key roles in processes such as ribosome maturation, transcription and DNA repair-replication. For biosynthesis of their Fe-S clusters, a dedicated cytosolic Fe-S protein assembly (CIA) machinery is required. Here, we identify the essential flavoprotein Tah18 as a previously unrecognized CIA component and show by cell biological, biochemical and spectroscopic approaches that the complex of Tah18 and the CIA protein Dre2 is part of an electron transfer chain functioning in an early step of cytosolic Fe-S protein biogenesis. Electrons are transferred from NADPH via the FAD- and FMN-containing Tah18 to the Fe-S clusters of Dre2. This electron transfer chain is required for assembly of target but not scaffold Fe-S proteins, suggesting a need for reduction in the generation of stably inserted Fe-S clusters. The pathway is conserved in eukaryotes, as human Ndor1-Ciapin1 proteins can functionally replace yeast Tah18-Dre2.","doi":"10.1038/nchembio.432","authors":"Netz DJ, Stümpfig M, Doré C, Mühlenhoff U, Pierik AJ, Lill R","authors_abbrev":"Netz DJ et al.","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2010-08-31","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11265754","title":"Fate of mat1 DNA strands during mating-type switching in fission yeast.","citation":"EMBO Rep 2000 Aug;1(2):145-50","abstract":"The mating-type switching of the fission yeast, Schizosaccharomyces pombe, is highly regulated. Two consecutive asymmetric divisions are required to produce one mating-type switched cell among the four progeny. Using DNA density-gradient centrifugation we demonstrate that one-fourth of the mat1 DNA is not replicated by the conventional semi-conservative mode, but instead both DNA strands are synthesized de novo. Our data are consistent with a gene conversion event, initiated by a site- and strand-specific DNA break (SSB). We further demonstrate that the virgin switched mat1-containing chromatid no longer contained the nick, while it is reintroduced during the lagging strand synthesis of the mat1 locus on the sister chromatid. This finding establishes at the molecular level a firm experimental link between the phenotype and genotype in the process of asymmetric mating-type switching during mitotic divisions.","authors":"Arcangioli B","authors_abbrev":"Arcangioli B","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2001-03-27","publication_year":"2000","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:836827","title":"Energy-dependent uptake of calcium by the yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1977 Feb 04;464(3):602-12","abstract":"1. In resting cells of the fission yeast Schizosaccharomyces pombe, the uptake of calcium is stimulated by the addition of 90 mM glucose in the presence as in the absence of respiration and inhibited by Antimycin A in the absence of exogenous carbon source. This uptake therefore requires fermentative or respiratory metabolic energy. 2. The calcium uptake by S. pombe exhibits saturation kinetics and high affinity for calcium. At external pH 4.5, the apparent Km is 45 muM ca2+ 400 muM of other divalent cations exert competitive inhibitions of calcium uptake in the following order of affinities: Sr2+ greater than Mn2+ greater than Co2+ greater than Mg2+. Inhibition by KCl is also observed but is of non-competitive type and requires high concentrations of the order of 40 mM. 3. At 30 degrees C, the uptake rate of calcium is about 10-times higher at pH 8925 than at pH 4.0. An extrusion of 45Ca2+, the rate of which is estimated to be lower than one-fifth of the uptake, is observed in the presence of glucose when the external pH is acid. 4. At external pH 4.5, low concentrations of lanthanum chloride, ruthenium red and hexamine cobaltichloride are inhibitory for the uptake of calcium by the yeast cells. 5. In presence of Antimycin A, the uncouplers: NaN3, dinitrophenol, and concentrations of crobonylcyanide m-chlorophenylhydrazone higher than 80 muM inhibit the calcium uptake by glycolysing cells. In the presence of glucose, the K+ ionophore Dio-9 dnhances severalfold the uptake of calcium even at 2 degrees C. 6. It is concluded that S. pombe possess an active transport system for low concentrations of calcium. This transport seems to be dependent on an electric potential (negative inside) across the cellular membrane.","authors":"Boutry M, Foury F, Goffeau A","authors_abbrev":"Boutry M et al.","pubmed_publication_date":"04 Feb 1977","pubmed_entrez_date":"1977-02-04","publication_year":"1977","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9125132","title":"Role of the fission yeast nim 1 protein kinase in the cell cycle response to nutritional signals.","citation":"Biochem Biophys Res Commun 1997 Mar 06;232(1):204-8","abstract":"The fission yeast cdr1/nim1 protein kinase phosphorylates and inactivates the weel cdc2-inhibitory kinase. We have investigated the role played by cdr1/nim1 in the connection between nutritional signals and the cell cycle machinery. We show that loss of nim1 activity impairs the appropriate cellular adaptation to nutritional changes. However, the reduction in cell size at division in response to nitrogen starvation is independent of nim1. Moreover, we report that nim1 is an unstable protein that is rapidly degraded upon starvation, through a mechanism that is dependent upon protein synthesis. We propose that nim1, as a constitutive indirect activator of cdc2 at mitosis, favors the cellular response to starvation but does not actively participate in it. On the contrary, upon nitrogen starvation nim1 must be actively destroyed to protect the cells from a commitment into the cell cycle under unfavourable growth conditions.","authors":"Belenguer P, Pelloquin L, Oustrin ML, Ducommun B","authors_abbrev":"Belenguer P et al.","pubmed_publication_date":"06 Mar 1997","pubmed_entrez_date":"1997-03-06","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38376816","title":"PomBase: a Global Core Biodata Resource-growth, collaboration, and sustainability.","citation":"Genetics 2024 Feb 20;","abstract":"PomBase (https://www.pombase.org), the model organism database (MOD) for fission yeast, was recently awarded Global Core Biodata Resource (GCBR) status by the Global Biodata Coalition (GBC; https://globalbiodata.org/) after a rigorous selection process. In this MOD review, we present PomBase's continuing growth and improvement over the last 2 years. We describe these improvements in the context of the qualitative GCBR indicators related to scientific quality, comprehensivity, accelerating science, user stories, and collaborations with other biodata resources. This review also showcases the depth of existing connections both within the biocuration ecosystem and between PomBase and its user community.","doi":"10.1093/genetics/iyae007","authors":"Rutherford KM, Lera-Ramírez M, Wood V","authors_abbrev":"Rutherford KM et al.","pubmed_publication_date":"20 Feb 2024","pubmed_entrez_date":"2024-02-20","publication_year":"2024","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2024-02-21 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9471999","title":"Oscillatory nuclear movement in fission yeast meiotic prophase is driven by astral microtubules, as revealed by continuous observation of chromosomes and microtubules in living cells.","citation":"J Cell Sci 1998 Mar;111 ( Pt 6):701-12","abstract":"Using a computerized fluorescence microscope system to observe fluorescently stained cellular structures in vivo, we have examined the dynamics of chromosomes and microtubules during the process of meiosis in the fission yeast Schizosaccharomyces pombe. Fission yeast meiotic prophase is characterized by a distinctive type of nuclear movement that is led by telomeres clustered at the spindle-pole body (the centrosome-equivalent structure in fungi): the nucleus oscillates back and forth along the cell axis, moving continuously between the two ends of the cell for some hours prior to the meiotic divisions. To obtain a dynamic view of this oscillatory nuclear movement in meiotic prophase, we visualized microtubules and chromosomes in living cells using jellyfish green fluorescent protein fused with alpha-tubulin and a DNA-specific fluorescent dye, Hoechst 33342, respectively. Continuous observation of chromosomes and microtubules in these cells demonstrated that the oscillatory nuclear movement is mediated by dynamic reorganization of astral microtubules originating from the spindle-pole body. During each half-oscillatory period, the microtubules extending rearward from the leading edge of the nucleus elongate to drive the nucleus to one end of the cell. When the nucleus reversed direction, its motion during the second half of the oscillation was not driven by the same microtubules that drove its motion during the first half, but rather by newly assembled microtubules. Reversible inhibition of nuclear movement by an inhibitor of microtubule polymerization, thiabendazole, confirmed the involvement of astral microtubules in oscillatory nuclear movement. The speed of the movement fluctuated within a range 0 to 15 micron/minute, with an average of about 5 microm/minute. We propose a model in which the oscillatory nuclear movement is mediated by dynamic instability and selective stabilization of astral microtubules.","authors":"Ding DQ, Chikashige Y, Haraguchi T, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"Mar 1998","pubmed_entrez_date":"1998-05-12","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16207082","title":"Psc3 cohesin of Schizosaccharomyces pombe: cell cycle analysis and identification of three distinct isoforms.","citation":"Biol Chem 2005 Jul;386(7):613-21","abstract":"Cohesins are a group of proteins that function to mediate correct chromosome segregation, DNA repair and meiotic recombination. This report presents the amino acid sequence for the Schizosaccharomyces pombe cohesin Psc3 based on the translation of the cDNA sequence, showing that the protein is smaller than previously predicted. Interestingly, comparison of the amino acid and DNA coding sequences of Psc3 with fission yeast Rec11 meiotic region-specific recombination activator shows that both intron positioning within the genes and the amino-terminal half of the two proteins are highly conserved. We demonstrate that although the intergenic region upstream of the psc3+ start codon contains a consensus sequence for the cell-cycle regulatory MluI cell-cycle box, psc3+ transcription is not differentially regulated during the mitotic cell cycle. Finally, we demonstrate that an epitope-tagged version of Psc3 undergoes no major changes during the mitotic cell cycle. However, instead we identify at least three distinct isoforms of Psc3, suggesting that post-translational modification of Psc3 contributes to the regulation of cohesion function.","authors":"Ilyushik E, Pryce DW, Walerych D, Riddell T, Wakeman JA, McInerny CJ, McFarlane RJ","authors_abbrev":"Ilyushik E et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-10-07","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.20"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12589463","title":"Pre-mRNA splicing in Schizosaccharomyces pombe: regulatory role of a kinase conserved from fission yeast to mammals.","citation":"Curr Genet 2003 Feb;42(5):241-51","abstract":"Most primary messenger RNA transcripts (pre-mRNAs) in eukaryotes contain intervening sequences that must be precisely removed to generate a functional mRNA. The excision of the intervening sequences, the introns, from a pre-mRNA and the concomitant joining of the flanking sequences, the exons, is called pre-mRNA splicing. Pre-mRNA splicing takes place in large ribonucleoprotein machinery, the spliceosome. Although the function and components of this machinery appear to be highly conserved between organisms, many distinct differences between budding yeast, Saccharomyces cerevisiae, and fission yeast, Schizosaccharomyces pombe, have been found, emphasizing their evolutionary distance. Most interestingly, fission yeast appears to reflect the more conservative evolutionary development regarding pre-mRNA splicing. Many spliceosomal components, including the five small nuclear RNAs, which most likely form the catalytic core of the spliceosome, show a higher degree of similarity with the components of the splicing machinery found in mammals. In addition, several regulatory components of the spliceosome detected in mammals are absent in Sac. cerevisiae, but present in Sch. pombe. Here, we review recent progress made in our understanding of the control of pre-mRNA splicing in Sch. pombe. The focus is on Prp4p kinase, first discovered in fission yeast and also present in mammals, but absent in Sac. cerevisiae. Results from both mammals and Sch. pombe suggest that Prp4p plays a key role in regulating pre-mRNA splicing and in connecting this process with the cell cycle.","authors":"Kuhn AN, Käufer NF","authors_abbrev":"Kuhn AN et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-02-18","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26857675","title":"The informational architecture of the cell.","citation":"Philos Trans A Math Phys Eng Sci 2016 Mar 13;374(2063)","abstract":"We compare the informational architecture of biological and random networks to identify informational features that may distinguish biological networks from random. The study presented here focuses on the Boolean network model for regulation of the cell cycle of the fission yeast Schizosaccharomyces pombe. We compare calculated values of local and global information measures for the fission yeast cell cycle to the same measures as applied to two different classes of random networks: Erdös-Rényi and scale-free. We report patterns in local information processing and storage that do indeed distinguish biological from random, associated with control nodes that regulate the function of the fission yeast cell-cycle network. Conversely, we find that integrated information, which serves as a global measure of 'emergent' information processing, does not differ from random for the case presented. We discuss implications for our understanding of the informational architecture of the fission yeast cell-cycle network in particular, and more generally for illuminating any distinctive physics that may be operative in life.","doi":"10.1098/rsta.2015.0057","authors":"Walker SI, Kim H, Davies PC","authors_abbrev":"Walker SI et al.","pubmed_publication_date":"13 Mar 2016","pubmed_entrez_date":"2016-02-10","publication_year":"2016","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2016-02-11 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22319459","title":"Raf1 Is a DCAF for the Rik1 DDB1-like protein and has separable roles in siRNA generation and chromatin modification.","citation":"PLoS Genet 2012 Feb;8(2):e1002499","abstract":"Non-coding transcription can trigger histone post-translational modifications forming specialized chromatin. In fission yeast, heterochromatin formation requires RNAi and the histone H3K9 methyltransferase complex CLRC, composed of Clr4, Raf1, Raf2, Cul4, and Rik1. CLRC mediates H3K9 methylation and siRNA production; it also displays E3-ubiquitin ligase activity in vitro. DCAFs act as substrate receptors for E3 ligases and may couple ubiquitination with histone methylation. Here, structural alignment and mutation of signature WDxR motifs in Raf1 indicate that it is a DCAF for CLRC. We demonstrate that Raf1 promotes H3K9 methylation and siRNA amplification via two distinct, separable functions. The association of the DCAF Raf1 with Cul4-Rik1 is critical for H3K9 methylation, but dispensable for processing of centromeric transcripts into siRNAs. Thus the association of a DCAF, Raf1, with its adaptor, Rik1, is required for histone methylation and to allow RNAi to signal to chromatin.","doi":"10.1371/journal.pgen.1002499","authors":"Buscaino A, White SA, Houston DR, Lejeune E, Simmer F, de Lima Alves F, Diyora PT, Urano T, Bayne EH, Rappsilber J, Allshire RC","authors_abbrev":"Buscaino A et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2012-02-10","publication_year":"2012","canto_session_key":"b00c58b9eabd7812","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC11E10.08","SPBC428.08c","SPCC613.12c","SPCC970.07c","SPBP8B7.28c","SPCC188.13c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:32720681","title":"Transcriptional interference at tandem lncRNA and protein-coding genes: an emerging theme in regulation of cellular nutrient homeostasis.","citation":"Nucleic Acids Res 2020 Sep 04;48(15):8243-8254","abstract":"Tandem transcription interference occurs when the act of transcription from an upstream promoter suppresses utilization of a co-oriented downstream promoter. Because eukaryal genomes are liberally interspersed with transcription units specifying long non-coding (lnc) RNAs, there are many opportunities for lncRNA synthesis to negatively affect a neighboring protein-coding gene. Here, I review two eukaryal systems in which lncRNA interference with mRNA expression underlies a regulated biological response to nutrient availability. Budding yeast SER3 is repressed under serine-replete conditions by transcription of an upstream SRG1 lncRNA that traverses the SER3 promoter and elicits occlusive nucleosome rearrangements. SER3 is de-repressed by serine withdrawal, which leads to shut-off of SRG1 synthesis. The fission yeast phosphate homeostasis (PHO) regulon comprises three phosphate acquisition genes - pho1, pho84, and tgp1 - that are repressed under phosphate-replete conditions by 5' flanking lncRNAs prt, prt2, and nc-tgp1, respectively. lncRNA transcription across the PHO mRNA promoters displaces activating transcription factor Pho7. PHO mRNAs are transcribed during phosphate starvation when lncRNA synthesis abates. The PHO regulon is de-repressed in phosphate-replete cells by genetic manipulations that favor 'precocious' lncRNA 3'-processing/termination upstream of the mRNA promoters. PHO lncRNA termination is governed by the Pol2 CTD code and is subject to metabolite control by inositol pyrophosphates.","doi":"10.1093/nar/gkaa630","authors":"Shuman S","authors_abbrev":"Shuman S","pubmed_publication_date":"04 Sep 2020","pubmed_entrez_date":"2020-07-29","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-07-30 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24862735","title":"In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery.","citation":"Angew Chem Int Ed Engl 2014 Jul 07;53(28):7354-9","abstract":"In eukaryotic cells, components of the 5' to 3' mRNA degradation machinery can undergo a rapid phase transition. The resulting cytoplasmic foci are referred to as processing bodies (P-bodies). The molecular details of the self-aggregation process are, however, largely undetermined. Herein, we use a bottom-up approach that combines NMR spectroscopy, isothermal titration calorimetry, X-ray crystallography, and fluorescence microscopy to probe if mRNA degradation factors can undergo phase transitions in vitro. We show that the Schizosaccharomyces pombe Dcp2 mRNA decapping enzyme, its prime activator Dcp1, and the scaffolding proteins Edc3 and Pdc1 are sufficient to reconstitute a phase-separation process. Intermolecular interactions between the Edc3 LSm domain and at least 10 helical leucine-rich motifs in Dcp2 and Pdc1 build the core of the interaction network. We show that blocking of these interactions interferes with the clustering behavior, both in vitro and in vivo.","doi":"10.1002/anie.201402885","authors":"Fromm SA, Kamenz J, Nöldeke ER, Neu A, Zocher G, Sprangers R","authors_abbrev":"Fromm SA et al.","pubmed_publication_date":"07 Jul 2014","pubmed_entrez_date":"2014-05-28","publication_year":"2014","canto_session_key":"77b0eb6fc0d96d2f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-19 07:28:49","canto_approved_date":"2023-02-19 07:28:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-19 07:28:30","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19A8.12","SPBC18E5.11c","SPAC20G4.08"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-02-19","pdb_entries":[{"pdb_id":"4q2s","gene_chains":[{"gene_uniquename":"SPAC20G4.08","chain":"A","position":"932-1070"}],"title":"Crystal Structure of S. pombe Pdc1 Ge1 Domain","entry_authors":"Noeldeke ER,Neu A,Zocher G,Sprangers R","entry_authors_abbrev":"Noeldeke ER et al.","reference_uniquename":"PMID:24862735","experimental_method":"X-ray","resolution":"1.35"}]},{"uniquename":"PMID:12058071","title":"The G1/S cyclin Cig2p during meiosis in fission yeast.","citation":"Mol Biol Cell 2002 Jun;13(6):2080-90","abstract":"Cyclin-dependent kinases (CDKs) are important for both mitotic and meiotic cell cycles. In fission yeast, the major CDK, Cdc2p is involved in premeiotic DNA replication and in meiosis II. One of its partners, the mitotic cyclin Cdc13p is known to be required for meiosis, whereas there are no studies on the G1/S cyclin Cig2p. In this article, we have studied the regulation of the Cdc2p/Cdc13p and Cdc2p/Cig2p complexes during synchronous meiosis. We observed that Cdc2p/Cig2p kinase is activated in an unexpected biphasic manner, first at onset of premeiotic S phase and again during meiotic nuclear divisions. The role of Cig2p during meiosis was investigated using cig2-deleted strains that exhibit delays in onset of both S phase and meiotic divisions as well as an inefficient completion of MII. Furthermore, analysis of cig2 transcripts revealed a meiosis-specific regulation of cig2 expression during MI/MII dependent upon the Mei4p transcription factor leading to a different transcription start site at this stage of meiosis.","authors":"Borgne A, Murakami H, Ayté J, Nurse P","authors_abbrev":"Borgne A et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-06-12","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10224084","title":"A fission yeast gene for mitochondrial sulfide oxidation.","citation":"J Biol Chem 1999 May 07;274(19):13250-7","abstract":"A cadmium-hypersensitive mutant of the fission yeast Schizosaccharomyces pombe was found to accumulate abnormally high levels of sulfide. The gene required for normal regulation of sulfide levels, hmt2(+), was cloned by complementation of the cadmium-hypersensitive phenotype of the mutant. Cell fractionation and immunocytochemistry indicated that HMT2 protein is localized to mitochondria. Sequence analysis revealed homology between HMT2 and sulfide dehydrogenases from photosynthetic bacteria. HMT2 protein, produced in and purified from Escherichia coli, was soluble, bound FAD, and catalyzed the reduction of quinone (coenzyme Q2) by sulfide. HMT2 activity was also detected in isolated fission yeast mitochondria. We propose that HMT2 functions as a sulfide:quinone oxidoreductase. Homologous enzymes may be widespread in higher organisms, as sulfide-oxidizing activities have been described previously in animal mitochondria, and genes of unknown function, but with similarity to hmt2(+), are present in the genomes of flies, worms, rats, mice, and humans.","authors":"Vande Weghe JG, Ow DW","authors_abbrev":"Vande Weghe JG et al.","pubmed_publication_date":"07 May 1999","pubmed_entrez_date":"1999-05-01","publication_year":"1999","canto_session_key":"169c0f8873eee853","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-21 14:07:35","canto_approved_date":"2023-03-15 17:29:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-24 16:19:03","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC10F6.01c","SPBC2G5.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-10-21"},{"uniquename":"PMID:32991693","title":"Amino Acids Whose Intracellular Levels Change Most During Aging Alter Chronological Life Span of Fission Yeast.","citation":"J Gerontol A Biol Sci Med Sci 2021 Jan 18;76(2):205-210","abstract":"Amino acid deprivation or supplementation can affect cellular and organismal life span, but we know little about the role of concentration changes in free, intracellular amino acids during aging. Here, we determine free amino acid levels during chronological aging of nondividing fission yeast cells. We compare wild-type with long-lived mutant cells that lack the Pka1 protein of the protein kinase A signalling pathway. In wild-type cells, total amino acid levels decrease during aging, but much less so in pka1 mutants. Two amino acids strongly change as a function of age: glutamine decreases, especially in wild-type cells, while aspartate increases, especially in pka1 mutants. Supplementation of glutamine is sufficient to extend the chronological life span of wild-type but not of pka1Δ cells. Supplementation of aspartate, on the other hand, shortens the life span of pka1Δ but not of wild-type cells. Our results raise the possibility that certain amino acids are biomarkers of aging, and their concentrations during aging can promote or limit cellular life span.","doi":"10.1093/gerona/glaa246","authors":"Rallis C, Mülleder M, Smith G, Au YZ, Ralser M, Bähler J","authors_abbrev":"Rallis C et al.","pubmed_publication_date":"18 Jan 2021","pubmed_entrez_date":"2020-09-29","publication_year":"2021","canto_session_key":"d4459ffecf00da08","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-10-01 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38780300","title":"Nitrogen availability is important for preventing catastrophic mitosis in fission yeast.","citation":"J Cell Sci 2024 May 23;","abstract":"Mitosis is a critical stage in the cell cycle, controlled by a vast network of regulators responding to multiple internal and external factors. The fission yeast Schizosaccharomyces pombe may demonstrate catastrophic mitotic phenotypes due to mutations or drug treatments. One of the factors provoking catastrophic mitosis is a disturbed lipid metabolism, resulting from e.g. mutations in acetyl-CoA/biotin carboxylase (cut6), in fatty acid synthase (fas2/lsd1), or in the transcriptional regulator of lipid metabolism (cbf11) genes, as well as treatment with inhibitors of fatty acid synthesis. It was previously shown that mitotic fidelity in lipid metabolism mutants can be partially rescued by ammonium chloride. In this study we demonstrate that mitotic fidelity can be improved by multiple nitrogen sources. Moreover, this improvement is not limited to lipid metabolism disturbances but also applies to a number of unrelated mitotic mutants. Interestingly, the partial rescue is not achieved by restoring the lipid metabolism state, but rather indirectly. Our results highlight a novel role for nitrogen availability in mitotic fidelity.","doi":"10.1242/jcs.262196","authors":"Zemlianski V, Marešová A, Princová J, Holič R, Häsler R, Ramos Del Río MJ, Lhoste L, Zarechyntsava M, Převorovský M","authors_abbrev":"Zemlianski V et al.","pubmed_publication_date":"23 May 2024","pubmed_entrez_date":"2024-05-23","publication_year":"2024","canto_session_key":"13e26365fef6c9cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Viacheslav Zemlianski","canto_first_approved_date":"2024-09-19 13:00:53","canto_approved_date":"2024-09-19 13:00:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-09-07 19:31:36","canto_added_date":"2024-05-23 23:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":107,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Viacheslav Zemlianski","community_curator":true,"annotation_count":44,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.04","SPAC10F6.09c","SPAC1786.01c","SPAC17C9.13c","SPBP4H10.11c","SPBC14C8.01c","SPAC4A8.11c","SPAC869.10c","SPAC926.09c","SPAC1039.09","SPBC30D10.10c","SPAC1B3.16c","SPCC736.08","SPCC962.03c","SPAC56E4.04c","SPAC22A12.06c","SPAC6F12.15c","SPCC74.03c","SPAC26H5.05","SPCC1450.16c","SPBC106.09","SPCC5E4.06","SPCC5E4.04","SPBC146.03c","SPCC1281.06c","SPBC359.03c","SPCC1235.02","SPBC18H10.02","SPBC216.07c","SPAP7G5.06"],"gene_count":30,"ltp_gene_count":27,"approved_date":"2024-09-19"},{"uniquename":"PMID:24465549","title":"A conserved non-canonical docking mechanism regulates the binding of dual specificity phosphatases to cell integrity mitogen-activated protein kinases (MAPKs) in budding and fission yeasts.","citation":"PLoS One 2014;9(1):e85390","abstract":"Dual-specificity MAPK phosphatases (MKPs) are essential for the negative regulation of MAPK pathways. Similar to other MAPK-interacting proteins, most MKPs bind MAPKs through specific docking domains known as D-motifs. However, we found that the Saccharomyces cerevisiae MKP Msg5 binds the MAPK Slt2 within the cell wall integrity (CWI) pathway through a distinct motif (IYT). Here, we demonstrate that the IYT motif mediates binding of the Msg5 paralogue Sdp1 to Slt2 as well as of the MKP Pmp1 to its CWI MAPK counterpart Pmk1 in the evolutionarily distant yeast Schizosaccharomyces pombe. As a consequence, removal of the IYT site in Msg5, Sdp1 and Pmp1 reduces MAPK trapping caused by the overexpression of catalytically inactive versions of these phosphatases. Accordingly, an intact IYT site is necessary for inactive Sdp1 to prevent nuclear accumulation of Slt2. We also show that both Ile and Tyr but not Thr are essential for the functionality of the IYT motif. These results provide mechanistic insight into MKP-MAPK interplay and stress the relevance of this conserved non-canonical docking site in the regulation of the CWI pathway in fungi.","doi":"10.1371/journal.pone.0085390","authors":"Sacristán-Reviriego A, Madrid M, Cansado J, Martín H, Molina M","authors_abbrev":"Sacristán-Reviriego A et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-01-28","publication_year":"2014","canto_session_key":"8294316f396aaa06","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1685.01","SPBC119.08"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:14730023","title":"The conserved RNA recognition motif 3 of U2 snRNA auxiliary factor (U2AF 65) is essential in vivo but dispensable for activity in vitro.","citation":"RNA 2004 Feb;10(2):240-53","abstract":"The general splicing factor U2AF(65) recognizes the polypyrimidine tract (Py tract) that precedes 3' splice sites and has three RNA recognition motifs (RRMs). The C-terminal RRM (RRM3), which is highly conserved, has been proposed to contribute to Py-tract binding and establish protein-protein contacts with splicing factors mBBP/SF1 and SAP155. Unexpectedly, we find that the human RRM3 domain is dispensable for U2AF(65) activity in vitro. However, it has an essential function in Schizosaccharomyces pombe distinct from binding to the Py tract or to mBBP/SF1 and SAP155. First, deletion of RRM3 from the human protein has no effect on Py-tract binding. Second, RRM123 and RRM12 select similar sequences from a random pool of RNA. Third, deletion of RRM3 has no effect on the splicing activity of U2AF(65) in vitro. However, deletion of the RRM3 domain of S. pombe U2AF(59) abolishes U2AF function in vivo. In addition, certain amino acid substitutions on the four-stranded beta-sheet surface of RRM3 compromise U2AF function in vivo without affecting binding to mBBP/SF1 or SAP155 in vitro. We propose that RRM3 has an unrecognized function that is possibly relevant for the splicing of only a subset of cellular introns. We discuss the implications of these observations on previous models of U2AF function.","authors":"Banerjee H, Rahn A, Gawande B, Guth S, Valcarcel J, Singh R","authors_abbrev":"Banerjee H et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2004-01-20","publication_year":"2004","canto_session_key":"ccebb5707c119ed6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-08-29 14:50:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-05 14:11:22","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.09c","SPBC146.07","SPCC962.06c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-08-05"},{"uniquename":"EMBL:AJ632008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.42"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18235244","title":"MAPK mediated cell cycle regulation is associated with Cdc25 turnover in S. pombe after exposure to genotoxic stress.","citation":"Cell Cycle 2008 Feb 01;7(3):365-72","abstract":"Genotoxic stress caused by carcinogens like cigarette smoke activate both the MAPK pathway and the S phase checkpoint in Schizosacchaomyces pombe. But the cross talk between these two pathways has not been investigated in great detail in fission yeast. This study deals with the molecular mechanism of co-ordination between the two regulatory pathways. We show that both the pathways have a common effector molecule, namely Cdc25, the cell cycle regulatory phosphatase. We demonstrate that the MAPK Sty1 interacts with Cdc25 and prevents mitotic entry in S.pombe cells exposed to CSE. To our knowledge, this is the first demonstration of interaction between Sty1 and Cdc25 in S. pombe. The functional significance of this interaction lies in effecting Cdc25 turnover after CSE exposure in S.pombe. We show that Cdc25 turnover after CSE treatment is dependent on the presence of Rad3 activity and Sty1-Cdc25 interaction. Our study suggests that the cigarette smoke extract (CSE) induced stress is counteracted by the simultaneous activation of a mitotic checkpoint in addition to the previously described S phase checkpoint. We also show that Sty1 activity is not essential for activation of the S phase checkpoint.","authors":"Sundaram G, Palchaudhuri S, Dixit S, Chattopadhyay D","authors_abbrev":"Sundaram G et al.","pubmed_publication_date":"01 Feb 2008","pubmed_entrez_date":"2008-02-01","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28334955","title":"The Schizosaccharomyces pombe PPR protein Ppr10 associates with a novel protein Mpa1 and acts as a mitochondrial translational activator.","citation":"Nucleic Acids Res 2017 Apr 07;45(6):3323-3340","abstract":"The pentatricopeptide repeat (PPR) proteins characterized by tandem repeats of a degenerate 35-amino-acid motif function in all aspects of organellar RNA metabolism, many of which are essential for organellar gene expression. In this study, we report the characterization of a fission yeast Schizosaccharomyces pombe PPR protein, Ppr10 and a novel Ppr10-associated protein, designated Mpa1. The ppr10 deletion mutant exhibits growth defects in respiratory media, and is dramatically impaired for viability during the late-stationary phase. Deletion of ppr10 affects the accumulation of specific mitochondrial mRNAs. Furthermore, deletion of ppr10 severely impairs mitochondrial protein synthesis, suggesting that Ppr10 plays a general role in mitochondrial protein synthesis. Ppr10 interacts with Mpa1 in vivo and in vitro and the two proteins colocalize in the mitochondrial matrix. The ppr10 and mpa1 deletion mutants exhibit very similar phenotypes. One of Mpa1's functions is to maintain the normal protein level of Ppr10 protein by protecting it from degradation by the mitochondrial matrix protease Lon1. Our findings suggest that Ppr10 functions as a general mitochondrial translational activator, likely through interaction with mitochondrial mRNAs and mitochondrial translation initiation factor Mti2, and that Ppr10 requires Mpa1 association for stability and function.","doi":"10.1093/nar/gkx127","authors":"Wang Y, Yan J, Zhang Q, Ma X, Zhang J, Su M, Wang X, Huang Y","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"07 Apr 2017","pubmed_entrez_date":"2017-03-24","publication_year":"2017","canto_session_key":"1769f7fc9f807232","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2018-04-02 21:34:55","canto_approved_date":"2025-09-04 06:30:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-30 08:15:55","canto_added_date":"2017-03-25 01:15:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":74,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMIT.01","SPMIT.04","SPMIT.10","SPAC22F3.06c","SPMIT.09","SPMIT.07","SPBC18H10.11c","SPMIT.05","SPAPB1E7.11c","SPMIT.08","SPBC106.19","SPCC11E10.04","SPBC1271.15c","SPMIT.11"],"gene_count":14,"ltp_gene_count":5,"approved_date":"2018-04-02"},{"uniquename":"EMBL:AU010970","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28515143","title":"Cyclin C influences the timing of mitosis in fission yeast.","citation":"Mol Biol Cell 2017 Jul 01;28(13):1738-1744","abstract":"The multiprotein Mediator complex is required for the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator contains the Cdk8 regulatory subcomplex, which directs periodic transcription and influences cell cycle progression in fission yeast. Here we investigate the role of CycC, the cognate cyclin partner of Cdk8, in cell cycle control. Previous reports suggested that CycC interacts with other cellular Cdks, but a fusion of CycC to Cdk8 reported here did not cause any obvious cell cycle phenotypes. We find that Cdk8 and CycC interactions are stabilized within the Mediator complex and the activity of Cdk8-CycC is regulated by other Mediator components. Analysis of a mutant yeast strain reveals that CycC, together with Cdk8, primarily affects M-phase progression but mutations that release Cdk8 from CycC control also affect timing of entry into S phase.","doi":"10.1091/mbc.E16-11-0787","authors":"Banyai G, Szilagyi Z, Baraznenok V, Khorosjutina O, Gustafsson CM","authors_abbrev":"Banyai G et al.","pubmed_publication_date":"01 Jul 2017","pubmed_entrez_date":"2017-05-19","publication_year":"2017","canto_session_key":"0947642294e6ecc0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-05-20 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC31F10.04c","SPBC14F5.08","SPAC5D6.05","SPAC17C9.05c","SPBC12D12.06","SPBC28F2.12","SPAC589.02c","SPAC23H4.17c","SPAC688.08"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:12243351","title":"Regulation of Schizosaccharomyces pombe gene encoding copper/zinc superoxide dismutase.","citation":"Mol Cells 2002 Aug 31;14(1):43-9","abstract":"Copper/zinc superoxide dismutase (Cu/Zn SOD) is an abundant enzyme that scavenges superoxide radicals. To independently examine the regulation of the Cu/Zn SOD gene of the fission yeast Schizosaccharomyces pombe, the 882 bp upstream region of the Cu/Zn SOD gene was fused into the promoterless beta-galactosidase gene of the shuttle vector YEp357R, which generated the fusion plasmid pSC601. Cupric chloride (4.5 microM), aluminum chloride (10 mM), cadmium chloride (30 microM, 50 microM), mercuric chloride (1 microM), zinc chloride (11 mM), and hydrogen peroxide (0.3 mM) enhanced the synthesis of beta-galactosidase from the fusion plasmid. These results indicate that the expression of the S. pombe Cu/Zn SOD gene is, therefore, regulated by various metal ions, however superoxide-generating menadione did not affect the expression of the S. pombe Cu/Zn SOD gene. The expression of the S. pombe Cu/Zn SOD gene is also regulated by the transcription factor Pap1.","authors":"Lee YY, Jung HI, Park EH, Sa JH, Lim CJ","authors_abbrev":"Lee YY et al.","pubmed_publication_date":"31 Aug 2002","pubmed_entrez_date":"2002-09-24","publication_year":"2002","canto_session_key":"5794c9a15ec2623e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-20 13:14:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-20 13:14:02","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC821.10c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-11-20"},{"uniquename":"EMBL:SPD237","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14506866","title":"Amino acid substitution of the largest subunit of yeast RNA polymerase II: effect of a temperature-sensitive mutation related to G1 cell cycle arrest.","citation":"Curr Microbiol 2003 Aug;47(2):159-62","abstract":"A mammalian temperature-sensitive mutant tsAF8 shows cell cycle arrest at nonpermissive temperatures in mid-G1 phase. DNA sequence comparison of the largest subunit of RNA polymerase II (Rpb1) from the wild-type and the mutant shows that the mutant phenotype results from a (hemizygous) C-to-A variation at nucleotide 944 in one rpb1 allele, giving rise to an Ala-to-Asp substitution at residue 315 in the protein. This amino acid substitution was introduced into the Schizosaccharomyces pombe rpb1 gene. Whereas tsAF8 cells showed growth defects and altered Rpb1 distribution at nonpermissive temperatures, yeast cells harboring this amino acid substitution did not show apparent temperature sensitivity. The effect of another temperature-sensitive Rpb1 mutation was also small. These results suggest that mutation of the rpb1 gene, which is critical in mammalian cells, may not be deleterious in yeast cells.","authors":"Sugaya K","authors_abbrev":"Sugaya K","pubmed_publication_date":"Aug 2003","pubmed_entrez_date":"2003-09-26","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12478386","title":"Prospects for functional genomics in Schizosaccharomyces pombe.","citation":"Curr Genet 2002 Nov;42(2):73-84","abstract":"Schizosaccharomyces pombe is well established as an experimental organism for basic research, with well developed technologies for molecular biology, genetics and cell biology. Its full genome sequence has recently been published. Here, the prerequisites for functional genomics studies in Sch. pombe are examined and compared with those of some established prominent functional genomics model organisms, especially Saccharomyces cerevisiae. It is argued that functional genomics studies in certain areas of cellular and molecular biology could potentially be more efficiently performed in Sch. pombe than in most other experimental organisms.","authors":"Sunnerhagen P","authors_abbrev":"Sunnerhagen P","pubmed_publication_date":"Nov 2002","pubmed_entrez_date":"2002-12-13","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22976295","title":"Psk1, an AGC kinase family member in fission yeast, is directly phosphorylated and controlled by TORC1 and functions as S6 kinase.","citation":"J Cell Sci 2012 Dec 01;125(Pt 23):5840-9","abstract":"Target of rapamycin (TOR), an evolutionarily conserved serine/threonine protein kinase, plays pivotal roles in several important cellular processes in eukaryotes. In the fission yeast Schizosaccharomyces pombe, TOR complex 1 (TORC1), which includes Tor2 as a catalytic subunit, manages the switch between cell proliferation and differentiation by sensing nutrient availability. However, little is known about the direct target of TORC1 that plays key roles in nutrient-dependent TORC1 signaling in fission yeast. Here we report that in fission yeast, three AGC kinase family members, named Psk1, Sck1 and Sck2, which exhibit high homology with human S6K1, are phosphorylated under nutrient-rich conditions and are dephosphorylated by starvation conditions. Among these, Psk1 is necessary for phosphorylation of ribosomal protein S6. Furthermore, Psk1 phosphorylation is regulated by TORC1 in nutrient-dependent and rapamycin-sensitive manners in vivo. Three conserved regulatory motifs (the activation loop, the hydrophobic and the turn motifs) in Psk1 are phosphorylated and these modifications are required for Psk1 activity. In particular, phosphorylation of the hydrophobic motif is catalyzed by TORC1 in vivo and in vitro. Ksg1, a homolog of PDK1, is also important for Psk1 phosphorylation in the activation loop and for its activity. The TORC1 components Pop3, Toc1 and Tco89, are dispensable for Psk1 regulation, but disruption of pop3(+) causes an increase in the sensitivity of TORC1 to rapamycin. Taken together, these results provide convincing evidence that TORC1/Psk1/Rps6 constitutes a nutrient-dependent signaling pathway in fission yeast.","doi":"10.1242/jcs.111146","authors":"Nakashima A, Otsubo Y, Yamashita A, Sato T, Yamamoto M, Tamanoi F","authors_abbrev":"Nakashima A et al.","pubmed_publication_date":"01 Dec 2012","pubmed_entrez_date":"2012-09-15","publication_year":"2012","canto_session_key":"f07cd572b2d0adcf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-04 16:28:05","canto_approved_date":"2025-09-03 20:54:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-29 17:52:03","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":88,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP18G5.03","SPAC13G6.07c","SPBC106.10","SPAC22E12.14c","SPAC630.13c","SPCC162.12","SPCC4G3.08","SPCC576.15c","SPAPB1E7.12","SPCC24B10.07","SPAC1B9.02c","SPBC21B10.05c","SPBC216.07c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2018-10-04"},{"uniquename":"PMID:20679485","title":"BRCT domain interactions with phospho-histone H2A target Crb2 to chromatin at double-strand breaks and maintain the DNA damage checkpoint.","citation":"Mol Cell Biol 2010 Oct;30(19):4732-43","abstract":"Relocalization of checkpoint proteins to chromatin flanking DNA double-strand breaks (DSBs) is critical for cellular responses to DNA damage. Schizosaccharomyces pombe Crb2, which mediates Chk1 activation by Rad3(ATR), forms ionizing radiation-induced nuclear foci (IRIF). Crb2 C-terminal BRCT domains (BRCT(2)) bind histone H2A phosphorylated at a C-terminal SQ motif by Tel1(ATM) and Rad3(ATR), although the functional significance of this interaction is controversial. Here, we show that polar interactions of Crb2 serine-548 and lysine-619 with the phosphate group of phospho-H2A (γ-H2A) are critical for Crb2 IRIF formation and checkpoint function. Mutations of these BRCT(2) domain residues have additive effects when combined in a single allele. Combining either mutation with an allele that eliminates the threonine-215 cyclin-dependent kinase phosphorylation site completely abrogates Crb2 IRIF and function. We propose that cooperative phosphate interactions in the BRCT(2) γ-H2A-binding pocket of Crb2, coupled with tudor domain interactions with lysine-20 dimethylation of histone H4, facilitate stable recruitment of Crb2 to chromatin surrounding DSBs, which in turn mediates efficient phosphorylation of Chk1 that is required for a sustained checkpoint response. This mechanism of cooperative interactions with the γ-H2A/X phosphate is likely conserved in S. pombe Brc1 and human Mdc1 genome maintenance proteins.","doi":"10.1128/MCB.00413-10","authors":"Sofueva S, Du LL, Limbo O, Williams JS, Russell P","authors_abbrev":"Sofueva S et al.","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2010-08-04","publication_year":"2010","canto_session_key":"288cc0705ff9b896","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2018-09-19 10:54:09","canto_approved_date":"2026-02-17 15:32:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-16 09:28:50","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":66,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.06c","SPAC30D11.10","SPBC342.05","SPCC622.08c","SPCC1259.13","SPBC582.05c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-09-19"},{"uniquename":"PMID:30236788","title":"Cmk2 kinase is essential for survival in arsenite by modulating translation together with RACK1 orthologue Cpc2 in Schizosaccharomyces pombe.","citation":"Free Radic Biol Med 2018 Dec;129:116-126","abstract":"Different studies have demonstrated multiple effects of arsenite on human physiology. However, there are many open questions concerning the mechanism of response to arsenite. Schizosaccharomyces pombe activates the Sty1 MAPK pathway as a common response to several stress conditions. The specificity of the response is due to the activation of different transcription factors and specific targets such the Cmk2 MAPKAP kinase. We have previously shown that Cmk2 is phosphorylated and activated by the MAPK Sty1 in response to oxidative stress. Here, we report that Cmk2 kinase is specifically necessary to overcome the stress caused by metalloid agents, in particular arsenite. Deletion of cmk2 increases the protein level of various components of the MAPK pathway. Moreover, Cmk2 negatively regulates translation through the Cpc2 kinase: the RACK1 orthologue in fission yeast. RACK1 is a receptor for activated C-kinase. Interestingly, RACK1 is a constituent of the eukaryotic ribosome specifically localized in the head region of the 40 S subunit. Cmk2 controls arsenite response through Cpc2 and it does so through Cpc2 ribosomal function, as observed in genetic analysis using a Cpc2 mutant unable to bind to ribosome. These findings suggest a role for Cmk2 in regulating translation and facilitating adaptation to arsenite stress in the ribosome.","doi":"10.1016/j.freeradbiomed.2018.09.024","authors":"Sanchez-Marinas M, Gimenez-Zaragoza D, Martin-Ramos E, Llanes J, Cansado J, Pujol MJ, Bachs O, Aligue R","authors_abbrev":"Sanchez-Marinas M et al.","pubmed_publication_date":"Dec 2018","pubmed_entrez_date":"2018-09-22","publication_year":"2018","canto_session_key":"c3ed213cd628a007","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-09-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6B12.15","SPAC222.07c","SPAC24B11.06c","SPAC23A1.06c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:7909513","title":"A B-type cyclin negatively regulates conjugation via interacting with cell cycle 'start' genes in fission yeast.","citation":"EMBO J 1994 Apr 15;13(8):1863-72","abstract":"In the fission yeast Schizosaccharomyces pombe, the cdc10+/SWI family members constitute the cell cycle 'start' genes. res1+ and res2+ are the newly identified members of this family and encode putative association partners of the Cdc10 protein. The Pat1 kinase plays a pivotal role in switching between vegetative growth and sexual development, and its inactivation in haploid cells induces unconditional growth arrest and subsequent meiosis. We have identified as an extragenic suppressor of a temperature sensitive pat1-114 mutant, a new B-type cyclin that negatively regulates conjugation by interacting with these 'start' genes. This cyclin, named Cyc17, is highly homologous with Cdc13, but has no detectable activity as a mitotic cyclin. Deletion of cyc17+ markedly enhances conjugation, despite the presence of nitrogen source, and accelerates growth arrest in G1 upon nitrogen starvation. Conversely, overexpression of the cyc17+ gene strongly inhibits conjugation. The cyc17+ gene is transcribed into 3.2 kb poly(A)+ and 3.0 kb poly(A)- RNAs. Only the poly(A)+ species is expressed during vegetative growth and periodically with a peak in the G1 and S phases of the cell cycle. On the other hand, the poly(A)- transcript is highly induced during conjugation. This induction is lost in res2- cells, whereas the poly(A)+ transcript is significantly reduced in res1- cells. However, the mating inhibition as well as the ability to rescue the pat1 mutation by overexpression of res1+ and res2+ are totally abolished in cyc17- cells. Thus, in S.pombe, a B-type cyclin, regulated by the newly identified cell cycle 'start' genes, plays a crucial role in the control of sexual development.","authors":"Obara-Ishihara T, Okayama H","authors_abbrev":"Obara-Ishihara T et al.","pubmed_publication_date":"15 Apr 1994","pubmed_entrez_date":"1994-04-15","publication_year":"1994","canto_session_key":"e583692a60c79c22","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-07-28 14:15:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-14 10:07:07","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC11B10.09","SPBC725.16","SPBC336.12c","SPAC22F3.09c","SPAPB2B4.03","SPBC19C2.05","SPBC19F5.01c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2014-07-14"},{"uniquename":"PMID:15590667","title":"Two steps in Maf1-dependent repression of transcription by RNA polymerase III.","citation":"J Biol Chem 2005 Feb 25;280(8):6455-62","abstract":"In Saccharomyces cerevisiae, Maf1 is essential for mediating the repression of transcription by RNA polymerase (pol) III in response to diverse cellular conditions. These conditions activate distinct signaling pathways that converge at or above Maf1. Thus, Maf1-dependent repression is thought to involve a common set of downstream inhibitory effects on the pol III machinery. Here we provide support for this view and define two steps in Maf1-dependent transcriptional repression. We show that chlorpromazine (CPZ)-induced repression of pol III transcription is achieved by inhibiting de novo assembly of transcription factor (TF) IIIB onto DNA as well as the recruitment of pol III to preassembled TFIIIB.DNA complexes. Additionally Brf1 was identified as a target of repression in extracts of CPZ-treated cells. Maf1-Brf1 and Maf1-pol III interactions were implicated in the inhibition of TFIIIB.DNA complex assembly and polymerase recruitment by recombinant Maf1. Co-immunoprecipitation experiments confirmed these interactions in yeast extracts and demonstrated that Maf1 does not differentially sequester Brf1 or pol III under repressing conditions. The results suggest that Maf1 functions by a non-stoichiometric mechanism to repress pol III transcription.","authors":"Desai N, Lee J, Upadhya R, Chu Y, Moir RD, Willis IM","authors_abbrev":"Desai N et al.","pubmed_publication_date":"25 Feb 2005","pubmed_entrez_date":"2004-12-14","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31G5.12c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:14731600","title":"Cold fission: splitting the pombe cell at room temperature.","citation":"Trends Cell Biol 1994 Mar;4(3):96-101","abstract":"The mechanisms responsible for cytokinesis and its coordination with other events of the cell cycle are poorly understood. Genetic studies of cytokinesis in fission yeast are one useful approach to this problem. A number of conditional mutants of fission yeast that show defects in the formation of the septum of cytokinesis have been identified. Cloning of the genes affected in these mutants has begun to shed light upon the elements required to direct the construction of the division septum and also upon how the initiation of septum formation may be coordinated with mitosis.","authors":"Fankhauser C, Simanis V","authors_abbrev":"Fankhauser C et al.","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22184112","title":"Histone H3 lysine 14 acetylation is required for activation of a DNA damage checkpoint in fission yeast.","citation":"J Biol Chem 2012 Feb 03;287(6):4386-93","abstract":"Histone lysine acetylation has emerged as a key regulator of genome organization. However, with a few exceptions, the contribution of each acetylated lysine to cellular functions is not well understood because of the limited specificity of most histone acetyltransferases and histone deacetylases. Here we show that the Mst2 complex in Schizosaccharomyces pombe is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with Gcn5 to regulate global levels of H3K14 acetylation (H3K14ac). By analyzing the effect of H3K14ac loss through both enzymatic inactivation and histone mutations, we found that H3K14ac is critical for DNA damage checkpoint activation by directly regulating the compaction of chromatin and by recruiting chromatin remodeling protein complex RSC.","doi":"10.1074/jbc.M111.329417","authors":"Wang Y, Kallgren SP, Reddy BD, Kuntz K, López-Maury L, Thompson J, Watt S, Ma C, Hou H, Shi Y, Yates JR, Bähler J, O'Connell MJ, Jia S","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"03 Feb 2012","pubmed_entrez_date":"2011-12-21","publication_year":"2012","canto_session_key":"0ce3225c0996b774","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.05","SPBC16G5.13","SPBC17D11.04c","SPAC17G8.13c","SPAC1834.04","SPAC823.14","SPAC23D3.01","SPAC22H12.02","SPBC1734.15","SPBC8D2.04","SPAC1250.01","SPBC1105.11c","SPAC6F6.09"],"gene_count":13,"ltp_gene_count":13},{"uniquename":"PMID:22474084","title":"A highly efficient multifunctional tandem affinity purification approach applicable to diverse organisms.","citation":"Mol Cell Proteomics 2012 Aug;11(8):501-11","abstract":"Determining the localization, binding partners, and secondary modifications of individual proteins is crucial for understanding protein function. Several tags have been constructed for protein localization or purification under either native or denaturing conditions, but few tags permit all three simultaneously. Here, we describe a multifunctional tandem affinity purification (MAP) method that is both highly efficient and enables protein visualization. The MAP tag utilizes affinity tags inserted into an exposed surface loop of mVenus offering two advantages: (1) mVenus fluorescence can be used for protein localization or FACS-based selection of cell lines; and (2) spatial separation of the affinity tags from the protein results in high recovery and reduced variability between proteins. MAP purification was highly efficient in multiple organisms for all proteins tested. As a test case, MAP combined with liquid chromatography-tandem MS identified known and new candidate binding partners and modifications of the kinase Plk1. Thus the MAP tag is a new powerful tool for determining protein modification, localization, and interactions.","doi":"10.1074/mcp.O111.016246","authors":"Ma H, McLean JR, Chao LF, Mana-Capelli S, Paramasivam M, Hagstrom KA, Gould KL, McCollum D","authors_abbrev":"Ma H et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-04-05","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:48:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21299964","title":"[What defines the genetic map? The specification of meiotic recombination sites].","citation":"Med Sci (Paris) 2011 Jan;27(1):63-9","abstract":"During meiosis, homologous reciprocal recombination events or crossing-over determine the genetic map and are known not to be randomly distributed in the genome. Recent studies in yeasts and mammals reveal some key features of the molecular mechanism involved in this distribution. Through different molecular processes, specific histone post-translational modifications are induced at specific genomic sites, called hotspots, where initiation of meiotic recombination takes place. These sites are some transcription promoters in S. cerevisiae or binding sites for transcription factors in S. pombe, where chromatin modifiers are recruited. In mammals, the sites are DNA sequences recognized by the PRDM9 protein which has the ability both to bind DNA and to induce the trimethylation of the lysine 4 of histone H3. The properties of the chromatin at these sites, and potentially the binding of additional factors, allow the recruitment of proteins involved in the formation of DNA double strand breaks that initiate meiotic recombination.","doi":"10.1051/medsci/201127163","authors":"Grey C, Sommermeyer V, Borde V, de Massy B","authors_abbrev":"Grey C et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2011-02-09","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30797551","title":"TORC1 regulates autophagy induction in response to proteotoxic stress in yeast and human cells.","citation":"Biochem Biophys Res Commun 2019 Apr 02;511(2):434-439","abstract":"Misfolded and aggregated proteins are eliminated to maintain protein homeostasis. Autophagy contributes to the removal of protein aggregates. However, if and how proteotoxic stress induces autophagy is poorly understood. Here we show that proteotoxic stress after treatment with azetidine-2-carboxylic acid (AZC), a toxic proline analog, induces autophagy in budding yeast. AZC treatment attenuated target of rapamycin complex 1 (TORC1) activity, resulting in the dephosphorylation of Atg13, a key factor of autophagy. By contrast, AZC treatment did not affect target of rapamycin complex 2 (TORC2). Proteotoxic stress also induced TORC1 inactivation and autophagy in fission yeast and human cells. This study suggested that TORC1 is a conserved key factor to cope with proteotoxic stress in eukaryotic cells.","doi":"10.1016/j.bbrc.2019.02.077","authors":"Suda K, Kaneko A, Shimobayashi M, Nakashima A, Maeda T, Hall MN, Ushimaru T","authors_abbrev":"Suda K et al.","pubmed_publication_date":"02 Apr 2019","pubmed_entrez_date":"2019-02-25","publication_year":"2019","canto_session_key":"e839ec65082d969d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-02-26 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15298676","title":"Meiosis induced by inactivation of Pat1 kinase proceeds with aberrant nuclear positioning of centromeres in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Cells 2004 Aug;9(8):671-84","abstract":"Nuclear organization of chromosomes proceeds with significant changes during meiosis. In the fission yeast Schizosaccharomyces pombe, centromeres are clustered at the spindle-pole body (SPB) during the mitotic cell cycle; however, during meiotic prophase telomeres become clustered to the SPB and centromeres dissociate from the SPB. We followed the movement of telomeres, centromeres and sister chromatids in living S. pombe cells that were induced to meiosis by inactivation of Pat1 kinase (a key negative regulator of meiosis). Time-course observation in living cells determined the temporal order of DNA synthesis, telomere clustering, centromere separation and meiotic chromosome segregation. When meiosis was induced by Pat1 inactivation at the G1 phase of mitosis, telomeres clustered to the SPB as per normal meiosis, but in most cells the centromeres remained partially associated with the SPB. When meiosis was initiated at the G2 phase by Pat1 inactivation, both telomeres and centromeres retained their mitotic nuclear positions in the majority of cells. These results indicate that the progression of meiosis induced by Pat1 inactivation is aberrant from normal meiosis in some events. As Pat1 inactivation is often useful to induce S. pombe cells synchronously into meiosis, the temporal order of chromosomal events determined here will provide landmarks for the progression of meiosis downstream the Pat1 inactivation.","authors":"Chikashige Y, Kurokawa R, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"Aug 2004","pubmed_entrez_date":"2004-08-10","publication_year":"2004","canto_session_key":"e06c92411147182b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-23 14:08:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-23 14:08:44","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-23"},{"uniquename":"PMID:36505930","title":"FK506-binding protein, FKBP12, promotes serine utilization and negatively regulates threonine deaminase in fission yeast.","citation":"iScience 2022 Dec 22;25(12):105659","abstract":"FK506-binding protein with a molecular weight of 12 kDa (FKBP12) is a receptor of the immunosuppressive drugs, FK506 and rapamycin. The physiological functions of FKBP12 remain ambiguous because of its nonessentiality and multifunctionality. Here, we show that FKBP12 promotes the utilization of serine as a nitrogen source and regulates the isoleucine biosynthetic pathway in fission yeast. In screening for small molecules that inhibit serine assimilation, we found that the growth of fission yeast cells in medium supplemented with serine as the sole nitrogen source, but not in glutamate-supplemented medium, was suppressed by FKBP12 inhibitors. Knockout of FKBP12 phenocopied the action of these compounds in serine-supplemented medium. Metabolome analyses and genetic screens identified the threonine deaminase, Tda1, to be regulated downstream of FKBP12. Genetic and biochemical analyses unveiled the negative regulation of Tda1 by FKBP12. Our findings reveal new roles of FKBP12 in amino acid biosynthesis and nitrogen metabolism homeostasis.","doi":"10.1016/j.isci.2022.105659","authors":"Sasaki M, Nishimura S, Yashiroda Y, Matsuyama A, Kakeya H, Yoshida M","authors_abbrev":"Sasaki M et al.","pubmed_publication_date":"22 Dec 2022","pubmed_entrez_date":"2022-12-12","publication_year":"2022","canto_session_key":"c0d300fc2977c65c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-12-13 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41501458","title":"Stress controls heterochromatin inheritance via histone H3 ubiquitylation.","citation":"Nature 2026 Jan 07;","abstract":"Heterochromatin, marked by histone H3 lysine 9 methylation, can be epigenetically inherited through cell division 1-3 , maintaining gene repression that preserves cell identity and enables adaptation to environmental challenges 2-6 . Studies on Schizosaccharomyces pombe have shown that heterochromatin propagation depends on the read-write mechanism, wherein a sufficient density of H3K9me3-modified nucleosomes, stabilized by histone deacetylases, concentrates Clr4 SUV39H  on chromatin to promote further deposition of H3K9 methylation 7-9 . Whether other mechanisms control heterochromatin propagation by means of Clr4 SUV39H , a subunit of the E3 ubiquitin ligase complex ClrC 10-12 , was unknown. Here we uncover a ubiquitin-dependent heterochromatin heritability regulatory hub (HRH) that broadly governs heterochromatin propagation, even without histone deacetylase activity. The HRH is tuned by the limiting factor Raf1 DDB2 , a substrate receptor for the ClrC ubiquitin ligase. In addition to linking Clr4 SUV39H  to other ClrC components on chromatin, Raf1 DDB2  acts in a dosage-dependent manner to promote ubiquitination of histone H3 at lysine 14 (H3K14ub), which is critical for heterochromatin self-propagation. HRH is intricately linked to environmentally responsive pathways, including nonsense-mediated decay (NMD) and target of rapamycin (TOR) signalling, enabling cells to adapt to changing conditions. By modulating heterochromatin propagation, cells leverage the HRH to gain resistance to antifungal agents and adapt to high temperature. Thus, heterochromatin self-propagation is actively regulated by means of H3K14ub in response to external stimuli, with broad implications for understanding mechanisms governing rapid changes in the epigenetic landscape in physiology and disease.","doi":"10.1038/s41586-025-09899-8","authors":"Bhatt B, Wei Y, Pradhan AK, Dhakshnamoorthy J, Zofall M, Xiao H, Vijayakumari D, Jain S, Folco HD, Qi H, Ball DA, Karpova TS, Wheeler D, Wong J, Grewal SIS","authors_abbrev":"Bhatt B et al.","pubmed_publication_date":"07 Jan 2026","pubmed_entrez_date":"2026-01-07","publication_year":"2026","canto_session_key":"97e9e18455ebeeed","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-01-09 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35849625","title":"Structural insights into Pot1-ssDNA, Pot1-Tpz1 and Tpz1-Ccq1 Interactions within fission yeast shelterin complex.","citation":"PLoS Genet 2022 Jul;18(7):e1010308","abstract":"The conserved shelterin complex caps chromosome ends to protect telomeres and regulate telomere replication. In fission yeast Schizosaccharomyces pombe, shelterin consists of telomeric single- and double-stranded DNA-binding modules Pot1-Tpz1 and Taz1-Rap1 connected by Poz1, and a specific component Ccq1. While individual structures of the two DNA-binding OB folds of Pot1 (Pot1OB1-GGTTAC and Pot1OB2-GGTTACGGT) are available, structural insight into recognition of telomeric repeats with spacers by the complete DNA-binding domain (Pot1DBD) remains an open question. Moreover, structural information about the Tpz1-Ccq1 interaction requires to be revealed for understanding how the specific component Ccq1 of S. pombe shelterin is recruited to telomeres to function as an interacting hub. Here, we report the crystal structures of Pot1DBD-single-stranded-DNA, Pot1372-555-Tpz1185-212 and Tpz1425-470-Ccq1123-439 complexes and propose an integrated model depicting the assembly mechanism of the shelterin complex at telomeres. The structure of Pot1DBD-DNA unveils how Pot1 recognizes S. pombe degenerate telomeric sequences. Our analyses of Tpz1-Ccq1 reveal structural basis for the essential role of the Tpz1-Ccq1 interaction in telomere recruitment of Ccq1 that is required for telomere maintenance and telomeric heterochromatin formation. Overall, our findings provide valuable structural information regarding interactions within fission yeast shelterin complex at 3' ss telomeric overhang.","doi":"10.1371/journal.pgen.1010308","authors":"Sun H, Wu Z, Zhou Y, Lu Y, Lu H, Chen H, Shi S, Zeng Z, Wu J, Lei M","authors_abbrev":"Sun H et al.","pubmed_publication_date":"Jul 2022","pubmed_entrez_date":"2022-07-18","publication_year":"2022","canto_session_key":"a167803b4c2f3def","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-07-20 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.07","SPAC6F6.16c","SPAC26H5.06"],"gene_count":3,"ltp_gene_count":3,"pdb_entries":[{"pdb_id":"7cuj","gene_chains":[{"gene_uniquename":"SPAC6F6.16c","chain":"C/D","position":"426-470"},{"gene_uniquename":"SPCC188.07","chain":"A/B","position":"123-439"}],"title":"Crystal structure of fission yeast Ccq1 and Tpz1","entry_authors":"Sun H,Wu Z,Wu J,Lei M","entry_authors_abbrev":"Sun H et al.","reference_uniquename":"PMID:35849625","experimental_method":"X-ray","resolution":"2.4"},{"pdb_id":"7cuh","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A","position":"1-339"}],"title":"Crystal structure of fission yeast Pot1 and ssDNA","entry_authors":"Sun H,Wu Z,Wu J,Lei M","entry_authors_abbrev":"Sun H et al.","reference_uniquename":"PMID:35849625","experimental_method":"X-ray","resolution":"3.0"},{"pdb_id":"7cui","gene_chains":[{"gene_uniquename":"SPAC26H5.06","chain":"A/C","position":"357-555"},{"gene_uniquename":"SPAC6F6.16c","chain":"B/D","position":"164-240"}],"title":"Crystal structure of fission yeast Pot1 and Tpz1","entry_authors":"Sun H,Wu Z,Wu J,Lei M","entry_authors_abbrev":"Sun H et al.","reference_uniquename":"PMID:35849625","experimental_method":"X-ray","resolution":"2.6"}]},{"uniquename":"PMID:40709928","title":"The negligible mutagenic effects of norfloxacin on the genome of the fission yeast  Schizosaccharomyces pombe  ATCC-16979.","citation":"Microbiol Spectr 2025 Jul 25;:e0023325","abstract":"Antibiotic therapy is commonly used in various medical scenarios, and some antibiotics will stay in the blood serum for days. Previous studies have demonstrated that the fluoroquinolone antibiotic norfloxacin exerts mutagenic effects on the whole genomes of target bacteria. However, whether and to what degree these effects compromise non-target eukaryotic genomes remains unclear. Here, we explored this using mutation accumulation experiments with the fission yeast  Schizosaccharomyces pombe  ATCC-16979, treated with or without norfloxacin at a dose comparable to the therapeutic concentration found in patient blood. Based on a  de novo  assembly and the mutation accumulation lines without treatment, ATCC-16979 demonstrates a strong mutation bias in the A/T direction (4.33). Furthermore, norfloxacin treatment did not significantly elevate the genomic mutation rate of the fission yeast, based on the analysis of 94 mutation accumulation lines run for ~169,000 cell divisions in total. Nucleotide excision repair was induced by the norfloxacin treatment and might help to counteract the possible mutagenic effects of norfloxacin, as revealed by RNAseq-based differential gene-expression analyses. Norfloxacin thus poses a negligible genotoxic threat to eukaryotic and potentially human genomes, bolstering the safe clinical use of this important antibiotic.IMPORTANCEThis study addresses concerns about the potential mutagenic side effects of antibiotics, specifically norfloxacin, which is widely used in clinical settings. While previous research has shown that norfloxacin can cause mutations in bacteria, it was unclear whether it could also harm human or other eukaryotic genomes. By using the fission yeast  Schizosaccharomyces pombe  as a model, we found that norfloxacin treatment did not significantly increase the mutation rate in eukaryotic cells, possibly resulting from a cellular repair mechanism counteracting potential DNA damage. These findings provide reassurance that, at therapeutic levels, norfloxacin does not pose a significant genetic risk to eukaryotic organisms, supporting its continued safe use in medical treatments.","doi":"10.1128/spectrum.00233-25","authors":"Lin T, Wu X, Lan Y, Huang Y, Deng Z, Zhang Y, Lynch M, Long H, Pan J","authors_abbrev":"Lin T et al.","pubmed_publication_date":"25 Jul 2025","pubmed_entrez_date":"2025-07-25","publication_year":"2025","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2025-07-25 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19467630","title":"Development, evaluation and application of tripeptidyl-peptidase II sequence signatures.","citation":"Arch Biochem Biophys 2009 Apr 01;484(1):39-45","abstract":"Tripeptidyl-peptidase II (TPP II) is a cytosolic peptidase that has been implicated in fat formation and cancer, apparently independent of the enzymatic activity. In search for alternative functional regions, conserved motifs were identified and eleven signatures were constructed. Seven of the signatures covered previously investigated residues, whereas the functional importance of the other motifs is unknown. This provides directions for future investigations of alternative activities of TPP II. The obtained signatures provide an efficient bioinformatic tool for the identification of TPP II homologues. Hence, a TPP II sequence homologue from fission yeast, Schizosaccharomyces pombe, was identified and demonstrated to encode the TPP II-like protein previously reported as multicorn. Furthermore, an homologous protein was found in the prokaryote Blastopirellula marina, albeit the TPP II function was apparently not conserved. This gene is probably the result of a rare gene transfer from eukaryote to prokaryote.","doi":"10.1016/j.abb.2009.01.007","authors":"Eriksson S, Gutiérrez OA, Bjerling P, Tomkinson B","authors_abbrev":"Eriksson S et al.","pubmed_publication_date":"01 Apr 2009","pubmed_entrez_date":"2009-05-27","publication_year":"2009","canto_session_key":"de53106121064e17","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pernilla Bjerling","canto_approved_date":"2013-07-01 18:00:07","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-06-25 20:42:05","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Pernilla Bjerling","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-06-25"},{"uniquename":"PMID:37288768","title":"Altered cohesin dynamics and H3K9 modifications contribute to mitotic defects in the cbf11Δ lipid metabolism mutant.","citation":"J Cell Sci 2023 Jun 01;136(11)","abstract":"Mitotic fidelity is crucial for the faithful distribution of genetic information into the daughter cells. Many fungal species, including the fission yeast Schizosaccharomyces pombe, undergo a closed form of mitosis, during which the nuclear envelope does not break down. In S. pombe, numerous processes have been identified that contribute to successful completion of mitosis. Notably, perturbations of lipid metabolism can lead to catastrophic mitosis and the 'cut' phenotype. It has been suggested that these mitotic defects are caused by insufficient membrane phospholipid supply during the anaphase nuclear expansion. However, it is not clear whether additional factors are involved. In this study, we characterized in detail mitosis in an S. pombe mutant lacking the Cbf11 transcription factor, which regulates lipid metabolism genes. We show that in cbf11Δ cells mitotic defects have already appeared prior to anaphase, before the nuclear expansion begins. Moreover, we identify altered cohesin dynamics and centromeric chromatin structure as additional factors affecting mitotic fidelity in cells with disrupted lipid homeostasis, providing new insights into this fundamental biological process.","doi":"10.1242/jcs.261265","authors":"Vishwanatha A, Princová J, Hohoš P, Zach R, Převorovský M","authors_abbrev":"Vishwanatha A et al.","pubmed_publication_date":"01 Jun 2023","pubmed_entrez_date":"2023-06-08","publication_year":"2023","canto_session_key":"d735a52f09029ebf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Akshay Vishwanatha","canto_first_approved_date":"2023-10-05 16:23:30","canto_approved_date":"2023-11-27 18:51:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-03 22:49:03","canto_added_date":"2023-05-19 00:15:04","annotation_curators":[{"name":"Akshay Vishwanatha","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.17c","SPCC736.08","SPBC29A10.04","SPCC1322.12c","SPAC110.02","SPBC800.05c","SPBC20F10.06"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2023-10-05"},{"uniquename":"PMID:11891124","title":"A unified view of the DNA-damage checkpoint.","citation":"Curr Opin Cell Biol 2002 Apr;14(2):237-45","abstract":"Recent investigation of the DNA-damage checkpoint in several organisms has highlighted the conservation of this pathway. The checkpoint's signal transduction pathway consists of four conserved classes of molecules: two large protein kinases having homology to phosphatidylinositol 3-kinases, three \"sensor\" proteins with homology to proliferating cell nuclear antigen, two serine/threonine (S/T) kinases, and two adaptors for the S/T kinases. This review compares the role of these four classes of checkpoint proteins in humans and model organisms.","authors":"Melo J, Toczyski D","authors_abbrev":"Melo J et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-03-14","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28913346","title":"Live fast, die fast principle in a single cell of fission yeast.","citation":"Microb Cell 2017 Aug 13;4(9):308-310","abstract":"Growth and death are both fundamental macroscopic properties for all living matters, and thus cell division and mortality rates are good parameters for characterizing cellular physiology in a given environment. While population growth rates in various conditions have been reported in literature, death rate is rarely measured, especially in favorable culture conditions where cells grow exponentially. In our recent study (Nakaoka and Wakamoto, 2017), we developed a microfluidics-based platform to track multiple single cell lineages until death. The system enabled us to monitor both cell growth and death in controlled steady environments, and we confirmed the absence of replicative aging in fission yeast old-pole cell lineages by showing remarkable constancy both in cell division and mortality rates. Furthermore, we revealed a growth-death trade-off relation in non-stressed conditions. The phenomenological law that constrains macroscopic physiological parameters could provide a new quantitative insight into possible balanced-growth states in various environments.","doi":"10.15698/mic2017.09.591","authors":"Nakaoka H","authors_abbrev":"Nakaoka H","pubmed_publication_date":"13 Aug 2017","pubmed_entrez_date":"2017-09-16","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-09-17 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33223513","title":"Systematic Target Screening Revealed That Tif302 Could Be an Off-Target of the Antifungal Terbinafine in Fission Yeast.","citation":"Biomol Ther (Seoul) 2021 Mar 01;29(2):234-247","abstract":"We used a heterozygous gene deletion library of fission yeasts comprising all essential and non-essential genes for a microarray screening of target genes of the antifungal terbinafine, which inhibits ergosterol synthesis via the Erg1 enzyme. We identified 14 heterozygous strains corresponding to 10 non-essential [7 ribosomal-protein (RP) coding genes,  spt7 ,  spt20 , and  elp2 ] and 4 essential genes ( tif302 ,  rpl2501 ,  rpl31 , and  erg1 ). Expectedly, their  erg1  mRNA and protein levels had decreased compared to the control strain SP286. When we studied the action mechanism of the non-essential target genes using cognate haploid deletion strains, knockout of SAGA-subunit genes caused a down-regulation in  erg1  transcription compared to the control strain ED668. However, knockout of RP genes conferred no susceptibility to ergosterol-targeting antifungals. Surprisingly, the RP genes participated in the  erg1  transcription as components of repressor complexes as observed in a comparison analysis of the experimental ratio of  erg1  mRNA. To understand the action mechanism of the interaction between the drug and the novel essential target genes, we performed isobologram assays with terbinafine and econazole (or cycloheximide). Terbinafine susceptibility of the  tif302  heterozygous strain was attributed to both decreased  erg1  mRNA levels and inhibition of translation. Moreover, Tif302 was required for efficacy of both terbinafine and cycloheximide. Based on a molecular modeling analysis, terbinafine could directly bind to Tif302 in yeasts, suggesting Tif302 as a potential off-target of terbinafine. In conclusion, this genome-wide screening system can be harnessed for the identification and characterization of target genes under any condition of interest.","doi":"10.4062/biomolther.2020.166","authors":"Lee S, Nam M, Lee AR, Lee J, Woo J, Kang NS, Balupuri A, Lee M, Kim SY, Ro H, Choi YW, Kim DU, Hoe KL","authors_abbrev":"Lee S et al.","pubmed_publication_date":"01 Mar 2021","pubmed_entrez_date":"2020-11-23","publication_year":"2021","canto_session_key":"4072a96378948dec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sol Lee","canto_first_approved_date":"2020-12-16 15:38:25","canto_approved_date":"2021-04-09 15:19:47","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-12-11 03:48:27","canto_added_date":"2020-11-25 01:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":341,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sol Lee","community_curator":true,"annotation_count":14,"orcid":"0000-0003-1743-2419","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23A1.11","SPCC895.06","SPBC713.12","SPBC106.18","SPBC21C3.13","SPBP22H7.08","SPBC1709.18","SPBC17G9.07","SPAC25G10.06","SPCC18B5.01c","SPBC25H2.11c","SPCC1259.01c","SPAC17C9.16c","SPBC21H7.02","SPCC1902.01","SPCC1322.11","SPCC31H12.04c","SPBC11C11.09c","SPBC18H10.14","SPBC13E7.10c","SPAC20G4.03c","SPAC4D7.10c","SPAC25G10.08","SPAC890.08"],"gene_count":24,"ltp_gene_count":24,"approved_date":"2020-12-16"},{"uniquename":"PMID:7785323","title":"Effects of phleomycin-induced DNA damage on the fission yeast Schizosaccharomyces pombe cell cycle.","citation":"Yeast 1995 Mar;11(3):225-31","abstract":"The effect of phleomycin, a bleomycin-like antibiotic, has been investigated in the fission yeast, Schizosaccharomyces pombe. We report that in response to phleomycin-induced DNA damage, growth was inhibited and S. pombe cells arrested in the G2-phase of the cell cycle. DNA repair mutants rad9 and rad17 did not arrest and were hypersensitive to phleomycin. Cell cycle mutants that entered mitosis without monitoring the completion of DNA replication also displayed an increased sensitivity to this DNA-damaging agent. Thus, phleomycin could be used as a tool in the fission yeast S. pombe model system for the study of DNA damage and cell cycle checkpoints, or as a new selective agent.","authors":"Belenguer P, Oustrin ML, Tiraby G, Ducommun B","authors_abbrev":"Belenguer P et al.","pubmed_publication_date":"Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000093","title":"Representation for the degradation to or via a chemical as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the degradation of a chemical entity to or via an other chemical entity as biological processes. The underlying equivalence axiom templates are \"GO:0009056 and 'has input' some S and 'has output' some T\" (catabolism to) and \"GO:0009056 and 'has input' some S and 'has intermediate' some I\" (catabolism via), where S,T, and I are chemical entities (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25812159","title":"Kojak: efficient analysis of chemically cross-linked protein complexes.","citation":"J Proteome Res 2015 May 01;14(5):2190-8","abstract":"Protein chemical cross-linking and mass spectrometry enable the analysis of protein-protein interactions and protein topologies; however, complicated cross-linked peptide spectra require specialized algorithms to identify interacting sites. The Kojak cross-linking software application is a new, efficient approach to identify cross-linked peptides, enabling large-scale analysis of protein-protein interactions by chemical cross-linking techniques. The algorithm integrates spectral processing and scoring schemes adopted from traditional database search algorithms and can identify cross-linked peptides using many different chemical cross-linkers with or without heavy isotope labels. Kojak was used to analyze both novel and existing data sets and was compared to existing cross-linking algorithms. The algorithm provided increased cross-link identifications over existing algorithms and, equally importantly, the results in a fraction of computational time. The Kojak algorithm is open-source, cross-platform, and freely available. This software provides both existing and new cross-linking researchers alike an effective way to derive additional cross-link identifications from new or existing data sets. For new users, it provides a simple analytical resource resulting in more cross-link identifications than other methods.","doi":"10.1021/pr501321h","authors":"Hoopmann MR, Zelter A, Johnson RS, Riffle M, MacCoss MJ, Davis TN, Moritz RL","authors_abbrev":"Hoopmann MR et al.","pubmed_publication_date":"01 May 2015","pubmed_entrez_date":"2015-03-27","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-02-03 01:15:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31287970","title":"Reconstitution of Microtubule Nucleation In Vitro Reveals Novel Roles for Mzt1.","citation":"Curr Biol 2019 Jul 08;29(13):2199-2207.e10","abstract":"Microtubule (MT) nucleation depends on the γ-tubulin complex (γ-TuC), in which multiple copies of the heterotetrameric γ-tubulin small complex (γ-TuSC) associate to form a ring-like structure (in metazoans, γ-tubulin ring complex; γ-TuRC) [1-7]. Additional conserved regulators of the γ-TuC include the small protein Mzt1 (MOZART1 in human; GIP1/1B and GIP2/1A in plants) [8-13] and proteins containing a Centrosomin Motif 1 (CM1) domain [10, 14-19]. Many insights into γ-TuC regulators have come from in vivo analysis in fission yeast Schizosaccharomyces pombe. The S. pombe CM1 protein Mto1 recruits the γ-TuC to microtubule-organizing centers (MTOCs) [14, 20-22], and analysis of Mto1[bonsai], a truncated version of Mto1 that cannot localize to MTOCs, has shown that Mto1 also has a role in γ-TuC activation [23]. S. pombe Mzt1 interacts with γ-TuSC and is essential for γ-TuC function and localization to MTOCs [11, 12]. However, the mechanisms by which Mzt1 functions remain unclear. Here we describe reconstitution of MT nucleation using purified recombinant Mto1[bonsai], the Mto1 partner protein Mto2, γ-TuSC, and Mzt1. Multiple copies of the six proteins involved coassemble to form a 34-40S ring-like \"MGM\" holocomplex that is a potent MT nucleator in vitro. Using purified MGM and subcomplexes, we investigate the role of Mzt1 in MT nucleation. Our results suggest that Mzt1 is critical to stabilize Alp6, the S. pombe homolog of human γ-TuSC protein GCP3, in an \"interaction-competent\" form within the γ-TuSC. This is essential for MGM to become a functional nucleator.","doi":"10.1016/j.cub.2019.05.058","authors":"Leong SL, Lynch EM, Zou J, Tay YD, Borek WE, Tuijtel MW, Rappsilber J, Sawin KE","authors_abbrev":"Leong SL et al.","pubmed_publication_date":"08 Jul 2019","pubmed_entrez_date":"2019-07-10","publication_year":"2019","canto_session_key":"df057bdbc097c01d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-07-11 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31476650","title":"Molecular choreography of pre-mRNA splicing by the spliceosome.","citation":"Curr Opin Struct Biol 2019 Dec;59:124-133","abstract":"The spliceosome executes eukaryotic precursor messenger RNA (pre-mRNA) splicing to remove noncoding introns through two sequential transesterification reactions, branching and exon ligation. The fidelity of this process is based on the recognition of the conserved sequences in the intron and dynamic compositional and structural rearrangement of this multi-megadalton machinery. Since atomic visualization of the splicing active site in an endogenous Schizosaccharomyces pombe spliceosome in 2015, high-resolution cryoelectron microscopy (cryo-EM) structures of other spliceosome intermediates began to uncover the molecular mechanism. Recent advances in the structural biology of the spliceosome make it clearer the mechanisms of its assembly, activation, disassembly and exon ligation. Together, these discrete structural images give rise to a molecular choreography of the spliceosome.","doi":"10.1016/j.sbi.2019.07.010","authors":"Wan R, Bai R, Shi Y","authors_abbrev":"Wan R et al.","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-09-03","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-09-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22298427","title":"Roles of putative Rho-GEF Gef2 in division-site positioning and contractile-ring function in fission yeast cytokinesis.","citation":"Mol Biol Cell 2012 Apr;23(7):1181-95","abstract":"Cytokinesis is crucial for integrating genome inheritance and cell functions. In multicellular organisms, Rho-guanine nucleotide exchange factors (GEFs) and Rho GTPases are key regulators of division-plane specification and contractile-ring formation during cytokinesis, but how they regulate early steps of cytokinesis in fission yeast remains largely unknown. Here we show that putative Rho-GEF Gef2 and Polo kinase Plo1 coordinate to control the medial cortical localization and function of anillin-related protein Mid1. The division-site positioning defects of gef2Δ plo1-ts18 double mutant can be partially rescued by increasing Mid1 levels. We find that Gef2 physically interacts with the Mid1 N-terminus and modulates Mid1 cortical binding. Gef2 localization to cortical nodes and the contractile ring depends on its last 145 residues, and the DBL-homology domain is important for its function in cytokinesis. Our data suggest the interaction between Rho-GEFs and anillins is an important step in the signaling pathways during cytokinesis. In addition, Gef2 also regulates contractile-ring function late in cytokinesis and may negatively regulate the septation initiation network. Collectively, we propose that Gef2 facilitates and stabilizes Mid1 binding to the medial cortex, where the localized Mid1 specifies the division site and induces contractile-ring assembly.","doi":"10.1091/mbc.E11-09-0800","authors":"Ye Y, Lee IJ, Runge KW, Wu JQ","authors_abbrev":"Ye Y et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-02-03","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31A2.16","SPCC4B3.15","SPAC24B11.11c","SPAC23C11.16","SPAC57A10.02","SPAC4A8.05c","SPCC1739.11c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:31828313","title":"Homologous recombination repair intermediates promote efficient de novo telomere addition at DNA double-strand breaks.","citation":"Nucleic Acids Res 2020 Feb 20;48(3):1271-1284","abstract":"The healing of broken chromosomes by de novo telomere addition, while a normal developmental process in some organisms, has the potential to cause extensive loss of heterozygosity, genetic disease, or cell death. However, it is unclear how de novo telomere addition (dnTA) is regulated at DNA double-strand breaks (DSBs). Here, using a non-essential minichromosome in fission yeast, we identify roles for the HR factors Rqh1 helicase, in concert with Rad55, in suppressing dnTA at or near a DSB. We find the frequency of dnTA in rqh1Δ rad55Δ cells is reduced following loss of Exo1, Swi5 or Rad51. Strikingly, in the absence of the distal homologous chromosome arm dnTA is further increased, with nearly half of the breaks being healed in rqh1Δ rad55Δ or rqh1Δ exo1Δ cells. These findings provide new insights into the genetic context of highly efficient dnTA within HR intermediates, and how such events are normally suppressed to maintain genome stability.","doi":"10.1093/nar/gkz1109","authors":"Davé A, Pai CC, Durley SC, Hulme L, Sarkar S, Wee BY, Prudden J, Tinline-Purvis H, Cullen JK, Walker C, Watson A, Carr AM, Murray JM, Humphrey TC","authors_abbrev":"Davé A et al.","pubmed_publication_date":"20 Feb 2020","pubmed_entrez_date":"2019-12-13","publication_year":"2020","canto_session_key":"a8dfe7d57753a2f6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PB_REF:0000010","title":"GO-CAM Causal Activity Model Curation","abstract":"GO CAMs (Causal Activity Models) are pathway models curated manually by combining standard GO annotations. GO-CAM models can connect different pieces of information about the function of a gene product (joining together different annotations for the same gene product), and/or connect different gene products together by specifying how the activity of one gene product can affect the activity of another gene product. All connections in a GO-CAM model are made using clearly defined semantic relations from the Relations Ontology (https://obofoundry.org/ontology/ro.html). For more details about GO-CAMs see PMID:31548717.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22344254","title":"The Vam6 and Gtr1-Gtr2 pathway activates TORC1 in response to amino acids in fission yeast.","citation":"J Cell Sci 2012 Apr 15;125(Pt 8):1920-8","abstract":"The Rag family of GTPases has been implicated in the TORC1 activation in Drosophila and in mammalian cells in response to amino acids. We have investigated the role of the Rag GTPases Gtr1 and Gtr2 in TORC1 regulation in Schizosaccharomyces pombe. Fission yeast Gtr1 and Gtr2 are non-essential proteins that enhance cell growth in the presence of amino acids in the medium. The function of Gtr1 and Gtr2 in nutrient signaling is further supported by the observation that even in rich medium the deletion of either gene results in the promotion of mating, meiosis and sporulation, consistent with the downregulation of TORC1. We show that Gtr1 and Gtr2 colocalize with TORC1 in vacuoles, where TORC1 is presumably activated. Epistasis analyses indicated that Gtr1 and Gtr2 function downstream of Vam6 and upstream of TORC1 in response to amino acid signals. Our data demonstrate the existence of an evolutionarily conserved pathway with the Vam6 and Gtr1-Gtr2 pathway activating TORC1, which in turns stimulates cell growth and inhibits sexual differentiation.","doi":"10.1242/jcs.094219","authors":"Valbuena N, Guan KL, Moreno S","authors_abbrev":"Valbuena N et al.","pubmed_publication_date":"15 Apr 2012","pubmed_entrez_date":"2012-02-21","publication_year":"2012","canto_session_key":"936a8cb7143741d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-02-07 14:20:21","canto_approved_date":"2025-09-03 18:55:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-07 14:20:13","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H4.14","SPBC216.07c","SPAC57A7.11","SPBC337.13c","SPBC21B10.05c","SPAC13G6.07c","SPCC777.05"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2021-02-07"},{"uniquename":"PMID:22416758","title":"Mpg2 interacts and cooperates with Mpg1 to maintain yeast glycosylation.","citation":"FEMS Yeast Res 2012 Aug;12(5):511-20","abstract":"Using a yeast two-hybrid screen, we isolated a gene from Schizosaccharomyces pombe, whose product interacts with Mpg1, a GDP-mannose-1-phosphate guanylyltransferase involved in the maintenance of cell wall integrity and glycosylation. We have designated this gene mpg2 based on its similarity to Mpg1. Mpg2 is evolutionarily conserved in higher eukaryotes. In the absence of Mpg2, defects in cell growth and sensitivity to hygromycin B are observed. When mpg1 is depleted, the lack of mpg2 causes a synthetic enhancement of the growth defect, the sensitivity to hygromycin B and the cell cycle phenotype previously reported for mpg1 mutant. Finally, Mpg1 overexpression complements the Δmpg2 mutant phenotypes. Taken together, these results indicate that mpg1 and mpg2 function together in glycosylation and septum formation.","doi":"10.1111/j.1567-1364.2012.00801.x","authors":"Muñoz-Centeno MC, Martín-Guevara C, Flores A, Pérez-Pulido AJ, Antúnez-Rodríguez C, Castillo AG, Sanchez-Durán M, Mier P, Bejarano ER","authors_abbrev":"Muñoz-Centeno MC et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-03-16","publication_year":"2012","canto_session_key":"1eb406bf7346ff24","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-03-17 11:51:53","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-01 09:47:10","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC191.11","SPCC1906.01","SPBC13G1.02"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2013-02-01"},{"uniquename":"PMID:20723757","title":"The monopolin complex crosslinks kinetochore components to regulate chromosome-microtubule attachments.","citation":"Cell 2010 Aug 20;142(4):556-67","abstract":"The monopolin complex regulates different types of kinetochore-microtubule attachments in fungi, ensuring sister chromatid co-orientation in Saccharomyces cerevisiae meiosis I and inhibiting merotelic attachment in Schizosaccharomyces pombe mitosis. In addition, the monopolin complex maintains the integrity and silencing of ribosomal DNA (rDNA) repeats in the nucleolus. We show here that the S. cerevisiae Csm1/Lrs4 monopolin subcomplex has a distinctive V-shaped structure, with two pairs of protein-protein interaction domains positioned approximately 10 nm apart. Csm1 presents a conserved hydrophobic surface patch that binds two kinetochore proteins: Dsn1, a subunit of the outer-kinetochore MIND/Mis12 complex, and Mif2/CENP-C. Csm1 point-mutations that disrupt kinetochore-subunit binding also disrupt sister chromatid co-orientation in S. cerevisiae meiosis I. We further show that the same Csm1 point-mutations affect rDNA silencing, probably by disrupting binding to the rDNA-associated protein Tof2. We propose that Csm1/Lrs4 functions as a molecular clamp, crosslinking kinetochore components to enforce sister chromatid co-orientation in S. cerevisiae meiosis I and to suppress merotelic attachment in S. pombe mitosis, and crosslinking rDNA repeats to aid rDNA silencing.","doi":"10.1016/j.cell.2010.07.017","authors":"Corbett KD, Yip CK, Ee LS, Walz T, Amon A, Harrison SC","authors_abbrev":"Corbett KD et al.","pubmed_publication_date":"20 Aug 2010","pubmed_entrez_date":"2010-08-21","publication_year":"2010","canto_session_key":"58a7e493af7097b3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-04-23 21:21:21","canto_approved_date":"2023-04-07 07:11:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-13 15:05:18","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.04","SPAC11E3.03","SPBC1861.01c","SPBC409.09c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-04-23"},{"uniquename":"PMID:163826","title":"Stimulation of active uptake of nucleosides and amino acids by cyclic adenosine 3' :5'-monophosphate in the yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1975 Mar 25;250(6):2354-62","abstract":"In conditions of glucose starvation, the maximum velocity of the mediated transport of nonmetabolized and metabolized amino acids, uridine, adenosine, and sucrose across the plasma membrane is stimulated by a factor of two by the addition of 1 mM adenosine 3':5'-monophosphate to Schizosaccharomyces pombe 972h- wild strain, to the glucose-super-repressed and derepressed mutants COB5 and COB6, and to Saccharomyces cerevisiae strain IL 216-IA. The mediated uptake of 2-D-deoxyglucose and the apparently nonmediated uptake of guanosine are not stimulated by the cyclic nucleotide. N6,O2'-Dibutyryl adenosine 3':5'-monophosphate is also efficient, whereas theophylline, guanosine 3':5'-monophosphate, 5'-AMP, ATP, and adenosine are ineffective. The cellular ATP content of glycerol-grown S. pombe COB5 is about 10 nmol per mg of protein and is not decreased by further incubation in the starvation medium. The addition of 100 mM glucose markedly enhances transport without any increase of the cellular ATP content. The addition of antimycin A or Dio-9 decreases markedly both cellular ATP content and transport. The addition of 2.5 mM glucose to antimycin A-containing medium restores both transport is not necessarily of mitochondrial origin. The uptake of 2-D-deoxyglucose is unaffected by the respiratory inhibitors. Stimulation of uptake by cyclic adenosine 3':5'-monophosphate occurs only in glucose-deprived cells. The addition of 10 mM glucose elicits the disappearance of the stimulation and prevents the 30% decrease of the cellular adenosine 3':5'-monophosphate content produced by glucose starvation. Adenosine 3':5'-'monophosphate does not enhance the steady state ATP level but requires cellular ATP produced either by endogenous respiration or, in the absence of respiration blocked by antimycin A, by further addition of 2.5 mM glucose. Stimulation of active uptake by adenosine 3':5'-monophosphate does not require protein synthesis because the addition of cycloheximide or anisomycin does not prevent the stimulation of L-leucine uptake. In the absence of respiration, Dio-9, and ATPase inhibitor, suppresses instantaneously the cellular ejection of protons as well as the uptake of uridine and amino acids. It abolishes also the adenosine 3':5'-monophosphate-stimulated transport. In the presence of antimycin A, specific mitochondrial ATPase inhibitors such as venruricidin A do not inhibit metabolite uptakes and their stimulation by adenosine 3':5'-monophosphate. These results suggest that in these conditions, the target of Dio-9 is not the mitochondrial ATPase but a plasma membrane proton-translocating function generating an electrochemical gradient required for active transport. That adenosine 3':5'-monophosphate enhances the Dio-9-sensitive proton extrusion supports the view that the cyclic nucleotide might modulate the plasma membrane ATPase.","authors":"Foury F, Goffeau A","authors_abbrev":"Foury F et al.","pubmed_publication_date":"25 Mar 1975","pubmed_entrez_date":"1975-03-25","publication_year":"1975","canto_session_key":"8f452867489bb675","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-24 10:48:13","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-24 10:47:43","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-24"},{"uniquename":"PMID:8159167","title":"Molecular cloning and characterization of the Schizosaccharomyces pombe his3 gene for use as a selectable marker.","citation":"Mol Gen Genet 1994 Jan;242(2):169-76","abstract":"A DNA fragment which carries the his3 gene of Schizosaccharomyces pombe has been isolated and characterized for use as a selectable marker in transformations. The his3 gene encodes the imidazole acetol phosphate transaminase enzyme (E.C.2.6.1.9), which is responsible for converting imidazole acetol-P to histidinol-P in step 8 of histidine biosynthesis. The nucleotide sequences of a 2196 bp gene fragment and a corresponding cDNA clone were determined. Three intron sequences punctuate the 1451 bp coding region which generates a predicted polypeptide of 384 amino acids with a molecular mass of 42736 daltons. Northern analysis of his3 mRNAs indicates that the transcript is approximately 1.6 kb in size. Steady-state levels are down-regulated by nitrogen limitation but are unaffected by histidine starvation. The deduced amino acid sequence was compared to the Saccharomyces cerevisiae HIS5, Escherichia coli HisC, and Salmonella typhimurium HisC proteins, all of which are imidazole acetol phosphate transaminases. The S. pombe his3 protein was 49.5% identical to the S. cerevisiae HIS5 protein and 21.5% identity was found when all four proteins were compared. The shuttle vector pBG1 was constructed by subcloning the smallest functional region of his3 and the S. pombe ars1 sequence into pUC18 for use in transformation of His3--S. pombe strains. New S. pombe strains in which the his3 gene was deleted have also been constructed.","authors":"Burke JD, Gould KL","authors_abbrev":"Burke JD et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_session_key":"0a40f4c64a0b82cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-22 10:47:25","canto_approved_date":"2020-07-07 15:57:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-22 10:47:17","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-22"},{"uniquename":"PMID:8695917","title":"Genetic analysis of the sam mutations, which induce sexual development with no requirement for nutritional starvation in fission yeast.","citation":"Biosci Biotechnol Biochem 1996 Jun;60(6):994-9","abstract":"The cAMP pathway and the Ras pathway are the two major pathways to sexual development in the fission yeast Schizosaccharomyces pombe. To understand the cAMP pathway or the related pathway, we analyzed mutants that display a phenotype similar to cyr1-, that is, hyper-sporulation. Nine mutants termed sam (sporulation abnormal mutant), which are highly inclined to sexual development despite the presence of nitrogen sources, were partially characterized. Cyclic AMP was detected in all nine sam mutant cells, and over-expression of the adenylyl cyclase gene (cyr1) failed to suppress the hyper-sporulation phenotype of these sam mutants, suggesting that none of the sam mutants were likely to be allelic to cyr1. Epistatic tests of sam mutants showed that they were divided into two dominant and seven recessive mutants. Dominants were able to make spores in sam/sam+ heterodiploid cells upon abundant nutrients. Both two dominant mutants bypassed the inability to make spores in ras1 deficient diploid cells, suppressed the deficiency to execute sporulation in byr2 deficient diploid cells, but failed to suppress the byr1 deficiency. Two dominant mutations seem not to occur within the byr2 gene.","authors":"Katayama S, Ozoe F, Kurokawa R, Tanaka K, Nakagawa T, Matsuda H, Kawamukai M","authors_abbrev":"Katayama S et al.","pubmed_publication_date":"Jun 1996","pubmed_entrez_date":"1996-06-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19542312","title":"Functional genomics of adhesion, invasion, and mycelial formation in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2009 Aug;8(8):1298-306","abstract":"Investigation into the switch between single-celled and filamentous forms of fungi may provide insights into cell polarity, differentiation, and fungal pathogenicity. At the molecular level, much of this investigation has fallen on two closely related budding yeasts, Candida albicans and Saccharomyces cerevisiae. Recently, the much more distant fission yeast Schizosaccharomyces pombe was shown to form invasive filaments after nitrogen limitation (E. Amoah-Buahin, N. Bone, and J. Armstrong, Eukaryot. Cell 4:1287-1297, 2005) and this genetically tractable organism provides an alternative system for the study of dimorphic growth. Here we describe a second mode of mycelial formation of S. pombe, on rich media. Screening of an S. pombe haploid deletion library identified 12 genes required for mycelial development which encode potential transcription factors, orthologues of S. cerevisiae Sec14p and Tlg2p, and the formin For3, among others. These were further grouped into two phenotypic classes representing different stages of the process. We show that galactose-dependent cell adhesion and actin assembly are both required for mycelial formation and mutants lacking a range of genes controlling cell polarity all produce mycelia but with radically altered morphology.","doi":"10.1128/EC.00078-09","authors":"Dodgson J, Avula H, Hoe KL, Kim DU, Park HO, Hayles J, Armstrong J","authors_abbrev":"Dodgson J et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-06-23","publication_year":"2009","canto_session_key":"fb6fc36eb3781b5f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-12-21 09:56:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-03 13:01:38","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_19542312_phaf.tsv"}],"genes":["SPAC23H3.13c","SPCC1223.06","SPBC1706.01","SPCC1494.10","SPAC3C7.12","SPBC106.10","SPBC21.05c","SPCC126.04c","SPCC895.05","SPAC18G6.15","SPBC19C7.02","SPAC23D3.09","SPCC1753.02c","SPBC1289.10c","SPBC32H8.07","SPAC3H8.10","SPBC19C7.03","SPBC215.04","SPAC823.05c","SPAC2F7.08c","SPBC30B4.03c","SPBC1604.20c","SPBC11B10.07c"],"gene_count":23,"ltp_gene_count":0,"approved_date":"2014-11-03"},{"uniquename":"PMID:30569039","title":"Mouse REC114 is essential for meiotic DNA double-strand break formation and forms a complex with MEI4.","citation":"Life Sci Alliance 2018 Dec;1(6):e201800259","abstract":"Programmed formation of DNA double-strand breaks (DSBs) initiates the meiotic homologous recombination pathway. This pathway is essential for proper chromosome segregation at the first meiotic division and fertility. Meiotic DSBs are catalyzed by Spo11. Several other proteins are essential for meiotic DSB formation, including three evolutionarily conserved proteins first identified in  Saccharomyces cerevisiae  (Mer2, Mei4, and Rec114). These three  S. cerevisiae  proteins and their mouse orthologs (IHO1, MEI4, and REC114) co-localize on the axes of meiotic chromosomes, and mouse IHO1 and MEI4 are essential for meiotic DSB formation. Here, we show that mouse  Rec114  is required for meiotic DSB formation. Moreover, MEI4 forms a complex with REC114 and IHO1 in mouse spermatocytes, consistent with cytological observations. We then demonstrated in vitro the formation of a stable complex between REC114 C-terminal domain and MEI4 N-terminal domain. We further determine the structure of the REC114 N-terminal domain that revealed similarity with Pleckstrin homology domains. These analyses provide direct insights into the architecture of these essential components of the meiotic DSB machinery.","doi":"10.26508/lsa.201800259","authors":"Kumar R, Oliver C, Brun C, Juarez-Martinez AB, Tarabay Y, Kadlec J, de Massy B","authors_abbrev":"Kumar R et al.","pubmed_publication_date":"Dec 2018","pubmed_entrez_date":"2018-12-21","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:25065","SPCC1753.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20118213","title":"Sterol regulatory element binding proteins in fungi: hypoxic transcription factors linked to pathogenesis.","citation":"Eukaryot Cell 2010 Mar;9(3):352-9","abstract":"Sterol regulatory element binding proteins (SREBPs) are membrane-bound transcription factors whose proteolytic activation is controlled by the cellular sterol concentration. Mammalian SREBPs are activated in cholesterol-depleted cells and serve to regulate cellular lipid homeostasis. Recent work demonstrates that SREBP is functionally conserved in fungi. While the ability to respond to sterols is conserved, fungal SREBPs are hypoxic transcription factors required for adaptation to a low-oxygen environment. In the fission yeast Schizosaccharomyces pombe, oxygen regulates the SREBP homolog Sre1 by independently controlling both its proteolytic activation and its degradation. SREBP is also required for adaptation to hypoxia in the human pathogens Cryptococcus neoformans and Aspergillus fumigatus. In these organisms, SREBP is required for virulence and resistance to antifungal drugs, making the SREBP pathway a potential target for antifungal therapy.","doi":"10.1128/EC.00358-09","authors":"Bien CM, Espenshade PJ","authors_abbrev":"Bien CM et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2010-02-02","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000059","title":"Representation of regulation in the Gene Ontology (molecular function) ","abstract":"We have created a standard template for the definition of classes for the regulation of a molecular function. This includes the definitions for positive and negative regulation. The equivalence axiom templates are \"GO:0065007 and 'regulates' some X\" (regulation), \"GO:0065007 and 'negatively_regulates' some X\" (negative regulation), and \"GO:0065007 and 'positively_regulates' some X\" (positive regulation), where X is a molecular function.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25806683","title":"Recombination occurs within minutes of replication blockage by RTS1 producing restarted forks that are prone to collapse.","citation":"Elife 2015 Mar 25;4:e04539","abstract":"The completion of genome duplication during the cell cycle is threatened by the presence of replication fork barriers (RFBs). Following collision with a RFB, replication proteins can dissociate from the stalled fork (fork collapse) rendering it incapable of further DNA synthesis unless recombination intervenes to restart replication. We use time-lapse microscopy and genetic assays to show that recombination is initiated within ∼ 10 min of replication fork blockage at a site-specific barrier in fission yeast, leading to a restarted fork within ∼ 60 min, which is only prevented/curtailed by the arrival of the opposing replication fork. The restarted fork is susceptible to further collapse causing hyper-recombination downstream of the barrier. Surprisingly, in our system fork restart is unnecessary for maintaining cell viability. Seemingly, the risk of failing to complete replication prior to mitosis is sufficient to warrant the induction of recombination even though it can cause deleterious genetic change.","doi":"10.7554/eLife.04539","authors":"Nguyen MO, Jalan M, Morrow CA, Osman F, Whitby MC","authors_abbrev":"Nguyen MO et al.","pubmed_publication_date":"25 Mar 2015","pubmed_entrez_date":"2015-03-26","publication_year":"2015","canto_session_key":"3e0b9737ed67db9f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-27 01:15:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26859269","title":"Posttranslational Regulation: A Way to Evolve.","citation":"Curr Biol 2016 Feb 08;26(3):R119-21","abstract":"A new study shows that differences in the regulation of lipin can account for the different strategies of nuclear division in two closely related fission yeast species.","doi":"10.1016/j.cub.2015.12.027","authors":"Prasad R, Barral Y","authors_abbrev":"Prasad R et al.","pubmed_publication_date":"08 Feb 2016","pubmed_entrez_date":"2016-02-10","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-02-11 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8049484","title":"Investigations into the control of cell form and polarity: the use of morphological mutants in fission yeast.","citation":"Dev Suppl 1993;:289-99","abstract":"The fission yeast has been extensively used for investigating the cell cycle and is now being used to initiate studies into the control of cell form. There are a number of factors contributing to the generation of polarity in this organism, which are closely linked with the control of the cell cycle, including the redistributions of cytoskeletal components throughout the cycle and their correlation with patterns of end growth seen at different cell cycle stages. The controlled positioning of elements such as the nucleus and septum with respect to other cellular structures in order to produce viable daughter cells is clearly an important part of the fission yeast life cycle. This review will describe work already published concerning the control of cell form in this organism, including the isolation of various mutants displaying abnormal polarity, and will introduce work currently in progress to identify new elements involved in this control.","authors":"Snell V, Nurse P","authors_abbrev":"Snell V et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30651569","title":"A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing.","citation":"Nat Commun 2019 Jan 16;10(1):251","abstract":"Gene regulatory mechanisms rely on a complex network of RNA processing factors to prevent untimely gene expression. In fission yeast, the highly conserved ortholog of human ERH, called Erh1, interacts with the YTH family RNA binding protein Mmi1 to form the Erh1-Mmi1 complex (EMC) implicated in gametogenic gene silencing. However, the structural basis of EMC assembly and its functions are poorly understood. Here, we present the co-crystal structure of the EMC that consists of Erh1 homodimers interacting with Mmi1 in a 2:2 stoichiometry via a conserved molecular interface. Structure-guided mutation of the Mmi1 Trp112  residue, which is required for Erh1 binding, causes defects in facultative heterochromatin assembly and gene silencing while leaving Mmi1-mediated transcription termination intact. Indeed, EMC targets masked in mmi1∆ due to termination defects are revealed in mmi1 W112A . Our study delineates EMC requirements in gene silencing and identifies an ERH interface required for interaction with an RNA binding protein.","doi":"10.1038/s41467-018-08273-9","authors":"Xie G, Vo TV, Thillainadesan G, Holla S, Zhang B, Jiang Y, Lv M, Xu Z, Wang C, Balachandran V, Shi Y, Li F, Grewal SIS","authors_abbrev":"Xie G et al.","pubmed_publication_date":"16 Jan 2019","pubmed_entrez_date":"2019-01-18","publication_year":"2019","canto_session_key":"7028528d63b6dda5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tommy Vo","canto_first_approved_date":"2023-11-19 11:30:42","canto_approved_date":"2023-11-19 17:56:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-19 11:26:26","canto_added_date":"2019-01-19 01:15:04","annotation_curators":[{"name":"Tommy Vo","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.12c","SPAC19G12.17"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-11-19","pdb_entries":[{"pdb_id":"6akj","gene_chains":[{"gene_uniquename":"SPAC19G12.17","chain":"A/B","position":"1-104"},{"gene_uniquename":"SPCC736.12c","chain":"A/B","position":"96-122"}],"title":"The crystal structure of EMC complex","entry_authors":"Li F","entry_authors_abbrev":"Li F","reference_uniquename":"PMID:30651569","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:41279293","title":"Long-read Sequencing of Nascent RNA from Budding and Fission Yeasts.","citation":"bioRxiv 2025 Oct 06;","abstract":"Gene expression requires DNA transcription and simultaneous RNA processing steps that transform the precursor RNA into fully mature RNA. In eukaryotes, the processing of protein-encoding messenger RNAs (mRNAs) includes 5' end capping, editing, splicing, RNA modification, poly-adenylation cleavage, and polyadenylation. Short-read sequencing of total or messenger RNA largely reveals the final output of transcription and processing because it utilizes 1) steady-state, mature RNA that is mostly processed and 2) sequencing reads that are too short to detect adjacent processing events (e.g. two adjacent introns). In contrast, long-read sequencing of nascent RNA allows the detection of rarer, full-length transcripts that are in the process of being transcribed and processed. The 3' end of each nascent RNA establishes the position of RNA polymerase II (Pol II) along the gene at the time of cell lysis, providing a 'timeline' for RNA processing events. In addition, the density of 3' ends along genes or at gene landmarks reflects Pol II density, which is related to changes in transcription elongation rate. In organisms with complex gene architectures, information about splicing across multiple introns within the same transcript can be extracted, as well as the location of transcription start sites (TSSs) and polyA cleavage sites. Here, we describe the isolation of nascent RNA from the yeasts  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe  , preparation of a cDNA library for long-read sequencing on Oxford Nanopore Technologies or Pacific Biosciences platforms, and initial data analysis steps. These methods comprise versatile and powerful tools for the investigation of coupled RNA synthesis and processing.","doi":"10.1101/2025.10.06.680282","authors":"Robik KD, Alpert T, Reimer KA, Bech P, Herzel L, Schärfen L, Straube K, Neugebauer KM","authors_abbrev":"Robik KD et al.","pubmed_publication_date":"06 Oct 2025","pubmed_entrez_date":"2025-11-24","publication_year":"2025","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2025-11-25 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9105045","title":"cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin.","citation":"J Cell Biol 1997 Apr 07;137(1):169-82","abstract":"As in many other eukaryotic cells, cell division in fission yeast depends on the assembly of an actin ring that circumscribes the middle of the cell. Schizosaccharomyces pombe cdc12 is an essential gene necessary for actin ring assembly and septum formation. Here we show that cdc12p is a member of a family of proteins including Drosophila diaphanous, Saccharomyces cerevisiae BNI1, and S. pombe fus1, which are involved in cytokinesis or other actin-mediated processes. Using indirect immunofluorescence, we show that cdc12p is located in the cell division ring and not in other actin structures. When overexpressed, cdc12p is located at a medial spot in interphase that anticipates the future ring site. cdc12p localization is altered in actin ring mutants. cdc8 (tropomyosin homologue), cdc3 (profilin homologue), and cdc15 mutants exhibit no specific cdc12p staining during mitosis. cdc4 mutant cells exhibit a medial cortical cdc12p spot in place of a ring. mid1 mutant cells generally exhibit a cdc12p spot with a single cdc12p strand extending in a random direction. Based on these patterns, we present a model in which ring assembly originates from a single point on the cortex and in which a molecular pathway for the functions of cytokinesis proteins is suggested. Finally, we found that cdc12 and cdc3 mutants show a synthetic-lethal genetic interaction, and a proline-rich domain of cdc12p binds directly to profilin cdc3p in vitro, suggesting that one function of cdc12p in ring assembly is to bind profilin.","authors":"Chang F, Drubin D, Nurse P","authors_abbrev":"Chang F et al.","pubmed_publication_date":"07 Apr 1997","pubmed_entrez_date":"1997-04-07","publication_year":"1997","canto_session_key":"7ced7ee21306a509","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-09-17 14:33:13","canto_approved_date":"2020-01-22 14:30:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-04 15:54:30","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.15c","SPAC1F5.04c","SPCC4B3.15","SPAC27F1.02c","SPAP8A3.08","SPAC20G8.05c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-09-17"},{"uniquename":"PMID:35622906","title":"Distribution of γ-tubulin ring complex at the  Schizosaccharomyces pombe  spindle pole.","citation":"MicroPubl Biol 2021;2021","abstract":"Microtubule nucleation is mediated by the conserved γ-tubulin ring complex (γ-TuRC). Using super-resolution microscopy, we investigate the distribution of γ-TuRC components at the spindle pole body (SPB) in wild-type  Schizosaccharomyces pombe  . We observed asymmetric distribution of γ-TuRC on its nuclear and cytoplasmic surfaces, consistent with the uneven distribution of microtubules. Examination of deletion mutants in the three non-essential γ-TuRC subunits showed defects in γ-TuRC accumulation on the old and new SPB, particularly in cells lacking  alp16+   (the Gcp6 ortholog) that may explain the monopolar spindles observed in this mutant upon mitotic entry.","doi":"10.17912/micropub.biology.000464","authors":"Saha S, Unruh JR, Jaspersen SL","authors_abbrev":"Saha S et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2022-05-27","publication_year":"2021","canto_session_key":"57009ca6a21af022","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-07-14 08:34:11","canto_approved_date":"2022-07-14 08:34:12","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-07-14 07:56:23","canto_added_date":"2022-05-29 00:15:04","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":3,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC211.06","SPCC4G3.19","SPBC365.15"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2022-07-14"},{"uniquename":"PMID:10923022","title":"Mutations in the large subunit of U2AF disrupt pre-mRNA splicing, cell cycle progression and nuclear structure.","citation":"Yeast 2000 Aug;16(11):1001-13","abstract":"The prp2 gene of fission yeast has previously been shown to encode the large subunit of the splicing factor spU2AF. SpU2AF(59) is an evolutionarily conserved protein that has an arginine/serine-rich region and three RNA recognition motifs (RRMs). We have sequenced three temperature-sensitive alleles of prp2 and determined that the mutations result in single amino acid changes within one of the RRMs or between RRMs. All mutant alleles of prp2 have pre-mRNA splicing defects at the non-permissive temperature. Although the mutant strains are growth-arrested at 37 degrees C, they do not elongate like typical fission yeast cell cycle mutants. The DNA of the prp2(-) strains stains more intensely than a wild-type strain, suggesting that the chromatin may be condensed. Ultrastructural studies show differences in the mutant nuclei including a prominent distinction between the chromatin- and non-chromatin-enriched regions compared to the more homogenous wild-type nucleus. Two-hybrid assays indicate that some of the wild-type protein interactions are altered in the mutant strains. These results suggest that normal functioning of spU2AF(59) may be essential not only for pre-mRNA splicing but also for the maintenance of proper nuclear structure and normal cell cycle progression.","authors":"Beales M, Flay N, McKinney R, Habara Y, Ohshima Y, Tani T, Potashkin J","authors_abbrev":"Beales M et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2000-08-03","publication_year":"2000","canto_session_key":"d5d0ef3568cea1fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-21 14:12:30","canto_approved_date":"2021-11-10 12:25:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-21 14:12:23","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":41,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC962.06c","SPAC27F1.09c","SPBC1289.02c","SPBC146.07","SPAC2G11.14","SPAP8A3.06"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2014-08-21"},{"uniquename":"PMID:20980525","title":"Determinants that specify the integration pattern of retrotransposon Tf1 in the fbp1 promoter of Schizosaccharomyces pombe.","citation":"J Virol 2011 Jan;85(1):519-29","abstract":"Long terminal repeat (LTR) retrotransposons are closely related to retroviruses and, as such, are important models for the study of viral integration and target site selection. The transposon Tf1 of Schizosaccharomyces pombe integrates with a strong preference for the promoters of polymerase II (Pol II)-transcribed genes. Previous work in vivo with plasmid-based targets revealed that the patterns of insertion were promoter specific and highly reproducible. To determine which features of promoters are recognized by Tf1, we studied integration in a promoter that has been characterized. The promoter of fbp1 has two upstream activating sequences, UAS1 and UAS2. We found that integration was targeted to two windows, one 180 nucleotides (nt) upstream and the other 30 to 40 nt downstream of UAS1. A series of deletions in the promoter showed that the integration activities of these two regions functioned autonomously. Integration assays of UAS2 and of a synthetic promoter demonstrated that strong promoter activity alone was not sufficient to direct integration. The factors that modulate the transcription activities of UAS1 and UAS2 include the activators Atf1p, Pcr1p, and Rst2p as well as the repressors Tup11p, Tup12p, and Pka1p. Strains lacking each of these proteins revealed that Atf1p alone mediated the sites of integration. These data indicate that Atf1p plays a direct and specific role in targeting integration in the promoter of fbp1.","doi":"10.1128/JVI.01719-10","authors":"Majumdar A, Chatterjee AG, Ripmaster TL, Levin HL","authors_abbrev":"Majumdar A et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-10-29","publication_year":"2011","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30810475","title":"Early splicing functions of fission yeast Prp16 and its unexpected requirement for gene Silencing is governed by intronic features.","citation":"RNA Biol 2019 Jun;16(6):754-769","abstract":"Prp16 is a DEAH box pre-mRNA splicing factor that triggers a key spliceosome conformational switch to facilitate second step splicing in Saccharomyces cerevisiae. However, Prp16 functions are largely unexplored in Schizosaccharomyces pombe, an attractive model with exon-intron architecture more relevant to several other eukaryotes. Here, we generated mis-sense alleles in SpPrp16 whose consequences on genome-wide splicing uncover its nearly global splicing role with only a small subset of unaffected introns. Prp16 dependent and independent intron categories displayed a striking difference in the strength of intronic 5' splice site (5'SS)-U6 snRNA and branch site (BS)-U2 snRNA interactions. Selective weakening of these interactions could convert a Prp16 dependent intron into an independent one. These results point to the role of SpPrp16 in destabilizing 5'SS-U6snRNA and BS-U2snRNA interactions which plausibly trigger structural alterations in the spliceosome to facilitate first step catalysis. Our data suggest that SpPrp16 interactions with early acting factors, its enzymatic activities and association with intronic elements collectively account for efficient and accurate first step catalysis. In addition to splicing derangements in the spprp16F528S mutant, we show that SpPrp16 influences cell cycle progression and centromeric heterochromatinization. We propose that strong 5'SS-U6 snRNA and BS-U2 snRNA complementarity of intron-like elements in non-coding RNAs which lead to complete splicing arrest and impaired Seb1 functions at the pericentromeric loci may cumulatively account for the heterochromatin defects in spprp16F528S cells. These findings suggest that the diverse Prp16 functions within a genome are likely governed by its intronic features that influence splice site-snRNA interaction strength.","doi":"10.1080/15476286.2019.1585737","authors":"Vijayakumari D, Sharma AK, Bawa PS, Kumar R, Srinivasan S, Vijayraghavan U","authors_abbrev":"Vijayakumari D et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-02-28","publication_year":"2019","canto_session_key":"8c7b04a443ae9d43","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Drisya Vijayakumari","canto_first_approved_date":"2019-07-07 21:08:31","canto_approved_date":"2026-01-29 13:06:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-27 15:14:30","canto_added_date":"2019-03-01 01:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":40,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Drisya Vijayakumari","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC215.12","SPNCRNA.362","SPBC19C2.01","SPAC144.06","SPBC19G7.17","SPBC1711.17","SPNCRNA.232","SPNCRNA.231","SPBC119.18","SPNCRNA.230","SPBC26H8.07c","SPAC222.09","SPAC29E6.08","SPAC10F6.02c","SPCC1235.15","SPAC17A5.02c","SPCC736.11"],"gene_count":17,"ltp_gene_count":6,"approved_date":"2019-07-07"},{"uniquename":"PMID:22274912","title":"Identification and mechanistic studies of a novel ubiquitin E1 inhibitor.","citation":"J Biomol Screen 2012 Apr;17(4):421-34","abstract":"Protein degradation via the ubiquitin-proteasome pathway is important for a diverse number of cellular processes ranging from cell signaling to development. Disruption of the ubiquitin pathway occurs in a variety of human diseases, including several cancers and neurological disorders. Excessive proteolysis of tumor suppressor proteins, such as p27, occurs in numerous aggressive human tumors. To discover small-molecule inhibitors that potentially prevent p27 degradation, we developed a series of screening assays, including a cell-based screen of a small-molecule compound library and two novel nucleotide exchange assays. Several small-molecule inhibitors, including NSC624206, were identified and subsequently verified to prevent p27 ubiquitination in vitro. The mechanism of NSC624206 inhibition of p27 ubiquitination was further unraveled using the nucleotide exchange assays and shown to be due to antagonizing ubiquitin activating enzyme (E1). We determined that NSC624206 and PYR-41, a recently reported inhibitor of ubiquitin E1, specifically block ubiquitin-thioester formation but have no effect on ubiquitin adenylation. These studies reveal a novel E1 inhibitor that targets a specific step of the E1 activation reaction. NSC624206 could, therefore, be potentially useful for the control of excessive ubiquitin-mediated proteolysis in vivo.","doi":"10.1177/1087057111433843","authors":"Ungermannova D, Parker SJ, Nasveschuk CG, Chapnick DA, Phillips AJ, Kuchta RD, Liu X","authors_abbrev":"Ungermannova D et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-01-26","publication_year":"2012","canto_session_key":"07959b62da8057a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-03-11 17:32:24","canto_approved_date":"2023-03-11 17:32:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-11 17:32:12","canto_added_date":"2023-02-21 19:07:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1604.21c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2023-03-11"},{"uniquename":"PMID:36200871","title":"Membrane stretching activates calcium permeability of a putative channel Pkd2 during fission yeast cytokinesis.","citation":"Mol Biol Cell 2022 Dec 01;33(14):ar134","abstract":"Pkd2 is the fission yeast homologue of polycystins. This putative ion channel localizes to the plasma membrane. It is required for the expansion of cell volume during interphase growth and cytokinesis, the last step of cell division. However, the channel activity of Pkd2 remains untested. Here, we examined the calcium permeability and mechanosensitivity of Pkd2 through in vitro reconstitution and calcium imaging of  pkd2  mutant cells. Pkd2 was translated and inserted into the lipid bilayers of giant unilamellar vesicles using a cell-free expression system. The reconstituted Pkd2 permeated calcium when the membrane was stretched via hypoosmotic shock. In vivo, inactivation of Pkd2 through a temperature-sensitive mutation  pkd2-B42  reduced the average intracellular calcium level by 34%. Compared with the wild type, the hypomorphic mutation  pkd2-81KD  reduced the amplitude of hypoosmotic shock-triggered calcium spikes by 59%. During cytokinesis, mutations of  pkd2  reduced the calcium spikes, accompanying cell separation and the ensuing membrane stretching, by 60%. We concluded that fission yeast polycystin Pkd2 allows calcium influx when activated by membrane stretching, representing a likely mechanosensitive channel that contributes to the cytokinetic calcium spikes.","doi":"10.1091/mbc.E22-07-0248","authors":"Poddar A, Hsu YY, Zhang F, Shamma A, Kreais Z, Muller C, Malla M, Ray A, Liu AP, Chen Q","authors_abbrev":"Poddar A et al.","pubmed_publication_date":"01 Dec 2022","pubmed_entrez_date":"2022-10-06","publication_year":"2022","canto_session_key":"b897e8a27ea98541","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Qian Chen","canto_first_approved_date":"2023-02-03 15:02:15","canto_approved_date":"2024-05-16 13:30:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-02 21:06:31","canto_added_date":"2022-10-08 00:15:04","annotation_curators":[{"name":"Qian Chen","community_curator":true,"annotation_count":4,"orcid":"0000-0002-2768-6570","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPAC821.12","SPAC1F7.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-02-03"},{"uniquename":"PMID:21900503","title":"The Pot1a-associated proteins Tpt1 and Pat1 coordinate telomere protection and length regulation in Tetrahymena.","citation":"Mol Biol Cell 2011 Nov;22(21):4161-70","abstract":"We have identified two new telomere proteins, Tpt1 and Pat1, from the ciliate Tetrahymena thermophila. Although Tetrahymena telomerase is well characterized, only one telomere protein had previously been identified. This was the G-overhang binding-protein Pot1a. Tpt1 and Pat1 were isolated as Pot1a binding partners and shown to localize to telomeres. As Tpt1 and Pat1 were both found to be essential, conditional cell lines were generated to explore their function. Tpt1 depletion caused a rapid growth arrest and telomere elongation in the absence of cell division. The phenotype was similar to that seen after Pot1a depletion suggesting that Tpt1 and Pot1a function together to regulate telomere length and prevent telomere deprotection. In contrast, Pat1 depletion had a modest effect on cell growth but caused progressive telomere shortening similar to that observed upon TERT depletion. Thus Pat1 appears to be needed for telomerase to maintain the chromosome terminus. Analysis of Pot1a-Tpt1-Pat1 complex formation using purified proteins indicated that Tpt1 interacts directly with Pot1a while Pat1 interacts with Tpt1. Our results indicate that Tpt1 is the Tetrahymena equivalent of mammalian TPP1, Schizosaccharomyces pombe Tpz1, and Oxytricha nova TEBPβ.","doi":"10.1091/mbc.E11-06-0551","authors":"Linger BR, Morin GB, Price CM","authors_abbrev":"Linger BR et al.","pubmed_publication_date":"Nov 2011","pubmed_entrez_date":"2011-09-09","publication_year":"2011","canto_session_key":"4a881356cc658169","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-12-15 22:05:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-15 22:05:06","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-12-15"},{"uniquename":"PMID:20967237","title":"Fission yeast cells undergo nuclear division in the absence of spindle microtubules.","citation":"PLoS Biol 2010 Oct 12;8(10):e1000512","abstract":"Mitosis in eukaryotic cells employs spindle microtubules to drive accurate chromosome segregation at cell division. Cells lacking spindle microtubules arrest in mitosis due to a spindle checkpoint that delays mitotic progression until all chromosomes have achieved stable bipolar attachment to spindle microtubules. In fission yeast, mitosis occurs within an intact nuclear membrane with the mitotic spindle elongating between the spindle pole bodies. We show here that in fission yeast interference with mitotic spindle formation delays mitosis only briefly and cells proceed to an unusual nuclear division process we term nuclear fission, during which cells perform some chromosome segregation and efficiently enter S-phase of the next cell cycle. Nuclear fission is blocked if spindle pole body maturation or sister chromatid separation cannot take place or if actin polymerization is inhibited. We suggest that this process exhibits vestiges of a primitive nuclear division process independent of spindle microtubules, possibly reflecting an evolutionary intermediate state between bacterial and Archeal chromosome segregation where the nucleoid divides without a spindle and a microtubule spindle-based eukaryotic mitosis.","doi":"10.1371/journal.pbio.1000512","authors":"Castagnetti S, Oliferenko S, Nurse P","authors_abbrev":"Castagnetti S et al.","pubmed_publication_date":"12 Oct 2010","pubmed_entrez_date":"2010-10-23","publication_year":"2010","canto_session_key":"439dbaa9865b09a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-09-30 15:56:55","canto_approved_date":"2022-08-29 18:03:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-03 13:36:31","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":27,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.03c","SPBC26H8.07c","SPBC12D12.01","SPAC1F5.04c","SPAC4A8.15c","SPAC27F1.04c","SPAP8A3.08","SPBC11C11.03","SPAC25G10.07c","SPBC21.06c","SPBC20F10.06","SPAC1782.09c","SPBC800.05c","SPAC27F1.02c","SPAC24H6.05","SPCC1739.11c","SPAC1786.03","SPCC5E4.04","SPBC409.06"],"gene_count":19,"ltp_gene_count":11,"approved_date":"2021-09-30"},{"uniquename":"PMID:22087580","title":"Spindles and active vortices in a model of confined filament-motor mixtures.","citation":"BMC Biophys 2011 Nov 16;4:18","abstract":"Robust self-organization of subcellular structures is a key principle governing the dynamics and evolution of cellular life. In fission yeast cells undergoing division, the mitotic spindle spontaneously emerges from the interaction of microtubules, motor proteins and the confining cell walls, and asters and vortices have been observed to self-assemble in quasi-two dimensional microtubule-kinesin assays. There is no clear microscopic picture of the role of the active motors driving this pattern formation, and the relevance of continuum modeling to filament-scale structures remains uncertain.\nHere we present results of numerical simulations of a discrete filament-motor protein model confined to a pressurised cylindrical box. Stable spindles, nematic configurations, asters and high-density semi-asters spontaneously emerge, the latter pair having also been observed in cytosol confined within emulsion droplets. State diagrams are presented delineating each stationary state as the pressure, motor speed and motor density are varied. We further highlight a parameter regime where vortices form exhibiting collective rotation of all filaments, but have a finite life-time before contracting to a semi-aster. Quantifying the distribution of life-times suggests this contraction is a Poisson process. Equivalent systems with fixed volume exhibit persistent vortices with stochastic switching in the direction of rotation, with switching times obeying similar statistics to contraction times in pressurised systems. Furthermore, we show that increasing the detachment rate of motors from filament plus-ends can both destroy vortices and turn some asters into vortices.\nWe have shown that discrete filament-motor protein models provide new insights into the stationary and dynamical behavior of active gels and subcellular structures, because many phenomena occur on the length-scale of single filaments. Based on our findings, we argue the need for a deeper understanding of the microscopic activities underpinning macroscopic self-organization in active gels and urge further experiments to help bridge these lengths.","doi":"10.1186/2046-1682-4-18","authors":"Head DA, Briels W, Gompper G","authors_abbrev":"Head DA et al.","pubmed_publication_date":"16 Nov 2011","pubmed_entrez_date":"2011-11-18","publication_year":"2011","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18408053","title":"Rtr1 is the Saccharomyces cerevisiae homolog of a novel family of RNA polymerase II-binding proteins.","citation":"Eukaryot Cell 2008 Jun;7(6):938-48","abstract":"Cells must rapidly sense and respond to a wide variety of potentially cytotoxic external stressors to survive in a constantly changing environment. In a search for novel genes required for stress tolerance in Saccharomyces cerevisiae, we identified the uncharacterized open reading frame YER139C as a gene required for growth at 37 degrees C in the presence of the heat shock mimetic formamide. YER139C encodes the closest yeast homolog of the human RPAP2 protein, recently identified as a novel RNA polymerase II (RNAPII)-associated factor. Multiple lines of evidence support a role for this gene family in transcription, prompting us to rename YER139C RTR1 (regulator of transcription). The core RNAPII subunits RPB5, RPB7, and RPB9 were isolated as potent high-copy-number suppressors of the rtr1Delta temperature-sensitive growth phenotype, and deletion of the nonessential subunits RPB4 and RPB9 hypersensitized cells to RTR1 overexpression. Disruption of RTR1 resulted in mycophenolic acid sensitivity and synthetic genetic interactions with a number of genes involved in multiple phases of transcription. Consistently, rtr1Delta cells are defective in inducible transcription from the GAL1 promoter. Rtr1 constitutively shuttles between the cytoplasm and nucleus, where it physically associates with an active RNAPII transcriptional complex. Taken together, our data reveal a role for members of the RTR1/RPAP2 family as regulators of core RNAPII function.","doi":"10.1128/EC.00042-08","authors":"Gibney PA, Fries T, Bailer SM, Morano KA","authors_abbrev":"Gibney PA et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-15","publication_year":"2008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23A1.16c","HGNC:25791"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8462872","title":"Sequence of the Schizosaccharomyces pombe gtp1 gene and identification of a novel family of putative GTP-binding proteins.","citation":"Gene 1993 Mar 30;125(2):191-3","abstract":"A new gene, gtp1, has been identified by sequence analysis in Schizosaccharomyces pombe. The open reading frame was identified downstream from the stf1 locus. The deduced GTP1 protein has strong sequence similarity to a family of putative GTP-binding proteins from Halobacterium cutirubrum, Bacillus subtilis, Drosophila melanogaster and mouse. The conserved P-loop phosphate-binding motif places gtp1 in a family separate from previously described groups of such proteins.","authors":"Hudson JD, Young PG","authors_abbrev":"Hudson JD et al.","pubmed_publication_date":"30 Mar 1993","pubmed_entrez_date":"1993-03-30","publication_year":"1993","canto_session_key":"3a9e97e0b037dd77","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 22:22:53","canto_approved_date":"2018-12-22 22:22:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 22:22:45","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:24297439","title":"Sck1 negatively regulates Gpa2-mediated glucose signaling in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2014 Feb;13(2):202-8","abstract":"Schizosaccharomyces pombe detects extracellular glucose via a G protein-mediated cyclic AMP (cAMP)-signaling pathway activating protein kinase A (PKA) and regulating transcription of genes involved in metabolism and sexual development. In this pathway, Gpa2 Gα binds to and activates adenylyl cyclase in response to glucose detection by the Git3 G protein-coupled receptor. Using a two-hybrid screen to identify extrinsic regulators of Gpa2, we isolated a clone that expresses codons 471 to 696 of the Sck1 kinase, which appears to display a higher affinity for Gpa2(K270E)-activated Gα relative to Gpa2(+) Gα. Deletion of sck1(+) or mutational inactivation of the Sck1 kinase produces phenotypes reflecting increased PKA activity in strains expressing Gpa2(+) or Gpa2(K270E), suggesting that Sck1 negatively regulates PKA activation through Gpa2. In contrast to the Gpa2(K270E) GDP-GTP exchange rate mutant, GTPase-defective Gpa2(R176H) weakly binds Sck1 in the two-hybrid screen and a deletion of sck1(+) in a Gpa2(R176H) strain confers phenotypes consistent with a slight reduction in PKA activity. Finally, deleting sck1(+) in a gpa2Δ strain results in phenotypes consistent with a second role for Sck1 acting in parallel with PKA. In addition to this parallel role with PKA, our data suggest that Sck1 negatively regulates Gpa2, possibly targeting the nucleotide-free form of the protein that may expose the one and only AKT/PKB consensus site in Gpa2 for Sck1 to bind. This dual role for Sck1 may allow S. pombe to produce distinct biological responses to glucose and nitrogen starvation signals that both activate the Wis1-Spc1/StyI stress-activated protein kinase (SAPK) pathway.","doi":"10.1128/EC.00277-13","authors":"Mudge DK, Yang F, Currie BM, Kim JM, Yeda K, Bashyakarla VK, Ivey FD, Hoffman CS","authors_abbrev":"Mudge DK et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-12-04","publication_year":"2014","canto_session_key":"037e100417a6b899","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Charlie Hoffman","canto_first_approved_date":"2017-07-26 15:18:55","canto_approved_date":"2025-06-12 05:55:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-02 11:44:10","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Charlie Hoffman","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPAC23H3.13c","SPBC1198.14c","SPCC1753.02c","SPAC1B9.02c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-07-26"},{"uniquename":"PMID:1766866","title":"The ste4+ gene, essential for sexual differentiation of Schizosaccharomyces pombe, encodes a protein with a leucine zipper motif.","citation":"Nucleic Acids Res 1991 Dec;19(25):7043-7","abstract":"Ste4- mutants of Schizosaccharomyces pombe are unable to undergo both mating and meiosis. We have cloned the ste4+ gene and its cDNA. The gene encodes a 264 amino acid protein with a typical leucine zipper motif homologous with the jun family. However, unlike the jun family, this protein does not have a typical basic region that precedes the leucine zipper. The transcription of this gene absolutely depends on the ste11+ gene and increases several fold upon nitrogen starvation, a general signal for sexual differentiation. Whereas ste4+ is essential for mating and meiosis, its overexpression inhibits these processes.","authors":"Okazaki N, Okazaki K, Tanaka K, Okayama H","authors_abbrev":"Okazaki N et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"bfb885d23d7654df","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-02-08 14:28:54","canto_approved_date":"2022-07-22 14:34:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-01 09:38:14","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1565.04c","SPBC32C12.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-02-08"},{"uniquename":"PMID:9337070","title":"Interaction of the DNA topoisomerase II catalytic inhibitor meso-2,3-bis(3,5-dioxopiperazine-1-yl)butane (ICRF-193), a bisdioxopiperazine derivative, with the conserved region(s) of eukaryotic but not prokaryotic enzyme.","citation":"Biochem Pharmacol 1997 Sep 01;54(5):545-50","abstract":"ICRF-193 [meso-2,3-bis(3,5-dioxopiperazine-1-yl)butane], a bisdioxopiperazine compound, has been shown to be a catalytic inhibitor of DNA topoisomerase II by stabilizing the enzyme in the form of a closed \"protein clamp,\" an intermediate form in the catalytic cycle (Roca et al., Proc Natl Acad Sci USA 91: 1781-1785, 1994). In view of its usefulness as a probe in the functional analysis of the enzyme, we tried further to define the domain(s) of the enzyme interacting with the drug by examining its inhibitory activity on type II topoisomerases from various species of eukaryotes and prokaryotes. ICRF-193 inhibited the enzyme from yeast, fly, frog, plant, and mammals at IC50 values in the range of 1-13 microM. Experiments using fission yeast truncated mutant type II enzyme lacking both amino-terminal 74 amino acids and carboxy-terminal 265 amino acids revealed that ICRF-193 interacts with the 125 kDa \"core\" polypeptide of the enzyme. In contrast, prokaryotic type II enzymes, Escherichia coli DNA gyrase, topo IV, and phage T4 topo, were not affected by the drug. From these results, the domain(s) common to eukaryotic but not to prokaryotic type II enzymes interacting with ICRF-193 was speculated.","authors":"Sato M, Ishida R, Narita T, Kato J, Ikeda H, Fukazawa H, Andoh T","authors_abbrev":"Sato M et al.","pubmed_publication_date":"01 Sep 1997","pubmed_entrez_date":"1997-10-23","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20936170","title":"Early Steps in the DNA Base Excision Repair Pathway of a Fission Yeast Schizosaccharomyces pombe.","citation":"J Nucleic Acids 2010 Sep 16;2010","abstract":"DNA base excision repair (BER) accounts for maintaining genomic integrity by removing damaged bases that are generated endogenously or induced by genotoxic agents. In this paper, we describe the roles of enzymes functioning in the early steps of BER in fission yeast. Although BER is an evolutionarily conserved process, some unique features of the yeast repair pathway were revealed by genetic and biochemical approaches. AP sites generated by monofunctional DNA glycosylases are incised mainly by AP lyase activity of Nth1p, a sole bifunctional glycosylase in yeast, to leave a blocked 3' end. The major AP endonuclease Apn2p functions predominantly in removing the 3' block. Finally, a DNA polymerase fills the gap, and a DNA ligase seals the nick (Nth1p-dependent or short patch BER). Apn1p backs up Apn2p. In long patch BER, Rad2p endonuclease removes flap DNA containing a lesion after DNA synthesis. A UV-specific endonuclease Uve1p engages in an alternative pathway by nicking DNA on the 5' side of oxidative damage. Nucleotide excision repair and homologous recombination are involved in repair of BER intermediates including the AP site and single-strand break with the 3' block. Other enzymes working in 3' end processing are also discussed.","doi":"10.4061/2010/450926","authors":"Kanamitsu K, Ikeda S","authors_abbrev":"Kanamitsu K et al.","pubmed_publication_date":"16 Sep 2010","pubmed_entrez_date":"2010-10-12","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20133687","title":"Synergistic roles of the proteasome and autophagy for mitochondrial maintenance and chronological lifespan in fission yeast.","citation":"Proc Natl Acad Sci U S A 2010 Feb 23;107(8):3540-5","abstract":"Regulations of proliferation and quiescence in response to nutritional cues are important for medicine and basic biology. The fission yeast Schizosaccharomyces pombe serves as a model, owing to the shift of proliferating cells to the metabolically active quiescence (designate G0 phase hereafter) by responding to low nitrogen source. S. pombe G0 phase cells keep alive for months without growth and division. Nitrogen replenishment reinstates vegetative proliferation phase (designate VEG). Some 40 genes required for G0 maintenance were identified, but many more remain to be identified. We here show, using mutants, that the proteasome is required for maintaining G0 quiescence. Functional outcomes of proteasome in G0 and VEG phases appear to be distinct. Upon proteasome dysfunction, a number of antioxidant proteins and compounds responsive to ROS (reactive oxygen species) are produced. In addition, autophagy-mediated destruction of mitochondria occurs, which suppresses the loss of viability by eliminating ROS-generating mitochondria. These defensive responses are found in G0 but not in VEG, suggesting that the main function of proteasome in G0 phase homeostasis is to minimize ROS. Proteasome and autophagy are thus collaborative to support the lifespan of S. pombe G0 phase.","doi":"10.1073/pnas.0911055107","authors":"Takeda K, Yoshida T, Kikuchi S, Nagao K, Kokubu A, Pluskal T, Villar-Briones A, Nakamura T, Yanagida M","authors_abbrev":"Takeda K et al.","pubmed_publication_date":"23 Feb 2010","pubmed_entrez_date":"2010-02-06","publication_year":"2010","canto_session_key":"e6d5e590b3725826","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-28 10:42:41","canto_approved_date":"2026-01-29 11:54:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-22 15:24:05","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":75,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1420.03","SPAC31G5.13","SPCC1682.16","SPAC3A11.12c","SPAC607.05","SPBC119.01","SPBP8B7.24c","SPAC22F8.06","SPAC4A8.13c","SPBC16C6.07c","SPMIT.11","SPBC582.03","SPAC23D3.07","SPBP19A11.03c","SPAC6G10.04c","SPBC577.10","SPAC17H9.12c","SPBC582.07c","SPBC4.07c","SPBC646.16","SPCC63.12c","SPBC4C3.10c","SPAC637.10c","SPAC140.01","SPAC1782.01","SPBC23G7.12c","SPAPB8E5.02c","SPAC31A2.04c","SPAC323.02c","SPCC16A11.16c","SPBC16G5.01","SPBC409.06","SPAC1805.17","SPAC13C5.01c","SPAC17C9.13c","SPBC106.16","SPCC576.10c","SPAC31G5.14","SPCC14G10.03c","SPBC56F2.12","SPBC342.04","SPCC1442.06","SPCC1682.10","SPCC1795.04c","SPAC23G3.11","SPBC17D11.07c"],"gene_count":46,"ltp_gene_count":39,"approved_date":"2017-06-28"},{"uniquename":"GO_REF:0000051","title":"S. pombe keyword mapping","abstract":"Keywords derived from manually curated primary annotation, e.g. gene product descriptions, are mapped to GO terms. Annotations made by this method have the evidence code Non-traceable Author Statement (NAS), and are filtered from the PomBase annotation files wherever another annotation exists that is equally or more specific, and supported by experimental or manually evaluated comparative evidence (such as ISS and its subtypes). Formerly GOC:pombekw2GO.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1A6.09c","SPBP8B7.07c","SPAC644.06c","SPBC17A3.06","SPCC70.09c","SPBC725.14","SPAC1142.07c","SPBC646.13","SPAC23G3.02c","SPSNRNA.04","SPBC3E7.10","SPAC17A2.06c","SPBP23A10.06","SPBC1D7.03","SPAC3F10.16c","SPCC16C4.12","SPBC660.15","SPBC16H5.06","SPBC32F12.06","SPAC25G10.01","SPAC869.08","SPCC965.07c","SPMTR.02","SPBC1921.05","SPAC3G9.04","SPAPB8E5.09","SPAC644.14c","SPBC27B12.14","SPCC622.09","SPCC18.01c","SPAC3A11.12c","SPAC140.01","SPAC664.15","SPAC1A6.01c","SPBC1778.09","SPBC23G7.12c","SPCC1393.02c","SPCC970.08","SPCC830.10","SPAC26F1.02","SPCC2H8.04","SPBC18H10.15","SPBC14C8.03","SPAC1834.03c","SPBC646.14c","SPCC663.18","SPBC428.16c","SPAC3A12.12","SPBC16G5.13","SPBC19C2.05","SPAC2C4.04c","SPCC1795.02c","SPBC646.07c","SPAC823.15","SPAC19B12.05c","SPBC1271.12","SPAC20G4.02c","SPAC17G6.06","SPAC29E6.06c","SPAC27E2.10c","SPBC16E9.17c","SPAC1B2.02c","SPAC328.01c","SPAC22G7.02","SPBC28F2.11","SPAC1527.01","SPAC4G9.06c","SPAC1D4.11c","SPBC2G2.14","SPCC1672.05c","SPAC890.03","SPBC23G7.17c","SPBC577.14c","SPAC23D3.02","SPAC23A1.07","SPCC162.11c","SPBC1709.13c","SPAC23A1.12c","SPAC6F12.11c","SPAC3H5.04","SPAC922.03","SPAC30D11.10","SPAC24C9.09","SPBC27B12.10c","SPAC56E4.03","SPCC320.05","SPAC1B2.05","SPMTR.01","SPBC1734.14c","SPAC212.12","SPBC17G9.07","SPBC337.08c","SPAC6C3.08","SPBC646.08c","SPAC22E12.09c","SPAC15A10.12c","SPAC4F10.04","SPAC1556.08c","SPAC22H10.09","SPBC25B2.09c","SPAC14C4.14","SPBC577.06c","SPBC354.07c","SPBC2G2.11","SPBC1734.05c","SPAC1705.03c","SPAC11E3.06","SPAC13G6.10c","SPAC5D6.07c","SPBC215.01","SPBC902.02c","SPBC365.16","SPBC12D12.07c","SPCC306.11","SPBC146.08c","SPCC965.04c","SPCC24B10.16c","SPAC26F1.13c","SPBC15D4.06","SPBC1683.05","SPBC30D10.07c","SPBC29A10.04","SPAC2F3.06c","SPBC428.15","SPCC576.10c","SPAC19G12.07c","SPBC1826.01c","SPCC1223.07c","SPCC24B10.09","SPAC1783.05","SPBC25D12.04","SPAC17G6.05c","SPAC20H4.07","SPMITTRNAMET.01","SPBC800.13","SPCC550.14","SPAC16C9.07","SPBC902.03","SPAC30D11.03","SPBC800.05c","SPAC22H10.03c","SPAC227.15","SPAC23C11.11","SPBC119.07","SPBC83.05","SPBC216.01c","SPCC663.01c","SPAC7D4.09c","SPBC1105.12","SPBC29A10.10c","SPCC1259.11c","SPBC26H8.07c","SPCC18.08","SPBC17A3.04c","SPCC191.09c","SPAC1952.10c","SPBC12C2.12c","SPBC1709.09","SPBC16C6.07c","SPBC337.15c","SPBC530.14c","SPCC126.13c","SPBC11C11.06c","SPCC330.12c","SPAC806.05","SPBC32C12.03c","SPCC1742.01","SPCC576.04","SPBC20F10.04c","SPAC823.17","SPACUNK4.12c","SPAC3F10.03","SPBC3B8.01c","SPAC11D3.15","SPBC8D2.15","SPAC4G8.04","SPAC3A11.03","SPAC664.09","SPCC5E4.06","SPAC222.12c","SPAC30C2.06c","SPAC3G9.06","SPAC1F7.04","SPCC320.11c","SPCC1739.04c","SPBC18E5.06","SPAC26H5.02c","SPCC1020.13c","SPAC1420.04c","SPAC19B12.13","SPBC21.07c","SPAPB1A10.14","SPBC660.14","SPBC20F10.10","SPAC22F3.15","SPAC9.03c","SPCC962.02c","SPCC794.08","SPAC14C4.02c","SPAC6G10.05c","SPAC30D11.07","SPAC13A11.04c","SPCC126.04c","SPAC56E4.06c","SPAC767.01c","SPBC17D1.04","SPAC22E12.03c","SPBC418.02","SPBC1215.02c","SPCC1183.11","SPBC17G9.11c","SPAC6B12.06c","SPAC1834.06c","SPBC947.03c","SPCC663.05c","SPBPJ4664.02","SPBC17G9.05","SPBC15D4.15","SPBC17F3.02","SPAC12B10.02c","SPAC23H3.04","SPCC1840.02c","SPAC17G8.03c","SPAC13F5.04c","SPAC16A10.04","SPBC13G1.12","SPBPB8B6.05c","SPAC2F7.09c","SPBC25D12.06","SPCC4B3.08","SPAC31F12.01","SPAC1B3.11c","SPBC1271.03c","SPBC1861.09","SPBC2G2.09c","SPAC9E9.10c","SPCC126.10","SPBC19C7.03","SPAC343.06c","SPBPB2B2.02","SPBC1A4.03c","SPAC644.07","SPCC737.06c","SPAC19G12.02c","SPAC27E2.05","SPBC1289.16c","SPBC83.16c","SPBC16A3.15c","SPCC330.01c","SPAC19G12.03","SPBC19C7.04c","SPBP8B7.09c","SPAC25B8.04c","SPBC8D2.03c","SPAC17A5.15c","SPAC2C4.16c","SPAC521.05","SPAC11E3.13c","SPAC8E11.03c","SPBC1734.02c","SPBC19C2.09","SPAC688.04c","SPBC215.14c","SPAC1782.08c","SPAC688.10","SPBC17G9.13c","SPAC3C7.07c","SPAC821.04c","SPCC162.01c","SPAC823.03","SPCC63.08c","SPBC25B2.10","SPBC3E7.15c","SPBC428.12c","SPBC405.06","SPAC13G7.12c","SPBC776.16","SPCC757.05c","SPAC186.03","SPBC83.14c","SPAPB18E9.04c","SPBC21H7.03c","SPAC3G9.16c","SPAC31G5.11","SPBC31F10.03","SPCC970.09","SPSNRNA.01","SPBC146.12","SPAC29B12.01","SPAC3C7.05c","SPBC1773.10c","SPAC1B1.03c","SPBC3B8.10c","SPAC977.12","SPAC4A8.12c","SPBC83.08","SPAC27E2.03c","SPAC4G8.05","SPCC285.14","SPBP23A10.16","SPAC2F7.13c","SPBPB21E7.09","SPBC660.11","SPCC736.03c","SPBC19F5.01c","SPAC1002.01","SPBC19C7.02","SPAC27E2.06c","SPAC22F3.13","SPAPB1A10.02","SPBC2D10.11c","SPBC14C8.05c","SPAC3H1.13","SPBC1604.09c","SPBC4.07c","SPBC23G7.09","SPAC1327.01c","SPAC1002.17c","SPAC10F6.09c","SPAC19B12.03","SPBC19C7.06","SPBC8D2.06","SPBC26H8.05c","SPBP19A11.01","SPBC839.05c","SPAC9E9.14","SPAC926.09c","SPAC23C4.02","SPAC1002.18","SPAC24H6.05","SPAC3C7.03c","SPAC23D3.03c","SPBPB10D8.01","SPAC7D4.07c","SPBC1604.08c","SPBC8D2.12c","SPAC644.08","SPCPB1C11.03","SPBC336.03","SPBC30B4.05","SPAC23A1.16c","SPCC1672.06c","SPCC1020.02","SPBC1105.17","SPBC1685.11","SPBC23E6.07c","SPCC1020.10","SPCC1682.16","SPAC11D3.14c","SPBC17G9.03c","SPBC21B10.12","SPAC1805.17","SPAC869.10c","SPCC16C4.08c","SPAC11E3.14","SPBC25H2.02","SPAPB1A10.16","SPCC31H12.05c","SPCC4G3.11","SPBC902.04","SPCC830.07c","SPBC1921.03c","SPCC31H12.06","SPAC1039.01"],"gene_count":364,"ltp_gene_count":0},{"uniquename":"PMID:30141044","title":"Functional Analysis of the Yeast LINC Complex Using Fluctuation Spectroscopy and Super-Resolution Imaging.","citation":"Methods Mol Biol 2018;1840:137-161","abstract":"The Saccharomyces cerevisiae and Schizosaccharomyces pombe genomes encode a single SUN domain-containing protein, Mps3 and Sad1, respectively. Both localize to the yeast centrosome (known as the spindle pole body, SPB) and are essential for bipolar spindle formation. In addition, Mps3 and Sad1 play roles in chromosome organization in both mitotic and meiotic cells that are independent of their SPB function. To dissect the function of Mps3 at the nuclear envelope (NE) and SPB, we employed cell imaging methods such as scanning fluorescence cross-correlation spectroscopy (SFCCS) and single particle averaging with structured illumination microscopy (SPA-SIM) to determine the strength, nature, and location of protein-protein interactions in vivo. We describe how these same techniques can also be used in fission yeast to analyze Sad1, providing evidence of their applicability to other NE proteins and systems.","doi":"10.1007/978-1-4939-8691-0_12","authors":"Unruh JR, Slaughter BD, Jaspersen SL","authors_abbrev":"Unruh JR et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-08-25","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-08-26 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8967907","title":"Comparative amino acid sequence analysis of the C6 zinc cluster family of transcriptional regulators.","citation":"Nucleic Acids Res 1996 Dec 01;24(23):4599-607","abstract":"The C6 zinc cluster family of fungal regulatory proteins shares as DNA-binding motif the C6 zinc cluster, also known as the Zn(II)2Cys6 binuclear cluster. This family includes transcriptional activators like Gal4p, Leu3p, Hap1p, Put3p and Cha4p from Saccharomyces cerevisiae, qutA and amdR from Aspergillus, nit4 from Neurospora and Ntf1 from Schizosaccharomyces pombe. Seventy-nine proteins were retrieved from databases by homology to the C6 zinc cluster. All were fungal and 56 were found in the entire genome sequence of S.cerevisiae. Sequence analysis suggests that 60 of the 79 proteins possess one or more coiled-coil dimerization regions succeeding the C6 zinc cluster. Previous comparisons of Gal4p and seven other C6 zinc cluster proteins identified an additional region with weak homology. This region, designated the middle homology region (MHR), was shown to be present in 50 of the 79 proteins. Although reported mutation and deletion analyses suggest a role of MHR in regulation of protein activity, no function has yet been assigned specifically to this region. We find that the family of MHR sequences is confined to C6 zinc cluster proteins and hypothesize that one MHR function is to assist the C6 zinc cluster in DNA target discrimination.","authors":"Schjerling P, Holmberg S","authors_abbrev":"Schjerling P et al.","pubmed_publication_date":"01 Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9182664","title":"Type II myosin heavy chain encoded by the myo2 gene composes the contractile ring during cytokinesis in Schizosaccharomyces pombe.","citation":"J Cell Biol 1997 Jun 16;137(6):1309-19","abstract":"We cloned the myo2 gene of Schizosaccharomyces pombe, which encodes a type II myosin heavy chain, by virtue of its ability to promote diploidization in fission yeast cells. The myo2 gene encodes 1,526 amino acids in a single open reading frame. Myo2p shows homology to the head domains and the coiledcoil tail of the conventional type II myosin heavy chain and carries putative binding sites for ATP and actin. It also carries the IQ motif, which is a presumed binding site for the myosin light chain. However, Myo2p apparently carries only one IQ motif, while its counterparts in other species have two. There are nine proline residues, which should break alpha-helix, in the COOH-terminal coiled-coil region of Myo2p. Thus, Myo2p is rather unusual as a type II myosin heavy chain. Disruption of myo2 inhibited cell proliferation. myo2Delta cells showed normal punctate distribution of interphase actin, but they produced irregular actin rings and septa and were impaired in cell separation. Overproduction of Myo2p was also lethal, apparently blocking actin relocation. Nuclear division proceeded without actin ring formation and cytokinesis in cells overexpressing Myo2p, giving rise to multinucleated cells with dumbbell morphology. Analysis using tagged Myo2p revealed that Myo2p colocalizes with actin in the contractile ring, suggesting that Myo2p is a component of the ring and responsible for its contraction. Furthermore, genetic evidence suggested that the acto-myosin system may interact with the Ras pathway, which regulates mating and the maintenance of cell morphology in S. pombe.","authors":"Kitayama C, Sugimoto A, Yamamoto M","authors_abbrev":"Kitayama C et al.","pubmed_publication_date":"16 Jun 1997","pubmed_entrez_date":"1997-06-16","publication_year":"1997","canto_session_key":"92a03014a03e35ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-01 13:14:06","canto_approved_date":"2020-01-22 20:52:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-26 17:43:59","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22H10.07","SPAC16E8.09","SPCC645.05c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-06-01"},{"uniquename":"PMID:11399082","title":"Biochemical characterization of the structure-specific DNA-binding protein Cmb1 from Schizosaccharomyces pombe.","citation":"J Mol Biol 2001 Jun 22;309(5):1101-15","abstract":"Cmb1, a novel HMG box protein from Schizosaccharomyces pombe, has been characterized biochemically using glutaraldehyde cross-linking, gel-filtration and analytical ultracentrifugation. It was identified as a monomeric, non-spherical protein, with a tendency to aggregate in solution. Limited proteolysis with trypsin and chymotrypsin showed that the C-terminal HMG box was a compact, proteolytically stable domain and the N-terminal region of Cmb1 was relatively unstructured and more easily digested. As Cmb1 was previously identified as a potential mismatch-binding protein, the binding constants and stoichiometry for both homoduplex and heteroduplex DNA were determined using an IASys resonant mirror biosensor. Cmb1 indeed demonstrated a tighter association with mismatched DNA, especially with the C/Delta-mismatch. Expression constructs of Cmb1 were made to study the sections of the protein involved in DNA binding. Constructs with the N-terminal region absent revealed that the C-terminal HMG box was the primary DNA-binding region. The presence of the N-terminal region did, however, facilitate tighter binding to both homoduplex and heteroduplex DNA. The amino acid residues isoleucine 14 and leucine 39 were located as putative intercalating residues using structure guided homology modelling. The model templates were derived from two distinct HMG:DNA complexes: HMG-D bound to homoduplex DNA and HMG 1 bound to cisplatin DNA. Binding studies using the Cmb1 HMG box with point mutations in these residues showed that isoleucine 14 was important for the binding of Cmb1 to homoduplex DNA, but affected binding to mismatches to a lesser extent. In contrast, leucine 39 appeared to have a more significant function in binding to mismatched DNA.","authors":"Sassoon J, Lilie H, Baumann U, Kohli J","authors_abbrev":"Sassoon J et al.","pubmed_publication_date":"22 Jun 2001","pubmed_entrez_date":"2001-06-12","publication_year":"2001","canto_session_key":"f05dccddcd6526b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-20 15:27:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-20 15:27:38","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-20"},{"uniquename":"PMID:26193331","title":"The 3' to 5' Exoribonuclease DIS3: From Structure and Mechanisms to Biological Functions and Role in Human Disease.","citation":"Biomolecules 2015 Jul 17;5(3):1515-39","abstract":"DIS3 is a conserved exoribonuclease and catalytic subunit of the exosome, a protein complex involved in the 3' to 5' degradation and processing of both nuclear and cytoplasmic RNA species. Recently, aberrant expression of DIS3 has been found to be implicated in a range of different cancers. Perhaps most striking is the finding that DIS3 is recurrently mutated in 11% of multiple myeloma patients. Much work has been done to elucidate the structural and biochemical characteristics of DIS3, including the mechanistic details of its role as an effector of RNA decay pathways. Nevertheless, we do not understand how DIS3 mutations can lead to cancer. There are a number of studies that pertain to the function of DIS3 at the organismal level. Mutant phenotypes in S. pombe, S. cerevisiae and Drosophila suggest DIS3 homologues have a common role in cell-cycle progression and microtubule assembly. DIS3 has also recently been implicated in antibody diversification of mouse B-cells. This article aims to review current knowledge of the structure, mechanisms and functions of DIS3 as well as highlighting the genetic patterns observed within myeloma patients, in order to yield insight into the putative role of DIS3 mutations in oncogenesis.","doi":"10.3390/biom5031515","authors":"Robinson SR, Oliver AW, Chevassut TJ, Newbury SF","authors_abbrev":"Robinson SR et al.","pubmed_publication_date":"17 Jul 2015","pubmed_entrez_date":"2015-07-21","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-07-22 00:20:46","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC26H8.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11073978","title":"Mex67p of Schizosaccharomyces pombe interacts with Rae1p in mediating mRNA export.","citation":"Mol Cell Biol 2000 Dec;20(23):8767-82","abstract":"We identified the Schizosaccharomyces pombe mex67 gene (spmex67) as a multicopy suppressor of rae1-167 nup184-1 synthetic lethality and the rae1-167 ts mutation. spMex67p, a 596-amino-acid-long protein, has considerable sequence similarity to the Saccharomyces cerevisiae Mex67p (scMex67p) and human Tap. In contrast to scMEX67, spmex67 is essential for neither growth nor nuclear export of mRNA. However, an spmex67 null mutation (Deltamex67) is synthetically lethal with the rae1-167 mutation and accumulates poly(A)(+) RNA in the nucleus. We identified a central region (149 to 505 amino acids) within spMex67p that associates with a complex containing Rae1p that complements growth and mRNA export defects of the rae1-167 Deltamex67 synthetic lethality. This region is devoid of RNA-binding, N-terminal nuclear localization, and the C-terminal nuclear pore complex-targeting regions. The (149-505)-green fluorescent protein (GFP) fusion is found diffused throughout the cell. Overexpression of spMex67p inhibits growth and mRNA export and results in the redistribution of the diffused localization of the (149-505)-GFP fusion to the nucleus and the nuclear periphery. These results suggest that spMex67p competes for essential mRNA export factor(s). Finally, we propose that the 149-505 region of spMex67p could act as an accessory factor in Rae1p-dependent transport and that spMex67p participates at various common steps with Rae1p export complexes in promoting the export of mRNA.","authors":"Yoon JH, Love DC, Guhathakurta A, Hanover JA, Dhar R","authors_abbrev":"Yoon JH et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-14","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1921.03c","SPAP27G11.10c","SPCC1739.14","SPBC16A3.05c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:37864786","title":"Analyzing self-assembled spindle dynamics in fission yeast meiosis using in vivo fluorescence imaging.","citation":"STAR Protoc 2023 Oct 20;4(4):102655","abstract":"Chromosome segregation in female meiosis in many metazoans is mediated by acentrosomal spindles. The analysis of the dynamics of self-assembled spindles is a challenge due to the low availability of oocytes. Here, we present a protocol for analyzing self-assembled spindle dynamics in fission yeast meiosis using in vivo fluorescence imaging. We describe steps for starter culture preparation, meiosis induction, and sample preparation. We then detail procedures for acquisition and analysis of images of self-assembled spindles. For complete details on the use and execution of this protocol, please refer to Pineda-Santaella and Fernández-Álvarez (2019) 1  and Pineda-Santaella et al. (2021). 2 .","doi":"10.1016/j.xpro.2023.102655","authors":"Pineda-Santaella A, Martín-García R, Fernández-Álvarez A","authors_abbrev":"Pineda-Santaella A et al.","pubmed_publication_date":"20 Oct 2023","pubmed_entrez_date":"2023-10-21","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-10-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12455993","title":"Divergent subunit interactions among fungal mRNA 5'-capping machineries.","citation":"Eukaryot Cell 2002 Jun;1(3):448-57","abstract":"The Saccharomyces cerevisiae mRNA capping enzyme consists of two subunits: an RNA 5'-triphosphatase (RTPase) and GTP::mRNA guanylyltransferase (GTase). The GTase subunit (Ceg1) binds to the phosphorylated carboxyl-terminal domain of the largest subunit (CTD-P) of RNA polymerase II (pol II), coupling capping with transcription. Ceg1 bound to the CTD-P is inactive unless allosterically activated by interaction with the RTPase subunit (Cet1). For purposes of comparison, we characterize here the related GTases and RTPases from the yeasts Schizosaccharomyces pombe and Candida albicans. Surprisingly, the S. pombe capping enzyme subunits do not interact with each other. Both can independently interact with CTD-P of pol II, and the GTase is not repressed by CTD-P binding. The S. pombe RTPase gene (pct1+) is essential for viability. Pct1 can replace the S. cerevisiae RTPase when GTase activity is supplied by the S. pombe or mouse enzymes but not by the S. cerevisiae GTase. The C. albicans capping enzyme subunits do interact with each other. However, this interaction is not essential in vivo. Our results reveal an unexpected diversity among the fungal capping machineries.","authors":"Takagi T, Cho EJ, Janoo RT, Polodny V, Takase Y, Keogh MC, Woo SA, Fresco-Cohen LD, Hoffman CS, Buratowski S","authors_abbrev":"Takagi T et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-11-29","publication_year":"2002","canto_session_key":"d384a52dcc0dc8a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-05-26 16:52:28","canto_approved_date":"2023-12-10 10:02:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-10 11:21:10","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.04","SPBC2F12.08c","SPBC28F2.12"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2014-05-26"},{"uniquename":"PMID:16195226","title":"Sap1p binds to Ter1 at the ribosomal DNA of Schizosaccharomyces pombe and causes polar replication fork arrest.","citation":"J Biol Chem 2005 Nov 25;280(47):39135-42","abstract":"Eukaryotic DNA replication forks stall at natural replication fork barriers or Ter sites located within the ribosomal DNA (rDNA) intergenic spacer regions during unperturbed DNA replication. The rDNA intergenic spacer of the fission yeast Schizosaccharomyces pombe contains four polar or orientation-specific fork barriers, Ter1-3 and RFP4. Whereas the transcription terminator Reb1p binds Ter2 and Ter3 to arrest replication, the factor(s) responsible for fork arrest at Ter1 and RFP4 remain unknown. Using linker scanning mutagenesis, we have narrowed down minimal Ter1 to 21 bp. Sequence analysis revealed the presence of a consensus binding motif for the essential switch-activating and genome-stabilizing protein Sap1p within this region. Recombinant Sap1p bound Ter1 with high specificity, and endogenous Ter1 binding activity contained Sap1p and comigrated with the Sap1p-Ter1 complex. Circular permutation analysis suggested that Sap1p bends Ter1 and SAS1 upon binding. Targeted mutational analysis revealed that Ter1 mutations, which prevent Sap1p binding in vitro, are defective for replication fork arrest in vivo, whereas mutations that do not affect Sap1p binding remain competent to arrest replication. The results confirm the hypothesis that the chromatin organizer Sap1p binds site-specifically to genomic regions other than SAS1 and support the notion that Sap1p binds the rDNA fork barrier Ter1 to cause polar replication fork arrest at this site but not at SAS1.","authors":"Krings G, Bastia D","authors_abbrev":"Krings G et al.","pubmed_publication_date":"25 Nov 2005","pubmed_entrez_date":"2005-10-01","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1672.02c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:34101381","title":"Fission Yeast Schizosaccharomyces pombe: A Unicellular \"Micromammal\" Model Organism.","citation":"Curr Protoc 2021 Jun;1(6):e151","abstract":"The fission yeast Schizosaccharomyces pombe is a rod-shaped unicellular eukaryote, well known for its contributions as a model organism for our understanding of regulation and conservation of the eukaryotic cell cycle. As a yeast divergent from the budding yeast Saccharomyces cerevisiae, S. pombe shares more common features with humans including gene structures, chromatin dynamics, and the prevalence of introns, as well as the control of gene expression through pre-mRNA splicing, epigenetic gene silencing, and RNAi pathways. With the advent of new methodologies for research, S. pombe has become an increasingly used model to investigate various molecular and cellular processes over the last 50 years. Also, S. pombe serves as an excellent system for undergraduate students to obtain hands-on research experience. Versatile experimental approaches are amenable using the fission yeast system due to its relative ease of maintenance, its inherent cellular properties, its power in classic and molecular genetics, and its feasibility in genomics and proteomics analyses. This article provides an overview of S. pombe's rise as a valuable model organism and presents examples to highlight the significance of S. pombe as a unicellular \"micromammal\" in investigating biological questions. We especially focus on the advantages of and the advancements in using fission yeast for studying biological processes that are characteristic of metazoans to decipher the underlining molecular mechanisms fundamental to all eukaryotes. © 2021 Wiley Periodicals LLC.","doi":"10.1002/cpz1.151","authors":"Vyas A, Freitas AV, Ralston ZA, Tang Z","authors_abbrev":"Vyas A et al.","pubmed_publication_date":"Jun 2021","pubmed_entrez_date":"2021-06-08","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-06-10 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39892963","title":"The losses of Lem2 and Bqt4 exhibit similar impacts on intracellular movement dynamics in fission yeast.","citation":"Biochem Biophys Res Commun 2025 Feb 16;749:151326","abstract":"Quantifying movement dynamics inside a cell provides a deeper understanding of cellular functions. The 3-dimensional live observation has been widely applied to movement dynamics research. Fission yeast is an ideal model organism for studying cellular movement dynamics. In this study, we developed a novel method to quantify intracellular movement in wild-type cells, using a vector originating from the cell center as the movement reference. This method obtained more movement information, including movement direction, compared to the previously reported method, which used a single point as the movement reference. Using this new method, we quantified intracellular movement in wild type, bqt4Δ, and lem2Δ cells across various parameters. We characterized the nature of intracellular movement in wild-type cells and revealed that the losses of Bqt4 and Lem2, two inner membrane proteins, impact intracellular movement in a similar pattern, although distinct differences were also observed. These findings offer new insights into the study of the overlapping and distinct functions of Bqt4 and Lem2. This study provides a novel method for evaluating the intracellular movement dynamics, contributing to the understanding of intracellular movement nature, biophysical properties, and the evaluation of genes or proteins from an intracellular movement perspective.","doi":"10.1016/j.bbrc.2025.151326","authors":"Wang K, Ueno M","authors_abbrev":"Wang K et al.","pubmed_publication_date":"16 Feb 2025","pubmed_entrez_date":"2025-02-01","publication_year":"2025","canto_session_key":"a93538fdf940a21d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-02-03 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.10","SPBC19C7.10"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:11084925","title":"From transcription regulation to cell cycle checkpoint.","citation":"Novartis Found Symp 2000;229:19-24; discussion 24-6","abstract":"","authors":"Cai R, Fischer D, Yan-Neale Y, Xu H, Cohen D","authors_abbrev":"Cai R et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-11-21","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18254379","title":"RT-PCR method for selective detection of silent gene transcripts in silencing mutants in homothallic strains of Schizosaccharomyces pombe.","citation":"Biotechniques 2008 Jan;44(1):54, 56, 58","abstract":"Here we describe a method that allows selective detection of silent copy transcripts in homothallic strains of Schizosaccharomyces pombe in the presence of the active cassettes. The method involving RT-PCR (reverse transcriptase polymerase chain reaction) exploits our observation that the silent copy transcripts extend beyond the regions of homology to the flanking sequences specific for the donor cassettes, thus allowing design of oligos that are specific for the different donors. The results are validated using a known silencing mutant swi6.","authors":"Ahmed S, Singh J","authors_abbrev":"Ahmed S et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22300234","title":"Lipid droplet de novo formation and fission are linked to the cell cycle in fission yeast.","citation":"Traffic 2012 May;13(5):705-14","abstract":"Cells sequester neutral lipids in bodies called lipid droplets. Thus, the formation and breakdown of the droplets are important for cellular metabolism; unfortunately, these processes are difficult to quantify. Here, we used time-lapse confocal microscopy to track the formation, movement and size changes of lipid droplets throughout the cell cycle in fission yeast Schizosaccharomyces pombe. In theory, the number of lipid droplets in these cells must increase for daughter cells to have the same number of droplets as the parent at a reference point in the cell cycle. We observed stable droplet formation events in G2 phase that were divided evenly between de novo formation of nascent droplets and fission of preexisting droplets. The observations that lipid droplet number is linked to the cell cycle and that droplets can form via fission were both new discoveries. Thus, we scrutinized each fission event for multiple signatures to eliminate possible artifacts from our microscopy. We augmented our time-lapse confocal microscopy with electron microscopy, which showed lipid droplet 'intermediates': droplets shaped like dumbbells that are potentially in transition states between two spherical droplets. Using these complementary microscopy techniques and also dynamic simulations, we show that lipid droplets can form by fission.","doi":"10.1111/j.1600-0854.2012.01339.x","authors":"Long AP, Manneschmidt AK, VerBrugge B, Dortch MR, Minkin SC, Prater KE, Biggerstaff JP, Dunlap JR, Dalhaimer P","authors_abbrev":"Long AP et al.","pubmed_publication_date":"May 2012","pubmed_entrez_date":"2012-02-04","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10701132","title":"Identification of rpaP1-5 and rpaP2-6 genes encoding two additional variants of the 60S acidic ribosomal proteins of Schizosaccharomyces pombe.","citation":"Genome 2000 Feb;43(1):205-7","abstract":"In the fission yeast, four genes (rpaP1-1, rpaP1-3, rpaP2-2, and rpaP2-4) encoding two variants of the RpaP1 and RpaP2 ribosomal proteins (rp) have been characterized. We have identified cDNA for additional variants called RpaP1.5 and RpaP2.6. Sequence comparison suggests that RpaP1.5 diverged before RpaP1.1 and RpaP1.3 and that RpaP2.6 is closer to RpaP2.2 than to RpaP2.4. The corresponding genes, rpaP1-5 and rpaP2-6, are transcribed coordinately with other rp genes.","authors":"Bonnet C, Perret E, Bonnin O, Picard A, Caput D, Lenaers G","authors_abbrev":"Bonnet C et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-03-04","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29892076","title":"Structural insights into the stimulation of S. pombe Dnmt2 catalytic efficiency by the tRNA nucleoside queuosine.","citation":"Sci Rep 2018 Jun 11;8(1):8880","abstract":"Dnmt2 methylates cytosine at position 38 of tRNA Asp  in a variety of eukaryotic organisms. A correlation between the presence of the hypermodified nucleoside queuosine (Q) at position 34 of tRNA Asp  and the Dnmt2 dependent C38 methylation was recently found in vivo for S. pombe and D. discoideum. We demonstrate a direct effect of the Q-modification on the methyltransferase catalytic efficiency in vitro, as V max /K 0.5  of purified S. pombe Dnmt2 shows an increase for in vitro transcribed tRNA Asp  containing Q34 to 6.27 ∗ 10 -3  s -1  µM -1  compared to 1.51 ∗ 10 -3  s -1  µM -1  for the unmodified substrate. Q34tRNA Asp  exhibits an only slightly increased affinity for Dnmt2 in comparison to unmodified G34tRNA. In order to get insight into the structural basis for the Q-dependency, the crystal structure of S. pombe Dnmt2 was determined at 1.7 Å resolution. It closely resembles the known structures of human and E. histolytica Dnmt2, and contains the entire active site loop. The interaction with tRNA was analyzed by means of mass-spectrometry using UV cross-linked Dnmt2-tRNA complex. These cross-link data and computational docking of Dnmt2 and tRNA Asp  reveal Q34 positioned adjacent to the S-adenosylmethionine occupying the active site, suggesting that the observed increase of Dnmt2 catalytic efficiency by queuine originates from optimal positioning of the substrate molecules and residues relevant for methyl transfer.","doi":"10.1038/s41598-018-27118-5","authors":"Johannsson S, Neumann P, Wulf A, Welp LM, Gerber HD, Krull M, Diederichsen U, Urlaub H, Ficner R","authors_abbrev":"Johannsson S et al.","pubmed_publication_date":"11 Jun 2018","pubmed_entrez_date":"2018-06-13","publication_year":"2018","canto_session_key":"2e1a4eecbb8ccb28","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-06-14 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPATRNAASP.01","SPBC19C2.02"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"6fdf","gene_chains":[{"gene_uniquename":"SPBC19C2.02","chain":"A/B/C/D","position":"2-330"}],"title":"Crystal structure of S. pombe Dnmt2 methyltransferase","entry_authors":"Johannsson S,Neumann P,Ficner R","entry_authors_abbrev":"Johannsson S et al.","reference_uniquename":"PMID:29892076","experimental_method":"X-ray","resolution":"1.697"}]},{"uniquename":"PMID:17307401","title":"The novel gene mus7(+) is involved in the repair of replication-associated DNA damage in fission yeast.","citation":"DNA Repair (Amst) 2007 Jun 01;6(6):770-80","abstract":"The progression of replication forks is often impeded by obstacles that cause them to stall or collapse, and appropriate responses to replication-associated DNA damage are important for genome integrity. Here we identified a new gene, mus7(+), that is involved in the repair of replication-associated DNA damage in the fission yeast Schizosaccharomyces pombe. The Deltamus7 mutant shows enhanced sensitivity to methyl methanesulfonate (MMS), camptothecin, and hydroxyurea, agents that cause replication fork stalling or collapse, but not to ultraviolet light or X-rays. Epistasis analysis of MMS sensitivity indicates that Mus7 functions in the same pathway as Mus81, a subunit of the Mus81-Eme1 structure-specific endonuclease, which has been implicated in the repair of the replication-associated DNA damage. In Deltamus7 and Deltamus81 cells, the repair of MMS-induced DNA double-strand breaks (DSBs) is severely impaired. Moreover, some cells with either mutation are hyper-elongated or enlarged, and most of these cells accumulate in late G2 phase. Spontaneous Rad22 (recombination mediator protein RAD52 homolog) foci increase in S phase to late G2 phase in Deltamus7 and Deltamus81 cells. These results suggest that replication-associated DSBs accumulate in these cells and that Rad22 foci form in the absence of Mus7 or Mus81. We also found that the rate of spontaneous conversion-type recombination is reduced in mitotic Deltamus7 cells, suggesting that Rhp51- (RAD51 homolog) dependent homologous recombination is disturbed in this mutant. From these data, we propose that Mus7 functions in the repair of replication-associated DSBs by promoting RAD51-dependent conversion-type recombination downstream of Rad22 and Mus81.","authors":"Yokoyama M, Inoue H, Ishii C, Murakami Y","authors_abbrev":"Yokoyama M et al.","pubmed_publication_date":"01 Jun 2007","pubmed_entrez_date":"2007-02-20","publication_year":"2007","canto_session_key":"c981881e2d6e2ab9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-17 16:02:15","canto_approved_date":"2021-06-21 15:28:23","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-04-17 16:02:01","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":50,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6B12.02c","SPCC4G3.05c","SPBC1703.14c","SPBC19C7.09c","SPBC3E7.08c","SPAC30D11.10","SPAC2G11.12"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-04-17"},{"uniquename":"EMBL:AF087832","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22180499","title":"MADS box transcription factor Mbx2/Pvg4 regulates invasive growth and flocculation by inducing gsf2+ expression in fission yeast.","citation":"Eukaryot Cell 2012 Feb;11(2):151-8","abstract":"The fission yeast Schizosaccharomyces pombe exhibits invasive growth and nonsexual flocculation in response to nitrogen limitation. Gsf2, a flocculin of fission yeast, is required not only for nonsexual flocculation but also for invasive growth through the recognition of galactose residues on cell surface glycoconjugates. We found that pyruvylation negatively regulates nonsexual flocculation by capping the galactose residues of N-linked galactomannan. We investigated whether pyruvylation also regulates invasive growth. The pvg4(+) gene originally was isolated as a multicopy suppressor of a pvg4 mutant defective in the pyruvylation of N-linked oligosaccharides. However, we did not detect a defect in cell surface pyruvylation in the pvg4/mbx2 deletion mutant, as assessed by alcian blue staining and a Q-Sepharose binding assay. Instead, the deletion prevented invasive growth under conditions of low nitrogen and high glucose, and it reduced the adhesion and flocculation of otherwise flocculent mutants by reducing gsf2(+) expression. mbx2(+)-overexpressing strains exhibited nonsexual and calcium-dependent aggregation, which was inhibited in the presence of galactose but mediated by the induction of gsf2(+). These findings indicate that Mbx2 mediates invasive growth and flocculation via the transcriptional activation of gsf2(+) in fission yeast. In addition, we found that fission yeast Mbx2 induces the nonsexual flocculation of budding yeast by the activation of FLO1.","doi":"10.1128/EC.05276-11","authors":"Matsuzawa T, Yoritsune K, Takegawa K","authors_abbrev":"Matsuzawa T et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-12-20","publication_year":"2012","canto_session_key":"3f5875a2c3abe932","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2017-10-25 15:40:00","canto_approved_date":"2023-01-27 08:42:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-20 09:55:47","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC317.01","SPBC1921.06c","SPAC27E2.07","SPAC1D4.11c","SPCC1742.01","SPBC15D4.02","SPAC8F11.10c","SPAC22F8.02c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-10-25"},{"uniquename":"PMID:34200466","title":"The Multiple Functions of Rho GTPases in Fission Yeasts.","citation":"Cells 2021 Jun 07;10(6)","abstract":"The Rho family of GTPases represents highly conserved molecular switches involved in a plethora of physiological processes. Fission yeast  Schizosaccharomyces pombe  has become a fundamental model organism to study the functions of Rho GTPases over the past few decades. In recent years, another fission yeast species,  Schizosaccharomyces japonicus , has come into focus offering insight into evolutionary changes within the genus. Both fission yeasts contain only six Rho-type GTPases that are spatiotemporally controlled by multiple guanine-nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and whose intricate regulation in response to external cues is starting to be uncovered. In the present review, we will outline and discuss the current knowledge and recent advances on how the fission yeasts Rho family GTPases regulate essential physiological processes such as morphogenesis and polarity, cellular integrity, cytokinesis and cellular differentiation.","doi":"10.3390/cells10061422","authors":"Vicente-Soler J, Soto T, Franco A, Cansado J, Madrid M","authors_abbrev":"Vicente-Soler J et al.","pubmed_publication_date":"07 Jun 2021","pubmed_entrez_date":"2021-07-02","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-07-04 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03","SPAC1F7.04"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:17018289","title":"Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin.","citation":"Mol Cell 2006 Oct 06;24(1):13-23","abstract":"ADF/cofilins are key regulators of actin dynamics during cellular motility, yet their precise role and mechanism of action are shrouded in ambiguity. Direct observation of actin filaments by evanescent wave microscopy showed that cofilins from fission yeast and human do not increase the rate that pointed ends of actin filaments shorten beyond the rate for ADP-actin subunits, but both cofilins inhibit elongation and subunit dissociation at barbed ends. Direct observation also showed that cofilins from fission yeast, Acanthamoeba, and human sever actin filaments optimally at low-cofilin binding densities well below their K(d)s, but not at high binding densities. High concentrations of cofilin nucleate actin assembly. Thus, the action of cofilins in cells will depend on the local concentration of active cofilins: low concentrations favor severing, whereas high concentrations favor nucleation. These results establish a clear paradigm for actin turnover by cofilin in cells.","authors":"Andrianantoandro E, Pollard TD","authors_abbrev":"Andrianantoandro E et al.","pubmed_publication_date":"06 Oct 2006","pubmed_entrez_date":"2006-10-05","publication_year":"2006","canto_session_key":"9b92e5ccdcf83bcc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-09-19 17:50:22","canto_approved_date":"2023-03-03 13:40:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-19 17:50:13","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-09-19","pdb_entries":[{"pdb_id":"2i2q","gene_chains":[{"gene_uniquename":"SPAC20G4.06c","chain":"A","position":"1-137"}],"title":"Fission Yeast cofilin","entry_authors":"Andrianantoandro E,Pollard TD","entry_authors_abbrev":"Andrianantoandro E et al.","reference_uniquename":"PMID:17018289","experimental_method":"X-ray","resolution":"1.72"}]},{"uniquename":"PMID:11063680","title":"Fission yeast Ras1 effector Scd1 interacts with the spindle and affects its proper formation.","citation":"Genetics 2000 Nov;156(3):995-1004","abstract":"Ras1 GTPase is the Schizosaccharomyces pombe homolog of the mammalian Ha-Ras proto-oncoprotein. Ras1 interacts with Scd1 (aka Ral1), a presumptive guanine nucleotide exchange factor for Cdc42sp, to control organization of the cytoskeleton. In this study, we demonstrated that the scd1 deletion (scd1Delta) induced hypersensitivity to microtubule destabilizing drugs and instability of the minichromosome. Overexpression of scd1 induced formation of abnormal spindles and chromosome missegregation. The scd1 deletion worsened the defects of spindle formation in tubulin mutants; by contrast, it did not induce lethality in mutants defective in the spindle pole bodies. These genetic data suggest that Scd1 can interact with tubulin with substantial specificity to affect proper spindle formation and chromosome segregation. Subcellular localization data further illustrated that a GFP-Scd1 fusion protein can associate with the spindle. Finally, we showed that unlike ras1Delta and scd1Delta, byr2Delta (affecting the Ras1 effector for mating) is not synthetically lethal with the tubulin mutations. These data collectively suggest that the Ras1 pathway can impinge upon microtubules through Scd1, but not Byr2, to affect proper spindle formation and chromosome segregation.","authors":"Li YC, Chen CR, Chang EC","authors_abbrev":"Li YC et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-11-07","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPAC16E8.09","SPBC26H8.07c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:37485020","title":"Replication stress by MMS stimulates DNA synthesis in post-replicative G2-phase in  S. pombe  .","citation":"MicroPubl Biol 2023;2023","abstract":"DNA replication is generally limited to S-phase but replication stress can drive cells to undergo DNA synthesis outside of S-phase. Mitotic DNA synthesis pathway is known to be activated to deal with replication stress-induced chromosomal instability. There is also growing evidence that residual DNA synthesis can occur in G2. We demonstrate that fission yeast cells stimulate DNA synthesis in G2-phase but not in M-phase in response to DNA alkylating agent MMS. Auxin-induced degradation of DNA replication helicase Mcm4 during G2, but not during mitosis, inhibits post-replicative DNA synthesis.","doi":"10.17912/micropub.biology.000852","authors":"Kim SM, Forsburg SL","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-07-24","publication_year":"2023","canto_session_key":"3b5a07e48aab4e40","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-07-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20467261","title":"Isolation and characterization of ethanol-producing Schizosaccharomyces pombe CHFY0201.","citation":"J Microbiol Biotechnol 2010 Apr;20(4):828-34","abstract":"Ethanol-producing yeast strain, CHFY0201 was isolated from soil in South Korea using an enrichment technique in a yeast peptone dextrose medium supplemented with 5% (w/v) ethanol at 30 degrees C. The phenotypic and physiological characteristics, as well as molecular phylogenetic analysis based on the D1/D2 domains of the large subunit (26S) rDNA gene and the internally transcribed spacer (ITS) 1+2 regions suggested that the CHFY0201 was novel strain of Schizosaccharomyces pombe. During shaking flask cultivation, the highest ethanol productivity and theoretical yield of S. pombe CHFY0201 in YPD media containing 9.5% total sugars was 0.59 +/- 0.01 g/l/h and 88.4 +/- 0.91%, respectively. Simultaneous saccharification and fermentation for ethanol production was carried out using liquefied cassava (Manihot esculenta) powder in a 5 l lab-scale jar fermenter at 32 degrees C for 66 h with an agitation speed of 120 rpm. Under these conditions, S. pombe CHFY0201 yielded a final ethanol concentration of 72.1 +/- 0.27 g/l and a theoretical yield of 82.7 +/- 1.52% at a maximum ethanol productivity of 1.16 +/- 0.07 g/l/h. These results suggest that S. pombe CHFY0201 is a potential producer for industrial bioethanol production.","authors":"Choi GW, Um HJ, Kim M, Kim Y, Kang HW, Chung BW, Kim YH","authors_abbrev":"Choi GW et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-05-15","publication_year":"2010","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31463572","title":"MSTO1 mutations cause mtDNA depletion, manifesting as muscular dystrophy with cerebellar involvement.","citation":"Acta Neuropathol 2019 Dec;138(6):1013-1031","abstract":"MSTO1 encodes a cytosolic mitochondrial fusion protein, misato homolog 1 or MSTO1. While the full genotype-phenotype spectrum remains to be explored, pathogenic variants in MSTO1 have recently been reported in a small number of patients presenting with a phenotype of cerebellar ataxia, congenital muscle involvement with histologic findings ranging from myopathic to dystrophic and pigmentary retinopathy. The proposed underlying pathogenic mechanism of MSTO1-related disease is suggestive of impaired mitochondrial fusion secondary to a loss of function of MSTO1. Disorders of mitochondrial fusion and fission have been shown to also lead to mitochondrial DNA (mtDNA) depletion, linking them to the mtDNA depletion syndromes, a clinically and genetically diverse class of mitochondrial diseases characterized by a reduction of cellular mtDNA content. However, the consequences of pathogenic variants in MSTO1 on mtDNA maintenance remain poorly understood. We present extensive phenotypic and genetic data from 12 independent families, including 15 new patients harbouring a broad array of bi-allelic MSTO1 pathogenic variants, and we provide functional characterization from seven MSTO1-related disease patient fibroblasts. Bi-allelic loss-of-function variants in MSTO1 manifest clinically with a remarkably consistent phenotype of childhood-onset muscular dystrophy, corticospinal tract dysfunction and early-onset non-progressive cerebellar atrophy. MSTO1 protein was not detectable in the cultured fibroblasts of all seven patients evaluated, suggesting that pathogenic variants result in a loss of protein expression and/or affect protein stability. Consistent with impaired mitochondrial fusion, mitochondrial networks in fibroblasts were found to be fragmented. Furthermore, all fibroblasts were found to have depletion of mtDNA ranging from 30 to 70% along with alterations to mtDNA nucleoids. Our data corroborate the role of MSTO1 as a mitochondrial fusion protein and highlight a previously unrecognized link to mtDNA regulation. As impaired mitochondrial fusion is a recognized cause of mtDNA depletion syndromes, this novel link to mtDNA depletion in patient fibroblasts suggests that MSTO1-deficiency should also be considered a mtDNA depletion syndrome. Thus, we provide mechanistic insight into the disease pathogenesis associated with MSTO1 mutations and further define the clinical spectrum and the natural history of MSTO1-related disease.","doi":"10.1007/s00401-019-02059-z","authors":"Donkervoort S, Sabouny R, Yun P, Gauquelin L, Chao KR, Hu Y, Al Khatib I, Töpf A, Mohassel P, Cummings BB, Kaur R, Saade D, Moore SA, Waddell LB, Farrar MA, Goodrich JK, Uapinyoying P, Chan SHS, Javed A, Leach ME, Karachunski P, Dalton J, Medne L, Harper A, Thompson C, Thiffault I, Specht S, Lamont RE, Saunders C, Racher H, Bernier FP, Mowat D, Witting N, Vissing J, Hanson R, Coffman KA, Hainlen M, Parboosingh JS, Carnevale A, Yoon G, Schnur RE, Care4Rare Canada Consortium, Boycott KM, Mah JK, Straub V, Foley AR, Innes AM, Bönnemann CG, Shutt TE","authors_abbrev":"Donkervoort S et al.","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-08-30","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30C2.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11983175","title":"Meiotic DNA breaks at the S. pombe recombination hot spot M26.","citation":"Mol Cell 2002 Apr;9(4):847-55","abstract":"The ade6-M26 allele of Schizosaccharomyces pombe creates a well-defined meiotic recombination hot spot that requires a specific sequence, 5'-ATGACGT-3', and the Atf1*Pcr1 transcription factor for activity. We find that M26 stimulates the formation of meiosis-specific double-strand DNA breaks at multiple sites surrounding M26. Like hot spot activity, breakage requires the M26 heptamer, Pcr1, and the general recombination factor Rec12. When the M26 heptamer is moved to new positions within ade6, new break sites are observed spanning approximately 0.5-2 kb around the moved heptamer. Break frequency is strongly correlated with recombination frequency for these alleles. The occurrence of breaks at M26 suggests mechanistic similarities to hot spots in the distantly related yeast Saccharomyces cerevisiae.","authors":"Steiner WW, Schreckhise RW, Smith GR","authors_abbrev":"Steiner WW et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-05-02","publication_year":"2002","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14527419","title":"The endogenous Mus81-Eme1 complex resolves Holliday junctions by a nick and counternick mechanism.","citation":"Mol Cell 2003 Sep;12(3):747-59","abstract":"Functional studies strongly suggest that the Mus81-Eme1 complex resolves Holliday junctions (HJs) in fission yeast, but in vitro it preferentially cleaves flexible three-way branched structures that model replication forks or 3' flaps. Here we report that a nicked HJ is the preferred substrate of endogenous and recombinant Mus81-Eme1. Cleavage occurs specifically on the strand that opposes the nick, resulting in resolution of the structure into linear duplex products. Resolving cuts made by the endogenous Mus81-Eme1 complex on an intact HJ are quasi-simultaneous, indicating that Mus81-Eme1 resolves HJs by a nick and counternick mechanism, with a large rate enhancement of the second cut arising from the flexible nature of the nicked HJ intermediate. Recombinant Mus81-Eme1 is ineffective at making the first cut. We also report that HJs accumulate in a DNA polymerase alpha mutant that lacks Mus81, providing further evidence that the Mus81-Eme1 complex targets HJs in vivo.","authors":"Gaillard PHL, Noguchi E, Shanahan P, Russell P","authors_abbrev":"Gaillard PHL et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-10-07","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4G3.05c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:2328719","title":"The pat1 protein kinase controls transcription of the mating-type genes in fission yeast.","citation":"EMBO J 1990 May;9(5):1401-6","abstract":"The developmental programme of fission yeast brings about a transition from mitotic cell division to the dormant state of ascospores. In response to nitrogen starvation, two cells of opposite mating type conjugate to form a diploid zygote, which then undergoes meiosis and sporulation. This differentiation process is characterized by a transcriptional induction of the mating-type genes. Conjugation can also be induced in pat1-ts mutants by a shift to a semi-permissive temperature. The pat1 gene encodes a protein kinase, which also functions further downstream in the developmental pathway controlling entry into meiosis. We have analysed transcriptional induction of mating-type genes in various strains--with and without a pat1-ts allele. In wild-type cells of P-mating type derepression occurs in two rounds. First, the mat1-Pc gene is induced in response to nitrogen starvation. Mutants in the map1 gene are defective in this process. In the following step the mat1-Pm gene is expressed in response to a pheromone signal generated by cells of M mating type. Both these controls are derepressed in the pat1-ts mutant at semipermissive temperature. Previous work has established that expression of the mating-type genes in the zygote leads to complete loss of pat1 protein kinase activity causing entry into meiosis. Thus, pat1 can promote its own inactivation. We suggest a model according to which a stepwise inactivation of pat1 leads to sequential derepression of the processes of conjugation and meiosis.","authors":"Nielsen O, Egel R","authors_abbrev":"Nielsen O et al.","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_session_key":"d47046a87d5d426","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-03-22 19:02:13","canto_approved_date":"2026-04-08 07:30:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-24 15:11:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.06","SPBC19C2.05","SPMTR.01","SPBC23G7.09","SPMTR.02"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2012-03-22"},{"uniquename":"PMID:30348841","title":"Brc1 Promotes the Focal Accumulation and SUMO Ligase Activity of Smc5-Smc6 during Replication Stress.","citation":"Mol Cell Biol 2019 Jan 15;39(2)","abstract":"As genetic instability drives disease or loss of cell fitness, cellular safeguards have evolved to protect the genome, especially during sensitive cell cycle phases, such as DNA replication. Fission yeast Brc1 has emerged as a key factor in promoting cell survival when replication forks are stalled or collapsed. Brc1 is a multi-BRCT protein that is structurally related to the budding yeast Rtt107 and human PTIP DNA damage response factors, but functional similarities appear limited. Brc1 is a dosage suppressor of a mutation in the essential Smc5-Smc6 genome stability complex and is thought to act in a bypass pathway. In this study, we reveal an unexpectedly intimate connection between Brc1 and Smc5-Smc6 function. Brc1 is required for the accumulation of the Smc5-Smc6 genome stability complex in foci during replication stress and for activation of the intrinsic SUMO ligase activity of the complex by collapsed replication forks. Moreover, we show that the chromatin association and SUMO ligase activity of Smc5-Smc6 require the Nse5-Nse6 heterodimer, explaining how this nonessential cofactor critically supports the DNA repair roles of Smc5-Smc6. We also found that Brc1 interacts with Nse5-Nse6, as well as gamma-H2A, so it can tether Smc5-Smc6 at replicative DNA lesions to promote survival.","doi":"10.1128/MCB.00271-18","authors":"Oravcová M, Gadaleta MC, Nie M, Reubens MC, Limbo O, Russell P, Boddy MN","authors_abbrev":"Oravcová M et al.","pubmed_publication_date":"15 Jan 2019","pubmed_entrez_date":"2018-10-24","publication_year":"2019","canto_session_key":"5a8021665769078b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Martina Oravcova","canto_first_approved_date":"2022-09-09 10:39:44","canto_approved_date":"2024-06-28 08:52:53","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2022-09-09 08:58:01","canto_added_date":"2018-10-25 00:15:04","annotation_curators":[{"name":"Martina Oravcova","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.05c","SPAC11E3.08c","SPBC20F10.04c","SPCC622.08c","SPBC1734.06","SPAC14C4.02c","SPBC651.10","SPAC16A10.06c","SPAC19G12.06c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2022-09-09"},{"uniquename":"PMID:22487684","title":"ATP analog-sensitive Pat1 protein kinase for synchronous fission yeast meiosis at physiological temperature.","citation":"Cell Cycle 2012 Apr 15;11(8):1626-33","abstract":"To study meiosis, synchronous cultures are often indispensable, especially for physical analyses of DNA and proteins. A temperature-sensitive allele of the Pat1 protein kinase (pat1-114) has been widely used to induce synchronous meiosis in the fission yeast Schizosaccharomyces pombe, but pat1-114-induced meiosis differs from wild-type meiosis, and some of these abnormalities might be due to higher temperature needed to inactivate the Pat1 kinase. Here, we report an ATP analog-sensitive allele of Pat1 [Pat1(L95A), designated pat1-as2] that can be used to generate synchronous meiotic cultures at physiological temperature. In pat1-as2 meiosis, chromosomes segregate with higher fidelity, and spore viability is higher than in pat1-114 meiosis, although recombination is lower by a factor of 2-3 in these mutants than in starvation-induced pat1(+) meiosis. Addition of the mat-Pc gene improved chromosome segregation and spore viability to nearly the level of starvation-induced meiosis. We conclude that pat1-as2 mat-Pc cells offer synchronous meiosis with most tested properties similar to those of wild-type meiosis.","doi":"10.4161/cc.20052","authors":"Cipak L, Hyppa RW, Smith GR, Gregan J","authors_abbrev":"Cipak L et al.","pubmed_publication_date":"15 Apr 2012","pubmed_entrez_date":"2012-04-11","publication_year":"2012","canto_session_key":"5330bb4f66962798","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21531710","title":"Identification of noncoding transcripts from within CENP-A chromatin at fission yeast centromeres.","citation":"J Biol Chem 2011 Jul 01;286(26):23600-7","abstract":"The histone H3 variant CENP-A is the most favored candidate for an epigenetic mark that specifies the centromere. In fission yeast, adjacent heterochromatin can direct CENP-A(Cnp1) chromatin establishment, but the underlying features governing where CENP-A(Cnp1) chromatin assembles are unknown. We show that, in addition to centromeric regions, a low level of CENP-A(Cnp1) associates with gene promoters where histone H3 is depleted by the activity of the Hrp1(Chd1) chromatin-remodeling factor. Moreover, we demonstrate that noncoding RNAs are transcribed by RNA polymerase II (RNAPII) from CENP-A(Cnp1) chromatin at centromeres. These analyses reveal a similarity between centromeres and a subset of RNAPII genes and suggest a role for remodeling at RNAPII promoters within centromeres that influences the replacement of histone H3 with CENP-A(Cnp1).","doi":"10.1074/jbc.M111.228510","authors":"Choi ES, Strålfors A, Castillo AG, Durand-Dubief M, Ekwall K, Allshire RC","authors_abbrev":"Choi ES et al.","pubmed_publication_date":"01 Jul 2011","pubmed_entrez_date":"2011-05-03","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26071525","title":"Molecular control of the Wee1 regulatory pathway by the SAD kinase Cdr2.","citation":"J Cell Sci 2015 Aug 01;128(15):2842-53","abstract":"Cell growth and division are tightly coordinated to maintain cell size constant during successive cell cycles. In Schizosaccharomyces pombe, the SAD kinase Cdr2 regulates the cell size at division and the positioning of the division plane. Cdr2 forms nodes on the medial cortex containing factors that constitute an inhibitory pathway for Wee1. This pathway is regulated by polar gradients of the DYRK kinase Pom1, and involves a direct inhibitor of Wee1, the SAD kinase Cdr1. Cdr2 also interacts with the anillin Mid1, which defines the division plane, and with additional components of the medial cortical nodes, including Blt1, which participate in the mitotic-promoting and cytokinetic functions of nodes. Here, we show that the interaction of Cdr2 with Wee1 and Mid1 requires the UBA domain of Cdr2, which is necessary for its kinase activity. In contrast, Cdr1 associates with the C-terminus of Cdr2, which is composed of basic and KA-1 lipid-binding domains. Mid1 also interacts with the C-terminus of Cdr2 and might bridge the N- and C-terminal domains, whereas Blt1 associates with the central spacer region. We propose that the association of Cdr2 effectors with different domains might constrain Cdr1 and Wee1 spatially to promote Wee1 inhibition upon Cdr2 kinase activation.","doi":"10.1242/jcs.173146","authors":"Guzmán-Vendrell M, Rincon SA, Dingli F, Loew D, Paoletti A","authors_abbrev":"Guzmán-Vendrell M et al.","pubmed_publication_date":"01 Aug 2015","pubmed_entrez_date":"2015-06-14","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-06-15 00:20:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.06c","SPAC57A10.02","SPCC4B3.15","SPCC18B5.03"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:9649514","title":"The M26 hotspot of Schizosaccharomyces pombe stimulates meiotic ectopic recombination and chromosomal rearrangements.","citation":"Genetics 1998 Jul;149(3):1191-204","abstract":"Homologous recombination is increased during meiosis between DNA sequences at the same chromosomal position (allelic recombination) and at different chromosomal positions (ectopic recombination). Recombination hotspots are important elements in controlling meiotic allelic recombination. We have used artificially dispersed copies of the ade6 gene in Schizosaccharomyces pombe to study hotspot activity in meiotic ectopic recombination. Ectopic recombination was reduced 10-1000-fold relative to allelic recombination, and was similar to the low frequency of ectopic recombination between naturally repeated sequences in S. pombe. The M26 hotspot was active in ectopic recombination in some, but not all, integration sites, with the same pattern of activity and inactivity in ectopic and allelic recombination. Crossing over in ectopic recombination, resulting in chromosomal rearrangements, was associated with 35-60% of recombination events and was stimulated 12-fold by M26. These results suggest overlap in the mechanisms of ectopic and allelic recombination and indicate that hotspots can stimulate chromosomal rearrangements.","authors":"Virgin JB, Bailey JP","authors_abbrev":"Virgin JB et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-07-03","publication_year":"1998","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24161933","title":"Determinants of robustness in spindle assembly checkpoint signalling.","citation":"Nat Cell Biol 2013 Nov;15(11):1328-39","abstract":"The spindle assembly checkpoint is a conserved signalling pathway that protects genome integrity. Given its central importance, this checkpoint should withstand stochastic fluctuations and environmental perturbations, but the extent of and mechanisms underlying its robustness remain unknown. We probed spindle assembly checkpoint signalling by modulating checkpoint protein abundance and nutrient conditions in fission yeast. For core checkpoint proteins, a mere 20% reduction can suffice to impair signalling, revealing a surprising fragility. Quantification of protein abundance in single cells showed little variability (noise) of critical proteins, explaining why the checkpoint normally functions reliably. Checkpoint-mediated stoichiometric inhibition of the anaphase activator Cdc20 (Slp1 in Schizosaccharomyces pombe) can account for the tolerance towards small fluctuations in protein abundance and explains our observation that some perturbations lead to non-genetic variation in the checkpoint response. Our work highlights low gene expression noise as an important determinant of reliable checkpoint signalling.","doi":"10.1038/ncb2864","authors":"Heinrich S, Geissen EM, Kamenz J, Trautmann S, Widmer C, Drewe P, Knop M, Radde N, Hasenauer J, Hauf S","authors_abbrev":"Heinrich S et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-10-29","publication_year":"2013","canto_session_key":"ed9652a888c24c94","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silke Hauf","canto_first_approved_date":"2020-06-03 15:58:03","canto_approved_date":"2024-03-29 12:13:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-05-31 21:07:59","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":8,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Silke Hauf","community_curator":true,"annotation_count":18,"orcid":"0000-0001-5938-721X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Silke Hauf","file_curator_role":"community","annotation_file_curators":[{"name":"Silke Hauf","community_curator":true,"annotation_count":32,"orcid":"0000-0001-5938-721X","file_type":"quantitative_gene_expression","file_name":"PMID_24161933_Heinrich_protein_quantitative_expression.txt"}],"genes":["SPCC1322.12c","SPAC959.09c","SPBC20F10.06","SPAC821.08c","SPBC3D6.04c","SPAC23H3.08c","SPBC83.04","SPCC1795.01c","SPBC106.01","SPAC6F12.15c","SPCC1223.02"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2020-06-03"},{"uniquename":"PMID:18059475","title":"Cdc2p controls the forkhead transcription factor Fkh2p by phosphorylation during sexual differentiation in fission yeast.","citation":"EMBO J 2008 Jan 09;27(1):132-42","abstract":"In most eukaryotes, cyclin-dependent kinases (Cdks) play a central role in control of cell-cycle progression. Cdks are inactivated from the end of mitosis to the start of the next cell cycle as well as during sexual differentiation. The forkhead-type transcription factor Fkh2p is required for the periodic expression of many genes and for efficient mating in the fission yeast Schizosaccharomyces pombe. However, the mechanism responsible for coordination of cell-cycle progression with sexual differentiation is still unknown. We now show that Fkh2p is phosphorylated by Cdc2p (Cdk1) and that phosphorylation of Fkh2p on T314 or S462 by this Cdk blocks mating in S. pombe by preventing the induction of ste11+ transcription, which is required for the onset of sexual development. We propose that functional interaction between Cdks and forkhead transcription factors may link the mitotic cell cycle and sexual differentiation.","authors":"Shimada M, Yamada-Namikawa C, Murakami-Tonami Y, Yoshida T, Nakanishi M, Urano T, Murakami H","authors_abbrev":"Shimada M et al.","pubmed_publication_date":"09 Jan 2008","pubmed_entrez_date":"2007-12-07","publication_year":"2008","canto_session_key":"5fd244fcaaf1c2fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-29 15:28:50","canto_approved_date":"2026-04-08 10:47:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-22 15:18:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":49,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.08c","SPBC582.03","SPBC16G5.15c","SPBC4C3.12","SPAC1142.08","SPAPB2B4.03","SPBC32C12.02","SPBC32H8.11","SPBC11B10.09","SPAC20G8.05c","SPAC3F10.15c"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2018-08-29"},{"uniquename":"PMID:41206762","title":"Species-specific production of nitrogen signaling factors that mediate cell-cell communication in yeast.","citation":"Biosci Biotechnol Biochem 2025 Nov 08;","abstract":"In the fission yeast Schizosaccharomyces pombe, 10(R)-acetoxy-8(Z)-octadecenoic acid and 10(R)-hydroxy-8(Z)-octadecenoic acid (collectively termed nitrogen signaling factors, NSFs), function as signaling molecules mediating cell-cell communication in nitrogen catabolite repression. However, it remains unclear whether production of these compounds is conserved across related yeasts. Here, we developed a sensitive liquid chromatography-mass spectrometry-based method for their absolute quantification and applied it to diverse yeast species. Both compounds were detected in Schizosaccharomyces octosporus, Schizosaccharomyces osmophilus, Schizosaccharomyces cryophilus as well as in S. pombe, but not in Schizosaccharomyces japonicus or Saccharomyces cerevisiae. Moreover, natural isolates of S. pombe produced levels similar to or lower than those of the laboratory strain. These findings indicate that the ability to produce NSFs is partially conserved within the Schizosaccharomyces genus and suggest that these molecules are utilized across related species in nature.","doi":"10.1093/bbb/zbaf165","authors":"Li H, Usui M, Matoba H, Hirai G, Yoshida M, Yashiroda Y","authors_abbrev":"Li H et al.","pubmed_publication_date":"08 Nov 2025","pubmed_entrez_date":"2025-11-09","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-11-10 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7736356","title":"Pattern of polar extension of the cell wall in the fission yeast Schizosaccharomyces pombe.","citation":"Can J Microbiol 1995 Mar;41(3):273-7","abstract":"The indirect fluorescent-antibody technique has been used to establish the pattern of polar extension in the fission yeast Schizosaccharomyces pombe 160 over a complete cell cycle in liquid medium, thus avoiding the possibility of perturbations being introduced by growth on an agar pad, which is the technique used in most other investigations. Nearly all of the cells (about 98%) showed more growth at the old end than at the new end that was formed by cleavage of the septum at the previous division. Importantly, there was no evidence of the abnormal growth pattern (i.e., the significant contribution of new ends to extension) in cells of S. pombe growing on agar pads reported by Miyata et al. (H. Miyata, M. Miyata, and B.F. Johnson. 1986. Can. J. Microbiol. 32: 528-530 and 1990. Can. J. Microbiol. 36: 390-394). In addition, extension over the cycle was inversely related to birth length (cells shorter than the mean at birth tended to produce daughter cells longer than themselves and vice versa), there was a small but significant asymmetry in the position of the septum, and the time of initiation of extension at the new end was estimated at about 0.24 of the cycle.","authors":"May JW, Mitchison JM","authors_abbrev":"May JW et al.","pubmed_publication_date":"Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15337454","title":"Refinement of the structures of cell-wall glucans of Schizosaccharomyces pombe by chemical modification and NMR spectroscopy.","citation":"Carbohydr Res 2004 Sep 13;339(13):2255-65","abstract":"Alkali extraction and methylation analyses in the 1970s revealed that the cell walls of the yeast Schizosaccharomyces pombe contain a (1-->3)-alpha-d-glucan, a (1-->3)-beta-d-glucan, a (1-->6)-beta-d-glucan, and a alpha-galactomannan. To refine the structures of these polysaccharides, cell-wall glucans of S. pombe were extracted, fractionated, and analyzed by NMR spectroscopy. S. pombe cells were treated with 3% NaOH, and alkali-soluble and insoluble fractions were prepared. The alkali-insoluble fraction was treated with 0.5M acetic acid or Zymolyase 100T to yield an alkali-insoluble, acetic acid-insoluble fraction, an alkali-insoluble, Zymolyase-insoluble fraction, and an alkali-insoluble, Zymolyase-soluble fraction. (13)C NMR and 2D-NMR spectra disclosed that the cell wall of S. pombe is composed of three types of glucans, specifically, a (1-->3)-alpha-d-glucan, a (1-->3)-beta-d-glucan, which may either be linear or slightly branched, and a highly branched (1-->6)-beta-d-glucan, in addition to alpha-galactomannan. The highly branched (1-->6)-beta-d-glucan was identified by selective periodate degradation of side-chain glucose as a highly (1-->3)-beta-branched (1-->6)-beta-d-glucan with more branches than that of Saccharomyces cerevisiae. Flexibility of these polysaccharides in the cell wall was analyzed by (13)C NMR spectra in D(2)O. The data collectively indicate that (1-->3)-alpha- and (1-->3)-beta-d-glucans are rigid and contribute to the cell shape, while the highly branched (1-->6)-beta-d-glucan and alpha-galactomannan are flexible.","authors":"Sugawara T, Takahashi S, Osumi M, Ohno N","authors_abbrev":"Sugawara T et al.","pubmed_publication_date":"13 Sep 2004","pubmed_entrez_date":"2004-09-01","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7796804","title":"A pre-start checkpoint preventing mitosis in fission yeast acts independently of p34cdc2 tyrosine phosphorylation.","citation":"EMBO J 1995 Jun 15;14(12):2760-71","abstract":"We have monitored the tyrosine (Y15) phosphorylated and dephosphorylated forms of p34cdc2 from Schizosaccharomyces pombe as cells proceed through the cell cycle. Y15 is dephosphorylated in G1 before start and becomes phosphorylated only after cells pass start and enter late G1. This transition is associated with a switch from one checkpoint which restrains mitosis in pre-start G1, by a mechanism independent from Y15 phosphorylation, to a second checkpoint acting post-start during late G1 and S phase operating through Y15 phosphorylation. The pre-start checkpoint may act by preventing formation of the p34cdc2/p56cdc13 complex. The complex between Y15-phosphorylated p34cdc2 and p56cdc13 accumulates during S phase and G2, but the level generated is not solely dependent on the amount of p34cdc2 and p56cdc13 present in the cell. The extent of p56cdc13 breakdown at the end of mitosis may be determined by the amount complexed with p34cdc2. We have also shown that an insoluble form of p34cdc2 is associated with the progression of the cell through late G1 into S phase.","authors":"Hayles J, Nurse P","authors_abbrev":"Hayles J et al.","pubmed_publication_date":"15 Jun 1995","pubmed_entrez_date":"1995-06-15","publication_year":"1995","canto_session_key":"3d3eef26565fa966","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-11-15 15:20:10","canto_approved_date":"2026-01-29 19:45:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-27 10:48:52","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":29,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC25H2.13c","SPBC660.14","SPCC1259.13","SPBC11B10.09","SPAC24H6.05","SPAC1F7.05","SPBC336.12c","SPAC20G4.04c","SPBC582.03"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2017-11-15"},{"uniquename":"PMID:21060862","title":"Continuous requirement for the Clr4 complex but not RNAi for centromeric heterochromatin assembly in fission yeast harboring a disrupted RITS complex.","citation":"PLoS Genet 2010 Oct 28;6(10):e1001174","abstract":"Formation of centromeric heterochromatin in fission yeast requires the combined action of chromatin modifying enzymes and small RNAs derived from centromeric transcripts. Positive feedback mechanisms that link the RNAi pathway and the Clr4/Suv39h1 histone H3K9 methyltransferase complex (Clr-C) result in requirements for H3K9 methylation for full siRNA production and for siRNA production to achieve full histone methylation. Nonetheless, it has been proposed that the Argonaute protein, Ago1, is the key initial trigger for heterochromatin assembly via its association with Dicer-independent \"priRNAs.\" The RITS complex physically links Ago1 and the H3-K9me binding protein Chp1. Here we exploit an assay for heterochromatin assembly in which loss of silencing by deletion of RNAi or Clr-C components can be reversed by re-introduction of the deleted gene. We showed previously that a mutant version of the RITS complex (Tas3(WG)) that biochemically separates Ago1 from Chp1 and Tas3 proteins permits maintenance of heterochromatin, but prevents its formation when Clr4 is removed and re-introduced. Here we show that the block occurs with mutants in Clr-C, but not mutants in the RNAi pathway. Thus, Clr-C components, but not RNAi factors, play a more critical role in assembly when the integrity of RITS is disrupted. Consistent with previous reports, cells lacking Clr-C components completely lack H3K9me2 on centromeric DNA repeats, whereas RNAi pathway mutants accumulate low levels of H3K9me2. Further supporting the existence of RNAi-independent mechanisms for establishment of centromeric heterochromatin, overexpression of clr4(+) in clr4Δago1Δ cells results in some de novo H3K9me2 accumulation at centromeres. These findings and our observation that ago1Δ and dcr1Δ mutants display indistinguishable low levels of H3K9me2 (in contrast to a previous report) challenge the model that priRNAs trigger heterochromatin formation. Instead, our results indicate that RNAi cooperates with RNAi-independent factors in the assembly of heterochromatin.","doi":"10.1371/journal.pgen.1001174","authors":"Shanker S, Job G, George OL, Creamer KM, Shaban A, Partridge JF","authors_abbrev":"Shanker S et al.","pubmed_publication_date":"28 Oct 2010","pubmed_entrez_date":"2010-11-10","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC83.03c","SPCC11E10.08","SPAC3A11.08","SPCC613.12c","SPCC970.07c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:20338033","title":"Genome-wide characterisation of the Gcn5 histone acetyltransferase in budding yeast during stress adaptation reveals evolutionarily conserved and diverged roles.","citation":"BMC Genomics 2010 Mar 25;11:200","abstract":"Gcn5 is a transcriptional coactivator with histone acetyltransferase activity that is conserved with regard to structure as well as its histone substrates throughout the eukaryotes. Gene regulatory networks within cells are thought to be evolutionarily diverged. The use of evolutionarily divergent yeast species, such as S. cerevisiae and S. pombe, which can be studied under similar environmental conditions, provides an opportunity to examine the interface between conserved regulatory components and their cellular applications in different organisms.\nWe show that Gcn5 is important for a common set of stress responses in evolutionarily diverged yeast species and that the activity of the conserved histone acetyltransferase domain is required. We define a group of KCl stress response genes in S. cerevisiae that are specifically dependent on Gcn5. Gcn5 is localised to many Gcn5-dependent genes including Gcn5 repressed targets such as FLO8. Gcn5 regulates divergent sets of KCl responsive genes in S. cerevisiae and S. pombe. Genome-wide localization studies showed a tendency for redistribution of Gcn5 during KCl stress adaptation in S. cerevisiae from short genes to the transcribed regions of long genes. An analogous redistribution was not observed in S. pombe.\nGcn5 is required for the regulation of divergent sets of KCl stress-response genes in S. cerevisiae and S. pombe even though it is required a common group of stress responses, including the response to KCl. Genes that are physically associated with Gcn5 require its activity for their repression or activation during stress adaptation, providing support for a role of Gcn5 as a corepressor as well as a coactivator. The tendency of Gcn5 to re-localise to the transcribed regions of long genes during KCl stress adaptation suggests that Gcn5 plays a specific role in the expression of long genes under adaptive conditions, perhaps by regulating transcriptional elongation as has been seen for Gcn5 in S. pombe. Interestingly an analogous redistribution of Gcn5 is not seen in S. pombe. The study thus provides important new insights in relation to why coregulators like Gcn5 are required for the correct expression of some genes but not others.","doi":"10.1186/1471-2164-11-200","authors":"Xue-Franzén Y, Johnsson A, Brodin D, Henriksson J, Bürglin TR, Wright AP","authors_abbrev":"Xue-Franzén Y et al.","pubmed_publication_date":"25 Mar 2010","pubmed_entrez_date":"2010-03-27","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2144896","title":"Immunoprecipitation distinguishes non-overlapping groups of snRNPs in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1990 Sep 11;18(17):5207-12","abstract":"The large number of snRNAs in the fission yeast Schizosaccharomyces pombe can be divided into four non-overlapping groups by immunoprecipitation with antibodies directed against mammalian snRNP proteins. 1) Of the abundant snRNAs, anti-Sm sera precipitate only the spliceosomal snRNAs U1, U2, U4, U5 and U6. Surprisingly, three Sm-sera tested distinguish between U2, U4 and U5 and U1 from S.pombe; one precipitating only U1 and two precipitating U2, U4 and U5 but not U1. 2) A group of 11 moderately abundant snRNAs are not detectably precipitated by human anti-Sm sera, but are specifically precipitated by monoclonal antibody H57 specific for the human B/B' polypeptides. From Aspergillus nidulans this antibody also precipitates at least 12 snRNAs. 3) Anti-(U3)RNP sera do not precipitate the above snRNAs, but precipitate at least 6 further snRNAs, including the homologues of U3. Both the anti-(U3)RNP sera and H57 also efficiently precipitate a number of discrete non-capped RNAs. 4) A small number of additional snRNAs are not detectably precipitated by any anti-serum tested to date, further analysis may identify antisera specific for these snRNPs. Western blots of purified snRNP proteins were used to identify the S.pombe proteins responsible for these immunoprecipitations. Several Sm-sera decorate a 16.3kD protein which may be a D protein homologue, monoclonal H57 decorates a further protein of 16kD and an anti-(U3)RNP serum decorates the homologue of the 36kD U3-specific protein, fibrillarin.","authors":"Tollervey D, Tessars G, Lührmann R","authors_abbrev":"Tollervey D et al.","pubmed_publication_date":"11 Sep 1990","pubmed_entrez_date":"1990-09-11","publication_year":"1990","canto_session_key":"72876004f5f70ac3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-18 19:53:56","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-18 19:52:00","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.06","SPSNRNA.01","SPSNRNA.04","SPSNRNA.02","SPSNRNA.05"],"gene_count":5,"ltp_gene_count":0,"approved_date":"2014-06-18"},{"uniquename":"PMID:10718616","title":"Backbone NMR assignment of the 19 kDa translationally controlled tumor-associated protein p23fyp from Schizosaccharomyces pombe.","citation":"J Biomol NMR 2000 Jan;16(1):83-4","abstract":"","authors":"Baxter NJ, Thaw P, Higgins LD, Sedelnikova SE, Bramley AL, Price C, Waltho JP, Craven CJ","authors_abbrev":"Baxter NJ et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-03-16","publication_year":"2000","canto_session_key":"4bd3f2cdd88e2551","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 10:08:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-20 10:08:42","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F12.02c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:32610137","title":"Promiscuous Binding of Microprotein Mozart1 to γ-Tubulin Complex Mediates Specific Subcellular Targeting to Control Microtubule Array Formation.","citation":"Cell Rep 2020 Jun 30;31(13):107836","abstract":"How γ-tubulin ring complex (γ-TuRC), a master template for microtubule nucleation, is spatially and temporally regulated for the assembly of new microtubule arrays remains unclear. Here, we report that an evolutionarily conserved microprotein, Mozart1 (Mzt1), regulates subcellular targeting and microtubule formation activity of γ-TuRC at different cell cycle stages. Crystal structures of protein complexes demonstrate that Mzt1 promiscuously interacts with the N-terminal domains of multiple γ-tubulin complex protein subunits in γ-TuRC via an intercalative binding mode. Genetic- and microscopy-based analyses show that promiscuous binding of Mzt1 in γ-TuRC controls specific subcellular localization of γ-TuRC to modulate microtubule nucleation and stabilization in fission yeast. Moreover, we find Mzt1-independent targeting of γ-TuRC to be crucial for mitotic spindle assembly, demonstrating the cell-cycle-dependent regulation and function of γ-TuRC. Our findings reveal a microprotein-mediated regulatory mechanism underlying microtubule cytoskeleton formation, whereby Mzt1 binding promiscuity confers localization specificity on the multi-protein complex γ-TuRC.","doi":"10.1016/j.celrep.2020.107836","authors":"Huang TL, Wang HJ, Chang YC, Wang SW, Hsia KC","authors_abbrev":"Huang TL et al.","pubmed_publication_date":"30 Jun 2020","pubmed_entrez_date":"2020-07-02","publication_year":"2020","canto_session_key":"c2090d25fb675f86","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-07-03 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC806.08c","SPAC9G1.15c"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"6l80","gene_chains":[{"gene_uniquename":"SPAC9G1.15c","chain":"B/D","position":"1-64"},{"gene_uniquename":"SPAC806.08c","chain":"A/C","position":"1-109"}],"title":"Crystal structure of pombe Mod21 N-terminus and Mozart1","entry_authors":"Huang TL,Wang HJ,Wang SW,Hsia KC","entry_authors_abbrev":"Huang TL et al.","reference_uniquename":"PMID:32610137","experimental_method":"X-ray","resolution":"2.0004976"}]},{"uniquename":"PMID:17340144","title":"Modeling the septation initiation network (SIN) in fission yeast cells.","citation":"Curr Genet 2007 Apr;51(4):245-55","abstract":"Cytokinesis in fission yeast is controlled by a signal transduction pathway called the Septation Initiation Network (SIN). From a dynamical point of view the most interesting questions about the regulation of fission yeast cytokinesis are: how do wild type cells ensure that septation is initiated only once per cycle? Why does the control system stay in a continuously septating state in some mutant strains? And how is it that the SIN remains active when cytokinesis fails? To answer these questions we construct a simplified mathematical model of the SIN and graft this regulatory module onto our previous model of cyclin-dependent kinase (Cdk) dynamics in fission yeast cells. The SIN is both activated and inhibited by mitotic Cdk/cyclin complexes. As a consequence of this dual regulation, the SIN gets activated only once at the end of mitosis, when Cdk activity drops. The mathematical model describes the timing of septation not only in wild type cells but also in mutants where components of the SIN are knocked out. The model predicts phenotypes of some uncharacterized mutant cells and shows how a cytokinesis checkpoint can stop the cell cycle if septation fails.","authors":"Csikász-Nagy A, Kapuy O, Gyorffy B, Tyson JJ, Novák B","authors_abbrev":"Csikász-Nagy A et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-03-07","publication_year":"2007","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38801067","title":"Repression of pervasive antisense transcription is the primary role of fission yeast RNA polymerase II CTD serine 2 phosphorylation.","citation":"Nucleic Acids Res 2024 May 27;","abstract":"The RNA polymerase II carboxy-terminal domain (CTD) consists of conserved heptapeptide repeats that can be phosphorylated to influence distinct stages of the transcription cycle, including RNA processing. Although CTD-associated proteins have been identified, phospho-dependent CTD interactions have remained elusive. Proximity-dependent biotinylation (PDB) has recently emerged as an alternative approach to identify protein-protein associations in the native cellular environment. In this study, we present a PDB-based map of the fission yeast RNAPII CTD interactome in living cells and identify phospho-dependent CTD interactions by using a mutant in which Ser2 was replaced by alanine in every repeat of the fission yeast CTD. This approach revealed that CTD Ser2 phosphorylation is critical for the association between RNAPII and the histone methyltransferase Set2 during transcription elongation, but is not required for 3' end processing and transcription termination. Accordingly, loss of CTD Ser2 phosphorylation causes a global increase in antisense transcription, correlating with elevated histone acetylation in gene bodies. Our findings reveal that the fundamental role of CTD Ser2 phosphorylation is to establish a chromatin-based repressive state that prevents cryptic intragenic transcription initiation.","doi":"10.1093/nar/gkae436","authors":"Boulanger C, Haidara N, Yague-Sanz C, Larochelle M, Jacques PÉ, Hermand D, Bachand F","authors_abbrev":"Boulanger C et al.","pubmed_publication_date":"27 May 2024","pubmed_entrez_date":"2024-05-27","publication_year":"2024","canto_session_key":"55b19e9ebe24eac2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-05-27 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11244061","title":"Functional characterization of alanine racemase from Schizosaccharomyces pombe: a eucaryotic counterpart to bacterial alanine racemase.","citation":"J Bacteriol 2001 Apr;183(7):2226-33","abstract":"Schizosaccharomyces pombe has an open reading frame, which we named alr1(+), encoding a putative protein similar to bacterial alanine racemase. We cloned the alr1(+) gene in Escherichia coli and purified the gene product (Alr1p), with an M(r) of 41,590, to homogeneity. Alr1p contains pyridoxal 5'-phosphate as a coenzyme and catalyzes the racemization of alanine with apparent K(m) and V(max) values as follows: for L-alanine, 5.0 mM and 670 micromol/min/mg, respectively, and for D-alanine, 2.4 mM and 350 micromol/min/mg, respectively. The enzyme is almost specific to alanine, but L-serine and L-2-aminobutyrate are racemized slowly at rates 3.7 and 0.37% of that of L-alanine, respectively. S. pombe uses D-alanine as a sole nitrogen source, but deletion of the alr1(+) gene resulted in retarded growth on the same medium. This indicates that S. pombe has catabolic pathways for both enantiomers of alanine and that the pathway for L-alanine coupled with racemization plays a major role in the catabolism of D-alanine. Saccharomyces cerevisiae differs markedly from S. pombe: S. cerevisiae uses L-alanine but not D-alanine as a sole nitrogen source. Moreover, D-alanine is toxic to S. cerevisiae. However, heterologous expression of the alr1(+) gene enabled S. cerevisiae to grow efficiently on D-alanine as a sole nitrogen source. The recombinant yeast was relieved from the toxicity of D-alanine.","authors":"Uo T, Yoshimura T, Tanaka N, Takegawa K, Esaki N","authors_abbrev":"Uo T et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-03-13","publication_year":"2001","canto_session_key":"4ea854110d54d22c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-05 08:23:07","canto_approved_date":"2025-09-24 19:45:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-23 14:06:31","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC965.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-05"},{"uniquename":"PMID:22326183","title":"The utility of porous graphitic carbon as a stationary phase in proteomics workflows: two-dimensional chromatography of complex peptide samples.","citation":"J Chromatogr A 2012 Apr 06;1232:276-80","abstract":"We present the first investigation into the utility of porous graphitic carbon (PGC) as a stationary phase in proteomic workflows involving complex samples. PGC offers chemical and physical robustness and is capable of withstanding extremes of pH and higher temperatures than traditional stationary phases, without the likelihood of catastrophic failure. In addition, unlike separations driven by ion exchange mechanisms, there is no requirement for high levels of non-volatile salts such as potassium chloride in the elution buffers, which must be removed prior to LC-MS analysis. Here we present data which demonstrate that PGC affords excellent peptide separation in a complex whole cell lysate digest sample, with good orthogonality to a typical low pH reversed-phase system. As strong cation exchange (SCX) is currently the most popular first dimension for 2D peptide separations, we chose to compare the performance of a PGC and SCX separation as the first dimension in a comprehensive 2D-LC-MS/MS workflow. A significant increase, in the region of 40%, in peptide identifications is reported with off-line PGC fractionation compared to SCX. Around 14,000 unique peptides were identified at an estimated false discovery rate of 1% (n=3 replicates) from starting material constituting only 100 μg of protein extract.","doi":"10.1016/j.chroma.2012.01.015","authors":"Griffiths JR, Perkins S, Connolly Y, Zhang L, Holland M, Barattini V, Pereira L, Edge A, Ritchie H, Smith DL","authors_abbrev":"Griffiths JR et al.","pubmed_publication_date":"06 Apr 2012","pubmed_entrez_date":"2012-02-14","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39666777","title":"Fission yeast essential nuclear pore protein Nup211 regulates the expression of genes involved in cytokinesis.","citation":"PLoS One 2024;19(12):e0312095","abstract":"Nuclear pore proteins control nucleocytoplasmic transport; however, certain nucleoporins play regulatory roles in activities such as transcription and chromatin organization. The fission yeast basket nucleoporin Nup211 is implicated in mRNA export and is essential for cell viability. Nup211 preferentially associates with heterochromatin, however, it is unclear whether it plays a role in regulating transcription. To better understand its functions, we constructed a nup211 \"shut-off\" strain and observed that Nup211 depletion led to severe defects in cell cycle progression, including septation and cytokinesis. Using RNA-Seq and RT-qPCR, we revealed that loss of Nup211 significantly altered the mRNA levels of a set of genes crucial for cell division. Using domain analysis and CRISPR/cas9 technology, we determined that the first 655 residues of Nup211 are sufficient for viability. This truncated protein was detected at the nuclear periphery. Furthermore, exogenous expression of this domain in nup211 shut-off cells effectively restored both cell morphology and transcript abundance for some selected genes. Our findings unveil a novel role for Nup211 in regulating gene expression.","doi":"10.1371/journal.pone.0312095","authors":"Kamel D, Sookdeo A, Ikenouchi A, Zhong H","authors_abbrev":"Kamel D et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-12-12","publication_year":"2024","canto_session_key":"e5d482e80f83526c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Domenick Kamel","canto_first_approved_date":"2025-03-12 15:54:16","canto_approved_date":"2025-03-12 15:54:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-05 17:32:19","canto_added_date":"2024-12-13 00:25:05","annotation_curators":[{"name":"Domenick Kamel","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC162.08c","SPAPJ760.03c","SPBC19G7.05c","SPBC4F6.12","SPBC19G7.06","SPAC2F7.03c","SPBC11C11.05","SPBC29B5.01","SPAC14C4.09","SPBC646.06c"],"gene_count":10,"ltp_gene_count":1,"approved_date":"2025-03-12"},{"uniquename":"PMID:26343233","title":"A vector system for efficient and economical switching of a ura4(+) module to three commonly used antibiotic marker cassettes in Schizosaccharomyces pombe.","citation":"Yeast 2015 Nov;32(11):671-82","abstract":"We describe here the development of a set of plasmid vectors that allow simple, efficient and economical switching of a ura4(+) module in existing Schizosaccharomyces pombe strains to any of the three routinely used antibiotic marker cassettes, kanMX6, hphMX6 and natMX6. In principle, the applications of this system can also be extended to switching ura4(+) for additional MX6 module-based cassettes, such as bleMX6, as long as the antibiotic marker has been cloned into an ura4(+) module-switching vector. We illustrate the application of this set of vectors in exchange of the ura4(+) marker in existing strains with three antibiotic marker cassettes with high efficiency.","doi":"10.1002/yea.3088","authors":"Chen Y, Chen L, An K, Wang Y, Jin Q","authors_abbrev":"Chen Y et al.","pubmed_publication_date":"Nov 2015","pubmed_entrez_date":"2015-09-08","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-09-09 00:19:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9930653","title":"Effects of the myosin inhibitor 2,3-butanedione monoxime on the physiology of fission yeast.","citation":"Eur J Cell Biol 1998 Dec;77(4):284-93","abstract":"F-actin and associated myosins are thought to take part in a wide range of cellular processes, like motility and contraction, polarized growth, and secretion. The reagent 2,3-butanedione monoxime (BDM) is a well characterized inhibitor of the contraction of vertebrate muscle that reversibly affects myosin function and influences the intracellular concentration of Ca2+. Here we describe the influence of BDM on growth and division of the fission yeast Schizosaccharomyces pombe. At concentrations from 1-30 mM, BDM gradually inhibited formation and growth of S. pombe colonies on agar plates, with a lethal effect at > or = 15 mM. In strains of S. pombe that were blocked by elevated temperature from entry into mitosis, drug treatment reversibly decreased microtubule-independent tip growth and septation, with an IC50 value around 12 mM; nuclear division, on the other hand, was essentially unaffected by up to 15 mM BDM. At 30 mM BDM the secretion of invertase, which required both F-actin and microtubules, was decreased to the same extent as that seen when cytochalasin D was used to disrupt F-actin. However, the actin cytoskeleton was insensitive to up to 10 mM BDM, while the actin patches lost their polar distribution at 20-30 mM BDM. Cells treated with 5-20 mM BDM for 3 hours and then high pressure frozen did not show an accumulation of secretory vesicles. However, 10 mM BDM treatment disorganized the fungal cell wall, resulting in some unusually thick parts lying next to regions were the wall was almost absent. These defects could be rescued by incubating the cells in inhibitors of glucanases. Osmolytic stabilization with sorbitol rescued the effect of 15 mM BDM on colony survival, indicating that the secretion of wall components and/or wall-modifying enzymes may be the principal reason for cell death caused by BDM. Our results are consistent with the hypothesis that BDM influences actin-dependent processes in fission yeast and that actomyosin-dependent motility contributes to the secretory process of tip growth.","authors":"Steinberg G, McIntosh JR","authors_abbrev":"Steinberg G et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1999-02-04","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF07297","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21B10.11","YIL102C-A"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:14687915","title":"The translationally controlled tumour protein (TCTP).","citation":"Int J Biochem Cell Biol 2004 Mar;36(3):379-85","abstract":"The translationally controlled tumour protein (TCTP) is a highly conserved protein that is widely expressed in all eukaryotic organisms. Based on its sequence, TCTP was listed as a separate protein family in protein databases but the recent elucidation of the solution structure of the fission yeast orthologue places it close to a family of small chaperone proteins. The molecular functions determined so far, Ca(2+)- and microtubule-binding, have been mapped to an alpha-helical region of the molecule. TCTP expression is highly regulated both at the transcriptional and translational level and by a wide range of extracellular signals. TCTP has been implicated in important cellular processes, such as cell growth, cell cycle progression, malignant transformation and in the protection of cells against various stress conditions and apoptosis. In addition, an extracellular, cytokine-like function has been established for TCTP, and the protein has been implicated in various medically relevant processes.","authors":"Bommer UA, Thiele BJ","authors_abbrev":"Bommer UA et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2003-12-23","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23151475","title":"RNAi triggered by specialized machinery silences developmental genes and retrotransposons.","citation":"Nature 2013 Jan 24;493(7433):557-60","abstract":"RNA interference (RNAi) is a conserved mechanism in which small interfering RNAs (siRNAs) guide the degradation of cognate RNAs, but also promote heterochromatin assembly at repetitive DNA elements such as centromeric repeats. However, the full extent of RNAi functions and its endogenous targets have not been explored. Here we show that, in the fission yeast Schizosaccharomyces pombe, RNAi and heterochromatin factors cooperate to silence diverse loci, including sexual differentiation genes, genes encoding transmembrane proteins, and retrotransposons that are also targeted by the exosome RNA degradation machinery. In the absence of the exosome, transcripts are processed preferentially by the RNAi machinery, revealing siRNA clusters and a corresponding increase in heterochromatin modifications across large domains containing genes and retrotransposons. We show that the generation of siRNAs and heterochromatin assembly by RNAi is triggered by a mechanism involving the canonical poly(A) polymerase Pla1 and an associated RNA surveillance factor Red1, which also activate the exosome. Notably, siRNA production and heterochromatin modifications at these target loci are regulated by environmental growth conditions, and by developmental signals that induce gene expression during sexual differentiation. Our analyses uncover an interaction between RNAi and the exosome that is conserved in Drosophila, and show that differentiation signals modulate RNAi silencing to regulate developmental genes.","doi":"10.1038/nature11716","authors":"Yamanaka S, Mehta S, Reyes-Turcu FE, Zhuang F, Fuchs RT, Rong Y, Robb GB, Grewal SI","authors_abbrev":"Yamanaka S et al.","pubmed_publication_date":"24 Jan 2013","pubmed_entrez_date":"2012-11-16","publication_year":"2013","canto_session_key":"3b95a13f67aa0090","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-07-03 08:03:41","canto_approved_date":"2025-07-03 08:03:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-07-03 08:03:35","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":51,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.04","SPAC1006.03c","SPAC14C4.05c","SPBC428.08c","SPAC14C4.03","SPAC1F3.01","SPAC6F12.09","SPCC1442.04c","SPAC14C4.08","SPCC736.11","SPAPB15E9.03c","SPAC4A8.05c","SPCC188.13c","SPBC16E9.12c","SPAC14C4.07"],"gene_count":15,"ltp_gene_count":9,"approved_date":"2025-07-03"},{"uniquename":"EMBL:AB084859","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.47"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17308035","title":"Conservation of a masked nuclear export activity of La proteins and its effects on tRNA maturation.","citation":"Mol Cell Biol 2007 May;27(9):3303-12","abstract":"La is an RNA-processing-associated phosphoprotein so highly conserved that the human La protein (hLa) can replace the tRNA-processing function of the fission yeast La protein (Sla1p) in vivo. La proteins contain multiple trafficking elements that support interactions with RNAs in different subcellular locations. Prior data indicate that deletion of a nuclear retention element (NRE) causes nuclear export of La and dysfunctional processing of associated pre-tRNAs that are spliced but 5' and 3' unprocessed, with an accompanying decrease in tRNA-mediated suppression, in fission yeast. To further pursue these observations, we first identified conserved residues in the NREs of hLa and Sla1p that when substituted mimic the NRE deletion phenotype. NRE-defective La proteins then deleted of other motifs indicated that RNA recognition motif 1 (RRM1) is required for nuclear export. Mutations of conserved RRM1 residues restored nuclear accumulation of NRE-defective La proteins. Some RRM1 mutations restored nuclear accumulation, prevented disordered pre-tRNA processing, and restored suppression, indicating that the tRNA-related activity of RRM1 and its nuclear export activity could be functionally separated. When mapped onto an hLa structure, the export-sensitive residues comprised surfaces distinct from the RNA-binding surface of RRM1. The data indicate that the NRE has been conserved to mask or functionally override an equally conserved nuclear export activity of RRM1. The data suggest that conserved elements mediate nuclear retention, nuclear export, and RNA-binding activities of the multifunctional La protein and that their interrelationship contributes to the ability of La to engage its different classes of RNA ligands in different cellular locations.","authors":"Bayfield MA, Kaiser TE, Intine RV, Maraia RJ","authors_abbrev":"Bayfield MA et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-02-20","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A10.10c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:22562166","title":"Synthesis and production of unsaturated and polyunsaturated fatty acids in yeast: current state and perspectives.","citation":"Appl Microbiol Biotechnol 2012 Jul;95(1):1-12","abstract":"Recently, many genes involved in the formation of unsaturated and polyunsaturated fatty acids (PUFAs) were isolated. In most cases, their activities were confirmed by expressing them in the well-studied model organism Saccharomyces cerevisiae because its fatty acid compositions are very simple and it does not contain PUFAs. Taking advantage of its genetic tractability and increasing wealth of accessible data, many groups are attempting to produce various useful fatty acids in the model yeasts, mainly in S. cerevisiae. This review describes typical such examples including a very recent study on the expression of a fatty acid hydroxylase gene in fission yeast Schizosaccharomyces pombe. Furthermore, the impact of the genetically engineered alteration of fatty acid composition on the stress tolerance is presented because unsaturated fatty acids have crucial roles in membrane fluidity and signaling processes. Lastly, recent attempts at increasing lipid content in S. cerevisiae are discussed.","doi":"10.1007/s00253-012-4105-1","authors":"Uemura H","authors_abbrev":"Uemura H","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-05-08","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ617313","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8346680","title":"Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe.","citation":"Yeast 1993 Jun;9(6):637-44","abstract":"Aminopeptidase yspI was purified to apparent homogeneity from the fission yeast Schizosaccharomyces pombe. The molecular mass of the native enzyme was estimated to be 184 kDa by gel filtration chromatography. A value of 92 kDa was calculated after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is thus a dimer with two identical subunits. Optimum pH for cleavage of synthetic aminoacyl-4-nitroanilides is 7.0. Mercury ions, EDTA and chloroquine were found to be potent inhibitors of aminopeptidase yspI activity. Substrate specificity studies indicate that the purified enzyme cleaves L-lysine-4-nitroanilide with high efficiency.","authors":"Arbesú MJ, Valle E, Suárez-Rendueles P","authors_abbrev":"Arbesú MJ et al.","pubmed_publication_date":"Jun 1993","pubmed_entrez_date":"1993-06-01","publication_year":"1993","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27803256","title":"Micrococcal Nuclease Digestion of Schizosaccharomyces pombe Chromatin.","citation":"Cold Spring Harb Protoc 2016 Nov 01;2016(11)","abstract":"Digestion of chromatin with micrococcal nuclease (MNase) is widely used to probe nucleosome organization. Analysis of MNase digests by end-labeling techniques or overlapping quantitative polymerase chain reaction (qPCR) can be used to map locus-specific nucleosome positions. Furthermore, the application of genomic technologies can provide genome-wide views of nucleosome position and occupancy. This protocol provides a basic method for MNase digestion of Schizosaccharomyces pombe chromatin and depends on the production of permeabilized spheroplasts.","doi":"10.1101/pdb.prot091538","authors":"Cam HP, Whitehall S","authors_abbrev":"Cam HP et al.","pubmed_publication_date":"01 Nov 2016","pubmed_entrez_date":"2016-11-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-04 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35858772","title":"The functional analysis of the ubiquitin ligase Brl2 in the repair of DNA double-strand breaks.","citation":"Yi Chuan 2022 Jul 20;44(7):609-617","abstract":"Mono-ubiquitination of histone H2B plays a critical role in the regulation of gene transcription, DNA replication, and DNA damage repair. In Schizosaccharomyces pombe, Brl2 is an E3 ubiquitin ligase and required for the ubiquitination of H2B at lysine residue 119. Currently, there are few studies related to the function of Brl2 in DNA damage repair. Using camptothecin (CPT) to induce DNA double-strand breaks (DSBs) in S. pombe, we investigated the effect of Brl2 on DSB repair, and found that brl2-null mutants showed greater sensitivity to CPT when compared with wild-type (WT) cells, as well as having a drastically reduced spontaneous recombinant frequency. The fluorescent analysis demonstrated that Brl2 was co-localized with the recombination factor Rad52 at DSBs. Moreover, Brl2 promoted the recruitment of Rad52 to DSBs. Under CPT-induced DSBs, Brl2 was phosphorylated. These findings indicate that Brl2 plays a critical role in DNA homologous recombination and its mediated repair of DSBs.","doi":"10.16288/j.yczz.22-031","authors":"Liu XQ, Chang FR, Liu SJ, Wu F, Kong DC","authors_abbrev":"Liu XQ et al.","pubmed_publication_date":"20 Jul 2022","pubmed_entrez_date":"2022-07-20","publication_year":"2022","canto_session_key":"950a1d8d6480f647","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-07-23 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC970.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15834794","title":"Expression of Escherichia coli AppA2 phytase in four yeast systems.","citation":"Biotechnol Lett 2005 Mar;27(5):327-34","abstract":"To develop an effective fermentation system for producing Escherichia coliphytase AppA2, we expressed the enzyme in three inducible yeast systems: Saccharomyces cerevisiae (pYES2), Schizosaccharomyces pombe (pDS472a), and Pichia pastoris (pPICZ alphaA), and one constitutive system: P. pastoris (pGAPZalphaA). All four systems produced an extracellular functional AppA2 phytase with apparent molecular masses ranging from 51.5 to 56 kDa. During 8-day batch fermentation in shaking flasks, the inducible Pichia system produced the highest activity (272 units ml(-1) medium), whereas the Schizo. pombe system produced the lowest activity (2.8 units ml(-1)). The AppA2 phytase expressed in Schizo. pombe had 60-75% lower K(m)for sodium phytate and 28% higher heat-stability at 65 degrees C than that expressed in other three systems. However, all four recombinant AppA2 phytases had pH optimum at 3.5 and temperature optimum at 55 degrees C and similar efficacy in hydrolyzing phytate-phosphate from soybean meal.","authors":"Lee S, Kim T, Stahl CH, Lei XG","authors_abbrev":"Lee S et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-04-19","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26369364","title":"Mutation of histone H3 serine 86 disrupts GATA factor Ams2 expression and precise chromosome segregation in fission yeast.","citation":"Sci Rep 2015 Sep 15;5:14064","abstract":"Eukaryotic genomes are packed into discrete units, referred to as nucleosomes, by organizing around scaffolding histone proteins. The interplay between these histones and the DNA can dynamically regulate the function of the chromosomal domain. Here, we interrogated the function of a pair of juxtaposing serine residues (S86 and S87) that reside within the histone fold of histone H3. We show that fission yeast cells expressing a mutant histone H3 disrupted at S86 and S87 (hht2-S86AS87A) exhibited unequal chromosome segregation, disrupted transcriptional silencing of centromeric chromatin, and reduced expression of Ams2, a GATA-factor that regulates localization of the centromere-specific histone H3 variant CENP-A. We found that overexpression of ams2(+) could suppress the chromosome missegregation phenotype that arose in the hht2-S86AS87A mutant. We further demonstrate that centromeric localization of SpCENP-A(cnp1-1) was significantly compromised in hht2-S86AS87A, suggesting synergism between histone H3 and the centromere-targeting domain of SpCENP-A. Taken together, our work presents evidence for an uncharacterized serine residue in fission yeast histone H3 that affects centromeric integrity via regulating the expression of the SpCENP-A-localizing Ams2 protein. [173/200 words].","doi":"10.1038/srep14064","authors":"Lim KK, Ong TY, Tan YR, Yang EG, Ren B, Seah KS, Yang Z, Tan TS, Dymock BW, Chen ES","authors_abbrev":"Lim KK et al.","pubmed_publication_date":"15 Sep 2015","pubmed_entrez_date":"2015-09-16","publication_year":"2015","canto_session_key":"8acbb19b9968971d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-23 14:05:19","canto_approved_date":"2023-08-29 13:17:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-23 14:04:48","canto_added_date":"2015-09-17 00:19:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC290.04","SPBC8D2.04","SPBC1105.11c","SPAC24H6.05","SPBC1105.17","SPAC1834.04"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-10-23"},{"uniquename":"PMID:39094566","title":"Mrc1 regulates parental histone segregation and heterochromatin inheritance.","citation":"Mol Cell 2024 Jul 23;","abstract":"Chromatin-based epigenetic memory relies on the symmetric distribution of parental histones to newly synthesized daughter DNA strands, aided by histone chaperones within the DNA replication machinery. However, the mechanism of parental histone transfer remains elusive. Here, we reveal that in fission yeast, the replisome protein Mrc1 plays a crucial role in promoting the transfer of parental histone H3-H4 to the lagging strand, ensuring proper heterochromatin inheritance. In addition, Mrc1 facilitates the interaction between Mcm2 and DNA polymerase alpha, two histone-binding proteins critical for parental histone transfer. Furthermore, Mrc1's involvement in parental histone transfer and epigenetic inheritance is independent of its known functions in DNA replication checkpoint activation and replisome speed control. Instead, Mrc1 interacts with Mcm2 outside of its histone-binding region, creating a physical barrier to separate parental histone transfer pathways. These findings unveil Mrc1 as a key player within the replisome, coordinating parental histone segregation to regulate epigenetic inheritance.","doi":"10.1016/j.molcel.2024.07.002","authors":"Toda T, Fang Y, Shan CM, Hua X, Kim JK, Tang LC, Jovanovic M, Tong L, Qiao F, Zhang Z, Jia S","authors_abbrev":"Toda T et al.","pubmed_publication_date":"23 Jul 2024","pubmed_entrez_date":"2024-08-02","publication_year":"2024","canto_session_key":"392ba8f02601d540","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Songtao Jia","canto_first_approved_date":"2026-04-30 13:16:21","canto_approved_date":"2026-06-09 08:21:38","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-04-09 01:46:13","canto_added_date":"2024-08-03 23:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":68,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Songtao Jia","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC211.04c","SPAC694.06c","SPCC18B5.11c","SPBC216.06c","SPCC1682.02c","SPCC16A11.17","SPAPB1E7.02c","SPAC3H5.06c","SPBC4.04c","SPBC30D10.04","SPAC1B2.05","SPBC216.05"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2026-04-30"},{"uniquename":"PMID:20875427","title":"The roles of stress-activated Sty1 and Gcn2 kinases and of the protooncoprotein homologue Int6/eIF3e in responses to endogenous oxidative stress during histidine starvation.","citation":"J Mol Biol 2010 Nov 26;404(2):183-201","abstract":"In fission yeast, Sty1 and Gcn2 are important protein kinases that regulate gene expression in response to amino acid starvation. The translation factor subunit Int6/eIF3e promotes Sty1-dependent response by increasing the abundance of Atf1, a transcription factor targeted by Sty1. While Gcn2 promotes expression of amino acid biosynthesis enzymes, the mechanism and function of Sty1 activation and Int6/eIF3e involvement during this nutrient stress are not understood. Here we show that mutants lacking sty1(+) or gcn2(+) display reduced viabilities during histidine depletion stress in a manner suppressible by the antioxidant N-acetyl cysteine, suggesting that these protein kinases function to alleviate endogenous oxidative damage generated during nutrient starvation. Int6/eIF3e also promotes cell viability by a mechanism involving the stimulation of Sty1 response to oxidative damage. In further support of these observations, microarray data suggest that, during histidine starvation, int6Δ increases the duration of Sty1-activated gene expression linked to oxidative stress due to the initial attenuation of Sty1-dependent transcription. Moreover, loss of gcn2 induces the expression of a new set of genes not activated in wild-type cells starved for histidine. These genes encode heatshock proteins, redox enzymes, and proteins involved in mitochondrial maintenance, in agreement with the idea that oxidative stress is imposed on gcn2Δ cells. Furthermore, early Sty1 activation promotes rapid Gcn2 activation on histidine starvation. These results suggest that Gcn2, Sty1, and Int6/eIF3e are functionally integrated and cooperate to respond to oxidative stress generated during histidine starvation.","doi":"10.1016/j.jmb.2010.09.016","authors":"Nemoto N, Udagawa T, Ohira T, Jiang L, Hirota K, Wilkinson CR, Bähler J, Jones N, Ohta K, Wek RC, Asano K","authors_abbrev":"Nemoto N et al.","pubmed_publication_date":"26 Nov 2010","pubmed_entrez_date":"2010-09-30","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPBC646.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8330264","title":"Caffeine tolerance in Schizosaccharomyces pombe: physiological adaptation and interaction with theophylline.","citation":"Can J Microbiol 1993 May;39(5):551-4","abstract":"Caffeine at concentrations of 8 mM or higher inhibited cell propagation and killed a fraction of the population. Cell inactivation increased incrementally with increasing concentrations. The survivors developed tolerance by physiological adaptation that enabled them to propagate in the presence of the drug, but the tolerance could easily be lost if the cells grew in the absence of caffeine for a few generations. Theophylline was found to diminish the toxic effect of caffeine. Possible mechanisms for the observed cellular response and its implications for studies of the effects of these drugs in eukaryotes are discussed.","authors":"Benkö Z, Sipiczki M","authors_abbrev":"Benkö Z et al.","pubmed_publication_date":"May 1993","pubmed_entrez_date":"1993-05-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18562696","title":"The meiosis-specific Sid2p-related protein Slk1p regulates forespore membrane assembly in fission yeast.","citation":"Mol Biol Cell 2008 Sep;19(9):3676-90","abstract":"Cytokinesis in all organisms involves the creation of membranous barriers that demarcate individual daughter cells. In fission yeast, a signaling module termed the septation initiation network (SIN) plays an essential role in the assembly of new membranes and cell wall during cytokinesis. In this study, we have characterized Slk1p, a protein-kinase related to the SIN component Sid2p. Slk1p is expressed specifically during meiosis and localizes to the spindle pole bodies (SPBs) during meiosis I and II in a SIN-dependent manner. Slk1p also localizes to the forespore membrane during sporulation. Cells lacking Slk1p display defects associated with sporulation, leading frequently to the formation of asci with smaller and/or fewer spores. The ability of slk1 Delta cells to sporulate, albeit inefficiently, is fully abolished upon compromise of function of Sid2p, suggesting that Slk1p and Sid2p play overlapping roles in sporulation. Interestingly, increased expression of the syntaxin Psy1p rescues the sporulation defect of sid2-250 slk1 Delta. Thus, it is likely that Slk1p and Sid2p play a role in forespore membrane assembly by facilitating recruitment of components of the secretory apparatus, such as Psy1p, to allow membrane expansion. These studies thereby provide a novel link between the SIN and vesicle trafficking during cytokinesis.","authors":"Yan H, Ge W, Chew TG, Chow JY, McCollum D, Neiman AM, Balasubramanian MK","authors_abbrev":"Yan H et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-06-20","publication_year":"2008","canto_session_key":"9248f079e7e06dd5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-16 15:54:08","canto_approved_date":"2024-09-25 14:07:22","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-16 15:53:57","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":40,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.11c","SPBC21.06c","SPAC9G1.09","SPAC24B11.11c","SPAC1565.06c","SPBC19G7.05c","SPAC1F3.06c","SPBC244.01c","SPBC1347.03","SPAC607.10","SPCC825.03c","SPCC417.06c","SPBC428.13c"],"gene_count":13,"ltp_gene_count":8,"approved_date":"2024-08-16"},{"uniquename":"PMID:24189946","title":"Gene activation by copy transposition in mating-type switching of a homothallic fission yeast.","citation":"Curr Genet 1981 Apr;3(1):5-12","abstract":"Mating-type switching in homothallic clones of the fission yeast, Schizosaccharomyces pombe, appears to follow the same route as previously found for \"mutations\" from homothallism to heterothallic ⊕ strains. A copy of mat2-P is transposed to and inserted at mat1, where it functionally replaces the mat1-M allele, and only the mat1 segment is expressed (!) to determine the actual mating type: mat1-M(!) mat2-P = ⊖ ⇌ ⊕ = mat1-P(!) mat2-P. This phenomenon has hitherto been concealed by the high switch-back rate from ⊕ to ⊖ observed in homothallic wild-type strains. It only becomes apparent in the presence of mutant \"switching genes\", which retard the rates of mating-type interconversion and temporarily freeze one or the other state of gene activation at the mat1 segment. Mutations to lowered rates of switching are found to map both inside and outside the mating-type locus. While the internal mutations of this kind exert their effect autonomously in the cis-configuration, the unlinked mutations are recessive to their wild-type alleles.","doi":"10.1007/BF00419574","authors":"Egel R, Gutz H","authors_abbrev":"Egel R et al.","pubmed_publication_date":"Apr 1981","pubmed_entrez_date":"2013-11-06","publication_year":"1981","canto_session_key":"13fac52a9d9415c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-05 23:00:23","canto_approved_date":"2022-12-13 10:40:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-05 22:59:53","canto_added_date":"2014-02-16 06:09:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.04","SPBC216.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-12-05"},{"uniquename":"EMBL:AU012903","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB178219","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPWOS2","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16348690","title":"Influence of Polyethylene Glycol on the Size of Schizosaccharomyces pombe Electropores.","citation":"Appl Environ Microbiol 1992 Apr;58(4):1201-6","abstract":"The role of polyethylene glycol (PEG) in the transformation of Schizosaccharomyces pombe by electroporation is investigated by fluorescein isothiocyanate-dextran uptake and transformation studies. It is shown that when S. pombe cells are electroporated in the presence of PEG, the permeability state created is sustained until removal of PEG. In addition, the permeability of electroporated S. pombe envelopes is further increased with longer incubation times in PEG. The increased permeability is apparently a result of enlarged pores (electropores) due to the presence of PEG. Comparison of a heat pulse transformation protocol with electroporation suggests a second role for PEG in the uptake of macromolecules. Since pores are not thought to be created during a heat pulse, the PEG may be facilitating the uptake of plasmid DNA. This facilitation of uptake would also be expected to affect DNA uptake by electroporated cells.","authors":"Hood MT, Stachow C","authors_abbrev":"Hood MT et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18265319","title":"S. pombe strain maintenance and media.","citation":"Curr Protoc Mol Biol 2003 Nov;Chapter 13:Unit 13.15","abstract":"Fission yeast can be grown and maintained using similar culture methods to those employed for budding yeast. The optimal media for S. pombe is somewhat different than that employed for S. cerevisiae, although budding yeast media can be used if necessary. Good sterile technique is essential to prevent contamination by airborne molds or bacteria.","doi":"10.1002/0471142727.mb1315s64","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2008-02-12","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26957021","title":"The RecQ DNA helicase Rqh1 constrains Exonuclease 1-dependent recombination at stalled replication forks.","citation":"Sci Rep 2016 Mar 09;6:22837","abstract":"DNA double-strand break (DSB) repair by homologous recombination (HR) involves resection of the break to expose a 3' single-stranded DNA tail. In budding yeast, resection occurs in two steps: initial short-range resection, performed by Mre11-Rad50-Xrs2 and Sae2; and long-range resection catalysed by either Exo1 or Sgs1-Dna2. Here we use genetic assays to investigate the importance of Exo1 and the Sgs1 homologue Rqh1 for DNA repair and promotion of direct repeat recombination in the fission yeast Schizosaccharomyces pombe. We find that Exo1 and Rqh1 function in alternative redundant pathways for promoting survival following replication fork breakage. Exo1 promotes replication fork barrier-induced direct repeat recombination but intriguingly limits recombination induced by fork breakage. Direct repeat recombination induced by ultraviolet light depends on either Exo1 or Rqh1. Finally, we show that Rqh1 plays a major role in limiting Exo1-dependent direct repeat recombination induced by replication fork stalling but only a minor role in constraining recombination induced by fork breakage. The implications of our findings are discussed in the context of the benefits that long-range resection may bring to processing perturbed replication forks.","doi":"10.1038/srep22837","authors":"Osman F, Ahn JS, Lorenz A, Whitby MC","authors_abbrev":"Osman F et al.","pubmed_publication_date":"09 Mar 2016","pubmed_entrez_date":"2016-03-10","publication_year":"2016","canto_session_key":"5911cf087ecba84c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-03-11 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC2G11.12","SPBC29A10.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:31586057","title":"Monitoring cytosolic H 2 O 2  fluctuations arising from altered plasma membrane gradients or from mitochondrial activity.","citation":"Nat Commun 2019 Oct 04;10(1):4526","abstract":"Genetically encoded probes monitoring H 2 O 2  fluctuations in living organisms are key to decipher redox signaling events. Here we use a new probe, roGFP2-Tpx1.C169S, to monitor pre-toxic fluctuations of peroxides in fission yeast, where the concentrations linked to signaling or to toxicity have been established. This probe is able to detect nanomolar fluctuations of intracellular H 2 O 2  caused by extracellular peroxides; expression of human aquaporin 8 channels H 2 O 2  entry into fission yeast decreasing membrane gradients. The probe also detects H 2 O 2  bursts from mitochondria after addition of electron transport chain inhibitors, the extent of probe oxidation being proportional to the mitochondrial activity. The oxidation of this probe is an indicator of steady-state levels of H 2 O 2  in different genetic backgrounds. Metabolic reprogramming during growth in low-glucose media causes probe reduction due to the activation of antioxidant cascades. We demonstrate how peroxiredoxin-based probes can be used to monitor physiological H 2 O 2  fluctuations.","doi":"10.1038/s41467-019-12475-0","authors":"Carmona M, de Cubas L, Bautista E, Moral-Blanch M, Medraño-Fernández I, Sitia R, Boronat S, Ayté J, Hidalgo E","authors_abbrev":"Carmona M et al.","pubmed_publication_date":"04 Oct 2019","pubmed_entrez_date":"2019-10-06","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-10-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19436749","title":"Phosphorylation-independent regulation of Atf1-promoted meiotic recombination by stress-activated, p38 kinase Spc1 of fission yeast.","citation":"PLoS One 2009;4(5):e5533","abstract":"Stress-activated protein kinases regulate multiple cellular responses to a wide variety of intracellular and extracellular conditions. The conserved, multifunctional, ATF/CREB protein Atf1 (Mts1, Gad7) of fission yeast binds to CRE-like (M26) DNA sites. Atf1 is phosphorylated by the conserved, p38-family kinase Spc1 (Sty1, Phh1) and is required for many Spc1-dependent stress responses, efficient sexual differentiation, and activation of Rec12 (Spo11)-dependent meiotic recombination hotspots like ade6-M26.\nWe sought to define mechanisms by which Spc1 regulates Atf1 function at the ade6-M26 hotspot. The Spc1 kinase was essential for hotspot activity, but dispensable for basal recombination. Unexpectedly, a protein lacking all eleven MAPK phospho-acceptor sites and detectable phosphorylation (Atf1-11M) was fully proficient for hotspot recombination. Furthermore, tethering of Atf1 to ade6 in the chromosome by a heterologous DNA binding domain bypassed the requirement for Spc1 in promoting recombination.\nThe Spc1 protein kinase regulates the pathway of Atf1-promoted recombination at or before the point where Atf1 binds to chromosomes, and this pathway regulation is independent of the phosphorylation status of Atf1. Since basal recombination is Spc1-independent, the principal function of the Spc1 kinase in meiotic recombination is to correctly position Atf1-promoted recombination at hotspots along chromosomes. We also propose new hypotheses on regulatory mechanisms for shared (e.g., DNA binding) and distinct (e.g., osmoregulatory vs. recombinogenic) activities of multifunctional, stress-activated protein Atf1.","doi":"10.1371/journal.pone.0005533","authors":"Gao J, Davidson MK, Wahls WP","authors_abbrev":"Gao J et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-05-14","publication_year":"2009","canto_session_key":"0b6d5503e51a6f05","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-27 13:51:20","canto_approved_date":"2024-03-28 12:39:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-11-26 08:38:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC29B5.01","SPCC1322.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-09-27"},{"uniquename":"PMID:9622480","title":"Functional analysis of amino acid residues essential for activity in the Na+/H+ exchanger of fission yeast.","citation":"Biochemistry 1998 Jun 09;37(23):8282-8","abstract":"We identified amino acid residues important for activity of sod2, the Na+/H+ antiporter of Schizosaccharomyces pombe. We mutated all eight His residues of sod2 into Arg. Only His367-->Arg affected function and resulted in complete inability of sod2 to allow growth of S. pombe in LiCl-containing medium. Mutant S. pombe (H367R) could not expel sodium in acidic (pH 4.0) medium and were defective in their ability to alkalinize external medium. When His367 was replaced by Asp, sodium export of S. pombe was suppressed at acidic pH while the sodium-dependent proton influx at pH 6.1 was increased compared to wild type. We also mutated three residues conserved in putative membrane regions of various eukaryotic and prokaryotic Na+/H+ exchangers. S. pombe containing Asp241-->Asn and Asp266, 267-->Asn mutations had greatly impaired growth in LiCl-containing medium. In addition, sodium-dependent proton influx at external pH 6. 1 was impaired. Sodium export from S. pombe cells at external pH 4.0 was also almost completely abolished by the D266,267N mutation; however, the D241N mutant protein retained almost normal Na+ export. The results demonstrate that His367, Asp241, and Asp266,267 are important in the function of the eukaryotic Na+/H+ exchanger sod2.","authors":"Dibrov P, Young PG, Fliegel L","authors_abbrev":"Dibrov P et al.","pubmed_publication_date":"09 Jun 1998","pubmed_entrez_date":"1998-06-19","publication_year":"1998","canto_session_key":"93dfcb17ff61262c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 13:29:24","canto_approved_date":"2023-05-15 13:12:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-08 20:34:12","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-31"},{"uniquename":"PMID:19155267","title":"Serine racemase with catalytically active lysinoalanyl residue.","citation":"J Biochem 2009 Apr;145(4):421-4","abstract":"Serine racemase synthesizes d-serine, a physiological agonist of the NMDA receptor in mammalian brains. Schizosaccharomyces pombe produces serine racemase (spSR) that is highly similar to the brain enzyme. Our mass-spectrometric and X-ray studies revealed that spSR is modified with its natural substrate serine. spSR remains partially active even though its essential Lys57 inherently forming a Schiff base with the coenzyme pyridoxal 5'-phosphate is converted to N(6)-(R-2-amino-2-carboxyethyl)-l-lysyl (lysino-d-alanyl) residue. This indicates that the alpha-amino group of the d-alanyl moiety of the lysino-d-alanyl residue serves as a catalytic base in the same manner as the epsilon-amino group of Lys57 of the original spSR.","doi":"10.1093/jb/mvp010","authors":"Yamauchi T, Goto M, Wu HY, Uo T, Yoshimura T, Mihara H, Kurihara T, Miyahara I, Hirotsu K, Esaki N","authors_abbrev":"Yamauchi T et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-01-22","publication_year":"2009","canto_session_key":"05fb9cabc575e97e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-10-31 22:00:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-31 12:26:19","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-31","pdb_entries":[{"pdb_id":"2zpu","gene_chains":[{"gene_uniquename":"SPCC320.14","chain":"A","position":"1-323"}],"title":"Crystal Structure of Modified Serine Racemase from S.pombe.","entry_authors":"Goto M","entry_authors_abbrev":"Goto M","reference_uniquename":"PMID:19155267","experimental_method":"X-ray","resolution":"1.7"}]},{"uniquename":"PMID:8746779","title":"The ade6 gene of the fission yeast as a target for antisense and ribozyme RNA-mediated suppression.","citation":"Antisense Res Dev 1995;5(4):295-305","abstract":"A genetic system for the analysis of antisense and ribozyme mechanisms is a much needed experimental tool, and yeast represent a favorable organism on which to base such a system. We have shown previously that the fission yeast Schizosaccharomyces pombe has potential to satisfy the requirements of such a system. This report describes experiments designed to determine if antisense and ribozyme RNA-mediated gene suppression will be generally applicable to other genes in S. pombe. Antisense and ribozyme RNAs designed to suppress the ade6 gene were expressed at high levels from episomal expression vectors. The ade6 gene was chosen as a target as mutations within the gene confer adenine auxotrophy and a red colony phenotype, and it was expected that antisense or ribozyme RNA-mediated mutant phenocopies would exhibit the same readily detectable phenotype. No phenotypic indication of ade6 suppression was detected in transformed yeast, and ade6 target mRNA was analyzed by primer extension and Northern analysis. Initially, conflicting results were obtained from these techniques, which were determined to be due to duplex formation between antisense and target RNA in vitro. No detectable reduction in the ade6 mRNA levels was found, and it was concluded that the gene was not suppressed by the antisense or ribozyme RNAs tested. These results confirm that in S. pombe as with other organisms, the susceptibility of genes to RNA-mediated suppression may be gene specific and that design of antisense and ribozyme genes will be an empirical process.","authors":"Atkins D, Patrikakis M, Izant JG","authors_abbrev":"Atkins D et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10418128","title":"Effects of pressure stress on the fission yeast Schizosaccharomyces pombe cold-sensitive mutant nda3.","citation":"FEMS Microbiol Lett 1999 Jul 01;176(1):31-8","abstract":"To investigate the influence of pressure stress on the cell cycle of Schizosaccharomyces pombe, we used a cold-sensitive nda3-KM311 mutant which arrests cell division at a step similar to the mitotic prophase, proposed by Hiraoka and colleagues (Cell 39 (1984) 349-358), under the restrictive temperature, 20 degrees C. The nda3-KM311 cells were first aerobically grown at 30 degrees C, transferred to 20 degrees C for 4 h and shifted to a permissive temperature of 36 degrees C for 15 min. The cells were treated with 100-200 MPa pressure and studied by electron and fluorescence microscopy. At 100 MPa, the nuclear membrane was damaged and the matrix of mitochondria had an electron-dense area. At 150 MPa, the nuclear membrane was broken over broad areas; numerous small vacuoles had fused into large pieces. Actin patches were concentrated in the central region and actin rings were seen in the 20 degrees C-grown cells. Even at 100 MPa, specific actin distribution was lost. Although at 100 MPa, long and fine actin cables were seen all over the cells, large actin patches and the actin rings remained in the center of the cell. They changed into thick and short cables at 150 MPa and above 200 MPa they decomposed but the actin ring was visible even with faint fluorescence. Immunoelectron microscopic observation confirmed this phenomenon.","authors":"Sato M, Hasegawa K, Shimada S, Osumi M","authors_abbrev":"Sato M et al.","pubmed_publication_date":"01 Jul 1999","pubmed_entrez_date":"1999-07-27","publication_year":"1999","canto_session_key":"13e843b27802fc33","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-28 14:02:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-02-28 14:02:19","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-02-28"},{"uniquename":"PMID:19033384","title":"The G1-S checkpoint in fission yeast is not a general DNA damage checkpoint.","citation":"J Cell Sci 2008 Dec 15;121(Pt 24):4047-54","abstract":"Inhibitory mechanisms called checkpoints regulate progression of the cell cycle in the presence of DNA damage or when a previous cell-cycle event is not finished. In fission yeast exposed to ultraviolet light the G1-S transition is regulated by a novel checkpoint that depends on the Gcn2 kinase. The molecular mechanisms involved in checkpoint induction and maintenance are not known. Here we characterise the checkpoint further by exposing the cells to a variety of DNA-damaging agents. Exposure to methyl methane sulphonate and hydrogen peroxide induce phosphorylation of eIF2alpha, a known Gcn2 target, and an arrest in G1 phase. By contrast, exposure to psoralen plus long-wavelength ultraviolet light, inducing DNA adducts and crosslinks, or to ionizing radiation induce neither eIF2alpha phosphorylation nor a cell-cycle delay. We conclude that the G1-S checkpoint is not a general DNA-damage checkpoint, in contrast to the one operating at the G2-M transition. The tight correlation between eIF2alpha phosphorylation and the presence of a G1-phase delay suggests that eIF2alpha phosphorylation is required for checkpoint induction. The implications for checkpoint signalling are discussed.","doi":"10.1242/jcs.035428","authors":"Krohn M, Skjølberg HC, Soltani H, Grallert B, Boye E","authors_abbrev":"Krohn M et al.","pubmed_publication_date":"15 Dec 2008","pubmed_entrez_date":"2008-11-27","publication_year":"2008","canto_session_key":"59469ef8c399b1f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"David Bradley","canto_first_approved_date":"2015-02-01 10:26:17","canto_approved_date":"2025-09-04 11:20:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-01 10:26:04","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"David Bradley","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.09","SPBC211.04c","SPAC3G9.09c","SPBC36B7.09"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2015-02-01"},{"uniquename":"PMID:12354095","title":"Calcineurin is implicated in the regulation of the septation initiation network in fission yeast.","citation":"Genes Cells 2002 Oct;7(10):1009-19","abstract":"In fission yeast, calcineurin has been implicated in cytokinesis because calcineurin-deleted cells form multiple septa and cell separation is impeded. However, this mechanism remains unclear.\nWe screened for mutations that confer synthetic lethality with calcineurin deletion and isolated a mutant, its 10-1/cdc7-i10, a novel allele of the cdc7+ gene involved in the septation initiation network (SIN). The mutation created a termination codon, resulting in the truncation of Cdc7 by 162 amino acids, which is not localized in the spindle pole body. Following treatment with the immune suppressive drug FK506, cdc7-i10 and the original cdc7-24 mutant cells showed highly elongated multinuclear morphology with few visible septa, closely resembling the phenotype at the restrictive temperature. Other SIN mutants, cdc11, spg1, sid2 and mob1 showed similar phenotypes following FK506 treatment. Consistent with this, expression of the constitutively active calcineurin suppressed the growth defects and septum initiation deficiency of these SIN mutants at the restrictive temperature. Moreover, electron microscopy revealed that calcineurin-deleted cells had very thick multiple septa which were partially and ectopically formed.\nThese results suggest that calcineurin is involved in the regulation of the SIN pathway, and is required for the proper formation and maturation of the septum in fission yeast.","authors":"Lu Y, Sugiura R, Yada T, Cheng H, Sio SO, Shuntoh H, Kuno T","authors_abbrev":"Lu Y et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-10-02","publication_year":"2002","canto_session_key":"3028eeb2a1aae09f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-17 11:35:39","canto_approved_date":"2026-01-31 12:46:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-15 10:59:59","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":53,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.13c","SPAC24B11.11c","SPCC1739.11c","SPBC21.06c","SPAC1565.06c","SPAC9G1.09","SPBC24C6.07","SPBP4H10.04"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2024-05-17"},{"uniquename":"PMID:17230583","title":"Mass spectrometric identification of covalently bound cell wall proteins from the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2007 Apr;24(4):267-78","abstract":"The cell wall of Schizosaccharomyces pombe is bilayered, consisting of an inner layer of mainly polysaccharides and an outer layer of galactomannoproteins. We present a detailed analysis of the cell wall proteome. Six covalently-bound cell wall proteins (CWPs) were identified using tandem mass spectrometry, including four predicted GPI-dependent CWPs (Gas1p, Gas5p, Ecm33p and Pwp1p) and two alkali-sensitive CWPs (Psu1p and Asl1p). Gas1p and Gas5p belong to glycoside hydrolase family 72, and are believed to be involved in 1,3-beta-glucan elongation. Ecm33p belongs to a ubiquitous fungal protein family with an unknown but crucial function in cell wall integrity. Pwp1p is an abundant protein with an unknown but probably non-enzymatic function. All four CWPs were present in HF-pyridine extracts, indicating that they are linked via a phosphodiester bridge to the glucan network. Psu1p is a homologue of the Saccharomyces cerevisiae Sun family, whereas Asl1p has no homologues in S. cerevisiae but is related to Aspergillus fumigatus and Ustilago maydis proteins. Finally, although the protein content of Sz. pombe cell walls is only slightly less than in S. cerevisiae and Candida albicans, the amount of carbohydrate added to the proteins was found to be two- to three-fold decreased, consistent with earlier reported differences in outer chain N-glycosylation.","authors":"de Groot PW, Yin QY, Weig M, Sosinska GJ, Klis FM, de Koster CG","authors_abbrev":"de Groot PW et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-01-19","publication_year":"2007","canto_session_key":"92f93fe306552df6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-07-10 22:19:56","canto_session_submitted_date":"2012-07-10 15:59:47","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC1705.03c","SPAC19B12.02c","SPAC11E3.13c","SPAC1002.13c","SPAC13G6.10c","SPCC1322.10"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2012-07-10"},{"uniquename":"PMID:6026396","title":"Forward mutation studies with N-nitroso-N-methyl-urethane and N-nitroso-N-ethylurethane in Schizosaccharomyces pombe.","citation":"Mutat Res 1967 Feb;4(1):31-6","abstract":"","authors":"Abbondandolo A, Loprieno N","authors_abbrev":"Abbondandolo A et al.","pubmed_publication_date":"Feb 1967","pubmed_entrez_date":"1967-02-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5058913","title":"Amino acid pool components as regulators of protein synthesis in the fission yeast, Schizosaccharomyces pombe.","citation":"Exp Cell Res 1972 Feb;70(2):381-9","abstract":"","authors":"Stebbing N","authors_abbrev":"Stebbing N","pubmed_publication_date":"Feb 1972","pubmed_entrez_date":"1972-02-01","publication_year":"1972","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8736868","title":"Characterisation of Sxa2, a carboxypeptidase involved in pheromone recovery in fission yeast.","citation":"Biochem Soc Trans 1996 May;24(2):210S","abstract":"","authors":"Ladds G, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"May 1996","pubmed_entrez_date":"1996-05-01","publication_year":"1996","canto_session_key":"224599b759ca656","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-01-06 16:24:12","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-02-03 09:31:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.06","SPAC1296.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-02-03"},{"uniquename":"PMID:2806887","title":"Meiotic recombination-deficient mutants of Schizosaccharomyces pombe.","citation":"Genetics 1989 Sep;123(1):45-54","abstract":"A mutant screen employing the ade6-M26 recombination hotspot was developed and used to isolate Schizosaccharomyces pombe mutants deficient in meiotic recombination. Nine rec mutations were recessive, defining six complementation groups, and reduced ade6 meiotic recombination 3-fold to greater than or equal to 300-fold when homozygous. Three recessive rec mutations analyzed further also reduced meiotic intragenic recombination at ura4 on chromosome III and intergenic recombination between pro2 and arg3 on chromosome I. The observed non-co-ordinate reductions of the recombinant frequencies in the three test intervals suggest a degree of locus (or intragenic vs. intergenic) specificity of the corresponding rec+ gene products. None of the mutations specifically inactivated the ade6-M26 hotspot. Additional rec genes may be identified with these methods.","authors":"Ponticelli AS, Smith GR","authors_abbrev":"Ponticelli AS et al.","pubmed_publication_date":"Sep 1989","pubmed_entrez_date":"1989-09-01","publication_year":"1989","canto_session_key":"43652d4348e2d1f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-31 08:59:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-31 08:58:26","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13","SPBC29A10.14","SPBC21B10.12","SPAC25G10.04c","SPCC330.05c","SPAC2G11.12","SPCC4E9.01c","SPCC1753.03c"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2014-07-31"},{"uniquename":"PMID:16168376","title":"SUMO modification is involved in the maintenance of heterochromatin stability in fission yeast.","citation":"Mol Cell 2005 Sep 16;19(6):817-28","abstract":"Several studies have suggested that SUMO may participate in the regulation of heterochromatin, but direct evidence is lacking. Here, we present a direct link between sumoylation and heterochromatin stability. SUMO deletion impaired silencing at heterochromatic regions and induced histone H3 Lys4 methylation, a hallmark of active chromatin in fission yeast. Our findings showed that the SUMO-conjugating enzyme Hus5/Ubc9 interacted with the conserved heterochromatin proteins Swi6, Chp2 (a paralog of Swi6), and Clr4 (H3 Lys9 methyltransferase). Moreover, chromatin immunoprecipitation (ChIP) revealed that Hus5 was highly enriched in heterochromatic regions in a heterochromatin-dependent manner, suggesting a direct role of Hus5 in heterochromatin formation. We also found that Swi6, Chp2, and Clr4 themselves can be sumoylated in vivo and defective sumoylation of Swi6 or Chp2 compromised silencing. These results indicate that Hus5 associates with heterochromatin through interactions with heterochromatin proteins and modifies substrates whose sumoylations are required for heterochromatin stability, including heterochromatin proteins themselves.","authors":"Shin JA, Choi ES, Kim HS, Ho JC, Watts FZ, Park SD, Jang YK","authors_abbrev":"Shin JA et al.","pubmed_publication_date":"16 Sep 2005","pubmed_entrez_date":"2005-09-20","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c","SPAC30D11.13","SPBC428.08c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:31066439","title":"The extruded non-template strand determines the architecture of R-loops.","citation":"Nucleic Acids Res 2019 Jul 26;47(13):6783-6795","abstract":"Three-stranded R-loop structures have been associated with genomic instability phenotypes. What underlies their wide-ranging effects on genome stability remains poorly understood. Here we combined biochemical and atomic force microscopy approaches with single molecule R-loop footprinting to demonstrate that R-loops formed at the model Airn locus in vitro adopt a defined set of three-dimensional conformations characterized by distinct shapes and volumes, which we call R-loop objects. Interestingly, we show that these R-loop objects impose specific physical constraints on the DNA, as revealed by the presence of stereotypical angles in the surrounding DNA. Biochemical probing and mutagenesis experiments revealed that the formation of R-loop objects at Airn is dictated by the extruded non-template strand, suggesting that R-loops possess intrinsic sequence-driven properties. Consistent with this, we show that R-loops formed at the fission yeast gene sum3 do not form detectable R-loop objects. Our results reveal that R-loops differ by their architectures and that the organization of the non-template strand is a fundamental characteristic of R-loops, which could explain that only a subset of R-loops is associated with replication-dependent DNA breaks.","doi":"10.1093/nar/gkz341","authors":"Carrasco-Salas Y, Malapert A, Sulthana S, Molcrette B, Chazot-Franguiadakis L, Bernard P, Chédin F, Faivre-Moskalenko C, Vanoosthuyse V","authors_abbrev":"Carrasco-Salas Y et al.","pubmed_publication_date":"26 Jul 2019","pubmed_entrez_date":"2019-05-09","publication_year":"2019","canto_session_key":"8346729845f62763","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-05-16 08:37:21","canto_approved_date":"2019-05-16 08:37:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-15 11:48:07","canto_added_date":"2019-05-10 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-05-16"},{"uniquename":"PMID:8796419","title":"Media for preservative resistant yeasts: a collaborative study.","citation":"Int J Food Microbiol 1996 Apr;29(2-3):167-75","abstract":"An international collaborative study was carried out to determine the most effective medium for selective isolation and enumeration of preservative resistant yeasts. Such a medium should prevent the growth of other yeasts such as Saccharomyces cerevisiae that are tolerant to lower levels of commonly used food preservatives, and sensitive yeasts such as Rhodotorula species. The study compared two non-selective media that are in common use for cultivation of yeasts from foods, Malt Extract agar (MEA) and Tryptone Glucose Yeast extract agar (TGY) with media made selective for preservative resistant yeasts by addition of 0.5% acetic acid to these two basal media (MEAA and TGYA). A fifth medium, Zygosaccharomyces bailii medium (ZBM) was also included in the study. These media were compared for their efficacy in selective isolation and enumeration of the preservative resistant yeasts Zygosaccharomyces bailii, Schizosaccharomyces pombe and Pichia membranaefaciens. MEA and TGY without acetic acid were used as control, non-selective media, and Rhodotorula glutinis was the preservative sensitive control culture. Seven laboratories in six countries took part in the study. Of the non-selective media, TGY generally gave the highest counts, and TGY amended with 0.5% acetic acid (TGYA) was the best medium for recovery of all three preservative-resistant yeasts. ZBM was found to be selective for Z. bailii, but counts of this yeast on ZBM were significantly lower than on TGYA. R. glutinis did not grow on any of the selective media.","authors":"Hocking AD","authors_abbrev":"Hocking AD","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11350031","title":"Mutation in the prp12+ gene encoding a homolog of SAP130/SF3b130 causes differential inhibition of pre-mRNA splicing and arrest of cell-cycle progression in Schizosaccharomyces pombe.","citation":"RNA 2001 May;7(5):671-81","abstract":"prp12-1 is one of the mutants defective in pre-mRNA splicing at a nonpermissive temperature in Schizosaccharomyces pombe. We found that the prp12+ gene encodes a protein highly homologous with a human splicing factor, SAP130/SF3b130, a subunit of a U2 snRNP-associated complex SF3b. Prp12p was shown to interact genetically with Prp10p that is a homolog of SAP155/SF3b155, another subunit in SF3b, suggesting that Prp12p is a functional homolog of human SAP130/SF3b130. Prp12p tagged with GFP is uniformly localized in the nuclear DNA region. In addition to pre-mRNA splicing defects, the prp12-1 mutant produced elongated cells, a typical phenotype of cell division cycle (cdc) mutants, suggesting a possible link between pre-mRNA splicing and cell-cycle progression. We examined kinetics of splicing defects in prp12-1 and several other prp mutants using northern blot hybridization and found that, among all the tested pre-mRNAs, only Tflld pre-mRNA with low splicing efficiency showed detectable splicing defects at the nonpermissive temperature in prp12-1. In addition, we found that other prp mutants with the cdc phenotype also showed differential splicing defects in tested pre-mRNAs at the nonpermissive temperature. On the other hand, prp mutants that do not exhibit the cdc phenotype showed a rapid and complete block of pre-mRNA splicing in all the tested pre-mRNAs at the nonpermissive temperature, indicating that prp mutants with weak splicing defects have a tendency to exhibit the cdc phenotype. These results suggest that the cdc phenotype in prp12-1 is caused by a selective reduction of spliced transcripts encoding a protein (or proteins) required for G2/M transition.","authors":"Habara Y, Urushiyama S, Shibuya T, Ohshima Y, Tani T","authors_abbrev":"Habara Y et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-15","publication_year":"2001","canto_session_key":"24a3853610543a99","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-09 16:36:31","canto_approved_date":"2024-02-21 17:31:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-07 15:55:46","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":102,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPAC27F1.09c","SPAC2G11.14","SPBC11B10.09","SPBC146.07","SPAC144.03","SPAPJ698.03c","SPAC3H5.07","SPBC18H10.12c","SPBC6B1.07","SPBC19C2.01","SPCC10H11.01"],"gene_count":12,"ltp_gene_count":6,"approved_date":"2015-06-09"},{"uniquename":"PMID:28292918","title":"Nonhomologous End-Joining with Minimal Sequence Loss Is Promoted by the Mre11-Rad50-Nbs1-Ctp1 Complex in  Schizosaccharomyces pombe .","citation":"Genetics 2017 May;206(1):481-496","abstract":"While the Mre11-Rad50-Nbs1 (MRN) complex has known roles in repair processes like homologous recombination and microhomology-mediated end-joining, its role in nonhomologous end-joining (NHEJ) is unclear as  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe , and mammals have different requirements for repairing cut DNA ends. Most double-strand breaks (DSBs) require nucleolytic processing prior to DNA ligation. Therefore, we studied repair using the  Hermes  transposon, whose excision leaves a DSB capped by hairpin ends similar to structures generated by palindromes and trinucleotide repeats. We generated single  Hermes  insertions using a novel  S. pombe  transient transfection system, and used  Hermes  excision to show a requirement for MRN in the NHEJ of nonligatable ends. NHEJ repair was indicated by the >1000-fold decrease in excision in cells lacking Ku or DNA ligase 4. Most repaired excision sites had <5 bp of sequence loss or mutation, characteristic for NHEJ and similar excision events in metazoans, and in contrast to the more extensive loss seen in  S. cerevisiae  S. pombe  NHEJ was reduced >1000-fold in cells lacking each MRN subunit, and loss of MRN-associated Ctp1 caused a 30-fold reduction. An Mre11 dimer is thought to hold DNA ends together for repair, and Mre11 dimerization domain mutations reduced repair 300-fold. In contrast, a  mre11  mutant defective in endonucleolytic activity, the same mutant lacking Ctp1, or the triple mutant also lacking the putative hairpin nuclease Pso2 showed wild-type levels of repair. Thus, MRN may act to recruit the hairpin opening activity that allows subsequent repair.","doi":"10.1534/genetics.117.200972","authors":"Li Y, Wang J, Zhou G, Lajeunesse M, Le N, Stawicki BN, Corcino YL, Berkner KL, Runge KW","authors_abbrev":"Li Y et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2017-03-16","publication_year":"2017","canto_session_key":"e67ad73a2a061795","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kurt Runge","canto_first_approved_date":"2017-05-03 13:22:00","canto_approved_date":"2024-06-26 09:53:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-26 14:59:45","canto_added_date":"2017-03-17 01:15:14","annotation_curators":[{"name":"Kurt Runge","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.09c","SPAC22A12.01c","SPCC338.08","SPAC13C5.07","SPAC1556.01c","SPCC126.02c","SPCC1183.05c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-05-03"},{"uniquename":"EMBL:AU011040","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21386897","title":"Systematic two-hybrid and comparative proteomic analyses reveal novel yeast pre-mRNA splicing factors connected to Prp19.","citation":"PLoS One 2011 Feb 28;6(2):e16719","abstract":"Prp19 is the founding member of the NineTeen Complex, or NTC, which is a spliceosomal subcomplex essential for spliceosome activation. To define Prp19 connectivity and dynamic protein interactions within the spliceosome, we systematically queried the Saccharomyces cerevisiae proteome for Prp19 WD40 domain interaction partners by two-hybrid analysis. We report that in addition to S. cerevisiae Cwc2, the splicing factor Prp17 binds directly to the Prp19 WD40 domain in a 1:1 ratio. Prp17 binds simultaneously with Cwc2 indicating that it is part of the core NTC complex. We also find that the previously uncharacterized protein Urn1 (Dre4 in Schizosaccharomyces pombe) directly interacts with Prp19, and that Dre4 is conditionally required for pre-mRNA splicing in S. pombe. S. pombe Dre4 and S. cerevisiae Urn1 co-purify U2, U5, and U6 snRNAs and multiple splicing factors, and dre4Δ and urn1Δ strains display numerous negative genetic interactions with known splicing mutants. The S. pombe Prp19-containing Dre4 complex co-purifies three previously uncharacterized proteins that participate in pre-mRNA splicing, likely before spliceosome activation. Our multi-faceted approach has revealed new low abundance splicing factors connected to NTC function, provides evidence for distinct Prp19 containing complexes, and underscores the role of the Prp19 WD40 domain as a splicing scaffold.","doi":"10.1371/journal.pone.0016719","authors":"Ren L, McLean JR, Hazbun TR, Fields S, Vander Kooi C, Ohi MD, Gould KL","authors_abbrev":"Ren L et al.","pubmed_publication_date":"28 Feb 2011","pubmed_entrez_date":"2011-03-10","publication_year":"2011","canto_session_key":"6326f4d611465327","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-23 14:31:14","canto_approved_date":"2024-10-21 07:11:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-04-22 09:08:05","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":139,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.01","SPAC2C4.03c","SPBP23A10.12","SPBC18H10.10c","SPAC26F1.03","SPBC12C2.06","SPBC887.05c","SPAC9.13c","SPAC13G7.06","SPBC19C2.08","SPCC962.06c","SPBC36.09","SPBC13E7.02","SPAC22F3.11c","SPAC343.17c","SPCC162.01c","SPAC22A12.16","SPAC26H5.10c","SPAC24H6.10c","SPCC16A11.13","SPBC713.05","SPAC20H4.06c","SPAC1F12.07","SPAC1486.03c","SPBC21C3.05","SPBC24C6.11","SPAC4A8.09c","SPAC227.12","SPAC31G5.01","SPBC31F10.11c","SPBC1861.08c","SPBC428.12c","SPAC57A10.03","SPAC56F8.05c","SPBC1289.11","SPAC27D7.07c","SPAC26A3.08","SPCC1281.02c","SPAC22F8.10c","SPAC30D11.09","SPAC19A8.10","SPBC20F10.01","SPAC6G10.10c","SPCC364.02c","SPBC1289.03c","SPAC167.03c","SPBC4B4.09","SPBC13E7.01","SPBC146.07","SPCC5E4.10c","SPAC4F8.12c","SPAC6F12.13c","SPBC3E7.13c","SPAC20H4.09","SPBC19C2.01","SPAC24H6.04","SPBC11G11.06c","SPCP1E11.07c","SPCC550.02c","SPBC30D10.13c","SPBC16H5.10c","SPAC1420.02c","SPBC119.13c","SPAC2F3.14c","SPBC13G1.02","SPBC8D2.09c","SPBC146.05c","SPBP22H7.07","SPAC31G5.18c","SPBC211.02c","SPAC29E6.02","SPAC3A12.11c","SPBC215.12","SPBC1711.17","SPAC1006.07","SPBC28F2.04c","SPBC342.02","SPBC646.09c","SPAC1F3.09","SPAC1782.03","SPBC19C2.14","SPAC13A11.02c","SPCC188.11","SPCC663.11","SPAPJ698.03c","SPBC3E7.14","SPAC23H3.02c","SPCC1020.06c","SPAC6F12.10c","SPAC10F6.02c","SPBC428.02c","SPBC337.06c","SPAC22A12.09c","SPBC1703.07","SPBC211.05","SPAC17G6.14c","SPBC6B1.10","SPAC19G12.07c","SPBC32F12.05c","SPBC530.14c","SPBC6B1.07","SPCC794.07","SPAC29A4.15","SPAC644.12","SPBC29A3.07c","SPBC646.02","SPBC1703.10","SPAC27F1.09c","SPAC29A4.08c","SPBC4B4.05","SPCC1620.10","SPCC1442.09","SPAC13C5.02","SPCC736.15","SPAC9.03c","SPAC1D4.04"],"gene_count":116,"ltp_gene_count":62,"approved_date":"2018-03-23"},{"uniquename":"EMBL:AB084817","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23795289","title":"Evolutionary principles of modular gene regulation in yeasts.","citation":"Elife 2013 Jun 18;2:e00603","abstract":"Divergence in gene regulation can play a major role in evolution. Here, we used a phylogenetic framework to measure mRNA profiles in 15 yeast species from the phylum Ascomycota and reconstruct the evolution of their modular regulatory programs along a time course of growth on glucose over 300 million years [corrected]. We found that modules have diverged proportionally to phylogenetic distance, with prominent changes in gene regulation accompanying changes in lifestyle and ploidy, especially in carbon metabolism. Paralogs have significantly contributed to regulatory divergence, typically within a very short window from their duplication. Paralogs from a whole genome duplication (WGD) event have a uniquely substantial contribution that extends over a longer span. Similar patterns occur when considering the evolution of the heat shock regulatory program measured in eight of the species, suggesting that these are general evolutionary principles. DOI:http://dx.doi.org/10.7554/eLife.00603.001.","doi":"10.7554/eLife.00603","authors":"Thompson DA, Roy S, Chan M, Styczynsky MP, Pfiffner J, French C, Socha A, Thielke A, Napolitano S, Muller P, Kellis M, Konieczka JH, Wapinski I, Regev A","authors_abbrev":"Thompson DA et al.","pubmed_publication_date":"18 Jun 2013","pubmed_entrez_date":"2013-06-25","publication_year":"2013","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1349418","title":"A leptomycin B resistance gene of Schizosaccharomyces pombe encodes a protein similar to the mammalian P-glycoproteins.","citation":"Mol Microbiol 1992 Mar;6(6):761-9","abstract":"Screening for leptomycin B (LMB)-resistant transformants in a gene library constructed in Schizosaccharomyces pombe with the chromosomal DNA of an LMB-resistant mutant of S. pombe and with multicopy plasmid pDB248' as the vector led to the isolation of a gene, named pmd1+, encoding a 1362-amino-acid protein. This protein showed great similarity in amino acid sequence to the mammalian P-glycoprotein encoded by the multidrug resistance gene, mdr, and the Saccharomyces cerevisiae a-factor transporter encoded by STE6. In addition, computer analyses predicted that the protein encoded by pmd1+ formed an intramolecular duplicated structure and each of the halves contained six transmembrane regions as well as two ATP-binding domains, as observed with the P-glycoproteins and the STE6 product. Consistent with this was that S. pombe cells containing the pmd1+ gene on a multicopy plasmid showed resistance not only to LMB but also to several cytotoxic agents. The pmd1 null mutants derived by gene disruption were viable and hypersensitive to these agents. All these data suggest that the pmd1+ gene encodes a protein that is a structural and functional counterpart of mammalian mdr proteins.","authors":"Nishi K, Yoshida M, Nishimura M, Nishikawa M, Nishiyama M, Horinouchi S, Beppu T","authors_abbrev":"Nishi K et al.","pubmed_publication_date":"Mar 1992","pubmed_entrez_date":"1992-03-01","publication_year":"1992","canto_session_key":"1654d009749b8a7b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-06 14:11:30","canto_approved_date":"2020-01-23 18:36:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-18 19:08:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC663.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-12-06"},{"uniquename":"PMID:14500820","title":"Genome-scale design of PCR primers and long oligomers for DNA microarrays.","citation":"Nucleic Acids Res 2003 Oct 01;31(19):5576-81","abstract":"During the last years, the demand for custom-made cDNA chips/arrays as well as whole genome chips is increasing rapidly. The efficient selection of gene-specific primers/oligomers is of the utmost importance for the successful production of such chips. We developed GenomePRIDE, a highly flexible and scalable software for designing primers/oligomers for large-scale projects. The program is able to generate either long oligomers (40-70 bases), or PCR primers for the amplification of gene-specific DNA fragments of user-defined length. Additionally, primers can be designed in-frame in order to facilitate large-scale cloning into expression vectors. Furthermore, GenomePRIDE can be adapted to specific applications such as the generation of genomic amplicon arrays or the design of fragments specific for alternative splice isoforms. We tested the performance of GenomePRIDE on the entire genomes of Listeria monocytogenes (1584 gene-specific PCRs, 48 long oligomers) as well as of eukaryotes such as Schizosaccharomyces pombe (5006 gene-specific PCRs), and Drosophila melanogaster (21 306 gene-specific PCRs). With its computing speed of 1000 primer pairs per hour and a PCR amplification success of 99%, GenomePRIDE represents an extremely cost- and time-effective program.","authors":"Haas SA, Hild M, Wright AP, Hain T, Talibi D, Vingron M","authors_abbrev":"Haas SA et al.","pubmed_publication_date":"01 Oct 2003","pubmed_entrez_date":"2003-09-23","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16385131","title":"Functional dissection of Ctr4 and Ctr5 amino-terminal regions reveals motifs with redundant roles in copper transport.","citation":"Microbiology (Reading) 2006 Jan;152(Pt 1):209-222","abstract":"Copper uptake in the fission yeast Schizosaccharomyces pombe is carried out by a heteromeric complex formed by two proteins, Ctr4 and Ctr5. In this study, a stable expression system using integrative plasmids was developed to investigate the respective roles of Ctr4 and Ctr5 in copper transport. It was shown that expression of full-length Ctr4 or truncated Ctr4 containing residues 106-289 was required for localization of Ctr5 to the plasma membrane. Likewise, when the full-length Ctr5 or truncated Ctr5 from residues 44-173 was co-expressed with Ctr4, this protein was visualized at the periphery of the cell. To determine the importance of the Mets motifs (consisting of five methionines arranged as Met-X2-Met-X-Met, where X is any amino acid) of Ctr4 and Ctr5 in the heteroprotein complex, we co-expressed Ctr5 lacking the Mets motif and Cys-X-Met-X-Met sequence with wild-type Ctr4 or its mutant derivatives. Conversely, Ctr4 lacking the Mets motif and Met(122) was expressed with wild-type Ctr5 or its mutant derivatives. These experiments revealed that the five Mets motifs of Ctr4 and the Ctr4 residue Met(122) have equally important roles in copper assimilation. Furthermore, the two partially overlapping Mets motifs and the Cys-X-Met-X-Met sequence in Ctr5 have redundant functions in copper transport, with the latter sequence making a greater contribution than the former. Together, the data reveal that co-expression of both Ctr4 and Ctr5 is necessary for the proper function and localization of the heteroprotein complex to the plasma membrane. Once on the cell surface, the N-terminal regions of Ctr4 and Ctr5 can function independently to transport copper; however, the greatest efficiency is achieved when both N termini are present.","doi":"10.1099/mic.0.28392-0","authors":"Beaudoin J, Laliberté J, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2005-12-31","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1393.10","SPAC1142.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:28657616","title":"Efficient conversion of N 6 -threonylcarbamoyladenosine (t 6 A) into a tRNA native hydantoin cyclic form (ct 6 A) performed at nucleoside and oligoribonucleotide levels.","citation":"Chem Commun (Camb) 2017 Jul 11;53(56):7945-7948","abstract":"A t 6 A nucleoside was efficiently and stereospecifically transformed into a hydantoin cyclic form of N 6 -l-threonylcarbamoyladenosine (ct 6 A) by the use of polymer bounded carbodiimide (EDC-P) and HOBt. The procedure was successfully applied for a post-synthetic conversion of t 6 A-containing RNA 17-mers (of the sequences of anticodon stem and loop (ASL) fragments of S. pombe tRNA i  and E. coli tRNA Lys ) into the products bearing the ct 6 A unit.","doi":"10.1039/c7cc03560h","authors":"Matuszewski M, Debiec K, Sochacka E","authors_abbrev":"Matuszewski M et al.","pubmed_publication_date":"11 Jul 2017","pubmed_entrez_date":"2017-06-29","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-06-30 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD259","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25651781","title":"Geranylgeranyltransferase Cwg2-Rho4/Rho5 module is implicated in the Pmk1 MAP kinase-mediated cell wall integrity pathway in fission yeast.","citation":"Genes Cells 2015 Apr;20(4):310-23","abstract":"Pmk1, a fission yeast homologue of mammalian ERK MAPK, regulates cell wall integrity, cytokinesis, RNA granule formation and ion homeostasis. Our screen for vic (viable in the presence of immunosuppressant and chloride ion) mutants identified regulators of the Pmk1 MAPK signaling, including Cpp1 and Rho2, based on the genetic interaction between calcineurin and Pmk1 MAPK. Here, we identified the vic2-1 mutants carrying a mis-sense mutation in the cwg2(+) gene encoding a beta subunit of geranylgeranyltransferase I (GGTase I), which participates in the post-translational C-terminal modification of several small GTPases, allowing their targeting to the membrane. Analysis of the vic2-1/cwg2-v2 mutant strain showed that the localization of Rho1, Rho4, Rho5 and Cdc42, both at the plasma and vacuolar membranes, was impaired in the vic2-1/cwg2-v2 mutant cells. In addition, Rho4 and Rho5 deletion cells exhibited the vic phenotype and cell wall integrity defects, shared phenotypes among the components of the Pmk1 MAPK pathway. Consistently, the phosphorylation of Pmk1 MAPK on heat shock was decreased in the cwg2-v2 mutants, and rho4- and rho5-null cells. Moreover, Rho4 and Rho5 associate with Pck1/Pck2. Possible roles of Cwg2, Rho4 and Rho5 in the Pmk1 signaling will be discussed.","doi":"10.1111/gtc.12222","authors":"Doi A, Kita A, Kanda Y, Uno T, Asami K, Satoh R, Nakano K, Sugiura R","authors_abbrev":"Doi A et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-02-06","publication_year":"2015","canto_session_key":"4d523e082a73fe18","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-02-07 01:15:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2E1P5.04c","SPBC119.08","SPBC12D12.04c","SPAC17G8.14c","SPAC20H4.11c","SPAC16A10.04","SPAC1F7.04"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:22592553","title":"Characterization of triglyceride lipase genes of fission yeast Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2012 Nov;96(4):981-91","abstract":"Triglycerides (TG) are major storage lipids for eukaryotic cells. In this study, we characterized three genes of fission yeast Schizosaccharomyces pombe, SPCC1450.16c, SPAC1786.01c, and SPAC1A6.05c, that show high homology to Saccharomyces cerevisiae TG lipase genes, TGL3, TGL4, and TGL5. Deletion of each gene increased TG content by approximately 1.7-fold compared to the parental wild-type strain, and their triple deletion mutant further increased TG content to 2.7-fold of the wild-type strain, suggesting that all three genes encode TG lipase and are functioning in S. pombe. The triple deletion mutant showed no growth defect in rich and synthetic medium, but its growth was sensitive to cerulenin, an inhibitor of fatty acid synthesis. This growth defect by cerulenin was restored by adding oleic acid in media, suggesting that these genes were involved in the mobilization of TG in S. pombe. When ricinoleic acid was produced in the triple mutant by introducing CpFAH12 fatty acid hydroxylase gene from Claviceps purpurea, percent composition of ricinoleic acid increased by 1.1-fold compared to the wild-type strain, in addition to a 1.6-fold increase in total fatty acid content per dry cell weight (DCW). In total, the ricinoleic acid production per DCW increased by 1.8-fold in the triple deletion mutant.","doi":"10.1007/s00253-012-4151-8","authors":"Yazawa H, Kumagai H, Uemura H","authors_abbrev":"Yazawa H et al.","pubmed_publication_date":"Nov 2012","pubmed_entrez_date":"2012-05-18","publication_year":"2012","canto_session_key":"fa1b6031c1a25b19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-06-08 08:34:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-07 09:39:35","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":39,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1786.01c","SPAC1A6.05c","SPCC1450.16c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-06-07"},{"uniquename":"PMID:18667531","title":"Nse1 RING-like domain supports functions of the Smc5-Smc6 holocomplex in genome stability.","citation":"Mol Biol Cell 2008 Oct;19(10):4099-109","abstract":"The Smc5-Smc6 holocomplex plays essential but largely enigmatic roles in chromosome segregation, and facilitates DNA repair. The Smc5-Smc6 complex contains six conserved non-SMC subunits. One of these, Nse1, contains a RING-like motif that often confers ubiquitin E3 ligase activity. We have functionally characterized the Nse1 RING-like motif, to determine its contribution to the chromosome segregation and DNA repair roles of Smc5-Smc6. Strikingly, whereas a full deletion of nse1 is lethal, the Nse1 RING-like motif is not essential for cellular viability. However, Nse1 RING mutant cells are hypersensitive to a broad spectrum of genotoxic stresses, indicating that the Nse1 RING motif promotes DNA repair functions of Smc5-Smc6. We tested the ability of both human and yeast Nse1 to mediate ubiquitin E3 ligase activity in vitro and found no detectable activity associated with full-length Nse1 or the isolated RING domains. Interestingly, however, the Nse1 RING-like domain is required for normal Nse1-Nse3-Nse4 trimer formation in vitro and for damage-induced recruitment of Nse4 and Smc5 to subnuclear foci in vivo. Thus, we propose that the Nse1 RING-like motif is a protein-protein interaction domain required for Smc5-Smc6 holocomplex integrity and recruitment to, or retention at, DNA lesions.","authors":"Pebernard S, Perry JJ, Tainer JA, Boddy MN","authors_abbrev":"Pebernard S et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-08-01","publication_year":"2008","canto_session_key":"c289620cc356e427","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-11-07 13:12:37","canto_approved_date":"2026-01-29 17:57:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-07 13:12:30","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPCC550.05","SPBC20F10.04c","SPCC4G3.05c","SPCC645.04"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2022-11-07"},{"uniquename":"PMID:5516452","title":"Flocculation in Schizosaccharomyces pombe.","citation":"J Gen Microbiol 1970 Dec;64(2):247-50","abstract":"","authors":"Calleja GB","authors_abbrev":"Calleja GB","pubmed_publication_date":"Dec 1970","pubmed_entrez_date":"1970-12-01","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PB_REF:0000009","title":"Distant orthologs supported by JackHMMR","abstract":"Ortholog predicted using jackHMMER iterative search (PMID:25943547), and manually reviewed for context (length, functional attributes and other features). See DOI: 10.1007/4735_97 for a description of our manual review process.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.13c","HGNC:11741","HGNC:13646","HGNC:29612","SPAC4G9.11c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:24210919","title":"Mtr4-like protein coordinates nuclear RNA processing for heterochromatin assembly and for telomere maintenance.","citation":"Cell 2013 Nov 21;155(5):1061-74","abstract":"The regulation of protein-coding and noncoding RNAs is linked to nuclear processes, including chromatin modifications and gene silencing. However, the mechanisms that distinguish RNAs and mediate their functions are poorly understood. We describe a nuclear RNA-processing network in fission yeast with a core module comprising the Mtr4-like protein, Mtl1, and the zinc-finger protein, Red1. The Mtl1-Red1 core promotes degradation of mRNAs and noncoding RNAs and associates with different proteins to assemble heterochromatin via distinct mechanisms. Mtl1 also forms Red1-independent interactions with evolutionarily conserved proteins named Nrl1 and Ctr1, which associate with splicing factors. Whereas Nrl1 targets transcripts with cryptic introns to form heterochromatin at developmental genes and retrotransposons, Ctr1 functions in processing intron-containing telomerase RNA. Together with our discovery of widespread cryptic introns, including in noncoding RNAs, these findings reveal unique cellular strategies for recognizing regulatory RNAs and coordinating their functions in response to developmental and environmental cues.","doi":"10.1016/j.cell.2013.10.027","authors":"Lee NN, Chalamcharla VR, Reyes-Turcu F, Mehta S, Zofall M, Balachandran V, Dhakshnamoorthy J, Taneja N, Yamanaka S, Zhou M, Grewal SI","authors_abbrev":"Lee NN et al.","pubmed_publication_date":"21 Nov 2013","pubmed_entrez_date":"2013-11-12","publication_year":"2013","canto_session_key":"1f991e4ad5694cb6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nathan Lee","canto_first_approved_date":"2018-04-25 11:39:57","canto_approved_date":"2025-06-24 07:48:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-30 15:59:51","canto_added_date":"2013-12-19 11:44:56","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":84,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Nathan Lee","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.15c","SPCC1442.04c","SPBC32H8.11","SPBP4G3.02","SPAC27D7.07c","SPAC29A4.08c","SPAC20H4.06c","SPAC1F7.01c","SPBP23A10.07","SPNCRNA.247","SPBC16H5.10c","SPAC1F3.01","SPBC428.08c","SPAC140.04","SPBC902.04","SPAC9.03c","SPBC646.04","SPAC26A3.08","SPAC2C4.03c","SPBC646.02","SPBC16E9.12c","SPAC4F8.12c","SPBC146.05c","SPAC222.09","SPBC216.02","SPBC1289.11","SPBP22H7.07","SPBC1709.08","SPBC215.12","SPSNORNA.35","SPBC26H8.10","SPAC27D7.13c","SPAC1006.03c","SPBC725.08","SPCC736.12c","SPAC17H9.02","SPNCRNA.405","SPAC1486.03c","SPSNORNA.32","SPAC17A2.08c","SPNCRNA.214","SPBC16G5.10","SPAC25G10.04c","SPBC20F10.05","SPAC1250.05","SPNCRNA.103","SPNCRNA.488","SPAC7D4.14c","SPAC6F12.16c","SPBC4C3.05c","SPCC1183.07"],"gene_count":51,"ltp_gene_count":39,"approved_date":"2018-04-25"},{"uniquename":"PMID:6597758","title":"Interallelic and intergenic conversion in three serine tRNA genes of Schizosaccharomyces pombe.","citation":"Cold Spring Harb Symp Quant Biol 1984;49:31-40","abstract":"","authors":"Kohli J, Munz P, Aebi R, Amstutz H, Gysler C, Heyer WD, Lehmann L, Schuchert P, Szankasi P, Thuriaux P","authors_abbrev":"Kohli J et al.","pubmed_publication_date":"1984","pubmed_entrez_date":"1984-01-01","publication_year":"1984","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22660415","title":"MPS1/Mph1 phosphorylates the kinetochore protein KNL1/Spc7 to recruit SAC components.","citation":"Nat Cell Biol 2012 Jun 03;14(7):746-52","abstract":"The genomic stability of all organisms depends on the precise partition of chromosomes to daughter cells. The spindle assembly checkpoint (SAC) senses unattached kinetochores and prevents premature entry to anaphase, thus ensuring that all chromosomes attach to opposite spindle poles (bi-orientation) during mitosis. MPS1 is an evolutionarily conserved protein kinase required for the SAC and chromosome bi-orientation. Yet, its primary cellular substrate has remained elusive. We show that fission yeast Mph1 (MPS1 homologue) phosphorylates the kinetochore protein Spc7 (KNL1/Blinkin homologue) at the MELT repeat sequences. This phosphorylation promotes the in vitro binding to the Bub1-Bub3 complex, which is required for kinetochore-based SAC activation (Mad1-Mad2-Mad3 localization) and chromosome alignment. Accordingly, a non-phosphorylatable spc7-12A mutation abolishes kinetochore targeting of Bub1-Bub3, whereas a phospho-mimetic spc7-12E mutation forces them to localize at kinetochores throughout the entire cell cycle, even in the absence of Mph1. Thus, MPS1/Mph1 kinase locating at the unattached kinetochores initially creates a mark, which is crucial for SAC activation and chromosome bi-orientation. This mechanism seems to be conserved in human cells.","doi":"10.1038/ncb2515","authors":"Yamagishi Y, Yang CH, Tanno Y, Watanabe Y","authors_abbrev":"Yamagishi Y et al.","pubmed_publication_date":"03 Jun 2012","pubmed_entrez_date":"2012-06-05","publication_year":"2012","canto_session_key":"682113d8f12b3fe4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2024-03-31 08:02:33","canto_approved_date":"2024-04-22 11:45:18","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-25 17:17:45","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":46,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":21,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1020.02","SPAC23H3.08c","SPBC3D6.04c","SPBC106.01","SPCC1322.12c","SPCC1795.01c","SPBC20F10.06"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2024-03-31"},{"uniquename":"PMID:182390","title":"On the reaction kinetics in water of 1,3-propane sultone and 1,4-butane sultone: a comparison of reaction rates and mutagenic activities of some alkylating agents.","citation":"Chem Biol Interact 1976 Jul;14(1-2):195-202","abstract":"To determine correlations between the biological action pattern and chemical reactivity of alkylating agents, the rate constants for reactions of 1,3-propane sultone and 1,4-butane sultone with a series of nucleophiles at 37 degrees C have been determined. Previously published data on the mutagenicity of the two sultones and of some alkyl methanesulfonates and dialkyl sulfates towards Schizosaccharomyces pombe have been used in the evaluation of the dependence of mutagenic effectiveness on chemical reactivity. It is of interest to note that the mutagenic effectiveness of the two sultones, if expressed per alkylating event at a certain low nucleophilicity is the same as that of e.g. methyl methanesulfonate and ethyl methanesulfonate.","authors":"Osterman-Golkar S, Wachtmeister CA","authors_abbrev":"Osterman-Golkar S et al.","pubmed_publication_date":"Jul 1976","pubmed_entrez_date":"1976-07-01","publication_year":"1976","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23166349","title":"Csi1 links centromeres to the nuclear envelope for centromere clustering.","citation":"J Cell Biol 2012 Nov 26;199(5):735-44","abstract":"In the fission yeast Schizosaccharomyces pombe, the centromeres of each chromosome are clustered together and attached to the nuclear envelope near the site of the spindle pole body during interphase. The mechanism and functional importance of this arrangement of chromosomes are poorly understood. In this paper, we identified a novel nuclear protein, Csi1, that localized to the site of centromere attachment and interacted with both the inner nuclear envelope SUN domain protein Sad1 and centromeres. Both Csi1 and Sad1 mutants exhibited centromere clustering defects in a high percentage of cells. Csi1 mutants also displayed a high rate of chromosome loss during mitosis, significant mitotic delays, and sensitivity to perturbations in microtubule-kinetochore interactions and chromosome numbers. These studies thus define a molecular link between the centromere and nuclear envelope that is responsible for centromere clustering.","doi":"10.1083/jcb.201208001","authors":"Hou H, Zhou Z, Wang Y, Wang J, Kallgren SP, Kurchuk T, Miller EA, Chang F, Jia S","authors_abbrev":"Hou H et al.","pubmed_publication_date":"26 Nov 2012","pubmed_entrez_date":"2012-11-21","publication_year":"2012","canto_session_key":"5c30b3bf5c5da95c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Haitong Hou","canto_first_approved_date":"2018-03-07 11:56:46","canto_approved_date":"2024-04-03 10:34:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-24 12:50:06","canto_added_date":"2012-11-23 09:47:11","annotation_curators":[{"name":"Haitong Hou","community_curator":true,"annotation_count":47,"orcid":null,"file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":1,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.20c","SPBC1105.17","SPCC1020.02","SPBC20F10.06","SPBC800.13","SPCC1322.12c","SPAC1805.07c","SPCC1223.15c","SPBC12D12.01","SPCC736.14","SPAC8C9.17c","SPCC417.02","SPAC27F1.04c","SPCC895.07","SPBC3B9.22c","SPBC409.04c","SPBC106.01","SPBC27.02c","SPBC32F12.08c","SPAC589.08c","SPCC1795.01c","SPBC3D6.04c","SPAC14C4.16","SPBC2G2.14","SPAC16A10.05c"],"gene_count":25,"ltp_gene_count":23,"approved_date":"2018-03-07"},{"uniquename":"PMID:29114019","title":"Native elongating transcript sequencing reveals global anti-correlation between sense and antisense nascent transcription in fission yeast.","citation":"RNA 2018 Feb;24(2):196-208","abstract":"Antisense transcription can regulate sense gene expression. However, previous annotations of antisense transcription units have been based on detection of mature antisense long noncoding (aslnc)RNAs by RNA-seq and/or microarrays, only giving a partial view of the antisense transcription landscape and incomplete molecular bases for antisense-mediated regulation. Here, we used native elongating transcript sequencing to map genome-wide nascent antisense transcription in fission yeast. Strikingly, antisense transcription was detected for most protein-coding genes, correlating with low sense transcription, especially when overlapping the mRNA start site. RNA profiling revealed that the resulting aslncRNAs mainly correspond to cryptic Xrn1/Exo2-sensitive transcripts (XUTs). ChIP-seq analyses showed that antisense (as)XUT's expression is associated with specific histone modification patterns. Finally, we showed that asXUTs are controlled by the histone chaperone Spt6 and respond to meiosis induction, in both cases anti-correlating with levels of the paired-sense mRNAs, supporting physiological significance to antisense-mediated gene attenuation. Our work highlights that antisense transcription is much more extended than anticipated and might constitute an additional nonpromoter determinant of gene regulation complexity.","doi":"10.1261/rna.063446.117","authors":"Wery M, Gautier C, Descrimes M, Yoda M, Vennin-Rendos H, Migeot V, Gautheret D, Hermand D, Morillon A","authors_abbrev":"Wery M et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2017-11-09","publication_year":"2018","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2017-11-10 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23525001","title":"Reversible thiol oxidation in the H2O2-dependent activation of the transcription factor Pap1.","citation":"J Cell Sci 2013 May 15;126(Pt 10):2279-84","abstract":"Reversible thiol oxidation is both a mark of hydrogen peroxide (H2O2) toxicity and an initiator of signalling events. H2O2 sensors contain exposed and reactive cysteine residues, which become transiently oxidized as an activation mechanism. In fission yeast, the Pap1 (pombe AP-1) transcription factor is normally cytosolic, and upon H2O2 stress it undergoes post-translational modifications impairing its nuclear export; genetic evidences suggested the formation of a disulphide bond in Pap1 as a triggering activation event. Nuclear Pap1 is then recruited to about 50-80 promoters and induces an adaptation response. We have now dissected the role of all seven cysteine residues in Pap1 using genetic and proteomic techniques, and we show that four of them are required for Pap1 to be activated by H2O2 stress. Thus, mutants lacking each one of these cysteine residues display sensitivity to peroxides. Furthermore, these mutant proteins do not become oxidized by H2O2 and cannot bind to promoters or trigger the Pap1-dependent gene expression program. We also demonstrate, by proteomic analysis of reduced and oxidized Pap1, that these four cysteine residues are reversibly oxidized upon H2O2 stress. Our study suggests that not just one but probably two disulphide bonds are required to promote the important conformational changes that trigger Pap1 activation and nuclear accumulation.","doi":"10.1242/jcs.124370","authors":"Calvo IA, Ayté J, Hidalgo E","authors_abbrev":"Calvo IA et al.","pubmed_publication_date":"15 May 2013","pubmed_entrez_date":"2013-03-26","publication_year":"2013","canto_session_key":"6e348c63b7404153","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elena Hidalgo","canto_approved_date":"2017-05-09 07:48:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-05 16:16:03","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":56,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Elena Hidalgo","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC609.04","SPAC3C7.14c","SPCC663.08c","SPBC3F6.03","SPBC106.02c","SPAC1783.07c","SPCC757.07c"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2016-07-05"},{"uniquename":"PMID:15060140","title":"In vivo dynamics of Swi6 in yeast: evidence for a stochastic model of heterochromatin.","citation":"Mol Cell Biol 2004 Apr;24(8):3157-67","abstract":"The mechanism for transcriptional silencing of pericentric heterochromatin is conserved from fission yeast to mammals. Silenced genome regions are marked by epigenetic methylation of histone H3, which serves as a binding site for structural heterochromatin proteins. In the fission yeast Schizosaccharomyces pombe, the major structural heterochromatin protein is Swi6. To gain insight into Swi6 function in vivo, we have studied its dynamics in the nucleus of living yeast. We demonstrate that, in contrast to mammalian cells, yeast heterochromatin domains undergo rapid, large-scale motions within the nucleus. Similar to the situation in mammalian cells, Swi6 does not permanently associate with these chromatin domains but binds only transiently to euchromatin and heterochromatin. Swi6 binding dynamics are dependent on growth status and on the silencing factors Clr4 and Rik1, but not Clr1, Clr2, or Clr3. By comparing the kinetics of mutant Swi6 proteins in swi6(-) and swi6(+) strains, we demonstrate that homotypic protein-protein interactions via the chromoshadow domain stabilize Swi6 binding to chromatin in vivo. Kinetic modeling allowed quantitative estimation of residence times and indicated the existence of at least two kinetically distinct populations of Swi6 in heterochromatin. The observed dynamics of Swi6 binding are consistent with a stochastic model of heterochromatin and indicate evolutionary conservation of heterochromatin protein binding properties from mammals to yeast.","authors":"Cheutin T, Gorski SA, May KM, Singh PB, Misteli T","authors_abbrev":"Cheutin T et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-04-03","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11073995","title":"Rdp1, a novel zinc finger protein, regulates the DNA damage response of rhp51(+) from Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2000 Dec;20(23):8958-68","abstract":"The Schizosaccharomyces pombe DNA repair gene rhp51(+) encodes a RecA-like protein with the DNA-dependent ATPase activity required for homologous recombination. The level of the rhp51(+) transcript is increased by a variety of DNA-damaging agents. Its promoter has two cis-acting DNA damage-responsive elements (DREs) responsible for DNA damage inducibility. Here we report identification of Rdp1, which regulates rhp51(+) expression through the DRE of rhp51(+). The protein contains a zinc finger and a polyalanine tract similar to ones previously implicated in DNA binding and transactivation or repression, respectively. In vitro footprinting and competitive binding assays indicate that the core consensus sequences (NGG/TTG/A) of DRE are crucial for the binding of Rdp1. Mutations of both DRE1 and DRE2 affected the damage-induced expression of rhp51(+), indicating that both DREs are required for transcriptional activation. In addition, mutations in the DREs significantly reduced survival rates after exposure to DNA-damaging agents, demonstrating that the damage response of rhp51(+) enhances the cellular repair capacity. Surprisingly, haploid cells containing a complete rdp1 deletion could not be recovered, indicating that rdp1(+) is essential for cell viability and implying the existence of other target genes. Furthermore, the DNA damage-dependent expression of rhp51(+) was significantly reduced in checkpoint mutants, raising the possibility that Rdp1 may mediate damage checkpoint-dependent transcription of rhp51(+).","authors":"Shim YS, Jang YK, Lim MS, Lee JS, Seong RH, Hong SH, Park SD","authors_abbrev":"Shim YS et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-14","publication_year":"2000","canto_session_key":"e0ef2d78919a9983","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-19 16:48:34","canto_approved_date":"2022-02-07 14:04:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-10 15:04:47","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPAC644.14c","SPCC1259.13","SPAC14C4.13","SPBC216.05","SPAC20G4.04c","SPCC18B5.11c","SPAC664.07c","SPAC1B1.01","SPAC9E9.08"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2018-03-19"},{"uniquename":"PMID:15296749","title":"Laser microsurgery in fission yeast; role of the mitotic spindle midzone in anaphase B.","citation":"Curr Biol 2004 Aug 10;14(15):1330-40","abstract":"During anaphase B in mitosis, polymerization and sliding of overlapping spindle microtubules (MTs) contribute to the outward movement the spindle pole bodies (SPBs). To probe the mechanism of spindle elongation, we combine fluorescence microscopy, photobleaching, and laser microsurgery in the fission yeast Schizosaccharomyces pombe.\nWe demonstrate that a green laser cuts intracellular structures in yeast cells with high spatial specificity. By using laser microsurgery, we cut mitotic spindles labeled with GFP-tubulin at various stages of anaphase B. Although cutting generally caused early anaphase spindles to disassemble, midanaphase spindle fragments continued to elongate. In particular, when the spindle was cut near a SPB, the larger spindle fragment continued to elongate in the direction of the cut. Photobleach marks showed that sliding of overlapping midzone MTs was responsible for the elongation of the spindle fragment. Spindle midzone fragments not connected to either of the two spindle poles also elongated. Equatorial microtubule organizing center (eMTOC) activity was not affected in cells with one detached pole but was delayed or absent in cells with two detached poles.\nThese studies reveal that the spindle midzone is necessary and sufficient for the stabilization of MT ends and for spindle elongation. By contrast, SPBs are not required for elongation, but they contribute to the attachment of the nuclear envelope and chromosomes to the spindle, and to cell cycle progression. Laser microsurgery provides a means by which to dissect the mechanics of the spindle in yeast.","authors":"Khodjakov A, La Terra S, Chang F","authors_abbrev":"Khodjakov A et al.","pubmed_publication_date":"10 Aug 2004","pubmed_entrez_date":"2004-08-07","publication_year":"2004","canto_session_key":"74c02a31b1c22007","canto_annotation_status":"APPROVED","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_first_approved_date":"2022-06-13 11:43:20","canto_approved_date":"2022-06-13 11:43:20","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-06-13 11:43:12","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2022-06-13"},{"uniquename":"PMID:24957674","title":"Yeast X-chromosome-associated protein 5 (Xap5) functions with H2A.Z to suppress aberrant transcripts.","citation":"EMBO Rep 2014 Aug;15(8):894-902","abstract":"Chromatin regulatory proteins affect diverse developmental and environmental response pathways via their influence on nuclear processes such as the regulation of gene expression. Through a genome-wide genetic screen, we implicate a novel protein called X-chromosome-associated protein 5 (Xap5) in chromatin regulation. We show that Xap5 is a chromatin-associated protein acting in a similar manner as the histone variant H2A.Z to suppress expression of antisense and repeat element transcripts throughout the fission yeast genome. Xap5 is highly conserved across eukaryotes, and a plant homolog rescues xap5 mutant yeast. We propose that Xap5 likely functions as a chromatin regulator in diverse organisms.","doi":"10.15252/embr.201438902","authors":"Anver S, Roguev A, Zofall M, Krogan NJ, Grewal SI, Harmer SL","authors_abbrev":"Anver S et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-06-25","publication_year":"2014","canto_session_key":"cfba7cb5d851df37","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shajahan Anver","canto_approved_date":"2016-02-08 15:16:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-02 09:00:49","canto_added_date":"2014-06-26 00:15:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Shajahan Anver","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC663.17","SPAC25H1.03","SPBC17A3.10","SPAPB15E9.03c","SPBC4F6.11c","SPAC5H10.09c","SPCC4G3.19","SPBC26H8.03","SPBC106.20","SPAC18B11.10","SPAC3G9.11c","SPBC3E7.10","SPAC31G5.11","SPBC17A3.06","SPBC16A3.12c","SPBC21C3.02c","SPBC11B10.07c","SPBC3H7.10","SPAC23C11.04c","SPAPB1E7.04c","SPCC188.13c","SPCC330.03c","SPAC3C7.04","SPBC337.03","SPAC140.02","SPBC30B4.06c","SPBC11C11.10","SPAC343.12","SPCC18.17c","SPBC21B10.08c","SPCP20C8.02c","SPCC1281.04","SPAC1486.04c","SPBC1683.02","SPAC1782.02c","SPAC824.04","SPAC22H10.02","SPAC19D5.03","SPBC19G7.06","SPAC3G6.01","SPCC1739.10","SPAC4A8.10","SPAC6G10.06","SPAC222.08c","SPAC1805.14","SPAC1782.09c","SPAC1805.04","SPAPB1A10.14","SPAC24B11.09","SPBC28F2.08c","SPAC139.06","SPAC630.07c","SPCC11E10.08","SPBC2A9.11c","SPBC1604.20c","SPAC15A10.06","SPCC4F11.03c","SPAC1039.02","SPBC947.03c","SPBC29A3.10c","SPAC12G12.03","SPAC22A12.17c","SPAC1F7.06","SPAC767.01c","SPAC458.02c","SPCC188.09c","SPBC6B1.05c","SPCC1235.11","SPCC1906.03","SPBC713.05","SPCC1620.08","SPAC9E9.11","SPBC685.06","SPCC965.13","SPAC977.17","SPBC31E1.02c","SPAC343.11c","SPCC1450.08c","SPBC16A3.01","SPBPB7E8.01","SPAC26A3.06","SPAC1250.03","SPCC162.04c","SPAC1805.06c","SPBC24C6.10c","SPCC126.04c","SPAC29B12.14c","SPBC25B2.01","SPBC20F10.05","SPAC8F11.02c","SPAC25B8.17","SPAC11E3.01c","SPAPB15E9.06","SPBC1215.01","SPBC4F6.10","SPAC589.07c","SPAC1F3.02c","SPCC1183.10","SPAC9.10","SPBC1A4.04","SPAC13G6.09","SPAC22E12.11c","SPBC106.12c","SPBC115.02c","SPAC2F7.08c","SPAC959.08","SPAPB1A10.03","SPAC9E9.13","SPAC1610.01","SPAC19A8.11c","SPBC354.10","SPAC12G12.01c","SPAC1783.02c","SPAC4F10.13c","SPAC1A6.03c","SPCC1223.02","SPBC1198.09","SPBC1198.06c","SPAC2H10.01","SPAC23E2.01","SPAC3C7.06c","SPAC56F8.06c","SPCC285.17","SPAC19B12.06c","SPAC14C4.12c","SPCC1020.12c","SPAC7D4.08","SPAC26H5.05","SPAC57A10.09c","SPAC3G9.15c","SPCC417.12","SPBC32C12.03c","SPAC3C7.01c","SPAC1527.02","SPAC6B12.06c","SPBC32F12.03c","SPAC22H10.09","SPAC824.02","SPBC115.03","SPAPYUG7.06","SPCC736.05","SPBC6B1.03c","SPBC409.11","SPBP4H10.18c","SPBC19G7.09","SPBC428.11","SPBC4B4.04","SPAC17C9.08","SPAC1F5.05c","SPAC19G12.08","SPAC29B12.10c","SPAPB1A10.13","SPAC30C2.04","SPBC660.11","SPBC29B5.04c","SPBC800.11","SPAC3G9.03","SPAC3H5.07","SPCC70.10","SPBC1778.09","SPAC9E9.03","SPAC1F7.08","SPBC16H5.12c","SPAC17C9.14","SPCC285.16c","SPBP26C9.03c","SPAC2F7.17","SPBC17G9.09","SPAC9G1.08c","SPAC2F7.03c","SPBC1773.06c","SPAC20H4.09","SPAC29A4.09","SPBC947.06c","SPCC569.07","SPBC16E9.12c","SPAC23H4.08","SPBC1685.15c","SPBC20F10.10","SPAC19A8.04","SPBC14F5.10c","SPAC4G9.16c","SPCC1442.11c","SPAC750.08c","SPCC622.15c","SPBC18H10.19","SPBC405.06","SPBC215.03c","SPCC306.11","SPAC9G1.07","SPBC8E4.03","SPCC1322.08","SPBC2G2.01c","SPAC4D7.07c","SPBC28E12.04","SPBC4C3.08","SPAC18B11.03c","SPCC1620.02","SPAC22F8.07c","SPCC1281.07c","SPCC970.11c","SPAC1093.06c","SPAC22E12.03c","SPCC285.07c","SPBP8B7.21","SPAC4G8.10","SPAC17H9.08","SPAC19E9.02","SPAC23C4.03","SPBC23E6.01c","SPCC4G3.18","SPAC977.05c","SPBC11G11.03","SPAC17C9.05c","SPAC17C9.07","SPBC776.14","SPAC1851.02","SPAC20H4.11c","SPCC622.08c","SPAC6G10.08","SPAC869.11","SPBC543.02c","SPBC2G2.14","SPBC83.17","SPAPB8E5.05","SPBC29A3.02c","SPAC20H4.03c","SPBC19C7.05","SPBC1539.08","SPAC1952.12c","SPAC343.10","SPAC9E9.12c","SPBC23E6.03c","SPAC16C9.05","SPBC16G5.13","SPBC800.03","SPAC12B10.03","SPAC17D4.03c","SPCC622.02","SPBC2F12.05c","SPCC1620.11","SPBC1683.10c","SPAC17A2.11","SPBC17D1.05","SPBC21D10.10","SPBC16E9.16c","SPAC1687.15","SPBC646.02","SPBP16F5.05c","SPBC2G5.06c","SPBC428.02c","SPCC1281.08","SPAC6F12.09","SPAC343.16","SPBC12C2.12c","SPBC2D10.06","SPBC1A4.05","SPAC1142.04","SPCC338.14","SPAC13C5.06c","SPAC6F6.13c","SPBP26C9.02c","SPCC1450.05c","SPAC1002.02","SPAC31A2.14","SPCC306.07c","SPACUNK4.16c","SPBC337.09","SPBC13G1.08c","SPBC1861.02","SPCC794.01c","SPAC4F10.19c","SPAC17D4.01","SPBC19C7.12c","SPCC306.09c","SPCC1450.06c","SPBC1683.09c","SPBC409.20c","SPBC36.05c","SPAC2F7.04","SPCP20C8.01c","SPAC13D6.03c","SPAC30D11.07","SPAC637.07","SPBC530.14c","SPBC2F12.11c","SPBC776.11","SPCC613.03","SPAC22F3.04","SPAC1705.02","SPBC29A10.01","SPBC1773.09c","SPAC23G3.03","SPBC215.11c","SPCC126.06","SPBC17G9.08c","SPCP1E11.03","SPAC3H1.03","SPCP1E11.11","SPCC622.12c","SPBC23E6.10c","SPBC16D10.08c","SPAC14C4.01c","SPAC22E12.01","SPCC306.06c","SPAC1093.01","SPCC330.06c","SPAC2C4.16c","SPBC354.12","SPAC31G5.21","SPAC16C9.06c","SPBC354.03","SPAPYUG7.04c","SPAC31A2.09c","SPAC922.05c","SPBC3H7.12","SPCC777.06c","SPAC1F5.03c","SPBP8B7.26","SPBC31F10.17c","SPAC1420.01c","SPAC30D11.02c","SPBC8E4.01c","SPAC3F10.05c","SPAC1071.02","SPBC19C7.01","SPAC6F12.03c","SPAC637.06","SPAC30D11.04c","SPAC922.04","SPAC30.04c","SPCC306.04c","SPCC777.04","SPAC167.04","SPAC9G1.11c","SPCC1322.03","SPCC1223.03c","SPBC31F10.13c","SPBC12C2.09c","SPAC664.02c","SPCC1020.13c","SPBC56F2.10c","SPCC794.02","SPCC132.04c","SPAC2C4.09","SPBC31F10.07","SPAC6G9.03c","SPACUNK4.09","SPBC29A10.07","SPAC458.04c","SPAPJ695.01c","SPBC31F10.02","SPAC4F10.14c","SPBC2A9.04c","SPAC4D7.02c","SPAC56E4.06c","SPAC1006.03c","SPBC18A7.02c","SPCC645.08c","SPAC1687.06c","SPCC1442.04c","SPCC622.04","SPAC2C4.17c","SPBC365.14c","SPAC13G7.03","SPBC1289.11","SPBC1921.07c","SPAC19B12.11c","SPCPB1C11.01","SPBC56F2.06","SPAC1952.06c","SPBC8D2.17","SPAC23H3.05c","SPAC11H11.03c","SPAC22E12.14c","SPBC13E7.08c","SPAC9E9.08","SPAC13A11.04c","SPAC3C7.10","SPAC806.04c","SPAC31G5.14","SPCC584.01c","SPAC8F11.10c","SPCC1322.02","SPBC543.10","SPBC17G9.07","SPAC1F7.05","SPBC800.09","SPAC9G1.02","SPAC31G5.12c","SPAC13G6.10c","SPAC26F1.01","SPBC1709.11c","SPAC694.04c","SPBC119.12","SPCC594.05c","SPAC222.16c","SPBC725.14","SPBC119.03","SPCC550.11","SPBC11G11.01","SPCC162.06c","SPBC8E4.05c","SPBC2G2.13c","SPAC890.03","SPBC27.02c","SPAC17C9.10","SPBC3B8.08","SPAC1B3.08","SPAC17C9.13c","SPAC23C11.14","SPBC428.08c","SPAC1805.07c","SPAC1805.08","SPAC6C3.08","SPAC24C9.05c","SPAC5H10.06c","SPBC18H10.07","SPCC330.11","SPAC27F1.05c","SPBC119.04","SPAC9E9.09c","SPBC16E9.02c","SPAC3C7.02c","SPBP23A10.14c","SPBC21C3.01c","SPAC17A5.05c","SPBC30B4.04c","SPCC74.06","SPBC4F6.12","SPBC1604.03c","SPAC1B3.16c","SPAC869.08","SPBC428.05c","SPAC13G7.13c","SPBC3H7.09","SPBC11B10.10c","SPCC622.01c","SPAC140.03","SPAC25G10.03","SPBC660.14","SPCC188.07","SPAC823.05c","SPBC2F12.03c","SPCC1739.15","SPAC16E8.17c","SPBC713.08","SPAC4F10.04","SPAC23G3.10c","SPAC26H5.08c","SPAC1805.10","SPBP8B7.30c","SPCC306.08c","SPAC513.03","SPAC23A1.03","SPBP8B7.09c","SPAC13G7.02c","SPAC139.01c","SPAC15E1.02c","SPCC1919.05","SPAC1F7.10","SPBC36.04","SPAC9.07c","SPAC4G9.10","SPAC9E9.17c","SPAC4G8.13c","SPBC27B12.11c","SPBC2G2.10c","SPCC794.03","SPAC1002.07c","SPCC613.01","SPAP14E8.02","SPAC29B12.04","SPAC1D4.09c","SPAC27E2.01","SPBC36.06c","SPCC576.12c","SPBC1861.03","SPCC663.14c","SPCC1884.01","SPAC9.02c"],"gene_count":481,"ltp_gene_count":3,"approved_date":"2014-07-02"},{"uniquename":"PMID:5728838","title":"Spontaneous frequencies of lethal-sectoring and mutation in radiation-sensitive strains of Schizosaccharomyces pombe.","citation":"Mutat Res 1968;6(3):475-8","abstract":"","authors":"Nasim A, Saunders AS","authors_abbrev":"Nasim A et al.","pubmed_publication_date":"1968","pubmed_entrez_date":"1968-11-01","publication_year":"1968","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12376568","title":"An evolutionarily conserved fission yeast protein, Ned1, implicated in normal nuclear morphology and chromosome stability, interacts with Dis3, Pim1/RCC1 and an essential nucleoporin.","citation":"J Cell Sci 2002 Nov 15;115(Pt 22):4375-85","abstract":"We identified a novel fission yeast gene, ned1(+), with pleiotropic mutations that have a high incidence of chromosome missegregation, aberrantly shaped nuclei, overdeveloped endoplasmic reticulum-like membranes, and increased sensitivity to a microtubule destabilizing agent. Ned1 protein, which was phosphorylated in a growth-related manner, interacted in a yeast two-hybrid system with Dis3 as well as with Pim1/RCC1 (nucleotide exchange factor for Ran). Ned1 also interacted with an essential nucleoporin, a probable homologue of mammalian Nup98/96. The ned1 gene displayed a variety of genetic interactions with factors involved in nuclear transport and chromosome segregation, including the crm1 (exportin), spi1 (small GTPase Ran), pim1, and dis genes. A substitution mutation that affected the two-hybrid interaction with Dis3 increased chromosome instability, suggesting the functional importance of the interaction. Overproduction of Ned1 protein induced formation of an abnormal microtubule bundle within the nucleus, apparently independently of the spindle pole body, but dependent on pim1(+) activity. The ned1(+) gene belongs to an evolutionarily conserved gene family, which includes the mouse Lpin genes, one of whose mutations is responsible for lipodystrophy.","authors":"Tange Y, Hirata A, Niwa O","authors_abbrev":"Tange Y et al.","pubmed_publication_date":"15 Nov 2002","pubmed_entrez_date":"2002-10-12","publication_year":"2002","canto_session_key":"4d6014a904a1e84b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-23 16:53:51","canto_approved_date":"2026-01-31 12:13:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-01 12:54:45","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":54,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1486.05","SPBC26H8.10","SPBC776.02c","SPAC1805.17","SPBC12D12.01","SPCC736.14","SPAC3C7.14c","SPBC354.02c","SPBC1289.03c","SPBC557.03c","YMR165C","SPAC1952.13"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2018-04-23"},{"uniquename":"PMID:1379173","title":"A mechanosensitive ion channel in Schizosaccharomyces pombe.","citation":"EMBO J 1992 Aug;11(8):2869-75","abstract":"Protoplast protuberances (blebs) of Schizosaccharomyces pombe were examined using the patch-clamp technique. In addition to several voltage-gated ion channels, we encountered the activities of a mechanosensitive ion channel with a conductance of 180 pS. Microscopic currents of one or two units were observed in some excised patches and ensemble currents of several tens of units were observed in all blebs examined in whole-bleb configuration. This channel opens at pressures of cm Hg applied to whole blebs and it passes cations, including Ca2+. It is inactivated by membrane depolarizations and blocked by Gd3+. We discuss the possible functions of such a channel, including its activation upon cell cycle dependent cytoskeletal reorganizations.","authors":"Zhou XL, Kung C","authors_abbrev":"Zhou XL et al.","pubmed_publication_date":"Aug 1992","pubmed_entrez_date":"1992-08-01","publication_year":"1992","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25351951","title":"Mutations in the tricarboxylic acid cycle enzyme, aconitase 2, cause either isolated or syndromic optic neuropathy with encephalopathy and cerebellar atrophy.","citation":"J Med Genet 2014 Dec;51(12):834-8","abstract":"Inherited optic neuropathy has been ascribed to mutations in mitochondrial fusion/fission dynamics genes, nuclear and mitochondrial DNA-encoded respiratory enzyme genes or nuclear genes of poorly known mitochondrial function. However, the disease causing gene remains unknown in many families.\nWe used exome sequencing in order to identify the gene responsible for isolated or syndromic optic atrophy in five patients from three independent families.\nWe found homozygous or compound heterozygous missense and frameshift mutations in the gene encoding mitochondrial aconitase (ACO2), a tricarboxylic acid cycle enzyme, catalysing interconversion of citrate into isocitrate. Unlike wild type ACO2, all mutant ACO2 proteins failed to complement the respiratory growth of a yeast aco1-deletion strain. Retrospective studies using patient-derived cultured skin fibroblasts revealed various degrees of deficiency in ACO2 activity, but also in ACO1 cytosolic activity.\nOur study shows that autosomal recessive ACO2 mutations can cause either isolated or syndromic optic neuropathy. This observation identifies ACO2 as the second gene responsible for non-syndromic autosomal recessive optic neuropathies and provides evidence for a genetic overlap between isolated and syndromic forms, giving further support to the view that optic atrophy is a hallmark of defective mitochondrial energy supply.","doi":"10.1136/jmedgenet-2014-102532","authors":"Metodiev MD, Gerber S, Hubert L, Delahodde A, Chretien D, Gérard X, Amati-Bonneau P, Giacomotto MC, Boddaert N, Kaminska A, Desguerre I, Amiel J, Rio M, Kaplan J, Munnich A, Rötig A, Rozet JM, Besmond C","authors_abbrev":"Metodiev MD et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-10-30","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC31H12.07","SPAC24C9.06c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:24177952","title":"The mitochondrial genome of the fission yeast Schizosaccharomyces pombe : 5. Characterization of mitochondrial deletion mutants.","citation":"Curr Genet 1984 Sep;8(7):517-24","abstract":"The three mutator strains ana (r)-8, ana (r)-14, and diu (r)-301 were shown to produce respiratory deficient mutants at different rates. The frequency of respiratory deficient mutants in a culture could be increased by adding ethidium bromide. According to their cytochrome spectra and enzymatic activities they form three classes, namely mutants defective in cytochrome oxidase, in cytochrome b, and in both cytochromes. By restriction enzyme analysis of mitochondrial DNA from about 100 mutants, 22 deletion mutants were identified. The deletions, ranging from 50 to 1,500 base pairs were physically mapped. Deletions were localized in the genes coding for subunit 1 of cytochrome oxidase with its two introns, within the cytochrome b gene and its intron, and within the genes for subunits 2 and 3 of cytochrome oxidase. In several cases, where the physical mapping yielded ambiguous results, pairwise genetic crosses ruled out an overlap between two neighbouring deletions.Using these mitochondrial deletion mutants as tester strains, it was shown that only tetrad analysis and chemical haploidization, but not mitotic segregation analysis, allows a decision between chromosomal and mitochondrial inheritance of respiratory deficiency in Schizosaccharomyces pombe.","doi":"10.1007/BF00410438","authors":"Ahne F, Merlos-Lange AM, Lang BF, Wolf K","authors_abbrev":"Ahne F et al.","pubmed_publication_date":"Sep 1984","pubmed_entrez_date":"2013-11-02","publication_year":"1984","canto_session_key":"fcee583911ed7102","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-04-09 17:44:27","canto_approved_date":"2018-04-09 17:44:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-07 19:44:21","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMIT.04","SPMIT.11"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-04-09"},{"uniquename":"PMID:29300771","title":"Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans.","citation":"PLoS One 2018;13(1):e0190524","abstract":"In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-dependent ATPase, was considered \"fungal-specific\", however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes. In order to determine whether divergent eEF3-like proteins from other eukaryotic organisms can provide the essential functions of eEF3 in budding yeast, the eEF3-like proteins from Schizosaccharomyes pombe and an oomycete, Phytophthora infestans, were cloned and expressed in Saccharomyces cerevisiae. Plasmid shuffling experiments showed that both S. pombe and P. infestans eEF3 can support the growth of S. cerevisiae in the absence of endogenous budding yeast eEF3. Consistent with its ability to provide the essential functions of eEF3, P. infestans eEF3 possessed ribosome-dependent ATPase activity. Yeast cells expressing P. infestans eEF3 displayed reduced protein synthesis due to defects in translation elongation/termination. Identification of eEF3 in divergent species will advance understanding of its function and the ribosome specific determinants that lead to its requirement as well as contribute to the identification of functional domains of eEF3 for potential drug discovery.","doi":"10.1371/journal.pone.0190524","authors":"Mateyak MK, Pupek JK, Garino AE, Knapp MC, Colmer SF, Kinzy TG, Dunaway S","authors_abbrev":"Mateyak MK et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-01-05","publication_year":"2018","canto_session_key":"518f010075250e18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-01-20 16:04:35","canto_approved_date":"2018-01-20 16:04:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-20 16:04:23","canto_added_date":"2018-01-09 01:15:23","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC417.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-01-20"},{"uniquename":"EMBL:AU014505","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16317047","title":"Ace2p contributes to fission yeast septin ring assembly by regulating mid2+ expression.","citation":"J Cell Sci 2005 Dec 15;118(Pt 24):5731-42","abstract":"The fission yeast Schizosaccharomyces pombe divides through constriction of an actomyosin-based contractile ring followed by formation and degradation of a medial septum. Formation of an organized septin ring is also important for the completion of S. pombe cell division and this event relies on the production of Mid2p. mid2+ mRNA and protein accumulate in mitosis. Recent microarray analyses identified mid2+ as a target of the Ace2p transcription factor, and ace2+ as a target of the Sep1p transcription factor. In this study, we find that Mid2p production is controlled by Ace2p functioning downstream of Sep1p. Consequently, both Sep1p and Ace2p are required for septin ring assembly and genetic analyses indicate that septin rings function in parallel with other Ace2p targets to achieve efficient cell division. Conversely, forced overproduction of Sep1p or Ace2p prevents septin ring disassembly. We find that Ace2p levels peak during anaphase and Ace2p is post-translationally modified by phosphorylation and ubiquitylation. Ace2p localizes symmetrically to dividing nuclei and functions independently of the septation initiation network.","authors":"Petit CS, Mehta S, Roberts RH, Gould KL","authors_abbrev":"Petit CS et al.","pubmed_publication_date":"15 Dec 2005","pubmed_entrez_date":"2005-12-01","publication_year":"2005","canto_session_key":"fe9525dbeb7dffdb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-22 15:51:56","canto_approved_date":"2024-08-13 15:50:15","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-22 15:51:49","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":34,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC16A3.01","SPBC4C3.12","SPAC6G10.12c","SPBC16G5.15c","SPBC19G7.06","SPAPJ760.03c","SPCC18.01c","SPAC19G12.16c","SPAPYUG7.03c","SPAC821.09","SPAC14C4.09"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2024-07-22"},{"uniquename":"PMID:20094030","title":"Structural diversity and dynamics of genomic replication origins in Schizosaccharomyces pombe.","citation":"EMBO J 2010 Mar 03;29(5):934-42","abstract":"DNA replication origins (ORI) in Schizosaccharomyces pombe colocalize with adenine and thymine (A+T)-rich regions, and earlier analyses have established a size from 0.5 to over 3 kb for a DNA fragment to drive replication in plasmid assays. We have asked what are the requirements for ORI function in the chromosomal context. By designing artificial ORIs, we have found that A+T-rich fragments as short as 100 bp without homology to S. pombe DNA are able to initiate replication in the genome. On the other hand, functional dissection of endogenous ORIs has revealed that some of them span a few kilobases and include several modules that may be as short as 25-30 contiguous A+Ts capable of initiating replication from ectopic chromosome positions. The search for elements with these characteristics across the genome has uncovered an earlier unnoticed class of low-efficiency ORIs that fire late during S phase. These results indicate that ORI specification and dynamics varies widely in S. pombe, ranging from very short elements to large regions reminiscent of replication initiation zones in mammals.","doi":"10.1038/emboj.2009.411","authors":"Cotobal C, Segurado M, Antequera F","authors_abbrev":"Cotobal C et al.","pubmed_publication_date":"03 Mar 2010","pubmed_entrez_date":"2010-01-23","publication_year":"2010","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17001618","title":"Combined use of two transcriptional reporters improves signalling assays for G protein-coupled receptors in fission yeast.","citation":"Yeast 2006 Sep;23(12):889-97","abstract":"The biochemical and genetic tractability of yeasts make them ideal hosts for the analysis of signalling from G protein-coupled receptors (GPCRs). Selected modifications to the strains allow the introduction of non-yeast components, while signal-dependent expression of reporter genes provides growth selection or enzyme read-out as assays for signalling. One issue with such systems is reporter expression in the absence of stimulation, usually because of spontaneous activation of intracellular signalling components and/or incomplete repression of the signal-dependent promoter. This limits the difference between reporter activity in the presence and absence of stimulation, often referred to as the signal:background ratio. In an effort to extend the applicability of the yeast system, we generated a Schizosaccharomyces pombe strain containing pheromone-dependent reporters for both growth selection and beta-galactosidase production. Simultaneous use of the two reporters provided several advantages over strains expressing only one reporter, particularly when coupled to the use of a competitive inhibitor of the nutritional reporter. For example, the beta-galactosidase signal:background ratio following stimulation with 10(-6) M P-factor increased from 35 for a strain containing a single lacZ reporter to almost 2500 for the double reporter. The sensitivity of the system was also improved, with higher signal:background ratios allowing detection of lower concentrations of P-factor. Although we have used Sz. pombe and focused on GPCR-based induction of beta-galactosidase, the principles described can be applied to other yeasts, different signalling pathways and alternative reporters.","authors":"Das A, Forfar R, Ladds G, Davey J","authors_abbrev":"Das A et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-09-27","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17459084","title":"X-ray tomography of Schizosaccharomyces pombe.","citation":"Differentiation 2007 Jul;75(6):529-35","abstract":"The genetic tractability of the unicellular yeast Schizosaccharomyces pombe has resulted in it becoming an important model organism for the study of many eukaryotic cellular processes, in particular cell division. Over the past few years much progress has been made toward understanding the mechanisms that regulate eukaryotic cell division and the cellular changes that occur-for example, the formation of the cytokinetic contractile ring. However, a full understanding requires both identification of the proteins involved and correlation of this information with images showing the location of molecules in context of the cell architecture. Electron microscopic analyses have revealed exquisite ultrastructural images of cell structure, but this technique typically requires extensive processing-procedures that are labor intensive and time consuming. Imaging techniques that can more rapidly obtain better resolution than light microscopy are needed to advance the use of this model system for precise molecular localization analyses. In this manuscript, we examined S. pombe using soft X-ray tomography, an imaging technique that generates three-dimensional (3-D) images of intact hydrated cells at better than 50 nm isotropic resolution. This technique uses X-rays in the \"water window,\" where organic material absorbs approximately an order of magnitude more strongly than water, producing high-contrast images of cellular structures. As cells are examined in the absence of any chemical fixatives, stains, or contrast enhancement reagents, the images reflect cellular structures in the near-native state. We conducted preliminary soft X-ray imaging of S. pombe cells before and during cell division that revealed subcellular organelles, the actomyosin ring, and the septum of dividing cells. These images reveal tantalizing details of the cytokinesis process and are the first steps in our goal of generating a portfolio of tomographic images that map the location of labeled molecules into high-resolution 3-D reconstructions of the cell.","authors":"Gu W, Etkin LD, Le Gros MA, Larabell CA","authors_abbrev":"Gu W et al.","pubmed_publication_date":"Jul 2007","pubmed_entrez_date":"2007-04-27","publication_year":"2007","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12952894","title":"Stable inheritance of telomere chromatin structure and function in the absence of telomeric repeats.","citation":"Genes Dev 2003 Sep 15;17(18):2271-82","abstract":"It is generally believed that telomeric repeats are a necessary and sufficient cis-element for telomere function. Here we show that telomere structure and meiotic function are stably inherited in fission yeast circular chromosomes that have lost all telomeric repeats. We found that the telomeric repeat binding protein, Taz1, and the heterochromatin protein, Swi6, remain associated with subtelomeres in the absence of telomeric repeats. We also found that the fusion point of circular chromosomes that lack telomeric repeats associates with SPB (the yeast counterpart of the centrosome) in the premeiotic horsetail stage, similarly to wild-type telomeres. However, a taz1+ deletion/reintroduction experiment revealed that the maintenance of Taz1 binding and premeiotic function is achieved via different strategies. Taz1 is recruited to subtelomeres by an autonomous element present in subtelomeric DNA, thus in a genetic mechanism. In contrast, the premeiotic subtelomere-SPB association is maintained in an epigenetic manner. These results shed light on the previously unrecognized role played by the subtelomere and underscore the robust nature of the functional telomere complex that is maintained by both genetic and epigenetic mechanisms. Furthermore, we suggest that the establishment and the maintenance of the functional telomere complex are mechanistically distinguishable.","authors":"Sadaie M, Naito T, Ishikawa F","authors_abbrev":"Sadaie M et al.","pubmed_publication_date":"15 Sep 2003","pubmed_entrez_date":"2003-09-04","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11553781","title":"Serine-345 is required for Rad3-dependent phosphorylation and function of checkpoint kinase Chk1 in fission yeast.","citation":"Proc Natl Acad Sci U S A 2001 Sep 25;98(20):11289-94","abstract":"Genome integrity is monitored by a checkpoint that delays mitosis in response to DNA damage. This checkpoint is enforced by Chk1, a protein kinase that inhibits the mitotic inducer Cdc25. In fission yeast, Chk1 is regulated by a group of proteins that includes Rad3, a protein kinase related to human ATM and ATR. These kinases phosphorylate serine or threonine followed by glutamine (SQ/TQ). Fission yeast and human Chk1 proteins share two conserved SQ motifs at serine-345 and serine-367. Serine-345 of human Chk1 is phosphorylated in response to DNA damage. Here we report that Rad3 and ATM phosphorylate serine-345 of fission yeast Chk1. Mutation of serine-345 (chk1-S345A) abrogates Rad3-dependent phosphorylation of Chk1 in vivo. The chk1-S345A cells are sensitive to DNA damage and are checkpoint defective. In contrast, mutations of serine-367 and other SQ/TQ sites do not substantially impair the checkpoint or cause damage sensitivity. These findings attest to the importance of serine-345 phosphorylation for Chk1 function and strengthen evidence that transduction of the DNA damage checkpoint signal requires direct phosphorylation of Chk1 by Rad3.","authors":"Lopez-Girona A, Tanaka K, Chen XB, Baber BA, McGowan CH, Russell P","authors_abbrev":"Lopez-Girona A et al.","pubmed_publication_date":"25 Sep 2001","pubmed_entrez_date":"2001-09-13","publication_year":"2001","canto_session_key":"1eee81410bebb43e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2017-11-28 13:39:17","canto_approved_date":"2025-09-04 11:22:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-17 19:04:10","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPBC216.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-11-28"},{"uniquename":"PMID:38592956","title":"Search for protein kinase(s) related to cell growth or viability maintenance in the presence of ethanol in budding and fission yeasts.","citation":"Biosci Biotechnol Biochem 2024 Apr 09;","abstract":"Alcohol fermentation comprises two phases: phase 1, alcohol fermentation occurs while yeast cells proliferate; phase 2, growth stops and alcohol fermentation continues. We categorized genes related to proliferation in low ethanol (phase 1) and viability in high ethanol (phase 2) as Alcohol Growth Ability (AGA) and Alcohol Viability (ALV), respectively. Although genes required for phase 1 are examined in budding yeast, those for phase 2 are unknown. We set conditions for ALV screening, searched for protein kinases (PKs) related to ALV in budding yeast, and expanded two screenings to fission yeast. Bub1 kinase was important for proliferation in low ethanol but not for viability in high ethanol, suggesting that the important PKs differ between the two phases. It was indeed the case. Further, three common PKs were identified as AGA in both yeasts, suggesting that the important cellular mechanism in phase 1 is conserved in both yeasts, at least partially.","doi":"10.1093/bbb/zbae044","authors":"Ushiyama Y, Nishida I, Tomiyama S, Tanaka H, Kume K, Hirata D","authors_abbrev":"Ushiyama Y et al.","pubmed_publication_date":"09 Apr 2024","pubmed_entrez_date":"2024-04-09","publication_year":"2024","canto_session_key":"563a36ae0a3c1f1e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-04-09 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11405625","title":"A novel Cdc20-related WD-repeat protein, Fzr1, is required for spore formation in Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2001 May;265(3):424-35","abstract":"Ste9/Srw1 which shows sequence homology to Hctl from budding yeast, is an activator of the anaphase-promoting complex (APC) in the fission yeast Schizosaccharomyces pombe. By homology search of the S. pombe genome, we identified the gene fr1+, which encodes the protein with the highest homology to Ste9 among five Cdc20-like proteins. Like Ste9, Fzr1 contains seven WD-repeats in its C-terminal region. In spite of this structural similarity, however, overproduction of either of these proteins cannot complement mutants lacking the other. fzr1+ is transcribed exclusively during meiosis and sporulation, suggesting that it plays a role in these processes. In fact, the fzr1 disruptant formed aberrant asci, which contained only one or two mature spores, though meiotic nuclear divisions proceeded with kinetics similar to wild type, and meiotic segregation of chromosomes was normal. Structural alteration of spindle pole bodies, which is a prerequisite for the formation of the forespore membrane, occurred normally in fzr1delta during the second meiotic division. Localization of spore rim marker proteins fused to green fluorescent protein showed that nascent prespores were irregularly shaped, small in size and few in number in fzr1delta cells compared to wild-type cells. Furthermore, electron microscopy revealed that the outer layer of the spore walls was often missing in fzr1delta spores. These results show that Fzr1 is specifically involved in the assembly of the spore envelope and also in spore maturation. Fzr1, a structural homolog of the APC regulator, therefore plays an important role in spore morphogenesis.","authors":"Asakawa H, Kitamura K, Shimoda C","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-06-19","publication_year":"2001","canto_session_key":"81cdad3b15bdd1e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Haruhiko Asakawa","canto_first_approved_date":"2015-05-01 14:27:32","canto_approved_date":"2026-01-04 11:02:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-13 01:15:48","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Haruhiko Asakawa","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.04","SPBC1198.12","SPBC32H8.11"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-05-01"},{"uniquename":"PMID:9003296","title":"5-Azacytidine treatment of the fission yeast leads to cytotoxicity and cell cycle arrest.","citation":"Mol Gen Genet 1996 Nov 27;253(1-2):128-37","abstract":"A fission yeast gene which shares considerable sequence homology with cytosine-specific DNA methyltransferases has recently been identified. This discovery has led us to investigate the effects of the treatment of fission yeast with the nucleoside analogue 5-azacytidine (5-azaC). 5-AzaC is known to inhibit cytosine methylation as a result of the formation of stable covalent complexes between DNA (cytosine-5) methyltransferases (C5 Mtases) and 5-azaC containing DNA. Here we demonstrate that 5-azaC treatment of Schizosaccharomyces pombe leads to reversible cell cycle arrest at the G2/M transition. This reversible arrest is dependent on the cell cycle checkpoint mechanisms which act to prevent the onset of mitosis in the presence of either damaged or unreplicated DNA. Treatment of S. pombe cell division cycle and checkpoint mutants indicates that 5-azaC causes DNA damage and is likely to inhibit a late stage in DNA replication. The data show that viability in the presence of the drug requires both the DNA damage and the replication checkpoint pathways to be functional. 5-AzaC also elicits a transcriptional response which is associated with DNA damage and the inhibition of DNA replication in fission yeast, and this response is absent in cells carrying G2 checkpoint mutations. The implications of these observations for both the use of 5-azaC in cancer chemotherapy and the existence of cytosine methylation in fission yeast are discussed.","authors":"Taylor EM, McFarlane RJ, Price C","authors_abbrev":"Taylor EM et al.","pubmed_publication_date":"27 Nov 1996","pubmed_entrez_date":"1996-11-27","publication_year":"1996","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23324799","title":"Characterisation of an intrinsically disordered protein complex of Swi5-Sfr1 by ion mobility mass spectrometry and small-angle X-ray scattering.","citation":"Analyst 2013 Mar 07;138(5):1441-9","abstract":"It is now recognized that intrinsically disordered proteins (IDPs) play important roles as hubs in intracellular networks, and their structural characterisation is of significance. However, due to their highly dynamic features, it is challenging to investigate the structures of IDPs solely by conventional methods. In the present study, we demonstrate a novel method to characterise protein complexes using electrospray ionization ion mobility mass spectrometry (ESI-IM-MS) in combination with small-angle X-ray scattering (SAXS). This method enables structural characterisation even of proteins that have difficulties in crystallisation. With this method, we have characterised the Schizosaccharomyces pombe Swi5-Sfr1 complex, which is expected to have a long disordered region at the N-terminal portion of Sfr1. ESI-IM-MS analysis of the Swi5-Sfr1 complex revealed that its experimental collision cross-section (CCS) had a wide distribution, and the CCS values of the most dominant ions were ∼56% of the theoretically calculated value based on the SAXS low-resolution model, suggesting a significant size reduction in the gas phase. The present study demonstrates that the newly developed method for calculation of the theoretical CCSs of the SAXS low-resolution models of proteins allows accurate evaluation of the experimental CCS values of IDPs provided by ESI-IM-MS by comparing with the low-resolution solution structures. Furthermore, it was revealed that the combination of ESI-IM-MS and SAXS is a promising method for structural characterisation of protein complexes that are unable to crystallise.","doi":"10.1039/c2an35878f","authors":"Saikusa K, Kuwabara N, Kokabu Y, Inoue Y, Sato M, Iwasaki H, Shimizu T, Ikeguchi M, Akashi S","authors_abbrev":"Saikusa K et al.","pubmed_publication_date":"07 Mar 2013","pubmed_entrez_date":"2013-01-18","publication_year":"2013","canto_session_key":"d5193a25d3e3ba9b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-11-05 12:14:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-05 12:13:31","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.03","SPBC28F2.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-11-05"},{"uniquename":"PMID:10728641","title":"Synchronization of yeast cell populations.","citation":"Methods Cell Sci 1999;21(2-3):87-93","abstract":"The study of synchronous populations of yeast cells has provided a wealth of information into regulatory aspects of the eukaryotic cell division cycle. Synchronized yeast cultures may also have potential benefit when exploiting yeasts in biotechnology. This paper provides an overview of the methods which have been used in the synchronization of cell division in budding and fission yeasts. The relative merits of these methods are outlined and protocols for preferred synchronization methods, based on size selection techniques, are described. In particular, centrifugal elutriation protocols for Saccharomyces cerevisiae (budding yeast) and Schizosaccharomyces pombe (fission yeast) are detailed as this method is regarded as one of the best ways of preparing 'unperturbed' synchronous yeast cultures for cell cycle studies.","authors":"Walker GM","authors_abbrev":"Walker GM","pubmed_publication_date":"1999","pubmed_entrez_date":"2000-03-23","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40654789","title":"A Chromosome End Without Terminal Telomere Repeats is Stable for Multiple Cell Divisions.","citation":"bioRxiv 2025 May 01;","abstract":"We have formed new short telomeres in  Schizosaccharomyces pombe  using an inducible nuclease that cuts near telomere repeats in cells that lack, cannot recruit or cannot fully activate telomerase. Sequencing these new telomeres showed that cells can divide at least 4 times with ~30 bp of non-telomeric sequence at the chromosome end in cells lacking telomerase, which contrasts with current models for the roles of terminal single-stranded telomere repeats and the telomere proteins in telomere protection and replication. Cells that cannot recruit or activate telomerase had similar results, with additional rearrangements or telomere repeat addition, respectively.","doi":"10.1101/2025.05.01.651670","authors":"Zhang H, Audry J, Runge KW","authors_abbrev":"Zhang H et al.","pubmed_publication_date":"01 May 2025","pubmed_entrez_date":"2025-07-14","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-14 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39140145","title":"Functional roles of the interaction of Moa1 with CENP-C and Rec8 in meiosis of  Schizosaccharomyces pombe .","citation":"Yi Chuan 2024 Aug;46(8):649-660","abstract":"The localization of the meiotic specific regulatory molecule Moa1 to the centromere is regulated by the kinetochore protein CENP-C, and participates in the cohesion of sister chromatids in the centromere region mediated by the cohesin Rec8. To examine the interaction of these proteins, we analyzed the interactions between Moa1 and Rec8, CENP-C by yeast two-hybrid assays and identified several amino acid residues in Moa1 required for the interaction with CENP-C and Rec8. The results revealed that the interaction between Moa1 and CENP-C is crucial for the Moa1 to participate in the regulation of monopolar attachment of sister kinetochores. However, mutation at S143 and T150 of Moa1, which are required for interaction with Rec8 in the two-hybrid assay, did not show significant defects. Mutations in amino acid residues may not be sufficient to interfere with the interaction between Moa1 and Rec8  in vivo . Further research is needed to determine the interaction domain between Moa1 and Rec8. This study revealed specific amino acid sites at which Moa1 affects the meiotic homologous chromosome segregation, providing a deeper understanding of the mechanism of meiotic chromosome segregation.","doi":"10.16288/j.yczz.24-035","authors":"Min Y, Ni ZH, Ma LL, Watanabe Y","authors_abbrev":"Min Y et al.","pubmed_publication_date":"Aug 2024","pubmed_entrez_date":"2024-08-14","publication_year":"2024","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2024-08-14 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41298081","title":"Gamete fusion triggers cytosolic functions and P-body recruitment of the RNA-binding protein Mei2 to drive fission yeast zygotic development.","citation":"Genes Dev 2025 Nov 26;","abstract":"Compartmentalized regulation of RNAs is emerging as a key driver of developmental transitions, with RNA-binding proteins performing specialized functions in different subcellular compartments. The RNA-binding protein Mei2, which arrests mitotic proliferation and drives zygotic development in fission yeast, was shown to function in the nucleus to trigger meiotic divisions. Here, using compartment-restricted alleles, we report that Mei2 functions in the cytosol to arrest mitotic growth and initiate development. We found that Mei2 is a zygote-specific component of P-bodies that inhibits the translation of tethered mRNAs. Importantly, we show that P-bodies are necessary for Mei2-driven development. Phosphorylation of Mei2 by the inhibitory Pat1 kinase impedes P-body recruitment of both Mei2 and its target RNA. Finally, we establish that Mei2 recruitment to P-bodies and its cytosolic functions, including translational repression of tethered RNAs, depend on the RNA-binding domain of Mei2 that is dispensable for nuclear Mei2 roles. Collectively, our results dissect how distinct pools of an RNA-binding protein control developmental stages and implicate P-bodies as key regulators of gamete-to-zygote transition.","doi":"10.1101/gad.353201.125","authors":"Araoyinbo A, Salat-Canela C, Vještica A","authors_abbrev":"Araoyinbo A et al.","pubmed_publication_date":"26 Nov 2025","pubmed_entrez_date":"2025-11-26","publication_year":"2025","canto_session_key":"79b3738c32e5c7ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ayokunle Araoyinbo","canto_first_approved_date":"2026-02-26 09:52:48","canto_approved_date":"2026-06-26 10:50:37","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-12-02 19:20:19","canto_added_date":"2025-11-28 00:25:04","annotation_curators":[{"name":"Ayokunle Araoyinbo","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":35,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18E5.11c","SPNCRNA.103","SPNCRNA.1715","SPAC18G6.09c","SPAC17A5.14","SPAC27D7.03c","SPAC8E11.02c","SPBC19C2.05","SPBC19G7.10c","SPBC119.04","SPBC776.09","SPAC20G4.02c"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2026-02-26"},{"uniquename":"PMID:15109393","title":"Rapid prefractionation of complex protein lysates with centrifugal membrane adsorber units improves the resolving power of 2D-PAGE-based proteome analysis.","citation":"BMC Genomics 2004 Apr 26;5(1):25","abstract":"Two-dimensional gel electrophoresis (2D-PAGE) has proven over the years to be a reliable and efficient method for separation of hundreds of proteins based on charge and mass. Nevertheless, the complexity of even the simplest proteomes limits the resolving power of 2D-PAGE. This limitation can be partially alleviated by sample prefractionation using a variety of techniques.\nHere, we have used Vivapure Ion Exchange centrifugal adsorber units to rapidly prefractionate total fission yeast protein lysate based on protein charge. Three fractions were prepared by stepwise elution with increasing sodium chloride concentrations. Each of the fractions, as well as the total lysate, were analyzed by 2D-PAGE. This simple prefractionation procedure considerably increased the resolving power of 2D-PAGE. Whereas 308 spots could be detected by analysing total protein lysate, 910 spots were observed upon prefractionation. Thorough gel image analysis demonstrated that prefractionation visualizes an additional set of 458 unique fission yeast proteins not detected in whole cell lysate.\nPrefractionation with Vivapure Q spin columns proved to be a simple, fast, reproducible, and cost-effective means of increasing the resolving power of 2D-PAGE using standard laboratory equipment.","authors":"Doud MK, Schmidt MW, Hines D, Naumann C, Kocourek A, Kashani-Poor N, Zeidler R, Wolf DA","authors_abbrev":"Doud MK et al.","pubmed_publication_date":"26 Apr 2004","pubmed_entrez_date":"2004-04-28","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25519574","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-12-20 01:16:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21901086","title":"Podbat: a novel genomic tool reveals Swr1-independent H2A.Z incorporation at gene coding sequences through epigenetic meta-analysis.","citation":"PLoS Comput Biol 2011 Aug;7(8):e1002163","abstract":"Epigenetic regulation consists of a multitude of different modifications that determine active and inactive states of chromatin. Conditions such as cell differentiation or exposure to environmental stress require concerted changes in gene expression. To interpret epigenomics data, a spectrum of different interconnected datasets is needed, ranging from the genome sequence and positions of histones, together with their modifications and variants, to the transcriptional output of genomic regions. Here we present a tool, Podbat (Positioning database and analysis tool), that incorporates data from various sources and allows detailed dissection of the entire range of chromatin modifications simultaneously. Podbat can be used to analyze, visualize, store and share epigenomics data. Among other functions, Podbat allows data-driven determination of genome regions of differential protein occupancy or RNA expression using Hidden Markov Models. Comparisons between datasets are facilitated to enable the study of the comprehensive chromatin modification system simultaneously, irrespective of data-generating technique. Any organism with a sequenced genome can be accommodated. We exemplify the power of Podbat by reanalyzing all to-date published genome-wide data for the histone variant H2A.Z in fission yeast together with other histone marks and also phenotypic response data from several sources. This meta-analysis led to the unexpected finding of H2A.Z incorporation in the coding regions of genes encoding proteins involved in the regulation of meiosis and genotoxic stress responses. This incorporation was partly independent of the H2A.Z-incorporating remodeller Swr1. We verified an Swr1-independent role for H2A.Z following genotoxic stress in vivo. Podbat is open source software freely downloadable from www.podbat.org, distributed under the GNU LGPL license. User manuals, test data and instructions are available at the website, as well as a repository for third party-developed plug-in modules. Podbat requires Java version 1.6 or higher.","doi":"10.1371/journal.pcbi.1002163","authors":"Sadeghi L, Bonilla C, Strålfors A, Ekwall K, Svensson JP","authors_abbrev":"Sadeghi L et al.","pubmed_publication_date":"Aug 2011","pubmed_entrez_date":"2011-09-09","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.10c","SPAC11E3.01c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:37052630","title":"Tfs1, transcription elongation factor TFIIS, has an impact on chromosome segregation affected by pka1 deletion in Schizosaccharomyces pombe.","citation":"Curr Genet 2023 Jun;69(2-3):115-125","abstract":"The cAMP-dependent protein kinase (PKA) pathway in Schizosaccharomyces pombe plays an important role in microtubule organization and chromosome segregation. Typically, loss of functional Pka1 induces sensitivity to the microtubule-destabilizing drug thiabendazole (TBZ) and chromosome mis-segregation. To determine the mechanism via which Pka1 is involved in these events, we explored the relevance of transcription factors by creating a double-deletion strain of pka1 and 102 individual genes encoding transcription factors. We found that rst2∆, tfs1∆, mca1∆, and moc3∆ suppressed the TBZ-sensitive phenotype of the pka1∆ strain, among which tfs1∆ was the strongest suppressor. All single mutants (rst2∆, tfs1∆, mca1∆, and moc3∆) showed a TBZ-tolerant phenotype. Tfs1 has two transcriptional domains (TFIIS and Zn finger domains), both of which contributed to the suppression of the pka1∆-induced TBZ-sensitive phenotype. pka1∆-induced chromosome mis-segregation was rescued by tfs1∆ in the presence of TBZ. tfs1 overexpression induced the TBZ-sensitive phenotype and a high frequency of chromosome mis-segregation, suggesting that the amount of Tfs1 must be strictly controlled. However, Tfs1-expression levels did not differ between the wild-type and pka1∆ strains, and the Tfs1-GFP protein was localized to the nucleus and cytoplasm in both strains, which excludes the direct regulation of expression and localization of Tfs1 by Pka1. Growth inhibition by TBZ in pka1∆ strains was notably rescued by double deletion of rst2 and tfs1 rather than single deletion of rst2 or tfs1, indicating that Rst2 and Tfs1 contribute independently to counteract TBZ toxicity. Our findings highlight Tfs1 as a key transcription factor for proper chromosome segregation.","doi":"10.1007/s00294-023-01268-0","authors":"Takenaka K, Nishioka S, Nishida Y, Kawamukai M, Matsuo Y","authors_abbrev":"Takenaka K et al.","pubmed_publication_date":"Jun 2023","pubmed_entrez_date":"2023-04-13","publication_year":"2023","canto_session_key":"06e82eaa6f509bdb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Matsuo","canto_first_approved_date":"2023-05-15 09:15:04","canto_approved_date":"2023-05-15 09:15:04","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-04-27 08:56:43","canto_added_date":"2023-04-14 00:15:04","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":9,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Yasuhiro Matsuo","community_curator":true,"annotation_count":39,"orcid":"0000-0002-2858-7179","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.02","SPCC736.08","SPAC20H4.03c","SPAC1F7.01c","SPBC19G7.16","SPAC821.07c","SPBC106.10","SPAPB1A11.04c","SPBC15D4.02","SPAC630.14c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2023-05-15"},{"uniquename":"EMBL:SPAB539","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9894912","title":"Cut5 is a component of the UV-responsive DNA damage checkpoint in fission yeast.","citation":"Mol Gen Genet 1998 Dec;260(5):426-33","abstract":"A checkpoint responding to DNA damage in G2 results in a delay in the onset of mitosis through inhibition of p34cdc2 kinase activity via maintenance of inhibitory tyrosine phosphorylation. Genetic analyses of this checkpoint in fission yeast have identified single alleles of several genes, suggesting these screens are not yet saturating, and hence further genes await identification. To fully understand the complexity of this checkpoint it will be necessary to define all the genes involved. To this end we screened for new mutants defective in the ability to delay mitosis in the presence of DNA-damaging agents. Twenty-four mutants were isolated that were defective in UV-C and MMS-induced checkpoint delay. Amongst these mutants was an allele of cut5 that was also defective in the checkpoint responses. We show here, contrary to previous reports, that the UV-C induced checkpoint response is defective in cut5 mutants. Therefore, like all other checkpoint mutants, cut5 is required for G2 checkpoint arrest following DNA damage, regardless of the nature of the lesions involved.","authors":"Verkade HM, O'Connell MJ","authors_abbrev":"Verkade HM et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1999-01-23","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.18c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:26605337","title":"An Effective Big Data Supervised Imbalanced Classification Approach for Ortholog Detection in Related Yeast Species.","citation":"Biomed Res Int 2015;2015:748681","abstract":"Orthology detection requires more effective scaling algorithms. In this paper, a set of gene pair features based on similarity measures (alignment scores, sequence length, gene membership to conserved regions, and physicochemical profiles) are combined in a supervised pairwise ortholog detection approach to improve effectiveness considering low ortholog ratios in relation to the possible pairwise comparison between two genomes. In this scenario, big data supervised classifiers managing imbalance between ortholog and nonortholog pair classes allow for an effective scaling solution built from two genomes and extended to other genome pairs. The supervised approach was compared with RBH, RSD, and OMA algorithms by using the following yeast genome pairs: Saccharomyces cerevisiae-Kluyveromyces lactis, Saccharomyces cerevisiae-Candida glabrata, and Saccharomyces cerevisiae-Schizosaccharomyces pombe as benchmark datasets. Because of the large amount of imbalanced data, the building and testing of the supervised model were only possible by using big data supervised classifiers managing imbalance. Evaluation metrics taking low ortholog ratios into account were applied. From the effectiveness perspective, MapReduce Random Oversampling combined with Spark SVM outperformed RBH, RSD, and OMA, probably because of the consideration of gene pair features beyond alignment similarities combined with the advances in big data supervised classification.","doi":"10.1155/2015/748681","authors":"Galpert D, Del Río S, Herrera F, Ancede-Gallardo E, Antunes A, Agüero-Chapin G","authors_abbrev":"Galpert D et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-11-26","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-27 01:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8144551","title":"Cloning of the pka1 gene encoding the catalytic subunit of the cAMP-dependent protein kinase in Schizosaccharomyces pombe.","citation":"J Biol Chem 1994 Apr 01;269(13):9632-7","abstract":"We have isolated Schizosaccharomyces pombe genes that confer sterility to the fission yeast cell when expressed from a multicopy plasmid. One of these genes strongly hybridized to a probe carrying the open reading frame of Saccharomyces cerevisiae TPK1, which encodes a catalytic subunit of the cAMP-dependent protein kinase (protein kinase A). This S. pombe gene, named pka1, has a coding potential of 512 amino acids, and the deduced gene product is 60% identical with the S. cerevisiae Tpk1 protein in the C-terminal 320 amino acids. Disruption of pka1 slows cell growth but is not lethal. The resultant cells, however, are highly derepressed for sexual development, readily undergoing conjugation and sporulation in the absence of nitrogen starvation. They are, thus, phenotypically indistinguishable from the adenylyl cyclase-defective (cyr1-) cells previously characterized, except that the pka1- spores are retarded in germination, whereas the cyr1- spores are not. Disruption of pka1 is epistatic to a defect in cgs1, which encodes the regulatory subunit of protein kinase A. These results strongly suggest that the product of pka1 is a catalytic subunit of protein kinase A and, furthermore, that S. pombe has only one gene encoding it. This situation contrasts with the case of S. cerevisiae, in which three genes encode the catalytic subunits.","authors":"Maeda T, Watanabe Y, Kunitomo H, Yamamoto M","authors_abbrev":"Maeda T et al.","pubmed_publication_date":"01 Apr 1994","pubmed_entrez_date":"1994-04-01","publication_year":"1994","canto_session_key":"27591db8eb4a97ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-20 14:35:33","canto_approved_date":"2026-01-31 15:55:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-24 09:08:44","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPAC31G5.11","SPBC119.11c","SPBC106.10","SPAC8C9.03"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-07-20"},{"uniquename":"GO_REF:0000060","title":"Representation of processes involved in other process in the Gene Ontology","abstract":"We have created a standard template for classes describing processes involved in other processes. The underlying equivalence axiom template is \"P and 'part_of' some W\", where P and W are biological processes.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7708725","title":"Schizosaccharomyces pombe mutants that are defective in glycoprotein galactosylation.","citation":"Proc Natl Acad Sci U S A 1995 Mar 28;92(7):2790-4","abstract":"Several mutants of Schizosaccharomyces pombe were obtained that are defective in protein glycosylation. One of the mutants, strain Sp550, makes galactomannoproteins with about half of the wild-type amount of galactose, whereas another strain, Sp137, makes glycoproteins that are almost devoid of galactose. Nondenaturing gel electrophoresis of cell extracts of both mutants revealed that they make invertases with a greatly increased mobility relative to the wild type. Additional study showed that Sp137 invertase has a subunit molecular mass that is about half that reported for the wild-type enzyme, owing to a reduction in carbohydrate content, whereas the native multimeric state appears unaltered. Structural studies on bulk cell-wall glycoprotein from Sp137 showed that the N-linked carbohydrate chains consist of a typical branched core oligosaccharide to which is attached an unsubstituted alpha 1-->6-polymannose outer chain. Consequently, the cells are agglutinated by antibodies against alpha 1-->6-linked mannose and have N-linked carbohydrate chains that are structurally analogous to the mnn2 mutant of Saccharomyces cerevisiae.","authors":"Ballou L, Ballou C","authors_abbrev":"Ballou L et al.","pubmed_publication_date":"28 Mar 1995","pubmed_entrez_date":"1995-03-28","publication_year":"1995","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25468329","title":"The value of mechanistic biophysical information for systems-level understanding of complex biological processes such as cytokinesis.","citation":"Biophys J 2014 Dec 02;107(11):2499-507","abstract":"This review illustrates the value of quantitative information including concentrations, kinetic constants and equilibrium constants in modeling and simulating complex biological processes. Although much has been learned about some biological systems without these parameter values, they greatly strengthen mechanistic accounts of dynamical systems. The analysis of muscle contraction is a classic example of the value of combining an inventory of the molecules, atomic structures of the molecules, kinetic constants for the reactions, reconstitutions with purified proteins and theoretical modeling to account for the contraction of whole muscles. A similar strategy is now being used to understand the mechanism of cytokinesis using fission yeast as a favorable model system.","doi":"10.1016/j.bpj.2014.10.031","authors":"Pollard TD","authors_abbrev":"Pollard TD","pubmed_publication_date":"02 Dec 2014","pubmed_entrez_date":"2014-12-04","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-12-05 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19443688","title":"Diverse roles of HP1 proteins in heterochromatin assembly and functions in fission yeast.","citation":"Proc Natl Acad Sci U S A 2009 Jun 02;106(22):8998-9003","abstract":"Conserved chromosomal HP1 proteins capable of binding to histone H3 methylated at lysine 9 are believed to provide a dynamic platform for the recruitment and/or spreading of various regulatory proteins involved in diverse chromosomal processes. The fission yeast Schizosaccharomyces pombe HP1 family members Chp2 and Swi6 are important for heterochromatin assembly and transcriptional silencing, but their precise roles are not fully understood. Here, we show that Swi6 and Chp2 associate with histone deacetylase (HDAC) protein complexes containing class I HDAC Clr6 and class II HDAC Clr3 (a component of Snf2/HDAC repressor complex), which are critical for transcriptional silencing of centromeric repeats targeted by the heterochromatin machinery. Mapping of RNA polymerase (Pol) II distribution in single and double mutant backgrounds revealed that Swi6 and Chp2 proteins and their associated HDAC complexes have overlapping functions in limiting Pol II occupancy across pericentromeric heterochromatin domains. The purified Swi6 fraction also contains factors involved in various chromosomal processes such as chromatin remodeling and DNA replication. Also, Swi6 copurifies with Mis4 protein, a cohesin loading factor essential for sister chromatid cohesion, and with centromere-specific histone H3 variant CENP-A, which is incorporated into chromatin in a heterochromatin-dependent manner. These analyses suggest that among other functions, HP1 proteins associate with chromatin-modifying factors that in turn cooperate to assemble repressive chromatin; thus, precluding accessibility of underlying DNA sequences to transcriptional machinery.","doi":"10.1073/pnas.0813063106","authors":"Fischer T, Cui B, Dhakshnamoorthy J, Zhou M, Rubin C, Zofall M, Veenstra TD, Grewal SI","authors_abbrev":"Fischer T et al.","pubmed_publication_date":"02 Jun 2009","pubmed_entrez_date":"2009-05-16","publication_year":"2009","canto_session_key":"d89a7babeb290b75","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-22 12:06:06","canto_approved_date":"2024-09-09 11:26:06","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-22 12:05:59","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":80,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.05c","SPCC622.09","SPCC290.02","SPAC4G9.08c","SPAC23H4.12","SPAC23C11.15","SPAC1783.05","SPBC2D10.17","SPBC660.13c","SPBC800.03","SPAC29B12.01","SPCC622.16c","SPAC1250.01","SPAC25A8.01c","SPAC1B3.17","SPBC365.10","SPAC31G5.19","SPBC839.12","SPAC10F6.08c","SPBC1A4.03c","SPAC23C4.15","SPCC1281.05","SPAC15A10.03c","SPBP35G2.10","SPAC1834.03c","SPAC21E11.03c","SPAC4H3.11c","SPBC1105.11c","SPBP23A10.13","SPAC31A2.05c","SPBC16C6.10","SPBC1D7.04","SPBC651.08c","SPBC2G5.07c","SPAC1687.01","SPBC1861.02","SPCC1682.04","SPCC188.07","SPBC1289.07c","SPBC11B10.10c","SPCC18.07","SPBC776.12c","SPBP8B7.19","SPBC1778.02","SPBC8D2.03c","SPAC1F3.07c","SPAPB1E7.03","SPCC1672.02c","SPAC664.01c","SPBC8D2.04","SPBC1105.17","SPCC622.08c","SPCC338.17c","SPAC1834.04","SPBC1105.12","SPAPB8E5.09","SPBP23A10.08","SPCC550.13","SPBC83.08","SPBC609.05","SPCC1919.14c","SPBC557.03c","SPCC330.13"],"gene_count":63,"ltp_gene_count":62,"approved_date":"2024-08-22"},{"uniquename":"PMID:29122971","title":"Poly(A) site choice and Pol2 CTD Serine-5 status govern lncRNA control of phosphate-responsive  tgp1  gene expression in fission yeast.","citation":"RNA 2018 Feb;24(2):237-250","abstract":"Expression of fission yeast glycerophosphate transporter Tgp1 is repressed in phosphate-rich medium and induced during phosphate starvation. Repression is enforced by transcription of the  nc-tgp1  locus upstream of  tgp1  to produce a long noncoding (lnc) RNA. Here we identify two essential elements of the  nc-tgp1  promoter: a TATA box  -30 TATATATA -23  and a HomolD box  -64 CAGTCACA -57 , mutations of which inactivate the  nc-tgp1  promoter and de-repress the downstream  tgp1  promoter under phosphate-replete conditions. The  nc-tgp1  lncRNA poly(A) site maps to nucleotide +1636 of the transcription unit, which coincides with the binding site for Pho7 ( 1632 TCGGACATTCAA 1643 ), the transcription factor that drives  tgp1  expression. Overlap between the lncRNA template and the  tgp1  promoter points to transcriptional interference as the simplest basis for lncRNA repression. We identify a shorter RNA derived from the  nc-tgp1  locus, polyadenylated at position +508, well upstream of the  tgp1  promoter. Mutating the  nc-tgp1-short  RNA polyadenylation signal abolishes de-repression of the downstream  tgp1  promoter elicited by Pol2 CTD Ser5Ala phospho-site mutation. Ser5 mutation favors utilization of the short RNA poly(A) site, thereby diminishing transcription of the lncRNA that interferes with the  tgp1  promoter. Mutating the  nc-tgp1-short  RNA polyadenylation signal attenuates induction of the  tgp1  promoter during phosphate starvation. Polyadenylation site choice governed by CTD Ser5 status adds a new level of lncRNA control of gene expression and reveals a new feature of the fission yeast CTD code.","doi":"10.1261/rna.063966.117","authors":"Sanchez AM, Shuman S, Schwer B","authors_abbrev":"Sanchez AM et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2017-11-11","publication_year":"2018","canto_session_key":"e720f14179755b56","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-11-12 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1271.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12463756","title":"Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe.","citation":"Biochemistry 2002 Dec 10;41(49):14560-8","abstract":"The fission yeast Pot1 (protection of telomeres) protein is a single-stranded telomeric DNA-binding protein and is required to protect the ends of chromosomes. Its N-terminal DNA-binding domain, Pot1pN, shows sequence similarity to the first OB fold of the telomere-binding protein alpha subunit of Oxytricha nova. The minimal-length telomeric ssDNA required to bind Pot1pN was determined to consist of six nucleotides, GGTTAC, by gel filtration chromatography and filter-binding assay (K(D) = 83 nM). Pot1pN is a monomer, and each monomer binds one hexanucleotide. Experiments with nucleotide substitutions demonstrated that the central four nucleotides are crucial for binding. The dependence of Pot1pN-ssDNA binding on salt concentration was consistent with a single ionic contact between the protein and the ssDNA phosphate backbone, such that at physiological salt condition 83% of the free energy of binding is nonelectrostatic. Subsequent binding experiments with longer ssDNAs indicated that Pot1pN binds to telomeric ssDNA with 3' end preference and in a highly cooperative manner that mainly results from DNA-induced protein-protein interactions. Together, the binding properties of Pot1pN suggest that the protein anchors itself at the very 3' end of a chromosome and then fills in very efficiently, coating the entire single-stranded overhang of the telomere.","authors":"Lei M, Baumann P, Cech TR","authors_abbrev":"Lei M et al.","pubmed_publication_date":"10 Dec 2002","pubmed_entrez_date":"2002-12-05","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:39940646","title":"The Ferroxidase-Permease System for Transport of Iron Across Membranes: From Yeast to Humans.","citation":"Int J Mol Sci 2025 Jan 21;26(3)","abstract":"Transport of iron across the cell membrane is a tightly controlled process carried out by specific proteins in all living cells. In yeast and in mammals, a system formed by an enzyme with ferroxidase activity coupled to a membrane transporter supports iron uptake or iron efflux, respectively. Ferroxidase belongs to the family of blue multicopper oxidases, enzymes able to couple the one-electron oxidation of substrate(s) to full reduction of molecular oxygen to water. On the other hand, the permeases are widely different and are specific to Fe 3+  and Fe 2+  in yeast and multicellular organisms, respectively. This review will describe the yeast and human ferroxidase-permease systems, highlighting similarities and differences in structure, function and regulation of the respective protein components.","doi":"10.3390/ijms26030875","authors":"Amadei M, Polticelli F, Musci G, Bonaccorsi di Patti MC","authors_abbrev":"Amadei M et al.","pubmed_publication_date":"21 Jan 2025","pubmed_entrez_date":"2025-02-13","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1683.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15316017","title":"Comparative mechanistic and substrate specificity study of inositol polyphosphate 5-phosphatase Schizosaccharomyces pombe Synaptojanin and SHIP2.","citation":"J Biol Chem 2004 Oct 22;279(43):44987-95","abstract":"Inositol-5-phosphatases are important enzymes involved in the regulation of diverse cellular processes from synaptic vesicle recycling to insulin signaling. We describe a comparative study of two representative inositol-5-phosphatases, Schizosaccharomyces pombe synaptojanin (SPsynaptojanin) and human SH2 domain-containing inositol-5-phosphatase SHIP2. We show that in addition to Mg2+, transition metals such as Mn2+, Co2+, and Ni2+ are also effective activators of SPsynaptojanin. In contrast, Ca2+ and Cu2+ are inhibitory. We provide evidence that Mg2+ binds the same site occupied by Ca2+ observed in the crystal structure of SPsynaptojanin complexed with inositol 1,4-bisphosphate (Ins(1,4)P2). Ionizations important for substrate binding and catalysis are defined for the SPsynaptojanin-catalyzed Ins(1,4,5)P3 reaction. Kinetic analysis with four phosphatidylinositol lipids bearing a 5-phosphate and 54 water-soluble inositol phosphates reveals that SP-synaptojanin and SHIP2 possess much broader substrate specificity than previously appreciated. The rank order for SPsynaptojanin is Ins(2,4,5)P3 > phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) approximately Ins(4,5)P2 approximately Ins(1,4,5)P3 approximately Ins(4,5,6)P3 > PtdIns(3,5)P2 approximately PtdIns(3,4,5)P3 approximately Ins(1,2,4,5)P4 approximately Ins(1,3,4,5)P4 approximately Ins-(2,4,5,6)P4 approximately Ins(1,2,4,5,6)P5. The rank order for SHIP2 is Ins(1,2,3,4,5)P5 > Ins(1,3,4,5)P4 > PtdIns(3,4,5)P4 approximately PtdIns(3,5)P2 approximately Ins(1,4,5,6)P4 approximately Ins(2,4,5,6)P4. Because inositol phosphate isomers elicit different biological activities, the extended substrate specificity for SPsynaptojanin and SHIP2 suggest that these enzymes likely have multiple roles in cell signaling and may regulate distinct pathways. The unique substrate specificity profiles and the importance of 2-position phosphate in binding also have important implications for the design of potent and selective SPsynaptojanin and SHIP2 inhibitors for pharmacological investigation.","authors":"Chi Y, Zhou B, Wang WQ, Chung SK, Kwon YU, Ahn YH, Chang YT, Tsujishita Y, Hurley JH, Zhang ZY","authors_abbrev":"Chi Y et al.","pubmed_publication_date":"22 Oct 2004","pubmed_entrez_date":"2004-08-19","publication_year":"2004","canto_session_key":"b91dabbdf32d8353","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-26 09:26:34","canto_approved_date":"2022-05-12 06:40:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-26 09:25:10","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2G2.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-26"},{"uniquename":"PMID:33064911","title":"Genes affecting the extension of chronological lifespan in Schizosaccharomyces pombe (fission yeast).","citation":"Mol Microbiol 2021 Apr;115(4):623-642","abstract":"So far, more than 70 genes involved in the chronological lifespan (CLS) of Schizosaccharomyces pombe (fission yeast) have been reported. In this mini-review, we arrange and summarize these genes based on the reported genetic interactions between them and the physical interactions between their products. We describe the signal transduction pathways that affect CLS in S. pombe: target of rapamycin complex 1, cAMP-dependent protein kinase, Sty1, and Pmk1 pathways have important functions in the regulation of CLS extension. Furthermore, the Php transcription complex, Ecl1 family proteins, cyclin Clg1, and the cyclin-dependent kinase Pef1 are important for the regulation of CLS extension in S. pombe. Most of the known genes involved in CLS extension are related to these pathways and genes. In this review, we focus on the individual genes regulating CLS extension in S. pombe and discuss the interactions among them.","doi":"10.1111/mmi.14627","authors":"Ohtsuka H, Shimasaki T, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2020-10-16","publication_year":"2021","canto_session_key":"d009a17ae3f45818","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2020-10-30 08:32:17","canto_approved_date":"2020-10-30 08:32:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-10-27 23:53:16","canto_added_date":"2020-10-20 00:15:06","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":5,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.07","SPBC26H8.06","SPBC26H8.13c","SPBC3F6.04c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2020-10-30"},{"uniquename":"PMID:19409973","title":"A new Schizosaccharomyces pombe chronological lifespan assay reveals that caloric restriction promotes efficient cell cycle exit and extends longevity.","citation":"Exp Gerontol 2009 Aug;44(8):493-502","abstract":"We describe a new chronological lifespan (CLS) assay for the yeast Schizosaccharomyces pombe. Yeast CLS assays monitor the loss of cell viability in a culture over time, and this new assay shows a continuous decline in viability without detectable regrowth until all cells in the culture are dead. Thus, the survival curve is not altered by the generation of mutants that can grow during the experiments, and one can monitor the entire lifespan of a strain until the number of viable cells has decreased over 10(6)-fold. This CLS assay recapitulates the evolutionarily conserved features of lifespan shortening by over nutrition, lifespan extension by caloric restriction, increased stress resistance of calorically restricted cells and lifespan control by the AKT kinases. Both S. pombe AKT kinase orthologs regulate CLS: loss of sck1(+) extended lifespan in over nutrition conditions, loss of sck2(+) extended lifespan under both normal and over nutrition conditions, and loss of both genes showed that sck1(+) and sck2(+) control different longevity pathways. The longest-lived S. pombe cells showed the most efficient cell cycle exit, demonstrating that caloric restriction links these two processes. This new S. pombe CLS assay will provide a valuable tool for aging research.","doi":"10.1016/j.exger.2009.04.004","authors":"Chen BR, Runge KW","authors_abbrev":"Chen BR et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-05-05","publication_year":"2009","canto_session_key":"ce8bad8c3e80ac94","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-01 10:08:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-01 10:02:02","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B9.02c","SPAC22E12.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-10-01"},{"uniquename":"PMID:18029449","title":"In search of an optimal ring to couple microtubule depolymerization to processive chromosome motions.","citation":"Proc Natl Acad Sci U S A 2007 Nov 27;104(48):19017-22","abstract":"Mitotic chromosome motions are driven by microtubules (MTs) and associated proteins that couple kinetochores to MT ends. A good coupler should ensure a high stability of attachment, even when the chromosome changes direction or experiences a large opposing force. The optimal coupler is also expected to be efficient in converting the energy of MT depolymerization into chromosome motility. As was shown years ago, a \"sleeve\"-based, chromosome-associated structure could, in principle, couple MT dynamics to chromosome motion. A recently identified kinetochore complex from yeast, the \"Dam1\" or \"DASH\" complex, may function as an encircling coupler in vivo. Some features of the Dam1 ring differ from those of the \"sleeve,\" but whether these differences are significant has not been examined. Here, we analyze theoretically the biomechanical properties of encircling couplers that have properties of the Dam1/DASH complex, such as its large diameter and inward-directed extensions. We demonstrate that, if the coupler is modeled as a wide ring with links that bind the MT wall, its optimal performance is achieved when the linkers are flexible and their binding to tubulin dimers is strong. The diffusive movement of such a coupler is limited, but MT depolymerization can drive its motion via a \"forced walk,\" whose features differ significantly from those of the mechanisms based on biased diffusion. Our analysis identifies key experimental parameters whose values should determine whether the Dam1/DASH ring moves via diffusion or a forced walk.","authors":"Efremov A, Grishchuk EL, McIntosh JR, Ataullakhanov FI","authors_abbrev":"Efremov A et al.","pubmed_publication_date":"27 Nov 2007","pubmed_entrez_date":"2007-11-22","publication_year":"2007","canto_session_key":"aba5c56d3616e342","canto_annotation_status":"APPROVED","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_approved_date":"2016-04-08 15:17:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-07 13:43:19","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC589.08c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2016-04-07"},{"uniquename":"PMID:25293972","title":"Increased meiotic crossovers and reduced genome stability in absence of Schizosaccharomyces pombe Rad16 (XPF).","citation":"Genetics 2014 Dec;198(4):1457-72","abstract":"Schizosaccharomyces pombe Rad16 is the ortholog of the XPF structure-specific endonuclease, which is required for nucleotide excision repair and implicated in the single strand annealing mechanism of recombination. We show that Rad16 is important for proper completion of meiosis. In its absence, cells suffer reduced spore viability and abnormal chromosome segregation with evidence for fragmentation. Recombination between homologous chromosomes is increased, while recombination within sister chromatids is reduced, suggesting that Rad16 is not required for typical homolog crossovers but influences the balance of recombination between the homolog and the sister. In vegetative cells, rad16 mutants show evidence for genome instability. Similar phenotypes are associated with mutants affecting Rhp14(XPA) but are independent of other nucleotide excision repair proteins such as Rad13(XPG). Thus, the XPF/XPA module of the nucleotide excision repair pathway is incorporated into multiple aspects of genome maintenance even in the absence of external DNA damage.","doi":"10.1534/genetics.114.171355","authors":"Mastro TL, Forsburg SL","authors_abbrev":"Mastro TL et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-10-09","publication_year":"2014","canto_session_key":"4b194d87908d8ec0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-10-10 00:16:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1734.06","SPCC338.05c","SPCC1259.13","SPAC30D11.07","SPAC17A5.11","SPCC4G3.05c","SPCC970.01","SPBC3D6.10","SPBC216.05","SPAC2G11.12","SPBC409.03","SPBC16D10.09","SPAC22F3.03c","SPCC553.07c","SPAC644.14c","SPBC16A3.11","SPAC3G6.06c","SPAC11E3.04c"],"gene_count":18,"ltp_gene_count":18},{"uniquename":"PMID:10641037","title":"A fission yeast kinesin affects Golgi membrane recycling.","citation":"Yeast 2000 Jan 30;16(2):149-66","abstract":"We report here an in vivo study of kinesin heavy chain (KHC) functions in yeast. We have identified in Schizosaccharomyces pombe a kinesin motor gene, klp3(+), which has the highest homology to the Neurospora crassa KHC. Using indirect immunofluorescence, HA epitope-tagged Klp3 protein is cytoplasmic and appears as one to a few distinct patches that are coincident with microtubules. The klp3 null allele is viable. In klp3 deleted cells, ER, Golgi and mitochondrial distribution appear normal. Mitochondrial distribution in S. pombe is known to be microtubule-associated. We show that latrunculin A does not cause mitochondria to aggregate, suggesting that mitochondrial distribution in fission yeast, unlike budding yeast, is not dependent upon actin-based processes. Neither latrunculin A nor thiabendazole affects ER or Golgi distribution. We also used the vital dye FM4-64 to visualize the internalization of the dye and its transport to vacuoles in fission yeast in the presence and absence of Klp3. We observed no significant difference between the wild-type and Klp3 null cells in either the dynamics of endocytosis or the distribution and fusion of vacuoles. The drug brefeldin A causes Golgi-to-ER recycling in wild-type fission yeast cells. Although recycling of Golgi to ER after brefeldin A treatment occurs in klp3 null cells, recycling is defective and the distribution pattern we see is different from that observed in the wild-type strain. We conclude that Klp3 plays a role in BFA-induced membrane transport. The nucleotide sequence of S. pombe klp3(+) was submitted to GenBank under Accession No. AF154055.","authors":"Brazer SC, Williams HP, Chappell TG, Cande WZ","authors_abbrev":"Brazer SC et al.","pubmed_publication_date":"30 Jan 2000","pubmed_entrez_date":"2000-01-21","publication_year":"2000","canto_session_key":"6e49b33e9e6d3a5f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-03-28 13:35:21","canto_approved_date":"2024-09-30 12:00:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-12-18 22:50:59","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A11.14c","SPAC1834.07","SPAC22A12.15c","SPAC13G6.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2022-03-28"},{"uniquename":"PMID:35783577","title":"Generation and characterization of a temperature-sensitive mutant allele of the second largest subunit of RNA polymerase I in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2022;2022","abstract":"RNA polymerase I (Pol I) is a highly conserved complex that catalyzes the transcription of rRNA precursors in the nucleolus. In this study, we isolated a temperature-sensitive (ts) allele of Rpa2, the second largest subunit of Pol I in the fission yeast  Schizosaccharomyces pombe  . We found that  rpa2   ts  cells were severely defective in growth at temperatures above 32 °C. We also found that  rpa2   ts  cells showed aberrant chromosome segregation and an abnormal ring-like nuclear structure at the restrictive temperature. These findings suggest that Rpa2 is essential for faithful nuclear division and nuclear structural organization in  S. pombe  .","doi":"10.17912/micropub.biology.000586","authors":"Ishida K, Tanaka K, Kawakami K","authors_abbrev":"Ishida K et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-07-05","publication_year":"2022","canto_session_key":"6fea8082937e4675","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kei Kawakami","canto_first_approved_date":"2022-09-30 08:52:18","canto_approved_date":"2026-01-29 17:13:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-27 12:28:01","canto_added_date":"2022-07-07 00:15:04","annotation_curators":[{"name":"Kei Kawakami","community_curator":true,"annotation_count":4,"orcid":"0000-0003-1134-7504","file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":1,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-09-30"},{"uniquename":"GO_REF:0000115","title":"Automatic Gene Ontology annotation of non-coding RNA sequences through association of Rfam records with GO terms","abstract":"Rfam (http://rfam.org, PMID:29112718) is a database of non-coding RNA families which are manually","authors":"RNAcentral (1). (1) European Bioinformatics Institute (EMBL-EBI), Hinxton, Cambridgeshire, United Kingdom","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.40","SPSNORNA.46","SPSNORNA.54","SPSNORNA.38","SPSNORNA.15","SPSNORNA.45","SPNCRNA.7474","SPSNORNA.02","SPSNORNA.13","SPSNORNA.43","SPSNORNA.39","SPSNORNA.48","SPSNORNA.41","SPRRNA.53","SPSNRNA.06","SPSNORNA.34","SPSNORNA.42","SPSNRNA.02","SPSNORNA.16","SPSNORNA.21","SPSNORNA.04","SPSNORNA.47","SPSNORNA.18","SPNCRNA.814","SPNCRNA.723","SPNCRNA.1041","SPNCRNA.1394","SPSNORNA.07","SPSNORNA.36","SPSNORNA.32","SPSNORNA.50","SPSNORNA.23","SPNCRNA.901","SPNCRNA.659","SPSNORNA.35"],"gene_count":35,"ltp_gene_count":0},{"uniquename":"PMID:3297353","title":"Identification of p34 and p13, human homologs of the cell cycle regulators of fission yeast encoded by cdc2+ and suc1+.","citation":"Cell 1987 Jul 17;50(2):319-25","abstract":"cdc2+ and CDC28 play central roles in the cell division cycles of the widely divergent yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae, respectively. The genes encode protein kinases that show 62% protein sequence identity and are capable of cross-complementation. Monoclonal antibodies were raised against p34cdc2, and a subset recognize p36cdc28. The cross-reacting antibodies detected a 34 kd homolog of the p34cdc2/p36CDC28, protein in HeLa cells. Human p34 was also recognized by an affinity-purified polyclonal anti-p34cdc2 serum. Peptide mapping of p34cdc2, p36CDC28, and human p34 revealed complete conservation of four tryptophan residues in the three proteins. p34 thus appears to be closely related to the two yeast proteins. In addition, a p34 immune complex showed protein kinase activity in vitro, and HeLa cell p34 interacts with p13, the human homolog of the suc1+ gene product of S. pombe.","authors":"Draetta G, Brizuela L, Potashkin J, Beach D","authors_abbrev":"Draetta G et al.","pubmed_publication_date":"17 Jul 1987","pubmed_entrez_date":"1987-07-17","publication_year":"1987","canto_session_key":"43d47b1d796f7bec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Jacky Hayles","canto_approved_date":"2015-08-26 09:50:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-25 14:11:51","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Jacky Hayles","community_curator":false,"annotation_count":2,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC1734.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-08-25"},{"uniquename":"PMID:7902990","title":"The Wellcome Lecture, 1992. Cell cycle control.","citation":"Philos Trans R Soc Lond B Biol Sci 1993 Sep 29;341(1298):449-54","abstract":"Genetic analysis using the fission yeast has provided a powerful methodology to investigate the eukaryotic cell cycle and its control. The onset of M-phase in fission yeast is controlled by a regulatory gene network which activates the p34cdc2 protein kinase encoded by the cdc2+ gene. The coupling of M-phase to the completion of S-phase also works through p34cdc2. A similar network is operative in vertebrate cells. Future work will focus on the controls regulating onset of S-phase and on the mechanisms by which a cell duplicates itself in space during division.","authors":"Nurse P","authors_abbrev":"Nurse P","pubmed_publication_date":"29 Sep 1993","pubmed_entrez_date":"1993-09-29","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9671458","title":"An RNA binding protein negatively controlling differentiation in fission yeast.","citation":"Mol Cell Biol 1998 Aug;18(8):4488-98","abstract":"The fission yeast Schizosaccharomyces pombe starts sexual development when starved for nutrients and simultaneously activated by mating pheromones. We have identified a new gene regulating the onset of this process. This gene, called nrd1(+), encodes a typical RNA binding protein that preferentially binds poly(U). Deletion of nrd1(+) causes cells to initiate sexual development without nutrient starvation. We have found that the biological role of nrd1(+) is to block the onset of sexual development by repressing the Ste11-regulated genes essential for conjugation and meiosis until cells reach a critical level of starvation.","authors":"Tsukahara K, Yamamoto H, Okayama H","authors_abbrev":"Tsukahara K et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-07-22","publication_year":"1998","canto_session_key":"dcb02623a1ab35b3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-02-09 23:35:33","canto_approved_date":"2026-01-31 15:53:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-20 16:28:18","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":41,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29B12.06c","SPAPB2B4.03","SPAC2F7.11","SPAC27D7.03c","SPBC106.10","SPBC409.07c","SPAC26A3.01","SPAC1296.03c","SPBC32C12.02","SPBC2D10.06","SPBC19C2.05"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2016-02-09"},{"uniquename":"InterPro:IPR005351","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18B11.08c","HGNC:30203"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15502821","title":"A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1.","citation":"Nat Cell Biol 2004 Nov;6(11):1135-41","abstract":"Defects in kinetochore proteins often lead to aneuploidy and cancer. Mis12-Mtw1 is a conserved, essential kinetochore protein family. Here, we show that a Mis12 core complex exists in Schizosaccharomyces pombe and human cells. Nine polypeptides bind to human hMis12; two of these, HEC1 and Zwint-1, are authentic kinetochore proteins. Four other human proteins of unknown function (c20orf172, DC8, PMF1 and KIAA1570) correspond to yeast Mis12-Mtw1 complex components and are shown to be required for chromosome segregation in HeLa cells using RNA interference (RNAi). Surprisingly, hMis12 also forms a stable complex with the centromeric heterochromatin components HP1alpha and HP1gamma. Double HP1 RNAi abolishes kinetochore localization of hMis12 and DC8. Therefore, centromeric HP1 may be the base to anchor the hMis12 core complex that is enriched with coiled coils and extends to outer Zwint-1 during mitosis.","authors":"Obuse C, Iwasaki O, Kiyomitsu T, Goshima G, Toyoda Y, Yanagida M","authors_abbrev":"Obuse C et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-27","publication_year":"2004","canto_session_key":"70c09a55da820950","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-01-24 11:00:15","canto_approved_date":"2023-06-08 20:50:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-22 17:07:39","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29E6.10c","SPBC409.04c","SPAC29E6.04","SPBC409.09c","SPAC1687.15","SPAC688.02c","SPCC1020.02"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-01-24"},{"uniquename":"PMID:21073853","title":"Application of a high-throughput fluorescent acetyltransferase assay to identify inhibitors of homocitrate synthase.","citation":"Anal Biochem 2011 Mar 01;410(1):133-40","abstract":"Homocitrate synthase (HCS) catalyzes the first step of l-lysine biosynthesis in fungi by condensing acetyl-coenzyme A and 2-oxoglutarate to form 3R-homocitrate and coenzyme A. Due to its conservation in pathogenic fungi, HCS has been proposed as a candidate for antifungal drug design. Here we report the development and validation of a robust fluorescent assay for HCS that is amenable to high-throughput screening for inhibitors in vitro. Using this assay, Schizosaccharomyces pombe HCS was screened against a diverse library of approximately 41,000 small molecules. Following confirmation, counter screens, and dose-response analysis, we prioritized more than 100 compounds for further in vitro and in vivo analysis. This assay can be readily adapted to screen for small molecule modulators of other acyl-CoA-dependent acyltransferases or enzymes that generate a product with a free sulfhydryl group, including histone acetyltransferases, aminoglycoside N-acetyltransferases, thioesterases, and enzymes involved in lipid metabolism.","doi":"10.1016/j.ab.2010.11.004","authors":"Bulfer SL, McQuade TJ, Larsen MJ, Trievel RC","authors_abbrev":"Bulfer SL et al.","pubmed_publication_date":"01 Mar 2011","pubmed_entrez_date":"2010-11-16","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16297994","title":"Fission yeast homologue of Tip41-like proteins regulates type 2A phosphatases and responses to nitrogen sources.","citation":"Biochim Biophys Acta 2005 Dec 15;1746(2):155-62","abstract":"A fission yeast (Schizosaccharomyces pombe) gene encoding a member of the TIP41-like protein family was identified and characterized. Deletion of the fission yeast tip41 gene leads to slower growth when ammonium chloride is the nitrogen source, but the growth rate is not affected when adenine is the nitrogen source. The tip41 mutant cells also enter the G1 phase of the cell cycle earlier than wild-type cells in response to nitrogen starvation. Overexpression of tip41(+) causes cell death, spherical cell morphology and blocks the shift to G1 phase upon nitrogen starvation. Overexpression of tip41(+) increases the activity of type 2A phosphatase. In a ppa2 deletion strain with reduced PP2A activity, overexpression of tip41(+) no longer blocks the shift to G1 upon nitrogen starvation. These results suggest that fission yeast Tip41 plays a role in cellular responses to nitrogen nutrient conditions at least partly through regulation of type 2A phosphatase activity.","authors":"Fenyvuesvolgyi C, Elder RT, Benko Z, Liang D, Zhao RY","authors_abbrev":"Fenyvuesvolgyi C et al.","pubmed_publication_date":"15 Dec 2005","pubmed_entrez_date":"2005-11-22","publication_year":"2005","canto_session_key":"87c7d481ace79172","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-04 16:40:08","canto_approved_date":"2021-03-08 19:33:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-23 18:17:48","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.16","SPBC16H5.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-07-04"},{"uniquename":"PMID:28168604","title":"The Natural Product Osthole Attenuates Yeast Growth by Extensively Suppressing the Gene Expressions of Mitochondrial Respiration Chain.","citation":"Curr Microbiol 2017 Mar;74(3):389-395","abstract":"The fast growing evidences have indicated that the natural product osthole is a promising drug candidate for fighting several serious human diseases, for example, cancer and inflammation. However, the mode-of-action (MoA) of osthole remains largely incomplete. In this study, we investigated the growth inhibition activity of osthole using fission yeast as a model, with the goal of understanding the osthole's mechanism of action, especially from the molecular level. Microarray analysis indicated that osthole has significant impacts on gene transcription levels (In total, 214 genes are up-regulated, and 97 genes are down-regulated). Gene set enrichment analysis (GSEA) indicated that 11 genes belong to the \"Respiration module\" category, especially including the components of complex III and V of mitochondrial respiration chain. Based on GSEA and network analysis, we also found that 54 up-regulated genes belong to the \"Core Environmental Stress Responses\" category, particularly including many transporter genes, which suggests that the rapidly activated nutrient exchange between cell and environment is part of the MoA of osthole. In summary, osthole can greatly impact on fission yeast transcriptome, and it primarily represses the expression levels of the genes in respiration chain, which next causes the inefficiency of ATP production and thus largely explains osthole's growth inhibition activity in Schizosaccharomyces pombe (S. pombe). The complexity of the osthole's MoA shown in previous studies and our current research demonstrates that the omics approach and bioinformatics tools should be applied together to acquire the complete landscape of osthole's growth inhibition activity.","doi":"10.1007/s00284-016-1191-9","authors":"Wang Z, Shen Y","authors_abbrev":"Wang Z et al.","pubmed_publication_date":"Mar 2017","pubmed_entrez_date":"2017-02-08","publication_year":"2017","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2017-02-10 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10683155","title":"A novel mutant allele of the chromatin-bound fission yeast checkpoint protein Rad17 separates the DNA structure checkpoints.","citation":"J Cell Sci 2000 Mar;113 ( Pt 6):1075-88","abstract":"To further dissect the genetic differences between the checkpoint pathway following S-phase cdc arrest versus DNA damage, a genetic screen was performed for checkpoint mutants that were unable to arrest mitosis following cell-cycle arrest with a temperature-sensitive DNA polymerase delta mutant, cdc20-M10. One such checkpoint mutant, rad17-d14, was found to display the cut phenotype following S-phase arrest by cdc20-M10, but not by the DNA synthesis inhibitor hydroxyurea, reminiscent of the chk1 mutant. Unlike chk1 , rad17-d14 was not sensitive to UV irradiation. Interestingly, the ionising radiation sensitivity of rad17-d14 was only at higher doses, and cells were found to be defective in properly arresting cell division following irradiation in S phase, but not G(2) phase. Biochemical analysis attributes the checkpoint defects of rad17-d14 to the failure to phosphorylate the checkpoint effector Chk1p. To investigate if Rad17p monitors the genome for abnormal DNA structures specifically during DNA synthesis, chromatin association of Rad17p was analysed. Rad17p was found to be chromatin associated throughout the cell cycle, not just during S phase. This interaction occurred irrespective of the arrest with cdc20-M10 and, surprisingly, was also independent of the other checkpoint Rad proteins, and the cell-cycle effectors Chk1p and Cds1p.","authors":"Griffiths D, Uchiyama M, Nurse P, Wang TS","authors_abbrev":"Griffiths D et al.","pubmed_publication_date":"Mar 2000","pubmed_entrez_date":"2000-02-22","publication_year":"2000","canto_session_key":"c7ee4622fd63b2da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-05-01 16:02:51","canto_approved_date":"2025-09-03 13:34:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-01 16:02:13","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPCC16A11.17","SPCC1259.13","SPCC18B5.11c","SPAC14C4.13","SPAC1952.07","SPAC27E2.05","SPAC9E9.08","SPAC20G4.04c","SPAC1F7.05","SPAC664.07c","SPBC216.05"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2015-05-01"},{"uniquename":"PMID:19357077","title":"Autoinhibition and autoactivation of the DNA replication checkpoint kinase Cds1.","citation":"J Biol Chem 2009 Jun 05;284(23):16016-27","abstract":"Cds1 is the ortholog of Chk2 and the major effector of the DNA replication checkpoint in Schizosaccharomyces pombe. Previous studies have shown that Cds1 is activated by a two-stage mechanism. In the priming stage, the sensor kinase Rad3 and the mediator Mrc1 function to phosphorylate a threonine residue, Thr(11), in the SQ/TQ domain of Cds1. In the autoactivation stage, primed Cds1 molecules dimerize via intermolecular interactions between the phosphorylated Thr(11) in one Cds1 and the forkhead-associated domain of the other. Dimerization activates Cds1, probably by promoting autophosphorylation. To define the mechanisms for the autoactivation of primed Cds1 and the regulation of this process, we carried out genetic and biochemical studies to identify phosphorylatable residues required for checkpoint activation. Our data indicate that dimerization of Cds1 promotes trans-autophosphorylation of a number of residues in the catalytic domain, but phosphorylation of a highly conserved threonine residue (Thr(328)) in the activation loop is the only covalent modification required for kinase activation in vitro and in vivo. Autophosphorylation of Thr(328) and kinase activation in unprimed, monomeric Cds1 are strongly inhibited by the C-terminal 27-amino acid tail of the enzyme. This autoinhibitory effect may play an important role in preventing spontaneous activation of the replication checkpoint during normal cell cycles. The two-stage activation pathway and the autoinhibition mechanism, which are probably shared by other members of the Chk2 family, provide sensitivity, specificity, and noise immunity, properties required for the replication checkpoint.","doi":"10.1074/jbc.M900785200","authors":"Xu YJ, Kelly TJ","authors_abbrev":"Xu YJ et al.","pubmed_publication_date":"05 Jun 2009","pubmed_entrez_date":"2009-04-10","publication_year":"2009","canto_session_key":"488ebe84ae41b570","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yongjie Xu","canto_first_approved_date":"2017-01-23 18:15:32","canto_approved_date":"2023-12-20 21:15:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-10 09:21:16","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":104,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yongjie Xu","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC18B5.03"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2017-01-23"},{"uniquename":"PMID:10954610","title":"The stress-activated MAP kinase Sty1/Spc1 and a 3'-regulatory element mediate UV-induced expression of the uvi15(+) gene at the post-transcriptional level.","citation":"Nucleic Acids Res 2000 Sep 01;28(17):3392-402","abstract":"Exposure of Schizosaccharomyces pombe cells to UV light results in increased uvi15(+) gene expression at both the mRNA and protein levels, leading to elevated cell survival. This UV-induced expression of the uvi15(+) gene was reduced in Deltasty1 and Deltawis1 cells lacking the stress-activated protein kinase pathway, but not in DNA damage checkpoint mutants. To further understand the cellular mechanisms responsible for this UV-induced expression, the transcription rate and mRNA half-life were investigated. Transcription run-on assays revealed that the rate of uvi15(+) transcription was increased 1.8-fold regardless of Sty1 when cells were UV irradiated. The half-life of uvi15(+) mRNA was also increased 1.5-fold after UV irradiation, but it was decreased in the Deltasty1 background for both basal and UV-induced mRNAs, indicating that the stress-activated MAPK cascade can mediate UV-induced gene expression by increasing mRNA half-life. Deletion analyses identified a 54 nt element downstream of the distal poly(A) site, which was involved in the increased half-life of uvi15(+) mRNA. These results suggest that both Sty1 and the 3'-regulatory element regulate UV-induced expression of the uvi15(+) gene at the post-transcriptional level.","authors":"Kim M, Lee W, Park J, Kim JB, Jang YK, Seong RH, Choe SY, Park SD","authors_abbrev":"Kim M et al.","pubmed_publication_date":"01 Sep 2000","pubmed_entrez_date":"2000-08-23","publication_year":"2000","canto_session_key":"88f605195653964e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-09-14 12:45:18","canto_approved_date":"2025-09-02 21:42:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-20 17:17:07","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC14C4.13","SPAC24B11.06c","SPAC664.07c","SPBC216.05","SPBC29B5.01","SPAC9E9.08","SPAC1783.07c","SPCC18B5.11c","SPBC649.04","SPCC1259.13","SPAC20G4.04c","SPAC1952.07"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2017-09-14"},{"uniquename":"PMID:10099785","title":"Regulation of D-glucose-6-phosphate dehydrogenase from Schizosaccharomyces pombe.","citation":"Biochem Cell Biol 1998;76(4):645-8","abstract":"D-Glucose-6-phosphate dehydrogenase is a regulatory enzyme of the oxidative pentose phosphate pathway in Schizasaccharomyces pombe. The enzyme is subject to negative cooperative regulation by D-glucose-6-phosphate as characterized by the Hill coefficient of 0.68 +/- 0.04. D-Glyceraldehyde-3-phosphate and D-ribulose-5-phosphate rectify the negative cooperativity as evidenced from a change in the Hill coefficients to 0.98 +/- 0.05 and 1.02 +/- 0.05, respectively. These pentose phosphate pathway intermediates also inhibit the enzyme competitively with respect to D-glucose-6-phosphate. Thus, D-glucose-6-phosphate dehydrogenase provides an avenue for regulating the partitioning of D-glucose between the redundant branches of the oxidative phosphate pathway in S. pombe.","authors":"Tsai CS, Chen Q","authors_abbrev":"Tsai CS et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1999-04-01","publication_year":"1998","canto_session_key":"0d88655be77c4a88","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-10-16 08:42:19","canto_approved_date":"2018-10-16 08:42:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-16 08:17:35","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.18"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-16"},{"uniquename":"PMID:31553675","title":"The phosphatase inhibitor Sds23 regulates cell division symmetry in fission yeast.","citation":"Mol Biol Cell 2019 Nov 01;30(23):2880-2889","abstract":"Animal and fungal cells divide through the assembly, anchoring, and constriction of a contractile actomyosin ring (CAR) during cytokinesis. The timing and position of the CAR must be tightly controlled to prevent defects in cell division, but many of the underlying signaling events remain unknown. The conserved heterotrimeric protein phosphatase PP2A controls the timing of events in mitosis, and upstream pathways including Greatwall-Ensa regulate PP2A activity. A role for PP2A in CAR regulation has been less clear, although loss of PP2A in yeast causes defects in cytokinesis. Here, we report that Sds23, an inhibitor of PP2A family protein phosphatases, promotes the symmetric division of fission yeast cells through spatial control of cytokinesis. We found that  sds23∆  cells divide asymmetrically due to misplaced CAR assembly, followed by sliding of the CAR away from its assembly site. These mutant cells exhibit delayed recruitment of putative CAR anchoring proteins including the glucan synthase Bgs1. Our observations likely reflect a broader role for regulation of PP2A in cell polarity and cytokinesis because  sds23∆  phenotypes were exacerbated when combined with mutations in the fission yeast Ensa homologue, Igo1. These results identify the PP2A regulatory network as a critical component in the signaling pathways coordinating cytokinesis.","doi":"10.1091/mbc.E19-05-0254","authors":"Schutt KL, Moseley JB","authors_abbrev":"Schutt KL et al.","pubmed_publication_date":"01 Nov 2019","pubmed_entrez_date":"2019-09-26","publication_year":"2019","canto_session_key":"c5dc199536ca9ad1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Katherine Schutt","canto_first_approved_date":"2020-07-24 14:19:29","canto_approved_date":"2023-06-10 06:32:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-07-21 01:46:26","canto_added_date":"2019-09-27 00:15:04","annotation_curators":[{"name":"Katherine Schutt","community_curator":true,"annotation_count":29,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB18E9.02c","SPBC646.13","SPCC794.08","SPAC24H6.05","SPBC19G7.05c","SPBC23G7.08c","SPBC11C11.02","SPAC57A10.02","SPAC2F7.03c","SPAC10F6.16","SPCC4B3.15"],"gene_count":11,"ltp_gene_count":5,"approved_date":"2020-07-24"},{"uniquename":"PMID:15099522","title":"Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe.","citation":"Mol Cell 2004 Apr 23;14(2):233-45","abstract":"Translation termination in eukaryotes is governed by two interacting release factors, eRF1 and eRF3. The crystal structure of the eEF1alpha-like region of eRF3 from S. pombe determined in three states (free protein, GDP-, and GTP-bound forms) reveals an overall structure that is similar to EF-Tu, although with quite different domain arrangements. In contrast to EF-Tu, GDP/GTP binding to eRF3c does not induce dramatic conformational changes, and Mg(2+) is not required for GDP binding to eRF3c. Mg(2+) at higher concentration accelerates GDP release, suggesting a novel mechanism for nucleotide exchange on eRF3 from that of other GTPases. Mapping sequence conservation onto the molecular surface, combined with mutagenesis analysis, identified the eRF1 binding region, and revealed an essential function for the C terminus of eRF3. The N-terminal extension, rich in acidic amino acids, blocks the proposed eRF1 binding site, potentially regulating eRF1 binding to eRF3 in a competitive manner.","authors":"Kong C, Ito K, Walsh MA, Wada M, Liu Y, Kumar S, Barford D, Nakamura Y, Song H","authors_abbrev":"Kong C et al.","pubmed_publication_date":"23 Apr 2004","pubmed_entrez_date":"2004-04-22","publication_year":"2004","canto_session_key":"e2a88aee041b259a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-18 18:21:04","canto_approved_date":"2022-11-10 18:18:12","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-09-18 18:20:52","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.01","SPCC584.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-09-18","pdb_entries":[{"pdb_id":"1r5n","gene_chains":[{"gene_uniquename":"SPCC584.04","chain":"A","position":"196-662"}],"title":"Crystal Structure Analysis of sup35 complexed with GDP","entry_authors":"Kong C,Song H","entry_authors_abbrev":"Kong C et al.","reference_uniquename":"PMID:15099522","experimental_method":"X-ray","resolution":"2.9"},{"pdb_id":"1r5o","gene_chains":[{"gene_uniquename":"SPCC584.04","chain":"A","position":"196-662"}],"title":"crystal structure analysis of sup35 complexed with GMPPNP","entry_authors":"Kong C,Song H","entry_authors_abbrev":"Kong C et al.","reference_uniquename":"PMID:15099522","experimental_method":"X-ray","resolution":"3.2"},{"pdb_id":"1r5b","gene_chains":[{"gene_uniquename":"SPCC584.04","chain":"A","position":"196-662"}],"title":"Crystal structure analysis of sup35","entry_authors":"Kong C,Song H","entry_authors_abbrev":"Kong C et al.","reference_uniquename":"PMID:15099522","experimental_method":"X-ray","resolution":"2.35"}]},{"uniquename":"PMID:21725325","title":"Coordination of DNA replication and histone modification by the Rik1-Dos2 complex.","citation":"Nature 2011 Jul 03;475(7355):244-8","abstract":"Histone modification marks have an important role in many chromatin processes. During DNA replication, both heterochromatin and euchromatin are disrupted ahead of the replication fork and are then reassembled into their original epigenetic states behind the fork. How histone marks are accurately inherited from generation to generation is still poorly understood. In fission yeast (Schizosaccharomyces pombe), RNA interference (RNAi)-mediated histone methylation is cell cycle regulated. Centromeric repeats are transiently transcribed in the S phase of the cell cycle and are processed into short interfering RNAs (siRNAs) by the complexes RITS (RNA-induced initiation of transcriptional gene silencing) and RDRC (RNA-directed RNA polymerase complex). The small RNAs together with silencing factors-including Dos1 (also known as Clr8 and Raf1), Dos2 (also known as Clr7 and Raf2), Rik1 and Lid2-promote heterochromatic methylation of histone H3 at lysine 9 (H3K9) by a histone methyltransferase, Clr4 (refs 8-13). The methylation of H3K9 provides a binding site for Swi6, a structural and functional homologue of metazoan heterochromatin protein 1 (HP1). Here we characterize a silencing complex in fission yeast that contains Dos2, Rik1, Mms19 and Cdc20 (the catalytic subunit of DNA polymerase-ε). This complex regulates RNA polymerase II (RNA Pol II) activity in heterochromatin and is required for DNA replication and heterochromatin assembly. Our findings provide a molecular link between DNA replication and histone methylation, shedding light on how epigenetic marks are transmitted during each cell cycle.","doi":"10.1038/nature10161","authors":"Li F, Martienssen R, Cande WZ","authors_abbrev":"Li F et al.","pubmed_publication_date":"03 Jul 2011","pubmed_entrez_date":"2011-07-05","publication_year":"2011","canto_session_key":"a3663cd38f1f2a12","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-11 10:40:57","canto_approved_date":"2020-04-30 08:24:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-18 10:13:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPBC28F2.12","SPCC11E10.08","SPCC970.07c","SPAC1071.02","SPCC188.13c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-10-11"},{"uniquename":"PMID:31554660","title":"Vigilin protein Vgl1 is required for heterochromatin-mediated gene silencing in  Schizosaccharomyces pombe .","citation":"J Biol Chem 2019 Nov 29;294(48):18029-18040","abstract":"Heterochromatin is a conserved feature of eukaryotic genomes and regulates various cellular processes, including gene silencing, chromosome segregation, and maintenance of genome stability. In the fission yeast  Schizosaccharomyces pombe , heterochromatin formation involves methylation of lysine 9 in histone H3 (H3K9), which recruits Swi6/HP1 proteins to heterochromatic loci. The Swi6/HP1-H3K9me3 chromatin complex lies at the center of heterochromatic macromolecular assemblies and mediates many functions of heterochromatin by recruiting a diverse set of regulators. However, additional factors may be required for proper heterochromatin organization, but they are not fully known. Here, using several molecular and biochemical approaches, we report that Vgl1, a member of a large family of multiple KH-domain proteins, collectively known as vigilins, is indispensable for the heterochromatin-mediated gene silencing in  S. pombe  ChIP analysis revealed that Vgl1 binds to pericentromeric heterochromatin in an RNA-dependent manner and that Vgl1 deletion leads to loss of H3K9 methylation and Swi6 recruitment to centromeric and telomeric heterochromatic loci. Furthermore, we show that Vgl1 interacts with the H3K9 methyltransferase, Clr4, and that loss of Vgl1 impairs Clr4 recruitment to heterochromatic regions of the genome. These findings uncover a novel role for Vgl1 as a key regulator in heterochromatin-mediated gene silencing in  S. pombe .","doi":"10.1074/jbc.RA119.009262","authors":"Farooq Z, Abdullah E, Banday S, Ganai SA, Rashid R, Mushtaq A, Rashid S, Altaf M","authors_abbrev":"Farooq Z et al.","pubmed_publication_date":"29 Nov 2019","pubmed_entrez_date":"2019-09-27","publication_year":"2019","canto_session_key":"4bb49dd30b805a0c","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-09-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21436456","title":"Clr4/Suv39 and RNA quality control factors cooperate to trigger RNAi and suppress antisense RNA.","citation":"Science 2011 Mar 25;331(6024):1624-7","abstract":"Pervasive transcription of eukaryotic genomes generates a plethora of noncoding RNAs. In fission yeast, the heterochromatin factor Clr4/Suv39 methyltransferase facilitates RNA interference (RNAi)-mediated processing of centromeric transcripts into small interfering RNAs (siRNAs). Clr4 also mediates degradation of antisense RNAs at euchromatic loci, but the underlying mechanism has remained elusive. We show that Clr4 and the RNAi effector RITS (RNA-induced transcriptional silencing) interact with Mlo3, a protein related to mRNA quality control and export factors. Loss of Clr4 impairs RITS interaction with Mlo3, which is required for centromeric siRNA production and antisense suppression. Mlo3 also interacts with the RNA surveillance factor TRAMP, which suppresses antisense RNAs targeted by Clr4 and RNAi. These findings link Clr4 to RNA quality control machinery and suggest a pathway for processing potentially deleterious RNAs through the coordinated actions of RNAi and other RNA processing activities.","doi":"10.1126/science.1198712","authors":"Zhang K, Fischer T, Porter RL, Dhakshnamoorthy J, Zofall M, Zhou M, Veenstra T, Grewal SI","authors_abbrev":"Zhang K et al.","pubmed_publication_date":"25 Mar 2011","pubmed_entrez_date":"2011-03-26","publication_year":"2011","canto_session_key":"2278d0c4da671cf5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-15 16:42:03","canto_approved_date":"2025-09-04 07:26:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-15 16:12:50","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3H7.13","SPNCRNA.2244","SPAC4F10.09c","SPAC926.08c","SPCP1E11.08","SPAC22G7.05","SPCC18.05c","SPCC1919.09","SPBC16H5.08c","SPBC16A3.08c","SPBC1D7.04","SPAC222.06","SPBC11B10.10c","SPAC1687.11","SPCC16C4.16c","SPAC17C9.03","SPAC2C4.03c","SPAC23H4.02","SPBC29A3.16","SPBC800.06","SPAC57A10.10c","SPAC4H3.07c","SPBC26H8.08c","SPBC365.04c","SPBC12C2.13c","SPCC1795.11","SPAC16C9.06c","SPCC11E10.08","SPCC18.12c","SPBC19F5.05c","SPAC4D7.05","SPBC16H5.12c","SPBC428.08c","SPBC17D11.05","SPAC16.02c","SPAC22F8.09","SPAC1952.15c","SPAC32A11.04c","SPCC1672.07","SPAC4A8.16c","SPCC1827.05c","SPAC17H9.05","SPAC16E8.06c","SPAC23G3.06","SPAC6F6.03c","SPCC126.15c","SPCC1322.10","SPBC4F6.14","SPAC17A5.14","SPCC1183.07","SPAC6F12.16c","SPBC18H10.04c","SPAC3G9.09c","SPAC26H5.10c","SPBC20F10.01","SPAC18G6.02c","SPBP8B7.16c","SPCP1E11.11","SPBC17G9.09","SPCC736.12c","SPNCRNA.5580","SPAC1093.04c","SPAC3G6.04","SPAC8F11.04","SPBC106.12c","SPCC306.07c","SPAC890.04c","SPAC1142.04","SPCC1840.03","SPCC126.11c","SPBC9B6.07","SPAC1F7.02c","SPBC354.01","SPAC227.02c","SPAC1834.04","SPAC12G12.13c","SPBC4F6.13c","SPBC651.01c","SPBP8B7.20c","SPAC10F6.08c","SPAC664.01c","SPBP35G2.08c","SPBC428.19c","SPNCRNA.5527","SPAC1486.09","SPCC1450.04"],"gene_count":86,"ltp_gene_count":82,"approved_date":"2024-01-15"},{"uniquename":"EMBL:D38180","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7934850","title":"Repair of cyclobutane pyrimidine dimers and 6-4 photoproducts in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Microbiol 1993 Nov;10(4):885-90","abstract":"We have measured repair of both of the major lesions induced by ultraviolet irradiation (cyclobutane pyrimidine dimers and 6-4 photoproducts) in wild-type Schizosaccharomyces pombe and in selected rad mutants, including mutants with deletions in genes from the main phenotypic groups. We find that rad13 delta, rad15 and rad16 delta, which are the S. pombe homologues of the excision-defective Saccharomyces cerevisiae rad2, rad3 and rad1, respectively, repair lesions somewhat more slowly than the wild type, but still have considerable repair capacity. rad2 delta, also a presumed excision-defective mutant, behaves similarly. rad8 and rad9 delta, which belong to different phenotypic groups, repair lesions at the same rate as wild-type cells. These findings provide new evidence that S. pombe has a second repair system for removing ultraviolet damage, which is absent in S. cerevisiae. Surprisingly, this second mechanism repairs lesions very efficiently; its possible nature is discussed.","authors":"McCready S, Carr AM, Lehmann AR","authors_abbrev":"McCready S et al.","pubmed_publication_date":"Nov 1993","pubmed_entrez_date":"1993-11-01","publication_year":"1993","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21760946","title":"Identification of genes affecting the toxicity of anti-cancer drug bortezomib by genome-wide screening in S. pombe.","citation":"PLoS One 2011;6(7):e22021","abstract":"Bortezomib/PS-341/Velcade, a proteasome inhibitor, is widely used to treat multiple myeloma. While several mechanisms of the cytotoxicity of the drug were proposed, the actual mechanism remains elusive. We aimed to identify genes affecting the cytotoxicity of Bortezomib in the fission yeast S. pombe as the drug inhibits this organism's cell division cycle like proteasome mutants. Among the 2815 genes screened (covering 56% of total ORFs), 19 genes, whose deletions induce strong synthetic lethality with Bortezomib, were identified. The products of the 19 genes included four ubiquitin enzymes and one nuclear proteasome factor, and 13 of them are conserved in humans. Our results will provide useful information for understanding the actions of Bortezomib within cells.","doi":"10.1371/journal.pone.0022021","authors":"Takeda K, Mori A, Yanagida M","authors_abbrev":"Takeda K et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-07-16","publication_year":"2011","canto_session_key":"b4d469fc8ee43736","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-12-20 09:47:58","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-12-19 15:43:11","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":255,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_21760946_phaf.tsv"}],"genes":["SPBC106.10","SPAC1687.05","SPBC1604.20c","SPAC3G6.13c","SPAC1B3.02c","SPBC15C4.06c","SPAC1782.05","SPBP35G2.07","SPAC1093.01","SPBC16H5.12c","SPBC1709.14","SPBC359.03c","SPCC285.10c","SPAC17A5.14","SPAC24H6.03","SPBC215.03c","SPBP23A10.14c","SPAC1610.02c","SPBC2F12.15c","SPBC28F2.11","SPBC342.01c","SPBC839.05c","SPBC31A8.01c","SPAC8F11.05c","SPAC8E11.02c","SPAC6G9.14","SPCC1281.04","SPBC12C2.02c","SPAC8F11.02c","SPAC110.02","SPBC14C8.05c","SPCC1223.04c","SPCC11E10.08","SPBC577.02","SPBP4H10.16c","SPCC4G3.08","SPAC4C5.02c","SPAC227.11c","SPAC30.02c","SPAC3G6.01","SPBC56F2.11","SPBC947.08c","SPAC17A5.16","SPCC663.01c","SPAC167.06c","SPAC3G9.01","SPAC10F6.13c","SPAC29B12.10c","SPAC959.07","SPBC16A3.03c","SPAC1805.14","SPBC4F6.06","SPBC1D7.04","SPBC13E7.03c","SPBC337.03","SPAC458.06","SPCC594.05c","SPBP8B7.09c","SPAC1952.02","SPAC4D7.10c","SPAC4F10.02","SPBC29A3.14c","SPBC1778.10c","SPBC32H8.07","SPBPJ4664.01","SPBC56F2.08c","SPAC23A1.03","SPAC22H10.02","SPBC409.20c","SPAC13G7.07","SPAC19A8.10","SPBC2F12.11c","SPAC1782.08c","SPAC1A6.09c","SPAC977.05c","SPAC6G9.01c","SPAC1142.08","SPCC16C4.20c","SPCC338.16","SPCC1739.14","SPCC4G3.04c","SPAC13G7.06","SPCC16C4.11","SPBC428.02c","SPBC30D10.04","SPBC1711.14","SPAC9.02c","SPAC31F12.01","SPCC1235.03","SPAPB1A10.03","SPCC1259.01c","SPBC25B2.08","SPCC285.09c","SPBC11C11.11c","SPCC970.07c","SPBC14F5.03c","SPAC17H9.10c","SPBC1685.05","SPAC9E9.03","SPBC409.06","SPAC23A1.11","SPBC25H2.09","SPAC6G10.12c","SPBC887.11","SPBC337.09","SPBC1718.03","SPAC4F10.04","SPBC29A3.12","SPCC1682.12c","SPBC27B12.11c","SPBC887.13c","SPAC13G6.09","SPBC24C6.05","SPBC839.03c","SPAC1F12.09","SPAC4H3.03c","SPCC584.15c","SPAC30D11.04c","SPAC959.08","SPAC977.14c","SPBC902.05c","SPAC13A11.05","SPAC343.12","SPAC513.04","SPAC1805.07c","SPBC119.06","SPBC25H2.16c","SPBC12C2.08","SPBC21H7.04","SPAC23H3.05c","SPAC22E12.03c","SPAC3C7.03c","SPAC9E9.11","SPAC20H4.07","SPBC947.02","SPCC31H12.05c","SPAC1B3.16c","SPBC1685.15c","SPCC1450.03","SPAC1F12.07","SPAC56F8.04c","SPBC3B9.11c","SPBC1D7.03","SPAC4G8.13c","SPAPB1A10.14","SPCC1259.08","SPCC1450.07c","SPAC3H5.12c","SPAC4H3.01","SPAC6G9.04","SPAC22E12.19","SPCC550.03c","SPAC922.05c","SPAC22F8.11","SPAC56E4.07","SPBC1198.09","SPBC29A3.02c","SPBP8B7.27","SPBC776.11","SPAC3H5.10","SPBC32F12.03c","SPBC32F12.07c","SPAPB1A11.04c","SPBC6B1.08c","SPBC9B6.07","SPAC3G6.07","SPBC30B4.03c","SPBC21B10.13c","SPCC24B10.06","SPCC11E10.04","SPAC227.17c","SPCC24B10.09","SPCC1739.07","SPBC31F10.02","SPBC6B1.06c","SPBC337.11","SPBC428.08c","SPAC11G7.02","SPAC3H8.08c","SPAC750.01","SPAC15A10.03c","SPBC354.03","SPCC1020.08","SPCC1739.10","SPBP8B7.28c","SPBC902.03","SPCC338.14","SPAC20H4.02","SPAC24H6.06","SPCC364.03","SPCC162.12","SPBC27.02c","SPAC23H3.13c","SPAC4F10.13c","SPBC16D10.11c","SPCC162.10","SPBC1271.05c","SPAC22A12.17c","SPBC23G7.13c","SPBC1921.07c","SPAPB1E7.02c","SPBC28F2.08c","SPAC1006.01","SPAC140.02","SPBC800.04c","SPAC11G7.04","SPBC31F10.10c","SPAC29E6.07","SPBC8E4.05c","SPCC126.04c","SPBC29A3.10c","SPAC10F6.08c","SPAC29B12.04","SPBC31E1.01c","SPBC23G7.07c","SPAC8C9.10c","SPAC2C4.16c","SPBC2D10.05","SPCC306.11","SPAC22F8.12c","SPAC513.03","SPAC13G6.10c","SPBC6B1.03c","SPAC589.10c","SPBC839.04","SPAC1805.01c","SPBC106.04","SPAC9E9.09c","SPBC13E7.11","SPAC3G6.05","SPCC1235.11","SPBC8D2.03c","SPBC530.01","SPCC1223.05c","SPAC806.05","SPAC22E12.05c","SPAC8E11.07c","SPBC11C11.09c","SPBC23E6.08","SPAC4D7.11","SPCC417.02","SPCC825.03c","SPAC19A8.04","SPAC17C9.13c","SPBC17G9.10","SPAC18G6.02c","SPBC887.17","SPBC947.06c","SPBC1861.07","SPAC6G9.03c","SPBC12D12.06","SPBC1604.08c","SPAC19A8.11c","SPBC2D10.18","SPBC725.10"],"gene_count":255,"ltp_gene_count":0,"approved_date":"2013-12-19"},{"uniquename":"PMID:16418535","title":"Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis.","citation":"J Cell Biol 2006 Jan 16;172(2):269-79","abstract":"The conserved FER-CIP4 homology (FCH) domain is found in the pombe Cdc15 homology (PCH) protein family members, including formin-binding protein 17 (FBP17). However, the amino acid sequence homology extends beyond the FCH domain. We have termed this region the extended FC (EFC) domain. We found that FBP17 coordinated membrane deformation with actin cytoskeleton reorganization during endocytosis. The EFC domains of FBP17, CIP4, and other PCH protein family members show weak homology to the Bin-amphiphysin-Rvs (BAR) domain. The EFC domains bound strongly to phosphatidylserine and phosphatidylinositol 4,5-bisphosphate and deformed the plasma membrane and liposomes into narrow tubules. Most PCH proteins possess an SH3 domain that is known to bind to dynamin and that recruited and activated neural Wiskott-Aldrich syndrome protein (N-WASP) at the plasma membrane. FBP17 and/or CIP4 contributed to the formation of the protein complex, including N-WASP and dynamin-2, in the early stage of endocytosis. Furthermore, knockdown of endogenous FBP17 and CIP4 impaired endocytosis. Our data indicate that PCH protein family members couple membrane deformation to actin cytoskeleton reorganization in various cellular processes.","authors":"Tsujita K, Suetsugu S, Sasaki N, Furutani M, Oikawa T, Takenawa T","authors_abbrev":"Tsujita K et al.","pubmed_publication_date":"16 Jan 2006","pubmed_entrez_date":"2006-01-19","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32316868","title":"Enhanced lactic acid bacteria viability with yeast coincubation under acidic conditions.","citation":"Biosci Biotechnol Biochem 2020 Aug;84(8):1706-1713","abstract":"The enhancing effects of yeasts on the viability of lactic acid bacteria (LAB) under acidic conditions were investigated.  Meyerozyma guilliermondii , coaggregative with both LAB strains under acidic conditions, significantly enhanced the viability of  Lactobacillus pentosus  and  L. paracasei  in pH 3.0 lactic acid (LA) buffer at 10°C (p < 0.05). Non-coaggregative yeasts ( Saccharomyces cerevisiae, Schizosaccharomyces pombe , and  Cyberlindnera saturnus ) also significantly enhanced the LAB viability (p < 0.05), and physical contact between LAB and yeasts was not essential for the viability-enhancing effect, indicating that the coaggregation had no relation to the enhancing mechanism. Although yeast metabolites and LA assimilation had no enhancing effect, hydrogen peroxide (H 2 O 2 ) decreased after yeast coincubation, and H 2 O 2  elimination improved  L. pentosus  viability. H 2 O 2  elimination alone did not sufficiently improve  L. paracasei  viability, but the addition of antioxidants was effective. These results suggest that the antioxidant activity of yeast increased the LAB viability under acidic conditions.","doi":"10.1080/09168451.2020.1756213","authors":"Hirai S, Kawasumi T","authors_abbrev":"Hirai S et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-04-23","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-04-24 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10949293","title":"Regulation of chromatin structure by site-specific histone H3 methyltransferases.","citation":"Nature 2000 Aug 10;406(6796):593-9","abstract":"The organization of chromatin into higher-order structures influences chromosome function and epigenetic gene regulation. Higher-order chromatin has been proposed to be nucleated by the covalent modification of histone tails and the subsequent establishment of chromosomal subdomains by non-histone modifier factors. Here we show that human SUV39H1 and murine Suv39h1--mammalian homologues of Drosophila Su(var)3-9 and of Schizosaccharomyces pombe clr4--encode histone H3-specific methyltransferases that selectively methylate lysine 9 of the amino terminus of histone H3 in vitro. We mapped the catalytic motif to the evolutionarily conserved SET domain, which requires adjacent cysteine-rich regions to confer histone methyltransferase activity. Methylation of lysine 9 interferes with phosphorylation of serine 10, but is also influenced by pre-existing modifications in the amino terminus of H3. In vivo, deregulated SUV39H1 or disrupted Suv39h activity modulate H3 serine 10 phosphorylation in native chromatin and induce aberrant mitotic divisions. Our data reveal a functional interdependence of site-specific H3 tail modifications and suggest a dynamic mechanism for the regulation of higher-order chromatin.","authors":"Rea S, Eisenhaber F, O'Carroll D, Strahl BD, Sun ZW, Schmid M, Opravil S, Mechtler K, Ponting CP, Allis CD, Jenuwein T","authors_abbrev":"Rea S et al.","pubmed_publication_date":"10 Aug 2000","pubmed_entrez_date":"2000-08-19","publication_year":"2000","canto_session_key":"06af3ce7197812c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2026-02-09 09:54:01","canto_approved_date":"2026-02-09 10:01:17","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-02-09 09:53:56","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.04","SPBC8D2.04","SPBC428.08c","SPBC1105.11c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2026-02-09"},{"uniquename":"PMID:8226998","title":"Post-translational processing of Schizosaccharomyces pombe YPT5 protein. In vitro and in vivo analysis of processing mutants.","citation":"J Biol Chem 1993 Nov 15;268(32):24467-74","abstract":"SpYPT5p is a member of the rab/YPT small GTP-binding protein family, which is believed to be involved in the regulation of intracellular trafficking. The protein sequence terminates with a CXC motif, and in our previous report (Newman, C. M. H., Giannakouros, T., Hancock, J. F., Fawell, E. H., Armstrong, J., and Magee, A. I. (1992) J. Biol. Chem. 267, 11329-11336) we have shown that SpYPT5p is prenylated both in vivo and in vitro, where geranylgeranylation was confirmed, and carboxyl-methylated. In order to dissect the role of prenylation of each cysteine, we have generated C-terminal mutants where either one or both cysteine(s) were replaced by serine and expressed them in vitro in reticulocyte lysates and in vivo in transfected COS cells. Our results suggest that both cysteines of the CXC motif are prenylated but that the rate of prenylation of the two cysteines is different. The upstream cysteine was found to be preferentially prenylated in reticulocyte lysates unless cytosol from COS cells was added. A separate activity could therefore be required for prenylation of the second cysteine, or the presence of an additional factor is needed to allow accumulation of doubly prenylated SpYPT5p. However, the modification of the upstream cysteine is not a prerequisite for the prenylation of the other. Furthermore, gene replacement in Schizosaccharomyces pombe revealed that each cysteine of the CXC motif can individually support function. Carboxyl methylation occurred only on protein which had been prenylated on the C-terminal cysteine and was required for efficient membrane binding in vitro.","authors":"Giannakouros T, Newman CM, Craighead MW, Armstrong J, Magee AI","authors_abbrev":"Giannakouros T et al.","pubmed_publication_date":"15 Nov 1993","pubmed_entrez_date":"1993-11-15","publication_year":"1993","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC6F6.15"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34309513","title":"A Brownian ratchet model for DNA loop extrusion by the cohesin complex.","citation":"Elife 2021 Jul 26;10","abstract":"The cohesin complex topologically encircles DNA to promote sister chromatid cohesion. Alternatively, cohesin extrudes DNA loops, thought to reflect chromatin domain formation. Here, we propose a structure-based model explaining both activities. ATP and DNA binding promote cohesin conformational changes that guide DNA through a kleisin N-gate into a DNA gripping state. Two HEAT-repeat DNA binding modules, associated with cohesin's heads and hinge, are now juxtaposed. Gripping state disassembly, following ATP hydrolysis, triggers unidirectional hinge module movement, which completes topological DNA entry by directing DNA through the ATPase head gate. If head gate passage fails, hinge module motion creates a Brownian ratchet that, instead, drives loop extrusion. Molecular-mechanical simulations of gripping state formation and resolution cycles recapitulate experimentally observed DNA loop extrusion characteristics. Our model extends to asymmetric and symmetric loop extrusion, as well as z-loop formation. Loop extrusion by biased Brownian motion has important implications for chromosomal cohesin function.","doi":"10.7554/eLife.67530","authors":"Higashi TL, Pobegalov G, Tang M, Molodtsov MI, Uhlmann F","authors_abbrev":"Higashi TL et al.","pubmed_publication_date":"26 Jul 2021","pubmed_entrez_date":"2021-07-26","publication_year":"2021","canto_session_key":"936cb01541f616b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-09-05 15:12:48","canto_approved_date":"2021-09-05 15:12:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-08-03 12:57:32","canto_added_date":"2021-07-28 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAC1687.18c","SPAC17H9.20","SPAC31A2.05c","SPAC10F6.09c","SPBC29A10.04"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2021-09-05"},{"uniquename":"PMID:1807836","title":"A novel method for in situ screening of yeast colonies with the beta-glucuronidase reporter gene.","citation":"Curr Genet 1991 Nov;20(5):437-9","abstract":"Expression of the beta-galactosidase gene in yeast has served as a screening marker for many purposes. Here it is shown that in two yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe, the beta-glucuronidase (GUS) gene can be used as an alternative marker. Since the histochemical substrate can not be taken up by yeast cells, direct colony screening of plates was found to be impossible. However, by a replica plating technique, GUS expression became visibly detectable within 10 min when the GUS gene was strongly expressed. The staining method could still be performed for expression at a 100-fold lower level, but incubation times of several hours were needed. Furthermore, specific GUS expression levels of yeast protein extracts could be quantified by a fluorometric assay which is both very simple to perform and highly sensitive. Since the GUS gene can also tolerate large N-terminal fusions, this method should be particularly attractive for studying such diverse problems as transcriptional and translational regulation or subcellular localization in yeast.","authors":"Hirt H","authors_abbrev":"Hirt H","pubmed_publication_date":"Nov 1991","pubmed_entrez_date":"1991-11-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10480889","title":"Transcription dependence and the roles of two excision repair pathways for UV damage in fission yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1999 Sep 17;274(38):26822-7","abstract":"Fission yeasts Schizosaccharomyces pombe possess two types of excision repair systems for UV-induced DNA damage, nucleotide excision repair (NER) and UV-damaged DNA endonuclease (UVDE)-dependent excision repair (UVER). Despite its high efficiency in damage removal, UVER defects have less effect on UV survival than NER defects. To understand the differential roles of two pathways, we examined strand-specific damage removal at the myo2 and rpb2 loci. Although NER removes cyclobutane pyrimidine dimers from the transcribed strand more rapidly than from the nontranscribed strand, UVER repairs cyclobutane pyrimidine dimers equally on both strands and at a much higher rate than NER. The low rate of damage removal from the nontranscribed strand in the absence of UVER indicates inefficient global genome repair (GGR) in this organism and a possible function of UVER as an alternative to GGR. Disruption of rhp26, the S. pombe homolog of CSB/RAD26, eliminated the strand bias of NER almost completely and resulted in a significant increase of UV sensitivity of cells in a uvdeDelta background. We suggest that the combination of transcription-coupled repair of NER and rapid UVER contributes to UV survival in growing S. pombe cells, which is accomplished by transcription-coupled repair and GGR in other organisms.","authors":"Yasuhira S, Morimyo M, Yasui A","authors_abbrev":"Yasuhira S et al.","pubmed_publication_date":"17 Sep 1999","pubmed_entrez_date":"1999-09-10","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCP25A2.02c","SPBC19C7.09c","SPBC3E7.08c","SPBC216.05"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:24173154","title":"Visualization of chromosomes in mitotically arrested cells of the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1983 Apr;7(2):123-8","abstract":"Three sets of mitotic chromosomes were observed in wild type or cdc mutants (nda3-KM311 and nda2-KM52) of the fission yeast S. pombe by the DAPI staining method. The block of microtubular functions by thiabendazole or by the mutations caused their individual appearance in mitotically arrested cells. The chromosomes have a characteristic size; the length ratio of short, medium and long ones was roughly 1:2:3, consistent with the previous genetical data (Kohli et al. 1977). Double staining with ethidium bromide and DAPI showed that the nucleolus was always associated with the shortest chromosome. Pair-like structures resembling sister chromatids were also seen.","doi":"10.1007/BF00365637","authors":"Umesono K, Hiraoka Y, Toda T, Yanagida M","authors_abbrev":"Umesono K et al.","pubmed_publication_date":"Apr 1983","pubmed_entrez_date":"2013-11-01","publication_year":"1983","canto_session_key":"0d95e09251af4ed9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-04-29 18:02:13","canto_approved_date":"2026-01-31 15:46:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 18:02:03","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPBC26H8.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-04-29"},{"uniquename":"PMID:7992507","title":"nmt2 of fission yeast: a second thiamine-repressible gene co-ordinately regulated with nmt1.","citation":"Yeast 1994 Aug;10(8):1075-82","abstract":"We previously described a screen for thiamine-repressible genes in Schizosaccharomyces pombe and reported on one such gene, nmt1, required for thiamine biosynthesis. Here we describe a second gene, nmt2, recovered in the same screen. Disruption of nmt2 also resulted in thiamine auxotrophy, indicating a role for the nmt2 gene product in thiamine biosynthesis. Both genes are highly transcribed in minimal medium and repressed in medium containing thiamine, and nuclear 'run-on' experiments confirm that expression in both cases is controlled by the rate of transcription initiation. The virtually identical kinetics of induction and repression suggest that the two genes are co-ordinately regulated. Sequence comparison of the two promoters reveals a canonical TATA box, downstream of which is a perfectly conserved 11 bp element. Transcript mapping experiments show that transcription initiation of both genes is centred on this element.","authors":"Manetti AG, Rosetto M, Maundrell KG","authors_abbrev":"Manetti AG et al.","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_session_key":"c6573f77d7263495","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-07-31 12:58:29","canto_approved_date":"2023-09-08 09:02:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 12:57:44","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:16537923","title":"Sterol regulatory element binding protein is a principal regulator of anaerobic gene expression in fission yeast.","citation":"Mol Cell Biol 2006 Apr;26(7):2817-31","abstract":"Fission yeast sterol regulatory element binding protein (SREBP), called Sre1p, functions in an oxygen-sensing pathway to allow adaptation to fluctuating oxygen concentrations. The Sre1p-Scp1p complex responds to oxygen-dependent sterol synthesis as an indirect measure of oxygen availability. To examine the role of Sre1p in anaerobic gene expression in Schizosaccharomyces pombe, we performed transcriptional profiling experiments after a shift to anaerobic conditions for 1.5 h. Of the 4,940 genes analyzed, expression levels of 521 (10.5%) and 686 (13.9%) genes were significantly increased and decreased, respectively, under anaerobic conditions. Sre1p controlled 68% of genes induced > or = 2-fold. Oxygen-requiring biosynthetic pathways for ergosterol, heme, sphingolipid, and ubiquinone were primary targets of Sre1p. Induction of glycolytic genes and repression of mitochondrial oxidative phosphorylation genes largely did not require Sre1p. Using chromatin immunoprecipitation, we demonstrated that Sre1p acts directly at target gene promoters and stimulates its own transcription under anaerobic conditions. sre1+ promoter analysis identified two DNA elements that are both necessary and sufficient for oxygen-dependent, Sre1p-dependent transcription. Interestingly, these elements are homologous to sterol regulatory elements bound by mammalian SREBP, highlighting the evolutionary conservation between Sre1p and SREBP. We conclude that Sre1p is a principal activator of anaerobic gene expression, upregulating genes required for nonrespiratory oxygen consumption.","authors":"Todd BL, Stewart EV, Burg JS, Hughes AL, Espenshade PJ","authors_abbrev":"Todd BL et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-03-16","publication_year":"2006","canto_session_key":"b2d538188151fdf1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2020-12-07 15:23:30","canto_approved_date":"2022-02-26 08:12:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-05 10:12:29","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Peter 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does the G protein, Gi2, transduce mitogenic signals?","citation":"J Cell Biochem 1994 Apr;54(4):415-22","abstract":"Serpentine receptors coupled to the heterotrimeric G protein, Gi2, are capable of stimulating DNA synthesis in a variety of cell types. A common feature of the Gi2-coupled stimulation of DNA synthesis is the activation of the mitogen-activated protein kinases (MAPKs). The regulation of MAPK activation by the Gi2-coupled thrombin and acetylcholine muscarinic M2 receptors occurs by a sequential activation of a network of protein kinases. The MAPK kinase (MEK) which phosphorylates and activates MAPK is also activated by phosphorylation. MEK is phosphorylated and activated by either Raf or MEK kinase (MEKK). Thus, Raf and MEKK converge at MEK to regulate MAPK. Gi2-coupled receptors are capable of activating MEK and MAPK by Raf-dependent and Raf-independent mechanisms. Pertussis toxin catalyzed ADP-ribosylation of alpha i2 inhibits both the Raf-dependent and -independent pathways activated by Gi2-coupled receptors. The Raf-dependent pathway involves Ras activation, while the Raf-independent activation of MEK and MAPK does not involve Ras. The Raf-independent activation of MEK and MAPK most likely involves the activation of MEKK. The vertebrate MEKK is homologous to the Ste11 and Byr2 protein kinases in the yeast Saccharomyces cerevisiae and Schizosaccharomyces pombe, respectively. The yeast Ste11 and Byr2 protein kinases are involved in signal transduction cascades initiated by pheromone receptors having a 7 membrane spanning serpentine structure coupled to G proteins. MEKK appears to be conserved in the regulation of G protein-coupled signal pathways in yeast and vertebrates. Raf represents a divergence in vertebrates from the yeast pheromone-responsive protein kinase system.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Johnson GL, Gardner AM, Lange-Carter C, Qian NX, Russell M, Winitz S","authors_abbrev":"Johnson GL et al.","pubmed_publication_date":"Apr 1994","pubmed_entrez_date":"1994-04-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32783879","title":"Modeling the Control of Meiotic Cell Divisions: Entry, Progression, and Exit.","citation":"Biophys J 2020 Sep 01;119(5):1015-1024","abstract":"Upon nitrogen starvation, Schizosaccharomyces pombe exit the mitotic cell cycle and become irreversibly committed to the completion of meiosis program. Meiotic cell divisions are coordinated with sporulation events to produce haploid spores. In the last few decades, experiments on fission yeast have revealed different molecular players involved in two meiotic cell divisions, meiosis I (MI) and meiosis II (MII). How the MI entry, MI-to-MII transition, and MII exit occur because of the dynamics of the regulatory network is not well understood. In this work, we developed a comprehensive mathematical model of the network that describes the temporal dynamics of meiotic progression. The model accounts for the phenotypes of several experimental data (single and multiple mutations). We demonstrate the control strategy involving multiple feedback loops to yield two successive division cycles. The differential regulation of anaphase-promoting complex/cyclosome (APC/C) coactivators and its inhibitors is crucial for the dynamics of both MI-to-MII transition and MII exit. This model generates mechanistic insights that help in further experiments and modeling.","doi":"10.1016/j.bpj.2020.07.017","authors":"Dangarh P, Pandey N, Vinod PK","authors_abbrev":"Dangarh P et al.","pubmed_publication_date":"01 Sep 2020","pubmed_entrez_date":"2020-08-14","publication_year":"2020","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2020-08-15 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009244","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD129","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26275777","title":"Functional interaction of Rpb1 and Spt5 C-terminal domains in co-transcriptional histone modification.","citation":"Nucleic Acids Res 2015 Nov 16;43(20):9766-75","abstract":"Transcription by RNA polymerase II (RNAPII) is accompanied by a conserved pattern of histone modifications that plays important roles in regulating gene expression. The establishment of this pattern requires phosphorylation of both Rpb1 (the largest RNAPII subunit) and the elongation factor Spt5 on their respective C-terminal domains (CTDs). Here we interrogated the roles of individual Rpb1 and Spt5 CTD phospho-sites in directing co-transcriptional histone modifications in the fission yeast Schizosaccharomyces pombe. Steady-state levels of methylation at histone H3 lysines 4 (H3K4me) and 36 (H3K36me) were sensitive to multiple mutations of the Rpb1 CTD repeat motif (Y1S2P3T4S5P6S7). Ablation of the Spt5 CTD phospho-site Thr1 reduced H3K4me levels but had minimal effects on H3K36me. Nonetheless, Spt5 CTD mutations potentiated the effects of Rpb1 CTD mutations on H3K36me, suggesting overlapping functions. Phosphorylation of Rpb1 Ser2 by the Cdk12 orthologue Lsk1 positively regulated H3K36me but negatively regulated H3K4me. H3K36me and histone H2B monoubiquitylation required Rpb1 Ser5 but were maintained upon inactivation of Mcs6/Cdk7, the major kinase for Rpb1 Ser5 in vivo, implicating another Ser5 kinase in these regulatory pathways. Our results elaborate the CTD 'code' for co-transcriptional histone modifications.","doi":"10.1093/nar/gkv837","authors":"Mbogning J, Pagé V, Burston J, Schwenger E, Fisher RP, Schwer B, Shuman S, Tanny JC","authors_abbrev":"Mbogning J et al.","pubmed_publication_date":"16 Nov 2015","pubmed_entrez_date":"2015-08-16","publication_year":"2015","canto_session_key":"3741edebdad0c9cf","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-17 00:18:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPBC19F8.07","SPBC32H8.10","SPAC2F3.15"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:21866258","title":"\"Chromosome kissing\" and modulation of replication termination.","citation":"Bioarchitecture 2011 Jan;1(1):24-28","abstract":"Previously, inter-chromosomal interactions called \"chromosome kissing\" have been reported to control tissue-specific transcription and cell fate determination. Using the fission yeast as a model system we have shown that physiologically programmed replication termination is also modulated by chromosome kissing. The published report reviewed here shows that a myb-like replication terminator protein Reb1 of S. pombe and its cognate binding sites (Ter) are involved in chromosome kissing that promotes a cooperative mechanism of replication termination. We also suggest that at least one other replication terminator protein namely Sap1, which is also an origin binding protein, is likely to be involved in a similar mechanism of control not only of fork arrest but also of replication initiation and in possible ori-Ter interaction. We discuss the roles of chromatin remodeling and other proteins in this novel mechanism of replication control.","authors":"Bastia D, Singh SK","authors_abbrev":"Bastia D et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2011-08-26","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26446992","title":"Chromatin association of the SMC5/6 complex is dependent on binding of its NSE3 subunit to DNA.","citation":"Nucleic Acids Res 2016 Feb 18;44(3):1064-79","abstract":"SMC5/6 is a highly conserved protein complex related to cohesin and condensin, which are the key components of higher-order chromatin structures. The SMC5/6 complex is essential for proliferation in yeast and is involved in replication fork stability and processing. However, the precise mechanism of action of SMC5/6 is not known. Here we present evidence that the NSE1/NSE3/NSE4 sub-complex of SMC5/6 binds to double-stranded DNA without any preference for DNA-replication/recombination intermediates. Mutations of key basic residues within the NSE1/NSE3/NSE4 DNA-binding surface reduce binding to DNA in vitro. Their introduction into the Schizosaccharomyces pombe genome results in cell death or hypersensitivity to DNA damaging agents. Chromatin immunoprecipitation analysis of the hypomorphic nse3 DNA-binding mutant shows a reduced association of fission yeast SMC5/6 with chromatin. Based on our results, we propose a model for loading of the SMC5/6 complex onto the chromatin.","doi":"10.1093/nar/gkv1021","authors":"Zabrady K, Adamus M, Vondrova L, Liao C, Skoupilova H, Novakova M, Jurcisinova L, Alt A, Oliver AW, Lehmann AR, Palecek JJ","authors_abbrev":"Zabrady K et al.","pubmed_publication_date":"18 Feb 2016","pubmed_entrez_date":"2015-10-09","publication_year":"2016","canto_session_key":"05d874b97fecccf7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-12-09 05:53:54","canto_approved_date":"2024-03-13 09:37:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-01 17:26:22","canto_added_date":"2015-10-10 00:18:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPCC550.05","SPBC20F10.04c","SPCC5E4.06","SPCC645.04","SPBC582.05c","SPAC14C4.02c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2016-12-09"},{"uniquename":"PMID:9102632","title":"Functional analysis of the fission yeast Prp4 protein kinase involved in pre-mRNA splicing and isolation of a putative mammalian homologue.","citation":"Nucleic Acids Res 1997 Mar 01;25(5):1028-35","abstract":"The prp4 gene of Schizosaccharomyces pombe encodes a protein kinase. A physiological substrate is not yet known. A mutational analysis of prp4 revealed that the protein consists of a short N-terminal domain, containing several essential motifs, which is followed by the kinase catalytic domain comprising the C-terminus of the protein. Overexpression of N-terminal mutations disturbs mitosis and produces elongated cells, Using a PCR approach, we isolated a putative homologue of Prp4 from human and mouse cells. The mammalian kinase domain is 53% identical to the kinase domain of Prp4. The short N-terminal domains share <20% identical amino acids, but contain conserved motifs. A fusion protein consisting of the N-terminal region from S. pombe followed by the mammalian kinase domain complements a temperature-sensitive prp4 mutation of S. pombe. Prp4 and the recombinant yeast/mouse protein kinase phosphorylate the human SR splicing factor ASF/SF2 in vitro in its RS domain.","authors":"Gross T, Lützelberger M, Weigmann H, Klingenhoff A, Shenoy S, Käufer NF","authors_abbrev":"Gross T et al.","pubmed_publication_date":"01 Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_session_key":"fa5b7731c210afc9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-01 06:44:40","canto_approved_date":"2022-03-14 08:37:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-25 16:48:31","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-06-01"},{"uniquename":"PMID:24936793","title":"Fusion of protein aggregates facilitates asymmetric damage segregation.","citation":"PLoS Biol 2014 Jun;12(6):e1001886","abstract":"Asymmetric segregation of damaged proteins at cell division generates a cell that retains damage and a clean cell that supports population survival. In cells that divide asymmetrically, such as Saccharomyces cerevisiae, segregation of damaged proteins is achieved by retention and active transport. We have previously shown that in the symmetrically dividing Schizosaccharomyces pombe there is a transition between symmetric and asymmetric segregation of damaged proteins. Yet how this transition and generation of damage-free cells are achieved remained unknown. Here, by combining in vivo imaging of Hsp104-associated aggregates, a form of damage, with mathematical modeling, we find that fusion of protein aggregates facilitates asymmetric segregation. Our model predicts that, after stress, the increased number of aggregates fuse into a single large unit, which is inherited asymmetrically by one daughter cell, whereas the other one is born clean. We experimentally confirmed that fusion increases segregation asymmetry, for a range of stresses, and identified Hsp16 as a fusion factor. Our work shows that fusion of protein aggregates promotes the formation of damage-free cells. Fusion of cellular factors may represent a general mechanism for their asymmetric segregation at division.","doi":"10.1371/journal.pbio.1001886","authors":"Coelho M, Lade SJ, Alberti S, Gross T, Tolić IM","authors_abbrev":"Coelho M et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-06-18","publication_year":"2014","canto_session_key":"24045a664a77f653","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-12-18 17:08:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-12-18 17:07:30","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.02c","SPBC16D10.08c","SPAC10F6.03c","SPAC23H4.06","SPAC13G7.02c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-12-18"},{"uniquename":"PMID:36568394","title":" Schizosaccharomyces pombe  Grx4, Fep1, and Php4:  In silico  analysis and expression response to different iron concentrations.","citation":"Front Genet 2022;13:1069068","abstract":"Due to iron's essential role in cellular metabolism, most organisms must maintain their homeostasis. In this regard, the fission yeast  Schizosaccharomyces pombe  (sp) uses two transcription factors to regulate intracellular iron levels: spFep1 under iron-rich conditions and spPhp4 under iron-deficient conditions, which are controlled by spGrx4. However, bioinformatics analysis to understand the role of the spGrx4/spFep1/spPhp4 axis in maintaining iron homeostasis in  S. pombe  is still lacking. Our study aimed to perform bioinformatics analysis on  S. pombe  proteins and their sequence homologs in  Aspergillus flavus  (af),  Saccharomyces cerevisiae  (sc), and  Homo sapiens  (hs) to understand the role of spGrx4, spFep1, and spPhp4 in maintaining iron homeostasis. The three genes' expression patterns were also examined at various iron concentrations. A multiple sequence alignment analysis of spGrx4 and its sequence homologs revealed a conserved cysteine residue in each PF00085 domain. Blast results showed that hsGLRX3 is most similar to spGrx4. In addition, spFep1 is most closely related in sequence to scDal80, whereas scHap4 is most similar to spFep1. We also found two highly conserved motifs in spFep1 and its sequence homologs that are significant for iron transport systems because they contain residues involved in iron homeostasis. The scHap4 is most similar to spPhp4. Using STRING to analyze protein-protein interactions, we found that spGrx4 interacts strongly with spPhp4 and spFep1. Furthermore, spGrx4, spPhp4, and spFep1 interact with spPhp2, spPhp3, and spPhp5, indicating that the three proteins play cooperative roles in iron homeostasis. At the highest level of Fe,  spgrx4  had the highest expression, followed by  spfep1 , while  spphp4  had the lowest expression; a contrast occurred at the lowest level of Fe, where  spgrx4  expression remained constant. Our findings support the notion that organisms develop diverse strategies to maintain iron homeostasis.","doi":"10.3389/fgene.2022.1069068","authors":"Ebrahim A, Alfwuaires MA, Abukhalil MH, Alasmari F, Ahmad F, Yao R, Luo Y, Huang Y","authors_abbrev":"Ebrahim A et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-12-26","publication_year":"2022","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2022-12-27 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23E2.01","SPBC16E9.01c","SPBC26H8.06"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:15809069","title":"Characterization of O-mannosyltransferase family in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2005 May 13;330(3):813-20","abstract":"Protein O-glycosylation is an essential protein modification in eukaryotic cells. In Saccharomyces cerevisiae, O-mannosylation is initiated in the lumen of the endoplasmic reticulum by O-mannosyltransferase gene products (Pmt1p-7p). A search of the Schizosaccharomyces pombe genome database revealed a total of three O-glycoside mannosyltransferase homologs (ogm1+, ogm2+, and ogm4+), closely related to Saccharomyces cerevisiae PMT1, PMT2, and PMT4. Although individual ogm genes were not found to be essential, ogm1Delta and ogm4Delta mutants exhibited aberrant morphology and failed to agglutinate during mating. The phenotypes of the ogm4Delta mutant were not complemented by overexpression of ogm1+ or ogm2+, suggesting that each of the Ogm proteins does not have overlapping functions. Heterologous expression of a chitinase from S. cerevisiae in the ogm mutants revealed that O-glycosylation of chitinase had decreased in ogm1Delta cells. A GFP-tagged Fus1p from S. cerevisiae was specifically not glycosylated and accumulated in the Golgi in ogm4Delta cells. These results indicate that O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins in S. pombe.","authors":"Tanaka N, Fujita Y, Suzuki S, Morishita M, Giga-Hama Y, Shimoda C, Takegawa K","authors_abbrev":"Tanaka N et al.","pubmed_publication_date":"13 May 2005","pubmed_entrez_date":"2005-04-06","publication_year":"2005","canto_session_key":"4ac217676e2be734","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-05-19 12:58:20","canto_approved_date":"2024-06-20 11:25:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-19 12:58:12","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1E7.09","SPBC16C6.09","SPAC22A12.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-05-19"},{"uniquename":"PMID:21653323","title":"ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria.","citation":"Blood 2011 Aug 11;118(6):1443-51","abstract":"Mutations in the uroporphyrinogen III synthase (UROS) gene cause congenital erythropoietic porphyria (CEP), an autosomal-recessive inborn error of erythroid heme biosynthesis. Clinical features of CEP include dermatologic and hematologic abnormalities of variable severity. The discovery of a new type of erythroid porphyria, X-linked dominant protoporphyria (XLDPP), which results from increased activity of 5-aminolevulinate synthase 2 (ALAS2), the rate-controlling enzyme of erythroid heme synthesis, led us to hypothesize that the CEP phenotype may be modulated by sequence variations in the ALAS2 gene. We genotyped ALAS2 in 4 unrelated CEP patients exhibiting the same C73R/P248Q UROS genotype. The most severe of the CEP patients, a young girl, proved to be heterozygous for a novel ALAS2 mutation: c.1757 A > T in exon 11. This mutation is predicted to affect the highly conserved and penultimate C-terminal amino acid of ALAS2 (Y586). The rate of 5-aminolevulinate release from Y586F was significantly increased over that of wild-type ALAS2. The contribution of the ALAS2 gain-of-function mutation to the CEP phenotype underscores the importance of modifier genes underlying CEP. We propose that ALAS2 gene mutations should be considered not only as causative of X-linked sideroblastic anemia (XLSA) and XLDPP but may also modulate gene function in other erythropoietic disorders.","doi":"10.1182/blood-2011-03-342873","authors":"To-Figueras J, Ducamp S, Clayton J, Badenas C, Delaby C, Ged C, Lyoumi S, Gouya L, de Verneuil H, Beaumont C, Ferreira GC, Deybach JC, Herrero C, Puy H","authors_abbrev":"To-Figueras J et al.","pubmed_publication_date":"11 Aug 2011","pubmed_entrez_date":"2011-06-10","publication_year":"2011","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F3.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10394366","title":"The crystal structure of rna1p: a new fold for a GTPase-activating protein.","citation":"Mol Cell 1999 Jun;3(6):781-91","abstract":"rna1p is the Schizosaccharomyces pombe ortholog of the mammalian GTPase-activating protein (GAP) of Ran. Both proteins are essential for nuclear transport. Here, we report the crystal structure of rna1p at 2.66 A resolution. It contains 11 leucine-rich repeats that adopt the nonglobular shape of a crescent, bearing no resemblance to RhoGAP or RasGAP. The invariant residues of RanGAP form a contiguous surface, strongly indicating the Ran-binding interface. Alanine mutations identify Arg-74 as a critical residue for GTP hydrolysis. In contrast to RasGAP and RhoGAP, Arg-74 could be substituted by lysine and contributed significantly to the binding of Ran. Therefore, we suggest a GAP mechanism for rna1p, which constitutes a variation of the arginine finger mechanism found for Ras GAP and RhoGAP.","authors":"Hillig RC, Renault L, Vetter IR, Drell T, Wittinghofer A, Becker J","authors_abbrev":"Hillig RC et al.","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-07-08","publication_year":"1999","canto_session_key":"7fc130918b3b18ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-02-13 15:04:09","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-03 15:46:20","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.07","SPBC1289.03c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-09-03","pdb_entries":[{"pdb_id":"1yrg","gene_chains":[{"gene_uniquename":"SPAC22E12.07","chain":"A/B","position":"2-386"}],"title":"THE CRYSTAL STRUCTURE OF RNA1P: A NEW FOLD FOR A GTPASE-ACTIVATING PROTEIN","entry_authors":"Hillig RC,Renault L,Vetter IR,Drell T,Wittinghofer A,Becker J","entry_authors_abbrev":"Hillig RC et al.","reference_uniquename":"PMID:10394366","experimental_method":"X-ray","resolution":"2.66"}]},{"uniquename":"PMID:8887553","title":"The fission yeast Cdc1 protein, a homologue of the small subunit of DNA polymerase delta, binds to Pol3 and Cdc27.","citation":"EMBO J 1996 Sep 02;15(17):4613-28","abstract":"cdc1+ is required for cell cycle progression in Schizosaccharomyces pombe. Cells carrying temperature-sensitive cdc1 mutants undergo cell cycle arrest when shifted to the restrictive temperature, becoming highly elongated. Here we describe the cloning and sequencing of cdc1+, which is shown to encode a 462 residue protein that displays significant sequence similarity to the small subunit of mammalian DNA polymerase delta. cdc1+ interacts genetically with pol3+, which encodes the large subunit of DNA polymerase delta in fission yeast, and the Cdc1 protein binds to Pol3 in vitro, strongly suggesting that Cdc1 is likely to be the small subunit of Pol delta. In addition, we show that cdc1+ overexpression is sufficient to rescue cells carrying temperature-sensitive cdc27 alleles and that the Cdc1 and Cdc27 proteins interact in vivo and in vitro. Deletion of either cdc1+ or cdc27+ results in cell cycle arrest with the arrested cells having a single nucleus with 2C DNA content. No evidence was obtained for a cut phenotype, indicating that neither cdc1+ nor cdc27+ is required for checkpoint function. cdc1 mutant cells are supersensitive to the DNA synthesis inhibitor hydroxyurea and to the DNA damaging agent MMS, display increased frequency of mini-chromosome loss and have an extended S phase.","authors":"MacNeill SA, Moreno S, Reynolds N, Nurse P, Fantes PA","authors_abbrev":"MacNeill SA et al.","pubmed_publication_date":"02 Sep 1996","pubmed_entrez_date":"1996-09-02","publication_year":"1996","canto_session_key":"c5bcc1ff40b42c22","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-15 11:19:12","canto_approved_date":"2024-04-04 15:18:35","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-02-14 15:55:23","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.02c","SPAC27E2.05","SPBC1734.02c","SPBC336.04"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-04-15"},{"uniquename":"PMID:26168240","title":"Quantitative Fitness Analysis Identifies exo1∆ and Other Suppressors or Enhancers of Telomere Defects in Schizosaccharomyces pombe.","citation":"PLoS One 2015;10(7):e0132240","abstract":"Synthetic genetic array (SGA) has been successfully used to identify genetic interactions in S. cerevisiae and S. pombe. In S. pombe, SGA methods use either cycloheximide (C) or heat shock (HS) to select double mutants before measuring colony size as a surrogate for fitness. Quantitative Fitness Analysis (QFA) is a different method for determining fitness of microbial strains. In QFA, liquid cultures are spotted onto solid agar and growth curves determined for each spot by photography and model fitting. Here, we compared the two S. pombe SGA methods and found that the HS method was more reproducible for us. We also developed a QFA procedure for S. pombe. We used QFA to identify genetic interactions affecting two temperature sensitive, telomere associated query mutations (taz1Δ and pot1-1). We identify exo1∆ and other gene deletions as suppressors or enhancers of S. pombe telomere defects. Our study identifies known and novel gene deletions affecting the fitness of strains with telomere defects. The interactions we identify may be relevant in human cells.","doi":"10.1371/journal.pone.0132240","authors":"Narayanan S, Dubarry M, Lawless C, Banks AP, Wilkinson DJ, Whitehall SK, Lydall D","authors_abbrev":"Narayanan S et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-07-14","publication_year":"2015","canto_session_key":"c307c99f0ab4c96e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-07-16 00:20:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30969896","title":"Microtubule polymerase and processive plus-end tracking functions originate from distinct features within TOG domain arrays.","citation":"Mol Biol Cell 2019 Jun 01;30(12):1490-1504","abstract":"XMAP215/Stu2/Alp14 accelerates tubulin polymerization while processively tracking microtubule (MT) plus ends via tumor overexpressed gene (TOG) domain arrays. It remains poorly understood how these functions arise from tubulin recruitment, mediated by the distinct TOG1 and TOG2 domains, or the assembly of these arrays into large square complexes. Here, we describe a relationship between MT plus-end tracking and polymerase functions revealing their distinct origin within TOG arrays. We study Alp14 mutants designed based on structural models, with defects in either tubulin recruitment or self-organization. Using in vivo live imaging in fission yeast and in vitro MT dynamics assays, we show that tubulins recruited by TOG1 and TOG2 serve concerted, yet distinct, roles in MT plus-end tracking and polymerase functions. TOG1 is critical for processive plus-end tracking, whereas TOG2 is critical for accelerating tubulin polymerization. Inactivating interfaces that stabilize square complexes lead to defects in both processive MT plus-end tracking and polymerase. Our studies suggest that a dynamic cycle between square and unfurled TOG array states gives rise to processive polymerase activity at MT plus ends.","doi":"10.1091/mbc.E19-02-0093","authors":"Cook BD, Chang F, Flor-Parra I, Al-Bassam J","authors_abbrev":"Cook BD et al.","pubmed_publication_date":"01 Jun 2019","pubmed_entrez_date":"2019-04-11","publication_year":"2019","canto_session_key":"1d1dc27a44d1cf55","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-04-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22549465","title":"New romance between RNA degradation pathways: Mmi1 and RNAi meet on heterochromatic islands.","citation":"EMBO J 2012 May 16;31(10):2242-3","abstract":"EMBO J 31 10, 2296–2308 (2012); published online April 20 2012 Meiosis is one of the most dramatic differentiation programmes a cell can undertake, since it leads to an irreversible reduction of the cell’s genetic content. It therefore comes as no surprise that meiosis should be tightly regulated. In this issue Hiriart et al (2012) identify a new layer of regulation in which the RNA interference (RNAi) pathway dampens the expression of meiotic genes during vegetative growth in fission yeast. Their study converges with a recent publication by Zofall et al (2012) to reveal how components of the RNAi pathway, the Mmi1 RNA elimination system and chromatin modifications contribute to the maintenance of the vegetative state until a decision is made to enter meiosis.","doi":"10.1038/emboj.2012.138","authors":"Holm LR, Thon G","authors_abbrev":"Holm LR et al.","pubmed_publication_date":"16 May 2012","pubmed_entrez_date":"2012-05-03","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22542487","title":"Characterization of bifunctional sphingolipid Δ4-desaturases/C4-hydroxylases of trypanosomatids by liquid chromatography-electrospray tandem mass spectrometry.","citation":"Mol Biochem Parasitol 2012 Jul;184(1):29-38","abstract":"Six genes encoding putative sphingolipid desaturases have been identified in trypanosomatid genomes: one in Trypanosoma brucei (TbSLdes protein), one in Trypanosoma cruzi (TcSLdes) and four in Leishmania major (LmSLdes1-4), tandemly arrayed on chromosome 26. The six amino acid sequences showed the three characteristic histidine boxes, with a long spacer between the first and second box, as in fungal desaturases and bifunctional desaturases/hydroxylases, to which they are phylogenetically related. We functionally characterized the trypanosomatid enzymes by their expression in Saccharomyces cerevisiae sur2Δ mutant, which lacks C4-hydroxylase activity. The sphingoid base profile (dinitrophenyl derivatives) of each yeast mutant transformed with each one of the different parasite genes was analyzed by HPLC, using a sur2Δ mutant expressing the Schyzosaccharomyces pombe sphingolipid desaturase (SpSLdes) as positive control. TbSLdes was capable of desaturating endogenous sphingolipids at levels comparable to those found in SpSLdes. By contrast, L. major and T. cruzi enzymes showed either no or negligible activities. Using the HPLC system coupled to electrospray tandem quadrupole/time of flight mass spectrometry we were able to detect significant levels of desaturated and hydroxylated sphingoid bases in extracts of all transformed yeast mutants, except for those transformed with the empty vector. These results indicate that S. pombe, T. brucei, T. cruzi and L. major enzymes are all bifunctional. Using the same methodology, desaturated and hydroxylated sphingoid bases were detected in T. cruzi epimastigotes and L. major promastigote cells, as described previously, and in T. brucei procyclic and bloodstream forms for the first time.","doi":"10.1016/j.molbiopara.2012.04.005","authors":"Vacchina P, Tripodi KE, Escalante AM, Uttaro AD","authors_abbrev":"Vacchina P et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-05-01","publication_year":"2012","canto_session_key":"c953dccdaa5bc8bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-06-28 05:04:25","canto_approved_date":"2025-02-21 23:44:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-27 18:10:35","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.15c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-06-28"},{"uniquename":"PMID:32650322","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2020-07-12 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12963726","title":"Schizosaccharomyces pombe cells deficient in triacylglycerols synthesis undergo apoptosis upon entry into the stationary phase.","citation":"J Biol Chem 2003 Nov 21;278(47):47145-55","abstract":"Triacylglycerols (TAG) are important energy storage molecules for nearly all eukaryotic organisms. In this study, we found that two gene products (Plh1p and Dga1p) are responsible for the terminal step of TAG synthesis in the fission yeast Schizosaccharomyces pombe through two different mechanisms: Plh1p is a phospholipid diacylglycerol acyltransferase, whereas Dga1p is an acyl-CoA:diacylglycerol acyltransferase. Cells with both dga1+ and plh1+ deleted (DKO cells) lost viability upon entry into the stationary phase and demonstrated prominent apoptotic markers. Exponentially growing DKO cells also underwent dramatic apoptosis when briefly treated with diacylglycerols (DAGs) or free fatty acids. We provide strong evidence suggesting that DAG, not sphingolipids, mediates fatty acids-induced lipoapoptosis in yeast. Lastly, we show that generation of reactive oxygen species is essential to lipoapoptosis.","authors":"Zhang Q, Chieu HK, Low CP, Zhang S, Heng CK, Yang H","authors_abbrev":"Zhang Q et al.","pubmed_publication_date":"21 Nov 2003","pubmed_entrez_date":"2003-09-10","publication_year":"2003","canto_session_key":"38a7316338b92681","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-07-15 09:48:53","canto_approved_date":"2020-06-19 12:38:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-05 14:44:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1235.15","SPBC776.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-07-15"},{"uniquename":"PMID:16990792","title":"Ordered assembly of Sld3, GINS and Cdc45 is distinctly regulated by DDK and CDK for activation of replication origins.","citation":"EMBO J 2006 Oct 04;25(19):4663-74","abstract":"Initiation of chromosome DNA replication in eukaryotes is tightly regulated through assembly of replication factors at replication origins. Here, we investigated dependence of the assembly of the initiation complex on particular factors using temperature-sensitive fission yeast mutants. The psf3-1 mutant, a GINS component mutant, arrested with unreplicated DNA at the restrictive temperature and the DNA content gradually increased, suggesting a defect in DNA replication. The mutation impaired GINS complex formation, as shown by pull-down experiments. Chromatin immunoprecipitation assays indicated that GINS integrity was required for origin loading of Psf2, Cut5 and Cdc45, but not Sld3. In contrast, loading of Psf2 onto origins depended on Sld3 and Cut5 but not on Cdc45. These results suggest that Sld3 functions furthest upstream in initiation complex assembly, followed by GINS and Cut5, then Cdc45. Consistent with this conclusion, Cdc7-Dbf4 kinase (DDK) but not cyclin-dependent kinase (CDK) was required for Sld3 loading, whereas recruitment of the other factors depended on both kinases. These results suggest that DDK and CDK regulate distinct steps in activation of replication origins in fission yeast.","authors":"Yabuuchi H, Yamada Y, Uchida T, Sunathvanichkul T, Nakagawa T, Masukata H","authors_abbrev":"Yabuuchi H et al.","pubmed_publication_date":"04 Oct 2006","pubmed_entrez_date":"2006-09-23","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC725.13c","SPBP23A10.09","SPBP4H10.21c","SPAC17D4.02","SPBC25H2.13c","SPAC23C4.18c","SPAC6B12.11","SPAC24H6.06","SPAC227.16c"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:23687372","title":"New roles of the fission yeast eIF2α kinases Hri1 and Gcn2 in response to nutritional stress.","citation":"J Cell Sci 2013 Jul 15;126(Pt 14):3010-20","abstract":"In fission yeast, three distinct eukaryotic initiation factor 2α (eIF2α) kinases (Hri1, Hri2 and Gcn2), regulate protein synthesis in response to various environmental stresses. Thus, Gcn2 is activated early after exposure to hydrogen peroxide (H2O2) and methyl methanesulfonate (MMS), whereas Hri2 is the primary activated eIF2α kinase in response to heat shock. The function of Hri1 is still not completely understood. It is also known that the mitogen-activated protein kinase Sty1 negatively regulates Gcn2 and Hri2 activities under oxidative stress. In this study, we demonstrate that Hri1 is mainly activated, and its expression upregulated, during transition from exponential growth to the stationary phase in response to nutritional limitation. Accordingly, both Hri1 and Gcn2, but not Hri2, are activated upon nitrogen source deprivation. In contrast, Hri2 is stimulated early during glucose starvation. We also found that Gcn2 is implicated in nitrogen starvation-induced growth arrest in the cell cycle G1 phase as well as in the non-selective protein degradation process caused upon this particular cellular stress. Moreover, Gcn2, but not Hri1 or Hri2, is essential for survival of cells growing in minimal medium, upon oxidative stress or glucose limitation. We further show that eIF2α phosphorylation at serine 52 by the eIF2α kinases is necessary for efficient cell cycle arrest in the G1 phase, for the consequent protein degradation and for sexual differentiation, under nitrogen starvation. Therefore, the eIF2α kinase signalling pathway modulates G1 phase cell cycle arrest, cell survival and mating under nutritional stress in the fission yeast Schizosaccharomyces pombe.","doi":"10.1242/jcs.118067","authors":"Martín R, Berlanga JJ, de Haro C","authors_abbrev":"Martín R et al.","pubmed_publication_date":"15 Jul 2013","pubmed_entrez_date":"2013-05-21","publication_year":"2013","canto_session_key":"56ab0acf3aa326fc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-11-09 11:58:19","canto_approved_date":"2021-09-17 15:05:57","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-02-17 15:11:25","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC26F1.10c","SPAC3G9.09c","SPAC222.07c","SPAC20G4.03c","SPBC11B10.09","SPBC36B7.09","SPAC24B11.06c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2017-11-09"},{"uniquename":"PMID:16491385","title":"Cloning the Schizosaccharomyces pombe lys2+ gene and construction of new molecular genetic tools.","citation":"Curr Genet 2006 Jun;49(6):414-20","abstract":"Molecular genetic analyses in Schizosaccharomyces pombe rely on selectable markers that are used in cloning vectors or to mark targeted gene deletions and other integrated constructs. In this study, we used genetic mapping data and genomic sequence information to predict the identity of the S. pombe lys2(+) gene, which is homologous to Saccharomyces cerevisiae LYS4(+). We confirmed this prediction, showing that the cloned SPAC343.16 gene can complement a lys2-97 mutant allele, and constructed the lys2(+)-based cloning vector pRH3. In addition, we deleted the S. pombe his7(+) gene with a lys2(+) -marked polymerase chain reaction (PCR) product and the S. pombe lys2(+) gene with a his7(+)-marked PCR product. Strains carrying these deletions of lys2(+) or his7(+) serve as relatively efficient hosts for the deletion of the ade6(+) gene by lys2(+)-- or his7(+)--marked PCR products when compared with hosts carrying lys2 or his7 point mutations. Therefore, these studies provide plasmids and strains allowing the use of lys2(+) as a selectable marker, along with improved strains for the use of his7(+) to mark gene deletions.","authors":"Hoffman RL, Hoffman CS","authors_abbrev":"Hoffman RL et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-02-24","publication_year":"2006","canto_session_key":"ecdd458c35a584ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2012-04-24 22:03:45","canto_session_submitted_date":"2012-04-24 22:03:33","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP7G5.04c","SPAC343.16"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-04-24"},{"uniquename":"PMID:1842338","title":"Regulation of cdc2 activity in Schizosaccharomyces pombe: the role of phosphorylation.","citation":"Semin Cell Biol 1991 Aug;2(4):195-204","abstract":"The cdc2 protein kinase, first identified as a cell cycle gene required for transition into the S- and M-phases of budding and fission yeast, has been shown to act as a key component in the regulation of the eukaryotic cell cycle. The periodic activation of cdc2 kinase, which is required for entry into M-phase, is regulated by subunit association with cyclin B, the cdc25, wee1, mik1 gene products and differential phosphorylation of the cdc2 protein. Phosphorylation at Tyr 15 inhibits activation of the cdc2/cdc13 complex whereas phosphorylation of Thr 167 is required for kinase activity.","authors":"Fleig UN, Gould KL","authors_abbrev":"Fleig UN et al.","pubmed_publication_date":"Aug 1991","pubmed_entrez_date":"1991-08-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28238661","title":"Motor Activity Dependent and Independent Functions of Myosin II Contribute to Actomyosin Ring Assembly and Contraction in Schizosaccharomyces pombe.","citation":"Curr Biol 2017 Mar 06;27(5):751-757","abstract":"Cytokinesis depends on a contractile actomyosin ring in many eukaryotes [1-3]. Myosin II is a key component of the actomyosin ring, although whether it functions as a motor or as an actin cross-linker to exert its essential role is disputed [1, 4, 5]. In Schizosaccharomyces pombe, the myo2-E1 mutation affects the upper 50 kDa sub-domain of the myosin II heavy chain, and cells carrying this lethal mutation are defective in actomyosin ring assembly at the non-permissive temperature [6, 7]. myo2-E1 also affects actomyosin ring contraction when rings isolated from permissive temperature-grown cells are incubated with ATP [8]. Here we report isolation of a compensatory suppressor mutation in the lower 50 kDa sub-domain (myo2-E1-Sup1) that reverses the inability of myo2-E1 to form colonies at the restrictive temperature. myo2-E1-Sup1 is capable of assembling normal actomyosin rings, although rings isolated from myo2-E1-Sup1 are defective in ATP-dependent contraction in vitro. Furthermore, the product of myo2-E1-Sup1 does not translocate actin filaments in motility assays in vitro. Superimposition of myo2-E1 and myo2-E1-Sup1 on available rigor and blebbistatin-bound myosin II structures suggests that myo2-E1-Sup1 may represent a novel actin translocation-defective allele. Actomyosin ring contraction and viability of myo2-E1-Sup1 cells depend on the late cytokinetic S. pombe myosin II isoform, Myp2p, a non-essential protein that is normally dispensable for actomyosin ring assembly and contraction. Our work reveals that Myo2p may function in two different and essential modes during cytokinesis: a motor activity-independent form that can promote actomyosin ring assembly and a motor activity-dependent form that supports ring contraction.","doi":"10.1016/j.cub.2017.01.028","authors":"Palani S, Chew TG, Ramanujam S, Kamnev A, Harne S, Chapa-Y-Lazo B, Hogg R, Sevugan M, Mishra M, Gayathri P, Balasubramanian MK","authors_abbrev":"Palani S et al.","pubmed_publication_date":"06 Mar 2017","pubmed_entrez_date":"2017-02-28","publication_year":"2017","canto_session_key":"9a5c66e724eee872","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-01 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAC4A8.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:24586893","title":"Wat1/pop3, a conserved WD repeat containing protein acts synergistically with checkpoint kinase Chk1 to maintain genome ploidy in fission yeast S. pombe.","citation":"PLoS One 2014;9(2):e89587","abstract":"Aberrant chromosome segregation defects can lead to aneuploidy, a common characteristic of human solid tumors. Aneuploidy is generated due to defects in the mitotic spindle or due to inefficient mitotic checkpoint response. We have isolated a novel mutant allele of wat1, a WD repeat containing protein that exhibits conditional synthetic lethality with chk1 knock out. We observed only a marginal decrease in the level of α tubulin protein level in wat1-17 mutants after prolong exposure at semi permissive temperature. Interestingly the protein level of α-tubulin was reduced in the chk1Δ wat1-17 double mutant at 18°C with defective microtubule structure. Consistent with loss of microtubule structure in the chk1 deletion background, the double mutant of wat1-17 chk1Δ was hypersensitive to the microtubule destabilizing agent TBZ suggesting severe defects in microtubule integrity in wat1-17 mutant in the absence of Chk1. Combination of wat1-17 with the chk1 deletion also aggravates the defects in the maintenance of genome ploidy. The mutation in wat1-17 was mapped to Cys 233 that was changed to tyrosine. Based on the molecular modeling studies, we hypothesize that the substitution of the bulky Tyr residue at Cys233 position in wat1-17 mutant results in conformational changes. This in turn can affect its intercations with other interacting partners and perturb the overall functions of the Wat1 protein.","doi":"10.1371/journal.pone.0089587","authors":"Verma SK, Ranjan R, Kumar V, Siddiqi MI, Ahmed S","authors_abbrev":"Verma SK et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-03-04","publication_year":"2014","canto_session_key":"4e7e30e382d662d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-02-08 19:11:37","canto_approved_date":"2023-11-27 19:13:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-10 04:29:29","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21B10.05c","SPBC146.07","SPCC1259.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-02-08"},{"uniquename":"PMID:40973456","title":"Runaway evolution of telomeres in ascomycetous yeasts was accompanied by the replacement of ancestral telomeric proteins.","citation":"Nucleic Acids Res 2025 Sep 05;53(17)","abstract":"Telomeres are crucial parts of eukaryotic chromosomes, contributing to DNA replication, chromosome segregation, and genome stability. While in most phylogenetic lineages, telomere-maintenance systems are conserved, ascomycetous yeasts exhibit a high degree of variability in telomeric repeats and the associated proteins. The determinants that enabled this divergent evolutionary process, however, have been unclear. Here, we show that DNA-binding properties of yeast telomere-binding proteins (TBPs) support the scenario where the gradual divergence of telomeric repeats led to their replacement. We analyzed the DNA-protein interactions between Tay1p from Yarrowia lipolytica, Rap1p from Saccharomyces cerevisiae, and Taz1p from Schizosaccharomyces pombe and a set of telomeric repeats from several yeast species and delineated how the ancestral (Tay1p-like) TBPs were replaced by Rap1p (in budding yeasts) or Taz1p (in fission yeasts). We also postulate two different driving forces for these replacements: (i) Tay1p-to-Rap1p transition appears to be driven by differences in sequence preferences of Tay1p and Rap1p, while (ii) Taz1p became the principal TBP in fission yeast presumably due to its DNA-binding flexibility. Together, our results suggest that in telomeric DNA-protein complexes, the replacement of protein component triggered by the initial variation in DNA sequence space opens the door to further divergence in a runaway-style evolution.","doi":"10.1093/nar/gkaf906","authors":"Červenák F, Virágová S, Sopkovičová M, Kodada D, Galla E, Sepšiová R, Procházková K, Tomáška Ľ","authors_abbrev":"Červenák F et al.","pubmed_publication_date":"05 Sep 2025","pubmed_entrez_date":"2025-09-19","publication_year":"2025","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2025-09-20 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15359282","title":"Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance.","citation":"EMBO J 2004 Oct 01;23(19):3844-53","abstract":"Sumoylation represents a conserved mechanism of post-translational protein modification. We report that Pli1p, the unique fission yeast member of the SP-RING family, is a SUMO E3 ligase in vivo and in vitro. pli1Delta cells display no obvious mitotic growth defects, but are sensitive to the microtubule-destabilizing drug TBZ and exhibit enhanced minichromosome loss. The weakened centromeric function of pli1Delta cells may be related to the defective heterochromatin structure at the central core, as shown by the reduced silencing of an ura4 variegation reporter gene inserted at cnt and imr. Interestingly, pli1Delta cells also exhibit enhanced loss of the ura4 reporter at these loci, likely by gene conversion using homologous sequences as information donors. Moreover, pli1Delta cells exhibit consistent telomere length increase, possibly achieved by a similar process. Point mutations within the RING finger of Pli1p totally or partially reproduce the pli1 deletion phenotypes, thus correlating with their sumoylation activity. Altogether, these results strongly suggest that Pli1p, and by extension sumoylation, is involved in mechanisms that regulate recombination in particular heterochromatic repeated sequences.","authors":"Xhemalce B, Seeler JS, Thon G, Dejean A, Arcangioli B","authors_abbrev":"Xhemalce B et al.","pubmed_publication_date":"01 Oct 2004","pubmed_entrez_date":"2004-09-11","publication_year":"2004","canto_session_key":"eff3b387846d7c66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-15 18:10:51","canto_approved_date":"2024-04-04 17:14:56","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-14 14:09:04","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":23,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPBC365.06","SPAC1556.01c","SPAC30D11.13","SPAC4C5.04","SPAC1687.05","SPAC30D11.10"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2024-03-15"},{"uniquename":"PMID:22918952","title":"Multiple protein kinases influence the redistribution of fission yeast Clp1/Cdc14 phosphatase upon genotoxic stress.","citation":"Mol Biol Cell 2012 Oct;23(20):4118-28","abstract":"The Cdc14 phosphatase family antagonizes Cdk1 phosphorylation and is important for mitotic exit. To access their substrates, Cdc14 phosphatases are released from nucleolar sequestration during mitosis. Clp1/Flp1, the Schizosaccharomyces pombe Cdc14 orthologue, and Cdc14B, a mammalian orthologue, also exit the nucleolus during interphase upon DNA replication stress or damage, respectively, implicating Cdc14 phosphatases in the response to genotoxic insults. However, a mechanistic understanding of Cdc14 phosphatase nucleolar release under these conditions is incomplete. We show here that relocalization of Clp1 during genotoxic stress is governed by complex phosphoregulation. Specifically, the Rad3 checkpoint effector kinases Cds1 and/or Chk1, the cell wall integrity mitogen-activated protein kinase Pmk1, and the cell cycle kinase Cdk1 directly phosphorylate Clp1 to promote genotoxic stress-induced nucleoplasmic accumulation. However, Cds1 and/or Chk1 phosphorylate RxxS sites preferentially upon hydroxyurea treatment, whereas Pmk1 and Cdk1 preferentially phosphorylate Clp1 TP sites upon H(2)O(2) treatment. Abolishing both Clp1 RxxS and TP phosphosites eliminates any genotoxic stress-induced redistribution. Reciprocally, preventing dephosphorylation of Clp1 TP sites shifts the distribution of the enzyme to the nucleoplasm constitutively. This work advances our understanding of pathways influencing Clp1 localization and may provide insight into mechanisms controlling Cdc14B phosphatases in higher eukaryotes.","doi":"10.1091/mbc.E12-06-0475","authors":"Broadus MR, Gould KL","authors_abbrev":"Broadus MR et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-25","publication_year":"2012","canto_session_key":"d378014af8ea8779","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2018-09-14 15:13:45","canto_approved_date":"2020-12-04 16:44:00","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-08-22 16:50:09","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC216.05","SPCC1259.13","SPBC119.08","SPBC11B10.09","SPAC1782.09c","SPAC8E11.02c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-09-14"},{"uniquename":"PMID:29722930","title":"Septins regulate the equatorial dynamics of the separation initiation network kinase Sid2p and glucan synthases to ensure proper cytokinesis.","citation":"FEBS J 2018 Jul;285(13):2468-2480","abstract":"Septins generally function as scaffolds and as cortical barriers to restrict the diffusion of membrane proteins. In the fission yeast Schizosaccharomyces pombe, septins form a ring structure at the septum after spindle breakdown during the constriction of the contractile actomyosin ring (CAR) and serve as a scaffold to recruit glucanases to mediate ultimate daughter cell separation. Despite this, it remains unclear if septins play any significant roles before the cell separation during cytokinesis. Employing live cell microscopy, we carefully examined SIN (Septation Initiation Network) signaling and glucan synthases, two key factors ensuring proper function of the CAR. In the absence of the core septin component Spn1p, the formation of a compact CAR is advanced and the CAR constriction rate is slightly but significantly decreased. Moreover, the SIN kinase Sid2p and the glucan synthases Bgs1p and Ags1p form an equatorial ring quite prematurely, but their maintenance at the equatorial region is diminished spn1Δ cells. These findings suggest that septins act as key players in an accurate establishment and the maintenance of CAR by orchestrating the equatorial dynamics of Sid2p and glucan synthases. Hence, this work demonstrates that, in addition to their function during ultimate cell septation, septins have important roles in regulating earlier cytokinetic events, including CAR assembly and constriction, SIN signaling, and the cortical dynamics of the glucan synthases.","doi":"10.1111/febs.14487","authors":"Zheng S, Dong F, Rasul F, Yao X, Jin QW, Zheng F, Fu C","authors_abbrev":"Zheng S et al.","pubmed_publication_date":"Jul 2018","pubmed_entrez_date":"2018-05-04","publication_year":"2018","canto_session_key":"3f7e2cdbb78f8e13","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-05-05 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1A4.05","SPAC4F10.11"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:19887589","title":"Fission yeast Myo51 is a meiotic spindle pole body component with discrete roles during cell fusion and spore formation.","citation":"J Cell Sci 2009 Dec 01;122(Pt 23):4330-40","abstract":"Class V myosins are dimeric actin-associated motor proteins that deliver cellular cargoes to discrete cellular locations. Fission yeast possess two class V myosins, Myo51 and Myo52. Although Myo52 has been shown to have roles in vacuole distribution, cytokinesis and cell growth, Myo51 has no as yet discernible function in the vegetative life cycle. Here, we uncover distinct functions for this motor protein during mating and meiosis. Not only does Myo51 transiently localise to a foci at the site of cell fusion upon conjugation, but overexpression of the Myo51 globular tail also leads to disruption of cell fusion. Upon completion of meiotic prophase Myo51 localises to the outside of the spindle pole bodies (SPBs), where it remains until completion of meiosis II. Association of Myo51 with SPBs is not dependent upon actin or the septation initiation network (SIN); however, it is dependent on a stable microtubule cytoskeleton and the presence of the Cdc2-CyclinB complex. We observe a rapid and dynamic exchange of Myo51 at the SPB during meiosis I but not meiosis II. Finally, we show that Myo51 has an important role in regulating spore formation upon completion of meiosis.","doi":"10.1242/jcs.055202","authors":"Doyle A, Martín-García R, Coulton AT, Bagley S, Mulvihill DP","authors_abbrev":"Doyle A et al.","pubmed_publication_date":"01 Dec 2009","pubmed_entrez_date":"2009-11-06","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19278635","title":"Cell polarization: it's all about being in shape.","citation":"Curr Biol 2009 Mar 10;19(5):R205-6","abstract":"In eukaryotic cells microtubules and actin filaments help to generate the spatial organization of the cytoplasm that is required for polarity and shape. Recent work in fission yeast demonstrates that changing cell shape in turn reorganizes the cytoskeleton and cell polarization machinery.","doi":"10.1016/j.cub.2009.01.024","authors":"Srinivasan R, Mishra M","authors_abbrev":"Srinivasan R et al.","pubmed_publication_date":"10 Mar 2009","pubmed_entrez_date":"2009-03-13","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21132016","title":"Yox1 links MBF-dependent transcription to completion of DNA synthesis.","citation":"EMBO Rep 2011 Jan;12(1):84-9","abstract":"When DNA replication is challenged cells activate a DNA synthesis checkpoint, blocking cell cycle progression until they are able to overcome the replication defects. In fission yeast, Cds1 is the effector kinase of this checkpoint, inhibiting M-phase entry, stabilizing stalled replication forks and triggering transcriptional activation of S-phase genes. The molecular basis of this last effect is largely unknown. The Mlu1 binding factor (MBF) complex controls the transcription of S-phase genes. We purified novel interactors of the MBF complex and identified the repressor Yox1. When the DNA synthesis checkpoint is activated, Yox1 is phosphorylated, which abrogates its binding to MBF. MBF-dependent transcription therefore remains active until cells are able to overcome this challenge.","doi":"10.1038/embor.2010.187","authors":"Gómez-Escoda B, Ivanova T, Calvo IA, Alves-Rodrigues I, Hidalgo E, Ayté J","authors_abbrev":"Gómez-Escoda B et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-12-07","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC21B10.13c","SPBC725.16","SPCC18B5.11c","SPBC336.12c","SPAC22F3.09c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:10473635","title":"Rad18 is required for DNA repair and checkpoint responses in fission yeast.","citation":"Mol Biol Cell 1999 Sep;10(9):2905-18","abstract":"To survive damage to the genome, cells must respond by activating both DNA repair and checkpoint responses. Using genetic screens in the fission yeast Schizosaccharomyces pombe, we recently isolated new genes required for DNA damage checkpoint control. We show here that one of these strains defines a new allele of the previously described rad18 gene, rad18-74. rad18 is an essential gene, even in the absence of extrinsic DNA damage. It encodes a conserved protein related to the structural maintenance of chromosomes proteins. Point mutations in rad18 lead to defective DNA repair pathways responding to both UV-induced lesions and, as we show here, double-stranded breaks. Furthermore, rad18p is required to maintain cell cycle arrest in the presence of DNA damage, and failure of this leads to highly aberrant mitoses. A gene encoding a BRCT-containing protein, brc1, was isolated as an allele-specific high-copy suppressor of rad18-74. brc1 is required for mitotic fidelity and for cellular viability in strains with rad18 mutations but is not essential for DNA damage responses. Mutations in rad18 and brc1 are synthetically lethal with a topoisomerase II mutant (top2-191), indicating that these proteins play a role in chromatin organization. These studies show a role for chromatin organization in the maintenance or activation of responses to DNA damage.","authors":"Verkade HM, Bugg SJ, Lindsay HD, Carr AM, O'Connell MJ","authors_abbrev":"Verkade HM et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-09-03","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19E9.02","SPBC1A4.03c","SPCC5E4.06","SPBC582.05c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:8000531","title":"Glucose-transport-deficient mutants of Schizosaccharomyces pombe: phenotype, genetics and use for genetic complementation.","citation":"Microbiology (Reading) 1994 Oct;140 ( Pt 10):2617-23","abstract":"Glucose-transport-deficient mutants of Schizosaccharomyces pombe were obtained by treatment of wild-type cells (972h-) with N-methyl-N'-nitro-N- nitrosoguanidine, and by selection of resulting mutants on gluconate medium containing 0.05% 2-deoxy-D-glucose (2DG). One mutant, designated YGS-B22, was unable to grow on D-glucose and/or D-fructose as a carbon source (Glc/Fru-), and was resistant to 2DG; hence, none of the three sugars was taken up by the mutant cells. The hexokinase activity in the wild-type and the mutant cells was equal. Genetic purification of YGS-B22 by back-crossing with a leucine-auxotrophic mutant and the wild-type resulted in two strains: YGS-4, with reduced 2DG resistance, and YGS-5, which had lost 2DG-resistance. YGS-5 grew in D-glucose-containing media, albeit very slowly. No measurable sugar uptake was detectable in either of the two mutants within the 1 h test interval. Tetrad analyses proved a Mendelian segregation of growth on D-glucose and leucine auxotrophy. However, 2DG resistance did not co-segregate with the Glc/Fru- phenotype, indicating that the transport deficiency and 2DG resistance characters are not encoded on the same genomic locus. Using a genomic bank of Sch. pombe, two transformants, YGS-5-G7 and YGS-5-G12, were found which had regained the wild-type growth and transport phenotype by complementation. Correspondingly, both D-glucose uptake and 2DG accumulation were restored in the transformed strains.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Milbradt B, Höfer M","authors_abbrev":"Milbradt B et al.","pubmed_publication_date":"Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_session_key":"cb152da725a506ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-27 15:48:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-27 15:45:28","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC548.07c","SPCC1235.14","SPCC1235.13"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2012-11-27"},{"uniquename":"PMID:8212899","title":"Cloning and sequence of ADP-ribosylation factor 1 (ARF1) from Schizosaccharomyces pombe.","citation":"Yeast 1993 Aug;9(8):923-7","abstract":"A gene encoding a homologue of the ADP-ribosylation factor (ARF) family of small GTP binding proteins was cloned from a Schizosaccharomyces pombe cDNA library by a functional screen of suppressors of sensitivity to 3-aminotriazole in a gcn3 null strain of Saccharomyces cerevisiae. Two independent isolates each contained the full coding region of the ARF1 gene. The encoded SpARF1 protein has a predicted molecular weight of 20,618 and is 88% and 79% identical to human and S. cerevisiae ARF1 proteins, respectively. As independent isolates were obtained, this effect of the SpARF1 appears to be a real phenomenon, but cannot currently be easily understood within the context of the evidence for a role(s) for ARF proteins in the protein secretory pathway.","authors":"Erickson FL, Hannig EM, Krasinskas A, Kahn RA","authors_abbrev":"Erickson FL et al.","pubmed_publication_date":"Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_session_key":"1b014f4f6c484833","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 13:27:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 13:27:36","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4F6.18c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-07-31"},{"uniquename":"PMID:8879046","title":"Defining the role of Sxa1 during pheromone adaptation in Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1996 Aug;24(3):502S","abstract":"","authors":"Hughes M, Ladds G, Davey J","authors_abbrev":"Hughes M et al.","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_session_key":"4c6458be418faa18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:46:08","canto_session_submitted_date":"2012-02-27 11:06:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PANTHER:PTHR10335","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:3599","SPBC4.02c","HGNC:35458"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU008058","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15173383","title":"The C-terminal zinc finger of the catalytic subunit of DNA polymerase delta is responsible for direct interaction with the B-subunit.","citation":"Nucleic Acids Res 2004;32(10):3005-16","abstract":"DNA polymerase delta (Pol delta) plays a central role in eukaryotic chromosomal DNA replication, repair and recombination. In fission yeast, Pol delta is a tetrameric enzyme, comprising the catalytic subunit Pol3 and three smaller subunits, Cdc1, Cdc27 and Cdm1. Previous studies have demonstrated a direct interaction between Pol3 and Cdc1, the B-subunit of the complex. Here it is shown that removal of the tandem zinc finger modules located at the C-terminus of Pol3 by targeted proteolysis renders the Pol3 protein non-functional in vivo, and that the C-terminal zinc finger module ZnF2 is both necessary and sufficient for binding to the B-subunit in vivo and in vitro. Extensive mutagenesis of the ZnF2 module identifies important residues for B-subunit binding. In particular, disruption of the ZnF2 module by substitution of the putative metal-coordinating cysteines with alanine abolishes B-subunit binding and in vivo function. Finally, evidence is presented suggesting that the ZnF region is post-translationally modified in fission yeast cells.","authors":"Sanchez Garcia J, Ciufo LF, Yang X, Kearsey SE, MacNeill SA","authors_abbrev":"Sanchez Garcia J et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-06-03","publication_year":"2004","canto_session_key":"44ae5ece389a1b0a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-30 16:59:18","canto_approved_date":"2024-03-28 16:42:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-06-08 13:42:20","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.04","SPAC27E2.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-07-30"},{"uniquename":"PMID:11523791","title":"A homologue of the Rad18 postreplication repair gene is required for DNA damage responses throughout the fission yeast cell cycle.","citation":"Mol Genet Genomics 2001 Aug;265(6):993-1003","abstract":"Cells activate DNA repair pathways and cell cycle checkpoints when they suffer damage to their genome. They also activate tolerance pathways that facilitate survival. In Escherichia coli, a mechanism known as postreplication repair (PRR) is used to bypass lesions that would otherwise present a physical block to DNA polymerase. PRR has also been proposed to occur in eukaryotic cells, although the partitioning of DNA synthesis to a discrete S-phase would suggest that it is only operative within a defined period of the cell cycle. Eukaryotic PRR has been most extensively studied in the budding yeast Saccharomyces cerevisiae. Two important genes for components of this repair pathway are RAD6, which encodes an ubiquitin-conjugating enzyme, and RAD18, which encodes a RING-finger protein and forms a heterodimer with Rad6p. Rad18p can also bind to DNA. We report here the identification of the Schizosaccharomyces pombe homologue of RAD18, which we have denoted rhp18. rhp18 mutants are hypersensitive to DNA-damaging agents, but show this hypersensitivity throughout the cell cycle. rhp18 mutants are characterised by a longer than usual DNA damage checkpoint arrest that is required for their residual viability following irradiation. Genetic analyses show that rhp18 controls a unique DNA damage repair/tolerance pathway that extends beyond the requirement to tolerate damage during S-phase, suggesting a broader definition of the function of this eukaryotic PRR protein.","authors":"Verkade HM, Teli T, Laursen LV, Murray JM, O'Connell MJ","authors_abbrev":"Verkade HM et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-08-29","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC2G11.12","SPAC644.14c","SPBC19C7.09c","SPBC216.05","SPBC1734.06","SPBC3E7.08c","SPAC18B11.07c"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:19462967","title":"Kinetic, dynamic, ligand binding properties, and structural models of a dual-substrate specific nudix hydrolase from Schizosaccharomyces pombe.","citation":"Biochemistry 2009 Jul 07;48(26):6224-39","abstract":"Schizosaccharomyces pombe Aps1 is a nudix hydrolase that catalyzes the hydrolysis of both diadenosine 5',5'''-P(1),P(n)-oligophosphates and diphosphoinositol polyphosphates in vitro. Nudix hydrolases act upon a wide variety of substrates, despite having a common 23 amino acid catalytic motif; hence, the residues responsible for substrate specificity are considered to reside outside the common catalytic nudix motif. The specific residues involved in binding each substrate of S. pombe Aps1 are unknown. In this study, we have conducted mutational and kinetic studies in combination with structural homology modeling and NMR spectroscopic analyses to identify potential residues involved in binding each class of substrates. This study demonstrates several major findings with regard to Aps1. First, the determination of the kinetic parameters of K(m) and k(cat) indicated that the initial 31 residues of Aps1 are not involved in substrate binding or catalysis with respect to Ap(6)A. Second, NMR spectroscopic analyses revealed the secondary structure and three dynamic backbone regions, one of which corresponds to a large insert in Aps1 as compared to other putative fungal orthologues. Third, two structural models of Aps1Delta2-19, based on the crystal structures of human DIPP1 and T. thermophilus Ndx1, were generated using homology modeling. The structural models were in excellent agreement with the NMR-derived secondary structure of Aps1Delta2-19. Fourth, NMR chemical shift mapping in conjunction with structural homology models indicated several residues outside the catalytic nudix motif that are involved in specific binding of diphosphoinositol polyphosphate or diadenosine oligophosphate ligands.","doi":"10.1021/bi802266g","authors":"Garza JA, Ilangovan U, Hinck AP, Barnes LD","authors_abbrev":"Garza JA et al.","pubmed_publication_date":"07 Jul 2009","pubmed_entrez_date":"2009-05-26","publication_year":"2009","canto_session_key":"935ec0b0acd37508","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-12 11:19:04","canto_approved_date":"2024-06-12 11:19:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 11:18:58","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G6.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-06-12"},{"uniquename":"PMID:11180456","title":"Hyperthermotolerant fission yeast mutations, sow1 and sow2, suppress the cell cycle defect and stress sensitivity of MAP kinase kinase wis1Delta.","citation":"Yeast 2001 Feb;18(3):229-38","abstract":"Wis1 is a mitogen-activated protein kinase kinase (MAPKK) that regulates mitosis and mediates stress responses in the fission yeast, Schizosaccharomyces pombe. wis1Delta strains are viable but stress-sensitive and show a mitotic delay. At high temperatures, wis1Delta cells cease division but cellular growth continues. Mutations that suppress the heat sensitivity of a wis1Delta strain were isolated and map to two apparently novel loci, sow1 (for suppressor of wis1Delta) and sow2. In addition to suppressing wis1Delta heat sensitivity, sow1 and sow2 can suppress wis1Delta osmosensitivity and cell cycle defects. sow1 and sow2 mutants in a wis1+ background were able to grow at higher temperatures than wild-type and sow1 showed a mitotic advance. The sow genes may therefore define a novel connection between stress tolerance and cell cycle control.","authors":"Prochnik S, Fantes P","authors_abbrev":"Prochnik S et al.","pubmed_publication_date":"Feb 2001","pubmed_entrez_date":"2001-02-17","publication_year":"2001","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19473886","title":"Taking the time to make important decisions: the checkpoint effector kinases Chk1 and Chk2 and the DNA damage response.","citation":"DNA Repair (Amst) 2009 Sep 02;8(9):1047-54","abstract":"The cellular DNA damage response (DDR) is activated by many types of DNA lesions. Upon recognition of DNA damage by sensor proteins, an intricate signal transduction network is activated to coordinate diverse cellular outcomes that promote genome integrity. Key components of the DDR in mammalian cells are the checkpoint effector kinases Chk1 and Chk2 (referred to henceforth as the effector kinases; orthologous to spChk1 and spCds1 in the fission yeast S. pombe and scChk1 and scRad53 in the budding yeast S. cerevisiae). These evolutionarily conserved and structurally divergent kinases phosphorylate numerous substrates to regulate the DDR. This review will focus on recent advances in our understanding of the structure, regulation, and functions of the effector kinases in the DDR, as well as their potential roles in human disease.","doi":"10.1016/j.dnarep.2009.04.012","authors":"Stracker TH, Usui T, Petrini JH","authors_abbrev":"Stracker TH et al.","pubmed_publication_date":"02 Sep 2009","pubmed_entrez_date":"2009-05-29","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22017866","title":"Sterols for Oxygen: The Metabolic Burden of Microbial SREBP.","citation":"Mol Cell 2011 Oct 21;44(2):172-4","abstract":"In this issue of Molecular Cell, Lee et al. (2011) report a novel mechanism for oxygen-sensing in S. pombe, whereby the 2-OG-Fe(II) dioxygenase Ofd protein regulates both the DNA-binding activity and the degradation of the hypoxia regulated transcription factor, Sre1p.","doi":"10.1016/j.molcel.2011.10.004","authors":"Osborne TF","authors_abbrev":"Osborne TF","pubmed_publication_date":"21 Oct 2011","pubmed_entrez_date":"2011-10-25","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15899844","title":"Fission yeast rad51 and dmc1, two efficient DNA recombinases forming helical nucleoprotein filaments.","citation":"Mol Cell Biol 2005 Jun;25(11):4377-87","abstract":"Homologous recombination is important for the repair of double-strand breaks during meiosis. Eukaryotic cells require two homologs of Escherichia coli RecA protein, Rad51 and Dmc1, for meiotic recombination. To date, it is not clear, at the biochemical level, why two homologs of RecA are necessary during meiosis. To gain insight into this, we purified Schizosaccharomyces pombe Rad51 and Dmc1 to homogeneity. Purified Rad51 and Dmc1 form homo-oligomers, bind single-stranded DNA preferentially, and exhibit DNA-stimulated ATPase activity. Both Rad51 and Dmc1 promote the renaturation of complementary single-stranded DNA. Importantly, Rad51 and Dmc1 proteins catalyze ATP-dependent strand exchange reactions with homologous duplex DNA. Electron microscopy reveals that both S. pombe Rad51 and Dmc1 form nucleoprotein filaments. Rad51 formed helical nucleoprotein filaments on single-stranded DNA, whereas Dmc1 was found in two forms, as helical filaments and also as stacked rings. These results demonstrate that Rad51 and Dmc1 are both efficient recombinases in lower eukaryotes and reveal closer functional and structural similarities between the meiotic recombinase Dmc1 and Rad51. The DNA strand exchange activity of both Rad51 and Dmc1 is most likely critical for proper meiotic DNA double-strand break repair in lower eukaryotes.","authors":"Sauvageau S, Stasiak AZ, Banville I, Ploquin M, Stasiak A, Masson JY","authors_abbrev":"Sauvageau S et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-05-19","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.03c","SPAC644.14c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:16299470","title":"The wild-type Schizosaccharomyces pombe mat1 imprint consists of two ribonucleotides.","citation":"EMBO Rep 2006 Jan;7(1):59-65","abstract":"The imprint at the mat1 locus of Schizosaccharomyces pombe acts to initiate the replication-coupled recombination event that underlies mating-type switching. However, the nature of the imprint has been an area of dispute. Two alternative models have been proposed: one stated that the imprint is a nick in the DNA, whereas our data suggested that it consists of one or two ribonucleotides incorporated into the otherwise intact DNA duplex. Here, we verify key predictions of the RNA model by characterization of wild-type genomic DNA purified under conditions known to hydrolyse DNA-RNA-DNA hybrid strands. First, we observe one-nucleotide gap at the hydrolysed DNA, as expected from the presence of two ribonucleotides. Second, using a novel assay based on ligation-mediated PCR, a 3'-terminal ribonucleotide is detected at the hydrolysed imprint. Our observations allow the unification of available data sets characterizing the wild-type imprint.","authors":"Vengrova S, Dalgaard JZ","authors_abbrev":"Vengrova S et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2005-11-22","publication_year":"2006","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC01163","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19567474","title":"Transmembrane segments of the dynamin Msp1p uncouple its functions in the control of mitochondrial morphology and genome maintenance.","citation":"J Cell Sci 2009 Aug 01;122(Pt 15):2632-9","abstract":"Mitochondrial morphology depends on the equilibrium between antagonistic fission and fusion forces acting on mitochondrial membranes. Inactivation of fusion induces the loss of mtDNA. When both fusion and fission are simultaneously inactivated, the loss of mtDNA is alleviated, along with mitochondrial fragmentation. Mechanisms involved in mtDNA maintenance thus seem to depend on a coordinated regulation of fusion and fission forces. We have studied the role of the dynamin Msp1p, a fusion effector in mitochondrial morphology, in relation to the maintenance of mtDNA. Two hydrophobic regions of Msp1p, predicted to be transmembrane segments, were shown to anchor the long form of the protein into mitochondrial membranes, whereas the short form, lacking these two domains, behaved as a peripheral membrane protein. Both domains were essential for the fusogenic activity of Msp1p, but deletion of the second domain alone induced loss of mtDNA and thus lethality. Our results demonstrate that the role of Msp1p in the control of mitochondrial morphology is distinct from that required for genome maintenance, and that only the latter function is essential for cell viability. This parallels recent observations that have distinguished the role of OPA1, the human orthologue of Msp1p, in mitochondrial dynamics from that in cristae organization and apoptosis. Furthermore, our observations may contribute to our understanding of the pathological mechanisms resulting from mutations in OPA1 that give rise to the ADOA syndromes.","doi":"10.1242/jcs.040139","authors":"Diot A, Guillou E, Daloyau M, Arnauné-Pelloquin L, Emorine LJ, Belenguer P","authors_abbrev":"Diot A et al.","pubmed_publication_date":"01 Aug 2009","pubmed_entrez_date":"2009-07-02","publication_year":"2009","canto_session_key":"e479cd586b7c6c9b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-21 08:39:49","canto_approved_date":"2024-08-21 08:39:49","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-21 08:39:43","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":5,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-08-21"},{"uniquename":"PMID:29290560","title":"ER-PM Contacts Restrict Exocytic Sites for Polarized Morphogenesis.","citation":"Curr Biol 2018 Jan 08;28(1):146-153.e5","abstract":"Spatial control of exocytosis underlies polarized cell morphogenesis. In rod-shaped fission yeast, exocytic vesicles are conveyed along the actin cytoskeleton by myosin V motors toward growing cell ends [1, 2], the major sites for exocytosis. However, actomyosin-based vesicle delivery is dispensable for polarized secretion and cylindrical cell shape of fission yeast [3]. Thus, additional mechanisms should function in the spatial confinement of exocytosis. Here we report a novel role of endoplasmic reticulum (ER)-plasma membrane (PM) contacts in restricting exocytic sites for polarized fission yeast morphogenesis. We show that fission yeast cells deficient in both ER-PM contacts and actomyosin-based secretory vesicle transport display aberrant globular cell shape due to delocalized exocytosis. By artificially manipulating the strength and extent of ER-PM contacts in wild-type and mutant cells that exhibit induced ectopic exocytosis, we demonstrate that exocytosis and ER-PM contact formation are spatially incompatible. Furthermore, extensive ER-PM junctions at the non-growing lateral cell cortex prevent the PM from exocytic vesicle tethering and hence attenuate growth potential at cell sides. We thus propose that ER-PM contacts function as a new morphogenetic module by limiting exocytosis to growing cell tips in fission yeast. A similar mechanism could apply to other cell types with prominent ER-PM contacts.","doi":"10.1016/j.cub.2017.11.055","authors":"Ng AYE, Ng AQE, Zhang D","authors_abbrev":"Ng AYE et al.","pubmed_publication_date":"08 Jan 2018","pubmed_entrez_date":"2018-01-02","publication_year":"2018","canto_session_key":"a4e15abcd73293ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dan Zhang","canto_first_approved_date":"2018-01-26 16:19:43","canto_approved_date":"2024-04-02 14:48:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-10 06:30:36","canto_added_date":"2018-01-03 01:15:14","annotation_curators":[{"name":"Dan Zhang","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.12","SPCC970.09","SPCC1235.10c","SPAC110.03","SPAC6G9.11","SPCC1919.10c","SPBC2D10.14c","SPCC895.05","SPAC23C4.08","SPBC16G5.05c","SPAC17C9.12"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2018-01-26"},{"uniquename":"PMID:17348709","title":"A novel lumazine synthase inhibitor derived from oxidation of 1,3,6,8-tetrahydroxy-2,7-naphthyridine to a tetraazaperylenehexaone derivative.","citation":"J Org Chem 2007 Apr 13;72(8):2769-76","abstract":"Air oxidation of 1,3,6,8-tetrahydroxy-2,7-naphthyridine afforded 2,5,8,11-tetraaza-5,11-dihydro-4,10-dihydroxyperylene-1,3,6,7,9,12-hexaone. X-ray crystallography of the product revealed that it exists in the meso form in the solid state. The mechanism of product formation most likely involves oxidative phenolic coupling and oxidation. The product proved to be a competitive inhibitor of Schizosaccharomyces pombe lumazine synthase with a Ki of 66+/-13 microM in Tris buffer and 22+/-4 microM in phosphate buffer. This is significantly more potent than the reactant (Ki 350+/-76 microM, competitive inhibition), which had previously been identified as a lumazine synthase inhibitor by high-throughput screening. Ab initio calculations indicate that the meso form is slightly less stable than the enantiomeric form, and that the two forms interconvert rapidly at room temperature.","authors":"Zhang Y, Illarionov B, Bacher A, Fischer M, Georg GI, Ye QZ, Vander Velde D, Fanwick PE, Song Y, Cushman M","authors_abbrev":"Zhang Y et al.","pubmed_publication_date":"13 Apr 2007","pubmed_entrez_date":"2007-03-14","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24013504","title":"Tpz1 controls a telomerase-nonextendible telomeric state and coordinates switching to an extendible state via Ccq1.","citation":"Genes Dev 2013 Sep 01;27(17):1917-31","abstract":"Telomeres are nucleoprotein complexes comprising telomeric DNA repeats bound by the multiprotein shelterin complex. A dynamic binary switch between telomerase-extendible and telomerase-nonextendible telomeric states determines telomere length homeostasis. However, the molecular nature of the nonextendible state is largely unknown. Here, we show that, in fission yeast, Tpz1 (the ortholog of human TPP1)-mediated complete linkage within the shelterin complex, bridging telomeric dsDNA to ssDNA, controls the telomerase-nonextendible state. Disruption of this linkage leads to unregulated telomere elongation while still retaining the shelterin components on telomeres. Therefore, the linkage within the shelterin components, rather than the individual shelterin components per se, defines the telomerase-nonextendible state. Furthermore, epistasis analyses reveal that Tpz1 also participates in the activation of telomeres to the extendible state via its interaction with Ccq1. Our results suggest critical regulatory roles of Tpz1 in the telomere binary switch.","doi":"10.1101/gad.219485.113","authors":"Jun HI, Liu J, Jeong H, Kim JK, Qiao F","authors_abbrev":"Jun HI et al.","pubmed_publication_date":"01 Sep 2013","pubmed_entrez_date":"2013-09-10","publication_year":"2013","canto_session_key":"e62b222855e26bac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Feng Qiao","canto_first_approved_date":"2015-11-20 14:30:21","canto_approved_date":"2022-05-18 12:21:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-15 08:05:35","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Feng Qiao","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPAC26H5.06","SPAC16A10.07c","SPAC19G12.13c","SPAC644.14c","SPBC1778.02","SPAC6F6.16c","SPCC188.07","SPAC3C7.03c"],"gene_count":9,"ltp_gene_count":4,"approved_date":"2015-11-20"},{"uniquename":"PMID:29618050","title":"Control of mRNA decapping by autoinhibition.","citation":"Nucleic Acids Res 2018 Jul 06;46(12):6318-6329","abstract":"5' mediated cytoplasmic RNA decay is a conserved cellular process in eukaryotes. While the functions of the structured core domains in this pathway are well-studied, the role of abundant intrinsically disordered regions (IDRs) is lacking. Here we reconstitute the Dcp1:Dcp2 complex containing a portion of the disordered C-terminus and show its activity is autoinhibited by linear interaction motifs. Enhancers of decapping (Edc) 1 and 3 cooperate to activate decapping by different mechanisms: Edc3 alleviates autoinhibition by binding IDRs and destabilizing an inactive form of the enzyme, whereas Edc1 stabilizes the transition state for catalysis. Both activators are required to fully stimulate an autoinhibited Dcp1:Dcp2 as Edc1 alone cannot overcome the decrease in activity attributed to the C-terminal extension. Our data provide a mechanistic framework for combinatorial control of decapping by protein cofactors, a principle that is likely conserved in multiple 5' mRNA decay pathways.","doi":"10.1093/nar/gky233","authors":"Paquette DR, Tibble RW, Daifuku TS, Gross JD","authors_abbrev":"Paquette DR et al.","pubmed_publication_date":"06 Jul 2018","pubmed_entrez_date":"2018-04-05","publication_year":"2018","canto_session_key":"326d36874fd21ffd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-07-31 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4473963","title":"Autolytic activities associated with conjugation and sporulation in fission yeast.","citation":"Arch Microbiol 1974;99(3):241-9","abstract":"","authors":"Kröning A, Egel R","authors_abbrev":"Kröning A et al.","pubmed_publication_date":"1974","pubmed_entrez_date":"1974-01-01","publication_year":"1974","canto_session_key":"7def9efd73cabe8c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-19 16:39:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-19 16:39:17","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-05-19"},{"uniquename":"PMID:26350316","title":"The Long Terminal Repeat Retrotransposons Tf1 and Tf2 of Schizosaccharomyces pombe.","citation":"Microbiol Spectr 2015 Aug;3(4)","abstract":"The long terminal repeat (LTR) retrotransposons Tf1 and Tf2 of Schizosaccharomyces pombe are active mobile elements of the Ty3/gypsy family. The mobilization of these retrotransposons depends on particle formation, reverse transcription and integration, processes typical of other LTR retrotransposons. However, Tf1 and Tf2 are distinct from other LTR elements in that they assemble virus-like particles from a single primary translation product, initiate reverse transcription with an unusual self-priming mechanism, and, in the case of Tf1, integrate with a pattern that favors specific promoters of RNA pol II-transcribed genes. To avoid the chromosome instability and genome damage that results from increased copy number, S. pombe applies a variety of defense mechanisms that restrict Tf1 and Tf2 activity. The mRNA of the Tf elements is eliminated by an exosome-based pathway when cells are in favorable conditions whereas nutrient deprivation triggers an RNA interference-dependent pathway that results in the heterochromatization of the elements. Interestingly, Tf1 integrates into the promoters of stress-induced genes and these insertions are capable of increasing the expression of adjacent genes. These properties of Tf1 transposition raise the possibility that Tf1 benefits cells with specific insertions by providing resistance to environmental stress.","doi":"10.1128/microbiolspec.MDNA3-0040-2014","authors":"Esnault C, Levin HL","authors_abbrev":"Esnault C et al.","pubmed_publication_date":"Aug 2015","pubmed_entrez_date":"2015-09-10","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-09-11 00:19:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11168594","title":"Transcription organization and mRNA levels of the genes for all 12 subunits of the fission yeast RNA polymerase II.","citation":"Genes Cells 2001 Jan;6(1):25-36","abstract":"The RNA polymerase II (Pol II) of eukaryotes is composed of 12 subunits, of which five are shared among Pol I, Pol II and Pol III. At present, however, little is known about the regulation of synthesis and assembly of the 12 Pol II subunits. To obtain an insight into the regulation of synthesis of these 12 Pol II subunits, Rpb1 to Rpb12, in the fission yeast Schizosaccharomyces pombe, we analysed the transcriptional organization of the rpb genes by use of the oligo capping method, and determined mRNA levels by quantitative competitive PCR assay. The intracellular concentrations of the 12 Rpb subunits in growing S. pombe cells are different, within a range of 15-fold difference between the least abundant Rpb3 and the most abundant Rpb12. The transcription of one group of genes including rpb3, rpb4, rpb5, rpb6, rpb7 and rpb10 is mainly initiated at a single site, while that of the other group of genes for rpb1, rpb2, rpb8, rpb9, rpb11 and rpb12 is initiated at multiple sites. The promoters of the first group of genes contain the TATA box sequence between -26 and -62, while the second group of genes carry TATA-less promoters. Several common sequence segments, tentatively designated 'Rpb motifs', were identified in the promoter regions of the rpb genes. Competitive PCR analysis indicated that mRNAs for Rpb1, Rpb3, Rpb7 and Rpb9 were among the group which had a low abundance, while the levels of Rpb6 and Rpb10 mRNAs were about fivefold, and that of Rpb2 mRNA was about 40-fold higher than the Rpb3 mRNA level. The levels of rpb mRNAs do not correlate with those of Rpb proteins. The protein-to-mRNA ratio or the translation efficiency is low for the rpb1, rpb2, rpb3 and rpb11 genes, encoding the homologues of subunits beta', beta, alpha and alpha, respectively, of the prokaryotic RNA polymerase core enzyme.","authors":"Sakurai H, Ishihama A","authors_abbrev":"Sakurai H et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-02-13","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2630561","title":"Dynamics of cytoplasmic organelles in the cell cycle of the fission yeast Schizosaccharomyces pombe: three-dimensional reconstruction from serial sections.","citation":"J Cell Sci 1989 Dec;94 ( Pt 4):647-56","abstract":"Changes in the ultrastructure of the fission yeast Schizosaccharomyces pombe during the cell division cycle were analyzed by three-dimensional reconstruction of serial section electron micrographs of freeze-substituted cells. Cytoplasmic vesicles were found at the cell ends during interphase and at the equatorial zone of cells undergoing cytokinesis. Filasomes behaved in a similar but temporally retarded way to vesicles. Microfilament(mf)-associated granules were found attached to the plasma membrane at the growing ends. Microfilaments were identified against the plasma membrane and adjacent to developing septa. From these observations it is suggested that mf-associated structures such as filasomes constitute dense knots of actin network that function in localized cell wall growth by controlling the deposition of cytoplasmic vesicles. Dictyosomes occur as tubular and fenestrated cisternae with associated cytoplasmic vesicles. They were distributed uniformly in the cytoplasm and did not change significantly during the cell cycle. Changes in the three-dimensional localization of cytoplasmic microtubules and mitochondria are also described.","authors":"Kanbe T, Kobayashi I, Tanaka K","authors_abbrev":"Kanbe T et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19430466","title":"The kinesin-14 Klp2 organizes microtubules into parallel bundles by an ATP-dependent sorting mechanism.","citation":"Nat Cell Biol 2009 Jun;11(6):724-30","abstract":"The dynamic organization of microtubules into parallel arrays allows interphase cells to set up multi-lane highways for intracellular transport and M-phase cells to build the mitotic and meiotic spindles. Here we show that a minimally reconstituted system composed of Klp2, a kinesin-14 from the fission yeast Schizosaccharomyces pombe, together with microtubules assembled from purified S. pombe tubulin, autonomously assembles bundles of parallel microtubules. Bundles form by an ATP-dependent sorting mechanism that requires the full-length Klp2 motor. By this mechanism, antiparallel-overlapped microtubules slide over one another until they dissociate from the bundles, whereas parallel-overlapped microtubules are selectively trapped by an energy-dissipating force-balance mechanism. Klp2-driven microtubule sorting provides a robust pathway for the organization of microtubules into parallel arrays. In vivo evidence indicates that Klp2 is required for the proper organization of S. pombe interphase microtubules into bipolar arrays of parallel-overlapped microtubules, suggesting that kinesin-14-dependent microtubule sorting may have wide biological importance.","doi":"10.1038/ncb1878","authors":"Braun M, Drummond DR, Cross RA, McAinsh AD","authors_abbrev":"Braun M et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-05-12","publication_year":"2009","canto_session_key":"e01fd0fde5718e3f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-30 18:31:50","canto_approved_date":"2018-01-30 18:31:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-26 16:10:30","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-01-30"},{"uniquename":"PMID:24291789","title":"Biochemical reconstitution of topological DNA binding by the cohesin ring.","citation":"Nature 2014 Jan 16;505(7483):367-71","abstract":"Cohesion between sister chromatids, mediated by the chromosomal cohesin complex, is a prerequisite for faithful chromosome segregation in mitosis. Cohesin also has vital roles in DNA repair and transcriptional regulation. The ring-shaped cohesin complex is thought to encircle sister DNA strands, but its molecular mechanism of action is poorly understood and the biochemical reconstitution of cohesin activity in vitro has remained an unattained goal. Here we reconstitute cohesin loading onto DNA using purified fission yeast cohesin and its loader complex, Mis4(Scc2)-Ssl3(Scc4) (Schizosaccharomyces pombe gene names appear throughout with their more commonly known Saccharomyces cerevisiae counterparts added in superscript). Incubation of cohesin with DNA leads to spontaneous topological loading, but this remains inefficient. The loader contacts cohesin at multiple sites around the ring circumference, including the hitherto enigmatic Psc3(Scc3) subunit, and stimulates cohesin's ATPase, resulting in efficient topological loading. The in vitro reconstitution of cohesin loading onto DNA provides mechanistic insight into the initial steps of the establishment of sister chromatid cohesion and other chromosomal processes mediated by cohesin.","doi":"10.1038/nature12867","authors":"Murayama Y, Uhlmann F","authors_abbrev":"Murayama Y et al.","pubmed_publication_date":"16 Jan 2014","pubmed_entrez_date":"2013-12-03","publication_year":"2014","canto_session_key":"711d04e89064d5c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Frank Uhlmann","canto_first_approved_date":"2017-03-15 14:25:31","canto_approved_date":"2024-11-04 13:50:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-29 16:53:02","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Frank Uhlmann","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAC17H9.20","SPAC31A2.05c","SPAC10F6.09c","SPAC1687.18c","SPBC29A10.04"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-03-15"},{"uniquename":"PMID:23322785","title":"The fission yeast minichromosome maintenance (MCM)-binding protein (MCM-BP), Mcb1, regulates MCM function during prereplicative complex formation in DNA replication.","citation":"J Biol Chem 2013 Mar 08;288(10):6864-80","abstract":"The minichromosome maintenance (MCM) complex is a replicative helicase, which is essential for chromosome DNA replication. In recent years, the identification of a novel MCM-binding protein (MCM-BP) in most eukaryotes has led to numerous studies investigating its function and its relationship to the MCM complex. However, the mechanisms by which MCM-BP functions and associates with MCM complexes are not well understood; in addition, the functional role of MCM-BP remains controversial and may vary between model organisms. The present study aims to elucidate the nature and biological function of the MCM-BP ortholog, Mcb1, in fission yeast. The Mcb1 protein continuously interacts with MCM proteins during the cell cycle in vivo and can interact with any individual MCM subunit in vitro. To understand the detailed characteristics of mcb1(+), two temperature-sensitive mcb1 gene mutants (mcb1(ts)) were isolated. Extensive genetic analysis showed that the mcb1(ts) mutants were suppressed by a mcm5(+) multicopy plasmid and displayed synthetic defects with many S-phase-related gene mutants. Moreover, cyclin-dependent kinase modulation by Cig2 repression or Rum1 overproduction suppressed the mcb1(ts) mutants, suggesting the involvement of Mcb1 in pre-RC formation during DNA replication. These data are consistent with the observation that Mcm7 loading onto replication origins is reduced and S-phase progression is delayed in mcb1(ts) mutants. Furthermore, the mcb1(ts) mutation led to the redistribution of MCM subunits to the cytoplasm, and this redistribution was dependent on an active nuclear export system. These results strongly suggest that Mcb1 promotes efficient pre-RC formation during DNA replication by regulating the MCM complex.","doi":"10.1074/jbc.M112.432393","authors":"Santosa V, Martha S, Hirose N, Tanaka K","authors_abbrev":"Santosa V et al.","pubmed_publication_date":"08 Mar 2013","pubmed_entrez_date":"2013-01-17","publication_year":"2013","canto_session_key":"633557cb6cc412dc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB2B4.03","SPCC16A11.17","SPCC1795.11","SPAC1B2.05","SPBC336.04","SPBC646.14c","SPBC1347.10","SPBC32F12.09","SPBC211.04c","SPAC23C4.18c","SPCC18B5.11c","SPCC1259.13","SPAC1687.04","SPBC25D12.03c","SPBC776.12c","SPAC1805.17","SPAC3H5.06c","SPBC4.04c","SPBC29A10.15","SPCC1682.02c","SPBC216.05","SPAC17D4.02","SPBC1734.02c"],"gene_count":23,"ltp_gene_count":23},{"uniquename":"PMID:2679933","title":"Fission yeast.","citation":"Biotechnology 1989;13:53-64","abstract":"","authors":"Yamamoto M","authors_abbrev":"Yamamoto M","pubmed_publication_date":"1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14674689","title":"Functional analysis of amino acids of the Na+/H+ exchanger that are important for proton translocation.","citation":"Mol Cell Biochem 2003 Dec;254(1-2):117-24","abstract":"The Na+/H+ exchanger is an integral membrane protein found in the plasma membrane of eukaryotic and prokaryotic cells. In eukaryotes it functions to exchange one proton for a sodium ion. In mammals it removes intracellular protons while in plants and fungal cells the plasma membrane form removes intracellular sodium in exchange for extracellular protons. In this study we used the Na+/H+ exchanger of Schizosaccharomyces pombe (Sod2) as a model system to study amino acids critical for activity of the protein. Twelve mutant forms of the Na+/H+ exchanger were examined for their ability to translocate protons as assessed by a Cytosensor microphysiometer. Mutation of the amino acid Histidine 367 resulted in defective proton translocation. The acidic residues Asp145, Asp178, Asp266 and Asp267 were important in the proton translocation activity of the Na+/H+ exchanger. Mutation of amino acids His98, His233 and Asp241 did not significantly impair proton translocation by the Na+/H+ exchanger. These results confirm that polar amino acids are important in proton flux activity of Na+/H+ exchangers.","authors":"Wiebe CA, Rieder C, Young PG, Dibrov P, Fliegel L","authors_abbrev":"Wiebe CA et al.","pubmed_publication_date":"Dec 2003","pubmed_entrez_date":"2003-12-17","publication_year":"2003","canto_session_key":"cd4a6de179174568","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-11 09:09:52","canto_approved_date":"2022-06-14 15:31:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-11 09:09:26","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-12-11"},{"uniquename":"PMID:20444689","title":"Methylation of ribosomal protein L42 regulates ribosomal function and stress-adapted cell growth.","citation":"J Biol Chem 2010 Jul 16;285(29):22448-60","abstract":"Lysine methylation is one of the most common protein modifications. Although lysine methylation of histones has been extensively studied and linked to gene regulation, that of non-histone proteins remains incompletely understood. Here, we show a novel regulatory role of ribosomal protein methylation. Using an in vitro methyltransferase assay, we found that Schizosaccharomyces pombe Set13, a SET domain protein encoded by SPAC688.14, specifically methylates lysine 55 of ribosomal protein L42 (Rpl42). Mass spectrometric analysis revealed that endogenous Rpl42 is monomethylated at lysine 55 in wild-type S. pombe cells and that the methylation is lost in Delta set13 mutant cells. Delta set13 and Rpl42 methylation-deficient mutant S. pombe cells showed higher cycloheximide sensitivity and defects in stress-responsive growth control compared with wild type. Genetic analyses suggested that the abnormal growth phenotype was distinct from the conserved stress-responsive pathway that modulates translation initiation. Furthermore, the Rpl42 methylation-deficient mutant cells showed a reduced ability to survive after entering stationary phase. These results suggest that Rpl42 methylation plays direct roles in ribosomal function and cell proliferation control independently of the general stress-response pathway.","doi":"10.1074/jbc.M110.132274","authors":"Shirai A, Sadaie M, Shinmyozu K, Nakayama J","authors_abbrev":"Shirai A et al.","pubmed_publication_date":"16 Jul 2010","pubmed_entrez_date":"2010-05-07","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC15E1.03","SPAC688.14","SPBC36B7.09"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:21075050","title":"New insights into galactose metabolism by Schizosaccharomyces pombe: isolation and characterization of a galactose-assimilating mutant.","citation":"J Biosci Bioeng 2011 Feb;111(2):158-66","abstract":"The fission yeast Schizosaccharomyces pombe cannot use galactose as a carbon or energy source, and little is known about galactose metabolism in this species. Here we report isolation of a galactose-assimilating mutant that grows on a medium containing galactose as a sole carbon source through use of a proofreading-deficient DNA polymerase δ variant encoded by cdc6-1. Based on comparative analysis of gene expression profiles in the wild-type and the mutant (FG2-8), we found that SPBPB2B2.10c (gal7+), SPBPB2B2.12c (gal10+) and SPBPB2B2.13 (gal1+), homologous to Saccharomyces cerevisiae GAL7, GAL10 and GAL1, respectively, and SPBPB2B2.08, SPBPB2B2.09c, and SPBPB2B2.11 that localize close to the gal genes, were highly expressed and dramatically induced by addition of galactose. The gal7Δ strain, carrying an integrated ura4+ marker at the gal7+ locus, grew on 5-fluoroorotic acid (5-FOA)-containing medium. In contrast, the FG2-8 gal7Δ strain could not grow on 5-FOA medium. In addition, expression of gal7+, SPBPB2B2.13, gal10+ and gal1+ genes increased in the wild-type strain when carried on a vector, and these transformants grew on galactose medium. We suggest that gal7+, gal10+, and gal1+ are localized close to a chromosomal terminal repressed by gene silencing in S. pombe. In contrast, gene silencing was defective in the FG2-8 strain making galactose assimilation possible.","doi":"10.1016/j.jbiosc.2010.10.007","authors":"Matsuzawa T, Fujita Y, Tanaka N, Tohda H, Itadani A, Takegawa K","authors_abbrev":"Matsuzawa T et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2010-11-16","publication_year":"2011","canto_session_key":"b05ad3bfefc1de38","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2015-07-23 09:55:10","canto_approved_date":"2025-02-12 09:05:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-23 09:53:21","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPB2B2.10c","SPBPB2B2.11","SPBPB2B2.08","SPAC664.01c","SPBPB2B2.12c","SPBPB2B2.13","SPBPB2B2.09c"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2015-07-23"},{"uniquename":"PMID:24498240","title":"Rho1 GTPase and PKC ortholog Pck1 are upstream activators of the cell integrity MAPK pathway in fission yeast.","citation":"PLoS One 2014;9(1):e88020","abstract":"In the fission yeast Schizosaccharomyces pombe the cell integrity pathway (CIP) orchestrates multiple biological processes like cell wall maintenance and ionic homeostasis by fine tuning activation of MAPK Pmk1 in response to various environmental conditions. The small GTPase Rho2 positively regulates the CIP through protein kinase C ortholog Pck2. However, Pmk1 retains some function in mutants lacking either Rho2 or Pck2, suggesting the existence of additional upstream regulatory elements to modulate its activity depending on the nature of the environmental stimulus. The essential GTPase Rho1 is a candidate to control the activity of the CIP by acting upstream of Pck2, whereas Pck1, a second PKC ortholog, appears to negatively regulate Pmk1 activity. However, the exact regulatory nature of these two proteins within the CIP has remained elusive. By exhaustive characterization of strains expressing a hypomorphic Rho1 allele (rho1-596) in different genetic backgrounds we show that both Rho1 and Pck1 are positive upstream regulatory members of the CIP in addition to Rho2 and Pck2. In this new model Rho1 and Rho2 control Pmk1 basal activity during vegetative growth mainly through Pck2. Notably, whereas Rho2-Pck2 elicit Pmk1 activation in response to most environmental stimuli, Rho1 drives Pmk1 activation through either Pck2 or Pck1 exclusively in response to cell wall damage. Our study reveals the intricate and complex functional architecture of the upstream elements participating in this signaling pathway as compared to similar routes from other simple eukaryotic organisms.","doi":"10.1371/journal.pone.0088020","authors":"Sánchez-Mir L, Soto T, Franco A, Madrid M, Viana RA, Vicente J, Gacto M, Pérez P, Cansado J","authors_abbrev":"Sánchez-Mir L et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-06","publication_year":"2014","canto_session_key":"760045d7bb2de1aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jose Cansado","canto_first_approved_date":"2024-07-05 08:37:26","canto_approved_date":"2024-10-26 07:33:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-03 12:52:15","canto_added_date":"2014-02-16 05:46:49","annotation_curators":[{"name":"Jose Cansado","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.08","SPAC17G8.14c","SPAC16.01","SPAC1F3.02c","SPBC12D12.04c","SPAC1F7.04"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2024-07-05"},{"uniquename":"PMID:25837586","title":"Spontaneous Cdc42 polarization independent of GDI-mediated extraction and actin-based trafficking.","citation":"PLoS Biol 2015 Apr;13(4):e1002097","abstract":"The small Rho-family GTPase Cdc42 is critical for cell polarization and polarizes spontaneously in absence of upstream spatial cues. Spontaneous polarization is thought to require dynamic Cdc42 recycling through Guanine nucleotide Dissociation Inhibitor (GDI)-mediated membrane extraction and vesicle trafficking. Here, we describe a functional fluorescent Cdc42 allele in fission yeast, which demonstrates Cdc42 dynamics and polarization independent of these pathways. Furthermore, an engineered Cdc42 allele targeted to the membrane independently of these recycling pathways by an amphipathic helix is viable and polarizes spontaneously to multiple sites in fission and budding yeasts. We show that Cdc42 is highly mobile at the membrane and accumulates at sites of activity, where it displays slower mobility. By contrast, a near-immobile transmembrane domain-containing Cdc42 allele supports viability and polarized activity, but does not accumulate at sites of activity. We propose that Cdc42 activation, enhanced by positive feedback, leads to its local accumulation by capture of fast-diffusing inactive molecules.","doi":"10.1371/journal.pbio.1002097","authors":"Bendezú FO, Vincenzetti V, Vavylonis D, Wyss R, Vogel H, Martin SG","authors_abbrev":"Bendezú FO et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-04-04","publication_year":"2015","canto_session_key":"8c5b305baa755d41","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2018-03-19 16:53:51","canto_approved_date":"2026-02-17 15:40:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-10 15:36:01","canto_added_date":"2015-04-05 00:19:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.14c","SPAC16E8.09","SPBC1706.01","SPAC6F12.06","SPAC24H6.09","SPAC688.11","SPCC895.05","SPAC110.03","SPBC336.12c","SPAC22H10.07","SPCC1223.06"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2018-03-19"},{"uniquename":"PMID:8467814","title":"Characterization of the fission yeast mcs2 cyclin and its associated protein kinase activity.","citation":"EMBO J 1993 Apr;12(4):1723-32","abstract":"We have previously described the isolation of mcs2-75, a mutation obtained as an allele-specific suppressor of a dominant allele of cdc2. mcs2 was cloned and determined to be an essential gene, the product of which shares homology with the cyclin family of proteins. In contrast to the behavior of some, but not all cyclins, the mcs2 protein is constant in its abundance and localization throughout the cell cycle. A kinase activity that co-precipitates with mcs2 can be detected when myelin basic protein (MBP) is provided as an exogenous substrate. This kinase activity is constant throughout the cell cycle. mcs2 does not appear to associate with the cdc2 protein kinase or an antigenically related kinase. Finally, a protein kinase termed csk1 (cyclin suppressing kinase) was isolated as a high copy suppressor of an mcs2 mutation. csk1 is not essential, however, the level of kinase activity that co-precipitates with mcs2 is reduced approximately 3-fold in strains harboring a csk1 null allele. Therefore, csk1 may encode a protein kinase physically associated with mcs2 or alternatively may function as an upstream activator of the mcs2-associated kinase.","authors":"Molz L, Beach D","authors_abbrev":"Molz L et al.","pubmed_publication_date":"Apr 1993","pubmed_entrez_date":"1993-04-01","publication_year":"1993","canto_session_key":"f3f7dbc4ff7e57ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-09 09:55:11","canto_approved_date":"2021-02-11 22:10:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-08 12:51:18","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.06c","SPBP16F5.02","SPBC11B10.09","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-06-09"},{"uniquename":"PMID:1461727","title":"Detection and characterization of a ring chromosome in the fission yeast Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1992 Nov 25;20(22):5943-5","abstract":"NotI and SfiI genomic restriction maps were used to detect and characterize a ring chromosome II in a Schizosaccharomyces pombe strain with a meiotic defect on chromosome II. The ring chromosome was formed by an intrachromosomal fusion near, or at, the very ends of chromosome II.","authors":"Fan JB, Rochet M, Gaillardin C, Smith CL","authors_abbrev":"Fan JB et al.","pubmed_publication_date":"25 Nov 1992","pubmed_entrez_date":"1992-11-25","publication_year":"1992","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37275474","title":"Atg1, a key regulator of autophagy, functions to promote MAPK activation and cell death upon calcium overload in fission yeast.","citation":"Microb Cell 2023 Jun 05;10(6):133-140","abstract":"Autophagy promotes or inhibits cell death depending on the environment and cell type. Our previous findings suggested that Atg1 is genetically involved in the regulation of Pmk1 MAPK in fission yeast. Here, we showed that Δ atg1  displays lower levels of Pmk1 MAPK phosphorylation than did the wild-type (WT) cells upon treatment with a 1,3-β-D-glucan synthase inhibitor micafungin or CaCl 2 , both of which activate Pmk1. Moreover, the overproduction of Atg1, but not that of the kinase inactivating Atg1 D193A  activates Pmk1 without any extracellular stimuli, suggesting that Atg1 may promote Pmk1 MAPK signaling activation. Notably, the overproduction of Atg1 induces a toxic effect on the growth of WT cells and the deletion of Pmk1 failed to suppress the cell death induced by Atg1, indicating that the Atg1-mediated cell death requires additional mechanism(s) other than Pmk1 activation. Moreover,  atg1  gene deletion induces tolerance to micafungin and CaCl 2 , whereas  pmk1  deletion induces severe sensitivities to these compounds. The Δ atg1 Δ pmk1  double mutants display intermediate sensitivities to these compounds, showing that  atg1  deletion partly suppressed growth inhibition induced by Δ pmk1 . Thus, Atg1 may act to promote cell death upon micafungin and CaCl 2  stimuli regardless of Pmk1 MAPK activity. Since micafungin and CaCl 2  are intracellular calcium inducers, our data reveal a novel role of the autophagy regulator Atg1 to induce cell death upon calcium overload independent of its role in Pmk1 MAPK activation.","doi":"10.15698/mic2023.06.798","authors":"Takasaki T, Utsumi R, Shimada E, Bamba A, Hagihara K, Satoh R, Sugiura R","authors_abbrev":"Takasaki T et al.","pubmed_publication_date":"05 Jun 2023","pubmed_entrez_date":"2023-06-05","publication_year":"2023","canto_session_key":"37c367b793fded41","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-06-06 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42330073","title":"A point mutation in the FAT domain constitutively increases the kinase activity of Rad3ATR and bypasses the requirement for 9-1-1 phosphorylation to activate the DNA replication checkpoint.","citation":"PLoS Genet 2026 Jun 22;22(6):e1012213","abstract":"Ataxia telangiectasia and Rad3-related (ATR) initiates cell cycle checkpoints to maintain genome integrity in the presence of replication stress or various forms of DNA damage. However, how ATR is activated for checkpoint initiation remains incompletely understood. The canonical model suggests that binding of an ATR-activator protein relieves the autoinhibitory PIKK regulatory domain (PRD) within the kinase domain, thereby activating ATR by granting substrate access to the catalytic centre. To better understand the checkpoint initiation mechanism, we conducted a genetic screen in fission yeast that identified a charge-reversal mutation, E1369K, in the conserved FRAP-ATM-TRRAP (FAT) domain of Rad3, the ortholog of ATR. In vitro kinase assays show that the mutation converts Rad3 into a constitutively active form. This allows rescue of the Rad3 kinase signaling defect in cells lacking the phosphorylation of the Rad9-Rad1-Hus1 (9-1-1) complex specifically in the DNA replication checkpoint, not the damage checkpoint pathway. Since the mutation is not in the kinase domain and is away from the PRD, these findings show that, in addition to the canonical mechanism, Rad3 may also be activated allosterically via the FAT domain, a mechanism likely conserved in higher eukaryotes.","doi":"10.1371/journal.pgen.1012213","authors":"Dev K, Rider SD, Singh B, Saini A, Xu YJ","authors_abbrev":"Dev K et al.","pubmed_publication_date":"22 Jun 2026","pubmed_entrez_date":"2026-06-22","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-22 23:25:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11255254","title":"Construction of FLAG and histidine tagging vectors for Schizosaccharomyces pombe.","citation":"Yeast 2001 Mar 30;18(5):463-8","abstract":"Schizosaccharomyces pombe is becoming an increasingly popular model system for investigating important cellular processes. To facilitate detection, purification and functional studies of Sz. pombe gene products, we constructed two tagging expression vectors for use in Sz. pombe. These vectors allow proteins to be expressed ectopically as fusion proteins with a FLAG epitope and six histidine residue tags attached to their N-terminus or C-terminus. The function and applicability of these vectors were examined and the results are shown using the N-terminal tagging vector encoding Sfc6p, a subunit of the Sz. pombe RNA polymerase III general transcription factor, TFIIIC.","authors":"Huang Y, Hamada M, Patel J, Maraia RJ","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"30 Mar 2001","pubmed_entrez_date":"2001-03-20","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15281132","title":"Function-dependent clustering of orthologues and paralogues of cyclophilins.","citation":"Proteins 2004 Sep 01;56(4):808-20","abstract":"The 18 kDa archetypal cyclosporin-A binding protein, cyclophilin-A, has multiple paralogues in the human genome. Only 18 of those paralogues have been detected as mRNAs or proteins whose masses vary from 18 to 354 kDa, whereas the functional significance of the open reading frames (ORFs) encoding other paralogues of cyclophilin-A remains unknown. The genomes of Drosophila melanogaster, Caenorhabditis elegans, Arabidopsis thaliana, Schizosaccharomyces pombe, and Saccharomyces cerevisiae encode different numbers of the cyclophilin paralogues, some of which are orthologous to the human cyclophilins. A library of novel algorithms was developed and used for computation of the conservation levels for hydrophobicity and bulkiness profiles, and amino acid compositions (AACs) of 303 aligned sequences of cyclophilins. The majority of the paralogues and orthologues encoded in these 6 genomes differ considerably from each other. Some of the orthologues and paralogues have high correlation coefficients (CCFs) for pairwise compared hydrophobicity and bulkiness profiles, and whose AACs differ to a low degree. Convergence of these three properties of the polypeptide chain and apparent conservation of the typical sequence hallmarks and parameters allowed for the clustering of the functionally related orthologues and paralogues of the cyclophilins. The clustering method allowed for sorting out the cyclophilins into several distinct classes. Analyses of the overlapping clusters of sequences permitted delineation of some hypothetical pathways that might have led to the creation of certain paralogues of cyclophilins in the eukaryotic genomes.","authors":"Galat A","authors_abbrev":"Galat A","pubmed_publication_date":"01 Sep 2004","pubmed_entrez_date":"2004-07-29","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15210864","title":"Mcp7, a meiosis-specific coiled-coil protein of fission yeast, associates with Meu13 and is required for meiotic recombination.","citation":"Nucleic Acids Res 2004;32(11):3325-39","abstract":"We previously showed that Meu13 of Schizosaccharomyces pombe functions in homologous pairing and recombination at meiosis I. Here we show that a meiosis-specific gene encodes a coiled-coil protein that complexes with Meu13 during meiosis in vivo. This gene denoted as mcp7+ (after meiotic coiled-coil protein) is an ortholog of Mnd1 of Saccharomyces cerevisiae. Mcp7 proteins are detected on meiotic chromatin. The phenotypes of mcp7Delta cells are similar to those of meu13Delta cells as they show reduced recombination rates and spore viability and produce spores with abnormal morphology. However, a delay in initiation of meiosis I chromosome segregation of mcp7Delta cells is not so conspicuous as meu13Delta cells, and no meiotic delay is observed in mcp7Deltameu13Delta cells. Mcp7 and Meu13 proteins depend on each other differently; Mcp7 becomes more stable in meu13Delta cells, whereas Meu13 becomes less stable in mcp7Delta cells. Genetic analysis shows that Mcp7 acts in the downstream of Dmc1, homologs of Escherichia coli RecA protein, for both recombination and subsequent sporulation. Taken together, we conclude that Mcp7 associates with Meu13 and together they play a key role in meiotic recombination.","authors":"Saito TT, Tougan T, Kasama T, Okuzaki D, Nojima H","authors_abbrev":"Saito TT et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-06-24","publication_year":"2004","canto_session_key":"6344b68037683a3b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-23 14:11:35","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-23 14:11:27","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":37,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13A11.03","SPAC8E11.03c","SPAC17A5.11","SPAC14C4.13","SPAC222.15"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-10-23"},{"uniquename":"PMID:31784357","title":"Native Chromatin Proteomics Reveals a Role for Specific Nucleoporins in Heterochromatin Organization and Maintenance.","citation":"Mol Cell 2020 Jan 02;77(1):51-66.e8","abstract":"Spatially and functionally distinct domains of heterochromatin and euchromatin play important roles in the maintenance of chromosome stability and regulation of gene expression, but a comprehensive knowledge of their composition is lacking. Here, we develop a strategy for the isolation of native Schizosaccharomyces pombe heterochromatin and euchromatin fragments and analyze their composition by using quantitative mass spectrometry. The shared and euchromatin-specific proteomes contain proteins involved in DNA and chromatin metabolism and in transcription, respectively. The heterochromatin-specific proteome includes all proteins with known roles in heterochromatin formation and, in addition, is enriched for subsets of nucleoporins and inner nuclear membrane (INM) proteins, which associate with different chromatin domains. While the INM proteins are required for the integrity of the nucleolus, containing ribosomal DNA repeats, the nucleoporins are required for aggregation of heterochromatic foci and epigenetic inheritance. The results provide a comprehensive picture of heterochromatin-associated proteins and suggest a role for specific nucleoporins in heterochromatin function.","doi":"10.1016/j.molcel.2019.10.018","authors":"Iglesias N, Paulo JA, Tatarakis A, Wang X, Edwards AL, Bhanu NV, Garcia BA, Haas W, Gygi SP, Moazed D","authors_abbrev":"Iglesias N et al.","pubmed_publication_date":"02 Jan 2020","pubmed_entrez_date":"2019-12-01","publication_year":"2020","canto_session_key":"c64f8844d5e0c730","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-12-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c","SPAC664.01c","SPCC1450.02"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:37979174","title":"Reticulons bind sphingolipids to activate the endoplasmic reticulum cell cycle checkpoint, the ER surveillance pathway.","citation":"Cell Rep 2023 Dec 26;42(12):113403","abstract":"The inheritance of a functional endoplasmic reticulum (ER) is ensured by the ER stress surveillance (ERSU) pathway. Here, we made the unexpected discovery that reticulon 1 (Rtn1) and Yop1, well-known ER-curvature-generating proteins, each possess two sphingolipid-binding motifs within their transmembrane domains and that these motifs recognize the ER-stress-induced sphingolipid phytosphingosine (PHS), resulting in an ER inheritance block. Upon binding PHS, Rtn1/Yop1 accumulate on the ER tubule, poised to enter the emerging daughter cell, and cause its misdirection to the bud scars (i.e., previous cell division sites). Amino acid changes in the conserved PHS-binding motifs preclude Rtn1 or Yop1 from binding PHS and diminish their enrichment on the tubular ER, ultimately preventing the ER-stress-induced inheritance block. Conservation of these sphingolipid-binding motifs in human reticulons suggests that sphingolipid binding to Rtn1 and Yop1 represents an evolutionarily conserved mechanism that enables cells to respond to ER stress.","doi":"10.1016/j.celrep.2023.113403","authors":"Piña F, Yan B, Hu J, Niwa M","authors_abbrev":"Piña F et al.","pubmed_publication_date":"26 Dec 2023","pubmed_entrez_date":"2023-11-18","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC31A8.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8978030","title":"Identification of residues in fission yeast and human p34cdc2 required for S-M checkpoint control.","citation":"Genetics 1996 Dec;144(4):1413-24","abstract":"In fission yeast, regulation of p34cdc2 plays an important role in the checkpoint coupling mitosis to completion of DNA replication. The cdc2 mutations cdc2-3w (C67Y) and cdc2-4w (C67F) abolish checkpoint control without seriously affecting normal cell proliferation. However the molecular basis of this phenotype is not known. To better understand the role of p34cdc2 in checkpoint control, we have screened for more mutations in Schizosaccharomyces pombe cdc2 with this phenotype. We have isolated cdc2-3w and cdc2-4w, as well as three new cdc2 alleles: cdc2-6w (N66I), cdc2-7w (E8V) and cdc2-8w (K9E). The altered residues map to two different regions on opposite faces of the protein, suggesting that the interaction between p34cdc2 and components of the checkpoint pathway may be complex. In contrast to cdc2-3w and cdc2-4w, the new mutations alter residues that are conserved between the fission yeast cdc2+ and other cdks, including the human CDC2 protein. Expression of the equivalent human CDC2 mutants in fission yeast abolishes checkpoint control, suggesting that these residues could be involved in checkpoint-dependent regulation of other eukaryotic cdks.","authors":"Basi G, Enoch T","authors_abbrev":"Basi G et al.","pubmed_publication_date":"Dec 1996","pubmed_entrez_date":"1996-12-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31165882","title":"Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity.","citation":"Nucleic Acids Res 2019 Jul 26;47(13):6726-6736","abstract":"Heterochromatin is a distinctive chromatin structure that is essential for chromosome segregation, genome stability and regulation of gene expression. H3K9 methylation (H3K9me), a hallmark of heterochromatin, is deposited by the Su(var)3-9 family of proteins; however, the mechanism by which H3K9 methyltransferases bind and methylate the nucleosome is poorly understood. In this work we determined the interaction of Clr4, the fission yeast H3K9 methyltransferase, with nucleosomes using nuclear magnetic resonance, biochemical and genetic assays. Our study shows that the Clr4 chromodomain binds the H3K9me3 tail and that both, the chromodomain and the disordered region connecting the chromodomain and the SET domain, bind the nucleosome core. We show that interaction of the disordered region with the nucleosome core is independent of H3K9me and contributes to H3K9me in vitro and in vivo. Moreover, we show that those interactions with the nucleosome core are contributing to de novo deposition of H3K9me and to establishment of heterochromatin.","doi":"10.1093/nar/gkz480","authors":"Akoury E, Ma G, Demolin S, Brönner C, Zocco M, Cirilo A, Ivic N, Halic M","authors_abbrev":"Akoury E et al.","pubmed_publication_date":"26 Jul 2019","pubmed_entrez_date":"2019-06-06","publication_year":"2019","canto_session_key":"5d4773961b0ebfd5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-06-07 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22086920","title":"Yeast sterol regulatory element-binding protein (SREBP) cleavage requires Cdc48 and Dsc5, a ubiquitin regulatory X domain-containing subunit of the Golgi Dsc E3 ligase.","citation":"J Biol Chem 2012 Jan 02;287(1):672-681","abstract":"Schizosaccharomyces pombe Sre1 is a membrane-bound transcription factor that controls adaptation to hypoxia. Like its mammalian homolog, sterol regulatory element-binding protein (SREBP), Sre1 activation requires release from the membrane. However, in fission yeast, this release occurs through a strikingly different mechanism that requires the Golgi Dsc E3 ubiquitin ligase complex and the proteasome. The mechanistic details of Sre1 cleavage, including the link between the Dsc E3 ligase complex and proteasome, are not well understood. Here, we present results of a genetic selection designed to identify additional components required for Sre1 cleavage. From the selection, we identified two new components of the fission yeast SREBP pathway: Dsc5 and Cdc48. The AAA (ATPase associated with diverse cellular activities) ATPase Cdc48 and Dsc5, a ubiquitin regulatory X domain-containing protein, interact with known Dsc complex components and are required for SREBP cleavage. These findings provide a mechanistic link between the Dsc E3 ligase complex and the proteasome in SREBP cleavage and add to a growing list of similarities between the Dsc E3 ligase and membrane E3 ligases involved in endoplasmic reticulum-associated degradation.","doi":"10.1074/jbc.M111.317370","authors":"Stewart EV, Lloyd SJ, Burg JS, Nwosu CC, Lintner RE, Daza R, Russ C, Ponchner K, Nusbaum C, Espenshade PJ","authors_abbrev":"Stewart EV et al.","pubmed_publication_date":"02 Jan 2012","pubmed_entrez_date":"2011-11-17","publication_year":"2012","canto_session_key":"dcad060c8a9084fc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2024-06-12 07:23:27","canto_approved_date":"2025-09-15 08:13:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 07:23:18","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Peter Espenshade","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.15c","SPAC20H4.02","SPBC19C2.09","SPBC947.10","SPAC1565.08","SPCC285.11","SPAC4D7.11","SPAC1486.02c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2024-06-12"},{"uniquename":"PMID:29502950","title":"Equatorial Assembly of the Cell-Division Actomyosin Ring in the Absence of Cytokinetic Spatial Cues.","citation":"Curr Biol 2018 Mar 19;28(6):955-962.e3","abstract":"The position of the division site dictates the size and fate of daughter cells in many organisms. In animal cells, division-site placement involves overlapping mechanisms, including signaling from the central spindle microtubules, astral microtubules, and spindle poles and through polar contractions [1-3]. In fission yeast, division-site positioning requires overlapping mechanisms involving the anillin-related protein Mid1 and the tip complex (comprising the Kelch-repeat protein Tea1, the Dyrk-kinase Pom1, and the SH3-domain protein Tea4) [4-11]. In addition to these factors, cell shape has also been shown to participate in the maintenance of the position of the actomyosin ring [12-14]. The first principles guiding actomyosin ring placement, however, have not been elucidated in any organism. Because actomyosin ring positioning, ring assembly, and cell morphogenesis are genetically separable in fission yeast, we have used it to derive actomyosin ring placement mechanisms from first principles. We report that, during ring assembly in the absence of cytokinetic cues (anillin-related Mid1 and tip-complex proteins), actin bundles follow the path of least curvature and assemble actomyosin rings in an equatorial position in spherical protoplasts and along the long axis in cylindrical cells and compressed protoplasts. The equatorial position of rings is abolished upon treatment of protoplasts with an actin-severing compound or by slowing down actin polymerization. We propose that the physical properties of actin filaments/bundles play key roles in actomyosin ring assembly and positioning, and that key cytokinetic molecules may modulate the length of actin filaments to promote ring assembly along the short axis.","doi":"10.1016/j.cub.2018.01.088","authors":"Lim TC, Hatano T, Kamnev A, Balasubramanian MK, Chew TG","authors_abbrev":"Lim TC et al.","pubmed_publication_date":"19 Mar 2018","pubmed_entrez_date":"2018-03-06","publication_year":"2018","canto_session_key":"695a769fbfafe217","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-03-07 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB017605","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011609","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:499357","title":"Cell division in yeasts. III. The biased, asymmetric location of the septum in the fission yeast cell, Schizosaccharomyces pombe.","citation":"Exp Cell Res 1979 Oct 15;123(2):253-9","abstract":"","authors":"Johnson BF, Calleja GB, Boisclair I, Yoo BY","authors_abbrev":"Johnson BF et al.","pubmed_publication_date":"15 Oct 1979","pubmed_entrez_date":"1979-10-15","publication_year":"1979","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40193710","title":"An enzymatic-independent function of palmitoyl hydrolase in cohesin loading onto chromosome.","citation":"Nucleic Acids Res 2025 Mar 20;53(6)","abstract":"Sister chromatid cohesion is mediated by a conserved multiprotein complex called cohesin. The loading of cohesin onto chromosomes involves the RSC (remodels the structure of chromatin) chromatin remodeling complex. Here, we demonstrate that the fission yeast Phi1, a palmitoyl hydrolase inactive protein 1, serves to bridge the interaction between cohesin and the RSC complex. Phi1 interacts with Rad21 in cohesin and Snf21, the RSC complex ATPase, to promote chromosome loading of cohesin. The identified characteristic features of Phi1 are conserved in the human homologues Apt1 and Apt2, which interact with Rad21 and Brg1, the human homologue of Snf21, in an enzymatic-independent manner. Intriguingly, the cohesin-Apt1-Brg1 complex is upregulated in C4-2B prostate cancer cells, and co-depletion of Apt1 and Apt2 by small interfering RNA triggers mitotic catastrophe in these cells. In addition, Apt1 nuclear localization is associated with poor clinical outcomes in prostate cancer. These results suggest a pro-survival function against mitotic stress for the complex.","doi":"10.1093/nar/gkaf257","authors":"Wang YT, Hsiao WY, Pham TV, Huang BR, Yeh SD, Hsu EC, Wang SW","authors_abbrev":"Wang YT et al.","pubmed_publication_date":"20 Mar 2025","pubmed_entrez_date":"2025-04-07","publication_year":"2025","canto_session_key":"33e4f8032d381a85","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shao-Win Wang","canto_first_approved_date":"2025-04-14 10:50:54","canto_approved_date":"2025-04-14 10:50:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-11 05:47:00","canto_added_date":"2025-04-07 23:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":22,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Shao-Win Wang","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAC664.01c","SPBC20F10.06","SPAC1250.01","SPCC663.12","SPCC1322.12c","SPAC9G1.08c","SPAC8E11.04c","SPAC1687.18c","SPAC31A2.05c"],"gene_count":10,"ltp_gene_count":5,"approved_date":"2025-04-14"},{"uniquename":"EMBL:AU007277","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008160","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:977546","title":"Temperature-sensitive mutant of Schizosaccharomyces pombe exhibiting enhanced radiation sensitivity.","citation":"J Bacteriol 1976 Nov;128(2):536-9","abstract":"A conditional lethal and radiation-sensitive mutant of Schizosaccharomyces pombe is described in which both characteristics result from a single gene mutation. Confirmation of the pleiotropic nature of this mutant was obtained by tetrad analysis and by testing the radiation sensitivity of a large number of revertants that grew normally at the restrictive temperature. The colony-forming ability of the mutant after ultraviolet radiation, gamma radiation, and ethyl methane sulfonate treatment is considerably altered by the post-treatment incubation temperature, showing higher survival at 25 than at 30degreesC. The radiosensitivity of the mutant is also influenced by the stage of growth. The difference in radiation sensitivity between the wild type and mutant is greater when log-phase cultures are compared. The characteristics of this mutant suggest that it is defective in a step common to both deoxyribonucleic acid replication and repair.","authors":"Duck P, Nasim A, James AP","authors_abbrev":"Duck P et al.","pubmed_publication_date":"Nov 1976","pubmed_entrez_date":"1976-11-01","publication_year":"1976","canto_session_key":"4fa98283f1953e35","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2012-11-22 16:44:27","canto_approved_date":"2026-01-29 13:21:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-22 16:43:09","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.18c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-11-22"},{"uniquename":"PMID:35996688","title":"Photo Phenosizer, a rapid machine learning-based method to measure cell dimensions in fission yeast.","citation":"MicroPubl Biol 2022;2022","abstract":"Cell metrics such as area, length, and width provide informative data about cell cycle dynamics. Factors that affect these dimensions include environmental conditions and genotypic differences. Fission yeast (  Schizosaccharomyces pombe  ) is a rod-shaped ascomycete fungus in which cell cycle progression is linked to changes in cell length. Microscopy work to obtain these metrics places considerable burdens on time and effort. We now report on Photo Phenosizer (PP), a machine learning-based methodology that measures cell dimensions in fission yeast. It does this in an unbiased, automated manner and streamlines workflow from image acquisition to statistical analysis. Using this new approach, we constructed an efficient and flexible pipeline for experiments involving different growth media (YES and EMM) and treatments (Untreated and MMS) as well as different genotypes (  cut6-621  versus wildtype). This methodology allows for the analysis of larger sample sizes and faster image processing relative to manual segmentation. Our findings suggest that researchers using PP can quickly and efficiently determine cell size differences under various conditions that highlight genetic or environmental disruptions.","doi":"10.17912/micropub.biology.000620","authors":"Vo M, Kuo-Esser L, Dominguez M, Barta H, Graber M, Rausenberger A, Miller R, Sommer N, Escorcia W","authors_abbrev":"Vo M et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-08-23","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-08-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3417637","title":"Sulfide stabilization of the cadmium-gamma-glutamyl peptide complex of Schizosaccharomyces pombe.","citation":"J Biol Chem 1988 Sep 15;263(26):12832-5","abstract":"Addition of cadmium salts to the growth medium of Schizosaccharomyces pombe leads to synthesis of a Cd.gamma-Glu peptide complex and an enhanced generation of sulfide ions. The gamma-Glu peptide complex functions in the detoxification of heavy metal ions. Native Cd.gamma-Glu peptide complexes contain acid-labile sulfide in the metal-thiolate cluster. Two forms of the complex exist differing primarily in their sulfide content. Sulfide concentrations up to 0.2 and 1.2 mol/mol of peptide were observed in native isolates of forms I and II, respectively. Addition of sulfide to the low sulfide form I converted it to a complex similar to form II. Properties of the Cd.gamma-Glu peptide complex were altered by the incorporation of sulfide ions. Sulfide-dependent electronic transitions in the ultraviolet were evident, and the absorbance maximum of the transition was related to the sulfide content and the bound metal ion. High sulfide forms of the Cd and Zn complexes exhibited absorbance peaks at 318 nm and 255 nm, respectively. Incorporation of sulfide into the Cd.gamma-Glu peptide complex imparted greater thermodynamic stability to the complex, an increased Stokes radius, and an enhanced Cd(II) binding capacity. Sulfide generation may be a cellular response in part to enhance the effectiveness of the gamma-Glu peptide system for Cd(II) detoxification.","authors":"Reese RN, Winge DR","authors_abbrev":"Reese RN et al.","pubmed_publication_date":"15 Sep 1988","pubmed_entrez_date":"1988-09-15","publication_year":"1988","canto_session_key":"f6597de885c5253c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-07-01 10:50:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-13 14:00:21","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-06-13"},{"uniquename":"PMID:21801748","title":"Regulation of HMG-CoA reductase in mammals and yeast.","citation":"Prog Lipid Res 2011 Oct;50(4):403-10","abstract":"HMG-CoA reductase (HMGR), a highly conserved, membrane-bound enzyme, catalyzes a rate-limiting step in sterol and isoprenoid biosynthesis and is the primary target of hypocholesterolemic drug therapy. HMGR activity is tightly regulated to ensure maintenance of lipid homeostasis, disruption of which is a major cause of human morbidity and mortality. HMGR regulation takes place at the levels of transcription, translation, post-translational modification and degradation. In this review, we discuss regulation of mammalian, Saccharomyces cerevisiae and Schizosaccharomyces pombe HMGR and highlight recent advances in the field. We find that the general features of HMGR regulation, including a requirement for the HMGR-binding protein Insig, are remarkably conserved between mammals and ascomycetous fungi, including S. cerevisiae and S. pombe. However the specific details by which this regulation occurs differ in surprising ways, revealing the broad evolutionary themes underlying both HMGR regulation and Insig function.","doi":"10.1016/j.plipres.2011.07.002","authors":"Burg JS, Espenshade PJ","authors_abbrev":"Burg JS et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-08-02","publication_year":"2011","canto_session_key":"c7867613a814143d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-10-19 13:18:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-09 20:05:52","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC409.07c","SPCC162.09c","SPAC9G1.02","SPCC1739.12","SPCC306.05c","SPBC646.13"],"gene_count":7,"ltp_gene_count":0,"approved_date":"2012-07-09"},{"uniquename":"PMID:7070512","title":"Molecular rearrangement of mating-type genes in fission yeast.","citation":"Nature 1982 Apr 15;296(5858):682-3","abstract":"","authors":"Beach D, Nurse P, Egel R","authors_abbrev":"Beach D et al.","pubmed_publication_date":"15 Apr 1982","pubmed_entrez_date":"1982-04-15","publication_year":"1982","canto_session_key":"94fc40a24bf6de4a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-12-05 23:05:21","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-05 23:05:13","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-12-05"},{"uniquename":"PMID:16793396","title":"Analysis of the DNA unwinding activity of RecQ family helicases.","citation":"Methods Enzymol 2006;409:86-100","abstract":"The RecQ family of DNA helicases is highly conserved in evolution from bacteria to mammals. There are five human RecQ family members (RECQ1, BLM, WRN, RECQ4 and RECQ5), defects, three of which give rise to inherited human disorders. Mutations of BLM have been identified in patients with Bloom's syndrome, WRN has been shown to be mutated in Werner's syndrome, while mutations of RECQ4 have been associated with at least a subset of cases of both Rothmund-Thomson syndrome and RAPADILINO. The most characteristic features of these diseases are a predisposition to the development of malignancies of different types (particularly in Bloom's syndrome), some aspects of premature aging (particularly in Werner's syndrome), and on the cellular level, genome instability. In order to gain understanding of the molecular defects underlying these diseases, many laboratories have focused their research on a study of the biochemical properties of human RecQ helicases, particularly those associated with disease, and of RecQ proteins from other organisms (e.g., Sgs1p of budding yeast, Rqh1p of fission yeast, and RecQ of E.coli). In this chapter, we summarize the assay systems that we employ to analyze the catalytic properties of the BLM helicase. We have successfully used these methods for the study of other RecQ and non-RecQ helicases, indicating that they are likely to be applicable to all helicases.","authors":"Bachrati CZ, Hickson ID","authors_abbrev":"Bachrati CZ et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-06-24","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33131423","title":"Structure of  S. pombe  telomerase protein Pof8 C-terminal domain is an xRRM conserved among LARP7 proteins.","citation":"RNA Biol 2021 Aug;18(8):1181-1192","abstract":"La-related proteins 7 (LARP7) are a class of RNA chaperones that bind the 3' ends of RNA and are constitutively associated with their specific target RNAs. In metazoa, Larp7 binds to the long non-coding 7SK RNA as a core component of the 7SK RNP, a major regulator of eukaryotic transcription. In the ciliate  Tetrahymena  the LARP7 protein p65 is a component of telomerase, an essential ribonucleoprotein complex that maintains the telomeric DNA at eukaryotic chromosome ends. p65 is important for the ordered assembly of telomerase RNA (TER) with telomerase reverse transcriptase. Unexpectedly,  Schizosaccharomyces pombe  Pof8 was recently identified as a LARP7 protein and a core component of fission yeast telomerase essential for biogenesis. LARP7 proteins have a conserved N-terminal La motif and RRM1 (La module) and C-terminal RRM2 with specific RNA substrate recognition attributed to RRM2, first structurally characterized in p65 as an atypical RRM named xRRM. Here we present the X-ray crystal structure and NMR studies of  S. pombe  Pof8 RRM2. Sequence and structure comparison of Pof8 RRM2 to p65 and human Larp7 xRRMs reveals conserved features for RNA binding with the main variability in the length of the non-canonical helix α3. This study shows that Pof8 has conserved xRRM features, providing insight into TER recognition and the defining characteristics of the xRRM.","doi":"10.1080/15476286.2020.1836891","authors":"Basu R, Eichhorn CD, Cheng R, Peterson RD, Feigon J","authors_abbrev":"Basu R et al.","pubmed_publication_date":"Aug 2021","pubmed_entrez_date":"2020-11-02","publication_year":"2021","canto_session_key":"b1205c5aa6adcabb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-11-05 13:18:45","canto_approved_date":"2020-11-05 13:18:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-05 13:18:19","canto_added_date":"2020-11-04 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G6.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-11-05","pdb_entries":[{"pdb_id":"6tzn","gene_chains":[{"gene_uniquename":"SPAC17G6.17","chain":"A","position":"282-402"}],"title":"Structure of S. pombe telomerase accessory protein Pof8 C-terminal domain","entry_authors":"Basu RS,Cascio D,Eichhorn CD,Feigon J","entry_authors_abbrev":"Basu RS et al.","reference_uniquename":"PMID:33131423","experimental_method":"X-ray","resolution":"1.35"}]},{"uniquename":"EMBL:AU013199","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25053838","title":"The effect of Pot1 binding on the repair of thymine analogs in a telomeric DNA sequence.","citation":"Nucleic Acids Res 2014 Aug;42(14):9063-73","abstract":"Telomeric DNA can form duplex regions or single-stranded loops that bind multiple proteins, preventing it from being processed as a DNA repair intermediate. The bases within these regions are susceptible to damage; however, mechanisms for the repair of telomere damage are as yet poorly understood. We have examined the effect of three thymine (T) analogs including uracil (U), 5-fluorouracil (5FU) and 5-hydroxymethyluracil (5hmU) on DNA-protein interactions and DNA repair within the GGTTAC telomeric sequence. The replacement of T with U or 5FU interferes with Pot1 (Pot1pN protein of Schizosaccharomyces pombe) binding. Surprisingly, 5hmU substitution only modestly diminishes Pot1 binding suggesting that hydrophobicity of the T-methyl group likely plays a minor role in protein binding. In the GGTTAC sequence, all three analogs can be cleaved by DNA glycosylases; however, glycosylase activity is blocked if Pot1 binds. An abasic site at the G or T positions is cleaved by the endonuclease APE1 when in a duplex but not when single-stranded. Abasic site formation thermally destabilizes the duplex that could push a damaged DNA segment into a single-stranded loop. The inability to enzymatically cleave abasic sites in single-stranded telomere regions would block completion of the base excision repair cycle potentially causing telomere attrition.","doi":"10.1093/nar/gku602","authors":"Theruvathu JA, Darwanto A, Hsu CW, Sowers LC","authors_abbrev":"Theruvathu JA et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-07-24","publication_year":"2014","canto_session_key":"2033086de4d6a285","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-07-25 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11014802","title":"Glucose monitoring in fission yeast via the Gpa2 galpha, the git5 Gbeta and the git3 putative glucose receptor.","citation":"Genetics 2000 Oct;156(2):513-21","abstract":"The fission yeast Schizosaccharomyces pombe responds to environmental glucose by activating adenylate cyclase. The resulting cAMP signal activates protein kinase A (PKA). PKA inhibits glucose starvation-induced processes, such as conjugation and meiosis, and the transcription of the fbp1 gene that encodes the gluconeogenic enzyme fructose-1,6-bisphosphatase. We previously identified a collection of git genes required for glucose repression of fbp1 transcription, including pka1/git6, encoding the PKA catalytic subunit, git2/cyr1, encoding adenylate cyclase, and six \"upstream\" genes required for adenylate cyclase activation. The git8 gene, identical to gpa2, encodes the alpha subunit of a heterotrimeric guanine-nucleotide binding protein (Galpha) while git5 encodes a Gbeta subunit. Multicopy suppression studies with gpa2(+) previously indicated that S. pombe adenylate cyclase activation may resemble that of the mammalian type II enzyme with sequential activation by Galpha followed by Gbetagamma. We show here that an activated allele of gpa2 (gpa2(R176H), carrying a mutation in the coding region for the GTPase domain) fully suppresses mutations in git3 and git5, leading to a refinement in our model. We describe the cloning of git3 and show that it encodes a putative seven-transmembrane G protein-coupled receptor. A git3 deletion confers the same phenotypes as deletions of other components of the PKA pathway, including a germination delay, constitutive fbp1 transcription, and starvation-independent conjugation. Since the git3 deletion is fully suppressed by the gpa2(R176H) allele with respect to fbp1 transcription, git3 appears to encode a G protein-coupled glucose receptor responsible for adenylate cyclase activation in S. pombe.","authors":"Welton RM, Hoffman CS","authors_abbrev":"Welton RM et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-10-03","publication_year":"2000","canto_session_key":"3a02661c59ca34de","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-11 16:25:43","canto_approved_date":"2026-04-08 11:01:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-11 16:25:35","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21C3.20c","SPBC32H8.07","SPBC19C7.03","SPBC1198.14c","SPAC23H3.13c","SPBC106.10","SPCC1753.02c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2017-10-11"},{"uniquename":"PMID:24021628","title":"Structure-function analysis of Hmo1 unveils an ancestral organization of HMG-Box factors involved in ribosomal DNA transcription from yeast to human.","citation":"Nucleic Acids Res 2013 Dec;41(22):10135-49","abstract":"Ribosome biogenesis is a major metabolic effort for growing cells. In Saccharomyces cerevisiae, Hmo1, an abundant high-mobility group box protein (HMGB) binds to the coding region of the RNA polymerase I transcribed ribosomal RNAs genes and the promoters of ∼70% of ribosomal protein genes. In this study, we have demonstrated the functional conservation of eukaryotic HMGB proteins involved in ribosomal DNA (rDNA) transcription. We have shown that when expressed in budding yeast, human UBF1 and a newly identified Sp-Hmo1 (Schizosaccharomyces pombe) localize to the nucleolus and suppress growth defect of the RNA polymerase I mutant rpa49-Δ. Owing to the multiple functions of both proteins, Hmo1 and UBF1 are not fully interchangeable. By deletion and domains swapping in Hmo1, we identified essential domains that stimulate rDNA transcription but are not fully required for stimulation of ribosomal protein genes expression. Hmo1 is organized in four functional domains: a dimerization module, a canonical HMGB motif followed by a conserved domain and a C-terminal nucleolar localization signal. We propose that Hmo1 has acquired species-specific functions and shares with UBF1 and Sp-Hmo1 an ancestral function to stimulate rDNA transcription.","doi":"10.1093/nar/gkt770","authors":"Albert B, Colleran C, Léger-Silvestre I, Berger AB, Dez C, Normand C, Perez-Fernandez J, McStay B, Gadal O","authors_abbrev":"Albert B et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-09-12","publication_year":"2013","canto_session_key":"40033bc053698144","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-06-04 14:31:25","canto_approved_date":"2020-11-11 13:08:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-22 13:05:19","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["HGNC:12511","SPBC28F2.11","SPAC2F3.03c","YDR174W"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-04"},{"uniquename":"PMID:17072882","title":"Role of Rho GTPases and Rho-GEFs in the regulation of cell shape and integrity in fission yeast.","citation":"Yeast 2006 Oct 15;23(13):1031-43","abstract":"The Rho family of GTPases are highly conserved molecular switches that control some of the most fundamental processes of cell biology, including morphogenesis, vesicular transport, cell division and motility. Guanine nucleotide-exchange factors (GEFs) are directly responsible for the activation of Rho-family GTPases in response to extracellular stimuli. In fission yeast, there are seven Dbl-related GEFs and they activate six Rho-type GTPases within a particular spatio-temporal context. The failure to do so might have consequences reflected in aberrant phenotypes and in some cases lead to cell death. In this review, we briefly summarize the role of Rho GTPases and Rho-GEFs in the establishment and maintenance of cell polarity and cell integrity in Schizosaccharomyces pombe.","authors":"García P, Tajadura V, García I, Sánchez Y","authors_abbrev":"García P et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19756689","title":"SUMOylation is required for normal development of linear elements and wild-type meiotic recombination in Schizosaccharomyces pombe.","citation":"Chromosoma 2010 Feb;119(1):59-72","abstract":"In the fission yeast, Schizosaccharomyces pombe, synaptonemal complexes (SCs) are not formed during meiotic prophase. However, structures resembling the axial elements of SCs, the so-called linear elements (LinEs) appear. By in situ immunostaining, we found Pmt3 (S. pombe's SUMO protein) transiently along LinEs, suggesting that SUMOylation of some component(s) of LinEs occurs during meiosis. Mutation of the SUMO ligase Pli1 caused aberrant LinE formation and reduced genetic recombination indicating a role for SUMOylation of LinEs for the regulation of meiotic recombination. Western blot analysis of TAP-tagged Rec10 demonstrated that there is a Pli1-dependent posttranslational modification of this protein, which is a major LinE component and a distant homolog of the SC protein Red1. Mass spectrometry (MS) analysis revealed that Rec10 is both phosphorylated and ubiquitylated, but no evidence for SUMOylation of Rec10 was found. These findings indicate that the regulation of LinE and Rec10 function is modulated by Pli1-dependent SUMOylation of LinE protein(s) which directly or indirectly regulates Rec10 modification. On the side, MS analysis confirmed the interaction of Rec10 with the known LinE components Rec25, Rec27, and Hop1 and identified the meiotically upregulated protein Mug20 as a novel putative LinE-associated protein.","doi":"10.1007/s00412-009-0241-5","authors":"Spirek M, Estreicher A, Csaszar E, Wells J, McFarlane RJ, Watts FZ, Loidl J","authors_abbrev":"Spirek M et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2009-09-17","publication_year":"2010","canto_session_key":"6c7a8fb8c4d34c59","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2012-09-17 14:10:26","canto_approved_date":"2022-10-04 13:57:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-17 14:10:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.04c","SPAC10F6.09c","SPAC1687.05","SPBC106.09","SPBC577.05c","SPCC1235.05c","SPBC36B7.06c","SPBC29A10.04","SPAC17A5.18c","SPBC1718.02","SPAC29B12.07","SPCC1739.13","SPBC365.06","SPBC32F12.11"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2012-09-17"},{"uniquename":"PMID:32152323","title":"Time-lapse single-cell transcriptomics reveals modulation of histone H3 for dormancy breaking in fission yeast.","citation":"Nat Commun 2020 Mar 09;11(1):1265","abstract":"How quiescent cells break dormancy is a key issue in eukaryotic cells including cancer. Fungal spores, for example, remain quiescent for long periods until nourished, although the mechanisms by which dormancy is broken remain enigmatic. Transcriptome analysis could provide a clue, but methods to synchronously germinate large numbers of spores are lacking, and thus it remains a challenge to analyse gene expression upon germination. Hence, we develop methods to assemble transcriptomes from individual, asynchronous spore cells of fission yeast undergoing germination to assess transcriptomic changes over time. The virtual time-lapse analyses highlights one of three copies of histone H3 genes whose transcription fluctuates during the initial stage of germination. Disruption of this temporal fluctuation causes defects in spore germination despite no visible defects in other stages of the life cycle. We conclude that modulation of histone H3 expression is a crucial 'wake-up' trigger at dormancy breaking.","doi":"10.1038/s41467-020-15060-y","authors":"Tsuyuzaki H, Hosokawa M, Arikawa K, Yoda T, Okada N, Takeyama H, Sato M","authors_abbrev":"Tsuyuzaki H et al.","pubmed_publication_date":"09 Mar 2020","pubmed_entrez_date":"2020-03-11","publication_year":"2020","canto_session_key":"5af819a61b47875b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2020-09-22 15:31:39","canto_approved_date":"2024-04-03 09:57:49","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-09-19 10:58:00","canto_added_date":"2020-03-12 01:15:04","annotation_curators":[{"name":"Masamitsu Sato","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.04","SPBC8D2.04","SPBC1105.11c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-09-22"},{"uniquename":"PMID:8021562","title":"Changes in the distribution of F-actin in the fission yeast Schizosaccharomyces pombe by arresting growth in distilled water: correlative studies with fluorescence and electron microscopy.","citation":"J Electron Microsc (Tokyo) 1994 Feb;43(1):20-4","abstract":"Freeze-substitution electron microscopy of Schizosaccharomyces pombe cells starved in distilled water was conducted to define ultrastructural counterparts of actin visualized by fluorescence microscopy using rhodamine-conjugated phalloidin (Rh-ph). Starvation in distilled water caused remarkable changes in actin distribution and ultrastructural changes in S. pombe. Fluorescence microscopy of the starved cells showed that the dots of actin at the growing ends became thick actin cables via an enlarged patched form of actin. These changes were reversible, and growth-arrested cells resumed their original pattern of actin distribution upon return to growth medium. Electron microscopy of starved cells showed bundles of thin filaments and clusters of filamentous balls in the cytoplasm, which corresponded to the actin cables and enlarged actin dots, respectively, as seen by fluorescence microscopy. Vesicles polarized at the growing cell ends were dispersed in the cytoplasm by distilled water treatment, indicating that actin organization plays a role in directing vesicle location.","authors":"Kanbe T, Akashi T, Tanaka K","authors_abbrev":"Kanbe T et al.","pubmed_publication_date":"Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19001374","title":"Drosophila ABC transporter, DmHMT-1, confers tolerance to cadmium. DmHMT-1 and its yeast homolog, SpHMT-1, are not essential for vacuolar phytochelatin sequestration.","citation":"J Biol Chem 2009 Jan 02;284(1):354-362","abstract":"Half-molecule ATP-binding cassette transporters of the HMT-1 (heavy metal tolerance factor 1) subfamily are required for Cd2+ tolerance in Schizosaccharomyces pombe, Caenorhabditis elegans, and Chlamydomonas reinhardtii. Based on studies of S. pombe, it has been proposed that SpHMT-1 transports heavy metal.phytochelatin (PC) complexes into the vacuolysosomal compartment. PCs are glutathione derivatives synthesized by PC synthases (PCS) in plants, fungi, and C. elegans in response to heavy metals. Our previous studies in C. elegans, however, suggested that HMT-1 and PCS-1 do not necessarily act in concert in metal detoxification. To further explore this inconsistency, we have gone on to test whether DmHMT-1, an HMT-1 from a new source, Drosophila, whose genome lacks PCS homologs, functions in heavy metal detoxification. In so doing, we show that heterologously expressed DmHMT-1 suppresses the Cd2+ hypersensitivity of S. pombe hmt-1 mutants and localizes to the vacuolar membrane but does not transport Cd.PC complexes. Crucially, similar analyses of S. pombe hmt-1 mutants extend this finding to show that SpHMT-1 itself either does not transport Cd.PC complexes or is not the principal Cd.PC/apoPC transporter. Consistent with this discovery and with our previous suggestion that HMT-1 and PCS-1 do not operate in a simple linear metal detoxification pathway, we demonstrate that, unlike PCS-deficient cells, which are hypersensitive to several heavy metals, SpHMT-1-deficient cells are hypersensitive to Cd2+, but not to Hg2+ or As3+. These findings significantly change our current understanding of the function of HMT-1 proteins and invoke a PC-independent role for these transporters in Cd2+ detoxification.","doi":"10.1074/jbc.M806501200","authors":"Sooksa-Nguan T, Yakubov B, Kozlovskyy VI, Barkume CM, Howe KJ, Thannhauser TW, Rutzke MA, Hart JJ, Kochian LV, Rea PA, Vatamaniuk OK","authors_abbrev":"Sooksa-Nguan T et al.","pubmed_publication_date":"02 Jan 2009","pubmed_entrez_date":"2008-11-13","publication_year":"2009","canto_session_key":"211be4406f38d208","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-03-26 09:35:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-06-20 13:47:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.09c","SPAC3H1.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-06-20"},{"uniquename":"PMID:11270571","title":"A novel genetic screen identifies checkpoint-defective alleles of Schizosaccharomyces pombe chk1.","citation":"Curr Genet 2001 Jan;38(6):299-306","abstract":"The protein kinase Chk1 is required in the fission yeast Schizosaccharomyces pombe for delaying cell cycle progression in response to DNA damage. Chk1 becomes phosphorylated when DNA is damaged by a variety of agents, including the anti-tumor drug camptothecin. To further characterize the behavior of Chk1 in response to DNA damage, we used PCR-based mutagenesis of the chk1 gene coupled with in vivo gap repair to generate mutant alleles. Of 44 chk1 mutants recovered, six encode full-length proteins that confer a DNA damage-sensitive phenotype. All of the alleles render cells checkpoint-defective, but confer subtle differences in sensitivity to camptothecin or UV light. Mutant alleles were sequenced and served to identify regions of the protein that are critical for checkpoint function.","authors":"Wan S, Walworth NC","authors_abbrev":"Wan S et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-03-29","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPCC18B5.03","SPAC20G8.01"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:20306","title":"Purification and comparative study of adenine and guanine phosphoribosyltransferases from Schizosaccharomyces pombe.","citation":"Eur J Biochem 1977 Jul 01;77(1):77-85","abstract":"","authors":"Nagy M, Ribet AM","authors_abbrev":"Nagy M et al.","pubmed_publication_date":"01 Jul 1977","pubmed_entrez_date":"1977-07-01","publication_year":"1977","canto_session_key":"641e9af49e65dc1e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-09 17:07:29","canto_approved_date":"2020-01-23 13:18:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-13 15:24:49","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.13c","SPAC23A1.03","SPAC4D7.08c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-02-09"},{"uniquename":"PMID:9695827","title":"Fission yeast cut mutations revisited: control of anaphase.","citation":"Trends Cell Biol 1998 Apr;8(4):144-9","abstract":"Studies of anaphase are approaching a golden age. Several different disciplines have contributed immensely to advances in our understanding of cell-cycle control and chromosome and spindle dynamics during mitosis. This article describes control of anaphase based on results obtained from Schizosaccharomyces pombe cut (cell untimely torn) mutants. These temperature-sensitive mutants were isolated by selection for uncoordinated mitosis with aberrant sister-chromatid separation and post-anaphase events. Characterization of some of the cut gene products has led to identification of novel molecular events related to chromosome condensation, sister-chromatid separation, anaphase-promoting proteolysis, fatty-acid metabolism, and cell-cycle arrest induced by stress or a replication block.","authors":"Yanagida M","authors_abbrev":"Yanagida M","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-08-08","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22275432","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4A8.05c","SPCC645.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:24278726","title":"The Reporter System for GPCR Assay with the Fission Yeast Schizosaccharomyces pombe.","citation":"Scientifica (Cairo) 2012;2012:674256","abstract":"G protein-coupled receptors (GPCRs) are associated with a great variety of biological activities. Yeasts are often utilized as a host for heterologous GPCR assay. We engineered the intense reporter plasmids for fission yeast to produce green fluorescent protein (GFP) through its endogenous GPCR pathway. As a control region of GFP expression on the reporter plasmid, we focused on seven endogenous genes specifically activated through the pathway. When upstream regions of these genes were used as an inducible promoter in combination with LPI terminator, the mam2 upstream region produced GFP most rapidly and intensely despite the high background. Subsequently, LPI terminator was replaced with the corresponding downstream regions. The SPBC4.01 downstream region enhanced the response with the low background. Furthermore, combining SPBC4.01 downstream region with the sxa2 upstream region, the signal to noise ratio was obviously better than those of other regions. We also evaluated the time- and dose-dependent GFP productions of the strains transformed with the reporter plasmids. Finally, we exhibited a model of simplified GPCR assay with the reporter plasmid by expressing endogenous GPCR under the control of the foreign promoter.","doi":"10.6064/2012/674256","authors":"Sasuga S, Osada T","authors_abbrev":"Sasuga S et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2013-11-27","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:48:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39057793","title":"Advanced Protocol for Molecular Characterization of Viral Genome in Fission Yeast ( Schizosaccharomyces pombe ).","citation":"Pathogens 2024 Jul 04;13(7)","abstract":"Fission yeast, a single-cell eukaryotic organism, shares many fundamental cellular processes with higher eukaryotes, including gene transcription and regulation, cell cycle regulation, vesicular transport and membrane trafficking, and cell death resulting from the cellular stress response. As a result, fission yeast has proven to be a versatile model organism for studying human physiology and diseases such as cell cycle dysregulation and cancer, as well as autophagy and neurodegenerative diseases like Alzheimer's, Parkinson's, and Huntington's diseases. Given that viruses are obligate intracellular parasites that rely on host cellular machinery to replicate and produce, fission yeast could serve as a surrogate to identify viral proteins that affect host cellular processes. This approach could facilitate the study of virus-host interactions and help identify potential viral targets for antiviral therapy. Using fission yeast for functional characterization of viral genomes offers several advantages, including a well-characterized and haploid genome, robustness, cost-effectiveness, ease of maintenance, and rapid doubling time. Therefore, fission yeast emerges as a valuable surrogate system for rapid and comprehensive functional characterization of viral proteins, aiding in the identification of therapeutic antiviral targets or viral proteins that impact highly conserved host cellular functions with significant virologic implications. Importantly, this approach has a proven track record of success in studying various human and plant viruses. In this protocol, we present a streamlined and scalable molecular cloning strategy tailored for genome-wide and comprehensive functional characterization of viral proteins in fission yeast.","doi":"10.3390/pathogens13070566","authors":"Zhang J, Benko Z, Zhang C, Zhao RY","authors_abbrev":"Zhang J et al.","pubmed_publication_date":"04 Jul 2024","pubmed_entrez_date":"2024-07-26","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-07-26 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34851403","title":"Direct evaluation of cohesin-mediated sister kinetochore associations at meiosis I in fission yeast.","citation":"J Cell Sci 2022 Jan 01;135(1)","abstract":"Kinetochores drive chromosome segregation by mediating chromosome interactions with the spindle. In higher eukaryotes, sister kinetochores are separately positioned on opposite sides of sister centromeres during mitosis, but associate with each other during meiosis I. Kinetochore association facilitates the attachment of sister chromatids to the same pole, enabling the segregation of homologous chromosomes toward opposite poles. In the fission yeast, Schizosaccharomyces pombe, Rec8-containing meiotic cohesin is suggested to establish kinetochore associations by mediating cohesion of the centromere cores. However, cohesin-mediated kinetochore associations on intact chromosomes have never been demonstrated directly. In the present study, we describe a novel method for the direct evaluation of kinetochore associations on intact chromosomes in live S. pombe cells, and demonstrate that sister kinetochores and the centromere cores are positioned separately on mitotic chromosomes but associate with each other on meiosis I chromosomes. Furthermore, we demonstrate that kinetochore association depends on meiotic cohesin and the cohesin regulators Moa1 and Mrc1, and requires mating-pheromone signaling for its establishment. These results confirm cohesin-mediated kinetochore association and its regulatory mechanisms, along with the usefulness of the developed method for its analysis. This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.259102","authors":"Nambu M, Kishikawa A, Yamada T, Ichikawa K, Kira Y, Itabashi Y, Honda A, Yamada K, Murakami H, Yamamoto A","authors_abbrev":"Nambu M et al.","pubmed_publication_date":"01 Jan 2022","pubmed_entrez_date":"2021-12-01","publication_year":"2022","canto_session_key":"f93022f938a65fbf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ayumu Yamamoto","canto_first_approved_date":"2023-06-19 14:49:43","canto_approved_date":"2024-02-21 18:55:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-10 07:57:23","canto_added_date":"2021-12-03 01:15:04","annotation_curators":[{"name":"Ayumu Yamamoto","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC694.06c","SPAC664.01c","SPBC29A10.14","SPBP35G2.03c","SPBC19C2.05","SPAC15E1.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2023-06-19"},{"uniquename":"PMID:14298939","title":"SELECTIVE SYNTHESIS OF MESSENGER RNA IN A FISSION YEAST DURING A STEP-DOWN, AND ITS RELATION TO THE CELL CYCLE. BULK EXPERIMENTS.","citation":"Exp Cell Res 1965 Feb;37:259-77","abstract":"","authors":"MITCHISON JM, GROSS PR","authors_abbrev":"MITCHISON JM et al.","pubmed_publication_date":"Feb 1965","pubmed_entrez_date":"1965-02-01","publication_year":"1965","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41562396","title":"The THO complex in Schizosaccharomyces pombe-dissecting the composition and functional hierarchy.","citation":"FEBS Lett 2026 Jan 21;","abstract":"The THO complex was initially identified in Saccharomyces cerevisiae with five subunits: Hpr1p, Tho2p, Mft1p, Thp2p, and Tex1p. It plays a major role in mRNA processing and nuclear export. Here, we aimed to identify the putative homologs in Schizosaccharomyces pombe. Among eight candidates, genetic analysis showed tho1, tho2, and pci2 are essential, while mutants of tho5 and tho7 exhibited growth defects along with genome instability and impaired mRNA export. Subcellular localization studies showed all putative homologs except Tho3 are localized to the nucleus, whereas Pci2 localizes to the nuclear envelope. Yeast two-hybrid and immunoprecipitation-mass spectrometry confirmed Tho1, Tho2, Tho5, and Tho7 form the core THO complex. This work defines the THOC complex in S. pombe and supports Pci2 as a component of TREX-2 at the nuclear periphery during mRNA export.","doi":"10.1002/1873-3468.70288","authors":"He W, Huang C, Huang Q, Ma W","authors_abbrev":"He W et al.","pubmed_publication_date":"21 Jan 2026","pubmed_entrez_date":"2026-01-21","publication_year":"2026","canto_session_key":"a6575cc77581f14c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-01-22 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12456009","title":"The fission yeast ubiquitin-conjugating enzymes UbcP3, Ubc15, and Rhp6 affect transcriptional silencing of the mating-type region.","citation":"Eukaryot Cell 2002 Aug;1(4):613-25","abstract":"Genes transcribed by RNA polymerase II are silenced when introduced near the mat2 or mat3 mating-type loci of the fission yeast Schizosaccharomyces pombe. Silencing is mediated by a number of gene products and cis-acting elements. We report here the finding of novel trans-acting factors identified in a screen for high-copy-number disruptors of silencing. Expression of cDNAs encoding the putative E2 ubiquitin-conjugating enzymes UbcP3, Ubc15 (ubiquitin-conjugating enzyme), or Rhp6 (Rad homolog pombe) from the strong nmt1 promoter derepressed the silent mating-type loci mat2 and mat3 and reporter genes inserted nearby. Deletion of rhp6 slightly derepressed an ade6 reporter gene placed in the mating-type region, whereas disruption of ubcP3 or ubc15 had no obvious effect on silencing. Rhp18 is the S. pombe homolog of Saccharomyces cerevisiae Rad18p, a DNA-binding protein that physically interacts with Rad6p. Rhp18 was not required for the derepression observed when UbcP3, Ubc15, or Rhp6 was overproduced. Overexpressing Rhp6 active-site mutants showed that the ubiquitin-conjugating activity of Rhp6 is essential for disruption of silencing. However, high dosage of UbcP3, Ubc15, or Rhp6 was not suppressed by a mutation in the 26S proteasome, suggesting that loss of silencing is not due to an increased degradation of silencing factors but rather to the posttranslational modification of proteins by ubiquitination. We discuss the implications of these results for the possible modes of action of UbcP3, Ubc15, and Rhp6.","authors":"Nielsen IS, Nielsen O, Murray JM, Thon G","authors_abbrev":"Nielsen IS et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-11-29","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27887640","title":"Functional and regulatory profiling of energy metabolism in fission yeast.","citation":"Genome Biol 2016 Nov 25;17(1):240","abstract":"The control of energy metabolism is fundamental for cell growth and function and anomalies in it are implicated in complex diseases and ageing. Metabolism in yeast cells can be manipulated by supplying different carbon sources: yeast grown on glucose rapidly proliferates by fermentation, analogous to tumour cells growing by aerobic glycolysis, whereas on non-fermentable carbon sources metabolism shifts towards respiration.\nWe screened deletion libraries of fission yeast to identify over 200 genes required for respiratory growth. Growth media and auxotrophic mutants strongly influenced respiratory metabolism. Most genes uncovered in the mutant screens have not been implicated in respiration in budding yeast. We applied gene-expression profiling approaches to compare steady-state fermentative and respiratory growth and to analyse the dynamic adaptation to respiratory growth. The transcript levels of most genes functioning in energy metabolism pathways are coherently tuned, reflecting anticipated differences in metabolic flows between fermenting and respiring cells. We show that acetyl-CoA synthase, rather than citrate lyase, is essential for acetyl-CoA synthesis in fission yeast. We also investigated the transcriptional response to mitochondrial damage by genetic or chemical perturbations, defining a retrograde response that involves the concerted regulation of distinct groups of nuclear genes that may avert harm from mitochondrial malfunction.\nThis study provides a rich framework of the genetic and regulatory basis of energy metabolism in fission yeast and beyond, and it pinpoints weaknesses of commonly used auxotroph mutants for investigating metabolism. As a model for cellular energy regulation, fission yeast provides an attractive and complementary system to budding yeast.","authors":"Malecki M, Bitton DA, Rodríguez-López M, Rallis C, Calavia NG, Smith GC, Bähler J","authors_abbrev":"Malecki M et al.","pubmed_publication_date":"25 Nov 2016","pubmed_entrez_date":"2016-11-27","publication_year":"2016","canto_session_key":"3c66d095896b8ee5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Michal Malecki","canto_first_approved_date":"2017-03-15 11:05:48","canto_approved_date":"2023-04-03 16:06:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-14 14:50:41","canto_added_date":"2016-11-28 01:15:12","annotation_curators":[{"name":"Michal Malecki","community_curator":true,"annotation_count":2,"orcid":"0000-0002-1525-5036","file_type":null,"file_name":null}],"file_curator_name":"Michal Malecki","file_curator_role":"community","annotation_file_curators":[{"name":"Michal Malecki","community_curator":true,"annotation_count":402,"orcid":"0000-0002-1525-5036","file_type":"PHAF","file_name":"PMID_27887640_phaf.tsv"}],"genes":["SPAPB1A10.14","SPAC23C11.08","SPBC2G2.03c","SPBC16A3.08c","SPBC2A9.02","SPAC1F12.05","SPAC1952.09c","SPBC800.05c","SPAC1B9.02c","SPAC12B10.04","SPAC6F6.11c","SPAC6B12.05c","SPBC800.07c","SPBC691.04","SPBC3H7.03c","SPAC23D3.09","SPBC106.17c","SPBC1539.04","SPAC23C4.09c","SPBPB10D8.06c","SPBC16G5.15c","SPBC25D12.06","SPAC1556.04c","SPBC31E1.01c","SPCC736.02","SPBP8B7.08c","SPBC1D7.04","SPBC32F12.07c","SPAC18B11.02c","SPAC15A10.11","SPBC1A4.02c","SPBC1198.14c","SPBC18E5.11c","SPCC1840.09","SPAC3F10.04","SPBC27.08c","SPAC12B10.11","SPAC3H5.08c","SPCC1682.08c","SPAC22H12.01c","SPAC3A12.13c","SPAC14C4.06c","SPBC2G2.10c","SPCC663.12","SPCC1620.08","SPBC12D12.07c","SPBC21C3.08c","SPAC11D3.03c","SPAC1F8.06","SPCC285.10c","SPAC9G1.04","SPAC18G6.13","SPAC4G9.20c","SPCC16C4.12","SPAC23C4.12","SPBC32F12.12c","SPBC651.06","SPAC227.17c","SPBC106.07c","SPAC23C4.06c","SPAC6F12.03c","SPBC651.09c","SPCC4B3.06c","SPAC13G6.14","SPAC13G7.11","SPAC17H9.12c","SPAC959.04c","SPCC736.06","SPBC4B4.03","SPBC83.18c","SPAC19G12.13c","SPAC24H6.03","SPBC2A9.11c","SPAC15F9.02","SPAC17H9.08","SPCC1919.07","SPAC1610.02c","SPBC1E8.02","SPCC285.13c","SPCC1020.06c","SPAPJ691.03","SPCC1235.08c","SPBC1289.14","SPAC26A3.14c","SPAC17G8.13c","SPAC30C2.02","SPAC1D4.05c","SPAC1071.02","SPAC29A4.18","SPBC21H7.04","SPBC31F10.03","SPBC3E7.05c","SPBC106.05c","SPAC23D3.11","SPAC15A10.03c","SPAC12B10.09","SPCC1442.05c","SPCC1840.02c","SPBC18H10.04c","SPAC1782.08c","SPCC162.11c","SPAC1610.03c","SPAC18G6.04c","SPAC9.12c","SPBC609.02","SPBC1921.01c","SPAC15A10.15","SPAC823.16c","SPCC1393.09c","SPAC27D7.04","SPBC16C6.04","SPCC1183.09c","SPCC584.03c","SPBC1215.01","SPBC56F2.03","SPBC800.08","SPBPB2B2.02","SPAC23D3.04c","SPCC4B3.03c","SPAC637.07","SPAC1D4.11c","SPBC1683.03c","SPBC23G7.08c","SPCC191.02c","SPAC2F7.17","SPAC4G8.11c","SPBPB2B2.13","SPCC16A11.07","SPAC17H9.09c","SPBC36.11","SPAC1A6.04c","SPAC1687.15","SPAC2F7.09c","SPBC28E12.04","SPAC22F3.06c","SPCC306.07c","SPBC2G2.07c","SPAC22H10.09","SPBC16A3.03c","SPAC823.10c","SPCC18B5.03","SPBC428.02c","SPAC1805.09c","SPBC25B2.04c","SPBC146.12","SPBC947.15c","SPAC17H9.19c","SPAC323.04","SPBC3B8.03","SPBC56F2.11","SPAC9.07c","SPAC922.05c","SPAC4F8.03","SPAC630.04c","SPBC1198.11c","SPAC5H10.04","SPBC30B4.06c","SPAC1F3.09","SPNCRNA.9001","SPBC336.01","SPAC688.11","SPBC354.10","SPAC6C3.05","SPAC31G5.11","SPAC1296.02","SPCC31H12.06","SPBC106.02c","SPBC543.10","SPAC1B3.05","SPBC4F6.08c","SPCC576.14","SPBC27B12.10c","SPBC25H2.16c","SPBPB10D8.07c","SPBC25H2.09","SPAC1805.02c","SPAC1565.03","SPAC13F5.03c","SPAC1250.04c","SPBC3H7.07c","SPAC1486.01","SPAC25B8.05","SPAC3F10.06c","SPAC15E1.09","SPAC3H8.09c","SPBC660.10","SPAC17A2.09c","SPAC27F1.05c","SPAC31A2.13c","SPAC17A2.10c","SPBC146.09c","SPBC543.07","SPBPB2B2.10c","SPAC1B3.01c","SPAC19G12.05","SPBC3B9.04","SPBC36.10","SPBC19G7.04","SPAC3A12.12","SPAC3C7.03c","SPCC736.11","SPBC685.03","SPBC11G11.03","SPBC16D10.11c","SPBP23A10.16","SPAC16.01","SPCC576.12c","SPAC11G7.06c","SPAC22G7.07c","SPBC776.01","SPBC30D10.10c","SPAC1565.04c","SPBC36.04","SPCC63.02c","SPAC2F7.10","SPAC13A11.03","SPCC553.01c","SPAC6B12.12","SPAC222.05c","SPAP8A3.04c","SPCC645.07","SPCC31H12.05c","SPAC57A7.08","SPAC4A8.04","SPCC4G3.04c","SPAC14C4.01c","SPBC21C3.11","SPAC9E9.10c","SPAP8A3.07c","SPBC27B12.08","SPAC1071.11","SPAC22F3.07c","SPBC428.03c","SPAC3F10.05c","SPBC1709.09","SPAC12B10.03","SPBC119.06","SPCC4B3.15","SPBC215.05","SPAC6F6.01","SPBC428.15","SPBC27.06c"],"gene_count":242,"ltp_gene_count":2,"approved_date":"2017-03-15"},{"uniquename":"PMID:8893552","title":"Identification of plant cytoskeletal, cell cycle-related and polarity-related proteins using Schizosaccharomyces pombe.","citation":"Plant J 1996 Oct;10(4):761-9","abstract":"The fission yeast Schizosaccharomyces pombe has been used to identify Arabidopsis thaliana proteins that may play a role in cell shape maintenance or cell cycle regulation. An Arabidopsis thaliana cDNA library was constructed in pREP5N vector under the control of the inducible nmt1 promoter and transformed into S. pombe. Expression of the A. thaliana sequences was induced and clones showing severe morphological changes were identified and analysed. Comparison of the sequences of the inserts with the sequence data bases revealed that several cDNAs encode proteins known to play a role in function of the cytoskeleton, the cell cycle and establishment of cell polarity. These include alpha-1, alpha-2, alpha-6 and beta-6 tubulins, myosin heavy chain-like protein, ubiquitin conjugating enzymes UBC9 (E2), 26S protease subunits, Ranbinding protein, myb protein, PRL1 gene product and rho protein. Approximately 30% of the clones encode novel sequences. The results suggest that S. pombe phenotypic screening can be used to identify plant proteins involved in cell shape maintenance and regulation during cell cycle and development.","authors":"Xia G, Ramachandran S, Hong Y, Chan YS, Simanis V, Chua NH","authors_abbrev":"Xia G et al.","pubmed_publication_date":"Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33836577","title":"A conserved Ctp1/CtIP C-terminal peptide stimulates Mre11 endonuclease activity.","citation":"Proc Natl Acad Sci U S A 2021 Mar 16;118(11)","abstract":"The Mre11-Rad50-Nbs1 complex (MRN) is important for repairing DNA double-strand breaks (DSBs) by homologous recombination (HR). The endonuclease activity of MRN is critical for resecting 5'-ended DNA strands at DSB ends, producing 3'-ended single-strand DNA, a prerequisite for HR. This endonuclease activity is stimulated by Ctp1, the  Schizosaccharomyces pombe  homolog of human CtIP. Here, with purified proteins, we show that Ctp1 phosphorylation stimulates MRN endonuclease activity by inducing the association of Ctp1 with Nbs1. The highly conserved extreme C terminus of Ctp1 is indispensable for MRN activation. Importantly, a polypeptide composed of the conserved 15 amino acids at the C terminus of Ctp1 (CT15) is sufficient to stimulate Mre11 endonuclease activity. Furthermore, the CT15 equivalent from CtIP can stimulate human MRE11 endonuclease activity, arguing for the generality of this stimulatory mechanism. Thus, we propose that Nbs1-mediated recruitment of CT15 plays a pivotal role in the activation of the Mre11 endonuclease by Ctp1/CtIP.","doi":"10.1073/pnas.2016287118","authors":"Zdravković A, Daley JM, Dutta A, Niwa T, Murayama Y, Kanamaru S, Ito K, Maki T, Argunhan B, Takahashi M, Tsubouchi H, Sung P, Iwasaki H","authors_abbrev":"Zdravković A et al.","pubmed_publication_date":"16 Mar 2021","pubmed_entrez_date":"2021-04-10","publication_year":"2021","canto_session_key":"7bf1fc1e6f06a613","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroshi Iwasaki","canto_first_approved_date":"2021-06-18 16:09:52","canto_approved_date":"2023-04-03 14:44:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-15 10:34:13","canto_added_date":"2021-04-12 00:15:07","annotation_curators":[{"name":"Hiroshi Iwasaki","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.08","SPAC13C5.07","SPBC6B1.09c","SPAC23C11.11","SPAC1556.01c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2021-06-18"},{"uniquename":"PMID:8299425","title":"RAS function and protein kinase cascades.","citation":"Ciba Found Symp 1993;176:53-61; discussion 61-6","abstract":"This paper reviews recent progress in understanding the function of RAS in three systems: the budding yeast (Saccharomyces cerevisiae), the fission yeast (Schizosaccharomyces pombe) and Xenopus laevis oocytes. One of the functions of RAS in S. cerevisiae is the stimulation of adenylate cyclase. This leads to the activation of the cAMP-dependent protein kinases--a function that has probably not been conserved in evolution. The immediate function of RAS in S. pombe is not known, but it may lead to the activation of a protein kinase cascade. This cascade has likely been conserved in evolution and linkage between it and RAS can be demonstrated in cell-free extracts from Xenopus oocytes. The Xenopus cell-free system provides a means to test specific hypotheses about RAS function and to isolate targets of RAS.","authors":"Marcus S, Wigler M, Xu HP, Ballester R, Kawamukai M, Polverino A","authors_abbrev":"Marcus S et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36001961","title":"Single-chromosome fission yeast models reveal the configuration robustness of a functional genome.","citation":"Cell Rep 2022 Aug 23;40(8):111237","abstract":"In eukaryotic organisms, genetic information is usually carried on multiple chromosomes. Whether and how the number and configuration of chromosomes affect organismal fitness and speciation remain unclear. Here, we have successfully established several single-chromosome fission yeast Schizosaccharomyces pombe strains, in which the three natural chromosomes have been fused into one giant chromosome in different orders. Chromosome fusions accompanied by the deletions of telomeres and centromeres result in the loss of chromosomal interactions and a drastic change of global chromosome organization, but alter gene expression marginally. The single-chromosome strains display little defects in cell morphology, mitosis, genotoxin sensitivity, and meiosis. Crosses between a wild-type strain and a single-chromosome strain or between two single-chromosome strains with different fusion orders suffer defective meiosis and poor spore viability. We conclude that eukaryotic genomes are robust against dramatic chromosomal reconfiguration, and stochastic changes in chromosome number and genome organization during evolution underlie reproductive isolation and speciation.","doi":"10.1016/j.celrep.2022.111237","authors":"Gu X, Ye T, Zhang XR, Nie L, Wang H, Li W, Lu R, Fu C, Du LL, Zhou JQ","authors_abbrev":"Gu X et al.","pubmed_publication_date":"23 Aug 2022","pubmed_entrez_date":"2022-08-24","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-08-26 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10861204","title":"DNA replication and damage checkpoints and meiotic cell cycle controls in the fission and budding yeasts.","citation":"Biochem J 2000 Jul 01;349(Pt 1):1-12","abstract":"The cell cycle checkpoint mechanisms ensure the order of cell cycle events to preserve genomic integrity. Among these, the DNA-replication and DNA-damage checkpoints prevent chromosome segregation when DNA replication is inhibited or DNA is damaged. Recent studies have identified an outline of the regulatory networks for both of these controls, which apparently operate in all eukaryotes. In addition, it appears that these checkpoints have two arrest points, one is just before entry into mitosis and the other is prior to chromosome separation. The former point requires the central cell-cycle regulator Cdc2 kinase, whereas the latter involves several key regulators and substrates of the ubiquitin ligase called the anaphase promoting complex. Linkages between these cell-cycle regulators and several key checkpoint proteins are beginning to emerge. Recent findings on post-translational modifications and protein-protein interactions of the checkpoint proteins provide new insights into the checkpoint responses, although the functional significance of these biochemical properties often remains unclear. We have reviewed the molecular mechanisms acting at the DNA-replication and DNA-damage checkpoints in the fission yeast Schizosaccharomyces pombe, and the modifications of these controls during the meiotic cell cycle. We have made comparisons with the controls in fission yeast and other organisms, mainly the distantly related budding yeast.","authors":"Murakami H, Nurse P","authors_abbrev":"Murakami H et al.","pubmed_publication_date":"01 Jul 2000","pubmed_entrez_date":"2000-06-22","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19064926","title":"Modulation of RNA polymerase II subunit composition by ubiquitylation.","citation":"Proc Natl Acad Sci U S A 2008 Dec 16;105(50):19649-54","abstract":"Emerging evidence suggests that components of the ubiquitin-proteasome system are involved in the regulation of gene expression. A variety of factors, including transcriptional activators, coactivators, and histones, are controlled by ubiquitylation, but the mechanisms through which this modification can function in transcription are generally unknown. Here, we report that the Saccharomyces cerevisiae protein Asr1 is a RING finger ubiquitin-ligase that binds directly to RNA polymerase II via the carboxyl-terminal domain (CTD) of the largest subunit of the enzyme. We show that interaction of Asr1 with the CTD depends on serine-5 phosphorylation within the CTD and results in ubiquitylation of at least 2 subunits of the enzyme, Rpb1 and Rpb2. Ubiquitylation by Asr1 leads to the ejection of the Rpb4/Rpb7 heterodimer from the polymerase complex and is associated with inactivation of polymerase function. Our data demonstrate that ubiquitylation can directly alter the subunit composition of a core component of the transcriptional machinery and provide a paradigm for how ubiquitin can influence gene activity.","doi":"10.1073/pnas.0809372105","authors":"Daulny A, Geng F, Muratani M, Geisinger JM, Salghetti SE, Tansey WP","authors_abbrev":"Daulny A et al.","pubmed_publication_date":"16 Dec 2008","pubmed_entrez_date":"2008-12-10","publication_year":"2008","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC126.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9368044","title":"Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins.","citation":"J Biol Chem 1997 Nov 21;272(47):29742-51","abstract":"Crm1 of Schizosaccharomyces pombe, a nuclear protein essential for proliferation and chromosome region maintenance, is a possible target of leptomycin B, an antifungal and antitumor antibiotic with cell cycle-arresting activity. cDNA encoding a human homolog of Crm1 was cloned. Human CRM1 (hCRM1) consisted of 1071 amino acids, of which the sequence showed 52% homology with S. pombe Crm1. hCRM1 weakly complemented the cold-sensitive mutation of S. pombe crm1-809, as did S. pombe crm1+. Overproduction of hCRM1 under the control of a series of nmt1 promoters suppressed cell proliferation in wild-type S. pombe in an expression level-dependent manner. A similar inhibitory effect was also observed for crm1+. Cells overproducing either hCRM1 or S. pombe Crm1 were distinctly larger than uninduced cells and contained compacted and fragmented nuclei. Furthermore, calcofluor staining demonstrated that most of these cells formed two septa per cell and accumulated a large amount of chitin or its related polysaccharides around the septa. Closely similar phenotypes between hCRM1- and S. pombe Crm1-induced cells indicate that the cloned cDNA encodes a functional homolog of S. pombe crm1+. Northern blot analyses with RNAs isolated from synchronized mammalian cells showed that the expression of mammalian CRM1 was initiated in late G1 and reached a peak at G2/M, although its protein level unchanged during the cell cycle. Transient expression of hCRM1 fused to the green fluorescent protein (GFP) in NIH3T3 cells showed that hCRM1 was localized preferentially in the nuclear envelope and was also detectable in the nucleoplasm and the cytoplasm. A crm1 mutation of S. pombe caused nuclear import of a GFP fusion protein containing a nuclear export signal but no change in the distribution of a GFP fusion protein containing a nuclear localization signal. All of these data suggest that CRM1 is a novel cell-cycle regulated gene that is essential for the nuclear export signal-dependent nuclear export of proteins.","authors":"Kudo N, Khochbin S, Nishi K, Kitano K, Yanagida M, Yoshida M, Horinouchi S","authors_abbrev":"Kudo N et al.","pubmed_publication_date":"21 Nov 1997","pubmed_entrez_date":"1997-12-31","publication_year":"1997","canto_session_key":"82e75444a0553c25","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-15 09:37:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-04-25 06:41:08","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-04-25"},{"uniquename":"PMID:4822119","title":"The wall structure of Schizosaccharomyces pombe.","citation":"J Gen Microbiol 1974 Mar;81(1):199-206","abstract":"","authors":"Bush DA, Horisberger M, Horman I, Wursch P","authors_abbrev":"Bush DA et al.","pubmed_publication_date":"Mar 1974","pubmed_entrez_date":"1974-03-01","publication_year":"1974","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15059961","title":"RNase-sensitive DNA modification(s) initiates S. pombe mating-type switching.","citation":"Genes Dev 2004 Apr 01;18(7):794-804","abstract":"Mating-type switching in fission yeast depends on an imprint at the mat1 locus. Previous data showed that the imprint is made in the DNA strand replicated as lagging. We now identify this imprint as an RNase-sensitive modification and suggest that it consists of one or two RNA residues incorporated into the mat1 DNA. Formation of the imprint requires swi1- and swi3-dependent pausing of the replication fork. Interestingly, swi1 and swi3 mutations that abolish pausing do not affect the use of lagging-strand priming site during replication. We show that the pausing of replication and subsequent formation of the imprint occur after the leading-strand replication complex has passed the site of the imprint and after lagging-strand synthesis has initiated at this proximal priming site. We propose a model in which a swi1- and swi3-dependent signal during lagging-strand synthesis leads to pausing of leading-strand replication and the introduction of the imprint.","authors":"Vengrova S, Dalgaard JZ","authors_abbrev":"Vengrova S et al.","pubmed_publication_date":"01 Apr 2004","pubmed_entrez_date":"2004-04-03","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC30D10.04"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:17891150","title":"A conserved motif in Argonaute-interacting proteins mediates functional interactions through the Argonaute PIWI domain.","citation":"Nat Struct Mol Biol 2007 Oct;14(10):897-903","abstract":"Argonaute (Ago) proteins mediate silencing of nucleic acid targets by small RNAs. In fission yeast, Ago1, Tas3 and Chp1 assemble into a RITS complex, which silences transcription near centromeres. Here we describe a repetitive motif within Tas3, termed the 'Argonaute hook', that is conserved from yeast to humans and binds Ago proteins through their PIWI domains in vitro and in vivo. Site-directed mutation of key residues in the motif disrupts Ago binding and heterochromatic silencing in vivo. Unexpectedly, a PIWI domain pocket that binds the 5' end of the short interfering RNA guide strand is required for direct binding of the Ago hook. Moreover, wild-type but not mutant Ago hook peptides derepress microRNA-mediated translational silencing of a target messenger RNA. Proteins containing the conserved Ago hook may thus be important regulatory components of effector complexes in RNA interference.","authors":"Till S, Lejeune E, Thermann R, Bortfeld M, Hothorn M, Enderle D, Heinrich C, Hentze MW, Ladurner AG","authors_abbrev":"Till S et al.","pubmed_publication_date":"Oct 2007","pubmed_entrez_date":"2007-09-25","publication_year":"2007","canto_session_key":"b3680419df0057b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-06-12 12:28:22","canto_approved_date":"2024-06-12 12:28:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 12:28:16","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC83.03c","SPCC736.11"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-06-12"},{"uniquename":"PMID:11087749","title":"Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe, interacts with a phosphatidylinositol 4-kinase.","citation":"J Biol Chem 2001 Feb 23;276(8):5932-42","abstract":"The proposed function of Cdc4p, an essential contractile ring protein in Schizosaccharomyces pombe, is that of a myosin essential light chain. However, five conditionally lethal cdc4 alleles exhibit complementation in diploids. Such interallelic complementation is not readily explained if the sole function of Cdc4p is that of a myosin essential light chain. Complementation of cdc4 alleles could occur only if different mutant forms can assemble into an active oligomeric complex or if Cdc4p has more than one essential function. To search for other proteins that may interact with Cdc4p, we performed a two-hybrid screen and identified two such candidates: one similar to Saccharomyces cerevisiae Vps27p and the other a putative phosphatidylinositol (PI) 4-kinase. Binding of Cdc4p to the latter and to myosin heavy chain (Myo2p) was confirmed by immunosorbent assays. Deletion studies demonstrated interaction between the Cdc4p C-terminal domain and the PI 4-kinase C-terminal domain. Furthermore, interaction was abolished by the Cdc4p C-terminal domain point mutation, Gly107 to Ser. This allele also causes failure of cytokinesis. Ectopic expression of the PI 4-kinase C-terminal domain caused cytokinesis defects that were most extreme in cells carrying the G107S allele. We suggest that Cdc4p plays multiple roles in cytokinesis and that interaction with a PI 4-kinase may be important for contractile ring assembly and/or function.","authors":"Desautels M, Den Haese JP, Slupsky CM, McIntosh LP, Hemmingsen SM","authors_abbrev":"Desautels M et al.","pubmed_publication_date":"23 Feb 2001","pubmed_entrez_date":"2000-11-23","publication_year":"2001","canto_session_key":"d7be232176eaf5f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-30 17:05:30","canto_approved_date":"2024-04-03 15:46:52","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-12-30 17:05:21","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAP8A3.08","SPAC22E12.16c","SPAC19A8.05c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2020-12-30"},{"uniquename":"PMID:10660466","title":"A cell viability assay based on monitoring respiration by optical oxygen sensing.","citation":"Anal Biochem 2000 Feb 15;278(2):221-7","abstract":"A cell viability assay based on monitoring of the metabolic activity of living cells via their consumption of dissolved oxygen has been developed. It uses a microwell plate format and disposable phosphorescent sensor inserts incorporated into each sample. The wells are subsequently sealed from ambient oxygen using a layer of mineral oil, and periodically scanned from underneath with a simple fiber-optic phosphorescent phase detector. Thus, dissolved oxygen levels and time profiles of cell respiration can be determined noninvasively and compared to each other. The system was tested by monitoring the viability of the fission yeast Schizosaccharomyces pombe. In comparison with the conventional cell densitometry assay, the optical oxygen sensor method could reliably monitor lower numbers of cells (10(4)-10(5) vs 10(6)-10(7) cells/ml for densitometry), and accurately determine culture viability within 1 h. The assay was then applied to determine the viability of samples treated with toxic agents such as azide and in response to expression of a physiological inducer of cell death, the Bcl-2 family member Bak. The results obtained confirm that measurement of cell respiration by this assay can serve as a predictable, reliable, and fast method for high-throughput determination of cell viability and growth.","authors":"O'Riordan TC, Buckley D, Ogurtsov V, O'Connor R, Papkovsky DB","authors_abbrev":"O'Riordan TC et al.","pubmed_publication_date":"15 Feb 2000","pubmed_entrez_date":"2000-02-08","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8782402","title":"Purification and some properties of phospholipase B from Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 1996 Jul;60(7):1087-92","abstract":"Phospholipase B from Schizosaccharomyces pombe was purified by ammonium sulfate fractionation and chromatographed on phenyl-Sepharose CL-4B, DEAE-Toyopearl 650M, and TSK gel G4000SW columns. The purified enzyme was a glycoprotein with molecular weight of approximately 300,000 and 100,000-150,000 by gel filtration and SDS-polyacrylamide gel electrophoresis, respectively. The isoelectric point was pH 4.7. The optimum pH of the enzyme was 2.5 and no activity was detected at neutral and alkaline pHs. The enzyme was not heat-stable. Enzyme activity was slightly stimulated by divalent ions except Fe2+ and 0.1% sodium deoxycholate, and inhibited by Fe2+, Fe3+, 0.1% sodium dodecyl sulfate, and 0.01% cetyltrimethylammonium bromide. The enzyme hydrolyzed mono- and diacylphospholipids, and phosphatidylinositol was hydrolyzed most preferentially. Triglyceride was not hydrolyzed. The enzyme also had acyltransferase activity on lysophosphatidylcholine, forming the corresponding diacylphosphatidylcholine.","authors":"Oishi H, Tsuda S, Watanabe Y, Tamai Y","authors_abbrev":"Oishi H et al.","pubmed_publication_date":"Jul 1996","pubmed_entrez_date":"1996-07-01","publication_year":"1996","canto_session_key":"2e95cca2fe376b8b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-02-01 18:11:37","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-02-01 18:11:02","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-02-01"},{"uniquename":"PMID:24269998","title":"Overcoming the metabolic burden of protein secretion in Schizosaccharomyces pombe--a quantitative approach using 13C-based metabolic flux analysis.","citation":"Metab Eng 2014 Jan;21:34-45","abstract":"Protein secretion in yeast is generally associated with a burden to cellular metabolism. To investigate this metabolic burden in Schizosaccharomyces pombe, we constructed a set of strains secreting the model protein maltase in different amounts. We quantified the influence of protein secretion on the metabolism applying (13)C-based metabolic flux analysis in chemostat cultures. Analysis of the macromolecular biomass composition revealed an increase in cellular lipid content at elevated levels of protein secretion and we observed altered metabolic fluxes in the pentose phosphate pathway, the TCA cycle, and around the pyruvate node including mitochondrial NADPH supply. Supplementing acetate to glucose or glycerol minimal media was found to improve protein secretion, accompanied by an increased cellular lipid content and carbon flux through the TCA cycle as well as increased mitochondrial NADPH production. Thus, systematic metabolic analyses can assist in identifying factors limiting protein secretion and in deriving strategies to overcome these limitations.","doi":"10.1016/j.ymben.2013.11.001","authors":"Klein T, Lange S, Wilhelm N, Bureik M, Yang TH, Heinzle E, Schneider K","authors_abbrev":"Klein T et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2013-11-26","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11533722","title":"A journey into space.","citation":"Nat Rev Mol Cell Biol 2001 Sep;2(9):647-56","abstract":"The fission yeast, Schizosaccharomyces pombe, has been used as a model eukaryote to study processes such as the cell cycle and cell morphology. In this single-celled organism, growing in a straight line and maintaining the nucleus in the centre of the cell depend on intracellular positional information. Microtubules and microtubular transport are important for generating positional information within the fission yeast cell, and these molecular mechanisms are also probably relevant for generating positional information in other eukaryotic cells.","authors":"Hayles J, Nurse P","authors_abbrev":"Hayles J et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-09-05","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8001791","title":"Three additional linkage groups that repress transcription and meiotic recombination in the mating-type region of Schizosaccharomyces pombe.","citation":"Genetics 1994 Sep;138(1):29-38","abstract":"The mating-type genes of Schizosaccharomyces pombe are found at three locations in the same chromosomal region. These genes are in an active configuration at the mat1 locus and in an inactive configuration at the mat2 and mat3 loci. The mechanism that represses transcription of mat2 and mat3 also inactivates other promoters introduced nearby and is accompanied by a block to meiotic recombination in the mat2-mat3 interval, suggesting that this mechanism involves a particular chromatin structure. We present evidence that the transcription and recombination blocks require three newly defined trans-acting loci, clr2, clr3 and clr4, in addition to the previously identified clr1, rik1 and swi6 loci. We also investigated the role of mat2 cis-acting sequences in silencing. Four cis-acting elements that repress mat2 in a plasmid context were previously identified. Deletion of two of these elements proved to have little effect in a chromosomal context. However, when combined with mutations in trans-acting genes, deletion of the same two elements greatly enhanced mat2 expression. The observed cumulative effects suggest a redundancy in the silencing mechanism.","authors":"Thon G, Cohen A, Klar AJ","authors_abbrev":"Thon G et al.","pubmed_publication_date":"Sep 1994","pubmed_entrez_date":"1994-09-01","publication_year":"1994","canto_session_key":"c29a669c56729926","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Genevieve Thon","canto_first_approved_date":"2013-11-18 11:20:22","canto_approved_date":"2021-11-24 21:21:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-13 17:56:32","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Genevieve Thon","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.17","SPBC428.08c","SPBC800.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-11-18"},{"uniquename":"PMID:33445784","title":"The  S. pombe  CDK5 Orthologue Pef1 Cooperates with Three Cyclins, Clg1, Pas1 and Psl1, to Promote Pre-Meiotic DNA Replication.","citation":"Biomolecules 2021 Jan 12;11(1)","abstract":"Meiosis is a specialized cell division process that mediates genetic information transfer to the next generation. Meiotic chromosomal segregation occurs when DNA replication is completed during the pre-meiotic S phase. Here, we show that  Schizosaccharomyces pombe  Pef1, an orthologue of mammalian cyclin-dependent kinase 5 (CDK5), is required to promote pre-meiotic DNA replication. We examined the efficiency of meiotic initiation using  pat1-114  mutants and found that, meiotic nuclear divisions did not occur in the  pef1Δ pat1-114  strain. Deletion of  pef1  also suppressed the expression of DNA replication factors and the phosphorylation of Cdc2 Tyr-15. The double deletion of  clg1  and  psl1  arrested meiotic initiation in  pat1-114  mutant cells, similar to that of  pef1 -deficient cells. Meiotic progression was also slightly delayed in the  pas1 -deficient strain. Our results reveal that Pef1 regulates cyclin-coordinated meiotic progression.","doi":"10.3390/biom11010089","authors":"Matsuda S, Kikkawa U, Nakashima A","authors_abbrev":"Matsuda S et al.","pubmed_publication_date":"12 Jan 2021","pubmed_entrez_date":"2021-01-15","publication_year":"2021","canto_session_key":"7b05e83a7380e28f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-01-17 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16C4.11","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"Pfam:PF06148","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC36.08c","HGNC:6546"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35820914","title":"Antagonistic effects of mitochondrial matrix and intermembrane space proteases on yeast aging.","citation":"BMC Biol 2022 Jul 12;20(1):160","abstract":"In many organisms, aging is characterized by a loss of mitochondrial homeostasis. Multiple factors such as respiratory metabolism, mitochondrial fusion/fission, or mitophagy have been linked to cell longevity, but the exact impact of each one on the aging process is still unclear.\nUsing the deletion mutant collection of the fission yeast Schizosaccharomyces pombe, we have developed a genome-wide screening for mutants with altered chronological lifespan. We have identified four mutants associated with proteolysis at the mitochondria that exhibit opposite effects on longevity. The analysis of the respiratory activity of these mutants revealed a positive correlation between increased respiration rate and prolonged lifespan. We also found that the phenotype of the long-lived protease mutants could not be explained by impaired mitochondrial fusion/fission activities, but it was dependent on mitophagy induction. The anti-aging role of mitophagy was supported by the effect of a mutant defective in degradation of mitochondria, which shortened lifespan of the long-lived mutants.\nOur characterization of the mitochondrial protease mutants demonstrates that mitophagy sustains the lifespan extension of long-lived mutants displaying a higher respiration potential.","doi":"10.1186/s12915-022-01352-w","authors":"Vega M, Castillo D, de Cubas L, Wang Y, Huang Y, Hidalgo E, Cabrera M","authors_abbrev":"Vega M et al.","pubmed_publication_date":"12 Jul 2022","pubmed_entrez_date":"2022-07-12","publication_year":"2022","canto_session_key":"00548851c7ec9684","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Montserrat Vega","canto_first_approved_date":"2024-12-30 19:18:58","canto_approved_date":"2025-01-01 15:40:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-29 19:49:46","canto_added_date":"2022-07-15 00:15:03","annotation_curators":[{"name":"Montserrat Vega","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":309,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_35820914_long_lived.phaf.tsv"},{"name":"Val Wood","community_curator":false,"annotation_count":163,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_35820914_short_lived.phaf.tsv"}],"genes":["SPAC26A3.09c","SPAC23D3.01","SPAC3A11.03","SPCC794.10","SPCC1235.11","SPAC694.02","SPBC36B7.02","SPAC1556.02c","SPBC428.05c","SPAC1F3.06c","SPAC23A1.06c","SPCC613.06","SPBPB10D8.02c","SPAC1006.09","SPCC965.04c","SPBC342.01c","SPCPB1C11.01","SPBC21C3.02c","SPBC1683.02","SPAC343.06c","SPMIT.01","SPBC215.14c","SPBC25B2.04c","SPCC126.04c","SPBC16G5.13","SPBC2D10.12","SPAC2G11.10c","SPAC1D4.06c","SPBC16G5.03","SPAC18G6.15","SPAC15E1.07c","SPBC646.13","SPBC1709.09","SPCC1223.01","SPAC1783.02c","SPBC713.09","SPBC215.02","SPAC29A4.05","SPAC4F10.14c","SPBC25H2.09","SPAC227.11c","SPBC28F2.10c","SPAC328.03","SPAC11E3.04c","SPBP23A10.14c","SPBC215.10","SPAC1002.12c","SPCC970.07c","SPBCPT2R1.03","SPAC1B3.08","SPBC106.17c","SPBC13E7.03c","SPCC550.08","SPCC553.03","SPCC794.07","SPBC9B6.07","SPCC31H12.06","SPBC16C6.03c","SPAC227.07c","SPAC57A7.08","SPMIT.04","SPAC4G8.06c","SPAC227.03c","SPCC1739.06c","SPAC26F1.08c","SPCC965.08c","SPBC12C2.08","SPAC4G9.16c","SPCC74.09","SPAC2C4.14c","SPCC622.14","SPBC887.11","SPAC2G11.05c","SPBC18E5.13","SPAC29E6.09","SPAC869.03c","SPCC16A11.04","SPBC19F8.02","SPBC1921.03c","SPBC3E7.02c","SPBC23G7.08c","SPAC683.02c","SPBC19C7.12c","SPBC651.09c","SPAPB24D3.04c","SPAC6F6.09","SPBC3H7.14","SPAC5H10.01","SPAC22F3.06c","SPAC3G6.01","SPAC1687.05","SPCC18.17c","SPBP8B7.21","SPCC4B3.03c","SPAC10F6.06","SPCC1393.09c","SPBC947.04","SPBC29A10.02","SPBC3E7.10","SPAC17A5.18c","SPBC3B9.05","SPAC1782.06c","SPBC15D4.09c","SPAC637.03","SPAC1D4.01","SPBC365.12c","SPAP8A3.13c","SPBPB10D8.05c","SPCC584.01c","SPAC7D4.03c","SPCC191.09c","SPBPB10D8.07c","SPBC106.10","SPAC1565.03","SPCC1235.12c","SPBC609.05","SPAC4F10.04","SPBC24C6.06","SPCC306.11","SPCC965.10","SPAC9E9.05","SPBC12C2.12c","SPAC17A5.11","SPBC365.10","SPAC20H4.02","SPAC17H9.09c","SPCC777.13","SPBC530.08","SPBC428.11","SPAC9G1.04","SPAPB8E5.08","SPAC9E9.09c","SPAC3F10.16c","SPCC16A11.01","SPCC584.13","SPBC776.11","SPCC1682.01","SPBC12C2.02c","SPAC750.06c","SPAC24B11.10c","SPBP8B7.23","SPAC890.07c","SPAC1A6.08c","SPBC887.10","SPAC11E3.08c","SPAC29A4.02c","SPAC6F6.11c","SPBC1683.07","SPCC736.11","SPAC57A7.07c","SPAC17G6.15c","SPBC839.06","SPAC1805.10","SPAC1687.12c","SPCC594.02c","SPBC1D7.04","SPCC1020.07","SPBC18H10.18c","SPAC13G7.07","SPAP14E8.02","SPCC188.09c","SPAC6F6.01","SPAC2C4.08","SPAC16A10.05c","SPBC354.05c","SPAC17D4.03c","SPCC663.04","SPBC21C3.20c","SPAC1782.04","SPAC26A3.10","SPBC1778.02","SPAC30D11.02c","SPAC630.14c","SPCC1235.15","SPBC3D6.02","SPAC8E11.05c","SPAC5H10.02c","SPBC1539.03c","SPAP32A8.02","SPAC1639.02c","SPBC359.01","SPCC1442.02","SPBC21B10.08c","SPAC23C11.08","SPAC664.12c","SPAC19B12.07c","SPCC4B3.06c","SPCC1281.07c","SPBC23G7.12c","SPBP4H10.12","SPCC777.06c","SPAC16.04","SPBC359.05","SPAC25B8.09","SPCC1739.08c","SPAC3G9.03","SPAC3G9.08","SPCC364.06","SPAC1002.17c","SPAC20G8.10c","SPBC30D10.18c","SPBC800.11","SPAC24B11.12c","SPBC29B5.02c","SPAC30C2.05","SPCC622.15c","SPBC16D10.02","SPAC3H8.02","SPAC6G10.11c","SPCC584.16c","SPBP26C9.02c","SPAC8E11.02c","SPAPB8E5.06c","SPCC737.06c","SPBC14F5.13c","SPAC1002.18","SPCC126.09","SPCC1682.12c","SPBC1921.04c","SPBC31F10.05","SPAC3H5.08c","SPBC1347.07","SPAC222.08c","SPBC28E12.04","SPAC16C9.05","SPBC543.09","SPBC3E7.15c","SPAC10F6.12c","SPAC1556.04c","SPBC13G1.10c","SPAC2F3.11","SPBC1709.14","SPAC30.02c","SPAC4D7.06c","SPBC16G5.17","SPAC56E4.07","SPAC144.01","SPBC11G11.01","SPAC1751.04","SPAP7G5.04c","SPAC13G7.03","SPBC1718.03","SPBC3B8.03","SPBC530.05","SPAC24C9.08","SPAC22G7.08","SPCC330.11","SPCC1682.14","SPAC13G6.02c","SPBC3E7.08c","SPAC6G10.08","SPBC27.08c","SPAC6G9.04","SPBC365.03c","SPMIT.11","SPACUNK4.19","SPCC584.02","SPBC800.04c","SPAC1071.07c","SPAC6G10.10c","SPCC1919.04","SPAC31A2.13c","SPBC1734.11","SPAC3A11.07","SPCC16C4.01","SPAC589.11","SPCC1795.03","SPAC17D4.04","SPCC553.01c","SPBC530.11c","SPBC2F12.03c","SPBC800.08","SPBC32F12.11","SPAC17H9.13c","SPAC1D4.05c","SPBC336.03","SPAC30C2.07","SPAC1420.03","SPAC4G8.10","SPAC23D3.03c","SPAC24B11.09","SPAC14C4.11","SPAC4G8.05","SPBC1105.04c","SPCC1442.17c","SPAC15E1.09","SPCC1753.02c","SPAC18B11.04","SPBC2A9.02","SPBC16E9.06c","SPAC2G11.03c","SPCC70.10","SPBPB2B2.10c","SPAC343.20","SPBC2D10.20","SPAC1610.01","SPCC1840.03","SPBC2G5.02c","SPAC2G11.07c","SPAC57A10.08c","SPBC713.07c","SPCC1442.16c","SPAC1296.02","SPAC17A2.06c","SPAC1F5.03c","SPAC4G9.10","SPAC19G12.15c","SPAC977.16c","SPAC3H5.12c","SPAC57A10.06","SPCC622.08c","SPCC962.04","SPAC1687.15","SPBC1718.06","SPAC19G12.03","SPCC1442.05c","SPAC5D6.02c","SPAC1296.04","SPCC1259.11c","SPAC31G5.14","SPCC1919.12c","SPAC13G7.12c","SPCC297.05","SPCC737.04","SPBC1683.03c","SPBC1861.07","SPAC20H4.10","SPAP14E8.04","SPAC1F3.03","SPCC1620.04c","SPCC2H8.05c","SPCC550.07","SPAC3A12.10","SPBC8D2.02c","SPCC1919.13c","SPBP35G2.07","SPAC6G9.09c","SPAC2F7.03c","SPAC7D4.08","SPAC12B10.11","SPBP8B7.25","SPAC56F8.14c","SPAC1786.04","SPBC29A10.12","SPBC1683.09c","SPAC4G9.15","SPAC227.06","SPCC162.01c","SPAC26F1.10c","SPAC3H8.09c","SPAC4D7.11","SPAC694.06c","SPAC513.03","SPBC17A3.10","SPAC6C3.06c","SPCC31H12.02c","SPBC18E5.07","SPAC22E12.18","SPCC338.08","SPCC757.09c","SPAC1071.11","SPAC6F12.06","SPAC4C5.02c","SPCC1620.07c","SPAC3C7.03c","SPBC543.07","SPBC29A3.10c","SPAC8C9.07","SPBC16D10.05","SPAC13C5.04","SPBC8E4.03","SPBC19F8.06c","SPBC1D7.03","SPAC2F3.18c","SPAC6F12.04","SPCC736.02","SPAC3A12.17c","SPAC3H8.08c","SPAC1B3.03c","SPBC20F10.07","SPAPB2C8.01","SPAC23H3.13c","SPAP27G11.02","SPAC1F7.11c","SPAC1952.05","SPCC16C4.06c","SPAC12G12.03","SPAC22F8.03c","SPAC18B11.07c","SPAC24B11.06c","SPBC409.16c","SPAC1039.04","SPCC777.15","SPBC4F6.06","SPAC23A1.16c","SPAPB24D3.07c","SPAC1687.06c","SPAC8E11.01c","SPBC31F10.09c","SPAC17C9.07","SPAC222.05c","SPBC3D6.04c","SPAC227.14","SPAC31A2.09c","SPBC215.05","SPAC3G6.03c","SPBC19G7.02","SPCC18.02","SPBC354.07c","SPAC17A2.09c","SPAC1F7.09c","SPAC11D3.03c","SPBC16H5.08c","SPAC22H10.09","SPBC1861.05","SPAC1805.09c","SPBC30D10.10c","SPBC947.14c","SPBC582.10c","SPCC777.10c","SPAC1002.02","SPAC26F1.09","SPCC24B10.08c","SPCC11E10.07c","SPCC1183.11","SPBC1D7.05","SPAC343.15","SPCC794.03","SPBC21C3.11","SPMIT.07","SPAC823.03","SPBC21C3.13","SPBC14F5.10c","SPAC23C11.01","SPCC16C4.14c","SPBC337.09","SPBC646.06c","SPBC17D11.03c","SPAC1002.03c","SPCC1235.09","SPAC27D7.09c","SPBC1711.03","SPBC902.05c","SPBC2G5.06c","SPAC1952.09c","SPAC23G3.05c","SPAC56F8.16","SPAC17D4.01","SPCC1281.04","SPBC21B10.12","SPCC1322.02","SPAC6G10.03c","SPBC3E7.16c","SPAC17G8.09","SPBC12C2.07c","SPCC126.01c","SPCC23B6.05c","SPAC1782.08c","SPBC1711.13","SPBC36.04","SPCC1235.08c","SPAC26A3.07c","SPBC1289.10c","SPAC869.11","SPBC24C6.09c","SPCC74.06","SPBC1105.13c","SPAC9.08c","SPBC16A3.02c","SPAC23C4.09c","SPAC664.04c","SPBC32H8.07","SPAC3C7.14c","SPBC16A3.08c","SPCC1739.07","SPAC806.07","SPAC1071.04c","SPBC713.03","SPAC1399.02","SPBC18H10.08c","SPAC14C4.01c","SPAC17G8.05"],"gene_count":482,"ltp_gene_count":478,"approved_date":"2024-12-30"},{"uniquename":"PMID:12582133","title":"Bgs3p, a putative 1,3-beta-glucan synthase subunit, is required for cell wall assembly in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2003 Feb;2(1):159-69","abstract":"beta-Glucans are the main components of the fungal cell wall. Fission yeast possesses a family of beta-glucan synthase-related genes. We describe here the cloning and characterization of bgs3(+), a new member of this family. bgs3(+) was cloned as a suppressor of a mutant hypersensitive to Echinocandin and Calcofluor White, drugs that interfere with cell wall biosynthesis. Disruption of the gene is lethal, and a decrease in Bgs3p levels leads to rounded cells with thicker walls, slightly reduces the amount of the beta-glucan, and raises the amount of alpha-glucan polymer. These cells finally died. bgs3(+) is expressed in vegetative cells grown in different conditions and during mating and germination and is not enhanced by stress situations. Consistent with the observed expression pattern, Bgs3-green fluorescence protein (GFP-Bgs3p) was found at the growing tips during interphase and at the septum prior to cytokinesis, always localized to growth areas. We also found GFP-Bgs3p in mating projections, during the early stages of zygote formation, and at the growing pole during ascospore germination. We conclude that Bgs3p localization is restricted to growth areas and that Bgs3p is a glucan synthase homologue required for cell wall biosynthesis and cell elongation in the fission yeast life cycle.","authors":"Martín V, García B, Carnero E, Durán A, Sánchez Y","authors_abbrev":"Martín V et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-02-13","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19B12.03"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:18753627","title":"Mcm4 C-terminal domain of MCM helicase prevents excessive formation of single-stranded DNA at stalled replication forks.","citation":"Proc Natl Acad Sci U S A 2008 Sep 02;105(35):12973-8","abstract":"The minichromosome maintenance (MCM) helicase, composed of subunits Mcm2-7, is essential for the initiation and elongation phases of DNA replication. Even when DNA synthesis is blocked, MCM continues DNA unwinding to some extent for activation of the replication checkpoint and then stops. However, the mechanism of regulation of MCM-helicase activity remains unknown. Here, we show that truncation of the Mcm4 C-terminal domain (CTD) in fission yeast results in hypersensitivity to replication block caused by dNTP depletion. The truncation mcm4-c84 does not affect the activation of the replication checkpoint pathway but delays its attenuation during recovery from replication block. Two dimensional gel electrophoresis showed that mcm4-c84 delays the disappearance of replication intermediates, indicating that the Mcm4 CTD is required for efficient recovery of stalled replication forks. Remarkably, chromatin immunoprecipitation revealed that mcm4-c84 brings about an increase rather than a decrease in the association of the single-stranded DNA-binding protein RPA to stalled forks, and MCM and the accessory complex GINS are unaffected. These results suggest that the Mcm4 CTD is required to suspend MCM-helicase activity after the formation of single-stranded DNA sufficient for checkpoint activation.","doi":"10.1073/pnas.0805307105","authors":"Nitani N, Yadani C, Yabuuchi H, Masukata H, Nakagawa T","authors_abbrev":"Nitani N et al.","pubmed_publication_date":"02 Sep 2008","pubmed_entrez_date":"2008-08-30","publication_year":"2008","canto_session_key":"de1e1946e680a0bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-22 16:44:28","canto_approved_date":"2023-08-31 08:44:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-20 13:40:36","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPCC16A11.17","SPBC216.05","SPCC1753.01c","SPCC18B5.11c","SPAC1F7.05","SPBC725.13c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2015-12-22"},{"uniquename":"PMID:31129857","title":"Spatiotemporal control of spindle disassembly in fission yeast.","citation":"Cell Mol Life Sci 2019 Sep;76(18):3543-3551","abstract":"Maintenance of genomic stability during cell division is one of the most important cellular tasks, and it critically depends on the faithful replication of the genetic material and its equal partitioning into daughter cells, gametes, or spores in the case of yeasts. Defective mitotic spindle assembly and disassembly both result in changes in cellular ploidy that ultimately impinge proliferation fitness and might increase tumor malignancy. Although a great progress has been made in understanding how spindles are assembled to orchestrate chromosome segregation, much less is known about how they are disassembled once completed their function. Here, we review two recently uncovered mechanisms of spindle disassembly that operate at different stages of the fission yeast life cycle.","doi":"10.1007/s00018-019-03139-9","authors":"Salas-Pino S, Daga RR","authors_abbrev":"Salas-Pino S et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-05-27","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-29 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15004232","title":"Identification and characterization of two novel proteins affecting fission yeast gamma-tubulin complex function.","citation":"Mol Biol Cell 2004 May;15(5):2287-301","abstract":"The gamma-tubulin complex, via its ability to organize microtubules, is critical for accurate chromosome segregation and cytokinesis in the fission yeast, Schizosaccharomyces pombe. To better understand its roles, we have purified the S. pombe gamma-tubulin complex. Mass spectrometric analyses of the purified complex revealed known components and identified two novel proteins (i.e., Mbo1p and Gfh1p) with homology to gamma-tubulin-associated proteins from other organisms. We show that both Mbo1p and Gfh1p localize to microtubule organizing centers. Although cells deleted for either mbo1(+) or gfh1(+) are viable, they exhibit a number of defects associated with altered microtubule function such as defects in cell polarity, nuclear positioning, spindle orientation, and cleavage site specification. In addition, mbo1Delta and gfh1Delta cells exhibit defects in astral microtubule formation and anchoring, suggesting that these proteins have specific roles in astral microtubule function. This study expands the known roles of gamma-tubulin complex components in organizing different types of microtubule structures in S. pombe.","authors":"Venkatram S, Tasto JJ, Feoktistova A, Jennings JL, Link AJ, Gould KL","authors_abbrev":"Venkatram S et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-03-09","publication_year":"2004","canto_session_key":"b5fde7a48c34bee4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-06 21:38:02","canto_approved_date":"2022-07-21 08:18:17","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2016-09-27 16:06:22","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.06c","SPBC365.15","SPBC428.13c","SPAC3A12.14","SPCC417.07c","SPBC428.20c","SPBC211.06","SPCC4G3.19","SPBC32F12.04"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-10-06"},{"uniquename":"PMID:11861905","title":"Glucose-inducible expression of rrg1+ in Schizosaccharomyces pombe: post-transcriptional regulation of mRNA stability mediated by the downstream region of the poly(A) site.","citation":"Nucleic Acids Res 2002 Mar 01;30(5):1145-53","abstract":"rrg1+(rapid response to glucose) has been isolated previously as a UV-inducible gene in Schizosaccharomyces pombe, designated as uvi22+. However, it was revealed that the transcript level of this gene was regulated by glucose, not by DNA-damaging agents. Glucose depletion led to a rapid decrease in the level of rrg1+ mRNA, by approximately 50% within 30 min. This effect was readily reversed upon re-introduction of glucose within 1 h. High concentrations (4 and 8%) of glucose showed similar effects on increasing the rrg1+ mRNA level compared with 2% glucose, while a low concentration (0.1%) was not effective in raising the rrg1+ mRNA level. In addition, sucrose and fructose could increase rrg1+ mRNA level. Interestingly, the rapid decline in mRNA level seen upon glucose deprivation resulted from precipitous reduction of mRNA half-life. Serial and internal deletions within the 3'-flanking region of rrg1+ revealed that a 210-nt region downstream of the distal poly(A) site was critical for glucose-regulated expression. Moreover, this downstream region participated in 3'-end formation of mRNA. Taken together, this is the first report on glucose-inducible expression regulated post-transcriptionally by control of mRNA stability in S.pombe.","authors":"Kim MJ, Kim JB, Kim DS, Park SD","authors_abbrev":"Kim MJ et al.","pubmed_publication_date":"01 Mar 2002","pubmed_entrez_date":"2002-02-28","publication_year":"2002","canto_session_key":"c8ccb11c47a11d42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-02-02 09:52:00","canto_approved_date":"2022-02-07 19:23:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-28 20:47:42","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-02-02"},{"uniquename":"PMID:21993292","title":"Microtubule nucleation by γ-tubulin complexes.","citation":"Nat Rev Mol Cell Biol 2011 Oct 12;12(11):709-21","abstract":"Microtubule nucleation is regulated by the γ-tubulin ring complex (γTuRC) and related γ-tubulin complexes, providing spatial and temporal control over the initiation of microtubule growth. Recent structural work has shed light on the mechanism of γTuRC-based microtubule nucleation, confirming the long-standing hypothesis that the γTuRC functions as a microtubule template. The first crystallographic analysis of a non-γ-tubulin γTuRC component (γ-tubulin complex protein 4 (GCP4)) has resulted in a new appreciation of the relationships among all γTuRC proteins, leading to a refined model of their organization and function. The structures have also suggested an unexpected mechanism for regulating γTuRC activity via conformational modulation of the complex component GCP3. New experiments on γTuRC localization extend these insights, suggesting a direct link between its attachment at specific cellular sites and its activation.","doi":"10.1038/nrm3209","authors":"Kollman JM, Merdes A, Mourey L, Agard DA","authors_abbrev":"Kollman JM et al.","pubmed_publication_date":"12 Oct 2011","pubmed_entrez_date":"2011-10-14","publication_year":"2011","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC211.06","SPBC365.15","SPBC428.20c","SPCC4G3.19","SPAC806.08c"],"gene_count":5,"ltp_gene_count":0},{"uniquename":"PMID:24847916","title":"Genome-wide screens for sensitivity to ionizing radiation identify the fission yeast nonhomologous end joining factor Xrc4.","citation":"G3 (Bethesda) 2014 May 21;4(7):1297-306","abstract":"Nonhomologous end joining (NHEJ) is the main means for repairing DNA double-strand breaks (DSBs) in human cells. Molecular understanding of NHEJ has benefited from analyses in the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe. In human cells, the DNA ligation reaction of the classical NHEJ pathway is carried out by a protein complex composed of DNA ligase IV (LigIV) and XRCC4. In S. cerevisiae, this reaction is catalyzed by a homologous complex composed of Dnl4 and Lif1. Intriguingly, no homolog of XRCC4 has been found in S. pombe, raising the possibility that such a factor may not always be required for classical NHEJ. Here, through screening the ionizing radiation (IR) sensitivity phenotype of a genome-wide fission yeast deletion collection in both the vegetative growth state and the spore state, we identify Xrc4, a highly divergent homolog of human XRCC4. Like other fission yeast NHEJ factors, Xrc4 is critically important for IR resistance of spores, in which no homologous recombination templates are available. Using both extrachromosomal and chromosomal DSB repair assays, we show that Xrc4 is essential for classical NHEJ. Exogenously expressed Xrc4 colocalizes with the LigIV homolog Lig4 at the chromatin region of the nucleus in a mutually dependent manner. Furthermore, like their human counterparts, Xrc4 and Lig4 interact with each other and this interaction requires the inter-BRCT linker and the second BRCT domain of Lig4. Our discovery of Xrc4 suggests that an XRCC4 family protein is universally required for classical NHEJ in eukaryotes.","doi":"10.1534/g3.114.011841","authors":"Li J, Yu Y, Suo F, Sun LL, Zhao D, Du LL","authors_abbrev":"Li J et al.","pubmed_publication_date":"21 May 2014","pubmed_entrez_date":"2014-05-23","publication_year":"2014","canto_session_key":"21c36c32abbfd61b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun Li","canto_first_approved_date":"2014-10-30 14:59:11","canto_approved_date":"2025-09-03 17:23:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-30 05:41:56","canto_added_date":"2014-06-04 10:44:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jun Li","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC24B10.14c","YGL090W","HGNC:12831","SPBC543.03c","SPAC6G9.16c","SPAC2F7.06c","SPCC126.02c","SPCC1183.05c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-10-30"},{"uniquename":"PMID:12718879","title":"Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p.","citation":"Mol Cell 2003 Apr;11(4):927-38","abstract":"The COP9/signalosome (CSN) is known to remove the stimulatory NEDD8 modification from cullins. The activity of the fission yeast cullins Pcu1p and Pcu3p is dramatically stimulated when retrieved from csn mutants but inhibited by purified CSN. This inhibition is independent of cullin deneddylation but mediated by the CSN-associated deubiquitylating enzyme Ubp12p, which forms a complex with Pcu3p in a CSN-dependent manner. In ubp12 mutants, as in csn mutants, Pcu3p activity is stimulated. CSN is required for efficient targeting of Ubp12p to the nucleus, where both cullins reside. Finally, the CSN/Ubp12p pathway maintains the stability of the Pcu1p-associated substrate-specific adaptor protein Pop1p. We propose that CSN/Ubp12p-mediated deubiquitylation creates an environment for the safe de novo assembly of cullin complexes by counteracting the autocatalytic destruction of adaptor proteins.","authors":"Zhou C, Wee S, Rhee E, Naumann M, Dubiel W, Wolf DA","authors_abbrev":"Zhou C et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-04-30","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1494.05c","SPAC1687.13c","SPBC215.03c","SPAC24H6.03"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:29855479","title":"Fission Yeast Sirtuin Hst4 Functions in Preserving Genomic Integrity by Regulating Replisome Component Mcl1.","citation":"Sci Rep 2018 May 31;8(1):8496","abstract":"The Schizosaccharomyces pombe sirtuin Hst4, functions in the maintenance of genome stability by regulating histone H3 lysine56 acetylation (H3K56ac) and promoting cell survival during replicative stress. However, its molecular function in DNA damage survival is unclear. Here, we show that hst4 deficiency in the fission yeast causes S phase delay and DNA synthesis defects. We identified a novel functional link between hst4 and the replisome component mcl1 in a suppressor screen aimed to identify genes that could restore the slow growth and Methyl methanesulphonate (MMS) sensitivity phenotypes of the hst4Δ mutant. Expression of the replisome component Mcl1 rescues hst4Δ phenotypes. Interestingly, hst4 and mcl1 show an epistatic interaction and suppression of hst4Δ phenotypes by mcl1 is H3K56 acetylation dependent. Furthermore, Hst4 was found to regulate the expression of mcl1. Finally, we show that hSIRT2 depletion results in decreased levels of And-1 (human orthologue of Mcl1), establishing the conservation of this mechanism. Moreover, on induction of replication stress (MMS treatment), Mcl1 levels decrease upon Hst4 down regulation. Our results identify a novel function of Hst4 in regulation of DNA replication that is dependent on H3K56 acetylation. Both SIRT2 and And-1 are deregulated in cancers. Therefore, these findings could be of therapeutic importance in future.","doi":"10.1038/s41598-018-26476-4","authors":"Konada L, Aricthota S, Vadla R, Haldar D","authors_abbrev":"Konada L et al.","pubmed_publication_date":"31 May 2018","pubmed_entrez_date":"2018-06-02","publication_year":"2018","canto_session_key":"1b21fcb464449578","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-06-03 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1834.04","SPAPB1E7.02c","SPAC1783.04c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:39934121","title":"Conserved GTPase OLA1 promotes efficient translation on D/E-rich mRNA.","citation":"Nat Commun 2025 Feb 11;16(1):1549","abstract":"The TRAFAC (translation factors) GTPase OLA1 plays a critical role in various stress responses and is implicated in the regulation of tumor progression. It is conserved from bacteria to eukaryotes and regulates the translation through binding to the ribosome. Here, we report the cryo-electron microscopy structure of its Escherichia coli homolog, YchF, with the 50S subunit. In this structure, YchF is positioned at the side of the 50S subunit by engaging with uL14, bL19, and rRNA helix H62 through its helical and ATPase domains. We further demonstrate that the helical domain is essential for OLA1/YchF to function. A comprehensive analysis of the structure and Ribo-seq data points out that OLA1/YchF promotes the splitting of ribosomes into subunits on D/E-rich mRNA. Our findings provide crucial structural insights into the molecular mechanism of OLA1/YchF-associated translation-stalling regulation, which maintains the translation of genes involved in stress response and tumor progression.","doi":"10.1038/s41467-025-56797-8","authors":"Yu T, Li X, Dong W, Zhou Q, Li Q, Du Z, Zeng F","authors_abbrev":"Yu T et al.","pubmed_publication_date":"11 Feb 2025","pubmed_entrez_date":"2025-02-11","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27E2.03c","SPACUNK4.13c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8569688","title":"Caffeine-resistance in fission yeast is caused by mutations in a single essential gene, crm1+.","citation":"Mol Gen Genet 1996 Jan 15;250(1):59-68","abstract":"Caffeine is a base analogue and is known to affect a wide variety of cellular processes. In order to dissect genetically molecules which mediate the biological effects of caffeine, temperature-sensitive (ts) and caffeine-resistant mutants were isolated from fission yeast, Schizosaccharomyces pombe. Surprisingly, all twelve ts isolates contained a mutation in the same locus, crm1. Cells of the ts crm1 mutant showed an abnormal chromosome structure at the restrictive temperature, an elevated expression of Pap1-dependent transcription, and cross-resistance to an unrelated drug such as staurosporine. Overproduction of pap1+ also conferred caffeine resistance, whilst the resistance of the crm1 mutant is abolished in the pap1- background. These results show that the crm1+ gene is a major locus for caffeine resistance, which arises from Pap1-dependent transcriptional activation.","authors":"Kumada K, Yanagida M, Toda T","authors_abbrev":"Kumada K et al.","pubmed_publication_date":"15 Jan 1996","pubmed_entrez_date":"1996-01-15","publication_year":"1996","canto_session_key":"0e62c4b4df94eb73","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-12 16:12:50","canto_approved_date":"2026-01-29 21:02:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-03-16 14:28:55","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.14c","SPAC31G5.13","SPAC1783.07c","SPAC1805.17"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2012-12-12"},{"uniquename":"PMID:18978356","title":"Formin differentially utilizes profilin isoforms to rapidly assemble actin filaments.","citation":"J Biol Chem 2009 Jan 02;284(1):673-684","abstract":"Cells contain multiple formin isoforms that drive the assembly of profilin-actin for diverse processes. Given that many organisms also contain several profilin isoforms, specific formin/profilin pairs might be matched to optimally stimulate actin polymerization. We utilized a combination of bulk actin polymerization and single filament total internal reflection fluorescence microscopy assays to measure the effect of different profilin isoforms on the actin assembly properties of the cytokinesis formins from fission yeast (Cdc12p) and the nematode worm (CYK-1). We discovered that Cdc12p only effectively utilizes the single fission yeast profilin isoform SpPRF. Conversely, CYK-1 prefers the essential worm cytokinesis profilin CePFN-1 to the two non-essential worm profilin isoforms (SpPRF = CePFN-1 > CePFN-2 > CePFN-3). Chimeras containing the profilin-binding formin homology 1 (FH1) domain from one formin and the barbed-end associated FH2 domain from the other formin, revealed that both the FH1 and FH2 domains help confer profilin isoform specialization. Although the Cdc12p and CYK-1 FH1 domains cannot differentiate between profilin isoforms in the absence of actin, formin FH1 domains appear to preferentially select specific isoforms of profilin-actin. Surprisingly, analysis of profilin point mutants revealed that differences in highly conserved residues in both the poly-L-proline and actin binding regions of profilin do not explain their differential utilization by formin. Therefore, rapid formin-mediated elongation of profilin-actin depends upon favorable interactions of profilin-actin with the FH1 domain as well as the barbed-end associated FH2 domain. Specific formin FH1FH2 domains are tailored to optimally utilize actin bound to particular profilin isoforms.","doi":"10.1074/jbc.M804201200","authors":"Neidt EM, Scott BJ, Kovar DR","authors_abbrev":"Neidt EM et al.","pubmed_publication_date":"02 Jan 2009","pubmed_entrez_date":"2008-11-04","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10926502","title":"Sequence conservation provides the best prediction of the role of proline residues in p13suc1.","citation":"J Mol Biol 2000 Aug 04;301(1):199-204","abstract":"The unique nature of the proline side-chain imposes severe constraints on the polypeptide backbone, and thus it seems likely that it plays a special structural or functional role in the architecture of proteins. We have investigated the role of proline residues in suc1, a member of the cyclin-dependent kinase (cks) family of proteins, whose known function is to bind to and regulate the activity of the major mitotic cdk. The effect on stability of mutation to alanine of all but two of the eight proline residues is correlated with their conservation within the family. The remaining two proline residues are located in the hinge loop between two beta-strands that mediates a domain-swapping process involving exchange of a beta-strand between two monomers to form a dimer pair. Mutation of these proline residues to alanine stabilises the protein. cdk binding is unaffected by these mutations, but dimerisation is altered. We propose, therefore, that the double-proline motif is conserved for the purpose of domain swapping, which suggests that this phenomenon plays a role in the function of cks proteins. Thus, the conservation of the proline residues is a good indicator of their roles in suc1, either in the stabilisation of the native state or in performing functions that are as yet unknown. In addition, the strain resulting from two of the proline residues was relieved successfully by mutation of the preceeding residue to glycine, suggesting a general method for designing more stable proteins.","authors":"Schymkowitz JW, Rousseau F, Itzhaki LS","authors_abbrev":"Schymkowitz JW et al.","pubmed_publication_date":"04 Aug 2000","pubmed_entrez_date":"2000-08-05","publication_year":"2000","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38117001","title":"Schizosaccharomyces pombe as a fundamental model for research on mitochondrial gene expression: Progress, achievements and outlooks.","citation":"IUBMB Life 2023 Dec 20;","abstract":"Schizosaccharomyces pombe (fission yeast) is an attractive model for mitochondrial research. The organism resembles human cells in terms of mitochondrial inheritance, mitochondrial transport, sugar metabolism, mitogenome structure and dependence of viability on the mitogenome (the petite-negative phenotype). Transcriptions of these genomes produce only a few polycistronic transcripts, which then undergo processing as per the tRNA punctuation model. In general, the machinery for mitochondrial gene expression is structurally and functionally conserved between fission yeast and humans. Furthermore, molecular research on S. pombe is supported by a considerable number of experimental techniques and database resources. Owing to these advantages, fission yeast has significantly contributed to biomedical and fundamental research. Here, we review the current state of knowledge regarding S. pombe mitochondrial gene expression, and emphasise the pertinence of fission yeast as both a model and tool, especially for studies on mitochondrial translation.","doi":"10.1002/iub.2801","authors":"Dinh N, Bonnefoy N","authors_abbrev":"Dinh N et al.","pubmed_publication_date":"20 Dec 2023","pubmed_entrez_date":"2023-12-20","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-12-21 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11973289","title":"Different phenotypes in vivo are associated with ATPase motif mutations in Schizosaccharomyces pombe minichromosome maintenance proteins.","citation":"Genetics 2002 Apr;160(4):1305-18","abstract":"The six conserved MCM proteins are essential for normal DNA replication. They share a central core of homology that contains sequences related to DNA-dependent and AAA(+) ATPases. It has been suggested that the MCMs form a replicative helicase because a hexameric subcomplex formed by MCM4, -6, and -7 proteins has in vitro DNA helicase activity. To test whether ATPase and helicase activities are required for MCM protein function in vivo, we mutated conserved residues in the Walker A and Walker B motifs of MCM4, -6, and -7 and determined that equivalent mutations in these three proteins have different in vivo effects in fission yeast. Some mutations reported to abolish the in vitro helicase activity of the mouse MCM4/6/7 subcomplex do not affect the in vivo function of fission yeast MCM complex. Mutations of consensus CDK sites in Mcm4p and Mcm7p also have no phenotypic consequences. Co-immunoprecipitation analyses and in situ chromatin-binding experiments were used to study the ability of the mutant Mcm4ps to associate with the other MCMs, localize to the nucleus, and bind to chromatin. We conclude that the role of ATP binding and hydrolysis is different for different MCM subunits.","authors":"Gómez EB, Catlett MG, Forsburg SL","authors_abbrev":"Gómez EB et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-26","publication_year":"2002","canto_session_key":"0d06afc3089ee763","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-15 12:43:16","canto_approved_date":"2024-04-04 09:53:32","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-11-15 17:26:37","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4.04c","SPAC1B2.05","SPBC211.04c","SPCC16A11.17","SPBC25D12.03c","SPCC1682.02c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-06-15"},{"uniquename":"PMID:37990810","title":"Cellular responses to compound stress induced by atmospheric-pressure plasma in fission yeast.","citation":"J Cell Sci 2023 Dec 01;136(23)","abstract":"The stress response is one of the most fundamental cellular processes. Although the molecular mechanisms underlying responses to a single stressor have been extensively studied, cellular responses to multiple stresses remain largely unknown. Here, we characterized fission yeast cellular responses to a novel stress inducer, non-thermal atmospheric-pressure plasma. Plasma irradiation generates ultraviolet radiation, electromagnetic fields and a variety of chemically reactive species simultaneously, and thus can impose multiple stresses on cells. We applied direct plasma irradiation to fission yeast and showed that strong plasma irradiation inhibited fission yeast growth. We demonstrated that mutants lacking sep1 and ace2, both of which encode transcription factors required for proper cell separation, were resistant to plasma irradiation. Sep1-target transcripts were downregulated by mild plasma irradiation. We also demonstrated that plasma irradiation inhibited the target of rapamycin kinase complex 1 (TORC1). These observations indicate that two pathways, namely the Sep1-Ace2 cell separation pathway and TORC1 pathway, operate when fission yeast cope with multiple stresses induced by plasma irradiation.","doi":"10.1242/jcs.261292","authors":"Otsubo Y, Yamashita A, Goto Y, Sakai K, Iida T, Yoshimura S, Johzuka K","authors_abbrev":"Otsubo Y et al.","pubmed_publication_date":"01 Dec 2023","pubmed_entrez_date":"2023-11-22","publication_year":"2023","canto_session_key":"9de1d7e0ee730091","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-11-23 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10417652","title":"An RGS protein regulates the pheromone response in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Microbiol 1999 Aug;33(3):623-34","abstract":"The rate and extent of a cell's response to an extracellular stimulus is influenced by regulators that act on the intracellular signalling machinery. Although not directly involved in propagating the intracellular signal, regulators control the activity of the proteins that transmit the signals. To understand this aspect of cell signalling, we have studied the pheromone response pathway in the fission yeast Schizosaccharomyces pombe, a relatively simple signalling system in a genetically tractable organism. We demonstrate this approach by investigating the role of Rgs1, a member of the Regulator of G protein Signalling (RGS) family of proteins. The rgs1 gene was identified through the Sz. pombe genome sequencing project (accession number Q09777) and recognized as having similarity to RGS proteins [Tesmer et al. (1997) Cell 89: 251-261], but this is the first report concerning the activity of the protein. Strains lacking rgs1 (Deltargs1) are hypersensitive to pheromone stimulation and unable to conjugate with a mating partner. Inhibition of mating occurs at a relative late stage in the process as Deltargs1 strains exhibit pheromone-dependent transcription and form shmoos. Expression of SST2 (an RGS protein that regulates pheromone signalling in the budding yeast Saccharomyces cerevisiae) overcomes the hypersensitivity of the Deltargs1 strains but fails to rescue their mating defect.","authors":"Watson P, Davis K, Didmon M, Broad P, Davey J","authors_abbrev":"Watson P et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-07-27","publication_year":"1999","canto_session_key":"2ad41d1fab1e751c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-24 09:28:15","canto_approved_date":"2020-12-03 17:13:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-02-18 18:33:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-24"},{"uniquename":"PMID:26455310","title":"Wall mechanics and exocytosis define the shape of growth domains in fission yeast.","citation":"Nat Commun 2015 Oct 12;6:8400","abstract":"The amazing structural variety of cells is matched only by their functional diversity, and reflects the complex interplay between biochemical and mechanical regulation. How both regulatory layers generate specifically shaped cellular domains is not fully understood. Here, we report how cell growth domains are shaped in fission yeast. Based on quantitative analysis of cell wall expansion and elasticity, we develop a model for how mechanics and cell wall assembly interact and use it to look for factors underpinning growth domain morphogenesis. Surprisingly, we find that neither the global cell shape regulators Cdc42-Scd1-Scd2 nor the major cell wall synthesis regulators Bgs1-Bgs4-Rgf1 are reliable predictors of growth domain geometry. Instead, their geometry can be defined by cell wall mechanics and the cortical localization pattern of the exocytic factors Sec6-Syb1-Exo70. Forceful re-directioning of exocytic vesicle fusion to broader cortical areas induces proportional shape changes to growth domains, demonstrating that both features are causally linked.","doi":"10.1038/ncomms9400","authors":"Abenza JF, Couturier E, Dodgson J, Dickmann J, Chessel A, Dumais J, Salas REC","authors_abbrev":"Abenza JF et al.","pubmed_publication_date":"12 Oct 2015","pubmed_entrez_date":"2015-10-13","publication_year":"2015","canto_session_key":"fad29fb0e08f71fe","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-10-14 00:19:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29018935","title":"A curious new role for MRN in Schizosaccharomyces pombe non-homologous end-joining.","citation":"Curr Genet 2018 Apr;64(2):359-364","abstract":"Chromosomal breaks can be healed by several repair processes, including one called non-homologous end-joining (NHEJ) where the two broken ends are ligated together with a loss of 0-5 bp of DNA. The protein requirements for NHEJ of cut DNA ends in the budding yeast Saccharomyces cerevisiae include its version of the Mre11-Rad50-Nbs1 (MRN) complex. In contrast, the fission yeast Schizosaccharomyces pombe and mammalian cells do not require MRN for this process. Recent work in S. pombe used transposon excision to generate breaks that were capped by DNA hairpins, which must be opened to produce ligatable ends. Repair in S. pombe was through an NHEJ reaction that now requires MRN. Surprisingly, wild type cells and MRN mutants that lack nuclease activity showed the same levels of excision. These genetic results suggest that MRN recruits an unknown hairpin-opening nuclease for this unusual NHEJ reaction.","doi":"10.1007/s00294-017-0760-1","authors":"Runge KW, Li Y","authors_abbrev":"Runge KW et al.","pubmed_publication_date":"Apr 2018","pubmed_entrez_date":"2017-10-12","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-10-13 00:15:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10564662","title":"Although calnexin is essential in S. pombe, its highly conserved central domain is dispensable for viability.","citation":"J Cell Sci 1999 Dec;112 ( Pt 23):4449-60","abstract":"In mammalian cells, the calnexin/calreticulin chaperones play a key role in glycoprotein folding and its control within the endoplasmic reticulum (ER), by interacting with folding intermediates via their monoglucosylated glycans. This lectin activity has been mapped in mammalian calnexin/calreticulin chaperones to the central region, which is a highly conserved feature of calnexin/calreticulin molecules across species. The central domain has also been implicated in Ca(2+) binding, and it has been proposed to be involved in the regulation of calcium homeostasis in the ER. Herein, we show that although the Schizosaccharomyces pombe calnexin is essential for viability, cells lacking its 317-amino-acid highly conserved central region are viable under normal growth conditions. However, the central region appears to be necessary for optimal growth under high ER-stress, suggesting that this region is important under extreme folding situations (such as DTT and temperature). The minimal length of calnexin required for viability spans the C-terminal 123 residues. Furthermore, cells with the central domain of the protein deleted were affected in their morphology at 37 degrees C, probably due to a defect in cell wall synthesis, although these mutant cells exhibited the same calcium tolerance as wild-type cells at 30 degrees C.","authors":"Elagöz A, Callejo M, Armstrong J, Rokeach LA","authors_abbrev":"Elagöz A et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-11-24","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24089141","title":"DNA intermediates of meiotic recombination in synchronous S. pombe at optimal temperature.","citation":"Nucleic Acids Res 2014 Jan;42(1):359-69","abstract":"Crossovers formed by recombination between homologous chromosomes are important for proper homolog segregation during meiosis and for generation of genetic diversity. Optimal molecular analysis of DNA intermediates of recombination requires synchronous cultures. We previously described a mutant, pat1-as2, of the fission yeast Schizosaccharomyces pombe that undergoes synchronous meiosis at 25°C when an ATP analog is added to the culture. Here, we compare recombination intermediates in pat1-as2 at 25°C with those in the widely used pat1-114 temperature-sensitive mutant at 34°C, a temperature higher than optimal. DNA double-strand breaks at most hotspots are similarly abundant in the two conditions but, remarkably, a few hotspots are distinctly deficient at 25°C. In both conditions, Holliday junctions at DNA break hotspots form more frequently between sister chromatids than between homologs, but a novel species, perhaps arising from invasion by only one end of broken DNA, is more readily observed at 25°C. Our results confirm the validity of previous assays of recombination intermediates in S. pombe and provide new information on the mechanism of meiotic recombination.","doi":"10.1093/nar/gkt861","authors":"Hyppa RW, Fowler KR, Cipak L, Gregan J, Smith GR","authors_abbrev":"Hyppa RW et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2013-10-04","publication_year":"2014","canto_session_key":"8f8995060ea2e88c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-03-26 13:27:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-02-17 01:12:44","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4G3.05c","SPBC19C2.05","SPAC17A5.11","SPAC1556.01c"],"gene_count":4,"ltp_gene_count":0,"approved_date":"2014-02-17"},{"uniquename":"PMID:2680532","title":"A review of mitosis in the fission yeast Schizosaccharomyces pombe.","citation":"Exp Cell Res 1989 Oct;184(2):273-86","abstract":"Mitosis and cell division are the final events of the cell cycle, resulting in the precise segregation of chromosomes into two daughter cells. A highly controlled and accurate segregation of the chromosomes is required to ensure that each daughter cell receives a complete genome and remains viable. The fission yeast, Schizosaccharomyces pombe, is a unicellular eukaryotic organism which is particularly convenient for investigating these problems. It is very amenable to genetic analysis and its predominantly haploid life cycle has allowed the isolation of recessive temperature-sensitive mutants unable to complete the cell cycle. Classical genetic analysis of these mutants has been used to identify over 40 gene functions that are required for cell cycle progress in S. pombe. Many of these genes have now been cloned and sequenced and in some cases the encoded gene product has been identified. This approach, coupling classical and molecular genetics, allows identification of the molecules important in the mitotic processes and provides a means for establishing what functional roles they may play.","authors":"Hayles J, Nurse P","authors_abbrev":"Hayles J et al.","pubmed_publication_date":"Oct 1989","pubmed_entrez_date":"1989-10-01","publication_year":"1989","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11085271","title":"spo12 is a multicopy suppressor of mcs3 that is periodically expressed in fission yeast mitosis.","citation":"Mol Gen Genet 2000 Oct;264(3):306-16","abstract":"Hyperactivation of Cdc2 in fission yeast causes cells to undergo a lethal premature mitosis, a phenomenon called mitotic catastrophe. This phenotype is observed in cdc2-3w wee1-50 cells at high temperature and is suppressed by a single recessive mutant, mcs3-12. Mcs3 acts independently of the Wee1 kinase and Cdc25 phosphatase, two major regulators of Cdc2. We have isolated multicopy suppressors of the cell cycle arrest phenotype of mcs3-12 wee1-50 cdc25-22 cells, but did not identify the mcs3 gene itself. Instead several known mitotic regulators were isolated, including the Cdc25 phosphatase, Wis2 cyclophilin, Cek1 kinase, and an Hsp90 homologue, Swo1. We also isolated clones encoding non-functional, truncated forms of the Wee1 kinase and Dis2 type 1 phosphatase. In addition we identified a multicopy suppressor that encodes a structural homologue of the budding yeast SPO12 gene. We find that overexpression of fission yeast spo12 not only suppresses the phenotype of the mcs3-12 wee1-50 cdc25-22 strain, but also that of a win1-1 wee1-50 cdc25-22 strain at high temperature, indicating that the function of spo12 is not directly related to mcs3. We show that spo12 mRNA is periodically expressed during the fission yeast cell cycle, peaking at the G2/M transition coincidently with cdc15. Deletion of spo12, however, has no overt effect on either the mitotic or meiotic cell cycles, except when the function of the major B type cyclin, Cdc13, is compromised.","authors":"Samuel JM, Fournier N, Simanis V, Millar JB","authors_abbrev":"Samuel JM et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-11-21","publication_year":"2000","canto_session_key":"73732efda97a7246","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-07-15 10:34:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-15 10:34:48","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.15c","SPAC24H6.05","SPCC18B5.03","SPCC1450.11c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-07-15"},{"uniquename":"PMID:4698209","title":"Biosynthesis of branched-chain amino acids in Schizosaccharomyces pombe: regulatory properties of threonine deaminase.","citation":"J Bacteriol 1973 Apr;114(1):323-31","abstract":"Biosynthetic threonine deaminase (TD) from Schizosaccharomyces pombe has been partially purified from crude extracts by treatment with protamine sulfate, ammonium sulfate precipitation, and gel filtration through Sephadex G-25. In both crude extracts and purified preparations, TD showed marked stimulation by pyridoxal phosphate. A pH optimum for activity was found at pH 9.0, whereas the inhibition caused by the natural feedback inhibitor, l-isoleucine, was maximal at pH 7.4. l-Threonine exhibits homotropic cooperative effects at low pH (7.0-8.0), which are eliminated at pH 9.0, and the affinity for substrate (in terms of K(m)) increased with increasing pH. Enzyme activity could be completely inhibited by isoleucine over a pH range of 7.4 to 9.0; the amount of isoleucine required for 50% inhibition increased with increasing pH. Isoleucine inhibition was pseudocompetitive with respect to substrate and increased the cooperative effects of threonine. l-Valine was found to reverse isoleucine inhibition; it also activated the enzyme in a pH range of 7.0 to 8.0 by eliminating the cooperative effects of threonine, thus normalizing the substrate saturation curves at these pH values. l-Leucine was shown to be a competitive inhibitor with respect to threonine, and to be able partially to reverse isoleucine inhibition. Treatment of TD with mercurials did not result in desensitization to isoleucine inhibition. However, at pH 10, virtually no sensitivity of the enzyme to isoleucine was observed while activity remained strong, which suggests the existence of separate sites on the TD molecule for binding threonine and isoleucine. A tentative model is presented which unifies the kinetic results reported here in terms of the interactions of TD with its effector molecules.","authors":"McDonald RA, Kaplan JG","authors_abbrev":"McDonald RA et al.","pubmed_publication_date":"Apr 1973","pubmed_entrez_date":"1973-04-01","publication_year":"1973","canto_session_key":"89847d660dffdb32","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-08-16 13:29:41","canto_approved_date":"2024-07-25 15:38:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-13 17:34:34","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"vw253@cam.ac.uk","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1677.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-08-16"},{"uniquename":"PMID:15050371","title":"The protein kinase kin1 is required for cellular symmetry in fission yeast.","citation":"Biol Cell 2004 Mar;96(2):169-79","abstract":"The fission yeast Schizosaccharomyces pombe is a highly polarized unicellular eukaryote with two opposite growing poles in which F-actin cytoskeleton is focused. The KIN1/PAR-1/MARK protein family is composed of conserved eukaryotic serine/threonine kinases which are involved in cell polarity, microtubule stability or cell cycle regulation. Here, we investigate the function of the fission yeast KIN1/PAR-1/MARK member, kin1p. Using a deletion allele (kin1Delta), we show that kin1 mutation promotes a delay in septation. Kin1p regulates the structure of the new cell end after cytokinesis by modulating cell wall remodeling. Abnormal shaped interphase kin1Delta cells misplace F-actin patches and the premitotic nucleus. Thus, mitotic kin1Delta cells misposition the F-actin ring assembly site that is dependent on the position of the interphase nucleus. The resulting asymmetric cell division produces daughter cells with distinct shapes. Overexpressed kin1p accumulates asymmetrically at the cell cortex and affects cell shape, F-actin organization and microtubules. Our results suggest that correct dosage of kin1p at the cortex is required for spatial organization of the fission yeast cell.","authors":"La Carbona S, Allix C, Philippe M, Le Goff X","authors_abbrev":"La Carbona S et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-03-31","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4F6.06"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:11096119","title":"The fission yeast TOR homolog, tor1+, is required for the response to starvation and other stresses via a conserved serine.","citation":"J Biol Chem 2001 Mar 09;276(10):7027-32","abstract":"Targets of rapamycin (TORs) are conserved phosphatidylinositol kinase-related kinases that are involved in the coordination between nutritional or mitogenic signals and cell growth. Here we report the initial characterization of two Schizosaccharomyces pombe TOR homologs, tor1(+) and tor2(+). tor2(+) is an essential gene, whereas tor1(+) is required only under starvation and other stress conditions. Specifically, Deltator1 cells fail to enter stationary phase or undergo sexual development and are sensitive to cold, osmotic stress, and oxidative stress. In complex with the prolyl isomerase FKBP12, the drug rapamycin binds a conserved domain in TORs, FRB, thus inhibiting some of the functions of TORs. Mutations at a conserved serine within the FRB domain of Saccharomyces cerevisiae TOR proteins led to rapamycin resistance but did not otherwise affect the functions of the proteins. The S. pombe tor1(+) exhibits different features; substitution of the conserved serine residue, Ser(1834), with arginine compromises its functions and has no effect on the inhibition that rapamycin exerts on sexual development in S. pombe.","authors":"Weisman R, Choder M","authors_abbrev":"Weisman R et al.","pubmed_publication_date":"09 Mar 2001","pubmed_entrez_date":"2000-11-30","publication_year":"2001","canto_session_key":"3c604e8199f9bf8b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-20 14:56:23","canto_approved_date":"2019-06-14 12:17:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-20 14:55:10","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.07c","SPBC30D10.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-10-20"},{"uniquename":"PMID:10099784","title":"Purification and kinetic characterization of 6-phosphogluconate dehydrogenase from Schizosaccharomyces pombe.","citation":"Biochem Cell Biol 1998;76(4):637-44","abstract":"6-Phosphogluconate dehydrogenase is the pivotal enzyme that links the gluconate route and the oxidative phase of the pentose phosphate pathway in Schizosaccharomyces pombe. The enzyme differs from the known 6-phosphogluconate dehydrogenases of other sources in that the Schizosaccharomyces enzyme is tetrameric having a subunit mass of 38 kDa, that it requires NADP+ obligatorily for activity, and that it can be activated by divalent metal ions such as Co2+ and Mn2+. Steady-state kinetic studies were undertaken. Initial rate and product inhibition results suggest that 6-phosphogluconate dehydrogenase from Schizosaccharomyces pombe catalyzes NADP(+)-linked oxidative decarboxylation of 6-phosphogluconate by an equilibrium random mechanism with two independent binding sites, namely one site for the nicotinamide coenzyme, NADP+/NADPH, and another site for 6-phosphogluconate-D-ribulose-5-phosphate and for CO2. Studies of pH dependence implicated a basic residue with a pK value of 7.4 in the binding of 6-phosphogluconate and an acidic residue with a pK value of 6.7 in the cation-mediated interaction of NADP+ with the enzyme.","authors":"Tsai CS, Chen Q","authors_abbrev":"Tsai CS et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1999-04-01","publication_year":"1998","canto_session_key":"ae4d2e85829f81c7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-15 17:15:21","canto_approved_date":"2019-01-09 16:26:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-15 17:15:10","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.16"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-12-15"},{"uniquename":"PMID:4020341","title":"The all2 gene is required for the induction of the purine deamination pathway in Schizosaccharomyces pombe.","citation":"J Gen Microbiol 1985 Mar;131(3):527-32","abstract":"Five mutants were isolated at the all2 gene on the basis of their inability to utilize hypoxanthine as a sole source of nitrogen. These mutants failed to utilize the purines adenine, hypoxanthine, xanthine, uric acid, allantoin and allantoic acid, although they could utilize urea and ammonium. The all2 mutants appeared to be defective in purine induction of uricase, allantoinase, allantoicase and ureidoglycollase activities but retained wild-type activity of the constitutively synthesized urease. The all2 mutations were recessive.","authors":"Fluri R, Kinghorn JR","authors_abbrev":"Fluri R et al.","pubmed_publication_date":"Mar 1985","pubmed_entrez_date":"1985-03-01","publication_year":"1985","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23410379","title":"Edge usage, motifs, and regulatory logic for cell cycling genetic networks.","citation":"Phys Rev E Stat Nonlin Soft Matter Phys 2013 Jan;87(1):012727","abstract":"The cell cycle is a tightly controlled process, yet it shows marked differences across species. Which of its structural features follow solely from the ability to control gene expression? We tackle this question in silico by examining the ensemble of all regulatory networks which satisfy the constraint of producing a given sequence of gene expressions. We focus on three cell cycle profiles coming from baker's yeast, fission yeast, and mammals. First, we show that the networks in each of the ensembles use just a few interactions that are repeatedly reused as building blocks. Second, we find an enrichment in network motifs that is similar in the two yeast cell cycle systems investigated. These motifs do not have autonomous functions, yet they reveal a regulatory logic for cell cycling based on a feed-forward cascade of activating interactions.","authors":"Zagorski M, Krzywicki A, Martin OC","authors_abbrev":"Zagorski M et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2013-02-16","publication_year":"2013","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30963244","title":"Regulation of centromeric heterochromatin in the cell cycle by phosphorylation of histone H3 tyrosine 41.","citation":"Curr Genet 2019 Aug;65(4):829-836","abstract":"Constitutive heterochromatin packages long stretches of repetitive DNA sequences at the centromere and telomere, and ensures genomic integrity at these loci by preventing aberrant recombination and transcription. The chromatin scaffold of heterochromatin is dynamically regulated in the cell cycle, and inheritance of the epigenetically silenced state is dependent on a transcriptional event imposed on the underlying non-coding RNA in conjunction with the DNA replicative phase. Heterochromatin becomes transiently loosened in response to a reduction in the binding of Swi6, a heterochromatin protein, and this allows RNA polymerase II access to the underlying sequence. The derived transcripts, in turn, drive heterochromatin formation via the recruitment of other silencing factors. It remains unclear how heterochromatin becomes decompacted in a cell cycle-specific manner. Here, we describe a mechanism of heterochromatin decompaction initiated by a novel histone modification, histone H3 tyrosine 41 phosphorylation (H3Y41p). We will discuss how H3Y41p cooperates with other regulatory pathways to enforce cell cycle-dependent regulation of constitutive heterochromatin.","doi":"10.1007/s00294-019-00962-2","authors":"Ren B, Chen ES","authors_abbrev":"Ren B et al.","pubmed_publication_date":"Aug 2019","pubmed_entrez_date":"2019-04-10","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-04-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17289942","title":"Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase.","citation":"Science 2007 Mar 23;315(5819):1726-9","abstract":"The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Here, we report crystal structures at 2.9 and 2.6 A resolution for ATP- and AMP-bound forms of a core alphabetagamma adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the gamma subunit, with their respective phosphate groups positioned near function-impairing mutants. Unexpectedly, ATP binds without counterions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge.","authors":"Townley R, Shapiro L","authors_abbrev":"Townley R et al.","pubmed_publication_date":"23 Mar 2007","pubmed_entrez_date":"2007-02-10","publication_year":"2007","canto_session_key":"4a9fc7321cca8383","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-19 14:54:58","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-09 11:26:53","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1919.03c","SPCC74.03c","SPAC1556.08c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-08-09","pdb_entries":[{"pdb_id":"2ooy","gene_chains":[{"gene_uniquename":"SPCC74.03c","chain":"A/C","position":"440-576"},{"gene_uniquename":"SPCC1919.03c","chain":"B/D","position":"203-298"},{"gene_uniquename":"SPAC1556.08c","chain":"E/G","position":"2-334"}],"title":"Crystal structure of the adenylate sensor from AMP-activated protein kinase complexed with ATP","entry_authors":"Townley R,Shapiro L","entry_authors_abbrev":"Townley R et al.","reference_uniquename":"PMID:17289942","experimental_method":"X-ray","resolution":"2.88"},{"pdb_id":"2oox","gene_chains":[{"gene_uniquename":"SPCC74.03c","chain":"A/C","position":"440-576"},{"gene_uniquename":"SPCC1919.03c","chain":"B/D","position":"203-298"},{"gene_uniquename":"SPAC1556.08c","chain":"E/G","position":"2-334"}],"title":"Crystal structure of the adenylate sensor from AMP-activated protein kinase complexed with AMP","entry_authors":"Townley R,Shapiro L","entry_authors_abbrev":"Townley R et al.","reference_uniquename":"PMID:17289942","experimental_method":"X-ray","resolution":"2.6"}]},{"uniquename":"PMID:7332933","title":"Regulation of RNA synthesis in fission yeast. The effect of a Tetrahymena peptide factor on RNA synthesis in exponentially multiplying yeast cells.","citation":"Cell Biol Int Rep 1981 Nov;5(11):1019-26","abstract":"","authors":"Kramhøft B, Andersen HA","authors_abbrev":"Kramhøft B et al.","pubmed_publication_date":"Nov 1981","pubmed_entrez_date":"1981-11-01","publication_year":"1981","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084814","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19487461","title":"Cyclin-dependent kinase inhibits reinitiation of a normal S-phase program during G2 in fission yeast.","citation":"Mol Cell Biol 2009 Aug;29(15):4025-32","abstract":"To achieve faithful replication of the genome once in each cell cycle, reinitiation of S phase is prevented in G(2) and origins are restricted from refiring within S phase. We have investigated the block to rereplication during G(2) in fission yeast. The DNA synthesis that occurs when G(2)/M cyclin-dependent kinase (CDK) activity is depleted has been assumed to be repeated rounds of S phase without mitosis, but this has not been demonstrated to be the case. We show here that on G(2)/M CDK depletion in G(2), repeated S phases are induced, which are correlated with normal G(1)/S transcription and attainment of doublings in cell size. Mostly normal mitotic S-phase origins are utilized, although at different efficiencies, and replication is essentially equal across the genome. We conclude that CDK inhibits reinitiation of S phase during G(2), and if G(2)/M CDK is depleted, replication results from induction of a largely normal S-phase program with only small differences in origin usage and efficiency.","doi":"10.1128/MCB.00185-09","authors":"Kiang L, Heichinger C, Watt S, Bähler J, Nurse P","authors_abbrev":"Kiang L et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-06-03","publication_year":"2009","canto_session_key":"6c335a4e1d1a262d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-06-28 21:32:41","canto_approved_date":"2024-08-13 16:07:22","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-05-30 13:15:34","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jacky Hayles","community_curator":true,"annotation_count":5,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC582.03","SPAC24H6.05","SPAP14E8.02","SPBC336.12c","SPAPB2B4.03"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2018-06-28"},{"uniquename":"PMID:31911490","title":"RNA-Binding Protein Rnc1 Regulates Cell Length at Division and Acute Stress Response in Fission Yeast through Negative Feedback Modulation of the Stress-Activated Mitogen-Activated Protein Kinase Pathway.","citation":"mBio 2020 Jan 07;11(1)","abstract":"RNA-binding proteins (RBPs) play a major role during control of mRNA localization, stability, and translation and are central to most cellular processes. In the fission yeast  Schizosaccharomyces pombe , the multiple K homology (KH) domain RBP Rnc1 downregulates the activity of the cell integrity pathway (CIP) via stabilization of  pmp1  +  mRNA, which encodes the Pmp1 phosphatase that inactivates Pmk1, the mitogen-activated protein kinase (MAPK) component of this signaling cascade. However, Rnc1 likely regulates the half-life/stability of additional mRNAs. We show that Rnc1 downregulates the activity of Sty1, the MAPK of the stress-activated MAPK pathway (SAPK), during control of cell length at division and recovery in response to acute stress. Importantly, this control strictly depends on Rnc1's ability to bind mRNAs encoding activators (Wak1 MAPKKK, Wis1 MAPKK) and downregulators (Atf1 transcription factor, Pyp1 and Pyp2 phosphatases) of Sty1 phosphorylation through its KH domains. Moreover, Sty1 is responsible for Rnc1 phosphorylation  in vivo  at multiple phosphosites during growth and stress, and these modifications trigger Rnc1 for proper binding and destabilization of the above mRNA targets. Phosphorylation by Sty1 prompts Rnc1-dependent mRNA destabilization to negatively control SAPK signaling, thus revealing an additional feedback mechanism that allows precise tuning of MAPK activity during unperturbed cell growth and stress. IMPORTANCE  Control of mRNA localization, stability, turnover, and translation by RNA-binding proteins (RBPs) influences essential processes in all eukaryotes, including signaling by mitogen-activated protein kinase (MAPK) pathways. We describe that in the fission yeast  Schizosaccharomyces pombe  the RBP Rnc1 negatively regulates cell length at division during unperturbed growth and recovery after acute stress by reducing the activity of the MAPK Sty1, which regulates cell growth and differentiation during environmental cues. This mechanism relies on Rnc1 binding to specific mRNAs encoding both enhancers and negative regulators of Sty1 activity. Remarkably, multiple phosphorylation of Rnc1 by Sty1 favors RBP binding and destabilization of the above mRNAs. Thus, posttranscriptional modulation of MAP kinase signaling by RNA-binding proteins emerges as a major regulatory mechanism that dictates the growth cycle and cellular adaptation in response to the changing environment in eukaryotic organisms.","doi":"10.1128/mBio.02815-19","authors":"Prieto-Ruiz F, Vicente-Soler J, Franco A, Gómez-Gil E, Sánchez-Marinas M, Vázquez-Marín B, Aligué R, Madrid M, Moreno S, Soto T, Cansado J","authors_abbrev":"Prieto-Ruiz F et al.","pubmed_publication_date":"07 Jan 2020","pubmed_entrez_date":"2020-01-09","publication_year":"2020","canto_session_key":"714b38967995ac5b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Francisco Prieto-Ruiz","canto_first_approved_date":"2020-10-15 16:45:58","canto_approved_date":"2024-02-08 23:17:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-10-13 15:30:09","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Francisco Prieto-Ruiz","community_curator":true,"annotation_count":82,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4F11.02","SPBC1685.01","SPCC757.09c","SPBC409.07c","SPAC26F1.10c","SPAC9G1.02","SPAC24B11.06c","SPAC19D5.01","SPBC119.08","SPBC887.10","SPBC29B5.01"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2020-10-15"},{"uniquename":"PMID:8524274","title":"The rad18 gene of Schizosaccharomyces pombe defines a new subgroup of the SMC superfamily involved in DNA repair.","citation":"Mol Cell Biol 1995 Dec;15(12):7067-80","abstract":"The rad18 mutant of Schizosaccharomyces pombe is very sensitive to killing by both UV and gamma radiation. We have cloned and sequenced the rad18 gene and isolated and sequenced its homolog from Saccharomyces cerevisiae, designated RHC18. The predicted Rad18 protein has all the structural properties characteristic of the SMC family of proteins, suggesting a motor function--the first implicated in DNA repair. Gene deletion shows that both rad18 and RHC18 are essential for proliferation. Genetic and biochemical analyses suggest that the product of the rad18 gene acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair. This second repair pathway involves the products of the rhp51 gene (the homolog of the RAD51 gene of S. cerevisiae) and the rad2 gene.","authors":"Lehmann AR, Walicka M, Griffiths DJ, Murray JM, Watts FZ, McCready S, Carr AM","authors_abbrev":"Lehmann AR et al.","pubmed_publication_date":"Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"93cee25f8a94c044","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-12-16 13:28:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-26 12:34:29","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.06","SPBC3E7.08c","SPAC644.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-11-26"},{"uniquename":"PMID:38051102","title":"Fission Yeast TORC1 Promotes Cell Proliferation through Sfp1, a Transcription Factor Involved in Ribosome Biogenesis.","citation":"Mol Cell Biol 2023 Dec 05;:1-18","abstract":"Target of rapamycin complex 1 (TORC1) is activated in response to nutrient availability and growth factors, promoting cellular anabolism and proliferation. To explore the mechanism of TORC1-mediated proliferation control, we performed a genetic screen in fission yeast and identified Sfp1, a zinc-finger transcription factor, as a multicopy suppressor of temperature-sensitive TORC1 mutants. Our observations suggest that TORC1 phosphorylates Sfp1 and protects Sfp1 from proteasomal degradation. Transcription analysis revealed that Sfp1 positively regulates genes involved in ribosome production together with two additional transcription factors, Ifh1/Crf1 and Fhl1. Ifh1 physically interacts with Fhl1, and the nuclear localization of Ifh1 is regulated in response to nutrient levels in a manner dependent on TORC1 and Sfp1. Taken together, our data suggest that the transcriptional regulation of the genes involved in ribosome biosynthesis by Sfp1, Ifh1, and Fhl1 is one of the key pathways through which nutrient-activated TORC1 promotes cell proliferation.","doi":"10.1080/10985549.2023.2282349","authors":"Tai YT, Fukuda T, Morozumi Y, Hirai H, Oda AH, Kamada Y, Akikusa Y, Kanki T, Ohta K, Shiozaki K","authors_abbrev":"Tai YT et al.","pubmed_publication_date":"05 Dec 2023","pubmed_entrez_date":"2023-12-05","publication_year":"2023","canto_session_key":"5e8e362b7dec8c54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yen Teng Tai","canto_first_approved_date":"2024-01-01 17:00:58","canto_approved_date":"2025-09-22 06:28:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-15 03:27:31","canto_added_date":"2023-12-06 00:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":216,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yen Teng Tai","community_curator":true,"annotation_count":1,"orcid":"0000-0002-0764-5034","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB8E5.06c","SPBC16H5.08c","SPAC4F10.09c","SPBC23G7.15c","SPBC24C6.02","SPBC2G2.05","SPCC1322.15","SPAC959.07","SPAC890.04c","SPAC20G8.09c","SPAC664.05","SPAC19B12.11c","SPAC890.08","SPBP8B7.20c","SPAC23H3.03c","SPBC3D6.15","SPAC18G6.07c","SPCC1672.07","SPCC18.12c","SPCP1E11.08","SPAC23A1.11","SPAC1142.08","SPAC806.03c","SPCC613.06","SPCC830.03","SPBC21B10.10","SPBC106.18","SPBC16D10.11c","SPAPB1E7.12","SPAC959.03c","SPAC3G9.03","SPAC23H4.15","SPBC4F6.13c","SPBC14F5.06","SPBC18H10.14","SPCC1393.03","SPCP31B10.08c","SPCC16A11.02","SPAC664.04c","SPBC839.05c","SPBC11C11.09c","SPBC839.04","SPBC2F12.04","SPBC2D10.10c","SPBC18H10.13","SPCC364.03","SPBC685.07c","SPBC1711.16","SPBC11C11.07","SPBC1711.07","SPAC959.08","SPAC144.11","SPAC644.15","SPCC576.11","SPAC22H10.11c","SPBC26H8.04c","SPBC8D2.10c","SPBC21H7.04","SPBC23E6.05","SPAC22E12.13c","SPBC4F6.04","SPBC1711.06","SPBC685.06","SPCC576.08c","SPAC140.02","SPAC16C9.03","SPAC1B3.13","SPAC8F11.04","SPBC651.01c","SPAC1556.05c","SPAC1565.05","SPAC1B9.03c","SPCC5E4.07","SPAC4F8.04","SPBC23G7.07c","SPBP22H7.08","SPBC16H5.10c","SPAC6F12.16c","SPBC800.06","SPBC215.06c","SPAC521.05","SPAC589.10c","SPBC1604.06c","SPAC6G9.09c","SPAC29A4.04c","SPCC16C4.08c","SPAC1486.09","SPCC1494.06c","SPBC26H8.08c","SPBC839.13c","SPAC1F7.13c","SPBC29A3.16","SPAP7G5.05","SPAC1805.12c","SPCC330.09","SPAC6G9.02c","SPBC17D1.06","SPBC19F5.05c","SPBC649.02","SPCP1E11.09c","SPCC330.14c","SPBC16G5.01","SPCC576.09","SPAC3F10.16c","SPAC1783.08c","SPBC646.10c","SPAC31G5.17c","SPAC1687.11","SPBP4H10.13","SPBC216.07c","SPAC30D11.03","SPAC1687.06c","SPAC31G5.03","SPBC1604.09c","SPAC823.08c","SPBC336.02","SPCC1919.09","SPBC11G11.03","SPAC13G6.07c","SPBC4F6.14","SPAC57A7.06","SPBC2F12.07c","SPAC16.05c","SPBC1921.01c","SPAC1071.07c","SPCC1322.11","SPAC26A3.04","SPBC3F6.04c","SPAC2F7.05c","SPAC1F7.02c","SPAC222.06","SPBC29A3.06","SPBC543.04","SPCC4G3.08","SPBC577.02","SPAC607.03c","SPAC3F10.17","SPBC20F10.01","SPAC664.06","SPAC19A8.07c","SPAC3H5.05c","SPAC1071.08","SPAC3G6.04","SPAC664.08c","SPAC22A12.04c","SPAC22G7.05","SPBP8B7.16c","SPBC3B8.09","SPAC1142.04","SPAC1782.10c","SPAC11G7.04","SPAC17G6.06","SPAC3H5.07"],"gene_count":153,"ltp_gene_count":8,"approved_date":"2024-01-01"},{"uniquename":"PMID:37772819","title":"Activities, substrate specificity, and genetic interactions of fission yeast Siw14, a cysteinyl-phosphatase-type inositol pyrophosphatase.","citation":"mBio 2023 Sep 29;14(5):e0205623","abstract":"Inositol pyrophosphate 1,5-IP 8  is a signaling molecule that regulates phosphate and polyphosphate homeostasis in the fission yeast  Schizosaccharomyces pombe . 1,5-IP 8  levels are dictated by a balance between the Asp1 kinase domain that converts 5-IP 7  to 1,5-IP 8  and two pyrophosphatases-the Asp1 pyrophosphatase domain (histidine acid phosphatase family) and the Aps1 pyrophosphatase enzyme (Nudix family)-that hydrolyze the β-phosphates of 1,5-IP 8 . Here, we characterize  S. pombe  Siw14 (SpSiw14), a cysteinyl-phosphatase family member and a homolog of  Saccharomyces cerevisiae  Siw14, as a third fission yeast pyrophosphatase implicated in inositol pyrophosphate catabolism. We find that SpSiw14's substrate repertoire embraces inorganic pyrophosphate, inorganic polyphosphate, and the inositol pyrophosphates 5-IP 7 , 1-IP 7 , and 1,5-IP 8 , in addition to the generic substrate  p -nitrophenylphosphate. Genetic analyses revealed that (i) elimination of the SpSiw14 protein or inactivation of the SpSiw14 pyrophosphatase by the C189S mutation had no effect on  S. pombe  growth but was lethal in the absence of Aps1 and (ii) the synthetic lethality of  siw14 ∆  aps1 ∆ depended on the synthesis of 1,5-IP 8  by the Asp1 kinase. We conclude that SpSiw14 and Aps1 pyrophosphatases have essential but redundant functions in fission yeast, and that their synthetic lethality is a consequence of the toxic effects of too much 1,5-IP 8 . Suppression of  siw14 ∆  aps1 ∆ lethality by loss-of-function mutations of components of the fission yeast 3'-processing/termination machinery fortifies the case for overzealous transcription termination as the basis for 1,5-IP 8  toxicosis. IMPORTANCE The inositol pyrophosphate signaling molecule 1,5-IP 8  modulates fission yeast phosphate homeostasis via its action as an agonist of RNA 3'-processing and transcription termination. Cellular 1,5-IP 8  levels are determined by a balance between the activities of the inositol polyphosphate kinase Asp1 and several inositol pyrophosphatase enzymes. Here, we characterize  Schizosaccharomyces pombe  Siw14 (SpSiw14) as a cysteinyl-phosphatase-family pyrophosphatase enzyme capable of hydrolyzing the phosphoanhydride substrates inorganic pyrophosphate, inorganic polyphosphate, and inositol pyrophosphates 5-IP 7 , 1-IP 7 , and 1,5-IP 8 . Genetic analyses implicate SpSiw14 in 1,5-IP 8  catabolism  in vivo , insofar as: loss of SpSiw14 activity is lethal in the absence of the Nudix-type inositol pyrophosphatase enzyme Aps1; and  siw14 ∆  aps1 ∆ lethality depends on synthesis of 1,5-IP 8  by the Asp1 kinase. Suppression of  siw14 ∆  aps1 ∆ lethality by loss-of-function mutations of 3'-processing/termination factors points to precocious transcription termination as the cause of 1,5-IP 8  toxicosis.","doi":"10.1128/mbio.02056-23","authors":"Sanchez AM, Schwer B, Jork N, Jessen HJ, Shuman S","authors_abbrev":"Sanchez AM et al.","pubmed_publication_date":"29 Sep 2023","pubmed_entrez_date":"2023-09-29","publication_year":"2023","canto_session_key":"59d6007b5a42a1e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2023-10-11 14:33:04","canto_approved_date":"2023-11-10 18:55:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-06 19:57:40","canto_added_date":"2023-09-29 23:25:05","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":40,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.11c","SPBC725.10","SPBC16E9.16c","SPAC15E1.02c","SPBC17A3.03c","SPBC776.02c","SPCC16C4.03","SPAC3G9.04","SPAC6B12.07c","SPAC13G6.14","SPBC28F2.12","SPACUNK4.17","SPBC1683.09c","SPCC70.08c","SPCC74.02c","SPAC637.03","SPCC1672.06c","SPBC337.03","SPBC14F5.01","SPAC26H5.09c","SPAC27D7.03c","SPACUNK4.14","SPAP8A3.04c","SPAC824.04"],"gene_count":24,"ltp_gene_count":12,"approved_date":"2023-10-11"},{"uniquename":"PMID:11007995","title":"Specific and nonspecific enzymes involved in the catabolism of mononucleoside and dinucleoside polyphosphates.","citation":"Pharmacol Ther 2000;87(2-3):117-39","abstract":"This review concerns enzymes that can degrade nucleoside 5'-tetra- and pentaphosphates (p(4)N and p(5)N) and those that can degrade various dinucleoside polyphosphates (Np(3-6)N'). Most of these enzymes are hydrolases, and they occur in all types of organisms. Certain fungi and protozoa also possess specific Np(n)N' phosphorylases. Specific p(4)N hydrolases have been demonstrated in mammals and in plants. In yeast, p(4)N and p(5)N are hydrolyzed by exopolyphosphatases. Among other hydrolases that can degrade these minor mononucleotides are phosphatases, apyrase, and (asymmetrical) Np(4)N' hydrolase, as well as the nonspecific adenylate deaminase. Np(n)N's are good substrates for Type I phosphodiesterases and nucleotide pyrophosphatases, and diadenosine polyphosphates are easily deaminated to diinosine polyphosphates by nonspecific adenylate deaminases. Specific Np(3)N' hydrolases occur in both prokaryotes and eukaryotes. Interestingly, the human fragile histidine triad (Fhit) tumor suppressor protein appears to be a typical Np(3)N' hydrolase. Among the specific Np(4)N' hydrolases are asymmetrically cleaving ones, which are typical of higher eukaryotes, and symmetrically cleaving enzymes found in Physarum polycephalum and in many bacteria. An enzyme that hydrolyzes both diadenosine tetraphosphate and diadenosine triphosphate has been found in the fission yeast Schizosaccharomyces pombe. Its amino acid sequence is similar to that of the human Fhit/Np(3)N' hydrolase. Very recently, a typical (asymmetrical) Np(4)N' hydrolase has been demonstrated for the first time in a bacterium-the pathogenic Bartonella bacilliformis. Another novelty is the discovery of diadenosine 5', 5\"'-P(1),P 6-hexaphosphate hydrolases in budding and fission yeasts and in mammalian cells. These enzymes and the (asymmetrical) Np(4)N' hydrolases have the amino acid motif typical of the MutT (or Nudix hydrolase) family. In contrast, the Schizosaccharomyces pombe Ap(4)A/Ap(3)A hydrolase, the human Fhit protein, and the yeast Np(n)N' phosphorylases belong to a superfamily GAFH, which includes the histidine triad proteins.","authors":"Guranowski A","authors_abbrev":"Guranowski A","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-09-29","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31880940","title":"Endocrine-Independent Cytotoxicity of Bisphenol A Is Mediated by Increased Levels of Reactive Oxygen Species and Affects Cell Cycle Progression.","citation":"J Agric Food Chem 2020 Jan 22;68(3):869-875","abstract":"Bisphenol A (BPA) is used for the production of plastics and epoxy resins, which are part of packaging materials for food and beverages, and can migrate into food and the environment, thus exposing human beings to its effects. Exposure to BPA has been associated with oxidative stress, cell cycle changes, and genotoxicity, and is mediated by its known endocrine-disrupting activity. Possible BPA cytotoxicity without mediation by estrogen receptors has been reported in the literature. Here, we show the toxic effects of BPA by live-cell imaging on the fission yeast  Schizosaccharomyces pombe , an experimental model lacking estrogen receptors, which were in line with data from flow cytometry on intracellular oxidation (76.4 ± 14.4 and 19.4 ± 16.1% of fluorescent cells for BPA treatment and control, respectively;  p  < 0.05) as well as delay in cell cycle progression (after 90 min of experiment, 48.4 ± 4.30 and 64.6 ± 5.46% of cells with a 4C DNA content for BPA treatment and control, respectively;  p  < 0.05) upon exposure to BPA. These results strongly support the possibilities that BPA-induced cell cycle changes can be independent of estrogen receptors and that live-cell imaging is a powerful tool for genotoxic analysis.","doi":"10.1021/acs.jafc.9b06853","authors":"Špačková J, Oliveira D, Puškár M, Ďurovcová I, Gaplovská-Kyselá K, Oliveira R, Ševčovičová A","authors_abbrev":"Špačková J et al.","pubmed_publication_date":"22 Jan 2020","pubmed_entrez_date":"2019-12-28","publication_year":"2020","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20495382","title":"SMC complexes and topoisomerase II work together so that sister chromatids can work apart.","citation":"Cell Cycle 2010 Jun 01;9(11):2065-70","abstract":"The pairing of sister chromatids in interphase facilitates error-free homologous recombination (HR). Sister chromatids are held together by cohesin, one of three Structural Maintenance of Chromosomes (SMC) complexes. In mitosis, chromosome condensation is controlled by another SMC complex, condensin, and the type II topoisomerase (Top2). In prophase, cohesin is stripped from chromosome arms, but remains at centromeres until anaphase, whereupon it is removed via proteolytic cleavage. The third SMC complex, Smc5/6, is generally described as a regulator of HR-mediated DNA repair. However, cohesin and condensin are also required for DNA repair, and HR genes are not essential for cell viability, but the SMC complexes are. Smc5/6 null mutants die in mitosis, and in fission yeast, Smc5/6 hypomorphs show lethal mitoses following genotoxic stress, or when combined with a Top2 mutant, top2-191. We found these mitotic defects are due to retention of cohesin on chromosome arms. We also show that Top2 functions in the cohesin cycle, and accumulating data suggests this is not related to its decatenation activity. Thus the SMC complexes and Top2 functionally interact, and any DNA repair function ascribed to Smc5/6 is likely a reflection of a more fundamental role in the regulation of chromosome structure.","authors":"Tapia-Alveal C, Outwin EA, Trempolec N, Dziadkowiec D, Murray JM, O'Connell MJ","authors_abbrev":"Tapia-Alveal C et al.","pubmed_publication_date":"01 Jun 2010","pubmed_entrez_date":"2010-05-25","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.07c","SPBC1A4.03c","SPCC5E4.06"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:36797353","title":"Cryo-EM structure and function of S. pombe complex IV with bound respiratory supercomplex factor.","citation":"Commun Chem 2023 Feb 16;6(1):32","abstract":"Fission yeast Schizosaccharomyces pombe serves as model organism for studying higher eukaryotes. We combined the use of cryo-EM and spectroscopy to investigate the structure and function of affinity purified respiratory complex IV (CIV) from S. pombe. The reaction sequence of the reduced enzyme with O 2  proceeds over a time scale of µs-ms, similar to that of the mammalian CIV. The cryo-EM structure of CIV revealed eleven subunits as well as a bound hypoxia-induced gene 1 (Hig1) domain of respiratory supercomplex factor 2 (Rcf2). These results suggest that binding of Rcf2 does not require the presence of a CIII-CIV supercomplex, i.e. Rcf2 is a component of CIV. An AlphaFold-Multimer model suggests that the Hig1 domains of both Rcf1 and Rcf2 bind at the same site of CIV suggesting that their binding is mutually exclusive. Furthermore, the differential functional effect of Rcf1 or Rcf2 is presumably caused by interactions of CIV with their different non-Hig1 domain parts.","doi":"10.1038/s42004-023-00827-3","authors":"Moe A, Ädelroth P, Brzezinski P, Näsvik Öjemyr L","authors_abbrev":"Moe A et al.","pubmed_publication_date":"16 Feb 2023","pubmed_entrez_date":"2023-02-16","publication_year":"2023","canto_session_key":"f879676c15830c6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-10 08:31:00","canto_approved_date":"2025-06-17 15:33:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-10 08:34:17","canto_added_date":"2023-02-18 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.04","SPCC338.10c","SPAC1565.01","SPMIT.04","SPMIT.01","SPBC2F12.17","SPAC1296.02","SPCC417.16","SPCC1442.08c","SPAC24C9.16c","SPCC1259.05c","SPCC1739.09c","SPMIT.11"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2023-03-10","pdb_entries":[{"pdb_id":"8c8q","gene_chains":[{"gene_uniquename":"SPBC2F12.17","chain":"G","position":"1-59"},{"gene_uniquename":"SPCC1739.09c","chain":"K","position":"1-130"},{"gene_uniquename":"SPCC338.10c","chain":"E","position":"1-186"},{"gene_uniquename":"SPCC1442.08c","chain":"J","position":"1-86"},{"gene_uniquename":"SPCC1259.05c","chain":"I","position":"1-58"},{"gene_uniquename":"SPMIT.01","chain":"A","position":"1-537"},{"gene_uniquename":"SPMIT.04","chain":"C","position":"1-269"},{"gene_uniquename":"SPMIT.11","chain":"B","position":"1-248"},{"gene_uniquename":"SPAC1296.02","chain":"D","position":"1-159"},{"gene_uniquename":"SPAC1565.01","chain":"L","position":"1-242"},{"gene_uniquename":"SPAC24C9.16c","chain":"H","position":"1-66"},{"gene_uniquename":"SPAC1B2.04","chain":"F","position":"1-140"}],"title":"Cytochrome c oxidase from Schizosaccharomyces pombe","entry_authors":"Moe A,Adelroth P,Brzezinski P,Nasvik Ojemyr L","entry_authors_abbrev":"Moe A et al.","reference_uniquename":"PMID:36797353","experimental_method":"EM","resolution":"3.36"}]},{"uniquename":"PMID:14519123","title":"Fission yeast decaprenyl diphosphate synthase consists of Dps1 and the newly characterized Dlp1 protein in a novel heterotetrameric structure.","citation":"Eur J Biochem 2003 Oct;270(20):4113-21","abstract":"The analysis of the structure and function of long chain-producing polyprenyl diphosphate synthase, which synthesizes the side chain of ubiquinone, has largely focused on the prokaryotic enzymes, and little is known about the eukaryotic counterparts. Here we show that decaprenyl diphosphate synthase from Schizosaccharomyces pombe is comprised of a novel protein named Dlp1 acting in partnership with Dps1. Dps1 is highly homologous to other prenyl diphosphate synthases but Dlp1 shares only weak homology with Dps1. We showed that the two proteins must be present simultaneously in Escherichia coli transformants before ubiquinone-10, which is produced by S. pombe but not by E. coli, is generated. Furthermore, the two proteins were shown to form a heterotetrameric complex. This is unlike the prokaryotic counterparts, which are homodimers. The deletion mutant of dlp1 lacked the enzymatic activity of decaprenyl diphosphate synthase, did not produce ubiquinone-10 and had the typical ubiquinone-deficient S. pombe phenotypes, namely hypersensitivity to hydrogen peroxide, the need for antioxidants for growth on minimal medium and an elevated production of H2S. Both the dps1 (formerly dps) and dlp1 mutants could generate ubiquinone when they were transformed with a bacterial decaprenyl diphosphate synthase, which functions in its host as a homodimer. This indicates that both dps1 and dlp1 are required for the S. pombe enzymatic activity. Thus, decaprenyl diphosphate from a eukaryotic origin has a heterotetrameric structure that is not found in prokaryotes.","authors":"Saiki R, Nagata A, Uchida N, Kainou T, Matsuda H, Kawamukai M","authors_abbrev":"Saiki R et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2003-10-02","publication_year":"2003","canto_session_key":"ddcbe348d70876b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-26 16:46:24","canto_approved_date":"2024-07-02 13:08:38","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-11-26 16:46:18","canto_added_date":"2012-02-24 05:50:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.12","SPBPJ4664.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-11-26"},{"uniquename":"PMID:10913970","title":"Nutrition and phylogeny of predacious yeasts.","citation":"Can J Microbiol 2000 Jun;46(6):495-505","abstract":"Yeast predation was studied with respect to the range of its distribution among ascomycetous yeasts, the range of yeast species that can be affected, and nutritional aspects of the phenomenon. The yeasts identified as predators belong to the Saccharomycopsis clade as defined on the basis of rDNA sequence relatedness. The 11 recognized species in the clade, plus three undescribed but related Candida species, were shown to be incapable of utilizing sulfate as sole source of sulfur, and all but two (Saccharomycopsis capsularis and Saccharomycopsis vini) were observed to penetrate and kill other yeasts under some conditions. Other unrelated sulfate transport-deficient yeasts (strains in the genera Pichia and Candida and the two known species of Starmera) are not predacious. The predacious species vary considerably as to the optimal environmental conditions that favour predation. Some are inhibited by the presence of rich nitrogenous nutrients, organic sulfur compounds, or higher concentrations of ammonium nitrogen, whereas other species may be stimulated under the same conditions. An attempt was made to correlate prey susceptibility to the excretion of substances that stimulate the growth of predators, but no correlation was detected between the two phenomena. The range of susceptible prey covers both ascomycetes and basidiomycetes, and includes Schizosaccharomyces pombe, which was previously thought to be immune. The achlorophyllous alga Prototheca zopfii is not killed by predacious yeasts, but the initial steps of penetration have been observed in some cases. Predacious species attack other predacious species, and in some cases, young cultures may penetrate older cultures of the same strain.","authors":"Lachance MA, Pupovac-Velikonja A, Natarajan S, Schlag-Edler B","authors_abbrev":"Lachance MA et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-07-29","publication_year":"2000","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16009599","title":"Inactivation of RAD52 aggravates RAD54 defects in mice but not in Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2005 Sep 28;4(10):1121-8","abstract":"RAD52 and RAD54 genes from Saccharomyces cerevisiae are required for double-strand break repair through homologous recombination and show epistatic interactions i.e., single and double mutant strains are equally sensitive to DNA damaging agents. In here we combined mutations in RAD52 and RAD54 homologs in Schizosaccharomyces pombe and mice. The analysis of mutant strains in S. pombe demonstrated nearly identical sensitivities of rhp54, rad22A and rad22B double and triple mutants to X-rays, cis-diamminedichloroplatinum and hydroxyurea. In this respect, the fission yeast homologs of RAD54 and RAD52 closely resemble their counterparts in S. cerevisiae. To verify if inactivation of RAD52 affects the DNA damage sensitivities of RAD54 deficient mice, several endpoints were studied in double mutant mice and in bone marrow cells derived from these animals. Haemopoietic depression in bone marrow and the formation of micronuclei after in vivo exposure to mitomycine C (MMC) was not increased in either single or double mutant mice in comparison to wildtype animals. The induction of sister chromatid exchanges in splenocytes was slightly reduced in the RAD54 mutant. A similar reduction was detected in the double mutant. However, a deficiency of RAD52 exacerbates the MMC survival of RAD54 mutant mice and also has a distinct effect on the survival of bone marrow cells after exposure to ionizing radiation. These findings may be explained by additive defects in HR in the double mutant but may also indicate a more prominent role for single-strand annealing in the absence of Rad54.","authors":"de Vries FA, Zonneveld JB, van Duijn-Goedhart A, Roodbergen M, Boei J, van Buul PP, Essers J, van Steeg H, van Zeeland AA, van Benthem J, Pastink A","authors_abbrev":"de Vries FA et al.","pubmed_publication_date":"28 Sep 2005","pubmed_entrez_date":"2005-07-13","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20949524","title":"Natural history of Christianson syndrome.","citation":"Am J Med Genet A 2010 Nov;152A(11):2775-83","abstract":"Christianson syndrome is an X-linked mental retardation syndrome characterized by microcephaly, impaired ocular movement, severe global developmental delay, hypotonia which progresses to spasticity, and early onset seizures of variable types. Gilfillan et al.2008] reported mutations in SLC9A6, the gene encoding the sodium/hydrogen exchanger NHE6, in the family first reported and in three others. They also noted the clinical similarities to Angelman syndrome and found cerebellar atrophy on MRI and elevated glutamate/glutamine in the basal ganglia on MRS. Here we report on nonsense mutations in two additional families. The natural history is detailed in childhood and adult life, the similarities to Angelman syndrome confirmed, and the MRI/MRS findings documented in three affected boys.","doi":"10.1002/ajmg.a.33093","authors":"Schroer RJ, Holden KR, Tarpey PS, Matheus MG, Griesemer DA, Friez MJ, Fan JZ, Simensen RJ, Strømme P, Stevenson RE, Stratton MR, Schwartz CE","authors_abbrev":"Schroer RJ et al.","pubmed_publication_date":"Nov 2010","pubmed_entrez_date":"2010-10-16","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15A10.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11937031","title":"CDK phosphorylation of Drc1 regulates DNA replication in fission yeast.","citation":"Curr Biol 2002 Apr 02;12(7):599-605","abstract":"Cyclin-dependent kinases (CDKs) are absolutely required for DNA replication in eukaryotic cells. CDKs are thought to activate one or more replication factors, but the identities of these proteins are unknown. Here we describe fission yeast Drc1, a protein required for DNA replication that is phosphorylated by Cdc2. Drc1 depletion leads to catastrophic mitotic divisions with incompletely replicated DNA, indicating that Drc1 is required for DNA synthesis and S-M replication checkpoint control. Drc1 associates with Cdc2 and is phosphorylated at the onset of S phase when Cdc2 is activated. Mutant Drc1 that lacks CDK phosphorylation sites is nonfunctional and fails to interact with Cut5 replication factor. These data suggest that Cdc2 promotes DNA replication by phosphorylating Drc1 and regulating its association with Cut5.","authors":"Noguchi E, Shanahan P, Noguchi C, Russell P","authors_abbrev":"Noguchi E et al.","pubmed_publication_date":"02 Apr 2002","pubmed_entrez_date":"2002-04-09","publication_year":"2002","canto_session_key":"8e48c14b6338b11","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-04 16:46:43","canto_approved_date":"2026-02-01 09:39:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-10-10 10:10:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03","SPAC6B12.11","SPBC32F12.09","SPAC23C4.18c","SPBC14C8.07c","SPAPB2B4.03"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-04-04"},{"uniquename":"PMID:15714295","title":"Unique regulation of glyoxalase I activity during osmotic stress response in the fission yeast Schizosaccharomyces pombe: neither the mRNA nor the protein level of glyoxalase I increase under conditions that enhance its activity.","citation":"Arch Microbiol 2005 Mar;183(3):224-7","abstract":"Glyoxalase I is a ubiquitous enzyme that catalyzes the conversion of methylglyoxal, a toxic 2-oxoaldehyde derived from glycolysis, to S-D-lactoylglutathione. The activity of glyoxalase I in the fission yeast Schizosaccharomyces pombe was increased by osmotic stress induced by sorbitol. However, neither the mRNA levels of its structural gene nor its protein levels increased under the same conditions. Cycloheximide blocked the induction of glyoxalase I activity in cells exposed to osmotic stress. In addition, glyoxalase I activity was increased in stress-activated protein kinase-deficient mutants (wis1 and spc1). We present evidence for the post-translational regulation of glyoxalase I by osmotic stress in the fission yeast.","authors":"Takatsume Y, Izawa S, Inoue Y","authors_abbrev":"Takatsume Y et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-02-17","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12C2.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24190059","title":"Putative frameshift suppressors in Schizosaccharomyces pombe.","citation":"Curr Genet 1981 May;3(2):133-43","abstract":"Nine genetically distinct suppressors of ICR-170-induced ade6 and ade7 mutations have been identified in Schizosaccharomyces pombe. The nine suppressors of ICR-170-induced and spontaneous origin have been assigned to the three chromosomes by haploidization and meiotic analysis. They do not suppress missense or nonsense mutations and are therefore likely to be frameshift suppressors. Based on the spectrum of suppression, the nine suppressors fall into two mutually exclusive groups. Group I comprises the two dominant suppressors sufl and suf11. Group II consists of the seven dominant suppressors suf2 through suf8. The suppressors of both groups are inefficient and all lead to a marked reduction of growth rate. Within suppressor groups, combinations of suppressors lead to drastic reductions of growth rates and to an increased efficiency of suppression. Freely segregating modifiers of suppression increasing and decreasing the efficiency of supression have been found for all the suppressors. The two omnipotent suppressors sup1 and sup2 increase the efficiency of suppression of some frameshift suppressors. The suf5 locus is unstable and reverts at very high frequency both meiotically and mitotically.","doi":"10.1007/BF00365717","authors":"Hottinger H, Leupold U","authors_abbrev":"Hottinger H et al.","pubmed_publication_date":"May 1981","pubmed_entrez_date":"2013-11-06","publication_year":"1981","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 06:09:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9439726","title":"Molecular mechanisms controlling sensitivity to toxic metal ions in yeast.","citation":"Toxicol Appl Pharmacol 1997 Dec;147(2):312-8","abstract":"Contamination of the environment has made toxic metal ions a major health issue. The use of yeasts as model systems for the identification of molecular mechanisms that control sensitivity to these agents is particularly attractive because of the ease of genetic manipulation and the availability of the complete Saccharomyces cerevisiae genomic sequence. This paper reviews information on those genes and mechanisms that have been identified in both the budding yeast S. cerevisiae and the fission yeast Schizosaccharomyces pombe as being capable of modulating sensitivity to important toxic metals. The factors that influence sensitivity to toxic metal ions include cellular thiols (glutathione, phytochelatins, labile sulfide, and metallothioneins) and the products of genes directly and indirectly involved in the transport or sequestration of the metal ion. A complete understanding of the molecular basis of sensitivity to toxic metal ions in lower organisms is expected to provide useful insights in the metal ion detoxification pathways and diseases related to these pathways in humans.","authors":"Perego P, Howell SB","authors_abbrev":"Perego P et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1998-01-24","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30715470","title":"RNA surveillance by uridylation-dependent RNA decay in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2019 Apr 08;47(6):3045-3057","abstract":"Uridylation-dependent RNA decay is a widespread eukaryotic pathway modulating RNA homeostasis. Terminal uridylyltransferases (Tutases) add untemplated uridyl residues to RNA 3'-ends, marking them for degradation by the U-specific exonuclease Dis3L2. In Schizosaccharomyces pombe, Cid1 uridylates a variety of RNAs. In this study, we investigate the prevalence and impact of uridylation-dependent RNA decay in S. pombe by transcriptionally profiling cid1 and dis3L2 deletion strains. We found that the exonuclease Dis3L2 represents a bottleneck in uridylation-dependent mRNA decay, whereas Cid1 plays a redundant role that can be complemented by other Tutases. Deletion of dis3L2 elicits a cellular stress response, upregulating transcription of genes involved in protein folding and degradation. Misfolded proteins accumulate in both deletion strains, yet only trigger a strong stress response in dis3L2 deficient cells. While a deletion of cid1 increases sensitivity to protein misfolding stress, a dis3L2 deletion showed no increased sensitivity or was even protective. We furthermore show that uridylyl- and adenylyltransferases cooperate to generate a 5'-NxAUUAAAA-3' RNA motif on dak2 mRNA. Our studies elucidate the role of uridylation-dependent RNA decay as part of a global mRNA surveillance, and we found that perturbation of this pathway leads to the accumulation of misfolded proteins and elicits cellular stress responses.","doi":"10.1093/nar/gkz043","authors":"Chung CZ, Jaramillo JE, Ellis MJ, Bour DYN, Seidl LE, Jo DHS, Turk MA, Mann MR, Bi Y, Haniford DB, Duennwald ML, Heinemann IU","authors_abbrev":"Chung CZ et al.","pubmed_publication_date":"08 Apr 2019","pubmed_entrez_date":"2019-02-05","publication_year":"2019","canto_session_key":"223eb35ca89ea574","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-02-06 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18416603","title":"Reconstitution of DNA strand exchange mediated by Rhp51 recombinase and two mediators.","citation":"PLoS Biol 2008 Apr 15;6(4):e88","abstract":"In the fission yeast Schizosaccharomyces pombe, genetic evidence suggests that two mediators, Rad22 (the S. pombe Rad52 homolog) and the Swi5-Sfr1 complex, participate in a common pathway of Rhp51 (the S. pombe Rad51 homolog)-mediated homologous recombination (HR) and HR repair. Here, we have demonstrated an in vitro reconstitution of the central step of DNA strand exchange during HR. Our system consists entirely of homogeneously purified proteins, including Rhp51, the two mediators, and replication protein A (RPA), which reflects genetic requirements in vivo. Using this system, we present the first robust biochemical evidence that concerted action of the two mediators directs the loading of Rhp51 onto single-stranded DNA (ssDNA) precoated with RPA. Dissection of the reaction reveals that Rad22 overcomes the inhibitory effect of RPA on Rhp51-Swi5-Sfr1-mediated strand exchange. In addition, Rad22 negates the requirement for a strict order of protein addition to the in vitro system. However, despite the presence of Rad22, Swi5-Sfr1 is still essential for strand exchange. Importantly, Rhp51, but neither Rad22 nor the Swi5-Sfr1 mediator, is the factor that displaces RPA from ssDNA. Swi5-Sfr1 stabilizes Rhp51-ssDNA filaments in an ATP-dependent manner, and this stabilization is correlated with activation of Rhp51 for the strand exchange reaction. Rad22 alone cannot activate the Rhp51 presynaptic filament. AMP-PNP, a nonhydrolyzable ATP analog, induces a similar stabilization of Rhp51, but this stabilization is independent of Swi5-Sfr1. However, hydrolysis of ATP is required for processive strand transfer, which results in the formation of a long heteroduplex. Our in vitro reconstitution system has revealed that the two mediators have indispensable, but distinct, roles for mediating Rhp51 loading onto RPA-precoated ssDNA.","doi":"10.1371/journal.pbio.0060088","authors":"Kurokawa Y, Murayama Y, Haruta-Takahashi N, Urabe I, Iwasaki H","authors_abbrev":"Kurokawa Y et al.","pubmed_publication_date":"15 Apr 2008","pubmed_entrez_date":"2008-04-18","publication_year":"2008","canto_session_key":"8490fc7b048193c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-12 09:20:42","canto_approved_date":"2024-07-12 09:20:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-12 09:20:37","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPBC409.03","SPBC28F2.07","SPAC644.14c"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2024-07-12"},{"uniquename":"PMID:33244789","title":"Strongly oversized fission yeast cells lack any size control and tend to grow linearly rather than bilinearly.","citation":"Yeast 2021 Mar;38(3):206-221","abstract":"During the mitotic cycle, the rod-shaped fission yeast cells grow only at their tips. The newly born cells grow first unipolarly at their old end, but later in the cycle, the 'new end take-off' event occurs, resulting in bipolar growth. Photographs were taken of several steady-state and induction synchronous cultures of different cell cycle mutants of fission yeast, generally larger than wild type. Length measurements of many individual cells were performed from birth to division. For all the measured growth patterns, three different functions (linear, bilinear and exponential) were fitted, and the most adequate one was chosen by using specific statistical criteria, considering the altering parameter numbers. Although the growth patterns were heterogeneous in all the cultures studied, we could find some tendencies. In cultures with sufficiently wide size distribution, cells large enough at birth tend to grow linearly, whereas the other cells generally tend to grow bilinearly. We have found that among bilinearly growing cells, the larger they are at birth, the rate change point during their bilinear pattern occurs earlier in the cycle. This shifting near to the beginning of the cycle might finally cause a linear pattern, if the cells are even larger. In all of the steady-state cultures studied, a size control mechanism operates to maintain homeostasis. By contrast, strongly oversized cells of induction synchronous cultures lack any sizer, and their cycle rather behaves like an adder. We could determine the critical cell size for both the G1 and G2 size controls, where these mechanisms become cryptic. TAKE AWAY: Most individual fission yeast cells in steady-state cultures grow bilinearly. In strongly oversized fission yeast cells, linear growth dominates over bilinear. Above birth length thresholds, both the G1 and G2 size controls become cryptic.","doi":"10.1002/yea.3535","authors":"Nagy Z, Medgyes-Horváth A, Vörös E, Sveiczer Á","authors_abbrev":"Nagy Z et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2020-11-27","publication_year":"2021","canto_session_key":"12f56c5cf98104ce","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-11-29 01:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD138","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36305816","title":"A guard protein mediated quality control mechanism monitors 5'-capping of pre-mRNAs.","citation":"Nucleic Acids Res 2022 Oct 28;50(19):11301-11314","abstract":"Efficient gene expression requires properly matured mRNAs for functional transcript translation. Several factors including the guard proteins monitor maturation and act as nuclear retention factors for unprocessed pre-mRNAs. Here we show that the guard protein Npl3 monitors 5'-capping. In its absence, uncapped transcripts resist degradation, because the Rat1-Rai1 5'-end degradation factors are not efficiently recruited to these faulty transcripts. Importantly, in npl3Δ, these improperly capped transcripts escape this quality control checkpoint and leak into the cytoplasm. Our data suggest a model in which Npl3 associates with the Rai1 bound pre-mRNAs. In case the transcript was properly capped and is thus CBC (cap binding complex) bound, Rai1 dissociates from Npl3 allowing the export factor Mex67 to interact with this guard protein and support nuclear export. In case Npl3 does not detect proper capping through CBC attachment, Rai1 binding persists and Rat1 can join this 5'-complex to degrade the faulty transcript.","doi":"10.1093/nar/gkac952","authors":"Klama S, Hirsch AG, Schneider UM, Zander G, Seel A, Krebber H","authors_abbrev":"Klama S et al.","pubmed_publication_date":"28 Oct 2022","pubmed_entrez_date":"2022-10-28","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2777915","title":"Characterization of the fission yeast cdc10+ protein that is required for commitment to the cell cycle.","citation":"J Cell Sci 1989 Jan;92 ( Pt 1):51-6","abstract":"We have used antiserum raised against a beta-galactosidase-cdc10+ fusion protein to identify the protein product of the cdc10+ start gene of Schizosaccharomyces pombe. This gene is required for progress through the G1 phase of the cell cycle and for activating processes such as the increase in histone mRNA level in preparation for S phase. The protein has an apparent molecular weight of 87,000 and is phosphorylated on multiple serine residues. The protein remains phosphorylated throughout the mitotic cell cycle and shows no significant steady-state changes in level. The antiserum has also detected a protein similar in size to p87cdc10 in human cells.","authors":"Simanis V, Nurse P","authors_abbrev":"Simanis V et al.","pubmed_publication_date":"Jan 1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_session_key":"08532f14c26cfcfc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-06-30 16:56:06","canto_approved_date":"2024-04-04 11:09:15","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-06-30 15:46:13","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-30"},{"uniquename":"PMID:22976354","title":"Determining proteome-wide expression levels using reverse protein arrays in fission yeast.","citation":"Nat Protoc 2012 Oct;7(10):1830-5","abstract":"Global protein expression profiling of various mutants or growth conditions is currently a major challenge in biology. Here we provide a protocol for a strategy that we recently developed that couples ORFeome-based (ORF denotes open reading frame) expression to reverse protein arrays; this approach accurately quantifies more than 99% of the predicted fission yeast proteins in various genetic backgrounds. The first stage of this two-stage protocol requires mass mating between any fertile fission yeast mutant of interest and the integrated fission yeast-tagged ORFeome followed by selection of recombinant haploids. The second stage of the protocol, called reverse protein arrays, involves simple large-scale extraction of total proteins, which are then spotted on nitrocellulose membranes for detection by quantitative dot blot. When handled manually, the entire protocol takes about 2 months. However, the process could easily be automated and should also be applicable to other organisms.","doi":"10.1038/nprot.2012.114","authors":"Bauer F, Matsuyama A, Yoshida M, Hermand D","authors_abbrev":"Bauer F et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-09-15","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15489193","title":"Programmed cell death in fission yeast.","citation":"FEMS Yeast Res 2004 Nov;5(2):111-7","abstract":"Recently a metacaspase, encoded by YCA1, has been implicated in a primitive form of apoptosis or programmed cell death in yeast. Previously it had been shown that over-expression of mammalian pro-apoptotic proteins can induce cell death in yeast, but the mechanism of how cell death occurred was not clearly established. More recently, it has been shown that DNA or oxidative damage, or other cell cycle blocks, can result in cell death that mimics apoptosis in higher cells. Also, in fission yeast deletion of genes required for triacylglycerol synthesis leads to cell death and expression of apoptotic markers. A metacaspase sharing greater than 40% identity to budding yeast Yca1 has been identified in fission yeast, however, its role in programmed cell death is not yet known. Analysis of the genetic pathways that influence cell death in yeast may provide insights into the mechanisms of apoptosis in all eukaryotic organisms.","authors":"Rodriguez-Menocal L, D'Urso G","authors_abbrev":"Rodriguez-Menocal L et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-19","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30528393","title":"Schizosaccharomyces pombe contains separate CC- and A-adding tRNA nucleotidyltransferases.","citation":"Biochem Biophys Res Commun 2019 Jan 15;508(3):785-790","abstract":"A specific cytidine-cytidine-adenosine (CCA) sequence is required at the 3'-terminus of all functional tRNAs. This sequence is added during tRNA maturation or repair by tRNA nucleotidyltransferase enzymes. While most eukaryotes have a single enzyme responsible for CCA addition, some bacteria have separate CC- and A-adding activities. The fungus, Schizosaccharomyces pombe, has two genes (cca1 and cca2) that are thought, based on predicted amino acid sequences, to encode tRNA nucleotidyltransferases. Here, we show that both genes together are required to complement a Saccharomyces cerevisiae strain bearing a null mutation in the single gene encoding its tRNA nucleotidyltransferase. Using enzyme assays we show further that the purified S. pombe cca1 gene product specifically adds two cytidine residues to a tRNA substrate lacking this sequence while the cca2 gene product specifically adds the terminal adenosine residue thereby completing the CCA sequence. These data indicate that S. pombe represents the first eukaryote known to have separate CC- and A-adding activities for tRNA maturation and repair. In addition, we propose that a novel structural change in a tRNA nucleotidyltransferase is responsible for defining a CC-adding enzyme.","doi":"10.1016/j.bbrc.2018.11.131","authors":"Reid NE, Ngou JS, Joyce PBM","authors_abbrev":"Reid NE et al.","pubmed_publication_date":"15 Jan 2019","pubmed_entrez_date":"2018-12-12","publication_year":"2019","canto_session_key":"f0d230c2ef37468d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nathalie Reid","canto_first_approved_date":"2019-04-23 12:24:51","canto_approved_date":"2024-02-14 16:14:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-04-23 12:22:33","canto_added_date":"2018-12-13 01:15:04","annotation_curators":[{"name":"Nathalie Reid","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.10","SPAC1093.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-04-23"},{"uniquename":"PMID:34133218","title":"Redistribution of centrosomal proteins by centromeres and Polo kinase controls partial nuclear envelope breakdown in fission yeast.","citation":"Mol Biol Cell 2021 Aug 01;32(16):1487-1500","abstract":"Proper mitotic progression in  Schizosaccharomyces pombe  requires partial nuclear envelope breakdown (NEBD) and insertion of the spindle pole body (SPB-yeast centrosome) to build the mitotic spindle. Linkage of the centromere to the SPB is vital to this process, but why that linkage is important is not well understood. Utilizing high-resolution structured illumination microscopy, we show that the conserved Sad1-UNC-84 homology-domain protein Sad1 and other SPB proteins redistribute during mitosis to form a ring complex around SPBs, which is a precursor for localized NEBD and spindle formation. Although the Polo kinase Plo1 is not necessary for Sad1 redistribution, it localizes to the SPB region connected to the centromere, and its activity is vital for redistribution of other SPB ring proteins and for complete NEBD at the SPB to allow for SPB insertion. Our results lead to a model in which centromere linkage to the SPB drives redistribution of Sad1 and Plo1 activation that in turn facilitate partial NEBD and spindle formation through building of a SPB ring structure.","doi":"10.1091/mbc.E21-05-0239","authors":"Bestul AJ, Yu Z, Unruh JR, Jaspersen SL","authors_abbrev":"Bestul AJ et al.","pubmed_publication_date":"01 Aug 2021","pubmed_entrez_date":"2021-06-16","publication_year":"2021","canto_session_key":"4b79f8edcf2340db","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-06-13 19:18:48","canto_approved_date":"2026-06-13 19:18:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-06-06 14:47:02","canto_added_date":"2021-07-05 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.10","SPBC1604.18c","SPBC19C7.10","SPCC4G3.11","SPAC8F11.06","SPAC1786.03","SPBC649.05","SPBC12D12.01","SPBC11B10.09","SPCC320.13c","SPBC2G2.14","SPBC947.12","SPAC23C11.16"],"gene_count":13,"ltp_gene_count":8,"approved_date":"2026-06-13"},{"uniquename":"PMID:33534609","title":"Computational modeling of chromosome re-replication in mutant strains of fission yeast.","citation":"Mol Biol Cell 2021 Apr 19;32(9):830-841","abstract":"Typically cells replicate their genome only once per division cycle, but under some circumstances, both natural and unnatural, cells synthesize an overabundance of DNA, either in a disorganized manner (\"overreplication\") or by a systematic doubling of chromosome number (\"endoreplication\"). These variations on the theme of DNA replication and division have been studied in strains of fission yeast,  Schizosaccharomyces pombe , carrying mutations that interfere with the function of mitotic cyclin-dependent kinase (Cdk1:Cdc13) without impeding the roles of DNA-replication loading factor (Cdc18) and S-phase cyclin-dependent kinase (Cdk1:Cig2). Some of these mutations support endoreplication, and some overreplication. In this paper, we propose a dynamical model of the interactions among the proteins governing DNA replication and cell division in fission yeast. By computational simulations of the mathematical model, we account for the observed phenotypes of these re-replicating mutants, and by theoretical analysis of the dynamical system, we provide insight into the molecular distinctions between overreplicating and endoreplicating cells. In the case of induced overproduction of regulatory proteins, our model predicts that cells first switch from normal mitotic cell cycles to growth-controlled endoreplication, and ultimately to disorganized overreplication, parallel to the slow increase of protein to very high levels.","doi":"10.1091/mbc.E20-09-0610","authors":"Novák B, Tyson JJ","authors_abbrev":"Novák B et al.","pubmed_publication_date":"19 Apr 2021","pubmed_entrez_date":"2021-02-03","publication_year":"2021","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2021-02-05 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37893202","title":"A Normalization Protocol Reduces Edge Effect in High-Throughput Analyses of Hydroxyurea Hypersensitivity in Fission Yeast.","citation":"Biomedicines 2023 Oct 18;11(10)","abstract":"Edge effect denotes better growth of microbial organisms situated at the edge of the solid agar media. Although the precise reason underlying edge effect is unresolved, it is generally attributed to greater nutrient availability with less competing neighbors at the edge. Nonetheless, edge effect constitutes an unavoidable confounding factor that results in misinterpretation of cell fitness, especially in high-throughput screening experiments widely employed for genome-wide investigation using microbial gene knockout or mutant libraries. Here, we visualize edge effect in high-throughput high-density pinning arrays and report a normalization approach based on colony growth rate to quantify drug (hydroxyurea)-hypersensitivity in fission yeast strains. This normalization procedure improved the accuracy of fitness measurement by compensating cell growth rate discrepancy at different locations on the plate and reducing false-positive and -negative frequencies. Our work thus provides a simple and coding-free solution for a struggling problem in robotics-based high-throughput screening experiments.","doi":"10.3390/biomedicines11102829","authors":"Lam UT, Nguyen TTT, Raechell R, Yang J, Singer H, Chen ES","authors_abbrev":"Lam UT et al.","pubmed_publication_date":"18 Oct 2023","pubmed_entrez_date":"2023-10-28","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-10-28 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5878260","title":"Nitrous acid-induced mosaicism in schizosaccharomyces pombe.","citation":"Mutat Res 1965 Oct;2(5):395-402","abstract":"","authors":"Nasim A, Clarke CH","authors_abbrev":"Nasim A et al.","pubmed_publication_date":"Oct 1965","pubmed_entrez_date":"1965-10-01","publication_year":"1965","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18397885","title":"The GP(Y/F) domain of TF1 integrase multimerizes when present in a fragment, and substitutions in this domain reduce enzymatic activity of the full-length protein.","citation":"J Biol Chem 2008 Jun 06;283(23):15965-74","abstract":"Integrases (INs) of retroviruses and long terminal repeat retrotransposons possess a C-terminal domain with DNA binding activity. Other than this binding activity, little is known about how the C-terminal domain contributes to integration. A stretch of conserved amino acids called the GP(Y/F) domain has been identified within the C-terminal IN domains of two distantly related families, the gamma-retroviruses and the metavirus retrotransposons. To enhance understanding of the C-terminal domain, we examined the function of the GP(Y/F) domain in the IN of Tf1, a long terminal repeat retrotransposon of Schizosaccharomyces pombe. The activities of recombinant IN were measured with an assay that modeled the reverse of integration called disintegration. Although deletion of the entire C-terminal domain disrupted disintegration activity, an alanine substitution (P365A) in a conserved amino acid of the GP(Y/F) domain did not significantly reduce disintegration. When assayed for the ability to join two molecules of DNA in a reaction that modeled forward integration, the P365A substitution disrupted activity. UV cross-linking experiments detected DNA binding activity in the C-terminal domain and found that this activity was not reduced by substitutions in two conserved amino acids of the GP(Y/F) domain, G364A and P365A. Gel filtration and cross-linking of a 71-amino acid fragment containing the GP(Y/F) domain revealed a surprising ability to form dimers, trimers, and tetramers that was disrupted by the G364A and P365A substitutions. These results suggest that the GP(Y/F) residues may play roles in promoting multimerization and intermolecular strand joining.","doi":"10.1074/jbc.M801354200","authors":"Ebina H, Chatterjee AG, Judson RL, Levin HL","authors_abbrev":"Ebina H et al.","pubmed_publication_date":"06 Jun 2008","pubmed_entrez_date":"2008-04-10","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR12652","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YOL147C","HGNC:8852","HGNC:8853","SPAC1F12.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:27061734","title":"Condensin-mediated chromosome organization in fission yeast.","citation":"Curr Genet 2016 Nov;62(4):739-743","abstract":"Genome/chromosome structures are formed by a hierarchy of organizing processes ranging from gene interactions to chromosome territory formation. The SMC complex, cohesin, mediates interactions among enhancers and promoters, thereby regulating transcription. Another SMC complex, condensin, also plays critical roles in genome organization, although the detailed mechanisms remain much less well understood. Here, we discuss our recent findings on how fission yeast condensin mediates interactions among genes and how condensin-dependent interactions play dual roles in the chromosome territory arrangement during interphase and in mitotic chromosome organization, which supports the fidelity of chromosome segregation. Our studies suggest that condensin serves as a functional ligature connecting gene interactions, chromosome territory arrangement, transcriptional regulation, and chromosome segregation.","authors":"Iwasaki O, Noma KI","authors_abbrev":"Iwasaki O et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-04-11","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-04-13 00:15:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17161897","title":"Mitochondrial topoisomerases and alternative splicing of the human TOP1mt gene.","citation":"Biochimie 2007 Apr;89(4):474-81","abstract":"Mitochondria are the only organelles containing metabolically active DNA besides nuclei. By analogy with the nuclear topoisomerases, mitochondrial topoisomerase activities are probably critical for maintaining the topology of mitochondrial DNA during replication, transcription, and repair. Mitochondrial diseases include a wide range of defects including neurodegeneracies, myopathies, metabolic abnormalities and premature aging. Vertebrates only have one known specific mitochondrial topoisomerase gene (TOP1mt), coding for a type IB topoisomerase. Like the mitochondrial DNA and RNA polymerase, the TOP1mt gene is encoded in the nuclear genome. The TOP1mt gene possesses the 13 exon Top1B signature motif and codes for a mitochondrial targeting signals at the N-terminus of the Top1mt polypeptide. This review summarizes our current knowledge of mitochondrial topoisomerases (type IA, IB and type II) in eukaryotes including budding and fission yeasts (Saccharomyces cerevisiae and Schizosaccharomyces pombe) and protozoan parasites (kinetoplastidiae and plasmodium). It also includes new data showing alternative splice variants of human TOP1mt.","authors":"Zhang H, Meng LH, Pommier Y","authors_abbrev":"Zhang H et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2006-12-13","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21745468","title":"LAMMER kinase Kic1 is involved in pre-mRNA processing.","citation":"Exp Cell Res 2011 Oct 01;317(16):2308-20","abstract":"The LAMMER kinases are conserved through evolution. They play vital roles in cell growth/differentiation, development, and metabolism. One of the best known functions of the kinases in animal cells is the regulation of pre-mRNA splicing. Kic1 is the LAMMER kinase in fission yeast Schizosaccharomyces pombe. Despite the reported pleiotropic effects of kic1+ deletion/overexpression on various cellular processes the involvement of Kic1 in splicing remains elusive. In this study, we demonstrate for the first time that Kic1 not only is required for efficient splicing but also affects mRNA export, providing evidence for the conserved roles of LAMMER kinases in the unicellular context of fission yeast. Consistent with the hypothesis of its direct participation in multiple steps of pre-mRNA processing, Kic1 is predominantly present in the nucleus during interphase. In addition, the kinase activity of Kic1 plays a role in modulating its own cellular partitioning. Interestingly, Kic1 expression oscillates in a cell cycle-dependent manner and the peak level coincides with mitosis and cytokinesis, revealing a potential mechanism for controlling the kinase activity during the cell cycle. The novel information about the in vivo functions and regulation of Kic1 offers insights into the conserved biological roles fundamental to LAMMER kinases in eukaryotes.","doi":"10.1016/j.yexcr.2011.06.014","authors":"Tang Z, Luca M, Portillio J, Ngo B, Chang C, Wen T, Murray J, Carr A","authors_abbrev":"Tang Z et al.","pubmed_publication_date":"01 Oct 2011","pubmed_entrez_date":"2011-07-13","publication_year":"2011","canto_session_key":"64d2c81c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-11-06 16:33:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-06-21 20:55:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.05c","SPBC530.14c","SPAC1D4.11c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-06-21"},{"uniquename":"PMID:29317645","title":"Computational modelling of meiotic entry and commitment.","citation":"Sci Rep 2018 Jan 09;8(1):180","abstract":"In response to developmental and environmental conditions, cells exit the mitotic cell cycle and enter the meiosis program to generate haploid gametes from diploid germ cells. Once cells decide to enter the meiosis program they become irreversibly committed to the completion of meiosis irrespective of the presence of cue signals. How meiotic entry and commitment occur due to the dynamics of the regulatory network is not well understood. Therefore, we constructed a mathematical model of the regulatory network that controls the transition from mitosis to meiosis in Schizosaccharomyces pombe. Upon nitrogen starvation, yeast cells exit mitosis and undergo conjugation and meiotic entry. The model includes the regulation of Mei2, an RNA binding protein required for conjugation and meiotic entry, by multiple feedback loops involving Pat1, a kinase that keeps cells in mitosis, and Ste11, a transcription activator required for the sexual differentiation. The model accounts for various experimental observations and demonstrates that the activation of Mei2 is bistable, which ensures the irreversible commitment to meiosis. Further, we show by integrating the meiosis-specific regulation with a cell cycle model, the dynamics of cell cycle exit, G1 arrest and entry into meiosis under nitrogen starvation.","doi":"10.1038/s41598-017-17478-9","authors":"Bhola T, Kapuy O, Vinod PK","authors_abbrev":"Bhola T et al.","pubmed_publication_date":"09 Jan 2018","pubmed_entrez_date":"2018-01-11","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-01-12 01:15:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28191457","title":"The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants in  Schizosaccharomyces pombe .","citation":"Microb Cell 2017 Jan;4(1):16-28","abstract":"Prions are protein-based infectious entities associated with fatal brain diseases in animals, but also modify a range of host-cell phenotypes in the budding yeast,  Saccharomyces cerevisiae . Many questions remain about the evolution and biology of prions. Although several functionally distinct prion-forming proteins exist in  S. cerevisiae , [HET-s] of  Podospora anserina  is the only other known fungal prion. Here we investigated prion-like, protein-based epigenetic transmission in the fission yeast  Schizosaccharomyces pombe . We show that  S. pombe  cells can support the formation and maintenance of the prion form of the  S. cerevisiae  Sup35 translation factor [ PSI  + ], and that the formation and propagation of these Sup35 aggregates is inhibited by guanidine hydrochloride, indicating commonalities in prion propagation machineries in these evolutionary diverged yeasts. A proteome-wide screen identified the Ctr4 copper transporter subunit as a putative prion with a predicted prion-like domain. Overexpression of the  ctr4  gene resulted in large Ctr4 protein aggregates that were both detergent and proteinase-K resistant. Cells carrying such [ CTR  + ] aggregates showed increased sensitivity to oxidative stress, and this phenotype could be transmitted to aggregate-free [ ctr  - ] cells by transformation with [ CTR  + ] cell extracts. Moreover, this [ CTR  + ] phenotype was inherited in a non-Mendelian manner following mating with naïve [ ctr  - ] cells, but intriguingly the [ CTR  + ] phenotype was not eliminated by guanidine-hydrochloride treatment. Thus, Ctr4 exhibits multiple features diagnostic of other fungal prions and is the first example of a prion in fission yeast. These findings suggest that transmissible protein-based determinants of traits may be more widespread among fungi.","doi":"10.15698/mic2017.01.552","authors":"Sideri T, Yashiroda Y, Ellis DA, Rodríguez-López M, Yoshida M, Tuite MF, Bähler J","authors_abbrev":"Sideri T et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2017-02-14","publication_year":"2017","canto_session_key":"7792eb73b01ab912","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jurg Bahler","canto_first_approved_date":"2017-04-17 19:38:27","canto_approved_date":"2023-04-03 17:13:14","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2017-02-24 17:12:23","canto_added_date":"2017-02-15 01:15:13","annotation_curators":[{"name":"Jurg Bahler","community_curator":true,"annotation_count":2,"orcid":"0000-0003-4036-1532","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1393.10","SPAC1142.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-04-17"},{"uniquename":"PMID:3502942","title":"Sequence of the bifunctional ade1 gene in the purine biosynthetic pathway of the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1987;12(8):591-7","abstract":"The ade1 gene of the fission yeast Schizosaccharomyces pombe encodes a bifunctional polypeptide with glycinamide ribotide synthetase (GARSase) and aminoimidazole ribotide synthetase (AIRSase) enzyme activities. These enzyme activities carry out the 2nd and 5th steps, respectively, of the purine synthetic pathway. We report the cloning of the ade1 gene on a 4.4 kb Sau3A insert in the yeast shuttle vector pWH5. Integration of this genomic insert at or near the ade1 locus and its ability to complement, by transformation, three different types of ade1 mutants proved that it contains the ade1 chromosomal gene. Analysis of the nucleotide sequence of this insert revealed the presence of an uninterrupted open reading frame of 2,367 pb. This sequence, and the predicted 789 amino acid sequence encoded, both show a high degree of homology with the functionally equivalent ade5,7 gene sequence of Saccharomyces cerevisiae (approx. 60% overall in both cases) and Gart gene sequences of Drosophila melanogaster. The size of the ade1 RNA transcript is about 2.7 kb.","authors":"McKenzie R, Schuchert P, Kilbey B","authors_abbrev":"McKenzie R et al.","pubmed_publication_date":"1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_session_key":"851c2db3460a139c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:27:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-28 17:26:52","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC405.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-28"},{"uniquename":"PMID:9134774","title":"Antimicrobial action of essential oils: the effect of dimethylsulphoxide on the activity of cinnamon oil.","citation":"Lett Appl Microbiol 1997 Apr;24(4):269-75","abstract":"Fifty-one essential oils extracted from plants of known origin were tested for their antimicrobial activity against three bacteria, Pseudomonas aeruginosa, Staphylococcus aureus, Escherichia coli and four yeasts, Torulopsis utilis, Schizosaccharomyces pombe, Candida albicans and Saccharomyces cerevisiae using the drop diffusion method. All showed antimicrobial activity against at least one of the micro-organisms. Following this preliminary screening, 13 essential oils showing antimicrobial activity against at least five of the micro-organisms were tested in the range 50 micrograms ml-1 to 500 micrograms ml-1 using broth micro dilution techniques with dimethylsulphoxide (DMSO) as a dispersing solvent. The concentration of most of the oils required for total inhibition of growth was > 500 micrograms ml-1. Further studies on the antimicrobial action of cinnamon oil in the range 10-150 micrograms ml-1 showed that 50-fold higher activity was found when no dispersing solvent was used.","authors":"Hili P, Evans CS, Veness RG","authors_abbrev":"Hili P et al.","pubmed_publication_date":"Apr 1997","pubmed_entrez_date":"1997-04-01","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19308703","title":"Heterochromatin and the cohesion of sister chromatids.","citation":"Chromosome Res 2009;17(2):229-38","abstract":"Heterochromatin, once thought to be the useless junk of chromosomes, is now known to play significant roles in biology. Underlying much of this newfound fame are links between the repressive chromatin structure and cohesin, the protein complex that mediates sister chromatid cohesion. Heterochromatin-mediated recruitment and retention of cohesin to domains flanking centromeres promotes proper attachment of chromosomes to the mitotic and meiotic spindles. Heterochromatin assembled periodically between convergently transcribed genes also recruits cohesin, which promotes a novel form of transcription termination. Heterochromatin-like structures in budding yeast also recruit cohesin. Here the complex appears to regulate transcriptional silencing and recombination between repeated DNA sequences. The link between heterochromatin and cohesin is particularly relevant to human health. In Roberts-SC phocomelia syndrome, heterochromatic cohesion is selectively lost due to mutation of the acetyltransferase responsible for cohesin activation. In this review I discuss recent work that relates to these relationships between heterochromatin and cohesin.","doi":"10.1007/s10577-008-9012-z","authors":"Gartenberg M","authors_abbrev":"Gartenberg M","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-03-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34067465","title":"The Meiosis-Specific Crs1 Cyclin Is Required for Efficient S-Phase Progression and Stable Nuclear Architecture.","citation":"Int J Mol Sci 2021 May 22;22(11)","abstract":"Cyclins and CDKs (Cyclin Dependent Kinases) are key players in the biology of eukaryotic cells, representing hubs for the orchestration of physiological conditions with cell cycle progression. Furthermore, as in the case of meiosis, cyclins and CDKs have acquired novel functions unrelated to this primal role in driving the division cycle. Meiosis is a specialized developmental program that ensures proper propagation of the genetic information to the next generation by the production of gametes with accurate chromosome content, and meiosis-specific cyclins are widespread in evolution. We have explored the diversification of CDK functions studying the meiosis-specific Crs1 cyclin in fission yeast. In addition to the reported role in DSB (Double Strand Break) formation, this cyclin is required for meiotic S-phase progression, a canonical role, and to maintain the architecture of the meiotic chromosomes. Crs1 localizes at the SPB (Spindle Pole Body) and is required to stabilize the cluster of telomeres at this location ( bouquet  configuration), as well as for normal SPB motion. In addition, Crs1 exhibits CDK(Cdc2)-dependent kinase activity in a biphasic manner during meiosis, in contrast to a single wave of protein expression, suggesting a post-translational control of its activity. Thus, Crs1 displays multiple functions, acting both in cell cycle progression and in several key meiosis-specific events.","doi":"10.3390/ijms22115483","authors":"Bustamante-Jaramillo LF, Ramos C, Martín-Castellanos C","authors_abbrev":"Bustamante-Jaramillo LF et al.","pubmed_publication_date":"22 May 2021","pubmed_entrez_date":"2021-06-02","publication_year":"2021","canto_session_key":"51fe04707302115f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Cristina Martín-Castellanos","canto_first_approved_date":"2024-10-16 10:12:29","canto_approved_date":"2024-10-16 10:12:29","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-10-01 10:26:20","canto_added_date":"2021-06-04 00:15:04","annotation_curators":[{"name":"Cristina Martín-Castellanos","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":4,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC2G2.09c","SPAPB2B4.03","SPAC6G9.13c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-10-16"},{"uniquename":"PMID:14517947","title":"Genetic variation in a haplotype block spanning IDE influences Alzheimer disease.","citation":"Hum Mutat 2003 Nov;22(5):363-71","abstract":"Linkage studies have identified a large (>60-Mb) region on chromosome 10q that segregates with Alzheimer Disease (AD). Within the region, the gene for insulin degrading enzyme (IDE) represents a notable biological candidate given that it degrades amyloid beta-protein (one of the major constituents of senile plaques) and the intracellular amyloid precursor protein (APP) domain released by gamma-secretase processing. We have used a single nucleotide polymorphism (SNP) genetic association strategy to investigate AD in relation to a 480-kb region encompassing IDE. A 276-kb linkage disequilibrium block was revealed that spans three genes (IDE, KNSL1, and HHEX). Assessing this block in several independent sets of case-control materials (early- and late-onset AD) and focusing also upon quantitative measures that are pertinent to AD diagnosis and severity (MMSE scores, microtubule-associated protein Tau [MAPT] levels in CSF, degree of brain pathology, and age-at-onset) produced extensive evidence for significant AD association. Signals (p-values ranging from 0.05 to <1x10(-9)) were generally stronger when examining haplotypes rather than individual SNPs, and quantitative trait tests most uniformly revealed the detected associations. Consistent risk alleles and haplotypes were apparent across the study, with effects in some cases as large as that of the epsilon4 allele of APOE. A subsequent mutation screen of exons in all three suspect genes provided no evidence for common causative mutations. These results provide substantial evidence that genetic variation within or extremely close to IDE impacts both disease risk and traits related to the severity of AD.","authors":"Prince JA, Feuk L, Gu HF, Johansson B, Gatz M, Blennow K, Brookes AJ","authors_abbrev":"Prince JA et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-10-01","publication_year":"2003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPACUNK4.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24108582","title":"Molecular component distribution imaging of living cells by multivariate curve resolution analysis of space-resolved Raman spectra.","citation":"J Biomed Opt 2014 Jan;19(1):011016","abstract":"Label-free Raman microspectroscopy combined with a multivariate curve resolution (MCR) analysis can be a powerful tool for studying a wide range of biomedical molecular systems. The MCR with the alternating least squares (MCR-ALS) technique, which retrieves the pure component spectra from complicatedly overlapped spectra, has been successfully applied to in vivo and molecular-level analysis of living cells. The principles of the MCR-ALS analysis are reviewed with a model system of titanium oxide crystal polymorphs, followed by two examples of in vivo Raman imaging studies of living yeast cells, fission yeast, and budding yeast. Due to the non-negative matrix factorization algorithm used in the MCR-ALS analysis, the spectral information derived from this technique is just ready for physical and/or chemical interpretations. The corresponding concentration profiles provide the molecular component distribution images (MCDIs) that are vitally important for elucidating life at the molecular level, as stated by Schroedinger in his famous book, \"What is life?\" Without any a priori knowledge about spectral profiles, time- and space-resolved Raman measurements of a dividing fission yeast cell with the MCR-ALS elucidate the dynamic changes of major cellular components (lipids, proteins, and polysaccharides) during the cell cycle. The MCR-ALS technique also resolves broadly overlapped OH stretch Raman bands of water, clearly indicating the existence of organelle-specific water structures in a living budding yeast cell.","doi":"10.1117/1.JBO.19.1.011016","authors":"Ando M, Hamaguchi HO","authors_abbrev":"Ando M et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2013-10-11","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19911051","title":"The Schizosaccharomyces pombe JmjC-protein, Msc1, prevents H2A.Z localization in centromeric and subtelomeric chromatin domains.","citation":"PLoS Genet 2009 Nov;5(11):e1000726","abstract":"Eukaryotic genomes are repetitively packaged into chromatin by nucleosomes, however they are regulated by the differences between nucleosomes, which establish various chromatin states. Local chromatin cues direct the inheritance and propagation of chromatin status via self-reinforcing epigenetic mechanisms. Replication-independent histone exchange could potentially perturb chromatin status if histone exchange chaperones, such as Swr1C, loaded histone variants into wrong sites. Here we show that in Schizosaccharomyces pombe, like Saccharomyces cerevisiae, Swr1C is required for loading H2A.Z into specific sites, including the promoters of lowly expressed genes. However S. pombe Swr1C has an extra subunit, Msc1, which is a JumonjiC-domain protein of the Lid/Jarid1 family. Deletion of Msc1 did not disrupt the S. pombe Swr1C or its ability to bind and load H2A.Z into euchromatin, however H2A.Z was ectopically found in the inner centromere and in subtelomeric chromatin. Normally this subtelomeric region not only lacks H2A.Z but also shows uniformly lower levels of H3K4me2, H4K5, and K12 acetylation than euchromatin and disproportionately contains the most lowly expressed genes during vegetative growth, including many meiotic-specific genes. Genes within and adjacent to subtelomeric chromatin become overexpressed in the absence of either Msc1, Swr1, or paradoxically H2A.Z itself. We also show that H2A.Z is N-terminally acetylated before, and lysine acetylated after, loading into chromatin and that it physically associates with the Nap1 histone chaperone. However, we find a negative correlation between the genomic distributions of H2A.Z and Nap1/Hrp1/Hrp3, suggesting that the Nap1 chaperones remove H2A.Z from chromatin. These data describe H2A.Z action in S. pombe and identify a new mode of chromatin surveillance and maintenance based on negative regulation of histone variant misincorporation.","doi":"10.1371/journal.pgen.1000726","authors":"Buchanan L, Durand-Dubief M, Roguev A, Sakalar C, Wilhelm B, Strålfors A, Shevchenko A, Aasland R, Shevchenko A, Ekwall K, Francis Stewart A","authors_abbrev":"Buchanan L et al.","pubmed_publication_date":"Nov 2009","pubmed_entrez_date":"2009-11-14","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC550.12","SPAC343.11c","SPBC32H8.12c","SPBP23A10.08","SPAC11E3.01c","SPBP35G2.13c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:39096900","title":"Nucleosome remodeler exclusion by histone deacetylation enforces heterochromatic silencing and epigenetic inheritance.","citation":"Mol Cell 2024 Sep 05;84(17):3175-3191.e8","abstract":"Heterochromatin enforces transcriptional gene silencing and can be epigenetically inherited, but the underlying mechanisms remain unclear. Here, we show that histone deacetylation, a conserved feature of heterochromatin domains, blocks SWI/SNF subfamily remodelers involved in chromatin unraveling, thereby stabilizing modified nucleosomes that preserve gene silencing. Histone hyperacetylation, resulting from either the loss of histone deacetylase (HDAC) activity or the direct targeting of a histone acetyltransferase to heterochromatin, permits remodeler access, leading to silencing defects. The requirement for HDAC in heterochromatin silencing can be bypassed by impeding SWI/SNF activity. Highlighting the crucial role of remodelers, merely targeting SWI/SNF to heterochromatin, even in cells with functional HDAC, increases nucleosome turnover, causing defective gene silencing and compromised epigenetic inheritance. This study elucidates a fundamental mechanism whereby histone hypoacetylation, maintained by high HDAC levels in heterochromatic regions, ensures stable gene silencing and epigenetic inheritance, providing insights into genome regulatory mechanisms relevant to human diseases.","doi":"10.1016/j.molcel.2024.07.006","authors":"Sahu RK, Dhakshnamoorthy J, Jain S, Folco HD, Wheeler D, Grewal SIS","authors_abbrev":"Sahu RK et al.","pubmed_publication_date":"05 Sep 2024","pubmed_entrez_date":"2024-08-03","publication_year":"2024","canto_session_key":"42496a50873f70a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rakesh Kumar Sahu","canto_first_approved_date":"2025-07-02 09:15:28","canto_approved_date":"2026-06-24 06:27:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-13 15:11:27","canto_added_date":"2025-01-16 15:57:31","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":14,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Rakesh Kumar Sahu","community_curator":true,"annotation_count":62,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.08c","SPAC29B12.01","SPAC11E3.01c","SPCC1620.14c","SPAC664.01c","SPBC800.03","SPBC26H8.09c","SPAC1250.01","SPAC17G8.13c","SPBC4B4.03","SPAC1952.05","SPAC3G6.01","SPBP35G2.10"],"gene_count":13,"ltp_gene_count":11,"approved_date":"2025-07-02"},{"uniquename":"PMID:9034337","title":"Chk1 is a wee1 kinase in the G2 DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation.","citation":"EMBO J 1997 Feb 03;16(3):545-54","abstract":"The G2 DNA damage checkpoint ensures maintenance of cell viability by delaying progression into mitosis in cells which have suffered genomic damage. It is controlled by a number of proteins which are hypothesized to transduce signals through cell cycle regulators to delay activation of p34cdc2. Studies in mammalian cells have correlated induction of inhibitory tyrosine 15 (Y15) phosphorylation on p34cdc2 with the response to DNA damage. However, genetic studies in fission yeast have suggested that the major Y15 kinase, p107wee1, is not required for the cell cycle delay in response to DNA damage, although it is required for survival after irradiation. Thus, the target of the checkpoint, and hence the mechanism of cell cycle delay, remains unknown. We show here that Y15 phosphorylation is maintained in checkpoint-arrested fission yeast cells. Further, wee1 is required for cell cycle arrest induced by up-regulation of an essential component of this checkpoint, chk1. We observed that p107wee1 is hyperphosphorylated in cells delayed by chk1 overexpression or UV irradiation, and that p56chk1 can phosphorylate p107wee1 directly in vitro. These observations suggest that in response to DNA damage p107wee1 is phosphorylated by p56chk1 in vivo, and this results in maintenance of Y15 phosphorylation and hence G2 delay. In the absence of wee1, other Y15 kinases, such as p66mik1, may partially substitute for p107wee1 to induce cell cycle delay, but this wee1-independent delay is insufficient to maintain full viability. This study establishes a link between a G2 DNA damage checkpoint function and a core cell cycle regulator.","authors":"O'Connell MJ, Raleigh JM, Verkade HM, Nurse P","authors_abbrev":"O'Connell MJ et al.","pubmed_publication_date":"03 Feb 1997","pubmed_entrez_date":"1997-02-03","publication_year":"1997","canto_session_key":"98f0242de16564e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-04-17 11:07:34","canto_approved_date":"2023-04-13 12:19:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-10 10:51:40","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":15,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC24H6.05","SPAC644.06c","SPCC18B5.03","SPBC660.14","SPBC11B10.09"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-04-17"},{"uniquename":"PMID:10409438","title":"Cloning and mapping of the XRN2 gene to human chromosome 20p11.1-p11.2.","citation":"Genomics 1999 Jul 15;59(2):252-4","abstract":"The Dhm1 gene is the mouse homologue of the dhp1(+) gene of Schizosaccharomyces pombe, which is involved in homologous recombination and RNA metabolism, such as RNA synthesis and RNA trafficking, in S. pombe. Complementation analysis showed the Dhm1 gene on a multicopy plasmid can rescue the temperature-sensitivity mutation of dhp1(ts) and the lethality of the dhp1 null mutation. This finding suggests that Dhm1 has a function in mouse similar to that of dhp1(+). The human homologue of this gene, XRN2, has been identified. A 3.6-kb transcript of XRN2 was detected in 16 tissues examined and was more abundant in testis. By radiation hybrid panel mapping, the XRN2 gene was localized to chromosome 20p11.1-p11.2 between markers D20S180 and D20S871.","authors":"Zhang M, Yu L, Xin Y, Hu P, Fu Q, Yu C, Zhao S","authors_abbrev":"Zhang M et al.","pubmed_publication_date":"15 Jul 1999","pubmed_entrez_date":"1999-07-20","publication_year":"1999","canto_session_key":"b939fd0015e26df6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 17:30:20","canto_session_submitted_date":"2012-03-03 17:30:06","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.12c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:19858289","title":"Mss51 and Ssc1 facilitate translational regulation of cytochrome c oxidase biogenesis.","citation":"Mol Cell Biol 2010 Jan;30(1):245-59","abstract":"The intricate biogenesis of multimeric organellar enzymes of dual genetic origin entails several levels of regulation. In Saccharomyces cerevisiae, mitochondrial cytochrome c oxidase (COX) assembly is regulated translationally. Synthesis of subunit 1 (Cox1) is contingent on the availability of its assembly partners, thereby acting as a negative feedback loop that coordinates COX1 mRNA translation with Cox1 utilization during COX assembly. The COX1 mRNA-specific translational activator Mss51 plays a fundamental role in this process. Here, we report that Mss51 successively interacts with the COX1 mRNA translational apparatus, newly synthesized Cox1, and other COX assembly factors during Cox1 maturation/assembly. Notably, the mitochondrial Hsp70 chaperone Ssc1 is shown to be an Mss51 partner throughout its metabolic cycle. We conclude that Ssc1, by interacting with Mss51 and Mss51-containing complexes, plays a critical role in Cox1 biogenesis, COX assembly, and the translational regulation of these processes.","doi":"10.1128/MCB.00983-09","authors":"Fontanesi F, Soto IC, Horn D, Barrientos A","authors_abbrev":"Fontanesi F et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-10-28","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25B8.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12081644","title":"Fission yeast chk1 mutants show distinct responses to different types of DNA damaging treatments.","citation":"Genes Cells 2002 Jul;7(7):663-73","abstract":"Chk1 kinase is activated by phosphorylation at serine-345 by Rad3 checkpoint kinase and is required for DNA damage checkpoint in late S and G2 phase of S. pombe cell cycle. We studied the ability of two chk1 mutants, chk1-1 and chk1-2, to undergo phosphorylation and to delay cell cycle progression in response to different types of DNA lesions.\nBoth the Chk1-1 and Chk1-2 mutant proteins are phosphorylated to various extents when DNA is damaged in early G2 phase of cell cycle by either UV irradiation or gamma irradiation. However, chk1-2 mutant does not delay cell cycle progression in a dose dependent manner specifically upon gamma irradiations. This defect is not associated with an important loss of survival. Furthermore, both chk1 mutants survive to Camptothecin treatment despite undetectable Chk1-1 or Chk1-2 phosphorylated forms. We show that both mutant proteins are not phosphorylated in cds1 devoid cells treated with ribonucleotide reductase inhibitor hydroxyurea or when the replisome is affected by a thermosensitive mutation in DNA polymerase delta. This inability is associated with the loss of checkpoint function. We found that an increased level of Crb2/Rhp9 protein specifically complements the defect of the chk1-1 mutant allowing Chk1-1 phosphorylation upon treatment with hydroxyurea of dcds1 cells.\nMutants chk1-1 and chk1-2 behave differently according to the type of lesion generated on DNA.","authors":"Francesconi S, Smeets M, Grenon M, Tillit J, Blaisonneau J, Baldacci G","authors_abbrev":"Francesconi S et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-06-26","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC342.05","SPCC1259.13"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:35048989","title":"The Cdc42 GTPase-activating protein Rga6 promotes the cortical localization of septin.","citation":"J Cell Sci 2022 Feb 15;135(4)","abstract":"Septins are a family of filament-forming GTP-binding proteins that regulate fundamental cellular activities, such as cytokinesis and cell polarity. In general, septin filaments function as barriers and scaffolds on the cell cortex. However, little is known about the mechanism that governs the recruitment and localization of the septin complex to the cell cortex. Here, we identified the Cdc42 GTPase-activating protein Rga6 as a key protein involved in promoting the localization of the septin complex to the cell cortex in the fission yeast Schizosaccharomyces pombe. Rga6 interacts with the septin complex and partially colocalizes with the septin complex on the cell cortex. Live-cell microscopy analysis further showed septin enrichment at the cortical regions adjacent to the growing cell tip. The septin enrichment likely plays a crucial role in confining active Cdc42 to the growing cell tip. Hence, our findings support a model whereby Rga6 regulates polarized cell growth partly through promoting targeted localization of the septin complex on the cell cortex. This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.259228","authors":"Zheng S, Zheng B, Liu Z, Ma X, Liu X, Yao X, Wei W, Fu C","authors_abbrev":"Zheng S et al.","pubmed_publication_date":"15 Feb 2022","pubmed_entrez_date":"2022-01-20","publication_year":"2022","canto_session_key":"bd3b292ab4e2a48a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-01-22 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC354.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11560889","title":"Multiple interactions among the components of the recombinational DNA repair system in Schizosaccharomyces pombe.","citation":"Genetics 2001 Sep;159(1):91-105","abstract":"Schizosaccharomyces pombe Rhp55 and Rhp57 are RecA-like proteins involved in double-strand break (DSB) repair. Here we demonstrate that Rhp55 and Rhp57 proteins strongly interact in vivo, similar to Saccharomyces cerevisiae Rad55p and Rad57p. Mutations in the conserved ATP-binding/hydrolysis folds of both the Rhp55 and Rhp57 proteins impaired their function in DNA repair but not in cell proliferation. However, when combined, ATPase fold mutations in Rhp55p and Rhp57p resulted in severe defects of both functions, characteristic of the deletion mutants. Yeast two-hybrid analysis also revealed other multiple in vivo interactions among S. pombe proteins involved in recombinational DNA repair. Similar to S. cerevisiae Rad51p-Rad54p, S. pombe Rhp51p and Rhp54p were found to interact. Both putative Rad52 homologs in S. pombe, Rad22p and Rti1p, were found to interact with the C-terminal region of Rhp51 protein. Moreover, Rad22p and Rti1p exhibited mutual, as well as self-, interactions. In contrast to the S. cerevisiae interacting pair Rad51p-Rad55p, S. pombe Rhp51 protein strongly interacted with Rhp57 but not with Rhp55 protein. In addition, the Rti1 and Rad22 proteins were found to form a complex with the large subunit of S. pombe RPA. Our data provide compelling evidence that most, but not all, of the protein-protein interactions found in S. cerevisiae DSB repair are evolutionarily conserved.","authors":"Tsutsui Y, Khasanov FK, Shinagawa H, Iwasaki H, Bashkirov VI","authors_abbrev":"Tsutsui Y et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-09-19","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.03c","SPAC30D11.10","SPAC644.14c","SPBC660.13c","SPBC4C3.05c","SPAC20H4.07","SPAC15A10.03c","SPBC119.14"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:11499925","title":"Expression, processing and high level secretion of a virus toxin in fission yeast.","citation":"Appl Microbiol Biotechnol 2001 Jul;56(1-2):165-72","abstract":"The virally encoded K28 toxin of Saccharomyces cerevisiae kills sensitive yeast cells in a multi-step receptor-mediated fashion by cell cycle arrest and inhibition of DNA synthesis. In vivo, the toxin is translated as a 38 kDa preprotoxin (pptox) which is enzymatically processed to the biologically active alpha/beta heterodimer during passage through the yeast secretory pathway. Here, we demonstrate that Schizosaccharomyces pombe, a yeast from which no natural toxin-secreting killer strains are known, is perfectly capable of expressing a killer phenotype. Episomal as well as integrating K28 pptox gene cassettes were constructed that allowed a tightly thiamine-regulated killer phenotype expression under transcriptional control of the Sch. pombe nmt1 promotor. Northern analysis of the toxin-coding transcript as well as Western analysis of the secreted toxin indicated that fission yeast is capable of expressing a correctly processed and fully functional virus toxin. Moreover, toxin secretion in recombinant Sch. pombe was at least ten-fold higher than in any natural and/or recombinant Sac. cerevisiae killer strain, indicating that pptox-derived vectors might be attractive in the fast growing field of heterologous protein expression and secretion in yeast.","authors":"Heintel T, Zagorc T, Schmitt MJ","authors_abbrev":"Heintel T et al.","pubmed_publication_date":"Jul 2001","pubmed_entrez_date":"2001-08-14","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36947867","title":"New TSPO Crystal Structures of Mutant and Heme-Bound Forms with Altered Flexibility, Ligand Binding, and Porphyrin Degradation Activity.","citation":"Biochemistry 2023 Apr 04;62(7):1262-1273","abstract":"The ancient protein TSPO (translocator protein 18kD) is found in all kingdoms and was originally identified as a binding site of benzodiazepine drugs. Its physiological function remains unclear, although porphyrins are conserved ligands. Several crystal structures of bacterial TSPO and nuclear magnetic resonance structures of a mouse form have revealed monomer and dimer configurations, but there have been no reports of structures with a physiological ligand. Here, we present the first X-ray structures of  Rhodobacter sphaeroides  TSPO with a physiological ligand bound. Two different variants (substituting threonine for alanine at position 139 (A139T) and phenylalanine for alanine at position 138 (A138F)) yielded well-diffracting crystals giving structures of both apo- and heme-containing forms. Both variants have wild-type micromolar affinity for heme and protoporphyrin IX, but A139T has very low ability to accelerate the breakdown of porphyrin in the presence of light and oxygen. The binding of heme to one protomer of the dimer of either mutant induces a more rigid structure, both in the heme-binding protomer and the protomer without heme bound, demonstrating an allosteric response. Ensemble refinement of the X-ray data reveals distinct regions of altered flexibility in response to single heme binding to the dimer. The A139T variant shows a more rigid structure overall, which may relate to extra hydrogen bonding of waters captured in the heme crevice. As TSPO has been suggested to have a role in heme delivery from mitochondria to the cytoplasm, the new structures provide potential clues regarding the structural basis of such activity.","doi":"10.1021/acs.biochem.2c00612","authors":"Liu J, Hiser C, Li F, Hall R, Garavito RM, Ferguson-Miller S","authors_abbrev":"Liu J et al.","pubmed_publication_date":"04 Apr 2023","pubmed_entrez_date":"2023-03-22","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC725.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7957086","title":"Preferential strand transfer and hybrid DNA formation at the recombination hotspot ade6-M26 of Schizosaccharomyces pombe.","citation":"EMBO J 1994 Nov 01;13(21):5212-9","abstract":"The ade6-M26 mutation of Schizosaccharomyces pombe stimulates intragenic and intergenic meiotic recombination. M26 is a single base pair change creating a specific heptanucleotide sequence that is crucial for recombination hotspot activity. This sequence is recognized by proteins that may facilitate rate-limiting steps of recombination at the ade6 locus. To start the elucidation of the intermediate DNA structures formed during M26 recombination, we have analyzed the aberrant segregation patterns of two G to C transversion mutations flanking the heptanucleotide sequence in crosses homozygous for M26. At both sites the level of post-meiotic segregation is typical for G to C transversion mutations in S. pombe in general. Quantitative treatment of the data provides strong evidence for heteroduplex DNA being the major recombination intermediate at the M26 site. We can now exclude a double-strand gap repair mechanism to account for gene conversion across the recombination hotspot. Furthermore, the vast majority (> 95%) of the heteroduplexes covering either of the G to C transversion sites are produced by transfer of the transcribed DNA strand. These results are consistent with ade6-M26 creating an initiation site for gene conversion by the introduction of a single-strand or a double-strand break in its vicinity, followed by transfer of the transcribed DNA strands for heteroduplex DNA formation.","authors":"Schär P, Kohli J","authors_abbrev":"Schär P et al.","pubmed_publication_date":"01 Nov 1994","pubmed_entrez_date":"1994-11-01","publication_year":"1994","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26566175","title":"A selective autophagy pathway takes an unconventional route.","citation":"Autophagy 2015;11(12):2381-2","abstract":"Selective autophagy transports specific cytoplasmic materials into lysosomes/vacuoles. In the case of macroautophagy the selectivity is mediated by receptors, which usually link the cargos to the machinery that sequesters them into the forming autophagosome. In our recent work, we found that fission yeast Nbr1, a homolog of the mammalian macroautophagy receptor NBR1, acts together with an unconventional autophagy-associated cargo sequestration apparatus, the endosomal sorting complexes required for transport (ESCRTs), to deliver 2 hydrolytic enzymes from the cytosol to the vacuole lumen. In this pathway, which we term the Nbr1-mediated vacuolar targeting (NVT) pathway, soluble cargos transit through the multi-vesicular body (MVB), rather than the autophagosome, on their way to the vacuole. Our findings reveal a novel mode of action of macroautophagy receptors and broaden our understanding of ESCRT-mediated autophagy.","doi":"10.1080/15548627.2015.1110669","authors":"Liu XM, Du LL","authors_abbrev":"Liu XM et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-11-14","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-11-15 01:19:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP35G2.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11056543","title":"Type II myosin regulatory light chain relieves auto-inhibition of myosin-heavy-chain function.","citation":"Nat Cell Biol 2000 Nov;2(11):855-8","abstract":"The F-actin based motor protein myosin II has a key role in cytokinesis. Here we show that the Schizosaccharomyces pombe regulatory light chain (RLC) protein Rlc1p binds to Myo2p in manner that is dependent on the IQ sequence motif (the RLC-binding site), and that Rlc1p is a component of the actomyosin ring. Rlc1p is important for cytokinesis at all growth temperatures and is essential for this process at lower temperatures. Interestingly, all deleterious phenotypes associated with the loss of Rlc1p function are suppressed by deletion of the RLC binding site on Myo2p. We conclude that the sole essential function of RLCs in fission yeast is to relieve the auto-inhibition of myosin II function, which is mediated by the RLC-binding site, on the myosin heavy chain (MHC).","authors":"Naqvi NI, Wong KC, Tang X, Balasubramanian MK","authors_abbrev":"Naqvi NI et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-11-01","publication_year":"2000","canto_session_key":"7f406346f52bc707","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-01-02 16:55:12","canto_approved_date":"2020-01-28 11:50:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-25 16:12:58","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAP8A3.08","SPAC926.03","SPAC4A8.05c","SPCC645.05c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-01-02"},{"uniquename":"PMID:27266525","title":"Nucleosome eviction in mitosis assists condensin loading and chromosome condensation.","citation":"EMBO J 2016 Jul 15;35(14):1565-81","abstract":"Condensins associate with DNA and shape mitotic chromosomes. Condensins are enriched nearby highly expressed genes during mitosis, but how this binding is achieved and what features associated with transcription attract condensins remain unclear. Here, we report that condensin accumulates at or in the immediate vicinity of nucleosome-depleted regions during fission yeast mitosis. Two transcriptional coactivators, the Gcn5 histone acetyltransferase and the RSC chromatin-remodelling complex, bind to promoters adjoining condensin-binding sites and locally evict nucleosomes to facilitate condensin binding and allow efficient mitotic chromosome condensation. The function of Gcn5 is closely linked to condensin positioning, since neither the localization of topoisomerase II nor that of the cohesin loader Mis4 is altered in gcn5 mutant cells. We propose that nucleosomes act as a barrier for the initial binding of condensin and that nucleosome-depleted regions formed at highly expressed genes by transcriptional coactivators constitute access points into chromosomes where condensin binds free genomic DNA.","doi":"10.15252/embj.201592849","authors":"Toselli-Mollereau E, Robellet X, Fauque L, Lemaire S, Schiklenk C, Klein C, Hocquet C, Legros P, N'Guyen L, Mouillard L, Chautard E, Auboeuf D, Haering CH, Bernard P","authors_abbrev":"Toselli-Mollereau E et al.","pubmed_publication_date":"15 Jul 2016","pubmed_entrez_date":"2016-06-09","publication_year":"2016","canto_session_key":"85fdd62940045b20","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-06-10 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.10c","SPAC1952.05","SPBC1A4.03c","SPCC24B10.08c","SPAC17G8.13c","SPBC146.03c","SPCC306.03c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:4314233","title":"Regulation of the biosynthesis of purine nucleotides in Schizosaccharomyces pombe. I. Properties of the phosphoribosylpyrophosphate: glutamine amidotransferase of the wild strain and of a mutant desensitized towards feedback modifiers.","citation":"Biochim Biophys Acta 1970 Mar 18;198(3):471-81","abstract":"","authors":"Nagy M","authors_abbrev":"Nagy M","pubmed_publication_date":"18 Mar 1970","pubmed_entrez_date":"1970-03-18","publication_year":"1970","canto_session_key":"04eae585f954a5e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-07-11 16:01:37","canto_approved_date":"2022-02-03 20:42:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-02 08:08:58","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4D7.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-07-11"},{"uniquename":"PMID:15632072","title":"Functional comparison of the Tup11 and Tup12 transcriptional corepressors in fission yeast.","citation":"Mol Cell Biol 2005 Jan;25(2):716-27","abstract":"Gene duplication is considered an important evolutionary mechanism. Unlike many characterized species, the fission yeast Schizosaccharomyces pombe contains two paralogous genes, tup11+ and tup12+, that encode transcriptional corepressors similar to the well-characterized budding yeast Tup1 protein. Previous reports have suggested that Tup11 and Tup12 proteins play redundant roles. Consistently, we show that the two Tup proteins can interact together when expressed at normal levels and that each can independently interact with the Ssn6 protein, as seen for Tup1 in budding yeast. However, tup11- and tup12- mutants have different phenotypes on media containing KCl and CaCl2. Consistent with the functional difference between tup11- and tup12- mutants, we identified a number of genes in genome-wide gene expression experiments that are differentially affected by mutations in the tup11+ and tup12+ genes. Many of these genes are differentially derepressed in tup11- mutants and are over-represented in genes that have previously been shown to respond to a range of different stress conditions. Genes specifically derepressed in tup12- mutants require the Ssn6 protein for their repression. As for Tup12, Ssn6 is also required for efficient adaptation to KCl- and CaCl2-mediated stress. We conclude that Tup11 and Tup12 are at least partly functionally diverged and suggest that the Tup12 and Ssn6 proteins have adopted a specific role in regulation of the stress response.","authors":"Fagerström-Billai F, Wright AP","authors_abbrev":"Fagerström-Billai F et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2005-01-06","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.14c","SPAC18B11.10","SPBC23E6.09"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:19250904","title":"Regulation of Set9-mediated H4K20 methylation by a PWWP domain protein.","citation":"Mol Cell 2009 Feb 27;33(4):428-37","abstract":"Methylation of histone H4 lysine 20 (H4K20me) is essential for recruiting checkpoint proteins 53BP1/Crb2 to DNA lesions and subsequent activation of a DNA-damage checkpoint. In fission yeast, Set9 (spKMT5) catalyzes mono-, di-, and trimethylation of H4K20. However, the mechanisms that regulate Set9 function are poorly understood. Here, we identified a PWWP domain protein Pdp1 as a Set9-associated factor. Pdp1 binds to histones and is required for Set9 chromatin localization. Yeast cells without Pdp1 were deficient in all three states of H4K20me, sensitive to genotoxic treatments, and impaired in Crb2 recruitment. The PWWP domain of Pdp1 binds to H4K20me, and mutations within the PWWP domain that abrogated this interaction in vitro reduced both the association of Set9 with chromatin and the extent of H4K20me in vivo. These results demonstrate that the PWWP domain is a new methyl-lysine recognition motif that plays important roles in epigenetic regulation.","doi":"10.1016/j.molcel.2009.02.002","authors":"Wang Y, Reddy B, Thompson J, Wang H, Noma K, Yates JR, Jia S","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"27 Feb 2009","pubmed_entrez_date":"2009-03-03","publication_year":"2009","canto_session_key":"7a38c014384c9f45","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-12-01 11:49:15","canto_approved_date":"2025-09-04 09:11:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-23 14:43:08","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":55,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_19250904_phaf.tsv"}],"genes":["SPAC1834.03c","SPCC1259.13","SPBC216.05","SPBC342.05","SPCC622.09","SPBC29A3.13","SPCC4B3.12"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2016-12-01"},{"uniquename":"PMID:22808312","title":"Mfc1 is a novel copper transporter during meiosis.","citation":"Commun Integr Biol 2012 Mar 01;5(2):118-21","abstract":"Meiosis is a specialized cell division process by which diploid germ line cells generate haploid gametes, which are required for sexual reproduction. During this process, several micronutrients are required, including copper ions. Despite important roles for copper-dependent proteins during meiosis, their mechanisms of action remain poorly understood. In a recently publication, we reported the discovery of Mfc1, the first example ever reported of a meiosis-specific copper transporter. Although Mfc1 did not exhibit any significant amino acid sequence similarities with members of the Ctr family of copper transporters, it harbored putative copper coordination motifs. Microarray data showed that mfc1(+) was the most highly induced of all meiotic genes detected under copper-limiting conditions. Analysis of Mfc1 localization during meiosis revealed that it localized at the forespore membrane during middle and late phases of the meiotic program. Interestingly, live-cell copper imaging using a copper-binding tracker revealed accumulation of copper ions into the forespore in wild-type cells. In contrast, mutant cells lacking Mfc1 displayed an intracellular distribution of copper ions that was dispersed throughout the ascospores without any marked preference for the forespore. We propose that Mfc1 is required to mobilize copper into the forespore, thereby providing copper to copper-requiring enzymes of the developing spores.","doi":"10.4161/cib.18716","authors":"Beaudoin J, Ioannoni R, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"01 Mar 2012","pubmed_entrez_date":"2012-07-19","publication_year":"2012","canto_session_key":"afb5b3fe7238c8b8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013552","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12455970","title":"A long terminal repeat retrotransposon of fission yeast has strong preferences for specific sites of insertion.","citation":"Eukaryot Cell 2002 Feb;1(1):44-55","abstract":"The successful dispersal of transposons depends on the critical balance between the fitness of the host and the ability of the transposon to insert into the host genome. One method transposons may use to avoid the disruption of coding sequences is to target integration into safe havens. We explored the interaction between the long terminal repeat retrotransposon Tf1 and the genome of the yeast Schizosaccharomyces pombe. Using techniques that were specifically designed to detect integration of Tf1 throughout the genome and to avoid bias in this detection, we generated 51 insertion events. Although 60.2% of the genome of S. pombe is coding sequence, all but one of the insertions occurred in intergenic regions. We also found that Tf1 was significantly more likely to insert into intergenic regions that included polymerase II promoters than into regions between convergent gene pairs. Interestingly, 8 of the 51 insertion sites were isolated multiple times from genetically independent cultures. This result suggests that specific sites in intergenic regions are targeted by Tf1. Perhaps the most surprising observation was that per kilobase of nonrepetitive sequence, Tf1 was significantly more likely to insert into chromosome 3 than into one of the other two chromosomes. This preference was found not to be due to differences in the distribution or composition of intergenic sequences within the three chromosomes.","authors":"Singleton TL, Levin HL","authors_abbrev":"Singleton TL et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-11-29","publication_year":"2002","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24069138","title":"Boolean network model predicts knockout mutant phenotypes of fission yeast.","citation":"PLoS One 2013;8(9):e71786","abstract":"networks of switches) are extremely simple mathematical models of biochemical signaling networks. Under certain circumstances, Boolean networks, despite their simplicity, are capable of predicting dynamical activation patterns of gene regulatory networks in living cells. For example, the temporal sequence of cell cycle activation patterns in yeasts S. pombe and S. cerevisiae are faithfully reproduced by Boolean network models. An interesting question is whether this simple model class could also predict a more complex cellular phenomenology as, for example, the cell cycle dynamics under various knockout mutants instead of the wild type dynamics, only. Here we show that a Boolean network model for the cell cycle control network of yeast S. pombe correctly predicts viability of a large number of known mutants. So far this had been left to the more detailed differential equation models of the biochemical kinetics of the yeast cell cycle network and was commonly thought to be out of reach for models as simplistic as Boolean networks. The new results support our vision that Boolean networks may complement other mathematical models in systems biology to a larger extent than expected so far, and may fill a gap where simplicity of the model and a preference for an overall dynamical blueprint of cellular regulation, instead of biochemical details, are in the focus.","doi":"10.1371/journal.pone.0071786","authors":"Davidich MI, Bornholdt S","authors_abbrev":"Davidich MI et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-09-27","publication_year":"2013","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19516326","title":"Cell cycle: Cell division brought down to size.","citation":"Nature 2009 Jun 11;459(7248):782-3","abstract":"","doi":"10.1038/459782a","authors":"Sawin KE","authors_abbrev":"Sawin KE","pubmed_publication_date":"11 Jun 2009","pubmed_entrez_date":"2009-06-12","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8143860","title":"A comparison of demethoxyviridin and wortmannin as inhibitors of phosphatidylinositol 3-kinase.","citation":"FEBS Lett 1994 Apr 04;342(2):109-14","abstract":"The mammalian Ptdlns 3-kinase is shown to be inhibited by low nanomolar concentrations of demethoxyviridin, an antifungal agent structurally related to wortmannin. The inhibitory potency of both compounds could be observed in purified Ptdlns 3-kinase whether or not the regulatory subunit (p85 alpha) was present, suggesting that the inhibitors bind to the catalytic subunit (p110) of the Ptdlns 3-kinase. These inhibitors also show similar potency against the intrinsic p85-phosphorylating activity of the p110-kinase. However, the structurally related Ptdlns 3-kinase from Saccharomyces cerevisiae (Vps34p) is not inhibited by either compound. Both inhibitors target the mammalian Ptdlns 3-kinase in vitro and in vivo, implying that these compounds should be useful in suppressing Ptdlns 3-kinase in mammalian systems. The inhibitors did not affect the mammalian Ptdlns 4-kinase, but they are able to inhibit a membrane-associated Ptdlns 4-kinase from Schizosaccharomyces pombe.","authors":"Woscholski R, Kodaki T, McKinnon M, Waterfield MD, Parker PJ","authors_abbrev":"Woscholski R et al.","pubmed_publication_date":"04 Apr 1994","pubmed_entrez_date":"1994-04-04","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24531659","title":"Centromeric histone H2B monoubiquitination promotes noncoding transcription and chromatin integrity.","citation":"Nat Struct Mol Biol 2014 Mar;21(3):236-43","abstract":"Functional centromeres are essential for proper cell division. Centromeres are established largely by epigenetic processes resulting in incorporation of the histone H3 variant CENP-A. Here, we demonstrate the direct involvement of H2B monoubiquitination, mediated by RNF20 in humans or Brl1 in Schizosaccharomyces pombe, in centromeric chromatin maintenance. Monoubiquinated H2B (H2Bub1) is needed for this maintenance, promoting noncoding transcription, centromere integrity and accurate chromosomal segregation. A transient pulse of centromeric H2Bub1 leads to RNA polymerase II-mediated transcription of the centromere's central domain, coupled to decreased H3 stability. H2Bub1-deficient cells have centromere cores that, despite their intact centromeric heterochromatin barriers, exhibit characteristics of heterochromatin, such as silencing histone modifications, reduced nucleosome turnover and reduced levels of transcription. In the H2Bub1-deficient cells, centromere functionality is hampered, thus resulting in unequal chromosome segregation. Therefore, centromeric H2Bub1 is essential for maintaining active centromeric chromatin.","doi":"10.1038/nsmb.2776","authors":"Sadeghi L, Siggens L, Svensson JP, Ekwall K","authors_abbrev":"Sadeghi L et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-02-18","publication_year":"2014","canto_session_key":"842a54cdf3dfb43f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20204527","title":"A second protein disulfide isomerase plays a protective role against nitrosative and nutritional stresses in Schizosaccharomyces pombe.","citation":"Mol Biol Rep 2010 Dec;37(8):3663-71","abstract":"In the present work, a second gene encoding protein disulfide isomerase (PDI2) was cloned and characterized from Schizosaccharomyces pombe, and its regulation was studied. The structural gene encoding PDI2 was amplified from the genomic DNA using PCR, and ligated into the E. coli-yeast shuttle vector pRS316 to generate the recombinant plasmid pYPDI2. The determined DNA sequence carries 2,578 bp and is able to encode a protein of 726 amino acid sequence with CGAC at the putative active site. The fission yeast cells harboring pYPDI2 contained 1.62- and 2.73-fold higher PDI activity than the control yeast cells in exponential and stationary phases, respectively, indicating that the cloned gene is in vivo functioning. The PDI2 mRNA levels in both vector control and pYPDI2-containing yeast cells were found to be significantly higher in the stationary phase than in the exponential phase, suggesting that expression of the PDI2 gene is under stationary control. The yeast cells harboring pYPDI2 showed enhanced survival on minimal media plates containing nitric oxide (NO)-generating sodium nitroprusside (SNP) and no nitrogen. The synthesis of β-galactosidase from the PDI2-lacZ fusion gene was markedly enhanced in the Pap1-positive KP1 cells by SNP and nitrogen starvation. However, the enhancement in the synthesis of β-galactosidase from the PDI2-lacZ fusion gene by SNP and nitrogen starvation appeared to be relatively reduced in the Pap1-negative TP108-3C cells than in the Pap1-positive KP1 cells. The PDI2 mRNA level was elevated by SNP and nitrogen starvation in the Pap1-positive cells but not in the Pap1-negative cells. In brief, the S. pombe PDI2 plays a protective role against nitrosative and nutritional stresses, and is positively regulated by NO and nitrogen starvation in a Pap1-dependent manner.","doi":"10.1007/s11033-010-0018-1","authors":"Lee EH, Hyun DH, Park EH, Lim CJ","authors_abbrev":"Lee EH et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-03-06","publication_year":"2010","canto_session_key":"830462c45bbca0d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-06-03 09:13:46","canto_approved_date":"2019-10-13 15:53:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-03 09:13:01","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.13c","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-06-03"},{"uniquename":"PMID:39340300","title":"The Swi5-Sfr1 complex regulates Dmc1- and Rad51-driven DNA strand exchange proceeding through two distinct three-stranded intermediates by different mechanisms.","citation":"Nucleic Acids Res 2024 Sep 28;","abstract":"In eukaryotes, Dmc1 and Rad51 are key proteins of homologous recombination. The Swi5-Sfr1 complex in fission yeast, a conserved auxiliary factor, stimulates DNA strand exchange driven by both Dmc1 and Rad51. Interestingly, biochemical analysis suggested that Swi5-Sfr1 regulates strand exchange activities of these recombinases differently, but the mechanisms were unclear. We previously developed a real-time system to analyze Rad51-driven DNA strand exchange and identified two topologically distinct three-stranded intermediates (complex 1 (C1) and complex 2 (C2)). Swi5-Sfr1 facilitates the C1-C2 transition and releases single-stranded DNA (ssDNA) from C2, acting as a strand exchange activator. In this study, we investigated fission yeast Dmc1-driven DNA strand exchange and the role of Swi5-Sfr1 in Dmc1 activity in real-time. Kinetic analysis revealed a three-step model for the Dmc1-driven reaction, similar to that of Rad51. Although Swi5-Sfr1 stimulated the Dmc1-driven reaction, it had a weaker impact than Rad51. Furthermore, Swi5-Sfr1 enhanced the association of Dmc1 with ssDNA by promoting filament nucleus formation, acting as a mediator, unlike its role with Rad51. This stimulation mechanism also differs from that of Ca2+ or ATP analog, AMP-PNP. Our findings suggest that Swi5-Sfr1 stimulates strand exchange activities of Dmc1 and Rad51 via different reaction steps.","doi":"10.1093/nar/gkae841","authors":"Ito K, Maki T, Kanamaru S, Takahashi M, Iwasaki H","authors_abbrev":"Ito K et al.","pubmed_publication_date":"28 Sep 2024","pubmed_entrez_date":"2024-09-28","publication_year":"2024","canto_session_key":"d5dd0fdecc7a84ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroshi Iwasaki","canto_first_approved_date":"2026-04-08 07:16:14","canto_approved_date":"2026-04-08 07:16:14","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-03-27 04:15:36","canto_added_date":"2024-09-29 23:25:05","annotation_curators":[{"name":"Hiroshi Iwasaki","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.03c","SPAC644.14c","SPBC28F2.07","SPBC409.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2026-04-08"},{"uniquename":"PMID:9559556","title":"Characterization of the Prk1 protein kinase from Schizosaccharomyces pombe.","citation":"Yeast 1998 Mar 30;14(5):485-92","abstract":"We report the isolation and characterization of a protein kinase from the fission yeast Schizosaccharomyces pombe. The proposed Prk1 protein contains 352 amino acids and has significant homology to the Ume5p kinase (also known as Srb10p, Ssn3p and Are1p) of the budding yeast Saccharomyces cerevisiae, a cyclin-dependent kinase involved in regulating the transcription of a diverse set of genes. Disruption of the prk1 gene increases flocculation but does not appear to have any other significant effect on cell behaviour. This defect can be overcome by expressing the UME5 gene, indicating that Prk1 is the fission yeast homologue of Ume5p.","authors":"Watson P, Davey J","authors_abbrev":"Watson P et al.","pubmed_publication_date":"30 Mar 1998","pubmed_entrez_date":"1998-04-29","publication_year":"1998","canto_session_key":"e43ab58908bb095","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-09-26 15:05:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-04-27 16:15:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H4.17c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-04-27"},{"uniquename":"EMBL:AU013030","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29034432","title":"YKL071W from Saccharomyces cerevisiae encodes a novel aldehyde reductase for detoxification of glycolaldehyde and furfural derived from lignocellulose.","citation":"Appl Microbiol Biotechnol 2017 Dec;101(23-24):8405-8418","abstract":"Aldehydes generated as by-products during the pretreatment of lignocellulose are the key inhibitors to Saccharomyces cerevisiae, which is considered as the most promising microorganism for industrial production of biofuel, xylitol as well as other special chemicals from lignocellulose. S. cerevisiae has the inherent ability to in situ detoxify aldehydes to corresponding alcohols by multiple aldehyde reductases. Herein, we report that an uncharacterized open reading frame YKL071W from S. cerevisiae encodes a novel \"classical\" short-chain dehydrogenase/reductase (SDR) protein with NADH-dependent enzymatic activities for reduction of furfural (FF), glycolaldehyde (GA), formaldehyde (FA), and benzaldehyde (BZA). This enzyme showed much better specific activities for reduction of GA and FF than FA and BZA, and displayed much higher Km and Kcat/Km but lower Vmax and Kcat for reduction of GA than FF. For this enzyme, the optimum pH was 5.5 and 6.0 for reduction of GA and FF, and the optimum temperature was 30 °C for reduction of GA and FF. Both pH and temperature affected stability of this enzyme in a similar trend for reduction of GA and FF. Cu 2+ , Zn 2+ , Ni 2+ , and Fe 3+  had severe inhibition effects on enzyme activities of Ykl071wp for reduction of GA and FF. Transcription of YKL071W in S. cerevisiae was significantly upregulated under GA and FF stress conditions, and its transcription is most probably regulated by transcription factor genes of YAP1, CAD1, PDR3, and STB5. This research provides guidelines to identify more uncharacterized genes with reductase activities for detoxification of aldehydes derived from lignocellulose in S. cerevisiae.","doi":"10.1007/s00253-017-8567-z","authors":"Wang H, Ouyang Y, Zhou C, Xiao D, Guo Y, Wu L, Li X, Gu Y, Xiang Q, Zhao K, Yu X, Zou L, Ma M","authors_abbrev":"Wang H et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-10-17","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC663.08c","SPCC663.09c","SPCC663.06c","SPCC24B10.20"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:8621081","title":"The Schizosaccharomyces pombe spqM gene is a new member of the Qm transcription factor family.","citation":"Gene 1996 Apr 17;170(1):153-4","abstract":"The Qm family of proteins, which are found in a wide variety of species such as budding yeast, plants and humans, are believed to play a role in gene expression. Here, we report the isolation ofaa gene, spqM, from the fission yeast Schizosaccharomyces pombe, whose deduced amino-acid sequence shared 71.6 to 61.36% identity with members of the Qm family. The high degree of conservation of the Qm members suggest that they were selectively conserved, because of an important biological role.","authors":"Masson JY, Vadnais J, Ramotar D","authors_abbrev":"Masson JY et al.","pubmed_publication_date":"17 Apr 1996","pubmed_entrez_date":"1996-04-17","publication_year":"1996","canto_session_key":"ff85bc2e33c6e82b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-01 12:53:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-01 12:53:38","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-08-01"},{"uniquename":"PMID:38900638","title":"The condensation of HP1α/Swi6 imparts nuclear stiffness.","citation":"Cell Rep 2024 Jun 19;43(7):114373","abstract":"Biomolecular condensates have emerged as major drivers of cellular organization. It remains largely unexplored, however, whether these condensates can impart mechanical function(s) to the cell. The heterochromatin protein HP1α (Swi6 in Schizosaccharomyces pombe) crosslinks histone H3K9 methylated nucleosomes and has been proposed to undergo condensation to drive the liquid-like clustering of heterochromatin domains. Here, we leverage the genetically tractable S. pombe model and a separation-of-function allele to elucidate a mechanical function imparted by Swi6 condensation. Using single-molecule imaging, force spectroscopy, and high-resolution live-cell imaging, we show that Swi6 is critical for nuclear resistance to external force. Strikingly, it is the condensed yet dynamic pool of Swi6, rather than the chromatin-bound molecules, that is essential to imparting mechanical stiffness. Our findings suggest that Swi6 condensates embedded in the chromatin meshwork establish the emergent mechanical behavior of the nucleus as a whole, revealing that biomolecular condensation can influence organelle and cell mechanics.","doi":"10.1016/j.celrep.2024.114373","authors":"Williams JF, Surovtsev IV, Schreiner SM, Chen Z, Raiymbek G, Nguyen H, Hu Y, Biteen JS, Mochrie SGJ, Ragunathan K, King MC","authors_abbrev":"Williams JF et al.","pubmed_publication_date":"19 Jun 2024","pubmed_entrez_date":"2024-06-20","publication_year":"2024","canto_session_key":"16f5c219058b95cb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-06-20 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18782833","title":"The human mitochondrial ribosome recycling factor is essential for cell viability.","citation":"Nucleic Acids Res 2008 Oct;36(18):5787-99","abstract":"The molecular mechanism of human mitochondrial translation has yet to be fully described. We are particularly interested in understanding the process of translational termination and ribosome recycling in the mitochondrion. Several candidates have been implicated, for which subcellular localization and characterization have not been reported. Here, we show that the putative mitochondrial recycling factor, mtRRF, is indeed a mitochondrial protein. Expression of human mtRRF in fission yeast devoid of endogenous mitochondrial recycling factor suppresses the respiratory phenotype. Further, human mtRRF is able to associate with Escherichia coli ribosomes in vitro and can associate with mitoribosomes in vivo. Depletion of mtRRF in human cell lines is lethal, initially causing profound mitochondrial dysmorphism, aggregation of mitoribosomes, elevated mitochondrial superoxide production and eventual loss of OXPHOS complexes. Finally, mtRRF was shown to co-immunoprecipitate a large number of mitoribosomal proteins attached to other mitochondrial proteins, including putative members of the mitochondrial nucleoid.","doi":"10.1093/nar/gkn576","authors":"Rorbach J, Richter R, Wessels HJ, Wydro M, Pekalski M, Farhoud M, Kühl I, Gaisne M, Bonnefoy N, Smeitink JA, Lightowlers RN, Chrzanowska-Lightowlers ZM","authors_abbrev":"Rorbach J et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-09-11","publication_year":"2008","canto_session_key":"51ca213800ebbff3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-11-22 12:53:50","canto_approved_date":"2021-10-07 08:09:30","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-10-06 10:14:20","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["HGNC:7234","SPMIT.11","SPBC1709.09"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2017-11-22"},{"uniquename":"PMID:28341698","title":" Schizosaccharomyces pombe  MutSα and MutLα Maintain Stability of Tetra-Nucleotide Repeats and Msh3 of Hepta-Nucleotide Repeats.","citation":"G3 (Bethesda) 2017 May 05;7(5):1463-1473","abstract":"Defective mismatch repair (MMR) in humans is associated with colon cancer and instability of microsatellites, that is, DNA sequences with one or several nucleotides repeated. Key factors of eukaryotic MMR are the heterodimers MutSα (Msh2-Msh6), which recognizes base-base mismatches and unpaired nucleotides in DNA, and MutLα (Mlh1-Pms1), which facilitates downstream steps. In addition, MutSβ (Msh2-Msh3) recognizes DNA loops of various sizes, although our previous data and the data presented here suggest that Msh3 of  Schizosaccharomyces pombe  does not play a role in MMR. To test microsatellite stability in  S. pombe  and hence DNA loop repair, we have inserted tetra-, penta-, and hepta-nucleotide repeats in the  ade6  gene and determined their Ade +  reversion rates and spectra in wild type and various mutants. Our data indicate that loops with four unpaired nucleotides in the nascent and the template strand are the upper limit of MutSα- and MutLα-mediated MMR in  S. pombe  Stability of hepta-nucleotide repeats requires Msh3 and Exo1 in MMR-independent processes as well as the DNA repair proteins Rad50, Rad51, and Rad2 FEN1  Most strikingly, mutation rates in the double mutants  msh3 exo1  and  msh3 rad51  were decreased when compared to respective single mutants, indicating that Msh3 prevents error prone processes carried out by Exo1 and Rad51. We conclude that Msh3 has no obvious function in MMR in  S. pombe , but contributes to DNA repeat stability in MMR-independent processes.","doi":"10.1534/g3.117.040816","authors":"Villahermosa D, Christensen O, Knapp K, Fleck O","authors_abbrev":"Villahermosa D et al.","pubmed_publication_date":"05 May 2017","pubmed_entrez_date":"2017-03-26","publication_year":"2017","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-29 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPBC29A10.05","SPAC8F11.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:15573098","title":"Intra-nuclear microtubules and a mitotic spindle orientation checkpoint.","citation":"Nat Cell Biol 2004 Dec;6(12):1245-6","abstract":"Cells of the fission yeast Schizosaccharomyces pombe have a checkpoint mechanism that reportedly monitors the orientation of the mitotic spindle. Astral microtubules in pre-anaphase spindles are thought to contact the contractile actin ring at the plasma membrane in order to rotate the spindle and to sense spindle orientation. Here, we show that these microtubules are actually inside the nuclear envelope.","authors":"Zimmerman S, Daga RR, Chang F","authors_abbrev":"Zimmerman S et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-12-02","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32892625","title":"Molecular Mechanism for the Actin-Binding Domain of α-Actinin Ain1 Elucidated by Molecular Dynamics Simulations and Mutagenesis Experiments.","citation":"J Phys Chem B 2020 Oct 01;124(39):8495-8503","abstract":"In the fission yeast  Schizosaccharomyces pombe , α-actinin Ain1 bundles F-actin into the contractile ring (CR) in the middle of the cell. Previous studies have proposed that a conformational change of the actin-binding domain (ABD) of Ain1 enhances the actin-binding activity. However, the molecular mechanism of the conformational change remains to be unveiled at an atomic resolution due to the difficulties of experimental techniques to observe them. In the present study, we performed a set of microsecond-order molecular dynamics (MD) simulations for ABD of Ain1. Our MD simulations for a pathogenic point mutation (R216E) in ABD did not result in large domain motions as previously expected. However, local motions of the loop regions were detected. Besides the three conventional actin-binding sites, we found characteristic electrostatic interactions with the N-terminal of actin. The mutagenesis experiment in fission yeast showed that collapses of the electrostatic interactions at the binding site abolished the proper localization of Ain1 to the CR. Furthermore, the MD simulation of F-actin with the Ain1 ABD R216E indicated that the stronger affinity is caused by a direct interaction of the point mutation. Our findings might be applicable to other highly conserved ABP family proteins to explain their binding affinities.","doi":"10.1021/acs.jpcb.0c04623","authors":"Morita R, Nakano K, Shigeta Y, Harada R","authors_abbrev":"Morita R et al.","pubmed_publication_date":"01 Oct 2020","pubmed_entrez_date":"2020-09-07","publication_year":"2020","canto_session_key":"3232c9219ab0f2d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rikuri Morita","canto_first_approved_date":"2020-12-01 14:51:22","canto_approved_date":"2023-01-26 10:37:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-01 07:39:30","canto_added_date":"2020-09-09 00:15:13","annotation_curators":[{"name":"Rikuri Morita","community_curator":true,"annotation_count":2,"orcid":"0000-0002-0465-5528","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-12-01"},{"uniquename":"PMID:11739788","title":"G2/M arrest caused by actin disruption is a manifestation of the cell size checkpoint in fission yeast.","citation":"Mol Biol Cell 2001 Dec;12(12):3892-903","abstract":"In budding yeast, actin disruption prevents nuclear division. This has been explained as activation of a morphogenesis checkpoint monitoring the integrity of the actin cytoskeleton. The checkpoint operates through inhibitory tyrosine phosphorylation of Cdc28, the budding yeast Cdc2 homolog. Wild-type Schizosaccharomyces pombe cells also arrest before mitosis after actin depolymerization. Oversized cells, however, enter mitosis uninhibited. We carried out a careful analysis of the kinetics of mitotic initiation after actin disruption in undersized and oversized cells. We show that an inability to reach the mitotic size threshold explains the arrest in smaller cells. Among the regulators that control the level of the inhibitory Cdc2-Tyr15 phosphorylation, the Cdc25 protein tyrosine phosphatase is required to link cell size monitoring to mitotic control. This represents a novel function of the Cdc25 phosphatase. Furthermore, we demonstrate that this cell size-monitoring system fulfills the formal criteria of a cell cycle checkpoint.","authors":"Rupes I, Webb BA, Mak A, Young PG","authors_abbrev":"Rupes I et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-12-12","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9378413","title":"Potassium transport in Schizosaccharomyces pombe.","citation":"Folia Microbiol (Praha) 1997;42(3):227-9","abstract":"","authors":"Heyer M, Lichtenberg-Fraté H, Reid JD, Höfer M","authors_abbrev":"Heyer M et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20541496","title":"Cytokinesis: ER keeps Mid1 in the middle.","citation":"Curr Biol 2010 Jun 08;20(11):R484-6","abstract":"How cells mark the region of the plasma membrane where the cleavage furrow will assemble is a classic question in cell biology. A new study has shown an unexpected role for cortically associated endoplasmic reticulum in positioning the site of cell division.","doi":"10.1016/j.cub.2010.04.046","authors":"McCollum D","authors_abbrev":"McCollum D","pubmed_publication_date":"08 Jun 2010","pubmed_entrez_date":"2010-06-15","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16040599","title":"Contrasting effects of Elg1-RFC and Ctf18-RFC inactivation in the absence of fully functional RFC in fission yeast.","citation":"Nucleic Acids Res 2005;33(13):4078-89","abstract":"Proliferating cell nuclear antigen loading onto DNA by replication factor C (RFC) is a key step in eukaryotic DNA replication and repair processes. In this study, the C-terminal domain (CTD) of the large subunit of fission yeast RFC is shown to be essential for its function in vivo. Cells carrying a temperature-sensitive mutation in the CTD, rfc1-44, arrest with incompletely replicated chromosomes, are sensitive to DNA damaging agents, are synthetically lethal with other DNA replication mutants, and can be suppressed by mutations in rfc5. To assess the contribution of the RFC-like complexes Elg1-RFC and Ctf18-RFC to the viability of rfc1-44, genes encoding the large subunits of these complexes have been deleted and overexpressed. Inactivation of Ctf18-RFC by the deletion of ctf18+, dcc1+ or ctf8+ is lethal in an rfc1-44 background showing that full Ctf18-RFC function is required in the absence of fully functional RFC. In contrast, rfc1-44 elg1Delta cells are viable and overproduction of Elg1 in rfc1-44 is lethal, suggesting that Elg1-RFC plays a negative role when RFC function is inhibited. Consistent with this, the deletion of elg1+ is shown to restore viability to rfc1-44 ctf18Delta cells.","authors":"Kim J, Robertson K, Mylonas KJ, Gray FC, Charapitsa I, MacNeill SA","authors_abbrev":"Kim J et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-07-26","publication_year":"2005","canto_session_key":"220d35c90a1310b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-03 17:15:38","canto_approved_date":"2023-03-16 13:43:18","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2015-12-03 17:15:29","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":66,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC947.11c","SPBC83.14c","SPAC27E2.10c","SPAC31A2.15c","SPAC27E2.05","SPBC23E6.07c","SPBC1734.02c","SPBC902.02c","SPBC16D10.04c","SPAC23D3.02","SPAC19D5.11c","SPAC1687.03c","SPBC336.04"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2015-12-03"},{"uniquename":"PMID:9245826","title":"Protein kinase Sck1 is involved in trehalase activation by glucose and nitrogen source in the fission yeast Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 1997 Jul;143 ( Pt 7):2457-2463","abstract":"Trehalase activity is markedly enhanced upon addition of glucose and a nitrogen source to cells of the fission yeast Schizosaccharomyces pombe. This increase corresponds to a post-translational activation of the enzyme, which is controlled by cAMP-dependent and cAMP-independent pathways. Recent work has shown that overexpression of SCK1 in Schiz. pombe is able to suppress mutations that result in reduced Pka1 (cAMP-dependent protein kinase A activity, suggesting that Sck1 (suppressor of loss of cAMP-dependent protein kinase) might be a functional analogue of Pka1 in the fission yeast. Here, an analysis of the possible role of Sck1 in the activation of trehalase triggered by glucose and a nitrogen source is reported in cells that were deficient in either Pka1, Sck1 or both protein kinases. The results showed that, except in repressed cells, Sck1 probably mediates a cAMP-independent activation of trehalase following the signal(s) triggered by glucose and the nitrogen source. The absence of functional Sck1 in depressed cells renders trehalase insensitive to activation by glucose and the nitrogen source even in the presence of Pka1, indicating that the Sck1-dependent, cAMP-independent pathway is the main signalling pathway controlling trehalase activation under derepression conditions. It is proposed that, during the activation of trehalase induced by glucose or a nitrogen source, the cAMP-Pka1 activation pathway previously characterized is to some extent parallel to this newly described one which includes Sck1 as phosphorylating enzyme. Neither of these two pathways, however, plays a key role in the heat-induced increase in trehalase activity.","doi":"10.1099/00221287-143-7-2457","authors":"Soto T, Fernandez J, Cansado J, Vicente-Soler J, Gacto M","authors_abbrev":"Soto T et al.","pubmed_publication_date":"Jul 1997","pubmed_entrez_date":"1997-07-01","publication_year":"1997","canto_session_key":"b647f6d193522336","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-04-30 08:57:23","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-04-30 08:57:14","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B9.02c","SPBC106.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-04-30"},{"uniquename":"PMID:9819416","title":"Multiple orientation-dependent, synergistically interacting, similar domains in the ribosomal DNA replication origin of the fission yeast, Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1998 Dec;18(12):7294-303","abstract":"Previous investigations have shown that the fission yeast, Schizosaccharomyces pombe, has DNA replication origins (500 to 1500 bp) that are larger than those in the budding yeast, Saccharomyces cerevisiae (100 to 150 bp). Deletion and linker substitution analyses of two fission yeast origins revealed that they contain multiple important regions with AT-rich asymmetric (abundant A residues in one strand and T residues in the complementary strand) sequence motifs. In this work we present the characterization of a third fission yeast replication origin, ars3001, which is relatively small ( approximately 570 bp) and responsible for replication of ribosomal DNA. Like previously studied fission yeast origins, ars3001 contains multiple important regions. The three most important of these regions resemble each other in several ways: each region is essential for origin function and is at least partially orientation dependent, each region contains similar clusters of A+T-rich asymmetric sequences, and the regions can partially substitute for each other. These observations suggest that ars3001 function requires synergistic interactions between domains binding similar proteins. It is likely that this requirement extends to other fission yeast origins, explaining why such origins are larger than those of budding yeast.","authors":"Kim SM, Huberman JA","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1998-11-20","publication_year":"1998","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2822024","title":"Denaturation and renaturation of the monomeric phosphoglycerate mutase from Schizosaccharomyces pombe.","citation":"Biochem J 1987 Jul 15;245(2):525-30","abstract":"The denaturation by guanidinium chloride of the monomeric phosphoglycerate mutase from Schizosaccharomyces pombe was studied. The loss in activity broadly parallels the changes in protein structure detected by fluorescence and c.d. Renaturation can be brought about by dilution of the denaturing agent. These processes were compared with those in the enzymes from baker's yeast and rabbit muscle, which are tetrameric and dimeric respectively. The effects of the cofactor 2,3-bisphosphoglycerate on the structure and stability of the S. pombe enzyme were also investigated.","authors":"Johnson CM, Price NC","authors_abbrev":"Johnson CM et al.","pubmed_publication_date":"15 Jul 1987","pubmed_entrez_date":"1987-07-15","publication_year":"1987","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23966136","title":"A microfluidic synchronizer for fission yeast cells.","citation":"Lab Chip 2013 Oct 21;13(20):4071-7","abstract":"Among all the cell cycle synchronization technologies, the baby machine may be considered as the most artifact-free method. A baby machine incubates \"mother cells\" under normal conditions and collects their \"babies\", producing cell cultures that are similar not only in cell cycle phase but also in age. Unlike many other synchronization methods, no cell-cycle-blocking agent or metabolic stress is introduced in this method. Several macroscale and microfluidic baby machines have been developed for producing synchronized cell colonies. However, for rod-shaped cells like fission yeast (Schizosaccharomyces pombe), it is still a challenge to immobilize only the mother cells in a microfluidic device. Here we presented a new baby machine suitable for fission yeast. The device is fixed one end of the cell and releases the free-end daughter cell every time the cell finishes cytokinesis. A variety of structures for cell immobilization were attempted to find the optimal design. For the convenience of collection and further assay, we integrated into our baby machine chip a cell screener, which exploited the deformation of polymer material to switch between opening and closing states. Synchronous populations of fission yeast cells were produced with this device, its working detail was analyzed and performance was evaluated. The device provides a new on-chip tool for cell biology studies.","doi":"10.1039/c3lc50639h","authors":"Tian Y, Luo C, Ouyang Q","authors_abbrev":"Tian Y et al.","pubmed_publication_date":"21 Oct 2013","pubmed_entrez_date":"2013-08-23","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8163505","title":"Cytoplasmic forms of fission yeast casein kinase-1 associate primarily with the particulate fraction of the cell.","citation":"J Biol Chem 1994 Apr 22;269(16):12014-23","abstract":"Two novel casein kinase-1 homologs, cki1+ and cki2+, have been isolated from Schizosaccharomyces pombe and characterized. Both genes reside on chromosome II and encode approximately 50-kDa proteins that are related structurally and enzymatically to the YCK gene products of budding yeast. Subcellular fractionation experiments demonstrate that Cki1 and Cki2 are both cytoplasmic enzymes that do not overlap in subcellular distribution and that probably play distinct roles within the cell. Although gene disruption experiments show that neither cki1+ nor cki2+ is essential for cell viability, overexpression of cki2 leads to a severe growth defect and aberrant morphology. Cells become round or pear shaped and separate poorly following septation. These results suggest that of the four members of the casein kinase-1 family recognized in fission yeast, one member, Cki2, may contribute to the regulation of cell morphology.","authors":"Wang PC, Vancura A, Desai A, Carmel G, Kuret J","authors_abbrev":"Wang PC et al.","pubmed_publication_date":"22 Apr 1994","pubmed_entrez_date":"1994-04-22","publication_year":"1994","canto_session_key":"1b9692f34c4ac74a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 13:48:21","canto_approved_date":"2023-12-23 15:19:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-29 16:28:02","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.06c","SPBP35G2.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-17"},{"uniquename":"PMID:9819418","title":"The mating-type proteins of fission yeast induce meiosis by directly activating mei3 transcription.","citation":"Mol Cell Biol 1998 Dec;18(12):7317-26","abstract":"Cell type control of meiotic gene regulation in the budding yeast Saccharomyces cerevisiae is mediated by a cascade of transcriptional repressors, a1-alpha2 and Rme1. Here, we investigate the analogous regulatory pathway in the fission yeast Schizosaccharomyces pombe by analyzing the promoter of mei3, the single gene whose expression is sufficient to trigger meiosis. The mei3 promoter does not appear to contain a negative regulatory element that represses transcription in haploid cells. Instead, correct regulation of mei3 transcription depends on a complex promoter that contains at least five positive elements upstream of the TATA sequence. These elements synergistically activate mei3 transcription, thereby constituting an on-off switch for the meiosis pathway. Element C is a large region containing multiple sequences that resemble binding sites for Mc, an HMG domain protein encoded by the mating-type locus. The function of element C is extremely sensitive to spacing changes but not to linker-scanning mutations, suggesting the possibility that Mc functions as an architectural transcription factor. Altered-specificity experiments indicate that element D interacts with Pm, a homeodomain protein encoded by the mating-type locus. This indicates that Pm functions as a direct activator of the meiosis pathway, whereas the homologous mating-type protein in S. cerevisiae (alpha2) functions as a repressor. Thus, despite the strong similarities between the mating-type loci of S. cerevisiae and S. pombe, the regulatory logic that governs the tight control of the key meiosis-inducing genes in these organisms is completely different.","authors":"Van Heeckeren WJ, Dorris DR, Struhl K","authors_abbrev":"Van Heeckeren WJ et al.","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1998-11-20","publication_year":"1998","canto_session_key":"fc936f5c09b314ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 10:05:41","canto_approved_date":"2024-03-27 06:39:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-06 16:50:12","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMTR.02","SPBC119.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-10"},{"uniquename":"PMID:7550745","title":"Electroporation of Schizosaccharomyces pombe.","citation":"Methods Mol Biol 1995;47:273-8","abstract":"","authors":"Hood MT, Stachow CS","authors_abbrev":"Hood MT et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30925937","title":"Unexpected insertion of carrier DNA sequences into the fission yeast genome during CRISPR-Cas9 mediated gene deletion.","citation":"BMC Res Notes 2019 Mar 29;12(1):191","abstract":"The fission yeast Schizosaccharomyces pombe is predicted to encode ~ 200 proteins of < 100 amino acids, including a number of previously uncharacterised proteins that are found conserved in related Schizosaccharomyces species only. To begin an investigation of the function of four of these so-called microproteins (designated Smp1-Smp4), CRISPR-Cas9 genome editing technology was used to delete the corresponding genes in haploid fission yeast cells.\nNone of the four microprotein-encoding genes was essential for viability, meiosis or sporulation, and the deletion cells were no more sensitive to a range of cell stressors than wild-type, leaving the function of the proteins unresolved. During CRISPR-Cas9 editing however, a number of strains were isolated in which additional sequences were inserted into the target loci at the Cas9 cut site. Sequencing of the inserts revealed these to be derived from the chum salmon Oncorhynchus keta, the source of the carrier DNA used in the S. pombe transformation.","doi":"10.1186/s13104-019-4228-x","authors":"Longmuir S, Akhtar N, MacNeill SA","authors_abbrev":"Longmuir S et al.","pubmed_publication_date":"29 Mar 2019","pubmed_entrez_date":"2019-03-31","publication_year":"2019","canto_session_key":"d833bfae23694c5b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Stuart MacNeill","canto_first_approved_date":"2019-04-16 09:42:56","canto_approved_date":"2019-04-18 14:59:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-04-15 09:35:21","canto_added_date":"2019-04-01 00:15:04","annotation_curators":[{"name":"Stuart MacNeill","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":60,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30B4.09","SPCPB16A4.07","SPBC13G1.16","SPAC25B8.20"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-04-16"},{"uniquename":"PMID:16469495","title":"Motor proteins at the microtubule plus-end.","citation":"Trends Cell Biol 2006 Mar;16(3):135-43","abstract":"The plus-end of the microtubule has a central role in the interactions that occur between the microtubule and actin cytoskeletons. The recent identification of a family of proteins that congregate at the plus-end is enabling an increased mechanistic understanding of how this cross talk is accomplished. These proteins, termed plus-end tracking proteins because they appear to associate with the plus-end as it grows, have already been shown to regulate microtubule dynamics and to facilitate the formation of connections between the plus-end and the actin-rich cortex. Several motor proteins, including an actin-based motor, microtubule-based motors that move towards either end of the microtubule and microtubule motors that depolymerize microtubule ends, can now be added to the list of plus-end tracking proteins. Here, we discuss how the presence of these motors at the plus-end seems to drive several fundamental cellular processes involving force generation at the interface between microtubule ends and the cortex, vesicle translocation following search and capture, microtubule disassembly and the delivery of signals to the cortex that govern actin assembly and cell polarity.","authors":"Wu X, Xiang X, Hammer JA","authors_abbrev":"Wu X et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-02-14","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31892813","title":"Crosstalk between autophagy and apoptosis induced by camphor in Schizosaccharomyces pombe.","citation":"Turk J Biol 2019;43(6):382-390","abstract":"Camphor is widely used in pharmacy, the food industry, and cosmetics. In this study, we evaluate inhibitory and cytotoxic effects of camphor in the fission yeast ( Schizosaccharomyces pombe ), which presents a unicellular model in mechanistic toxicology and cell biology. Low-dose camphor exposure (0.4 mg/mL) activated autophagy, which was shown by GFP-Atg8 dots and transcriptional upregulation of Atg6 (Beclin-1 ortholog). Autophagy was also confirmed by using autophagy-deficient cells, which showed reduction in GFP-Atg8 dot formation. However, high-dose camphor exposure (0.8 mg/mL) caused dramatic cell death ratios, demonstrated by spot and colony-forming assays, even in autophagy-deficient cells. To unravel the underlying mechanism, this time, apoptosis-deficient cells were exposed to low- and high-dose camphor. Apoptosis was also confirmed by acridine orange/ethidium bromide staining. Among yeast apoptosis mediators, Aif1 was found to mediate camphor-induced cell death. In conclusion, differential regulation of autophagy and apoptosis, and switches between them, were found to be dose-dependent. The potential effects of camphor on autophagy and apoptotic cell death and underlying mechanisms were clarified in basic unicellular eukaryotic model,  S. pombe .","doi":"10.3906/biy-1908-11","authors":"Ağuş HH, Yilmaz S, Şengöz CO","authors_abbrev":"Ağuş HH et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2020-01-02","publication_year":"2019","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26F1.14c","SPBP8B7.24c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:25584793","title":"Global resource distribution: allocation of actin building blocks by profilin.","citation":"Dev Cell 2015 Jan 12;32(1):5-6","abstract":"How cells regulate the distribution of a limited pool of actin between two competing structures has long been a mystery. Complementary studies from Suarez et al. (2015) and Rotty et al. (2015) now show that profilin controls the partitioning of actin monomers between competing actin networks assembled by Arp2/3 complex and formins or Ena/VASP.","doi":"10.1016/j.devcel.2014.12.022","authors":"Henty-Ridilla JL, Goode BL","authors_abbrev":"Henty-Ridilla JL et al.","pubmed_publication_date":"12 Jan 2015","pubmed_entrez_date":"2015-01-14","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-03-12 01:15:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1327149","title":"Functional and structural conservation of Schizosaccharomyces pombe dTMP kinase gene.","citation":"Biochim Biophys Acta 1992 Sep 24;1132(2):222-4","abstract":"We describe the isolation and identification of the Schizosaccharomyces pombe dTMP kinase gene by the complementation of a Saccharomyces cerevisiae cell cycle mutant cell, cdc8. The isolated cDNA contains an open reading frame which can encode a protein with the molecular weight of 24,151. The deduced protein sequence is highly conserved among known dTMP kinase sequences from different organisms. The isolated gene should facilitate our study of its enzymatic activity, as well as nucleotide metabolism and cell cycle regulation in this organism.","authors":"Abaigar LT, Yeh YI, Jong AY","authors_abbrev":"Abaigar LT et al.","pubmed_publication_date":"24 Sep 1992","pubmed_entrez_date":"1992-09-24","publication_year":"1992","canto_session_key":"05bd6f77383c498e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 11:55:37","canto_session_submitted_date":"2012-03-03 11:54:54","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC70.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-03-03"},{"uniquename":"PMID:23712692","title":"Adaptation to tert-butyl hydroperoxide at a plasma membrane level in the fission yeast Schizosaccharomyces pombe parental strain and its t-BuOOH-resistant mutant.","citation":"J Basic Microbiol 2014 Mar;54(3):215-25","abstract":"The one-gene mutant hyd1-190 of the fission yeast Schizosaccharomyces pombe displayed four-fold resistance to tert-butyl hydroperoxide (t-BuOOH) in comparison with its parental strain hyd(+). The cells of hyd1-190 exhibited a quantitative alteration in the sterol content and hence in the fatty acid composition of the plasma membrane, reflected in a two-fold amphotericin B sensitivity, increased rigidity of the plasma membrane, revealed by an elevated (Δ7.9 °C) phase-transition temperature, measured by means of electron paramagnetic resonance spectroscopy, and a significantly decreased uptake of glycerol. Treatment of the strains with a subinhibitory concentration (0.2 mM) of t-BuOOH induced adaptation via modification of the sterol and fatty acid compositions, resulting in increased (Δ3.95 °C) and decreased (Δ6.83 °C) phase-transition temperatures of the hyd(+) and hyd1-190 strains, respectively, in order to defend the cells against the consequences of t-BuOOH-induced external oxidative stress. However, in contrast with hyd(+), hyd1-190 lacks the ability to adapt to t-BuOOH at a cell level.","doi":"10.1002/jobm.201200580","authors":"Kálmán N, Gazdag Z, Čertík M, Belágyi J, Selim SA, Pócsi I, Pesti M","authors_abbrev":"Kálmán N et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2013-05-29","publication_year":"2014","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1272249","title":"Effect of protein synthesis inhibition on recovery of UV- and gamma-irridated Schizosaccharomyces pombe from repair inhibition by caffeine.","citation":"Mol Gen Genet 1976 Apr 23;145(1):1-5","abstract":"The progress of repair in Schizosaccharomyces pombe may be followed during post-irradiation incubation by measuring, after various intervals, the ability of UV- or gamma-irradiated cells to avoid enhanced lethality when exposed to the repair inhibitor caffeine (Gentner and Werner, 1975). This technique has now been used to investigate the effect of inhibition of protein synthesis on repair of UV- and gamma-irradiation-induced damage in this organism. When protein synthesis was inhibited with cycloheximide in UV-irradiated wild-type cells, only a small amount of recovery from caffeine inhibition occurred; this indicated that post-irradiation protein synthesis was required for repair, and in particular for the recombinational repair pathway, which is a major mechanism for repair of UV damage in this organism. In gamma-irradiated wild-type cells, inhibition of post-irradiation protein synthesis reduced the rate of recovery from repair inhibition by caffeine, but full recovery from caffeine-sensitive damage did occur at longer incubation times. We attribute the reduction in rate to the effect of protein synthesis inhibition on the recombinational repair pathway, because this pathway is known to be involved in the repair of both gamma-ray and UV damage. The recovery that took place at the slower rate must reflect a caffeine-sensitive pathway which is involved only in repair of gamma-ray damage and which does not require post-irradiation protein synthesis for activity.","authors":"Gentner NE, Werner MM","authors_abbrev":"Gentner NE et al.","pubmed_publication_date":"23 Apr 1976","pubmed_entrez_date":"1976-04-23","publication_year":"1976","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37725645","title":"Distinct regions of the kinesin-5 C-terminal tail are essential for mitotic spindle midzone localization and sliding force.","citation":"Proc Natl Acad Sci U S A 2023 Sep 26;120(39):e2306480120","abstract":"Kinesin-5 motor proteins play essential roles during mitosis in most organisms. Their tetrameric structure and plus-end-directed motility allow them to bind to and move along antiparallel microtubules, thereby pushing spindle poles apart to assemble a bipolar spindle. Recent work has shown that the C-terminal tail is particularly important to kinesin-5 function: The tail affects motor domain structure, ATP hydrolysis, motility, clustering, and sliding force measured for purified motors, as well as motility, clustering, and spindle assembly in cells. Because previous work has focused on presence or absence of the entire tail, the functionally important regions of the tail remain to be identified. We have therefore characterized a series of kinesin-5/Cut7 tail truncation alleles in fission yeast. Partial truncation causes mitotic defects and temperature-sensitive growth, while further truncation that removes the conserved BimC motif is lethal. We compared the sliding force generated by  cut7  mutants using a kinesin-14 mutant background in which some microtubules detach from the spindle poles and are pushed into the nuclear envelope. These Cut7-driven protrusions decreased as more of the tail was truncated, and the most severe truncations produced no observable protrusions. Our observations suggest that the C-terminal tail of Cut7p contributes to both sliding force and midzone localization. In the context of sequential tail truncation, the BimC motif and adjacent C-terminal amino acids are particularly important for sliding force. In addition, moderate tail truncation increases midzone localization, but further truncation of residues N-terminal to the BimC motif decreases midzone localization.","doi":"10.1073/pnas.2306480120","authors":"Gergely ZR, Jones MH, Zhou B, Cash C, McIntosh JR, Betterton MD","authors_abbrev":"Gergely ZR et al.","pubmed_publication_date":"26 Sep 2023","pubmed_entrez_date":"2023-09-19","publication_year":"2023","canto_session_key":"7f1dc29239d93d50","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-09-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21208191","title":"The fission yeast Schizosaccharomyces pombe has two distinct tRNase Z(L)s encoded by two different genes and differentially targeted to the nucleus and mitochondria.","citation":"Biochem J 2011 Apr 01;435(1):103-11","abstract":"tRNase Z is the endonuclease that is involved in tRNA 3'-end maturation by removal of the 3'-trailer sequences from tRNA precursors. Most eukaryotes examined to date, including the budding yeast Saccharomyces cerevisiae and humans, have a single long form of tRNase Z (tRNase ZL). In contrast, the fission yeast Schizosaccharomyces pombe contains two candidate tRNase ZLs encoded by the essential genes sptrz1+ and sptrz2+. In the present study, we have expressed recombinant SpTrz1p and SpTrz2p in S. pombe. Both recombinant proteins possess precursor tRNA 3'-endonucleolytic activity in vitro. SpTrz1p localizes to the nucleus and has a simian virus 40 NLS (nuclear localization signal)-like NLS at its N-terminus, which contains four consecutive arginine and lysine residues between residues 208 and 211 that are critical for the NLS function. In contrast, SpTrz2p is a mitochondrial protein with an N-terminal MTS (mitochondrial-targeting signal). High-level overexpression of sptrz1+ has no detectable phenotypes. In contrast, strong overexpression of sptrz2+ is lethal in wild-type cells and results in morphological abnormalities, including swollen and round cells, demonstrating that the correct expression level of sptrz2+ is critical. The present study provides evidence for partitioning of tRNase Z function between two different proteins in S. pombe, although we cannot rule out specialized functions for each protein.","doi":"10.1042/BJ20101619","authors":"Gan X, Yang J, Li J, Yu H, Dai H, Liu J, Huang Y","authors_abbrev":"Gan X et al.","pubmed_publication_date":"01 Apr 2011","pubmed_entrez_date":"2011-01-07","publication_year":"2011","canto_session_key":"44703db6ac552c71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-03-21 15:18:01","canto_approved_date":"2024-04-04 10:38:10","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-05-06 20:18:42","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.10","SPBC3D6.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-21"},{"uniquename":"PMID:34347367","title":"piRNA- and siRNA-mediated transcriptional repression in Drosophila, mice, and yeast: new insights and biodiversity.","citation":"EMBO Rep 2021 Oct 05;22(10):e53062","abstract":"The PIWI-interacting RNA (piRNA) pathway acts as a self-defense mechanism against transposons to maintain germline genome integrity. Failures in the piRNA pathway cause DNA damage in the germline genome, disturbing inheritance of \"correct\" genetic information by the next generations and leading to infertility. piRNAs execute transposon repression in two ways: degrading their RNA transcripts and compacting the genomic loci via heterochromatinization. The former event is mechanistically similar to siRNA-mediated RNA cleavage that occurs in the cytoplasm and has been investigated in many species including nematodes, fruit flies, and mammals. The latter event seems to be mechanistically parallel to siRNA-centered kinetochore assembly and subsequent chromosome segregation, which has so far been studied particularly in fission yeast. Despite the interspecies conservations, the overall schemes of the nuclear events show clear biodiversity across species. In this review, we summarize the recent progress regarding piRNA-mediated transcriptional silencing in Drosophila and discuss the biodiversity by comparing it with the equivalent piRNA-mediated system in mice and the siRNA-mediated system in fission yeast.","doi":"10.15252/embr.202153062","authors":"Onishi R, Yamanaka S, Siomi MC","authors_abbrev":"Onishi R et al.","pubmed_publication_date":"05 Oct 2021","pubmed_entrez_date":"2021-08-04","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-08-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15189449","title":"Sorting nexin homologues are targets of phosphatidylinositol 3-phosphate in sporulation of Schizosaccharomyces pombe.","citation":"Genes Cells 2004 Jun;9(6):561-74","abstract":"Schizosaccharomyces pombe defective in phosphatidylinositol (PtdIns) 3-kinase shows various defects in forespore membrane formation, including onset, growth orientation, and closure. Downstream factors of PtdIns 3-kinase in this system were explored. Among various phox homology (PX) domain-containing proteins, Vps5p and Vps17p, homologues of sorting nexins, were found to be required for efficient sporulation. Cells defective in these proteins showed a disordered growth orientation of the forespore membrane, as is the case with Deltapik3 cells. Vps5p and Vps17p with mutations in the PX domains failed to suppress the defects of their relevant disruptants. Vps5p and Vps17p migrated toward the the forespore membrane in a pik3+-dependent manner, suggesting that these proteins may interact with PtdIns(3)P. Electron-microscopic analysis revealed that the forespore membrane fails to engulf the nucleus in some of these cells, accumulating vesicle-like bodies similar to those seen in Deltaspo3 cells. These results suggest that Vps5p and Vps17p are the targets of PtdIns(3)P in vesicle transport required for onset of the forespore membrane formation.","authors":"Koga T, Onishi M, Nakamura Y, Hirata A, Nakamura T, Shimoda C, Iwaki T, Takegawa K, Fukui Y","authors_abbrev":"Koga T et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-06-11","publication_year":"2004","canto_session_key":"a8add27e026359e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-10 21:01:36","canto_approved_date":"2026-02-06 17:15:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-09 12:09:27","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":57,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.12","SPBC887.06c","SPAC3A11.06","SPCC16A11.08","SPCC16A11.04","SPAC5D6.07c","SPAC607.10","SPCPJ732.01","SPCC825.03c","SPCC594.06c","SPAPJ696.01c","SPAC19G12.10c","SPBC1711.11","SPAC458.05","SPAC15E1.06","SPCC777.13","SPCC1450.12","SPCC1682.15","SPBC14F5.11c"],"gene_count":19,"ltp_gene_count":17,"approved_date":"2017-01-10"},{"uniquename":"PMID:21423721","title":"Chiasmata promote monopolar attachment of sister chromatids and their co-segregation toward the proper pole during meiosis I.","citation":"PLoS Genet 2011 Mar;7(3):e1001329","abstract":"The chiasma is a structure that forms between a pair of homologous chromosomes by crossover recombination and physically links the homologous chromosomes during meiosis. Chiasmata are essential for the attachment of the homologous chromosomes to opposite spindle poles (bipolar attachment) and their subsequent segregation to the opposite poles during meiosis I. However, the overall function of chiasmata during meiosis is not fully understood. Here, we show that chiasmata also play a crucial role in the attachment of sister chromatids to the same spindle pole and in their co-segregation during meiosis I in fission yeast. Analysis of cells lacking chiasmata and the cohesin protector Sgo1 showed that loss of chiasmata causes frequent bipolar attachment of sister chromatids during anaphase. Furthermore, high time-resolution analysis of centromere dynamics in various types of chiasmate and achiasmate cells, including those lacking the DNA replication checkpoint factor Mrc1 or the meiotic centromere protein Moa1, showed the following three outcomes: (i) during the pre-anaphase stage, the bipolar attachment of sister chromatids occurs irrespective of chiasma formation; (ii) the chiasma contributes to the elimination of the pre-anaphase bipolar attachment; and (iii) when the bipolar attachment remains during anaphase, the chiasmata generate a bias toward the proper pole during poleward chromosome pulling that results in appropriate chromosome segregation. Based on these results, we propose that chiasmata play a pivotal role in the selection of proper attachments and provide a backup mechanism that promotes correct chromosome segregation when improper attachments remain during anaphase I.","doi":"10.1371/journal.pgen.1001329","authors":"Hirose Y, Suzuki R, Ohba T, Hinohara Y, Matsuhara H, Yoshida M, Itabashi Y, Murakami H, Yamamoto A","authors_abbrev":"Hirose Y et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-03-23","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPBP35G2.03c","SPBC32F12.02","SPAC17A5.11"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:22876361","title":"Endoplasmic reticulum involvement in yeast cell death.","citation":"Front Oncol 2012;2:87","abstract":"Yeast cells undergo programed cell death (PCD) with characteristic markers associated with apoptosis in mammalian cells including chromatin breakage, nuclear fragmentation, reactive oxygen species generation, and metacaspase activation. Though significant research has focused on mitochondrial involvement in this phenomenon, more recent work with both Saccharomyces cerevisiae and Schizosaccharomyces pombe has also implicated the endoplasmic reticulum (ER) in yeast PCD. This minireview provides an overview of ER stress-associated cell death (ER-SAD) in yeast. It begins with a description of ER structure and function in yeast before moving to a discussion of ER-SAD in both mammalian and yeast cells. Three examples of yeast cell death associated with the ER will be highlighted here including inositol starvation, lipid toxicity, and the inhibition of N-glycosylation. It closes by suggesting ways to further examine the involvement of the ER in yeast cell death.","doi":"10.3389/fonc.2012.00087","authors":"Austriaco N","authors_abbrev":"Austriaco N","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-10","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC167.01","SPCC576.04"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:34114564","title":"CDK control pathways integrate cell size and ploidy information to control cell division.","citation":"Elife 2021 Jun 11;10","abstract":"Maintenance of cell size homeostasis is a property that is conserved throughout eukaryotes. Cell size homeostasis is brought about by the co-ordination of cell division with cell growth and requires restriction of smaller cells from undergoing mitosis and cell division, whilst allowing larger cells to do so. Cyclin-CDK is the fundamental driver of mitosis and therefore ultimately ensures size homeostasis. Here we dissect determinants of CDK activity in vivo to investigate how cell size information is processed by the cell cycle network in fission yeast. We develop a high-throughput single-cell assay system of CDK activity in vivo and show that inhibitory tyrosine phosphorylation of CDK encodes cell size information, with the phosphatase PP2A aiding to set a size threshold for division. CDK inhibitory phosphorylation works synergistically with PP2A to prevent mitosis in smaller cells. Finally, we find that diploid cells of equivalent size to haploid cells exhibit lower CDK activity in response to equal cyclin-CDK enzyme concentrations, suggesting that CDK activity is reduced by increased DNA levels. Therefore, scaling of cyclin-CDK levels with cell size, CDK inhibitory phosphorylation, PP2A, and DNA-dependent inhibition of CDK activity, all inform the cell cycle network of cell size, thus contributing to cell size homeostasis.","doi":"10.7554/eLife.64592","authors":"Patterson JO, Basu S, Rees P, Nurse P","authors_abbrev":"Patterson JO et al.","pubmed_publication_date":"11 Jun 2021","pubmed_entrez_date":"2021-06-11","publication_year":"2021","canto_session_key":"a08eb18aaeb41cfe","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-13 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7672363","title":"The cytotoxicity of anthramycin to mutants of Schizosaccharomyces pombe deficient in DNA damage responses.","citation":"Biochem Soc Trans 1995 May;23(2):331S","abstract":"","authors":"Hafiz F, Thurston DE, Carr AM, Jones RW","authors_abbrev":"Hafiz F et al.","pubmed_publication_date":"May 1995","pubmed_entrez_date":"1995-05-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18265318","title":"Overview of Schizosaccharomyces pombe.","citation":"Curr Protoc Mol Biol 2003 Nov;Chapter 13:Unit 13.14","abstract":"The fission yeast S. pombe provides an attractive alternative system to budding yeast S. cerevisiae for studies of fundamental cell biology. Fission yeast is a particularly powerful model for studies of cell cycle, chromosome dynamics, and polarity. Other areas of study are also expanding. Conceptually similar genetic tools are available in both systems, and both organisms have completely sequenced genomes.","doi":"10.1002/0471142727.mb1314s64","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2008-02-12","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10637292","title":"Myosin-II tails confer unique functions in Schizosaccharomyces pombe: characterization of a novel myosin-II tail.","citation":"Mol Biol Cell 2000 Jan;11(1):79-91","abstract":"Schizosaccharomyces pombe has two myosin-IIs, Myo2p and Myp2p, which both concentrate in the cleavage furrow during cytokinesis. We studied the phenotype of mutant myosin-II strains to examine whether these myosins have overlapping functions in the cell. myo2(+) is essential. myp2(+) cannot rescue loss of myo2(+) even at elevated levels of expression. myp2(+) is required under specific nutritional conditions; thus myo2(+) cannot rescue under these conditions. Studies with chimeras show that the tails rather than the structurally similar heads determine the gene-specific functions of myp2(+) and myo2(+). The Myo2p tail is a rod-shaped coiled-coil dimer that aggregates in low salt like other myosin-II tails. The Myp2p tail is monomeric in high salt and is insoluble in low salt. Biophysical properties of the full-length Myp2p tail and smaller subdomains indicate that two predicted coiled-coil regions fold back on themselves to form a rod-shaped antiparallel coiled coil. This suggests that Myp2p is the first type II myosin with only one head. The C-terminal two-thirds of Myp2p tail are essential for function in vivo and may interact with components of the salt response pathway.","authors":"Bezanilla M, Pollard TD","authors_abbrev":"Bezanilla M et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-19","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAC4A8.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:21107719","title":"Fission yeast ucp3 gene encodes a putative Arf6 GTPase-activating protein.","citation":"Mol Biol Rep 2011 Aug;38(6):3875-82","abstract":"In fission yeast Schizosaccharomyces pombe, the directions of cell growth change from a monopolar manner to a bipolar manner, which is known as 'New End Take Off' (NETO). We previously found that Arf6, a member (class III) of the ADP-ribosylation factor GTPase (Arf) family, is necessary for NETO in fission yeast. Here we report the characterization of a S. pombe gene, ucp3, encoding a putative Arf GTPase-activating protein (GAP) for Arf6. The Ucp3 contains Arf GAP domain, and has a high similarity to Gts1, which was identified as a GAP for Arf3 (class III Arf) in Saccharomyces cerevisiae. Overexpression of ucp3 inhibited growth from new end possibly by disturbing the GDP/GTP-cycling of Arf6. Gene disruption of ucp3 revealed that Ucp3 is essential for cell viability. Ucp3 uniformly localizes to the cell periphery. And its localization is not dependent on microtubules, actin cytoskeletons, Arf6 and Syt22 (guanine nucleotide exchange factor for Arf6). We hypothesize that Ucp3 functions as a GAP for Arf6. Moreover, Ucp3 might have another function important for cell viability.","doi":"10.1007/s11033-010-0503-6","authors":"Fujita A, Misumi Y","authors_abbrev":"Fujita A et al.","pubmed_publication_date":"Aug 2011","pubmed_entrez_date":"2010-11-26","publication_year":"2011","canto_session_key":"9c50d59be8aa45eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-07 17:51:32","canto_approved_date":"2022-10-03 21:22:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-27 16:13:13","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21D10.05c","SPAC11E3.11c","SPBC1539.08"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-09-07"},{"uniquename":"PMID:31428061","title":"Novel Cell Wall Antifungals Reveal a Special Synergistic Activity in  pbr1  Mutants Resistant to the Glucan Synthesis Antifungals Papulacandins and Echinocandins.","citation":"Front Microbiol 2019;10:1692","abstract":"A series of 4 - (arylmethylene)-3-isochromanones have been prepared with base-catalyzed Knoevenagel condensation starting from 3-isochromanone and aromatic aldehydes. The outcome of the reaction- the isomeric composition of the products depends on the aromatic aldehyde applied. These reactions afforded mostly the more stable  E -diastereoisomer, but some condensations resulted in the Z-diastereoisomer or mixture of the stereoisomers ( 1 - 16 ). The products showed antifungal effect against some pathogenic fungi. We wanted to extend this study and to synthesize a new generation of 4 - (arylmethylene)-3-isochromanones. These condensations led mostly to  E -diastereoisomers ( 17 - 30 ). The structure verifications were performed by FT IR,  1 H and 13 C NMR methods. Both the  1 - 16  and the novel  17 - 30  compounds have been screened against the three yeast models, fission yeast  Schizosaccharomyces pombe  (wild-type, and  pbr1-6  and  pbr1-8  mutants resistant to specific cell wall synthesis inhibitors), budding yeast  Saccharomyces cerevisiae  (wild-type and  pbr1-1 ) and pathogenic yeast  Candida albicans  (wild-type, ATCC 26555, 90028 and SC5314). Osmotic protection with sorbitol attenuated the  in vivo  inhibition in living cells suggesting a cell wall-specific antifungal effect. Moreover, the  S. pombe  wild-type and mutant strains were tested for their resistant or sensitive  in vitro  β(1,3)-glucan synthase (GS) activity. We found both  in vivo  in living cells and  in vitro  in the enzymatic GS assay a synergistic effect of higher sensitivity of the  pbr1  mutants resistant to the specific GS inhibitors papulacandins and echinocandins. These results may provide new insights into new strategies of combined antifungal therapy of GS inhibitors directed against spontaneous mutants resistant to echinocandins.","doi":"10.3389/fmicb.2019.01692","authors":"Berzaghi R, Agócs A, Curto MA, Gulyás-Fekete G, Kocsis B, Ribas JC, Lóránd T","authors_abbrev":"Berzaghi R et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-08-21","publication_year":"2019","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2019-08-22 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8854878","title":"Cell cycle control of S phase: a comparison of two yeasts.","citation":"Chromosoma 1996 Oct;105(4):197-203","abstract":"The mechanisms responsible for correct timing of DNA synthesis within the cell cycle and for limiting replication to one round per cell cycle are basically similar in the two model yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe, despite many differences in detail. In both cases, the timing of initiation and the prevention of additional rounds are controlled by the activity levels of B-type cyclins. These similarities are likely to extend to other eukaryotic organisms.","authors":"Huberman JA","authors_abbrev":"Huberman JA","pubmed_publication_date":"Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20847589","title":"Isolation of a fission yeast mutant cell affected in MAP kinase signaling and sterol biosynthesis.","citation":"Kobe J Med Sci 2009 Jun 05;55(2):E30-5","abstract":"We have previously demonstrated that calcineurin and the Pmk1 MAP kinase pathway play an antagonistic role in Cl-homeostasis. Using this relationship, we screened for mutations that show vic (viable in the presence of immunosuppressant and chloride ion) phenotype and isolated a vic6 mutant cell. The vic6 mutant cells also showed sensitivity to high temperature. Using this phenotype, we isolated hmg1+ gene, encoding a HMG-CoA reductase. Consistently, the vic6 mutant cells exhibited hypersensitivity to miconazole, an inhibitor of ergosterol biosynthesis and showed aberrant intracellular localization of filipin, suggesting that the mutant cells are affected in the sterol biosynthesis. In addition, overexpression of the hmg1+ gene complemented the phenotype of vic1-1/cpp1-v1 mutant cells, an allele of the gene encoding a farnesyltransferase, whereas overexpression of the cpp1+ gene exacerbated the temperature-sensitive phenotype of the vic6 mutant cells.","authors":"Imagawa K, Fang Y, Sugiura R, Zhou X, Ma Y, Kuno T","authors_abbrev":"Imagawa K et al.","pubmed_publication_date":"05 Jun 2009","pubmed_entrez_date":"2010-09-18","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC162.09c","SPAC17G6.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:X52732","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2205842","title":"A gene from S. pombe with homology to E. coli RNAse III blocks conjugation and sporulation when overexpressed in wild type cells.","citation":"Nucleic Acids Res 1990 Sep 11;18(17):5304","abstract":"","authors":"Xu HP, Riggs M, Rodgers L, Wigler M","authors_abbrev":"Xu HP et al.","pubmed_publication_date":"11 Sep 1990","pubmed_entrez_date":"1990-09-11","publication_year":"1990","canto_session_key":"1fc9c6d25b1eb4ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-05-06 09:47:00","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-06 09:46:53","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-06"},{"uniquename":"PMID:28801462","title":"Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.","citation":"J Biol Chem 2017 Sep 29;292(39):16014-16023","abstract":"Ribosomal translation factors are fundamental for protein synthesis and highly conserved in all kingdoms of life. The essential eukaryotic elongation factor 1A (eEF1A) delivers aminoacyl tRNAs to the A-site of the translating 80S ribosome. Several studies have revealed that eEF1A is posttranslationally modified. Using MS analysis, site-directed mutagenesis, and X-ray structural data analysis of  Saccharomyces cerevisiae  eEF1A, we identified a posttranslational modification in which the α amino group of mono-l-glutamine is covalently linked to the side chain of glutamate 45 in eEF1A. The MS analysis suggested that all eEF1A molecules are modified by this glutaminylation and that this posttranslational modification occurs at all stages of yeast growth. The mutational studies revealed that this glutaminylation is not essential for the normal functions of eEF1A in  S. cerevisiae  However, eEF1A glutaminylation slightly reduced growth under antibiotic-induced translational stress conditions. Moreover, we identified the same posttranslational modification in eEF1A from  Schizosaccharomyces pombe  but not in various other eukaryotic organisms tested despite strict conservation of the Glu 45  residue among these organisms. We therefore conclude that eEF1A glutaminylation is a yeast-specific posttranslational modification that appears to influence protein translation.","doi":"10.1074/jbc.M117.801035","authors":"Jank T, Belyi Y, Wirth C, Rospert S, Hu Z, Dengjel J, Tzivelekidis T, Andersen GR, Hunte C, Schlosser A, Aktories K","authors_abbrev":"Jank T et al.","pubmed_publication_date":"29 Sep 2017","pubmed_entrez_date":"2017-08-13","publication_year":"2017","canto_session_key":"db6e166f0f947f58","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-05-15 20:23:54","canto_approved_date":"2020-05-15 20:23:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-05-15 12:38:03","canto_added_date":"2017-08-14 00:15:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC839.15c","SPCC794.09c","SPAC23A1.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-05-15"},{"uniquename":"PMID:13390941","title":"[Research on anti-inositols; action of isomytilitol on Schizosaccharomyces pombe (Lindner) liquefaciens strain (Osterwalder) Dekker].","citation":"Schweiz Z Pathol Bakteriol 1956;19(5):647-54","abstract":"","authors":"POSTERNAK T, SCHOPFER WH","authors_abbrev":"POSTERNAK T et al.","pubmed_publication_date":"1956","pubmed_entrez_date":"1956-01-01","publication_year":"1956","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33668093","title":"Direct Regulation of DNA Repair by E2F and RB in Mammals and Plants: Core Function or Convergent Evolution?","citation":"Cancers (Basel) 2021 Feb 24;13(5)","abstract":"Members of the E2F transcription factor family regulate the expression of genes important for DNA replication and mitotic cell division in most eukaryotes. Homologs of the retinoblastoma (RB) tumor suppressor inhibit the activity of E2F factors, thus controlling cell cycle progression. Organisms such as budding and fission yeast have lost genes encoding E2F and RB, but have gained genes encoding other proteins that take on E2F and RB cell cycle-related functions. In addition to regulating cell proliferation, E2F and RB homologs have non-canonical functions outside the mitotic cell cycle in a variety of eukaryotes. For example, in both mammals and plants, E2F and RB homologs localize to DNA double-strand breaks (DSBs) and directly promote repair by homologous recombination (HR). Here, we discuss the parallels between mammalian E2F1 and RB and their  Arabidopsis  homologs, E2FA and RB-related (RBR), with respect to their recruitment to sites of DNA damage and how they help recruit repair factors important for DNA end resection. We also explore the question of whether this role in DNA repair is a conserved ancient function of the E2F and RB homologs in the last eukaryotic common ancestor or whether this function evolved independently in mammals and plants.","doi":"10.3390/cancers13050934","authors":"Manickavinayaham S, Dennehey BK, Johnson DG","authors_abbrev":"Manickavinayaham S et al.","pubmed_publication_date":"24 Feb 2021","pubmed_entrez_date":"2021-03-06","publication_year":"2021","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-03-08 01:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15340008","title":"Requirement for Schizosaccharomyces pombe Top3 in the maintenance of chromosome integrity.","citation":"J Cell Sci 2004 Sep 15;117(Pt 20):4769-78","abstract":"In Schizosaccharomyces pombe, topoisomerase III is encoded by a single gene, top3(+), which is essential for cell viability and proper chromosome segregation. Deletion of rqh1(+), which encodes the sole RecQ family helicase in S. pombe, suppresses the lethality caused by loss of top3. Here, we provide evidence suggesting that the lethality in top3 mutants is due to accumulation of aberrant DNA structures that arise during S phase, as judged by pulsed-field gel electrophoresis. Using a top3 shut-off strain, we show here that depletion of Top3 activates the DNA damage checkpoint associated with phosphorylation of the checkpoint kinase Chk1. Despite activation of this checkpoint, top3 cells exit the arrest but fail to undergo faithful chromosome segregation. However, these mitotic defects are secondary to chromosomal abnormalities that lead to the lethality, because advance into mitosis did not adversely affect cell survival. Furthermore, top3 function is required for maintenance of nucleolar structure, possibly due to its ability to prevent recombination at the rDNA loci. Our data are consistent with the notion that Top3 has a key function in homologous recombinational repair during S phase that is essential for ensuring subsequent fidelity of chromosome segregation.","authors":"Win TZ, Goodwin A, Hickson ID, Norbury CJ, Wang SW","authors_abbrev":"Win TZ et al.","pubmed_publication_date":"15 Sep 2004","pubmed_entrez_date":"2004-09-02","publication_year":"2004","canto_session_key":"443d8e38e12610f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-15 17:12:15","canto_approved_date":"2024-03-18 13:22:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-18 11:32:35","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":18,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPAC9E9.08","SPCC1259.13","SPBC16G5.12c","SPBC216.05","SPAC14C4.13","SPCC18B5.11c","SPAC2G11.12"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2024-03-15"},{"uniquename":"PMID:16361268","title":"Dynamic regulation of replication independent deposition of histone H3 in fission yeast.","citation":"Nucleic Acids Res 2005;33(22):7102-10","abstract":"Recently, a histone H3 variant in Drosophila and humans, the H3.3 protein, was shown to replace canonical H3 in active chromatin in a replication-independent (RI) manner. In the fission yeast Schizosaccharomyces pombe, there exists a single form of H3, which is equivalent to H3.3 and is thought to participate in both replication-independent (RI) and replication-coupled (RC) nucleosome assembly. In this study, we show that RI deposition of H3 at heterochromatic regions is consistently lower than that at a gene-free euchromatic region, and deletion of the conserved heterochromatin-specific proteins Swi6 or Clr4 markedly increases RI deposition at heterochromatic regions such as the silent mating-type loci or centromeres. These results clearly show that RI deposition of H3 occurs preferentially in euchromatic regions. We also observed that RI deposition of H3 could be increased at the thi3(+) gene when transcription is induced, indicating transcription further facilitates RI deposition of H3. Taken together, these observations demonstrate that selective deposition of histone H3.3 at transcriptionally active chromatin by the RI assembly pathway is conserved in fission yeast and, thus, our data support an essential role of histone H3 replacement in maintaining active chromatin among diverse eukaryotic organisms ranging from fission yeast to humans.","authors":"Choi ES, Shin JA, Kim HS, Jang YK","authors_abbrev":"Choi ES et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-12-20","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21340036","title":"Application of GFAT as a novel selection marker to mediate gene expression.","citation":"PLoS One 2011 Feb 14;6(2):e17082","abstract":"The enzyme glutamine: fructose-6-phosphate aminotransferase (GFAT), also known as glucosamine synthase (GlmS), catalyzes the formation of glucosamine-6-phosphate from fructose-6-phosphate and is the first and rate-limiting enzyme of the hexosamine biosynthetic pathway. For the first time, the GFAT gene was proven to possess a function as an effective selection marker for genetically modified (GM) microorganisms. This was shown by construction and analysis of two GFAT deficient strains, E. coli ΔglmS and S. pombe Δgfa1, and the ability of the GFAT encoding gene to mediate plasmid selection. The gfa1 gene of the fission yeast Schizosaccharomyces pombe was deleted by KanMX6-mediated gene disruption and the Cre-loxP marker removal system, and the glmS gene of Escherichia coli was deleted by using λ-Red mediated recombinase system. Both E. coli ΔglmS and S. pombe Δgfa1 could not grow normally in the media without addition of glucosamine. However, the deficiency was complemented by transforming the plasmids that expressed GFAT genes. The xylanase encoding gene, xynA2 from Thermomyces lanuginosus was successfully expressed and secreted by using GFAT as selection marker in S. pombe. Optimal glucosamine concentration for E. coli ΔglmS and S. pombe Δgfa1 growth was determined respectively. These findings provide an effective technique for the construction of GM bacteria without an antibiotic resistant marker, and the construction of GM yeasts to be applied to complex media.","doi":"10.1371/journal.pone.0017082","authors":"Wu G, Sun Y, Qu W, Huang Y, Lu L, Li L, Shao W","authors_abbrev":"Wu G et al.","pubmed_publication_date":"14 Feb 2011","pubmed_entrez_date":"2011-02-23","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8082199","title":"Meiosis-dependent mRNA splicing of the fission yeast Schizosaccharomyces pombe mes1+ gene.","citation":"Curr Genet 1994 Jun;25(6):497-503","abstract":"The mes1+ gene of the fission yeast Schizosaccharomyces pombe is essential for the second meiotic division. We have cloned a 1.1-kb HindIII fragment containing mes1+ by complementation from an S. pombe genomic library. Sequencing of the genomic and cDNA fragments indicates the existence of one small intron of 75 nucleotides, although both the 5'(G/GTTAGT) and 3'(CAG/T) intron-exon junctions deviate from the consensus sequences proposed for S. pombe. The putative translation product of the mature mes1+ mRNA is a 11-kDa protein of 101 amino acids which has no significant homology to any previously-reported proteins. Disruption of mes1 has no effect on cell growth but causes an arrest of meiosis before the second meiotic division. Northern-blot analysis revealed that mes1+ was preferentially transcribed under conditions of nitrogen starvation. When a h90 homothallic strain was shifted to a nitrogen-deficient medium, a pre-mRNA accumulated and then was gradually processed to generate a mature mRNA. This splicing did not occur in either a heterothallic haploid strain or in a homothallic mei2 mutant strain which was defective in the initiation of meiosis. Expression of the first exon alone was not able to suppress the mes1 null allele. These results indicate that mes1+ is required for the completion of meiosis, that splicing is required for the function of the mes1+ gene, and that this splicing requires the function of the mei2+ product.","authors":"Kishida M, Nagai T, Nakaseko Y, Shimoda C","authors_abbrev":"Kishida M et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_session_key":"fea9083a122cbdb2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-08 10:22:19","canto_approved_date":"2022-08-29 16:44:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-08 10:22:12","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5D6.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-08"},{"uniquename":"PMID:32317395","title":"Translesion synthesis polymerases contribute to meiotic chromosome segregation and cohesin dynamics in  S  chizosaccharomyces  pombe .","citation":"J Cell Sci 2020 May 22;133(10)","abstract":"Translesion synthesis polymerases (TLSPs) are non-essential error-prone enzymes that ensure cell survival by facilitating DNA replication in the presence of DNA damage. In addition to their role in bypassing lesions, TLSPs have been implicated in meiotic double-strand break repair in several systems. Here, we examine the joint contribution of four TLSPs to meiotic progression in the fission yeast  Schizosaccharomyces pombe.  We observed a dramatic loss of spore viability in fission yeast lacking all four TLSPs, which is accompanied by disruptions in chromosome segregation during meiosis I and II. Rec8 cohesin dynamics are altered in the absence of the TLSPs. These data suggest that the TLSPs contribute to multiple aspects of meiotic chromosome dynamics.","doi":"10.1242/jcs.238709","authors":"Mastro TL, Tripathi VP, Forsburg SL","authors_abbrev":"Mastro TL et al.","pubmed_publication_date":"22 May 2020","pubmed_entrez_date":"2020-04-23","publication_year":"2020","canto_session_key":"0de1ba3c4ca5c174","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-04-24 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU007356","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31778539","title":"Nuclear magnetic resonance investigation of water transport through the plasma membrane of various yeast species.","citation":"FEMS Microbiol Lett 2019 Sep 01;366(18)","abstract":"A specific technique of nuclear magnetic resonance (NMR) spectroscopy, filter-exchange spectroscopy (FEXSY), was employed to investigate water transport through the plasma membrane in intact yeast cells. This technique allows water transport to be monitored directly, thus avoiding the necessity to subject the cells to any rapid change in the external conditions, e.g. osmotic shock. We established a sample preparation protocol, a data analysis procedure and verified the applicability of FEXSY experiments. We recorded the exchange rates in the temperature range 10-40°C for Saccharomyces cerevisiae. The resulting activation energy of 29 kJ mol-1 supports the hypothesis that water exchange is facilitated by water channels-aquaporins. Furthermore, we measured for the first time water exchange rates in three other phylogenetically unrelated yeast species (Schizosaccharomyces pombe, Candida albicans and Zygosaccharomyces rouxii) and observed remarkably different water exchange rates between these species. Findings of our work contribute to a better understanding of as fundamental a cell process as the control of water transport through the plasma membrane.","doi":"10.1093/femsle/fnz220","authors":"Šoltésová M, Elicharová H, Srb P, Růžička M, Janisova L, Sychrová H, Lang J","authors_abbrev":"Šoltésová M et al.","pubmed_publication_date":"01 Sep 2019","pubmed_entrez_date":"2019-11-29","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-11-30 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20362451","title":"Electrical control of cell polarization in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Biol 2010 Apr 27;20(8):710-6","abstract":"Electric signals surround tissues and cells and have been proposed to participate in directing cell polarity in processes such as development, wound healing, and host invasion [1, 2]. The application of exogenous electric fields (EFs) can direct cell polarization in cell types ranging from bacteria and fungi to neurons and neutrophils [3-7]. The mechanisms by which EFs modulate cell polarity, however, remain poorly understood. Here we introduce the fission yeast Schizosaccharomyces pombe as a model organism to elucidate the mechanisms underlying this process. In these rod-shaped cells, an exogenous EF reorients cell growth in a direction orthogonal to the field, producing cells with a bent morphology. A candidate genetic screen identifies conserved factors involved in this process: an integral membrane proton ATPase pma1p that regulates intracellular pH, the small GTPase cdc42p, and the formin for3p that assembles actin cables. Interestingly, mutants in these genes still respond to the EF but orient in a different direction, toward the anode. In addition, EFs also cause electrophoretic movement of cell wall synthase complex proteins toward the anode. These data suggest molecular models for how the EF reorients cell polarization by modulating intracellular pH and steering cell polarity factors in multiple directions.","doi":"10.1016/j.cub.2010.02.047","authors":"Minc N, Chang F","authors_abbrev":"Minc N et al.","pubmed_publication_date":"27 Apr 2010","pubmed_entrez_date":"2010-04-06","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC895.05","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:4716872","title":"The effect of radiation sensitivity and cell stage on liquid holding response in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1973 May 28;122(4):331-8","abstract":"","authors":"Shahin MM, Nasim A","authors_abbrev":"Shahin MM et al.","pubmed_publication_date":"28 May 1973","pubmed_entrez_date":"1973-05-28","publication_year":"1973","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16224022","title":"Counting cytokinesis proteins globally and locally in fission yeast.","citation":"Science 2005 Oct 14;310(5746):310-4","abstract":"We used fluorescence microscopy to measure global and local concentrations of 28 cytoskeletal and signaling proteins fused to yellow fluorescent protein (YFP) in the fission yeast Schizosaccharomyces pombe. Native promoters controlled the expression of these functional YFP fusion proteins. Fluorescence measured by microscopy or flow cytometry was directly proportional to protein concentration measured by quantitative immunoblotting. Global cytoplasmic concentrations ranged from 0.04 (formin Cdc12p) to 63 micromolar (actin). Proteins concentrated up to 100 times in contractile rings and 7500 times in spindle pole bodies at certain times in the cell cycle. This approach can be used to measure the global and local concentrations of any fusion protein.","authors":"Wu JQ, Pollard TD","authors_abbrev":"Wu JQ et al.","pubmed_publication_date":"14 Oct 2005","pubmed_entrez_date":"2005-10-15","publication_year":"2005","canto_session_key":"5e8a0f2e010cd3fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-11-26 14:16:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-23 22:30:43","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"file_curator_name":"Samuel Marguerat","file_curator_role":"community","annotation_file_curators":[{"name":"Samuel Marguerat","community_curator":true,"annotation_count":27,"orcid":"0000-0002-2402-3165","file_type":"quantitative_gene_expression","file_name":"PMID_16224022_Wu_protein_quantitative_expression.txt"}],"genes":["SPAC4A8.05c","SPAPYUG7.03c","SPBC12D12.04c","SPAC4F8.13c","SPCC645.05c","SPCC645.07","SPBC12D12.01","SPBC21.06c","SPBC1778.06c","SPBC1778.08c","SPAC15A10.08","SPCC613.04c","SPAC4F10.11","SPAC9G1.11c","SPAP8A3.08","SPAC1F5.04c","SPAC23C11.16","SPBC14C8.06","SPCC645.06c","SPAC926.03","SPBC1709.01","SPCC4B3.15","SPAC17G8.04c","SPAC11H11.06","SPAC631.01c","SPBC32H8.12c","SPAC630.03"],"gene_count":27,"ltp_gene_count":0,"approved_date":"2016-11-23"},{"uniquename":"PMID:18088324","title":"Dynamin-dependent biogenesis, cell cycle regulation and mitochondrial association of peroxisomes in fission yeast.","citation":"Traffic 2008 Mar;9(3):353-65","abstract":"Peroxisomes were visualized for the first time in living fission yeast cells. In small, newly divided cells, the number of peroxisomes was low but increased in parallel with the increase in cell length/volume that accompanies cell cycle progression. In cells grown in oleic acid, both the size and the number of peroxisomes increased. The peroxisomal inventory of cells lacking the dynamin-related proteins Dnm1 or Vps1 was similar to that in wild type. By contrast, cells of the double mutant dnm1Delta vps1Delta contained either no peroxisomes at all or a small number of morphologically aberrant organelles. Peroxisomes exhibited either local Brownian movement or longer-range linear displacements, which continued in the absence of either microtubules or actin filaments. On the contrary, directed peroxisome motility appeared to occur in association with mitochondria and may be an indirect function of intrinsic mitochondrial dynamics. We conclude that peroxisomes are present in fission yeast and that Dnm1 and Vps1 act redundantly in peroxisome biogenesis, which is under cell cycle control. Peroxisome movement is independent of the cytoskeleton but is coupled to mitochondrial dynamics.","authors":"Jourdain I, Sontam D, Johnson C, Dillies C, Hyams JS","authors_abbrev":"Jourdain I et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2007-12-20","publication_year":"2008","canto_session_key":"2deeaba54114ac3e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-09 09:35:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-16 07:50:37","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC767.01c","SPBC13G1.03c","SPBC725.07","SPBC12C2.08"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-07-16"},{"uniquename":"PMID:9786087","title":"The myosin ATPase inhibitor 2,3-butanedione-2-monoxime (BDM) inhibits tip growth and cytokinesis in the fission yeast, Schizosaccharomyces pombe.","citation":"Cell Motil Cytoskeleton 1998;41(2):117-25","abstract":"The growth of fission yeast cultures was reversibly inhibited by exposure to the myosin-ATPase inhibitor 2,3-butanedione-2-monoxime (BDM). Wild-type cells treated with 20 mM BDM for approximately two generation times were smaller than untreated controls and had a septation index approximately twice that seen in the absence of the inhibitor. The organization of actin at the cell poles was somewhat disorganized in the presence of BDM; however, cells formed a cytokinetic actin ring. When nitrogen-starved stationary-phase cells were reinoculated into fresh medium in the presence of BDM, the time taken to repolarize the actin cytoskeleton and to resume the characteristic vegetative cell shape before initiation of the first cell division were both substantially delayed. BDM significantly inhibited the increase in cell length of cdc25.22 cells arrested for cell cycle progress by incubation at the restrictive temperature and substantially delayed the initiation of both mitosis and cytokinesis in arrested cdc25.22 cells after release of the temperature block. These results suggest that tip growth and cytokinesis--processes in fission yeast that involve the actin cytoskeleton--also require myosin activity.","authors":"May KM, Wheatley SP, Amin V, Hyams JS","authors_abbrev":"May KM et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-10-24","publication_year":"1998","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10726658","title":"The influence of antisense gene location on target gene suppression in the fission yeast Schizosaccharomyces pombe.","citation":"Antisense Nucleic Acid Drug Dev 2000 Feb;10(1):29-34","abstract":"A fission yeast model was employed to investigate the influence of antisense gene location on the efficacy of antisense RNA-mediated target gene suppression. Fission yeast transformants were generated that contained the target lacZ gene at a fixed position and a single copy antisense lacZ gene integrated into various genomic locations, including the same locus as the target gene. No significant difference in lacZ suppression was observed when the antisense gene was integrated in close proximity to the target gene locus compared with other genomic locations, indicating that target and antisense gene colocalization is not a critical factor for efficient antisense RNA-mediated gene expression in vivo. Instead, increased lacZ downregulation correlated with an increase in antisense dose, with the steady-state levels of antisense RNA being dependent on genomic position effects and transgene copy number.","authors":"Raponi M, Atkins D, Dawes IW, Arndt GM","authors_abbrev":"Raponi M et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-03-22","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20694150","title":"Copper-dependent trafficking of the Ctr4-Ctr5 copper transporting complex.","citation":"PLoS One 2010 Aug 04;5(8):e11964","abstract":"In Schizosaccharomyces pombe, copper uptake is carried out by a heteromeric complex formed by the Ctr4 and Ctr5 proteins. Copper-induced differential subcellular localization may play a critical role with respect to fine tuning the number of Ctr4 and Ctr5 molecules at the cell surface.\nWe have developed a bimolecular fluorescence complementation (BiFC) assay to analyze protein-protein interactions in vivo in S. pombe. The assay is based on the observation that N- and C-terminal subfragments of the Venus fluorescent protein can reconstitute a functional fluorophore only when they are brought into tight contact. Wild-type copies of the ctr4(+) and ctr5(+) genes were inserted downstream of and in-frame with the nonfluorescent C-terminal (VC) and N-terminal (VN) coding fragments of Venus, respectively. Co-expression of Ctr4-VC and Ctr5-VN fusion proteins allowed their detection at the plasma membrane of copper-limited cells. Similarly, cells co-expressing Ctr4-VN and Ctr4-VC in the presence of Ctr5-Myc(12) displayed a fluorescence signal at the plasma membrane. In contrast, Ctr5-VN and Ctr5-VC co-expressed in the presence of Ctr4-Flag(2) failed to be visualized at the plasma membrane, suggesting a requirement for a combination of two Ctr4 molecules with one Ctr5 molecule. We found that plasma membrane-located Ctr4-VC-Ctr5-VN fluorescent complexes were internalized when the cells were exposed to high levels of copper. The copper-induced internalization of Ctr4-VC-Ctr5-VN complexes was not dependent on de novo protein synthesis. When cells were transferred back from high to low copper levels, there was reappearance of the BiFC fluorescent signal at the plasma membrane.\nThese findings reveal a copper-dependent internalization and recycling of the heteromeric Ctr4-Ctr5 complex as a function of copper availability.","doi":"10.1371/journal.pone.0011964","authors":"Ioannoni R, Beaudoin J, Mercier A, Labbé S","authors_abbrev":"Ioannoni R et al.","pubmed_publication_date":"04 Aug 2010","pubmed_entrez_date":"2010-08-10","publication_year":"2010","canto_session_key":"af0c57973f645afa","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1393.10","SPAC1142.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:16465239","title":"Expression of bak in S. pombe results in a lethality mediated through interaction with the calnexin homologue Cnx1.","citation":"Cell Death Differ 1997 May;4(4):263-71","abstract":"Expression studies in the yeast S. pombe have been utilised to establish the basis for a genetic analysis designed to identify the lethal partners of the pro-apoptotic proteins bak and bax. Bak expression in S. pombe is lethal and this lethality is rescued by co-expression of bcl-2 or bcl-x(L). S. pombe cells expressing bak have a terminal phenotype in which the majority of cells are blocked in the G1 phase of the cell cycle while the remainder of cells, unable to complete M-phase, mis-coordinate the timing of subsequent events in the cell cycle. Although bax expression in S. pombe gives rise to a slow growth phenotype, not a lethality, bax expressing cells display the same cell cycle phenotypes described for bak. Electron microscopy of cells expressing bak reveals a dramatic accumulation of large vesicular structures. A two-hybrid screen designed to identify S. pombe proteins which interact with bak, isolated the S. pombe calnexin homologue cnx1. Genetic analysis demonstrates that the Cnx1 domain which binds to bak in two-hybrid experiments, is necessary for bak lethality in S. pombe. This report identifies a lethal interacting partner for bak and the observations suggest a model for bak mediated lethality which can be tested in higher cells.","authors":"Torgler CN, de Tiani M, Raven T, Aubry JP, Brown R, Meldrum E","authors_abbrev":"Torgler CN et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8200530","title":"Switching gene swi6, involved in repression of silent mating-type loci in fission yeast, encodes a homologue of chromatin-associated proteins from Drosophila and mammals.","citation":"Gene 1994 May 27;143(1):139-43","abstract":"The switching gene swi6 of Schizosaccharomyces pombe is involved in the repression of the silent mating-type loci mat2 and mat3. We have cloned the gene by functional complementation of the switching defect of the swi6-115 mutation. DNA sequence analyses revealed an open reading frame of 984 bp coding for a putative protein of 328 amino acids (aa). The isolation of a swi6 cDNA confirmed this result. Gene replacement showed that swi6 is not essential for viability. The Swi6 protein is very hydrophilic; it contains 41% charged aa. A region of 48 aa is homologous to a sequence motif found in the chromatin-associated proteins, HP1 and Polycomb (Drosophila melanogaster), M31, M32 and M33 (mouse), and the human HSM1 protein. This motif is called chromo domain (chromatin organization modifier). Our results indicate that Swi6 is a structural component of chromatin. Swi6 may have the function to compact mat2 and mat3 into a heterochromatin-like conformation which represses the transcription of these silent cassettes.","authors":"Lorentz A, Ostermann K, Fleck O, Schmidt H","authors_abbrev":"Lorentz A et al.","pubmed_publication_date":"27 May 1994","pubmed_entrez_date":"1994-05-27","publication_year":"1994","canto_session_key":"5954413bec1318d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-09-05 13:39:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-05 13:39:37","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-05"},{"uniquename":"PMID:8247131","title":"Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit.","citation":"Nature 1993 Nov 25;366(6453):355-7","abstract":"We have isolated a mutant, mts2, in the fission yeast Schizosaccharomyces pombe which is defective in chromosome segregation. The predicted amino-acid sequence of the cloned mts2+ gene product is 75% identical to the S4 subunit of the human 26S ATP/ubiquitin-dependent protease. The human S4 subunit complementary DNA expressed from an S. pombe expression plasmid can rescue an S. pombe mts2 gene disruption. Both observations demonstrate that the mts2+ gene is the S. pombe homologue of the human S4 subunit. In addition, we provide genetic evidence for a physical interaction between the S4 and the related S7 subunit in the 26S multiprotein protease. We show that polyubiquitin-conjugated proteins accumulate in the mts2 mutant at the restrictive temperature, demonstrating that the mutant has an in vivo defect in the ubiquitin-dependent proteolysis pathway. Finally, the phenotype for the mts2 mutant indicates that protein degradation by the 26S protease is essential not for entry into but for the completion of mitosis.","authors":"Gordon C, McGurk G, Dillon P, Rosen C, Hastie ND","authors_abbrev":"Gordon C et al.","pubmed_publication_date":"25 Nov 1993","pubmed_entrez_date":"1993-11-25","publication_year":"1993","canto_session_key":"ee92e3801448ef56","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-11 23:22:40","canto_approved_date":"2018-06-12 07:12:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-11 23:22:12","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-11"},{"uniquename":"PMID:27154402","title":"TERRA promotes telomerase-mediated telomere elongation in Schizosaccharomyces pombe.","citation":"EMBO Rep 2016 Jul;17(7):999-1012","abstract":"Telomerase-mediated telomere elongation provides cell populations with the ability to proliferate indefinitely. Telomerase is capable of recognizing and extending the shortest telomeres in cells; nevertheless, how this mechanism is executed remains unclear. Here, we show that, in the fission yeast Schizosaccharomyces pombe, shortened telomeres are highly transcribed into the evolutionarily conserved long noncoding RNA TERRA A fraction of TERRA produced upon telomere shortening is polyadenylated and largely devoid of telomeric repeats, and furthermore, telomerase physically interacts with this polyadenylated TERRA in vivo We also show that experimentally enhanced transcription of a manipulated telomere promotes its association with telomerase and concomitant elongation. Our data represent the first direct evidence that TERRA stimulates telomerase recruitment and activity at chromosome ends in an organism with human-like telomeres.","doi":"10.15252/embr.201541708","authors":"Moravec M, Wischnewski H, Bah A, Hu Y, Liu N, Lafranchi L, King MC, Azzalin CM","authors_abbrev":"Moravec M et al.","pubmed_publication_date":"Jul 2016","pubmed_entrez_date":"2016-05-08","publication_year":"2016","canto_session_key":"b784945eb11bc9fb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-05-09 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8946912","title":"The dmf1/mid1 gene is essential for correct positioning of the division septum in fission yeast.","citation":"Genes Dev 1996 Nov 01;10(21):2707-19","abstract":"Little is known about the mechanisms that establish the position of the division plane in eukaryotic cells. Wild-type fission yeast cells divide by forming a septum in the middle of the cell at the end of mitosis. Dmf1 mutants complete mitosis and initiate septum formation, but the septa that form are positioned at random locations and angles in the cell, rather than in the middle. We have cloned the dmf1 gene as a suppressor of the cdc7-24 mutant. The dmf1 mutant is allelic with mid1. The gene encodes a novel protein containing a putative nuclear localization signal, and a carboxy-terminal PH domain. In wild-type cells, Dmf1p is nuclear during interphase, and relocates to form a medial ring at the cell cortex coincident with the onset of mitosis. This relocalization occurs before formation of the actin ring and is associated with increased phosphorylation of Dmf1p. The Dmf1p ring can be formed in the absence of an actin ring, but depends on some of the genes required for actin ring formation. When the septum is completed and the cells separate, Dmf1p staining is once again nuclear. These data implicate Dmf1p as an important element in assuring correct placement of the division septum in Schizosaccharomyces pombe cells.","authors":"Sohrmann M, Fankhauser C, Brodbeck C, Simanis V","authors_abbrev":"Sohrmann M et al.","pubmed_publication_date":"01 Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_session_key":"9ef4c870fd50a8b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-31 11:28:57","canto_approved_date":"2019-10-31 11:28:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-29 15:36:37","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPYUG7.03c","SPCC18B5.03","SPCC4B3.15","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2019-10-31"},{"uniquename":"PMID:24514982","title":"A divide and conquer strategy for the maximum likelihood localization of low intensity objects.","citation":"Opt Express 2014 Jan 13;22(1):210-28","abstract":"In cell biology and other fields the automatic accurate localization of sub-resolution objects in images is an important tool. The signal is often corrupted by multiple forms of noise, including excess noise resulting from the amplification by an electron multiplying charge-coupled device (EMCCD). Here we present our novel Nested Maximum Likelihood Algorithm (NMLA), which solves the problem of localizing multiple overlapping emitters in a setting affected by excess noise, by repeatedly solving the task of independent localization for single emitters in an excess noise-free system. NMLA dramatically improves scalability and robustness, when compared to a general purpose optimization technique. Our method was successfully applied for in vivo localization of fluorescent proteins.","doi":"10.1364/OE.22.000210","authors":"Krull A, Steinborn A, Ananthanarayanan V, Ramunno-Johnson D, Petersohn U, Tolić-Nørrelykke IM","authors_abbrev":"Krull A et al.","pubmed_publication_date":"13 Jan 2014","pubmed_entrez_date":"2014-02-12","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-10-08 00:15:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8170927","title":"Mutational analysis supports a structural model for the cell cycle protein kinase p34.","citation":"Protein Eng 1994 Feb;7(2):243-53","abstract":"Structural models for the eukaryotic cell cycle control protein p34 from human, S. pombe and S. cerevisiae have been derived from the crystallographic coordinates of the cAMP-dependent protein kinase (cAPK) catalytic subunit (active conformation) and compared with the structure of inactive CDK2 apoenzyme. Differences between the p34 and cAPK catalytic sites provide a possible explanation for their different substrate specificities. The p34 models localize Tyr15 and Thr14 close to the sites of catalysis and substrate recognition where their phosphorylation could inhibit p34 kinase activity either by blocking MgATP or substrate binding. The conserved sequences PSTAIRE and LYLIFEFL are both close to the catalytic site and accessible on the protein surface available to mediate interactions with other proteins. It is predicted that p34 has an active-site cleft composed almost entirely of sequences common to all protein kinases and sequences unique to the p34 protein family. Genetic and biochemical analyses of p34 have shown that it interacts extensively with a number of other proteins. The model allows the relative disposition of these sites of mutation to each other and to the sites of catalysis and substrate recognition to be appreciated. Surface regions on p34 that are important for function have been identified. These sites identify residues that may interact with p13suc1, cyclin, p107wee1 and p80cdc25.","authors":"Endicott JA, Nurse P, Johnson LN","authors_abbrev":"Endicott JA et al.","pubmed_publication_date":"Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_session_key":"8e23c976e5849c97","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-11-29 16:51:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-20 14:37:30","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC1734.14c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2016-10-20"},{"uniquename":"PMID:29898918","title":"Mutations that prevent methylation of cohesin render sensitivity to DNA damage in  S. pombe .","citation":"J Cell Sci 2018 Jul 06;131(13)","abstract":"The canonical role of cohesin is to mediate sister chromatid cohesion. In addition, cohesin plays important roles in processes such as DNA repair and regulation of gene expression. Mounting evidence suggests that various post-translational modifications, including phosphorylation, acetylation and sumoylation regulate cohesin functions. Our mass spectrometry analysis of cohesin purified from  Schizosaccharomyces pombe  cells revealed that the cohesin subunit Psm1 is methylated on two evolutionarily conserved lysine residues, K536 and K1200. We found that mutations that prevent methylation of Psm1 K536 and K1200 render sensitivity to DNA-damaging agents and show positive genetic interactions with mutations in genes encoding the Mus81-Eme1 endonuclease. Yeast two-hybrid and co-immunoprecipitation assays showed that there were interactions between subunits of the cohesin and Mus81-Eme1 complexes. We conclude that cohesin is methylated and that mutations that prevent methylation of Psm1 K536 and K1200 show synthetic phenotypes with mutants defective in the homologous recombination DNA repair pathway.","doi":"10.1242/jcs.214924","authors":"Sanyal S, Molnarova L, Richterova J, Huraiova B, Benko Z, Polakova S, Cipakova I, Sevcovicova A, Gaplovska-Kysela K, Mechtler K, Cipak L, Gregan J","authors_abbrev":"Sanyal S et al.","pubmed_publication_date":"06 Jul 2018","pubmed_entrez_date":"2018-06-15","publication_year":"2018","canto_session_key":"2f54522ed2a9d3d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Swastika Sanyal","canto_first_approved_date":"2018-07-04 15:06:17","canto_approved_date":"2024-02-28 10:00:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-27 13:05:58","canto_added_date":"2018-06-16 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":30,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Swastika Sanyal","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP27G11.15","SPAPB1E7.06c","SPBC29A10.14","SPBC28F2.07","SPBC29A10.04","SPAC17H9.20","SPAC20H4.07","SPCC338.17c","SPAC4H3.05","SPCC4E9.01c","SPCC4G3.05c","SPAC3C7.03c","SPAC30D11.10","SPAC2G11.12","SPAC10F6.09c"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2018-07-04"},{"uniquename":"PMID:19629157","title":"Identification of a topological characteristic responsible for the biological robustness of regulatory networks.","citation":"PLoS Comput Biol 2009 Jul;5(7):e1000442","abstract":"Attribution of biological robustness to the specific structural properties of a regulatory network is an important yet unsolved problem in systems biology. It is widely believed that the topological characteristics of a biological control network largely determine its dynamic behavior, yet the actual mechanism is still poorly understood. Here, we define a novel structural feature of biological networks, termed 'regulation entropy', to quantitatively assess the influence of network topology on the robustness of the systems. Using the cell-cycle control networks of the budding yeast (Saccharomyces cerevisiae) and the fission yeast (Schizosaccharomyces pombe) as examples, we first demonstrate the correlation of this quantity with the dynamic stability of biological control networks, and then we establish a significant association between this quantity and the structural stability of the networks. And we further substantiate the generality of this approach with a broad spectrum of biological and random networks. We conclude that the regulation entropy is an effective order parameter in evaluating the robustness of biological control networks. Our work suggests a novel connection between the topological feature and the dynamic property of biological regulatory networks.","doi":"10.1371/journal.pcbi.1000442","authors":"Wu Y, Zhang X, Yu J, Ouyang Q","authors_abbrev":"Wu Y et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-07-25","publication_year":"2009","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084861","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.53"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24484658","title":"Reconstituting functional microtubule-barrier interactions.","citation":"Methods Cell Biol 2014;120:69-90","abstract":"Local interactions between the tips of microtubules and the cell cortex, or other cellular components such as kinetochores, play an important role in essential cellular processes like establishing cell polarity, distribution of organelles, and microtubule aster and chromosome positioning. Here we present two in vitro assays that specifically mimic microtubule-cortex interactions by employing selectively functionalized microfabricated barriers that allow for the immobilization of proteins with a range of affinities. We describe the microfabrication process to create gold or glass barriers and the subsequent functionalization of these barriers using self-assembled thiol monolayers or polylysine-poly(ethylene glycol), respectively. Near-permanent attachment of proteins is obtained using biotinylated surfaces combined with streptavidin and biotinylated proteins. Lower affinity interactions, further tunable with the addition of imidazole, are obtained using nickel-nitrilotriacetic acid (Ni(II)-NTA) functionalization combined with his-tagged proteins. Both mono-NTA and tris-NTA compounds are used. We show an assay to reconstitute the \"end-on\" interaction between dynamic microtubule tips and barrier-attached dynein, mimicking the cellular situation at the cortex and at kinetochores. In a second assay, we reconstitute microtubule-based delivery of end-tracking proteins to functionalized barriers, mimicking the transport of cell-end markers to the cell poles in interphase fission yeast cells.","doi":"10.1016/B978-0-12-417136-7.00005-7","authors":"Taberner N, Weber G, You C, Dries R, Piehler J, Dogterom M","authors_abbrev":"Taberner N et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-04","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12930957","title":"Nuclear factories for signalling and repairing DNA double strand breaks in living fission yeast.","citation":"Nucleic Acids Res 2003 Sep 01;31(17):5064-73","abstract":"In mammalian and budding yeast cells treated with genotoxic agents, different proteins implicated in detecting, signalling or repairing DNA lesions form nuclear foci. We studied foci formed by proteins involved in these processes in living fission yeast cells, which is amenable to genetic and molecular analysis. Using fluorescent tags, we analysed subnuclear localisations of the DNA damage checkpoint protein Rad9, of the homologous recombination protein Rad22 and of PCNA, which are implicated in many aspects of DNA metabolism. After inducing double strand breaks (DSBs) with ionising radiations, Rad22, Rad9 and PCNA form a low number of nuclear foci. Rad9 recruitment to foci depends on the presence of Rad1, Hus1 and Rad17, but is independent of downstream checkpoint effectors and of homologous recombination proteins. Likewise, Rad22 and PCNA form foci despite inactive homologous recombination repair and impaired DNA damage checkpoint. Rad22 and Rad9 foci co-localise completely, whereas PCNA co-localises with Rad22 and Rad9 only partially. Foci do not disassemble in cells unable to repair DNA by homologous recombination. Thus, in fission yeast, DSBs are detected by the DNA damage checkpoint and are repaired by homologous recombination at a few spatially confined subnuclear compartments where Rad22, Rad9 and PCNA concentrate independently.","authors":"Meister P, Poidevin M, Francesconi S, Tratner I, Zarzov P, Baldacci G","authors_abbrev":"Meister P et al.","pubmed_publication_date":"01 Sep 2003","pubmed_entrez_date":"2003-08-22","publication_year":"2003","canto_session_key":"25bff57360ee7d2f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-02-29 15:59:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-02-29 15:59:14","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC9E9.08","SPBC342.05","SPAC13C5.07","SPBC16D10.09","SPAC644.14c","SPAC20G4.04c","SPAC1556.01c","SPAC1952.07","SPCC18B5.11c","SPAC14C4.13","SPBC216.05","SPAC30D11.10","SPAC664.07c"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2016-02-29"},{"uniquename":"PMID:3785193","title":"Differential expressions of essential and nonessential alpha-tubulin genes in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1986 Jun;6(6):2168-78","abstract":"The fission yeast Schizosaccharomyces pombe has two alpha-tubulin genes and one beta-tubulin gene. Gene disruption experiments showed that the alpha 1-tubulin gene (NDA2) is essential whereas the alpha 2 gene is dispensable. The alpha 2-disrupted cells missing alpha 2 transcript and alpha 2 polypeptide could grow and sporulate normally. The alpha 2 gene, however, was expressed in the wild type and the alpha 1 mutant. Alpha 2-Tubulin was distinguished as an electrophoretic band and was assembled into microtubules. The alpha 2-disrupted cells had an increased sensitivity to an antimicrotubule drug thiabendazole, and the alpha 1(cold-sensitive [cs]) alpha 2 (disrupted) cells became not only cs but also temperature sensitive. Northern blot experiments indicated that alpha 2 transcription was minor and constitutive whereas alpha 1 transcription was major and modulated, depending on the gene copy number of the alpha 2 gene. The amounts of alpha 1 and alpha 2 polypeptides estimated by beta-galactosidase activities of the lacZ-fused genes integrated on the chromosome and by intensities of the electrophoretic bands in crude tubulin fractions, however, were comparable, indicating that alpha 2 tubulin is not a minor subtype. We assume that the cells of Schizosaccharomyces pombe have no excess tubulin pool. alpha 1 mutants would then be blocked in the cell cycle because only half the amount of functional alpha-tubulin required for growth can be produced by the alpha 2 gene. On the other hand, the alpha 2-disrupted cells became viable because the synthesis of alpha 1 tubulin was increased by transcriptional or translational modulation or both. The real cause for essential alpha 1 and dispensable alpha 2 genes seems to be in their regulatory sequences instead of the coding sequences.","authors":"Adachi Y, Toda T, Niwa O, Yanagida M","authors_abbrev":"Adachi Y et al.","pubmed_publication_date":"Jun 1986","pubmed_entrez_date":"1986-06-01","publication_year":"1986","canto_session_key":"1010b1ba89954039","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-09 17:29:23","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-16 22:19:26","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPBC800.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-10-16"},{"uniquename":"PMID:18422602","title":"Schizosaccharomyces pombe Snf2SR, a novel SNF2 family protein, interacts with Ran GTPase and modulates both RanGEF and RanGAP activities.","citation":"Genes Cells 2008 Jun;13(6):571-82","abstract":"Snf2SR, a suppressor of rna1(ts), which is a temperature-sensitive mutation in Schizosaccharomyces pombe RanGAP (GTPase activating protein), possesses both the SNF2 and the helicase domains conserved in the chromatin remodeling SNF2 ATPase/helicase protein family. We have now clarified a function of Snf2SR. Snf2SR indeed showed DNA-stimulated ATPase activity, proving that it is a member of the SNF2 ATPase/helicase family. Consistent with this role, Snf2SR was localized in the nucleus and cell fractionation analysis revealed that Snf2SR was tightly associated with the nuclear matrix. The disruption of snf2SR(+) was detrimental for a cell proliferation of S. pombe. Snf2SR that did not enhance RanGAP activity by itself, but abolished histone-H3-mediated RanGAP inhibition, as previously reported for the histone H3 methyltransferase, Clr4, another rna1(ts) suppressor. In contrast to Clr4, Snf2SR directly bound to the GDP-bound form of the S. pombe Ran homologue Spi1 and enhanced the nucleotide exchange activity of Pim1, the S. pombe RanGEF (guanine nucleotide exchange factor). Over-expression of Spi1-G18V, a Ran GTPase mutant fixed in the GTP-bound form, was lethal to S. pombe Deltasnf2SR. Together, our results indicate that Snf2SR is involved in the Ran GTPase cycle in vivo.","doi":"10.1111/j.1365-2443.2008.01190.x","authors":"Ohba T, Nishijima H, Nishitani H, Nishimoto T","authors_abbrev":"Ohba T et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-22","publication_year":"2008","canto_session_key":"bc16edfb200d65c2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-09-23 15:19:58","canto_approved_date":"2022-05-08 15:32:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-23 15:19:47","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1289.03c","SPBC557.03c","SPAC22E12.07","SPAC25A8.01c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2021-09-23"},{"uniquename":"PMID:6262315","title":"Partial purification of RNase P from Schizosaccharomyces pombe.","citation":"J Biol Chem 1981 May 25;256(10):5058-63","abstract":"Ribonuclease P from the fission yeast Schizosaccharomyces pombe was partially purified using DEAE-cellulose and phosphocellulose column chromatography. The yeast RNase P enzyme cleaves Escherichia coli tRNATyr precursor to give tRNATyr containing its mature 5' end. The enzyme activity is inhibited after treatment with nucleases; this indicates the requirement of a nucleic acid component for activity. The enzyme purification was greatly facilitated by using a synthetically prepared radioactive ApApApCOH ligated to the 5'-terminal phosphate of E. coli tRNAfMet (ApApApCp-tRNA) substrate. (p denotes a [32P]phosphate group.) This substrate was cleaved by yeast RNase P to the mature tRNA and a tetranucleoside triphosphate ApApApCOH. The synthetic substrate allowed the utilization of a simple assay procedure measuring the trichloroacetic acid solubility of the ApApApC product, thus avoiding the more cumbersome gel electrophoric separation of reaction products.","authors":"Kline L, Nishikawa S, Söll D","authors_abbrev":"Kline L et al.","pubmed_publication_date":"25 May 1981","pubmed_entrez_date":"1981-05-25","publication_year":"1981","canto_session_key":"6664dc9b8f0a3b88","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-09-04 10:36:16","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-04 09:48:03","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6C3.09","SPCC16C4.05","SPBC1709.20","SPAC25B8.16","SPBC1703.01c","SPNCRNA.128","SPBC1105.16c","SPCC830.09c","SPAC3A12.04c"],"gene_count":9,"ltp_gene_count":1,"approved_date":"2014-09-04"},{"uniquename":"PMID:7780738","title":"A small peptide inhibitor of DNA replication defines the site of interaction between the cyclin-dependent kinase inhibitor p21WAF1 and proliferating cell nuclear antigen.","citation":"Curr Biol 1995 Mar 01;5(3):275-82","abstract":"p21WAF1 is a potent inhibitor of the cell-cycle regulatory cyclin-dependent kinases (Cdks). It acts on Cdks in the G1 and S phases of the cell cycle, and also binds to proliferating cell nuclear antigen (PCNA), blocking DNA replication in vitro. Transcription of p21WAF1 can be induced by the human tumour suppressor protein p53, suggesting that the action of p21WAF1 may be important in cancer prevention. We have investigated the interaction between p21WAF1 and PCNA using a genetic two-hybrid screen and with arrays of synthetic peptides derived from the p21WAF1 protein sequence.\nWe have established that the carboxy-terminal region of p21WAF1 interacts with PCNA in a yeast two-hybrid screen. Interaction with p21WAF1 involves the central loop of PCNA, which connects the two domains of the PCNA monomer. The interaction was finely mapped using peptides derived from the entire sequence of the p21WAF1 protein, and the critical residues were found to be QTSMTDFY (amino acids 144-151 of p21WAF1). Remarkably, a 20-residue peptide containing this sequence inhibited replication of simian virus 40 (SV40) DNA in vitro and could capture PCNA from whole cell extracts, demonstrating that small molecules can retain the biological activity characteristic of the whole protein. Sequential alanine-scan mutations of the peptide demonstrated that its ability to block replication correlates with its affinity for binding PCNA.\nWe have shown that PCNA and the cell-cycle regulator p21WAF1 interact in vivo, and that this interaction requires the central loop of PCNA and an eight amino-acid motif from the carboxyl terminus of p21WAF1.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Warbrick E, Lane DP, Glover DM, Cox LS","authors_abbrev":"Warbrick E et al.","pubmed_publication_date":"01 Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_session_key":"51dcb273cfccbcd1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-29 15:42:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-29 15:41:57","canto_added_date":"2016-09-21 00:21:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-09-29"},{"uniquename":"PMID:25414342","title":"Rad51/Dmc1 paralogs and mediators oppose DNA helicases to limit hybrid DNA formation and promote crossovers during meiotic recombination.","citation":"Nucleic Acids Res 2014 Dec 16;42(22):13723-35","abstract":"During meiosis programmed DNA double-strand breaks (DSBs) are repaired by homologous recombination using the sister chromatid or the homologous chromosome (homolog) as a template. This repair results in crossover (CO) and non-crossover (NCO) recombinants. Only CO formation between homologs provides the physical linkages guiding correct chromosome segregation, which are essential to produce healthy gametes. The factors that determine the CO/NCO decision are still poorly understood. Using Schizosaccharomyces pombe as a model we show that the Rad51/Dmc1-paralog complexes Rad55-Rad57 and Rdl1-Rlp1-Sws1 together with Swi5-Sfr1 play a major role in antagonizing both the FANCM-family DNA helicase/translocase Fml1 and the RecQ-type DNA helicase Rqh1 to limit hybrid DNA formation and promote Mus81-Eme1-dependent COs. A common attribute of these protein complexes is an ability to stabilize the Rad51/Dmc1 nucleoprotein filament, and we propose that it is this property that imposes constraints on which enzymes gain access to the recombination intermediate, thereby controlling the manner in which it is processed and resolved.","doi":"10.1093/nar/gku1219","authors":"Lorenz A, Mehats A, Osman F, Whitby MC","authors_abbrev":"Lorenz A et al.","pubmed_publication_date":"16 Dec 2014","pubmed_entrez_date":"2014-11-22","publication_year":"2014","canto_session_key":"903cb37e16a1d237","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alexander Lorenz","canto_first_approved_date":"2016-09-07 13:39:22","canto_approved_date":"2025-05-29 15:13:29","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-09-03 11:51:25","canto_added_date":"2014-11-23 01:15:38","annotation_curators":[{"name":"Alexander Lorenz","community_curator":true,"annotation_count":154,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.03c","SPBC1685.11","SPBC11B10.06","SPAC8E11.03c","SPAC17H9.03c","SPAC2G11.12","SPAC9.05","SPCC4G3.05c","SPBC28F2.07"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-09-07"},{"uniquename":"PMID:33417242","title":"Effect of alcoholic and acetous fermentations on the phenolic acids of Kei-apple (Dovyalis caffra L.) fruit.","citation":"J Sci Food Agric 2021 Aug 15;101(10):4315-4320","abstract":"The Kei apple is a tree found on the African continent. Limited information exists on the effect of alcoholic and acetous fermentation on the phytochemicals of Kei apple. The fruit has increased concentrations of l-malic, ascorbic, and phenolic acids among other compounds. Juice was co-inoculated with Schizosaccharomyces pombe (Sp) and Saccharomyces cerevisiae (Sc) to induce alcoholic fermentation (AF). Acetous fermentation followed AF, using an acetic acid bacteria (AAB) consortium.\nSaccharomyces cerevisiae + Sp wines and vinegars had the highest pH. Total acidity, soluble solids and l-malic acid decreased during AF and acetous fermentation, and was highest in Sc wines and vinegars. Volatile acidity (VA) concentration was highest in Sp vinegars but was not significantly different from Sc and Sc + Sp vinegars. Gallic acid was highest in Sp wines and vinegars, whereas syringic acid was highest in Sc wines and vinegars. The Sc + Sp wines were highest in caffeic, p-coumaric, and protocatechuic acids. Schizosaccharomyces pombe vinegars were highest in caffeic and p-coumaric acids. Highest concentrations of ferulic and sinapic acids were found in Sp and Sc wines, respectively. Chlorogenic acid was most abundant phenolic acid in both wines and vinegars.\nSaccharomyces cerevisiae + Sp and Sc fermentation had a positive effect on most phenolic acids; Sc + AAB had an increased effect on syringic and chlorogenic acids, whereas Sp + AAB resulted in an increase in gallic, caffeic, and p-coumaric acids. The AAB selected had minimal performance with respect to VA production in comparison to commercial vinegars. Acetic acid bacteria selection for acetous fermentation should therefore be reconsidered and the decrease of certain phenolic acids during acetous fermentation needs to be investigated. © 2021 Society of Chemical Industry.","doi":"10.1002/jsfa.11071","authors":"Minnaar P, Jolly N, Beukes L, Benito S","authors_abbrev":"Minnaar P et al.","pubmed_publication_date":"15 Aug 2021","pubmed_entrez_date":"2021-01-08","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-01-10 01:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27844442","title":"Quantifying Force and Viscoelasticity Inside Living Cells Using an Active-Passive Calibrated Optical Trap.","citation":"Methods Mol Biol 2017;1486:513-536","abstract":"As described in the previous chapters, optical tweezers have become a tool of precision for in vitro single-molecule investigations, where the single molecule of interest most often is studied in purified form in an experimental assay with a well-controlled fluidic environment. A well-controlled fluidic environment implies that the physical properties of the liquid, most notably the viscosity, are known and the fluidic environment can, for calibrational purposes, be treated as a simple liquid.In vivo, however, optical tweezers have primarily been used as a tool of manipulation and not so often for precise quantitative force measurements, due to the unknown value of the spring constant of the optical trap formed within the cell's viscoelastic cytoplasm. Here, we describe a method for utilizing optical tweezers for quantitative in vivo force measurements. The experimental protocol and the protocol for data analysis rely on two types of experiments, passive observation of the thermal motion of a trapped object inside a living cell, followed by observations of the response of the trapped object when subject to controlled oscillations of the optical trap. One advantage of this calibration method is that the size and refractive properties of the trapped object and the viscoelastic properties of its environment need not be known. We explain the protocol and demonstrate its use with experiments of trapped granules inside live S. pombe cells.","doi":"10.1007/978-1-4939-6421-5_20","authors":"Ritter CM, Mas J, Oddershede L, Berg-Sørensen K","authors_abbrev":"Ritter CM et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2016-11-16","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-17 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8573678","title":"A model for a bistable biochemical trigger of mitosis.","citation":"Biophys Chem 1996 Jan;57(2-3):239-51","abstract":"The activation of maturation promoting factor (MPF, cyclin B/Cdc2), which starts mitosis, is modeled as a bistable biochemical switch or trigger. A small, slow parameter change can cause an abrupt transition by a saddle-node bifurcation from a stable steady state of low activity to one of high activity. The switch is not reversed if the parameter change is reversed (hysteresis). The dynamical features necessary for this triggering action are the presence of two stable steady states (low-activity and high-activity), and one unstable steady state. The key biochemical kinetic features of the model are (1) mutual activation by MPF and Cdc25, which makes the activation of MPF effectively autocatalytic, and (2) binding of MPF by Suc1, which inhibits MPF autocatalysis and stabilizes the low-activity steady state until the amount of MPF begins to approach or exceed stoichiometrically the amount of Suc1, then allows strong autocatalysis and full activation. The special virtues of bistable triggering, and the general types of biochemical mechanism which can produce it, are discussed.","authors":"Thron CD","authors_abbrev":"Thron CD","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5094802","title":"Mosaicism and lethal sectoring in G1 cells of Schizosaccharomyces pombe.","citation":"Mutat Res 1971 Jun;12(2):143-50","abstract":"","authors":"Abbondandolo A, Simi S","authors_abbrev":"Abbondandolo A et al.","pubmed_publication_date":"Jun 1971","pubmed_entrez_date":"1971-06-01","publication_year":"1971","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF11968","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.10","HGNC:26475"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23397571","title":"Transcriptional regulation of the copper transporter mfc1 in meiotic cells.","citation":"Eukaryot Cell 2013 Apr;12(4):575-90","abstract":"Mfc1 is a meiosis-specific protein that mediates copper transport during the meiotic program in Schizosaccharomyces pombe. Although the mfc1(+) gene is induced at the transcriptional level in response to copper deprivation, the molecular determinants that are required for its copper starvation-dependent induction are unknown. Promoter deletion and site-directed mutagenesis have allowed identification of a new cis-regulatory element in the promoter region of the mfc1(+) gene. This cis-acting regulatory sequence containing the sequence TCGGCG is responsible for transcriptional activation of mfc1(+) under low-copper conditions. The TCGGCG sequence contains a CGG triplet known to serve as a binding site for members of the Zn(2)Cys(6) binuclear cluster transcriptional regulator family. In agreement with this fact, one member of this group of regulators, denoted Mca1, was found to be required for maximum induction of mfc1(+) gene expression. Analysis of Mca1 cellular distribution during meiosis revealed that it colocalizes with both chromosomes and sister chromatids during early, middle, and late phases of the meiotic program. Cells lacking Mca1 exhibited a meiotic arrest at metaphase I under low-copper conditions. Binding studies revealed that the N-terminal 150-residue segment of Mca1 expressed as a fusion protein in Escherichia coli specifically interacts with the TCGGCG sequence of the mfc1(+) promoter. Taken together, these results identify the cis-regulatory TCGGCG sequence and the transcription factor Mca1 as critical components for activation of the meiotic copper transport mfc1(+) gene in response to copper starvation.","doi":"10.1128/EC.00019-13","authors":"Beaudoin J, Ioannoni R, Mailloux S, Plante S, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2013-02-12","publication_year":"2013","canto_session_key":"255b672ea4790714","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19118689","title":"Chapter 20: Automated spatial mapping of microtubule catastrophe rates in fission yeast.","citation":"Methods Cell Biol 2008;89:521-38","abstract":"Microtubules (MTs) are cytoskeletal polymers whose spatial organization is dynamically regulated, depending on their biological function during different cell cycle stages. Growing MT ends are, for example, specifically targeted towards the cortex of motile or growing cells during interphase or towards chromosomal attachment sites during mitosis. An important parameter that cells use to control the average length of MTs, and thus the distance over which these targeting processes may operate, is the so-called catastrophe frequency f(cat): the rate at which MTs switch from a growing to a shrinking state. To understand how spatial targeting and the local control of f(cat) are related, quantitative in vivo measurements are needed that allow for the measurement of f(cat) in a spatially resolved way. Since catastrophes are intrinsically stochastic events, it is essential to acquire enough statistics to obtain the underlying rate constant f(cat). Here, we present automated image processing methodology, developed using GFP-tubulin expressing fission yeast cells, that makes it possible to measure f(cat) both spatially resolved and with high statistical accuracy. Although certain aspects of the analysis are specific to the system under investigation the basic concepts of the methodology are applicable to any kind of movies of fluorescently labeled MTs.","doi":"10.1016/S0091-679X(08)00620-1","authors":"Tischer C, Brunner D, Dogterom M","authors_abbrev":"Tischer C et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2009-01-03","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12127768","title":"Fission yeast blooms in Kyoto.","citation":"Trends Genet 2002 Jul;18(7):342-3","abstract":"","authors":"Pasion S","authors_abbrev":"Pasion S","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-07-20","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12966087","title":"Novel essential DNA repair proteins Nse1 and Nse2 are subunits of the fission yeast Smc5-Smc6 complex.","citation":"J Biol Chem 2003 Nov 14;278(46):45460-7","abstract":"The structural maintenance of chromosomes (SMC) family of proteins play essential roles in genomic stability. SMC heterodimers are required for sister-chromatid cohesion (Cohesin: Smc1 & Smc3), chromatin condensation (Condensin: Smc2 & Smc4), and DNA repair (Smc5 & Smc6). The SMC heterodimers do not function alone and must associate with essential non-SMC subunits. To gain further insight into the essential and DNA repair roles of the Smc5-6 complex, we have purified fission yeast Smc5 and identified by mass spectrometry the co-precipitating proteins, Nse1 and Nse2. We show that both Nse1 and Nse2 interact with Smc5 in vivo, as part of the Smc5-6 complex. Nse1 and Nse2 are essential proteins and conserved from yeast to man. Loss of Nse1 and Nse2 function leads to strikingly similar terminal phenotypes to those observed for Smc5-6 inactivation. In addition, cells expressing hypomorphic alleles of Nse1 and Nse2 are, like Smc5-6 mutants, hypersensitive to DNA damage. Epistasis analysis suggests that like Smc5-6, Nse1, and Nse2 function together with Rhp51 in the homologous recombination repair of DNA double strand breaks. The results of this study strongly suggest that Nse1 and Nse2 are novel non-SMC subunits of the fission yeast Smc5-6 DNA repair complex.","authors":"McDonald WH, Pavlova Y, Yates JR, Boddy MN","authors_abbrev":"McDonald WH et al.","pubmed_publication_date":"14 Nov 2003","pubmed_entrez_date":"2003-09-11","publication_year":"2003","canto_session_key":"b401e8548347ee00","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-02-13 16:11:32","canto_approved_date":"2026-01-29 18:02:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-25 15:58:23","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC550.05","SPCC5E4.06","SPAC16A10.06c","SPAC14C4.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-02-13"},{"uniquename":"PMID:6117557","title":"Electrogenic proton translocation coupled to ATP hydrolysis by the plasma membrane Mg2+-dependent ATPase of yeast in reconstituted proteoliposomes.","citation":"J Biol Chem 1981 Dec 10;256(23):12081-7","abstract":"The purified plasma membrane Mg2+-dependent ATPase of the yeast Schizosaccharomyces pombe was incorporated in liposomes using a cholate-dialysis method. The ATPase activity of the incorporated enzyme was stimulated by the H+-conducting agent carbonyl cyanide m-chlorophenylhydrazone and to a much lower extent of the K+-ionophore valinomycin in the presence of potassium. The K+/H+ exchanger nigericin (plus K+) did not stimulate ATPase activity, whereas the combined addition of both nigericin plus valinomycin was strongly stimulatory. The incorporated ATPase activity was controlled by the generated electrochemical H+ gradient since only conditions which collapse both the membrane potential and the pH gradient stimulated fully the ATPase activity of the incorporated enzyme. Direct measurement of proton movement with a pH glass electrode showed a fast and transient proton entry into the proteoliposomes upon addition of MgATP in the presence of the charge-compensating cation K+ (plus valinomycin). Moreover, during the steady state ATP hydrolysis, a H+ entry was again observed when the membrane potential was collapsed upon addition of valinomycin in the presence of K+. These data demonstrate that the plasma membrane ATPase of yeast cells is involved in electrogenic H+ translocation coupled to ATP hydrolysis since the purified enzyme incorporated in the liposomes is virtually free of mitochondrial F1F0-ATPase contaminant.","authors":"Villalobo A, Boutry M, Goffeau A","authors_abbrev":"Villalobo A et al.","pubmed_publication_date":"10 Dec 1981","pubmed_entrez_date":"1981-12-10","publication_year":"1981","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23427262","title":"The internal loop of fission yeast Ndc80 binds Alp7/TACC-Alp14/TOG and ensures proper chromosome attachment.","citation":"Mol Biol Cell 2013 Apr;24(8):1122-33","abstract":"The Ndc80 outer kinetochore complex plays a critical role in kinetochore-microtubule attachment, yet our understanding of the mechanism by which this complex interacts with spindle microtubules for timely and accurate chromosome segregation remains limited. Here we address this issue using an ndc80 mutant (ndc80-NH12) from fission yeast that contains a point mutation within a ubiquitous internal loop. This mutant is normal for assembly of the Ndc80 complex and bipolar spindle formation yet defective in proper end-on attachment to the spindle microtubule, with chromosome alignment defects and missegregation happening later during mitosis. We find that ndc80-NH12 exhibits impaired localization of the microtubule-associated protein complex Alp7/transforming acidic coiled coil (TACC)-Alp14/tumor-overexpressed gene (TOG) to the mitotic kinetochore. Consistently, wild-type Ndc80 binds these two proteins, whereas the Ndc80-NH12 mutant protein displays a substantial reduction of interaction. Crucially, forced targeting of Alp7-Alp14 to the outer kinetochore rescues ndc80-NH12-mutant phenotypes. The loop was previously shown to bind Dis1/TOG, by which it ensures initial chromosome capture during early mitosis. Strikingly, ndc80-NH12 is normal in Dis1 localization. Genetic results indicate that the loop recruits Dis1/TOG and Alp7/TACC-Alp14/TOG independently. Our work therefore establishes that the Ndc80 loop plays sequential roles in spindle-kinetochore attachment by connecting the Ndc80 complex to Dis1/TOG and Alp7/TACC-Alp14/TOG.","doi":"10.1091/mbc.E12-11-0817","authors":"Tang NH, Takada H, Hsu KS, Toda T","authors_abbrev":"Tang NH et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2013-02-22","publication_year":"2013","canto_session_key":"02ecd4cbe772e63c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-10-26 15:37:11","canto_approved_date":"2020-07-07 17:01:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-20 06:39:24","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12D12.01","SPAC1687.20c","SPAC890.02c","SPCC736.14","SPCC188.04c","SPAC27F1.04c","SPBC800.05c","SPBC11C11.03","SPBC20F10.06","SPBC649.05","SPCC895.07"],"gene_count":11,"ltp_gene_count":5,"approved_date":"2017-10-26"},{"uniquename":"PMID:11812792","title":"Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.","citation":"J Biol Chem 2002 Apr 05;277(14):12375-81","abstract":"Cyclin-dependent kinase subunit (CKS) proteins bind to cyclin-dependent kinases and target various proteins to phosphorylation and proteolysis during cell division. Crystal structures showed that CKS can exist both in a closed monomeric conformation when bound to the kinase and in an inactive C-terminal beta-strand-exchanged conformation. With the exception of the hinge loop, however, both crystal structures are identical, and no new protein interface is formed in the dimer. Protein engineering studies have pinpointed the crucial role of the proline 90 residue of the p13(suc1) CKS protein from Schizosaccharomyces pombe in the monomer-dimer equilibrium and have led to the concept of a loaded molecular spring of the beta-hinge motif. Mutation of this hinge proline into an alanine stabilizes the protein and prevents the occurrence of swapping. However, other mutations further away from the hinge as well as ligand binding can equally shift the equilibrium between monomer and dimer. To address the question of differential affinity through relief of the strain, here we compare the ligand binding of the monomeric form of wild-type S. pombe p13(suc1) and its hinge mutant P90A in solution by NMR spectroscopy. We indeed observed a 5-fold difference in affinity with the wild-type protein being the most strongly binding. Our structural study further indicates that both wild-type and the P90A mutant proteins adopt in solution the closed conformation but display different dynamic properties in the C-terminal beta-sheet involved in domain swapping and protein interactions.","authors":"Odaert B, Landrieu I, Dijkstra K, Schuurman-Wolters G, Casteels P, Wieruszeski JM, Inze D, Scheek R, Lippens G","authors_abbrev":"Odaert B et al.","pubmed_publication_date":"05 Apr 2002","pubmed_entrez_date":"2002-01-29","publication_year":"2002","canto_session_key":"8ef010999dcba297","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-05-20 14:19:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-20 14:18:49","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.14c","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-05-20"},{"uniquename":"PMID:8227043","title":"The Schizosaccharomyces pombe mating-type gene mat-Mc encodes a sequence-specific DNA-binding high mobility group box protein.","citation":"J Biol Chem 1993 Nov 25;268(33):24813-7","abstract":"The Schizosaccharomyces pombe gene mat-Mc plays a determinative role in the sexual differentiation of the fission yeast. The mat-Mc protein has been suggested to belong to a novel family of so-called high mobility group (HMG) box proteins, characterized by homology to high mobility group-1 and -2 proteins. Several HMG box proteins, including the mammalian sex-determining gene product SRY and the lymphoid transcription factors TCF-1 and LEF-1, have been shown to bind to DNA in a sequence-specific fashion. To analyze possible DNA-binding properties of mat-Mc, we have cloned and expressed its putative HMG box in Escherichia coli. Gel retardation analysis revealed that the mat-Mc HMG box recognizes the AACAAAG heptamer in a sequence-specific fashion. Combined T-->C and A-->I substitutions on both strands of the AACAAAG heptamer, which change the surface of the major groove while leaving the minor groove intact, did not interfere with sequence-specific binding of mat-Mc. Methylation interference analysis confirmed that the mat-Mc HMG box contacts adenine residues in the minor groove. By using a circular permutation assay, the mat-Mc HMG box was observed to bend DNA. These results indicate that mat-Mc is indeed a member of the HMG box family with DNA-binding characteristics assigned earlier to other members of this novel transcription factor family.","authors":"Dooijes D, van de Wetering M, Knippels L, Clevers H","authors_abbrev":"Dooijes D et al.","pubmed_publication_date":"25 Nov 1993","pubmed_entrez_date":"1993-11-25","publication_year":"1993","canto_session_key":"289cf1b4df3fdf68","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-28 13:56:47","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-24 14:58:30","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-24"},{"uniquename":"PMID:10467003","title":"The pub1 E3 ubiquitin ligase negatively regulates leucine uptake in response to NH(4)(+) in fission yeast.","citation":"Curr Genet 1999 Jul;35(6):593-601","abstract":"Fission yeast strains auxotrophic for leucine are unable to proliferate in normally supplemented minimal media adjusted to pH 6. 4 or above. High-pH sensitivity can be suppressed by the loss of Pub1, an E3 ubiquitin ligase, or by the replacement of NH(4)(+) with a non-repressing source of nitrogen such as L-proline. In this report we show pub1 to be required for the rapid down-regulation of leucine uptake observed in response to the addition of NH(4)(+) to the growth media. Furthermore, we corroborate earlier results demonstrating the transport of leucine to be negatively influenced by high extracellular pH. pub1 is homologous to the budding yeast nitrogen permease inactivator, NPI1/RSP5, which mediates the ubiquitination and subsequent destruction of NH(4)(+)-sensitive permeases. The high-pH sensitivity of cells auxotrophic for leucine thus seems to reflect an inability of NH(4)(+)-insensitive permeases to transport sufficient leucine under conditions where the proton gradient driving nutrient transport is low, and NH(4)(+)-sensitive permeases have been destroyed. Intriguingly, the partial suppression of both high pH sensitivity, and the inactivating effect of NH(4)(+) on leucine transport, seen in pub1-1 point mutants, becomes as complete as seen in pub1Delta backgrounds when cells have concomitantly lost the function of the spc1 stress-activated MAPK.","authors":"Karagiannis J, Saleki R, Young PG","authors_abbrev":"Karagiannis J et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-08-31","publication_year":"1999","canto_session_key":"c125d6353dbf552d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-24 14:25:40","canto_approved_date":"2026-05-29 09:47:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-07 22:49:10","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11G7.02","SPAC24B11.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-10-24"},{"uniquename":"PANTHER:PTHR10927","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21C3.19","HGNC:19440"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30003614","title":"The multistress-induced Translocator protein (TSPO) differentially modulates storage lipids metabolism in seeds and seedlings.","citation":"Plant J 2018 Oct;96(2):274-286","abstract":"Translocator proteins (TSPO) are conserved membrane proteins extensively studied in mammals, but their function is still unclear. Angiosperm TSPO are transiently induced by abiotic stresses in vegetative tissues. We showed previously that constitutive expression of the Arabidopsis TSPO (AtTSPO) could be detrimental to the cell. Degradation of AtTSPO requires an active autophagy pathway. We show here that genetic modifications of TSPO expression in plant and yeast cells reduce the levels of cytoplasmic lipid droplets (LD). Transgenic Arabidopsis seedlings overexpressing AtTSPO contain less LD as compared with wild type (WT). LD levels were increased in Arabidopsis AtTSPO knockout (KO) seedlings. Deletion of the Schizosaccharomyces pombe TSPO resulted in an increase in LD level in the cell. As compared with the WT, the mutant strain was more sensitive to cerulenin, an inhibitor of fatty acids and sterol biosynthesis. We found that in contrast with seedlings, overexpression of AtTSPO (OE) resulted in an up to 50% increase in seeds fatty acids as compared with WT. A time course experiment revealed that after 4 days of seed imbibition, the levels of triacylglycerol (TAG) was still higher in the OE seeds as compared with WT or KO seeds. However, the de novo synthesis of phospholipids and TAG after 24 h of imbibition was substantially reduced in OE seeds as compared with WT or KO seeds. Our findings support a plant TSPO role in energy homeostasis in a tissue-specific manner, enhancing fatty acids and LD accumulation in mature seeds and limiting LD levels in seedlings.","doi":"10.1111/tpj.14028","authors":"Jurkiewicz P, Melser S, Maucourt M, Ayeb H, Veljanovski V, Maneta-Peyret L, Hooks M, Rolin D, Moreau P, Batoko H","authors_abbrev":"Jurkiewicz P et al.","pubmed_publication_date":"Oct 2018","pubmed_entrez_date":"2018-07-14","publication_year":"2018","canto_session_key":"24a8d08a6dd2cb25","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-07-23 09:06:46","canto_approved_date":"2025-09-03 19:06:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-21 06:18:16","canto_added_date":"2018-07-15 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-07-23"},{"uniquename":"InterPro:IPR027850","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:26319","SPBC14F5.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16291723","title":"Cell wall remodeling at the fission yeast cell division site requires the Rho-GEF Rgf3p.","citation":"J Cell Sci 2005 Dec 01;118(Pt 23):5563-73","abstract":"Cytokinesis in Schizosaccharomyces pombe is accompanied by several stages of cell wall remodeling at the division site. Coincident with actomyosin ring constriction, primary and secondary septa are deposited and then the primary septum is degraded to release daughter cells from one another. These steps require the activities of glucan synthases and glucanases, respectively, which must be coordinated with one another to prevent cell lysis. The lad1-1 mutation undergoes cell lysis specifically at cell division owing to the absence of the Rgf3p Rho1-guanine nucleotide exchange factor (GEF) at the division site. Electron microscopic analysis indicates that lysis occurs only as the primary septum begins to be degraded. Overproduction of either Rho1p or the previously uncharacterized Rab-GTPase-activating protein (GAP) involved in secretion, Gyp10p, suppresses lad1-1 lethality. Rgf3p is periodically produced in an Ace2p-dependent manner and localizes to the medial region of the cell early in mitosis, a pattern of expression distinct from the highly related Rho-GEF, Rgf1p. Although rgf1+ is not an essential gene, it is synthetically lethal with rgf2-deleted cells whereas no negative genetic interactions were detected between rgf2-deleted cells and lad1-1. Our data suggest that the three closely related fission yeast Rho-GEF molecules perform two distinct essential functions. Rgf3p appears necessary to stimulate Rho1p-mediated activation of a glucan synthase crucial after septation for proper new cell-end formation.","authors":"Morrell-Falvey JL, Ren L, Feoktistova A, Haese GD, Gould KL","authors_abbrev":"Morrell-Falvey JL et al.","pubmed_publication_date":"01 Dec 2005","pubmed_entrez_date":"2005-11-18","publication_year":"2005","canto_session_key":"bfdd2ebf8fdc9f81","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-01-05 18:17:22","canto_approved_date":"2026-01-31 12:28:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-12-29 20:07:50","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.06c","SPAC1006.06","SPCC645.07","SPBC106.20","SPAC6G10.12c","SPAC1F7.04","SPBC651.03c","SPBC16A3.01"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2022-01-05"},{"uniquename":"PMID:10880460","title":"Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast.","citation":"EMBO J 2000 Jul 03;19(13):3475-84","abstract":"A ubiquitin-like modifier, NEDD8, is covalently attached to cullin-family proteins, but its physiological role is poorly understood. Here we report that the NEDD8-modifying pathway is essential for cell viability and function of Pcu1 (cullin-1 orthologue) in fission yeast. Pcu1 assembled on SCF ubiquitin-ligase was completely modified by NEDD8. Pcu1(K713R) defective for NEDD8 conjugation lost the ability to complement lethality due to pcu1 deletion. Forced expression of Pcu1(K713R) or depletion of NEDD8 in cells resulted in impaired cell proliferation and marked stabilization of the cyclin-dependent kinase inhibitor Rum1, which is a substrate of the SCF complex. Based on these findings, we propose that covalent modification of cullin-1 by the NEDD8 system plays an essential role in the function of SCF in fission yeast.","authors":"Osaka F, Saeki M, Katayama S, Aida N, Toh-E A, Kominami K, Toda T, Suzuki T, Chiba T, Tanaka K, Kato S","authors_abbrev":"Osaka F et al.","pubmed_publication_date":"03 Jul 2000","pubmed_entrez_date":"2000-07-06","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPCC777.10c","SPBC12D12.08c","SPAC17G6.12","SPAC3A11.08","SPBC1718.01","SPAC24H6.12c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:35121625","title":"Environmental control of Pub1 (NEDD4 family E3 ligase) in  Schizosaccharomyces pombe  is regulated by TORC2 and Gsk3.","citation":"Life Sci Alliance 2022 May;5(5)","abstract":"Cells respond to changing nutrient environments by adjusting the abundance of surface nutrient transporters and receptors. This can be achieved by modulating ubiquitin-dependent endocytosis, which in part is regulated by the NEDD4 family of E3 ligases. Here we report novel regulation of Pub1, a fission yeast  Schizosaccharomyces pombe  member of the NEDD4-family of E3 ligases. We show that nitrogen stress inhibits Pub1 function, thereby increasing the abundance of the amino acid transporter Aat1 at the plasma membrane and enhancing sensitivity to the toxic arginine analogue canavanine. We show that TOR complex 2 (TORC2) signalling negatively regulates Pub1, thus TORC2 mutants under nutrient stress have decreased Aat1 at the plasma membrane and are resistant to canavanine. Inhibition of TORC2 signalling increases Pub1 phosphorylation, and this is dependent on Gsk3 activity. Addition of the Tor inhibitor Torin1 increases phosphorylation of Pub1 at serine 199 (S199) by 2.5-fold, and Pub1 protein levels in S199A phospho-ablated mutants are reduced. S199 is conserved in NEDD4 and is located immediately upstream of a WW domain required for protein interaction. Together, we describe how the major TORC2 nutrient-sensing signalling network regulates environmental control of Pub1 to modulate the abundance of nutrient transporters.","doi":"10.26508/lsa.202101082","authors":"Wang T, Woodman P, Humphrey SJ, Petersen J","authors_abbrev":"Wang T et al.","pubmed_publication_date":"May 2022","pubmed_entrez_date":"2022-02-05","publication_year":"2022","canto_session_key":"1ec7f335d8a3e517","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-02-07 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10961446","title":"The Cdc42p GTPase is targeted to the site of cell division in the fission yeast Schizosaccharomyces pombe.","citation":"Eur J Cell Biol 2000 Jul;79(7):469-77","abstract":"The Rho-family GTPase Cdc42p regulates many aspects of cell polarity and growth in eukaryotic cells, including the organization of the actin cytoskeleton. To further examine Cdc42p function in the fission yeast Schizosaccharomyces pombe, a functional green fluorescent protein (GFP)-Cdc42p fusion protein was generated. GFP-Cdc42p was observed at the medial region of the cell at the cell-division site early in cytokinesis and remained there through cell separation, and was also localized to the periphery of the cell and to internal membranes. Unexpectedly, treatment with the actin-depolymerizing drug latrunculin-A disrupted the medial region targeting pattern, and cells deficient in the actin-binding proteins tropomyosin and profilin also did not exhibit medial GFP-Cdc42p staining. In addition, medial GFP-Cdc42p localization was eliminated in a number of cytokinesis mutants, including strains defective in assembling the medial actinomyosin ring, medial ring contraction, and septum assembly. GFP-Cdc42p targeting was less affected in mutants that formed misplaced or multiple septa. These results suggest that the localization of Cdc42p at the cell-division site was dependent upon the actin cytoskeleton and that Cdc42p may function in the interdependent processes of cytokinesis and septation.","authors":"Merla A, Johnson DI","authors_abbrev":"Merla A et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-08-29","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:12569356","title":"hob1+, the fission yeast homolog of Bin1, is dispensable for endocytosis or actin organization, but required for the response to starvation or genotoxic stress.","citation":"Oncogene 2003 Feb 06;22(5):637-48","abstract":"BAR (Bin/Amphiphysin/Rvs) adapter proteins have been suggested to regulate endocytosis, actin organization, apoptosis, and transcription, but their precise roles are obscure. There are at least five mammalian genes that encode BAR adapter proteins, including the evolutionarily conserved and ubiquitously expressed Bin1/Amphiphysin-II and Bin3 genes. Bin1 holds special interest as certain splice isoforms localize to the nucleus, interact with the c-Abl and c-Myc oncoproteins, and display tumor suppressor properties. To obtain functional insights, we embarked upon a genetic analysis of the two BAR adapter proteins expressed in the fission yeast Schizosaccharomyces pombe. In a previous work, a role in actin organization and cytokinesis was identified for the Bin3 homolog hob3+. In this study, a role in stress signaling was defined for the Bin1 homolog, hob1+. Notably, hob1+ was dispensable for endocytosis, actin organization, or osmotic sensitivity. Instead, mutation of hob1+ led to slight cell elongation and faulty cell cycle arrest upon nutrient starvation. These defects were complemented by Bin1, but not by Amphiphysin-I, arguing that these genes have distinct functions despite their structural similarity. hob1 delta mutant cells were also hypersensitive to genotoxic stress. This was not related to a faulty checkpoint response, but mutation in the checkpoint gene rad3(+) further exacerbated the sensitivity of hob1 delta mutant cells. Interestingly, mutation of the cell cycle regulator wee1+ partially relieved the sensitivity defect, suggesting that hob1+ may influence the efficiency of DNA repair or checkpoint release after DNA damage. Genetic and biochemical evidence indicated that hob3+ is epistatic to hob1+ in the response to genotoxic stress. Our findings indicate that the Bin1 homolog hob1+ participates in DNA damage signaling and they suggest a novel role for BAR adapter proteins in stress response processes.","authors":"Routhier EL, Donover PS, Prendergast GC","authors_abbrev":"Routhier EL et al.","pubmed_publication_date":"06 Feb 2003","pubmed_entrez_date":"2003-02-06","publication_year":"2003","canto_session_key":"96f359bfc036b3a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-11 14:41:34","canto_approved_date":"2024-06-11 14:41:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-11 14:41:27","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC21D10.12","SPBC725.09c","SPBC216.05"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-06-11"},{"uniquename":"PMID:1735124","title":"A mating deficient and temperature-sensitive lethal mutant of Schizosaccharomyces pombe defines a new fertility locus.","citation":"Curr Genet 1992 Jan;21(1):17-22","abstract":"A recessive mutant allele, mef1-84, of a novel locus mapping on the left arm of chromosome I, between ade3 and ura1, 5 cM apart from lys5, confers temperature-sensitive growth and mating deficiency at the non-restrictive temperatures for growth. Two other mutations suppress the phenotype conferred by mef1-84: sts1-1 suppresses the temperature-sensitive growth only, and smd1-35 suppresses both temperature-sensitive growth and mating deficiency.","authors":"Rusu M","authors_abbrev":"Rusu M","pubmed_publication_date":"Jan 1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21512312","title":"Clp1p and Mid1p form links between cell cycle progression and gene expression at cytokinesis in fission yeast.","citation":"Cell Cycle 2011 Apr 15;10(8):1184-5","abstract":"","doi":"10.4161/cc.10.8.15346","authors":"McInerny CJ","authors_abbrev":"McInerny CJ","pubmed_publication_date":"15 Apr 2011","pubmed_entrez_date":"2011-04-23","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18716058","title":"Regulation of Chk1 by its C-terminal domain.","citation":"Mol Biol Cell 2008 Nov;19(11):4546-53","abstract":"Chk1 is a protein kinase that is the effector molecule in the G2 DNA damage checkpoint. Chk1 homologues have an N-terminal kinase domain, and a C-terminal domain of approximately 200 amino acids that contains activating phosphorylation sites for the ATM/R kinases, though the mechanism of activation remains unknown. Structural studies of the human Chk1 kinase domain show an open conformation; the activity of the kinase domain alone is substantially higher in vitro than full-length Chk1, and coimmunoprecipitation studies suggest the C-terminal domain may contain an autoinhibitory activity. However, we show that truncation of the C-terminal domain inactivates Chk1 in vivo. We identify additional mutations within the C-terminal domain that activate ectopically expressed Chk1 without the need for activating phosphorylation. When expressed from the endogenous locus, activated alleles show a temperature-sensitive loss of function, suggesting these mutations confer a semiactive state to the protein. Intragenic suppressors of these activated alleles cluster to regions in the catalytic domain on the face of the protein that interacts with substrate, suggesting these are the regions that interact with the C-terminal domain. Thus, rather than being an autoinhibitory domain, the C-terminus of Chk1 also contains domains critical for adopting an active configuration.","authors":"Kosoy A, O'Connell MJ","authors_abbrev":"Kosoy A et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-08-22","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-11-27 01:17:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29576528","title":"ZUFSP Deubiquitylates K63-Linked Polyubiquitin Chains to Promote Genome Stability.","citation":"Mol Cell 2018 Apr 05;70(1):165-174.e6","abstract":"Deubiquitylating enzymes (DUBs) enhance the dynamics of the versatile ubiquitin (Ub) code by reversing and regulating cellular ubiquitylation processes at multiple levels. Here we discovered that the uncharacterized human protein ZUFSP (zinc finger with UFM1-specific peptidase domain protein/C6orf113/ZUP1), which has been annotated as a potentially inactive UFM1 protease, and its fission yeast homolog Mug105 define a previously unrecognized class of evolutionarily conserved cysteine protease DUBs. Human ZUFSP selectively interacts with and cleaves long K63-linked poly-Ub chains by means of tandem Ub-binding domains, whereas it displays poor activity toward mono- or di-Ub substrates. In cells, ZUFSP is recruited to and regulates K63-Ub conjugates at genotoxic stress sites, promoting chromosome stability upon replication stress in a manner dependent on its catalytic activity. Our findings establish ZUFSP as a new type of linkage-selective cysteine peptidase DUB with a role in genome maintenance pathways.","doi":"10.1016/j.molcel.2018.02.024","authors":"Haahr P, Borgermann N, Guo X, Typas D, Achuthankutty D, Hoffmann S, Shearer R, Sixma TK, Mailand N","authors_abbrev":"Haahr P et al.","pubmed_publication_date":"05 Apr 2018","pubmed_entrez_date":"2018-03-27","publication_year":"2018","canto_session_key":"704f8fa424f73c89","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-03-28 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12447351","title":"Methyl magic and HAT tricks.","citation":"Nat Struct Biol 2002 Dec;9(12):888-91","abstract":"","authors":"Dutnall RN, Denu JM","authors_abbrev":"Dutnall RN et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2002-11-26","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8251158","title":"Rapid transformation of cryopreserved competent Schizosaccharomyces pombe cells.","citation":"Biotechniques 1993 Oct;15(4):598, 600","abstract":"","authors":"Bröker M","authors_abbrev":"Bröker M","pubmed_publication_date":"Oct 1993","pubmed_entrez_date":"1993-10-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19523829","title":"Phosphorylation state defines discrete roles for monopolin in chromosome attachment and spindle elongation.","citation":"Curr Biol 2009 Jun 23;19(12):985-95","abstract":"It is unknown how oscillations in Cdk1 activity drive the dramatic changes in chromosome and spindle dynamics that occur at the metaphase/anaphase transition.\nWe show that the Schizosaccharomyces pombe monopolin complex has distinct functions in metaphase and anaphase that are determined by the phosphorylation state of its Mde4 subunit. When Cdk1 activity is high in metaphase, Mde4 is hyperphosphorylated on Cdk1 phosphorylation sites and localizes to kinetochores. A nonphosphorylatable mutant of Mde4 does not localize to kinetochores, appears prematurely on the metaphase spindle, and interferes with spindle dynamics and chromosome segregation, illustrating the importance of Cdk1 phosphorylation in regulating metaphase monopolin activity. When Cdk1 activity drops in anaphase, dephosphorylation of Mde4 triggers monopolin localization to the mitotic spindle, where it promotes spindle elongation and integrity, coupling the late mitotic loss of Cdk1 activity to anaphase spindle dynamics.\nTogether, these findings illustrate how the sequential phosphorylation and dephosphorylation of monopolin helps ensure the orderly execution of discrete steps in mitosis.","doi":"10.1016/j.cub.2009.05.042","authors":"Choi SH, Péli-Gulli MP, Mcleod I, Sarkeshik A, Yates JR, Simanis V, McCollum D","authors_abbrev":"Choi SH et al.","pubmed_publication_date":"23 Jun 2009","pubmed_entrez_date":"2009-06-16","publication_year":"2009","canto_session_key":"2f5adb6aec169e1f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-02-24 15:37:39","canto_approved_date":"2024-04-30 05:44:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-16 15:37:07","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.04","SPBC11B10.09","SPCC1795.01c","SPBC20F10.06","SPAC1782.09c","SPCC1322.12c","SPAC11E3.03","SPBC3D6.04c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-02-24"},{"uniquename":"PMID:25658582","title":"Cell cycle control by a minimal Cdk network.","citation":"PLoS Comput Biol 2015 Feb;11(2):e1004056","abstract":"In present-day eukaryotes, the cell division cycle is controlled by a complex network of interacting proteins, including members of the cyclin and cyclin-dependent protein kinase (Cdk) families, and the Anaphase Promoting Complex (APC). Successful progression through the cell cycle depends on precise, temporally ordered regulation of the functions of these proteins. In light of this complexity, it is surprising that in fission yeast, a minimal Cdk network consisting of a single cyclin-Cdk fusion protein can control DNA synthesis and mitosis in a manner that is indistinguishable from wild type. To improve our understanding of the cell cycle regulatory network, we built and analysed a mathematical model of the molecular interactions controlling the G1/S and G2/M transitions in these minimal cells. The model accounts for all observed properties of yeast strains operating with the fusion protein. Importantly, coupling the model's predictions with experimental analysis of alternative minimal cells, we uncover an explanation for the unexpected fact that elimination of inhibitory phosphorylation of Cdk is benign in these strains while it strongly affects normal cells. Furthermore, in the strain without inhibitory phosphorylation of the fusion protein, the distribution of cell size at division is unusually broad, an observation that is accounted for by stochastic simulations of the model. Our approach provides novel insights into the organization and quantitative regulation of wild type cell cycle progression. In particular, it leads us to propose a new mechanistic model for the phenomenon of mitotic catastrophe, relying on a combination of unregulated, multi-cyclin-dependent Cdk activities.","doi":"10.1371/journal.pcbi.1004056","authors":"Gérard C, Tyson JJ, Coudreuse D, Novák B","authors_abbrev":"Gérard C et al.","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2015-02-07","publication_year":"2015","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2015-02-08 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17384198","title":"Crm1-mediated nuclear export of the Schizosaccharomyces pombe transcription factor Cuf1 during a shift from low to high copper concentrations.","citation":"Eukaryot Cell 2007 May;6(5):764-75","abstract":"In this study, we examine the fate of the nuclear pool of the Schizosaccharomyces pombe transcription factor Cuf1 in response to variations in copper levels. A nuclear pool of Cuf1-green fluorescent protein (GFP) was generated by expressing a functional cuf1(+)-GFP allele in the presence of a copper chelator. We then extinguished cuf1(+)-GFP expression and tracked the changes in the localization of the nuclear pool of Cuf1-GFP in the presence of low or high copper concentrations. Treating cells with copper as well as silver ions resulted in the nuclear export of Cuf1. We identified a leucine-rich nuclear export signal (NES), (349)LAALNHISAL(358), within the C-terminal region of Cuf1. Mutations in this sequence abrogated Cuf1 export from the nucleus. Furthermore, amino acid substitutions that impair Cuf1 NES function resulted in increased target gene expression and a concomitant cellular hypersensitivity to copper. Export of the wild-type Cuf1 protein was inhibited by leptomycin B (LMB), a specific inhibitor of the nuclear export protein Crm1. We further show that cells expressing a temperature-sensitive mutation in crm1(+) exhibit increased nuclear accumulation of Cuf1 at the nonpermissive temperature. Although wild-type Cuf1 is localized in the nucleus in both conditions, we observed that the protein can still be inactivated by copper, resulting in the repression of ctr4(+) gene expression in the presence of exogenous copper. These results demonstrate that nuclear accumulation of Cuf1 per se is not sufficient to cause the unregulated expression of the copper transport genes like ctr4(+). In addition to nuclear localization, a functional Cys-rich domain or NES element in Cuf1 is required to appropriately regulate copper transport gene expression in response to changes in intracellular copper concentration.","authors":"Beaudoin J, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-03-27","publication_year":"2007","canto_session_key":"c4bde8dec8dacbec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-28 10:40:16","canto_approved_date":"2022-02-02 16:43:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-28 10:40:10","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1393.10","SPAC1805.17","SPAC31A2.11c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2017-06-28"},{"uniquename":"PMID:1850709","title":"New vectors in fission yeast: application for cloning the his2 gene.","citation":"Gene 1991 Mar 01;99(1):47-54","abstract":"We describe a new Escherichia coli vector (pON5) that allows positive selection for recombinant clones. In this plasmid, the bla gene from pBR322 is permanently active, whereas the neo gene from transposon Tn5 is repressed by the cI-encoded lambda repressor. When DNA is inserted into the Bc/I or HindIII restriction sites situated within the cI gene, the neo gene becomes transcribed from the lambda pR promoter. We have also made a Schizosaccharomyces pombe derivative of pON5 (= pON163) by introducing the fission yeast ars1 and ura4+ sequences. We show that this plasmid is capable of transforming Sc. pombe ura4 strains, as well as ura 3 strains of the distantly related budding yeast Saccharomyces cerevisiae. We have used pON163 for the construction of two fission yeast genomic libraries. From these gene banks clones were isolated that were able to complement fission yeast his2 mutants. Such plasmids could also rescue his4C mutants of Sa. cerevisiae, defective in the histidinol dehydrogenase activity of the multifunctional HIS4 gene product. Finally, we describe the plasmid pDW232 which is useful for functional analysis of fission yeast genes. It is a pGEM3 derivative adapted to fission yeast, carrying multiple cloning sites between the T7 and SP6 promoters, together with ars1 and ura4+ from Sc. pombe.","authors":"Weilguny D, Praetorius M, Carr A, Egel R, Nielsen O","authors_abbrev":"Weilguny D et al.","pubmed_publication_date":"01 Mar 1991","pubmed_entrez_date":"1991-03-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1204651","title":"Turnover of polyadenylated messenger RNA in fission yeast. Evidence for the control of protein synthesis at the translational level.","citation":"Eur J Biochem 1975 Dec 15;60(2):477-86","abstract":"Polyadenylated RNA was isolated from fission yeast (Schizosaccharomyces pombe) total RNA using oligo(dT)-cellulose, and was studied as a model for messenger RNA. The half-life of poly adenylated RNA was measured by two independent methods. (a) The rate of labelling of polyadenylated RNA during incubation of cells with [5-3H]uridine was measured. A half-life of 40-45 min was found by comparing the experimental data with theoretical curves calculated for labelling of RNAs with various half-lives. The influence of precursor-pool specific activity on RNA labelling kinetics is considered. (b) Cells were labelled with [5-3H]uridine then further RNA synthesis was inhibited by addition of 8-hydroxyquinoline. The rate of loos of radioactivity from polyadenylated RNA indicated a half-life of 50 min. The half-life found by these two methods is about one-third of the cell doubling time, and is much longer than previous estimates by indirect methods of yeast messenger RNA half-life. Both experimental methods provided evidence for the existence of tas a half-life of 40-50 min; a much smaller population is probably turning over more rapidly. After inhibition of RNA synthesis by 8-hydroxyquinoline, the rate of total protein synthesis declined much more rapidly than the polyadenylated RNA content of the cells. However, 60 min after inhibition of RNA synthesis there was a small rise in the rate of portein synthesis. These data are interpreted as evidence for mechanisms controlling protein synthesis which operate at the level of messenger RNA translation.","authors":"Fraser RS","authors_abbrev":"Fraser RS","pubmed_publication_date":"15 Dec 1975","pubmed_entrez_date":"1975-12-15","publication_year":"1975","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18662996","title":"The DNA replication checkpoint directly regulates MBF-dependent G1/S transcription.","citation":"Mol Cell Biol 2008 Oct;28(19):5977-85","abstract":"The DNA replication checkpoint transcriptionally upregulates genes that allow cells to adapt to and survive replication stress. Our results show that, in the fission yeast Schizosaccharomyces pombe, the replication checkpoint regulates the entire G(1)/S transcriptional program by directly regulating MBF, the G(1)/S transcription factor. Instead of initiating a checkpoint-specific transcriptional program, the replication checkpoint targets MBF to maintain the normal G(1)/S transcriptional program during replication stress. We propose a mechanism for this regulation, based on in vitro phosphorylation of the Cdc10 subunit of MBF by the Cds1 replication-checkpoint kinase. Replacement of two potential phosphorylation sites with phosphomimetic amino acids suffices to promote the checkpoint transcriptional program, suggesting that Cds1 phosphorylation directly regulates MBF-dependent transcription. The conservation of MBF between fission and budding yeast, and recent results implicating MBF as a target of the budding yeast replication checkpoint, suggests that checkpoint regulation of the MBF transcription factor is a conserved strategy for coping with replication stress. Furthermore, the structural and regulatory similarity between MBF and E2F, the metazoan G(1)/S transcription factor, suggests that this checkpoint mechanism may be broadly conserved among eukaryotes.","doi":"10.1128/MCB.00596-08","authors":"Dutta C, Patel PK, Rosebrock A, Oliva A, Leatherwood J, Rhind N","authors_abbrev":"Dutta C et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-07-30","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.14","SPBC216.05","SPCC18B5.11c","SPBC336.12c"],"gene_count":4,"ltp_gene_count":3},{"uniquename":"PMID:10227167","title":"Identification of the catalase gene promoter region involved in superinduction in Schizosaccharomyces pombe caused by cycloheximide and hydrogen peroxide.","citation":"FEMS Microbiol Lett 1999 Apr 15;173(2):373-8","abstract":"Superinduction of the catalase gene was observed in Schizosaccharomyces pombe cells treated with cycloheximide and hydrogen peroxide. The promoter analysis of the catalase gene revealed that element A (the region from -111 to -90, numbered with the transcription start site as +1), involved in the induction of the gene under oxidative stress, was required for superinduction by hydrogen peroxide and cycloheximide. Although Atf1 is a transcription factor responsible for the induction of the catalase gene by several stresses, a disruptant of atf1 exhibited superinduction. Moreover, in a deletion mutant that lacks element A but has an Atf1 binding site, the cells treated with hydrogen peroxide and cycloheximide expressed as much catalase mRNA as those treated with hydrogen peroxide alone. This suggests that cycloheximide does not stabilize the catalase mRNA but enhances the transcription via element A. Staurosporine, a strong inhibitor of protein phosphorylation, did not inhibit superinduction.","authors":"Nakagawa CW, Yamada K, Mutoh N","authors_abbrev":"Nakagawa CW et al.","pubmed_publication_date":"15 Apr 1999","pubmed_entrez_date":"1999-05-05","publication_year":"1999","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1915277","title":"A novel switch-activating site (SAS1) and its cognate binding factor (SAP1) required for efficient mat1 switching in Schizosaccharomyces pombe.","citation":"EMBO J 1991 Oct;10(10):3025-32","abstract":"The pattern of parental DNA strand inheritance at the mating type locus (mat1) determines the pattern of mat1 switching in a cell lineage by regulating the formation of the site-specific double-stranded break (DSB) required for mating type interconversion in Schizosaccharomyces pombe. To study the molecular basis of this programmable cell type change, we conducted structural and functional analyses of the DNA sequence flanking the DSB at mat1. We have identified and characterized a DNA-binding activity that interacts with a specific sequence located 140 bp from the DSB site. Deletion analysis of DNA sequences located distal to mat1 cassette revealed the presence of at least two switch-activating sites (SAS1 and SAS2), both of which are required for generating an efficient level of DSBs and consequently, for efficient switching. We found that SAS1 overlaps with the target site of the DNA-binding activity called SAP1 (for switch-activating protein). Point mutations generated in the SAS1 element that adversely affect binding of SAP1 protein in vitro were found to reduce the efficiency of switching in vivo, suggesting the requirement of SAP1 for switching. Pedigree analysis revealed that SAS1 is equally required for initial switching (one switch in four grand-daughters of a cell) and for consecutive switching (where the sister of a recently switched cell switches again), indicating that the two developmentally asymmetric cell divisions required to generate a particular pattern of switching share the same molecular control mechanism.","authors":"Arcangioli B, Klar AJ","authors_abbrev":"Arcangioli B et al.","pubmed_publication_date":"Oct 1991","pubmed_entrez_date":"1991-10-01","publication_year":"1991","canto_session_key":"8c8265c05538c545","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-28 16:55:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-23 14:00:49","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-23"},{"uniquename":"PMID:41251311","title":"Nuclear enlargement induced by overexpression of nuclear export signal is associated with abnormal nuclear division in Schizosaccharomyces pombe.","citation":"Biol Open 2025 Nov 18;","abstract":"The size of the nucleus is tightly coordinated with cell size across eukaryotes, yet the physiological significance of maintaining proper nuclear dimensions remains poorly understood. Here, we investigate how nuclear size dysregulation resulting from perturbed nucleocytoplasmic transport affects mitotic fidelity in Schizosaccharomyces pombe. Overexpression of a GFP-tagged nuclear export signal (NES-GFP) induces nuclear expansion, leading to severe growth defects and frequent errors in chromosome segregation during mitosis. Live-cell imaging revealed that enlarged nuclei underwent delayed mitotic progression and abnormal nuclear division. Strikingly, genetic suppression of nuclear expansion alleviated these defects, whereas enhancement of nuclear size exacerbated them. Together, these findings suggest that maintaining proper nuclear dimensions contributes to accurate chromosome segregation, although additional effects of NES-GFP overproduction and other factors influencing nuclear size should be further examined.","doi":"10.1242/bio.062331","authors":"Fujimoto T, Watanabe S, Imamura Y, Mizunuma M, Kume K","authors_abbrev":"Fujimoto T et al.","pubmed_publication_date":"18 Nov 2025","pubmed_entrez_date":"2025-11-18","publication_year":"2025","canto_session_key":"151b9837644df7ff","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-11-19 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32755595","title":"A Structure-Based Mechanism for DNA Entry into the Cohesin Ring.","citation":"Mol Cell 2020 Sep 17;79(6):917-933.e9","abstract":"Despite key roles in sister chromatid cohesion and chromosome organization, the mechanism by which cohesin rings are loaded onto DNA is still unknown. Here we combine biochemical approaches and cryoelectron microscopy (cryo-EM) to visualize a cohesin loading intermediate in which DNA is locked between two gates that lead into the cohesin ring. Building on this structural framework, we design experiments to establish the order of events during cohesin loading. In an initial step, DNA traverses an N-terminal kleisin gate that is first opened upon ATP binding and then closed as the cohesin loader locks the DNA against the ATPase gate. ATP hydrolysis will lead to ATPase gate opening to complete DNA entry. Whether DNA loading is successful or results in loop extrusion might be dictated by a conserved kleisin N-terminal tail that guides the DNA through the kleisin gate. Our results establish the molecular basis for cohesin loading onto DNA.","doi":"10.1016/j.molcel.2020.07.013","authors":"Higashi TL, Eickhoff P, Sousa JS, Locke J, Nans A, Flynn HR, Snijders AP, Papageorgiou G, O'Reilly N, Chen ZA, O'Reilly FJ, Rappsilber J, Costa A, Uhlmann F","authors_abbrev":"Higashi TL et al.","pubmed_publication_date":"17 Sep 2020","pubmed_entrez_date":"2020-08-07","publication_year":"2020","canto_session_key":"1b6d5c7f5b74e301","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-08-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.04","SPAC31A2.05c","SPCC338.17c","SPAC10F6.09c"],"gene_count":4,"ltp_gene_count":4,"pdb_entries":[{"pdb_id":"6yuf","gene_chains":[{"gene_uniquename":"SPAC10F6.09c","chain":"C","position":"1-1194"},{"gene_uniquename":"SPBC29A10.04","chain":"A","position":"1-1228"},{"gene_uniquename":"SPCC338.17c","chain":"B","position":"1-628"},{"gene_uniquename":"SPAC31A2.05c","chain":"D","position":"1-1587"}],"title":"Cohesin complex with loader gripping DNA","entry_authors":"Higashi TL,Eickhoff P,Sousa JS,Costa A,Uhlmann F","entry_authors_abbrev":"Higashi TL et al.","reference_uniquename":"PMID:32755595","experimental_method":"EM","resolution":"3.94"}]},{"uniquename":"PMID:31262821","title":"Replication fork stalling elicits chromatin compaction for the stability of stalling replication forks.","citation":"Proc Natl Acad Sci U S A 2019 Jul 16;116(29):14563-14572","abstract":"DNA replication forks in eukaryotic cells stall at a variety of replication barriers. Stalling forks require strict cellular regulations to prevent fork collapse. However, the mechanism underlying these cellular regulations is poorly understood. In this study, a cellular mechanism was uncovered that regulates chromatin structures to stabilize stalling forks. When replication forks stall, H2BK33, a newly identified acetylation site, is deacetylated and H3K9 trimethylated in the nucleosomes surrounding stalling forks, which results in chromatin compaction around forks. Acetylation-mimic H2BK33Q and its deacetylase  clr6 - 1  mutations compromise this fork stalling-induced chromatin compaction, cause physical separation of replicative helicase and DNA polymerases, and significantly increase the frequency of stalling fork collapse. Furthermore, this fork stalling-induced H2BK33 deacetylation is independent of checkpoint. In summary, these results suggest that eukaryotic cells have developed a cellular mechanism that stabilizes stalling forks by targeting nucleosomes and inducing chromatin compaction around stalling forks. This mechanism is named the \"Chromsfork\" control: Chromatin Compaction Stabilizes Stalling Replication Forks.","doi":"10.1073/pnas.1821475116","authors":"Feng G, Yuan Y, Li Z, Wang L, Zhang B, Luo J, Ji J, Kong D","authors_abbrev":"Feng G et al.","pubmed_publication_date":"16 Jul 2019","pubmed_entrez_date":"2019-07-03","publication_year":"2019","canto_session_key":"9da79dd548ac369e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Gang Feng","canto_first_approved_date":"2026-01-19 09:44:48","canto_approved_date":"2026-02-26 16:38:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-11-04 03:47:57","canto_added_date":"2020-04-04 00:15:04","annotation_curators":[{"name":"Gang Feng","community_curator":true,"annotation_count":31,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":39,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC132.02","SPAC664.07c","SPBC216.05","SPCC1259.13","SPCC622.09","SPAC3G9.07c","SPBC25D12.03c","SPAC1952.07","SPBC36.05c","SPCC18B5.11c","SPBC16D10.07c","SPAC20G4.04c","SPAC17D4.02","SPCC23B6.03c","SPAC1783.04c","SPBC800.03"],"gene_count":16,"ltp_gene_count":14,"approved_date":"2026-01-19"},{"uniquename":"PMID:31805521","title":"Set1/COMPASS repels heterochromatin invasion at euchromatic sites by disrupting Suv39/Clr4 activity and nucleosome stability.","citation":"Genes Dev 2020 Jan 01;34(1-2):99-117","abstract":"Protection of euchromatin from invasion by gene-repressive heterochromatin is critical for cellular health and viability. In addition to constitutive loci such as pericentromeres and subtelomeres, heterochromatin can be found interspersed in gene-rich euchromatin, where it regulates gene expression pertinent to cell fate. While heterochromatin and euchromatin are globally poised for mutual antagonism, the mechanisms underlying precise spatial encoding of heterochromatin containment within euchromatic sites remain opaque. We investigated ectopic heterochromatin invasion by manipulating the fission yeast mating type locus boundary using a single-cell spreading reporter system. We found that heterochromatin repulsion is locally encoded by Set1/COMPASS on certain actively transcribed genes and that this protective role is most prominent at heterochromatin islands, small domains interspersed in euchromatin that regulate cell fate specifiers. Sensitivity to invasion by heterochromatin, surprisingly, is not dependent on Set1 altering overall gene expression levels. Rather, the gene-protective effect is strictly dependent on Set1's catalytic activity. H3K4 methylation, the Set1 product, antagonizes spreading in two ways: directly inhibiting catalysis by Suv39/Clr4 and locally disrupting nucleosome stability. Taken together, these results describe a mechanism for spatial encoding of euchromatic signals that repel heterochromatin invasion.","doi":"10.1101/gad.328468.119","authors":"Greenstein RA, Barrales RR, Sanchez NA, Bisanz JE, Braun S, Al-Sady B","authors_abbrev":"Greenstein RA et al.","pubmed_publication_date":"01 Jan 2020","pubmed_entrez_date":"2019-12-06","publication_year":"2020","canto_session_key":"86c15aae088c3ccc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11854402","title":"Essential role of MCM proteins in premeiotic DNA replication.","citation":"Mol Biol Cell 2002 Feb;13(2):435-44","abstract":"A critical event in eukaryotic DNA replication involves association of minichromosome maintenance (MCM2-7) proteins with origins, to form prereplicative complexes (pre-RCs) that are competent for initiation. The ability of mutants defective in MCM2-7 function to complete meiosis had suggested that pre-RC components could be irrelevant to premeiotic S phase. We show here that MCM2-7 proteins bind to chromatin in fission yeast cells preparing for meiosis and during premeiotic S phase in a manner suggesting they in fact are required for DNA replication in the meiotic cycle. This is confirmed by analysis of a degron mcm4 mutant, which cannot carry out premeiotic DNA replication. Later in meiosis, Mcm4 chromatin association is blocked between meiotic nuclear divisions, presumably accounting for the absence of a second round of DNA replication. Together, these results emphasize similarity between replication mechanisms in mitotic and meiotic cell cycles.","authors":"Lindner K, Gregán J, Montgomery S, Kearsey SE","authors_abbrev":"Lindner K et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-02-21","publication_year":"2002","canto_session_key":"7097a362b55929af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-12 14:31:37","canto_approved_date":"2024-11-14 09:29:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-13 14:17:47","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPBC4.04c","SPBC211.04c","SPBC19C2.05","SPBC25D12.03c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2015-06-12"},{"uniquename":"PMID:22344694","title":"The transcription factors Pap1 and Prr1 collaborate to activate antioxidant, but not drug tolerance, genes in response to H2O2.","citation":"Nucleic Acids Res 2012 Jun;40(11):4816-24","abstract":"In response to hydrogen peroxide (H(2)O(2)), the transcription factor Pap1 from Schizosaccharomyces pombe regulates transcription of genes required for adaptation to oxidative stress and for tolerance to toxic drugs. H(2)O(2) induces oxidation of Pap1, its nuclear accumulation and expression of more than fifty Pap1-dependent genes. Oxidation and nuclear accumulation of Pap1 can also be accomplished by genetic inhibition of thioredoxin reductase. Furthermore, genetic alteration of the nuclear export pathway, or mutations in Pap1 nuclear export signal trigger nuclear accumulation of reduced Pap1. We show here that a subset of Pap1-dependent genes, such as those coding for the efflux pump Caf5, the ubiquitin-like protein Obr1 or the dehydrogenase SPCC663.08c, only require nuclear Pap1 for activation, whereas another subset of genes, those coding for the antioxidants catalase, sulfiredoxin or thioredoxin reductase, do need oxidized Pap1 to form a heterodimer with the constitutively nuclear transcription factor Prr1. The ability of Pap1 to bind and activate drug tolerance promoters is independent on Prr1, whereas its affinity for the antioxidant promoters is significantly enhanced upon association with Prr1. This finding suggests that the activation of both antioxidant and drug resistance genes in response to oxidative stress share a common inducer, H(2)O(2), but alternative effectors.","doi":"10.1093/nar/gks141","authors":"Calvo IA, García P, Ayté J, Hidalgo E","authors_abbrev":"Calvo IA et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2012-02-21","publication_year":"2012","canto_session_key":"edf9edf5b9dffcea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elena Hidalgo","canto_first_approved_date":"2017-09-14 13:18:11","canto_approved_date":"2022-06-01 15:05:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-05 15:50:50","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":71,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Elena Hidalgo","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.14","SPBC609.04","SPAC1783.07c","SPAC3C7.14c","SPCC663.08c","SPCC576.03c","SPCC757.07c","SPBC365.13c","SPBC3F6.03","SPBC29B5.01","SPBC13G1.13","SPBC106.02c"],"gene_count":12,"ltp_gene_count":6,"approved_date":"2017-09-14"},{"uniquename":"PMID:10512862","title":"Requirement of sequences outside the conserved kinase domain of fission yeast Rad3p for checkpoint control.","citation":"Mol Biol Cell 1999 Oct;10(10):3223-38","abstract":"The fission yeast Rad3p checkpoint protein is a member of the phosphatidylinositol 3-kinase-related family of protein kinases, which includes human ATMp. Mutation of the ATM gene is responsible for the disease ataxia-telangiectasia. The kinase domain of Rad3p has previously been shown to be essential for function. Here, we show that although this domain is necessary, it is not sufficient, because the isolated kinase domain does not have kinase activity in vitro and cannot complement a rad3 deletion strain. Using dominant negative alleles of rad3, we have identified two sites N-terminal to the conserved kinase domain that are essential for Rad3p function. One of these sites is the putative leucine zipper, which is conserved in other phosphatidylinositol 3-kinase-related family members. The other is a novel motif, which may also mediate Rad3p protein-protein interactions.","authors":"Chapman CR, Evans ST, Carr AM, Enoch T","authors_abbrev":"Chapman CR et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-10-08","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05","SPCC1259.13"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7802705","title":"Dnacin A1 and dnacin B1 are antitumor antibiotics that inhibit cdc25B phosphatase activity.","citation":"Biochem Pharmacol 1994 Nov 29;48(11):2139-41","abstract":"The p80cdc25 protein is a protein phosphatase directly involved in p34cdc2 protein kinase activation by dephosphorylation. The cdc25B gene is one of three human cdc25 homologs which can complement the temperature-sensitive cdc25 mutation of Schizosaccharomyces pombe, and is expressed a high levels in human cell lines, particularly in some cancer cells. A fusion protein of glutathione-S-transferase (GST) and the catalytic domain of cdc25B protein was constructed and found to retain phosphatase activity in the manner of a p80cdc25 phosphatase by using a chromogenic substrate, p-nitrophenylphosphate. Two benzoquinoid antitumor compounds, dnacin A1 and dnacin B1, inhibited phosphatase activity in a non-competitive manner.","authors":"Horiguchi T, Nishi K, Hakoda S, Tanida S, Nagata A, Okayama H","authors_abbrev":"Horiguchi T et al.","pubmed_publication_date":"29 Nov 1994","pubmed_entrez_date":"1994-11-29","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39527194","title":"Analysis of Cell Wall Mechanics in Fission Yeast.","citation":"Methods Mol Biol 2025;2862:77-91","abstract":"The growth and shape of fungal cells, such as fission yeast, are strongly constrained by the mechanics of their cell wall (CW). The cell wall encases the plasma membrane and defines instantaneous cell shapes by opposing turgor pressure-derived stress on the cell surface. Measuring cell wall mechanical properties may thus bring key insights into the regulation of cell morphogenesis, cell growth, but also cell surface integrity and survival. The fission yeast cell wall has a thickness of a few tens to hundreds of nanometers, and bulk elasticity similar to that of rubber (tens of MPa). These mechanical properties vary locally around single cells, for instance, at the new vs. old growing ends, or birth scars, and may also largely depend on growth conditions and life cycle phases. While cell wall thickness and mechanics have been traditionally measured by complex methodologies including electron microscopy and atomic force microscopy, we here propose a method based on light microscopy to infer with medium-throughput cell wall mechanical properties, as well as turgor pressure in time and space in living cells. This analysis will enhance our appreciation of the mechanical regulation of fission yeast cell morphogenesis and may be directly transferable to the study of other fungal cells.","doi":"10.1007/978-1-0716-4168-2_6","authors":"Reignier Y, Minc N","authors_abbrev":"Reignier Y et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3076287","title":"Intersecting cell cycles.","citation":"Trends Genet 1988 Oct;4(10):275-6","abstract":"","authors":"Fantes P","authors_abbrev":"Fantes P","pubmed_publication_date":"Oct 1988","pubmed_entrez_date":"1988-10-01","publication_year":"1988","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1421165","title":"Genetic analysis of ras homologs in yeasts.","citation":"Semin Cancer Biol 1992 Aug;3(4):209-18","abstract":"Ras proteins with extensive structural homology to mammalian p21ras have been studied in the two yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Comparative analysis of these two yeasts has revealed significant differences in the biochemical and physiological functions that are controlled by this subgroup of eukaryotic GTP-binding regulatory proteins. Despite such divergence of cellular functions, proteins and mechanisms involved in the regulation and modification of Ras proteins are highly conserved in yeasts and other eukaryotes. Genetic analysis of the function of yeast proteins that regulate or modify Ras proteins has provided important information about Ras proteins in general.","authors":"Powers S","authors_abbrev":"Powers S","pubmed_publication_date":"Aug 1992","pubmed_entrez_date":"1992-08-01","publication_year":"1992","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10564266","title":"Cell cycle-regulated transcription in fission yeast: Cdc10-Res protein interactions during the cell cycle and domains required for regulated transcription.","citation":"Mol Biol Cell 1999 Nov;10(11):3705-15","abstract":"In Schizosaccharomyces pombe the MBF (DSC1) complex mediates transcriptional activation at Start and is composed of a common subunit called Cdc10 in combination with two alternative DNA-binding partners, Res1 and Res2. It has been suggested that a high-activity MBF complex (at G1/S) is switched to a low-activity complex (in G2) by the incorporation of the negative regulatory subunit Res2. We have analyzed MBF protein-protein interactions and find that both Res proteins are associated with Cdc10 throughout the cell cycle, arguing against this model. Furthermore we demonstrate that Res2 is capable of interacting with a mutant form of Cdc10 that has high transcriptional activity. It has been shown previously that both Res proteins are required for periodic cell cycle-regulated transcription. Therefore a series of Res1-Res2 hybrid molecules was used to determine the domains that are specifically required to regulate periodic transcription. In Res2 the nature of the C-terminal region is critical, and in both Res1 and Res2, a domain overlapping the N-terminal ankyrin repeat and a recently identified activation domain is important for mediating cell cycle-regulated transcription.","authors":"Whitehall S, Stacey P, Dawson K, Jones N","authors_abbrev":"Whitehall S et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-11-17","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F3.09c","SPBC725.16","SPBC336.12c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:1655700","title":"Phosphatidylglycerolphosphate synthase expression in Schizosaccharomyces pombe is regulated by the phospholipid precursors inositol and choline.","citation":"J Bacteriol 1991 Oct;173(19):6132-8","abstract":"The enzyme phosphatidylglycerolphosphate synthase (PGPS; CDP-diacylglycerol glycerol 3-phosphate 3-phosphatidyltransferase; EC 2.7.8.5) catalyzes the committed step in the cardiolipin biosynthetic pathway. To study the regulation of PGPS in Schizosaccharomyces pombe, we characterized the enzyme biochemically. Maximum activity occurred in the presence of 6 mM Triton X-100 at pH 7.5. The apparent Km values for CDP-diacylglycerol and glycerol 3-phosphate were 130 and 26 microM, respectively. Optimal activity was at 35 degrees C, and enzyme activity was labile above 40 degrees C. Thioreactive agents were inhibitory to PGPS activity. To determine whether S. pombe PGPS is regulated by phospholipid precursors, we examined the time-dependent expression of PGPS upon inositol and choline starvation. Starvation for inositol resulted in a threefold increase in PGPS expression in wild-type cells. In cho1 and cho2 mutants, which are blocked in phosphatidylcholine synthesis, starvation for choline resulted in transient derepression of PGPS expression. In choline auxotrophs starved for inositol, PGPS was derepressed 2.5- to 3-fold in the presence of choline and less or not at all in the absence of choline. This is the first description of PGPS regulation in S. pombe and the first demonstration of inositol-mediated regulation in the inositol-requiring yeast species.","authors":"Karkhoff-Schweizer RR, Kelly BL, Greenberg ML","authors_abbrev":"Karkhoff-Schweizer RR et al.","pubmed_publication_date":"Oct 1991","pubmed_entrez_date":"1991-10-01","publication_year":"1991","canto_session_key":"a875c813b300d3ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:44:18","canto_session_submitted_date":"2012-02-27 11:08:23","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:37939086","title":"Structure and function of the  S. pombe  III-IV-cyt  c  supercomplex.","citation":"Proc Natl Acad Sci U S A 2023 Nov 14;120(46):e2307697120","abstract":"The respiratory chain in aerobic organisms is composed of a number of membrane-bound protein complexes that link electron transfer to proton translocation across the membrane. In mitochondria, the final electron acceptor, complex IV (CIV), receives electrons from dimeric complex III (CIII 2 ), via a mobile electron carrier, cytochrome  c . In the present study, we isolated the CIII 2 CIV supercomplex from the fission yeast  Schizosaccharomyces pombe  and determined its structure with bound cyt.  c  using single-particle electron cryomicroscopy. A respiratory supercomplex factor 2 was found to be bound at CIV distally positioned in the supercomplex. In addition to the redox-active metal sites, we found a metal ion, presumably Zn 2+ , coordinated in the CIII subunit Cor1, which is encoded by the same gene ( qcr  1 ) as the mitochondrial-processing peptidase subunit β. Our data show that the isolated CIII 2 CIV supercomplex displays proteolytic activity suggesting a dual role of CIII 2  in  S. pombe . As in the supercomplex from  S. cerevisiae , subunit Cox5 of CIV faces towards one CIII monomer, but in  S. pombe,  the two complexes are rotated relative to each other by ~45°. This orientation yields equal distances between the cyt.  c  binding sites at CIV and at each of the two CIII monomers. The structure shows cyt.  c  bound at four positions, but only along one of the two symmetrical branches. Overall, this combined structural and functional study reveals the integration of peptidase activity with the CIII 2  respiratory system and indicates a two-dimensional cyt.  c  diffusion mechanism within the CIII 2 -CIV supercomplex.","doi":"10.1073/pnas.2307697120","authors":"Moe A, Dimogkioka AR, Rapaport D, Öjemyr LN, Brzezinski P","authors_abbrev":"Moe A et al.","pubmed_publication_date":"14 Nov 2023","pubmed_entrez_date":"2023-11-08","publication_year":"2023","canto_session_key":"f4afedf4b8f5c28e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-11-09 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC338.10c","SPBC16H5.06","SPBC16C6.08c","SPMIT.01","SPAC1782.07","SPCC1682.01","SPCC613.10","SPBC2F12.17","SPMIT.04","SPCC1259.05c","SPBC29A3.18","SPMIT.11","SPCC1442.08c","SPCC737.02c","SPMIT.05","SPAC1296.02","SPAC1565.01","SPAC24C9.16c","SPBP4H10.08","SPCC1739.09c","SPBP23A10.15c","SPAC1B2.04"],"gene_count":22,"ltp_gene_count":22,"pdb_entries":[{"pdb_id":"8q1b","gene_chains":[{"gene_uniquename":"SPBC2F12.17","chain":"g","position":"1-59"},{"gene_uniquename":"SPBC16C6.08c","chain":"F/Q","position":"1-214"},{"gene_uniquename":"SPBC29A3.18","chain":"D/O","position":"1-307"},{"gene_uniquename":"SPCC1682.01","chain":"I/T","position":"1-67"},{"gene_uniquename":"SPCC1739.09c","chain":"k","position":"1-130"},{"gene_uniquename":"SPCC737.02c","chain":"G/R","position":"1-137"},{"gene_uniquename":"SPCC338.10c","chain":"e","position":"1-186"},{"gene_uniquename":"SPCC1442.08c","chain":"j","position":"1-86"},{"gene_uniquename":"SPCC1259.05c","chain":"i","position":"1-58"},{"gene_uniquename":"SPMIT.05","chain":"C/N","position":"1-387"},{"gene_uniquename":"SPMIT.01","chain":"a","position":"1-537"},{"gene_uniquename":"SPMIT.04","chain":"c","position":"1-269"},{"gene_uniquename":"SPMIT.11","chain":"b","position":"1-248"},{"gene_uniquename":"SPAC1782.07","chain":"H/S","position":"1-92"},{"gene_uniquename":"SPCC613.10","chain":"B/M","position":"1-426"},{"gene_uniquename":"SPAC1296.02","chain":"d","position":"1-159"},{"gene_uniquename":"SPBC16H5.06","chain":"E/P","position":"1-228"},{"gene_uniquename":"SPAC1565.01","chain":"l","position":"1-242"},{"gene_uniquename":"SPAC24C9.16c","chain":"h","position":"1-66"},{"gene_uniquename":"SPBP4H10.08","chain":"J/U","position":"1-79"},{"gene_uniquename":"SPBP23A10.15c","chain":"A/L","position":"1-457"},{"gene_uniquename":"SPAC1B2.04","chain":"f","position":"1-140"}],"title":"III2-IV1 respiratory supercomplex from S. pombe","entry_authors":"Moe A,Brzezinski P","entry_authors_abbrev":"Moe A et al.","reference_uniquename":"PMID:37939086","experimental_method":"EM","resolution":"3.4"}]},{"uniquename":"PMID:30600396","title":"Spatiotemporal regulation of the Dma1-mediated mitotic checkpoint coordinates mitosis with cytokinesis.","citation":"Curr Genet 2019 Jun;65(3):663-668","abstract":"During cell division, the timing of mitosis and cytokinesis must be ordered to ensure that each daughter cell receives a complete, undamaged copy of the genome. In fission yeast, the septation initiation network (SIN) is responsible for this coordination, and a mitotic checkpoint dependent on the E3 ubiquitin ligase Dma1 and the protein kinase CK1 controls SIN signaling to delay cytokinesis when there are errors in mitosis. The participation of kinases and ubiquitin ligases in cell cycle checkpoints that maintain genome integrity is conserved from yeast to human, making fission yeast an excellent model system in which to study checkpoint mechanisms. In this review, we highlight recent advances and remaining questions related to checkpoint regulation, which requires the synchronized modulation of protein ubiquitination, phosphorylation, and subcellular localization.","doi":"10.1007/s00294-018-0921-x","authors":"Cullati SN, Gould KL","authors_abbrev":"Cullati SN et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-01-03","publication_year":"2019","canto_session_key":"cd71adde23af09c0","canto_annotation_status":"APPROVED","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_first_approved_date":"2026-03-05 07:07:46","canto_approved_date":"2026-03-05 07:07:46","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-03-04 16:04:59","canto_added_date":"2019-01-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G8.10c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2026-03-05"},{"uniquename":"PMID:31582398","title":"Cortical tethering of mitochondria by the anchor protein Mcp5 enables uniparental inheritance.","citation":"J Cell Biol 2019 Nov 04;218(11):3560-3571","abstract":"During sexual reproduction in eukaryotes, processes such as active degradation and dilution of paternal mitochondria ensure maternal mitochondrial inheritance. In the isogamous organism fission yeast, we employed high-resolution fluorescence microscopy to visualize mitochondrial inheritance during meiosis by differentially labeling mitochondria of the two parental cells. Remarkably, mitochondria, and thereby mitochondrial DNA from the parental cells, did not mix upon zygote formation but remained segregated at the poles by attaching to clusters of the anchor protein Mcp5 via its coiled-coil domain. We observed that this tethering of parental mitochondria to the poles results in uniparental inheritance of mitochondria, wherein two of the four spores formed subsequently contained mitochondria from one parent and the other spores contained mitochondria from the other parent. Further, the presence of dynein on an Mcp5 cluster precluded the attachment of mitochondria to the same cluster. Taken together, we reveal a distinct mechanism that achieves uniparental inheritance by segregation of parental mitochondria.","doi":"10.1083/jcb.201901108","authors":"Chacko LA, Mehta K, Ananthanarayanan V","authors_abbrev":"Chacko LA et al.","pubmed_publication_date":"04 Nov 2019","pubmed_entrez_date":"2019-10-05","publication_year":"2019","canto_session_key":"2ac0f6929f53ddce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Leeba Ann Chacko","canto_first_approved_date":"2020-03-24 09:36:35","canto_approved_date":"2022-03-17 18:07:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-12 09:26:47","canto_added_date":"2019-10-06 00:15:04","annotation_curators":[{"name":"Leeba Ann Chacko","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.02","SPAC1093.06c","SPBC25B2.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-03-24"},{"uniquename":"EMBL:AU012111","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15213253","title":"DNA damage checkpoint maintenance through sustained Chk1 activity.","citation":"J Cell Sci 2004 Jul 15;117(Pt 16):3489-98","abstract":"The G2 DNA damage checkpoint prevents mitotic entry in the presence of DNA damage. This requires the activation of the phosphoinositide-3-kinase-related protein kinases ATR and ATM in human cells and the ATR homologue Rad3 in the fission yeast Schizosaccharomyces pombe. Rad3 activates the effector protein kinase Chk1 by phosphorylation. However, in fission yeast, inactivation of Rad3 following checkpoint activation has no impact on checkpoint duration. This demonstrates that Rad3 is not required for checkpoint maintenance and that the processes of checkpoint initiation and maintenance are distinct. Chk1 is required for checkpoint initiation but its role in checkpoint maintenance has not been investigated. We show here that Chk1 kinase activity is rapidly induced following irradiation and is maintained for the duration of a checkpoint arrest. On entry to mitosis, there is a transient decrease in Chk1 activity and phosphorylation, but Chk1 activity remains higher than that observed in unirradiated cells. We have generated temperature-sensitive alleles of chk1, which phenocopy chk1 deletion at the non-permissive temperature. Using these alleles, we have shown that inactivation of Chk1 during a checkpoint arrest leads to premature checkpoint termination, resulting in catastrophic mitoses that are a hallmark of checkpoint failure. Therefore, unlike Rad3, Chk1 is an important determinant of both checkpoint initiation and maintenance.","authors":"Latif C, den Elzen NR, O'Connell MJ","authors_abbrev":"Latif C et al.","pubmed_publication_date":"15 Jul 2004","pubmed_entrez_date":"2004-06-24","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11715016","title":"Mrc1 transduces signals of DNA replication stress to activate Rad53.","citation":"Nat Cell Biol 2001 Nov;3(11):958-65","abstract":"Cells experiencing DNA replication stress activate a response pathway that delays entry into mitosis and promotes DNA repair and completion of DNA replication. The protein kinases ScRad53 and SpCds1 (in baker's and fission yeast, respectively) are central to this pathway. We describe a conserved protein Mrc1, mediator of the replication checkpoint, required for activation of ScRad53 and SpCds1 during replication stress. mrc1 mutants are sensitive to hydroxyurea and have a checkpoint defect similar to rad53 and cds1 mutants. Mrc1 may be the replicative counterpart of Rad9 and Crb2, which are required for activating ScRad53 and Chk1 in response to DNA damage.","authors":"Alcasabas AA, Osborn AJ, Bachant J, Hu F, Werler PJ, Bousset K, Furuya K, Diffley JF, Carr AM, Elledge SJ","authors_abbrev":"Alcasabas AA et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2001-11-21","publication_year":"2001","canto_session_key":"fa2d5cdf7c915314","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-03-21 12:19:05","canto_approved_date":"2021-01-05 15:28:18","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-03-21 12:19:39","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC694.06c","SPCC1259.13","SPCC18B5.11c","HGNC:19715","SPBC216.05","SPBC342.05"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2018-03-21"},{"uniquename":"PMID:15615784","title":"Nak1 interacts with Hob1 and Wsp1 to regulate cell growth and polarity in Schizosaccharomyces pombe.","citation":"J Cell Sci 2005 Jan 01;118(Pt 1):199-210","abstract":"We have previously reported that Nak1, a group-II germinal center (GC) kinase, is essential for polarized growth in Schizosaccharomyces pombe. Here, we provide evidence that Nak1 regulates cell growth and polarity, in part, through its interactions with Hob1 (an Rvs167/amphiphysin homolog) and Wsp1 (Wiskott-Aldrich-syndrome-protein homolog). We found that Nak1, Hob1 and Wsp1 interact physically, and that both Hob1/green-fluorescent-protein (Hob1-GFP) and Wsp1-GFP fusion proteins localized to F-actin patches at growing cell ends and medial division sites. Hob1-GFP was dissociated from patches in cells lacking Wsp1. Also, Hob1 overexpression dissociated Wsp1-GFP from foci, inhibited Wsp1-directed F-actin formation in vitro and partially restored polarity defects associated with Wsp1 overexpression or nak1 repression. Furthermore, loss of both Wsp1 and Hob1 resulted in rounded cells, slow growth and multiple septae. Together, these observations suggest that Hob1 and Wsp1 cooperate to mediate cell polarity, growth and division. Repression of nak1 resulted in a random redistribution of Hob1-GFP and Wsp1-GFP foci, and inhibition of Wsp1-directed F-actin formation in vitro. Furthermore, hob1delta and wsp1delta mutants exhibited synthetic growth defects in combination with nak1 repression, suggesting that Nak1 has redundant functions with Hob1 and Wsp1. Collectively, our results suggest that Nak1 both regulates and cooperates with Hob1 and Wsp1 to promote F-actin formation and polarized cell growth.","authors":"Huang TY, Renaud-Young M, Young D","authors_abbrev":"Huang TY et al.","pubmed_publication_date":"01 Jan 2005","pubmed_entrez_date":"2004-12-24","publication_year":"2005","canto_session_key":"4a75629ac3e4b424","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-20 15:42:12","canto_approved_date":"2022-10-04 14:08:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-20 15:41:52","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":67,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21D10.12","SPBC17F3.02","SPAC4F10.15c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-07-20"},{"uniquename":"PMID:26215567","title":"A novel 3' splice site recognition by the two zinc fingers in the U2AF small subunit.","citation":"Genes Dev 2015 Aug 01;29(15):1649-60","abstract":"The pre-mRNA splicing reaction of eukaryotic cells has to be carried out extremely accurately, as failure to recognize the splice sites correctly causes serious disease. The small subunit of the U2AF heterodimer is essential for the determination of 3' splice sites in pre-mRNA splicing, and several single-residue mutations of the U2AF small subunit cause severe disorders such as myelodysplastic syndromes. However, the mechanism of RNA recognition is poorly understood. Here we solved the crystal structure of the U2AF small subunit (U2AF23) from fission yeast, consisting of an RNA recognition motif (RRM) domain flanked by two conserved CCCH-type zinc fingers (ZFs). The two ZFs are positioned side by side on the β sheet of the RRM domain. Further mutational analysis revealed that the ZFs bind cooperatively to the target RNA sequence, but the RRM domain acts simply as a scaffold to organize the ZFs and does not itself contact the RNA directly. This completely novel and unexpected mode of RNA-binding mechanism by the U2AF small subunit sheds light on splicing errors caused by mutations of this highly conserved protein.","doi":"10.1101/gad.267104.115","authors":"Yoshida H, Park SY, Oda T, Akiyoshi T, Sato M, Shirouzu M, Tsuda K, Kuwasako K, Unzai S, Muto Y, Urano T, Obayashi E","authors_abbrev":"Yoshida H et al.","pubmed_publication_date":"01 Aug 2015","pubmed_entrez_date":"2015-07-29","publication_year":"2015","canto_session_key":"45eb64491541b97f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-07-30 00:19:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC146.07","SPAP8A3.06"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"4yh8","gene_chains":[{"gene_uniquename":"SPBC146.07","chain":"B","position":"93-161"},{"gene_uniquename":"SPAP8A3.06","chain":"A","position":"1-216"}],"title":"Structure of yeast U2AF complex","entry_authors":"Yoshida H,Park SY,Urano T,Obayashi E","entry_authors_abbrev":"Yoshida H et al.","reference_uniquename":"PMID:26215567","experimental_method":"X-ray","resolution":"1.7"}]},{"uniquename":"PMID:24963130","title":"The KASH protein Kms2 coordinates mitotic remodeling of the spindle pole body.","citation":"J Cell Sci 2014 Aug 15;127(Pt 16):3625-40","abstract":"Defects in the biogenesis of the spindle pole body (SPB), the yeast centrosome equivalent, can lead to monopolar spindles and mitotic catastrophe. The KASH domain protein Kms2 and the SUN domain protein Sad1 colocalize within the nuclear envelope at the site of SPB attachment during interphase and at the spindle poles during mitosis in Schizosaccharomyces pombe. We show that Kms2 interacts with the essential SPB components Cut12 and Pcp1 and the Polo kinase Plo1. Depletion of Kms2 delays mitotic entry and leads to defects in the insertion of the SPB into the nuclear envelope, disrupting stable bipolar spindle formation. These effects are mediated in part by a delay in the recruitment of Plo1 to the SPB at mitotic entry. Plo1 activity supports mitotic SPB remodeling by driving a burst of incorporation of Cut12 and Pcp1. Thus, a fission yeast SUN-KASH complex plays an important role in supporting the remodeling of the SPB at mitotic entry.","doi":"10.1242/jcs.154997","authors":"Wälde S, King MC","authors_abbrev":"Wälde S et al.","pubmed_publication_date":"15 Aug 2014","pubmed_entrez_date":"2014-06-26","publication_year":"2014","canto_session_key":"1b9146dba1a740a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Megan King","canto_first_approved_date":"2016-04-28 16:49:17","canto_approved_date":"2024-06-26 10:27:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-28 12:44:44","canto_added_date":"2014-06-28 00:15:27","annotation_curators":[{"name":"Megan King","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPBC26H8.07c","SPAC24H6.05","SPBC12D12.01","SPAC6G9.06c","SPAC23C11.16","SPBC947.12","SPBC428.20c","SPAC3G9.12","SPBC649.05","SPAC1786.03","SPAC3A11.05c","SPBC2F12.13"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2016-04-28"},{"uniquename":"PMID:9653157","title":"sud1(+) targets cyclin-dependent kinase-phosphorylated Cdc18 and Rum1 proteins for degradation and stops unwanted diploidization in fission yeast.","citation":"Proc Natl Acad Sci U S A 1998 Jul 07;95(14):8159-64","abstract":"In the fission yeast Schizosaccharomyces pombe, S phase is limited to a single round per cell cycle through cyclin-dependent kinase phosphorylation of critical replication factors, including the Cdc18 replication initiator protein. Because defects in Cdc18 phosphorylation lead to a hyperstable and hyperactive form of Cdc18 that promotes high levels of overreplication in vivo, we wished to identify the components of the Cdc18 proteolysis pathway in fission yeast. In this paper we describe one such component, encoded by the sud1(+) gene. sud1(+) shares homology with the budding yeast CDC4 gene and is required to prevent spontaneous re-replication in fission yeast. Cells lacking sud1(+) accumulate high levels of Cdc18 and the CDK inhibitor Rum1, because they cannot degrade these two key cell cycle regulators. Through genetic analysis we show that hyperaccumulation of Rum1 contributes to re-replication in Deltasud1 cells, but is not the cause of the defect in Cdc18 proteolysis. Rather, Sud1 itself is associated with the ubiquitin pathway in fission yeast and binds to Cdc18 in vivo. Most importantly, Sud1-Cdc18 binding requires prior phosphorylation of the Cdc18 polypeptide at CDK consensus sites. These results provide a biochemical mechanism for the phosphorylation-dependent degradation of Cdc18 and other cell cycle regulators, including Rum1. Evolutionary conservation of the Sud1/CDC4 pathway suggests that phosphorylation-coupled proteolysis may be a general feature of nearly all eukaryotic cell cycles.","authors":"Jallepalli PV, Tien D, Kelly TJ","authors_abbrev":"Jallepalli PV et al.","pubmed_publication_date":"07 Jul 1998","pubmed_entrez_date":"1998-07-08","publication_year":"1998","canto_session_key":"0c180e0969ef689c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-03-06 17:19:35","canto_approved_date":"2026-01-29 13:34:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-03-06 11:04:52","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4.07c","SPBC32F12.09","SPAC4D7.03","SPBC16G5.01","SPBC14C8.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-03-06"},{"uniquename":"PMID:36361590","title":"Defining the Functional Interactome of Spliceosome-Associated G-Patch Protein Gpl1 in the Fission Yeast  Schizosaccharomyces pombe .","citation":"Int J Mol Sci 2022 Oct 24;23(21)","abstract":"Pre-mRNA splicing plays a fundamental role in securing protein diversity by generating multiple transcript isoforms from a single gene. Recently, it has been shown that specific G-patch domain-containing proteins are critical cofactors involved in the regulation of splicing processes. In this study, using the knock-out strategy, affinity purification and the yeast-two-hybrid assay, we demonstrated that the spliceosome-associated G-patch protein Gpl1 of the fission yeast  S. pombe  mediates interactions between putative RNA helicase Gih35 (SPAC20H4.09) and WD repeat protein Wdr83, and ensures their binding to the spliceosome. Furthermore, RT-qPCR analysis of the splicing efficiency of deletion mutants indicated that the absence of any of the components of the Gpl1-Gih35-Wdr83 complex leads to defective splicing of  fet5  and  pwi1 , the reference genes whose unspliced isoforms harboring premature stop codons are targeted for degradation by the nonsense-mediated decay (NMD) pathway. Together, our results shed more light on the functional interactome of G-patch protein Gpl1 and revealed that the Gpl1-Gih35-Wdr83 complex plays an important role in the regulation of pre-mRNA splicing in  S. pombe .","doi":"10.3390/ijms232112800","authors":"Selicky T, Jurcik M, Mikolaskova B, Pitelova A, Mayerova N, Kretova M, Osadska M, Jurcik J, Holic R, Kohutova L, Bellova J, Benko Z, Gregan J, Bagelova Polakova S, Barath P, Cipak L, Cipakova I","authors_abbrev":"Selicky T et al.","pubmed_publication_date":"24 Oct 2022","pubmed_entrez_date":"2022-11-11","publication_year":"2022","canto_session_key":"f45b7c9c20201a38","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lubos Cipak","canto_first_approved_date":"2022-11-28 12:43:14","canto_approved_date":"2022-11-28 14:50:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-28 10:21:00","canto_added_date":"2022-11-16 01:15:04","annotation_curators":[{"name":"Lubos Cipak","community_curator":true,"annotation_count":206,"orcid":"0000-0001-7897-6001","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29E6.02","SPAC27D7.07c","SPBP4H10.04","SPAC1556.01c","SPBC1709.05","SPBC106.06","SPBC29A10.13","SPAC10F6.02c","SPAC139.02c","SPAC4D7.03","SPBC1A4.08c","SPAC926.04c","SPCC188.11","SPBC31F10.11c","SPBC9B6.08","SPAC6G9.02c","SPBC211.02c","SPCC364.02c","SPBC1921.06c","SPCC550.02c","SPBC16H5.02","SPBC1289.11","SPBC337.06c","SPAC513.01c","SPBC646.02","SPBP22H7.07","SPAC664.11","SPBC17D11.02c","SPAC20H4.06c","SPCC5E4.10c","SPAC1D4.04","SPBC24C6.04","SPBC4B4.05","SPAC9.03c","SPAC17H9.02","SPBC18H10.10c","SPAC140.04","SPCC1795.11","SPAC1420.02c","SPAC4A8.09c","SPAC4F8.12c","SPBC20F10.05","SPBP8B7.11","SPBC16H5.08c","SPBC28F2.03","SPBC13E7.01","SPAC22A12.15c","SPAC4F8.13c","SPAC6F6.08c","SPBC215.12","SPBP8B7.16c","SPAC1F8.07c","SPAC140.02","SPBC8D2.09c","SPBC365.05c","SPBC1861.08c","SPAC57A7.04c","SPAC17A2.08c","SPBC337.05c","SPBC3E7.13c","SPBC28F2.04c","SPCC338.15","SPBC646.11","SPBC16H5.10c","SPBC25H2.12c","SPAC22A12.11","SPAC17C9.03","SPAC1486.03c","SPCC825.05c","SPAC26A3.08","SPAC644.12","SPAC2C4.03c","SPBC24C6.11","SPAC17G6.13","SPBC12D12.03","SPAC8C9.04","SPAC3A12.11c","SPAC31G5.18c","SPBC713.05","SPBC1815.01","SPBC36.09","SPCC1183.11","SPAC22E12.11c","SPAC4H3.10c","SPAC29A4.08c","SPAC20H4.09","SPCC417.08","SPCC737.07c","SPBC32F12.05c","SPBC6B1.10","SPAC4A8.11c","SPCP1E11.07c","SPBC19C2.14","SPCC13B11.01","SPBC14F5.04c","SPCP1E11.08","SPAC4D7.12c"],"gene_count":97,"ltp_gene_count":92,"approved_date":"2022-11-28"},{"uniquename":"PMID:9092625","title":"Characterisation of Schizosaccharomyces pombe rad31, a UBA-related gene required for DNA damage tolerance.","citation":"Nucleic Acids Res 1997 Mar 15;25(6):1162-9","abstract":"The fission yeast rad31-1 mutant is sensitive to both UV and ionising radiation and exhibits a growth defect at 35 degrees C. In addition, the mutant displays defects in cell morphology and nuclear division at 26 degrees C which are exaggerated at 35 degrees C. We have cloned the rad31 gene and have shown that it is not essential for viability, although cells containing a disrupted rad31 gene grow slowly. The null allele has similar cell and nuclear morphologies to the original allele and displays an extremely high frequency of loss of minichromosomes. rad31 is not required for either the S/M or G2/M checkpoint, however double mutant analysis indicates that rad31 acts in a process which is defective in the checkpoint rad mutants and which involves hus5 . Sequence analysis indicates that rad31 encodes a protein which is related to ubiquitin activating proteins and more particularly to an ORF in Saccharomyces cerevisiae and to the Arabidopsis thaliana AXR1 and human APP-BP1 genes. We have isolated the S.cerevisiae sequence, which we have named RHC31 ( ad31homologue in S. erevisiae), since we show that it can complement the slow growth phenotype and radiation sensitivity of S.pombe rad31.","authors":"Shayeghi M, Doe CL, Tavassoli M, Watts FZ","authors_abbrev":"Shayeghi M et al.","pubmed_publication_date":"15 Mar 1997","pubmed_entrez_date":"1997-03-15","publication_year":"1997","canto_session_key":"9d68bc80736f1fb4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-05-13 09:45:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-13 09:28:49","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPCC1259.13","SPAC23C4.12","SPAC4C5.04","SPAC30D11.13","SPAC20G4.04c","SPAC13G6.01c","SPBC336.12c","SPCC18B5.03","SPAC664.07c","SPAC14C4.13","SPBC3E7.08c","SPAC13C5.07","SPAC1D4.12"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2014-05-13"},{"uniquename":"PMID:15314153","title":"The B-subunit of DNA polymerase alpha-primase associates with the origin recognition complex for initiation of DNA replication.","citation":"Mol Cell Biol 2004 Sep;24(17):7419-34","abstract":"The B-subunit (p70/Pol12p) of the DNA polymerase alpha-primase (Polalpha-primase) complex is thought to have a regulatory role in an early stage of S phase. We generated a panel of fission yeast thermosensitive mutants of the B-subunit (termed Spb70) to investigate its role in initiation of DNA replication by genetic and biochemical approaches. Here, we show that the fission yeast Spb70 genetically interacts and coprecipitates with origin recognition complex proteins Orp1/Orc1 and Orp2/Orc2 and primase coupling subunit Spp2/p58. A fraction of Spb70 associates with Orp2 on chromatin throughout the cell cycle independent of the other subunits of Polalpha-primase. Furthermore, primase Spp2/p58 subunit preferentially associates with the unphosphorylated Orp2, and the association requires Spb70. Mutations in orp2+ that abolish or mimic the Cdc2 phosphorylation of Orp2 suppress or exacerbate the thermosensitivity of the spb70 mutants, respectively, indicating that an unphosphorylated Orp2 promotes an Spb70-dependent replication event. Together, these results indicate that the chromatin-bound B-subunit in association with origin recognition complex mediates recruiting Polalpha-primase complex onto replication origins in G1 pre-Start through an interaction with primase Spp2/p58 subunit. Our results thus suggest a role for the recruited Polalpha-primase in the initiation of both leading and lagging strands at the replication origins.","authors":"Uchiyama M, Wang TS","authors_abbrev":"Uchiyama M et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-08-18","publication_year":"2004","canto_session_key":"dfae0c881b3c5469","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-12-22 14:13:28","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-10-27 15:51:43","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":54,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17D11.06","SPAC3H5.06c","SPAC17D4.02","SPBC685.09","SPAC6B12.10c","SPCC553.09c","SPBC29A10.15"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2014-10-27"},{"uniquename":"PMID:2108906","title":"An inducible expression vector for both fission and budding yeast.","citation":"Gene 1990 Feb 14;86(2):257-61","abstract":"We have developed a vector system for inducible gene expression in both fission yeast (Schizosaccharomyces pombe) and budding yeast (Saccharomyces cerevisiae). The autonomously replicating expression vector contains multiple glucocorticoid response elements, rendering a linked promoter inducible 20-70-fold by glucocorticoid hormones in the presence of the mammalian glucocorticoid receptor. A polylinker with several unique cloning sites allows insertion of cDNAs of interest. Glucocorticoids are gratuitous signalling molecules in yeast, exerting little or no effect on the expression of genes other than those fused to the regulated promoter.","authors":"Picard D, Schena M, Yamamoto KR","authors_abbrev":"Picard D et al.","pubmed_publication_date":"14 Feb 1990","pubmed_entrez_date":"1990-02-14","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20236312","title":"Mixed lineage leukemia: histone H3 lysine 4 methyltransferases from yeast to human.","citation":"FEBS J 2010 Apr;277(8):1805-21","abstract":"The fourth lysine of histone H3 is post-translationally modified by a methyl group via the action of histone methyltransferase, and such a covalent modification is associated with transcriptionally active and/or repressed chromatin states. Thus, histone H3 lysine 4 methylation has a crucial role in maintaining normal cellular functions. In fact, misregulation of this covalent modification has been implicated in various types of cancer and other diseases. Therefore, a large number of studies over recent years have been directed towards histone H3 lysine 4 methylation and the enzymes involved in this covalent modification in eukaryotes ranging from yeast to human. These studies revealed a set of histone H3 lysine 4 methyltransferases with important cellular functions in different eukaryotes, as discussed here.","doi":"10.1111/j.1742-4658.2010.07607.x","authors":"Malik S, Bhaumik SR","authors_abbrev":"Malik S et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-03-19","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25038083","title":"Cross kingdom functional conservation of the core universally conserved threonylcarbamoyladenosine tRNA synthesis enzymes.","citation":"Eukaryot Cell 2014 Sep;13(9):1222-31","abstract":"Threonylcarbamoyladenosine (t(6)A) is a universal modification located in the anticodon stem-loop of tRNAs. In yeast, both cytoplasmic and mitochondrial tRNAs are modified. The cytoplasmic t(6)A synthesis pathway was elucidated and requires Sua5p, Kae1p, and four other KEOPS complex proteins. Recent in vitro work suggested that the mitochondrial t(6)A machinery of Saccharomyces cerevisiae is composed of only two proteins, Sua5p and Qri7p, a member of the Kae1p/TsaD family (L. C. K. Wan et al., Nucleic Acids Res. 41:6332-6346, 2013, http://dx.doi.org/10.1093/nar/gkt322). Sua5p catalyzes the first step leading to the threonyl-carbamoyl-AMP intermediate (TC-AMP), while Qri7 transfers the threonyl-carbamoyl moiety from TC-AMP to tRNA to form t(6)A. Qri7p localizes to the mitochondria, but Sua5p was reported to be cytoplasmic. We show that Sua5p is targeted to both the cytoplasm and the mitochondria through the use of alternative start sites. The import of Sua5p into the mitochondria is required for this organelle to be functional, since the TC-AMP intermediate produced by Sua5p in the cytoplasm is not transported into the mitochondria in sufficient amounts. This minimal t(6)A pathway was characterized in vitro and, for the first time, in vivo by heterologous complementation studies in Escherichia coli. The data revealed a potential for TC-AMP channeling in the t(6)A pathway, as the coexpression of Qri7p and Sua5p is required to complement the essentiality of the E. coli tsaD mutant. Our results firmly established that Qri7p and Sua5p constitute the mitochondrial pathway for the biosynthesis of t(6)A and bring additional advancement in our understanding of the reaction mechanism.","doi":"10.1128/EC.00147-14","authors":"Thiaville PC, El Yacoubi B, Perrochia L, Hecker A, Prigent M, Thiaville JJ, Forterre P, Namy O, Basta T, de Crécy-Lagard V","authors_abbrev":"Thiaville PC et al.","pubmed_publication_date":"Sep 2014","pubmed_entrez_date":"2014-07-20","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC895.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20709788","title":"Ccq1p and the condensin proteins Cut3p and Cut14p prevent telomere entanglements in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2010 Oct;9(10):1612-21","abstract":"The Schizosaccharomyces pombe telomere-associated protein Ccq1p has previously been shown to participate in telomerase recruitment, heterochromatin formation, and suppression of checkpoint activation. Here we characterize a critical role for Ccq1p in mitotic transit. We show that mitotic cells lacking Ccq1p lose minichromosomes at high frequencies but that conditional knockdown of Ccq1p expression results in telomere bridging within one cell cycle. Elevating Ccq1p expression resolves the telomere entanglements caused by decreased Taz1p activity. Ccq1p affects telomere resolution in the absence of changes in telomere size, indicating a role for Ccq1p that is independent of telomere length regulation. Using affinity purification, we identify the condensin proteins Cut3p and Cut14p as candidate Ccq1p interactors in this activity. Condensin loss-of-function disrupts Ccq1p telomeric localization and normal intertelomere clustering, while condensin overexpression relieves the chromosome segregation defects associated with conditional Ccq1p knockdown. These data suggest that Ccq1p and condensins collaborate to mediate resolution of telomeres in mitosis and regulate intertelomeric clustering during interphase.","doi":"10.1128/EC.00339-09","authors":"Motwani T, Doris R, Holmes SG, Flory MR","authors_abbrev":"Motwani T et al.","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2010-08-17","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.06c","SPBC146.03c","SPCC188.07","SPAC16A10.07c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:9891378","title":"GFP fusion proteins as probes for cytology in fission yeast.","citation":"Methods Cell Biol 1999;58:123-38","abstract":"","authors":"Sawin KE","authors_abbrev":"Sawin KE","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-01-19","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28922417","title":"Lingering single-strand breaks trigger Rad51-independent homology-directed repair of collapsed replication forks in the polynucleotide kinase/phosphatase mutant of fission yeast.","citation":"PLoS Genet 2017 Sep;13(9):e1007013","abstract":"The DNA repair enzyme polynucleotide kinase/phosphatase (PNKP) protects genome integrity by restoring ligatable 5'-phosphate and 3'-hydroxyl termini at single-strand breaks (SSBs). In humans, PNKP mutations underlie the neurological disease known as MCSZ, but these individuals are not predisposed for cancer, implying effective alternative repair pathways in dividing cells. Homology-directed repair (HDR) of collapsed replication forks was proposed to repair SSBs in PNKP-deficient cells, but the critical HDR protein Rad51 is not required in PNKP-null (pnk1Δ) cells of Schizosaccharomyces pombe. Here, we report that pnk1Δ cells have enhanced requirements for Rad3 (ATR/Mec1) and Chk1 checkpoint kinases, and the multi-BRCT domain protein Brc1 that binds phospho-histone H2A (γH2A) at damaged replication forks. The viability of pnk1Δ cells depends on Mre11 and Ctp1 (CtIP/Sae2) double-strand break (DSB) resection proteins, Rad52 DNA strand annealing protein, Mus81-Eme1 Holliday junction resolvase, and Rqh1 (BLM/WRN/Sgs1) DNA helicase. Coupled with increased sister chromatid recombination and Rad52 repair foci in pnk1Δ cells, these findings indicate that lingering SSBs in pnk1Δ cells trigger Rad51-independent homology-directed repair of collapsed replication forks. From these data, we propose models for HDR-mediated tolerance of persistent SSBs with 3' phosphate in pnk1Δ cells.","doi":"10.1371/journal.pgen.1007013","authors":"Sanchez A, Gadaleta MC, Limbo O, Russell P","authors_abbrev":"Sanchez A et al.","pubmed_publication_date":"Sep 2017","pubmed_entrez_date":"2017-09-19","publication_year":"2017","canto_session_key":"5b5e46476125df7d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2018-04-20 13:46:34","canto_approved_date":"2018-04-20 13:46:34","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-04-16 18:20:20","canto_added_date":"2017-09-20 00:15:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":71,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPCC4G3.05c","SPBC4F6.15c","SPCC338.08","SPAC2G11.12","SPAC13C5.07","SPAC15A10.03c","SPCC1259.13","SPBC582.05c","SPAC30D11.10","SPBC543.03c","SPBC29A10.05","SPAPB1E7.06c","SPAC644.14c","SPCC18B5.11c","SPAC23C11.04c"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2018-04-20"},{"uniquename":"PMID:21484407","title":"Manganese SOD mimics are effective against heat stress in a mutant fission yeast deficient in mitochondrial superoxide dismutase.","citation":"Biol Trace Elem Res 2011 Dec;144(1-3):1344-50","abstract":"Previous studies revealed a close connection between heat shock and manganese-dependent superoxide dismutase (SOD2) in eukaryotes. This paper shows that SOD mimics based on manganese complexes caused an increase in thermotolerance for a mutant fission yeast deficient in mitochondrial superoxide dismutase. Manganese compounds used for tests are SOD mimics, from two different classes: salen manganese (EUK-8) and Mn porphyrin (Mn(III)TE-2-PyP(5+)). The tests were conducted using a Schizosaccharomyces pombe model, comparing the viability of two strains at chronic heat stress (37°C)--a wild type versus a strain with the mitochondrial superoxide dismutase gene deleted [SOD2(-)]. The presence of massive free radical species in S. pombe SOD2(-) was demonstrated using a luminol-enhanced chemiluminescence test derived from a menadione-mediated survival protocol.\nSurvival tests revealed that the SOD2-deleted S. pombe is about 100 times more sensitive to heat stress than the wild-type strain. This survival deficit can be corrected by EUK-8 and Mn(III)TE-2-PyP(5+) to almost the same degree but not by manganese chloride II (MnCl(2)). Using a simple spot assay for viability testing, this new model proved to be an easy alternative for the initial estimation of manganese SOD mimics efficiency.","doi":"10.1007/s12011-011-9035-8","authors":"Stoica BA, Rusu M, Petreus T, Nechifor M","authors_abbrev":"Stoica BA et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-04-13","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32571823","title":"NADPH-Cytochrome P450 Reductase Ccr1 Is a Target of Tamoxifen and Participates in Its Antifungal Activity via Regulating Cell Wall Integrity in Fission Yeast.","citation":"Antimicrob Agents Chemother 2020 Aug 20;64(9)","abstract":"Invasive fungal diseases are a leading cause of mortality among immunocompromised populations. Treatment is notoriously difficult due to the limited number of antifungal drugs as well as the emergence of drug resistance. Tamoxifen (TAM), a selective estrogen receptor modulator frequently used for the treatment of breast cancer, has been found to have antifungal activities and may be a useful addition to the agents used to treat fungal infectious diseases. However, the molecular mechanisms underlying its antifungal actions remain obscure. Here, we screened for mutations that confer sensitivity to azole antifungal drugs by using the fission yeast  Schizosaccharomyces pombe  as a model and isolated a mutant with a mutation in  cls1  ( ccr1 ), an allele of the gene encoding the NADPH-cytochrome P450 reductase Ccr1. We found that strains with a deletion of the  ccr1  +  gene exhibited hypersensitivities to various drugs, including antifungal drugs (azoles, terbinafine, micafungin), the immunosuppressor FK506, and the anticancer drugs TAM and 5-fluorouracil (5-FU). Unexpectedly, the overexpression of Ccr1 caused yeast cell resistance to TAM but not the other drugs tested here. Additionally, strains with a deletion of Ccr1 displayed pleiotropic phenotypes, including defects in cell wall integrity and vacuole fusion, enhanced calcineurin activity, as well as increased intracellular Ca 2+  levels. Overexpression of the constitutively active calcineurin suppressed the drug-sensitive phenotypes of the Δ ccr1  cells. Notably, TAM treatment of wild-type cells resulted in pleiotropic phenotypes, similar to those of cells lacking Ccr1. Furthermore, TAM inhibited Ccr1 NADPH-cytochrome P450 reductase activities in a dose-dependent manner. Moreover, TAM treatment also inhibited the NADPH-cytochrome P450 reductase activities of  Candida albicans  and resulted in defective cell wall integrity. Collectively, our findings suggest that Ccr1 is a novel target of TAM and is involved in the antifungal activity of TAM by regulating cell wall integrity in fission yeast.","doi":"10.1128/AAC.00079-20","authors":"Liu Q, Guo X, Jiang G, Wu G, Miao H, Liu K, Chen S, Sakamoto N, Kuno T, Yao F, Fang Y","authors_abbrev":"Liu Q et al.","pubmed_publication_date":"20 Aug 2020","pubmed_entrez_date":"2020-06-24","publication_year":"2020","canto_session_key":"bfcb5a1106855fcd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yue Fang","canto_first_approved_date":"2020-09-03 17:07:38","canto_approved_date":"2024-03-29 09:48:12","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-09-02 08:22:48","canto_added_date":"2020-06-25 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yue Fang","community_curator":true,"annotation_count":33,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.01","SPBP4H10.04","SPBC119.08","SPAC13A11.02c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2020-09-03"},{"uniquename":"PMID:10445882","title":"Pac1p, an RNase III homolog, is required for formation of the 3' end of U2 snRNA in Schizosaccharomyces pombe.","citation":"RNA 1999 Aug;5(8):1083-98","abstract":"Like its homologs in higher eukaryotes, the U2 snRNA in Schizosaccharomyces pombe is transcribed by RNA polymerase II and is not polyadenylated. Instead, an RNA stem-loop structure located downstream of the U2 snRNA coding sequence and transcribed as part of a 3' extended precursor serves as a signal for 3'-end formation. We have identified three mutants that have temperature-sensitive defects in U2 snRNA 3'-end formation. In these mutants, the synthesis of the major snRNAs is also affected and unprocessed rRNA precursors accumulate at the restrictive temperature. Two of these mutants contain the same G-to-A transition within the pac1 gene, whereas the third contains a lesion outside the pac1 locus, indicating that at least two genes are involved. The pac1+ gene is codominant with the mutant allele and can rescue the temperature-sensitive phenotype and the defects in snRNA and rRNA synthesis, if overexpressed. In vitro, Pac1p, an RNase III homolog, can cleave a synthetic U2 precursor within the signal for 3'-end formation, generating a product that is a few nucleotides longer than mature U2 snRNA. In addition, U2 precursors are cleaved and trimmed to the mature size in extracts made from wild-type S. pombe cells. However, extracts made from pac1 mutant cells are unable to do so unless they are supplemented with purified recombinant Pac1p. Thus, the 3' end of S. pombe U2 snRNA is generated by a processing reaction that requires Pac1p and an additional component, and can be dissociated from transcription in vitro.","authors":"Zhou D, Frendewey D, Lobo Ruppert SM","authors_abbrev":"Zhou D et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-08-13","publication_year":"1999","canto_session_key":"c242b94e8f530220","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-12-22 13:15:22","canto_approved_date":"2022-03-29 10:16:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-30 10:50:37","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.11c","SPSNRNA.02","SPSNRNA.01","SPSNRNA.04","SPSNRNA.05"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2014-12-22"},{"uniquename":"EMBL:SPC03110","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24637836","title":"Characterization of nuclear pore complex components in fission yeast Schizosaccharomyces pombe.","citation":"Nucleus 2014;5(2):149-62","abstract":"The nuclear pore complex (NPC) is an enormous proteinaceous complex composed of multiple copies of about 30 different proteins called nucleoporins. In this study, we analyzed the composition of the NPC in the model organism Schizosaccharomyces pombe using strains in which individual nucleoporins were tagged with GFP. We identified 31 proteins as nucleoporins by their localization to the nuclear periphery. Gene disruption analysis in previous studies coupled with gene disruption analysis in the present study indicates that 15 of these nucleoporins are essential for vegetative cell growth and the other 16 nucleoporins are non-essential. Among the 16 non-essential nucleoporins, 11 are required for normal progression through meiosis and their disruption caused abnormal spore formation or poor spore viability. Based on fluorescence measurements of GFP-fused nucleoporins, we estimated the composition of the NPC in S. pombe and found that the organization of the S. pombe NPC is largely similar to that of other organisms; a single NPC was estimated as being 45.8-47.8 MDa in size. We also used fluorescence measurements of single NPCs and quantitative western blotting to analyze the composition of the Nup107-Nup160 subcomplex, which plays an indispensable role in NPC organization and function. Our analysis revealed low amounts of Nup107 and Nup131 and high amounts of Nup132 in the Nup107-Nup160 subcomplex, suggesting that the composition of this complex in S. pombe may differ from that in S. cerevisiae and humans. Comparative analysis of NPCs in various organisms will lead to a comprehensive understanding of the functional architecture of the NPC.","doi":"10.4161/nucl.28487","authors":"Asakawa H, Yang HJ, Yamamoto TG, Ohtsuki C, Chikashige Y, Sakata-Sogawa K, Tokunaga M, Iwamoto M, Hiraoka Y, Haraguchi T","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-03-19","publication_year":"2014","canto_session_key":"6ad90d4a01aee5f2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Haruhiko Asakawa","canto_first_approved_date":"2018-03-06 15:21:17","canto_approved_date":"2025-09-03 20:28:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-31 06:43:13","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Haruhiko Asakawa","community_curator":true,"annotation_count":78,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.16c","SPAC19E9.01c","SPBC17G9.04c","SPCC290.03c","SPAP27G11.10c","SPBP35G2.06c","SPAC4F10.18","SPAC1486.05","SPAC22G7.09c","SPAC1786.03","SPBC15D4.10c","SPBC13A2.02","SPBC29A10.07","SPAC890.06","SPCC1620.11","SPCC1739.14","SPAC30D11.04c","SPBC428.01c","SPBC1539.04","SPBC19G7.15","SPAC1002.02","SPAC23D3.06c","SPBC215.15","SPAC1805.04","SPCC285.13c","SPAC15F9.02","SPBC29A10.06c","SPAC26A3.15c","SPBC16A3.05c","SPCC162.08c","SPCC18B5.07c"],"gene_count":31,"ltp_gene_count":30,"approved_date":"2018-03-06"},{"uniquename":"PMID:1783290","title":"swi6, a gene required for mating-type switching, prohibits meiotic recombination in the mat2-mat3 \"cold spot\" of fission yeast.","citation":"Genetics 1991 Dec;129(4):1033-42","abstract":"Mitotic interconversion of the mating-type locus (mat1) of the fission yeast Schizosaccharomyces pombe is initiated by a double-strand break at mat1. The mat2 and mat3 loci act as nonrandom donors of genetic information for mat1 switching such that switches occur primarily (or only) to the opposite mat1 allele. Location of the mat1 \"hot spot\" for transposition should be contrasted with the \"cold spot\" of meiotic recombination located within the adjoining mat2-mat3 interval. That is, meiotic interchromosomal recombination in mat2, mat3 and the intervening 15-kilobase region does not occur at all. swi2 and swi6 switching-deficient mutants possess the normal level of double-strand break at mat1, yet they fail to switch efficiently. By testing for meiotic recombination in the cold spot, we found the usual lack of recombination in a swi2 mutant but a significant level of recombination in a swi6 mutant. Therefore, the swi6 gene function is required to keep the donor loci inert for interchromosomal recombination. This finding, combined with the additional result that switching primarily occurs intrachromosomally, suggests that the donor loci are made accessible for switching by folding them onto mat1, thus causing the cold spot of recombination.","authors":"Klar AJ, Bonaduce MJ","authors_abbrev":"Klar AJ et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"2ce05300b6339e71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-03-22 18:44:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-08 15:00:14","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-08"},{"uniquename":"PMID:11260264","title":"Functional analysis of the C-terminal cytoplasmic region of the M-factor receptor in fission yeast.","citation":"Genes Cells 2001 Mar;6(3):201-14","abstract":"Yeast mating-pheromone receptors facilitate the study of G protein-coupled signal transduction. To date, molecular dissection of the budding yeast alpha-factor receptor has been done extensively, but little analysis has been performed with pheromone receptors of fission yeast, another genetically tractable yeast species.\nWe analysed the fission yeast M-factor receptor Map3p. Truncation of the C-terminal 54 amino acids made Map3p dominant-negative over the wild-type. This form, called Map3-dn9p, was competent in the induction of pheromone-dependent gene expression, although it could not direct proper conjugation. Map3-dn9p failed both to provoke the orientated projection of conjugation tubes and to induce adaptation to the pheromone signal associated with endocytosis of the receptor. Deletion and substitution analyses suggested that the integrity of the C-terminal region, rather than a specific subgroup of amino acid residues therein, was vital for the respective Map3p activities. Ubiquitination of the C-terminus was not absolutely essential for Map3p function.\nThe C-terminal region of Map3p is dispensable for the pheromone signalling per se, but is pivotal for adaptation and pheromone-induced conjugation tube formation, as is true with the budding yeast alpha-factor receptor. However, the mechanisms which induce adaptation appear to differ between fission and budding yeast concerning the necessity of ubiquitination.","authors":"Hirota K, Tanaka K, Watanabe Y, Yamamoto M","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-03-22","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1518044","title":"Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction.","citation":"J Mol Biol 1992 Aug 20;226(4):1051-72","abstract":"NADH:ubiquinone oxidoreductase, the first enzyme in the respiratory electron transport chain of mitochondria, is a membrane-bound multi-subunit assembly, and the bovine heart enzyme is now known to contain about 40 different polypeptides. Seven of them are encoded in the mitochondrial DNA; the remainder are the products of nuclear genes and are imported into the organelle. The primary structures of 12 of the nuclear coded subunits have been described and those of a further 20 are described here. The subunits have been sequenced by following a strategy based on the polymerase chain reaction. This strategy has been tailored from existing methods with the twofold aim of avoiding the use of cDNA libraries, and of obtaining a cDNA sequence rapidly with minimal knowledge of protein sequence, such as can be determined in a single N-terminal sequence experiment on a polypeptide spot on a two-dimensional gel. The utility and speed of this strategy have been demonstrated by sequencing cDNAs encoding 32 nuclear-coded-membrane associated proteins found in bovine heart mitochondria, and the procedures employed are illustrated with reference to the cDNA sequence of the 20 subunits of NADH:ubiquinone oxidoreductase that are presented. Extensive use has also been made of electrospray mass spectrometry to measure molecular masses of the purified subunits. This has corroborated the protein sequences of subunits with unmodified N terminals, and their measured molecular masses agree closely with those calculated from the protein sequences. Nine of the subunits, B8, B9, B12, B13, B14, B15, B17, B18 and B22 have modified alpha-amino groups. The measured molecular masses of subunits B8, B13, B14 and B17 are consistent with the post-translational removal of the initiator methionine and N-acetylation of the adjacent amino acid. The initiator methionine of subunit B18 has been removed and the N-terminal glycine modified by myristoylation. Subunits B9 and B12 appear to have N-terminal and other modifications of a hitherto unknown nature. The sequences of the subunits of bovine complex I provide important clues about the location of iron-sulphur clusters and substrate and cofactor binding sites, and give valuable information about the topology of the complex. No function has been ascribed to many of the subunits, but some of the sequences indicate the presence of hitherto unsuspected biochemical functions. Most notably the identification of an acyl carrier protein in both the bovine and Neurospora crassa complexes provides evidence that part of the complex may play a role in fatty acid biosynthesis in the organelle, possibly in the formation of cardiolipin.(ABSTRACT TRUNCATED AT 400 WORDS)","authors":"Walker JE, Arizmendi JM, Dupuis A, Fearnley IM, Finel M, Medd SM, Pilkington SJ, Runswick MJ, Skehel JM","authors_abbrev":"Walker JE et al.","pubmed_publication_date":"20 Aug 1992","pubmed_entrez_date":"1992-08-20","publication_year":"1992","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC13G1.06c","SPAC11E3.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:32491985","title":"A conserved RNA degradation complex required for spreading and epigenetic inheritance of heterochromatin.","citation":"Elife 2020 Jun 03;9","abstract":"Heterochromatic domains containing histone H3 lysine 9 methylation (H3K9me) can be epigenetically inherited independently of underlying DNA sequence. To gain insight into the mechanisms that mediate epigenetic inheritance, we used a  Schizosaccharomyces pombe  inducible heterochromatin formation system to perform a genetic screen for mutations that abolish heterochromatin inheritance without affecting its establishment. We identified mutations in several pathways, including the conserved and essential Rix1-associated complex (henceforth the rixosome), which contains RNA endonuclease and polynucleotide kinase activities with known roles in ribosomal RNA processing. We show that the rixosome is required for spreading and epigenetic inheritance of heterochromatin in fission yeast. Viable rixosome mutations that disrupt its association with Swi6/HP1 fail to localize to heterochromatin, lead to accumulation of heterochromatic RNAs, and block spreading of H3K9me and silencing into actively transcribed regions. These findings reveal a new pathway for degradation of heterochromatic RNAs with essential roles in heterochromatin spreading and inheritance.","doi":"10.7554/eLife.54341","authors":"Shipkovenska G, Durango A, Kalocsay M, Gygi SP, Moazed D","authors_abbrev":"Shipkovenska G et al.","pubmed_publication_date":"03 Jun 2020","pubmed_entrez_date":"2020-06-04","publication_year":"2020","canto_session_key":"5b788d471b9dd10f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-06-05 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4G3.18"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22505610","title":"Cylindrical cellular geometry ensures fidelity of division site placement in fission yeast.","citation":"J Cell Sci 2012 Aug 15;125(Pt 16):3850-7","abstract":"Successful cytokinesis requires proper assembly of the contractile actomyosin ring, its stable positioning on the cell surface and proper constriction. Over the years, many of the key molecular components and regulators of the assembly and positioning of the actomyosin ring have been elucidated. Here we show that cell geometry and mechanics play a crucial role in the stable positioning and uniform constriction of the contractile ring. Contractile rings that assemble in locally spherical regions of cells are unstable and slip towards the poles. By contrast, actomyosin rings that assemble on locally cylindrical portions of the cell under the same conditions do not slip, but uniformly constrict the cell surface. The stability of the rings and the dynamics of ring slippage can be described by a simple mechanical model. Using fluorescence imaging, we verify some of the quantitative predictions of the model. Our study reveals an intimate interplay between geometry and actomyosin dynamics, which are likely to apply in a variety of cellular contexts.","doi":"10.1242/jcs.103788","authors":"Mishra M, Huang Y, Srivastava P, Srinivasan R, Sevugan M, Shlomovitz R, Gov N, Rao M, Balasubramanian M","authors_abbrev":"Mishra M et al.","pubmed_publication_date":"15 Aug 2012","pubmed_entrez_date":"2012-04-17","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPCC1223.06","SPCC895.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:9655186","title":"Physiological consequences of expression of the Na+/H+ antiporter sod2 in Escherichia coli.","citation":"Mol Cell Biochem 1998 Jun;183(1-2):125-32","abstract":"Sod2 is the sodium-proton antiporter on the plasma membrane of the fission yeast Schizosaccharomyces pombe. It is vitally important for sodium export and pH homeostasis in this organism. Recently, the sod2 gene has been cloned and sequenced. However, initial attempts to express sod2 in Escherichia coli using the T7 promoter failed. In the present work we examined physiological consequences of expression of sod2 in E. coli. To alleviate problems caused by expression of sod2 we: (i) used sodium-free media at all steps; (ii) used the moderate tac promoter for expression and; (iii) used E. coli strain MH1 which has impaired sodium exchange. The effect of sod2 expression on E. coli varied depending on the E. coli genotype. When sod2 was expressed in BL21 cells which have normal Na+/H+ antiporters, the result was a Li+ sensitive phenotype. LiCl completely arrested or prevented growth of BL21 E. coli transformed with the sod2 gene. The effect on growth was pronounced in media of low external pH. Sod2 was then expressed in E. coli MH1 which is devoid of endogenous Na+/H+ antiporters. These cells became more resistant to external LiCl, but only in Na+ containing media. In the absence of external Na+, the presence of sod2 reduced growth. The results are explained in a model which demonstrates the physiological consequences of interference by expression of a foreign electroneutral Na+/H+ antiporter in conjunction with different housekeeping systems of E. coli host cells.","authors":"Dibrov P, Young PG, Fliegel L","authors_abbrev":"Dibrov P et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-07-09","publication_year":"1998","canto_session_key":"05567236c5692d63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-11-30 18:16:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-30 18:16:39","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-30"},{"uniquename":"PMID:9252327","title":"Telomerase catalytic subunit homologs from fission yeast and human.","citation":"Science 1997 Aug 15;277(5328):955-9","abstract":"Catalytic protein subunits of telomerase from the ciliate Euplotes aediculatus and the yeast Saccharomyces cerevisiae contain reverse transcriptase motifs. Here the homologous genes from the fission yeast Schizosaccharomyces pombe and human are identified. Disruption of the S. pombe gene resulted in telomere shortening and senescence, and expression of mRNA from the human gene correlated with telomerase activity in cell lines. Sequence comparisons placed the telomerase proteins in the reverse transcriptase family but revealed hallmarks that distinguish them from retroviral and retrotransposon relatives. Thus, the proposed telomerase catalytic subunits are phylogenetically conserved and represent a deep branch in the evolution of reverse transcriptases.","authors":"Nakamura TM, Morin GB, Chapman KB, Weinrich SL, Andrews WH, Lingner J, Harley CB, Cech TR","authors_abbrev":"Nakamura TM et al.","pubmed_publication_date":"15 Aug 1997","pubmed_entrez_date":"1997-08-15","publication_year":"1997","canto_session_key":"270b9bbbfc56bc72","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-02-07 22:49:01","canto_approved_date":"2018-02-13 19:02:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-02-07 17:33:38","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-02-07"},{"uniquename":"PMID:15157893","title":"Analysis of chromatin in fission yeast.","citation":"Methods 2004 Jul;33(3):252-9","abstract":"The use of fission yeast as a model system for studies of chromosome biology has contributed to several key advances in the last few years. The structure of its large complex centromeres and composition of its transcriptionally silent heterochromatin resemble those of metazoa. The application of chromatin immunoprecipitation to fission yeast has been instrumental in these advances and we describe an improved version of this technique in detail. In addition, we describe several other techniques, which are useful in the analysis of chromatin in fission yeast.","authors":"Pidoux A, Mellone B, Allshire R","authors_abbrev":"Pidoux A et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26175449","title":"Monitoring SPB biogenesis in fission yeast with high resolution and quantitative fluorescent microscopy.","citation":"Methods Cell Biol 2015;129:383-392","abstract":"Like centrosomes, yeast spindle pole bodies (SPBs) undergo a tightly controlled duplication cycle in order to restrict their number to one or two per cell and promote the assembly of a bipolar spindle at mitotic entry. This conservative duplication cycle is tightly coordinated with cell cycle progression although the mechanisms that ensure this coordination remain largely unknown. In this chapter, we describe simple high resolution microscopy- and quantitative light microscopy-based methods that allow to monitor SPB biogenesis in fission yeast and may be useful to study the molecular pathways controlling the successive phases of the duplication cycle.","doi":"10.1016/bs.mcb.2015.03.005","authors":"Bouhlel IB, Scheffler K, Tran PT, Paoletti A","authors_abbrev":"Bouhlel IB et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-07-16","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-07-17 00:20:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC8D2.05c","SPCC1682.04"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:23122962","title":"Cdk11-cyclinL controls the assembly of the RNA polymerase II mediator complex.","citation":"Cell Rep 2012 Nov 29;2(5):1068-76","abstract":"The large Mediator (L-Mediator) is a general coactivator of RNA polymerase II transcription and is formed by the reversible association of the small Mediator (S-Mediator) and the kinase-module-harboring Cdk8. It is not known how the kinase module association/dissociation is regulated. We describe the fission yeast Cdk11-L-type cyclin pombe (Lcp1) complex and show that its inactivation alters the global expression profile in a manner very similar to that of mutations of the kinase module. Cdk11 is broadly distributed onto chromatin and phosphorylates the Med27 and Med4 Mediator subunits on conserved residues. The association of the kinase module and the S-Mediator is strongly decreased by the inactivation of either Cdk11 or the mutation of its target residues on the Mediator. These results show that Cdk11-Lcp1 regulates the association of the kinase module and the S-Mediator to form the L-Mediator complex.","doi":"10.1016/j.celrep.2012.09.027","authors":"Drogat J, Migeot V, Mommaerts E, Mullier C, Dieu M, van Bakel H, Hermand D","authors_abbrev":"Drogat J et al.","pubmed_publication_date":"29 Nov 2012","pubmed_entrez_date":"2012-11-06","publication_year":"2012","canto_session_key":"223397563bf5eae7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-22 15:42:48","canto_approved_date":"2025-02-22 20:26:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-22 15:42:42","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":39,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1393.10","SPAC1786.02","SPAC23H4.17c","SPAC1296.05c","SPAC2F3.15","SPBC18H10.15","SPBPB2B2.06c","SPBC14F5.08","SPBC1105.06","SPAC17C9.05c","SPBC19F8.07","SPAC25B8.13c","SPBC28F2.12","SPBPB7E8.01","SPBC947.04"],"gene_count":15,"ltp_gene_count":8,"approved_date":"2024-02-22"},{"uniquename":"PMID:11941510","title":"Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces pombe Isa1.","citation":"J Biol Inorg Chem 2002 Apr;7(4-5):526-32","abstract":"Eukaryotic Isa1 is one of several mitochondrial proteins that have been implicated in Fe-S cluster assembly paths in vivo. We report the first biochemical characterization of an eukaryotic member of this family and discuss this in the context of results from in vivo studies and studies of bacterial homologues. Schizosaccharomyces pombe Isa1 is a multimeric protein carrying [2Fe-2S](2+) clusters that have been characterized by Mössbauer and optical spectroscopic studies. Complex formation with a redox-active ferredoxin has been identified through crosslinking experiments and the coordination chemistry and stability of the native clusters has been investigated through site-directed mutagenesis and spectroscopic analysis. Electronic supplementary material to this paper, containing Mössbauer and UV-visible spectra for mutant Isa1 proteins, can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00775-001-0330-2.","authors":"Wu G, Mansy SS, Hemann C, Hille R, Surerus KK, Cowan JA","authors_abbrev":"Wu G et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-10","publication_year":"2002","canto_session_key":"5bcb2e3d060b5e23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-06 15:53:03","canto_approved_date":"2024-10-25 23:10:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-22 23:18:40","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.10c","SPCC645.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-09-06"},{"uniquename":"PMID:139890","title":"Mitochondrial adenosine triphosphatase of the fission yeast, Schizosaccharomyces pombe 972h-. Changes in activity and oligomycin-sensitivity during the cell cycle of catabolite-repressed and -de-repressed cells.","citation":"Biochem J 1977 Jan 15;162(1):39-46","abstract":"1. Changes in activity of ATPase (adenosine triphosphatase) during the cell cycle of Schizosaccharomyces pombe were analysed in cell-free extracts of cells harvested from different stages of growth of synchronous cultures and also after cell-cycle fractionation. 2. Oligomycin-sensitive ATPase oscillates in both glucose-repressed synchronous cultures and shows four maxima of activity approximately equally spaced through the cell cycle. The amplitude of the oscillations accounts for between 13 and 80% of the total activity at different times in the cell cycle. 3. Oligomycin sensitivity varies over a fourfold range at different stages of the cell cycle. 4. The periodicity of maximum oligomycin sensitivity is one-quarter of a cell cycle. 5. These results were confirmed for the first three-quarters of the cell cycle by cell-cycle fractionation. 6. In cells growing synchronously with glycerol, ATPase activity increases in a stepwise pattern, with two steps per cell cycle; the first of these occurs at 0.54 of the cell cycle and the second at 0.95. 7. These results are discussed in relation to previously obtained data on the development of mitochondrial activities during the cell cycle.","authors":"Edwards SW, Lloyd D","authors_abbrev":"Edwards SW et al.","pubmed_publication_date":"15 Jan 1977","pubmed_entrez_date":"1977-01-15","publication_year":"1977","canto_session_key":"c077589625a3805a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-24 10:52:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-24 10:52:19","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-24"},{"uniquename":"PMID:33683349","title":"The fission yeast S-phase cyclin Cig2 can drive mitosis.","citation":"Genetics 2021 Mar 03;217(1):1-12","abstract":"Commitment to mitosis is regulated by cyclin-dependent kinase (CDK) activity. In the fission yeast Schizosaccharomyces pombe, the major B-type cyclin, Cdc13, is necessary and sufficient to drive mitotic entry. Furthermore, Cdc13 is also sufficient to drive S phase, demonstrating that a single cyclin can regulate alternating rounds of replication and mitosis, and providing the foundation of the quantitative model of CDK function. It has been assumed that Cig2, a B-type cyclin expressed only during S phase and incapable of driving mitosis in wild-type cells, was specialized for S-phase regulation. Here, we show that Cig2 is capable of driving mitosis. Cig2/CDK activity drives mitotic catastrophe-lethal mitosis in inviably small cells-in cells that lack CDK inhibition by tyrosine-phosphorylation. Moreover, Cig2/CDK can drive mitosis in the absence of Cdc13/CDK activity and constitutive expression of Cig2 can rescue loss of Cdc13 activity. These results demonstrate that in fission yeast, not only can the presumptive M-phase cyclin drive S phase, but the presumptive S-phase cyclin can drive M phase, further supporting the quantitative model of CDK function. Furthermore, these results provide an explanation, previously proposed on the basis of computational analyses, for the surprising observation that cells expressing a single-chain Cdc13-Cdc2 CDK do not require Y15 phosphorylation for viability. Their viability is due to the fact that in such cells, which lack Cig2/CDK complexes, Cdc13/CDK activity is unable to drive mitotic catastrophe.","doi":"10.1093/genetics/iyaa002","authors":"Pickering M, Magner M, Keifenheim D, Rhind N","authors_abbrev":"Pickering M et al.","pubmed_publication_date":"03 Mar 2021","pubmed_entrez_date":"2021-03-08","publication_year":"2021","canto_session_key":"ab08277b7b3bc9c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nick Rhind","canto_first_approved_date":"2021-04-13 09:03:52","canto_approved_date":"2023-10-09 08:57:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-22 12:44:35","canto_added_date":"2021-03-10 01:15:04","annotation_curators":[{"name":"Nick Rhind","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC660.14","SPCC18B5.03","SPAPB2B4.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2021-04-13"},{"uniquename":"PMID:24876389","title":"Fission yeast arrestin-related trafficking adaptor, Arn1/Any1, is ubiquitinated by Pub1 E3 ligase and regulates endocytosis of Cat1 amino acid transporter.","citation":"Biol Open 2014 May 29;3(6):542-52","abstract":"The Tsc1-Tsc2 complex homologous to human tuberous sclerosis complex proteins governs amino acid uptake by regulating the expression and intracellular distribution of amino acid transporters in Schizosaccharomyces pombe. Here, we performed a genetic screening for molecules that are involved in amino acid uptake and found Arn1 (also known as Any1). Arn1 is homologous to ART1, an arrestin-related trafficking adaptor (ART) in Saccharomyces cerevisiae, and contains a conserved arrestin motif, a ubiquitination site, and two PY motifs. Overexpression of arn1(+) confers canavanine resistance on cells, whereas its disruption causes hypersensitivity to canavanine. We also show that Arn1 regulates endocytosis of the Cat1 amino acid transporter. Furthermore, deletion of arn1(+) suppresses a defect of amino acid uptake and the aberrant Cat1 localization in tsc2Δ. Arn1 interacts with and is ubiquitinated by the Pub1 ubiquitin ligase, which is necessary to regulate Cat1 endocytosis. Cat1 undergoes ubiquitinations on lysine residues within the N-terminus, which are mediated, in part, by Arn1 to determine Cat1 localization. Correctively, Arn1 is an ART in S. pombe and contributes to amino acid uptake through regulating Cat1 endocytosis in which Tsc2 is involved.","doi":"10.1242/bio.20148367","authors":"Nakashima A, Kamada S, Tamanoi F, Kikkawa U","authors_abbrev":"Nakashima A et al.","pubmed_publication_date":"29 May 2014","pubmed_entrez_date":"2014-05-31","publication_year":"2014","canto_session_key":"7fae84167ce708af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Akio Nakashima","canto_first_approved_date":"2019-01-30 18:16:02","canto_approved_date":"2026-04-22 21:39:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-01 12:26:01","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Akio Nakashima","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC869.11","SPBC18H10.20c","SPAC630.13c","SPAC11G7.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-01-30"},{"uniquename":"PMID:17219024","title":"Telomeres in meiotic recombination: the yeast side story.","citation":"Cell Mol Life Sci 2007 Jan;64(2):125-30","abstract":"The aim of this review is threefold. First, we want to report on recent observations on the role of telomeres in the alignment of homolog and non-homologues in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe and the relationship of early telomere clustering to later recombination events. Second, we compare the similarities and differences between synaptic and asynaptic yeasts. Third, we report on the increasing evidence of the effect of meiosis on telomeric sequences that suggest an induction of a specific form of recombination processes termed telomere rapid deletion.","authors":"Joseph I, Lustig AJ","authors_abbrev":"Joseph I et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2007-01-16","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1313771","title":"A mouse cdc25 homolog is differentially and developmentally expressed.","citation":"Genes Dev 1992 Apr;6(4):578-90","abstract":"The timing and activation of the p34cdc2 kinase in mammals is associated with dephosphorylation of phosphotyrosine and phosphothreonine residues on the p34cdc2 kinase. For fission yeast, the timing of mitosis is regulated by cyclic accumulation of cdc25, which promotes dephosphorylation of p34cdc2 and concomitant protein kinase activation. We report the identification and characterization of a structural and functional mouse homolog, Cdc25M2, of the cdc25 phosphatase. Cdc25M2 shows high sequence identity to the previously reported human homolog cdc25Hu2. Cdc25M2 can functionally complement for a Schizosaccharomyces pombe cdc25ts mutation, and when expressed in Escherichia coli and purified, Cdc25M2 is an active phosphatase. cdc25M2 mRNA shows variation in expression in different tissues in the mouse embryo and is expressed in a developmental and cell-cycle-dependent fashion. We suggest that the expression and accumulation of the cdc25 mitotic inducer may play a critical role in the regulation of mouse development.","authors":"Kakizuka A, Sebastian B, Borgmeyer U, Hermans-Borgmeyer I, Bolado J, Hunter T, Hoekstra MF, Evans RM","authors_abbrev":"Kakizuka A et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"064ef25b05be7b4f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 11:43:07","canto_session_submitted_date":"2012-03-03 11:42:14","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"EMBL:AU007954","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27063594","title":"Cell length growth patterns in fission yeast reveal a novel size control mechanism operating in late G2 phase.","citation":"Biol Cell 2016 Sep;108(9):259-77","abstract":"Because cylindrically shaped fission yeast cells grow exclusively at their tips, cell volume is proportional to length and can be easily monitored by time-lapse microscopy. Here, we analysed the growth pattern of individual cells from several fission yeast strains to determine the growth function that describes them most adequately and to perform size control studies.\nThe growth pattern of most cells during their growth period is best described by a bilinear function (i.e., two linear segments of different growth rates separated by a rate-change point). Linear growth patterns were also observed in several cases, but exponential ones only rarely. Since the bilinear patterns are separated into two segments by a breakpoint, we examined the existence of size control by regression analyses of the appropriate growth parameters in both segments. This confirmed the existence of known size controls in late G1, mid-G2 and late G2 during the fission yeast cycle. The present analyses also revealed that, contrary to the commonly accepted current view, late G2 size control is a general characteristic third event in the cycle. The level of the critical late G2 size that needs to be reached in an individual fission yeast cell is influenced by the growth rate of the cell in a manner similar to budding yeast, suggesting an evolutionary conserved mechanism.\nThe present study of individual cell growth patterns in wild-type and several cell cycle mutant fission yeast strains confirmed that, for most cells, growth is best described by a bilinear function. Three different size control mechanisms were found to operate in the different strains, and, as a novel observation, cell size was always found to be monitored before mitotic onset, irrespective of the existence of any earlier size checkpoints.\nStudying the pattern of growth and the mechanism of size control helps to clarify the connections between cell growth and division, since their coordination must work properly to maintain size homeostasis. In this study, we argue that most individual fission yeast cells grow following a bilinear pattern, and we confirm the existence of three different size control mechanisms.","doi":"10.1111/boc.201500066","authors":"Horváth A, Rácz-Mónus A, Buchwald P, Sveiczer Á","authors_abbrev":"Horváth A et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-04-12","publication_year":"2016","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2016-04-13 00:15:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25774602","title":"Rapid epigenetic adaptation to uncontrolled heterochromatin spreading.","citation":"Elife 2015 Mar 16;4","abstract":"Heterochromatin, a highly compact chromatin state characterized by histone H3K9 methylation and HP1 protein binding, silences the underlying DNA and influences the expression of neighboring genes. However, the mechanisms that regulate heterochromatin spreading are not well understood. In this study, we show that the conserved Mst2 histone acetyltransferase complex in fission yeast regulates histone turnover at heterochromatin regions to control heterochromatin spreading and prevents ectopic heterochromatin assembly. The combined loss of Mst2 and the JmjC domain protein Epe1 results in uncontrolled heterochromatin spreading and massive ectopic heterochromatin, leading to severe growth defects due to the inactivation of essential genes. Interestingly, these cells quickly recover by accumulating heterochromatin at genes essential for heterochromatin assembly, leading to their reduced expression to restrain heterochromatin spreading. Our studies discover redundant pathways that control heterochromatin spreading and prevent ectopic heterochromatin assembly and reveal a fast epigenetic adaptation response to changes in heterochromatin landscape.","doi":"10.7554/eLife.06179","authors":"Wang J, Reddy BD, Jia S","authors_abbrev":"Wang J et al.","pubmed_publication_date":"16 Mar 2015","pubmed_entrez_date":"2015-03-17","publication_year":"2015","canto_session_key":"a5b8cd021280b981","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-07 17:35:10","canto_approved_date":"2021-11-03 19:31:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-07 17:35:04","canto_added_date":"2015-03-18 01:15:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c","SPCC11E10.08","SPAC664.01c","SPBC428.07","SPCC622.16c","SPBC16E9.12c","SPCC736.12c","SPBC17D11.04c","SPBC428.08c","SPAC17G8.13c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2016-10-07"},{"uniquename":"PMID:32355220","title":"DNA replication machinery prevents Rad52-dependent single-strand annealing that leads to gross chromosomal rearrangements at centromeres.","citation":"Commun Biol 2020 Apr 30;3(1):202","abstract":"Homologous recombination between repetitive sequences can lead to gross chromosomal rearrangements (GCRs). At fission yeast centromeres, Rad51-dependent conservative recombination predominantly occurs between inverted repeats, thereby suppressing formation of isochromosomes whose arms are mirror images. However, it is unclear how GCRs occur in the absence of Rad51 and how GCRs are prevented at centromeres. Here, we show that homology-mediated GCRs occur through Rad52-dependent single-strand annealing (SSA). The rad52-R45K mutation, which impairs SSA activity of Rad52 protein, dramatically reduces isochromosome formation in rad51 deletion cells. A ring-like complex Msh2-Msh3 and a structure-specific endonuclease Mus81 function in the Rad52-dependent GCR pathway. Remarkably, mutations in replication fork components, including DNA polymerase α and Swi1/Tof1/Timeless, change the balance between Rad51-dependent recombination and Rad52-dependent SSA at centromeres, increasing Rad52-dependent SSA that forms isochromosomes. Our results uncover a role of DNA replication machinery in the recombination pathway choice that prevents Rad52-dependent GCRs at centromeres.","doi":"10.1038/s42003-020-0934-0","authors":"Onaka AT, Su J, Katahira Y, Tang C, Zafar F, Aoki K, Kagawa W, Niki H, Iwasaki H, Nakagawa T","authors_abbrev":"Onaka AT et al.","pubmed_publication_date":"30 Apr 2020","pubmed_entrez_date":"2020-05-02","publication_year":"2020","canto_session_key":"845e17d046d8c896","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takuro Nakagawa","canto_first_approved_date":"2020-07-01 15:03:54","canto_approved_date":"2025-09-04 12:45:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-27 15:25:26","canto_added_date":"2020-05-03 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Takuro Nakagawa","community_curator":true,"annotation_count":42,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.01c","SPAC644.14c","SPBC25H2.13c","SPCC4G3.05c","SPAC3H5.06c","SPBC216.06c","SPAC664.01c","SPCC285.16c","SPBC14C8.07c","SPAC30D11.10","SPBC1703.04","SPAC15A10.03c","SPCC553.09c","SPBC119.14","SPCC338.16","SPAC8F11.03"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2020-07-01"},{"uniquename":"PMID:33674718","title":"lncRNA transcription induces meiotic recombination through chromatin remodelling in fission yeast.","citation":"Commun Biol 2021 Mar 05;4(1):295","abstract":"Noncoding RNAs (ncRNAs) are involved in various biological processes, including gene expression, development, and disease. Here, we identify a novel consensus sequence of a cis-element involved in long ncRNA (lncRNA) transcription and demonstrate that lncRNA transcription from this cis-element activates meiotic recombination via chromatin remodeling. In the fission yeast fbp1 gene, glucose starvation induces a series of promoter-associated lncRNAs, referred to as metabolic-stress-induced lncRNAs (mlonRNAs), which contribute to chromatin remodeling and fbp1 activation. Translocation of the cis-element required for mlonRNA into a well-characterized meiotic recombination hotspot, ade6-M26, further stimulates transcription and meiotic recombination via local chromatin remodeling. The consensus sequence of this cis-element (mlon-box) overlaps with meiotic recombination sites in the fission yeast genome. At one such site, the SPBC24C6.09c upstream region, meiotic double-strand break (DSB) formation is induced in an mlon-box-dependent manner. Therefore, mlonRNA transcription plays a universal role in chromatin remodeling and the regulation of transcription and recombination.","doi":"10.1038/s42003-021-01798-8","authors":"Senmatsu S, Asada R, Oda A, Hoffman CS, Ohta K, Hirota K","authors_abbrev":"Senmatsu S et al.","pubmed_publication_date":"05 Mar 2021","pubmed_entrez_date":"2021-03-06","publication_year":"2021","canto_session_key":"e23661ed8a70f16d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-03-08 01:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16860728","title":"Cell polarity: formin on the move.","citation":"Curr Biol 2006 Jul 25;16(14):R535-8","abstract":"Formins assemble actin filaments that are typically arranged in long bundles. A new study has discovered that a fission yeast polarity formin transiently assembles short actin filaments at the cell tip, and then releases from the cortex and rides into the cell interior on filaments within the bundle.","authors":"Kovar DR","authors_abbrev":"Kovar DR","pubmed_publication_date":"25 Jul 2006","pubmed_entrez_date":"2006-07-25","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1867471","title":"Ultrastructure and cell wall composition in cell division cycle mutants of Schizosaccharomyces pombe deficient in septum formation.","citation":"Antonie Van Leeuwenhoek 1991 Apr;59(3):155-65","abstract":"A number of temperature-sensitive cdc- mutants of Schizosaccharomyces pombe that are affected in septum formation were analyzed with respect to their ultrastructure and the composition of their cell wall polymers. One mutant strain, cdc 16-116, has a cell wall composition similar to the wild type (strain 972 h-). However two other mutants, cdc 4 and cdc 7, show a higher galactomannan content and a lower alpha-glucan content. In all the mutants tested, total glucose incorporation, protein, RNA and DNA synthesis increased similarly to wild type over 3 1/2 h. After 2-3 h of incubation at the non permissive temperature -35 degrees C-, cell numbers remained constant although, increases in optical densities at 600 nm were observed. According to scanning electron microscopy, the mutants had aberrant shapes after 5 h of incubation at 35 degrees C. Transmission electron microscopy showed that cdc 3 is unable to complete septum formation. cdc 4 showed the most varied morphological shapes and aberrant depositions of cell wall material. cdc 8 exhibited a deranged plasma membrane and cell wall regions near of cell poles; an abnormal septum and several nuclei. cdc 7 showed elongated cells with several nuclei and with an apparently normal cell wall completely lacking in septum and septal material. cdc 16 showed more than one septum per cell.","authors":"Mateos P, Domínguez A","authors_abbrev":"Mateos P et al.","pubmed_publication_date":"Apr 1991","pubmed_entrez_date":"1991-04-01","publication_year":"1991","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18219492","title":"The Tsc/Rheb signaling pathway controls basic amino acid uptake via the Cat1 permease in fission yeast.","citation":"Mol Genet Genomics 2008 May;279(5):441-50","abstract":"The Tsc/Rheb signaling pathway plays critical roles in the control of growth and cell cycle. Studies in fission yeast have also implicated its importance in the regulation of amino acid uptake. Disruption of tsc2+, one of the tsc+ genes, has been shown to result in decreased arginine uptake and resistance to canavanine. A similar effect is also seen with other basic amino acids. We have identified a permease responsible for the uptake of basic amino acids by genetic complementation and disruption. SPAC869.11 (termed Cat1 for cationic amino acid transporter) contains 12 predicted transmembrane domains and its overexpression in wild type fission yeast leads to the increased uptake of basic amino acids and sensitivity to canavanine. Disruption of cat1+ in the deltatsc2 background interfered with the suppression of the canavanine-resistant phenotype of Atsc2 mutants by a dominant negative Rheb. In deltatsc2 mutant strains, the amount of Cat1 was not altered, but instead was mislocalized. This mislocalization was suppressed by the expression of dominant negative Rheb. In addition, we found that the loss of the E3 ubiquitin ligase, Pub1, also restores proper localization. These results provide a crucial link between Tsc/Rheb signaling and the regulation of the basic amino acid permease in fission yeast.","doi":"10.1007/s00438-008-0320-y","authors":"Aspuria PJ, Tamanoi F","authors_abbrev":"Aspuria PJ et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-01-26","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC869.11","SPBC428.16c","SPAC630.13c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:289891","title":"2 micrometer covalently closed non-mitochondrial circular DNA in the petite-negative yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1979 May 04;172(2):165-9","abstract":"A population of small covalently closed non-mitochondrial circular DNA molecules was isolated from the petite-negative yeast Schizosaccharomyces pombe. The mean length of these molecules, possessing the same density as nuclear DNA (1.695 g/cm3) is 1.95 +/- 0.18 micrometer. The presence of these minicircles in crude mitochondrial preparations indicates their tight association with mitochondrial particles. Their disappearance after DNase treatment of mitochondria demonstrates their extramitochondrial location.","authors":"Del Giudice L, Wolf K, Sassone-Corsi P, Mazza A","authors_abbrev":"Del Giudice L et al.","pubmed_publication_date":"04 May 1979","pubmed_entrez_date":"1979-05-04","publication_year":"1979","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39638797","title":"The Greatwall-Endosulfine-PP2A/B55 pathway regulates entry into quiescence by enhancing translation of Elongator-tunable transcripts.","citation":"Nat Commun 2024 Dec 05;15(1):10603","abstract":"Quiescent cells require a continuous supply of proteins to maintain protein homeostasis. In fission yeast, entry into quiescence is triggered by nitrogen stress, leading to the inactivation of TORC1 and the activation of TORC2. In this study, we demonstrate that the Greatwall-Endosulfine-PPA/B55 pathway connects the downregulation of TORC1 with the upregulation of TORC2, resulting in the activation of Elongator-dependent tRNA modifications crucial for sustaining the translation programme during entry into quiescence. This mechanism promotes U 34  and A 37  tRNA modifications at the anticodon stem loop, enhancing translation efficiency and fidelity of mRNAs enriched for AAA versus AAG lysine codons. Notably, several of these mRNAs encode TORC1 inhibitors, TORC2 activators, tRNA modifiers, and proteins necessary for telomeric and subtelomeric functions. Therefore, we propose a mechanism by which cells respond to nitrogen stress at the level of translation, involving a coordinated interplay between tRNA epitranscriptome and biased codon usage.","doi":"10.1038/s41467-024-55004-4","authors":"Encinar Del Dedo J, Suárez MB, López-San Segundo R, Vázquez-Bolado A, Sun J, García-Blanco N, García P, Tricquet P, Chen JS, Dedon PC, Gould KL, Hidalgo E, Hermand D, Moreno S","authors_abbrev":"Encinar Del Dedo J et al.","pubmed_publication_date":"05 Dec 2024","pubmed_entrez_date":"2024-12-05","publication_year":"2024","canto_session_key":"ad091c96ef4fb84a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-12-07 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20919928","title":"Two-component mediated peroxide sensing and signal transduction in fission yeast.","citation":"Antioxid Redox Signal 2011 Jul 01;15(1):153-65","abstract":"Two-component related proteins play a major role in regulating the oxidative stress response in the fission yeast, Schizosaccharomyces pombe. For example, the peroxide-sensing Mak2 and Mak3 histidine kinases regulate H(2)O(2)-induced activation of the Sty1 stress-activated protein kinase pathway, and the Skn7-related response regulator transcription factor, Prr1, is essential for activation of the core oxidative stress response genes. Here, we investigate the mechanism by which the S. pombe two-component system senses H(2)O(2), and the potential role of two-component signaling in the regulation of Prr1. Significantly, we demonstrate that PAS and GAF domains present in the Mak2 histidine kinase are essential for redox-sensing and activation of Sty1. In addition, we find that Prr1 is required for the transcriptional response to a wide range of H(2)O(2) concentrations and, furthermore, that two-component regulation of Prr1 is specifically required for the response of cells to high levels of H(2)O(2). Significantly, this provides the first demonstration that the conserved two-component phosphorylation site on Skn7-related proteins influences resistance to oxidative stress and oxidative stress-induced gene expression. Collectively, these data provide new insights into the two-component mediated sensing and signaling mechanisms underlying the response of S. pombe to oxidative stress.","doi":"10.1089/ars.2010.3345","authors":"Quinn J, Malakasi P, Smith DA, Cheetham J, Buck V, Millar JB, Morgan BA","authors_abbrev":"Quinn J et al.","pubmed_publication_date":"01 Jul 2011","pubmed_entrez_date":"2010-10-06","publication_year":"2011","canto_session_key":"a73237e21c888959","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-04 11:13:46","canto_approved_date":"2026-01-27 14:10:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-23 10:36:31","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":52,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.14","SPBC725.02","SPCC757.07c","SPBC32F12.03c","SPBC3F6.03","SPAC27E2.09","SPCC74.06","SPAC1834.08","SPAC24B11.06c","SPBC887.10"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2017-08-04"},{"uniquename":"PMID:18047809","title":"Ectopic expression of mitochondria endonuclease Pnu1p from Schizosaccharomyces pombe induces cell death of the yeast.","citation":"J Biochem Mol Biol 2007 Nov 30;40(6):1095-9","abstract":"Endonuclease G (EndoG) is a mitochondrial non-specific nuclease that is highly conserved among the eukaryotes. Although the precise role of EndoG in mitochondria is not yet known, the enzyme is released from the mitochondria and digests nuclear DNA during apoptosis in mammalian cells. Schizosaccharomyces pombe has an EndoG homolog Pnu1p (previously named SpNuc1) that is produced as a precursor protein with a mitochondrial targeting sequence. During the sorting into mitochondria the signal sequence is cleaved to yield the functionally active endonuclease. From the analogy to EndoG, active extramitochondrial Pnu1p may trigger cell killing by degrading nuclear DNA. Here, we tested this possibility by expressing a truncated Pnu1p lacking the signal sequence in the extramitochondrial region of pnu1-deleted cells. The truncated Pnu1p was localized in the cytosol and nuclei of yeast cells. And ectopic expression of active Pnu1p led to cell death with fragmentation of nuclear DNA. This suggests that the Pnu1p is possibly involved in a certain type of yeast cell death via DNA fragmentation. Although expression of human Bak in S. pombe was lethal, Pnu1p nuclease is not necessary for hBak-induced cell death.","authors":"Oda K, Kawasaki N, Fukuyama M, Ikeda S","authors_abbrev":"Oda K et al.","pubmed_publication_date":"30 Nov 2007","pubmed_entrez_date":"2007-12-01","publication_year":"2007","canto_session_key":"cf1ee8bcd8481ca9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-22 16:02:48","canto_approved_date":"2020-11-03 16:39:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-04-27 17:58:25","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-22"},{"uniquename":"PMID:35743069","title":"Chl1, an ATP-Dependent DNA Helicase, Inhibits DNA:RNA Hybrids Formation at DSB Sites to Maintain Genome Stability in  S. pombe .","citation":"Int J Mol Sci 2022 Jun 14;23(12)","abstract":"As an ATP-dependent DNA helicase, human ChlR1/DDX11 (Chl1 in yeast) can unwind both DNA:RNA and DNA:DNA substrates in vitro. Studies have demonstrated that ChlR1 plays a vital role in preserving genome stability by participating in DNA repair and sister chromatid cohesion, whereas the ways in which the biochemical features of ChlR1 function in DNA metabolism are not well understood. Here, we illustrate that Chl1 localizes to double-strand DNA break (DSB) sites and restrains DNA:RNA hybrid accumulation at these loci. Mutation of Chl1 strongly impairs DSB repair capacity by homologous recombination (HR) and nonhomologous end-joining (NHEJ) pathways, and deleting RNase H further reduces DNA repair efficiency, which indicates that the enzymatic activities of Chl1 are needed in  Schizosaccharomyces pombe . In addition, we found that the Rpc37 subunit of RNA polymerase III (RNA Pol III) interacts directly with Chl1 and that deletion of Chl1 has no influence on the localization of Rpc37 at DSB site, implying the role of Rpc37 in the recruitment of Chl1 to this site.","doi":"10.3390/ijms23126631","authors":"He D, Du Z, Xu H, Bao X","authors_abbrev":"He D et al.","pubmed_publication_date":"14 Jun 2022","pubmed_entrez_date":"2022-06-24","publication_year":"2022","canto_session_key":"37f98db19ab81e11","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-06-26 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21089479","title":"[Replication fork stabilization by replication stress checkpoint control].","citation":"Tanpakushitsu Kakusan Koso 2009 Mar;54(4 Suppl):380-7","abstract":"","authors":"Tanaka K","authors_abbrev":"Tanaka K","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2010-11-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21046351","title":"Isolation of synthetic lethal mutations in the rsm1-null mutant of fission yeast.","citation":"J Microbiol 2010 Oct;48(5):701-5","abstract":"To identify mutations in genes that are genetically linked to rsm1, we performed a synthetic lethal genetic screen in the fission yeast, Schizosaccharomyces pombe. Four mutations that showed synthetic lethality in combination with the rsm1null allele were isolated from approximately 320,000 colonies and defined in three complementation groups. One mutant (SLrsm1) exhibited a significant accumulation of poly(A)(+) RNA in the nucleus under synthetic lethal conditions, while the rest had no mRNA export defects. In addition, some genes (spmex67, rae1, or mlo3) required for mRNA export complemented the growth defects of the identified mutants. These results suggest that the isolated mutants contain mutations in genes that are involved in mRNA export and/or pre-mRNA retention.","doi":"10.1007/s12275-010-0353-x","authors":"Moon D, Park YS, Kim CY, Yoon JH","authors_abbrev":"Moon D et al.","pubmed_publication_date":"Oct 2010","pubmed_entrez_date":"2010-11-04","publication_year":"2010","canto_session_key":"6ec559929f0ebf92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-02 11:30:27","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-02 11:30:05","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1753.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-12-02"},{"uniquename":"PMID:24215641","title":"New vectors for epitope tagging and gene disruption in Schizosaccharomyces pombe.","citation":"Biotechniques 2013 Nov;55(5):257-63","abstract":"We describe a series of new vectors for PCR-based epitope tagging and gene disruption in the fission yeast Schizosaccharomyces pombe, an exceptional model organism for the study of cellular processes. The vectors are designed for amplification of gene-targeting DNA cassettes and integration into specific genetic loci, allowing expression of proteins fused to 12 tandem copies of the Pk (V5) epitope or 5 tandem copies of the FLAG epitope with a glycine linker. These vectors are available with various antibiotic or nutritional markers and are useful for protein studies using biochemical and cell biological methods. We also describe new vectors for fluorescent protein-tagging and gene disruption using ura4MX6, LEU2MX6, and his3MX6 selection markers, allowing researchers in the S. pombe community to disrupt genes and manipulate genomic loci using primer sets already available for the widely used pFA6a-MX6 system. Our new vectors may also be useful for gene manipulation in Saccharomyces cerevisiae.","doi":"10.2144/000114100","authors":"Gadaleta MC, Iwasaki O, Noguchi C, Noma K, Noguchi E","authors_abbrev":"Gadaleta MC et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-11-13","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25688135","title":"Telomeres and centromeres have interchangeable roles in promoting meiotic spindle formation.","citation":"J Cell Biol 2015 Feb 16;208(4):415-28","abstract":"Telomeres and centromeres have traditionally been considered to perform distinct roles. During meiotic prophase, in a conserved chromosomal configuration called the bouquet, telomeres gather to the nuclear membrane (NM), often near centrosomes. We found previously that upon disruption of the fission yeast bouquet, centrosomes failed to insert into the NM at meiosis I and nucleate bipolar spindles. Hence, the trans-NM association of telomeres with centrosomes during prophase is crucial for efficient spindle formation. Nonetheless, in approximately half of bouquet-deficient meiocytes, spindles form properly. Here, we show that bouquet-deficient cells can successfully undergo meiosis using centromere-centrosome contact instead of telomere-centrosome contact to generate spindle formation. Accordingly, forced association between centromeres and centrosomes fully rescued the spindle defects incurred by bouquet disruption. Telomeres and centromeres both stimulate focal accumulation of the SUN domain protein Sad1 beneath the centrosome, suggesting a molecular underpinning for their shared spindle-generating ability. Our observations demonstrate an unanticipated level of interchangeability between the two most prominent chromosomal landmarks.","doi":"10.1083/jcb.201409058","authors":"Fennell A, Fernández-Álvarez A, Tomita K, Cooper JP","authors_abbrev":"Fennell A et al.","pubmed_publication_date":"16 Feb 2015","pubmed_entrez_date":"2015-02-18","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-02-19 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPAC6G9.13c","SPBC582.06c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:18680119","title":"A revisionist replicon model for higher eukaryotic genomes.","citation":"J Cell Biochem 2008 Oct 01;105(2):321-9","abstract":"The replicon model devised to explain replication control in bacteria has served as the guiding paradigm in the search for origins of replication in the more complex genomes of eukaryotes. In Saccharomyces cerevisiae, this model has proved to be extremely useful, leading to the identification of specific genetic elements (replicators) and the interacting initiator proteins that activate them. However, replication control in organisms ranging from Schizosaccharomyces pombe to mammals is far more fluid: only a small number of origins seem to represent classic replicators, while the majority correspond to zones of inefficient, closely spaced start sites none of which are indispensable for origin activity. In addition, it is apparent that the epigenetic state of a given sequence largely determines its ability to be used as a replication initiation site. These conclusions were arrived at over a period of three decades, and required the development of several novel replicon mapping techniques, as well as new ways of examining the chromatin architecture of any sequence of interest. Recently, methods have been elaborated for isolating all of the active origins in the genomes of higher eukaryotes en masse. Microarray analyses and more recent high-throughput sequencing technology will allow all the origins to be mapped onto the chromosomes of any organism whose genome has been sequenced. With the advent of whole-genome studies on gene expression and chromatin composition, the field is now positioned to define both the genetic and epigenetic rules that govern origin activity.","doi":"10.1002/jcb.21828","authors":"Hamlin JL, Mesner LD, Lar O, Torres R, Chodaparambil SV, Wang L","authors_abbrev":"Hamlin JL et al.","pubmed_publication_date":"01 Oct 2008","pubmed_entrez_date":"2008-08-06","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8771707","title":"Review: the Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts.","citation":"Yeast 1996 May;12(6):523-9","abstract":"All eight of the CCT1-CCT8 genes encoding the subunits of the Cct chaperonin complex in Saccharomyces cerevisiae have been identified, including three that were uncovered by the systematic sequencing of the yeast genome. Although most of the properties of the eukaryotic Cct chaperonin have been elucidated with mammalian systems in vitro, studies with S. cerevisiae conditional mutants revealed that Cct is required for assembly of microtubules and actin in vivo. Cct subunits from the other yeasts, Candida albicans and Schizosaccharomyces pombe, also have been identified from partial and complete DNA sequencing of genes. Cct8p from C. albicans, the only other completely sequenced Cct protein from a fungal species other than S. cerevisiae, is 72% and 61% similar to the S. cerevisiae and mouse Cct8 proteins, respectively.","authors":"Stoldt V, Rademacher F, Kehren V, Ernst JF, Pearce DA, Sherman F","authors_abbrev":"Stoldt V et al.","pubmed_publication_date":"May 1996","pubmed_entrez_date":"1996-05-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40484900","title":"Characterization of P-type H + -ATPase Pma1 inhibitors that extend chronological lifespan in fission yeast.","citation":"Mol Genet Genomics 2025 Jun 08;300(1):58","abstract":"Inhibition of the activity of Pma1, a widely conserved P-type proton exporting ATPase, has been shown to extend the chronological lifespan (CLS) in fission yeast Schizosaccharomyces pombe. To develop a specific inhibitor for Pma1 of S. pombe, we focused on Si01, a candidate inhibitor of Saccharomyces cerevisiae Pma1. First, we have established a method for synthesis of Si01 and then investigated its Pma1 inhibitory activity and lifespan extension effect in fission yeast. Second, we also synthesized derivatives of Si01 and determined the minimum structure required for inhibition of S. pombe Pma1. Here we showed that the inhibitory activity of Pma1 correlates with the effect of lifespan extension. Si01 reduced the activity of purified Pma1 protein and extended the CLS of not only fission yeast but also budding yeast. These results provide a molecular basis for understanding the mechanism of Pma1 inhibition and the potential for developing molecules that regulate lifespan.","doi":"10.1007/s00438-025-02264-4","authors":"Tamura M, Yamashita W, Hibi T, Inui S, Tanaka K, Ozako M, Shimasaki T, Ohtsuka H, Shibuya M, Yamamoto Y, Yokoshima S, Aiba H","authors_abbrev":"Tamura M et al.","pubmed_publication_date":"08 Jun 2025","pubmed_entrez_date":"2025-06-08","publication_year":"2025","canto_session_key":"a7cd1bf05d9ff4a2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_first_approved_date":"2026-02-24 20:42:08","canto_approved_date":"2026-02-24 20:42:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-02-13 09:40:14","canto_added_date":"2025-06-09 23:25:04","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":1,"orcid":"0000-0002-7775-0446","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2026-02-24"},{"uniquename":"PMID:9442273","title":"The value of lipid composition in the taxonomy of the Schizosaccharomycetales.","citation":"Antonie Van Leeuwenhoek 1997 Nov;72(4):327-35","abstract":"In this study, the lipid fractions i.e. neutral (NL), phospho-(PL) and glycolipids (GL) with associated fatty acids (FAs) of 54 strains, representing the Schizosaccharomycetales, were analyzed during stationary growth phase and compared. Trace amounts of linoleic acid (18:2) were present in most of the strains representing Schizosaccharomyces. An increased percentage 18:2 was observed in the PL fraction when compared to the NL fraction. This is possibly related to membranes requiring polyunsaturated FAs for fluidity. On the basis of the percentage oleic acid (18:1) and 18:2 FAs in the different lipid fractions, the Schizosaccharomycetales can clearly be divided into two groups i.e. Group 1 (represented by the genus Hasegawaea) comprising strains producing relatively large amounts of 18:2 and relatively low amounts of 18:1 when compared to Group 2 (represented by the genus Schizosaccharomyces comprising Schizosaccharomyces octosporus and Schizosaccharomyces pombe). These results are in accordance with 18S and 26S rRNA base sequence analyses and emphasize the difference between the genera Hasegawaea and Schizosaccharomyces. Utilizing gas chromatography-mass spectrometry analyses, it was found that these strains were all capable of producing gamma-linolenic acid. This further emphasizes the uniqueness of this order in the Dikaryomycota.","authors":"Jeffery J, Kock JL, Botha A, Coetzee DJ, Botes PJ","authors_abbrev":"Jeffery J et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-01-27","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20826805","title":"Fission yeast germinal center (GC) kinase Ppk11 interacts with Pmo25 and plays an auxiliary role in concert with the morphogenesis Orb6 network (MOR) in cell morphogenesis.","citation":"J Biol Chem 2010 Nov 05;285(45):35196-205","abstract":"How cell morphology and the cell cycle are coordinately regulated is a fundamental subject in cell biology. In fission yeast, 2 germinal center kinases (GCKs), Sid1 and Nak1, play an essential role in septation/cytokinesis and cell separation/cell polarity control, respectively, as components of the septation initiation network (SIN) and the morphogenesis Orb6 network (MOR). Here we show that a third GCK, Ppk11, is also required for efficient cell separation particularly, at a high temperature. Although Ppk11 is not essential for cell division, this kinase plays an auxiliary role in concert with MOR in cell morphogenesis. Ppk11 physically interacts with the MOR component Pmo25 and is localized to the septum, by which Ppk11 is crucial for Pmo25 targeting/accumulation to the septum. The conserved C-terminal WDF motif of Ppk11 is essential for both septum accumulation of Pmo25 and efficient cell separation. In contrast its kinase activity is required only for cell separation. Thus, both interaction of Ppk11 with Pmo25 and Ppk11 kinase activity are critical for efficient cell separation.","doi":"10.1074/jbc.M110.176867","authors":"Goshima T, Kume K, Koyano T, Ohya Y, Toda T, Hirata D","authors_abbrev":"Goshima T et al.","pubmed_publication_date":"05 Nov 2010","pubmed_entrez_date":"2010-09-10","publication_year":"2010","canto_session_key":"fc448a004fc8f2f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-18 22:07:46","canto_approved_date":"2023-05-19 20:59:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-18 22:07:35","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":53,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2C4.14c","SPAC821.12","SPBP19A11.04c","SPAC1834.06c","SPAC9G1.09","SPAC24B11.11c","SPAC20G8.05c","SPBC11B10.09","SPBC21.06c","SPBC17F3.02"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2016-10-18"},{"uniquename":"EMBL:SPU97399","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2186047","title":"Intramitotic controls in the fission yeast Schizosaccharomyces pombe: the effect of cell size on spindle length and the timing of mitotic events.","citation":"J Cell Biol 1990 May;110(5):1617-21","abstract":"We have used a new cinemicroscopy technique in combination with antitubulin immunofluorescence microscopy to investigate the timing of mitotic events in cells of the fission yeast Schizosaccharomyces pombe having lengths at division between 7 and 60 microns. Wild-type fission yeast cells divide at a length of 14 microns. Separation of daughter nuclei (anaphase B) proceeds at a rate of 1.6 +/- 0.2 microns min-1, until the spindle extends the length of the cell. Coincident with spindle depolymerization, the nuclei reverse direction and take up positions that will become the center of the two daughter cells. This post-mitotic nuclear migration occurs at a rate of 1.4 +/- 0.5 microns-1. In cells in which the weel+ gene is overexpressed fivefold and that have an average length at mitosis of 28 microns, the rate of nuclear separation was only slightly reduced but, as spindles in these cells measure 20-22 microns, the duration of anaphase B was extended by approximately 40%. By contrast, in the mutant weel.50, which divides at 7 microns, both the rate and duration of anaphase B were indistinguishable from wild type. Nuclei reach the ends of these cells earlier but remain there until a point corresponding to the time of postmitotic nuclear migration in wild type. Thus, the events of mitosis can be extended but not abbreviated. These results are discussed in terms of a mitotic termination control that monitors many different events, one of which is spindle elongation.","authors":"Hagan IM, Riddle PN, Hyams JS","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_session_key":"20d4154e6b32a4f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-13 07:29:26","canto_approved_date":"2019-06-14 12:56:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-13 07:29:14","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-05-13"},{"uniquename":"PMID:9988759","title":"Functional organization of two large subunits of the fission yeast Schizosaccharomyces pombe RNA polymerase II. Location of the catalytic sites.","citation":"J Biol Chem 1999 Feb 19;274(8):5104-13","abstract":"The catalytically competent transcription complex of RNA polymerase II from the fission yeast Schizosaccharomyces pombe was affinity labeled with photoreactive nucleotide analogues incorporated at 3' termini of nascent RNA chains. To locate the catalytic site for RNA polymerization, the labeled subunits were separated by SDS-polyacrylamide gel electrophoresis and subjected to partial proteolysis. After microsequencing of proteolytic fragments, a complex multidomain organization was indicated for both of the two large subunits, Rpb1 and Rpb2, with the most available sites of proteolysis in junctions between the conserved sequences among RNA polymerase from both prokaryotes and eukaryotes. The cross-linking studies indicate the following: (i) the 3' termini of growing RNA chains are most extensively cross-linked to the second largest subunit Rpb2 between amino acids 825 and 994; (ii) the regions 298-535 of Rpb2 and 614-917 of Rpb1 are cross-linked to less extents, suggesting that these regions are situated in the vicinity of the catalytic site. All these regions include the conserved sequences of RNA polymerases, and the catalytic site of Rpb2 belongs to an NH2-terminal part of its conserved sequence H.","authors":"Wlassoff WA, Kimura M, Ishihama A","authors_abbrev":"Wlassoff WA et al.","pubmed_publication_date":"19 Feb 1999","pubmed_entrez_date":"1999-02-13","publication_year":"1999","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23G3.01"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:31475990","title":"Navigating MARRVEL, a Web-Based Tool that Integrates Human Genomics and Model Organism Genetics Information.","citation":"J Vis Exp 2019 Aug 15;(150)","abstract":"Through whole-exome/genome sequencing, human geneticists identify rare variants that segregate with disease phenotypes. To assess if a specific variant is pathogenic, one must query many databases to determine whether the gene of interest is linked to a genetic disease, whether the specific variant has been reported before, and what functional data is available in model organism databases that may provide clues about the gene's function in human. MARRVEL (Model organism Aggregated Resources for Rare Variant ExpLoration) is a one-stop data collection tool for human genes and variants and their orthologous genes in seven model organisms including in mouse, rat, zebrafish, fruit fly, nematode worm, fission yeast, and budding yeast. In this Protocol, we provide an overview of what MARRVEL can be used for and discuss how different datasets can be used to assess whether a variant of unknown significance (VUS) in a known disease-causing gene or a variant in a gene of uncertain significance (GUS) may be pathogenic. This protocol will guide a user through searching multiple human databases simultaneously starting with a human gene with or without a variant of interest. We also discuss how to utilize data from OMIM, ExAC/gnomAD, ClinVar, Geno2MP, DGV and DECHIPHER. Moreover, we illustrate how to interpret a list of ortholog candidate genes, expression patterns, and GO terms in model organisms associated with each human gene. Furthermore, we discuss the value protein structural domain annotations provided and explain how to use the multiple species protein alignment feature to assess whether a variant of interest affects an evolutionarily conserved domain or amino acid. Finally, we will discuss three different use-cases of this website. MARRVEL is an easily accessible open access website designed for both clinical and basic researchers and serves as a starting point to design experiments for functional studies.","doi":"10.3791/59542","authors":"Wang J, Liu Z, Bellen HJ, Yamamoto S","authors_abbrev":"Wang J et al.","pubmed_publication_date":"15 Aug 2019","pubmed_entrez_date":"2019-09-03","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-09-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PB_REF:0000002","title":"Manual Ortholog Curation","abstract":"PomBase derives manually curated orthologs from a variety of sources. In some cases the consensus ortholog from the major ortholog predictors (Compara, Inparanoid, OrthoMCL) is used. Many distant orthologs have also been identified by PSI-BLAST matches that are uniformly one-to one across species (described in detail in reference [1]); these alignments have been submitted to the Pfam protein family database. Other ortholog predictions come from experimental data demonstrating functional correspondence or involving membership of corresponding complexes. These predictions are also aligned and submitted to Pfam before inclusion. PomBase's approach ensures that the breadth of coverage is greater than any individual prediction method, and includes many ortholog calls which are not detected by any automated method. Gradually, we will add and display supporting references for all orthology calls. [1] V. Wood (2006), Schizosaccharomyces pombe comparative genomics; from sequence to systems. In: Comparative Genomics Using Fungi as Models (P. Sunnerhagen and J. Piskur, eds.), Topics in Current Genetics 15:233-285.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11231017","title":"Schizosaccharomyces pombe och1(+) encodes alpha-1,6-mannosyltransferase that is involved in outer chain elongation of N-linked oligosaccharides.","citation":"FEBS Lett 2001 Jan 26;489(1):75-80","abstract":"The fission yeast Schizosaccharomyces pombe attaches an outer chain containing mannose and galactose to the N-linked oligosaccharides on many of its glycoproteins. We identified an S. pombe och1 mutant that did not synthesize the outer chains on acid phosphatase. The S. pombe och1(+) gene was a functional homolog of Saccharomyces cerevisiae OCH1, and its gene product (SpOch1p) incorporated alpha-1,6-linked mannose into pyridylaminated Man(9)GlcNAc(2), indicating that och1(+) encodes an alpha-1,6-mannosyltransferase. Our results indicate that SpOch1p is a key enzyme of outer chain elongation. The substrate specificity of SpOch1p was different from that of S. cerevisiae OCH1 gene product (ScOch1p), suggesting that SpOch1p may have a wider substrate specificity than that of ScOch1p.","authors":"Yoko-o T, Tsukahara K, Watanabe T, Hata-Sugi N, Yoshimatsu K, Nagasu T, Jigami Y","authors_abbrev":"Yoko-o T et al.","pubmed_publication_date":"26 Jan 2001","pubmed_entrez_date":"2001-03-07","publication_year":"2001","canto_session_key":"c4735d3b81a5d777","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-02 05:17:24","canto_approved_date":"2021-09-14 08:41:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-02 05:17:18","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-01-02"},{"uniquename":"PMID:7612397","title":"Ultrastructure of the cell wall of Schizosaccharomyces pombe following treatment with various glucanases.","citation":"J Struct Biol 1995;114(2):140-52","abstract":"The ultrastructure of isolated cell walls of Schizosaccharomyces pombe was studied by electron microscopy after treatment with the following purified enzymes: endo-beta-(1-->3)-glucanase, endo-beta-(-->6)-glucanase, and endo-alpha-(1-->3)-glucanase produced by Bacillus circulans; exo-beta-(1-->3)-glucanase and endo-beta-(1-->3)-glucanase produced by Schizosaccharomyces japonicus var. versatilis. The exo-beta-(1-->3)-glucanase had no detectable effect on the walls, but amorphous wall material was removed by action of the endo-beta-(1-->3)- and endo-beta-(1-->6)-glucanases of B. circulans to reveal a wall component consisting of densely interwoven microfibrils. The fibrils were hydrolyzed by treatment with the Schiz. japonicus endo-beta-(1-->3)-glucanase followed by B. circulans endo-alpha-(1-->3)-glucanase--suggesting that they were composed of -beta-(1-->3)-linked glucan and alpha-(1-->3)-linked glucan. The presence of a fibrillar component in untreated walls was evident after negative staining.","authors":"Kopecká M, Fleet GH, Phaff HJ","authors_abbrev":"Kopecká M et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17614787","title":"Lessons learned from studies of fission yeast mating-type switching and silencing.","citation":"Annu Rev Genet 2007;41:213-36","abstract":"Stably maintaining specific states of gene expression during cell division is crucial for cellular differentiation. In fission yeast, such patterns result from directed gene rearrangements and chromosomally inherited epigenetic gene control mechanisms that control mating cell type. Recent advances have shown that a specific DNA strand at the mat1 locus is \"differentiated\" by a novel strand-specific imprint so that nonequivalent sister chromatids are produced. Therefore, cellular differentiation is a natural consequence of the fact that DNA strands are complementary and nonequivalent. Another epigenetic control that \"silences\" library copies of mat-information is due to heterochromatin organization. This is a clear case where Mendel's gene is composed of DNA plus the associated epigenetic moiety. Following up on initial genetic studies with more recent molecular investigations, this system has become one of the prominent models to understand mechanisms of gene regulation, genome integrity, and cellular differentiation. By applying lessons learned from these studies, such epigenetic gene control mechanisms, which must be installed in somatic cells, might explain mechanisms of cellular differentiation and development in higher eukaryotes.","authors":"Klar AJ","authors_abbrev":"Klar AJ","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-07-07","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27035982","title":"Functional architecture of the Reb1-Ter complex of Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 2016 Apr 19;113(16):E2267-76","abstract":"Reb1 ofSchizosaccharomyces pomberepresents a family of multifunctional proteins that bind to specific terminator sites (Ter) and cause polar termination of transcription catalyzed by RNA polymerase I (pol I) and arrest of replication forks approaching the Ter sites from the opposite direction. However, it remains to be investigated whether the same mechanism causes arrest of both DNA transactions. Here, we present the structure of Reb1 as a complex with a Ter site at a resolution of 2.7 Å. Structure-guided molecular genetic analyses revealed that it has distinct and well-defined DNA binding and transcription termination (TTD) domains. The region of the protein involved in replication termination is distinct from the TTD. Mechanistically, the data support the conclusion that transcription termination is not caused by just high affinity Reb1-Ter protein-DNA interactions. Rather, protein-protein interactions between the TTD with the Rpa12 subunit of RNA pol I seem to be an integral part of the mechanism. This conclusion is further supported by the observation that double mutations in TTD that abolished its interaction with Rpa12 also greatly reduced transcription termination thereby revealing a conduit for functional communications between RNA pol I and the terminator protein.","doi":"10.1073/pnas.1525465113","authors":"Jaiswal R, Choudhury M, Zaman S, Singh S, Santosh V, Bastia D, Escalante CR","authors_abbrev":"Jaiswal R et al.","pubmed_publication_date":"19 Apr 2016","pubmed_entrez_date":"2016-04-02","publication_year":"2016","canto_session_key":"a964074ea4198275","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-21 19:07:02","canto_approved_date":"2026-02-16 16:40:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-20 09:09:03","canto_added_date":"2016-04-03 00:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.11c","SPCC1259.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-11-21","pdb_entries":[{"pdb_id":"5eyb","gene_chains":[{"gene_uniquename":"SPBC1198.11c","chain":"A/B","position":"146-504"}],"title":"X-ray Structure of Reb1-Ter Complex","entry_authors":"Jaiswal R,Choudhury M,Zaman S,Singh S,Santosh V,Bastia D,Escalante CR","entry_authors_abbrev":"Jaiswal R et al.","reference_uniquename":"PMID:27035982","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:20485751","title":"Deletion of btn1, an orthologue of CLN3, increases glycolysis and perturbs amino acid metabolism in the fission yeast model of Batten disease.","citation":"Mol Biosyst 2010 Jun;6(6):1093-102","abstract":"The neuronal ceroid lipofuscinoses (NCLs) constitute a group of autosomal recessive neurodegenerative diseases affecting children. To date, the disease pathogenesis remains unknown, although the role of lysosomal impairment is widely recognized across the different diseases. Recently, the creation of simple models of juvenile NCL (Batten disease) has provided additional insights into the disease mechanism at the molecular level. We report defects in metabolism identified in the Schizosacchromyces pombe yeast model, where btn1, the orthologue of CLN3, has been deleted, using a metabolomics approach based on high resolution 1H and 13C NMR spectroscopy. Such changes represent the first documented metabolic changes associated with deletion of btn1. A decrease in extracellular glucose and increases in the concentration of extracellular ethanol and alanine labelling demonstrate increased glycolytic flux that may arise from vacuolar impairment, whilst amino acid changes were detected which were also in accordance with defective vacuolar functionality. That these changes were detected using a metabolomic based approach advocates its use to further analyse other yeast models of human disease to better understand the function of orthologue genes.","doi":"10.1039/b915670d","authors":"Pears MR, Codlin S, Haines RL, White IJ, Mortishire-Smith RJ, Mole SE, Griffin JL","authors_abbrev":"Pears MR et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-05-21","publication_year":"2010","canto_session_key":"d2471144913831bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-15 17:40:32","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-15 17:40:25","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC607.09c","SPBC1A4.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-10-15"},{"uniquename":"PMID:21502415","title":"Assembly and functions of heterochromatin in the fission yeast genome.","citation":"Cold Spring Harb Symp Quant Biol 2010;75:259-67","abstract":"In eukaryotic genomes, heterochromatin regulates various chromosomal processes including suppression of transcription and illegitimate recombination as well as proper segregation of chromosomes during cell division. Recent studies using the fission yeast Schizosaccharomyces pombe model system have revealed a complex interplay among RNA polymerase II transcription, RNAi machinery, and factors involved in posttranslational modifications of histones that are critical for the assembly and maintenance of heterochromatin. Heterochromatin proteins targeted to specific sites in the genome can spread across extended chromosomal domains and mediate epigenetic genome control by providing a recruitment platform for various factors including chromatin-modifying activities. In this chapter, we discuss mechanisms of heterochromatin assembly in fission yeast and highlight emerging evidence suggesting the involvement of heterochromatin factors in the suppression of noncoding RNAs across the genome.","doi":"10.1101/sqb.2010.75.055","authors":"Aygün O, Grewal SI","authors_abbrev":"Aygün O et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2011-04-20","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24186976","title":"Dual regulation of Dmc1-driven DNA strand exchange by Swi5-Sfr1 activation and Rad22 inhibition.","citation":"Genes Dev 2013 Nov 01;27(21):2299-304","abstract":"Both ubiquitously expressed Rad51 and meiosis-specific Dmc1 are required for crossover production during meiotic recombination. The budding yeast Rad52 and its fission yeast ortholog, Rad22, are \"mediators;\" i.e., they help load Rad51 onto ssDNA coated with replication protein A (RPA). Here we show that the Swi5-Sfr1 complex from fission yeast is both a mediator that loads Dmc1 onto ssDNA and a direct \"activator\" of DNA strand exchange by Dmc1. In stark contrast, Rad22 inhibits Dmc1 action by competing for its binding to RPA-coated ssDNA. Thus, Rad22 plays dual roles in regulating meiotic recombination: activating Rad51 and inhibiting Dmc1.","doi":"10.1101/gad.218693.113","authors":"Murayama Y, Kurokawa Y, Tsutsui Y, Iwasaki H","authors_abbrev":"Murayama Y et al.","pubmed_publication_date":"01 Nov 2013","pubmed_entrez_date":"2013-11-05","publication_year":"2013","canto_session_key":"281e81f28d87cf76","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroshi Iwasaki","canto_first_approved_date":"2016-11-11 11:24:00","canto_approved_date":"2025-09-04 06:44:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-05 03:21:50","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Hiroshi Iwasaki","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.13c","SPBC28F2.07","SPBC409.03","SPAC8E11.03c","SPAC30D11.10"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-11-11"},{"uniquename":"PANTHER:PTHR12418","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:26755","HGNC:17947","SPAC3A12.08","SPAPB2B4.06","SPBC26H8.11c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:17581129","title":"The (1,3)beta-D-glucan synthase subunit Bgs1p is responsible for the fission yeast primary septum formation.","citation":"Mol Microbiol 2007 Jul;65(1):201-17","abstract":"Cytokinesis is a crucial event in the cell cycle of all living cells. In fungal cells, it requires co-ordinated contraction of an actomyosin ring and synthesis of both plasmatic membrane and a septum structure that will constitute the new cell wall end. Schizosaccharomyces pombe contains four essential putative (1,3)beta-d-glucan synthase catalytic subunits, Bgs1p to Bgs4p. Here we examined the function of Bgs1p in septation by studying the lethal phenotypes of bgs1(+) shut-off and bgs1Delta cells and demonstrated that Bgs1p is responsible and essential for linear (1,3)beta-d-glucan and primary septum formation. bgs1(+) shut-off generates a more than 300-fold Bgs1p reduction, but the septa still present large amounts of disorganized linear (1,3)beta-d-glucan and partial primary septa. Conversely, both structures are absent in bgs1Delta cells, where there is no Bgs1p. The septum analysis of bgs1(+)-repressed cells indicates that linear (1,3)beta-d-glucan is necessary but not sufficient for primary septum formation. Linear (1,3)beta-d-glucan is the polysaccharide that specifically interacts with the fluorochrome Calcofluor white in fission yeast. We also show that in the absence of Bgs1p abnormal septa are formed, but the cells cannot separate and eventually die.","authors":"Cortés JC, Konomi M, Martins IM, Muñoz J, Moreno MB, Osumi M, Durán A, Ribas JC","authors_abbrev":"Cortés JC et al.","pubmed_publication_date":"Jul 2007","pubmed_entrez_date":"2007-06-22","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18375616","title":"Transcription factors Pcr1 and Atf1 have distinct roles in stress- and Sty1-dependent gene regulation.","citation":"Eukaryot Cell 2008 May;7(5):826-35","abstract":"The mitogen-activated protein kinase Sty1 is essential for the regulation of transcriptional responses that promote cell survival in response to different types of environmental stimuli in Schizosaccharomyces pombe. Upon stress activation, Sty1 reversibly accumulates in the nucleus, where it stimulates gene expression via the Atf1 transcription factor. The Atf1 protein forms a heterodimer with Pcr1, but the specific role of this association is controversial. We have carried out a comparative analysis of strains lacking these proteins individually. We demonstrate that Atf1 and Pcr1 have similar but not identical roles in S. pombe, since cells lacking Pcr1 do not share all the phenotypes reported for Deltaatf1 cells. Northern blot and microarray analyses demonstrate that the responses to specific stresses of cells lacking either Pcr1 or Atf1 do not fully overlap, and even though most Atf1-dependent genes induced by osmotic stress are also Pcr1 dependent, a subset of genes require only the presence of Atf1 for their induction. Whereas binding of Atf1 to most stress-dependent genes requires the presence of Pcr1, we demonstrate here that Atf1 can bind to the Pcr1-independent promoters in a Deltapcr1 strain in vivo. Furthermore, these analyses show that both proteins have a global repressive effect on stress-dependent and stress-independent genes.","doi":"10.1128/EC.00465-07","authors":"Sansó M, Gogol M, Ayté J, Seidel C, Hidalgo E","authors_abbrev":"Sansó M et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-04-01","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC21E11.03c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:895561","title":"[Infrared spectrum of yeast cell walls].","citation":"Mikrobiologiia 1977;46(3):521-4","abstract":"Infrared spectra of whole cells and cell walls were studied with Schizosaccharomyces pombe, Endomyces magnusii. Rhodotorula rubra, and Candida lipolytica. Qualitative analysis of the spectra and comparison of the spectra recorded for the cells and for their walls led to a conclusion that, contrary to the common viewpoint, an ir spectrum of the whole cell of any yeast species was determined by the components contained in the cell rather wall than by all components of the cell.","authors":"Zaslavskiĭ BIu, Guliaeva ND, Rogozhin SV","authors_abbrev":"Zaslavskiĭ BIu et al.","pubmed_publication_date":"1977","pubmed_entrez_date":"1977-05-01","publication_year":"1977","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012832","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23419716","title":"Fungal cell wall organization and biosynthesis.","citation":"Adv Genet 2013;81:33-82","abstract":"The composition and organization of the cell walls from Saccharomyces cerevisiae, Candida albicans, Aspergillus fumigatus, Schizosaccharomyces pombe, Neurospora crassa, and Cryptococcus neoformans are compared and contrasted. These cell walls contain chitin, chitosan, β-1,3-glucan, β-1,6-glucan, mixed β-1,3-/β-1,4-glucan, α-1,3-glucan, melanin, and glycoproteins as major constituents. A comparison of these cell walls shows that there is a great deal of variability in fungal cell wall composition and organization. However, in all cases, the cell wall components are cross-linked together to generate a cell wall matrix. The biosynthesis and properties of each of the major cell wall components are discussed. The chitin and glucans are synthesized and extruded into the cell wall space by plasma membrane-associated chitin synthases and glucan synthases. The glycoproteins are synthesized by ER-associated ribosomes and pass through the canonical secretory pathway. Over half of the major cell wall proteins are modified by the addition of a glycosylphosphatidylinositol anchor. The cell wall glycoproteins are also modified by the addition of O-linked oligosaccharides, and their N-linked oligosaccharides are extensively modified during their passage through the secretory pathway. These cell wall glycoprotein posttranslational modifications are essential for cross-linking the proteins into the cell wall matrix. Cross-linking the cell wall components together is essential for cell wall integrity. The activities of four groups of cross-linking enzymes are discussed. Cell wall proteins function as cross-linking enzymes, structural elements, adhesins, and environmental stress sensors and protect the cell from environmental changes.","doi":"10.1016/B978-0-12-407677-8.00002-6","authors":"Free SJ","authors_abbrev":"Free SJ","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-02-20","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011612","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9512560","title":"A common 40 amino acid motif in eukaryotic RNases H1 and caulimovirus ORF VI proteins binds to duplex RNAs.","citation":"Nucleic Acids Res 1998 Apr 01;26(7):1834-40","abstract":"Eukaryotic RNases H from Saccharomyces cerevisiae , Schizosaccharomyces pombe and Crithidia fasciculata , unlike the related Escherichia coli RNase HI, contain a non-RNase H domain with a common motif. Previously we showed that S.cerevisiae RNase H1 binds to duplex RNAs (either RNA-DNA hybrids or double-stranded RNA) through a region related to the double-stranded RNA binding motif. A very similar amino acid sequence is present in caulimovirus ORF VI proteins. The hallmark of the RNase H/caulimovirus nucleic acid binding motif is a stretch of 40 amino acids with 11 highly conserved residues, seven of which are aromatic. Point mutations, insertions and deletions indicated that integrity of the motif is important for binding. However, additional amino acids are required because a minimal peptide containing the motif was disordered in solution and failed to bind to duplex RNAs, whereas a longer protein bound well. Schizosaccharomyces pombe RNase H1 also bound to duplex RNAs, as did proteins in which the S.cerevisiae RNase H1 binding motif was replaced by either the C.fasciculata or by the cauliflower mosaic virus ORF VI sequence. The similarity between the RNase H and the caulimovirus domain suggest a common interaction with duplex RNAs of these two different groups of proteins.","authors":"Cerritelli SM, Fedoroff OY, Reid BR, Crouch RJ","authors_abbrev":"Cerritelli SM et al.","pubmed_publication_date":"01 Apr 1998","pubmed_entrez_date":"1998-05-30","publication_year":"1998","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10407269","title":"DNA sequencing and analysis of a 67.4 kb region from the right arm of Schizosaccharomyces pombe chromosome II reveals 28 open reading frames including the genes his5, pol5, ppa2, rip1, rpb8 and skb1.","citation":"Yeast 1999 Jul;15(10A):893-901","abstract":"67 393 bp of contiguous DNA located between markers cdc18 and cdc14 on the right arm of fission yeast chromosome II has been sequenced as part of the European Union Schizosaccharomyces pombe genome sequencing project. The complete sequence, contained in cosmid clones c15C4 and c21H7, has been determined on both strands. Sequence analysis shows that it contains 28 open reading frames capable of coding for proteins, 16 split by one or more introns, but no tRNA, rRNA or transposon sequences. The gene density is one per 2. 4 kb. Six genes have been previously described (his5, pol5, ppa2, rip1, rpb8 and skb1) and 22 are novel. Of the novel genes, 14 have significant similarity with proteins of known function, three have similarities with proteins of unknown function and five show no extensive similarities with known proteins. Sequence similarities suggest that three of the novel genes encode ATP-dependent RNA helicases, two encode transcription factor components and others encode a G-protein, a dehydrogenase, a Rab escort protein, an Abc1-like protein, a lipase, an ATP-binding transport protein, an amino acid permease, an acid phosphatase and a mannosyltransferase.","authors":"Xiang Z, Lyne MH, Wood V, Rajandream MA, Barrell BG, Aves SJ","authors_abbrev":"Xiang Z et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-17","publication_year":"1999","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF10232","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:19971","SPBC21.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7634333","title":"The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis.","citation":"Cell 1995 Aug 11;82(3):435-44","abstract":"The S. pombe cdc15 gene is essential for cell division. cdc15ts mutants do not form a septum, but growth and nuclear division continue, leading to formation of multinucleate cells. The earliest step in septum formation and cytokinesis, rearrangement of actin to the center of the cell, is associated with appearance of hypophosphorylated cdc15p and formation of a cdc15p ring, which colocalizes with actin. Loss of cdc15p function impairs formation of the actin ring. The abundance of cdc15 mRNA varies through the cell division cycle, peaking in early mitosis before septation. Expression of cdc15 in G2-arrested cells induces actin rearrangement to the center of the cell. These data implicate cdc15p as a key element in mediating the cytoskeletal rearrangements required for cytokinesis.","authors":"Fankhauser C, Reymond A, Cerutti L, Utzig S, Hofmann K, Simanis V","authors_abbrev":"Fankhauser C et al.","pubmed_publication_date":"11 Aug 1995","pubmed_entrez_date":"1995-08-11","publication_year":"1995","canto_session_key":"edebae52f6a8d212","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-10-28 16:32:47","canto_approved_date":"2021-01-22 16:28:42","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-03-06 12:12:30","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPAC20G8.05c","SPCC1739.11c","SPAP8A3.08","SPBC24C6.07"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-10-28"},{"uniquename":"PMID:3185514","title":"The role of sterility genes (ste and aff) in the initiation of sexual development in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1988 Aug;213(2-3):529-34","abstract":"Haploid homothallic strains of Schizosaccharomyces pombe with mutations in any of nine \"sterility genes\" (ste) do not mate with wild-type fertile strains. Those defective in genes ste1 to ste4 and ste7 to ste9 are also deficient in meiosis and sporulation. I found that the ste1, ste3 and ste8 genes act very early in the sexual development, presumably before the pat1-controlled conjugation-specific event. ste5 and ste6 exert their function downstream of pat1 in the initiation of conjugation and do not play any role in the meiotic pathway. ste2, ste4, ste7 and ste9 are involved in both sexual pathways: they seem to act downstream of pat1 in conjugation but upstream of pat1 in the initiation of meiosis. A new gene, aff1, whose defective allele suppresses the pat1-114-provoked haploid sporulation and arrest of vegetative growth is also described. It is supposed that the aff1+ gene product participates in a cascade of regulatory events, as a factor antagonistic to pat1.","authors":"Sipiczki M","authors_abbrev":"Sipiczki M","pubmed_publication_date":"Aug 1988","pubmed_entrez_date":"1988-08-01","publication_year":"1988","canto_session_key":"0633e53adb862559","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-06-15 15:46:00","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-05 15:50:11","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC1D4.13","SPAC1565.04c","SPCC1442.01","SPBC1D7.05","SPAC144.13c","SPAC23E2.03c","SPBC19C2.05","SPAC17H9.09c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2013-02-05"},{"uniquename":"PMID:19587793","title":"Essential role for Schizosaccharomyces pombe pik1 in septation.","citation":"PLoS One 2009 Jul 09;4(7):e6179","abstract":"Schizosaccharomyces pombe pik1 encodes a phosphatidylinositol 4-kinase, reported to bind Cdc4, but not Cdc4(G107S).\nGene deletion revealed that pik1 is essential. In cells with pik1 deleted, ectopic expression of a loss-of-function allele, created by fusion to a temperature-sensitive dihydrofolate reductase, allowed normal cell proliferation at 25 degrees C. At 36 degrees C, cells arrested with abnormally thick, misplaced or supernumerary septa, indicating a defect late in septation. In addition to being Golgi associated, ectopically expressed GFP-tagged Pik1 was observed at the medial cell plane late in cytokinesis. New alleles, created by site-directed mutagenesis, were expressed ectopically. Lipid kinase and Cdc4-binding activity assays were performed. Pik1(D709A) was kinase-dead, but bound Cdc4. Pik1(R838A) did not bind Cdc4, but was an active kinase. Genomic integration of these substitutions in S. pombe and complementation studies in Saccharomyces cerevisiae pik1-101 cells revealed that D709 is essential in both cases while R838 is dispensable. In S. pombe, ectopic expression of pik1 was dominantly lethal; while, pik1(D709A,R838A) was innocuous, pik1(R838A) was almost innocuous, and pik1(D709A) produced partial lethality and septation defects. The pik1 ectopic expression lethal phenotype was suppressed in cdc4(G107S). Thus, D709 is essential for kinase activity and septation.\nPik1 kinase activity is required for septation. The Pik1 R838 residue is required for important protein-protein interactions, possibly with Cdc4.","doi":"10.1371/journal.pone.0006179","authors":"Park JS, Steinbach SK, Desautels M, Hemmingsen SM","authors_abbrev":"Park JS et al.","pubmed_publication_date":"09 Jul 2009","pubmed_entrez_date":"2009-07-10","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9739083","title":"Cdc18p can block mitosis by two independent mechanisms.","citation":"J Cell Sci 1998 Oct;111 ( Pt 20):3101-8","abstract":"The DNA replication checkpoint is required to maintain the integrity of the genome, inhibiting mitosis until S phase has been successfully completed. The checkpoint preventing premature mitosis in Schizosaccharomyces pombe relies on phosphorylation of the tyrosine-15 residue on cdc2p to prevent its activation and hence mitosis. The cdc18 gene is essential for both generating the DNA replication checkpoint and the initiation of S phase, thus providing a key role for the overall control and coordination of the cell cycle. We show that the C terminus of the protein is capable of both initiating DNA replication and the checkpoint function of cdc18p. The C terminus of cdc18p acts upstream of the DNA replication checkpoint genes rad1, rad3, rad9, rad17, hus1 and cut5 and requires the wee1p/mik1p tyrosine kinases to block mitosis. The N terminus of cdc18p can also block mitosis but does so in the absence of the DNA replication checkpoint genes and the wee1p/mik1p kinases therefore acting downstream of these genes. Because the N terminus of cdc18p associates with cdc2p in vivo, we suggest that by binding the cdc2p/cdc13p mitotic kinase directly, it exerts an effect independently of the normal checkpoint control, probably in an unphysiological manner.","authors":"Greenwood E, Nishitani H, Nurse P","authors_abbrev":"Greenwood E et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-09-18","publication_year":"1998","canto_session_key":"52e0036cabf3303e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-03-26 10:04:37","canto_approved_date":"2022-12-12 15:45:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-16 13:17:05","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":71,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.13","SPAC1952.07","SPBC32F12.09","SPAC20G4.04c","SPBC11B10.09","SPBC582.03","SPBC660.14","SPAC23C4.18c","SPBC14C8.07c","SPCC18B5.03","SPAC664.07c","SPBC216.05"],"gene_count":12,"ltp_gene_count":10,"approved_date":"2018-03-26"},{"uniquename":"PMID:21310713","title":"Monitoring DNA replication in fission yeast by incorporation of 5-ethynyl-2'-deoxyuridine.","citation":"Nucleic Acids Res 2011 May;39(9):e60","abstract":"We report procedures to allow incorporation and detection of 5-ethynyl-2'-deoxyuridine (EdU) in fission yeast, a thymidine analogue which has some technical advantages over use of bromodeoxyuridine. Low concentrations of EdU (1 µM) are sufficient to allow detection of incorporation in cells expressing thymidine kinase and human equilibrative nucleoside transporter 1 (hENT1). However EdU is toxic and activates the rad3-dependent checkpoint, resulting in cell cycle arrest, potentially limiting its applications for procedures which require labelling over more than one cell cycle. Limited DNA synthesis, when elongation is largely blocked by hydroxyurea, can be readily detected by EdU incorporation using fluorescence microscopy. Thus EdU should be useful for detecting early stages of S phase, or DNA synthesis associated with DNA repair and recombination.","doi":"10.1093/nar/gkr063","authors":"Hua H, Kearsey SE","authors_abbrev":"Hua H et al.","pubmed_publication_date":"May 2011","pubmed_entrez_date":"2011-02-12","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36302945","title":"Ferrichrome, a fungal-type siderophore, confers high ammonium tolerance to fission yeast.","citation":"Sci Rep 2022 Oct 27;12(1):17411","abstract":"Microorganisms and plants produce siderophores, which function to transport environmental iron into cells as well as participate in cellular iron use and deposition. Their biological functions are diverse although their role in primary metabolism is poorly understood. Ferrichrome is a fungal-type siderophore synthesized by nonribosomal peptide synthetase (NRPS). Herein we show that ferrichrome induces adaptive growth of fission yeast on high ammonium media. Ammonium is a preferred nitrogen source as it suppresses uptake and catabolism of less preferred nitrogen sources such as leucine through a mechanism called nitrogen catabolite repression (NCR). Therefore, the growth of fission yeast mutant cells with leucine auxotrophy is suppressed in the presence of high concentrations of ammonium. This growth suppression was canceled by ferrichrome in a manner dependent on the amino acid transporter Cat1. Additionally, growth retardation of wild-type cells by excess ammonium was exacerbated by deleting the NRPS gene sib1, which is responsible for the biosynthesis of ferrichrome, suggesting that intrinsically produced ferrichrome functions in suppressing the metabolic action of ammonium. Furthermore, ferrichrome facilitated the growth of both wild-type and sib1-deficient cells under low glucose conditions. These results suggest that intracellular iron regulates primary metabolism, including NCR, which is mediated by siderophores.","doi":"10.1038/s41598-022-22108-0","authors":"Chiu PC, Nakamura Y, Nishimura S, Tabuchi T, Yashiroda Y, Hirai G, Matsuyama A, Yoshida M","authors_abbrev":"Chiu PC et al.","pubmed_publication_date":"27 Oct 2022","pubmed_entrez_date":"2022-10-27","publication_year":"2022","canto_session_key":"f836ef569847294d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shinichi Nishimura","canto_first_approved_date":"2023-05-23 16:08:58","canto_approved_date":"2023-05-23 16:08:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-04-11 09:36:33","canto_added_date":"2022-10-30 00:15:04","annotation_curators":[{"name":"Shinichi Nishimura","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18H10.20c","SPBC1A4.02c","SPAC23G3.02c","SPAC869.11","SPBC4F6.09","SPCC965.11c","SPAC11G7.02"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2023-05-23"},{"uniquename":"PMID:32657391","title":"The ortholog conjecture revisited: the value of orthologs and paralogs in function prediction.","citation":"Bioinformatics 2020 Jul 01;36(Suppl_1):i219-i226","abstract":"The computational prediction of gene function is a key step in making full use of newly sequenced genomes. Function is generally predicted by transferring annotations from homologous genes or proteins for which experimental evidence exists. The 'ortholog conjecture' proposes that orthologous genes should be preferred when making such predictions, as they evolve functions more slowly than paralogous genes. Previous research has provided little support for the ortholog conjecture, though the incomplete nature of the data cast doubt on the conclusions.\nWe use experimental annotations from over 40 000 proteins, drawn from over 80 000 publications, to revisit the ortholog conjecture in two pairs of species: (i) Homo sapiens and Mus musculus and (ii) Saccharomyces cerevisiae and Schizosaccharomyces pombe. By making a distinction between questions about the evolution of function versus questions about the prediction of function, we find strong evidence against the ortholog conjecture in the context of function prediction, though questions about the evolution of function remain difficult to address. In both pairs of species, we quantify the amount of information that would be ignored if paralogs are discarded, as well as the resulting loss in prediction accuracy. Taken as a whole, our results support the view that the types of homologs used for function transfer are largely irrelevant to the task of function prediction. Maximizing the amount of data used for this task, regardless of whether it comes from orthologs or paralogs, is most likely to lead to higher prediction accuracy.\nhttps://github.com/predragradivojac/oc.\nSupplementary data are available at Bioinformatics online.","doi":"10.1093/bioinformatics/btaa468","authors":"Stamboulian M, Guerrero RF, Hahn MW, Radivojac P","authors_abbrev":"Stamboulian M et al.","pubmed_publication_date":"01 Jul 2020","pubmed_entrez_date":"2020-07-14","publication_year":"2020","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2020-07-15 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9565672","title":"The gene for ribosomal protein L7a-1 in Schizosaccharomyces pombe contains an intron after the initiation codon.","citation":"Biochim Biophys Acta 1998 Apr 29;1397(2):146-50","abstract":"The gene encoding ribosomal protein L7a-1 in the fission yeast Schizosaccharomyces pombe is identified by the similarity of its open reading frame to the respective gene in Saccharomyces cerevisiae. The L7a gene is encoded in two different genomic environments as frequently found for ribosomal protein genes in this organism. One of these genes, L75a-1, is located on chromosome 2. The two consensus promoter elements homol D and homol E are both identified upstream of the start codon of this gene. The ATG start codon is separated from the main reading frame by an intron of 66 nucleotides.","authors":"Marchfelder A, Clayton DA, Brennicke A","authors_abbrev":"Marchfelder A et al.","pubmed_publication_date":"29 Apr 1998","pubmed_entrez_date":"1998-06-06","publication_year":"1998","canto_session_key":"1b7fe05d638c9998","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-29 12:20:46","canto_approved_date":"2019-11-29 12:20:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-29 12:20:40","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.04","SPBC18H10.12c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2019-11-29"},{"uniquename":"PMID:8692700","title":"The Schizosaccharomyces pombe pla1 gene encodes a poly(A) polymerase and can functionally replace its Saccharomyces cerevisiae homologue.","citation":"Nucleic Acids Res 1996 Jul 01;24(13):2585-91","abstract":"We have isolated the poly(A) polymerase (PAP) encoding gene pla1 [for poly(A) polymerase] from the fission yeast Schizosaccharomyces pombe. Protein sequence alignments with other poly(A) polymerases reveal that pla1 is more closely related to Saccharomyces cerevisiae PAP than to bovine PAP. The two yeast poly(A) polymerases share significant sequence homology not only in the generally conserved N-terminal part but also in the C-terminus. Furthermore, pla1 rescues a S. cerevisiae PAP1 disruption mutant. An extract from the complemented strain is active in the specific in vitro polyadenylation assay. In contrast, recombinant PLA1 protein can not replace bovine PAP in the mammalian in vitro polyadenylation assay. These results indicate a high degree of conservation of the polyadenylation machinery among the evolutionary diverged budding and fission yeasts.","authors":"Ohnacker M, Minvielle-Sebastia L, Keller W","authors_abbrev":"Ohnacker M et al.","pubmed_publication_date":"01 Jul 1996","pubmed_entrez_date":"1996-07-01","publication_year":"1996","canto_session_key":"41e7240019821ed5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-07-31 15:06:49","canto_approved_date":"2024-02-08 13:52:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 15:06:42","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC646.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:16233343","title":"Biosynthesis, bioproduction and novel roles of ubiquinone.","citation":"J Biosci Bioeng 2002;94(6):511-7","abstract":"Ubiquinone (coenzyme Q) is a well-known component of the electron transfer system in living organisms. It is known that ubiquinone transfers electrons from Complex I (or Complex II) to Complex III in the respiratory chain. However, recent evidence indicates that an involvement in respiration is not the sole role of ubiquinone, and various novel roles have been elucidated. A role as a lipid soluble antioxidant is now widely accepted. The relationship between lifespan and ubiquinone has attracted much interest based on the study of a Caenorhabditis elegans clk-1 mutant. The connection between disulfide bond formation and ubiquinone (or menaquinone) in Escherichia coli has been well studied. The production of hydrogen sulfide in a ubiquinone-deficient fission yeast is an interesting phenotype recently observed. These are some examples of the novel roles of ubiquinone and this review summarizes the recent findings relating to the biosynthesis, bioproduction and novel roles of ubiquinone.","authors":"Kawamukai M","authors_abbrev":"Kawamukai M","pubmed_publication_date":"2002","pubmed_entrez_date":"2005-10-20","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8068327","title":"Improved method for rapid transformation of intact Schizosaccharomyces pombe cells.","citation":"Biotechniques 1994 May;16(5):798-800","abstract":"","authors":"Kanter-Smoler G, Dahlkvist A, Sunnerhagen P","authors_abbrev":"Kanter-Smoler G et al.","pubmed_publication_date":"May 1994","pubmed_entrez_date":"1994-05-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39724842","title":"Photoprotection and antioxidant activity of eumelanin from Streptomyces lasalocidi NTB 42 and its photoprotective effects on Schizosaccharomyces pombe ARC039.","citation":"J Photochem Photobiol B 2024 Dec 22;262:113085","abstract":"This study evaluated the photoprotective and antioxidant properties of eumelanin derived from Streptomyces lasalocidi NTB 42 (eumelanin NTB 42). This study also investigated the cellular-level photoprotective effects of eumelanin using Schizosaccharomyces pombe ARC039 as a model organism and its ability to enhance the Sun Protection Factor (SPF) of commercial sunscreens. The thermal and light stability and total phenolic and flavonoid contents were analyzed. Antioxidant activity was assessed using hydroxyl radicals (OH), and superoxide anions (O 2  .- ) radical-scavenging assays. The efficacy of photoprotection was determined using various in vitro methods, yeast cell viability assays, and enhanced SPF values of commercial sunscreen products. Eumelanin NTB 42 exhibited both thermal and photostabilities. The total phenolic and flavonoid contents were reported as 88.82 ± 0.68 mg gallic acid equivalent (GAE)/g and 53.24 ± 2.66 mg quercetin equivalent (QE)/g, respectively, representing the first report on microbial eumelanin. Eumelanin NTB 42 demonstrated significant scavenging activity against OH and O 2  .- . It also displays notable photoprotective effects against UV-B radiation, offering broad-spectrum coverage and optimal protection against UV-A radiation. It effectively acted as a sunblock against UV-A and UV-B radiation. Furthermore, eumelanin NTB 42 enhanced S. pombe ARC039 cell viability after exposure to UV-B and UV-C for 30-90 min. It also augmented the SPF value of commercial products at a minimum concentration of 0.0025 %. These findings highlight the potential antioxidant and photoprotective properties of eumelanin NTB 42, suggesting its applicability as a raw material for sunscreen formulations in the cosmetic industry.","doi":"10.1016/j.jphotobiol.2024.113085","authors":"Asril M, Astuti RI, Rusmana I, Wahyudi AT","authors_abbrev":"Asril M et al.","pubmed_publication_date":"22 Dec 2024","pubmed_entrez_date":"2024-12-26","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-12-28 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20360683","title":"Splicing-dependent NMD does not require the EJC in Schizosaccharomyces pombe.","citation":"EMBO J 2010 May 05;29(9):1537-51","abstract":"Nonsense-mediated mRNA decay (NMD) is a translation-linked process that destroys mRNAs with premature translation termination codons (PTCs). In mammalian cells, NMD is also linked to pre-mRNA splicing, usually PTCs trigger strong NMD only when positioned upstream of at least one intron. The exon junction complex (EJC) is believed to mediate the link between splicing and NMD in these systems. Here, we report that in Schizosaccharomyces pombe splicing also enhances NMD, but against the EJC model prediction, an intron stimulated NMD regardless of whether it is positioned upstream or downstream of the PTC and EJC components are not required. Still the effect of splicing seems to be direct-we have found that the important NMD determinant is the proximity of an intron to the PTC, not just the occurrence of splicing. On the basis of these results, we propose a new model to explain how splicing could affect NMD.","doi":"10.1038/emboj.2010.48","authors":"Wen J, Brogna S","authors_abbrev":"Wen J et al.","pubmed_publication_date":"05 May 2010","pubmed_entrez_date":"2010-04-03","publication_year":"2010","canto_session_key":"6df01632fc970fbe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-11-03 12:51:58","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-03 12:51:29","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16C9.06c","SPAC19A8.08","SPBC13G1.14c","SPBC3B9.08c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-11-03"},{"uniquename":"PMID:15948966","title":"Convergent evolution of hydroxylation mechanisms in the fungal kingdom: molybdenum cofactor-independent hydroxylation of xanthine via alpha-ketoglutarate-dependent dioxygenases.","citation":"Mol Microbiol 2005 Jul;57(1):276-90","abstract":"The xanthine oxidases and dehydrogenases are among the most conserved enzymes in all living kingdoms. They contain the molybdopterin cofactor Moco. We show here that in the fungi, in addition to xanthine dehydrogenase, a completely different enzyme is able to catalyse the oxidation of xanthine to uric acid. In Aspergillus nidulans this enzyme is coded by the xanA gene. We have cloned the xanA gene and determined its sequence. A deletion of the gene has the same phenotype as the previously known xanA1 miss-sense mutation. Homologues of xanA exist only in the fungal kingdom. We have inactivated the cognate gene of Schizosaccharomyces pombe and this results in strongly impaired xanthine utilization as a nitrogen source. We have shown that the Neurospora crassa homologue is functionally equivalent to xanA. The enzyme coded by xanA is an alpha-ketoglutarate- and Fe(II)-dependent dioxygenase which shares a number of properties with other enzymes of this group. This work shows that only in the fungal kingdom, an alternative mechanism of xanthine oxidation, not involving Moco, has evolved using the dioxygenase scaffold.","authors":"Cultrone A, Scazzocchio C, Rochet M, Montero-Morán G, Drevet C, Fernández-Martín R","authors_abbrev":"Cultrone A et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-06-14","publication_year":"2005","canto_session_key":"525329ba6a2d8440","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-07-06 23:26:23","canto_approved_date":"2025-09-20 19:45:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-22 08:52:42","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC576.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-07-06"},{"uniquename":"PMID:2204827","title":"Eukaryotic DNA ligases.","citation":"Mutat Res 1990;236(2-3):277-87","abstract":"Recent studies on eukaryotic DNA ligases are briefly reviewed. The two distinguishable enzymes from mammalian cells, DNA ligase I and DNA ligase II, have been purified to homogeneity and characterized biochemically. Two distinct DNA ligases have also been identified in Drosophila melanogaster embryos. The genes encoding DNA ligases from Schizosaccharomyces pombe, Saccharomyces cerevisiae and vaccinia virus have been cloned and sequenced. These 3 proteins exhibit about 30% amino acid sequence identity; the 2 yeast enzymes share 53% amino acid sequence identity or conserved changes. Altered DNA ligase I activity has been found in cell lines from patients with Bloom's syndrome, although a causal link between the enzyme deficiency and the disease has not yet been proven.","authors":"Lasko DD, Tomkinson AE, Lindahl T","authors_abbrev":"Lasko DD et al.","pubmed_publication_date":"1990","pubmed_entrez_date":"1990-09-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF06624","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:20607","HGNC:10759","SPCC330.20"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:39527191","title":"Measuring Cell Dimensions in Fission Yeast Using Machine Learning.","citation":"Methods Mol Biol 2025;2862:33-46","abstract":"In fission yeast (Schizosaccharomyces pombe), cell length is a crucial indicator of cell cycle progression. Microscopy screens that examine the effect of agents or genotypes suspected of altering genomic or metabolic stability and thus cell size are crucial for studying disruptions to cell cycle dynamics. This method is based on using an automated cell segmentation algorithm to measure S. pombe cells imaged by brightfield (BF) microscopy methods. PhotoPhenosizer (PP) is a machine learning-based tool designed for automated cell measuring and dimensional analysis of morphology frequency distributions. Integration of this method into large-scale pipelines for tracking cell dimension change streamlines morphological measurements, which facilitates the examination of cellular responses to genomic and metabolic stresses. In this protocol, we use PP to observe the effect of genomic instability on cell size dynamics over a 12-day chronological lifespan assay. Our results show that relative to wild-type cells, a replication stress mutant shows larger cells during chronological aging in excess glucose media. Our results are consistent with activation of checkpoints that regulate cell morphology in response to DNA damage. This method's application highlights the relevance of its incorporation in experimental routines that require large-scale image processing and its adoption by users with routine needs in S. pombe molecular research projects.","doi":"10.1007/978-1-0716-4168-2_3","authors":"Lawson K, Skrtic S, Vo M, Escorcia W","authors_abbrev":"Lawson K et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21340088","title":"Microarray-based target identification using drug hypersensitive fission yeast expressing ORFeome.","citation":"Mol Biosyst 2011 May;7(5):1463-72","abstract":"Identification of the cellular target of small molecules is a major challenge to developing biological tools and drug leads. Here we report a novel microarray-based system for identification of the target or the target pathway of small molecules using a set of drug-hypersensitive fission yeast strains that collectively overexpress each gene in the open reading frame-ome. The major advantage of this method is that it provides genome-wide interrogation but requires a relatively small amount of the test compound. Using this system, we identified 28 genes linked to etoposide sensitivity, which included genes for the drug target topoisomerase II and other plausible factors that regulate etoposide tolerance. Thus, our approach can accelerate the process of target identification of small molecules, which has the potential to reveal highly conserved genes of clinical relevance.","doi":"10.1039/c0mb00326c","authors":"Arita Y, Nishimura S, Matsuyama A, Yashiroda Y, Usui T, Boone C, Yoshida M","authors_abbrev":"Arita Y et al.","pubmed_publication_date":"May 2011","pubmed_entrez_date":"2011-02-23","publication_year":"2011","canto_session_key":"3932fba28567af8a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-10 08:01:03","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-01 13:07:37","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":279,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_21340088_phaf.tsv"}],"genes":["SPBC1A4.03c","SPAC1006.09","SPAC3G9.14","SPCC18B5.03","SPBC776.04","SPAC31A2.10","SPAC25A8.01c","SPAC17C9.03","SPBPB7E8.02","SPBC660.15","SPBC19F8.03c","SPCC1682.08c","SPAC821.04c","SPBC21D10.05c","SPAC1805.17","SPAC1610.01","SPBC660.14","SPAC29A4.05","SPBC691.04","SPAC9E9.10c","SPAC222.09","SPAC24C9.13c","SPBC1706.01","SPAC56F8.10","SPCC4G3.14","SPCC1902.01","SPBC30B4.05","SPBC146.05c","SPBC216.07c","SPBP23A10.07","SPBC211.04c","SPCC1393.08","SPBC25B2.02c","SPBC25H2.03","SPBC17A3.05c","SPBC28E12.03","SPAC25G10.07c","SPCC1450.11c","SPCC23B6.04c","SPCC663.03","SPBC12C2.06","SPBC1773.09c","SPAC1751.01c","SPBC409.07c","SPAC15A10.10","SPAC12G12.13c","SPCC645.05c","SPCC1259.09c","SPCC74.09","SPAC1527.03","SPCC965.04c","SPAC12G12.14c","SPAC3G9.12","SPAC1F3.06c","SPAC4H3.11c","SPBC13E7.11","SPBC19G7.13","SPCC330.04c","SPBC354.05c","SPAC10F6.02c","SPAC3F10.11c","SPAC23E2.01","SPBC16G5.09","SPAC4D7.01c","SPAPB1A10.09","SPAC1B1.01","SPBC651.01c","SPAC959.03c","SPAC6F12.05c","SPAC30D11.10","SPAC29E6.10c","SPAC4A8.05c","SPBC16C6.02c","SPAC6G9.04","SPAC3H1.11","SPAC1B1.03c","SPAC12B10.12c","SPAC3H1.09c","SPAC10F6.09c","SPCC970.08","SPAC3A12.16c","SPAC1635.01","SPBC1604.20c","SPCC1259.11c","SPBC56F2.08c","SPAC19G12.14","SPBC146.06c","SPAC15A10.01","SPAC4H3.05","SPBC36B7.09","SPAPB24D3.09c","SPAC227.03c","SPCC736.14","SPBC9B6.11c","SPAC14C4.05c","SPBC543.09","SPAC10F6.17c","SPAC1783.05","SPBC2F12.13","SPAC15A10.15","SPAC17A2.09c","SPCC737.09c","SPAC30.04c","SPAC17C9.06","SPBC365.15","SPCC18B5.01c","SPAC2H10.01","SPCC550.11","SPBC8D2.20c","SPCC1020.05","SPAC1786.02","SPAC9E9.12c","SPBC543.03c","SPBC19C2.05","SPBC32F12.09","SPBC16C6.09","SPCC1919.10c","SPBC23E6.01c","SPCC825.03c","SPBC800.09","SPAC6G9.14","SPAC343.06c","SPAC3A11.14c","SPBC2G2.10c","SPAC2F3.06c","SPBC13A2.02","SPAC10F6.14c","SPAC3A12.03c","SPBC1734.12c","SPBC9B6.09c","SPBC4C3.05c","SPCC1840.03","SPAC3A11.07","SPAC20G4.03c","SPBC14C8.02","SPBC29A10.02","SPAC19B12.03","SPAC3A11.08","SPAC6F12.02","SPAC13A11.02c","SPBC15D4.02","SPAC664.11","SPAC644.14c","SPCC1840.02c","SPBC359.05","SPAC4F8.13c","SPCC737.03c","SPAC23H3.11c","SPBC29A10.10c","SPAC8E11.03c","SPAC890.02c","SPAC1565.06c","SPAC23D3.06c","SPCC736.03c","SPBC11G11.07","SPAC23D3.14c","SPAC1834.08","SPBC646.04","SPAC4G9.05","SPAC14C4.03","SPAC23D3.01","SPCC1259.13","SPAC56F8.02","SPAC8F11.06","SPBC1105.04c","SPBC28F2.12","SPAC328.01c","SPBC1703.03c","SPBC26H8.13c","SPAC2F3.04c","SPBC557.03c","SPBC947.12","SPBC1215.01","SPBC23G7.06c","SPAC824.02","SPBC16A3.17c","SPBC19G7.05c","SPBC13E7.03c","SPAC3F10.12c","SPAC57A10.12c","SPBC15D4.10c","SPCC1827.03c","SPCC1183.07","SPCC4B3.16","SPCC16A11.17"],"gene_count":185,"ltp_gene_count":2,"approved_date":"2014-10-01"},{"uniquename":"GO_REF:0000028","title":"Criteria for IDA, IEP, ISS, IGC, RCA, and IEA assignment in PAMGO_MGG","abstract":"This GO reference describes the criteria used in assigning the evidence codes of IDA (ECO:0000314), IEP (ECO:0000270), ISS (ECO:0000250), IGC (ECO_0000317), RCA (ECO:0000245) and IEA (ECO:0000501) to annotate gene products from PAMGO_MGG. Standard BLASTP from NCBI was used (http://www.ncbi.nih.gov/blast) to iteratively search reciprocal best hits and thus identify orthologs between predicted proteins of Magnaporthe grisea and GO proteins from multiple organisms with published association to GO terms. The alignments were manually reviewed for those hits with e-value equal to zero and with 80% or better coverage of both query and subject sequences, and for those hits with e<=10^-20, pid >=35 and sequence coverage >=80%. Furthermore, experimental or reviewed data from literature and other sources were incorporated into the GO annotation. IDA was assigned to an annotation if normal function of its gene was determined through transfections into a cell line and overexpression. IEP was assigned to an annotation if according to microarray experiments, its gene was upregulated in a biological process and the fold change was equal to or bigger than 10, or if according to Massively Parallel Signature Sequencing (MPSS), its gene was upregulated only in a certain biological process and the fold change was equal to or bigger than 10. ISS was assigned to an annotation if the entry at the With_column was experimentally characterized and the pairwise alignments were manually reviewed. IGC was assigned to an annotation if it based on comparison and analysis of gene location and structure, clustering of genes, and phylogenetic reconstruction of these genes. RCA was assigned to an annotation if it based on integrated computational analysis of whole genome microarray data, and matches to InterPro, pfam, and COG etc. IEA was assigned to an annotation if its function assignment based on computational work, and no manual review was done.","authors":"PAMGO_MGG curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25157670","title":"One motif to bind them: A small-XXX-small motif affects transmembrane domain 1 oligomerization, function, localization, and cross-talk between two yeast GPCRs.","citation":"Biochim Biophys Acta 2014 Dec;1838(12):3036-51","abstract":"G protein-coupled receptors (GPCRs) are the largest family of cell-surface receptors in mammals and facilitate a range of physiological responses triggered by a variety of ligands. GPCRs were thought to function as monomers, however it is now accepted that GPCR homo- and hetero-oligomers also exist and influence receptor properties. The Schizosaccharomyces pombe GPCR Mam2 is a pheromone-sensing receptor involved in mating and has previously been shown to form oligomers in vivo. The first transmembrane domain (TMD) of Mam2 contains a small-XXX-small motif, overrepresented in membrane proteins and well-known for promoting helix-helix interactions. An ortholog of Mam2 in Saccharomyces cerevisiae, Ste2, contains an analogous small-XXX-small motif which has been shown to contribute to receptor homo-oligomerization, localization and function. Here we have used experimental and computational techniques to characterize the role of the small-XXX-small motif in function and assembly of Mam2 for the first time. We find that disruption of the motif via mutagenesis leads to reduction of Mam2 TMD1 homo-oligomerization and pheromone-responsive cellular signaling of the full-length protein. It also impairs correct targeting to the plasma membrane. Mutation of the analogous motif in Ste2 yielded similar results, suggesting a conserved mechanism for assembly. Using co-expression of the two fungal receptors in conjunction with computational models, we demonstrate a functional change in G protein specificity and propose that this is brought about through hetero-dimeric interactions of Mam2 with Ste2 via the complementary small-XXX-small motifs. This highlights the potential of these motifs to affect a range of properties that can be investigated in other GPCRs.","doi":"10.1016/j.bbamem.2014.08.019","authors":"Lock A, Forfar R, Weston C, Bowsher L, Upton GJ, Reynolds CA, Ladds G, Dixon AM","authors_abbrev":"Lock A et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-08-27","publication_year":"2014","canto_session_key":"06731a3fa8de7da9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-21 12:59:42","canto_approved_date":"2020-12-13 11:38:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-21 12:59:27","canto_added_date":"2014-08-28 00:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11H11.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-21"},{"uniquename":"PMID:29249658","title":"Mechanisms Connecting the Conserved Protein Kinases Ssp1, Kin1, and Pom1 in Fission Yeast Cell Polarity and Division.","citation":"Curr Biol 2018 Jan 08;28(1):84-92.e4","abstract":"Connections between the protein kinases that function within complex cell polarity networks are poorly understood. Rod-shaped fission yeast cells grow in a highly polarized manner, and genetic screens have identified many protein kinases, including the CaMKK-like Ssp1 and the MARK/PAR-1 family kinase Kin1, that are required for polarized growth and cell shape, but their functional mechanisms and connections have been unknown [1-5]. We found that Ssp1 promotes cell polarity by phosphorylating the activation loop of Kin1. Kin1 regulates cell polarity and cytokinesis through unknown mechanisms [4-7]. We performed a large-scale phosphoproteomic screen and found that Kin1 phosphorylates itself and Pal1 to promote growth at cell tips, and these proteins are interdependent for localization to growing cell tips. Additional Kin1 substrates for cell polarity and cytokinesis (Tea4, Mod5, Cdc15, and Cyk3) were also phosphorylated by a second kinase, the DYRK family member Pom1 [8]. Kin1 and Pom1 were enriched at opposite ends of growing cells, and they phosphorylated largely non-overlapping sites on shared substrates. Combined inhibition of both Kin1and Pom1 led to synthetic defects in their shared substrates Cdc15 and Cyk3, confirming a non-redundant functional connection through shared substrates. These findings uncover a new Ssp1-Kin1 signaling pathway, and define its functional and mechanistic connection with Pom1 signaling for cell polarity and cytokinesis. These kinases are conserved in many eukaryotes including humans, suggesting that similar connections and mechanisms might operate in a broad range of cells.","doi":"10.1016/j.cub.2017.11.034","authors":"Lee ME, Rusin SF, Jenkins N, Kettenbach AN, Moseley JB","authors_abbrev":"Lee ME et al.","pubmed_publication_date":"08 Jan 2018","pubmed_entrez_date":"2017-12-19","publication_year":"2018","canto_session_key":"e58982138a6526c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"James Moseley","canto_first_approved_date":"2018-03-21 18:13:09","canto_approved_date":"2023-03-15 17:27:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-19 14:47:12","canto_added_date":"2017-12-20 01:15:15","annotation_curators":[{"name":"James Moseley","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":45,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1706.01","SPAC2F7.03c","SPBC4F6.06","SPAC24H6.05","SPCP1E11.04c","SPAC24H6.09","SPCC297.03","SPAC20G8.05c","SPBC530.04","SPAC9G1.06c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2018-03-21"},{"uniquename":"PMID:41695819","title":"Flavor enhancement of Yunnan Arabica coffee via Kombucha yeast consortium fermentation: microbial dynamics and physicochemical transformations.","citation":"Food Sci Biotechnol 2026 Feb;35(3):557-570","abstract":"The online version contains supplementary material available at 10.1007/s10068-025-02056-x.","doi":"10.1007/s10068-025-02056-x","authors":"Zhao S, Duan S, Li J, Luo H, Chen Y, Zhou S, Gong C, Fang C, Yang R","authors_abbrev":"Zhao S et al.","pubmed_publication_date":"Feb 2026","pubmed_entrez_date":"2026-02-16","publication_year":"2026","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2026-02-17 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37358275","title":"Alignment of Synchronized Time-Series Data Using the Characterizing Loss of Cell Cycle Synchrony Model for Cross-Experiment Comparisons.","citation":"J Vis Exp 2023 Jun 09;(196)","abstract":"Investigating the cell cycle often depends on synchronizing cell populations to measure various parameters in a time series as the cells traverse the cell cycle. However, even under similar conditions, replicate experiments display differences in the time required to recover from synchrony and to traverse the cell cycle, thus preventing direct comparisons at each time point. The problem of comparing dynamic measurements across experiments is exacerbated in mutant populations or in alternative growth conditions that affect the synchrony recovery time and/or the cell-cycle period. We have previously published a parametric mathematical model named Characterizing Loss of Cell Cycle Synchrony (CLOCCS) that monitors how synchronous populations of cells release from synchrony and progress through the cell cycle. The learned parameters from the model can then be used to convert experimental time points from synchronized time-series experiments into a normalized time scale (lifeline points). Rather than representing the elapsed time in minutes from the start of the experiment, the lifeline scale represents the progression from synchrony to cell-cycle entry and then through the phases of the cell cycle. Since lifeline points correspond to the phase of the average cell within the synchronized population, this normalized time scale allows for direct comparisons between experiments, including those with varying periods and recovery times. Furthermore, the model has been used to align cell-cycle experiments between different species (e.g., Saccharomyces cerevisiae and Schizosaccharomyces pombe), thus enabling direct comparison of cell-cycle measurements, which may reveal evolutionary similarities and differences.","doi":"10.3791/65466","authors":"Campione SA, Kelliher CM, Orlando DA, Tran TQ, Haase SB","authors_abbrev":"Campione SA et al.","pubmed_publication_date":"09 Jun 2023","pubmed_entrez_date":"2023-06-26","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-06-27 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9762442","title":"Fission yeast expression vectors adapted for positive identification of gene insertion and green fluorescent protein fusion.","citation":"Biotechniques 1998 Sep;25(3):438-40, 442, 444","abstract":"A pYZ series of fission yeast expression vectors, derivatives of the pREP series, was designed to allow positive identification of cloned gene insertion and fusion to the green fluorescent protein (GFP) gene for in vivo analysis of gene expression. To validate this new vector system, the human immunodeficiency virus type 1 (HIV-1) vpr gene of viral isolate pNL4-3 was expressed in the pYZ1N vector. Vpr-induced phenotypic changes were the same as those observed with vpr expressed from pREP1N. Consistent with observations in mammalian cells, a Vpr-GFP fusion protein localizes on the nuclear membrane of fission yeast cells. Additionally, we were able to detect a naturally occurring mixture of vpr genes from a plasma sample of an HIV-infected pediatric long-term surviving patient. These pYZ vectors expedite gene cloning for general purposes and are particularly suited for largescale random gene screening.","authors":"Zhao Y, Elder RT, Chen M, Cao J","authors_abbrev":"Zhao Y et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-10-08","publication_year":"1998","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007032","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17211885","title":"Chromatin dynamics of unfolding and refolding controlled by the nucleosome repeat length and the linker and core histones.","citation":"Biopolymers 2007 Mar;85(4):295-307","abstract":"Chromatin is composed of genomic DNA and histones, forming a hierarchical architecture in the nucleus. The chromatin hierarchy is common among eukaryotes despite different intrinsic properties of the genome. To investigate an effect of the differences in genome organization, chromatin unfolding processes were comparatively analyzed using Schizosaccaromyces pombe, Saccharomyces cerevisiae, and chicken erythrocyte. NaCl titration showed dynamic changes of the chromatin. 400-1000 mM NaCl facilitated beads with approximately 115 nm in diameter in S. pombe chromatin. A similar transition was also observed in S. cerevisiae chromatin. This process did not involve core histone dissociation from the chromatin, and the persistence length after the transition was approximately 26 nm for S. pombe and approximately 28 nm for S. cerevisiae, indicating a salt-induced unfolding to \"beads-on-a-string\" fibers. Reduced salt concentration recovered the original structure, suggesting that electrostatic interaction would regulate this discrete folding-unfolding process. On the other hand, the linker histone was extracted from chicken chromatin at 400 mM NaCl, and AFM observed the \"beads-on-a-string\" fibers around a nucleus. Unlike yeast chromatin, therefore, this unfolding was irreversible because of linker histone dissociation. These results indicate that the chromatin unfolding and refolding depend on the presence and absence of the linker histone, and the length of the linker DNA.","authors":"Kobori T, Iwamoto S, Takeyasu K, Ohtani T","authors_abbrev":"Kobori T et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-01-11","publication_year":"2007","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20604974","title":"Coupling histone homeostasis to centromere integrity via the ubiquitin-proteasome system.","citation":"Cell Div 2010 Jul 07;5:18","abstract":"In many eukaryotes, histone gene expression is regulated in a cell cycle-dependent manner, with a spike pattern at S phase. In fission yeast the GATA-type transcription factor Ams2 is required for transcriptional activation of all the core histone genes during S phase and Ams2 protein levels per se show concomitant periodic patterns. We have recently unveiled the molecular mechanisms underlying Ams2 fluctuation during the cell cycle. We have found that Ams2 stability varies during the cell cycle, and that the ubiquitin-proteasome pathway is responsible for Ams2 instability. Intriguingly, Ams2 proteolysis requires Hsk1-a Cdc7 homologue in fission yeast generally called Dbf4-dependent protein kinase (DDK)-and the SCF ubiquitin ligase containing the substrate receptor Pof3 F-box protein. Here, we discuss why histone synthesis has to occur only during S phase. Our results indicate that excess synthesis of core histones outside S phase results in deleterious effects on cell survival. In particular, functions of the centromere, in which the centromere-specific H3 variant CENP-A usually form centromeric nucleosomes, are greatly compromised. This defect is, at least in part, ascribable to abnormal incorporation of canonical histone H3 into these nucleosomes. Finally, we address the significance and potential implications of our work from an evolutionary point of view.","doi":"10.1186/1747-1028-5-18","authors":"Takayama Y, Toda T","authors_abbrev":"Takayama Y et al.","pubmed_publication_date":"07 Jul 2010","pubmed_entrez_date":"2010-07-08","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25977474","title":"A role for F-BAR protein Rga7p during cytokinesis in S. pombe.","citation":"J Cell Sci 2015 Jul 01;128(13):2259-68","abstract":"F-BAR proteins are known to participate in cytokinesis, but their mechanisms are not well understood. Here we investigated Rga7p, an Schizosaccharomyces pombe F-BAR protein with a RhoGAP domain. Localization of Rga7p to the cytokinetic cleavage furrow depends on its F-BAR domain, actin filaments, the formins Cdc12p and For3p, and the presence of a contractile ring. Rga7p is not required for the constriction of the contractile ring but does participate in the transport of a β-glucan synthetase (Bgs4p) from the late Golgi compartments to plasma membrane that is adjacent to the contractile ring. Cells without Rga7p moved Bgs4p normally from the poles to the Golgi complex near to the cell center, but Bgs4p then moved slowly from the late Golgi compartments to the cleavage site. The late arrival and lower than normal numbers of Bgs4p result in septal defects late in cytokinesis, and in the lysis of separating cells, similar to that in cells with mutations in the cwg1(+) gene (which encodes Bgs4p).","doi":"10.1242/jcs.162974","authors":"Arasada R, Pollard TD","authors_abbrev":"Arasada R et al.","pubmed_publication_date":"01 Jul 2015","pubmed_entrez_date":"2015-05-16","publication_year":"2015","canto_session_key":"09b5fcafa2826d4a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-23 12:40:40","canto_approved_date":"2026-01-30 13:47:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-23 12:40:28","canto_added_date":"2015-05-17 00:19:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":57,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.08c","SPAC1F5.04c","SPAC24B11.11c","SPAC926.03","SPAC4F8.13c","SPCC645.05c","SPBC19G7.05c","SPBC9B6.08","SPCC1840.02c","SPCC895.05","SPAC20G8.05c"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2018-03-23"},{"uniquename":"PMID:22589550","title":"HIRA, a conserved histone chaperone, plays an essential role in low-dose stress response via transcriptional stimulation in fission yeast.","citation":"J Biol Chem 2012 Jul 06;287(28):23440-50","abstract":"Cells that have been pre-exposed to mild stress (priming stress) acquire transient resistance to subsequent severe stress even under different combinations of stresses. This phenomenon is called cross-tolerance. Although it has been reported that cross-tolerance occurs in many organisms, the molecular basis is not clear yet. Here, we identified slm9(+) as a responsible gene for the cross-tolerance in the fission yeast Schizosaccharomyces pombe. Slm9 is a homolog of mammalian HIRA histone chaperone. HIRA forms a conserved complex and gene disruption of other HIRA complex components, Hip1, Hip3, and Hip4, also yielded a cross-tolerance-defective phenotype, indicating that the fission yeast HIRA is involved in the cross-tolerance as a complex. We also revealed that Slm9 was recruited to the stress-responsive gene loci upon stress treatment in an Atf1-dependent manner. The expression of stress-responsive genes under stress conditions was compromised in HIRA disruptants. Consistent with this, Pol II recruitment and nucleosome eviction at these gene loci were impaired in slm9Δ cells. Furthermore, we found that the priming stress enhanced the expression of stress-responsive genes in wild-type cells that were exposed to the severe stress. These observations suggest that HIRA functions in stress response through transcriptional regulation.","doi":"10.1074/jbc.M112.349944","authors":"Chujo M, Tarumoto Y, Miyatake K, Nishida E, Ishikawa F","authors_abbrev":"Chujo M et al.","pubmed_publication_date":"06 Jul 2012","pubmed_entrez_date":"2012-05-17","publication_year":"2012","canto_session_key":"018caef5dabb7ab5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"TreeFam:TF106366","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1620.06c","HGNC:9462","HGNC:9465","SPBC3D6.06c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:23956092","title":"[Cnb1 involved in cytokinesis in Schizosaccharomyces pombe].","citation":"Yi Chuan 2013 Aug;35(8):1030-9","abstract":"Serine/Threonine-specific calcineurin (CN) is highly conserved in eukaryotes, which plays an important role in transcriptional regulation. In Schizosaccharomyces pombe, CN exists as a heterodimer composed by catalytic subunit Ppb1 and regulatory subunit Cnb1. Deletion of cnb1+ reduced the growth rate of cells, and caused a chained phenotype, and had delay in cytokinesis. In cytokinesis, Cnb1 could form CN complex with Ppb1 and could colocalize and constrict with the contractile ring at division plane. Tubulin could cross the septum in cnb1Δ strain, suggesting that the septum is not fully matured. These results suggest Cnb1 might be involved in maturation of septum. The signals of septins in cnb1Δ strain were also analyzed. Septins include Spn1, Spn2, Spn3, and Spn4. Septins help to guide hydrolytic enzymes for septum degrada-tion. Eighty percent of cnb1Δ cells lacked the signals of Spn2 or Spn3 at septum, and twenty percent of cnb1Δ cells lacked the signals of Spn1 or Spn4 at septum. The reduction of the septin signals was not due to impaired transcription of septins, since the protein levels of septins in the cnb1Δ cells were not decreased. These results imply that Cnb1 might regulate the stability of septin ring in a transcription-independent manner. In general, our study showed that Cnb1 contributes to the maturation of septum and the stability of septin ring and is important in the cytokinesis.","authors":"Fan JQ, Deng XL, Feng BW, Wang JF, Yu Y, Lv H","authors_abbrev":"Fan JQ et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-08-20","publication_year":"2013","canto_session_key":"f48d48d052e6ec31","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-12-18 17:17:47","canto_approved_date":"2019-11-29 14:30:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-22 08:14:29","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.01","SPAC4F10.11","SPAC9G1.11c","SPAC821.06","SPCC830.06","SPBP4H10.04","SPCC645.05c"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2013-12-18"},{"uniquename":"PMID:7891698","title":"p13suc1 of Schizosaccharomyces pombe regulates two distinct forms of the mitotic cdc2 kinase.","citation":"Mol Cell Biol 1995 Apr;15(4):2028-36","abstract":"suc1 is an essential gene initially identified for its ability to rescue certain temperature-sensitive alleles of cdc2 in Schizosaccharomyces pombe. The role of suc1 in the regulation of the cdc2 kinase is not well understood. In our study, we have characterized the biochemical effect of loss of suc1 function on specific cdc2-cyclin complexes. We show that the cig1 cyclin is associated with cdc2 and that the cdc2-cig1 kinase is activated at mitosis, with kinetics similar to those of the cdc2-cdc13 kinase. We provide evidence that loss of suc1 function affects the kinase activity of the two distinct mitotic forms of the cdc2 kinase. We also show that a dramatic increase in the level of the cdc13 protein is associated with loss of suc1. These results suggest that mitosis cannot be properly completed in the absence of suc1, possibly because of an increase in the level of cdc2-cdc13 complex, and support the idea of a role for suc1 in the regulation of multiple forms of the cdc2 kinase.","authors":"Basi G, Draetta G","authors_abbrev":"Basi G et al.","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10851063","title":"Modulation of STAT signaling by STAT-interacting proteins.","citation":"Oncogene 2000 May 15;19(21):2638-44","abstract":"STATs (signal transducer and activator of transcription) play important roles in numerous cellular processes including immune responses, cell growth and differentiation, cell survival and apoptosis, and oncogenesis. In contrast to many other cellular signaling cascades, the STAT pathway is direct: STATs bind to receptors at the cell surface and translocate into the nucleus where they function as transcription factors to trigger gene activation. However, STATs do not act alone. A number of proteins are found to be associated with STATs. These STAT-interacting proteins function to modulate STAT signaling at various steps and mediate the crosstalk of STATs with other cellular signaling pathways. This article reviews the roles of STAT-interacting proteins in the regulation of STAT signaling. Oncogene (2000).","authors":"Shuai K","authors_abbrev":"Shuai K","pubmed_publication_date":"15 May 2000","pubmed_entrez_date":"2000-06-13","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006480","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11715048","title":"Men and sin: what's the difference?","citation":"Nat Rev Mol Cell Biol 2001 Nov;2(11):815-26","abstract":"A conserved signalling cascade--termed the mitotic-exit network in budding yeast and the septation-initiation network in fission yeast--controls key events during exit from mitosis and cytokinesis. Although the components of these signalling networks are highly conserved between the two yeasts, the outputs seem quite different. How, then, do these two pathways function, and how are they regulated?","authors":"Bardin AJ, Amon A","authors_abbrev":"Bardin AJ et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2001-11-21","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1367727","title":"Expression cloning systems.","citation":"Curr Opin Biotechnol 1991 Oct;2(5):735-41","abstract":"This review will cover the use of expression cloning in Xenopus oocytes, fission yeast, and mammalian cells. Of the systems covered herein, transient expression cloning systems in Xenopus oocytes and mammalian cells have proven to be the most effective and versatile, as demonstrated by the large number of cDNA clones isolated by these two methods in the past year. Of particular interest, are recent advances in the screening methodologies used in conjunction with transient expression in mammalian cells which have permitted the application of this system in the isolation of cDNAs encoding intracellular proteins.","authors":"Aruffo A","authors_abbrev":"Aruffo A","pubmed_publication_date":"Oct 1991","pubmed_entrez_date":"1991-10-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPU88525","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18845843","title":"A G2-phase microtubule-damage response in fission yeast.","citation":"Genetics 2008 Dec;180(4):2073-80","abstract":"Microtubules assume a variety of structures throughout the different stages of the cell cycle. Ensuring the correct assembly of such structures is essential to guarantee cell division. During mitosis, it is well established that the spindle assembly checkpoint monitors the correct attachment of sister chromatids to the mitotic spindle. However, the role that microtubule cytoskeleton integrity plays for cell-cycle progression during interphase is uncertain. Here we describe the existence of a mechanism, independent of the mitotic checkpoint, that delays entry into mitosis in response to G(2)-phase microtubule damage. Disassembly of the G(2)-phase microtubule array leads to the stabilization of the universal mitotic inhibitor Wee1, thus actively delaying entry into mitosis via inhibitory Cdc2 Tyr15 phosphorylation.","doi":"10.1534/genetics.108.094797","authors":"Balestra FR, Jimenez J","authors_abbrev":"Balestra FR et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-10-11","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24256277","title":"Systematic genetic analysis of transcription factors to map the fission yeast transcription-regulatory network.","citation":"Biochem Soc Trans 2013 Dec;41(6):1696-700","abstract":"Mapping transcriptional-regulatory networks requires the identification of target genes, binding specificities and signalling pathways of transcription factors. However, the characterization of each transcription factor sufficiently for deciphering such networks remains laborious. The recent availability of overexpression and deletion strains for almost all of the transcription factor genes in the fission yeast Schizosaccharomyces pombe provides a valuable resource to better investigate transcription factors using systematic genetics. In the present paper, I review and discuss the utility of these strain collections combined with transcriptome profiling and genome-wide chromatin immunoprecipitation to identify the target genes of transcription factors.","doi":"10.1042/BST20130224","authors":"Chua G","authors_abbrev":"Chua G","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27172183","title":"Interconnections Between RNA-Processing Pathways Revealed by a Sequencing-Based Genetic Screen for Pre-mRNA Splicing Mutants in Fission Yeast.","citation":"G3 (Bethesda) 2016 Jun 01;6(6):1513-23","abstract":"Pre-mRNA splicing is an essential component of eukaryotic gene expression and is highly conserved from unicellular yeasts to humans. Here, we present the development and implementation of a sequencing-based reverse genetic screen designed to identify nonessential genes that impact pre-mRNA splicing in the fission yeast Schizosaccharomyces pombe, an organism that shares many of the complex features of splicing in higher eukaryotes. Using a custom-designed barcoding scheme, we simultaneously queried ∼3000 mutant strains for their impact on the splicing efficiency of two endogenous pre-mRNAs. A total of 61 nonessential genes were identified whose deletions resulted in defects in pre-mRNA splicing; enriched among these were factors encoding known or predicted components of the spliceosome. Included among the candidates identified here are genes with well-characterized roles in other RNA-processing pathways, including heterochromatic silencing and 3' end processing. Splicing-sensitive microarrays confirm broad splicing defects for many of these factors, revealing novel functional connections between these pathways.","doi":"10.1534/g3.116.027508","authors":"Larson A, Fair BJ, Pleiss JA","authors_abbrev":"Larson A et al.","pubmed_publication_date":"01 Jun 2016","pubmed_entrez_date":"2016-05-13","publication_year":"2016","canto_session_key":"82de682f1e2c24b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-06-08 15:58:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-06-08 15:53:22","canto_added_date":"2016-05-15 00:15:13","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":70,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_27172183_phaf.tsv"}],"genes":["SPBC800.04c","SPAC222.07c","SPAC1006.03c","SPCC285.14","SPAC17G8.05","SPBC1604.08c","SPAC4D7.12c","SPBC29A3.08","SPBP18G5.03","SPAPYUG7.04c","SPAC4F10.18","SPAC3G9.04","SPBC19C7.02","SPAC18G6.13","SPBC28F2.08c","SPBC13G1.08c","SPAC959.08","SPBC1734.05c","SPBC11B10.10c","SPBC1D7.03","SPAC4G9.02","SPAC1B3.05","SPAC110.02","SPCC825.05c","SPAC3H5.04","SPBC30D10.04","SPAC644.14c","SPCC4G3.11","SPCP1E11.07c","SPBC19C2.14","SPBC16C6.09","SPBP8B7.11","SPBC1348.03","SPBC2F12.12c","SPBC14C8.05c","SPBC29A3.05","SPAC890.06","SPAC20H4.06c","SPAC18G6.10","SPCC162.01c","SPCC550.03c","SPBC1709.11c","SPCC18.13","SPBC713.05","SPCC4B3.08","SPCC584.12","SPBC342.06c","SPAC17G8.07","SPAC22E12.03c","SPAC140.04","SPCC736.07c","SPAC4F10.07c","SPCC74.02c","SPBC557.04","SPAC22H10.11c","SPAC27D7.12c","SPCC18B5.01c","SPAC6B12.05c","SPBC2D10.13","SPAPYUG7.06","SPBP35G2.13c","SPBC17G9.08c","SPAC30D11.09"],"gene_count":63,"ltp_gene_count":0,"approved_date":"2016-06-08"},{"uniquename":"EMBL:SPD181","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12110682","title":"Elf1p, a member of the ABC class of ATPases, functions as a mRNA export factor in Schizosacchromyces pombe.","citation":"J Biol Chem 2002 Sep 13;277(37):33580-9","abstract":"Rae1p and Mex67p/Tap are conserved mRNA export factors. We have used synthetic lethal genetic screens in Schizosaccharomyces pombe to identify mutations in genes that are functionally linked to rae1 and mex67 in mRNA export. From these screens, we have isolated mutations in a putative S. pombe homologue of the Candida albicans elf1 gene. The elf1 of S. pombe is not an essential gene. When elf1 mutations are combined with rae1-167 mutation, growth and mRNA export is inhibited in the double mutants. This inhibition can be suppressed by the multicopy expression of mex67 suggesting that Mex67p can substitute for the loss of Elf1p function. Elf1p is a non-membrane member of the ATP-binding cassette (ABC) class of ATPase and the GFP-Elf1p fusion localizes to the cytoplasm. Elf1p, expressed and purified from Escherichia coli, binds and hydrolyzes ATP. A mutant Elf1p that carries a glycine to aspartic acid (G731D) mutation within the Walker A domain of the second ATP site retains the ATP binding but loses its ATPase activity in vitro. This mutant protein no longer functions in mRNA export. Taken together, our results show that Elf1p functions as a mRNA export factor along with Rae1p and Mex67p in S. pombe.","authors":"Kozak L, Gopal G, Yoon JH, Sauna ZE, Ambudkar SV, Thakurta AG, Dhar R","authors_abbrev":"Kozak L et al.","pubmed_publication_date":"13 Sep 2002","pubmed_entrez_date":"2002-07-12","publication_year":"2002","canto_session_key":"3bbd2be8f7178620","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-12-15 16:30:27","canto_approved_date":"2021-06-16 13:01:56","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-12-15 16:30:20","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.05c","SPBC1921.03c","SPAP27G11.10c","SPAC3C7.08c","SPCC1739.14"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-12-15"},{"uniquename":"PMID:19755492","title":"Schizosaccharomyces pombe Cds1Chk2 regulates homologous recombination at stalled replication forks through the phosphorylation of recombination protein Rad60.","citation":"J Cell Sci 2009 Oct 15;122(Pt 20):3638-43","abstract":"The Schizosaccharomyces pombe rad60 gene is essential for cell growth and is involved in repairing DNA double-strand breaks. Rad60 physically interacts with, and is functionally related to, the structural maintenance of chromosomes 5 and 6 protein complex (Smc5/6). Rad60 is phosphorylated in response to hydroxyurea (HU)-induced DNA replication arrest in a Cds1(Chk2)-dependent manner. Rad60 localizes in nucleus in unchallenged cells, but becomes diffused throughout the cell in response to HU. To understand the role of Rad60 phosphorylation, we mutated the putative phosphorylation target motifs of Cds1(Chk2) and have identified two Cds1(Chk2) target residues responsible for Rad60 dispersal in response to HU. We show that the phosphorylation-defective rad60 mutation partially suppresses HU sensitivity and the elevated recombination frequency of smc6-X. Our data suggest that Rad60 phosphorylation is required to regulate homologous recombination at stalled replication forks, probably by regulating Smc5/6.","doi":"10.1242/jcs.046508","authors":"Miyabe I, Morishita T, Shinagawa H, Carr AM","authors_abbrev":"Miyabe I et al.","pubmed_publication_date":"15 Oct 2009","pubmed_entrez_date":"2009-09-17","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC5E4.06","SPCC18B5.11c","SPBC1921.02"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:21561865","title":"The phosphorylation network for efficient activation of the DNA replication checkpoint in fission yeast.","citation":"J Biol Chem 2011 Jul 01;286(26):22864-74","abstract":"Protein phosphorylation is the hallmark of checkpoint activation. Hundreds of targets of checkpoint kinases have been identified recently by genome-wide investigations. However, the complete picture of a phosphorylation network required for activation of a checkpoint pathway has not been available. The DNA replication checkpoint in Schizosaccharomyces pombe contains two major protein kinases, the sensor kinase Rad3 and the effector kinase Cds1, with the latter mediating most of the checkpoint functions. We show here that when DNA replication is arrested, efficient activation of Cds1 requires five phosphorylations that cooperate in a parallel or a sequential manner. Phosphorylation of a threonine residue (Thr(11)) in Cds1 by Rad3 occurs at a basal level in the absence of three other parallel Rad3-dependent phosphorylations on the mediator Mrc1 and Rad9 in the checkpoint clamp complex. However, the three parallel Rad3-dependent phosphorylations are all required for efficient phosphorylation of Thr(11) in Cds1 by Rad3. Phosphorylation of Thr(11) has been shown previously to promote autophosphorylation of Thr(328) in the kinase domain of Cds1, which directly activates the enzyme, leading to full activation of the checkpoint pathway. Interestingly, phosphorylation of Mrc1 by Rad3 does not require the phosphorylation of Rad9, suggesting that activation of the sensor kinase Rad3 in the replication checkpoint of fission yeast may involve a different mechanism.","doi":"10.1074/jbc.M111.236687","authors":"Yue M, Singh A, Wang Z, Xu YJ","authors_abbrev":"Yue M et al.","pubmed_publication_date":"01 Jul 2011","pubmed_entrez_date":"2011-05-13","publication_year":"2011","canto_session_key":"a5f8ece090d3d081","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-06-08 10:24:21","canto_approved_date":"2025-09-04 09:19:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-15 14:08:49","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":190,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_21561865_phaf.tsv"}],"genes":["SPAC664.07c","SPCC23B6.03c","SPAC20G4.04c","SPBC342.05","SPAC9E9.08","SPBC216.05","SPCC18B5.11c","SPAC14C4.13","SPAC1952.07","SPCC1259.13","SPAC694.06c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2018-06-08"},{"uniquename":"PMID:18430957","title":"The Rad52 homologs Rad22 and Rti1 of Schizosaccharomyces pombe are not essential for meiotic interhomolog recombination, but are required for meiotic intrachromosomal recombination and mating-type-related DNA repair.","citation":"Genetics 2008 Apr;178(4):2399-412","abstract":"Proteins of the RAD52 epistasis group play an essential role in repair of some types of DNA damage and genetic recombination. In Schizosaccharomyces pombe, Rad22 (a Rad52 ortholog) has been shown to be as necessary for repair and recombination events during vegetative growth as its Saccharomyces cerevisiae counterpart. This finding contrasts with previous reports where, due to suppressor mutations in the fbh1 gene, rad22 mutants did not display a severe defect. We have analyzed the roles of Rad22 and Rti1, another Rad52 homolog, during meiotic recombination and meiosis in general. Both proteins play an important role in spore viability. During meiotic prophase I, they partially colocalize and partially localize to Rad51 foci and linear elements. Genetic analysis showed that meiotic interchromosomal crossover and conversion events were unexpectedly not much affected by deletion of either or both genes. A strong decrease of intrachromosomal recombination assayed by a gene duplication construct was observed. Therefore, we propose that the most important function of Rad22 and Rti1 in S. pombe meiosis is repair of double-strand breaks with involvement of the sister chromatids. In addition, a novel mating-type-related repair function of Rad22 specific to meiosis and spore germination is described.","doi":"10.1534/genetics.107.085696","authors":"Octobre G, Lorenz A, Loidl J, Kohli J","authors_abbrev":"Octobre G et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-04-24","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28461681","title":"Analysis of RNA Metabolism in Fission Yeast.","citation":"Cold Spring Harb Protoc 2017 May 01;2017(5)","abstract":"Here we focus on the biogenesis and function of messenger RNA (mRNA) in fission yeast cells. Following a general introduction that also briefly touches on other classes of RNA, we provide an overview of methods used to analyze mRNAs throughout their life cycles.","doi":"10.1101/pdb.top079798","authors":"Wise JA, Nielsen O","authors_abbrev":"Wise JA et al.","pubmed_publication_date":"01 May 2017","pubmed_entrez_date":"2017-05-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-05-05 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008306","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40901873","title":"Nonlinear memory in cell-division dynamics across species.","citation":"Proc Natl Acad Sci U S A 2025 Sep 09;122(36):e2417416122","abstract":"Regulation of cell growth and division is essential to achieve cell-size homeostasis. Recent advances in imaging technologies, such as \"mother machines\" for bacteria or yeast, have allowed long-term tracking of cell-size dynamics across many generations, and thus have brought major insights into the mechanisms underlying cell-size control. However, understanding the governing rules of cell growth and division within a quantitative dynamical-systems framework remains a major challenge. Here, we implement and apply a framework that makes it possible to infer stochastic-differential-equation models with Poisson noise directly from experimentally measured time series for cellular growth and division. To account for potential nonlinear memory effects, we parameterize the Poisson intensity of stochastic cell-division events in terms of both the cell's current size and its ancestral history. By applying the algorithm to experimentally measured cell-size trajectories, we are able to quantitatively evaluate the linear one-step memory hypothesis underlying the popular \"sizer,\" \"adder,\" and \"timer\" models of cell homeostasis. For  Escherichia coli  and  Bacillus subtilis  bacteria,  Schizosaccharomyces pombe  yeast and  Dictyostelium discoideum  amoebae, we find that in many cases, the inferred stochastic models have a substantial nonlinear memory component. This suggests a need to reevaluate and generalize some of the currently prevailing linear-memory paradigms of cell homeostasis. More broadly, the underlying inference framework is directly applicable to identify quantitative models for stochastic jump processes in a wide range of scientific disciplines.","doi":"10.1073/pnas.2417416122","authors":"Zhang S, Fei C, Dunkel J","authors_abbrev":"Zhang S et al.","pubmed_publication_date":"09 Sep 2025","pubmed_entrez_date":"2025-09-03","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-09-03 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29039458","title":"DNA polymerase 5 acetylation by Eso1 is essential for Schizosaccharomyces pombe viability.","citation":"Int J Mol Med 2017 Dec;40(6):1907-1913","abstract":"Eco1/Eso1 protein plays an important role in chromosome segregation, DNA repair and gene regulation. Eco1 mutation induces Roberts syndrome clinically and rDNA transcription disorders in vivo. In this study, we examined the role of Eso1 protein binding to polymerase 5 (Pol5) and the acetylation of Pol5 protein in the regulation of Schizosaccharomyces pombe (S. pombe) viability. Immunoprecipitation and mass spectrometry assays identified Eso1 protein binding to Cdc2, Pol5 and Cdc21, as well as other proteins. Pol5 protein specifically bound to Eso1 protein, but not to the Rad30 part or Rad30 part plus the additional zinc finger domain of Eco1 protein. Mass spectrometry data further identified several acetylation or trimethylation modification sites in the lysine residues of the Pol5 protein. However, the mutation of the Pol5 K47 site to arginine was lethal to S. pombe. Eso1 protein was able to acetylate Pol5 protein and mediate S. pombe viability. On the whole, our data indicate that the Eso1 interaction with Pol5 which acetylates Pol5 protein is essential for S. pombe viability.","doi":"10.3892/ijmm.2017.3192","authors":"Chen Z, Cao H, Lu Y, Ren Q, Sun L","authors_abbrev":"Chen Z et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-10-18","publication_year":"2017","canto_session_key":"a3f9dac017960a74","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-10-20 00:15:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.11","SPBC14C8.14c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:33625871","title":"Direct and indirect regulation of Pom1 cell size pathway by the protein phosphatase 2C Ptc1.","citation":"Mol Biol Cell 2021 Apr 15;32(8):703-711","abstract":"The fission yeast cells  Schizosaccharomyces pombe  divide at constant cell size regulated by environmental stimuli. An important pathway of cell size control involves the membrane-associated DYRK-family kinase Pom1, which forms decreasing concentration gradients from cell poles and inhibits mitotic inducers at midcell. Here, we identify the phosphatase 2C Ptc1 as negative regulator of Pom1. Ptc1 localizes to cell poles in a manner dependent on polarity and cell-wall integrity factors. We show that Ptc1 directly binds Pom1 and can dephosphorylate it in vitro but modulates Pom1 localization indirectly upon growth in low-glucose conditions by influencing microtubule stability. Thus, Ptc1 phosphatase plays both direct and indirect roles in the Pom1 cell size control pathway.","doi":"10.1091/mbc.E20-08-0508","authors":"Gerganova V, Bhatia P, Vincenzetti V, Martin SG","authors_abbrev":"Gerganova V et al.","pubmed_publication_date":"15 Apr 2021","pubmed_entrez_date":"2021-02-24","publication_year":"2021","canto_session_key":"6da98f48297f6a17","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-02-26 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7260241","title":"Oscillations of redox states in synchronously dividing cultures of Acanthamoeba castellanii and Schizosaccharomyces pombe.","citation":"Biophys J 1980 Jan;29(1):1-11","abstract":"The redox state of the mitochondria of Acanthamoeba castellanii and Schizosaccharomyces pombe was assessed with a flying-spot fluorometer (Chance et al. 1978. Am. J. Physiol. 235:H 809) that provides excitation appropriate for oxidized flavoprotein or reduced pyridine nucleotide. Fluorescence signals could be resolved from the thin films of cultures that were only one cell deep. In both organisms anoxia was associated with an increased pyridine nucleotide and decreased flavoprotein fluorescence. The addition of mitochondrial uncoupling agents increased the flavoprotein fluorescence and the fluorometer was able to resolve uncoupler-sensitive and uncoupler-insensitive fractions of S. pombe cultures. In both synchronous and asynchronous cultures of A. castellanii and S. pombe the mitochondrial redox state oscillates with a period of 4.5 +/- 1.0 min. Oscillations with much longer period, of the order of an hour, are observed in synchronous cultures and these oscillations correlate with similar oscillations in respiratory rate, uncoupler sensitivity, and adenine nucleotide pool sizes. The results are consistent with the hypothesis that synchronous cultures of A. castellanii and S. pombe oscillate between the ADP-limited (state 4) and ADP-sufficient (state 3) respiratory states, i.e., exhibit in vivo respiratory control.","authors":"Bashford CL, Chance B, Lloyd D, Poole RK","authors_abbrev":"Bashford CL et al.","pubmed_publication_date":"Jan 1980","pubmed_entrez_date":"1980-01-01","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33526714","title":"Activation of meiotic recombination by nuclear import of the DNA break hotspot-determining complex in fission yeast.","citation":"J Cell Sci 2021 Feb 22;134(4)","abstract":"Meiotic recombination forms crossovers important for proper chromosome segregation and offspring viability. This complex process involves many proteins acting at each of the multiple steps of recombination. Recombination initiates by formation of DNA double-strand breaks (DSBs), which in the several species examined occur with high frequency at special sites (DSB hotspots). In  Schizosaccharomyces pombe , DSB hotspots are bound with high specificity and strongly activated by linear element (LinE) proteins Rec25, Rec27 and Mug20, which form colocalized nuclear foci with Rec10, essential for all DSB formation and recombination. Here, we test the hypothesis that the nuclear localization signal (NLS) of Rec10 is crucial for coordinated nuclear entry after forming a complex with other LinE proteins. In NLS mutants, all LinE proteins were abundant in the cytoplasm, not the nucleus; DSB formation and recombination were much reduced but not eliminated. Nuclear entry of limited amounts of Rec10, apparently small enough for passive nuclear entry, can account for residual recombination. LinE proteins are related to synaptonemal complex proteins of other species, suggesting that they also share an NLS, not yet identified, and undergo protein complex formation before nuclear entry.This article has an associated First Person interview with Mélody Wintrebert, joint first author of the paper.","doi":"10.1242/jcs.253518","authors":"Wintrebert M, Nguyen MC, Smith GR","authors_abbrev":"Wintrebert M et al.","pubmed_publication_date":"22 Feb 2021","pubmed_entrez_date":"2021-02-02","publication_year":"2021","canto_session_key":"bc37079d00ce0453","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Randy Hyppa","canto_first_approved_date":"2021-12-10 20:19:24","canto_approved_date":"2022-05-31 06:38:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-12-09 00:18:28","canto_added_date":"2021-02-04 01:15:06","annotation_curators":[{"name":"Randy Hyppa","community_curator":true,"annotation_count":30,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.04c","SPBC36B7.06c","SPAC17A5.18c","SPBC577.05c"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2021-12-10"},{"uniquename":"PMID:17005570","title":"The Smc5-Smc6 DNA repair complex. bridging of the Smc5-Smc6 heads by the KLEISIN, Nse4, and non-Kleisin subunits.","citation":"J Biol Chem 2006 Dec 01;281(48):36952-9","abstract":"Structural maintenance of chromosomes (SMC) proteins play fundamental roles in many aspects of chromosome organization and dynamics. The SMC complexes form unique structures with long coiled-coil arms folded at a hinge domain, so that the globular N- and C-terminal domains are brought together to form a \"head.\" Within the Smc5-Smc6 complex, we previously identified two subcomplexes containing Smc6-Smc5-Nse2 and Nse1-Nse3-Nse4. A third subcomplex containing Nse5 and -6 has also been identified recently. We present evidence that Nse4 is the kleisin component of the complex, which bridges the heads of Smc5 and -6. The C-terminal part of Nse4 interacts with the head domain of Smc5, and structural predictions for Nse4 proteins suggest similar motifs that are shared within the kleisin family. Specific mutations within a predicted winged helix motif of Nse4 destroy the interaction with Smc5. We propose that Nse4 and its orthologs form the delta-kleisin subfamily. We further show that Nse3, as well as Nse5 and Nse6, also bridge the heads of Smc5 and -6. The Nse1-Nse3-Nse4 and Nse5-Nse6 subcomplexes bind to the Smc5-Smc6 heads domain at different sites.","authors":"Palecek J, Vidot S, Feng M, Doherty AJ, Lehmann AR","authors_abbrev":"Palecek J et al.","pubmed_publication_date":"01 Dec 2006","pubmed_entrez_date":"2006-09-29","publication_year":"2006","canto_session_key":"077db45134eec113","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Edita Balkoova","canto_first_approved_date":"2016-08-22 11:26:21","canto_approved_date":"2021-10-12 13:38:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-07 10:57:33","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Edita Balkoova","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.04","SPAC11E3.08c","SPBC20F10.04c","SPBC651.10","SPAC14C4.02c","SPCC5E4.06"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-08-22"},{"uniquename":"EMBL:AU010049","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16453669","title":"Transcription of the cdc2 cell cycle control gene of the fission yeast Schizosaccharomyces pombe.","citation":"EMBO J 1986 Feb;5(2):369-73","abstract":"The cdc2 gene plays a central role in the control of the mitotic cell cycle of the fission yeast Schizosaccharomyces pombe. It is required in G1 at start for commitment to the mitotic cycle and then again in G2 where it determines the timing of mitosis. We have identified the cdc2 gene transcript as a 1.6-kb polyadenylated mRNA. This transcript is generated after four introns have been spliced out; there is no evidence for differential splicing. The level of cdc2 transcript does not change during a shift between cell proliferation and stationary phase or during the mitotic cell cycle. Overproduction of the cdc2 transcript does not alter the normal cell cycle. We conclude that the cell cycle is not controlled by changes in either the cdc2 transcript level or in its processing. A gene adjacent to cdc2 called cdc2L has also been identified. This encodes three transcripts of 1.0-1.3 kb in length, at least two of which are cell cycle regulated. Their levels peak during S-phase and are increased in certain cell cycle mutants. This gene may code for a product which is required for the mitotic cell cycle.","authors":"Durkacz B, Carr A, Nurse P","authors_abbrev":"Durkacz B et al.","pubmed_publication_date":"Feb 1986","pubmed_entrez_date":"1986-02-01","publication_year":"1986","canto_session_key":"a579eb876752f3ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-05-02 14:15:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-29 14:11:10","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC11B10.10c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2015-04-29"},{"uniquename":"PMID:16478992","title":"Requirement of fission yeast Cid14 in polyadenylation of rRNAs.","citation":"Mol Cell Biol 2006 Mar;26(5):1710-21","abstract":"Polyadenylation in eukaryotes is conventionally associated with increased nuclear export, translation, and stability of mRNAs. In contrast, recent studies suggest that the Trf4 and Trf5 proteins, members of a widespread family of noncanonical poly(A) polymerases, share an essential function in Saccharomyces cerevisiae that involves polyadenylation of nuclear RNAs as part of a pathway of exosome-mediated RNA turnover. Substrates for this pathway include aberrantly modified tRNAs and precursors of snoRNAs and rRNAs. Here we show that Cid14 is a Trf4/5 functional homolog in the distantly related fission yeast Schizosaccharomyces pombe. Unlike trf4 trf5 double mutants, cells lacking Cid14 are viable, though they suffer an increased frequency of chromosome missegregation. The Cid14 protein is constitutively nucleolar and is required for normal nucleolar structure. A minor population of polyadenylated rRNAs was identified. These RNAs accumulated in an exosome mutant, and their presence was largely dependent on Cid14, in line with a role for Cid14 in rRNA degradation. Surprisingly, both fully processed 25S rRNA and rRNA processing intermediates appear to be channeled into this pathway. Our data suggest that additional substrates may include the mRNAs of genes involved in meiotic regulation. Polyadenylation-assisted nuclear RNA turnover is therefore likely to be a common eukaryotic mechanism affecting diverse biological processes.","authors":"Win TZ, Draper S, Read RL, Pearce J, Norbury CJ, Wang SW","authors_abbrev":"Win TZ et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-02-16","publication_year":"2006","canto_session_key":"db750e6d73814392","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-07-31 16:06:22","canto_approved_date":"2023-03-14 19:29:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-29 17:20:41","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPBC11C11.03","SPBC32C12.02","SPCC663.12","SPBC26H8.07c","SPAC12G12.13c","SPCC1322.12c","SPAC664.01c","SPAC27D7.03c","SPBC1703.14c","SPBC26H8.10","SPBC20F10.06"],"gene_count":12,"ltp_gene_count":7,"approved_date":"2015-07-31"},{"uniquename":"PMID:34686329","title":"The Hsp90 cochaperone TTT promotes cotranslational maturation of PIKKs prior to complex assembly.","citation":"Cell Rep 2021 Oct 19;37(3):109867","abstract":"Phosphatidylinositol 3-kinase-related kinases (PIKKs) are a family of kinases that control fundamental processes, including cell growth, DNA damage repair, and gene expression. Although their regulation and activities are well characterized, little is known about how PIKKs fold and assemble into active complexes. Previous work has identified a heat shock protein 90 (Hsp90) cochaperone, the TTT complex, that specifically stabilizes PIKKs. Here, we describe a mechanism by which TTT promotes their de novo maturation in fission yeast. We show that TTT recognizes newly synthesized PIKKs during translation. Although PIKKs form multimeric complexes, we find that they do not engage in cotranslational assembly with their partners. Rather, our findings suggest a model by which TTT protects nascent PIKK polypeptides from misfolding and degradation because PIKKs acquire their native state after translation is terminated. Thus, PIKK maturation and assembly are temporally segregated, suggesting that the biogenesis of large complexes requires both dedicated chaperones and cotranslational interactions between subunits.","doi":"10.1016/j.celrep.2021.109867","authors":"Toullec D, Elías-Villalobos A, Faux C, Noly A, Lledo G, Séveno M, Helmlinger D","authors_abbrev":"Toullec D et al.","pubmed_publication_date":"19 Oct 2021","pubmed_entrez_date":"2021-10-23","publication_year":"2021","canto_session_key":"0f72d4033c5d842f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dom Helmlinger","canto_first_approved_date":"2023-09-06 08:05:55","canto_approved_date":"2026-02-12 10:57:41","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-09-05 13:14:44","canto_added_date":"2021-10-25 00:15:04","annotation_curators":[{"name":"Dom Helmlinger","community_curator":true,"annotation_count":144,"orcid":"0000-0003-1501-0423","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPBC216.05","SPAPB1E7.12","SPAC458.03","SPAC13G6.07c","SPCC24B10.07","SPAC1006.02","SPBC216.07c","SPAC926.04c","SPBC1604.17c","SPCC622.13c","SPBC83.08","SPAC1F5.11c","SPBC30D10.10c","SPCC23B6.03c","SPAC27D7.03c","SPBP16F5.03c","SPAPB8E5.09"],"gene_count":18,"ltp_gene_count":12,"approved_date":"2023-09-06"},{"uniquename":"PMID:24434141","title":"The ribosomal protein rpl26 promoter is required for its 3' sense terminus ncRNA transcription in Schizosaccharomyces pombe, implicating a new transcriptional mechanism for ncRNAs.","citation":"Biochem Biophys Res Commun 2014 Jan 31;444(1):86-91","abstract":"Transcriptome studies have revealed that many non-coding RNAs (ncRNAs) are located near the 3' sense terminus of protein-coding genes. However, the transcription and function of these RNAs remain elusive. Here, we identify a 3' sense termini-associated sRNA (TASR) downstream of rpl26 in Schizosaccharomyces pombe (S. pombe). Structure and function assays indicate that the TASR is an H/ACA box snoRNA required for 18S rRNA pseudouridylation at U121 and U305 sites and is therefore a cognate of snR49 from the budding yeast. Transcriptional studies show that pre-snR49 overlaps most of the coding sequence (CDS) of rpl26. Using scanning deletion analysis within promoter region, we show that the rpl26 promoter is required for the 3' TASR transcription. Interestingly, chromosomal synteny of rpl26-snR49 is found in the Schizosaccharomyces groups. Taken together, we have revealed a new transcriptional mechanism for 3' sense TASRs, which are transcribed by the same promoter as their upstream protein genes. These results further suggest that the origin and function of 3' sense ncRNAs are associated with upstream genes in higher eukaryotes.","doi":"10.1016/j.bbrc.2014.01.018","authors":"Leng XM, Diao LT, Li B, Bi YZ, Chen CJ, Zhou H, Qu LH","authors_abbrev":"Leng XM et al.","pubmed_publication_date":"31 Jan 2014","pubmed_entrez_date":"2014-01-18","publication_year":"2014","canto_session_key":"71f58e295904b714","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084854","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.42"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30065087","title":"Do Fungi Undergo Apoptosis-Like Programmed Cell Death?","citation":"mBio 2018 Jul 31;9(4)","abstract":"This question of whether fungi undergo apoptosis-like programmed cell death can be separated into two questions. One question is about applying the term \"apoptosis\" to fungi, and the other is a more challenging question of whether fungi have evolved mechanisms that inflict self-injury. The answers to both questions depend on the definitions applied to \"apoptosis\" and \"programmed cell death.\" Considering how these and other cell death terms originated and are currently defined for animals, some confusion arises when the terms are applied to fungi. While it is difficult to defend the concept of fungal apoptosis, the more interesting issue is whether fungi will eventually be found to encode programmed or extemporaneous self-destructive processes, as suggested by intriguing new findings.","doi":"10.1128/mBio.00948-18","authors":"Hardwick JM","authors_abbrev":"Hardwick JM","pubmed_publication_date":"31 Jul 2018","pubmed_entrez_date":"2018-08-02","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-10-05 15:16:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20301561","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21C3.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2665366","title":"Estimation of phylogenetic distances among ascomycetous yeasts from partial sequencing of ribosomal RNA.","citation":"Yeast 1989 Apr;5 Spec No:S351-4","abstract":"Extent of taxonomic resolution obtained from nuclear DNA complementarity and ribosomal RNA sequencing is discussed. The phylogenetic relationships of Schizosaccharomyces pombe, Pichia stipitis, Pachysolen tannophilus, and Saccharomyces cerevisiae are compared from partial sequences of 18S and 26S ribosomal RNA.","authors":"Kurtzman CP","authors_abbrev":"Kurtzman CP","pubmed_publication_date":"Apr 1989","pubmed_entrez_date":"1989-04-01","publication_year":"1989","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18025105","title":"Global role for polyadenylation-assisted nuclear RNA degradation in posttranscriptional gene silencing.","citation":"Mol Cell Biol 2008 Jan;28(2):656-65","abstract":"Fission yeast Cid14, a component of the TRAMP (Cid14/Trf4-Air1-Mtr4 polyadenylation) complex, polyadenylates nuclear RNA and stimulates degradation by the exosome for RNA quality control. Here, we analyze patterns of global gene expression in cells lacking the Cid14 or the Dis3/Rpr44 subunit of the nuclear exosome. We found that transcripts from many genes induced during meiosis, including key regulators, accumulated in the absence of Cid14 or Dis3. Moreover, our data suggest that additional substrates include transcripts involved in heterochromatin assembly. Mutant cells lacking Cid14 and/or Dis3 accumulate transcripts corresponding to naturally silenced repeat elements within heterochromatic domains, reflecting defects in centromeric gene silencing and derepression of subtelomeric gene expression. We also uncover roles for Cid14 and Dis3 in maintaining the genomic integrity of ribosomal DNA. Our data indicate that polyadenylation-assisted nuclear RNA turnover functions in eliminating a variety of RNA targets to control diverse processes, such as heterochromatic gene silencing, meiotic differentiation, and maintenance of genomic integrity.","authors":"Wang SW, Stevenson AL, Kearsey SE, Watt S, Bähler J","authors_abbrev":"Wang SW et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-11-21","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC26H8.10","SPAC12G12.13c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:32932721","title":"Activation of Cdc42 GTPase upon CRY2-Induced Cortical Recruitment Is Antagonized by GAPs in Fission Yeast.","citation":"Cells 2020 Sep 12;9(9)","abstract":"The small GTPase Cdc42 is critical for cell polarization in eukaryotic cells. In rod-shaped fission yeast  Schizosaccharomyces pombe  cells, active GTP-bound Cdc42 promotes polarized growth at cell poles, while inactive Cdc42-GDP localizes ubiquitously also along cell sides. Zones of Cdc42 activity are maintained by positive feedback amplification involving the formation of a complex between Cdc42-GTP, the scaffold Scd2, and the guanine nucleotide exchange factor (GEF) Scd1, which promotes the activation of more Cdc42. Here, we use the CRY2-CIB1 optogenetic system to recruit and cluster a cytosolic Cdc42 variant at the plasma membrane and show that this leads to its moderate activation also on cell sides. Surprisingly, Scd2, which binds Cdc42-GTP, is still recruited to CRY2-Cdc42 clusters at cell sides in individual deletion of the GEFs Scd1 or Gef1. We show that activated Cdc42 clusters at cell sides are able to recruit Scd1, dependent on the scaffold Scd2. However, Cdc42 activity is not amplified by positive feedback and does not lead to morphogenetic changes, due to antagonistic activity of the GTPase activating protein Rga4. Thus, the cell architecture is robust to moderate activation of Cdc42 at cell sides.","doi":"10.3390/cells9092089","authors":"Lamas I, Weber N, Martin SG","authors_abbrev":"Lamas I et al.","pubmed_publication_date":"12 Sep 2020","pubmed_entrez_date":"2020-09-16","publication_year":"2020","canto_session_key":"4ddaf53dca77bae5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-09-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9858548","title":"The msh2 gene of Schizosaccharomyces pombe is involved in mismatch repair, mating-type switching, and meiotic chromosome organization.","citation":"Mol Cell Biol 1999 Jan;19(1):241-50","abstract":"We have identified in the fission yeast Schizosaccharomyces pombe a MutS homolog that shows highest homology to the Msh2 subgroup. msh2 disruption gives rise to increased mitotic mutation rates and increased levels of postmeiotic segregation of genetic markers. In bandshift assays performed with msh2Delta cell extracts, a general mismatch-binding activity is absent. By complementation assays, we showed that S. pombe msh2 is allelic with the previously identified swi8 and mut3 genes, which are involved in mating-type switching. The swi8-137 mutant has a mutation in the msh2 gene which causes a truncated Msh2 peptide lacking a putative DNA-binding domain. Cytological analysis revealed that during meiotic prophase of msh2-defective cells, chromosomal structures were frequently formed; such structures are rarely found in the wild type. Our data show that besides having a function in mismatch repair, S. pombe msh2 is required for correct termination of copy synthesis during mating-type switching as well as for proper organization of chromosomes during meiosis.","authors":"Rudolph C, Kunz C, Parisi S, Lehmann E, Hartsuiker E, Fartmann B, Kramer W, Kohli J, Fleck O","authors_abbrev":"Rudolph C et al.","pubmed_publication_date":"Jan 1999","pubmed_entrez_date":"1998-12-22","publication_year":"1999","canto_session_key":"2f510be5fd1e3df3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-07-18 11:31:49","canto_approved_date":"2021-12-10 12:26:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-18 11:30:54","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-07-18"},{"uniquename":"EMBL:AU013939","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22855558","title":"Meiotic DNA joint molecule resolution depends on Nse5-Nse6 of the Smc5-Smc6 holocomplex.","citation":"Nucleic Acids Res 2012 Oct;40(19):9633-46","abstract":"Faithful chromosome segregation in meiosis is crucial to form viable, healthy offspring and in most species, it requires programmed recombination between homologous chromosomes. In fission yeast, meiotic recombination is initiated by Rec12 (Spo11 homolog) and generates single Holliday junction (HJ) intermediates, which are resolved by the Mus81-Eme1 endonuclease to generate crossovers and thereby allow proper chromosome segregation. Although Mus81 contains the active site for HJ resolution, the regulation of Mus81-Eme1 is unclear. In cells lacking Nse5-Nse6 of the Smc5-Smc6 genome stability complex, we observe persistent meiotic recombination intermediates (DNA joint molecules) resembling HJs that accumulate in mus81Δ cells. Elimination of Rec12 nearly completely rescues the meiotic defects of nse6Δ and mus81Δ single mutants and partially rescues nse6Δ mus81Δ double mutants, indicating that these factors act after DNA double-strand break formation. Likewise, expression of the bacterial HJ resolvase RusA partially rescues the defects of nse6Δ, mus81Δ and nse6Δ mus81Δ mitotic cells, as well as the meiotic defects of nse6Δ and mus81Δ cells. Partial rescue likely reflects the accumulation of structures other than HJs, such as hemicatenanes, and an additional role for Nse5-Nse6 most prominent during mitotic growth. Our results indicate a regulatory role for the Smc5-Smc6 complex in HJ resolution via Mus81-Eme1.","doi":"10.1093/nar/gks713","authors":"Wehrkamp-Richter S, Hyppa RW, Prudden J, Smith GR, Boddy MN","authors_abbrev":"Wehrkamp-Richter S et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-03","publication_year":"2012","canto_session_key":"3407f728d0cdab81","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.03c","SPAC17A5.11","SPAC11E3.08c","SPCC4G3.05c","SPAC644.14c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:29610759","title":"Molecular signature of the imprintosome complex at the mating-type locus in fission yeast.","citation":"Microb Cell 2018 Jan 16;5(4):169-183","abstract":"Genetic and molecular studies have indicated that an epigenetic imprint at  mat1 , the sexual locus of fission yeast, initiates mating type switching. The polar DNA replication of  mat1  generates an imprint on the Watson strand. The process by which the imprint is formed and maintained through the cell cycle remains unclear. To understand better the mechanism of imprint formation and stability, we characterized the recruitment of early players of mating type switching at the  mat1  region. We found that the switch activating protein 1 (Sap1) is preferentially recruited inside the  mat1M  allele on a sequence ( SS13 ) that enhances the imprint. The lysine specific demethylases, Lsd1/2, that control the replication fork pause at  MPS1  and the formation of the imprint are specifically drafted inside of  mat1 , regardless of the allele. The CENP-B homolog, Abp1, is highly enriched next to  mat1  but it is not required in the process. Additionally, we established the computational signature of the imprint. Using this signature, we show that both sides of the imprinted molecule are bound by Lsd1/2 and Sap1, suggesting a nucleoprotein protective structure defined as imprintosome.","doi":"10.15698/mic2018.04.623","authors":"Raimondi C, Jagla B, Proux C, Waxin H, Gangloff S, Arcangioli B","authors_abbrev":"Raimondi C et al.","pubmed_publication_date":"16 Jan 2018","pubmed_entrez_date":"2018-04-04","publication_year":"2018","canto_session_key":"e04e3fecdc0c6d2b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-05-14 11:13:41","canto_approved_date":"2025-09-03 12:58:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-04 14:14:17","canto_added_date":"2018-04-05 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.09","SPBC146.09c","SPAC1142.03c","SPAC23E2.02","SPCC1672.02c","SPBC216.06c","SPBC1105.04c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2018-05-14"},{"uniquename":"PMID:15643072","title":"Mcl1p is a polymerase alpha replication accessory factor important for S-phase DNA damage survival.","citation":"Eukaryot Cell 2005 Jan;4(1):166-77","abstract":"Mcl1p is an essential fission yeast chromatin-binding protein that belongs to a family of highly conserved eukaryotic proteins important for sister chromatid cohesion. The essential function is believed to result from its role as a Pol1p (polymerase alpha) accessory protein, a conclusion based primarily on analogy to Ctf4p's interaction with Pol1p. In this study, we show that Mcl1p also binds to Pol1p with high affinity for the N terminus of Pol1p during S phase and DNA damage. Characterization of an inducible allele of mcl1+, (nmt41)mcl1-MH, shows that altered expression levels of Mcl1p lead to sensitivity to DNA-damaging agents and synthetic lethality with the replication checkpoint mutations rad3Delta, rqh1Delta, and hsk1-1312. Further, we find that the overexpression of the S-phase checkpoint kinase, Cds1, or the loss of Hsk1 kinase activity can disrupt Mcl1p's interaction with chromatin and Pol1p during replication arrest with hydroxyurea. We take these data to mean that Mcl1p is a dynamic component of the polymerase alpha complex during replication and is important for the replication stress response in fission yeast.","authors":"Williams DR, McIntosh JR","authors_abbrev":"Williams DR et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2005-01-12","publication_year":"2005","canto_session_key":"3d88b1b5a61259cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-12-22 16:31:21","canto_approved_date":"2024-04-08 12:52:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-13 15:25:37","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.08","SPAC3H5.06c","SPCC18B5.11c","SPAPB1E7.02c","SPBC776.12c","SPCC1322.12c","SPAC2G11.12","SPAC664.07c","SPBC216.05","SPAC644.14c","SPAC15A10.03c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2015-12-22"},{"uniquename":"PMID:23261462","title":"Formation of non-toxic Aβ fibrils by small heat shock protein under heat-stress conditions.","citation":"Biochem Biophys Res Commun 2013 Jan 25;430(4):1259-64","abstract":"Small heat shock protein (sHsp) is a molecular chaperone with a conserved alpha-crystallin domain that can prevent protein aggregation. It has been shown that sHsps exist as oligomers (12-40 mer) and their dissociation into small dimers or oligomers is functionally important. Since several sHsps are upregulated and co-localized with amyloid-β (Aβ) in senile plaques of patients with Alzheimer's disease (AD), sHsps are thought to be involved in AD. Previous studies have also shown that sHsp can prevent Aβ aggregation in vitro. However, it remains unclear how the quaternary structure of sHsp influences Aβ aggregation. In this study, we report for the first time the effect of the quaternary structure of sHsp on Aβ aggregation using sHsp from the fission yeast Schizosaccharomyces pombe (SpHsp16.0) showing a clear temperature-dependent structural transition between an oligomer (30 °C) and dimer (50 °C) state. Aβ aggregation was inhibited by the oligomeric form of SpHsp16.0. In contrast, amyloid fibrils were formed in the presence of dimeric SpHsp16.0. Interestingly, these amyloid fibrils consisted of both Aβ and SpHsp16.0 and showed a low ThT intensity and low cytotoxicity due to their low binding affinity to the cell surface. These results suggest the formation of novel fibrillar Aβ amyloid with different characteristics from that of the authentic Aβ amyloid fibrils formed in the absence of sHsp. Our results also suggest the potential protective role of sHsp in AD under stress conditions.","doi":"10.1016/j.bbrc.2012.12.059","authors":"Sakono M, Utsumi A, Zako T, Abe T, Yohda M, Maeda M","authors_abbrev":"Sakono M et al.","pubmed_publication_date":"25 Jan 2013","pubmed_entrez_date":"2012-12-25","publication_year":"2013","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14527422","title":"BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases.","citation":"Mol Cell 2003 Sep;12(3):783-90","abstract":"Cullins (CULs) are subunits of a prominent class of RING ubiquitin ligases. Whereas the subunits and substrates of CUL1-associated SCF complexes and CUL2 ubiquitin ligases are well established, they are largely unknown for other cullin family members. We show here that S. pombe CUL3 (Pcu3p) forms a complex with the RING protein Pip1p and all three BTB/POZ domain proteins encoded in the fission yeast genome. The integrity of the BTB/POZ domain, which shows similarity to the cullin binding proteins SKP1 and elongin C, is required for this interaction. Whereas Btb1p and Btb2p are stable proteins, Btb3p is ubiquitylated and degraded in a Pcu3p-dependent manner. Btb3p degradation requires its binding to a conserved N-terminal region of Pcu3p that precisely maps to the equivalent SKP1/F box adaptor binding domain of CUL1. We propose that the BTB/POZ domain defines a recognition motif for the assembly of substrate-specific RING/cullin 3/BTB ubiquitin ligase complexes.","authors":"Geyer R, Wee S, Anderson S, Yates J, Wolf DA","authors_abbrev":"Geyer R et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-10-07","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC23H4.18c","SPAC13D6.04c","SPAC24H6.03","SPBC119.02","SPCC330.11","SPBC25B2.06c","SPBC12D12.08c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:35568117","title":"TripletGO: Integrating Transcript Expression Profiles with Protein Homology Inferences for Gene Function Prediction.","citation":"Genomics Proteomics Bioinformatics 2022 Oct;20(5):1013-1027","abstract":"Gene Ontology (GO) has been widely used to annotate functions of genes and gene products. Here, we proposed a new method, TripletGO, to deduce GO terms of protein-coding and non-coding genes, through the integration of four complementary pipelines built on transcript expression profile, genetic sequence alignment, protein sequence alignment, and naïve probability. TripletGO was tested on a large set of 5754 genes from 8 species (human, mouse, Arabidopsis, rat, fly, budding yeast, fission yeast, and nematoda) and 2433 proteins with available expression data from the third Critical Assessment of Protein Function Annotation challenge (CAFA3). Experimental results show that TripletGO achieves function annotation accuracy significantly beyond the current state-of-the-art approaches. Detailed analyses show that the major advantage of TripletGO lies in the coupling of a new triplet network-based profiling method with the feature space mapping technique, which can accurately recognize function patterns from transcript expression profiles. Meanwhile, the combination of multiple complementary models, especially those from transcript expression and protein-level alignments, improves the coverage and accuracy of the final GO annotation results. The standalone package and an online server of TripletGO are freely available at https://zhanggroup.org/TripletGO/.","doi":"10.1016/j.gpb.2022.03.001","authors":"Zhu YH, Zhang C, Liu Y, Omenn GS, Freddolino PL, Yu DJ, Zhang Y","authors_abbrev":"Zhu YH et al.","pubmed_publication_date":"Oct 2022","pubmed_entrez_date":"2022-05-14","publication_year":"2022","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2022-05-16 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12669083","title":"Yeasts make their mark.","citation":"Nat Cell Biol 2003 Apr;5(4):294-9","abstract":"Budding and fission yeast serve as genetic model organisms for the study of the molecular mechanisms of cell polarity in single cells. Similar to other polarized eukaryotic cells, yeast cells have polarity programmes that regulate where they grow and divide. Here, we describe recent advances in defining the proteins that establish cell polarity and the numerous molecular interactions that may link these factors to the actin cytoskeleton. As many of these components are identified, a comprehensive understanding of complex pathways is beginning to emerge.","authors":"Chang F, Peter M","authors_abbrev":"Chang F et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-04-02","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8955119","title":"Schizosaccharomyces pombe has a novel eukaryotic initiation factor 4F complex containing a cap-binding protein with the human eIF4E C-terminal motif KSGST.","citation":"J Biol Chem 1996 Dec 20;271(51):32818-24","abstract":"Genetic and biochemical analyses were performed on the cytoplasmic cap-binding complex (eukaryotic initiation factor (eIF) 4F) of Schizosaccharomyces pombe. Genomic and cDNA sequencing of the S. pombe gene (tif1) encoding the cap-binding component eIF4E revealed the presence of two introns in a reading frame of 219 codons. The encoded sequence of 218 amino acids shows a greater degree of identity to the mammalian eIF4E sequence than does its counterpart from Saccharomyces cerevisiae. In particular, unlike its S. cerevisiae counterpart, S.pombe eIF4E has a C-terminal Ser209 within the motif KSGST that is a site of phosphorylation in hamster and rabbit eIF4E. Of relevance to its potential regulatory role, eIF4E was found to be encoded by an mRNA with a six-nucleotide leader and to be of low abundance in vivo. Cross-linking experiments identified S. pombe eIF4E as the major cap-binding protein while a further protein, p36, also showed cap-dependent binding. eIF4A was not associated with the cap-binding complex. While S. pombe eIF4E was shown capable of binding S. cerevisiae p20, an equivalent protein was absent from the eIF4F complex isolated from S. pombe cells. S. pombe 4F therefore shows a remarkable combination of structural and functional properties, some of which it shares with its higher and its lower eukaryotic counterparts.","authors":"Ptushkina M, Fierro-Monti I, van den Heuvel J, Vasilescu S, Birkenhäger R, Mita K, McCarthy JE","authors_abbrev":"Ptushkina M et al.","pubmed_publication_date":"20 Dec 1996","pubmed_entrez_date":"1996-12-20","publication_year":"1996","canto_session_key":"9f25b078fb181765","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-13 18:03:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-13 12:30:33","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16E8.15"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2016-09-13"},{"uniquename":"PMID:40306164","title":"Crystal structure of GH71 α-1,3-glucanase Agn1p from Schizosaccharomyces pombe: an enzyme regulating cell division in fission yeast.","citation":"Biochem Biophys Res Commun 2025 Jun 20;766:151907","abstract":"Agn1p is a glycoside hydrolase family 71 α-1,3-glucanase from Schizosaccharomyces pombe. It is involved in cell division and releases nigero-pentaose from α-1,3-glucan as a primary hydrolysate. In this study, we used x-ray crystallography to determine the molecular structure of Agn1p, achieving a resolution of 1.80 Å for its free form and 2.10 Å for the substrate complex structure of an inactive mutant. We find that Agn1p comprises eight α-helices and sixteen β-strands, and these combined into a classical (α/β) 8  TIM-barrel core domain and a β-sandwich accessory domain. The TIM-barrel had a deep cavity in the center. Next, to determine which amino acid residues are involved in the catalytic reaction, we conducted substitution experiments on Asp-69, Asp-237, and Glu-240, three residues located in the cavity, preparing the corresponding substitution mutants D69N, D237A, D237N, E240A and E240Q. We found that the far-UV CD spectra of the five substitution mutants were similar to those of wild-type Agn1p, but all five mutants lost α-1,3-glucan hydrolyzing activity. We also obtained the cocrystal of the D237N mutant and nigero-heptaose, and its structure was determined. Specifically, we observed the electron density for the hexamer or pentamer sugar portion of nigero-heptaose. Moreover, the substrates were located in the vicinity of Asp-69, Asp-237, and Glu-240. Overall, these results suggest that Agn1p contains a stable substrate binding site for the hexamer or pentamer sugar structure of nigero-oligosaccharide.","doi":"10.1016/j.bbrc.2025.151907","authors":"Horaguchi Y, Saitoh H, Konno H, Makabe K, Yano S","authors_abbrev":"Horaguchi Y et al.","pubmed_publication_date":"20 Jun 2025","pubmed_entrez_date":"2025-04-30","publication_year":"2025","canto_session_key":"397cccc0b9c2f4c1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-05-01 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14668362","title":"Five RecA-like proteins of Schizosaccharomyces pombe are involved in meiotic recombination.","citation":"Genetics 2003 Nov;165(3):1031-43","abstract":"The genome of Schizosaccharomyces pombe contains five genes that code for proteins with sequence similarity to the Escherichia coli recombination protein RecA: rad51+, rhp55+, rhp57+, rlp1+, and dmc1+. We analyzed the effect of deletion of each of these genes on meiotic recombination and viability of spores. Meiotic recombination levels were different from wild type in all recA-related mutants in several genetic intervals, suggesting that all five RecA homologs of S. pombe are required for normal levels of meiotic recombination. Spore viability was reduced in rad51, rhp55, and rhp57 mutants, but not in rlp1 and dmc1. It is argued that reduction of crossover is not the only cause for the observed reduction of spore viability. Analysis of double and triple mutants revealed that Rad51 and Dmc1 play major and partially overlapping roles in meiotic recombination, while Rhp55, Rhp57, and Rlp1 play accessory roles. Remarkably, deletion of Rlp1 decreases the frequency of intergenic recombination (crossovers), but increases intragenic recombination (gene conversion). On the basis of our results, we present a model for the involvement of five RecA-like proteins of S. pombe in meiotic recombination and discuss their respective roles.","authors":"Grishchuk AL, Kohli J","authors_abbrev":"Grishchuk AL et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-12-12","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.03c","SPAC644.14c","SPAC8E11.03c","SPAC20H4.07","SPBC1685.11"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"EMBL:AU010127","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24204285","title":"Two portable recombination enhancers direct donor choice in fission yeast heterochromatin.","citation":"PLoS Genet 2013 Oct;9(10):e1003762","abstract":"Mating-type switching in fission yeast results from gene conversions of the active mat1 locus by heterochromatic donors. mat1 is preferentially converted by mat2-P in M cells and by mat3-M in P cells. Here, we report that donor choice is governed by two portable recombination enhancers capable of promoting use of their adjacent cassette even when they are transposed to an ectopic location within the mat2-mat3 heterochromatic domain. Cells whose silent cassettes are swapped to mat2-M mat3-P switch mating-type poorly due to a defect in directionality but cells whose recombination enhancers were transposed together with the cassette contents switched like wild type. Trans-acting mutations that impair directionality affected the wild-type and swapped cassettes in identical ways when the recombination enhancers were transposed together with their cognate cassette, showing essential regulatory steps occur through the recombination enhancers. Our observations lead to a model where heterochromatin biases competitions between the two recombination enhancers to achieve directionality.","doi":"10.1371/journal.pgen.1003762","authors":"Jakočiūnas T, Holm LR, Verhein-Hansen J, Trusina A, Thon G","authors_abbrev":"Jakočiūnas T et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-11-09","publication_year":"2013","canto_session_key":"08070f92a4eeb8a1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34428580","title":"Global view of dynamic expression and precise mapping of mitochondrial tRNAs-derived fragments during stressed conditions in S. pombe.","citation":"Mitochondrion 2021 Sep;60:219-227","abstract":"In this study, we provide a global view of population and processing of mitochondrial tRNAs-derived fragments (mt-tRFs) in fission yeast Schizosaccharomyces pombe. Here, mt-tRFs of 15-30 nucleotides were retrieved from S. pombe small RNA libraries obtained from unstressed, stress, and during stationary phase conditions. We demonstrate that production of these fragments increase during heat stress and stationary phase conditions in S. pombe, especially (most notably) in stationary phase. Analysis of data also reveals depending on the tRNA, either 5'-mt-tRF or 3'-mt-tRF was found and major mt-tRNA processing sites have been precisely identified. Furthermore, RNA-seq reveals that inactivation of trz2 encoding S. pombe mitochondrial tRNase Z L  globally impairs mt-tRF processing. Finally, our result showed mt-tRFs were predicted to target mitochondrial genome mapping mtDNA-encoded protein gene. These observations suggest that mitochondrial tRFs may play an important regulatory role in response to stress and development.","doi":"10.1016/j.mito.2021.08.012","authors":"Hu Y, Wu L, Zhang P, Wang Z, Shang J, Huang Y","authors_abbrev":"Hu Y et al.","pubmed_publication_date":"Sep 2021","pubmed_entrez_date":"2021-08-24","publication_year":"2021","canto_session_key":"06bf5588a3929a85","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-08-26 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31178220","title":"Structures of the Mitochondrial CDP-DAG Synthase Tam41 Suggest a Potential Lipid Substrate Pathway from Membrane to the Active Site.","citation":"Structure 2019 Aug 06;27(8):1258-1269.e4","abstract":"In mitochondria, CDP-diacylglycerol (CDP-DAG) is a crucial precursor for cardiolipin biosynthesis. Mitochondrial CDP-DAG is synthesized by the translocator assembly and maintenance protein 41 (Tam41) through an elusive process. Here we show that Tam41 adopts sequential catalytic mechanism, and report crystal structures of the bulk N-terminal region of Tam41 from Schizosaccharomyces pombe in the apo and CTP-bound state. The structure reveals that Tam41 contains a nucleotidyltransferase (NTase) domain and a winged helix domain. CTP binds to an \"L\"-shaped pocket sandwiched between the two domains. Rearrangement of a loop region near the active site is essential for opening the CTP-binding pocket. Docking of phosphatidic acid/CDP-DAG in the structure suggests a lipid entry/exit pathway connected to the \"L\"-shaped pocket. The C-terminal region of SpTam41 contains a positively charged amphipathic helix crucial for membrane association and participates in binding phospholipids. These results provide detailed insights into the mechanism of CDP-DAG biosynthesis in mitochondria.","doi":"10.1016/j.str.2019.04.017","authors":"Jiao H, Yin Y, Liu Z","authors_abbrev":"Jiao H et al.","pubmed_publication_date":"06 Aug 2019","pubmed_entrez_date":"2019-06-11","publication_year":"2019","canto_session_key":"2b7ee740ec49d7f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-02-29 15:20:49","canto_approved_date":"2020-03-06 16:36:59","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-02-19 14:55:30","canto_added_date":"2019-06-12 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-02-29","pdb_entries":[{"pdb_id":"6ig4","gene_chains":[{"gene_uniquename":"SPBC1A4.06c","chain":"A/B","position":"28-319"}],"title":"Structure of mitochondrial CDP-DAG synthase Tam41, delta 74","entry_authors":"Jiao HZ,Yin Y,Liu ZF","entry_authors_abbrev":"Jiao HZ et al.","reference_uniquename":"PMID:31178220","experimental_method":"X-ray","resolution":"2.261"},{"pdb_id":"6ig2","gene_chains":[{"gene_uniquename":"SPBC1A4.06c","chain":"A/B/C/D","position":"28-319"}],"title":"Structure of mitochondrial CDP-DAG synthase Tam41 complexed with CTP, delta 74, F240A","entry_authors":"Jiao HZ,Yin Y,Liu ZF","entry_authors_abbrev":"Jiao HZ et al.","reference_uniquename":"PMID:31178220","experimental_method":"X-ray","resolution":"2.882"}]},{"uniquename":"PMID:1438695","title":"Radiation-induced mitotic delay: a genetic characterization in the fission yeast.","citation":"Radiat Res 1992 Nov;132(2):144-52","abstract":"Radiation-induced mitotic delay is under investigation in the fission yeast, Schizosaccharomyces pombe. A large range of cell cycle- and radiation-sensitive mutants of this yeast is available to facilitate this effort. Through an examination of such mutants it has been shown that the X-ray transition point and the p34cdc2 execution point are coincident; wee1- strains are not delayed by irradiation; and the radiation-sensitive mutants rad1-1, rad3-136, rad9-192, and rad17-W are not delayed by radiation or by inhibitors of DNA synthesis, including hydroxyurea. A model is proposed: Damaged DNA generates a signal to delay mitosis which is carried by the products of the rad genes to activate the tyrosine kinase p110wee1. This in turn inactivates the serine/threonine kinase p34cdc2, thereby blocking entry to mitosis. Unreplicated DNA also initiates a signal to delay mitosis which is carried by these same rad genes but, as indicated in the literature, transmission to p34cdc2 does not require p110wee1. The delay-deficient rad mutants may possess some properties of tumor suppressor genes, with implications for mutagenesis and oncogenesis.","authors":"Rowley R","authors_abbrev":"Rowley R","pubmed_publication_date":"Nov 1992","pubmed_entrez_date":"1992-11-01","publication_year":"1992","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8274857","title":"Lineage-dependent mating-type transposition in fission and budding yeast.","citation":"Curr Opin Genet Dev 1993 Oct;3(5):745-51","abstract":"The basis of cellular differentiation is perhaps best understood in the yeast mating-type switching system. The yeast cell produces daughter cells that differ from each other or from their parent cell via developmentally regulated genomic rearrangements. Recent experiments on cell-type determination in fission yeast have revealed that this process is determined by the inheritance of specific parental chromosome strands by the progeny cells.","authors":"Klar AJ","authors_abbrev":"Klar AJ","pubmed_publication_date":"Oct 1993","pubmed_entrez_date":"1993-10-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38450805","title":"Reinstatement of the fission yeast species Schizosaccharomyces versatilis Wickerham et Duprat, a sibling species of Schizosaccharomyces japonicus.","citation":"Yeast 2024 Mar;41(3):108-127","abstract":"Schizosaccharomyces japonicus Yukawa et Maki (1931) and Schizosaccharomyces versatilis Wickerham et Duprat (1945) have been treated as varieties of S. japonicus or as conspecific, based on various approaches including mating trials and nDNA/nDNA optical reassociation studies. However, the type strains of S. japonicus and S. versatilis differ by five substitutions (99.15% identity) and one 1-bp indel in the sequences of the D1/D2 domain of the 26S rRNA gene, and 23 substitutions (96.3% identity) and 31-bp indels in the sequences of internal transcribed spacer (ITS) of rRNA, suggesting that they may not be conspecific. To reassess their taxonomic status, we conducted mating trials and whole-genome analyses. Mating trials using the type strains showed a strong but incomplete prezygotic sterility barrier, yielding interspecies mating products at two orders of magnitude lower efficiency than intraspecies matings. These mating products, which were exclusively allodiploid hybrids, were unable to undergo the haplontic life cycle of the parents. We generated chromosome-level gap-less genome assemblies for both type strains. Whole genome sequences yielded an average nucleotide identity (ANI) of 86.4%, indicating clear separation of S. japonicus and S. versatilis. Based on these findings, we propose the reinstatement of S. versatilis as a distinct species (holotype strain: CBS 103 T  and ex-types: NRRL Y-1026, NBRC 1607, ATCC 9987, PYCC 7100; Mycobank no.: 847838).","doi":"10.1002/yea.3922","authors":"Brysch-Herzberg M, Jia GS, Sipiczki M, Seidel M, Zhang WC, Du LL","authors_abbrev":"Brysch-Herzberg M et al.","pubmed_publication_date":"Mar 2024","pubmed_entrez_date":"2024-03-07","publication_year":"2024","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2024-03-09 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16038088","title":"The yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe: models for cell biology research.","citation":"Gravit Space Biol Bull 2005 Jun;18(2):3-9","abstract":"Yeast species provide excellent models for fundamental biological research. In this review, I will describe characteristics of the two most common laboratory systems: the fission yeast Schizosaccharomyces pombe, and the budding yeast Saccharomyces cerevisiae. They have substantial similarities that make them powerful as research tools, and also striking biological differences that make them complementary experimental models. Each provides unique tools for understanding environmental effects on cellular systems.","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-07-26","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22895252","title":"A novel RNAi protein, Dsh1, assembles RNAi machinery on chromatin to amplify heterochromatic siRNA.","citation":"Genes Dev 2012 Aug 15;26(16):1811-24","abstract":"In fission yeast, siRNA is generated from pericentromeric noncoding RNA by the RNAi machinery. siRNA synthesis and heterochromatin formation are interdependent, forming a self-reinforcing loop on chromatin. In this system, siRNA is amplified by the RNA-dependent RNA polymerase complex (RDRC) and the endoribonuclease Dcr1, which synthesizes dsRNA and processes the dsRNA, respectively. The amplification is essential for stable heterochromatin formation. Here, a novel gene, dsh1(+) (defect of the gene silencing at centromeric heterochromatin), is identified as an essential component of RNAi-directed heterochromatin assembly. Loss of dsh1(+) abolishes normal RNAi function and heterochromatic gene silencing at pericentromeres. Dsh1 interacts with Dcr1 and RDRC and couples the reactions of both proteins to the effective production of siRNA in vivo. Dsh1 binds to heterochromatin in the absence of RDRC, while RDRC requires Dsh1 for its chromatin-binding activity, suggesting that Dsh1 recruits RDRC to chromatin. Immunofluorescence analysis shows that Dsh1 forms foci at the nuclear periphery, and some Dsh1 foci colocalize with Dcr1 and RDRC. Dsh1 is required for the colocalization of Dcr1 and RDRC. Moreover, loss of the nuclear periphery localization of Dsh1 abolishes Dsh1 function. Taken together, these results suggest that Dsh1 assembles the RNAi machinery on heterochromatin and forms a perinuclear compartment for amplification of heterochromatic siRNA.","doi":"10.1101/gad.190272.112","authors":"Kawakami K, Hayashi A, Nakayama J, Murakami Y","authors_abbrev":"Kawakami K et al.","pubmed_publication_date":"15 Aug 2012","pubmed_entrez_date":"2012-08-17","publication_year":"2012","canto_session_key":"f1732559a5f79ef5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-01 09:30:09","canto_approved_date":"2024-06-07 14:54:56","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-05-20 13:00:34","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPAC18G6.02c","SPAC1786.03","SPAC6F12.09","SPBC582.04c","SPBC428.08c","SPCC736.11","SPBC83.03c","SPBC29B5.01","SPAC18G6.10","SPCC188.13c"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2015-06-01"},{"uniquename":"PMID:18701708","title":"Calnexin is involved in apoptosis induced by endoplasmic reticulum stress in the fission yeast.","citation":"Mol Biol Cell 2008 Oct;19(10):4404-20","abstract":"Stress conditions affecting the functions of the endoplasmic reticulum (ER) cause the accumulation of unfolded proteins. ER stress is counteracted by the unfolded-protein response (UPR). However, under prolonged stress the UPR initiates a proapoptotic response. Mounting evidence indicate that the ER chaperone calnexin is involved in apoptosis caused by ER stress. Here, we report that overexpression of calnexin in Schizosaccharomyces pombe induces cell death with apoptosis markers. Cell death was partially dependent on the Ire1p ER-stress transducer. Apoptotic death caused by calnexin overexpression required its transmembrane domain (TM), and involved sequences on either side of the ER membrane. Apoptotic death caused by tunicamycin was dramatically reduced in a strain expressing endogenous levels of calnexin lacking its TM and cytosolic tail. This demonstrates the involvement of calnexin in apoptosis triggered by ER stress. A genetic screen identified the S. pombe homologue of the human antiapoptotic protein HMGB1 as a suppressor of apoptotic death due to calnexin overexpression. Remarkably, overexpression of human calnexin in S. pombe also provoked apoptotic death. Our results argue for the conservation of the role of calnexin in apoptosis triggered by ER stress, and validate S. pombe as a model to elucidate the mechanisms of calnexin-mediated cell death.","authors":"Guérin R, Arseneault G, Dumont S, Rokeach LA","authors_abbrev":"Guérin R et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-08-15","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21270388","title":"Augmented annotation of the Schizosaccharomyces pombe genome reveals additional genes required for growth and viability.","citation":"Genetics 2011 Apr;187(4):1207-17","abstract":"Genome annotation is a synthesis of computational prediction and experimental evidence. Small genes are notoriously difficult to detect because the patterns used to identify them are often indistinguishable from chance occurrences, leading to an arbitrary cutoff threshold for the length of a protein-coding gene identified solely by in silico analysis. We report a systematic reappraisal of the Schizosaccharomyces pombe genome that ignores thresholds. A complete six-frame translation was compared to a proteome data set, the Pfam domain database, and the genomes of six other fungi. Thirty-nine novel loci were identified. RT-PCR and RNA-Seq confirmed transcription at 38 loci; 33 novel gene structures were delineated by 5' and 3' RACE. Expression levels of 14 transcripts fluctuated during meiosis. Translational evidence for 10 genes, evolutionary conservation data supporting 35 predictions, and distinct phenotypes upon ORF deletion (one essential, four slow-growth, two delayed-division phenotypes) suggest that all 39 predictions encode functional proteins. The popularity of S. pombe as a model organism suggests that this augmented annotation will be of interest in diverse areas of molecular and cellular biology, while the generality of the approach suggests widespread applicability to other genomes.","doi":"10.1534/genetics.110.123497","authors":"Bitton DA, Wood V, Scutt PJ, Grallert A, Yates T, Smith DL, Hagan IM, Miller CJ","authors_abbrev":"Bitton DA et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2011-01-29","publication_year":"2011","canto_session_key":"520be2a3e4ed5074","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2012-06-06 10:45:39","canto_approved_date":"2021-10-07 16:18:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-06-06 10:44:53","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23A1.20","SPBC8D2.23","SPCC330.20","SPAC1B3.21","SPAC13F5.07c","SPBC839.20","SPAC4D7.15","SPAPB17E12.14c","SPBC3H7.18","SPBC32F12.16","SPBC1709.12","SPBC887.22","SPCC4B3.20","SPBC1105.19","SPBC17D1.17","SPBC14C8.19","SPBC24C6.13","SPBC839.19","SPCP20C8.04","SPBC30D10.21","SPAC6B12.19","SPAC18B11.05","SPBC1711.10c","SPBC56F2.15","SPAC13F5.04c","SPAC688.04c","SPAC186.06","SPCC330.21","SPAC17G8.15","SPAC1F7.14c","SPAC1486.11","SPBC16H5.12c","SPBC1711.18","SPAC16E8.18c","SPRRNA.53","SPAC19G12.17","SPAC15A10.17","SPAC11D3.11c","SPAC3H5.13","SPAC688.11","SPAC1805.18","SPCC4G3.15c","SPAC926.10","SPAC222.19","SPBC530.16","SPBC409.23","SPAC3A11.03","SPACUNK4.14","SPBC25H2.11c","SPAC3G9.17","SPAC4D7.14","SPAC29A4.03c","SPAC823.04","SPBP8B7.31","SPBC29A10.17","SPBC4F6.10","SPCC1322.16","SPAC4F10.22","SPAC9G1.15c"],"gene_count":59,"ltp_gene_count":7,"approved_date":"2012-06-06"},{"uniquename":"PMID:38321948","title":"Ccq1 restrains Mre11-mediated degradation to distinguish short telomeres from double-strand breaks.","citation":"Nucleic Acids Res 2024 Feb 07;","abstract":"Telomeres protect chromosome ends and are distinguished from DNA double-strand breaks (DSBs) by means of a specialized chromatin composed of DNA repeats bound by a multiprotein complex called shelterin. We investigated the role of telomere-associated proteins in establishing end-protection by studying viable mutants lacking these proteins. Mutants were studied using a Schizosaccharomyces pombe model system that induces cutting of a 'proto-telomere' bearing telomere repeats to rapidly form a new stable chromosomal end, in contrast to the rapid degradation of a control DSB. Cells lacking the telomere-associated proteins Taz1, Rap1, Poz1 or Rif1 formed a chromosome end that was stable. Surprisingly, cells lacking Ccq1, or impaired for recruiting Ccq1 to the telomere, converted the cleaved proto-telomere to a rapidly degraded DSB. Ccq1 recruits telomerase, establishes heterochromatin and affects DNA damage checkpoint activation; however, these functions were separable from protection of the new telomere by Ccq1. In cells lacking Ccq1, telomere degradation was greatly reduced by eliminating the nuclease activity of Mre11 (part of the Mre11-Rad50-Nbs1/Xrs2 DSB processing complex), and higher amounts of nuclease-deficient Mre11 associated with the new telomere. These results demonstrate a novel function for S. pombe Ccq1 to effect end-protection by restraining Mre11-dependent degradation of the DNA end.","doi":"10.1093/nar/gkae044","authors":"Audry J, Zhang H, Kerr C, Berkner KL, Runge KW","authors_abbrev":"Audry J et al.","pubmed_publication_date":"07 Feb 2024","pubmed_entrez_date":"2024-02-07","publication_year":"2024","canto_session_key":"5937eb847b8666ff","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-02-08 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15802523","title":"A postsynaptic role for Rhp55/57 that is responsible for cell death in Deltarqh1 mutants following replication arrest in Schizosaccharomyces pombe.","citation":"Genetics 2005 Jun;170(2):519-31","abstract":"Following replication arrest, multiple cellular responses are triggered to maintain genomic integrity. In fission yeast, the RecQ helicase, Rqh1, plays a critical role in this process. This is demonstrated in Deltarqh1 cells that, following treatment with hydroxyurea (HU), undergo an aberrant mitosis leading to cell death. Previous data suggest that Rqh1 functions with homologous recombination (HR) in recovery from replication arrest. We have found that loss of the HR genes rhp55(+) or rhp57(+), but not rhp51(+) or rhp54(+), suppresses the HU sensitivity of Deltarqh1 cells. Much of this suppression requires Rhp51 and Rhp54. In addition, this suppression is partially dependent on swi5(+). In budding yeast, overexpressing Rad51 (the Rhp51 homolog) minimized the need for Rad55/57 (Rhp55/57) in nucleoprotein filament formation. We overexpressed Rhp51 in Schizosaccharomyces pombe and found that it greatly reduced the requirement for Rhp55/57 in recovery from DNA damage. However, overexpressing Rhp51 did not change the Deltarhp55 suppression of the HU sensitivity of Deltarqh1, supporting an Rhp55/57 function during HR independent of nucleoprotein filament formation. These results are consistent with Rqh1 playing a role late in HR following replication arrest and provide evidence for a postsynaptic function for Rhp55/57.","authors":"Hope JC, Maftahi M, Freyer GA","authors_abbrev":"Hope JC et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-04-02","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPAC15A10.03c","SPAC644.14c","SPBC409.03","SPAC3C7.03c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:22570491","title":"Yeast adaptor protein, Nbp2p, is conserved regulator of fungal Ptc1p phosphatases and is involved in multiple signaling pathways.","citation":"J Biol Chem 2012 Jun 22;287(26):22133-41","abstract":"Nbp2p is an Src homology 3 (SH3) domain-containing yeast protein that is involved in a variety of cellular processes. This small adaptor protein binds to a number of different proteins through its SH3 domain, and a region N-terminal to the SH3 domain binds to the protein phosphatase, Ptc1p. Despite its involvement in a large number of physical and genetic interactions, the only well characterized function of Nbp2p is to recruit Ptc1p to the high osmolarity glycerol pathway, which results in down-regulation of this pathway. In this study, we have discovered that Nbp2p orthologues exist in all Ascomycete and Basidiomycete fungal genomes and that all possess an SH3 domain and a conserved novel Ptc1p binding motif. The ubiquitous occurrence of these two features, which we have shown are both critical for Nbp2p function in Saccharomyces cerevisiae, implies that a conserved role of Nbp2p in all of these fungal species is the targeting of Ptc1p to proteins recognized by the SH3 domain. We also show that in a manner analogous to its role in the high osmolarity glycerol pathway, Nbp2p functions in the down-regulation of the cell wall integrity pathway through SH3 domain-mediated interaction with Bck1p, a component kinase of this pathway. Based on functional studies on the Schizosaccharomyces pombe and Neurospora crassa Nbp2p orthologues and the high conservation of the Nbp2p binding site in Bck1p orthologues, this function of Nbp2p appears to be conserved across Ascomycetes. Our results also clearly imply a function for the Nbp2p-Ptc1p complex other cellular processes.","doi":"10.1074/jbc.M112.348052","authors":"Stanger K, Gorelik M, Davidson AR","authors_abbrev":"Stanger K et al.","pubmed_publication_date":"22 Jun 2012","pubmed_entrez_date":"2012-05-10","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F3.02c","SPCC24B10.13"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:9917066","title":"Molecular genetic analysis of U2AF59 in Schizosaccharomyces pombe: differential sensitivity of introns to mutational inactivation.","citation":"RNA 1999 Jan;5(1):49-65","abstract":"The large subunit of the mammalian U2AF heterodimer (U2AF65) is essential for splicing in vitro. To expand our understanding of how this protein functions in vivo, we have created a null allele of the gene encoding the Schizosaccharomyces pombe ortholog, U2AF59, and employed it in a variety of genetic complementation assays. First, analysis of an extensive series of double amino acid substitutions indicates that this splicing factor is surprisingly refractory to mutations. Second, despite extensive structural conservation, we find that metazoan large subunit orthologs cannot substitute in vivo for fission yeast U2AF59. Third, because the activity of U2AF65 in vitro involves binding to the 3' polypyrimidine tract, we examined the splicing of introns containing or lacking this feature in a U2AF59 mutant described here as well as a previously isolated temperature-sensitive mutant (Potashkin et al., 1993, Science 262:573-575). Our data indicate that all four introns tested, including two that lack extensive runs of pyrimidines between the branchpoint and 3' splice site, show splicing defects upon shifting to the nonpermissive condition. In all cases, splicing is blocked prior to the first transesterification reaction in the mutants, consistent with the role inferred for human U2AF65 based on in vitro experiments.","authors":"Romfo CM, Lakhe-Reddy S, Wise JA","authors_abbrev":"Romfo CM et al.","pubmed_publication_date":"Jan 1999","pubmed_entrez_date":"1999-01-23","publication_year":"1999","canto_session_key":"72012f5a69c300fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-05-02 15:34:42","canto_approved_date":"2026-02-06 14:04:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 16:38:20","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":31,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_9917066_phaf.tsv"}],"genes":["SPCC285.09c","SPBC11B10.09","SPBC146.07","SPBC26H8.07c","SPAC3A12.14"],"gene_count":5,"ltp_gene_count":1,"approved_date":"2017-05-02"},{"uniquename":"PMID:8405927","title":"Effect of ethanol on the sterols of the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 1993 Aug 01;111(2-3):171-5","abstract":"Ergosterol, lanosterol and two further unidentified sterols were detected and quantified in Schizosaccharomyces pombe cell extracts. In cells grown under anaerobic conditions, the levels of these sterols were dramatically reduced with a concomitant increase of their squalene precursor as compared with cells growing under aerobic conditions. Presence of ethanol resulted in a decrease in the sterol content under aerobic conditions. On the contrary, under anaerobic conditions presence of ethanol resulted in a three-fold increase of total sterols. Lanosterol was the main constituent of this elevation. It is suggested that lanosterol in parallel with unsaturated fatty acids is responsible for maintaining membrane integrity of S. pombe cells growing in the presence of ethanol.","authors":"Koukkou AI, Tsoukatos D, Drainas C","authors_abbrev":"Koukkou AI et al.","pubmed_publication_date":"01 Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24621506","title":"Dissecting the first and the second meiotic divisions using a marker-less drug-hypersensitive fission yeast.","citation":"Cell Cycle 2014;13(8):1327-34","abstract":"Faithful chromosome segregation during meiosis is indispensable to prevent birth defects and infertility. Canonical genetic manipulations have not been very useful for studying meiosis II, since mutations of genes involved in cell cycle regulation or chromosome segregation may affect meiosis I, making interpretations of any defects observed in meiosis II complicated. Here we present a powerful strategy to dissect meiosis I and meiosis II, using chemical inhibitors in genetically tractable model organism fission yeast (Schizosaccharomyces pombe). As various chemical probes are not active in fission yeast, mainly due to an effective multidrug resistance (MDR) response, we have recently developed a drug-hypersensitive MDR-sup strain by suppression of the key genes responsible for MDR response. We further developed the MDR-supML (marker-less) strain by deleting 7 MDR genes without commonly used antibiotic markers. The new strain makes fluorescent tagging and gene deletion much simpler, which enables effective protein visualization in varied genetic backgrounds. Using the MDR-supML strain with chemical inhibitors and live cell fluorescence microscopy, we established cell cycle arrest at meiosis I and meiosis II and examined Aurora-dependent spindle assembly checkpoint (SAC) regulation during meiosis. We found that Aurora B/Ark1 kinase activity is required for recruitment of Bub1, an essential SAC kinase, to unattached kinetochore in prometaphase I and prometaphase II as in mitosis. Thus, Aurora's role in SAC activation is likely conserved in mitosis, meiosis I, and meiosis II. Together, our MDR-supML strain will be useful to dissect complex molecular mechanisms in mitosis and 2 successive meiotic divisions.","doi":"10.4161/cc.28294","authors":"Aoi Y, Sato M, Sutani T, Shirahige K, Kapoor TM, Kawashima SA","authors_abbrev":"Aoi Y et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-03-14","publication_year":"2014","canto_session_key":"108e9f8b302aa2c7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12867036","title":"Sir2 regulates histone H3 lysine 9 methylation and heterochromatin assembly in fission yeast.","citation":"Curr Biol 2003 Jul 15;13(14):1240-6","abstract":"Hypoacetylated histones are a hallmark of heterochromatin in organisms ranging from yeast to humans. Histone deacetylation is carried out by both NAD(+)-dependent and NAD(+)-independent enzymes. In the budding yeast Saccharomyces cerevisiae, deacetylation of histones in heterochromatic chromosomal domains requires Sir2, a phylogenetically conserved NAD(+)-dependent deacetylase. In the fission yeast Schizosaccharomyces pombe, NAD(+)-independent histone deacetylases are required for the formation of heterochromatin, but the role of Sir2-like deacetylases in this process has not been evaluated. Here, we show that spSir2, the S. pombe Sir2-like protein that is the most closely related to the S. cerevisiae Sir2, is an NAD(+)-dependent deacetylase that efficiently deacetylates histone H3 lysine 9 (K9) and histone H4 lysine 16 (K16) in vitro. In sir2 Delta cells, silencing at the donor mating-type loci, telomeres, and the inner centromeric repeats (imr) is abolished, while silencing at the outer centromeric repeats (otr) and rDNA is weakly reduced. Furthermore, Sir2 is required for hypoacetylation and methylation of H3-K9 and for the association of Swi6 with the above loci in vivo. Our findings suggest that the NAD(+)-dependent deacetylase Sir2 plays an important and conserved role in heterochromatin assembly in eukaryotes.","authors":"Shankaranarayana GD, Motamedi MR, Moazed D, Grewal SI","authors_abbrev":"Shankaranarayana GD et al.","pubmed_publication_date":"15 Jul 2003","pubmed_entrez_date":"2003-07-18","publication_year":"2003","canto_session_key":"9d58ec3ae4a32b92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-04 09:48:45","canto_approved_date":"2024-04-27 08:18:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-03 12:59:15","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPBC36.05c","SPBC428.08c","SPBC16D10.07c","SPAC664.01c"],"gene_count":5,"ltp_gene_count":1,"approved_date":"2024-02-04"},{"uniquename":"PMID:93918","title":"Inhibition kinetics of the plasma membrane ATPase activity of the yeast Schizosaccharomyces pombe [proceedings].","citation":"Arch Int Physiol Biochim 1979 Oct;87(4):810-2","abstract":"","authors":"Dufour JP, Boutry M, Goffeau A","authors_abbrev":"Dufour JP et al.","pubmed_publication_date":"Oct 1979","pubmed_entrez_date":"1979-10-01","publication_year":"1979","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38048463","title":"Rex1BD and the 14-3-3 protein control heterochromatin organization at tandem repeats by linking RNAi and HDAC.","citation":"Proc Natl Acad Sci U S A 2023 Dec 12;120(50):e2309359120","abstract":"Tandem DNA repeats are often organized into heterochromatin that is crucial for genome organization and stability. Recent studies revealed that individual repeats within tandem DNA repeats can behave very differently. How DNA repeats are assembled into distinct heterochromatin structures remains poorly understood. Here, we developed a genome-wide genetic screen using a reporter gene at different units in a repeat array. This screen led to identification of a conserved protein Rex1BD required for heterochromatin silencing. Our structural analysis revealed that Rex1BD forms a four-helix bundle structure with a distinct charged electrostatic surface. Mechanistically, Rex1BD facilitates the recruitment of Clr6 histone deacetylase (HDAC) by interacting with histones. Interestingly, Rex1BD also interacts with the 14-3-3 protein Rad25, which is responsible for recruiting the RITS (RNA-induced transcriptional silencing) complex to DNA repeats. Our results suggest that coordinated action of Rex1BD and Rad25 mediates formation of distinct heterochromatin structure at DNA repeats via linking RNAi and HDAC pathways.","doi":"10.1073/pnas.2309359120","authors":"Gao J, Sun W, Li J, Ban H, Zhang T, Liao J, Kim N, Lee SH, Dong Q, Madramootoo R, Chen Y, Li F","authors_abbrev":"Gao J et al.","pubmed_publication_date":"12 Dec 2023","pubmed_entrez_date":"2023-12-04","publication_year":"2023","canto_session_key":"c1c81dc437d962d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-25 15:08:04","canto_approved_date":"2024-06-07 13:15:30","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-25 14:02:30","canto_added_date":"2023-12-06 00:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":30,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC613.12c","SPAC29A4.18","SPAC18G6.02c","SPBC16D10.07c","SPAC17A2.13c","SPBC36.05c","SPCC188.13c","SPCC364.06","SPCC622.08c","SPCC622.09","SPAC4H3.06","SPAC664.01c"],"gene_count":12,"ltp_gene_count":7,"approved_date":"2024-03-25","pdb_entries":[{"pdb_id":"8j0h","gene_chains":[{"gene_uniquename":"SPAC4H3.06","chain":"A/B/C/D/E/F/G/H","position":"1-131"}],"title":"Crystal structure of the fission yeast Rex1BD protein(C4H3.06)","entry_authors":"Li J,Sun W,Chen Y","entry_authors_abbrev":"Li J et al.","reference_uniquename":"PMID:38048463","experimental_method":"X-ray","resolution":"3.383"}]},{"uniquename":"PANTHER:PTHR42051","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1A10.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2236039","title":"A putative protein kinase gene (kin1+) is important for growth polarity in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1990 Nov;87(21):8272-6","abstract":"Mixed synthetic oligonucleotides encoding a sequence conserved among tyrosine-specific protein kinases were used to probe the genome of the fission yeast Schizosaccharomyces pombe. A single gene (kin1+) was isolated that encodes a putative protein kinase closely related to the KIN1- and KIN2-encoded serine/threonine-specific protein kinases of Saccharomyces cerevisiae. kin1+ is transcribed into a 3.5-kilobase mRNA that contains an uninterrupted open reading frame encoding a polypeptide of 98 kDa. In contrast to results obtained with kin mutants of S. cerevisiae, disruption of the Sc. pombe kin1+ gene resulted in recessive morphological and growth defects. kin1-disrupted cells grew slowly on enriched medium and grew as spheres, in contrast to wild-type Sc. pombe cells, which grow as rods. Relative to kin1+ cells, kin1-disrupted cells were differentially sensitive to lysis by treatment with alpha- and beta-glucanases, suggesting an alteration in either the composition or the organization of their cell walls.","authors":"Levin DE, Bishop JM","authors_abbrev":"Levin DE et al.","pubmed_publication_date":"Nov 1990","pubmed_entrez_date":"1990-11-01","publication_year":"1990","canto_session_key":"246fd447dd1ab258","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-09-17 13:52:52","canto_approved_date":"2023-12-27 20:30:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-23 15:22:59","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"vw253 cam.ac.uk","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-17"},{"uniquename":"PMID:38598558","title":"Mathematical model for the role of multiple pericentromeric repeats on heterochromatin assembly.","citation":"PLoS Comput Biol 2024 Apr 10;20(4):e1012027","abstract":"Although the length and constituting sequences for pericentromeric repeats are highly variable across eukaryotes, the presence of multiple pericentromeric repeats is one of the conserved features of the eukaryotic chromosomes. Pericentromeric heterochromatin is often misregulated in human diseases, with the expansion of pericentromeric repeats in human solid cancers. In this article, we have developed a mathematical model of the RNAi-dependent methylation of H3K9 in the pericentromeric region of fission yeast. Our model, which takes copy number as an explicit parameter, predicts that the pericentromere is silenced only if there are many copies of repeats. It becomes bistable or desilenced if the copy number of repeats is reduced. This suggests that the copy number of pericentromeric repeats alone can determine the fate of heterochromatin silencing in fission yeast. Through sensitivity analysis, we identified parameters that favor bistability and desilencing. Stochastic simulation shows that faster cell division and noise favor the desilenced state. These results show the unexpected role of pericentromeric repeat copy number in gene silencing and provide a quantitative basis for how the copy number allows or protects repetitive and unique parts of the genome from heterochromatin silencing, respectively.","doi":"10.1371/journal.pcbi.1012027","authors":"Ghimire P, Motamedi M, Joh R","authors_abbrev":"Ghimire P et al.","pubmed_publication_date":"10 Apr 2024","pubmed_entrez_date":"2024-04-10","publication_year":"2024","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2024-04-10 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11284010","title":"Hut1 proteins identified in Saccharomyces cerevisiae and Schizosaccharomyces pombe are functional homologues involved in the protein-folding process at the endoplasmic reticulum.","citation":"Yeast 2001 Apr;18(6):543-54","abstract":"The Saccharomyces cerevisiae HUT1 gene (scHUT1) and the Schizosaccharomyces pombe hut1(+) gene (sphut1(+)) encode hydrophobic proteins with approximately 30% identity to a human UDP-galactose transporter-related gene (UGTrel1) product. These proteins show a significant similarity to the nucleotide sugar transporter and are conserved in many eukaryotic species, but their physiological functions are not known. Both scHUT1 and sphut1(+) genes are non-essential for cell growth under normal conditions, and their disruptants show no defects in the modification of O- and N-linked oligosaccharides, but are sensitive to a membrane-permeable reducing agent, dithiothreitol (DTT). Consistent with this phenotype, scHUT1 has genetic interaction with ERO1, which plays an essential role in the oxidation of secretory proteins at the endoplasmic reticulum (ER). Overexpression of the MPD1 or MPD2 genes, which were isolated as multicopy suppressors of protein disulphide isomerase (PDI) depletion, could not replace the essential function of PDI in Delta hut1 S. cerevisiae cells. Our results indicate that scHut1p and spHut1p are functional homologues, and their physiological function is to maintain the optimal environment for the folding of secretory pathway proteins in the ER.","authors":"Nakanishi H, Nakayama K, Yokota A, Tachikawa H, Takahashi N, Jigami Y","authors_abbrev":"Nakanishi H et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-04-03","publication_year":"2001","canto_session_key":"980d77156c24f22a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-09-20 13:47:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 10:00:12","canto_added_date":"2012-02-24 05:51:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.04c","SPBC839.11c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2013-09-20"},{"uniquename":"PMID:22253882","title":"The RNA binding protein Csx1 promotes sexual differentiation in Schizosaccharomyces pombe.","citation":"PLoS One 2012;7(1):e30067","abstract":"Sexual differentiation is a highly regulated process in the fission yeast Schizosaccharomyces pombe and is triggered by nutrient depletion, mainly nitrogen source. One of the key regulatory proteins in fission yeast sexual differentiation is the transcription factor Ste11. Ste11 regulates the transcription of many genes required for the initial steps of conjugation and meiosis, and its deficiency leads to sterility. Ste11 activity is mainly regulated at two levels: phosphorylation and abundance of its mRNA. Csx1 is an RNA binding protein that we have previously described to bind and regulate the turnover rate of the mRNA encoding the transcription factor Atf1 in the presence of oxidative stress. We have observed that Csx1-deficient cells have defects in sexual differentiation and are partially sterile. We investigated how Csx1 is regulating this process in S. pombe. Csx1 associates with ste11+ mRNA and cells lacking Csx1 are sterile with a reduced amount of ste11+ mRNA. Overexpression of ste11+ mRNA completely rescues the mating deficiencies of csx1Δ cells. Here, we present a novel mechanism of ste11+ mRNA positive regulation through the activity of Csx1, an RNA binding protein that also have key functions in the response to oxidative stress in fission yeast. This finding opens interesting question about the possible coordination of sexual differentiation and oxidative stress response in eukaryotes and the role of RNA binding proteins in the adaptation to environmental signals.","doi":"10.1371/journal.pone.0030067","authors":"Matia-Gonzalez AM, Sotelo J, Rodriguez-Gabriel MA","authors_abbrev":"Matia-Gonzalez AM et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-01-19","publication_year":"2012","canto_session_key":"4c351db7ebe737e8","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A2.09c","SPBC32C12.02"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:21089501","title":"[Regulation of telomere DNA by telomere-specific chromatin structure].","citation":"Tanpakushitsu Kakusan Koso 2009 Mar;54(4 Suppl):514-20","abstract":"","authors":"Kanoh J","authors_abbrev":"Kanoh J","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2010-11-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1996094","title":"p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts.","citation":"Mol Cell Biol 1991 Mar;11(3):1326-33","abstract":"The human p68 protein is an RNA-dependent ATPase and RNA helicase which was first identified because of its immunological cross-reaction with a viral RNA helicase, simian virus 40 large T antigen. It belongs to a recently discovered family of proteins (DEAD box proteins) that share extensive regions of amino acid sequence homology, are ubiquitous in living organisms, and are involved in many aspects of RNA metabolism, including splicing, translation, and ribosome assembly. We have shown by immunofluorescent microscopy that mammalian p68, which is excluded from the nucleoli during interphase, translocates to prenucleolar bodies during telophase. We have cloned 55% identical genes from both Schizosaccharomyces pombe and Saccharomyces cerevisiae and shown that they are essential in both yeasts. The human and yeast genes contain a large intron whose position has been precisely conserved. In S. cerevisiae, the intron is unusual both because of its size and because of its location near the 3' end of the gene. We discuss possible functional roles for such an unusual intron in an RNA helicase gene.","authors":"Iggo RD, Jamieson DJ, MacNeill SA, Southgate J, McPheat J, Lane DP","authors_abbrev":"Iggo RD et al.","pubmed_publication_date":"Mar 1991","pubmed_entrez_date":"1991-03-01","publication_year":"1991","canto_session_key":"8a463471279b29b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2012-07-16 15:44:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-03-03 12:47:44","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP8B7.16c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-03-03"},{"uniquename":"PMID:10369673","title":"Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast.","citation":"EMBO J 1999 Jun 15;18(12):3325-33","abstract":"Phytochelatins play major roles in metal detoxification in plants and fungi. However, genes encoding phytochelatin synthases have not yet been identified. By screening for plant genes mediating metal tolerance we identified a wheat cDNA, TaPCS1, whose expression in Saccharomyces cerevisiae results in a dramatic increase in cadmium tolerance. TaPCS1 encodes a protein of approximately 55 kDa with no similarity to proteins of known function. We identified homologs of this new gene family from Arabidopsis thaliana, Schizosaccharomyces pombe, and interestingly also Caenorhabditis elegans. The Arabidopsis and S.pombe genes were also demonstrated to confer substantial increases in metal tolerance in yeast. PCS-expressing cells accumulate more Cd2+ than controls. PCS expression mediates Cd2+ tolerance even in yeast mutants that are either deficient in vacuolar acidification or impaired in vacuolar biogenesis. PCS-induced metal resistance is lost upon exposure to an inhibitor of glutathione biosynthesis, a process necessary for phytochelatin formation. Schizosaccharomyces pombe cells disrupted in the PCS gene exhibit hypersensitivity to Cd2+ and Cu2+ and are unable to synthesize phytochelatins upon Cd2+ exposure as determined by HPLC analysis. Saccharomyces cerevisiae cells expressing PCS produce phytochelatins. Moreover, the recombinant purified S.pombe PCS protein displays phytochelatin synthase activity. These data demonstrate that PCS genes encode phytochelatin synthases and mediate metal detoxification in eukaryotes.","authors":"Clemens S, Kim EJ, Neumann D, Schroeder JI","authors_abbrev":"Clemens S et al.","pubmed_publication_date":"15 Jun 1999","pubmed_entrez_date":"1999-06-16","publication_year":"1999","canto_session_key":"168bceb80cef3319","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-21 14:30:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-10 15:49:42","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H1.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-10"},{"uniquename":"PMID:24155978","title":"Possible involvement of nitric oxide and reactive oxygen species in glucose deprivation-induced activation of transcription factor rst2.","citation":"PLoS One 2013;8(10):e78012","abstract":"Glucose is one of the most important sources of cellular nutrition and glucose deprivation induces various cellular responses. In Schizosaccharomyces pombe, zinc finger protein Rst2 is activated upon glucose deprivation, and regulates gene expression via the STREP (stress response element of Schizosaccharomyces pombe) motif. However, the activation mechanism of Rst2 is not fully understood. We monitored Rst2 transcriptional activity in living cells using a Renilla luciferase reporter system. Hydrogen peroxide (H2O2) enhanced Rst2 transcriptional activity upon glucose deprivation and free radical scavenger inhibited Rst2 transcriptional activity upon glucose deprivation. In addition, deletion of the trx2 (+) gene encoding mitochondrial thioredoxin enhanced Rst2 transcriptional activity. Notably, nitric oxide (NO) generators enhanced Rst2 transcriptional activity upon glucose deprivation as well as under glucose-rich conditions. Furthermore, NO specific scavenger inhibited Rst2 transcriptional activity upon glucose deprivation. Altogether, our data suggest that NO and reactive oxygen species may be involved in the activation of transcription factor Rst2.","doi":"10.1371/journal.pone.0078012","authors":"Kato T, Zhou X, Ma Y","authors_abbrev":"Kato T et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-10-25","publication_year":"2013","canto_session_key":"b096f47215a08c2e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-01-20 18:51:03","canto_approved_date":"2021-01-22 12:28:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-31 05:54:27","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.02","SPAC24B11.06c","SPBC106.10","SPAC7D4.07c","SPAC1783.07c","SPBC12D12.07c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2019-01-20"},{"uniquename":"PMID:2298254","title":"Effects of leptomycin B on the cell cycle of fibroblasts and fission yeast cells.","citation":"Exp Cell Res 1990 Mar;187(1):150-6","abstract":"An antifungal antibiotic, leptomycin B (LMB), which induced cell elongation of fission yeast, Schizosaccharomyces pombe, was found to be a unique inhibitor of the cell cycle of mammalian and fission yeast cells. Proliferation of rat 3Y1 fibroblasts was reversibly blocked by LMB in both the G1 and G2 phases and the treated cells were presumably introduced into the resting state (GO). After removal of LMB, proliferative tetraploid cells were produced from the cells which had been arrested by LMB at the G2 phase, as a result of DNA replication without passage through the M phase. LMB also inhibited the proliferation of S. pombe in both the G1 and G2 phases. These results suggest that the molecular target of LMB is one of the components necessary for progression of both G1 and G2 in the eukaryotic cell cycle.","authors":"Yoshida M, Nishikawa M, Nishi K, Abe K, Horinouchi S, Beppu T","authors_abbrev":"Yoshida M et al.","pubmed_publication_date":"Mar 1990","pubmed_entrez_date":"1990-03-01","publication_year":"1990","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23690545","title":"Control of Sty1 MAPK activity through stabilisation of the Pyp2 MAPK phosphatase.","citation":"J Cell Sci 2013 Aug 01;126(Pt 15):3324-32","abstract":"In all eukaryotes tight control of mitogen-activated protein kinase (MAPK) activity plays an important role in modulating intracellular signalling in response to changing environments. The fission yeast MAPK Sty1 (also known as Spc1 or Phh1) is highly activated in response to a variety of external stresses. To avoid segregation of damaged organelles or chromosomes, strong Sty1 activation transiently blocks mitosis and cell division until such stresses have been dealt with. MAPK phosphatases dephosphorylate Sty1 to reduce kinase activity. Therefore, tight control of MAPK phosphatases is central for stress adaptation and for cell division to resume. In contrast to Pyp1, the fission yeast Pyp2 MAPK phosphatase is under environmental control. Pyp2 has a unique sequence (the linker region) between the catalytic domain and the N-terminal MAPK-binding site. Here we show that the Pyp2 linker region is a destabilisation domain. Furthermore, the linker region is highly phosphorylated to increase Pyp2 protein stability and this phosphorylation is Sty1 dependent. Our data suggests that Sty1 activation promotes Pyp2 phosphorylation to increase the stability of the phosphatase. This MAPK-dependent Pyp2 stabilisation allows cells to attenuate MAPK signalling and resume cell division, once stresses have been dealt with.","doi":"10.1242/jcs.122531","authors":"Kowalczyk KM, Hartmuth S, Perera D, Stansfield P, Petersen J","authors_abbrev":"Kowalczyk KM et al.","pubmed_publication_date":"01 Aug 2013","pubmed_entrez_date":"2013-05-22","publication_year":"2013","canto_session_key":"1f11c6ccf7a93b35","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Katarzyna Kowalczyk","canto_first_approved_date":"2026-04-29 10:26:22","canto_approved_date":"2026-04-29 10:26:23","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-04-23 06:23:05","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Katarzyna Kowalczyk","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":24,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC19D5.01","SPAC24B11.06c","SPBC409.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2026-04-29"},{"uniquename":"EMBL:AF073893","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32182184","title":"Cdc42 promotes Bgs1 recruitment for septum synthesis and glucanase localization for cell separation during cytokinesis in fission yeast.","citation":"Small GTPases 2021 Jul;12(4):257-264","abstract":"Cytokinesis in fission yeast involves actomyosin ring constriction concurrent to septum synthesis followed by septum digestion resulting in cell separation. A recent report indicates that endocytosis is required for septum synthesis and cell separation. The conserved GTPase Cdc42 is required for membrane trafficking and promotes endocytosis. Cdc42 is activated by Guanine nucleotide exchange factors (GEFs). Cdc42 GEFs have been shown to promote timely initiation of septum synthesis and proper septum morphology. Here we show that Cdc42 promotes the recruitment of the major primary septum synthesizing enzyme Bgs1 and consequent ring constriction. Cdc42 is also required for proper localization of the septum digesting glucanases at the division site. Thus, Cdc42 is required to promote multiple steps during cytokinesis.","doi":"10.1080/21541248.2020.1743926","authors":"Onwubiko UN, Rich-Robinson J, Mustaf RA, Das ME","authors_abbrev":"Onwubiko UN et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2020-03-18","publication_year":"2021","canto_session_key":"f0b2fc70769777ce","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-03-19 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03","SPAC821.09","SPBC19G7.05c","SPAC14C4.09"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:33225241","title":"The Hsp40 Mas5 Connects Protein Quality Control and the General Stress Response through the Thermo-sensitive Pyp1.","citation":"iScience 2020 Nov 20;23(11):101725","abstract":"Upon heat shock, the fission yeast Hsp40 chaperone Mas5 drives temperature-sensitive proteins toward protein aggregate centers (PACs) to avoid their degradation until lower temperatures favor their refolding. We show here that cells lacking Mas5 are resistant to oxidative stress. Components of the general stress pathways, the MAP kinase Sty1 and the transcription factor Atf1, are suppressors of this phenotype. Strain  Δmas5  expresses higher levels of Sty1- and Atf1-dependent stress genes than wild-type cells. Pyp1, the main tyrosine phosphatase maintaining Sty1 inactive in the absence of stress, is a temperature-sensitive protein that aggregates upon temperature up-shifts in a Mas5-dependent manner. In strain  Δmas5,  Pyp1 is sent to proteasomal degradation even in the absence of stress. We propose that Pyp1 is a thermo-sensitive phosphatase, which during heat stress coalescences into PACs in a Mas5-dependent manner, to promote full activation of the anti-stress Sty1-Atf1 cascade.","doi":"10.1016/j.isci.2020.101725","authors":"Boronat S, Marte L, Vega M, García-Santamarina S, Cabrera M, Ayté J, Hidalgo E","authors_abbrev":"Boronat S et al.","pubmed_publication_date":"20 Nov 2020","pubmed_entrez_date":"2020-11-23","publication_year":"2020","canto_session_key":"6fc9b53e91be9283","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Susanna Boronat","canto_first_approved_date":"2021-01-28 16:49:44","canto_approved_date":"2024-06-28 09:22:16","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-01-18 14:06:37","canto_added_date":"2020-11-25 01:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Susanna Boronat","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.02c","SPBC29B5.01","SPAP8A3.04c","SPBC16D10.08c","SPCC757.07c","SPCC1739.13","SPBC1734.11","SPAC13G7.02c","SPAC24B11.06c","SPBC32F12.03c","SPAC26F1.10c","SPAC1783.07c"],"gene_count":12,"ltp_gene_count":9,"approved_date":"2021-01-28"},{"uniquename":"PMID:9892665","title":"Moe1, a conserved protein in Schizosaccharomyces pombe, interacts with a Ras effector, Scd1, to affect proper spindle formation.","citation":"Proc Natl Acad Sci U S A 1999 Jan 19;96(2):517-22","abstract":"In fission yeast, Scd1/Ral1 is a putative guanine nucleotide exchange factor for Cdc42sp and also acts as a Ras1 effector necessary for the regulation of cytoskeleton organization. In this study, we have characterized a protein, Moe1, that binds directly to Scd1. A moe1 null (Delta) mutant exhibits numerous phenotypes indicative of abnormal microtubule functioning, including an abnormality in the spindle. moe1Delta mutants are resistant to microtubule destabilizing agents; moreover, moe1Delta rescued the growth defects of tubulin mutants containing unstable microtubules. These results suggest that Moe1 induces instability in microtubules. Biochemical and subcellular localization studies suggest that Moe1 and Scd1 colocalize in the nucleus. Furthermore, loss of function in Scd1 or Ras1 also induced abnormality in the spindle and is synthetically lethal with moe1Delta producing cells that lack a detectable spindle. These data demonstrate that Moe1 is a component of the Ras1 pathway necessary for proper spindle formation in the nucleus. Human and nematode Moe1 both can substitute for yeast Moe1, indicating that the function of Moe1 in spindle formation has been conserved substantially during evolution.","authors":"Chen CR, Li YC, Chen J, Hou MC, Papadaki P, Chang EC","authors_abbrev":"Chen CR et al.","pubmed_publication_date":"19 Jan 1999","pubmed_entrez_date":"1999-01-20","publication_year":"1999","canto_session_key":"0ce84786ff8858d0","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC637.07","SPAC110.03","HGNC:3278","SPAC16E8.09","SPAC22H10.07","SPAC17H9.09c","SPBC16A3.15c","SPBC26H8.07c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:39527190","title":"High-Throughput Measurement of Single-Fission Yeast Cell Volume Using Fluorescence Exclusion.","citation":"Methods Mol Biol 2025;2862:7-32","abstract":"Cell volume is a critical parameter for the biology of living species and has an impact on virtually all cellular functions. In Schizosaccharomyces pombe, the regulation of cell size has been the focus of intense investigation, and mechanisms that couple size control with cell cycle progression have been identified. In fission yeast, cell length at division is generally used as a proxy for determining cell size. However, it only allows for an inaccurate evaluation of this critical parameter and neglects potential changes in cell morphology and diameter, which can strongly impact cell volume. Until recently, one of the major obstacles for studying the complexity of cell size regulation in fission yeast has been the lack of a robust method for high-throughput, direct measurement of single-cell volume. Here, we provide a comprehensive protocol for S. pombe cell volume determination based on the Fluorescence eXclusion method and microfluidics technologies. This approach makes it possible to reliably describe cell volume and its distribution in populations of fission yeast cells.","doi":"10.1007/978-1-0716-4168-2_2","authors":"Venkova L, García-Ruano D, Jain A, Charvin G, Coudreuse D","authors_abbrev":"Venkova L et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30782292","title":"Hydrogen peroxide-induced oxidative stress upregulates ght5 gene belonging to hexose transporters in Schizosaccharomyces pombe.","citation":"Cell Mol Biol (Noisy-le-grand) 2019 Jan 31;65(1):41-45","abstract":"Hydrogen peroxide is an agent that triggers oxidative stress. Glucose, which is a source of carbon and energy has a regulatory role in many metabolic processes such as growth rate, fermentation capacity and stress response. Schizosaccharomyces pombe has eight hexose transporters with a different affinity for glucose and/or related monosaccharides. In S. pombe, Ght5 is a glucose transporter with high-affinity. We aimed to investigate the effects of H2O2-induced oxidative stress on hexose transporters using glucose repression-resistant mutant strains (ird5 and ird11) of S. pombe. We analyzed the percentage of glucose consumption in S. pombe wild-type and mutant cells under stressed and non-stressed conditions. Then we compared the expression levels of the genes encoding hexose transporters under the same conditions. We confirmed that the glucose consumption efficiencies of the mutants were slower than the wild-type as in earlier study under non-stressed condition. The percentage of glucose consumption reduced by approximately two-fold in ird11 and wild-type, but not change in ird5, under a stressed condition. There is no difference between cells shape and size of S. pombe strains under stressed and non-stressed conditions. Under stress-induced condition, the expression levels of ght3, ght4 genes in ird11 and wild-type, and ght4, ght6 genes in ird5 decreased, but that of ght5 gene remarkably increased in only wild-type. We suggested that oxidative stress caused by H2O2 leads to upregulation of the ght5 gene in S. pombe.","authors":"Kına UY, Palabiyik B","authors_abbrev":"Kına UY et al.","pubmed_publication_date":"31 Jan 2019","pubmed_entrez_date":"2019-02-21","publication_year":"2019","canto_session_key":"edb7b33c2bb25522","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-02-22 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1235.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33771877","title":"RNA polymerase backtracking results in the accumulation of fission yeast condensin at active genes.","citation":"Life Sci Alliance 2021 Jun;4(6)","abstract":"The mechanisms leading to the accumulation of the SMC complexes condensins around specific transcription units remain unclear. Observations made in bacteria suggested that RNA polymerases (RNAPs) constitute an obstacle to SMC translocation, particularly when RNAP and SMC travel in opposite directions. Here we show in fission yeast that gene termini harbour intrinsic condensin-accumulating features whatever the orientation of transcription, which we attribute to the frequent backtracking of RNAP at gene ends. Consistent with this, to relocate backtracked RNAP2 from gene termini to gene bodies was sufficient to cancel the accumulation of condensin at gene ends and to redistribute it evenly within transcription units, indicating that RNAP backtracking may play a key role in positioning condensin. Formalization of this hypothesis in a mathematical model suggests that the inclusion of a sub-population of RNAP with longer dwell-times is essential to fully recapitulate the distribution profiles of condensin around active genes. Taken together, our data strengthen the idea that dense arrays of proteins tightly bound to DNA alter the distribution of condensin on chromosomes.","doi":"10.26508/lsa.202101046","authors":"Rivosecchi J, Jost D, Vachez L, Gautier FD, Bernard P, Vanoosthuyse V","authors_abbrev":"Rivosecchi J et al.","pubmed_publication_date":"Jun 2021","pubmed_entrez_date":"2021-03-27","publication_year":"2021","canto_session_key":"d21245ab5467d47b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Vincent Vanoosthuyse","canto_first_approved_date":"2021-04-28 13:43:36","canto_approved_date":"2024-04-04 09:02:44","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-04-07 06:53:54","canto_added_date":"2021-03-29 00:15:07","annotation_curators":[{"name":"Vincent Vanoosthuyse","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPAC1705.03c","SPAC19B12.02c","SPBC21H7.05","SPCC306.03c","SPAC29E6.08","SPBC146.03c","SPAC20H4.03c","SPBC1105.05","SPCC330.13","SPAC821.09","SPAC23C4.15","SPAC6G9.10c"],"gene_count":13,"ltp_gene_count":3,"approved_date":"2021-04-28"},{"uniquename":"PMID:29428193","title":"Interactions between RNAP III transcription machinery and tRNA processing factors.","citation":"Biochim Biophys Acta Gene Regul Mech 2018 Apr;1861(4):354-360","abstract":"Eukaryotes have at least three nuclear RNA polymerases to carry out transcription. While RNA polymerases I and II are responsible for ribosomal RNA transcription and messenger RNA transcription, respectively, RNA Polymerase III transcribes approximately up to 300 nt long noncoding RNAs, including tRNA. For all three RNAPs, the nascent transcripts generated undergo extensive post-transcriptional processing. Transcription of mRNAs by RNAP II and their processing are coupled with the aid of the C-terminal domain of the RNAP II. RNAP I transcription and the processing of its transcripts are co-localized to the nucleolus and to some extent, rRNA processing occurs co-transcriptionally. Here, I review the current evidence for the interaction between tRNA processing factors and RNA polymerase III. These interactions include the moonlighting functions of tRNA processing factors in RNAP III transcription and the indirect effect of tRNA transcription levels on tRNA modification machinery.","doi":"10.1016/j.bbagrm.2018.02.003","authors":"Arimbasseri GA","authors_abbrev":"Arimbasseri GA","pubmed_publication_date":"Apr 2018","pubmed_entrez_date":"2018-02-12","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-08-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000052","title":"Gene Ontology annotation based on curation of immunofluorescence data","abstract":"GO Cellular Component terms are manually assigned by curators studying high resolution confocal microscopy images of immunohistochemically stained tissue. The methodology uses antibody-based proteomics which combines high-throughput generation of affinity-purified antibodies with protein profiling in a variety of cells and tissues. Further information on the annotation methods can be found at http://www.proteinatlas.org/about/assays+annotation <br>Annotations are only exported to the GO Consortium if the localizations are supported by literature, according to the following validation grading:<br>Supportive - Subcellular localization supported by literature.<br>1) One/multiple localizations supported by literature.<br>2) Multiple localizations partly supported (at least one) by literature.<br>3) One/multiple localizations in cytoplasm (i.e. Golgi, mitochondria, ER etc) with literature supporting cytoplasmic localization. <br>Prior to February 2013, all Human Protein Atlas annotations were referenced by PMID:18029348 (Barbe et al. 2008 Mol. Cell Proteomics. 7:499-508), a paper describing the protein localization pilot study and methodology used by the Human Protein Atlas. However, it has been decided that these annotations are more correctly described by a GO reference.<br>Resource URL: http://www.proteinatlas.org <br>Protein subcellular localization images can be viewed on the Human Protein Atlas website, e.g. http://www.proteinatlas.org/ENSG00000175899/summary#ifcelline","authors":"Human Protein Atlas","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25690009","title":"Pombe's thirteen - control of fission yeast cell division by the septation initiation network.","citation":"J Cell Sci 2015 Apr 15;128(8):1465-74","abstract":"The septation initiation network (SIN) regulates aspects of cell growth and division in Schizosaccharomyces pombe and is essential for cytokinesis. Insufficient signalling results in improper assembly of the contractile ring and failure of cytokinesis, generating multinucleated cells, whereas too much SIN signalling uncouples cytokinesis from the rest of the cell cycle. SIN signalling is therefore tightly controlled to coordinate cytokinesis with chromosome segregation. Signalling originates from the cytoplasmic face of the spindle pole body (SPB), and asymmetric localisation of some SIN proteins to one of the two SPBs during mitosis is important for regulation of the SIN. Recent studies have identified in vivo substrates of the SIN, which include components involved in mitotic control, those of the contractile ring and elements of the signalling pathway regulating polarised growth. The SIN is also required for spore formation following meiosis. This has provided insights into how the SIN performs its diverse functions in the cell cycle and shed new light on its regulation.","doi":"10.1242/jcs.094821","authors":"Simanis V","authors_abbrev":"Simanis V","pubmed_publication_date":"15 Apr 2015","pubmed_entrez_date":"2015-02-19","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-02-20 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33719348","title":"Duplex Telomere-Binding Proteins in Fungi With Canonical Telomere Repeats: New Lessons in the Rapid Evolution of Telomere Proteins.","citation":"Front Genet 2021;12:638790","abstract":"The telomere protein assemblies in different fungal lineages manifest quite profound structural and functional divergence, implying a high degree of flexibility and adaptability. Previous comparative analyses of fungal telomeres have focused on the role of telomere sequence alterations in promoting the evolution of corresponding proteins, particularly in budding and fission yeast. However, emerging evidence suggests that even in fungi with the canonical 6-bp telomere repeat unit, there are significant remodeling of the telomere assembly. Indeed, a new protein family can be recruited to serve dedicated telomere functions, and then experience subsequent loss in sub-branches of the clade. An especially interesting example is the Tay1 family of proteins, which emerged in fungi prior to the divergence of basidiomycetes from ascomycetes. This relatively recent protein family appears to have acquired its telomere DNA-binding activity through the modification of another Myb-containing protein. Members of the Tay1 family evidently underwent rather dramatic functional diversification, serving, e.g., as transcription factors in fission yeast while acting to promote telomere maintenance in basidiomycetes and some hemi-ascomycetes. Remarkably, despite its distinct structural organization and evolutionary origin, a basidiomycete Tay1 appears to promote telomere replication using the same mechanism as mammalian TRF1, i.e., by recruiting and regulating Blm helicase activity. This apparent example of convergent evolution at the molecular level highlight the ability of telomere proteins to acquire new interaction targets. The remarkable evolutionary history of Tay1 illustrates the power of protein modularity and the facile acquisition of nucleic acid/protein-binding activity to promote telomere flexibility.","doi":"10.3389/fgene.2021.638790","authors":"Lue NF","authors_abbrev":"Lue NF","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-03-15","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-03-17 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31048492","title":"Structural basis for eIF2B inhibition in integrated stress response.","citation":"Science 2019 May 03;364(6439):495-499","abstract":"A core event in the integrated stress response, an adaptive pathway common to all eukaryotic cells in response to various stress stimuli, is the phosphorylation of eukaryotic translation initiation factor 2 (eIF2). Normally, unphosphorylated eIF2 transfers the methionylated initiator tRNA to the ribosome in a guanosine 5'-triphosphate-dependent manner. By contrast, phosphorylated eIF2 inhibits its specific guanine nucleotide exchange factor, eIF2B. To elucidate how the eIF2 phosphorylation status regulates the eIF2B activity, we determined cryo-electron microscopic and crystallographic structures of eIF2B in complex with unphosphorylated or phosphorylated eIF2. The unphosphorylated and phosphorylated forms of eIF2 bind to eIF2B in completely different manners: the nucleotide exchange-active and -inactive modes, respectively. These structures explain how phosphorylated eIF2 dominantly inhibits the nucleotide exchange activity of eIF2B.","doi":"10.1126/science.aaw4104","authors":"Kashiwagi K, Yokoyama T, Nishimoto M, Takahashi M, Sakamoto A, Yonemochi M, Shirouzu M, Ito T","authors_abbrev":"Kashiwagi K et al.","pubmed_publication_date":"03 May 2019","pubmed_entrez_date":"2019-05-04","publication_year":"2019","canto_session_key":"f78e319b6068bbc7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-28 19:05:32","canto_approved_date":"2023-03-09 16:06:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-28 19:04:21","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4D7.09","SPAC343.14c","SPAC8C9.15c","SPAC3G9.09c","SPCC11E10.07c","SPAC21E11.06"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2023-02-28","pdb_entries":[{"pdb_id":"6jly","gene_chains":[{"gene_uniquename":"SPAC8C9.15c","chain":"I/J","position":"1-678"},{"gene_uniquename":"SPAC4D7.09","chain":"E/F","position":"1-458"},{"gene_uniquename":"SPAC21E11.06","chain":"G/H","position":"1-467"},{"gene_uniquename":"SPCC11E10.07c","chain":"A/B","position":"1-341"},{"gene_uniquename":"SPAC343.14c","chain":"C/D","position":"1-393"}],"title":"eIF2a - eIF2B complex","entry_authors":"Kashiwagi K,Ito T","entry_authors_abbrev":"Kashiwagi K et al.","reference_uniquename":"PMID:31048492","experimental_method":"X-ray","resolution":"3.5"},{"pdb_id":"6jlz","gene_chains":[{"gene_uniquename":"SPAC8C9.15c","chain":"I/J","position":"1-678"},{"gene_uniquename":"SPAC4D7.09","chain":"E/F","position":"1-458"},{"gene_uniquename":"SPAC21E11.06","chain":"G/H","position":"1-467"},{"gene_uniquename":"SPCC11E10.07c","chain":"A/B","position":"1-341"},{"gene_uniquename":"SPAC343.14c","chain":"C/D","position":"1-393"}],"title":"P-eIF2a - eIF2B complex","entry_authors":"Kashiwagi K,Ito T","entry_authors_abbrev":"Kashiwagi K et al.","reference_uniquename":"PMID:31048492","experimental_method":"X-ray","resolution":"3.35"}]},{"uniquename":"PMID:20603070","title":"Controlling cytokinesis through promiscuous phosphorylation outside BARs.","citation":"Mol Cell 2010 Jul 09;39(1):3-5","abstract":"In this issue of Molecular Cell, Roberts-Galbraith and colleagues report that a key cytokinetic regulator in fission yeast, Cdc15, is phosphorylated on numerous sites that collectively, but not individually, control its oligomerization state and its associations with the plasma membrane and interacting proteins.","doi":"10.1016/j.molcel.2010.06.028","authors":"Glotzer M","authors_abbrev":"Glotzer M","pubmed_publication_date":"09 Jul 2010","pubmed_entrez_date":"2010-07-07","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9651503","title":"Identification of a novel casein kinase-1 homolog in fission yeast Schizosaccharomyces pombe.","citation":"Gene 1998 Jul 03;214(1-2):131-7","abstract":"Fission yeast cells lacking either the ste9+- or rum1+ function cannot enter the cell differentiation pathway upon nutritional starvation. Sterility in both mutants is suppressed by the srs1-S41 mutation. A gene encoding a novel casein kinase-1 (CK1) isoform, cki3+, was isolated as a high-copy-number suppressor gene of the srs1 mutation. Cki3 protein is structurally more related to the Cki/Yck subfamily proteins than those of the Hhp/Hrr25 subfamily. A mutant cki3 gene in which a highly conserved lysine residue in the kinase subdomain II was substituted to arginine lost the ability to recover the growth defect in the srs1 mutant, indicating that catalytic activity was necessary for suppression. Gene disruption revealed that cki3+ was dispensable for cell viability, and cells lacking functional cki3+ exhibited no characteristic phenotype. Thus, S. pombe has three highly related CK1 isoforms (Cki1, Cki2 and Cki3), but none of them has an essential function.","authors":"Kitamura K, Yamashita I","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"03 Jul 1998","pubmed_entrez_date":"1998-07-04","publication_year":"1998","canto_session_key":"9ffcc61dd29b2c64","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-12 21:08:42","canto_approved_date":"2024-03-28 12:59:15","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-06-12 21:53:50","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC144.13c","SPAC1805.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-12"},{"uniquename":"PMID:30640587","title":"How the cell cycle clock ticks.","citation":"Mol Biol Cell 2019 Jan 15;30(2):169-172","abstract":"Eukaryotic cell division has been studied thoroughly and is understood in great mechanistic detail. Paradoxically, however, we lack an understanding of its core control process, in which the master regulator of the cell cycle, cyclin-dependent kinase (CDK), temporally coordinates an array of complex molecular events. The core elements of the CDK control system are conserved in eukaryotic cells, which contain multiple cyclin-CDK forms that have poorly defined and partially overlapping responsibilities in the cell cycle. However, a single CDK can drive all events of cell division in both mammalian and yeast cells, and in fission yeast a single mitotic cyclin can drive the cell cycle without major problems. But how can the same CDK induce different events when activated at different times during the cell cycle? This question, which has bewildered cell cycle researchers for decades, now has a sufficiently clear mechanistic answer. This Perspective aims to provide a synthesis of recent data to facilitate a better understanding of this central cellular control system.","doi":"10.1091/mbc.E18-05-0272","authors":"Örd M, Loog M","authors_abbrev":"Örd M et al.","pubmed_publication_date":"15 Jan 2019","pubmed_entrez_date":"2019-01-15","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-01-16 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9718372","title":"Evidence for a novel MAPKKK-independent pathway controlling the stress activated Sty1/Spc1 MAP kinase in fission yeast.","citation":"J Cell Sci 1998 Sep;111 ( Pt 18):2799-807","abstract":"The fission yeast Sty1/Spc1 MAP kinase, like the mammalian JNK/SAPK and p38/CSBP1 kinases, is activated by a range of environmental insults including osmotic stress, hydrogen peroxide, heat shock, UV light and the protein synthesis inhibitor anisomycin. Sty1 is activated by a single MAPKK, Wis1. We demonstrate that the conserved MAPKKK phosphorylation sites Ser 469 and Thr 473 in the catalytic domain of Wis1 are normally essential for Sty1 activation. However, when mildly overexpressed, a mutant Wis1 kinase lacking these conserved phosphorylation sites is able to support stress inducible gene expression and activation of the Sty1 MAP kinase in response to an oxidative or osmotic stress or to a mild heat shock. We show that phosphorylation and activation of Sty1 under these conditions is not due to inactivation of the Pyp1 MAP kinase phosphatase. These results reveal a novel MAPKKK-independent pathway by which the Wis1 MAPKK can activate the Sty1 MAPK in response to stress in fission yeast.","authors":"Shieh JC, Martin H, Millar JB","authors_abbrev":"Shieh JC et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-08-27","publication_year":"1998","canto_session_key":"3d47d60b7e868097","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 16:38:07","canto_approved_date":"2022-11-21 11:14:19","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-02-28 10:50:45","canto_added_date":"2012-02-24 05:53:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":50,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC215.05","SPAC19D5.01","SPAC24B11.06c","SPAC9G1.02","SPCC757.07c","SPBC409.07c"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2018-10-31"},{"uniquename":"PMID:30266808","title":"Dissection of two parallel pathways for formin-mediated actin filament elongation.","citation":"J Biol Chem 2018 Nov 16;293(46):17917-17928","abstract":"Formins direct the elongation of unbranched actin filaments that are incorporated into a diverse set of cytoskeletal structures. Elongation of formin-bound filaments occurs along two parallel pathways. The formin homology 2 (FH2) pathway allows actin monomers to bind directly to barbed ends bound by dimeric FH2 domains. The formin homology 1 (FH1) pathway involves transfer of profilin-bound actin to the barbed end from polyproline tracts located in the disordered FH1 domains. Here, we used a total internal reflection fluorescence (TIRF) microscopy-based fluorescence approach to determine the fraction of actin subunits incorporated via the FH1 and FH2 pathways during filament elongation mediated by two formins. We found that the fraction of filament elongation that occurs via each pathway directly depends on the efficiency of the other pathway, indicating that these two pathways compete with each other for subunit addition by formins. We conclude that this competition allows formins to compensate for changes in the efficiency of one pathway by adjusting the frequency of subunit addition via the other, thus increasing the overall robustness of formin-mediated actin polymerization.","doi":"10.1074/jbc.RA118.004845","authors":"Sherer LA, Zweifel ME, Courtemanche N","authors_abbrev":"Sherer LA et al.","pubmed_publication_date":"16 Nov 2018","pubmed_entrez_date":"2018-09-30","publication_year":"2018","canto_session_key":"75119561f58ef44c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-04-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F5.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16999687","title":"Identification of a mitochondrial alcohol dehydrogenase in Schizosaccharomyces pombe: new insights into energy metabolism.","citation":"Biochem J 2007 Jan 15;401(2):459-64","abstract":"In the present study we have shown that mitochondria isolated from Schizosaccharomyces pombe exhibit antimycin A-sensitive oxygen uptake activity that is exclusively dependent on ethanol and is inhibited by trifluoroethanol, a potent inhibitor of ADH (alcohol dehydrogenase). Ethanol-dependent respiratory activity has, to our knowledge, not been reported in S. pombe mitochondria to date, which is surprising as it has been concluded previously that only one ADH gene, encoding a cytosolic enzyme, occurs in this yeast. Spectrophotometric enzyme assays reveal that ADH activity in isolated mitochondria is increased approximately 16-fold by Triton X-100, which demonstrates that the enzyme is located in the matrix. Using genetic knockouts, we show conclusively that the novel mitochondrial ADH is encoded by adh4 and, as such, is unrelated to ADH isoenzymes found in mitochondria of other yeasts. By performing a modular-kinetic analysis of mitochondrial electron transfer, we furthermore show how ethanol-dependent respiratory activity (which involves oxidation of matrix-located NADH) compares with that observed when succinate or externally added NADH are used as substrates. This analysis reveals distinct kinetic differences between substrates which fully explain the lack of respiratory control generally observed during ethanol oxidation in yeast mitochondria.","authors":"Crichton PG, Affourtit C, Moore AL","authors_abbrev":"Crichton PG et al.","pubmed_publication_date":"15 Jan 2007","pubmed_entrez_date":"2006-09-27","publication_year":"2007","canto_session_key":"b778909d64b7c7a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-03-01 13:41:38","canto_approved_date":"2025-11-24 13:58:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-01 13:42:05","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5H10.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-03-01"},{"uniquename":"PMID:40849408","title":"A repurposed AMP binding domain reveals mitochondrial protein AMPylation as a regulator of cellular metabolism.","citation":"Nat Commun 2025 Aug 23;16(1):7863","abstract":"Protein AMPylation, the covalent addition of adenosine monophosphate (AMP) to protein substrates, has been known as a post translational modification for over 50 years. Research in this field is largely underdeveloped due to the lack of tools that enable the systematic identification of AMPylated substrates. Here, we address this gap by developing an enrichment technique to isolate and study AMPylated proteins using a nucleotide-binding protein, hinT. Cryo-EM reconstruction of an AMPylated protein bound to hinT provides a structural basis for AMP selectivity. Using structure guided mutagenesis, we optimize enrichment to identify novel substrates of the evolutionarily conserved AMPylase, Selenoprotein O. We show that mammalian Selenoprotein O regulates metabolic flux through AMPylation of key mitochondrial proteins including glutamate dehydrogenase and pyruvate dehydrogenase. Our findings highlight the broader significance of AMPylation, an emerging post translational modification with critical roles in signal transduction and disease pathology. Furthermore, we establish a powerful enrichment platform for the discovery of novel AMPylated proteins to study the mechanisms and significance of protein AMPylation in cellular function.","doi":"10.1038/s41467-025-63014-z","authors":"Gonzalez A, Pon A, Servage K, Pawłowski K, Han Y, Sreelatha A","authors_abbrev":"Gonzalez A et al.","pubmed_publication_date":"23 Aug 2025","pubmed_entrez_date":"2025-08-23","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC30D10.13c","SPCC622.12c","SPAC20G4.05c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:11376151","title":"Comprehensive isolation of meiosis-specific genes identifies novel proteins and unusual non-coding transcripts in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2001 Jun 01;29(11):2327-37","abstract":"In order to isolate meiosis-specific genes in Schizosaccharomyces pombe, we have constructed a subtracted cDNA library enriched in clones whose expression is enhanced during meiosis induced by nitrogen starvation. Using northern blot analysis, we isolated 31 kinds of clones whose expression was induced in a meiosis/sporulation-specific manner. We comprehensively named them meu after meiotic expression upregulated. The transcription of 20 meu genes was found to be dependent on the mei4(+) gene, which encodes a transcription factor required for the progression of meiosis. DNA sequencing indicated that most of the meu genes encode novel proteins. Notably, five of the meu genes harbor no apparent protein coding sequences, and the transcripts form stable hairpin structures, suggesting that they may generate non-coding RNAs or antisense RNAS: The results presented here imply that RNAs are also important for the comprehensive characterization of genomic expression.","authors":"Watanabe T, Miyashita K, Saito TT, Yoneki T, Kakihara Y, Nabeshima K, Kishi YA, Shimoda C, Nojima H","authors_abbrev":"Watanabe T et al.","pubmed_publication_date":"01 Jun 2001","pubmed_entrez_date":"2001-05-29","publication_year":"2001","canto_session_key":"08ef865fc3772098","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-21 08:31:37","canto_approved_date":"2019-11-21 08:31:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-21 08:29:34","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1A6.06c","SPCC1223.12c","SPCPJ732.03","SPNCRNA.928","SPAC1F8.05","SPNCRNA.29","SPBC19F8.06c","SPBC146.11c","SPCC1259.14c","SPCC1281.08","SPBC16A3.13","SPAC1610.03c","SPBC428.07","SPBC14C8.05c","SPCC1235.13","SPCC550.10","SPNCRNA.587","SPBC409.11","SPNCRNA.17","SPBC1347.03","SPNCRNA.07","SPAC1556.06","SPCC613.11c","SPBC27.03","SPAC222.15"],"gene_count":25,"ltp_gene_count":0,"approved_date":"2019-11-21"},{"uniquename":"PMID:35148940","title":"A focus on yeast mating: From pheromone signaling to cell-cell fusion.","citation":"Semin Cell Dev Biol 2023 Jan 15;133:83-95","abstract":"Cells live in a chemical environment and are able to orient towards chemical cues. Unicellular haploid fungal cells communicate by secreting pheromones to reproduce sexually. In the yeast models Saccharomyces cerevisiae and Schizosaccharomyces pombe, pheromonal communication activates similar pathways composed of cognate G-protein-coupled receptors and downstream small GTPase Cdc42 and MAP kinase cascades. Local pheromone release and sensing, at a mobile surface polarity patch, underlie spatial gradient interpretation to form pairs between two cells of distinct mating types. Concentration of secretion at the point of cell-cell contact then leads to local cell wall digestion for cell fusion, forming a diploid zygote that prevents further fusion attempts. A number of asymmetries between mating types may promote efficiency of the system. In this review, we present our current knowledge of pheromone signaling in the two model yeasts, with an emphasis on how cells decode the pheromone signal spatially and ultimately fuse together. Though overall pathway architectures are similar in the two species, their large evolutionary distance allows to explore how conceptually similar solutions to a general biological problem can arise from divergent molecular components.","doi":"10.1016/j.semcdb.2022.02.003","authors":"Sieber B, Coronas-Serna JM, Martin SG","authors_abbrev":"Sieber B et al.","pubmed_publication_date":"15 Jan 2023","pubmed_entrez_date":"2022-02-12","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-02-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPBC21D10.06c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:17036054","title":"Microtubule depolymerization can drive poleward chromosome motion in fission yeast.","citation":"EMBO J 2006 Oct 18;25(20):4888-96","abstract":"Prometaphase kinetochores interact with spindle microtubules (MTs) to establish chromosome bi-orientation. Before becoming bi-oriented, chromosomes frequently exhibit poleward movements (P-movements), which are commonly attributed to minus end-directed, MT-dependent motors. In fission yeast there are three such motors: dynein and two kinesin-14s, Pkl1p and Klp2p. None of these enzymes is essential for viability, and even the triple deletion grows well. This might be due to the fact that yeasts kinetochores are normally juxtapolar at mitosis onset, removing the need for poleward chromosome movement during prometaphase. Anaphase P-movement might also be dispensable in a spindle that elongates significantly. To test this supposition, we have analyzed kinetochore dynamics in cells whose kinetochore-pole connections have been dispersed. In cells recovering from this condition, the maximum rate of poleward kinetochore movement was unaffected by the deletion of any or all of these motors, strongly suggesting that other factors, like MT depolymerization, can cause such movements in vivo. However, Klp2p, which localizes to kinetochores, contributed to the effectiveness of P-movement by promoting the shortening of kinetochore fibers.","authors":"Grishchuk EL, McIntosh JR","authors_abbrev":"Grishchuk EL et al.","pubmed_publication_date":"18 Oct 2006","pubmed_entrez_date":"2006-10-13","publication_year":"2006","canto_session_key":"d8565d86bd6dba28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-07-18 11:10:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-28 09:53:24","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.10","SPAC3A11.14c","SPBC26H8.07c","SPAC1093.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-06-28"},{"uniquename":"PMID:7498541","title":"The osmo-inducible gpd1+ gene is a target of the signaling pathway involving Wis1 MAP-kinase kinase in fission yeast.","citation":"FEBS Lett 1995 Dec 04;376(3):199-201","abstract":"The gpd1+ gene of Schizosaccharomyces pombe encodes an isozyme of NADH-dependent glycerol-3-phosphate dehydrogenases that is involved in glycerol synthesis, whose expression is induced upon an upshift of the medium osmolarity. We provide evidence that this osmotic induction of gpd1+ in S. pombe is under the control of a MAP-signaling pathway involving the wis1+ gene-product, which is a homologue of MAP-kinase kinases. The results suggested that the gpd1+ gene is a downstream target of the osmosensing signaling that is transmitted through Wis1, thereby defects of either of these genes result in the similar phenotype, namely, osmosensitive for growth, because of the failure in accumulation of the intracellular osmoprotectant, glycerol.","authors":"Aiba H, Yamada H, Ohmiya R, Mizuno T","authors_abbrev":"Aiba H et al.","pubmed_publication_date":"04 Dec 1995","pubmed_entrez_date":"1995-12-04","publication_year":"1995","canto_session_key":"f33b93b809413908","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-29 12:55:12","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-25 14:00:30","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPBC215.05","SPAC23D3.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-10-25"},{"uniquename":"PMID:22844101","title":"The ATPase activity of Fml1 is essential for its roles in homologous recombination and DNA repair.","citation":"Nucleic Acids Res 2012 Oct;40(19):9584-95","abstract":"In fission yeast, the DNA helicase Fml1, which is an orthologue of human FANCM, is a key component of the machinery that drives and governs homologous recombination (HR). During the repair of DNA double-strand breaks by HR, it limits the occurrence of potentially deleterious crossover recombinants, whereas at stalled replication forks, it promotes HR to aid their recovery. Here, we have mutated conserved residues in Fml1's Walker A (K99R) and Walker B (D196N) motifs to determine whether its activities are dependent on its ability to hydrolyse ATP. Both Fml1(K99R) and Fml1(D196N) are proficient for DNA binding but totally deficient in DNA unwinding and ATP hydrolysis. In vivo both mutants exhibit a similar reduction in recombination at blocked replication forks as a fml1Δ mutant indicating that Fml1's motor activity, fuelled by ATP hydrolysis, is essential for its pro-recombinogenic role. Intriguingly, both fml1(K99R) and fml1(D196N) mutants exhibit greater sensitivity to genotoxins and higher levels of crossing over during DSB repair than a fml1Δ strain. These data suggest that without its motor activity, the binding of Fml1 to its DNA substrate can impede alternative mechanisms of repair and crossover avoidance.","doi":"10.1093/nar/gks715","authors":"Nandi S, Whitby MC","authors_abbrev":"Nandi S et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-07-31","publication_year":"2012","canto_session_key":"fd90d55a80efff42","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9.05"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:38889682","title":"Mitochondrial biology: Unique membrane remodeling from the matrix.","citation":"Curr Biol 2024 Jun 17;34(12):R581-R583","abstract":"A new study reports the identification of a fission yeast dynamin superfamily protein, Mmc1, that self-assembles on the matrix side of the inner mitochondrial membrane and interacts with subunits of the mitochondrial contact site and cristae organizing system to maintain cristae architecture.","doi":"10.1016/j.cub.2024.05.010","authors":"Mears JA","authors_abbrev":"Mears JA","pubmed_publication_date":"17 Jun 2024","pubmed_entrez_date":"2024-06-18","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-06-19 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19838807","title":"Protein structure calculation with data imputation: the use of substitute restraints.","citation":"J Biomol NMR 2009 Dec;45(4):397-411","abstract":"The amount of experimental restraints e.g., NOEs is often too small for calculating high quality three-dimensional structures by restrained molecular dynamics. Considering this as a typical missing value problem we propose here a model based data imputation technique that should lead to an improved estimation of the correct structure. The novel automated method implemented in AUREMOL makes a more efficient use of the experimental information to obtain NMR structures with higher accuracy. It creates a large set of substitute restraints that are used either alone or together with the experimental restraints. The new approach was successfully tested on three examples: firstly, the Ras-binding domain of Byr2 from Schizosaccharomyces pombe, the mutant HPr (H15A) from Staphylococcus aureus, and a X-ray structure of human ubiquitin. In all three examples, the quality of the resulting final bundles was improved considerably by the use of additional substitute restraints, as assessed quantitatively by the calculation of RMSD values to the \"true\" structure and NMR R-factors directly calculated from the original NOESY spectra or the published diffraction data.","doi":"10.1007/s10858-009-9379-y","authors":"Cano C, Brunner K, Baskaran K, Elsner R, Munte CE, Kalbitzer HR","authors_abbrev":"Cano C et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-10-20","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16799560","title":"Separate RNA-binding surfaces on the multifunctional La protein mediate distinguishable activities in tRNA maturation.","citation":"Nat Struct Mol Biol 2006 Jul;13(7):611-8","abstract":"By sequence-specific binding to 3' UUU-OH, the La protein shields precursor (pre)-RNAs from 3' end digestion and is required to protect defective pre-transfer RNAs from decay. Although La is comprised of a La motif and an RNA-recognition motif (RRM), a recent structure indicates that the RRM beta-sheet surface is not involved in UUU-OH recognition, raising questions as to its function. Progressively defective suppressor tRNAs in Schizosaccharomyces pombe reveal differential sensitivities to La and Rrp6p, a 3' exonuclease component of pre-tRNA decay. 3' end protection is compromised by mutations to the La motif but not the RRM surface. The most defective pre-tRNAs require a second activity of La, in addition to 3' protection, that requires an intact RRM surface. The two activities of La in tRNA maturation map to its two conserved RNA-binding surfaces and suggest a modular model that has implications for its other ligands.","authors":"Huang Y, Bayfield MA, Intine RV, Maraia RJ","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-06-27","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2590529","title":"Acetate assimilation by the fission yeast, Schizosaccharomyces pombe.","citation":"Biochem Cell Biol 1989 Aug;67(8):464-7","abstract":"The fission yeast Schizosaccharomyces pombe utilizes acetate at subinhibitory concentrations in the presence of D-glucose. The nonionized form of acetate is preferentially utilized, oxidized to 14CO2, and assimilated into lipids and proteins. Acetyl CoA synthetase activity greatly increases in the yeast cells grown in media containing acetate. However, glyoxylate cycle enzymes are not detectable in Schizosaccharomyces pombe. [1-14C]Acetate is incorporated into stereols, sterol esters, neutral lipids, and phospholipids. Assimilation of [1-14C]acetate into the peptide structure of proteins was confirmed by a proteolytic digestion experiment.","authors":"Tsai CS, Mitton KP, Johnson BF","authors_abbrev":"Tsai CS et al.","pubmed_publication_date":"Aug 1989","pubmed_entrez_date":"1989-08-01","publication_year":"1989","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR000999","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1539.01c","HGNC:14514"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11710979","title":"Cellular signalling and the complexity of biological timing: insights from the ultradian clock of Schizosaccharomyces pombe.","citation":"Philos Trans R Soc Lond B Biol Sci 2001 Nov 29;356(1415):1725-33","abstract":"The molecular bases of circadian clocks are complex and cannot be sufficiently explained by the relatively simple feedback loops, based on transcription and translation, of current models. The existence of additional oscillators has been demonstrated experimentally, but their mechanism(s) have so far resisted elucidation and any universally conserved clock components have yet to be identified. The fission yeast, Schizosaccharomyces pombe, as a simple and well-characterized eukaryote, is a useful model organism in the investigation of many aspects of cell regulation. In fast-growing cells of the yeast an ultradian clock operates, which can serve as a model system to analyse clock complexity. This clock shares strict period homeostasis and efficient entrainment with circadian clocks but, because of its short period of 30 min, mechanisms other than a transcription/translation-based feedback loop must be working. An initial systematic screen involving over 200 deletion mutants has shown that major cellular signalling pathways (calcium/phosphoinositide, mitogen-activated protein kinase and cAMP/protein kinase A) are crucial for the normal functioning of this ultradian clock. A comparative examination of the role of cellular signalling pathways in the S.pombe ultradian clock and in the circadian timekeeping of different eukaryotes may indicate common principles in biological timing processes that are universally conserved amongst eukaryotes.","authors":"Kippert F","authors_abbrev":"Kippert F","pubmed_publication_date":"29 Nov 2001","pubmed_entrez_date":"2001-11-17","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26752674","title":"Regulation of the antioxidant system in cells of the fission yeast Schizosaccharomyces pombe after combined treatment with patulin and citrinin.","citation":"Toxicon 2016 Mar 01;111:100-7","abstract":"The effects of combined treatment with patulin (PAT) and citrinin (CTN) on Schizosaccharomyces pombe cells were investigated in acute toxicity tests. In comparison with the controls the exposure of fission yeast cells (10(7) cells ml(-1)) to PAT + CTN (250 μM each) for 1 h at a survival rate of 66.6% significantly elevated the concentration of total reactive oxygen species (ROS) via increased levels of peroxides without affecting the concentrations of superoxides or the hydroxyl radical. This treatment induced a 3.08-fold increase in the specific concentration of glutathione and elevated specific activities of catalase and glutathione S-transferase, while at the same time the activity of glutathione reductase decreased. The pattern of the ROS was the same as that induced by CTN (Máté et al., 2014), while the presence of PAT in the PAT + CTN combination treatment modified the activities of the antioxidant system (Papp et al., 2012) in comparison with the individual PAT or CTN treatment, suggesting toxin-specific regulation of glutathione and the enzymes of the antioxidant system and the possibility that the transcription factor (pap1 and atf1) -regulated processes might be influenced directly by ROS.","doi":"10.1016/j.toxicon.2015.12.021","authors":"Papp G, Máté G, Mike N, Gazdag Z, Pesti M","authors_abbrev":"Papp G et al.","pubmed_publication_date":"01 Mar 2016","pubmed_entrez_date":"2016-01-12","publication_year":"2016","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28811350","title":"Defining the DNA Binding Site Recognized by the Fission Yeast Zn 2 Cys 6  Transcription Factor Pho7 and Its Role in Phosphate Homeostasis.","citation":"mBio 2017 Aug 15;8(4)","abstract":"Fission yeast phosphate homeostasis entails transcriptional induction of genes encoding phosphate-mobilizing proteins under conditions of phosphate starvation. Transcription factor Pho7, a member of the Zn 2 Cys 6  family of fungal transcription regulators, is the central player in the starvation response. The DNA binding sites in the promoters of phosphate-responsive genes have not been defined, nor have any structure-function relationships been established for the Pho7 protein. Here we narrow this knowledge gap by (i) delineating an autonomous DNA-binding domain (DBD) within Pho7 that includes the Zn 2 Cys 6  module, (ii) deploying recombinant Pho7 DBD in DNase I footprinting and electrophoretic mobility shift assays (EMSAs) to map the Pho7 recognition sites in the promoters of the phosphate-regulated  pho1  and  tgp1  genes to a 12-nucleotide sequence motif [5'-TCG(G/C)(A/T)xxTTxAA], (iii) independently identifying the same motif as a Pho7 recognition element via  in silico  analysis of available genome-wide ChIP-seq data, (iv) affirming that mutations in the two Pho7 recognition sites in the  pho1  promoter efface  pho1  expression  in vivo , and (v) establishing that the zinc-binding cysteines and a pair of conserved arginines in the DBD are essential for Pho7 activity  in vivo  IMPORTANCE  Fungi respond to phosphate starvation by inducing the transcription of a set of phosphate acquisition genes that comprise a phosphate regulon. Pho7, a member of the Zn 2 Cys 6  family of fungal transcription regulators, is the central player in the phosphate starvation response in fission yeast. The present study identifies a 12-nucleotide Pho7 DNA binding motif [5'-TCG(G/C)(A/T)xxTTxAA] in the promoters of phosphate-regulated genes, pinpoints DNA and protein features important for Pho7 binding to DNA, and correlates them with Pho7-dependent gene expression  in vivo  The results highlight distinctive properties of Pho7 vis-a-vis other fungal zinc binuclear cluster transcription factors as well as the divergent cast of transcription factors deployed for phosphate homeostasis in fission yeast versus budding yeast.","doi":"10.1128/mBio.01218-17","authors":"Schwer B, Sanchez AM, Garg A, Chatterjee D, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"15 Aug 2017","pubmed_entrez_date":"2017-08-17","publication_year":"2017","canto_session_key":"163961d04bcaf919","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Angad Garg","canto_first_approved_date":"2018-09-07 09:02:45","canto_approved_date":"2023-02-21 12:05:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-09-06 15:03:25","canto_added_date":"2017-08-17 00:15:13","annotation_curators":[{"name":"Angad Garg","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPBC1271.09","SPBC27B12.11c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2018-09-07"},{"uniquename":"PMID:25721271","title":"Fungal genome sequencing: basic biology to biotechnology.","citation":"Crit Rev Biotechnol 2016 Aug;36(4):743-59","abstract":"The genome sequences provide a first glimpse into the genomic basis of the biological diversity of filamentous fungi and yeast. The genome sequence of the budding yeast, Saccharomyces cerevisiae, with a small genome size, unicellular growth, and rich history of genetic and molecular analyses was a milestone of early genomics in the 1990s. The subsequent completion of fission yeast, Schizosaccharomyces pombe and genetic model, Neurospora crassa initiated a revolution in the genomics of the fungal kingdom. In due course of time, a substantial number of fungal genomes have been sequenced and publicly released, representing the widest sampling of genomes from any eukaryotic kingdom. An ambitious genome-sequencing program provides a wealth of data on metabolic diversity within the fungal kingdom, thereby enhancing research into medical science, agriculture science, ecology, bioremediation, bioenergy, and the biotechnology industry. Fungal genomics have higher potential to positively affect human health, environmental health, and the planet's stored energy. With a significant increase in sequenced fungal genomes, the known diversity of genes encoding organic acids, antibiotics, enzymes, and their pathways has increased exponentially. Currently, over a hundred fungal genome sequences are publicly available; however, no inclusive review has been published. This review is an initiative to address the significance of the fungal genome-sequencing program and provides the road map for basic and applied research.","doi":"10.3109/07388551.2015.1015959","authors":"Sharma KK","authors_abbrev":"Sharma KK","pubmed_publication_date":"Aug 2016","pubmed_entrez_date":"2015-02-28","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-03-01 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7961734","title":"Low molecular weight protein-tyrosine phosphatases are highly conserved between fission yeast and man.","citation":"J Biol Chem 1994 Nov 11;269(45):27996-9","abstract":"Cdc25 protein phosphatase dephosphorylates tyrosine 15 of Cdc2, thereby activating Cdc2/cyclin B kinase, which then brings about mitosis. A fission yeast (Schizosaccharomyces pombe) cDNA expression library was screened for clones that rescue cdc25-22. In addition to the cdc25+ and pyp3+ protein-tyrosine phosphatase genes, a third gene was discovered. This gene, named stp1+ (small tyrosine phosphatase), encodes a approximately 17.5-kDa protein that is approximately 42% identical to members of an unusual class of small (approximately 18 kDa) cytosolic phosphatases previously known to exist only in mammalian species. The biological functions of these proteins are unknown, but they have vigorous protein-tyrosine phosphatase activity in vitro and have a sequence motif, Cys-X5-Arg, that is present at the active sites of all known types of protein-tyrosine phosphatases. Sequence homology between S. pombe Stp1 and its mammalian homologs is particularly high in the active site region of the proteins. Rescue of cdc25-22 by overproduction of Stp1 protein is probably due to an ability of Stp1 to dephosphorylate tyrosine 15 of Cdc2. Disruption of stp1+ causes no obvious phenotype. The fact that Stp1 homologs are highly conserved between yeast and man suggests that they have important functions.","authors":"Mondesert O, Moreno S, Russell P","authors_abbrev":"Mondesert O et al.","pubmed_publication_date":"11 Nov 1994","pubmed_entrez_date":"1994-11-11","publication_year":"1994","canto_session_key":"6a184a91912e9122","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-01-23 17:49:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-24 16:26:23","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.09","SPAC1071.12c","SPAC24H6.05"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-10-24"},{"uniquename":"PMID:20816984","title":"A structural hinge in eukaryotic MutY homologues mediates catalytic activity and Rad9-Rad1-Hus1 checkpoint complex interactions.","citation":"J Mol Biol 2010 Oct 29;403(3):351-70","abstract":"The DNA glycosylase MutY homologue (MYH or MUTYH) removes adenines misincorporated opposite 8-oxoguanine as part of the base excision repair pathway. Importantly, defects in human MYH (hMYH) activity cause the inherited colorectal cancer syndrome MYH-associated polyposis. A key feature of MYH activity is its coordination with cell cycle checkpoint via interaction with the Rad9-Rad1-Hus1 (9-1-1) complex. The 9-1-1 complex facilitates cell cycle checkpoint activity and coordinates this activity with ongoing DNA repair. The interdomain connector (IDC, residues 295-350) between the catalytic domain and the 8-oxoguanine recognition domain of hMYH is a critical element that maintains interactions with the 9-1-1 complex. We report the first crystal structure of a eukaryotic MutY protein, a fragment of hMYH (residues 65-350) that consists of the catalytic domain and the IDC. Our structure reveals that the IDC adopts a stabilized conformation projecting away from the catalytic domain to form a docking scaffold for 9-1-1. We further examined the role of the IDC using Schizosaccharomyces pombe MYH as model system. In vitro studies of S. pombe MYH identified residues I261 and E262 of the IDC (equivalent to V315 and E316 of the hMYH IDC) as critical for maintaining the MYH/9-1-1 interaction. We determined that the eukaryotic IDC is also required for DNA damage selection and robust enzymatic activity. Our studies also provide the first evidence that disruption of the MYH/9-1-1 interaction diminishes the repair of oxidative DNA damage in vivo. Thus, preserving the MYH/9-1-1 interaction contributes significantly to minimizing the mutagenic potential of oxidative DNA damage.","doi":"10.1016/j.jmb.2010.08.045","authors":"Luncsford PJ, Chang DY, Shi G, Bernstein J, Madabushi A, Patterson DN, Lu AL, Toth EA","authors_abbrev":"Luncsford PJ et al.","pubmed_publication_date":"29 Oct 2010","pubmed_entrez_date":"2010-09-07","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G4.04c","SPAC26A3.02","SPAC1952.07"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:36123402","title":"The inner nuclear membrane protein Lem2 coordinates RNA degradation at the nuclear periphery.","citation":"Nat Struct Mol Biol 2022 Sep;29(9):910-921","abstract":"Transcriptionally silent chromatin often localizes to the nuclear periphery. However, whether the nuclear envelope (NE) is a site for post-transcriptional gene repression is not well understood. Here we demonstrate that Schizosaccharomyces pombe Lem2, an NE protein, regulates nuclear-exosome-mediated RNA degradation. Lem2 deletion causes accumulation of RNA precursors and meiotic transcripts and de-localization of an engineered exosome substrate from the nuclear periphery. Lem2 does not directly bind RNA but instead interacts with the exosome-targeting MTREC complex and its human homolog PAXT to promote RNA recruitment. This pathway acts largely independently of nuclear bodies where exosome factors assemble. Nutrient availability modulates Lem2 regulation of meiotic transcripts, implying that this pathway is environmentally responsive. Our work reveals that multiple spatially distinct degradation pathways exist. Among these, Lem2 coordinates RNA surveillance of meiotic transcripts and non-coding RNAs by recruiting exosome co-factors to the nuclear periphery.","doi":"10.1038/s41594-022-00831-6","authors":"Martín Caballero L, Capella M, Barrales RR, Dobrev N, van Emden T, Hirano Y, Suma Sreechakram VN, Fischer-Burkart S, Kinugasa Y, Nevers A, Rougemaille M, Sinning I, Fischer T, Hiraoka Y, Braun S","authors_abbrev":"Martín Caballero L et al.","pubmed_publication_date":"Sep 2022","pubmed_entrez_date":"2022-09-19","publication_year":"2022","canto_session_key":"63ff789b6ebec1cb","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-22 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3241625","title":"Observations on integrative transformation in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1988 Dec;215(1):87-93","abstract":"Three different Schizosaccharomyces pombe strains have been transformed with a circular or linearized non-ars plasmid carrying the ura4+ gene as a selectable marker. The first strain shows full homology between the genomic ura4-294 gene (point mutation) and the marker gene on the plasmid. The second strain carries a 600 bp deletion (ura4-D6) that decreases homology between plasmid and chromosome. No homology remains in the third strain which has a complete deletion of the ura4 gene on the chromosome (ura4-D18). When sequence homology exists between transforming DNA and the chromosomal ura4 region, gene conversion is strongly preferred over integration of the circular plasmid. Reduction of the length of homology leads to a decrease of transformation frequencies, and homology dependent as well as a minority of homology independent integrations are observed. In the complete absence of homology two rare types of transformants are encountered: either the circular plasmid replicates autonomously, although it is devoid of an ars sequence, or alternatively the plasmid integrates into the genome at various positions. Transformation with plasmid cut within the coding region of ura4 can lead to tandemly arranged multiple integrations, when no homology exists between the free ends and the chromosome. The integrations occur at the ura4 locus, when homology is retained between plasmid and chromosome, and at various sites in the genome of the strain with a complete deletion of the ura4 gene. The results suggest that homology dependent events (conversion, integration) are strongly preferred in transformation of S. pombe with non-ars plasmids. In addition low frequency integration by illegitimate recombination is observed.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Grimm C, Kohli J","authors_abbrev":"Grimm C et al.","pubmed_publication_date":"Dec 1988","pubmed_entrez_date":"1988-12-01","publication_year":"1988","canto_session_key":"d976e4a7ff421b27","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-07-07 16:21:20","canto_approved_date":"2024-07-15 11:54:27","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-07-07 16:21:12","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-07-07"},{"uniquename":"PMID:3448096","title":"Schizosaccharomyces pombe mutants affected in their division response to starvation.","citation":"J Cell Sci 1987 Oct;88 ( Pt 3):295-304","abstract":"Schizosaccharomyces pombe mutants have been selected on the basis of an altered response to nutritional stimulation of cell division (changed division response, cdr). Two new loci (cdr1 and cdr2) were identified and characterized. When suspended in nitrogen-free medium wild-type cells underwent stimulated rates of division and became reduced to approximately 30% in protein content with a concomitant 3.6-fold increase in cell number after 24 h starvation. cdr cells had significantly smaller increases in cell number. The ratio of starved/unstarved protein content was higher for the cdr strains than for the wild type. cdr cells were also affected in their response to nitrogen-source shifts from proline to glutamate (or vice versa) or when shifted from serine phosphate to inorganic phosphate, showing that the alteration in division response was not restricted to nitrogen metabolism. Upon nitrogen starvation wild-type cells arrested prior to the cdc10 execution point, whereas cdr cells arrested later in the cell cycle. cdc25-22 cdr1 or cdr2 double mutants grew very slowly and were extremely elongated at all temperatures; the restrictive temperature was reduced to 27 degrees C. wee1 was epistatic to cdr mutations with respect to cell length at the cell plate stage. cdr+ genes are postulated to play a role in the nutritional modulation of the mitotic size control.","authors":"Young PG, Fantes PA","authors_abbrev":"Young PG et al.","pubmed_publication_date":"Oct 1987","pubmed_entrez_date":"1987-10-01","publication_year":"1987","canto_session_key":"b5e73159bb3ebdf8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-04-29 20:34:47","canto_approved_date":"2025-09-03 10:24:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-18 15:58:39","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPCC18B5.03","SPBC336.12c","SPBC11B10.09","SPAC644.06c","SPAC24H6.05"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-04-29"},{"uniquename":"PMID:24354645","title":"Cell polarization in budding and fission yeasts.","citation":"FEMS Microbiol Rev 2014 Mar;38(2):228-53","abstract":"Polarization is a fundamental cellular property, which is essential for the function of numerous cell types. Over the past three to four decades, research using the best-established yeast systems in cell biological research, Saccharomyces cerevisiae (or budding yeast) and Schizosaccharomyces pombe (or fission yeast), has brought to light fundamental principles governing the establishment and maintenance of a polarized, asymmetric state. These two organisms, though both ascomycetes, are evolutionarily very distant and exhibit distinct shapes and modes of growth. In this review, we compare and contrast the two systems. We first highlight common cell polarization pathways, detailing the contribution of Rho GTPases, the cytoskeleton, membrane trafficking, lipids, and protein scaffolds. We then contrast the major differences between the two organisms, describing their distinct strategies in growth site selection and growth zone dimensions and compartmentalization, which may be the basis for their distinct shapes.","doi":"10.1111/1574-6976.12055","authors":"Martin SG, Arkowitz RA","authors_abbrev":"Martin SG et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2013-12-21","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15887295","title":"SAC-ing mitotic errors: how the spindle assembly checkpoint (SAC) plays defense against chromosome mis-segregation.","citation":"Cell Motil Cytoskeleton 2005 Jul;61(3):145-60","abstract":"","authors":"Kadura S, Sazer S","authors_abbrev":"Kadura S et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-05-12","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29996109","title":"Quantitative Phosphoproteomics Reveals the Signaling Dynamics of Cell-Cycle Kinases in the Fission Yeast Schizosaccharomyces pombe.","citation":"Cell Rep 2018 Jul 10;24(2):503-514","abstract":"Multiple protein kinases regulate cell-cycle progression, of which the cyclin-dependent kinases (CDKs) are thought to act as upstream master regulators. We have used quantitative phosphoproteomics to analyze the fission yeast cell cycle at sufficiently high temporal resolution to distinguish fine-grain differences in substrate phosphorylation dynamics on a proteome-wide scale. This dataset provides a useful resource for investigating the regulatory dynamics of cell-cycle kinases and their substrates. For example, our analysis indicates that the substrates of different mitotic kinases (CDK, NIMA-related, Polo-like, and Aurora) are phosphorylated in sequential, kinase-specific waves during mitosis. Phosphoproteomics analysis after chemical-genetic manipulation of CDK activity suggests that the timing of these waves is established by the differential dependency of the downstream kinases on upstream CDK. We have also examined the temporal organization of phosphorylation during G1/S, as well as the coordination between the NDR-related kinase Orb6, which controls polarized growth, and other cell-cycle kinases.","doi":"10.1016/j.celrep.2018.06.036","authors":"Swaffer MP, Jones AW, Flynn HR, Snijders AP, Nurse P","authors_abbrev":"Swaffer MP et al.","pubmed_publication_date":"10 Jul 2018","pubmed_entrez_date":"2018-07-12","publication_year":"2018","canto_session_key":"23e4a902cf4e6605","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-07-17 16:20:50","canto_approved_date":"2018-07-17 16:20:50","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-07-17 16:20:26","canto_added_date":"2018-07-13 00:15:06","annotation_curators":[],"file_curator_name":"Matthew Swaffer","file_curator_role":"community","annotation_file_curators":[{"name":"Matthew 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of the requirement for cdc16p GAP function in Schizosaccharomyces pombe by mutation of the septation initiation network genes.","citation":"Arch Microbiol 2001 Jan;175(1):62-9","abstract":"The onset of septum formation in the fission yeast Schizosaccharomyces pombe is signaled via the spglp GTPase-switch, which is part of the septation initiation network. This is negatively regulated by the two-component GTPase-activating protein (GAP) comprised of the products of the cdc16 and byr4 genes. Loss-of-function mutations in either of these genes result in multiple rounds of septum formation without cell cleavage. In this work, we demonstrate that attenuation of the protein kinase cdc7p can rescue the lethality of a null allele of cdc16. This observation provides the basis for selection of chromosomal mutations and multicopy suppressors that attenuate the signaling of septation. Using this screen, mutations in all the previously described septation initiation network genes were obtained, with the exception of byr4, sid4 and plo1. We also demonstrate that increased expression of the dma1 gene can rescue the lethality of a null allele of cdc16. The implications for the regulation of septum formation in fission yeast are discussed.","authors":"Fournier N, Cerutti L, Beltraminelli N, Salimova E, Simanis V","authors_abbrev":"Fournier N et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-03-29","publication_year":"2001","canto_session_key":"5309bbb3babb1fef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-17 16:26:25","canto_approved_date":"2024-05-17 16:26:25","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-05-17 16:26:17","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":14,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPAC9G1.09","SPBC428.13c","SPAC222.10c","SPAC6F6.08c","SPAC24B11.11c","SPBC21.06c","SPAC17G8.10c","SPBC24C6.07","SPAC1565.06c","SPCC1739.11c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2024-05-17"},{"uniquename":"PMID:26581324","title":"Cleavage and polyadenylation factor, Rna14 is an essential protein required for the maintenance of genomic integrity in fission yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2016 Feb;1863(2):189-97","abstract":"Faithful segregation of chromosomes is essential for the maintenance of genome integrity. In a genetic screen to identify genes related to checkpoint function, we have characterized the role of rna14, an essential gene in the maintenance of chromosome dynamics. We demonstrate that Rna14 localizes in the nucleus and in the absence of functional Rna14, the cells exhibit chromosomal segregation defects. The mutant allele of rna14 exhibits genetic interaction with key kinetochore components and spindle checkpoint proteins. Inactivation of rna14 leads to accumulation of Bub1-GFP foci, a protein required for spindle checkpoint activation that could be due to the defects in the attachment of mitotic spindle to the chromosome. Consistently, the double mutant of rna14-11 and bub1 knockout exhibits high degree of chromosome mis-segregation. At restrictive condition, the rna14-11 mutant cells exhibit defects in cell cycle progression with high level of septation. The orthologs of Rna14 in Saccharomyces cerevisiae (sc Rna14) and human (CstF3) contain similar domain architecture and are required for 3'-end processing of pre-mRNA. We have also demonstrated that the fission yeast Rna14 is required to prevent transcriptional read-through. These findings reveal the importance of transcription termination in the maintenance of genomic stability through the regulation of kinetochore function.","doi":"10.1016/j.bbamcr.2015.11.007","authors":"Sonkar A, Yadav S, Ahmed S","authors_abbrev":"Sonkar A et al.","pubmed_publication_date":"Feb 2016","pubmed_entrez_date":"2015-11-20","publication_year":"2016","canto_session_key":"63b67c3174262a0a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shakil Ahmed","canto_first_approved_date":"2015-12-16 16:16:11","canto_approved_date":"2023-06-08 09:12:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-04 05:17:16","canto_added_date":"2015-11-21 01:19:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Shakil Ahmed","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.04c","SPAC6F12.17","SPBC20F10.06","SPCC1322.12c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-12-16"},{"uniquename":"PMID:24563858","title":"Thiol-based H2O2 signalling in microbial systems.","citation":"Redox Biol 2014;2:395-9","abstract":"Cysteine residues, and in particular their thiolate groups, react not only with reactive oxygen species but also with electrophiles and with reactive nitrogen species. Thus, cysteine oxidation has often been linked to the toxic effects of some of these reactive molecules. However, thiol-based switches are common in protein sensors of antioxidant cascades, in both prokaryotic and eukaryotic organisms. We will describe here three redox sensors, the transcription factors OxyR, Yap1 and Pap1, which respond by disulfide bond formation to hydrogen peroxide stress, focusing specially on the differences among the three peroxide-sensing mechanisms.","doi":"10.1016/j.redox.2014.01.015","authors":"Boronat S, Domènech A, Paulo E, Calvo IA, García-Santamarina S, García P, Encinar Del Dedo J, Barcons A, Serrano E, Carmona M, Hidalgo E","authors_abbrev":"Boronat S et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-25","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25778913","title":"A nucleosome turnover map reveals that the stability of histone H4 Lys20 methylation depends on histone recycling in transcribed chromatin.","citation":"Genome Res 2015 Jun;25(6):872-83","abstract":"Nucleosome composition actively contributes to chromatin structure and accessibility. Cells have developed mechanisms to remove or recycle histones, generating a landscape of differentially aged nucleosomes. This study aimed to create a high-resolution, genome-wide map of nucleosome turnover in Schizosaccharomyces pombe. The recombination-induced tag exchange (RITE) method was used to study replication-independent nucleosome turnover through the appearance of new histone H3 and the disappearance or preservation of old histone H3. The genome-wide location of histones was determined by chromatin immunoprecipitation-exonuclease methodology (ChIP-exo). The findings were compared with diverse chromatin marks, including histone variant H2A.Z, post-translational histone modifications, and Pol II binding. Finally, genome-wide mapping of the methylation states of H4K20 was performed to determine the relationship between methylation (mono, di, and tri) of this residue and nucleosome turnover. Our analysis showed that histone recycling resulted in low nucleosome turnover in the coding regions of active genes, stably expressed at intermediate levels. High levels of transcription resulted in the incorporation of new histones primarily at the end of transcribed units. H4K20 was methylated in low-turnover nucleosomes in euchromatic regions, notably in the coding regions of long genes that were expressed at low levels. This transcription-dependent accumulation of histone methylation was dependent on the histone chaperone complex FACT. Our data showed that nucleosome turnover is highly dynamic in the genome and that several mechanisms are at play to either maintain or suppress stability. In particular, we found that FACT-associated transcription conserves histones by recycling them and is required for progressive H4K20 methylation.","doi":"10.1101/gr.188870.114","authors":"Svensson JP, Shukla M, Menendez-Benito V, Norman-Axelsson U, Audergon P, Sinha I, Tanny JC, Allshire RC, Ekwall K","authors_abbrev":"Svensson JP et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-03-18","publication_year":"2015","canto_session_key":"e16fd94fffcf9fdc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-19 01:15:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12531016","title":"Structural and functional conservation of error-free DNA postreplication repair in Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2002 Nov 03;1(11):869-80","abstract":"DNA postreplication repair (PRR) is a cellular process by which cells survive replication-blocking lesions without removing the lesion. In the budding yeast Saccharomyces cerevisiae, MMS2 plays a key role in the error-free PRR pathway: the mms2 null mutant displays an increased spontaneous mutation rate and sensitivity to a variety of DNA damaging agents. In contrast, its human homologs appear to play a different role. In order to address whether the MMS2-mediated PRR pathway is conserved in eukaryotes, we isolated a Schizosaccharomyces pombe cDNA homologous to MMS2, which we named spm2(+). Using spm2(+) as a bait in a yeast two-hybrid screen, we identified a fission yeast cDNA homologous to UBC13 from various species and named it spu13(+). Two-hybrid analysis confirmed physical interaction between Spm2 and Spu13, and between Spm2 and budding yeast Ubc13. Genetic analysis shows that both spm2(+) and spu13(+) are able to functionally complement the corresponding budding yeast mutants. Furthermore, deletion of either spm2(+), spu13(+) or both genes from fission yeast results in an increased sensitivity to DNA damaging agents, suggesting that spm2(+) and spu13(+) indeed function in PRR. The fact that the spm2(-) spu13(-) double mutant showed sensitivity similar to that of the single mutant indicates that these two gene products act at the same step. Hence, our data strongly support the hypothesis that the PRR function mediated by UBC13-MMS2 is conserved throughout eukaryotes.","authors":"Brown M, Zhu Y, Hemmingsen SM, Xiao W","authors_abbrev":"Brown M et al.","pubmed_publication_date":"03 Nov 2002","pubmed_entrez_date":"2003-01-18","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11E3.04c","SPCC338.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8862002","title":"Production of cadmium sulphide microcrystallites in batch cultivation by Schizosaccharomyces pombe.","citation":"J Biotechnol 1996 Jul 31;48(3):259-67","abstract":"Cadmium sulphate was added to separate batch cultures of Schizosaccharomyces pombe during different growth phases to determine the effect on cadmium sulphide microcrystallite production. Exit gas analysis was used to determine the impact on metabolism. Addition during the early-exponential growth phase resulted in an immediate intracellular uptake of cadmium, followed by rapid efflux from the cells, permanent reduction in cell metabolism and a lower intracellular inorganic sulphide content. This response was not suitable for cadmium sulphide microcrystallite production. Stationary phase cultures did not induce cadmium sulphide microcrystallite production. However, the addition of cadmium sulphate to a culture during the mid-exponential growth phase increased the intracellular cadmium and inorganic sulphide concentrations for approximately 8 h before reaching a saturation level for the cell. This resulted in a significant level of cadmium sulphide microcrystallite production.","authors":"Williams P, Keshavarz-Moore E, Dunnill P","authors_abbrev":"Williams P et al.","pubmed_publication_date":"31 Jul 1996","pubmed_entrez_date":"1996-07-31","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27736907","title":"Scarless Gene Tagging with One-Step Transformation and Two-Step Selection in Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"PLoS One 2016;11(10):e0163950","abstract":"Gene tagging with fluorescent proteins is commonly applied to investigate the localization and dynamics of proteins in their cellular environment. Ideally, a fluorescent tag is genetically inserted at the endogenous locus at the N- or C- terminus of the gene of interest without disrupting regulatory sequences including the 5' and 3' untranslated region (UTR) and without introducing any extraneous unwanted \"scar\" sequences, which may create unpredictable transcriptional or translational effects. We present a reliable, low-cost, and highly efficient method for the construction of such scarless C-terminal and N-terminal fusions with fluorescent proteins in yeast. The method relies on sequential positive and negative selection and uses an integration cassette with long flanking regions, which is assembled by two-step PCR, to increase the homologous recombination frequency. The method also enables scarless tagging of essential genes with no need for a complementing plasmid. To further ease high-throughput strain construction, we have computationally automated design of the primers, applied the primer design code to all open reading frames (ORFs) of the budding yeast Saccharomyces cerevisiae (S. cerevisiae) and the fission yeast Schizosaccharomyces pombe (S. pombe), and provide here the computed sequences. To illustrate the scarless N- and C-terminal gene tagging methods in S. cerevisiae, we tagged various genes including the E3 ubiquitin ligase RSP5, the proteasome subunit PRE1, and the eleven Rab GTPases with yeast codon-optimized mNeonGreen or mCherry; several of these represent essential genes. We also implemented the scarless C-terminal gene tagging method in the distantly related organism S. pombe using kanMX6 and HSV1tk as positive and negative selection markers, respectively, as well as ura4. The scarless gene tagging methods presented here are widely applicable to visualize and investigate the functional roles of proteins in living cells.","doi":"10.1371/journal.pone.0163950","authors":"Landgraf D, Huh D, Hallacli E, Lindquist S","authors_abbrev":"Landgraf D et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-10-14","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-10-15 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000109","title":"Gene Ontology annotation based on curation of genome-wide subcellular localisation of proteins using fluorescent protein tagging in Trypanosoma brucei","abstract":"Trypanosomes are exquisitely structured cells in which protein localisation can be extremely informative for likely function. TrypTag is a project using expression of N- and C-terminal mNeonGreen fusion proteins from the endogenous loci to determine the subcellular localisation of every gene in the Trypanosoma brucei genome. GO Cellular Component terms are manually assigned by curators studying fluorescence microscope images of the resulting cells labelled with mNeonGreen fusion proteins. As trypanosomes are a pathogenic basal eukaryote, this will indicate likely function of both highly conserved eukaryote genes and parasite-specific genes. Resource URL: http://www.tryptag.org Protein subcellular localisation images can be viewed on the Tryptag website, e.g. http://www.tryptag.org?id=Tb927.8.1550","authors":"TrypTag","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25447915","title":"A methods review on use of nonsense suppression to study 3' end formation and other aspects of tRNA biogenesis.","citation":"Gene 2015 Feb 01;556(1):35-50","abstract":"Suppressor tRNAs bear anticodon mutations that allow them to decode premature stop codons in metabolic marker gene mRNAs, that can be used as in vivo reporters of functional tRNA biogenesis. Here, we review key components of a suppressor tRNA system specific to Schizosaccharomyces pombe and its adaptations for use to study specific steps in tRNA biogenesis. Eukaryotic tRNA biogenesis begins with transcription initiation by RNA polymerase (pol) III. The nascent pre-tRNAs must undergo folding, 5' and 3' processing to remove the leader and trailer, nuclear export, and splicing if applicable, while multiple complex chemical modifications occur throughout the process. We review evidence that precursor-tRNA processing begins with transcription termination at the oligo(T) terminator element, which forms a 3' oligo(U) tract on the nascent RNA, a sequence-specific binding site for the RNA chaperone, La protein. The processing pathway bifurcates depending on a poorly understood property of pol III termination that determines the 3' oligo(U) length and therefore the affinity for La. We thus review the pol III termination process and the factors involved including advances using gene-specific random mutagenesis by dNTP analogs that identify key residues important for transcription termination in certain pol III subunits. The review ends with a 'technical approaches' section that includes a parts lists of suppressor-tRNA alleles, strains and plasmids, and graphic examples of its diverse uses.","doi":"10.1016/j.gene.2014.11.034","authors":"Rijal K, Maraia RJ, Arimbasseri AG","authors_abbrev":"Rijal K et al.","pubmed_publication_date":"01 Feb 2015","pubmed_entrez_date":"2014-12-03","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-12-04 01:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4G9.08c","SPAC22A12.05","SPCC330.13","SPCC18.07"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"EMBL:AU009952","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32264036","title":"New visible light excitable donor-acceptor 7-hydroxy-coumarins as blue fluorescent probes for selective staining of vacuoles in yeasts and L. donovani.","citation":"J Mater Chem B 2017 Apr 14;5(14):2580-2587","abstract":"In order to address the existing limitations of the commercially available fluorescent probe CMAC (7-amino-4-chloromethylcoumarin), a new series of highly fluorescent donor-acceptor 7-hydroxy-coumarin derivatives was prepared and these derivatives were used as vacuole specific fluorescent probes for live cell imaging of unicellular parasitic protozoa L. donovani promastigotes and yeast cells S. pombe and S. cerevisiae. The synthesized 7-hydroxy-coumarins exhibited interesting photophysical properties and have advantages such as excitation in the visible region, good water solubility, photo-stability, good quantum yield and low cytotoxicity.","doi":"10.1039/c6tb03257e","authors":"Raghuvanshi A, Kumar Jha A, Kathuria M, Priya Awasthi B, Purohit D, Mitra K, Goel A","authors_abbrev":"Raghuvanshi A et al.","pubmed_publication_date":"14 Apr 2017","pubmed_entrez_date":"2020-04-09","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-04-11 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12235386","title":"Topoisomerase III is required for accurate DNA replication and chromosome segregation in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2002 Sep 15;30(18):4022-31","abstract":"The deletion of the top3(+) gene leads to defective nuclear division and lethality in Schizosaccharo myces pombe. This lethality is suppressed by concomitant loss of rqh1(+), the RecQ helicase. Despite extensive investigation, topoisomerase III function and its relationship with RecQ helicase remain poorly understood. We generated top3 temperature-sensitive (top3-ts) mutants and found these to be defective in nuclear division and cytokinesis and to be sensitive to DNA-damaging agents. A temperature shift of top3-ts cells to 37 degrees C, or treatment with hydroxyurea at the permissive temperature, caused an increase in 'cut' (cell untimely torn) cells and elevated rates of minichromosome loss. The viability of top3-ts cells was decreased by a temperature shift during S-phase when compared with a similar treatment in other cell cycle stages. Furthermore, the top3-ts mutant was not sensitive to M-phase specific drugs. These results indicate that topoisomerase III may play an important role in DNA metabolism during DNA replication to ensure proper chromosome segregation. Our data are consistent with Top3 acting downstream of Rqh1 to process the toxic DNA structure produced by Rqh1.","authors":"Oh M, Choi IS, Park SD","authors_abbrev":"Oh M et al.","pubmed_publication_date":"15 Sep 2002","pubmed_entrez_date":"2002-09-18","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPBC16G5.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:17189249","title":"Tel2 is required for activation of the Mrc1-mediated replication checkpoint.","citation":"J Biol Chem 2007 Feb 23;282(8):5346-55","abstract":"Proteins belonging to the Tel2/Rad-5/Clk-2 family are conserved among eukaryotes and are involved in various cellular processes, such as cell proliferation, telomere maintenance, the biological clock, and the DNA damage checkpoint. However, the molecular mechanisms underlying the functions of these molecules remain largely unclear. Here we report that in the fission yeast, Schizosaccharomyces pombe, Tel2 is required for efficient phosphorylation of Mrc1, a mediator of DNA replication checkpoint signaling, and for activation of Cds1, a replication checkpoint kinase, when DNA replication is blocked by hydroxyurea. In fact, Tel2 is required for survival of replication fork arrest and for the replication checkpoint in cells lacking Chk1, another checkpoint kinase the role of which overlaps that of Cds1 in cell cycle arrest by replication block. In addition, Tel2 plays important roles in entry into S phase and in genome stability. Tel2 is essential for vegetative cell growth, and the tel2Delta strain accumulated cells with 1C DNA content after germination. In the absence of hydroxyurea, Tel2 is vital in the mutant lacking Swi1, a component of the replication fork protection complex, and multiple Rad22 DNA repair foci were frequently observed in Tel2-repressed swi1Delta cells especially at S phase. In contrast, the cds1Deltaswi1Delta mutant did not show such lethality. These results indicate that S. pombe Tel2 plays important roles in the Mrc1-mediated replication checkpoint as well as in the Cds1-independent regulation of genome integrity.","authors":"Shikata M, Ishikawa F, Kanoh J","authors_abbrev":"Shikata M et al.","pubmed_publication_date":"23 Feb 2007","pubmed_entrez_date":"2006-12-26","publication_year":"2007","canto_session_key":"6d2d5b10bcbc0a55","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-01-14 16:20:22","canto_approved_date":"2023-09-06 06:17:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-09 08:15:43","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC458.03","SPCC18B5.03","SPAC694.06c","SPBC216.06c","SPCC18B5.11c","SPBC216.05"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2014-01-14"},{"uniquename":"PMID:16371130","title":"Loss of RanGEF/Pim1 activity abolishes the orchestration of Ran-mediated mitotic cellular events in S. pombe.","citation":"Genes Cells 2006 Jan;11(1):29-46","abstract":"RCC1, a conserved chromosomal protein with a seven-bladed propeller is a GDP/GTP nucleotide exchange factor for RanGTPase that mediates various cellular events. We isolated 16 temperature-sensitive (ts) mutants of S. pombeRCC1-homolog, pim1+, by error-prone PCR. Five pim1(ts) mutants had a single mutation. The obtained pim1(ts) mutations and previously reported mutations were localized on similar sites in seven RCC1 repeats. Those mutations resulted in a reduced binding of Pim1 with Spi1. All pim1(ts) mutants showed a defect in nucleocytoplasmic protein transports, whereas the majority of them showed a normal mRNA export. In all pim1(ts) examined, chromosomal DNA replication was completed. However, mitotic spindle formation was abrogated, the septum was formed being uncoupled with nuclear division and abnormally widened, thus resulting in chromosomal DNA mis-segregation and the accumulation of enucleated cells. As a result, a defect of RanGEF/Pim1 abolished the orchestration of sequential mitotic events, spindle formation, septation and cytokinesis that are essential to produce two identical daughter cells.","authors":"Hirose E, Mukai M, Shimada A, Nishitani H, Shibata Y, Nishimoto T","authors_abbrev":"Hirose E et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2005-12-24","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC557.03c","SPBC1289.03c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7476862","title":"Functional analysis of the Drosophila CDC2 Dm gene in fission yeast.","citation":"Mol Gen Genet 1995 Sep 20;248(5):621-8","abstract":"The cdc2+ gene product (p34cdc2) is a protein kinase that regulates entry into mitosis in all eukaryotic cells. The role that p34cdc2 plays in the cell cycle has been extensively investigated in a number of organisms, including the fission yeast Schizosaccharomyces pombe. To study the degree of functional conservation among evolutionarily distant p34cdc2 proteins, we have constructed a S. pombe strain in which the yeast cdc2+ gene has been replaced by its Drosophila homologue CDC2Dm (the CDC2Dm strain). This CDC2Dm S. pombe strain is viable, capable of mating and producing four viable meiotic products, indicating that the fly p34CDC2Dm recognizes all the essential S. pombe cdc2+ substrates, and that it is recognized by cyclin partners and other elements required for its activity. The p34CDC2Dm protein yields a lethal phenotype in combination with the mutant B-type cyclin p56cdc13-117, suggesting that this S. pombe cyclin might interact less efficiently with the Drosophila protein than with its native p34cdc2 counterpart. This CDC2Dm strain also responds to nutritional starvation and to incomplete DNA synthesis, indicating that proteins involved in these signal transduction pathways, interact properly with p34CDC2Dm (and/or that p34cdc2-independent pathways are used). The CDC2Dm gene produces a 'wee' phenotype, and it is largely insensitive to the action of the S. pombe wee1+ mitotic inhibitor, suggesting that Drosophila wee1+ homologue might not be functionally conserved. This CDC2Dm strain is hypersensitive to UV irradiation, to the same degree as wee1-deficient mutants. A strain which co-expresses the Drosophila and yeast cdc2+ genes shows a dominant wee phenotype, but displays a wild-type sensitivity to UV irradiation, suggesting that p34cdc2 triggers mitosis and influences the UV sensitivity by independent mechanisms.","authors":"Bejarano ER, Muñoz MJ, Jimenez J","authors_abbrev":"Bejarano ER et al.","pubmed_publication_date":"20 Sep 1995","pubmed_entrez_date":"1995-09-20","publication_year":"1995","canto_session_key":"3c298b57414bd6a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 14:04:44","canto_session_submitted_date":"2012-03-03 14:04:27","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:23980472","title":"[Heterochromatin assembly and RNA silencing].","citation":"Seikagaku 2013 Jul;85(7):565-70","abstract":"","authors":"Nakayama J","authors_abbrev":"Nakayama J","pubmed_publication_date":"Jul 2013","pubmed_entrez_date":"2013-08-29","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-11-01 02:19:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9506280","title":"Fatty acid profiling: a feasible typing system to trace yeast contamination in wine bottling plants.","citation":"Int J Food Microbiol 1997 Sep 16;38(2-3):143-55","abstract":"The long-chain fatty acid composition of yeast strains was determined for several species associated with the wine industry. The Saccharomyces cerevisiae, Zygosaccharomyces bailii, Saccharomycodes ludwigii, Schizosaccharomyces pombe, Brettanomyces/Dekkera spp., Pichia anomala, Pichia membranaefaciens and Lodderomyces elongisporus species presented distinct fatty acid profiles after multivariate statistical analysis. The Zygosaccharomyces rouxii species showed profiles similar to Zygosaccharomyces bailii. The use of fatty acid profiling in wine bottling plants and wines makes it possible to trace the origin of the strains responsible for spoiling the final product. In one case the origin was found at the outlet of the finishing filter and identified as Zygosaccharomyces bailii. In the other case the source of contamination was discovered in the heads of the filling machine and assigned to the Pichia membranaefaciens species. The results point out the discriminating power and the industrial applicability of the technique described in this work to analyse yeast long-chain fatty acid compositions.","authors":"Malfeito-Ferreira M, Tareco M, Loureiro V","authors_abbrev":"Malfeito-Ferreira M et al.","pubmed_publication_date":"16 Sep 1997","pubmed_entrez_date":"1998-03-20","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8390662","title":"Functional interchangeability of the structurally similar tetranucleotide loops GAAA and UUCG in fission yeast signal recognition particle RNA.","citation":"Proc Natl Acad Sci U S A 1993 Jun 15;90(12):5409-13","abstract":"Signal recognition particle (SRP) RNA exhibits significant primary sequence conservation only in domain IV, a bulged hairpin capped by a GNRA (N, any nucleotide; R, purine) tetranucleotide loop except in plant homologs. Tetraloops conforming to this sequence or to the consensus UNCG enhance the stability of synthetic RNA hairpins and have strikingly similar three-dimensional structures. To determine the biological relevance of this similarity, as well as to assess the relative contributions of sequence and structure to the function of the domain IV tetraloop, we replaced the GAAA sequence in fission yeast SRP RNA with UUCG. Haploid strains harboring this substitution are viable, providing experimental evidence for the functional equivalence of the two tetraloops. We next tested the two sequences found in plant SRP RNAs at this location for function in the context of the Schizosaccharomyces pombe RNA. While substitution of CUUC does not allow growth, a viable strain results from replacing GAAA with UUUC. Although the viable tetraloop substitution mutants exhibit wild-type growth under normal conditions, all three express conditional defects. To determine whether this might be a consequence of structural perturbations, we performed enzymatic probing. The results indicate that RNAs containing tetraloop substitutions exhibit subtle differences from the wild type not only in the tetraloop itself, but also in the 3-base pair adjoining stem. To directly assess the importance of the latter structure, we disrupted it partially or completely and made the compensatory mutations to restore the helix. Surprisingly, mutant RNAs with as little as one Watson-Crick base pair can support growth.","authors":"Selinger D, Liao X, Wise JA","authors_abbrev":"Selinger D et al.","pubmed_publication_date":"15 Jun 1993","pubmed_entrez_date":"1993-06-15","publication_year":"1993","canto_session_key":"29adab3910cf5781","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2016-06-16 13:25:35","canto_approved_date":"2023-07-31 08:50:59","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-06-10 14:05:10","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":41,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_8390662_phaf.tsv"}],"genes":["SPNCRNA.98"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-06-16"},{"uniquename":"PMID:15331764","title":"Nse1, Nse2, and a novel subunit of the Smc5-Smc6 complex, Nse3, play a crucial role in meiosis.","citation":"Mol Biol Cell 2004 Nov;15(11):4866-76","abstract":"The structural maintenance of chromosomes (SMC) family of proteins play key roles in the organization, packaging, and repair of chromosomes. Cohesin (Smc1+3) holds replicated sister chromatids together until mitosis, condensin (Smc2+4) acts in chromosome condensation, and Smc5+6 performs currently enigmatic roles in DNA repair and chromatin structure. The SMC heterodimers must associate with non-SMC subunits to perform their functions. Using both biochemical and genetic methods, we have isolated a novel subunit of the Smc5+6 complex, Nse3. Nse3 is an essential nuclear protein that is required for normal mitotic chromosome segregation and cellular resistance to a number of genotoxic agents. Epistasis with Rhp51 (Rad51) suggests that like Smc5+6, Nse3 functions in the homologous recombination based repair of DNA damage. We previously identified two non-SMC subunits of Smc5+6 called Nse1 and Nse2. Analysis of nse1-1, nse2-1, and nse3-1 mutants demonstrates that they are crucial for meiosis. The Nse1 mutant displays meiotic DNA segregation and homologous recombination defects. Spore viability is reduced by nse2-1 and nse3-1, without affecting interhomolog recombination. Finally, genetic interactions shared by the nse mutants suggest that the Smc5+6 complex is important for replication fork stability.","authors":"Pebernard S, McDonald WH, Pavlova Y, Yates JR, Boddy MN","authors_abbrev":"Pebernard S et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-08-28","publication_year":"2004","canto_session_key":"675da45d71de6897","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-03-23 16:26:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-26 15:19:41","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14F5.04c","SPBC685.06","SPCC5E4.06","SPBC582.05c","SPCC1827.05c","SPAC644.14c","SPAC17A5.11","SPAC6G10.07","SPAC16A10.06c","SPAC14C4.02c","SPBC20F10.04c","SPCC645.04","SPBC651.10","SPCC550.05"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2014-11-26"},{"uniquename":"PMID:9296386","title":"Evidence for cell cycle-specific, spindle pole body-mediated, nuclear positioning in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1997 Aug;110 ( Pt 16):1851-66","abstract":"Specific changes in spatial order occur during cell cycle progression in fission yeast. Growth of the rod-shaped cells is highly regulated and undergoes a cell cycle and size-regulated switch from monopolar to bipolar tip extension. During both phases of growth, the interphase nucleus is maintained in a central location. Following the separation of the genome to the cell tips in mitosis, the two nuclei migrate back towards the cell equator before stopping in two new positions that will become the middle of the two new cells. Here we use simultaneous labeling of microtubules, chromatin and spindle pole bodies in wild-type and cdc mutants, to show that nuclear positioning is achieved by regulation of spindle pole body-mediated nuclear migration. We show that the number and location of nuclear positioning signals is regulated in a cell cycle-specific manner and that spindle pole body-mediated forces are likely to be responsible for maintaining correct nuclear position once the nuclei have reached the appropriate position in the cell. Accentuating the movement of the nuclei back towards the cell equator after mitosis by artificially increasing cell length shows that the spindle pole body leads the nucleus during this migration. When multiple spindle pole bodies are associated with the same or different nuclei they all go to the same point indicating that the different spindle pole bodies are responding to the same positional cue. In a septation-defective mutant cell, which contains four nuclei, the spindle pole bodies on the four different nuclei initially group as two pairs in regions that would become the middle of the new cells, were the cell able to divide. In the subsequent interphase, the nuclei aggregate as a group of four in the centre of the cell. The presence of two or three clusters of spindle pole bodies in larger cells with eight nuclei suggests that the mechanisms specifying the normally central location for multiple nuclei may be unable to operate properly as the cells get larger. Perturbation of microtubules with the microtubule poison thiabendazole prevents the spindle pole body clustering in septation mutants, demonstrating that nuclear positioning requires a functional microtubule cytoskeleton.","authors":"Hagan I, Yanagida M","authors_abbrev":"Hagan I et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26892493","title":"Identification of novel secreted fatty acids that regulate nitrogen catabolite repression in fission yeast.","citation":"Sci Rep 2016 Feb 19;6:20856","abstract":"Uptake of poor nitrogen sources such as branched-chain amino acids is repressed in the presence of high-quality nitrogen sources such as NH4(+) and glutamate (Glu), which is called nitrogen catabolite repression. Amino acid auxotrophic mutants of the fission yeast Schizosaccharomyces pombe were unable to grow on minimal medium containing NH4Cl or Glu even when adequate amounts of required amino acids were supplied. However, growth of these mutant cells was recovered in the vicinity of colonies of the prototrophic strain, suggesting that the prototrophic cells secrete some substances that can restore uptake of amino acids by an unknown mechanism. We identified the novel fatty acids, 10(R)-acetoxy-8(Z)-octadecenoic acid and 10(R)-hydroxy-8(Z)-octadecenoic acid, as secreted active substances, referred to as Nitrogen Signaling Factors (NSFs). Synthetic NSFs were also able to shift nitrogen source utilization from high-quality to poor nitrogen sources to allow adaptive growth of the fission yeast amino acid auxotrophic mutants in the presence of high-quality nitrogen sources. Finally, we demonstrated that the Agp3 amino acid transporter was involved in the adaptive growth. The data highlight a novel intra-species communication system for adaptation to environmental nutritional conditions in fission yeast.","doi":"10.1038/srep20856","authors":"Sun X, Hirai G, Ueki M, Hirota H, Wang Q, Hongo Y, Nakamura T, Hitora Y, Takahashi H, Sodeoka M, Osada H, Hamamoto M, Yoshida M, Yashiroda Y","authors_abbrev":"Sun X et al.","pubmed_publication_date":"19 Feb 2016","pubmed_entrez_date":"2016-02-20","publication_year":"2016","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-21 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9628926","title":"Genetic characterisation of hda1+, a putative fission yeast histone deacetylase gene.","citation":"Nucleic Acids Res 1998 Jul 01;26(13):3247-54","abstract":"hda1+ (histone deacetylase 1) is a fission yeast gene which is highly similar in sequence to known histone deacetylase genes in humans and budding yeast. We have investigated if this putative histone deacetylase contributes to transcriptional silencing in the fission yeast Schizosaccharomyces pombe. A precise deletion allele of the hda1+ open reading frame was created. Cells lacking the hda1+ gene are viable. However, genetic analysis reveals that cells without hda1 + display enhanced gene repression/silencing of marker genes, residing adjacent to telomeres, close to the silent mating-type loci and within centromere I. This phenotype is very similar to that recently reported for rpd3 mutants both in Drosophila and budding yeast. No defects in chromosome segregation or changes in telomere length were detected. Cells lacking the hda1+ gene display reduced sporulation. Growth of hda1 cells is partially inhibited by low concentrations of Trichostatin A (TSA), a known inhibitor of histone deacetylase enzymes. TSA treatment is also able to overcome the enhanced silencing found in heterochromatic regions of hda1 cells. These results indicate a genetic redundancy with respect to deacetylase genes and partially overlapping functions of these in fission yeast. The significance of these results is discussed in the light of recent discoveries from other eukaryotes.","authors":"Olsson TG, Ekwall K, Allshire RC, Sunnerhagen P, Partridge JF, Richardson WA","authors_abbrev":"Olsson TG et al.","pubmed_publication_date":"01 Jul 1998","pubmed_entrez_date":"1998-06-17","publication_year":"1998","canto_session_key":"c061236e9784a19a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-09 12:11:44","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-09 12:11:35","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-09"},{"uniquename":"PMID:18257391","title":"Mouse and human La proteins differ in kinase substrate activity and activation mechanism for tRNA processing.","citation":"Gene Expr 2007;14(2):71-81","abstract":"The La protein interacts with a variety of small RNAs as well as certain growth-associated mRNAs such as Mdm2 mRNA. Human La (hLa) phosphoprotein is so highly conserved that it can replace the tRNA processing function of the fission yeast La protein in vivo. We used this system, which is based on tRNA-mediated suppression (TMS) of ade6-704 in S. pombe, to compare the activities of mouse and human La proteins. Prior studies indicate that hLa is activated by phosphorylation of serine-366 by protein kinase CK2, neutralizing a negative effect of a short basic motif (SBM). First, we report the sequence mapping of the UGA stop codon that requires suppressor tRNA for TMS, to an unexpected site in S. pombe ade6-704. Next, we show that, unlike hLa, native mLa is unexpectedly inactive for TMS, although its intrinsic activity is revealed by deletion of its SBM. We then show that mLa is not phosphorylated by CK2, accounting for the mechanistic difference between mLa and hLa. We found a PKA/PKG target sequence in mLa (S199) that is not present in hLa, and show that PKA/PKG efficiently phosphorylates mLa S199 in vitro. A noteworthy conclusion that comes from this work is that this fission yeast system can be used to gain insight into differences in control mechanisms used by La proteins of different mammalian species. Finally, RNA binding assays indicate that while mutation of mLa S199 has little effect on pre-tRNA binding, it substantially decreases binding to a probe derived from Mdm2 mRNA. In closing, we note that species-specific signaling through La may be relevant to the La-dependent Mdm2 pathways of p53 metabolism and cancer progression in mice and humans.","authors":"Park JM, Intine RV, Maraia RJ","authors_abbrev":"Park JM et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2008-02-09","publication_year":"2007","canto_session_key":"6d8e5bb149dd8a29","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-21 09:00:02","canto_approved_date":"2021-06-30 16:15:06","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-03-21 08:59:55","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.10c","SPCC1322.13"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-03-21"},{"uniquename":"PMID:39736178","title":"Optimization of the quality of sea buckthorn juice by enzymatic digestion and inoculation sequence.","citation":"Food Chem 2024 Dec 24;470:142623","abstract":"Sea buckthorn, rich in nutrients and bioactive compounds such as phenolics, fatty acids, and vitamins, presents processing challenges due to its intense sourness and bland flavor. This study addresses key challenges in flavor enhancement and sourness reduction by evaluating the effects of pectinase treatment and inoculation sequences on the overall quality. Optimal malic acid degradation and antioxidant occurred when Schizosaccharomyces pombe (S. pombe) was inoculated after pectinase digestion of the pulp, while sequential inoculation with Saccharomyces cerevisiae and S. pombe produced the most favorable flavor profile. S. pombe effectively promoted the degradation of malic and quinic acids during fermentation, improving color, antioxidant activity, and flavor characteristics. These findings highlight the critical role of pectinase digestion and inoculation sequence, offering practical guidance for optimizing large-scale fermentation processes and strain selection to develop innovative sea buckthorn beverages and enhance their market potential.","doi":"10.1016/j.foodchem.2024.142623","authors":"Wang J, Zhang Y, Zhang B, Han Y, Li J, Zhang B, Jiang Y","authors_abbrev":"Wang J et al.","pubmed_publication_date":"24 Dec 2024","pubmed_entrez_date":"2024-12-30","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2025-01-01 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40247490","title":"From noisy cell size control to population growth: When variability can be beneficial.","citation":"Phys Rev E 2025 Mar;111(3-1):034407","abstract":"Single-cell experiments revealed substantial variability in generation times, growth rates, but also in birth and division sizes between genetically identical cells. Understanding how these fluctuations determine the fitness of the population, i.e., its growth rate, is necessary in any quantitative theory of evolution. Here, we develop a biologically relevant model which accounts for the stochasticity in single-cell growth rates, birth sizes, and division sizes. We derive expressions for the population growth rate and mean birth size in the population in terms of single-cell fluctuations. Allowing division sizes to fluctuate reveals how the mechanism of cell size control (timer, sizer, and adder) influences population growth. Surprisingly, we find that fluctuations in single-cell growth rates can be beneficial for population growth when slow-growing cells tend to divide at smaller sizes than fast-growing cells. Our framework is not limited to exponentially growing cells like Escherichia coli, and we derive similar expressions for cells with linear and bilinear growth laws, such as Mycobacterium tuberculosis and fission yeast Schizosaccharomyces pombe, respectively.","doi":"10.1103/PhysRevE.111.034407","authors":"Genthon A","authors_abbrev":"Genthon A","pubmed_publication_date":"Mar 2025","pubmed_entrez_date":"2025-04-18","publication_year":"2025","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2025-04-18 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"TreeFam:TF105639","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YLR045C","SPCC895.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25332400","title":"N-terminal phosphorylation of HP1α increases its nucleosome-binding specificity.","citation":"Nucleic Acids Res 2014 Nov 10;42(20):12498-511","abstract":"Heterochromatin protein 1 (HP1) is an evolutionarily conserved chromosomal protein that binds to lysine 9-methylated histone H3 (H3K9me), a hallmark of heterochromatin. Although HP1 phosphorylation has been described in several organisms, the biological implications of this modification remain largely elusive. Here we show that HP1's phosphorylation has a critical effect on its nucleosome binding properties. By in vitro phosphorylation assays and conventional chromatography, we demonstrated that casein kinase II (CK2) is the kinase primarily responsible for phosphorylating the N-terminus of human HP1α. Pull-down assays using in vitro-reconstituted nucleosomes showed that unmodified HP1α bound H3K9-methylated and H3K9-unmethylated nucleosomes with comparable affinity, whereas CK2-phosphorylated HP1α showed a high specificity for H3K9me3-modified nucleosomes. Electrophoretic mobility shift assays showed that CK2-mediated phosphorylation diminished HP1α's intrinsic DNA binding, which contributed to its H3K9me-independent nucleosome binding. CK2-mediated phosphorylation had a similar effect on the nucleosome-binding specificity of fly HP1a and S. pombe Swi6. These results suggested that HP1 phosphorylation has an evolutionarily conserved role in HP1's recognition of H3K9me-marked nucleosomes.","doi":"10.1093/nar/gku995","authors":"Nishibuchi G, Machida S, Osakabe A, Murakoshi H, Hiragami-Hamada K, Nakagawa R, Fischle W, Nishimura Y, Kurumizaka H, Tagami H, Nakayama J","authors_abbrev":"Nishibuchi G et al.","pubmed_publication_date":"10 Nov 2014","pubmed_entrez_date":"2014-10-22","publication_year":"2014","canto_session_key":"34f90a1facdd9e18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-11-18 12:14:40","canto_approved_date":"2024-05-07 16:43:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-07 16:30:05","canto_added_date":"2014-10-23 00:15:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPAC23C11.11"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-11-18"},{"uniquename":"PMID:12361567","title":"cis-acting DNA from fission yeast centromeres mediates histone H3 methylation and recruitment of silencing factors and cohesin to an ectopic site.","citation":"Curr Biol 2002 Oct 01;12(19):1652-60","abstract":"Metazoan centromeres are generally composed of large repetitive DNA structures packaged in heterochromatin. Similarly, fission yeast centromeres contain large inverted repeats and two distinct silenced domains that are both required for centromere function. The central domain is flanked by outer repetitive elements coated in histone H3 methylated on lysine 9 and bound by conserved heterochromatin proteins. This centromeric heterochromatin is required for cohesion between sister centromeres. Defective heterochromatin causes premature sister chromatid separation and chromosome missegregation. The role of cis-acting DNA sequences in the formation of centromeric heterochromatin has not been established.\nA deletion strategy was used to identify centromeric sequences that allow heterochromatin formation in fission yeast. Fragments from the outer repeats are sufficient to cause silencing of an adjacent gene when inserted at a euchromatic chromosomal locus. This silencing is accompanied by the local de novo methylation of histone H3 on lysine 9, recruitment of known heterochromatin components, Swi6 and Chp1, and the provision of a new strong cohesin binding site. In addition, we demonstrate that the chromodomain of Chp1 binds to MeK9-H3 and that Chp1 itself is required for methylation of histone H3 on lysine 9.\nA short sequence, reiterated at fission yeast centromeres, can direct silent chromatin assembly and cohesin recruitment in a dominant manner. The heterochromatin formed at the euchromatic locus is indistinguishable from that found at endogenous centromeres. Recruitment of Rad21-cohesin underscores the link between heterochromatin and chromatid cohesion and indicates that these centromeric elements act independently of kinetochore activity to recruit cohesin.","authors":"Partridge JF, Scott KS, Bannister AJ, Kouzarides T, Allshire RC","authors_abbrev":"Partridge JF et al.","pubmed_publication_date":"01 Oct 2002","pubmed_entrez_date":"2002-10-04","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12072458","title":"Expression-state boundaries in the mating-type region of fission yeast.","citation":"Genetics 2002 Jun;161(2):611-22","abstract":"A transcriptionally silent chromosomal domain is found in the mating-type region of fission yeast. Here we show that this domain is delimited by 2-kb inverted repeats, IR-L and IR-R. IR-L and IR-R prevent the expansion of transcription-permissive chromatin into the silenced region and that of silenced chromatin into the expressed region. Their insulator activity is partially orientation dependent. The silencing defects that follow deletion or inversion of IR-R are suppressed by high dosage of the chromodomain protein Swi6. Combining chromosomal deletions and Swi6 overexpression shows that IR-L and IR-R provide firm borders in a region where competition between silencing and transcriptional competence occurs. IR-R possesses autonomously replicating sequence (ARS) activity, leading to a model where replication factors, or replication itself, participate in boundary formation.","authors":"Thon G, Bjerling P, Bünner CM, Verhein-Hansen J","authors_abbrev":"Thon G et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-06-20","publication_year":"2002","canto_session_key":"31759412a215c82a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-07-11 15:19:02","canto_approved_date":"2024-07-11 15:19:02","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-11 15:18:55","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2024-07-11"},{"uniquename":"PMID:19714219","title":"Fission yeast Tel1(ATM) and Rad3(ATR) promote telomere protection and telomerase recruitment.","citation":"PLoS Genet 2009 Aug;5(8):e1000622","abstract":"The checkpoint kinases ATM and ATR are redundantly required for maintenance of stable telomeres in diverse organisms, including budding and fission yeasts, Arabidopsis, Drosophila, and mammals. However, the molecular basis for telomere instability in cells lacking ATM and ATR has not yet been elucidated fully in organisms that utilize both the telomere protection complex shelterin and telomerase to maintain telomeres, such as fission yeast and humans. Here, we demonstrate by quantitative chromatin immunoprecipitation (ChIP) assays that simultaneous loss of Tel1(ATM) and Rad3(ATR) kinases leads to a defect in recruitment of telomerase to telomeres, reduced binding of the shelterin complex subunits Ccq1 and Tpz1, and increased binding of RPA and homologous recombination repair factors to telomeres. Moreover, we show that interaction between Tpz1-Ccq1 and telomerase, thought to be important for telomerase recruitment to telomeres, is disrupted in tel1Delta rad3Delta cells. Thus, Tel1(ATM) and Rad3(ATR) are redundantly required for both protection of telomeres against recombination and promotion of telomerase recruitment. Based on our current findings, we propose the existence of a regulatory loop between Tel1(ATM)/Rad3(ATR) kinases and Tpz1-Ccq1 to ensure proper protection and maintenance of telomeres in fission yeast.","doi":"10.1371/journal.pgen.1000622","authors":"Moser BA, Subramanian L, Khair L, Chang YT, Nakamura TM","authors_abbrev":"Moser BA et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-08-29","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06","SPCC23B6.03c","SPCC188.07","SPBC216.05"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:6587363","title":"Genes required for initiation and resolution steps of mating-type switching in fission yeast.","citation":"Proc Natl Acad Sci U S A 1984 Jun;81(11):3481-5","abstract":"The fission yeast Schizosaccharomyces pombe switches mating type by transposition of a copy of DNA derived from either of the two storage cassettes, mat2 -P and mat3 -M, into the expression locus, mat1 . The recombinational event of switching is initiated by a double-stranded DNA break present in approximately 20% of the molecules at mat1 . Fifty-three mutants defective in switching of mating type have been isolated previously, and each has been assigned to 1 of 10 linkage groups. One group consists of cis-acting mutations at mat1 , which reduce the amount of the DNA double-strand cut. The remaining nine groups are mutations in genes that are unlinked to the mating-type locus and are studied here. Three ( swi1 , -3, -7) are required for formation of the double-strand cut, whereas the others are not. Mutants of three genes ( swi4 , -8, -9) undergo high-frequency rearrangement of the mating-type locus indicative of errors of resolution of recombinational intermediates. The remaining three ( swi2 , -5, -6) have normal levels of cut, do not make errors of resolution, and possibly are required either for efficient utilization of the cut or determining the directionality of switching. The data suggest that the switching process can be dissected into genetically distinguishable steps.","authors":"Egel R, Beach DH, Klar AJ","authors_abbrev":"Egel R et al.","pubmed_publication_date":"Jun 1984","pubmed_entrez_date":"1984-06-01","publication_year":"1984","canto_session_key":"57b18143cd825c2e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-02 15:34:06","canto_approved_date":"2022-12-12 17:23:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-08 14:50:04","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.01","SPBC216.06c","SPAC664.01c","SPBC409.03","SPAC1142.03c","SPAC8F11.03","SPBC30D10.04","SPBC19G7.01c","SPAC3H5.06c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2018-03-02"},{"uniquename":"PMID:39855709","title":"[A flavin-containing monooxygenase from  Schizosaccharomyces pombe : characterization and application in the synthesis of  S -methyl-L-cysteine sulfoxide].","citation":"Sheng Wu Gong Cheng Xue Bao 2025 Jan 25;41(1):474-485","abstract":" S -methyl-L-cysteine sulfoxide (SMCO) is a non-protein sulfur-containing amino acid with a variety of functions. There are few reports on the enzymes catalyzing the biosynthesis of SMCO from  S -methyl-L-cysteine (SMC). In this study, the flavin-containing monooxygenase gene derived from  Schizosaccharomyces pombe  ( spfmo ) was heterologously expressed in  Escherichia coli  BL21(DE3) and the enzymatic properties of the expressed protein were analyzed. The optimum catalytic conditions of the recombinant SpFMO were 30 ℃ and pH 8.0, under which the enzyme activity reached 72.77 U/g. An appropriate amount of Mg 2+  improved the enzyme activity. The enzyme kinetic analysis showed that the  K  m  and  k  cat / K  m  of SpFMO on the substrate SMC were 23.89 μmol/L and 61.71 L/(min·mmol), respectively. Under the optimal reaction conditions, the yield of SMCO synthesized from SMC catalyzed by SpFMO was 12.31% within 9 h. This study provides reference for the enzymatic synthesis of SMCO.","doi":"10.13345/j.cjb.240324","authors":"Lian M, Song Z, Gao W, Zhu G, Dong M, Li Y, Liu Y, Wang F, Lu F","authors_abbrev":"Lian M et al.","pubmed_publication_date":"25 Jan 2025","pubmed_entrez_date":"2025-01-24","publication_year":"2025","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2025-01-26 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23825576","title":"Biochemical characterization of Paracoccidioides brasiliensis α-1,3-glucanase Agn1p, and its functionality by heterologous Expression in Schizosaccharomyces pombe.","citation":"PLoS One 2013;8(6):e66853","abstract":"α-1,3-Glucan is present as the outermost layer of the cell wall in the pathogenic yeastlike (Y) form of Paracoccidioides brasiliensis. Based on experimental evidence, this polysaccharide has been proposed as a fungal virulence factor. To degrade α-1,3-glucan and allow remodeling of the cell wall, α-1,3-glucanase is required. Therefore, the study of this enzyme, its encoding gene, and regulatory mechanisms, might be of interest to understand the morphogenesis and virulence process in this fungus. A single gene, orthologous to other fungal α-1,3-glucanase genes, was identified in the Paracoccidioides genome, and labeled AGN1. Transcriptional levels of AGN1 and AGS1 (α-1,3-glucan synthase-encoding gene) increased sharply when the pathogenic Y phase was cultured in the presence of 5% horse serum, a reported booster for cell wall α-1,3-glucan synthesis in this fungus. To study the biochemical properties of P. brasiliensis Agn1p, the enzyme was heterologously overexpressed, purified, and its activity profile determined by means of the degradation of carboxymethyl α-1,3-glucan (SCMG, chemically modified from P. brasiliensis α-1,3-glucan), used as a soluble substrate for the enzymatic reaction. Inhibition assays, thin layer chromatography and enzymatic reactions with alternative substrates (dextran, starch, chitin, laminarin and cellulose), showed that Agn1p displays an endolytic cut pattern and high specificity for SCMG. Complementation of a Schizosaccharomyces pombe agn1Δ strain with the P. brasiliensis AGN1 gene restored the wild type phenotype, indicating functionality of the gene, suggesting a possible role of Agn1p in the remodeling of P. brasiliensis Y phase cell wall. Based on amino acid sequence, P. brasiliensis Agn1p, groups within the family 71 of fungal glycoside hydrolases (GH-71), showing similar biochemical characteristics to other members of this family. Also based on amino acid sequence alignments, we propose a subdivision of fungal GH-71 into at least five groups, for which specific conserved sequences can be identified.","doi":"10.1371/journal.pone.0066853","authors":"Villalobos-Duno H, San-Blas G, Paulinkevicius M, Sánchez-Martín Y, Nino-Vega G","authors_abbrev":"Villalobos-Duno H et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-05","publication_year":"2013","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27272176","title":"Multiplexing Genetic and Nucleosome Positioning Codes: A Computational Approach.","citation":"PLoS One 2016;11(6):e0156905","abstract":"Eukaryotic DNA is strongly bent inside fundamental packaging units: the nucleosomes. It is known that their positions are strongly influenced by the mechanical properties of the underlying DNA sequence. Here we discuss the possibility that these mechanical properties and the concomitant nucleosome positions are not just a side product of the given DNA sequence, e.g. that of the genes, but that a mechanical evolution of DNA molecules might have taken place. We first demonstrate the possibility of multiplexing classical and mechanical genetic information using a computational nucleosome model. In a second step we give evidence for genome-wide multiplexing in Saccharomyces cerevisiae and Schizosacharomyces pombe. This suggests that the exact positions of nucleosomes play crucial roles in chromatin function.","doi":"10.1371/journal.pone.0156905","authors":"Eslami-Mossallam B, Schram RD, Tompitak M, van Noort J, Schiessel H","authors_abbrev":"Eslami-Mossallam B et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-06-09","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-06-10 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23456650","title":"Protective roles of methionine-R-sulfoxide reductase against stresses in Schizosaccharomyces pombe.","citation":"J Basic Microbiol 2014 Jan;54(1):72-80","abstract":"The Schizosaccharomyces pombe msrB(+) gene encoding methionine-R-sulfoxide reductase (MsrB) was cloned into the shuttle vector pRS316 to generate the recombinant plasmid pFMetSO. The msrB(+) mRNA level was significantly increased in the S. pombe cells harboring pFMetSO, indicating that the cloned msrB(+) gene is functioning. In the presence of 0.1 mM L-methionine-(R,S)-sulfoxide, the S. pombe cells harboring pFMetSO could grow normally but the growth of the vector control cells was almost arrested. The S. pombe cells harboring pFMetSO exhibited the enhanced growth on the minimal medium plates with stress-inducing agents, such as hydrogen peroxide, superoxide radical-generating menadione (MD), nitric oxide (NO)-generating sodium nitroprusside (SNP), and cadmium (Cd), when compared with the vector control cells. They also gave rise to the enhanced growth at the high incubation temperature of 37 °C than the vector control cells. The S. pombe cells harboring pFMetSO contained lower reactive oxygen species (ROS) and higher total glutathione (GSH) levels than the vector control cells. In brief, the S. pombe MsrB plays a protective role against oxidative, nitrosative, and thermal stresses, and is involved in diminishing intracellular ROS level.","doi":"10.1002/jobm.201200397","authors":"Jo H, Cho YW, Ji SY, Kang GY, Lim CJ","authors_abbrev":"Jo H et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2013-03-05","publication_year":"2014","canto_session_key":"835a92232f152677","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-20 10:54:12","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-02-20 10:54:05","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-02-20"},{"uniquename":"PMID:9207111","title":"Position- and orientation-independent activity of the Schizosaccharomyces pombe meiotic recombination hot spot M26.","citation":"Proc Natl Acad Sci U S A 1997 Jul 08;94(14):7446-51","abstract":"The activity of the M26 meiotic recombination hot spot of Schizosaccharomyces pombe depends on the presence of the heptamer 5'-ATGACGT-3'. Transplacement of DNA fragments containing the ade6-M26 gene to other chromosomal loci has previously demonstrated that the heptamer functions in some, but not all, transplacements, suggesting that hot spot activity depends on chromosomal context. In this study, hot spot activity was tested in the absence of gross DNA changes by using site-directed mutagenesis to create the heptamer sequence at novel locations in the genome. When created by mutagenesis of 1-4 bp in the ade6 and ura4 genes, the heptamer was active as a recombination hot spot, in an orientation-independent manner, at all locations tested. Thus, the heptamer sequence can create an active hot spot in other chromosomal contexts, provided that the gross chromosomal structure is not altered; this result is consistent with the hypothesis that a specific higher-order chromatin structure is required for M26 hot spot activity.","authors":"Fox ME, Virgin JB, Metzger J, Smith GR","authors_abbrev":"Fox ME et al.","pubmed_publication_date":"08 Jul 1997","pubmed_entrez_date":"1997-07-08","publication_year":"1997","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7821791","title":"A copy-number-controlled expression vector for the fission yeast Schizosaccharomyces pombe.","citation":"Gene 1994 Dec 15;150(2):275-80","abstract":"A novel expression vector for the fission yeast Schizosaccharomyces pombe carries the neomycin-resistance-encoding gene regulated by the SV40 early promoter, and its copy number is controlled by the level of Geneticin (G418). Foreign gene expression is driven by the human cytomegalovirus (hCMV) promoter which is transcriptionally active in S. pombe. Moreover, the vector expresses foreign genes at high levels, due to the 5'-untranslated region (5'-UTR) containing an A + T-rich sequence of about 50 nucleotides located between the TATA box of the hCMV promoter and the start codon. Recombinant human lipocortin I was produced at levels of up to 50% of the total soluble protein in the presence of 100-200 micrograms/ml of G418 in the media. Southern and Northern blotting showed that this high level of expression was due to an increase in copy number induced by G418, the high transcriptional activity of the hCMV promoter and the high translational efficiency of the 5'-UTR. We modified the vector into an 'ATG vector', named pTL2M, that maintains the 5'-UTR optimized for gene expression and into which any foreign gene, whose exact sequence is known, can be easily inserted.","authors":"Tohda H, Okada H, Giga-Hama Y, Okayama H, Kumagai H","authors_abbrev":"Tohda H et al.","pubmed_publication_date":"15 Dec 1994","pubmed_entrez_date":"1994-12-15","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15498101","title":"Germinating fission yeast spores delay in G1 in response to UV irradiation.","citation":"BMC Cell Biol 2004 Oct 21;5(1):40","abstract":"Checkpoint mechanisms prevent cell cycle transitions until previous events have been completed or damaged DNA has been repaired. In fission yeast, checkpoint mechanisms are known to regulate entry into mitosis, but so far no checkpoint inhibiting S phase entry has been identified.\nWe have studied the response of germinating Schizosaccharomyces pombe spores to UV irradiation in G1. When germinating spores are irradiated in early G1 phase, entry into S phase is delayed. We argue that the observed delay is caused by two separate mechanisms. The first takes place before entry into S phase, does not depend on the checkpoint proteins Rad3, Cds1 and Chk1 and is independent of Cdc2 phosphorylation. Furthermore, it is not dependent upon inhibiting the Cdc10-dependent transcription required for S phase entry, unlike a G1/S checkpoint described in budding yeast. We show that expression of Cdt1, a protein essential for initiation of DNA replication, is delayed upon UV irradiation. The second part of the delay occurs after entry into S phase and depends on Rad3 and Cds1 and is probably due to the intra-S checkpoint. If the germinating spores are irradiated in late G1, they enter S phase without delay and arrest in S phase, suggesting that the delay we observe upon UV irradiation in early G1 is not caused by nonspecific effects of UV irradiation.\nWe have studied the response of germinating S. pombe spores to UV irradiation in G1 and shown that S phase entry is delayed by a mechanism that is different from classical checkpoint responses. Our results point to a mechanism delaying expression of proteins required for S phase entry.","authors":"Nilssen EA, Synnes M, Tvegård T, Vebø H, Boye E, Grallert B","authors_abbrev":"Nilssen EA et al.","pubmed_publication_date":"21 Oct 2004","pubmed_entrez_date":"2004-10-23","publication_year":"2004","canto_session_key":"35b2dc8faa294262","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-01-18 15:36:24","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-01-18 15:35:57","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPAC694.06c","SPCC18B5.11c","SPAC22F3.09c","SPBC342.05","SPAC664.07c","SPBC216.05","SPBC32F12.09","SPAC20G4.04c","SPCC1259.13","SPAC14C4.13","SPAC9E9.08"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2016-01-18"},{"uniquename":"PMID:25392301","title":"Fission yeast profilin is tailored to facilitate actin assembly by the cytokinesis formin Cdc12.","citation":"Mol Biol Cell 2015 Jan 15;26(2):283-93","abstract":"The evolutionarily conserved small actin-monomer binding protein profilin is believed to be a housekeeping factor that maintains a general pool of unassembled actin. However, despite similar primary sequences, structural folds, and affinities for G-actin and poly-L-proline, budding yeast profilin ScPFY fails to complement fission yeast profilin SpPRF temperature-sensitive mutant cdc3-124 cells. To identify profilin's essential properties, we built a combinatorial library of ScPFY variants containing either WT or SpPRF residues at multiple positions and carried out a genetic selection to isolate variants that support life in fission yeast. We subsequently engineered ScPFY(9-Mut), a variant containing nine substitutions in the actin-binding region, which complements cdc3-124 cells. ScPFY(9-Mut), but not WT ScPFY, suppresses severe cytokinesis defects in cdc3-124 cells. Furthermore, the major activity rescued by ScPFY(9-Mut) is the ability to enhance cytokinesis formin Cdc12-mediated actin assembly in vitro, which allows cells to assemble functional contractile rings. Therefore an essential role of profilin is to specifically facilitate formin-mediated actin assembly for cytokinesis in fission yeast.","doi":"10.1091/mbc.E13-05-0281","authors":"Bestul AJ, Christensen JR, Grzegorzewska AP, Burke TA, Sees JA, Carroll RT, Sirotkin V, Keenan RJ, Kovar DR","authors_abbrev":"Bestul AJ et al.","pubmed_publication_date":"15 Jan 2015","pubmed_entrez_date":"2014-11-14","publication_year":"2015","canto_session_key":"b6e71cdecca45457","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-11-15 01:16:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15867927","title":"Tea for three: control of fission yeast polarity.","citation":"Nat Cell Biol 2005 May;7(5):450-1","abstract":"","authors":"Snaith HA, Sawin KE","authors_abbrev":"Snaith HA et al.","pubmed_publication_date":"May 2005","pubmed_entrez_date":"2005-05-04","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3148731","title":"Phylogenetic calibration of the 5' terminal domain of large rRNA achieved by determining twenty eucaryotic sequences.","citation":"J Mol Evol 1988 Dec;28(1-2):113-24","abstract":"Due to their high information content and their particular mode of variation, large rRNA molecules potentially represent powerful indicators of phylogenetic relationships. Even partial sequences may suffice to generate reliable estimations, provided they correspond to well-chosen portions of the molecule. We have systematically analyzed a specific portion of the large rRNA (the region extending over nearly 400 nucleotides from the 5' end) as a general index of eucaryotic phylogeny. By means of fast and direct rRNA sequencing, we have determined the sequence of this region for 20 additional eucaryotes, including several representatives of each vertebrate class, an invertebrate metazoan (mussel), a fungus (Schizosaccharomyces pombe), and three higher plants. Comparative treatment of these new data and previously reported rRNA sequences shows that this region can serve as an indicator of eucaryotic phylogeny for evaluating both long-range and short-range relationships. Its conservative domains appear to possess a rather uniform rate of nucleotide changes in all the eucaryotic lineages analyzed and the phylogenetic tree we derived agrees with classical views.","authors":"Qu LH, Nicoloso M, Bachellerie JP","authors_abbrev":"Qu LH et al.","pubmed_publication_date":"Dec 1988","pubmed_entrez_date":"1988-12-01","publication_year":"1988","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC01094","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8809106","title":"BTF3 is evolutionarily conserved in fission yeast.","citation":"Biochim Biophys Acta 1996 Sep 11;1308(3):182-4","abstract":"BTF3 is a protein initially identified in HeLa cells that may be involved in the initiation of transcription. Although its specific role in transcription is unclear, BTF3 can form a stable complex with RNA polymerase II. Recently, BTF3 has also been shown to bind to nascent polypeptide chains. We have cloned a homolog of BTF3 from the fission yeast, Schizosaccharomyces pombe. This homolog, spBTF3, encodes a putative 151 amino acid protein that shares 72% similarity with human BTF3, 73% similarity with the Caenorhabditis elegans homolog and between 52 and 53% similarity with the Saccharomyces cerevisiae homologs, EGD1 and BTT1.","authors":"Potashkin J, Wentz-Hunter K, Callaci J","authors_abbrev":"Potashkin J et al.","pubmed_publication_date":"11 Sep 1996","pubmed_entrez_date":"1996-09-11","publication_year":"1996","canto_session_key":"902d34bf4abe94ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-09 15:24:25","canto_approved_date":"2019-01-09 15:24:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 15:21:11","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-09"},{"uniquename":"PMID:35536002","title":"Activities and Structure-Function Analysis of Fission Yeast Inositol Pyrophosphate (IPP) Kinase-Pyrophosphatase Asp1 and Its Impact on Regulation of  pho1  Gene Expression.","citation":"mBio 2022 Jun 28;13(3):e0103422","abstract":"Inositol pyrophosphates (IPPs) are signaling molecules that regulate cellular phosphate homeostasis in diverse eukaryal taxa. In fission yeast, mutations that increase 1,5-IP 8  derepress the  PHO  regulon while mutations that ablate IP 8  synthesis are  PHO  hyper-repressive. Fission yeast Asp1, the principal agent of 1,5-IP 8  dynamics, is a bifunctional enzyme composed of an N-terminal IPP kinase domain and a C-terminal IPP pyrophosphatase domain. Here we conducted a biochemical characterization and mutational analysis of the autonomous Asp1 kinase domain (aa 1-385). Reaction of Asp1 kinase with IP 6  and ATP resulted in both IP 6  phosphorylation to 1-IP 7  and hydrolysis of the ATP γ-phosphate, with near-equal partitioning between productive 1-IP 7  synthesis and unproductive ATP hydrolysis under optimal kinase conditions. By contrast, reaction of Asp1 kinase with 5-IP 7  is 22-fold faster than with IP 6  and is strongly biased in favor of IP 8  synthesis versus ATP hydrolysis. Alanine scanning identified essential constituents of the active site. We deployed the Ala mutants to show that derepression of  pho1  expression correlated with Asp1's kinase activity. In the case of full-length Asp1, the activity of the C-terminal pyrophosphatase domain stifled net phosphorylation of the 1-position during reaction of Asp1 with ATP and either IP 6  or 5-IP 7 . We report that inorganic phosphate is a concentration-dependent enabler of net IP 8  synthesis by full-length Asp1  in vitro , by virtue of its antagonism of IP 8  turnover.  IMPORTANCE  Expression of the fission yeast phosphate regulon is sensitive to the intracellular level of the inositol pyrophosphate (IPP) signaling molecule 1,5-IP 8 . IP 8  dynamics are determined by Asp1, a bifunctional enzyme comprising N-terminal IPP 1-kinase and C-terminal IPP 1-pyrophosphatase domains that catalyze IP 8  synthesis and catabolism, respectively. Here, we interrogated the activities and specificities of the Asp1 kinase domain and full length Asp1. We find that reaction of Asp1 kinase with 5-IP 7  is 22-fold faster than with IP 6  and is strongly biased in favor of IP 8  synthesis versus the significant unproductive ATP hydrolysis seen during its reaction with IP 6 . We report that full-length Asp1 catalyzes futile cycles of 1-phosphate phosphorylation by its kinase component and 1-pyrophosphate hydrolysis by its pyrophosphatase component that result in unproductive net consumption of the ATP substrate. Net synthesis of 1,5-IP 8  is enabled by physiological concentrations of inorganic phosphate that selectively antagonize IP 8  turnover.","doi":"10.1128/mbio.01034-22","authors":"Benjamin B, Garg A, Jork N, Jessen HJ, Schwer B, Shuman S","authors_abbrev":"Benjamin B et al.","pubmed_publication_date":"28 Jun 2022","pubmed_entrez_date":"2022-05-10","publication_year":"2022","canto_session_key":"06a0bcdb548ec92c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Bradley Benjamin","canto_first_approved_date":"2022-10-19 12:18:48","canto_approved_date":"2024-08-13 15:37:01","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2022-10-04 17:59:43","canto_added_date":"2022-05-12 00:15:03","annotation_curators":[{"name":"Bradley Benjamin","community_curator":true,"annotation_count":1,"orcid":"0000-0002-8732-2330","file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":27,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPCC1672.06c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2022-10-19"},{"uniquename":"PMID:17053780","title":"Genome-wide characterization of fission yeast DNA replication origins.","citation":"EMBO J 2006 Nov 01;25(21):5171-9","abstract":"Eukaryotic DNA replication is initiated from multiple origins of replication, but little is known about the global regulation of origins throughout the genome or in different types of cell cycles. Here, we identify 401 strong origins and 503 putative weaker origins spaced in total every 14 kb throughout the genome of the fission yeast Schizosaccharomyces pombe. The same origins are used during premeiotic and mitotic S-phases. We found that few origins fire late in mitotic S-phase and that activating the Rad3 dependent S-phase checkpoint by inhibiting DNA replication had little effect on which origins were fired. A genome-wide analysis of eukaryotic origin efficiencies showed that efficiency was variable, with large chromosomal domains enriched for efficient or inefficient origins. Average efficiency is twice as high during mitosis compared with meiosis, which can account for their different S-phase lengths. We conclude that there is a continuum of origin efficiency and that there is differential origin activity in the mitotic and meiotic cell cycles.","authors":"Heichinger C, Penkett CJ, Bähler J, Nurse P","authors_abbrev":"Heichinger C et al.","pubmed_publication_date":"01 Nov 2006","pubmed_entrez_date":"2006-10-21","publication_year":"2006","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1165770","title":"Genetic control of cell size at cell division in yeast.","citation":"Nature 1975 Aug 14;256(5518):547-51","abstract":"","authors":"Nurse P","authors_abbrev":"Nurse P","pubmed_publication_date":"14 Aug 1975","pubmed_entrez_date":"1975-08-14","publication_year":"1975","canto_session_key":"49463cfe74c11d1f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2019-03-28 17:12:46","canto_approved_date":"2021-09-28 17:35:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-27 13:09:53","canto_added_date":"2014-02-28 14:30:43","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":6,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-03-28"},{"uniquename":"PMID:19229492","title":"Overexpression of bacterioferritin comigratory protein (Bcp) enhances viability and reduced glutathione level in the fission yeast under stress.","citation":"J Microbiol 2009 Feb;47(1):60-7","abstract":"The structural gene encoding bacterioferritin comigratory protein (Bcp) was amplified using PCR from the genomic DNA of Schizosaccharomyces pombe, and transferred into the shuttle vector pRS316 to generate the recombinant plasmid pBCPlO. The bcp(+) mRNA level in the pBCPlO-containing yeast cells was significantly higher than that in the control yeast cells, indicating that the cloned gene is functioning. The S. pombe cells harboring the plasmid pBCPIO exhibited higher survival on the solid minimal media with hydrogen peroxide, tert-BOOH or cadmium than the control yeast cells. They also exhibited enhanced cellular viability in the liquid media containing the stressful agents. The increased viabilities of the fission yeast cells harboring the plasmid pBCP10 were also obtained with 0.4% glucose or 0.4% sucrose as a sole carbon source, and nitrogen starvation, compared with those of the control yeast cells. The total glutathione (GSH) content and total GSH/GSSG ratio were significantly higher in the yeast cells harboring the plasmid pBCP10 than in the control yeast cells. In brief, the S. pombe Bcp plays a protective role in the defensive response to oxidative stress possibly via up-regulation of total and reduced glutathione levels.","doi":"10.1007/s12275-008-0077-3","authors":"Kang GY, Park EH, Kim K, Lim CJ","authors_abbrev":"Kang GY et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2009-02-21","publication_year":"2009","canto_session_key":"10a68ff4ce106ab3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-30 10:14:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-30 10:14:46","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1773.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-30"},{"uniquename":"PMID:20924356","title":"The APC/C subunit Cdc16/Cut9 is a contiguous tetratricopeptide repeat superhelix with a homo-dimer interface similar to Cdc27.","citation":"EMBO J 2010 Nov 03;29(21):3733-44","abstract":"The anaphase-promoting complex/cyclosome (APC/C), an E3 ubiquitin ligase responsible for controlling cell cycle transitions, is a multisubunit complex assembled from 13 different proteins. Numerous APC/C subunits incorporate multiple copies of the tetratricopeptide repeat (TPR). Here, we report the crystal structure of Schizosaccharomyces pombe Cut9 (Cdc16/Apc6) in complex with Hcn1 (Cdc26), showing that Cdc16/Cut9 is a contiguous TPR superhelix of 14 TPR units. A C-terminal block of TPR motifs interacts with Hcn1, whereas an N-terminal TPR block mediates Cdc16/Cut9 self-association through a homotypic interface. This dimer interface is structurally related to the N-terminal dimerization domain of Cdc27, demonstrating that both Cdc16/Cut9 and Cdc27 form homo-dimers through a conserved mechanism. The acetylated N-terminal Met residue of Hcn1 is enclosed within a chamber created from the Cut9 TPR superhelix. Thus, in complex with Cdc16/Cut9, the N-acetyl-Met residue of Hcn1, a putative degron for the Doa10 E3 ubiquitin ligase, is inaccessible for Doa10 recognition, protecting Hcn1/Cdc26 from ubiquitin-dependent degradation. This finding may provide a structural explanation for a mechanism to control the stoichiometry of proteins participating in multisubunit complexes.","doi":"10.1038/emboj.2010.247","authors":"Zhang Z, Kulkarni K, Hanrahan SJ, Thompson AJ, Barford D","authors_abbrev":"Zhang Z et al.","pubmed_publication_date":"03 Nov 2010","pubmed_entrez_date":"2010-10-07","publication_year":"2010","canto_session_key":"b37da6edde2961c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-11-26 14:05:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-26 14:05:48","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.15c","SPAC23C11.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-11-26","pdb_entries":[{"pdb_id":"2xpi","gene_chains":[{"gene_uniquename":"SPAC23C11.12","chain":"B/E","position":"1-80"},{"gene_uniquename":"SPAC6F12.15c","chain":"A/D","position":"1-597"}],"title":"Crystal structure of APC/C hetero-tetramer Cut9-Hcn1","entry_authors":"Zhang Z,Kulkarni KA,Barford D","entry_authors_abbrev":"Zhang Z et al.","reference_uniquename":"PMID:20924356","experimental_method":"X-ray","resolution":"2.6"}]},{"uniquename":"PMID:28634040","title":"1,2,4-Triazole and 1,3,4-oxadiazole analogues: Synthesis, MO studies, in silico molecular docking studies, antimalarial as DHFR inhibitor and antimicrobial activities.","citation":"Bioorg Med Chem 2017 Aug 01;25(15):4064-4075","abstract":"1,2,4-Triazole and 1,3,4-oxadiazole analogues are of interest due to their potential activity against microbial and malarial infections. In search of suitable antimicrobial and antimalarial compounds, we report here the synthesis, characterization and biological activities of 1,2,4-triazole and 1,3,4-oxadiazole analogues (SS 1-SS 10). The molecules were characterized by IR, mass,  1 H NMR,  13 C NMR and elemental analysis. The in vitro antimicrobial activity was investigated against pathogenic strains, the results were explained with the help of DFT and PM6 molecular orbital calculations. In vitro cytotoxicity and genotoxicity of the molecules were studied against S. pombe cells. In vitro antimalarial activity was studied. The active compounds were further evaluated for enzyme inhibition efficacy against the receptor Pf-DHFR computationally as well as in vitro to prove their candidature as lead dihydrofolate reductase inhibitors.","doi":"10.1016/j.bmc.2017.05.054","authors":"Thakkar SS, Thakor P, Doshi H, Ray A","authors_abbrev":"Thakkar SS et al.","pubmed_publication_date":"01 Aug 2017","pubmed_entrez_date":"2017-06-22","publication_year":"2017","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2017-06-23 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41082120","title":"Using CMAC Staining for Vacuole Characterization in Yeast.","citation":"Methods Mol Biol 2026;2976:175-188","abstract":"CMAC (7-amino-4-chloromethylcoumarin) staining is a valuable tool for visualizing acidic organelles, including vacuoles, in yeast cells. By selectively accumulating in acidic compartments, CMAC allows specific labeling and visualization of vacuoles in living or fixed cells, aiding in the investigation of vacuole dynamics, morphology, and distribution under various conditions. This staining method provides a clear contrast against cellular autofluorescence, enhancing imaging clarity. It can be combined with automated imaging capture for faster throughput and analysis.Characterizing vacuole phenotypes using CMAC staining contributes to our understanding of cellular homeostasis and disease mechanisms in yeast. It has applications in studying fundamental cellular processes, including endocytic trafficking and autophagy, as well as in drug screening assays, and can be used in yeast models of disease to offer insights into potential therapeutic targets for diseases affecting the lysosome, including neurodegenerative diseases.","doi":"10.1007/978-1-0716-4844-5_13","authors":"Clemente-Ramos JÁ, Mole SE","authors_abbrev":"Clemente-Ramos JÁ et al.","pubmed_publication_date":"2026","pubmed_entrez_date":"2025-10-13","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-10-13 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9557545","title":"[Molecular mechanisms for the regulation of meiosis in fission yeast].","citation":"Tanpakushitsu Kakusan Koso 1998 Mar;43(4):314-21","abstract":"","authors":"Yamashita A, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"Mar 1998","pubmed_entrez_date":"1998-04-29","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15121844","title":"The splicing factor U2AF small subunit is functionally conserved between fission yeast and humans.","citation":"Mol Cell Biol 2004 May;24(10):4229-40","abstract":"The small subunit of U2AF, which functions in 3' splice site recognition, is more highly conserved than its heterodimeric partner yet is less thoroughly investigated. Remarkably, we find that the small subunit of Schizosaccharomyces pombe U2AF (U2AF(SM)) can be replaced in vivo by its human counterpart, demonstrating that the conservation extends to function. Precursor mRNAs accumulate in S. pombe following U2AF(SM) depletion in a time frame consistent with a role in splicing. A comprehensive mutational analysis reveals that all three conserved domains are required for viability. Notably, however, a tryptophan in the pseudo-RNA recognition motif implicated in a key contact with the large subunit by crystallographic data is dispensable whereas amino acids implicated in RNA recognition are critical. Mutagenesis of the two zinc-binding domains demonstrates that they are neither equivalent nor redundant. Finally, two- and three-hybrid analyses indicate that mutations with effects on large-subunit interactions are rare whereas virtually all alleles tested diminished RNA binding by the heterodimer. In addition to demonstrating extraordinary conservation of U2AF small-subunit function, these results provide new insights into the roles of individual domains and residues.","authors":"Webb CJ, Wise JA","authors_abbrev":"Webb CJ et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-05-04","publication_year":"2004","canto_session_key":"72862a5b1395f450","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-07 17:31:00","canto_approved_date":"2025-09-03 13:48:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-07 17:30:53","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_15121844_phaf.tsv"}],"genes":["SPAP8A3.06","SPAC6F6.08c","SPAC16.02c","SPBC146.07"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2014-08-07"},{"uniquename":"PMID:15546621","title":"An SMC-domain protein in fission yeast links telomeres to the meiotic centrosome.","citation":"Mol Cell 2004 Nov 19;16(4):619-30","abstract":"Abnormal centrosomal structures similar to those occurring in human cancers are induced in fission yeast by overexpression of the pericentrin homolog Pcp1p. Analysis of abnormal Pcp1p-containing structures with quantitative mass spectrometry and isotope-coded affinity tags identified a coiled-coil, structural maintenance of chromosomes (SMC) domain protein. This protein, termed Ccq1p (coiled-coil protein quantitatively enriched), localizes with Taz1p to telomeres in normal vegetative cells. Fluorescence resonance energy transfer (FRET) measurements indicate that Ccq1p also interacts with centrosomal Pcp1p in mating pheromone-stimulated cells containing centrosomally clustered telomeres. We provide evidence that the Ccq1p-Pcp1p interaction, while essential for meiosis, is deleterious when forced to occur during vegetative growth. Cells lacking one ccq1 allele exhibit a loss-of-function phenotype including abnormally long cell length, chromosome segregation failure, telomeric shortening, and defective telomeric clustering during meiotic prophase. Our data indicate a mechanism underlying meiotic chromosomal bouquet formation and suggest a recruitment model for supernumerary centrosome toxicity.","authors":"Flory MR, Carson AR, Muller EG, Aebersold R","authors_abbrev":"Flory MR et al.","pubmed_publication_date":"19 Nov 2004","pubmed_entrez_date":"2004-11-18","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6G9.06c","SPCC188.07"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:14653990","title":"Regulated mRNA stability of the Cdk inhibitor Rum1 links nutrient status to cell cycle progression.","citation":"Curr Biol 2003 Dec 02;13(23):2015-24","abstract":"The survival of a cell depends on continuous sensing of the nutritional environment and appropriate coordination of the cell cycle. The fission yeast Schizosaccharomyces pombe is an excellent model system in which to study these processes. In the presence of nutrients, fission yeast cells grow and divide, spending most of their time in G2; when nutrients are limiting, they are promoted into mitosis and arrest the cell cycle in G1. The molecular mechanisms underlying this response are currently unknown.\nHere, we show that expression of the fission yeast Cdk inhibitor Rum1, a key regulator of Cdc2/cyclin B in G1, is subject to regulated mRNA stability in response to nutrient deprivation. In complete minimal medium, rum1 mRNAs are very unstable. Following nitrogen starvation, rum1 mRNAs are rapidly stabilized, allowing the accumulation of Rum1 protein to delay the G1 phase of the subsequent cell cycle. Instability of rum1 mRNAs in complete minimal medium depends on the presence of AU-rich elements in the 3'UTR. We also show that lack of this mechanism has consequences in the mitotic cell cycle, in meiosis, and in the control of ploidy.\nWe propose that mRNA stability is an important mechanism to fine tune the expression of the rum1 gene, in order to allow the production of appropriate levels of Rum1 protein in response to changes in the nutritional environment.","authors":"Daga RR, Bolaños P, Moreno S","authors_abbrev":"Daga RR et al.","pubmed_publication_date":"02 Dec 2003","pubmed_entrez_date":"2003-12-05","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31719112","title":"Checkpoint Regulation of Nuclear Tos4 Defines S Phase Arrest in Fission Yeast.","citation":"G3 (Bethesda) 2020 Jan 07;10(1):255-266","abstract":"From yeast to humans, the cell cycle is tightly controlled by regulatory networks that regulate cell proliferation and can be monitored by dynamic visual markers in living cells. We have observed S phase progression by monitoring nuclear accumulation of the FHA-containing DNA binding protein Tos4, which is expressed in the G1/S phase transition. We use Tos4 localization to distinguish three classes of DNA replication mutants: those that arrest with an apparent 1C DNA content and accumulate Tos4 at the restrictive temperature; those that arrest with an apparent 2C DNA content, that do not accumulate Tos4; and those that proceed into mitosis despite a 1C DNA content, again without Tos4 accumulation. Our data indicate that Tos4 localization in these conditions is responsive to checkpoint kinases, with activation of the Cds1 checkpoint kinase promoting Tos4 retention in the nucleus, and activation of the Chk1 damage checkpoint promoting its turnover. Tos4 localization therefore allows us to monitor checkpoint-dependent activation that responds to replication failure in early  vs.  late S phase.","doi":"10.1534/g3.119.400726","authors":"Kim SM, Tripathi VP, Shen KF, Forsburg SL","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"07 Jan 2020","pubmed_entrez_date":"2019-11-14","publication_year":"2020","canto_session_key":"bcb5a5b99a75c27a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Seong Min Kim","canto_first_approved_date":"2020-03-30 14:14:45","canto_approved_date":"2024-07-02 17:12:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-19 17:21:41","canto_added_date":"2019-11-15 01:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Seong Min Kim","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC20G8.01","SPAC17C9.01c","SPBC14C8.07c","SPBC336.04","SPBC106.09","SPBC336.12c","SPBC1734.02c","SPBC26H8.07c","SPAC1F7.05","SPAC17D4.02","SPCC1259.13","SPAC23C4.18c","SPAC6F12.15c","SPAP14E8.02","SPBC776.12c","SPCC16A11.17","SPCC18B5.11c"],"gene_count":18,"ltp_gene_count":5,"approved_date":"2020-03-30"},{"uniquename":"PMID:28292899","title":"Fission yeast myosin I facilitates PI(4,5)P 2 -mediated anchoring of cytoplasmic dynein to the cortex.","citation":"Proc Natl Acad Sci U S A 2017 Mar 28;114(13):E2672-E2681","abstract":"Several key processes in the cell, such as vesicle transport and spindle positioning, are mediated by the motor protein cytoplasmic dynein, which produces force on the microtubule. For the functions that require movement of the centrosome and the associated nuclear material, dynein needs to have a stable attachment at the cell cortex. In fission yeast, Mcp5 is the anchor protein of dynein and is required for the oscillations of the horsetail nucleus during meiotic prophase. Although the role of Mcp5 in anchoring dynein to the cortex has been identified, it is unknown how Mcp5 associates with the membrane as well as the importance of the underlying attachment to the nuclear oscillations. Here, we set out to quantify Mcp5 organization and identify the binding partner of Mcp5 at the membrane. We used confocal and total internal reflection fluorescence microscopy to count the number of Mcp5 foci and the number of Mcp5 molecules in an individual focus. Further, we quantified the localization pattern of Mcp5 in fission yeast zygotes and show by perturbation of phosphatidylinositol 4-phosphate 5-kinase that Mcp5 binds to phosphatidylinositol 4,5-bisphosphate [PI(4,5)P 2 ]. Remarkably, we discovered that the myosin I protein in fission yeast, Myo1, which is required for organization of sterol-rich domains in the cell membrane, facilitates the localization of Mcp5 and that of cytoplasmic dynein on the membrane. Finally, we demonstrate that Myo1-facilitated association of Mcp5 and dynein to the membrane determines the dynamics of nuclear oscillations and, in essence, dynein activity.","doi":"10.1073/pnas.1615883114","authors":"Thankachan JM, Nuthalapati SS, Addanki Tirumala N, Ananthanarayanan V","authors_abbrev":"Thankachan JM et al.","pubmed_publication_date":"28 Mar 2017","pubmed_entrez_date":"2017-03-16","publication_year":"2017","canto_session_key":"15a5190fe0560730","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Vaishnavi Ananthanarayanan","canto_first_approved_date":"2019-05-11 18:11:18","canto_approved_date":"2026-04-06 16:03:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-04-23 09:21:45","canto_added_date":"2017-03-17 01:15:15","annotation_curators":[{"name":"Vaishnavi Ananthanarayanan","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29A4.05","SPAC19G12.14","SPBC216.02","SPBC146.13c","SPAC1093.06c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2019-05-11"},{"uniquename":"GO_REF:0000064","title":"Representation of cell components as part of other cell components in the Gene Ontology","abstract":"We have created a standard template for classes describing cell components as part of other cell components. The underlying equivalence axiom template is \"P and 'part_of' some W\", where P and W are cell components.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34228709","title":"Expression of the cancer-associated DNA polymerase ε P286R in fission yeast leads to translesion synthesis polymerase dependent hypermutation and defective DNA replication.","citation":"PLoS Genet 2021 Jul;17(7):e1009526","abstract":"Somatic and germline mutations in the proofreading domain of the replicative DNA polymerase ε (POLE-exonuclease domain mutations, POLE-EDMs) are frequently found in colorectal and endometrial cancers and, occasionally, in other tumours. POLE-associated cancers typically display hypermutation, and a unique mutational signature, with a predominance of C > A transversions in the context TCT and C > T transitions in the context TCG. To understand better the contribution of hypermutagenesis to tumour development, we have modelled the most recurrent POLE-EDM (POLE-P286R) in Schizosaccharomyces pombe. Whole-genome sequencing analysis revealed that the corresponding pol2-P287R allele also has a strong mutator effect in vivo, with a high frequency of base substitutions and relatively few indel mutations. The mutations are equally distributed across different genomic regions, but in the immediate vicinity there is an asymmetry in AT frequency. The most abundant base-pair changes are TCT > TAT transversions and, in contrast to human mutations, TCG > TTG transitions are not elevated, likely due to the absence of cytosine methylation in fission yeast. The pol2-P287R variant has an increased sensitivity to elevated dNTP levels and DNA damaging agents, and shows reduced viability on depletion of the Pfh1 helicase. In addition, S phase is aberrant and RPA foci are elevated, suggestive of ssDNA or DNA damage, and the pol2-P287R mutation is synthetically lethal with rad3 inactivation, indicative of checkpoint activation. Significantly, deletion of genes encoding some translesion synthesis polymerases, most notably Pol κ, partially suppresses pol2-P287R hypermutation, indicating that polymerase switching contributes to this phenotype.","doi":"10.1371/journal.pgen.1009526","authors":"Soriano I, Vazquez E, De Leon N, Bertrand S, Heitzer E, Toumazou S, Bo Z, Palles C, Pai CC, Humphrey TC, Tomlinson I, Cotterill S, Kearsey SE","authors_abbrev":"Soriano I et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-07-06","publication_year":"2021","canto_session_key":"a17bd0ab5d302ba7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Stephen Kearsey","canto_first_approved_date":"2021-09-14 14:44:58","canto_approved_date":"2025-09-03 11:43:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-02 11:17:37","canto_added_date":"2021-07-08 00:15:04","annotation_curators":[{"name":"Ignacio Soriano","community_curator":true,"annotation_count":26,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Stephen Kearsey","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.01c","SPAC688.10","SPBC16A3.11","SPBC887.14c","SPAC1F7.05","SPCC18B5.11c","SPBC25H2.13c","SPCC553.07c","SPBC660.13c","SPBC216.05","SPCC1259.13","SPBC336.04"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2021-09-14"},{"uniquename":"PMID:1946720","title":"The effects of odors from stressed mice on conspecific behavior.","citation":"Physiol Behav 1991 Jul;50(1):221-7","abstract":"Four experiments correlate conspecific reactions to odors from stressed (foot shocked) BALB/cJ mice with the frequency of specific motor activities and taste avoidance. Where behavior was restricted to forward and backward movement in a tube, animals tended to avoid the side where the odors from stressed animals entered. In a more socially complex home cage (3 recipients) a wide variety of behaviors were affected by odors from stressed conspecifics. Animals were alerted by the odor, searched out the source of the odor and showed increases in general activity, rearing, and air sampling. Many of these behaviors habituated with continuous exposure. The major response to odors from stressed animals was to increase \"vigilance.\" A restriction of behavioral opportunities will lead to odor avoidance; however, when the environment permits, the behavioral reaction to odors becomes more complex. These odors failed to produce conditioned taste aversion, suggesting a sensory specificity in the use of these odors.","authors":"Zalaquett C, Thiessen D","authors_abbrev":"Zalaquett C et al.","pubmed_publication_date":"Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42231506","title":"Dbp7 interacts with RNA exosome component Dis3 to mediate CENP-A loading to centromeres.","citation":"Genome Biol 2026 Jun 02;","abstract":"Centromeres are crucial for proper chromosome segregation during cell division. Centromeres in most eukaryotes are epigenetically defined by the histone H3 variant, CENP-A. Centromeric regions are typically transcribed into non-coding RNAs that contribute to centromere functions. However, the precise role of centromeric RNAs in CENP-A loading, in particular the formation of R-loops, remains poorly understood and the mechanisms that safeguard centromeres from R-loop-associated defects are still largely unclear.\nTogether, this study uncovers a previously unrecognized CENP-A loading mechanism, by which Dbp7 and Dis3 act together to bind to centromeric transcripts and in turn mediate recruitment of CENP-A via the CENP-A chaperone Sim3, providing mechanistic insight into R-loop resolution at centromeres.","doi":"10.1186/s13059-026-04133-8","authors":"Gao J, Gao F, Dong Q, Li Z, Mao L, Ali M, Liao J, Yang J, Li F","authors_abbrev":"Gao J et al.","pubmed_publication_date":"02 Jun 2026","pubmed_entrez_date":"2026-06-03","publication_year":"2026","canto_session_key":"5fd5b7dec650b9b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Fei Li","canto_first_approved_date":"2026-06-21 13:24:48","canto_approved_date":"2026-06-21 13:24:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-06-12 18:59:46","canto_added_date":"2026-06-03 23:25:06","annotation_curators":[{"name":"Fei Li","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.06c","SPBC26H8.10","SPBC1105.17","SPBC21H7.04","SPBC577.15c","SPAC1687.20c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2026-06-21"},{"uniquename":"PMID:19945358","title":"Linking up and interacting with BRCT domains.","citation":"DNA Repair (Amst) 2010 Feb 04;9(2):103-8","abstract":"BRCT domains are present in an ever expanding family of proteins that includes many DNA repair and checkpoint proteins. The most prominent member of the BRCT family is BRCA1, mutations in which are responsible for a high proportion of breast and ovarian cancers. BRCT domains act as protein-protein interaction modules and facilitate the formation of hetero- and homo-oligomers. The domains occur either singly or in pairs, with up to eight domains in a single protein. When in pairs the domains are separated by a short inter-BRCT linker. Numerous crystal structures have been determined for BRCT domains from a range of different proteins, which indicate that the overall structure of the BRCT domains is generally well conserved. In contrast, the positions and structures of the linker regions are more varied, as are the roles of the linkers. Here, we describe the protein-protein interactions involving three different inter-BRCT linker regions, those of DNA ligase IV (LigIV), Schizosaccharomyces pombe Crb2 and human 53BP1.","doi":"10.1016/j.dnarep.2009.10.010","authors":"Watts FZ, Brissett NC","authors_abbrev":"Watts FZ et al.","pubmed_publication_date":"04 Feb 2010","pubmed_entrez_date":"2009-12-01","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28032397","title":"DNA base excision repair and nucleotide excision repair synergistically contribute to survival of stationary-phase cells of the fission yeast Schizosaccharomyces pombe.","citation":"Cell Biol Int 2017 Mar;41(3):276-286","abstract":"Defects of genome maintenance may causally contribute to aging. In general, base excision repair (BER) is involved in the repair of subtle base lesions and AP sites, and bulky helix-distorting lesions are restored by nucleotide excision repair (NER). Here, we measured the chronological lifespan (CLS) of BER- and NER-deficient mutants of the fission yeast Schizosaccharomyces pombe, and observed the aging process of cells. The CLS of the nth1 (gene for DNA glycosylase/AP lyase) mutant and the rad16 (a homolog of human XPF) mutant were slightly shorter than that of the wild-type (WT) strain. However, survival of the nth1Δ rad16Δ double mutant was significantly reduced after entry into the stationary phase. Deletion of rad16 in an AP endonuclease mutant apn2Δ also accelerated chronological aging. These results indicate that BER and NER synergistically contribute to genome maintenance in non-dividing cells. Reactive oxygen species (ROS) accumulated in cells during the stationary phase, and nth1Δ rad16Δ cells produced more ROS than WT cells. High mutation frequencies and nuclear DNA fragmentation were observed in nth1Δ rad16Δ stationary-phase cells concurrent with apoptotic-like cell death. Calorie restriction significantly reduced the level of ROS in the stationary phase and extended the CLS of nth1Δ rad16Δ cells. Therefore, ROS production critically affects the survival of the DNA repair mutant during chronological aging.","doi":"10.1002/cbin.10722","authors":"Senoo T, Kawano S, Ikeda S","authors_abbrev":"Senoo T et al.","pubmed_publication_date":"Mar 2017","pubmed_entrez_date":"2016-12-30","publication_year":"2017","canto_session_key":"2313988c3426286f","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-12-31 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16820484","title":"Old yellow enzymes protect against acrolein toxicity in the yeast Saccharomyces cerevisiae.","citation":"Appl Environ Microbiol 2006 Jul;72(7):4885-92","abstract":"Acrolein is a ubiquitous reactive aldehyde which is formed as a product of lipid peroxidation in biological systems. In this present study, we screened the complete set of viable deletion strains in Saccharomyces cerevisiae for sensitivity to acrolein to identify cell functions involved in resistance to reactive aldehydes. We identified 128 mutants whose gene products are localized throughout the cell. Acrolein-sensitive mutants were distributed among most major biological processes but particularly affected gene expression, metabolism, and cellular signaling. Surprisingly, the screen did not identify any antioxidants or similar stress-protective molecules, indicating that acrolein toxicity may not be mediated via reactive oxygen species. Most strikingly, a mutant lacking an old yellow enzyme (OYE2) was identified as being acrolein sensitive. Old yellow enzymes are known to reduce alpha,beta-unsaturated carbonyl compounds in vitro, but their physiological roles have remained uncertain. We show that mutants lacking OYE2, but not OYE3, are sensitive to acrolein, and overexpression of both isoenzymes increases acrolein tolerance. Our data indicate that OYE2 is required for basal levels of tolerance, whereas OYE3 expression is particularly induced following acrolein stress. Despite the range of alpha,beta-unsaturated carbonyl compounds that have been identified as substrates of old yellow enzymes in vitro, we show that old yellow enzymes specifically mediate resistance to small alpha,beta-unsaturated carbonyl compounds, such as acrolein, in vivo.","authors":"Trotter EW, Collinson EJ, Dawes IW, Grant CM","authors_abbrev":"Trotter EW et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-07-06","publication_year":"2006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC5H10.10","SPAC5H10.04"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:24451546","title":"Genetic and physical interaction of Ssp1 CaMKK and Rad24 14-3-3 during low pH and osmotic stress in fission yeast.","citation":"Open Biol 2014 Jan 22;4(1):130127","abstract":"The Ssp1 calmodulin kinase kinase (CaMKK) is necessary for stress-induced re-organization of the actin cytoskeleton and initiation of growth at the new cell end following division in Schizosaccharomyces pombe. In addition, it regulates AMP-activated kinase and functions in low glucose tolerance. ssp1(-) cells undergo mitotic delay at elevated temperatures and G2 arrest in the presence of additional stressors. Following hyperosmotic stress, Ssp1-GFP forms transient foci which accumulate at the cell membrane and form a band around the cell circumference, but not co-localizing with actin patches. Hyperosmolarity-induced localization to the cell membrane occurs concomitantly with a reduction of its interaction with the 14-3-3 protein Rad24, but not Rad25 which remains bound to Ssp1. The loss of rad24 in ssp1(-) cells reduces the severity of hyperosmotic stress response and relieves mitotic delay. Conversely, overexpression of rad24 exacerbates stress response and concomitant cell elongation. rad24(-) does not impair stress-induced localization of Ssp1 to the cell membrane, however this response is almost completely absent in cells overexpressing rad24.","doi":"10.1098/rsob.130127","authors":"Freitag SI, Wong J, Young PG","authors_abbrev":"Freitag SI et al.","pubmed_publication_date":"22 Jan 2014","pubmed_entrez_date":"2014-01-24","publication_year":"2014","canto_session_key":"050e6c8b4bb141e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-09 08:20:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-02-26 09:49:33","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A2.13c","SPAC24H6.05","SPAC8E11.02c","SPCC297.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-02-26"},{"uniquename":"PMID:31848341","title":"Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone.","citation":"Nat Commun 2019 Dec 17;10(1):5764","abstract":"The fundamental unit of chromatin, the nucleosome, is an intricate structure that requires histone chaperones for assembly. ATAD2 AAA+ ATPases are a family of histone chaperones that regulate nucleosome density and chromatin dynamics. Here, we demonstrate that the fission yeast ATAD2 homolog, Abo1, deposits histone H3-H4 onto DNA in an ATP-hydrolysis-dependent manner by in vitro reconstitution and single-tethered DNA curtain assays. We present cryo-EM structures of an ATAD2 family ATPase to atomic resolution in three different nucleotide states, revealing unique structural features required for histone loading on DNA, and directly visualize the transitions of Abo1 from an asymmetric spiral (ATP-state) to a symmetric ring (ADP- and apo-states) using high-speed atomic force microscopy (HS-AFM). Furthermore, we find that the acidic pore of ATP-Abo1 binds a peptide substrate which is suggestive of a histone tail. Based on these results, we propose a model whereby Abo1 facilitates H3-H4 loading by utilizing ATP.","doi":"10.1038/s41467-019-13743-9","authors":"Cho C, Jang J, Kang Y, Watanabe H, Uchihashi T, Kim SJ, Kato K, Lee JY, Song JJ","authors_abbrev":"Cho C et al.","pubmed_publication_date":"17 Dec 2019","pubmed_entrez_date":"2019-12-19","publication_year":"2019","canto_session_key":"e9f930991ecca318","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-07-07 12:16:11","canto_approved_date":"2025-12-12 21:05:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-08 11:44:55","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.19"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-07-07","pdb_entries":[{"pdb_id":"6jpq","gene_chains":[{"gene_uniquename":"SPAC31G5.19","chain":"A/B/C/D/E/F","position":"1-1190"}],"title":"CryoEM structure of Abo1 hexamer - ADP complex","entry_authors":"Cho C,Jang J,Song JJ","entry_authors_abbrev":"Cho C et al.","reference_uniquename":"PMID:31848341","experimental_method":"EM","resolution":"4.44"},{"pdb_id":"6jq0","gene_chains":[{"gene_uniquename":"SPAC31G5.19","chain":"A/B/C/D/E/F","position":"1-1190"}],"title":"CryoEM structure of Abo1 Walker B (E372Q) mutant hexamer - ATP complex","entry_authors":"Cho C,Jang J,Song JJ","entry_authors_abbrev":"Cho C et al.","reference_uniquename":"PMID:31848341","experimental_method":"EM","resolution":"3.54"},{"pdb_id":"6jpu","gene_chains":[{"gene_uniquename":"SPAC31G5.19","chain":"A/B/C/D/E/F","position":"1-1190"}],"title":"CryoEM structure of Abo1 hexamer - apo complex","entry_authors":"Cho C,Jang J,Song JJ","entry_authors_abbrev":"Cho C et al.","reference_uniquename":"PMID:31848341","experimental_method":"EM","resolution":"4.27"}]},{"uniquename":"PMID:24623809","title":"The DNA damage checkpoint pathway promotes extensive resection and nucleotide synthesis to facilitate homologous recombination repair and genome stability in fission yeast.","citation":"Nucleic Acids Res 2014 May;42(9):5644-56","abstract":"DNA double-strand breaks (DSBs) can cause chromosomal rearrangements and extensive loss of heterozygosity (LOH), hallmarks of cancer cells. Yet, how such events are normally suppressed is unclear. Here we identify roles for the DNA damage checkpoint pathway in facilitating homologous recombination (HR) repair and suppressing extensive LOH and chromosomal rearrangements in response to a DSB. Accordingly, deletion of Rad3(ATR), Rad26ATRIP, Crb2(53BP1) or Cdc25 overexpression leads to reduced HR and increased break-induced chromosome loss and rearrangements. We find the DNA damage checkpoint pathway facilitates HR, in part, by promoting break-induced Cdt2-dependent nucleotide synthesis. We also identify additional roles for Rad17, the 9-1-1 complex and Chk1 activation in facilitating break-induced extensive resection and chromosome loss, thereby suppressing extensive LOH. Loss of Rad17 or the 9-1-1 complex results in a striking increase in break-induced isochromosome formation and very low levels of chromosome loss, suggesting the 9-1-1 complex acts as a nuclease processivity factor to facilitate extensive resection. Further, our data suggest redundant roles for Rad3ATR and Exo1 in facilitating extensive resection. We propose that the DNA damage checkpoint pathway coordinates resection and nucleotide synthesis, thereby promoting efficient HR repair and genome stability.","doi":"10.1093/nar/gku190","authors":"Blaikley EJ, Tinline-Purvis H, Kasparek TR, Marguerat S, Sarkar S, Hulme L, Hussey S, Wee BY, Deegan RS, Walker CA, Pai CC, Bähler J, Nakagawa T, Humphrey TC","authors_abbrev":"Blaikley EJ et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2014-03-14","publication_year":"2014","canto_session_key":"0147ff680b7a48ca","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC29B12.03","SPBC29A10.05","SPAC9E9.08"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:21166477","title":"Addressing trypsin bias in large scale (phospho)proteome analysis by size exclusion chromatography and secondary digestion of large post-trypsin peptides.","citation":"J Proteome Res 2011 Feb 04;10(2):800-11","abstract":"In the vast majority of bottom-up proteomics studies, protein digestion is performed using only mammalian trypsin. Although it is clearly the best enzyme available, the sole use of trypsin rarely leads to complete sequence coverage, even for abundant proteins. It is commonly assumed that this is because many tryptic peptides are either too short or too long to be identified by RPLC-MS/MS. We show through in silico analysis that 20-30% of the total sequence of three proteomes (Schizosaccharomyces pombe, Saccharomyces cerevisiae, and Homo sapiens) is expected to be covered by Large post-Trypsin Peptides (LpTPs) with M(r) above 3000 Da. We then established size exclusion chromatography to fractionate complex yeast tryptic digests into pools of peptides based on size. We found that secondary digestion of LpTPs followed by LC-MS/MS analysis leads to a significant increase in identified proteins and a 32-50% relative increase in average sequence coverage compared to trypsin digestion alone. Application of the developed strategy to analyze the phosphoproteomes of S. pombe and of a human cell line identified a significant fraction of novel phosphosites. Overall our data indicate that specific targeting of LpTPs can complement standard bottom-up workflows to reveal a largely neglected portion of the proteome.","doi":"10.1021/pr100951t","authors":"Tran BQ, Hernandez C, Waridel P, Potts A, Barblan J, Lisacek F, Quadroni M","authors_abbrev":"Tran BQ et al.","pubmed_publication_date":"04 Feb 2011","pubmed_entrez_date":"2010-12-21","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8389306","title":"Negative regulation of mitosis by the fission yeast protein phosphatase ppa2.","citation":"Genes Dev 1993 Jun;7(6):1059-71","abstract":"To understand the role of the type 2A-like protein phosphatase in the cell division cycle, we investigated the mutant phenotypes obtained when the fission yeast ppa1+ and ppa2+ phosphatase genes (which encode polypeptides with approximately 80% identity to mammalian type 2A phosphatases) were either deleted or overexpressed. We also investigated the in vivo effect of okadaic acid, an inhibitor of protein serine/threonine phosphatases, on cell division. We show that ppa2+ interacts genetically with the cell cell regulators cdc25+ and wee1+, as a ppa2 deletion is lethal when combined with wee1-50 but partially suppresses the conditional lethality of cdc25-22 mutation. Evidence that ppa2+ negatively controls the entry into mitosis, possibly through the regulation of cdc2 tyrosine phosphorylation, is presented. ppa2 phosphatase is abundant in the cytoplasm, in contrast to the type 1-like phosphatase dis2, which is enriched in the nucleus. Overproduced ppa1 or ppa2 proteins accumulate in the cytoplasm near the nuclear periphery, and cells arrest in interphase. Okadaic acid-treated cells, like a ppa2 deletion, are short in length and display protein hyperphosphorylation. Cytokinesis is also inhibited, producing binucleated cells. We show that ppa2 is the genetic locus controlling okadaic acid sensitivity. The ppa2 deletion reveals the same hyperphosphorylated proteins as okadaic acid. When a strain deleted for ppa2 is treated with okadaic acid, cell size is reduced further to that of wee1-50 mutant strain or overexpressing the cdc25+ gene product, suggesting functional relationship of ppa2 with the cdc25 tyrosine phosphatase and/or the wee1 kinase in cell cycle control.","authors":"Kinoshita N, Yamano H, Niwa H, Yoshida T, Yanagida M","authors_abbrev":"Kinoshita N et al.","pubmed_publication_date":"Jun 1993","pubmed_entrez_date":"1993-06-01","publication_year":"1993","canto_session_key":"635732abd73e57de","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-21 08:32:59","canto_approved_date":"2024-02-22 10:56:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-21 08:32:47","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16H5.07c","SPBC26H8.10","SPAC24H6.05","SPCC31H12.05c","SPCC18B5.03","SPAC823.15","SPBC776.02c","SPCC1739.12","SPBC11B10.09","SPCC736.14"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2016-06-21"},{"uniquename":"PMID:22182414","title":"Small heat-shock protein Hsp9 has dual functions in stress adaptation and stress-induced G2-M checkpoint regulation via Cdc25 inactivation in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2012 Jan 06;417(1):613-8","abstract":"The small heat-shock protein Hsp9 from Schizosaccharomyces pombe was previously reported to be a homologue of Saccharomyces cerevisiae HSP12. Although Hsp9 is expressed in response to heat shock and nutritional limitation, its function is still not completely understood. Here, we explored the biological function of Hsp9 in S. pombe. The hsp9 gene might play a role in stress adaptation; hsp9 deletion caused heat sensitivity and overexpression induced heat tolerance. In addition, Hsp9 also contribute to cell cycle regulation in the nucleus. Δhsp9 cells grew more quickly and were shorter in length than wild-type cells. Moreover, Δhsp9 cells did not achieve checkpoint arrest under stress conditions, leading to cell death, and exhibited a short doubling time and short G2 phase. Overexpression of hsp9 induced cell cycle delay, increased the population of G2 phase cells, and rescued the phenotypes of cdc2-33, cdc25-22, Δrad24, and Δrad25 mutants, suggesting that Hsp9 probably regulates Cdc2 phosphorylation by modulating the Cdc25 activity. Indeed, immunoprecipitation experiments revealed that Hsp9 is associated with 14-3-3 and Cdc25. In Δhsp9 cells, the association of 14-3-3 with Cdc25 was weakened and Cdc2 phosphorylaton was reduced. Together, our data suggest that Hsp9 has dual functions in stress adaptation and regulating a G2-M checkpoint by the Cdc25 inactivation; this differs from S. cerevisiae HSP12, which maintains cell membrane stability under stress conditions.","doi":"10.1016/j.bbrc.2011.12.017","authors":"Ahn J, Won M, Choi JH, Kyun ML, Cho HS, Park HM, Kang CM, Chung KS","authors_abbrev":"Ahn J et al.","pubmed_publication_date":"06 Jan 2012","pubmed_entrez_date":"2011-12-21","publication_year":"2012","canto_session_key":"069c6c97566e7bcc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-07 16:58:48","canto_approved_date":"2021-02-18 14:17:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-13 07:12:34","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPCC18B5.03","SPBC11B10.09","SPAC17A2.13c","SPAC24H6.05","SPAP8A3.04c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-02-07"},{"uniquename":"EMBL:AU013255","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9455213","title":"[Schizosaccharomyces pombe].","citation":"Tanpakushitsu Kakusan Koso 1997 Dec;42(17 Suppl):2920-6","abstract":"","authors":"Morimyo M, Mita K, Higashi T, Sugaya K, Hongo E, Ajimura M, Sasanuma S, Nohata J, Kimura T, Inoue H, Ishihara Y, Koike S","authors_abbrev":"Morimyo M et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1998-02-10","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8585995","title":"Yeast and mammalian replication intermediates migrate similarly in two-dimensional gels.","citation":"Chromosoma 1995 Nov;104(2):92-102","abstract":"In the budding yeast, Saccharomyces cerevisiae, DNA replication initiates at specific, discrete chromosomal locations. At each initiation site, a single small replication bubble is generated, which subsequently expands at Y-like replication forks. We wanted to know whether other eukaryotic organisms utilize similar initiation mechanisms. For this purpose, replication intermediates (RIs) from three different organisms (Schizosaccharomyces pombe, Chinese hamster and human) were mixed individually with RIs from S. cerevisiae and then subjected to two-dimensional (2D) gel electrophoresis under conditions known to resolve molecules having different structures. All of the RIs detected by the hybridization probes we used for each organism migrated nearly identically to specific RIs of similar size from S. cerevisiae, implying that the detected RIs from all the studied organisms have very similar structures and may therefore employ the same basic initiation mechanism.","authors":"Brun C, Dijkwel PA, Little RD, Hamlin JL, Schildkraut CL, Huberman JA","authors_abbrev":"Brun C et al.","pubmed_publication_date":"Nov 1995","pubmed_entrez_date":"1995-11-01","publication_year":"1995","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19168987","title":"Essential roles of Snf21, a Swi2/Snf2 family chromatin remodeler, in fission yeast mitosis.","citation":"Genes Genet Syst 2008 Oct;83(5):361-72","abstract":"ATP-dependent chromatin remodelers (ADCRs) convert local chromatin structure into both transcriptional active and repressive state. Recent studies have revealed that ADCRs play diverse regulatory roles in chromosomal events such as DNA repair and recombination. Here we have newly identified a fission yeast gene encoding a Swi2/Snf2 family ADCR. The amino acid sequence of this gene, snf21(+), implies that Snf21 is a fission yeast orthologue of the budding yeast Sth1, the catalytic core of the RSC chromatin remodeling complex. The snf21(+) gene product is a nuclear protein essential to cell viability: the null mutant cells stop growing after several rounds of cell divisions. A temperature sensitive allele of snf21(+), snf21-36 exhibits at non-permissive temperature (34 degrees C) a cell cycle arrest at G2-M phase and defects in chromosome segregation, thereby causing cell elongation, lack of cell growth, and death of some cell population. snf21-36 shows thiabendazole (TBZ) sensitivity even at permissive temperature (25 degrees C). The TBZ sensitivity becomes severer as snf21-36 is combined with the deletion of a centromere-localized Mad2 spindle checkpoint protein. The cell cycle arrest phenotype at 34 degrees C cannot be rescued by the mad2(+) deletion, although it is substantially alleviated at 30 degrees C in mad2Delta. These data suggest that Snf21 plays an essential role in mitosis possibly functioning in centromeric chromatin.","authors":"Yamada K, Hirota K, Mizuno K, Shibata T, Ohta K","authors_abbrev":"Yamada K et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2009-01-27","publication_year":"2008","canto_session_key":"0e60aa30681d4ab9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-02 17:08:16","canto_approved_date":"2023-02-12 21:02:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-02 17:08:09","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1250.01","SPBC20F10.06"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-03-02"},{"uniquename":"PMID:18304578","title":"The 3' ends of mature transcripts are generated by a processosome complex in fission yeast mitochondria.","citation":"J Mol Biol 2008 Apr 04;377(4):1024-37","abstract":"In this article, we report on the genetic analysis of the Schizosaccharomyces pombe open reading frames SPCC1322.01 and SPAC637.11, respectively, which encode proteins that are similar to the exoribonuclease Dss1p and the RNA helicase Suv3p, respectively, forming the mitochondrial degradosome of Saccharomyces cerevisiae. While the helicase Suv3p is exchangeable between S. cerevisiae and S. pombe, the functions of Dss1p and the putative fission yeast RNase protein are specific for each species. Unlike S. cerevisiae mutants lacking a functional degradosome, the major defect of fission yeast knock-out strains is their inability to perform downstream processing of transcripts. In addition, the lack of pah1 results in instability of mitochondrial RNA ends. Overexpression of par1 and pah1 has no significant effect on the steady-state levels of mitochondrial RNAs. The Pet127p-stimulated RNA degradation activity is independent of Par1p/Pah1p in fission yeast mitochondria. The results presented herein indicate that both fission yeast proteins play only a minor role (if at all) in mitochondrial RNA degradation. We assume that the RNA-degrading function was taken over by other enzymes in fission yeast mitochondria, while the former degradosome proteins were recruited to new cellular pathways, for example, RNA processing in fission yeast (as discussed in this article) or mitochondrial DNA replication, apoptosis, or chromatin maintenance in eukaryotes, during evolution.","doi":"10.1016/j.jmb.2008.01.038","authors":"Hoffmann B, Nickel J, Speer F, Schafer B","authors_abbrev":"Hoffmann B et al.","pubmed_publication_date":"04 Apr 2008","pubmed_entrez_date":"2008-02-29","publication_year":"2008","canto_session_key":"846ae2deaee419eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-07 17:09:23","canto_approved_date":"2025-05-30 09:26:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-29 17:44:29","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC637.11","SPCC1322.01","SPCC1183.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-03-07"},{"uniquename":"PMID:21960007","title":"Analysis of substrate specificity of Schizosaccharomyces pombe Mag1 alkylpurine DNA glycosylase.","citation":"EMBO Rep 2011 Dec 01;12(12):1286-92","abstract":"DNA glycosylases specialized for the repair of alkylation damage must identify, with fine specificity, a diverse array of subtle modifications within DNA. The current mechanism involves damage sensing through interrogation of the DNA duplex, followed by more specific recognition of the target base inside the active site pocket. To better understand the physical basis for alkylpurine detection, we determined the crystal structure of Schizosaccharomyces pombe Mag1 (spMag1) in complex with DNA and performed a mutational analysis of spMag1 and the close homologue from Saccharomyces cerevisiae (scMag). Despite strong homology, spMag1 and scMag differ in substrate specificity and cellular alkylation sensitivity, although the enzymological basis for their functional differences is unknown. We show that Mag preference for 1,N(6)-ethenoadenine (ɛA) is influenced by a minor groove-interrogating residue more than the composition of the nucleobase-binding pocket. Exchanging this residue between Mag proteins swapped their ɛA activities, providing evidence that residues outside the extrahelical base-binding pocket have a role in identification of a particular modification in addition to sensing damage.","doi":"10.1038/embor.2011.189","authors":"Adhikary S, Eichman BF","authors_abbrev":"Adhikary S et al.","pubmed_publication_date":"01 Dec 2011","pubmed_entrez_date":"2011-10-01","publication_year":"2011","canto_session_key":"bcb8d4f171dffc70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-11-23 18:17:01","canto_approved_date":"2025-02-26 22:13:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-22 20:27:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB24D3.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-11-23","pdb_entries":[{"pdb_id":"3s6i","gene_chains":[{"gene_uniquename":"SPAPB24D3.04c","chain":"A/D","position":"1-228"}],"title":"Schizosaccaromyces pombe 3-methyladenine DNA glycosylase (Mag1) in complex with abasic-DNA.","entry_authors":"Adhikary S,Eichman BF","entry_authors_abbrev":"Adhikary S et al.","reference_uniquename":"PMID:21960007","experimental_method":"X-ray","resolution":"2.28"}]},{"uniquename":"PMID:24352239","title":"Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification.","citation":"Nature 2014 Jan 23;505(7484):564-8","abstract":"Nucleosomes are decorated with numerous post-translational modifications capable of influencing many DNA processes. Here we describe a new class of histone modification, methylation of glutamine, occurring on yeast histone H2A at position 105 (Q105) and human H2A at Q104. We identify Nop1 as the methyltransferase in yeast and demonstrate that fibrillarin is the orthologue enzyme in human cells. Glutamine methylation of H2A is restricted to the nucleolus. Global analysis in yeast, using an H2AQ105me-specific antibody, shows that this modification is exclusively enriched over the 35S ribosomal DNA transcriptional unit. We show that the Q105 residue is part of the binding site for the histone chaperone FACT (facilitator of chromatin transcription) complex. Methylation of Q105 or its substitution to alanine disrupts binding to FACT in vitro. A yeast strain mutated at Q105 shows reduced histone incorporation and increased transcription at the ribosomal DNA locus. These features are phenocopied by mutations in FACT complex components. Together these data identify glutamine methylation of H2A as the first histone epigenetic mark dedicated to a specific RNA polymerase and define its function as a regulator of FACT interaction with nucleosomes.","doi":"10.1038/nature12819","authors":"Tessarz P, Santos-Rosa H, Robson SC, Sylvestersen KB, Nelson CJ, Nielsen ML, Kouzarides T","authors_abbrev":"Tessarz P et al.","pubmed_publication_date":"23 Jan 2014","pubmed_entrez_date":"2013-12-20","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.08c","SPAC19G12.06c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:30223456","title":"Effect of  Lachancea thermotolerans  on the Formation of Polymeric Pigments during Sequential Fermentation with  Schizosaccharosmyces pombe  and  Saccharomyces cerevisiae .","citation":"Molecules 2018 Sep 14;23(9)","abstract":"Anthocyanins in red grape musts may evolve during the winemaking process and wine aging for several different reasons; colour stability and evolution is a complex process that may depend on grape variety, winemaking technology, fermentative yeast selection, co-pigmentation phenomena and polymerization. The condensation of flavanols with anthocyanins may occur either with the flavylium ion or with the hemiacetal formation in order to produce oligomers and polymers. The kinetics of the reaction are enhanced by the presence of metabolic acetaldehyde, promoting the formation of pyranoanthocyanin-type dimers or flavanol-ethyl-anthocyanin structures. The experimental design carried out using white must corrected with the addition of malvidin-3- O -glucoside and flavanols, suggests that non- Saccharomyces  yeasts are able to provide increased levels of colour intensity and larger polymeric pigment ratios and polymerization indexes. The selection of non- Saccharomyces  genera, in particular  Lachancea thermotolerans  and  Schizosaccharomyces pombe  in sequential fermentation, have provided experimental wines with increased fruity esters, as well as producing wines with potential pigment compositions, even though there is an important reduction of total anthocyanins.","doi":"10.3390/molecules23092353","authors":"Escott C, Morata A, Ricardo-da-Silva JM, Callejo MJ, González MDC, Suarez-Lepe JA","authors_abbrev":"Escott C et al.","pubmed_publication_date":"14 Sep 2018","pubmed_entrez_date":"2018-09-19","publication_year":"2018","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2018-09-19 10:20:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5148013","title":"Growth and changes in pool and macromolecular components of Schizosaccharomyces pombe during the cell cycle.","citation":"J Cell Sci 1971 Nov;9(3):701-17","abstract":"","authors":"Stebbing N","authors_abbrev":"Stebbing N","pubmed_publication_date":"Nov 1971","pubmed_entrez_date":"1971-11-01","publication_year":"1971","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15147268","title":"Molecular interactions of fission yeast Skp1 and its role in the DNA damage checkpoint.","citation":"Genes Cells 2004 May;9(5):367-82","abstract":"Skp1 is a central component of the E3 ubiquitin ligase SCF (Skp1-Cullin-1-F-box). It forms an adapter bridge between Cullin-1 and the substrate-determining component, the F-box protein. In order to establish the role of Skp1, a temperature sensitive (ts) screen was carried out using mutagenic PCR (polymerase chain reaction) and 9 independent ts mutants were isolated. Mapping the mutated residues on the 3-D structure of human Skp1 suggested that the mutants would be compromised in binding to F-box proteins but not Cullin-1 (Pcu1). In order to assess the binding properties of ts Skp1, 12 F-box proteins and Pcu1 were epitope-tagged, and co-immunoprecipitation performed. This systematic analysis showed that ts Skp1 retains binding to Pcu1. However, binding to three specific F-box proteins, essential Pof1, Pof3 involved in maintaining genome integrity, and nonessential Pof10, was reduced. skp1ts cells exhibit a G2 cell cycle delay, which is attributable to activation of the DNA damage checkpoint. Intriguingly, contrary to pof3 mutants, in which this checkpoint is required for survival, checkpoint abrogation in skp1(ts) suppresses a G2 delay and furthermore almost rescues the ts phenotype. The activation mechanism of the DNA damage checkpoint therefore differs between pof3Delta and skp1(ts), implicating a novel role for Skp1 in the checkpoint-signalling cascade.","authors":"Lehmann A, Katayama S, Harrison C, Dhut S, Kitamura K, McDonald N, Toda T","authors_abbrev":"Lehmann A et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-05-19","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC409.05","SPBC3H7.06c","SPAC29E6.01","SPAC57A10.05c","SPBC56F2.01","SPBC1718.01","SPBC1703.06","SPBC25B2.11","SPBC216.05","SPCC1259.13","SPCC1827.08c","SPAC17G6.17","SPBC29A3.08","SPBC336.01","SPCC338.16","SPBC1271.01c","SPAC17G6.12","SPAC6F6.02c"],"gene_count":18,"ltp_gene_count":18},{"uniquename":"PMID:19189958","title":"Fission yeast rgf2p is a rho1p guanine nucleotide exchange factor required for spore wall maturation and for the maintenance of cell integrity in the absence of rgf1p.","citation":"Genetics 2009 Apr;181(4):1321-34","abstract":"Schizosaccharomyces pombe Rho1p is essential, directly activates beta-1,3-glucan synthase, and participates in the regulation of morphogenesis. In S. pombe, Rho1p is activated by at least three guanine nucleotide exchange factors (GEFs): Rgf1p, Rgf2p, and Rgf3p. In this study we show that Rgf2p is a Rho1p GEF required for sporulation. The rgf2+ deletion did not affect forespore membrane formation and the nuclei were encapsulated properly. However, the mutant ascospores appeared dark and immature. The rgf2Delta zygotes were not able to release the ascospores spontaneously, and the germination efficiency was greatly reduced compared to wild-type (wt) spores. This phenotype resembles that of the mutants in bgs2+, which encodes a sporulation-specific glucan synthase subunit. In fact, glucan synthase activity was diminished in sporulating rgf2Delta diploids. Rgf2p also plays a role in beta-glucan biosynthesis during vegetative growth. Overexpression of rgf2+ specifically increased GTP-bound Rho1p, caused changes in cell morphology, and elicited an increase in beta-1,3-glucan synthase activity. Moreover, the simultaneous disruption of rgf1+ and rgf2+ was lethal and both Rgf1p and Rgf2p were able to partially substitute for each other. Our results suggest that Rgf1p and Rgf2p are alternative GEFs with an essential overlapping function in Rho1p activation during vegetative growth.","doi":"10.1534/genetics.108.094839","authors":"García P, García I, Marcos F, de Garibay GR, Sánchez Y","authors_abbrev":"García P et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-02-05","publication_year":"2009","canto_session_key":"c3eceb1486a6bc53","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-06-14 14:22:40","canto_approved_date":"2025-12-16 01:37:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-08 15:14:31","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":46,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.06","SPCC645.07","SPCC645.06c","SPAC24C9.07c","SPAC1F7.04"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2022-06-14"},{"uniquename":"PMID:22629372","title":"Conserved Orb6 phosphorylation sites are essential for polarized cell growth in Schizosaccharomyces pombe.","citation":"PLoS One 2012;7(5):e37221","abstract":"The Ndr-related Orb6 kinase is a key regulator of polarized cell growth in fission yeast, however the mechanism of Orb6 activation is unclear. Activation of other Ndr kinases involves both autophosphorylation and phosphorylation by an upstream kinase. Previous reports suggest that the Nak1 kinase functions upstream from Orb6. Supporting this model, we show that HA-Orb6 overexpression partially restored cell polarity in nak1 ts cells. We also demonstrated by coimmunoprecipitation and in vitro binding assays that Nak1 and Orb6 physically interact, and that the Nak1 C-terminal region is required for Nak1/Orb6 complex formation in vivo. However, results from in vitro kinase assays did not show phosphorylation of recombinant Orb6 by HA-Nak1, suggesting that Orb6 activation may not involve direct phosphorylation by Nak1. To investigate the role of Orb6 phosphorylation and activity, we substituted Ala at the ATP-binding and conserved phosphorylation sites. Overexpression of kinase-dead HA-Orb6(K122A) in wild-type cells resulted in a loss of cell polarity, suggesting that it has a dominant-negative effect, and it failed to rescue the polarity defect of nak1 or orb6 ts mutants. Recombinant GST-Orb6(S291A) did not autophosphorylate in vitro suggesting that Ser291 is the primary autophosphorylation site. HA-Orb6(S291A) overexpression only partially rescued the orb6 polarity defect and failed to rescue the nak1 defect, suggesting that autophosphorylation is important for Orb6 function. GST-Orb6(T456A) autophosphorylated in vitro, indicating that the conserved phosphorylation site at Thr456 is not essential for kinase activity. However, HA-Orb6(T456A) overexpression had similar effects as overexpressing kinase-dead HA-Orb6(K122A), suggesting that Thr456 is essential for Orb6 function in vivo. Also, we found that both phosphorylation site mutations impaired the ability of Myc-Nak1 to coimmunoprecipitate with HA-Orb6. Together, our results suggest a model whereby autophosphorylation of Ser291 and phosphorylation of Thr456 by an upstream kinase promote Nak1/Orb6 complex formation and Orb6 activation.","doi":"10.1371/journal.pone.0037221","authors":"Liu G, Young D","authors_abbrev":"Liu G et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-05-26","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC17F3.02","SPAC821.12"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11124699","title":"The Schizosaccharomyces pombe GPI8 gene complements a Saccharomyces cerevisiae GPI8 anchoring mutant.","citation":"Yeast 2001 Jan 15;18(1):33-9","abstract":"The final step in glycosylphosphatidylinositol (GPI) anchoring of cell surface proteins consists of a transamidation reaction, in which preassembled GPI donors are substituted for C-terminal signal sequences in nascent polypeptides. The Saccharomyces cerevisiae GPI8 gene (ScGPI8) encodes a protein which is involved in the GPI transamidation reaction. We have cloned and isolated the Schizosaccharomyces pombe GPI8 homologous gene (SpGPI8). The SpGPI8 gene encodes a protein of 411 amino acids with a calculated molecular weight of about 47 kDa. It shows 53.5% identity with the ScGPI8 and complements a S. cerevisiae GPI8 anchoring mutant.","authors":"Shams-Eldin H, Azzouz N, Eckert V, Blaschke T, Kedees MH, Hübel A, Schwarz RT","authors_abbrev":"Shams-Eldin H et al.","pubmed_publication_date":"15 Jan 2001","pubmed_entrez_date":"2000-12-22","publication_year":"2001","canto_session_key":"89ccdbbf847ae4fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-10 17:12:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-10 17:12:42","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-10"},{"uniquename":"PMID:1502179","title":"Simple derivation of TFIID-dependent RNA polymerase II transcription systems from Schizosaccharomyces pombe and other organisms, and factors required for transcriptional activation.","citation":"Proc Natl Acad Sci U S A 1992 Aug 15;89(16):7659-63","abstract":"Resolution of whole cell extract through two chromatographic steps yields a single protein fraction requiring only the addition of TFIID for the initiation of transcription at RNA polymerase II promoters. This approach allows the convenient generation of RNA polymerase II transcription systems from Saccharomyces cerevisiae, human lymphocytes, and Schizosaccharomyces pombe. TFIIDs from all three organisms are interchangeable among all three systems. The S. cerevisiae and Sch. pombe systems support effects of acidic activator proteins, provided a further protein fraction from S. cerevisiae is supplied. This further fraction is distinct from the mediator of transcriptional activation described previously and represents a second component in addition to general initiation factors that may facilitate a response to acidic activators.","authors":"Flanagan PM, Kelleher RJ, Tschochner H, Sayre MH, Kornberg RD","authors_abbrev":"Flanagan PM et al.","pubmed_publication_date":"15 Aug 1992","pubmed_entrez_date":"1992-08-15","publication_year":"1992","canto_session_key":"d861f5ae79ef76eb","canto_annotation_status":"APPROVED","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_approved_date":"2014-11-20 10:51:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-20 10:51:14","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-11-20"},{"uniquename":"PMID:9753423","title":"Meiotic telomeres: a matchmaker for homologous chromosomes.","citation":"Genes Cells 1998 Jul;3(7):405-13","abstract":"Telomeres, with their special structures and special schemes of synthesis, are essential for protecting the ends of eukaryotic linear chromosomes during cell proliferation. In addition to this basic function, the meiosis-specific functions of telomeres have long been inferred from the cytological observations of characteristic chromosome configurations in meiotic prophase. Recent studies in the fission yeast Schizosaccharomyces pombe have provided deeper insights into the role of meiotic telomeres in the pairing of homologous chromosomes. Here I have summarized our current understanding of the meiotic behaviour of telomeres in S. pombe, and discuss the role of telomeres in meiosis.","authors":"Hiraoka Y","authors_abbrev":"Hiraoka Y","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-09-30","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24936648","title":"Stressed yeast paint a picture of dorian gray.","citation":"PLoS Biol 2014 Jun;12(6):e1001885","abstract":"","doi":"10.1371/journal.pbio.1001885","authors":"Roberts RG","authors_abbrev":"Roberts RG","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-06-18","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-08-07 00:27:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12925774","title":"Schizosacchromyces pombe Dpb2 binds to origin DNA early in S phase and is required for chromosomal DNA replication.","citation":"Mol Biol Cell 2003 Aug;14(8):3427-36","abstract":"Genetic evidence suggests that DNA polymerase epsilon (Pol epsilon) has a noncatalytic essential role during the early stages of DNA replication initiation. Herein, we report the cloning and characterization of the second largest subunit of Pol epsilon in fission yeast, called Dpb2. We demonstrate that Dpb2 is essential for cell viability and that a temperature-sensitive mutant of dpb2 arrests with a 1C DNA content, suggesting that Dpb2 is required for initiation of DNA replication. Using a chromatin immunoprecipitation assay, we show that Dpb2, binds preferentially to origin DNA at the beginning of S phase. We also show that the C terminus of Pol epsilon associates with origin DNA at the same time as Dpb2. We conclude that Dpb2 is an essential protein required for an early step in DNA replication. We propose that the primary function of Dpb2 is to facilitate assembly of the replicative complex at the start of S phase. These conclusions are based on the novel cell cycle arrest phenotype of the dpb2 mutant, on the previously uncharacterized binding of Dpb2 to replication origins, and on the observation that the essential function of Pol epsilon is not dependent on its DNA synthesis activity.","authors":"Feng W, Rodriguez-Menocal L, Tolun G, D'Urso G","authors_abbrev":"Feng W et al.","pubmed_publication_date":"Aug 2003","pubmed_entrez_date":"2003-08-20","publication_year":"2003","canto_session_key":"ff8c38cbaa71124d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-11-06 14:27:16","canto_approved_date":"2020-06-19 12:29:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-06 14:27:12","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP8B7.14c","SPBC336.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-06"},{"uniquename":"PMID:40526720","title":"The oncogene SLC35F2 is a high-specificity transporter for the micronutrients queuine and queuosine.","citation":"Proc Natl Acad Sci U S A 2025 Jun 24;122(25):e2425364122","abstract":"The nucleobase queuine (q) and its nucleoside queuosine (Q) are micronutrients derived from bacteria that are acquired from the gut microbiome and/or diet in humans. Following cellular uptake, Q is incorporated at the wobble base (position 34) of tRNAs that decode histidine, tyrosine, aspartate, and asparagine codons, which is important for efficient translation. Early studies suggested that cytosolic uptake of queuine is mediated by a selective transporter that is regulated by mitogenic signals, but the identity of this transporter has remained elusive. Here, through a cross-species bioinformatic search and genetic validation, we have identified the solute carrier family member SLC35F2 as a unique transporter for both queuine and queuosine in  Schizosaccharomyces pombe  and  Trypanosoma brucei . Furthermore, gene disruption in human HeLa cells revealed that SLC35F2 is the sole transporter for queuosine (K m  174 nM) and a high-affinity transporter for the queuine nucleobase (K m  67 nM), with the additional presence of second low-affinity queuine transporter (K m  259 nM). Ectopic expression of labeled SLC35F2 reveals localization to the cell membrane and Golgi apparatus via immunofluorescence. Competition uptake studies show that SLC35F2 is not a general transporter for other canonical ribonucleobases or ribonucleosides but selectively imports q and Q. The identification of SLC35F2, an oncogene, as the transporter of both q and Q advances our understanding of how intracellular levels of queuine and queuosine are regulated and how their deficiency contributes to a variety of pathophysiological conditions, including neurological disorders and cancer.","doi":"10.1073/pnas.2425364122","authors":"Burtnyak L, Yuan Y, Stojek E, Pan X, Gunaratne L, Silveira d'Almeida G, Fergus C, Martinelli M, J Reed C, Fernandez J, Patel BI, Marquez I, Ehrenhofer-Murray AE, Swairjo MA, Alfonzo JD, Green BD, Kelly VP, de Crécy-Lagard V","authors_abbrev":"Burtnyak L et al.","pubmed_publication_date":"24 Jun 2025","pubmed_entrez_date":"2025-06-17","publication_year":"2025","canto_session_key":"0f1e77edf7ff06af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-02-06 19:30:42","canto_approved_date":"2026-02-06 19:30:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-02-06 19:30:29","canto_added_date":"2025-06-18 23:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2026-02-06"},{"uniquename":"PMID:28572514","title":"Cell-surface copper transporters and superoxide dismutase 1 are essential for outgrowth during fungal spore germination.","citation":"J Biol Chem 2017 Jul 14;292(28):11896-11914","abstract":"During fungal spore germination, a resting spore returns to a conventional mode of cell division and resumes vegetative growth, but the requirements for spore germination are incompletely understood. Here, we show that copper is essential for spore germination in  Schizosaccharomyces pombe  Germinating spores develop a single germ tube that emerges from the outer spore wall in a process called outgrowth. Under low-copper conditions, the copper transporters Ctr4 and Ctr5 are maximally expressed at the onset of outgrowth. In the case of Ctr6, its expression is broader, taking place before and during outgrowth. Spores lacking Ctr4, Ctr5, and the copper sensor Cuf1 exhibit complete germination arrest at outgrowth. In contrast,  ctr6  deletion only partially interferes with formation of outgrowing spores. At outgrowth, Ctr4-GFP and Ctr5-Cherry first co-localize at the spore contour, followed by re-location to a middle peripheral spore region. Subsequently, they move away from the spore body to occupy the periphery of the nascent cell. After breaking of spore dormancy, Ctr6 localizes to the vacuole membranes that are enriched in the spore body relative to the germ tube. Using a copper-binding tracker, results showed that labile copper is preferentially localized to the spore body. Further analysis showed that Ctr4 and Ctr6 are required for copper-dependent activation of the superoxide dismutase 1 (SOD1) during spore germination. This activation is critical because the loss of SOD1 activity blocked spore germination at outgrowth. Taken together, these results indicate that cell-surface copper transporters and SOD1 are required for completion of the spore germination program.","doi":"10.1074/jbc.M117.794677","authors":"Plante S, Normant V, Ramos-Torres KM, Labbé S","authors_abbrev":"Plante S et al.","pubmed_publication_date":"14 Jul 2017","pubmed_entrez_date":"2017-06-03","publication_year":"2017","canto_session_key":"bc974ef58d58c8aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Samuel Plante","canto_first_approved_date":"2017-09-14 15:09:24","canto_approved_date":"2024-06-26 10:49:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-14 15:09:17","canto_added_date":"2017-06-04 00:15:15","annotation_curators":[{"name":"Samuel Plante","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.10c","SPBC23G7.16","SPCC1393.10","SPAC31A2.11c","SPAC1142.05","SPAC2E1P3.04"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-09-14"},{"uniquename":"PMID:41903918","title":"A fission yeast-based platform for nematode PDE inhibitor discovery.","citation":"Cell Signal 2026 Mar 26;:112508","abstract":"Class I cyclic nucleotide phosphodiesterases (PDEs) form a family of enzymes that hydrolyze the signaling molecules cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP). Highly potent and selective inhibitors of mammalian PDEs have been developed, demonstrating that this enzyme family is eminently druggable. The genomes of the free-living nematode and model organism Caenorhabditis elegans and those of related parasitic nematodes possess six PDE genes representing six of the eleven PDE families found in mammals. Here, we expressed the C. elegans PDEs or their catalytic domains in the fission yeast Schizosaccharomyces pombe and screened a collection of small molecule inhibitors of mammalian PDEs obtained from our previous high throughput screens for ones with activity against one or more C. elegans PDEs. Consistent with an earlier study, the C. elegans PDE-4 enzyme is relatively insensitive to mammalian PDE4 inhibitors such as Rolipram, as are PDE-4 enzymes from three parasitic nematodes. Much of this is due to a single amino acid difference between mammalian PDE4s and nematode PDE4, as replacing arginine 580 with threonine in C. elegans PDE-4 restores substantial sensitivity to Rolipram. Finally, several of the most effective C. elegans PDE inhibitors were tested for their impact on C. elegans growth and fertility, two of which displayed toxic effects on C. elegans viability and fecundity using two different assessment methods, while a third showed a significant effect on fecundity. The strategy described herein offers an approach for discovery of novel anthelmintic and nematicidal compounds targeting parasitic nematode PDEs.","doi":"10.1016/j.cellsig.2026.112508","authors":"Bibeau S, Chen N, Sutoris H, Ly J, Eberhard J, Hubbell SM, Banda E, Povh E, Anindya CS, Berwanger MR, Sinise SE, Zhang X, Morken JP, Galande KK, Cote RH, Dranchak PK, Inglese J, Hoffman CS","authors_abbrev":"Bibeau S et al.","pubmed_publication_date":"26 Mar 2026","pubmed_entrez_date":"2026-03-28","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-03-29 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17543869","title":"Polarity determinants Tea1p, Tea4p, and Pom1p inhibit division-septum assembly at cell ends in fission yeast.","citation":"Dev Cell 2007 Jun;12(6):987-96","abstract":"Correct positioning of the cell-division plane is crucial for cell function in all organisms. The fission yeast Schizosaccharomyces pombe divides by utilizing an actomyosin-based contractile ring and is an attractive model for the study of cytokinesis. The metazoan anillin-related protein Mid1p stimulates medial assembly of the division septum by recruiting actomyosin-ring components to the medial cortex. Here, we describe an inhibitory mechanism, involving the cell-end-localized polarity determinants Tea1p, Tea4p/Wsh3p, and Pom1p (tip complex), which prevents division-septum assembly at the cell ends. While Mid1p and the tip complex are dispensable for cell viability, their simultaneous loss leads to lethality. The FER/CIP homology protein Cdc15p, which organizes the actomyosin ring and cell membranes during cytokinesis, is a candidate for regulation by the tip complex. Since dual regulation of division-site placement is also seen in nematodes, such regulation might be a general feature of eukaryotic cytokinesis.","authors":"Huang Y, Chew TG, Ge W, Balasubramanian MK","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-06-05","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9790975","title":"A mutation Ser213/Asn in the hexokinase 1 from Schizosaccharomyces pombe increases its affinity for glucose.","citation":"Biochem Biophys Res Commun 1998 Oct 29;251(3):714-9","abstract":"Alignment of amino acids of the region implicated in glucose binding from a series of hexokinases showed that Schizosaccharomyces pombe hexokinase 1 had a Ser residue in a place where all other kinases had an Asn. We changed an AGT codon to AAT to place an Asn in the Ser213 position. This mutation decreased Km for glucose from 9.4 mM to 1.6 mM and the ratio Vmax (Fructose)/Vmax (Glucose) from 5 to 2.5. Also the Km for 2-deoxyglucose decreased from 2.7 mM to 0.8 mM. A mutation in the similar position of S. pombe hexokinase 2 (Asn196/Ser) increased the Km for glucose from 0.16 mM to 0.56 mM. Fermentation of glucose is not detectable in a S. pombe mutant with only hexokinase 1 activity but expression of the hxk1(S213/N) gene conferred ability to ferment the sugar. While the mutated hexokinase 1 partially mimicked S. cerevisiae hexokinase II in catabolite repression of invertase, the wild type one could not substitute for it.","authors":"Petit T, Herrero P, Gancedo C","authors_abbrev":"Petit T et al.","pubmed_publication_date":"29 Oct 1998","pubmed_entrez_date":"1998-10-29","publication_year":"1998","canto_session_key":"19d14958354d3dcb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-06-08 08:55:06","canto_approved_date":"2025-01-14 08:00:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-07 09:46:45","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.07c","SPAC24H6.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-06-08"},{"uniquename":"PMID:9504913","title":"The identification of cDNAs that affect the mitosis-to-interphase transition in Schizosaccharomyces pombe, including sbp1, which encodes a spi1p-GTP-binding protein.","citation":"Genetics 1998 Feb;148(2):645-56","abstract":"Perturbations of the spi1p GTPase system in fission yeast, caused by mutation or overexpression of several regulatory proteins, result in a unique terminal phenotype that includes condensed chromosomes, a wide medial septum, and a fragmented nuclear envelope. To identify potential regulators or targets of the spi1p GTPase system, a screen for cDNAs whose overexpression results in this terminal phenotype was conducted, and seven clones that represent three genes, named med1, med2, and med3 (mitotic exit defect), were identified. Their genetic interaction with the spi1p GTPase system was established by showing that the spi1p guanine nucleotide exchange factor mutant pim1-d1ts was hypersensitive to their overexpression. med1 encodes a homologue of the human Ran-binding protein, RanBP1, and has been renamed sbp1 (spi1-binding protein). sbp1p binds to spi1p-GTP and costimulates the GTPase-activating protein (GAP)-catalyzed GTPase activity. Cells in which sbp1p is depleted or overproduced phenocopy cells in which the balance between spi1p-GTP and spi1p-GDP is perturbed by other means. Therefore, sbp1p mediates and/or regulates the essential functions of the spi1p GTPase system. med2 and med3 encode novel fission yeast proteins that, based on our phenotypic analyses, are likely to identify additional regulators or effectors of the spi1p GTPase system.","authors":"He X, Hayashi N, Walcott NG, Azuma Y, Patterson TE, Bischoff FR, Nishimoto T, Sazer S","authors_abbrev":"He X et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-03-20","publication_year":"1998","canto_session_key":"cd15abc2b56fbe3f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-01-23 17:27:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-01 14:48:24","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.07","SPBC1289.03c","SPBC557.03c","SPBC1773.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-09-01"},{"uniquename":"PMID:40645175","title":"Mosaic evolution of clathrin-mediated endocytosis in fungi.","citation":"Curr Biol 2025 Aug 04;35(15):3674-3686.e4","abstract":"Clathrin-mediated endocytosis is an ancient eukaryotic trafficking pathway, which transports plasma membrane and associated cargo into the cell and is involved in numerous cell- and tissue-level processes. Cargo selection and clathrin-coated vesicle formation are mediated by over 60 proteins that assemble in a regular and sequential manner at the plasma membrane. Decades of endocytosis studies have followed the tenet that uncovering the conserved core molecular mechanisms is sufficient to understand a cellular process. However, this approach also revealed a number of cell-type- or species-related variations that challenge the notion of a universally conserved, core mechanism. In this paper, we refocus on the endocytic diversity to understand how evolution shapes endocytic mechanisms. We define a comparative evolutionary cell biology approach that uses dikarya fungi as a model clade and live-cell fluorescence microscopy to study endocytosis dynamics in three species: Saccharomyces cerevisiae, Schizosaccharomyces pombe, and Ustilago maydis. Our results quantitatively define several phenotypic differences between the species. We uncover differences that impact the endocytic early phase, the protein assembly order, actin regulation, membrane invagination, and scission. These findings demonstrate a mosaic evolution of endocytic traits, suggesting ancestral states and directions of change. We also investigate phenotypic plasticity and robustness against environmental conditions. Lastly, we demonstrate that relatively minor evolutionary changes can majorly impact endocytic phenotypes. These findings promote an appreciation of endocytic variation as not auxiliary, but vital to the mechanistic understanding of this conserved cellular pathway.","doi":"10.1016/j.cub.2025.06.052","authors":"Picco A, Toret CP, Rivier-Cordey AS, Kaksonen M","authors_abbrev":"Picco A et al.","pubmed_publication_date":"04 Aug 2025","pubmed_entrez_date":"2025-07-11","publication_year":"2025","canto_session_key":"c9ccdd286f6e831a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-12 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36472074","title":"A unified framework for measuring selection on cellular lineages and traits.","citation":"Elife 2022 Dec 06;11","abstract":"Intracellular states probed by gene expression profiles and metabolic activities are intrinsically noisy, causing phenotypic variations among cellular lineages. Understanding the adaptive and evolutionary roles of such variations requires clarifying their linkage to population growth rates. Extending a cell lineage statistics framework, here we show that a population's growth rate can be expanded by the cumulants of a fitness landscape that characterize how fitness distributes in a population. The expansion enables quantifying the contribution of each cumulant, such as variance and skewness, to population growth. We introduce a function that contains all the essential information of cell lineage statistics, including mean lineage fitness and selection strength. We reveal a relation between fitness heterogeneity and population growth rate response to perturbation. We apply the framework to experimental cell lineage data from bacteria to mammalian cells, revealing distinct levels of growth rate gain from fitness heterogeneity across environments and organisms. Furthermore, third or higher order cumulants' contributions are negligible under constant growth conditions but could be significant in regrowing processes from growth-arrested conditions. We identify cellular populations in which selection leads to an increase of fitness variance among lineages in retrospective statistics compared to chronological statistics. The framework assumes no particular growth models or environmental conditions, and is thus applicable to various biological phenomena for which phenotypic heterogeneity and cellular proliferation are important.","doi":"10.7554/eLife.72299","authors":"Yamauchi S, Nozoe T, Okura R, Kussell E, Wakamoto Y","authors_abbrev":"Yamauchi S et al.","pubmed_publication_date":"06 Dec 2022","pubmed_entrez_date":"2022-12-06","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-12-07 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24173150","title":"The genetic fine structure of nonsense suppressors in Schizosaccharomyces pombe : II. sup8 and sup10.","citation":"Curr Genet 1983 Apr;7(2):101-8","abstract":"Meiotic fine-structure maps of two efficient UGA suppressors of Schizosaccharomyces pombe which are known (sup8-e) or inferred (sup10-e) to code for two leucine tRNAs carrying the mutant anticodon U(*)CA (Kohli et al. 1979, 1980a, b; Wetzel et al. 1979; Mao et al. 1981) are presented. In both cases, the recombination frequencies given by the primary site of the anticodon mutation fitwell into the map defined by the sites of a number of inactivating secondary mutations. This contrasts the corresponding situation found in the serine tRNA genes sup3 and sup9 where the anticodon site exhibits a specific marker effect which strongly increases recombination frequencies in crosses with all revertant sites, due to a decrease in the efficiency of excision repair of base-pair mismatches whenever the anticodon site is included in hybrid-DNA (Hofer et al. 1979; Munz and Leupold 1979; Thuriaux et al. 1980). A pronounced specific marker effect which leads to a several fold increase of the recombination frequencies over those expected is observed, however, at one of the secondary inactivating sites mapping in the leucine tRNA gene sup8.","doi":"10.1007/BF00365633","authors":"Munz P, Dorsch-Häsler K, Leupold U","authors_abbrev":"Munz P et al.","pubmed_publication_date":"Apr 1983","pubmed_entrez_date":"2013-11-01","publication_year":"1983","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"TreeFam:TF313964","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:3019","SPAC17G8.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12445777","title":"The constraints protein-protein interactions place on sequence divergence.","citation":"J Mol Biol 2002 Nov 29;324(3):399-407","abstract":"Structural analyses on a small number of protein families have shown that residues in protein interfaces are more conserved than average amino acid residues. This is also true of other ligand-binding and active site residues. This raises the question whether protein interactions place additional constraints on sequence divergence beyond this general background of functional restrictions on all different types of proteins. In order to investigate this, the sequence identities of Saccharomyces cerevisiae (SC) proteins to their Schizosaccharomyces pombe (SP) orthologues were used as a measure of sequence divergence. The SC proteins were divided into those in stable complexes, those that participate in transient interactions and the remaining proteins. All types of proteins can undergo extensive divergence: all three sequence identity distributions range from less than 20 to over 90%. However, overall, protein interactions do place additional constraints on sequence divergence and the distributions differ significantly: proteins not known to be involved in interactions have an average sequence identity of 38% while this value is 46% for proteins in stable complexes. Proteins that have transient interactions are intermediate between the two, with an average sequence identity of 41%. This trend is independent of whether the proteins are involved in informational functions (transcription, translation and replication) or not and of protein dispensability.","authors":"Teichmann SA","authors_abbrev":"Teichmann SA","pubmed_publication_date":"29 Nov 2002","pubmed_entrez_date":"2002-11-26","publication_year":"2002","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8474436","title":"Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation.","citation":"Mol Cell Biol 1993 May;13(5):2706-17","abstract":"Squalene synthetase (farnesyl diphosphate:farnesyl diphosphate farnesyltransferase; EC 2.5.1.21) is thought to represent a major control point of isoprene and sterol biosynthesis in eukaryotes. We demonstrate structural and functional conservation between the enzymes from humans, a budding yeast (Saccharomyces cerevisiae), and a fission yeast (Schizosaccharomyces pombe). The amino acid sequences of the human and S. pombe proteins deduced from cloned cDNAs were compared to those of the known S. cerevisiae protein. All are predicted to encode C-terminal membrane-spanning proteins of approximately 50 kDa with similar hydropathy profiles. Extensive sequence conservation exists in regions of the enzyme proposed to interact with its prenyl substrates (i.e., two farnesyl diphosphate molecules). Many of the highly conserved regions are also present in phytoene and prephytoene diphosphate synthetases, enzymes which catalyze prenyl substrate condensation reactions analogous to that of squalene synthetase. Expression of cDNA clones encoding S. pombe or hybrid human-S. cerevisiae squalene synthetases reversed the ergosterol requirement of S. cerevisiae cells bearing ERG9 gene disruptions, showing that these enzymes can functionally replace the S. cerevisiae enzyme. Inhibition of sterol synthesis in S. cerevisiae and S. pombe cells or in cultured human fibroblasts by treatment with the 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitor lovastatin resulted in elevated levels of squalene synthetase mRNA in all three cell types.","authors":"Robinson GW, Tsay YH, Kienzle BK, Smith-Monroy CA, Bishop RW","authors_abbrev":"Robinson GW et al.","pubmed_publication_date":"May 1993","pubmed_entrez_date":"1993-05-01","publication_year":"1993","canto_session_key":"63140c499a32ee9b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-09-11 14:04:07","canto_approved_date":"2026-05-28 10:03:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 14:03:59","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC646.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-11"},{"uniquename":"PMID:17209013","title":"Role of SUMO in the dynamics of telomere maintenance in fission yeast.","citation":"Proc Natl Acad Sci U S A 2007 Jan 16;104(3):893-8","abstract":"The sheltering of chromosome ends from illegitimate DNA repair reactions and telomere length homeostasis are critical for preserving genomic integrity. Growing evidence implicates covalent protein modification by SUMO (small ubiquitin-like modifier) (sumoylation) in the regulation of numerous DNA transactions, including DNA repair and transcription, as well as heterochromatin formation and maintenance. We have recently shown that fission yeast Pli1p is a SUMO E3 ligase and that pli1 mutants, which are impaired for global sumoylation, are viable, but exhibit de-regulated homologous recombination and marked defects in chromosome segregation and centromeric silencing, as well as a consistent increase in telomere length. In this work, we explore the mechanisms underlying sumoylation-dependent telomere maintenance. We show that Pli1p, but not the related Nse2p, is the principal SUMO E3 ligase enzyme involved. Using both a pli1 mutation and a physiological \"knockdown\" of sumoylation, achieved by inducible expression of a dominant negative form of the conjugating enzyme Ubc9p, we further show that telomere lengthening induced by lack of sumoylation is not due to unscheduled telomere-telomere recombination. Instead, sumoylation increases telomerase activity, therefore suggesting that this modification controls the activity of a positive or negative regulator of telomerase.","authors":"Xhemalce B, Riising EM, Baumann P, Dejean A, Arcangioli B, Seeler JS","authors_abbrev":"Xhemalce B et al.","pubmed_publication_date":"16 Jan 2007","pubmed_entrez_date":"2007-01-09","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC23B6.03c","SPAC1687.05","SPAC16A10.06c","SPAC26H5.06","SPAC1556.01c","SPBC216.06c","SPAC6F6.17","SPCC126.02c","SPAC3H5.06c"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"EMBL:SP50769","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19748350","title":"Resolving the CSN and CAND1 paradoxes.","citation":"Mol Cell 2009 Sep 11;35(5):547-9","abstract":"In this issue of Molecular Cell, Schmidt et al. (2009) untangle the interplay between the COP9 signalosome (CSN), cullin-associated and neddylation-dissociated 1 (CAND1) protein, and cullin-RING ubiquitin ligases (CRLs).","doi":"10.1016/j.molcel.2009.08.011","authors":"Dubiel W","authors_abbrev":"Dubiel W","pubmed_publication_date":"11 Sep 2009","pubmed_entrez_date":"2009-09-15","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9256450","title":"Modeling the control of DNA replication in fission yeast.","citation":"Proc Natl Acad Sci U S A 1997 Aug 19;94(17):9147-52","abstract":"A central event in the eukaryotic cell cycle is the decision to commence DNA replication (S phase). Strict controls normally operate to prevent repeated rounds of DNA replication without intervening mitoses (\"endoreplication\") or initiation of mitosis before DNA is fully replicated (\"mitotic catastrophe\"). Some of the genetic interactions involved in these controls have recently been identified in yeast. From this evidence we propose a molecular mechanism of \"Start\" control in Schizosaccharomyces pombe. Using established principles of biochemical kinetics, we compare the properties of this model in detail with the observed behavior of various mutant strains of fission yeast: wee1(-) (size control at Start), cdc13Delta and rum1(OP) (endoreplication), and wee1(-) rum1Delta (rapid division cycles of diminishing cell size). We discuss essential features of the mechanism that are responsible for characteristic properties of Start control in fission yeast, to expose our proposal to crucial experimental tests.","authors":"Novak B, Tyson JJ","authors_abbrev":"Novak B et al.","pubmed_publication_date":"19 Aug 1997","pubmed_entrez_date":"1997-08-19","publication_year":"1997","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8247736","title":"Purification and characterization of RNases from fission yeast under nitrogen-starvation.","citation":"Nucleic Acids Symp Ser 1993;(29):129-30","abstract":"Two RNases were purified from nitrogen-starved fission yeast cells in which cellular RNA was being degraded drastically. The two RNases showed similar properties. Their molecular weight in native form was about 170kDa. They were endoRNases which required divalent cations.","authors":"Uritani M, Iwasawa J","authors_abbrev":"Uritani M et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12177319","title":"Morphogenetic checkpoint in fission yeast? Yes!","citation":"Microbiology (Reading) 2002 Aug;148(Pt 8):2270-2271","abstract":"","doi":"10.1099/00221287-148-8-2270","authors":"Sveiczer A, Csikasz-Nagy A, Novak B","authors_abbrev":"Sveiczer A et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-08-15","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21862839","title":"Model of myosin node aggregation into a contractile ring: the effect of local alignment.","citation":"J Phys Condens Matter 2011 Sep 21;23(37):374103","abstract":"Actomyosin bundles frequently form through aggregation of membrane-bound myosin clusters. One such example is the formation of the contractile ring in fission yeast from a broad band of cortical nodes. Nodes are macromolecular complexes containing several dozens of myosin-II molecules and a few formin dimers. The condensation of a broad band of nodes into the contractile ring has been previously described by a search, capture, pull and release (SCPR) model. In SCPR, a random search process mediated by actin filaments nucleated by formins leads to transient actomyosin connections among nodes that pull one another into a ring. The SCPR model reproduces the transport of nodes over long distances and predicts observed clump-formation instabilities in mutants. However, the model does not generate transient linear elements and meshwork structures as observed in some wild-type and mutant cells during ring assembly. As a minimal model of node alignment, we added short-range aligning forces to the SCPR model representing currently unresolved mechanisms that may involve structural components, cross-linking and bundling proteins. We studied the effect of the local node alignment mechanism on ring formation numerically. We varied the new parameters and found viable rings for a realistic range of values. Morphologically, transient structures that form during ring assembly resemble those observed in experiments with wild-type and cdc25-22 cells. Our work supports a hierarchical process of ring self-organization involving components drawn together from distant parts of the cell followed by progressive stabilization.","doi":"10.1088/0953-8984/23/37/374103","authors":"Ojkic N, Wu JQ, Vavylonis D","authors_abbrev":"Ojkic N et al.","pubmed_publication_date":"21 Sep 2011","pubmed_entrez_date":"2011-08-25","publication_year":"2011","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32722101","title":"Fission Yeast Polarization: Modeling Cdc42 Oscillations, Symmetry Breaking, and Zones of Activation and Inhibition.","citation":"Cells 2020 Jul 24;9(8)","abstract":"Cells polarize for growth, motion, or mating through regulation of membrane-bound small GTPases between active GTP-bound and inactive GDP-bound forms. Activators (GEFs, GTP exchange factors) and inhibitors (GAPs, GTPase activating proteins) provide positive and negative feedbacks. We show that a reaction-diffusion model on a curved surface accounts for key features of polarization of model organism fission yeast. The model implements Cdc42 membrane diffusion using measured values for diffusion coefficients and dissociation rates and assumes a limiting GEF pool (proteins Gef1 and Scd1), as in prior models for budding yeast. The model includes two types of GAPs, one representing tip-localized GAPs, such as Rga3; and one representing side-localized GAPs, such as Rga4 and Rga6, that we assume switch between fast and slow diffusing states. After adjustment of unknown rate constants, the model reproduces active Cdc42 zones at cell tips and the pattern of GEF and GAP localization at cell tips and sides. The model reproduces observed tip-to-tip oscillations with periods of the order of several minutes, as well as asymmetric to symmetric oscillations transitions (corresponding to NETO \"new end take off\"), assuming the limiting GEF amount increases with cell size.","doi":"10.3390/cells9081769","authors":"Khalili B, Lovelace HD, Rutkowski DM, Holz D, Vavylonis D","authors_abbrev":"Khalili B et al.","pubmed_publication_date":"24 Jul 2020","pubmed_entrez_date":"2020-07-30","publication_year":"2020","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2020-07-31 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11683277","title":"Fission yeast (Schizosaccharomyces pombe) cells defective in the MutY-homologous glycosylase activity have a mutator phenotype and are sensitive to hydrogen peroxide.","citation":"Mol Genet Genomics 2001 Oct;266(2):336-42","abstract":"The modified base 7,8-dihydro-8-oxo-guanine (8-oxoG) is one of the most stable deleterious products of oxidative DNA damage because it mispairs with adenine during DNA replication. In the fission yeast Schizosaccharomyces pombe, the MutY homolog (SpMYH) is responsible for removing misincorporated adenines from A/8-oxoG or A/G mismatches and thus preventing G:C to T:A mutations. In order to study the functional role of SpMYH, an SpMYH knockout strain was constructed. The SpMYH knockout strain, which does not express SpMYH and has no A/8-oxoG glycosylase activity, displays a 36-fold higher frequency of spontaneous mutations than the wild type strain. Disruption of SpMYH causes increased sensitivity to H2O2 but not to UV-irradiation. Expression of SpMYH in the mutant cells restores the adenine glycosylase activity, reduces the mutation frequency, and elevates the resistance to H2O2. Asp172 of SpMYH is conserved in a helix-hairpin-helix superfamily of glycosylases. The SpMYHA strain expressing D172N SpMYH retained the mutator phenotype. Moreover, when D172N mutant SpMYH was expressed in the wild-type cells, the mutation frequency observed was even higher than that of the parental strains. Thus, a mutant SpMYH that retains substrate-binding activity but is defective in glycosylase activity exhibits a dominant negative effect. This is the first demonstration that a MutY homolog plays an important role in protecting cells against oxidative DNA damage in eukaryotes.","authors":"Chang DY, Gu Y, Lu AL","authors_abbrev":"Chang DY et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-10-31","publication_year":"2001","canto_session_key":"43b1e32796233413","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-10-08 15:37:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-05-29 13:13:21","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-05-29"},{"uniquename":"PMID:8431459","title":"Amiloride and 5-(N-ethyl-N-isopropyl) amiloride inhibit medium acidification and glucose metabolism by the fission yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1993 Feb 09;1145(2):266-72","abstract":"We have investigated the mechanism by which amiloride and 5-(N-ethyl-N-isopropyl)amiloride (EIPA) inhibit glucose-stimulated medium acidification in the fission yeast Schizosaccharomyces pombe. The addition of glucose to an unbuffered suspension of cells results in the extrusion of acid. This process was inhibited by diethylstilbestrol (DES), an inhibitor of the H(+)-ATPase (IC50 71 microM), and also by amiloride (IC50 824 microM) and EIPA (IC50 203 microM). The presence of 100 mM NaCl reduced the degree of inhibition observed for amiloride and EIPA, but had no effect on inhibition by DES. N-Methylglucosamine partially protected the cells against the effect of amiloride, but choline chloride did not, suggesting that sodium may be important in the action of amiloride. To establish the site of action of amiloride and EIPA, ATP hydrolysis assays were performed on isolated plasma membranes. H(+)-ATPase activity was inhibited by orthovanadate, but not by amiloride or EIPA. However, both amiloride and EIPA were found to inhibit the incorporation of radioactivity from labelled glucose in S. pombe, with IC50 values of 879 and 272 microM for amiloride and EIPA respectively. Again, 100 mM NaCl was found to reduce the effectiveness of inhibition. Amiloride had no effect on the uptake of 2-deoxyglucose under the same conditions, indicating that amiloride does not inhibit the glucose transporter. We propose that amiloride and EIPA disrupt glucose-induced acidification by inhibiting glucose metabolism.","authors":"Haworth RS, Cragoe EJ, Fliegel L","authors_abbrev":"Haworth RS et al.","pubmed_publication_date":"09 Feb 1993","pubmed_entrez_date":"1993-02-09","publication_year":"1993","canto_session_key":"2ae494e22079c491","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-12-01 11:45:04","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-01 11:44:55","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-12-01"},{"uniquename":"PMID:12529438","title":"Global transcriptional responses of fission yeast to environmental stress.","citation":"Mol Biol Cell 2003 Jan;14(1):214-29","abstract":"We explored transcriptional responses of the fission yeast Schizosaccharomyces pombe to various environmental stresses. DNA microarrays were used to characterize changes in expression profiles of all known and predicted genes in response to five stress conditions: oxidative stress caused by hydrogen peroxide, heavy metal stress caused by cadmium, heat shock caused by temperature increase to 39 degrees C, osmotic stress caused by sorbitol, and DNA damage caused by the alkylating agent methylmethane sulfonate. We define a core environmental stress response (CESR) common to all, or most, stresses. There was a substantial overlap between CESR genes of fission yeast and the genes of budding yeast that are stereotypically regulated during stress. CESR genes were controlled primarily by the stress-activated mitogen-activated protein kinase Sty1p and the transcription factor Atf1p. S. pombe also activated gene expression programs more specialized for a given stress or a subset of stresses. In general, these \"stress-specific\" responses were less dependent on the Sty1p mitogen-activated protein kinase pathway and may involve specific regulatory factors. Promoter motifs associated with some of the groups of coregulated genes were identified. We compare and contrast global regulation of stress genes in fission and budding yeasts and discuss evolutionary implications.","authors":"Chen D, Toone WM, Mata J, Lyne R, Burns G, Kivinen K, Brazma A, Jones N, Bähler J","authors_abbrev":"Chen D et al.","pubmed_publication_date":"Jan 2003","pubmed_entrez_date":"2003-01-17","publication_year":"2003","canto_session_key":"e1524afe2c679c65","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-23 17:40:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-23 17:16:55","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1318,"orcid":"0000-0003-4148-4606","file_type":"qualitative_gene_expression","file_name":"PMID_12529438_Chen_qualitative_expression.txt"}],"genes":["SPAC30C2.02","SPAC11D3.01c","SPAC3C7.02c","SPCC576.03c","SPCC663.07c","SPBC11B10.09","SPAC26F1.07","SPCC16A11.15c","SPBC1271.07c","SPAC1002.13c","SPAC1002.19","SPBC21C3.08c","SPCC297.04c","SPCC417.05c","SPBC25B2.05","SPAC22H10.13","SPAC139.05","SPCC757.12","SPBC19C7.04c","SPCC1450.13c","SPAP8A3.04c","SPBC19F5.05c","SPCC1223.03c","SPBC16D10.01c","SPAC25H1.02","SPBC428.10","SPBP26C9.03c","SPAC1B3.03c","SPACUNK4.15","SPAC3C7.05c","SPBC2G2.08","SPAC11E3.09","SPBC1271.05c","SPAC8F11.04","SPAC2F3.03c","SPAC13G7.13c","SPAC23D3.11","SPAC23A1.14c","SPAC6G10.03c","SPCC830.07c","SPBC36.01c","SPBC660.07","SPAC2C4.15c","SPBC1347.02","SPAC20G8.09c","SPCC191.01","SPBPB2B2.05","SPAC22G7.08","SPAC56F8.09","SPCC18.12c","SPAC17H9.04c","SPAC23D3.12","SPCC4G3.03","SPAC1002.17c","SPACUNK4.17","SPCC4F11.04c","SPBC20F10.01","SPAC1F7.02c","SPAC11E3.14","SPAC18B11.06","SPBP23A10.11c","SPAC22E12.03c","SPBC32H8.07","SPBC3H7.02","SPCC757.03c","SPBP16F5.08c","SPCC584.16c","SPAC6G10.12c","SPAC513.02","SPAC1F3.09","SPAC4F10.20","SPCC1235.01","SPAC23G3.03","SPAC607.08c","SPBC32F12.03c","SPBP4H10.10","SPAC57A10.12c","SPBC1711.07","SPAC977.13c","SPCC306.08c","SPBC106.10","SPBPB10D8.01","SPBC29A3.08","SPAC31A2.12","SPBC409.13","SPCC330.07c","SPAC4H3.03c","SPBC776.17","SPAC637.03","SPCC1322.08","SPBC36.03c","SPAC13G7.02c","SPBC14F5.06","SPBC215.06c","SPCC320.11c","SPBC1271.08c","SPCC63.14","SPAC23C4.17","SPAC19G12.09","SPBC3H7.09","SPBC1734.01c","SPBC8D2.18c","SPAC2E1P3.01","SPAC821.09","SPBC215.11c","SPBC660.05","SPBC16E9.16c","SPBC2G5.06c","SPAC23D3.05c","SPBC16D10.08c","SPAC6B12.07c","SPAC513.06c","SPAPB1A11.03","SPBC17D11.03c","SPAC22G7.11c","SPAC4D7.02c","SPCC338.18","SPCC794.04c","SPBC19C2.04c","SPCC1223.09","SPCC18B5.02c","SPCC965.13","SPBC30D10.14","SPAC3C7.14c","SPCC24B10.20","SPAC926.08c","SPBC23G7.10c","SPAC5H10.02c","SPAC11E3.06","SPCC736.15","SPBC11G11.03","SPAC21E11.04","SPCC550.10","SPCC663.06c","SPBC660.06","SPBC1289.14","SPAPB8E5.04c","SPAC9.10","SPAC2G11.11c","SPAC21E11.03c","SPBC887.15c","SPAC23A1.03","SPCC1393.12","SPCC1281.07c","SPBC1861.02","SPAC1F7.12","SPCC663.08c","SPCC24B10.11c","SPCC1183.11","SPAC688.04c","SPBC365.12c","SPBC21H7.06c","SPBC8D2.10c","SPAC977.16c","SPAC29B12.14c","SPAC19B12.08","SPAC1399.04c","SPAC57A10.09c","SPBC29B5.01","SPBP8B7.16c","SPBC119.03","SPBC29A3.01","SPBC14F5.03c","SPBC215.05","SPAC1805.09c","SPAC6G9.10c","SPCC338.13","SPCC1827.01c","SPBPB10D8.02c","SPAC4G9.11c","SPAC2F7.11","SPCC645.14c","SPAC977.05c","SPAC222.06","SPAC167.06c","SPBC20F10.10","SPCC584.13","SPAC1039.10","SPBC4F6.17c","SPAC26F1.11","SPAC513.07","SPBC19F5.04","SPAC30.01c","SPAC27D7.03c","SPCC18B5.01c","SPCC1183.07","SPAC14C4.09","SPAC23H3.15c","SPCC126.03","SPAC343.12","SPBC23G7.06c","SPCC1494.03","SPCC613.08","SPBC2D10.05","SPCPB1C11.03","SPAC27D7.11c","SPBC1539.04","SPAC1F8.04c","SPAC9E9.04","SPBC20F10.03","SPAC10F6.06","SPAC19D5.01","SPAC664.06","SPAC3C7.13c","SPAC1B3.06c","SPAC29B12.10c","SPAC22E12.13c","SPBC4F6.14","SPBC1683.01","SPAC23H4.15","SPCC1450.04","SPAPB24D3.08c","SPCC576.04","SPAC4G8.03c","SPBC428.03c","SPBC359.06","SPAC2E1P3.04","SPBC8E4.01c","SPBC21C3.19","SPBC1652.01","SPAC6F6.02c","SPAC2F3.05c","SPBC1773.05c","SPBC106.17c","SPAC19A8.07c","SPCC290.02","SPBC16A3.17c","SPBC800.06","SPAC6G9.02c","SPAC24B11.06c","SPBC1198.02","SPBPB2B2.08","SPBC725.02","SPACUNK4.16c","SPBP8B7.20c","SPAC4A8.04","SPAC222.08c","SPAC23C11.06c","SPBC776.08c","SPCC1223.14","SPBC16A3.02c","SPAC869.09","SPBC1773.17c","SPAC343.20","SPBC359.05","SPBC25B2.09c","SPAC27D7.09c","SPBC725.04","SPAC25B8.12c","SPCC757.07c","SPAC1039.01","SPBC16D10.06","SPAC19B12.01","SPBC839.07","SPBC947.04","SPAC11E3.01c","SPAC1142.04","SPBPB7E8.01","SPBC3B9.01","SPAC11D3.13","SPCC965.06","SPBC2F12.09c","SPBC29B5.02c","SPBC23E6.05","SPBC11C11.06c","SPBC12D12.07c","SPBC609.04","SPAC328.03","SPBC725.01","SPAC5H10.06c","SPAC869.02c","SPCC1442.16c","SPCC330.04c","SPCC330.06c","SPAC57A7.11","SPBC25D12.04","SPAC4H3.08","SPAC9E9.11","SPBC725.03","SPCP31B10.06","SPCC18.03","SPCC1739.06c","SPAC1B3.15c","SPAC10F6.03c","SPBC12C2.04","SPBC56F2.06","SPAC513.03","SPAC22H12.01c","SPBC1773.06c","SPAC1002.18","SPBC21B10.12","SPBC106.02c","SPBC1604.01","SPAC2C4.17c","SPAC683.02c","SPAC869.05c","SPBC359.02","SPAC4A8.03c","SPAC1B9.03c","SPBC106.14c","SPBC29A3.06","SPAC15E1.02c","SPBC1711.12","SPAC3A11.06","SPAC25B8.13c","SPAC2E12.03c","SPBC947.06c","SPAC22F8.05","SPBC2A9.02","SPAC823.08c","SPAC57A10.05c","SPAC1486.09","SPAC26F1.04c","SPAPB1A10.14","SPBC3E7.02c","SPBC1711.08","SPAC23H4.06","SPBC14F5.09c","SPBC32H8.05","SPAC8C9.03","SPBC1105.14","SPAC22A12.17c","SPBC725.10","SPBC3F6.03","SPBC29A3.16","SPCC320.03","SPBC1778.01c","SPCC61.03","SPBPB2B2.06c","SPBC16E9.10c","SPAC26F1.14c","SPCC1020.10","SPBC887.17","SPAPB1A10.05","SPCP1E11.11","SPBC23G7.11","SPCC4F11.02","SPBC16C6.12c","SPAC8E11.10","SPAC890.05","SPBC1105.13c","SPAC3A12.18","SPBC24C6.09c","SPAC1002.20","SPAC521.03","SPBC3B8.05","SPAC56E4.03","SPACUNK4.10","SPCC576.02","SPAC57A7.05","SPBC1347.11","SPAC227.18","SPAC16A10.01","SPBC83.15","SPCC338.12","SPAC23G3.02c","SPBC23E6.09","SPBC9B6.07","SPBC409.12c"],"gene_count":359,"ltp_gene_count":0,"approved_date":"2016-02-23"},{"uniquename":"PMID:33357436","title":"Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis.","citation":"Cell Rep 2020 Dec 22;33(12):108526","abstract":"Many eukaryotes assemble an actin- and myosin-based cytokinetic ring (CR) on the plasma membrane (PM) for cell division, but how it is anchored there remains unclear. In Schizosaccharomyces pombe, the F-BAR protein Cdc15 links the PM via its F-BAR domain to proteins in the CR's interior via its SH3 domain. However, Cdc15's F-BAR domain also directly binds formin Cdc12, suggesting that Cdc15 may polymerize a protein network directly adjacent to the membrane. Here, we determine that the F-BAR domain binds Cdc12 using residues on the face opposite its membrane-binding surface. These residues also bind paxillin-like Pxl1, promoting its recruitment with calcineurin to the CR. Mutation of these F-BAR domain residues results in a shallower CR, with components localizing ∼35% closer to the PM than in wild type, and aberrant CR constriction. Thus, F-BAR domains serve as oligomeric membrane-bound platforms that can modulate the architecture of an entire actin structure.","doi":"10.1016/j.celrep.2020.108526","authors":"Snider CE, Chandra M, McDonald NA, Willet AH, Collier SE, Ohi MD, Jackson LP, Gould KL","authors_abbrev":"Snider CE et al.","pubmed_publication_date":"22 Dec 2020","pubmed_entrez_date":"2020-12-28","publication_year":"2020","canto_session_key":"ceb4bd4bfdcc4dae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chloe Snider","canto_first_approved_date":"2021-01-13 17:08:27","canto_approved_date":"2025-10-17 14:03:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-12 17:08:56","canto_added_date":"2020-12-30 01:15:06","annotation_curators":[{"name":"Chloe Snider","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.12","SPAC1F5.04c","SPAC20G8.05c","SPBC11C11.02","SPBC83.18c","SPAC4A8.05c","SPBP4H10.04"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2021-01-13","pdb_entries":[{"pdb_id":"6xj1","gene_chains":[{"gene_uniquename":"SPAC20G8.05c","chain":"A/B","position":"19-312"}],"title":"Crystal Structure of CDC15 F-BAR Domain from Schizosaccharomyces pombe","entry_authors":"Chandra M,Jackson LP,Snider CE,Gould KL","entry_authors_abbrev":"Chandra M et al.","reference_uniquename":"PMID:33357436","experimental_method":"X-ray","resolution":"3.52"}]},{"uniquename":"PMID:672902","title":"Genetical studies on revertants to sensitivity from a cycloheximide resistant strain of Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1978 Jun 14;162(2):213-9","abstract":"Six UV induced cycloheximide-sensitive revertants were isolated from the cyh1-C7 strain of Schizosaccharomyces pombe which is resistant to cycloheximide. In all cases reversion to sensitivity was due to a forward mutation in a second suppressor gene. Genetical analysis showed that at least two genes, designated scr1 and scr2 (scr=suppression of cycloheximide resistance) were involved. Both scr1 and scr2 suppressed the resistance of six independently isolated alleles at the cyh1 locus. They had no effect on two known nonsense mutations in the ade7 locus. The cyh1-C7 strain has an altered 60S ribosomal protein which can be detected by two-dimensional polyacrylamide gel electrophoresis. In two suppressed strains, cyh1-C7 scr1 and cyh1-C7 scr2, the original altered protein was present. However no further ribosomal protein differences were observed which could be correlated with the presence of the scr genes. Both scr mutations conferred cold sensitivity on the organism indicating that they were of the missense type. Hence it seems certain that scr1 and scr2 are not mutations in tRNA genes leading to either nonsense or missense suppression. There is however no direct evidence that they code for ribosomal proteins and exert their effect on cyh1-C7 at the ribosomal level.","authors":"Ibrahim MA, Coddington A","authors_abbrev":"Ibrahim MA et al.","pubmed_publication_date":"14 Jun 1978","pubmed_entrez_date":"1978-06-14","publication_year":"1978","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2520196","title":"Effects of asymmetric division on a stochastic model of the cell division cycle.","citation":"Math Biosci 1989 Oct;96(2):165-84","abstract":"The stochastic model of cell division formulated by Alt and Tyson is generalized to the case of imprecise binary fission. Closed-form expressions are derived for the generation-time distribution, the birth-size and division-size distributions, the beta curve, and the correlation coefficient of generation times of sister cells. The theoretical results are compared to observations of cell division statistics in a culture of fission yeast.","authors":"Tyson JJ","authors_abbrev":"Tyson JJ","pubmed_publication_date":"Oct 1989","pubmed_entrez_date":"1989-10-01","publication_year":"1989","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084849","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.37"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9734781","title":"Defect in cytokinesis of fission yeast induced by mutation in the WD40 repeat motif of a TFIID subunit.","citation":"Genes Cells 1998 Jun;3(6):347-55","abstract":"TBP-associated factors contain a variety of structural motifs and their related in vivo significance has remained unclear. We have attempted to identify specific biological phenomena linked to a particular domain of a TAF by analysing domain-exchanged chimeric mutants between Schizosaccharomyces pombe (Sp) and Saccharomyces cerevisiae (Sc) counterparts.\nContrary to the case of TBP, Sp TAF containing the WD40 repeat cannot be exchanged for its Sc counterpart, despite their highly conserved primary structures. This 'species-specific' function locates in the N-terminal region. The C-terminal region, largely consisting of the WD40 repeat, is exchangeable for the corresponding region of its Sc counterpart. Growth of the strain harbouring this C-terminal chimeric mutant is temperature-sensitive. The chimeric gene product did not disappear at a restrictive temperature, a finding which strongly suggests that the growth defect is caused by an aberration in the interactions through the WD40 repeat structural motif. With temperature elevation, the chimeric mutants underwent drastic morphological changes due to a defect in cytokinesis.\nThe WD40 repeat of TAF is primarily involved in reactions which might regulate cytokinesis in Sp.","authors":"Yamamoto T, Horikoshi M","authors_abbrev":"Yamamoto T et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-09-12","publication_year":"1998","canto_session_key":"99535c35ecc60bde","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-15 17:13:21","canto_approved_date":"2018-12-15 17:13:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-15 17:13:13","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.14"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2018-12-15"},{"uniquename":"PMID:25783886","title":"A yeast-based high-throughput screen for modulators of phosphodiesterase activity.","citation":"Methods Mol Biol 2015;1294:181-90","abstract":"Cell-based high-throughput screens (HTSs) targeting heterologously expressed proteins in yeast identify compounds that often display relevant biological activity when tested in cell culture. We developed a fission yeast-based HTS to detect small-molecule inhibitors of mammalian cyclic nucleotide phosphodiesterases (PDEs). These screens are carried out in Schizosaccharomyces pombe using a PKA-repressed fbp1-ura4 reporter whose expression due to low PKA activity prevents cells from growing in medium containing the pyrimidine analog 5-fluoro orotic acid (5FOA). We describe here the steps required to construct strains for screening and to optimize conditions for successful screens.","doi":"10.1007/978-1-4939-2537-7_14","authors":"de Medeiros AS, Hoffman CS","authors_abbrev":"de Medeiros AS et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-19","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-03-20 01:16:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPST11P","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22088094","title":"Integrity of chromatin and replicating DNA in nuclei released from fission yeast by semi-automated grinding in liquid nitrogen.","citation":"BMC Res Notes 2011 Nov 16;4:499","abstract":"Studies of nuclear function in many organisms, especially those with tough cell walls, are limited by lack of availability of simple, economical methods for large-scale preparation of clean, undamaged nuclei.\nHere we present a useful method for nuclear isolation from the important model organism, the fission yeast, Schizosaccharomyces pombe. To preserve in vivo molecular configurations, we flash-froze the yeast cells in liquid nitrogen. Then we broke their tough cell walls, without damaging their nuclei, by grinding in a precision-controlled motorized mortar-and-pestle apparatus. The cryo-ground cells were resuspended and thawed in a buffer designed to preserve nuclear morphology, and the nuclei were enriched by differential centrifugation. The washed nuclei were free from contaminating nucleases and have proven well-suited as starting material for genome-wide chromatin analysis and for preparation of fragile DNA replication intermediates.\nWe have developed a simple, reproducible, economical procedure for large-scale preparation of endogenous-nuclease-free, morphologically intact nuclei from fission yeast. With appropriate modifications, this procedure may well prove useful for isolation of nuclei from other organisms with, or without, tough cell walls.","doi":"10.1186/1756-0500-4-499","authors":"Givens RM, Mesner LD, Hamlin JL, Buck MJ, Huberman JA","authors_abbrev":"Givens RM et al.","pubmed_publication_date":"16 Nov 2011","pubmed_entrez_date":"2011-11-18","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000025","title":"Operon structure as IGC evidence","abstract":"Genes in prokaryotic organisms are often arranged in operons. Genes in an operon are all transcribed into one mRNA. Generally the genes in the operons code for proteins that all have related functions. For example, they may be the steps in a biochemical pathway, or they may be the subunits of a protein complex. Often the genes in operons shared between organisms are syntenic; that is, the same genes are in the same order in the operon in different species. When assessing sequence-comparison-based evidence during the process of manual annotation of a genome, it is often the case that some of the genes in the operon will have strong sequence-based evidence while others will have weak evidence. If seen alone, not in the presence of an operon, the weak evidence in question may not be sufficient to make a functional annotation. However, in the presence of an operon in which there is strong evidence for some of the genes, the very presence of the gene in the operon is a strong indication that the gene shares in the process carried out by the operon. If the putative function is one expected to exist for the process in question and particularly if that function has been observed in the same operon in another species, then the annotation should be made. This type of evidence is inferred from the context of the gene in an operon, and therefore the evidence code is IGC \"inferred from genomic context.\"","authors":"Michelle Gwinn, TIGR curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1A10.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12706511","title":"Relation between cell wall chitin content and susceptibility to amphotericin B in Kluyveromyces, Candida and Schizosaccharomyces species.","citation":"Res Microbiol 2003 Apr;154(3):215-22","abstract":"Yeast strains belonging to the genera Candida, Kluyveromyces and Schizosaccharomyces were tested for their susceptibility (or resistance) to amphotericin B (AmB) in relation to their cell wall chitin content. Results showed that membrane sterol contents did not enable us to explain resistance or susceptibility of these yeasts to AmB. Indeed, we noted that resistant strains were as rich in ergosterol as sensitive strains. The suppression of the wall of yeasts induced an increase in susceptibility to AmB. Strains with high cell wall chitin content were more sensitive to this polyenic antifungal agent than strains with low chitin content. Growth of the yeasts in the presence of chitin induced a resistance of the yeasts to AmB. Similar results were obtained after treatment of the cells by chitinase. In contrast, growth of the yeasts in the presence of chitin synthase activators induced high susceptibility to AmB. Yeast cell wall chitin is an aminopolysaccharide, usually at low concentrations. In Schizosaccharomyces pombe its presence was not established. This polymer is associated with glucans in the wall matrix of the lateral wall and in the budding scars. Even at low content, this polymer seems to play an essential role in the sensitivity (or resistance) of yeast cells to AmB.","authors":"Bahmed K, Bonaly R, Coulon J","authors_abbrev":"Bahmed K et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-04-23","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5078136","title":"UV-induced replicating instability in fission yeast Schizosaccharomyces pombe.","citation":"Mutat Res 1972 Nov;16(3):249-64","abstract":"","authors":"Dubinin NP, Kurennaya ON, Kurlapova LD, Tarasov VA","authors_abbrev":"Dubinin NP et al.","pubmed_publication_date":"Nov 1972","pubmed_entrez_date":"1972-11-01","publication_year":"1972","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16354704","title":"Rhp51-dependent recombination intermediates that do not generate checkpoint signal are accumulated in Schizosaccharomyces pombe rad60 and smc5/6 mutants after release from replication arrest.","citation":"Mol Cell Biol 2006 Jan;26(1):343-53","abstract":"The Schizosaccharomyces pombe rad60 gene is essential for cell growth and is involved in repairing DNA double-strand breaks. Rad60 physically interacts with and is functionally related to the structural maintenance of chromosomes 5 and 6 (SMC5/6) protein complex. In this study, we investigated the role of Rad60 in the recovery from the arrest of DNA replication induced by hydroxyurea (HU). rad60-1 mutant cells arrested mitosis normally when treated with HU. Significantly, Rad60 function is not required during HU arrest but is required on release. However, the mutant cells underwent aberrant mitosis accompanied by irregular segregation of chromosomes, and DNA replication was not completed, as revealed by pulsed-field gel electrophoresis. The deletion of rhp51 suppressed the aberrant mitosis of rad60-1 cells and caused mitotic arrest. These results suggest that Rhp51 and Rad60 are required for the restoration of a stalled or collapsed replication fork after release from the arrest of DNA replication by HU. The rad60-1 mutant was proficient in Rhp51 focus formation after release from the HU-induced arrest of DNA replication or DNA-damaging treatment. Furthermore, the lethality of a rad60-1 rqh1Delta double mutant was suppressed by the deletion of rhp51 or rhp57. These results suggest that Rad60 is required for recombination repair at a step downstream of Rhp51. We propose that Rhp51-dependent DNA structures that cannot activate the mitotic checkpoints accumulate in rad60-1 cells.","authors":"Miyabe I, Morishita T, Hishida T, Yonei S, Shinagawa H","authors_abbrev":"Miyabe I et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2005-12-16","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC644.14c","SPCC18B5.11c","SPBC1921.02","SPAC20H4.07","SPAC2G11.12"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:21449049","title":"A novel fission yeast mei4 mutant that allows efficient synchronization of telomere dispersal and the first meiotic division.","citation":"Yeast 2011 Jun;28(6):467-79","abstract":"The progression of meiosis is controlled by a number of gene-expression systems in the fission yeast Schizosaccharomyces pombe. A forkhead-type transcription factor Mei4 activates a number of genes essential for progression from the middle to late stages of meiosis, which include meiosis I, meiosis II and sporulation. The mei4-deletion mutant (mei4Δ) arrests after meiotic prophase and does not enter meiosis I. To further analyse the Mei4 function, we isolated novel temperature-sensitive mei4 alleles. The two alleles isolated in the initial screen turned out to contain a substitution at N136 in the forkhead DNA-binding domain. Among site-directed mutants that carried a point mutation at this position, the mei4-N136A mutant showed the most severe temperature sensitivity. The mei4-N136A mutant arrested before meiosis I at the restrictive temperature, as did the mei4Δ mutant. In fission yeast, the telomeres are clustered at the spindle pole body (SPB) in meiotic prophase and disperse from it at the onset of meiosis I. The mei4Δ mutant was found to arrest with its telomeres clustered at the SPB, demonstrating a role for Mei4 in telomere dispersion. The mei4-N136A mutant also arrested with clustered telomeres at the restrictive temperature, and the clustering was synchronously resolved after a temperature down-shift, indicating that mei4-N136A is a reversible allele. Hence, the mei4-N136A mutant will be a unique tool to synchronize the meiotic cell cycle from meiosis I onwards and may facilitate analyses of cellular activities occurring during meiosis I.","doi":"10.1002/yea.1851","authors":"Kakui Y, Sato M, Tanaka K, Yamamoto M","authors_abbrev":"Kakui Y et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-03-31","publication_year":"2011","canto_session_key":"ce69bd1defde2d3e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2019-10-24 07:31:33","canto_approved_date":"2019-10-24 07:31:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-10-03 13:35:56","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Masamitsu Sato","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-10-24"},{"uniquename":"PMID:15371597","title":"swi1- and swi3-dependent and independent replication fork arrest at the ribosomal DNA of Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 2004 Sep 28;101(39):14085-90","abstract":"Replication forks are arrested at specific sequences to facilitate a variety of DNA transactions. Forks also stall at sites of DNA damage, and the regression of stalled forks without rescue can cause genetic instability. Therefore, unraveling the mechanisms of fork arrest and of rescue of stalled forks is of considerable general interest. In Schizosaccharomyces pombe, products of two mating-type switching genes, swi1 and swi3, participate in fork arrest at the mating-type switch locus. Here, we show that these proteins also act at three termini (Ter) also called replication fork barriers in the spacer regions of rDNA but not at a fourth site, RFP4, which is nonfunctional when present in a plasmid. Two of the Swi1p- and Swi3p-dependent sites were also dependent on the transcription terminator Reb1p. Furthermore, hydroxyurea-induced replication stress mimicked the effect of swi1 or swi3 mutations at these sites. A swi1 mutant that failed to arrest forks at the mating-type fork barrier RTS1 was functional at the rDNA Ter sites, suggesting some specificity of action. Both WT and mutant forms of Swi1p were physically localized at the Ter sites in vivo. The results support the notion that Swi1p and Swi3p act at several different protein-DNA complexes in the rDNA spacer regions to arrest replication but that not all fork barriers required their activity to arrest forks.","authors":"Krings G, Bastia D","authors_abbrev":"Krings G et al.","pubmed_publication_date":"28 Sep 2004","pubmed_entrez_date":"2004-09-17","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16896217","title":"Stress-specific role of fission yeast Gcn5 histone acetyltransferase in programming a subset of stress response genes.","citation":"Eukaryot Cell 2006 Aug;5(8):1337-46","abstract":"Gcn5 is a coactivator protein that contributes to gene activation by acetylating specific lysine residues within the N termini of histone proteins. Gcn5 has been intensively studied in the budding yeast, Saccharomyces cerevisiae, but the features of genes that determine whether they require Gcn5 during activation have not been conclusively clarified. To allow comparison with S. cerevisiae, we have studied the genome-wide role of Gcn5 in the distantly related fission yeast, Schizosaccharomyces pombe. We show that Gcn5 is specifically required for adaptation to KCl- and CaCl(2)-mediated stress in S. pombe. We have characterized the genome-wide gene expression responses to KCl stress and show that Gcn5 is involved in the regulation of a subset of stress response genes. Gcn5 is most clearly associated with KCl-induced genes, but there is no correlation between Gcn5 dependence and the extent of their induction. Instead, Gcn5-dependent KCl-induced genes are specifically enriched in four different DNA motifs. The Gcn5-dependent KCl-induced genes are also associated with biological process gene ontology terms such as carbohydrate metabolism, glycolysis, and nicotinamide metabolism that together constitute a subset of the ontology parameters associated with KCl-induced genes.","authors":"Johnsson A, Xue-Franzén Y, Lundin M, Wright AP","authors_abbrev":"Johnsson A et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-10","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15957216","title":"Chromosome walking shows a highly homologous repetitive sequence present in all the centromere regions of fission yeast.","citation":"EMBO J 1986 May;5(5):1011-21","abstract":"By cloning centromere-linked genes followed by partial overlapping hybridization, we constructed a 210-kb map encompassing the centromere in chromosome II and a 60-kp map near the centromere of chromosome I in the fission yeast Schizosaccharomyces pombe which has three chromosomes. Integration of the cloned sequences into the chromosome and subsequent analyses of tetrads and dyads revealed an approximately 50 kb long domain located in the middle of the 210-kb map, tightly linked to the centromere and greatly reduced in meiotic recombination. This domain contained at least two classes of repetitive sequences. One, designated yn1, was specifically present in a particular chromosome and repeated three times in the 210-kb map of chromosome II. The other, designated dg, was located in all the centromere regions of three chromosomes. One (dgI) and two (dgIIa, dgIIb) copies of the dg were found in the maps of chromosomes I and II, respectively. The dgIIa and dgIIb were arranged with a 20-kb interval within the repetitive domain. In the centric region of chromosome II, 3-4 copies of the dg appeared to exist. By determining the nucleotide sequences of dgI and dgIIa, the dg was identified to be 3.8 kb long. The sequence homology was 99% between dgI and dgIIa. These extraordinarily homologous sequences seemed not to be transcribed into RNA nor to be encoding any protein. The larger part of the dg sequence was internally non-repetitious, a 600-bp region existed which consisted of stretches of several short repeating units. The structures in or surrounding the centromeres of S. pombe appear to be much more complex than those of the budding yeast Saccharomyces cerevisiae.","authors":"Nakaseko Y, Adachi Y, Funahashi S, Niwa O, Yanagida M","authors_abbrev":"Nakaseko Y et al.","pubmed_publication_date":"May 1986","pubmed_entrez_date":"1986-05-01","publication_year":"1986","canto_session_key":"0f85527ebb3ecbd3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 22:10:32","canto_approved_date":"2018-12-22 22:10:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 22:10:25","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:19563125","title":"Assays used to study the DNA replication checkpoint in fission yeast.","citation":"Methods Mol Biol 2009;521:493-507","abstract":"The DNA replication checkpoint, also known as the intra-S or S-phase checkpoint, plays a central role in ensuring the accuracy of DNA replication. When replication is impeded by DNA damage or other conditions, this checkpoint delays cell cycle progression and coordinates resumption of replication with DNA repair pathways. One of its critical functions is to stabilize stalled replication forks in a replication-competent state, presumably by maintaining proper assembly of replisome components and preserving DNA structures. Here we describe a series of assays used to study the replication checkpoint. These assays allow us to investigate the specific functions of proteins involved in the replication checkpoint in fission yeast.","doi":"10.1007/978-1-60327-815-7_28","authors":"Noguchi E, Ansbach AB, Noguchi C, Russell P","authors_abbrev":"Noguchi E et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39603377","title":"Schizosaccharomyces pombe Grx4 is subject to autophagic degradation under nitrogen- and iron- starvation and ER-stress.","citation":"Arch Biochem Biophys 2024 Nov 25;764:110227","abstract":"Glutaredoxins (Grxs) are small, heat-stable proteins that serve as multi-functional glutathione （GSH）-dependent thiol transferases. Recent studies have elucidated their role in regulating cellular iron and copper homeostases. In Schizosaccharomyces pombe, five Grxs (Grx1-5) have been identified. Among them， Grx4 and its homologs possess a C-terminal glutaredoxin domain (GRX) and an N-terminal thioredoxin-like domain (TRX). The functional roles of the GRX and TRX domains in Grx4 were investigated by constructing strains that express a truncated Grx4 under the regulation of either a constitutive cam1 promoter or its native promoter. Our findings indicated that two autophagy-related (Atg) protein 8 (Atg8)-interacting motifs (AIM), FLKI and FQEI, in the TRX domain of Grx4 are sufficient to induce autophagic degradation under nitrogen- and iron-starvation, respectively. Moreover, the expression level of a vacuolar ferrous iron transporter Pcl1 was altered in Δatg5 or Δatg8 strains under iron starvation,suggesting that autophagy is required for maintaining iron homeostasis in S. pombe. Further investigations revealed that Grx4 is required for cellular survival and endoplasmic reticulum (ER) autophagy (ER-phagy) during dithiothreitol (DTT) treatment, implying a potential correlation between Grxs and ER-stress. Additionally, loss of Grx4 disrupts nuclear integrity during ER stress, highlighting the versatility and importance of further investigations into the functions of Grx4.","doi":"10.1016/j.abb.2024.110227","authors":"Li R, Huang Y","authors_abbrev":"Li R et al.","pubmed_publication_date":"25 Nov 2024","pubmed_entrez_date":"2024-11-27","publication_year":"2024","canto_session_key":"5daf034d80762897","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-11-29 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6580524","title":"Regulation of the maximal rate of RNA synthesis in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1983;192(1-2):212-7","abstract":"Of interest to many biologists is how growth, e.g., RNA synthesis, and cell division are mutually controlled. One method of establishing the nature of the control is to determine what \"factors\" are limiting when cells synthesize RNA at a maximal rate. The transcription maximum (maximum rate of RNA synthesis) has been determined in cell division mutants that continue to grow but fail to divide to determine if there is a cell cycle control over RNA synthesis. There is no correlation between transcription maximum and DNA synthesis or septation which suggests that these events do not exert a direct cell cycle control over RNA synthesis in exponentially growing cells. In addition, the lack of strong correlation between the transcription maximum and cell size or gene dosage indicates that the rate of RNA synthesis is not directly regulated by either of these parameters. The possibility that the maximum rate is determined by a concentration effect of an end product which acts in the nucleus, such as a specific RNA or protein, could not be ruled out and evidence is presented in support of such a model.","authors":"Elliott SG","authors_abbrev":"Elliott SG","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-01-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18235246","title":"Aurora B kinases restrict chromosome decondensation to telophase of mitosis.","citation":"Cell Cycle 2008 Feb 01;7(3):293-6","abstract":"The Aurora kinases comprise a family of evolutionary conserved serine/threonine kinases that have important functions in centrosome duplication, mitotic spindle assembly, chromosome condensation, chromosome biorientation on the spindle and chromosome segregation. Vertebrates have three Aurora kinases, Aurora-A, -B and -C, while invertebrates have only Aurora-A and -B and yeasts have a single Aurora kinase, IpI1 in S. cerevisiae and Ark1 in S. pombe. Recently, the role of Aurora kinases in chromosome condensation has been defined; Aurora B plays a crucial role in the axial shortening of chromosomes during anaphase, presumably in order to prevent chromosome arms from becoming trapped within the cytokinetic plate.","authors":"Vas AC, Clarke DJ","authors_abbrev":"Vas AC et al.","pubmed_publication_date":"01 Feb 2008","pubmed_entrez_date":"2008-02-01","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7589895","title":"Liver fructose-1,6-bisphosphatase cDNA: trans-complementation of fission yeast and characterization of two human transcripts.","citation":"Differentiation 1995 Jul;59(1):51-60","abstract":"The SV40 early promoter is active both in mammalian cells and in the fission yeast Schizosaccharomyces pombe, and is used to drive full-length cDNA in polyvalent pcD-libraries. Two such liver libraries, of human and rat origin, were used to trans-complement a S. pombe mutant deficient in fructose-1,6-bisphosphatase (Fru-1,6-Pase) activity, a key gluconeogenic enzyme restricted to liver, kidney and intestine in mammals. A rat liver Fru-1,6-Pase cDNA was readily cloned and sequenced. Complementary PCR experiments revealed full-length Fru-1,6-Pase cDNA also present in the human liver library, however at a low abundance. Two human liver transcripts were thus characterized. Contrary to expectation, they were not differentially spliced products. They both encoded the same protein and were generated by a polyadenylation choice mechanism. The longest transcript comprised two polyadenylation signals and a consensus GT-rich element for the 3' processing of the upstream site. Rapid amplification of cDNA ends-polymerase chain reaction (RACE-PCR) analysis of 3' ends from hepatic, renal and intestinal mRNA disclosed that both Fru-1,6-Pase transcripts are expressed in the three main gluconeogenic cell types and are subject to insulin differential modulation. On the other hand, overcoming liver cell heterogeneity problems, sequence analysis of 16 independent clones of 3' end-cDNA demonstrated that, in addition to a monocytic type corresponding to a previously described lambda gt11 clone, human liver does not contain a hepatic type Fru-1,6-Pase comprising a liver-specific carboxyl-terminal extension like its rat counterpart. This liver-specific extension is involved in enzyme up-regulation and appears to give a conclusive advantage to the rat hepatic enzyme over the human one when trans-complementing mutant yeast.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Bertolotti R, Armbruster-Hilbert L, Okayama H","authors_abbrev":"Bertolotti R et al.","pubmed_publication_date":"Jul 1995","pubmed_entrez_date":"1995-07-01","publication_year":"1995","canto_session_key":"ce1953ef136c0cdf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 14:22:31","canto_session_submitted_date":"2012-03-03 14:22:10","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1198.14c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"EMBL:SPD262","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5311945","title":"Repair of prelethal and premutational damages in Schizosaccharomyces pombe.","citation":"Antonie Van Leeuwenhoek 1969 Jun;35:Suppl:C15-6","abstract":"","authors":"Loprieno N, Guglielminetti R","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"Jun 1969","pubmed_entrez_date":"1969-06-01","publication_year":"1969","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22768388","title":"Translational control of cell division by Elongator.","citation":"Cell Rep 2012 May 31;1(5):424-33","abstract":"Elongator is required for the synthesis of the mcm(5)s(2) modification found on tRNAs recognizing AA-ending codons. In order to obtain a global picture of the role of Elongator in translation, we used reverse protein arrays to screen the fission yeast proteome for translation defects. Unexpectedly, this revealed that Elongator inactivation mainly affected three specific functional groups including proteins implicated in cell division. The absence of Elongator results in a delay in mitosis onset and cytokinesis defects. We demonstrate that the kinase Cdr2, which is a central regulator of mitosis and cytokinesis, is under translational control by Elongator due to the Lysine codon usage bias of the cdr2 coding sequence. These findings uncover a mechanism by which the codon usage, coupled to tRNA modifications, fundamentally contributes to gene expression and cellular functions.","authors":"Bauer F, Matsuyama A, Candiracci J, Dieu M, Scheliga J, Wolf DA, Yoshida M, Hermand D","authors_abbrev":"Bauer F et al.","pubmed_publication_date":"31 May 2012","pubmed_entrez_date":"2012-07-07","publication_year":"2012","canto_session_key":"496a21574b3d3a26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-04-17 19:43:43","canto_approved_date":"2022-08-17 18:12:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-05 13:49:20","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":57,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPCC11E10.06c","SPBC2G5.03","SPAC18G6.02c","SPBC3H7.10","SPAC6F12.09","SPAC24H6.05","SPBC36.07","SPATRNALYS.03","SPBTRNALYS.06","SPAC29A4.20","SPATRNALYS.02","SPAC57A10.02","SPCC736.11","SPBC11B10.09"],"gene_count":15,"ltp_gene_count":9,"approved_date":"2017-04-17"},{"uniquename":"EMBL:AJ632007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.41"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29316864","title":"Overexpression of the transcription factor Rst2 in Schizosaccharomyces pombe indicates growth defect, mitotic defects, and microtubule disorder.","citation":"Biosci Biotechnol Biochem 2018 Feb;82(2):247-257","abstract":"In Schizosaccharomyces pombe, the transcription factor Rst2 regulates ste11 in meiosis and fbp1 in glucogenesis downstream of the cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) pathway. Here, we demonstrate that Rst2 regulates additional cellular events. Overexpressed Rst2 elevated the frequency of oval, bent, branched, septated, and multi-septated cells. Cells showed normal nuclear divisions but exhibited abnormal nuclear organization at low frequency. In oval cells, microtubules were curved but they were rescued by the deletion of mal3. Since growth defect was not rescued by mal3 deletion, we argue that it is regulated independently. Loss of functional Pka1 exaggerated growth defect upon Rst2 overexpression because its downregulation by Pka1 was lost. Overexpression of Rst2 also caused sensitivity to KCl and CaCl 2 . These findings suggest that, in addition to meiosis and glucogenesis, Rst2 is involved in cellular events such as regulation of cell growth, cell morphology, mitosis progression, microtubules structure, nuclear structure, and stress response.","doi":"10.1080/09168451.2017.1415126","authors":"Takenaka K, Tanabe T, Kawamukai M, Matsuo Y","authors_abbrev":"Takenaka K et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2018-01-11","publication_year":"2018","canto_session_key":"c796a227230bddce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Matsuo","canto_first_approved_date":"2018-02-09 14:58:08","canto_approved_date":"2024-03-20 14:39:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-22 03:26:52","canto_added_date":"2018-01-12 01:15:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Yasuhiro Matsuo","community_curator":true,"annotation_count":20,"orcid":"0000-0002-2858-7179","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.02","SPAC18G6.15","SPAC8C9.03","SPBC106.10","SPBC32C12.02"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-02-09"},{"uniquename":"PMID:9264467","title":"Calmodulin localizes to the spindle pole body of Schizosaccharomyces pombe and performs an essential function in chromosome segregation.","citation":"J Cell Sci 1997 Aug;110 ( Pt 15):1805-12","abstract":"The essential calmodulin genes in both Saccharomyces cerevisiae and Schizosaccharomyces pombe were precisely replaced with genes encoding fusions between calmodulin and the green fluorescent protein (GFP). In living budding yeast the GFP-calmodulin fusion protein (GFP-Cmd1p) localized simultaneously to sites of cell growth and to the spindle pole body (SPB), the yeast analog of the centrosome. Having demonstrated proper localization of GFP-calmodulin in budding yeast, we examined the localization of a fusion between GFP and calmodulin (GFP-Camlp) in fission yeast, where calmodulin had not been localized by any method. We find GFP-Camlp also localizes both to sites of polarized cell growth and to the fission yeast SPB. The localization of calmodulin to the SPB by GFP fusion was confirmed by indirect immunofluorescence. Antiserum to S. pombe calmodulin labeled the ends of the mitotic spindle stained with anti-tubulin antiserum. This pattern was identical to that seen using antiserum to Sad1p, a known SPB component. We then characterized the defects in a temperature-sensitive S. pombe calmodulin mutant. Mutant cam1-E14 cells synchronized in S phase completed DNA synthesis, but lost viability during transit of mitosis. Severe defects in chromosome segregation, including hypercondensation, fragmentation, and unequal allocation of chromosomal material were observed. Immunofluorescence analysis of tubulin revealed a population of cells containing either broken or mislocalized mitotic spindles, which were never observed in wild-type cells. Taken together with the subcellular localization of calmodulin, the observed spindle and chromosome segregation defects suggest that calmodulin performs an essential role during mitosis at the fission yeast SPB.","authors":"Moser MJ, Flory MR, Davis TN","authors_abbrev":"Moser MJ et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"14430dbee89c6c54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-07 16:07:15","canto_approved_date":"2019-05-10 09:19:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-06-04 09:42:20","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-03-07"},{"uniquename":"EMBL:SPC04594","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27322068","title":"A family of metal-dependent phosphatases implicated in metabolite damage-control.","citation":"Nat Chem Biol 2016 Aug;12(8):621-7","abstract":"DUF89 family proteins occur widely in both prokaryotes and eukaryotes, but their functions are unknown. Here we define three DUF89 subfamilies (I, II, and III), with subfamily II being split into stand-alone proteins and proteins fused to pantothenate kinase (PanK). We demonstrated that DUF89 proteins have metal-dependent phosphatase activity against reactive phosphoesters or their damaged forms, notably sugar phosphates (subfamilies II and III), phosphopantetheine and its S-sulfonate or sulfonate (subfamily II-PanK fusions), and nucleotides (subfamily I). Genetic and comparative genomic data strongly associated DUF89 genes with phosphoester metabolism. The crystal structure of the yeast (Saccharomyces cerevisiae) subfamily III protein YMR027W revealed a novel phosphatase active site with fructose 6-phosphate and Mg(2+) bound near conserved signature residues Asp254 and Asn255 that are critical for activity. These findings indicate that DUF89 proteins are previously unrecognized hydrolases whose characteristic in vivo function is to limit potentially harmful buildups of normal or damaged phosphometabolites.","doi":"10.1038/nchembio.2108","authors":"Huang L, Khusnutdinova A, Nocek B, Brown G, Xu X, Cui H, Petit P, Flick R, Zallot R, Balmant K, Ziemak MJ, Shanklin J, de Crécy-Lagard V, Fiehn O, Gregory JF, Joachimiak A, Savchenko A, Yakunin AF, Hanson AD","authors_abbrev":"Huang L et al.","pubmed_publication_date":"Aug 2016","pubmed_entrez_date":"2016-06-21","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1393.13","SPAC806.04c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:32190820","title":"RPA and Pif1 cooperate to remove G-rich structures at both leading and lagging strand.","citation":"Cell Stress 2020 Jan 17;4(3):48-63","abstract":"In  Saccharomyces cerevisiae , the absence of Pif1 helicase induces the instability of G4-containing CEB1 minisatellite during leading strand but not lagging strand replication. We report that RPA and Pif1 cooperate to maintain CEB1 stability when the G4 forming strand is either on the leading or lagging strand templates. At the leading strand, RPA acts in the same pathway as Pif1 to maintain CEB1 stability. Consistent with this result, RPA co-precipitates with Pif1. This association between Pif1 and RPA is affected by the  rfa1-D228Y  mutation that lowers the affinity of RPA in particular for G-rich single-stranded DNA. At the lagging strand, in contrast to  pif1 Δ, the  rfa1-D228Y  mutation strongly increases the frequency of CEB1 rearrangements. We explain that Pif1 is dispensable at the lagging strand DNA by the ability of RPA by itself to prevent formation of stable G-rich secondary structures during lagging strand synthesis. Remarkably, overexpression of Pif1 rescues the instability of CEB1 at the lagging strand in the  rfa1-D228Y  mutant indicating that Pif1 can also act at the lagging strand. We show that the effects of the  rfa1-D228Y  ( rpa1-D223Y  in fission yeast) are conserved in  Schizosaccharomyces pombe . Finally, we report that RNase H1 interacts in a DNA-dependent manner with RPA in budding yeast, however overexpression of RNase H1 does not rescue CEB1 instability observed in  pif1 Δ and  rfa1-D228Y  mutants. Collectively these results add new insights about the general role of RPA in preventing formation of DNA secondary structures and in coordinating the action of factors aimed at resolving them.","doi":"10.15698/cst2020.03.214","authors":"Maestroni L, Audry J, Luciano P, Coulon S, Géli V, Corda Y","authors_abbrev":"Maestroni L et al.","pubmed_publication_date":"17 Jan 2020","pubmed_entrez_date":"2020-03-20","publication_year":"2020","canto_session_key":"522ca528a6db2d91","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-03-21 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24704079","title":"Activation of the γ-tubulin complex by the Mto1/2 complex.","citation":"Curr Biol 2014 Apr 14;24(8):896-903","abstract":"The multisubunit γ-tubulin complex (γ-TuC) is critical for microtubule nucleation in eukaryotic cells, but it remains unclear how the γ-TuC becomes active specifically at microtubule-organizing centers (MTOCs) and not more broadly throughout the cytoplasm. In the fission yeast Schizosaccharomyces pombe, the proteins Mto1 and Mto2 form the Mto1/2 complex, which interacts with the γ-TuC and recruits it to several different types of cytoplasmic MTOC sites. Here, we show that the Mto1/2 complex activates γ-TuC-dependent microtubule nucleation independently of localizing the γ-TuC. This was achieved through the construction of a \"minimal\" version of Mto1/2, Mto1/2[bonsai], that does not localize to any MTOC sites. By direct imaging of individual Mto1/2[bonsai] complexes nucleating single microtubules in vivo, we further determine the number and stoichiometry of Mto1, Mto2, and γ-TuC subunits Alp4 (GCP2) and Alp6 (GCP3) within active nucleation complexes. These results are consistent with active nucleation complexes containing ∼13 copies each of Mto1 and Mto2 per active complex and likely equimolar amounts of γ-tubulin. Additional experiments suggest that Mto1/2 multimers act to multimerize the fission yeast γ-tubulin small complex and that multimerization of Mto2 in particular may underlie assembly of active microtubule nucleation complexes.","doi":"10.1016/j.cub.2014.03.006","authors":"Lynch EM, Groocock LM, Borek WE, Sawin KE","authors_abbrev":"Lynch EM et al.","pubmed_publication_date":"14 Apr 2014","pubmed_entrez_date":"2014-04-08","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC417.07c","SPBC902.06","SPBC32F12.04"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23934882","title":"Negative functional interaction between cell integrity MAPK pathway and Rho1 GTPase in fission yeast.","citation":"Genetics 2013 Oct;195(2):421-32","abstract":"Rho1 GTPase is the main activator of cell wall glucan biosynthesis and regulates actin cytoskeleton in fungi, including Schizosaccharomyces pombe. We have obtained a fission yeast thermosensitive mutant strain carrying the rho1-596 allele, which displays reduced Rho1 GTPase activity. This strain has severe cell wall defects and a thermosensitive growth, which is partially suppressed by osmotic stabilization. In a global screening for rho1-596 multicopy suppresors the pmp1+ gene was identified. Pmp1 is a dual specificity phosphatase that negatively regulates the Pmk1 mitogen-activated protein kinase (MAPK) cell integrity pathway. Accordingly, elimination of Pmk1 MAPK partially rescued rho1-596 thermosensitivity, corroborating the unexpected antagonistic functional relationship of these genes. We found that rho1-596 cells displayed increased basal activation of the cell integrity MAPK pathway and therefore were hypersensitive to MgCl2 and FK506. Moreover, the absence of calcineurin was lethal for rho1-596. We found a higher level of calcineurin activity in rho1-596 than in wild-type cells, and overexpression of constitutively active calcineurin partially rescued rho1-596 thermosensitivity. All together our results suggest that loss of Rho1 function causes an increase in the cell integrity MAPK activity, which is detrimental to the cells and turns calcineurin activity essential.","doi":"10.1534/genetics.113.154807","authors":"Viana RA, Pinar M, Soto T, Coll PM, Cansado J, Pérez P","authors_abbrev":"Viana RA et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-08-13","publication_year":"2013","canto_session_key":"967dc28677d1eae3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pilar Perez","canto_first_approved_date":"2015-04-27 15:21:25","canto_approved_date":"2020-03-27 11:22:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-01 12:25:21","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Pilar Perez","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16.01","SPAC1F7.04","SPBC19G7.05c","SPCC830.06","SPBC119.08","SPAC24B11.06c","SPAC26F1.10c","SPCC1281.01","SPAC23C4.08","SPBP4H10.04","SPBC1685.01"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2015-04-27"},{"uniquename":"PMID:10390527","title":"Removal of cyclobutane pyrimidine dimers by the UV damage repair and nucleotide excision repair pathways of Schizosaccharomyces pombe at nucleotide resolution.","citation":"Nucleic Acids Res 1999 Jul 15;27(14):2868-74","abstract":"In Schizosaccharomyces pombe two different repair mechanisms remove UV-induced lesions from DNA, i.e. nucleotide excision repair (NER) and UV damage repair (UVDR). Here, the kinetics of removal of cyclobutane pyrimidine dimers (CPDs) by both pathways is determined at base resolution in the transcribed strand (TS) and the non-transcribed strand (NTS) of the sprpb2 +gene. UVDR does not remove lesions in a strand-specific manner, indicating that UVDR is neither stimulated nor inhibited by RNA polymerase II transcription. In contrast, in a UVDR-deficient strain the TS is repaired preferentially. This strong strand bias suggests that in S.pombe, as in other species, NER is coupled to transcription. In repair-proficient S.pombe the TS is repaired very rapidly, as a consequence of two efficiently operating pathways, while the NTS is repaired more slowly, mainly by UVDR. Furthermore, we demonstrate that UVDR is not always faster than NER.","authors":"Lombaerts M, Tijsterman M, Brandsma JA, Verhage RA, Brouwer J","authors_abbrev":"Lombaerts M et al.","pubmed_publication_date":"15 Jul 1999","pubmed_entrez_date":"1999-07-03","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.09c","SPBC3E7.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:23267073","title":"Cell cycle-dependent deposition of CENP-A requires the Dos1/2-Cdc20 complex.","citation":"Proc Natl Acad Sci U S A 2013 Jan 08;110(2):606-11","abstract":"Centromeric histone CENP-A, a variant of canonical histone H3, plays a central role in proper chromosome segregation. Loading of CENP-A at centromeres is cell cycle-regulated: parental CENP-A is deposited at centromeres during S phase, whereas newly synthesized CENP-A is deposited during later stages of the cell cycle. The mechanisms involved in deposition of CENP-A at centromeres during S phase remain poorly understood. In fission yeast, loading of CENP-A during S phase is regulated by the GATA-type factor, Ams2. Here we show that the Dos1/2-Cdc20 complex, previously characterized as a silencing complex essential for inheritance of H3K9 methylation during S phase, is also required for localization of CENP-A(cnp1) at centromeres at this stage. Disruption of Dos1 (also known as Raf1/Clr8/Cmc1), Dos2 (also known as Raf2/Clr7/Cmc2), or Cdc20, a DNA polymerase epsilon subunit, results in dissociation of CENP-A from centromeres and mislocalization of the protein to noncentromeric sites. All three mutants display spindle disorganization and mitotic defects. Inactivation of Dos1 or Cdc20 also results in accumulation of noncoding RNA transcripts from centromeric cores, a feature common to mutants affecting kinetochore integrity. We further find that Dos1 physically associates with Ams2 and is required for the association of Ams2 with centromeric cores during S phase. Finally, we show that Dos2 associates with centromeric cores during S phase and that its recruitment to centromeric cores depends on Cdc20. This study identifies a physical link between DNA replication and CENP-A assembly machinery and provides mechanistic insight into how CENP-A is faithfully inherited during S phase.","doi":"10.1073/pnas.1214874110","authors":"Gonzalez M, He H, Sun S, Li C, Li F","authors_abbrev":"Gonzalez M et al.","pubmed_publication_date":"08 Jan 2013","pubmed_entrez_date":"2012-12-26","publication_year":"2013","canto_session_key":"3f4a98f0a3fa938f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"fl43","canto_first_approved_date":"2018-02-14 16:21:11","canto_approved_date":"2021-12-06 20:16:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-24 21:59:37","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":46,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"fl43","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.20c","SPBC1861.01c","SPBC25H2.13c","SPCC613.12c","SPCC290.04","SPCC970.07c","SPBC1105.17"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2018-02-14"},{"uniquename":"PMID:22456315","title":"New insights into the SAGA complex from studies of the Tra1 subunit in budding and fission yeast.","citation":"Transcription 2012;3(1):13-8","abstract":"The SAGA complex is a conserved, multifunctional co-activator that controls the transcription of many inducible genes in response to environmental changes. Recent studies have provided new insights into the functions of one of its subunits, Tra1/TRRAP, and suggest that it controls SAGA activity in response to external stimuli.","doi":"10.4161/trns.3.1.19271","authors":"Helmlinger D","authors_abbrev":"Helmlinger D","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-03-30","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20015352","title":"Global transcriptional response after exposure of fission yeast cells to ultraviolet light.","citation":"BMC Cell Biol 2009 Dec 16;10:87","abstract":"In many cell types, including the fission yeast Schizosaccharomyces pombe, a set of checkpoints are induced by perturbations of the cell cycle or by DNA damage. Many of the checkpoint responses include a substantial change of the transcriptional pattern. As part of characterising a novel G1/S checkpoint in fission yeast we have investigated whether a transcriptional response is induced after irradiation with ultraviolet light.\nMicroarray analyses were used to measure the global transcription levels of all open reading frames of fission yeast after 254 nm ultraviolet irradiation, which is known to induce a G1/S checkpoint. We discovered a surprisingly weak transcriptional response, which is quite unlike the marked changes detected after some other types of treatment and in several other checkpoints. Interestingly, the alterations in gene expression after ultraviolet irradiation were not similar to those observed after ionising radiation or oxidative stress. Pathway analysis suggests that there is little systematic transcriptional response to the irradiation by ultraviolet light, but a marked, coordinated transcriptional response was noted on progression of the cells from G1 to S phase.\nThere is little response in fission yeast to ultraviolet light at the transcriptional level. Amongst the genes induced or repressed after ultraviolet irradiation we found none that are likely to be involved in the G1/S checkpoint mechanism, suggesting that the checkpoint is not dependent upon transcriptional regulation.","doi":"10.1186/1471-2121-10-87","authors":"Skjølberg HC, Fensgård O, Nilsen H, Grallert B, Boye E","authors_abbrev":"Skjølberg HC et al.","pubmed_publication_date":"16 Dec 2009","pubmed_entrez_date":"2009-12-18","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29975157","title":"Analysis of the contribution of phosphoinositides to medial septation in fission yeast highlights the importance of PI(4,5)P 2  for medial contractile ring anchoring.","citation":"Mol Biol Cell 2018 Sep 01;29(18):2148-2155","abstract":"In Schizosaccharomyces pombe, loss of the plasma membrane PI4-kinase scaffold Efr3 leads to sliding of the cytokinetic ring (CR) away from the cell center during anaphase, implicating phosphoinositides (PIPs) in CR anchoring. However, whether other PIP regulators contribute to CR anchoring has not been investigated. Here we report that mutants of other PIP kinases and their regulators divide with off-center septa, similar to efr3∆. Using new biosensors for S. pombe PIPs, we confirm that these mutants have disrupted PIP composition. We extend a previous finding that a mutant known to decrease PI(3,5)P 2  levels indirectly affects CR positioning by increasing vacuole size which disrupts nuclear position at the onset of mitosis. Indeed, we found that other mutants with increased vacuole size also disrupt medial division via this mechanism. Although elevated plasma membrane PI(4,5)P 2  levels do not affect medial cytokinesis, mutants with decreased levels display CR sliding events indicating a specific role for PI(4,5)P 2  in CR anchoring.","doi":"10.1091/mbc.E18-03-0179","authors":"Snider CE, Willet AH, Brown HT, Gould KL","authors_abbrev":"Snider CE et al.","pubmed_publication_date":"01 Sep 2018","pubmed_entrez_date":"2018-07-06","publication_year":"2018","canto_session_key":"260be70a4dcbc884","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chloe Snider","canto_first_approved_date":"2018-07-17 15:57:31","canto_approved_date":"2024-09-11 07:12:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-10 20:16:57","canto_added_date":"2018-07-07 00:15:04","annotation_curators":[{"name":"Chloe Snider","community_curator":true,"annotation_count":45,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC343.19","SPBC609.02","SPAC9G1.10c","SPAC19A8.03","SPAC19G12.14","SPBC3E7.01","SPBC577.13","SPCPB16A4.02c","SPAC5D6.07c","SPAC458.05","SPAC18B11.04","SPCC645.07","SPAC20G8.05c","SPAC1093.03","SPAC16E8.09","SPCC16A11.01","SPBC2G2.02","SPAC3H1.09c","SPCC794.08","SPAC3C7.01c","SPBC577.06c","SPBC25H2.03"],"gene_count":22,"ltp_gene_count":18,"approved_date":"2018-07-17"},{"uniquename":"PMID:22226946","title":"The Ubiquitin ligase Ubr11 is essential for oligopeptide utilization in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2012 Mar;11(3):302-10","abstract":"Uptake of extracellular oligopeptides in yeast is mediated mainly by specific transporters of the peptide transporter (PTR) and oligopeptide transporter (OPT) families. Here, we investigated the role of potential peptide transporters in the yeast Schizosaccharomyces pombe. Utilization of naturally occurring dipeptides required only Ptr2/SPBC13A2.04c and none of the other 3 OPT proteins (Isp4, Pgt1, and Opt3), whereas only Isp4 was indispensable for tetrapeptide utilization. Both Ptr2 and Isp4 localized to the cell surface, but under rich nutrient conditions Isp4 localized in the Golgi apparatus through the function of the ubiquitin ligase Pub1. Furthermore, the ubiquitin ligase Ubr11 played a significant role in oligopeptide utilization. The mRNA levels of both the ptr2 and isp4 genes were significantly reduced in ubr11Δ cells, and the dipeptide utilization defect in the ubr11Δ mutant was rescued by the forced expression of Ptr2. Consistent with its role in transcriptional regulation of peptide transporter genes, the Ubr11 protein was accumulated in the nucleus. Unlike the situation in Saccharomyces cerevisiae, the oligopeptide utilization defect in the S. pombe ubr11Δ mutant was not rescued by inactivation of the Tup11/12 transcriptional corepressors, suggesting that the requirement for the Ubr ubiquitin ligase in the upregulation of peptide transporter mRNA levels is conserved in both yeasts; however, the actual mechanism underlying the control appears to be different. We also found that the peptidomimetic proteasome inhibitor MG132 was still operative in a strain lacking all known PTR and OPT peptide transporters. Therefore, irrespective of its peptide-like structure, MG132 is carried into cells independently of the representative peptide transporters.","doi":"10.1128/EC.05253-11","authors":"Kitamura K, Nakase M, Tohda H, Takegawa K","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"Mar 2012","pubmed_entrez_date":"2012-01-10","publication_year":"2012","canto_session_key":"4ddf3364ed97a8f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-12-05 17:28:01","canto_approved_date":"2022-01-05 15:22:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-24 14:11:11","canto_added_date":"2012-02-17 18:22:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC13A2.04c","SPAC18B11.10","SPAC29B12.10c","SPAC630.14c","SPBC19C7.02","SPAC11G7.02","SPBC29B5.02c","SPCC1840.12","SPAC15A10.11"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2017-12-05"},{"uniquename":"PMID:22988247","title":"Identification of novel α1,3-galactosyltransferase and elimination of α-galactose-containing glycans by disruption of multiple α-galactosyltransferase genes in Schizosaccharomyces pombe.","citation":"J Biol Chem 2012 Nov 09;287(46):38866-75","abstract":"The oligosaccharides from fission yeast Schizosaccharomyces pombe contain large amounts of D-galactose (Gal) in addition to D-mannose (Man), in contrast to the budding yeast Saccharomyces cerevisiae. Detailed structural analysis has revealed that the Gal residues are attached to the N- and O-linked oligosaccharides via α1,2- or α1,3-linkages. Previously we constructed and characterized a septuple α-galactosyltransferase disruptant (7GalTΔ) anticipating a complete lack of α-Gal residues. However, the 7GalTΔ strain still contained oligosaccharides consisting of α1,3-linked Gal residues, indicating the presence of at least one more additional unidentified α1,3-galactosyltransferase. In this study we searched for unidentified putative glycosyltransferases in the S. pombe genome sequence and identified three novel genes, named otg1(+)-otg3(+) (α one, three-galactosyltransferase), that belong to glycosyltransferase gene family 8 in the Carbohydrate Active EnZymes (CAZY) database. Gal-recognizing lectin blotting and HPLC analyses of pyridylaminated oligosaccharides after deletion of these three additional genes from 7GalTΔ strain demonstrated that the resultant disruptant missing 10 α-galactosyltransferase genes, 10GalTΔ, exhibited a complete loss of galactosylation. In an in vitro galactosylation assay, the otg2(+) gene product had Gal transfer activity toward a pyridylaminated Man(9)GlcNAc(2) oligosaccharide and pyridylaminated Manα1,2-Manα1,2-Man oligosaccharide. In addition, the otg3(+) gene product exhibited Gal transfer activity toward the pyridylaminated Man(9)GlcNAc(2) oligosaccharide. Generation of an α1,3-linkage was confirmed by HPLC analysis, α-galactosidase digestion analysis, (1)H NMR spectroscopy, and LC-MS/MS analysis. These results indicate that Otg2p and Otg3p are involved in α1,3-galactosylation of S. pombe oligosaccharides.","doi":"10.1074/jbc.M112.347351","authors":"Ohashi T, Fujiyama K, Takegawa K","authors_abbrev":"Ohashi T et al.","pubmed_publication_date":"09 Nov 2012","pubmed_entrez_date":"2012-09-19","publication_year":"2012","canto_session_key":"0e85b84df580612d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2017-11-08 14:55:38","canto_approved_date":"2021-06-02 10:21:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-01 07:44:13","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":30,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.06c","SPAC5H10.13c","SPAC637.06","SPBC4C3.08","SPBC4C3.09","SPCC1795.03","SPBC1289.13c","SPCC736.04c","SPAC1006.05c","SPAC5H10.12c","SPAC5H10.11","SPBC8D2.17"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2017-11-08"},{"uniquename":"PMID:17248713","title":"Mating-Type Mutations in SCHIZOSACCHAROMYCES POMBE: Isolation of Mutants and Analysis of Strains with an h or h Phenotype.","citation":"Genetics 1976 Jun;83(2):259-73","abstract":"Mutants defective in various steps of the sexual cycle have been isolated from homothallic strains of Schizosaccharomyces pombe by Bresch, Müller and Egel (1968). These mutants include heterothallic h(+) and h(-) strains. We have isolated additional h(+) and h(- ) mutants from homothallic strains. Those mutants which are due to mutations in the mating-type region were analyzed in detail. Our results show that the mating-type gene mat2 not only has a function in copulation and meiosis, but that it also regulates the formation of the map1 gene product (map1 is a mating-type auxiliary gene). Some of the h( -) mutants have lost only one of the three functions while others are defective in at least two, and perhaps all three, functions. Further, we show that the mat1(-) allele of h(90) strains can mutate to mat1(+) but that mutations in mat2 appear to affect the mutational behavior of mat1. Finally, we describe a new inactive mating-type allele, mat2*, which is different from mat2(0) in that it can mutate to mat2(+).","authors":"Meade JH, Gutz H","authors_abbrev":"Meade JH et al.","pubmed_publication_date":"Jun 1976","pubmed_entrez_date":"1976-06-01","publication_year":"1976","canto_session_key":"f033fde52b328f44","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-05-10 14:38:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-10 14:38:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-05-10"},{"uniquename":"PMID:12615927","title":"Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins.","citation":"J Biol Chem 2003 May 09;278(19):16791-6","abstract":"Fission yeast Rhp23 and Pus1 represent two families of multiubiquitin chain-binding proteins that associate with the proteasome. We show that both proteins bind to different regions of the proteasome subunit Mts4. The binding site for Pus1 was mapped to a cluster of repetitive sequences also found in the proteasome subunit SpRpn2 and the anaphase-promoting complex/cyclosome (APC/C) subunit Cut4. The putative role of Pus1 as a factor involved in allocation of ubiquitinylated substrates for the proteasome is discussed.","authors":"Seeger M, Hartmann-Petersen R, Wilkinson CR, Wallace M, Samejima I, Taylor MS, Gordon C","authors_abbrev":"Seeger M et al.","pubmed_publication_date":"09 May 2003","pubmed_entrez_date":"2003-03-05","publication_year":"2003","canto_session_key":"250962459bf6bd5e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-18 13:44:54","canto_approved_date":"2021-10-30 17:05:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-03 13:32:11","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":39,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.09","SPCC1442.07c","SPBP19A11.03c","SPBC2D10.12","SPAC637.10c","SPAC6F12.15c","SPBC4.07c","SPBC17D11.07c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-01-18"},{"uniquename":"PMID:23658229","title":"Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast.","citation":"Nucleic Acids Res 2013 Jul;41(13):6674-86","abstract":"Zinc-finger domains are found in many nucleic acid-binding proteins in both prokaryotes and eukaryotes. Proteins carrying zinc-finger domains have important roles in various nuclear transactions, including transcription, mRNA processing and mRNA export; however, for many individual zinc-finger proteins in eukaryotes, the exact function of the protein is not fully understood. Here, we report that Red5 is involved in efficient suppression of specific mRNAs during vegetative growth of Schizosaccharomyces pombe. Red5, which contains five C3H1-type zinc-finger domains, localizes to the nucleus where it forms discrete dots. A red5 point mutation, red5-2, results in the upregulation of specific meiotic mRNAs in vegetative mutant red5-2 cells; northern blot data indicated that these meiotic mRNAs in red5-2 cells have elongated poly(A) tails. RNA-fluorescence in situ hybridization results demonstrate that poly(A)(+) RNA species accumulate in the nucleolar regions of red5-deficient cells. Moreover, Red5 genetically interacts with several mRNA export factors. Unexpectedly, three components of the nuclear pore complex also suppress a specific set of meiotic mRNAs. These results indicate that Red5 function is important to meiotic mRNA degradation; they also suggest possible connections among selective mRNA decay, mRNA export and the nuclear pore complex in vegetative fission yeast.","doi":"10.1093/nar/gkt363","authors":"Sugiyama T, Wanatabe N, Kitahata E, Tani T, Sugioka-Sugiyama R","authors_abbrev":"Sugiyama T et al.","pubmed_publication_date":"Jul 2013","pubmed_entrez_date":"2013-05-10","publication_year":"2013","canto_session_key":"bdc65ab8c484c62c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-20 16:08:07","canto_approved_date":"2022-02-16 16:21:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-17 08:26:38","canto_added_date":"2013-05-14 09:18:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":129,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15F9.02","SPBC359.02","SPBP35G2.06c","SPBC2G2.09c","SPBC1347.12","SPBC106.12c","SPBP8B7.04","SPAC750.07c","SPCC285.13c","SPAC19D5.04","SPBC2D10.06","SPAC17A5.18c","SPBC29A10.14","SPBC216.02","SPAC57A10.04","SPAC19E9.01c","SPBC16E9.12c","SPCC70.06","SPBC29A10.07","SPAC1556.06","SPCC1840.01c","SPBC3B9.16c","SPBC1711.14","SPAC32A11.01","SPBC582.06c","SPBC6B1.12c","SPAC1F3.01","SPAC30D11.04c","SPBC16A3.05c","SPBC337.12","SPBC32H8.11","SPAC212.08c","SPNCRNA.103","SPAC3G6.02","SPCC330.03c","SPCC70.09c","SPAC1F8.05","SPBC646.17c","SPBC1271.06c","SPAC222.15","SPCC31H12.03c","SPAC17G6.14c","SPBC1D7.04","SPCC1739.14","SPAC1006.03c","SPCC4E9.01c","SPAC212.06c","SPAP27G11.08c","SPAC14C4.03","SPAC15E1.07c","SPAC140.02","SPCC622.08c","SPBC1921.03c","SPAC27D7.13c","SPBC29A10.02","SPBC1289.14","SPBP4G3.03","SPAC17H9.18c","SPAC328.05"],"gene_count":59,"ltp_gene_count":24,"approved_date":"2015-05-20"},{"uniquename":"PMID:31895039","title":"The CDK Pef1 and protein phosphatase 4 oppose each other for regulating cohesin binding to fission yeast chromosomes.","citation":"Elife 2020 Jan 02;9","abstract":"Cohesin has essential roles in chromosome structure, segregation and repair. Cohesin binding to chromosomes is catalyzed by the cohesin loader, Mis4 in fission yeast. How cells fine tune cohesin deposition is largely unknown. Here, we provide evidence that Mis4 activity is regulated by phosphorylation of its cohesin substrate. A genetic screen for negative regulators of Mis4 yielded a CDK called Pef1, whose closest human homologue is CDK5. Inhibition of Pef1 kinase activity rescued cohesin loader deficiencies. In an otherwise wild-type background, Pef1 ablation stimulated cohesin binding to its regular sites along chromosomes while ablating Protein Phosphatase 4 had the opposite effect. Pef1 and PP4 control the phosphorylation state of the cohesin kleisin Rad21. The CDK phosphorylates Rad21 on Threonine 262. Pef1 ablation, non-phosphorylatable Rad21-T262 or mutations within a Rad21 binding domain of Mis4 alleviated the effect of PP4 deficiency. Such a CDK/PP4-based regulation of cohesin loader activity could provide an efficient mechanism for translating cellular cues into a fast and accurate cohesin response.","doi":"10.7554/eLife.50556","authors":"Birot A, Tormos-Pérez M, Vaur S, Feytout A, Jaegy J, Alonso Gil D, Vazquez S, Ekwall K, Javerzat JP","authors_abbrev":"Birot A et al.","pubmed_publication_date":"02 Jan 2020","pubmed_entrez_date":"2020-01-03","publication_year":"2020","canto_session_key":"cfc48f029a6c9660","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jean-Paul Javerzat","canto_first_approved_date":"2020-11-04 17:54:30","canto_approved_date":"2024-11-28 17:01:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-10-19 09:31:35","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Jean-Paul Javerzat","community_curator":true,"annotation_count":58,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPCC338.17c","SPAC10F6.09c","SPAC1687.18c","SPBC29A10.04","SPCC16C4.11","SPAC664.01c","SPBC26H8.05c","SPAC19E9.03","SPBC16A3.11","SPBC1D7.03","SPBC20F10.10"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2020-11-04"},{"uniquename":"PMID:17306542","title":"Interphase microtubules determine the initial alignment of the mitotic spindle.","citation":"Curr Biol 2007 Mar 06;17(5):438-44","abstract":"In the fission yeast Schizosaccharomyces pombe, interphase microtubules (MTs) position the nucleus [1, 2], which in turn positions the cell-division plane [1, 3]. It is unclear how the spindle orients, with respect to the predetermined division plane, to ensure that the chromosomes are segregated across this plane. It has been proposed that, during prometaphase, the astral MT interaction with the cell cortex aligns the spindle with the cell axis [4] and also participates in a spindle orientation checkpoint (SOC), which delays entry into anaphase as long as the spindle is misaligned [5-7]. Here, we trace the position of the spindle throughout mitosis in a single-cell assay. We find no evidence for the SOC. We show that the spindle is remarkably well aligned with the cell longitudinal axis at the onset of mitosis, by growing along the axis of the adjacent interphase MT. Misalignment of nascent spindles can give rise to anucleate cells when spindle elongation is impaired. We propose a new role for interphase microtubules: through interaction with the spindle pole body, interphase microtubules determine the initial alignment of the spindle in the subsequent cell division.","authors":"Vogel SK, Raabe I, Dereli A, Maghelli N, Tolić-Nørrelykke I","authors_abbrev":"Vogel SK et al.","pubmed_publication_date":"06 Mar 2007","pubmed_entrez_date":"2007-02-20","publication_year":"2007","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19563128","title":"Monitoring homologous recombination following replication fork perturbation in the fission yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2009;521:535-52","abstract":"Replication forks (RFs) frequently encounter barriers or lesions in template DNA that can cause them to stall and/or break. Efficient genome duplication therefore depends on multiple mechanisms that variously act to stabilize, repair, and restart perturbed RFs. Integral to at least some of these mechanisms are homologous recombination (HR) proteins, but our knowledge of how they act to ensure high-fidelity genome replication remains incomplete. To help better understand the relationship between DNA replication and HR, fission yeast strains have been engineered to contain intrachromosmal recombination substrates consisting of non-tandem direct repeats of ade6 heteroalleles. The substrates have been modified to include site-specific RF barriers within the duplication. Importantly, direct repeat recombinants appear to arise predominantly during DNA replication via sister chromatid interactions and are induced by factors that perturb RFs. Using simple plating experiments to assay recombinant formation, these strains have proved to be useful tools in monitoring the effects of impeding RFs on HR and its genetic control. The strains are available on request, and here we describe in detail how some of them can be used to determine the effect of your mutation of choice on spontaneous, DNA damage-induced, and replication block-induced recombinant formation.","doi":"10.1007/978-1-60327-815-7_31","authors":"Osman F, Whitby MC","authors_abbrev":"Osman F et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23709180","title":"The fission yeast synaptobrevin ortholog Syb1 plays an important role in forespore membrane formation and spore maturation.","citation":"Eukaryot Cell 2013 Sep;12(9):1162-70","abstract":"Synaptobrevin, also called vesicle-associated membrane protein (VAMP), is a component of the plasma membrane N-methylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, which plays a key role in intracellular membrane fusion. Previous studies have revealed that, similar to synaptobrevin in other organisms, the fission yeast synaptobrevin ortholog Syb1 associates with post-Golgi secretory vesicles and is essential for cytokinesis and cell elongation. Here, we report that Syb1 has a role in sporulation. After nitrogen starvation, green fluorescent protein (GFP)-Syb1 is found in intracellular dots. As meiosis proceeds, GFP-Syb1 accumulates around the nucleus and then localizes at the forespore membrane (FSM). We isolated a syb-S1 mutant, which exhibits a defect in sporulation. In syb1-S1 mutants, the FSM begins to form but fails to develop a normal morphology. Electron microscopy shows that an abnormal spore wall is often formed in syb1-S1 mutant spores. Although most syb1-S1 mutant spores are germinated, they are less tolerant to ethanol than wild-type spores. The syb1-S1 allele carries a missense mutation, resulting in replacement of a conserved cysteine residue adjacent to the transmembrane domain, which reduces the stability and abundance of the Syb1 protein. Taken together, these results indicate that Syb1 plays an important role in both FSM assembly and spore wall formation.","doi":"10.1128/EC.00061-13","authors":"Yamaoka T, Imada K, Fukunishi K, Yamasaki Y, Shimoda C, Nakamura T","authors_abbrev":"Yamaoka T et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-05-28","publication_year":"2013","canto_session_key":"5f0299d44219d535","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Taro Nakamura","canto_first_approved_date":"2026-05-27 13:37:30","canto_approved_date":"2026-05-27 13:37:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-05-27 09:02:47","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Taro Nakamura","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC825.03c","SPBC800.05c","SPAC17A5.04c","SPAC6G9.11","SPBC26H8.02c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2026-05-27"},{"uniquename":"EMBL:AU012872","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31225876","title":"Ancestral Admixture Is the Main Determinant of Global Biodiversity in Fission Yeast.","citation":"Mol Biol Evol 2019 Sep 01;36(9):1975-1989","abstract":"Mutation and recombination are key evolutionary processes governing phenotypic variation and reproductive isolation. We here demonstrate that biodiversity within all globally known strains of Schizosaccharomyces pombe arose through admixture between two divergent ancestral lineages. Initial hybridization was inferred to have occurred ∼20-60 sexual outcrossing generations ago consistent with recent, human-induced migration at the onset of intensified transcontinental trade. Species-wide heritable phenotypic variation was explained near-exclusively by strain-specific arrangements of alternating ancestry components with evidence for transgressive segregation. Reproductive compatibility between strains was likewise predicted by the degree of shared ancestry. To assess the genetic determinants of ancestry block distribution across the genome, we characterized the type, frequency, and position of structural genomic variation using nanopore and single-molecule real-time sequencing. Despite being associated with double-strand break initiation points, over 800 segregating structural variants exerted overall little influence on the introgression landscape or on reproductive compatibility between strains. In contrast, we found strong ancestry disequilibrium consistent with negative epistatic selection shaping genomic ancestry combinations during the course of hybridization. This study provides a detailed, experimentally tractable example that genomes of natural populations are mosaics reflecting different evolutionary histories. Exploiting genome-wide heterogeneity in the history of ancestral recombination and lineage-specific mutations sheds new light on the population history of S. pombe and highlights the importance of hybridization as a creative force in generating biodiversity.","doi":"10.1093/molbev/msz126","authors":"Tusso S, Nieuwenhuis BPS, Sedlazeck FJ, Davey JW, Jeffares DC, Wolf JBW","authors_abbrev":"Tusso S et al.","pubmed_publication_date":"01 Sep 2019","pubmed_entrez_date":"2019-06-22","publication_year":"2019","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2019-06-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34688247","title":"Using multi-layer perceptron to identify origins of replication in eukaryotes via informative features.","citation":"BMC Bioinformatics 2021 Oct 23;22(1):516","abstract":"The origin is the starting site of DNA replication, an extremely vital part of the informational inheritance between parents and children. More importantly, accurately identifying the origin of replication has great application value in the diagnosis and treatment of diseases related to genetic information errors, while the traditional biological experimental methods are time-consuming and laborious.\nWe carried out research on the origin of replication in a variety of eukaryotes and proposed a unique prediction method for each species. Throughout the experiment, we collected data from 7 species, including Homo sapiens, Mus musculus, Drosophila melanogaster, Arabidopsis thaliana, Kluyveromyces lactis, Pichia pastoris and Schizosaccharomyces pombe. In addition to the commonly used sequence feature extraction methods PseKNC-II and Base-content, we designed a feature extraction method based on TF-IDF. Then the two-step method was utilized for feature selection. After comparing a variety of traditional machine learning classification models, the multi-layer perceptron was employed as the classification algorithm. Ultimately, the data and codes involved in the experiment are available at https://github.com/Sarahyouzi/EukOriginPredict .\nThe prediction accuracy of the training set of the above-mentioned seven species after 100 times fivefold cross validation reach 92.60%, 90.80%, 91.22%, 96.15%, 96.72%, 99.86%, 96.72%, respectively. It denotes that compared with other methods, the methods we designed could accomplish superior performance. In addition, our experiments reveals that the models of multiple species could predict each other with high accuracy, and the results of STREME shows that they have a certain common motif.","doi":"10.1186/s12859-021-04431-x","authors":"Fan Y, Wang W","authors_abbrev":"Fan Y et al.","pubmed_publication_date":"23 Oct 2021","pubmed_entrez_date":"2021-10-24","publication_year":"2021","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2021-10-27 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR014430","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19G12.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:36108046","title":"Recovery from spindle checkpoint-mediated arrest requires a novel Dnt1-dependent APC/C activation mechanism.","citation":"PLoS Genet 2022 Sep;18(9):e1010397","abstract":"The activated spindle assembly checkpoint (SAC) potently inhibits the anaphase-promoting complex/cyclosome (APC/C) to ensure accurate chromosome segregation at anaphase. Early studies have recognized that the SAC should be silenced within minutes to enable rapid APC/C activation and synchronous segregation of chromosomes once all kinetochores are properly attached, but the underlying silencers are still being elucidated. Here, we report that the timely silencing of SAC in fission yeast requires dnt1+, which causes severe thiabendazole (TBZ) sensitivity and increased rate of lagging chromosomes when deleted. The absence of Dnt1 results in prolonged inhibitory binding of mitotic checkpoint complex (MCC) to APC/C and attenuated protein levels of Slp1Cdc20, consequently slows the degradation of cyclin B and securin, and eventually delays anaphase entry in cells released from SAC activation. Interestingly, Dnt1 physically associates with APC/C upon SAC activation. We propose that this association may fend off excessive and prolonged MCC binding to APC/C and help to maintain Slp1Cdc20 stability. This may allow a subset of APC/C to retain activity, which ensures rapid anaphase onset and mitotic exit once SAC is inactivated. Therefore, our study uncovered a new player in dictating the timing and efficacy of APC/C activation, which is actively required for maintaining cell viability upon recovery from the inhibition of APC/C by spindle checkpoint.","doi":"10.1371/journal.pgen.1010397","authors":"Bai S, Sun L, Wang X, Wang SM, Luo ZQ, Wang Y, Jin QW","authors_abbrev":"Bai S et al.","pubmed_publication_date":"Sep 2022","pubmed_entrez_date":"2022-09-15","publication_year":"2022","canto_session_key":"dcbc3aa3fb96acba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li Sun","canto_first_approved_date":"2023-01-20 17:25:36","canto_approved_date":"2024-05-16 14:18:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-01-12 02:39:42","canto_added_date":"2022-09-20 00:15:04","annotation_curators":[{"name":"Li Sun","community_curator":true,"annotation_count":22,"orcid":"0000-0003-0708-2881","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25D12.02c","SPAC589.08c","SPCC736.14","SPBC582.03","SPBC20F10.06","SPAC6F12.14","SPBC11C11.03","SPAPB1A10.09","SPBC14C8.01c","SPCC1795.01c","SPAC17C9.01c","SPBC27.02c","SPCC320.13c","SPCC962.02c","SPAC890.02c","SPAC19G12.01c","SPAC16A10.05c","SPAC821.08c","SPAC11E3.03","SPCC895.07","SPBC26H8.07c","SPBC1105.06"],"gene_count":22,"ltp_gene_count":17,"approved_date":"2023-01-20"},{"uniquename":"PMID:1500423","title":"cdc25 is a nuclear protein expressed constitutively throughout the cell cycle in nontransformed mammalian cells.","citation":"J Cell Biol 1992 Aug;118(4):785-94","abstract":"A family of proteins homologous to the cdc25 gene product of the fission yeast bear specific protein tyrosine phosphatase activity involved in the activation of the p34cdc2-cyclin B kinase. Using affinity-purified antibodies raised against a synthetic peptide corresponding to the catalytic site of the cdc25 phosphatase, we show that cdc25 protein is constitutively expressed throughout the cell cycle of nontransformed mammalian fibroblasts and does not undergo major changes in protein level. By indirect immunofluorescence, cdc25 protein is found essentially localized in the nucleus throughout interphase and during early prophase. Just before the complete nuclear envelope breakdown at the prophase-prometaphase boundary, cdc25 proteins are redistributed throughout the cytoplasm. During metaphase and anaphase, cdc25 staining remains distributed throughout the cell and excludes the condensed chromosomes. The nuclear locale reappears during telophase. In light of the recent data describing the cytoplasmic localization of cyclin B protein (Pines, J., and T. Hunter. 1991. J. Cell Biol. 115:1-17), the data presented here suggest that separation in two distinct cellular compartments of the cdc25 phosphatase and its substrate p34cdc2-cyclin B may be of importance in the regulation of the cdc2 kinase activity.","authors":"Girard F, Strausfeld U, Cavadore JC, Russell P, Fernandez A, Lamb NJ","authors_abbrev":"Girard F et al.","pubmed_publication_date":"Aug 1992","pubmed_entrez_date":"1992-08-01","publication_year":"1992","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:9339351","title":"Identification of the ure1+ gene encoding urease in fission yeast.","citation":"Curr Genet 1997 Sep;32(3):244-6","abstract":"Cloning and sequencing of the ure1+ gene of Schizosaccharomyces pombe indicated that it encodes the urease which had been biochemically identified. The fission yeast urease has a one-subunit structure like those from plants but different from bacterial ureases which are composed of two or three distinct subunits. Genetic analyses showed that the ure1+ gene product is actually involved in urea metabolism.","authors":"Tange Y, Niwa O","authors_abbrev":"Tange Y et al.","pubmed_publication_date":"Sep 1997","pubmed_entrez_date":"1997-10-27","publication_year":"1997","canto_session_key":"525b70a4b9a10b41","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-30 14:27:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-30 14:27:03","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.11c","SPCC330.05c","SPBC1711.13","SPBC1A4.02c"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2015-04-30"},{"uniquename":"PMID:19915076","title":"abc3+ encodes an iron-regulated vacuolar ABC-type transporter in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2010 Jan;9(1):59-73","abstract":"Studies have shown the fundamental contribution of the yeast vacuole as a site for storage and detoxification of metals. Whereas the transmembrane proteins responsible for iron transport into and out of the vacuole have been identified in Saccharomyces cerevisiae, less information is available concerning the mobilization of vacuolar iron stores in Schizosaccharomyces pombe. In this study, we report the identification of a gene designated abc3(+) that encodes a protein which exhibits sequence homology with the ABCC subfamily of ATP-binding cassette transporters. The transcription of abc3(+) is induced by low concentrations of iron but repressed by high levels of iron. The iron-mediated repression of abc3(+) required a functional fep1(+) gene. Chromatin immunoprecipitation assays showed that Fep1 associates with the abc3(+) promoter in vivo, in an iron-dependent manner. Microscopic analyses revealed that a functional Abc3-green fluorescent protein localizes to the membrane vacuole when iron levels were low. Abc3 was required for growth in low-iron medium in the absence of the transport system mediated by Fio1 and Fip1. abc3Delta cells exhibited increased levels of expression of the frp1(+)-encoded ferric reductase, suggesting a loss of Fep1 repression and, consequently, the activation of Fep1-regulated genes. When abc3(+) was expressed using the nmt1(+) promoter system, its induction led to a reduced transcriptional activity of the frp1(+) gene. Because S. pombe does not possess vacuolar membrane-localized orthologs to S. cerevisiae Fth1, Fet5, and Smf3, our findings suggested that Abc3 may be responsible for mobilizing stored iron from the vacuole to the cytosol in response to iron deficiency.","doi":"10.1128/EC.00262-09","authors":"Pouliot B, Jbel M, Mercier A, Labbé S","authors_abbrev":"Pouliot B et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-11-17","publication_year":"2010","canto_session_key":"feedc5a07a1dde86","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-05 08:15:50","canto_approved_date":"2024-04-03 12:34:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-05 08:15:44","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.12c","SPBC1683.09c","SPBC16E9.01c","SPBC359.05","SPAC23E2.01","SPCC737.09c","SPBC1683.10c","SPAC30.04c","SPAC1F7.08","SPAC1F7.07c","SPBC4F6.09","SPAC3F10.11c"],"gene_count":12,"ltp_gene_count":5,"approved_date":"2019-06-05"},{"uniquename":"EMBL:SPC07521","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38837646","title":"The HMG-box module in FACT is critical for suppressing epigenetic variegation of heterochromatin in fission yeast.","citation":"Genes Cells 2024 Jun 05;","abstract":"Chromatin condensation state is the key for retrieving genetic information. High-mobility group protein (HMG) proteins exhibit DNA-binding and bending activities, playing an important role in the regulation of chromatin structure. We have shown that nucleosomes tightly packaged into heterochromatin undergo considerable dynamic histone H2A-H2B maintenance via the direct interaction between HP1/Swi6 and facilitate chromatin transcription (FACT), which is composed of the Spt16/Pob3 heterodimer and Nhp6. In this study, we analyzed the role of Nhp6, an HMG box protein, in the FACT at heterochromatin. Pob3 mutant strains showed derepressed heterochromatin-dependent gene silencing, whereas Nhp6 mutant strains did not show significant defects in chromatin regulation or gene expression, suggesting that these two modules play different roles in chromatin regulation. We expressed a protein fusing Nhp6 to the C-terminus of Pob3, which mimics the multicellular FACT component Ssrp1. The chromatin-binding activity of FACT increased with the number of Nhp6 fused to Pob3, and the heterochromatin formation rate was promoted more strongly. Furthermore, we demonstrated that this promotion of heterochromatinization inhibited the heterochromatic variegation caused by epe1 +  disruption. Heterochromatic variegation can be observed in a variety of regulatory steps; however, when it is caused by fluctuations in chromatin arrangement, it can be eliminated through the strong recruitment of the FACT complex.","doi":"10.1111/gtc.13132","authors":"Takahata S, Taguchi A, Takenaka A, Mori M, Chikashige Y, Tsutsumi C, Hiraoka Y, Murakami Y","authors_abbrev":"Takahata S et al.","pubmed_publication_date":"05 Jun 2024","pubmed_entrez_date":"2024-06-05","publication_year":"2024","canto_session_key":"4e7189bd13bf7958","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-06-05 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC609.05","SPBP8B7.19","SPAC57A10.09c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:30397104","title":"Fidelity in RNA-based recognition of transposable elements.","citation":"Philos Trans R Soc Lond B Biol Sci 2018 Nov 05;373(1762)","abstract":"Genomes are under constant threat of invasion by transposable elements and other genomic parasites. How can host genomes recognize these elements and target them for degradation? This requires a system that is highly adaptable, and at the same time highly specific. Current data suggest that perturbation of transcription patterns by transposon insertions could be detected by the RNAi surveillance pathway. Multiple transposon insertions might generate sufficient amounts of primal small RNAs to initiate generation of secondary small RNAs and silencing. At the same time primal small RNAs need to be constantly degraded to reduce the level of noise small RNAs below the threshold required for initiation of silencing. Failure in RNA degradation results in loss of fidelity of small RNA pathways and silencing of ectopic targets.This article is part of the theme issue '5' and 3' modifications controlling RNA degradation'.","doi":"10.1098/rstb.2018.0168","authors":"Ugolini I, Halic M","authors_abbrev":"Ugolini I et al.","pubmed_publication_date":"05 Nov 2018","pubmed_entrez_date":"2018-11-07","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-08 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11739793","title":"The Schizosaccharomyces pombe spo3+ gene is required for assembly of the forespore membrane and genetically interacts with psy1(+)-encoding syntaxin-like protein.","citation":"Mol Biol Cell 2001 Dec;12(12):3955-72","abstract":"Formation of the forespore membrane, which becomes the plasma membrane of spores, is an intriguing step in the sporulation of the fission yeast Schizosaccharomyces pombe. Here we report two novel proteins that localize to the forespore membrane. spo3(+) encodes a potential membrane protein, which was expressed only during sporulation. Green fluorescent protein (GFP) fusion revealed that Spo3 localized to the forespore membrane. The spo3 disruptant was viable and executed meiotic nuclear divisions as efficiently as the wild type but did not form spores. One of the spo3 alleles, spo3-KC51, was dose-dependently suppressed by psy1(+), which encodes a protein similar to mammalian syntaxin-1A, a component of the plasma membrane docking/fusion complex. psy1(+) was essential for vegetative growth, and its transcription was enhanced during sporulation. As expected, Psy1 localized to the plasma membrane during vegetative growth. Interestingly, Psy1 on the plasma membrane disappeared immediately after first meiotic division and relocalized to the forespore membrane as the second division initiated. In the spo3 null mutant, the forespore membrane was initiated but failed to develop a normal morphology. Electron microscopy revealed that membrane vesicles were accumulated in the cytoplasm of immature spo3Delta asci. These results suggest that Spo3 is a key component of the forespore membrane and is essential for its assembly acting in collaboration with the syntaxin-like protein.","authors":"Nakamura T, Nakamura-Kubo M, Hirata A, Shimoda C","authors_abbrev":"Nakamura T et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-12-12","publication_year":"2001","canto_session_key":"56a166785d462f8d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-29 16:08:57","canto_approved_date":"2026-05-28 13:13:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-31 11:53:01","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC607.10","SPBC119.04","SPCC825.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-09-29"},{"uniquename":"PMID:25030924","title":"Using LacO arrays to monitor DNA double-strand break dynamics in live Schizosaccharomyces pombe cells.","citation":"Methods Mol Biol 2014;1176:127-41","abstract":"LacO arrays, when combined with LacI-GFP, have been a valuable tool for studying nuclear architecture and chromatin dynamics. Here, we outline an experimental approach to employ the LacO/LacI-GFP system in S. pombe to assess DNA double-strand break (DSB) dynamics and the contribution of chromatin state to DSB repair. Previously, integration of long, highly repetitive LacO arrays in S. pombe has been a challenge. To address this problem, we have developed a novel approach, based on the principles used for homologous recombination-based genome engineering in higher eukaryotes, to integrate long, repetitive LacO arrays with targeting efficiencies as high as 70 %. Combining this facile LacO/LacI-GFP system with a site-specific, inducible DSB provides a means to monitor DSB dynamics at engineered sites within the genome.","doi":"10.1007/978-1-4939-0992-6_11","authors":"Leland BA, King MC","authors_abbrev":"Leland BA et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-07-18","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-07-19 00:15:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27068713","title":"Timeless protection of telomeres.","citation":"Curr Genet 2016 Nov;62(4):725-730","abstract":"The DNA replication machinery encounters problems at numerous genomic regions that are inherently difficult to replicate. These genomic regions include telomeres, which contain repetitive DNA and telomere-binding proteins. If not properly regulated, replication of such genomic regions can result in DNA damage, leading to genomic instability. Studies implicated a role of Timeless-related proteins at difficult-to-replicate genomic regions, including telomeres. However, how these proteins maintain telomeres was elusive. In a recent report, we described the role of Swi1, a Timeless-related protein, in telomere maintenance in fission yeast. We demonstrated that Swi1 is required for proper replication of repeat DNA sequences at telomeres. We also showed that Swi1-deficient cells utilize recombination-based ALT (alternative lengthening of telomeres)-like mechanisms to maintain telomeres in the absence of telomerase. Here, we highlight these findings and present additional data to discuss the role of Swi1 Timeless  in telomere protection and ALT prevention.","authors":"Gadaleta MC, González-Medina A, Noguchi E","authors_abbrev":"Gadaleta MC et al.","pubmed_publication_date":"Nov 2016","pubmed_entrez_date":"2016-04-13","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-04-15 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19G7.13","SPBC216.06c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:40083061","title":"Heterochromatin Protein Swi6 Suppresses Aberrant Gene Conversion at mat Loci by Adjusting the Balance Between the Two Pathways of Swi2 and Rad57.","citation":"Genes Cells 2025 Mar;30(2):e70012","abstract":"Heterochromatin protein 1 (HP1) is a highly conserved, canonical factor involved in heterochromatin formation. HP1 has been shown to interact with proteins other than silencing factors and heterochromatin effectors. In fission yeast, the loss of the HP1 homolog Swi6 disrupts heterochromatin structure and affects mating type switching at the mat locus, where heterochromatin exists; however, cell growth is unaffected. In this study, we focused on the Swi6 dimerization domain, which provides a binding surface for various interactors. We isolated a distinctive swi6H321Q mutant that does not affect heterochromatin structure but causes variegation in growth defects and abnormal recombination at the mat locus. This mutation disrupts the interaction between Swi6 and Swi2, a mat locus-specific recombination protein. The AT-hook motif of Swi2, which is also required for chromatin localization at the mat locus, is necessary for growth inhibition, suggesting that mislocalization of Swi2 at the mat locus induces growth inhibition. Genetic analysis revealed that abnormal recombination at the mat region was independent of Swi2 but dependent on the Rad57-dependent homologous recombination pathway. These results suggest that Swi6 plays an important role in gene conversion at the mat locus by producing an appropriate selection of homologous recombination factors.","doi":"10.1111/gtc.70012","authors":"Fujioka T, Murakami Y, Takahata S","authors_abbrev":"Fujioka T et al.","pubmed_publication_date":"Mar 2025","pubmed_entrez_date":"2025-03-14","publication_year":"2025","canto_session_key":"41eab02aa83eb155","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-03-15 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20H4.07","SPBC354.05c","SPAC664.01c","SPAC1142.03c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:19919183","title":"CYP21-catalyzed production of the long-term urinary metandienone metabolite 17beta-hydroxymethyl-17 alpha-methyl-18-norandrosta-1,4,13-trien-3-one: a contribution to the fight against doping.","citation":"Biol Chem 2010 Jan;391(1):119-27","abstract":"Anabolic-androgenic steroids are some of the most frequently misused drugs in human sports. Recently, a previously unknown urinary metabolite of metandienone, 17beta-hydroxymethyl-17 alpha-methyl-18-norandrosta-1,4,13-trien-3-one (20OH-NorMD), was discovered via LC-MS/MS and GC-MS. This metabolite was reported to be detected in urine samples up to 19 days after administration of metandienone. However, so far it was not possible to obtain purified reference material of this metabolite and to confirm its structure via NMR. Eleven recombinant strains of the fission yeast Schizosaccharomyces pombe that express different human hepatic or steroidogenic cytochrome P450 enzymes were screened for production of this metabolite in a whole-cell biotransformation reaction. 17,17-Dimethyl-18-norandrosta-1,4,13-trien-3-one, chemically derived from metandienone, was used as substrate for the bioconversion, because it could be converted to the final product in a single hydroxylation step. The obtained results demonstrate that CYP21 and to a lesser extent also CYP3A4 expressing strains can catalyze this steroid hydroxylation. Subsequent 5 l-scale fermentation resulted in the production and purification of 10 mg of metabolite and its unequivocal structure determination via NMR. The synthesis of this urinary metandienone metabolite via S. pombe-based whole-cell biotransformation now allows its use as a reference substance in doping control assays.","doi":"10.1515/BC.2010.002","authors":"Zöllner A, Parr MK, Drăgan CA, Dräs S, Schlörer N, Peters FT, Maurer HH, Schänzer W, Bureik M","authors_abbrev":"Zöllner A et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-11-19","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24034318","title":"Measurement of in vivo RNA synthesis rates.","citation":"Methods Enzymol 2013;530:117-35","abstract":"A technique is described to directly measure ongoing transcription from individual genes in permeabilized cells of either the budding yeast Saccharomyces cerevisiae or the fission yeast Schizosaccharomyces pombe. Transcription run-on (TRO) analysis is used to compare the relative rates of synthesis for specific transcripts in cells grown under different environmental conditions or harvested at different stages of development. As the amount of an individual RNA species present at any given time is determined by its net rate of synthesis and degradation, an accurate picture of transcription per se can be obtained only by directly measuring de novo synthesis of RNA (if you are interested in RNA degradation, see Method for measuring mRNA decay rate in Saccharomyces cerevisiae). Most techniques employed to measure changes in the relative levels of individual transcripts present under different conditions, including Northern analysis (see Northern blotting), RT-PCR (see Reverse-transcription PCR (RT-PCR)), nuclease protection assays (see Explanatory Chapter: Nuclease Protection Assays), and genome-wide assays, such as microarray analysis and high throughput RNA sequencing, measure changes in the steady-state level of a transcript, which may or may not reflect the actual changes in transcription of the gene. Recent studies carried out in fission yeast have demonstrated that increases in the steady-state level (accumulation) of many individual mRNAs occur without any significant changes in transcription rates (McPheeters et al., 2009), highlighting the important role of regulated RNA stability in determining gene expression programs (Harigaya et al., 2006).","doi":"10.1016/B978-0-12-420037-1.00006-3","authors":"McPheeters DS, Wise JA","authors_abbrev":"McPheeters DS et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-09-17","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8804400","title":"The G protein beta subunit Gpb1 of Schizosaccharomyces pombe is a negative regulator of sexual development.","citation":"Mol Gen Genet 1996 Aug 27;252(1-2):20-32","abstract":"A Schizosaccharomyces pombe homolog of mammalian genes encoding G protein beta subunits, gpb1+, was cloned by the polymerase chain reaction using primer pairs that correspond to sequences conserved in several G beta genes of other species followed by screening of genomic and cDNA libraries. The gpb1 gene encodes 317 amino acids that show 47% homology with human G beta 1 and G beta 2 and 40% homology with Saccharomyces cerevisiae G beta protein. Disruption of the gpb1 gene indicated that this gene is not required for vegetative cell growth. However, gpb1-disrupted haploid cells mated and sporulated faster than wild-type cells, both in sporulation (MEA) and in complex medium (YE): when examined 23 h after transfer to sporulation medium, 35% of gpb1-disrupted haploid pairs had undergone conjugation and sporulation, whereas only 3-5% of wild-type haploid pairs had done so. Overexpression of the gpb1 gene suppressed this facilitated conjugation and sporulation phenotype of gpb1-disrupted cells but did not cause any obvious effect in wild-type cells. Co-disruption of one of the two S. pombe G alpha-subunit genes, gpa2, in the gpb1-disrupted cells did not change the accelerated conjugation and sporulation phenotype of the gpb1- cells. However, co-disruption of the ras1 gene abolished the gpb1- phenotype. These results suggest that Gpb1 is a negative regulator of conjugation and sporulation that apparently works upstream of Ras1 function in S. pombe. The possible relationship of Gpb1 to two previously identified, putative G alpha proteins of S. pombe is discussed.","authors":"Kim DU, Park SK, Chung KS, Choi MU, Yoo HS","authors_abbrev":"Kim DU et al.","pubmed_publication_date":"27 Aug 1996","pubmed_entrez_date":"1996-08-27","publication_year":"1996","canto_session_key":"d8d3bfcf3cf532c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-17 11:16:51","canto_approved_date":"2026-04-08 11:01:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-01 18:02:58","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC32H8.07","SPBC24C6.06","SPAC23H3.13c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-03-17"},{"uniquename":"PMID:26803803","title":"CryoEM structures of two spliceosomal complexes: starter and dessert at the spliceosome feast.","citation":"Curr Opin Struct Biol 2016 Feb;36:48-57","abstract":"The spliceosome is formed on pre-mRNA substrates from five small nuclear ribonucleoprotein particles (U1, U2, U4/U6 and U5 snRNPs), and numerous non-snRNP factors. Saccharomyces cerevisiae U4/U6.U5 tri-snRNP comprises U5 snRNA, U4/U6 snRNA duplex and approximately 30 proteins and represents a substantial part of the spliceosome before activation. Schizosaccharomyces pombe U2.U6.U5 spliceosomal complex is a post-catalytic intron lariat spliceosome containing U2 and U5 snRNPs, NTC (nineteen complex), NTC-related proteins (NTR), U6 snRNA, and an RNA intron lariat. Two recent papers describe near-complete atomic structures of these complexes based on cryoEM single-particle analysis. The U4/U6.U5 tri-snRNP structure provides crucial insight into the activation mechanism of the spliceosome. The U2.U6.U5 complex reveals the striking architecture of NTC and NTR and important features of the group II intron-like catalytic RNA core remaining after spliced mRNA is released. These two structures greatly advance our understanding of the mechanism of pre-mRNA splicing.","doi":"10.1016/j.sbi.2015.12.005","authors":"Nguyen TH, Galej WP, Fica SM, Lin PC, Newman AJ, Nagai K","authors_abbrev":"Nguyen TH et al.","pubmed_publication_date":"Feb 2016","pubmed_entrez_date":"2016-01-25","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-01-26 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15598736","title":"Atomic force microscopic analysis of the binding of the Schizosaccharomyces pombe origin recognition complex and the spOrc4 protein with origin DNA.","citation":"Proc Natl Acad Sci U S A 2004 Dec 28;101(52):17952-7","abstract":"In eukaryotes, the initiation of DNA replication requires the interaction between origin sequences and the origin recognition complex (ORC), which is highly conserved. In this report, atomic force microscopy (AFM) was used to examine the binding of Schizosaccharomyces pombe (sp) ORC and the spOrc4 protein with the sp autonomously replicating sequence 1 (ars1). AFM imaging revealed that spORC binding to ars1 occurred solely through spOrc4p and depended on the N-terminal AT-hook domains present in spOrc4p. At high molar ratios of spORC (or spOrc4p alone) to DNA (6:1), all of the input ars1 was bound in a one protein complex to one plasmid manner. Restriction digestion and AFM analysis of protein-DNA fragments revealed the presence of two binding sites in ars1. One site mapped to a region centered at nucleotide 838 of ars1 previously detected by DNase I protection that was reported to be essential for the autonomously replicating sequence activity of ars1. The second site mapped to a previously uncharacterized region centered at nucleotide 1148. AFM showed that the length of the DNA fragment complexed with either spORC or spOrc4p was shortened by approximately 140 bp, suggesting the wrapping of two turns of the DNA around the spOrc4p alone as well as the spOrc4p in spORC. We also show that treatment of the spORC (spOrc4p)-ars1 complex with topoisomerase I induced a negative shift in the topoisomer distribution. These findings suggest that the binding of spORC to origin DNA alters the structure of the DNA. Thus, in the case of spORC, due to its unusual spOrc4p, at least two factors are likely to influence ars1 activation. These include the selective binding of the complex to A- and T-rich regions and the alteration of the DNA structure due to its wrapping around spOrc4p.","authors":"Gaczynska M, Osmulski PA, Jiang Y, Lee JK, Bermudez V, Hurwitz J","authors_abbrev":"Gaczynska M et al.","pubmed_publication_date":"28 Dec 2004","pubmed_entrez_date":"2004-12-16","publication_year":"2004","canto_session_key":"9e69d4f99d9ce3e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-10-30 10:54:56","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-10-30 10:54:48","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-30"},{"uniquename":"PMID:9219337","title":"Identification and preliminary characterization of p31, a new PSTAIRE-related protein in fission yeast.","citation":"Yeast 1997 Jun 30;13(8):727-34","abstract":"One of the defining characteristics of the catalytic subunit of the cyclin-dependent protein kinases (cdks) is the so-called PSTAIRE motif. Western blots of fission yeast cytosolic extracts using a monoclonal antibody against the PSTAIRE peptide revealed two bands at 34 kDa (p34cdc2) and 31 kDa (p31). Polyclonal antibodies to the C-terminus of p34cdc2 or to the full-length protein recognized the 34 kDa band but not p31. Overexpression of the cdc2+ gene resulted in the increase of the 34 kDa band but not p31. Like p34cdc2, the level of p31 revealed no obvious cell cycle regulation but the protein was present in spores where p34cdc2 was barely detectable. p31 expression was unaffected by removal of either phosphate or ammonium from the growth medium, although the level of p34cdc2 was reduced in the absence of phosphate. p31 was not associated with cyclin B, nor was it adsorbed to p13suc1 Sepharose beads, two characteristics of p34cdc2. p31 did, however, interact with p15, the starfish homologue of p13suc1. p31 was present in cells in which cdc2+ was replaced by its budding yeast homologue CDC28. When fission yeast cytosolic extracts were subjected to gel filtration chromatography, p31 eluted in two peaks, one at approximately 100 kDa, the other at approximately 30 kDa. We conclude that p31 is a novel fission yeast PSTAIRE protein and therefore, potentially, a new cdk.","authors":"Tournier S, Gachet Y, Hyams JS","authors_abbrev":"Tournier S et al.","pubmed_publication_date":"30 Jun 1997","pubmed_entrez_date":"1997-06-30","publication_year":"1997","canto_session_key":"8bd998a8144eefc5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-04-29 21:30:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 19:04:43","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16C4.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-29"},{"uniquename":"PMID:2837648","title":"Identification of an essential Schizosaccharomyces pombe RNA homologous to the 7SL component of signal recognition particle.","citation":"Mol Cell Biol 1988 Apr;8(4):1580-90","abstract":"We have cloned the gene encoding a novel small cytoplasmic RNA from the fission yeast Schizosaccharomyces pombe. Four lines of evidence support the idea that this RNA is a homolog of the 7SL RNA component of mammalian signal recognition particle (SRP), which targets presecretory proteins to the endoplasmic reticulum membrane. First, it shares limited but significant primary sequence homology with previously identified 7SL RNAs and can be folded into a similar secondary structure. Second, it possesses the 5' triphosphate characteristic of unprocessed RNA polymerase III transcripts, and moreover, it is the only fission yeast RNA in this size range with such a terminus. Third, its behavior in cell fractionation experiments suggests that it is part of a small ribonucleoprotein which forms salt-labile contacts with larger structures. Fourth, the particle containing S. pombe 7SL RNA resembles mammalian SRP in both size (11S) and affinity for DEAE-Sepharose. Disruption of the single-copy gene, designated slr1+, reveals that the RNA is indispensable for growth in fission yeast. This result is not surprising, since secretion is an essential cellular process.","authors":"Brennwald P, Liao X, Holm K, Porter G, Wise JA","authors_abbrev":"Brennwald P et al.","pubmed_publication_date":"Apr 1988","pubmed_entrez_date":"1988-04-01","publication_year":"1988","canto_session_key":"d877da09e6003baa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 16:02:37","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-13 10:00:57","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.98"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-13"},{"uniquename":"PMID:8451187","title":"The silent P mating type locus in fission yeast contains two autonomously replicating sequences.","citation":"Nucleic Acids Res 1993 Feb 25;21(4):855-61","abstract":"We show that in fission yeast two DNA fragments at the silent P mating type locus provide plasmids with the capability of autonomous replication. Bacterial vectors containing these sequences replicate in a polymeric form in fission yeast very much like plasmids with the commonly used replication sequence ars1, do. There are, however, several differences between the two new ars sequences. The percentage of cells containing the plasmid during selection, the plasmid copy number and the plasmid segregation during mitosis are all dependent on the choice of the ars sequence. A DNA fragment with ars activity from the left side of the silent P cassette represses the expression of the marker gene, ura4+, at least three hundred fold compared to plasmids containing only the other new ars sequence or only ars1. The importance of replication in this promoter independent transcriptional regulation is further substantiated by the fact that the repression is partially released in the presence of ars1 on the same plasmid.","authors":"Olsson T, Ekwall K, Ruusala T","authors_abbrev":"Olsson T et al.","pubmed_publication_date":"25 Feb 1993","pubmed_entrez_date":"1993-02-25","publication_year":"1993","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12521309","title":"Post-transcriptional regulation of ura4+ gene expression by glucose in Schizosaccharomyces pombe.","citation":"Mol Cells 2002 Dec 31;14(3):437-43","abstract":"Glucose-inducible gene expression is a fundamental cellular response for optimal cell growth, but identities of glucose-inducible genes and its regulatory mechanism remain largely elusive in Schizosaccharomyces pombe. Here we report that ura4+, encoding orotidine monophosphate decarboxylase (OMPdecase), shows glucose-inducible expression regulated at post-transcriptional level. The ura4+ mRNA level was rapidly decreased by approximately 50% within 20 min after glucose depletion and it was readily recovered upon glucose-readdition within 1 h. Glucose at above 2% similarly raised the transcript level of ura4+, while low concentration (0.1%) was not effective. Interestingly, control of mRNA turnover would be the main regulatory step of the glucose-dependent expression of ura4+. Moreover, stress-activated MAPK (SAPK) pathway was partially responsible for the glucose-regulated expression of ura4+ and rrg1+, another example of glucose-dependent mRNA stability control in S. pombe. These results suggest that the SAPK pathway might participate in the glucose-dependent regulation of ura4+ and rrg1+ mRNA stabilities.","authors":"Kim MJ, Kim M, Park SD","authors_abbrev":"Kim MJ et al.","pubmed_publication_date":"31 Dec 2002","pubmed_entrez_date":"2003-01-11","publication_year":"2002","canto_session_key":"0f25fa31b6307c43","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-02-29 14:18:36","canto_approved_date":"2020-02-29 14:18:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-29 14:18:30","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC330.05c","SPCC338.11c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2020-02-29"},{"uniquename":"PMID:3026914","title":"The mosaic cox1 gene in the mitochondrial genome of Schizosaccharomyces pombe: minimal structural requirements and evolution of group I introns.","citation":"Gene 1986;45(3):289-97","abstract":"The gene encoding subunit 1 of cytochrome oxidase (cox1) in the fission yeast Schizosaccharomyces pombe is polymorphic. In strain 50 it contains two group I introns with open reading frames (ORFs) in phase with the upstream exons (Lang, 1984). In strain EF1 two additional very short group I introns which do not possess ORFs were detected by DNA sequencing. These two introns (AI2a and AI3) share distinct characteristics concerning their nucleotide sequence and secondary structure and are located at identical positions as the introns AI4 and AI5 beta, respectively, in the cox1 gene of Saccharomyces cerevisiae. The sequence homology of the cob and cox1 genes around the splice points of introns AI2a, AI4, and BI4 (cob intron 4) might reflect horizontal gene transfer between the distantly related species S. pombe and S. cerevisiae.","authors":"Trinkl H, Wolf K","authors_abbrev":"Trinkl H et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25167576","title":"Proceedings of the The 7th International Fission Yeast Meeting: Pombe 2013, June 24-29, 2013, London, England.","citation":"Biochem Soc Trans 2013 Dec;41(6):1629-771","abstract":"","authors":"","authors_abbrev":"","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2014-08-30","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-08-31 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36978953","title":"Expression of the H 2 O 2  Biosensor roGFP-Tpx1.C160S in Fission and Budding Yeasts and Jurkat Cells to Compare Intracellular H 2 O 2  Levels, Transmembrane Gradients, and Response to Metals.","citation":"Antioxidants (Basel) 2023 Mar 13;12(3)","abstract":"Intracellular hydrogen peroxide (H 2 O 2 ) levels can oscillate from low, physiological concentrations, to intermediate, signaling ones, and can participate in toxic reactions when overcoming certain thresholds. Fluorescent protein-based reporters to measure intracellular H 2 O 2  have been developed in recent decades. In particular, the redox-sensitive green fluorescent protein (roGFP)-based proteins fused to peroxiredoxins are among the most sensitive H 2 O 2  biosensors. Using fission yeast as a model system, we recently demonstrated that the gradient of extracellular-to-intracellular peroxides through the plasma membrane is around 300:1, and that the concentration of physiological H 2 O 2  is in the low nanomolar range. Here, we have expressed the very sensitive probe roGFP2-Tpx1.C169S in two other model systems, budding yeast and human Jurkat cells. As in fission yeast, the biosensor is ~40-50% oxidized in these cell types, suggesting similar peroxide steady-state levels. Furthermore, probe oxidation upon the addition of extracellular peroxides is also quantitatively similar, suggesting comparable plasma membrane H 2 O 2  gradients. Finally, as a proof of concept, we have applied different concentrations of zinc to all three model systems and have detected probe oxidation, demonstrating that an excess of this metal can cause fluctuations of peroxides, which are moderate in yeasts and severe in mammalian cells. We conclude that the principles governing H 2 O 2  fluxes are very similar in different model organisms.","doi":"10.3390/antiox12030706","authors":"de Cubas L, Mallor J, Herrera-Fernández V, Ayté J, Vicente R, Hidalgo E","authors_abbrev":"de Cubas L et al.","pubmed_publication_date":"13 Mar 2023","pubmed_entrez_date":"2023-03-29","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-03-30 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23615450","title":"Separate roles of IQGAP Rng2p in forming and constricting the Schizosaccharomyces pombe cytokinetic contractile ring.","citation":"Mol Biol Cell 2013 Jun;24(12):1904-17","abstract":"Eukaryotic cells require IQGAP family multidomain adapter proteins for cytokinesis, but many questions remain about how IQGAPs contribute to the process. Here we show that fission yeast IQGAP Rng2p is required for both the normal process of contractile ring formation from precursor nodes and an alternative mechanism by which rings form from strands of actin filaments. Our work adds to previous studies suggesting a role for Rng2p in node and ring formation. We demonstrate that Rng2p is also required for normal ring constriction and septum formation. Systematic analysis of domain-deletion mutants established how the four domains of Rng2p contribute to cytokinesis. Contrary to a previous report, the actin-binding calponin homology domain of Rng2p is not required for viability, ring formation, or ring constriction. The IQ motifs are not required for ring formation but are important for ring constriction and septum formation. The GTPase-activating protein (GAP)-related domain is required for node-based ring formation. The Rng2p C-terminal domain is the only domain essential for viability. Our studies identified several distinct functions of Rng2 at multiple stages of cytokinesis.","doi":"10.1091/mbc.E12-10-0775","authors":"Tebbs IR, Pollard TD","authors_abbrev":"Tebbs IR et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-04-26","publication_year":"2013","canto_session_key":"aac2a8d125c42565","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-05 09:01:30","canto_approved_date":"2024-07-04 14:35:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-17 17:22:31","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.13c","SPAC20G8.05c","SPBC19G7.05c","SPCC645.05c","SPAC24B11.11c","SPCC4B3.15","SPBC428.13c","SPAP8A3.08","SPBC1A4.05"],"gene_count":9,"ltp_gene_count":3,"approved_date":"2019-11-05"},{"uniquename":"PMID:22132152","title":"P(5A)-type ATPase Cta4p is essential for Ca2+ transport in the endoplasmic reticulum of Schizosaccharomyces pombe.","citation":"PLoS One 2011;6(11):e27843","abstract":"This study establishes the role of P(5A)-type Cta4 ATPase in Ca(2+) sequestration in the endoplasmic reticulum by detecting an ATP-dependent, vanadate-sensitive and FCCP insensitive (45)Ca(2+)-transport in fission yeast membranes isolated by cellular fractionation. Specifically, the Ca(2+)-ATPase transport activity was decreased in ER membranes isolated from cells lacking a cta4(+) gene. Furthermore, a disruption of cta4(+) resulted in 6-fold increase of intracellular Ca(2+) levels, sensitivity towards accumulation of misfolded proteins in ER and ER stress, stimulation of the calcineurin phosphatase activity and vacuolar Ca(2+) pumping. These data provide compelling biochemical evidence for a P(5A)-type Cta4 ATPase as an essential component of Ca(2+) transport system and signaling network which regulate, in conjunction with calcineurin, the ER functionality in fission yeast.","doi":"10.1371/journal.pone.0027843","authors":"Lustoza AC, Palma LM, Façanha AR, Okorokov LA, Okorokova-Façanha AL","authors_abbrev":"Lustoza AC et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-12-02","publication_year":"2011","canto_session_key":"04bb144c0a472009","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-13 12:57:54","canto_approved_date":"2023-08-28 15:34:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-25 18:00:26","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.15c","SPBP4H10.04","SPACUNK4.07c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2018-11-13"},{"uniquename":"PMID:19269364","title":"Establishing the program of origin firing during S phase in fission Yeast.","citation":"Cell 2009 Mar 06;136(5):852-64","abstract":"Initiation of eukaryotic DNA synthesis occurs at origins of replication that are utilized with characteristic times and frequencies during S phase. We have investigated origin usage by evaluating the kinetics of replication factor binding in fission yeast and show that similar to metazoa, ORC binding is periodic during the cell cycle, increasing during mitosis and peaking at M/G1. At an origin, the timing of ORC binding in M and pre-RC assembly in G1 correlates with the timing of firing during S, and the level of pre-IC formation reflects origin efficiency. Extending mitosis allows ORC to become more equally associated with origins and leads to genome-wide changes in origin usage, while overproduction of pre-IC factors increases replication of both efficient and inefficient origins. We propose that differential recruitment of ORC to origins during mitosis followed by competition among origins for limiting replication factors establishes the timing and efficiency of origin firing.","doi":"10.1016/j.cell.2009.01.017","authors":"Wu PY, Nurse P","authors_abbrev":"Wu PY et al.","pubmed_publication_date":"06 Mar 2009","pubmed_entrez_date":"2009-03-10","publication_year":"2009","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14532136","title":"Rec8 cleavage by separase is required for meiotic nuclear divisions in fission yeast.","citation":"EMBO J 2003 Oct 15;22(20):5643-53","abstract":"Sister chromatid cohesion in meiosis is established by cohesin complexes, including the Rec8 subunit. During meiosis I, sister chromatid cohesion is destroyed along the chromosome arms to release connections of recombined homologous chromosomes (homologues), whereas centromeric cohesion persists until it is finally destroyed at anaphase II. In fission yeast, as in mammals, distinct cohesin complexes are used depending on the chromosomal region; Rec8 forms a complex with Rec11 (equivalent to SA3) mainly along chromosome arms, while Psc3 (equivalent to SA1 and SA2) forms a complex mainly in the vicinity of the centromeres. Here we show that separase activation and resultant Rec8 cleavage are required for meiotic chromosome segregation in fission yeast. A non-cleavable form of Rec8 blocks disjunction of homologues at meiosis I. However, displacing non-cleavable Rec8 restrictively from the chromosome arm by genetically depleting Rec11 alleviated the blockage of homologue segregation, but not of sister segregation. We propose that the segregation of homologues at meiosis I and of sisters at meiosis II requires the cleavage of Rec8 along chromosome arms and at the centromeres, respectively.","authors":"Kitajima TS, Miyazaki Y, Yamamoto M, Watanabe Y","authors_abbrev":"Kitajima TS et al.","pubmed_publication_date":"15 Oct 2003","pubmed_entrez_date":"2003-10-09","publication_year":"2003","canto_session_key":"7519fc48320b66a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-05-31 05:12:42","canto_approved_date":"2023-09-12 13:42:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-30 12:14:10","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.04","SPBC14C8.01c","SPCC4E9.01c","SPAC17A5.11","SPBC29A10.14"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-05-31"},{"uniquename":"PMID:17639451","title":"Another way to move chromosomes.","citation":"Chromosoma 2007 Dec;116(6):497-505","abstract":"A typical way of moving chromosomes is exemplified by mitotic segregation, in which the centromere is directly captured by spindle microtubules. In this study, we highlight another way of moving chromosomes remotely from outside the nucleus, which involves SUN and KASH domain nuclear envelope proteins. SUN and KASH domain protein families are known to connect the nucleus to cytoskeletal networks and play a role in migration and positioning of the nucleus. Recent studies in the fission yeast Schizossacharomyces pombe demonstrated an additional role for the SUN-KASH protein complex in chromosome movements. During meiotic prophase, telomeres are moved to rearrange chromosomes within the nucleus. The SUN-KASH protein complex located in the nuclear envelope is involved in this process. Telomeres are connected to the SUN protein on the nucleoplasmic side, and the dynein motor complex binds to the KASH protein on the cytoplasmic side. Telomeres are then moved along the nuclear envelope using cytoplasmic microtubules. These findings illustrate a general mechanism for transmitting a cytoskeletal driving force to chromosomes across the nuclear envelope.","authors":"Chikashige Y, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-07-20","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6308018","title":"Nucleoside diphosphokinase and cell cycle control in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1983 Mar;60:355-65","abstract":"Centrifugal elutriation was used to prepare synchronous cultures of Schizosaccharomyces pombe. Nucleoside diphosphokinase activity was measured throughout the cell cycle. In the wild-type strain (972) nucleoside diphosphokinase activity doubled in a stepwise fashion. The midpoint of the rise in enzyme activity was at 0.65 of a cycle, 0.29 of a cycle before the next S phase. Synchronous cultures of the mutant wee 1-6 were also prepared. In this strain S phase is delayed, occurring about 0.3 cycle later than in the wild-type. In wee 1-6 the midpoint of the stepwise doubling in nucleoside diphosphokinase activity occurred at 0.084; showing that the rise in enzyme activity is also delayed. Addition of cycloheximide to an exponentially growing culture caused an immediate inhibition of protein synthesis, yet nucleoside diphosphokinase activity continued to increase exponentially for a further 300 min. This indicates that the stepwise doubling of nucleoside diphosphokinase activity during the cell cycle is not achieved by a simple control on protein synthesis. Two temperature-sensitive cdc- mutants were also used: cdc2-33, a mutant whose single genetic lesion results in the twin defects of a loss of mitotic control and a loss of commitment to the cell cycle; and cdc 10-129, which has a defect in DNA replication. In both mutants a temperature shift-up of an asynchronously growing culture from the permissive (25 degrees C) to the restrictive temperature (36.5 degrees C) results in a rapid inhibition of DNA replication. In both mutants nucleoside diphosphokinase continues to increase exponentially. Therefore, although nucleoside diphosphokinase is required for DNA replication, apparently DNA replication is not required for an increase in nucleoside diphosphokinase activity.","authors":"Dickinson JR","authors_abbrev":"Dickinson JR","pubmed_publication_date":"Mar 1983","pubmed_entrez_date":"1983-03-01","publication_year":"1983","canto_session_key":"736108da153162b5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-04 18:36:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-04 18:36:04","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC70.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-03-04"},{"uniquename":"PMID:15040954","title":"A distinct type of alcohol dehydrogenase, adh4+, complements ethanol fermentation in an adh1-deficient strain of Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2004 Mar;4(6):649-54","abstract":"In the fission yeast Schizosaccharomyces pombe, only one alcohol dehydrogenase gene, adh1(+), has been identified. To elucidate the influence of adh1(+) on ethanol fermentation, we constructed the adh1 null strain (delta adh1). The delta adh1 cells still produced ethanol and grew fermentatively as the wild-type cells. Both DNA microarray and RT-PCR analysis demonstrated that this ethanol production is caused by the enhanced expression of a Saccharomyces cerevisiae ADH4-like gene product (SPAC5H10.06C named adh4(+)). Since the strain lacking both adh1 and adh4 genes (delta adh1 delta adh4) showed non-fermentative retarded growth, only these two ADHs produce ethanol for fermentative growth. This is the first observation that a S. cerevisiae ADH4-like alcohol dehydrogenase functions in yeast ethanol fermentation.","authors":"Sakurai M, Tohda H, Kumagai H, Giga-Hama Y","authors_abbrev":"Sakurai M et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-03-26","publication_year":"2004","canto_session_key":"dde3c6ac603a05eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-09 18:00:17","canto_approved_date":"2025-01-23 20:51:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-29 08:20:58","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5H10.06c","SPCC13B11.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-02-09"},{"uniquename":"PMID:31276588","title":"Inositol pyrophosphates impact phosphate homeostasis via modulation of RNA 3' processing and transcription termination.","citation":"Nucleic Acids Res 2019 Sep 19;47(16):8452-8469","abstract":"Fission yeast phosphate acquisition genes pho1, pho84, and tgp1 are repressed in phosphate-rich medium by transcription of upstream lncRNAs. Here, we show that phosphate homeostasis is subject to metabolite control by inositol pyrophosphates (IPPs), exerted through the 3'-processing/termination machinery and the Pol2 CTD code. Increasing IP8 (via Asp1 IPP pyrophosphatase mutation) de-represses the PHO regulon and leads to precocious termination of prt lncRNA synthesis. pho1 de-repression by IP8 depends on cleavage-polyadenylation factor (CPF) subunits, termination factor Rhn1, and the Thr4 letter of the CTD code. pho1 de-repression by mutation of the Ser7 CTD letter depends on IP8. Simultaneous inactivation of the Asp1 and Aps1 IPP pyrophosphatases is lethal, but this lethality is suppressed by mutations of CPF subunits Ppn1, Swd22, Ssu72, and Ctf1 and CTD mutation T4A. Failure to synthesize IP8 (via Asp1 IPP kinase mutation) results in pho1 hyper-repression. Synthetic lethality of asp1Δ with Ppn1, Swd22, and Ssu72 mutations argues that IP8 plays an important role in essential 3'-processing/termination events, albeit in a manner genetically redundant to CPF. Transcriptional profiling delineates an IPP-responsive regulon composed of genes overexpressed when IP8 levels are increased. Our results establish a novel role for IPPs in cell physiology.","doi":"10.1093/nar/gkz567","authors":"Sanchez AM, Garg A, Shuman S, Schwer B","authors_abbrev":"Sanchez AM et al.","pubmed_publication_date":"19 Sep 2019","pubmed_entrez_date":"2019-07-06","publication_year":"2019","canto_session_key":"5f8aff66a56b4439","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Angad Garg","canto_first_approved_date":"2022-11-07 06:34:29","canto_approved_date":"2024-10-08 08:56:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-10-21 16:50:57","canto_added_date":"2019-07-07 00:15:04","annotation_curators":[{"name":"Angad Garg","community_curator":true,"annotation_count":166,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPBC317.01","SPAC27D7.09c","SPAPB15E9.01c","SPBC337.03","SPBC25B2.08","SPBC1604.03c","SPAC27D7.03c","SPBC409.08","SPBPB7E8.01","SPBC19C7.05","SPAC824.04","SPBC354.12","SPAC1F8.06","SPBP8B7.26","SPAC5D6.08c","SPCC794.09c","SPBC776.02c","SPAC1002.12c","SPBC8E4.12c","SPAC1039.02","SPAC1786.02","SPBP4G3.02","SPAPB24D3.07c","SPBC3B9.11c","SPBC8E4.01c","SPBPB2B2.06c","SPAPB18E9.05c","SPBC1683.01","SPBC3H7.05c","SPNCRNA.1712","SPAC343.12","SPAC23A1.10","SPBC36.03c","SPAC1002.19","SPAC1039.01","SPAC750.01","SPAC1002.17c","SPBC947.04","SPAC3G9.04","SPBC1271.09","SPCC1672.06c","SPCC74.02c","SPAC13G7.13c","SPBC1815.01","SPBC32F12.11","SPBC11B10.08","SPBC16A3.08c","SPCC364.06","SPCC1442.01","SPAC17C9.16c","SPAC13G6.14"],"gene_count":52,"ltp_gene_count":10,"approved_date":"2022-11-07"},{"uniquename":"PMID:17052979","title":"Properties of the type B histone acetyltransferase Hat1: H4 tail interaction, site preference, and involvement in DNA repair.","citation":"J Biol Chem 2007 Jan 12;282(2):836-42","abstract":"The Hat1 histone acetyltransferase catalyzes the acetylation of H4 at lysines 5 and 12, the same sites that are acetylated in newly synthesized histone H4. By performing histone acetyltransferase (HAT) assays on various synthetic H4 N-terminal peptides, we have examined the interactions between Hat1 and the H4 tail domain. It was found that acetylation requires the presence of positively charged amino acids at positions 8 and 16 of H4, positions that are normally occupied by lysine; however, lysine per se is not essential and can be replaced by arginine. In contrast, replacing Lys-8 and -16 of H4 with glutamines reduces acetylation to background levels. Similarly, phosphorylation of Ser-1 of the H4 tail depresses acetylation by both yeast Hat1p and the human HAT-B complex. These results strongly support the model proposed by Ramakrishnan and colleagues for the interaction between Hat1 and the H4 tail (Dutnall, R. N., Tafrov, S. T., Sternglanz, R., and Ramakrishnan, V. (1998) Cell 94, 427-438) and may have implications for the genetic analysis of histone acetylation. It was also found that Lys-12 of H4 is preferentially acetylated by human HAT-B, in further agreement with the proposed model of H4 tail binding. Finally, we have demonstrated that deletion of the hat1 gene from the fission yeast Schizosaccharomyces pombe causes increased sensitivity to the DNA-damaging agent methyl methanesulfonate in the absence of any additional mutations. This is in contrast to results obtained with a Saccharomyces cerevisiae hat1Delta strain, which must also carry mutations of the acetylatable lysines of H3 for heightened methyl methanesulfonate sensitivity to be observed. Thus, although the role of Hat1 in DNA damage repair is evolutionarily conserved, the ability of H3 acetylation to compensate for Hat1 deletion appears to be more variable.","authors":"Benson LJ, Phillips JA, Gu Y, Parthun MR, Hoffman CS, Annunziato AT","authors_abbrev":"Benson LJ et al.","pubmed_publication_date":"12 Jan 2007","pubmed_entrez_date":"2006-10-21","publication_year":"2007","canto_session_key":"8fa379c24392afae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-05-05 15:59:03","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-05 15:58:57","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC139.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-05-05"},{"uniquename":"PMID:11733770","title":"Network dynamics and cell physiology.","citation":"Nat Rev Mol Cell Biol 2001 Dec;2(12):908-16","abstract":"Complex assemblies of interacting proteins carry out most of the interesting jobs in a cell, such as metabolism, DNA synthesis, movement and information processing. These physiological properties play out as a subtle molecular dance, choreographed by underlying regulatory networks. To understand this dance, a new breed of theoretical molecular biologists reproduces these networks in computers and in the mathematical language of dynamical systems.","authors":"Tyson JJ, Chen K, Novak B","authors_abbrev":"Tyson JJ et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-12-06","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26436826","title":"Polymerase δ replicates both strands after homologous recombination-dependent fork restart.","citation":"Nat Struct Mol Biol 2015 Nov;22(11):932-8","abstract":"To maintain genetic stability, DNA must be replicated only once per cell cycle, and replication must be completed even when individual replication forks are inactivated. Because fork inactivation is common, passive convergence of an adjacent fork is insufficient to rescue all inactive forks. Thus, eukaryotic cells have evolved homologous recombination-dependent mechanisms to restart persistent inactive forks. Completing DNA synthesis via homologous recombination-restarted replication (HoRReR) ensures cell survival, but at a cost. One such cost is increased mutagenesis because HoRReR is more error prone than canonical replication. This increased error rate implies the HoRReR mechanism is distinct from that of a canonical fork. Here we demonstrate, in Schizosaccharomyces pombe, that a DNA sequence duplicated by HoRReR during S phase is replicated semiconservatively, but both the leading and lagging strands are synthesized by DNA polymerase δ.","doi":"10.1038/nsmb.3100","authors":"Miyabe I, Mizuno K, Keszthelyi A, Daigaku Y, Skouteri M, Mohebi S, Kunkel TA, Murray JM, Carr AM","authors_abbrev":"Miyabe I et al.","pubmed_publication_date":"Nov 2015","pubmed_entrez_date":"2015-10-06","publication_year":"2015","canto_session_key":"593e1f8fb43caaa9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tony Carr","canto_first_approved_date":"2017-04-12 16:08:18","canto_approved_date":"2019-10-01 13:25:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-04-07 15:07:51","canto_added_date":"2015-10-07 00:18:41","annotation_curators":[{"name":"Tony Carr","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.04","SPAC3H5.06c","SPBC25H2.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-04-12"},{"uniquename":"PMID:15654021","title":"Mcp6, a meiosis-specific coiled-coil protein of Schizosaccharomyces pombe, localizes to the spindle pole body and is required for horsetail movement and recombination.","citation":"J Cell Sci 2005 Jan 15;118(Pt 2):447-59","abstract":"We report here that a meiosis-specific gene of Schizosaccharomyces pombe denoted mcp6+ (meiotic coiled-coil protein) encodes a protein that is required for the horsetail movement of chromosomes at meiosis I. The mcp6+ gene is specifically transcribed during the horsetail phase. Green fluorescent protein (GFP)-tagged Mcp6 appears at the start of karyogamy, localizes to the spindle-pole body (SPB) and then disappears before chromosome segregation at meiosis I. In the mcp6Delta strain, the horsetail movement was either hampered (zygotic meiosis) or abolished (azygotic meiosis) and the pairing of homologous chromosomes was impaired. Accordingly, the allelic recombination rates of the mcp6Delta strain were only 10-40% of the wild-type rates. By contrast, the ectopic recombination rate of the mcp6Delta strain was twice the wild-type rate. This is probably caused by abnormal homologous pairing in mcp6Delta cells because of aberrant horsetail movement. Fluorescent microscopy indicates that SPB components such as Sad1, Kms1 and Spo15 localize normally in mcp6Delta cells. Because Taz1 and Swi6 also localized with Sad1 in mcp6Delta cells, Mcp6 is not required for telomere clustering. In a taz1Delta strain, which does not display telomere clustering, and the dhc1-d3 mutant, which lacks horsetail movement, Mcp6 localized with Sad1 normally. However, we observed abnormal astral microtubule organization in mcp6Delta cells. From these results, we conclude that Mcp6 is necessary for neither SPB organization nor telomere clustering, but is required for proper astral microtubule positioning to maintain horsetail movement.","authors":"Saito TT, Tougan T, Okuzaki D, Kasama T, Nojima H","authors_abbrev":"Saito TT et al.","pubmed_publication_date":"15 Jan 2005","pubmed_entrez_date":"2005-01-18","publication_year":"2005","canto_session_key":"f64617d6d7cb9323","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-02-13 16:05:14","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-28 15:01:47","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPAC3A11.05c","SPAC664.01c","SPAC1F3.06c","SPBC582.06c","SPBC12D12.01","SPAC16A10.07c"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2014-11-28"},{"uniquename":"EMBL:AU009763","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30051891","title":"Automethylation-induced conformational switch in Clr4 (Suv39h) maintains epigenetic stability.","citation":"Nature 2018 Aug;560(7719):504-508","abstract":"Histone H3 lysine 9 methylation (H3K9me) mediates heterochromatic gene silencing and is important for genome stability and the regulation of gene expression 1-4 . The establishment and epigenetic maintenance of heterochromatin involve the recruitment of H3K9 methyltransferases to specific sites on DNA, followed by the recognition of pre-existing H3K9me by the methyltransferase and methylation of proximal histone H3 5-11 . This positive feedback loop must be tightly regulated to prevent deleterious epigenetic gene silencing. Extrinsic anti-silencing mechanisms involving histone demethylation or boundary elements help to limit the spread of inappropriate H3K9me 12-15 . However, how H3K9 methyltransferase activity is locally restricted or prevented from initiating random H3K9me-which would lead to aberrant gene silencing and epigenetic instability-is not fully understood. Here we reveal an autoinhibited conformation in the conserved H3K9 methyltransferase Clr4 (also known as Suv39h) of the fission yeast Schizosaccharomyces pombe that has a critical role in preventing aberrant heterochromatin formation. Biochemical and X-ray crystallographic data show that an internal loop in Clr4 inhibits the catalytic activity of this enzyme by blocking the histone H3K9 substrate-binding pocket, and that automethylation of specific lysines in this loop promotes a conformational switch that enhances the H3K9me activity of Clr4. Mutations that are predicted to disrupt this regulation lead to aberrant H3K9me, loss of heterochromatin domains and inhibition of growth, demonstrating the importance of the intrinsic inhibition and auto-activation of Clr4 in regulating the deposition of H3K9me and in preventing epigenetic instability. Conservation of the Clr4 autoregulatory loop in other H3K9 methyltransferases and the automethylation of a corresponding lysine in the human SUV39H2 homologue 16  suggest that the mechanism described here is broadly conserved.","doi":"10.1038/s41586-018-0398-2","authors":"Iglesias N, Currie MA, Jih G, Paulo JA, Siuti N, Kalocsay M, Gygi SP, Moazed D","authors_abbrev":"Iglesias N et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-07-28","publication_year":"2018","canto_session_key":"2709030dec2bc3c1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-07-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c","SPCC622.16c","SPCC736.11"],"gene_count":3,"ltp_gene_count":3,"pdb_entries":[{"pdb_id":"6bp4","gene_chains":[{"gene_uniquename":"SPBC428.08c","chain":"A/B","position":"192-490"}],"title":"Structure of the S. pombe Clr4 catalytic domain bound to SAM","entry_authors":"Currie MA,Moazed D","entry_authors_abbrev":"Currie MA et al.","reference_uniquename":"PMID:30051891","experimental_method":"X-ray","resolution":"2.7701"},{"pdb_id":"6box","gene_chains":[{"gene_uniquename":"SPBC428.08c","chain":"A/B","position":"192-490"}],"title":"Structure of the S. pombe Clr4 catalytic domain bound to SAH","entry_authors":"Currie MA,Moazed D","entry_authors_abbrev":"Currie MA et al.","reference_uniquename":"PMID:30051891","experimental_method":"X-ray","resolution":"2.412"}]},{"uniquename":"EMBL:AU008004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9335328","title":"Condensins, cohesins, and chromosome architecture: how to make and break a mitotic chromosome.","citation":"Cell 1997 Oct 03;91(1):5-8","abstract":"","authors":"Heck MM","authors_abbrev":"Heck MM","pubmed_publication_date":"03 Oct 1997","pubmed_entrez_date":"1997-10-23","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010793","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR43601","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12D12.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33663806","title":"Nuclear Periphery and Telomere Maintenance: TERRA Joins the Stage.","citation":"Trends Genet 2021 Jul;37(7):608-611","abstract":"Long noncoding (lnc)RNAs derived from telomeres, the ends of linear eukaryotic chromosomes, help to maintain telomere length and stability by multiple means, including regulation of telomerase activity and recombination-based telomere maintenance. New findings in yeast promote a model in which telomere attachment to the nuclear envelope regulates telomere transcription and maintenance.","doi":"10.1016/j.tig.2021.02.003","authors":"Juríková K, De Wulf P, Cusanelli E","authors_abbrev":"Juríková K et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-03-05","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-03-07 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15935756","title":"Gross chromosomal rearrangements and elevated recombination at an inducible site-specific replication fork barrier.","citation":"Cell 2005 Jun 03;121(5):689-702","abstract":"Genomic rearrangements linked to aberrant recombination are associated with cancer and human genetic diseases. Such recombination has indirectly been linked to replication fork stalling. Using fission yeast, we have developed a genetic system to block replication forks at nonhistone/DNA complexes located at a specific euchromatic site. We demonstrate that stalled replication forks lead to elevated intrachromosomal and ectopic recombination promoting site-specific gross chromosomal rearrangements. We show that recombination is required to promote cell viability when forks are stalled, that recombination proteins associate with sites of fork stalling, and that recombination participates in deleterious site-specific chromosomal rearrangements. Thus, recombination is a \"double-edged sword,\" preventing cell death when the replisome disassembles at the expense of genetic stability.","authors":"Lambert S, Watson A, Sheedy DM, Martin B, Carr AM","authors_abbrev":"Lambert S et al.","pubmed_publication_date":"03 Jun 2005","pubmed_entrez_date":"2005-06-07","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15146064","title":"Disruption of astral microtubule contact with the cell cortex activates a Bub1, Bub3, and Mad3-dependent checkpoint in fission yeast.","citation":"Mol Biol Cell 2004 Jul;15(7):3345-56","abstract":"In animal and yeast cells, the mitotic spindle is aligned perpendicularly to the axis of cell division. This ensures that sister chromatids are separated to opposite sides of the cytokinetic actomyosin ring. In fission yeast, spindle rotation is dependent upon the interaction of astral microtubules with the cortical actin cytoskeleton. In this article, we show that addition of Latrunculin A, which prevents spindle rotation, delays the separation of sister chromatids and anaphase promoting complex-mediated destruction of spindle-associated Securin and Cyclin B. Moreover, we find that whereas sister kinetochore pairs normally congress to the spindle midzone before anaphase onset, this congression is disrupted when astral microtubule contact with the actin cytoskeleton is disturbed. By analyzing the timing of kinetochore separation, we find that this anaphase delay requires the Bub3, Mad3, and Bub1 but not the Mad1 or Mad2 spindle assembly checkpoint proteins. In agreement with this, we find that Bub1 remains associated with kinetochores when spindles are mispositioned. These data indicate that, in fission yeast, astral microtubule contact with the medial cell cortex is monitored by a subset of spindle assembly checkpoint proteins. We propose that this checkpoint ensures spindles are properly oriented before anaphase takes place.","authors":"Tournier S, Gachet Y, Buck V, Hyams JS, Millar JB","authors_abbrev":"Tournier S et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-18","publication_year":"2004","canto_session_key":"451f87e20600a5b7","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1322.12c","SPBC19G7.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:40668621","title":"Physical constraints and biological regulations underlie universal osmoresponses.","citation":"Elife 2025 Jul 16;13","abstract":"Microorganisms constantly transition between environments with dramatically different external osmolarities. However, theories of microbial osmoresponse integrating physical constraints and biological regulations are lacking. Here, we propose such a theory, utilizing the separation of timescales for passive responses and active regulations. We demonstrate that regulations of osmolyte production and cell-wall synthesis assist cells in coping with intracellular crowding effects and adapting to a broad range of external osmolarity. Furthermore, we predict a threshold value above which cells cannot grow, ubiquitous across bacteria and yeast. Intriguingly, the theory predicts a dramatic speedup of cell growth after an abrupt decrease in external osmolarity due to cell-wall synthesis regulation. Our theory rationalizes the unusually fast growth observed in fission yeast after an oscillatory osmotic perturbation, and the predicted growth rate peaks match quantitatively with experimental measurements. Our study reveals the physical basis of osmoresponse, yielding far-reaching implications for microbial physiology.","doi":"10.7554/eLife.102858","authors":"Ye Y, Wang Q, Lin J","authors_abbrev":"Ye Y et al.","pubmed_publication_date":"16 Jul 2025","pubmed_entrez_date":"2025-07-16","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-07-16 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27250946","title":"Analyzing Schizosaccharomyces pombe DNA Content by Flow Cytometry.","citation":"Cold Spring Harb Protoc 2016 Jun 01;2016(6)","abstract":"Flow cytometry can be used to measure the DNA content of individual cells. The data are usually presented as DNA histograms that can be used to examine the cells' progression through the cell cycle. Under standard growth conditions, fission yeast cells do not complete cytokinesis until after G1 phase; therefore, DNA histograms show one major peak representing cells in G1 (2×1C DNA) and G2 phase (1×2C DNA). By analysis of the duration of the fluorescence signal as well as the intensity of the DNA-related signal, it is possible to discriminate between cells in M/G1, S, and G2 This protocol describes how to prepare cells for flow cytometry and analyze them. We also describe the application of barcoding for more accurate comparison of samples.","doi":"10.1101/pdb.prot091280","authors":"Boye E, Anda S, Rothe C, Stokke T, Grallert B","authors_abbrev":"Boye E et al.","pubmed_publication_date":"01 Jun 2016","pubmed_entrez_date":"2016-06-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-06-04 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24256273","title":"Regulation of entry into gametogenesis by Ste11: the endless game.","citation":"Biochem Soc Trans 2013 Dec;41(6):1673-8","abstract":"Sexual reproduction is a fundamental aspect of eukaryotic cells, and a conserved feature of gametogenesis is its dependency on a master regulator. The ste11 gene was isolated more than 20 years ago by the Yamamoto laboratory as a suppressor of the uncontrolled meiosis driven by a pat1 mutant. Numerous studies from this laboratory and others have established the role of the Ste11 transcription factor as the master regulator of the switch between proliferation and differentiation in fission yeast. The transcriptional and post-transcriptional controls of ste11 expression are intricate, but most are not redundant. Whereas the transcriptional controls ensure that the gene is transcribed at a high level only when nutrients are rare, the post-transcriptional controls restrict the ability of Ste11 to function as a transcription factor to the G1-phase of the cell cycle from where the differentiation programme is initiated. Several feedback loops ensure that the cell fate decision is irreversible. The complete panel of molecular mechanisms operating to warrant the timely expression of the ste11 gene and its encoded protein basically mirrors the advances in the understanding of the numerous ways by which gene expression can be modulated.","doi":"10.1042/BST20130225","authors":"Anandhakumar J, Fauquenoy S, Materne P, Migeot V, Hermand D","authors_abbrev":"Anandhakumar J et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25319828","title":"Crystal structure of a Fanconi anemia-associated nuclease homolog bound to 5' flap DNA: basis of interstrand cross-link repair by FAN1.","citation":"Genes Dev 2014 Oct 15;28(20):2276-90","abstract":"Fanconi anemia (FA) is an autosomal recessive genetic disorder caused by defects in any of 15 FA genes responsible for processing DNA interstrand cross-links (ICLs). The ultimate outcome of the FA pathway is resolution of cross-links, which requires structure-selective nucleases. FA-associated nuclease 1 (FAN1) is believed to be recruited to lesions by a monoubiquitinated FANCI-FANCD2 (ID) complex and participates in ICL repair. Here, we determined the crystal structure of Pseudomonas aeruginosa FAN1 (PaFAN1) lacking the UBZ (ubiquitin-binding zinc) domain in complex with 5' flap DNA. All four domains of the right-hand-shaped PaFAN1 are involved in DNA recognition, with each domain playing a specific role in bending DNA at the nick. The six-helix bundle that binds the junction connects to the catalytic viral replication and repair (VRR) nuclease (VRR nuc) domain, enabling FAN1 to incise the scissile phosphate a few bases distant from the junction. The six-helix bundle also inhibits the cleavage of intact Holliday junctions. PaFAN1 shares several conserved features with other flap structure-selective nucleases despite structural differences. A clamping motion of the domains around the wedge helix, which acts as a pivot, facilitates nucleolytic cleavage. The PaFAN1 structure provides insights into how archaeal Holliday junction resolvases evolved to incise 5' flap substrates and how FAN1 integrates with the FA complex to participate in ICL repair.","doi":"10.1101/gad.248492.114","authors":"Gwon GH, Kim Y, Liu Y, Watson AT, Jo A, Etheridge TJ, Yuan F, Zhang Y, Kim Y, Carr AM, Cho Y","authors_abbrev":"Gwon GH et al.","pubmed_publication_date":"15 Oct 2014","pubmed_entrez_date":"2014-10-17","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22A12.01c","SPBC146.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:10559953","title":"Meiosis: Rec8 is the reason for cohesion.","citation":"Nat Cell Biol 1999 Sep;1(5):E125-7","abstract":"","authors":"Stoop-Myer C, Amon A","authors_abbrev":"Stoop-Myer C et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-11-13","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41986306","title":"Structural insights into the gating mechanism of the fission yeast phosphate exporter SpXpr1.","citation":"Cell Discov 2026 Apr 15;12(1)","abstract":"Phosphate homeostasis is essential for fundamental cellular processes, including energy metabolism, signal transduction, and nucleic acid synthesis. Although XPR1 family proteins are conserved phosphate exporters throughout eukaryotes, their structural mechanisms in organisms other than mammals and plants remain largely unexplored. Here, we presented high-resolution cryo-electron microscopy (cryo-EM) structures of Schizosaccharomyces pombe Xpr1 (SpXpr1) in both the apo and inositol hexakisphosphate (InsP6)-bound states. While SpXpr1 shares conserved phosphate coordination sites with its human and plant orthologs, SpXpr1 employs a unique dual gating mechanism: (1) an intracellular gate formed by the N-loop of the SPX domain, stabilized by a preceding N-helix and an extended TM10 helix and (2) an extracellular ECL plug  occluding the exit. We further showed that InsP6 binding induces allosteric destabilization of the N-loop gate, facilitating phosphate release. Functional validation through phosphate efflux assays in Homo sapiens XPR1 (HsXPR1)-knockout cells and whole-cell patch-clamp recordings confirmed the structural observations. Our findings elucidated a unique gating mechanism of SpXpr1 and offer evolutionary perspectives on phosphate regulation across eukaryotes.","doi":"10.1038/s41421-026-00883-8","authors":"Yang H, Wang Y, Yue C, Li X, Wang Y, Yu Y, Shen H","authors_abbrev":"Yang H et al.","pubmed_publication_date":"15 Apr 2026","pubmed_entrez_date":"2026-04-15","publication_year":"2026","canto_session_key":"fb52d0dd2e887d8e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-16 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33400299","title":"Role of mitochondrial complex III/IV in the activation of transcription factor Rst2 in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2021 Jun;115(6):1323-1338","abstract":"Mitochondria play essential roles in eukaryotic cells for glucose metabolism to produce ATP. In Schizosaccharomyces pombe, transcription factor Rst2 can be activated upon glucose deprivation. However, the link between Rst2 and mitochondrial function remains elusive. Here, we monitored Rst2 transcriptional activity in living cells using a Renilla luciferase reporter system, and found that inhibition of mitochondrial complex III/IV caused cells to produce reactive oxygen species (ROS) and nitric oxide (NO), which in turn activated Rst2. Furthermore, Rst2-GFP was observed to translocate from cytoplasm to nucleus upon mitochondrial complex III/IV inhibitors treatment, and deletion of genes associated with complex III/IV resulted in delayed process of Rst2-GFP nuclear exportation under glucose-rich condition. In particular, we found that Rst2 was phosphorylated following the treatment of complex III/IV inhibitors or SNAP. Altogether, our findings suggest that mitochondrial complex III/IV participates in the activation of Rst2 through ROS and NO generation in Schizosaccharomyces pombe.","doi":"10.1111/mmi.14678","authors":"Jiang G, Liu Q, Kato T, Miao H, Gao X, Liu K, Chen S, Sakamoto N, Kuno T, Fang Y","authors_abbrev":"Jiang G et al.","pubmed_publication_date":"Jun 2021","pubmed_entrez_date":"2021-01-05","publication_year":"2021","canto_session_key":"d6a88cd70209aaf6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yue Fang","canto_first_approved_date":"2021-01-29 09:14:51","canto_approved_date":"2022-11-16 16:47:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-21 16:16:55","canto_added_date":"2021-01-07 01:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yue Fang","community_curator":true,"annotation_count":36,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.04c","SPCC1682.01","SPAC1B2.04","SPBC26H8.12","SPBC1198.01","SPBC16H5.06","SPAC6F12.02","SPAC1556.02c","SPAC20G8.04c","SPBC106.10","SPAC1296.02","SPCC613.10","SPAC8C9.03","SPBC16C6.08c","SPAC24C9.16c","SPBC16A3.16","SPBC119.06","SPAC869.02c"],"gene_count":18,"ltp_gene_count":18,"approved_date":"2021-01-29"},{"uniquename":"PMID:23830945","title":"Studies on the kinetics of killing and the proposed mechanism of action of microemulsions against fungi.","citation":"Int J Pharm 2013 Sep 15;454(1):226-32","abstract":"Microemulsions are physically stable oil/water clear dispersions, spontaneously formed and thermodynamically stable. They are composed in most cases of water, oil, surfactant and cosurfactant. Microemulsions are stable, self-preserving antimicrobial agents in their own right. The observed levels of antimicrobial activity associated with microemulsions may be due to the direct effect of the microemulsions themselves on the bacterial cytoplasmic membrane. The aim of this work is to study the growth behaviour of different microbes in presence of certain prepared physically stable microemulsion formulae over extended periods of time. An experiment was designed to study the kinetics of killing of a microemulsion preparation (17.3% Tween-80, 8.5% n-pentanol, 5% isopropyl myristate and 69.2% sterile distilled water) against selected test microorganisms (Candida albicans, Aspergillus niger, Schizosaccharomyces pombe and Rhodotorula spp.). Secondly, an experiment was designed to study the effects of the microemulsion preparation on the cytoplasmic membrane structure and function of selected fungal species by observation of 260 nm component leakage. Finally, the effects of the microemulsion on the fungal membrane structure and function using S. pombe were studied using transmission electron microscopy. The results showed that the prepared microemulsions are stable, effective antimicrobial systems with effective killing rates against C. albicans, A. niger, S. pombe and Rhodotorula spp. The results indicate a proposed mechanism of action of significant anti-membrane activity, resulting in the gross disturbance and dysfunction of the cytoplasmic membrane structure which is followed by cell wall modifications, cytoplasmic coagulation, disruption of intracellular metabolism and cell death.","doi":"10.1016/j.ijpharm.2013.06.049","authors":"Al-Adham IS, Ashour H, Al-Kaissi E, Khalil E, Kierans M, Collier PJ","authors_abbrev":"Al-Adham IS et al.","pubmed_publication_date":"15 Sep 2013","pubmed_entrez_date":"2013-07-09","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17137508","title":"Genomewide identification of pheromone-targeted transcription in fission yeast.","citation":"BMC Genomics 2006 Nov 30;7:303","abstract":"Fission yeast cells undergo sexual differentiation in response to nitrogen starvation. In this process haploid M and P cells first mate to form diploid zygotes, which then enter meiosis and sporulate. Prior to mating, M and P cells communicate with diffusible mating pheromones that activate a signal transduction pathway in the opposite cell type. The pheromone signalling orchestrates mating and is also required for entry into meiosis.\nHere we use DNA microarrays to identify genes that are induced by M-factor in P cells and by P-factor in M-cells. The use of a cyr1 genetic background allowed us to study pheromone signalling independently of nitrogen starvation. We identified a total of 163 genes that were consistently induced more than two-fold by pheromone stimulation. Gene disruption experiments demonstrated the involvement of newly discovered pheromone-induced genes in the differentiation process. We have mapped Gene Ontology (GO) categories specifically associated with pheromone induction. A direct comparison of the M- and P-factor induced expression pattern allowed us to identify cell-type specific transcripts, including three new M-specific genes and one new P-specific gene.\nWe found that the pheromone response was very similar in M and P cells. Surprisingly, pheromone control extended to genes fulfilling their function well beyond the point of entry into meiosis, including numerous genes required for meiotic recombination. Our results suggest that the Ste11 transcription factor is responsible for the majority of pheromone-induced transcription. Finally, most cell-type specific genes now appear to be identified in fission yeast.","authors":"Xue-Franzén Y, Kjaerulff S, Holmberg C, Wright A, Nielsen O","authors_abbrev":"Xue-Franzén Y et al.","pubmed_publication_date":"30 Nov 2006","pubmed_entrez_date":"2006-12-02","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006811","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9757124","title":"Crystallographic characterization of Pap1-DNA complex.","citation":"Acta Crystallogr D Biol Crystallogr 1998 Sep 01;54(Pt 5):1014-6","abstract":"Pap1 is a fission yeast transcription factor that activates genes related with resistance against staurosporine, a potent inhibitor of protein kinase C, and has been shown to be involved in cell growth, cell cycle, carcinogenesis and differentiation. Pap1 has the bZIP DNA-binding domain but binds to non-consensus DNA sequences for the bZIP motif. Highly ordered crystals of the DNA-binding domain complexed with a DNA fragment that has an ATF/CREB-like non-consensus sequence have been obtained. The crystals grew by the vapor-diffusion technique with polyethylene glycol 6000 and belong to space group R3 with a = b = 240.78, c = 43.85 A. A 2.0 A resolution data set was collected with a cryo-crystallographic technique.","authors":"Fujii Y, Ohira T, Kyougoku Y, Toda T, Yanagida M, Hakoshima T","authors_abbrev":"Fujii Y et al.","pubmed_publication_date":"01 Sep 1998","pubmed_entrez_date":"1998-10-03","publication_year":"1998","canto_session_key":"8b10585c0b18a3e7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-28 13:49:19","canto_approved_date":"2022-11-07 11:39:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-20 12:13:33","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-28"},{"uniquename":"PMID:35090053","title":"Decline of ergothioneine in frailty and cognition impairment.","citation":"FEBS Lett 2022 May;596(10):1270-1278","abstract":"Ergothioneine is a well-known antioxidant that is abundant in both human red blood cells and in fission yeast responding to nutritional stress. In frail elderly people, whose ageing organs undergo functional decline, there is a correlation between ergothioneine levels and cognitive, but not skeletal muscle decline. In patients suffering from dementia, including Alzheimer's disease with hippocampal atrophy, deteriorating cognitive ability is correlated with declining ergothioneine levels. S-methyl-ergothioneine, trimethyl-histidine and three other trimethyl-ammonium compounds also decrease sharply in dementia, whereas compounds such as indoxyl-sulfate and quinolinic acid increase, possibly exacerbating the disease. Using these opposing dementia markers, not only diagnosis, but also therapeutic interventions to mitigate cognitive decline may now become possible.","doi":"10.1002/1873-3468.14299","authors":"Kondoh H, Teruya T, Kameda M, Yanagida M","authors_abbrev":"Kondoh H et al.","pubmed_publication_date":"May 2022","pubmed_entrez_date":"2022-01-28","publication_year":"2022","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2022-01-30 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1547778","title":"Species specific protein--DNA interactions may determine the chromatin units of genes in S.cerevisiae and in S.pombe.","citation":"EMBO J 1992 Mar;11(3):1177-85","abstract":"Yeast genes, such as URA3, are chromatin units characterized by positioned nucleosomes and flanking nuclease sensitive regions (NSRs). To investigate the structural determinants at the chromatin level in vivo, the URA3 gene was dissected into three parts (U5', Umid and U3'), and the chromatin structures of the individual parts were analysed after insertion into minichromosomes and after chromatin assembly in vivo in Saccharomyces cerevisiae. While nucleosome positions were altered on Umid, the 5'-end and the 3'-end of URA3 maintained their native structures (a positioned nucleosome and a NSR each) independent of the site or orientation of insertion. This suggests that the chromatin unit of the native URA3 gene is dominated by strong protein boundaries at the 5'- and 3'-ends. In an alternative approach, we investigated whether nucleosome positions or NSRs were maintained when the whole URA3 gene was placed on a shuttle vector and assembled into chromatin by Schizosaccharomyces pombe providing different proteins, but the same nucleosomal spacing. In a complementary exchange experiment, the ade6 gene of S.pombe was shuttled to S.cerevisiae. In spite of a general conservation of histone proteins and nucleosome core structures, neither nucleosome positions nor NSRs were maintained in the heterologous background. The results demonstrate that chromatin structures are species specific and that the structural boundaries of yeast genes may be dominated by strong species specific protein-DNA interactions.","authors":"Bernardi F, Zatchej M, Thoma F","authors_abbrev":"Bernardi F et al.","pubmed_publication_date":"Mar 1992","pubmed_entrez_date":"1992-03-01","publication_year":"1992","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23563150","title":"Characterization of genome-reduced fission yeast strains.","citation":"Nucleic Acids Res 2013 May 01;41(10):5382-99","abstract":"The Schizosaccharomyces pombe genome is one of the smallest among the free-living eukaryotes. We further reduced the S. pombe gene number by large-scale gene deletion to identify a minimal gene set required for growth under laboratory conditions. The genome-reduced strain has four deletion regions: 168.4 kb in the left arm of chromosome I, 155.4 kb in the right arm of chromosome I, 211.7 kb in the left arm of chromosome II and 121.6 kb in the right arm of chromosome II. The deletions corresponded to a loss of 223 genes of the original ~5100. The quadruple-deletion strain, with a total deletion size of 657.3 kb, showed a decreased ability to uptake glucose and some amino acids in comparison with the parental strain. The strain also showed increased gene expression of the mating pheromone M-factor precursor and the nicotinamide adenine dinucleotide phosphate -specific glutamate dehydrogenase. There was also a 2.7-fold increase in the concentration of cellular adenosine triphosphate, and levels of the heterologous proteins, enhanced green fluorescent protein and secreted human growth hormone were increased by 1.7- and 1.8-fold, respectively. The transcriptome data from this study have been submitted to the Gene Expression Omnibus (GEO: http://www.ncbi.nlm.nih.gov/geo/) under the accession number GSE38620 (http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?token=vjkxjewuywgcovc&acc=GSE38620).","doi":"10.1093/nar/gkt233","authors":"Sasaki M, Kumagai H, Takegawa K, Tohda H","authors_abbrev":"Sasaki M et al.","pubmed_publication_date":"01 May 2013","pubmed_entrez_date":"2013-04-09","publication_year":"2013","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20668161","title":"Proteasome nuclear import mediated by Arc3 can influence efficient DNA damage repair and mitosis in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2010 Sep 15;21(18):3125-36","abstract":"Proteasomes must remove regulatory molecules and abnormal proteins throughout the cell, but how proteasomes can do so efficiently remains unclear. We have isolated a subunit of the Arp2/3 complex, Arc3, which binds proteasomes. When overexpressed, Arc3 rescues phenotypes associated with proteasome deficiencies; when its expression is repressed, proteasome deficiencies intensify. Arp2/3 is best known for regulating membrane dynamics and vesicular transport; thus, we performed photobleaching experiments and showed that proteasomes are readily imported into the nucleus but exit the nucleus slowly. Proteasome nuclear import is reduced when Arc3 is inactivated, leading to hypersensitivity to DNA damage and inefficient cyclin-B degradation, two events occurring in the nucleus. These data suggest that proteasomes display Arc3-dependent mobility in the cell, and mobile proteasomes can efficiently access substrates throughout the cell, allowing them to effectively regulate cell-compartment-specific activities.","doi":"10.1091/mbc.E10-06-0506","authors":"Cabrera R, Sha Z, Vadakkan TJ, Otero J, Kriegenburg F, Hartmann-Petersen R, Dickinson ME, Chang EC","authors_abbrev":"Cabrera R et al.","pubmed_publication_date":"15 Sep 2010","pubmed_entrez_date":"2010-07-30","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4.07c","SPBC646.09c","SPAC1420.03","SPBC582.07c","SPBP19A11.03c","SPAC11H11.06","SPBC1778.08c","SPCC1322.12c","SPAC630.03"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:14993467","title":"The involvement of Srs2 in post-replication repair and homologous recombination in fission yeast.","citation":"Nucleic Acids Res 2004;32(4):1480-91","abstract":"Homologous recombination is important for the repair of double-strand breaks and daughter strand gaps, and also helps restart stalled and collapsed replication forks. However, sometimes recombination is inappropriate and can have deleterious consequences. To temper recombination, cells have employed DNA helicases that unwind joint DNA molecules and/or dissociate recombinases from DNA. Budding yeast Srs2 is one such helicase. It can act by dissociating Rad51 nucleoprotein filaments, and is required for channelling DNA lesions to the post-replication repair (PRR) pathway. Here we have investigated the role of Srs2 in controlling recombination in fission yeast. Similar to budding yeast, deletion of fission yeast srs2 results in hypersensitivity to a range of DNA damaging agents, rhp51-dependent hyper-recombination and synthetic sickness when combined with rqh1- that is suppressed by deleting rhp51, rhp55 or rhp57. Epistasis analysis indicates that Srs2 and the structure-specific endonuclease Mus81-Eme1 function in a sub-pathway of PRR for the tolerance/repair of UV-induced damage. However, unlike in Saccharomyces cerevisiae, Srs2 is not required for channelling lesions to the PRR pathway in Schizosaccharomyces pombe. In addition to acting as an antirecombinase, we also show that Srs2 can aid the recombinational repair of camptothecin-induced collapsed replication forks, independently of PRR.","authors":"Doe CL, Whitby MC","authors_abbrev":"Doe CL et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-03-03","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4H3.05","SPAC18B11.07c","SPAC13G6.01c","SPCC4G3.05c","SPAC644.14c","SPAC20H4.07","SPBC1734.06","SPAC2G11.12","SPAC15A10.03c","SPAC3C7.03c"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:9415380","title":"Type II myosin involved in cytokinesis in the fission yeast, Schizosaccharomyces pombe.","citation":"Cell Motil Cytoskeleton 1997;38(4):385-96","abstract":"We have cloned an unique gene encoding the heavy chain of a type II myosin in the fission yeast, Schizosaccharomyces pombe. The myo2+ gene encodes a protein of 1526 amino acids with a predicted molecular weight of 177 kDa and containing consensus binding motifs for both essential and regulatory light chains. The S. pombe myo2+ head domain is 45% identical to myosin IIs from Saccharomyces cerevisiae and Homo sapiens and 40% identical to Drosophila melanogaster Structurally, myo2+ most closely resembles budding yeast MYO1, the tails of both myosin IIs containing a number of proline residues that are predicted to substantially disrupt the ability of these myosins to form coiled coils. The myo2+ gene is located on chromosome III, 8.3 map units from ade6+. Deletion of approximately 70% of the coding sequence of myo2+ is lethal but myo2delta spores can acquire a suppressor mutation that allows them to form viable microcolonies consisting of filaments of branched cells with aberrant septa. Overexpression of myo2+ results in the inhibition of cytokinesis; cells become elongated and multinucleate and fail to assemble a functional cytokinetic actin ring and are either aseptate or form aberrant septa. These results suggest that a contractile actin-myosin based cytokinetic mechanism appeared early in the evolution of eukaryotic cells and further emphasise the utility of fission yeast as a model organism in which to study the molecular and cellular basis of cytokinesis.","authors":"May KM, Watts FZ, Jones N, Hyams JS","authors_abbrev":"May KM et al.","pubmed_publication_date":"1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_session_key":"21d961ac9764aa8a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-11-23 12:20:52","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-11-20 11:30:11","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-20"},{"uniquename":"PMID:17512405","title":"RNAi-dependent and -independent RNA turnover mechanisms contribute to heterochromatic gene silencing.","citation":"Cell 2007 May 18;129(4):707-21","abstract":"In fission yeast, the RNAi pathway is required for heterochromatin-dependent silencing of transgene insertions at centromeric repeats and acts together with other pathways to silence transgenes at the silent mating-type locus. Here, we show that transgene transcripts at centromeric repeats are processed into siRNAs and are therefore direct targets of RNAi. Furthermore, we show that Cid14, a member of the Trf4/5 family of poly(A) polymerases, has poly(A) polymerase activity that is required for heterochromatic gene silencing. Surprisingly, while siRNA levels in cid14Delta cells are dramatically reduced, the structural integrity of heterochromatin appears to be preserved. Cid14 resides in a complex similar to the TRAMP complex found in budding yeast, which is part of a nuclear surveillance mechanism that degrades aberrant transcripts. Our findings indicate that polyadenylation by a TRAMP-like complex contributes to robust silencing of heterochromatic genes in fission yeast via the recruitment of the exosome and/or the RNAi machinery.","authors":"Bühler M, Haas W, Gygi SP, Moazed D","authors_abbrev":"Bühler M et al.","pubmed_publication_date":"18 May 2007","pubmed_entrez_date":"2007-05-22","publication_year":"2007","canto_session_key":"6ba7e958410b1f95","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-20 09:12:20","canto_approved_date":"2025-11-12 11:11:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-18 12:21:12","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":45,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPAC19D5.03","SPBC1685.06","SPAC17H9.01","SPAC664.01c","SPAC12G12.13c","SPAC212.11","SPBC26H8.10","SPBC28F2.12","SPBP35G2.08c","SPAC6F12.16c","SPCC736.11","SPAC821.04c","SPAC18G6.02c","SPCC188.13c","SPAC1F3.01"],"gene_count":16,"ltp_gene_count":13,"approved_date":"2024-01-20"},{"uniquename":"PMID:1297333","title":"Regulation of p105wee1 and p34cdc2 during meiosis in Schizosaccharomyces pombe.","citation":"Biochem Cell Biol 1992;70(10-11):1088-96","abstract":"Temperature-sensitive pat1 mutants of the fission yeast Schizosaccharomyces pombe can be induced to undergo meiosis at the restrictive temperature, irrespective of the mat1 configuration and the nutritional conditions. Using a combination of exit from stationary phase and thermal inactivation of the 52-kilodalton protein kinase that is encoded by the pat1 (also called ran1) gene, highly synchronous meiotic cultures were obtained. Synthesis and tyrosyl phosphorylation of p34cdc2 was evident during meiotic G1 and S phases. During this period there was increased expression of p105wee1, a protein kinase implicated in the tyrosyl phosphorylation of p34cdc2. Following a relatively brief G2 period, during which a reduction in the steady-state level of p105wee1 occurred, there was an approximately 19-fold increase in the histone H1 phosphotransferase activity of p34cdc2. Only a single peak of histone H1 kinase activation was observed, which implies that unlike meiosis in amphibians and echinoderms, p34cdc2 is functional only during one of the meiotic divisions in S. pombe, presumably meiosis II. Stimulation of the kinase activity of p34cdc2 was associated with its tyrosyl dephosphorylation. This is analogous to mitotic M phase and suggests parallels in the mechanism of activation of p34cdc2 during mitosis and one of the meiotic divisions in S. pombe.","authors":"Daya-Makin M, Szankasi P, Tang L, MacRae D, Pelech SL","authors_abbrev":"Daya-Makin M et al.","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26143918","title":"Intercalating dyes for enhanced contrast in second-harmonic generation imaging of protein crystals.","citation":"Acta Crystallogr D Biol Crystallogr 2015 Jul;71(Pt 7):1471-7","abstract":"The second-harmonic generation (SHG) activity of protein crystals was found to be enhanced by up to ∼1000-fold by the intercalation of SHG phores within the crystal lattice. Unlike the intercalation of fluorophores, the SHG phores produced no significant background SHG from solvated dye or from dye intercalated into amorphous aggregates. The polarization-dependent SHG is consistent with the chromophores adopting the symmetry of the crystal lattice. In addition, the degree of enhancement for different symmetries of dyes is consistent with theoretical predictions based on the molecular nonlinear optical response. Kinetics studies indicate that intercalation arises over a timeframe of several minutes in lysozyme, with detectable enhancements within seconds. These results provide a potential means to increase the overall diversity of protein crystals and crystal sizes amenable to characterization by SHG microscopy.","doi":"10.1107/S1399004715008287","authors":"Newman JA, Scarborough NM, Pogranichniy NR, Shrestha RK, Closser RG, Das C, Simpson GJ","authors_abbrev":"Newman JA et al.","pubmed_publication_date":"Jul 2015","pubmed_entrez_date":"2015-07-07","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-04-21 00:15:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22268381","title":"The karyopherin Sal3 is required for nuclear import of the core RNA interference pathway protein Rdp1.","citation":"Traffic 2012 Apr;13(4):520-31","abstract":"RNA-dependent RNA polymerase activity is required for RNA interference (RNAi) in many lower eukaryotes including the fission yeast Schizosacchromyces pombe. Together with Ago1 and Dcr1, the RNA-dependent RNA polymerase Rdp1 is critical for RNA-dependent transcriptional- and post-transcriptional gene silencing. Although the bulk of Rdp1 is localized to the nucleus, Ago1 and Dcr1 are primarily cytoplasmic. This may reflect the fact that Rdp1 is required early in the RNAi pathway to generate double strand RNA from transcripts that originate from centromeric loci. The relatively large size of Rdp1 (139.4 kD) precludes passive diffusion of the enzyme into the nucleus suggesting that karyopherin-dependent transport is involved in nuclear targeting of this enzyme. In this study, we report that the karyopherin/importin β3 homolog Sal3 is required for nuclear import of Rdp1 in S. pombe. Loss of nuclear Rdp1 was associated with substantially reduced transcriptional gene silencing, and surprisingly, post-transcriptional gene silencing which occurs in the cytoplasm of other eukaryotes, was also significantly affected. Together, these results identify Sal3 as a modulator of RNAi-dependent transcriptional gene silencing as well as a potential link between nuclear import and post-transcriptional gene silencing.","doi":"10.1111/j.1600-0854.2012.01333.x","authors":"Park J, Freitag SI, Young PG, Hobman TC","authors_abbrev":"Park J et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-01-25","publication_year":"2012","canto_session_key":"b5ff1c5ed18d1f76","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-30 12:17:31","canto_approved_date":"2025-09-04 10:14:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-30 12:17:24","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.09","SPCC188.13c","SPCC1840.03","SPCC736.11","SPAC22G7.02","SPCC1322.06","SPBC14F5.03c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2019-10-30"},{"uniquename":"PMID:16286472","title":"Rad3-Cds1 mediates coupling of initiation of meiotic recombination with DNA replication. Mei4-dependent transcription as a potential target of meiotic checkpoint.","citation":"J Biol Chem 2006 Jan 20;281(3):1338-44","abstract":"Premeiotic S-phase and meiotic recombination are known to be strictly coupled in Saccharomyces cerevisiae. However, the checkpoint pathway regulating this coupling has been largely unknown. In fission yeast, Rad3 is known to play an essential role in coordination of DNA replication and cell division during both mitotic growth and meiosis. Here we have examined whether the Rad3 pathway also regulates the coupling of DNA synthesis and recombination. Inhibition of premeiotic S-phase with hydroxyurea completely abrogates the progression of meiosis, including the formation of DNA double-strand breaks (DSBs). DSB formation is restored in rad3 mutant even in the presence of hydroxyurea, although repair of DSBs does not take place or is significantly delayed, indicating that the subsequent recombination steps may be still inhibited. Examination of the roles of downstream checkpoint kinases reveals that Cds1, but not Chk1 or Mek1, is required for suppression of DSB in the presence of hydroxyurea. Transcriptional induction of some rec+ genes essential for DSB occurs at a normal timing and to a normal level in the absence of DNA synthesis in both the wild-type and cds1delta cells. On the other hand, the transcriptional induction of the mei4+ transcription factor and cdc25+ phosphatase, which is significantly suppressed by hydroxyurea in the wild-type cells, occurs almost to a normal level in cds1delta cells even in the presence of hydroxyurea. These results show that the Rad3-Cds1 checkpoint pathway coordinates initiation of meiotic recombination and meiotic cell divisions with premeiotic DNA synthesis. Because mei4+ is known to be required for DSB formation and cdc25+ is required for activation of meiotic cell divisions, we propose an intriguing possibility that the Rad3-Cds1 meiotic checkpoint pathway may target transcription of these factors.","authors":"Ogino K, Masai H","authors_abbrev":"Ogino K et al.","pubmed_publication_date":"20 Jan 2006","pubmed_entrez_date":"2005-11-16","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9651494","title":"Mosaic structure of the cox2 gene in the petite negative yeast Schizosaccharomyces pombe: a group II intron is inserted at the same location as the otherwise unrelated group II introns in the mitochondria of higher plants.","citation":"Gene 1998 Jul 03;214(1-2):101-12","abstract":"In contrast to homologous genes in other fungal mitochondrial genomes, the gene encoding subunit 2 of cytochrome oxidase (cox2) in several Schizosaccharomyces pombe strains contains a large group II intron. Its 2436 nucleotides can be folded into a typical group II intron secondary structure, possessing all the expected sequence motifs for subgroup IIA1 (Michel et al., 1989). This intron is remarkable for the following reasons: (i) Five nucleotide changes were observed compared with the continuous form of the cox2 gene in the reference strain 50 at the 3'-exon sequence, but not in the 5'-exon. (ii) One of these changes occurred at the splice point leading to a serine instead of a threonine residue in the deduced cox2 polypeptide. In all cases, the alterations resulted in the replacement of more frequently used codons by rare ones. (iii) Although the intron is able to undergo splicing, the sequence motifs thought to be necessary for interaction between the 5'-exon and the intron during the splicing process (the EBS1/IBS1 as well as the EBS2/IBS2 pairings) are unusual. (iv) The intron is inserted at the same location in the cox2 gene as the otherwise unrelated intron from higher plants.","authors":"Schäfer B, Kaulich K, Wolf K","authors_abbrev":"Schäfer B et al.","pubmed_publication_date":"03 Jul 1998","pubmed_entrez_date":"1998-07-04","publication_year":"1998","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23928301","title":"Partitioning of the nuclear and mitochondrial tRNA 3'-end processing activities between two different proteins in Schizosaccharomyces pombe.","citation":"J Biol Chem 2013 Sep 20;288(38):27415-27422","abstract":"tRNase Z is an essential endonuclease responsible for tRNA 3'-end maturation. tRNase Z exists in a short form (tRNase Z(S)) and a long form (tRNase Z(L)). Prokaryotes have only tRNase Z(S), whereas eukaryotes can have both forms of tRNase Z. Most eukaryotes characterized thus far, including Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, and humans, contain only one tRNase Z(L) gene encoding both nuclear and mitochondrial forms of tRNase Z(L). In contrast, Schizosaccharomyces pombe contains two essential tRNase Z(L) genes (trz1 and trz2) encoding two tRNase Z(L) proteins, which are targeted to the nucleus and mitochondria, respectively. Trz1 protein levels are notably higher than Trz2 protein levels. Here, using temperature-sensitive mutants of trz1 and trz2, we provide in vivo evidence that trz1 and trz2 are involved in nuclear and mitochondrial tRNA 3'-end processing, respectively. In addition, trz2 is also involved in generation of the 5'-ends of other mitochondrial RNAs, whose 5'-ends coincide with the 3'-end of tRNA. Thus, our results provide a rare example showing partitioning of the nuclear and mitochondrial tRNase Z(L) activities between two different proteins in S. pombe. The evolution of two tRNase Z(L) genes and their differential expression in fission yeast may avoid toxic off-target effects.","doi":"10.1074/jbc.M113.501569","authors":"Zhang X, Zhao Q, Huang Y","authors_abbrev":"Zhang X et al.","pubmed_publication_date":"20 Sep 2013","pubmed_entrez_date":"2013-08-10","publication_year":"2013","canto_session_key":"c10105abb43a8beb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-09 13:28:47","canto_approved_date":"2026-06-23 08:20:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-21 23:00:18","canto_added_date":"2013-08-21 15:09:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMITTRNALYS.01","SPMITTRNAARG.01","SPBC3D6.03c","SPAC1D4.10","SPMITTRNAARG.02","SPMITTRNAHIS.01"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2018-08-09"},{"uniquename":"PMID:26545776","title":"Identification of Rbd2 as a candidate protease for sterol regulatory element binding protein (SREBP) cleavage in fission yeast.","citation":"Biochem Biophys Res Commun 2015 Dec 25;468(4):606-10","abstract":"Lipid homeostasis in mammalian cells is regulated by sterol regulatory element-binding protein (SREBP) transcription factors that are activated through sequential cleavage by Golgi Site-1 and Site-2 proteases. Fission yeast SREBP, Sre1, engages a different mechanism involving the Golgi Dsc E3 ligase complex, but it is not clearly understood exactly how Sre1 is proteolytically cleaved and activated. In this study, we screened the Schizosaccharomyces pombe non-essential haploid deletion collection to identify missing components of the Sre1 cleavage machinery. Our screen identified an additional component of the SREBP pathway required for Sre1 proteolysis named rhomboid protein 2 (Rbd2). We show that an rbd2 deletion mutant fails to grow under hypoxic and hypoxia-mimetic conditions due to lack of Sre1 activity and that this growth phenotype is rescued by Sre1N, a cleaved active form of Sre1. We found that the growth inhibition phenotype under low oxygen conditions is specific to the strain with deletion of rbd2, not any other fission yeast rhomboid-encoding genes. Our study also identified conserved residues of Rbd2 that are required for Sre1 proteolytic cleavage. All together, our results suggest that Rbd2 is a functional SREBP protease with conserved residues required for Sre1 cleavage and provide an important piece of the puzzle to understand the mechanisms for Sre1 activation and the regulation of various biological and pathological processes involving SREBPs.","doi":"10.1016/j.bbrc.2015.10.165","authors":"Kim J, Ha HJ, Kim S, Choi AR, Lee SJ, Hoe KL, Kim DU","authors_abbrev":"Kim J et al.","pubmed_publication_date":"25 Dec 2015","pubmed_entrez_date":"2015-11-08","publication_year":"2015","canto_session_key":"d9fdf75b5d260a41","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-11-09 01:19:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC790.03","SPBC3B9.15c","SPBC19C2.09","SPBC947.10"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:27037078","title":"Synthetic Genetic Arrays: Automation of Yeast Genetics.","citation":"Cold Spring Harb Protoc 2016 Apr 01;2016(4):pdb.top086652","abstract":"Genome-sequencing efforts have led to great strides in the annotation of protein-coding genes and other genomic elements. The current challenge is to understand the functional role of each gene and how genes work together to modulate cellular processes. Genetic interactions define phenotypic relationships between genes and reveal the functional organization of a cell. Synthetic genetic array (SGA) methodology automates yeast genetics and enables large-scale and systematic mapping of genetic interaction networks in the budding yeast,Saccharomyces cerevisiae SGA facilitates construction of an output array of double mutants from an input array of single mutants through a series of replica pinning steps. Subsequent analysis of genetic interactions from SGA-derived mutants relies on accurate quantification of colony size, which serves as a proxy for fitness. Since its development, SGA has given rise to a variety of other experimental approaches for functional profiling of the yeast genome and has been applied in a multitude of other contexts, such as genome-wide screens for synthetic dosage lethality and integration with high-content screening for systematic assessment of morphology defects. SGA-like strategies can also be implemented similarly in a number of other cell types and organisms, includingSchizosaccharomyces pombe,Escherichia coli, Caenorhabditis elegans, and human cancer cell lines. The genetic networks emerging from these studies not only generate functional wiring diagrams but may also play a key role in our understanding of the complex relationship between genotype and phenotype.","doi":"10.1101/pdb.top086652","authors":"Kuzmin E, Costanzo M, Andrews B, Boone C","authors_abbrev":"Kuzmin E et al.","pubmed_publication_date":"01 Apr 2016","pubmed_entrez_date":"2016-04-03","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-04-04 00:15:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10861909","title":"A family of multifunctional thiamine-repressible expression vectors for fission yeast.","citation":"Yeast 2000 Jun 30;16(9):861-72","abstract":"A series of thiamine-repressible shuttle vectors has been constructed to allow a more efficient DNA manipulation in Schizosaccharomyces pombe. These high-copy-number vectors with regulatable expression (pJR) are based on the backbone of the pREP-3X, pREP-41X and pREP-81X plasmids. The pJR vectors are all uniform in structure, containing: (a) sequences for replication (ori) and selection (AmpR) in Escherichia coli; (b) the f1 ori sequence of the phage f1 for packaging of ssDNA, making them suitable for site-directed mutagenesis; and (c) the ars1 sequence for replication in S. pombe. The pJR vectors differ among them in: (a) the selectable marker (Saccharomyces cerevisiae LEU 2 gene, which complements S. pombe leu1- gene and S. pombe ura4+ and his3+ genes); (b) the thiamine-repressible nmt1 promoter (3X, 41X and 81X with extremely high, moderate or low transcription efficiency, respectively); and (c) the multiple cloning site (two multiple cloning sites, with 12 restriction sites each). The expression level of the pJR vectors has been analysed using the beta-galactosidase gene as reporter. Three levels of expression for each nmt1 promoter version, with any selectable marker and for either repressed or induced conditions, have been found. The expression is dependent on the distance to the initiation codon, varying from 0.001 to 15 times the activity characterized for the pREP plasmids. Also, the gene expression has been found to be extremely sensitive to the nucleotide sequence prior to the initiation codon, being up to 50-fold higher with an A/T sequence than with a G/C sequence. Finally, the beta-galactosidase mRNA levels were found to be similar in each nmt1 series, suggesting a translational effect on gene expression. As a result, any of these 18 new vectors allow performing gene expression in fission yeast, as well as a more versatile cloning, sequencing and mutagenesis, directly in the plasmid without the need for subcloning into intermediary vectors.","authors":"Moreno MB, Durán A, Ribas JC","authors_abbrev":"Moreno MB et al.","pubmed_publication_date":"30 Jun 2000","pubmed_entrez_date":"2000-06-22","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27618268","title":"Bub3-Bub1 Binding to Spc7/KNL1 Toggles the Spindle Checkpoint Switch by Licensing the Interaction of Bub1 with Mad1-Mad2.","citation":"Curr Biol 2016 Oct 10;26(19):2642-2650","abstract":"The spindle assembly checkpoint (SAC) ensures that sister chromatids do not separate until all chromosomes are attached to spindle microtubules and bi-oriented. Spindle checkpoint proteins, including Mad1, Mad2, Mad3 (BubR1), Bub1, Bub3, and Mph1 (Mps1), are recruited to unattached and/or tensionless kinetochores. SAC activation catalyzes the conversion of soluble Mad2 (O-Mad2) into a form (C-Mad2) that binds Cdc20, BubR1, and Bub3 to form the mitotic checkpoint complex (MCC), a potent inhibitor of the anaphase-promoting complex (APC/C). SAC silencing de-represses Cdc20-APC/C activity allowing poly-ubiquitination of Securin and Cyclin B, leading to the dissolution of sister chromatids and anaphase onset [1]. Understanding how microtubule interaction at kinetochores influences the timing of anaphase requires an understanding of how spindle checkpoint protein interaction with the kinetochore influences spindle checkpoint signaling. We, and others, recently showed that Mph1 (Mps1) phosphorylates multiple conserved MELT motifs in the Spc7 (Spc105/KNL1) protein to recruit Bub1, Bub3, and Mad3 (BubR1) to kinetochores [2-4]. In budding yeast, Mps1 phosphorylation of a central non-catalytic region of Bub1 promotes its association with the Mad1-Mad2 complex, although this association has not yet been detected in other organisms [5]. Here we report that multisite binding of Bub3 to the Spc7 MELT array toggles the spindle checkpoint switch by permitting Mph1 (Mps1)-dependent interaction of Bub1 with Mad1-Mad2.","doi":"10.1016/j.cub.2016.07.040","authors":"Mora-Santos MD, Hervas-Aguilar A, Sewart K, Lancaster TC, Meadows JC, Millar JB","authors_abbrev":"Mora-Santos MD et al.","pubmed_publication_date":"10 Oct 2016","pubmed_entrez_date":"2016-09-13","publication_year":"2016","canto_session_key":"f6a5a7da08695182","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-15 12:08:21","canto_approved_date":"2026-01-15 08:49:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-01-17 21:44:02","canto_added_date":"2017-12-28 01:15:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":36,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.01","SPBC776.02c","SPAC23H3.08c","SPCC1795.01c","SPBC106.01","SPCC1020.02","SPBC20F10.06","SPAC23C11.16","SPBC26H8.07c","SPCC1322.12c","SPBC582.03","SPBC3D6.04c"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2018-01-15"},{"uniquename":"PMID:32920715","title":"FSH1 encodes lysophospholipase activity in Saccharomyces cerevisiae.","citation":"Biotechnol Lett 2021 Jan;43(1):279-286","abstract":"To elucidate the role of FSH1 (family of serine hydrolase) in lipid homeostasis.\nProteins in various species containing alpha/beta hydrolase domain are known to be involved in lipid metabolism. In silico analysis of the FSH1 gene in Saccharomyces cerevisiae revealed the presence of alpha/beta hydrolase domain (ABHD) and a lipase motif (GXSXG), however its function in lipid metabolism remained elusive. The overexpression of FSH1 in WT and fsh1Δ cells showed a significant reduction in the cellular phospholipid levels and an increase in the triacylglycerol levels and lipid droplet (LD) number. Furthermore, the purified recombinant protein Fsh1p was identified as a lysophospholipase that specifically acts on lysophosphatidylserine (LPS) and impacts the lipid homeostasis in S. cerevisiae.\nThese results depicted that Fsh1p has a role on lipid homeostasis and is a lysophospholipase that hydrolyzes lysophosphatidylserine (LPS).","doi":"10.1007/s10529-020-03004-x","authors":"Ramachandran G, Chidambaram R, Nachiappan V","authors_abbrev":"Ramachandran G et al.","pubmed_publication_date":"Jan 2021","pubmed_entrez_date":"2020-09-13","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1223.08c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPC03596","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15620885","title":"A glucanase-driven fractionation allows redefinition of Schizosaccharomyces pombe cell wall composition and structure: assignment of diglucan.","citation":"Anal Biochem 2005 Jan 15;336(2):202-12","abstract":"Purified endoglucanases have been used to determine the composition of Schizosaccharomyces pombe cell wall. This structure has been traditionally studied after isolating its components (mannoproteins, alpha1,3-glucan, beta1,3-glucan, and a branched beta-glucan) with hot alkali. Instead, we sequentially removed the polysaccharides by digesting with endo-beta1,3-glucanase and with a novel endo-alpha1,3-glucanase (mutanase). After this gentle isolation we observed that a branched beta1,3-beta1,6-glucan is much more abundant than previously described. By scaling-up the new protocol we prepared large amounts of the highly branched glucan and determined its structural features. We have named this highly branched beta-glucan diglucan, reflecting its two types of beta linkages. We have also identified an insoluble endoglucanase-resistant type of 1,3-linked glucan present in S. pombe cell walls. We redefined the wall composition of S. pombe vegetative cells by this new method. Finally, to demonstrate its application, we determined the cell wall composition of known mutant strains.","authors":"Magnelli PE, Cipollo JF, Robbins PW","authors_abbrev":"Magnelli PE et al.","pubmed_publication_date":"15 Jan 2005","pubmed_entrez_date":"2004-12-29","publication_year":"2005","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41909949","title":"Exploration of the proxiOME of large subunit ribosomal proteins reveals Acl1 and Bcl1 as cooperating dedicated chaperones of Rpl1.","citation":"Nucleic Acids Res 2026 Mar 19;54(6)","abstract":"In eukaryotes, most newly synthesized ribosomal proteins (r-proteins) need to rapidly and safely get into the nucleus to reach their assembly site on pre-ribosomal particles. However, only for few r-proteins tailored support mechanisms involving so-called dedicated chaperones (DCs) could so far be revealed. Here, with the primary aim of identifying novel DCs, we performed TurboID-based proximity labelling with all 46 large subunit r-proteins of Saccharomyces cerevisiae, which unveiled the fungi-specific Acl1 and the conserved Bcl1 as candidate DCs of Rpl1. We show that the functionally cooperating Acl1 and Bcl1 both directly interact with Rpl1, form a trimeric Acl1-Rpl1-Bcl1 complex, and enable the nuclear import of Rpl1. Moreover, our crystal structure of the minimal Acl1-Rpl1 complex reveals how Acl1's ankyrin repeat domain shields a positively charged ribosomal RNA-binding surface of Rpl1. Our proximity labelling approach also permitted to establish novel interactions between four r-proteins and distinct importins and to illuminate r-protein neighbourhoods on successive pre-60S particles. Additionally, reciprocal proximity labelling with the known DCs indicates that almost all appear to be transiently associated with pre-ribosomal particles. Our study provides for the first time comprehensive insight into the physical proximities of large subunit r-proteins along their entire life cycle.","doi":"10.1093/nar/gkag264","authors":"Favre S, Pillet B, Burchert F, Siva Sankar D, Méndez-Godoy A, Kiontke S, Dengjel J, Bange G, Kressler D","authors_abbrev":"Favre S et al.","pubmed_publication_date":"19 Mar 2026","pubmed_entrez_date":"2026-03-30","publication_year":"2026","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCP1E11.10","SPCC1183.08c","SPCC63.06"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:23885124","title":"Fission yeast MOZART1/Mzt1 is an essential γ-tubulin complex component required for complex recruitment to the microtubule organizing center, but not its assembly.","citation":"Mol Biol Cell 2013 Sep;24(18):2894-906","abstract":"γ-Tubulin plays a universal role in microtubule nucleation from microtubule organizing centers (MTOCs) such as the animal centrosome and fungal spindle pole body (SPB). γ-Tubulin functions as a multiprotein complex called the γ-tubulin complex (γ-TuC), consisting of GCP1-6 (GCP1 is γ-tubulin). In fungi and flies, it has been shown that GCP1-3 are core components, as they are indispensable for γ-TuC complex assembly and cell division, whereas the other three GCPs are not. Recently a novel conserved component, MOZART1, was identified in humans and plants, but its precise functions remain to be determined. In this paper, we characterize the fission yeast homologue Mzt1, showing that it is essential for cell viability. Mzt1 is present in approximately equal stoichiometry with Alp4/GCP2 and localizes to all the MTOCs, including the SPB and interphase and equatorial MTOCs. Temperature-sensitive mzt1 mutants display varying degrees of compromised microtubule organization, exhibiting multiple defects during both interphase and mitosis. Mzt1 is required for γ-TuC recruitment, but not sufficient to localize to the SPB, which depends on γ-TuC integrity. Intriguingly, the core γ-TuC assembles in the absence of Mzt1. Mzt1 therefore plays a unique role within the γ-TuC components in attachment of this complex to the major MTOC site.","doi":"10.1091/mbc.E13-05-0235","authors":"Masuda H, Mori R, Yukawa M, Toda T","authors_abbrev":"Masuda H et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-07-26","publication_year":"2013","canto_session_key":"26c28361072dd950","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2013-12-04 12:17:17","canto_approved_date":"2025-09-04 07:15:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-01 15:48:24","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Hiro Masuda","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Takashi Toda","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPBC800.05c","SPBC428.20c","SPBC365.15","SPAC9G1.15c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2013-12-04"},{"uniquename":"PMID:17561805","title":"Dynein participates in chromosome segregation in fission yeast.","citation":"Biol Cell 2007 Nov;99(11):627-37","abstract":"In eukaryotic cells, proper formation of the spindle is necessary for successful cell division. For faithful segregation of sister chromatids, each sister kinetochore must attach to microtubules that extend to opposite poles (chromosome bi-orientation). At the metaphase-anaphase transition, cohesion between sister chromatids is removed, and each sister chromatid is pulled to opposite poles of the cell by microtubule-dependent forces.\nWe have studied the role of the minus-end-directed motor protein dynein by analysing kinetochore dynamics in fission yeast cells deleted for the dynein heavy chain (Dhc1) or the light chain (Dlc1). In these mutants, we found an increased frequency of cells showing defects in chromosome segregation, which leads to the appearance of lagging chromosomes and an increased rate of chromosome loss. By following simultaneously kinetochore dynamics and localization of the checkpoint protein Mad2, we provide evidence that dynein function is not necessary for spindle-assembly checkpoint inactivation. Instead, we have demonstrated that loss of dynein function alters chromosome segregation and activates the Mad2-dependent spindle-assembly checkpoint.\nThese results show an unexpected role for dynein in the control of chromosome segregation in fission yeast, most probably operating during the process of bi-orientation during early mitosis.","authors":"Courtheoux T, Gay G, Reyes C, Goldstone S, Gachet Y, Tournier S","authors_abbrev":"Courtheoux T et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-06-15","publication_year":"2007","canto_session_key":"5d95c2f1713ccd8c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-02-01 15:45:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-28 16:35:25","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.08","SPAC18G6.15","SPAC1093.06c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-11-28"},{"uniquename":"PMID:26990647","title":"Swi1Timeless Prevents Repeat Instability at Fission Yeast Telomeres.","citation":"PLoS Genet 2016 Mar;12(3):e1005943","abstract":"Genomic instability associated with DNA replication stress is linked to cancer and genetic pathologies in humans. If not properly regulated, replication stress, such as fork stalling and collapse, can be induced at natural replication impediments present throughout the genome. The fork protection complex (FPC) is thought to play a critical role in stabilizing stalled replication forks at several known replication barriers including eukaryotic rDNA genes and the fission yeast mating-type locus. However, little is known about the role of the FPC at other natural impediments including telomeres. Telomeres are considered to be difficult to replicate due to the presence of repetitive GT-rich sequences and telomere-binding proteins. However, the regulatory mechanism that ensures telomere replication is not fully understood. Here, we report the role of the fission yeast Swi1(Timeless), a subunit of the FPC, in telomere replication. Loss of Swi1 causes telomere shortening in a telomerase-independent manner. Our epistasis analyses suggest that heterochromatin and telomere-binding proteins are not major impediments for telomere replication in the absence of Swi1. Instead, repetitive DNA sequences impair telomere integrity in swi1Δ mutant cells, leading to the loss of repeat DNA. In the absence of Swi1, telomere shortening is accompanied with an increased recruitment of Rad52 recombinase and more frequent amplification of telomere/subtelomeres, reminiscent of tumor cells that utilize the alternative lengthening of telomeres pathway (ALT) to maintain telomeres. These results suggest that Swi1 ensures telomere replication by suppressing recombination and repeat instability at telomeres. Our studies may also be relevant in understanding the potential role of Swi1(Timeless) in regulation of telomere stability in cancer cells.","doi":"10.1371/journal.pgen.1005943","authors":"Gadaleta MC, Das MM, Tanizawa H, Chang YT, Noma K, Nakamura TM, Noguchi E","authors_abbrev":"Gadaleta MC et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2016-03-19","publication_year":"2016","canto_session_key":"7433fd9f135a932e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Eishi Noguchi","canto_first_approved_date":"2026-05-22 05:44:01","canto_approved_date":"2026-05-22 05:44:01","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-02-27 14:36:40","canto_added_date":"2016-03-29 00:15:12","annotation_curators":[{"name":"Eishi Noguchi","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":32,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.08","SPBC2D10.13","SPCC23B6.03c","SPAC30D11.10","SPAC19G12.13c","SPAC6F6.17","SPAC16A10.07c","SPAC664.01c","SPBC30D10.04","SPCC1259.13","SPBC216.06c","SPBC216.05","SPBC428.08c","SPBC29A3.14c","SPCC18B5.11c","SPAC644.14c"],"gene_count":16,"ltp_gene_count":15,"approved_date":"2026-05-22"},{"uniquename":"PMID:27480719","title":"Synchronizing Progression of Schizosaccharomyces pombe Cells from Prophase through Mitosis and into S Phase with nda3-KM311 Arrest Release.","citation":"Cold Spring Harb Protoc 2016 Aug 01;2016(8)","abstract":"Here, we describe how the rapid reversibility of the nda3-KM311 cold-sensitive β-tubulin mutation was optimized by Mitsuhiro Yanagida's laboratory to synchronize mitotic progression in an entire cell population. The inability to form microtubules following the loss of β-tubulin function at 20°C triggers the spindle assembly checkpoint, which arrests mitotic progression. Restoration of β-tubulin function by rewarming to 30°C (or higher) releases the arrest, generating a highly synchronous progression through mitosis. The viability of nda3-KM311 strains at 30°C makes it feasible to generate double mutants between nda3-KM311 and any temperature-sensitive mutant that can also grow at 30°C. These double mutants can be used in reciprocal shift analyses, in which cold-induced early mitotic arrest is relieved by a shift to 36°C, which then inactivates the product of the second mutant gene. The addition of microtubule depolymerizing drugs before the return to 36°C will maintain checkpoint signaling at 36°C transiently, permitting analysis of the impact of temperature-sensitive mutations on checkpoint function. Silencing the checkpoint of nda3-KM311-arrested cells at 20°C through chemical inhibition of aurora kinase is a powerful way to study checkpoint recovery pathways and mitotic exit without anaphase.","doi":"10.1101/pdb.prot091256","authors":"Hagan IM, Grallert A, Simanis V","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"01 Aug 2016","pubmed_entrez_date":"2016-08-03","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-08-04 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32817556","title":"Integrity of a heterochromatic domain ensured by its boundary elements.","citation":"Proc Natl Acad Sci U S A 2020 Sep 01;117(35):21504-21511","abstract":"In fission yeast, the inverted repeats  IR-L  and  IR-R  function as boundary elements at the edges of a 20-kb silent heterochromatic domain where nucleosomes are methylated at histone H3K9. Each repeat contains a series of B-box motifs physically associated with the architectural TFIIIC complex and with other factors including the replication regulator Sap1 and the Rix1 complex (RIXC). We demonstrate here the activity of these repeats in heterochromatin formation and maintenance. Deletion of the entire  IR-R  repeat or, to a lesser degree, deletion of just the B boxes impaired the de novo establishment of the heterochromatic domain. Nucleation proceeded normally at the RNA interference (RNAi)-dependent element  cenH  but subsequent propagation to the rest of the region occurred at reduced rates in the mutants. Once established, heterochromatin was unstable in the mutants. These defects resulted in bistable populations of cells occupying alternate \"on\" and \"off\" epigenetic states. Deleting  IR-L  in combination with  IR-R  synergistically tipped the balance toward the derepressed state, revealing a concerted action of the two boundaries at a distance. The nuclear rim protein Amo1 has been proposed to tether the mating-type region and its boundaries to the nuclear envelope, where Amo1 mutants displayed milder phenotypes than boundary mutants. Thus, the boundaries might facilitate heterochromatin propagation and maintenance in ways other than just through Amo1, perhaps by constraining a looped domain through pairing.","doi":"10.1073/pnas.2010062117","authors":"Charlton SJ, Jørgensen MM, Thon G","authors_abbrev":"Charlton SJ et al.","pubmed_publication_date":"01 Sep 2020","pubmed_entrez_date":"2020-08-21","publication_year":"2020","canto_session_key":"f0c27afd512b81c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sebastian Charlton","canto_first_approved_date":"2021-02-19 11:18:39","canto_approved_date":"2021-02-19 11:18:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-02-10 09:36:46","canto_added_date":"2020-08-22 00:15:05","annotation_curators":[{"name":"Sebastian Charlton","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC15D4.10c","SPAC14C4.05c","SPBC19C7.10","SPAC18G6.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2021-02-19"},{"uniquename":"PMID:15225554","title":"A 2-Cys peroxiredoxin regulates peroxide-induced oxidation and activation of a stress-activated MAP kinase.","citation":"Mol Cell 2004 Jul 02;15(1):129-39","abstract":"Oxidative stress-induced cell damage is an important component of many diseases and ageing. In eukaryotes, activation of JNK/p38 stress-activated protein kinase (SAPK) signaling pathways is critical for the cellular response to stress. 2-Cys peroxiredoxins (2-Cys Prx) are highly conserved, extremely abundant antioxidant enzymes that catalyze the breakdown of peroxides to protect cells from oxidative stress. Here we reveal that Tpx1, the single 2-Cys Prx in Schizosaccharomyces pombe, is required for the peroxide-induced activation of the p38/JNK homolog, Sty1. Tpx1 activates Sty1, downstream of previously identified redox sensors, by a mechanism that involves formation of a peroxide-induced disulphide complex between Tpx1 and Sty1. We have identified conserved cysteines in Tpx1 and Sty1 that are essential for normal peroxide-induced Tpx1-Sty1 disulphide formation and Tpx1-dependent regulation of peroxide-induced Sty1 activation. Thus we provide new insight into the response of SAPKs to diverse stimuli by revealing a mechanism for SAPK activation specifically by oxidative stress.","authors":"Veal EA, Findlay VJ, Day AM, Bozonet SM, Evans JM, Quinn J, Morgan BA","authors_abbrev":"Veal EA et al.","pubmed_publication_date":"02 Jul 2004","pubmed_entrez_date":"2004-07-01","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPCC576.03c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:27197211","title":"Divergence of a conserved elongation factor and transcription regulation in budding and fission yeast.","citation":"Genome Res 2016 Jun;26(6):799-811","abstract":"Complex regulation of gene expression in mammals has evolved from simpler eukaryotic systems, yet the mechanistic features of this evolution remain elusive. Here, we compared the transcriptional landscapes of the distantly related budding and fission yeast. We adapted the Precision Run-On sequencing (PRO-seq) approach to map the positions of RNA polymerase active sites genome-wide in Schizosaccharomyces pombe and Saccharomyces cerevisiae. Additionally, we mapped preferred sites of transcription initiation in each organism using PRO-cap. Unexpectedly, we identify a pause in early elongation, specific to S. pombe, that requires the conserved elongation factor subunit Spt4 and resembles promoter-proximal pausing in metazoans. PRO-seq profiles in strains lacking Spt4 reveal globally elevated levels of transcribing RNA Polymerase II (Pol II) within genes in both species. Messenger RNA abundance, however, does not reflect the increases in Pol II density, indicating a global reduction in elongation rate. Together, our results provide the first base-pair resolution map of transcription elongation in S. pombe and identify divergent roles for Spt4 in controlling elongation in budding and fission yeast.","doi":"10.1101/gr.204578.116","authors":"Booth GT, Wang IX, Cheung VG, Lis JT","authors_abbrev":"Booth GT et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-05-20","publication_year":"2016","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2016-05-21 00:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38404922","title":"Diverse modes of chromosome terminal deletion in spontaneous canavanine-resistant  Schizosaccharomyces pombe  mutants.","citation":"MicroPubl Biol 2024;2024","abstract":"Canavanine resistance has been used to analyze mutation rates in the fission yeast  Schizosaccharomyces pombe  . However, the genetic basis of canavanine resistance in this organism remains incompletely understood. Here, we performed whole genome sequencing on five spontaneously arising canavanine-resistant  S. pombe  mutants, including the  can2-1  mutant isolated in the 1970s. This analysis revealed that three mutants, including  can2-1  , experienced terminal deletions of the left arm of chromosome II, leading to the loss of multiple amino acid transporter genes. Interestingly, these three mutants underwent chromosome terminal deletion through distinct mechanisms, including homology-driven translocation, homology-independent chromosome fusion, and de novo telomere addition. Our findings shed new light on the genetic basis of canavanine resistance and mechanisms underlying chromosome terminal deletions in fission yeast.","doi":"10.17912/micropub.biology.001132","authors":"Lyu XH, Suo F, Li W, Jia GS, Yang YS, Du LL","authors_abbrev":"Lyu XH et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-02-26","publication_year":"2024","canto_session_key":"283bb41fb7d43ee6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-10-14 08:51:20","canto_approved_date":"2024-10-14 08:51:20","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-10-11 04:07:24","canto_added_date":"2024-02-27 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC651.08c","SPCC1223.07c","SPBC359.01","SPBC359.03c","SPBC460.01c"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2024-10-14"},{"uniquename":"PMID:2849043","title":"Evidence that DNA topoisomerase I is necessary for the cytotoxic effects of camptothecin.","citation":"Mol Pharmacol 1988 Dec;34(6):755-60","abstract":"The budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe are both sensitive to camptothecin, an inhibitor of DNA topoisomerase I. An S. cerevisiae DNA repair mutant, rad52, is hypersensitive to the drug. In both species, topoisomerase I mutants totally lacking the enzyme are completely resistant to the drug. A strain with a mutation leading to a temperature-sensitive topoisomerase I exhibits temperature dependence in its in vivo response to camptothecin. A strain carrying a plasmid that overproduces topoisomerase I is hypersensitive to the drug. The rad52 mutant is killed by overproduction of the enzyme, even in the absence of the drug. The response of several of these strains to camptothecin analogs, to DNA topoisomerase II inhibitors, and to other drugs is reported. The cytotoxic effects of camptothecin are discussed in terms of the drug extending the lifetime of a topoisomerase I-DNA covalent intermediate, which is recognized as DNA damage by a DNA repair system.","authors":"Eng WK, Faucette L, Johnson RK, Sternglanz R","authors_abbrev":"Eng WK et al.","pubmed_publication_date":"Dec 1988","pubmed_entrez_date":"1988-12-01","publication_year":"1988","canto_session_key":"1a1c5dc821a44d18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-03-04 15:24:20","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-25 09:29:12","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1703.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-25"},{"uniquename":"PMID:1899284","title":"The Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae HAP2 reveals selective and stringent conservation of the small essential core protein domain.","citation":"Mol Cell Biol 1991 Feb;11(2):611-9","abstract":"The fission yeast Schizosaccharomyces pombe is immensely diverged from budding yeast (Saccharomyces cerevisiae) on an evolutionary time scale. We have used a fission yeast library to clone a homolog of S. cerevisiae HAP2, which along with HAP3 and HAP4 forms a transcriptional activation complex that binds to the CCAAT box. The S. pombe homolog php2 (S. pombe HAP2) was obtained by functional complementation in an S. cerevisiae hap2 mutant and retains the ability to associate with HAP3 and HAP4. We have previously demonstrated that the HAP2 subunit of the CCAAT-binding transcriptional activation complex from S. cerevisiae contains a 65-amino-acid \"essential core\" structure that is divisible into subunit association and DNA recognition domains. Here we show that Php2 contains a 60-amino-acid block that is 82% identical to this core. The remainder of the 334-amino-acid protein is completely without homology to HAP2. The function of php2 in S. pombe was investigated by disrupting the gene. Strikingly, like HAP2 in S. cerevisiae, the S. pombe gene is specifically involved in mitochondrial function. This contrasts to the situation in mammals, in which the homologous CCAAT-binding complex is a global transcriptional activator.","authors":"Olesen JT, Fikes JD, Guarente L","authors_abbrev":"Olesen JT et al.","pubmed_publication_date":"Feb 1991","pubmed_entrez_date":"1991-02-01","publication_year":"1991","canto_session_key":"30e4ef054e6bbaf7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-08-03 15:37:49","canto_approved_date":"2021-04-15 16:31:08","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-04 09:02:19","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-08-03"},{"uniquename":"PMID:24521463","title":"A genetic approach to study H2O2 scavenging in fission yeast--distinct roles of peroxiredoxin and catalase.","citation":"Mol Microbiol 2014 Apr;92(2):246-57","abstract":"The main peroxiredoxin in Schizosaccharomyces pombe, Tpx1, is important to sustain aerobic growth, and cells lacking this protein are only able to grow on solid plates under anaerobic conditions. We have found that deletion of the gene coding for thioredoxin reductase, trr1, is a suppressor of the sensitivity to aerobic growth of Δtpx1 cells, so that cells lacking both proteins are able to grow on solid plates in the presence of oxygen. We have investigated this suppression effect, and determined that it depends on the presence of catalase, which is constitutively expressed in Δtrr1 cells in a transcription factor Pap1-dependent manner. A complete characterization of the repertoire of hydrogen peroxide scavenging activities in fission yeast suggests that Tpx1 is the only enzyme with sufficient sensitivity for peroxides and cellular abundance as to control the low levels produced during aerobic growth, catalase being the next barrier of detoxification when the steady-state levels of peroxides are increased in Δtpx1 cells. Gpx1, the only glutathione peroxidase encoded by the S. pombe genome, only has a minor secondary role when extracellular peroxides are added. Our study proposes non-overlapping roles for the different hydrogen peroxide scavenging activities of this eukaryotic organism.","doi":"10.1111/mmi.12548","authors":"Paulo E, García-Santamarina S, Calvo IA, Carmona M, Boronat S, Domènech A, Ayté J, Hidalgo E","authors_abbrev":"Paulo E et al.","pubmed_publication_date":"Apr 2014","pubmed_entrez_date":"2014-02-14","publication_year":"2014","canto_session_key":"199abb8a7b85407c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-24 15:52:48","canto_approved_date":"2025-05-28 22:28:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-05 12:10:59","canto_added_date":"2014-02-16 05:46:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Elena Hidalgo","community_curator":false,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.06c","SPCC576.03c","SPBC32F12.03c","SPCC757.07c","SPBC29B5.01","SPAC1783.07c","SPBC3F6.03","SPBC1773.02c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-07-24"},{"uniquename":"PMID:15381397","title":"Unique biosynthesis of dehydroquinic acid?","citation":"Bioorg Chem 2004 Oct;32(5):309-15","abstract":"A search of the genomic sequences of the thermophilic microorganisms Aquifex aeolicus, Archaeoglobus fulgidus, Methanobacterium thermoautotrophicum, and Methanococcus jannaschii for the first seven enzymes (aroG, B, D, E, K, A, and C ) involved in the shikimic acid biosynthetic pathway reveal two key enzymes are missing. The first enzyme in the pathway, 3-deoxy-d-arabino-heptulosonic acid 7-phosphate synthase (aroG) and the second enzyme in the pathway, 5-dehydroquinic acid synthase (aroB) are \"missing.\" The remaining five genes for the shikimate pathway in these organism are present and are similar to the corresponding Escherichia coli genes. The genomic sequences of the thermophiles Pyrococcus abyssi and Thermotoga maritima contain the aroG and aroB genes. Several fungi such as Aspergillus fumigatus, Aspergillus nidulans, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Pneumocystis carinii f. sp. carinii, and Neurospora crassa contain the gene aroM, a pentafunctional enzyme whose overall activity is equivalent to the combined catalytic activities of proteins expressed by aroB, D, E, K, and A genes. Two of these fungi also lack an aroG gene. A discussion of potential reasons for these missing enzymes is presented.","authors":"Woodard RW","authors_abbrev":"Woodard RW","pubmed_publication_date":"Oct 2004","pubmed_entrez_date":"2004-09-24","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27223649","title":"Unraveling Site-Specific and Combinatorial Histone Modifications Using High-Resolution Mass Spectrometry in Histone Deacetylase Mutants of Fission Yeast.","citation":"J Proteome Res 2016 Jul 01;15(7):2132-42","abstract":"Histone deacetylases (HDACs) catalyze the removal of acetylation marks from lysine residues on histone and nonhistone substrates. Their activity is generally associated with essential cellular processes such as transcriptional repression and heterochromatin formation. Interestingly, abnormal activity of HDACs has been reported in various types of cancers, which makes them a promising therapeutic target for cancer treatment. In the current study, we aim to understand the mechanisms underlying the function of HDACs using an in-depth quantitative analysis of changes in histone acetylation levels in Schizosaccharomyces pombe (S. pombe) lacking major HDAC activities. We employed a targeted quantitative mass spectrometry approach to profile changes of acetylation and methylation at multiple lysine residues on the N-terminal tail of histones H3 and H4. Our analyses identified a number of histone acetylation sites that are significantly affected by S. pombe HDAC mutations. We discovered that mutation of the Class I HDAC known as Clr6 causes a major increase in the abundance of triacetylated H4 molecules at K5, K8, and K12. A clr6-1 hypomorphic mutation also increased the abundance of multiple acetyl-lysines in histone H3. In addition, our study uncovered a few crosstalks between histone acetylation and methylation upon deletion of HDACs Hos2 and Clr3. We anticipate that the results from this study will greatly improve our current understanding of the mechanisms involved in HDAC-mediated gene regulation and heterochromatin assembly.","doi":"10.1021/acs.jproteome.5b01156","authors":"Abshiru N, Rajan RE, Verreault A, Thibault P","authors_abbrev":"Abshiru N et al.","pubmed_publication_date":"01 Jul 2016","pubmed_entrez_date":"2016-05-26","publication_year":"2016","canto_session_key":"83ed035e12b1754a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-05-27 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25521247","title":"Mechanical design principles of a mitotic spindle.","citation":"Elife 2014 Dec 18;3:e03398","abstract":"An organised spindle is crucial to the fidelity of chromosome segregation, but the relationship between spindle structure and function is not well understood in any cell type. The anaphase B spindle in fission yeast has a slender morphology and must elongate against compressive forces. This 'pushing' mode of chromosome transport renders the spindle susceptible to breakage, as observed in cells with a variety of defects. Here we perform electron tomographic analyses of the spindle, which suggest that it organises a limited supply of structural components to increase its compressive strength. Structural integrity is maintained throughout the spindle's fourfold elongation by organising microtubules into a rigid transverse array, preserving correct microtubule number and dynamically rescaling microtubule length.","doi":"10.7554/eLife.03398","authors":"Ward JJ, Roque H, Antony C, Nédélec F","authors_abbrev":"Ward JJ et al.","pubmed_publication_date":"18 Dec 2014","pubmed_entrez_date":"2014-12-19","publication_year":"2014","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-12-20 01:16:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20519959","title":"S. pombe genome deletion project: an update.","citation":"Cell Cycle 2010 Jun 15;9(12):2399-402","abstract":"The fission yeast Schizosaccharomyces pombe is a model organism used widely to study various aspects of eukaryotic biology. A collection of heterozygous diploid strains containing individual deletions in nearly all S. pombe genes has been created using a PCR based strategy. However, deletion of some genes has not been possible using this methodology. Here we use an efficient knockout strategy based on plasmids that contain large regions homologous to the target gene to delete an additional 29 genes. The collection of deletion mutants now covers 99% of the fission yeast open reading frames.","authors":"Spirek M, Benko Z, Carnecka M, Rumpf C, Cipak L, Batova M, Marova I, Nam M, Kim DU, Park HO, Hayles J, Hoe KL, Nurse P, Gregan J","authors_abbrev":"Spirek M et al.","pubmed_publication_date":"15 Jun 2010","pubmed_entrez_date":"2010-06-04","publication_year":"2010","canto_session_key":"30a1db59c11b37b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-21 09:39:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-12 15:57:05","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":51,"orcid":"0000-0001-6330-7526","file_type":"PHAF","file_name":"PMID_20519959_phaf.tsv"}],"genes":["SPAC23C4.04c","SPAC1952.13","SPAC4D7.08c","SPBPB8B6.03","SPAC589.12","SPBC3H7.15","SPAC1786.02","SPBC23G7.09","SPBC119.10","SPAC23D3.14c","SPBC146.13c","SPCC290.04","SPBC16C6.09","SPAC2C4.11c","SPAC3A11.05c","SPBPB8B6.06c","SPAPB1A10.16","SPAC9.09","SPAC56F8.10","SPAC56F8.07","SPAPB15E9.01c","SPBC21D10.06c","SPCC1393.14","SPBC16G5.19","SPBC215.15","SPBC800.14c","SPBP23A10.11c","SPAPB18E9.02c","SPCC18.04","SPBC17G9.06c","SPCC191.02c","SPBC32F12.01c","SPAC1F7.04","SPBC685.08","SPAC30D11.09","SPCC1682.05c","SPBC1778.01c","SPAC3H8.10","SPBC6B1.12c","SPCC645.05c","SPAPB1E7.02c","SPBC543.04","SPAC1250.07","SPBC428.19c","SPAC2F7.16c","SPAC1B1.03c","SPBC365.05c","SPAC1F3.04c","SPAC15E1.03","SPAC27E2.12"],"gene_count":50,"ltp_gene_count":0,"approved_date":"2012-11-12"},{"uniquename":"PMID:9742398","title":"Conjugation in S. pombe: identification of a microtubule-organising centre, a requirement for microtubules and a role for Mad2.","citation":"Curr Biol 1998 Aug 27;8(17):963-6","abstract":"During the G1 phase of the cell cycle, cells of the fission yeast Schizosaccharomyces pombe can be induced to mate by nitrogen starvation and the presence of mating pheromones. Polarised growth towards cells of the opposite mating type (P or M) leads to the formation of a projection tip and, upon contact, localised cell wall degradation results in conjugation and cell fusion [1]. Here, we have investigated the role of microtubules in this process. We describe a previously unidentified microtubule-organising centre (MTOC) that forms at projection tips upon cell-to-cell contact, before cells fuse. Treatment of mating cells with the microtubule-destabilising drug thiabendazole (TBZ) showed that microtubule integrity was required for mating at two distinct stages: during projection tip formation and cell fusion. Projection tip formation requires filamentous (F) actin function [2] and microtubules are required for the localisation of F actin to the projection tip. We also identify a role during mating for Mad2--a mitotic checkpoint protein that is required in all eukaryotes to maintain the mitotic state in response to microtubule depolymerisation [3]. S. pombe mad2 mutant cells were compromised in their ability to mate upon removal of TBZ, indicating that in fission yeast, in the absence of microtubules, Mad2 is also required to maintain mating competence.","authors":"Petersen J, Heitz MJ, Hagan IM","authors_abbrev":"Petersen J et al.","pubmed_publication_date":"27 Aug 1998","pubmed_entrez_date":"1998-09-22","publication_year":"1998","canto_session_key":"5accdfac6f642a2c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-14 16:54:43","canto_approved_date":"2026-01-04 12:49:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-14 16:54:35","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPBC354.01","SPAC20G4.02c","SPBC20F10.06"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2018-06-14"},{"uniquename":"PMID:6526270","title":"Sequence of the cell division gene CDC2 from Schizosaccharomyces pombe; patterns of splicing and homology to protein kinases.","citation":"Gene 1984 Nov;31(1-3):129-34","abstract":"The complete nucleotide sequence of a 2.9-kb DNA fragment containing the CDC2 gene-complementing activity from Schizosaccharomyces pombe has been determined. Within this region lies a 1.69-kb DNA sequence whose predicted amino acid sequence shows extensive homology to that previously deduced for the CDC28 gene product from Saccharomyces cerevisiae [Lörincz and Reed, Nature 307 (1984) 183-185]. Taken with the earlier observation that mutants in CDC2 can be rescued by the presence of the CDC28 gene [Beach, Durkacz and Nurse, Nature 300 (1982) 706-709], these results strongly suggest that the two genes code for similar functions. In contrast to the CDC28 gene, however, which contains no introns, the CDC2 coding sequence is split by four introns and from a comparison of the two sequences a consensus sequence for intron splicing in S. pombe can be established. Both CDC2 and CDC28 contain the consensus sequences for the ATP binding and phosphorylation acceptor sites of protein kinases such as bovine cAMP-dependent protein kinase (bov PK) and the src family of viral oncogene products.","authors":"Hindley J, Phear GA","authors_abbrev":"Hindley J et al.","pubmed_publication_date":"Nov 1984","pubmed_entrez_date":"1984-11-01","publication_year":"1984","canto_session_key":"b454d44b7871cf46","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-05 07:09:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-04 18:37:14","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-03-04"},{"uniquename":"PMID:37164017","title":"Optimization of energy production and central carbon metabolism in a non-respiring eukaryote.","citation":"Curr Biol 2023 Jun 05;33(11):2175-2186.e5","abstract":"Most eukaryotes respire oxygen, using it to generate biomass and energy. However, a few organisms have lost the capacity to respire. Understanding how they manage biomass and energy production may illuminate the critical points at which respiration feeds into central carbon metabolism and explain possible routes to its optimization. Here, we use two related fission yeasts, Schizosaccharomyces pombe and Schizosaccharomyces japonicus, as a comparative model system. We show that although S. japonicus does not respire oxygen, unlike S. pombe, it is capable of efficient NADH oxidation, amino acid synthesis, and ATP generation. We probe possible optimization strategies through the use of stable isotope tracing metabolomics, mass isotopologue distribution analysis, genetics, and physiological experiments. S. japonicus appears to have optimized cytosolic NADH oxidation via glycerol-3-phosphate synthesis. It runs a fully bifurcated TCA pathway, sustaining amino acid production. Finally, we propose that it has optimized glycolysis to maintain high ATP/ADP ratio, in part by using the pentose phosphate pathway as a glycolytic shunt, reducing allosteric inhibition of glycolysis and supporting biomass generation. By comparing two related organisms with vastly different metabolic strategies, our work highlights the versatility and plasticity of central carbon metabolism in eukaryotes, illuminating critical adaptations supporting the preferential use of glycolysis over oxidative phosphorylation.","doi":"10.1016/j.cub.2023.04.046","authors":"Alam S, Gu Y, Reichert P, Bähler J, Oliferenko S","authors_abbrev":"Alam S et al.","pubmed_publication_date":"05 Jun 2023","pubmed_entrez_date":"2023-05-10","publication_year":"2023","canto_session_key":"f38f39f8014a9104","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Snezhana Oliferenko","canto_first_approved_date":"2023-06-19 14:58:28","canto_approved_date":"2024-10-01 07:06:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-05-18 14:33:21","canto_added_date":"2023-05-12 00:15:04","annotation_curators":[{"name":"Snezhana Oliferenko","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1620.08","SPAC6C3.04","SPAC11G7.03","SPCC306.08c","SPAC24C9.06c","SPAC4H3.10c","SPBC947.15c","SPBC3H7.03c","SPCC330.12c","SPAC3A11.07","SPBP4H10.15","SPBC776.15c","SPAC1556.02c","SPBC16H5.06","SPCC18.18c","SPAC16E8.17c","SPAC1B2.04","SPBC215.05"],"gene_count":18,"ltp_gene_count":14,"approved_date":"2023-06-19"},{"uniquename":"PMID:19844703","title":"N- and O-linked oligosaccharides completely lack galactose residues in the gms1och1 mutant of Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2010 Mar;86(1):263-72","abstract":"Unlike their counterparts in budding yeast Saccharomyces cerevisiae, the glycoproteins of Schizosaccharomyces pombe contain, in addition to alpha-D-mannose (Man), a large number of alpha-D-galactose (Gal) residues. In both yeasts, large outer chains are attached to the oligosaccharide cores of glycoproteins during export via Golgi. Formation of the yeast-specific large outer chain is initiated by alpha-1,6-mannosylatransferase encoded by the och1+ gene, the disruption of which blocked outer chain elongation. We previously reported that N-linked oligosaccharide structures of S. pombe och1Delta mutant consisted of Gal(2-6)Man(9)GlcNAc(2) with alpha-linked Gal residues attached to the core oligosaccharide moiety. The disruption of gms1+, a gene encoding the UDP-galactose transporter required for the synthesis of galactomannan, abolished cell surface galactosylation in S. pombe. In this study, we constructed a gms1Deltaoch1Delta double mutant and determined the N- and O-linked oligosaccharide structures present on the cell surface. Oligosaccharides were liberated from glycoproteins by hydrazinolysis and labeled with the fluorophore, 2-aminopyridine. The pyridylaminated N-linked oligosaccharides were analyzed by high-performance liquid chromatography in combination with alpha1,2-mannosidase digestion and partial acetolysis. These analyses revealed that the N-linked oligosaccharides of gms1Deltaoch1Delta cells consisted of alpha1,2-linked Man-extended core oligosaccharides (Man(8-12)GlcNAc2) from which the fission yeast-specific alpha-linked Gal residues were completely absent.","doi":"10.1007/s00253-009-2297-9","authors":"Ohashi T, Takegawa K","authors_abbrev":"Ohashi T et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2009-10-22","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1006.05c","SPCC1795.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:29236736","title":"Functions for fission yeast splicing factors SpSlu7 and SpPrp18 in alternative splice-site choice and stress-specific regulated splicing.","citation":"PLoS One 2017;12(12):e0188159","abstract":"Budding yeast spliceosomal factors ScSlu7 and ScPrp18 interact and mediate intron 3'ss choice during second step pre-mRNA splicing. The fission yeast genome with abundant multi-intronic transcripts, degenerate splice signals and SR proteins is an apt unicellular fungal model to deduce roles for core spliceosomal factors in alternative splice-site choice, intron retention and to study the cellular implications of regulated splicing. From our custom microarray data we deduce a stringent reproducible subset of S. pombe alternative events. We examined the role of factors SpSlu7 or SpPrp18 for these splice events and investigated the relationship to growth phase and stress. Wild-type log and stationary phase cells showed ats1+ exon 3 skipped and intron 3 retained transcripts. Interestingly the non-consensus 5'ss in ats1+ intron 3 caused SpSlu7 and SpPrp18 dependent intron retention. We validated the use of an alternative 5'ss in dtd1+ intron 1 and of an upstream alternative 3'ss in DUF3074 intron 1. The dtd1+ intron 1 non-canonical 5'ss yielded an alternative mRNA whose levels increased in stationary phase. Utilization of dtd1+ intron 1 sub-optimal 5' ss required functional SpPrp18 and SpSlu7 while compromise in SpSlu7 function alone hampered the selection of the DUF3074 intron 1 non canonical 3'ss. We analysed the relative abundance of these splice isoforms during mild thermal, oxidative and heavy metal stress and found stress-specific splice patterns for ats1+ and DUF3074 intron 1 some of which were SpSlu7 and SpPrp18 dependent. By studying ats1+ splice isoforms during compromised transcription elongation rates in wild-type, spslu7-2 and spprp18-5 mutant cells we found dynamic and intron context-specific effects in splice-site choice. Our work thus shows the combinatorial effects of splice site strength, core splicing factor functions and transcription elongation kinetics to dictate alternative splice patterns which in turn serve as an additional recourse of gene regulation in fission yeast.","doi":"10.1371/journal.pone.0188159","authors":"Melangath G, Sen T, Kumar R, Bawa P, Srinivasan S, Vijayraghavan U","authors_abbrev":"Melangath G et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-12-14","publication_year":"2017","canto_session_key":"044936ba4adeb8dc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-12-15 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8529881","title":"Identification of Schizosaccharomyces pombe gene psk1+, encoding a novel putative serine/threonine protein kinase, whose mutation conferred resistance to phenylarsine oxide.","citation":"Gene 1995 Dec 01;166(1):155-9","abstract":"We have identified a novel putative protein kinase-encoding gene from Schizosaccharomyces pombe (Sp), designated psk1+, by using a highly conserved amino acid (aa) sequence motif to design amplification of DNA fragments using PCR. The putative translation product of psk1+ contains 436 aa, with a molecular mass of 49,317 Da. A single psk1+ was identified by genomic Southern blot analysis, and the genomic mapping indicated that psk1+ was localized in Sp chromosome III. Growth of wild-type Sp cells was inhibited by 0.5 microM phenylarsine oxide, a protein tyrosine phosphatase inhibitor, but psk1- cells were relatively resistant to this drug.","authors":"Mukai H, Miyahara M, Takanaga H, Kitagawa M, Shibata H, Shimakawa M, Ono Y","authors_abbrev":"Mukai H et al.","pubmed_publication_date":"01 Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"fafb883b15d2587b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-10-26 13:21:59","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-16 11:49:20","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-16"},{"uniquename":"PMID:12931193","title":"Feedback regulation of MAPK signalling by an RNA-binding protein.","citation":"Nature 2003 Aug 21;424(6951):961-5","abstract":"Mitogen-activated protein kinases (MAPKs) are evolutionarily conserved enzymes that convert extracellular signals into various outputs such as cell growth, differentiation and cell death. MAPK phosphatases selectively inactivate MAPKs by dephosphorylating critical phosphothreonine and phosphotyrosine residues. The transcriptional induction of MAPK phosphatase expression by various stimuli, including MAPK activation, has been well documented as a negative-feedback mechanism of MAPK signalling. Here we show that Rnc1, a novel K-homology-type RNA-binding protein in fission yeast, binds and stabilizes Pmp1 messenger RNA, the MAPK phosphatase for Pmk1 (refs 10, 11). Rnc1 therefore acts as a negative regulator of Pmk1 signalling. Notably, Pmk1 phosphorylates Rnc1, causing enhancement of the RNA-binding activity of Rnc1. Thus, Rnc1 is a component of a new negative-feedback loop that regulates the Pmk1 pathway through its binding to Pmp1 mRNA. Our findings--the post-transcriptional mRNA stabilization of a MAPK phosphatase mediated by an RNA-binding protein--provide an additional regulatory mechanism for fine-tuning of MAPK signalling pathways.","authors":"Sugiura R, Kita A, Shimizu Y, Shuntoh H, Sio SO, Kuno T","authors_abbrev":"Sugiura R et al.","pubmed_publication_date":"21 Aug 2003","pubmed_entrez_date":"2003-08-22","publication_year":"2003","canto_session_key":"747342ebb6e04e9d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-10 12:30:33","canto_approved_date":"2022-02-01 17:49:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-21 13:19:32","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":43,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBP4H10.04","SPBC119.08","SPCC757.09c","SPBC543.07","SPBC1685.01"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-10-10"},{"uniquename":"PMID:21076007","title":"Deconvolution of chromatin immunoprecipitation-microarray (ChIP-chip) analysis of MBF occupancies reveals the temporal recruitment of Rep2 at the MBF target genes.","citation":"Eukaryot Cell 2011 Jan;10(1):130-41","abstract":"MBF (or DSC1) is known to regulate transcription of a set of G(1)/S-phase genes encoding proteins involved in regulation of DNA replication. Previous studies have shown that MBF binds not only the promoter of G(1)/S-phase genes, but also the constitutive genes; however, it was unclear if the MBF bindings at the G(1)/S-phase and constitutive genes were mechanistically distinguishable. Here, we report a chromatin immunoprecipitation-microarray (ChIP-chip) analysis of MBF binding in the Schizosaccharomyces pombe genome using high-resolution genome tiling microarrays. ChIP-chip analysis indicates that the majority of the MBF occupancies are located at the intragenic regions. Deconvolution analysis using Rpb1 ChIP-chip results distinguishes the Cdc10 bindings at the Rpb1-poor loci (promoters) from those at the Rpb1-rich loci (intragenic sequences). Importantly, Res1 binding at the Rpb1-poor loci, but not at the Rpb1-rich loci, is dependent on the Cdc10 function, suggesting a distinct binding mechanism. Most Cdc10 promoter bindings at the Rpb1-poor loci are associated with the G(1)/S-phase genes. While Res1 or Res2 is found at both the Cdc10 promoter and intragenic binding sites, Rep2 appears to be absent at the Cdc10 promoter binding sites but present at the intragenic sites. Time course ChIP-chip analysis demonstrates that Rep2 is temporally accumulated at the coding region of the MBF target genes, resembling the RNAP-II occupancies. Taken together, our results show that deconvolution analysis of Cdc10 occupancies refines the functional subset of genomic binding sites. We propose that the MBF activator Rep2 plays a role in mediating the cell cycle-specific transcription through the recruitment of RNAP-II to the MBF-bound G(1)/S-phase genes.","doi":"10.1128/EC.00218-10","authors":"Eshaghi M, Zhu L, Chu Z, Li J, Chan CS, Shahab A, Karuturi RK, Liu J","authors_abbrev":"Eshaghi M et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-11-16","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28784663","title":"The 19S proteasome is directly involved in the regulation of heterochromatin spreading in fission yeast.","citation":"J Biol Chem 2017 Oct 13;292(41):17144-17155","abstract":"Cumulative evidence suggests that non-proteolytic functions of the proteasome are involved in transcriptional regulation, mRNA export, and ubiquitin-dependent histone modification and thereby modulate the intracellular levels of regulatory proteins implicated in controlling key cellular functions. To date, the non-proteolytic roles of the proteasome have been mainly investigated in euchromatin; their effects on heterochromatin are largely unknown. Here, using fission yeast as a model, we randomly mutagenized the subunits of the 19S proteasome subcomplex and sought to uncover a direct role of the proteasome in heterochromatin regulation. We identified a mutant allele,  rpt4-1 , that disrupts a non-proteolytic function of the proteasome, also known as a non-proteolytic allele. Experiments performed using  rpt4-1  cells revealed that the proteasome is involved in the regulation of heterochromatin spreading to prevent its uncontrolled invasion into neighboring euchromatin regions. Intriguingly, the phenotype of the non-proteolytic  rpt4-1  mutant resembled that of  epe1 Δ cells, which lack the Epe1 protein that counteracts heterochromatin spreading. Both mutants exhibited variegated gene-silencing phenotypes across yeast colonies, spreading of heterochromatin, bypassing of the requirement for RNAi in heterochromatin formation at the outer repeat region ( otr ), and up-regulation of RNA polymerase II. Further analysis revealed Mst2, another factor that antagonizes heterochromatin spreading, may function redundantly with Rpt4. These observations suggest that the 19S proteasome may be involved in modulating the activities of Epe1 and Mst2. In conclusion, our findings indicate that the proteasome appears to have a heterochromatin-regulating function that is independent of its canonical function in proteolysis.","doi":"10.1074/jbc.M117.790824","authors":"Seo HD, Choi Y, Kim M, Kang K, Urano T, Lee D","authors_abbrev":"Seo HD et al.","pubmed_publication_date":"13 Oct 2017","pubmed_entrez_date":"2017-08-09","publication_year":"2017","canto_session_key":"2064950edce427fd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-08-10 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1682.10","SPAC13C5.01c","SPCC16A11.16c","SPBP19A11.03c","SPBC4.07c","SPCC1682.16","SPAC23D3.07","SPAC22F8.06","SPAC4A8.13c","SPAC631.02","SPAC31A2.04c","SPBC17D11.07c","SPBC582.07c","SPAC1420.03","SPBC4C3.10c","SPAC637.10c","SPAC6G10.04c","SPCC576.10c","SPCC63.12c","SPBC119.01","SPCC188.13c","SPCC622.16c","SPCC1442.06","SPAC607.05","SPBC16G5.01","SPAC323.02c","SPBC106.16","SPBC577.10","SPBC13E7.08c","SPCC1795.04c","SPBC342.04","SPAC23G3.11","SPCC736.11","SPAC31G5.13","SPBC16C6.07c"],"gene_count":35,"ltp_gene_count":34},{"uniquename":"PMID:9804804","title":"The high mobility group domain protein Cmb1 of Schizosaccharomyces pombe binds to cytosines in base mismatches and opposite chemically altered guanines.","citation":"J Biol Chem 1998 Nov 13;273(46):30398-405","abstract":"The mismatch-binding activity Cmb1 of Schizosaccharomyces pombe was enriched from wild type cells, and N-terminal sequencing enabled cloning of the respective gene. The deduced amino acid sequence of cmb1(+) contains a high mobility group domain, a motif that is common to a heterogeneous family of DNA-binding proteins. In crude protein extracts of a cmb1 gene-disruption strain, specific binding to C/T, C/A, and C/Delta was abolished. Weak binding to C/C revealed the presence of a second mismatch-binding activity, Cmb2. Cmb1, enriched from S. pombe and purified from Escherichia coli, bound specifically to C/C, C/T, C/A, T/T, and C/Delta but showed little or no affinity to other mismatches and small loops. Cmb1 recognizes 1,2 GpG intrastrand cross-links, produced by the chemotherapeutic drug cisplatin, when two cytosines are opposite the cross-linked guanines but not when other bases are present. Consistently, O6-methylguanine:C but not O6-methylguanine/T lesions were bound. Thus, cytosines in mismatches and opposite chemically modified guanines are the preferred target of Cmb1 recognition. cmb1 mutant cells are more sensitive to cisplatin than wild type cells, indicating a role of Cmb1 in repair of cisplatin-induced DNA damage.","authors":"Fleck O, Kunz C, Rudolph C, Kohli J","authors_abbrev":"Fleck O et al.","pubmed_publication_date":"13 Nov 1998","pubmed_entrez_date":"1998-11-07","publication_year":"1998","canto_session_key":"4696010b81ed78d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-13 15:36:16","canto_approved_date":"2025-02-02 13:33:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-07 13:53:07","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-13"},{"uniquename":"PMID:27560651","title":"The effect of magnesium on mitotic spindle formation in Schizosaccharomyces pombe.","citation":"Genet Mol Biol 2016;39(3):459-64","abstract":"Magnesium (Mg2+), an essential ion for cells and biological systems, is involved in a variety of cellular processes, including the formation and breakdown of microtubules. The results of a previous investigation suggested that as cells grow the intracellular Mg2+ concentration falls, thereby stimulating formation of the mitotic spindle. In the present work, we used a Mg2+-deficient Schizosaccharomyces pombe strain GA2, in which two essential membrane Mg2+ transporter genes (homologs of ALR1 and ALR2 in Saccharomyces cerevisae) were deleted, and its parental strain Sp292, to examine the extent to which low Mg2+ concentrations can affect mitotic spindle formation. The two S. pombe strains were transformed with a plasmid carrying a GFP-α2-tubulin construct to fluorescently label microtubules. Using the free Mg2+-specific fluorescent probe mag-fura-2, we confirmed that intracellular free Mg2+ levels were lower in GA2 than in the parental strain. Defects in interphase microtubule organization, a lower percentage of mitotic spindle formation and a reduced mitotic index were also observed in the GA2 strain. Although there was interphase microtubule polymerization, the lower level of mitotic spindle formation in the Mg2+-deficient strain suggested a greater requirement for Mg2+ in this phenomenon than previously thought.","doi":"10.1590/1678-4685-GMB-2015-0239","authors":"Uz G, Sarikaya AT","authors_abbrev":"Uz G et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-08-26","publication_year":"2016","canto_session_key":"3bd00175a6e61e42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-12-09 10:54:23","canto_approved_date":"2022-05-18 14:10:17","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2016-10-28 09:06:20","canto_added_date":"2016-08-27 00:15:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27B12.12c","SPAC17A2.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-12-09"},{"uniquename":"PMID:25254656","title":"The Vip1 inositol polyphosphate kinase family regulates polarized growth and modulates the microtubule cytoskeleton in fungi.","citation":"PLoS Genet 2014 Sep;10(9):e1004586","abstract":"Microtubules (MTs) are pivotal for numerous eukaryotic processes ranging from cellular morphogenesis, chromosome segregation to intracellular transport. Execution of these tasks requires intricate regulation of MT dynamics. Here, we identify a new regulator of the Schizosaccharomyces pombe MT cytoskeleton: Asp1, a member of the highly conserved Vip1 inositol polyphosphate kinase family. Inositol pyrophosphates generated by Asp1 modulate MT dynamic parameters independent of the central +TIP EB1 and in a dose-dependent and cellular-context-dependent manner. Importantly, our analysis of the in vitro kinase activities of various S. pombe Asp1 variants demonstrated that the C-terminal phosphatase-like domain of the dual domain Vip1 protein negatively affects the inositol pyrophosphate output of the N-terminal kinase domain. These data suggest that the former domain has phosphatase activity. Remarkably, Vip1 regulation of the MT cytoskeleton is a conserved feature, as Vip1-like proteins of the filamentous ascomycete Aspergillus nidulans and the distantly related pathogenic basidiomycete Ustilago maydis also affect the MT cytoskeleton in these organisms. Consistent with the role of interphase MTs in growth zone selection/maintenance, all 3 fungal systems show aspects of aberrant cell morphogenesis. Thus, for the first time we have identified a conserved biological process for inositol pyrophosphates.","doi":"10.1371/journal.pgen.1004586","authors":"Pöhlmann J, Risse C, Seidel C, Pohlmann T, Jakopec V, Walla E, Ramrath P, Takeshita N, Baumann S, Feldbrügge M, Fischer R, Fleig U","authors_abbrev":"Pöhlmann J et al.","pubmed_publication_date":"Sep 2014","pubmed_entrez_date":"2014-09-26","publication_year":"2014","canto_session_key":"893c5c2ae65e3990","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ursula Fleig","canto_first_approved_date":"2019-05-29 14:22:11","canto_approved_date":"2024-01-03 19:24:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-20 13:53:18","canto_added_date":"2014-09-27 00:16:14","annotation_curators":[{"name":"Ursula Fleig","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.06c","SPAC13G6.14","SPAC18G6.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-05-29"},{"uniquename":"PMID:4156516","title":"Cyclid AMP and catabolite repression in yeasts, In Schizosaccharomyces pombe glucose lowers both intracellular adenosine 3':5'-monophosphate levels and the activity of catabolite-sensitive enzymes.","citation":"Eur J Biochem 1974 Nov 01;49(1):305-16","abstract":"","authors":"Schlanderer G, Dellweg H","authors_abbrev":"Schlanderer G et al.","pubmed_publication_date":"01 Nov 1974","pubmed_entrez_date":"1974-11-01","publication_year":"1974","canto_session_key":"14600e58a4c852e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-12-05 19:33:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-05 19:33:16","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-12-05"},{"uniquename":"PMID:17371846","title":"Genome-wide dynamics of SAPHIRE, an essential complex for gene activation and chromatin boundaries.","citation":"Mol Cell Biol 2007 Jun;27(11):4058-69","abstract":"In this study, we characterize a four-protein nucleosome-binding complex from Schizosaccharomyces pombe, termed SAPHIRE, that includes two orthologs of human Lsd1, a histone demethylase. The SAPHIRE complex is essential for cell viability, whereas saphire mutants lacking key conserved catalytic residues are viable but thermosensitive, suggesting that SAPHIRE has both an important enzymatic function and an essential nonenzymatic function. SAPHIRE is present in (or adjacent to) particular heterochromatic loci and also in the transcription start site regions of many highly active polymerase II genes. However, ribosomal protein genes are notably SAPHIRE deficient. SAPHIRE promotes activation, as target genes are selectively attenuated in saphire mutants. Interestingly, saphire mutants display increased histone H3 lysine 4 dimethylation, a modification typically associated with euchromatin. SAPHIRE localization is dynamic, as activated genes rapidly acquire SAPHIRE. Furthermore, saphire mutants dramatically shift a heterochromatin-euchromatin boundary in Chr1, suggesting a novel role in boundary regulation.","authors":"Gordon M, Holt DG, Panigrahi A, Wilhelm BT, Erdjument-Bromage H, Tempst P, Bähler J, Cairns BR","authors_abbrev":"Gordon M et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-03-21","publication_year":"2007","canto_session_key":"ffbb86b907aa5e22","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-06-26 09:10:45","canto_approved_date":"2024-06-26 09:10:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-21 15:19:36","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":35,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.09c","SPCC4G3.07c","SPAC30D11.08c","SPAC23E2.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-06-26"},{"uniquename":"EMBL:AU010350","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9436991","title":"Negative regulation of Cdc18 DNA replication protein by Cdc2.","citation":"Mol Biol Cell 1998 Jan;9(1):63-73","abstract":"Fission yeast Cdc18, a homologue of Cdc6 in budding yeast and metazoans, is periodically expressed during the S phase and required for activation of replication origins. Cdc18 overexpression induces DNA rereplication without mitosis, as does elimination of Cdc2-Cdc13 kinase during G2 phase. These findings suggest that illegitimate activation of origins may be prevented through inhibition of Cdc18 by Cdc2. Consistent with this hypothesis, we report that Cdc18 interacts with Cdc2 in association with Cdc13 and Cig2 B-type cyclins in vivo. Cdc18 is phosphorylated by the associated Cdc2 in vitro. Mutation of a single phosphorylation site, T104A, activates Cdc18 in the rereplication assay. The cdc18-K9 mutation is suppressed by a cig2 mutation, providing genetic evidence that Cdc2-Cig2 kinase inhibits Cdc18. Moreover, constitutive expression of Cig2 prevents rereplication in cells lacking Cdc13. These findings identify Cdc18 as a key target of Cdc2-Cdc13 and Cdc2-Cig2 kinases in the mechanism that limits chromosomal DNA replication to once per cell cycle.","authors":"Lopez-Girona A, Mondesert O, Leatherwood J, Russell P","authors_abbrev":"Lopez-Girona A et al.","pubmed_publication_date":"Jan 1998","pubmed_entrez_date":"1998-03-14","publication_year":"1998","canto_session_key":"48ef5d49bc0230cb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-02-24 15:36:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-14 15:14:46","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4E9.02","SPBC11B10.09","SPBC582.03","SPBC685.09","SPAPB2B4.03","SPBC32F12.09","SPBC14C8.07c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2015-12-14"},{"uniquename":"PMID:10353894","title":"Position effect variegation at the mating-type locus of fission yeast: a cis-acting element inhibits covariegated expression of genes in the silent and expressed domains.","citation":"Genetics 1999 Jun;152(2):495-508","abstract":"Schizosaccharomyces pombe switches its mating type by transposing a copy of unexpressed genes from the respective mat2 or mat3 cassettes to mat1. The donor cassettes are located in a silent domain that is separated from the expressed mat1 cassette by the L region. We monitored the expression of ade6 from sites in the L region and examined the relationship between the expression state at these sites and at sites within the silent domain. Results indicate that: (1) the silent domain extends into the L region, but repression is gradually alleviated with increasing distance from mat2, and overexpression of swi6 enhances PEV in the L region; (2) a transcriptionally active chromatin state, associated with reporter gene expression in the L region, spreads toward the silent domain; (3) a cis-acting element, located at the junction between the L region and mat2-P, ensures repression in the silent domain, regardless of the expression state in the L region; and (4) repression in mat1-P cells is less stringently controlled than in mat1-M cells. We discuss the functional organization of the mat region and genetic elements that ensure separation between repressed and derepressed domains.","authors":"Ayoub N, Goldshmidt I, Cohen A","authors_abbrev":"Ayoub N et al.","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-06-03","publication_year":"1999","canto_session_key":"e5bfc5adba7c836b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-06-15 20:58:26","canto_approved_date":"2024-06-15 20:58:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 15:33:46","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2024-06-15"},{"uniquename":"PMID:30199529","title":"Implications of alternative routes to APC/C inhibition by the mitotic checkpoint complex.","citation":"PLoS Comput Biol 2018 Sep;14(9):e1006449","abstract":"The mitotic checkpoint (also called spindle assembly checkpoint) is a signaling pathway that ensures faithful chromosome segregation. Mitotic checkpoint proteins inhibit the anaphase-promoting complex (APC/C) and its activator Cdc20 to prevent precocious anaphase. Checkpoint signaling leads to a complex of APC/C, Cdc20, and checkpoint proteins, in which the APC/C is inactive. In principle, this final product of the mitotic checkpoint can be obtained via different pathways, whose relevance still needs to be fully ascertained experimentally. Here, we use mathematical models to compare the implications on checkpoint response of the possible pathways leading to APC/C inhibition. We identify a previously unrecognized funneling effect for Cdc20, which favors Cdc20 incorporation into the inhibitory complex and therefore promotes checkpoint activity. Furthermore, we find that the presence or absence of one specific assembly reaction determines whether the checkpoint remains functional at elevated levels of Cdc20, which can occur in cancer cells. Our results reveal the inhibitory logics behind checkpoint activity, predict checkpoint efficiency in perturbed situations, and could inform molecular strategies to treat malignancies that exhibit Cdc20 overexpression.","doi":"10.1371/journal.pcbi.1006449","authors":"Gross F, Bonaiuti P, Hauf S, Ciliberto A","authors_abbrev":"Gross F et al.","pubmed_publication_date":"Sep 2018","pubmed_entrez_date":"2018-09-11","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2019-02-01 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38578823","title":"CDK activity at the centrosome regulates the cell cycle.","citation":"Cell Rep 2024 Apr 04;43(4):114066","abstract":"In human cells and yeast, an intact \"hydrophobic patch\" substrate docking site is needed for mitotic cyclin centrosomal localization. A hydrophobic patch mutant (HPM) of the fission yeast mitotic cyclin Cdc13 cannot enter mitosis, but whether this is due to defective centrosomal localization or defective cyclin-substrate docking more widely is unknown. Here, we show that artificially restoring Cdc13-HPM centrosomal localization promotes mitotic entry and increases CDK (cyclin-dependent kinase) substrate phosphorylation at the centrosome and in the cytoplasm. We also show that the S-phase B-cyclin hydrophobic patch is required for centrosomal localization but not for S phase. We propose that the hydrophobic patch is essential for mitosis due to its requirement for the local concentration of cyclin-CDK with CDK substrates and regulators at the centrosome. Our findings emphasize the central importance of the centrosome as a hub coordinating cell-cycle control and explain why the cyclin hydrophobic patch is essential for mitosis.","doi":"10.1016/j.celrep.2024.114066","authors":"Roberts EL, Greenwood J, Kapadia N, Auchynnikava T, Basu S, Nurse P","authors_abbrev":"Roberts EL et al.","pubmed_publication_date":"04 Apr 2024","pubmed_entrez_date":"2024-04-05","publication_year":"2024","canto_session_key":"123d6b38e02c1faf","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-04-05 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16762840","title":"Swi6/HP1 recruits a JmjC domain protein to facilitate transcription of heterochromatic repeats.","citation":"Mol Cell 2006 Jun 09;22(5):681-92","abstract":"Heterochromatin formation is generally thought to result in transcriptional repression of target loci. However, RNAi-mediated heterochromatin assembly requires RNA polymerase II (Pol II) transcription. The mechanism facilitating Pol II accessibility to heterochromatin is unknown. We show that the fission yeast Epe1, a JmjC domain-containing protein and a negative regulator of heterochromatin, is distributed across all major heterochromatic domains and at certain meiotic genes. Remarkably, Epe1 is recruited to heterochromatic loci by the heterochromatin protein Swi6/HP1. Moreover, Epe1 acts in a heterochromatin-specific context to promote Pol II accessibility by counteracting repressive chromatin. This requires Epe1's JmjC domain, although the mechanism utilized might be distinct from other JmjC proteins that possess known demethylase activities. We also find that Epe1 is preferentially recruited to inverted repeats flanking centromeres to restrain the spread of pericentromeric heterochromatin. Our analyses suggest that Swi6/HP1 recruits opposing chromatin-modifying activities, the balancing of which is crucial for heterochromatin maintenance.","authors":"Zofall M, Grewal SI","authors_abbrev":"Zofall M et al.","pubmed_publication_date":"09 Jun 2006","pubmed_entrez_date":"2006-06-10","publication_year":"2006","canto_session_key":"5a546d70bc11f7b5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-25 12:37:26","canto_approved_date":"2024-01-25 12:37:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-17 17:07:25","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPCC736.11","SPCC330.05c","SPCC794.12c","SPCC622.16c","SPAC3H8.10","SPBC428.08c","SPNCRNA.84","SPBC24C6.09c","SPBC32H8.11","SPAPB8E5.03","SPNCRNA.95","SPCC18B5.01c","SPBC28F2.12","SPBC800.03","SPAC27D7.13c","SPAC13A11.03"],"gene_count":17,"ltp_gene_count":5,"approved_date":"2024-01-25"},{"uniquename":"PMID:19056896","title":"The S. pombe SAGA complex controls the switch from proliferation to sexual differentiation through the opposing roles of its subunits Gcn5 and Spt8.","citation":"Genes Dev 2008 Nov 15;22(22):3184-95","abstract":"The SAGA complex is a conserved multifunctional coactivator known to play broad roles in eukaryotic transcription. To gain new insights into its functions, we performed biochemical and genetic analyses of SAGA in the fission yeast, Schizosaccharomyces pombe. Purification of the S. pombe SAGA complex showed that its subunit composition is identical to that of Saccharomyces cerevisiae. Analysis of S. pombe SAGA mutants revealed that SAGA has two opposing roles regulating sexual differentiation. First, in nutrient-rich conditions, the SAGA histone acetyltransferase Gcn5 represses ste11(+), which encodes the master regulator of the mating pathway. In contrast, the SAGA subunit Spt8 is required for the induction of ste11(+) upon nutrient starvation. Chromatin immunoprecipitation experiments suggest that these regulatory effects are direct, as SAGA is physically associated with the ste11(+) promoter independent of nutrient levels. Genetic tests suggest that nutrient levels do cause a switch in SAGA function, as spt8Delta suppresses gcn5Delta with respect to ste11(+) derepression in rich medium, whereas the opposite relationship, gcn5Delta suppression of spt8Delta, occurs during starvation. Thus, SAGA plays distinct roles in the control of the switch from proliferation to differentiation in S. pombe through the dynamic and opposing activities of Gcn5 and Spt8.","doi":"10.1101/gad.1719908","authors":"Helmlinger D, Marguerat S, Villén J, Gygi SP, Bähler J, Winston F","authors_abbrev":"Helmlinger D et al.","pubmed_publication_date":"15 Nov 2008","pubmed_entrez_date":"2008-12-06","publication_year":"2008","canto_session_key":"fc9305f756e323a2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 19:46:52","canto_approved_date":"2026-04-08 10:57:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-08-28 13:03:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":73,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP16F5.03c","SPCC16C4.18c","SPAC4D7.10c","SPCC126.04c","SPBC25H2.11c","SPBC1921.07c","SPBC887.18c","SPAC12G12.05c","SPAC15A10.02","SPAC1952.05","SPCC5E4.03c","SPCC61.02","SPBC21H7.02","SPBC28F2.10c","SPAC6F12.02","SPBC14C8.17c","SPAC57A10.14","SPAC27D7.03c","SPCC24B10.08c","SPBC32C12.02","SPBC6B1.12c","SPAC13A11.04c"],"gene_count":22,"ltp_gene_count":21,"approved_date":"2019-01-30"},{"uniquename":"PMID:15218150","title":"RNAi-independent heterochromatin nucleation by the stress-activated ATF/CREB family proteins.","citation":"Science 2004 Jun 25;304(5679):1971-6","abstract":"At the silent mating-type interval of fission yeast, the RNA interference (RNAi) machinery cooperates with cenH, a DNA element homologous to centromeric repeats, to initiate heterochromatin formation. However, in RNAi mutants, heterochromatin assembly can still occur at low efficiency. Here, we report that Atf1 and Pcr1, two ATF/CREB family proteins, act in a parallel mechanism to the RNAi pathway for heterochromatin nucleation. Deletion of atf1 or pcr1 alone has little effect on silencing at the mating-type region, but when combined with RNAi mutants, double mutants fail to nucleate heterochromatin assembly. Moreover, deletion of atf1 or pcr1 in combination with cenH deletion causes loss of silencing and heterochromatin formation. Furthermore, Atf1 and Pcr1 bind to the mating-type region and target histone H3 lysine-9 methylation and the Swi6 protein essential for heterochromatin assembly. These analyses link ATF/CREB family proteins, involved in cellular response to environmental stresses, to nucleation of constitutive heterochromatin.","authors":"Jia S, Noma K, Grewal SI","authors_abbrev":"Jia S et al.","pubmed_publication_date":"25 Jun 2004","pubmed_entrez_date":"2004-06-26","publication_year":"2004","canto_session_key":"aed076cba91d48c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-09 06:58:46","canto_approved_date":"2024-10-01 06:28:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-02 13:30:08","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":74,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPCC188.13c","SPAC6F12.09","SPAC664.01c","SPBC428.08c","SPAC21E11.03c","SPCC736.11"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2024-05-09"},{"uniquename":"PMID:18276645","title":"Oxygen-dependent, alternative promoter controls translation of tco1+ in fission yeast.","citation":"Nucleic Acids Res 2008 Apr;36(6):2024-31","abstract":"Eukaryotic cells respond to changes in environmental oxygen supply by increasing transcription and subsequent translation of gene products required for adaptation to low oxygen. In fission yeast, the ortholog of mammalian sterol regulatory element binding protein (SREBP), called Sre1, activates low-oxygen gene expression and is essential for anaerobic growth. Previous studies in multiple organisms indicate that SREBP transcription factors function as positive regulators of gene expression by increasing transcription. Here, we describe a unique mechanism by which activation of Sre1-dependent transcription downregulates protein expression under low oxygen. Paradoxically, Sre1 inhibits expression of tco1(+) gene product by activating its transcription. Under low oxygen, Sre1 directs transcription of tco1(+) from an alternate, upstream promoter and inhibits expression of the normoxic tco1(+) transcript. The resulting low-oxygen transcript contains an additional 751 nt in the 5' untranslated region that is predicted to form a stable, complex secondary structure. Interestingly, polysome profile experiments revealed that this new longer transcript is translationally silent, leading to a decrease in Tco1 protein expression under low oxygen. Together, these results describe a new mechanism for oxygen-dependent control of gene expression and provide an example of negative regulation of protein expression by an SREBP homolog.","doi":"10.1093/nar/gkn027","authors":"Sehgal A, Hughes BT, Espenshade PJ","authors_abbrev":"Sehgal A et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-02-16","publication_year":"2008","canto_session_key":"fd7d19b1aed14f7c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-09-30 09:13:16","canto_approved_date":"2024-03-29 12:57:39","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-09-30 09:13:07","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.09","SPAC17G6.02c","SPNCRNA.600"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2020-09-30"},{"uniquename":"PMID:8223594","title":"Identification of a 100-kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe.","citation":"Eur J Biochem 1993 Oct 15;217(2):501-7","abstract":"Ribonuclease P from the fission yeast Schizosaccharomyces pombe has been purified to apparent homogeneity. A purification of 23,000-fold was achieved by four fractionation steps with DEAE-cellulose chromatography, phosphocellulose chromatography, glycerol-gradient fractionation and finally tRNA-affinity chromatography. A 100-kDa protein was present in the most pure preparations in amounts approximately stoichiometric with the previously identified RNA components of the enzyme, K1-RNA and K2-RNA [Krupp, G., Cherayil, B., Frendeway, D., Nishikawa, S. & Söll, D. (1986) EMBO J. 5, 1697-1703]. A cross-linking experiment utilizing a 4-thiouridine-substituted precursor tRNA demonstrated that the 100-kDa protein interacts with the ribonuclease P substrate in a specific fashion. We therefore conclude that the protein component of S. pombe ribonuclease P is a 100-kDa protein.","authors":"Zimmerly S, Drainas D, Sylvers LA, Söll D","authors_abbrev":"Zimmerly S et al.","pubmed_publication_date":"15 Oct 1993","pubmed_entrez_date":"1993-10-15","publication_year":"1993","canto_session_key":"4c4585dd12eaea94","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-09-17 13:56:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-20 14:43:43","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.16","SPNCRNA.128"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-20"},{"uniquename":"PMID:13678610","title":"Cell polarity: a new mod(e) of anchoring.","citation":"Curr Biol 2003 Sep 16;13(18):R711-3","abstract":"Microtubules play a central role in the establishment of cell polarity by directing the transport of polarity determinants to their site of action. Recent work has revealed a novel membrane-anchoring mechanism which complements the microtubule transport of the fission yeast polarity determinant tea1p to ensure its retention at the cell tip.","authors":"Martin SG, Chang F","authors_abbrev":"Martin SG et al.","pubmed_publication_date":"16 Sep 2003","pubmed_entrez_date":"2003-09-19","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37990966","title":"Chemogenetic Manipulation of Endogenous Proteins in Fission Yeast Using a Self-Localizing Ligand-Induced Protein Translocation System.","citation":"ACS Chem Biol 2023 Dec 15;18(12):2506-2515","abstract":"Cells sense extracellular stimuli through membrane receptors and process information through an intracellular signaling network. Protein translocation triggers intracellular signaling, and techniques such as chemically induced dimerization (CID) have been used to manipulate signaling pathways by altering the subcellular localization of signaling molecules. However, in the fission yeast  Schizosaccharomyces pombe , the commonly used FKBP-FRB system has technical limitations, and therefore, perturbation tools with low cytotoxicity and high temporal resolution are needed. We here applied our recently developed self-localizing ligand-induced protein translocation (SLIPT) system to  S. pombe  and successfully perturbed several cell cycle-related proteins. The SLIPT system utilizes self-localizing ligands to recruit binding partners to specific subcellular compartments such as the plasma membrane or nucleus. We optimized the self-localizing ligands to maintain the long-term recruitment of target molecules to the plasma membrane. By knocking in genes encoding the binding partners for self-localizing ligands, we observed changes in the localization of several endogenous molecules and found perturbations in the cell cycle and associated phenotypes. This study demonstrates the effectiveness of the SLIPT system as a chemogenetic tool for rapid perturbation of endogenous molecules in  S. pombe , providing a valuable approach for studying intracellular signaling and cell cycle regulation with an improved temporal resolution.","doi":"10.1021/acschembio.3c00478","authors":"Nakamura A, Goto Y, Sugiyama H, Tsukiji S, Aoki K","authors_abbrev":"Nakamura A et al.","pubmed_publication_date":"15 Dec 2023","pubmed_entrez_date":"2023-11-22","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-11-23 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10766226","title":"Cell cycle. A new check on issuing the licence.","citation":"Nature 2000 Apr 06;404(6778):560-1","abstract":"","authors":"Blow JJ, Tada S","authors_abbrev":"Blow JJ et al.","pubmed_publication_date":"06 Apr 2000","pubmed_entrez_date":"2000-04-15","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27923119","title":"Interphase Positioning of Centromeres Sets Up Spindle Assembly.","citation":"Dev Cell 2016 Dec 05;39(5):527-528","abstract":"It has been known for many years that centromeres cluster at the spindle pole body in fission yeast. In this issue of Developmental Cell, Fernández-Álvarez et al. (2016) reveal that the functional significance of clustering is to promote spindle assembly by modulating nuclear envelope integrity at the onset of mitosis.","doi":"10.1016/j.devcel.2016.11.014","authors":"Funabiki H","authors_abbrev":"Funabiki H","pubmed_publication_date":"05 Dec 2016","pubmed_entrez_date":"2016-12-07","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-12-08 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1534406","title":"The Schizosaccharomyces pombe rhp3+ gene required for DNA repair and cell viability is functionally interchangeable with the RAD3 gene of Saccharomyces cerevisiae.","citation":"Nucleic Acids Res 1992 May 11;20(9):2327-34","abstract":"The RAD3 gene of Saccharomyces cerevisiae is required for excision repair and is essential for cell viability. RAD3 encoded protein possesses a single stranded DNA-dependent ATPase and DNA and DNA.RNA helicase activities. Mutational studies have indicated a requirement for the RAD3 helicase activities in excision repair. To examine the extent of conservation of structure and function of RAD3 during eukaryotic evolution, we have cloned the RAD3 homolog, rhp3+, from the distantly related yeast Schizosaccharomyces pombe. RAD3 and rhp3+ encoded proteins are highly similar, sharing 67% identical amino acids. We show that like RAD3, rhp3+ is indispensable for excision repair and cell viability, and our studies indicate a requirement of the putative rhp3+ DNA helicase activity in DNA repair. We find that the RAD3 and rhp3+ genes can functionally substitute for one another. The level of complementation provided by the rhp3+ gene in S.cerevisiae rad3 mutants or by the RAD3 gene in S.pombe rhp3 mutants is remarkable in that both the excision repair and viability defects in both yeasts are restored to wild type levels. These observations suggest a parallel evolutionary conservation of other protein components with which RAD3 interacts in mediating its DNA repair and viability functions.","authors":"Reynolds PR, Biggar S, Prakash L, Prakash S","authors_abbrev":"Reynolds PR et al.","pubmed_publication_date":"11 May 1992","pubmed_entrez_date":"1992-05-11","publication_year":"1992","canto_session_key":"a13c28b0b31f2f04","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-20 16:23:26","canto_approved_date":"2021-04-16 13:31:33","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-12-27 02:46:41","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-20"},{"uniquename":"PMID:8736869","title":"Maturation of Krp1, an endopeptidase from the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1996 May;24(2):211S","abstract":"","authors":"Powner D, Davey J","authors_abbrev":"Powner D et al.","pubmed_publication_date":"May 1996","pubmed_entrez_date":"1996-05-01","publication_year":"1996","canto_session_key":"14f96251db4cbe9b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-01-22 17:32:17","canto_approved_date":"2020-01-22 17:32:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2020-01-22 17:32:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-01-22"},{"uniquename":"PMID:18216844","title":"Genomics: fighting fire with fire.","citation":"Nature 2008 Jan 24;451(7177):412-3","abstract":"","doi":"10.1038/451412a","authors":"Voytas DF","authors_abbrev":"Voytas DF","pubmed_publication_date":"24 Jan 2008","pubmed_entrez_date":"2008-01-25","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19054771","title":"A common highly conserved cadmium detoxification mechanism from bacteria to humans: heavy metal tolerance conferred by the ATP-binding cassette (ABC) transporter SpHMT1 requires glutathione but not metal-chelating phytochelatin peptides.","citation":"J Biol Chem 2009 Feb 20;284(8):4936-43","abstract":"Cadmium poses a significant threat to human health due to its toxicity. In mammals and in bakers' yeast, cadmium is detoxified by ATP-binding cassette transporters after conjugation to glutathione. In fission yeast, phytochelatins constitute the co-substrate with cadmium for the transporter SpHMT1. In plants, a detoxification mechanism similar to the one in fission yeast is supposed, but the molecular nature of the transporter is still lacking. To investigate further the relationship between SpHMT1 and its co-substrate, we overexpressed the transporter in a Schizosaccharomyces pombe strain deleted for the phytochelatin synthase gene and heterologously in Saccharomyces cerevisiae and in Escherichia coli. In all organisms, overexpression of SpHMT1 conferred a markedly enhanced tolerance to cadmium but not to Sb(III), AgNO(3), As(III), As(V), CuSO(4), or HgCl(2). Abolishment of the catalytic activity by expression of SpHMT1(K623M) mutant suppressed the cadmium tolerance phenotype independently of the presence of phytochelatins. Depletion of the glutathione pool inhibited the SpHMT1 activity but not that of AtHMA4, a P-type ATPase, indicating that GSH is necessary for the SpHMT1-mediated cadmium resistance. In E. coli, SpHMT1 was targeted to the periplasmic membrane and led to an increased amount of cadmium in the periplasm. These results demonstrate that SpHMT1 confers cadmium tolerance in the absence of phytochelatins but depending on the presence of GSH and ATP. Our results challenge the dogma of the two separate cadmium detoxification pathways and demonstrate that a common highly conserved mechanism has been selected during the evolution from bacteria to humans.","doi":"10.1074/jbc.M808130200","authors":"Prévéral S, Gayet L, Moldes C, Hoffmann J, Mounicou S, Gruet A, Reynaud F, Lobinski R, Verbavatz JM, Vavasseur A, Forestier C","authors_abbrev":"Prévéral S et al.","pubmed_publication_date":"20 Feb 2009","pubmed_entrez_date":"2008-12-05","publication_year":"2009","canto_session_key":"5174d555951bc95c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-21 13:16:11","canto_approved_date":"2022-02-02 11:45:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-28 16:02:59","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H1.10","SPCC737.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-10-21"},{"uniquename":"PMID:2038306","title":"Expression of a dominant negative allele of cdc2 prevents activation of the endogenous p34cdc2 kinase.","citation":"Mol Gen Genet 1991 May;226(3):432-40","abstract":"The cdc2 gene of the fission yeast Schizosaccharomyces pombe encodes a 34 kDa phosphoprotein with serine/threonine protein kinase activity that acts as the key component in regulation of the eukaryotic cell cycle. We used a repressible promoter fused to the cdc2 cDNA to isolate conditionally dominant negative mutants of cdc2. One of these mutants, DL5, is described in this paper. Overexpression of the mutant protein in a wild-type cdc2 background is lethal and confers cell cycle arrest with a typical cdc- phenotype. Sequencing of the mutant cdc2 gene revealed a single amino acid substitution in a region highly conserved in cdc2-like proteins. The mutant protein exhibits no protein kinase activity, but is able to bind a component(s) required for an active protein kinase complex and thereby prevents binding of this component(s) to the co-existing wild-type cdc2 protein. We also demonstrate that S. pombe p34cdc2 contains no phosphoserine.","authors":"Fleig UN, Nurse P","authors_abbrev":"Fleig UN et al.","pubmed_publication_date":"May 1991","pubmed_entrez_date":"1991-05-01","publication_year":"1991","canto_session_key":"1ff973d4c300af54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_approved_date":"2018-03-26 12:56:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-28 16:09:50","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":17,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-09-28"},{"uniquename":"PMID:15094387","title":"The fission yeast ptr1+ gene involved in nuclear mRNA export encodes a putative ubiquitin ligase.","citation":"Biochem Biophys Res Commun 2004 May 14;317(4):1138-43","abstract":"Fission yeast ptr1-1 is one of the mRNA transport mutants that accumulate poly(A)+ RNA in the nuclei at the nonpermissive temperature. We found that the ptr1+ gene encodes a homolog of Saccharomyces cerevisiae Tom1p, a hect type ubiquitin ligase. In ptr1-1, a conserved amino acid in the hect domain of Ptr1p is mutated. The ptr1+ gene is essential for growth and its mutation did not affect nuclear protein export. A ptr1-1 rae1-167 double mutant showed a synthetic effect on a growth defect, indicating that Ptr1p functionally interacts with an essential mRNA export factor Rae1p. We also isolated a multi-copy suppressor for ptr1-1 and found that it is the mpd2+ gene isolated as a multi-copy suppressor of cdc7-PD1.","authors":"Andoh T, Azad AK, Shigematsu A, Ohshima Y, Tani T","authors_abbrev":"Andoh T et al.","pubmed_publication_date":"14 May 2004","pubmed_entrez_date":"2004-04-20","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.05c","SPAC4F10.13c","SPAC19D5.04"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:12121616","title":"A CDK-activating kinase network is required in cell cycle control and transcription in fission yeast.","citation":"Curr Biol 2002 Jul 09;12(13):1100-5","abstract":"Cyclin-dependent kinases (CDKs) involved in cell cycle control require activation by phosphorylation, but CDK-activating kinase (CAK) has diverged between metazoans and budding yeast. Fission yeast has two CAKs: the essential Mcs6 complex, homologous to the metazoan CDK7 complex implicated in cell cycle control and transcription; and Csk1, a nonessential ortholog of budding yeast Cak1. Both can activate the major CDK, Cdc2, but Csk1 can also activate Mcs6, so it was unclear whether the pathway is a linear cascade or a network. Here, we show that a mutation, mcs6-13, which selectively abrogates CDK activation, blocks both G1/S and G2/M transitions, but only when csk1(+) is absent. In contrast, gradual depletion or rapid inactivation of Mcs6 in csk1(+) cells causes cell separation defects or growth arrest, respectively, accompanied by decreased phosphorylation of RNA polymerase II (RNAP II), but not of Cdc2. Finally, neither cell cycle arrest nor CAK failure is recapitulated by a second mutation in mcs6-13 that prevents Mcs6 activation by Csk1, indicating that Csk1 activates Cdc2 directly in vivo. Thus, Mcs6 acts in concert with Csk1 to activate Cdc2 and independently to support transcription and facilitate cell separation. Csk1 likewise has multiple physiologic targets, including Mcs6 and Cdc2.","authors":"Saiz JE, Fisher RP","authors_abbrev":"Saiz JE et al.","pubmed_publication_date":"09 Jul 2002","pubmed_entrez_date":"2002-07-18","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1D4.06c","SPBC19F8.07"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:26432170","title":"Distinct biological activity of threonine monophosphorylated MAPK isoforms during the stress response in fission yeast.","citation":"Cell Signal 2015 Dec;27(12):2534-42","abstract":"Mitogen-activated protein kinases (MAPKs) define a specific group of eukaryotic protein kinases which regulate a number of cellular functions by transducing extracellular signals to intracellular responses. Unlike other protein kinases, catalytic activation of MAPKs by MAPKKs depends on dual phosphorylation at two tyrosine and threonine residues within the conserved TXY motif, and this has been proposed to occur in an ordered fashion, where the initial phosphorylation on tyrosine is followed by phosphorylation at the threonine residue. However, monophosphorylated MAPKs also exist in vivo, and although threonine phosphorylated isoforms retain some catalytic activity, their functional significance remains to be further elucidated. In the fission yeast Schizosaccharomyces pombe MAPKs Sty1 and Pmk1 control multiple aspects of fission yeast life cycle, including morphogenesis, cell cycle, and cellular response to a variety of stressful situations. In this work we show that a trapping mechanism increases MAPKK binding and tyrosine phosphorylation of both Sty1 and Pmk1 when subsequent phosphorylation at threonine is hampered, indicating that a sequential and likely processive mechanism might be responsible for MAPK activation in this simple organism. Whereas threonine-monophosphorylated Sty1 showed a limited biological activity particularly at the transcriptional level, threonine-monophosphorylated Pmk1 was able to execute most of the biological functions of the dually phosphorylated kinase. Thus, threonine monophosphorylated MAPKs might display distinct functional relevance among eukaryotes.","doi":"10.1016/j.cellsig.2015.09.017","authors":"Vázquez B, Soto T, del Dedo JE, Franco A, Vicente J, Hidalgo E, Gacto M, Cansado J, Madrid M","authors_abbrev":"Vázquez B et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-10-04","publication_year":"2015","canto_session_key":"6e672f9c7d609994","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-10-05 00:18:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC119.08","SPAC24B11.06c","SPBC409.07c","SPBC543.07"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"EMBL:SPD146","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27473316","title":"Characterization of a Novel MMS-Sensitive Allele of Schizosaccharomyces pombe mcm4.","citation":"G3 (Bethesda) 2016 Oct 13;6(10):3049-3063","abstract":"The minichromosome maintenance (MCM) complex is the conserved helicase motor of the eukaryotic replication fork. Mutations in the Mcm4 subunit are associated with replication stress and double strand breaks in multiple systems. In this work, we characterize a new temperature-sensitive allele of Schizosaccharomyces pombe mcm4 +  Uniquely among known mcm4 alleles, this mutation causes sensitivity to the alkylation damaging agent methyl methanesulfonate (MMS). Even in the absence of treatment or temperature shift, mcm4-c106 cells show increased repair foci of RPA and Rad52, and require the damage checkpoint for viability, indicating genome stress. The mcm4-c106 mutant is synthetically lethal with mutations disrupting fork protection complex (FPC) proteins Swi1 and Swi3. Surprisingly, we found that the deletion of rif1 +  suppressed the MMS-sensitive phenotype without affecting temperature sensitivity. Together, these data suggest that mcm4-c106 destabilizes replisome structure.","doi":"10.1534/g3.116.033571","authors":"Ranatunga NS, Forsburg SL","authors_abbrev":"Ranatunga NS et al.","pubmed_publication_date":"13 Oct 2016","pubmed_entrez_date":"2016-07-31","publication_year":"2016","canto_session_key":"37bb638001aa60fe","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-08-01 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05","SPAPB1E7.02c","SPCC338.05c","SPAC3G6.11","SPCC553.07c","SPAC6F6.17","SPBC30D10.04","SPAC1556.01c","SPBC776.12c","SPCC1259.13","SPBC16D10.09","SPAC688.10","SPBC16A3.11","SPAC694.06c","SPCC16A11.17","SPBC1347.01c","SPAC11E3.04c","SPBC336.04","SPBC216.06c","SPCC4G3.05c","SPCC550.13","SPAC13G6.01c"],"gene_count":22,"ltp_gene_count":22},{"uniquename":"PMID:18366437","title":"Rad3 and Sty1 function in Schizosaccharomyces pombe: an integrated response to DNA damage and environmental stress?","citation":"Mol Microbiol 2008 Apr;68(2):246-54","abstract":"In Schizosaccharomyces pombe, the Ataxia Telangiectasia-mutated (Atm)/Atm and Rad 3 Related (Atr) homologue Rad3 is an essential regulator of the response to DNA damage and stalled replication forks. Rad3 activates the downstream kinases Chk1 and Cds1. These kinases in turn inhibit cell cycle progression by mediating Cdc2 phosphorylation. Studies in both yeast and mammalian cells suggest additional roles for Rad3 in regulating cellular responses to environmental stress. In S. pombe, cellular responses to various environmental stresses are regulated primarily through the stress-activated MAP kinase p38 homologue Sty1. An important function of Sty1 is to drive cells rapidly through mitosis by facilitating the accumulation of Cdc25. Interestingly, Sty1 is activated simultaneously with Rad3 following exposure to UV radiation or ionizing radiation (IR). Similarly, exposure to environmental stresses induces the expression of rad3(+), cds1(+) and other checkpoint regulator genes. It is currently unclear how the pathways regulated by Sty1 and Rad3 and their opposing effects on mitosis are integrated. Recent studies suggest that Sty1 and Rad3 function together to regulate the expression of several stress response genes following exposure to IR. In this review, we discuss current knowledge on the interaction of Rad3/Atm and Sty1/p38 in regulating cellular responses to environmental stress and DNA damage.","doi":"10.1111/j.1365-2958.2008.06147.x","authors":"Alao JP, Sunnerhagen P","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-03-28","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7700230","title":"DNA polymerase delta is required for the replication feedback control of cell cycle progression in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1995 Mar 10;246(5):561-9","abstract":"DNA replication and DNA repair are essential cell cycle steps ensuring correct transmission of the genome. The feedback replication control system links mitosis to completion of DNA replication and partially overlaps the radiation checkpoint control. Deletion of the chk1/rad27 gene abolishes the radiation but not the replication feedback control. Thermosensitive mutations in the DNA polymerase delta, cdc18 or cdc20 genes lead cells to arrest in the S phase of the cell cycle. We show that strains carrying any of these mutations enter lethal mitosis in the absence of the radiation checkpoint chk1/rad27. We interpret these data as an indication that an assembled replisome is essential for replication dependent control of mitosis and we propose that the arrest of the cell cycle in the thermosensitive mutants is due to the chk1+/rad27+ pathway, which monitors directly DNA for signs of damage.","authors":"Francesconi S, De Recondo AM, Baldacci G","authors_abbrev":"Francesconi S et al.","pubmed_publication_date":"10 Mar 1995","pubmed_entrez_date":"1995-03-10","publication_year":"1995","canto_session_key":"a5fe0a4e622f51f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-08-18 16:08:56","canto_approved_date":"2026-01-30 14:11:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-28 14:39:47","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPCC1259.13","SPBC336.04","SPBC14C8.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-08-18"},{"uniquename":"PMID:19686603","title":"Functional mapping of the fission yeast DNA polymerase delta B-subunit Cdc1 by site-directed and random pentapeptide insertion mutagenesis.","citation":"BMC Mol Biol 2009 Aug 17;10:82","abstract":"DNA polymerase delta plays an essential role in chromosomal DNA replication in eukaryotic cells, being responsible for synthesising the bulk of the lagging strand. In fission yeast, Pol delta is a heterotetrameric enzyme comprising four evolutionarily well-conserved proteins: the catalytic subunit Pol3 and three smaller subunits Cdc1, Cdc27 and Cdm1. Pol3 binds directly to the B-subunit, Cdc1, which in turn binds the C-subunit, Cdc27. Human Pol delta comprises the same four subunits, and the crystal structure was recently reported of a complex of human p50 and the N-terminal domain of p66, the human orthologues of Cdc1 and Cdc27, respectively.\nTo gain insights into the structure and function of Cdc1, random and directed mutagenesis techniques were used to create a collection of thirty alleles encoding mutant Cdc1 proteins. Each allele was tested for function in fission yeast and for binding of the altered protein to Pol3 and Cdc27 using the two-hybrid system. Additionally, the locations of the amino acid changes in each protein were mapped onto the three-dimensional structure of human p50. The results obtained from these studies identify amino acid residues and regions within the Cdc1 protein that are essential for interaction with Pol3 and Cdc27 and for in vivo function. Mutations specifically defective in Pol3-Cdc1 interactions allow the identification of a possible Pol3 binding surface on Cdc1.\nIn the absence of a three-dimensional structure of the entire Pol delta complex, the results of this study highlight regions in Cdc1 that are vital for protein function in vivo and provide valuable clues to possible protein-protein interaction surfaces on the Cdc1 protein that will be important targets for further study.","doi":"10.1186/1471-2199-10-82","authors":"Sanchez Garcia J, Baranovskiy AG, Knatko EV, Gray FC, Tahirov TH, MacNeill SA","authors_abbrev":"Sanchez Garcia J et al.","pubmed_publication_date":"17 Aug 2009","pubmed_entrez_date":"2009-08-19","publication_year":"2009","canto_session_key":"82c72ac61a6cf9b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-26 11:10:05","canto_approved_date":"2022-12-12 15:10:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-06-04 15:50:24","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":129,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.02c","SPAC27E2.05","SPBC336.04"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-10-26"},{"uniquename":"PMID:32681306","title":"Comparing the utility of in vivo transposon mutagenesis approaches in yeast species to infer gene essentiality.","citation":"Curr Genet 2020 Dec;66(6):1117-1134","abstract":"In vivo transposon mutagenesis, coupled with deep sequencing, enables large-scale genome-wide mutant screens for genes essential in different growth conditions. We analyzed six large-scale studies performed on haploid strains of three yeast species (Saccharomyces cerevisiae, Schizosaccaromyces pombe, and Candida albicans), each mutagenized with two of three different heterologous transposons (AcDs, Hermes, and PiggyBac). Using a machine-learning approach, we evaluated the ability of the data to predict gene essentiality. Important data features included sufficient numbers and distribution of independent insertion events. All transposons showed some bias in insertion site preference because of jackpot events, and preferences for specific insertion sequences and short-distance vs long-distance insertions. For PiggyBac, a stringent target sequence limited the ability to predict essentiality in genes with few or no target sequences. The machine learning approach also robustly predicted gene function in less well-studied species by leveraging cross-species orthologs. Finally, comparisons of isogenic diploid versus haploid S. cerevisiae isolates identified several genes that are haplo-insufficient, while most essential genes, as expected, were recessive. We provide recommendations for the choice of transposons and the inference of gene essentiality in genome-wide studies of eukaryotic haploid microbes such as yeasts, including species that have been less amenable to classical genetic studies.","doi":"10.1007/s00294-020-01096-6","authors":"Levitan A, Gale AN, Dallon EK, Kozan DW, Cunningham KW, Sharan R, Berman J","authors_abbrev":"Levitan A et al.","pubmed_publication_date":"Dec 2020","pubmed_entrez_date":"2020-07-19","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-07-20 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000061","title":"Representation of a molecular function involved in a biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing molecular function involved in other biological processes. The underlying equivalence axiom template is \"P and 'part_of' some W\", where P is a molecular function and W is a biological processes.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19500597","title":"Investigating the two-moment characterisation of subcellular biochemical networks.","citation":"J Theor Biol 2009 Oct 07;260(3):340-52","abstract":"While ordinary differential equations (ODEs) form the conceptual framework for modelling many cellular processes, specific situations demand stochastic models to capture the influence of noise. The most common formulation of stochastic models for biochemical networks is the chemical master equation (CME). While stochastic simulations are a practical way to realise the CME, analytical approximations offer more insight into the influence of noise. Towards that end, the two-moment approximation (2MA) is a promising addition to the established analytical approaches including the chemical Langevin equation (CLE) and the related linear noise approximation (LNA). The 2MA approach directly tracks the mean and (co)variance which are coupled in general. This coupling is not obvious in CME and CLE and ignored by LNA and conventional ODE models. We extend previous derivations of 2MA by allowing (a) non-elementary reactions and (b) relative concentrations. Often, several elementary reactions are approximated by a single step. Furthermore, practical situations often require the use of relative concentrations. We investigate the applicability of the 2MA approach to the well-established fission yeast cell cycle model. Our analytical model reproduces the clustering of cycle times observed in experiments. This is explained through multiple resettings of M-phase promoting factor (MPF), caused by the coupling between mean and (co)variance, near the G2/M transition.","doi":"10.1016/j.jtbi.2009.05.022","authors":"Ullah M, Wolkenhauer O","authors_abbrev":"Ullah M et al.","pubmed_publication_date":"07 Oct 2009","pubmed_entrez_date":"2009-06-09","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20661445","title":"Rad3 decorates critical chromosomal domains with gammaH2A to protect genome integrity during S-Phase in fission yeast.","citation":"PLoS Genet 2010 Jul 22;6(7):e1001032","abstract":"Schizosaccharomyces pombe Rad3 checkpoint kinase and its human ortholog ATR are essential for maintaining genome integrity in cells treated with genotoxins that damage DNA or arrest replication forks. Rad3 and ATR also function during unperturbed growth, although the events triggering their activation and their critical functions are largely unknown. Here, we use ChIP-on-chip analysis to map genomic loci decorated by phosphorylated histone H2A (gammaH2A), a Rad3 substrate that establishes a chromatin-based recruitment platform for Crb2 and Brc1 DNA repair/checkpoint proteins. Unexpectedly, gammaH2A marks a diverse array of genomic features during S-phase, including natural replication fork barriers and a fork breakage site, retrotransposons, heterochromatin in the centromeres and telomeres, and ribosomal RNA (rDNA) repeats. gammaH2A formation at the centromeres and telomeres is associated with heterochromatin establishment by Clr4 histone methyltransferase. We show that gammaH2A domains recruit Brc1, a factor involved in repair of damaged replication forks. Brc1 C-terminal BRCT domain binding to gammaH2A is crucial in the absence of Rqh1(Sgs1), a RecQ DNA helicase required for rDNA maintenance whose human homologs are mutated in patients with Werner, Bloom, and Rothmund-Thomson syndromes that are characterized by cancer-predisposition or accelerated aging. We conclude that Rad3 phosphorylates histone H2A to mobilize Brc1 to critical genomic domains during S-phase, and this pathway functions in parallel with Rqh1 DNA helicase in maintaining genome integrity.","doi":"10.1371/journal.pgen.1001032","authors":"Rozenzhak S, Mejía-Ramírez E, Williams JS, Schaffer L, Hammond JA, Head SR, Russell P","authors_abbrev":"Rozenzhak S et al.","pubmed_publication_date":"22 Jul 2010","pubmed_entrez_date":"2010-07-28","publication_year":"2010","canto_session_key":"08562810fce65760","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2015-02-05 11:09:27","canto_approved_date":"2024-05-02 07:49:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-28 19:40:21","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":43,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.06c","SPBC216.05","SPCC18B5.11c","SPAC2G11.12","SPAC16A10.07c","SPBC30D10.04","SPAC19G12.06c","SPCC622.08c","SPCC23B6.03c","SPBC582.05c","SPBC428.08c","SPAC664.01c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2015-02-05"},{"uniquename":"PMID:30078721","title":"Pericentromere-Specific Cohesin Complex Prevents Meiotic Pericentric DNA Double-Strand Breaks and Lethal Crossovers.","citation":"Mol Cell 2018 Aug 16;71(4):540-553.e4","abstract":"In most eukaryotes, meiotic crossovers are essential for error-free chromosome segregation but are specifically repressed near centromeres to prevent missegregation. Recognized for >85 years, the molecular mechanism of this repression has remained unknown. Meiotic chromosomes contain two distinct cohesin complexes: pericentric complex (for segregation) and chromosomal arm complex (for crossing over). We show that the pericentric-specific complex also actively represses pericentric meiotic double-strand break (DSB) formation and, consequently, crossovers. We uncover the mechanism by which fission yeast heterochromatin protein Swi6 (mammalian HP1-homolog) prevents recruitment of activators of meiotic DSB formation. Localizing missing activators to wild-type pericentromeres bypasses repression and generates abundant crossovers but reduces gamete viability. The molecular mechanism elucidated here likely extends to other species, including humans, where pericentric crossovers can result in disorders, such as Down syndrome. These mechanistic insights provide new clues to understand the roles played by multiple cohesin complexes, especially in human infertility and birth defects.","doi":"10.1016/j.molcel.2018.06.035","authors":"Nambiar M, Smith GR","authors_abbrev":"Nambiar M et al.","pubmed_publication_date":"16 Aug 2018","pubmed_entrez_date":"2018-08-07","publication_year":"2018","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-08-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4E9.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12787490","title":"Regulation of the gene encoding glutathione synthetase from the fission yeast.","citation":"J Biochem Mol Biol 2003 May 31;36(3):326-31","abstract":"The fission yeast cells that contained the cloned glutathione synthetase (GS) gene showed 1.4-fold higher glutathione (GSH) content and 1.9-fold higher GS activity than the cells without the cloned GS gene. Interestingly, gamma-glutamylcysteine synthetase activity increased 2.1-fold in the S. pombe cells that contained the cloned GS gene. The S. pombe cells that harbored the multicopy-number plasmid pRGS49 (containing the cloned GS gene) showed a higher level of survival on solid media with cadmium chloride (1 mM) or mercuric chloride (10 microM) than the cells that harbored the YEp357R vector. The 506 bp upstream sequence from the translational initiation point and N-terminal 8 amino acid-coding region were fused into the promoterless beta-galactosidase gene of the shuttle vector YEp367R to generate the fusion plasmid pUGS39. Synthesis of beta-galactosidase from the fusion plasmid pUGS39 was significantly enhanced by cadmium chloride and NO-generating S-nitroso-N-acetylpenicillamine (SNAP) and sodium nitroprusside (SN). It was also induced by L-buthionine-(S,R)-sulfoximine, a specific inhibitor of gamma-glutamylcysteine synthetase (GCS). We also found that the expression of the S. pombe GS gene is regulated by the Atf1-Spc1-Wis1 signal pathway.","authors":"Kim SJ, Shin YH, Kim K, Park EH, Sa JH, Lim CJ","authors_abbrev":"Kim SJ et al.","pubmed_publication_date":"31 May 2003","pubmed_entrez_date":"2003-06-06","publication_year":"2003","canto_session_key":"65eca0c4040c4148","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-04 10:33:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-19 10:07:44","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC1783.07c","SPAC3F10.04","SPAC24B11.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-11-19"},{"uniquename":"PMID:19285552","title":"Dual positive and negative regulation of GPCR signaling by GTP hydrolysis.","citation":"Cell Signal 2009 Jul;21(7):1151-60","abstract":"G protein-coupled receptors (GPCRs) regulate a variety of intracellular pathways through their ability to promote the binding of GTP to heterotrimeric G proteins. Regulator of G protein signaling (RGS) proteins increases the intrinsic GTPase activity of Galpha-subunits and are widely regarded as negative regulators of G protein signaling. Using yeast we demonstrate that GTP hydrolysis is not only required for desensitization, but is essential for achieving a high maximal (saturated level) response. Thus RGS-mediated GTP hydrolysis acts as both a negative (low stimulation) and positive (high stimulation) regulator of signaling. To account for this we generated a new kinetic model of the G protein cycle where Galpha(GTP) enters an inactive GTP-bound state following effector activation. Furthermore, in vivo and in silico experimentation demonstrates that maximum signaling output first increases and then decreases with RGS concentration. This unimodal, non-monotone dependence on RGS concentration is novel. Analysis of the kinetic model has revealed a dynamic network motif that shows precisely how inclusion of the inactive GTP-bound state for the Galpha produces this unimodal relationship.","doi":"10.1016/j.cellsig.2009.03.004","authors":"Smith B, Hill C, Godfrey EL, Rand D, van den Berg H, Thornton S, Hodgkin M, Davey J, Ladds G","authors_abbrev":"Smith B et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-03-17","publication_year":"2009","canto_session_key":"20028534fec00d20","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-19 08:16:29","canto_approved_date":"2025-12-14 10:20:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-16 16:18:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.12c","SPBC24C6.06"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-09-19"},{"uniquename":"PMID:8604986","title":"Molecular cloning of a Schizosaccharomyces pombe cDNA encoding lanosterol synthase and investigation of conserved tryptophan residues.","citation":"Biochem Biophys Res Commun 1996 Feb 15;219(2):327-31","abstract":"A Schizosaccharomyces pombe cDNA encoding lanosterol synthase was cloned by complementing a Saccharomyces cerevisiae lanosterol synthase mutant. The predicted 83-kDa protein is 54-58% identical to other lanosterol synthases. The previously known lanosterol synthases contain 229 conserved residues, which should encompass the catalytically essential amino acids. This number is decreased dramatically by including the Sc. pombe lanosterol synthase in the analysis; 42 residues are no longer conserved and therefore are catalytically nonessential. We have begun mutagenic studies to identify catalytic residues from the remaining conserved residues. Mutant Sa. cerevisiae lanosterol synthase genes were generated in which phenylalanine was specifically substituted for conserved tryptophan residues. All of the resultant mutant enzymes retained the ability to complement the Sc. cerevisiae lanosterol synthase mutant, suggesting that these conserved tryptophan residues are not catalytically essential.","authors":"Corey EJ, Matsuda SP, Baker CH, Ting AY, Cheng H","authors_abbrev":"Corey EJ et al.","pubmed_publication_date":"15 Feb 1996","pubmed_entrez_date":"1996-02-15","publication_year":"1996","canto_session_key":"f446fb0239797428","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 14:39:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 14:39:39","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13G7.01c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-07-31"},{"uniquename":"PMID:39485800","title":"Structural duality enables a single protein to act as a toxin-antidote pair for meiotic drive.","citation":"Proc Natl Acad Sci U S A 2024 Nov 05;121(45):e2408618121","abstract":"In sexual reproduction, selfish genetic elements known as killer meiotic drivers (KMDs) bias inheritance by eliminating gametes that do not carry them. The selective killing behavior of most KMDs can be explained by a toxin-antidote model, where a toxin harms all gametes while an antidote provides resistance to the toxin in carriers. This study investigates whether and how the KMD element  tdk1  in the fission yeast  Schizosaccharomyces pombe  deploys this strategy. Intriguingly,  tdk1  relies on a single protein product, Tdk1, for both killing and resistance. We show that Tdk1 exists in a nontoxic tetrameric form during vegetative growth and meiosis but transforms into a distinct toxic form in spores. This toxic form acquires the ability to interact with the histone reader Bdf1 and assembles into supramolecular foci that disrupt mitosis in noncarriers after spore germination. In contrast, Tdk1 synthesized during germination of carrier spores is nontoxic and acts as an antidote, dismantling the preformed toxic Tdk1 assemblies. Replacement of the N-terminal region of Tdk1 with a tetramer-forming peptide reveals its dual roles in imposing an autoinhibited tetrameric conformation and facilitating the assembly of supramolecular foci when autoinhibition is released. Moreover, we successfully reconstituted a functional KMD element by combining a construct that exclusively expresses Tdk1 during meiosis (\"toxin-only\") with another construct that expresses Tdk1 specifically during germination (\"antidote-only\"). This work uncovers a remarkable example of a single protein employing structural duality to form a toxin-antidote pair, expanding our understanding of the mechanisms underlying toxin-antidote systems.","doi":"10.1073/pnas.2408618121","authors":"Hua Y, Zhang J, Yang MY, Ren JY, Suo F, Liang L, Dong MQ, Ye K, Du LL","authors_abbrev":"Hua Y et al.","pubmed_publication_date":"05 Nov 2024","pubmed_entrez_date":"2024-11-01","publication_year":"2024","canto_session_key":"383a6e4a068f07e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yu Hua","canto_first_approved_date":"2025-01-10 12:33:43","canto_approved_date":"2025-01-10 12:35:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-12-26 14:49:29","canto_added_date":"2024-11-02 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":7,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Yu Hua","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1450.02","SPCC330.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2025-01-10","pdb_entries":[{"pdb_id":"9ja6","gene_chains":[{"gene_uniquename":"SPCC330.04c","chain":"A/A/B/B/C/C/D/D","position":"1-357"}],"title":"Cryo-EM structure of Tdk1 tetramer complex","entry_authors":"Zhang J,Ye K","entry_authors_abbrev":"Zhang J et al.","reference_uniquename":"PMID:39485800","experimental_method":"EM","resolution":"4.4"}]},{"uniquename":"PMID:12760050","title":"DNA damage checkpoint control of mitosis in fission yeast.","citation":"Cold Spring Harb Symp Quant Biol 2000;65:353-9","abstract":"","authors":"Rhind N, Baber-Furnari BA, Lopez-Girona A, Boddy MN, Brondello JM, Moser B, Shanahan P, Blasina A, McGowan C, Russell P","authors_abbrev":"Rhind N et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2003-05-23","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12181330","title":"Crp79p, like Mex67p, is an auxiliary mRNA export factor in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2002 Aug;13(8):2571-84","abstract":"The export of mRNA from the nucleus to the cytoplasm involves interactions of proteins with mRNA and the nuclear pore complex. We isolated Crp79p, a novel mRNA export factor from the same synthetic lethal screen that led to the identification of spMex67p in Schizosaccharomyces pombe. Crp79p is a 710-amino-acid-long protein that contains three RNA recognition motif domains in tandem and a distinct C-terminus. Fused to green fluorescent protein (GFP), Crp79p localizes to the cytoplasm. Like Mex67p, Crp79-GFP binds poly(A)(+) RNA in vivo, shuttles between the nucleus and the cytoplasm, and contains a nuclear export activity at the C-terminus that is Crm1p-independent. All of these properties are essential for Crp79p to promote mRNA export. Crp79p import into the nucleus depends on the Ran system. A domain of spMex67p previously identified as having a nuclear export activity can functionally substitute for the nuclear export activity at the C-terminus of Crp79p. Although both Crp79p and spMex67p function to export mRNA, Crp79p does not substitute for all of spMex67p functions and probably is not a functional homologue of spMex67p. We propose that Crp79p is a nonessential mRNA export carrier in S. pombe.","authors":"Thakurta AG, Whalen WA, Yoon JH, Bharathi A, Kozak L, Whiteford C, Love DC, Hanover JA, Dhar R","authors_abbrev":"Thakurta AG et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-08-16","publication_year":"2002","canto_session_key":"3b211355644f4b72","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 14:01:58","canto_approved_date":"2024-04-03 08:20:50","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-01-20 16:07:46","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":44,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.14","SPAP27G11.10c","SPBC16A3.05c","SPBC557.03c","SPBC1921.03c","SPAC1610.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-09-17"},{"uniquename":"PMID:34895466","title":"Diverse mating phenotypes impact the spread of  wtf  meiotic drivers in  Schizosaccharomyces pombe .","citation":"Elife 2021 Dec 13;10","abstract":"Meiotic drivers are genetic elements that break Mendel's law of segregation to be transmitted into more than half of the offspring produced by a heterozygote. The success of a driver relies on outcrossing (mating between individuals from distinct lineages) because drivers gain their advantage in heterozygotes. It is, therefore, curious that  Schizosaccharomyces pombe , a species reported to rarely outcross, harbors many meiotic drivers. To address this paradox, we measured mating phenotypes in  S. pombe  natural isolates. We found that the propensity for cells from distinct clonal lineages to mate varies between natural isolates and can be affected both by cell density and by the available sexual partners. Additionally, we found that the observed levels of preferential mating between cells from the same clonal lineage can slow, but not prevent, the spread of a  wtf  meiotic driver in the absence of additional fitness costs linked to the driver. These analyses reveal parameters critical to understanding the evolution of  S. pombe  and help explain the success of meiotic drivers in this species.","doi":"10.7554/eLife.70812","authors":"López Hernández JF, Helston RM, Lange JJ, Billmyre RB, Schaffner SH, Eickbush MT, McCroskey S, Zanders SE","authors_abbrev":"López Hernández JF et al.","pubmed_publication_date":"13 Dec 2021","pubmed_entrez_date":"2021-12-13","publication_year":"2021","canto_session_key":"b855ecc307eb12e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-12-18 20:23:45","canto_approved_date":"2026-06-17 13:14:30","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-04-04 10:05:57","canto_added_date":"2021-12-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC548.03c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2021-12-18"},{"uniquename":"PMID:19682091","title":"Fission yeast Ku protein is required for recovery from DNA replication stress.","citation":"Genes Cells 2009 Sep;14(9):1091-103","abstract":"The fundamental function of the conserved Ku70-Ku80 heterodimer is to promote the non-homologous end-joining (NHEJ) pathway in double-strand break repair. Although it is thought that Ku plays several roles other than NHEJ in maintaining chromosomal integrity including telomere protection, these precise functions remain unclear. In this study, we describe a novel role of fission yeast Ku proteins encoded by pku70(+) and pku80(+) genes in dealing with DNA replication stress. In the absence of Rqh1, the fission yeast RecQ helicase, the cells are sensitive to reagents inducing replication stress. pkuDeltarqh1Delta double mutant showed synergistic sensitivities to these reagents. However, this synthetic phenotype was not observed when rqh1Delta mutant was coupled with the deletion of lig4(+) that encodes a ligase essential for NHEJ, indicating that the role of Ku in replication stress is NHEJ independent. pkuDeltarqh1Delta double mutant also showed highly variable copy numbers of rDNA repeats even under unstressed condition. Furthermore, the double mutant exhibited inefficient replication resumption after transient replication stalling. These results suggest the possibility that Ku proteins play an important role in genome integrity recovering replication stress.","doi":"10.1111/j.1365-2443.2009.01337.x","authors":"Miyoshi T, Kanoh J, Ishikawa F","authors_abbrev":"Miyoshi T et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-08-18","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPBC543.03c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:1825699","title":"Fission yeast p107wee1 mitotic inhibitor is a tyrosine/serine kinase.","citation":"Nature 1991 Feb 28;349(6312):808-11","abstract":"The fission yeast wee1+ gene product is a dose-dependent, negative regulator of entry into mitosis. wee1+ encodes a protein of relative molecular mass 107,000 (Mr 107K), the C-terminal third of which has strong similarities with the serine/threonine protein kinase family. Here we report that p107wee1 immune complexes phosphorylate p107wee1 equally on serine and tyrosine residues, and also phosphorylate an exogenous substrate, angiotensin II, on tyrosine. Both kinase activities are attributable to p107wee1 because they are also observed when wee1+ is expressed in heterologous systems; both are abolished by a point mutation in the ATP-binding domain, and both behave like an asymmetric monomer of Mr114K on gel filtration and density-gradient centrifugation. Thus the wee1+ gene product is representative of a novel class of protein kinase that phosphorylates both serine and tyrosine residues.","authors":"Featherstone C, Russell P","authors_abbrev":"Featherstone C et al.","pubmed_publication_date":"28 Feb 1991","pubmed_entrez_date":"1991-02-28","publication_year":"1991","canto_session_key":"6745da7b0165e94c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-17 09:22:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-14 18:25:24","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-14"},{"uniquename":"EMBL:AU007864","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34194665","title":"Functional and structural investigation of N-terminal domain of the SpTad2/3 heterodimeric tRNA deaminase.","citation":"Comput Struct Biotechnol J 2021;19:3384-3393","abstract":"Editing is a post-transcriptional process that changes the content of nucleic acids occurring on both DNA and RNA levels. Inosine at position 34 in tRNA is one such example, commonly produced via the deamination of A34, catalyzed by adenosine deaminase acting on tRNA (ADAT or Tad). The formation of inosine is essential for cell viability. The eukaryotic deaminases normally consist of the catalytic subunit Tad2 and the structural subunit Tad3, but the catalytic process is poorly understood. Despite the conservation of the (pseudo-) catalytic domains, the heterodimeric enzyme Tad2/3 also possesses additional domains that could exhibit novel functions. Here we present the structure of the N-terminal domain of the  Schizosaccharomyces pombe  Tad2/3 heterodimeric tRNA(A34) deaminase (N-SpTad2), which shares ~30% sequence identities with uridine-cytidine or pantothenate kinases, but lacks the predicted kinase functions. While biochemical assays indicated that the domain is not a nucleic-acid binder, it is able to significantly influence the A34-tRNA deamination activity of the holoenzyme. Through co-expression and purification analyses, we deduce that N-SpTad2 plays a role in mediating protein-protein contacts and enhancing the stability and solubility of SpTad2/3, without which the deaminase is not functional. Taken together, our structural and biochemical studies highlighted the importance of the additional domains to the intrinsic deaminase functions of heterodimeric Tad2/3 enzymes and promoted our understanding on this essential post-transcriptional tRNA modification.","doi":"10.1016/j.csbj.2021.06.008","authors":"Liu X, Zhou J, Ge R, Xie W","authors_abbrev":"Liu X et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-07-01","publication_year":"2021","canto_session_key":"d651509e58b938b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-03-05 14:46:04","canto_approved_date":"2023-03-05 14:46:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-01 20:34:55","canto_added_date":"2021-07-03 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.10","SPAP27G11.04c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2023-03-05","pdb_entries":[{"pdb_id":"7eey","gene_chains":[{"gene_uniquename":"SPBC16D10.10","chain":"A/B/C/D","position":"1-202"}],"title":"The structure of the N-terminal doamin of the Schizosaccharomyces pombe Tad2 adenosine deaminase","entry_authors":"Xie W,Liu X,Zhou J","entry_authors_abbrev":"Xie W et al.","reference_uniquename":"PMID:34194665","experimental_method":"X-ray","resolution":"2.6"}]},{"uniquename":"PMID:19620282","title":"The fission yeast HIRA histone chaperone is required for promoter silencing and the suppression of cryptic antisense transcripts.","citation":"Mol Cell Biol 2009 Sep;29(18):5158-67","abstract":"The assembly of nucleosomes by histone chaperones is an important component of transcriptional regulation. Here, we have assessed the global roles of the HIRA histone chaperone in Schizosaccharomyces pombe. Microarray analysis indicates that inactivation of the HIRA complex results in increased expression of at least 4% of fission yeast genes. HIRA-regulated genes overlap with those which are normally repressed in vegetatively growing cells, such as targets of the Clr6 histone deacetylase and silenced genes located in subtelomeric regions. HIRA is also required for silencing of all 13 intact copies of the Tf2 long terminal repeat (LTR) retrotransposon. However, the role of HIRA is not restricted to bona fide promoters, because HIRA also suppresses noncoding transcripts from solo LTR elements and spurious antisense transcripts from cryptic promoters associated with transcribed regions. Furthermore, the HIRA complex is essential in the absence of the quality control provided by nuclear exosome-mediated degradation of illegitimate transcripts. This suggests that HIRA restricts genomic accessibility, and consistent with this, the chromosomes of cells lacking HIRA are more susceptible to genotoxic agents that cause double-strand breaks. Thus, the HIRA histone chaperone is required to maintain the protective functions of chromatin.","doi":"10.1128/MCB.00698-09","authors":"Anderson HE, Wardle J, Korkut SV, Murton HE, López-Maury L, Bähler J, Whitehall SK","authors_abbrev":"Anderson HE et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-07-22","publication_year":"2009","canto_session_key":"54da5827399abb86","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-04-19 23:04:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-04-19 23:04:39","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F3.01","SPBC36.05c","SPBC15D4.03","SPBC31F10.13c","SPAC23E2.01","SPBC31F10.14c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-04-19"},{"uniquename":"PMID:41149761","title":"Identification and Functions of lncRNAs in Fungi.","citation":"Noncoding RNA 2025 Oct 07;11(5)","abstract":"Long noncoding RNAs (lncRNAs) are transcripts generated by polymerase II, therefore subject to 5' capping and 3' polyadenylation, categorized as such when they are at least 200 nt in size and lack coding function. The lncRNAs were initially interpreted as spurious transcription products, but over the last two decades an increasing amount of evidence has accumulated for regulatory functions. They are found in all taxonomic groups, including bacteria, archaea, fungi, animals and plants. In fungi, global analyses anticipate their presence in higher numbers than initially expected considering the simplicity of these organisms. Except for the numerous studies performed in budding and fission yeast, relatively few lncRNAs have been investigated in sufficient detail in the rest of the fungi, but their number has increased steadily in recent years. The lncRNAs can be transcribed from intergenic regions or coincide totally or partially with protein-coding genes, in which case they are most frequently antisense transcripts. Their regulatory functions can be performed by a wide variety of mechanisms, both in  cis  on neighboring genes and in  trans  on distant genes or on proteins. Among the most frequent mechanisms are interference on the transcription of neighboring genes and generation of epigenetic modifications in the environment of target genes. Here, we review the most representative cases of global analyses of the presence of lncRNAs in fungal transcriptomes and describe the lncRNAs that have received more detailed attention.","doi":"10.3390/ncrna11050072","authors":"Avalos J, Perera-Bonaño A, Limón MC","authors_abbrev":"Avalos J et al.","pubmed_publication_date":"07 Oct 2025","pubmed_entrez_date":"2025-10-28","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-10-29 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24342487","title":"Spatiotemporal organization of microbial cells by protein concentration gradients.","citation":"Trends Microbiol 2014 Feb;22(2):65-73","abstract":"The formation of protein concentration gradients is an effective means to restrict the activity of regulatory factors in space, thereby critically contributing to the spatiotemporal organization of biological systems. Although widely observed for extracellular proteins involved in tissue patterning, the implementation of this regulatory strategy was thought to be impossible in single, micron-sized cells. Recently, however, several intracellular proteins were shown to establish gradient-like distribution patterns, thereby relaying positional information to their downstream targets. In this review, we discuss gradient-forming systems from different microbial species, with an emphasis on their mode of action and the common principles that underlie their function.","doi":"10.1016/j.tim.2013.11.005","authors":"Kiekebusch D, Thanbichler M","authors_abbrev":"Kiekebusch D et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-12-18","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-09-24 00:15:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F7.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29975113","title":"Relief of the Dma1-mediated checkpoint requires Dma1 autoubiquitination and dynamic localization.","citation":"Mol Biol Cell 2018 Sep 01;29(18):2176-2189","abstract":"Chromosome segregation and cell division are coupled to prevent aneuploidy and cell death. In the fission yeast Schizosaccharomyces pombe, the septation initiation network (SIN) promotes cytokinesis, but upon mitotic checkpoint activation, the SIN is actively inhibited to prevent cytokinesis from occurring before chromosomes have safely segregated. SIN inhibition during the mitotic checkpoint is mediated by the E3 ubiquitin ligase Dma1. Dma1 binds to the CK1-phosphorylated SIN scaffold protein Sid4 at the spindle pole body (SPB), and ubiquitinates it. Sid4 ubiquitination antagonizes the SPB localization of the Pololike kinase Plo1, the major SIN activator, so that SIN signaling is delayed. How this checkpoint is silenced once spindle defects are resolved has not been clear. Here we establish that Dma1 transiently leaves SPBs during anaphase B due to extensive autoubiquitination. The SIN is required for Dma1 to return to SPBs later in anaphase. Blocking Dma1 removal from SPBs by permanently tethering it to Sid4 prevents SIN activation and cytokinesis. Therefore, controlling Dma1's SPB dynamics in anaphase is an essential step in S. pombe cell division and the silencing of the Dma1-dependent mitotic checkpoint.","doi":"10.1091/mbc.E18-04-0261","authors":"Jones CM, Chen JS, Johnson AE, Elmore ZC, Cullati SN, Beckley JR, Gould KL","authors_abbrev":"Jones CM et al.","pubmed_publication_date":"01 Sep 2018","pubmed_entrez_date":"2018-07-06","publication_year":"2018","canto_session_key":"f30149c5fcc7f553","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-Song Chen","canto_first_approved_date":"2018-07-31 19:25:13","canto_approved_date":"2026-05-29 17:21:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-31 16:20:44","canto_added_date":"2018-07-07 00:15:04","annotation_curators":[{"name":"Jun-Song Chen","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16G5.01","SPCC16A11.12c","SPBC244.01c","SPAC328.06","SPAC23G3.08c","SPAC17G8.10c","SPBC6B1.06c","SPAC4H3.11c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-07-31"},{"uniquename":"PMID:23658422","title":"FYPO: the fission yeast phenotype ontology.","citation":"Bioinformatics 2013 Jul 01;29(13):1671-8","abstract":"To provide consistent computable descriptions of phenotype data, PomBase is developing a formal ontology of phenotypes observed in fission yeast.\nThe fission yeast phenotype ontology (FYPO) is a modular ontology that uses several existing ontologies from the open biological and biomedical ontologies (OBO) collection as building blocks, including the phenotypic quality ontology PATO, the Gene Ontology and Chemical Entities of Biological Interest. Modular ontology development facilitates partially automated effective organization of detailed phenotype descriptions with complex relationships to each other and to underlying biological phenomena. As a result, FYPO supports sophisticated querying, computational analysis and comparison between different experiments and even between species.\nFYPO releases are available from the Subversion repository at the PomBase SourceForge project page (https://sourceforge.net/p/pombase/code/HEAD/tree/phenotype_ontology/). The current version of FYPO is also available on the OBO Foundry Web site (http://obofoundry.org/).","doi":"10.1093/bioinformatics/btt266","authors":"Harris MA, Lock A, Bähler J, Oliver SG, Wood V","authors_abbrev":"Harris MA et al.","pubmed_publication_date":"01 Jul 2013","pubmed_entrez_date":"2013-05-10","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8387850","title":"Behaviour of plasmid containing C4A2 repeats in S. cerevisiae and S. pombe.","citation":"Biochem Mol Biol Int 1993 Mar;29(4):673-85","abstract":"Plasmid, which combined the complete genome of BPV-I, yeast ARS, LEU yeast selectable marker gene, the NEO selectable marker gene and inverted (C4A2)n telomeric repeat gene sequences cloned originally from Tetrahymena thermophila, was constructed. It was introduced in either circular or linear form to Saccharomyces cerevisiae or Schizosaccharomyces pombe. Although both yeasts could replicate the plasmid extrachromosomally, irrespective of whether it was introduced as a circular or linear structure, the yeasts did differ in their ability to resolve a circular plasmid carrying the telomeric sequences into linear forms. S. cerevisiae was found to resolve the circular form of pCA/LEU/ARS to the linear structure, whereas circular pCA/LEU/ARS remained circular in S. pombe. On the other hand, pCA/LEU/ARS which had been previously linearised at the telomeric sequence was maintained as a linear structure in S. pombe and S. cerevisiae.","authors":"Shervington AA, Sparey JA, Bostock CJ","authors_abbrev":"Shervington AA et al.","pubmed_publication_date":"Mar 1993","pubmed_entrez_date":"1993-03-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6268620","title":"The nucleotide sequence of 5S ribosomal RNA from Schizosaccharomyces pombe.","citation":"J Biochem 1981 May;89(5):1663-6","abstract":"The nucleotide sequence of 5S rRNA from the fission yeast, S. pombe, has been established by post labeling procedures combined with cataloging RNase T1- and A-oligonucleotides derived from unlabeled 5S rRNA. The sequence consists of 119 nucleotides without a modified base and shows more dissimilarities (at 38 positions) from that of S. cerevisiae than from that of humans (at 33 positions).","authors":"Komiya H, Miyazaki M, Takemura S","authors_abbrev":"Komiya H et al.","pubmed_publication_date":"May 1981","pubmed_entrez_date":"1981-05-01","publication_year":"1981","canto_session_key":"b3f42f94184e7937","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 17:42:56","canto_approved_date":"2019-01-31 17:42:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 17:42:46","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPRRNA.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:24550462","title":"Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy.","citation":"Proc Natl Acad Sci U S A 2014 Mar 18;111(11):4019-24","abstract":"The mechanisms by which gene expression is regulated by oxygen are of considerable interest from basic science and therapeutic perspectives. Using mass spectrometric analyses of Saccharomyces cerevisiae ribosomes, we found that the amino acid residue in closest proximity to the decoding center, Pro-64 of the 40S subunit ribosomal protein Rps23p (RPS23 Pro-62 in humans) undergoes posttranslational hydroxylation. We identify RPS23 hydroxylases as a highly conserved eukaryotic subfamily of Fe(II) and 2-oxoglutarate dependent oxygenases; their catalytic domain is closely related to transcription factor prolyl trans-4-hydroxylases that act as oxygen sensors in the hypoxic response in animals. The RPS23 hydroxylases in S. cerevisiae (Tpa1p), Schizosaccharomyces pombe and green algae catalyze an unprecedented dihydroxylation modification. This observation contrasts with higher eukaryotes, where RPS23 is monohydroxylated; the human Tpa1p homolog OGFOD1 catalyzes prolyl trans-3-hydroxylation. TPA1 deletion modulates termination efficiency up to ∼10-fold, including of pathophysiologically relevant sequences; we reveal Rps23p hydroxylation as its molecular basis. In contrast to most previously characterized accuracy modulators, including antibiotics and the prion state of the S. cerevisiae translation termination factor eRF3, Rps23p hydroxylation can either increase or decrease translational accuracy in a stop codon context-dependent manner. We identify conditions where Rps23p hydroxylation status determines viability as a consequence of nonsense codon suppression. The results reveal a direct link between oxygenase catalysis and the regulation of gene expression at the translational level. They will also aid in the development of small molecules altering translational accuracy for the treatment of genetic diseases linked to nonsense mutations.","doi":"10.1073/pnas.1311750111","authors":"Loenarz C, Sekirnik R, Thalhammer A, Ge W, Spivakovsky E, Mackeen MM, McDonough MA, Cockman ME, Kessler BM, Ratcliffe PJ, Wolf A, Schofield CJ","authors_abbrev":"Loenarz C et al.","pubmed_publication_date":"18 Mar 2014","pubmed_entrez_date":"2014-02-20","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.13","SPAC23C11.02c","SPBC6B1.08c"],"gene_count":3,"ltp_gene_count":1},{"uniquename":"PMID:23912279","title":"Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.","citation":"Nat Struct Mol Biol 2013 Sep;20(9):1098-105","abstract":"N-terminal acetylation is ubiquitous among eukaryotic proteins and controls a myriad of biological processes. Of the N-terminal acetyltransferases (NATs) that facilitate this cotranslational modification, the heterodimeric NatA complex has the most diversity for substrate selection and modifies the majority of all N-terminally acetylated proteins. Here, we report the X-ray crystal structure of the 100-kDa holo-NatA complex from Schizosaccharomyces pombe, in the absence and presence of a bisubstrate peptide-CoA-conjugate inhibitor, as well as the structure of the uncomplexed Naa10p catalytic subunit. The NatA-Naa15p auxiliary subunit contains 13 tetratricopeptide motifs and adopts a ring-like topology that wraps around the NatA-Naa10p subunit, an interaction that alters the Naa10p active site for substrate-specific acetylation. These studies have implications for understanding the mechanistic details of other NAT complexes and how regulatory subunits modulate the activity of the broader family of protein acetyltransferases.","doi":"10.1038/nsmb.2636","authors":"Liszczak G, Goldberg JM, Foyn H, Petersson EJ, Arnesen T, Marmorstein R","authors_abbrev":"Liszczak G et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-08-06","publication_year":"2013","canto_session_key":"90f7e4d9459a5548","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-20 16:34:35","canto_approved_date":"2022-01-18 15:13:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-19 12:40:42","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15E1.08","SPCC338.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-11-20","pdb_entries":[{"pdb_id":"4kvm","gene_chains":[{"gene_uniquename":"SPCC338.07c","chain":"A/B/C/D","position":"1-729"},{"gene_uniquename":"SPAC15E1.08","chain":"E/F/G/H","position":"1-156"}],"title":"The NatA (Naa10p/Naa15p) amino-terminal acetyltransferase complex bound to a bisubstrate analog","entry_authors":"Liszczak GP,Marmorstein RQ","entry_authors_abbrev":"Liszczak GP et al.","reference_uniquename":"PMID:23912279","experimental_method":"X-ray","resolution":"2.597"},{"pdb_id":"4kvx","gene_chains":[{"gene_uniquename":"SPAC15E1.08","chain":"A/B","position":"1-156"}],"title":"Crystal structure of Naa10 (Ard1) bound to AcCoA","entry_authors":"Liszczak GP,Marmorstein RQ","entry_authors_abbrev":"Liszczak GP et al.","reference_uniquename":"PMID:23912279","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"4kvo","gene_chains":[{"gene_uniquename":"SPCC338.07c","chain":"A/B/C/D","position":"1-729"},{"gene_uniquename":"SPAC15E1.08","chain":"E/F/G/H","position":"1-156"}],"title":"The NatA (Naa10p/Naa15p) amino-terminal acetyltrasferase complex bound to AcCoA","entry_authors":"Liszczak GP,Marmorstein RQ","entry_authors_abbrev":"Liszczak GP et al.","reference_uniquename":"PMID:23912279","experimental_method":"X-ray","resolution":"3.15"}]},{"uniquename":"EMBL:SP41368","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011804","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.133"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24752843","title":"Schizosaccharomyces pombe and its Ni(II)-insensitive mutant GA1 in Ni(II) uptake from aqueous solutions: a biodynamic model.","citation":"Appl Microbiol Biotechnol 2014 Aug;98(15):6859-69","abstract":"In the present study, Ni(II) uptake from aqueous solution by living cells of the Schizosaccharomyces pombe haploid 972 with h (-) mating type and a Ni(II)-insensitive mutant GA1 derived from 972 was investigated at various initial glucose and Ni(II) concentrations. A biodynamic model was developed to predict the unsteady and steady-state phases of the uptake process. Gompertz growth and uptake process parameters were optimized to predict the maximum growth rate μ m and the process metric C r, the remaining Ni(II) content in the aqueous solution. The simulated overall metal uptake values were found to be in acceptable agreement with experimental results. The model validation was done through regression statistics and uncertainty and sensitivity analyses. To gain insight into the phenomenon of Ni(II) uptake by wild-type and mutant S. pombe, probable active and passive metal transport mechanisms in yeast cells were discussed in view of the simulation results. The present work revealed the potential of mutant GA1 to remove Ni(II) cations from aqueous media. The results obtained provided new insights for understanding the combined effect of biosorption and bioaccumulation processes for metal removal and offered a possibility for the use of growing mutant S. pombe cell in bioremediation.","doi":"10.1007/s00253-014-5740-5","authors":"Sayar NA, Durmaz-Sam S, Kazan D, Sayar AA","authors_abbrev":"Sayar NA et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-04-23","publication_year":"2014","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9450029","title":"Loss of Prk1 leads to cell aggregation in the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1997 Nov;25(4):S601","abstract":"","authors":"Watson P, Davey J","authors_abbrev":"Watson P et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-02-05","publication_year":"1997","canto_session_key":"1ff5b9ffa8f643b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-06-22 07:11:16","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-06-20 09:35:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H4.17c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-06-20"},{"uniquename":"PMID:9472077","title":"The Ste16 WD-repeat protein regulates cell-cycle progression under starvation through the Rum1 protein in Schizosaccharomyces pombe.","citation":"Curr Genet 1998 Jan;33(1):29-37","abstract":"The haploid cells of the fission yeast, Schizosaccharomyces pombe, are arrested in the G1-phase by nitrogen starvation and are committed to sexual reproduction (mating and sporulation). We isolated the sterile mutants which were defective in G1 arrest following nitrogen starvation. Genetic analysis of these mutants defined a single locus designated as ste16. The nucleotide sequence revealed that ste16+ encodes an 82-kDa protein containing eight WD40-repeats in its carboxy terminal half. The ste16 disruptant was viable, but arrested the cell cycle in the G2-phase after the nutritional down-shift. When transferred to fresh growth medium, the G2-arrested ste16Delta haploids resumed the mitotic cycle from the S-phase, resulting in diploidization. This diploidization phenomenon was completely suppressed by the null mutation of rum1 encoding the inhibitor of Cdc2 kinase. As the Rum1 protein level was remarkably elevated in the ste16Delta, the Ste16 protein negatively controls the Rum1 level. The loss of function of ste16 disturbs the cell-cycle progression and impairs the mechanism for the maintenance of ploidy.","authors":"Maekawa H, Kitamura K, Shimoda C","authors_abbrev":"Maekawa H et al.","pubmed_publication_date":"Jan 1998","pubmed_entrez_date":"1998-04-04","publication_year":"1998","canto_session_key":"3e366f2127c72b67","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-04-26 14:35:51","canto_approved_date":"2026-06-25 18:03:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-04-26 14:35:46","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.01","SPBC32F12.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-04-26"},{"uniquename":"PMID:12206652","title":"Mac1, a fission yeast transmembrane protein localizing to the poles and septum, is required for correct cell separation at high temperatures.","citation":"Biol Cell 2002 Jun;94(3):127-37","abstract":"Schizosaccharomyces pombe represents a genetic model system for studying cell polarity and division in eukaryotes. We report here the identification of Mac1, a novel fission yeast protein that localized predominantly to the cell tips and septum. Sequences corresponding to roughly the first 180 amino acids of Mac1, which exhibited weak homology to the transmembrane domains of the Aspergillus Pall protein [Mol. Microbiol. 30 (1998) 259], were found to specify localization to the cell periphery. The other 574 amino acids of Mac1 localized to the cytoplasm when expressed alone, thus suggesting that the N-terminal part of Mac1 functions as a plasma membrane anchor for the rest of the protein. In pom1 null mutant cells, which never switch from unipolar to bipolar growth but, instead, grow exclusively at the randomly chosen end [Genes Dev. 12 (1998) 1356], Mac1 was, nevertheless, found at both poles, thus suggesting that Mac1 does not specifically localize to the sites of growth. mac1 null mutant cells had no overt phenotype at 22-32 degrees C, but, nevertheless, displayed a marked decrease in viability at 34-36 degrees C, accompanied by severe separation defects. Overexpression of mac1 resulted in similar defects. Our data suggest that a correct dosage of Mac1 is needed for correct cell separation at elevated temperatures of growth.","authors":"Grandin N, Charbonneau M","authors_abbrev":"Grandin N et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-09-11","publication_year":"2002","canto_session_key":"d56066b34a046b53","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-14 21:44:45","canto_approved_date":"2022-01-24 12:03:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-14 21:44:34","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPAC13G7.04c","SPCC1281.01","SPAC2F7.03c","SPBC1289.04c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-12-14"},{"uniquename":"Pfam:PF03062","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3H7.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25952948","title":"Exploiting the multiplexing capabilities of tandem mass tags for high-throughput estimation of cellular protein abundances by mass spectrometry.","citation":"Methods 2015 Sep 01;85:100-107","abstract":"The generation of dynamic models of biological processes critically depends on the determination of precise cellular concentrations of biomolecules. Measurements of system-wide absolute protein levels are particularly valuable information in systems biology. Recently, mass spectrometry based proteomics approaches have been developed to estimate protein concentrations on a proteome-wide scale. However, for very complex proteomes, fractionation steps are required, increasing samples number and instrument analysis time. As a result, the number of full proteomes that can be routinely analyzed is limited. Here we combined absolute quantification strategies with the multiplexing capabilities of isobaric tandem mass tags to determine cellular protein abundances in a high throughput and proteome-wide scale even for highly complex biological systems, such as a whole human cell line. We generated two independent data sets to demonstrate the power of the approach regarding sample throughput, dynamic range, quantitative precision and accuracy as well as proteome coverage in comparison to existing mass spectrometry based strategies.","doi":"10.1016/j.ymeth.2015.04.032","authors":"Ahrné E, Martinez-Segura A, Syed AP, Vina-Vilaseca A, Gruber AJ, Marguerat S, Schmidt A","authors_abbrev":"Ahrné E et al.","pubmed_publication_date":"01 Sep 2015","pubmed_entrez_date":"2015-05-09","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-05-10 00:19:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17905925","title":"Functional characterization of the fission yeast phosphatidylserine synthase gene, pps1, reveals novel cellular functions for phosphatidylserine.","citation":"Eukaryot Cell 2007 Nov;6(11):2092-101","abstract":"To investigate the contributions of phosphatidylserine to the growth and morphogenesis of the rod-shaped fission yeast Schizosaccharomyces pombe, we have characterized the single gene in this organism, pps1, encoding a predicted phosphatidylserine synthase. S. pombe pps1Delta mutants grow slowly in rich medium and are inviable in synthetic minimal medium. They do not produce detectable phosphatidylserine in vivo and possess negligible in vitro phosphatidylserine synthase activity, indicating that pps1 encodes the major phosphatidylserine synthase activity in S. pombe. Supplementation of growth medium with ethanolamine partially suppresses the growth-defective phenotype of pps1Delta cells, reflecting the likely importance of phosphatidylserine as a precursor for phosphatidylethanolamine in S. pombe. In medium lacking ethanolamine, pps1Delta mutants exhibit striking cell morphology, cytokinesis, actin cytoskeleton, and cell wall remodeling and integrity defects. Overexpression of pps1 likewise leads to defects in cell morphology and cytokinesis, thus implicating phosphatidylserine as a dosage-dependent regulator of these processes. During log-phase growth, green fluorescent protein-Pps1p fusion proteins are concentrated at the cell and nuclear peripheries as well as presumptive endoplasmic reticulum membranes, while in stationary-phase cells, they are redistributed to unusual cytoplasmic structures of unknown origin. Moreover, stationary-phase pps1Delta cultures retain very poor viability relative to wild-type S. pombe cells, even in medium containing ethanolamine, demonstrating a role for phosphatidylserine in the physiological adaptations required for stationary-phase survival. Our findings reveal novel cellular functions for phosphatidylserine and emphasize the usefulness of S. pombe as a model organism for elucidating potentially conserved biological and molecular functions of this phospholipid.","authors":"Matsuo Y, Fisher E, Patton-Vogt J, Marcus S","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"Nov 2007","pubmed_entrez_date":"2007-10-02","publication_year":"2007","canto_session_key":"61b0bcb9898f64f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-03-27 14:37:33","canto_approved_date":"2021-04-08 07:03:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-27 16:27:24","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1442.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-03-27"},{"uniquename":"EMBL:AB084870","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.58"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22212525","title":"Chronological lifespan extension by Ecl1 family proteins depends on Prr1 response regulator in fission yeast.","citation":"Genes Cells 2012 Jan;17(1):39-52","abstract":"ecl1+, ecl2+ and ecl3+ genes encode highly homologous small proteins, and their over-expressions confer both H2O2 stress resistance and chronological lifespan extension on Schizosaccharomyces pombe. However, the mechanisms of how these Ecl1 family proteins function have not been elucidated. In this study, we conducted microarray analysis and identified that the expression of genes involved in sexual development and stress responses was affected by the over-expression of Ecl1 family proteins. In agreement with the mRNA expression profile, the cells over-expressing Ecl1 family proteins showed high mating efficiency and resistant phenotype to H2O2. We showed that the H2O2-resistant phenotype depends on catalase Ctt1, and over-expression of ctt1+ does not affect chronological lifespan. Furthermore, we showed that six genes, ste11+, spk1+, hsr1+, rsv2+, hsp9+ and lsd90+, whose expressions are increased in cells over-expressing Ecl1 family proteins are involved in chronological lifespan in fission yeast. Among these genes, the induction of ste11+ and hsr1+ was dependent on a transcription factor Prr1, and we showed that the extensions of chronological lifespan by Ecl1 family proteins are remarkably diminished in prr1 deletion mutant. From these results, we propose that Ecl1-family proteins conduct H2O2 stress resistance and chronological lifespan extension in ctt1+- and prr1+-dependent manner, respectively.","doi":"10.1111/j.1365-2443.2011.01571.x","authors":"Ohtsuka H, Azuma K, Kubota S, Murakami H, Giga-Hama Y, Tohda H, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2012-01-04","publication_year":"2012","canto_session_key":"b5250ba4e2e55f61","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-10 17:27:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-25 16:27:51","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":70,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16E9.16c","SPAP8A3.04c","SPBC1105.14","SPBC32C12.02","SPAC8C9.14","SPAC3H1.11","SPBP35G2.16c","SPAC31G5.09c","SPBC8E4.12c","SPCC70.12c","SPCC757.07c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2014-09-25"},{"uniquename":"PMID:19033386","title":"Stress-regulated kinase pathways in the recovery of tip growth and microtubule dynamics following osmotic stress in S. pombe.","citation":"J Cell Sci 2008 Dec 15;121(Pt 24):4055-68","abstract":"The cell-integrity and stress-response MAP kinase pathways (CIP and SRP, respectively) are stimulated by various environmental stresses. Ssp1 kinase modulates actin dynamics and is rapidly recruited to the plasma membrane following osmotic stress. Here, we show that osmotic stress arrested tip growth, induced the deposition of abnormal cell-wall deposits at tips and led to disassociation of F-actin foci from cell tips together with a reduction in the amount of F-actin in these foci. Osmotic stress also ;froze' the dynamics of interphase microtubule bundles, with microtubules remaining static for approximately 38 minutes (at 30 degrees C) before fragmenting upon return to dynamic behaviour. The timing with which microtubules resumed dynamic behaviour relied upon SRP activation of Atf1-mediated transcription, but not on either CIP or Ssp1 signalling. Analysis of the recovery of tip growth showed that: (1) the timing of recovery was controlled by SRP-stimulated Atf1 transcription; (2) re-establishment of polarized tip growth was absolutely dependent upon SRP and partially dependent upon Ssp1 signalling; and (3) selection of the site for polarized tip extension required Ssp1 and the SRP-associated polarity factor Wsh3 (also known as Tea4). CIP signalling did not impact upon any aspect of recovery. The normal kinetics of tip growth following osmotic stress of plo1.S402A/E mutants established that SRP control over the resumption of tip growth after osmotic stress is distinct from its control of tip growth following heat or gravitational stresses.","doi":"10.1242/jcs.034488","authors":"Robertson AM, Hagan IM","authors_abbrev":"Robertson AM et al.","pubmed_publication_date":"15 Dec 2008","pubmed_entrez_date":"2008-11-27","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2839469","title":"Characterization of the ATPase and GTPase activities of elongation factor 3 (EF-3) purified from yeasts.","citation":"J Biochem 1988 Mar;103(3):522-30","abstract":"Three steps of chromatography of a post-ribosomal supernatant fraction have provided a highly purified preparation of peptide elongation factor 3 (EF-3) with a molecular weight of 125,000 from the typical budding yeast Saccharomyces carlsbergensis and of the factor with a molecular weight of 120,000 from the fission yeast Schizosaccharomyces pombe. Both of the proteins consist of a single peptide chain. The purified factors fulfilled the requirement for polyphenylalanine synthesis on yeast ribosomes and exhibited strong ATPase and GTPase activities dependent on yeast ribosomes. The activity profiles of the nucleotidases dependent on pH and salt concentration and the inhibition studies indicated that the ATPase and GTPase activities of EF-3 were displayed by the same active site with a wide substrate specificity, showing the highest activity with ATP. Those experiments also revealed that the ATPase and GTPase of EF-3 were characteristically different from the GTPases of EF-1 alpha and EF-2. Both Km and kcat of EF-3 for ATP (Km = 0.12 mM and Kcat = 610 mol/mol/min) and GTP (Km = 0.20 mM and kcat = 390 mol/mol/min) are much higher than those of the GTPases of EF-1 alpha and EF-2. Inactivation experiments and studies on the ATP effect led us to conclude that this ATPase activity was an essential requirement for the functional role of EF-3 and therefore, in addition to the GTPases of EF-1 alpha and EF-2, the third nucleoside triphosphate hydrolyzing step by the ATPase of EF-3 was necessary for the yeast peptide elongation cycle.","authors":"Uritani M, Miyazaki M","authors_abbrev":"Uritani M et al.","pubmed_publication_date":"Mar 1988","pubmed_entrez_date":"1988-03-01","publication_year":"1988","canto_session_key":"cbe01c1c77a184f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-30 14:27:39","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-30 14:27:31","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-09-30"},{"uniquename":"PMID:11917007","title":"Transcriptional silencing in Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2002 Apr 01;30(7):1465-82","abstract":"Transcriptional silencing is a heritable form of gene inactivation that involves the assembly of large regions of DNA into a specialized chromatin structure that inhibits transcription. This phenomenon is responsible for inhibiting transcription at silent mating-type loci, telomeres and rDNA repeats in both budding yeast Saccharomyces cerevisiae and fission yeast Schizosaccharomyces pombe, as well as at centromeres in fission yeast. Although transcriptional silencing in both S.cerevisiae and S.pombe involves modification of chromatin, no apparent amino acid sequence similarities have been reported between the proteins involved in establishment and maintenance of silent chromatin in these two distantly related yeasts. Silencing in S.cerevisiae is mediated by Sir2p-containing complexes, whereas silencing in S.pombe is mediated primarily by Swi6-containing complexes. The Swi6 complexes of S.pombe contain proteins closely related to their counterparts in higher eukaryotes, but have no apparent orthologs in S.cerevisiae. Silencing proteins from both yeasts are also actively involved in other chromosome-related nuclear functions, including DNA repair and the regulation of chromatin structure.","authors":"Huang Y","authors_abbrev":"Huang Y","pubmed_publication_date":"01 Apr 2002","pubmed_entrez_date":"2002-03-28","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR001911","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:14046","SPBC839.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU008781","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22464190","title":"Epigenetic inactivation and subsequent heterochromatinization of a centromere stabilize dicentric chromosomes.","citation":"Curr Biol 2012 Apr 24;22(8):658-67","abstract":"The kinetochore is a multiprotein complex that forms on a chromosomal locus designated as the centromere, which links the chromosome to the spindle during mitosis and meiosis. Most eukaryotes, with the exception of holocentric species, have a single distinct centromere per chromosome, and the presence of multiple centromeres on a single chromosome is predicted to cause breakage and/or loss of that chromosome. However, some stably maintained non-Robertsonian translocated chromosomes have been reported, suggesting that the excessive centromeres are inactivated by an as yet undetermined mechanism.\nWe have developed systems to generate dicentric chromosomes containing two centromeres by fusing two chromosomes in fission yeast. Although the majority of cells harboring the artificial dicentric chromosome are arrested with elongated cell morphology in a manner dependent on the DNA structure checkpoint genes, a portion of the cells survive by converting the dicentric chromosome into a stable functional monocentric chromosome; either centromere was inactivated epigenetically or by DNA rearrangement. Mutations compromising kinetochore formation increased the frequency of epigenetic centromere inactivation. The inactivated centromere is occupied by heterochromatin and frequently reactivated in heterochromatin- or histone deacetylase-deficient mutants.\nChromosomes with multiple centromeres are stabilized by epigenetic centromere inactivation, which is initiated by kinetochore disassembly. Consequent heterochromatinization and histone deacetylation expanding from pericentric repeats to the central domain prevent reactivation of the inactivated centromere.","doi":"10.1016/j.cub.2012.02.062","authors":"Sato H, Masuda F, Takayama Y, Takahashi K, Saitoh S","authors_abbrev":"Sato H et al.","pubmed_publication_date":"24 Apr 2012","pubmed_entrez_date":"2012-04-03","publication_year":"2012","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17347150","title":"Interaction between heat shock transcription factors (HSFs) and divergent binding sequences: binding specificities of yeast HSFs and human HSF1.","citation":"J Biol Chem 2007 May 04;282(18):13334-41","abstract":"The target genes of the heat shock transcription factor (HSF) contain a cis-acting sequence, the heat shock element (HSE), which consists of multiple inverted repeats of the sequence 5'-nGAAn-3'. Using data acquired in this and a previous study, we have identified the HSEs in 59 of 62 target genes of Saccharomyces cerevisiae Hsf1. The Hsf1 protein recognizes continuous and discontinuous repeats of the nGAAn unit; the nucleotide sequences and configuration of the units diverge slightly among functional HSEs. When Schizosaccharomyces pombe HSF was expressed in S. cerevisiae cells, heat shock induced S. pombe HSF to bind to various HSE types, which properly activated transcription from almost all target genes, suggesting that the S. pombe genome also contains divergent HSEs. Human HSF1 induced the heat shock response via HSEs with continuous units in S. cerevisiae cells but failed to do so via HSEs with discontinuous units. Binding of human HSF1 to the discontinuous type of HSE was observed in vitro but was significantly inhibited in vivo. These results show that human HSF1 recognizes HSEs in a slightly different way than yeast HSFs and suggest that the configuration of the unit is an important determinant for HSF-HSE interactions.","authors":"Sakurai H, Takemori Y","authors_abbrev":"Sakurai H et al.","pubmed_publication_date":"04 May 2007","pubmed_entrez_date":"2007-03-10","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2E12.02"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"EMBL:AU011009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18312697","title":"Essential and distinct roles of the F-box and helicase domains of Fbh1 in DNA damage repair.","citation":"BMC Mol Biol 2008 Mar 03;9:27","abstract":"DNA double-strand breaks (DSBs) are induced by exogenous insults such as ionizing radiation and chemical exposure, and they can also arise as a consequence of stalled or collapsed DNA replication forks. Failure to repair DSBs can lead to genomic instability or cell death and cancer in higher eukaryotes. The Schizosaccharomyces pombe fbh1 gene encodes an F-box DNA helicase previously described to play a role in the Rhp51 (an orthologue of S. cerevisiae RAD51)-dependent recombinational repair of DSBs. Fbh1 fused to GFP localizes to discrete nuclear foci following DNA damage.\nTo determine the functional roles of the highly conserved F-box and helicase domains, we have characterized fbh1 mutants carrying specific mutations in these domains. We show that the F-box mutation fbh1-fb disturbs the nuclear localization of Fbh1, conferring an fbh1 null-like phenotype. Moreover, nuclear foci do not form in fbh1-fb cells with DNA damage even if Fbh1-fb is targeted to the nucleus by fusion to a nuclear localization signal sequence. In contrast, the helicase mutation fbh1-hl causes the accumulation of Fbh1 foci irrespective of the presence of DNA damage and confers damage sensitivity greater than that conferred by the null allele. Additional mutation of the F-box alleviates the hypermorphic phenotype of the fbh1-hl mutant.\nThese results suggest that the F-box and DNA helicase domains play indispensable but distinct roles in Fbh1 function. Assembly of the SCFFbh1 complex is required for both the nuclear localization and DNA damage-induced focus formation of Fbh1 and is therefore prerequisite for the Fbh1 recombination function.","doi":"10.1186/1471-2199-9-27","authors":"Sakaguchi C, Morishita T, Shinagawa H, Hishida T","authors_abbrev":"Sakaguchi C et al.","pubmed_publication_date":"03 Mar 2008","pubmed_entrez_date":"2008-03-04","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.01","SPBC409.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:22608712","title":"The contribution of CLIP2 haploinsufficiency to the clinical manifestations of the Williams-Beuren syndrome.","citation":"Am J Hum Genet 2012 Jun 08;90(6):1071-8","abstract":"Williams-Beuren syndrome is a rare contiguous gene syndrome, characterized by intellectual disability, facial dysmorphisms, connective-tissue abnormalities, cardiac defects, structural brain abnormalities, and transient infantile hypercalcemia. Genes lying telomeric to RFC2, including CLIP2, GTF2I and GTF2IRD1, are currently thought to be the most likely major contributors to the typical Williams syndrome cognitive profile, characterized by a better-than-expected auditory rote-memory ability, a relative sparing of language capabilities, and a severe visual-spatial constructive impairment. Atypical deletions in the region have helped to establish genotype-phenotype correlations. So far, however, hardly any deletions affecting only a single gene in the disease region have been described. We present here two healthy siblings with a pure, hemizygous deletion of CLIP2. A putative role in the cognitive and behavioral abnormalities seen in Williams-Beuren patients has been suggested for this gene on the basis of observations in a knock-out mouse model. The presented siblings did not show any of the clinical features associated with the syndrome. Cognitive testing showed an average IQ for both and no indication of the Williams syndrome cognitive profile. This shows that CLIP2 haploinsufficiency by itself does not lead to the physical or cognitive characteristics of the Williams-Beuren syndrome, nor does it lead to the Williams syndrome cognitive profile. Although contribution of CLIP2 to the phenotype cannot be excluded when it is deleted in combination with other genes, our results support the hypothesis that GTF2IRD1 and GTF2I are the main genes causing the cognitive defects associated with Williams-Beuren syndrome.","doi":"10.1016/j.ajhg.2012.04.020","authors":"Vandeweyer G, Van der Aa N, Reyniers E, Kooy RF","authors_abbrev":"Vandeweyer G et al.","pubmed_publication_date":"08 Jun 2012","pubmed_entrez_date":"2012-05-22","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.12"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:843164","title":"Selective spore survival during replica-plating of fission yeast.","citation":"Arch Microbiol 1977 Feb 04;112(1):109-10","abstract":"Vegetative cells of Schizosaccharomyces pombe, upon exposure to acetone vapours, are inactivated at a faster rate than ascospores of this yeast. This observation has been used to develop a simple and fast method by which colonies can be replica-plated and only spores survive in the replicas. The colony patterns are exposed to acetone while still on the velvet used for replica-plating.","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"04 Feb 1977","pubmed_entrez_date":"1977-02-04","publication_year":"1977","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18756382","title":"TOR signaling in fission yeast.","citation":"Crit Rev Biochem Mol Biol 2008;43(4):277-83","abstract":"Fission yeast has two TOR kinases, Tor1 and Tor2. Recent studies have indicated that this microbe has a TSC/Rheb/TOR pathway like higher eukaryotes. Two TOR complexes, namely TORC1 and TORC2, have been identified in this yeast, as in budding yeast and mammals. Fission yeast TORC1, which contains Tor2, and TORC2, which contains Tor1, apparently have opposite functions with regard to the promotion of G1 arrest and sexual development. Rapamycin does not inhibit growth of wild-type fission yeast cells, unlike other eukaryotic cells, but precise analyses have revealed that rapamycin affects certain cellular functions involving TOR in this yeast. It appears that fission yeast has a potential to be an ideal model system to investigate the TOR signaling pathways.","doi":"10.1080/10409230802254911","authors":"Otsubo Y, Yamamato M","authors_abbrev":"Otsubo Y et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-08-30","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32341083","title":"Active Replication Checkpoint Drives Genome Instability in Fission Yeast  mcm4  Mutant.","citation":"Mol Cell Biol 2020 Jun 29;40(14)","abstract":"Upon replication fork arrest, the replication checkpoint kinase Cds1 is stimulated to preserve genome integrity. Robust activation of Cds1 in response to hydroxyurea prevents the endonuclease Mus81 from cleaving the stalled replication fork inappropriately. However, we find that the response is different in temperature-sensitive  mcm4  mutants, affecting a subunit of the MCM replicative helicase. We show that Cds1 inhibition of Mus81 promotes genomic instability and allows  mcm4-dg  cells to evade cell cycle arrest. Cds1 regulation of Mus81 activity also contributes to the formation of the replication stress-induced DNA damage markers replication protein A (RPA) and Ku. These results identify a surprising role for Cds1 in driving DNA damage and disrupted chromosomal segregation under certain conditions of replication stress.","doi":"10.1128/MCB.00033-20","authors":"Kim SM, Forsburg SL","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"29 Jun 2020","pubmed_entrez_date":"2020-04-29","publication_year":"2020","canto_session_key":"20a419e583ad61e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Seong Min Kim","canto_first_approved_date":"2020-05-28 16:33:34","canto_approved_date":"2021-11-08 16:43:42","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-05-18 19:43:04","canto_added_date":"2020-04-30 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":60,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Seong Min Kim","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPBC29A10.05","SPCC126.02c","SPCC4G3.05c","SPCC1259.13","SPCC18B5.11c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2020-05-28"},{"uniquename":"PMID:19942857","title":"Analysis of small RNA in fission yeast; centromeric siRNAs are potentially generated through a structured RNA.","citation":"EMBO J 2009 Dec 16;28(24):3832-44","abstract":"The formation of heterochromatin at the centromeres in fission yeast depends on transcription of the outer repeats. These transcripts are processed into siRNAs that target homologous loci for heterochromatin formation. Here, high throughput sequencing of small RNA provides a comprehensive analysis of centromere-derived small RNAs. We found that the centromeric small RNAs are Dcr1 dependent, carry 5'-monophosphates and are associated with Ago1. The majority of centromeric small RNAs originate from two remarkably well-conserved sequences that are present in all centromeres. The high degree of similarity suggests that this non-coding sequence in itself may be of importance. Consistent with this, secondary structure-probing experiments indicate that this centromeric RNA is partially double-stranded and is processed by Dicer in vitro. We further demonstrate the existence of small centromeric RNA in rdp1Delta cells. Our data suggest a pathway for siRNA generation that is distinct from the well-documented model involving RITS/RDRC. We propose that primary transcripts fold into hairpin-like structures that may be processed by Dcr1 into siRNAs, and that these siRNAs may initiate heterochromatin formation independent of RDRC activity.","doi":"10.1038/emboj.2009.351","authors":"Djupedal I, Kos-Braun IC, Mosher RA, Söderholm N, Simmer F, Hardcastle TJ, Fender A, Heidrich N, Kagansky A, Bayne E, Wagner EG, Baulcombe DC, Allshire RC, Ekwall K","authors_abbrev":"Djupedal I et al.","pubmed_publication_date":"16 Dec 2009","pubmed_entrez_date":"2009-11-28","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5878305","title":"Investigations on reversions to methionine independence induced by mutagens in Schizosaccharomyces pombe.","citation":"Mutat Res 1965 Aug;2(4):312-9","abstract":"","authors":"Loprieno N, Clarke CH","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"Aug 1965","pubmed_entrez_date":"1965-08-01","publication_year":"1965","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18562692","title":"Latrunculin A delays anaphase onset in fission yeast by disrupting an Ase1-independent pathway controlling mitotic spindle stability.","citation":"Mol Biol Cell 2008 Sep;19(9):3713-23","abstract":"It has been proposed previously that latrunculin A, an inhibitor of actin polymerization, delays the onset of anaphase by causing spindle misorientation in fission yeast. However, we show that Delta mto1 cells, which are defective in nucleation of cytoplasmic microtubules, have profoundly misoriented spindles but are not delayed in the timing of sister chromatid separation, providing compelling evidence that fission yeast does not possess a spindle orientation checkpoint. Instead, we show that latrunculin A delays anaphase onset by disrupting interpolar microtubule stability. This effect is abolished in a latrunculin A-insensitive actin mutant and exacerbated in cells lacking Ase1, which cross-links antiparallel interpolar microtubules at the spindle midzone both before and after anaphase. These data indicate that both Ase1 and an intact actin cytoskeleton are required for preanaphase spindle stability. Finally, we show that loss of Ase1 activates a checkpoint that requires only the Mad3, Bub1, and Mph1, but not Mad1, Mad2, or Bub3 checkpoint proteins.","authors":"Meadows JC, Millar J","authors_abbrev":"Meadows JC et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-06-20","publication_year":"2008","canto_session_key":"c9f65982114faaaa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-02-08 10:10:41","canto_approved_date":"2024-07-15 10:47:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-18 09:46:20","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":16,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPBC32H8.12c","SPBC20F10.06","SPAPB1A10.09","SPCC1795.01c","SPCC1322.12c","SPBC106.01","SPCC417.07c","SPBC29B5.01","SPBC3D6.04c","SPAC23H3.08c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2023-02-08"},{"uniquename":"PMID:25956076","title":"Diversity in the organization of centromeric chromatin.","citation":"Curr Opin Genet Dev 2015 Apr;31:28-35","abstract":"Centromeric chromatin is distinguished primarily by nucleosomes containing the histone variant cenH3, which organizes the kinetochore that links the chromosome to the spindle apparatus. Whereas budding yeast have simple 'point' centromeres with single cenH3 nucleosomes, and fission yeast have 'regional' centromeres without obvious sequence specificity, the centromeres of most organisms are embedded in highly repetitive 'satellite' DNA. Recent studies have revealed a remarkable diversity in centromere chromatin organization among different lineages, including some that have lost cenH3 altogether. We review recent progress in understanding point, regional and satellite centromeres, as well as less well-studied centromere types, such as holocentromeres. We also discuss the formation of neocentromeres, the role of pericentric heterochromatin, and the structure and composition of the cenH3 nucleosome.","doi":"10.1016/j.gde.2015.03.010","authors":"Steiner FA, Henikoff S","authors_abbrev":"Steiner FA et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-05-10","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-05-11 00:19:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21723825","title":"Cofilin-linked changes in actin filament flexibility promote severing.","citation":"Biophys J 2011 Jul 06;101(1):151-9","abstract":"The actin regulatory protein, cofilin, increases the bending and twisting elasticity of actin filaments and severs them. It has been proposed that filaments partially decorated with cofilin accumulate stress from thermally driven shape fluctuations at bare (stiff) and decorated (compliant) boundaries, thereby promoting severing. This mechanics-based severing model predicts that changes in actin filament compliance due to cofilin binding affect severing activity. Here, we test this prediction by evaluating how the severing activities of vertebrate and yeast cofilactin scale with the flexural rigidities determined from analysis of shape fluctuations. Yeast actin filaments are more compliant in bending than vertebrate actin filaments. Severing activities of cofilactin isoforms correlate with changes in filament flexibility. Vertebrate cofilin binds but does not increase the yeast actin filament flexibility, and does not sever them. Imaging of filament thermal fluctuations reveals that severing events are associated with local bending and fragmentation when deformations attain a critical angle. The critical severing angle at boundaries between bare and cofilin-decorated segments is smaller than in bare or fully decorated filaments. These measurements support a cofilin-severing mechanism in which mechanical asymmetry promotes local stress accumulation and fragmentation at boundaries of bare and cofilin-decorated segments, analogous to failure of some nonprotein materials.","doi":"10.1016/j.bpj.2011.05.049","authors":"McCullough BR, Grintsevich EE, Chen CK, Kang H, Hutchison AL, Henn A, Cao W, Suarez C, Martiel JL, Blanchoin L, Reisler E, De La Cruz EM","authors_abbrev":"McCullough BR et al.","pubmed_publication_date":"06 Jul 2011","pubmed_entrez_date":"2011-07-05","publication_year":"2011","canto_session_key":"bccce01623a519f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-30 12:19:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-30 12:19:16","canto_added_date":"2016-09-21 00:19:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC20G4.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-09-30"},{"uniquename":"PMID:23874237","title":"Modification of tRNA(Lys) UUU by elongator is essential for efficient translation of stress mRNAs.","citation":"PLoS Genet 2013;9(7):e1003647","abstract":"The Elongator complex, including the histone acetyl transferase Sin3/Elp3, was isolated as an RNA polymerase II-interacting complex, and cells deficient in Elongator subunits display transcriptional defects. However, it has also been shown that Elongator mediates the modification of some tRNAs, modulating translation efficiency. We show here that the fission yeast Sin3/Elp3 is important for oxidative stress survival. The stress transcriptional program, governed by the Sty1-Atf1-Pcr1 pathway, is affected in mutant cells, but not severely. On the contrary, cells lacking Sin3/Elp3 cannot modify the uridine wobble nucleoside of certain tRNAs, and other tRNA modifying activities such as Ctu1-Ctu2 are also essential for normal tolerance to H2O2. In particular, a plasmid over-expressing the tRNA(Lys) UUU complements the stress-related phenotypes of Sin3/Elp3 mutant cells. We have determined that the main H2O2-dependent genes, including those coding for the transcription factors Atf1 and Pcr1, are highly expressed mRNAs containing a biased number of lysine-coding codons AAA versus AAG. Thus, their mRNAs are poorly translated after stress in cells lacking Sin3/Elp3 or Ctu2, whereas a mutated atf1 transcript with AAA-to-AAG lysine codons is efficiently translated in all strain backgrounds. Our study demonstrates that the lack of a functional Elongator complex results in stress phenotypes due to its contribution to tRNA modification and subsequent translation inefficiency of certain stress-induced, highly expressed mRNAs. These results suggest that the transcriptional defects of these strain backgrounds may be a secondary consequence of the deficient expression of a transcription factor, Atf1-Pcr1, and other components of the transcriptional machinery.","doi":"10.1371/journal.pgen.1003647","authors":"Fernández-Vázquez J, Vargas-Pérez I, Sansó M, Buhne K, Carmona M, Paulo E, Hermand D, Rodríguez-Gabriel M, Ayté J, Leidel S, Hidalgo E","authors_abbrev":"Fernández-Vázquez J et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-23","publication_year":"2013","canto_session_key":"94edce7baeb65d9d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elena Hidalgo","canto_first_approved_date":"2014-03-20 15:26:54","canto_approved_date":"2025-10-26 09:00:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-05 12:36:59","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Elena Hidalgo","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2G5.03","SPATRNALYS.03","SPCC757.07c","SPBC32F12.03c","SPAC1952.05","SPBC106.02c","SPBC800.03","SPAC30.02c","SPBTRNALYS.06","SPATRNALYS.02","SPATRNAGLU.02","SPBC36.07","SPBC29B5.01","SPCC11E10.06c","SPAC24B11.06c","SPBTRNAGLN.02","SPAP8A3.04c","SPAC29A4.20","SPBC19C2.13c","SPAC21E11.03c","SPBC215.05"],"gene_count":21,"ltp_gene_count":13,"approved_date":"2014-03-20"},{"uniquename":"PMID:10463156","title":"Restoration of inositol prototrophy in the fission yeast Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 1999 Aug;145 ( Pt 8):1903-1910","abstract":"The biosynthesis of inositol requires only two enzymes, inositol-1-phosphate synthase (encoded by INO1) and an inositol monophosphatase, but the regulation of inositol biosynthesis is under multiple controls and is exquisitely regulated. In the budding yeast Saccharomyces cerevisiae, mutations in any of 26 different genes lead to inositol auxotrophy. The fission yeast Schizosaccharomyces pombe, however, is a natural inositol auxotroph. An investigation has been initiated to examine the possible reasons that might have led to inositol auxotrophy in Sch. pombe. Complementation with a genomic library of an inositol prototrophic yeast indicated that a Pichia pastoris INO1 gene alone could confer inositol prototrophy to Sch. pombe and that the gene was absent in Sch. pombe. To investigate possible reasons for the loss of INO1 gene in Sch. pombe, an attempt was made to disrupt inositol homeostasis in Sch. pombe by overproduction of intracellular inositol, but this did not lead to any discernible adverse effects. The sources of inositol in the natural environment of Sch. pombe were also examined. As the natural environment of Sch. pombe contains significant amounts of phytic acid (inositol hexaphosphate), an investigation was carried out and it was discovered that Sch. pombe can utilize phytic acid as a source of inositol under very specific conditions.","doi":"10.1099/13500872-145-8-1903","authors":"Ingavale SS, Bachhawat AK","authors_abbrev":"Ingavale SS et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-08-27","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25348260","title":"Kinesin-14 and kinesin-5 antagonistically regulate microtubule nucleation by γ-TuRC in yeast and human cells.","citation":"Nat Commun 2014 Oct 28;5:5339","abstract":"Bipolar spindle assembly is a critical control point for initiation of mitosis through nucleation and organization of spindle microtubules and is regulated by kinesin-like proteins. In fission yeast, the kinesin-14 Pkl1 binds the γ-tubulin ring complex (γ-TuRC) microtubule-organizing centre at spindle poles and can alter its structure and function. Here we show that kinesin-14 blocks microtubule nucleation in yeast and reveal that this inhibition is countered by the kinesin-5 protein, Cut7. Furthermore, we demonstrate that Cut7 binding to γ-TuRC and the Cut7 BimC domain are both required for inhibition of Pkl1. We also demonstrate that a yeast kinesin-14 peptide blocks microtubule nucleation in two human breast cancer cell lines, suggesting that this mechanism is evolutionarily conserved. In conclusion, using genetic, biochemical and cell biology approaches we uncover antagonistic control of microtubule nucleation at γ-TuRC by two kinesin-like proteins, which may represent an attractive anti-mitotic target for cancer therapies.","doi":"10.1038/ncomms6339","authors":"Olmsted ZT, Colliver AG, Riehlman TD, Paluh JL","authors_abbrev":"Olmsted ZT et al.","pubmed_publication_date":"28 Oct 2014","pubmed_entrez_date":"2014-10-29","publication_year":"2014","canto_session_key":"5d43b3c8107ba0de","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2023-09-25 12:58:34","canto_approved_date":"2024-04-04 09:22:16","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-09-25 12:57:55","canto_added_date":"2014-10-30 01:15:26","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":10,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.15","SPAC25G10.07c","SPAC3A11.14c","SPBC32F12.04"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2023-09-25"},{"uniquename":"PMID:34169534","title":"Molecular and structural mechanisms of ZZ domain-mediated cargo selection by Nbr1.","citation":"EMBO J 2021 Aug 02;40(15):e107497","abstract":"In selective autophagy, cargo selectivity is determined by autophagy receptors. However, it remains scarcely understood how autophagy receptors recognize specific protein cargos. In the fission yeast Schizosaccharomyces pombe, a selective autophagy pathway termed Nbr1-mediated vacuolar targeting (NVT) employs Nbr1, an autophagy receptor conserved across eukaryotes including humans, to target cytosolic hydrolases into the vacuole. Here, we identify two new NVT cargos, the mannosidase Ams1 and the aminopeptidase Ape4, that bind competitively to the first ZZ domain of Nbr1 (Nbr1-ZZ1). High-resolution cryo-EM analyses reveal how a single ZZ domain recognizes two distinct protein cargos. Nbr1-ZZ1 not only recognizes the N-termini of cargos via a conserved acidic pocket, similar to other characterized ZZ domains, but also engages additional parts of cargos in a cargo-specific manner. Our findings unveil a single-domain bispecific mechanism of autophagy cargo recognition, elucidate its underlying structural basis, and expand the understanding of ZZ domain-mediated protein-protein interactions.","doi":"10.15252/embj.2020107497","authors":"Wang YY, Zhang J, Liu XM, Li Y, Sui J, Dong MQ, Ye K, Du LL","authors_abbrev":"Wang YY et al.","pubmed_publication_date":"02 Aug 2021","pubmed_entrez_date":"2021-06-25","publication_year":"2021","canto_session_key":"338df954e1fab0ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li-Lin Du","canto_first_approved_date":"2021-07-27 14:16:16","canto_approved_date":"2021-07-27 15:12:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-07-18 09:12:14","canto_added_date":"2021-06-30 00:15:04","annotation_curators":[{"name":"Li-Lin Du","community_curator":true,"annotation_count":21,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC513.05","SPBC1921.05","SPBP35G2.11c","SPCC1322.05c","SPAC19A8.05c","SPAC4F10.02"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2021-07-27","pdb_entries":[{"pdb_id":"7dde","gene_chains":[{"gene_uniquename":"SPAC4F10.02","chain":"A/A/C/C/E/E/G/G/I/I/K/K/M/M/O/O/Q/Q/S/S/V/V/X/X","position":"7-473"},{"gene_uniquename":"SPBP35G2.11c","chain":"A/A/C/C/E/E/G/G/I/I/K/K/M/M/O/O/Q/Q/S/S/V/V/X/X","position":"53-129"}],"title":"Cryo-EM structure of the Ape4 and Nbr1 complex","entry_authors":"Zhang J,Ye K","entry_authors_abbrev":"Zhang J et al.","reference_uniquename":"PMID:34169534","experimental_method":"EM","resolution":"2.26"},{"pdb_id":"7dd9","gene_chains":[{"gene_uniquename":"SPBP35G2.11c","chain":"A/A/C/C/E/E/G/G","position":"53-180"},{"gene_uniquename":"SPAC513.05","chain":"A/A/C/C/E/E/G/G","position":"1-1077"}],"title":"Cryo-EM structure of the Ams1 and Nbr1 complex","entry_authors":"Zhang J,Ye K","entry_authors_abbrev":"Zhang J et al.","reference_uniquename":"PMID:34169534","experimental_method":"EM","resolution":"2.4"}]},{"uniquename":"PMID:26746798","title":"Inner nuclear membrane protein Lem2 facilitates Rad3-mediated checkpoint signaling under replication stress induced by nucleotide depletion in fission yeast.","citation":"Cell Signal 2016 Apr;28(4):235-45","abstract":"DNA replication checkpoint is a highly conserved cellular signaling pathway critical for maintaining genome integrity in eukaryotes. It is activated when DNA replication is perturbed. In Schizosaccharomyces pombe, perturbed replication forks activate the sensor kinase Rad3 (ATR/Mec1), which works cooperatively with mediator Mrc1 and the 9-1-1 checkpoint clamp to phosphorylate the effector kinase Cds1 (CHK2/Rad53). Phosphorylation of Cds1 promotes autoactivation of the kinase. Activated Cds1 diffuses away from the forks and stimulates most of the checkpoint responses under replication stress. Although this signaling pathway has been well understood in fission yeast, how the signaling is initiated and thus regulated remains incompletely understood. Previous studies have shown that deletion of lem2(+) sensitizes cells to the inhibitor of ribonucleotide reductase, hydroxyurea. However, the underlying mechanism is still not well understood. This study shows that in the presence of hydroxyurea, Lem2 facilitates Rad3-mediated checkpoint signaling for Cds1 activation. Without Lem2, all known Rad3-dependent phosphorylations critical for replication checkpoint signaling are seriously compromised, which likely causes the aberrant mitosis and drug sensitivity observed in this mutant. Interestingly, the mutant is not very sensitive to DNA damage and the DNA damage checkpoint remains largely intact, suggesting that the main function of Lem2 is to facilitate checkpoint signaling in response to replication stress. Since Lem2 is an inner nuclear membrane protein, these results also suggest that the replication checkpoint may be spatially regulated inside the nucleus, a previously unknown mechanism.","doi":"10.1016/j.cellsig.2015.12.009","authors":"Xu YJ","authors_abbrev":"Xu YJ","pubmed_publication_date":"Apr 2016","pubmed_entrez_date":"2016-01-10","publication_year":"2016","canto_session_key":"bfe0472c4af56347","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yongjie Xu","canto_first_approved_date":"2017-10-20 17:15:00","canto_approved_date":"2021-10-19 14:53:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-10-19 17:28:12","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yongjie Xu","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c","SPAC18G6.10","SPBC25D12.04","SPBC216.05","SPCC23B6.03c","SPCC18B5.11c","SPAC694.06c","SPCC1259.13"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2017-10-20"},{"uniquename":"PMID:9202173","title":"Osmo-stress-induced changes in neutral trehalase activity of the fission yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1997 Jun 05;1357(1):41-8","abstract":"Exposure of repressed growing cultures of Schizosaccharomyces pombe to various extracellular concentrations of NaCl, sorbitol or glycerol resulted in a reversible increase in neutral trehalase activity which was maintained while the cells were in the presence of high environmental osmolarity. Treatment of osmo-stress-induced trehalase by phosphatase lead to a decreased activity indicating that the active enzyme is phosphorylated. The stress response following the osmotic shock required protein synthesis and was independent of the cAMP-dependent protein kinase pathway. Cells disrupted for wis] or phh1 (identical to sty1 and spc1), which encode members of the mitogen-activated protein kinase (MAPK) cascade, showed that the osmo-stress-induced increase in trehalase markedly diminished. In contrast, the heat shock-induced increase in trehalase remained unchanged in these cells. Taken together, the data suggest that the elevation of trehalase activity in Schiz. pombe under conditions of high osmolarity is due to de novo synthesis of the enzyme and that this process is modulated through a MAPK signal transduction pathway as part of the physiological response to the osmotic stress. The wisl-phhl MAPK cascade, however, does not appear to form part of the mechanism underlaying the increase in trehalase after heat stress.","authors":"Fernández J, Soto T, Vicente-Soler J, Cansado J, Gacto M","authors_abbrev":"Fernández J et al.","pubmed_publication_date":"05 Jun 1997","pubmed_entrez_date":"1997-06-05","publication_year":"1997","canto_session_key":"d0c2d05f4db2d947","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-20 14:31:06","canto_approved_date":"2024-08-20 14:31:06","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-20 14:31:00","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":5,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC24B11.06c","SPBC106.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2024-08-20"},{"uniquename":"PMID:22245228","title":"Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival.","citation":"Mol Cell 2012 Feb 10;45(3):398-408","abstract":"Eukaryotic 2-Cys peroxiredoxins (Prx) are abundant antioxidant enzymes whose thioredoxin peroxidase activity plays an important role in protecting against oxidative stress, aging, and cancer. Paradoxically, this thioredoxin peroxidase activity is highly sensitive to inactivation by peroxide-induced Prx hyperoxidation. However, any possible advantage in preventing Prx from removing peroxides under oxidative stress conditions has remained obscure. Here we demonstrate that, in cells treated with hydrogen peroxide, the Prx Tpx1 is a major substrate for thioredoxin in the fission yeast Schizosaccharomyces pombe and, as such, competitively inhibits thioredoxin-mediated reduction of other oxidized proteins. Consequently, we reveal that the hyperoxidation of Tpx1 is critical to allow thioredoxin to act on other substrates ensuring repair of oxidized proteins and cell survival following exposure to toxic levels of hydrogen peroxide. We conclude that the inactivation of the thioredoxin peroxidase activity of Prx is important to maintain thioredoxin activity and cell viability under oxidative stress conditions.","doi":"10.1016/j.molcel.2011.11.027","authors":"Day AM, Brown JD, Taylor SR, Rand JD, Morgan BA, Veal EA","authors_abbrev":"Day AM et al.","pubmed_publication_date":"10 Feb 2012","pubmed_entrez_date":"2012-01-17","publication_year":"2012","canto_session_key":"7b18cacb1717e352","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-15 11:36:38","canto_approved_date":"2023-03-23 13:55:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-04 09:51:28","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":42,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC7D4.07c","SPBC106.02c","SPAC29E6.05c","SPAC1783.07c","SPCC576.03c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-08-15"},{"uniquename":"PMID:19495005","title":"Vibrationally resonant imaging of a single living cell by supercontinuum-based multiplex coherent anti-Stokes Raman scattering microspectroscopy.","citation":"Opt Express 2005 Feb 21;13(4):1322-7","abstract":"Supercontinuum-based multiplex coherent anti-Stokes Raman scattering (CARS) microspectroscopy has been applied to vibrational imaging of a living fission yeast cell. We have successfully extracted only a vibrationally resonant CARS image from a characteristic spectral profile in the C-H stretching vibrational region. Using our simple but sensitive analysis, the vibrational contrast is significantly improved in comparison with a CARS imaging at a fixed Raman shift. The CARS image of a living yeast cell indicates several areas at which the signal is remarkably strong. They are considered to arise from mitochondria.","authors":"Kano H, Hamaguchi HO","authors_abbrev":"Kano H et al.","pubmed_publication_date":"21 Feb 2005","pubmed_entrez_date":"2009-06-05","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16738311","title":"Fission yeast Cid12 has dual functions in chromosome segregation and checkpoint control.","citation":"Mol Cell Biol 2006 Jun;26(12):4435-47","abstract":"Fission yeast Cid12 is a member of the Cid1 family of specialized poly(A) polymerases. Like cells lacking cid1, cid12Delta mutants were shown to have checkpoint defects when DNA replication was inhibited. Here, we show that Cid12 is also required for faithful chromosome segregation and that mutation of amino acid residues predicted to be essential for poly(A) polymerase activity resulted in loss of Cid12 function in vivo. Cells lacking Cid12 had an increased chromosome segregation failure rate due to precocious loss of sister chromatid cohesion at the centromere but not along the chromosome arms. In keeping with a recently described function for Cid12 in RNA interference (RNAi)-mediated heterochromatin assembly, this was accompanied by an accumulation of polyadenylated transcripts corresponding to naturally silenced repeat elements within heterochromatic domains, with consequent defects in centromeric gene silencing. These cells also suffered increased meiotic defects, and their viability was dependent on the spindle checkpoint protein Bub1. To account for the effects of Cid12 on various aspects of DNA metabolism, including chromosome segregation and the checkpoint control, we suggest that Cid12 has dual functions in RNAi silencing and regulating mRNA stability.","authors":"Win TZ, Stevenson AL, Wang SW","authors_abbrev":"Win TZ et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-06-02","publication_year":"2006","canto_session_key":"995720e27a54ba1b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-09-13 14:05:10","canto_approved_date":"2024-06-28 10:42:42","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-12-23 11:45:45","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":47,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.17","SPCC338.17c","SPBC25H2.13c","SPAC6F12.09","SPAC1952.07","SPBC26H8.07c","SPBC1734.02c","SPCC1322.12c","SPCC663.12","SPAC18G6.02c","SPBC11C11.03","SPCC18B5.11c","SPCC1259.13"],"gene_count":13,"ltp_gene_count":10,"approved_date":"2016-09-13"},{"uniquename":"PMID:16341225","title":"Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe.","citation":"Nat Struct Mol Biol 2006 Jan;13(1):63-70","abstract":"Decapping is a key step in both general and nonsense-mediated 5' --> 3' mRNA-decay pathways. Removal of the cap structure is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of a C-terminally truncated Schizosaccharomyces pombe Dcp2p reveals two distinct domains: an all-helical N-terminal domain and a C-terminal domain that is a classic Nudix fold. The C-terminal domain of both Saccharomyces cerevisiae and S. pombe Dcp2p proteins is sufficient for decapping activity, although the N-terminal domain can affect the efficiency of Dcp2p function. The binding of Dcp2p to Dcp1p is mediated by a conserved surface on its N-terminal domain, and the N-terminal domain is required for Dcp1p to stimulate Dcp2p activity. The flexible nature of the N-terminal domain relative to the C-terminal domain suggests that Dcp1p binding to Dcp2p may regulate Dcp2p activity through conformational changes of the two domains.","authors":"She M, Decker CJ, Chen N, Tumati S, Parker R, Song H","authors_abbrev":"She M et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2005-12-13","publication_year":"2006","canto_session_key":"92cda7cb8c6c7a8c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-07 14:44:24","canto_approved_date":"2023-05-17 15:45:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-30 17:46:13","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19A8.12","SPBC3B9.21"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-07","pdb_entries":[{"pdb_id":"2a6t","gene_chains":[{"gene_uniquename":"SPAC19A8.12","chain":"A/B","position":"1-266"}],"title":"Crystal structure of S.pombe mRNA decapping enzyme Dcp2p","entry_authors":"She M,Chen N,Song H","entry_authors_abbrev":"She M et al.","reference_uniquename":"PMID:16341225","experimental_method":"X-ray","resolution":"2.5"}]},{"uniquename":"PMID:11595165","title":"A novel copper-regulated promoter system for expression of heterologous proteins in Schizosaccharomyces pombe.","citation":"Gene 2001 Aug 08;273(2):191-8","abstract":"The increasing use of the fission yeast Schizosaccharomyces pombe as a model organism for elucidating the mechanisms of critical biological processes such as cell-cycle control, DNA replication, and stress-mediated signal transduction has fostered the development and utilization of expression systems for gene function analysis. Using the promoter of the ctr4(+) copper transporter gene from S. pombe, we created a series of vectors, named pctr4(+)-X, which regulate the expression of heterologous genes as a function of copper availability. In this system, the addition of copper ions at levels that are non-toxic to yeast cells represses gene expression, while copper deprivation strongly induces gene expression. Conveniently, changes of growth medium or carbon sources are not required to shut down or induce gene expression. The Cu-starvation-mediated inducible expression system is rapid, producing heterologous proteins within 3 h, with sustained expression of proteins that persists for several hours. The pctr4(+)-X expression vectors harbor unique restriction sites constructed in-frame to DNA sequences encoding for epitope tags, which facilitate the detection or purification of the heterologous proteins using commercially available antibodies and affinity columns. Furthermore, the pctr4(+)-X copper-regulatable protein expression vectors have been constructed with three different selectable markers, offering more versatility for studying gene function in fission yeast.","authors":"Bellemare DR, Sanschagrin M, Beaudoin J, Labbé S","authors_abbrev":"Bellemare DR et al.","pubmed_publication_date":"08 Aug 2001","pubmed_entrez_date":"2001-10-12","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11335037","title":"Establishment of a cellular axis in fission yeast.","citation":"Trends Genet 2001 May;17(5):273-8","abstract":"Recent studies in fission yeast Schizosaccharomyces pombe reveal how cells establish a cellular axis that specifies domains as the functional 'ends' and 'middle' of the cell. During interphase, dynamic microtubules position the nucleus at the middle of the cell and orientate microtubule 'plus' ends towards the ends of the cell. At the cell ends, the microtubule plus ends might establish a zone of polarized cell growth and actin assembly by depositing factors such as Tea1p. At the cell middle, the nucleus might specify the position of the actin contractile ring and the future cell division site by positioning cytokinesis factors such as Mid1p.","authors":"Chang F","authors_abbrev":"Chang F","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-04","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30155942","title":"Sfh1, an essential component of the RSC chromatin remodeling complex, maintains genome integrity in fission yeast.","citation":"Genes Cells 2018 Sep;23(9):738-752","abstract":"Abp1 is a fission yeast CENP-B homologue that contributes to centromere function, silencing at pericentromeric heterochromatin and silencing of retrotransposons. We identified the sfh1 gene, encoding a core subunit of the fission yeast chromatin remodeling complex RSC as an Abp1-interacting protein. Because sfh1 is essential for growth, we isolated temperature-sensitive sfh1 mutants. These mutants showed defects in centromere functions, reflected by sensitivity to an inhibitor of spindle formation and minichromosome instability. Sfh1 localized at both kinetochore and pericentromeric heterochromatin regions. Although sfh1 mutations had minor effect on silencing at these regions, they decreased the levels of cohesin on centromeric heterochromatin. Sfh1 also localized at a retrotransposon, Tf2, in a partly Abp1-dependent manner, and assisted in silencing of Tf2 by Abp1 probably in the same pathway as a histone chaperon, HIRA, which is also known to involve in Tf2 repression. Furthermore, sfh1 mutants were sensitive to several DNA-damaging treatments (HU, MMS, UV and X-ray). Increase in spontaneous foci of Rad22, a recombination Mediator protein Rad52 homologue, in sfh1 mutant suggests that RSC functions in homologous recombination repair of double-stranded break downstream of the Rad22 recruitment. These results indicate that RSC plays multiple roles in the maintenance of genome integrity.","doi":"10.1111/gtc.12629","authors":"Kotomura N, Tsunemine S, Kuragano M, Asanuma T, Nakagawa H, Tanaka K, Murakami Y","authors_abbrev":"Kotomura N et al.","pubmed_publication_date":"Sep 2018","pubmed_entrez_date":"2018-08-30","publication_year":"2018","canto_session_key":"9f41c25a49997c0e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Satoru Tsunemine","canto_first_approved_date":"2025-09-29 09:43:05","canto_approved_date":"2025-09-30 06:55:23","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-08-14 18:18:42","canto_added_date":"2018-08-31 00:15:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":9,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Satoru Tsunemine","community_curator":true,"annotation_count":69,"orcid":"0000-0001-5225-7156","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPBC1105.04c","SPAC30D11.10","SPCC16A11.14","SPBC32H8.12c","SPBC31F10.13c"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2025-09-29"},{"uniquename":"PMID:1963809","title":"Use of the Tn903 neomycin-resistance gene for promoter analysis in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1990 Dec;18(6):511-6","abstract":"The bacterial neo gene from transposon Tn903 (Tn601) was used for dominant transformation of the fission yeast Schizosaccharomyces pombe. It was found that high transformation efficiency was dependent on a high level of promoter activity, mediated by the strong promoter of the Schizosaccharomyces pombe alcohol dehydrogenase gene (adh1), as shown by comparing the efficiency of transformation to G418-resistance, the resistance levels of transformed cells, and the in vitro amino-glycoside phosphotransferase activity. On the other hand, the heterologous promoter of the Saccharomyces cerevisiae alcohol dehydrogenase I gene (adc1) is shown to be a weak promoter in Schizosaccharomyces pombe, though its activity is significantly enhanced in cells grown on glycerol as a carbon source. This system for selection and detection of promoter-active sequences may provide a useful basis for the analysis of promoter elements in fission yeast.","authors":"Lang-Hinrichs C, Dössereck C, Fath I, Stahl U","authors_abbrev":"Lang-Hinrichs C et al.","pubmed_publication_date":"Dec 1990","pubmed_entrez_date":"1990-12-01","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20178743","title":"Dicer-independent primal RNAs trigger RNAi and heterochromatin formation.","citation":"Cell 2010 Feb 19;140(4):504-16","abstract":"Assembly of fission yeast pericentromeric heterochromatin and generation of small interfering RNAs (siRNAs) from noncoding centromeric transcripts are mutually dependent processes. How this interdependent positive feedback loop is first triggered is a fundamental unanswered question. Here, we show that two distinct Argonaute (Ago1)-dependent pathways mediate small RNA generation. RNA-dependent RNA polymerase complex (RDRC) and Dicer act on specific noncoding RNAs to generate siRNAs by a mechanism that requires the slicer activity of Ago1 but is independent of pre-existing heterochromatin. In the absence of RDRC or Dicer, a distinct class of small RNAs, called primal small RNAs (priRNAs), associates with Ago1. priRNAs are degradation products of abundant transcripts, which bind to Ago1 and target antisense transcripts that result from bidirectional transcription of DNA repeats. Our results suggest that a transcriptome surveillance mechanism based on random association of RNA degradation products with Argonaute triggers siRNA amplification and heterochromatin assembly within DNA repeats.","doi":"10.1016/j.cell.2010.01.019","authors":"Halic M, Moazed D","authors_abbrev":"Halic M et al.","pubmed_publication_date":"19 Feb 2010","pubmed_entrez_date":"2010-02-25","publication_year":"2010","canto_session_key":"76dce1150495eda7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-11-19 16:13:09","canto_approved_date":"2024-11-19 16:13:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-11-19 16:13:03","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":42,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.08","SPCC663.12","SPBC428.08c","SPAC12G12.13c","SPAC664.01c","SPCC188.13c","SPBC26H8.10","SPBC83.03c","SPAC18G6.02c","SPAC140.03","SPCC736.11","SPAC13G7.07","SPAC1F3.01","SPAC6F12.09"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2024-11-19"},{"uniquename":"PMID:18481973","title":"Progress towards understanding the mechanism of cytokinesis in fission yeast.","citation":"Biochem Soc Trans 2008 Jun;36(Pt 3):425-30","abstract":"We use fission yeast to study the molecular mechanism of cytokinesis. We benefit from a long history in genetic analysis of the cell cycle in fission yeast, which provided the most complete inventory of cytokinesis proteins. We used fluorescence microscopy of proteins tagged with fluorescent proteins to establish the temporal and spatial pathway for the assembly and constriction of the contractile ring. We combined biochemical analysis of purified proteins (myosin-II, profilin, formin Cdc12p and cofilin), observations of fluorescent fusion proteins in live cells and mathematical modelling to formulate and test a simple hypothesis for the assembly of the contractile ring. This model involves the formation of 65 nodes containing myosin-II and formin Cdc12p around the equator of the cell. As a cell enters anaphase, actin filaments grow from formin Cdc12p in these nodes. Myosin captures actin filaments from adjacent nodes and pulls intermittently to condense the nodes into a contractile ring.","doi":"10.1042/BST0360425","authors":"Pollard TD","authors_abbrev":"Pollard TD","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-05-17","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12501333","title":"Induction of sexual co-flocculation of heterothallic fission yeast (Schizosaccharomyces pombe) cells by mating pheromones.","citation":"J Gen Appl Microbiol 1997 Jun;43(3):169-174","abstract":"Heterothallic fission yeast (Schizosaccharomyces pombe) cells preincubated with sex pheromone, P- or M-factor of the obverse mating-type cells, in mannose synthetic medium (MSM) results in remarkably increased sexual co-flocculation with obverse mating-type cells almost without time lag, i.e., within 10 min. By contrast, comparable flocculation requires over 1 h if untreated control cells are mixed with obverse mating-type cells. The agglutinin of P cells is more inducible than that of M cells. These pheromonal inductions of sexual co-flocculation are inhibited by the addition of cycloheximide or tunicamycin during preincubation but not by chloramphenicol or hydroxyurea. These results demonstrate that, in addition to (a) the repression of cell division (G1 arrest) and (b) the activation of cell wall autolytic processes (mating-specific elongation of cells: formation of their conjugation tubes), mating pheromones of fission yeast have another important role; (c) to induce sexual co-flocculation (agglutinability). Using our experimental system of preincubation with sexual pheromones, we show that M-agglutinin is heat-stable and its induction is inhibited by tunicamycin, but that P-agglutinin is heat-labile and its induction is only partially inhibited by tunicamycin.","authors":"Miyata M, Matsuoka M, Inada T","authors_abbrev":"Miyata M et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"02662a5f9bd3c604","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-06 11:55:22","canto_approved_date":"2020-12-03 15:46:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-27 12:37:43","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC513.03","SPAPB8E5.05","SPBPJ4664.03","SPCC1795.06"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-02-06"},{"uniquename":"EMBL:AU010387","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23813957","title":"The fission yeast β-arrestin-like protein Any1 is involved in TSC-Rheb signaling and the regulation of amino acid transporters.","citation":"J Cell Sci 2013 Sep 01;126(Pt 17):3972-81","abstract":"Rheb GTPase and the Tsc1-Tsc2 protein complex, which serves as a GTPase-activating protein for Rheb, have crucial roles in the regulation of cell growth in response to extracellular conditions. In Schizosaccharomyces pombe, Rheb and Tsc1-Tsc2 regulate cell cycle progression, the onset of meiosis and the uptake of amino acids. In cells lacking Tsc2 (Δtsc2), the amino acid transporter Aat1, which is normally expressed on the plasma membrane under starvation conditions, is confined to the Golgi. Here, we show that the loss of either pub1(+), encoding an E3 ubiquitin ligase, or any1(+), encoding a β-arrestin-like protein, allows constitutive expression of Aat1 on the plasma membrane in Δtsc2 cells, suggesting that Pub1 and Any1 are required for localization of Aat1 to the Golgi. Subsequent analysis revealed that, in the Golgi, Pub1 and Any1 form a complex that ubiquitylates Aat1. Physical interaction of Pub1 and Any1 is more stable in Δtsc2 cells than in wild-type cells and is independent of Tor2 activity. These results indicate that the TSC-Rheb signaling pathway regulates the localization of amino acid transporters via Pub1 and Any1 in a Tor2-independent manner. Our study demonstrates that, unlike in budding yeast (in which Rsp5 and ARTs, a pair of proteins analogous to Pub1 and Any1, respectively, primarily act to reduce expression of the transporters on plasma membrane when nutrients are abundant), the primary role of fission yeast Pub1 and Any1 is to store the transporter in the Golgi under nutrient-rich conditions.","doi":"10.1242/jcs.128355","authors":"Nakase Y, Nakase M, Kashiwazaki J, Murai T, Otsubo Y, Mabuchi I, Yamamoto M, Takegawa K, Matsumoto T","authors_abbrev":"Nakase Y et al.","pubmed_publication_date":"01 Sep 2013","pubmed_entrez_date":"2013-07-02","publication_year":"2013","canto_session_key":"d4ff7f4bbd92e85b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2026-04-07 07:13:00","canto_approved_date":"2026-04-24 13:07:51","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-10-28 11:13:22","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":85,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.04","SPCC584.13","SPAC27D7.03c","SPAC630.13c","SPAC11D3.08c","SPAC11G7.02","SPAPB24D3.02c","SPBC359.03c","SPAC22F3.13","SPBC216.07c","SPBC18H10.20c","SPBC428.16c"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2026-04-07"},{"uniquename":"PMID:20410137","title":"Mug28, a meiosis-specific protein of Schizosaccharomyces pombe, regulates spore wall formation.","citation":"Mol Biol Cell 2010 Jun 15;21(12):1955-67","abstract":"The meiosis-specific mug28(+) gene of Schizosaccharomyces pombe encodes a putative RNA-binding protein with three RNA recognition motifs (RRMs). Live observations of meiotic cells that express Mug28 tagged with green fluorescent protein (GFP) revealed that Mug28 is localized in the cytoplasm, and accumulates around the nucleus from metaphase I to anaphase II. Disruption of mug28(+) generated spores with low viability, due to the aberrant formation of the forespore membrane (FSM). Visualization of the FSM in living cells expressing GFP-tagged Psy1, an FSM protein, indicated that mug28Delta cells harbored abnormal FSMs that contained buds, and had a delayed disappearance of Meu14, a leading edge protein. Electron microscopic observation revealed that FSM formation was abnormal in mug28Delta cells, showing bifurcated spore walls that were thicker than the nonbifurcated spore walls of the wild type. Analysis of Mug28 mutants revealed that RRM3, in particular phenylalanin-466, is of primary importance for the proper localization of Mug28, spore viability, and FSM formation. Together, we conclude that Mug28 is essential for the proper maturation of the FSM and the spore wall.","authors":"Shigehisa A, Okuzaki D, Kasama T, Tohda H, Hirata A, Nojima H","authors_abbrev":"Shigehisa A et al.","pubmed_publication_date":"15 Jun 2010","pubmed_entrez_date":"2010-04-23","publication_year":"2010","canto_session_key":"544dd1cb893ee606","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-16 17:41:46","canto_approved_date":"2024-04-03 15:15:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-03 09:52:39","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.03","SPAC343.07","SPCC1223.12c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-10-16"},{"uniquename":"PMID:21307582","title":"Atg22p, a vacuolar membrane protein involved in the amino acid compartmentalization of Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2011;75(2):385-7","abstract":"The fission yeast Schizosaccharomyces pombe has a homolog of the budding yeast Atg22p, which is involved in spore formation (Mukaiyama H. et al., Microbiology, 155, 3816-3826 (2009)). GFP-tagged Atg22p in the fission yeast was localized to the vacuolar membrane. Upon disruption of atg22, the amino acid levels of the cellular fraction as well as the vacuolar fraction decreased. The uptake of several amino acids, such as lysine, histidine, and arginine, was impaired in atg22Δ cells. S. pombe Atg22p plays an important role in the compartmentalization of amino acids.","authors":"Sugimoto N, Iwaki T, Chardwiriyapreecha S, Shimazu M, Kawano M, Sekito T, Takegawa K, Kakinuma Y","authors_abbrev":"Sugimoto N et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-02-11","publication_year":"2011","canto_session_key":"a8d91f7b56db5cd1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-11-03 10:25:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-03 10:25:01","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":40,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-03"},{"uniquename":"PMID:34303934","title":"Breakers and amplifiers in chromatin circuitry: acetylation and ubiquitination control the heterochromatin machinery.","citation":"Curr Opin Struct Biol 2021 Dec;71:156-163","abstract":"Eukaryotic genomes are segregated into active euchromatic and repressed heterochromatic compartments. Gene regulatory networks, chromosomal structures, and genome integrity rely on the timely and locus-specific establishment of active and silent states to protect the genome and provide the basis for cell division and specification of cellular identity. Here, we focus on the mechanisms and molecular machinery that establish heterochromatin in Schizosaccharomyces pombe and compare it with Saccharomyces cerevisiae and the mammalian polycomb system. We present recent structural and mechanistic evidence, which suggests that histone acetylation protects active transcription by disrupting the positive feedback loops used by the heterochromatin machinery and that H2A and H3 monoubiquitination actively drives heterochromatin, whereas H2B monoubiquitination mobilizes the defenses to quench heterochromatin.","doi":"10.1016/j.sbi.2021.06.012","authors":"Bailey LT, Northall SJ, Schalch T","authors_abbrev":"Bailey LT et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-07-25","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-07-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10572167","title":"Taz1p and Teb1p, two telobox proteins in Schizosaccharomyces pombe, recognize different telomere-related DNA sequences.","citation":"Nucleic Acids Res 1999 Dec 15;27(24):4687-94","abstract":"Band shift assays were used to study proteins from the fission yeast that bind double-stranded telomeric repeat sequences. We also examine general DNA binding properties of the telobox domain, which characterizes telomere-binding proteins from a range of species. We demonstrate that Taz1p has a high affinity for the fission yeast telomeric repeat, consistent with genetic results implicating this protein in telomere maintenance. A second Schizosaccharomyces pombe telobox protein, Teb1p, is shown to bind with high affinity to the vertebrate repeat and with low affinity to the fission yeast telomeric DNA. When tested on G-rich single-stranded telomeric DNA, all these proteins bind with very low affinity, much like the human telomere-binding protein TRF1. Recombinant proteins containing just the telobox domains reproduce the specificity of binding demonstrated for the corresponding full-length proteins, indicating that the telobox domain is indeed responsible for specific DNA recognition. The presence of possible Teb1p-binding sites upstream of many genes suggests a role for this protein as a general transcription factor. Finally, band shift experiments with whole cell extracts from wild-type and taz1 (-)strains suggest that in addition to Taz1p, S.pombe has another major telomere-binding activity.","authors":"Vassetzky NS, Gaden F, Brun C, Gasser SM, Gilson E","authors_abbrev":"Vassetzky NS et al.","pubmed_publication_date":"15 Dec 1999","pubmed_entrez_date":"1999-11-26","publication_year":"1999","canto_session_key":"262e63c803c82332","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-07 10:39:23","canto_approved_date":"2019-06-07 10:39:23","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-06-07 10:39:17","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G7.10","SPAC16A10.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-06-07"},{"uniquename":"PMID:18346214","title":"btn1 affects endocytosis, polarization of sterol-rich membrane domains and polarized growth in Schizosaccharomyces pombe.","citation":"Traffic 2008 Jun;9(6):936-50","abstract":"btn1, the Schizosaccharomyces pombe orthologue of the human Batten disease gene CLN3, exerts multiple cellular effects. As well as a role in vacuole pH homoeostasis, we now show that Btn1p is essential for growth at high temperatures. Its absence results in progressive defects at 37 degrees C that culminate in total depolarized growth and cell lysis. These defects are preceded by a progressive failure to correctly polarize sterol-rich domains after cytokinesis and are accompanied by loss of Myo1p localization. Furthermore, we found that in Sz. pombe, sterol spreading is linked to defective formation/polarization of F-actin patches and disruption of endocytosis and that these processes are aberrant in btn1Delta cells. Consistent with a role for Btn1p in polarized growth, Btn1p has an altered location at 37 degrees C and is retained in actin-dependent endomembrane structures near the cell poles or septum.","doi":"10.1111/j.1600-0854.2008.00735.x","authors":"Codlin S, Haines RL, Mole SE","authors_abbrev":"Codlin S et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-03-19","publication_year":"2008","canto_session_key":"5980fec446cd2efb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-23 14:00:19","canto_approved_date":"2020-01-13 17:23:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-23 14:00:13","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPBC146.13c","SPAC607.09c","SPAC688.11"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-10-23"},{"uniquename":"PMID:27974503","title":"Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast.","citation":"Genetics 2017 Feb;205(2):673-690","abstract":"Despite its biological and medical relevance, traffic from the Golgi to the plasma membrane (PM) is one of the least understood steps of secretion. Exomer is a protein complex that mediates the trafficking of certain cargoes from the trans-Golgi network/early endosomes to the PM in budding yeast. Here, we show that in Schizosaccharomyces pombe the Cfr1 and Bch1 proteins constitute the simplest form of an exomer. Cfr1 co-immunoprecipitates with Assembly Polypeptide adaptor 1 (AP-1), AP-2, and Golgi-localized, gamma-adaptin ear domain homology, ARF-binding (GGA) subunits, and cfr1 +  interacts genetically with AP-1 and GGA genes. Exomer-defective cells exhibit multiple mild defects, including alterations in the morphology of Golgi stacks and the distribution of the synaptobrevin-like Syb1 protein, carboxypeptidase missorting, and stress sensitivity. S. pombe apm1Δ cells exhibit a defect in trafficking through the early endosomes that is severely aggravated in the absence of exomer. apm1Δ cfr1Δ cells exhibit a dramatic disorganization of intracellular compartments, including massive accumulation of electron-dense tubulovesicular structures. While the trans-Golgi network/early endosomes are severely disorganized in the apm1Δ cfr1Δ strain, gga21Δ gga22Δ cfr1Δ cells exhibit a significant disturbance of the prevacuolar/vacuolar compartments. Our findings show that exomer collaborates with clathrin adaptors in trafficking through diverse cellular compartments, and that this collaboration is important to maintain their integrity. These results indicate that the effect of eliminating exomer is more pervasive than that described to date, and suggest that exomer complexes might participate in diverse steps of vesicle transport in other organisms.","doi":"10.1534/genetics.116.193458","authors":"Hoya M, Yanguas F, Moro S, Prescianotto-Baschong C, Doncel C, de León N, Curto MÁ, Spang A, Valdivieso MH","authors_abbrev":"Hoya M et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-12-16","publication_year":"2017","canto_session_key":"725500622fa77149","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Henar Valdivieso","canto_first_approved_date":"2017-01-10 10:20:48","canto_approved_date":"2026-01-29 14:25:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-22 11:20:20","canto_added_date":"2016-12-17 01:15:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":95,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Henar Valdivieso","community_curator":true,"annotation_count":43,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.09c","SPAC22E12.05c","SPAC30.01c","SPAC6G9.11","SPAC6G9.12","SPBC25H2.16c","SPAC458.05","SPBC691.03c","SPBC31F10.16","SPCC1840.02c","SPBC19G7.05c","SPBC1289.01c","SPBC9B6.08","SPAC19B12.03","SPCC1281.01","SPAC688.11","SPBC651.11c","SPAC19A8.05c","SPBC29A10.08","SPAC1071.10c","SPBP16F5.07","SPAC1F3.05","SPAC19G12.10c","SPAC19B12.02c","SPAC1F7.04","SPBC24C6.05","SPBC1709.01"],"gene_count":27,"ltp_gene_count":18,"approved_date":"2017-01-10"},{"uniquename":"PMID:30914423","title":"Isolation of Fission Yeast Condensin Temperature-Sensitive Mutants with Single Amino Acid Substitutions Targeted to Hinge Domain.","citation":"G3 (Bethesda) 2019 May 07;9(5):1777-1783","abstract":"Essential genes cannot be deleted from the genome; therefore, temperature-sensitive (ts) mutants and cold-sensitive (cs) mutants are very useful to discover functions of essential genes in model organisms such as  Schizosaccharomyces pombe  and  Saccharomyces cerevisiae  To isolate ts/cs mutants for essential genes of interest, error-prone mutagenesis (or random mutagenesis) coupled with  in vitro  selection has been widely used. However, this method often introduces multiple silent mutations, in addition to the mutation responsible for ts/cs, with the result that one cannot discern which mutation is responsible for the ts/cs phenotype. In addition, the location of the responsible mutation introduced is random, whereas it is preferable to isolate ts/cs mutants with single amino acid substitutions, located in a targeted motif or domain of the protein of interest. To solve these problems, we have developed a method to isolate ts/cs mutants with single amino acid substitutions in targeted regions using site-directed mutagenesis. This method takes advantage of the empirical fact that single amino acid substitutions (L/S -> P or G/A -> E/D) often cause ts or cs. Application of the method to condensin and cohesin hinge domains was successful: ∼20% of the selected single amino acid substitutions turned out to be ts or cs. This method is versatile in fission yeast and is expected to be broadly applicable to isolate ts/cs mutants with single amino acid substitutions in targeted regions of essential genes. 11 condensin hinge ts mutants were isolated using the method and their responsible mutations are broadly distributed in hinge domain. Characterization of these mutants will be very helpful to understand the function of hinge domain.","doi":"10.1534/g3.119.400156","authors":"Xu X, Yanagida M","authors_abbrev":"Xu X et al.","pubmed_publication_date":"07 May 2019","pubmed_entrez_date":"2019-03-28","publication_year":"2019","canto_session_key":"a33807201a53c48d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xingya Xu","canto_first_approved_date":"2019-05-18 15:11:50","canto_approved_date":"2019-06-06 12:06:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-17 20:40:31","canto_added_date":"2019-03-29 01:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Xingya Xu","community_curator":true,"annotation_count":13,"orcid":"0000-0002-3728-2633","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.06c","SPBC146.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-05-18"},{"uniquename":"EMBL:AU010212","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6835236","title":"Evaluation of epichlorohydrin (ECH) genotoxicity. Microsomal epoxide hydrolase-dependent deactivation of ECH mutagenicity in Schizosaccharomyces pombe in vitro.","citation":"Mutat Res 1983 Apr;109(1):41-52","abstract":"The mutagenic effect of epichlorohydrin (ECH) on the yeast Schizosaccharomyces pombe was studied in vitro in the presence of mouse-liver S9 mix and microsomal and cytosolic fractions. The incubations were always performed in the absence of NADPH-generating systems. S9 mix and microsomes from phenobarbital-pretreated mice significantly reduced ECH mutagenicity, whereas the cytosol did not result in any deactivating effect. The various protein contents of the subcellular fractions were not involved in any scavenger effect as regards ECH mutagenic activity. Moreover, the addition of reduced glutathione to the incubation mixtures indicated that it did not play an important role, either per se or through the enzyme(s) glutathione-S-epoxide transferase(s), in preventing ECH genotoxicity. Our results suggest that microsomal epoxide hydrolase(s) represents the major step in the detoxifying pathway of ECH. These observations were supported by measurements of the specific epoxide hydrolase activity in the various fractions on the same substrate.","authors":"Rossi AM, Migliore L, Loprieno N, Romano M, Salmona M","authors_abbrev":"Rossi AM et al.","pubmed_publication_date":"Apr 1983","pubmed_entrez_date":"1983-04-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35555719","canto_session_key":"5716fb2624c3d974","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-05-15 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24928430","title":"Fission yeast mtr1p regulates interphase microtubule cortical dwell-time.","citation":"Biol Open 2014 Jun 13;3(7):591-6","abstract":"The microtubule cytoskeleton plays important roles in cell polarity, motility and division. Microtubules inherently undergo dynamic instability, stochastically switching between phases of growth and shrinkage. In cells, some microtubule-associated proteins (MAPs) and molecular motors can further modulate microtubule dynamics. We present here the fission yeast mtr1(+), a new regulator of microtubule dynamics that appears to be not a MAP or a motor. mtr1-deletion (mtr1Δ) primarily results in longer microtubule dwell-time at the cell tip cortex, suggesting that mtr1p acts directly or indirectly as a destabilizer of microtubules. mtr1p is antagonistic to mal3p, the ortholog of mammalian EB1, which stabilizes microtubules. mal3Δ results in short microtubules, but can be partially rescued by mtr1Δ, as the double mutant mal3Δ mtr1Δ exhibits longer microtubules than mal3Δ single mutant. By sequence homology, mtr1p is predicted to be a component of the ribosomal quality control complex. Intriguingly, deletion of a predicted ribosomal gene, rps1801, also resulted in longer microtubule dwell-time similar to mtr1Δ. The double-mutant mal3Δ rps1801Δ also exhibits longer microtubules than mal3Δ single mutant alone. Our study suggests a possible involvement of mtr1p and the ribosome complex in modulating microtubule dynamics.","doi":"10.1242/bio.20148607","authors":"Carlier-Grynkorn F, Ji L, Fraisier V, Lombard B, Dingli F, Loew D, Paoletti A, Ronot X, Tran PT","authors_abbrev":"Carlier-Grynkorn F et al.","pubmed_publication_date":"13 Jun 2014","pubmed_entrez_date":"2014-06-15","publication_year":"2014","canto_session_key":"2911e7e541770e14","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-07-21 09:53:02","canto_approved_date":"2023-07-21 09:53:16","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-07-21 09:49:40","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":9,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC132.01c","SPAC18G6.15","SPBC16D10.11c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-07-21"},{"uniquename":"PMID:8303296","title":"RNA polymerase II initiation factor interactions and transcription start site selection.","citation":"Science 1994 Feb 11;263(5148):805-7","abstract":"An RNA polymerase II transcription system was resolved and reconstituted from extracts of Schizosaccharomyces pombe. Exchange with components of a Saccharomyces cerevisiae system was undertaken to reveal the factor or factors responsible for the difference in location of the transcription start site, about 30 base pairs and 40 to 120 base pairs downstream of the TATA box in S. pombe and S. cerevisiae, respectively. Two components, counterparts of human transcription factor IIF (TFIIF) and TFIIH, could be exchanged individually between systems without effect on the start site. Three components, counterparts of human TFIIB, TFIIE, and RNA polymerase II, could not be exchanged individually but could be swapped in the pairs TFIIE-TFIIH and TFIIB-RNA polymerase II, which demonstrates that there are functional interactions between these components. Moreover, exchange of the latter pair shifted the starting position, which shows that TFIIB and RNA polymerase II are solely responsible for determining the start site of transcription.","authors":"Li Y, Flanagan PM, Tschochner H, Kornberg RD","authors_abbrev":"Li Y et al.","pubmed_publication_date":"11 Feb 1994","pubmed_entrez_date":"1994-02-11","publication_year":"1994","canto_session_key":"c2e9522523bee6fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-15 10:54:41","canto_approved_date":"2024-06-15 10:54:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-15 10:54:29","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":56,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.13c","SPCC1682.07","SPAC458.07","SPAC23G3.09","SPCC1620.09c","SPBC13G1.13","SPCC5E4.03c","SPBC32F12.15","SPAC3A12.05c","SPAC22H12.02","SPAC29E6.08","SPCC1259.06","SPAC12G12.05c","SPAC13F5.02c","SPAC2G11.14","SPCC1672.08c","SPAC16E8.11c","SPBC21H7.02","SPAC823.06","SPAC1002.04c","SPAC15A10.02","SPBC15D4.14","SPCC1494.02c","SPAC1D4.12","SPAC17A5.06","SPBC30B4.07c","SPAC16E8.16","SPCC16C4.18c"],"gene_count":28,"ltp_gene_count":28,"approved_date":"2024-06-15"},{"uniquename":"PMID:18725402","title":"The Schizosaccharomyces pombe Pfh1p DNA helicase is essential for the maintenance of nuclear and mitochondrial DNA.","citation":"Mol Cell Biol 2008 Nov;28(21):6594-608","abstract":"Schizosaccharomyces pombe Pfh1p is an essential member of the Pif family of 5'-3' DNA helicases. The two Saccharomyces cerevisiae homologs, Pif1p and Rrm3p, function in nuclear DNA replication, telomere length regulation, and mitochondrial genome integrity. We demonstrate here the existence of multiple Pfh1p isoforms that localized to either nuclei or mitochondria. The catalytic activity of Pfh1p was essential in both cellular compartments. The absence of nuclear Pfh1p resulted in G(2) arrest and accumulation of DNA damage foci, a finding suggestive of an essential role in DNA replication. Exogenous DNA damage resulted in localization of Pfh1p to DNA damage foci, suggesting that nuclear Pfh1p also functions in DNA repair. The absence of mitochondrial Pfh1p caused rapid depletion of mitochondrial DNA. Despite localization to nuclei and mitochondria in S. pombe, neither of the S. cerevisiae homologs, nor human PIF1, suppressed the lethality of pfh1Delta cells. However, the essential nuclear function of Pfh1p could be supplied by Rrm3p. Expression of Rrm3p suppressed the accumulation of DNA damage foci but not the hydroxyurea sensitivity of cells depleted of nuclear Pfh1p. Together, these data demonstrate that Pfh1p has essential roles in the replication of both nuclear and mitochondrial DNA.","doi":"10.1128/MCB.00191-08","authors":"Pinter SF, Aubert SD, Zakian VA","authors_abbrev":"Pinter SF et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-08-30","publication_year":"2008","canto_session_key":"cf76a8fb166d50ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-04-28 08:43:49","canto_approved_date":"2025-07-02 07:46:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-23 10:34:33","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":16,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-04-28"},{"uniquename":"PMID:16118186","title":"Activation of an alternative, rec12 (spo11)-independent pathway of fission yeast meiotic recombination in the absence of a DNA flap endonuclease.","citation":"Genetics 2005 Dec;171(4):1499-511","abstract":"Spo11 or a homologous protein appears to be essential for meiotic DNA double-strand break (DSB) formation and recombination in all organisms tested. We report here the first example of an alternative, mutationally activated pathway for meiotic recombination in the absence of Rec12, the Spo11 homolog of Schizosaccharomyces pombe. Rad2, a FEN-1 flap endonuclease homolog, is involved in processing Okazaki fragments. In its absence, meiotic recombination and proper segregation of chromosomes were restored in rec12Delta mutants to nearly wild-type levels. Although readily detectable in wild-type strains, meiosis-specific DSBs were undetectable in recombination-proficient rad2Delta rec12Delta strains. On the basis of the biochemical properties of Rad2, we propose that meiotic recombination by this alternative (Rec*) pathway can be initiated by non-DSB lesions, such as nicks and gaps, which accumulate during premeiotic DNA replication in the absence of Okazaki fragment processing. We compare the Rec* pathway to alternative pathways of homologous recombination in other organisms.","authors":"Farah JA, Cromie G, Davis L, Steiner WW, Smith GR","authors_abbrev":"Farah JA et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-08-25","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPAC3G6.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:16873283","title":"The self primer of the long terminal repeat retrotransposon Tf1 is not removed during reverse transcription.","citation":"J Virol 2006 Aug;80(16):8267-70","abstract":"The long terminal repeat retrotransposon Tf1 of Schizosaccharomyces pombe uses a unique mechanism of self priming to initiate reverse transcription. Instead of using a tRNA, Tf1 primes minus-strand synthesis with an 11-nucleotide RNA removed from the 5' end of its own transcript. We tested whether the self primer of Tf1 was similar to tRNA primers in being removed from the cDNA by RNase H. Our analysis of Tf1 cDNA extracted from virus-like particles revealed the surprising observation that the dominant species of cDNA retained the self primer. This suggests that integration of the cDNA relies on mechanisms other than reverse transcription to remove the primer.","authors":"Atwood-Moore A, Yan K, Judson RL, Levin HL","authors_abbrev":"Atwood-Moore A et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-07-29","publication_year":"2006","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10652203","title":"Comparative analysis of artificial antisense RNA regulation in fission yeast and human cells.","citation":"Biochem Biophys Res Commun 2000 Feb 05;268(1):8-13","abstract":"The fission yeast Schizosaccharomyces pombe has recently been established as an experimental model for the study of antisense RNA-mediated gene suppression. To validate the use of S. pombe as a host for identifying antisense genes for use in human cells, it was important to determine if sequences identified in yeast were as equally effective in a human cell line. This report describes the comparison of a range of lacZ antisense RNAs targeting a lacZ gene expressed in HeLa cells in a comparable manner to its expression in S. pombe cells in earlier studies. In both cell types, the same lacZ gene target was expressed using the same promoter. Antisense genes were expressed episomally in both experimental systems and the levels of suppression determined. In all cases, the relative level of suppression of the lacZ gene was similar in the mammalian and yeast cells. This result indicates that, at least for lacZ antisense RNA, results obtained in fission yeast are predictive of their behavior in the mammalian cellular environment.","authors":"Clarke ML, Patrikakis M, Atkins D","authors_abbrev":"Clarke ML et al.","pubmed_publication_date":"05 Feb 2000","pubmed_entrez_date":"2000-02-01","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34910579","title":"Involvement of Smi1 in cell wall integrity and glucan synthase Bgs4 localization during fission yeast cytokinesis.","citation":"Mol Biol Cell 2022 Feb 01;33(2):ar17","abstract":"Cytokinesis is the final step of the cell-division cycle. In fungi, it relies on the coordination of constriction of an actomyosin contractile ring and construction of the septum at the division site. Glucan synthases synthesize glucans, which are the major components in fungal cell walls and division septa. It is known that Rho1 and Rho2 GTPases regulate glucan synthases Bgs1, Bgs4, and Ags1, and that Sbg1 and the F-BAR protein Cdc15 play roles in Bgs1 stability and delivery to the plasma membrane. Here we characterize Smi1, an intrinsically disordered protein that interacts with Bgs4 and regulates its trafficking and localization in fission yeast. Smi1 is important for septum integrity, and its absence causes severe lysis during cytokinesis. Smi1 localizes to secretory vesicles and moves together with Bgs4 toward the division site. The concentrations of the glucan synthases Bgs1 and Bgs4 and the glucanases Agn1 and Bgl2 decrease at the division site in the  smi1  mutant, but Smi1 seems to be more specific to Bgs4. Mistargeting of Smi1 to mitochondria mislocalizes Bgs4 but not Bgs1. Together, our data reveal a novel regulator of glucan synthases and glucanases, Smi1, which is more important for Bgs4 trafficking, stability, and localization during cytokinesis.","doi":"10.1091/mbc.E21-04-0214","authors":"Longo LVG, Goodyear EG, Zhang S, Kudryashova E, Wu JQ","authors_abbrev":"Longo LVG et al.","pubmed_publication_date":"01 Feb 2022","pubmed_entrez_date":"2021-12-15","publication_year":"2022","canto_session_key":"7ea26987e7982227","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Valle Guilhen Longo, Larissa","canto_first_approved_date":"2022-03-15 12:55:38","canto_approved_date":"2025-12-06 22:27:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-11 13:55:46","canto_added_date":"2021-12-17 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Valle Guilhen Longo, Larissa","community_curator":true,"annotation_count":37,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPAC11E3.02c","SPAC6G9.11","SPBC23G7.08c","SPBC30D10.17c","SPCC645.06c","SPAC17G8.14c","SPBC1105.05","SPAC821.09","SPBC12D12.04c","SPBC19G7.08c","SPBC428.13c","SPCC1281.01","SPAC14C4.09","SPAC688.07c","SPAC18G6.03","SPAC26H5.08c","SPCC1840.02c","SPBP22H7.03","SPBC1709.01","SPCC645.05c","SPCC1919.10c"],"gene_count":22,"ltp_gene_count":16,"approved_date":"2022-03-15"},{"uniquename":"PMID:10847685","title":"A chromodomain protein, Swi6, performs imprinting functions in fission yeast during mitosis and meiosis.","citation":"Cell 2000 Apr 28;101(3):307-17","abstract":"Inheritance of stable states of gene expression is essential for cellular differentiation. In fission yeast, an epigenetic imprint marking the mating-type (mat2/3) region contributes to inheritance of the silenced state, but the nature of the imprint is not known. We show that a chromodomain-containing Swi6 protein is a dosage-critical component involved in imprinting the mat locus. Transient overexpression of Swi6 alters the epigenetic imprint at the mat2/3 region and heritably converts the expressed state to the silenced state. The establishment and maintenance of the imprint are tightly coupled to the recruitment and the persistence of Swi6 at the mat2/3 region during mitosis as well as meiosis. Remarkably, Swi6 remains bound to the mat2/3 interval throughout the cell cycle and itself seems to be a component of the imprint. Our analyses suggest that the unit of inheritance at the mat2/3 locus comprises the DNA plus the associated Swi6 protein complex.","authors":"Nakayama J, Klar AJ, Grewal SI","authors_abbrev":"Nakayama J et al.","pubmed_publication_date":"28 Apr 2000","pubmed_entrez_date":"2000-06-10","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9566891","title":"Fission yeast rad12+ regulates cell cycle checkpoint control and is homologous to the Bloom's syndrome disease gene.","citation":"Mol Cell Biol 1998 May;18(5):2721-8","abstract":"The human BLM gene is a member of the Escherichia coli recQ helicase family, which includes the Saccharomyces cerevisiae SGS1 and human WRN genes. Defects in BLM are responsible for the human disease Bloom's syndrome, which is characterized in part by genomic instability and a high incidence of cancer. Here we describe the cloning of rad12+, which is the fission yeast homolog of BLM and is identical to the recently reported rhq1+ gene. We showed that rad12 null cells are sensitive to DNA damage induced by UV light and gamma radiation, as well as to the DNA synthesis inhibitor hydroxyurea. Overexpression of the wild-type rad12+ gene also leads to sensitivity to these agents and to defects associated with the loss of the S-phase and G2-phase checkpoint control. We showed genetically and biochemically that rad12+ acts upstream from rad9+, one of the fission yeast G2 checkpoint control genes, in regulating exit from the S-phase checkpoint. The physical chromosome segregation defects seen in rad12 null cells combined with the checkpoint regulation defect seen in the rad12+ overproducer implicate rad12+ as a key coupler of chromosomal integrity with cell cycle progression.","authors":"Davey S, Han CS, Ramer SA, Klassen JC, Jacobson A, Eisenberger A, Hopkins KM, Lieberman HB, Freyer GA","authors_abbrev":"Davey S et al.","pubmed_publication_date":"May 1998","pubmed_entrez_date":"1998-05-05","publication_year":"1998","canto_session_key":"91394a9225fea0a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-13 15:34:46","canto_approved_date":"2021-01-05 15:21:48","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-11-07 09:05:52","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.09c","SPAC664.07c","SPAC2G11.12"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2019-11-13"},{"uniquename":"PMID:26909973","title":"Molecular properties of the N-terminal extension of the fission yeast kinesin-5, Cut7.","citation":"Genet Mol Res 2016 Feb 11;15(1)","abstract":"Kinesin-5 plays an essential role in spindle formation and function, and serves as a potential target for anti-cancer drugs. The aim of this study was to elucidate the molecular properties of the N-terminal extension of the Schizosaccharomyces pombe kinesin-5, Cut7. This extension is rich in charged amino acids and predicted to be intrinsically disordered. In S. pombe cells, a Cut7 construct lacking half the N-terminal extension failed to localize along the spindle microtubules and formed a monopolar spindle. However, a construct lacking the entire N-terminal extension exhibited normal localization and formed a typical bipolar spindle. In addition, in vitro analyses revealed that the truncated Cut7 constructs demonstrated similar motile velocities and directionalities as the wild-type motor protein, but the microtubule landing rates were significantly reduced. These findings suggest that the N-terminal extension is not required for normal Cut7 intracellular localization or function, but alters the microtubule-binding properties of this protein in vitro.","doi":"10.4238/gmr.15017799","authors":"Edamatsu M","authors_abbrev":"Edamatsu M","pubmed_publication_date":"11 Feb 2016","pubmed_entrez_date":"2016-02-25","publication_year":"2016","canto_session_key":"c82cae310ce15f6f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-28 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16904286","title":"Conflicting phylogenetic position of Schizosaccharomyces pombe.","citation":"Genomics 2006 Oct;88(4):387-93","abstract":"The phylogenetic position of the fission yeast Schizosaccharomyces pombe in the fungal Tree of Life is still controversial. Three alternative phylogenetic positions have been proposed in the literature, namely (1) a position basal to the Hemiascomycetes and Euascomycetes, (2) a position as a sister group to the Euascomycetes with the Hemiascomycetes as a basal branch, or (3) a sister group to the Hemiascomycetes with Euascomycetes as a basal branch. Here we compared 91 clusters of orthologous proteins containing a single orthologue that are shared by 19 eukaryote genomes. The major part of these 91 orthologues supports a phylogenetic position of S. pombe as a basal lineage among the Ascomycota, thus supporting the second proposition. Interestingly, part of the orthologous proteins supported a fourth, not yet described alternative, in which S. pombe is basal to both Basidiomycota and Ascomycota. Both topologies of phylogenetic trees are well supported. We believe that both reflect correctly the phylogenetic history of the species concerned. This apparent paradox may point to a heterogeneous nuclear genome of the fungi. Importantly, this needs to be taken in consideration for a correct understanding of the fungal Tree of Life.","authors":"Kuramae EE, Robert V, Snel B, Boekhout T","authors_abbrev":"Kuramae EE et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-08-15","publication_year":"2006","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12589464","title":"Heterologous expression and characterization of Schizosaccharomyces pombe vacuolar carboxypeptidase Y in Saccharomyces cerevisiae.","citation":"Curr Genet 2003 Feb;42(5):252-9","abstract":"To investigate the intracellular transport mechanism of the vacuolar carboxypeptidase of Schizosaccharomyces pombe (SpCPY), SpCPY was expressed in Saccharomyces cerevisiae and its biosynthesis and sorting were examined. When Sac. cerevisiae prc1Delta, devoid of intrinsic (Sc) CPY activity, was transformed with a plasmid carrying the Sch. pombe cpy1(+) gene, CPY activity was restored. Pulse-chase experiments revealed that SpCPY is initially synthesized in a pro-precursor form and then converted to a heterodimer, the mature form, in Sac. cerevisiae cells. SpCPY was not processed into intermediate or mature forms in pep4 mutant cells, indicating that SpCPY was proteolytically cleaved in a PEP4-dependent manner in Sac. cerevisiae. Several vps mutants, which are defective in vacuolar protein-sorting, exhibited a defect in the maturation of SpCPY. Moreover, the maturation of SpCPY was severely inhibited in a vps10 strain, although the pro- segment of SpCPY does not contain a QRPL-like sequence, which is the putative targeting signal of ScCPY. When SpCPY was expressed in a wild-type strain, more than 90% of ScCPY was normally sorted to the vacuole, indicating that SpCPY does not compete with ScCPY for vacuolar sorting. In contrast, expression of SpCPY resulted in a missorting of a ScCPY-invertase fusion protein to the cell surface. These results suggested that there are two different binding sites for SpCPY and ScCPY on Vps10p and that the binding of SpCPY to Vps10p interferes with the binding of a ScCPY-invertase fusion protein.","authors":"Takegawa K, Tokudomi S, Bhuiyan MS, Tabuchi M, Fujita Y, Iwaki T, Utsumi S, Tanaka N","authors_abbrev":"Takegawa K et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-02-18","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24124602","title":"Dopa-responsive dystonia: functional analysis of single nucleotide substitutions within the 5' untranslated GCH1 region.","citation":"PLoS One 2013;8(10):e76975","abstract":"Mutations in the GCH1 gene are associated with childhood onset, dopa-responsive dystonia (DRD). Correct diagnosis of DRD is crucial, given the potential for complete recovery once treated with L-dopa. The majority of DRD associated mutations lie within the coding region of the GCH1 gene, but three additional single nucleotide sequence substitutions have been reported within the 5' untranslated (5'UTR) region of the mRNA. The biologic significance of these 5'UTR GCH1 sequence substitutions has not been analyzed.\nLuciferase reporter assays, quantitative real time PCR and RNA decay assays, combined with bioinformatics, revealed a pathogenic 5'UTR GCH1 substitution. The +142C>T single nucleotide 5'UTR substitution that segregates with affected status in DRD patients, substantially attenuates translation without altering RNA expression levels or stability. The +142C>T substitution disrupts translation most likely by creating an upstream initiation start codon (uAUG) and an upstream open reading frame (uORF).\nThis is the first GCH1 regulatory substitution reported to act at a post-transcriptional level, increasing the list of genetic diseases caused by abnormal translation and reaffirming the importance of investigating potential regulatory substitutions in genetic diseases.","doi":"10.1371/journal.pone.0076975","authors":"Armata IA, Balaj L, Kuster JK, Zhang X, Tsai S, Armatas AA, Multhaupt-Buell TJ, Soberman R, Breakefield XO, Ichinose H, Sharma N","authors_abbrev":"Armata IA et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-10-15","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29071446","title":"Sequence requirement of the ade6-4095 meiotic recombination hotspot in Schizosaccharomyces pombe.","citation":"Genetica 2018 Feb;146(1):65-74","abstract":"Homologous recombination occurs at a greatly elevated frequency in meiosis compared to mitosis and is initiated by programmed double-strand DNA breaks (DSBs). DSBs do not occur at uniform frequency throughout the genome in most organisms, but occur preferentially at a limited number of sites referred to as hotspots. The location of hotspots have been determined at nucleotide-level resolution in both the budding and fission yeasts, and while several patterns have emerged regarding preferred locations for DSB hotspots, it remains unclear why particular sites experience DSBs at much higher frequency than other sites with seemingly similar properties. Short sequence motifs, which are often sites for binding of transcription factors, are known to be responsible for a number of hotspots. In this study we identified the minimum sequence required for activity of one of such motif identified in a screen of random sequences capable of producing recombination hotspots. The experimentally determined sequence, GGTCTRGACC, closely matches the previously inferred sequence. Full hotspot activity requires an effective sequence length of 9.5 bp, whereas moderate activity requires an effective sequence length of approximately 8.2 bp and shows significant association with DSB hotspots. In combination with our previous work, this result is consistent with a large number of different sequence motifs capable of producing recombination hotspots, and supports a model in which hotspots can be rapidly regenerated by mutation as they are lost through recombination.","doi":"10.1007/s10709-017-9997-3","authors":"Foulis SJ, Fowler KR, Steiner WW","authors_abbrev":"Foulis SJ et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2017-10-27","publication_year":"2018","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2017-10-28 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7882425","title":"Biochemical and genetical studies of NADP-specific glutamate dehydrogenase in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1994 Oct;26(4):315-20","abstract":"The initial velocity, pH and temperature optima, and Km values of Schizosaccharomyces pombe NADP-glutamate dehydrogenase (NADP-GDH:EC 1.4.1.4) have been determined. NADP-GDH was found to be specific for the substrates used in the reaction mixtures. NADP-GDH activity showed a sigmoidal response to changes in alpha-ketoglutarate concentrations, following Hill kinetics with a coefficient nH = 2. A two-fold and a three-fold increase in activity was found in extracts of cells grown on a medium containing cytosine or histidine as a sole nitrogen source, respectively, relative to the activity found in cells grown on other sole nitrogen sources including ammonium, adenine, arginine, aspartate, asparagine, glutamate, glutamine, leucine, lysine, proline, uridine and urea. Five NADP-GDH-defective mutants were isolated on the basis of no growth on ammonium plus allantoin as sole nitrogen sources. The mutants also failed to grow on allantoin alone but, in contrast, they were phenotypically indistinguishable from the wild-type growing on solid minimal medium with ammonium. Additionally, the mutants were found to grow as wild-type on minimal medium with alanine, arginine, asparagine, aspartate, glutamate, glutamine, leucine, ornithine and proline in the absence or presence of allantoin. In liquid minimal medium with ammonium as sole nitrogen source they had a slower growth than the wild-type. Normal growth was observed in cells grown on alanine, arginine, asparagine, aspartate, glutamate, glutamine, leucine, ornithine and proline. The mutants had undetectable levels of NADP-GDH activity, but retained wild-type levels of NAD-GDH, glutame synthase (GOGAT) and glutamine synthetase (GS).(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Perysinakis A, Kinghorn JR, Drainas C","authors_abbrev":"Perysinakis A et al.","pubmed_publication_date":"Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_session_key":"90e0fd0aa0ce5178","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-25 14:48:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-25 14:48:42","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-01-25"},{"uniquename":"PMID:10735857","title":"Multiple hexose transporters of Schizosaccharomyces pombe.","citation":"J Bacteriol 2000 Apr;182(8):2153-62","abstract":"We have identified a family of six hexose transporter genes (Ght1 to Ght6) in the fission yeast Schizosaccharomyces pombe. Sequence homology to Saccharomyces cerevisiae and mammalian hexose transporters (Hxtp and GLUTp, respectively) and secondary-structure predictions of 12 transmembrane domains for each of the Ght proteins place them into the sugar porter subfamily within the major facilitator superfamily. Interestingly, among this sugar porter family, the emerging S. pombe hexose transporter family clusters are separate from monosaccharide transporters of other yeasts (S. cerevisiae, Kluyveromyces lactis, and Candida albicans) and of humans, suggesting that these proteins form a distinct structural family of hexose transporters. Expression of the Ght1, Ght2, Ght5, and Ght6 genes in the S. cerevisiae mutant RE700A may functionally complement its D-glucose uptake-deficient phenotype. Northern blot analysis and reverse transcription-PCR showed that among all Ght's of S. pombe, Ght5 is the most prominently expressed hexose transporter. Ght1p, Ght2p, and Ght5p displayed significantly higher specificities for D-glucose than for D-fructose. Analysis of the previously described S. pombe D-glucose transport-deficient mutant YGS-5 revealed that this strain is defective in the Ght1, Ght5, and Ght6 genes. Based on an analysis of three S. pombe strains bearing single or double mutations in Ght3 and Ght4, we conclude that the Ght3p function is required for D-gluconate transport in S. pombe. The function of Ght4p remains to be clarified. Ght6p exhibited a slightly higher affinity to D-fructose than to D-glucose, and among the Ght's it is the transporter with the highest specificity for D-fructose.","authors":"Heiland S, Radovanovic N, Höfer M, Winderickx J, Lichtenberg H","authors_abbrev":"Heiland S et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-03-29","publication_year":"2000","canto_session_key":"495144e748000da3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-29 16:17:28","canto_approved_date":"2023-10-08 10:30:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-30 23:02:17","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1683.08","SPCC1235.13","SPCC1235.14","SPCC548.07c","SPAC1F8.01","SPBC4B4.08"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2017-03-29"},{"uniquename":"PMID:11125054","title":"YPD, PombePD and WormPD: model organism volumes of the BioKnowledge library, an integrated resource for protein information.","citation":"Nucleic Acids Res 2001 Jan 01;29(1):75-9","abstract":"The BioKnowledge Library is a relational database and web site (http://www.proteome.com) composed of protein-specific information collected from the scientific literature. Each Protein Report on the web site summarizes and displays published information about a single protein, including its biochemical function, role in the cell and in the whole organism, localization, mutant phenotype and genetic interactions, regulation, domains and motifs, interactions with other proteins and other relevant data. This report describes four species-specific volumes of the BioKnowledge Library, concerned with the model organisms Saccharomyces cerevisiae (YPD), Schizosaccharomyces pombe (PombePD) and Caenorhabditis elegans (WormPD), and with the fungal pathogen Candida albicans (CalPD). Protein Reports of each species are unified in format, easily searchable and extensively cross-referenced between species. The relevance of these comprehensively curated resources to analysis of proteins in other species is discussed, and is illustrated by a survey of model organism proteins that have similarity to human proteins involved in disease.","authors":"Costanzo MC, Crawford ME, Hirschman JE, Kranz JE, Olsen P, Robertson LS, Skrzypek MS, Braun BR, Hopkins KL, Kondu P, Lengieza C, Lew-Smith JE, Tillberg M, Garrels JI","authors_abbrev":"Costanzo MC et al.","pubmed_publication_date":"01 Jan 2001","pubmed_entrez_date":"2000-01-11","publication_year":"2001","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19563122","title":"Measuring DNA content by flow cytometry in fission yeast.","citation":"Methods Mol Biol 2009;521:449-61","abstract":"Flow cytometry is an essential tool to monitor DNA content and determine cell cycle distribution. Its utility reflects the relative ease of sample preparation and the stochiometric nature of the most popular DNA-binding dyes (propidium iodide and Sytox Green). Mammalian precedents using flow cytometry for replication and cell biology studies are attractive examples for S. pombe researchers. However, the study of DNA replication with multicolor analysis has lagged behind that in mammalian cells. We present basic and advanced protocols for analysis of DNA replication in fission yeast by flow cytometry including whole cell, nuclear \"ghosts,\" and two-color imaging with BrdU.","doi":"10.1007/978-1-60327-815-7_25","authors":"Sabatinos SA, Forsburg SL","authors_abbrev":"Sabatinos SA et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10975257","title":"Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases from Kluyveromyces lactis and Schizosaccharomyces pombe.","citation":"Curr Genet 2000 Aug;38(2):87-94","abstract":"Krebs cycle NAD+ -isocitrate dehydrogenase (Idh) binds to the 5-UTRs of all mitochondrial mRNAs in Saccharomyces cerevisiae. We hypothesize that this leader-binding activity plays a role in translational regulation, thereby linking mitochondrial biogenesis to the need for respiratory function. Analysis of effects of leader binding on mitochondrial translation is complicated by the involvement of the enzyme in mitochondrial metabolism. We have therefore searched for an Idh altered in RNA binding, but retaining full enzyme activity. Idh from Kluyveromyces lactis and Schizosaccharomyces pombe was partially purified and examined for the ability to bind Cox2 mRNA. Sch. pombe Idh, like the S. cerevisiae enzyme, has high affinity for both its own, K. lactis and S. cerevisiae COX2 leaders. In contrast. Idh purified from K. lactis shows only low affinity for all mRNAs tested. To determine what distinguishes K. lactis Idh from S. cerevisiae Idh, genes encoding the two subunits of Idh in K. lactis were cloned and sequenced. Sequence comparison revealed high levels of similarity throughout the proteins, in particular in regions involved in enzyme activity, co-factor and regulator binding. Non-conserved residues between the subunits from the two yeasts are candidates for involvement in the interaction with RNA.","authors":"Elzinga SD, van Oosterum K, Maat C, Grivell LA, van der Spek H","authors_abbrev":"Elzinga SD et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2000-09-07","publication_year":"2000","canto_session_key":"7d3570f156233499","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-11 17:19:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 16:47:34","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11G7.03","SPBC902.05c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-09-11"},{"uniquename":"PMID:1829983","title":"A fission yeast B-type cyclin functioning early in the cell cycle.","citation":"Cell 1991 Jul 12;66(1):149-59","abstract":"We have cloned a fission yeast gene, cig1+, encoding a 48 kd product that is most similar to cyclin B proteins. The cig1+ protein has a \"cyclin box\" approximately 40% identical to B-type cyclins of other species, but lacks the \"destruction box\" required for proteolysis of mitotic cyclins. Deletion of cig1+ had no observable effect on cell viability or progression through G2 or M phase, but instead caused a marked lag in the progression from G1 to S phase. G1 constituted approximately 70% of the cell cycle in cig1 deletion strains, as compared with less than 10% in cig1+ strains. Constitutive cig1+ overexpression was lethal, causing cessation of growth and arrest in G1. Expression of cig1+ failed to rescue an S. cerevisiae strain lacking CLN Start cyclins. Thus, cig1+ identifies a new class of B-type cyclin acting in G1 or S phase that appears to be functionally distinct from all previously described cyclin proteins.","authors":"Bueno A, Richardson H, Reed SI, Russell P","authors_abbrev":"Bueno A et al.","pubmed_publication_date":"12 Jul 1991","pubmed_entrez_date":"1991-07-12","publication_year":"1991","canto_session_key":"b65b4c7d7b9528f2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-08 15:27:16","canto_approved_date":"2026-06-26 08:06:25","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-08-11 16:25:41","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPAPB2B4.03","SPBC11B10.09","SPCC4E9.02"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2015-10-08"},{"uniquename":"PMID:23389634","title":"Response regulator-mediated MAPKKK heteromer promotes stress signaling to the Spc1 MAPK in fission yeast.","citation":"Mol Biol Cell 2013 Apr;24(7):1083-92","abstract":"The Spc1 mitogen-activated protein kinase (MAPK) cascade in fission yeast is activated by two MAPK kinase kinase (MAPKKK) paralogues, Wis4 and Win1, in response to multiple forms of environmental stress. Previous studies identified Mcs4, a \"response regulator\" protein that associates with the MAPKKKs and receives peroxide stress signals by phosphorelay from the Mak2/Mak3 sensor histidine kinases. Here we show that Mcs4 has an unexpected, phosphorelay-independent function in promoting heteromer association between the Wis4 and Win1 MAPKKKs. Only one of the MAPKKKs in the heteromer complex needs to be catalytically active, but disturbing the integrity of the complex by mutations to Mcs4, Wis4, or Win1 results in reduced MAPKKK-MAPKK interaction and, consequently, compromised MAPK activation. The physical interaction among Mcs4, Wis4, and Win1 is constitutive and not responsive to stress stimuli. Therefore the Mcs4-MAPKKK heteromer complex might serve as a stable platform/scaffold for signaling proteins that convey input and output of different stress signals. The Wis4-Win1 complex discovered in fission yeast demonstrates that heteromer-mediated mechanisms are not limited to mammalian MAPKKKs.","doi":"10.1091/mbc.E12-10-0727","authors":"Morigasaki S, Ikner A, Tatebe H, Shiozaki K","authors_abbrev":"Morigasaki S et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2013-02-08","publication_year":"2013","canto_session_key":"7415c70250f4c0b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaz Shiozaki","canto_first_approved_date":"2019-01-30 18:25:47","canto_approved_date":"2024-04-04 13:48:59","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-08-07 15:35:27","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":38,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kaz Shiozaki","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPBC887.10","SPAC24B11.06c","SPAC9G1.02","SPAC1006.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-01-30"},{"uniquename":"PMID:31364709","title":"Intraspecific Diversity of Fission Yeast Mitochondrial Genomes.","citation":"Genome Biol Evol 2019 Aug 01;11(8):2312-2329","abstract":"The fission yeast Schizosaccharomyces pombe is an important model organism, but its natural diversity and evolutionary history remain under-studied. In particular, the population genomics of the S. pombe mitochondrial genome (mitogenome) has not been thoroughly investigated. Here, we assembled the complete circular-mapping mitogenomes of 192 S. pombe isolates de novo, and found that these mitogenomes belong to 69 nonidentical sequence types ranging from 17,618 to 26,910 bp in length. Using the assembled mitogenomes, we identified 20 errors in the reference mitogenome and discovered two previously unknown mitochondrial introns. Analyzing sequence diversity of these 69 types of mitogenomes revealed two highly distinct clades, with only three mitogenomes exhibiting signs of inter-clade recombination. This diversity pattern suggests that currently available S. pombe isolates descend from two long-separated ancestral lineages. This conclusion is corroborated by the diversity pattern of the recombination-repressed K-region located between donor mating-type loci mat2 and mat3 in the nuclear genome. We estimated that the two ancestral S. pombe lineages diverged about 31 million generations ago. These findings shed new light on the evolution of S. pombe and the data sets generated in this study will facilitate future research on genome evolution.","doi":"10.1093/gbe/evz165","authors":"Tao YT, Suo F, Tusso S, Wang YK, Huang S, Wolf JBW, Du LL","authors_abbrev":"Tao YT et al.","pubmed_publication_date":"01 Aug 2019","pubmed_entrez_date":"2019-08-01","publication_year":"2019","canto_session_key":"97ae62f3a3b65885","canto_annotation_status":"APPROVED","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_first_approved_date":"2021-01-16 12:14:05","canto_approved_date":"2021-01-16 12:14:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-16 12:13:50","canto_added_date":"2019-08-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPMITTRNAPRO.01","SPMITTRNALYS.01","SPMITTRNAGLN.01","SPMIT.06","SPMITTRNASER.02","SPMITTRNALEU.02","SPMIT.03","SPMIT.04","SPMITTRNAILE.02","SPRRNA.02","SPMIT.08","SPMITTRNAMET.01","SPMITTRNAARG.01","SPMITTRNALEU.01","SPMIT.10","SPMIT.11","SPMITTRNAGLY.01","SPMITTRNACYS.01","SPMITTRNAVAL.01","SPMIT.01","SPMITTRNATRP.01","SPMITTRNAALA.01","SPMITTRNAGLU.01","SPRRNA.01","SPMITTRNATHR.01","SPMITTRNATYR.01","SPMIT.09","SPMIT.05","SPMITTRNAASN.01","SPMITTRNAHIS.01","SPMITTRNASER.01","SPMITTRNAMET.02","SPMITTRNAILE.01","SPMITNCRNA.01","SPMIT.02","SPMIT.07","SPMITTRNAASP.01","SPMITTRNAARG.02","SPMITTRNAPHE.01"],"gene_count":39,"ltp_gene_count":0,"approved_date":"2021-01-16"},{"uniquename":"PMID:34688157","title":"Sulfide-quinone oxidoreductase is required for cysteine synthesis and indispensable to mitochondrial health.","citation":"Redox Biol 2021 Nov;47:102169","abstract":"Mitochondrial dysfunction is related to common age-related disorders, including neurodegenerative diseases, metabolic syndrome, and carcinogenesis. Therefore, maintaining the functionality and integrity of mitochondria is important for human health. Herein, we found that sulfide:quinone oxidoreductase (Sqr), which oxidizes hydrogen sulfide to reactive sulfur species (RSS), was indispensable to mitochondria health in the eukaryotic model microorganism Schizosaccharomyces pombe. Sqr knock-out led to morphological changes and functional deficiencies of mitochondria and apoptosis in S. pombe. The Sqr knock-out strain displayed the same phenotypes as the cysteine-synthesis-deficient strain, and cysteine addition complemented the effects caused by Sqr knock-out. In S. pombe, Sqr was the main RSS producer in mitochondria, and RSS instead of H 2 S was used by cysteine synthase to synthesize cysteine. This finding rewrites the cysteine biosynthesis route in S. pombe and may also in other eukaryotes and prokaryotes, and highlights the importance of cysteine and RSS in maintaining mitochondrial health.","doi":"10.1016/j.redox.2021.102169","authors":"Zhang X, Xin Y, Chen Z, Xia Y, Xun L, Liu H","authors_abbrev":"Zhang X et al.","pubmed_publication_date":"Nov 2021","pubmed_entrez_date":"2021-10-23","publication_year":"2021","canto_session_key":"f48a193fe5227c32","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-10-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25664996","title":"Synthetic polyamines: new compounds specific to actin dynamics for mammalian cell and fission yeast.","citation":"Bioarchitecture 2014;4(4-5):144-8","abstract":"Actin is a major actor in the determination of cell shape. On the one hand, site-directed assembly/disassembly cycles of actin filaments drive protrusive force leading to lamellipodia and filopodia dynamics. Force produced by actin similarly contributes in membrane scission in endocytosis or Golgi remodeling. On the other hand, cellular processes like adhesion, immune synapse, cortex dynamics or cytokinesis are achieved by combining acto-myosin contractility and actin assembly in a complex and not fully understood manner. New chemical compounds are therefore needed to disentangle acto-myosin and actin dynamics. We have found that synthetic, cell permeant, short polyamines are promising new actin regulators in this context. They generate growth and stabilization of lamellipodia within minutes by slowing down the actin assembly/disassembly cycle and facilitating nucleation. We now report that these polyamines also slow down cytokinetic ring closure in fission yeast. This shows that these synthetic compounds are active also in yeasts, and these experiments specifically highlight that actin depolymerization is involved in the ring closure. Thus, synthetic polyamines appear to be potentially powerful agents in a quantitative approach to the role of actin in complex processes in cell biology, developmental biology and potentially cancer research.","doi":"10.4161/19490992.2014.965111","authors":"Riveline D, Thiagarajan R, Lehn JM, Carlier MF","authors_abbrev":"Riveline D et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2015-02-10","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-02-12 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPCDT1MR","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18437702","title":"A series of promoters for constitutive expression of heterologous genes in fission yeast.","citation":"Yeast 2008 May;25(5):371-6","abstract":"Inducible/repressible promoters are useful for the maintenance of toxic genes or timely expression. For ectopic expression of cloned genes in the fission yeast Schizosaccharomyces pombe, the thiamine-regulatable nmt1 promoter has been widely used, since the transcriptional activity of this promoter can be controlled by thiamine. However, this property sometimes limits a certain type of research, since the expression inevitably requires cells to be cultivated under the conditions that induce promoter activation. To allow constitutive expression of heterologous genes, we cloned three promoters of cam1+, tif51+ and ef1a-c+. Construction of a series of vectors comprising these promoters and their introduction into the fission yeast cells demonstrated that the activity was different among these promoters but was not affected by cultured media commonly used in fission yeast. Therefore, a promoter with appropriate strength would be selectable from these promoters, depending on the genes to be expressed.","doi":"10.1002/yea.1593","authors":"Matsuyama A, Shirai A, Yoshida M","authors_abbrev":"Matsuyama A et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-04-26","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15356001","title":"The Soh1/MED31 protein is an ancient component of Schizosaccharomyces pombe and Saccharomyces cerevisiae Mediator.","citation":"J Biol Chem 2004 Nov 19;279(47):49455-9","abstract":"We here demonstrated that the Soh1/MED31 protein is a stable component of Mediator complex isolated from Schizosaccharomyces pombe and Saccharomyces cerevisiae. Bioinformatic analysis traces the Soh1/MED31 family of Mediator subunits to the point of major eukaryotic divergence, before the appearance of the canonical heptapeptide repeat structure of the RNA polymerase II C-terminal domain.","authors":"Linder T, Gustafsson CM","authors_abbrev":"Linder T et al.","pubmed_publication_date":"19 Nov 2004","pubmed_entrez_date":"2004-09-10","publication_year":"2004","canto_session_key":"188ba95477b67399","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-10-27 16:08:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-10-27 16:08:40","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14F5.08","SPCP31B10.03c","SPBC31F10.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-10-27"},{"uniquename":"PMID:25798942","title":"The Fun30 chromatin remodeler Fft3 controls nuclear organization and chromatin structure of insulators and subtelomeres in fission yeast.","citation":"PLoS Genet 2015 Mar;11(3):e1005101","abstract":"In eukaryotic cells, local chromatin structure and chromatin organization in the nucleus both influence transcriptional regulation. At the local level, the Fun30 chromatin remodeler Fft3 is essential for maintaining proper chromatin structure at centromeres and subtelomeres in fission yeast. Using genome-wide mapping and live cell imaging, we show that this role is linked to controlling nuclear organization of its targets. In fft3∆ cells, subtelomeres lose their association with the LEM domain protein Man1 at the nuclear periphery and move to the interior of the nucleus. Furthermore, genes in these domains are upregulated and active chromatin marks increase. Fft3 is also enriched at retrotransposon-derived long terminal repeat (LTR) elements and at tRNA genes. In cells lacking Fft3, these sites lose their peripheral positioning and show reduced nucleosome occupancy. We propose that Fft3 has a global role in mediating association between specific chromatin domains and the nuclear envelope.","doi":"10.1371/journal.pgen.1005101","authors":"Steglich B, Strålfors A, Khorosjutina O, Persson J, Smialowska A, Javerzat JP, Ekwall K","authors_abbrev":"Steglich B et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-03-24","publication_year":"2015","canto_session_key":"fd4f3f52f1d38106","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-15 16:21:00","canto_approved_date":"2025-09-03 19:42:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-15 16:20:50","canto_added_date":"2015-03-25 01:15:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.05c","SPBC19C7.10","SPBC17G9.04c","SPCC306.03c","SPCC16C4.14c","SPAC25A8.01c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-02-15"},{"uniquename":"PMID:31782368","title":"Development of A Fission Yeast Cell-Based Platform for High Throughput Screening of HIV-1 Protease Inhibitors.","citation":"Curr HIV Res 2019;17(6):429-440","abstract":"HIV-1 protease inhibitor (PI) is one of the most potent classes of drugs in combinational antiretroviral therapies (cART). When a PI is used in combination with other anti- HIV drugs, cART can often suppress HIV-1 below detection thus prolonging the patient's lives. However, the challenge often faced by patients is the emergence of HIV-1 drug resistance. Thus, PIs with high genetic-barrier to drug-resistance are needed.\nThe objective of this study was to develop a novel and simple fission yeast (Schizosaccharomyces pombe) cell-based system that is suitable for high throughput screening (HTS) of small molecules against HIV-1 protease (PR).\nA fission yeast RE294-GFP strain that stably expresses HIV-1 PR and green fluorescence protein (GFP) under the control of an inducible nmt1 promoter was used. Production of HIV-1 PR induces cellular growth arrest, which was used as the primary endpoint for the search of PIs and was quantified by an absorbance-based method. Levels of GFP production were used as a counter-screen control to eliminate potential transcriptional nmt1 inhibitors.\nBoth the absorbance-based HIV-1 PR assay and the GFP-based fluorescence assay were miniaturized and optimized for HTS. A pilot study was performed using a small drug library mixed with known PI drugs and nmt1 inhibitors. With empirically adjusted and clearly defined double-selection criteria, we were able to correctly identify the PIs and to exclude all hidden nmt1 inhibitors.\nWe have successfully developed and validated a fission yeast cell-based HTS platform for the future screening and testing of HIV-1 PR inhibitors.","doi":"10.2174/1570162X17666191128102839","authors":"Benko Z, Zhang J, Zhao RY","authors_abbrev":"Benko Z et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-11-30","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-12-01 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26246599","title":"Phosphorylation-dependent inhibition of Cdc42 GEF Gef1 by 14-3-3 protein Rad24 spatially regulates Cdc42 GTPase activity and oscillatory dynamics during cell morphogenesis.","citation":"Mol Biol Cell 2015 Oct 01;26(19):3520-34","abstract":"Active Cdc42 GTPase, a key regulator of cell polarity, displays oscillatory dynamics that are anticorrelated at the two cell tips in fission yeast. Anticorrelation suggests competition for active Cdc42 or for its effectors. Here we show how 14-3-3 protein Rad24 associates with Cdc42 guanine exchange factor (GEF) Gef1, limiting Gef1 availability to promote Cdc42 activation. Phosphorylation of Gef1 by conserved NDR kinase Orb6 promotes Gef1 binding to Rad24. Loss of Rad24-Gef1 interaction increases Gef1 protein localization and Cdc42 activation at the cell tips and reduces the anticorrelation of active Cdc42 oscillations. Increased Cdc42 activation promotes precocious bipolar growth activation, bypassing the normal requirement for an intact microtubule cytoskeleton and for microtubule-dependent polarity landmark Tea4-PP1. Further, increased Cdc42 activation by Gef1 widens cell diameter and alters tip curvature, countering the effects of Cdc42 GTPase-activating protein Rga4. The respective levels of Gef1 and Rga4 proteins at the membrane define dynamically the growing area at each cell tip. Our findings show how the 14-3-3 protein Rad24 modulates the availability of Cdc42 GEF Gef1, a homologue of mammalian Cdc42 GEF DNMBP/TUBA, to spatially control Cdc42 GTPase activity and promote cell polarization and cell shape emergence.","doi":"10.1091/mbc.E15-02-0095","authors":"Das M, Nuñez I, Rodriguez M, Wiley DJ, Rodriguez J, Sarkeshik A, Yates JR, Buchwald P, Verde F","authors_abbrev":"Das M et al.","pubmed_publication_date":"01 Oct 2015","pubmed_entrez_date":"2015-08-07","publication_year":"2015","canto_session_key":"3223cbaa5cb930cf","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-09 00:19:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.12","SPBC28E12.03","SPBC1706.01","SPAC8E11.02c","SPAC24H6.09"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:34762489","title":"Nuclear pores dilate and constrict in cellulo.","citation":"Science 2021 Dec 10;374(6573):eabd9776","abstract":"In eukaryotic cells, nuclear pore complexes (NPCs) fuse the inner and outer nuclear membranes and mediate nucleocytoplasmic exchange. They are made of 30 different nucleoporins and form a cylindrical architecture around an aqueous central channel. This architecture is highly dynamic in space and time. Variations in NPC diameter have been reported, but the physiological circumstances and the molecular details remain unknown. Here, we combined cryo–electron tomography with integrative structural modeling to capture a molecular movie of the respective large-scale conformational changes in cellulo. Although NPCs of exponentially growing cells adopted a dilated conformation, they reversibly constricted upon cellular energy depletion or conditions of hypertonic osmotic stress. Our data point to a model where the nuclear envelope membrane tension is linked to the conformation of the NPC.","doi":"10.1126/science.abd9776","authors":"Zimmerli CE, Allegretti M, Rantos V, Goetz SK, Obarska-Kosinska A, Zagoriy I, Halavatyi A, Hummer G, Mahamid J, Kosinski J, Beck M","authors_abbrev":"Zimmerli CE et al.","pubmed_publication_date":"10 Dec 2021","pubmed_entrez_date":"2021-11-11","publication_year":"2021","canto_session_key":"6ede70db7dbad9c0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-25 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:457803","title":"A control acting over the initiation of DNA replication in the yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1979 Apr;36:155-68","abstract":"The control of cell division in the yeast Schizosaccharomyces pombe appears to be quite different to that of any other eukaryotic organisms for it is usually exerted not at the initiation of S-phase but at that of mitosis. However, it has been suggested that a control over the initiation of S-phase does also exist but that its action is redundant whilst the mitotic control is operating. This study has chosen conditions in which the latter appears to be largely absent in order to study the cryptic S-phase control. The timing of S-phase has been studied in cells grown at varying rates under nitrogen limitation in a chemostat. It is found that under these conditions the control of cell division resembles that of other eukaryotes. As the dilution rate of the chemostat is reduced, all increase in the generation time can be accounted for by a lengthened G1 period. In contrast, the length of S + G2 remains invariant. Thus, there must indeed be a control acting in G1 in S. pombe. An analysis of the size of cells at different growth rates shows that the initiation of S-phase is correlated with a particular cell size.","authors":"Nasmyth KA","authors_abbrev":"Nasmyth KA","pubmed_publication_date":"Apr 1979","pubmed_entrez_date":"1979-04-01","publication_year":"1979","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16222246","title":"Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation.","citation":"Nature 2005 Dec 22;438(7071):1116-22","abstract":"Tri-methylation of histone H3 lysine 9 is important for recruiting heterochromatin protein 1 (HP1) to discrete regions of the genome, thereby regulating gene expression, chromatin packaging and heterochromatin formation. Here we show that HP1alpha, -beta, and -gamma are released from chromatin during the M phase of the cell cycle, even though tri-methylation levels of histone H3 lysine 9 remain unchanged. However, the additional, transient modification of histone H3 by phosphorylation of serine 10 next to the more stable methyl-lysine 9 mark is sufficient to eject HP1 proteins from their binding sites. Inhibition or depletion of the mitotic kinase Aurora B, which phosphorylates serine 10 on histone H3, causes retention of HP1 proteins on mitotic chromosomes, suggesting that H3 serine 10 phosphorylation is necessary for the dissociation of HP1 from chromatin in M phase. These findings establish a regulatory mechanism of protein-protein interactions, through a combinatorial readout of two adjacent post-translational modifications: a stable methylation and a dynamic phosphorylation mark.","authors":"Fischle W, Tseng BS, Dormann HL, Ueberheide BM, Garcia BA, Shabanowitz J, Hunt DF, Funabiki H, Allis CD","authors_abbrev":"Fischle W et al.","pubmed_publication_date":"22 Dec 2005","pubmed_entrez_date":"2005-10-14","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-21 14:22:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10545452","title":"Drc1p/Cps1p, a 1,3-beta-glucan synthase subunit, is essential for division septum assembly in Schizosaccharomyces pombe.","citation":"Genetics 1999 Nov;153(3):1193-203","abstract":"Schizosaccharomyces pombe divides by medial fission through the use of an actomyosin-based contractile ring. A division septum is formed centripetally, concomitant with ring constriction. Although several genes essential for cytokinesis have been described previously, enzymes that participate in the assembly of the division septum have not been identified. Here we describe a temperature-sensitive mutation, drc1-191, that prevents division septum assembly and causes mutant cells to arrest with a stable actomyosin ring. Unlike the previously characterized cytokinesis mutants, which undergo multiple mitotic cycles, drc1-191 is the first cytokinesis mutant that arrests with two interphase nuclei. Interestingly, unlike drc1-191, drc1-null mutants proceed through multiple mitotic cycles, leading to the formation of large cells with many nuclei. drc1 is allelic to cps1, which encodes a 1,3-beta-glucan synthase subunit. We conclude that Drc1p/Cps1p is not required for cell elongation and cell growth, but plays an essential role in assembly of the division septum. Furthermore, it appears that constriction of the actomyosin ring might depend on assembly of the division septum. We discuss possible mechanisms that account for the differences in the phenotypes of the drc1-191 and the drc1-null mutants and also reflect the potential links between Drc1p and other cytokinesis regulators.","authors":"Liu J, Wang H, McCollum D, Balasubramanian MK","authors_abbrev":"Liu J et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-11-05","publication_year":"1999","canto_session_key":"58a02b795c025a88","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-11-09 13:54:31","canto_approved_date":"2023-05-04 11:09:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-09 13:42:25","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPCC645.05c","SPBC19G7.05c","SPAC20G8.05c","SPAC1565.06c","SPAC27F1.02c","SPAC24B11.11c","SPBC24C6.07","SPAC9G1.09","SPCC613.04c","SPCC1739.11c","SPBC21.06c","SPAC4A8.15c","SPBC244.01c","SPBC776.12c","SPAC4F8.13c","SPAP8A3.08"],"gene_count":17,"ltp_gene_count":5,"approved_date":"2022-11-09"},{"uniquename":"PMID:8799851","title":"The kinetics of the B cyclin p56cdc13 and the phosphatase p80cdc25 during the cell cycle of the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1996 Jun;109 ( Pt 6):1647-53","abstract":"The levels of the B cyclin p56cdc13 and the phosphatase p80cdc25 have been followed in selection-synchronised cultures of Schizosaccharomyces pombe wild-type and wee1 mutant cells. p56cdc13 has also been followed in induction-synchronised cells of the mutant cdc2-33. The main conclusions are: (1) cdc13 levels in wild-type cells start to rise from base line at about mid-G2, reach a peak before mitosis and then fall slowly through G1. Cells exit mitosis with appreciable levels of cdc13. (2) cdc13 levels in wee1 cells fall to zero in interphase. They also start to rise at the beginning of G2, which may be related to the absence of a mitotic size control. (3) cdc25 starts to rise later and reaches a peak after mitosis. This is not what would be expected from a simple mitotic inducer and suggests that cdc25 has an important function at the end of mitosis. (4) An upper (heavier) band of cdc25 peaks at the same time as the main band but rises and falls more rapidly. If this is a hyperphosphorylated form, its timing shows that it is most unlikely to function in the ways shown for such a form in eggs and mammalian cells. (5) Experiments with the mutant cdc10-129 and with hydroxyurea show that the initial signal to begin synthesis of cdc13 originates at Start. (6) In induction synchrony, where G2 spans across cell division, there is evidence that some events in one cycle cannot start in the previous one. (7) Revised timings are given for the times of mitosis in these cultures.","authors":"Creanor J, Mitchison JM","authors_abbrev":"Creanor J et al.","pubmed_publication_date":"Jun 1996","pubmed_entrez_date":"1996-06-01","publication_year":"1996","canto_session_key":"7c80e0a2a39ec200","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-11-21 14:29:53","canto_approved_date":"2019-06-14 13:00:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-11-15 12:22:13","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":4,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC582.03","SPAC24H6.05","SPBC336.12c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2018-11-21"},{"uniquename":"PMID:11212119","title":"Synthesis and antifungal activities of novel 1,3-beta-D-glucan synthase inhibitors. Part 1.","citation":"Bioorg Med Chem Lett 2001 Feb 12;11(3):395-8","abstract":"Highly potent 1,3-beta-D-glucan synthase inhibitors 10, 11 and 13 have been identified by the chemical modification of the fungicidal macrocyclic lipopeptidolactone, RO-09-3655 (1), isolated from the cultured broth of Deuteromycotinia spp. D-Ornithine derivative (10) showed improved antifungal activity in the systemic candidiasis model in mice and reduced hepatotoxicity in vitro, as compared with 1.","authors":"Masubuchi K, Okada T, Kohchi M, Sakaitani M, Mizuguchi E, Shirai H, Aoki M, Watanabe T, Kondoh O, Yamazaki T, Satoh Y, Kobayashi K, Inoue T, Horii I, Shimma N","authors_abbrev":"Masubuchi K et al.","pubmed_publication_date":"12 Feb 2001","pubmed_entrez_date":"2001-02-24","publication_year":"2001","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17993570","title":"Functional characterization of Pneumocystis carinii brl1 by transspecies complementation analysis.","citation":"Eukaryot Cell 2007 Dec;6(12):2448-52","abstract":"Pneumocystis jirovecii is a fungus which causes severe opportunistic infections in immunocompromised humans. The brl1 gene of P. carinii infecting rats was identified and characterized by using bioinformatics in conjunction with functional complementation in Saccharomyces cerevisiae and Schizosaccharomyces pombe. The ectopic expression of this gene rescues null alleles of essential nuclear membrane proteins of the Brr6/Brl1 family in both yeasts.","authors":"Lo Presti L, Cockell M, Cerutti L, Simanis V, Hauser PM","authors_abbrev":"Lo Presti L et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-11-13","publication_year":"2007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8F11.06"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:2832735","title":"Structural organization and functional analysis of centromeric DNA in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1988 Feb;8(2):754-63","abstract":"Centromeric DNA in the fission yeast Schizosaccharomyces pombe was isolated by chromosome walking and by field inversion gel electrophoretic fractionation of large genomic DNA restriction fragments. The centromere regions of the three chromosomes were contained on three SalI fragments (120 kilobases [kb], chromosome III; 90 kb, chromosome II; and 50 kb, chromosome I). Each fragment contained several repetitive DNA sequences, including repeat K (6.4 kb), repeat L (6.0 kb), and repeat B, that occurred only in the three centromere regions. On chromosome II, these repeats were organized into a 35-kb inverted repeat that included one copy of K and L in each arm of the repeat. Site-directed integration of a plasmid containing the yeast LEU2 gene into K repeats at each of the centromeres or integration of an intact K repeat into a chromosome arm had no effect on mitotic or meiotic centromere function. The centromeric repeat sequences were not transcribed and possessed many of the properties of constitutive heterochromatin. Thus, S. pombe is an excellent model system for studies on the role of repetitive sequence elements in centromere function.","authors":"Fishel B, Amstutz H, Baum M, Carbon J, Clarke L","authors_abbrev":"Fishel B et al.","pubmed_publication_date":"Feb 1988","pubmed_entrez_date":"1988-02-01","publication_year":"1988","canto_session_key":"e84f4ec5b002a010","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 14:37:58","canto_approved_date":"2019-01-07 14:37:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 14:37:52","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:23967182","title":"A yeast-based chemical screen identifies a PDE inhibitor that elevates steroidogenesis in mouse Leydig cells via PDE8 and PDE4 inhibition.","citation":"PLoS One 2013;8(8):e71279","abstract":"A cell-based high-throughput screen (HTS) was developed to detect phosphodiesterase 8 (PDE8) and PDE4/8 combination inhibitors. By replacing the Schizosaccharomyces pombe PDE gene with the murine PDE8A1 gene in strains lacking adenylyl cyclase, we generated strains whose protein kinase A (PKA)-stimulated growth in 5-fluoro orotic acid (5FOA) medium reflects PDE8 activity. From our previously-identified PDE4 and PDE7 inhibitors, we identified a PDE4/8 inhibitor that allowed us to optimize screening conditions. Of 222,711 compounds screened, ∼0.2% displayed composite Z scores of >20. Additional yeast-based assays using the most effective 367 compounds identified 30 candidates for further characterization. Among these, compound BC8-15 displayed the lowest IC₅₀ value for both PDE4 and PDE8 inhibition in in vitro enzyme assays. This compound also displays significant activity against PDE10A and PDE11A. BC8-15 elevates steroidogenesis in mouse Leydig cells as a single pharmacological agent. Assays using BC8-15 and two structural derivatives support a model in which PDE8 is a primary regulator of testosterone production by Leydig cells, with an additional role for PDE4 in this process. BC8-15, BC8-15A, and BC8-15C, which are commercially available compounds, display distinct patterns of activity against PDE4, PDE8, PDE10A, and PDE11A, representing a chemical toolkit that could be used to examine the biological roles of these enzymes in cell culture systems.","doi":"10.1371/journal.pone.0071279","authors":"Demirbas D, Wyman AR, Shimizu-Albergine M, Cakici O, Beavo JA, Hoffman CS","authors_abbrev":"Demirbas D et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-08-23","publication_year":"2013","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25643023","title":"PRIMED: PRIMEr database for deleting and tagging all fission and budding yeast genes developed using the open-source genome retrieval script (GRS).","citation":"PLoS One 2015;10(2):e0116657","abstract":"The fission (Schizosaccharomyces pombe) and budding (Saccharomyces cerevisiae) yeasts have served as excellent models for many seminal discoveries in eukaryotic biology. In these organisms, genes are deleted or tagged easily by transforming cells with PCR-generated DNA inserts, flanked by short (50-100 bp) regions of gene homology. These PCR reactions use especially designed long primers, which, in addition to the priming sites, carry homology for gene targeting. Primer design follows a fixed method but is tedious and time-consuming especially when done for a large number of genes. To automate this process, we developed the Python-based Genome Retrieval Script (GRS), an easily customizable open-source script for genome analysis. Using GRS, we created PRIMED, the complete PRIMEr D atabase for deleting and C-terminal tagging genes in the main S. pombe and five of the most commonly used S. cerevisiae strains. Because of the importance of noncoding RNAs (ncRNAs) in many biological processes, we also included the deletion primer set for these features in each genome. PRIMED are accurate and comprehensive and are provided as downloadable Excel files, removing the need for future primer design, especially for large-scale functional analyses. Furthermore, the open-source GRS can be used broadly to retrieve genome information from custom or other annotated genomes, thus providing a suitable platform for building other genomic tools by the yeast or other research communities.","doi":"10.1371/journal.pone.0116657","authors":"Cummings MT, Joh RI, Motamedi M","authors_abbrev":"Cummings MT et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-02-03","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-02-04 01:15:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15857958","title":"Roles of Pdk1p, a fission yeast protein related to phosphoinositide-dependent protein kinase, in the regulation of mitosis and cytokinesis.","citation":"Mol Biol Cell 2005 Jul;16(7):3162-75","abstract":"Proteins related to the phosphoinositide-dependent protein kinase family have been identified in the majority of eukaryotes. Although much is known about upstream mechanisms that regulate the PDK1-family of kinases in metazoans, how these kinases regulate cell growth and division remains unclear. Here, we characterize a fission yeast protein related to members of this family, which we have termed Pdk1p. Pdk1p localizes to the spindle pole body and the actomyosin ring in early mitotic cells. Cells deleted for pdk1 display multiple defects in mitosis and cytokinesis, all of which are exacerbated when the function of fission yeast polo kinase, Plo1p, is partially compromised. We conclude that Pdk1p functions in concert with Plo1p to regulate multiple processes such as the establishment of a bipolar mitotic spindle, transition to anaphase, placement of the actomyosin ring and proper execution of cytokinesis. We also present evidence that the effects of Pdk1p on cytokinesis are likely mediated via the fission yeast anillin-related protein, Mid1p, and the septation initiation network.","authors":"Bimbó A, Liu J, Balasubramanian MK","authors_abbrev":"Bimbó A et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-04-29","publication_year":"2005","canto_session_key":"d4228b03e96911f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-08-01 09:55:43","canto_approved_date":"2024-09-25 14:21:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2022-08-01 09:46:40","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":45,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPCC4B3.15","SPAC24H6.05","SPAC1565.06c","SPBC244.01c","SPAP8A3.08","SPBC106.01","SPAC1782.09c","SPBC1778.10c","SPAC23C11.16","SPAPB1A10.09"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2022-08-01"},{"uniquename":"PMID:22625857","title":"DNA replication: Pif1 pulls the plug on stalled replication forks.","citation":"Curr Biol 2012 May 22;22(10):R404-5","abstract":"The conserved PIF helicase family appears to function in replication to ensure termination and passage through regions that slow or arrest replication fork movement. Findings in fission yeast extend evidence from budding yeast, and argue for universal mechanisms that ensure replication integrity.","doi":"10.1016/j.cub.2012.04.015","authors":"Shimada K, Gasser SM","authors_abbrev":"Shimada K et al.","pubmed_publication_date":"22 May 2012","pubmed_entrez_date":"2012-05-26","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15106121","title":"DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4).","citation":"Am J Hum Genet 2004 Jun;74(6):1128-35","abstract":"Juvenile amyotrophic lateral sclerosis (ALS4) is a rare autosomal dominant form of juvenile amyotrophic lateral sclerosis (ALS) characterized by distal muscle weakness and atrophy, normal sensation, and pyramidal signs. Individuals affected with ALS4 usually have an onset of symptoms at age <25 years, a slow rate of progression, and a normal life span. The ALS4 locus maps to a 1.7-Mb interval on chromosome 9q34 flanked by D9S64 and D9S1198. To identify the molecular basis of ALS4, we tested 19 genes within the ALS4 interval and detected missense mutations (T3I, L389S, and R2136H) in the Senataxin gene (SETX). The SETX gene encodes a novel 302.8-kD protein. Although its function remains unknown, SETX contains a DNA/RNA helicase domain with strong homology to human RENT1 and IGHMBP2, two genes encoding proteins known to have roles in RNA processing. These observations of ALS4 suggest that mutations in SETX may cause neuronal degeneration through dysfunction of the helicase activity or other steps in RNA processing.","authors":"Chen YZ, Bennett CL, Huynh HM, Blair IP, Puls I, Irobi J, Dierick I, Abel A, Kennerson ML, Rabin BA, Nicholson GA, Auer-Grumbach M, Wagner K, De Jonghe P, Griffin JW, Fischbeck KH, Timmerman V, Cornblath DR, Chance PF","authors_abbrev":"Chen YZ et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-04-24","publication_year":"2004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30230996","title":"Evolution of 1, 3, 5-trisubstituted bipyrazole scaffold based platinum(II) complexes as a biological active agent.","citation":"Nucleosides Nucleotides Nucleic Acids 2018;37(8):455-483","abstract":"Square planar mononuclear platinum(II) complexes having general formula [Pt(L n )Cl 2 ], (where, L n  = L 1-4 ) were synthesized with neutral bidentate heterocyclic 1,3,5-trisubstituted bipyrazole based ligands. The synthesized compounds were characterized by physicochemical method such as TGA, molar conductance, micro-elemental analysis and magnetic moment, and spectroscopic method such as, FT-IR, UV-vis,  1 H NMR,  13 C NMR and mass spectrometry. Biological applications of the compounds were carried out using in vitro brine shrimp lethality bioassay, in vitro antimicrobial study against five different pathogens, and cellular level cytotoxicity against Schizosaccharomyces pombe (S. Pombe) cells. Pt(II) complexes were tested for DNA interaction activities using electronic absorption titration, viscosity measurements study, fluorescence quenching technique and molecular docking assay. Binding constants (K b ) of ligands and complexes were observed in the range of 0.23-1.07 × 10 5  M -1  and 0.51-3.13 × 10 5  M -1 , respectively. Pt(II) complexes (I-IV) display an excellent binding tendency to biomolecule (DNA) and possess comparatively high binding constant (K b ) values than the ligands. The DNA binding study indicate partial intercalative mode of binding in complex-DNA. The gel electrophoresis activity was carried out to examine DNA nuclease property of pUC19 plasmid DNA.","doi":"10.1080/15257770.2018.1498510","authors":"Lunagariya MV, Thakor KP, Pursuwani BH, Patel MN","authors_abbrev":"Lunagariya MV et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-09-20","publication_year":"2018","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2018-09-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8440738","title":"Yeast AMP deaminase. Catalytic activity in Schizosaccharomyces pombe and chromosomal location in Saccharomyces cerevisiae.","citation":"J Biol Chem 1993 Feb 25;268(6):4549-55","abstract":"The AMP deaminase gene was mapped to chromosome XIII of Saccharomyces cerevisiae strain JM1901. The AMP deaminase gene is located near SUP5, GAL80, SUF7, and SUF22. The presence of AMP deaminase in the fission yeast Schizosaccharomyces pombe was examined by comparing DNA hybridization, protein immunoreactivity, and catalytic activity from S. cerevisiae, known to contain the protein, to S. pombe. DNA hybridization experiments using the cloned S. cerevisiae AMP deaminase gene failed to hybridize to the genomic DNA from S. pombe strain 972h-s. Protein extracts from S. pombe and S. cerevisiae were analyzed in parallel and exhibited comparable AMP deaminase activities. Analysis of reaction intermediates in cell extracts of S. pombe established that IMP is formed directly from AMP without intervening steps. The AMP deaminase of S. pombe was purified 1,100-fold to a specific catalytic activity of 67 mumol/min/mg of protein. Purified protein interacted weakly with polyclonal antibodies prepared against S. cerevisiae AMP deaminase. AMP deaminases from both S. cerevisiae and S. pombe were activated by ATP with micromolar activation constants, are inhibited by coformycin, and are specific for AMP when compared to other purine nucleosides and nucleotides. The results establish that S. pombe contains an AMP deaminase with catalytic properties similar to that from S. cerevisiae, even though the DNA sequences of the genes and the immunoreactivity of the protein from S. pombe differs considerably from the AMP deaminase of S. cerevisiae. Genetic analysis of the pathways of purine metabolism in S. pombe (Pourquié, J., and Heslot, H. (1971) Genet. Res. 18, 33-44) had indicated the absence of AMP deaminase. The presence of a regulated AMP deaminase in S. pombe supports the hypothesis that eukaryotes regulate adenine nucleotide pools by the activity of AMP deaminase.","authors":"Sollitti P, Merkler DJ, Estupiñán B, Schramm VL","authors_abbrev":"Sollitti P et al.","pubmed_publication_date":"25 Feb 1993","pubmed_entrez_date":"1993-02-25","publication_year":"1993","canto_session_key":"970a33dafdeff450","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 14:13:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 14:13:19","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC106.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:16362057","title":"Histone demethylation by a family of JmjC domain-containing proteins.","citation":"Nature 2006 Feb 16;439(7078):811-6","abstract":"Covalent modification of histones has an important role in regulating chromatin dynamics and transcription. Whereas most covalent histone modifications are reversible, until recently it was unknown whether methyl groups could be actively removed from histones. Using a biochemical assay coupled with chromatography, we have purified a novel JmjC domain-containing protein, JHDM1 (JmjC domain-containing histone demethylase 1), that specifically demethylates histone H3 at lysine 36 (H3-K36). In the presence of Fe(ii) and alpha-ketoglutarate, JHDM1 demethylates H3-methyl-K36 and generates formaldehyde and succinate. Overexpression of JHDM1 reduced the level of dimethyl-H3-K36 (H3K36me2) in vivo. The demethylase activity of the JmjC domain-containing proteins is conserved, as a JHDM1 homologue in Saccharomyces cerevisiae also has H3-K36 demethylase activity. Thus, we identify the JmjC domain as a novel demethylase signature motif and uncover a protein demethylation mechanism that is conserved from yeast to human.","authors":"Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, Zhang Y","authors_abbrev":"Tsukada Y et al.","pubmed_publication_date":"16 Feb 2006","pubmed_entrez_date":"2005-12-20","publication_year":"2006","canto_session_key":"18216fcd7408df54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-12-19 15:43:11","canto_approved_date":"2026-01-22 16:44:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-12-19 15:43:05","canto_added_date":"2025-10-22 11:45:02","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.16c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-12-19"},{"uniquename":"PMID:18227226","title":"Development of a fission yeast-based high-throughput screen to identify chemical regulators of cAMP phosphodiesterases.","citation":"J Biomol Screen 2008 Jan;13(1):62-71","abstract":"Cyclic nucleotide phosphodiesterases (PDEs) comprise a superfamily of enzymes that serve as drug targets in many human diseases. There is a continuing need to identify high-specificity inhibitors that affect individual PDE families or even subtypes within a single family. The authors describe a fission yeast-based high-throughput screen to detect inhibitors of heterologously expressed adenosine 3',5'-cyclic monophosphate (cAMP) PDEs. The utility of this system is demonstrated by the construction and characterization of strains that express mammalian PDE2A, PDE4A, PDE4B, and PDE8A and respond appropriately to known PDE2A and PDE4 inhibitors. High-throughput screens of 2 bioactive compound libraries for PDE inhibitors using strains expressing PDE2A, PDE4A, PDE4B, and the yeast PDE Cgs2 identified known PDE inhibitors and members of compound classes associated with PDE inhibition. The authors verified that the furanocoumarin imperatorin is a PDE4 inhibitor based on its ability to produce a PDE4-specific elevation of cAMP levels. This platform can be used to identify PDE activators, as well as genes encoding PDE regulators, which could serve as targets for future drug screens.","doi":"10.1177/1087057107312127","authors":"Ivey FD, Wang L, Demirbas D, Allain C, Hoffman CS","authors_abbrev":"Ivey FD et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2008-01-30","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37988290","title":"Condensin positioning at telomeres by shelterin proteins drives sister-telomere disjunction in anaphase.","citation":"Elife 2023 Nov 21;12","abstract":"The localization of condensin along chromosomes is crucial for their accurate segregation in anaphase. Condensin is enriched at telomeres but how and for what purpose had remained elusive. Here, we show that fission yeast condensin accumulates at telomere repeats through the balancing acts of Taz1, a core component of the shelterin complex that ensures telomeric functions, and Mit1, a nucleosome remodeler associated with shelterin. We further show that condensin takes part in sister-telomere separation in anaphase, and that this event can be uncoupled from the prior separation of chromosome arms, implying a telomere-specific separation mechanism. Consistent with a cis-acting process, increasing or decreasing condensin occupancy specifically at telomeres modifies accordingly the efficiency of their separation in anaphase. Genetic evidence suggests that condensin promotes sister-telomere separation by counteracting cohesin. Thus, our results reveal a shelterin-based mechanism that enriches condensin at telomeres to drive in cis their separation during mitosis.","doi":"10.7554/eLife.89812","authors":"Colin L, Reyes C, Berthezene J, Maestroni L, Modolo L, Toselli E, Chanard N, Schaak S, Cuvier O, Gachet Y, Coulon S, Bernard P, Tournier S","authors_abbrev":"Colin L et al.","pubmed_publication_date":"21 Nov 2023","pubmed_entrez_date":"2023-11-21","publication_year":"2023","canto_session_key":"e8cf3680d2266cd1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-11-22 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9451802","title":"Size control in the cell cycle.","citation":"Cell Biol Int 1997 Aug;21(8):461-3","abstract":"","authors":"Mitchison JM, Novak B, Sveiczer A","authors_abbrev":"Mitchison JM et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17070958","title":"SR proteins: a foot on the exon before the transition from intron to exon definition.","citation":"Trends Genet 2007 Jan;23(1):5-7","abstract":"Two recent publications illuminate the evolution of alternative splicing, showing that a SR (serine-arginine-rich) protein that regulates alternative splicing in multicellular organisms is also found in a unicellular organism without alternative splicing, in which it can assist in the splicing of weak introns. Moreover, insertion of SR proteins into an organism lacking such proteins can restore the splicing of weak introns. These results imply that SR proteins had already facilitated the splicing of weak introns before the evolution of alternative splicing.","authors":"Ram O, Ast G","authors_abbrev":"Ram O et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2006-10-31","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40901732","title":"Induction of post-meiotic DNA double-strand breaks by the Pnu1 endonuclease in  Schizosaccharomyces pombe .","citation":"Mol Biol Cell 2025 Sep 03;:mbcE25050246","abstract":"Meiosis is a source of genetic variation in eukaryotes. Meiosis in the eukaryotic fission yeast  Schizosaccharomyces pombe  leads to the formation of spores that are particularly resistant to environmental stresses. In addition to external factors, internal processes may nevertheless contribute to cellular stress and impact the genome. This study investigates the role of Pnu1 as the major meiotic nuclease in  S. pombe . Transcription and cellular expression of Pnu1 are regulated upon specific phases of meiosis while its mitochondrial localization is also altered during this process. As a result, Pnu1 induces fragmentation of both genomic and mitochondrial DNA in the post meiotic phase. This sugar-non-specific endonuclease generates random double-strand breaks across the genome, an activity that appears to be mediated by direct interaction with chromatin. Given the high spore viability (∼95%) and the widespread occurrence of this phenomenon, this fragmentation appears to be physiological rather than apoptotic as observed in mammals. EndoG is the mammalian homolog of Pnu1 and is a caspases-independent apoptotic endonuclease that can allow cell survival. This study further describes the dynamics of Pnu1 action and support the conclusion that Pnu1 is a major meiotic endonuclease of  S. pombe  responsible for a transient post-meiotic fragmentation of cellular DNA potentially contributing to genetic variability.","doi":"10.1091/mbc.E25-05-0246","authors":"Mourrain L, Cavé T, Boissonneault G","authors_abbrev":"Mourrain L et al.","pubmed_publication_date":"03 Sep 2025","pubmed_entrez_date":"2025-09-03","publication_year":"2025","canto_session_key":"be795f552b08bebf","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-03 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31235585","title":"Structural basis for adenylation and thioester bond formation in the ubiquitin E1.","citation":"Proc Natl Acad Sci U S A 2019 Jul 30;116(31):15475-15484","abstract":"The ubiquitin (Ub) and Ub-like (Ubl) protein-conjugation cascade is initiated by E1 enzymes that catalyze Ub/Ubl activation through C-terminal adenylation, thioester bond formation with an E1 catalytic cysteine, and thioester bond transfer to Ub/Ubl E2 conjugating enzymes. Each of these reactions is accompanied by conformational changes of the E1 domain that contains the catalytic cysteine (Cys domain). Open conformations of the Cys domain are associated with adenylation and thioester transfer to E2s, while a closed conformation is associated with pyrophosphate release and thioester bond formation. Several structures are available for Ub E1s, but none has been reported in the open state before pyrophosphate release or in the closed state. Here, we describe the structures of  Schizosaccharomyces pombe  Ub E1 in these two states, captured using semisynthetic Ub probes. In the first, with a Ub-adenylate mimetic (Ub-AMSN) bound, the E1 is in an open conformation before release of pyrophosphate. In the second, with a Ub-vinylsulfonamide (Ub-AVSN) bound covalently to the catalytic cysteine, the E1 is in a closed conformation required for thioester bond formation. These structures provide further insight into Ub E1 adenylation and thioester bond formation. Conformational changes that accompany Cys-domain rotation are conserved for SUMO and Ub E1s, but changes in Ub E1 involve additional surfaces as mutational and biochemical analysis of residues within these surfaces alter Ub E1 activities.","doi":"10.1073/pnas.1905488116","authors":"Hann ZS, Ji C, Olsen SK, Lu X, Lux MC, Tan DS, Lima CD","authors_abbrev":"Hann ZS et al.","pubmed_publication_date":"30 Jul 2019","pubmed_entrez_date":"2019-06-26","publication_year":"2019","canto_session_key":"803b4beeddd658b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-08-13 10:47:54","canto_approved_date":"2019-08-13 10:47:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-13 09:41:08","canto_added_date":"2019-06-28 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.12c","SPBC1604.21c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-08-13","pdb_entries":[{"pdb_id":"6o82","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A/C","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-76"}],"title":"S. pombe ubiquitin E1 complex with a ubiquitin-AMP mimic","entry_authors":"Olsen SK,Lima CD","entry_authors_abbrev":"Olsen SK et al.","reference_uniquename":"PMID:31235585","experimental_method":"X-ray","resolution":"2.604"},{"pdb_id":"6o83","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A/C","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-75"}],"title":"S. pombe ubiquitin E1~ubiquitin-AMP tetrahedral intermediate mimic","entry_authors":"Hann ZS,Lima CD","entry_authors_abbrev":"Hann ZS et al.","reference_uniquename":"PMID:31235585","experimental_method":"X-ray","resolution":"3.153"}]},{"uniquename":"PMID:20501954","title":"Search for kinases related to transition of growth polarity in fission yeast.","citation":"Biosci Biotechnol Biochem 2010;74(5):1129-33","abstract":"In eukaryotes, cell polarity is essential for cell proliferation, differentiation, and development. It is regulated in 3 steps: establishment, maintenance, and transition. Compared to current knowledge of establishment and maintenance, the mechanism regulating the transition of cell polarity is poorly understood. In fission yeast during the G2 phase, growth polarity undergoes a dramatic transition, from monopolar to bipolar growth (termed NETO: new end take off). In this study, we screened systematically for protein kinases related to NETO using a genome-wide kinase deletion library. Analysis of these deletions suggested that 35 and 2 kinases had a putative positive and a negative role, respectively, in NETO. Moreover, 5 kinases were required for NETO-delay in the G1-arrested cdc10 mutant. These results suggest that many signaling pathways are involved in the regulation of NETO.","authors":"Koyano T, Kume K, Konishi M, Toda T, Hirata D","authors_abbrev":"Koyano T et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-05-27","publication_year":"2010","canto_session_key":"c5648278e253b705","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-06-27 17:42:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-08 12:16:36","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":103,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPAC2F7.03c","SPAC1F3.02c","SPBC4F6.06","SPAC1D4.11c","SPAC2C4.14c","SPAC22E12.14c","SPBC337.04","SPAC23A1.06c","SPAC2F3.15","SPCC16C4.11","SPAC3C7.06c","SPCC74.03c","SPBC12D12.04c","SPBC119.08","SPAC1D4.13","SPCC1919.01","SPAC1006.09","SPAC644.06c","SPBC18H10.15","SPBC543.07","SPAC29A4.16","SPCC1450.11c","SPACUNK12.02c","SPAC17G8.14c","SPAC31G5.09c","SPAC890.03","SPAC1687.15","SPBC3H7.15","SPBC106.10","SPAC12B10.14c","SPBC530.14c","SPAC1805.01c","SPAC823.03","SPCC24B10.07","SPBC336.12c","SPBC409.07c","SPAC1805.05","SPBC119.07","SPAC167.01","SPCC297.03","SPBC21.07c","SPAC23H4.17c","SPAC9G1.02","SPAC4G8.05","SPCC18B5.03"],"gene_count":46,"ltp_gene_count":46,"approved_date":"2014-08-08"},{"uniquename":"PMID:17013412","title":"Organizing cytoplasmic microtubules: no nucleus, no problem.","citation":"Nat Cell Biol 2006 Oct;8(10):1041-3","abstract":"","authors":"Horio T, Toda T","authors_abbrev":"Horio T et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-10-03","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19394293","title":"An alpha motif at Tas3 C terminus mediates RITS cis spreading and promotes heterochromatic gene silencing.","citation":"Mol Cell 2009 Apr 24;34(2):155-67","abstract":"RNA interference (RNAi) plays a pivotal role in the formation of heterochromatin at the fission yeast centromeres. The RNA-induced transcriptional silencing (RITS) complex, composed of heterochromatic small interfering RNAs (siRNAs), the siRNA-binding protein Ago1, the chromodomain protein Chp1, and the Ago1/Chp1-interacting protein Tas3, provides a physical tether between the RNAi and heterochromatin assembly pathways. Here, we report the structural and functional characterization of a C-terminal Tas3 alpha-helical motif (TAM), which self-associates into a helical polymer and is required for cis spreading of RITS in centromeric DNA regions. Site-directed mutations of key residues within the hydrophobic monomer-monomer interface disrupt Tas3-TAM polymeric self-association in vitro and result in loss of gene silencing, spreading of RITS, and a dramatic reduction in centromeric siRNAs in vivo. These results demonstrate that, in addition to the chromodomain of Chp1 and siRNA-loaded Ago1, Tas3 self-association is required for RITS spreading and efficient heterochromatic gene silencing at centromeric repeat regions.","doi":"10.1016/j.molcel.2009.02.032","authors":"Li H, Motamedi MR, Yip CK, Wang Z, Walz T, Patel DJ, Moazed D","authors_abbrev":"Li H et al.","pubmed_publication_date":"24 Apr 2009","pubmed_entrez_date":"2009-04-28","publication_year":"2009","canto_session_key":"55b9bee3eb3b5a49","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-09 19:03:12","canto_approved_date":"2023-03-09 19:03:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-01 12:44:03","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC83.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-03-09","pdb_entries":[{"pdb_id":"3d1d","gene_chains":[{"gene_uniquename":"SPBC83.03c","chain":"A/B/C/D/E/F","position":"426-545"}],"title":"Hexagonal crystal structure of Tas3 C-terminal alpha motif","entry_authors":"Li H,Patel DJ","entry_authors_abbrev":"Li H et al.","reference_uniquename":"PMID:19394293","experimental_method":"X-ray","resolution":"2.6"},{"pdb_id":"3d1b","gene_chains":[{"gene_uniquename":"SPBC83.03c","chain":"A/B/C","position":"426-545"}],"title":"Tetragonal crystal structure of Tas3 C-terminal alpha motif","entry_authors":"Li H,Patel DJ","entry_authors_abbrev":"Li H et al.","reference_uniquename":"PMID:19394293","experimental_method":"X-ray","resolution":"1.7"}]},{"uniquename":"EMBL:AU009502","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24375893","title":"Identification of two forms of the Eso1 protein in Schizosaccharomyces pombe.","citation":"Cell Biol Int 2014 May;38(5):682-8","abstract":"In Schizosaccharomyces pombe, Eso1p is a protein fusion. Two-thirds of its N-terminus is conserved to budding yeast Rad30, which functions in error-free replication of UV-damaged DNA. A third of the C-terminus is highly conserved to budding yeast Eco1, a lysine acetyltransferase, which is essential for the establishment of cohesion. Both Rad30p and Eco1p need to be finely tuned in budding yeast. Given the distinct function existed in Rad30p and Eco1p, it is enigmatic how the Eso1p, the protein fusion regulated in S. pombe, works. We have identified two forms of the Eso1 protein by Western blot, and detected the Eco1-homology fragment by M/S analysis following TAP purification of Eso1 protein. The result raises the possibility that Eso1 might be processed in vivo to release the Eco1-homology fragment, which allows the independent regulation of Rad30-homology and Eco1-homology fragments.","doi":"10.1002/cbin.10230","authors":"Chen Z, Cao H, Guo W, Lu Y","authors_abbrev":"Chen Z et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2013-12-31","publication_year":"2014","canto_session_key":"9f2623bf1566ff37","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPD183","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9742395","title":"Byr4 and Cdc16 form a two-component GTPase-activating protein for the Spg1 GTPase that controls septation in fission yeast.","citation":"Curr Biol 1998 Aug 27;8(17):947-54","abstract":"Spatial and temporal control of cytokinesis ensures the accurate transmission of genetic material and the correct development of multicellular organisms. An excellent model system in which to study cytokinesis is Schizosaccharomyces pombe because there are similarities between cytokinesis in S. pombe and mammals and because genes involved in S. pombe cytokinesis have been characterized. In particular, formation of the septum is positively regulated by the Spg1 GTPase and its effector, the Cdc7 kinase. Septation is negatively regulated by Cdc16, a protein similar to GTPase-activating proteins (GAPs) for Ypt GTPases, and by Byr4, a protein of unknown biochemical function. This study investigates the relationship between Byr4, Cdc16, and Spg1.\nGenetic interactions were observed between byr4, cdc16, and spg1 mutants. Byr4 bound to Cdc16 and Spg1 in yeast two-hybrid assays and in coprecipitations in vitro and in yeast. Byr4 inhibited the dissociation and hydrolysis of GTP bound to Spg1, but when Byr4 and Cdc16 were combined together they displayed Spg1GAP activity in vitro; Cdc16 alone had no detectable GAP activity. The binding of Byr4 to Spg1 and the Byr4-Cdc16 Spg1GAP activity were specific because Byr4 and Cdc16 did not bind to or affect the GTPase activities of the seven known S pombe Ypt family GTPase.\nByr4 and Cdc16 form a two-component GAP for the Spg1 GTPase. Byr4 and Cdc16 appear to negatively regulate septation in S. pombe by modulating the nucleotide state of Spg1 possibly in a spatially or temporally controlled manner.","authors":"Furge KA, Wong K, Armstrong J, Balasubramanian M, Albright CF","authors_abbrev":"Furge KA et al.","pubmed_publication_date":"27 Aug 1998","pubmed_entrez_date":"1998-09-22","publication_year":"1998","canto_session_key":"88aac1769dbd1134","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-01 18:13:26","canto_approved_date":"2026-01-31 14:36:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-01 18:13:18","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPAC1565.06c","SPAC222.10c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-03-01"},{"uniquename":"EMBL:AU007055","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27902423","title":"Characterization of  cis -elements in the promoter of  trz2  encoding  Schizosaccharomyces pombe  mitochondrial tRNA 3'-end processing enzyme.","citation":"Microbiology (Reading) 2017 Jan;163(1):75-85","abstract":"The endonuclease tRNase Z is responsible for the 3'-end processing of tRNA precursors, which is one of the essential steps in tRNA maturation. The fission yeast  Schizosaccharomyces pombe  contains two essential tRNase Z L  genes ( trz1  and  trz2 ) involved in nuclear and mitochondrial tRNA 3'-end processing, respectively. Our previous studies suggest that  trz2  is expressed at a very low level. Here we report characterization of the  trz2  promoter. Using  lacZ  as a reporter, we show that the  trz2  promoter contains a HomolD box and a very weak diverged TATA element. The HomolD box is usually found in the promoters of  S. pombe  ribosomal protein genes.  lacZ  reporter assays suggest that the HomolD box regulates the expression of both  trz2  and the ribosomal protein gene  rps2501 , which are arranged head-to-head on opposite strands. Overexpression of Rrn7, a candidate HomolD box-binding protein, up-regulates expression of  lacZ  under the control of the  trz2  promoter or the  rps2501  promoter. Functional complementation studies suggest that the TATA-like element is essential for  trz2  expression, whereas the HomolD box may play a nonessential regulatory role. We also demonstrate that a 57 nt negative regulatory element (NRE) located between the HomolD box and the TATA-like element represses the expression of  lacZ  under the control of the  trz2  promoter. Our results suggest that the low-level  trz2  expression may arise from a low level of transcription caused by lack of a strong TATA box and the NRE. Our analysis also suggests that  trz2  and  rps2501  may be coregulated by the HomolD box.","doi":"10.1099/mic.0.000398","authors":"Liu J, Huang L, Wang Y, Huang Y","authors_abbrev":"Liu J et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2016-12-01","publication_year":"2017","canto_session_key":"7777e3bab77e1283","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2017-11-20 16:29:59","canto_approved_date":"2023-01-12 17:37:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-12 02:33:16","canto_added_date":"2016-12-03 01:15:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.15","SPBC336.09c","SPAC5D6.01","SPAC694.05c","SPAC1D4.10","SPBC3D6.03c"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2017-11-20"},{"uniquename":"PMID:8168485","title":"res2+, a new member of the cdc10+/SWI4 family, controls the 'start' of mitotic and meiotic cycles in fission yeast.","citation":"EMBO J 1994 Apr 15;13(8):1873-80","abstract":"In the fission yeast Schizosaccharomyces pombe, the cdc10+ and res1+ genes play a crucial role in the start of mitotic and meiotic cycles. They encode structurally related transcriptional complex proteins and regulate some S phase-specific genes. Here we report the identification of a new member of this family named as res2+. res2+ has been isolated as a multicopy suppressor of a res1- null mutant and specifies a 73 kDa protein, which has two copies of the Swi/ankyrin motif and shares the highest sequence and structure similarity with the Res1 protein. res2+ is largely redundant in function with res1+ and is required for the initiation of mitotic and premeiotic DNA synthesis, but has an additional role in meiotic division. Unlike res1+, res2+ is highly induced during conjugation and strongly depends on cdc10+ for its activity. We conclude that the fission yeast contains two functionally overlapping parallel 'start' systems, Res1-Cdc10 and Res2-Cdc10, the former of which plays a major role in mitotic cycle whereas the latter in meiotic cycle.","authors":"Miyamoto M, Tanaka K, Okayama H","authors_abbrev":"Miyamoto M et al.","pubmed_publication_date":"15 Apr 1994","pubmed_entrez_date":"1994-04-15","publication_year":"1994","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F3.09c","SPBC725.16","SPBC336.12c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:31599583","title":"Sparticolins A-G, Biologically Active Oxidized Spirodioxynaphthalene Derivatives from the Ascomycete  Sparticola junci .","citation":"J Nat Prod 2019 Oct 25;82(10):2878-2885","abstract":"To explore the chemical diversity of metabolites from new species of Dothideomycetes, the ex-type strain of  Sparticola junci  was investigated. Seven highly oxygenated and functionalized spirodioxynaphthalene natural products incorporating carboxyalkylidene-cyclopentanoid ( 1 - 4 ), carboxyl-functionalized oxabicyclo[3.3.0]octane ( 5 - 6 ), and annelated 2-cyclopentenone/δ-lactone ( 7 ) units, sparticolins A-G, were isolated from submerged cultures of the fungus. Their chemical structures including their relative (and absolute) configurations were established through spectroscopic and X-ray crystallographic analyses. Sparticolin B ( 2 ) exhibited inhibitory activity against the Gram-positive bacteria  Bacillus subtilis ,  Micrococcus luteus , and  Staphylococcus aureus , while sparticolin G ( 7 ) showed antifungal activities against  Schizosaccharomyces pombe  and  Mucor hiemalis . All other sparticolins were only weakly active against  S. aureus  and also showed weak activities against the nematode  Caenorhabditis elegans . Compounds  2  and  7  also showed moderate cytotoxic activities against seven mammalian cell lines.","doi":"10.1021/acs.jnatprod.9b00604","authors":"Phukhamsakda C, Macabeo APG, Huch V, Cheng T, Hyde KD, Stadler M","authors_abbrev":"Phukhamsakda C et al.","pubmed_publication_date":"25 Oct 2019","pubmed_entrez_date":"2019-10-11","publication_year":"2019","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2019-10-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28148853","title":"Large-Scale Immunoprecipitation from Fission Yeast Cell Extracts.","citation":"Cold Spring Harb Protoc 2017 Feb 01;2017(2)","abstract":"We outline immunoprecipitation (IP) procedures to isolate the large quantities of a molecule of interest that are required to identify posttranslational modifications (PTMs) in subsequent targeted mass spectrometry analysis. In situ denaturation by trichloroacetic acid precipitation inhibits the activities of modifying enzymes that could alter the PTM profile to preserve the PTMs on a target of interest throughout the precipitation step. In contrast, isolation of the same molecule with the nondenaturing variation on this IP procedure can maintain associations with partner molecules whose PTMs can also be mapped, albeit with the caveat that modifications could have occurred during the extended IP period.","doi":"10.1101/pdb.prot091595","authors":"Grallert A, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"01 Feb 2017","pubmed_entrez_date":"2017-02-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-02-04 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26563290","title":"Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling.","citation":"J Lipid Res 2016 Jan;57(1):6-24","abstract":"Glycosylphosphatidylinositols (GPIs) act as membrane anchors of many eukaryotic cell surface proteins. GPIs in various organisms have a common backbone consisting of ethanolamine phosphate (EtNP), three mannoses (Mans), one non-N-acetylated glucosamine, and inositol phospholipid, whose structure is EtNP-6Manα-2Manα-6Manα-4GlNα-6myoinositol-P-lipid. The lipid part is either phosphatidylinositol of diacyl or 1-alkyl-2-acyl form, or inositol phosphoceramide. GPIs are attached to proteins via an amide bond between the C-terminal carboxyl group and an amino group of EtNP. Fatty chains of inositol phospholipids are inserted into the outer leaflet of the plasma membrane. More than 150 different human proteins are GPI anchored, whose functions include enzymes, adhesion molecules, receptors, protease inhibitors, transcytotic transporters, and complement regulators. GPI modification imparts proteins with unique characteristics, such as association with membrane microdomains or rafts, transient homodimerization, release from the membrane by cleavage in the GPI moiety, and apical sorting in polarized cells. GPI anchoring is essential for mammalian embryogenesis, development, neurogenesis, fertilization, and immune system. Mutations in genes involved in remodeling of the GPI lipid moiety cause human diseases characterized by neurological abnormalities. Yeast Saccharomyces cerevisiae has >60 GPI-anchored proteins (GPI-APs). GPI is essential for growth of yeast. In this review, we discuss biosynthesis of GPI-APs in mammalian cells and yeast with emphasis on the lipid moiety.","doi":"10.1194/jlr.R063313","authors":"Kinoshita T, Fujita M","authors_abbrev":"Kinoshita T et al.","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2015-11-14","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1002.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23612539","title":"Lysine-specific histone demethylase LSD1 and the dynamic control of chromatin.","citation":"Biol Chem 2013 Aug;394(8):1019-28","abstract":"The flavin adenine dinucleotide-dependent amine oxidase LSD1 is the first molecularly defined histone demethylase, which specifically demethylates H3K4me1/me2. The enzyme dynamically controls a large variety of biological processes and is associated with protein complexes controlling transcriptional repression and activation. Molecular analysis of the Drosophila LSD1 homolog revealed new insights into the epigenetic control of heterochromatin formation during early embryogenesis, the establishment of transcriptional gene silencing and the epigenetic mechanisms associated with the maintenance of stem cell identity in primordial germline cells. This review summarizes our recent knowledge about the control of enzymatic activity and molecular function of LSD1 enzyme complexes in different model organisms including Schizosaccharomyces pombe, Drosophila and mammals. Finally, new developments in applied cancer research based on molecular analysis of LSD1 in cancer cells are discussed.","doi":"10.1515/hsz-2013-0119","authors":"Rudolph T, Beuch S, Reuter G","authors_abbrev":"Rudolph T et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-04-25","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28446597","title":"The histone variant H2A.Z promotes splicing of weak introns.","citation":"Genes Dev 2017 Apr 01;31(7):688-701","abstract":"Multiple lines of evidence implicate chromatin in the regulation of premessenger RNA (pre-mRNA) splicing. However, the influence of chromatin factors on cotranscriptional splice site usage remains unclear. Here we investigated the function of the highly conserved histone variant H2A.Z in pre-mRNA splicing using the intron-rich model yeast  Schizosaccharomyces pombe  Using epistatic miniarray profiles (EMAPs) to survey the genetic interaction landscape of the Swr1 nucleosome remodeling complex, which deposits H2A.Z, we uncovered evidence for functional interactions with components of the spliceosome. In support of these genetic connections, splicing-specific microarrays show that H2A.Z and the Swr1 ATPase are required during temperature stress for the efficient splicing of a subset of introns. Notably, affected introns are enriched for H2A.Z occupancy and more likely to contain nonconsensus splice sites. To test the significance of the latter correlation, we mutated the splice sites in an affected intron to consensus and found that this suppressed the requirement for H2A.Z in splicing of that intron. These data suggest that H2A.Z occupancy promotes cotranscriptional splicing of suboptimal introns that may otherwise be discarded via proofreading ATPases. Consistent with this model, we show that overexpression of splicing ATPase Prp16 suppresses both the growth and splicing defects seen in the absence of H2A.Z.","doi":"10.1101/gad.295287.116","authors":"Nissen KE, Homer CM, Ryan CJ, Shales M, Krogan NJ, Patrick KL, Guthrie C","authors_abbrev":"Nissen KE et al.","pubmed_publication_date":"01 Apr 2017","pubmed_entrez_date":"2017-04-28","publication_year":"2017","canto_session_key":"ba57135bde9e7e32","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-12-17 10:57:13","canto_approved_date":"2022-08-04 14:54:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-02 15:32:11","canto_added_date":"2017-04-29 00:15:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":72,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.14","SPCC550.02c","SPBC1861.08c","SPBC365.05c","SPBC19C2.08","SPAC607.03c","SPBC577.07","SPBC16H5.10c","SPCC1620.10","SPBC31F10.11c","SPAC4A8.09c","SPAC167.03c","SPAC19A8.13","SPAP8A3.06","SPBC146.07","SPBP35G2.09","SPBC3E7.13c","SPBC18H10.10c","SPBC4B4.09","SPBC16H5.05c","SPBC146.05c","SPAC29A4.08c","SPAC22F3.11c","SPCC10H11.02","SPAC31G5.01","SPBC6B1.07","SPAPJ698.03c","SPCC16A11.13","SPCP1E11.07c","SPAC227.12","SPCC10H11.01","SPCC162.01c","SPCC576.13","SPAC222.18","SPAC17A2.08c","SPAC9.03c","SPBPJ4664.05","SPAC23D3.08","SPBC1289.11","SPCC16A11.05c","SPBC24C6.11","SPBC19C2.01","SPBC29A3.07c","SPBC646.02","SPAC3A12.11c","SPAC644.12","SPBC3B9.02c","SPAC17G6.14c","SPBC13E7.02","SPAC688.03c","SPBC211.05","SPBC21C3.05","SPAC22A12.09c","SPBC13E7.01","SPBC1289.12","SPBC23E6.01c","SPBP22H7.07","SPAC27F1.09c","SPBC1861.04c","SPAC16.02c","SPBC215.12","SPAC3H5.04","SPBC887.05c","SPCC126.14","SPBC83.09c","SPCC188.11","SPBC1711.17","SPBC31E1.03","SPAC11E3.01c","SPAC22F8.10c","SPBC1289.02c","SPAC4F8.12c","SPBC839.10","SPBC11B10.10c","SPBC36.09","SPAC1486.03c","SPBC119.13c","SPAC4D7.13","SPCC1281.02c","SPBC6B1.10","SPAC29E6.02","SPCC962.06c","SPBC28F2.04c","SPBC337.06c","SPBC4B4.07c","SPCC63.11","SPBC211.02c","SPAC10F6.02c","SPCC4B3.14","SPAC23H3.02c","SPAC30D11.09","SPBC11C11.08","SPBC11C11.01","SPBC32F12.05c","SPBC8D2.09c","SPCC825.05c"],"gene_count":96,"ltp_gene_count":12,"approved_date":"2019-12-17"},{"uniquename":"PMID:9180132","title":"The Josef Steiner Lecture: CDKs and cell-cycle control in fission yeast: relevance to other eukaryotes and cancer.","citation":"Int J Cancer 1997 May 29;71(5):707-8","abstract":"","authors":"Nurse P","authors_abbrev":"Nurse P","pubmed_publication_date":"29 May 1997","pubmed_entrez_date":"1997-05-29","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25428987","title":"The Cdc15 and Imp2 SH3 domains cooperatively scaffold a network of proteins that redundantly ensure efficient cell division in fission yeast.","citation":"Mol Biol Cell 2015 Jan 15;26(2):256-69","abstract":"Schizosaccharomyces pombe cdc15 homology (PCH) family members participate in numerous biological processes, including cytokinesis, typically by bridging the plasma membrane via their F-BAR domains to the actin cytoskeleton. Two SH3 domain-containing PCH family members, Cdc15 and Imp2, play critical roles in S. pombe cytokinesis. Although both proteins localize to the contractile ring, with Cdc15 preceding Imp2, only cdc15 is an essential gene. Despite these distinct roles, the SH3 domains of Cdc15 and Imp2 cooperate in the essential process of recruiting other proteins to stabilize the contractile ring. To better understand the connectivity of this SH3 domain-based protein network at the CR and its function, we used a biochemical approach coupled to proteomics to identify additional proteins (Rgf3, Art1, Spa2, and Pos1) that are integrated into this network. Cell biological and genetic analyses of these SH3 partners implicate them in a range of activities that ensure the fidelity of cell division, including promoting cell wall metabolism and influencing cell morphogenesis.","doi":"10.1091/mbc.E14-10-1451","authors":"Ren L, Willet AH, Roberts-Galbraith RH, McDonald NA, Feoktistova A, Chen JS, Huang H, Guillen R, Boone C, Sidhu SS, Beckley JR, Gould KL","authors_abbrev":"Ren L et al.","pubmed_publication_date":"15 Jan 2015","pubmed_entrez_date":"2014-11-28","publication_year":"2015","canto_session_key":"d5300c7f4c45c39f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Janel R. Beckley","canto_first_approved_date":"2018-03-21 16:02:45","canto_approved_date":"2026-02-14 10:01:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-18 20:33:17","canto_added_date":"2014-11-29 01:17:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Janel R. Beckley","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPBC4F6.12","SPAC20G8.05c","SPAC16E8.08","SPAC9G1.06c","SPBC19G7.08c","SPBC83.18c","SPAC3G9.05","SPCC645.06c","SPBC11C11.02"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2018-03-21"},{"uniquename":"PMID:33008060","title":"Caffeine Stabilises Fission Yeast Wee1 in a Rad24-Dependent Manner but Attenuates Its Expression in Response to DNA Damage.","citation":"Microorganisms 2020 Sep 30;8(10)","abstract":"The widely consumed neuroactive compound caffeine has generated much interest due to its ability to override the DNA damage and replication checkpoints. Previously Rad3 and its homologues was thought to be the target of caffeine's inhibitory activity. Later findings indicate that the Target of Rapamycin Complex 1 (TORC1) is the preferred target of caffeine. Effective Cdc2 inhibition requires both the activation of the Wee1 kinase and inhibition of the Cdc25 phosphatase. The TORC1, DNA damage, and environmental stress response pathways all converge on Cdc25 and Wee1. We previously demonstrated that caffeine overrides DNA damage checkpoints by modulating Cdc25 stability. The effect of caffeine on cell cycle progression resembles that of TORC1 inhibition. Furthermore, caffeine activates the Sty1 regulated environmental stress response. Caffeine may thus modulate multiple signalling pathways that regulate Cdc25 and Wee1 levels, localisation and activity. Here we show that the activity of caffeine stabilises both Cdc25 and Wee1. The stabilising effect of caffeine and genotoxic agents on Wee1 was dependent on the Rad24 chaperone. Interestingly, caffeine inhibited the accumulation of Wee1 in response to DNA damage. Caffeine may modulate cell cycle progression through increased Cdc25 activity and Wee1 repression following DNA damage via TORC1 inhibition, as TORC1 inhibition increased DNA damage sensitivity.","doi":"10.3390/microorganisms8101512","authors":"Alao JP, Johansson-Sjölander J, Rallis C, Sunnerhagen P","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"30 Sep 2020","pubmed_entrez_date":"2020-10-03","publication_year":"2020","canto_session_key":"945752034ffb20ce","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-10-05 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:26986212","title":"Cuf2 Is a Transcriptional Co-Regulator that Interacts with Mei4 for Timely Expression of Middle-Phase Meiotic Genes.","citation":"PLoS One 2016;11(3):e0151914","abstract":"The Schizosaccharomyces pombe cuf2+ gene encodes a nuclear regulator that is required for timely activation and repression of several middle-phase genes during meiotic differentiation. In this study, we sought to gain insight into the mechanism by which Cuf2 regulates meiotic gene expression. Using a chromatin immunoprecipitation approach, we demonstrate that Cuf2 is specifically associated with promoters of both activated and repressed target genes, in a time-dependent manner. In case of the fzr1+ gene whose transcription is positively affected by Cuf2, promoter occupancy by Cuf2 results in a concomitant increased association of RNA polymerase II along its coding region. In marked contrast, association of RNA polymerase II with chromatin decreases when Cuf2 negatively regulates target gene expression such as wtf13+. Although Cuf2 operates through a transcriptional mechanism, it is unable to perform its function in the absence of the Mei4 transcription factor, which is a member of the conserved forkhead protein family. Using coimmunoprecipitation experiments, results showed that Cuf2 is a binding partner of Mei4. Bimolecular fluorescence complementation experiments brought further evidence that an association between Cuf2 and Mei4 occurs in the nucleus. Analysis of fzr1+ promoter regions revealed that two FLEX-like elements, which are bound by the transcription factor Mei4, are required for chromatin occupancy by Cuf2. Together, results reported here revealed that Cuf2 and Mei4 co-regulate the timely expression of middle-phase genes during meiosis.","doi":"10.1371/journal.pone.0151914","authors":"Ioannoni R, Brault A, Labbé S","authors_abbrev":"Ioannoni R et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-03-18","publication_year":"2016","canto_session_key":"d0c7146980e2f7ef","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC584.02","SPBC32H8.11"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11029034","title":"Protection of telomeres by the Ku protein in fission yeast.","citation":"Mol Biol Cell 2000 Oct;11(10):3265-75","abstract":"Schizosaccharomyces pombe cells survive loss of telomeres by a unique pathway of chromosome circularization. Factors potentially involved in this survival mechanism include the heterodimeric Ku protein and ligase IV, both of which are involved in the repair of DNA double-strand breaks in mammalian cells. Furthermore, Ku plays a role in telomere maintenance as well as in DNA double-strand break repair in Saccharomyces cerevisiae. We have identified Ku and ligase IV homologues in S. pombe and analyzed their functions during normal growth and in cells undergoing senescence. In the absence of either a Ku subunit (pku70(+)) or ligase IV (lig4(+)), nonhomologous DNA end-joining was severely reduced. Lack of functional Ku led to shorter but stable telomeres and caused striking rearrangements of telomere-associated sequences, indicating a function for Ku in inhibiting recombinational activities near chromosome ends. In contrast to S. cerevisiae, concurrent deletion of pku70(+) and the gene for the catalytic subunit of telomerase (trt1(+)) was not lethal, allowing for the first time the dissection of the roles of Ku during senescence. Our results support a model in which Ku protects chromosome termini from nucleolytic and recombinational activities but is not involved in the formation of chromosome end fusions during senescence. The conclusion that nonhomologous end-joining is not required for chromosome circularization was further supported by analysis of survivors in strains lacking the genes for both trt1(+) and lig4(+).","authors":"Baumann P, Cech TR","authors_abbrev":"Baumann P et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-10-12","publication_year":"2000","canto_session_key":"ac48987d259c18a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-09-05 15:00:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-13 11:47:17","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.02c","SPCC1183.05c","SPBC29A3.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-10-13"},{"uniquename":"EMBL:AU012819","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10207183","title":"Schizosaccharomyces pombe produces novel Gal0-2Man1-3 O-linked oligosaccharides.","citation":"Glycobiology 1999 May;9(5):507-15","abstract":"Schizosaccharomyces pombe whole-cell glycoproteins, previously depleted of N-linked glycans by sequential treatment with endo-ss-N-acetylglucosaminidase H and peptide-N4-asparagine amidohydrolase F, were ss-eliminated with 0.1 M NaOH/1 M NaBH4 to release the O-linked oligosaccharides. The saccharide-alditols were separated by gel-exclusion chromatography into pools from Hexitol to Hex4Hexitol in size. Analysis of the Hexitol pool indicated Man to be the only sugar linked to Ser or Thr residues. The Hex1Hexitol pool contained two components, Galalpha1,2Man-ol (2A) and Manalpha1, 2Man-ol (2B). The Hex2Hexitol pool contained two components, Galalpha1,2Manalpha1,2Man-ol (3A) and Manalpha1,2Manalpha1,2Man-ol (3B). The two Hex3Hexitol components were Galalpha1,2(Galalpha1, 3)Manalpha1,2Man-ol (4A) and Manalpha1,2(Galalpha1,3)Manalpha1, 2Man-ol (4B). The Hex4Hexitol component was found to be a single isomer with the composition of Galalpha1,2(Galalpha1,3)Manalpha1, 2Manalpha1,2Man-ol (5AB). Surprisingly, galactobiose was not detected in any of these oligosaccharides. The gma12 (T. G. Chappell and G. Warren (1989) J. Cell Biol., 109, 2693-2707) and gth1 (T. G. Chappell personal communication) alpha1, 2-galactosyltransferase-deficient mutants and the gma12/gth1 double mutant S.pombe strains were similarly examined. The results indicated that gma12p is solely responsible for the addition of terminal alpha1,2-linked Gal in compound 2A, while one or both of gma12p and gth1p are required for the alpha1,2-linked Gal in 4A. Both transferases are largely responsible for terminal Gal in isomer 5AB. Neither gma12 nor gth1 had any discernible effect on the structure of the large N-linked galactomannans as determined by 1H NMR spectroscopy. Thus, while gth1p and gma12p appear responsible for adding alpha1,2-linked Gal to terminal Man, neither adds galactose side chains to the N-linked poly alpha1,6-Man outerchain, nor the O-linked branch-forming alpha1,3-linked Gal. Furthermore, the presence of Hexalpha1,2(Galalpha1,3)Manalpha1,2- structures in the O-linked glycans implies the presence of a novel branch-forming alpha1,3-galactosyltransferase in S.pombe.","authors":"Gemmill TR, Trimble RB","authors_abbrev":"Gemmill TR et al.","pubmed_publication_date":"May 1999","pubmed_entrez_date":"1999-04-20","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31186279","title":"The asymmetric chemical structures of two mating pheromones reflect their differential roles in mating of fission yeast.","citation":"J Cell Sci 2019 Jun 25;132(12)","abstract":"In the fission yeast  Schizosaccharomyces pombe , the mating reaction is controlled by two mating pheromones, M-factor and P-factor, secreted by M- and P-type cells, respectively. M-factor is a C-terminally farnesylated lipid peptide, whereas P-factor is a simple peptide. To examine whether this chemical asymmetry in the two pheromones is essential for conjugation, we constructed a mating system in which either pheromone can stimulate both M- and P-cells, and examined whether the resulting autocrine strains can mate. Autocrine M-cells responding to M-factor successfully mated with P-factor-lacking P-cells, indicating that P-factor is not essential for conjugation; by contrast, autocrine P-cells responding to P-factor were unable to mate with M-factor-lacking M-cells. The sterility of the autocrine P-cells was completely restored by expressing the M-factor receptor. These observations indicate that the different chemical characteristics of the two types of pheromone, a lipid and a simple peptide, are not essential; however, a lipid peptide might be required for successful mating. Our findings allow us to propose a model of the differential roles of M-factor and P-factor in conjugation of  S. pombe This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.230722","authors":"Seike T, Maekawa H, Nakamura T, Shimoda C","authors_abbrev":"Seike T et al.","pubmed_publication_date":"25 Jun 2019","pubmed_entrez_date":"2019-06-13","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-06-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30730059","title":"Iron regulates hexose transporters in Schizosaccharomyces pombe.","citation":"J Basic Microbiol 2019 May;59(5):458-464","abstract":"This study focuses on the effect of iron on hexose transporters which perform glucose uptake. For this aim, we investigated the role of iron in glucose utilization and expression of hexose transporters in Schizosaccharomyces pombe. We applied different iron concentrations (1, 2, 5, 10 mM) to the cells grown up to mid-logarithmic phase. According to analysis of cell viability and morphology, we determined 2 mM and 5 mM as non-toxic and toxic doses, respectively. Besides, glucose consumption efficiency increased (1.5-fold) in the cells which were exposed to these iron concentrations. qRT-PCR analysis of hexose transporter genes showed that the expression of ght2 and ght8 genes were downregulated under both non-toxic and toxic iron conditions, but that of ght5 gene was significantly decreased only by toxic iron dose. In conclusion, it was suggested for the first time in this study that the Ght5 protein, as being high affinity hexose transporter, might play a role in sensing and signaling of iron stress.","doi":"10.1002/jobm.201800618","authors":"Özkan E, Kartal B, Yılmazer M, Palabıyık B","authors_abbrev":"Özkan E et al.","pubmed_publication_date":"May 2019","pubmed_entrez_date":"2019-02-08","publication_year":"2019","canto_session_key":"58baa149dfbd771b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-13 16:30:23","canto_approved_date":"2019-11-13 16:30:23","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-12 18:21:10","canto_added_date":"2019-02-09 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1235.14","SPBC4B4.08","SPBC1683.08","SPBC1348.14c","SPAC1F8.01","SPCC548.07c","SPCC1235.13","SPCC548.06c"],"gene_count":8,"ltp_gene_count":0,"approved_date":"2019-11-13"},{"uniquename":"PMID:21803169","title":"Cell polarity in fission yeast: a matter of confining, positioning, and switching growth zones.","citation":"Semin Cell Dev Biol 2011 Oct;22(8):799-805","abstract":"The two key processes in growth polarisation are the generation of a confined region and the correct positioning of that region. Fission yeast has greatly contributed to the study of cell polarisation, particularly in the aspect of growth site positioning, which involves the interphase microtubule cytoskeleton. Here we review the mechanisms of growth polarity in vegetatively growing fission yeast cells. These seemingly simple cells show astonishingly complex growth polarity behaviour, including polarity switching and integrating multiple levels of control by the cell cycle machinery. We aim to extract and highlight the underlying concepts and discuss these in context of current understanding; showing how relevant proteins are networked to integrate the various machineries.","doi":"10.1016/j.semcdb.2011.07.013","authors":"Huisman SM, Brunner D","authors_abbrev":"Huisman SM et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-08-02","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR10655","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.04c","HGNC:6737","HGNC:20440","SPAC9G1.08c","HGNC:6738"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:16998476","title":"Self-organization of microtubule bundles in anucleate fission yeast cells.","citation":"Nat Cell Biol 2006 Oct;8(10):1108-13","abstract":"Self-organization of cellular structures is an emerging principle underlying cellular architecture. Properties of dynamic microtubules and microtubule-binding proteins contribute to the self-assembly of structures such as microtubule asters. In the fission yeast Schizosaccharomyces pombe, longitudinal arrays of cytoplasmic microtubule bundles regulate cell polarity and nuclear positioning. These bundles are thought to be organized from the nucleus at multiple interphase microtubule organizing centres (iMTOCs). Here, we find that microtubule bundles assemble even in cells that lack a nucleus. These bundles have normal organization, dynamics and orientation, and exhibit anti-parallel overlaps in the middle of the cell. The mechanisms that are responsible for formation of these microtubule bundles include cytoplasmic microtubule nucleation, microtubule release from the equatorial MTOC (eMTOC), and the dynamic fusion and splitting of microtubule bundles. Bundle formation and organization are dependent on mto1p (gamma-TUC associated protein), ase1p (PRC1), klp2p (kinesin-14) and tip1p (CLIP-170). Positioning of nuclear fragments and polarity factors by these microtubules illustrates how self-organization of these bundles contributes to establishing global spatial order.","authors":"Daga RR, Lee KG, Bratman S, Salas-Pino S, Chang F","authors_abbrev":"Daga RR et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-09-26","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14474650","title":"The incorporation of protein and carbohydrate precursors during the cell cycle of a fission yeast.","citation":"Exp Cell Res 1962 Feb;26:144-57","abstract":"","authors":"MITCHISON JM, WILBUR KM","authors_abbrev":"MITCHISON JM et al.","pubmed_publication_date":"Feb 1962","pubmed_entrez_date":"1962-02-01","publication_year":"1962","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22750657","title":"Protein phosphatase Z modulates oxidative stress response in fungi.","citation":"Fungal Genet Biol 2012 Sep;49(9):708-16","abstract":"The genome of the filamentous fungus Aspergillus nidulans harbors the gene ppzA that codes for the catalytic subunit of protein phosphatase Z (PPZ), and the closely related opportunistic pathogen Aspergillus fumigatus encompasses a highly similar PPZ gene (phzA). When PpzA and PhzA were expressed in Saccharomyces cerevisiae or Schizosaccharomyces pombe they partially complemented the deleted phosphatases in the ppz1 or the pzh1 mutants, and they also mimicked the effect of Ppz1 overexpression in slt2 MAP kinase deficient S. cerevisiae cells. Although ppzA acted as the functional equivalent of the known PPZ enzymes its disruption in A. nidulans did not result in the expected phenotypes since it failed to affect salt tolerance or cell wall integrity. However, the inactivation of ppzA resulted in increased sensitivity to oxidizing agents like tert-butylhydroperoxide, menadione, and diamide. To demonstrate the general validity of our observations we showed that the deletion of the orthologous PPZ genes in other model organisms, such as S. cerevisiae (PPZ1) or Candida albicans (CaPPZ1) also caused oxidative stress sensitivity. Thus, our work reveals a novel function of the PPZ enzyme in A. nidulans that is conserved in very distantly related fungi.","doi":"10.1016/j.fgb.2012.06.010","authors":"Leiter É, González A, Erdei É, Casado C, Kovács L, Ádám C, Oláh J, Miskei M, Molnar M, Farkas I, Hamari Z, Ariño J, Pócsi I, Dombrádi V","authors_abbrev":"Leiter É et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-07-04","publication_year":"2012","canto_session_key":"94a5caadf150bcfe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-03-27 16:22:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-03-27 16:21:59","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-03-27"},{"uniquename":"PMID:33579781","title":"Transcriptional profiling of fission yeast RNA polymerase II CTD mutants.","citation":"RNA 2021 Feb 12;27(5):560-70","abstract":"The carboxyl-terminal domain (CTD) of RNA polymerase II (Pol2) consists of tandem repeats of a consensus heptapeptide Y 1  S 2  P 3  T 4  S 5  P 6  S 7  The CTD recruits numerous proteins that drive or regulate gene expression. The trafficking of CTD-interacting proteins is orchestrated by remodeling CTD primary structure via Ser/Thr/Tyr phosphorylation and proline  cis-trans  isomerization, which collectively inscribe a CTD code. The fission yeast CTD consists of 29 heptad repeats. To decipher the output of the fission yeast CTD code, we genetically manipulated CTD length and amino acid content and then gauged the effects of these changes on gene expression. Whereas deleting 11 consensus heptads has no obvious effect on fission yeast growth, RNA-seq revealed that 25% of the protein-coding transcripts were dysregulated by CTD truncation. We profiled the transcriptomes of full-length CTD mutants, in which: all Tyr1 residues were replaced by Phe; all Ser2, Thr4, or Ser7 positions were changed to Ala; and half of the essential CTD code \"letters\" Pro3, Ser5, and Pro6 were mutated to Ala. Overlapping RNA-seq profiles suggested that a quarter of the complement of up-regulated mRNAs and half of the down-regulated mRNAs seen in full-length CTD mutants might be attributable to a decrement in wild-type CTD heptad number. Concordant mutant-specific transcriptional profiles were observed for  Y1F ,  S2A , and  T4A  cells, and for  P6•P6A  and  S5•S5A  cells, suggesting that Tyr1-Ser2-Thr4 and Ser5-Pro6 comprise distinct \"words\" in the fission yeast CTD code. The phosphate regulon, which is repressed by lncRNA-mediated transcription interference, is de-repressed by CTD mutations P6•P6A and S5•S5A. De-repression of pho1 in P6•P6A and S5•S5A cells depends on cleavage and polyadenylation factor subunits Swd22 and Ppn1 and transcription termination factor Rhn1, signifying that Pro6 and Ser5 mutations elicit precocious lncRNA 3'-processing/termination.","doi":"10.1261/rna.078682.121","authors":"Garg A, Sanchez AM, Schwer B, Shuman S","authors_abbrev":"Garg A et al.","pubmed_publication_date":"12 Feb 2021","pubmed_entrez_date":"2021-02-13","publication_year":"2021","canto_session_key":"66d1d84a63cd8a3e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Angad Garg","canto_first_approved_date":"2022-11-18 13:52:23","canto_approved_date":"2024-03-19 08:06:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-15 21:28:33","canto_added_date":"2021-02-15 01:15:04","annotation_curators":[{"name":"Angad Garg","community_curator":true,"annotation_count":29,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.02c","SPAC1F7.08","SPAC824.04","SPAC23G3.02c","SPAC3G9.04","SPBC776.02c","SPBC28F2.12","SPBC4F6.09","SPAC1F8.03c","SPAC1F7.07c","SPAC1F8.02c","SPBC1271.09","SPCC74.02c","SPAC23G3.03","SPBC337.03","SPBC8E4.01c","SPBC3B9.11c","SPBP4G3.02","SPBC1683.09c"],"gene_count":19,"ltp_gene_count":6,"approved_date":"2022-11-18"},{"uniquename":"EMBL:AJ632017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.50"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12568722","title":"A simple Cre-loxP method for chromosomal N-terminal tagging of essential and non-essential Schizosaccharomyces pombe genes.","citation":"Gene 2003 Jan 30;304:133-41","abstract":"To facilitate the N-terminal tagging of essential genes at their genomic locus and under control of their own promoters we have developed a series of novel polymerase chain reaction templates. Initially, a 1.8 kb DNA fragment is integrated upstream of the ATG of the gene of interest. This fragment encodes the tag, a loxP site, a selectable marker, an exogenous nmt1 promoter and a second loxP site. In a single homologous integration event, the gene of interest is placed under control of the thiamine regulated nmt1 promoter, allowing identification of potential integrants on the basis of phenotype. Subsequently, this integrant strain is transformed with a plasmid expressing the Cre recombinase. This results in excision of the marker and nmt1 promoter and leaves sequences encoding an in-frame tag at the N-terminus of the gene of interest under the control of its native promoter. We have created TAP-cdc22, TAP-suc22 and TAP-rad50 strains using this N-tagging system, and developed a range of vectors for introducing TAP-, (His)10HA-, (His)6Myc- and EGFP.","authors":"Werler PJ, Hartsuiker E, Carr AM","authors_abbrev":"Werler PJ et al.","pubmed_publication_date":"30 Jan 2003","pubmed_entrez_date":"2003-02-06","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27749909","title":"A New Membrane Protein Sbg1 Links the Contractile Ring Apparatus and Septum Synthesis Machinery in Fission Yeast.","citation":"PLoS Genet 2016 Oct;12(10):e1006383","abstract":"Cytokinesis in many organisms requires a plasma membrane anchored actomyosin ring, whose contraction facilitates cell division. In yeast and fungi, actomyosin ring constriction is also coordinated with division septum assembly. How the actomyosin ring interacts with the plasma membrane and the plasma membrane-localized septum synthesizing machinery remains poorly understood. In Schizosaccharomyces pombe, an attractive model organism to study cytokinesis, the β-1,3-glucan synthase Cps1p / Bgs1p, an integral membrane protein, localizes to the plasma membrane overlying the actomyosin ring and is required for primary septum synthesis. Through a high-dosage suppressor screen we identified an essential gene, sbg1+ (suppressor of beta glucan synthase 1), which suppressed the colony formation defect of Bgs1-defective cps1-191 mutant at higher temperatures. Sbg1p, an integral membrane protein, localizes to the cell ends and to the division site. Sbg1p and Bgs1p physically interact and are dependent on each other to localize to the division site. Loss of Sbg1p results in an unstable actomyosin ring that unravels and slides, leading to an inability to deposit a single contiguous division septum and an important reduction of the β-1,3-glucan proportion in the cell wall, coincident with that observed in the cps1-191 mutant. Sbg1p shows genetic and / or physical interaction with Rga7p, Imp2p, Cdc15p, and Pxl1p, proteins known to be required for actomyosin ring integrity and efficient septum synthesis. This study establishes Sbg1p as a key member of a group of proteins that link the plasma membrane, the actomyosin ring, and the division septum assembly machinery in fission yeast.","doi":"10.1371/journal.pgen.1006383","authors":"Sethi K, Palani S, Cortés JC, Sato M, Sevugan M, Ramos M, Vijaykumar S, Osumi M, Naqvi NI, Ribas JC, Balasubramanian M","authors_abbrev":"Sethi K et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-10-18","publication_year":"2016","canto_session_key":"a0155f941d09ffb2","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-10-19 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP22H7.03","SPAC20G8.05c","SPBC11C11.02","SPBC23G7.08c","SPBC19G7.05c","SPBC4F6.12","SPAC1782.09c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:34523683","title":"Cdc42 reactivation at growth sites is regulated by local cell-cycle-dependent loss of its GTPase-activating protein Rga4 in fission yeast.","citation":"J Cell Sci 2021 Oct 01;134(19)","abstract":"In fission yeast, polarized cell growth stops during division and resumes after cytokinesis completes and cells separate. It is unclear how growth reactivation is timed to occur immediately after cell separation. We uncoupled these sequential events by delaying cytokinesis with a temporary Latrunculin A treatment. Mitotic cells recovering from treatment initiate end growth during septation, displaying a polar elongation simultaneous with septation (PrESS) phenotype. PrESS cell ends reactivate Cdc42, a major regulator of polarized growth, during septation, but at a fixed time after anaphase B. A candidate screen implicates Rga4, a negative regulator of Cdc42, in this process. We show that Rga4 appears punctate at the cell sides during G2, but is diffuse during mitosis, extending to the ends. Although the Morphogenesis Orb6 (MOR) pathway is known to promote cell separation and growth by activating protein synthesis, we find that, for polarized growth, removal of Rga4 from the ends is also necessary. Therefore, we propose that growth resumes after division once the MOR pathway is activated and the ends lose Rga4 in a cell-cycle-dependent manner.","doi":"10.1242/jcs.259291","authors":"Rich-Robinson J, Russell A, Mancini E, Das M","authors_abbrev":"Rich-Robinson J et al.","pubmed_publication_date":"01 Oct 2021","pubmed_entrez_date":"2021-09-15","publication_year":"2021","canto_session_key":"b985cb4ee3e632ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maitreyi Das","canto_first_approved_date":"2025-03-26 10:22:32","canto_approved_date":"2025-03-26 10:22:32","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-03-01 15:08:46","canto_added_date":"2021-09-17 00:15:04","annotation_curators":[{"name":"Maitreyi Das","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":8,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC17F3.02","SPAC110.03","SPBP19A11.04c","SPAC24B11.06c","SPAC24H6.09","SPCC1223.06","SPBC28E12.03"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2025-03-26"},{"uniquename":"PMID:12707717","title":"An inventory of the P-type ATPases in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 2003 Jul;43(4):273-80","abstract":"The analysis of the Schizosaccharomyces pombe genome revealed the presence of 14 putative P-type ATPases. The clustering of ATPases resembles that of Saccharomyces cerevisiae, indicating that the main classes of pumps were already present before the split of the Archiascomycetes from the other Ascomycota. The overall amino acid identity between fission and budding yeast P-type ATPases is generally low (30-50%). This is similar to the fungus-plant and fungus-animal comparisons, suggesting that fungal ATPases underwent an extensive process of diversification. Unlike Sac. cerevisiae, fission yeast lacks Na(+)-ATPases, has a single heavy-metal ATPase and three ATPases of unknown specificity. The observed divergence within these fungi might reflect physiological differences, including adaptation to environmental stresses.","authors":"Okorokova-Façanha AL, Okorokov LA, Ekwall K","authors_abbrev":"Okorokova-Façanha AL et al.","pubmed_publication_date":"Jul 2003","pubmed_entrez_date":"2003-04-23","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6094975","title":"The mitochondrial genome of the fission yeast Schizosaccharomyces pombe. 3. Gene mapping in strain EF1 (CBS 356) and analysis of hybrids between the strains EF1 and ade7-50h-.","citation":"Mol Gen Genet 1984;196(3):473-81","abstract":"The Schizosaccharomyces pombe strain EF1 (CBS 356) is haploid, prototrophic, respiratory competent, and of homothallic mating type. From restriction enzyme analysis the length of the mitochondrial genome is 17.3 kilobase pairs, which is in good agreement with the value of 17.1 kilobase pairs determined by electron microscopy. The mitochondrial genome of strain EF1 is thus about 2.3 kilobase pairs shorter than that of strain ade7-50h- (about 19.4 kilobase pairs). A restriction map was constructed for 11 enzymes: For most, but not all of them, the pattern is nearly identical to that of strain ade7-50h-. The genes for the large ribosomal RNA, the subunits 1, 2, and 3 of cytochrome c oxidase, subunits 6 and 9 of ATP synthetase, and cytochrome b were localized by hybridization with mitochondrial DNA probes from Saccharomyces cerevisiae. The gene order was found to be the same in both yeast strains. From Southern hybridization of strain ade7-50h- with nick-translated mitochondrial DNA from strain EF1 it is evident that strain EF1 does not possess the intron, which is present in the cytochrome b gene of Schizosaccharomyces pombe strain ade7-50h-. Crosses between strain ade7-50h- and EF1 demonstrate that both the nuclear and the mitochondrial genomes are able to recombine. The mitochondrial genomes of 2 out of 30 independently isolated hybrids between the two strains are described as the result of recombination between the two parental mitochondrial genomes.","authors":"Zimmer M, Lückemann G, Lang BF, Wolf K","authors_abbrev":"Zimmer M et al.","pubmed_publication_date":"1984","pubmed_entrez_date":"1984-01-01","publication_year":"1984","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010234","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16299000","title":"Inactivation of homocitrate synthase causes lysine auxotrophy in copper/zinc-containing superoxide dismutase-deficient yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 2006 Jan 20;281(3):1345-51","abstract":"The fission yeast Schizosaccharomyces pombe lacking copper/zinc-containing superoxide dismutase (CuZn-SOD) is auxotrophic for lysine and sulfurous amino acids under aerobic growth conditions. A multicopy suppressor gene (phx1+) that restored the growth of CuZn-SOD-deficient cells on minimal medium was isolated. It encodes a putative DNA-binding protein with a conserved homeobox domain. Overproduction of Phx1 increased the amount of several proteins, and one of those turned out to be a putative homocitrate synthase (HCS) encoded by the lys4+ gene in S. pombe as judged by mass spectrometric analysis. Consistent with this observation, overexpression of the lys4+ gene increased HCS enzyme activity and was sufficient to suppress the lysine requirement of the CuZn-SOD-deficient cells. Enzyme activity and Western blot analyses revealed that the activity and protein level of HCS were dramatically reduced upon depletion of CuZn-SOD. Treatment of exponentially growing S. pombe cells with paraquat, a superoxide generator, caused a decrease in the amount of Lys4 protein as expected. These results led us to conclude that HCS, the first enzyme in the alpha-aminoadipate-mediated pathway for lysine synthesis common in fungi and some bacteria, is a labile target of oxidative stress caused by CuZn-SOD depletion and that its synthesis is positively regulated by the putative transcriptional regulator Phx1.","authors":"Kwon ES, Jeong JH, Roe JH","authors_abbrev":"Kwon ES et al.","pubmed_publication_date":"20 Jan 2006","pubmed_entrez_date":"2005-11-22","publication_year":"2006","canto_session_key":"110f413a16dde4e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-07 17:09:34","canto_approved_date":"2026-03-09 15:52:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-16 07:44:05","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC32A11.03c","SPAC821.10c","SPBC1105.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-09-07"},{"uniquename":"PMID:40829803","title":"MoDorado: enhanced detection of tRNA modifications in nanopore sequencing by off-label use of modification callers.","citation":"Nucleic Acids Res 2025 Aug 11;53(15)","abstract":"Rapid and accurate identification of transfer RNA (tRNA) modifications is crucial for understanding their role in protein translation and disease. However, their detection on tRNAs is challenging due to high modification density. With the release of the nanopore direct RNA sequencing kit SQK-RNA004, de novo modification calling models became available for pseudouridine (Ψ), m6A, inosine, and m5C, as part of the Dorado basecaller. By applying the Ψ model to tRNAs, we mapped both known and previously uncharacterized Ψ sites in Schizosaccharomyces pombe, and identified the corresponding pseudouridine synthases. This led to the discovery of two novel modification sites, Pus7-dependent Ψ8 and Pus1-dependent Ψ22. Furthermore, we have developed MoDorado, an algorithm to detect modifications beyond those used in model training (\"off-label use\"). It does so by assessing differences in modification predictions between modified and nonmodified samples using pre-trained, modification-specific models. By repurposing the Ψ/m6A/inosine/m5C models, MoDorado detected seven additional modifications (ncm5U, mcm5U, mcm5s2U, m7G, queuosine, m1A, and i6A), thus generating an expanded map of these tRNA modifications in S. pombe. This work provides a generalized framework for leveraging pre-trained models in determining the intricate landscape of tRNA modifications.","doi":"10.1093/nar/gkaf795","authors":"Rübsam FNM, Liu-Wei W, Sun Y, Patel BI, van der Toorn W, Piechotta M, Dieterich C, Kleist MV, Ehrenhofer-Murray AE","authors_abbrev":"Rübsam FNM et al.","pubmed_publication_date":"11 Aug 2025","pubmed_entrez_date":"2025-08-19","publication_year":"2025","canto_session_key":"13da312bf804d2d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ann Ehrenhofer-Murray","canto_first_approved_date":"2025-09-17 18:25:54","canto_approved_date":"2025-10-29 07:51:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-09-03 07:46:13","canto_added_date":"2025-08-20 23:25:04","annotation_curators":[{"name":"Ann Ehrenhofer-Murray","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC343.15","SPBC3H7.10","SPAC25B8.05","SPAC18B11.02c","SPBC800.08","SPBC11C11.10","SPCPB16A4.04c","SPCC16C4.06c","SPCC126.03","SPBC887.11","SPBC1A4.09"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2025-09-17"},{"uniquename":"PMID:34749087","title":"Phenolic compound profiles in Finnish apple (Malus × domestica Borkh.) juices and ciders fermented with Saccharomyces cerevisiae and Schizosaccharomyces pombe strains.","citation":"Food Chem 2022 Mar 30;373(Pt B):131437","abstract":"The phenolic compounds in juices and ciders made with Saccharomyces cerevisiae or Schizosaccharomyces pombe from eleven Finnish apple cultivars were analyzed using liquid chromatographic and mass spectrometric methods combined with multivariate data analysis. In general, the ciders contained less phenolic compounds than corresponding apple juices. In the studied apple juices and ciders, hydroxycinnamic acids were the most predominant, accounting for around 80% of total phenolic compounds. Apple juices contained more flavonol glycosides and dihydrochalcones whereas cider processing resulted in increased amount of free hydroxycinnamic acids. The contents of individual phenolic compounds were more dependent on the apple cultivars than the yeast species. Certain cultivars contained remarkably higher contents of dihydrochalcones and hydroxycinnamic acids when comparing with other cultivars. Ciders made using S. pombe remained higher contents of procyanidins and (+)-catechin while S. cerevisiae ciders contained higher individual hydroxycinnamic acids, such as 5-O-caffeoylquinic acid, 4-O-caffeoylquinic acid, 3-O-p-coumaroylquinic acid, and 4-O-p-coumaroylquinic acid.","doi":"10.1016/j.foodchem.2021.131437","authors":"He W, Laaksonen O, Tian Y, Heinonen M, Bitz L, Yang B","authors_abbrev":"He W et al.","pubmed_publication_date":"30 Mar 2022","pubmed_entrez_date":"2021-11-08","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-11-10 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15843986","title":"Preliminary crystallographic analysis of the Cks protein p13(suc1P90AP92A) from Schizosacharromyces pombe.","citation":"Eur Biophys J 2005 Jul;34(5):430-3","abstract":"The p13(suc1) is the fission yeast member of the Cks (Cdc28-dependant kinase subunit) family of proteins. The Cks proteins bind to and are required for the function of cyclin-dependant kinase (Cdk) proteins during cell cycle progression in eukaryotic cells. Two conformations of Cks have been detected crystallographically; a compact monomer with the C-terminal fourth beta-strand inserted into the core of the molecule between strands 2 and 3, and a strand-exchanged dimer where the fourth beta-strand is inserted into the core of the dimer partner in an equivalent position. There is a highly conserved \"hinge\" region consisting of the motif PEP, N-terminal to the fourth beta-strand. In the monomer this motif constitutes a beta-turn, while in the dimeric structure it is extended, allowing strand exchange. The mutant protein p13(suc1P90AP92A), in which alanine residues replace both prolines of the turn, provides an opportunity to examine the role of the prolines in this hinge region and how they may allow for the formation of strand-exchanged dimers by Cks proteins. We have expressed and purified this mutant protein. Two millimolar p13(suc1P90AP92A) crystallised in 50 mM tris(hydroxymethyl)aminomethane pH 7.5, 30% poly(ethylene glycol) 1500. Diffraction data were collected at room temperature on an MAR345 image plate using Cu Kalpha radiation from a Rigaku RU200 rotating-anode generator source to 2.70A. The crystal has unit cell parameters a=b=75.1 A, c=34.9 A, alpha=beta=90 degrees , gamma=120 degrees. Diffraction data were indexed to the space group P6 and systematic absences 00l indicate a screw axis consistent with P6(3).","authors":"Kelly JA, Williams EA, Wilce MC","authors_abbrev":"Kelly JA et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-04-22","publication_year":"2005","canto_session_key":"93312a0c6167bade","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-06 09:48:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 09:48:10","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1734.14c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-06"},{"uniquename":"PMID:10407262","title":"The topoisomerase I poison camptothecin generates a Chk1-dependent DNA damage checkpoint signal in fission yeast.","citation":"Yeast 1999 Jul;15(10A):821-8","abstract":"The protein kinase Chk1 is essential for the DNA damage checkpoint. Cells lacking Chk1 are hypersensitive to DNA-damaging agents such as UV light and gamma-irradiation because they fail to arrest the cell cycle when DNA damage is generated. Phosphorylation of Chk1 occurs after DNA damage and is dependent on the integrity of the DNA damage checkpoint pathway. We have tested whether a topoisomerase I inhibitor, camptothecin (CPT), generates DNA damage in the fission yeast Schizosaccharomyces pombe that results in Chk1 phosphorylation. We demonstrate that Chk1 is phosphorylated in response to CPT treatment in a time- and dose-dependent manner and that phosphorylation is dependent on an intact DNA damage checkpoint pathway. Furthermore, we show that cells must be actively dividing in order for CPT to generate a Chk1-responsive DNA damage signal. This observation is consistent with a model whereby the cytotoxic event caused by CPT treatment is the production of a DNA double-strand break resulting from the collision of a DNA replication fork with a trapped CPT-topoisomerase I cleavable complex. Cells lacking Chk1 are hypersensitive to CPT treatment, suggesting that the DNA damage checkpoint pathway can be an important determinant for CPT sensitivity or resistance. Finally, as a well-characterized, soluble agent that specifically causes DNA damage, CPT will allow a biochemical analysis of the checkpoint pathway that responds to DNA damage.","authors":"Wan S, Capasso H, Walworth NC","authors_abbrev":"Wan S et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-17","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC1952.07","SPBC1703.14c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10966477","title":"Regulation of chromosome replication.","citation":"Annu Rev Biochem 2000;69:829-80","abstract":"The initiation of DNA replication in eukaryotic cells is tightly controlled to ensure that the genome is faithfully duplicated once each cell cycle. Genetic and biochemical studies in several model systems indicate that initiation is mediated by a common set of proteins, present in all eukaryotic species, and that the activities of these proteins are regulated during the cell cycle by specific protein kinases. Here we review the properties of the initiation proteins, their interactions with each other, and with origins of DNA replication. We also describe recent advances in understanding how the regulatory protein kinases control the progress of the initiation reaction. Finally, we describe the checkpoint mechanisms that function to preserve the integrity of the genome when the normal course of genome duplication is perturbed by factors that damage the DNA or inhibit DNA synthesis.","authors":"Kelly TJ, Brown GW","authors_abbrev":"Kelly TJ et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-08-31","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009909","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29046339","title":"A checkpoint-independent mechanism delays entry into mitosis after UV irradiation.","citation":"J Cell Sci 2017 Dec 01;130(23):4028-4037","abstract":"When cells are exposed to stress they delay entry into mitosis. The most extensively studied mechanism behind this delay is the DNA-damage-induced G2/M checkpoint. Here, we show the existence of an additional stress-response pathway in  Schizosaccharomyces pombe  that is independent of the classic ATR/Rad3-dependent checkpoint. This novel mechanism delays entry mitosis independently of the spindle assembly checkpoint and the mitotic kinases Fin1, Ark1 and Plo1. The pathway delays activation of the mitotic cyclin-dependent kinase (CDK) Cdc2 after UV irradiation. Furthermore, we demonstrate that translation of the mitotic cyclin Cdc13 is selectively downregulated after UV irradiation, and we propose that this downregulation of Cdc13 contributes to the delayed activation of Cdc2 and the delayed mitosis.","doi":"10.1242/jcs.204693","authors":"Rothe C, Rødland GE, Anda S, Stonyte V, Boye E, Lopez-Aviles S, Grallert B","authors_abbrev":"Rothe C et al.","pubmed_publication_date":"01 Dec 2017","pubmed_entrez_date":"2017-10-20","publication_year":"2017","canto_session_key":"4e4a86f0fc5eb0d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-10-05 12:34:52","canto_approved_date":"2018-10-05 12:34:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-09-06 14:31:53","canto_added_date":"2017-12-05 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC216.05"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2018-10-05"},{"uniquename":"PMID:29369362","title":"Influence of Selected Saccharomyces and Schizosaccharomyces Strains and Their Mixed Cultures on Chemical Composition of Apple Wines.","citation":"J Food Sci 2018 Feb;83(2):424-431","abstract":"Currently in apple winemaking, pure cultures of Saccharomyces cerevisiae and S. bayanus strains are mainly used. The aim of this study was to determine the influence of Saccharomyces cerevisiae (Johannisberg Riesling - LOCK 105), S. bayanus (DSMZ 3774), S. paradoxus (CBS 7302), and Schizosaccharomyces pombe (DSMZ 70576) applied in pure and mixed cultures on the chemical composition and sensory profile of apple wines. Pasteurized Gloster apple musts with addition of sucrose (up to 22°Blg) were inoculated with specific volume (0.6 g dry weight per liter) of yeast pure or mixed cultures (in a ratio of 1:1, 1:1:1, or 1:1:1:1) and fermented for 28 d at 22 °C. The influence of pure/mixed culture on the chemical composition, volatile profile, and sensory properties of apple wines was determined using high-performance liquid chromatography (HPLC) and gas chromatography (GC) methods. All pure culture of yeasts used for the apple wines production are characterized by good enological profiles. S. bayanus and Sch. pombe are the most distinct to S. cerevisiae. S. bayanus strain increases the level of malic acid and carbonyl compounds in apple wines, whereas Sch. pombe highly deacidifies it and produces the most of glycerol, esters, and acetic acid. The wines obtained with these 2 species gained also, respectively, the best and the worse notes during sensory analysis. Mixed cultures (in most cases) produce greater amounts of ethanol, methanol, and volatile esters compared to pure cultures. The presence of S. bayanus in the mixed culture is beneficial for the quality of apple wines.\nGood understanding of the properties of yeasts and the procedures for their selection will make it easier to find strains that could improve the quality of wine. Since wine is formed by the action of a number of species and strains of yeasts, many authors have studied the effect of mixed cultures on the final quality of the product. Most of this research was focused on the effect of the inoculation of Saccharomyces yeast with other species on the aroma of wine. However, there is a little data on the fermentation using simultaneous inoculation of different strains of S. cerevisiae.","doi":"10.1111/1750-3841.14042","authors":"Satora P, Semik-Szczurak D, Tarko T, Bułdys A","authors_abbrev":"Satora P et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2018-01-26","publication_year":"2018","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2018-01-27 01:15:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31315658","title":"Leo1 is essential for the dynamic regulation of heterochromatin and gene expression during cellular quiescence.","citation":"Epigenetics Chromatin 2019 Jul 17;12(1):45","abstract":"Cellular quiescence is a reversible differentiation state during which cells modify their gene expression program to inhibit metabolic functions and adapt to a new cellular environment. The epigenetic changes accompanying these alterations are not well understood. We used fission yeast cells as a model to study the regulation of quiescence. When these cells are starved for nitrogen, the cell cycle is arrested in G1, and the cells enter quiescence (G0). A gene regulatory program is initiated, including downregulation of thousands of genes-for example, those related to cell proliferation-and upregulation of specific genes-for example, autophagy genes-needed to adapt to the physiological challenge. These changes in gene expression are accompanied by a marked alteration of nuclear organization and chromatin structure.\nHere, we investigated the role of Leo1, a subunit of the conserved RNA polymerase-associated factor 1 (Paf1) complex, in the quiescence process using fission yeast as the model organism. Heterochromatic regions became very dynamic in fission yeast in G0 during nitrogen starvation. The reduction of heterochromatin in early G0 was correlated with reduced target of rapamycin complex 2 (TORC2) signaling. We demonstrated that cells lacking Leo1 show reduced survival in G0. In these cells, heterochromatic regions, including subtelomeres, were stabilized, and the expression of many genes, including membrane transport genes, was abrogated. TOR inhibition mimics the effect of nitrogen starvation, leading to the expression of subtelomeric genes, and this effect was suppressed by genetic deletion of leo1.\nWe identified a protein, Leo1, necessary for survival during quiescence. Leo1 is part of a conserved protein complex, Paf1C, linked to RNA polymerase II. We showed that Leo1, acting downstream of TOR, is crucial for the dynamic reorganization of chromosomes and the regulation of gene expression during cellular quiescence. Genes encoding membrane transporters are not expressed in quiescent leo1 mutant cells, and cells die after 2 weeks of nitrogen starvation. Taken together, our results suggest that Leo1 is essential for the dynamic regulation of heterochromatin and gene expression during cellular quiescence.","doi":"10.1186/s13072-019-0292-7","authors":"Oya E, Durand-Dubief M, Cohen A, Maksimov V, Schurra C, Nakayama JI, Weisman R, Arcangioli B, Ekwall K","authors_abbrev":"Oya E et al.","pubmed_publication_date":"17 Jul 2019","pubmed_entrez_date":"2019-07-19","publication_year":"2019","canto_session_key":"624d205232adf87e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Karl Ekwall","canto_first_approved_date":"2020-09-30 06:43:20","canto_approved_date":"2020-11-03 17:43:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-21 11:30:00","canto_added_date":"2019-07-20 00:15:04","annotation_curators":[{"name":"Karl Ekwall","community_curator":true,"annotation_count":5,"orcid":"0000-0002-3029-4041","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.14c","SPAC664.03","SPBC17G9.02c","SPBC13E7.08c","SPCC24B10.07"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-09-30"},{"uniquename":"PMID:40578557","title":"Phosphorylation-mediated Regulation of the NADPH-dependent Glutamate Dehydrogenase, SpGdh1, from Schizosaccharomyces pombe.","citation":"J Biol Chem 2025 Jun 25;:110422","abstract":"Glutamate dehydrogenase from the yeast Schizosaccharomyces pombe (SpGdh1) is a pivotal enzyme that catalyzes the conversion of 2-oxoglutarate and ammonium to glutamate using NADPH as a coenzyme. Although SpGdh1 is phosphorylated at several residues, the impact of phosphorylation on enzyme activity and the underlying molecular mechanisms remain unclear. To elucidate the phosphorylation-mediated regulation of SpGdh1, we determined the crystal structure of SpGdh1 binding 2-iminoglutarate (2-IG) and NADP + . The results of the structural analysis revealed that four serine residues for phosphorylation were located near the active site. Ser252 directly interacted with the 2'-phosphate group of the adenine ribose moiety of NADP + , suggesting that the phosphorylation of Ser252 interfered with NADP +  binding. To confirm this hypothesis, we prepared SpGdh1 phosphorylation-mimic (Ser to Glu) variants of SpGdh1 at these four Ser residues. The results of a kinetic analysis revealed that the replacement of these four residues increased the apparent K m  NADP(H)  value and decreased catalytic efficiency, k cat /K m  NADP(H) .In contrast, substitutions decreased the apparent K m  NAD(H)  value and increased catalytic efficiency, k cat /K m  NAD(H) . Therefore, the Ser to Glu replacement caused net shifts in the coenzyme specificities (NADPH to NADH and NADP +  to NAD + ) of 55- and 2900-fold, respectively. This is the first study to reveal the effects of the phosphorylation of SpGdh1 on its activity.","doi":"10.1016/j.jbc.2025.110422","authors":"Wang YF, Tomita T, Yoshida A, Kosono S, Nishiyama M","authors_abbrev":"Wang YF et al.","pubmed_publication_date":"25 Jun 2025","pubmed_entrez_date":"2025-06-27","publication_year":"2025","canto_session_key":"6a6fa7401876491c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-06-28 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC622.12c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"9kl6","gene_chains":[{"gene_uniquename":"SPCC622.12c","chain":"A","position":"2-451"}],"title":"Crystal structure of NADP-specific glutamate dehydrogenase Gdh1 from Schizosaccharomyces pombe in complex with alpha-iminoglutarate and NADP+","entry_authors":"Tomita T,Yoshida A,Nishiyama M","entry_authors_abbrev":"Tomita T et al.","reference_uniquename":"PMID:40578557","experimental_method":"X-ray","resolution":"1.45"}]},{"uniquename":"PMID:12056900","title":"Purification and partial characterization of a DNA 3'-phosphatase from Schizosaccharomyces pombe.","citation":"Biochemistry 2002 Jun 18;41(24):7688-94","abstract":"Cells that depend on oxygen for survival constantly produce reactive oxygen species that attack DNA to produce a variety of lesions, including single-strand breaks with 3'-blocking groups such as 3'-phosphate and 3'-phosphoglycolate. These 3'-blocking ends prevent the activity of DNA polymerase and are generally removed by DNA repair proteins with 3'-diesterase activity. We report here the purification and partial characterization of a 45 kDa protein from Schizosaccharomyces pombe total extract based on the ability of this protein to process bleomycin- or H(2)O(2)-damaged DNA in vitro to allow DNA repair synthesis by DNA polymerase I. Further analysis revealed that the 45 kDa protein removes 3'-phosphate ends created by the Escherichia coli fpg AP lyase following the incision of AP site but is unable to process the 3'-alpha,beta unsaturated aldehyde generated by E. coli endonuclease III. The protein cannot cleave DNA bearing AP sites, suggesting that it is not an AP endonuclease or AP lyase. We conclude that the 45 kDa protein purified from S. pombe is a DNA 3'-phosphatase.","authors":"Jilani A, Ramotar D","authors_abbrev":"Jilani A et al.","pubmed_publication_date":"18 Jun 2002","pubmed_entrez_date":"2002-06-12","publication_year":"2002","canto_session_key":"d23920dd53aeb0c5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-20 13:52:58","canto_approved_date":"2019-12-03 19:18:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 09:34:27","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-20"},{"uniquename":"PMID:28515144","title":"Transient activation of fission yeast AMPK is required for cell proliferation during osmotic stress.","citation":"Mol Biol Cell 2017 Jul 01;28(13):1804-1814","abstract":"The heterotrimeric kinase AMPK acts as an energy sensor to coordinate cell metabolism with environmental status in species from yeast through humans. Low intracellular ATP leads to AMPK activation through phosphorylation of the activation loop within the catalytic subunit. Other environmental stresses also activate AMPK, but it is unclear whether cellular energy status affects AMPK activation under these conditions. Fission yeast AMPK catalytic subunit Ssp2 is phosphorylated at Thr-189 by the upstream kinase Ssp1 in low-glucose conditions, similar to other systems. Here we find that hyperosmotic stress induces strong phosphorylation of Ssp2-T189 by Ssp1. Ssp2-pT189 during osmotic stress is transient and leads to transient regulation of AMPK targets, unlike sustained activation by low glucose. Cells lacking this activation mechanism fail to proliferate after hyperosmotic stress. Activation during osmotic stress requires energy sensing by AMPK heterotrimer, and osmotic stress leads to decreased intracellular ATP levels. We observed mitochondrial fission during osmotic stress, but blocking fission did not affect AMPK activation. Stress-activated kinases Sty1 and Pmk1 did not promote AMPK activation but contributed to subsequent inactivation. Our results show that osmotic stress induces transient energy stress, and AMPK activation allows cells to manage this energy stress for proliferation in new osmotic states.","doi":"10.1091/mbc.E17-04-0235","authors":"Schutt KL, Moseley JB","authors_abbrev":"Schutt KL et al.","pubmed_publication_date":"01 Jul 2017","pubmed_entrez_date":"2017-05-19","publication_year":"2017","canto_session_key":"cf2b7c05db3b7535","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Katherine Schutt","canto_first_approved_date":"2018-11-02 15:17:14","canto_approved_date":"2025-09-03 14:22:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-29 19:13:09","canto_added_date":"2017-05-20 00:15:13","annotation_curators":[{"name":"Katherine Schutt","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC1556.08c","SPAC57A10.02","SPBC215.05","SPAC24B11.06c","SPCC297.03","SPAC767.01c","SPBC1D7.02c","SPBC12C2.08","SPAC23D3.04c","SPCC74.03c","SPCC1919.03c","SPBC119.08"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2018-11-02"},{"uniquename":"PMID:17523390","title":"Cell wall ultrastructure of flocculent and non-flocculent Schizosaccharomyces pombe strains. Effect of cell wall hydrolysing enzymes on flocculation and cell wall ultastructure.","citation":"Acta Microbiol Immunol Hung 2007 Mar;54(1):35-46","abstract":"Scanning and transmission electron microscopic studies revealed the presence of slime-like, amorphous material on the surface of Schizosaccahromyces pombe RIVE 4-2-1 cells, independently, whether they were in flocculated or in non-flocculated state. Close contact of the adjacent cells via the merging outermost cell wall layers was found, however, only in the case of floc formation, which was induced by cultivating the cells in the presence of 6% (v/v) ethanol. Irreversible loss of the flocculation ability of the cells by treatment with proteinases suggests that proteinaceous cell surface molecules as lectins contribute to the cell-to-cell interaction during flocculation. Both proteinase K and pronase treatments removed a distinct outer layer of the cell wall, which indicated that the protein moieties of the phosphogalactomannan outer surface layer has a crucial role in the maintenance of cell wall integrity. In the case of lysing enzyme treatment the removal of the outermost layer was also observed as the first step of the cell wall digestion, while driselase treatment resulted in almost complete digestion of the cell wall.","authors":"Geleta A, Kristóf Z, Maráz A","authors_abbrev":"Geleta A et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-05-26","publication_year":"2007","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33475472","title":"Atg43, a novel autophagy-related protein, serves as a mitophagy receptor to bridge mitochondria with phagophores in fission yeast.","citation":"Autophagy 2021 Mar;17(3):826-827","abstract":"Mitophagy is a selective type of autophagy in which damaged or unnecessary mitochondria are sequestered by double-membranous structures called phagophores and delivered to vacuoles/lysosomes for degradation. The molecular mechanisms underlying mitophagy have been studied extensively in budding yeast and mammalian cells. To gain more diverse insights, our recent study identified Atg43 as a mitophagy receptor in the fission yeast  Schizosaccharomyces pombe . Atg43 is localized on the mitochondrial outer membrane through the Mim1-Mim2 complex and binds to Atg8, a ubiquitin-like protein conjugated to phagophore membranes. Artificial tethering of Atg8 to mitochondria can bypass the requirement of Atg43 for mitophagy, suggesting that the main role of Atg43 in mitophagy is to stabilize phagophore expansion on mitochondria by interacting with Atg8. Atg43 shares no sequence similarity with mitophagy receptors in other organisms and has a mitophagy-independent function, raising the possibility that Atg43 has acquired the mitophagic function by convergent evolution.","doi":"10.1080/15548627.2021.1874662","authors":"Fukuda T, Kanki T","authors_abbrev":"Fukuda T et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2021-01-21","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-01-23 01:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.01c","SPBP8B7.24c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"EMBL:D89104","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7744766","title":"Isolation of Schizosaccharomyces pombe isopentenyl diphosphate isomerase cDNA clones by complementation and synthesis of the enzyme in Escherichia coli.","citation":"J Biol Chem 1995 May 12;270(19):11298-303","abstract":"Isopentenyl diphosphate (IPP) isomerase catalyzes an essential activation step in the isoprene biosynthetic pathway. The Saccharomyces cerevisiae gene for IPP isomerase, IDI1, was recently isolated and characterized (Anderson, M. S., Muehlbacher, M., Street, I. P., Proffitt, J., and Poulter, C. D. (1989) J. Biol. Chem. 264, 19169-19175), and the wild-type gene, IDI1, was disrupted with a LEU2 marker to create a diploid yeast strain heterozygous for the idi1::leu2 disruption, which revealed that IDI1 was an essential single-copy gene (Mayer, M.P., Hahn, F. M., Stillman, D. J., and Poulter, C. D. (1992) Yeast 8, 743-748). We now report the isolation of a cDNA clone from Schizosaccharomyces pombe by a plasmid shuffle-mediated complementation of the LEU2 disrupted yeast gene. The S. pombe clone encoded a 26,864-dalton polypeptide of 227 amino acids with a high degree of similarity to the S. cerevisiae IDI1 enzyme. S. pombe IPP isomerase contained the essential Cys and Glu catalytic residues identified in yeast isomerase (Street, I. P., Coffman, H. R., Baker, J., and Poulter, C. (1994) Biochemistry 33, 4212-4217) but was significantly smaller than the S. cerevisiae enzyme. The plasmid shuffle technique is an excellent procedure for screening expression libraries for IPP isomerase activity by complementation of the idi1 mutation.","authors":"Hahn FM, Poulter CD","authors_abbrev":"Hahn FM et al.","pubmed_publication_date":"12 May 1995","pubmed_entrez_date":"1995-05-12","publication_year":"1995","canto_session_key":"49f1cecbd98bcc9a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-28 17:08:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-21 11:10:46","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-21"},{"uniquename":"PMID:31666919","title":"Rho Family GTPases in Fission Yeast Cytokinesis.","citation":"Commun Integr Biol 2019;12(1):171-180","abstract":"During cytokinesis, actomyosin ring constriction drives furrow formation. In animal cells, Rho GTPases drive this process through the positioning and assembly of the actomyosin ring, and through extracellular matrix remodeling within the furrow. In the fission yeast  S. pombe , actomyosin ring constriction and septum formation are concurrent processes. While  S. pombe  is the primary source from which the mechanics of ring assembly and constriction stem, much less is known about the regulation of Rho GTPases that control these processes. Of the six Rho GTPases encoded in  S. pombe , only Rho1, the RhoA homologue, has been shown to be essential for cytokinesis. While Rho3, Rho4, and Cdc42 have defined roles in cytokinesis, Rho2 and Rho5 play minor to no roles in this process. Here we review the roles of the Rho GTPases during cytokinesis, with a focus on their regulation, and discuss whether crosstalk between GTPases, as has been reported in other organisms, exists during cytokinesis in  S. pombe .","doi":"10.1080/19420889.2019.1678453","authors":"Hercyk B, Das M","authors_abbrev":"Hercyk B et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-11-01","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-11-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.09","SPAC16A10.04","SPAC16E8.09","SPAC1F7.04","SPAC20H4.11c","SPAC23C4.08","SPAC110.03","SPAC16.01"],"gene_count":8,"ltp_gene_count":0},{"uniquename":"PMID:16548067","title":"A parallel proteomic and metabolomic analysis of the hydrogen peroxide- and Sty1p-dependent stress response in Schizosaccharomyces pombe.","citation":"Proteomics 2006 May;6(9):2772-96","abstract":"Using an integrated approach incorporating proteomics, metabolomics and published mRNA data, we have investigated the effects of hydrogen peroxide on wild type and a Sty1p-deletion mutant of the fission yeast Schizosaccharomyces pombe. Differential protein expression analysis based on the modification of proteins with matched fluorescent labelling reagents (2-D-DIGE) is the foundation of the quantitative proteomics approach. This study identifies 260 differentially expressed protein isoforms from 2-D-DIGE gels using MALDI MS and reveals the complexity of the cellular response to oxidative stress and the dependency on the Sty1p stress-activated protein kinase. We show the relationship between these protein changes and mRNA expression levels identified in a parallel whole genome study, and discuss the regulatory mechanisms involved in protecting cells against hydrogen peroxide and the involvement of Sty1p-dependent stress-activated protein kinase signalling. Metabolomic profiling of 29 intermediates using 1H NMR was also conducted alongside the protein analysis using the same sample sets, allowing examination of how the protein changes might affect the metabolic pathways and biological processes involved in the oxidative stress response. This combined analysis identifies a number of interlinked metabolic pathways that exhibit stress- and Sty1-dependent patterns of regulation.","authors":"Weeks ME, Sinclair J, Butt A, Chung YL, Worthington JL, Wilkinson CR, Griffiths J, Jones N, Waterfield MD, Timms JF","authors_abbrev":"Weeks ME et al.","pubmed_publication_date":"May 2006","pubmed_entrez_date":"2006-03-21","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16394583","title":"The cation-transporting P-type ATPase Cta4 is required for assembly of the forespore membrane in fission yeast.","citation":"Genes Genet Syst 2005 Oct;80(5):317-24","abstract":"A novel sporulation-deficient mutant, sev4-L5, was isolated in a genetic screen of a collection of temperature-sensitive mutants of Schizosaccharomyces pombe. The wild-type sev4 gene was identified as cta4+, which encodes a putative cation-transporting P-type ATPase. The sev4-L5 allele harbored a single missense mutation that caused replacement of Gly615 with a glutamate at the putative ATP-binding site. Similar to cta4-null mutants, sev4-L5 exhibited defects in growth at high and low temperatures, and sensitivity to high and extremely low concentrations of Ca2+. The cta4+ mRNA level was considerably enhanced during meiosis. When sev4-L5 cells were incubated in sporulation medium at the permissive temperature, meiotic nuclear divisions proceeded with normal kinetics, but spores were not formed. Structural alteration of the spindle pole body, which is prerequisite to construction of the forespore membrane in wild type, was incomplete. Consequently, formation of the forespore membrane was severely impaired. These observations show that perturbation of Ca2+ homeostasis by mutation of cta4/sev4 blocks sporulation mainly by interfering with forespore membrane assembly.","authors":"Yoshida SH, Nakamura T, Shimoda C","authors_abbrev":"Yoshida SH et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2006-01-06","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPACUNK4.07c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:20639859","title":"14-3-3gamma mediates Cdc25A proteolysis to block premature mitotic entry after DNA damage.","citation":"EMBO J 2010 Aug 18;29(16):2802-12","abstract":"14-3-3 proteins control various cellular processes, including cell cycle progression and DNA damage checkpoint. At the DNA damage checkpoint, some subtypes of 14-3-3 (beta and zeta isoforms in mammalian cells and Rad24 in fission yeast) bind to Ser345-phosphorylated Chk1 and promote its nuclear retention. Here, we report that 14-3-3gamma forms a complex with Chk1 phosphorylated at Ser296, but not at ATR sites (Ser317 and Ser345). Ser296 phosphorylation is catalysed by Chk1 itself after Chk1 phosphorylation by ATR, and then ATR sites are rapidly dephosphorylated on Ser296-phosphorylated Chk1. Although Ser345 phosphorylation is observed at nuclear DNA damage foci, it occurs more diffusely in the nucleus. The replacement of endogenous Chk1 with Chk1 mutated at Ser296 to Ala induces premature mitotic entry after ultraviolet irradiation, suggesting the importance of Ser296 phosphorylation in the DNA damage response. Although Ser296 phosphorylation induces the only marginal change in Chk1 catalytic activity, 14-3-3gamma mediates the interaction between Chk1 and Cdc25A. This ternary complex formation has an essential function in Cdc25A phosphorylation and degradation to block premature mitotic entry after DNA damage.","doi":"10.1038/emboj.2010.157","authors":"Kasahara K, Goto H, Enomoto M, Tomono Y, Kiyono T, Inagaki M","authors_abbrev":"Kasahara K et al.","pubmed_publication_date":"18 Aug 2010","pubmed_entrez_date":"2010-07-20","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC24H6.05","SPAC8E11.02c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:30246828","title":"Biosynthesis and isolation of selenoneine from genetically modified fission yeast.","citation":"Metallomics 2018 Oct 17;10(10):1532-1538","abstract":"Selenoneine, a naturally occurring form of selenium, is the selenium analogue of ergothioneine, a sulfur species with health relevance not only as a purported antioxidant but likely also beyond. Selenoneine has been speculated to exhibit similar effects. To study selenoneine's health properties as well as its metabolic transformation, the pure compound is required. Chemical synthesis of selenoneine, however, is challenging and biosynthetic approaches have been sought. We herein report the biosynthesis and isolation of selenoneine from genetically modified fission yeast Schizosaccharomyces pombe grown in a medium containing sodium selenate. After cell lysis and extraction with methanol, selenoneine was purified by three consecutive preparative reversed-phase HPLC steps. The product obtained at the mg level was characterised by high resolution mass spectrometry, NMR and HPLC/ICPMS. Biosynthesis was found to be a promising alternative to chemical synthesis, and should be suitable for upscaling to produce higher amounts of this important selenium species in the future.","doi":"10.1039/c8mt00200b","authors":"Turrini NG, Kroepfl N, Jensen KB, Reiter TC, Francesconi KA, Schwerdtle T, Kroutil W, Kuehnelt D","authors_abbrev":"Turrini NG et al.","pubmed_publication_date":"17 Oct 2018","pubmed_entrez_date":"2018-09-25","publication_year":"2018","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2018-09-26 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1577774","title":"Isolation and characterization of a second protein tyrosine phosphatase gene, PTP2, from Saccharomyces cerevisiae.","citation":"J Biol Chem 1992 May 15;267(14):10024-30","abstract":"A putative protein tyrosine phosphatase (PTPase) gene, PTP2, was cloned from Saccharomyces cerevisiae. The complete yeast PTP2 gene encodes a 750-amino acid residue protein with a predicted mass of 86 kDa. The conserved PTPase domain was localized in the C-terminal half of the protein. Amino acid sequence alignment of the yeast PTPase domain with other phosphatases indicated approximately 20-25% sequence identity with the mammalian PTPase and a similar degree of identity with the PTPase encoded by the yeast PTP1 gene. The PTP2 gene is closely linked to the yeast RET1 and STE4 genes and is localized on the right arm of chromosome 15. Gene disruption experiments demonstrated that neither PTP2 alone nor PTP2 in combination with PTP1 was essential for growth under the conditions tested. The ability of PTP2 to complement the cdc25-22 mutant of Schizosaccharomyces pombe was also examined, and unlike the human T-cell PTPase, which was able to complement the cdc25-22 mutant, the S. cerevisiae PTP2 was unable to complement the cdc25-22 mutant of S. pombe.","authors":"Guan K, Deschenes RJ, Dixon JE","authors_abbrev":"Guan K et al.","pubmed_publication_date":"15 May 1992","pubmed_entrez_date":"1992-05-15","publication_year":"1992","canto_session_key":"908e30fc914304d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 11:59:58","canto_session_submitted_date":"2012-03-03 11:59:41","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"EMBL:AB084850","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.1493"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34344846","title":"An RNAi-independent role of AP1-like stress response factor Pap1 in centromere and mating-type silencing in  Schizosaccaromyces pombe .","citation":"J Biosci 2021;46","abstract":"Gene silencing in  S. pombe  occurs by heterochromatin formation at the centromere ( cen ), mating-type ( mat ) and telomere loci. It is mediated by silencing factors including Swi6, Clr1-4, Rhp6 and Pola. RNAi pathway also plays a role in establishment of silencing at the  mat  and  cen  loci. Recently, the stress response factors, Atf1 and Pcr1were shown to play an RNAi-independent role in silencing at the  mat3  locus through a  cis -acting Atf1-binding site located within the repression element  REIII  and recruitment of the silencing factors Clr3 and Clr6. Another  cis -acting site, named repression element  REII  abutting the  mat2  locus, also establishes heterochromatin structure through Clr5 and histone deacetylases but independently of H3-Lys9-methylation and RNAi. Here, we report the occurrence of binding sites for another oxidative response factor, the pombe AP1- like factor Pap1, at the mating-type, centromere and telomere loci. By genetic studies we show that these sites play a role in silencing at the outer repeats of centromeres as well as mating-type locus and this effect is mediated through Pap1 binding site and interaction with and recruitment of the HP1/Swi6. Importantly,  pap1 Δ cells display a silencing defect even in absence of the oxidative stress. Such a role of Pap1 in heterochromatin formation may be evolutionarily conserved.","authors":"Kumar A, Nanda JS, Saini S, Singh J","authors_abbrev":"Kumar A et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-08-04","publication_year":"2021","canto_session_key":"63bb131c65e29178","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-08-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30793188","title":"A conserved genetic interaction between Spt6 and Set2 regulates H3K36 methylation.","citation":"Nucleic Acids Res 2019 May 07;47(8):3888-3903","abstract":"The transcription elongation factor Spt6 and the H3K36 methyltransferase Set2 are both required for H3K36 methylation and transcriptional fidelity in Saccharomyces cerevisiae. However, the nature of the requirement for Spt6 has remained elusive. By selecting for suppressors of a transcriptional defect in an spt6 mutant, we have isolated several highly clustered, dominant SET2 mutations (SET2sup mutations) in a region encoding a proposed autoinhibitory domain. SET2sup mutations suppress the H3K36 methylation defect in the spt6 mutant, as well as in other mutants that impair H3K36 methylation. We also show that SET2sup mutations overcome the requirement for certain Set2 domains for H3K36 methylation. In vivo, SET2sup mutants have elevated levels of H3K36 methylation and the purified Set2sup mutant protein has greater enzymatic activityin vitro. ChIP-seq studies demonstrate that the H3K36 methylation defect in the spt6 mutant, as well as its suppression by a SET2sup mutation, occurs at a step following the recruitment of Set2 to chromatin. Other experiments show that a similar genetic relationship between Spt6 and Set2 exists in Schizosaccharomyces pombe. Taken together, our results suggest a conserved mechanism by which the Set2 autoinhibitory domain requires multiple Set2 interactions to ensure that H3K36 methylation occurs specifically on actively transcribed chromatin.","doi":"10.1093/nar/gkz119","authors":"Gopalakrishnan R, Marr SK, Kingston RE, Winston F","authors_abbrev":"Gopalakrishnan R et al.","pubmed_publication_date":"07 May 2019","pubmed_entrez_date":"2019-02-23","publication_year":"2019","canto_session_key":"edd4b4693fe18759","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-05-05 18:34:30","canto_approved_date":"2020-07-02 15:01:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-13 19:29:47","canto_added_date":"2019-02-24 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29B12.02c","SPAC1F7.01c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-05-05"},{"uniquename":"PMID:7698660","title":"Schizosaccharomyces pombe and Candida albicans cDNA homologues of the Saccharomyces cerevisiae UBC4 gene.","citation":"Gene 1995 Mar 21;155(1):137-8","abstract":"cDNA homologues of the Saccharomyces cerevisiae UBC4 and UBC5 genes, encoding putative ubiquitin conjugating enzymes, were isolated and characterized from the fission yeast Schizosaccharomyces pombe and from the pathogenic dimorphic yeast Candida albicans. The Sz. pombe and C. albicans deduced amino-acid sequences are 82.3 and 90.5% similar to the Sa. cerevisiae UBC4 gene product, respectively.","authors":"Damagnez V, Rolfe M, Cottarel G","authors_abbrev":"Damagnez V et al.","pubmed_publication_date":"21 Mar 1995","pubmed_entrez_date":"1995-03-21","publication_year":"1995","canto_session_key":"689c447df2b8bed5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-04-28 16:50:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-28 15:17:44","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC119.02"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2016-04-28"},{"uniquename":"PMID:15765057","title":"The Schizosaccharomyces pombe gene encoding gamma-glutamyl transpeptidase I is regulated by non-fermentable carbon sources and nitrogen starvation.","citation":"J Microbiol 2005 Feb;43(1):44-8","abstract":"In our previous study, the first structural gene (GGTI) encoding g-glutamyl transpeptidase was cloned and characterized from the fission yeast Schizosaccharomyces pombe, and its transcription, using the GGTI-lacZ fusion gene, containing the 1,085 bp upstream region from the translational initiation point, was found to be enhanced by sodium nitroprusside and L-buthionine-(S,R)-sulfoximine (BSO). In the present work, regulation of the GGTI gene was further elucidated. Non-fermentable carbon sources, such as acetate and ethanol, markedly enhanced the synthesis of beta-galactosidase from the GGTI-lacZ fusion gene. However, its induction by non-fermentable carbon sources appeared to be independent of the presence of the Pap1 protein. Nitrogen starvation also gave rise to induction of GGTI gene expression in a Pap1-independent manner. The three additional fusion plasmids, carrying 754, 421 and 156 bp regions, were constructed. The sequence responsible for the induction by non-fermentable carbon sources and nitrogen starvation was identified to exist within a -421 bp region of the GGTI gene. Taken together, the S. pombe GGTI gene is regulated by non-fermentable carbon sources and nitrogen starvation.","authors":"Kim HG, Park HJ, Kang HJ, Lim HW, Kim K, Park EH, Ahn K, Lim CJ","authors_abbrev":"Kim HG et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2005-03-15","publication_year":"2005","canto_session_key":"4ceda21f11a0f386","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-03 20:10:06","canto_approved_date":"2024-03-30 08:24:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-01 20:05:31","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC664.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-12-03"},{"uniquename":"PMID:29958934","title":"Schizosaccharomyces pombe cardiolipin synthase is part of a mitochondrial fusion protein regulated by intron retention.","citation":"Biochim Biophys Acta Mol Cell Biol Lipids 2018 Oct;1863(10):1331-1344","abstract":"Cardiolipin (CL) is a unique lipid component of mitochondria in all eukaryotes. It is important for the architecture of mitochondrial membranes and for mitochondrial dynamics. CL also creates a highly specific microenvironment of mitochondrial protein machineries. CL biosynthetic pathway is, however, only partially characterized in the fission yeast Schizosaccharomyces pombe. Here we show that CL synthase is an essential protein in S. pombe. It is encoded by the ORF SPAC22A12.08c as a C terminal part of a tandem fusion protein together with a mitochondrial hydrolase of unknown function. Expression of S. pombe CL synthase is able to complement deletion of the CRD1 gene of Saccharomyces cerevisiae and, vice versa, S. cerevisiae CRD1 gene complements deletion of S. pombe SPAC22A12.08c. The proper expression of CL synthase and its partner in the tandem protein, the mitochondrial hydrolase, is regulated at the level of alternate intron splicing. The first part of the SPAC22A12.08c fusion protein could be translated from both major SPAC22A12.08c derived mRNAs, with and without intron IV. Functional CL synthase, however, is produced only from the minor SPAC22A12.08c derived mRNA that has intron IV retained. Thus, intron retention is a novel mechanism for the differential expression of two proteins that evolved as a fusion protein and are under the control of the same promoter.","doi":"10.1016/j.bbalip.2018.06.019","authors":"Virčíková V, Pokorná L, Tahotná D, Džugasová V, Balážová M, Griač P","authors_abbrev":"Virčíková V et al.","pubmed_publication_date":"Oct 2018","pubmed_entrez_date":"2018-07-01","publication_year":"2018","canto_session_key":"334c62cb526e72c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Griac Peter","canto_first_approved_date":"2021-04-23 14:53:47","canto_approved_date":"2021-05-04 09:11:58","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-04-12 07:41:19","canto_added_date":"2018-07-02 00:15:04","annotation_curators":[{"name":"Griac Peter","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-04-23"},{"uniquename":"PMID:6798911","title":"[Microbial growth synchronization by immobilization onto solid carriers (author's transl)].","citation":"Ann Microbiol (Paris) 1981;132B(2):241-55","abstract":"Immobilization of Saccharomyces uvarum onto solid carriers modifies their growth. When adsorbed onto glass or brick beads, synchronous yeast cycles and reduced generation times can be observed. The same phenomena take place when the cells are bound to the glass by glutaraldehyde. Synchronization of growth is also obtained with Schizosaccharomyces pombe amd Bacillus megaterium. These modifications do not result from an immobilization of cells in a particular state or from an interaction before linking.","authors":"Navarro JM, Durand G","authors_abbrev":"Navarro JM et al.","pubmed_publication_date":"1981","pubmed_entrez_date":"1981-09-01","publication_year":"1981","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15237962","title":"Effect of Schizosaccharomyces pombe on aromatic compounds in dry sherry wines containing high levels of gluconic acid.","citation":"J Agric Food Chem 2004 Jul 14;52(14):4529-34","abstract":"Volatile compounds have been determined in control dry sherry wines and those supplemented with gluconic acid, which were inoculated with the Schizosaccharomyces pombe 1379 (ATCC 26760) yeast strain. These compounds were grouped, according to volatiles exhibiting the identical odor quality, into nine groups of the same odor character (aromatic series) as a way of establishing the aroma profile for the studied wines. Control and supplemented wines showed changes in the balsamic, spicy, roasty, and fruity aromatic series, and tasters judged the aroma as typical of wines subjected to biological aging. This fission yeast may be used as a treatment to reduce gluconic acid contents in wines obtained from rotten grapes, making feasible the incorporation of these wines into the biological aging process. In addition, this procedure may also help to accelerate the traditional biological aging in sherry winemaking due to the contribution of some specific compounds by S. pombe to the wine.","authors":"Peinado RA, Mauricio JC, Medina M, Moreno JJ","authors_abbrev":"Peinado RA et al.","pubmed_publication_date":"14 Jul 2004","pubmed_entrez_date":"2004-07-09","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16478994","title":"Autoregulation of ribosome biosynthesis by a translational response in fission yeast.","citation":"Mol Cell Biol 2006 Mar;26(5):1731-42","abstract":"Maintaining the appropriate balance between the small and large ribosomal subunits is critical for translation and cell growth. We previously identified the 40S ribosomal protein S2 (rpS2) as a substrate of the protein arginine methyltransferase 3 (RMT3) and reported a misregulation of the 40S/60S ratio in rmt3 deletion mutants of Schizosaccharomyces pombe. For this study, using DNA microarrays, we have investigated the genome-wide biological response of rmt3-null cells to this ribosomal subunit imbalance. Whereas little change was observed at the transcriptional level, a number of genes showed significant alterations in their polysomal-to-monosomal ratios in rmt3Delta mutants. Importantly, nearly all of the 40S ribosomal protein-encoding mRNAs showed increased ribosome density in rmt3 disruptants. Sucrose gradient analysis also revealed that the ribosomal subunit imbalance detected in rmt3-null cells is due to a deficit in small-subunit levels and can be rescued by rpS2 overexpression. Our results indicate that rmt3-null fission yeast compensate for the reduced levels of small ribosomal subunits by increasing the ribosome density, and likely the translation efficiency, of 40S ribosomal protein-encoding mRNAs. Our findings support the existence of autoregulatory mechanisms that control ribosome biosynthesis and translation as an important layer of gene regulation.","authors":"Bachand F, Lackner DH, Bähler J, Silver PA","authors_abbrev":"Bachand F et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-02-16","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC8D2.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21091496","title":"Conserved components, but distinct mechanisms for the placement and assembly of the cell division machinery in unicellular and filamentous ascomycetes.","citation":"Mol Microbiol 2010 Dec;78(5):1058-76","abstract":"Cytokinesis is essential for cell proliferation, yet its molecular description is challenging, because >100 conserved proteins must be spatially and temporally co-ordinated. Despite the high importance of a tight co-ordination of cytokinesis with chromosome and organelle segregation, the mechanism for determining the cell division plane is one of the least conserved aspects of cytokinesis in eukaryotic cells. Budding and fission yeast have developed fundamentally distinct mechanisms to ensure proper nuclear segregation. The extent to which these pathways are conserved in multicellular fungi remains unknown. Recent progress indicates common components, but different mechanisms that are required for proper selection of the septation site in the different groups of Ascomycota. Cortical cues are used in yeast- and filament-forming species of the Saccharomycotina clade that are established at the incipient bud site or the hyphal tip respectively. In contrast, septum formation in the filament-forming Pezizomycotina species Aspergillus nidulans and Neurospora crassa seems more closely related to the fission yeast programme in that they may combine mitotic signals with a cell end-based marker system and Rho GTPase signalling. Thus, significant differences in the use and connection of conserved signalling modules become apparent that reflect the phylogenetic relationship of the analysed models.","doi":"10.1111/j.1365-2958.2010.07392.x","authors":"Seiler S, Justa-Schuch D","authors_abbrev":"Seiler S et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-11-25","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12390246","title":"Cut1/separase C-terminus affects spindle pole body positioning in interphase of fission yeast: pointed nuclear formation.","citation":"Genes Cells 2002 Nov;7(11):1113-24","abstract":"The separase-securin complex is required for anaphase. Separase activated by securin destruction cleaves the cohesin subunit Scc1/Rad21 enriched in kinetochores. Fission yeast Cut1/separase resides in interphase cytoplasm and mobilizes to the spindle and the spindle pole bodies (SPBs) in mitosis, while Cut2/securin remains in the nucleus from interphase to metaphase, and temporarily locates at the short spindle.\nWe here report a novel SPB-led dynamic nuclear movement in fission yeast, when the Cut1 C-terminal fragment is over-expressed. The tip of the pointed nucleus contained both SPB and centromeric DNA, and rapidly moved along the bundled cytoplasmic microtubules. The same pointed nucleus was produced when the human separase C-fragment was over-expressed. The pointed nuclear formation did not require the protease site of separase, but required the conserved C-terminus and a microtubule- and kinetochore-binding protein Mtc1/Alp14, a homologue of frog XMAP215 and budding yeast Stu2. The movement-inducing C-fragment should be cytoplasmic, as the pointed nucleus was abolished when the fragment contained the NLS (nuclear localization signal).\nOverproduced separase C-fragment abolishes correct SPB-positioning in interphase. Resulting pointed nuclear formation (alternatively called 'pigtail movement') requires cytoplasmic microtubules and Mtc1/Alp14.","authors":"Nakamura T, Nagao K, Nakaseko Y, Yanagida M","authors_abbrev":"Nakamura T et al.","pubmed_publication_date":"Nov 2002","pubmed_entrez_date":"2002-10-23","publication_year":"2002","canto_session_key":"3926aad5386b9286","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-11-14 11:42:19","canto_approved_date":"2024-04-03 08:10:18","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-04-05 11:26:31","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.14","SPAC1093.06c","SPCC338.17c","SPCC5E4.04","SPCC895.07"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-11-14"},{"uniquename":"PMID:15380088","title":"Phosphoinositides: older than we first thought?","citation":"Curr Biol 2004 Sep 21;14(18):R762-4","abstract":"Despite nearly 50 years of study, it is good to see that phosphoinositides are still capable of springing the odd surprise. Signaling by the second messenger phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3)) was thought to be absent in yeast, but a recent paper now describes the presence of PtdIns(3,4,5)P(3) in Schizosaccharomyces pombe.","authors":"Cooke FT","authors_abbrev":"Cooke FT","pubmed_publication_date":"21 Sep 2004","pubmed_entrez_date":"2004-09-24","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2195725","title":"Centromeres of budding and fission yeasts.","citation":"Trends Genet 1990 May;6(5):150-4","abstract":"Centromeres of the budding yeast Saccharomyces cerevisiae are structurally relatively simple, are specified by only about 125 base pairs of DNA, and contain no repeated DNA sequences. The centromere regions in the fission yeast Schizosaccharomyces pombe span many kilobase pairs of DNA and contain repeated DNA sequences that appear to be necessary for full centromere function. A portion of the repeated sequences is organized into a large inverted repeated structure in the centromere region of each S. pombe chromosome. Fission yeast provides an excellent model system for studying the role of repeated DNA sequences in centromere function.","authors":"Clarke L","authors_abbrev":"Clarke L","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8497322","title":"Fission yeast chk1 protein kinase links the rad checkpoint pathway to cdc2.","citation":"Nature 1993 May 27;363(6427):368-71","abstract":"The dependence of cell-cycle progression on the integrity of the genome has been described as checkpoint control. A number of mutants of the fission yeast Schizosaccharomyces pombe, selected for their sensitivity to DNA damage caused by radiation (rad mutants) or to the DNA synthesis inhibitor hydroxyurea (hus mutants) have been classified as checkpoint mutants because they fail to arrest the cell cycle in response to DNA damage or incompletely replicated DNA. Coupling of the checkpoint pathways that monitor DNA repair and replication to control of the cell cycle is essential. In a search for components that interact with the cell-cycle regulatory kinase p34cdc2, we have identified a novel fission yeast protein kinase homologue which is involved in cell-cycle arrest when DNA damage has occurred or when unligated DNA is present. We have called the gene encoding this protein chk1 for checkpoint kinase. Multiple copies of chk1 partially rescue the ultraviolet sensitivity of rad1-1, a mutant deficient in checkpoint control. Identification of a gene involved in checkpoint control as a rescue of a cdc2 mutant links the rad1-dependent DNA-damage-sensing pathway and p34cdc2 activity.","authors":"Walworth N, Davey S, Beach D","authors_abbrev":"Walworth N et al.","pubmed_publication_date":"27 May 1993","pubmed_entrez_date":"1993-05-27","publication_year":"1993","canto_session_key":"9442751303a5f327","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-04 11:40:32","canto_approved_date":"2025-09-04 12:44:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-20 14:59:50","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC11B10.09","SPAC1952.07","SPCC1259.13","SPAC20G8.01","SPAC24H6.05"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-01-04"},{"uniquename":"PMID:12389037","title":"Structure of the SET domain histone lysine methyltransferase Clr4.","citation":"Nat Struct Biol 2002 Nov;9(11):828-32","abstract":"Methylation of histone H3 lysine 9 is an important component of the 'histone code' for heterochromatic gene silencing. The SET domain-containing Clr4 protein, a close relative of Su(var)3-9 proteins in higher eukaryotes, specifically methylates lysine 9 of histone H3 and is essential for silencing in Schizosaccharomyces pombe. Here we report the 2.3 A resolution crystal structure of the catalytic domain of Clr4. The structure reveals an overall fold rich in beta-strands, a potential active site consisting of a SAM-binding pocket, and a connected groove that could accommodate the binding of the N-terminal tail of histone H3. The pre-SET motif contains a triangular zinc cluster coordinated by nine cysteines distant from the active site, whereas the post-SET region is largely flexible but proximal to the active site. The structure provides insights into the architecture of SET domain histone methyltransferases and establishes a paradigm for further characterization of the Clr4 family of epigenetic regulators.","authors":"Min J, Zhang X, Cheng X, Grewal SI, Xu RM","authors_abbrev":"Min J et al.","pubmed_publication_date":"Nov 2002","pubmed_entrez_date":"2002-10-22","publication_year":"2002","canto_session_key":"582786fcfe8ca514","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-07-25 15:22:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-25 14:39:01","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-25","pdb_entries":[{"pdb_id":"1mvh","gene_chains":[{"gene_uniquename":"SPBC428.08c","chain":"A","position":"192-490"}],"title":"structure of the SET domain histone lysine methyltransferase Clr4","entry_authors":"Min JR,Zhang X,Cheng XD,Grewal SIS,Xu R-M","entry_authors_abbrev":"Min JR et al.","reference_uniquename":"PMID:12389037","experimental_method":"X-ray","resolution":"2.3"},{"pdb_id":"1mvx","gene_chains":[{"gene_uniquename":"SPBC428.08c","chain":"A","position":"192-490"}],"title":"structure of the SET domain histone lysine methyltransferase Clr4","entry_authors":"Min JR,Zhang X,Cheng XD,Grewal SIS,Xu R-M","entry_authors_abbrev":"Min JR et al.","reference_uniquename":"PMID:12389037","experimental_method":"X-ray","resolution":"3.0"}]},{"uniquename":"PMID:23609449","title":"Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum.","citation":"J Biol Chem 2013 Jun 07;288(23):16460-16475","abstract":"Here we report for the first time the three-dimensional structure of a mannose 6-phosphate receptor homology (MRH) domain present in a protein with enzymatic activity, glucosidase II (GII). GII is involved in glycoprotein folding in the endoplasmic reticulum. GII removes the two innermost glucose residues from the Glc3Man9GlcNAc2 transferred to nascent proteins and the glucose added by UDP-Glc:glycoprotein glucosyltransferase. GII is composed of a catalytic GIIα subunit and a regulatory GIIβ subunit. GIIβ participates in the endoplasmic reticulum localization of GIIα and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GIIβ MRH domain by NMR spectroscopy. It adopts a β-barrel fold similar to that of other MRH domains, but its binding pocket is the most shallow known to date as it accommodates a single mannose residue. In addition, we identified a conserved residue outside the binding pocket (Trp-409) present in GIIβ but not in other MRHs that influences GII glucose trimming activity.","doi":"10.1074/jbc.M113.450239","authors":"Olson LJ, Orsi R, Alculumbre SG, Peterson FC, Stigliano ID, Parodi AJ, D'Alessio C, Dahms NM","authors_abbrev":"Olson LJ et al.","pubmed_publication_date":"07 Jun 2013","pubmed_entrez_date":"2013-04-24","publication_year":"2013","canto_session_key":"2b922d5a01cbc543","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-20 08:09:19","canto_approved_date":"2023-02-20 08:09:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 18:14:52","canto_added_date":"2013-08-22 05:19:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC825.02","SPAC1002.03c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2023-02-20","pdb_entries":[{"pdb_id":"2lvx","gene_chains":[{"gene_uniquename":"SPCC825.02","chain":"A","position":"380-473"}],"title":"MRH domain of the Glucosidase II beta subunit from S. pombe","entry_authors":"Dahms NM,Olson LJ,Peterson FC","entry_authors_abbrev":"Dahms NM et al.","reference_uniquename":"PMID:23609449","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:31332096","title":"A  tel2  Mutation That Destabilizes the Tel2-Tti1-Tti2 Complex Eliminates Rad3 ATR  Kinase Signaling in the DNA Replication Checkpoint and Leads to Telomere Shortening in Fission Yeast.","citation":"Mol Cell Biol 2019 Oct 15;39(20)","abstract":"In response to perturbed DNA replication, ATR (ataxia telangiectasia and Rad3-related) kinase is activated to initiate the checkpoint signaling necessary for maintaining genome integrity and cell survival. To better understand the signaling mechanism, we carried out a large-scale genetic screen in fission yeast looking for mutants with enhanced sensitivity to hydroxyurea. From a collection of ∼370 primary mutants, we found a few mutants in which Rad3 (ATR ortholog)-mediated phospho-signaling was significantly compromised. One such mutant carried an uncharacterized mutation in  tel2 , a gene encoding an essential and highly conserved eukaryotic protein. Previous studies in various biological models have shown that Tel2 mainly functions in Tel2-Tti1-Tti2 (TTT) complex that regulates the steady-state levels of all phosphatidylinositol 3-kinase-like protein kinases, including ATR. We show here that although the levels of Rad3 and Rad3-mediated phospho-signaling in DNA damage checkpoint were moderately reduced in the  tel2  mutant, the phospho-signaling in the DNA replication checkpoint was almost completely eliminated. In addition, the  tel2  mutation caused telomere shortening. Since the interactions of Tel2 with Tti1 and Tti2 were significantly weakened by the mutation, destabilization of the TTT complex likely contributes to the observed checkpoint and telomere defects.","doi":"10.1128/MCB.00175-19","authors":"Xu YJ, Khan S, Didier AC, Wozniak M, Liu Y, Singh A, Nakamura TM","authors_abbrev":"Xu YJ et al.","pubmed_publication_date":"15 Oct 2019","pubmed_entrez_date":"2019-07-24","publication_year":"2019","canto_session_key":"34f78a5c7e2cca72","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yongjie Xu","canto_first_approved_date":"2019-10-17 14:46:02","canto_approved_date":"2023-05-03 16:22:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-17 09:15:01","canto_added_date":"2019-07-25 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":40,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Yongjie Xu","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC23B6.03c","SPBC1604.17c","SPCC1259.13","SPAC664.07c","SPCC18B5.11c","SPCC622.13c","SPBC25D12.04","SPAC14C4.13","SPBC342.05","SPAC458.03","SPAC9E9.08","SPBC216.05","SPAC694.06c"],"gene_count":13,"ltp_gene_count":11,"approved_date":"2019-10-17"},{"uniquename":"PMID:1533272","title":"A dominant negative allele of p34cdc2 shows altered phosphoamino acid content and sequesters p56cdc13 cyclin.","citation":"Mol Cell Biol 1992 May;12(5):2295-301","abstract":"The cdc2 gene product, a 34-kDa phosphoprotein with serine/threonine protein kinase activity, has been implicated as the key component in the regulation of the eucaryotic cell cycle. Activation of the cdc2 protein kinase is regulated by its phosphorylation state and by interaction with other proteins. We have mutagenized the fission yeast cdc2 gene to obtain conditionally dominant negative alleles. One of these mutants, named DL2, is characterized in this report. Overexpression of the mutant protein in a wild-type cdc2 background is lethal and leads to arrest in the G2 phase of the cell cycle. The mutant phenotype is the result of a single amino acid change in the GDSEID motif of the protein, a region of identity in all cdc2 homologs, and results in a nonfunctional protein that shows an altered content of phosphothreonine. Multicopy suppressors of the dominant negative phenotype have been isolated, and one of these has been shown to encode the cdc13 cyclin B gene product.","authors":"Fleig UN, Gould KL, Nurse P","authors_abbrev":"Fleig UN et al.","pubmed_publication_date":"May 1992","pubmed_entrez_date":"1992-05-01","publication_year":"1992","canto_session_key":"43f8a34aa26e2202","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-08-21 15:43:50","canto_approved_date":"2022-07-28 20:11:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-29 14:52:49","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":6,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-08-21"},{"uniquename":"EMBL:SPO5825","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18799612","title":"The Hsk1(Cdc7) replication kinase regulates origin efficiency.","citation":"Mol Biol Cell 2008 Dec;19(12):5550-8","abstract":"Origins of DNA replication are generally inefficient, with most firing in fewer than half of cell cycles. However, neither the mechanism nor the importance of the regulation of origin efficiency is clear. In fission yeast, origin firing is stochastic, leading us to hypothesize that origin inefficiency and stochasticity are the result of a diffusible, rate-limiting activator. We show that the Hsk1-Dfp1 replication kinase (the fission yeast Cdc7-Dbf4 homologue) plays such a role. Increasing or decreasing Hsk1-Dfp1 levels correspondingly increases or decreases origin efficiency. Furthermore, tethering Hsk1-Dfp1 near an origin increases the efficiency of that origin, suggesting that the effective local concentration of Hsk1-Dfp1 regulates origin firing. Using photobleaching, we show that Hsk1-Dfp1 is freely diffusible in the nucleus. These results support a model in which the accessibility of replication origins to Hsk1-Dfp1 regulates origin efficiency and provides a potential mechanistic link between chromatin structure and replication timing. By manipulating Hsk1-Dfp1 levels, we show that increasing or decreasing origin firing rates leads to an increase in genomic instability, demonstrating the biological importance of appropriate origin efficiency.","authors":"Patel PK, Kommajosyula N, Rosebrock A, Bensimon A, Leatherwood J, Bechhoefer J, Rhind N","authors_abbrev":"Patel PK et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-09-19","publication_year":"2008","canto_session_key":"d86fee516651e370","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nick Rhind","canto_first_approved_date":"2014-09-25 07:35:12","canto_approved_date":"2024-04-04 10:05:20","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-09-26 15:26:46","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Nick Rhind","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.12c","SPCC550.13"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-09-25"},{"uniquename":"EMBL:AU013567","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11431703","title":"Regulation of premeiotic S phase and recombination-related double-strand DNA breaks during meiosis in fission yeast.","citation":"Nat Genet 2001 Jul;28(3):290-3","abstract":"The meiotic cell cycle is characterized by high levels of recombination induced by DNA double-strand breaks (DSBs), which appear after completion of premeiotic S phase, leading to the view that initiation of recombination depends on meiotic DNA replication. It has also been indicated that DNA replication initiation proteins may differ between the meiotic and mitotic cell cycles, giving rise to an altered S phase, which could contribute to the high level of recombination during meiosis. We have investigated these possibilities in the fission yeast Schizosaccharomyces pombe and found that core DNA replication initiation proteins used during the mitotic cell cycle, including Cdc18p (budding yeast Cdc6p), Cdc19p (Mcm2p), Cdc21p (Mcm4p) and Orp1p (Orc1p), are also required for premeiotic S phase. Reduced activity of these proteins prevents completion of DNA replication but not formation of DSBs. We conclude that recombination-related DSB formation does not depend on the completion of meiotic DNA replication and we propose two parallel developmental sequences during the meiotic cell cycle: one for premeiotic S phase and the other for initiating recombination.","authors":"Murakami H, Nurse P","authors_abbrev":"Murakami H et al.","pubmed_publication_date":"Jul 2001","pubmed_entrez_date":"2001-06-30","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19339546","title":"How to scaffold the contractile ring for a safe cytokinesis - lessons from Anillin-related proteins.","citation":"J Cell Sci 2009 Apr 15;122(Pt 8):1071-9","abstract":"The ingression of a cleavage furrow separates the two daughter cells at the end of cell division. In many organisms this furrow ingression is driven by the assembly and contraction of actomyosin filaments, forming a contractile ring. To achieve a successful cytokinesis, these actomyosin filaments need to be assembled in an organized manner. For this purpose, a network of cytoskeletal proteins is built at the cleavage site to act as a scaffold for actomyosin filaments and to connect them to the plasma membrane. The Drosophila melanogaster protein Anillin, and its related proteins in other organisms, has a pivotal role in the organization of this scaffold in many species, ranging from yeast to humans. Recent studies indicate that Anillin-related proteins interact not only with the structural components of the contractile ring, but also with the signalling factors that control their dynamics. In addition, Drosophila Anillin connects the actomyosin ring to the spindle microtubules through its interaction with the RacGAP component of the centralspindlin complex. Here I review the structures and functions of Anillin and Anillin-related proteins in various model systems, and aim to highlight both the common and distinctive features of these essential organizers of the molecular machinery that drives furrow ingression.","doi":"10.1242/jcs.034785","authors":"D'Avino PP","authors_abbrev":"D'Avino PP","pubmed_publication_date":"15 Apr 2009","pubmed_entrez_date":"2009-04-03","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17407755","title":"Microtubule organization: cell shape is destiny.","citation":"Curr Biol 2007 Apr 03;17(7):R249-51","abstract":"A simple self-assembly pathway generates cytoplasmic microtubule bundles that can locate the cell center and guide spindle assembly in fission yeast. The cylindrical cell shape automatically corrects spindle orientation errors, rendering a checkpoint unnecessary.","authors":"Haase SB, Lew DJ","authors_abbrev":"Haase SB et al.","pubmed_publication_date":"03 Apr 2007","pubmed_entrez_date":"2007-04-05","publication_year":"2007","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11350071","title":"Characterization of the manganese-containing superoxide dismutase and its gene regulation in stress response of Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2001 May 18;283(4):908-14","abstract":"Fission yeast Schizosaccharomyces pombe contains two superoxide dismutases (SODs), one in the cytosol and the other in mitochondria. The sod2+ gene encoding putative mitochondrial superoxide dismutase containing manganese (MnSOD) has been isolated. Purification and analysis of the sod2+ gene product revealed that it contained only manganese as a cofactor, thus verified to be a genuine MnSOD. It was localized in mitochondria as expected. Its N-terminal amino acid sequence indicated that the mitochondrial targeting sequence of 21 amino acids was removed. The native form consisted of two identical subunits. The sod2+ expression was induced by external stresses, such as treatments with superoxide generators, high osmolarity, and heat. The induction by these stress treatments depended on Wis1-Spc1 MAPK signal transduction pathway being independent of transcription factors Atf1 or Pap1. The sod2 disruption rendered cells sensitive to various superoxide-generators, heat, and high osmolarity, suggesting that the mitochondrial MnSOD acts as a general defense agent against multiple stresses.","authors":"Jeong JH, Kwon ES, Roe JH","authors_abbrev":"Jeong JH et al.","pubmed_publication_date":"18 May 2001","pubmed_entrez_date":"2001-05-15","publication_year":"2001","canto_session_key":"8e7ac9ef1c529780","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-02 17:19:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-06 11:13:27","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC1486.01","SPAC24B11.06c","SPBC29B5.01","SPAC821.10c","SPAC1783.07c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-11-06"},{"uniquename":"PMID:25052092","title":"F-BAR domain protein Rga7 collaborates with Cdc15 and Imp2 to ensure proper cytokinesis in fission yeast.","citation":"J Cell Sci 2014 Oct 01;127(Pt 19):4146-58","abstract":"F-BAR domain proteins act as linkers between the cell cortex and cytoskeleton, and are involved in membrane binding and bending. Rga7 is one of the seven F-BAR proteins present in the fission yeast Schizosaccharomyces pombe. In addition to the F-BAR domain in the N-terminal region, Rga7 possesses a Rho GTPase-activating protein (GAP) domain at its C-terminus. We show here that Rga7 is necessary to prevent fragmentation of the contracting ring and incorrect septum synthesis. Accordingly, cultures of cells lacking Rga7 contain a higher percentage of dividing cells and more frequent asymmetric or aberrant septa, which ultimately might cause cell death. The Rga7 F-BAR domain is necessary for the protein localization to the division site and to the cell tips, and also for the Rga7 roles in cytokinesis. In contrast, Rga7 GAP catalytic activity seems to be dispensable. Moreover, we demonstrate that Rga7 cooperates with the two F-BAR proteins Cdc15 and Imp2 to ensure proper cytokinesis. We have also detected association of Rga7 with Imp2, and its binding partners Fic1 and Pxl1. Taken together, our findings suggest that Rga7 forms part of a protein complex that coordinates the late stages of cytokinesis.","doi":"10.1242/jcs.146233","authors":"Martín-García R, Coll PM, Pérez P","authors_abbrev":"Martín-García R et al.","pubmed_publication_date":"01 Oct 2014","pubmed_entrez_date":"2014-07-24","publication_year":"2014","canto_session_key":"d019d2682b15d6bb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-07-25 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G8.05c","SPBC23G7.08c","SPBC11C11.02","SPBC83.18c","SPBC4F6.12"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:20333190","title":"Protein subcellular relocalization in the evolution of yeast singleton and duplicate genes.","citation":"Genome Biol Evol 2009 Jul 22;1:198-204","abstract":"Gene duplication is the primary source of new genes, but the mechanisms underlying the functional divergence and retention of duplicate genes are not well understood. Because eukaryotic proteins are localized to subcellular structures and localization can be altered by a single amino acid replacement, it was recently proposed that protein subcellular relocalization (PSR) plays an important role in the functional divergence and retention of duplicate genes. Although numerous examples of distinct subcellular localizations of paralogous proteins have been reported, it is unknown whether PSR occurs more frequently after gene duplication than without duplication. By analyzing experimentally determined and computationally predicted genome-wide protein subcellular localization data of the budding yeast Saccharomyces cerevisiae and two other fungi (Schizosaccharomyces pombe and Kluyveromyces waltii), we show that even singleton genes have an appreciable rate of relocalization in evolution and that duplicate genes do not relocalize more frequently than singletons. These results suggest that subcellular relocalization is unlikely to have been a major mechanism for duplicate gene retention and functional divergence at the genomic scale.","doi":"10.1093/gbe/evp021","authors":"Qian W, Zhang J","authors_abbrev":"Qian W et al.","pubmed_publication_date":"22 Jul 2009","pubmed_entrez_date":"2010-03-25","publication_year":"2009","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15372076","title":"A chromodomain protein, Chp1, is required for the establishment of heterochromatin in fission yeast.","citation":"EMBO J 2004 Oct 01;23(19):3825-35","abstract":"The chromodomain is a conserved motif that functions in the epigenetic control of gene expression. Here, we report the functional characterization of a chromodomain protein, Chp1, in the heterochromatin assembly in fission yeast. We show that Chp1 is a structural component of three heterochromatic regions-centromeres, the mating-type region, and telomeres-and that its localization in these regions is dependent on the histone methyltransferase Clr4. Although deletion of the chp1(+) gene causes centromere-specific decreases in Swi6 localization and histone H3-K9 methylation, we show that the role of Chp1 is not exclusive to the centromeres. We found that some methylation persists in native centromeric regions in the absence of Chp1, which is also true for the mating-type region and telomeres, and determined that Swi6 and Chp2 are critical to maintaining this residual methylation. We also show that Chp1 participates in the establishment of repressive chromatin in all three chromosomal regions. These results suggest that different heterochromatic regions share common structural properties, and that centromeric heterochromatin requires Chp1-mediated establishment steps differently than do other heterochromatic regions.","authors":"Sadaie M, Iida T, Urano T, Nakayama J","authors_abbrev":"Sadaie M et al.","pubmed_publication_date":"01 Oct 2004","pubmed_entrez_date":"2004-09-17","publication_year":"2004","canto_session_key":"3c257a83101c8398","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-01-25 12:28:39","canto_approved_date":"2024-04-29 15:26:12","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-01-23 18:16:43","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":46,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.08","SPCC736.11","SPCC188.13c","SPAC664.01c","SPAC18G6.02c","SPBC3B9.21","SPBC16C6.10","SPBC428.08c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2024-01-25"},{"uniquename":"PMID:10978278","title":"The cofactor-dependent pathways for alpha- and beta-tubulins in microtubule biogenesis are functionally different in fission yeast.","citation":"Genetics 2000 Sep;156(1):93-103","abstract":"The biogenesis of microtubules in the cell comprises a series of complex steps, including protein-folding reactions catalyzed by chaperonins. In addition a group of evolutionarily conserved proteins, called cofactors (A to E), is required for the production of assembly-competent alpha-/beta-tubulin heterodimers. Using fission yeast, in which alp11(+), alp1(+), and alp21(+), encoding the homologs for cofactors B, D, and E, respectively, are essential for cell viability, we have undertaken the genetic analysis of alp31(+), the homolog of cofactor A. Gene disruption analysis shows that, unlike the three genes mentioned above, alp31(+) is dispensable for cell growth and division. Nonetheless, detailed analysis of alp31-deleted cells demonstrates that Alp31(A) is required for the maintenance of microtubule structures and, consequently, the proper control of growth polarity. alp31-deleted cells show genetic interactions with mutations in beta-tubulin, but not in alpha-tubulin. Budding yeast cofactor A homolog RBL2 is capable of suppressing the polarity defects of alp31-deleted cells. We conclude that the cofactor-dependent biogenesis of microtubules comprises an essential and a nonessential pathway, both of which are required for microtubule integrity.","authors":"Radcliffe PA, Garcia MA, Toda T","authors_abbrev":"Radcliffe PA et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-09-09","publication_year":"2000","canto_session_key":"c578121eb386a5c8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-09-14 17:09:05","canto_approved_date":"2023-05-15 13:10:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-14 16:57:29","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.04c","SPAC22H10.10","SPBC26H8.07c","SPBC16A3.15c","SPAC8E11.07c","SPBC800.05c","SPAC13D6.05"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2017-09-14"},{"uniquename":"PMID:9372932","title":"The Saccharomyces cerevisiae Hap5p homolog from fission yeast reveals two conserved domains that are essential for assembly of heterotetrameric CCAAT-binding factor.","citation":"Mol Cell Biol 1997 Dec;17(12):7008-18","abstract":"The CCAAT-binding factor is an evolutionarily conserved heteromeric transcription factor that binds to CCAAT box-containing upstream activation sites within the promoters of numerous eukaryotic genes. The CCAAT-binding factor from Saccharomyces cerevisiae is a heterotetramer that contains the subunits Hap2p, Hap3p, Hap4p, and Hap5p and that functions in the activation of genes involved in respiratory metabolism. Here we describe the isolation of the cDNA encoding the Schizosaccharomyces pombe homolog of Hap5p, designated php5+. We have shown that Php5p is a subunit of the CCAAT-binding factor in fission yeast and is required for transcription of the S. pombe cyc1+ gene. Analysis of the evolutionarily conserved regions of Hap5p, Php5p, and the mammalian homolog CBF-C revealed two essential domains within Hap5p that are required for DNA binding and transcriptional activation. One is an 87-amino-acid core domain that is conserved among Hap5p, Php5p, and CBF-C and that is required for the assembly of the Hap2p-Hap3p-Hap5p heterotrimer both in vitro and in vivo. A second domain that is essential for the recruitment of Hap4p into the CCAAT-binding complex was identified in Hap5p and Php5p.","authors":"McNabb DS, Tseng KA, Guarente L","authors_abbrev":"McNabb DS et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1997-12-31","publication_year":"1997","canto_session_key":"74545e6c72c4b96b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-05-17 13:47:38","canto_approved_date":"2021-03-05 13:12:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-24 05:43:44","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC191.07","SPBC3B8.02","SPBC725.11c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2019-05-17"},{"uniquename":"PMID:1737756","title":"A DNA exonuclease induced during meiosis of Schizosaccharomyces pombe.","citation":"J Biol Chem 1992 Feb 15;267(5):3014-23","abstract":"In meiotic cells of the fission yeast Schizosaccharomyces pombe, a DNA exonuclease activity increased approximately 5-fold after premeiotic S-phase and decreased to the initial level before the meiotic divisions. We have purified this activity, designated exonuclease I, to near homogeneity. The activity co-purified with a polypeptide with an apparent molecular weight of 36,000. With a linear double-stranded DNA substrate, exonuclease I degraded only the 5'-ended strand from each end to produce 3'-single-stranded tails. The enzyme also acted on nicked circular DNA with comparable affinity. The meiotic induction of exonuclease I and its mode of action, similar to that of recombination-promoting exonucleases from bacteria, suggest that exonuclease I is involved in meiotic homologous recombination in S. pombe.","authors":"Szankasi P, Smith GR","authors_abbrev":"Szankasi P et al.","pubmed_publication_date":"15 Feb 1992","pubmed_entrez_date":"1992-02-15","publication_year":"1992","canto_session_key":"7fbc2ef53372ef74","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-02-05 11:51:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-04-22 14:45:43","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-22"},{"uniquename":"PMID:23050226","title":"A genetic screen to discover pathways affecting cohesin function in Schizosaccharomyces pombe identifies chromatin effectors.","citation":"G3 (Bethesda) 2012 Oct;2(10):1161-8","abstract":"Cohesion, the force that holds sister chromatids together from the time of DNA replication until separation at the metaphase to anaphase transition, is mediated by the cohesin complex. This complex is also involved in DNA damage repair, chromosomes condensation, and gene regulation. To learn more about the cellular functions of cohesin, we conducted a genetic screen in Schizosaccharomyces pombe with two different cohesin mutants (eso1-G799D and mis4-242). We found synthetic negative interactions with deletions of genes involved in DNA replication and heterochromatin formation. We also found a few gene deletions that rescued the growth of eso1-G799D at the nonpermissive temperature, and these genes partially rescue the lagging chromosome phenotype. These genes are all chromatin effectors. Overall, our screen revealed an intimate association between cohesin and chromatin.","doi":"10.1534/g3.112.003327","authors":"Chen Z, McCrosky S, Guo W, Li H, Gerton JL","authors_abbrev":"Chen Z et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-10-11","publication_year":"2012","canto_session_key":"e674fe7ceba478aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-26 16:08:54","canto_approved_date":"2019-05-30 12:13:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-23 18:42:58","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":47,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24C9.08","SPBP8B7.10c","SPAC6G9.15c","SPBC1709.05","SPAC16E8.13","SPCC364.05","SPAC4F10.02","SPAC17G6.03","SPAC25A8.01c","SPAC110.02","SPAC16E8.05c","SPAC1071.09c","SPCC1235.03","SPAC12B10.15c","SPBC27.02c","SPAC11G7.01","SPBC30B4.01c","SPBC17G9.12c","SPAC19A8.14","SPCC569.05c","SPAC19D5.11c","SPAC869.09","SPCC188.12","SPCC4G3.08","SPAC3C7.10","SPAC3G9.05","SPBC6B1.08c","SPCC18.02","SPBC577.02","SPAC977.11","SPBC3H7.09","SPBC4F6.09","SPCC285.16c","SPBC609.02","SPAC9E9.05","SPAC637.10c","SPCC1682.14","SPBC1706.01","SPCC895.06","SPBC13E7.06","SPCC191.09c","SPAC1039.08","SPBC1105.09","SPAC11D3.02c","SPBC11B10.05c","SPAC12B10.12c","SPAC1786.01c","SPBC1734.11","SPAC1705.02","SPAP27G11.16","SPAC3C7.13c","SPACUNK4.09","SPCC285.13c","SPAC9.13c","SPAC3G6.11","SPAC18G6.05c","SPCC1494.09c","SPAC30.02c","SPAC1834.09","SPBP8B7.25","SPBC1711.08","SPAC14C4.12c","SPAC6G9.10c","SPAC630.06c","SPBP35G2.10","SPBC31F10.10c","SPAC1805.07c","SPAC3C7.12","SPBC25H2.09","SPAC4G9.10","SPBC23E6.01c","SPBC16A3.11","SPBC15D4.15","SPAC688.14","SPCC74.05","SPAC17H9.01","SPBC2D10.16","SPCP1E11.10","SPCC306.02c","SPAC17C9.15c","SPAC144.06","SPAC26H5.05","SPBC25B2.10","SPBC29A3.13","SPBC428.17c","SPAC1071.03c","SPAC15E1.05c","SPBC1683.06c","SPAC1952.07","SPBPB10D8.06c","SPAC23D3.01","SPAC13G7.05","SPAC17C9.05c","SPBC1271.03c","SPAC664.01c","SPCC1753.03c","SPAC17A2.06c","SPCC1840.09","SPAC23A1.11","SPAC23D3.12","SPBC651.06","SPAC17H9.10c","SPAC22E12.19","SPAC23C11.15","SPBC13G1.12","SPCC970.07c","SPBC428.08c","SPBC947.08c","SPBC2A9.04c","SPBC11B10.10c","SPBC2D10.17","SPAC1B3.17","SPAC4A8.04","SPBC2G5.04c","SPBC20F10.02c","SPBC2G2.02","SPBC800.03","SPBC83.11","SPAC15E1.10","SPCC794.07","SPAC3A11.13","SPBC30D10.04","SPCC23B6.05c","SPBC336.13c","SPBC21D10.09c","SPBC1271.05c","SPCC364.07","SPAC458.04c","SPBC3B8.10c","SPBC29A3.18","SPAC3G9.04","SPAC20H4.06c","SPCC1450.05c","SPBC1685.08","SPBC29A10.05","SPCC548.07c","SPCC74.09","SPBC4F6.10","SPBC2G2.14","SPCC757.02c","SPAC3G6.09c","SPAC167.04","SPAC1805.15c","SPBC31F10.03","SPCC970.05","SPAC57A7.09","SPCC31H12.06","SPAPJ691.02","SPBC428.10","SPBC1683.08","SPBC20F10.03","SPBC337.09","SPBC365.08c","SPBC646.02","SPAC13G6.01c","SPBC13E7.08c","SPCC4G3.19","SPBC1703.04","SPBC651.11c","SPBC13G1.08c","SPBC1709.18","SPAC2F3.12c","SPAC23H4.02","SPBC17D1.05","SPBC354.10","SPAC637.03","SPBC106.04","SPCC11E10.08","SPCC1450.03","SPAC212.04c","SPAC26A3.06","SPAC17H9.08","SPBC29A3.10c","SPAC823.16c","SPAC23H3.15c","SPAC31A2.05c","SPBC428.05c","SPBC1734.05c","SPAC27D7.03c","SPAC29A4.02c","SPAC1039.02","SPBP8B7.28c","SPBC16E9.15","SPAC16.04","SPAC4D7.06c","SPCP1E11.05c","SPBC21B10.13c","SPBC25H2.08c","SPCC23B6.04c","SPBC354.12","SPBP8B7.09c","SPCC1223.12c","SPAC1B3.03c","SPBC354.15","SPBC23G7.15c","SPBC409.19c","SPAC1002.06c","SPAC3G6.06c","SPAC26F1.10c","SPAC4F10.14c","SPBC19G7.18c","SPAC22H10.13","SPAC23D3.09","SPBC216.01c","SPAC6F12.09","SPAC9.12c","SPCC1393.02c","SPAC18G6.15","SPAC8E11.02c","SPCPB16A4.04c","SPAC7D4.02c","SPAC1B3.05","SPBC17D11.03c","SPAC1687.06c","SPAC1782.06c","SPAC4H3.03c","SPBC11B10.09","SPAC17G8.13c","SPAC18G6.02c","SPBC25H2.05","SPAC17A2.11","SPAC2F3.02","SPCC736.08","SPBC800.02","SPAC664.07c","SPBC1348.14c","SPAC167.01","SPCC1322.10","SPAC22H10.02","SPBC3B8.05","SPBC83.17","SPAC26A3.02","SPCC132.04c","SPCC777.07","SPAC27E2.01","SPBC1198.12","SPAPB8E5.06c","SPAC23H4.16c","SPBC317.01","SPCC757.09c","SPCC594.06c","SPAC9E9.08","SPAPB1E7.07","SPCC24B10.19c","SPCC584.16c","SPAC922.04","SPBC31F10.07","SPCC338.16","SPAC20G4.04c","SPAC1F12.02c","SPCPB16A4.06c","SPAC14C4.06c","SPAC22H10.04","SPAC3H5.10","SPAC27D7.06","SPBC651.04","SPCC70.10","SPBC30D10.05c","SPBC428.03c","SPBC1703.12","SPAC3H1.12c","SPAC4H3.06","SPBC1348.01","SPBC119.05c","SPAC806.04c","SPCC576.12c","SPCC965.08c","SPBC577.06c","SPCC11E10.05c","SPAC1F12.04c","SPBC336.03","SPAC20H4.10","SPBC13E7.03c","SPAC4H3.04c","SPBC1105.01","SPAPB1A10.03","SPAC1834.05","SPCC622.16c","SPBC19G7.04","SPBP4H10.04","SPBC19G7.03c","SPAC26H5.04","SPCC1183.02","SPAC5H10.09c","SPAC26A3.16","SPAC17D4.01","SPBC13A2.04c","SPBC11C11.11c","SPBC902.06","SPBC2D10.13","SPBC19C7.02","SPCC1393.10","SPBC336.14c","SPBC15D4.01c","SPAC4F8.01","SPAPB24D3.07c","SPAC19B12.08","SPBC3B8.03","SPCC162.10","SPBC17G9.09","SPAC8C9.11","SPCC1259.08"],"gene_count":302,"ltp_gene_count":10,"approved_date":"2016-02-26"},{"uniquename":"EMBL:SPD174","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013846","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11950884","title":"Different mechanisms of cell polarisation in vegetative and shmooing growth in fission yeast.","citation":"J Cell Sci 2002 Apr 15;115(Pt 8):1651-62","abstract":"Schizosaccharomyces pombe cells have two polarised growth modes: an intrinsic vegetative growth mode, determined by an internal positioning mechanism and an extrinsic shmooing growth mode, activated by external pheromone. We have analysed the role of the cell end marker Tea1p, the CLIP170 like protein Tip1p, the kinesin like protein Tea2p and the Dyrk-like kinase Pom1p, during the switch between the two growth patterns, with the intention of studying the switch away from the vegetative growth mode. In vegetative growth these morphological factors are concentrated at cell ends, whereas during shmooing growth they are delocalised from the cell ends. In the absence of Tea1p, Tip1p and Tea2p, vegetative cells display microtubule and cell polarisation defects, but shmooing cells are indistinguishable from wild-type and shmoo more readily. These results suggest that Tea1p, Tip1p and Tea2p are not required for polarised growth during shmooing, but form part of the intrinsic vegetative growth mode that needs to be dismantled before cells can generate an extrinsic growth patterns. In contrast, Pom1p appears to have a role in the initial stages of the switch to the shmooing growth mode.","authors":"Niccoli T, Nurse P","authors_abbrev":"Niccoli T et al.","pubmed_publication_date":"15 Apr 2002","pubmed_entrez_date":"2002-04-16","publication_year":"2002","canto_session_key":"66b7ec899d565a8b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-07-10 21:46:20","canto_approved_date":"2025-09-04 10:06:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-02 14:06:35","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":15,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.12","SPAC1296.03c","SPBC19C7.03","SPCC1223.06","SPBC1604.20c","SPAC2F7.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2021-07-10"},{"uniquename":"EMBL:AU014221","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24634168","title":"Proteome-wide search for PP2A substrates in fission yeast.","citation":"Proteomics 2014 Jun;14(11):1367-80","abstract":"PP2A (protein phosphatase 2A) is a major phosphatase in eukaryotic cells that plays an essential role in many processes. PP2A mutations in Schizosaccharomyces pombe result in defects of cell cycle control, cytokinesis and morphogenesis. Which PP2A substrates are responsible for these changes is not known. In this work, we searched for PP2A substrates in S. pombe using two approaches, 2D-DIGE analysis of PP2A complex mutants and identification of PP2A interacting proteins. In both cases, we used MS to identify proteins of interest. In the DIGE experiment, we compared proteomes of wild-type S. pombe, deletion of pta2, the phosphoactivator of the PP2A catalytic subunit, and pab1-4, a mutant of B-type PP2A regulatory subunit. A total of 1742 protein spots were reproducibly resolved by 2D-DIGE and 51 spots demonstrated significant changes between PP2A mutants and the wild-type control. MS analysis of these spots identified 27 proteins that include key regulators of glycerol synthesis, carbon metabolism, amino acid biosyntesis, vitamin production, and protein folding. Importantly, we independently identified a subset of these proteins as PP2A binding partners by affinity precipitation, suggesting they may be direct targets of PP2A. We have validated our approach by demonstrating that phosphorylation of Gpd1, a key enzyme in glycerol biogenesis, is regulated by PP2A and that ability of cells to respond to osmotic stress by synthesizing glycerol is compromised in the PP2A mutants. Our work contributes to a better understanding of PP2A function and identifies potential PP2A substrates.","doi":"10.1002/pmic.201300136","authors":"Bernal M, Zhurinsky J, Iglesias-Romero AB, Sanchez-Romero MA, Flor-Parra I, Tomas-Gallardo L, Perez-Pulido AJ, Jimenez J, Daga RR","authors_abbrev":"Bernal M et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-03-18","publication_year":"2014","canto_session_key":"2e0dd451cce16cf9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-01-10 23:14:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-06-30 17:12:55","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC584.01c","SPBC646.10c","SPBC11B10.10c","SPBC3F6.04c","SPAC637.07","SPCC1322.04","SPAPJ698.02c","SPBC16H5.07c","SPBC14F5.05c","SPBC1709.05","SPBC17D1.06","SPBC17D11.05","SPBC19C2.07","SPBC2D10.10c","SPAC4H3.10c","SPAC29B12.03","SPAC3A12.10","SPBC14F5.13c","SPAC6F6.03c","SPAC29A4.04c","SPAP8A3.09c","SPAC1F5.02","SPBC32F12.11","SPBC83.14c","SPCC13B11.01","SPBC646.09c","SPCC1902.02","SPAC1782.05","SPAC23G3.06","SPCC1795.11","SPAC664.08c","SPAC823.15","SPBP22H7.02c","SPCC1739.13","SPBP8B7.11","SPBC19F8.03c","SPBC685.06","SPAC1782.09c","SPAC57A7.12","SPAC821.10c","SPBC1734.01c","SPBC17D11.07c","SPBC1709.02c","SPBC32H8.12c","SPAC227.07c","SPAC12G12.04","SPBC215.05","SPAC140.02","SPBC530.10c","SPAC23A1.10","SPCC188.02","SPCC594.01"],"gene_count":52,"ltp_gene_count":3,"approved_date":"2016-06-30"},{"uniquename":"PMID:20581463","title":"Casein kinase 1 is required for efficient removal of Rec8 during meiosis I.","citation":"Cell Cycle 2010 Jul 01;9(13):2657-62","abstract":"Segregation of chromosomes during meiosis depends on separase cleavage of Rec8, the meiosis-specific alpha-kleisin subunit of cohesin. We mapped Rec8 phosphorylation sites by mass spectrometry and show that Rec8 phosphorylation is required for proper chromosome disjunction during meiosis. We further show that the fission yeast casein kinase 1 (CK1) delta/epsilon isoforms Hhp1 and Hhp2 are required for full levels of Rec8 phosphorylation and for efficient removal of Rec8 at the onset of anaphase I. Our data are consistent with the model that Hhp1/Hhp2-dependent phosphorylation of Rec8 is required for separase-mediated cleavage of Rec8 during meiosis I.","doi":"10.4161/cc.9.13.12146","authors":"Rumpf C, Cipak L, Dudas A, Benko Z, Pozgajova M, Riedel CG, Ammerer G, Mechtler K, Gregan J","authors_abbrev":"Rumpf C et al.","pubmed_publication_date":"01 Jul 2010","pubmed_entrez_date":"2010-06-29","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPAC23C4.12","SPBC3H7.15"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:12515583","title":"No simple dependence between protein evolution rate and the number of protein-protein interactions: only the most prolific interactors tend to evolve slowly.","citation":"BMC Evol Biol 2003 Jan 06;3:1","abstract":"It has been suggested that rates of protein evolution are influenced, to a great extent, by the proportion of amino acid residues that are directly involved in protein function. In agreement with this hypothesis, recent work has shown a negative correlation between evolutionary rates and the number of protein-protein interactions. However, the extent to which the number of protein-protein interactions influences evolutionary rates remains unclear. Here, we address this question at several different levels of evolutionary relatedness.\nManually curated data on the number of protein-protein interactions among Saccharomyces cerevisiae proteins was examined for possible correlation with evolutionary rates between S. cerevisiae and Schizosaccharomyces pombe orthologs. Only a very weak negative correlation between the number of interactions and evolutionary rate of a protein was observed. Furthermore, no relationship was found between a more general measure of the evolutionary conservation of S. cerevisiae proteins, based on the taxonomic distribution of their homologs, and the number of protein-protein interactions. However, when the proteins from yeast were assorted into discrete bins according to the number of interactions, it turned out that 6.5% of the proteins with the greatest number of interactions evolved, on average, significantly slower than the rest of the proteins. Comparisons were also performed using protein-protein interaction data obtained with high-throughput analysis of Helicobacter pylori proteins. No convincing relationship between the number of protein-protein interactions and evolutionary rates was detected, either for comparisons of orthologs from two completely sequenced H. pylori strains or for comparisons of H. pylori and Campylobacter jejuni orthologs, even when the proteins were classified into bins by the number of interactions.\nThe currently available comparative-genomic data do not support the hypothesis that the evolutionary rates of the majority of proteins substantially depend on the number of protein-protein interactions they are involved in. However, a small fraction of yeast proteins with the largest number of interactions (the hubs of the interaction network) tend to evolve slower than the bulk of the proteins.","authors":"Jordan IK, Wolf YI, Koonin EV","authors_abbrev":"Jordan IK et al.","pubmed_publication_date":"06 Jan 2003","pubmed_entrez_date":"2003-01-08","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10571085","title":"S. pombe Pbh1p: an inhibitor of apoptosis domain containing protein is essential for chromosome segregation.","citation":"FEBS Lett 1999 Oct 22;460(1):187-90","abstract":"Proteins containing the baculovirus inhibitor of apoptosis repeats (BIR domains) have been identified in a wide range of species. BIR domain containing proteins are thought to inhibit caspases and thereby cause inhibition of apoptosis. A BIR domain containing protein has been recently identified by the Schizosaccharomyces pombe genome sequencing project. However, caspase-like proteins have not been found in yeasts, suggesting that the BIR domain containing proteins might play a fundamental role in cell regulation, in addition to their well-characterized role in inhibition of apoptosis. In this study, we have characterized Pbh1p, an S. pombe BIR domain containing protein. Construction and analysis of a null mutant in pbh1+ revealed that pbh1+ is essential for cell viability. Moreover, cells devoid of Pbh1p are defective in chromosome condensation and chromosome segregation. Thus, proper chromosome segregation requires the function of Pbh1p. Over-production of Pbh1p led to abnormalities in mitosis and cytokinesis, suggesting that the levels of Pbh1p are important for regulation of mitosis and cytokinesis.","authors":"Rajagopalan S, Balasubramanian MK","authors_abbrev":"Rajagopalan S et al.","pubmed_publication_date":"22 Oct 1999","pubmed_entrez_date":"1999-11-26","publication_year":"1999","canto_session_key":"921e21cdb5841a14","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-09 18:22:07","canto_approved_date":"2020-03-20 17:35:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-17 08:37:25","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC962.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-02-09"},{"uniquename":"PMID:19563123","title":"Microscopy techniques to examine DNA replication in fission yeast.","citation":"Methods Mol Biol 2009;521:463-82","abstract":"Temporal and spatial visualization of replication proteins and associated structures within the narrow confines of a yeast nucleus is technically challenging. Choosing the appropriate method depends upon the parameters of the experiment, the nature of the molecules to be observed, and the hypothesis to be tested. In this chapter, we review three broad types of visualization: whole cell fluorescence or immunofluorescence, which is useful for questions of timing and chromatin association; nuclear spreads, which provide greater resolution within the chromatin for colocalization and region-specific effects; and chromatin fibers, which allow observation of labeled proteins and newly synthesized DNA on a linear chromosome. We discuss applications of these protocols and some considerations for choosing methods and fluorophores.","doi":"10.1007/978-1-60327-815-7_26","authors":"Green MD, Sabatinos SA, Forsburg SL","authors_abbrev":"Green MD et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21559379","title":"The HIRA complex subunit Hip3 plays important roles in the silencing of meiosis-specific genes in Schizosaccharomyces pombe.","citation":"PLoS One 2011 Apr 29;6(4):e19442","abstract":"The control of gene expression is essential for growth and responses to environmental changes in various organisms. It is known that some meiosis-specific genes are silenced during mitosis and expressed upon nitrogen starvation in Schizosaccharomyces pombe. When the factors responsible for this regulation were studied, a hip3 mutant was isolated via discovery of a defect in the transcriptional repression of meiosis-specific genes. Hip3 is a subunit of the HIRA (histone regulatory complex A) complex, which consists of four subunits (Hip1, Hip3, Hip4 and Slm9) and acts as a histone chaperone that is independent of DNA replication.\nIn a search for mutants, the meiosis-specific gene SPCC663.14c(+) was identified by screening for genes that are silenced during mitosis and induced upon nitrogen starvation. A reporter plasmid that expresses the ura4(+) gene driven by the SPCC663.14c(+) promoter was constructed. Screening for suppressor mutants was then carried out in nitrogen-rich medium without uracil. A mutant with a mutation in the hip3(+) gene was isolated and named hip3-1. This mutation alleviated the transcriptional repression of the ura4(+) gene on the reporter plasmid and of the endogenous SPCC663.14c(+) gene in the presence of nitrogen. A ChIP assay revealed that RNA polymerase II (Pol II) and TFIIE were enriched at the SPCC663.14c(+) locus, whereas the levels of histone H3 were decreased in hip3-1 cells. Intriguingly, histone H3 was heavily modified at the SPCC663.14c(+) locus in hip3-1 cells; these modifications included tri-methylation and acetylation of H3 lysine 9 (H3K9), mono-methylation of H3 arginine 2 (H3R2), and tri-methylation of H3 lysine 4 (H3K4). In addition, the tri-methylation of H3K9 and H3K4 were strongly elevated in hip3-1 mutants.\nTaken together, these results indicate that Hip3 plays important roles in the control of histone modifications at meiosis-specific gene loci and induces their transcriptional repression.","doi":"10.1371/journal.pone.0019442","authors":"Mizuki F, Tanaka A, Hirose Y, Ohkuma Y","authors_abbrev":"Mizuki F et al.","pubmed_publication_date":"29 Apr 2011","pubmed_entrez_date":"2011-05-12","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC31F10.14c","SPCC663.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8590407","title":"Increased thermal stability of the enzyme content in permeabilized whole cells from the fission yeast Schizosaccharomyces pombe by exogenous trehalose and other compounds.","citation":"Can J Microbiol 1995 Oct;41(10):936-41","abstract":"Cells of the fission yeast Schizosaccharomyces pombe were permeabilized by treatment with toluene-ethanol. The permeabilized cells lost the bulk of the internal trehalose pool while most of the alkaline phosphatase, invertase, alpha-glucosidase, or neutral trehalase activities located inside the cells remained unaffected. This system was used as an in situ assay to determine the involvement of trehalose in enzyme protection during thermal treatments. The addition of trehalose to suspensions of permeabilized cells resulted in a sugar-dependent thermoprotection of the internal marker enzymes. This approach demonstrates that in whole cells of the fission yeast trehalose plays a physiological role as a protective molecule against thermal denaturation of cellular enzymes.","authors":"Fernández J, Soto T, Vicente-Soler J, Cansado J, Gacto M","authors_abbrev":"Fernández J et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8741848","title":"Nucleolar accumulation of poly (A)+ RNA in heat-shocked yeast cells: implication of nucleolar involvement in mRNA transport.","citation":"Mol Biol Cell 1996 Jan;7(1):173-92","abstract":"Transport of mRNA from the nucleus to the cytoplasm plays an important role in gene expression in eukaryotic cells. In wild-type Schizosaccharomyces pombe cells poly(A)+ RNA is uniformly distributed throughout the nucleoplasm and cytoplasm. However, we found that a severe heat shock blocks mRNA transport in S. pombe, resulting in the accumulation of bulk poly(A)+ RNA, as well as a specific intron-less transcript, in the nucleoli. Pretreatment of cells with a mild heat shock, which induces heat shock proteins, before a severe heat shock protects the mRNA transport machinery and allows mRNA transport to proceed unimpeded. In heat-shocked S. pombe cells, the nucleolar region condensed into a few compact structures. Interestingly, poly(A)+ RNA accumulated predominantly in the condensed nucleolar regions of the heat-shocked cells. These data suggest that the yeast nucleolus may play a role in mRNA transport in addition to its roles in rRNA synthesis and preribosome assembly.","authors":"Tani T, Derby RJ, Hiraoka Y, Spector DL","authors_abbrev":"Tani T et al.","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9177184","title":"Interaction of the S phase regulator cdc18 with cyclin-dependent kinase in fission yeast.","citation":"Proc Natl Acad Sci U S A 1997 Jun 10;94(12):6142-7","abstract":"The fission yeast gene cdc18(+) is required for entry into S phase and for coupling mitosis to the successful completion of S phase. Cdc18 is a highly unstable protein that is expressed only once per cell cycle at the G1/S boundary. Overexpression of Cdc18 causes a mitotic delay and reinitiation of DNA replication, suggesting that the inactivation of Cdc18 plays a role in preventing rereplication within a given cell cycle. In this paper, we present evidence that Cdc18 is associated with active cyclin-dependent kinase in vivo. We have expressed Cdc18 as a glutathione S-transferase fusion in fission yeast and demonstrated that the fusion protein is functional in vivo. We find that the Cdc18 fusion protein copurifies with a kinase activity capable of phosphorylating histone H1 and Cdc18. The activity was identified by a variety of methods as the cyclin-dependent kinase containing the product of the cdc2(+) gene. The amino terminus of Cdc18 is required for association with cyclin-dependent kinase, but the association does not require the consensus cyclin-dependent kinase phosphorylation sites in this region. Additionally, both G1/S and mitotic forms of cyclin-dependent kinase phosphorylate and interact with Cdc18. These interactions between Cdc18 and cyclin-dependent kinases suggest mechanisms by which cyclin-dependent kinases could activate the initiation of DNA replication and could prevent rereplication.","authors":"Brown GW, Jallepalli PV, Huneycutt BJ, Kelly TJ","authors_abbrev":"Brown GW et al.","pubmed_publication_date":"10 Jun 1997","pubmed_entrez_date":"1997-06-10","publication_year":"1997","canto_session_key":"58e0190b91ae4c1c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-08-21 13:59:54","canto_approved_date":"2025-09-04 12:20:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-28 13:57:15","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPBC11B10.09","SPAPB2B4.03","SPBC582.03","SPBC685.09"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-08-21"},{"uniquename":"PMID:11104523","title":"Membrane traffic between genomes.","citation":"Genome Biol 2000;1(1):REVIEWS104","abstract":"Proteins of the Rab and SNARE families target vesicles to their intracellular destinations. A comparison of these families from the budding yeast, fission yeast, nematode and fruitfly genomes has implications for the organization of membrane traffic in different organisms.","authors":"Armstrong J","authors_abbrev":"Armstrong J","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-12-06","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24114984","title":"What is the total number of protein molecules per cell volume? A call to rethink some published values.","citation":"Bioessays 2013 Dec;35(12):1050-5","abstract":"Novel methods such as mass-spectrometry enable a view of the proteomes of cells in unprecedented detail. Recently, these efforts have culminated in quantitative measurements of the number of copies per cell for most expressed proteins in organisms ranging from bacteria to mammalian cells. Here, we estimate the expected total number of proteins per unit of cell volume using known parameters related to the composition of cells such as the fraction of cell mass that is protein, and the average protein length. Using simple arguments, we estimate a range of 2-4 million proteins per cubic micron (i.e. 1 fL) in bacteria, yeast, and mammalian cells. Interestingly, we find that measured values that are reported for fission yeast and mammalian cells are often about 3-10 times lower. We discuss this apparent discrepancy and how to use the estimate as benchmark to recalibrate proteome-wide quantitative censuses or to revisit assumptions about cell composition.","doi":"10.1002/bies.201300066","authors":"Milo R","authors_abbrev":"Milo R","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-10-12","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26869222","title":"Nuclear envelope expansion is crucial for proper chromosomal segregation during a closed mitosis.","citation":"J Cell Sci 2016 Mar 15;129(6):1250-9","abstract":"Here, we screened a 10,371 library of diverse molecules using a drug-sensitive fission yeast strain to identify compounds which cause defects in chromosome segregation during mitosis. We identified a phosphorium-ylide-based compound Cutin-1 which inhibits nuclear envelope expansion and nuclear elongation during the closed mitosis of fission yeast, and showed that its target is the β-subunit of fatty acid synthase. A point mutation in the dehydratase domain of Fas1 conferred in vivo and in vitro resistance to Cutin-1. Time-lapse photomicrography showed that the bulk of the chromosomes were only transiently separated during mitosis, and nucleoli separation was defective. Subsequently sister chromatids re-associated leading to chromosomal mis-segregation. These segregation defects were reduced when the nuclear volume was increased and were increased when the nuclear volume was reduced. We propose that there needs to be sufficient nuclear volume to allow the nuclear elongation necessary during a closed mitosis to take place for proper chromosome segregation, and that inhibition of fatty acid synthase compromises nuclear elongation and leads to defects in chromosomal segregation.","doi":"10.1242/jcs.181560","authors":"Takemoto A, Kawashima SA, Li JJ, Jeffery L, Yamatsugu K, Elemento O, Nurse P","authors_abbrev":"Takemoto A et al.","pubmed_publication_date":"15 Mar 2016","pubmed_entrez_date":"2016-02-13","publication_year":"2016","canto_session_key":"1bc92c0f892db627","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2016-12-04 20:58:14","canto_approved_date":"2025-09-03 16:45:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-04 15:51:06","canto_added_date":"2016-02-14 01:15:13","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":21,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.09c","SPBC146.03c","SPAC24H6.05","SPCC18B5.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-12-04"},{"uniquename":"PMID:12058079","title":"Schizosaccharomyces pombe pfh1+ encodes an essential 5' to 3' DNA helicase that is a member of the PIF1 subfamily of DNA helicases.","citation":"Mol Biol Cell 2002 Jun;13(6):2180-91","abstract":"The Saccharomyces cerevisiae Pif1p DNA helicase is the prototype member of a helicase subfamily conserved from yeast to humans. S. cerevisiae has two PIF1-like genes, PIF1 itself and RRM3, that have roles in maintenance of telomeric, ribosomal, and mitochondrial DNA. Here we describe the isolation and characterization of pfh1+, a Schizosaccharomyces pombe gene that encodes a Pif1-like protein. Pfh1p was the only S. pombe protein with high identity to Saccharomyces Pif1p. Unlike the two S. cerevisiae Pif1 subfamily proteins, the S. pombe Pfh1p was essential. Like Saccharomyces Pif1p, a truncated form of the S. pombe protein had 5' to 3' DNA helicase activity. Point mutations in an invariant lysine residue in the ATP binding pocket of Pfh1p had the same phenotype as deleting pfh1+, demonstrating that the ATPase/helicase activity of Pfh1p was essential. Although mutant spores depleted for Pfh1p proceeded through S phase, they arrested with a terminal cellular phenotype consistent with a postinitiation defect in DNA replication. Telomeric DNA was modestly shortened in the absence of Pfh1p. However, genetic analysis demonstrated that maintenance of telomeric DNA was not the sole essential function of S. pombe Pfh1p.","authors":"Zhou JQ, Qi H, Schulz VP, Mateyak MK, Monson EK, Zakian VA","authors_abbrev":"Zhou JQ et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-06-12","publication_year":"2002","canto_session_key":"784abb5e1b2aad4e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-13 13:46:24","canto_approved_date":"2025-05-19 16:02:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-13 13:45:07","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.14c","SPBC29A3.14c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-08-13"},{"uniquename":"EMBL:AU010774","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23281010","title":"Examining post-translational modification-mediated protein-protein interactions using a chemical proteomics approach.","citation":"Protein Sci 2013 Mar;22(3):287-95","abstract":"Post-translational modifications (PTM) of proteins can control complex and dynamic cellular processes via regulating interactions between key proteins. To understand these regulatory mechanisms, it is critical that we can profile the PTM-dependent protein-protein interactions. However, identifying these interactions can be very difficult using available approaches, as PTMs can be dynamic and often mediate relatively weak protein-protein interactions. We have recently developed CLASPI (cross-linking-assisted and stable isotope labeling in cell culture-based protein identification), a chemical proteomics approach to examine protein-protein interactions mediated by methylation in human cell lysates. Here, we report three extensions of the CLASPI approach. First, we show that CLASPI can be used to analyze methylation-dependent protein-protein interactions in lysates of fission yeast, a genetically tractable model organism. For these studies, we examined trimethylated histone H3 lysine-9 (H3K9Me₃)-dependent protein-protein interactions. Second, we demonstrate that CLASPI can be used to examine phosphorylation-dependent protein-protein interactions. In particular, we profile proteins recognizing phosphorylated histone H3 threonine-3 (H3T3-Phos), a mitotic histone \"mark\" appearing exclusively during cell division. Our approach identified survivin, the only known H3T3-Phos-binding protein, as well as other proteins, such as MCAK and KIF2A, that are likely to be involved in weak but selective interactions with this histone phosphorylation \"mark\". Finally, we demonstrate that the CLASPI approach can be used to study the interplay between histone H3T3-Phos and trimethylation on the adjacent residue lysine 4 (H3K4Me₃). Together, our findings indicate the CLASPI approach can be broadly applied to profile protein-protein interactions mediated by PTMs.","doi":"10.1002/pro.2210","authors":"Li X, Foley EA, Kawashima SA, Molloy KR, Li Y, Chait BT, Kapoor TM","authors_abbrev":"Li X et al.","pubmed_publication_date":"Mar 2013","pubmed_entrez_date":"2013-01-03","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1105.11c","SPAC664.01c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:15802566","title":"Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous.","citation":"Science 2005 May 13;308(5724):1032-4","abstract":"The existence of specialized molecular chaperones that interact directly with ribosomes is well established in microorganisms. Such proteins bind polypeptides exiting the ribosomal tunnel and provide a physical link between translation and protein folding. We report that ribosome-associated molecular chaperones have been maintained throughout eukaryotic evolution, as illustrated by Mpp11, the human ortholog of the yeast ribosome-associated J protein Zuo. When expressed in yeast, Mpp11 partially substituted for Zuo by partnering with the multipurpose Hsp70 Ssa, the homolog of mammalian Hsc70. We propose that in metazoans, ribosome-associated Mpp11 recruits the multifunctional soluble Hsc70 to nascent polypeptide chains as they exit the ribosome.","authors":"Hundley HA, Walter W, Bairstow S, Craig EA","authors_abbrev":"Hundley HA et al.","pubmed_publication_date":"13 May 2005","pubmed_entrez_date":"2005-04-02","publication_year":"2005","canto_session_key":"d9b99ec4e8dd8960","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-09-30 09:37:03","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-09-30 09:36:57","canto_added_date":"2015-09-30 09:24:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1778.01c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-09-30"},{"uniquename":"EMBL:AU011747","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:200419","title":"Change in location of ornithine carbamoyltransferase and carbamoylphosphate synthetase among yeasts in relation to the arginase/ornithine carbamoyltransferase regulatory complex and the energy status of the cells.","citation":"Eur J Biochem 1977 Oct 03;79(2):473-81","abstract":"","authors":"Urrestarazu LA, Vissers S, Wiame JM","authors_abbrev":"Urrestarazu LA et al.","pubmed_publication_date":"03 Oct 1977","pubmed_entrez_date":"1977-10-03","publication_year":"1977","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC215.08c","SPBC56F2.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:15195092","title":"Periodic gene expression program of the fission yeast cell cycle.","citation":"Nat Genet 2004 Aug;36(8):809-17","abstract":"Cell-cycle control of transcription seems to be universal, but little is known about its global conservation and biological significance. We report on the genome-wide transcriptional program of the Schizosaccharomyces pombe cell cycle, identifying 407 periodically expressed genes of which 136 show high-amplitude changes. These genes cluster in four major waves of expression. The forkhead protein Sep1p regulates mitotic genes in the first cluster, including Ace2p, which activates transcription in the second cluster during the M-G1 transition and cytokinesis. Other genes in the second cluster, which are required for G1-S progression, are regulated by the MBF complex independently of Sep1p and Ace2p. The third cluster coincides with S phase and a fourth cluster contains genes weakly regulated during G2 phase. Despite conserved cell-cycle transcription factors, differences in regulatory circuits between fission and budding yeasts are evident, revealing evolutionary plasticity of transcriptional control. Periodic transcription of most genes is not conserved between the two yeasts, except for a core set of approximately 40 genes that seem to be universally regulated during the eukaryotic cell cycle and may have key roles in cell-cycle progression.","authors":"Rustici G, Mata J, Kivinen K, Lió P, Penkett CJ, Burns G, Hayles J, Brazma A, Nurse P, Bähler J","authors_abbrev":"Rustici G et al.","pubmed_publication_date":"Aug 2004","pubmed_entrez_date":"2004-06-15","publication_year":"2004","canto_session_key":"f167451b59729b35","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-03-14 11:09:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-03-14 11:09:07","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4C3.12","SPAC23C11.16","SPBC2F12.13","SPAC6G10.12c","SPBC16G5.15c","SPBC32F12.09","SPCC320.13c","SPAC4A8.05c"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2017-03-14"},{"uniquename":"EMBL:AB084869","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.57"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2557350","title":"Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growth.","citation":"J Cell Biol 1989 Dec;109(6 Pt 2):3223-30","abstract":"We have isolated and sequenced genes from Saccharomyces cerevisiae (SRP54SC) and Schizosaccharomyces pombe (SRP54sp) encoding proteins homologous to both the 54-kD protein subunit (SRP54mam) of the mammalian signal recognition particle (SRP) and the product of a gene of unknown function in Escherichia coli, ffh (Römisch, K., J. Webb, J. Herz, S. Prehn, R. Frank, M. Vingron, and B. Dobberstein. 1989. Nature (Lond.). 340:478-482; Bernstein H. D., M. A. Poritz, K. Strub, P. J. Hoben, S. Brenner, P. Walter. 1989. Nature (Lond.). 340:482-486). To accomplish this we took advantage of short stretches of conserved sequence between ffh and SRP54mam and used the polymerase chain reaction (PCR) to amplify fragments of the homologous yeast genes. The DNA sequences predict proteins for SRP54sc and SRP54sp that are 47% and 52% identical to SRP54mam, respectively. Like SRP54mam and ffh, both predicted yeast proteins contain a GTP binding consensus sequence in their NH2-terminal half (G-domain), and methionine-rich sequences in their COOH-terminal half (M-domain). In contrast to SRP54mam and ffh the yeast proteins contain additional Met-rich sequences inserted at the COOH-terminal portion of the M-domain. SRP54sp contains a 480-nucleotide intron located 78 nucleotides from the 5' end of the open reading frame. Although the function of the yeast homologues is unknown, gene disruption experiments in S. cerevisiae show that the gene is essential for growth. The identification of SRP54sc and SRP54sp provides the first evidence for SRP related proteins in yeast.","authors":"Hann BC, Poritz MA, Walter P","authors_abbrev":"Hann BC et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_session_key":"3606e930415e37a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-12 16:09:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-12 16:09:23","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.06c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-12"},{"uniquename":"PMID:18256600","title":"Formation and branch migration of Holliday junctions mediated by eukaryotic recombinases.","citation":"Nature 2008 Feb 21;451(7181):1018-21","abstract":"Holliday junctions (HJs) are key intermediates in homologous recombination and are especially important for the production of crossover recombinants. Bacterial RecA family proteins promote the formation and branch migration of HJs in vitro by catalysing a reciprocal DNA-strand exchange reaction between two duplex DNA molecules, one of which contains a single-stranded DNA region that is essential for initial nucleoprotein filament formation. This activity has been reported only for prokaryotic RecA family recombinases, although eukaryotic homologues are also essential for HJ production in vivo. Here we show that fission yeast (Rhp51) and human (hRad51) RecA homologues promote duplex-duplex DNA-strand exchange in vitro. As with RecA, a HJ is formed between the two duplex DNA molecules, and reciprocal strand exchange proceeds through branch migration of the HJ. In contrast to RecA, however, strand exchange mediated by eukaryotic recombinases proceeds in the 3'-->5' direction relative to the single-stranded DNA region of the substrate DNA. The opposite polarity of Rhp51 makes it especially suitable for the repair of DNA double-strand breaks, whose repair is initiated at the processed ends of breaks that have protruding 3' termini.","doi":"10.1038/nature06609","authors":"Murayama Y, Kurokawa Y, Mayanagi K, Iwasaki H","authors_abbrev":"Murayama Y et al.","pubmed_publication_date":"21 Feb 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35314558","title":"Ellagic Acid Combined with Tacrolimus Showed Synergistic Cell Growth Inhibition in Fission Yeast.","citation":"Biocontrol Sci 2022;27(1):31-39","abstract":"Calcineurin (CN) is a conserved Ca 2+ -calmodulin activated protein phosphatase, which plays important roles in immune regulation, cardiac hypertrophy, and apoptosis in humans. In pathogenic fungi, CN is essential for stress survival, sexual development, and virulence. The immunosuppressant tacrolimus (FK506) is a specific inhibitor of CN in humans and fungi including nonpathogenic fission yeast. Although calcineurin inhibition by FK506 or CN deletion in fission yeast does not induce growth defects, treatment with some anti-fungal drugs such as micafungin and valproic acid, induced synthetic lethality with calcineurin inhibition. Here, we searched for the compounds that induce synthetic growth defects with CN inhibition in fission yeast. We found that ellagic acid (EA) preferentially induced growth inhibition in CN deletion cells. Consistently, co-treatment with EA and FK506 induced severe growth inhibition in the wild-type cells, whereas neither of the single treatment with each compound did so. Moreover, deletion of the calcineurin-regulated transcription factor Prz1 also induced a marked EA sensitivity. Intriguingly, EA also enhanced the growth inhibitory effect of other anti-fungal drugs, including micafungin and miconazole. Thus, our data suggesting the synergistic growth inhibitory effect of the calcineurin inhibitor FK506 and EA may be useful to understand the mechanism to overcome the antifungal resistance.","doi":"10.4265/bio.27.31","authors":"Hagihara K, Hosonaka K, Hoshino S, Iwata K, Ogawa N, Satoh R, Takasaki T, Maeda T, Sugiura R","authors_abbrev":"Hagihara K et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-03-22","publication_year":"2022","canto_session_key":"be36348b82e1f2a0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-03-24 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26211610","title":"Cdc123, a Cell Cycle Regulator Needed for eIF2 Assembly, Is an ATP-Grasp Protein with Unique Features.","citation":"Structure 2015 Sep 01;23(9):1596-1608","abstract":"Eukaryotic initiation factor 2 (eIF2), a heterotrimeric guanosine triphosphatase, has a central role in protein biosynthesis by supplying methionylated initiator tRNA to the ribosomal translation initiation complex and by serving as a target for translational control in response to stress. Recent work identified a novel step indispensable for eIF2 function: assembly of eIF2 from its three subunits by the cell proliferation protein Cdc123. We report the first crystal structure of a Cdc123 representative, that from Schizosaccharomyces pombe, both isolated and bound to domain III of Saccharomyces cerevisiae eIF2γ. The structures show that Cdc123 resembles enzymes of the ATP-grasp family. Indeed, Cdc123 binds ATP-Mg(2+), and conserved residues contacting ATP-Mg(2+) are essential for Cdc123 to support eIF2 assembly and cell viability. A docking of eIF2αγ onto Cdc123, combined with genetic and biochemical experiments, allows us to propose a model explaining how Cdc123 participates in the biogenesis of eIF2 through facilitating assembly of eIF2γ to eIF2α.","doi":"10.1016/j.str.2015.06.014","authors":"Panvert M, Dubiez E, Arnold L, Perez J, Mechulam Y, Seufert W, Schmitt E","authors_abbrev":"Panvert M et al.","pubmed_publication_date":"01 Sep 2015","pubmed_entrez_date":"2015-07-28","publication_year":"2015","canto_session_key":"ece9ad1695cc8646","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-08-25 11:21:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-08-25 11:21:33","canto_added_date":"2015-07-29 00:21:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP27G11.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-08-25","pdb_entries":[{"pdb_id":"4zgn","gene_chains":[{"gene_uniquename":"SPAP27G11.03","chain":"A","position":"1-319"}],"title":"Structure Cdc123 complexed with the C-terminal domain of eIF2gamma","entry_authors":"Panvert M,Dubiez E,Arnold L,Perez J,Seufert W,Mechulam Y,Schmitt E","entry_authors_abbrev":"Panvert M et al.","reference_uniquename":"PMID:26211610","experimental_method":"X-ray","resolution":"2.9"},{"pdb_id":"4zgp","gene_chains":[{"gene_uniquename":"SPAP27G11.03","chain":"A/B","position":"1-274"}],"title":"Structure of Cdc123 from Schizosaccharomyces pombe","entry_authors":"Panvert M,Dubiez E,Arnold L,Perez J,Seufert W,Mechulam Y,Schmitt E","entry_authors_abbrev":"Panvert M et al.","reference_uniquename":"PMID:26211610","experimental_method":"X-ray","resolution":"1.85"},{"pdb_id":"4zgq","gene_chains":[{"gene_uniquename":"SPAP27G11.03","chain":"A","position":"1-319"}],"title":"Structure of Cdc123 bound to eIF2-gammaDIII domain","entry_authors":"Panvert M,Dubiez E,Arnold L,Perez J,Seufert W,Mechulam Y,Schmitt E","entry_authors_abbrev":"Panvert M et al.","reference_uniquename":"PMID:26211610","experimental_method":"X-ray","resolution":"3.0"},{"pdb_id":"4zgo","gene_chains":[{"gene_uniquename":"SPAP27G11.03","chain":"A/B","position":"1-319"}],"title":"Structure of C-terminally truncated Cdc123 from Schizosaccharomyces pombe","entry_authors":"Panvert M,Dubiez E,Arnold L,Perez J,Seufert W,Mechulam Y,Schmitt E","entry_authors_abbrev":"Panvert M et al.","reference_uniquename":"PMID:26211610","experimental_method":"X-ray","resolution":"2.063"}]},{"uniquename":"PMID:26024503","title":"Mechanical and molecular basis for the symmetrical division of the fission yeast nuclear envelope.","citation":"Phys Chem Chem Phys 2015 Jun 28;17(24):15629-36","abstract":"In fission yeast Schizosaccharomyces pombe, the nuclear envelope remains intact throughout mitosis and undergoes a series of symmetrical morphological changes when the spindle pole bodies (SPBs), embedded in the nuclear envelope, are pushed apart by elongating spindle microtubules. These symmetrical membrane shape transformations do not correspond to the shape behavior of an analogous system based on lipid vesicles. Here we report that the symmetry of the dividing fission yeast nucleus is ensured by SPB-chromosome attachments, as loss of kinetochore clustering in the vicinity of SPBs results in the formation of abnormal asymmetric shapes with long membrane tethers. We integrated these findings in a biophysical model, which explains the symmetry of the nuclear shapes on the basis of forces exerted by chromosomes clustered at SPBs on the extending nuclear envelope. Based on this analysis we conclude that the fission yeast nuclear envelope exhibits the same mechanical properties as simple lipid vesicles, but interactions with other cellular components, such as chromosomes, influence the nuclear shape during mitosis, allowing the formation of otherwise energetically unfavorable symmetrical dumbbell structures upon spindle elongation. The model allows us to explain the appearance of abnormal asymmetric shapes in fission yeast mutants with mis-segregated chromosomes as well as with altered nuclear membrane composition.","doi":"10.1039/c5cp01243k","authors":"Castagnetti S, Božič B, Svetina S","authors_abbrev":"Castagnetti S et al.","pubmed_publication_date":"28 Jun 2015","pubmed_entrez_date":"2015-05-30","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-05-31 00:19:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15796926","title":"Localization and function of three monothiol glutaredoxins in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2005 May 06;330(2):604-10","abstract":"The fission yeast Schizosaccharomyces pombe contains two dithiol glutaredoxins (Grx1 and Grx2) and genes for three putative monothiol glutaredoxins (grx3, 4, and 5). We investigated the expression, sub-cellular localization, and functions of the three monothiol glutaredoxins. Fluorescence microscopy revealed that Grx3 is targeted to nuclear rim and endoplasmic reticulum, Grx4 primarily to the nucleus, and Grx5 to mitochondria. Null mutation of grx3 did not significantly affect growth and resistance against various oxidants, whereas grx5 mutation caused slow growth and sensitivity toward oxidants such as hydrogen peroxide, paraquat, and diamide. The grx2grx5 double mutation, deficient in all mitochondrial glutaredoxins, caused further retardation in growth and severe sensitivity toward all the oxidants tested. The grx4 mutation was not viable, suggesting a critical role of Grx4 for the physiology of S. pombe. Overproduction of Grx3 and Grx5, but not the truncated form of Grx5 without mitochondrial target sequence, severely retarded growth as Grx2 did, supporting the idea that Grx2, 3, and 5 are targeted to organellar compartments. Our results propose a distinct role for each glutaredoxin to maintain thiol redox balance, and hence the growth and stress resistance, of the fission yeast.","authors":"Chung WH, Kim KD, Roe JH","authors_abbrev":"Chung WH et al.","pubmed_publication_date":"06 May 2005","pubmed_entrez_date":"2005-03-31","publication_year":"2005","canto_session_key":"64a7476996f97189","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-03 11:02:18","canto_approved_date":"2022-02-07 17:18:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 14:52:59","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15E1.09","SPBC26H8.06","SPCC1450.06c","SPAPB2B4.02","SPAC4F10.20"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-06-03"},{"uniquename":"PMID:8574406","title":"Adaptive response of Schizosaccharomyces pombe to hydrogen peroxide and menadione.","citation":"Microbiology (Reading) 1995 Dec;141 ( Pt 12):3127-32","abstract":"The response of Schizosaccharomyces pombe to oxidative stresses has been examined. On challenging Schiz. pombe for 60 min at early exponential phase with either 40 mM H2O2 or 6 mM menadione (MD), a superoxide-generating agent, less than 10% of the cells survived. Pretreating Schiz. pombe cells with 0.2 mM H2O2 or 0.2 mM MD for 1 h significantly increased survival of these lethal doses of each oxidant, indicating the existence of an adaptive response to oxidative stress. Furthermore, cells pretreated with a low dose of MD became resistant to a lethal dose of H2O2. However, cells pretreated with H2O2 became only partially resistant to a lethal dose of MD. Adaptation was accompanied by the induction of several oxidative defence enzymes. The presence of 0.2 mM H2O2 induced catalase by 2.8-fold and peroxidase by 2.0-fold The presence of 0.2 mM MD induced catalase by 2.0-fold, glucose-6-phosphate dehydrogenase by 1.9-fold, glutathione reductase by 2.7-fold, peroxidase by 3.0-fold, and superoxide dismutase (SOD) by 2.1-fold. The higher induction of these defence enzymes by MD may explain why MD-pretreated cells were better adapted to lethal doses of oxidants than H2O2-pretreated ones. All these enzymes except SOD and peroxidase increased more than 5.0-fold as cells proceeded into stationary phase. The GSH/GSSG ratio also increased by 60%. These changes accord with the observation that stationary phase cells survive oxidant treatment better than cells in vegetative growth.","authors":"Lee J, Dawes IW, Roe JH","authors_abbrev":"Lee J et al.","pubmed_publication_date":"Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2598273","title":"Some of the swi genes of Schizosaccharomyces pombe also have a function in the repair of radiation damage.","citation":"Curr Genet 1989 Aug;16(2):89-94","abstract":"In Schizosaccharomyces pombe the frequency of mating-type (MT) switching is reduced by mutations in the swi genes. The ten hitherto known swi genes can be subdivided into three classes: Ia, Ib and II. Strains having swi5 (class Ib), swi9 (class II) and swi10 (class II) mutations do not only show reduced MT switching, but also exhibit an increased sensitivity to UV- and gamma-rays. For that reason, 19 previously described rad genes were tested for their effect on MT switching. We found that swi9, \"rad10\", \"rad16\" and \"rad20\" are allelic with each other indicating that the former allocation of these rad mutations to three different genes must have been erroneous. Among the remaining 16 rad genes examined, rad22 seems to be a new class II swi gene. The double mutants swi5 swi9 and swi5 swi10, but not swi9 swi10, are much more sensitive to radiation than the respective single mutants. Thus a cumulative increase in sensitivity occurs only if the mutants belong to different classes; previously the same correlation was found with regard to cumulative effects in MT switching.","authors":"Schmidt H, Kapitza-Fecke P, Stephen ER, Gutz H","authors_abbrev":"Schmidt H et al.","pubmed_publication_date":"Aug 1989","pubmed_entrez_date":"1989-08-01","publication_year":"1989","canto_session_key":"04fb586f59d968bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-12-12 03:41:36","canto_approved_date":"2023-09-08 09:12:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-21 11:20:09","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.15c","SPCC970.01","SPBC409.03","SPAC30D11.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-12-12"},{"uniquename":"PMID:39391964","title":"Evolutionary modes of wtf meiotic driver genes in Schizosaccharomyces pombe.","citation":"Genome Biol Evol 2024 Oct 11;","abstract":"Killer meiotic drivers (KMDs) are a class of selfish genetic elements that bias inheritance in their favor by destroying meiotic progeny that do not carry them. How KMDs evolve is not well understood. In the fission yeast Schizosaccharomyces pombe, the largest gene family, known as the wtf genes, is a KMD family that causes intraspecific hybrid sterility. Here, we investigate how wtf genes evolve using long-read-based genome assemblies of 31 distinct S. pombe natural isolates, which encompass the known genetic diversity of S. pombe. Our analysis, involving nearly 1,000 wtf genes in these isolates, yields a comprehensive portrayal of the intraspecific diversity of wtf genes. Leveraging single-nucleotide polymorphisms in adjacent unique sequences, we pinpoint wtf-gene-containing loci that have recently undergone gene conversion events and infer their pre-gene-conversion state. These events include the revival of wtf pseudogenes, lending support to the notion that gene conversion plays a role in preserving this gene family from extinction. Moreover, our investigation reveals that solo long terminal repeats (LTRs) of retrotransposons, frequently found near wtf genes, can act as recombination arms, influencing the upstream regulatory sequences of wtf genes. Additionally, our exploration of the outer boundaries of wtf genes uncovers a previously unrecognized type of directly oriented repeats flanking wtf genes. These repeats may have facilitated the early expansion of the wtf gene family in S. pombe. Our findings enhance the understanding of the mechanisms influencing the evolution of this KMD gene family.","doi":"10.1093/gbe/evae221","authors":"Xu YH, Suo F, Zhang XR, Du TY, Hua Y, Jia GS, Zheng JX, Du LL","authors_abbrev":"Xu YH et al.","pubmed_publication_date":"11 Oct 2024","pubmed_entrez_date":"2024-10-11","publication_year":"2024","canto_session_key":"6679b7b03789d727","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-10-11 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9552387","title":"Regulation of Cdc2 activity by phosphorylation at T14/Y15.","citation":"Prog Cell Cycle Res 1996;2:99-105","abstract":"The highly conserved Cdc2 serine/threonine kinase plays a central role in cell cycle progression. Although Cdc2 levels remain constant throughout the cell cycle, Cdc2 kinase activity peaks at the G2/M boundary, in order to drive entry into mitosis. In the model organism Schizosaccharomysces pombe, potentially active Cdc2/Cdc13 kinase complex accumulates throughout the S and G2 phases of the cell cycle. This complex, however, is maintained in an active state by Wee1/Mik1-mediated phosphorylation at Y15 (and, possibly, T14). At the G2/M boundary, the Cdc25 protein phosphatase is activated to dephosphorylate the Cdc2/Cdc13 complex, resulting in abrupt activation of Cdc2 kinase activity and entry into mitosis.","authors":"Berry LD, Gould KL","authors_abbrev":"Berry LD et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27098497","title":"CRL4(Wdr70) regulates H2B monoubiquitination and facilitates Exo1-dependent resection.","citation":"Nat Commun 2016 Apr 21;7:11364","abstract":"Double-strand breaks repaired by homologous recombination (HR) are first resected to form single-stranded DNA, which binds replication protein A (RPA). RPA attracts mediators that load the Rad51 filament to promote strand invasion, the defining feature of HR. How the resection machinery navigates nucleosome-packaged DNA is poorly understood. Here we report that in Schizosaccharomyces pombe a conserved DDB1-CUL4-associated factor (DCAF), Wdr70, is recruited to DSBs as part of the Cullin4-DDB1 ubiquitin ligase (CRL4(Wdr70)) and stimulates distal H2B lysine 119 mono-ubiquitination (uH2B). Wdr70 deletion, or uH2B loss, results in increased loading of the checkpoint adaptor and resection inhibitor Crb2(53BP1), decreased Exo1 association and delayed resection. Wdr70 is dispensable for resection upon Crb2(53BP1) loss, or when the Set9 methyltransferase that creates docking sites for Crb2 is deleted. Finally, we establish that this histone regulatory cascade similarly controls DSB resection in human cells.","doi":"10.1038/ncomms11364","authors":"Zeng M, Ren L, Mizuno K, Nestoras K, Wang H, Tang Z, Guo L, Kong D, Hu Q, He Q, Du L, Carr AM, Liu C","authors_abbrev":"Zeng M et al.","pubmed_publication_date":"21 Apr 2016","pubmed_entrez_date":"2016-04-22","publication_year":"2016","canto_session_key":"3a957560e28cf7a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Cong Liu","canto_first_approved_date":"2018-10-04 09:13:47","canto_approved_date":"2023-04-14 16:54:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-04 04:14:45","canto_added_date":"2016-04-23 00:15:13","annotation_curators":[{"name":"Cong Liu","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":101,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.07c","SPCC622.09","SPAC1687.13c","SPCC338.08","SPBC660.13c","SPBC215.03c","SPAC2G11.12","SPAC13A11.04c","SPCC1259.13","SPAC29B12.03","SPAC343.17c","SPAC30D11.10","SPAC17H9.10c","SPAC3A11.08","SPBC29A10.05","SPAC13C5.07","SPCC4B3.12","SPBC216.05","SPBC342.05","SPCC1919.15"],"gene_count":20,"ltp_gene_count":14,"approved_date":"2018-10-04"},{"uniquename":"PMID:24497846","title":"A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability.","citation":"PLoS Genet 2014 Jan;10(1):e1004140","abstract":"Cells are regularly exposed to stress conditions that may lead to protein misfolding. To cope with this challenge, molecular chaperones selectively target structurally perturbed proteins for degradation via the ubiquitin-proteasome pathway. In mammals the co-chaperone BAG-1 plays an important role in this system. BAG-1 has two orthologues, Bag101 and Bag102, in the fission yeast Schizosaccharomyces pombe. We show that both Bag101 and Bag102 interact with 26S proteasomes and Hsp70. By epistasis mapping we identify a mutant in the conserved kinetochore component Spc7 (Spc105/Blinkin) as a target for a quality control system that also involves, Hsp70, Bag102, the 26S proteasome, Ubc4 and the ubiquitin-ligases Ubr11 and San1. Accordingly, chromosome missegregation of spc7 mutant strains is alleviated by mutation of components in this pathway. In addition, we isolated a dominant negative version of the deubiquitylating enzyme, Ubp3, as a suppressor of the spc7-23 phenotype, suggesting that the proteasome-associated Ubp3 is required for this degradation system. Finally, our data suggest that the identified pathway is also involved in quality control of other kinetochore components and therefore likely to be a common degradation mechanism to ensure nuclear protein homeostasis and genome integrity.","doi":"10.1371/journal.pgen.1004140","authors":"Kriegenburg F, Jakopec V, Poulsen EG, Nielsen SV, Roguev A, Krogan N, Gordon C, Fleig U, Hartmann-Petersen R","authors_abbrev":"Kriegenburg F et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2014-02-06","publication_year":"2014","canto_session_key":"aec91591ee01e7f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_first_approved_date":"2015-04-27 15:35:42","canto_approved_date":"2026-01-30 15:33:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-05 14:12:17","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":40,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.14","SPBC14F5.07","SPBP19A11.03c","SPBC4.07c","SPBC16G5.11c","SPAC15A10.11","SPACUNK4.06c","SPAC6C3.08","SPAC24B11.07c","SPBC17D11.02c","SPAC664.11","SPBC530.03c","SPAC167.07c","SPBC19C7.02","SPAC31G5.13","SPAC17H9.19c","SPCC11E10.08","SPAC664.10","SPAC1687.20c","SPBP8B7.08c","SPCC1919.03c","SPCC1020.02","SPBC2A9.04c","SPBC119.02","SPBP8B7.21","SPCC162.11c"],"gene_count":26,"ltp_gene_count":26,"approved_date":"2015-04-27"},{"uniquename":"PMID:12734194","title":"The glutathione synthetase of Schizosaccharomyces pombe is synthesized as a homodimer but retains full activity when present as a heterotetramer.","citation":"J Biol Chem 2003 Oct 10;278(41):40152-61","abstract":"Glutathione synthetase was overexpressed as a histidine-tagged protein in Schizosaccharomyces pombe and purified by two-step affinity chromatography. The recovered enzyme occurred in two different forms: a homodimeric protein consisting of two identical 56-kDa subunits and a heterotetrameric protein composed of two 32-kDa and two 24-kDa subfragments. Both forms are encoded by the GSH2 gene. The 56-Da protein corresponds to the complete GSH2 open reading frame, while the subfragments are produced following the cleavage of this larger protein by a metalloprotease. A stable homodimer was obtained by site-directed mutagenesis to remove the protease cleavage site, and this showed normal activity. A structural model of the fission yeast glutathione synthetase was produced, based on the x-ray coordinates of the human enzyme. According to this model the interacting domains of the proteolytic subfragments are strongly entangled. The subfragments were therefore coexpressed as independent proteins. These subfragments assembled correctly to yield functional heterotetramers with equivalent activity to the wild type enzyme. Furthermore, a permuted version of the protein was created. This also showed normal levels of glutathione synthetase activity. These data provide novel insight into the mechanisms of protein folding and the structure and evolution of the glutathione synthetase family.","authors":"Phlippen N, Hoffmann K, Fischer R, Wolf K, Zimmermann M","authors_abbrev":"Phlippen N et al.","pubmed_publication_date":"10 Oct 2003","pubmed_entrez_date":"2003-05-08","publication_year":"2003","canto_session_key":"2a242dacca6eb363","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-24 17:06:55","canto_approved_date":"2024-03-28 14:52:16","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-11-24 17:06:42","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-24"},{"uniquename":"PMID:1705653","title":"The mitochondrial genome of fission yeast: inability of all introns to splice autocatalytically, and construction and characterization of an intronless genome.","citation":"Mol Gen Genet 1991 Jan;225(1):158-67","abstract":"In this paper we report the inability of four group I introns in the gene encoding subunit I of cytochrome c oxidase (cox1) and the group II intron in the apocytochrome b gene (cob) to splice autocatalytically. Furthermore we present the characterization of the first cox1 intron in the mutator strain anar-14 and the construction and characterization of strains with intronless mitochondrial genomes. We provide evidence that removal of introns at the DNA level (termed DNA splicing) is dependent on an active RNA maturase. Finally we demonstrate that the absence of introns does not abolish homologous mitochondrial recombination.","authors":"Schäfer B, Merlos-Lange AM, Anderl C, Welser F, Zimmer M, Wolf K","authors_abbrev":"Schäfer B et al.","pubmed_publication_date":"Jan 1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3882415","title":"Increased mutagenicity of chromium compounds by nitrilotriacetic acid.","citation":"Environ Mutagen 1985;7(2):185-200","abstract":"Nitrilotriacetic acid trisodium salt (NTA), which is a substitute for polyphosphates in household laundry detergents, and N-nitrosoiminodiacetic acid (NIDA), a derivative of NTA produced by metabolism of soil microorganisms, were tested for in vitro mutagenicity in bacteria and yeasts. No gene reversions in five strains of Salmonella typhimurium (TA 1535, TA1537, TA1538, TA98, and TA100), no forward gene mutations in Schizosaccharomyces pombe P1, and no mitotic gene conversions at two loci in Saccharomyces cerevisiae D4 were induced by NTA (up to 870 micrograms/plate or 40 micrograms/ml) and NIDA (up to 2,000 micrograms/plate or 1,000 micrograms/ml), independently of the presence of rat liver metabolic activation. The influence of NTA on the mutagenic and clastogenic activity of several chromium compounds was examined in the Salmonella/microsome assay and in the sister chromatid exchange (SCE) assay in mammalian cell cultures (Chinese hamster ovary [CHO] line). NTA does not affect the genetic inactivity of water-soluble Cr(III) (Cr2[SO4]3) and the direct mutagenicity of soluble Cr(VI) (Na2CrO4,K2Cr2O7) compounds. The very insoluble Cr(VI) compounds PbCrO4 and PbCrO4 X PbO are instead clearly mutagenic in the Salmonella/microsome assay (TA100 strain) only in the presence of NTA or NaOH. The mutagenicity of lead chromates is correlated with the amounts of Cr(VI) solubilized by NTA or alkali, as detected by the colorimetric reaction with diphenylcarbazide and atomic absorption spectrophotometry. In the SCE assay, the insoluble lead chromates are directly clastogenic owing to prolonged treatment conditions and cellular endocytosis. The chromosome-damaging activity of PbCrO4 is significantly increased by NTA but not by NaOH.","authors":"Loprieno N, Boncristiani G, Venier P, Montaldi A, Majone F, Bianchi V, Paglialunga S, Levis AG","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12479804","title":"Dma1 prevents mitotic exit and cytokinesis by inhibiting the septation initiation network (SIN).","citation":"Dev Cell 2002 Dec;3(6):779-90","abstract":"In the fission yeast Schizosaccharomyces pombe, the septation initiation network (SIN) triggers cytokinesis after mitosis. We investigated the relationship between Dma1p, a spindle checkpoint protein and cytokinesis inhibitor, and the SIN. Deletion of dma1 inactivates the spindle checkpoint and allows precocious SIN activation, while overexpressing Dma1p reduces SIN signaling. Dma1p seems to function by inhibiting the SIN activator, Plo1p kinase, since dma1 overexpression and deletion phenotypes suggest that Dma1p antagonizes Plo1p localization. Furthermore, failure to maintain high cyclin-dependent kinase (CDK) activity during spindle checkpoint activation in dma1 deletion cells requires Plo1p. Dma1p itself localizes to spindle pole bodies through interaction with Sid4p. Our observations suggest that Dma1p functions to prevent mitotic exit and cytokinesis during spindle checkpoint arrest by inhibiting SIN signaling.","authors":"Guertin DA, Venkatram S, Gould KL, McCollum D","authors_abbrev":"Guertin DA et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2002-12-14","publication_year":"2002","canto_session_key":"c5face93b651d68a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-02-02 11:00:22","canto_approved_date":"2022-09-22 08:09:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-30 17:35:51","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1782.09c","SPBC11B10.09","SPBC26H8.07c","SPAC23C11.16","SPAC6F6.08c","SPAC24B11.11c","SPAC9G1.09","SPBC244.01c","SPAC17G8.10c","SPBC21.06c"],"gene_count":10,"ltp_gene_count":5,"approved_date":"2019-02-02"},{"uniquename":"PMID:30123624","title":"Antifungal compound honokiol triggers oxidative stress responsive signalling pathway and modulates central carbon metabolism.","citation":"Mycology 2016;7(3):124-133","abstract":"The fast growing evidences have shown that the plant-derived compound honokiol is a promising candidate for treating multiple human diseases, such as inflammation and cancer. However, the mode-of-action (MoA) of honokiol remains largely unclear. Here, we studied the antifungal activity of honokiol in fission yeast model, with the goal of understanding the honokiol's mechanism of action from the molecular level. We found that honokiol can inhibit the yeast growth at a dose-dependent way. Microarray analysis showed that honokiol has wide impacts on the fission yeast transcription levels (in total, 512 genes are up-regulated, and 42 genes are down-regulated). Gene set enrichment analysis indicated that over 45% up-regulated genes belong to the core environmental stress responses category. Moreover, network analysis suggested that there are extensive gene-gene interactions amongst the co-expression gene lists, which can assemble several biofunctionally important modules. It is noteworthy that several key components of central carbon metabolism, such as glucose transporters and metabolic enzymes of glycolysis, are involved in honokiol's MoA. The complexity of the honokiol's MoA displayed in previous studies and this work demonstrates that multiple omics approaches and bioinformatics tools should be applied together to achieve the complete scenario of honokiol's antifungal function.","doi":"10.1080/21501203.2016.1221862","authors":"Wang Z, Shen Y","authors_abbrev":"Wang Z et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2018-08-21","publication_year":"2016","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2018-08-23 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21057196","title":"Prevention of merotelic chromosome attachments by the monopolin complex.","citation":"Cell Cycle 2010 Nov 01;9(21):4258","abstract":"","doi":"10.4161/cc.9.21.13526","authors":"McCollum D","authors_abbrev":"McCollum D","pubmed_publication_date":"01 Nov 2010","pubmed_entrez_date":"2010-11-09","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10547441","title":"Ultrastructure of cell wall of the cps8 actin mutant cell in Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 1999 Nov 01;180(1):31-7","abstract":"A Schizosaccharomyces pombe cps8 mutant, of which the gene encodes a mutant actin with an amino acid substitution of Asp for Gly(273) [J. Ishiguro and W. Kobayashi (1996) FEBS Lett. 392, 237-241], was used to determine the role of the actin cytoskeleton in cell wall formation. In the cps8 mutant cells, atomic force microscopic and scanning electron microscopic images showed abnormal depolarized and branched morphology. Fibrous material covered a part of the surface of growing cps8 cells. Transmission electron microscopic images showed variable thickness of the cell wall due to multilayering of cell wall materials, and aberrant multisepta due to diagonal growth of the primary septum, whereas the normal primary septum grows at a right angle from the cortex. This abnormal septum formation may induce abnormality of the cell with multinuclei and/or multisepta, caused by non-separation of daughter cells. These results indicate that actin plays an important role in cell wall and septum formation.","authors":"Ishijima SA, Konomi M, Takagi T, Sato M, Ishiguro J, Osumi M","authors_abbrev":"Ishijima SA et al.","pubmed_publication_date":"01 Nov 1999","pubmed_entrez_date":"1999-11-05","publication_year":"1999","canto_session_key":"8355ff75101b4d60","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-16 09:18:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-22 15:32:28","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-22"},{"uniquename":"GO_REF:0000063","title":"Representation of processes regulated by other regulating processes in the Gene Ontology","abstract":"We have created a standard template for classes describing processes regulated by other regulating processes. The underlying equivalence axiom template is \"R and 'results_in' some P\", where R is a biological process and P is a regulation of biological process subclass.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8702843","title":"Purification, gene cloning, and reconstitution of the heterotrimeric single-stranded DNA-binding protein from Schizosaccharomyces pombe.","citation":"J Biol Chem 1996 Aug 23;271(34):20868-78","abstract":"We have purified a single-stranded DNA-binding protein (SSB) from Schizosaccharomyces pombe (Sp) and have shown that it is composed of three subunits of 68, 30, and 12 kDa. The SpSSB supports T antigen-dependent unwinding of SV40 ori containing DNA, but is not functional in the SV40 in vitro replication reaction. All three genes that encode the SpSSB subunit have been isolated. The cloned cDNA of the ssb1(+), encoding the p68 subunit, contains 609 amino acids (68.3 kDa), while that of the ssb2(+), encoding the p30 subunit, contains a 279 amino acids (30.3 kDa). The genomic DNA clone of the p12 subunit gene (ssb3(+)) has 2 introns and an open reading frame of 104 amino acids (11.8 kDa). Significant homology is observed among the largest and middle subunits of eukaryotic SSBs, but there is poor homology among the smallest subunits. In addition, we have reconstituted the SpSSB complex by coexpression of all three subunits in Escherichia coli. The reconstituted complex is active in single-stranded DNA binding and the T antigen-dependent unwinding of SV40 ori DNA. Finally, we observed a cell cycle-dependent phosphorylation pattern of the p30 subunit of SpSSB, which is similar to that observed for the human and Saccharomyces cerevisiae SSB.","authors":"Ishiai M, Sanchez JP, Amin AA, Murakami Y, Hurwitz J","authors_abbrev":"Ishiai M et al.","pubmed_publication_date":"23 Aug 1996","pubmed_entrez_date":"1996-08-23","publication_year":"1996","canto_session_key":"28aaa27988f3162a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-07-31 16:15:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 16:15:22","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC23B6.05c","SPCC1753.01c","SPBC660.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-07-31"},{"uniquename":"PMID:35218318","title":"Phytase expressed from Saccharomyces pombe ameliorates footpad lesions in cage-reared broiler chicks.","citation":"Vet Med Sci 2022 Mar;8(2):654-659","abstract":"The condition of footpad is an important aspect of poultry welfare. This is a problem that plagues the poultry industry because it occurs whether birds are reared in the cage or on the floor. It is reported that feeding phytase to floor-reared broiler chicks could ameliorate footpad lesions, which is related to the reduction of litter moisture. However, some studies reported that phytase supplementation could ameliorate footpad lesions, but did not affect litter quality. Therefore, phytase supplementation may have other potential mechanisms to improve the footpad lesions. Cage-reared broiler chicks were used in this study because they had no access to litter.\nA total of 234 1-day-old broiler chicks were randomly assigned to three groups based on the initial body weight (42.22 ± 0.18 g) with six replicate cages and 13 birds (mixed sex) per cage. The experimental period was 45 days. Dietary treatments were based on a corn-soybean meal-basal diet and supplemented with 500 and 750 FTU/kg Saccharomyces pombe expressed phytase. The unit of phytase (FTU) was defined as the amount of enzyme that catalyzes the release of one micromole phosphate from phytate per minute at 37°C and pH 5.5.\nWe found that dietary supplementation of S. pombe expressed phytase could improve calcium and phosphorus digestibility and subsequent improvement in toe ash, thus ameliorating footpad lesions in broiler chicks with no access to litter.","doi":"10.1002/vms3.745","authors":"Dang X, Chun SG, Kim IH","authors_abbrev":"Dang X et al.","pubmed_publication_date":"Mar 2022","pubmed_entrez_date":"2022-02-26","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-02-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28512211","title":"Correction for Bernard et al., \"Splicing Factor Spf30 Assists Exosome-Mediated Gene Silencing in Fission Yeast\".","citation":"Mol Cell Biol 2017 Jun 01;37(11)","abstract":"","doi":"10.1128/MCB.00115-17","authors":"Bernard P, Drogat J, Dheur S, Genier S, Javerzat JP","authors_abbrev":"Bernard P et al.","pubmed_publication_date":"01 Jun 2017","pubmed_entrez_date":"2017-05-18","publication_year":"2017","canto_session_key":"82c7a0b2a9f1b6c8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-05-19 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8367300","title":"Fission yeast with DNA polymerase delta temperature-sensitive alleles exhibits cell division cycle phenotype.","citation":"Nucleic Acids Res 1993 Aug 11;21(16):3821-8","abstract":"DNA polymerases alpha and delta are essential enzymes believed to play critical roles in initiation and replication of chromosome DNA. In this study, we show that the genes for Schizosaccharomyces pombe (S.pombe) DNA polymerase alpha and delta (pol alpha+ and pol delta+) are essential for cell viability. Disruption of either the pol alpha+ or pol delta+ gene results in distinct terminal phenotypes. The S.pombe pol delta+ gene is able to complement the thermosensitive cdc2-2 allele of Saccharomyces cerevisiae (S.cerevisiae) at the restrictive temperature. By random mutagenesis in vitro, we generated three pol delta conditional lethal alleles. We replaced the wild type chromosomal copy of pol delta+ gene with the mutagenized sequence and characterized the thermosensitive alleles in vivo. All three thermosensitive mutants exhibit a typical cell division cycle (cdc) terminal phenotype similar to that of the disrupted pol delta+ gene. Flow cytometric analysis showed that at the nonpermissive temperature all three mutants were arrested in S phase of the cell cycle. The three S.pombe conditional pol delta alleles were recovered and sequenced. The mutations causing the thermosensitive phenotype are missense mutations. The altered amino acid residues are uniquely conserved among the known polymerase delta sequences.","authors":"Francesconi S, Park H, Wang TS","authors_abbrev":"Francesconi S et al.","pubmed_publication_date":"11 Aug 1993","pubmed_entrez_date":"1993-08-11","publication_year":"1993","canto_session_key":"4852bbb0f1d3de60","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 14:16:09","canto_approved_date":"2026-01-29 15:36:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-26 11:19:56","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c","SPBC336.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-17"},{"uniquename":"EMBL:AU010748","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29423847","title":"Total RNA Isolation and Quantification of Specific RNAs in Fission Yeast.","citation":"Methods Mol Biol 2018;1721:63-72","abstract":"The fission yeast, Schizosaccharomyces pombe, is an important model organism for investigations of gene regulation. Essential to such studies is the ability to quantify the levels of a specific RNA. We describe a protocol for the isolation and quantification of RNA in S. pombe using reverse-transcription followed by quantitative PCR. In this procedure, the cells are lysed using zirconia beads, then total RNA is selectively isolated away from proteins and DNA using the Trizol reagent. Contaminating DNA is then removed from the RNA by using TURBO DNase, which is easily inactivated and requires no subsequent clean-up step. The RNA is then reverse transcribed into cDNA using random nine-mers and oligo dT primers . Quantitative PCR using SYBR green is then performed to quantify RNA levels. This protocol has been tested on several S. pombe genotypes and generates highly reproducible results.","doi":"10.1007/978-1-4939-7546-4_6","authors":"Roth R, Madhani HD, Garcia JF","authors_abbrev":"Roth R et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18381891","title":"Structure-system correlation identifies a gene regulatory Mediator submodule.","citation":"Genes Dev 2008 Apr 01;22(7):872-7","abstract":"A combination of crystallography, biochemistry, and gene expression analysis identifies the coactivator subcomplex Med8C/18/20 as a functionally distinct submodule of the Mediator head module. Med8C forms a conserved alpha-helix that tethers Med18/20 to the Mediator. Deletion of Med8C in vivo results in dissociation of Med18/20 from Mediator and in loss of transcription activity of extracts. Deletion of med8C, med18, or med20 causes similar changes in the yeast transcriptome, establishing Med8C/18/20 as a predominantly positive, gene-specific submodule required for low transcription levels of nonactivated genes, including conjugation genes. The presented structure-based system perturbation is superior to gene deletion analysis of gene regulation.","doi":"10.1101/gad.465108","authors":"Larivière L, Seizl M, van Wageningen S, Röther S, van de Pasch L, Feldmann H, Strässer K, Hahn S, Holstege FC, Cramer P","authors_abbrev":"Larivière L et al.","pubmed_publication_date":"01 Apr 2008","pubmed_entrez_date":"2008-04-03","publication_year":"2008","canto_session_key":"59833033df9870b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-15 10:14:09","canto_approved_date":"2023-02-15 10:14:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-15 10:12:48","canto_added_date":"2016-09-21 00:18:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5D6.05","SPBC21.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-02-15","pdb_entries":[{"pdb_id":"3c0t","gene_chains":[{"gene_uniquename":"SPAC5D6.05","chain":"A","position":"1-207"},{"gene_uniquename":"SPBC21.04","chain":"B","position":"180-200"}],"title":"Structure of the Schizosaccharomyces pombe Mediator subcomplex Med8C/18","entry_authors":"Lariviere L,Seizl M,van Wageningen S,Roether S,van de Pasch L,Feldmann H,Straesser K,Hahn S,Holstege CP,Cramer P","entry_authors_abbrev":"Lariviere L et al.","reference_uniquename":"PMID:18381891","experimental_method":"X-ray","resolution":"2.4"}]},{"uniquename":"PMID:12702279","title":"An overview on glutathione in Saccharomyces versus non-conventional yeasts.","citation":"FEMS Yeast Res 2002 Aug;2(3):295-305","abstract":"Glutathione (GSH: L-gamma-glutamyl-L-cysteinylglycine) is present in high concentrations up to 10 mM in yeast cells. Its very low redox potential (E'(o)=-240 mV for thiol disulfide exchange) gives this tripeptide the properties of a cellular redox buffer. In Saccharomyces cerevisiae and non-conventional yeasts (NCY), GSH may be involved in basic cellular functions such as the maintenance of mitochondrial and membrane integrity. GSH also assumes pivotal roles in (i) response to sulfur and nitrogen starvation; (ii) detoxification of endogenous toxic metabolites, such as excess formaldehyde produced during the growth of the methylotrophic yeasts Hansenula polymorpha, Candida boidinii and Kloeckera sp.; (iii) protection against oxidative stress provoked by exposure of the cells to reactive oxygen species including peroxides and hydroperoxides; (iv) detoxification of xenobiotics such as halogenated aromatics, alkylating agents and arsenite; (v) resistance to heavy-metal stress exemplified by the responses of S. cerevisiae and Schizosaccharomyces pombe to cadmium salts; (vi) yeast<-->mycelium transition in Candida and Aureobasidium sp.","authors":"Penninckx MJ","authors_abbrev":"Penninckx MJ","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2003-04-19","publication_year":"2002","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16400613","title":"A mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency.","citation":"Am J Hum Genet 2006 Feb;78(2):345-9","abstract":"Ubiquinone (coenzyme Q(10) or CoQ(10)) is a lipid-soluble component of virtually all cell membranes, where it functions as a mobile electron and proton carrier. CoQ(10) deficiency is inherited as an autosomal recessive trait and has been associated with three main clinical phenotypes: a predominantly myopathic form with central nervous system involvement, an infantile encephalomyopathy with renal dysfunction, and an ataxic form with cerebellar atrophy. In two siblings of consanguineous parents with the infantile form of CoQ(10) deficiency, we identified a homozygous missense mutation in the COQ2 gene, which encodes para-hydroxybenzoate-polyprenyl transferase. The A-->G transition at nucleotide 890 changes a highly conserved tyrosine to cysteine at amino acid 297 within a predicted transmembrane domain. Radioisotope assays confirmed a severe defect of CoQ(10) biosynthesis in the fibroblasts of one patient. This mutation in COQ2 is the first molecular cause of primary CoQ(10) deficiency.","authors":"Quinzii C, Naini A, Salviati L, Trevisson E, Navas P, Dimauro S, Hirano M","authors_abbrev":"Quinzii C et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-01-10","publication_year":"2006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC56F8.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:36732376","title":"Molecular evolutionary insight of structural zinc atom in yeast xylitol dehydrogenases and its application in bioethanol production by lignocellulosic biomass.","citation":"Sci Rep 2023 Feb 02;13(1):1920","abstract":"Xylitol dehydrogenase (XDH) catalyzes the NAD + -dependent oxidization of xylitol into D-xylulose, and belongs to a zinc-dependent medium-chain dehydrogenase/reductase family. This protein family consists of enzymes with one or two zinc atoms per subunit, among which catalytic zinc is necessary for the activity. Among many XDHs from yeast and fungi, XDH from Pichia stipitis is one of the key enzymes for bioethanol production by lignocellulosic biomass, and possesses only a catalytic zinc atom. Despite its importance in bioindustry, a structural data of XDH has not yet been available, and little insight into the role of a second zinc atom in this protein family is known. We herein report the crystal structure of XDH from P. stipitis using a thermostabilized mutant. In the refined structure, a second zinc atom clearly coordinated with four artificially introduced cysteine ligands. Homologous mutations in XDH from Saccharomyces cerevisiae also stabilized and enhanced activity. The substitution of each of the four cysteine ligands with an aspartate in XDH from Schizosaccharomyces pombe contributed to the significantly better maintenance of activity and thermostability than their substitution with a serine, providing a novel hypothesis for how this zinc atom was eliminated.","doi":"10.1038/s41598-023-29195-7","authors":"Yoshiwara K, Watanabe S, Watanabe Y","authors_abbrev":"Yoshiwara K et al.","pubmed_publication_date":"02 Feb 2023","pubmed_entrez_date":"2023-02-02","publication_year":"2023","canto_session_key":"748bbb19f8ada8a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-06-22 07:24:41","canto_approved_date":"2023-06-22 19:54:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-22 07:24:33","canto_added_date":"2023-02-04 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1773.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-06-22"},{"uniquename":"PMID:9563836","title":"Mutant PCNA alleles are associated with cdc phenotypes and sensitivity to DNA damage in fission yeast.","citation":"Mol Gen Genet 1998 Mar;257(5):505-18","abstract":"Twenty-eight site-directed mutations were introduced into the fission yeast gene (pcn1+) that encodes proliferating cell nuclear antigen (PCNA) and their in vivo effects analyzed in a strain with a null pcn1 background. Mutants defective in enhancing processivity of DNA polymerase delta have previously been identified. In this study, we assessed all of the mutants for their sensitivities to temperature, hydroxyurea, UV irradiation and methyl methanesulfonate (MMS), and specific mutants were also tested for sensitivity to gamma irradiation. One cold-sensitive allele, pcn1-3, was characterized in detail. This mutant had a recessive cold-sensitive cdc phenotype and showed sensitivity to hydroxyurea, UV, and gamma irradiation. At the non-permissive temperature pcn1-3 protein was able to form homotrimers in solution and showed increased stimulation of both synthetic activity and processivity of DNA polymerase delta relative to the wild-type Pcn1+ protein. Epistasis analyses indicated that pcn1-3 is defective in the repair pathway involving rad2+ but not defective in the classical nucleotide excision repair pathway involving rad13+. Furthermore, pcn1-3 is either synthetically or conditionally lethal in null checkpoint rad backgrounds and displays a mitotic catastrophe phenotype in these backgrounds. A model for how pcn1-3 defects may affect DNA repair and replication is presented.","authors":"Arroyo MP, Wang TS","authors_abbrev":"Arroyo MP et al.","pubmed_publication_date":"Mar 1998","pubmed_entrez_date":"1998-05-01","publication_year":"1998","canto_session_key":"cbcd80a7a8babbfc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-01-29 13:29:11","canto_approved_date":"2024-01-11 20:29:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-19 14:32:18","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":173,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_9563836_phaf.tsv"}],"genes":["SPCC1259.13","SPBC216.05","SPAC664.07c","SPAC1952.07","SPBC16D10.09","SPAC14C4.13","SPAC3G6.06c","SPAC9E9.08","SPBC3E7.08c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-01-29"},{"uniquename":"PMID:38940614","title":"Activities and genetic interactions of fission yeast Aps1, a Nudix-type inositol pyrophosphatase and inorganic polyphosphatase.","citation":"mBio 2024 Jun 28;:e0108424","abstract":"","doi":"10.1128/mbio.01084-24","authors":"Ghosh S, Sanchez AM, Schwer B, Prucker I, Jork N, Jessen HJ, Shuman S","authors_abbrev":"Ghosh S et al.","pubmed_publication_date":"28 Jun 2024","pubmed_entrez_date":"2024-06-28","publication_year":"2024","canto_session_key":"69599d2112745bb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2024-08-02 14:05:03","canto_approved_date":"2024-08-02 14:05:03","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-24 19:02:42","canto_added_date":"2024-06-28 23:25:05","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":49,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":36,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17A3.03c","SPBC1271.09","SPCC1672.06c","SPAC222.09","SPCC970.08","SPAC13G6.14","SPBP4G3.02"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2024-08-02"},{"uniquename":"PMID:9201719","title":"The Cdc2 protein kinase controls Cdc10/Sct1 complex formation.","citation":"Mol Biol Cell 1997 Jun;8(6):1105-15","abstract":"In the fission yeast Schizosaccharomyces pombe, the execution of Start requires the activity of the Cdc2 protein kinase and the Cdc10/Sct1 transcription complex. The loss of any of these genes leads to G1 arrest and activation of the mating pathway under appropriate conditions. We have undertaken a genetic and biochemical analysis of these genes and their protein products to elucidate the molecular mechanism that governs the regulation of Start. We demonstrate that serine-196 of Cdc10 is phosphorylated in vivo and provide evidence that suggests that phosphorylation of this residue is required for Cdc10 function. Substitution of serine-196 of Cdc10 with alanine (Cdc10 S196A) leads to inactivation of Cdc10. We show that Cdc10 S196A is incapable of associating with Sct1 to form a heteromeric complex, whereas substitution of this serine with aspartic acid (S196D) restores DNA-binding activity by allowing Cdc10 to associate with Sct1. Furthermore, we demonstrate that Cdc2 activity is required for the formation of the heteromeric Sct1/Cdc10 transcription complex and that the Cdc10 S196D mutation alleviates this requirement. We thus provide biochemical evidence to demonstrate one mechanism by which the Cdc2 protein kinase may regulate Start in the fission yeast cell cycle.","authors":"Connolly T, Caligiuri M, Beach D","authors_abbrev":"Connolly T et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15388803","title":"Identification and cloning of two putative subunits of DNA polymerase epsilon in fission yeast.","citation":"Nucleic Acids Res 2004;32(16):4945-53","abstract":"DNA polymerase epsilon (Pol epsilon) is a multi-subunit enzyme required for the initiation of chromosomal DNA replication. Here, we report the cloning of two fission yeast genes, called dpb3+ and dpb4+ that encode proteins homologous to the two smallest subunits of Pol epsilon. Although Dpb4 is not required for cell viability, Deltadpb4 mutants are synthetically lethal with mutations in four genes required for DNA replication initiation, cdc20+ (encoding DNA Pol epsilon), cut5+ (homologous to DPB11/TopBP1), sna41+ (homologous to CDC45) and cdc21+ (encoding Mcm4, a component of the pre-replicative complex). In contrast to Dpb4, Dpb3 is essential for cell cycle progression. A glutathione S-transferase pull-down assay indicates that Dpb3 physically interacts with both Dpb2 and Dpb4, suggesting that Dpb3 associates with other members of the Pol epsilon complex. Depletion of Dpb3 leads to an accumulation of cells in S phase consistent with Dpb3 having a role in DNA replication. In addition, many of the cells have a bi-nucleate or multinucleate phenotype, indicating that cell separation is also inhibited. Finally, we have examined in vivo localization of green fluorescent protein (GFP)-tagged Dpb3 and Dpb4 and found that both proteins are localized to the nucleus consistent with their proposed role in DNA replication. However, in the absence of Dpb3, GFP-Dpb4 appears to be more dispersed throughout the cell, suggesting that Dpb3 may be important in establishing or maintaining normal localization of Dpb4.","authors":"Spiga MG, D'Urso G","authors_abbrev":"Spiga MG et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-09-25","publication_year":"2004","canto_session_key":"08dc04f357b0310b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-08 15:00:22","canto_approved_date":"2022-06-14 10:35:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-28 16:25:22","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.15","SPAC17G8.03c","SPBC25H2.13c","SPCC16A11.17","SPBP8B7.14c","SPAC23C4.18c","SPAC17D4.02","SPBC3D6.09"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2019-01-08"},{"uniquename":"PMID:36617881","title":"Tandemly repeated genes promote RNAi-mediated heterochromatin formation via an antisilencing factor, Epe1, in fission yeast.","citation":"Genes Dev 2022 Nov;36(21-24):1145-1159","abstract":"In most eukaryotes, constitutive heterochromatin, defined by histone H3 lysine 9 methylation (H3K9me), is enriched on repetitive DNA, such as pericentromeric repeats and transposons. Furthermore, repetitive transgenes also induce heterochromatin formation in diverse model organisms. However, the mechanisms that promote heterochromatin formation at repetitive DNA elements are still not clear. Here, using fission yeast, we show that tandemly repeated mRNA genes promote RNA interference (RNAi)-mediated heterochromatin formation in cooperation with an antisilencing factor, Epe1. Although the presence of tandemly repeated genes itself does not cause heterochromatin formation, once complementary small RNAs are artificially supplied in  trans , the RNAi machinery assembled on the repeated genes starts producing cognate small RNAs in  cis  to autonomously maintain heterochromatin at these sites. This \"repeat-induced RNAi\" depends on the copy number of repeated genes and Epe1, which is known to remove H3K9me and derepress the transcription of genes underlying heterochromatin. Analogous to repeated genes, the DNA sequence underlying constitutive heterochromatin encodes widespread transcription start sites (TSSs), from which Epe1 activates ncRNA transcription to promote RNAi-mediated heterochromatin formation. Our results suggest that when repetitive transcription units underlie heterochromatin, Epe1 generates sufficient transcripts for the activation of RNAi without disruption of heterochromatin.","doi":"10.1101/gad.350129.122","authors":"Asanuma T, Inagaki S, Kakutani T, Aburatani H, Murakami Y","authors_abbrev":"Asanuma T et al.","pubmed_publication_date":"Nov 2022","pubmed_entrez_date":"2023-01-09","publication_year":"2022","canto_session_key":"4e65ebe2b1bbb71f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yota Murakami","canto_first_approved_date":"2023-03-14 13:29:03","canto_approved_date":"2024-04-05 14:18:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-11 18:02:02","canto_added_date":"2023-01-10 01:15:05","annotation_curators":[{"name":"Yota Murakami","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.11","SPAC18G6.02c","SPAC6F12.09","SPCC622.16c","SPBC428.08c","SPCC11E10.08"],"gene_count":6,"ltp_gene_count":1,"approved_date":"2023-03-14"},{"uniquename":"PMID:36830739","title":"Exploring Genetic Interactions with Telomere Protection Gene  pot1  in Fission Yeast.","citation":"Biomolecules 2023 Feb 15;13(2)","abstract":"The regulation of telomere length has a significant impact on cancer risk and aging in humans. Circular chromosomes are found in humans and are often unstable during mitosis, resulting in genome instability. Some types of cancer have a high frequency of a circular chromosome. Fission yeast is a good model for studying the formation and stability of circular chromosomes as deletion of  pot1  (encoding a telomere protection protein) results in rapid telomere degradation and chromosome fusion. Pot1 binds to single-stranded telomere DNA and is conserved from fission yeast to humans. Loss of  pot1  leads to viable strains in which all three fission yeast chromosomes become circular. In this review, I will introduce  pot1  genetic interactions as these inform on processes such as the degradation of uncapped telomeres, chromosome fusion, and maintenance of circular chromosomes. Therefore, exploring genes that genetically interact with  pot1  contributes to finding new genes and/or new functions of genes related to the maintenance of telomeres and/or circular chromosomes.","doi":"10.3390/biom13020370","authors":"Ueno M","authors_abbrev":"Ueno M","pubmed_publication_date":"15 Feb 2023","pubmed_entrez_date":"2023-02-25","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-02-26 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5804681","title":"The nature of spontaneous mutations during vegetative growth in Schizosaccharomyc pombe.","citation":"Mol Gen Genet 1969;104(1):40-50","abstract":"","authors":"Loprieno N, Bonatti S, Abbondandolo A, Guglielminetti R","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"1969","pubmed_entrez_date":"1969-01-01","publication_year":"1969","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34155201","title":"Composition and stage dynamics of mitochondrial complexes in Plasmodium falciparum.","citation":"Nat Commun 2021 Jun 21;12(1):3820","abstract":"Our current understanding of mitochondrial functioning is largely restricted to traditional model organisms, which only represent a fraction of eukaryotic diversity. The unusual mitochondrion of malaria parasites is a validated drug target but remains poorly understood. Here, we apply complexome profiling to map the inventory of protein complexes across the pathogenic asexual blood stages and the transmissible gametocyte stages of Plasmodium falciparum. We identify remarkably divergent composition and clade-specific additions of all respiratory chain complexes. Furthermore, we show that respiratory chain complex components and linked metabolic pathways are up to 40-fold more prevalent in gametocytes, while glycolytic enzymes are substantially reduced. Underlining this functional switch, we find that cristae are exclusively present in gametocytes. Leveraging these divergent properties and stage dynamics for drug development presents an attractive opportunity to discover novel classes of antimalarials and increase our repertoire of gametocytocidal drugs.","doi":"10.1038/s41467-021-23919-x","authors":"Evers F, Cabrera-Orefice A, Elurbe DM, Kea-Te Lindert M, Boltryk SD, Voss TS, Huynen MA, Brandt U, Kooij TWA","authors_abbrev":"Evers F et al.","pubmed_publication_date":"21 Jun 2021","pubmed_entrez_date":"2021-06-22","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:2285","SPCC1259.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19815668","title":"A simple method for directional transcriptome sequencing using Illumina technology.","citation":"Nucleic Acids Res 2009 Dec;37(22):e148","abstract":"High-throughput sequencing of cDNA has been used to study eukaryotic transcription on a genome-wide scale to single base pair resolution. In order to compensate for the high ribonuclease activity in bacterial cells, we have devised an equivalent technique optimized for studying complete prokaryotic transcriptomes that minimizes the manipulation of the RNA sample. This new approach uses Illumina technology to sequence single-stranded (ss) cDNA, generating information on both the direction and level of transcription throughout the genome. The protocol, and associated data analysis programs, are freely available from http://www.sanger.ac.uk/Projects/Pathogens/Transcriptome/. We have successfully applied this method to the bacterial pathogens Salmonella bongori and Streptococcus pneumoniae and the yeast Schizosaccharomyces pombe. This method enables experimental validation of genetic features predicted in silico and allows the easy identification of novel transcripts throughout the genome. We also show that there is a high correlation between the level of gene expression calculated from ss-cDNA and double-stranded-cDNA sequencing, indicting that ss-cDNA sequencing is both robust and appropriate for use in quantitative studies of transcription. Hence, this simple method should prove a useful tool in aiding genome annotation and gene expression studies in both prokaryotes and eukaryotes.","doi":"10.1093/nar/gkp811","authors":"Croucher NJ, Fookes MC, Perkins TT, Turner DJ, Marguerat SB, Keane T, Quail MA, He M, Assefa S, Bähler J, Kingsley RA, Parkhill J, Bentley SD, Dougan G, Thomson NR","authors_abbrev":"Croucher NJ et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-10-10","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8791678","title":"Cell cycle control in fission yeast and mammals: identification of new regulatory mechanisms.","citation":"Adv Cancer Res 1996;69:17-62","abstract":"","authors":"Okayama H, Nagata A, Jinno S, Murakami H, Tanaka K, Nakashima N","authors_abbrev":"Okayama H et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084864","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.52"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7859738","title":"Counteractive roles of protein phosphatase 2C (PP2C) and a MAP kinase kinase homolog in the osmoregulation of fission yeast.","citation":"EMBO J 1995 Feb 01;14(3):492-502","abstract":"With the goal of discovering the cellular functions of type 2C protein phosphatases, we have cloned and analyzed two ptc (phosphatase two C) genes, ptc2+ and ptc3+, from the fission yeast Schizosaccharomyces pombe. Together with the previously identified ptc1+ gene, the enzymes encoded by these genes account for approximately 90% of the measurable PP2C activity in fission yeast cells. No obvious growth defects result from individual disruptions of ptc genes, but a delta ptc1 delta ptc3 double mutant displays aberrant cell morphology and temperature-sensitive cell lysis that is further accentuated in a delta ptc1 delta ptc2 delta ptc3 triple mutant. These phenotypes are almost completely suppressed by the presence of osmotic stabilizers, strongly indicating that PP2C has an important role in osmoregulation. Genetic suppression of delta ptc1 delta ptc3 lethality identified two loci, mutations of which render cells hypersensitive to high-osmolarity media. One locus is identical to wis1+, encoding a MAP kinase kinase (MEK) homolog. The Wis1 sequence is most closely related to the Saccharomyces cerevisiae MEK encoded by PBS2, which is required for osmoregulation. These data indicate that divergent yeasts have functionally conserved MAP kinase pathways, which are required to increase intracellular osmotic concentrations in response to osmotic stress. Moreover, our observations implicate PP2C enzymes as also having an important role in signal transduction processes involved in osmoregulation, probably acting to negatively regulate the osmosensing signal that is transmitted through Wis1 MAP kinase kinase.","authors":"Shiozaki K, Russell P","authors_abbrev":"Shiozaki K et al.","pubmed_publication_date":"01 Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_session_key":"425e79613088cd53","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-26 10:52:40","canto_approved_date":"2023-05-03 16:24:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-21 16:22:08","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.07c","SPCC4F11.02","SPCC1223.11","SPBC409.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-07-26"},{"uniquename":"PMID:7651433","title":"Replication of centromere II of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1995 Sep;15(9):5165-72","abstract":"The centromeric DNAs of Schizosaccharomyces pombe chromosomes resemble those of higher eukaryotes in being large and composed predominantly of repeated sequences. To begin a detailed analysis of the mode of replication of a complex centromere, we examined whether any sequences within S. pombe centromere II (cen2) have the ability to mediate autonomous replication. We found a high density of segments with such activity, including at least eight different regions comprising most of the repeated and unique centromeric DNA elements. A physical mapping analysis using two-dimensional gels showed that autonomous replication initiated within the S. pombe sequences in each plasmid. A two-dimensional gel analysis of replication on the chromosomes revealed that the K and L repeat elements, which occur in multiple copies at all three centromeres and comprise approximately 70% of total centromeric DNA mass in S. pombe, are both sites of replication initiation. In contrast, the unique cen2 central core, which contains multiple segments that can support autonomous replication, appears to be repressed for initiation on the chromosome. We discuss the implications of these findings for our understanding of DNA replication and centromere function.","authors":"Smith JG, Caddle MS, Bulboaca GH, Wohlgemuth JG, Baum M, Clarke L, Calos MP","authors_abbrev":"Smith JG et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33103994","title":"A novel checkpoint pathway controls actomyosin ring constriction trigger in fission yeast.","citation":"Elife 2020 Oct 26;9","abstract":"In fission yeast, the septation initiation network (SIN) ensures temporal coordination between actomyosin ring (CAR) constriction with membrane ingression and septum synthesis. However, questions remain about CAR regulation under stress conditions. We show that Rgf1p (Rho1p GEF), participates in a delay of cytokinesis under cell wall stress (blankophor, BP). BP did not interfere with CAR assembly or the rate of CAR constriction, but did delay the onset of constriction in the wild type cells but not in the  rgf1 Δ cells. This delay was also abolished in the absence of Pmk1p, the MAPK of the cell integrity pathway (CIP), leading to premature abscission and a multi-septated phenotype. Moreover, cytokinesis delay correlates with maintained SIN signaling and depends on the SIN to be achieved. Thus, we propose that the CIP participates in a checkpoint, capable of triggering a CAR constriction delay through the SIN pathway to ensure that cytokinesis terminates successfully.","doi":"10.7554/eLife.59333","authors":"Edreira T, Celador R, Manjón E, Sánchez Y","authors_abbrev":"Edreira T et al.","pubmed_publication_date":"26 Oct 2020","pubmed_entrez_date":"2020-10-26","publication_year":"2020","canto_session_key":"d38e3ba32b1cfba3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-10-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36980258","title":"Actin-Microtubule Crosstalk Imparts Stiffness to the Contractile Ring in Fission Yeast.","citation":"Cells 2023 Mar 16;12(6)","abstract":"Actin-microtubule interactions are critical for cell division, yet how these networks of polymers mutually influence their mechanical properties and functions in live cells remains unknown. In fission yeast, the post-anaphase array (PAA) of microtubules assembles in the plane of the contractile ring, and its assembly relies on the Myp2p-dependent recruitment of Mto1p, a component of equatorial microtubule organizing centers (eMTOCs). The general organization of this array of microtubules and the impact on their physical attachment to the contractile ring remain unclear. We found that Myp2p facilitates the recruitment of Mto1p to the inner face of the contractile ring, where the eMTOCs polymerize microtubules without their direct interaction. The PAA microtubules form a dynamic polygon of Ase1p crosslinked microtubules inside the contractile ring. The specific loss of PAA microtubules affects the mechanical properties of the contractile ring of actin by lowering its stiffness. This change in the mechanical properties of the ring has no measurable impact on cytokinesis or on the anchoring of the ring. Our work proposes that the PAA microtubules exploit the contractile ring for their assembly and function during cell division, while the contractile ring may receive no benefit from these interactions.","doi":"10.3390/cells12060917","authors":"Bellingham-Johnstun K, Tyree ZL, Martinez-Baird J, Thorn A, Laplante C","authors_abbrev":"Bellingham-Johnstun K et al.","pubmed_publication_date":"16 Mar 2023","pubmed_entrez_date":"2023-03-29","publication_year":"2023","canto_session_key":"7a2d3b5bc9c7749b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kimberly Bellingham-Johnstun","canto_first_approved_date":"2023-07-03 08:42:46","canto_approved_date":"2023-07-03 08:42:46","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-06-28 05:05:38","canto_added_date":"2023-03-30 00:15:06","annotation_curators":[{"name":"Kimberly Bellingham-Johnstun","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":12,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPAC18G6.15","SPAC4A8.05c","SPCC417.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2023-07-03"},{"uniquename":"PMID:31833215","title":"Maf1-dependent transcriptional regulation of tRNAs prevents genomic instability and is associated with extended lifespan.","citation":"Aging Cell 2020 Feb;19(2):e13068","abstract":"Maf1 is the master repressor of RNA polymerase III responsible for transcription of tRNAs and 5S rRNAs. Maf1 is negatively regulated via phosphorylation by the mTOR pathway, which governs protein synthesis, growth control, and lifespan regulation in response to nutrient availability. Inhibiting the mTOR pathway extends lifespan in various organisms. However, the downstream effectors for the regulation of cell homeostasis that are critical to lifespan extension remain elusive. Here we show that fission yeast Maf1 is required for lifespan extension. Maf1's function in tRNA repression is inhibited by mTOR-dependent phosphorylation, whereas Maf1 is activated via dephosphorylation by protein phosphatase complexes, PP4 and PP2A. Mutational analysis reveals that Maf1 phosphorylation status influences lifespan, which is correlated with elevated tRNA and protein synthesis levels in maf1∆ cells. However, mTOR downregulation, which negates protein synthesis, fails to rescue the short lifespan of maf1∆ cells, suggesting that elevated protein synthesis is not a cause of lifespan shortening in maf1∆ cells. Interestingly, maf1∆ cells accumulate DNA damage represented by formation of Rad52 DNA damage foci and Rad52 recruitment at tRNA genes. Loss of the Rad52 DNA repair protein further exacerbates the shortened lifespan of maf1∆ cells. Strikingly, PP4 deletion alleviates DNA damage and rescues the short lifespan of maf1∆ cells even though tRNA synthesis is increased in this condition, suggesting that elevated DNA damage is the major cause of lifespan shortening in maf1∆ cells. We propose that Maf1-dependent inhibition of tRNA synthesis controls fission yeast lifespan by preventing genomic instability that arises at tRNA genes.","doi":"10.1111/acel.13068","authors":"Shetty M, Noguchi C, Wilson S, Martinez E, Shiozaki K, Sell C, Mell JC, Noguchi E","authors_abbrev":"Shetty M et al.","pubmed_publication_date":"Feb 2020","pubmed_entrez_date":"2019-12-14","publication_year":"2020","canto_session_key":"0e416dbb3b3521ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Eishi Noguchi","canto_first_approved_date":"2020-04-20 11:03:14","canto_approved_date":"2025-05-27 14:16:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-11 08:49:29","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Eishi Noguchi","community_curator":true,"annotation_count":30,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":33,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPAC823.15","SPCC4G3.08","SPBC26H8.05c","SPBC16H5.07c","SPAC31G5.12c","SPBC216.07c","SPBC336.07"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2020-04-20"},{"uniquename":"PMID:9790976","title":"Identification of a fission yeast dynamin-related protein involved in mitochondrial DNA maintenance.","citation":"Biochem Biophys Res Commun 1998 Oct 29;251(3):720-6","abstract":"Members of the dynamin-related proteins family have been identified in a wide range of organisms, however their precise functions remain elusive. We have identified a new member of that GTPase family in the fission yeast Schizosaccharomyces pombe. We show that Msp1+ is an essential nuclear gene encoding a 101 kDa protein whose closest homologue is the S. cerevisiae MGM1 gene product. We also report that msp1 conditional loss of function affects the maintenance of mitochondrial DNA and leads to growth arrest associated with respiratory deficiency.","authors":"Pelloquin L, Belenguer P, Menon Y, Ducommun B","authors_abbrev":"Pelloquin L et al.","pubmed_publication_date":"29 Oct 1998","pubmed_entrez_date":"1998-10-29","publication_year":"1998","canto_session_key":"2faa6d6c19bb1b1a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-11-03 12:54:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-27 11:23:45","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-27"},{"uniquename":"PMID:31341193","title":"Ent3 and GGA adaptors facilitate diverse anterograde and retrograde trafficking events to and from the prevacuolar endosome.","citation":"Sci Rep 2019 Jul 24;9(1):10747","abstract":"Carboxypeptidases Y (Cpy1) and S (Cps1), the receptor Vps10, and the ATPase subunit Vph1 follow the carboxypeptidase Y (CPY) pathway from the trans-Golgi network (TGN) to the prevacuolar endosome (PVE). Using Schizosaccharomyces pombe quantitative live-cell imaging, biochemical and genetic analyses, we extended the previous knowledge and showed that collaboration between Gga22, the dominant Golgi-localized Gamma-ear-containing ARF-binding (GGA) protein, and Gga21, and between Gga22 and the endosomal epsin Ent3, was required for efficient: i) Vps10 anterograde trafficking from the TGN to the PVE; ii) Vps10 retrograde trafficking from the PVE to the TGN; iii) Cps1 exit from the TGN, and its sorting in the PVE en route to the vacuole; and iv) Syb1/Snc1 recycling to the plasma membrane through the PVE. Therefore, monomeric clathrin adaptors facilitated the trafficking of Vps10 in both directions of the CPY pathway, and facilitated trafficking events of Cps1 in different organelles. By contrast, they were dispensable for Vph1 trafficking. Thus, these adaptors regulated the traffic of some, but not all, of the cargo of the CPY pathway, and regulated the traffic of cargoes that do not follow this pathway. Additionally, this collaboration was required for PVE organization and efficient growth under stress.","doi":"10.1038/s41598-019-47035-5","authors":"Yanguas F, Moscoso-Romero E, Valdivieso MH","authors_abbrev":"Yanguas F et al.","pubmed_publication_date":"24 Jul 2019","pubmed_entrez_date":"2019-07-26","publication_year":"2019","canto_session_key":"b6f52423002339f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Henar Valdivieso","canto_first_approved_date":"2019-08-15 14:56:26","canto_approved_date":"2025-09-03 12:24:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-02 10:54:19","canto_added_date":"2019-07-27 00:15:03","annotation_curators":[{"name":"Henar Valdivieso","community_curator":true,"annotation_count":52,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC9B6.08","SPBC25H2.16c","SPAC6G9.11","SPBC16C6.06","SPAC16E8.07c","SPAC1F3.05","SPBP16F5.07","SPAC19A8.05c","SPCC794.11c","SPBC31E1.04","SPCC777.13","SPAC19G12.10c","SPAC4A8.04","SPAC24C9.08"],"gene_count":14,"ltp_gene_count":8,"approved_date":"2019-08-15"},{"uniquename":"EMBL:AU010789","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27854023","title":"Chromatin Immunoprecipitation of Histone Modifications in Fission Yeast.","citation":"Methods Mol Biol 2017;1528:199-210","abstract":"Chromatin immunoprecipitation (ChIP) is a sensitive, accurate, and reliable technique widely used to analyze protein-DNA interactions at specific binding sites in vivo. It has been a particularly powerful technique for mapping of histone modification patterns both at individual loci and genome-wide. Here we provide a detailed protocol for ChIP of histone modifications associated with active transcription in fission yeast (Schizosaccharomyces pombe).","authors":"Mbogning J, Tanny JC","authors_abbrev":"Mbogning J et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2016-11-18","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-19 01:15:23","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41032311","title":"Adaptations and maladaptations due to evolution at constant, but not at fluctuating temperatures.","citation":"J Evol Biol 2025 Oct 01;","abstract":"Climate change exposes populations to more frequent periods of extreme temperatures and faster temperature fluctuations. Theoretical models suggest that different types of adaptations should occur in constant versus fluctuating environments of varying frequency. Furthermore, it has been hypothesized that the number and severity of fitness trade-offs evolving in fluctuating environments depends on population size. To evaluate whether specific types of adaptations evolve at fluctuating temperatures and how population size might affect the evolution of trade-offs, we performed an evolution experiment with fission yeast (Schizosaccharomyces pombe). Small and large populations were evolved for 500 generations at constant and fluctuating temperatures, after which the evolved strains were competed against ancestral strains in their respective selection environments, and in alternative environments to detect fitness trade-offs. We observed significant adaptation and maladaptation only to constant heat, but not to fluctuating temperatures. Moreover, population size did not have significant effect on capacity of adaptation or trade-offs in alternative environments. Our results suggest that constant extreme temperatures may act as stronger selective pressures than temperature variations, and that fitness trade-offs are unlikely to constrain adaptation to fluctuating temperatures. Future experiments in fluctuating temperatures should consider that number of generations required for populations to adapt may be longer than for constant environments.","doi":"10.1093/jeb/voaf118","authors":"Räsänen E, Nieminen V, Summanen PAM, de la Peña MV, Makkonen P, Suisto K, Ketola T, Kronholm I","authors_abbrev":"Räsänen E et al.","pubmed_publication_date":"01 Oct 2025","pubmed_entrez_date":"2025-10-01","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-10-01 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14573463","title":"Schizosaccharomyces pombe Ras1 effector, Scd1, interacts with Klp5 and Klp6 kinesins to mediate cytokinesis.","citation":"Genetics 2003 Oct;165(2):477-88","abstract":"Fission yeast Scd1 is an exchange factor for Cdc42 and an effector of Ras1. In a screen for scd1 interacting genes, we isolated klp5 and klp6, which encode presumptive kinesins. Klp5 and Klp6 form a complex to control the same processes, which so far include microtubule dynamics and chromosome segregation. We showed that klp5 or klp6 inactivation in combination with the scd1 deletion (scd1delta) created a synthetic temperature-dependent growth defect. Further genetic analysis demonstrated that Klp5 and Klp6 interacted specifically with the Ras1-Scd1 pathway, but not with the Ras1-Byr2 pathway. In addition, Klp5 and Klp6 can stably associate with Scd1 and Cdc42. A deletion in the Scd1 C terminus, which contains the PB1 domain, prevented Scd1 binding to Klp5/6 and caused a growth defect in Klp5/6 mutant cells that is indistinguishable from that induced by scd1delta. Analysis of the double-mutant phenotype indicated that at the nonpermissive temperature, cells failed to undergo cytokinesis efficiently. These cells contained abnormal contractile rings in which F-actin and Mid1, a key regulator of F-actin ring formation and positioning, are mispositioned and fragmented. These data suggest that Klp5/6 cooperate with the Ras1-Scd1 pathway to influence proper formation of the contractile ring for cytokinesis.","authors":"Li Y, Chang EC","authors_abbrev":"Li Y et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2003-10-24","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2F12.13","SPAC16E8.09","SPBC1604.14c","SPBC1685.15c","SPAC110.03","SPAC17H9.09c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:22809626","title":"Dnt1 acts as a mitotic inhibitor of the spindle checkpoint protein dma1 in fission yeast.","citation":"Mol Biol Cell 2012 Sep;23(17):3348-56","abstract":"The Schizosaccharomyces pombe checkpoint protein Dma1 couples mitotic progression with cytokinesis and is important in delaying mitotic exit and cytokinesis when kinetochores are not properly attached to the mitotic spindle. Dma1 is a ubiquitin ligase and potential functional relative of the human tumor suppressor Chfr. Dma1 delays mitotic exit and cytokinesis by ubiquitinating a scaffold protein (Sid4) of the septation initiation network, which, in turn, antagonizes the ability of the Polo-like kinase Plo1 to promote cell division. Here we identify Dnt1 as a Dma1-binding protein. Several lines of evidence indicate that Dnt1 inhibits Dma1 function during metaphase. First, Dnt1 interacts preferentially with Dma1 during metaphase. Second, Dma1 ubiquitin ligase activity and Sid4 ubiquitination are elevated in dnt1 cells. Third, the enhanced mitotic defects in dnt1Δ plo1 double mutants are partially rescued by deletion of dma1(+), suggesting that the defects in dnt1 plo1 double mutants are attributable to excess Dma1 activity. Taken together, these data show that Dnt1 acts to restrain Dma1 activity in early mitosis to allow normal mitotic progression.","doi":"10.1091/mbc.E11-12-1020","authors":"Wang Y, Li WZ, Johnson AE, Luo ZQ, Sun XL, Feoktistova A, McDonald WH, McLeod I, Yates JR, Gould KL, McCollum D, Jin QW","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-07-20","publication_year":"2012","canto_session_key":"cf4899040d72592d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Quan-wen Jin","canto_first_approved_date":"2017-06-26 16:55:58","canto_approved_date":"2025-04-13 08:11:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-11 04:59:14","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Quan-wen Jin","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPAC343.03","SPBC244.01c","SPAC17G8.10c","SPBC25D12.02c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-06-26"},{"uniquename":"PMID:24920823","title":"Cdk1 promotes cytokinesis in fission yeast through activation of the septation initiation network.","citation":"Mol Biol Cell 2014 Aug 01;25(15):2250-9","abstract":"In Schizosaccharomyces pombe, late mitotic events are coordinated with cytokinesis by the septation initiation network (SIN), an essential spindle pole body (SPB)-associated kinase cascade, which controls the formation, maintenance, and constriction of the cytokinetic ring. It is not fully understood how SIN initiation is temporally regulated, but it depends on the activation of the GTPase Spg1, which is inhibited during interphase by the essential bipartite GTPase-activating protein Byr4-Cdc16. Cells are particularly sensitive to the modulation of Byr4, which undergoes cell cycle-dependent phosphorylation presumed to regulate its function. Polo-like kinase, which promotes SIN activation, is partially responsible for Byr4 phosphorylation. Here we show that Byr4 is also controlled by cyclin-dependent kinase (Cdk1)-mediated phosphorylation. A Cdk1 nonphosphorylatable Byr4 phosphomutant displays severe cell division defects, including the formation of elongated, multinucleate cells, failure to maintain the cytokinetic ring, and compromised SPB association of the SIN kinase Cdc7. Our analyses show that Cdk1-mediated phosphoregulation of Byr4 facilitates complete removal of Byr4 from metaphase SPBs in concert with Plo1, revealing an unexpected role for Cdk1 in promoting cytokinesis through activation of the SIN pathway.","doi":"10.1091/mbc.E14-04-0936","authors":"Rachfall N, Johnson AE, Mehta S, Chen JS, Gould KL","authors_abbrev":"Rachfall N et al.","pubmed_publication_date":"01 Aug 2014","pubmed_entrez_date":"2014-06-13","publication_year":"2014","canto_session_key":"d0dd7cb7b7db147e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nicole Rachfall","canto_first_approved_date":"2017-02-24 15:39:44","canto_approved_date":"2025-09-04 06:50:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-20 15:33:47","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Nicole Rachfall","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPBC11B10.09","SPAC1565.06c","SPAC222.10c","SPBC1773.01","SPBC21.06c","SPAC6F6.08c","SPBC428.13c","SPCC1739.11c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-02-24"},{"uniquename":"PMID:24954052","title":"Formins determine the functional properties of actin filaments in yeast.","citation":"Curr Biol 2014 Jul 07;24(13):1525-30","abstract":"The actin cytoskeleton executes a broad range of essential functions within a living cell. The dynamic nature of the actin polymer is modulated to facilitate specific cellular processes at discrete locations by actin-binding proteins (ABPs), including the formins and tropomyosins (Tms). Formins nucleate actin polymers, while Tms are conserved dimeric proteins that form polymers along the length of actin filaments. Cells possess different Tm isoforms, each capable of differentially regulating the dynamic and functional properties of the actin polymer. However, the mechanism by which a particular Tm localizes to a specific actin polymer is unknown. Here we show that specific formin family members dictate which Tm isoform will associate with a particular actin filament to modulate its dynamic and functional properties at specific cellular locations. Exchanging the localization of the fission yeast formins For3 and Cdc12 results in an exchange in localizations of Tm forms on actin polymers. This nucleator-driven switch in filament composition is reflected in a switch in actin dynamics, together with a corresponding change in the filament's ability to regulate ABPs and myosin motor activity. These data establish a role for formins in dictating which specific Tm variant will associate with a growing actin filament and therefore specify the functional capacity of the actin filaments that they create.","doi":"10.1016/j.cub.2014.05.034","authors":"Johnson M, East DA, Mulvihill DP","authors_abbrev":"Johnson M et al.","pubmed_publication_date":"07 Jul 2014","pubmed_entrez_date":"2014-06-24","publication_year":"2014","canto_session_key":"34d3b03da3308cde","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dan Mulvihill","canto_first_approved_date":"2018-01-30 20:21:47","canto_approved_date":"2025-12-13 03:43:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-02 16:09:36","canto_added_date":"2014-06-25 00:15:30","annotation_curators":[{"name":"Dan Mulvihill","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.06c","SPCC645.05c","SPAC4F8.13c","SPAC1F5.04c","SPCC1919.10c","SPAC27F1.02c","SPCC895.05"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2018-01-30"},{"uniquename":"PMID:6490749","title":"Septum pattern in ts mutants of Schizosaccharomyces pombe defective in genes cdc3, cdc4, cdc8 and cdc12.","citation":"J Cell Sci 1984 Jul;69:47-65","abstract":"Septum-defective mutants of Schizosaccharomyces pombe impaired in cdc genes 3, 4, 8 and 12 were compared by fluorescence microscopy, freeze-etching and ultrathin sectioning. This approach made it possible to recognize the internal organization of defective phenotypes under restrictive conditions. Of special interest in this study was the pattern of unusual septum malformations found to be regular features of the terminal phenotypes of the mutants. Their overall topology was visualized at the cellular level by primulin fluorescence. The subcellular location of septum defects was found to be identical in origin to the compartment where normal septum was assembled in the wild type. Delocalized septation involved both microfibrillar and matrix components, which participated in the final assembly of malformations. Unique contour views of delocalized septa were exposed by freeze-fracturing. Cytoplasmic microtubules and microfilaments were detected in ultrathin sections of the cytoplasm of mutant cells. The internal organization of malformation-accumulating phenotypes suggested a disruption of the directional mechanism that steers septum material to the periplasm at the cell equator.","authors":"Streiblová E, Hasek J, Jelke E","authors_abbrev":"Streiblová E et al.","pubmed_publication_date":"Jul 1984","pubmed_entrez_date":"1984-07-01","publication_year":"1984","canto_session_key":"4a8e1e2dd8c6d041","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-09-16 13:21:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-04-18 09:11:38","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21B10.05c","SPAC1F5.04c","SPAC4A8.15c","SPAC27F1.02c","SPAP8A3.08"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2013-04-18"},{"uniquename":"PMID:40434897","title":"Amino acid-level differences in alpha tubulin sequences are uniquely required for meiosis.","citation":"Mol Biol Cell 2025 May 28;:mbcE24110529","abstract":"Members of the tubulin gene family members are essential components of the cytoskeleton, however functional diversity of tubulin isoforms is poorly understood. Here we addressed this question using  Schizosaccharomyces pombe  as a model system. These yeast encode two α- tubulins,  nda2  and  atb2 , that are very similar at the amino acid level but differ in their roles in organism's survival:  nda2  deletion is lethal, while lack of  atb2  does not interfere with cell viability. Using CRISPR-Cas9 gene editing, we generated a yeast strain expressing  atb2  amino acid sequence utilizing  nda2  codon usage in the native  nda2  locus. Such  nda2 -coded  atb2  (NCA) yeast, unlike  nda2  knockout, were viable and displayed no visible abnormalities in vegetative life cycle. Instead, they displayed strong impairments in sporulation and meiosis, linked to altered balance of several spindle proteins. Our data indicate that  nda2  protein is uniquely required for normal meiosis, and identify novel protein- and nucleotide-level determinants driving functional distinction between closely related tubulin isoforms.","doi":"10.1091/mbc.E24-11-0529","authors":"Chen L, Chen X, Kashina A","authors_abbrev":"Chen L et al.","pubmed_publication_date":"28 May 2025","pubmed_entrez_date":"2025-05-28","publication_year":"2025","canto_session_key":"8c6b80f849bdfaa4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-05-28 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16544289","title":"The more the merrier: comparative analysis of microarray studies on cell cycle-regulated genes in fission yeast.","citation":"Yeast 2006 Mar;23(4):261-277","abstract":"The last two years have seen the publication of three genome-wide gene expression studies of the fission yeast cell cycle. While these microarray papers largely agree on the main patterns of cell cycle-regulated transcription and its control, there are discrepancies with regard to the identity and numbers of periodically expressed genes. We present benchmark and reproducibility analyses showing that the main discrepancies do not reflect differences in the data themselves (microarray or synchronization methods seem to lead only to minor biases) but rather in the interpretation of the data. Our reanalysis of the three datasets reveals that combining all independent information leads to an improved identification of periodically expressed genes. These evaluations suggest that the available microarray data do not allow reliable identification of more than about 500 cell cycle-regulated genes. The temporal expression pattern of the top 500 periodically expressed genes is generally consistent across experiments and the three studies, together with our integrated analysis, provide a coherent and rich source of information on cell cycle-regulated gene expression in Schizosaccharomyces pombe. The reanalysed datasets and other supplementary information are available from an accompanying website: http://www.cbs.dtu.dk/cellcycle/. We hope that this paper will resolve the apparent discrepancies between the previous studies and be useful both for wet-lab biologists and for theoretical scientists who wish to take advantage of the data for follow-up work.","doi":"10.1002/yea.1351","authors":"Marguerat S, Jensen TS, de Lichtenberg U, Wilhelm BT, Jensen LJ, Bähler J","authors_abbrev":"Marguerat S et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-03-18","publication_year":"2006","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37453417","title":"Structure of the Schizosaccharomyces pombe Gtr-Lam complex reveals evolutionary divergence of mTORC1-dependent amino acid sensing.","citation":"Structure 2023 Sep 07;31(9):1065-1076.e5","abstract":"mTORC1 is a protein kinase complex that controls cellular growth in response to nutrient availability. Amino acid signals are transmitted toward mTORC1 via the Rag/Gtr GTPases and their upstream regulators. An important regulator is LAMTOR, which localizes Rag/Gtr on the lysosomal/vacuole membrane. In human cells, LAMTOR consists of five subunits, but in yeast, only three or four. Currently, it is not known how variation of the subunit stoichiometry may affect its structural organization and biochemical properties. Here, we report a 3.1 Å-resolution structural model of the Gtr-Lam complex in Schizosaccharomyces pombe. We found that SpGtr shares conserved architecture as HsRag, but the intersubunit communication that coordinates nucleotide loading on the two subunits differs. In contrast, SpLam contains distinctive structural features, but its GTP-specific GEF activity toward SpGtr is evolutionarily conserved. Our results revealed unique evolutionary paths of the protein components of the mTORC1 pathway.","doi":"10.1016/j.str.2023.06.012","authors":"Tettoni SD, Egri SB, Doxsey DD, Veinotte K, Ouch C, Chang JY, Song K, Xu C, Shen K","authors_abbrev":"Tettoni SD et al.","pubmed_publication_date":"07 Sep 2023","pubmed_entrez_date":"2023-07-15","publication_year":"2023","canto_session_key":"c36c09a4561df48f","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-07-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27697163","title":"Cell wall polysaccharides released during the alcoholic fermentation by Schizosaccharomyces pombe and S. japonicus: quantification and characterization.","citation":"Food Microbiol 2017 Feb;61:136-149","abstract":"The present work demonstrates that yeasts belonging to the Schizosaccharomyces genus release a high quantity of polysaccharides of cell wall origin starting from the onset of the alcoholic fermentation. By the end of the alcoholic fermentation, all of the Schizosaccharomyces yeast strains released a quantity of polysaccharides approximately 3-7 times higher than that released by a commercial Saccharomyces cerevisiae yeast strain under the same fermentative conditions of synthetic juice. A higher content of polysaccharide was found in media fermented by Schizosaccharomyces japonicus with respect to that of Schizosaccharomyces pombe. Some of the strains evaluated were also able to produce high levels of pyruvic acid, which has been shown to be an important compound for color stability of wine. The presence of strains with different malic acid consumption patterns along with high polysaccharide release would enable production of naturally modified wines with enhanced mouth feel and reduced acidity. The chemical analysis of the released polysaccharides demonstrated divergence between the two yeast species S. pombe and S. japonicus. A different mannose/galactose ratio and a different percentage of proteins was observed on the polysaccharides released by S. pombe as compared to S. japonicus. Analysis of the proteins released in the media revealed the presence of a glycoprotein with a molecular size around 32-33 kDa only for the species S. japonicus. Mass spectrometry analysis of carbohydrate moieties showed similar proportions among the N-glycan chains released in the media by both yeast species but differences between the two species were also observed. These observations suggest a possible role of rapid MALDI-TOF screening of N-glycans compositional fingerprint as a taxonomic tool for this genus. Polysaccharides release in the media, in particular galactomannoproteins in significant amounts, could make these yeasts particularly interesting also for the industrial production of exogenous polysaccharide preparations.","doi":"10.1016/j.fm.2016.08.010","authors":"Domizio P, Liu Y, Bisson LF, Barile D","authors_abbrev":"Domizio P et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-10-05","publication_year":"2017","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-10-07 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR23106","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:24684","SPCC1442.13c","HGNC:11183","SPBC30B4.02c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:10651900","title":"Cell cycle mechanisms of sister chromatid separation; roles of Cut1/separin and Cut2/securin.","citation":"Genes Cells 2000 Jan;5(1):1-8","abstract":"The correct transmission of chromosomes from mother to daughter cells is fundamental for genetic inheritance. Separation and segregation of sister chromatids in growing cells occurs in the cell cycle stage called 'anaphase'. The basic process of sister chromatid separation is similar in all eukaryotes: many gene products required are conserved. In this review, the roles of two proteins essential for the onset of anaphase in fission yeast, Cut2/securin and Cut1/separin, are discussed with regard to cell cycle regulation, and compared with the postulated roles of homologous proteins in other organisms. Securin, like mitotic cyclins, is the target of the anaphase promoting complex (APC)/cyclosome and is polyubiquitinated before destruction in a manner dependent upon the destruction sequence. The anaphase never occurs properly in the absence of securin destruction. In human cells, securin is an oncogene. Separin is a large protein (MW approximately 180 kDa), the C-terminus of which is conserved, and is thought to be inhibited by association with securin at the nonconserved N-terminus. In the budding yeast, Esp1/separin is thought to be a component of proteolysis against Scc1, an essential subunit of cohesin which is thought to link duplicated sister chromatids up to the anaphase. Whether fission yeast Cut1/separin is also implicated in proteolysis of cohesin is discussed.","authors":"Yanagida M","authors_abbrev":"Yanagida M","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-29","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14C8.01c","SPAC343.03","SPCC5E4.04"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:8203144","title":"Inhibition of protein synthesis disrupts the Golgi apparatus in the fission yeast, Schizosaccharomyces pombe.","citation":"Yeast 1994 Jan;10(1):1-11","abstract":"Schizosaccharomyces pombe was treated with either cycloheximide or anisomycin at levels sufficient to inhibit > 95% of protein synthesis for periods upon to 3 h, equivalent to one cell cycle. Treatment for as little as 1 h caused significant loss of the Golgi apparatus by both immunofluorescence and electron microscopy. The loss was quantitated by stereology on electron micrographs. Nearly 90% of the stacked Golgi was lost over a 3 h period. No other intracellular membrane compartment seemed to be affected. Measurement of enzyme activities confirmed these observations. The activity of a resident of the Golgi apparatus, alpha-1,2 galactosyltransferase, was reduced over this time, whereas the endoplasmic reticulum marker, BiP, and the cytoplasmic enzyme, hexokinase, were unaffected. The morphological changes associated with cycloheximide addition were reversed on its removal, though there was a lag before cells recommenced growth or secretion of the enzyme, acid phosphatase.","authors":"Ayscough K, Warren G","authors_abbrev":"Ayscough K et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28846478","title":"New roles for Dicer in the nucleolus and its relevance to cancer.","citation":"Cell Cycle 2017 Sep 17;16(18):1643-1653","abstract":"The nucleolus is a distinct compartment of the nucleus responsible for ribosome biogenesis. Mis-regulation of nucleolar functions and of the cellular translation machinery has been associated with disease, in particular with many types of cancer. Indeed, many tumor suppressors (p53, Rb, PTEN, PICT1, BRCA1) and proto-oncogenes (MYC, NPM) play a direct role in the nucleolus, and interact with the RNA polymerase I transcription machinery and the nucleolar stress response. We have identified Dicer and the RNA interference pathway as having an essential role in the nucleolus of quiescent Schizosaccharomyces pombe cells, distinct from pericentromeric silencing, by controlling RNA polymerase I release. We propose that this novel function is evolutionarily conserved and may contribute to the tumorigenic pre-disposition of DICER1 mutations in mammals.","doi":"10.1080/15384101.2017.1361568","authors":"Roche B, Arcangioli B, Martienssen R","authors_abbrev":"Roche B et al.","pubmed_publication_date":"17 Sep 2017","pubmed_entrez_date":"2017-08-29","publication_year":"2017","canto_session_key":"16df748186a7cf46","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-08-30 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28167404","title":"Comparison of extracellular Cys/Trp motif between Schizosaccharomyces pombe Ctr4 and Ctr5.","citation":"J Inorg Biochem 2017 Apr;169:97-105","abstract":"The reduction and binding of copper ions to the Cys/Trp motif, which is characterized by two cysteines and two tryptophans, in the extracellular N-terminal domain of the copper transporter (Ctr) protein of fungi are investigated using the model peptides of Ctr4 and Ctr5 from Schizosaccharomyces pombe. The Cys/Trp motif of Ctr5 can reduce Cu(II) and ligate Cu(I), which is the same as that of Ctr4 previously reported. Titration of Cu(II) and Cu(I) ions indicates that both the Cys/Trp motifs of Ctr4 and Ctr5 reduce two Cu(II) and bind two Cu(I) per one peptide. However, the coordination structure of the Cu(I)-peptide complex differs between Ctr4 and Ctr5. Cu(I) is bound to the Cys/Trp motif of Ctr5 via cysteine thiolate-Cu(I) bonds and cation-π interaction with tryptophan, as reported for Ctr4, and a histidine residue in the Cys/Trp motif of Ctr5 is suggested to interact with Cu(I) via its Nτ atom. Ctr4 and Ctr5 exhibit a heterotrimeric form within cell membranes and the copper transport mechanism of the Ctr4/Ctr5 heterotrimer is discussed along with quantitative evaluation of the Cu(I)-binding constant of the Cys/Trp motif.","doi":"10.1016/j.jinorgbio.2017.01.009","authors":"Okada M, Miura T, Nakabayashi T","authors_abbrev":"Okada M et al.","pubmed_publication_date":"Apr 2017","pubmed_entrez_date":"2017-02-08","publication_year":"2017","canto_session_key":"219a429e5ae9ff9e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-10 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11580838","title":"Failure to farnesylate Rheb protein contributes to the enrichment of G0/G1 phase cells in the Schizosaccharomyces pombe farnesyltransferase mutant.","citation":"Mol Microbiol 2001 Sep;41(6):1339-47","abstract":"Protein farnesylation is important for a number of physiological processes, including proliferation and cell morphology. The Schizosaccharomyces pombe mutant, cpp1-, defective in farnesylation, exhibits distinct phenotypes, including morphological changes and sensitivity to the arginine analogue, canavanine. In this work, we report a novel phenotype of this mutant, enrichment of G0/G1 phase cells. This phenotype results mainly from the inability to farnesylate the Rheb G-protein, as normal cell cycle progression can be restored to the mutant by expressing a mutant form of SpRheb (SpRheb-CVIL) that can bypass farnesylation. In contrast, a farnesylation-defective mutant of SpRheb (SpRheb-SVIA) is incapable of restoring the normal cell cycle profile to the cpp1- mutant. Inhibition of SpRheb expression leads to the accumulation of cells at the G0/G1 phase of the cell cycle. This growth arrest phenotype of the sprheb- disruption can be complemented by the introduction of wild-type sprheb+. The complementation is dependent on farnesylation, as the farnesylation-defective SpRheb-SVIA mutant is incapable of complementing the sprheb- disruption. Other mutants of SpRheb, E40K and S20N, are also incapable of complementing the sprheb- disruption. Furthermore, efficient complementation can be obtained by the expression of human Rheb but not Saccharomyces cerevisiae Rheb. Our findings suggest that protein farnesylation is important for cell cycle progression of S. pombe cells and that farnesylated SpRheb is critical in this process.","authors":"Yang W, Tabancay AP, Urano J, Tamanoi F","authors_abbrev":"Yang W et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-10-03","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28742002","title":"Cdc42 activation state affects its localization and protein levels in fission yeast.","citation":"Microbiology (Reading) 2017 Aug;163(8):1156-1166","abstract":"Rho GTPases control polarized cell growth and are well-known regulators of exocytic and endocytic processes. Cdc42 is an essential GTPase, conserved from yeast to humans, that is critical for cell polarization. Cdc42 is negatively regulated by the GTPase-activating proteins (GAPs) and the GDP dissociation inhibitors (GDIs), and positively regulated by guanine nucleotide exchange factors (GEFs). Cdc42 GTPase can be found in a GTP- or GDP-bound state, which determines the ability to bind downstream effector proteins and activate signalling pathways. Only GTP-bound Cdc42 is active. In this study we have analysed the localization of the different nucleotide-bound states of Cdc42 in  Schizosaccharomyces pombe : the wild-type Cdc42 protein that cycles between an active and inactive form, the Cdc42G12V form that is permanently bound to GTP and the Cdc42T17N form that is constitutively inactive. Our results indicate that Cdc42 localizes to several membrane compartments in the cell and this localization is mediated by its C-terminal prenylation. Constitutively active Cdc42 localizes mainly to the plasma membrane and concentrates at the growing tips where it is considerably less dynamic than wild-type or GDP-bound Cdc42. Additionally we show that the activation state of Cdc42 also participates in the regulation of its protein levels mediated by endocytosis and by the exocyst complex.","doi":"10.1099/mic.0.000503","authors":"Estravís M, Rincón SA, Portales E, Pérez P, Santos B","authors_abbrev":"Estravís M et al.","pubmed_publication_date":"Aug 2017","pubmed_entrez_date":"2017-07-26","publication_year":"2017","canto_session_key":"a7b4a76383a0fd29","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-07-27 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16855022","title":"Chs5/6 complex: a multiprotein complex that interacts with and conveys chitin synthase III from the trans-Golgi network to the cell surface.","citation":"Mol Biol Cell 2006 Oct;17(10):4157-66","abstract":"In Saccharomyces cerevisiae, the polysaccharide chitin is deposited at the mother bud junction by an integral membrane enzyme, chitin synthase 3 (Chs3p). The traffic of Chs3p to the cell surface from the trans-Golgi network (TGN) depends on two proteins, Chs5p and Chs6p, which sort selected cargo proteins into secretory vesicles. We have found that Chs5p forms a large higher-order complex of around 1 MDa with Chs6p and three Chs6 paralogs: Bch1p, Bud7p, and Bch2p. The Chs5/6 complex transiently interacts with its cargo, Chs3p, and the presence of Chs3p in the complex is dependent on every subunit. Chs5p and Chs6p have unique and crucial roles in Chs3p transport because either a chs5delta or chs6delta mutant drastically reduces the level of Chs3p bound to the remaining subunits of the complex. Bch1p and Bud7p appear to have a redundant function in Chs3p transport because deletion of both is necessary to displace Chs3p from the complex. The role of Bch2p in Chs3p binding is the least important. Chs5p is essential for structural integrity of the Chs5/6 complex and may act as a scaffold through which the other subunits assemble. Our results suggest a model of protein sorting at the TGN that involves a peripheral, possibly coat, complex that includes multiple related copies of a specificity determining subunit.","authors":"Sanchatjate S, Schekman R","authors_abbrev":"Sanchatjate S et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-07-21","publication_year":"2006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC31F10.16","SPAC6G9.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:17500045","title":"Alkyltransferase-like proteins.","citation":"DNA Repair (Amst) 2007 Aug 01;6(8):1222-8","abstract":"Recent in silico analysis has revealed the presence of a group of proteins in pro and lower eukaryotes, but not in Man, that show extensive amino acid sequence similarity to known O(6)-alkylguanine-DNA alkyltransferases, but where the cysteine at the putative active site is replaced by another residue, usually tryptophan. Here we review recent work on these proteins, which we designate as alkyltransferase-like (ATL) proteins, and consider their mechanism of action and role in protecting the host organisms against the biological effects of O(6)-alkylating agents, and their evolution. ATL proteins from Escherichia coli (eAtl, transcribed from the ybaz open reading frame) and Schizosaccharomyces pombe (Atl1) are able to bind to a range of O(6)-alkylguanine residues in DNA and to reversibly inhibit the action of the human alkyltransferase (MGMT) upon these substrates. Isolated proteins were not able to remove the methyl group in O(6)-methylguanine-containing DNA or oligonucleotides, neither did they display glycosylase or endonuclease activity. S. pombe does not contain a functional alkyltransferase and atl1 inactivation sensitises this organism to a variety of alkylating agents, suggesting that Atl1 acts by binding to O(6)-alkylguanine lesions and signalling them for processing by other DNA repair pathways. Currently we cannot exclude the possibility that ATL proteins arose through independent mutation of the alkyltransferase gene in different organisms. However, analyses of the proteins from E. coli and S. pombe, are consistent with a common function.","authors":"Margison GP, Butt A, Pearson SJ, Wharton S, Watson AJ, Marriott A, Caetano CM, Hollins JJ, Rukazenkova N, Begum G, Santibáñez-Koref MF","authors_abbrev":"Margison GP et al.","pubmed_publication_date":"01 Aug 2007","pubmed_entrez_date":"2007-05-15","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21828039","title":"Mfc1 is a novel forespore membrane copper transporter in meiotic and sporulating cells.","citation":"J Biol Chem 2011 Sep 30;286(39):34356-72","abstract":"To gain insight in the molecular basis of copper homeostasis during meiosis, we have used DNA microarrays to analyze meiotic gene expression in the model yeast Schizosaccharomyces pombe. Profiling data identified a novel meiosis-specific gene, termed mfc1(+), that encodes a putative major facilitator superfamily-type transporter. Although Mfc1 does not exhibit any significant sequence homology with the copper permease Ctr4, it contains four putative copper-binding motifs that are typically found in members of the copper transporter family of copper transporters. Similarly to the ctr4(+) gene, the transcription of mfc1(+) was induced by low concentrations of copper. However, its temporal expression profile during meiosis was distinct to ctr4(+). Whereas Ctr4 was observed at the plasma membrane shortly after induction of meiosis, Mfc1 appeared later in precursor vesicles and, subsequently, at the forespore membrane of ascospores. Using the fluorescent copper-binding tracker Coppersensor-1 (CS1), labile cellular copper was primarily detected in the forespores in an mfc1(+)/mfc1(+) strain, whereas an mfc1Δ/mfc1Δ mutant exhibited an intracellular dispersed punctate distribution of labile copper ions. In addition, the copper amine oxidase Cao1, which localized primarily in the forespores of asci, was fully active in mfc1(+)/mfc1(+) cells, but its activity was drastically reduced in an mfc1Δ/mfc1Δ strain. Furthermore, our data showed that meiotic cells that express the mfc1(+) gene have a distinct developmental advantage over mfc1Δ/mfc1Δ mutant cells when copper is limiting. Taken together, the data reveal that Mfc1 serves to transport copper for accurate and timely meiotic differentiation under copper-limiting conditions.","doi":"10.1074/jbc.M111.280396","authors":"Beaudoin J, Ioannoni R, López-Maury L, Bähler J, Ait-Mohand S, Guérin B, Dodani SC, Chang CJ, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"30 Sep 2011","pubmed_entrez_date":"2011-08-11","publication_year":"2011","canto_session_key":"fa89b880e6cd4f8d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-11-06 16:42:50","canto_approved_date":"2024-07-01 17:12:25","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-02-12 14:24:25","canto_added_date":"2012-02-17 17:24:52","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":74,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G6.13","SPAC139.05","SPCC550.06c","SPBC1198.01","SPAC15E1.02c","SPBC428.11","SPAC3G9.11c","SPCC1393.12","SPBC1711.08","SPCC663.11","SPBC4F6.17c","SPAC977.16c","SPCC364.07","SPCC663.03","SPAC589.02c","SPAC24C9.12c","SPAP8A3.04c","SPAC23C11.06c","SPAPB1A11.01","SPAC27D7.09c","SPBC3E7.02c","SPCC1223.02","SPNCRNA.84","SPAC3C7.14c","SPAC31A2.11c","SPAC22H10.13","SPCC1393.10","SPCC965.11c","SPAC869.09","SPAC23H4.15","SPAC926.04c","SPCC18B5.01c","SPAC19G12.09","SPBC16E9.16c","SPBC23G7.16","SPAC19A8.16","SPAC343.12","SPAC750.01","SPNCRNA.96","SPBC660.16","SPAC22G7.11c","SPAC57A7.09","SPAC13G7.02c","SPAC3G9.13c","SPBC16D10.06","SPAC977.14c","SPCC16A11.15c","SPBC26H8.01","SPCC1739.05","SPAC664.11","SPAC1142.05","SPBC16D10.08c","SPCC4B3.06c","SPAC4F10.17","SPBC530.07c","SPAC9E9.13","SPAC1F8.04c","SPCC338.18","SPBC32F12.03c","SPAPB1A11.02","SPBC1289.14","SPCC757.03c","SPAC5H10.02c","SPAC2E1P3.04","SPBC119.03","SPAC1B3.03c","SPBC1198.14c","SPNCRNA.80"],"gene_count":68,"ltp_gene_count":68,"approved_date":"2015-11-06"},{"uniquename":"PMID:22673520","title":"Constitutively active Cullin-RING-Ligases fail to rescue loss of NEDD8 conjugation in Schizosaccharomyces pombe.","citation":"FEBS Lett 2012 May 21;586(10):1522-8","abstract":"In fission yeast, the only known essential function of Ned8p is the modification of the cullin, Pcu1p, and subsequent Cullin-RING-Ligase (CRL) activation and substrate ubiquitination. We show here that a functional Pcu1p mutant, deleted for its C-terminal autoinhibitory domain, which negates the requirement of neddylation for ligase activity, is unable to rescue the loss of neddylation. These findings suggest that the neddylation of non-cullin substrate(s) are required for Schizosaccharomyces pombe viability.","doi":"10.1016/j.febslet.2012.04.011","authors":"Girdwood D, Robertson M, Gordon C","authors_abbrev":"Girdwood D et al.","pubmed_publication_date":"21 May 2012","pubmed_entrez_date":"2012-06-08","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1687.13c","SPAC24H6.12c","SPBC839.03c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:39120426","title":"Analysis of transcriptional response in haploid and diploid Schizosaccharomyces pombe under genotoxic stress.","citation":"G3 (Bethesda) 2024 Aug 09;","abstract":"Whole genome duplications are implicated in genome instability and tumorigenesis. Human and yeast polyploids exhibit increased replication stress and chromosomal instability, both hallmarks of cancer. In this study, we investigate the transcriptional response of Schizosaccharomyces pombe to increased ploidy generally, and in response to treatment with the genotoxin methyl methanesulfonate (MMS). We find that treatment of MMS induces upregulation of genes involved in general response to genotoxins, in addition to cell cycle regulatory genes. Downregulated genes are enriched in transport and sexual reproductive pathways. We find that the diploid response to MMS is muted compared to the haploid response, although the enriched pathways remain largely the same. Overall, our data suggests that the global S. pombe transcriptome doubles in response to increased ploidy but undergoes modest transcriptional changes in both unperturbed and genotoxic stress conditions.","doi":"10.1093/g3journal/jkae177","authors":"Park JM, Forsburg SL","authors_abbrev":"Park JM et al.","pubmed_publication_date":"09 Aug 2024","pubmed_entrez_date":"2024-08-09","publication_year":"2024","canto_session_key":"7c6acba10d98e9e4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-08-09 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33024177","title":"Pomegranate: 2D segmentation and 3D reconstruction for fission yeast and other radially symmetric cells.","citation":"Sci Rep 2020 Oct 06;10(1):16580","abstract":"Three-dimensional (3D) segmentation of cells in microscopy images is crucial to accurately capture signals that extend across optical sections. Using brightfield images for segmentation has the advantage of being minimally phototoxic and leaving all other channels available for signals of interest. However, brightfield images only readily provide information for two-dimensional (2D) segmentation. In radially symmetric cells, such as fission yeast and many bacteria, this 2D segmentation can be computationally extruded into the third dimension. However, current methods typically make the simplifying assumption that cells are straight rods. Here, we report Pomegranate, a pipeline that performs the extrusion into 3D using spheres placed along the topological skeletons of the 2D-segmented regions. The diameter of these spheres adapts to the cell diameter at each position. Thus, Pomegranate accurately represents radially symmetric cells in 3D even if cell diameter varies and regardless of whether a cell is straight, bent or curved. We have tested Pomegranate on fission yeast and demonstrate its ability to 3D segment wild-type cells as well as classical size and shape mutants. The pipeline is available as a macro for the open-source image analysis software Fiji/ImageJ. 2D segmentations created within or outside Pomegranate can serve as input, thus making this a valuable extension to the image analysis portfolio already available for fission yeast and other radially symmetric cell types.","doi":"10.1038/s41598-020-73597-w","authors":"Baybay EK, Esposito E, Hauf S","authors_abbrev":"Baybay EK et al.","pubmed_publication_date":"06 Oct 2020","pubmed_entrez_date":"2020-10-07","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-10-09 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10645488","title":"[Molecular evolution and structure of eukaryotic nuclear RNA polymerase subunits in light of the exon-intron organization of their genes].","citation":"Bioorg Khim 1999 Nov;25(11):828-37","abstract":"Analysis of literary data (for Saccharomyces cerevisiae, Caenorhabditis elegans, Arabidopsis thaliana, Homo sapiens, and some other Eucarya) and our data (for Schizosaccharomyces pombe) on the exon-intron organization of the genes encoding subunits of nuclear RNA polymerases showed that introns in the orthologous genes from different organisms are arranged nonrandomly, namely, their positions, if projected on the map of the comparison of the amino acid sequences of the orthologous subunits, not infrequently coincide in evolutionarily distant species. As a rule, intron positions correspond to the boundaries of the structurally conserved regions (domains) or to the sites of possible turns of the polypeptide chain. For example, introns flank the secondary structure elements in the Rpb8 subunit with the known three-dimensional structure or the structure-function modules in subunits Rpb10 and Rpc10. These facts are in agreement with the idea of the ancient origin of introns, and with the notion of evolution of ancient protein sequences through the assembly of their genes from short protoexons selected by the nature as far back as the RNA world times. Comparative analysis of the primary structures of the subunits of eukaryotic RNA polymerases allowed us to reveal a nuclear localization signal in subunit Rpb10 and some hypothetical archaeal homologues of subunit Rpc10.","authors":"Shpakovskiĭ GV, Lebedenko EN","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"2000-01-25","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15336631","title":"Identification and characterization of the rlp1+, the novel Rad51 paralog in the fission yeast Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2004 Oct 05;3(10):1363-74","abstract":"A new DNA repair gene from fission yeast Schizosaccharomyces pombe rlp1+ (RecA-like protein) has been identified. Rlp1 shows homology to RecA-like proteins, and is the third S. pombe Rad51 paralog besides Rhp55 and Rhp57. The new gene encodes a 363 aa protein with predicted Mr of 41,700 and has NTP-binding motif. The rlp1Delta mutant is sensitive to methyl methanesulfonate (MMS), ionizing radiation (IR), and camptothecin (CPT), although to a lesser extent than the deletion mutants of rhp55+ and rhp51+ genes. In contrast to other recombinational repair mutants, the rlp1Delta mutant does not exhibit sensitivity to UV light and mitomycin C (MMC). Mitotic recombination is moderately reduced in rlp1 mutant. Epistatic analysis of MMS and IR-sensitivity of rlp1Delta mutant indicates that rlp1+ acts in the recombinational pathway of double-strand break (DSB) repair together with rhp51+, rhp55+, and rad22+ genes. Yeast two-hybrid analysis suggests that Rlp1 may interact with Rhp57 protein. We propose that Rlp1 have an accessory role in repair of a subset of DNA damage induced by MMS and IR, and is required for the full extent of DNA recombination and cell survival under condition of a replication fork collapse.","authors":"Khasanov FK, Salakhova AF, Chepurnaja OV, Korolev VG, Bashkirov VI","authors_abbrev":"Khasanov FK et al.","pubmed_publication_date":"05 Oct 2004","pubmed_entrez_date":"2004-09-01","publication_year":"2004","canto_session_key":"2f48bc9798db3eed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-08 20:33:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-08 20:33:00","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.11","SPAC3C7.03c","SPAC644.14c","SPAC20H4.07","SPAC30D11.10","SPAC3G6.06c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-12-08"},{"uniquename":"PMID:11523775","title":"Gene insertion and replacement in Schizosaccharomyces pombe mediated by the Streptomyces bacteriophage phiC31 site-specific recombination system.","citation":"Mol Genet Genomics 2001 Aug;265(6):1031-8","abstract":"The site-specific recombination system used by the Streptomyces bacteriophage phiC31 was tested in the fission yeast Schizosaccharomyces pombe. A target strain with the phage attachment site attP inserted at the leu1 locus was co-transformed with one plasmid containing the bacterial attachment site attB linked to a ura4+ marker, and a second plasmid expressing the phiC31 integrase gene. High-efficiency transformation to the Ura+ phenotype occurred when the integrase gene was expressed. Southern analysis revealed that the attB-ura4+ plasmid integrated into the chromosomal attP site. Sequence analysis showed that the attBxattP recombination was precise. In another approach, DNA with a ura4+ marker flanked by two attB sites in direct orientation was used to transform S. pombe cells bearing an attP duplication. The phiC31 integrase catalyzed two reciprocal cross-overs, resulting in a precise gene replacement. The site-specific insertions are stable, as no excision (the reverse reaction) was observed on maintenance of the integrase gene in the integrant lines. The irreversibility of the phiC31 site-specific recombination system sets it apart from other systems currently used in eukaryotic cells, which reverse readily. Deployment of the phiC31 recombination provides new opportunities for directing transgene and chromosome rearrangements in eukaryotic systems.","authors":"Thomason LC, Calendar R, Ow DW","authors_abbrev":"Thomason LC et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-08-29","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30502955","title":"Profiling RNA Polymerase II Phosphorylation Genome-Wide in Fission Yeast.","citation":"Methods Enzymol 2018;612:489-504","abstract":"The RNA polymerase II carboxyl-terminal domain (CTD) consists of tandem repeats of consensus sequence Tyr 1 -Ser 2 -Pro 3 -Thr 4 -Ser 5 -Pro 6 -Ser 7 . Dynamic posttranslational modifications of the CTD generate a CTD code crucial for the cotranscriptional recruitment of factors that control transcription, chromatin modification, and RNA processing. Analysis of CTD phosphorylation by ChIP (Chromatin ImmunoPrecipitation) coupled with high-throughput DNA sequencing (ChIP-seq) is a powerful tool to investigate the changes in CTD phosphorylation during the transcription cycle. In this chapter, we describe a ChIP-seq protocol to profile the different CTD phospho-marks in fission yeast. Using this protocol, we have found that Tyr1P, Ser2P, and Thr4P signals are highest at gene 3' ends, whereas Ser5P is enriched across the gene bodies.","doi":"10.1016/bs.mie.2018.07.009","authors":"Kecman T, Heo DH, Vasiljeva L","authors_abbrev":"Kecman T et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-12-04","publication_year":"2018","canto_session_key":"da4a29388a396406","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-12-08 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37723847","title":"Pkd2, mutations linking to autosomal dominant polycystic kidney disease, localizes to the endoplasmic reticulum and regulates calcium signaling in fission yeast.","citation":"Genes Cells 2023 Nov;28(11):811-820","abstract":"Autosomal dominant polycystic kidney disease (ADPKD) is a renal disorder caused by mutations in the PKD2 gene, which encodes polycystin-2/Pkd2, a transient receptor potential channel. The precise role of Pkd2 in cyst formation remains unclear. The fission yeast Schizosaccharomyces pombe has a putative transient receptor potential channel, Pkd2, which shares similarities with human Pkd2. In this study, truncation analyses of fission yeast Pkd2 were conducted to investigate its localization and function. The results revealed that Pkd2 localizes not only to the plasma membrane but also to the endoplasmic reticulum (ER) in fission yeast. Furthermore, Pkd2 regulates calcium signaling in fission yeast, with the transmembrane domains of Pkd2 being sufficient for these processes. Specifically, the C-terminal region of Pkd2 plays a crucial role in the regulation of calcium signaling. Interestingly, human Pkd2 also localized to the ER and had some impact on calcium signaling in fission yeast. However, human Pkd2 failed to suppress the loss of fission yeast Pkd2. These findings indicate that hPkd2 may not completely substitute for cellular physiology of fission yeast Pkd2. This study provides insights into the localization and functional characteristics of Pkd2 in fission yeast, contributing to our understanding of the pathogenesis of ADPKD.","doi":"10.1111/gtc.13069","authors":"Koyano T, Fujimoto T, Onishi K, Matsuyama M, Fukushima M, Kume K","authors_abbrev":"Koyano T et al.","pubmed_publication_date":"Nov 2023","pubmed_entrez_date":"2023-09-19","publication_year":"2023","canto_session_key":"ae3cdbcd00418954","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takayuki Koyano","canto_first_approved_date":"2023-10-15 10:13:45","canto_approved_date":"2023-11-10 18:50:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-13 05:53:36","canto_added_date":"2023-09-20 00:15:04","annotation_curators":[{"name":"Takayuki Koyano","community_curator":true,"annotation_count":2,"orcid":"0000-0003-1675-2525","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.03","SPAC4G8.13c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-10-15"},{"uniquename":"PANTHER:PTHR15925","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.04","HGNC:14509"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20976105","title":"Silencing mediated by the Schizosaccharomyces pombe HIRA complex is dependent upon the Hpc2-like protein, Hip4.","citation":"PLoS One 2010 Oct 18;5(10):e13488","abstract":"HIRA (or Hir) proteins are conserved histone chaperones that function in multi-subunit complexes to mediate replication-independent nucleosome assembly. We have previously demonstrated that the Schizosaccharomyces pombe HIRA proteins, Hip1 and Slm9, form a complex with a TPR repeat protein called Hip3. Here we have identified a new subunit of this complex.\nTo identify proteins that interact with the HIRA complex, rapid affinity purifications of Slm9 were performed. Multiple components of the chaperonin containing TCP-1 complex (CCT) and the 19S subunit of the proteasome reproducibly co-purified with Slm9, suggesting that HIRA interacts with these complexes. Slm9 was also found to interact with a previously uncharacterised protein (SPBC947.08c), that we called Hip4. Hip4 contains a HRD domain which is a characteristic of the budding yeast and human HIRA/Hir-binding proteins, Hpc2 and UBN1. Co-precipitation experiments revealed that Hip4 is stably associated with all of the other components of the HIRA complex and deletion of hip4(+) resulted in the characteristic phenotypes of cells lacking HIRA function, such as temperature sensitivity, an elongated cell morphology and hypersensitivity to the spindle poison, thiabendazole. Moreover, loss of Hip4 function alleviated the heterochromatic silencing of reporter genes located in the mating type locus and centromeres and was associated with increased levels of non-coding transcripts derived from centromeric repeat sequences. Hip4 was also found to be required for the distinct form of silencing that controls the expression of Tf2 LTR retrotransposons.\nOverall, these results indicate that Hip4 is an integral component of the HIRA complex that is required for transcriptional silencing at multiple loci.","doi":"10.1371/journal.pone.0013488","authors":"Anderson HE, Kagansky A, Wardle J, Rappsilber J, Allshire RC, Whitehall SK","authors_abbrev":"Anderson HE et al.","pubmed_publication_date":"18 Oct 2010","pubmed_entrez_date":"2010-10-27","publication_year":"2010","canto_session_key":"10daa42b51138f14","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-07 15:39:01","canto_approved_date":"2022-06-23 12:43:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-07 15:38:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC222.12c","SPAC4A8.08c","SPAC1565.08","SPBC16C6.07c","SPCC417.08","SPCC1682.16","SPBC337.05c","SPBC530.10c","SPAPB8E5.09","SPBC800.05c","SPBC215.05","SPBC15D4.03","SPCC1827.06c","SPAC10F6.01c","HGNC:12506","SPBC947.08c","SPBC405.01","SPBC25H2.02","SPAC637.05c","SPAC13G7.02c","SPAC110.04c","SPBC19C2.07","SPBC31F10.14c","SPBC646.11","SPBC106.06","SPBC1105.02c","SPAC8E11.02c","SPBC365.16","SPAC22G7.06c","SPAC3A11.12c","SPAC17A5.15c","SPAC926.04c","SPBC12D12.03","SPBC4.07c","SPCC1223.08c","SPCC576.10c","SPBP35G2.07","SPBC14F5.04c","SPAC10F6.03c","SPBC26H8.07c","SPBP19A11.03c","SPBC31F10.13c"],"gene_count":41,"ltp_gene_count":4,"approved_date":"2016-04-07"},{"uniquename":"PMID:9810229","title":"Checkpoints on the road to mitosis.","citation":"Trends Biochem Sci 1998 Oct;23(10):399-402","abstract":"Eukaryotic organisms use cell-cycle checkpoints to ensure that nuclear division is restrained while DNA is undergoing replication or repair. Recent studies of the fission yeast Schizosaccharomyces pombe have illuminated these checkpoint mechanisms. These investigations have connected checkpoint proteins with central elements of the mitotic-control machinery.","authors":"Russell P","authors_abbrev":"Russell P","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-11-12","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11536333","title":"Analysis of 41 kb of the DNA sequence from the right arm of chromosome II of Schizosaccharomyces pombe.","citation":"Yeast 2001 Sep 15;18(12):1111-6","abstract":"We report the complete sequence of cosmid c18A7 (41 046 bp insert), located on the right arm of chromosome II of the Schizosaccharomyces pombe genome. The sequence, which partially overlaps with cosmids SPBC4F6 and SPBC336, contains 16 open reading frames (ORFs) capable of coding for proteins of at least 100 amino acid residues in length (one partial) and one small nucleolar RNA (snoRNA). Four known genes were found: swi10 (encoding a mating-type switching protein also involved in nucleotide excision repair); dim1 (encoding a dimethyladenosine transferase); arf1 (encoding ADP-ribosylation factor 1); and pol3 (cdc6) the partial fragment, encoding the 125 kDa catalytic subunit of the DNA polymerase type B. Six ORFs similar to known proteins were found. They include a transporter of the major facilitator superfamily class, a vacuolar sorting protein, an asparagine synthase, a nuclear protein, a reticulum oxidoreductin and a heat shock protein. Each protein product of the other six ORFs has conserved domains and can be assigned a molecular, but not a biological, function. The sequence has been submitted to the EMBL database under Accession No. AL080287.","authors":"Sánchez M, Revuelta JL, del Rey F, Gwilliam R, Skelton J, Churcher C, Rajandream MA, Wood V, Barrell B, Lyne R, Reinhardt R, Borzym K, Beck A, Moreno S, Domínguez A","authors_abbrev":"Sánchez M et al.","pubmed_publication_date":"15 Sep 2001","pubmed_entrez_date":"2001-09-06","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2740223","title":"Nucleotide sequence of a gene encoding a YPT1-related protein from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1989 Jun 12;17(11):4373","abstract":"","authors":"Fawell E, Hook S, Armstrong J","authors_abbrev":"Fawell E et al.","pubmed_publication_date":"12 Jun 1989","pubmed_entrez_date":"1989-06-12","publication_year":"1989","canto_session_key":"0e906986a6de9a4b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-20 16:07:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-20 13:48:21","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1703.10"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-11-20"},{"uniquename":"PMID:24333428","title":"Evolutionarily conserved IMPACT impairs various stress responses that require GCN1 for activating the eIF2 kinase GCN2.","citation":"Biochem Biophys Res Commun 2014 Jan 10;443(2):592-7","abstract":"In response to a range of environmental stresses, phosphorylation of the alpha subunit of the translation initiation factor 2 (eIF2α) represses general protein synthesis coincident with increased translation of specific mRNAs, such as those encoding the transcription activators GCN4 and ATF4. The eIF2α kinase GCN2 is activated by amino acid starvation by a mechanism involving GCN2 binding to an activator protein GCN1, along with association with uncharged tRNA that accumulates during nutrient deprivation. We previously showed that mammalian IMPACT and its yeast ortholog YIH1 bind to GCN1, thereby preventing GCN1 association with GCN2 and stimulation of this eIF2α kinase during amino acid depletion. GCN2 activity is also enhanced by other stresses, including proteasome inhibition, UV irradiation and lack of glucose. Here, we provide evidence that IMPACT affects directly and specifically the activation of GCN2 under these stress conditions in mammalian cells. We show that activation of mammalian GCN2 requires its interaction with GCN1 and that IMPACT promotes the dissolution of the GCN2-GCN1 complex. To a similar extent as the overexpression of YIH1, overexpression of IMPACT in yeast cells inhibited growth under all stress conditions that require GCN2 and GCN1 for cell survival, including exposure to acetic acid, high levels of NaCl, H₂O₂ or benomyl. This study extends our understanding of the roles played by GCN1 in GCN2 activation induced by a variety of stress arrangements and suggests that IMPACT and YIH1 use similar mechanisms for regulating this eIF2α kinase.","doi":"10.1016/j.bbrc.2013.12.021","authors":"Cambiaghi TD, Pereira CM, Shanmugam R, Bolech M, Wek RC, Sattlegger E, Castilho BA","authors_abbrev":"Cambiaghi TD et al.","pubmed_publication_date":"10 Jan 2014","pubmed_entrez_date":"2013-12-17","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.05c","SPBC36B7.09","SPAC27E2.02"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:17292401","title":"RNA degradation in fission yeast mitochondria is stimulated by a member of a new family of proteins that are conserved in lower eukaryotes.","citation":"J Mol Biol 2007 Mar 30;367(3):681-91","abstract":"We report here on the role of open reading frame (ORF) SPCC1183.04c of Schizosaccharomyces pombe in mitochondrial RNA metabolism. A mutant deleted for this ORF on chromosome III accumulates mitochondrial transcripts with the exception of the cob mRNA. A detailed Northern blot analysis showed that the effect results from a decrease in RNA degradation but not from RNA processing deficiencies. Overexpression of the SPCC1183.04c gene in a S. pombe wild-type strain is characterized by slow growth at 37 degrees C on non-fermentable carbon sources and a significant reduction of steady-state levels of mitochondrial transcripts. A NCBI BLASTP search with the amino acid sequence deduced from the S. pombe gene identified significant similarity to a number of proteins in fungi (e.g. Ascomycota, Basidiomycota) and in some non-fungal eukaryotes (e.g. ciliate, slime mold, red algae). By heterologous expression of SPCC1183.04c in a Saccharomyces cerevisiae pet127Delta strain, we demonstrate that the fission yeast protein and Pet127p from S. cerevisiae function similarly: The fission yeast gene complemented the respiratory defect associated with the pet127Delta allele and partially restored the RNA processing phenotype. Although it lacks any recognizable targeting signal, the S. pombe protein is imported into S. cerevisiae mitochondria in vivo. We conclude from our results that the fission yeast SPCC1183.04c gene is a member of a new protein family that functions to stimulate mitochondrial RNA degradation, a function that is conserved within the mitochondria of lower eukaryotes but seems to have been replaced by alternative pathways in metazoans and higher plants.","authors":"Wiesenberger G, Speer F, Haller G, Bonnefoy N, Schleiffer A, Schafer B","authors_abbrev":"Wiesenberger G et al.","pubmed_publication_date":"30 Mar 2007","pubmed_entrez_date":"2007-02-13","publication_year":"2007","canto_session_key":"96db0a6c64fc4961","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-07 17:07:12","canto_approved_date":"2025-05-30 09:52:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-18 11:55:37","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1183.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-03-07"},{"uniquename":"PMID:16506098","title":"Heterochromatin assembly: a new twist on an old model.","citation":"Chromosome Res 2006;14(1):83-94","abstract":"The organization of eukaryotic genomes requires a harmony between efficient compaction and accessibility. This is achieved through its packaging into chromatin. Chromatin can be subdivided into two general structural and functional compartments: euchromatin and heterochromatin. Euchromatin comprises most of the expressed genome, while heterochromatin participates intimately in the production of structures such as centromeres and telomeres essential for chromosome function. Studies in the fission yeast Schizosaccharomyces pombe have begun to highlight the genetic pathways critical for the assembly and epigenetic maintenance of heterochromatin, including key roles played by the RNAi machinery, H3 lysine 9 methylation and heterochromatin protein 1 (HP1). Recent studies have also identified a novel E3 ubiquitin ligase universally required for H3 K9 methylation. Here we outline these studies and propose several models for the role of this E3 ligase in heterochromatin assembly.","authors":"Horn PJ, Peterson CL","authors_abbrev":"Horn PJ et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-03-01","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20421724","title":"Phosphorylation-regulated binding of Ctp1 to Nbs1 is critical for repair of DNA double-strand breaks.","citation":"Cell Cycle 2010 Apr 15;9(8):1516-22","abstract":"Repair of DNA double-strand breaks (DSBs) is critical for cell survival and for maintaining genome stability in eukaryotes. In Schizosaccharomyces pombe, the Mre11-Rad50-Nbs1 (MRN) complex and Ctp1 cooperate to perform the initial steps that process and repair these DNA lesions via homologous recombination (HR). While Ctp1 is recruited to DSBs in an MRN-dependent manner, the specific mechanism of this process remained unclear. We recently found that Ctp1 is phosphorylated on a domain rich in putative Casein kinase 2 (CK2) phosphoacceptor sites that resembles the SDTD repeats of Mdc1. Furthermore, phosphorylation of this motif is required for interaction with the FHA domain of Nbs1 that localizes Ctp1 to DSB sites. Here, we review and discuss these findings, and we present new data that further characterize the cellular consequences of mutating CK2 phosphorylation motifs of Ctp1, including data showing that these sites are critical for meiosis.","authors":"Dodson GE, Limbo O, Nieto D, Russell P","authors_abbrev":"Dodson GE et al.","pubmed_publication_date":"15 Apr 2010","pubmed_entrez_date":"2010-04-28","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC338.08","SPBC6B1.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:16079177","title":"Characterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradation.","citation":"Mol Biol Cell 2005 Oct;16(10):4714-24","abstract":"It has been postulated that creation of Man8GlcNAc2 isomer B (M8B) by endoplasmic reticulum (ER) alpha-mannosidase I constitutes a signal for driving irreparably misfolded glycoproteins to proteasomal degradation. Contrary to a previous report, we were able to detect in vivo (but not in vitro) an extremely feeble ER alpha-mannosidase activity in Schizosaccharomyces pombe. The enzyme yielded M8B on degradation of Man9GlcNAc2 and was inhibited by kifunensin. Live S. pombe cells showed an extremely limited capacity to demannosylate Man9GlcNAc2 present in misfolded glycoproteins even after a long residence in the ER. In addition, no preferential degradation of M8B-bearing species was detected. Nevertheless, disruption of the alpha-mannosidase encoding gene almost totally prevented degradation of a misfolded glycoprotein. This and other conflicting reports may be best explained by assuming that the role of ER mannosidase on glycoprotein degradation is independent of its enzymatic activity. The enzyme, behaving as a lectin binding polymannose glycans of varied structures, would belong together with its enzymatically inactive homologue Htm1p/Mnl1p/EDEM, to a transport chain responsible for delivering irreparably misfolded glycoproteins to proteasomes. Kifunensin and 1-deoxymannojirimycin, being mannose homologues, would behave as inhibitors of the ER mannosidase or/and Htm1p/Mnl1p/EDEM putative lectin properties.","authors":"Movsichoff F, Castro OA, Parodi AJ","authors_abbrev":"Movsichoff F et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-08-05","publication_year":"2005","canto_session_key":"dd3fc9f60bb5d280","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-02-18 11:16:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-06-27 08:29:50","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC513.05","SPAC2E1P5.01c","SPAC23A1.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-06-27"},{"uniquename":"PMID:23160","title":"Some kinetic aspects of the mechanism of hydrolysis of phosphoric acid esters by nonspecific acid phosphatase from Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1978 Jan 12;522(1):122-9","abstract":"1. The kinetics of the hydrolysis of nitrophenylphosphate by nonspecific acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2.) from Schizosaccharomices pombe was studied. 2. The kinetic parameters, Km and V, were determined as well as the inhibition constants, K1, for the inhibitors, phosphate and fluoride, as a function of pH. 3. The results, interpreted according to the theories of Dixon and Waley indicated the presence of three ionizable groups on the enzyme itself and one on the enzyme-substrate complex. 4. A model of the hydrolysis of phosphoric acid monoesters by the S. pombe acid phosphatase is proposed based on the ionization state of the reactants and on the results of the inhibition by the competitive inhibitors.","authors":"Dibenedetto G, Mura U","authors_abbrev":"Dibenedetto G et al.","pubmed_publication_date":"12 Jan 1978","pubmed_entrez_date":"1978-01-12","publication_year":"1978","canto_session_key":"85d2941a97c295f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-23 17:43:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-23 17:43:23","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-23"},{"uniquename":"PMID:41103389","title":"The insight into instability mechanism of Jiangxiangxing  Baijiu  fermentation and the key functional regulation of  Schizosaccharomyces pombe .","citation":"Food Chem X 2025 Oct;31:103085","abstract":"Jiangxiangxing  Baijiu  (JXXB) suffers from quality instability due to its complex spontaneous fermentation. This study compared fermented grains from excellent (Group-E) and normal (Group-N) workshops, identifying 28 volatiles as distinguished substances for quality. The core functional species were revealed by integrated meta-genomic and meta-transcriptomic sequencing analysis. Moreover,  Schizosaccharomyces pombe  and  Acetilactobacillus jinshanensis  were demonstrated as key functional contributors, while only  Schi. pombe  was highlighted active participation in both heap fermentation and pit fermentation. Notably, the proportions and doses of the functional yeasts, particularly  Schi. pombe , were higher in Group-E, resulting in the higher quality. Furthermore, the industrial-scale bioaugmentation with  Schi. pombe  enhanced substrate utilization, elevated the production of flavor substances by 13.61 %, and improved the yield and excellent-quality proportion of base  Baijiu  by 32.18 % and 37.16 %, respectively. This study provided insights into the quality instability mechanism of JXXB, and fostered a foundation for ensuring consistent quality in solid-state fermentation.","doi":"10.1016/j.fochx.2025.103085","authors":"Shi G, Yan P, Shen S, Tang P, Chen P, Sun L, Xing S, Fang C, Li C, Lin L, Zhang C","authors_abbrev":"Shi G et al.","pubmed_publication_date":"Oct 2025","pubmed_entrez_date":"2025-10-17","publication_year":"2025","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2025-10-17 23:25:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35100446","title":"Acetylation stabilises calmodulin-regulated calcium signalling.","citation":"FEBS Lett 2022 Mar;596(6):762-771","abstract":"Calmodulin is a conserved calcium signalling protein that regulates a wide range of cellular functions. Amino-terminal acetylation is a ubiquitous post-translational modification that affects the majority of human proteins, to stabilise structure, as well as regulate function and proteolytic degradation. Here, we present data on the impact of amino-terminal acetylation upon structure and calcium signalling function of fission yeast calmodulin. We show that NatA-dependent acetylation stabilises the helical structure of the Schizosaccharomyces pombe calmodulin, impacting its ability to associate with myosin at endocytic foci. We go on to show that this conserved modification impacts both the calcium-binding capacity of yeast and human calmodulins. These findings have significant implications for research undertaken into this highly conserved essential protein.","doi":"10.1002/1873-3468.14304","authors":"Baker K, Geeves MA, Mulvihill DP","authors_abbrev":"Baker K et al.","pubmed_publication_date":"Mar 2022","pubmed_entrez_date":"2022-01-31","publication_year":"2022","canto_session_key":"0190151274104c5d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-02-02 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27655872","title":"A Golgi rhomboid protease Rbd2 recruits Cdc48 to cleave yeast SREBP.","citation":"EMBO J 2016 Nov 02;35(21):2332-2349","abstract":"Hypoxic growth of fungi requires sterol regulatory element-binding protein (SREBP) transcription factors, and human opportunistic fungal pathogens require SREBP activation for virulence. Proteolytic release of fission yeast SREBPs from the membrane in response to low oxygen requires the Golgi membrane-anchored Dsc E3 ligase complex. Using genetic interaction arrays, we identified Rbd2 as a rhomboid family protease required for SREBP proteolytic processing. Rbd2 is an active, Golgi-localized protease that cleaves the transmembrane segment of the TatA rhomboid model substrate. Epistasis analysis revealed that the Dsc E3 ligase acts on SREBP prior to cleavage by Rbd2. Using APEX2 proximity biotinylation, we demonstrated that Rbd2 binds the AAA-ATPase Cdc48 through a C-terminal SHP box. Interestingly, SREBP cleavage required Rbd2 binding of Cdc48, consistent with Cdc48 acting to recruit ubiquitinylated substrates. In support of this claim, overexpressing a Cdc48-binding mutant of Rbd2 bypassed the Cdc48 requirement for SREBP cleavage, demonstrating that Cdc48 likely plays a role in SREBP recognition. In the absence of functional Rbd2, SREBP precursor is degraded by the proteasome, indicating that Rbd2 activity controls the balance between SREBP activation and degradation.","authors":"Hwang J, Ribbens D, Raychaudhuri S, Cairns L, Gu H, Frost A, Urban S, Espenshade PJ","authors_abbrev":"Hwang J et al.","pubmed_publication_date":"02 Nov 2016","pubmed_entrez_date":"2016-09-23","publication_year":"2016","canto_session_key":"1edc814df6ff1176","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2017-01-04 17:12:04","canto_approved_date":"2025-09-02 20:38:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-30 19:58:59","canto_added_date":"2016-09-24 00:15:11","annotation_curators":[{"name":"Peter Espenshade","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":43,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC790.03","SPAC1486.02c","SPAC1565.08","SPBC947.10","SPBC354.05c","SPBC16G5.01","SPAC20H4.02","SPBC17D11.02c","SPAC4D7.11","SPBC19C2.09","SPBC14F5.07"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2017-01-04"},{"uniquename":"PMID:31061345","title":"[Fission Yeast as a Model System for Studying Cancer Signaling and Drug Discovery: Discovery of ACA-28 as a Novel Inducer of ERK-dependent Apoptosis Reveals a New Cancer Therapy].","citation":"Yakugaku Zasshi 2019;139(5):753-758","abstract":"Mitogen-activated protein kinase (MAPK) pathways are evolutionarily conserved kinase modules that link extracellular signals to the machinery that controls fundamental cellular processes such as growth, proliferation, differentiation, and apoptosis. The Ras/Raf/MEK/ERK MAPK pathway is one of the most studied of the mammalian MAPK pathways and has attracted intense research interest because of its critical involvement in the regulation of cell proliferation. The mutational activation of upstream signaling components that constitutively activate ERK MAPKs as seen in various primary tumor samples has validated this pathway for drug discovery. The fission yeast Schizosaccharomyces pombe is an important tool for cancer research. This well-studied model organism has enabled groundbreaking, Nobel Prize-winning discoveries and has provided insights into how both normal and cancerous cells grow and divide. We performed chemical genetic screening using a fission yeast phenotypic assay and demonstrated that ACA-28, a synthetic derivative of 1'-acetoxychavicol acetate (ACA), effectively inhibited the growth of melanoma cancer cells wherein ERK MAPK signaling is hyperactivated due to mutations in the upstream activating regulators. Importantly, the growth of normal human epidermal melanocytes was less affected by ACA-28. In addition, ACA-28 specifically induced apoptosis in NIH/3T3 cells oncogenically transformed with HER2/ErbB2 but not in the parental cells. Notably, the ACA-28-induced apoptosis was abrogated when ERK activation was blocked with the specific MEK inhibitor U0126. Consistently, ACA-28 more strongly stimulated ERK phosphorylation in melanoma cells as compared with normal human epidermal melanocytes. ACA-28 might serve as a promising seed compound to combat ERK-dependent cancers by stimulating oncogenic signaling.","doi":"10.1248/yakushi.18-00185-3","authors":"Sugiura R","authors_abbrev":"Sugiura R","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-05-08","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-09 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8413179","title":"Genetic analysis of human p34CDC2 function in fission yeast.","citation":"Mol Gen Genet 1993 Sep;240(3):315-22","abstract":"The p34cdc2 protein kinase plays a key role in the control of the mitotic cell cycle of fission yeast, being required for both entry into S-phase and for entry into mitosis in the mitotic cell cycle, as well as for the initiation of the second meiotic nuclear division. In recent years, structural and functional homologues of p34cdc2, as well as several of the proteins that interact with and regulate p34cdc2 function in fission yeast, have been identified in a wide range of higher eukaryotic cell types, suggesting that the control mechanisms uncovered in this simple eukaryote are likely to be well conserved across evolution. Here we describe the construction and characterisation of a fission yeast strain in which the endogenous p34cdc2 protein is entirely absent and is replaced by its human functional homologue p34CDC2. We have used this strain to analyse aspects of the function of the human p34CDC2 protein genetically. We show that the function of the human p34CDC2 protein in fission yeast cells is dependent upon the action of the protein tyrosine phosphatase p80cdc25, that it responds to altered levels of both the mitotic inhibitor p107wee1 and the p34cdc2-binding protein p13suc1, and is lethal in combination with the mutant B-type cyclin p56cdc13-117. In addition, we demonstrate that the human p34CDC2 protein is proficient for fission yeast meiosis, and examine the behaviour of two mutant p34CDC2 proteins in fission yeast.","authors":"MacNeill SA, Nurse P","authors_abbrev":"MacNeill SA et al.","pubmed_publication_date":"Sep 1993","pubmed_entrez_date":"1993-09-01","publication_year":"1993","canto_session_key":"873988311eb85ee1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-04-09 17:43:14","canto_approved_date":"2022-07-28 20:10:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-09 13:42:57","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC582.03","SPAC24H6.05","SPBC1734.14c","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":0,"approved_date":"2018-04-09"},{"uniquename":"PMID:21724934","title":"RNA interference in fungi: pathways, functions, and applications.","citation":"Eukaryot Cell 2011 Sep;10(9):1148-55","abstract":"Small RNA molecules of about 20 to 30 nucleotides function in gene regulation and genomic defense via conserved eukaryotic RNA interference (RNAi)-related pathways. The RNAi machinery consists of three core components: Dicer, Argonaute, and RNA-dependent RNA polymerase. In fungi, the RNAi-related pathways have three major functions: genomic defense, heterochromatin formation, and gene regulation. Studies of Schizosaccharomyces pombe and Neurospora, and other fungi have uncovered surprisingly diverse small RNA biogenesis pathways, suggesting that fungi utilize RNAi-related pathways in various cellular processes to adapt to different environmental conditions. These studies also provided important insights into how RNAi functions in eukaryotic systems in general. In this review, we will discuss our current understanding of the fungal RNAi-related pathways and their functions, with a focus on filamentous fungi. We will also discuss how RNAi can be used as a tool in fungal research.","doi":"10.1128/EC.05109-11","authors":"Dang Y, Yang Q, Xue Z, Liu Y","authors_abbrev":"Dang Y et al.","pubmed_publication_date":"Sep 2011","pubmed_entrez_date":"2011-07-05","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41330900","title":"PolySUMOylation of PCNA and Rad52 restricts centromeric recombination in fission yeast.","citation":"Nat Commun 2025 Dec 02;16(1):10837","abstract":"SUMOylation, a conserved post-translational modification in eukaryotes, regulates protein function, localization, and stability. However, the role of SUMO chains in genome maintenance is still emerging. Using Schizosaccharomyces pombe, we show that loss of SUMO chains results in spontaneous replication stress, DNA damage, and elevated centromeric recombination. To investigate SUMO-dependent interactome at the sites of Rad52 repair, we used a split-SUMO-ID proteomics approach. It allows the analysis of local SUMOylation content at the Rad52 repair sites, and enabled the identification of the essential replication factor PCNA. We found that SUMO chain-modified PCNA antagonizes Rad8-mediated PCNA polyubiquitination, modulating the choice of post-replication repair pathways at stalled forks within centromeres. In the absence of polySUMOylation, excessive PCNA polyubiquitination drives elevated recombination at centromeres. Artificial tethering of a SUMO chain to Rad52 suppresses this defect. Our findings uncover an essential role for SUMO chains in centromere maintenance by modulating DNA repair pathway choice under endogenous replication stress.","doi":"10.1038/s41467-025-65862-1","authors":"Markowska K, Litwin I, Misiorna D, Kończak J, Bogdańska A, Tomaszewska P, Tracz M, Haenen M, Kramarz K","authors_abbrev":"Markowska K et al.","pubmed_publication_date":"02 Dec 2025","pubmed_entrez_date":"2025-12-02","publication_year":"2025","canto_session_key":"73a5b4ec57c90b56","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Karol Kramarz","canto_first_approved_date":"2026-02-26 10:41:32","canto_approved_date":"2026-05-29 10:25:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-04-24 09:21:44","canto_added_date":"2025-12-04 00:25:05","annotation_curators":[{"name":"Karol Kramarz","community_curator":true,"annotation_count":1,"orcid":"0000-0001-9924-3106","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":99,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPBC83.08","SPAC1687.05","SPBC336.04","SPCC622.09","SPAC17A2.13c","SPBC365.06","SPBC16D10.09","SPAC30D11.10","SPCC23B6.05c","SPAC644.14c","SPAC16A10.06c","SPAC13G6.01c","SPBC1347.01c","SPAC688.10","SPAC8E11.02c","SPBC3D6.11c"],"gene_count":17,"ltp_gene_count":10,"approved_date":"2026-02-26"},{"uniquename":"PMID:19029536","title":"EnsemblCompara GeneTrees: Complete, duplication-aware phylogenetic trees in vertebrates.","citation":"Genome Res 2009 Feb;19(2):327-35","abstract":"We have developed a comprehensive gene orientated phylogenetic resource, EnsemblCompara GeneTrees, based on a computational pipeline to handle clustering, multiple alignment, and tree generation, including the handling of large gene families. We developed two novel non-sequence-based metrics of gene tree correctness and benchmarked a number of tree methods. The TreeBeST method from TreeFam shows the best performance in our hands. We also compared this phylogenetic approach to clustering approaches for ortholog prediction, showing a large increase in coverage using the phylogenetic approach. All data are made available in a number of formats and will be kept up to date with the Ensembl project.","doi":"10.1101/gr.073585.107","authors":"Vilella AJ, Severin J, Ureta-Vidal A, Heng L, Durbin R, Birney E","authors_abbrev":"Vilella AJ et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-11-26","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:18:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8599928","title":"A multicopy suppressor of a cell cycle defect in S. pombe encodes a heat shock-inducible 40 kDa cyclophilin-like protein.","citation":"EMBO J 1996 Feb 01;15(3):447-56","abstract":"Cyclophilins are peptidyl-prolyl cis-trans isomerases (PPIases) which have been implicated in intracellular protein folding, transport and assembly. Cyclophilins are also known as the intracellular receptors for the immunosuppressive drug cyclosporin A (CsA). The most common type of cyclophilins are the 18 kDa cytosolic proteins containing only the highly conserved core domain for PPIase and CsA binding activities. The wis2+ gene of the fission yeast Schizosaccharomyces pombe was isolated as a multicopy suppressor of wee1-50 cdc25-22 win1-1, a triple mutant strain which exhibits a cell cycle defect phenotype. Sequence analysis of wis2+ reveals that it encodes a 40 kDa cyclophilin-like protein, homologous to the mammalian cyclophilin 40. The 18 kDa cyclophilin domain (CyP-18) of wis2 is followed by a C-terminal region of 188 amino acids. The C-terminal region of wis2 is essential for suppression of the triple mutant defect. Furthermore this region of the protein is able to confer suppression activity on the 18 kDa S.pombe cyclophilin, cyp1, since a hybrid protein consisting of an 18 kDa S.pombe cyclophilin (cyp1) fused to the C-terminus of wis2 shows suppression activity. We also demonstrate that the level of wis2+ mRNA increases 10- to 20-fold upon heat shock of S.pombe cells suggesting a role for wis2+ in the heat-shock response.","authors":"Weisman R, Creanor J, Fantes P","authors_abbrev":"Weisman R et al.","pubmed_publication_date":"01 Feb 1996","pubmed_entrez_date":"1996-02-01","publication_year":"1996","canto_session_key":"b5b2fbc60c16e523","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-04-05 20:54:23","canto_approved_date":"2025-04-05 20:54:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-05 20:54:14","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-04-05"},{"uniquename":"PMID:19170768","title":"Localization of gene products using a chromosomally tagged GFP-fusion library in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Cells 2009 Feb;14(2):217-25","abstract":"We constructed a library of chromosomally-tagged green fluorescent protein (GFP) fusions in the fission yeast Schizosaccharomyces pombe. This library contains 1058 strains. In each strain, the coding sequence of GFP is integrated at the 3'-end of a particular chromosomal ORF such that the full-length GFP fusion construct is expressed under the control of the original promoter. Integration of the GFP coding sequence at the authentic chromosomal location of each gene was confirmed by PCR. Microscopic screening of these strains detected sufficient levels of GFP signal in 710 strains and allowed assignment of these GFP-fusion gene products with their intracellular localization: 374 proteins were localized in the nucleus, 65 proteins in the nucleolus, 34 proteins at the nuclear periphery, 27 proteins at the plasma membrane and cytoplasmic membranous structures, 24 proteins at the spindle pole body and microtubules, 92 proteins at cytoplasmic structures, and 94 proteins were uniformly distributed throughout the cytoplasm.","doi":"10.1111/j.1365-2443.2008.01264.x","authors":"Hayashi A, Ding DQ, Tsutsumi C, Chikashige Y, Masuda H, Haraguchi T, Hiraoka Y","authors_abbrev":"Hayashi A et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2009-01-28","publication_year":"2009","canto_session_key":"4412d1ad7ff87c4a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-12-07 11:12:37","canto_approved_date":"2017-12-07 11:12:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-07 11:12:31","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2017-12-07"},{"uniquename":"PMID:35190689","title":"Using deep learning to annotate the protein universe.","citation":"Nat Biotechnol 2022 Jun;40(6):932-937","abstract":"Understanding the relationship between amino acid sequence and protein function is a long-standing challenge with far-reaching scientific and translational implications. State-of-the-art alignment-based techniques cannot predict function for one-third of microbial protein sequences, hampering our ability to exploit data from diverse organisms. Here, we train deep learning models to accurately predict functional annotations for unaligned amino acid sequences across rigorous benchmark assessments built from the 17,929 families of the protein families database Pfam. The models infer known patterns of evolutionary substitutions and learn representations that accurately cluster sequences from unseen families. Combining deep models with existing methods significantly improves remote homology detection, suggesting that the deep models learn complementary information. This approach extends the coverage of Pfam by >9.5%, exceeding additions made over the last decade, and predicts function for 360 human reference proteome proteins with no previous Pfam annotation. These results suggest that deep learning models will be a core component of future protein annotation tools.","doi":"10.1038/s41587-021-01179-w","authors":"Bileschi ML, Belanger D, Bryant DH, Sanderson T, Carter B, Sculley D, Bateman A, DePristo MA, Colwell LJ","authors_abbrev":"Bileschi ML et al.","pubmed_publication_date":"Jun 2022","pubmed_entrez_date":"2022-02-22","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1486.11","HGNC:26946"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10502409","title":"Functional conservation and cell cycle localization of the Nhp2 core component of H + ACA snoRNPs in fission and budding yeasts.","citation":"Exp Cell Res 1999 Oct 10;252(1):165-74","abstract":"We report the identification of a novel nucleolar protein from fission yeast, p17(nhp2), which is homologous to the recently identified Nhp2p core component of H+ACA snoRNPs in Saccharomyces cerevisiae. We show that the fission yeast p17(nhp2) localizes to the nucleolus in live S. cerevisiae or Schizosaccharomyces pombe cells and is functionally conserved since the fission yeast gene can complement a deletion of the NHP2 gene in budding yeast. Analysis of p17(nhp2) during the mitotic cell cycles of living fission and budding yeast cells shows that this protein, and by implication H+ACA snoRNPs, remains localized with nucleolar material during mitosis, although the gross organization of partitioning of p17(nhp2) during anaphase is different in a comparison of the two yeasts. During anaphase in S. pombe p17(nhp2) trails segregating chromatin, while in S. cerevisiae the protein segregates alongside bulk chromatin. The pattern of segregation comparing haploid and diploid S. cerevisiae cells suggests that p17(nhp2) is closely associated with the rDNA during nuclear division.","authors":"Maiorano D, Brimage LJ, Leroy D, Kearsey SE","authors_abbrev":"Maiorano D et al.","pubmed_publication_date":"10 Oct 1999","pubmed_entrez_date":"1999-09-30","publication_year":"1999","canto_session_key":"7b4eb7259e99d4c2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-04 13:29:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 13:29:29","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1782.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:17397989","title":"Gradual melting of a replication origin (Schizosaccharomyces pombe ars1): in situ atomic force microscopy (AFM) analysis.","citation":"Biochimie 2007 Apr;89(4):534-41","abstract":"Local DNA melting is integral to fundamental processes such as replication or transcription. In vivo, these two processes do not occur on molecules free in solution but, instead, involve DNA molecules which are organized into DNA/proteins complexes. Atomic force microscopy imaging offers a possibility to look at individual molecules. It allowed us to follow the progress of local denaturation in liquid, but with the added constraints of DNA lying on a surface. We present a kinetic analysis of the mapping of the temperature-driven melting seen at a replication origin (Schizosaccharomyces pombe ars1). The results indicate an expected base composition dependency, but also a strong extremity effect. Noteworthy, a \"structural\" effect is clearly occurring - which is shown by the greater susceptibility of the strongly curved region present in the sequence to unwind. DNA melting, at this place, is seen to occur after an increase in the curvature amplitude and a simultaneous shift of the nucleotide sequence positioned at the apex. Because this may determine the position of the Replication Initiation (R.I.) site, the result suggests that eukaryotic replication origins, although described as possessing no consensus sequences, may well have their mechanics sustained by the properties of common structural features. Our analysis may, therefore, provide new information that will give genuine insights on how DNA molecules behave when organized into primosomes, replisomes, promoter initiation complexes, etc. and thus, be essential to better understanding the way genes function.","authors":"Marilley M, Milani P, Rocca-Serra J","authors_abbrev":"Marilley M et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-04-03","publication_year":"2007","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37953281","title":"Pot1 promotes telomere DNA replication via the Stn1-Ten1 complex in fission yeast.","citation":"Nucleic Acids Res 2023 Dec 11;51(22):12325-12336","abstract":"Telomeres are nucleoprotein complexes that protect the chromosome-ends from eliciting DNA repair while ensuring their complete duplication. Pot1 is a subunit of telomere capping complex that binds to the G-rich overhang and inhibits the activation of DNA damage checkpoints. In this study, we explore new functions of fission yeast Pot1 by using a pot1-1 temperature sensitive mutant. We show that pot1 inactivation impairs telomere DNA replication resulting in the accumulation of ssDNA leading to the complete loss of telomeric DNA. Recruitment of Stn1 to telomeres, an auxiliary factor of DNA lagging strand synthesis, is reduced in pot1-1 mutants and overexpression of Stn1 rescues loss of telomeres and cell viability at restrictive temperature. We propose that Pot1 plays a crucial function in telomere DNA replication by recruiting Stn1-Ten1 and Polα-primase complex to telomeres via Tpz1, thus promoting lagging-strand DNA synthesis at stalled replication forks.","doi":"10.1093/nar/gkad1036","authors":"Carvalho Borges PC, Bouabboune C, Escandell JM, Matmati S, Coulon S, Ferreira MG","authors_abbrev":"Carvalho Borges PC et al.","pubmed_publication_date":"11 Dec 2023","pubmed_entrez_date":"2023-11-12","publication_year":"2023","canto_session_key":"b17c1a5c7a58ba28","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-11-14 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9614176","title":"Cyclin B proteolysis and the cyclin-dependent kinase inhibitor rum1p are required for pheromone-induced G1 arrest in fission yeast.","citation":"Mol Biol Cell 1998 Jun;9(6):1309-21","abstract":"The blocking of G1 progression by fission yeast pheromones requires inhibition of the cyclin-dependent kinase cdc2p associated with the B-cyclins cdc13p and cig2p. We show that cyclosome-mediated degradation of cdc13p and cig2p is necessary for down-regulation of B-cyclin-associated cdc2p kinase activity and for phermone-induced G1 arrest. The cyclin-dependent kinase inhibitor rum1p is also required to maintain this G1 arrest; it binds both cdc13p and cig2p and is specifically required for cdc13p proteolysis. We propose that rum1p acts as an adaptor targeting cdc13p for degradation by the cyclosome. In contrast, the cig2p-cdc2p kinase can be down-regulated, and the cyclin cig2p can be proteolyzed independently of rum1p. We suggest that pheromone signaling inhibits the cig2p-cdc2p kinase, bringing about a transient G1 arrest. As a consequence, rum1p levels increase, thus inhibiting and inducing proteolysis of the cdc13p-cdc2p kinase; this is necessary to maintain G1 arrest. We have also shown that pheromone-induced transcription occurs only in G1 and is independent of rum1p.","authors":"Stern B, Nurse P","authors_abbrev":"Stern B et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-06-17","publication_year":"1998","canto_session_key":"c8f784dd2ebdf2e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-06-09 11:45:24","canto_approved_date":"2022-07-22 15:10:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-06 10:42:19","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jacky Hayles","community_curator":true,"annotation_count":11,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPBC336.12c","SPAC1F7.05","SPBC582.03","SPBC32F12.09","SPAC17C9.01c","SPAPB2B4.03","SPAC24H6.05","SPBC11B10.09","SPAC20G4.02c","SPBC23G7.17c","SPAC26A3.01"],"gene_count":12,"ltp_gene_count":4,"approved_date":"2018-06-09"},{"uniquename":"PMID:9693370","title":"Mutational effect of fission yeast polalpha on cell cycle events.","citation":"Mol Biol Cell 1998 Aug;9(8):2107-23","abstract":"Polalpha is the principal DNA polymerase for initiation of DNA replication and also functions in postinitiation DNA synthesis. In this study, we investigated the cell cycle responses induced by mutations in polalpha+. Germinating spores carrying either a deletion of polalpha+ (polalphaDelta) or a structurally intact but catalytically dead polalpha mutation proceed to inappropriate mitosis with no DNA synthesis. This suggests that the catalytic function, and not the physical presence of Polalpha, is required to generate the signal that prevents the cells from entering mitosis prematurely. Cells with a polalphats allele arrest the cell cycle near the hydroxyurea arrest point, but, surprisingly, polalphats in cdc20 (polepsilon mutant) background arrested with a cdc phenoytpe, not a polalphats-like phenotype. At 25 degrees C, replication perturbation caused by polalphats alleles induces Cds1 kinase activity and requires the checkpoint Rads, Cds1, and Rqh1, but not Chk1, to maintain cell viability. At 36 degrees C, replication disruption caused by polalphats alleles induces the phosphorylation of Chk1; however, mutant cells arrest with heterogeneous cell sizes with a population of the cells entering aberrant mitosis. Together, our results indicate that the initiation DNA structure synthesized by Polalpha is required to bring about the S phase to mitosis checkpoint, whereas replication defects of different severity caused by polalphats mutations induce differential downstream kinase responses.","authors":"Bhaumik D, Wang TS","authors_abbrev":"Bhaumik D et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-08-07","publication_year":"1998","canto_session_key":"05284071e0eba01a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-06-01 14:59:36","canto_approved_date":"2026-02-09 10:57:04","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-02-13 11:50:41","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":93,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c","SPBC11B10.09","SPBC4.04c","SPBC336.12c","SPAC3H5.06c","SPAC2G11.12","SPAC9E9.08","SPCC1259.13","SPBC25H2.13c","SPBC336.04","SPAC20G8.01","SPCC18B5.11c","SPAC14C4.13","SPAC1952.07","SPAC1F7.05","SPBC14C8.07c","SPCC16A11.17","SPAC24H6.05","SPBC216.05"],"gene_count":19,"ltp_gene_count":19,"approved_date":"2018-06-01"},{"uniquename":"PMID:22952839","title":"Swi1 associates with chromatin through the DDT domain and recruits Swi3 to preserve genomic integrity.","citation":"PLoS One 2012;7(8):e43988","abstract":"Swi1 and Swi3 form the replication fork protection complex and play critical roles in proper activation of the replication checkpoint and stabilization of replication forks in the fission yeast Schizosaccharomyces pombe. However, the mechanisms by which the Swi1-Swi3 complex regulates these processes are not well understood. Here, we report functional analyses of the Swi1-Swi3 complex in fission yeast. Swi1 possesses the DDT domain, a putative DNA binding domain found in a variety of chromatin remodeling factors. Consistently, the DDT domain-containing region of Swi1 interacts with DNA in vitro, and mutations in the DDT domain eliminate the association of Swi1 with chromatin in S. pombe cells. DDT domain mutations also render cells highly sensitive to S-phase stressing agents and induce strong accumulation of Rad22-DNA repair foci, indicating that the DDT domain is involved in the activity of the Swi1-Swi3 complex. Interestingly, DDT domain mutations also abolish Swi1's ability to interact with Swi3 in cells. Furthermore, we show that Swi1 is required for efficient chromatin association of Swi3 and that the Swi1 C-terminal domain directly interacts with Swi3. These results indicate that Swi1 associates with chromatin through its DDT domain and recruits Swi3 to function together as the replication fork protection complex.","doi":"10.1371/journal.pone.0043988","authors":"Noguchi C, Rapp JB, Skorobogatko YV, Bailey LD, Noguchi E","authors_abbrev":"Noguchi C et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-09-07","publication_year":"2012","canto_session_key":"8a099f2c6d1a0af1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-17 15:40:35","canto_approved_date":"2024-04-03 12:37:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-01 17:53:25","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.06c","SPBC30D10.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-09-17"},{"uniquename":"PMID:22685296","title":"Biological significance of nuclear localization of mitogen-activated protein kinase Pmk1 in fission yeast.","citation":"J Biol Chem 2012 Jul 27;287(31):26038-51","abstract":"Mitogen-activated protein kinase (MAPK) signaling pathways play a fundamental role in the response of eukaryotic cells to environmental changes. Also, much evidence shows that the stimulus-dependent nuclear targeting of this class of regulatory kinases is crucial for adequate regulation of distinct cellular events. In the fission yeast Schizosaccharomyces pombe, the cell integrity MAPK pathway, whose central element is the MAPK Pmk1, regulates multiple processes such as cell wall integrity, vacuole fusion, cytokinesis, and ionic homeostasis. In non-stressed cells Pmk1 is constitutively localized in both cytoplasm and nucleus, and its localization pattern appears unaffected by its activation status or in response to stress, thus questioning the biological significance of the presence of this MAPK into the nucleus. We have addressed this issue by characterizing mutants expressing Pmk1 versions excluded from the cell nucleus and anchored to the plasma membrane in different genetic backgrounds. Although nuclear Pmk1 partially regulates cell wall integrity at a transcriptional level, membrane-tethered Pmk1 performs many of the biological functions assigned to wild type MAPK like regulation of chloride homeostasis, vacuole fusion, and cellular separation. However, we found that down-regulation of nuclear Pmk1 by MAPK phosphatases induced by the stress activated protein kinase pathway is important for the fine modulation of extranuclear Pmk1 activity. These results highlight the importance of the control of MAPK activity at subcellular level.","doi":"10.1074/jbc.M112.345611","authors":"Sánchez-Mir L, Franco A, Madrid M, Vicente-Soler J, Villar-Tajadura MA, Soto T, Pérez P, Gacto M, Cansado J","authors_abbrev":"Sánchez-Mir L et al.","pubmed_publication_date":"27 Jul 2012","pubmed_entrez_date":"2012-06-12","publication_year":"2012","canto_session_key":"c7abc773ecff0380","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733418","title":"A Simple Method to Induce Meiosis and Sporulation Semisynchronously in the Fission Yeast  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Sep 01;2017(9):pdb.prot091785","abstract":" Schizosaccharomyces pombe  cells initiate a sexual differentiation program, which comprises meiosis and spore formation, on nitrogen starvation. This protocol describes a simple procedure to induce meiosis and sporulation semisynchronously in heterozygous diploid  S. pombe  cells. The procedure is appropriate for a variety of applications, including fluorescence-activated cell sorting (FACS) and northern and western blotting. Zygotic meiosis can also be induced by the same procedure, although less synchronously.","doi":"10.1101/pdb.prot091785","authors":"Yamashita A, Sakuno T, Watanabe Y, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"01 Sep 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17615301","title":"Multiple conserved domains of the nucleoporin Nup124p and its orthologs Nup1p and Nup153 are critical for nuclear import and activity of the fission yeast Tf1 retrotransposon.","citation":"Mol Biol Cell 2007 Sep;18(9):3692-708","abstract":"The nucleoporin Nup124p is a host protein required for the nuclear import of both, retrotransposon Tf1-Gag as well as the retroviral HIV-1 Vpr in fission yeast. The human nucleoporin Nup153 and the Saccharomyces cerevisiae Nup1p were identified as orthologs of Nup124p. In this study, we show that all three nucleoporins share a large FG/FXFG-repeat domain and a C-terminal peptide sequence, GRKIxxxxxRRKx, that are absolutely essential for Tf1 retrotransposition. Though the FXFG domain was essential, the FXFG repeats themselves could be eliminated without loss of retrotransposon activity, suggesting the existence of a common element unrelated to FG/FXFG motifs. The Nup124p C-terminal peptide, GRKIAVPRSRRKR, was extremely sensitive to certain single amino acid changes within stretches of the basic residues. On the basis of our comparative study of Nup124p, Nup1p, and Nup153 domains, we have developed peptides that specifically knockdown retrotransposon activity by disengaging the Tf1-Gag from its host nuclear transport machinery without any harmful consequence to the host itself. Our results imply that those domains challenged a specific pathway affecting Tf1 transposition. Although full-length Nup1p or Nup153 does not complement Nup124p, the functionality of their conserved domains with reference to Tf1 activity suggests that these three proteins evolved from a common ancestor.","authors":"Sistla S, Pang JV, Wang CX, Balasundaram D","authors_abbrev":"Sistla S et al.","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-07-07","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B1.03c","SPBC1604.08c","SPAC30D11.04c","SPCC962.03c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:38261971","title":"Checkpoint activation by Spd1: a competition-based system relying on tandem disordered PCNA binding motifs.","citation":"Nucleic Acids Res 2024 Jan 23;","abstract":"DNA regulation, replication and repair are processes fundamental to all known organisms and the sliding clamp proliferating cell nuclear antigen (PCNA) is central to all these processes. S-phase delaying protein 1 (Spd1) from S. pombe, an intrinsically disordered protein that causes checkpoint activation by inhibiting the enzyme ribonucleotide reductase, has one of the most divergent PCNA binding motifs known. Using NMR spectroscopy, in vivo assays, X-ray crystallography, calorimetry, and Monte Carlo simulations, an additional PCNA binding motif in Spd1, a PIP-box, is revealed. The two tandemly positioned, low affinity sites exchange rapidly on PCNA exploiting the same binding sites. Increasing or decreasing the binding affinity between Spd1 and PCNA through mutations of either motif compromised the ability of Spd1 to cause checkpoint activation in yeast. These results pinpoint a role for PCNA in Spd1-mediated checkpoint activation and suggest that its tandemly positioned short linear motifs create a neatly balanced competition-based system, involving PCNA, Spd1 and the small ribonucleotide reductase subunit, Suc22R2. Similar mechanisms may be relevant in other PCNA binding ligands where divergent binding motifs so far have gone under the PIP-box radar.","doi":"10.1093/nar/gkae011","authors":"Olsen JG, Prestel A, Kassem N, Broendum SS, Shamim HM, Simonsen S, Grysbæk M, Mortensen J, Rytkjær LL, Haxholm GW, Marabini R, Holmberg C, Carr AM, Crehuet R, Nielsen O, Kragelund BB","authors_abbrev":"Olsen JG et al.","pubmed_publication_date":"23 Jan 2024","pubmed_entrez_date":"2024-01-23","publication_year":"2024","canto_session_key":"1b993e4c45f765f0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-01-24 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.03","SPBC16D10.09"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"6qh1","gene_chains":[{"gene_uniquename":"SPBC16D10.09","chain":"A/B/C","position":"1-260"},{"gene_uniquename":"SPAC29B12.03","chain":"D","position":"29-38"}],"title":"The structure of Schizosaccharomyces pombe PCNA in complex with an Spd1 derived peptide","entry_authors":"Kragelund BB,Nielsen O,Olsen JG,Kassem N,Prestel A","entry_authors_abbrev":"Kragelund BB et al.","reference_uniquename":"PMID:38261971","experimental_method":"X-ray","resolution":"2.9"}]},{"uniquename":"PMID:19680287","title":"Bub1 and Bub3 promote the conversion from monopolar to bipolar chromosome attachment independently of shugoshin.","citation":"EMBO Rep 2009 Sep;10(9):1022-8","abstract":"The eukaryotic spindle assembly checkpoint (SAC) delays anaphase in the presence of chromosome attachment errors. Bub3 has been reported to be required for SAC activity in all eukaryotes examined so far. We find that Bub3, unlike its binding partner Bub1, is not essential for the SAC in fission yeast. As Bub3 is needed for the efficient kinetochore localization of Bub1, and of Mad1, Mad2 and Mad3, this implies that most SAC proteins do not need to be enriched at the kinetochores for the SAC to function. We find that Bub3 is also dispensable for shugoshin localization to the centromeres, which is the second known function of Bub1. Instead, Bub3, together with Bub1, has a specific function in promoting the conversion from chromosome mono-orientation to bi-orientation.","doi":"10.1038/embor.2009.183","authors":"Windecker H, Langegger M, Heinrich S, Hauf S","authors_abbrev":"Windecker H et al.","pubmed_publication_date":"Sep 2009","pubmed_entrez_date":"2009-08-15","publication_year":"2009","canto_session_key":"79a78f7ee5ca3dc5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silke Hauf","canto_first_approved_date":"2020-06-25 18:48:10","canto_approved_date":"2022-07-29 14:32:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-12 20:57:11","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Silke Hauf","community_curator":true,"annotation_count":31,"orcid":"0000-0001-5938-721X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.20","SPBC20F10.06","SPAC23H3.08c","SPAC15A10.15","SPCC1322.12c","SPBC3D6.04c","SPCC1795.01c","SPAC25G10.07c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2020-06-25"},{"uniquename":"PMID:33125774","title":"dnm1 deletion blocks mitochondrial fragmentation in Δfzo1 cells.","citation":"Yeast 2021 Mar;38(3):197-205","abstract":"Mitochondrial division and fusion play critical roles in maintaining functional mitochondria. Fzo1 is an outer mitochondrial membrane GTPase that played an essential role in mitochondrial fusion in budding yeast Saccharomyces cerevisiae. Here, we report the characterization of the Schizosaccharomyces pombe homologue of S. cerevisiae Fzo1p, Fzo1. Disruption of the fzo1 gene in S. pombe results in a fragmented mitochondrial morphology and a dramatically reduced growth on glycerol medium phenotype, indicating that deletion of fzo1 compromises respiratory function. Fluorescence microscopy shows that Fzo1p is located in the mitochondria. Overexpressing Fzo1 from a heterologous promoter induces mitochondrial aggregation. We also find that dnm1 mutations could both block mitochondrial fragmentation and rescue respiration growth defect in Δfzo1 single mutant cells. Our results proposed that a genetic interaction between fzo1 and a balance between division- and fusion-controlled mitochondrial shape and function in S. pombe. This study represents the first report of Fzo1 mediator of mitochondrial fusion in S. pombe.","doi":"10.1002/yea.3524","authors":"Yang Y, Hu Y, Wu L, Zhang P, Shang J","authors_abbrev":"Yang Y et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2020-10-30","publication_year":"2021","canto_session_key":"c16bb5917f987f09","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-11-01 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1706.03","SPBC12C2.08"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:106268","title":"Absence of mutagenicity of praziquantel, a new, effective, anti-schistosomal drug, in bacteria, yeasts, insects and mammalian cells.","citation":"Mutat Res 1978 Nov;58(2-3):133-42","abstract":"Praziquantel (Embay 8440, Droncit) a new, effective anti-schistosomal drug, was tested in various short-term assays that have shown a predictive value for the detection of potential carcinogens. Indicator organisms S. typhimurium strains, S. pombe, S. cerevisiae, cultured V79 Chinese hamster cells or human heteroploid cells and Drosophila melanogaster were treated with Praziquantel. The induction of reverse and forward mutations, mitotic gene conversions, X-linked recessive lethals, sister-chromatid exchanges and unscheduled DNA-repair synthesis was scored; rodent-liver microsome-, cell- and host-mediated assays were also performed. Hycanthone, another schistosomicide was included as a positive control. The absence of a genetic activity of Praziquantel uniformly observed in such a battery of tests (i) confirms the assumption that the anti-schistosomal effectiveness of this drug is not related to the mutagenic activity and (ii) should encourage the implementation of extended clinical and field trials.","authors":"Bartsch H, Kuroki T, Malaveille C, Loprieno N, Barale R, Abbondandolo A, Bonatti S, Rainaldi G, Vogel E, Davis A","authors_abbrev":"Bartsch H et al.","pubmed_publication_date":"Nov 1978","pubmed_entrez_date":"1978-11-01","publication_year":"1978","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3889548","title":"Replicating instabilities in yeast: occurrence in different mutational systems.","citation":"Mol Gen Genet 1985;199(1):152-3","abstract":"Following mutagenesis of yeast cells with nitrosoguanidine, primary mosaic colonies exhibiting prototrophic/auxotrophic phenotypes were obtained. Upon replating of these primary mosaics, numerous secondary mosaics were present in the progeny. This study shows that replicating instabilities occur at many different loci within the Schizosaccharomyces pombe genome. In addition, the ade-1 gene of Saccharomyces cerevisiae (causing red pigmentation) was used to show that the phenomenon also occurs in this yeast.","authors":"Nasim A, Stephen ER, Erratt JA","authors_abbrev":"Nasim A et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9559861","title":"Estimation of membrane potential deltapsi in reconstituted plasma membrane vesicles using a numerical model of oxonol VI distribution.","citation":"J Bioenerg Biomembr 1997 Dec;29(6):603-9","abstract":"A model of membrane potential-dependent distribution of oxonol VI to estimate the electrical potential difference deltapsi across Schizosaccharomyces pombe plasma membrane vesicles (PMV) has been developed. deltapsi was generated by the H+-ATPase reconstituted in the PMV. The model treatment was necessary since the usual calibration of the dye fluorescence changes by diffusion potentials (K+ + valinomycin) failed. The model allows for fitting of fluorescence changes at different vesicle and dye concentrations, yielding deltapsi in ATP-energized PMV of 80 mV. The described model treatment to estimate deltapsi may be applicable for other reconstituted membrane systems.","authors":"Portele A, Lenz J, Höfer M","authors_abbrev":"Portele A et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1998-04-29","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24815909","title":"Potential roles for interactions between the mitochondrial and nuclear DNA throughout the cell cycle of Schizosaccharomyces pombe.","citation":"Mitochondrion 2014 Jul;17:141-9","abstract":"Over the course of mitochondrial evolution, the majority of genes required for its function have been transferred and integrated into nuclear chromosomes. Ongoing transfer of mitochondrial DNA to the nucleus has been detected, but its functional significance has not been fully elucidated. Here by Genome Conformation Capture, we identify DNA-DNA interactions between the mitochondrial and nuclear chromosomes (mt-nDNA interactions) that vary in strength and number between the G1, G2 and M phases of the fission yeast cell cycle. Mt-nDNA interactions captured in mitotic anaphase were associated with nuclear genes required for the regulation of cell growth and energy availability. Furthermore, mt-nDNA interactions captured in the G1 phase involved high efficiency, early firing origins of DNA replication. Collectively, these results suggest functional roles for the ongoing transfer of regions of the mitochondrial genome to the nucleus.","doi":"10.1016/j.mito.2014.04.014","authors":"Grand RS, Martienssen R, O'Sullivan JM","authors_abbrev":"Grand RS et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-05-13","publication_year":"2014","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33767388","title":"Biomolecular condensates amplify mRNA decapping by biasing enzyme conformation.","citation":"Nat Chem Biol 2021 May;17(5):615-623","abstract":"Cells organize biochemical processes into biological condensates. P-bodies are cytoplasmic condensates that are enriched in enzymes important for mRNA degradation and have been identified as sites of both storage and decay. How these opposing outcomes can be achieved in condensates remains unresolved. mRNA decapping immediately precedes degradation, and the Dcp1/Dcp2 decapping complex is enriched in P-bodies. Here, we show that Dcp1/Dcp2 activity is modulated in condensates and depends on the interactions promoting phase separation. We find that Dcp1/Dcp2 phase separation stabilizes an inactive conformation in Dcp2 to inhibit decapping. The activator Edc3 causes a conformational change in Dcp2 and rewires the protein-protein interactions to stimulate decapping in condensates. Disruption of the inactive conformation dysregulates decapping in condensates. Our results indicate that the regulation of enzymatic activity in condensates relies on a coupling across length scales ranging from microns to ångstroms. We propose that this regulatory mechanism may control the functional state of P-bodies and related phase-separated compartments.","doi":"10.1038/s41589-021-00774-x","authors":"Tibble RW, Depaix A, Kowalska J, Jemielity J, Gross JD","authors_abbrev":"Tibble RW et al.","pubmed_publication_date":"May 2021","pubmed_entrez_date":"2021-03-26","publication_year":"2021","canto_session_key":"a161639df4496656","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36088506","title":"Mrz1, a Novel Mitochondrial Outer Membrane RING Finger Protein, is Degraded Through the Ubiquitin-Proteasome Pathway in Schizosaccharomyces pombe.","citation":"Curr Microbiol 2022 Sep 10;79(10):309","abstract":"The RING (Really Interesting New Gene) finger proteins are a large diverse group of Zinc finger proteins. Many determined RING finger proteins are ubiquitin-protein E3 ligases and RING E3s are the most abundant type of ubiquitin ligase. RING finger and RING finger E3s have been discovered in many organisms where they play various functions, including DNA repair, ubiquitination and mitochondrial protein quality control. In this study, we identified a novel mitochondrial protein (SPBC16G5.03) with predicted RING finger domain within an N-terminal 21-60 amino acids and named it Mrz1 (mitochondrial RING finger protein). Our results showed that Mrz1 is localized in the mitochondrial outer membrane. Deletion of mrz1 did not affect cell growth in an unstressed state, but increases sensitivity to selenite. We showed that Mrz1 was degraded during the stationary phase and blocked by addition proteasome inhibitor MG132. We further showed that the E2 enzyme Ubc13 was identified among 8 candidate proteins as the ubiquitin-conjugating enzyme in this system. These data suggested that the Mrz1 was degraded likely through the ubiquitin-proteasome system.","doi":"10.1007/s00284-022-02998-z","authors":"Liu Z, Zhang P, Li M, A L, Yang G, Yu Y, Lu H, Shang J, Huang Y","authors_abbrev":"Liu Z et al.","pubmed_publication_date":"10 Sep 2022","pubmed_entrez_date":"2022-09-10","publication_year":"2022","canto_session_key":"3456bd4243b2feac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2023-11-10 14:22:03","canto_approved_date":"2023-11-10 14:22:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-10 05:27:47","canto_added_date":"2022-09-14 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.04c","SPBC16G5.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-11-10"},{"uniquename":"PMID:35974206","title":"A context-dependent and disordered ubiquitin-binding motif.","citation":"Cell Mol Life Sci 2022 Aug 16;79(9):484","abstract":"Ubiquitin is a small, globular protein that is conjugated to other proteins as a posttranslational event. A palette of small, folded domains recognizes and binds ubiquitin to translate and effectuate this posttranslational signal. Recent computational studies have suggested that protein regions can recognize ubiquitin via a process of folding upon binding. Using peptide binding arrays, bioinformatics, and NMR spectroscopy, we have uncovered a disordered ubiquitin-binding motif that likely remains disordered when bound and thus expands the palette of ubiquitin-binding proteins. We term this motif Disordered Ubiquitin-Binding Motif (DisUBM) and find it to be present in many proteins with known or predicted functions in degradation and transcription. We decompose the determinants of the motif showing it to rely on features of aromatic and negatively charged residues, and less so on distinct sequence positions in line with its disordered nature. We show that the affinity of the motif is low and moldable by the surrounding disordered chain, allowing for an enhanced interaction surface with ubiquitin, whereby the affinity increases ~ tenfold. Further affinity optimization using peptide arrays pushed the affinity into the low micromolar range, but compromised context dependence. Finally, we find that DisUBMs can emerge from unbiased screening of randomized peptide libraries, featuring in de novo cyclic peptides selected to bind ubiquitin chains. We suggest that naturally occurring DisUBMs can recognize ubiquitin as a posttranslational signal to act as affinity enhancers in IDPs that bind to folded and ubiquitylated binding partners.","doi":"10.1007/s00018-022-04486-w","authors":"Dreier JE, Prestel A, Martins JM, Brøndum SS, Nielsen O, Garbers AE, Suga H, Boomsma W, Rogers JM, Hartmann-Petersen R, Kragelund BB","authors_abbrev":"Dreier JE et al.","pubmed_publication_date":"16 Aug 2022","pubmed_entrez_date":"2022-08-16","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.03","SPBC17D11.07c","SPBC337.08c","SPBP19A11.03c","SPAC3G6.02","SPAC19D5.04"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:9268024","title":"Characterisation of the Schizosaccharomyces pombe rad4/cut5 mutant phenotypes: dissection of DNA replication and G2 checkpoint control function.","citation":"Mol Gen Genet 1997 Jul;255(3):332-40","abstract":"Mutation of the essential Schizosaccharomyces pombe rad4/cut5 gene causes sensitivity to UV and ionising radiation at the permissive temperature whilst at the restrictive temperature cells fail to undergo DNA replication but still attempt mitosis owing to a defective S-phase checkpoint response. Many mutations in genes encoding DNA replication proteins also abolish checkpoint responses, possibly because the replication machinery is a pre-requisite for the generation of the signal. We demonstrate here that rad4/cut5 cells fail to arrest cell division when treated with the replication inhibitor hydroxyurea at the semi-permissive temperature 32 degrees C, but retain essentially normal replicative capacity. This demonstrates that the replication and checkpoint function of the rad4/cut5 gene product can be separated and that the Rad4 protein differs from other replication proteins in being directly involved in generating the S-phase checkpoint signal. Furthermore, we have investigated the checkpoint response or rad4/cut5-deficient cells to gamma-irradiation and UV-mimetic drugs. We find that, at the restrictive temperature, the rad4-/cut5- cells fail to delay mitosis in response to gamma-irradiation whilst retaining a normal checkpoint response to the UV-mimetic drug 4-nitroquinoline-1-oxide. The lack of the gamma-irradiation checkpoint is reminiscent of the deficiency associated with mutation of the human ATM locus, the causative deficiency of the heritable disorder ataxia telangiectasia. The implications of our results for the organisation of distinct checkpoint-response pathways in both fission yeast and mammalian cells are discussed. Moreover the data are consistent with a model in which the generation of the S-Phase checkpoint signal is DNA polymerase epsilon dependent.","authors":"McFarlane RJ, Carr AM, Price C","authors_abbrev":"McFarlane RJ et al.","pubmed_publication_date":"Jul 1997","pubmed_entrez_date":"1997-07-01","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.18c","SPAC1F7.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:38884719","title":"Posttranscriptional Regulation by Proteins and Noncoding RNAs.","citation":"Adv Exp Med Biol 2024;1441:313-339","abstract":"Posttranscriptional regulation comprises those mechanisms occurring after the initial copy of the DNA sequence is transcribed into an intermediate RNA molecule (i.e., messenger RNA) until such a molecule is used as a template to generate a protein. A subset of these posttranscriptional regulatory mechanisms essentially are destined to process the immature mRNA toward its mature form, conferring the adequate mRNA stability, providing the means for pertinent introns excision, and controlling mRNA turnover rate and quality control check. An additional layer of complexity is added in certain cases, since discrete nucleotide modifications in the mature RNA molecule are added by RNA editing, a process that provides large mature mRNA diversity. Moreover, a number of posttranscriptional regulatory mechanisms occur in a cell- and tissue-specific manner, such as alternative splicing and noncoding RNA-mediated regulation. In this chapter, we will briefly summarize current state-of-the-art knowledge of general posttranscriptional mechanisms, while major emphases will be devoted to those tissue-specific posttranscriptional modifications that impact on cardiac development and congenital heart disease.","doi":"10.1007/978-3-031-44087-8_17","authors":"Aranega AE, Franco D","authors_abbrev":"Aranega AE et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-06-17","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-06-17 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31042107","title":"Generation of temperature sensitive mutations with error-prone PCR in a gene encoding a component of the spindle pole body in fission yeast.","citation":"Biosci Biotechnol Biochem 2019 Sep;83(9):1717-1720","abstract":"Temperature-sensitive (ts) mutants provide powerful tools for investigation of cellular functions of essential genes. We report here asimple procedure to generate ts mutations using error-prone PCR within  pcp1  that encodes aspindle pole body (SPB) component in  Schizosaccharomyces pombe . This manipulation is not restricted to  pcp1 , and can be suited to any essential genes involved in other processes.","doi":"10.1080/09168451.2019.1611414","authors":"Tang NH, Fong CS, Masuda H, Jourdain I, Yukawa M, Toda T","authors_abbrev":"Tang NH et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-05-02","publication_year":"2019","canto_session_key":"412130e56f14334c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2019-05-18 10:08:37","canto_approved_date":"2019-06-06 12:29:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-18 07:30:43","canto_added_date":"2019-05-03 00:15:04","annotation_curators":[{"name":"Takashi Toda","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-05-18"},{"uniquename":"PMID:28338873","title":"Molecular dissection of the actin-binding ability of the fission yeast α-actinin, Ain1, in vitro and in vivo.","citation":"J Biochem 2017 Aug 01;162(2):93-102","abstract":"A contractile ring (CR) is involved in cytokinesis in animal and yeast cells. Although several types of actin-bundling proteins associate with F-actin in the CR, their individual roles in the CR have not yet been elucidated in detail. Ain1 is the sole α-actinin homologue in the fission yeast Schizosaccharomyces pombe and specifically localizes to the CR with a high turnover rate. S. pombe cells lacking the ain1+ gene show defects in cytokinesis under stress conditions. We herein investigated the biochemical activity and cellular localization mechanisms of Ain1. Ain1 showed weaker affinity to F-actin in vitro than other actin-bundling proteins in S. pombe. We identified a mutation that presumably loosened the interaction between two calponin-homology domains constituting the single actin-binding domain (ABD) of Ain1, which strengthened the actin-binding activity of Ain1. This mutant protein induced a deformation in the ring shape of the CR. Neither a truncated protein consisting only of an N-terminal ABD nor a truncated protein lacking a C-terminal region containing an EF-hand motif localized to the CR, whereas the latter was involved in the bundling of F-actin in vitro. We herein propose detailed mechanisms for how each part of the molecule is involved in the proper cellular localization and function of Ain1.","doi":"10.1093/jb/mvx008","authors":"Morita R, Takaine M, Numata O, Nakano K","authors_abbrev":"Morita R et al.","pubmed_publication_date":"01 Aug 2017","pubmed_entrez_date":"2017-03-25","publication_year":"2017","canto_session_key":"1ad0c6a096c036ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rikuri Morita","canto_first_approved_date":"2021-06-10 10:55:04","canto_approved_date":"2025-05-27 15:09:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-27 06:40:53","canto_added_date":"2017-03-27 00:15:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":30,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Rikuri Morita","community_curator":true,"annotation_count":8,"orcid":"0000-0002-0465-5528","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.08","SPBC32H8.12c","SPAC19G12.14"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2021-06-10"},{"uniquename":"PMID:25961982","title":"The epigenetic regulation of autonomous replicons.","citation":"Biomol Concepts 2010 May 01;1(1):17-30","abstract":"The discovery of autonomous replicating sequences (ARSs) in Saccharomyces cerevisiae in 1979 was considered a milestone in unraveling the regulation of replication in eukaryotic cells. However, shortly afterwards it became obvious that in Saccharomyces pombe and all other higher organisms ARSs were not sufficient to initiate independent replication. Understanding the mechanisms of replication is a major challenge in modern cell biology and is also a prerequisite to developing application-oriented autonomous replicons for gene therapeutic treatments. This review will focus on the development of non-viral episomal vectors, their use in gene therapeutic applications and our current knowledge about their epigenetic regulation.","doi":"10.1515/bmc.2010.009","authors":"Hagedorn C, Lipps HJ, Rupprecht S","authors_abbrev":"Hagedorn C et al.","pubmed_publication_date":"01 May 2010","pubmed_entrez_date":"2015-05-12","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-05-14 00:19:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24327658","title":"Casein kinase 1 regulates sterol regulatory element-binding protein (SREBP) to control sterol homeostasis.","citation":"J Biol Chem 2014 Jan 31;289(5):2725-35","abstract":"Sterol homeostasis is tightly controlled by the sterol regulatory element-binding protein (SREBP) transcription factor that is highly conserved from fungi to mammals. In fission yeast, SREBP functions in an oxygen-sensing pathway to promote adaptation to decreased oxygen supply that limits oxygen-dependent sterol synthesis. Low oxygen stimulates proteolytic cleavage of the SREBP homolog Sre1, generating the active transcription factor Sre1N that drives expression of sterol biosynthetic enzymes. In addition, low oxygen increases the stability and DNA binding activity of Sre1N. To identify additional signals controlling Sre1 activity, we conducted a genetic overexpression screen. Here, we describe our isolation and characterization of the casein kinase 1 family member Hhp2 as a novel regulator of Sre1N. Deletion of Hhp2 increases Sre1N protein stability and ergosterol levels in the presence of oxygen. Hhp2-dependent Sre1N degradation by the proteasome requires Hhp2 kinase activity, and Hhp2 binds and phosphorylates Sre1N at specific residues. Our results describe a role for casein kinase 1 as a direct regulator of sterol homeostasis. Given the role of mammalian Hhp2 homologs, casein kinase 1δ and 1ε, in regulation of the circadian clock, these findings may provide a mechanism for coordinating circadian rhythm and lipid metabolism.","doi":"10.1074/jbc.M113.511899","authors":"Brookheart RT, Lee CY, Espenshade PJ","authors_abbrev":"Brookheart RT et al.","pubmed_publication_date":"31 Jan 2014","pubmed_entrez_date":"2013-12-12","publication_year":"2014","canto_session_key":"83dde591569634d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2016-05-30 22:45:14","canto_approved_date":"2025-09-03 18:06:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-27 09:15:39","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Peter Espenshade","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.09","SPAC6B12.12","SPAC23C4.12","SPBC6B1.08c","SPBC1861.01c","SPAC222.11"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2016-05-30"},{"uniquename":"PMID:11071922","title":"A fission yeast homolog of Int-6, the mammalian oncoprotein and eIF3 subunit, induces drug resistance when overexpressed.","citation":"Mol Biol Cell 2000 Nov;11(11):3993-4003","abstract":"Through a screen to identify genes that induce multi-drug resistance when overexpressed, we have identified a fission yeast homolog of Int-6, a component of the human translation initiation factor eIF3. Disruption of the murine Int-6 gene by mouse mammary tumor virus (MMTV) has been implicated previously in tumorigenesis, although the underlying mechanism is not yet understood. Fission yeast Int6 was shown to interact with other presumptive components of eIF3 in vivo, and was present in size fractions consistent with its incorporation into a 43S translation preinitiation complex. Drug resistance induced by Int6 overexpression was dependent on the AP-1 transcription factor Pap1, and was associated with increased abundance of Pap1-responsive mRNAs, but not with Pap1 relocalization. Fission yeast cells lacking the int6 gene grew slowly. This growth retardation could be corrected by the expression of full length Int6 of fission yeast or human origin, or by a C-terminal fragment of the fission yeast protein that also conferred drug resistance, but not by truncated human Int-6 proteins corresponding to the predicted products of MMTV-disrupted murine alleles. Studies in fission yeast may therefore help to explain the ways in which Int-6 function can be perturbed during MMTV-induced mammary tumorigenesis.","authors":"Crane R, Craig R, Murray R, Dunand-Sauthier I, Humphrey T, Norbury C","authors_abbrev":"Crane R et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-11-10","publication_year":"2000","canto_session_key":"92e79844622a1b42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-02 16:15:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-13 10:41:59","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPBC3F6.03","SPBC646.09c","SPAC25G10.08","SPAC4D7.05","SPAC3C7.14c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2014-10-13"},{"uniquename":"PMID:19363481","title":"Molecular mimicry of SUMO promotes DNA repair.","citation":"Nat Struct Mol Biol 2009 May;16(5):509-16","abstract":"Rad60 family members contain functionally enigmatic, integral SUMO-like domains (SLDs). We show here that despite their divergence from SUMO, each Rad60 SLD interacts with a subset of SUMO pathway enzymes: SLD2 specifically binds the SUMO E2 conjugating enzyme (Ubc9), whereas SLD1 binds the SUMO E1 (Fub2, also called Uba2) activating and E3 (Pli1, also called Siz1 and Siz2) specificity enzymes. The molecular basis of this selectivity is revealed by our 0.97-A resolution crystal structure of Rad60 SLD2, which shows that apart from the conserved non-substrate SUMO:Ubc9 interface, the surface features of SLD2 are distinct from those of SUMO. Abrogation of the SLD2:Ubc9 FEG motif-dependent interaction results in hypersensitivity to genotoxic stress and an increase in spontaneous recombination associated with aberrant replication forks. Our results provide a mechanistic basis for the near-synonymous roles of Rad60 and SUMO in survival of genotoxic stress and suggest unprecedented DNA-damage-response functions for SLDs in regulating sumoylation.","doi":"10.1038/nsmb.1582","authors":"Prudden J, Perry JJ, Arvai AS, Tainer JA, Boddy MN","authors_abbrev":"Prudden J et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-04-14","publication_year":"2009","canto_session_key":"84dc6f3caefc7153","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-01 13:31:09","canto_approved_date":"2023-04-18 18:42:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-01 13:28:23","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.05c","SPAC17A5.07c","SPAC644.14c","SPAC1687.05","SPBC1921.02","SPBC3D6.11c","SPAC16A10.06c","SPAC11E3.08c","SPAC30D11.13","SPBC16H5.03c","SPAC2G11.12"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2023-03-01","pdb_entries":[{"pdb_id":"3goe","gene_chains":[{"gene_uniquename":"SPBC1921.02","chain":"A","position":"332-406"}],"title":"Molecular Mimicry of SUMO promotes DNA repair","entry_authors":"Perry JJP","entry_authors_abbrev":"Perry JJP","reference_uniquename":"PMID:19363481","experimental_method":"X-ray","resolution":"0.97"}]},{"uniquename":"PMID:8371982","title":"The fission yeast prp4+ gene involved in pre-mRNA splicing codes for a predicted serine/threonine kinase and is essential for growth.","citation":"Nucleic Acids Res 1993 Aug 25;21(17):4079-83","abstract":"Only four prp (pre-mRNA processing) genes of the fission yeast Schizosaccharomyces pombe have been reported. We exploited yeast genetics and identified and isolated the prp4 gene. Sequence analysis revealed that the splicing factor encoded by this gene contains the signature sequences that define the serine/threonine protein kinase family. This is the first kinase gene identified whose product is involved in pre-mRNA splicing. The prp4 gene contains one intron in the kinase domain. Gene replacement studies provided evidence that this gene is essential for growth and is located on chromosome III.","authors":"Alahari SK, Schmidt H, Käufer NF","authors_abbrev":"Alahari SK et al.","pubmed_publication_date":"25 Aug 1993","pubmed_entrez_date":"1993-08-25","publication_year":"1993","canto_session_key":"fcc0142cbab8adf6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 16:28:42","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-20 15:09:57","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-20"},{"uniquename":"PMID:34520548","title":"Fission yeast Stn1 maintains stability of repetitive DNA at subtelomere and ribosomal DNA regions.","citation":"Nucleic Acids Res 2021 Oct 11;49(18):10465-10476","abstract":"Telomere binding protein Stn1 forms the CST (Cdc13/CTC1-STN1-TEN1) complex in budding yeast and mammals. Likewise, fission yeast Stn1 and Ten1 form a complex indispensable for telomere protection. We have previously reported that stn1-1, a high-temperature sensitive mutant, rapidly loses telomere DNA at the restrictive temperature due to frequent failure of replication fork progression at telomeres and subtelomeres, both containing repetitive sequences. It is unclear, however, whether Stn1 is required for maintaining other repetitive DNAs such as ribosomal DNA. In this study, we have demonstrated that stn1-1 cells, even when grown at the permissive temperature, exhibited dynamic rearrangements in the telomere-proximal regions of subtelomere and ribosomal DNA repeats. Furthermore, Rad52 and γH2A accumulation was observed at ribosomal DNA repeats in the stn1-1 mutant. The phenotypes exhibited by the stn1-1 allele were largely suppressed in the absence of Reb1, a replication fork barrier-forming protein, suggesting that Stn1 is involved in the maintenance of the arrested replication forks. Collectively, we propose that Stn1 maintains the stability of repetitive DNAs at subtelomeres and rDNA regions.","doi":"10.1093/nar/gkab767","authors":"Yamamoto I, Nakaoka H, Takikawa M, Tashiro S, Kanoh J, Miyoshi T, Ishikawa F","authors_abbrev":"Yamamoto I et al.","pubmed_publication_date":"11 Oct 2021","pubmed_entrez_date":"2021-09-14","publication_year":"2021","canto_session_key":"9986bfe2ea6610b8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-09-16 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18592595","title":"A general model for aerobic yeast growth: batch growth.","citation":"Biotechnol Bioeng 1990 Apr 15;35(9):907-20","abstract":"A general model for aerobic yeast growth in batch culture is presented. It is based on the concept that the aerobic metabolism of all yeasts is determined by the relative sizes of the transport rate of sugar into the cell and the transport rate of respiratory intermediates into the mitochondrion. If the rate of sugar uptake rate exceeds the rate of transport of respiratory intermediates into the mitochondrion (as in Saccharomyces cerevisiae, S. uvarum, and S. pombe), the metabolism exhibits the features of ethanol excretion and limited specific oxygen uptake rate. If the rate of transport of respiratory intermediates into the mitochondrion is of the same order as the transport of sugar into the cell (as in Candida utilis), the metabolism is characterized by little or no ethanol excretion and a much higher specific oxygen uptake rate. Batch data from an extensive range of yeast and carbon sources is used to illustrate the use of this model. The ability of this model to fit such an extensive range of experimental data suggests that it can be used as a generalized model for aerobic yeast growth.","authors":"Barford JP","authors_abbrev":"Barford JP","pubmed_publication_date":"15 Apr 1990","pubmed_entrez_date":"1990-04-15","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16483310","title":"Genetic and functional interaction between Ryh1 and Ypt3: two Rab GTPases that function in S. pombe secretory pathway.","citation":"Genes Cells 2006 Mar;11(3):207-21","abstract":"We have previously isolated ypt3-i5 mutant and showed that Ypt3 GTPase functions in the fission yeast secretory pathway. Here, the same genetic screen led to the isolation of ryh1-i6, a mutant allele of the ryh1+ gene encoding a homolog of Rab6. The ryh1-i6 mutant showed phenotypes that support its role in retrograde traffic from endosome to the Golgi. Interestingly, ryh1+ gene deletion was synthetically lethal with ypt3-i5 mutation. Consistently, the over-expression of the GDP-conformational mutant, Ryh1T25 N, inhibited the growth of ypt3-i5 mutant but had no effect on that of wild-type cells. Furthermore, the over-expression of the Ryh1T25N mutant inhibited the acid phosphatase glycosylation and exacerbated the cell wall integrity of ypt3-i5 mutant, but had no effect on those of wild-type cells. GFP-Ryh1 and GFP-Ypt3 both localized at the Golgi/endosome, but showed distinct subcellular localizations. The localization of GFP-Ryh1 in ypt3-i5 mutant and that of GFP-Ypt3 in ryh1-i6 mutant were distinct from those in wild-type cells. In addition, Ryh1 as well as Ypt3 were shown to be involved in acid phosphatase secretion. These results suggest that Ryh1 is involved in the secretory pathway and may have a potential overlapping function with Ypt3 in addition to its role in recycling.","authors":"He Y, Sugiura R, Ma Y, Kita A, Deng L, Takegawa K, Matsuoka K, Shuntoh H, Kuno T","authors_abbrev":"He Y et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-02-18","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.03","SPBC13G1.11","SPAC4C5.02c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:19547744","title":"Evolution of phosphoregulation: comparison of phosphorylation patterns across yeast species.","citation":"PLoS Biol 2009 Jun 16;7(6):e1000134","abstract":"The extent by which different cellular components generate phenotypic diversity is an ongoing debate in evolutionary biology that is yet to be addressed by quantitative comparative studies. We conducted an in vivo mass-spectrometry study of the phosphoproteomes of three yeast species (Saccharomyces cerevisiae, Candida albicans, and Schizosaccharomyces pombe) in order to quantify the evolutionary rate of change of phosphorylation. We estimate that kinase-substrate interactions change, at most, two orders of magnitude more slowly than transcription factor (TF)-promoter interactions. Our computational analysis linking kinases to putative substrates recapitulates known phosphoregulation events and provides putative evolutionary histories for the kinase regulation of protein complexes across 11 yeast species. To validate these trends, we used the E-MAP approach to analyze over 2,000 quantitative genetic interactions in S. cerevisiae and Sc. pombe, which demonstrated that protein kinases, and to a greater extent TFs, show lower than average conservation of genetic interactions. We propose therefore that protein kinases are an important source of phenotypic diversity.","doi":"10.1371/journal.pbio.1000134","authors":"Beltrao P, Trinidad JC, Fiedler D, Roguev A, Lim WA, Shokat KM, Burlingame AL, Krogan NJ","authors_abbrev":"Beltrao P et al.","pubmed_publication_date":"16 Jun 2009","pubmed_entrez_date":"2009-06-24","publication_year":"2009","canto_session_key":"ab3c4e4feea56db4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-23 17:42:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-23 17:02:29","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val 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dividing cells of the fission yeast schizosaccharomyces pombe do age.","citation":"Biogerontology 2006 Aug;7(4):261-7","abstract":"Theories of the evolution of senescence state that symmetrically dividing organisms do not senesce. However, this view is challenged by experimental evidence. We measured by immunofluorescence the occurrence and intensity of protein carbonylation in single and symmetrically dividing cells of Schizosaccharomyces pombe. Cells of S. pombe show different levels of carbonylated proteins. Most cells have little damage, a few show a lot, an observation consistent with the gradual accumulation of carbonylation over time. At reproduction, oxidized proteins are shared between the two resulting cells. These results indicate that S. pombe does age, but does so in a different way from other studied species. Damaged cells give rise to damaged cells. The fact that cells with no or few carbonylated proteins constitute the main part of the population can explain why, although age is not reset to zero in one of the cells during division, the pool of young cells remains large enough to prevent the rapid extinction of the population.","authors":"Minois N, Frajnt M, Dölling M, Lagona F, Schmid M, Küchenhoff H, Gampe J, Vaupel JW","authors_abbrev":"Minois N et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-07-06","publication_year":"2006","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21030440","title":"Meiotic recombination protein Rec12: functional conservation, crossover homeostasis and early crossover/non-crossover decision.","citation":"Nucleic Acids Res 2011 Mar;39(4):1460-72","abstract":"In fission yeast and other eukaryotes, Rec12 (Spo11) is thought to catalyze the formation of dsDNA breaks (DSBs) that initiate homologous recombination in meiosis. Rec12 is orthologous to the catalytic subunit of topoisomerase VI (Top6A). Guided by the crystal structure of Top6A, we engineered the rec12 locus to encode Rec12 proteins each with a single amino acid substitution in a conserved residue. Of 21 substitutions, 10 significantly reduced or abolished meiotic DSBs, gene conversion, crossover recombination and the faithful segregation of chromosomes. Critical residues map within the metal ion-binding pocket toprim (E179A, D229A, D231A), catalytic region 5Y-CAP (R94A, D95A, Y98F) and the DNA-binding interface (K201A, G202E, R209A, K242A). A subset of substitutions reduced DSBs but maintained crossovers, demonstrating crossover homeostasis. Furthermore, a strong separation of function mutation (R304A) suggests that the crossover/non-crossover decision is established early by a protein-protein interaction surface of Rec12. Fission yeast has multiple crossovers per bivalent, and chromosome segregation was robust above a threshold of about one crossover per bivalent, below which non-disjunction occurred. These results support structural and functional conservation among Rec12/Spo11/Top6A family members for the catalysis of DSBs, and they reveal how Rec12 regulates other features of meiotic chromosome dynamics.","doi":"10.1093/nar/gkq993","authors":"Kan F, Davidson MK, Wahls WP","authors_abbrev":"Kan F et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2010-10-30","publication_year":"2011","canto_session_key":"54720864f1195f6b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12109159","title":"Genetics of sulphate assimilation in Schizosaccharomyces pombe (a short review).","citation":"Acta Microbiol Immunol Hung 2002;49(2-3):279-83","abstract":"Sulphur plays an important role in yeasts, especially in the biosynthesis of methionine and cysteine. The inorganic sulphur source, sulphate, is taken up by the cells via the sulphate-permease(s). After its transport, it is activated and subsequently reduced to sulphide or serves as a donor for sulphurylation reactions. Selenate anion (SeO4(2-)), which has the same metabolic pathway as sulphate, is toxic for the cells of Schizosaccharomyces pombe. We isolated selenate resistant mutants which cannot utilize sulphate, therefore they need organic sulphur source for growth. One of the selenate resistant mutants was successively transformed with S. pombe genomic libraries and the gene complementing the selenate resistance was identified as that of coding for the ATP-sulphurylase enzyme.","authors":"Simonics T, Bánszky L, Maráz A","authors_abbrev":"Simonics T et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-07-12","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11472912","title":"Decrease in cell surface galactose residues of Schizosaccharomyces pombe enhances its coflocculation with Pediococcus damnosus.","citation":"Appl Environ Microbiol 2001 Aug;67(8):3413-7","abstract":"Pediococcus damnosus can coflocculate with Saccharomyces cerevisiae and cause beer acidification that may or may not be desired. Similar coflocculations occur with other yeasts except for Schizosaccharomyces pombe which has galactose-rich cell walls. We compared coflocculation rates of S. pombe wild-type species TP4-1D, having a mannose-to-galactose ratio (Man:Gal) of 5 to 6 in the cell wall, with its glycosylation mutants gms1-1 (Man:Gal = 5:1) and gms1Delta (Man:Gal = 1:0). These mutants coflocculated at a much higher level (30 to 45%) than that of the wild type (5%). Coflocculation of the mutants was inhibited by exogenous mannose but not by galactose. The S. cerevisiae mnn2 mutant, with a mannan content similar to that of gms1Delta, also showed high coflocculation (35%) and was sensitive to mannose inhibition. Coflocculation of P. damnosus and gms1Delta (or mnn2) also could be inhibited by gms1Delta mannan (with unbranched alpha-1,6-linked mannose residues), concanavalin A (mannose and glucose specific), or NPA lectin (specific for alpha-1,6-linked mannosyl units). Protease treatment of the bacterial cells completely abolished coflocculation. From these results we conclude that mannose residues on the cell surface of S. pombe serve as receptors for a P. damnosus lectin but that these receptors are shielded by galactose residues in wild-type strains. Such interactions are important in the production of Belgian acid types of beers in which mixed cultures are used to improve flavor.","authors":"Peng X, Sun J, Michiels C, Iserentant D, Verachtert H","authors_abbrev":"Peng X et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-07-27","publication_year":"2001","canto_session_key":"4848741850c276d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-28 10:20:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-28 10:19:54","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-02-28"},{"uniquename":"PMID:11732635","title":"Characterization of a fission yeast mutant which displays defects in cell wall integrity and cytokinesis.","citation":"Genes Genet Syst 2001 Aug;76(4):257-69","abstract":"The fission yeast cps6-153 mutant was originally isolated based on its hypersensitivity to the spindle poison isopropyl N-3-chlorophenyl carbamate (CIPC). The mutant also shows defects in both cell wall integrity and cytokinesis, resulting in the accumulation of unseparated cells with weakened cell walls. The arrested cells display a disoriented alignment of cytoplasmic microtubules. When the mutant cells are cultivated at high temperature (35 degrees C), both cell walls and septa become very thick. Electron microscopy revealed the disorganized structure of the thickened cell walls and septa, in which fibrillar components were not completely masked with an amorphous matrix. rad25+ was cloned from a genomic library by complementation of the mutant phenotypes, suggesting the involvement of Rad25p, one of two 14-3-3 proteins in S. pombe, in the pathway of cell wall integrity and cytokinesis.","authors":"Ishiguro J, Shimada S, Gabriel M, Kopecká M","authors_abbrev":"Ishiguro J et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-12-06","publication_year":"2001","canto_session_key":"697b47c53465d4e9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-09-14 03:20:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-14 03:20:21","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A2.13c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2017-09-14"},{"uniquename":"GO_REF:0000002","title":"Comments","abstract":"Transitive assignment of GO terms based on InterPro classification. For any database entry (representing a protein or protein-coding gene) that has been annotated with one or more InterPro domains, the corresponding GO terms are obtained from a translation table of InterPro entries to GO terms (interpro2go) generated manually by the InterPro team at EBI. The mapping file is available at http://www.geneontology.org/external2go/interpro2go.","authors":"DDB, FB, MGI, GOA, ZFIN 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and transcription factors do the nucleocytoplasmic tango.","citation":"Genes Dev 1998 May 15;12(10):1391-7","abstract":"","authors":"Wilkinson MG, Millar JB","authors_abbrev":"Wilkinson MG et al.","pubmed_publication_date":"15 May 1998","pubmed_entrez_date":"1998-05-29","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18489912","title":"A yeast PAF acetylhydrolase ortholog suppresses oxidative death.","citation":"Free Radic Biol Med 2008 Aug 15;45(4):434-42","abstract":"Phospholipids containing sn-2 polyunsaturated fatty acyl residues are primary targets of oxidizing radicals, producing proapoptotic and membrane perturbing fragmented phospholipids. The only known phospholipases that specifically select these oxidized and/or short-chained phospholipids as substrates are mammalian group VII phospholipases A2s that were purified and cloned as PAF acetylhydrolases. Platelet-activating factor (PAF) is a short-chained phospholipid, and whether these enzymes actually are PAF hydrolases or evolved as oxidized phospholipid phospholipases is unknown. The fission yeast Schizosaccharomyces pombe, which does not form or use PAF as a signaling molecule, contains an open-reading frame potentially homologous to mammalian group VII phospholipase A2s. We cloned this SPBC106.11c locus and expressed it in distantly related Saccharomyces cerevisiae that lack homologous sequences. The S. pombe locus encoded a functional phospholipase A2, now renamed plg7+, that hydrolyzed PAF and a synthetic oxidized phospholipid. Expression of human type II PAF acetylhydrolase or S. pombe Plg7p enhanced the viability of S. cerevisiae subjected to oxidative stress. We conclude that a single-celled organism with an exceedingly spare genome still expresses an unusually discriminating phospholipase A2, and that selective hydrolysis of phospholipid oxidation products is an early, and critical, way to overcome oxidative membrane damage and oxidant-induced cell death.","doi":"10.1016/j.freeradbiomed.2008.04.034","authors":"Foulks JM, Weyrich AS, Zimmerman GA, McIntyre TM","authors_abbrev":"Foulks JM et al.","pubmed_publication_date":"15 Aug 2008","pubmed_entrez_date":"2008-05-21","publication_year":"2008","canto_session_key":"f96f905bc49f57b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-07 14:50:38","canto_approved_date":"2021-10-06 15:54:03","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-05 15:24:18","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-07"},{"uniquename":"PMID:18418055","title":"Protein complexes at the microtubule organizing center regulate bipolar spindle assembly.","citation":"Cell Cycle 2008 May 01;7(9):1246-53","abstract":"Bipolar spindle assembly is essential to genomic stability in dividing cells. Centrosomes or spindle pole bodies duplicated earlier at G(1)/S remain adjacent until triggered at mitotic onset to become bipolar. Pole reorientation is stabilized by microtubule interdigitation but mechanistic details for bipolarity remain incomplete. To investigate the contribution of spindle pole microtubule organizing center (MTOC) proteins in bipolarity, we applied genetic, structural and molecular biochemical analysis along with timelapse microscopy. Spindle formation was followed by an in vivo growth assay with the conditional allele cut7-22(ts), encoding fission yeast mitotic Kinesin-5, essential for bipolarity. By analysis of double and triple mutant strains of MTOC alleles and cut7-22(ts) we found that stabilized microtubules or increased bundling can rescue cut7-22(ts) associated bipolarity defects. These changes to microtubule dynamics and organization occurred through two surface domains on gamma-tubulin, a helix 11 domain and an adjacent site for binding MTOC protein Alp4. We demonstrate that Kinesin-14 Pkl1, known to oppose bipolarity, can bind to gamma-tubulin at helix 11 and that mutation of either of two conserved residues in helix 11 can impair Kinesin-14 binding. Altering the Alp4/gamma-tubulin interaction, conserved residues in helix 11 or deletion of pkl1 each are sufficient to rescue bipolarity in our cut7-22(ts) strain. Our findings provide novel insights into regulation of the bipolar mechanism through the MTOC complex.","authors":"Rodriguez AS, Batac J, Killilea AN, Filopei J, Simeonov DR, Lin I, Paluh JL","authors_abbrev":"Rodriguez AS et al.","pubmed_publication_date":"01 May 2008","pubmed_entrez_date":"2008-04-18","publication_year":"2008","canto_session_key":"2679a8daf1f7a180","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-16 16:17:34","canto_approved_date":"2020-07-10 14:41:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-14 15:56:00","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":42,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPAC3A11.14c","SPBC365.15","SPBC428.20c","SPAC25G10.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-11-16"},{"uniquename":"PMID:22095079","title":"The double-bromodomain proteins Bdf1 and Bdf2 modulate chromatin structure to regulate S-phase stress response in Schizosaccharomyces pombe.","citation":"Genetics 2012 Feb;190(2):487-500","abstract":"Bromodomain proteins bind acetylated histones to regulate transcription. Emerging evidence suggests that histone acetylation plays an important role in DNA replication and repair, although its precise mechanisms are not well understood. Here we report studies of two double bromodomain-containing proteins, Bdf1 and Bdf2, in fission yeast. Loss of Bdf1 or Bdf2 led to a reduction in the level of histone H4 acetylation. Both bdf1Δ and bdf2Δ cells showed sensitivity to DNA damaging agents, including camptothecin, that cause replication fork breakage. Consistently, Bdf1 and Bdf2 were important for recovery of broken replication forks and suppression of DNA damage. Surprisingly, deletion of bdf1 or bdf2 partially suppressed sensitivity of various checkpoint mutants including swi1Δ, mrc1Δ, cds1Δ, crb2Δ, chk1Δ, and rad3Δ, to hydroxyurea, a compound that stalls replication forks and activates the Cds1-dependent S-phase checkpoint. This suppression was not due to reactivation of Cds1. Instead, we found that bdf2 deletion alleviates DNA damage accumulation caused by defects in the DNA replication checkpoint. We also show that hydroxyurea sensitivity of mrc1Δ and swi1Δ was suppressed by mutations in histone H4 acetyltransferase subunits or histone H4. These results suggest that the double bromodomain-containing proteins modulate chromatin structure to coordinate DNA replication and S-phase stress response.","doi":"10.1534/genetics.111.135459","authors":"Garabedian MV, Noguchi C, Ziegler MA, Das MM, Singh T, Harper LJ, Leman AR, Khair L, Moser BA, Nakamura TM, Noguchi E","authors_abbrev":"Garabedian MV et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-11-19","publication_year":"2012","canto_session_key":"a100cec5b43cc083","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-06-26 16:35:11","canto_approved_date":"2024-04-14 10:15:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-26 16:35:01","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":107,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.08c","SPBC216.06c","SPBC342.05","SPCC1450.02","SPBC8D2.03c","SPAC694.06c","SPCC18B5.11c","SPBC216.05","SPAC631.02","SPCC1259.13","SPAC637.12c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2018-06-26"},{"uniquename":"PMID:23434529","title":"Synthesis of nordihydroguaiaretic acid derivatives and their bioactivities on S. pombe and K562 cell lines.","citation":"Eur J Med Chem 2013 Apr;62:605-13","abstract":"Nordihydroguaiaretic acid (NDGA) and its synthetic analogues are potentially useful in treating diseases related to cancers, diabetes, viral and bacterial infections, and inflammation. In this paper, we report the optimal synthetic methods and the bioactivity study of terameprocol 2, NDGA derivative 3, and its cyclized analogue 4. The IC50 of these three compounds 2, 3 and 4 on the growth metabolism of Schizosacchromyces pombe and K562 cell lines were determined by microcalorimetry. The preliminary results showed that the compounds 2, 3 and 4 possessed good inhibition activities on S. pombe and K562 cell lines, and exhibited bidirectional biological effect and Hormesis effect. In particular, terameprocol 2 was found to possess the most potent inhibitory effect on K562 cell lines.","doi":"10.1016/j.ejmech.2013.01.028","authors":"Li X, Jiang JH, Chen Q, Xiao SX, Li CH, Gu HW, Zhang H, Hu JL, Yao FH, Li QG","authors_abbrev":"Li X et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2013-02-26","publication_year":"2013","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22306653","title":"Germline mutations in DIS3L2 cause the Perlman syndrome of overgrowth and Wilms tumor susceptibility.","citation":"Nat Genet 2012 Feb 05;44(3):277-84","abstract":"Perlman syndrome is a congenital overgrowth syndrome inherited in an autosomal recessive manner that is associated with Wilms tumor susceptibility. We mapped a previously unknown susceptibility locus to 2q37.1 and identified germline mutations in DIS3L2, a homolog of the Schizosaccharomyces pombe dis3 gene, in individuals with Perlman syndrome. Yeast dis3 mutant strains have mitotic abnormalities. Yeast Dis3 and its human homologs, DIS3 and DIS3L1, have exoribonuclease activity and bind to the core RNA exosome complex. DIS3L2 has a different intracellular localization and lacks the PIN domain found in DIS3 and DIS3L1; nevertheless, we show that DIS3L2 has exonuclease activity. DIS3L2 inactivation was associated with mitotic abnormalities and altered expression of mitotic checkpoint proteins. DIS3L2 overexpression suppressed the growth of human cancer cell lines, and knockdown enhanced the growth of these cells. We also detected evidence of DIS3L2 mutations in sporadic Wilms tumor. These observations suggest that DIS3L2 has a critical role in RNA metabolism and is essential for the regulation of cell growth and division.","doi":"10.1038/ng.1071","authors":"Astuti D, Morris MR, Cooper WN, Staals RH, Wake NC, Fews GA, Gill H, Gentle D, Shuib S, Ricketts CJ, Cole T, van Essen AJ, van Lingen RA, Neri G, Opitz JM, Rump P, Stolte-Dijkstra I, Müller F, Pruijn GJ, Latif F, Maher ER","authors_abbrev":"Astuti D et al.","pubmed_publication_date":"05 Feb 2012","pubmed_entrez_date":"2012-02-07","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16C4.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8479431","title":"A study of integrative transformation in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1993 Apr;238(1-2):26-32","abstract":"Using the one-step gene disruption technique, we studied the effect of various parameters on the disruption frequency (percentage of homologous integrants) and transformation efficiency (number of transformants per microgram of input DNA) of integrative transformation in Schizosaccharomyces pombe. We used suc1 as the target gene for disruption and ura4 as the selectable marker. Our results are as follows. 1) Use of the strong adh1 promoter to drive the expression of ura4 did not affect the disruption frequency but modestly increased the transformation efficiency. 2) The transformation method had a profound effect, with the lithium acetate method yielding both a 10-fold higher disruption frequency compared to the protoplast method and a 5- to 10-fold higher transformation efficiency. 3) The presence of increasing amounts of non-homologous sequences at the ends of the transforming DNA decreased the disruption frequency by up to 5-fold but had no effect on the transformation efficiency. We also describe the use of the sup3-5 allele in an ade6-704 genetic background to discriminate between the products of homologous versus non-homologous integration, thereby promoting the identification of rare homologous integrants.","authors":"Grallert B, Nurse P, Patterson TE","authors_abbrev":"Grallert B et al.","pubmed_publication_date":"Apr 1993","pubmed_entrez_date":"1993-04-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7941746","title":"Molecular analysis of the malic enzyme gene (mae2) of Schizosaccharomyces pombe.","citation":"Yeast 1994 May;10(5):613-24","abstract":"Sequence analysis of a 4.6-kb HindIII fragment containing the malic enzyme gene (mae2) of Schizosaccharomyces pombe, revealed the presence of an open reading frame of 1695 nucleotides, coding for a 565 amino acid polypeptide. The mae2 gene is expressed constitutively and encodes a single mRNA transcript of 2.0 kb. The mae2 gene was mapped on chromosome III by chromoblotting. The coding region and inferred amino acid sequence showed significant homology with 12 malic enzyme genes and proteins from widely different origins. Eight highly homologous regions were found in these malic enzymes, suggesting that they contain functionally conserved amino acid sequences that are indispensable for activity of malic enzymes. Two of these regions have previously been reported to be NAD- and NADP-binding sites.","authors":"Viljoen M, Subden RE, Krizus A, Van Vuuren HJ","authors_abbrev":"Viljoen M et al.","pubmed_publication_date":"May 1994","pubmed_entrez_date":"1994-05-01","publication_year":"1994","canto_session_key":"4e4fbbfeed11ee9c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-30 18:02:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-30 18:02:40","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC794.12c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-30"},{"uniquename":"PMID:23700240","title":"Toxicity of ricinoleic acid production in fission yeast Schizosaccharomyces pombe is suppressed by the overexpression of plg7, a phospholipase A2 of a platelet-activating factor (PAF) family homolog.","citation":"Appl Microbiol Biotechnol 2013 Sep;97(18):8193-203","abstract":"In an effort to produce ricinoleic acid (RA), an important natural raw material with great values as a petrochemical replacement, in Schizosaccharomyces pombe, we introduced Claviceps purpurea oleate Δ12-hydroxylase gene (CpFAH12) to S. pombe, putting it under the control of an inducible nmt1 promoter. However, RA was toxic to S. pombe and the cells expressing CpFAH12 grew poorly at the normal growth temperature 30 °C. To address its toxic mechanism in S. pombe, we screened for a S. pombe cDNA library and identified plg7, which encodes a phospholipase A2, as a suppressor that restored the growth defect without affecting the RA production. A lacZ fusion experiment showed that the expression of plg7 was inducible by RA. Thin layer chromatographic analysis confirmed a reduction in RA moiety in phospholipids and a concomitant increase in free RA in the plg7 overexpressed strain. Since RA is synthesized at the sn-2 position of phosphatidylcholine by Fah12p, and phospholipase A2 hydrolyzes the sn-2 acyl bond of phospholipids, we speculate that plg7 is a stress-responsive gene, and removal of RA moieties from phospholipids, major components of lipid bilayer membrane, by Plg7p would be its suppression mechanism.","doi":"10.1007/s00253-013-4987-6","authors":"Yazawa H, Holic R, Kumagai H, Uemura H","authors_abbrev":"Yazawa H et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-05-24","publication_year":"2013","canto_session_key":"4c5f3797548c76dc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-02-19 18:12:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-19 18:12:51","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-02-19"},{"uniquename":"PMID:30301783","title":"The RHEB-mTOR axis regulates expression of  Tf2  transposons in fission yeast.","citation":"J Cell Sci 2018 Nov 21;131(22)","abstract":"The human  TSC2  gene, mutations in which predispose individuals to the disease tuberous sclerosis complex (TSC), encodes a GTPase-activating protein for the GTPase RHEB. Loss of TSC2 results in constitutive activation of RHEB and its target mammalian target of rapamycin (mTOR). We have previously reported that fission yeast ( Schizosaccharomyces pombe )  Tf2  retrotransposons (hereafter  Tf2 s) are abnormally induced upon nitrogen starvation in cells lacking the  tsc2 +   gene ( Δtsc2 ), a homolog of the human  TSC2  gene, and in cells with a dominant-active mutation in the fission yeast RHEB GTPase ( rhb1-DA4 ). We report here that induction of  Tf2 s in these mutants is suppressed upon overexpression of the  cgs2 +   gene, which encodes a cAMP-specific phosphodiesterase, or upon deletion of components in the glucose/cAMP signaling pathway, namely Cyr1, Pka1, Tor1 and the stress-activated transcription factor Atf1. The results suggest that the glucose/cAMP signaling pathway is downregulated when cells are starved for nitrogen. We also show that Tf2 proteins are degraded via autophagy, which is under control of Tor2, a homolog of human mTOR. It appears that failure in the two processes, downregulation of the glucose/cAMP signaling pathway and induction of autophagy, allows abnormal induction of  Tf2 s upon nitrogen starvation in  Δtsc2  and  rhb1-DA4  cells.","doi":"10.1242/jcs.221457","authors":"Nakase Y, Matsumoto T","authors_abbrev":"Nakase Y et al.","pubmed_publication_date":"21 Nov 2018","pubmed_entrez_date":"2018-10-11","publication_year":"2018","canto_session_key":"997da25b0914b868","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-10-13 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC285.09c","SPBC1105.04c","SPBC19C7.03","SPCC63.08c","SPBC428.16c","SPAC630.13c","SPBC216.07c","SPBC106.10"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PANTHER:PTHR43387","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC513.02","YKL128C","SPAC5H10.03"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:31474649","title":"Identification of 15 New Bypassable Essential Genes of Fission Yeast.","citation":"Cell Struct Funct 2019 Sep 27;44(2):113-119","abstract":"Every organism has a different set of genes essential for its viability. This indicates that an organism can become tolerant to the loss of an essential gene under certain circumstances during evolution, via the manifestation of 'masked' alternative mechanisms. In our quest to systematically uncover masked mechanisms in eukaryotic cells, we developed an extragenic suppressor screening method using haploid spores deleted of an essential gene in the fission yeast Schizosaccharomyces pombe. We screened for the 'bypass' suppressors of lethality of 92 randomly selected genes that are essential for viability in standard laboratory culture conditions. Remarkably, extragenic mutations bypassed the essentiality of as many as 20 genes (22%), 15 of which have not been previously reported. Half of the bypass-suppressible genes were involved in mitochondria function; we also identified multiple genes regulating RNA processing. 18 suppressible genes were conserved in the budding yeast Saccharomyces cerevisiae, but 13 of them were non-essential in that species. These trends suggest that essentiality bypass is not a rare event and that each organism may be endowed with secondary or backup mechanisms that can substitute for primary mechanisms in various biological processes. Furthermore, the robustness of our simple spore-based methodology paves the way for genome-scale screening.Key words: Schizosaccharomyces pombe, extragenic suppressor screening, bypass of essentiality (BOE), cut7 (kinesin-5), hul5 (E3 ubiquitin ligase).","doi":"10.1247/csf.19025","authors":"Takeda A, Saitoh S, Ohkura H, Sawin KE, Goshima G","authors_abbrev":"Takeda A et al.","pubmed_publication_date":"27 Sep 2019","pubmed_entrez_date":"2019-09-03","publication_year":"2019","canto_session_key":"549dcb6178093149","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-11-30 15:40:45","canto_approved_date":"2020-11-30 15:40:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-11-27 05:00:08","canto_added_date":"2019-09-04 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.14c","SPBP19A11.01","SPBC13E7.10c","SPBP23A10.08","SPBC2F12.08c","SPBC18E5.02c","SPBC13E7.06","SPBC1A4.11c","SPBC32F12.04","SPBC725.13c","SPBC8D2.14c","SPBC1773.11c","SPBC4F6.17c","SPBC216.07c","SPBC24C6.03","SPBC2F12.10","SPBC337.05c","SPBC3E7.14","SPBC582.07c","SPBC9B6.05c","SPBC18E5.12c","SPBC1A4.06c","SPBC557.03c","SPBC1703.10","SPBC119.11c","SPBC15D4.14","SPBC1709.20","SPBC2D10.08c","SPBC365.05c","SPBC106.15","SPBC646.05c","SPBC725.08","SPBC16G5.12c","SPBC12D12.03","SPBC1826.01c","SPBC336.08","SPBC36.08c","SPBC2G5.05","SPBC29A3.15c","SPBC25B2.09c","SPBC839.09c","SPBC15D4.04","SPBC1921.02","SPBC365.09c","SPBC8D2.13","SPBC9B6.04c","SPBC2F12.02c","SPAC3A11.14c","SPBC28E12.05","SPBC29A10.04","SPBC29A10.15","SPBC19G7.15","SPBC11G11.04","SPBC409.14c","SPBC1A4.01","SPBP23A10.09","SPBC29A3.06","SPBC18H10.14","SPAC14C4.14","SPBC2A9.08c","SPBC1271.13","SPBC1703.01c","SPBC9B6.08","SPBC1703.05","SPBC31E1.06","SPBC146.03c","SPBP16F5.06","SPBC12D12.08c","SPBC713.12","SPBC17A3.01c","SPBP23A10.15c","SPBC725.17c","SPBC19G7.13","SPBC1198.10c","SPBC12D12.01","SPBC18E5.03c","SPBC146.07","SPAC2G11.12","SPBC18H10.03","SPBC1A4.08c","SPBC24C6.07","SPBC2A9.09","SPAC25G10.07c","SPBC14C8.01c","SPBC336.15","SPBC1734.02c","SPCC576.10c","SPBC28F2.04c","SPAC167.07c","SPBC2A9.12","SPBC18H10.17c","SPBC1A4.07c","SPBC337.14","SPBC3H7.01","SPBC409.04c","SPBC646.07c","SPBC21D10.05c","SPBC8D2.15","SPBP18G5.02","SPBC29A3.16"],"gene_count":100,"ltp_gene_count":9,"approved_date":"2020-11-30"},{"uniquename":"PMID:32454109","title":"Transcription-facilitating histone chaperons interact with genomic and synthetic G4 structures.","citation":"Int J Biol Macromol 2020 Oct 01;160:1144-1157","abstract":"Affinity for G-quadruplex (G4) structures may be a common feature of transcription-facilitating histone chaperons (HCs). This assumption is based on previous unmatched studies of HCs FACT, nucleolin (NCL), BRD3, and ATRX. We verified this assumption and considered its implications for the therapeutic applications of synthetic (exogenous) G4s and the biological significance of genomic G4s. First, we questioned whether exogenous G4s that recognize cell-surface NCL and could trap other HCs in the nucleus are usable as anticancer agents. We performed in vitro binding assays and selected leading multi-targeted G4s. They exhibited minor effects on cell viability. The presumed NCL-regulated intracellular transport of G4s was inefficient or insufficient for tumor-specific G4 delivery. Next, to clarify whether G4s in the human genome could recruit HCs, we compared available HC ChIP-seq data with G4-seq/G4-ChIP-seq data. Several G4s, including the well-known c-Myc quadruplex structure, were found to be colocalized with HC occupancy sites in cancer cell lines. As evidenced by our molecular modeling data, c-Myc G4 might interfere with the HC function of BRD3 but is unlikely to prevent the BRD3-driven assembly of the chromatin remodeling complex. The c-Myc case illustrates the intricate role of genomic G4s in chromatin remodeling, nucleosome remodeling, and transcription.","doi":"10.1016/j.ijbiomac.2020.05.173","authors":"Pavlova II, Tsvetkov VB, Isaakova EA, Severov VV, Khomyakova EA, Lacis IA, Lazarev VN, Lagarkova MA, Pozmogova GE, Varizhuk AM","authors_abbrev":"Pavlova II et al.","pubmed_publication_date":"01 Oct 2020","pubmed_entrez_date":"2020-05-27","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC140.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18066763","title":"Fission yeast telomeric DNA binding protein Pot1 has the ability to unfold tetraplex structure of telomeric DNA.","citation":"Nucleosides Nucleotides Nucleic Acids 2007;26(10-12):1255-60","abstract":"To understand the regulation mechanism of fission yeast telomeric DNA, we analyzed the structural properties of 4Gn: d(G(n)TTAC)(4) (n = 3, 4) and their interaction with the single-stranded telomeric DNA binding domain of telomere-binding protein Pot1 (Pot1DBD). 4G4 adopted only an antiparallel tetraplex in spite of a mixture of parallel and antiparallel tetraplexes of 4G3. The antiparallel tetraplex of 4G4 became unfolded upon the interaction with Pot1DBD. Considering that the antiparallel tetraplex inhibits telomerase-mediated telomere elongation, we conclude that the ability of Pot1 to unfold the antiparallel tetraplex is required for telomerase-mediated telomere regulation.","authors":"Torigoe H","authors_abbrev":"Torigoe H","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-12-11","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28977643","title":"Regulation of mitotic recombination between DNA repeats in centromeres.","citation":"Nucleic Acids Res 2017 Nov 02;45(19):11222-11235","abstract":"Centromeres that are essential for faithful segregation of chromosomes consist of unique DNA repeats in many eukaryotes. Although recombination is under-represented around centromeres during meiosis, little is known about recombination between centromere repeats in mitotic cells. Here, we compared spontaneous recombination that occurs between ade6B/ade6X inverted repeats integrated at centromere 1 (cen1) or at a non-centromeric ura4 locus in fission yeast. Remarkably, distinct mechanisms of homologous recombination (HR) were observed in centromere and non-centromere regions. Rad51-dependent HR that requires Rad51, Rad54 and Rad52 was predominant in the centromere, whereas Rad51-independent HR that requires Rad52 also occurred in the arm region. Crossovers between inverted repeats (i.e. inversions) were under-represented in the centromere as compared to the arm region. While heterochromatin was dispensable, Mhf1/CENP-S, Mhf2/CENP-X histone-fold proteins and Fml1/FANCM helicase were required to suppress crossovers. Furthermore, Mhf1 and Fml1 were found to prevent gross chromosomal rearrangements mediated by centromere repeats. These data for the first time uncovered the regulation of mitotic recombination between DNA repeats in centromeres and its physiological role in maintaining genome integrity.","doi":"10.1093/nar/gkx763","authors":"Zafar F, Okita AK, Onaka AT, Su J, Katahira Y, Nakayama JI, Takahashi TS, Masukata H, Nakagawa T","authors_abbrev":"Zafar F et al.","pubmed_publication_date":"02 Nov 2017","pubmed_entrez_date":"2017-10-05","publication_year":"2017","canto_session_key":"abefd0a167d6fbd7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tako Nakagawa","canto_first_approved_date":"2017-12-01 09:37:50","canto_approved_date":"2017-12-01 09:37:50","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-10-19 10:36:19","canto_added_date":"2017-10-06 00:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Tako Nakagawa","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.03c","SPBC2D10.16","SPBC1861.01c","SPBC1105.17","SPAC30D11.10","SPBC428.08c","SPCC1672.10","SPAC688.02c","SPCC576.12c","SPCC970.12","SPBC800.13","SPAC644.14c","SPAC11E3.03","SPAC9.05"],"gene_count":14,"ltp_gene_count":6,"approved_date":"2017-12-01"},{"uniquename":"PMID:39835694","title":"In Vitro Formation of Actin Ring in the Fission Yeast Cell Extracts.","citation":"Cytoskeleton (Hoboken) 2025 Jan 21;","abstract":"Cytokinesis in animal and fungal cells requires the contraction of actomyosin-based contractile rings formed in the division cortex of the cell during late mitosis. However, the detailed mechanism remains incompletely understood. Here, we aim to develop a novel cell-free system by encapsulating cell extracts obtained from fission yeast cells within lipid vesicles, which subsequently leads to the formation of a contractile ring-like structure inside the vesicles. Using this system, we found that an actin ring structure formed in vesicles of a size similar to that of fission yeast cells, with the frequency of ring appearance increasing in the presence of PI(4,5)P 2  (PIP 2 ). In contrast, larger vesicles tended to form actin bundles, which were sometimes associated with ring structures or network-like structures. The effects of various inhibitors affecting cytoskeleton formation were investigated, revealing that actin polymerization was essential for the formation of these actin structures. Additionally, the involvement of ATP, the Schizosaccharomyces pombe PLK \"Plo1,\" and the small GTPase Rho was suggested to play a crucial role in this process. Examination of mitotic extracts revealed the formation of actin dot structures in phosphatidylethanolamine vesicles. However, most of these structures disappeared in the presence of PIP 2 , leading to the formation of actin Rings instead. Using extracts from cells expressing α-actinin Ain1 or myosin-II light chain Rlc1, both fused with fluorescent proteins, we found that these proteins colocalized with actin bundles. In summary, we have developed a new semi-in vitro system to investigate mechanisms such as cell division and cytoskeleton formation.","doi":"10.1002/cm.21997","authors":"Yoshihara S, Nakata T, Kashiwazaki J, Aoyama K, Mabuchi I","authors_abbrev":"Yoshihara S et al.","pubmed_publication_date":"21 Jan 2025","pubmed_entrez_date":"2025-01-21","publication_year":"2025","canto_session_key":"9a50151ca017dadd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-01-22 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11279180","title":"A chaperone for ribosome maturation.","citation":"J Biol Chem 2001 May 18;276(20):16655-9","abstract":"The nascent pre-rRNA of eukaryotic ribosomes is fully transcribed and assembled into an 80-90 S nucleolar particle before being cleaved into mature ribosomal RNA. The interdependence of steps in the processing of this precursor RNA indicates that RNA processing, at least in part, acts as a quality control mechanism that helps ensure that only functional RNA is incorporated into mature ribosomes. In search of structural components that underlie this interdependence using the Schizosaccharomyces pombe internal transcribed spacer 1 (ITS) as a ligand for affinity chromatography of ITS1-specific proteins, we have isolated a large spliceosome-like protein complex, a ribosome assembly chaperone (RAC) of 20 or more polypeptides (Lalev, A. I., Abeyrathne, P. D., and Nazar, R. N. (2000) J. Mol. Biol. 302, 65-77). When the ITS2 spacer was used in the present study to isolate ITS2-specific proteins, the same proteins were identified consistent with a complex containing multiple specific binding sites. Subsequent competition binding studies indicated that the protein complex actually contains independent binding sites for all four of the transcribed spacers in the pre-rRNA. Because disruption of protein-binding sites in these spacer RNAs is known to severely affect rRNA processing, taken together these results suggest that the RAC complex is a chaperone for ribosome maturation acting as a \"rack\" on which critical structure is organized.","authors":"Lalev AI, Nazar RN","authors_abbrev":"Lalev AI et al.","pubmed_publication_date":"18 May 2001","pubmed_entrez_date":"2001-03-30","publication_year":"2001","canto_session_key":"bb13b2df7877ff55","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-01-02 05:22:18","canto_approved_date":"2025-10-11 18:45:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-02 05:22:12","canto_added_date":"2012-02-24 05:51:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC70.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2021-01-02"},{"uniquename":"EMBL:SPD133","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24713849","title":"Post-transcriptional regulation of meiotic genes by a nuclear RNA silencing complex.","citation":"RNA 2014 Jun;20(6):867-81","abstract":"RNA is a central component of gene-silencing pathways that regulate diverse cellular processes. In the fission yeast Schizosaccharomyces pombe, an RNA-based mechanism represses meiotic gene expression during vegetative growth. This pathway depends on the zinc finger protein Red1, which is required to degrade meiotic mRNAs as well as to target histone H3 lysine 9 (H3K9) methylation, a repressive chromatin mark, to a subset of meiotic genes. However, the mechanism of Red1 function is unknown. Here we use affinity purification and mass spectrometry to identify a Red1-containing nuclear RNA silencing (NURS) complex. In addition to Red1, this complex includes the Mtl1, Red5, Ars2, Rmn1, and Iss10 proteins and associates with several other complexes that are involved in either signaling or mediating RNA silencing. By analyzing the effects of gene knockouts and inducible knockdown alleles, we show that NURS subunits regulate RNA degradation and H3K9 methylation at meiotic genes. We also identify roles for individual NURS subunits in interactions with Mmi1, an RNA-binding protein that marks meiotic RNAs for destruction, and the nuclear exosome RNA degradation complex. Finally, we show that the levels of H3K9 methylation at meiotic genes are not sufficient to restrict RNA polymerase II access or repress gene expression during vegetative growth. Our results demonstrate that Red1 partners with other proteins to silence meiotic gene expression at the post-transcriptional level. Conservation of a NURS-like complex in human cells suggests that this pathway plays an ancient and fundamental role in RNA silencing.","doi":"10.1261/rna.044479.114","authors":"Egan ED, Braun CR, Gygi SP, Moazed D","authors_abbrev":"Egan ED et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-04-10","publication_year":"2014","canto_session_key":"53af9f6726121d19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Emily Egan","canto_first_approved_date":"2015-08-05 14:53:07","canto_approved_date":"2022-02-07 15:31:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-31 15:03:08","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":43,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Emily Egan","community_curator":true,"annotation_count":131,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1565.08","SPBC13A2.01c","SPBC26H8.08c","SPAC23H4.09","SPCC550.02c","SPBC3E7.13c","SPBC31F10.11c","SPAC20H4.09","SPAC1783.07c","SPBC1198.13c","SPAC1782.08c","SPAC12G12.06c","SPCC16C4.18c","SPBC16H5.12c","SPCC1753.05","SPAC16E8.06c","SPAC1834.04","SPBC29A10.02","SPAC24H6.05","SPBC28F2.11","SPAC1F12.02c","SPAC140.04","SPAC23G3.01","SPBC839.10","SPBC26H8.10","SPAC19D5.05c","SPCC18.06c","SPBC3B8.09","SPBC18H10.17c","SPAC10F6.08c","SPBC32C12.02","SPBC1604.12","SPCC24B10.04","SPAC18B11.06","SPBC725.08","SPBC21C3.05","SPBC1709.08","SPAC27E2.03c","SPAC1F3.01","SPBC25H2.13c","SPBC11G11.04","SPBP35G2.13c","SPBC3D6.12","SPBC211.08c","SPCC31H12.08c","SPAC22H12.02","SPBC17G9.04c","SPAC5H10.05c","SPAC2G11.15c","SPBC21B10.05c","SPBC19G7.06","SPCC550.14","SPBC1539.10","SPBC691.04","SPCC757.08","SPCC16C4.11","SPAC22H10.02","SPBC21B10.08c","SPBC15C4.05","SPBC18H10.11c","SPAC25H1.08c","SPCC16C4.16c","SPAC1071.06","SPBC29A10.14","SPAC1B3.05","SPCC1322.16","SPBC776.09","SPCC1442.10c","SPBC8D2.12c","SPBC11G11.05","SPAC6B12.10c","SPAC9G1.05","SPAC4F8.12c","SPAC15E1.10","SPBC28F2.04c","SPBC83.14c","SPBC13E7.01","SPAC664.08c","SPBC19C2.14","SPBC13E7.10c","SPAC343.04c","SPCC962.03c","SPBC4F6.13c","SPAC644.16","SPBC582.03","SPBC18H10.10c","SPBC11G11.03","SPAC4G9.04c","SPBC839.07","SPBC14F5.03c","SPAC13D6.02c","SPAC20H4.06c","SPBC1289.03c","SPBC216.01c","SPAPB17E12.11","SPAC1142.04","SPBC31F10.13c","SPCC364.01","SPCC1739.03","SPBC115.01c","SPAC26H5.07c","SPBC211.02c","SPCC11E10.08","SPBC1105.06","SPAC57A7.06","SPAC17H9.12c","SPCC1259.03","SPAC19G12.13c","SPBC12C2.04","SPAPB1A10.09","SPAC26H5.04","SPCC18.12c","SPAC4F10.09c","SPBC19G7.10c","SPAC1006.07","SPBC215.06c","SPAC3A12.07","SPCC1672.07","SPCC737.04","SPAC9E9.13","SPCC1827.05c","SPBC25B2.05","SPBC6B1.07","SPAC4F10.06","SPBC1718.03","SPBC13E7.07","SPCC1672.02c","SPBC16H5.10c","SPCP1E11.07c","SPCC16C4.22","SPAC23C4.15","SPAC222.06","SPBP22H7.07","SPBC577.04","SPAPB21F2.03","SPBC1289.12","SPAC16E8.11c","SPBC365.04c","SPBC17D1.04","SPBC1289.07c","SPBC646.12c","SPBC3D6.09","SPBC646.04","SPBP35G2.09","SPAC1486.04c","SPAC3A12.11c","SPAC31G5.18c","SPAC6F12.16c","SPAC31A2.08","SPCC1235.07","SPAPJ698.03c","SPAC1687.03c","SPAC1565.05","SPAC29A4.04c","SPAC959.03c","SPBC16E9.10c","SPBC20F10.01","SPBC902.04","SPAC19B12.12c","SPBC32H8.10","SPBC106.13","SPBP8B7.20c","SPBC28F2.10c","SPBPB7E8.02","SPBC13G1.13","SPAC1687.01","SPBC1A4.07c","SPAC1486.03c","SPBC4B4.09","SPCP1E11.11","SPCC364.02c","SPAC17G8.13c","SPAPB24D3.07c","SPBC359.06","SPBC14C8.14c","SPAC2F7.14c","SPAC22G7.10","SPAC23A1.18c","SPAC644.12","SPBC1861.08c","SPAC3G6.03c","SPAC18G6.06","SPAC607.03c","SPBC530.14c","SPCC16C4.14c","SPBC4C3.05c","SPAC1F7.02c","SPBC29A3.16","SPBC1604.08c","SPAC12G12.02","SPBP4H10.18c","SPBC19F5.05c","SPAC13F5.02c","SPAC1952.03","SPBC839.12","SPAC21E11.03c","SPBC4F6.07c","SPAC23C11.11","SPAPB8E5.09","SPAC22A12.12c","SPBP23A10.07","SPAC29B12.06c","SPBC21B10.03c","SPBC32F12.05c","SPBC365.05c","SPAC6F6.03c","SPAC1006.03c","SPAC6G10.07","SPCC188.07","SPBC947.02","SPAC15F9.02","SPAC22E12.07","SPBC336.12c","SPBC14C8.12","SPBC2G5.02c","SPAC10F6.11c","SPBC16H5.15","SPBC32H8.11","SPAC17H9.05","SPCC74.03c","SPAC22F8.10c","SPAC1B9.03c","SPAC17G6.16c","SPBC30D10.06","SPBC16G5.10","SPBC8D2.09c","SPBP35G2.11c","SPAC16C9.06c","SPBC32H8.05","SPAC23G3.06","SPAC2G11.08c","SPAC6F12.17","SPCC1840.11","SPBC776.02c","SPAC1527.03","SPAC15E1.08","SPAC458.02c","SPCC1183.07","SPAC1B3.12c","SPBC4F6.14","SPBC83.17","SPAC32A11.02c","SPAC17G6.13","SPAC1834.03c","SPBC20F10.05","SPAC9.03c","SPAC27D7.07c","SPBC1289.11","SPAC2C4.03c","SPBC16E9.02c","SPAC20G8.09c","SPBC20F10.09","SPBC337.03","SPBC3E7.14","SPBC6B1.10","SPCC1620.07c","SPAC18G6.13","SPBC31A8.01c","SPBC337.12","SPCC330.10","SPBC2A9.02","SPBC3B8.08","SPAC2F3.03c","SPAC7D4.14c","SPAC17A2.08c","SPAC1556.01c","SPCC16A11.13","SPBC660.11","SPBC1D7.04","SPAC139.01c","SPAC17G6.10","SPBC646.10c","SPCC162.08c","SPAC3G6.04","SPCC970.07c","SPAC3C7.14c","SPBC17D1.06","SPBC24C6.11","SPAC4G8.13c","SPAC27F1.09c","SPAC23D3.08","SPCC4B3.15","SPAC2C4.10c","SPAC30C2.04","SPBC2D10.10c","SPCC1902.02","SPAC222.09","SPBC776.08c","SPAC1851.03","SPAC26A3.08","SPBC36.09","SPBC83.15","SPBC4B4.05","SPBC32F12.06","SPAC1782.10c","SPBC36.05c","SPCP1E11.04c","SPBC4F6.06","SPAC20G8.06","SPBC1921.07c","SPBC19F8.07","SPBC336.14c","SPAC23D3.02","SPAC6F12.14","SPBC16A3.08c","SPAC3A11.08","SPAC22H10.05c","SPAPJ691.02","SPAC23C11.03","SPBC28F2.02","SPAC22E12.18","SPAP8A3.06","SPAC2F7.11","SPBC3B9.07c","SPBC4B4.07c","SPBC11B10.09","SPBC31F10.14c","SPAP27G11.13c","SPAC1F7.04","SPBC651.01c","SPAC140.02","SPBC336.04","SPCC613.07","SPAC24B11.06c","SPBC26H8.11c","SPAC31G5.09c","SPCC1322.12c","SPAC683.02c","SPCC1795.11","SPBC646.02","SPBC29A10.06c","SPBC16E9.12c","SPCC1682.03c","SPAC890.04c","SPCC1739.07","SPCC364.06","SPAC14C4.06c","SPAC2E1P5.05","SPBC30D10.15","SPAC17H9.02","SPAC3G9.10c","SPBPB21E7.07","SPAC8F11.04","SPCC330.09","SPCC1620.01c","SPBC800.06","SPAC27E2.10c","SPBC29A10.05","SPCC970.01","SPAC6F12.15c","SPBC17D1.03c","SPBC29A3.07c","SPAC1782.06c","SPAC12G12.14c","SPBC557.02c","SPBC609.05","SPAC17H9.07","SPCC18.11c","SPBC19F8.05","SPBC713.05","SPBC1711.07","SPAC57A10.10c","SPBC19F5.02c","SPAC4D7.13","SPCC188.11","SPBC1711.16","SPCC1259.12c","SPCC736.12c","SPBC713.04c","SPBC11G11.06c","SPBC1921.03c","SPAC1F5.10","SPCP1E11.08","SPBC29A3.03c","SPAC22G7.04","SPAC227.07c","SPBC342.04","SPCC285.12","SPCC622.09","SPAC22A12.09c","SPAC16C9.04c","SPAC1F5.03c","SPAC227.02c","SPAC926.08c","SPAC10F6.02c","SPAC27D7.13c","SPAC12G12.07c","SPAC694.02","SPBC1711.08","SPBC2G2.09c","SPAC1B3.13","SPAC26A3.12c","SPAC19A8.13","SPAC4A8.09c","SPAC29A4.08c","SPACUNK4.11c","SPBP16F5.07","SPCC10H11.02","SPAC13G7.03","SPBC354.10","SPBC83.08","SPAC22F8.09","SPAC23G3.09","SPAC20G8.05c","SPAC22G7.05","SPAC3G9.07c","SPBC23E6.04c","SPCC553.06","SPBC2A9.12","SPBC1711.05","SPAC1B1.03c","SPBC1703.10","SPCC4G3.15c","SPBC215.12","SPBC3E7.07c","SPBC1604.09c","SPCC1739.05","SPAC6F12.11c","SPAP8A3.13c","SPCC965.10","SPCC622.08c","SPCC613.12c","SPBP8B7.11"],"gene_count":423,"ltp_gene_count":22,"approved_date":"2015-08-05"},{"uniquename":"PMID:23907979","title":"The fission yeast cell wall stress sensor-like proteins Mtl2 and Wsc1 act by turning on the GTPase Rho1p but act independently of the cell wall integrity pathway.","citation":"Microbiologyopen 2013 Oct;2(5):778-94","abstract":"Sensing stressful conditions that affect the cell wall reorganization is important for yeast survival. Here, we studied two proteins SpWsc1p and SpMtl2p with structural features indicative of plasma membrane-associated cell wall sensors. We found that Mtl2p and Wsc1p act by turning on the Rho1p GTPase. Each gene could be deleted individually without affecting viability, but the deletion of both was lethal and this phenotype was rescued by overexpression of the genes encoding either Rho1p or its GDP/GTP exchange factors (GEFs). In addition, wsc1Δ and mtl2Δ cells showed a low level of Rho1p-GTP under cell wall stress. Mtl2p-GFP (green fluorescent protein) localized to the cell periphery and was necessary for survival under different types of cell wall stress. Wsc1p-GFP was concentrated in patches at the cell tips, it interacted with the Rho-GEF Rgf2p, and its overexpression activated cell wall biosynthesis. Our results are consistent with the notion that cell wall assembly is regulated by two different networks involving Rho1p. One includes signaling from Mtl2p through Rho1p to Pck1p, while the second one implicates signaling from Wsc1p and Rgf2p through Rho1p to activate glucan synthase (GS). Finally, signaling through the mitogen-activated protein kinase (MAPK) Pmk1p remained active in mtl2Δ and wsc1Δ disruptants exposed to cell wall stress, suggesting that the cell wall stress-sensing spectrum of Schizosaccharomyces pombe sensor-like proteins differs from that of Saccharomyces cerevisiae.","doi":"10.1002/mbo3.113","authors":"Cruz S, Muñoz S, Manjón E, García P, Sanchez Y","authors_abbrev":"Cruz S et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-08-03","publication_year":"2013","canto_session_key":"28977e64fba675ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-07-14 21:54:55","canto_approved_date":"2025-09-03 18:29:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-07-01 22:37:51","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":38,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.06","SPAC24C9.07c","SPBC30B4.01c","SPBC119.08","SPCC645.06c","SPCC645.07","SPAC1F7.04","SPAC11G7.01","SPBC1706.01","SPBC12D12.04c","SPAC17G8.14c"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2022-07-14"},{"uniquename":"PMID:31586050","title":"Atomic-level insight into mRNA processing bodies by combining solid and solution-state NMR spectroscopy.","citation":"Nat Commun 2019 Oct 04;10(1):4536","abstract":"Liquid-liquid phase separation is increasingly recognized as a process involved in cellular organization. Thus far, a detailed structural characterization of this intrinsically heterogeneous process has been challenging. Here we combine solid- and solution-state NMR spectroscopy to obtain atomic-level insights into the assembly and maturation of cytoplasmic processing bodies that contain mRNA as well as enzymes involved in mRNA degradation. In detail, we have studied the enhancer of decapping 3 (Edc3) protein that is a central hub for processing body formation in yeast. Our results reveal that Edc3 domains exhibit diverse levels of structural organization and dynamics after liquid-liquid phase separation. In addition, we find that interactions between the different Edc3 domains and between Edc3 and RNA in solution are largely preserved in the condensed protein state, allowing processing bodies to rapidly form and dissociate upon small alterations in the cellular environment.","doi":"10.1038/s41467-019-12402-3","authors":"Damman R, Schütz S, Luo Y, Weingarth M, Sprangers R, Baldus M","authors_abbrev":"Damman R et al.","pubmed_publication_date":"04 Oct 2019","pubmed_entrez_date":"2019-10-06","publication_year":"2019","canto_session_key":"6ed80af6d4b36264","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14734657","title":"Role of microtubules and tea1p in establishment and maintenance of fission yeast cell polarity.","citation":"J Cell Sci 2004 Feb 15;117(Pt 5):689-700","abstract":"Microtubules and the protein tea1p have important roles in regulating cell polarity in the fission yeast Schizosaccharomyces pombe. Here, using combinations of drugs, environmental perturbations and genetic mutants, we demonstrate that once a cell polarity axis is established, microtubules have at best a minor role in maintaining the cortical actin cytoskeleton and the rate and direction of cell growth. In addition, we find that after perturbations that disrupt cell polarity and the cortical actin cytoskeleton, microtubules are not required for re-establishment of polarity per se. However, after such perturbations, the distribution of cytoplasmic microtubules plays an important role in dictating the position of sites of polarity re-establishment. Furthermore, this influence of microtubule distribution on site selection during polarity re-establishment requires the presence of tea1p, suggesting that tea1p is crucial for coupling microtubule distribution to the regulation of cell polarity. Our results suggest a model in which, at the cellular level, two distinct and separable mechanisms contribute to how tea1p regulates site selection during polarity re-establishment. First, tea1p remaining at cell tips after cortical depolarization can serve as a cortical landmark for microtubule-independent site selection; second, tea1p newly targeted to the cell cortex by association with microtubules can promote the formation of polarity axes de novo.","authors":"Sawin KE, Snaith HA","authors_abbrev":"Sawin KE et al.","pubmed_publication_date":"15 Feb 2004","pubmed_entrez_date":"2004-01-22","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25457676","title":"Assembly of fission yeast eisosomes in the plasma membrane of budding yeast: import of foreign membrane microdomains.","citation":"Eur J Cell Biol 2015 Jan;94(1):1-11","abstract":"Eisosomes are plasma membrane-associated protein complexes organizing the membrane compartment of Can1 (MCC), a membrane microdomain of specific structure and function in ascomycetous fungi. By heterologous expression of specific components of Schizosaccharomyces pombe eisosomes in Saccharomyces cerevisiae we reconstitute structures exhibiting the composition and morphology of S. pombe eisosome in the host plasma membrane. We show S. pombe protein Pil1 (SpPil1) to substitute the function of its S. cerevisiae homologue in building plasma membrane-associated assemblies recognized by inherent MCC/eisosome constituents Sur7 and Seg1. Our data indicate that binding of SpPil1 to the plasma membrane of S. cerevisiae also induces formation of furrow-like invaginations characteristic for MCC. To the best of our knowledge, this is the first report of interspecies transfer of a functional plasma membrane microdomain. In the described system, we identify a striking difference between eisosome stabilizer proteins Seg1 and SpSle1. While Seg1 recruits both Pil1 and SpPil1 to the plasma membrane, SpSle1 recognizes only its natural counterpart, SpPil1. In the presence of Pil1, SpSle1 is segregated outside the Pil1-organized eisosomes and forms independent microdomains in the host membrane.","doi":"10.1016/j.ejcb.2014.10.003","authors":"Vaskovicova K, Stradalova V, Efenberk A, Opekarova M, Malinsky J","authors_abbrev":"Vaskovicova K et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-12-03","publication_year":"2015","canto_session_key":"d9222c32ecc34244","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-12-04 01:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24938147","title":"Chromosome 9q33q34 microdeletion with early infantile epileptic encephalopathy, severe dystonia, abnormal eye movements, and nephroureteral malformations.","citation":"Pediatr Neurol 2014 Jul;51(1):170-5","abstract":"Microdeletion of chromosome 9q33q34 is an emerging disease disorder associated with early infantile epileptic encephalopathy, intellectual disability, and a variety of movement disorders.\nWe describe a male infant with early infantile epileptic encephalopathy with suppression-burst (Ohtahara syndrome) who carried a de novo 2.0-Mb microdeletion in chromosome 9q33q34, including STXBP1. The previously reported examples of 9q33q34 microdeletion including STXBP1 are reviewed.\nThe patient developed infantile spasms at 4 months of age, and these were refractory to multiple antiepileptic drugs. He also developed severe dystonia during infancy, rotatory nystagmus, and nephroureteral malformations. Immunoglobulin and clobazam administered at 11 months were effective for the spasms, but profound psychomotor retardation remained. A comparative genomic hybridization array analysis and the fluorescence in situ hybridization analysis revealed a de novo 2.0-Mb microdeletion in chromosome 9q33q34, which encompasses STXBP1, ENG, SPTAN1, and 52 other genes. A total of 14 patients (13 from the literature) with a 9q33q24 microdeletion including STXBP1 were reviewed, five of them displayed early infantile epileptic encephalopathy with suppression-burst, and six of them had early-onset epilepsy but not early infantile epileptic encephalopathy. Dystonia has been previously described in 9q33q34 deletions involving TOR1A but not STXBP1. Neither abnormal eye movements nor nephroureteral malformations has been previously described.\nThis patient adds unique clinical presentations of neurological and nephroureteral abnormalities to the features of 9q33q34 microdeletion.","doi":"10.1016/j.pediatrneurol.2014.03.013","authors":"Matsumoto H, Zaha K, Nakamura Y, Hayashi S, Inazawa J, Nonoyama S","authors_abbrev":"Matsumoto H et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-06-19","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC584.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11839792","title":"Three proteins required for early steps in the protein secretory pathway also affect nuclear envelope structure and cell cycle progression in fission yeast.","citation":"J Cell Sci 2002 Jan 15;115(Pt 2):421-31","abstract":"The Ran GTPase is an essential protein that has multiple functions in eukaryotic cells. Fission yeast cells in which Ran is misregulated arrest after mitosis with condensed, unreplicated chromosomes and abnormal nuclear envelopes. The fission yeast sns mutants arrest with a similar cell cycle block and interact genetically with the Ran system. sns-A10, sns-B2 and sns-B9 have mutations in the fission yeast homologues of S. cerevisiae Sar1p, Sec31p and Sec53p, respectively, which are required for the early steps of the protein secretory pathway. The three sns mutants accumulate a normally secreted protein in the endoplasmic reticulum (ER), have an increased amount of ER membrane, and the ER/nuclear envelope lumen is dilated. Neither a post-ER block in the secretory pathway, nor ER proliferation caused by overexpression of an integral ER membrane protein, results in a cell cycle-specific defect. Therefore, the arrest seen in sns-A10, sns-B2 and sns-B9 is most likely due to nuclear envelope defects that render the cells unable to re-establish the interphase organization of the nucleus after mitosis. As a consequence, these mutants are unable to decondense their chromosomes or to initiate of the next round of DNA replication.","authors":"Matynia A, Salus SS, Sazer S","authors_abbrev":"Matynia A et al.","pubmed_publication_date":"15 Jan 2002","pubmed_entrez_date":"2002-02-13","publication_year":"2002","canto_session_key":"50dfb504a775bd4d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-12-30 14:39:43","canto_approved_date":"2026-01-30 15:45:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-11 15:09:45","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31F10.06c","SPBC8D2.20c","SPAC1783.07c","SPAC1556.07"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2023-12-30"},{"uniquename":"PMID:1417773","title":"Structurally and functionally conserved regions of cytochrome P-450 reductase as targets for DNA amplification by the polymerase chain reaction. Cloning and nucleotide sequence of the Schizosaccharomyces pombe cDNA.","citation":"Biochem J 1992 Oct 01;287 ( Pt 1)(Pt 1):195-200","abstract":"1. Alignments of the available cytochrome P-450 reductase amino acid sequences, and comparison with the crystal structure of ferredoxin-NADP reductase, indicate that two highly conserved regions are of functional importance. 2. Degenerate oligonucleotide primers, based on these sequences, were used in the polymerase chain reaction to amplify a 309 bp fragment of the cytochrome P-450 reductase gene from Schizosaccharomyces pombe for use as an homologous probe. 3. A 2.6 kb cDNA was cloned from a lambda library, and sequencing revealed an open-reading frame of 2034 bp encoding a protein of M(r) 76774. This protein shares 38-41% identity with other eukaryotic cytochrome P-450 reductases, and 30% identity with that of Bacillus megaterium. 4. Comparison of the N-terminal FMN-binding domain with flavodoxin, and the C-terminal FAD- and NADP-binding domain with ferredoxin-NADP reductase, indicates the presence of several functionally conserved regions. 5. The Sc. pombe cytochrome P-450 reductase gene was shown to contain no introns.","authors":"Miles JS","authors_abbrev":"Miles JS","pubmed_publication_date":"01 Oct 1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_session_key":"8fbb9f4bd98c26ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:28:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-28 14:16:38","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.01"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-28"},{"uniquename":"PMID:32663505","title":"Adaptation to iron deficiency in human pathogenic fungi.","citation":"Biochim Biophys Acta Mol Cell Res 2020 Oct;1867(10):118797","abstract":"Iron is an essential micronutrient for virtually all eukaryotic organisms and plays a central role during microbial infections. Invasive fungal diseases are associated with strikingly high rates of mortality, but their impact on human health is usually underestimated. Upon a fungal infection, hosts restrict iron availability in order to limit the growth and virulence of the pathogen. Here, we use two model yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe, to delve into the response to iron deficiency of human fungal pathogens, such as Candida glabrata, Candida albicans, Aspergillus fumigatus and Cryptococcus neoformans. Fungi possess common and species-specific mechanisms to acquire iron and to control the response to iron limitation. Upon iron scarcity, fungi activate a wide range of elegant strategies to capture and import exogenous iron, mobilize iron from intracellular stores, and modulate their metabolism to economize and prioritize iron utilization. Hence, iron homeostasis genes represent remarkable virulence factors that can be used as targets for the development of novel antifungal treatments.","doi":"10.1016/j.bbamcr.2020.118797","authors":"Martínez-Pastor MT, Puig S","authors_abbrev":"Martínez-Pastor MT et al.","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-07-15","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-07-16 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15525536","title":"The S. pombe Cdc14-like phosphatase Clp1p regulates chromosome biorientation and interacts with Aurora kinase.","citation":"Dev Cell 2004 Nov;7(5):755-62","abstract":"The S. pombe Cdc14-related phosphatase Clp1p/Flp1p regulates G2/M transition by antagonizing CDK activity and is essential for coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. At the G2/M transition, Clp1p/Flp1p is released from the nucleolus and SPB and distributes throughout the nucleus to the spindle and the contractile ring. This early relocalization is analogous to vertebrate Cdc14 homologs and stands in contrast to S. cerevisiae Cdc14p, which is not released from the nucleolus until metaphase/anaphase transition. Here, we report that Clp1p/Flp1p localizes to kinetochores in prometaphase and functions in chromosome segregation, since deletion of clp1/flp1 causes cosegregation of sister chromatids, when sister kinetochores are prone to mono-orientation. Genetic, cytological, and biochemical experiments suggest that Clp1p/Flp1p functions together with Aurora kinase at kinetochores. Together, these results suggest that Clp1p/Flp1p has a role in repairing mono-orientation of sister kinetochores.","authors":"Trautmann S, Rajagopalan S, McCollum D","authors_abbrev":"Trautmann S et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-11-05","publication_year":"2004","canto_session_key":"fbade2fc32e2063d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-04 16:19:55","canto_approved_date":"2024-03-25 16:45:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-25 19:24:09","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.15","SPCC320.13c","SPBC20F10.06","SPAC1782.09c","SPCC962.02c","SPCC736.14","SPCC338.17c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2017-01-04"},{"uniquename":"PMID:24699070","title":"Phylogenetic and comparative functional analysis of the cell-separation α-glucanase Agn1p in Schizosaccharomyces.","citation":"Microbiology (Reading) 2014 Jun;160(Pt 6):1063-1074","abstract":"The post-cytokinetic separation of cells in cell-walled organisms involves enzymic processes that degrade a specific layer of the division septum and the region of the mother cell wall that edges the septum. In the fission yeast Schizosaccharomyces pombe, the 1,3-α-glucanase Agn1p, originally identified as a mutanase-like glycoside hydrolase family 71 (GH71) enzyme, dissolves the mother cell wall around the septum edge. Our search in the genomes of completely sequenced fungi identified GH71 hydrolases in Basidiomycota, Taphrinomycotina and Pezizomycotina, but not in Saccharomycotina. The most likely Agn1p orthologues in Pezizomycotina species are not mutanases having mutanase-binding domains, but experimentally non-characterized hypothetical proteins that have no carbohydrate-binding domains. The analysis of the GH71 domains corroborated the phylogenetic relationships of the Schizosaccharomyces species determined by previous studies, but suggested a closer relationship to the Basidiomycota proteins than to the Ascomycota proteins. In the Schizosaccharomyces genus, the Agn1p proteins are structurally conserved: their GH71 domains are flanked by N-terminal secretion signals and C-terminal sequences containing the conserved block YNFNA(Y)/HTG. The inactivation of the agn1(Sj) gene in Schizosaccharomyces japonicus, the only true dimorphic member of the genus, caused a severe cell-separation defect in its yeast phase, but had no effect on the hyphal growth and yeast-to-mycelium transition. It did not affect the mycelium-to-yeast transition either, only delaying the separation of the yeast cells arising from the fragmenting hyphae. The heterologous expression of agn1(Sj) partially rescued the separation defect of the agn1Δ cells of Schizosaccharomyces pombe. The results presented indicate that the fission yeast Agn1p 1,3-α-glucanases of Schizosaccharomyces japonicus and Schizosaccharomyces pombe share conserved functions in the yeast phase.","doi":"10.1099/mic.0.077511-0","authors":"Sipiczki M, Balazs A, Monus A, Papp L, Horvath A, Sveiczer A, Miklos I","authors_abbrev":"Sipiczki M et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-04-05","publication_year":"2014","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9748261","title":"A role for Saccharomyces cerevisiae fatty acid activation protein 4 in regulating protein N-myristoylation during entry into stationary phase.","citation":"J Biol Chem 1998 Oct 02;273(40):25864-74","abstract":"Saccharomyces cerevisiae contains four known acyl-CoA synthetases (fatty acid activation proteins, Faaps). Faa1p and Faa4p activate exogenously derived fatty acids. Acyl-CoA metabolism plays a critical role in regulating protein N-myristoylation by the essential enzyme, myristoyl-CoA:protein N-myristoyltransferase (Nmt1p). In this report, we have examined whether Faa1p and Faa4p have distinct roles in affecting protein N-myristoylation as cells transition from growth in rich media to a growth-arrested state during nutrient deprivation (stationary phase). The colony-forming potential of 10 isogenic strains was defined as a function of time spent in stationary phase. These strains contained either a wild type or mutant NMT1 allele, and wild type or null alleles of each FAA. Only the combination of the Nmt mutant (nmt451Dp; reduced affinity for myristoyl-CoA) and loss of Faa4p produced a dramatic loss of colony-forming units (CFU). The progressive millionfold reduction in CFU was associated with a deficiency in protein N-myristoylation that first appeared during logarithmic growth, worsened through the post-diauxic phase, and became extreme in stationary phase. Northern and Western blot analyses plus N-myristoyltransferase assays showed that Nmt is normally present only during the log and diauxic/post-diauxic periods, indicating that N-myristoylproteins present in stationary phase are \"inherited\" from these earlier phases. Moreover, FAA4 is the only FAA induced during the critical diauxic/early post-diauxic transition. Although substitution of nmt1-451D for NMT1 results in deficiencies in protein N-myristoylation, these deficiencies are modest and limited by compensatory responses that include augmented expression of nmt1-451D and precocious induction of FAA4 in log phase. Loss of Faa4p from nmt1-451D cells severely compromises their capacity to adequately myristoylate Nmt substrates prior to entry into stationary phase since none of the other Faaps are able to functionally compensate for its absence. To identify Nmt1p substrates that may affect maintenance of proliferative potential during stationary phase, we searched the yeast genome for known and putative N-myristoylproteins. Of the 64 genes found, 48 were successfully deleted in NMT1 cells. Removal of any one of the following nine substrates produced a loss of CFU similar to that observed in nmt1-451Dfaa4Delta cells: Arf1p, Arf2p, Sip2p, Van1p, Ptc2p, YBL049W (homology to Snf7p), YJR114W, YKR007W, and YMR077C. These proteins provide opportunities to further define the molecular mechanisms that regulate survival during stationary phase.","authors":"Ashrafi K, Farazi TA, Gordon JI","authors_abbrev":"Ashrafi K et al.","pubmed_publication_date":"02 Oct 1998","pubmed_entrez_date":"1998-09-25","publication_year":"1998","canto_curator_role":"PomBase","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPCC1919.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16897687","title":"Proteomic response of Schizosaccharomyces pombe to static and oscillating extremely low-frequency electromagnetic fields.","citation":"Proteomics 2006 Sep;6(17):4755-64","abstract":"There is considerable public concern regarding the health effects of exposure to low-frequency electromagnetic fields. In addition, the association between exposure and disease incidence or the possible biological effects of exposure are unclear. Using 2D-DIGE and MS in a blind study, we have investigated the effects of static and oscillating extremely low-frequency electromagnetic fields (ELF EMFs) on the proteomes of wild type Schizosaccharomyces pombe and a Sty1p deletion mutant which displays increased sensitivity to a variety of cellular stresses. Whilst this study identifies a number of protein isoforms that display significant differential expression across experimental conditions, there was no correlation between their patterns of expression and the ELF EMF exposure regimen. We conclude that there are no significant effects of either static or oscillating EMF on the yeast proteome at the sensitivity afforded by 2D-DIGE. We hypothesise that the proteins identified must be sensitive to subtle changes in culture and/or handling conditions, and that the identification of these proteins in other proteomic studies should be treated with some caution when the results of such studies are interpreted in a biological context.","authors":"Sinclair J, Weeks M, Butt A, Worthington JL, Akpan A, Jones N, Waterfield M, Allanand D, Timms JF","authors_abbrev":"Sinclair J et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-08-10","publication_year":"2006","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9135083","title":"Schizosaccharomyces pombe gad7+ encodes a phosphoprotein with a bZIP domain, which is required for proper G1 arrest and gene expression under nitrogen starvation.","citation":"Genes Cells 1996 Apr;1(4):391-408","abstract":"Fission yeast cells arrest at G1 phase when starved of nitrogen. The molecular mechanism that ensures this arrest is poorly understood. We took a genetic approach to this problem.\nThe fission yeast gad7-1 mutant failed to arrest at G1 when starved of nitrogen, and was poor in mating and sporulation. The gad7 gene was cloned by complementation. The deduced gad7 gene product was a bZIP protein of 566 amino acids, which could bind to the CRE (cAMP response element) sequence in vitro. Disruption of gad7 resulted in the same phenotypes as gad7-1. Expression of ste11, which encodes a key transcription factor for sexual development, was not inducible in the disruptant. Gad7 was co-immunoprecipitated with another bZIP protein Pcr1, suggesting that the two proteins form a heterodimer in vivo. Gad7 was phosphorylated, and the state of its phosphorylation appeared to be modified in pka1delta or wis1delta cells.\nGad7, a CRE-binding protein that cooperates with Pcr1, is required for proper G1 arrest and gene expression under nitrogen starvation. Gad7 is a phosphoprotein, whose activity may be regulated by protein kinases including the cAMP-dependent protein kinase (Pka1) and Wis1 osmosensory MAP kinase kinase.","authors":"Kanoh J, Watanabe Y, Ohsugi M, Iino Y, Yamamoto M","authors_abbrev":"Kanoh J et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_session_key":"6ff4c9edff12167b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-17 16:09:25","canto_approved_date":"2022-03-13 13:37:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-04 11:13:48","canto_added_date":"2012-02-24 05:53:56","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC21E11.03c","SPBC106.10","SPBC409.07c","SPCC18B5.03","SPBC29B5.01","SPAC8C9.03","SPBC32C12.02"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2015-11-17"},{"uniquename":"PMID:1647355","title":"Fission yeast promoter-probe vectors based on hygromycin resistance.","citation":"Gene 1991 Apr;100:241-5","abstract":"We have constructed fission yeast vectors that carry either complete or 5'-truncated alleles of the hph gene, encoding hygromycin B phosphotransferase. We show that plasmid-borne hph can be expressed in fission yeast to confer hygromycin resistance. The vectors permit selection or screening in fission yeast for promoter activity of DNA fragments from other species. We used the vectors to identify several genomic sequences from Physarum that provide promoter function in fission yeast.","authors":"Burland TG, Pallotta D, Tardif MC, Lemieux G, Dove WF","authors_abbrev":"Burland TG et al.","pubmed_publication_date":"Apr 1991","pubmed_entrez_date":"1991-04-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16033161","title":"Prion proteins: one surprise after another.","citation":"Harvey Lect 2002;98:173-205","abstract":"","authors":"Lindquist SL","authors_abbrev":"Lindquist SL","pubmed_publication_date":"2002","pubmed_entrez_date":"2005-07-22","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15755920","title":"Dim1p is required for efficient splicing and export of mRNA encoding lid1p, a component of the fission yeast anaphase-promoting complex.","citation":"Eukaryot Cell 2005 Mar;4(3):577-87","abstract":"Schizosaccharomyces pombe Dim1p is required for maintaining the steady-state level of the anaphase-promoting complex or cyclosome (APC/C) component Lid1p and thus for maintaining the steady-state level and activity of the APC/C. To gain further insight into Dim1p function, we have investigated the mechanism whereby Dim1p influences Lid1p levels. We show that S. pombe cells lacking Dim1p or Saccharomyces cerevisiae cells lacking its ortholog, Dib1p, are defective in generalized pre-mRNA splicing in vivo, a result consistent with the identification of Dim1p as a component of the purified yeast U4/U6.U5 tri-snRNP complex. Moreover, we find that Dim1p is part of a complex with the splicing factor Prp1p. However, although Dim1p is required for efficient splicing of lid1(+) pre-mRNA, circumventing the necessity for this particular function of Dim1p is insufficient for restoring normal Lid1p levels. Finally, we provide evidence that Dim1p also participates in the nuclear export of lid1(+) mRNA and that it is likely the combined loss of both of these two Dim1p functions which compromises Lid1p levels in the absence of proper Dim1p function. These data indicate that a mechanism acting at the level of mRNA impacts the functioning of the APC/C, a critical complex in controlling mitotic progression.","authors":"Carnahan RH, Feoktistova A, Ren L, Niessen S, Yates JR, Gould KL","authors_abbrev":"Carnahan RH et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-03-10","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.05c","SPAPJ698.03c","SPBC211.02c","SPAC27F1.09c","SPBC19C2.14","SPBC646.02","SPBP22H7.07","SPBC337.06c","SPAC31G5.01","SPBC119.13c","SPBC36.09","SPAC22F8.10c","SPAC2C4.03c","SPBC3E7.13c","SPBC887.05c","SPCC188.11","SPCC550.02c","SPAC26A3.08","SPAC27D7.07c","SPBC3B9.02c","SPBC29A3.07c","SPCC1281.02c","SPCC16A11.05c","SPAC10F6.02c","SPAC4F8.12c","SPBC365.05c","SPAC9.13c","SPBC31F10.11c","SPBC6B1.10","SPCC4B3.14","SPAC227.12","SPAC22A12.09c","SPBC13E7.02","SPBC1289.11","SPAC30D11.09","SPAC4A8.09c","SPAC167.03c","SPAC644.12","SPAC9.03c","SPBC215.12","SPBC21C3.05","SPBC28F2.04c","SPBC3E7.14","SPBC8D2.09c","SPCP1E11.07c","SPBC6B1.07","SPBC16H5.05c","SPBC24C6.11","SPCC1795.11","SPAC29A4.08c","SPAC3A12.11c","SPBC4B4.05","SPBC11G11.06c","SPAC29E6.02"],"gene_count":54,"ltp_gene_count":54},{"uniquename":"PMID:25987607","title":"The Msd1-Wdr8-Pkl1 complex anchors microtubule minus ends to fission yeast spindle pole bodies.","citation":"J Cell Biol 2015 May 25;209(4):549-62","abstract":"The minus ends of spindle microtubules are anchored to a microtubule-organizing center. The conserved Msd1/SSX2IP proteins are localized to the spindle pole body (SPB) and the centrosome in fission yeast and humans, respectively, and play a critical role in microtubule anchoring. In this paper, we show that fission yeast Msd1 forms a ternary complex with another conserved protein, Wdr8, and the minus end-directed Pkl1/kinesin-14. Individual deletion mutants displayed the identical spindle-protrusion phenotypes. Msd1 and Wdr8 were delivered by Pkl1 to mitotic SPBs, where Pkl1 was tethered through Msd1-Wdr8. The spindle-anchoring defect imposed by msd1/wdr8/pkl1 deletions was suppressed by a mutation of the plus end-directed Cut7/kinesin-5, which was shown to be mutual. Intriguingly, Pkl1 motor activity was not required for its anchoring role once targeted to the SPB. Therefore, spindle anchoring through Msd1-Wdr8-Pkl1 is crucial for balancing the Cut7/kinesin-5-mediated outward force at the SPB. Our analysis provides mechanistic insight into the spatiotemporal regulation of two opposing kinesins to ensure mitotic spindle bipolarity.","doi":"10.1083/jcb.201412111","authors":"Yukawa M, Ikebe C, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"25 May 2015","pubmed_entrez_date":"2015-05-20","publication_year":"2015","canto_session_key":"a11f462edea7ec81","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2018-09-22 20:40:06","canto_approved_date":"2022-07-12 08:05:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-29 18:57:03","canto_added_date":"2015-05-21 00:19:13","annotation_curators":[{"name":"Takashi Toda","community_curator":true,"annotation_count":58,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":39,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.08","SPBC13E7.06","SPBC26H8.07c","SPAC664.10","SPBC428.20c","SPAC25G10.07c","SPAC3A11.14c","SPBC32H8.09","SPBC365.15"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2018-09-22"},{"uniquename":"PMID:20869526","title":"Fission yeast a cellular model well suited for electron microscopy investigations.","citation":"Methods Cell Biol 2010;96:235-58","abstract":"The fission yeast Schizosaccharomyces pombe has become a prominent model in molecular biology, both in yeast genetics and to investigate the molecular mechanism of the cell cycle. It has also proved to be a suitable model organism for looking at cell architecture and ultrastructure using electron microscopy (EM). Here we discuss what makes S. pombe particularly suited to EM and summarize the important discoveries regarding cell organization that have emerged from such studies. We describe the procedures and conventional methods used in EM analysis of fission yeast cells, and lay particular emphasis on cryogenic procedures, which preserve the cell structure in a near-native state, allowing elaborate three-dimensional reconstruction using electron tomography. The chapter also gives several examples of how contemporary EM approaches can be applied to provide a detailed read-out of phenotypes in this versatile cell system. A list of instruments and detailed protocols are provided together with EM-specific reagents required for sample preparation. Finally, potential new avenues of research are discussed, anticipating forthcoming topics in EM as well as new approaches to fission yeast research in the future.","doi":"10.1016/S0091-679X(10)96011-1","authors":"Roque H, Antony C","authors_abbrev":"Roque H et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-09-28","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12659963","title":"Effects of hexavalent chromium on the plasma membranes of sensitive and tolerant mutants of Schizosaccharomyces pombe. An EPR study.","citation":"Biochim Biophys Acta 2003 Apr 01;1611(1-2):217-22","abstract":"The interactions of chromium(VI) with the plasma membranes of chromium-sensitive (chr-51S) and chromium-tolerant (chr1-66T) mutants and their parental strain (6chr(+)) of a Schizosaccharomyces pombe strain were studied by electron paramagnetic resonance (EPR) spectroscopy. 5-doxylstearic acid (5-SASL) and 3-doxylbutyric acid (HO-185) spin probes were used to label the membranes. The order parameter S from the EPR spectra was calculated at different temperatures (0-25 degrees C) in order to characterize the internal dynamics of the membranes. In control experiments, both mutants exhibited differences in structural transitions in the both 5-SASL- and the HO-185-labeled membranes in comparison with their parental strain, suggesting differences in the membrane composition and/or rotational dynamics of these mutants. Addition of K(2)Cr(2)O(7) (225 microM) induced small decreases in the phase transition temperatures of the 5-SASL-labeled membranes of the parental and chromium-sensitive strains. More pronounced effects of the chromium compound on the HO-185-labeled membranes were detected as evidence that the membrane perturbations are mostly localized in the environment of the lipid-water interface.","authors":"Farkas N, Pesti M, Belagyi J","authors_abbrev":"Farkas N et al.","pubmed_publication_date":"01 Apr 2003","pubmed_entrez_date":"2003-03-28","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30773398","title":"Set7 Is a H3K37 Methyltransferase in Schizosaccharomyces pombe and Is Required for Proper Gametogenesis.","citation":"Structure 2019 Apr 02;27(4):631-638.e8","abstract":"Histone methylation by histone methyltransferases (HMTases) has a key role in transcriptional regulation. Discrepancies between the known HMTases and the histone lysine methylome suggest that HMTases remain to be identified. Here we report the discovery, characterization, and crystal structure of Schizosaccharomyces pombe Set7, an HMTase methylating the uncharted histone H3 lysine 37 (H3K37) mark. Set7 forms a dimer with its substrate-binding site structurally specific to K37, not the neighboring well-studied K36 mark. We also discovered that H3K37 methylation levels dramatically increase during gametogenesis. Set7 deletion mutant cells show defects in gametogenesis and produce the abnormal number of spores with aberrant morphology. S. pombe gametogenesis shares similarities with mammalian spermatogenesis. These findings extend our understanding of epigenetic regulation during gametogenesis and support a link between Set7, the epigenetic H3K37 methyl mark, and proper gametogenesis.","doi":"10.1016/j.str.2019.01.011","authors":"Shen Y, Mevius DEHF, Caliandro R, Carrozzini B, Roh Y, Kim J, Kim S, Ha SC, Morishita M, di Luccio E","authors_abbrev":"Shen Y et al.","pubmed_publication_date":"02 Apr 2019","pubmed_entrez_date":"2019-02-19","publication_year":"2019","canto_session_key":"b7d8b3c8af45db70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Eric Diluccio","canto_first_approved_date":"2019-04-18 14:54:43","canto_approved_date":"2026-02-09 10:07:03","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-03-11 01:25:06","canto_added_date":"2019-02-20 01:15:04","annotation_curators":[{"name":"Eric Diluccio","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.04","SPAC29B12.02c","SPBC1105.11c","SPBC8D2.04","SPCC297.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-04-18","pdb_entries":[{"pdb_id":"5h6z","gene_chains":[{"gene_uniquename":"SPCC297.04c","chain":"A/B","position":"1-147"}],"title":"Crystal structure of Set7, a novel histone methyltransferase in Schizossacharomyces pombe","entry_authors":"Mevius DEHF,Shen Y,Morishita M,Carrozzini B,Caliandro R,di Luccio E","entry_authors_abbrev":"Mevius DEHF et al.","reference_uniquename":"PMID:30773398","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"5ww0","gene_chains":[{"gene_uniquename":"SPCC297.04c","chain":"A/B","position":"1-145"}],"title":"Crystal structure of Set7, a novel histone methyltransferase in Schizossacharomyces pombe","entry_authors":"Mevius DEHF,Shen Y,Morishita M,Carrozzini B,Caliandro R,di Luccio E","entry_authors_abbrev":"Mevius DEHF et al.","reference_uniquename":"PMID:30773398","experimental_method":"X-ray","resolution":"2.1"}]},{"uniquename":"EMBL:AU008890","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR31051","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:22420","SPBC16E9.19"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9395324","title":"The role of subunit VIII in the structural stability of the bc1 complex from Saccharomyces cerevisiae studied using hybrid complexes.","citation":"Eur J Biochem 1997 Nov 01;249(3):762-9","abstract":"The QCR8 genes encoding subunit VIII of the bc1 complex from Kluyveromyces lactis and Schizosaccharomyces pombe partially complement the respiratory-deficient phenotype of a S. cerevisiae QCR8-null mutant. This implies that the heterologous Qcr8 subunits can be imported by S. cerevisiae mitochondria and that they assemble to form a hybrid bc1 complex that is sufficiently active to support growth. In contrast, the QCR8 gene from bovine heart, encoding the 9.5-kDa subunit, is not able to restore respiratory function to the S. cerevisiae null mutant. This lack of functional complementation is directly attributable to the inability of S. cerevisiae mitochondria to import this protein as shown by in vitro assays. However, a hybrid gene encoding the N-terminal 26 residues of S. cerevisiae subunit VIII and the rest of the 9.5-kDa bovine heart homologue, was able to functionally complement the QCR8-null mutant, albeit to a very low extent. Successful import into S. cerevisiae mitochondria was confirmed by in vitro import experiments. Surprisingly, although assembly of these hybrid complexes is reduced to an extent that is proportional to the evolutionary distance of the homologue to S. cerevisiae, the specific activities of the assembled complexes are the same as for the wild-type bc1 complex. After solubilisation of the mitochondrial membranes with the mild detergent dodecyl maltoside, the wild-type enzyme can be inactivated by incubation at increased temperature, independent of protease activity. The rate of inactivation can be significantly increased by the addition of o-phenanthroline [Boumans, H., Grivell, L. A. & Berden, J. A. (1997) J. Biol. Chem. 272, 16753-16760]. The hybrid complexes are much more sensitive to both types of treatment. We conclude that substitution of subunit VIII by a homologous counterpart results in a loosening of the structure of the bc1 complex on the intermembrane space side, resulting in a less stable insertion of the Rieske Fe-S protein in vivo and therefore a lower stability of the assembled enzyme under certain in vitro conditions, but without an effect on catalytic activity.","authors":"Boumans H, Berden JA, Grivell LA","authors_abbrev":"Boumans H et al.","pubmed_publication_date":"01 Nov 1997","pubmed_entrez_date":"1997-12-12","publication_year":"1997","canto_session_key":"f1c410e1abd5d1f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-11-22 13:16:31","canto_approved_date":"2018-01-08 14:26:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-22 13:16:22","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1782.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-11-22"},{"uniquename":"PMID:29622660","title":"RNase H eliminates R-loops that disrupt DNA replication but is nonessential for efficient DSB repair.","citation":"EMBO Rep 2018 May;19(5)","abstract":"In  Saccharomyces cerevisiae , genome stability depends on RNases H1 and H2, which remove ribonucleotides from DNA and eliminate RNA-DNA hybrids (R-loops). In  Schizosaccharomyces pombe , RNase H enzymes were reported to process RNA-DNA hybrids produced at a double-strand break (DSB) generated by I-PpoI meganuclease. However, it is unclear if RNase H is generally required for efficient DSB repair in fission yeast, or whether it has other genome protection roles. Here, we show that  S. pombe rnh1∆ rnh201∆  cells, which lack the RNase H enzymes, accumulate R-loops and activate DNA damage checkpoints. Their viability requires critical DSB repair proteins and Mus81, which resolves DNA junctions formed during repair of broken replication forks. \"Dirty\" DSBs generated by ionizing radiation, as well as a \"clean\" DSB at a broken replication fork, are efficiently repaired in the absence of RNase H. RNA-DNA hybrids are not detected at a reparable DSB formed by fork collapse. We conclude that unprocessed R-loops collapse replication forks in  rnh1∆ rnh201∆  cells, but RNase H is not generally required for efficient DSB repair.","doi":"10.15252/embr.201745335","authors":"Zhao H, Zhu M, Limbo O, Russell P","authors_abbrev":"Zhao H et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-04-07","publication_year":"2018","canto_session_key":"27a007e297e373e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2018-04-20 11:34:04","canto_approved_date":"2018-04-20 11:34:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-04-16 17:31:09","canto_added_date":"2018-04-08 00:15:05","annotation_curators":[{"name":"Paul Russell","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.05c","SPAC30D11.10","SPBC216.05","SPCC1259.13","SPBC336.06c","SPAC4G9.02","SPCC338.08","SPAC1556.01c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2018-04-20"},{"uniquename":"PMID:15637058","title":"Extended DNA binding site in Pot1 broadens sequence specificity to allow recognition of heterogeneous fission yeast telomeres.","citation":"J Biol Chem 2005 Mar 11;280(10):9119-28","abstract":"The Pot1 (protection of telomeres) protein binds to single-stranded telomeric DNA and is essential for the protection of chromosome ends from degradation and end-to-end fusions. The Pot1 amino-terminal DNA binding domain, Pot1N, adopts an oligonucleotide/oligosaccharide binding fold and binds GGTTAC motifs cooperatively and with exceptionally high sequence specificity. We have now examined DNA binding to naturally occurring telomeric substrates based on the analysis of 100 cloned chromosome ends and in the context of the full-length Pot1 protein. Here, we describe several important differences between Pot1 and Pot1N with apparent consequences for chromosome end protection. Specifically, full-length Pot1.DNA complexes are more stable, and the minimal binding site for a Pot1 monomer is extended into two adjacent telomeric repeats. We provide evidence that Pot1 contains a second DNA binding motif that recognizes DNA with reduced sequence specificity compared with the domain present in Pot1N. The two DNA binding motifs cooperate, whereby the amino-terminal oligonucleotide/oligosaccharide binding fold determines the registry of binding, and the internal DNA binding motif stabilizes the complex and expands the protected region toward the 3' -end. Consistent with a role in chromosome end capping, Pot1 prevents access of telomerase to the 3'-end and protects against exonucleolytic degradation.","authors":"Trujillo KM, Bunch JT, Baumann P","authors_abbrev":"Trujillo KM et al.","pubmed_publication_date":"11 Mar 2005","pubmed_entrez_date":"2005-01-08","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:11970849","title":"Transcription factors regulating the response to oxidative stress in yeast.","citation":"Antioxid Redox Signal 2002 Feb;4(1):123-40","abstract":"A main avenue of defense against fungal infection uses oxidative killing of these and other microorganisms. Consequently, the ability of fungi to withstand an oxidative challenge has important implications for their ultimate pathogenicity in a host organism. Fungi also serve as an excellent model system for handling of reactive oxygen species in eukaryotic cells. For these reasons, a great deal of work has been invested in analyzing pathways involved in and the mechanisms regulating oxidative stress tolerance in fungi. The goal of this review is to discuss the current state of knowledge underlying the ability of fungal cells to mount a response to oxidative stress via activation of transcription factors. Studies in Saccharomyces cerevisiae have identified multiple transcriptional regulatory proteins that mediate tolerance to oxidative stress. Experiments focused on the fission yeast Schizosaccharomyces pombe have led to the discovery of protein kinase cascades highly related to mammalian stress-activated protein kinases. Recent studies on the pathogenic yeast Candida albicans have allowed analysis of the role of a critical oxidant-regulated transcription factor in this important human pathogen. Further understanding of oxidative stress resistance pathways in fungi is an important step toward understanding the molecular pathogenesis of these microorganisms.","authors":"Moye-Rowley WS","authors_abbrev":"Moye-Rowley WS","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-04-24","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34152622","title":"Automated tracking of S. pombe spindle elongation dynamics.","citation":"J Microsc 2021 Oct;284(1):83-94","abstract":"The mitotic spindle is a microtubule-based machine that pulls the two identical sets of chromosomes to opposite ends of the cell during cell division. The fission yeast Schizosaccharomyces pombe is an important model organism for studying mitosis due to its simple, stereotyped spindle structure and well-established genetic toolset. S. pombe spindle length is a useful metric for mitotic progression, but manually tracking spindle ends in each frame to measure spindle length over time is laborious and can limit experimental throughput. We have developed an ImageJ plugin that can automatically track S. pombe spindle length over time and replace manual or semi-automated tracking of spindle elongation dynamics. Using an algorithm that detects the principal axis of the spindle and then finds its ends, we reliably track the length of the spindle as the cell divides. The plugin integrates with existing ImageJ features, exports its data for further analysis outside of ImageJ and does not require any programming by the user. Thus, the plugin provides an accessible tool for quantification of S. pombe spindle length that will allow automatic analysis of large microscopy data sets and facilitate screening for effects of cell biological perturbations on mitotic progression.","doi":"10.1111/jmi.13044","authors":"Uzsoy ASM, Zareiesfandabadi P, Jennings J, Kemper AF, Elting MW","authors_abbrev":"Uzsoy ASM et al.","pubmed_publication_date":"Oct 2021","pubmed_entrez_date":"2021-06-21","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-06-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9765059","title":"Subcellular localization and possible function of actin, tropomyosin and actin-related protein 3 (Arp3) in the fission yeast Schizosaccharomyces pombe.","citation":"Eur J Cell Biol 1998 Aug;76(4):288-95","abstract":"We investigated subcellular localizations and interactions of actin and two actin cytoskeleton-related proteins, Cdc8 tropomyosin and actin-related protein 3, Arp3, in the fission yeast Schizosaccharomyces pombe, using specific antibodies and by gene disruption. Actin was localized to the medial microfilamentous ring in the region of the septum during cytokinesis and to cortical patches by immunoelectron microscopy. F-actin cables were detected throughout the cell cycle by fluorescent staining with Bodipy-phallacidin. Cables were often linked to the patches and to the medial ring during its formation. Tropomyosin was localized to the medial ring and the cables. It was also distributed in the cell as patches, although co-localization with F-actin was not frequent. In cdc8ts mutant cells, F-actin cables were not observed although the F-actin patches were detected and cell polarity was maintained. These observations suggest that the F-actin cables may be involved in the formation of the medial ring, and that tropomyosin plays an important role in organizing both the ring and the cable, but is not involved in the F-actin patch formation or maintenance of cell polarity. Binding of Arp3 to actin was revealed by immunoprecipitation as well as by DNase I column chromatography. Arp3 seemed to form a complex with several proteins in the cell extracts, as previously reported for other organisms. Contrary to a previous report (McCollum et al., EMBO J. 15, 6438-6446, 1996), Arp3 was found to be concentrated in the medial region from early anaphase to late cytokinesis. Following arp3 gene disruption, F-actin patches were delocalized throughout the cell and cells did not undergo polarized growth, suggesting that Arp3 influences the proper localization of the actin patches in the cell and thereby controls the polarized growth of the cell.","authors":"Arai R, Nakano K, Mabuchi I","authors_abbrev":"Arai R et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-10-09","publication_year":"1998","canto_session_key":"c8dbba9d6295c581","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-17 09:07:30","canto_approved_date":"2023-03-23 15:26:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-17 09:07:23","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC630.03","SPAC27F1.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-04-17"},{"uniquename":"PMID:9094438","title":"Identification and localization of the sod2 gene product in fission yeast.","citation":"FEBS Lett 1997 Mar 17;405(1):119-24","abstract":"Sod2, the Na+/H+ antiporter of the fission yeast Schizosaccharomyces pombe, was identified by addition of a hemagglutinin tag to the carboxyl terminus of the protein. The tagged protein was expressed in the sod2-deficient strain of S. pombe. Transformants retained tolerance to lithium (1-10 mM) at external pH values from 3.5 to 6.5. Both Na+-dependent proton uptake and active sodium extrusion were also restored in transformed cells, suggesting that a functional antiporter was present. The protein was present in a membrane fraction. In SDS PAGE it migrated as a single 47 kDa band. The protein could be efficiently solubilized with the non-ionic detergent, dodecyl maltoside. Immunofluorescent microscopy revealed an asymmetric distribution with preferable accumulation in polar tip areas. The results are the first identification and localization of the Na+/H+ exchanger in yeast cells.","authors":"Dibrov P, Smith JJ, Young PG, Fliegel L","authors_abbrev":"Dibrov P et al.","pubmed_publication_date":"17 Mar 1997","pubmed_entrez_date":"1997-03-17","publication_year":"1997","canto_session_key":"9c8ec231a8a2d503","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-03 17:32:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-04 11:15:36","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-04"},{"uniquename":"PMID:26804466","title":"Glucose restriction induces transient G2 cell cycle arrest extending cellular chronological lifespan.","citation":"Sci Rep 2016 Jan 25;6:19629","abstract":"While glucose is the fundamental source of energy in most eukaryotes, it is not always abundantly available in natural environments, including within the human body. Eukaryotic cells are therefore thought to possess adaptive mechanisms to survive glucose-limited conditions, which remain unclear. Here, we report a novel mechanism regulating cell cycle progression in response to abrupt changes in extracellular glucose concentration. Upon reduction of glucose in the medium, wild-type fission yeast cells undergo transient arrest specifically at G2 phase. This cell cycle arrest is dependent on the Wee1 tyrosine kinase inhibiting the key cell cycle regulator, CDK1/Cdc2. Mutant cells lacking Wee1 are not arrested at G2 upon glucose limitation and lose viability faster than the wild-type cells under glucose-depleted quiescent conditions, suggesting that this cell cycle arrest is required for extension of chronological lifespan. Our findings indicate the presence of a novel cell cycle checkpoint monitoring glucose availability, which may be a good molecular target for cancer therapy.","doi":"10.1038/srep19629","authors":"Masuda F, Ishii M, Mori A, Uehara L, Yanagida M, Takeda K, Saitoh S","authors_abbrev":"Masuda F et al.","pubmed_publication_date":"25 Jan 2016","pubmed_entrez_date":"2016-01-26","publication_year":"2016","canto_session_key":"0c7d8adf97f44a9f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shigeaki Saitoh","canto_first_approved_date":"2016-04-07 14:35:41","canto_approved_date":"2019-06-14 12:59:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-03-04 06:30:32","canto_added_date":"2016-01-27 01:15:31","annotation_curators":[{"name":"Shigeaki Saitoh","community_curator":true,"annotation_count":3,"orcid":"0000-0001-5408-296X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-04-07"},{"uniquename":"PMID:1128540","title":"Mutation and nuclear stage in Schizosaccharomyces pombe. II. Reverse mutations induced by x-rays in the absence of recombination.","citation":"Mutat Res 1975 Feb;27(2):235-40","abstract":"Induction of mutations by X-rays in Schizosaccharomyces pombe cells in which sister-strand recombination appears to be excluded is offered as evidence against a requirement for recombination in radiation-induced mutagenesis.","authors":"Rainaldi G, Abbondandolo A","authors_abbrev":"Rainaldi G et al.","pubmed_publication_date":"Feb 1975","pubmed_entrez_date":"1975-02-01","publication_year":"1975","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18301750","title":"Boolean network model predicts cell cycle sequence of fission yeast.","citation":"PLoS One 2008 Feb 27;3(2):e1672","abstract":"A Boolean network model of the cell-cycle regulatory network of fission yeast (Schizosaccharomyces Pombe) is constructed solely on the basis of the known biochemical interaction topology. Simulating the model in the computer faithfully reproduces the known activity sequence of regulatory proteins along the cell cycle of the living cell. Contrary to existing differential equation models, no parameters enter the model except the structure of the regulatory circuitry. The dynamical properties of the model indicate that the biological dynamical sequence is robustly implemented in the regulatory network, with the biological stationary state G1 corresponding to the dominant attractor in state space, and with the biological regulatory sequence being a strongly attractive trajectory. Comparing the fission yeast cell-cycle model to a similar model of the corresponding network in S. cerevisiae, a remarkable difference in circuitry, as well as dynamics is observed. While the latter operates in a strongly damped mode, driven by external excitation, the S. pombe network represents an auto-excited system with external damping.","doi":"10.1371/journal.pone.0001672","authors":"Davidich MI, Bornholdt S","authors_abbrev":"Davidich MI et al.","pubmed_publication_date":"27 Feb 2008","pubmed_entrez_date":"2008-02-28","publication_year":"2008","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15135028","title":"Effects of stochasticity in models of the cell cycle: from quantized cycle times to noise-induced oscillations.","citation":"J Theor Biol 2004 Jun 07;228(3):293-301","abstract":"Noise and fluctuations are ubiquitous in living systems. Still, the interaction between complex biochemical regulatory systems and the inherent fluctuations ('noise') is only poorly understood. As a paradigmatic example, we study the implications of noise on a recently proposed model of the eukaryotic cell cycle, representing a complex network of interactions between several genes and proteins. The purpose of this work is twofold: First, we show that the inclusion of noise into the description of the system accounts for several recent experimental findings, as e.g. the existence of quantized cycle times in wee1- cdc25delta double-mutant cells of fission yeast. In the main part, we then focus on more general aspects of the interplay between noise and the dynamics of the system. In particular, we demonstrate that a stochastic description leads to qualitative changes in the dynamics, such as the emergence of noise-induced oscillations. These findings will be discussed in the light of an ongoing debate on models of cell division as limit-cycle oscillators versus checkpoint mechanisms.","authors":"Steuer R","authors_abbrev":"Steuer R","pubmed_publication_date":"07 Jun 2004","pubmed_entrez_date":"2004-05-12","publication_year":"2004","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16005294","title":"Nuclear and division-plane positioning revealed by optical micromanipulation.","citation":"Curr Biol 2005 Jul 12;15(13):1212-6","abstract":"The position of the division plane affects cell shape and size, as well as tissue organization. Cells of the fission yeast Schizosaccharomyces pombe have a centrally placed nucleus and divide by fission at the cell center. Microtubules (MTs) are required for the central position of the nucleus. Genetic studies lead to the hypothesis that the position of the nucleus may determine the position of the division plane. Alternatively, the division plane may be positioned by the spindle or by morphogen gradients or reaction diffusion mechanisms. Here, we investigate the role of MTs in nuclear positioning and the role of the nucleus in division-plane positioning by displacing the nucleus with optical tweezers. A displaced nucleus returned to the cell center by MT pushing against the cell tips. Nuclear displacement during interphase or early prophase resulted in asymmetric cell division, whereas displacement during prometaphase resulted in symmetric division as in unmanipulated cells. These results suggest that the division plane is specified by the predividing nucleus. Because the yeast nucleus is centered by MTs during interphase but not in mitosis, we hypothesize that the establishment of the division plane at the beginning of mitosis is an optimal mechanism for accurate symmetric division in these cells.","authors":"Tolic-Nørrelykke IM, Sacconi L, Stringari C, Raabe I, Pavone FS","authors_abbrev":"Tolic-Nørrelykke IM et al.","pubmed_publication_date":"12 Jul 2005","pubmed_entrez_date":"2005-07-12","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10620777","title":"A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment.","citation":"Yeast 2000 Jan 15;16(1):71-80","abstract":"A genomic 38 kbp segment on the c1750 cosmid clone containing the cdc2 gene, located in the left arm of chromosome II from Schizosaccharomyces pombe, was sequenced. The segment was found to have five previously known genes, pht1, cdc2, his3, act1 and mei4. Among 11 coding sequences (CDSs) predicted by the gene finding software INTRON.PLOT., four CDSs, pi007, pi010, pi014 and pi016, had considerable similarity to 40S ribosomal protein, glycosyltransferase, cdc2-related protein kinase and alpha-1, 2-mannosyltransferase, respectively. Another unusually huge open reading frame (ORF) (pi011), consisting of 2233 amino acids, existed, having significant homology to alpha-amylase, granule-bound glycogen synthase and the Sz. pombe YS 1110 clone product at the N-terminal, middle and C-terminal regions, respectively. All the predicted 11 CDSs were experimentally analysed by RACE PCR. The sequencing of the RACE products revealed that there were two small overlaps at the 3' untranslated regions (UTRs) between pi004 and pi005 (17 bp) and between pi007 and pi008 (2 bp). The distances between 5' end of the 5'UTR and the putative translation initiation codon varied from 10 to 302 nucleotides (nt) among the nine CDSs successfully analysed by 5'-RACE. The expression level of each CDS on this clone was determined. Among the 16 genes on this clone, the previously determined genes, pht1, cdc2, his3 and act1, were found to be most highly expressed. Finally, cDNAs of all the newly identified genes were detected by RACE, proving the actual expression of these genes. The nucleotide sequence has been submitted to the EMBL database under Accession No. AB004534.","authors":"Machida M, Yamazaki S, Kunihiro S, Tanaka T, Kushida N, Jinnno K, Haikawa Y, Yamazaki J, Yamamoto S, Sekine M, Oguchi A, Nagai Y, Sakai M, Aoki K, Ogura K, Kudoh Y, Kikuchi H, Zhang MQ, Yanagida M","authors_abbrev":"Machida M et al.","pubmed_publication_date":"15 Jan 2000","pubmed_entrez_date":"2000-01-06","publication_year":"2000","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC8D2.05c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:21536008","title":"Structural and thermodynamic characterization of the adrenodoxin-like domain of the electron-transfer protein Etp1 from Schizosaccharomyces pombe.","citation":"J Inorg Biochem 2011 Jul;105(7):957-65","abstract":"The protein Etp1 of Schizosaccharomyces pombe consists of an amino-terminal COX15-like domain and a carboxy-terminal ferredoxin-like domain, Etp1(fd), which is cleaved off after mitochondrial import. The physiological function of Etp1(fd) is supposed to lie in the participation in the assembly of iron-sulfur clusters and the synthesis of heme A. In addition, the protein was shown to be the first microbial ferredoxin being able to support electron transfer in mitochondrial steroid hydroxylating cytochrome P450 systems in vivo and in vitro, replacing thereby the native redox partner, adrenodoxin. Despite a sequence similarity of 39% and the fact that fission yeast is a mesophilic organism, thermodynamic studies revealed that Etp1(fd) has a melting temperature more than 20°C higher than adrenodoxin. The three-dimensional structure of Etp1(fd) has been determined by crystallography. To the best of our knowledge it represents the first three-dimensional structure of a yeast ferredoxin. The structure-based sequence alignment of Etp1(fd) with adrenodoxin yields a rational explanation for their observed mutual exchangeability in the cytochrome P450 system. Analysis of the electron exchange with the S. pombe redox partner Arh1 revealed differences between Etp1(fd) and adrenodoxin, which might be linked to their different physiological functions in the mitochondria of mammals and yeast.","doi":"10.1016/j.jinorgbio.2011.04.001","authors":"Müller JJ, Hannemann F, Schiffler B, Ewen KM, Kappl R, Heinemann U, Bernhardt R","authors_abbrev":"Müller JJ et al.","pubmed_publication_date":"Jul 2011","pubmed_entrez_date":"2011-05-04","publication_year":"2011","canto_session_key":"bbaa96d60dc05b65","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-25 16:35:16","canto_approved_date":"2018-04-09 14:25:27","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-11 13:58:06","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B8.01c","SPAC22E12.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-10-25","pdb_entries":[{"pdb_id":"2wlb","gene_chains":[{"gene_uniquename":"SPAC22E12.10c","chain":"A/B","position":"516-603"}],"title":"Adrenodoxin-like ferredoxin Etp1fd(516-618) of Schizosaccharomyces pombe mitochondria","entry_authors":"Mueller JJ,Hannemann F,Schiffler B,Bernhardt R,Heinemann U","entry_authors_abbrev":"Mueller JJ et al.","reference_uniquename":"PMID:21536008","experimental_method":"X-ray","resolution":"2.6"}]},{"uniquename":"PMID:11426857","title":"Ethanol-induced cell aggregation (flocculation) and its physiological background in Schizosaccharomyces pombe rive 4-2-1.","citation":"Acta Biol Hung 2001;52(2-3):231-9","abstract":"Cell aggregation (flocculation) of the yeast Schizosaccharomyces pombe strain RIVE 4-2-1 developed in glucose-containing medium, but only in the presence of ethanol. Cell surface proteins which participated in cell to cell interactions were characterised by the susceptibility of flocculation to different proteolytic enzymes, heat treatment, denaturing and thiol compounds and by the inhibition of flocculation by sugars and derivatives. It was shown that a galactose-specific lectin was involved in this new type of flocculation.","authors":"Maráz A, Geleta A","authors_abbrev":"Maráz A et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-06-28","publication_year":"2001","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11942609","title":"Interactions of Cdc4p, a myosin light chain, with IQ-domain containing proteins in Schizosaccharomyces pombe.","citation":"Cell Struct Funct 2001 Dec;26(6):555-65","abstract":"The fission yeast Schizosaccharomyces pombe undergoes cell division through a medially placed actomyosin-based contractile ring. One of the key components of this ring is the F-actin based motor protein myosin II. The myosin II heavy chain Myo2p has two light-chain-binding domains, IQl and IQ2, which bind the essential light chain, Cdc4p, and the regulatory light chain, Rlc1p. Previously, we have reported the characterization of cells expressing Myo2p lacking the IQ2 domain that facilitates Myo2p interaction with Rlc1p. In this study, we have created and characterized S. pombe strains carrying precise deletions of IQ1 and the entire neck region encompassing the IQ1 and IQ2 domains. Surprisingly, we found that the entire neck region of Myo2p is dispensable for Myo2p function. Cells deleted for IQ1, IQ2 and the entire neck region of Myo2p do not display any obvious cytoskeletal abnormalities. Immunofluorescence studies indicated that Cdc4p localizes at the ring in early and late mitotic cells in a strain in which interactions of Cdc4p with both the myosin II heavy chains (Myo2p and Myp2p) are abolished. Unlike mutations in Rlc1p that are suppressed by a simultaneous deletion of its binding site on Myo2p, mutations in the essential light chain Cdc4p are not suppressed by deletion of its binding sites on Myo2p, suggesting that Cdc4p may have additional partners essential for cytokinesis. Consistent with this, we provide evidence that two other IQ-domain containing actomyosin ring proteins, Rng2p (an IQGAP-related protein) and Myo51p (a type V myosin heavy chain), physically interact with Cdc4p. We concluded that Cdc4p, a novel myosin light chain, interacts with multiple actomyosin ring components to effect cytokinesis.","authors":"D'souza VM, Naqvi NI, Wang H, Balasubramanian MK","authors_abbrev":"D'souza VM et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2002-04-11","publication_year":"2001","canto_session_key":"428e0a1e7cd80d7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-01-05 16:24:45","canto_approved_date":"2025-05-01 14:54:13","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-01-05 16:24:39","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPBC2D10.14c","SPAC4A8.05c","SPCC1919.10c","SPAC4F8.13c","SPAP8A3.08"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-01-05"},{"uniquename":"PMID:11737862","title":"RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans.","citation":"BMC Microbiol 2001;1:29","abstract":"The first two steps in the capping of cellular mRNAs are catalyzed by the enzymes RNA triphosphatase and RNA guanylyltransferase. Although structural and mechanistic differences between fungal and mammalian RNA triphosphatases recommend this enzyme as a potential antifungal target, it has not been determined if RNA triphosphatase is essential for the growth of fungal species that cause human disease.\nWe show by classical genetic methods that the triphosphatase (Pct1) and guanylyltransferase (Pce1) components of the capping apparatus in the fission yeast Schizosaccharomyces pombe are essential for growth. We were unable to disrupt both alleles of the Candida albicans RNA triphosphatase gene CaCET1, implying that the RNA triphosphatase enzyme is also essential for growth of C. albicans, a human fungal pathogen.\nOur results provide the first genetic evidence that cap synthesis is essential for growth of an organism other than Saccharomyces cerevisiae and they validate RNA triphosphatase as a target for antifungal drug discovery.","authors":"Pei Y, Schwer B, Saiz J, Fisher RP, Shuman S","authors_abbrev":"Pei Y et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-12-12","publication_year":"2001","canto_session_key":"47cef2a2368fadab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-03-27 15:37:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-10-16 09:59:27","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.08c","SPAC644.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-10-16"},{"uniquename":"PMID:39309899","title":"Optimisation of quality features of new wheat beers fermented through sequential inoculation of non- Saccharomyces and Saccharomyces  yeasts.","citation":"Heliyon 2024 Sep 30;10(18):e37598","abstract":"The choice of the starchy ingredients as well as that of the yeasts strongly can represent a useful tool to differentiate the final beers. Our research investigated twelve white beers obtained applying a 2-factor mixed 3-level/4-level experimental design. The first factor was the cereal mixture, with 3 combinations of barley malt (65 %) and unmalted wheat (35 % of common, durum, or emmer). The second factor was the yeast used to carry out the fermentation trials, i.e.: a  S. cerevisiae  starter strain (WB06); an oenological  S. cerevisiae  strain (9502); two mixed starters made of an oenological  Schizosaccharomyces pombe  strain (6956) and, alternatively, one of the two  S. cerevisiae  strains. Most beer attributes were significantly ( p  < 0.05) influenced by the two considered factors with the following exceptions: the wheat species did not affect maltotriose, maltose, pH, total and volatile acidity, floral flavour, and sweetness; the yeast did not exert significant effects on foam colour, turbidity, overall olfactory intensity, yeast flavour, and body. The flavour of fruits and aromatic herbs were not influenced by the factors studied. Alcohol content was maximised using the unmalted durum wheat (∼7 %) and  S. cerevisiae  WB06 (∼6.8 %). The beer antioxidant content was increased by the use of emmer (566 mg/L) and by the application of the mixed inoculum (478-487 mg/L). The beers made with unmalted common wheat and fermented by the  S. cerevisiae  strains alone obtained the best overall sensory score (3.7). As shown by the Principal Component Analysis, the beers were better classified by the type of unmalted wheat than by the fermenting yeast. A multiple regression analysis was performed by fitting the analytical parameters that highlighted significant differences among the beers to a second-order polynomial model. Data concerning colour, glycerol concentration, FC-TPC, and antioxidant activity were satisfactorily predicted (R 2  > 0.8) by the fitted models.","doi":"10.1016/j.heliyon.2024.e37598","authors":"Grieco F, Fiore A, Gerardi C, Tufariello M, Romano G, Baiano A","authors_abbrev":"Grieco F et al.","pubmed_publication_date":"30 Sep 2024","pubmed_entrez_date":"2024-09-23","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-09-23 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9524207","title":"Schizosaccharomyces pombe apn1 encodes a homologue of the Escherichia coli endonuclease IV family of DNA repair proteins.","citation":"Biochim Biophys Acta 1998 Mar 04;1396(1):15-20","abstract":"The Apn1 protein of the budding yeast Saccharomyces cerevisiae is a DNA repair enzyme that hydrolyzes apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. Yeast cells lacking Apn1 are hypersensitive to DNA damaging agents that produce AP sites and DNA strand breaks with blocked 3'-termini. In this study, we showed that the fission yeast Schizosaccharomyces pombe bears a homologue, Spapn1, that is 45% identical to S. cerevisiae Apn1. However, the Spapn1 gene is apparently not expressed. Active expression of S. cerevisiae Apn1 in S. pombe conferred no additional resistance to DNA damaging agents. These data suggest that the pathway by which S. pombe repairs AP sites is independent of a functional Apn1-like AP endonuclease.","authors":"Ramotar D, Vadnais J, Masson JY, Tremblay S","authors_abbrev":"Ramotar D et al.","pubmed_publication_date":"04 Mar 1998","pubmed_entrez_date":"1998-04-03","publication_year":"1998","canto_session_key":"3622eeefed7cfb40","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-03-01 10:45:26","canto_approved_date":"2024-02-16 10:21:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-03-01 10:45:20","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-03-01"},{"uniquename":"PMID:41916008","title":"The RNA molecule or the transcription process: which is critical in the regulation of fbp1 gene activation mediated by metabolic stress-induced lncRNA (mlonRNA) in fission yeast.","citation":"Biochem Biophys Res Commun 2026 Mar 26;815:153674","abstract":"Recent studies have revealed important roles of promoter-associated long noncoding RNAs (lncRNAs) in the regulation of adjacent genes. One of the first such RNA identified is the metabolic stress-induced lncRNA (mlonRNA) in fission yeast, which is involved in the activation of the fbp1 gene under glucose starvation. Whether this promoter-associated lncRNAs function through the RNA molecule itself or through the act of transcription remains a fundamental unresolved question. We here discriminate between a role of mlonRNA molecules and their transcriptional process by selectively inducing degradation of mlonRNA. To this end, we introduced hammerhead ribozyme, a self-cleaving RNA sequence, into the mlonRNA transcripts. We found that degradation of mlonRNA resulted in delayed chromatin remodeling, which was attributable to the delayed binding of a key transcription factor, Atf1 during the early phase of glucose starvation. In contrast, during the late phase of glucose starvation, when fbp1 is robustly induced, the mlonRNA degradation had no detectable effect on chromatin configuration or Atf1 binding. Notably, a mutant strain lacking mlonRNA transcription exhibited more severe defects in the chromatin remodeling and subsequent fbp1 induction. These results indicate that, in the mlonRNA-mediated regulation, the transcription process plays a pivotal role, whereas the mlonRNA molecules themselves function as a supportive regulator that facilitates a rapid response to stress. This study therefore provides a selective reevaluation of the mlonRNA molecules in fbp1 gene regulation by eliminating RNA transcripts without perturbing the transcriptional process.","doi":"10.1016/j.bbrc.2026.153674","authors":"Oe H, Hirota K","authors_abbrev":"Oe H et al.","pubmed_publication_date":"26 Mar 2026","pubmed_entrez_date":"2026-03-31","publication_year":"2026","canto_session_key":"fcc293f54f02fd5d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2026-05-22 06:20:31","canto_approved_date":"2026-05-22 06:20:31","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-04-09 23:46:55","canto_added_date":"2026-04-01 23:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.4604","SPNCRNA.1325","SPBC29B5.01","SPBC1198.14c","SPNCRNA.1326"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2026-05-22"},{"uniquename":"EMBL:AB084858","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC144.19"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19680223","title":"A non-canonical function of topoisomerase II in disentangling dysfunctional telomeres.","citation":"EMBO J 2009 Sep 16;28(18):2803-11","abstract":"The decatenation activity of topoisomerase II (Top2), which is widely conserved within the eukaryotic domain, is essential for chromosomal segregation in mitosis. It is less clear, however, whether Top2 performs the same function uniformly across the whole genome, and whether all its functions rely on decatenation. In the fission yeast, Schizosaccharomyces pombe, telomeres are bound by Taz1, which promotes smooth replication fork progression through the repetitive telomeric sequences. Hence, replication forks stall at taz1 Delta telomeres. This leads to telomeric entanglements at low temperatures (<or=20 degrees C) that cause chromosomal segregation defects and loss of viability. Here, we show that the appearance of entanglements, and the resulting cold sensitivity of taz1 Delta cells, is suppressed by mutated alleles of Top2 that confer slower catalytic turnover. This suppression does not rely on the decatenation activity of Top2. Rather, the enhanced presence of reaction intermediates in which Top2 is clamped around DNA, promotes the removal of telomeric entanglements in vivo, independently of catalytic cycle completion. We propose a model for how the clamped enzyme-DNA complex promotes proper chromosomal segregation.","doi":"10.1038/emboj.2009.223","authors":"Germe T, Miller K, Cooper JP","authors_abbrev":"Germe T et al.","pubmed_publication_date":"16 Sep 2009","pubmed_entrez_date":"2009-08-15","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7500954","title":"Hyperspeckled mutants of Schizosaccharomyces pombe: frequent mating-type switching without detectable double-strand breaks.","citation":"Mol Gen Genet 1995 Nov 27;249(3):297-300","abstract":"Mating-type (MT) switching in homothallic (h90) strains of Schizosaccharomyces pombe is initiated by a DNA double-strand break (DSB) at the distal end of the expression cassette mat1. The cis-acting smt-s1 mutation C13-P11 reduces the frequency of MT switching. It is a small deletion mapping approximately 50 bp distal to the site of the DSB. From the h90 smt-s1 strain we isolated 13 mutants with a hyperspeckled iodine reaction. In these mutants the frequency of MT switching is increased. The mutations define nine different hsp genes, none of which maps in or close to the MT region. We tested one mutant of each gene for the presence of DSBs at mat1. Curiously, in none of the h90 smt-s1 hsp strains could DSBs be detected, although some sporulate nearly as efficiently as the h90 smt-n wild type. The hsp mutations show no effect in smt-0 strains; the smt-0 deletion abolishes MT switching completely. Furthermore, we tested the interaction of hsp1-1 with swi1, swi2 and swi7 mutations. hsp1-1 has no effect in swi2 strains, whereas it increases MT switching in swi7 and, to a lesser degree, in swi1 mutants.","authors":"Michael H, Fecke HC, Fleck O, Gutz H","authors_abbrev":"Michael H et al.","pubmed_publication_date":"27 Nov 1995","pubmed_entrez_date":"1995-11-27","publication_year":"1995","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11705997","title":"Moe1 and spInt6, the fission yeast homologues of mammalian translation initiation factor 3 subunits p66 (eIF3d) and p48 (eIF3e), respectively, are required for stable association of eIF3 subunits.","citation":"J Biol Chem 2002 Jan 18;277(3):2360-7","abstract":"The protein encoded by the fission yeast gene, moe1(+) is the homologue of the p66/eIF3d subunit of mammalian translation initiation factor eIF3. In this study, we show that in fission yeast, Moe1 physically associates with eIF3 core subunits as well as with 40 S ribosomal particles as a constituent of the eIF3 protein complex that is similar in size to multisubunit mammalian eIF3. However, strains lacking moe1(+) (Deltamoe1) are viable and show no gross defects in translation initiation, although the rate of translation in the Deltamoe1 cells is about 30-40% slower than wild-type cells. Mutant Deltamoe1 cells are hypersensitive to caffeine and defective in spore formation. These phenotypes of Deltamoe1 cells are similar to those reported previously for deletion of the fission yeast int6(+) gene that encodes the fission yeast homologue of the p48/Int6/eIF3e subunit of mammalian eIF3. Further analysis of eIF3 subunits in Deltamoe1 or Deltaint6 cells shows that in these deletion strains, while all the eIF3 subunits are bound to 40 S particles, dissociation of ribosome-bound eIF3 results in the loss of stable association between the eIF3 subunits. In contrast, eIF3 isolated from ribosomes of wild-type cells are associated with one another in a protein complex. These observations suggest that Moe1 and spInt6 are each required for stable association of eIF3 subunits in fission yeast.","authors":"Bandyopadhyay A, Lakshmanan V, Matsumoto T, Chang EC, Maitra U","authors_abbrev":"Bandyopadhyay A et al.","pubmed_publication_date":"18 Jan 2002","pubmed_entrez_date":"2001-11-14","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4D7.05","SPBC646.09c","SPAC637.07"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:29643116","title":"Dynamic visits of cortical structures probe for cell size.","citation":"J Cell Biol 2018 May 07;217(5):1559-1561","abstract":"All cells show size homeostasis owing to coordination of division with growth. In this issue, Allard et al. (2018.  J. Cell Biol.  https://doi.org/10.1083/jcb.201709171) establish that transient inhibitory visits of a negative regulator of Cdk1 to cortical oligomeric platforms increase in number and duration with cell growth, suggesting how Cdk1 activation is coupled to cell size.","doi":"10.1083/jcb.201803079","authors":"Gerganova V, Martin SG","authors_abbrev":"Gerganova V et al.","pubmed_publication_date":"07 May 2018","pubmed_entrez_date":"2018-04-13","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-15 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23525885","title":"Ethanol-inducible gene expression using gld1 (+) promoter in the fission yeast Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2013 Aug;97(15):6835-43","abstract":"In the fission yeast Schizosaccharomyces pombe, the gld1 (+) gene encoding glycerol dehydrogenase is repressed by glucose and induced by ethanol and 1-propanol. The promoter region of gld1 (+) was cloned into a multicopy vector designated as pEG1 for evaluation as an ethanol-inducible expression vector using EGFP as a model heterologous protein. Expression of EGFP was repressed in the presence of high glucose and induced in the presence of ethanol, low-glucose, and 1-propanol in the absence of glucose. Addition of ethanol to cells harboring pEG1-EGFP was found to be the most effective means for inducing EGFP production. Protein yields were found to increase in proportion to ethanol concentration. As a further test of effectiveness, secreted recombinant human growth hormone was produced using the pEG1 expression vector in medium containing glycerol and ethanol. The pEG1 gene expression system is an effective tool for the production of heterologous proteins under glucose-limiting conditions, including medium containing glycerol as a carbon source.","doi":"10.1007/s00253-013-4812-2","authors":"Matsuzawa T, Tohda H, Takegawa K","authors_abbrev":"Matsuzawa T et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-03-26","publication_year":"2013","canto_session_key":"dc7659dad6b9f772","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-29 17:47:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-11 10:27:35","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13F5.03c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-04-11"},{"uniquename":"PMID:17919454","title":"Modulation of Spc1 stress-activated protein kinase activity by methylglyoxal through inhibition of protein phosphatase in the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2007 Nov 30;363(4):942-7","abstract":"Methylglyoxal, a ubiquitous metabolite derived from glycolysis has diverse physiological functions in yeast cells. Previously, we have reported that extracellularly added methylglyoxal activates Spc1, a stress-activated protein kinase (SAPK), in the fission yeast Schizosaccharomyces pombe [Y. Takatsume, S. Izawa, Y. Inoue, J. Biol. Chem. 281 (2006) 9086-9092]. Phosphorylation of Spc1 by treatment with methylglyoxal in S. pombe cells defective in glyoxalase I, an enzyme crucial for the metabolism of methylglyoxal, continues for a longer period than in wild-type cells. Here we show that methylglyoxal inhibits the activity of the protein phosphatase responsible for the dephosphorylation of Spc1 in vitro. In addition, we found that methylglyoxal inhibits human protein tyrosine phosphatase 1B (PTP1B) also. We propose a model for the regulation of the activity of the Spc1-SAPK signaling pathway by methylglyoxal in S. pombe.","authors":"Takatsume Y, Izawa S, Inoue Y","authors_abbrev":"Takatsume Y et al.","pubmed_publication_date":"30 Nov 2007","pubmed_entrez_date":"2007-10-09","publication_year":"2007","canto_session_key":"0c150cf128e60ab1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-02 10:08:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-23 18:16:50","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.12c","SPAC24B11.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-01-23"},{"uniquename":"PMID:24587136","title":"The oxidative stress responsive transcription factor Pap1 confers DNA damage resistance on checkpoint-deficient fission yeast cells.","citation":"PLoS One 2014;9(2):e89936","abstract":"Eukaryotic cells invoke mechanisms to promote survival when confronted with cellular stress or damage to the genome. The protein kinase Chk1 is an integral and conserved component of the DNA damage response pathway. Mutation or inhibition of Chk1 results in mitotic death when cells are exposed to DNA damage. Oxidative stress activates a pathway that results in nuclear accumulation of the bZIP transcription factor Pap1. We report the novel finding that fission yeast Pap1 confers resistance to drug- and non-drug-induced DNA damage even when the DNA damage checkpoint is compromised. Multi-copy expression of Pap1 restores growth to chk1-deficient cells exposed to camptothecin or hydroxyurea. Unexpectedly, increased Pap1 expression also promotes survival of chk1-deficient cells with mutations in genes encoding DNA ligase (cdc17) or DNA polymerase δ (cdc6), but not DNA replication initiation mutants. The ability of Pap1 to confer resistance to DNA damage was not specific to chk1 mutants, as it also improved survival of rad1- and rad9-deficient cells in the presence of CPT. To confer resistance to DNA damage Pap1 must localize to the nucleus and be transcriptionally active.","doi":"10.1371/journal.pone.0089936","authors":"Belfield C, Queenan C, Rao H, Kitamura K, Walworth NC","authors_abbrev":"Belfield C et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-03-04","publication_year":"2014","canto_session_key":"5619550487cc8115","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.07c","SPCC1259.13","SPBC336.04","SPAC1952.07","SPAC20G8.01","SPAC1783.07c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:26167880","title":"SR protein kinases promote splicing of nonconsensus introns.","citation":"Nat Struct Mol Biol 2015 Aug;22(8):611-7","abstract":"Phosphorylation of the spliceosome is essential for RNA splicing, yet how and to what extent kinase signaling affects splicing have not been defined on a genome-wide basis. Using a chemical genetic approach, we show in Schizosaccharomyces pombe that the SR protein kinase Dsk1 is required for efficient splicing of introns with suboptimal splice sites. Systematic substrate mapping in fission yeast and human cells revealed that SRPKs target evolutionarily conserved spliceosomal proteins, including the branchpoint-binding protein Bpb1 (SF1 in humans), by using an RXXSP consensus motif for substrate recognition. Phosphorylation of SF1 increases SF1 binding to introns with nonconsensus splice sites in vitro, and mutation of such sites to consensus relieves the requirement for Dsk1 and phosphorylated Bpb1 in vivo. Modulation of splicing efficiency through kinase signaling pathways may allow tuning of gene expression in response to environmental and developmental cues.","doi":"10.1038/nsmb.3057","authors":"Lipp JJ, Marvin MC, Shokat KM, Guthrie C","authors_abbrev":"Lipp JJ et al.","pubmed_publication_date":"Aug 2015","pubmed_entrez_date":"2015-07-14","publication_year":"2015","canto_session_key":"5c60eca96dccd1d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-07-04 17:32:10","canto_approved_date":"2024-07-04 17:32:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-04 17:31:46","canto_added_date":"2015-07-16 00:20:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":56,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.18","SPCC1620.11","SPAC27F1.09c","SPCC16C4.17","SPCC613.05c","SPBC1A4.03c","SPAPB1A10.09","SPAC3G9.05","SPBC11C11.08","SPBC17D1.02","SPBP22H7.08","SPCC1183.11","SPCC645.13","SPAC1565.08","SPAC19A8.13","SPBC646.13","SPAC1687.22c","SPAC9E9.11","SPAC25G10.01","SPBC106.04","SPCC1259.04","SPCC594.01","SPAC11H11.01","SPAC9G1.02","SPCC1322.01","SPBC725.02","SPCC162.12","SPAC1D4.11c","SPAC19A8.12","SPAC23C4.19","SPAC328.06","SPBC1289.17","SPAC23A1.09","SPAC1782.09c","SPAC1A6.09c","SPBC1685.01","SPBC32F12.11","SPAC57A7.12","SPBC725.09c","SPCC1322.10","SPCC1795.11","SPAC30D11.14c","SPCC825.05c","SPACUNK4.16c","SPBC1604.12","SPBC211.03c","SPCC962.06c","SPAP8A3.04c","SPBC887.15c","SPBC2F12.04","SPBC16H5.08c","SPCC162.07","SPBC23G7.08c","SPAC23G3.01","SPAC9G1.06c","SPBC17G9.05","SPAC1F3.06c","SPBC146.07","SPCC14G10.04","SPAC1565.05","SPAC22H12.01c","SPBC14C8.03","SPBC16H5.07c","SPAC1D4.14","SPAC13A11.01c","SPAC29B12.01","SPBC1271.02","SPBC1D7.02c","SPAC6G10.10c","SPCC1682.15","SPAC1071.10c","SPAC664.05","SPCC895.07","SPAC26F1.07","SPAC13G6.02c","SPAC1952.16","SPBC1215.01","SPAC1639.02c","SPAC17A5.06","SPAC11G7.02","SPAC10F6.02c","SPAC9E9.06c","SPCC1739.01","SPAC227.02c","SPAC3G6.01","SPBC3B9.19","SPAC21E11.05c","SPBC18E5.07","SPBC18H10.04c","SPCC777.14","SPAC1250.01","SPAC27E2.09","SPBC530.14c","SPAP8A3.12c","SPBC106.16","SPBC3B8.03","SPBC418.02","SPBC3H7.02","SPAC12G12.09","SPAC25H1.09","SPBC32H8.12c","SPBC14F5.06","SPBC31F10.09c","SPCC1682.02c","SPBC19G7.01c","SPCC777.02","SPBC14F5.04c","SPAC17C9.03","SPCC16C4.07","SPAC31A2.07c","SPCC1682.07","SPBC1703.12","SPAPB1E7.14","SPBP35G2.09","SPBC4F6.06","SPAC10F6.06","SPCC1020.09","SPCC1281.05","SPAC16.02c","SPAC11E3.02c","SPAC222.09","SPAC631.02","SPCC162.01c","SPAC6F12.16c","SPAPB8E5.06c","SPBC16H5.02","SPBC16A3.08c","SPCC297.05","SPCC1223.04c","SPBC365.11","SPAC806.03c","SPAC23G3.07c","SPAC30.01c","SPAC167.01","SPBC336.15","SPAC10F6.01c","SPBP35G2.14","SPBC14F5.05c","SPCC70.05c","SPCC417.08","SPBC16H5.12c","SPBC29A3.04","SPCP1E11.04c","SPAC227.10","SPBC16E9.16c","SPBC646.16","SPAC19G12.07c","SPAC17G6.11c","SPCC576.11","SPAC644.12","SPBC1289.04c","SPBC27.02c","SPBC336.14c","SPBC146.11c","SPBP4H10.18c","SPAC1093.06c","SPAC2C4.16c","SPAC959.09c","SPBC725.08","SPCC736.15","SPBC2D10.08c","SPBC11C11.02","SPAC140.02","SPAPB1E7.03","SPBP4H10.09","SPAC1D4.02c","SPAC23A1.08c","SPCC736.12c","SPCC1672.06c","SPAC144.13c","SPAC24B11.11c","SPBC16E9.02c","SPCC1753.04","SPAC3A11.09","SPAC20G8.05c","SPAC4F8.13c","SPAC1142.04","SPBC13E7.01","SPAC23A1.17","SPBC1685.04"],"gene_count":180,"ltp_gene_count":5,"approved_date":"2024-07-04"},{"uniquename":"PMID:34012021","title":"Fast photothermal spatial light modulation for quantitative phase imaging at the nanoscale.","citation":"Nat Commun 2021 May 19;12(1):2921","abstract":"Spatial light modulators have become an essential tool for advanced microscopy, enabling breakthroughs in 3D, phase, and super-resolution imaging. However, continuous spatial-light modulation that is capable of capturing sub-millisecond microscopic motion without diffraction artifacts and polarization dependence is challenging. Here we present a photothermal spatial light modulator (PT-SLM) enabling fast phase imaging for nanoscopic 3D reconstruction. The PT-SLM can generate a step-like wavefront change, free of diffraction artifacts, with a high transmittance and a modulation efficiency independent of light polarization. We achieve a phase-shift > π and a response time as short as 70 µs with a theoretical limit in the sub microsecond range. We used the PT-SLM to perform quantitative phase imaging of sub-diffractional species to decipher the 3D nanoscopic displacement of microtubules and study the trajectory of a diffusive microtubule-associated protein, providing insights into the mechanism of protein navigation through a complex microtubule network.","doi":"10.1038/s41467-021-23252-3","authors":"Robert HML, Holanová K, Bujak Ł, Vala M, Henrichs V, Lánský Z, Piliarik M","authors_abbrev":"Robert HML et al.","pubmed_publication_date":"19 May 2021","pubmed_entrez_date":"2021-05-20","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-06-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9573052","title":"Pom1p, a fission yeast protein kinase that provides positional information for both polarized growth and cytokinesis.","citation":"Genes Dev 1998 May 01;12(9):1356-70","abstract":"Schizosaccharomyces pombe cells have a well-defined pattern of polarized growth at the cell ends during interphase and divide symmetrically into two equal-sized daughter cells. We identified a gene, pom1, that provides positional information for both growth and division in S. pombe. pom1 mutants form functioning growth zones and division septa but show several abnormalities: (1) After division, cells initiate growth with equal frequencies from either the old or the new end; (2) most cells never switch to bipolar growth but instead grow exclusively at the randomly chosen end; (3) some cells mislocalize their growth axis altogether, leading to the formation of angled and branched cells; and (4) many cells misplace and/or misorient their septa, leading to asymmetric cell division. pom1 encodes a putative protein kinase that is concentrated at the new cell end during interphase, at both cell ends during mitosis, and at the septation site after mitosis. Small amounts of Pom1p are also found at the old cell end during interphase and associated with the actin ring during mitosis. Pom1p localization to the cell ends is independent of actin but requires microtubules and Tea1p. pom1 mutations are synthetically lethal with several other mutations that affect cytokinesis and/or the actin or microtubule cytoskeleton. Thus, Pom1p may position the growth and cytokinesis machineries by interaction with both the actin and microtubule cytoskeletons.","authors":"Bähler J, Pringle JR","authors_abbrev":"Bähler J et al.","pubmed_publication_date":"01 May 1998","pubmed_entrez_date":"1998-06-06","publication_year":"1998","canto_session_key":"74bee65e5e7abd26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-19 11:11:17","canto_approved_date":"2026-04-02 15:33:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-07 17:27:30","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPCC1223.06","SPCC4B3.15","SPBC800.05c","SPAC24H6.05","SPBC24C6.07","SPBC26H8.07c","SPAC4A8.15c","SPBC336.12c","SPAC2F7.03c","SPBC32H8.12c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2017-04-19"},{"uniquename":"PMID:10924454","title":"A new genetic method for isolating functionally interacting genes: high plo1(+)-dependent mutants and their suppressors define genes in mitotic and septation pathways in fission yeast.","citation":"Genetics 2000 Aug;155(4):1521-34","abstract":"We describe a general genetic method to identify genes encoding proteins that functionally interact with and/or are good candidates for downstream targets of a particular gene product. The screen identifies mutants whose growth depends on high levels of expression of that gene. We apply this to the plo1(+) gene that encodes a fission yeast homologue of the polo-like kinases. plo1(+) regulates both spindle formation and septation. We have isolated 17 high plo1(+)-dependent (pld) mutants that show defects in mitosis or septation. Three mutants show a mitotic arrest phenotype. Among the 14 pld mutants with septation defects, 12 mapped to known loci: cdc7, cdc15, cdc11 spg1, and sid2. One of the pld mutants, cdc7-PD1, was selected for suppressor analysis. As multicopy suppressors, we isolated four known genes involved in septation in fission yeast: spg1(+), sce3(+), cdc8(+), and rho1(+), and two previously uncharacterized genes, mpd1(+) and mpd2(+). mpd1(+) exhibits high homology to phosphatidylinositol 4-phosphate 5-kinase, while mpd2(+) resembles Saccharomyces cerevisiae SMY2; both proteins are involved in the regulation of actin-mediated processes. As chromosomal suppressors of cdc7-PD1, we isolated mutations of cdc16 that resulted in multiseptation without nuclear division. cdc16(+), dma1(+), byr3(+), byr4(+) and a truncated form of the cdc7 gene were isolated by complementation of one of these cdc16 mutations. These results demonstrate that screening for high dose-dependent mutants and their suppressors is an effective approach to identify functionally interacting genes.","authors":"Cullen CF, May KM, Hagan IM, Glover DM, Ohkura H","authors_abbrev":"Cullen CF et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2000-08-05","publication_year":"2000","canto_session_key":"0fbb3256cec3e029","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-12-10 16:21:45","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-12-10 16:20:47","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_10924454_phaf.tsv"}],"genes":["SPAC4F10.13c","SPAC17G8.10c","SPAC1F7.04","SPAC222.10c","SPAC6F6.08c","SPAC23C11.16","SPCC1739.11c","SPAC27F1.02c","SPAC1565.06c","SPAC13D6.02c","SPBC18H10.04c","SPBC21.06c","SPAC24B11.11c","SPAC13F5.05","SPAC20G8.05c"],"gene_count":15,"ltp_gene_count":13,"approved_date":"2015-12-10"},{"uniquename":"PMID:36259651","title":"Structure-based screening for functional non-coding RNAs in fission yeast identifies a factor repressing untimely initiation of sexual differentiation.","citation":"Nucleic Acids Res 2022 Oct 28;50(19):11229-11242","abstract":"Non-coding RNAs (ncRNAs) ubiquitously exist in normal and cancer cells. Despite their prevalent distribution, the functions of most long ncRNAs remain uncharacterized. The fission yeast Schizosaccharomyces pombe expresses &gt;1800 ncRNAs annotated to date, but most unconventional ncRNAs (excluding tRNA, rRNA, snRNA and snoRNA) remain uncharacterized. To discover the functional ncRNAs, here we performed a combinatory screening of computational and biological tests. First, all S. pombe ncRNAs were screened in silico for those showing conservation in sequence as well as in secondary structure with ncRNAs in closely related species. Almost a half of the 151 selected conserved ncRNA genes were uncharacterized. Twelve ncRNA genes that did not overlap with protein-coding sequences were next chosen for biological screening that examines defects in growth or sexual differentiation, as well as sensitivities to drugs and stresses. Finally, we highlighted an ncRNA transcribed from SPNCRNA.1669, which inhibited untimely initiation of sexual differentiation. A domain that was predicted as conserved secondary structure by the computational operations was essential for the ncRNA to function. Thus, this study demonstrates that in silico selection focusing on conservation of the secondary structure over species is a powerful method to pinpoint novel functional ncRNAs.","doi":"10.1093/nar/gkac825","authors":"Ono Y, Katayama K, Onuma T, Kubo K, Tsuyuzaki H, Hamada M, Sato M","authors_abbrev":"Ono Y et al.","pubmed_publication_date":"28 Oct 2022","pubmed_entrez_date":"2022-10-19","publication_year":"2022","canto_session_key":"0e755de48a2d8865","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-12-02 18:59:53","canto_approved_date":"2022-12-02 18:59:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-12-02 18:59:42","canto_added_date":"2022-10-21 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.1669","SPNCRNA.491","SPBC32C12.02"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2022-12-02"},{"uniquename":"PMID:21239883","title":"S. pombe replication protein Cdc18 (Cdc6) interacts with Swi6 (HP1) heterochromatin protein: region specific effects and replication timing in the centromere.","citation":"Cell Cycle 2011 Jan 15;10(2):323-36","abstract":"Heterochromatin in S. pombe is associated with gene silencing at telomeres, the mating locus and centromeres. The compact heterochromatin structure raises the question how it unpacks and reforms during DNA replication. We show that the essential DNA replication factor Cdc18 (CDC6) associates with heterochromatin protein 1 (Swi6) in vivo and in vitro. Biochemical mapping and mutational analysis of the association domains show that the N-terminus of Cdc18 interacts with the chromoshadow domain of Swi6. Mutations in Swi6 that disrupt this interaction disrupt silencing and delay replication in the centromere. A mutation cdc18-I43A that reduces Cdc18 association with Swi6 has no silencing defect at the centromere, but changes Swi6 distribution and accelerates the timing of centromere replication. We suggest that fine tuning of Swi6 association at replication origins is important for negative as well as positive control of replication initiation.","authors":"Li PC, Chretien L, Côté J, Kelly TJ, Forsburg SL","authors_abbrev":"Li PC et al.","pubmed_publication_date":"15 Jan 2011","pubmed_entrez_date":"2011-01-18","publication_year":"2011","canto_session_key":"d2dca1aa9a38613e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c","SPBC14C8.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12475973","title":"Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality control.","citation":"J Biol Chem 2003 Feb 28;278(9):7180-8","abstract":"RNA polymerase II (pol II) is subject to an early elongation delay induced by negative factors Spt5/Spt4 and NELF, which is overcome by the positive factor P-TEFb (Cdk9/cyclin T), a protein kinase that phosphorylates the pol II C-terminal domain (CTD) and the transcription elongation factor Spt5. Although the rationale for this arrest and restart is unclear, recent studies suggest a connection to mRNA capping, which is coupled to transcription elongation via physical and functional interactions between the cap-forming enzymes, the CTD-PO(4), and Spt5. Here we identify a novel interaction between fission yeast RNA triphosphatase Pct1, the enzyme that initiates cap formation, and Schizosaccharomyces pombe Cdk9. The C-terminal segment of SpCdk9 comprises a Pct1-binding domain distinct from the N-terminal Cdk domain. We show that the Cdk domain interacts with S. pombe Pch1, a homolog of cyclin T, and that the purified recombinant SpCdk9/Pch1 heterodimer can phosphorylate both the pol II CTD and the C-terminal domain of S. pombe Spt5. We provide genetic evidence that SpCdk9 and Pch1 are functional orthologs of the Saccharomyces cerevisiae CTD kinase Bur1/Bur2, a putative yeast P-TEFb. Mutations of the kinase active site and the regulatory T-loop of SpCdk9 abolish its activity in vivo. Deleting the C-terminal domain of SpCdk9 causes a severe growth defect. We suggest a model whereby Spt5-induced arrest of early elongation ensures a temporal window for recruitment of the capping enzymes, which in turn attract Cdk9 to alleviate the arrest. This elongation checkpoint may avoid wasteful rounds of transcription of uncapped pre-mRNAs.","authors":"Pei Y, Schwer B, Shuman S","authors_abbrev":"Pei Y et al.","pubmed_publication_date":"28 Feb 2003","pubmed_entrez_date":"2002-12-12","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.19","SPBC28F2.12","SPAC644.04","SPBC32F12.06","SPBC32H8.10"],"gene_count":5,"ltp_gene_count":3},{"uniquename":"PMID:11818066","title":"14-3-3 protein interferes with the binding of RNA to the phosphorylated form of fission yeast meiotic regulator Mei2p.","citation":"Curr Biol 2002 Jan 22;12(2):141-5","abstract":"The switch from mitosis to meiosis is controlled by the Pat1(Ran1) kinase-Mei2p system in Schizosaccharomyces pombe. Mei2p promotes both premeiotic DNA synthesis and meiosis I, and its RNA binding ability is essential for these two processes. Mei2p forms a dot structure in the nucleus prior to meiosis I, aided by a specific RNA species named \"meiRNA\". Pat1 kinase phosphorylates Mei2p on two positions and downregulates its activity. Pat1 kinase undergoes inactivation under meiotic conditions, as a result of the production of a tethering pseudosubstrate Mei3p, and accumulation of the unphosphorylated form of Mei2p commits cells to meiosis. However, the mechanism of how phosphorylation of Mei2p suppresses its activity to induce meiosis remains largely unknown. Here we show that S. pombe Rad24p, a 14-3-3 protein, functions as a negative factor for meiosis by antagonizing the function of meiRNA to promote the formation of a nuclear Mei2p dot. Rad24p binds preferentially to Mei2p phosphorylated by Pat1 kinase. It inhibits association of meiRNA to the phosphorylated form of Mei2p but not to the unphosphorylated form in vitro. We speculate that Rad24p, bound tightly to the residues phosphorylated by Pat1 kinase, may mask the RNA recognition motifs on Mei2p. This model will explain, at least partly, why phosphorylation by Pat1 kinase inhibits the meiosis-inducing activity of Mei2p.","authors":"Sato M, Watanabe Y, Akiyoshi Y, Yamamoto M","authors_abbrev":"Sato M et al.","pubmed_publication_date":"22 Jan 2002","pubmed_entrez_date":"2002-01-31","publication_year":"2002","canto_session_key":"9431349797d152cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-01-12 10:48:14","canto_approved_date":"2026-01-31 15:52:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-11 16:10:17","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPAC27D7.03c","SPNCRNA.103","SPAC8E11.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2021-01-12"},{"uniquename":"PMID:36037351","title":"A quantitative and spatial analysis of cell cycle regulators during the fission yeast cycle.","citation":"Proc Natl Acad Sci U S A 2022 Sep 06;119(36):e2206172119","abstract":"We have carried out a systems-level analysis of the spatial and temporal dynamics of cell cycle regulators in the fission yeast  Schizosaccharomyces pombe . In a comprehensive single-cell analysis, we have precisely quantified the levels of 38 proteins previously identified as regulators of the G2 to mitosis transition and of 7 proteins acting at the G1- to S-phase transition. Only 2 of the 38 mitotic regulators exhibit changes in concentration at the whole-cell level: the mitotic B-type cyclin Cdc13, which accumulates continually throughout the cell cycle, and the regulatory phosphatase Cdc25, which exhibits a complex cell cycle pattern. Both proteins show similar patterns of change within the nucleus as in the whole cell but at higher concentrations. In addition, the concentrations of the major fission yeast cyclin-dependent kinase (CDK) Cdc2, the CDK regulator Suc1, and the inhibitory kinase Wee1 also increase in the nucleus, peaking at mitotic onset, but are constant in the whole cell. The significant increase in concentration with size for Cdc13 supports the view that mitotic B-type cyclin accumulation could act as a cell size sensor. We propose a two-step process for the control of mitosis. First, Cdc13 accumulates in a size-dependent manner, which drives increasing CDK activity. Second, from mid-G2, the increasing nuclear accumulation of Cdc25 and the counteracting Wee1 introduce a bistability switch that results in a rapid rise of CDK activity at the end of G2 and thus, brings about an orderly progression into mitosis.","doi":"10.1073/pnas.2206172119","authors":"Curran S, Dey G, Rees P, Nurse P","authors_abbrev":"Curran S et al.","pubmed_publication_date":"06 Sep 2022","pubmed_entrez_date":"2022-08-29","publication_year":"2022","canto_session_key":"5f30c249c1aae9d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-08-31 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15644188","title":"Labeling and characterization of small RNAs associated with the RNA interference effector complex RITS.","citation":"Methods Enzymol 2005;392:297-307","abstract":"RNA interference (RNAi) is a gene silencing mechanism that acts at both the posttranscriptional and transcriptional levels. We have recently identified an RNA-containing complex, named RNA-induced transcriptional silencing (RITS), that directly links RNAi to transcriptional gene silencing in Schizosaccharomyces pombe. Here we review the affinity purification methods we use to isolate RITS and describe how to purify, detect, and analyze RNAs associated with this complex.","authors":"Verdel A, Moazed D","authors_abbrev":"Verdel A et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-01-13","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7844119","title":"Preparation of highly phosphorylating mitochondria from the yeast Schizosaccharomyces pombe.","citation":"J Bioenerg Biomembr 1994 Aug;26(4):447-56","abstract":"Schizosaccharomyces pombe yeast cells grown on either fermentable or respiratory media were efficiently converted to stable spheroplasts by the alpha-(1-->3)-glucanase Novozym 234 in the presence of 1.2 M sorbitol. Lysis of spheroplasts by gentle homogenization in dilute sorbitol resulted in the preparation of mitochondria with a structure similar to that observed within the starting yeast cells. The isolated mitochondria exhibited high oxidation rates with various respiratory substrates, NADH being the most efficient. The mitochondria appeared well coupled since the second State 4 rate observed after ADP consumption was identical to the initial one. The State 3 rate in the presence of ADP was completely inhibited by low oligomycin concentrations, similarly to the concomitant ATP synthesis of 900 nmol/min x mg protein. These NADH oxidation and dependent ATP-synthesis activities are much higher than those previously described for mitochondria isolated from Schizosaccharomyces pombe, and similar to the highest values reported for Saccharomyces cerevisiae.","authors":"Jault JM, Comte J, Gautheron DC, Di Pietro A","authors_abbrev":"Jault JM et al.","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31919190","title":"Hap2-Ino80-facilitated transcription promotes de novo establishment of CENP-A chromatin.","citation":"Genes Dev 2020 Feb 01;34(3-4):226-238","abstract":"Centromeres are maintained epigenetically by the presence of CENP-A, an evolutionarily conserved histone H3 variant, which directs kinetochore assembly and hence centromere function. To identify factors that promote assembly of CENP-A chromatin, we affinity-selected solubilized fission yeast CENP-A Cnp1  chromatin. All subunits of the Ino80 complex were enriched, including the auxiliary subunit Hap2. Chromatin association of Hap2 is Ies4-dependent. In addition to a role in maintenance of CENP-A Cnp1  chromatin integrity at endogenous centromeres, Hap2 is required for de novo assembly of CENP-A Cnp1  chromatin on naïve centromere DNA and promotes H3 turnover on centromere regions and other loci prone to CENP-A Cnp1  deposition. Prior to CENP-A Cnp1  chromatin assembly, Hap2 facilitates transcription from centromere DNA. These analyses suggest that Hap2-Ino80 destabilizes H3 nucleosomes on centromere DNA through transcription-coupled histone H3 turnover, driving the replacement of resident H3 nucleosomes with CENP-A Cnp1  nucleosomes. These inherent properties define centromere DNA by directing a program that mediates CENP-A Cnp1  assembly on appropriate sequences.","doi":"10.1101/gad.332536.119","authors":"Singh PP, Shukla M, White SA, Lafos M, Tong P, Auchynnikava T, Spanos C, Rappsilber J, Pidoux AL, Allshire RC","authors_abbrev":"Singh PP et al.","pubmed_publication_date":"01 Feb 2020","pubmed_entrez_date":"2020-01-11","publication_year":"2020","canto_session_key":"dcc617ca97e793d2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733409","title":"Using Pulsed-Field Gel Electrophoresis to Analyze  Schizosaccharomyces pombe  Chromosomes and Chromosomal Elements.","citation":"Cold Spring Harb Protoc 2018 Apr 02;2018(4)","abstract":"Pulsed field gel electrophoresis (PFGE) uses alternatively oriented pulsed electrical fields to separate large DNA molecules. Here, we describe PFGE protocols and conditions for separating and visualizing chromosomes between 0.5 and 6 Mb (optimal for analyzing the endogenous fission yeast chromosomes of 5.7, 4.6, and 3.5 Mb), and for shorter chromosomal elements of between 50 and 600 kb, such as the 530 kb Ch 16  minichromosome. In addition to determining chromosome size, this technique has a wide range of applications, including determining whether DNA replication or repair is complete, defining the molecular karyotype of cells, analyzing chromosomal rearrangements, assigning genes or constructs to particular chromosomes, and isolating DNA from specific chromosomes.","doi":"10.1101/pdb.prot092023","authors":"Pai CC, Walker C, Humphrey TC","authors_abbrev":"Pai CC et al.","pubmed_publication_date":"02 Apr 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32788233","title":"The  S. pombe  CDK5 ortholog Pef1 regulates sexual differentiation through control of the TORC1 pathway and autophagy.","citation":"J Cell Sci 2020 Sep 09;133(17)","abstract":"In  Schizosaccharomyces pombe , a general strategy for survival in response to environmental changes is sexual differentiation, which is triggered by TORC1 inactivation. However, mechanisms of TORC1 regulation in fission yeast remain poorly understood. In this study, we found that Pef1, which is an ortholog of mammalian CDK5, regulates the initiation of sexual differentiation through positive regulation of TORC1 activity. Conversely, deletion of  pef1  leads to activation of autophagy and subsequent excessive TORC1 reactivation during the early phases of the nitrogen starvation response. This excessive TORC1 reactivation results in the silencing of the Ste11-Mei2 pathway and mating defects. Additionally, we found that  pef1  genetically interacts with  tsc1  and  tsc2  for TORC1 regulation, and physically interacts with three cyclins, Clg1, Pas1 and Psl1. The double deletion of  clg1  and  pas1  promotes activation of autophagy and TORC1 during nitrogen starvation, similar to what is seen in  pef1Δ  cells. Overall, our work suggests that Pef1-Clg1 and Pef1-Pas1 complexes regulate initiation of sexual differentiation through control of the TSC-TORC1 pathway and autophagy.","doi":"10.1242/jcs.247817","authors":"Matsuda S, Kikkawa U, Uda H, Nakashima A","authors_abbrev":"Matsuda S et al.","pubmed_publication_date":"09 Sep 2020","pubmed_entrez_date":"2020-08-14","publication_year":"2020","canto_session_key":"ff0c7834412bc6c4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-08-15 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16C4.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"Pfam:PF10156","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:2375","SPBC31F10.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35325114","title":"Response to leucine in Schizosaccharomyces pombe (fission yeast).","citation":"FEMS Yeast Res 2022 Apr 26;22(1)","abstract":"Leucine (Leu) is a branched-chain, essential amino acid in animals, including humans. Fungi, including the fission yeast Schizosaccharomyces pombe, can biosynthesize Leu, but deletion of any of the genes in this biosynthesis leads to Leu auxotrophy. In this yeast, although a mutation in the Leu biosynthetic pathway, leu1-32, is clearly inconvenient for this species, it has increased its usefulness as a model organism in laboratories worldwide. Leu auxotrophy produces intracellular responses and phenotypes different from those of the prototrophic strains, depending on the growing environment, which necessitates a certain degree of caution in the analysis and interpretation of the experimental results. Under amino acid starvation, the amino acid-auxotrophic yeast induces cellular responses, which are conserved in higher organisms without the ability of synthesizing amino acids. This mini-review focuses on the roles of Leu in S. pombe and discusses biosynthetic pathways, contribution to experimental convenience using a plasmid specific for Leu auxotrophic yeast, signaling pathways, and phenotypes caused by Leu starvation. An accurate understanding of the intracellular responses brought about by Leu auxotrophy can contribute to research in various fields using this model organism and to the understanding of intracellular responses in higher organisms that cannot synthesize Leu.","doi":"10.1093/femsyr/foac020","authors":"Ohtsuka H, Shimasaki T, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"26 Apr 2022","pubmed_entrez_date":"2022-03-24","publication_year":"2022","canto_session_key":"9e08a5b153885482","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2022-07-01 08:32:22","canto_approved_date":"2026-01-14 23:46:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-05-12 00:49:57","canto_added_date":"2022-03-26 01:15:04","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":3,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-07-01"},{"uniquename":"Pfam:PF10198","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.10c","HGNC:19422"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU008786","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1547790","title":"Mating pheromones of the fission yeast Schizosaccharomyces pombe: purification and structural characterization of M-factor and isolation and analysis of two genes encoding the pheromone.","citation":"EMBO J 1992 Mar;11(3):951-60","abstract":"Conjugation in the fission yeast Schizosaccharomyces pombe is controlled by the action of mating pheromones. Here I describe the isolation and characterization of M-factor, the pheromone released by M-type cells. M-factor is a nanopeptide in which the carboxy-terminal cysteine residue is carboxy-methylated and S-alkylated, probably with a farnesyl residue: Tyr-Thr-Pro-Lys-Val-Pro-Tyr-Met-Cys(S-farnesyl)-OCH3. Evidence for this structure was obtained by amino acid analysis, mass spectrometry and tandem mass spectrometry of the native M-factor. Two genes encoding the M-factor were also identified and characterized. It appears that M-factor is synthesized as a larger precursor which is post-translationally cleaved and modified to yield the active pheromone. The proposed modifications are consistent with mechanisms known to exist in other yeast and higher eukaryotes.","authors":"Davey J","authors_abbrev":"Davey J","pubmed_publication_date":"Mar 1992","pubmed_entrez_date":"1992-03-01","publication_year":"1992","canto_session_key":"631cdfca46998f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-03-22 15:09:46","canto_session_submitted_date":"2012-02-16 21:37:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPJ4664.03","SPAPB8E5.05","SPAC513.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-02-16"},{"uniquename":"Pfam:PF10233","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.12c","HGNC:1365"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11956219","title":"Fep1, an iron sensor regulating iron transporter gene expression in Schizosaccharomyces pombe.","citation":"J Biol Chem 2002 Jun 21;277(25):22950-8","abstract":"Schizosaccharomyces pombe cells acquire iron under high affinity conditions through the action of a cell surface ferric reductase encoded by the frp1(+) gene and a two-component iron-transporting complex encoded by the fip1(+) and fio1(+) genes. When cells are grown in the presence of iron, transcription of all three genes is blocked. A conserved regulatory element, 5'-(A/T)GATAA-3', located upstream of the frp1(+), fip1(+), and fio1(+) genes, is necessary for iron repression. We have cloned a novel gene, termed fep1(+), which encodes an iron-sensing transcription factor. Binding studies reveal that the putative DNA binding domain of Fep1 expressed as a fusion protein in Escherichia coli specifically interacts with the 5'-(A/T)GATAA-3' sequence in an iron-dependent manner. In a fep1 Delta mutant strain, the fio1(+) gene is highly expressed and is unregulated by iron. Furthermore, the fep1 Delta mutation increases activity of the cell surface iron reductase and renders cells hypersensitive to the iron-dependent free radical generator phleomycin. Mutations in the transcriptional co-repressors tup11(+) and tup12(+) are phenocopies to fep1(+). Indeed, strains with both tup11 Delta and tup12 Delta deletions fail to sense iron. This suggests that in the presence of iron and Fep1, the Tup11 and Tup12 proteins may act as co-repressors for down-regulation of genes encoding components of the reductive iron transport machinery.","authors":"Pelletier B, Beaudoin J, Mukai Y, Labbé S","authors_abbrev":"Pelletier B et al.","pubmed_publication_date":"21 Jun 2002","pubmed_entrez_date":"2002-04-17","publication_year":"2002","canto_session_key":"59a29a545950ec9a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-15 08:09:13","canto_approved_date":"2023-07-13 19:16:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-06-12 12:23:29","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.14c","SPAC23E2.01","SPAC1F7.08","SPAC18B11.10"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-09-15"},{"uniquename":"PMID:9133664","title":"The Schizosaccharomyces pombe mra1 gene, which is required for cell growth and mating, can suppress the mating inefficiency caused by a deficit in the Ras1 activity.","citation":"Genes Cells 1996 Mar;1(3):303-15","abstract":"Schizosaccharomyces pombe Ras1 regulates two downstream pathways, namely the Byr2/Byr1/Spk1 mitogen-activated protein kinase cascade and the Cdc42sp small G protein pathway. The former is relevant to mating and sporulation, whereas the latter is relevant to mating, cell growth and cell morphology. We addressed whether Ras1 has any additional role in the regulation of cell physiology.\nUsing a specific mutation in the effector region of Ras1, we isolated a high-copy-number suppressor of the mating deficiency caused by a decrease of the Ras1 activity. The isolated gene, named mra1, encodes a novel protein of 359 amino acids, which has apparent homologues in rice and budding yeast. Disruption of mra1 indicated that it is essential for cell growth, and mutational analysis indicated that it is required for the promotion of mating. These two functions could be separated by mutations, suggesting that Mra1 is bifunctional. Overexpression of mra1 could also suppress the mating inefficiency caused by either overexpression of gap1, which is a downregulator of Ras1, or loss of function of zfs1, which is a gene relevant to the mating pheromone signalling. However, it could not suppress null mutations in genes involved in the two known pathways downstream of Ras1.\nMra1 is an apparent downstream factor of Ras1, which is essential for cell growth and relevant to mating but is not involved in the maintenance of cell morphology. Mra1 is unlikely to interact directly with the known pathways downstream of Ras1, implying that it may be a factor constituting a third pathway regulated by Ras1.","authors":"Hakuno F, Hughes DA, Yamamoto M","authors_abbrev":"Hakuno F et al.","pubmed_publication_date":"Mar 1996","pubmed_entrez_date":"1996-03-01","publication_year":"1996","canto_session_key":"413fd43e2b386dc6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-04-18 15:45:35","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-18 11:07:42","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.07c","SPBC21.05c","SPAC17H9.09c","SPBC646.12c","SPBC1718.07c","SPAC1D4.13","SPCC1442.01","SPAC16E8.09","SPAC22H10.07","SPBC1D7.05","SPAC31G5.09c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2014-09-18"},{"uniquename":"PMID:1661641","title":"Segregation of the nucleolus during mitosis in budding and fission yeast.","citation":"Cell Motil Cytoskeleton 1991;20(1):47-54","abstract":"The segregation of the nucleolus during mitosis was examined in Saccharomyces cerevisiae and Schizosaccharomyces pombe by indirect immunofluorescence using antibodies directed to highly conserved anti-nucleolus antigens. In mitotic S. pombe cells, the nucleolus appears to trail the bulk of the DNA. In wild-type cells of S. cerevisiae, the nucleolus segregates alongside the bulk of the genomic DNA. Based on its distance from the centromere, we would expect the rDNA in both organisms to segregate behind the majority of the genomic DNA, if telomeric regions trail centromeric regions as in other eukaryotes. We therefore suggest that in S. cerevisiae the nucleolus is attached to other parts of the nucleus which enable it to segregate along with the bulk of the DNA. The segregation of the nucleolus in topoisomerase mutants and nuclear division mutants of S. cerevisiae was also investigated. In cdc14 mutants which arrest at late anaphase, the vast majority of the DNA is separated, but the nucleolar antigens remain extended between the mother and daughter cells. Thus, the CDC14 gene of S. cerevisiae appears to be important for the separation of the nucleolus at mitosis.","authors":"Granot D, Snyder M","authors_abbrev":"Granot D et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10751142","title":"Tying the knot: linking cytokinesis to the nuclear cycle.","citation":"J Cell Sci 2000 May;113 ( Pt 9):1503-13","abstract":"For the survival of both the parent and the progeny, it is imperative that the process of their physical division (cytokinesis) be precisely coordinated with progression through the mitotic cell cycle. Recent studies in the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe are beginning to unravel the nature of the links between cytokinesis and the nuclear division cycle. The cyclin-dependent kinases and a novel surveillance mechanism that monitors cytokinesis and/or morphogenesis appear to play important regulatory roles in forging these links. It is becoming increasingly clear that the inactivation of the mitosis-promoting cyclin-dependent kinase, which marks the completion of the nuclear division cycle, is essential for actomyosin ring constriction and division septum assembly in both yeasts. Additionally, the spindle pole bodies are emerging as important transient locale for proteins that might play a key role in coupling the completion of mitosis to the onset of cytokinesis.","authors":"Balasubramanian MK, McCollum D, Surana U","authors_abbrev":"Balasubramanian MK et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-04-06","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35766443","title":"A multiplexed, three-dimensional pooling and next-generation sequencing strategy for creating barcoded mutant arrays: construction of a Schizosaccharomyces pombe transposon insertion library.","citation":"Nucleic Acids Res 2022 Sep 23;50(17):e102","abstract":"Arrayed libraries of defined mutants have been used to elucidate gene function in the post-genomic era. Yeast haploid gene deletion libraries have pioneered this effort, but are costly to construct, do not reveal phenotypes that may occur with partial gene function and lack essential genes required for growth. We therefore devised an efficient method to construct a library of barcoded insertion mutants with a wider range of phenotypes that can be generalized to other organisms or collections of DNA samples. We developed a novel but simple three-dimensional pooling and multiplexed sequencing approach that leveraged sequence information to reduce the number of required sequencing reactions by orders of magnitude, and were able to identify the barcode sequences and DNA insertion sites of 4391 Schizosaccharomyces pombe insertion mutations with only 40 sequencing preparations. The insertion mutations are in the genes and untranslated regions of nonessential, essential and noncoding RNA genes, and produced a wider range of phenotypes compared to the cognate deletion mutants, including novel phenotypes. This mutant library represents both a proof of principle for an efficient method to produce novel mutant libraries and a valuable resource for the S. pombe research community.","doi":"10.1093/nar/gkac546","authors":"Li Y, Molyneaux N, Zhang H, Zhou G, Kerr C, Adams MD, Berkner KL, Runge KW","authors_abbrev":"Li Y et al.","pubmed_publication_date":"23 Sep 2022","pubmed_entrez_date":"2022-06-29","publication_year":"2022","canto_session_key":"7dff448a17232311","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-07-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9605404","title":"DNA polymerase epsilon encoded by cdc20+ is required for chromosomal DNA replication in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Cells 1998 Feb;3(2):99-110","abstract":"DNA polymerase II (PolII), the homologue of mammalian DNA polymerase epsilon, is essential for chromosomal DNA replication in the budding yeast Saccharomyces cerevisiae and also participates in S-phase checkpoint control. An important issue is whether chromosomal DNA replication in other eukaryotes, including the fission yeast Schizosaccharomyces pombe--in which the characteristics of replication origins are poorly defined--also requires DNA polymerase epsilon. It has been shown that DNA polymerase epsilon is not required for the in vitro replication of SV40 DNA by human cell extracts.\nWe have cloned and sequenced S. pombe pol2+, which is identical to the cell-cycle gene cdc20+, encoding the catalytic polypeptide of DNA polymerase epsilon (Pol epsilon). The predicted amino acid sequence of Pol epsilon is highly homologous to that of S. cerevisiae PolII and human Pol epsilon. Consistent with this, the Pol epsilon polypeptide was recognized by polyclonal antibodies against S. cerevisiae PolII holoenzyme (PolII*). The terminal morphology of cells containing the disrupted pol2 gene was similar to that of DNA replication mutant cells and cdc20 mutant cells. Furthermore, the Pol epsilon activity from temperature-sensitive S. pombe cdc20 mutant cells was temperature-sensitive, and chromosomal DNA replication in the mutant cells was inhibited at the restrictive temperatures.\nThese data strongly suggest that Pol epsilon is required for normal chromosomal DNA replication in S. pombe, as is PolII in S. cerevisiae. Thus, eukaryotic chromosomal DNA is replicated differently from that of viral SV40 DNA.","authors":"Sugino A, Ohara T, Sebastian J, Nakashima N, Araki H","authors_abbrev":"Sugino A et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-05-30","publication_year":"1998","canto_session_key":"e01f3a23d82c5110","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-03-19 16:29:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-03-19 16:29:41","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-03-19"},{"uniquename":"PMID:27183195","title":"Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformation.","citation":"Nat Struct Mol Biol 2016 Jun;23(6):574-9","abstract":"The removal of the mRNA 5' cap (decapping) by Dcp2 shuts down translation and commits mRNA to full degradation. Dcp2 activity is enhanced by activator proteins such as Dcp1 and Edc1. However, owing to conformational flexibility, the active conformation of Dcp2 and the mechanism of decapping activation have remained unknown. Here, we report a 1.6-Å-resolution crystal structure of the Schizosaccharomyces pombe Dcp2-Dcp1 heterodimer in an unprecedented conformation that is tied together by an intrinsically disordered peptide from Edc1. In this ternary complex, an unforeseen rotation of the Dcp2 catalytic domain allows residues from both Dcp2 and Dcp1 to cooperate in RNA binding, thus explaining decapping activation by increased substrate affinity. The architecture of the Dcp2-Dcp1-Edc1 complex provides a rationale for the conservation of a sequence motif in Edc1 that is also present in unrelated decapping activators, thus indicating that the presently described mechanism of decapping activation is evolutionarily conserved.","doi":"10.1038/nsmb.3232","authors":"Valkov E, Muthukumar S, Chang CT, Jonas S, Weichenrieder O, Izaurralde E","authors_abbrev":"Valkov E et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-05-17","publication_year":"2016","canto_session_key":"91aceb16b53265e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-23 16:14:46","canto_approved_date":"2023-04-18 18:43:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-03 15:15:55","canto_added_date":"2016-05-19 00:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.09c","SPBC3B9.21","SPAC19A8.12"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-03-23","pdb_entries":[{"pdb_id":"5j3y","gene_chains":[{"gene_uniquename":"SPAC19A8.12","chain":"B/D","position":"1-242"},{"gene_uniquename":"SPBC3B9.21","chain":"A/C","position":"1-127"}],"title":"Crystal structure of S. pombe Dcp2:Dcp1 mRNA decapping complex","entry_authors":"Valkov E,Muthukumar S,Chang CT,Jonas S,Weichenrieder O,Izaurralde E","entry_authors_abbrev":"Valkov E et al.","reference_uniquename":"PMID:27183195","experimental_method":"X-ray","resolution":"3.288"},{"pdb_id":"5j3q","gene_chains":[{"gene_uniquename":"SPAC18G6.09c","chain":"B/D","position":"155-180"},{"gene_uniquename":"SPBC3B9.21","chain":"A/C","position":"1-127"}],"title":"Crystal structure of S. pombe Dcp1:Edc1 mRNA decapping complex","entry_authors":"Valkov E,Muthukumar S,Chang CT,Jonas S,Weichenrieder O,Izaurralde E","entry_authors_abbrev":"Valkov E et al.","reference_uniquename":"PMID:27183195","experimental_method":"X-ray","resolution":"1.87"},{"pdb_id":"5j3t","gene_chains":[{"gene_uniquename":"SPAC19A8.12","chain":"B","position":"1-242"},{"gene_uniquename":"SPAC18G6.09c","chain":"C","position":"155-180"},{"gene_uniquename":"SPBC3B9.21","chain":"A","position":"1-127"}],"title":"Crystal structure of S. pombe Dcp2:Dcp1:Edc1 mRNA decapping complex","entry_authors":"Valkov E,Muthukumar S,Chang CT,Jonas S,Weichenrieder O,Izaurralde E","entry_authors_abbrev":"Valkov E et al.","reference_uniquename":"PMID:27183195","experimental_method":"X-ray","resolution":"1.6"}]},{"uniquename":"PMID:40395999","title":"Cdc13 (cyclin B) is degraded by autophagy under sulfur depletion in fission yeast.","citation":"Autophagy Rep 2022;1(1):51-64","abstract":"Cyclins are degraded by the anaphase-promoting complex/cyclosome (APC/C)-mediated proteasome in normal mitosis. We showed that Cdc13 (cyclin B) is also degraded by macroautophagy/autophagy in sulfur-deficient fission yeast. Sulfur depletion causes G 2  cell cycle arrest and reduces cell size; however, the associated mechanisms are unknown. We found that autophagy is required for the degradation of Cdc13, which is associated with cell cycle arrest and reduced cell size, by examining cell morphology under sulfur depletion. The analysis of the Cdc13-GFP fusion protein supported the conclusion that Cdc13 is degraded by autophagy. Moreover, we showed that sulfur depletion results in the inactivation of target of rapamycin complex 1 (TORC1) activity via Ecl1-family proteins. Our data indicate that the cyclin is degraded by two different systems: APC/C-mediated proteasome and autophagy. The latter is induced under nutrient-depleted situations. This switch in degradation systems will contribute to appropriate cell cycle arrest when resources are depleted.  Abbreviations:  APC, anaphase-promoting complex; CDK, cyclin-dependent kinase; DB, destruction box; EMM, Edinburgh minimal medium; GFP, green fluorescent protein; PCR, polymerase chain reaction; TOR, target of rapamycin; UPS, ubiquitin-proteasome system.","doi":"10.1080/27694127.2022.2047442","authors":"Ohtsuka H, Hatta Y, Hayashi K, Shimasaki T, Otsubo Y, Ito Y, Tsutsui Y, Hattori N, Yamashita A, Murakami H, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2025-05-21","publication_year":"2022","canto_session_key":"d03f4f351b987011","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2025-07-02 08:37:23","canto_approved_date":"2025-07-03 10:42:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-09 04:04:52","canto_added_date":"2025-05-21 23:25:04","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":16,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F10.07c","SPBP35G2.16c","SPBC6B1.05c","SPCC70.12c","SPAC458.06","SPAC10F6.11c","SPBC582.03","SPAC1F5.10","SPCC417.09c","SPBC15D4.07c","SPAC25A8.02","SPBC11B10.09","SPAC25H1.03","SPBC4B4.10c","SPAC7D4.04","SPCC4G3.08","SPBC8E4.12c"],"gene_count":17,"ltp_gene_count":16,"approved_date":"2025-07-02"},{"uniquename":"PMID:23127610","title":"Fission yeast: in shape to divide.","citation":"Curr Opin Cell Biol 2012 Dec;24(6):858-64","abstract":"How are cell morphogenesis and cell cycle coordinated? The fission yeast is a rod-shaped unicellular organism widely used to study how a cell self-organizes in space and time. Here, we discuss recent advances in understanding how the cell acquires and maintains its regular rod shape and uses it to control cell division. The cellular body plan is established by microtubules, which mark antipodal growth zones and medial division. In turn, cellular dimensions are defined by the small GTPase Cdc42 and downstream regulators of vesicle trafficking. Yeast cells then repetitively use their simple rod shape to orchestrate the position and timing of cell division.","doi":"10.1016/j.ceb.2012.10.001","authors":"Hachet O, Bendezú FO, Martin SG","authors_abbrev":"Hachet O et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-11-07","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27432890","title":"Sar1 localizes at the rims of COPII-coated membranes in vivo.","citation":"J Cell Sci 2016 Sep 01;129(17):3231-7","abstract":"The Sar1 GTPase controls coat assembly on coat protein complex II (COPII)-coated vesicles, which mediate protein transport from the endoplasmic reticulum (ER) to the Golgi. The GTP-bound form of Sar1, activated by the ER-localized guanine nucleotide exchange factor (GEF) Sec12, associates with the ER membrane. GTP hydrolysis by Sar1, stimulated by the COPII-vesicle-localized GTPase-activating protein (GAP) Sec23, in turn causes Sar1 to dissociate from the membrane. Thus, Sar1 is cycled between active and inactive states, and on and off vesicle membranes, but its precise spatiotemporal regulation remains unknown. Here, we examined Sar1 localization on COPII-coated membranes in living Saccharomyces cerevisiae cells. Two-dimensional (2D) observation demonstrated that Sar1 showed modest accumulation around the ER exit sites (ERES) in a manner that was dependent on Sec16 function. Detailed three-dimensional (3D) observation further demonstrated that Sar1 localized at the rims of the COPII-coated membranes, but was excluded from the rest of the COPII membranes. Additionally, a GTP-locked form of Sar1 induced abnormally enlarged COPII-coated structures and covered the entirety of these structures. These results suggested that the reversible membrane association of Sar1 GTPase leads to its localization being restricted to the rims of COPII-coated membranes in vivo.","doi":"10.1242/jcs.189423","authors":"Kurokawa K, Suda Y, Nakano A","authors_abbrev":"Kurokawa K et al.","pubmed_publication_date":"01 Sep 2016","pubmed_entrez_date":"2016-07-20","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.07","SPCC31H12.07","SPBC31F10.06c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:11092853","title":"Phenotypes of fission yeast defective in ubiquinone production due to disruption of the gene for p-hydroxybenzoate polyprenyl diphosphate transferase.","citation":"J Bacteriol 2000 Dec;182(24):6933-9","abstract":"Ubiquinone is an essential component of the electron transfer system in both prokaryotes and eukaryotes and is synthesized from chorismate and polyprenyl diphosphate by eight steps. p-Hydroxybenzoate (PHB) polyprenyl diphosphate transferase catalyzes the condensation of PHB and polyprenyl diphosphate in ubiquinone biosynthesis. We isolated the gene (designated ppt1) encoding PHB polyprenyl diphosphate transferase from Schizosaccharomyces pombe and constructed a strain with a disrupted ppt1 gene. This strain could not grow on minimal medium supplemented with glucose. Expression of COQ2 from Saccharomyces cerevisiae in the defective S. pombe strain restored growth and enabled the cells to produce ubiquinone-10, indicating that COQ2 and ppt1 are functional homologs. The ppt1-deficient strain required supplementation with antioxidants, such as cysteine, glutathione, and alpha-tocopherol, to grow on minimal medium. This suggests that ubiquinone can act as an antioxidant, a premise supported by our observation that the ppt1-deficient strain is sensitive to H(2)O(2) and Cu(2+). Interestingly, we also found that the ppt1-deficient strain produced a significant amount of H(2)S, which suggests that oxidation of sulfide by ubiquinone may be an important pathway for sulfur metabolism in S. pombe. Ppt1-green fluorescent protein fusion proteins localized to the mitochondria, indicating that ubiquinone biosynthesis occurs in the mitochondria in S. pombe. Thus, analysis of the phenotypes of S. pombe strains deficient in ubiquinone production clearly demonstrates that ubiquinone has multiple functions in the cell apart from being an integral component of the electron transfer system.","authors":"Uchida N, Suzuki K, Saiki R, Kainou T, Tanaka K, Matsuda H, Kawamukai M","authors_abbrev":"Uchida N et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-28","publication_year":"2000","canto_session_key":"3e6436d7b5c490a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-13 12:35:29","canto_approved_date":"2024-09-08 11:33:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-16 13:55:12","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC56F8.04c","SPBPJ4664.01","SPBC2G5.06c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-12-13"},{"uniquename":"EMBL:AU006722","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24825827","title":"Every laboratory with a fluorescence microscope should consider counting molecules.","citation":"Mol Biol Cell 2014 May;25(10):1545-8","abstract":"Protein numbers in cells determine rates of biological processes, influence the architecture of cellular structures, reveal the stoichiometries of protein complexes, guide in vitro biochemical reconstitutions, and provide parameter values for mathematical modeling. The purpose of this essay is to increase awareness of methods for counting protein molecules using fluorescence microscopy and encourage more cell biologists to report these numbers. We address the state of the field in terms of utility and accuracy of the numbers reported and point readers to references for details of specific techniques and applications.","doi":"10.1091/mbc.E13-05-0249","authors":"Coffman VC, Wu JQ","authors_abbrev":"Coffman VC et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2014-05-15","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-01-16 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35277511","title":"The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme.","citation":"Nat Commun 2022 Mar 11;13(1):1277","abstract":"The telomerase holoenzyme is critical for maintaining eukaryotic genome integrity. In addition to a reverse transcriptase and an RNA template, telomerase contains additional proteins that protect the telomerase RNA and promote holoenzyme assembly. Here we report that the methyl phosphate capping enzyme (MePCE) Bmc1/Bin3 is a stable component of the S. pombe telomerase holoenzyme. Bmc1 associates with the telomerase holoenzyme and U6 snRNA through an interaction with the recently described LARP7 family member Pof8, and we demonstrate that these two factors are evolutionarily linked in fungi. Our data suggest that the association of Bmc1 with telomerase is independent of its methyltransferase activity, but rather that Bmc1 functions in telomerase holoenzyme assembly by promoting TER1 accumulation and Pof8 recruitment to TER1. Taken together, this work yields new insight into the composition, assembly, and regulation of the telomerase holoenzyme in fission yeast as well as the breadth of its evolutionary conservation.","doi":"10.1038/s41467-022-28985-3","authors":"Porat J, El Baidouri M, Grigull J, Deragon JM, Bayfield MA","authors_abbrev":"Porat J et al.","pubmed_publication_date":"11 Mar 2022","pubmed_entrez_date":"2022-03-12","publication_year":"2022","canto_session_key":"c49f61a6f4aa2c82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mark Bayfield","canto_first_approved_date":"2022-05-30 11:28:19","canto_approved_date":"2022-06-01 11:53:31","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-05-18 15:39:57","canto_added_date":"2022-03-15 01:15:05","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":31,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Mark Bayfield","community_curator":true,"annotation_count":3,"orcid":"0000-0002-8971-7598","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC285.12","SPCC18B5.09c","SPCC1840.10","SPBC20F10.09","SPNCRNA.214","SPBC2A9.10","SPAC25B8.16","SPSNRNA.06","SPAC2F3.17c","SPCC1620.01c","SPAC1F3.01","SPAC17G6.17","SPBC29A3.14c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2022-05-30"},{"uniquename":"PMID:41311426","title":"Dual spatio-functional control of a fission yeast-based bioprocessor upon chemical induction.","citation":"RSC Chem Biol 2025 Nov 17;","abstract":"Next-generation therapies are advancing beyond small molecules and proteins toward engineered living microorganisms that interact symbiotically with their host and respond to signals precisely when and where needed. Despite progress in the field, engineering cells to both produce biopharmaceuticals and achieve site-specific recruitment remains a challenge. In this work, we genetically engineered the mating pathway of  S. pombe  to create a \"bioprocessor\" that responds to a chemical trigger, an artificial replica of the sexual pheromone of the yeast cells, the P-factor, enabling functional control over the production of Albulin as a proof-of-concept biopharmaceutical. This activation simultaneously induces the expression of hydrophobic agglutinins on the cell surface, modifying surface chemistry and adhesion properties. Exploiting this modification, we could simultaneously implement spatial control, allowing selective adhesion to a hydrophobic target surface. Adhesion control tests confirmed the fundamental role of hydrophobic interactions in this adhesion process, enabling selective cell adherence only after activation with P-factor and expression of the agglutinins, even in presence of potentially interfering cells. This approach represents an important milestone in the development of a straightforward chemically-activated multi-control mechanisms, which enable precise and programmable responses in engineered cells. Such advancements pave the way for a new generation of bio-responsive materials and therapeutic devices, including functional implants and targeted delivery systems, where engineered cells can operate in synergy with host tissues, responding to specific environmental cues to produce therapeutic agents exactly when and where they are needed.","doi":"10.1039/d5cb00147a","authors":"Sakellakou SM, Migeot V, Carloni LE, Martino E, Sequeira AO, Morávková T, Riccio L, Melinte S, Maggini L, Hermand D, Bonifazi D","authors_abbrev":"Sakellakou SM et al.","pubmed_publication_date":"17 Nov 2025","pubmed_entrez_date":"2025-11-28","publication_year":"2025","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2025-11-29 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37923140","title":"Iron homeostasis proteins Grx4 and Fra2 control activity of the Schizosaccharomyces pombe iron repressor Fep1 by facilitating [2Fe-2S] cluster removal.","citation":"J Biol Chem 2023 Nov 03;299(12):105419","abstract":"The Bol2 homolog Fra2 and monothiol glutaredoxin Grx4 together play essential roles in regulating iron homeostasis in Schizosaccharomyces pombe. In vivo studies indicate that Grx4 and Fra2 act as coinhibitory partners that inactivate the transcriptional repressor Fep1 in response to iron deficiency. In Saccharomyces cerevisiae, Bol2 is known to form a [2Fe-2S]-bridged heterodimer with the monothiol Grxs Grx3 and Grx4, with the cluster ligands provided by conserved residues in Grx3/4 and Bol2 as well as GSH. In this study, we characterized this analogous [2Fe-2S]-bridged Grx4-Fra2 complex in S. pombe by identifying the specific residues in Fra2 that act as ligands for the Fe-S cluster and are required to regulate Fep1 activity. We present spectroscopic and biochemical evidence confirming the formation of a [2Fe-2S]-bridged Grx4-Fra2 heterodimer with His66 and Cys29 from Fra2 serving as Fe-S cluster ligands in S. pombe. In vivo transcription and growth assays confirm that both His66 and Cys29 are required to fully mediate the response of Fep1 to low iron conditions. Furthermore, we analyzed the interaction between Fep1 and Grx4-Fra2 using CD spectroscopy to monitor changes in Fe-S cluster coordination chemistry. These experiments demonstrate unidirectional [2Fe-2S] cluster transfer from Fep1 to Grx4-Fra2 in the presence of GSH, revealing the Fe-S cluster dependent mechanism of Fep1 inactivation mediated by Grx4 and Fra2 in response to iron deficiency.","doi":"10.1016/j.jbc.2023.105419","authors":"Hati D, Brault A, Gupta M, Fletcher K, Jacques JF, Labbé S, Outten CE","authors_abbrev":"Hati D et al.","pubmed_publication_date":"03 Nov 2023","pubmed_entrez_date":"2023-11-03","publication_year":"2023","canto_session_key":"005334747ce0c70e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Caryn Outten","canto_first_approved_date":"2024-07-05 09:54:22","canto_approved_date":"2025-05-27 09:55:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-19 17:07:56","canto_added_date":"2023-11-07 00:25:05","annotation_curators":[{"name":"Caryn Outten","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":12,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.11","SPAC23E2.01","SPBC1683.09c","SPBC26H8.06"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-07-05"},{"uniquename":"PMID:18664736","title":"The heterochromatin protein 1 (HP1) family: put away a bias toward HP1.","citation":"Mol Cells 2008 Sep 30;26(3):217-27","abstract":"Heterochromatin protein 1 (HP1) was first described in Drosophila melanogaster as a heterochromatin associated protein with dose-dependent effect on gene silencing. The HP1 family is evolutionarily highly conserved and there are multiple members within the same species. The multi-functionality of HP1 reflects its ability to interact with diverse nuclear proteins, ranging from histones and transcriptional co-repressors to cohesion and DNA replication factors. As its name suggests, HP1 is well-known as a silencing protein found at pericentromeres and telomeres. In contrast to previous views that heterochromatin is transcriptionally inactive; noncoding RNAs transcribed from heterochromatic DNA repeats regulates the assembly and function of heterochromatin ranging from fission yeast to animals. Moreover, more recent progress has shed light on the paradoxical properties of HP1 in the nucleus and has revealed, unexpectedly, its existence in the euchromatin. Therefore, HP1 proteins might participate in both transcription repression in heterochromatin and euchromatin.","authors":"Kwon SH, Workman JL","authors_abbrev":"Kwon SH et al.","pubmed_publication_date":"30 Sep 2008","pubmed_entrez_date":"2008-07-31","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1729129","title":"DNA polymerase alpha in the fission yeast Schizosaccharomyces pombe: identification and tracing of the catalytic subunit during the cell cycle.","citation":"Exp Cell Res 1992 Feb;198(2):183-90","abstract":"A recombinant protein was obtained in Escherichia coli by subcloning part of the Schizosaccharomyces pombe POL1 gene at the 3'-end of lacZ. Antibodies raised against this protein were used to identify the POL1 gene product in extracts of exponentially growing S. pombe cells. A major 170-kDa protein, whose structure and properties were typical of the catalytic subunit of eukaryotic DNA polymerases alpha (pol alpha), was detected. The same antibodies were used to trace pol alpha and to quantify its level during the S. pombe cell cycle. We found that pol alpha was present at all stages of the cycle and that its cellular pool was subject to limited (three-fold) increase in G1 and S phases, with a decline to the initial level soon after. In addition, we found that a second form of pol alpha with slightly lower molecular weight (165 kDa) existed only during late G1 and S phases. Moreover, absence of initiation or perturbations in the course of DNA replication induced overproduction of the 165-kDa form.","authors":"Bouvier D, Pignede G, Damagnez V, Tillit J, de Recondo AM, Baldacci G","authors_abbrev":"Bouvier D et al.","pubmed_publication_date":"Feb 1992","pubmed_entrez_date":"1992-02-01","publication_year":"1992","canto_session_key":"eb4e74785db97cc4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-24 10:26:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-18 08:13:39","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3H5.06c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-04-18"},{"uniquename":"PMID:25122751","title":"Binding of the transcription factor Atf1 to promoters serves as a barrier to phase nucleosome arrays and avoid cryptic transcription.","citation":"Nucleic Acids Res 2014;42(16):10351-9","abstract":"Schizosaccharomyces pombe displays a large transcriptional response common to several stress conditions, regulated primarily by the transcription factor Atf1. Atf1-dependent promoters contain especially broad nucleosome depleted regions (NDRs) prior to stress imposition. We show here that basal binding of Atf1 to these promoters competes with histones to create wider NDRs at stress genes. Moreover, deletion of atf1 results in nucleosome disorganization specifically at stress coding regions and derepresses antisense transcription. Our data indicate that the transcription factor binding to promoters acts as an effective barrier to fix the +1 nucleosome and phase downstream nucleosome arrays to prevent cryptic transcription.","doi":"10.1093/nar/gku704","authors":"García P, Paulo E, Gao J, Wahls WP, Ayté J, Lowy E, Hidalgo E","authors_abbrev":"García P et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-08-15","publication_year":"2014","canto_session_key":"369d95f63c03066b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Patricia Garcia","canto_first_approved_date":"2016-03-31 12:01:49","canto_approved_date":"2023-07-10 16:48:33","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-10-16 12:56:15","canto_added_date":"2014-08-16 00:15:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Patricia Garcia","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.05","SPCC757.07c","SPBC215.05","SPBC29B5.01","SPAC3G6.01","SPAP8A3.04c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-03-31"},{"uniquename":"PMID:23074192","title":"Pmt1, a Dnmt2 homolog in Schizosaccharomyces pombe, mediates tRNA methylation in response to nutrient signaling.","citation":"Nucleic Acids Res 2012 Dec;40(22):11648-58","abstract":"The fission yeast Schizosaccharomyces pombe carries a cytosine 5-methyltransferase homolog of the Dnmt2 family (termed pombe methyltransferase 1, Pmt1), but contains no detectable DNA methylation. Here, we found that Pmt1, like other Dnmt2 homologs, has in vitro methylation activity on cytosine 38 of tRNA(Asp) and, to a lesser extent, of tRNA(Glu), despite the fact that it contains a non-consensus residue in catalytic motif IV as compared with its homologs. In vivo tRNA methylation also required Pmt1. Unexpectedly, however, its in vivo activity showed a strong dependence on the nutritional status of the cell because Pmt1-dependent tRNA methylation was induced in cells grown in the presence of peptone or with glutamate as a nitrogen source. Furthermore, this induction required the serine/threonine kinase Sck2, but not the kinases Sck1, Pka1 or Tor1 and was independent of glucose signaling. Taken together, this work reveals a novel connection between nutrient signaling and tRNA methylation that thus may link tRNA methylation to processes downstream of nutrient signaling like ribosome biogenesis and translation initiation.","doi":"10.1093/nar/gks956","authors":"Becker M, Müller S, Nellen W, Jurkowski TP, Jeltsch A, Ehrenhofer-Murray AE","authors_abbrev":"Becker M et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-10-18","publication_year":"2012","canto_session_key":"4a7f9665ed7386e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-17 19:51:00","canto_approved_date":"2021-07-16 10:24:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-21 11:58:13","canto_added_date":"2012-11-13 08:02:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.10c","SPATRNAGLU.01","SPATRNAASP.01","SPAC23C4.17","SPBC106.10","SPATRNAASP.02","SPBC19C2.02","SPAC22E12.14c","SPAC1B9.02c","SPATRNAGLU.02","SPAC17D4.04"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2017-04-17"},{"uniquename":"PMID:41585493","title":"Fission yeast Whi5 represses MBF-dependent transcription in quiescent cells.","citation":"iScience 2026 Feb 20;29(2):114576","abstract":"When cells arrest in G1 to enter quiescence, the transcriptional machinery that drives the G1/S transition must be inactivated. In budding yeast and mammals, this repression is mediated by the Whi5 and Retinoblastoma (Rb) proteins, which inhibit the SBF and E2F transcription factors, respectively. In fission yeast, the MBF complex is functionally analogous to SBF and E2F, and Whi5/Mug54 has been predicted to act as a G1/S transcriptional repressor. Here, we show that upon nitrogen starvation, Whi5 accumulates in the nucleus and is required to repress MBF-dependent genes during quiescence. Mass spectrometry and bimolecular fluorescence complementation (BiFC) demonstrate that Whi5 physically associates with components of both the MBF complex and the histone deacetylase Clr6-I complex. Moreover, Whi5 is required for the interaction between MBF and Clr6-I, supporting a model in which Whi5 represses MBF-dependent genes in quiescent cells by recruiting HDAC activity to their promoters.","doi":"10.1016/j.isci.2025.114576","authors":"Gálvez-Merchán C, López-San Segundo R, Suárez MB, González-Álvarez D, Ayté J, Pérez-Hidalgo L, Moreno S","authors_abbrev":"Gálvez-Merchán C et al.","pubmed_publication_date":"20 Feb 2026","pubmed_entrez_date":"2026-01-26","publication_year":"2026","canto_session_key":"94f9813a9b422f6e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-01-29 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18265321","title":"Introduction of DNA into S. pombe cells.","citation":"Curr Protoc Mol Biol 2003 Nov;Chapter 13:Unit 13.17","abstract":"Methods of transformation rely upon conditioning cells to take up DNA, and growing them under selective conditions to establish and maintain the plasmid or integration. Different methods may be used, including electroporation, treatment with lithium cations, or protoplast treatment which removes the cell wall. Protoplasts prepared as for transformation can also be induced to fuse with each other and undergo karyogamy, which provides a means of mating sterile strains.","doi":"10.1002/0471142727.mb1317s64","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2008-02-12","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24559510","title":"Interaction of apurinic/apyrimidinic endonuclease 2 (Apn2) with Myh1 DNA glycosylase in fission yeast.","citation":"DNA Repair (Amst) 2014 Mar;15:1-10","abstract":"Oxidative DNA damage is repaired primarily by the base excision repair (BER) pathway in a process initiated by removal of base lesions or mismatched bases by DNA glycosylases. MutY homolog (MYH, MUTYH, or Myh1) is a DNA glycosylase which excises adenine paired with the oxidative lesion 8-oxo-7,8-dihydroguanine (8-oxoG, or G°), thus reducing G:C to T:A mutations. The resulting apurinic/apyrimidinic (AP) site is processed by an AP-endonuclease or a bifunctional glycosylase/lyase. We show here that the major Schizosaccharomyces pombe AP endonuclease, Apn2, binds to the inter-domain connector located between the N- and C-terminal domains of Myh1. This Myh1 inter-domain connector also interacts with the Hus1 subunit of the Rad9-Rad1-Hus1 checkpoint clamp. Mutagenesis studies indicate that Apn2 and Hus1 bind overlapping but different sequence motifs on Myh1. Mutation on I(261) of Myh1 reduces its interaction with Hus1, but only slightly attenuates its interaction with Apn2. However, E(262) of Myh1 is a key determinant for both Apn2 and Hus1 interactions. Like human APE1, Apn2 has 3'-phosphodiesterase activity. However, unlike hAPE1, Apn2 has a weak AP endonuclease activity which cleaves the AP sites generated by Myh1 glycosylase. Functionally, Apn2 stimulates Myh1 glycosylase activity and Apn2 phosphodiesterase activity is stimulated by Myh1. The cross stimulation of Myh1 and Apn2 enzymatic activities is dependent on their physical interaction. Thus, Myh1 and Apn2 constitute an initial BER complex.","doi":"10.1016/j.dnarep.2014.01.001","authors":"Jin J, Hwang BJ, Chang PW, Toth EA, Lu AL","authors_abbrev":"Jin J et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-02-25","publication_year":"2014","canto_session_key":"7c14e2249d56f984","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-25 11:34:00","canto_approved_date":"2022-11-01 13:31:54","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-03-28 10:27:02","canto_added_date":"2014-03-20 17:50:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.10","SPAC26A3.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-02-25"},{"uniquename":"PMID:10588638","title":"Replication factor C3 of Schizosaccharomyces pombe, a small subunit of replication factor C complex, plays a role in both replication and damage checkpoints.","citation":"Mol Biol Cell 1999 Dec;10(12):3991-4003","abstract":"We report here the isolation and functional analysis of the rfc3(+) gene of Schizosaccharomyces pombe, which encodes the third subunit of replication factor C (RFC3). Because the rfc3(+) gene was essential for growth, we isolated temperature-sensitive mutants. One of the mutants, rfc3-1, showed aberrant mitosis with fragmented or unevenly separated chromosomes at the restrictive temperature. In this mutant protein, arginine 216 was replaced by tryptophan. Pulsed-field gel electrophoresis suggested that rfc3-1 cells had defects in DNA replication. rfc3-1 cells were sensitive to hydroxyurea, methanesulfonate (MMS), and gamma and UV irradiation even at the permissive temperature, and the viabilities after these treatments were decreased. Using cells synchronized in early G2 by centrifugal elutriation, we found that the replication checkpoint triggered by hydroxyurea and the DNA damage checkpoint caused by MMS and gamma irradiation were impaired in rfc3-1 cells. Association of Rfc3 and Rad17 in vivo and a significant reduction of the phosphorylated form of Chk1 in rfc3-1 cells after treatments with MMS and gamma or UV irradiation suggested that the checkpoint signal emitted by Rfc3 is linked to the downstream checkpoint machinery via Rad17 and Chk1. From these results, we conclude that rfc3(+) is required not only for DNA replication but also for replication and damage checkpoint controls, probably functioning as a checkpoint sensor.","authors":"Shimada M, Okuzaki D, Tanaka S, Tougan T, Tamai KK, Shimoda C, Nojima H","authors_abbrev":"Shimada M et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-12-10","publication_year":"1999","canto_session_key":"a7499c82e9c96202","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-18 19:32:34","canto_approved_date":"2026-01-29 16:08:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-18 17:08:21","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":27,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.13","SPCC1259.13","SPAC27E2.10c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2016-04-18"},{"uniquename":"PMID:19073698","title":"Identification of protein-coding sequences using the hybridization of 18S rRNA and mRNA during translation.","citation":"Nucleic Acids Res 2009 Feb;37(2):591-601","abstract":"We introduce a new approach in this article to distinguish protein-coding sequences from non-coding sequences utilizing a period-3, free energy signal that arises from the interactions of the 3'-terminal nucleotides of the 18S rRNA with mRNA. We extracted the special features of the amplitude and the phase of the period-3 signal in protein-coding regions, which is not found in non-coding regions, and used them to distinguish protein-coding sequences from non-coding sequences. We tested on all the experimental genes from Saccharomyces cerevisiae and Schizosaccharomyces pombe. The identification was consistent with the corresponding information from GenBank, and produced better performance compared to existing methods that use a period-3 signal. The primary tests on some fly, mouse and human genes suggests that our method is applicable to higher eukaryotic genes. The tests on pseudogenes indicated that most pseudogenes have no period-3 signal. Some exploration of the 3'-tail of 18S rRNA and pattern analysis of protein-coding sequences supported further our assumption that the 3'-tail of 18S rRNA has a role of synchronization throughout translation elongation process. This, in turn, can be utilized for the identification of protein-coding sequences.","doi":"10.1093/nar/gkn917","authors":"Xing C, Bitzer DL, Alexander WE, Vouk MA, Stomp AM","authors_abbrev":"Xing C et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-12-17","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7885834","title":"Cloning and characterisation of the Schizosaccharomyces pombe rad32 gene: a gene required for repair of double strand breaks and recombination.","citation":"Nucleic Acids Res 1995 Feb 11;23(3):383-8","abstract":"A new Schizosaccharomyces pombe mutant (rad32) which is sensitive to gamma and UV irradiation is described. Pulsed field gel electrophoresis of DNA from irradiated cells indicates that the rad32 mutant, in comparison to wild type cells, has decreased ability to repair DNA double strand breaks. The mutant also undergoes decreased meiotic recombination and displays reduced stability of minichromosomes. The rad32 gene has been cloned by complementation of the UV sensitive phenotype. The gene, which is not essential for cell viability and is expressed at a moderate level in mitotically dividing cells, has significant homology to the meiotic recombination gene MRE11 of Saccharomyces cerevisiae. Epistasis analysis indicates that rad32 functions in a pathway which includes the rhp51 gene (the S.pombe homologue to S.cerevisiae RAD51) and that cells deleted for the rad32 gene in conjunction with either the rad3 deletion (a G2 checkpoint mutation) or the rad2 deletion (a chromosome stability and potential nucleotide excision repair mutation) are not viable.","authors":"Tavassoli M, Shayeghi M, Nasim A, Watts FZ","authors_abbrev":"Tavassoli M et al.","pubmed_publication_date":"11 Feb 1995","pubmed_entrez_date":"1995-02-11","publication_year":"1995","canto_session_key":"cb6a65f348103325","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-08-02 15:38:35","canto_approved_date":"2022-02-03 20:48:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-15 17:28:00","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.06c","SPBC3E7.08c","SPBC216.05","SPAC13C5.07"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-08-02"},{"uniquename":"PMID:39379376","title":"Ribosomes hibernate on mitochondria during cellular stress.","citation":"Nat Commun 2024 Oct 08;15(1):8666","abstract":"Cell survival under nutrient-deprived conditions relies on cells' ability to adapt their organelles and rewire their metabolic pathways. In yeast, glucose depletion induces a stress response mediated by mitochondrial fragmentation and sequestration of cytosolic ribosomes on mitochondria. This cellular adaptation promotes survival under harsh environmental conditions; however, the underlying mechanism of this response remains unknown. Here, we demonstrate that upon glucose depletion protein synthesis is halted. Cryo-electron microscopy structure of the ribosomes show that they are devoid of both tRNA and mRNA, and a subset of the particles depicted a conformational change in rRNA H69 that could prevent tRNA binding. Our in situ structural analyses reveal that the hibernating ribosomes tether to fragmented mitochondria and establish eukaryotic-specific, higher-order storage structures by assembling into oligomeric arrays on the mitochondrial surface. Notably, we show that hibernating ribosomes exclusively bind to the outer mitochondrial membrane via the small ribosomal subunit during cellular stress. We identify the ribosomal protein Cpc2/RACK1 as the molecule mediating ribosomal tethering to mitochondria. This study unveils the molecular mechanism connecting mitochondrial stress with the shutdown of protein synthesis and broadens our understanding of cellular responses to nutrient scarcity and cell quiescence.","doi":"10.1038/s41467-024-52911-4","authors":"Gemin O, Gluc M, Rosa H, Purdy M, Niemann M, Peskova Y, Mattei S, Jomaa A","authors_abbrev":"Gemin O et al.","pubmed_publication_date":"08 Oct 2024","pubmed_entrez_date":"2024-10-08","publication_year":"2024","canto_session_key":"43e8214a9219b277","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ahmad Jomaa","canto_first_approved_date":"2024-11-13 11:08:59","canto_approved_date":"2025-01-18 12:42:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-10-24 13:01:34","canto_added_date":"2024-10-11 23:25:05","annotation_curators":[{"name":"Ahmad Jomaa","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie 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S. pombe ribosome large subunit","entry_authors":"Gluc M,Gemin O,Purdy M,Mattei S,Jomaa A","entry_authors_abbrev":"Gluc M et 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S. pombe ribosome","entry_authors":"Gluc M,Gemin O,Purdy M,Mattei S,Jomaa A","entry_authors_abbrev":"Gluc M et al.","reference_uniquename":"PMID:39379376","experimental_method":"EM","resolution":"2.4"}]},{"uniquename":"PMID:28733405","title":"Analysis of DNA Replication in Fission Yeast by Combing.","citation":"Cold Spring Harb Protoc 2018 Mar 01;2018(3)","abstract":"DNA replication studies based on population experiments give an average estimate of replication kinetics from many cells. This average replication profile masks the stochastic nature of origin firing in eukaryotes, which is revealed by using single-molecule techniques, such as DNA combing. The analysis of replication kinetics by DNA combing involves isolating DNA from cells that have been pulse-labeled with thymidine analogs and stretching it on a silanized coverslip. The analog-labeled patches on the stretched DNA fibers can then be detected using fluorescent antibodies against the analog. Each fiber represents a part of the genome from a single cell; therefore, it is possible to study the variation in behavior of individual origins from one cell to another. Furthermore, each DNA fiber is uniformly stretched, making it possible to measure distances accurately at kilobase resolution. It is also possible to stretch a high density of fibers on coverslips enabling quantitative data collection.","doi":"10.1101/pdb.prot092015","authors":"Iyer DR, Das S, Rhind N","authors_abbrev":"Iyer DR et al.","pubmed_publication_date":"01 Mar 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4647695","title":"Estimation of parameters in population models for Schizosaccharomyces pombe from chemostat data.","citation":"Biotechnol Bioeng 1972 Nov;14(6):915-38","abstract":"","authors":"Kothari IR, Martin GC, Reilly PJ, Martin PJ, Eakman JM","authors_abbrev":"Kothari IR et al.","pubmed_publication_date":"Nov 1972","pubmed_entrez_date":"1972-11-01","publication_year":"1972","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29476094","title":"A family of unconventional deubiquitinases with modular chain specificity determinants.","citation":"Nat Commun 2018 Feb 23;9(1):799","abstract":"Deubiquitinating enzymes (DUBs) regulate ubiquitin signaling by trimming ubiquitin chains or removing ubiquitin from modified substrates. Similar activities exist for ubiquitin-related modifiers, although the enzymes involved are usually not related. Here, we report human ZUFSP (also known as ZUP1 and C6orf113) and fission yeast Mug105 as founding members of a DUB family different from the six known DUB classes. The crystal structure of human ZUFSP in covalent complex with propargylated ubiquitin shows that the DUB family shares a fold with UFM1- and Atg8-specific proteases, but uses a different active site more similar to canonical DUB enzymes. ZUFSP family members differ widely in linkage specificity through differential use of modular ubiquitin-binding domains (UBDs). While the minimalistic Mug105 prefers K48 chains, ZUFSP uses multiple UBDs for its K63-specific endo-DUB activity. K63 specificity, localization, and protein interaction network suggest a role for ZUFSP in DNA damage response.","doi":"10.1038/s41467-018-03148-5","authors":"Hermanns T, Pichlo C, Woiwode I, Klopffleisch K, Witting KF, Ovaa H, Baumann U, Hofmann K","authors_abbrev":"Hermanns T et al.","pubmed_publication_date":"23 Feb 2018","pubmed_entrez_date":"2018-02-25","publication_year":"2018","canto_session_key":"ea00a954772bc114","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-04-16 11:52:22","canto_approved_date":"2018-04-28 12:28:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-28 12:28:01","canto_added_date":"2018-02-28 22:13:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.08c","SPAC25H1.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-04-16"},{"uniquename":"PMID:19037101","title":"Mus81, Rhp51(Rad51), and Rqh1 form an epistatic pathway required for the S-phase DNA damage checkpoint.","citation":"Mol Biol Cell 2009 Feb;20(3):819-33","abstract":"The S-phase DNA damage checkpoint slows the rate of DNA synthesis in response to damage during replication. In the fission yeast Schizosaccharomyces pombe, Cds1, the S-phase-specific checkpoint effector kinase, is required for checkpoint signaling and replication slowing; upon treatment with the alkylating agent methyl methane sulfonate, cds1Delta mutants display a complete checkpoint defect. We have identified proteins downstream of Cds1 required for checkpoint-dependant slowing, including the structure-specific endonuclease Mus81 and the helicase Rqh1, which are implicated in replication fork stability and the negative regulation of recombination. Removing Rhp51, the Rad51 recombinase homologue, suppresses the slowing defect of rqh1Delta mutants, but not that of mus81Delta mutant, defining an epistatic pathway in which mus81 is epistatic to rhp51 and rhp51 is epistatic to rqh1. We propose that restraining recombination is required for the slowing of replication in response to DNA damage.","authors":"Willis N, Rhind N","authors_abbrev":"Willis N et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-11-28","publication_year":"2009","canto_session_key":"102f75d6a405d489","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-01-08 18:22:11","canto_approved_date":"2021-11-17 17:10:07","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-19 16:05:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":44,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1142.03c","SPBC28F2.07","SPAC20H4.07","SPBC216.05","SPAC694.06c","SPAC30D11.10","SPAC4H3.05","SPAC3C7.03c","SPAC644.14c","SPCC18B5.11c","SPAC2G11.12","SPBC409.03","SPBC216.06c","SPCC4G3.05c","SPBC428.08c","SPAPB1E7.06c","SPCC23B6.03c","SPAC664.01c","SPBC4F6.15c","SPAC15A10.03c","SPAC8E11.03c"],"gene_count":21,"ltp_gene_count":21,"approved_date":"2015-01-08"},{"uniquename":"PMID:9348288","title":"Mal3, the fission yeast homologue of the human APC-interacting protein EB-1 is required for microtubule integrity and the maintenance of cell form.","citation":"J Cell Biol 1997 Nov 03;139(3):717-28","abstract":"Through a screen designed to isolate novel fission yeast genes required for chromosome segregation, we have identified mal3+. The mal3-1 mutation decreased the transmission fidelity of a nonessential minichromosome and altered sensitivity to microtubule-destabilizing drugs. Sequence analysis revealed that the 35-kD Mal3 is a member of an evolutionary conserved protein family. Its human counterpart EB-1 was identified in an interaction screen with the tumour suppressor protein APC. EB-1 was able to substitute for the complete loss of the mal3+ gene product suggesting that the two proteins might have similar functions. Cells containing a mal3 null allele were viable but showed a variety of phenotypes, including impaired control of cell shape. A fusion protein of Mal3 with the Aequorea victoria green fluorescent protein led to in vivo visualization of both cytoplasmic and mitotic microtubule structures indicating association of Mal3 with microtubules. The absence of Mal3 protein led to abnormally short, often faint cytoplasmic microtubules as seen by indirect antitubulin immunofluorescence. While loss of the mal3+ gene product had no gross effect on mitotic spindle morphology, overexpression of mal3+ compromised spindle formation and function and led to severe growth inhibition and abnormal cell morphology. We propose that Mal3 plays a role in regulating the integrity of microtubules possibly by influencing their stability.","authors":"Beinhauer JD, Hagan IM, Hegemann JH, Fleig U","authors_abbrev":"Beinhauer JD et al.","pubmed_publication_date":"03 Nov 1997","pubmed_entrez_date":"1997-11-14","publication_year":"1997","canto_session_key":"dbb40646c21b43dd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-22 15:33:57","canto_approved_date":"2022-02-03 20:13:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-17 12:32:52","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPBC16A3.15c","SPBC26H8.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-09-22"},{"uniquename":"EMBL:AU006993","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31611173","title":"Temperature-sensitive cytoophidium assembly in Schizosaccharomyces pombe.","citation":"J Genet Genomics 2019 Sep 20;46(9):423-432","abstract":"The metabolic enzyme CTP synthase (CTPS) is able to compartmentalize into filaments, termed cytoophidia, in a variety of organisms including bacteria, budding yeast, fission yeast, fruit flies and mammals. A previous study in budding yeast shows that the filament-forming process of CTPS is not sensitive to temperature shift. Here we study CTPS filamentation in the fission yeast Schizosaccharomyces pombe. To our surprise, we find that both the length and the occurrence of cytoophidia in S. pombe decrease upon cold shock or heat shock. The temperature-dependent changes of cytoophidia are fast and reversible. Taking advantage of yeast genetics, we demonstrate that heat-shock proteins are required for cytoophidium assembly in S. pombe. Temperature sensitivity of cytoophidia makes S. pombe an attractive model system for future investigations of this novel membraneless organelle.","doi":"10.1016/j.jgg.2019.09.002","authors":"Zhang J, Liu JL","authors_abbrev":"Zhang J et al.","pubmed_publication_date":"20 Sep 2019","pubmed_entrez_date":"2019-10-16","publication_year":"2019","canto_session_key":"22ce1c41d43e1aef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-23 22:24:49","canto_approved_date":"2019-10-23 22:24:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-23 22:24:38","canto_added_date":"2019-10-17 00:15:21","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC10F6.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-10-23"},{"uniquename":"PMID:15056885","title":"A set of loxP marker cassettes for Cre-mediated multiple gene disruption in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2004 Mar;68(3):545-50","abstract":"For functional analysis, the presence of gene families and isoenzymes often makes it necessary to delete more than one gene, while the number of marker genes is limited in Schizosaccharomyces pombe. Here we describe a loxP-flanked ura4(+) cassette and Cre recombinase vector for a Cre-loxP-mediated marker removal procedure in S. pombe. This loxP-ura4-loxP cassette can be used for disruption of hmt1(+) as a model target gene. We have constructed two vectors which express Cre recombinase under the control of the nmt1 or nmt41 promoter. Excisive recombination at loxP sites in the chromosome was promoted efficiently and accurately when the Cre recombinase was expressed under the control of the nmt41 promoter. In addition, ura4(+) could be excised from the genome by Cre recombinase, when a single loxP site was adjacent to ura4. The use of the Cre-loxP system proved to be a practical strategy to excise a marker gene for repeated use in S. pombe.","authors":"Iwaki T, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-04-02","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1823651","title":"Formation and reversion of Schizosaccharomyces pombe cells with apical protoplast protuberances.","citation":"Folia Microbiol (Praha) 1991;36(2):153-7","abstract":"Lytic enzymes from the hepatopancreas of Helix pomatia do not induce a uniform digestion of the cell wall of Schizosaccharomyces pombe over the entire cell surface. Perforations are formed in growth zones through which a protoplast can locally protrude. Conditions were found under which the frequency of formation of apical protoplast protuberances is higher than 90% cells with such protuberances can reverse to normally multiplying cells.","authors":"Zemanová Z, Pavlícek I, Vondrejs V","authors_abbrev":"Zemanová Z et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17442892","title":"The conserved Spc7 protein is required for spindle integrity and links kinetochore complexes in fission yeast.","citation":"Mol Biol Cell 2007 Jul;18(7):2441-54","abstract":"Spc7, a member of the conserved Spc105/KNL-1 family of kinetochore proteins, was identified as an interaction partner of the EB1 homologue Mal3. Spc7 associates with the central centromere region of the chromosome but does not affect transcriptional silencing. Here, we show that Spc7 is required for the integrity of the spindle as well as for targeting of MIND but not of Ndc80 complex components to the kinetochore. Spindle defects in spc7 mutants were severe ranging from the inability to form a bipolar spindle in early mitosis to broken spindles in midanaphase B. spc7 mutant phenotypes were partially rescued by extra alpha-tubulin or extra Mal2. Thus, Spc7 interacts genetically with the Mal2-containing Sim4 complex.","authors":"Kerres A, Jakopec V, Fleig U","authors_abbrev":"Kerres A et al.","pubmed_publication_date":"Jul 2007","pubmed_entrez_date":"2007-04-20","publication_year":"2007","canto_session_key":"17ce40c3c1fbe060","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-16 15:28:59","canto_approved_date":"2026-01-30 15:24:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-19 14:38:41","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1020.02","SPBC18E5.03c","SPBC20F10.06","SPAC25B8.14","SPCC895.07","SPBC800.05c","SPBC409.04c","SPBC21.01","SPAC3G9.12","SPBC32F12.08c","SPCC736.14","SPBC106.01","SPBC336.08","SPAC688.02c","SPAC27F1.04c","SPAC1687.20c"],"gene_count":16,"ltp_gene_count":14,"approved_date":"2016-10-16"},{"uniquename":"PMID:15280647","title":"Bioinformatic analysis of the link between gene composition and expressivity in Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Antonie Van Leeuwenhoek 2004 Aug;86(2):135-47","abstract":"The compositional non-randomness was studied in genes of Saccharomyces cerevisiae and Schizosaccharomyces pombe. In both species, codon usage is well correlated with expressivity (measured as the codon adaptation index). Both species generally display higher nucleotide non-randomness in the group of highly expressed genes than in the lowly expressed genes. The highly expressed genes in both species are furthermore characterized by marked peaks in non-randomness at N=3 upstream of start codons, N=2 downstream of start codons and at N=1 and N=7 downstream of stop codons, indicating that these nucleotides may be key elements in translational regulation. Intragenic variation in codon usage was also observed to be linked to expressivity. It is suggested that the firm link between expressivity and codon usage calls for codon optimization. Based on bioinformatic calculations, examples of proteins are given for which codon optimizations might be relevant.","authors":"Fuglsang A","authors_abbrev":"Fuglsang A","pubmed_publication_date":"Aug 2004","pubmed_entrez_date":"2004-07-29","publication_year":"2004","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21123655","title":"Break-induced ATR and Ddb1-Cul4(Cdt)² ubiquitin ligase-dependent nucleotide synthesis promotes homologous recombination repair in fission yeast.","citation":"Genes Dev 2010 Dec 01;24(23):2705-16","abstract":"Nucleotide synthesis is a universal response to DNA damage, but how this response facilitates DNA repair and cell survival is unclear. Here we establish a role for DNA damage-induced nucleotide synthesis in homologous recombination (HR) repair in fission yeast. Using a genetic screen, we found the Ddb1-Cul4(Cdt)² ubiquitin ligase complex and ribonucleotide reductase (RNR) to be required for HR repair of a DNA double-strand break (DSB). The Ddb1-Cul4(Cdt)² ubiquitin ligase complex is required for degradation of Spd1, an inhibitor of RNR in fission yeast. Accordingly, deleting spd1(+) suppressed the DNA damage sensitivity and the reduced HR efficiency associated with loss of ddb1(+) or cdt2(+). Furthermore, we demonstrate a role for nucleotide synthesis in postsynaptic gap filling of resected ssDNA ends during HR repair. Finally, we define a role for Rad3 (ATR) in nucleotide synthesis and HR through increasing Cdt2 nuclear levels in response to DNA damage. Our findings support a model in which break-induced Rad3 and Ddb1-Cul4(Cdt)² ubiquitin ligase-dependent Spd1 degradation and RNR activation promotes postsynaptic ssDNA gap filling during HR repair.","doi":"10.1101/gad.1970810","authors":"Moss J, Tinline-Purvis H, Walker CA, Folkes LK, Stratford MR, Hayles J, Hoe KL, Kim DU, Park HO, Kearsey SE, Fleck O, Holmberg C, Nielsen O, Humphrey TC","authors_abbrev":"Moss J et al.","pubmed_publication_date":"01 Dec 2010","pubmed_entrez_date":"2010-12-03","publication_year":"2010","canto_session_key":"d105ec6194bdcab4","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.03","SPAC17H9.19c","SPBC29A10.05","SPCC126.02c","SPAC17H9.10c","SPBC216.05"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:422679","title":"Analysis of the significance of a periodic, cell size-controlled doubling in rates of macromolecular synthesis for the control of balanced exponential growth of fission yeast cells.","citation":"J Cell Sci 1979 Feb;35:41-51","abstract":"Mutant strains of the fission yeast Schizosaccharomyces pombe are available which divide at smaller mean sizes than wild type. Earlier work by the present authors has shown that all these strains double their rates of polyadenylated messenger RNA synthesis as a step once in each cell cycle. The smaller the cell, the later in the cycle is the doubling in rate of synthesis. Strains of all sizes, however, double their synthetic rate when at the same threshold size. We show here that the differences in cell cycle stage of doubling in rate of polyadenylated messenger RNA synthesis are enough to explain the reduced mean steady state polyadenylated messenger RNA contents of the smaller strains. The cell size-related control over doubling in rate of synthesis is also shown to maintain the mean polyadenylated messenger RNA content as a constant proportion of cell mass, irrespective of cell size. This control thus allows cells to maintain balanced exponential growth, even when absolute growth rate per cell is altered by mutation. It is also shown that the concentration of polyadenylated messenger RNA itself could act as a monitor of the threshold size triggering the doubling in rate of synthesis in each cell cycle.","authors":"Barnes A, Nurse P, Fraser RS","authors_abbrev":"Barnes A et al.","pubmed_publication_date":"Feb 1979","pubmed_entrez_date":"1979-02-01","publication_year":"1979","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28369658","title":"Tracking the evolution of 3D gene organization demonstrates its connection to phenotypic divergence.","citation":"Nucleic Acids Res 2017 May 05;45(8):4330-4343","abstract":"It has recently been shown that the organization of genes in eukaryotic genomes, and specifically in 3D, is strongly related to gene expression and function and partially conserved between organisms. However, previous studies of 3D genomic organization analyzed each organism independently from others. Here, we propose an approach for unified inter-organismal analysis of gene organization based on a network representation of Hi-C data. We define and detect four classes of spatially co-evolving orthologous modules (SCOMs), i.e. gene families that co-evolve in their 3D organization, based on patterns of divergence and conservation of distances. We demonstrate our methodology on Hi-C data from Saccharomyces cerevisiae and Schizosaccharomyces pombe, and identify, among others, modules relating to RNA splicing machinery and chromatin silencing by small RNA which are central to S. pombe's lifestyle. Our results emphasize the importance of 3D genomic organization in eukaryotes and suggest that the evolutionary mechanisms that shape gene organization affect the organism fitness and phenotypes. The proposed algorithms can be utilized in future studies of genome evolution and comparative analysis of spatial genomic organization in different tissues, conditions and single cells.","doi":"10.1093/nar/gkx205","authors":"Diament A, Tuller T","authors_abbrev":"Diament A et al.","pubmed_publication_date":"05 May 2017","pubmed_entrez_date":"2017-04-04","publication_year":"2017","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2017-04-05 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16920624","title":"CDC2 phosphorylation of the fission yeast dis1 ensures accurate chromosome segregation.","citation":"Curr Biol 2006 Aug 22;16(16):1627-35","abstract":"Shortened kinetochore microtubules take separated chromatids to the opposing spindle poles in anaphase. Fission yeast Dis1 belongs to the Dis1/XMAP215/TOG family that is required for proper microtubule dynamics. Here, we report that Dis1is regulated by Cdc2 phosphorylation and that this mitotic phosphorylation ensures the fidelity of chromosome segregation. Whereas mutants Dis1(6A) and Dis1(6E) that substitute all of the six Cdc2 sites for Ala or Glu, respectively, produce colonies at 22 degrees C-36 degrees C, Dis1(6A) but not Dis1(6E) loses a minichromosome and reveals aberrant chromosome segregation at significant frequencies. Dis1(WT) is recruited to two regions of the mitotic spindle: kinetochores (possibly also kinetochore microtubules) in metaphase and the pole-to-pole microtubule lattice in anaphase. Mutant Dis1(6E) preferentially binds to metaphase kinetochores, whereas Dis1(6A), which is located along microtubules, fails in its accumulation at kinetochores. Dis1(6A) displays synthetic lethality with the mis12-537, which is a mutant that compromises kinetochore function. Dis1(6E) mimics the Cdc2-phosphorylated form of Dis1(WT), whereas Dis1(6A) can partially rescue the phenotype resulting form deletion of Mtc1/Alp14, another XMAP215-like protein. In anaphase, dephosphorylated Dis1 and Dis1(6A), but not Dis1(6E), move to the spindle microtubule lattice near the SPBs. Cdc2 thus directly phosphorylates Dis1, and this phosphorylation regulates Dis1 localization in both metaphase and anaphase and ensures high-fidelity segregation.","authors":"Aoki K, Nakaseko Y, Kinoshita K, Goshima G, Yanagida M","authors_abbrev":"Aoki K et al.","pubmed_publication_date":"22 Aug 2006","pubmed_entrez_date":"2006-08-22","publication_year":"2006","canto_session_key":"94f70c9135257d87","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-04-20 09:01:25","canto_approved_date":"2021-12-13 12:59:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-19 12:05:14","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":32,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.14","SPBC11B10.09","SPCC895.07","SPBC776.02c","SPBC409.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2021-04-20"},{"uniquename":"PMID:1107988","title":"[Method for producing spheroplasts from yeast cells].","citation":"Prikl Biokhim Mikrobiol 1975;11(2):264-8","abstract":"A method for producing spheroplasts from yeast cells has been developed. The method involves: 1) prefreezing and thawing of cells in the minimal nutrient medium; 2) treatment with the mixture of 86 mM 2-mercaptoethanol, 5% sodium dodecylsulphate and 6% Triton X-100; 3) enzymic digestion by the digestive juice of grape helix. The formation of spheroplasts was controlled by microscopy and measurement of the optic density of the spheroplast suspension in the incubation medium and in 1% sodium dodecylsulphate. The method has been successfully tested on some bakery yeast: Saccharomyces cerevisiae, Saccharomyces paradoxus, Schizosaccharomyces pombe, Saccharomyces globosus, Saccharomyces carlsbergensis.","authors":"Luchkina LA, Bekker ML","authors_abbrev":"Luchkina LA et al.","pubmed_publication_date":"1975","pubmed_entrez_date":"1975-03-01","publication_year":"1975","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32361273","title":"Requirement of PP2A-B56 Par1  for the Stabilization of the CDK Inhibitor Rum1 and Activation of APC/C Ste9  during Pre-Start G1 in S. pombe.","citation":"iScience 2020 May 22;23(5):101063","abstract":"Exit from the cell cycle during the establishment of quiescence and upon cell differentiation requires the sustained inactivation of CDK complexes. Fission yeast cells deprived of nitrogen halt cell cycle progression in pre-Start G1, before becoming quiescent or undergoing sexual differentiation. The CDK inhibitor Rum1 and the APC/C activator Ste9 are fundamental for this arrest, but both are down-regulated by CDK complexes. Here, we show that PP2A-B56 Par1  is instrumental for Rum1 stabilization and Ste9 activation. In the absence of PP2A-B56 Par1 , cells fail to accumulate Rum1, and this results in persistent CDK activity, Ste9 inactivation, retention of the mitotic cyclin Cdc13, and impaired withdrawal from the cell cycle during nitrogen starvation. Importantly, mutation of a putative B56 interacting motif in Rum1 recapitulates these defects. These results underscore the relevance of CDK-counteracting phosphatases in cell differentiation, establishment of the quiescent state, and escape from it in cancer cells.","doi":"10.1016/j.isci.2020.101063","authors":"Stonyte V, Martín R, Segura-Peña D, Sekulić N, Lopez-Aviles S","authors_abbrev":"Stonyte V et al.","pubmed_publication_date":"22 May 2020","pubmed_entrez_date":"2020-05-04","publication_year":"2020","canto_session_key":"9b6d37d028f7da71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ruth Martin","canto_first_approved_date":"2020-10-05 16:55:22","canto_approved_date":"2025-09-04 11:29:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-29 09:09:59","canto_added_date":"2020-05-05 00:15:04","annotation_curators":[{"name":"Ruth Martin","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":35,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05","SPAC144.13c","SPAPB2B4.03","SPBC20F10.06","SPCC4E9.02","SPCC188.02","SPBC582.03","SPAC227.07c","SPAC31G5.09c","SPBC32F12.09","SPBC11B10.09","SPBC336.12c","SPAC1782.09c","SPAC27D7.03c","SPCC24B10.07","SPBC776.02c"],"gene_count":17,"ltp_gene_count":12,"approved_date":"2020-10-05"},{"uniquename":"PMID:9442101","title":"A novel fission yeast gene, tht1+, is required for the fusion of nuclear envelopes during karyogamy.","citation":"J Cell Biol 1998 Jan 26;140(2):247-58","abstract":"We have isolated a fission yeast karyogamy mutant, tht1, in which nuclear congression and the association of two spindle pole bodies occurs but the subsequent fusion of nuclear envelopes is blocked. The tht1 mutation does not prevent meiosis, so cells execute meiosis with two unfused nuclei, leading to the production of aberrant asci. The tht1(+) gene was cloned and sequenced. Predicted amino acid sequence has no significant homology to previously known proteins but strongly suggests that it is a type I membrane protein. The tht1(+) gene is dispensable for vegetative growth and expressed only in conjugating cells. Tht1p is a glycoprotein susceptible to endoglycosilase H digestion. Site- directed mutagenesis showed that the N-glycosylation site, as well as the COOH-terminal region of Tht1p, is essential for its function. A protease protection assay indicated that the COOH terminus is cytoplasmic. Immunocytological analysis using a HA-tagged Tht1p suggested that the protein is localized in nuclear envelopes and in the ER during karyogamy and that its levels are reduced in cells containing fused nuclei.","authors":"Tange Y, Horio T, Shimanuki M, Ding DQ, Hiraoka Y, Niwa O","authors_abbrev":"Tange Y et al.","pubmed_publication_date":"26 Jan 1998","pubmed_entrez_date":"1998-02-28","publication_year":"1998","canto_session_key":"5eae8ab56540b745","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-29 16:10:51","canto_approved_date":"2023-09-21 09:51:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-29 11:17:49","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13C5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-29"},{"uniquename":"PMID:14727060","title":"A fission yeast strain expressing human CDC25A phosphatase: a tool for selectivity studies of pharmacological inhibitors of CDC25.","citation":"Curr Genet 2004 May;45(5):283-8","abstract":"Fission yeast is a simple eukaryotic model organism in which many aspects of cell cycle control can be explored. We examined by homologous recombination whether the human CDC25A phosphatase could substitute for the function of the fission yeast Cdc25. We first show: (a). that CDC25A efficiently replaces the endogenous Cdc25 mitotic inducer for vegetative growth and (b). that CDC25A is able to partially restore a functional checkpoint in response to both ionising and UV irradiation, but not a DNA replication checkpoint. We then describe a simple assay in which we demonstrate that growth of the humanised CDC25A strain is strongly repressed in a CDC25-dependent manner by BN2003, a potent chemical inhibitor of CDC25 belonging to the benzothiazoledione family. The ease of manipulation of fission yeast humanised CDC25 cells and the simplicity of the above assay offer a powerful tool with which to investigate the specificity of pharmacological inhibitors of CDC25.","authors":"Mondesert O, Lemaire M, Brezak MC, Galera-Contour MO, Prevost G, Ducommun B, Bugler B","authors_abbrev":"Mondesert O et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-01-17","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9790950","title":"Isoform-specific phosphorylation of fission yeast type 2C protein phosphatase.","citation":"Biochem Biophys Res Commun 1998 Oct 09;251(1):296-300","abstract":"Protein phosphatase 2C (PP2C) is one of the four major protein serine/threonine phosphatases of eukaryotes and is implicated in the regulation of various cellular functions. With the goal of elucidating the mechanism responsible for regulating PP2C functions, we investigated the significance of phosphorylation of fission yeast Ptc1, Ptc2, and Ptc3, the yeast orthologs of mammalian PP2C. Both Ptc2 and Ptc3 but not Ptc1 were phosphorylated stoichiometrically by casein kinase II on serine residues at their carboxy-terminal regions. Mutational analysis of Ptc2 and Ptc3 revealed that serine residues of the conserved sequence (Ser-X-Ser-X-X-Glu/Asp) of these proteins were the phosphorylation sites. Interestingly, the activities of Ptc2 and Ptc3 were decreased 25 +/- 7.5% and increased 55 +/- 3.7%, respectively, by phosphorylation. In addition, the same site(s) of Ptc2 was phosphorylated when the protein was expressed in fission yeast cells. These results suggest that phosphorylation of PP2C plays important physiological roles in fission yeast cells.","authors":"Kobayashi T, Sadaie M, Ohnishi M, Wang H, Ikeda S, Hanada M, Yanagawa Y, Nakajima T, Tamura S","authors_abbrev":"Kobayashi T et al.","pubmed_publication_date":"09 Oct 1998","pubmed_entrez_date":"1998-10-29","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4F11.02","SPCC1223.11","SPAC2G11.07c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:4847566","title":"Studies concerning the biochemical genetics of activity and feedback inhibition mutants of Schizosaccharomyces pombe 3-deoxy-D-arabino-neptulosomate-7-phosphate synthase.","citation":"Biochim Biophys Acta 1974 Jun 18;350(2):328-35","abstract":"","authors":"Schweingruber ME, Wyssling HB","authors_abbrev":"Schweingruber ME et al.","pubmed_publication_date":"18 Jun 1974","pubmed_entrez_date":"1974-06-18","publication_year":"1974","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000097","title":"Gene Ontology annotation based on personal communication to FlyBase","abstract":"FlyBase occasionally makes GO annotations based on information that has been sent to us directly by researchers as a personal communication to FlyBase. In each case, the full details of the communication including any associated data and analyses are recorded in a FlyBase publication (FBrf) available from our website (http://flybase.org).","authors":"FlyBase","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10224243","title":"Caffeine-mediated override of checkpoint controls. A requirement for rhp6 (Schizosaccharomyces pombe).","citation":"Genetics 1999 May;152(1):61-71","abstract":"Cells exposed to inhibitors of DNA synthesis or suffering DNA damage are arrested or delayed in interphase through the action of checkpoint controls. If the arrested cell is exposed to caffeine, relatively normal cell cycle progression is resumed and, as observed in checkpoint control mutants, loss of checkpoint control activity is associated with a reduction in cell viability. To address the mechanism of caffeine's action on cell progression, fission yeast mutants that take up caffeine but are not sensitized to hydroxyurea (HU) by caffeine were selected. Mutants 788 and 1176 are point mutants of rhp6, the fission yeast homolog of the budding yeast RAD6 gene. Mutant rhp6-788 is slightly HU sensitive, radiosensitive, and exhibits normal checkpoint responses to HU, radiation, or inactivation of DNA ligase. However, the addition of caffeine does not override the associated cell cycle blocks. Both point and deletion mutations show synthetic lethality at room temperature with temperature-sensitive mutations in cyclin B (cdc13-117) or the phosphatase cdc25 (cdc25-22). These observations suggest that the rhp6 gene product, a ubiquitin-conjugating enzyme required for DNA damage repair, promotes entry to mitosis in response to caffeine treatment.","authors":"Rowley R, Zhang J","authors_abbrev":"Rowley R et al.","pubmed_publication_date":"May 1999","pubmed_entrez_date":"1999-05-04","publication_year":"1999","canto_session_key":"0b37e868b3a99cde","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-09 12:26:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-15 12:01:35","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.07c","SPAC20G8.01","SPBC582.03","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-08-15"},{"uniquename":"PMID:25217460","title":"Off-target effects of the septin drug forchlorfenuron on nonplant eukaryotes.","citation":"Eukaryot Cell 2014 Nov;13(11):1411-20","abstract":"The septins are a family of GTP-binding proteins that form cytoskeletal filaments. Septins are highly conserved and evolutionarily ancient but are absent from land plants. The synthetic plant cytokinin forchlorfenuron (FCF) was shown previously to inhibit budding yeast cell division and induce ectopic septin structures (M. Iwase, S. Okada, T. Oguchi, and A. Toh-e, Genes Genet. Syst. 79:199-206, 2004, http://dx.doi.org/10.1266/ggs.79.199). Subsequent studies in a wide range of eukaryotes have concluded that FCF exclusively inhibits septin function, yet the mechanism of FCF action in nonplant cells remains poorly understood. Here, we report that the cellular effects of FCF are far more complex than previously described. The reported growth arrest of budding yeast cells treated with 1 mM FCF partly reflects sensitization caused by a bud4 mutation present in the W303 strain background. In wild-type (BUD4(+)) budding yeast, growth was inhibited at FCF concentrations that had no detectable effect on septin structure or function. Moreover, FCF severely inhibited the proliferation of fission yeast cells, in which septin function is nonessential. FCF induced fragmentation of budding yeast mitochondrial reticula and the loss of mitochondrial membrane potential. Mitochondria also fragmented in cultured mammalian cells treated with concentrations of FCF that previously were assumed to target septins only. Finally, FCF potently inhibited ciliation and motility and induced mitochondrial disorganization in Tetrahymena thermophila without apparent alterations in septin structure. None of these effects was consistent with the inhibition of septin function. Our findings point to nonseptin targets as major concerns when using FCF.","doi":"10.1128/EC.00191-14","authors":"Heasley LR, Garcia G, McMurray MA","authors_abbrev":"Heasley LR et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-09-14","publication_year":"2014","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2014-09-15 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39527199","title":"CRISPR-Cas9 Genome Editing in Auxotrophic and Non-auxotrophic Fission Yeast Strains.","citation":"Methods Mol Biol 2025;2862:155-170","abstract":"The CRISPR/Cas system is a very powerful genome-editing tool that has been developed over the past decade to optimize genome editing for many organisms. Here, we describe a rapid genome-editing method for fission yeast using the CRISPR-Cas9 system. It allows rapid generation of desired auxotrophic and non-auxotrophic strains without perturbing the local genome content by avoiding the insertion of selection markers at target loci.","doi":"10.1007/978-1-0716-4168-2_11","authors":"Hayashi A, Nakayama JI, Tanaka K","authors_abbrev":"Hayashi A et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10617667","title":"Cloning of a calmodulin kinase I homologue from Schizosaccharomyces pombe.","citation":"J Biol Chem 2000 Jan 07;275(1):685-90","abstract":"By using (35)S-labeled calmodulin (CaM), we have isolated a full-length cDNA clone expressing the Schizosaccharomyces pombe homologue of calmodulin kinase I (CaMK-I), a gene we have named cmk1. It has been previously been shown in mammals that CaMK-I is a member of a CaM-dependent protein kinase cascade that ultimately regulates transcription factors such as ATF and cAMP-response element-binding protein. The cmk1 cDNA encodes a 335-amino acid protein with significant homology to mammalian CaMK-I, including a conserved sequence for phosphorylation by CaM kinase kinase. We have expressed the cmk1 cDNA in bacteria and yeast, and we have shown that it is a CaM-dependent protein kinase. A truncation mutant of cmk1 (d320) failed to bind CaM, indicating that the CaM-binding domain is at the extreme C terminus of the protein. The mRNA for cmk1 is expressed in a cell cycle-dependent manner, peaking at or near the G(1)/S boundary. Overexpression of wild-type cmk1 in S. pombe caused no apparent effects on growth and division. However, mutation of a predicted regulatory site (Thr-192) to aspartic acid resulted in hyperactivation of CMK1 activity in the presence of CaM and causes cell cycle arrest in vivo. Arrest is also accompanied by morphological defects. These results suggest the presence of a CaM-dependent protein kinase cascade in yeast and indicate that cmk1 may be important in cell cycle progression, a process known to be dependent on CaM in eukaryotic cells.","authors":"Rasmussen CD","authors_abbrev":"Rasmussen CD","pubmed_publication_date":"07 Jan 2000","pubmed_entrez_date":"2000-01-05","publication_year":"2000","canto_session_key":"a54f5f9a4591658c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-02 21:19:37","canto_approved_date":"2019-05-03 12:30:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-24 15:50:11","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPACUNK12.02c","SPAC3A12.14"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2016-10-02"},{"uniquename":"PMID:8879047","title":"Maturation of Krp1, an endopeptidase from the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1996 Aug;24(3):503S","abstract":"","authors":"Powner D, Davey J","authors_abbrev":"Powner D et al.","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_session_key":"9ff9e4a1410473cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-10-19 10:01:49","canto_approved_date":"2021-10-30 19:17:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-10-19 10:00:46","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-10-19"},{"uniquename":"PMID:16627997","title":"Polo-like kinases: a team in control of the division.","citation":"Cell Cycle 2006 Apr;5(8):853-64","abstract":"Polo, the founding member of the family of polo-like kinases (Plks) was identified in a Drosophila screen for mutants affecting spindle pole behavior.(1) Several mutants showed defects at their spindle poles and were hence named after the magnetic poles of the earth or geo-magnetic phenomena associated with them, like Polo and Aurora. Currently, the conserved family of Plks consists of many members throughout various species. Multiple Plks are present in mammalian cells (Plk1, Plk2/Snk, Plk3/Fnk/Prk, and Plk4/Sak) and Xenopus (Plx1-3), whereas in other species only one member has been identified, like Polo in Drosophila, Cdc5 in budding yeast and Plo1 in fission yeast. Plks are now viewed as important regulators of multiple functions before and during the mitotic cell division. In this review, we will focus our attention on human Plk1 and its family members Plk2-4 and the many roles they play during mitosis. Furthermore, we will describe the currently knowledge of the regulation of these functions.","authors":"van de Weerdt BC, Medema RH","authors_abbrev":"van de Weerdt BC et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-04-22","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14738748","title":"Recombination: Holliday junction resolution and crossover formation.","citation":"Curr Biol 2004 Jan 20;14(2):R56-8","abstract":"The heterodimeric nuclease Mus81-Eme1 has been proposed to be a Holliday junction resolvase and has now been found to be responsible for nearly all meiotic crossovers in fission yeast. The intriguing substrate preference of this enzyme for nicked Holliday junctions opens the possibility that crossover formation may not always involve double Holliday junctions.","authors":"Heyer WD","authors_abbrev":"Heyer WD","pubmed_publication_date":"20 Jan 2004","pubmed_entrez_date":"2004-01-24","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10664885","title":"Glucose- and K(+)-induced acidification in different yeast species.","citation":"Folia Microbiol (Praha) 1999;44(3):295-8","abstract":"The process of acidification of the external medium after addition of glucose and subsequently of KCl to a suspension of yeast cells varies substantially from species to species. After glucose it is most pronounced in Saccharomyces cerevisiae and Schizosaccharomyces pombe but is very much lower in Lodderomyces elongisporus, Dipodascus magnusii and Rhodotorula gracilis. Both the buffering capacity and the varied effects of vanadate, suloctidil and erythrosin B indicate that the acidification is by about one-half due to the activity of plasma membrane H(+)-ATPase and by about one-half to the extrusion of acidic metabolites from cells. This is supported by the finding that a respiratory quotient greater than one (in various strains of S. cerevisiae and in S. pombe) is indicative of a greater buffering capacity and overall acidification of the medium. Taking into account the virtually negligible buffering capacity of the medium in the pH range where the effect of K+ is observed, the effect of K+ is generally of a similar magnitude as that of adding glucose. It is clearly dependent on (anaerobic) production of metabolic energy, quite distinct from the dependence of the H(+)-ATPase-caused acidification.","authors":"Kotyk A, Lapathitis G, Krenková S","authors_abbrev":"Kotyk A et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"2000-02-09","publication_year":"1999","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23156671","title":"[Recombinational repair in Schizosaccharomyces pombe: the role of mediator proteins].","citation":"Mol Biol (Mosk) 2012;46(5):726-33","abstract":"Repair of double-stranded DNA breaks that occur spontaneously or under the influence of external factors, are critical for cell survival. Evolutionarily conserved mechanism for error-free recombinational repair plays a major role in maintaining genome integrity. Repair pathway is conservative and has a number of similarities in lower eukaryotes and vertebrates. This review examines the current state of studying the mechanism of recombinational repair double-stranded DNA breaks in the fission yeast Schizosaccharomyces pombe, notes the differences of this type of repair in Saccharomyces cerevisiae and higher eukaryotes.","authors":"Khasanova OS, Vagin DA, Khasanov FK","authors_abbrev":"Khasanova OS et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-11-20","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:BI542461","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22888038","title":"Mid1/anillin and the spatial regulation of cytokinesis in fission yeast.","citation":"Cytoskeleton (Hoboken) 2012 Oct;69(10):764-77","abstract":"Cell division is a critical and irreversible step in the cell cycle. The strategies that cells follow to regulate the position of the division plane must take into account the global geometry of the cell as well as position of the genetic material to ensure its accurate segregation into daughter cells of a given cell shape and size. Along the years, research on Schizosaccharomyces pombe, a well-recognized model organism for cell division studies has allowed a detailed molecular understanding of the spatial mechanisms regulating cytokinesis. Division plane position in this unicellular rod-shaped organism, which divides by the assembly and constriction of a medially placed actomyosin ring, largely depends on the anillin-like protein Mid1. Therefore, the major pathways controlling the position of the division plane converge on Mid1. In this review, we make an overview of the studies that have deciphered how Mid1 localization and scaffolding activities are controlled over the cell cycle to ensure the symmetrical division of fission yeast cells. These studies have revealed new mechanisms generating spatial information based on nuclear shuttling of the division plane factor Mid1 and on the establishment of cortical inhibitory gradients of the cell polarity kinase Pom1.","doi":"10.1002/cm.21056","authors":"Rincon SA, Paoletti A","authors_abbrev":"Rincon SA et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-14","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:45606","title":"The genetic fine structure of the complex locus aro3 involved in early aromatic amino acid biosynthesis in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1979;172(3):233-41","abstract":"The complex locus aro3 of Schizosaccharomyces pombe was subjected to genetical fine structure analysis. By comparing the complementation map and the meiotic recombination map, the aro3 locus could be subdivided into the five adjacent subregions A, B, C, D and E. Out of 115 aro3 alleles, 26 nonsense alleles and 30 missense alleles could be identified by the criteria of nonsense suppressor sensitivity and leakiness, respectively. Most alleles with a pleiotropic complementation pattern are of the nonsense type. We conclude from the polarity of the complementation patterns characterising the nonsense alleles that the translation direction proceeds from subregion. A to subregion E. Antipolar effects in complementation are more frequent than in the analogous system of the arom gene cluster of Neurospora crassa.","authors":"Strauss A","authors_abbrev":"Strauss A","pubmed_publication_date":"1979","pubmed_entrez_date":"1979-01-01","publication_year":"1979","canto_session_key":"54b41b6f8ef64116","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-25 13:35:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 16:07:31","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-09-24"},{"uniquename":"PMID:23640764","title":"Phosphorylations of Sds23/Psp1/Moc1 by stress-activated kinase and cAMP-dependent kinase are essential for regulating cell viability in prolonged stationary phase.","citation":"Yeast 2013 Oct;30(10):379-94","abstract":"Under nutritional deprivation caused by prolonged culture, actively growing cells prepare to enter stationary phase. We showed here that Sds23/Psp1/Moc1 was phosphorylated by both cAMP-dependent kinase and stress-activated MAP kinase Sty1 upon entry into stationary phase. Overexpression of the phosphorylation-defective mutant Sds23/Psp1/Moc1 induced cell death in prolonged culture and blocked re-entry into the cell division cycle. These phosphorylations are likely to be required for cell survival during stationary phase and for binding of Ufd2, a Schizosaccharomyces pombe homologue of multi-ubiquitin chain assembly factor E4. Deletion of the Ufd2 gene and overexpression of Sds23/Psp1/Moc1 increased cell viability in prolonged stationary phase. These results suggested that Ufd2 induces cell death in prolonged nutrient deprivation, that Sds23/Psp1/Moc1 may be a target protein of the ubiquitin-fusion degradation pathway for regulation of cell viability under this stress condition, and that Sty1 and PKA activity in stationary phase is essential for interaction between Sds23/Psp1/Moc1 and Ufd2.","doi":"10.1002/yea.2958","authors":"Jang YJ, Won M, Yoo HS","authors_abbrev":"Jang YJ et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-05-04","publication_year":"2013","canto_session_key":"68e7e491fe057f36","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC106.10","SPAC20H4.10","SPBC646.13","SPBC29B5.01","SPBC409.07c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"EMBL:AF197476","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10884352","title":"Solution structural studies and low-resolution model of the Schizosaccharomyces pombe sap1 protein.","citation":"J Mol Biol 2000 Jul 14;300(3):563-74","abstract":"Sap1 is a DNA-binding protein involved in controlling the mating type switch in fission yeast Schizosaccharomyces pombe. In the absence of any significant sequence similarity with any structurally known protein, a variety of biophysical techniques has been used to probe the solution low-resolution structure of the sap1 protein. First, sap1 is demonstrated to be an unusually elongated dimer in solution by measuring the translational diffusion coefficient with two independent techniques: dynamic light-scattering and ultracentrifugation. Second, sequence analysis revealed the existence of a long coiled-coil region, which is responsible for dimerization. The length of the predicted coiled-coil matches estimates drawn from the hydrodynamic experimental behaviour of the molecule. In addition, the same measurements done on a shorter construct with a coiled-coil region shortened by roughly one-half confirmed the localization of the long coiled-coil region. A crude T-shape model incorporating all these information was built. Third, small-angle X-ray scattering (SAXS) of the free molecule provided additional evidence for the model. In particular, the P(r) curve strikingly demonstrates the existence of long intramolecular distances. Using a novel 3D reconstruction algorithm, a low resolution 3D model of the protein has been independently constructed that matches the SAXS experimental data. It also fits the translation diffusion coefficients measurements and agrees with the first T-shaped model. This low-resolution model has clearly biologically relevant new functional implications, suggesting that sap1 is a bifunctional protein, with the two active sites being separated by as much as 120 A; a tetrapeptide repeated four times at the C terminus of the molecule is postulated to be of utmost functional importance.","authors":"Bada M, Walther D, Arcangioli B, Doniach S, Delarue M","authors_abbrev":"Bada M et al.","pubmed_publication_date":"14 Jul 2000","pubmed_entrez_date":"2000-07-08","publication_year":"2000","canto_session_key":"88c5b650d34150b9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-29 17:47:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-07 14:19:19","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-07"},{"uniquename":"PMID:20360068","title":"Systematic analysis of human protein complexes identifies chromosome segregation proteins.","citation":"Science 2010 Apr 30;328(5978):593-9","abstract":"Chromosome segregation and cell division are essential, highly ordered processes that depend on numerous protein complexes. Results from recent RNA interference screens indicate that the identity and composition of these protein complexes is incompletely understood. Using gene tagging on bacterial artificial chromosomes, protein localization, and tandem-affinity purification-mass spectrometry, the MitoCheck consortium has analyzed about 100 human protein complexes, many of which had not or had only incompletely been characterized. This work has led to the discovery of previously unknown, evolutionarily conserved subunits of the anaphase-promoting complex and the gamma-tubulin ring complex--large complexes that are essential for spindle assembly and chromosome segregation. The approaches we describe here are generally applicable to high-throughput follow-up analyses of phenotypic screens in mammalian cells.","doi":"10.1126/science.1181348","authors":"Hutchins JR, Toyoda Y, Hegemann B, Poser I, Hériché JK, Sykora MM, Augsburg M, Hudecz O, Buschhorn BA, Bulkescher J, Conrad C, Comartin D, Schleiffer A, Sarov M, Pozniakovsky A, Slabicki MM, Schloissnig S, Steinmacher I, Leuschner M, Ssykor A, Lawo S, Pelletier L, Stark H, Nasmyth K, Ellenberg J, Durbin R, Buchholz F, Mechtler K, Hyman AA, Peters JM","authors_abbrev":"Hutchins JR et al.","pubmed_publication_date":"30 Apr 2010","pubmed_entrez_date":"2010-04-03","publication_year":"2010","canto_session_key":"a95cd52da5e96064","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-12-31 12:19:07","canto_approved_date":"2023-12-31 12:19:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-31 00:27:49","canto_added_date":"2016-09-21 00:19:10","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:33830","SPAC9G1.15c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2023-12-31"},{"uniquename":"PMID:35474693","title":"Super-resolved live-cell imaging using random illumination microscopy.","citation":"Cell Rep Methods 2021 May 24;1(1):100009","abstract":"Current super-resolution microscopy (SRM) methods suffer from an intrinsic complexity that might curtail their routine use in cell biology. We describe here random illumination microscopy (RIM) for live-cell imaging at super-resolutions matching that of 3D structured illumination microscopy, in a robust fashion. Based on speckled illumination and statistical image reconstruction, easy to implement and user-friendly, RIM is unaffected by optical aberrations on the excitation side, linear to brightness, and compatible with multicolor live-cell imaging over extended periods of time. We illustrate the potential of RIM on diverse biological applications, from the mobility of proliferating cell nuclear antigen (PCNA) in U2OS cells and kinetochore dynamics in mitotic  S. pombe  cells to the 3D motion of myosin minifilaments deep inside  Drosophila  tissues. RIM's inherent simplicity and extended biological applicability, particularly for imaging at increased depths, could help make SRM accessible to biology laboratories.","doi":"10.1016/j.crmeth.2021.100009","authors":"Mangeat T, Labouesse S, Allain M, Negash A, Martin E, Guénolé A, Poincloux R, Estibal C, Bouissou A, Cantaloube S, Vega E, Li T, Rouvière C, Allart S, Keller D, Debarnot V, Wang XB, Michaux G, Pinot M, Le Borgne R, Tournier S, Suzanne M, Idier J, Sentenac A","authors_abbrev":"Mangeat T et al.","pubmed_publication_date":"24 May 2021","pubmed_entrez_date":"2022-04-27","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-04-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF087833","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37939137","title":"The ortholog of human REEP1-4 is required for autophagosomal enclosure of ER-phagy/nucleophagy cargos in fission yeast.","citation":"PLoS Biol 2023 Nov;21(11):e3002372","abstract":"Selective macroautophagy of the endoplasmic reticulum (ER) and the nucleus, known as ER-phagy and nucleophagy, respectively, are processes whose mechanisms remain inadequately understood. Through an imaging-based screen, we find that in the fission yeast Schizosaccharomyces pombe, Yep1 (also known as Hva22 or Rop1), the ortholog of human REEP1-4, is essential for ER-phagy and nucleophagy but not for bulk autophagy. In the absence of Yep1, the initial phase of ER-phagy and nucleophagy proceeds normally, with the ER-phagy/nucleophagy receptor Epr1 coassembling with Atg8. However, ER-phagy/nucleophagy cargos fail to reach the vacuole. Instead, nucleus- and cortical-ER-derived membrane structures not enclosed within autophagosomes accumulate in the cytoplasm. Intriguingly, the outer membranes of nucleus-derived structures remain continuous with the nuclear envelope-ER network, suggesting a possible outer membrane fission defect during cargo separation from source compartments. We find that the ER-phagy role of Yep1 relies on its abilities to self-interact and shape membranes and requires its C-terminal amphipathic helices. Moreover, we show that human REEP1-4 and budding yeast Atg40 can functionally substitute for Yep1 in ER-phagy, and Atg40 is a divergent ortholog of Yep1 and REEP1-4. Our findings uncover an unexpected mechanism governing the autophagosomal enclosure of ER-phagy/nucleophagy cargos and shed new light on the functions and evolution of REEP family proteins.","doi":"10.1371/journal.pbio.3002372","authors":"Zou CX, Ma ZH, Jiang ZD, Pan ZQ, Xu DD, Suo F, Shao GC, Dong MQ, Du LL","authors_abbrev":"Zou CX et al.","pubmed_publication_date":"Nov 2023","pubmed_entrez_date":"2023-11-08","publication_year":"2023","canto_session_key":"2dbe85a34294a16f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chen-Xi Zou","canto_first_approved_date":"2025-03-25 15:50:09","canto_approved_date":"2025-08-17 19:00:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-11 08:34:22","canto_added_date":"2023-11-09 00:25:04","annotation_curators":[{"name":"Chen-Xi Zou","community_curator":true,"annotation_count":38,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.12c","SPBP8B7.24c","SPAC222.14c","SPBC4B4.10c","SPBC31A8.01c","SPCC126.03","YOR152C","SPCC830.08c","SPAC17C9.12","SPBC30D10.09c","SPBC19C7.10","SPAC4H3.10c","SPAC22H12.05c","SPCC1620.07c","SPAC7D4.15c","SPAC6B12.08","SPBC16G5.05c","SPAC13A11.02c","SPBC1539.04"],"gene_count":18,"ltp_gene_count":15,"approved_date":"2025-03-25"},{"uniquename":"PMID:26254929","title":"Cell Cycle Synchronization Using a Microfluidic Synchronizer for Fission Yeast Cells.","citation":"Methods Mol Biol 2016;1342:259-68","abstract":"To produce synchronized cell colonies, many cell cycle synchronization technologies have been developed, among which the baby machine may be considered the most artifact-free. Baby machines incubate \"mother cells\" under normal conditions and collects their \"babies,\" producing cell cultures that are similar not only in cell cycle phase but also in age. Several macroscale and microfluidic baby machines have been applied to synchronized cell research. However, for rod-shaped cells like fission yeast (Schizosaccharomyces pombe), it is still a challenge to immobilize only the mother cells in a microfluidic device. Here, we present a new baby machine suitable for fission yeast. The device fixes one end of the cell and releases the free-end daughter cell every time the cell finishes cytokinesis. A variety of structures for cell immobilization were attempted to find the optimal design. For the convenience of collection and to enable further assays, we integrated a cell screener into the baby machine, which exploits the deformation of polymer material to switch between open and closed states. The device, producing synchronous populations of fission yeast cells, provides a new on-chip tool for cell biology studies.","doi":"10.1007/978-1-4939-2957-3_15","authors":"Wang S, Luo C","authors_abbrev":"Wang S et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-08-10","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-08-11 00:20:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17248775","title":"Genetic Mapping in SCHIZOSACCHAROMYCES POMBE by Mitotic and Meiotic Analysis and Induced Haploidization.","citation":"Genetics 1977 Nov;87(3):471-89","abstract":"The genetic maps of the fission yeast Schizosaccharomyces pombe were extended through the use of haploidization (spontaneous or induced by m-fluorophenylalanine), as well as by tetrad, random spore and mitotic analysis. A new diploidization method utilizing a meiosis-deficient mutant and improved haploidization techniques was employed. As a result of these and previous studies, 118 genetic markers have been assigned to 3 linkage groups. Centromere markers for all 3 chromosomes were identified and genetic maps containing a total of 71 genes were constructed. Our experiments indicate that 3 is very likely to be the haploid chromosome number of S. pombe .","authors":"Kohli J, Hottinger H, Munz P, Strauss A, Thuriaux P","authors_abbrev":"Kohli J et al.","pubmed_publication_date":"Nov 1977","pubmed_entrez_date":"1977-11-01","publication_year":"1977","canto_session_key":"f77a7f7ec22a38bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-12-24 17:19:33","canto_approved_date":"2024-11-08 21:50:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-20 19:22:50","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":55,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.15","SPBC14F5.09c","SPBC29A3.02c","SPBC902.05c","SPBC418.01c","SPAC821.11","SPAC4D7.08c","SPAC22G7.06c","SPAC9E9.03","SPAC6F12.10c","SPBC409.10","SPAC17C9.02c","SPBC2G2.08","SPBC15D4.09c","SPBC725.14","SPAC343.16","SPCC1322.13","SPCC569.08c","SPAC227.18","SPBC1105.02c","SPBC11B10.02c","SPCC1494.04c","SPBC405.01","SPCC330.05c","SPAC144.03","SPBC215.08c","SPBC1A4.02c","SPCC1442.09","SPCC777.09c","SPAC56F8.10","SPAC16.03c","SPCC1739.06c","SPBC16G5.08","SPAC57A10.12c","SPBC1539.09c","SPBC56F2.09c","SPAC4G9.10","SPAC25G10.05c","SPBC3E7.16c","SPBC1711.13","SPAP7G5.04c","SPAC17H9.13c","SPBC21H7.07c"],"gene_count":43,"ltp_gene_count":43,"approved_date":"2016-12-24"},{"uniquename":"PMID:31614546","title":"FRET Microscopy in Yeast.","citation":"Biosensors (Basel) 2019 Oct 11;9(4)","abstract":"Förster resonance energy transfer (FRET) microscopy is a powerful fluorescence microscopy method to study the nanoscale organization of multiprotein assemblies in vivo. Moreover, many biochemical and biophysical processes can be followed by employing sophisticated FRET biosensors directly in living cells. Here, we summarize existing FRET experiments and biosensors applied in yeasts  Saccharomyces cerevisiae  and  Schizosaccharomyces   pombe , two important models of fundamental biomedical research and efficient platforms for analyses of bioactive molecules. We aim to provide a practical guide on suitable FRET techniques, fluorescent proteins, and experimental setups available for successful FRET experiments in yeasts.","doi":"10.3390/bios9040122","authors":"Skruzny M, Pohl E, Abella M","authors_abbrev":"Skruzny M et al.","pubmed_publication_date":"11 Oct 2019","pubmed_entrez_date":"2019-10-17","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-10-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20970338","title":"Fission yeast Mto1 regulates diversity of cytoplasmic microtubule organizing centers.","citation":"Curr Biol 2010 Nov 09;20(21):1959-65","abstract":"Microtubule nucleation by the γ-tubulin complex occurs primarily at centrosomes, but more diverse types of microtubule organizing centers (MTOCs) also exist, especially in differentiated cells. Mechanisms generating MTOC diversity are poorly understood. Fission yeast Schizosaccharomyces pombe has multiple types of cytoplasmic MTOCs, and these vary through the cell cycle. Cytoplasmic microtubule nucleation in fission yeast depends on a complex of proteins Mto1 and Mto2 (Mto1/2), which localizes to MTOCs and interacts with the γ-tubulin complex. Localization of Mto1 to prospective MTOC sites has been proposed as a key step in γ-tubulin complex recruitment and MTOC formation, but how Mto1 localizes to such sites has not been investigated. Here we identify a short conserved C-terminal sequence in Mto1, termed MASC, important for targeting Mto1 to multiple distinct MTOCs. Different subregions of MASC target Mto1 to different MTOCs, and multimerization of MASC is important for efficient targeting. Mto1 targeting to the cell equator during division depends on direct interaction with unconventional type II myosin Myp2. Targeting to the spindle pole body during mitosis depends on Sid4 and Cdc11, components of the septation initiation network (SIN), but not on other SIN components.","doi":"10.1016/j.cub.2010.10.006","authors":"Samejima I, Miller VJ, Rincon SA, Sawin KE","authors_abbrev":"Samejima I et al.","pubmed_publication_date":"09 Nov 2010","pubmed_entrez_date":"2010-10-26","publication_year":"2010","canto_session_key":"5ad432fdb0ddc127","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC417.07c","SPAC4A8.05c","SPCC1739.11c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:21664573","title":"Spindle checkpoint silencing requires association of PP1 to both Spc7 and kinesin-8 motors.","citation":"Dev Cell 2011 Jun 14;20(6):739-50","abstract":"The spindle checkpoint is the prime cell-cycle control mechanism that ensures sister chromatids are bioriented before anaphase takes place. Aurora B kinase, the catalytic subunit of the chromosome passenger complex, both destabilizes kinetochore attachments that do not generate tension and simultaneously maintains the spindle checkpoint signal. However, it is unclear how the checkpoint is silenced following chromosome biorientation. We demonstrate that association of type 1 phosphatase (PP1(Dis2)) with both the N terminus of Spc7 and the nonmotor domains of the Klp5-Klp6 (kinesin-8) complex is necessary to counteract Aurora B kinase to efficiently silence the spindle checkpoint. The role of Klp5 and Klp6 in checkpoint silencing is specific to this class of kinesin and independent of their motor activities. These data demonstrate that at least two distinct pools of PP1, one kinetochore associated and the other motor associated, are needed to silence the spindle checkpoint.","doi":"10.1016/j.devcel.2011.05.008","authors":"Meadows JC, Shepperd LA, Vanoosthuyse V, Lancaster TC, Sochaj AM, Buttrick GJ, Hardwick KG, Millar JB","authors_abbrev":"Meadows JC et al.","pubmed_publication_date":"14 Jun 2011","pubmed_entrez_date":"2011-06-14","publication_year":"2011","canto_session_key":"bc6337774fa106c2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-26 10:40:46","canto_approved_date":"2019-06-06 13:00:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-18 15:18:49","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":43,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1020.02","SPBC776.02c","SPBC26H8.07c","SPCC320.13c","SPAC23H3.08c","SPCC1795.01c","SPBC20F10.06","SPAC19G12.01c","SPBC2F12.13","SPBC106.01","SPBC1685.15c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2018-03-26"},{"uniquename":"PMID:33901016","title":"Translational control of gene expression by eIF2 modulates proteostasis and extends lifespan.","citation":"Aging (Albany NY) 2021 Apr 26;13(8):10989-11009","abstract":"Although the stress response in eukaryotes depends on early events triggered in cells by environmental insults, long-term processes such as aging are also affected. The loss of cellular proteostasis greatly impacts aging, which is regulated by the balancing of protein synthesis and degradation systems. As translation is the input event in proteostasis, we decided to study the role of translational activity on cell lifespan. Our hypothesis was that a reduction on translational activity or specific changes in translation may increase cellular longevity. Using mutant strains of  Schizosaccharomyces pombe  and various stress conditions, we showed that translational reduction caused by phosphorylation of eukaryotic translation initiation factor 2 (eIF2) during the exponential growth phase enhances chronological lifespan (CLS). Furthermore, through next-generation sequence analysis, we found eIF2α phosphorylation-dependent translational activation of some specific genes, especially those involved in autophagy. This fact, together with the observed regulation of autophagy, points to a conserved mechanism involving general and specific control of translation and autophagy as mediators of the role of eIF2α phosphorylation in aging.","doi":"10.18632/aging.203018","authors":"Jiménez-Saucedo T, Berlanga JJ, Rodríguez-Gabriel M","authors_abbrev":"Jiménez-Saucedo T et al.","pubmed_publication_date":"26 Apr 2021","pubmed_entrez_date":"2021-04-26","publication_year":"2021","canto_session_key":"a2f09abbe092a3c8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-04-28 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29171599","title":"Ginger fermented with Schizosaccharomyces pombe alleviates memory impairment via protecting hippocampal neuronal cells in amyloid beta 1-42  plaque injected mice.","citation":"Food Funct 2018 Jan 24;9(1):171-178","abstract":"Ginger, which has been widely used for dietary condiment, has been reported to improve memory dysfunction in an animal model of Alzheimer's disease (AD). Recently, a few trials have been carried out to enhance the effects of ginger by improving the bioavailability of its relevant components via fermentation. Some reports have suggested that the fermented ginger has the ability to affect the AD in vitro systems; however, its anti-amnesic effects on an in vivo model still remain to be investigated. In the present study, we aimed to investigate the neuroprotective effects of ginger fermented with Schizosaccharomyces pombe (FG) in the in vivo models of AD. The neuroprotective effects were investigated by employing behavioral, western blotting, and immunohistochemical assays. The administration of FG improved recognition memory, impaired by scopolamine injection, than that of non-fermented ginger. In addition, FG ameliorated memory impairment in amyloid beta 1-42  (Aβ 1-42 ) plaque-injected mice via protecting neuronal cells in the CA3 area of the mouse hippocampus. Moreover, FG reinstated the pre- and postsynaptic protein levels decreased by Aβ 1-42  plaque-toxicity. Overall, these data suggest that FG attenuates memory impairment in Aβ 1-42  plaque-induced AD mice through inhibition of neuronal cell loss and synaptic disruption.","doi":"10.1039/c7fo01149k","authors":"Huh E, Lim S, Kim HG, Ha SK, Park HY, Huh Y, Oh MS","authors_abbrev":"Huh E et al.","pubmed_publication_date":"24 Jan 2018","pubmed_entrez_date":"2017-11-25","publication_year":"2018","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2017-11-27 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28432181","title":"Dual nature of pseudouridylation in U2 snRNA: Pus1p-dependent and Pus1p-independent activities in yeasts and higher eukaryotes.","citation":"RNA 2017 Jul;23(7):1060-1067","abstract":"The pseudouridine at position 43 in vertebrate U2 snRNA is one of the most conserved post-transcriptional modifications of spliceosomal snRNAs; the equivalent position is pseudouridylated in U2 snRNAs in different phyla including fungi, insects, and worms. Pseudouridine synthase Pus1p acts alone on U2 snRNA to form this pseudouridine in yeast  Saccharomyces cerevisiae  and mouse. Furthermore, in  S. cerevisiae , Pus1p is the only pseudouridine synthase for this position. Using an in vivo yeast cell system, we tested enzymatic activity of Pus1p from the fission yeast  Schizosaccharomyces pombe , the worm  Caenorhabditis elegans , the fruit fly  Drosophila melanogaster , and the frog  Xenopus tropicalis  We demonstrated that Pus1p from  C. elegans  has no enzymatic activity on U2 snRNA when expressed in yeast cells, whereas in similar experiments, position 44 in yeast U2 snRNA (equivalent to position 43 in vertebrates) is a genuine substrate for Pus1p from  S. cerevisiae ,  S. pombe ,  Drosophila ,  Xenopus , and mouse. However, when we analyzed U2 snRNAs from  Pus1  knockout mice and the  pus1Δ S. pombe  strain, we could not detect any changes in their modification patterns when compared to wild-type U2 snRNAs. In  S. pombe , we found a novel box H/ACA RNA encoded downstream from the  RPC10  gene and experimentally verified its guide RNA activity for positioning Ψ43 and Ψ44 in U2 snRNA. In vertebrates, we showed that SCARNA8 (also known as U92 scaRNA) is a guide for U2-Ψ43 in addition to its previously established targets U2-Ψ34/Ψ44.","doi":"10.1261/rna.061226.117","authors":"Deryusheva S, Gall JG","authors_abbrev":"Deryusheva S et al.","pubmed_publication_date":"Jul 2017","pubmed_entrez_date":"2017-04-23","publication_year":"2017","canto_session_key":"1e6975f2a6cb5e9d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2018-04-23 18:16:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-26 16:26:47","canto_added_date":"2017-04-24 00:15:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.03","SPNCRNA.1709","SPSNRNA.02"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2017-06-26"},{"uniquename":"PMID:22851695","title":"Mediator promotes CENP-a incorporation at fission yeast centromeres.","citation":"Mol Cell Biol 2012 Oct;32(19):4035-43","abstract":"At Schizosaccharomyces pombe centromeres, heterochromatin formation is required for de novo incorporation of the histone H3 variant CENP-A(Cnp1), which in turn directs kinetochore assembly and ultimately chromosome segregation during mitosis. Noncoding RNAs (ncRNAs) transcribed by RNA polymerase II (Pol II) directs heterochromatin formation through not only the RNA interference (RNAi) machinery but also RNAi-independent RNA processing factors. Control of centromeric ncRNA transcription is therefore a key factor for proper centromere function. We here demonstrate that Mediator directs ncRNA transcription and regulates centromeric heterochromatin formation in fission yeast. Mediator colocalizes with Pol II at centromeres, and loss of the Mediator subunit Med20 causes a dramatic increase in pericentromeric transcription and desilencing of the core centromere. As a consequence, heterochromatin formation is impaired via both the RNAi-dependent and -independent pathways, resulting in loss of CENP-A(Cnp1) from the core centromere, a defect in kinetochore function, and a severe chromosome segregation defect. Interestingly, the increased centromeric transcription observed in med20Δ cells appears to directly block CENP-A(Cnp1) incorporation since inhibition of Pol II transcription can suppress the observed phenotypes. Our data thus identify Mediator as a crucial regulator of ncRNA transcription at fission yeast centromeres and add another crucial layer of regulation to centromere function.","doi":"10.1128/MCB.00374-12","authors":"Carlsten JO, Szilagyi Z, Liu B, Lopez MD, Szászi E, Djupedal I, Nyström T, Ekwall K, Gustafsson CM, Zhu X","authors_abbrev":"Carlsten JO et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-08-02","publication_year":"2012","canto_session_key":"551398fef1425eba","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27181083","title":"Yeast buddies helping to unravel the complexity of neurodegenerative disorders.","citation":"Mech Ageing Dev 2017 Jan;161(Pt B):288-305","abstract":"Neurodegenerative disorders have a profound effect on the quality of life of patients and their environment. However, the development of adequate therapies requires accurate understanding of the underlying disease pathogenesis. On that account, yeast models can play an important role, as they enable the elucidation of the mechanisms leading to neurodegenerative disorders. Furthermore, by using so-called humanized yeast systems, the findings in yeast can be interpolated to humans. In this review, we will give an overview of the current body of knowledge on the use of yeast models with regard to Huntington's, Parkinson's and Alzheimer's disease. In addition to the results, obtained with the baker's yeast Saccharomyces cerevisiae, we also consider the existing literature on the less common but promising fission yeast Schizosaccharomyces pombe.","doi":"10.1016/j.mad.2016.05.002","authors":"Fruhmann G, Seynnaeve D, Zheng J, Ven K, Molenberghs S, Wilms T, Liu B, Winderickx J, Franssens V","authors_abbrev":"Fruhmann G et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2016-05-17","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-05-19 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15280881","title":"Junctions on the road to cancer.","citation":"Nat Struct Mol Biol 2004 Aug;11(8):693-5","abstract":"","authors":"Whitby MC","authors_abbrev":"Whitby MC","pubmed_publication_date":"Aug 2004","pubmed_entrez_date":"2004-07-29","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1368653","title":"Activity of poly(gamma-glutamylcysteinyl)glycine synthesis in crude extract of fission yeast, Schizosaccharomyces pombe.","citation":"Agric Biol Chem 1990 Nov;54(11):3025-6","abstract":"","authors":"Yoshimura E, Kabuyama Y, Yamazaki S, Toda S","authors_abbrev":"Yoshimura E et al.","pubmed_publication_date":"Nov 1990","pubmed_entrez_date":"1990-11-01","publication_year":"1990","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR28163","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1604.25","HGNC:40045"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AB084873","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.61"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37607906","title":"Histone H3 serine-57 is a CHK1 substrate whose phosphorylation affects DNA repair.","citation":"Nat Commun 2023 Aug 22;14(1):5104","abstract":"Histone post-translational modifications promote a chromatin environment that controls transcription, DNA replication and repair, but surprisingly few phosphorylations have been documented. We report the discovery of histone H3 serine-57 phosphorylation (H3S57ph) and show that it is implicated in different DNA repair pathways from fungi to vertebrates. We identified CHK1 as a major human H3S57 kinase, and disrupting or constitutively mimicking H3S57ph had opposing effects on rate of recovery from replication stress, 53BP1 chromatin binding, and dependency on RAD52. In fission yeast, mutation of all H3 alleles to S57A abrogated DNA repair by both non-homologous end-joining and homologous recombination, while cells with phospho-mimicking S57D alleles were partly compromised for both repair pathways, presented aberrant Rad52 foci and were strongly sensitised to replication stress. Mechanistically, H3S57ph loosens DNA-histone contacts, increasing nucleosome mobility, and interacts with H3K56. Our results suggest that dynamic phosphorylation of H3S57 is required for DNA repair and recovery from replication stress, opening avenues for investigating the role of this modification in other DNA-related processes.","doi":"10.1038/s41467-023-40843-4","authors":"Parisis N, Dans PD, Jbara M, Singh B, Schausi-Tiffoche D, Molina-Serrano D, Brun-Heath I, Hendrychová D, Maity SK, Buitrago D, Lema R, Nait Achour T, Giunta S, Girardot M, Talarek N, Rofidal V, Danezi K, Coudreuse D, Prioleau MN, Feil R, Orozco M, Brik A, Wu PJ, Krasinska L, Fisher D","authors_abbrev":"Parisis N et al.","pubmed_publication_date":"22 Aug 2023","pubmed_entrez_date":"2023-08-22","publication_year":"2023","canto_session_key":"56966daa19bbb083","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-08-24 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27382058","title":"Preferential Protection of Genetic Fidelity within Open Chromatin by the Mismatch Repair Machinery.","citation":"J Biol Chem 2016 Aug 19;291(34):17692-705","abstract":"Epigenetic systems are well known for the roles they play in regulating the differential expression of the same genome in different cell types. However, epigenetic systems can also directly impact genomic integrity by protecting genetic sequences. Using an experimental evolutionary approach, we studied rates of mutation in the fission yeast Schizosaccharomyces pombe strains that lacked genes encoding several epigenetic regulators or mismatch repair components. We report that loss of a functional mismatch repair pathway in S. pombe resulted in the preferential enrichment of mutations in euchromatin, indicating that the mismatch repair machinery preferentially protected genetic fidelity in euchromatin. This preference is probably determined by differences in the accessibility of chromatin at distinct chromatin regions, which is supported by our observations that chromatin accessibility positively correlated with mutation rates in S. pombe or human cancer samples with deficiencies in mismatch repair. Importantly, such positive correlation was not observed in S. pombe strains or human cancer samples with functional mismatch repair machinery.","doi":"10.1074/jbc.M116.719971","authors":"Sun L, Zhang Y, Zhang Z, Zheng Y, Du L, Zhu B","authors_abbrev":"Sun L et al.","pubmed_publication_date":"19 Aug 2016","pubmed_entrez_date":"2016-07-07","publication_year":"2016","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2016-07-08 00:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22042869","title":"A homolog of male sex-determining factor SRY cooperates with a transposon-derived CENP-B protein to control sex-specific directed recombination.","citation":"Proc Natl Acad Sci U S A 2011 Nov 15;108(46):18754-9","abstract":"Schizosaccharomyces pombe cells switch mating type by replacing genetic information at the expressed mat1 locus with sequences copied from mat2-P or mat3-M silent donor loci. The choice of donor locus is dictated by cell type, such that mat2 is the preferred donor in M cells and mat3 is the preferred donor in P cells. Donor choice involves a recombination-promoting complex (RPC) containing Swi2 and Swi5. In P cells, the RPC localizes to a specific DNA element located adjacent to mat3, but in M cells it spreads across the silent mating-type region, including mat2-P. This differential distribution of the RPC regulates nonrandom choice of donors. However, cell-type-specific differences in RPC localization are not understood. Here we show that the mat1-M-encoded factor Mc, which shares structural and functional similarities with the male sex-determining factor SRY, is highly enriched at the swi2 and swi5 loci and promotes elevated levels of RPC components. Loss of Mc reduces Swi2 and Swi5 to levels comparable to those in P cells and disrupts RPC spreading across the mat2/3 region. Mc also localizes to loci expressed preferentially in M cells and to retrotransposon LTRs. We demonstrate that Mc localization at LTRs and at swi2 requires Abp1, a homolog of transposon-derived CENP-B protein and that loss of Abp1 impairs Swi2 protein expression and the donor choice mechanism. These results suggest that Mc modulates levels of recombination factors, which is important for mating-type donor selection and for the biased gene conversion observed during meiosis, where M cells serve as preferential donors of genetic information.","doi":"10.1073/pnas.1109988108","authors":"Matsuda E, Sugioka-Sugiyama R, Mizuguchi T, Mehta S, Cui B, Grewal SI","authors_abbrev":"Matsuda E et al.","pubmed_publication_date":"15 Nov 2011","pubmed_entrez_date":"2011-11-02","publication_year":"2011","canto_session_key":"5fe4a0c49baf997f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-11 17:50:18","canto_approved_date":"2025-09-04 07:17:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-11 17:49:58","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":19,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.04c","SPAPB1A10.02","SPBC23G7.09","SPAC664.01c","SPAC1142.03c","SPBC409.03","SPAP11E10.02c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2024-07-11"},{"uniquename":"PMID:22705945","title":"Silent decision: HP1 protein escorts heterochromatic RNAs to their destiny.","citation":"EMBO J 2012 Aug 01;31(15):3237-8","abstract":"EMBO J advance online publication June 07 2012; doi:; DOI: 10.1016/j.molcel.2012.05.009 Heterochromatin is classically perceived to be refractory to transcription because of its compact structure. However, Keller et al (2012) now demonstrated that heterochromatic transcripts can accumulate even when heterochromatin is normally packaged. By tracking down the fate of these heterochromatic RNAs, they revealed a new post-transcriptional mechanism of silencing in heterochromatin that involves the dynamic turnover of HP1 Swi6  between its free, chromatin-bound and RNA-bound forms. The latter form escorts heterochromatic RNA to degradation.","doi":"10.1038/emboj.2012.172","authors":"Ren J, Martienssen RA","authors_abbrev":"Ren J et al.","pubmed_publication_date":"01 Aug 2012","pubmed_entrez_date":"2012-06-19","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9632761","title":"Tyrosine phosphorylation of cdc2 is required for the replication checkpoint in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1998 Jul;18(7):3782-7","abstract":"The DNA replication checkpoint inhibits mitosis in cells that are unable to replicate their DNA, as when nucleotide biosynthesis is inhibited by hydroxyurea. In the fission yeast Schizosaccharomyces pombe, genetic evidence suggests that this checkpoint involves the inhibition of Cdc2 activity through the phosphorylation of tyrosine-15. On the contrary, a recent biochemical study indicated that Cdc2 is in an activated state during a replication checkpoint, suggesting that phosphorylation of Cdc2 on tyrosine-15 is not part of the replication checkpoint mechanism. We have undertaken biochemical and genetic studies to resolve this controversy. We report that the DNA replication checkpoint in S. pombe is abrogated in cells that carry the allele cdc2-Y15F, expressing an unphosphorylatable form of Cdc2. Furthermore, Cdc2 isolated from replication checkpoint-arrested cells can be activated in vitro by Cdc25, the tyrosine phosphatase responsible for dephosphorylating Cdc2 in vivo, to the same extent as Cdc2 isolated from cdc25ts-blocked cells, indicating that hydroxyurea treatment causes Cdc2 activity to be maintained at a low level that is insufficient to induce mitosis. These studies show that inhibitory tyrosine-15 phosphorylation of Cdc2 is essential for the DNA replication checkpoint and suggests that Cdc25, and/or one or both of Wee1 and Mik1, the tyrosine kinases that phosphorylate Cdc2, are regulated by the replication checkpoint.","authors":"Rhind N, Russell P","authors_abbrev":"Rhind N et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-06-25","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:34415038","title":"The Hob proteins are novel and conserved lipid-binding proteins at ER-PM contact sites.","citation":"J Cell Sci 2022 Mar 01;135(5)","abstract":"Membrane contact sites are critical junctures for organelle signaling and communication. Endoplasmic reticulum-plasma membrane (ER-PM) contact sites were the first membrane contact sites to be described; however, the protein composition and molecular function of these sites is still emerging. Here, we leverage yeast and Drosophila model systems to uncover a novel role for the Hobbit (Hob) proteins at ER-PM contact sites. We find that Hobbit localizes to ER-PM contact sites in both yeast cells and the Drosophila larval salivary glands, and this localization is mediated by an N-terminal ER membrane anchor and conserved C-terminal sequences. The C-terminus of Hobbit binds to plasma membrane phosphatidylinositols, and the distribution of these lipids is altered in hobbit mutant cells. Notably, the Hobbit protein is essential for viability in Drosophila, providing one of the first examples of a membrane contact site-localized lipid binding protein that is required for development.","doi":"10.1242/jcs.259086","authors":"Neuman SD, Jorgensen JR, Cavanagh AT, Smyth JT, Selegue JE, Emr SD, Bashirullah A","authors_abbrev":"Neuman SD et al.","pubmed_publication_date":"01 Mar 2022","pubmed_entrez_date":"2021-08-20","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3H5.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25159149","title":"Contractile ring stability in S. pombe depends on F-BAR protein Cdc15p and Bgs1p transport from the Golgi complex.","citation":"Cell Rep 2014 Sep 11;8(5):1533-44","abstract":"Cdc15p is known to contribute to cytokinesis in fission yeast; however, the protein is not required to assemble the contractile ring of actin and myosin, but it helps to anchor the ring to the plasma membrane. Cdc15p has a lipid-binding F-BAR domain, suggesting that it provides a physical link between the plasma membrane and contractile ring proteins. However, we find that a more important function of Cdc15p during cytokinesis is to help deliver a transmembrane enzyme, Bgs1p (also called Cps1p), from the Golgi apparatus to the plasma membrane, where it appears to anchor the contractile ring. Bgs1p synthesizes the cell wall in the cleavage furrow, but its enzyme activity is not required to anchor the contractile ring. We estimate that ∼ 2,000 Bgs1p molecules are required to anchor the ring. Without Bgs1p anchors, contractile rings slide along the plasma membrane, a phenomenon that depends on an unconventional type II myosin called Myp2p.","doi":"10.1016/j.celrep.2014.07.048","authors":"Arasada R, Pollard TD","authors_abbrev":"Arasada R et al.","pubmed_publication_date":"11 Sep 2014","pubmed_entrez_date":"2014-08-28","publication_year":"2014","canto_session_key":"934ce36ca3fad0a8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-08-29 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4A8.05c","SPAC20G8.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:28093891","title":"Multifaceted effects of antimetabolite and anticancer drug, 2-deoxyglucose on eukaryotic cancer models budding and fission yeast.","citation":"IUBMB Life 2017 Mar;69(3):137-147","abstract":"Glycolytic inhibitors are of interest therapeutically as they are effective against cancers that display increased glycolytic rate and mitochondrial defects. 2-Deoxyglucose (2-DG) is one such glycolytic inhibitor and was identified to be a competitive inhibitor of glucose. Studies from past few decades have shown that the mechanism of action of 2-DG is complex involving several metabolic and signaling pathways. Budding yeast Saccharomyces cerevisiae and fission yeast Schizosaccharomyces pombe are two important models for studying metabolism, cell cycle and cell signaling. These two unicellular eukaryotes are Crabtree positive yeasts exhibiting a metabolism similar to that of cancer cells. Effects of 2-DG in yeast is of interest owing to these similarities and hence yeasts have emerged as ideal model organisms to study the mode of action and resistance to 2-DG. In this review, we summarize the studies on biological effect and resistance to 2-DG in budding and fission yeasts and give an insight into its possible mechanism of action as models for understanding cancer metabolism and drugs affecting cancer progression. © 2017 IUBMB Life, 69(3):137-147, 2017.","doi":"10.1002/iub.1599","authors":"Vishwanatha A, D'Souza CJ","authors_abbrev":"Vishwanatha A et al.","pubmed_publication_date":"Mar 2017","pubmed_entrez_date":"2017-01-18","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-01-19 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39105351","title":"A novel transcription factor Sdr1 involving sulfur depletion response in fission yeast.","citation":"Genes Cells 2024 Aug;29(8):667-680","abstract":"In the fission yeast Schizosaccharomyces pombe, the response to sulfur depletion has been less studied compared to the response to nitrogen depletion. Our study reveals that the fission yeast gene, SPCC417.09c, plays a significant role in the sulfur depletion response. This gene encodes a protein with a Zn 2 Cys 6  fungal-type DNA-binding domain and a transcription factor domain, and we have named it sdr1 +  (sulfur depletion response 1). Interestingly, while sulfur depletion typically induces autophagy akin to nitrogen depletion, we found that autophagy was not induced under sulfur depletion in the absence of sdr1 + . This suggests that sdr1 +  is necessary for the induction of autophagy under conditions of sulfur depletion. Although sdr1 +  is not essential for the growth of fission yeast, its overexpression, driven by the nmt1 promoter, inhibits growth. This implies that Sdr1 may possess cell growth-inhibitory capabilities. In addition, our analysis of Δsdr1 cells revealed that sdr1 +  also plays a role in regulating the expression of genes associated with the phosphate depletion response. In conclusion, our study introduces Sdr1 as a novel transcription factor that contributes to an appropriate cellular nutrient starvation response. It does so by inhibiting inappropriate cell growth and inducing autophagy in response to sulfur depletion.","doi":"10.1111/gtc.13136","authors":"Ohtsuka H, Ohara K, Shimasaki T, Hatta Y, Maekawa Y, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Aug 2024","pubmed_entrez_date":"2024-08-06","publication_year":"2024","canto_session_key":"78e9527109bc9ba8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2024-10-29 08:44:53","canto_approved_date":"2024-11-06 10:41:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-10-01 04:27:34","canto_added_date":"2024-08-06 23:25:04","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":27,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPBC1289.14","SPAC19D5.01","SPCC63.08c","SPBC839.06","SPCC16A11.08","SPBP35G2.16c","SPCC417.10","SPCC417.09c","SPBC2F12.09c","SPBC8E4.01c","SPCC70.12c","SPAC1F5.10","SPBC8E4.12c","SPBP4G3.02","SPBC27B12.11c"],"gene_count":16,"ltp_gene_count":13,"approved_date":"2024-10-29"},{"uniquename":"PMID:23178809","title":"Recombination-restarted replication makes inverted chromosome fusions at inverted repeats.","citation":"Nature 2013 Jan 10;493(7431):246-9","abstract":"Impediments to DNA replication are known to induce gross chromosomal rearrangements (GCRs) and copy-number variations (CNVs). GCRs and CNVs underlie human genomic disorders and are a feature of cancer. During cancer development, environmental factors and oncogene-driven proliferation promote replication stress. Resulting GCRs and CNVs are proposed to contribute to cancer development and therapy resistance. When stress arrests replication, the replisome remains associated with the fork DNA (stalled fork) and is protected by the inter-S-phase checkpoint. Stalled forks efficiently resume when the stress is relieved. However, if the polymerases dissociate from the fork (fork collapse) or the fork structure breaks (broken fork), replication restart can proceed either by homologous recombination or microhomology-primed re-initiation. Here we ascertain the consequences of replication with a fork restarted by homologous recombination in fission yeast. We identify a new mechanism of chromosomal rearrangement through the observation that recombination-restarted forks have a considerably high propensity to execute a U-turn at small inverted repeats (up to 1 in 40 replication events). We propose that the error-prone nature of restarted forks contributes to the generation of GCRs and gene amplification in cancer, and to non-recurrent CNVs in genomic disorders.","doi":"10.1038/nature11676","authors":"Mizuno K, Miyabe I, Schalbetter SA, Carr AM, Murray JM","authors_abbrev":"Mizuno K et al.","pubmed_publication_date":"10 Jan 2013","pubmed_entrez_date":"2012-11-27","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16042567","title":"Compartmentalized signalling of Ras.","citation":"Biochem Soc Trans 2005 Aug;33(Pt 4):657-61","abstract":"Ras proteins associate with cellular membranes by virtue of a series of post-translational modifications of their C-terminal CAAX sequences. The discovery that two of the three enzymes that modify CAAX proteins are restricted to the endoplasmic reticulum led to the recognition that all nascent Ras proteins transit endomembranes en route to the PM (plasma membrane) and that at steady-state N-Ras and H-Ras are highly expressed on the Golgi apparatus. To test the hypothesis that Ras proteins on internal membranes can signal, we developed a fluorescent probe that reports when and where in living cells Ras becomes active. We found that growth factors stimulated rapid and transient activation of Ras on the PM followed by delayed and sustained activation on the Golgi. We mapped one pathway responsible for this activity as involving PLCgamma (phospholipase Cgamma)/DAG (diacylglycerol)+Ca2+/RasGRP1. Using mammalian cells and fission yeast, we have shown that differential localization of activated Ras preferentially activates distinct signalling pathways. In very recent work, we have found that (i) the subcellular localization of K-Ras can be acutely modulated by phosphorylation of its C-terminal hypervariable region by PKC, (ii) among the membranes upon which phosphorylated K-Ras accumulates is the outer mitochondrial membrane and (iii) phosphorylated, internalized K-Ras promotes apoptosis. Thus the signalling output of Ras depends on its subcellular localization.","authors":"Philips MR","authors_abbrev":"Philips MR","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-07-27","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23444842","title":"Expression, purification and biochemical characterization of Schizosaccharomyces pombe Mcm4, 6 and 7.","citation":"BMC Biochem 2013 Feb 27;14:5","abstract":"The hetero-hexamer of the eukaryotic minichromosome maintenance (MCM) proteins plays an essential role in replication of genomic DNA. The ring-shaped Mcm2-7 hexamers comprising one of each subunit show helicase activity in vitro, and form double-hexamers on DNA. The Mcm4/6/7 also forms a hexameric complex with helicase activity in vitro.\nWe used an Escherichiai coli expression system to express various domains of Schizosaccharomyces pombe Mcm4, 6 and 7 in order to characterize their domain structure, oligomeric states, and possible inter-/intra-subunit interactions. We also successfully employed a co-expression system to express Mcm4/6/7 at the same time in Escherichiai coli, and have purified functional Mcm4/6/7 complex in a hexameric state in high yield and purity, providing a means for generating large quantity of proteins for future structural and biochemical studies.\nBased on our results and those of others, models were proposed for the subunit arrangement and architecture of both the Mcm4/6/7 hexamer and the Mcm2-7 double-hexamer.","doi":"10.1186/1471-2091-14-5","authors":"Xu M, Chang YP, Chen XS","authors_abbrev":"Xu M et al.","pubmed_publication_date":"27 Feb 2013","pubmed_entrez_date":"2013-03-01","publication_year":"2013","canto_session_key":"87ce105a27640d77","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-13 10:49:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-04 17:30:12","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC211.04c","SPBC25D12.03c","SPCC16A11.17"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-11-04"},{"uniquename":"PMID:34292936","title":"Fission yeast Rad8/HLTF facilitates Rad52-dependent chromosomal rearrangements through PCNA lysine 107 ubiquitination.","citation":"PLoS Genet 2021 Jul;17(7):e1009671","abstract":"Gross chromosomal rearrangements (GCRs), including translocation, deletion, and inversion, can cause cell death and genetic diseases such as cancer in multicellular organisms. Rad51, a DNA strand exchange protein, suppresses GCRs by repairing spontaneous DNA damage through a conservative way of homologous recombination, gene conversion. On the other hand, Rad52 that catalyzes single-strand annealing (SSA) causes GCRs using homologous sequences. However, the detailed mechanism of Rad52-dependent GCRs remains unclear. Here, we provide genetic evidence that fission yeast Rad8/HLTF facilitates Rad52-dependent GCRs through the ubiquitination of lysine 107 (K107) of PCNA, a DNA sliding clamp. In rad51Δ cells, loss of Rad8 eliminated 75% of the isochromosomes resulting from centromere inverted repeat recombination, showing that Rad8 is essential for the formation of the majority of isochromosomes in rad51Δ cells. Rad8 HIRAN and RING finger mutations reduced GCRs, suggesting that Rad8 facilitates GCRs through 3' DNA-end binding and ubiquitin ligase activity. Mms2 and Ubc4 but not Ubc13 ubiquitin-conjugating enzymes were required for GCRs. Consistent with this, mutating PCNA K107 rather than the well-studied PCNA K164 reduced GCRs. Rad8-dependent PCNA K107 ubiquitination facilitates Rad52-dependent GCRs, as PCNA K107R, rad8, and rad52 mutations epistatically reduced GCRs. In contrast to GCRs, PCNA K107R did not significantly change gene conversion rates, suggesting a specific role of PCNA K107 ubiquitination in GCRs. PCNA K107R enhanced temperature-sensitive growth defects of DNA ligase I cdc17-K42 mutant, implying that PCNA K107 ubiquitination occurs when Okazaki fragment maturation fails. Remarkably, K107 is located at the interface between PCNA subunits, and an interface mutation D150E bypassed the requirement of PCNA K107 and Rad8 ubiquitin ligase for GCRs. These data suggest that Rad8-dependent PCNA K107 ubiquitination facilitates Rad52-dependent GCRs by changing the PCNA clamp structure.","doi":"10.1371/journal.pgen.1009671","authors":"Su J, Xu R, Mongia P, Toyofuku N, Nakagawa T","authors_abbrev":"Su J et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-07-22","publication_year":"2021","canto_session_key":"bcf6fb6825f4c05f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takuro Nakagawa","canto_first_approved_date":"2021-08-11 14:40:14","canto_approved_date":"2021-08-12 10:25:34","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-07-30 08:20:05","canto_added_date":"2021-07-24 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":68,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Takuro Nakagawa","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.02","SPBC16D10.09","SPAC30D11.10","SPBC947.11c","SPAC11E3.04c","SPAC20G8.01","SPAC13G6.01c","SPCC4G3.05c","SPCC338.05c","SPAC8F11.03","SPAC644.14c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2021-08-11"},{"uniquename":"PMID:41971402","title":"From detail to diversity: Capturing the chemical signature of non- Saccharomyces  yeasts in white wine through GC×GC/TOF-MS metabolomics and complementary analytical approaches.","citation":"Food Chem X 2026 Apr;35:103789","abstract":"To gain a broad understanding of yeast species' effects, Malvazija istarska wines produced by sequential inoculation with five non- Saccharomyces  starters and monoculture fermentation with a  Saccharomyces cerevisiae×S. paradoxus  hybrid and a  S. cerevisiae  control were thoroughly analyzed. Two-dimensional gas chromatography/mass spectrometry, alongside conventional GC, enabled the identification of 399 volatile compounds and revealed many yeast-specific effects. Non- Saccharomyces  starters generally decreased the concentrations of acetaldehyde, 2-phenylethanol, fatty acids, and volatile phenols, while increasing the concentrations of isobutanol, its esters, and isoamyl acetate.  Torulaspora delbrueckii  had the most pronounced impact, with higher concentrations of short-chain ethyl esters and acetates, and lower levels of acetaldehyde, medium-chain acids, and their ethyl esters. The effects on terpenoids, norisoprenoids, thiols, C 6 -alcohols, ketones, lactones, and furanoids varied. Multivariate analysis revealed numerous yeast-specific volatile markers. Non- Saccharomyces  yeasts preserved more hydroxycinnamic acids. Overall, the results obtained provided an in-depth insight into the yeast-driven modulation of white wine chemical composition.","doi":"10.1016/j.fochx.2026.103789","authors":"Delač Salopek D, Vrhovsek U, Carlin S, Radeka S, Tomašević M, Lukić I","authors_abbrev":"Delač Salopek D et al.","pubmed_publication_date":"Apr 2026","pubmed_entrez_date":"2026-04-13","publication_year":"2026","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2026-04-13 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1908900","title":"Use of alpha-aminoadipate and lysine as sole nitrogen source by Schizosaccharomyces pombe and selected pathogenic fungi.","citation":"J Basic Microbiol 1991;31(2):149-56","abstract":"alpha-Aminodipate, an intermediate of the lysine biosynthetic pathway of fungi, or lysine when used as the sole nitrogen source in the medium was growth inhibitory and toxic to Saccharomyces cerevisiae. The fission yeast Schizosaccharomyces pombe and pathogenic fungi Candida albicans, Filobasidiella neoformans and Aspergillus fumigatus grew in the medium containing alpha-aminoadipate as the sole nitrogen source. C. albicans, A. fumigatus, and one of the strains of F. neoformans also grew in the medium containing lysine as the sole nitrogen source. When grown in the alpha-aminoadipate medium, only S. pombe accumulated a significant amount of alpha-ketoadipate in the culture supernatant. Also, 14C-alpha-aminoadipate was converted to 14C-alpha-ketoadipate in vivo. In the ammonium sulfate medium, S. pombe cells converted 14C-alpha-aminoadipate to lysine. The levels of glutamate-alpha-ketoadipate transaminase, an enzyme responsible for the conversion of alpha-aminoadipate to alpha-ketoadipate, and alpha-aminoadipate reductase, an enzyme required for the conversion of alpha-aminoadipate to lysine, were similar in S. pombe cells grown in the alpha-aminoadipate or ammonium sulfate medium. However, the level of homoisocitrate dehydrogenase, an enzyme before the alpha-ketoadipate step, was twelvefold lower in S. pombe cells grown in the alpha-aminoadipate medium compared to the level in cells grown in the ammonium sulfate medium. Pathogenic fungi used in this study did not accumulate alpha-ketoadipate and alpha-aminoadipate-delta-semialdehyde when grown in medium containing alpha-aminoadipate and lysine, respectively, as sole nitrogen source. However, only pathogenic fungi used both lysine and alpha-aminoadipate as sole nitrogen source. This unique metabolic property could be useful for the identification of these pathogens.","authors":"Ye ZH, Garrad RC, Winston MK, Bhattacharjee JK","authors_abbrev":"Ye ZH et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14625898","title":"Ksg1, a homologue of the phosphoinositide-dependent protein kinase 1, controls cell wall integrity in Schizosaccharomyces pombe.","citation":"J Basic Microbiol 2003;43(6):473-82","abstract":"It has previously been shown that the Schizosaccharomyces pombe mutant ksg1-358 has a mating and sporulation defect at 30 degrees C and that it is temperature sensitive for growth at 35 degrees C. However the molecular basis for these phenotypes remained largely unknown. In this study we show that ksg1-358 mutant cells lysed at the non-permissive temperature, which could be prevented by sorbitol. Overexpression of ksg1 using the nmt1-promoter showed slow growth and cells became swollen when incubated at 35 degrees C under low inositol conditions. Interestingly, in a two-hybrid assay we found that the ksg1-protein interacted with Pck1p, a protein implicated in regulating cell wall integrity in S. pombe. Genetic complementation assays showed that an overexpression of pck2, the homologue of pck1 involved in the regulation of cell wall synthesis, could partially rescue ksg1-358 phenotypes. We digested the ksg1-358 cell wall using beta-glucanase. We found that the ksg1-358 mutant was more resistant to cell lysis at 30 degrees C than the wildtype strain h972, which was similar to a pck1-deletion strain. A ksg1-overexpressing strain was hypersensitive towards beta-glucanase treatment similar to a pck2-deletion strain. The pck1-deletion partially rescued beta-glucanase hypersensitivity of the ksg1-overexpressing strain but the pck2-deletion increased it. The ksg1-358 mutation increased beta-glucanase resistance of a pck1-overexpressing strain but it had no effect on a pck2-overexpressing strain. Our results provide evidence that ksg1 is a novel regulator of cell wall integrity in the fission yeast Schizosaccharomyces pombe. They further suggest that Ksg1p acts in a pathway with Pck1p, possibly upstream and through direct interaction.","authors":"Gräub R, Hilti N, Niederberger C, Schweingruber ME","authors_abbrev":"Gräub R et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-11-20","publication_year":"2003","canto_session_key":"61076bdb7aff52c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-05-15 15:48:09","canto_approved_date":"2024-03-28 17:23:03","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-05-15 15:48:03","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.14c","SPCC576.15c","SPBC12D12.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-05-15"},{"uniquename":"PMID:2302195","title":"Electrofusion of oriented Schizosaccharomyces pombe cells through apical protoplast-protuberances.","citation":"Biochem Biophys Res Commun 1990 Jan 15;166(1):113-8","abstract":"The electrofusion of oriented Schizosaccharomyces pombe cells through apical protoplast-protuberances was demonstrated. The protuberances arose after an exposure of early-exponential phase cells to digestive enzymes from hepatopancreas of Helix pomatia. The orientation of cylindric cells within pearl chains was produced by the application of inhomogenous alternating electric fields.","authors":"Vondrejs V, Pavlícek I, Kothera M, Palková Z","authors_abbrev":"Vondrejs V et al.","pubmed_publication_date":"15 Jan 1990","pubmed_entrez_date":"1990-01-15","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11696345","title":"Cell cycle: the Flp side of Cdc14.","citation":"Curr Biol 2001 Oct 30;11(21):R872-4","abstract":"Despite their conserved structures, protein phosphatases of the budding yeast Cdc14p family appear to perform distinct physiological roles in controlling late events of the cell cycle in different organisms.","authors":"Oliferenko S, Balasubramanian MK","authors_abbrev":"Oliferenko S et al.","pubmed_publication_date":"30 Oct 2001","pubmed_entrez_date":"2001-11-07","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18522942","title":"Post-transcriptional regulation of the U3 small nucleolar RNA.","citation":"J Biol Chem 2008 Aug 01;283(31):21404-10","abstract":"A high copy shuttle vector was used to express a \"tagged\" U3 small nucleolar RNA (snoRNA) gene in Schizosaccharomyces pombe to examine regulatory responses to a high gene dosage. RNA analyses utilizing reverse transcription-PCR amplification and restriction fragment length polymorphism indicated that the tagged gene was both proportionally and highly expressed and that downstream processing and/or termination were critical to U3 snoRNA stability. In contrast, direct measurements of the total cellular U3 snoRNA showed essentially normal levels of mature RNA, although measurements of precursor levels confirmed a highly expressed gene construct. Taken together, the results indicated that the steady state amounts of mature U3 snoRNA were primarily regulated at the post-transcriptional level. This regulatory mechanism prevents over-accumulation of the cellular U3 snoRNA and can efficiently degrade mutant RNA molecules. Together with past studies on other 3' extended RNA precursors, the results support post-transcriptional regulation as a quality control mechanism in which appropriate amounts of functional RNA are stabilized by protein interaction while excess or defective RNA is rapidly degraded. Precursor processing in vitro and mutational analyses were consistent with this model.","doi":"10.1074/jbc.M802189200","authors":"Nabavi S, Nellimarla S, Nazar RN","authors_abbrev":"Nabavi S et al.","pubmed_publication_date":"01 Aug 2008","pubmed_entrez_date":"2008-06-05","publication_year":"2008","canto_session_key":"443d20fbac31cbaa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-08-15 14:27:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-15 14:27:33","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.07","SPSNRNA.03"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-08-15"},{"uniquename":"EMBL:AB084871","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.817"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21861884","title":"Biological interaction networks are conserved at the module level.","citation":"BMC Syst Biol 2011 Aug 23;5:134","abstract":"Orthologous genes are highly conserved between closely related species and biological systems often utilize the same genes across different organisms. However, while sequence similarity often implies functional similarity, interaction data is not well conserved even for proteins with high sequence similarity. Several recent studies comparing high throughput data including expression, protein-protein, protein-DNA, and genetic interactions between close species show conservation at a much lower rate than expected.\nIn this work we collected comprehensive high-throughput interaction datasets for four model organisms (S. cerevisiae, S. pombe, C. elegans, and D. melanogaster) and carried out systematic analyses in order to explain the apparent lower conservation of interaction data when compared to the conservation of sequence data. We first showed that several previously proposed hypotheses only provide a limited explanation for such lower conservation rates. We combined all interaction evidences into an integrated network for each species and identified functional modules from these integrated networks. We then demonstrate that interactions that are part of functional modules are conserved at much higher rates than previous reports in the literature, while interactions that connect between distinct functional modules are conserved at lower rates.\nWe show that conservation is maintained between species, but mainly at the module level. Our results indicate that interactions within modules are much more likely to be conserved than interactions between proteins in different modules. This provides a network based explanation to the observed conservation rates that can also help explain why so many biological processes are well conserved despite the lower levels of conservation for the interactions of proteins participating in these processes.Accompanying website: http://www.sb.cs.cmu.edu/CrossSP.","doi":"10.1186/1752-0509-5-134","authors":"Zinman GE, Zhong S, Bar-Joseph Z","authors_abbrev":"Zinman GE et al.","pubmed_publication_date":"23 Aug 2011","pubmed_entrez_date":"2011-08-25","publication_year":"2011","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18673459","title":"The Schizosaccharomyces pombe Map4 adhesin is a glycoprotein that can be extracted from the cell wall with alkali but not with beta-glucanases and requires the C-terminal DIPSY domain for function.","citation":"Mol Microbiol 2008 Sep;69(6):1476-90","abstract":"In fungi, cell adhesion is required for flocculation, mating and virulence, and it is mediated by covalently bound cell wall proteins termed adhesins. Map4, an adhesin required for mating in Schizosaccharomyces pombe, is N-glycosylated and O-glycosylated, and is an endogenous substrate for the mannosyl transferase Oma4p. Map4 has a modular structure with an N-terminal signal peptide, a serine and threonine (S/T)-rich domain that includes nine repeats of 36 amino acids (rich in serine and threonine residues, but lacking glutamines), and a C-terminal DIPSY domain with no glycosylphosphatidyl inositol (GPI)-anchor signal. Map4 can be extracted from cell walls with SDS/mercaptoethanol sample buffer or with mild alkali solutions. After extensive extraction with hot sample buffer, no more protein can be released by beta-glucanases or alkali. Additionally, none of the cysteine residues of the protein is required for its retention at the cell wall. These results show that Map4 is not directly bound to beta-glucans and point to the existence of alkali- and SDS/mercaptoethanol-sensitive linkages between cell wall proteins. The N-terminal S/T-rich regions are required for cell wall attachment, but the C-terminal DIPSY domain is required for agglutination and mating in liquid and solid media.","doi":"10.1111/j.1365-2958.2008.06375.x","authors":"Sharifmoghadam MR, Valdivieso MH","authors_abbrev":"Sharifmoghadam MR et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-08-05","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20032302","title":"The cell surface protein gene ecm33+ is a target of the two transcription factors Atf1 and Mbx1 and negatively regulates Pmk1 MAPK cell integrity signaling in fission yeast.","citation":"Mol Biol Cell 2010 Feb 15;21(4):674-85","abstract":"The highly conserved fission yeast Pmk1 MAPK pathway plays a key role in cell integrity by regulating Atf1, which belongs to the ATF/cAMP-responsive element-binding (CREB) protein family. We identified and characterized ecm33(+), which encodes a glycosyl-phosphatidylinositol (GPI)-anchored cell surface protein as a transcriptional target of Pmk1 and Atf1. We demonstrated that the gene expression of Ecm33 is regulated by two transcription factors Atf1 and a MADS-box-type transcription factor Mbx1. We identified a putative ATF/CREB-binding site and an RLM1-binding site in the ecm33(+) promoter region and monitored the transcriptional activity of Atf1 or Mbx1 in living cells using a destabilized luciferase reporter gene fused to three tandem repeats of the CRE and six tandem repeats of the Rlm1-binding sequence, respectively. These reporter genes reflect the activation of the Pmk1 pathway by various stimuli, thereby enabling the real-time monitoring of the Pmk1 cell integrity pathway. Notably, the Deltaecm33 cells displayed hyperactivation of the Pmk1 signaling together with hypersensitivity to Ca(2+) and an abnormal morphology, which were almost abolished by simultaneous deletion of the components of the Rho2/Pck2/Pmk1 pathway. Our results suggest that Ecm33 is involved in the negative feedback regulation of Pmk1 cell integrity signaling and is linked to cellular Ca(2+) signaling.","authors":"Takada H, Nishida A, Domae M, Kita A, Yamano Y, Uchida A, Ishiwata S, Fang Y, Zhou X, Masuko T, Kinoshita M, Kakehi K, Sugiura R","authors_abbrev":"Takada H et al.","pubmed_publication_date":"15 Feb 2010","pubmed_entrez_date":"2009-12-25","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPAC1705.03c","SPBC119.08","SPBC29B5.01","SPBC19G7.06"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:26519321","title":"A Review of Fluorescent Proteins for Use in Yeast.","citation":"Methods Mol Biol 2016;1369:309-46","abstract":"The field of fluorescent proteins (FPs) is constantly developing. The use of FPs changed the field of life sciences completely, starting a new era of direct observation and quantification of cellular processes. The broad spectrum of FPs (see Fig. 1) with a wide range of characteristics allows their use in many different experiments. This review discusses the use of FPs for imaging in budding yeast (Saccharomyces cerevisiae) and fission yeast Schizosaccharomyces pombe). The information included in this review is relevant for both species unless stated otherwise.","doi":"10.1007/978-1-4939-3145-3_21","authors":"Bialecka-Fornal M, Makushok T, Rafelski SM","authors_abbrev":"Bialecka-Fornal M et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-11-01","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-02 01:19:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11073977","title":"Damage tolerance protein Mus81 associates with the FHA1 domain of checkpoint kinase Cds1.","citation":"Mol Cell Biol 2000 Dec;20(23):8758-66","abstract":"Cds1, a serine/threonine kinase, enforces the S-M checkpoint in the fission yeast Schizosaccharomyces pombe. Cds1 is required for survival of replicational stress caused by agents that stall replication forks, but how Cds1 performs these functions is largely unknown. Here we report that the forkhead-associated-1 (FHA1) protein-docking domain of Cds1 interacts with Mus81, an evolutionarily conserved damage tolerance protein. Mus81 has an endonuclease homology domain found in the XPF nucleotide excision repair protein. Inactivation of mus81 reveals a unique spectrum of phenotypes. Mus81 enables survival of deoxynucleotide triphosphate starvation, UV radiation, and DNA polymerase impairment. Mus81 is essential in the absence of Bloom's syndrome Rqh1 helicase and is required for productive meiosis. Genetic epistasis studies suggest that Mus81 works with recombination enzymes to properly replicate damaged DNA. Inactivation of Mus81 triggers a checkpoint-dependent delay of mitosis. We propose that Mus81 is involved in the recruitment of Cds1 to aberrant DNA structures where Cds1 modulates the activity of damage tolerance enzymes.","authors":"Boddy MN, Lopez-Girona A, Shanahan P, Interthal H, Heyer WD, Russell P","authors_abbrev":"Boddy MN et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-14","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3E7.08c","SPBC336.04","SPCC18B5.11c","SPCC4G3.05c","SPCC1259.13","SPBC19C7.09c","SPAC3H5.06c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:11531413","title":"HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25.","citation":"Virology 2001 Sep 01;287(2):359-70","abstract":"Viral protein R (Vpr) of human immunodeficiency virus type 1 induces G2 arrest in cells from distantly related eukaryotes including human and fission yeast through inhibitory phosphorylation of tyrosine 15 (Tyr15) on Cdc2. Since the DNA damage and DNA replication checkpoints also induce G2 arrest through phosphorylation of Tyr15, it seemed possible that Vpr induces G2 arrest through the checkpoint pathways. However, Vpr does not use either the early or the late checkpoint genes that are required for G2 arrest in response to DNA damage or inhibition of DNA synthesis indicating that Vpr induces G2 arrest by an alternative pathway. It was found that protein phosphatase 2A (PP2A) plays an important role in the induction of G2 arrest by Vpr since mutations in genes coding for a regulatory or catalytic subunit of PP2A reduce Vpr-induced G2 arrest. Vpr was also found to upregulate PP2A, supporting a model in which Vpr activates the PP2A holoenzyme to induce G2 arrest. PP2A is known to interact genetically in fission yeast with the Wee1 kinase and Cdc25 phosphatase that act on Tyr15 of Cdc2. Both Wee1 and Cdc25 play a role in Vpr-induced G2 arrest since a wee1 deletion reduces Vpr-induced G2 arrest and a direct in vivo assay shows that Vpr inhibits Cdc25. Additional support for both Wee1 and Cdc25 playing a role in Vpr-induced G2 arrest comes from a genetic screen, which identified genes whose overexpression affects Vpr-induced G2 arrest. For this genetic screen, a strain was constructed in which cell killing by Vpr was nearly eliminated while the effect of Vpr on the cell cycle was clearly indicated by an increase in cell length. Overexpression of the wos2 gene, an inhibitor of Wee1, suppresses Vpr-induced G2 arrest while overexpression of rad25, an inhibitor of Cdc25, enhances Vpr-induced G2 arrest. These two genes may be part of the uncharacterized pathway for Vpr-induced G2 arrest in which Vpr upregulates PP2A to activate Wee1 and inhibit Cdc25.","authors":"Elder RT, Yu M, Chen M, Zhu X, Yanagida M, Zhao Y","authors_abbrev":"Elder RT et al.","pubmed_publication_date":"01 Sep 2001","pubmed_entrez_date":"2001-09-05","publication_year":"2001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:30190560","title":"Power law fitness landscapes and their ability to predict fitness.","citation":"Heredity (Edinb) 2018 Nov;121(5):482-498","abstract":"Whether or not evolution by natural selection is predictable depends on the existence of general patterns shaping the way mutations interact with the genetic background. This interaction, also known as epistasis, has been observed during adaptation (macroscopic epistasis) and in individual mutations (microscopic epistasis). Interestingly, a consistent negative correlation between the fitness effect of beneficial mutations and background fitness (known as diminishing returns epistasis) has been observed across different species and conditions. We tested whether the adaptation pattern of an additional species, Schizosaccharomyces pombe, followed the same trend. We used strains that differed by the presence of large karyotype differences and observed the same pattern of fitness convergence. Using these data along with published datasets, we measured the ability of different models to describe adaptation rates. We found that a phenotype-fitness landscape shaped like a power law is able to correctly predict adaptation dynamics in a variety of species and conditions. Furthermore we show that this model can provide a link between the observed macroscopic and microscopic epistasis. It may be very useful in the development of algorithms able to predict the adaptation of microorganisms from measures of the current phenotypes. Overall, our results suggest that even though adaptation quickly slows down, populations adapting to lab conditions may be quite far from a fitness peak.","doi":"10.1038/s41437-018-0143-5","authors":"Passagem-Santos D, Zacarias S, Perfeito L","authors_abbrev":"Passagem-Santos D et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-09-08","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-09-09 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28471318","title":"Substrate recognition of the catalytic α-subunit of glucosidase II from Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2017 Aug;81(8):1503-1511","abstract":"The recombinant catalytic α-subunit of N-glycan processing glucosidase II from Schizosaccharomyces pombe (SpGIIα) was produced in Escherichia coli. The recombinant SpGIIα exhibited quite low stability, with a reduction in activity to <40% after 2-days preservation at 4 °C, but the presence of 10% (v/v) glycerol prevented this loss of activity. SpGIIα, a member of the glycoside hydrolase family 31 (GH31), displayed the typical substrate specificity of GH31 α-glucosidases. The enzyme hydrolyzed not only α-(1→3)- but also α-(1→2)-, α-(1→4)-, and α-(1→6)-glucosidic linkages, and p-nitrophenyl α-glucoside. SpGIIα displayed most catalytic properties of glucosidase II. Hydrolytic activity of the terminal α-glucosidic residue of Glc 2 Man 3 -Dansyl was faster than that of Glc 1 Man 3 -Dansyl. This catalytic α-subunit also removed terminal glucose residues from native N-glycans (Glc 2 Man 9 GlcNAc 2  and Glc 1 Man 9 GlcNAc 2 ) although the activity was low.","doi":"10.1080/09168451.2017.1320520","authors":"Okuyama M, Miyamoto M, Matsuo I, Iwamoto S, Serizawa R, Tanuma M, Ma M, Klahan P, Kumagai Y, Tagami T, Kimura A","authors_abbrev":"Okuyama M et al.","pubmed_publication_date":"Aug 2017","pubmed_entrez_date":"2017-05-05","publication_year":"2017","canto_session_key":"6eb04bddfcb3a04d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-05-06 00:15:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17471961","title":"[RNA-protein complex that governs meiosis in fission yeast].","citation":"Tanpakushitsu Kakusan Koso 2006 Dec;51(16 Suppl):2443-9","abstract":"","authors":"Yamashita A, Harigaya Y, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2007-05-03","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10970777","title":"Disruption and overexpression of the Schizosaccharomyces pombe aph1 gene and the effects on intracellular diadenosine 5',5'''-P1, P4-tetraphosphate (Ap4A), ATP and ADP concentrations.","citation":"Biochem J 2000 Sep 15;350 Pt 3(Pt 3):663-9","abstract":"Diadenosine oligophosphates are ubiquitous compounds that were discovered over 30 years ago. Diadenosine 5',5\"'-P(1), P(4)-tetraphosphate (Ap(4)A) is the most studied member of this family, and its function in yeast is unknown. To investigate possible functions, we changed the intracellular Ap(4)A concentration in Schizosaccharomyces pombe via disruption and overexpression of the aph1 gene, which encodes an Ap(4)A hydrolase (Aph1). S. pombe Aph1 is 52% identical with a human tumour suppressor protein, Fhit, in a core region of 109 amino acids. Disruption of aph1 resulted in an 85% decrease in Ap(4)A hydrolase activity and a 290-fold increase in the intracellular Ap(4)A concentration. The disruption and subsequent increase in intracellular Ap(4)A concentration had no significant effect on the growth of S. pombe. Overexpression of the S. pombe aph1 gene, resulting in 17- and 84-fold increases in Ap(4)A hydrolase activity above wild-type levels, resulted in 60 and 80% decreases respectively in the intracellular Ap(4)A concentration. This represents the first report of a decrease in the intracellular Ap(4)A concentration in response to overexpression of a degradative enzyme in any eukaryotic organism. We describe a new S. pombe expression plasmid, pPOX, which was used to achieve the largest increase in expression of aph1. Overexpression of aph1 at the highest level resulted in a 46% increase in generation time in comparison with the control strain. Neither overexpression nor disruption had any effect on the intracellular ATP or ADP concentrations. This is the first report of ADP and ATP concentrations in S. pombe. These data also indicate that Aph1 functions in vivo to degrade Ap(4)A, and that high-level overexpression of this enzyme reduces the growth rate.","authors":"Ingram SW, Barnes LD","authors_abbrev":"Ingram SW et al.","pubmed_publication_date":"15 Sep 2000","pubmed_entrez_date":"2000-09-06","publication_year":"2000","canto_session_key":"e9e39a22b3cf3516","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-17 20:01:06","canto_approved_date":"2024-04-03 15:42:32","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-06-12 09:09:16","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-17"},{"uniquename":"PMID:26422458","title":"Asp1 from Schizosaccharomyces pombe binds a [2Fe-2S](2+) cluster which inhibits inositol pyrophosphate 1-phosphatase activity.","citation":"Biochemistry 2015 Oct 27;54(42):6462-74","abstract":"Iron-sulfur (Fe-S) clusters are widely distributed protein cofactors that are vital to cellular biochemistry and the maintenance of bioenergetic homeostasis, but to our knowledge, they have never been identified in any phosphatase. Here, we describe an iron-sulfur cluster in Asp1, a dual-function kinase/phosphatase that regulates cell morphogenesis in Schizosaccharomyces pombe. Full-length Asp1, and its phosphatase domain (Asp1(371-920)), were each heterologously expressed in Escherichia coli. The phosphatase activity is exquisitely specific: it hydrolyzes the 1-diphosphate from just two members of the inositol pyrophosphate (PP-InsP) signaling family, namely, 1-InsP7 and 1,5-InsP8. We demonstrate that Asp1 does not hydrolyze either InsP6, 2-InsP7, 3-InsP7, 4-InsP7, 5-InsP7, 6-InsP7, or 3,5-InsP8. We also recorded 1-phosphatase activity in a human homologue of Asp1, hPPIP5K1, which was heterologously expressed in Drosophila S3 cells with a biotinylated N-terminal tag, and then isolated from cell lysates with avidin beads. Purified, recombinant Asp1(371-920) contained iron and acid-labile sulfide, but the stoichiometry (0.8 atoms of each per protein molecule) indicates incomplete iron-sulfur cluster assembly. We reconstituted the Fe-S cluster in vitro under anaerobic conditions, which increased the stoichiometry to approximately 2 atoms of iron and acid-labile sulfide per Asp1 molecule. The presence of a [2Fe-2S](2+) cluster in Asp1(371-920) was demonstrated by UV-visible absorption, resonance Raman spectroscopy, and electron paramagnetic resonance spectroscopy. We determined that this [2Fe-2S](2+) cluster is unlikely to participate in redox chemistry, since it rapidly degraded upon reduction by dithionite. Biochemical and mutagenic studies demonstrated that the [2Fe-2S](2+) cluster substantially inhibits the phosphatase activity of Asp1, thereby increasing its net kinase activity.","doi":"10.1021/acs.biochem.5b00532","authors":"Wang H, Nair VS, Holland AA, Capolicchio S, Jessen HJ, Johnson MK, Shears SB","authors_abbrev":"Wang H et al.","pubmed_publication_date":"27 Oct 2015","pubmed_entrez_date":"2015-10-01","publication_year":"2015","canto_session_key":"83d3bee37f8b40fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Huanchen Wang","canto_first_approved_date":"2016-07-06 08:53:39","canto_approved_date":"2019-05-02 21:57:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-06-20 11:43:24","canto_added_date":"2015-10-02 00:18:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Huanchen Wang","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-07-06"},{"uniquename":"PMID:2004701","title":"A gene in Schizosaccharomyces pombe analogous to the RAD4 gene of Saccharomyces cerevisiae.","citation":"FEMS Microbiol Lett 1991 Jan 01;61(1):97-100","abstract":"A gene, analogous to the RAD4 gene, which is required for nucleotide excision repair in Saccharomyces cerevisiae, also exists in Schizosaccharomyces pombe. RNA isolated from wild type S. pombe cells strongly cross-hybridized with the 1.2 kb PvuII DNA fragment of the S. cerevisiae RAD4 genomic clone (pPC1). Chromosomal DNA isolated from S. pombe had similar restriction patterns to those from S. cerevisiae, as determined by Southern blot analysis. Two species of mRNA, 3.1 and 1.8 kb, were identified by Northern hybridization. The level of these transcripts did not increase upon UV-irradiation, suggesting that the RAD4-like gene in S. pombe is not UV-inducible.","authors":"Choi IS, Kim JB, Hong SH, Park SD","authors_abbrev":"Choi IS et al.","pubmed_publication_date":"01 Jan 1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_session_key":"54f074d999d5dd1b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 12:56:17","canto_session_submitted_date":"2012-03-03 12:55:47","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.18c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:12676088","title":"Telomere maintenance in fission yeast requires an Est1 ortholog.","citation":"Curr Biol 2003 Apr 01;13(7):575-80","abstract":"Telomerase regulation is critical to genome maintenance yet remains poorly understood. Without telomerase's ability to synthesize telomere repeats, chromosome ends shorten progressively, as conventional DNA polymerases cannot fully replicate the ends of linear molecules. In Saccharomyces cerevisiae, telomerase activity in vivo absolutely depends on a set of telomerase accessory proteins that includes Est1p, which appears to recruit or activate telomerase at the site of polymerization. Thus, est1Delta cells have the same cellular senescence phenotype as cells lacking either the catalytic protein subunit of telomerase or its template-containing RNA subunit. While the telomerase protein is highly conserved among eukaryotes, the apparent lack of Est1p homologs has frustrated efforts to describe a common mechanism of telomerase recruitment and activation. Here, we describe SpEst1p, a homolog of Est1p from the evolutionarily distant Schizosaccharomyces pombe. Like ScEst1p, SpEst1p is required for telomerase activity in vivo. Coupled with the identification of an orthologous Est1 protein in humans [10], this suggests a much wider conservation of telomerase regulation than was previously known. Strikingly, in cells with compromised telomere function (taz1Delta), SpEst1p loss confers a lethal germination phenotype, while telomerase loss does not, indicating that SpEst1p plays an unexpected additional role in chromosome end protection.","authors":"Beernink HT, Miller K, Deshpande A, Bucher P, Cooper JP","authors_abbrev":"Beernink HT et al.","pubmed_publication_date":"01 Apr 2003","pubmed_entrez_date":"2003-04-05","publication_year":"2003","canto_session_key":"4ebdf0faaedaf02f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-02 16:14:14","canto_approved_date":"2024-06-26 12:19:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-10 14:46:12","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.03c","SPAC16A10.07c","SPBC2D10.13","SPBC29A3.14c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-06-02"},{"uniquename":"PMID:37728314","title":"Inositol pyrophosphate dynamics reveals control of the yeast phosphate starvation program through 1,5-IP 8  and the SPX domain of Pho81.","citation":"Elife 2023 Sep 20;12","abstract":"Eukaryotic cells control inorganic phosphate to balance its role as essential macronutrient with its negative bioenergetic impact on reactions liberating phosphate. Phosphate homeostasis depends on the conserved INPHORS signaling pathway that utilizes inositol pyrophosphates and SPX receptor domains. Since cells synthesize various inositol pyrophosphates and SPX domains bind them promiscuously, it is unclear whether a specific inositol pyrophosphate regulates SPX domains in vivo, or whether multiple inositol pyrophosphates act as a pool. In contrast to previous models, which postulated that phosphate starvation is signaled by increased production of the inositol pyrophosphate 1-IP 7 , we now show that the levels of all detectable inositol pyrophosphates of yeast, 1-IP 7 , 5-IP 7 , and 1,5-IP 8 , strongly decline upon phosphate starvation. Among these, specifically the decline of 1,5-IP 8  triggers the transcriptional phosphate starvation response, the PHO pathway. 1,5-IP 8  inactivates the cyclin-dependent kinase inhibitor Pho81 through its SPX domain. This stimulates the cyclin-dependent kinase Pho85-Pho80 to phosphorylate the transcription factor Pho4 and repress the PHO pathway. Combining our results with observations from other systems, we propose a unified model where 1,5-IP 8  signals cytosolic phosphate abundance to SPX proteins in fungi, plants, and mammals. Its absence triggers starvation responses.","doi":"10.7554/eLife.87956","authors":"Chabert V, Kim GD, Qiu D, Liu G, Michaillat Mayer L, Jamsheer K M, Jessen HJ, Mayer A","authors_abbrev":"Chabert V et al.","pubmed_publication_date":"20 Sep 2023","pubmed_entrez_date":"2023-09-20","publication_year":"2023","canto_session_key":"50184c21d1355043","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-09-21 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6287225","title":"Structure of the Schizosaccharomyces pombe cytochrome c gene.","citation":"Mol Cell Biol 1982 Feb;2(2):106-16","abstract":"The cytochrome c gene of the fission yeast Schizosaccharomyces pombe has been cloned by using the Saccharomyces cerevisiae iso-1-cytochrome c gene as a molecular hybridization probe. The DNA sequence and the 5' termini of the mRNA transcripts of the gene have been determined. The DNA sequence has confirmed, with two exceptions, the previously determined protein sequence. The nonrandom distribution of silent third base differences which was observed between the two cytochrome c genes of S. cerevisiae does not extend to the S. pombe cytochrome c gene, suggesting that there are no constraints other than protein function and codon usage which have acted to conserve the cytochrome DNA sequences of the two yeasts. Introduction of the S. pombe cytochrome c gene on a yeast plasmid into a S. cerevisiae mutant which lacked functional cytochrome c transformed that recipient strain for the ability to grow on a nonfermentable carbon source. This implies that the S. pombe cytochrome c gene has all the regulatory signals which are required for its expression in S. cerevisiae, and that none of the amino acid differences between the cytochrome c proteins of the two yeasts has a drastic effect on the function of the protein in vivo.","authors":"Russell PR, Hall BD","authors_abbrev":"Russell PR et al.","pubmed_publication_date":"Feb 1982","pubmed_entrez_date":"1982-02-01","publication_year":"1982","canto_session_key":"69e21b542191908c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-07-25 14:52:26","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-07-02 13:12:59","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC191.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-07-02"},{"uniquename":"EMBL:AU011735","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28349389","title":"Quantitative Genome-Wide Measurements of Meiotic DNA Double-Strand Breaks and Protein Binding in S. pombe.","citation":"Methods Mol Biol 2017;1471:25-49","abstract":"The fission yeast Schizosaccharomyces pombe is especially well suited for studying meiosis in molecular detail. Experiments with S. pombe strains that undergo a nearly synchronous meiosis-at variable temperatures-have elucidated the mechanisms of meiotic progression and the proteins that are involved. For example, studies focused on the initiation of meiotic recombination by programmed DNA double-strand breaks (DSBs) have proven exceptionally informative. In meiosis, some regions of DNA have more frequent DSBs than the surrounding regions. These DSB hotspots can be visualized by Southern blot hybridization of restriction fragments ranging from kilobases (kb) to megabases (Mb) in size. More recently, the benefits of genome-wide analysis to map the distribution and frequency of meiotic DSBs have been attained, with resolution down to the nucleotide level. Infrequent, non-hotspot DSBs previously not detectable have been observed, creating a better understanding of how recombination is regulated. Additional genome-wide analyses have shown proteins that bind specifically to DSB hotspots, providing insight into how the DSB initiation complex functions. We describe here detailed methods for achieving these results.","doi":"10.1007/978-1-4939-6340-9_2","authors":"Hyppa RW, Fowler KR, Smith GR","authors_abbrev":"Hyppa RW et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-03-29","publication_year":"2017","canto_session_key":"492bf4821e95cc26","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-31 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010426","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1011009","title":"A function for the plasmalemma grooves of a fission yeast.","citation":"J Gen Microbiol 1976 Dec;97(2):161-7","abstract":"Ultrastructural studies on regenerating protoplasts of Schizosaccharomyces pombe show that the spatial differentiation of the plasmalemma into grooves and flat areas is reflected in a functional differentiation in cell-wall synthesis. The grooves are the initial site of production of wall fibrils.","authors":"Hereward FV","authors_abbrev":"Hereward FV","pubmed_publication_date":"Dec 1976","pubmed_entrez_date":"1976-12-01","publication_year":"1976","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29959912","title":"SAHA and cisplatin sensitize gastric cancer cells to doxorubicin by induction of DNA damage, apoptosis and perturbation of AMPK-mTOR signalling.","citation":"Exp Cell Res 2018 Sep 15;370(2):283-291","abstract":"Chemotherapy remains the most prescribed anti-cancer therapy, despite patients suffering severe side effects and frequently developing chemoresistance. These complications can be partially overcome by combining different chemotherapeutic agents that target multiple biological pathways. However, selecting efficacious drug combinations remains challenging. We previously used fission yeast Schizosaccharomycespombe as a surrogate model to predict drug combinations, and showed that suberoylanilide hydroxamic acid (SAHA) and cisplatin can sensitise gastric adenocarcinoma cells toward the cytotoxic effects of doxorubicin. Yet, how this combination undermines cell viability is unknown. Here, we show that SAHA and doxorubicin markedly enhance the cleavage of two apoptosis markers, caspase 3 and poly-ADP ribose polymerase (PARP-1), and increase the phosphorylation of γH2AX, a marker of DNA damage. Further, we found a prominent reduction in Ser485 phosphorylation of AMP-dependent protein kinase (AMPK), and reductions in its target mTOR and downstream ribosomal protein S6 phosphorylation. We show that SAHA contributes most of the effect, as confirmed using another histone deacetylase inhibitor, trichostatin A. Overall, our results show that the combination of SAHA and doxorubicin can induce apoptosis in gastric adenocarcinoma in a synthetically lethal manner, and that fission yeast offers an efficient tool for identifying potent drug combinations against human cancer cells.","doi":"10.1016/j.yexcr.2018.06.029","authors":"Seah KS, Loh JY, Nguyen TTT, Tan HL, Hutchinson PE, Lim KK, Dymock BW, Long YC, Lee EJD, Shen HM, Chen ES","authors_abbrev":"Seah KS et al.","pubmed_publication_date":"15 Sep 2018","pubmed_entrez_date":"2018-07-01","publication_year":"2018","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2018-07-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20071248","title":"Yeast as a model system to study RecQ helicase function.","citation":"DNA Repair (Amst) 2010 Mar 02;9(3):303-14","abstract":"Mutations in the highly conserved RecQ helicase, BLM, cause the rare cancer predisposition disorder, Bloom's syndrome. The orthologues of BLM in Saccharomyces cerevisiae and Schizosaccharomyces pombe are SGS1 and rqh1(+), respectively. Studies in these yeast species have revealed a plethora of roles for the Sgs1 and Rqh1 proteins in repair of double strand breaks, restart of stalled replication forks, processing of aberrant intermediates that arise during meiotic recombination, and maintenance of telomeres. In this review, we focus on the known roles of Sgs1 and Rqh1 and how studies in yeast species have improved our knowledge of how BLM suppresses neoplastic transformation.","doi":"10.1016/j.dnarep.2009.12.007","authors":"Ashton TM, Hickson ID","authors_abbrev":"Ashton TM et al.","pubmed_publication_date":"02 Mar 2010","pubmed_entrez_date":"2010-01-15","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23986475","title":"Spd1 accumulation causes genome instability independently of ribonucleotide reductase activity but functions to protect the genome when deoxynucleotide pools are elevated.","citation":"J Cell Sci 2013 Nov 01;126(Pt 21):4985-94","abstract":"Cullin4, Ddb1 and Cdt2 are core subunits of the ubiquitin ligase complex CRL4(Cdt2), which controls genome stability by targeting Spd1 for degradation during DNA replication and repair in fission yeast. Spd1 has an inhibitory effect on ribonucleotide reductase (RNR), the activity of which is required for deoxynucleotide (dNTP) synthesis. The failure to degrade Spd1 in mutants where CRL4(Cdt2) is defective leads to DNA integrity checkpoint activation and dependency. This correlates with a lower dNTP pool. Pools are restored in a spd1-deleted background and this also suppresses checkpoint activation and dependency. We hypothesized that fission yeast with RNR hyperactivity would display a mutator phenotype on their own, but also possibly repress aspects of the phenotype associated with the inability to target Spd1 for degradation. Here, we report that a mutation in the R1 subunit of ribonucleotide reductase cdc22 (cdc22-D57N), which alleviated allosteric feedback inhibition, caused a highly elevated dNTP pool that was further increased by deleting spd1. The Δspd1 cdc22-D57N double mutant had elevated mutation rates and was sensitive to damaging agents that cause DNA strand breaks, demonstrating that Spd1 can protect the genome when dNTP pools are high. In ddb1-deleted cells, cdc22-D57N also potently elevated RNR activity, but failed to allow cell growth independently of the intact checkpoint. Our results provide evidence that excess Spd1 interferes with other functions in addition to its inhibitory effect on ribonucleotide reduction to generate replication stress and genome instability.","doi":"10.1242/jcs.132837","authors":"Fleck O, Vejrup-Hansen R, Watson A, Carr AM, Nielsen O, Holmberg C","authors_abbrev":"Fleck O et al.","pubmed_publication_date":"01 Nov 2013","pubmed_entrez_date":"2013-08-30","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.10c","SPAC1F7.05","SPAC29B12.03"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:8710861","title":"p34cdc2 kinase activity is maintained upon activation of the replication checkpoint in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1996 Aug 06;93(16):8278-83","abstract":"All eukaryotes use feedback controls to order and coordinate cell cycle events. In Schizosaccharomyces pombe, several classes of checkpoint genes serve to ensure that DNA replication is complete and free of error before the onset of mitosis. Wild-type cells normally arrest upon inhibition of DNA synthesis or in response to DNA damage, although the exact mechanisms controlling this arrest are unclear. Genetic evidence in fission yeast suggests that the dependence of mitosis upon completion of DNA replication is linked to the regulation of the p34cdc2 cyclin-dependent kinase. It has been hypothesized that inhibition of DNA synthesis triggers down-regulation of p34cdc2 kinase activity, although this has never been shown biochemically. We analyzed the activity of p34cdc2 in wild-type and checkpoint-defective cells treated with a DNA synthesis inhibitor. Using standard in vitro assays we demonstrate that p34cdc2 kinase activity is maintained in wild-type cells arrested at the replication checkpoint. We also used a novel in vivo assay for p34cdc2 kinase activity, in which we expressed a fragment of the human retinoblastoma tumor suppressor protein in fission yeast. Phosphorylation of this fragment of the human retinoblastoma tumor suppressor protein is dependent on p34cdc2 kinase activity, and this activity is also maintained in cells arrested at the replication checkpoint. These data suggest that the mechanism for cell-cycle arrest in response to incomplete DNA synthesis is not dependent on the attenuation of p34cdc2 activity.","authors":"Knudsen KE, Knudsen ES, Wang JY, Subramani S","authors_abbrev":"Knudsen KE et al.","pubmed_publication_date":"06 Aug 1996","pubmed_entrez_date":"1996-08-06","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28284018","title":"Chemical shift assignments of the first and second RRMs of Nrd1, a fission yeast MAPK-target RNA binding protein.","citation":"Biomol NMR Assign 2017 Oct;11(2):123-126","abstract":"Negative regulator differentiation 1 (Nrd1), a fission yeast RNA binding protein, modulates cytokinesis and sexual development and contributes to stress granule formation in response to environmental stresses. Nrd1 comprises four RRM domains and binds and stabilizes Cdc4 mRNA that encodes the myosin II light chain. Nrd1 binds the Cpc2 fission-yeast RACK1 homolog, and the interaction promotes Nrd1 localization to stress granules. Interestingly, Pmk1 mitogen-activated protein kinase phosphorylates Thr40 in the unstructured N-terminal region and Thr126 in the first RRM domain of Nrd1. Phosphorylation significantly reduces RNA-binding activity and likely modulates Nrd1 function. To reveal the relationship between the structure and function of Nrd1 and how phosphorylation affects structure, we used heteronuclear NMR techniques to investigate the three-dimensional structure of Nrd1. Here we report the  1 H,  13 C, and  15 N resonance assignments of RRM1-RRM2 (residues 108-284) comprising the first and second RRMs obtained using heteronuclear NMR techniques. Secondary structures derived from the chemical shifts are reported. These data should contribute to the understanding of the three-dimensional structure of the RRM1-RRM2 region of Nrd1 and the perturbation caused by phosphorylation.","doi":"10.1007/s12104-017-9731-1","authors":"Kobayashi A, Kanaba T, Satoh R, Ito Y, Sugiura R, Mishima M","authors_abbrev":"Kobayashi A et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-03-12","publication_year":"2017","canto_session_key":"7f451ab5f169eacd","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-13 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6B12.15","SPAC2F7.11"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:26582768","title":"Abo1, a conserved bromodomain AAA-ATPase, maintains global nucleosome occupancy and organisation.","citation":"EMBO Rep 2016 Jan;17(1):79-93","abstract":"Maintenance of the correct level and organisation of nucleosomes is crucial for genome function. Here, we uncover a role for a conserved bromodomain AAA-ATPase, Abo1, in the maintenance of nucleosome architecture in fission yeast. Cells lacking abo1(+) experience both a reduction and mis-positioning of nucleosomes at transcribed sequences in addition to increased intragenic transcription, phenotypes that are hallmarks of defective chromatin re-establishment behind RNA polymerase II. Abo1 is recruited to gene sequences and associates with histone H3 and the histone chaperone FACT. Furthermore, the distribution of Abo1 on chromatin is disturbed by impaired FACT function. The role of Abo1 extends to some promoters and also to silent heterochromatin. Abo1 is recruited to pericentromeric heterochromatin independently of the HP1 ortholog, Swi6, where it enforces proper nucleosome occupancy. Consequently, loss of Abo1 alleviates silencing and causes elevated chromosome mis-segregation. We suggest that Abo1 provides a histone chaperone function that maintains nucleosome architecture genome-wide.","doi":"10.15252/embr.201540476","authors":"Gal C, Murton HE, Subramanian L, Whale AJ, Moore KM, Paszkiewicz K, Codlin S, Bähler J, Creamer KM, Partridge JF, Allshire RC, Kent NA, Whitehall SK","authors_abbrev":"Gal C et al.","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2015-11-20","publication_year":"2016","canto_session_key":"352bbbd10b1d6ce0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Simon Whitehall","canto_first_approved_date":"2016-03-04 09:52:22","canto_approved_date":"2025-12-11 10:07:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-05 11:00:16","canto_added_date":"2015-11-21 01:19:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Simon Whitehall","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.09c","SPBC31F10.13c","SPAC664.01c","SPAC1783.05","SPBC609.05","SPAC31G5.19","SPBC6B1.07","SPAC212.11","SPBC8D2.04","SPBC8D2.03c","SPBP8B7.19","SPBC428.08c","SPBC19C7.11","SPBC216.05","SPBP22H7.05c"],"gene_count":15,"ltp_gene_count":9,"approved_date":"2016-03-04"},{"uniquename":"PMID:10388808","title":"Characterization of the ptr6(+) gene in fission yeast: a possible involvement of a transcriptional coactivator TAF in nucleocytoplasmic transport of mRNA.","citation":"Genetics 1999 Jul;152(3):869-80","abstract":"Transport of mRNA from the nucleus to the cytoplasm is one of the important steps in gene expression in eukaryotic cells. To elucidate a mechanism of mRNA export, we identified a novel ptr [poly(A)+ RNA transport] mutation, ptr6, which causes accumulation of mRNA in the nucleus and inhibition of growth at the nonpermissive temperature. The ptr6(+) gene was found to encode an essential protein of 393 amino acids, which shares significant homology in amino acid sequence with yTAFII67 of budding yeast Saccharomyces cerevisiae and human hTAFII55, a subunit of the general transcription factor complex TFIID. A Ptr6p-GFP fusion protein is localized in the nucleus, suggesting that Ptr6p functions there. Northern blot analysis using probes for 10 distinct mRNAs showed that the amount of tbp+ mRNA encoding the TATA-binding protein is increased five- to sixfold, whereas amounts of others are rapidly decreased at the nonpermissive temperature in ptr6-1. ptr6 has no defects in nuclear import of an NLS-GFP fusion protein. These results suggest that Ptr6p required for mRNA transport is a Schizosaccharomyces pombe homologue of yTAFII67 and hTAFII55. This is the first report suggesting that a TAF is involved in the nucleocytoplasmic transport of mRNA in addition to the transcription of the protein-coding genes.","authors":"Shibuya T, Tsuneyoshi S, Azad AK, Urushiyama S, Ohshima Y, Tani T","authors_abbrev":"Shibuya T et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-02","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13F5.02c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:8255244","title":"Antigen localization in fission yeast.","citation":"Methods Cell Biol 1993;37:201-22","abstract":"","authors":"Alfa CE, Gallagher IM, Hyams JS","authors_abbrev":"Alfa CE et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29410177","title":"Mutation in fission yeast phosphatidylinositol 4-kinase Pik1 is synthetically lethal with defect in telomere protection protein Pot1.","citation":"Biochem Biophys Res Commun 2018 Feb 19;496(4):1284-1290","abstract":"Fission yeast Pik1p is one of three phosphatidylinositol 4-kinases associated with the Golgi complex, but its function is not fully understood. Deletion of pot1 +  causes telomere degradation and chromosome circularization. We searched for the gene which becomes synthetically lethal with pot1Δ. We obtained a novel pik1 mutant, pik1-1, which is synthetically lethal with pot1Δ. We found phosphoinositol 4-phosphate in the Golgi was reduced in pik1-1. To investigate the mechanism of the lethality of the pot1Δ pik1-1 double mutant, we constructed the nmt-pot1-aid pik1-1 strain, where Pot1 function becomes low by drugs, which leads to telomere loss and chromosome circularization, and found pik1-1 mutation does not affect telomere resection and chromosome circularization. Thus, our results suggest that pik1 +  is required for the maintenance of circular chromosomes.","doi":"10.1016/j.bbrc.2018.02.001","authors":"Sugihara A, Nguyen LC, Shamim HM, Iida T, Nakase M, Takegawa K, Senda M, Jida S, Ueno M","authors_abbrev":"Sugihara A et al.","pubmed_publication_date":"19 Feb 2018","pubmed_entrez_date":"2018-02-08","publication_year":"2018","canto_session_key":"d8ef213bfc28ed5b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-02-09 01:15:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22E12.16c","SPAC26H5.06"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:2996957","title":"Purification and preliminary characterization of phosphoglycerate mutase from Schizosaccharomyces pombe.","citation":"Int J Biochem 1985;17(7):843-6","abstract":"Phosphoglycerate mutase could be purified to over 95% homogeneity by a single step procedure involving elution from Cibacron Blue-Sepharose by a pulse of cofactor 2,3-bisphosphoglycerate. Although the enzyme has been isolated in only small quantities (c. 100 micrograms), gel filtration and sodium dodecylsulphate polyacrylamide gel electrophoresis indicated that it is monomeric with Mr approximately 23,000, an extremely low value for this enzyme. Preliminary investigations of the kinetic characteristics and the nature of important amino acid side chains have been undertaken.","authors":"Price NC, Duncan D, Ogg DJ","authors_abbrev":"Price NC et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_session_key":"c3e3b73641a8cf0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-09-24 12:21:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 12:19:53","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26F1.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-24"},{"uniquename":"PMID:2703462","title":"Sexual reproduction as a response to H2O2 damage in Schizosaccharomyces pombe.","citation":"J Bacteriol 1989 Apr;171(4):1893-7","abstract":"Although sexual reproduction is widespread, its adaptive advantage over asexual reproduction is unclear. One major advantage of sex may be its promotion of recombinational repair of DNA damage during meiosis. This idea predicts that treatment of the asexual form of a facultatively sexual-asexual eucaryote with a DNA-damaging agent may cause it to enter the sexual cycle more frequently. Endogenous hydrogen peroxide is a major natural source of DNA damage. Thus, we treated vegetative cells of Schizosaccharomyces pombe with hydrogen peroxide to test if sexual reproduction increases. Among untreated stationary-phase S. pombe populations the sexual spores produced by meiosis represented about 1% of the total cells. However, treatment of late-exponential-phase vegetative cells with hydrogen peroxide increased the percentage of meiotic spores in the stationary phase by 4- to 18-fold. Oxidative damage therefore induces sexual reproduction in a facultatively sexual organism, a result expected by the hypothesis that sex promotes DNA repair.","authors":"Bernstein C, Johns V","authors_abbrev":"Bernstein C et al.","pubmed_publication_date":"Apr 1989","pubmed_entrez_date":"1989-04-01","publication_year":"1989","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084887","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6708842","title":"[Cellular inequivalence in a culture of Schizosaccharomyces pombe].","citation":"Mikrobiologiia 1984;53(1):48-9","abstract":"The fission yeast Schizosaccharomyces pombe was grown in the chemostat at D = 0.03, 0.05, 0.1, 0.15 and 0.20 h-1. The dry weight and substrate quantities, the number of cells and their morphological characteristics were determined in the steady state. The curves for the cell number and dry weight demonstrate changes in the coordination between the processes of cell growth and division at various growth rates. The cell division was shown to be asymmetric under the conditions of substrate limitation.","authors":"Vraná D","authors_abbrev":"Vraná D","pubmed_publication_date":"1984","pubmed_entrez_date":"1984-01-01","publication_year":"1984","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15062095","title":"The microtubule plus end-tracking proteins mal3p and tip1p cooperate for cell-end targeting of interphase microtubules.","citation":"Curr Biol 2004 Apr 06;14(7):548-59","abstract":"CLIP-170 and EB1 protein family members localize to growing microtubule tips and link spatial information with the control of microtubule dynamics. It is unknown whether these proteins operate independently or whether their actions are coordinated. In fission yeast the CLIP-170 homolog tip1p is required for targeting of microtubules to cell ends, whereas the role of the EB1 homolog mal3p in microtubule organization has not been investigated.\nWe show that mal3p promotes the initiation of microtubule growth and inhibits catastrophes. Premature catastrophes occur randomly throughout the cell in the absence of mal3p. mal3p decorates the entire microtubule lattice and localizes to particles along the microtubules and at their growing tips. Particles move in two directions, outbound toward the cell ends or inbound toward the cell center. At cell ends, the microtubule tip-associated mal3p particles disappear followed by a catastrophe. mal3p localizes normally in tip1-deleted cells and disappears from microtubule tips preceding the premature catastrophes. In contrast, tip1p requires mal3p to localize at microtubule tips. mal3p and tip1p directly interact in vitro.\nmal3p and tip1p form a system allowing microtubules to target cell ends. We propose that mal3p stimulates growth initiation and maintains growth by suppressing catastrophes. At cell ends, mal3p disappears from microtubule tips followed by a catastrophe. mal3p is involved in recruiting tip1p to microtubule tips. This becomes important when microtubules contact the cell cortex outside the cell ends because mal3p dissociates prematurely without tip1p, which is followed by a premature catastrophe.","authors":"Busch KE, Brunner D","authors_abbrev":"Busch KE et al.","pubmed_publication_date":"06 Apr 2004","pubmed_entrez_date":"2004-04-06","publication_year":"2004","canto_session_key":"3248946eca150af0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-05-17 16:06:00","canto_approved_date":"2025-09-04 11:57:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-05-17 16:05:45","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":1,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPAC3C7.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-05-17"},{"uniquename":"PMID:22543982","title":"Hsp90 interaction with Cdc2 and Plo1 kinases contributes to actomyosin ring condensation in fission yeast.","citation":"Curr Genet 2012 Aug;58(4):191-203","abstract":"In Schizosaccharomyces pombe, cytokinesis occurs by ordered recruitment of actomyosin components at the division site, followed by lateral condensation to produce a ring-like structure early in anaphase, which eventually matures and contracts at the end of mitosis. We found that in temperature-sensitive hsp90-w1 mutant cells, encoding an Hsp90 mutant protein, ring components were recruited to form a cortical network at the division site, but this network failed to condense into a compact ring, suggesting a role for Hsp90 in this particular step. hsp90-w1 mutant shows strong genetic interaction with specific mutant alleles of the fission yeast cdc2, such as cdc2-33. Interestingly, actomyosin ring defects in hsp90-w1 cdc2-33 mutant cells resembled that of hsp90-w1 single mutant at restrictive temperature. Noteworthy, similar genetic interaction was found with a mutant allele of polo-like kinase, plo1-ts4, suggesting that Hsp90 collaborates with Cdc2 and Plo1 cell cycle kinases to condense medial ring components. In vitro analyses suggested that Cdc2 and Plo1 physically interact with Hsp90. Association of Cdc2 to Hsp90 was ATP independent, while Plo1 binds to this chaperone in an ATP-dependent manner, indicating that these two kinases interact with different Hsp90 complexes. Overall, our analyses of hsp90-w1 reveal a possible role for this chaperone in medial ring condensation in association with Cdc2 and Plo1 kinases.","doi":"10.1007/s00294-012-0376-4","authors":"Santino A, Tallada VA, Jimenez J, Garzón A","authors_abbrev":"Santino A et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-05-01","publication_year":"2012","canto_session_key":"5585aaa9a0926d69","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC21.06c","SPAC24B11.11c","SPAC23C11.16","SPAC926.04c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:15988139","title":"The Shizosaccharomyces pombe homolog (SpMYH) of the Escherichia coli MutY is required for removal of guanine from 8-oxoguanine/guanine mispairs to prevent G:C to C:G transversions.","citation":"J Radiat Res 2005 Jun;46(2):205-14","abstract":"The frequency of G:C-->C:G transversions significantly increases upon exposure of cells to ionizing radiation or reactive oxygen species. Transversions can be prevented by base excision repair, which removes the causative modified bases from DNA. Our previous studies revealed that MutY is responsible for removing guanine from 7,8-dihydro-8-oxoguanine/guanine mispairs (8-oxoG/G) and prevents the generation of G:C-->C:G transversions in E. coli. SpMYH, a homolog of E. coli MutY, had been identified and characterized in the fission yeast S. pombe. Purified SpMYH has adenine DNA glycosylase activity on A/8-oxoG and A/G mismatch-containing oligonucleotides. In this study, we examined whether SpMYH has a similar activity allowing it to remove G from 8-oxoG/G in DNA. The purified SpMYH tightly bound to duplex oligonucleotides containing 8-oxoG/G and removed the unmodified G from 8-oxoG/G as efficiently as A from 8-oxoG/A. The activity was absent in the cell extract prepared from an SpMYH-knockout strain of S. pombe. The expression of SpMYH markedly reduced the frequency of spontaneous G:C-->C:G transversions in the E. coli mutY mutant. These results demonstrate that SpMYH is involved in the repair of 8-oxoG/G, by which it prevents mutations induced by oxidative stress in S. pombe.","authors":"Doi T, Yonekura S, Tano K, Yasuhira S, Yonei S, Zhang QM","authors_abbrev":"Doi T et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-07-01","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.02"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:14702385","title":"Forespore membrane assembly in yeast: coordinating SPBs and membrane trafficking.","citation":"J Cell Sci 2004 Jan 26;117(Pt 3):389-96","abstract":"In the yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae, sporulation involves de novo synthesis of forespore membrane (FSM) within the cytoplasm of mother cells. The FSM ultimately becomes the plasma membrane of the developing ascospores. Several protein components of the FSM have been identified. Visualization of these proteins has demonstrated the dynamic nature of the genesis and development of the FSM. It begins to develop at the differentiated outer plaque of the spindle pole bodies (SPBs) and extends outwards, encapsulating each of the haploid nuclei produced by meiosis. Several coiled-coil proteins are specifically recruited to the SPBs and play indispensable roles in FSM assembly. Temporal and spatial coordination of meiotic nuclear divisions and membrane assembly is of special importance. Comparison of the processes of FSM assembly in these yeasts shows that the basic mechanism has been conserved, even though the individual proteins involved are often different. Understanding these dynamic aspects of yeast sporulation will help to elucidate a general mechanism for the cellularization of cytoplasm containing multiple nuclei.","authors":"Shimoda C","authors_abbrev":"Shimoda C","pubmed_publication_date":"26 Jan 2004","pubmed_entrez_date":"2004-01-02","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24448448","title":"Simple methods for the 3' biotinylation of RNA.","citation":"RNA 2014 Mar;20(3):421-7","abstract":"Biotinylation of RNA allows its tight coupling to streptavidin and is thus useful for many types of experiments, e.g., pull-downs. Here we describe three simple techniques for biotinylating the 3' ends of RNA molecules generated by chemical or enzymatic synthesis. First, extension with either the Schizosaccharomyces pombe noncanonical poly(A) polymerase Cid1 or Escherichia coli poly(A) polymerase and N6-biotin-ATP is simple, efficient, and generally applicable independently of the 3'-end sequences of the RNA molecule to be labeled. However, depending on the enzyme and the reaction conditions, several or many biotinylated nucleotides are incorporated. Second, conditions are reported under which splint-dependent ligation by T4 DNA ligase can be used to join biotinylated and, presumably, other chemically modified DNA oligonucleotides to RNA 3' ends even if these are heterogeneous as is typical for products of enzymatic synthesis. Third, we describe the use of 29 DNA polymerase for a template-directed fill-in reaction that uses biotin-dUTP and, thanks to the enzyme's proofreading activity, can cope with more extended 3' heterogeneities.","doi":"10.1261/rna.042986.113","authors":"Moritz B, Wahle E","authors_abbrev":"Moritz B et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-01-23","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008577","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1934083","title":"F-actin contractile rings in protoplasts of the yeast Schizosaccharomyces.","citation":"Cell Biol Int Rep 1991 Jul;15(7):607-10","abstract":"By rhodamine-phalloidin fluorescence, distinct continuous F-actin rings were visualized in 18-20% of the protoplasts of Schizosaccharomyces pombe and S. japonicus var. versatilis, in addition to randomly distributed F-actin dots. Whereas the reversion of ring-lacking protoplasts coincided with the polarization of the dotted F-actin pattern, the ring-containing protoplasts became furrowed as the F-actin rings constricted. The furrowing was more conspicuous in S. japonicus var. versatilis than in S. pombe protoplasts and it was blocked when the reversion was inhibited by Novozyme 234 indicating that the cell wall formation is essential for the F-actin ring constriction.","authors":"Jochová J, Rupes I, Streiblová E","authors_abbrev":"Jochová J et al.","pubmed_publication_date":"Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008198","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8344877","title":"BU-4794F, a new beta-1,3-glucan synthase inhibitor.","citation":"J Antibiot (Tokyo) 1993 Jun;46(6):952-60","abstract":"New beta-1,3-glucan synthase inhibitor (BU-4794F) was isolated from the culture broth of Gilmaniella sp. FA4459. Structural studies indicated that it was a novel member of the papulacandin group of antibiotics.","authors":"Aoki M, Andoh T, Ueki T, Masuyoshi S, Sugawara K, Oki T","authors_abbrev":"Aoki M et al.","pubmed_publication_date":"Jun 1993","pubmed_entrez_date":"1993-06-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2016051","title":"The mechanism of fission yeast mating type interconversion: seal/replicate/cleave model of replication across the double-stranded break site at mat1.","citation":"Genetics 1991 Mar;127(3):489-96","abstract":"The interconversion of cell type in the fission yeast, Schizosaccharomyces pombe, is initiated by a double-stranded break (DSB) found at the mating type locus (mat1). A heritable site- and strand-specific DNA \"imprinting\" event at mat1 was recently hypothesized to be required to make the mat1 locus cleavable, and the DSB was suggested to be produced one generation before the actual switching event. It is known that only one cell among four granddaughters of a cell ever switches, and the sister of the recently switched cell switches efficiently in consecutive cell divisions. The feature of consecutive switching creates a major difficulty of having to replicate chromosomes possessing the DSB. The mat1 cis-acting leaky mutation, called smt-s, reduces the level of the DSB required for switching and is shown here to be a 27-bp deletion located 50 bp away from the cut site. Determination of the pattern and frequency of switching of the mutant allele by cell lineage studies has allowed us to conclude the following: (1) the chromosome with the DSB is sealed and replicated, then one of the specific chromatids is cleaved again to generate switching-competent cells in consecutive cell divisions and (2) the smt-s mutation affects DNA cleavage and not the hypothesized DNA imprinting step.","authors":"Klar AJ, Bonaduce MJ, Cafferkey R","authors_abbrev":"Klar AJ et al.","pubmed_publication_date":"Mar 1991","pubmed_entrez_date":"1991-03-01","publication_year":"1991","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7813446","title":"A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.","citation":"EMBO J 1994 Dec 15;13(24):6099-106","abstract":"Wee1 protein kinase regulates the length of G2 phase by carrying out the inhibitory tyrosyl phosphorylation of Cdc2-cyclin B kinase. Mutations were isolated that suppressed the G2 cell cycle arrest caused by overproduction of Wee1. One class of swo (suppressor of wee1 overproduction) mutation, exemplified by swo1-26, also caused a temperature sensitive lethal phenotype in a wee1+ background. The swo1+ gene encodes a member of the Hsp90 family of stress proteins. Swo1 is essential for viability at all temperatures. Swo1 coimmunoprecipitates with Wee1, showing that the two proteins interact. The swo1-26 mutant undergoes premature mitosis when grown at a semi-permissive temperature. These data strongly indicate that formation of active Wee1 tyrosine kinase requires interaction with Swo1, perhaps in a manner analogous to the previously demonstrated interaction between Hsp90 and v-src tyrosine kinase. These observations demonstrate a unexpected role for Hsp90 in cell cycle control.","authors":"Aligue R, Akhavan-Niak H, Russell P","authors_abbrev":"Aligue R et al.","pubmed_publication_date":"15 Dec 1994","pubmed_entrez_date":"1994-12-15","publication_year":"1994","canto_session_key":"acb154d034f85813","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-11-01 14:29:06","canto_approved_date":"2021-11-03 19:06:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-24 16:54:20","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC18B5.03","SPAC926.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-11-01"},{"uniquename":"PMID:16967902","title":"Regulation of MAL1+ gene expression encoding maltase in Schizosaccharomyces pombe by added inositol.","citation":"Indian J Biochem Biophys 2006 Jun;43(3):143-7","abstract":"In this study, the effects of inositol addition on maltase activity and expression of MAL1+ gene encoding maltase in Schizosaccharomyces pombe were investigated. The maximum specific maltase activity was observed, when the concentration of inositol reached 6.0 microg/ml in the synthetic medium containing 2.0% glucose. At 1.0 microg/ml inositol concentration, the maltase activity continuously decreased, as initial glucose concentration was higher than 0.1%. mRNA encoding maltase and phosphatidylinositol (PI) content were higher in the cells grown in the synthetic medium with 6.0 microg/ml of inositol and 2.0% glucose than those with 1.0 microg/ml of inositol. These results demonstrated that higher inositol concentration in the synthetic medium could derepress MAL1+ gene expression in S. pombe and PI might be involved in derepression of MAL1+ gene expression in S. pombe probably by PI-type signalling pathway.","authors":"Yao S, Chi Z, He S","authors_abbrev":"Yao S et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-09-14","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013961","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15197176","title":"The fission yeast heterochromatin protein Rik1 is required for telomere clustering during meiosis.","citation":"J Cell Biol 2004 Jun 21;165(6):759-65","abstract":"Telomeres share the ability to silence nearby transcription with heterochromatin, but the requirement of heterochromatin proteins for most telomere functions is unknown. The fission yeast Rik1 protein is required for heterochromatin formation at centromeres and the mating-type locus, as it recruits the Clr4 histone methyltransferase, whose modification of histone H3 triggers binding by Swi6, a conserved protein involved in spreading of heterochromatin. Here, we demonstrate that Rik1 and Clr4, but not Swi6, are required along with the telomere protein Taz1 for crucial chromosome movements during meiosis. However, Rik1 is dispensable for the protective roles of telomeres in preventing chromosome end-fusion. Thus, a Swi6-independent heterochromatin function distinct from that at centromeres and the mating-type locus operates at telomeres during sexual differentiation.","authors":"Tuzon CT, Borgstrom B, Weilguny D, Egel R, Cooper JP, Nielsen O","authors_abbrev":"Tuzon CT et al.","pubmed_publication_date":"21 Jun 2004","pubmed_entrez_date":"2004-06-16","publication_year":"2004","canto_session_key":"8e262e350ffaf1d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-09 16:35:23","canto_approved_date":"2022-09-26 19:22:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-23 21:07:22","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.02c","SPCC11E10.08","SPAC16A10.07c","SPBC428.08c","SPAC664.01c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-11-09"},{"uniquename":"PMID:38511077","title":"Generation and characterization of temperature-sensitive alleles of the glucanosyltransferase Gas1 in Schizosaccharomyces pombe.","citation":"MicroPubl Biol 2024;2024","abstract":"The  Schizosaccharomyces pombe  Gas family of β-1,3-glucanosyltransferases modify the cell wall by elongating β-1,3-glucan chains. While  gas1Δ  cells are inviable under standard laboratory growth conditions, they are viable in the presence of an osmotic stabilizer. Even under these conditions however,  gas1Δ  cells are slow-growing and display cell separation and morphology defects. Here, we isolated and characterized two  gas1  temperature-sensitive alleles. Our data support that Gas1 is the primary  S. pombe  β-1,3-glucanosyltransferase important for cell separation and cell viability and provide useful tools for further analysis of  S. pombe  cell wall formation.","doi":"10.17912/micropub.biology.001144","authors":"Howard IV, Tavafoghi B, Igarashi MG, Ren L, Willet AH, Gould KL","authors_abbrev":"Howard IV et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-03-21","publication_year":"2024","canto_session_key":"7ffcdbf6d700d337","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2024-04-04 17:43:18","canto_approved_date":"2024-05-14 20:55:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-04 10:10:44","canto_added_date":"2024-03-22 00:25:05","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":7,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.08","SPBC19G7.05c","SPAC19B12.02c","SPBC342.03","SPAC11E3.13c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2024-04-04"},{"uniquename":"PMID:25771684","title":"Structure of the WD40 domain of SCAP from fission yeast reveals the molecular basis for SREBP recognition.","citation":"Cell Res 2015 Apr;25(4):401-11","abstract":"The sterol regulatory element-binding protein (SREBP) and SREBP cleavage-activating protein (SCAP) are central players in the SREBP pathway, which control the cellular lipid homeostasis. SCAP binds to SREBP through their carboxyl (C) domains and escorts SREBP from the endoplasmic reticulum to the Golgi upon sterol depletion. A conserved pathway, with the homologues of SREBP and SCAP being Sre1 and Scp1, was identified in fission yeast Schizosaccharomyces pombe. Here we report the in vitro reconstitution of the complex between the C domains of Sre1 and Scp1 as well as the crystal structure of the WD40 domain of Scp1 at 2.1 Å resolution. The structure reveals an eight-bladed β-propeller that exhibits several distinctive features from a canonical WD40 repeat domain. Structural and biochemical characterization led to the identification of two Scp1 elements that are involved in Sre1 recognition, an Arg/Lys-enriched surface patch on the top face of the WD40 propeller and a 30-residue C-terminal tail. The structural and biochemical findings were corroborated by in vivo examinations. These studies serve as a framework for the mechanistic understanding and further functional characterization of the SREBP and SCAP proteins in fission yeast and higher organisms.","doi":"10.1038/cr.2015.32","authors":"Gong X, Li J, Shao W, Wu J, Qian H, Ren R, Espenshade P, Yan N","authors_abbrev":"Gong X et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-03-17","publication_year":"2015","canto_session_key":"729fd40714dad360","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_approved_date":"2015-07-29 14:37:21","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-20 19:22:28","canto_added_date":"2015-03-18 01:15:35","annotation_curators":[{"name":"Peter Espenshade","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.09","SPBC3B9.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-07-20","pdb_entries":[{"pdb_id":"4yhc","gene_chains":[{"gene_uniquename":"SPBC3B9.15c","chain":"A/B","position":"567-1054"}],"title":"Crystal structure of the WD40 domain of SCAP from fission yeast","entry_authors":"Gong X,Li JX,Wu JP,Yan CY,Yan N","entry_authors_abbrev":"Gong X et al.","reference_uniquename":"PMID:25771684","experimental_method":"X-ray","resolution":"2.05"}]},{"uniquename":"PMID:20096118","title":"Expression profiling of S. pombe acetyltransferase mutants identifies redundant pathways of gene regulation.","citation":"BMC Genomics 2010 Jan 22;11:59","abstract":"Histone acetyltransferase enzymes (HATs) are implicated in regulation of transcription. HATs from different families may overlap in target and substrate specificity.\nWe isolated the elp3+ gene encoding the histone acetyltransferase subunit of the Elongator complex in fission yeast and characterized the phenotype of an Deltaelp3 mutant. We examined genetic interactions between Deltaelp3 and two other HAT mutants, Deltamst2 and Deltagcn5 and used whole genome microarray analysis to analyze their effects on gene expression.\nComparison of phenotypes and expression profiles in single, double and triple mutants indicate that these HAT enzymes have overlapping functions. Consistent with this, overlapping specificity in histone H3 acetylation is observed. However, there is no evidence for overlap with another HAT enzyme, encoded by the essential mst1+ gene.","doi":"10.1186/1471-2164-11-59","authors":"Nugent RL, Johnsson A, Fleharty B, Gogol M, Xue-Franzén Y, Seidel C, Wright AP, Forsburg SL","authors_abbrev":"Nugent RL et al.","pubmed_publication_date":"22 Jan 2010","pubmed_entrez_date":"2010-01-26","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.05","SPAC17G8.13c","SPAC29A4.20"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU007673","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23447405","title":"Quantitative analysis of human ras localization and function in the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2013 Apr;30(4):145-56","abstract":"Ras signalling is central to fundamental and diverse cellular processes. In higher eukaryotes ras signalling is highly complex, involving multiple isoforms, regulatory proteins and effectors. As a consequence, the study of ras activity in mammalian systems presents a number of technical challenges. The model organism Schizosaccharomyces pombe has previously proved a key system for the study of human signalling components and provides an ideal model for the study of ras, as it contains just one ras protein (Ras1p), which is non-essential and controls a number of downstream processes. Here we present data demonstrating the quantitative analysis of three distinct Ras1-related signalling outputs, utilizing the three most abundant human ras isoforms, H-Ras, N-Ras and K-Ras4B, in Sz. pombe. Further, we have characterized the localization of these three human ras isoforms in Sz. pombe, utilizing quantitative image analysis techniques. These data indicate that all three human ras isoforms are functional in fission yeast, displaying differing localization patterns which correlate strongly with function in the regulation of pheromone response and cell shape. These data demonstrate that such yeast strains could provide powerful tools for the investigation of ras biology, and potentially in the development of cancer therapies.","doi":"10.1002/yea.2949","authors":"Bond M, Croft W, Tyson R, Bretschneider T, Davey J, Ladds G","authors_abbrev":"Bond M et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2013-03-01","publication_year":"2013","canto_session_key":"ae4c9307abe4ff57","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mike bond","canto_first_approved_date":"2018-10-15 12:28:48","canto_approved_date":"2020-12-03 15:23:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-03-21 19:08:09","canto_added_date":"2013-03-21 18:37:25","annotation_curators":[{"name":"Mike bond","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.06","SPAC17H9.09c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2018-10-15"},{"uniquename":"PMID:6090122","title":"Isolation of type I and II DNA topoisomerase mutants from fission yeast: single and double mutants show different phenotypes in cell growth and chromatin organization.","citation":"EMBO J 1984 Aug;3(8):1737-44","abstract":"We have isolated mutants defective in DNA topoisomerases and an endonuclease from the fission yeast Schizosaccharomyces pombe by screening individual extracts of mutagenized cells. Two type I topoisomerase mutants (top1) and three endonuclease mutants (end1) were all viable. The double mutant top1 end1 was also viable and, in its extract, Mg2+- and ATP- dependent type II activity could be detected. Three temperature-sensitive (ts-) mutants having heat-sensitive (hs-) type II enzymes were isolated, and the ts- marker cosegregated with the hs- type II activity. All the ts- mutations fell in one gene (top2) tightly linked to leul in chromosome II. The nuclear division of single top2 mutants was blocked at the restrictive temperature, but the formation of a septum was not inhibited so that the nucleus was cut across with the cell plate. In contrast, the double top1 top2 mutants were rapidly arrested at various stages of the cell cycle, showing a strikingly altered nuclear chromatin region. The type II topoisomerase may have an essential role in the compaction and/or segregation of chromosomes during the nuclear division but also complement the defect of the type I enzyme whose major function is the maintenance of chromatin organization throughout the cell cycle.","authors":"Uemura T, Yanagida M","authors_abbrev":"Uemura T et al.","pubmed_publication_date":"Aug 1984","pubmed_entrez_date":"1984-08-01","publication_year":"1984","canto_session_key":"b2369c57c9545f6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-04-06 09:39:13","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-03-01 15:17:52","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":43,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.03c","SPAC17C9.08","SPBC1703.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-03-01"},{"uniquename":"PMID:12228806","title":"The genetic complexity of chitin synthesis in fungi.","citation":"Curr Genet 2002 Sep;41(6):367-78","abstract":"Chitin synthesis is a process maintained across the fungal kingdom that, thanks to the power of genetic manipulation of yeast cells, is now beginning to be understood. Chitin synthesis is based on the regulation of distinct chitin synthase isoenzymes whose number ranges from one in Schizosaccharomyces pombe to seven in some filamentous fungi, such as Aspergillus fumigatus. This high diversity makes it difficult to find a unique model of regulation. However, the results available suggest common themes in regulation. The arrival of the genomic era, together with the development of fungal genetic technology should allow experimental approaches to this process.","authors":"Roncero C","authors_abbrev":"Roncero C","pubmed_publication_date":"Sep 2002","pubmed_entrez_date":"2002-09-14","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34005275","canto_session_key":"4e00681d74fea79f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-20 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11447128","title":"A novel meiosis-specific protein of fission yeast, Meu13p, promotes homologous pairing independently of homologous recombination.","citation":"EMBO J 2001 Jul 16;20(14):3871-81","abstract":"Meiotic homologous pairing is crucial to proper homologous recombination, which secures subsequent reductional chromosome segregation. We have identified a novel meiosis-specific protein of fission yeast Schizosaccharomyces pombe, Meu13p, to be a molecule that is required for proper homologous pairing and recombination. Rec12p (homologue of Saccharomyces cerevisiae Spo11p), which is essential for the initiation of meiotic recombination, is also shown for the first time to participate in the pairing process of S.pombe. Meu13p, however, contributes to pairing through a recombination-independent mechanism, as disruption of the meu13(+) gene reduces pairing whether the rec12(+) gene is deleted or not. We also demonstrate a dynamic nature of homologous pairing in living meiotic cells, which is markedly affected by meu13 deletion. Meu13p is not required for telomere clustering and the nuclear movement process, which are well known requirements for efficient pairing in S.pombe. Based on these results, together with the localization of Meu13p on meiotic chromatin, we propose that Meu13p directly promotes proper homologous pairing and recombination.","authors":"Nabeshima K, Kakihara Y, Hiraoka Y, Nojima H","authors_abbrev":"Nabeshima K et al.","pubmed_publication_date":"16 Jul 2001","pubmed_entrez_date":"2001-07-12","publication_year":"2001","canto_session_key":"cb84b6d6f237fb11","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-03-09 16:16:00","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-05-27 16:46:00","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1753.03c","SPAC17A5.11","SPAC222.15"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-05-27"},{"uniquename":"PMID:30530492","title":"Yeast and human P4-ATPases transport glycosphingolipids using conserved structural motifs.","citation":"J Biol Chem 2019 Feb 08;294(6):1794-1806","abstract":"Lipid transport is an essential process with manifest importance to human health and disease. Phospholipid flippases (P4-ATPases) transport lipids across the membrane bilayer and are involved in signal transduction, cell division, and vesicular transport. Mutations in flippase genes cause or contribute to a host of diseases, such as cholestasis, neurological deficits, immunological dysfunction, and metabolic disorders. Genome-wide association studies have shown that  ATP10A  and  ATP10D  variants are associated with an increased risk of diabetes, obesity, myocardial infarction, and atherosclerosis. Moreover,  ATP10D  SNPs are associated with elevated levels of glucosylceramide (GlcCer) in plasma from diverse European populations. Although sphingolipids strongly contribute to metabolic disease, little is known about how GlcCer is transported across cell membranes. Here, we identify a conserved clade of P4-ATPases from  Saccharomyces cerevisiae  (Dnf1, Dnf2),  Schizosaccharomyces pombe  (Dnf2), and  Homo sapiens  (ATP10A, ATP10D) that transport GlcCer bearing an  sn2  acyl-linked fluorescent tag. Further, we establish structural determinants necessary for recognition of this sphingolipid substrate. Using enzyme chimeras and site-directed mutagenesis, we observed that residues in transmembrane (TM) segments 1, 4, and 6 contribute to GlcCer selection, with a conserved glutamine in the center of TM4 playing an essential role. Our molecular observations help refine models for substrate translocation by P4-ATPases, clarify the relationship between these flippases and human disease, and have fundamental implications for membrane organization and sphingolipid homeostasis.","doi":"10.1074/jbc.RA118.005876","authors":"Roland BP, Naito T, Best JT, Arnaiz-Yépez C, Takatsu H, Yu RJ, Shin HW, Graham TR","authors_abbrev":"Roland BP et al.","pubmed_publication_date":"08 Feb 2019","pubmed_entrez_date":"2018-12-12","publication_year":"2019","canto_session_key":"c1d8ed0226576290","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-05-17 12:50:20","canto_approved_date":"2023-02-24 13:29:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-16 14:18:31","canto_added_date":"2018-12-13 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-05-17"},{"uniquename":"PMID:20850009","title":"Regulation of replication termination by Reb1 protein-mediated action at a distance.","citation":"Cell 2010 Sep 17;142(6):868-78","abstract":"DNA transactions driven by long-range protein-mediated inter- and intrachromosomal interactions have been reported to influence gene expression. Here, we report that site-specific replication termination in Schizosaccharomyces pombe is modulated by protein-mediated interactions between pairs of Ter sites located either on the same or on different chromosomes. The dimeric Reb1 protein catalyzes termination and mediates interaction between Ter sites. The Reb1-dependent interactions between two antiparallel Ter sites in cis caused looping out of the intervening DNA in vitro and enhancement of fork arrest in vivo. A Ter site on chromosome 2 interacted pairwise with two Ter sites located on chromosome 1 by chromosome kissing. Mutational inactivation of the major interacting Ter site on chromosome 1 significantly reduced fork arrest at the Ter site on chromosome 2, thereby revealing a cooperative mechanism of control of replication termination.","doi":"10.1016/j.cell.2010.08.013","authors":"Singh SK, Sabatinos S, Forsburg S, Bastia D","authors_abbrev":"Singh SK et al.","pubmed_publication_date":"17 Sep 2010","pubmed_entrez_date":"2010-09-21","publication_year":"2010","canto_session_key":"5d87587c1b704846","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-07-20 08:00:57","canto_session_submitted_date":"2012-07-19 19:07:19","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1198.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-07-19"},{"uniquename":"PMID:41974504","title":"Nuclear basket subunits Nup211 and Rsm1 influence RNA 3'-processing and transcription termination in fission yeast.","citation":"RNA 2026 Apr 13;","abstract":"The fission yeast phosphate acquisition (PHO) regulon is repressed under phosphate-replete conditions by upstream lncRNA-mediated transcriptional interference. Inositol-1-pyrophosphates control PHO gene expression via their action as agonists of precocious PHO lncRNA 3'-processing/termination. Inositol pyrophosphatase-inactivating asp1-STF mutations that increase inositol-1-pyrophosphates elicit derepression of the PHO genes and a severe growth defect in YES medium. Previous studies demonstrated suppression of inositol pyrophosphate toxicosis by loss-of-function and hypomorphic mutations in 11 of the 14 subunits of the fission yeast Cleavage and Polyadenylation Factor (CPF) complex. Here, we report the identification and characterization of mutations in the Nup211 and Rsm1 subunits of the nuclear basket of the nuclear pore complex that suppress inositol pyrophosphate toxicosis. We localize Nup211's activity in asp1-STF toxicosis to the C-terminal segment that forms a globular module appended to the dimeric Nup211 coiled-coil of the nuclear basket strut. A triple-alanine mutation of a conserved Nup211 1821RDD1823 peptide sufficed to suppress asp1-STF toxicosis. We find that: (i) induced overexpression of the Nup211 C-terminal segment is itself toxic to fission yeast, and that this toxicity was abolished by the RDD-AAA mutation; and (ii) Nup211 C-terminal truncation confers synthetic growth defects when combined with loss-of-function mutations in CPF subunits Ppn1, Swd22, and Ssu72. Our results implicate the Nup211 C-terminus as part of a protein-protein interface that abets 3'-processing/termination.","doi":"10.1261/rna.081007.126","authors":"Bednor L, Innokentev A, Sanchez AM, Sem A, Schwer B, Shuman S","authors_abbrev":"Bednor L et al.","pubmed_publication_date":"13 Apr 2026","pubmed_entrez_date":"2026-04-13","publication_year":"2026","canto_session_key":"72253744aee8333c","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-05-14 19:52:30","canto_added_date":"2026-04-14 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32269268","title":"Abo1 is required for the H3K9me2 to H3K9me3 transition in heterochromatin.","citation":"Sci Rep 2020 Apr 08;10(1):6055","abstract":"Heterochromatin regulation is critical for genomic stability. Different H3K9 methylation states have been discovered, with distinct roles in heterochromatin formation and silencing. However, how the transition from H3K9me2 to H3K9me3 is controlled is still unclear. Here, we investigate the role of the conserved bromodomain AAA-ATPase, Abo1, involved in maintaining global nucleosome organisation in fission yeast. We identified several key factors involved in heterochromatin silencing that interact genetically with Abo1: histone deacetylase Clr3, H3K9 methyltransferase Clr4, and HP1 homolog Swi6. Cells lacking Abo1 cultivated at 30 °C exhibit an imbalance of H3K9me2 and H3K9me3 in heterochromatin. In abo1∆ cells, the centromeric constitutive heterochromatin has increased H3K9me2 but decreased H3K9me3 levels compared to wild-type. In contrast, facultative heterochromatin regions exhibit reduced H3K9me2 and H3K9me3 levels in abo1∆. Genome-wide analysis showed that abo1∆ cells have silencing defects in both the centromeres and subtelomeres, but not in a subset of heterochromatin islands in our condition. Thus, our work uncovers a role of Abo1 in stabilising directly or indirectly Clr4 recruitment to allow the H3K9me2 to H3K9me3 transition in heterochromatin.","doi":"10.1038/s41598-020-63209-y","authors":"Dong W, Oya E, Zahedi Y, Prasad P, Svensson JP, Lennartsson A, Ekwall K, Durand-Dubief M","authors_abbrev":"Dong W et al.","pubmed_publication_date":"08 Apr 2020","pubmed_entrez_date":"2020-04-10","publication_year":"2020","canto_session_key":"c8ce525d900e703a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Karl Ekwall","canto_first_approved_date":"2021-02-24 13:45:32","canto_approved_date":"2024-02-15 12:42:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-05 13:22:25","canto_added_date":"2020-04-11 00:15:03","annotation_curators":[{"name":"Karl Ekwall","community_curator":true,"annotation_count":4,"orcid":"0000-0002-3029-4041","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":30,"orcid":"0000-0003-4148-4606","file_type":"interaction","file_name":"PMID_32269268_scored_interactions.tab2.txt"}],"genes":["SPAC664.01c","SPCC338.16","SPCC306.04c","SPBC800.02","SPAC11E3.05","SPBC800.03","SPBC17D11.04c","SPAC19G12.03","SPAC343.11c","SPAC57A7.09","SPBC16A3.08c","SPBC216.05","SPBC32F12.07c","SPAC688.06c","SPAC13A11.04c","SPAC6G9.16c","SPAC17A2.06c","SPAC18G6.02c","SPBC18H10.06c","SPAC31G5.19","SPAC24B11.06c","SPAC1B3.17","SPAC9.05","SPAC22F3.02","SPCC1259.07","SPCC1393.08","SPCC550.14","SPBC1198.11c","SPBC428.08c","SPBC16C6.10","SPAC4G8.13c"],"gene_count":31,"ltp_gene_count":4,"approved_date":"2021-02-24"},{"uniquename":"PMID:8972180","title":"Roles of Wee1 and Nim1 protein kinases in regulating the switch from mitotic division to sexual development in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1997 Jan;17(1):10-7","abstract":"In self-fertile strains of the fission yeast Schizosaccharomyces pombe, nitrogen starvation initiates a program of sexual development in which cells express mating pheromones and receptors, arrest cell cycle progression in G1, and conjugate. This process is dependent on Rum1, an inhibitor of the Cdc2-Cdc13 and Cdc2-Cig2 cyclin B kinases. The M-phase induction activity of Cdc2-Cdc13 is inhibited by Wee1 tyrosine kinase, which phosphorylates Cdc2 on tyrosine-15. We report here that Wee1 activity is also important for mating. This discovery arose from studies of Nim1, a kinase which promotes mitosis by inhibiting Wee1. Nim1 was previously thought to have an important role in promoting mitosis during nitrogen starvation, but our studies revealed that Nim1 protein drops to an undetectable level within 15 min of nitrogen depletion. In contrast, Wee1 remains abundant, and tyrosine-phosphorylated Cdc2 is detected for at least 4 h after resuspension of cells in nitrogen-free medium. This suggested that maintenance of Wee1 activity may be important during the early stages of nitrogen starvation, a proposal confirmed by the observation that mating efficiency is reduced ca. fivefold in wee1- cells. Transcriptional induction of genes encoding mating factors and receptors is also delayed in wee1- cells. The wee1- mating defect is suppressed by deletion of cig2+, which encodes a B-type cyclin that promotes the onset of S and inhibits conjugation. These findings indicate that Wee1 and Rum1 act jointly to inhibit Cdc2 and promote sexual development in nitrogen-starved cells.","authors":"Wu L, Russell P","authors_abbrev":"Wu L et al.","pubmed_publication_date":"Jan 1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAPB2B4.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:42223017","title":"Interplay between cohesin and TORC1 links chromosome segregation and gene expression to environmental changes.","citation":"Elife 2026 Jun 01;14","abstract":"Cohesin is a DNA tethering complex essential for chromosome structure and function. In fission yeast, defects in the cohesin loader Mis4 result in chromosome segregation defects and dysregulated expression of genes near chromosome ends. A genetic screen for suppressors of the thermosensitive growth defect of  mis4-G1487D  identified several hypomorphic mutants of the Target of Rapamycin Complex 1 (TORC1), a conserved kinase that integrates cellular signals to regulate growth and metabolism through substrate-specific phosphorylation. Here, we demonstrate that the TORC1 pathway modulates cohesin functions in chromosome segregation and gene expression. In the context of compromised cohesin loading, the incidence of chromosome segregation defects was modulated by the growth medium in a TORC1-dependent manner. Pharmacological or genetic downregulation of TORC1 activity restored cohesin binding to its chromosomal sites and improved mitotic chromosome segregation. Notably, reduced TORC1 activity also increased cohesin binding and chromosome transmission fidelity in wild-type cells. These results suggest that environmental cues influence chromosome stability via TORC1. Biochemically, TORC1 co-purified with cohesin and reduced TORC1 activity correlated with decreased phosphorylation of specific residues on Mis4 and cohesin. Mutations in cohesin that mimic the non-phosphorylated state mirrored the effects of TORC1 downregulation, showing that TORC1 is part of the network that controls cohesin phosphorylation to modulate its functions. Finally, we show that the functional interaction between TORC1 and Mis4 extends to the regulation of stress-responsive genes. Our findings reveal a TORC1-cohesin link that may facilitate cellular adaptation to environmental changes. Given that TORC1 inhibitors and calorie restriction extend lifespan in diverse species, this connection raises the intriguing possibility that cohesin-mediated changes in chromosome structure contribute to these effects.","doi":"10.7554/eLife.108275","authors":"Besson D, Vaur S, Vazquez S, Tournier S, Gachet Y, Birot A, Claverol S, Marston AL, Damdimopoulos A, Ekwall K, Javerzat JP","authors_abbrev":"Besson D et al.","pubmed_publication_date":"01 Jun 2026","pubmed_entrez_date":"2026-06-01","publication_year":"2026","canto_session_key":"84f482e50b13a29c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-01 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16407242","title":"An evolutionarily conserved function of proliferating cell nuclear antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA damage.","citation":"J Biol Chem 2006 Feb 17;281(7):3753-6","abstract":"The DNA replication licensing factor Cdt1 is degraded by the ubiquitin-proteasome pathway during S phase of the cell cycle, to ensure one round of DNA replication during each cell division and in response to DNA damage to halt DNA replication. Constitutive expression of Cdt1 causes DNA re-replication and is associated with the development of a subset of human non-small cell-lung carcinomas. In mammalian cells, DNA damage-induced Cdt1 degradation is catalyzed by the Cul4-Ddb1-Roc1 E3 ubiquitin ligase. We report here that overexpression of the proliferating cell nuclear antigen (PCNA) inhibitory domain from the CDK inhibitors p21 and p57, but not the CDK-cyclin inhibitory domain, blocked Cdt1 degradation in cultured mammalian cells after UV irradiation. In vivo soluble Cdt1 and PCNA co-elute by gel filtration and associate with each other physically. Silencing PCNA in cultured mammalian cells or repression of pcn1 expression in fission yeast blocked Cdt1 degradation in response to DNA damage. Unexpectedly, deletion of Ddb1 in fission yeast cells also accumulated Cdt1 in the absence of DNA damage. We suggest that the Cul4-Ddb1 ligase evolved to ubiquitinate Cdt1 during normal cell growth as well as in response to DNA damage and a separate E3 ligase, possibly SCF(Skp2), evolved to either share or take over the function of Cdt1 ubiquitination during normal cell growth and that PCNA is involved in mediating Cdt1 degradation by the Cul4-Ddb1 ligase in response to DNA damage.","authors":"Hu J, Xiong Y","authors_abbrev":"Hu J et al.","pubmed_publication_date":"17 Feb 2006","pubmed_entrez_date":"2006-01-13","publication_year":"2006","canto_session_key":"b03ae5190e2fe612","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-03-31 15:45:34","canto_approved_date":"2025-09-04 10:11:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-31 15:45:29","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.10c","SPBC16D10.09","SPBC428.18","SPAC29B12.03"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2016-03-31"},{"uniquename":"PMID:22879382","title":"Signaling pathways for fission yeast sexual differentiation at a glance.","citation":"J Cell Sci 2012 Jun 15;125(Pt 12):2789-93","abstract":"","doi":"10.1242/jcs.094771","authors":"Otsubo Y, Yamamoto M","authors_abbrev":"Otsubo Y et al.","pubmed_publication_date":"15 Jun 2012","pubmed_entrez_date":"2012-08-11","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30181192","title":"Protection from Disulfide Stress by Inhibition of Pap1 Nuclear Export in  Schizosaccharomyces pombe .","citation":"Genetics 2018 Nov;210(3):857-868","abstract":"Appropriate subcellular localization of regulatory factors is critical for cellular function. Pap1, a nucleocytoplasmic shuttling transcription factor of  Schizosaccharomyces pombe , is redox regulated for localization and antistress function. In this study, we find that overproduction of a peptide conjugate containing the nuclear export signal of Oxs1, a conserved eukaryotic protein that, along with Pap1, regulates certain diamide responsive genes, can retain Pap1 in the nucleus before stress by competing for nuclear export. The nuclear retention of Pap1 upregulates several drug resistance genes to prime the cells for higher tolerance to disulfide stress. Overproduction of Oxs1 also upregulates these same genes, not by competing for export but by binding directly to the drug resistance gene promoters for Pap1-mediated activation. Of medical relevance is that this may suggest a gene therapy approach of using nuclear export signal conjugates to suppress the nuclear export of biomolecules.","doi":"10.1534/genetics.118.301527","authors":"Chen Y, Zhang Y, Dong Z, Ow DW","authors_abbrev":"Chen Y et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-09-06","publication_year":"2018","canto_session_key":"e3c1e5b363acdcce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yan Chen","canto_first_approved_date":"2020-12-15 15:56:04","canto_approved_date":"2026-02-04 07:43:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-12 00:05:25","canto_added_date":"2018-09-07 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yan Chen","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC663.08c","SPAC1783.07c","SPBC609.04","SPBC29A10.12","SPAC3C7.14c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-12-15"},{"uniquename":"PMID:10333521","title":"A new inducible protein expression system in fission yeast based on the glucose-repressed inv1 promoter.","citation":"Gene 1999 May 17;232(1):53-8","abstract":"Studies of the fission yeast Schizosaccharomyces pombe have made major contributions towards understanding cell-cycle control and many other important aspects of cell biology. A series of pREP expression vectors that utilize the thiamine-repressible nmt1 promoter are used routinely to manipulate the expression of genes in fission yeast. A shortcoming of the nmt1 promoter is that it is very slowly induced following removal of thiamine from the growth medium, requiring approx. 16h for full induction. Invertase, an enzyme responsible for sucrose metabolism, is regulated transcriptionally by glucose derepression in S. pombe. Using the inv1 promoter, we have developed the pINV1 set of inducible protein expression vectors. A shift from glucose to sucrose-based culture medium leads to a very rapid induction of the inv1 promoter. Genes that are regulated by the inv1 promoter are fully induced within 1h of the shift to sucrose-based medium. The pINV1 vectors utilize a simple induction protocol and enable studies in fission yeast requiring tight and rapid regulation of protein synthesis.","authors":"Iacovoni JS, Russell P, Gaits F","authors_abbrev":"Iacovoni JS et al.","pubmed_publication_date":"17 May 1999","pubmed_entrez_date":"1999-05-20","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012281","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ617355","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.26"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23203989","title":"The BioGRID interaction database: 2013 update.","citation":"Nucleic Acids Res 2013 Jan;41(Database issue):D816-23","abstract":"The Biological General Repository for Interaction Datasets (BioGRID: http//thebiogrid.org) is an open access archive of genetic and protein interactions that are curated from the primary biomedical literature for all major model organism species. As of September 2012, BioGRID houses more than 500 000 manually annotated interactions from more than 30 model organisms. BioGRID maintains complete curation coverage of the literature for the budding yeast Saccharomyces cerevisiae, the fission yeast Schizosaccharomyces pombe and the model plant Arabidopsis thaliana. A number of themed curation projects in areas of biomedical importance are also supported. BioGRID has established collaborations and/or shares data records for the annotation of interactions and phenotypes with most major model organism databases, including Saccharomyces Genome Database, PomBase, WormBase, FlyBase and The Arabidopsis Information Resource. BioGRID also actively engages with the text-mining community to benchmark and deploy automated tools to expedite curation workflows. BioGRID data are freely accessible through both a user-defined interactive interface and in batch downloads in a wide variety of formats, including PSI-MI2.5 and tab-delimited files. BioGRID records can also be interrogated and analyzed with a series of new bioinformatics tools, which include a post-translational modification viewer, a graphical viewer, a REST service and a Cytoscape plugin.","doi":"10.1093/nar/gks1158","authors":"Chatr-Aryamontri A, Breitkreutz BJ, Heinicke S, Boucher L, Winter A, Stark C, Nixon J, Ramage L, Kolas N, O'Donnell L, Reguly T, Breitkreutz A, Sellam A, Chen D, Chang C, Rust J, Livstone M, Oughtred R, Dolinski K, Tyers M","authors_abbrev":"Chatr-Aryamontri A et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2012-12-04","publication_year":"2013","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32546830","title":"A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6.","citation":"Sci Rep 2020 Jun 16;10(1):9694","abstract":"The SMC (Structural Maintenance of Chromosomes) complexes are composed of SMC dimers, kleisin and kleisin-interacting (HAWK or KITE) subunits. Mutual interactions of these subunits constitute the basal architecture of the SMC complexes. In addition, binding of ATP molecules to the SMC subunits and their hydrolysis drive dynamics of these complexes. Here, we developed new systems to follow the interactions between SMC5/6 subunits and the relative stability of the complex. First, we show that the N-terminal domain of the Nse4 kleisin molecule binds to the SMC6 neck and bridges it to the SMC5 head. Second, binding of the Nse1 and Nse3 KITE proteins to the Nse4 linker increased stability of the ATP-free SMC5/6 complex. In contrast, binding of ATP to SMC5/6 containing KITE subunits significantly decreased its stability. Elongation of the Nse4 linker partially suppressed instability of the ATP-bound complex, suggesting that the binding of the KITE proteins to the Nse4 linker constrains its limited size. Our data suggest that the KITE proteins may shape the Nse4 linker to fit the ATP-free complex optimally and to facilitate opening of the complex upon ATP binding. This mechanism suggests an important role of the KITE subunits in the dynamics of the SMC5/6 complexes.","doi":"10.1038/s41598-020-66647-w","authors":"Vondrova L, Kolesar P, Adamus M, Nociar M, Oliver AW, Palecek JJ","authors_abbrev":"Vondrova L et al.","pubmed_publication_date":"16 Jun 2020","pubmed_entrez_date":"2020-06-18","publication_year":"2020","canto_session_key":"fa8f1b63230268b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jan Palecek","canto_first_approved_date":"2020-07-28 17:13:56","canto_approved_date":"2024-03-29 12:54:24","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-07-02 13:14:34","canto_added_date":"2020-06-30 06:42:19","annotation_curators":[{"name":"Jan Palecek","community_curator":true,"annotation_count":12,"orcid":"0000-0002-6223-5169","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.02c","SPCC550.05","SPBC20F10.04c","SPCC5E4.06","SPAC11E3.08c","SPCC645.04","SPBC651.10"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2020-07-28"},{"uniquename":"PMID:25303777","title":"The Pif1 family helicase Pfh1 facilitates telomere replication and has an RPA-dependent role during telomere lengthening.","citation":"DNA Repair (Amst) 2014 Dec;24:80-86","abstract":"Pif1 family helicases are evolutionary conserved 5'-3' DNA helicases. Pfh1, the sole Schizosaccharomyces pombe Pif1 family DNA helicase, is essential for maintenance of both nuclear and mitochondrial DNAs. Here we show that its nuclear functions include roles in telomere replication and telomerase action. Pfh1 promoted semi-conservative replication through telomeric DNA, as replication forks moved more slowly through telomeres when Pfh1 levels were reduced. Unlike other organisms, S. pombe cells overexpressing Pfh1 displayed markedly longer telomeres. Because this lengthening occurred in the absence of homologous recombination but not in a replication protein A mutant (rad11-D223Y) that has defects in telomerase function, it is probably telomerase-mediated. The effects of Pfh1 on telomere replication and telomere length are likely direct as Pfh1 exhibited high telomere binding in cells expressing endogenous levels of Pfh1. These findings argue that Pfh1 is a positive regulator of telomere length and telomere replication.","doi":"10.1016/j.dnarep.2014.09.008","authors":"McDonald KR, Sabouri N, Webb CJ, Zakian VA","authors_abbrev":"McDonald KR et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-10-12","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-10-13 00:15:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC887.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPC12132","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12893961","title":"The fission yeast RPA51 is a functional homolog of the budding yeast A49 subunit of RNA polymerase I and required for maximizing transcription of ribosomal DNA.","citation":"Genes Genet Syst 2003 Jun;78(3):199-209","abstract":"Saccharomyces cerevisiae A49 and mouse PAF53 are subunits specific to RNA polymerase I (Pol I) in eukaryotes. It has been known that Pol I without A49 or PAF53 maintains non-specific transcription activities but a molecular role(s) of A49 (and PAF53) remains totally unknown. We studied the fission yeast gene encoding a protein of 415 amino acids exhibiting 30% and 19% identities to A49 and PAF53, respectively. We designate the corresponding protein RPA51 and gene encoding it rpa51+ since the gene encodes a Pol I subunit and an apparent molecular mass of the protein is 51 kDa. rpa51+ is required for cell growth at lower but not at higher temperatures and is able to complement S. cerevisiae rpa49Delta mutation, indicating that RPA51 is a functionally-conserved subunit of Pol I between the budding yeast and the fission yeast. Deletion analysis of rpa51+ shows that only two-thirds of the C-terminal region are required for the function. Transcripts analysis in vivo and in vitro shows that RPA51 plays a general role for maximizing transcription of rDNA whereas it is dispensable for non-specific transcription. We also found that RPA51 associates significantly with Pol I in the stationary phase, suggesting that Pol I inactivation in the stationary phase of yeast does not result from the RPA51 dissociation.","authors":"Nakagawa K, Hisatake K, Imazawa Y, Ishiguro A, Matsumoto M, Pape L, Ishihama A, Nogi Y","authors_abbrev":"Nakagawa K et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-08-02","publication_year":"2003","canto_session_key":"6cdebcc5bb8f2240","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-26 17:55:39","canto_approved_date":"2020-11-26 17:57:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-26 17:55:30","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F3.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-11-26"},{"uniquename":"EMBL:AU008489","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1874411","title":"Isolation and characterization of Schizosaccharomyces pombe mutants affected in mitotic recombination.","citation":"Genetics 1991 Jul;128(3):495-504","abstract":"A haploid Schizosaccharomyces pombe strain carrying a heteroallelic duplication of the ade6 gene was used to isolate mitotic recombination-deficient mutants. Recombination between the different copies of the ade6 gene can lead to Ade+ segregants. These are observed as growing papillae when colonies of a suitable size are replicated onto selective medium. We isolated mutants which show an altered papillation phenotype. With two exceptions, they exhibit a decrease in the frequency of mitotic recombination between the heteroalleles of the duplication. The two other mutants display a hyper-recombination phenotype. The 12 mutations were allocated to at least nine distinct loci by recombination tests. Of the eight rec mutants analyzed further, six were also affected in mitotic intergenic recombination in the intervals cen2-mat or cen3-arg 1. No effect on mitotic intragenic recombination was observed. These data suggest that mitotic gene conversion and crossing over can be separated mutationally. Meiotic recombination occurs at the wild-type frequency in all mutants investigated.","authors":"Gysler-Junker A, Bodi Z, Kohli J","authors_abbrev":"Gysler-Junker A et al.","pubmed_publication_date":"Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_session_key":"bef3394fa69e94a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-04 16:22:48","canto_approved_date":"2022-10-13 07:12:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-04 16:22:26","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-04"},{"uniquename":"PMID:27627185","title":"Crystal structure of eIF2B and insights into eIF2-eIF2B interactions.","citation":"FEBS J 2017 Mar;284(6):868-874","abstract":"Eukaryotic translation initiation factor 2B (eIF2B), a heterodecameric complex of two sets of the α, β, γ, δ, and ε subunits, is the guanine nucleotide exchange factor (GEF) specific for eIF2, a heterotrimeric G protein consisting of the α, β, and γ subunits. The eIF2 protein binds GTP on the γ subunits and delivers an initiator methionyl-tRNA (Met-tRNA i  Met  ) to the ribosome. The GEF activity of eIF2B is inhibited by stress-induced phosphorylation of Ser51 in the α subunit of eIF2, which leads to lower amounts of active eIF2 and a limited quantity of Met-tRNA i  M  et  for the ribosome, resulting in global repression of translation. However, the structural mechanism of the GEF activity inhibition remained enigmatic, and therefore the three-dimensional structure of the entire eIF2B molecule had been awaited. Recently, we determined the crystal structure of Schizosaccharomyces pombe eIF2B. In this Structural Snapshot, we present the structural features of eIF2B and the mechanism underlying the GEF activity inhibition by the phosphorylation of eIF2α, elucidated from structure-based in vitro analyses.","doi":"10.1111/febs.13896","authors":"Kashiwagi K, Ito T, Yokoyama S","authors_abbrev":"Kashiwagi K et al.","pubmed_publication_date":"Mar 2017","pubmed_entrez_date":"2016-09-15","publication_year":"2017","canto_session_key":"4172bbc99aeb070b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-25 15:14:08","canto_approved_date":"2023-11-13 16:15:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-25 15:13:55","canto_added_date":"2016-09-16 00:15:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.09c","SPCC11E10.07c","SPAC8C9.15c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-07-25"},{"uniquename":"PMID:12504018","title":"A role for chromatin remodeling in transcriptional termination by RNA polymerase II.","citation":"Mol Cell 2002 Dec;10(6):1441-52","abstract":"Chromatin remodeling can facilitate the recruitment of RNA polymerase II (Pol II) to targeted promoters, as well as enhancing the level of transcription. Here, we describe a further key role for chromatin remodeling in transcriptional termination. Using a genetic screen in S. pombe, we identified the CHD-Mi2 class chromatin remodeling ATPase, Hrp1, as a termination factor. In S. cerevisiae, we show that transcriptional termination and chromatin structure at the 3' ends of three genes all depend on the activity of the Hrp1 homolog, Chd1p, either alone or redundantly with the ISWI ATPases, Isw1p, and Isw2p. We suggest that chromatin remodeling of termination regions is a necessary prelude to efficient Pol II termination.","authors":"Alén C, Kent NA, Jones HS, O'Sullivan J, Aranda A, Proudfoot NJ","authors_abbrev":"Alén C et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2002-12-31","publication_year":"2002","canto_session_key":"6c7215acda2236c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-12 14:26:51","canto_approved_date":"2024-06-12 14:26:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-12 14:26:04","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-06-12"},{"uniquename":"PMID:27268234","title":"Both H4K20 mono-methylation and H3K56 acetylation mark transcription-dependent histone turnover in fission yeast.","citation":"Biochem Biophys Res Commun 2016 Aug 05;476(4):515-521","abstract":"Nucleosome dynamics facilitated by histone turnover is required for transcription as well as DNA replication and repair. Histone turnover is often associated with various histone modifications such as H3K56 acetylation (H3K56Ac), H3K36 methylation (H3K36me), and H4K20 methylation (H4K20me). In order to correlate histone modifications and transcription-dependent histone turnover, we performed genome wide analyses for euchromatic regions in G2/M-arrested fission yeast. The results show that transcription-dependent histone turnover at 5' promoter and 3' termination regions is directly correlated with the occurrence of H3K56Ac and H4K20 mono-methylation (H4K20me1) in actively transcribed genes. Furthermore, the increase of H3K56Ac and H4K20me1 and antisense RNA production was observed in the absence of the histone H3K36 methyltransferase Set2 and histone deacetylase complex (HDAC) that are involved in the suppression of histone turnover within the coding regions. These results together indicate that H4K20me1 as well as H3K56Ac are bona fide marks for transcription-dependent histone turnover in fission yeast.","doi":"10.1016/j.bbrc.2016.05.155","authors":"Yang H, Kwon CS, Choi Y, Lee D","authors_abbrev":"Yang H et al.","pubmed_publication_date":"05 Aug 2016","pubmed_entrez_date":"2016-06-09","publication_year":"2016","canto_session_key":"6e2ab1dbcb345a0f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Daeyoup Lee","canto_first_approved_date":"2024-05-24 16:42:54","canto_approved_date":"2024-05-24 16:42:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-05-12 06:22:48","canto_added_date":"2016-06-10 00:15:13","annotation_curators":[{"name":"Daeyoup Lee","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":8,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC342.06c","SPAC24H6.05","SPAC23H4.12","SPAC29B12.02c","SPCC4B3.12","SPBC8D2.04"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2024-05-24"},{"uniquename":"PMID:37550452","title":"The structure of the NuA4-Tip60 complex reveals the mechanism and importance of long-range chromatin modification.","citation":"Nat Struct Mol Biol 2023 Sep;30(9):1337-1345","abstract":"Histone acetylation regulates most DNA transactions and is dynamically controlled by highly conserved enzymes. The only essential histone acetyltransferase (HAT) in yeast, Esa1, is part of the 1-MDa NuA4 complex, which plays pivotal roles in both transcription and DNA-damage repair. NuA4 has the unique capacity to acetylate histone targets located several nucleosomes away from its recruitment site. Neither the molecular mechanism of this activity nor its physiological importance are known. Here we report the structure of the Pichia pastoris NuA4 complex, with its core resolved at 3.4-Å resolution. Three subunits, Epl1, Eaf1 and Swc4, intertwine to form a stable platform that coordinates all other modules. The HAT module is firmly anchored into the core while retaining the ability to stretch out over a long distance. We provide structural, biochemical and genetic evidence that an unfolded linker region of the Epl1 subunit is critical for this long-range activity. Specifically, shortening the Epl1 linker causes severe growth defects and reduced H4 acetylation levels over broad chromatin regions in fission yeast. Our work lays the foundations for a mechanistic understanding of NuA4's regulatory role and elucidates how its essential long-range activity is attained.","doi":"10.1038/s41594-023-01056-x","authors":"Fréchard A, Faux C, Hexnerova R, Crucifix C, Papai G, Smirnova E, McKeon C, Ping FLY, Helmlinger D, Schultz P, Ben-Shem A","authors_abbrev":"Fréchard A et al.","pubmed_publication_date":"Sep 2023","pubmed_entrez_date":"2023-08-07","publication_year":"2023","canto_session_key":"df17d2db3d735794","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dom Helmlinger","canto_first_approved_date":"2023-09-04 03:52:04","canto_approved_date":"2024-07-04 14:36:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-08-31 15:38:13","canto_added_date":"2023-08-09 00:15:04","annotation_curators":[{"name":"Dom Helmlinger","community_curator":true,"annotation_count":8,"orcid":"0000-0003-1501-0423","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC830.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-09-04"},{"uniquename":"PMID:11030618","title":"swi1 and swi3 perform imprinting, pausing, and termination of DNA replication in S. pombe.","citation":"Cell 2000 Sep 15;102(6):745-51","abstract":"The developmental program of cell-type switching of S. pombe requires a strand-specific imprinting event at the mating-type locus (mat1). Imprinting occurs only when mat1 is replicated in a specific direction and requires several trans-acting factors. This work shows (1) that the factors swi1p and swi3p act by pausing the replication fork at the imprinting site; and (2) that swi1p and swi3p are involved in termination at the mat1-proximal polar-terminator of replication (RTS1). A genetic screen to identify termination factors identified an allele that separated pausing/imprinting and termination functions of swip. These results suggest that swi1p and swi3p promote imprinting in novel ways both by pausing replication at mat1 and by terminating replication at RTS1.","authors":"Dalgaard JZ, Klar AJ","authors_abbrev":"Dalgaard JZ et al.","pubmed_publication_date":"15 Sep 2000","pubmed_entrez_date":"2000-10-13","publication_year":"2000","canto_session_key":"99bc68402289c0b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-06-18 15:11:07","canto_approved_date":"2024-06-26 16:34:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-17 08:41:04","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":17,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.06c","SPBC30D10.04","SPBC1703.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2024-06-18"},{"uniquename":"PMID:21056831","title":"Nuclear membrane: nuclear envelope PORosity in fission yeast meiosis.","citation":"Curr Biol 2010 Nov 09;20(21):R923-5","abstract":"The fission yeast Schizosaccharomyces pombe undergoes closed mitosis but 'virtual nuclear envelope breakdown' at anaphase of meiosis II, in which the nuclear envelope is structurally closed but functionally open.","doi":"10.1016/j.cub.2010.10.005","authors":"Sazer S","authors_abbrev":"Sazer S","pubmed_publication_date":"09 Nov 2010","pubmed_entrez_date":"2010-11-09","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11082048","title":"Identification of an alpha-tubulin mutant of fission yeast from gamma-tubulin-interacting protein screening: genetic evidence for alpha-/gamma-tubulin interaction.","citation":"J Cell Sci 2000 Dec;113 Pt 24:4557-62","abstract":"gamma-Tubulin has been determined to be a central element of microtubule nucleation and, thus, indispensable for cellular organization of the microtubule. Utilizing the fact that human gamma-tubulin can function in the fission yeast Schizosaccharomyces pombe, we have generated a unique mutant screening procedure which can specifically select mutants of genes encoding gamma-tubulin-interacting proteins. One of the isolated mutants, cs76, turned out to carry a mutation in the alpha 1-tubulin gene (nda2(+)). This result suggests a direct interaction between the alpha- and gamma-tubulins. We located the mutation site in the nda2 gene and characterized the mutant phenotype. Our results demonstrate the importance of the alpha-/gamma-tubulin interaction in microtubule nucleation and should complement previous knowledge.","authors":"Takeoka A, Shimizu M, Horio T","authors_abbrev":"Takeoka A et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-18","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPBC16A3.15c","SPBC800.05c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10196100","title":"Methods of assaying Bcl-2 and Bax family proteins in yeast.","citation":"Methods 1999 Apr;17(4):292-304","abstract":"Bcl-2 family proteins play an evolutionarily conserved role in regulating the life and death of the cell. Certain proapoptotic members of the Bcl-2 family, Bax and Bak, have intrinsic cytotoxic activities in that they not only induce or sensitize mammalian cells to undergo apoptosis but also display a lethal phenotype when ectopically expressed in two yeast species Saccharomyces cerevisiae and Schizosaccharomyces pombe. Furthermore, the antiapoptotic Bcl-2 and Bcl-XL proteins can protect yeast against Bax-mediated lethality, suggesting that the death-regulatory functions of these Bcl-2 family proteins are well preserved in yeast. These observations provide the opportunity to study the function of Bcl-2 family proteins in genetically tractable yeast and to apply classical yeast genetics and functional cloning approaches to the dissection of programmed cell death pathway regulated by Bcl-2 family proteins. We describe here methods used in our laboratory to express and to study the functions of Bcl-2 family proteins in both the budding yeast S. cerevisiae and the fission yeast S. pombe.","authors":"Xu Q, Jürgensmeier JM, Reed JC","authors_abbrev":"Xu Q et al.","pubmed_publication_date":"Apr 1999","pubmed_entrez_date":"1999-04-10","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16857169","title":"The role of Schizosaccharomyces pombe DNA repair enzymes Apn1p and Uve1p in the base excision repair of apurinic/apyrimidinic sites.","citation":"Biochem Biophys Res Commun 2006 Sep 08;347(4):889-94","abstract":"In Schizosaccharomyces pombe the repair of apurinic/apyrimidinic (AP) sites is mainly initiated by AP lyase activity of DNA glycosylase Nth1p. In contrast, the major AP endonuclease Apn2p functions by removing 3'-alpha,beta-unsaturated aldehyde ends induced by Nth1p, rather than by incising the AP sites. S. pombe possesses other minor AP endonuclease activities derived from Apn1p and Uve1p. In this study, we investigated the function of these two enzymes in base excision repair (BER) for methyl methanesulfonate (MMS) damage using the nth1 and apn2 mutants. Deletion of apn1 or uve1 from nth1Delta cells did not affect sensitivity to MMS. Exogenous expression of Apn1p failed to suppress the MMS sensitivity of nth1Delta cells. Although Apn1p and Uve1p incised the oligonucleotide containing an AP site analogue, these enzymes could not initiate repair of the AP sites in vivo. Despite this, expression of Apn1p partially restored the MMS sensitivity of apn2Delta cells, indicating that the enzyme functions as a 3'-phosphodiesterase to remove 3'-blocked ends. Localization of Apn1p in the nucleus and cytoplasm hints at an additional function of the enzyme other than nuclear DNA repair. Heterologous expression of Saccharomyces cerevisiae homologue of Apn1p completely restored the MMS resistance of the nth1Delta and apn2Delta cells. This result confirms a difference in the major pathway for processing the AP site between S. pombe and S. cerevisiae cells.","authors":"Tanihigashi H, Yamada A, Igawa E, Ikeda S","authors_abbrev":"Tanihigashi H et al.","pubmed_publication_date":"08 Sep 2006","pubmed_entrez_date":"2006-07-22","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3D6.10","SPAC30D11.07","SPCC622.17","SPBC19C7.09c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:8373587","title":"A method for the preparation and storage of frozen, competent Schizosaccharomyces pombe spheroplasts.","citation":"Biotechniques 1993 Aug;15(2):238","abstract":"","authors":"Zhao Y, Hopkins KM, Lieberman HB","authors_abbrev":"Zhao Y et al.","pubmed_publication_date":"Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18615848","title":"Role of heterochromatin in suppressing subtelomeric recombination in fission yeast.","citation":"Yeast 2008 Aug;25(8):537-48","abstract":"Telomere length is regulated by a complex interplay of several factors, including telomerase, telomere-binding proteins, DNA replication machinery and recombination. In yeast, DNA polymerase alpha is required for de novo synthesis of telomeres from broken ends of DNA, and it also suppresses the elongation of normal telomeric repeats. Heterochromatin proteins Clr1-Clr4 and Swi6 and DNA polalpha organize heterochromatin structure at mating type, centromere, rDNA and telomere regions that are refractory to transcription and recombination in Schizosaccharomyces pombe. Here, we have addressed the role of heterochromatin structure in regulating the integrity and organization of telomeric regions. Here, we show that subtelomeric duplication and rearrangements occur in polalpha and heterochromatin mutants and find that some of the putative duplication events are dependent on the Rad50 pathway. Thus, our study shows a role of heterochromatin in maintaining the integrity of the subtelomeric regions by suppressing their recombination in Sz. pombe.","doi":"10.1002/yea.1603","authors":"Bisht KK, Arora S, Ahmed S, Singh J","authors_abbrev":"Bisht KK et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-07-11","publication_year":"2008","canto_session_key":"71e68c1b5b6dc976","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-05-14 15:24:36","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-13 11:21:27","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPAC3H5.06c","SPBC543.03c","SPAC16A10.07c","SPBC2D10.17","SPAC1B3.17","SPCC18B5.11c","SPBC800.03","SPAC664.01c","SPBC428.08c","SPAC644.14c"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2015-02-13"},{"uniquename":"PMID:17846589","title":"Schizosaccharomyces pombe nup97, which Genetically Interacts with mex67, is essential for growth and involved in mRNA export.","citation":"J Microbiol 2007 Aug;45(4):344-9","abstract":"We have isolated previously three synthetic lethal mutants in Schizosaccharomyces pombe, which genetically interact with mex67, in order to identify the genes involved in mRNA export. A novel nup97 gene was isolated by complementation of the growth defect in one of the synthetic lethal mutants, SLMex3. The nup97 gene contains one intron and encodes an 851 amino-acid protein that is similar to nucleoporins, Npp106p in S. pombe and Nic96p in Saccharomyces cerevisiae. The nup97 gene is essential for vegetative growth, and nup97 null mutant harboring pREP41X-Nup97 showed poly(A)+ RNA export defect when expression of nup97 is repressed in the presence of thiamine. These results suggest that nup97 is involved in mRNA export from the nucleus to cytoplasm.","authors":"Cho HJ, Hwang DK, Jung SI, Yoon JH","authors_abbrev":"Cho HJ et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-09-12","publication_year":"2007","canto_session_key":"1ec1ca37cece68ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-02 17:29:36","canto_approved_date":"2022-12-13 10:26:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-01 20:47:51","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.14","SPCC1620.11","SPBC1921.03c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2015-06-02"},{"uniquename":"PMID:893556","title":"Fusion and erosion of cell walls during confugation in the fussion yeast (Schizosaccharomyces pombe).","citation":"J Cell Sci 1977 Jun;25:139-55","abstract":"Conjugation in Schizosaccharomyces pombe was studied by transmission electron microscopy. Mural and nuclear events were scored from induction, the initial event, to meiosis I, the start of sporulation. These morphogenic markers were separately identifiable as flocculation, copulation, conjugation-tube formation, cross-wall formation, cross-wall erosion, conjugation-tube expansion, cytoplasmic fusion, de-differentiation of site of union, nuclear migration and karyogamy. The following were identified as new structural elements: sex hairs, which presumably mediate hydrogen bonding between cells during flocculation; crimp at the site of union; dark patch, which presumably serves as a leak-proof seal at the time of cross-wall erosion; suture, an electron-dense seam formed by the union of a copulant pair; and small electron-dense particles close to the site of wall erosion. No special structures on the cell wall could be identified as indicative of specific sites for potential copulatory activity. The discontinuity of the 2 cell walls at the site of union became so de-differentiated after fusion and erosion that it was no longer possible to pinpoint the site of union.","authors":"Calleja GB, Yoo BY, Johnson BF","authors_abbrev":"Calleja GB et al.","pubmed_publication_date":"Jun 1977","pubmed_entrez_date":"1977-06-01","publication_year":"1977","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28954859","title":"A node organization in the actomyosin contractile ring generates tension and aids stability.","citation":"Mol Biol Cell 2017 Nov 07;28(23):3286-3297","abstract":"During cytokinesis, a contractile actomyosin ring constricts and divides the cell in two. How the ring marshals actomyosin forces to generate tension is not settled. Recently, a superresolution microscopy study of the fission yeast ring revealed that myosins and formins that nucleate actin filaments colocalize in plasma membrane-anchored complexes called nodes in the constricting ring. The nodes move bidirectionally around the ring. Here we construct and analyze a coarse-grained mathematical model of the fission yeast ring to explore essential consequences of the recently discovered ring ultrastructure. The model reproduces experimentally measured values of ring tension, explains why nodes move bidirectionally, and shows that tension is generated by myosin pulling on barbed-end-anchored actin filaments in a stochastic sliding-filament mechanism. This mechanism is not based on an ordered sarcomeric organization. We show that the ring is vulnerable to intrinsic contractile instabilities, and protection from these instabilities and organizational homeostasis require both component turnover and anchoring of components to the plasma membrane.","doi":"10.1091/mbc.E17-06-0386","authors":"Thiyagarajan S, Wang S, O'Shaughnessy B","authors_abbrev":"Thiyagarajan S et al.","pubmed_publication_date":"07 Nov 2017","pubmed_entrez_date":"2017-09-29","publication_year":"2017","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2017-09-30 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22433840","title":"Mcm10 plays an essential role in origin DNA unwinding after loading of the CMG components.","citation":"EMBO J 2012 May 02;31(9):2182-94","abstract":"The CMG complex composed of Mcm2-7, Cdc45 and GINS is postulated to be the eukaryotic replicative DNA helicase, whose activation requires sequential recruitment of replication proteins onto Mcm2-7. Current models suggest that Mcm10 is involved in assembly of the CMG complex, and in tethering of DNA polymerase α at replication forks. Here, we report that Mcm10 is required for origin DNA unwinding after association of the CMG components with replication origins in fission yeast. A combination of promoter shut-off and the auxin-inducible protein degradation (off-aid) system efficiently depleted cellular Mcm10 to <0.5% of the wild-type level. Depletion of Mcm10 did not affect origin loading of Mcm2-7, Cdc45 or GINS, but impaired recruitment of RPA and DNA polymerases. Mutations in a conserved zinc finger of Mcm10 abolished RPA loading after recruitment of Mcm10. These results show that Mcm10, together with the CMG components, plays a novel essential role in origin DNA unwinding through its zinc-finger function.","doi":"10.1038/emboj.2012.68","authors":"Kanke M, Kodama Y, Takahashi TS, Nakagawa T, Masukata H","authors_abbrev":"Kanke M et al.","pubmed_publication_date":"02 May 2012","pubmed_entrez_date":"2012-03-22","publication_year":"2012","canto_session_key":"9d672c9083882357","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC725.13c","SPCC16A11.17","SPAC17D4.02","SPBC211.04c","SPAC23C4.18c","SPAC227.16c","SPAC6B12.11","SPBC25H2.13c","SPBC4.04c","SPBP23A10.09","SPBP4H10.21c","SPBC1347.10","SPBP8B7.14c"],"gene_count":13,"ltp_gene_count":13},{"uniquename":"PMID:15572668","title":"C-terminal anchoring of mid1p to membranes stabilizes cytokinetic ring position in early mitosis in fission yeast.","citation":"Mol Cell Biol 2004 Dec;24(24):10621-35","abstract":"mid1p is a key factor for the central positioning of the cytokinetic ring in Schizosaccharomyces pombe. In interphase and early mitosis, mid1p forms a medial cortical band overlying the nucleus, which may represent a landmark for cytokinetic ring assembly. It compacts before anaphase into a tight ring with other cytokinetic ring components. We show here that mid1p binds to the medial cortex by at least two independent means. First, mid1p C-terminus association with the cortex requires a putative amphipathic helix adjacent to mid1p nuclear localization sequence (NLS), which is predicted to insert directly into the lipid bilayer. This association is stabilized by the polybasic NLS. mid1p mutated within the helix and the NLS forms abnormal filaments in early mitosis that are not properly anchored to the medial cortex. Misplaced rings assemble in late mitosis, indicating that mid1p C-terminus binding to membranes stabilizes cytokinetic ring position. Second, the N terminus of mid1p has the ability to associate faintly with the medial cortex and is sufficient to form tight rings. In addition, we show that mid1p oligomerizes. We propose that membrane-bound oligomers of mid1p assemble recruitment \"platforms\" for cytokinetic ring components at the medial cortex and stabilize the ring position during its compaction.","authors":"Celton-Morizur S, Bordes N, Fraisier V, Tran PT, Paoletti A","authors_abbrev":"Celton-Morizur S et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-12-02","publication_year":"2004","canto_session_key":"f64bdfbbde0df34c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-02 09:00:29","canto_approved_date":"2026-02-14 08:53:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-18 18:35:56","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":38,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPAC1F5.04c","SPCC645.05c","SPCC4B3.15"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2024-05-02"},{"uniquename":"PMID:27007548","title":"Selected Schizosaccharomyces pombe Strains Have Characteristics That Are Beneficial for Winemaking.","citation":"PLoS One 2016;11(3):e0151102","abstract":"At present, wine is generally produced using Saccharomyces yeast followed by Oenococus bacteria to complete malolactic fermentation. This method has some unsolved problems, such as the management of highly acidic musts and the production of potentially toxic products including biogenic amines and ethyl carbamate. Here we explore the potential of the fission yeast Schizosaccharomyces pombe to solve these problems. We characterise an extensive worldwide collection of S. pombe strains according to classic biochemical parameters of oenological interest. We identify three genetically different S. pombe strains that appear suitable for winemaking. These strains compare favourably to standard Saccharomyces cerevisiae winemaking strains, in that they perform effective malic acid deacidification and significantly reduce levels of biogenic amines and ethyl carbamate precursors without the need for any secondary bacterial malolactic fermentation. These findings indicate that the use of certain S. pombe strains could be advantageous for winemaking in regions where malic acid is problematic, and these strains also show superior performance with respect to food safety.","doi":"10.1371/journal.pone.0151102","authors":"Benito Á, Jeffares D, Palomero F, Calderón F, Bai FY, Bähler J, Benito S","authors_abbrev":"Benito Á et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-03-24","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000092","title":"Representation for the biosynthesis from or via a chemical as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the biosynthesis of a chemical entity from or via an other chemical entity as biological processes. The underlying equivalence axiom templates are \"GO:0009058 and 'has output' some T and 'has input' some F\" (biosynthesis from) and \"GO:0009058 and 'has output' some T and 'has intermediate' some I\" (biosynthesis via), where T,F, and I are chemical entities (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19748355","title":"F-box-directed CRL complex assembly and regulation by the CSN and CAND1.","citation":"Mol Cell 2009 Sep 11;35(5):586-97","abstract":"The COP9 signalosome (CSN) is thought to maintain the stability of cullin-RING ubiquitin ligases (CRL) by limiting the autocatalytic destruction of substrate adapters such as F box proteins (FBPs). CAND1, a protein associated with unneddylated CUL1, was proposed to assist in this role in an as yet unclear fashion. We found that only a subset of Schizosaccharomyces pombe FBPs, which feature a critical F box proline that promotes their interaction with CUL1, required CSN for stability. Unlike the CRL3 adaptor Btb3p, none of the CSN-sensitive FBPs were affected by deletion of ubp12. Contrary to current models, CAND1 does not control adaptor stability but maintains the cellular balance of CRL1 complexes by preventing rare FBPs from being outcompeted for binding to CUL1 by more ample adapters. These findings were integrated into a refined model of CRL control in which substrate availability toggles CRLs between independent CSN and CAND1 cycles.","doi":"10.1016/j.molcel.2009.07.024","authors":"Schmidt MW, McQuary PR, Wee S, Hofmann K, Wolf DA","authors_abbrev":"Schmidt MW et al.","pubmed_publication_date":"11 Sep 2009","pubmed_entrez_date":"2009-09-15","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC338.16","SPBC3H7.06c","SPBC1271.01c","SPAC57A10.05c","SPAC17G6.17","SPBC56F2.01","SPCC1827.08c","SPBC409.05","SPBC1703.06","SPAC1687.13c","SPAC17G6.12"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:15060174","title":"Swm1/Apc13 is an evolutionarily conserved subunit of the anaphase-promoting complex stabilizing the association of Cdc16 and Cdc27.","citation":"Mol Cell Biol 2004 Apr;24(8):3562-76","abstract":"The anaphase-promoting complex (APC/C) is a large ubiquitin-protein ligase which controls progression through anaphase by triggering the degradation of cell cycle regulators such as securin and B-type cyclins. The APC/C is an unusually complex ligase containing at least 10 different, evolutionarily conserved components. In contrast to APC/C's role in cell cycle regulation little is known about the functions of individual subunits and how they might interact with each other. Here, we have analyzed Swm1/Apc13, a small subunit recently identified in the budding yeast complex. Database searches revealed proteins related to Swm1/Apc13 in various organisms including humans. Both the human and the fission yeast homologues are associated with APC/C subunits, and they complement the phenotype of an SWM1 deletion mutant of budding yeast. Swm1/Apc13 promotes the stable association with the APC/C of the essential subunits Cdc16 and Cdc27. Accordingly, Swm1/Apc13 is required for ubiquitin ligase activity in vitro and for the timely execution of APC/C-dependent cell cycle events in vivo.","authors":"Schwickart M, Havlis J, Habermann B, Bogdanova A, Camasses A, Oelschlaegel T, Shevchenko A, Zachariae W","authors_abbrev":"Schwickart M et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-04-03","publication_year":"2004","canto_session_key":"3d41296f63009c80","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-07-16 14:13:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-07-16 14:13:26","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":27,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.01c","SPBC1A4.01","SPAC6F12.14","SPAC343.03","SPBP23A10.04","SPAC6F12.15c","SPBC28E12.01c","SPAC23C11.12","SPAC959.09c","SPAC27D7.05c","SPBC106.09","SPAC19G12.01c","SPBC83.04"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2015-07-16"},{"uniquename":"PMID:39910760","title":"Novel TORC1 inhibitor Ecl1 is regulated by phosphorylation in fission yeast.","citation":"Aging Cell 2025 Feb 05;:e14450","abstract":"Extender of chronological lifespan 1 (Ecl1) inhibits target of rapamycin complex 1 (TORC1) and is necessary for appropriate cellular responses to various stressors, such as starvation, in fission yeast. However, little is known about the effect of posttranslational modifications on Ecl1 regulation. Thus, we investigated the phosphorylation levels of Ecl1 extracted from yeast under conditions of sulfur or metal starvation. Mass spectrometry analysis revealed that Ecl1 was phosphorylated at Thr7, and the level was decreased by starvation. The phosphorylation-mimetic mutation of Thr7 significantly reduced the effects of Ecl1-induced cellular responses to starvation, suggesting that Ecl1 function was suppressed by Thr7 phosphorylation. By contrast, regardless of starvation exposure, TORC1 was significantly suppressed, even when Thr7 phosphorylation-mimetic Ecl1 was overexpressed. This indicated that Ecl1 suppressed TORC1 regardless of Thr7 phosphorylation. We newly identified that Ecl1 physically interacted with TORC1 subunit RAPTOR (Mip1). Based on these evidences, we propose that, Ecl1 has dual functional modes: quantity-dependent TORC1 inhibition and Thr7 phosphorylation-dependent control of cellular function.","doi":"10.1111/acel.14450","authors":"Ohtsuka H, Kawai S, Ito Y, Kato Y, Shimasaki T, Imada K, Otsubo Y, Yamashita A, Mishiro-Sato E, Kuwata K, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"05 Feb 2025","pubmed_entrez_date":"2025-02-06","publication_year":"2025","canto_session_key":"8c6d16a0b6951d6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2025-02-13 14:41:41","canto_approved_date":"2025-04-15 12:49:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-02-13 01:50:51","canto_added_date":"2025-02-07 00:25:05","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":9,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21B10.05c","SPBC216.07c","SPBC8E4.12c","SPCC4G3.08","SPAC57A7.11","SPBP35G2.16c","SPCC70.12c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2025-02-13"},{"uniquename":"PMID:23671279","title":"Receptor for activated C-kinase (RACK1) homolog Cpc2 facilitates the general amino acid control response through Gcn2 kinase in fission yeast.","citation":"J Biol Chem 2013 Jun 28;288(26):19260-8","abstract":"General amino acid control (GAAC) is crucial for sensing and adaptation to nutrient availability. Amino acid starvation activates protein kinase Gcn2, which plays a central role in the GAAC response by phosphorylating the α-subunit of eukaryotic initiation factor 2 (eIF2α), leading to the translational switch to stimulate selective expression of stress-responsive genes. We report here that in fission yeast Schizosaccharomyces pombe, Cpc2, a homolog of mammalian receptor for activated C-kinase (RACK1), is important for the GAAC response. Deletion of S. pombe cpc2 impairs the amino acid starvation-induced phosphorylation of eIF2α and the expression of amino acid biosynthesis genes, thereby rendering cells severely sensitive to amino acid limitation. Unlike the Saccharomyces cerevisiae Cpc2 ortholog, which normally suppresses the GAAC response, our findings suggest that S. pombe Cpc2 promotes the GAAC response. We also found that S. pombe Cpc2 is required for starvation-induced Gcn2 autophosphorylation, which is essential for Gcn2 function. These results indicate that S. pombe Cpc2 facilitates the GAAC response through the regulation of Gcn2 activation and provide a novel insight for the regulatory function of RACK1 on Gcn2-mediated GAAC response.","doi":"10.1074/jbc.M112.445270","authors":"Tarumoto Y, Kanoh J, Ishikawa F","authors_abbrev":"Tarumoto Y et al.","pubmed_publication_date":"28 Jun 2013","pubmed_entrez_date":"2013-05-15","publication_year":"2013","canto_session_key":"a9ee2fb1cb19f385","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yusuke Tarumoto","canto_first_approved_date":"2017-01-29 14:12:28","canto_approved_date":"2025-09-03 18:27:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-03 08:32:54","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":44,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Yusuke Tarumoto","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.09c","SPBC36B7.09","SPAC56E4.03","SPCC364.07","SPAC222.07c","SPAC1002.09c","SPAC227.18","SPBC3E7.16c","SPAC10F6.13c","SPAC4G9.10","SPBC19F5.04","SPBC16G5.14c","SPBC418.01c","SPAC6B12.15"],"gene_count":14,"ltp_gene_count":4,"approved_date":"2017-01-29"},{"uniquename":"PMID:24211211","title":"The small GTPase Rab5 homologue Ypt5 regulates cell morphology, sexual development, ion-stress response and vacuolar formation in fission yeast.","citation":"Biochem Biophys Res Commun 2013 Nov 29;441(4):867-72","abstract":"Inner-membrane transport is critical to cell function. Rab family GTPases play an important role in vesicle transport. In mammalian cells, Rab5 is reported to be involved in the regulation of endosome formation, phagocytosis and chromosome alignment. Here, we examined the role of the fission yeast Rab5 homologue Ypt5 using a point mutant allele. Mutant cells displayed abnormal cell morphology, mating, sporulation, endocytosis, vacuole fusion and responses to ion stress. Our data strongly suggest that fission yeast Rab5 is involved in the regulation of various types of cellular functions.","doi":"10.1016/j.bbrc.2013.10.158","authors":"Tsukamoto Y, Katayama C, Shinohara M, Shinohara A, Maekawa S, Miyamoto M","authors_abbrev":"Tsukamoto Y et al.","pubmed_publication_date":"29 Nov 2013","pubmed_entrez_date":"2013-11-12","publication_year":"2013","canto_session_key":"91724e5b296210af","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30154212","title":"Nutritional cell cycle reprogramming reveals that inhibition of Cdk1 is required for proper MBF-dependent transcription.","citation":"J Cell Sci 2018 Sep 20;131(18)","abstract":"In nature, cells and in particular unicellular microorganisms are exposed to a variety of nutritional environments. Fission yeast cells cultured in nitrogen-rich media grow fast, divide with a large size and show a short G1 and a long G2. However, when cultured in nitrogen-poor media, they exhibit reduced growth rate and cell size and a long G1 and a short G2. In this study, we compared the phenotypes of cells lacking the highly conserved cyclin-dependent kinase (Cdk) inhibitor Rum1 and the anaphase-promoting complex/cyclosome (APC/C) activator Ste9 in nitrogen-rich and nitrogen-poor media. Rum1 and Ste9 are dispensable for cell division in nitrogen-rich medium. However, in nitrogen-poor medium they are essential for generating a proper wave of MluI cell-cycle box binding factor (MBF)-dependent transcription at the end of G1, which is crucial for promoting a successful S phase. Mutants lacking Rum1 and Ste9 showed premature entry into S phase and a reduced wave of MBF-dependent transcription, leading to replication stress, DNA damage and G2 cell cycle arrest. This work demonstrates how reprogramming the cell cycle by changing the nutritional environment may reveal new roles for cell cycle regulators.","doi":"10.1242/jcs.218743","authors":"Rubio A, García-Blanco N, Vázquez-Bolado A, Belén Suárez M, Moreno S","authors_abbrev":"Rubio A et al.","pubmed_publication_date":"20 Sep 2018","pubmed_entrez_date":"2018-08-30","publication_year":"2018","canto_session_key":"709a7d61657ab430","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-08-31 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC144.13c","SPBC16H5.07c","SPCC18B5.11c","SPAC29B12.03","SPBC32F12.09","SPBC11B10.09","SPCC1259.13","SPBC216.05","SPBC16A3.07c"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:26525038","title":"Casein kinase 1γ acts as a molecular switch for cell polarization through phosphorylation of the polarity factor Tea1 in fission yeast.","citation":"Genes Cells 2015 Dec;20(12):1046-58","abstract":"Fission yeast undergoes growth polarity transition from monopolar to bipolar during G2 phase, designated NETO (New End Take Off). It is known that NETO onset involves two prerequisites, the completion of DNA replication and attainment of a certain cell size. However, the molecular mechanism remains unexplored. Here, we show that casein kinase 1γ, Cki3 is a critical determinant of NETO onset. Not only did cki3∆ cells undergo NETO during G1- or S-phase, but they also displayed premature NETO under unperturbed conditions with a smaller cell size, leading to cell integrity defects. Cki3 interacted with the polarity factor Tea1, of which phosphorylation was dependent on Cki3 kinase activity. GFP nanotrap of Tea1 by Cki3 led to Tea1 hyperphosphorylation with monopolar growth, whereas the same entrapment by kinase-dead Cki3 resulted in converse bipolar growth. Intriguingly, the Tea1 interactor Tea4 was dissociated from Tea1 by Cki3 entrapment. Mass spectrometry identified four phosphoserine residues within Tea1 that were hypophosphorylated in cki3∆ cells. Phosphomimetic Tea1 mutants showed compromised binding to Tea4 and NETO defects, indicating that these serine residues are critical for protein-protein interaction and NETO onset. Our findings provide significant insight into the mechanism by which cell polarization is regulated in a spatiotemporal manner.","doi":"10.1111/gtc.12309","authors":"Koyano T, Barnouin K, Snijders AP, Kume K, Hirata D, Toda T","authors_abbrev":"Koyano T et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-11-04","publication_year":"2015","canto_session_key":"1d23a09d00d999d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2017-01-31 18:23:16","canto_approved_date":"2025-12-20 10:07:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-29 01:38:29","canto_added_date":"2015-11-05 01:19:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":39,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Takashi Toda","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.06","SPAC1805.05","SPBC1706.01","SPBC776.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-01-31"},{"uniquename":"PMID:30086160","title":"A role for the transcription factor Mca1 in activating the meiosis-specific copper transporter Mfc1.","citation":"PLoS One 2018;13(8):e0201861","abstract":"When reproduction in fungi takes place by sexual means, meiosis enables the formation of haploid spores from diploid precursor cells. Copper is required for completion of meiosis in Schizosaccharomyces pombe. During the meiotic program, genes encoding copper transporters exhibit distinct temporal expression profiles. In the case of the major facilitator copper transporter 1 (Mfc1), its maximal expression is induced during middle-phase meiosis and requires the presence of the Zn6Cys2 binuclear cluster-type transcription factor Mca1. In this study, we further characterize the mechanism by which Mca1 affects the copper-starvation-induced expression of mfc1+. Using a chromatin immunoprecipitation (ChIP) approach, results showed that a functional Mca1-TAP occupies the mfc1+ promoter irrespective of whether this gene is transcriptionally active. Under conditions of copper starvation, results showed that the presence of Mca1 promotes RNA polymerase II (Pol II) occupancy along the mfc1+ transcribed region. In contrast, Pol II did not significantly occupy the mfc1+ locus in meiotic cells that were incubated in the presence of copper. Further analysis by ChIP assays revealed that binding of Pol II to chromatin at the chromosomal locus of mfc1+ is exclusively detected during meiosis and absent in cells proliferating in mitosis. Protein function analysis of a series of internal mutants compared to the full-length Mca1 identified a minimal form of Mca1 consisting of its DNA-binding domain (residues 1 to 150) fused to the amino acids 299 to 600. This shorter form is sufficient to enhance Pol II occupancy at the mfc1+ locus under low copper conditions. Taken together, these results revealed novel characteristics of Mca1 and identified an internal region of Mca1 that is required to promote Pol II-dependent mfc1+ transcription during meiosis.","doi":"10.1371/journal.pone.0201861","authors":"Beaudoin J, Ioannoni R, Normant V, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-08-08","publication_year":"2018","canto_session_key":"d9b6b322c8e283f6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-08-09 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26832414","title":"Condensin Promotes Position Effects within Tandem DNA Repeats via the RITS Complex.","citation":"Cell Rep 2016 Feb 09;14(5):1018-1024","abstract":"Tandem repetitive DNA is highly abundant in eukaryotic genomes and contributes to transcription control and genome stability. However, how the individual sequences within tandem repeats behave remains largely unknown. Here we develop a collection of fission yeast strains with a reporter gene inserted at different units in a tandem repeat array. We show that, contrary to what is usually assumed, transcriptional silencing and replication timing among the individual repeats differ significantly. RNAi-mediated H3K9 methylation is essential for the silencing position effect. A short hairpin RNA of ura4(+) induces silencing in trans within the tandem array in a position-dependent manner. Importantly, the position effect depends on the condensin subunit, cut3(+). Cut3 promotes the position effect via interaction with the RNA-induced transcriptional silencing (RITS) complex. This study reveals variations in silencing within tandem DNA repeats and provides mechanistic insights into how DNA repeats at the individual level are regulated.","doi":"10.1016/j.celrep.2016.01.006","authors":"He H, Zhang S, Wang D, Hochwagen A, Li F","authors_abbrev":"He H et al.","pubmed_publication_date":"09 Feb 2016","pubmed_entrez_date":"2016-02-03","publication_year":"2016","canto_session_key":"30e8708205f74a74","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-25 13:00:49","canto_approved_date":"2024-03-25 13:00:49","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-14 14:32:58","canto_added_date":"2016-02-04 01:15:13","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":7,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.17","SPAC18G6.02c","SPBC146.03c","SPCC613.12c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2024-03-25"},{"uniquename":"PMID:8001123","title":"A novel epigenetic effect can alter centromere function in fission yeast.","citation":"Cell 1994 Dec 02;79(5):865-74","abstract":"A novel epigenetic mechanism that can affect minichromosome centromere function in vivo has been identified in S. pombe. This epigenetic system can result in the conversion of a nonfunctional centromere to a functional one without changes in the content, structural arrangement, or chemical modification state of the minichromosomal DNA. The conversion from a centromere-inactive to an active state, which is evident with minichromosomes carrying abbreviated centromeric DNA constructions, occurs with a relatively high frequency during mitotic cell divisions and readily provides an in vivo assay for proper centromere formation. The centromere-targeted epigenetic system supports a model for centromere function that involves specific de novo folding of centromeric components into a higher order chromatin structure.","authors":"Steiner NC, Clarke L","authors_abbrev":"Steiner NC et al.","pubmed_publication_date":"02 Dec 1994","pubmed_entrez_date":"1994-12-02","publication_year":"1994","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17542643","title":"Bottleneck genes and community structure in the cell cycle network of S. pombe.","citation":"PLoS Comput Biol 2007 Jun;3(6):e103","abstract":"The identification of cell cycle-related genes is still a difficult task, even for organisms with relatively few genes such as the fission yeast. Several gene expression studies have been published on S. pombe showing similarities but also discrepancies in their results. We introduce a network in which the weight of each link is a function of the phase difference between the expression peaks of two genes. The analysis of the stability of the clustering through the computation of an entropy parameter reveals a structure made of four clusters, the first one corresponding to a robustly connected M-G1 component, the second to genes in the S phase, and the third and fourth to two G2 components. They are separated by bottleneck structures that appear to correspond to cell cycle checkpoints. We identify a number of genes that are located on these bottlenecks. They represent a novel group of cell cycle regulatory genes. They all show interesting functions, and they are supposed to be involved in the regulation of the transition from one phase to the next. We therefore present a comparison of the available studies on the fission yeast cell cycle and a general statistical bioinformatics methodology to find bottlenecks and gene community structures based on recent developments in network theory.","authors":"Caretta-Cartozo C, De Los Rios P, Piazza F, Liò P","authors_abbrev":"Caretta-Cartozo C et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-06-05","publication_year":"2007","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23516382","title":"Alternative splicing and subfunctionalization generates functional diversity in fungal proteomes.","citation":"PLoS Genet 2013;9(3):e1003376","abstract":"Alternative splicing is commonly used by the Metazoa to generate more than one protein from a gene. However, such diversification of the proteome by alternative splicing is much rarer in fungi. We describe here an ancient fungal alternative splicing event in which these two proteins are generated from a single alternatively spliced ancestral SKI7/HBS1 gene retained in many species in both the Ascomycota and Basidiomycota. While the ability to express two proteins from a single SKI7/HBS1 gene is conserved in many fungi, the exact mechanism by which they achieve this varies. The alternative splicing was lost in Saccharomyces cerevisiae following the whole-genome duplication event as these two genes subfunctionalized into the present functionally distinct HBS1 and SKI7 genes. When expressed in yeast, the single gene from Lachancea kluyveri generates two functionally distinct proteins. Expression of one of these proteins complements hbs1, but not ski7 mutations, while the other protein complements ski7, but not hbs1. This is the first known case of subfunctionalization by loss of alternative splicing in yeast. By coincidence, the ancestral alternatively spliced gene was also duplicated in Schizosaccharomyces pombe with subsequent subfunctionalization and loss of splicing. Similar subfunctionalization by loss of alternative splicing in fungi also explains the presence of two PTC7 genes in the budding yeast Tetrapisispora blattae, suggesting that this is a common mechanism to preserve duplicate alternatively spliced genes.","doi":"10.1371/journal.pgen.1003376","authors":"Marshall AN, Montealegre MC, Jiménez-López C, Lorenz MC, van Hoof A","authors_abbrev":"Marshall AN et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-03-22","publication_year":"2013","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27935167","title":"CK2 phospho-independent assembly of the Tel2-associated stress-signaling complexes in Schizosaccharomyces pombe.","citation":"Genes Cells 2017 Jan;22(1):59-70","abstract":"An evolutionarily conserved protein Tel2 regulates a variety of stress signals. In mammals, TEL2 associates with TTI1 and TTI2 to form the Triple T (TTT: TEL2-TTI1-TTI2) complex as well as with all the phosphatidylinositol 3-kinase-like kinases (PIKKs) and the R2TP (Ruvbl1-Ruvbl2-Tah1-Pih1 in budding yeast)/prefoldin-like complex that associates with HSP90. The phosphorylation of TEL2 by casein kinase 2 (CK2) enables direct binding of PIHD1 (mammalian Pih1) to TEL2 and is important for the stability and the functions of PIKKs. However, the regulatory mechanisms of Tel2 in fission yeast Schizosaccharomyces pombe remain largely unknown. Here, we report that S. pombe Tel2 is phosphorylated by CK2 at Ser490 and Thr493. Tel2 forms the TTT complex with Tti1 and Tti2 and also associates with PIKKs, Rvb2, and Hsp90 in vivo; however, the phosphorylation of Tel2 affects neither the stability of the Tel2-associated proteins nor their association with Tel2. Thus, Tel2 stably associates with its binding partners irrespective of its phosphorylation. Furthermore, the Tel2 phosphorylation by CK2 is not required for the various stress responses to which PIKKs are pivotal. Our results suggest that the Tel2-containing protein complexes are conserved among eukaryotes, but the molecular regulation of their formation has been altered during evolution.","doi":"10.1111/gtc.12454","authors":"Inoue H, Sugimoto S, Takeshita Y, Takeuchi M, Hatanaka M, Nagao K, Hayashi T, Kokubu A, Yanagida M, Kanoh J","authors_abbrev":"Inoue H et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2016-12-10","publication_year":"2017","canto_session_key":"528ea1bed9e365fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junko Kanoh","canto_first_approved_date":"2019-12-12 17:28:49","canto_approved_date":"2019-12-12 17:28:49","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-11-30 07:42:58","canto_added_date":"2016-12-11 01:15:11","annotation_curators":[{"name":"Junko Kanoh","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC83.08","SPAC23C11.11","SPCC622.13c","SPAC1F5.11c","SPBC1604.17c","SPAC458.03","SPAC1851.03","SPBC216.07c","SPAC926.04c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2019-12-12"},{"uniquename":"PMID:34907076","title":"Reactivation of transposable elements following hybridization in fission yeast.","citation":"Genome Res 2022 Feb;32(2):324-336","abstract":"Hybridization is thought to reactivate transposable elements (TEs) that were efficiently suppressed in the genomes of the parental hosts. Here, we provide evidence for this \"genomic shock hypothesis\" in the fission yeast  Schizosaccharomyces pombe  In this species, two divergent lineages ( Sp  and  Sk ) have experienced recent, likely human-induced, hybridization. We used long-read sequencing data to assemble genomes of 37 samples derived from 31  S. pombe  strains spanning a wide range of ancestral admixture proportions. A comprehensive TE inventory revealed exclusive presence of long terminal repeat (LTR) retrotransposons. Sequence analysis of active full-length elements, as well as solo LTRs, revealed a complex history of homologous recombination. Population genetic analyses of syntenic sequences placed insertion of many solo LTRs before the split of the  Sp  and  Sk  lineages. Most full-length elements were inserted more recently, after hybridization. With the exception of a single full-length element with signs of positive selection, both solo LTRs and, in particular, full-length elements carry signatures of purifying selection indicating effective removal by the host. Consistent with reactivation upon hybridization, the number of full-length LTR retrotransposons, varying extensively from zero to 87 among strains, significantly increases with the degree of genomic admixture. This study gives a detailed account of global TE diversity in  S. pombe , documents complex recombination histories within TE elements, and provides evidence for the \"genomic shock hypothesis.\"","doi":"10.1101/gr.276056.121","authors":"Tusso S, Suo F, Liang Y, Du LL, Wolf JBW","authors_abbrev":"Tusso S et al.","pubmed_publication_date":"Feb 2022","pubmed_entrez_date":"2021-12-15","publication_year":"2022","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-12-17 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19563101","title":"Checkpoint regulation of DNA replication.","citation":"Methods Mol Biol 2009;521:55-70","abstract":"We discuss the mechanisms regulating entry into and progression through S phase in eukaryotic cells. Methods to study the G1/S transition are briefly reviewed and an overview of G1/S-checkpoints is given, with particular emphasis on fission yeast. Thereafter we discuss different aspects of the intra-S checkpoint and introduce the main molecular players and mechanisms.","doi":"10.1007/978-1-60327-815-7_4","authors":"Boye E, Skjølberg HC, Grallert B","authors_abbrev":"Boye E et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1729722","title":"Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin.","citation":"Proc Natl Acad Sci U S A 1992 Jan 01;89(1):80-3","abstract":"Actins are a family of highly conserved proteins that are ubiquitously found among eukaryotic organisms. All actins that have previously been identified, including those of animals, plants, fungi, and protozoa, are 374-376 amino acids long and exhibit at least 70% amino acid sequence identity when compared with one another. We have cloned a gene from the fission yeast Schizosaccharomyces pombe that encodes a distantly related member of the actin protein family, herein referred to as act2. In contrast to all other actins, the derived amino acid sequence reveals that act2 is 427 residues long and exhibits only 35-40% identity to actins, including act1 from Sch. pombe. Comparison to the known x-ray crystallographic structure of rabbit skeletal muscle actin indicates that the ATP and divalent metal ion binding sites are largely conserved in act2, while regions involved in actin-actin and actin-myosin interactions are relatively divergent. Disruption of the act2 gene demonstrated that this gene encodes a function essential for germination of haploid spores. These findings indicate that while act2 and act1 are related proteins, they appear to have distinct functions. In addition, they demonstrate that the actin protein family is more diverse than was previously thought.","authors":"Lees-Miller JP, Henry G, Helfman DM","authors_abbrev":"Lees-Miller JP et al.","pubmed_publication_date":"01 Jan 1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_session_key":"3bf88ffa89c44f16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-01-19 15:09:12","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-12-27 02:51:17","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-27"},{"uniquename":"PMID:14749391","title":"U17/snR30 is a ubiquitous snoRNA with two conserved sequence motifs essential for 18S rRNA production.","citation":"Mol Cell Biol 2004 Feb;24(4):1769-78","abstract":"Saccharomyces cerevisiae snR30 is an essential box H/ACA small nucleolar RNA (snoRNA) required for the processing of 18S rRNA. Here, we show that the previously characterized human, reptilian, amphibian, and fish U17 snoRNAs represent the vertebrate homologues of yeast snR30. We also demonstrate that U17/snR30 is present in the fission yeast Schizosaccharomyces pombe and the unicellular ciliated protozoan Tetrahymena thermophila. Evolutionary comparison revealed that the 3'-terminal hairpins of U17/snR30 snoRNAs contain two highly conserved sequence motifs, the m1 (AUAUUCCUA) and m2 (AAACCAU) elements. Mutation analysis of yeast snR30 demonstrated that the m1 and m2 elements are essential for early cleavages of the 35S pre-rRNA and, consequently, for the production of mature 18S rRNA. The m1 and m2 motifs occupy the opposite strands of an internal loop structure, and they are located invariantly 7 nucleotides upstream from the ACA box of U17/snR30 snoRNAs. U17/snR30 is the first identified box H/ACA snoRNA that possesses an evolutionarily conserved role in the nucleolytic processing of eukaryotic pre-rRNA.","authors":"Atzorn V, Fragapane P, Kiss T","authors_abbrev":"Atzorn V et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2004-01-30","publication_year":"2004","canto_session_key":"4c0b99b1049ec3ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-15 11:13:54","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-15 11:13:28","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.20"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-15"},{"uniquename":"PMID:16473542","title":"Nomenclature and functions of RNA-directed RNA polymerases.","citation":"Trends Plant Sci 2006 Mar;11(3):142-51","abstract":"There is little relationship between eukaryotic RNA-directed RNA polymerases (RDRs), viral RNA-dependent RNA polymerases (RdRps) and DNA-dependent RNA polymerases, indicating that RDRs evolved as an independent class of enzymes early in evolution. In fungi, plants and several animal systems, RDRs play a key role in RNA-mediated gene silencing [post-transcriptional gene silencing (PTGS) in plants and RNA interference (RNAi) in non-plants] and are indispensable for heterochromatin formation, at least, in Schizosaccharomyces pombe and plants. Recent findings indicate that PTGS, RNAi and heterochromatin formation not only function as host defence mechanisms against invading nucleic acids but are also involved in natural gene regulation. RDRs are required for these processes, initiating a broad interest in this enzyme class.","authors":"Wassenegger M, Krczal G","authors_abbrev":"Wassenegger M et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-02-14","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7737676","title":"Isolation and characterization of two monoclonal antibodies raised against tms1 protein of fission yeast.","citation":"Hybridoma 1994 Dec;13(6):527-9","abstract":"Monoclonal antibodies were produced against recombinant tms1 protein of fission yeast. The antibodies of IgG3 subclass were isolated from serum-free cell culture medium and purified by affinity chromatography on protein A-Sepharose. The antibodies can be used to detect specifically the tms1 protein on immunoblots of total yeast lysates. In addition, native tms1 protein is specifically precipitated by these antibodies from yeast lysates.","authors":"Wagner P, Waschow C, Nastainczyk W, Montenarh M","authors_abbrev":"Wagner P et al.","pubmed_publication_date":"Dec 1994","pubmed_entrez_date":"1994-12-01","publication_year":"1994","canto_session_key":"61762cee33a54fcd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-04-04 11:08:23","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-02-26 16:19:35","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1773.05c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-02-26"},{"uniquename":"PMID:11267679","title":"Characterization and regulation of Schizosaccharomyces pombe gene encoding thioredoxin.","citation":"Biochim Biophys Acta 2001 Mar 19;1518(1-2):194-9","abstract":"A cDNA coding thioredoxin (TRX) was isolated from a cDNA library of Schizosaccharomyces pombe by colony hybridization. The 438 bp EcoRI fragment, which was detected by Southern hybridization, reveals an open reading frame which encodes a protein of 103 amino acids. The genomic DNA encoding TRX was also isolated from S. pombe chromosomal DNA using PCR. The cloned sequence contains 1795 bp and encodes a protein of 103 amino acids. However, the C-terminal region obtained from the cDNA clone is -Val-Arg-Leu-Asn-Arg-Ser-Leu, whereas the C-terminal region deduced from the genomic DNA appears to contain -Ala-Ser-Ile-Lys-Ala-Asn-Leu. This indicates that S. pombe cells contain two kinds of TRX genes which have dissimilar amino acid sequences only at the C-terminal regions. The heterologous TRX 1C produced from the cDNA clone could be used as a subunit of T7 DNA polymerase, while the TRX 1G from the genomic DNA could not. The upstream sequence and the region encoding the N-terminal 18 amino acids of the genomic DNA were fused into the promoterless beta-galactosidase gene of the shuttle vector YEp357 to generate the fusion plasmid pYKT24. Synthesis of beta-galactosidase from the fusion plasmid was found to be enhanced by hydrogen peroxide, menadione and aluminum chloride. It indicates that the expression of the cloned TRX gene is induced by oxidative stress.","authors":"Cho Y, Shin YH, Kim Y, Kim H, Lee Y, Park E, Fuchs JA, Lim C","authors_abbrev":"Cho Y et al.","pubmed_publication_date":"19 Mar 2001","pubmed_entrez_date":"2001-03-27","publication_year":"2001","canto_session_key":"0ad9c185363427b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:54:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 14:48:13","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC7D4.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-05"},{"uniquename":"PMID:28784611","title":"Phosphoinositide-mediated ring anchoring resists perpendicular forces to promote medial cytokinesis.","citation":"J Cell Biol 2017 Oct 02;216(10):3041-3050","abstract":"Many eukaryotic cells divide by assembling and constricting an actin- and myosin-based contractile ring (CR) that is physically linked to the plasma membrane (PM). In this study, we report that  Schizosaccharomyces pombe  cells lacking  efr3 , which encodes a conserved PM scaffold for the phosphatidylinositol-4 kinase Stt4, build CRs that can slide away from the cell middle during anaphase in a myosin V-dependent manner. The Efr3-dependent CR-anchoring mechanism is distinct from previously reported pathways dependent on the Fes/CIP4 homology Bin-Amphiphysin-Rvs167 (F-BAR) protein Cdc15 and paxillin Pxl1. In  efr3Δ , the concentrations of several membrane-binding proteins were reduced in the CR and/or on the PM. Our results suggest that proper PM lipid composition is important to stabilize the central position of the CR and resist myosin V-based forces to promote the fidelity of cell division.","doi":"10.1083/jcb.201705070","authors":"Snider CE, Willet AH, Chen JS, Arpağ G, Zanic M, Gould KL","authors_abbrev":"Snider CE et al.","pubmed_publication_date":"02 Oct 2017","pubmed_entrez_date":"2017-08-09","publication_year":"2017","canto_session_key":"f4da3c52016e8dca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2017-10-24 18:46:14","canto_approved_date":"2024-11-04 12:30:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-22 17:04:54","canto_added_date":"2017-08-10 00:15:14","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":29,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC577.06c","SPAC20G8.05c","SPCC1919.10c","SPAC323.01c","SPBC146.13c","SPAC16E8.09","SPAPYUG7.03c","SPCC645.07","SPBC4F6.12","SPCC4B3.15","SPCPB16A4.02c","SPBC2D10.14c","SPAC4A8.05c","SPBC1289.04c","SPAC637.04","SPCC645.05c","SPAC2F7.03c","SPCC794.08"],"gene_count":18,"ltp_gene_count":11,"approved_date":"2017-10-24"},{"uniquename":"PMID:36868227","title":"RNA:DNA hybrids from Okazaki fragments contribute to establish the Ku-mediated barrier to replication-fork degradation.","citation":"Mol Cell 2023 Apr 06;83(7):1061-1074.e6","abstract":"Nonhomologous end-joining (NHEJ) factors act in replication-fork protection, restart, and repair. Here, we identified a mechanism related to RNA:DNA hybrids to establish the NHEJ factor Ku-mediated barrier to nascent strand degradation in fission yeast. RNase H activities promote nascent strand degradation and replication restart, with a prominent role of RNase H2 in processing RNA:DNA hybrids to overcome the Ku barrier to nascent strand degradation. RNase H2 cooperates with the MRN-Ctp1 axis to sustain cell resistance to replication stress in a Ku-dependent manner. Mechanistically, the need of RNaseH2 in nascent strand degradation requires the primase activity that allows establishing the Ku barrier to Exo1, whereas impairing Okazaki fragment maturation reinforces the Ku barrier. Finally, replication stress induces Ku foci in a primase-dependent manner and favors Ku binding to RNA:DNA hybrids. We propose a function for the RNA:DNA hybrid originating from Okazaki fragments in controlling the Ku barrier specifying nuclease requirement to engage fork resection.","doi":"10.1016/j.molcel.2023.02.008","authors":"Audoynaud C, Schirmeisen K, Ait Saada A, Gesnik A, Fernández-Varela P, Boucherit V, Ropars V, Chaudhuri A, Fréon K, Charbonnier JB, Lambert SAE","authors_abbrev":"Audoynaud C et al.","pubmed_publication_date":"06 Apr 2023","pubmed_entrez_date":"2023-03-03","publication_year":"2023","canto_session_key":"f245abd7daba0a59","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-03-05 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33236313","title":"Ascorbic acid mitigates cadmium-induced stress, and contributes to ionome stabilization in fission yeast.","citation":"Environ Sci Pollut Res Int 2021 Mar;28(12):15380-15393","abstract":"Cadmium is a highly toxic environmental pollutant which through enhancement of reactive oxygen species (ROS) production triggers oxidative stress to the cell. Cell growth, a fundamental feature of all living organisms is closely connected to the cell shape and homeostasis. As these processes largely depend on cell fitness status and environmental conditions we have analyzed, the impact of different cadmium concentrations and the effect of ascorbic acid (ascorbate, AsA) supplementation on cell growth parameters, cell morphology, and ionome balance maintenance in Schizosaccharomyces pombe. We show that cadmium causes membrane lipid peroxidation resulting in cell shape alterations leading to growth impairment and through mineral elements disequilibrium affects ionome homeostasis in a dose- and time-dependent manner. AsA recognized as one of the most prominent antioxidants, when overdosed, displays considerable pro-oxidant activity, though precise dosing of its supplementation is desired. We present here that AsA under efficacious concentration largely improves cell condition affected by cadmium. Although, we clearly demonstrate the beneficial feature of AsA, further studies are required to fully understand its protective nature on cell homeostasis maintenance under conditions of the broken environment.","doi":"10.1007/s11356-020-11480-x","authors":"Navrátilová A, Kovár M, Požgajová M","authors_abbrev":"Navrátilová A et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2020-11-25","publication_year":"2021","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2020-11-27 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR13466","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC27B12.01c","HGNC:30884"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:36090151","title":"Fission yeast Dap1 heme iron-coordinating residue Y83 is required for cytochromes P450 function.","citation":"MicroPubl Biol 2022;2022","abstract":"Fission yeast Dap1 is a heme binding protein required for cytochromes P450 activity. Here, we tested whether Dap1 axial coordination of heme iron is required for its role in the function of the cytochrome P450 enzymes, Erg5 and Erg11. Two different  dap1  mutants predicted to alter iron coordination failed to rescue growth on cobalt chloride containing medium which requires Erg5 and Erg11. In addition, deletion of  dap1  +   did not affect expression of Erg5 or Erg11. PGRMC1, a mammalian Dap1 homolog, does not require heme binding to bind and stabilize cytochromes P450. These experiments highlight important functional differences between these conserved proteins.","doi":"10.17912/micropub.biology.000631","authors":"Zhao S, Hughes AL, Espenshade PJ","authors_abbrev":"Zhao S et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-09-12","publication_year":"2022","canto_session_key":"4c042f68b675355e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2022-09-27 07:55:37","canto_approved_date":"2022-09-27 07:55:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-21 15:35:22","canto_added_date":"2022-09-15 00:15:04","annotation_curators":[{"name":"Peter Espenshade","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-09-27"},{"uniquename":"PMID:15461661","title":"Local exposure of phosphatidylethanolamine on the yeast plasma membrane is implicated in cell polarity.","citation":"Genes Cells 2004 Oct;9(10):891-903","abstract":"Cell surface phosphatidylethanolamine (PE) of the yeast cell was probed by biotinylated Ro09-0198 (Bio-Ro), which specifically binds to PE and was visualized with fluorescein-labelled streptavidin. In Saccharomyces cerevisiae, the signals were observed at the presumptive bud site, the emerging small bud cortex, the bud neck of the late mitotic large-budded cells and the tip of the mating projection. In Schizosaccharomyces pombe, the signals were observed at one end or both ends of mono-nucleated cells and the division plane of the late mitotic cells. These sites were polarized ends in the yeast cells, implying that PE is exposed on the cell surface at cellular polarized ends. Treatment of S. cerevisiae cells with Ro09-0198 resulted in aberrant F-actin accumulation at the above sites, implying that limited surface exposure of PE is involved in the polarized organization of the actin cytoskeleton. Furthermore, S. cerevisiae ros3, dnf1 and dnf2 null mutants, which were known to be defective in the internalization of fluorescence-labelled PE, as well as the combinatorial mutants, were stained with Bio-Ro at the enlarging bud cortex, in addition to the Bio-Ro-staining sites of wild-type cells, suggesting that Ros3p, Dnf1p and Dnf2p are involved in the retrieval of exposed PE at the bud cortex.","authors":"Iwamoto K, Kobayashi S, Fukuda R, Umeda M, Kobayashi T, Ohta A","authors_abbrev":"Iwamoto K et al.","pubmed_publication_date":"Oct 2004","pubmed_entrez_date":"2004-10-06","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22451489","title":"Cyclin-dependent kinase 8 regulates mitotic commitment in fission yeast.","citation":"Mol Cell Biol 2012 Jun;32(11):2099-109","abstract":"Temporal changes in transcription programs are coupled to control of cell growth and division. We here report that Mediator, a conserved coregulator of eukaryotic transcription, is part of a regulatory pathway that controls mitotic entry in fission yeast. The Mediator subunit cyclin-dependent kinase 8 (Cdk8) phosphorylates the forkhead 2 (Fkh2) protein in a periodic manner that coincides with gene activation during mitosis. Phosphorylation prevents degradation of the Fkh2 transcription factor by the proteasome, thus ensuring cell cycle-dependent variations in Fkh2 levels. Interestingly, Cdk8-dependent phosphorylation of Fkh2 controls mitotic entry, and mitotic entry is delayed by inactivation of the Cdk8 kinase activity or mutations replacing the phosphorylated serine residues of Fkh2. In addition, mutations in Fkh2, which mimic protein phosphorylation, lead to premature mitotic entry. Therefore, Fkh2 regulates not only the onset of mitotic transcription but also the correct timing of mitotic entry via effects on the Wee1 kinase. Our findings thus establish a new pathway linking the Mediator complex to control of mitotic transcription and regulation of mitotic entry in fission yeast.","doi":"10.1128/MCB.06316-11","authors":"Szilagyi Z, Banyai G, Lopez MD, McInerny CJ, Gustafsson CM","authors_abbrev":"Szilagyi Z et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2012-03-28","publication_year":"2012","canto_session_key":"d3c28a9773ee0a38","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Zsolt Szilagyi","canto_first_approved_date":"2018-10-04 15:50:24","canto_approved_date":"2024-03-29 10:15:39","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-11-01 17:45:34","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Zsolt Szilagyi","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"vw253 cam.ac.uk","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPBC19G7.06","SPAC24H6.05","SPAC6G10.12c","SPAC821.08c","SPBC16G5.15c","SPBC14F5.08","SPBC11B10.09","SPBC32F12.09","SPCC18B5.03","SPBC16G5.01","SPAC23H4.17c"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2018-10-04"},{"uniquename":"PMID:18069982","title":"Yeast identification in grape juice concentrates from Argentina.","citation":"Lett Appl Microbiol 2008 Feb;46(2):192-7","abstract":"The purpose of this study was to identify yeast species present in spoiled and unspoiled grape juice concentrates from Argentine industries.\nOsmophilic and osmotolerant yeasts were isolated from spoiled--visually effervescent--and unspoiled--without any visible damage--grape juice concentrates by the spread-plate technique in two culture media. Yeast identification was done by classical and molecular methods. Zygosaccharomyces rouxii was the only species isolated from spoiled grape juice concentrates. In unspoiled samples, five different species were identified: Z. rouxii was isolated at a higher frequency, followed in decreasing order by Saccharomyces cerevisiae, Schizosaccharomyces pombe, Pichia anomala and Kluyveromyces delphensis.\nYeasts isolated from grape juice concentrates were characterized by a limited taxonomic diversity, where Z. rouxii was the main species isolated.\nGrape production in Argentina is mainly devoted to the industry where wine and grape juice concentrates represent major types of commercial products. Little information on common yeast contaminants is available for grape juice concentrates. This study constitutes the first report of osmophilic yeast species present in spoiled and unspoiled grape juice concentrates elaborated in Argentina.","authors":"Combina M, Daguerre C, Massera A, Mercado L, Sturm ME, Ganga A, Martinez C","authors_abbrev":"Combina M et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2007-12-12","publication_year":"2008","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19061185","title":"Fission yeast translation initiation factor 3 subunit eIF3h is not essential for global translation initiation, but deletion of eif3h+ affects spore formation.","citation":"Yeast 2008 Nov;25(11):809-23","abstract":"The fission yeast Schizosaccharomyces pombe homologue of the p40/eIF3h subunit of mammalian translation initiation factor eIF3 has been characterized in this study. We show that this protein physically associates with the 40S ribosomal particles as a constituent of the multimeric eIF3 protein complex, which consists of all five known eIF3 core subunits (eIF3a, eIF3b, eIF3c, eIF3g and eIF3i) as well as the five non-core subunits (eIF3d, eIF3e, eIF3f, eIF3h and eIF3m) that constitute an eIF3 holocomplex in fission yeast. However, affinity purification of eIF3 from fission yeast cells expressing TAP-tagged eIF3h suggests the presence of distinct forms of eIF3 that differ in their composition of the non-core subunits. Further characterization of eIF3h shows that strains lacking eif3h(+) (eif3hDelta) are viable and show no gross defects, either in vegetative growth or in the rate of in vivo protein synthesis. Polysome profile analysis shows no apparent defects in translation initiation. Furthermore, deletion of eif3h(+) does not affect the ability of the other eIF3 subunits to remain associated with one another in a tight protein complex similar to the situation in wild-type cells. Additionally, we show that human eIF3h can functionally substitute fission yeast eIF3h in complementing in vivo a genetic deletion of eif3h(+). Interestingly, mutant eif3hDelta cells show several prominent phenotypic properties. They are hypersensitive to caffeine and highly defective in meiosis, producing either no spores or incomplete tetrads with a very high frequency. The implications of these results in relation to the functions of eIF3h in Sz. pombe are discussed.","doi":"10.1002/yea.1635","authors":"Ray A, Bandyopadhyay A, Matsumoto T, Deng H, Maitra U","authors_abbrev":"Ray A et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-12-09","publication_year":"2008","canto_session_key":"a565f7295bbf694f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-01 13:27:18","canto_approved_date":"2022-01-25 08:42:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-15 16:04:09","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.05","SPBC646.09c","SPAC1751.03","SPAC4A8.16c","SPBC18H10.03","SPAC4D7.05","SPAC637.07","SPBC4C3.07","SPAC25G10.08","SPBC17D11.05","SPAC3A12.13c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2015-04-01"},{"uniquename":"EMBL:AU012012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9246181","title":"What will molecular biology contribute to our understanding of radiation-induced cell killing and carcinogenesis?","citation":"Int J Radiat Biol 1997 Jun;71(6):667-74","abstract":"The vast body of radiobiological data accumulated with mammalian systems in vitro and in vivo has had an enormous impact on radiotherapy. However, while quantitative, these data are essentially phenomenological, and it is only in the last decade or so that the techniques of molecular biology allow basic mechanisms to be understood. This will be illustrated by two examples, one involving cell killing and the other carcinogenesis. The identification and sequencing of repair and checkpoint control genes in the yeast S. pombe allow the mechanism of sensitivity/ resistance to radiation to be understood at the molecular level. The development of techniques to identify mutations in mismatch repair genes have made it possible to show that such mutations are associated with a wide range of human cancers and are a likely mechanism of radiation induced malignancies. Tikvah Alper would have been delighted to see the central role that micro-organisms have played in these recent developments.","authors":"Hall EJ","authors_abbrev":"Hall EJ","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39271159","title":"Interaction between ESCRT-III proteins and the yeast SERINC homolog Tms1.","citation":"Genetics 2024 Oct 07;228(2)","abstract":"The endosomal sorting complex required for transport (ESCRT)-III is involved in membrane remodeling and abscission during intraluminal vesicle (ILV) formation at endosomes. Our data now suggest that ESCRT-III function could be connected to lipid remodeling of the endosomal membrane. This notion is based on our finding that ESCRT-III proteins bind to the yeast serine incorporator (SERINC) homolog Tms1. Human SERINC3 and SERINC5 are HIV-1 restriction factors and have been shown to act as scramblases, flipping phospholipids between membrane leaflets. Due to the extraordinarily high sequence conservation between Tms1 and human SERINCs, it is likely that Tms1 is also a scramblase. While deletion of TMS1 had only a moderate effect on the sorting of multivesicular body (MVB) cargo proteins, the simultaneous deletion of a component of the Vps55/Vps68 complex led to a strong synergistic phenotype. This pronounced synergism suggests that Tms1 and Vps55/Vps68 perform a parallel function at endosomes. Vps55/Vps68 loosely resembles Tms1 in its overall structure. Thus, it is possible that Vps55/Vps68 is also a scramblase. Since both Vps55 and Tms1 physically interact with ESCRT-III proteins, we propose that the recruitment of a scramblase plays a crucial role in ESCRT-III-dependent membrane remodeling at endosomes.","doi":"10.1093/genetics/iyae132","authors":"Kölling R","authors_abbrev":"Kölling R","pubmed_publication_date":"07 Oct 2024","pubmed_entrez_date":"2024-09-13","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29423861","title":"Schizosaccharomyces pombe Isolation Protocol.","citation":"Methods Mol Biol 2018;1721:227-234","abstract":"This chapter describes a methodology to isolate yeast strains from Schizosaccharomyces pombe species. The method is based on a selective-differential medium that notably facilitates the isolation of S. pombe. The main difficulty in isolating microorganisms from this genus is their extremely low incidence in nature when they are compared to other microorganisms. The proposed methodology allows isolating and selecting strains from this species for industrial purposes. Methodologies allows detecting the presence of those yeasts when they are considered spoilage microorganisms. Several selective-differential agents based on the basic physiological characteristics of S. pombe species are exposed during the chapter introduction and the use is properly justified. Some of those representative characteristics are its extraordinary resistance to high sugar concentrations, sulfur dioxide, sorbic acid, benzoic acid, acetic acid, or their unique malo-ethanolic fermentation ability. The proposed selective medium is mainly based on S. pombe resistance to the antibiotic actidione and the unusual tolerance to the inhibitory agent benzoic acid compared to possible microorganisms that could produce false-positive results during an isolation process. In addition, malic acid is proposed as the main differential factor due to the exclusive ability of this species to metabolize malic acid into ethanol. This fact allows the detection of malic acid degradation. Cloramphenicol is used to inhibit bacteria growth and liquid media to avoid fungi development.","doi":"10.1007/978-1-4939-7546-4_20","authors":"Benito Á, Calderón F, Benito S","authors_abbrev":"Benito Á et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21248484","title":"Linking Cdc7 with the replication checkpoint.","citation":"Cell Cycle 2010 Dec 15;9(24):4787","abstract":"","doi":"10.4161/cc.9.24.14167","authors":"Vaziri C","authors_abbrev":"Vaziri C","pubmed_publication_date":"15 Dec 2010","pubmed_entrez_date":"2011-01-21","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11752677","title":"Fungal histidine kinases.","citation":"Sci STKE 2001 Sep 04;2001(98):re1","abstract":"Eukaryotic cells predominantly use serine, threonine, and tyrosine phosphorylation in various intracellular signal transduction pathways. In contrast, prokaryotic organisms employ numerous \"two-component\" systems, in which signaling is achieved by transferring a phosphoryl group from phosphohistidine in the \"sensor kinase\" component to aspartate in the \"response regulator\" component. In the last several years, genetic screens and genome projects have identified sensor kinases and response regulators in lower eukaryotes and plants, revealing that eukaryotic organisms also make use of His-Asp phosphotransfer in a limited number of signaling pathways. Extensive studies in yeasts have demonstrated that a variation of the two-component system, a multistep \"phosphorelay,\" is the prevailing mechanism among distantly related yeast species. In the budding yeast Saccharomyces cerevisiae, a His-Asp-His-Asp phosphorelay transmits osmotic stress signals to a mitogen-activated protein kinase (MAPK) cascade to induce adaptive responses. A phosphorelay in the fission yeast Schizosaccharomyces pombe, analogous to the S. cerevisiae phosphorelay, is responsible for MAPK activation in response to peroxide stress. Mammalian cells do not have any two-component or phosphorelay systems, although protein histidine kinases unrelated to the sensor kinase may be involved in cellular signaling. Because some phosphorelay proteins are essential for virulence of microbial pathogens, including the yeast fungus Candida albicans, novel antibiotics targeted to phosphorelays may be effective against eukaryotic pathogens without causing host cell damage.","authors":"Santos JL, Shiozaki K","authors_abbrev":"Santos JL et al.","pubmed_publication_date":"04 Sep 2001","pubmed_entrez_date":"2001-12-26","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPAB703","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9136000","title":"The Schizosaccharomyces pombe rec16 gene product regulates multiple meiotic events.","citation":"Genetics 1997 May;146(1):57-67","abstract":"Previously isolated meiotic recombination (rec) mutants of Schizosaccharomyces pombe define 16 complementation groups. The rec genes cloned and sequenced to date reveal little amino acid sequence identity to other reported proteins. We examined the rec mutants for alterations in meiotic events other than recombination to gain insight into the rec gene functions and to assess whether they affect recombination directly or indirectly. While mutations in the rec6-12, 14, 15 and 19 genes appeared to affect only meiotic recombination, a mutation in rec16 delayed meiotic DNA synthesis and, in some instances, reduced its amount; mitotic DNA synthesis was not detectably altered, indicating that the rec16 effect is limited to meiosis. In the rec16 mutant some meiotically induced transcripts (e.g., rec7 and 15) were significantly reduced in abundance, whereas others (e.g., rec10 and exo1) were induced and degraded with normal timing and extent during meiosis, indicating that the rec16 mutation leaves the basic meiotic program intact. These results indicate that the rec genes other than rec16 have their primary effect on meiotic recombination. In contrast, the rec16 gene product is essential for normal meiotic replication, recombination, and induction of some transcripts. These meiotic events may be coupled via a dependence of recombination and transcription on replication or via a cascade of gene expression.","authors":"Li YF, Smith GR","authors_abbrev":"Li YF et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"090a01d4a6643933","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-05-12 17:14:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-12 17:14:00","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.05","SPBC32F12.02","SPAC25G10.04c","SPBC409.03","SPBC1711.14","SPBC29A10.14","SPAC2G11.12","SPBC2D10.06","SPBC21B10.12","SPAC17A5.11","SPCC1753.03c"],"gene_count":11,"ltp_gene_count":5,"approved_date":"2015-05-12"},{"uniquename":"PMID:8598051","title":"Molecular analysis of a novel schizosaccharomyces pombe gene containing two RNP consensus-sequence RNA-binding domains.","citation":"Curr Genet 1996 Mar;29(4):307-15","abstract":"Proteins containing RNP consensus-sequence RNA-binding domains (CS-RBDs) play diverse roles in many aspects of RNA metabolism. Using a PCR strategy, we cloned portions of six new Schizosaccharomyces pombe genes encoding RBD proteins, including a putative homolog of the mammalian splicing factor SAP49. The genomic locus corresponding to a second PCR product, designated rnp24a, was cloned and characterized in detail. Sequence analysis revealed that the Rnp24 protein is highly charged and contains a second RBD with an unusually long Loop-3 sequence. Strains containing a disrupted copy of the rnp24 gene display neither loss of viability nor any discernible growth defects under a variety of conditions, suggesting that the function of Rnp24p overlaps with that of another fission yeast protein. Although database searches did not identify proteins that share extensive amino-acid identity with Rnp24p, phylogenetic analysis suggests that its closest relatives are metazoan hnRNP proteins. The lack of an observable phenotype in S. pombe cells lacking Rnp24p is consistent with this classification, since hnRNP proteins in higher cells include several distinct subfamilies with similar sequences and RNA-binding specificities.","authors":"VanHoy RW, Wise JA","authors_abbrev":"VanHoy RW et al.","pubmed_publication_date":"Mar 1996","pubmed_entrez_date":"1996-03-01","publication_year":"1996","canto_session_key":"c730219a79e3ac04","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-12-05 18:04:15","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-12-05 18:04:09","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-12-05"},{"uniquename":"EMBL:AU006509","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10348908","title":"A fission yeast gene (prr1(+)) that encodes a response regulator implicated in oxidative stress response.","citation":"J Biochem 1999 Jun;125(6):1061-6","abstract":"An inspection of the Schizosaccharomyces pombe genome database revealed that this eukaryotic microorganism possesses a gene that may encode a bacterial type of histidine-to-aspartate (His-Asp) phosphorelay component, namely, a response regulator. The predicted gene, named prr1(+) (S. pombe response regulator), encodes a protein that contains a typical phospho-accepting receiver domain, preceded by a mammalian heat shock factor (HSF)-like DNA-binding domain. Inactivation of this prr1(+) gene resulted in mutant cells defective in some aspects of stress responses, including sensitivity to oxidative stress, cold-temperature, and heavy metal toxicity. It was also demonstrated that Prr1 is required for the transcription of some genes (e.g., trr1(+), ctt1(+)), which are induced by oxidative stress. These results suggest that a His-Asp phosphorelay system may be involved in a stress-activated signaling pathway in S. pombe.","authors":"Ohmiya R, Kato C, Yamada H, Aiba H, Mizuno T","authors_abbrev":"Ohmiya R et al.","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-06-01","publication_year":"1999","canto_session_key":"825060cb21f98c3b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-03 14:54:55","canto_approved_date":"2022-06-06 06:34:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-02 11:46:22","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3F6.03","SPBC215.05","SPBC29B5.01","SPCC757.07c","SPAC1783.07c","SPAC24B11.06c","SPAC8C9.14"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2017-08-03"},{"uniquename":"PMID:26132084","title":"Cooperation between Paxillin-like Protein Pxl1 and Glucan Synthase Bgs1 Is Essential for Actomyosin Ring Stability and Septum Formation in Fission Yeast.","citation":"PLoS Genet 2015 Jul;11(7):e1005358","abstract":"In fungal cells cytokinesis requires coordinated closure of a contractile actomyosin ring (CAR) and synthesis of a special cell wall structure known as the division septum. Many CAR proteins have been identified and characterized, but how these molecules interact with the septum synthesis enzymes to form the septum remains unclear. Our genetic study using fission yeast shows that cooperation between the paxillin homolog Pxl1, required for ring integrity, and Bgs1, the enzyme responsible for linear β(1,3)glucan synthesis and primary septum formation, is required for stable anchorage of the CAR to the plasma membrane before septation onset, and for cleavage furrow formation. Thus, lack of Pxl1 in combination with Bgs1 depletion, causes failure of ring contraction and lateral cell wall overgrowth towards the cell lumen without septum formation. We also describe here that Pxl1 concentration at the CAR increases during cytokinesis and that this increase depends on the SH3 domain of the F-BAR protein Cdc15. In consequence, Bgs1 depletion in cells carrying a cdc15ΔSH3 allele causes ring disassembly and septation blockage, as it does in cells lacking Pxl1. On the other hand, the absence of Pxl1 is lethal when Cdc15 function is affected, generating a large sliding of the CAR with deposition of septum wall material along the cell cortex, and suggesting additional functions for both Pxl1 and Cdc15 proteins. In conclusion, our findings indicate that CAR anchorage to the plasma membrane through Cdc15 and Pxl1, and concomitant Bgs1 activity, are necessary for CAR maintenance and septum formation in fission yeast.","doi":"10.1371/journal.pgen.1005358","authors":"Cortés JC, Pujol N, Sato M, Pinar M, Ramos M, Moreno B, Osumi M, Ribas JC, Pérez P","authors_abbrev":"Cortés JC et al.","pubmed_publication_date":"Jul 2015","pubmed_entrez_date":"2015-07-02","publication_year":"2015","canto_session_key":"80b382d361649949","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pilar Perez","canto_first_approved_date":"2017-10-24 18:52:34","canto_approved_date":"2025-12-23 12:39:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-13 15:05:22","canto_added_date":"2015-07-03 00:20:35","annotation_curators":[{"name":"Juan Carlos García Cortés","community_curator":true,"annotation_count":5,"orcid":"0000-0002-2395-6668","file_type":null,"file_name":null},{"name":"Pilar Perez","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPCC1840.02c","SPCC1281.01","SPBC4F6.12","SPAC20G8.05c","SPBC17F3.01c"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2017-10-24"},{"uniquename":"PMID:15859341","title":"[Effect of flocculence of a self-flocculating yeast on its tolerance to ethanol and the mechanism].","citation":"Sheng Wu Gong Cheng Xue Bao 2005 Jan;21(1):123-8","abstract":"Investigation was undertaken for the purpose of examining any possible correlation between flocculence of a self-flocculating fusant of Schizosaccharomyces pombe mutant and Saccharomyces cerevisiae mutant (called fusant SPSC for short) and the tolerance of this strain to ethanol. When exposed to 18% (V/V) ethanol for 7 h at 30 degrees C, 52%, 37% and 9% of viability levels remained for the cells of fusant SPSC and its two parental strains, Sch. pombe mutant and S. cerevisiae mutant respectively. Analysis of phospholipid fatty acid composition of plasma membrane showed that the content of palmitic acid of each flocculating yeast (fusant SPSC or Sch. pombe mutant) was around 2-fold higher than that of free S. cerevisiae mutant, with remarkably lower contents of palmitoleic and oleic acids than the latter. When 0.1 mol/L sodium citrate was initially included in the medium in which cells of each flocculating yeast were grown, free cells rather than aggregates were finally obtained. Furthermore, the content of palmitic acid in the phospholipid fatty acid composition of the plasma membranes of the free cells of each flocculating yeast was found to decrease significantly, with a marked increase in the contents of palmitoleic and oleic acids. As a result, the characteristics of the phospholipid fatty acid composition of the plasma membranes of the free cells of each flocculating yeast were similar to those of S. cerevisiae mutant. Meanwhile, the disappearance of flocculence of each flocculating yeast caused by the action of sodium citrate brought about a steeply decreased tolerance of the free cells to ethanol, thus being equivalent to that of S. cerevisiae mutant. These data suggest that the stronger ethanol tolerance of each flocculating yeast is related to the higher content of palmitic acid in the phospholipid fatty acid composition of the plasma membranes. Thus, the enhancement by flocculence on the tolerance of yeast cells to ethanol as well as its mechanism are first reported in this work.","authors":"Hu CK, Bai FW, An LJ","authors_abbrev":"Hu CK et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2005-04-30","publication_year":"2005","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34634819","title":"Translational activators and mitoribosomal isoforms cooperate to mediate mRNA-specific translation in Schizosaccharomyces pombe mitochondria.","citation":"Nucleic Acids Res 2021 Nov 08;49(19):11145-11166","abstract":"Mitochondrial mRNAs encode key subunits of the oxidative phosphorylation complexes that produce energy for the cell. In Saccharomyces cerevisiae, mitochondrial translation is under the control of translational activators, specific to each mRNA. In Schizosaccharomyces pombe, which more closely resembles the human system by its mitochondrial DNA structure and physiology, most translational activators appear to be either lacking, or recruited for post-translational functions. By combining bioinformatics, genetic and biochemical approaches we identified two interacting factors, Cbp7 and Cbp8, controlling Cytb production in S. pombe. We show that their absence affects cytb mRNA stability and impairs the detection of the Cytb protein. We further identified two classes of Cbp7/Cbp8 partners and showed that they modulated Cytb or Cox1 synthesis. First, two isoforms of bS1m, a protein of the small mitoribosomal subunit, that appear mutually exclusive and confer translational specificity. Second, a complex of four proteins dedicated to Cox1 synthesis, which includes an RNA helicase that interacts with the mitochondrial ribosome. Our results suggest that S. pombe contains, in addition to complexes of translational activators, a heterogeneous population of mitochondrial ribosomes that could specifically modulate translation depending on the mRNA translated, in order to optimally balance the production of different respiratory complex subunits.","doi":"10.1093/nar/gkab789","authors":"Herbert CJ, Labarre-Mariotte S, Cornu D, Sophie C, Panozzo C, Michel T, Dujardin G, Bonnefoy N","authors_abbrev":"Herbert CJ et al.","pubmed_publication_date":"08 Nov 2021","pubmed_entrez_date":"2021-10-11","publication_year":"2021","canto_session_key":"166679a73087715a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nathalie Bonnefoy","canto_first_approved_date":"2025-03-31 12:29:37","canto_approved_date":"2025-09-03 10:22:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-31 12:29:31","canto_added_date":"2021-10-13 00:15:04","annotation_curators":[{"name":"Nathalie Bonnefoy","community_curator":true,"annotation_count":66,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23A1.18c","SPBC28E12.04","SPAC22H10.09","SPAP8A3.14c","SPBC660.11","SPMIT.11","SPMIT.01","SPMIT.05","SPBC1718.07c","SPBC16A3.03c","YJL209W","SPAC8C9.06c","SPBC11C11.07","SPBP19A11.03c","SPBC25D12.06","SPBC2G2.07c","SPAC5D6.12"],"gene_count":16,"ltp_gene_count":12,"approved_date":"2025-03-31"},{"uniquename":"EMBL:AU008659","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.134"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1706223","title":"mik1 and wee1 cooperate in the inhibitory tyrosine phosphorylation of cdc2.","citation":"Cell 1991 Mar 22;64(6):1111-22","abstract":"wee1 acts antagonistically to cdc25 in the tyrosine dephosphorylation and activation of cdc2, yet biochemical evidence suggests that wee1 is not required for tyrosine phosphorylation and its role is obscure. We show here that a related 66 kd kinase, called mik1, acts redundantly with wee1 in the negative regulation of cdc2 in S. pombe. A null allele of mik1 has no discernible phenotype, but a mik1 wee1 double mutant is hypermitotically lethal: all normal M phase checkpoints are bypassed, including the requirement for initiation of cell cycle \"start,\" completion of S phase, and function of the cdc25+ mitotic activator. In the absence of mik1 and wee1 activity, cdc2 rapidly loses phosphate on tyrosine, both in strains undergoing mitotic lethality and in those that are viable owing to a compensating mutation within cdc2. The data suggest that mik1 and wee1 act cooperatively on cdc2, either directly as the inhibitory tyrosine kinase or as essential activators of that kinase.","authors":"Lundgren K, Walworth N, Booher R, Dembski M, Kirschner M, Beach D","authors_abbrev":"Lundgren K et al.","pubmed_publication_date":"22 Mar 1991","pubmed_entrez_date":"1991-03-22","publication_year":"1991","canto_session_key":"aecebb59178d4cee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-25 09:21:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-20 15:27:09","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC660.14","SPCC18B5.03"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2014-01-20"},{"uniquename":"PMID:2586528","title":"Characterization of the Schizosaccharomyces pombe ral2 gene implicated in activation of the ras1 gene product.","citation":"Mol Cell Biol 1989 Dec;9(12):5617-22","abstract":"Mutations in the Schizosaccharomyces pombe ral2 gene cause a phenotype indistinguishable from that of the ras1-defective mutant. Using cloned ral2 DNA, we disrupted the chromosomal gene. The disruptants showed the same phenotype as the original ral2 isolates, i.e., they had spherical cells, had no detectable mating activity, and exhibited no response to the mating pheromone, but their vegetative growth was apparently normal. Sequence analysis of the ral2 gene suggests that it encodes a polypeptide of 611 amino acid residues whose predicted amino acid sequence shows no strong homology to any known protein. Either multiple copies or even a single copy of the ras1Val-17 allele, which is an activated form of ras1, restored rodlike cell morphology and ability to respond to the mating factor to ral2 mutants. These results suggest that the ral2 and ras1 gene products interact intimately and that the ral2 gene product is involved in activation of the ras1 protein in S. pombe.","authors":"Fukui Y, Miyake S, Satoh M, Yamamoto M","authors_abbrev":"Fukui Y et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_session_key":"28177197c391b5a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-08 11:42:38","canto_approved_date":"2026-04-08 11:05:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 07:40:27","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC21.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-06-08"},{"uniquename":"PMID:22645648","title":"The reverse, but coordinated, roles of Tor2 (TORC1) and Tor1 (TORC2) kinases for growth, cell cycle and separase-mediated mitosis in Schizosaccharomyces pombe.","citation":"Open Biol 2011 Nov;1(3):110007","abstract":"Target of rapamycin complexes (TORCs), which are vital for nutrient utilization, contain a catalytic subunit with the phosphatidyl inositol kinase-related kinase (PIKK) motif. TORC1 is required for cell growth, while the functions of TORC2 are less well understood. We show here that the fission yeast Schizosaccharomyces pombe TORC2 has a cell cycle role through determining the proper timing of Cdc2 Tyr15 dephosphorylation and the cell size under limited glucose, whereas TORC1 restrains mitosis and opposes securin-separase, which are essential for chromosome segregation. These results were obtained using the previously isolated TORC1 mutant tor2-L2048S in the phosphatidyl inositol kinase (PIK) domain and a new TORC2 mutant tor1-L2045D, which harbours a mutation in the same site. While mutated TORC1 and TORC2 displayed diminished kinase activity and FKBP12/Fkh1-dependent rapamycin sensitivity, their phenotypes were nearly opposite in mitosis. Premature mitosis and the G2-M delay occurred in TORC1 and TORC2 mutants, respectively. Surprisingly, separase/cut1-securin/cut2 mutants were rescued by TORC1/tor2-L2048S mutation or rapamycin addition or even Fkh1 deletion, whereas these mutants showed synthetic defect with TORC2/tor1-L2045D. TORC1 and TORC2 coordinate growth, mitosis and cell size control, such as Wee1 and Cdc25 do for the entry into mitosis.","doi":"10.1098/rsob.110007","authors":"Ikai N, Nakazawa N, Hayashi T, Yanagida M","authors_abbrev":"Ikai N et al.","pubmed_publication_date":"Nov 2011","pubmed_entrez_date":"2012-05-31","publication_year":"2011","canto_session_key":"8cef0a6f9aaae17e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Norihiko Nakazawa","canto_first_approved_date":"2018-09-14 15:52:53","canto_approved_date":"2026-02-06 16:22:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-29 14:46:07","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":41,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Norihiko Nakazawa","community_curator":true,"annotation_count":29,"orcid":"0000-0001-8386-0812","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1E7.12","SPBC30D10.10c","SPAC1782.09c","SPAPYUG7.02c","SPCC777.08c","SPAC57A7.11","SPAC13G6.07c","SPBC14C8.01c","SPCC5E4.04","SPBC11B10.09","SPCC162.12","SPBC12C2.02c","SPBC839.17c","SPBC216.07c"],"gene_count":14,"ltp_gene_count":11,"approved_date":"2018-09-14"},{"uniquename":"PMID:17130122","title":"Mutations in the SF1-U2AF59-U2AF23 complex cause exon skipping in Schizosaccharomyces pombe.","citation":"J Biol Chem 2007 Jan 26;282(4):2221-8","abstract":"To identify genes involved in the mechanism to ensure ordered 5' to 3' exon joining in constitutively spliced pre-mRNAs, we screened for mutants that cause exon skipping in the fission yeast Schizosaccharomyces pombe using a reporter plasmid, which contains the ura4+ gene with the nda3 intron 1-exon 2-intron 2 sequence. The reporter plasmid was designed to produce the functional ura4+ mRNA, when the central nda3 exon is skipped during the splicing reaction. We mutagenized cells harboring the plasmid by UV irradiation and isolated 34 ura+ mutants that grew on minimal medium. Of those, eight mutants were found to be temperature sensitive (ts) for growth. Complementation analyses revealed that the ts mutants belong to three distinct complementation groups named ods (ordered splicing) 1, 2, and 3. RT-PCR analyses showed that products of exon skipping were actually generated in the ods mutants. We cloned the genes responsible for the ods mutations, and found that ods1+, ods2+, and ods3+ encode splicing factors Prp2p/U2AF59, U2AF23, and SF1, respectively, which form a SF1-U2AF59-U2AF23 complex involved in recognition of the branch-point and 3' splice site sequences in a pre-mRNA. We also showed that mutations in the SF1-U2AF59-U2AF23 binding sequences in the reporter plasmid result in exon skipping in wild-type S. pombe cells. In addition, drugs that decrease the rate of transcription elongation were found to suppress the exon skipping in the ods mutants. These results suggest that co-transcriptional recognition of a nascent pre-mRNA by the SF1-U2AF59-U2AF23 complex is essential for ordered exon joining in constitutive splicing in S. pombe.","authors":"Haraguchi N, Andoh T, Frendewey D, Tani T","authors_abbrev":"Haraguchi N et al.","pubmed_publication_date":"26 Jan 2007","pubmed_entrez_date":"2006-11-30","publication_year":"2007","canto_session_key":"b1564cf7a7073d6f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-18 15:53:31","canto_approved_date":"2026-01-30 07:09:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-18 15:53:19","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC962.06c","SPBC146.07","SPAP8A3.06"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-08-18"},{"uniquename":"PMID:14759257","title":"A comprehensive evolutionary classification of proteins encoded in complete eukaryotic genomes.","citation":"Genome Biol 2004;5(2):R7","abstract":"Sequencing the genomes of multiple, taxonomically diverse eukaryotes enables in-depth comparative-genomic analysis which is expected to help in reconstructing ancestral eukaryotic genomes and major events in eukaryotic evolution and in making functional predictions for currently uncharacterized conserved genes.\nWe examined functional and evolutionary patterns in the recently constructed set of 5,873 clusters of predicted orthologs (eukaryotic orthologous groups or KOGs) from seven eukaryotic genomes: Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Arabidopsis thaliana, Saccharomyces cerevisiae, Schizosaccharomyces pombe and Encephalitozoon cuniculi. Conservation of KOGs through the phyletic range of eukaryotes strongly correlates with their functions and with the effect of gene knockout on the organism's viability. The approximately 40% of KOGs that are represented in six or seven species are enriched in proteins responsible for housekeeping functions, particularly translation and RNA processing. These conserved KOGs are often essential for survival and might approximate the minimal set of essential eukaryotic genes. The 131 single-member, pan-eukaryotic KOGs we identified were examined in detail. For around 20 that remained uncharacterized, functions were predicted by in-depth sequence analysis and examination of genomic context. Nearly all these proteins are subunits of known or predicted multiprotein complexes, in agreement with the balance hypothesis of evolution of gene copy number. Other KOGs show a variety of phyletic patterns, which points to major contributions of lineage-specific gene loss and the 'invention' of genes new to eukaryotic evolution. Examination of the sets of KOGs lost in individual lineages reveals co-elimination of functionally connected genes. Parsimonious scenarios of eukaryotic genome evolution and gene sets for ancestral eukaryotic forms were reconstructed. The gene set of the last common ancestor of the crown group consists of 3,413 KOGs and largely includes proteins involved in genome replication and expression, and central metabolism. Only 44% of the KOGs, mostly from the reconstructed gene set of the last common ancestor of the crown group, have detectable homologs in prokaryotes; the remainder apparently evolved via duplication with divergence and invention of new genes.\nThe KOG analysis reveals a conserved core of largely essential eukaryotic genes as well as major diversification and innovation associated with evolution of eukaryotic genomes. The results provide quantitative support for major trends of eukaryotic evolution noticed previously at the qualitative level and a basis for detailed reconstruction of evolution of eukaryotic genomes and biology of ancestral forms.","authors":"Koonin EV, Fedorova ND, Jackson JD, Jacobs AR, Krylov DM, Makarova KS, Mazumder R, Mekhedov SL, Nikolskaya AN, Rao BS, Rogozin IB, Smirnov S, Sorokin AV, Sverdlov AV, Vasudevan S, Wolf YI, Yin JJ, Natale DA","authors_abbrev":"Koonin EV et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-02-05","publication_year":"2004","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17264129","title":"Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins.","citation":"Nucleic Acids Res 2007;35(5):1391-401","abstract":"Characterization of spliceosomal complexes in the fission yeast Schizosaccharomyces pombe revealed particles sedimenting in the range of 30-60S, exclusively containing U1 snRNA. Here, we report the tandem affinity purification (TAP) of U1-specific protein complexes. The components of the complexes were identified using (LC-MS/MS) mass spectrometry. The fission yeast U1 snRNP contains 16 proteins, including the 7 Sm snRNP core proteins. In both fission and budding yeast, the U1 snRNP contains 9 and 10 U1 specific proteins, respectively, whereas the U1 particle found in mammalian cells contains only 3. Among the U1-specific proteins in S. pombe, three are homolog to the mammalian and six to the budding yeast Saccharomyces cerevisiae U1-specific proteins, whereas three, called U1H, U1J and U1L, are proteins specific to S. pombe. Furthermore, we demonstrate that the homolog of U1-70K and the three proteins specific to S. pombe are essential for growth. We will discuss the differences between the U1 snRNPs with respect to the organism-specific proteins found in the two yeasts and the resulting effect it has on pre-mRNA splicing.","authors":"Newo AN, Lützelberger M, Bottner CA, Wehland J, Wissing J, Jänsch L, Käufer NF","authors_abbrev":"Newo AN et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-02-01","publication_year":"2007","canto_session_key":"895b0c72805c8ffe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-08-13 14:04:16","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-13 14:04:08","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.14","SPAC23D3.08","SPAC19A8.13","SPAC2C4.03c","SPAC26A3.08","SPBC19C2.14","SPBC11G11.06c","SPBC4B4.07c","SPAC4D7.13","SPBC4B4.09","SPBC839.10","SPBP35G2.09","SPAC27D7.07c","SPBC4B4.05","SPCC16A11.13","SPBC1289.12"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2014-08-13"},{"uniquename":"PMID:2830493","title":"Identification of healed terminal DNA fragments in linear minichromosomes of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1987 Dec;7(12):4424-30","abstract":"The minichromosome Ch16 of the fission yeast Schizosaccharomyces pombe is derived from the centromeric region of chromosome III. We show that Ch16 and a shorter derivative, Ch12, made by gamma-ray cleavage, are linear molecules of 530 and 280 kilobases, respectively. Each minichromosome has two novel telomeres, as shown by genomic Southern hybridization with an S. pombe telomere probe. Comparison by hybridization of the minichromosomes and their chromosomal counterparts showed no signs of gross rearrangement. Cosmid clones covering the ends of the long arms of Ch16 and Ch12 were isolated, and subcloned fragments that contained the breakage sites were identified. They are apparently unique in the genome. By hybridization and Bal 31 digestion, the ends appear to consist of the broken-end sequences directly associated with short stretches (about 300 base pairs) of new DNA that hybridizes to a cloned S. pombe telomere. They do not contain the telomere-adjacent repeated sequences that are present in the normal chromosomes. The sizes of the short telomeric stretches are roughly the same as those of the normal chromosomes. Our results show that broken chromosomal ends in S. pombe can be healed by the de novo addition of the short telomeric repeats. The formation of Ch16 must have required two breakage-healing events, whereas a single cleavage-healing event in the long arm of Ch16 yielded Ch12.","authors":"Matsumoto T, Fukui K, Niwa O, Sugawara N, Szostak JW, Yanagida M","authors_abbrev":"Matsumoto T et al.","pubmed_publication_date":"Dec 1987","pubmed_entrez_date":"1987-12-01","publication_year":"1987","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41906638","title":"Nonsense mutations can increase mRNA levels.","citation":"Biol Open 2026 Apr 15;15(4)","abstract":"Nonsense mutations can reduce mRNA levels, as premature translation termination may lead to the activation of nonsense-mediated mRNA decay (NMD). To examine how positional context influences these outcomes, we introduced premature translation termination codons (PTCs) at 15 locations within the coding region of a GFP reporter gene in Schizosaccharomyces pombe. PTCs in the first third of the coding region consistently led to reduced mRNA levels. In contrast, most downstream PTCs showed modest or minimal reductions, and several were associated with increased mRNA levels relative to the PTC-less control transcript. Measurement of transcript stability for one such variant indicated that the increased abundance was not attributable to decreased turnover. UPF1 deletion in wild-type cells elevated the levels of transcripts that were reduced and, unexpectedly, further increased transcripts' abundance to exceed the control level. In spliced versions of these constructs, downstream PTCs generally reduced mRNA levels regardless of exon junction position. Overall, these observations indicate that an unexpected consequence of nonsense mutations can be increased mRNA levels. These findings may aid in the interpretation of the effects of nonsense mutations on mRNA abundance beyond the predictions of current NMD models and may also help in the design of eukaryotic gene expression constructs.","doi":"10.1242/bio.062444","authors":"Owuamalam PO, Hossain MN, Brogna S","authors_abbrev":"Owuamalam PO et al.","pubmed_publication_date":"15 Apr 2026","pubmed_entrez_date":"2026-03-30","publication_year":"2026","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2026-03-30 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16C9.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU006997","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10888658","title":"Evidence for the packaging of multiple copies of Tf1 mRNA into particles and the trans priming of reverse transcription.","citation":"J Virol 2000 Aug;74(15):7164-70","abstract":"Long terminal repeat (LTR)-containing retrotransposons and retroviruses are close relatives that possess similar mechanisms of reverse transcription. The particles of retroviruses package two copies of viral mRNA that both function as templates for the reverse transcription of the element. We studied the LTR-retrotransposon Tf1 of Schizosaccharomyces pombe to test whether multiple copies of transposon mRNA participate in the production of cDNA. Using the unique self-priming property of Tf1, we obtained evidence that multiple copies of Tf1 mRNA were packaged into virus-like particles. By coexpressing two distinct versions of Tf1, we found that the bulk of reverse transcription that was initiated on one mRNA template was subsequently transferred to others. In addition, the first 11 nucleotides of one mRNA were able to prime, in trans, the reverse transcription of another mRNA.","authors":"Haag AL, Lin JH, Levin HL","authors_abbrev":"Haag AL et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2000-07-11","publication_year":"2000","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14701807","title":"The molecular chaperone, Atp12p, from Homo sapiens. In vitro studies with purified wild type and mutant (E240K) proteins.","citation":"J Biol Chem 2004 Mar 05;279(10):9016-22","abstract":"Work in Saccharomyces cerevisiae has shown that Atp12p binds to unassembled alpha subunits of F(1) and in so doing prevents the alpha subunit from associating with itself in non-productive complexes during assembly of the F(1) moiety of the mitochondrial ATP synthase. We have developed a method to prepare recombinant Atp12p after expression of its human cDNA in bacterial cells. The molecular chaperone activity of HuAtp12p was studied using citrate synthase as a model substrate. Wild type HuAtp12p suppresses the aggregation of thermally inactivated citrate synthase. In contrast, the mutant protein HuAtp12p(E240K), which harbors a lysine at the position of the highly conserved Glu-240, fails to prevent citrate synthase aggregation at 43 degrees C. No significant differences were observed between the wild type and the mutant proteins as judged by sedimentation analysis, cysteine titration, tryptophan emission spectra, or limited proteolysis, which suggests that the E240K mutation alters the activity of HuAtp12p with minimal effects on the physical integrity of the protein. An additional important finding of this work is that the equilibrium chemical denaturation curve of HuAtp12p shows two components, the first of which is associated with protein aggregation. This result is consistent with a model for Atp12p structure in which there is a hydrophobic chaperone domain that is buried within the protein interior.","authors":"Hinton A, Gatti DL, Ackerman SH","authors_abbrev":"Hinton A et al.","pubmed_publication_date":"05 Mar 2004","pubmed_entrez_date":"2004-01-01","publication_year":"2004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.14","SPAC9.12c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:36784561","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2023-02-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12531715","title":"A comparative study on the biosorption characteristics of some yeasts for Remazol Blue reactive dye.","citation":"Chemosphere 2003 Mar;50(8):1075-83","abstract":"Biosorption capacities and rates of different kinds of dried yeasts (Saccharomyces cerevisiae, Schizosaccharomyces pombe, Kluyveromyces marxianus, Candida sp., C. tropicalis, C. lipolytica, C. utilis, C. quilliermendii and C. membranaefaciens) for Remazol Blue reactive dye from aqueous solutions were compared under laboratory conditions as a function of initial pH and initial dye concentration. Optimum initial biosorption pH was determined as 2 for all the yeasts. All the yeast species showed comparable and very high dye sorption at 100 mg/l initial dye concentration. The equilibrium sorption capacity of the biomass increased with increasing initial dye concentration up to 400 mg/l for Candida sp. C. lipolytica and C. tropicalis; up to 300 mg/l for C. quilliermendii and C. utilis and up to 200 mg/l for S. cerevisiae, S. pombe, K. marxianus and C. membranaefaciens while the adsorption yield of dye showed the opposite trend for all the yeasts. Among the nine yeast species, C. lipolytica exhibited the highest dye uptake capacity (Q(0) = 250 mg/g). Both the Freundlich and Langmuir adsorption models were found suitable for describing the biosorption of the dye by all the Candida yeasts (except C. membranaefaciens). The results indicated that the dye uptake process followed the pseudo-second-order kinetics for each dye-yeast system.","authors":"Aksu Z, Dönmez G","authors_abbrev":"Aksu Z et al.","pubmed_publication_date":"Mar 2003","pubmed_entrez_date":"2003-01-18","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11069778","title":"The Spd1p S phase inhibitor can activate the DNA replication checkpoint pathway in fission yeast.","citation":"J Cell Sci 2000 Dec;113 Pt 23:4341-50","abstract":"Spd1p (for S phase delayed) is a cell cycle inhibitor in Schizosaccharomyces pombe. Spd1p overexpression blocks the onset of both S phase and mitosis. In this study, we have investigated the mechanisms by which Spd1p overexpression blocks cell cycle progression, focussing on the block over mitotic onset. High levels of Spd1p lead to an increase in Y15 phosphorylation of Cdc2p and we show that the block over G(2) requires the Wee1p kinase and is dependent on the rad and chk1/cds1 checkpoint genes. We propose that high levels of Spd1p in G(2) cells activate the DNA replication checkpoint control, which leads to a Wee1p-dependent increase of Cdc2p Y15 phosphorylation blocking onset of mitosis. The Spd1p block at S phase onset may act by interfering directly with DNA replication, and also activates the G(2 )rad/hus checkpoint pathway to block mitosis.","authors":"Borgne A, Nurse P","authors_abbrev":"Borgne A et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-09","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.03"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:40629316","title":"Ca 2+ -dependent vesicular and non-vesicular lipid transfer controls hypoosmotic plasma membrane expansion.","citation":"BMC Biol 2025 Jul 09;23(1):207","abstract":"Robust coordination of surface and volume changes is critical for cell integrity. Few studies have elucidated the plasma membrane (PM) remodeling events during drastic cell surface and volume alteration, especially regarding PM sensing and its subsequent rearrangements.\nWe propose a cellular strategy that combines instantaneous non-vesicular lipid transfer with bulk exocytic membrane delivery to maintain PM integrity for dramatic cell surface/volume adaptation.","doi":"10.1186/s12915-025-02309-5","authors":"Mu B, Rutkowski DM, Grenci G, Vavylonis D, Zhang D","authors_abbrev":"Mu B et al.","pubmed_publication_date":"09 Jul 2025","pubmed_entrez_date":"2025-07-08","publication_year":"2025","canto_session_key":"f817d7555236b8ba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Baicong Mu","canto_first_approved_date":"2025-09-29 06:35:53","canto_approved_date":"2025-11-07 16:18:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-08-31 06:53:08","canto_added_date":"2025-07-09 23:25:05","annotation_curators":[{"name":"Baicong Mu","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":45,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB2B4.04c","SPBC215.01","SPCC1322.03","SPAC2C4.17c","SPBC839.06","SPBC215.14c","SPAC2G11.06","SPCP31B10.06","SPAC11E3.02c","SPCC663.14c","SPBC31E1.02c","SPAC977.17","SPCC736.15","SPCC1259.11c","SPBC16G5.05c","SPBC21C3.20c","SPAC6C3.06c","SPAC17C9.12","SPCC1183.11","SPAC1F5.08c","SPAC29A4.19c","SPCC962.01","SPAPYUK71.03c","SPAC4F8.01"],"gene_count":24,"ltp_gene_count":16,"approved_date":"2025-09-29"},{"uniquename":"PMID:10091581","title":"The Schizosaccharomyces pombe Pzh1 protein phosphatase regulates Na+ ion influx in a Trk1-independent fashion.","citation":"Eur J Biochem 1999 Feb;260(1):31-7","abstract":"We have previously shown that fission yeast encodes a PPZ-like phosphatase, designated Pzhl, which is an important determinant of cation homeostasis. pzh1 delta mutants display increased tolerance to Na+ ions, but they are hypersensitive to KC1 [Balcells, L., Gómez, N., Casamayor, A., Clotet, J. & Ariño, J. (1997) Eur. J. Biochem. 250, 476-483]. We have immunodetected Pzh1 in yeast extracts and found that this phosphatase is largely associated with particulate fractions. Cells defective in Pzh1 do not show altered efflux of Na+ or Li+ ions, but they accumulate these cations more slowly than wild-type cells. K+ ion content of pzh1 delta cells is about twice that of wild-type cells, and this can be explained by decreased efflux of K+. Therefore, Pzh1 may regulate both Na+ influx and K+ efflux in fission yeast. To test the possible relationship between K+ uptake, Na+ tolerance and Pzh1 function, we deleted the trk1+ gene, which encodes a putative high-affinity transporter of K+ ions. trkl delta mutants grew well even at relatively low concentrations of KCl and did not show significantly altered content or influx of K+ ions. However, they showed a Na(+)-sensitive phenotype which was greatly intensified by deletion of the sod2+ gene (which encodes the major determinant for efflux of Na+ ions), and clearly ameliorated by deletion of the pzh1 phosphatase, as well as by moderate concentrations of KCl in the medium. These results suggest that Trk1 does not mediate the effect of Pzh1 on NaCl tolerance and that fission yeast contains efficient systems, other than Trk1, for uptake of K+ ions.","authors":"Balcells L, Calero F, Gómez N, Ramos J, Ariño J","authors_abbrev":"Balcells L et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-03-26","publication_year":"1999","canto_session_key":"0369d33a270a1b0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-04-19 07:19:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-04-19 07:19:43","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.08","SPAC3F10.02c","SPAC977.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-04-19"},{"uniquename":"PMID:9872416","title":"Repression of enzymes of the pentose phosphate pathway by glucose in fission yeast.","citation":"FEBS Lett 1998 Dec 04;440(3):430-3","abstract":"We examine here the effect of carbon sources on the synthesis of the shunt pathway enzymes in the fission yeast Schizosaccharomyces pombe growing on a mixture of ethanol and glycerol. Delta-gluconolactone induces practically every one of these enzymes. Glucose in contrast tends to attenuate the synthesis of the majority of them. RNA analysis confirms that their induction and repression reflect changes in the levels of their transcripts.","authors":"Mehta S, Velmurugan S, Lobo Z","authors_abbrev":"Mehta S et al.","pubmed_publication_date":"04 Dec 1998","pubmed_entrez_date":"1999-01-01","publication_year":"1998","canto_session_key":"b05124975291e7b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-12-02 15:41:42","canto_approved_date":"2025-02-18 17:53:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-12-01 21:39:42","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.12","SPAC144.12","SPAC3C7.13c","SPCC1020.06c","SPCC16C4.10","SPAC31G5.05c","SPBC660.16","SPBC2G5.05"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2021-12-02"},{"uniquename":"PMID:38393470","title":"Artificial Modulation and Rewiring of Cell Cycle Progression Using Synthetic Circuits in Fission Yeast.","citation":"Methods Mol Biol 2024;2740:89-105","abstract":"Cell cycle control is a central aspect of the biology of proliferating eukaryotic cells. However, progression through the cell cycle relies on a highly complex network, making it difficult to unravel the core design principles underlying the mechanisms that sustain cell proliferation and the ways in which they interact with other cellular pathways. In this context, the use of a synthetic approach to simplify the cell cycle network in unicellular genetic models such as fission yeast has opened the door to studying the biology of proliferating cells from unique perspectives. Here, we provide a series of methods based on a minimal cell cycle module in the fission yeast Schizosaccharomyces pombe that allows for an unprecedented artificial control of cell cycle events, enabling the rewiring and remodeling of cell cycle progression.","doi":"10.1007/978-1-0716-3557-5_5","authors":"Jain A, Wu PJ, Coudreuse D","authors_abbrev":"Jain A et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-02-23","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-02-24 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24186545","title":"Benomyl resistant mutants of Schizosaccharomyces pombe cold-sensitive for mitosis.","citation":"Curr Genet 1982 Dec;6(3):195-201","abstract":"We have isolated 150 benomyl resistant mutants of the fission yeast Schizosaccharomyces pombe. Seven of these mutants were found to be cold sensitive for mitosis. These mutants were the subject of physiological, cytological and genetical characterisation. Growth and division of the seven mutants were similar to the wild type strain at 35 °C. After shift from the permissive (35 °C) to the restrictive temperature (20 °C) the mutants became blocked in mitosis whilst cellular growth continued. Consequently, elongate cells were formed. Six of the seven benomyl resistant mutants became blocked in mitosis at 20 °C with a single aberrant nucleus. In every case the benomyl resistant and cold sensitive phenotype was due to a mutation in a single nuclear gene. These mutants were found to comprise a single genetic linkage group (ben4) and were unlinked to existing TBZ/MBC resistant mutants of S. pombe. Whilst no cross resistance was found in our mutants to TBZ, six of the seven mutants were super sensitive to the spindle poison CIPC. We believe that the phenotype exhibited by these mutants is consistent with a defective tubulin subunit.","doi":"10.1007/BF00390338","authors":"Roy D, Fantes PA","authors_abbrev":"Roy D et al.","pubmed_publication_date":"Dec 1982","pubmed_entrez_date":"2013-11-05","publication_year":"1982","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 06:09:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41413728","title":"The Gene Ontology knowledgebase in 2026.","citation":"Nucleic Acids Res 2025 Dec 18;","abstract":"The Gene Ontology (GO) knowledgebase (https://geneontology.org) is a comprehensive resource describing the functions of genes. The GO knowledgebase is regularly updated and improved. We describe here the major updates that have been made in the past 3 years. The ontology and annotations have been expanded and revised, particularly in several areas of biology: cellular metabolism, multi-organism interactions (e.g. host-pathogen), extracellular matrix proteins, chromatin remodeling (e.g. the \"histone code\"), and noncoding RNA functions. We have released version 2 of a comprehensive set of integrated, reviewed annotations for human genes, which we call the \"functionome.\" We have also dramatically increased the number of GO-CAM models, with over 1500 models of metabolic and signaling pathways, primarily in human, mouse, budding and fission yeast, and fruit fly. Finally, we discuss our current recommendations and future prospects of AI in the use and development of GO.","doi":"10.1093/nar/gkaf1292","authors":"Gene Ontology Consortium\n","authors_abbrev":"Gene Ontology Consortium\n","pubmed_publication_date":"18 Dec 2025","pubmed_entrez_date":"2025-12-18","publication_year":"2025","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2025-12-20 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28539404","title":"Analysis of interphase node proteins in fission yeast by quantitative and superresolution fluorescence microscopy.","citation":"Mol Biol Cell 2017 Nov 07;28(23):3203-3214","abstract":"We used quantitative confocal microscopy and FPALM superresolution microscopy of live fission yeast to investigate the structures and assembly of two types of interphase nodes-multiprotein complexes associated with the plasma membrane that merge together and mature into the precursors of the cytokinetic contractile ring. During the long G2 phase of the cell cycle, seven different interphase node proteins maintain constant concentrations as they accumulate in proportion to cell volume. During mitosis, the total numbers of type 1 node proteins (cell cycle kinases Cdr1p, Cdr2p, Wee1p, and anillin Mid1p) are constant even when the nodes disassemble. Quantitative measurements provide strong evidence that both types of nodes have defined sizes and numbers of constituent proteins, as observed for cytokinesis nodes. Type 1 nodes assemble in two phases-a burst at the end of mitosis, followed by steady increase during interphase to double the initial number. Type 2 nodes containing Blt1p, Rho-GEF Gef2p, and kinesin Klp8p remain intact throughout the cell cycle and are constituents of the contractile ring. They are released from the contractile ring as it disassembles and then associate with type 1 nodes around the equator of the cell during interphase.","doi":"10.1091/mbc.E16-07-0522","authors":"Akamatsu M, Lin Y, Bewersdorf J, Pollard TD","authors_abbrev":"Akamatsu M et al.","pubmed_publication_date":"07 Nov 2017","pubmed_entrez_date":"2017-05-26","publication_year":"2017","canto_session_key":"450e8f96174e67ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-06-15 12:41:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-05-31 21:10:45","canto_added_date":"2017-05-27 00:15:14","annotation_curators":[],"file_curator_name":"Matthew Akamatsu","file_curator_role":"community","annotation_file_curators":[{"name":"Matthew Akamatsu","community_curator":true,"annotation_count":6,"orcid":"0000-0002-0286-5310","file_type":"quantitative_gene_expression","file_name":"PMID_28539404_Akamatsu_protein_quantitative_expression.txt"}],"genes":["SPAC57A10.02","SPAC644.06c","SPCC4B3.15","SPAC144.14","SPBC1A4.05","SPCC18B5.03"],"gene_count":6,"ltp_gene_count":0,"approved_date":"2017-05-31"},{"uniquename":"PMID:17112666","title":"Myocyte enhancing factor-2A in Alzheimer's disease: genetic analysis and association with MEF2A-polymorphisms.","citation":"Neurosci Lett 2007 Jan 03;411(1):47-51","abstract":"Polymorphisms at different genes have been proposed as determinants of the risk for developing late-onset Alzheimer's disease (LOAD). Among the several candidate genes are those that encode proteins involved in neuronal degeneration/survival. Studies of primary neuronal cultures supported that members of the myocyte enhancing factor-2 (MEF2) family of transcription factors have an anti-apoptotic effect, regulating the expression of proteins involved in neuronal survival and differentiation. We analysed the MEF2A gene in a total of 357 patients (mean age 72 years, range 60-97 years). Among others, a Pro279Leu in exon 8 and a polyglutamine (CAG) repeat polymorphisms in exon 12 were found. These variants were also genotyped in 495 healthy controls (>50 years old), and the frequencies were statistically compared. Eight patients were 279L (six P/L and two L/L), compared to only one control (2% vs. 0.2%; p=0.004, OR=11.32). There was a significantly higher frequency of 279L-carriers among APOE epsilon4+ (7/154=4.5%), compared to epsilon4- (1/203) (p=0.02). In conclusion, our work suggests that the variation at the MEF2A gene could be involved in the risk of developing LOAD. Because MEF2 has been related with neuronal survival, and the 279L allele has been related with a reduction in the transcriptional activation activity of MEF2A, the effect of this allele could be mediated through a down-regulation of antiapoptotic genes.","authors":"González P, Alvarez V, Menéndez M, Lahoz CH, Martínez C, Corao AI, Calatayud MT, Peña J, García-Castro M, Coto E","authors_abbrev":"González P et al.","pubmed_publication_date":"03 Jan 2007","pubmed_entrez_date":"2006-11-23","publication_year":"2007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11E3.06","SPBC19G7.06"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:28733396","title":"Two-Dimensional Gel Electrophoresis of DNA Replication Intermediates in  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2018 Mar 01;2018(3)","abstract":"Two-dimensional gel electrophoresis allows direct detection of DNA replication and recombination intermediates in preparations of total genomic DNA. This technique is widely used to identify replication origins in the yeast genome and is based on the different mobility in agarose gels of linear and branched DNA molecules depending on their mass and structure. During the first dimension, low-voltage and a low-percentage agarose gel favors separation of the molecules by their mass and minimizes the effect of their structure. In contrast, during the second dimension, a higher voltage, a higher percentage agarose gel, and the presence of ethidium bromide significantly delays the migration of branched structures relative to linear molecules of the same mass. This technique is appropriate for the detection of replication initiation and, therefore, an active origin of replication, within regions of approximately 2.5-5.5 kb. Consequently, it is not well suited for genome-wide replication analyses.","doi":"10.1101/pdb.prot092007","authors":"Sánchez M, Antequera F","authors_abbrev":"Sánchez M et al.","pubmed_publication_date":"01 Mar 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19096104","title":"High production of sulfide in coenzyme Q deficient fission yeast.","citation":"Biofactors 2008;32(1-4):91-8","abstract":"We have constructed coenzyme Q deficient fission yeast strains by deletion of ten different genes, all of which are absolutely required for the CoQ10 biosynthesis. We found that sulfide was highly accumulated in all fission yeast CoQ10 deficient mutants. In fission yeast sulfide is required for the synthesis of cysteine and homocysteine which are catalyzed by cysteine synthase (Cys1a) and homocysteine synthase (Met17), respectively. To better understand the relation between sulfide metabolism and coenzyme Q, we expressed cys1a, met17 and hmt2, which encodes sulfide-quinone oxidoreductase, in CoQ10 deficient mutants and other mutants, and measured the level of sulfide. Although expression of cys1a and met17 lowered sulfide production in CoQ10 deficient mutants, hmt2 did not lower the level of sulfide, because Hmt2 requires coenzyme Q for its function. In contrast, expression of hmt2 lowered sulfide production in cys1a and met17 mutants. These and other results indicate that coenzyme Q is important for sulfide oxidation through sulfide-quinone oxidoreductase to detoxify excess sulfide in fission yeast.","authors":"Zhang M, Wakitani S, Hayashi K, Miki R, Kawamukai M","authors_abbrev":"Zhang M et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-12-20","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22692683","title":"Miller (Genee-Wiedemann) syndrome represents a clinically and biochemically distinct subgroup of postaxial acrofacial dysostosis associated with partial deficiency of DHODH.","citation":"Hum Mol Genet 2012 Sep 15;21(18):3969-83","abstract":"Biallelic mutations in the gene encoding DHOdehase [dihydroorotate dehydrogenase (DHODH)], an enzyme required for de novo pyrimidine biosynthesis, have been identified as the cause of Miller (Genée-Weidemann or postaxial acrofacial dysostosis) syndrome (MIM 263750). We report compound heterozygous DHODH mutations in four additional families with typical Miller syndrome. Complementation in auxotrophic yeast demonstrated reduced pyrimidine synthesis and in vitro enzymatic analysis confirmed reduced DHOdehase activity in 11 disease-associated missense mutations, with 7 alleles showing discrepant activity between the assays. These discrepancies are partly explained by the domain structure of DHODH and suggest both assays are useful for interpretation of individual alleles. However, in all affected individuals, the genotype predicts that there should be significant residual DHOdehase activity. Urine samples obtained from two mutation-positive cases showed elevated levels of orotic acid (OA) but not dihydroorotate (DHO), an unexpected finding since these represent the product and the substrate of DHODH enzymatic activity, respectively. Screening of four unrelated cases with overlapping but atypical clinical features showed no mutations in either DHODH or the other de novo pyrimidine biosynthesis genes (CAD, UMPS), with these cases also showing normal levels of urinary OA and DHO. In situ analysis of mouse embryos showed Dhodh, Cad and Umps to be strongly expressed in the pharyngeal arch and limb bud, supporting a site- and stage-specific requirement for de novo pyrimidine synthesis. The developmental sensitivity to reduced pyrimidine synthesis capacity may reflect the requirement for an exceptional mitogenic response to growth factor signalling in the affected tissues.","doi":"10.1093/hmg/dds218","authors":"Rainger J, Bengani H, Campbell L, Anderson E, Sokhi K, Lam W, Riess A, Ansari M, Smithson S, Lees M, Mercer C, McKenzie K, Lengfeld T, Gener Querol B, Branney P, McKay S, Morrison H, Medina B, Robertson M, Kohlhase J, Gordon C, Kirk J, Wieczorek D, Fitzpatrick DR","authors_abbrev":"Rainger J et al.","pubmed_publication_date":"15 Sep 2012","pubmed_entrez_date":"2012-06-14","publication_year":"2012","canto_session_key":"8b6dcaf2931b8fc5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-05-22 08:41:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-16 15:31:24","canto_added_date":"2013-05-16 14:45:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-05-16"},{"uniquename":"PMID:22561213","title":"Replicating centromeric chromatin: spatial and temporal control of CENP-A assembly.","citation":"Exp Cell Res 2012 Jul 15;318(12):1353-60","abstract":"The centromere is the fundamental unit for insuring chromosome inheritance. This complex region has a distinct type of chromatin in which histone H3 is replaced by a structurally different homologue identified in humans as CENP-A. In metazoans, specific DNA sequences are neither required nor sufficient for centromere identity. Rather, an epigenetic mark comprised of CENP-A containing chromatin is thought to be the major determinant of centromere identity. In this view, CENP-A deposition and chromatin assembly are fundamental processes for the maintenance of centromeric identity across mitotic and meiotic divisions. Several lines of evidence support CENP-A deposition in metazoans occurring at only one time in the cell cycle. Such cell cycle-dependent loading of CENP-A is found in divergent species from human to fission yeast, albeit with differences in the cell cycle point at which CENP-A is assembled. Cell cycle dependent CENP-A deposition requires multiple assembly factors for its deposition and maintenance. This review discusses the regulation of new CENP-A deposition and its relevance to centromere identity and inheritance.","doi":"10.1016/j.yexcr.2012.04.007","authors":"Nechemia-Arbely Y, Fachinetti D, Cleveland DW","authors_abbrev":"Nechemia-Arbely Y et al.","pubmed_publication_date":"15 Jul 2012","pubmed_entrez_date":"2012-05-08","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25556969","title":"Global transcriptomic profiling of Schizosaccharomyces pombe in response to nitrosative stress.","citation":"Gene 2015 Mar 10;558(2):241-53","abstract":"Excess production of nitric oxide (NO) and reactive nitrogen intermediates (RNIs) cause nitrosative stress on cells. Schizosaccharomyces pombe was used as a model to study nitrosative stress response. This is the first report on the global gene expression profile in response to NO in S. pombe using microarray. Among the 4824 genes reported for S. pombe, 818 were differentially expressed by at least 2-fold upon NO donor treatment. We previously showed that Pap1, the Activator Protein 1 transcription factor is required to combat nitrosative stress. In this study, the transcriptional response to NO in a null mutant for pap1 identified 45 genes that seem to be controlled by Pap1. Surprisingly, Pap1 regulated genes in S. pombe were distinctly different under nitrosative stress than those reported under oxidative stress. Genes of the pathway meiosis, cell cycle, spliceosome and oxidative phosphorylation were mostly affected under nitrosative stress in the fission yeast.","doi":"10.1016/j.gene.2014.12.067","authors":"Biswas P, Ghosh S","authors_abbrev":"Biswas P et al.","pubmed_publication_date":"10 Mar 2015","pubmed_entrez_date":"2015-01-06","publication_year":"2015","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2015-01-07 01:15:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23703609","title":"TORC2 is required to maintain genome stability during S phase in fission yeast.","citation":"J Biol Chem 2013 Jul 05;288(27):19649-60","abstract":"DNA damage can occur due to environmental insults or intrinsic metabolic processes and is a major threat to genome stability. The DNA damage response is composed of a series of well coordinated cellular processes that include activation of the DNA damage checkpoint, transient cell cycle arrest, DNA damage repair, and reentry into the cell cycle. Here we demonstrate that mutant cells defective for TOR complex 2 (TORC2) or the downstream AGC-like kinase, Gad8, are highly sensitive to chronic replication stress but are insensitive to ionizing radiation. We show that in response to replication stress, TORC2 is dispensable for Chk1-mediated cell cycle arrest but is required for the return to cell cycle progression. Rad52 is a DNA repair and recombination protein that forms foci at DNA damage sites and stalled replication forks. TORC2 mutant cells show increased spontaneous nuclear Rad52 foci, particularly during S phase, suggesting that TORC2 protects cells from DNA damage that occurs during normal DNA replication. Consistently, the viability of TORC2-Gad8 mutant cells is dependent on the presence of the homologous recombination pathway and other proteins that are required for replication restart following fork replication stalling. Our findings indicate that TORC2 is required for genome integrity. This may be relevant for the growing amount of evidence implicating TORC2 in cancer development.","doi":"10.1074/jbc.M113.464974","authors":"Schonbrun M, Kolesnikov M, Kupiec M, Weisman R","authors_abbrev":"Schonbrun M et al.","pubmed_publication_date":"05 Jul 2013","pubmed_entrez_date":"2013-05-25","publication_year":"2013","canto_session_key":"65aac88117a2803a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronitt Weisman","canto_approved_date":"2015-04-27 15:06:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-24 14:58:19","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Ronitt Weisman","community_curator":true,"annotation_count":58,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPAC1851.04c","SPAC4C5.02c","SPBC30D10.10c","SPBC23E6.08","SPCC4G3.05c","SPAC3H8.05c","SPAC6B12.02c","SPAC644.14c","SPBC12C2.02c","SPAC694.06c","SPBC30D10.04","SPAC30D11.10","SPBC216.05","SPCC18B5.11c","SPCC1259.13","SPAPYUG7.02c","SPBC216.06c","SPBC1703.14c","SPBC582.05c","SPCC24B10.07"],"gene_count":21,"ltp_gene_count":21,"approved_date":"2013-09-24"},{"uniquename":"PMID:18566005","title":"Structural and functional analyses of the DMC1-M200V polymorphism found in the human population.","citation":"Nucleic Acids Res 2008 Jul;36(12):4181-90","abstract":"The M200V polymorphism of the human DMC1 protein, which is an essential, meiosis-specific DNA recombinase, was found in an infertile patient, raising the question of whether this homozygous human DMC1-M200V polymorphism may cause infertility by affecting the function of the human DMC1 protein. In the present study, we determined the crystal structure of the human DMC1-M200V variant in the octameric-ring form. Biochemical analyses revealed that the human DMC1-M200V variant had reduced stability, and was moderately defective in catalyzing in vitro recombination reactions. The corresponding M194V mutation introduced in the Schizosaccharomyces pombe dmc1 gene caused a significant decrease in the meiotic homologous recombination frequency. Together, these structural, biochemical and genetic results provide extensive evidence that the human DMC1-M200V mutation impairs its function, supporting the previous interpretation that this single-nucleotide polymorphism is a source of human infertility.","doi":"10.1093/nar/gkn362","authors":"Hikiba J, Hirota K, Kagawa W, Ikawa S, Kinebuchi T, Sakane I, Takizawa Y, Yokoyama S, Mandon-Pépin B, Nicolas A, Shibata T, Ohta K, Kurumizaka H","authors_abbrev":"Hikiba J et al.","pubmed_publication_date":"Jul 2008","pubmed_entrez_date":"2008-06-21","publication_year":"2008","canto_session_key":"97b66d126be0a391","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-05 15:16:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 15:16:18","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-05"},{"uniquename":"PMID:26359496","title":"Eisosomes Regulate Phosphatidylinositol 4,5-Bisphosphate (PI(4,5)P2) Cortical Clusters and Mitogen-activated Protein (MAP) Kinase Signaling upon Osmotic Stress.","citation":"J Biol Chem 2015 Oct 23;290(43):25960-73","abstract":"Eisosomes are multiprotein structures that generate linear invaginations at the plasma membrane of yeast cells. The core component of eisosomes, the BAR domain protein Pil1, generates these invaginations through direct binding to lipids including phosphoinositides. Eisosomes promote hydrolysis of phosphatidylinositol 4,5 bisphosphate (PI(4,5)P2) by functioning with synaptojanin, but the cellular processes regulated by this pathway have been unknown. Here, we found that PI(4,5)P2 regulation by eisosomes inhibits the cell integrity pathway, a conserved MAPK signal transduction cascade. This pathway is activated by multiple environmental conditions including osmotic stress in the fission yeast Schizosaccharomyces pombe. Activation of the MAPK Pmk1 was impaired by mutations in the phosphatidylinositol (PI) 5-kinase Its3, but this defect was suppressed by removal of eisosomes. Using fluorescent biosensors, we found that osmotic stress induced the formation of PI(4,5)P2 clusters that were spatially organized by eisosomes in both fission yeast and budding yeast cells. These cortical clusters contained the PI 5-kinase Its3 and did not assemble in the its3-1 mutant. The GTPase Rho2, an upstream activator of Pmk1, also co-localized with PI(4,5)P2 clusters under osmotic stress, providing a molecular link between these novel clusters and MAPK activation. Our findings have revealed that eisosomes regulate activation of MAPK signal transduction through the organization of cortical lipid-based microdomains.","doi":"10.1074/jbc.M115.674192","authors":"Kabeche R, Madrid M, Cansado J, Moseley JB","authors_abbrev":"Kabeche R et al.","pubmed_publication_date":"23 Oct 2015","pubmed_entrez_date":"2015-09-12","publication_year":"2015","canto_session_key":"4cac370557326a9e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-09-13 00:18:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006695","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10207075","title":"Rec8p, a meiotic recombination and sister chromatid cohesion phosphoprotein of the Rad21p family conserved from fission yeast to humans.","citation":"Mol Cell Biol 1999 May;19(5):3515-28","abstract":"Our work and that of others defined mitosis-specific (Rad21 subfamily) and meiosis-specific (Rec8 subfamily) proteins involved in sister chromatid cohesion in several eukaryotes, including humans. Mutation of the fission yeast Schizosaccharomyces pombe rec8 gene was previously shown to confer a number of meiotic phenotypes, including strong reduction of recombination frequencies in the central region of chromosome III, absence of linear element polymerization, reduced pairing of homologous chromosomes, reduced sister chromatid cohesion, aberrant chromosome segregation, defects in spore formation, and reduced spore viability. Here we extend the description of recombination reduction to the central regions of chromosomes I and II. We show at the protein level that expression of rec8 is meiosis specific and that Rec8p localizes to approximately 100 foci per prophase nucleus. Rec8p was present in an unphosphorylated form early in meiotic prophase but was phosphorylated prior to meiosis I, as demonstrated by analysis of the mei4 mutant blocked before meiosis I. Evidence for the persistence of Rec8p beyond meiosis I was obtained by analysis of the mutant mes1 blocked before meiosis II. A human gene, which we designate hrec8, showed significant primary sequence similarity to rec8 and was mapped to chromosome 14. High mRNA expression of mouse and human rec8 genes was found only in germ line cells, specifically in testes and, interestingly, in spermatids. hrec8 was also expressed at a low level in the thymus. Sequence similarity and testis-specific expression indicate evolutionarily conserved functions of Rec8p in meiosis. Possible roles of Rec8p in the integration of different meiotic events are discussed.","authors":"Parisi S, McKay MJ, Molnar M, Thompson MA, van der Spek PJ, van Drunen-Schoenmaker E, Kanaar R, Lehmann E, Hoeijmakers JH, Kohli J","authors_abbrev":"Parisi S et al.","pubmed_publication_date":"May 1999","pubmed_entrez_date":"1999-04-17","publication_year":"1999","canto_session_key":"35d761b3ba38e2ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-18 16:08:16","canto_approved_date":"2022-09-18 16:08:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-18 16:08:10","canto_added_date":"2012-02-24 05:52:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-09-18"},{"uniquename":"PMID:10718196","title":"mRNAs encoding zinc finger protein isoforms are expressed by alternative splicing of an in-frame intron in fission yeast.","citation":"DNA Res 2000 Feb 28;7(1):27-30","abstract":"We report here that a gene encoding a protein with three zinc fingers is expressed predominantly to produce a protein containing only two zinc fingers in the fission yeast Schizosaccharomyces pombe. A third zinc finger resides within the in-frame intron that is normally spliced out. By RT-PCR analysis, we detected a minor transcript encoding a protein with three zinc fingers. Such alternative splicing for assortment of zinc finger domains have been reported in animals and implicated in switching of the target genes expressed specifically during development. This is the first report of the occurrence of such zinc finger assortment in lower eucaryotes.","authors":"Okazaki K, Niwa O","authors_abbrev":"Okazaki K et al.","pubmed_publication_date":"28 Feb 2000","pubmed_entrez_date":"2000-03-16","publication_year":"2000","canto_session_key":"260b0436e133fc19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-05-25 15:42:26","canto_approved_date":"2018-05-25 15:42:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-24 13:27:09","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-05-25"},{"uniquename":"PMID:15525673","title":"The A78V mutation in the Mad3-like domain of Schizosaccharomyces pombe Bub1p perturbs nuclear accumulation and kinetochore targeting of Bub1p, Bub3p, and Mad3p and spindle assembly checkpoint function.","citation":"Mol Biol Cell 2005 Jan;16(1):385-95","abstract":"During mitosis, the spindle assembly checkpoint (SAC) responds to faulty attachments between kinetochores and the mitotic spindle by imposing a metaphase arrest until the defect is corrected, thereby preventing chromosome missegregation. A genetic screen to isolate SAC mutants in fission yeast yielded point mutations in three fission yeast SAC genes: mad1, bub3, and bub1. The bub1-A78V mutant is of particular interest because it produces a wild-type amount of protein that is mutated in the conserved but uncharacterized Mad3-like region of Bub1p. Characterization of mutant cells demonstrates that the alanine at position 78 in the Mad3-like domain of Bub1p is required for: 1) cell cycle arrest induced by SAC activation; 2) kinetochore accumulation of Bub1p in checkpoint-activated cells; 3) recruitment of Bub3p and Mad3p, but not Mad1p, to kinetochores in checkpoint-activated cells; and 4) nuclear accumulation of Bub1p, Bub3p, and Mad3p, but not Mad1p, in cycling cells. Increased targeting of Bub1p-A78V to the nucleus by an exogenous nuclear localization signal does not significantly increase kinetochore localization or SAC function, but GFP fused to the isolated Bub1p Mad 3-like accumulates in the nucleus. These data indicate that Bub1p-A78V is defective in both nuclear accumulation and kinetochore targeting and that a threshold level of nuclear Bub1p is necessary for the nuclear accumulation of Bub3p and Mad3p.","authors":"Kadura S, He X, Vanoosthuyse V, Hardwick KG, Sazer S","authors_abbrev":"Kadura S et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-11-05","publication_year":"2005","canto_session_key":"fe51b7d89bf7e586","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23H3.08c","SPCC1322.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU010497","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22533924","title":"EnzML: multi-label prediction of enzyme classes using InterPro signatures.","citation":"BMC Bioinformatics 2012 Apr 25;13:61","abstract":"Manual annotation of enzymatic functions cannot keep up with automatic genome sequencing. In this work we explore the capacity of InterPro sequence signatures to automatically predict enzymatic function.\nWe present EnzML, a multi-label classification method that can efficiently account also for proteins with multiple enzymatic functions: 50,000 in UniProt. EnzML was evaluated using a standard set of 300,747 proteins for which the manually curated Swiss-Prot and KEGG databases have agreeing Enzyme Commission (EC) annotations. EnzML achieved more than 98% subset accuracy (exact match of all correct Enzyme Commission classes of a protein) for the entire dataset and between 87 and 97% subset accuracy in reannotating eight entire proteomes: human, mouse, rat, mouse-ear cress, fruit fly, the S. pombe yeast, the E. coli bacterium and the M. jannaschii archaebacterium. To understand the role played by the dataset size, we compared the cross-evaluation results of smaller datasets, either constructed at random or from specific taxonomic domains such as archaea, bacteria, fungi, invertebrates, plants and vertebrates. The results were confirmed even when the redundancy in the dataset was reduced using UniRef100, UniRef90 or UniRef50 clusters.\nInterPro signatures are a compact and powerful attribute space for the prediction of enzymatic function. This representation makes multi-label machine learning feasible in reasonable time (30 minutes to train on 300,747 instances with 10,852 attributes and 2,201 class values) using the Mulan Binary Relevance Nearest Neighbours algorithm implementation (BR-kNN).","doi":"10.1186/1471-2105-13-61","authors":"De Ferrari L, Aitken S, van Hemert J, Goryanin I","authors_abbrev":"De Ferrari L et al.","pubmed_publication_date":"25 Apr 2012","pubmed_entrez_date":"2012-04-27","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26539043","title":"Screening Molecular Chaperones Similar to Small Heat Shock Proteins in Schizosaccharomyces pombe.","citation":"Mycobiology 2015 Sep;43(3):272-9","abstract":"To screen molecular chaperones similar to small heat shock proteins (sHsps), but without α-crystalline domain, heat-stable proteins from Schizosaccharomyces pombe were analyzed by 2-dimensional electrophoresis and matrix assisted laser desorption/ionization time-of-flight mass spectrometry. Sixteen proteins were identified, and four recombinant proteins, including cofilin, NTF2, pyridoxin biosynthesis protein (Snz1) and Wos2 that has an α-crystalline domain, were purified. Among these proteins, only Snz1 showed the anti-aggregation activity against thermal denaturation of citrate synthase. However, pre-heating of NTF2 and Wos2 at 70℃ for 30 min, efficiently prevented thermal aggregation of citrate synthase. These results indicate that Snz1 and NTF2 possess molecular chaperone activity similar to sHsps, even though there is no α-crystalline domain in their sequences.","doi":"10.5941/MYCO.2015.43.3.272","authors":"Han J, Kim K, Lee S","authors_abbrev":"Han J et al.","pubmed_publication_date":"Sep 2015","pubmed_entrez_date":"2015-11-06","publication_year":"2015","canto_session_key":"560240c2e986c309","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-11-07 01:19:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9E9.13","SPAC29B12.04"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:15743828","title":"RNA interference (RNAi)-dependent and RNAi-independent association of the Chp1 chromodomain protein with distinct heterochromatic loci in fission yeast.","citation":"Mol Cell Biol 2005 Mar;25(6):2331-46","abstract":"The establishment of centromeric heterochromatin in the fission yeast Schizosaccharomyces pombe is dependent on the RNA interference (RNAi) pathway. Dicer cleaves centromeric transcripts to produce short interfering RNAs (siRNAs) that actively recruit components of heterochromatin to centromeres. Both centromeric siRNAs and the heterochromatin component Chp1 are components of the RITS (RNA-induced initiation of transcriptional gene silencing) complex, and the association of RITS with centromeres is linked to Dicer activity. In turn, centromeric binding of RITS promotes Clr4-mediated methylation of histone H3 lysine 9 (K9), recruitment of Swi6, and formation of heterochromatin. Similar to centromeres, the mating type locus (Mat) is coated in K9-methylated histone H3 and is bound by Swi6. Here we report that Chp1 associates with the mating type locus and telomeres and that Chp1 localization to heterochromatin depends on its chromodomain and the C-terminal domain of the protein. Another protein component of the RITS complex, Tas3, also binds to Mat and telomeres. Tas3 interacts with Chp1 through the C-terminal domain of Chp1, and this interaction is necessary for Tas3 stability. Interestingly, in cells lacking the Argonaute (Ago1) protein component of the RITS complex, or lacking Dicer (and hence siRNAs), Chp1 and Tas3 can still bind to noncentromeric loci, although their association with centromeres is lost. Thus, Chp1 and Tas3 exist as an Ago1-independent subcomplex that associates with noncentromeric heterochromatin independently of the RNAi pathway.","authors":"Petrie VJ, Wuitschick JD, Givens CD, Kosinski AM, Partridge JF","authors_abbrev":"Petrie VJ et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-03-04","publication_year":"2005","canto_session_key":"5254065d0b16e9e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-29 22:03:42","canto_approved_date":"2025-09-03 14:14:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-29 21:01:47","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.11","SPCC188.13c","SPAC18G6.02c","SPBC83.03c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-02-29"},{"uniquename":"PMID:15667320","title":"Glucose sensing via the protein kinase A pathway in Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 2005 Feb;33(Pt 1):257-60","abstract":"The fission yeast Schizosaccharomyces pombe primarily detects glucose via a cAMP-signalling pathway. Components of this pathway include the Git3 G-protein-coupled receptor and a heterotrimeric G-protein, from which the Gpa2 Galpha subunit activates adenylate cyclase (Git2/Cyr1). Three additional proteins, Git1, Git7 and Git10 are required to generate a cAMP response even in a strain expressing an activated form of Gpa2, which is capable of bypassing the loss of the GPCR and Gbetagamma dimer. Therefore, Git1, Git7 and Git10 either act in a G-protein-independent manner or are required to stabilize or assemble a functional signalling complex. Although prior data suggested that the Cgs2 cAMP phosphodiesterase (PDE) does not regulate the cAMP response, we now have evidence that along with adenylate cyclase regulation, PDE activation is important for limiting the response to glucose. Finally, regulation of protein kinase A activation appears to involve both traditional post-translational regulation of the function of the components of the cAMP pathway and glucose-dependent transcriptional regulation of some of these cAMP pathway genes.","authors":"Hoffman CS","authors_abbrev":"Hoffman CS","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2005-01-26","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23H3.13c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:9755167","title":"The role of the destruction box and its neighbouring lysine residues in cyclin B for anaphase ubiquitin-dependent proteolysis in fission yeast: defining the D-box receptor.","citation":"EMBO J 1998 Oct 01;17(19):5670-8","abstract":"Programmed proteolysis of proteins such as mitotic cyclins and Cut2/Pds1p requires a 9-residue conserved motif known as the destruction box (D-box). Strong expression of protein fragments containing destruction boxes, such as the first 70 residues of Cdc13 (N70), inhibits the growth of Schizosaccharomyces pombe at metaphase. This inhibition can be overcome either by removal of all lysine residues from N70 using site-directed mutagenesis (K0-N70) or by raising the concentration of intracellular ubiquitin. Consistent with the idea that competition for ubiquitin accounts for some of its inhibitory effects, wild-type N70 not only stabilized D-box proteins, but also Rum1 and Cdc18, which are degraded by a different pathway. The K0-N70 construct was neither polyubiquitinated nor degraded in vitro, but it blocked the growth of strains of yeast in which anaphase-promoting complex/cyclosome (APC/C) function was compromised by mutation, and specifically inhibited proteolysis of APC/C substrates in vivo. Both K0-N70 and 20-residue D-box peptides blocked polyubiquitination of other D-box-containing substrates in a cell-free ubiquitination assay system. These data suggest the existence of a D-box receptor protein that recognizes D-boxes prior to ubiquitination.","authors":"Yamano H, Tsurumi C, Gannon J, Hunt T","authors_abbrev":"Yamano H et al.","pubmed_publication_date":"01 Oct 1998","pubmed_entrez_date":"1998-10-02","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F12.15c","SPAC17C9.01c","SPBC582.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:19931410","title":"Checkpoint kinase 1 modulates sensitivity to cisplatin after spindle checkpoint activation in SW620 cells.","citation":"Int J Biochem Cell Biol 2010 Feb;42(2):318-28","abstract":"Aneuploidy is a common feature of tumours that arise by errors in chromosome segregation during mitosis. The aim of this study was to evaluate possible signaling pathways involved in sensitization to chemotherapy in cells with chromosomal instability. We designed a screen using the fission yeast Squizossaccharomyces pombe, to isolate strains showing a phenotype of chromosome mis-segregation and higher sensitivity to the antitumoral drug Bleomycin. We examined differences in gene expression using a comparative analysis of genome-wide expression of the wild type strain and one of the mutants. The results revealed a set of genes involved in cell cycle control, including Mad3/BubR1 and Chk1. We then studied the levels of these two proteins in colorectal cancer human cell lines with different genomic content. Among these, SW620 cells showed higher BubR1 and Chk1 mRNA levels than control cells under normal conditions. Since Chk1 is required for both S and G2/M checkpoints, and the microtubule-destabilizing agent, nocodazole induces mitotic arrest, we attempted to investigate the potential anticancer effects of nocodazole in combination with cisplatin. These studies showed that SW620 cells undergo synergistic cell death after spindle checkpoint activation followed by cisplatin treatment, suggesting a role of Chk1 in this checkpoint, very likely dependent on BubR1 protein. Importantly, Chk1-depleted SW620 cells lost this synergistic effect. In summary, we propose that Chk1 could be a biomarker predictive of the efficacy of chemotherapy across different types of tumors with aneuploidy. These findings may be potentially very useful for the stratification of patients for treatment.","doi":"10.1016/j.biocel.2009.11.011","authors":"Peralta-Sastre A, Manguan-Garcia C, de Luis A, Belda-Iniesta C, Moreno S, Perona R, Sanchez-Perez I","authors_abbrev":"Peralta-Sastre A et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2009-11-26","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26864000","title":"Alp7/TACC-Alp14/TOG generates long-lived, fast-growing MTs by an unconventional mechanism.","citation":"Sci Rep 2016 Feb 11;6:20653","abstract":"Alp14 is a TOG-family microtubule polymerase from S. pombe that tracks plus ends and accelerates their growth. To interrogate its mechanism, we reconstituted dynamically unstable single isoform S. pombe microtubules with full length Alp14/TOG and Alp7, the TACC-family binding partner of Alp14. We find that Alp14 can drive microtubule plus end growth at GTP-tubulin concentrations at least 10-fold below the usual critical concentration, at the expense of increased catastrophe. This reveals Alp14 to be a highly unusual enzyme that biases the equilibrium for the reaction that it catalyses. Alp7/TACC enhances the effectiveness of Alp14, by increasing its occupancy. Consistent with this, we show in live cells that Alp7 deletion produces very similar MT dynamics defects to Alp14 deletion. The ability of Alp7/14 to accelerate and bias GTP-tubulin exchange at microtubule plus ends allows it to generate long-lived, fast-growing microtubules at very low cellular free tubulin concentrations.","doi":"10.1038/srep20653","authors":"Hussmann F, Drummond DR, Peet DR, Martin DS, Cross RA","authors_abbrev":"Hussmann F et al.","pubmed_publication_date":"11 Feb 2016","pubmed_entrez_date":"2016-02-12","publication_year":"2016","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-14 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC800.05c","SPBC26H8.07c","SPCC895.07","SPBC16A3.15c","SPAC890.02c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:28934593","title":"Big Lessons from Little Yeast: Budding and Fission Yeast Centrosome Structure, Duplication, and Function.","citation":"Annu Rev Genet 2017 Nov 27;51:361-383","abstract":"Centrosomes are a functionally conserved feature of eukaryotic cells that play an important role in cell division. The conserved γ-tubulin complex organizes spindle and astral microtubules, which, in turn, separate replicated chromosomes accurately into daughter cells. Like DNA, centrosomes are duplicated once each cell cycle. Although in some cell types it is possible for cell division to occur in the absence of centrosomes, these divisions typically result in defects in chromosome number and stability. In single-celled organisms such as fungi, centrosomes [known as spindle pole bodies (SPBs)] are essential for cell division. SPBs also must be inserted into the membrane because fungi undergo a closed mitosis in which the nuclear envelope (NE) remains intact. This poorly understood process involves events similar or identical to those needed for de novo nuclear pore complex assembly. Here, we review how analysis of fungal SPBs has advanced our understanding of centrosomes and NE events.","doi":"10.1146/annurev-genet-120116-024733","authors":"Cavanaugh AM, Jaspersen SL","authors_abbrev":"Cavanaugh AM et al.","pubmed_publication_date":"27 Nov 2017","pubmed_entrez_date":"2017-09-22","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-09-23 00:15:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC8D2.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12734020","title":"Domain fusion analysis by applying relational algebra to protein sequence and domain databases.","citation":"BMC Bioinformatics 2003 May 06;4:16","abstract":"Domain fusion analysis is a useful method to predict functionally linked proteins that may be involved in direct protein-protein interactions or in the same metabolic or signaling pathway. As separate domain databases like BLOCKS, PROSITE, Pfam, SMART, PRINTS-S, ProDom, TIGRFAMs, and amalgamated domain databases like InterPro continue to grow in size and quality, a computational method to perform domain fusion analysis that leverages on these efforts will become increasingly powerful.\nThis paper proposes a computational method employing relational algebra to find domain fusions in protein sequence databases. The feasibility of this method was illustrated on the SWISS-PROT+TrEMBL sequence database using domain predictions from the Pfam HMM (hidden Markov model) database. We identified 235 and 189 putative functionally linked protein partners in H. sapiens and S. cerevisiae, respectively. From scientific literature, we were able to confirm many of these functional linkages, while the remainder offer testable experimental hypothesis. Results can be viewed at http://calcium.uhnres.utoronto.ca/pi.\nAs the analysis can be computed quickly on any relational database that supports standard SQL (structured query language), it can be dynamically updated along with the sequence and domain databases, thereby improving the quality of predictions over time.","authors":"Truong K, Ikura M","authors_abbrev":"Truong K et al.","pubmed_publication_date":"06 May 2003","pubmed_entrez_date":"2003-05-08","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6887245","title":"Cell division cycle genes nda2 and nda3 of the fission yeast Schizosaccharomyces pombe control microtubular organization and sensitivity to anti-mitotic benzimidazole compounds.","citation":"J Mol Biol 1983 Aug 05;168(2):271-84","abstract":"Two genes, nda2 and nda3, previously defined by cold sensitive nuclear division arrest (nda) mutations in the fission yeast Schizosaccharomyces pombe were studied. A mutant nda2-KM52 was found to be supersensitive (at the permissive temperature) to the tubulin-binding drugs such as thiabendazole, methylbenzimidazol-2yl carbamate and nocodazole. A single mutation in nda2 appears to cause both drug supersensitivity and cold sensitivity. The defective phenotypes of nda2-KM52 with a low concentration of the drugs were characterized by nuclear displacement and anomalously situated spindle pole bodies. The allele of the other mutant, nda3-KM311, was sh216 to be linked closely to the ben1 locus, which determines resistance to the drug. The identity of ben1 and nda3 genes was proved by a newly isolated mutant ben1-TB1005; it manifests ben1 resistance and the cold sensitive nda3 phenotype. At 22 degrees C, ben1-TB1005 showed cell branching and deformation characteristic of nda3-KM311. Eleven mutants supersensitive to thiabendazole were newly isolated by replica plating. Four strains were mapped in nda2, while the other four were in nda3. Most of the isolated mutants were blocked at nuclear division in the presence of a low concentration of the drug. Thus, the products of genes nda2 and nda3 (ben1) interact directly or indirectly with the drugs and control, in different ways, microtubular organization in the cells of S. pombe.","authors":"Umesono K, Toda T, Hayashi S, Yanagida M","authors_abbrev":"Umesono K et al.","pubmed_publication_date":"05 Aug 1983","pubmed_entrez_date":"1983-08-05","publication_year":"1983","canto_session_key":"652ccd500039fcac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-09 18:28:20","canto_approved_date":"2024-09-28 14:09:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-20 15:15:13","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPBC26H8.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-02-09"},{"uniquename":"PMID:11516965","title":"Cell polarity: a tale of two Ts.","citation":"Curr Biol 2001 Aug 07;11(15):R600-2","abstract":"The microtubule cytoskeleton plays an important role in cell polarity. Central to this process in fission yeast is tea1p, a marker of polarized cell growth that is delivered to the cell surface in a microtubule-dependent fashion. Recent studies suggest that the actin-binding protein bud6p may be a tea1p effector.","authors":"Verde F","authors_abbrev":"Verde F","pubmed_publication_date":"07 Aug 2001","pubmed_entrez_date":"2001-08-23","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35012333","title":"Cleavage-Polyadenylation Factor Cft1 and SPX Domain Proteins Are Agents of Inositol Pyrophosphate Toxicosis in Fission Yeast.","citation":"mBio 2022 Feb 22;13(1):e0347621","abstract":"Inositol pyrophosphate (IPP) dynamics govern expression of the fission yeast phosphate homeostasis regulon via their effects on lncRNA-mediated transcription interference. The growth defects (ranging from sickness to lethality) elicited by fission yeast mutations that inactivate IPP pyrophosphatase enzymes are exerted via the agonistic effects of too much 1,5-IP8 on RNA 3'-processing and transcription termination. To illuminate determinants of IPP toxicosis, we conducted a genetic screen for spontaneous mutations that suppressed the sickness of Asp1 pyrophosphatase mutants. We identified a missense mutation, C823R, in the essential Cft1 subunit of the cleavage and polyadenylation factor complex that suppresses even lethal Asp1 IPP pyrophosphatase mutations, thereby fortifying the case for 3'-processing/termination as the target of IPP toxicity. The suppressor screen also identified Gde1 and Spx1 (SPAC6B12.07c), both of which have an IPP-binding SPX domain and both of which are required for lethality elicited by Asp1 mutations. A survey of other SPX proteins in the proteome identified the Vtc4 and Vtc2 subunits of the vacuolar polyphosphate polymerase as additional agents of IPP toxicosis. Gde1, Spx1, and Vtc4 contain enzymatic modules (glycerophosphodiesterase, RING finger ubiquitin ligase, and polyphosphate polymerase, respectively) fused to their IPP-sensing SPX domains. Structure-guided mutagenesis of the IPP-binding sites and the catalytic domains of Gde1 and Spx1 indicated that both modules are necessary to elicit IPP toxicity. Whereas Vtc4 polymerase catalytic activity is required for IPP toxicity, its IPP-binding site is not. Epistasis analysis, transcriptome profiling, and assays of Pho1 expression implicate Spx1 as a transducer of IP8 signaling to the 3'-processing/transcription termination machinery.  IMPORTANCE  Impeding the catabolism of the inositol pyrophosphate (IPP) signaling molecule IP8 is cytotoxic to fission yeast. Here, by performing a genetic suppressor screen, we identified several cellular proteins required for IPP toxicosis. Alleviation of IPP lethality by a missense mutation in the essential Cft1 subunit of the cleavage and polyadenylation factor consolidates previous evidence that toxicity results from IP8 action as an agonist of RNA 3'-processing and transcription termination. Novel findings are that IP8 toxicity depends on IPP-sensing SPX domain proteins with associated enzymatic functions: Gde1 (glycerophosphodiesterase), Spx1 (ubiquitin ligase), and Vtc2/4 (polyphosphate polymerase). The effects of Spx1 deletion on phosphate homeostasis imply a role for Spx1 in communicating an IP8-driven signal to the transcription and RNA processing apparatus.","doi":"10.1128/mbio.03476-21","authors":"Schwer B, Garg A, Sanchez AM, Bernstein MA, Benjamin B, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"22 Feb 2022","pubmed_entrez_date":"2022-01-11","publication_year":"2022","canto_session_key":"4228fd893e7a1a88","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2022-12-01 11:35:44","canto_approved_date":"2025-09-04 12:46:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-11-23 22:03:45","canto_added_date":"2022-01-13 01:15:04","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":151,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.14c","SPCC1672.06c","SPBC3B8.04c","SPCC74.02c","SPAC14C4.11","SPAPB1E7.05","SPAC222.09","SPBC776.02c","SPBC337.03","SPBC16H5.10c","SPAC6B12.07c","SPBC1271.09","SPBC8E4.01c","SPBP4G3.02","SPAC13G6.14","SPAC824.04","SPBC1709.08","SPAC3G9.04","SPCC1827.07c","SPBC3B9.11c","SPBPB8B6.04c","SPBC28F2.12"],"gene_count":22,"ltp_gene_count":19,"approved_date":"2022-12-01"},{"uniquename":"PMID:31768981","title":"Comparative Poly(A)+ RNA Interactome Capture of RNA Surveillance Mutants.","citation":"Methods Mol Biol 2020;2062:255-276","abstract":"RNA exosome complexes degrade many different RNA substrates. Substrate selection and targeting to the exosome complex rely on cofactors, which bind to the substrate RNA, recruit the exosome complex, and help to remodel the associated ribonucleoprotein particle to facilitate RNA degradation. These cofactors are RNA-binding proteins, but their interaction with RNA may be very transient because the RNAs they are bound to are rapidly turned over by the exosome complex. Hence, the cofactors involved in the degradation of many exosome substrates are unknown. Here, we describe comparative poly(A)+ RNA interactome capture as a method to screen for novel RNA-binding proteins involved in exosome-dependent RNA decay.For this, we compare the poly(A)+ RNA interactome of wild-type cells to that of RNA surveillance mutants, where the decay of exosome substrates is compromised and occupancy of exosome cofactors on RNA is strongly increased. More specifically, protein-RNA complexes in wild-type and mutant cells are UV-cross-linked in vivo after labeling with the photoactivatable nucleoside analogue 4-thiouracil. Following cell lysis, protein-RNA complexes are selected on oligo d(T) beads, subjected to stringent washes, and eluted in a low salt buffer. After RNase digestion of cross-linked RNA, RNA-binding proteins that are enriched in the mutant samples are identified by quantitative mass spectrometry. Here, we quantitatively compare the RNA-protein interactomes of wild-type and rrp6Δ cells to selectively determine cofactors of the nuclear RNA exosome complex in fission yeast. With minor modifications, the comparative interactome approach can easily be adapted to study a range of different RNA-dependent processes in various cellular systems.","doi":"10.1007/978-1-4939-9822-7_13","authors":"Kilchert C, Hester S, Castello A, Mohammed S, Vasiljeva L","authors_abbrev":"Kilchert C et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2019-11-27","publication_year":"2020","canto_session_key":"876a380ec9934901","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-11-28 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25916716","title":"Analyzing the Response to Dysfunction Replication Forks Using the RTS1 Barrier System in Fission Yeast.","citation":"Methods Mol Biol 2015;1300:239-59","abstract":"The study of how eukaryotic cells overcome problems associated with dysfunctional DNA replication forks is assisted by experimental systems that allow site-specific replication fork arrest. Here we provide protocols for the use of the fission yeast RTS1 replication fork barrier. The RTS1 barrier is a directional, or polar, replication fork barrier that evolved to ensure directional replication of the fission yeast mating-type locus. We have moved the 859 bp RTS1 sequence to another locus in the genome and demonstrated that it arrests replication forks in a dysfunctional confirmation and that replication is restarted within ~20 min by the action of homologous recombination. We describe here the barrier constructs currently available, the methods by which we regulate the activity of the barrier, how to synchronize cells for analysis of replication intermediates by 2D gel electrophoresis, and the use of a replication slippage assay to measure fork fidelity.","doi":"10.1007/978-1-4939-2596-4_15","authors":"Mohebi S, Lambert SA, Carr AM","authors_abbrev":"Mohebi S et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-04-29","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-04-30 00:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23936535","title":"Slx8 removes Pli1-dependent protein-SUMO conjugates including SUMOylated topoisomerase I to promote genome stability.","citation":"PLoS One 2013;8(8):e71960","abstract":"The SUMO-dependent ubiquitin ligase Slx8 plays key roles in promoting genome stability, including the processing of trapped Topoisomerase I (Top1) cleavage complexes and removal of toxic SUMO conjugates. We show that it is the latter function that constitutes Slx8's primary role in fission yeast. The SUMO conjugates in question are formed by the SUMO ligase Pli1, which is necessary for limiting spontaneous homologous recombination when Top1 is present. Surprisingly there is no requirement for Pli1 to limit recombination in the vicinity of a replication fork blocked at the programmed barrier RTS1. Notably, once committed to Pli1-mediated SUMOylation Slx8 becomes essential for genotoxin resistance, limiting both spontaneous and RTS1 induced recombination, and promoting normal chromosome segregation. We show that Slx8 removes Pli1-dependent Top1-SUMO conjugates and in doing so helps to constrain recombination at RTS1. Overall our data highlight how SUMOylation and SUMO-dependent ubiquitylation by the Pli1-Slx8 axis contribute in different ways to maintain genome stability.","doi":"10.1371/journal.pone.0071960","authors":"Steinacher R, Osman F, Lorenz A, Bryer C, Whitby MC","authors_abbrev":"Steinacher R et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-08-13","publication_year":"2013","canto_session_key":"f8fb1428c5594330","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1703.14c","SPBC3D6.11c","SPAC1687.05","SPAC16A10.06c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:12620220","title":"The telomere protein Taz1 is required to prevent and repair genomic DNA breaks.","citation":"Mol Cell 2003 Feb;11(2):303-13","abstract":"One fundamental function of telomeres is to prevent the ends of chromosomes from being sensed and treated as DNA damage. Here we present evidence for additional roles of telomeres in promoting proper chromosome segregation and DNA repair. We find that the fission yeast telomere protein Taz1p is required for cell cycle progression at 20 degrees C, a temperature at which taz1Delta cells exhibit a G(2)/M DNA damage checkpoint delay, chromosome missegregation, and DNA double-strand breaks (DSBs). Spindle assembly checkpoint components and a checkpoint-independent function of Rad3p are required for taz1Delta cells to survive at 20 degrees C. Disruption of topoisomerase II activity suppresses the cold sensitivity of taz1Delta cells, suggesting a scenario in which telomeric entanglement is the primary defect. Furthermore, hypersensitivity to treatments that induce DSBs suggests that Taz1p is involved in DSB repair. Our observations imply roles for Taz1p-containing telomeres in preventing and repairing DNA breaks throughout the genome.","authors":"Miller KM, Cooper JP","authors_abbrev":"Miller KM et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-03-07","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1322.12c","SPCC1259.13","SPBC1A4.03c","SPCC18B5.11c","SPBC106.01","SPAC16A10.07c","SPAC30D11.10","SPBC216.05"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:32461373","title":"Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches.","citation":"Proc Natl Acad Sci U S A 2020 Jun 16;117(24):13519-13528","abstract":"Networks of branched actin filaments formed by Arp2/3 complex generate and experience mechanical forces during essential cellular functions, including cell motility and endocytosis. External forces regulate the assembly and architecture of branched actin networks both in vitro and in cells. Considerably less is known about how mechanical forces influence the disassembly of actin filament networks, specifically, the dissociation of branches. We used microfluidics to apply force to branches formed from purified muscle actin and fission yeast Arp2/3 complex and observed debranching events in real time with total internal reflection fluorescence microscopy. Low forces in the range of 0 pN to 2 pN on branches accelerated their dissociation from mother filaments more than two orders of magnitude, from hours to <1 min. Neither force on the mother filament nor thermal fluctuations in mother filament shape influenced debranching. Arp2/3 complex at branch junctions adopts two distinct mechanical states with different sensitivities to force, which we name \"young/strong\" and \"old/weak.\" The \"young/strong\" state 1 has adenosine 5'-diphosphate (ADP)-P   i   bound to Arp2/3 complex. Phosphate release converts Arp2/3 complex into the \"old/weak\" state 2 with bound ADP, which is 20 times more sensitive to force than state 1. Branches with ADP-Arp2/3 complex are more sensitive to debranching by fission yeast GMF (glia maturation factor) than branches with ADP-P   i   -Arp2/3 complex. These findings suggest that aging of branch junctions by phosphate release from Arp2/3 complex and mechanical forces contribute to disassembling \"old\" actin filament branches in cells.","doi":"10.1073/pnas.1911183117","authors":"Pandit NG, Cao W, Bibeau J, Johnson-Chavarria EM, Taylor EW, Pollard TD, De La Cruz EM","authors_abbrev":"Pandit NG et al.","pubmed_publication_date":"16 Jun 2020","pubmed_entrez_date":"2020-05-29","publication_year":"2020","canto_session_key":"ac6c761c2aa0cb15","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-05-30 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR12092","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:19238","HGNC:9070","SPCPB16A4.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35770329","title":"Transcription factor Atf1-dependent degradation of the mitotic cyclin Cdc13 is regulated by multiple factors in Schizosaccharomyces pombe.","citation":"FEBS Lett 2022 Aug;596(16):2021-2030","abstract":"The bZIP transcription factor Atf1 is a key player in the transcriptional programme of Schizosaccharomyces pombe cell cycle. It also controls both expression and degradation of mitotic cyclin Cdc13. Temporal regulation of these opposing functions of Atf1 is critical for fidelity of cell division. Our investigations revealed that an increase in the activity of mitogen-activated protein kinase (MAPK) Spc1 during mitotic exit and the consequent phosphorylation of Atf1 along with the prevailing high activity of cyclin-dependent kinase Cdc2 regulate Cdc13 degradation. Our results also indicate the possibility of a complex interplay between Cdc2 inhibitory kinase Wee1, the anaphase-promoting complex and Atf1 during mitotic exit. These observations provide evidence of new regulatory mechanisms of mitotic exit.","doi":"10.1002/1873-3468.14439","authors":"Basu S, Ghosh P, Ghosal A, Datta S, Sundaram G","authors_abbrev":"Basu S et al.","pubmed_publication_date":"Aug 2022","pubmed_entrez_date":"2022-06-30","publication_year":"2022","canto_session_key":"ddcfec93cb7f8e86","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-07-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPBC582.03","SPBC887.22"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:15132994","title":"Recruitment of NIMA kinase shows that maturation of the S. pombe spindle-pole body occurs over consecutive cell cycles and reveals a role for NIMA in modulating SIN activity.","citation":"Genes Dev 2004 May 01;18(9):1007-21","abstract":"Mitotic exit in Saccharomyces cerevisiae and septation in Schizosaccharomyces pombe are regulated by a conserved signaling network called the mitotic exit and septum initiation networks (SIN), respectively. The network is active on one of the two anaphase B spindle-pole bodies (SPBs). Whereas the inherent asymmetry of growth by budding accounts for elements of the asymmetry in S. cerevisiae, it has been unclear how, or why, the pathway is asymmetric in S. pombe. We show that elements of SPB duplication in S. pombe are conservative, and that the SIN is active on the new SPB. SIN association with the new SPB persists after transient depolymerization of microtubules. The localization of the NIMA-related kinase, Fin1, reveals further complexity in SPB inheritance. Fin1 associates with the SPB bearing the older components in all cells and with the \"new\" SPB in half of the population. Fin1 only binds the new SPB when this new SPB has arisen from the duplication of an SPB that is two or more cycles old. Thus, each of the four SPBs generated over two consecutive cell cycles are different, because they have distinct fates in the next cell cycle. Fin1 binds the SPB once the SIN is active and the association requires the SIN inhibitors Byr4 and Cdc16. Fin1 physically associates with Byr4. Compromising Fin1 function leads to SIN activation on both anaphase B SPBs and promotes septation, indicating that Fin1 restrains SIN activity on the old SPB.","authors":"Grallert A, Krapp A, Bagley S, Simanis V, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"01 May 2004","pubmed_entrez_date":"2004-05-11","publication_year":"2004","canto_session_key":"477003fc9090fdf9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-03 07:09:17","canto_approved_date":"2022-08-29 15:06:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-12 11:58:10","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC222.10c","SPCC1739.11c","SPBC244.01c","SPAC6F6.08c","SPAC19E9.02"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2021-01-03"},{"uniquename":"PMID:18399939","title":"Polarized growth in fungi--interplay between the cytoskeleton, positional markers and membrane domains.","citation":"Mol Microbiol 2008 May;68(4):813-26","abstract":"One kind of the most extremely polarized cells in nature are the indefinitely growing hyphae of filamentous fungi. A continuous flow of secretion vesicles from the hyphal cell body to the growing hyphal tip is essential for cell wall and membrane extension. Because microtubules (MT) and actin, together with their corresponding motor proteins, are involved in the process, the arrangement of the cytoskeleton is a crucial step to establish and maintain polarity. In Saccharomyces cerevisiae and Schizosaccharomyces pombe, actin-mediated vesicle transportation is sufficient for polar cell extension, but in S. pombe, MTs are in addition required for the establishment of polarity. The MT cytoskeleton delivers the so-called cell-end marker proteins to the cell pole, which in turn polarize the actin cytoskeleton. Latest results suggest that this scenario may principally be conserved from S. pombe to filamentous fungi. In addition, in filamentous fungi, MTs could provide the tracks for long-distance vesicle movement. In this review, we will compare the interaction of the MT and the actin cytoskeleton and their relation to the cortex between yeasts and filamentous fungi. In addition, we will discuss the role of sterol-rich membrane domains in combination with cell-end marker proteins for polarity establishment.","doi":"10.1111/j.1365-2958.2008.06193.x","authors":"Fischer R, Zekert N, Takeshita N","authors_abbrev":"Fischer R et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-04-11","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9258671","title":"A WD repeat protein, Rec14, essential for meiotic recombination in Schizosaccharomyces pombe.","citation":"Genetics 1997 Aug;146(4):1253-64","abstract":"Mutations in the Schizosaccharomyces pombe rec14 gene reduce meiotic recombination by as much as a factor of 1000 in the three intervals tested on chromosomes I and III. A DNA clone complementing the rec14 mutation was shown by genetic and physical analysis to contain the rec14 gene, which was functional in plasmid-borne inserts as small as 1.4 kb. The rec14 gene contains two exons separated by a 53-bp intron, which was confirmed by analysis of rec14 transcripts. The spliced transcript encodes a protein product of 302 amino acids, which contains six WD repeat motifs found in the G-beta transducin family of proteins and other proteins, including the Saccharomyces cerevisiae Ski8 (Rec103) protein. Although the rec14 transcripts were present in mitotically dividing cells, rec14 mutations had no detectable effect on mitotic recombination. The pattern of expression of rec14 differes from that of previously analyzed S. pombe rec genes. Based upon mutant phenotypes and amino acid sequence similarities, we propose that S. pombe Rec14 is a functional homologue of S. cerevisiae Rec103.","authors":"Evans DH, Li YF, Fox ME, Smith GR","authors_abbrev":"Evans DH et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"df52943f991cb994","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-05-19 13:02:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 20:28:47","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-29"},{"uniquename":"PMID:23614676","title":"Yeast as a biosensor of detoxification: a tool for identifying new compounds that revert multidrug resistance.","citation":"Curr Drug Targets 2013 Aug;14(9):964-85","abstract":"During tumour progression, cells accumulate secondary mutations and/or chromosomal aberrations that generate genetic diversity within the tumour cell population. This may result in the acquisition of new properties that increase tumour malignancy, such as invasiveness or resistance to chemotherapy. One of the important mechanisms of chemotherapy resistance is overexpression or biochemical activation of ABC family transporters. ABC transporters remove anti tumour drugs from the cell, reducing their intracellular concentration and producing resistance against a wide range of chemically unrelated drugs, known as multidrug resistant phenotype (MDR). During recent decades, much effort has been devoted to the isolation of compounds able to inhibit the activity of these transporters. However, few such compounds have reached clinical practice and MDR remains a serious complication in cancer therapy. In an innovative approach to finding new ABC inhibitors, we propose using fission yeast Schizosaccharomyces pombe as a biosensor of detoxification that would enable cost-efficient screening of natural compounds and chemical libraries for molecules that revert the MDR phenotype. Existing fission yeast tools provide genetic, biochemical and cell biological analysis, thereby facilitating identification of drug targets. Putative inhibitors and modulators of ABC transporters could be used in combination with chemotherapeutic drugs for the treatment of multidrug resistant tumours.","authors":"Martín-Cordero C, Sanchez-Pico A, Leon-Gonzalez AJ, Perez-Pulido AJ, Daga RR","authors_abbrev":"Martín-Cordero C et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-04-26","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35472286","title":"Single amino acid substitutions in hydrophobic cores at a head-coiled coil junction region of cohesin facilitate its release of DNA during anaphase.","citation":"Open Biol 2022 Apr;12(4):210275","abstract":"Cohesin holds sister chromatids together and is cleaved by separase/Cut1 to release DNA during the transition from mitotic metaphase to anaphase. The cohesin complex consists of heterodimeric structural maintenance of chromosomes (SMC) subunits (Psm1 and Psm3), which possess a head and a hinge, separated by long coiled coils. Non-SMC subunits (Rad21, Psc3 and Mis4) bind to the SMC heads. Kleisin/Rad21's N-terminal domain (Rad21-NTD) interacts with Psm3's head-coiled coil junction (Psm3-HCJ). Spontaneous mutations that rescued the cleavage defects in temperature-sensitive (ts) separase mutants were identified in the interaction interface, but the underlying mechanism is yet to be understood. Here, we performed site-directed random mutagenesis to introduce single amino acid substitutions in Psm3-HCJ and Rad21-NTD, and then identified 300 mutations that rescued the cohesin-releasing defects in a separase ts mutant. Mutational analysis indicated that the amino acids involved in hydrophobic cores (which may be in close contact) in Psm3-HCJ and Rad21-NTD are hotspots, since 80 mutations (approx. 27%) were mapped in these locations. Properties of these substitutions indicate that they destabilize the interaction between the Psm3 head and Rad21-NTD. Thus, they may facilitate sister chromatid separation in a cleavage-independent way through cohesin structural re-arrangement.","doi":"10.1098/rsob.210275","authors":"Xu X, Kanai R, Wang L, Yanagida M","authors_abbrev":"Xu X et al.","pubmed_publication_date":"Apr 2022","pubmed_entrez_date":"2022-04-26","publication_year":"2022","canto_session_key":"591f3684653ee718","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-04-30 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22992726","title":"The SAGA histone acetyltransferase complex regulates leucine uptake through the Agp3 permease in fission yeast.","citation":"J Biol Chem 2012 Nov 02;287(45):38158-67","abstract":"Metabolic responses of unicellular organisms are mostly acute, transient, and cell-autonomous. Regulation of nutrient uptake in yeast is one such rapid response. High quality nitrogen sources such as NH(4)(+) inhibit uptake of poor nitrogen sources, such as amino acids. Both transcriptional and posttranscriptional mechanisms operate in nutrient uptake regulation; however, many components of this system remain uncharacterized in the fission yeast, Schizosaccharomyces pombe. Here, we demonstrate that the Spt-Ada-Gcn acetyltransferase (SAGA) complex modulates leucine uptake. Initially, we noticed that a branched-chain amino acid auxotroph exhibits a peculiar adaptive growth phenotype on solid minimal media containing certain nitrogen sources. In fact, the growth of many auxotrophic strains is inhibited by excess NH(4)Cl, possibly through nitrogen-mediated uptake inhibition of the corresponding nutrients. Surprisingly, DNA microarray analysis revealed that the transcriptional reprogramming during the adaptation of the branched-chain amino acid auxotroph was highly correlated with reprogramming observed in deletions of the SAGA histone acetyltransferase module genes. Deletion of gcn5(+) increased leucine uptake in the prototrophic background and rendered the leucine auxotroph resistant to NH(4)Cl. Deletion of tra1(+) caused the opposite phenotypes. The increase in leucine uptake in the gcn5Δ mutant was dependent on an amino acid permease gene, SPCC965.11c(+). The closest budding yeast homolog of this permease is a relatively nonspecific amino acid permease AGP3, which functions in poor nutrient conditions. Our analysis identified the regulation of nutrient uptake as a physiological function for the SAGA complex, providing a potential link between cellular metabolism and chromatin regulation.","doi":"10.1074/jbc.M112.411165","authors":"Takahashi H, Sun X, Hamamoto M, Yashiroda Y, Yoshida M","authors_abbrev":"Takahashi H et al.","pubmed_publication_date":"02 Nov 2012","pubmed_entrez_date":"2012-09-21","publication_year":"2012","canto_session_key":"641dfb8a512e9e23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Minoru Yoshida","canto_first_approved_date":"2017-10-22 17:36:43","canto_approved_date":"2024-07-15 11:47:16","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-11-11 14:20:40","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Minoru Yoshida","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13","SPCC330.05c","SPBC28F2.10c","SPBC428.02c","SPBC30D10.16","SPBC1711.13","SPCC965.11c","SPBC14C8.17c","SPBC1921.07c","SPBC1A4.02c","SPCC24B10.08c","SPAC630.13c","SPAC1952.05","SPAC3G9.07c","SPBC215.08c","SPCC126.04c","SPBP16F5.03c","SPBC800.03"],"gene_count":18,"ltp_gene_count":18,"approved_date":"2017-10-22"},{"uniquename":"PMID:20924116","title":"Fission yeast Swi1-Swi3 complex facilitates DNA binding of Mrc1.","citation":"J Biol Chem 2010 Dec 17;285(51):39609-22","abstract":"Replication fork protection complex Swi1-Swi3 and replication checkpoint mediator Mrc1 are required for maintenance of replication fork integrity during the course of DNA replication in the fission yeast Schizosaccharomyces pombe. These proteins play crucial roles in stabilizing stalled forks and activating replication checkpoint signaling pathways. Although they are conserved replication fork components, precise biochemical roles of these proteins are not known. Here we purified Mrc1 and Swi1-Swi3 proteins and show that these proteins bind to DNA independently but synergistically in vitro. Mrc1 binds preferentially to arrested fork or D-loop-like structures, although the affinity is relatively low, whereas the Swi1-Swi3 complex binds to double-stranded DNA with higher affinity. In the presence of a low concentration of Swi1-Swi3, Mrc1 generates a novel ternary complex and binds to various types of DNA with higher affinity. Moreover, purified Mrc1 and Swi1-Swi3 physically interact with each other, and this interaction is lost by mutations in the known DNA binding domain of Mrc1 (K235E,K236E). The interaction is also lost in a mutant form of Swi1 (E662K) that is specifically defective in polar fork arrest at a site called RTS1 and causes sensitivity to genotoxic agents, although the DNA binding affinity of Swi1-Swi3 is not affected by this mutation. As expected, the synergistic effect of the Swi1-Swi3 on DNA binding of Mrc1 is also lost by these mutations affecting the interaction between Mrc1 and Swi1-Swi3. Our results reveal an aspect of molecular interactions that may play an important role in replication pausing and fork stabilization.","doi":"10.1074/jbc.M110.173344","authors":"Tanaka T, Yokoyama M, Matsumoto S, Fukatsu R, You Z, Masai H","authors_abbrev":"Tanaka T et al.","pubmed_publication_date":"17 Dec 2010","pubmed_entrez_date":"2010-10-07","publication_year":"2010","canto_session_key":"a97bb48a3280a5fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-05-14 13:42:30","canto_approved_date":"2023-10-31 23:01:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-14 13:42:20","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":33,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC694.06c","SPBC216.06c","SPBC30D10.04"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-05-14"},{"uniquename":"PMID:2121749","title":"Changes in the rate of oxygen consumption in synchronous cultures of the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1990 Jul;96 ( Pt 3):429-33","abstract":"Oxygen consumption was measured with an oxygen electrode in synchronous cultures of S. pombe. There were changes during the cell cycle in the rate of oxygen uptake, which are most clearly shown as oscillations in acceleration curves (rate of the rate of uptake). Under various conditions of selection and induction synchrony the acceleration curves are similar to those found earlier for CO2 production. As with CO2 production, the oscillations continued after a block to the DNA-division cycle. There were, however, two differences between oxygen uptake and CO2 production. The oxygen oscillations were more marked and also were out of phase by half a cycle. The respiratory coefficient therefore changes through the cycle.","authors":"Novak B, Mitchison JM","authors_abbrev":"Novak B et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8580465","title":"The beta 7 integrins in mucosal homing and retention.","citation":"Semin Immunol 1995 Oct;7(5):335-42","abstract":"Lymphocytes recirculate extensively throughout the body and then localize in tissues and lymphoid organs. This is accomplished by an array of adhesion molecules on lymphocytes and counter-receptors on the vascular endothelium, extracellular matrix and the epithelium. Recent studies have identified several of the specific molecular interactions that mediate lymphocyte trafficking. Lymphocytes expressing alpha 4 beta 7 home to the intestine through recognition of the mucosal addressin cell adhesion molecule-1 (MAdCAM-1) expressed on Peyer's patch high endothelial venules. T cells in nearly all mucosal epithelial sites express the alpha E beta 7 integrin which has been shown to mediate lymphocyte binding to epithelial cell E-cadherin. Thus, members of the B7 subfamily of integrins, alpha E beta 7 and alpha 4 beta 7, and their counter-receptors, are believed to play key roles in directing lymphocyte traffic to and retention in mucosal organs.","authors":"Shaw SK, Brenner MB","authors_abbrev":"Shaw SK et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22G7.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9687516","title":"A site- and strand-specific DNA break confers asymmetric switching potential in fission yeast.","citation":"EMBO J 1998 Aug 03;17(15):4503-10","abstract":"Mating-type switching in the fission yeast Schizosaccharomyces pombe results in the transfer of genetic information from one of the two silent cassettes (mat2P or mat3M) to the transcriptionally active locus (mat1). The switching pattern is programmed by an imprinting event which restricts mat1 gene conversion to only one of the two sister cells, leading to asymmetric cell division. Biochemical analysis indicated that the mat1 locus contains a fragile chromosomal site. Southern hybridization and primer extension experiments showed that the fragility consists of a single-strand break (SSB). The nicked DNA is stable throughout the cell cycle. The features of the nick fulfil all the requirements for the 'epigenetic', site and strand-specific chromosome modification at the mat1 locus, providing strong evidence that an SSB can initiate mitotic and meiotic gene conversion during replication.","authors":"Arcangioli B","authors_abbrev":"Arcangioli B","pubmed_publication_date":"03 Aug 1998","pubmed_entrez_date":"1998-08-04","publication_year":"1998","canto_session_key":"e9a22bd2e7ef555b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-06-12 21:57:57","canto_approved_date":"2018-06-12 21:57:57","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-06-12 21:57:50","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-06-12"},{"uniquename":"EMBL:AU010220","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22093869","title":"Multiple end joining mechanisms repair a chromosomal DNA break in fission yeast.","citation":"DNA Repair (Amst) 2012 Feb 01;11(2):120-30","abstract":"Non-homologous end joining (NHEJ) is an important mechanism for repairing DNA double-strand breaks (DSBs). The fission yeast Schizosaccharomyces pombe has a conserved set of NHEJ factors including Ku, DNA ligase IV, Xlf1, and Pol4. Their roles in chromosomal DSB repair have not been directly characterized before. Here we used HO endonuclease to create a specific chromosomal DSB in fission yeast and examined the imprecise end joining events allowing cells to survive the continuous expression of HO. Our analysis showed that cell survival was significantly reduced in mutants defective for Ku, ligase IV, or Xlf1. Using Sanger sequencing and Illumina sequencing, we have characterized in depth the repair junction sequences in HO survivors. In wild type cells the majority of repair events were one-nucleotide insertions dependent on Ku, ligase IV, and Pol4. Our data suggest that fission yeast Pol4 is important for gap filling during NHEJ repair and can extend primers in the absence of terminal base pairing with the templates. In Ku and ligase IV mutants, the survivors mainly resulted from two types of alternative end joining events: one used microhomology flanking the HO site to delete sequences of hundreds to thousands of base pairs, the other rejoined the break using the HO-generated overhangs but also introduced one- or two-nucleotide base substitutions. The chromosomal repair assay we describe here should provide a useful tool for further exploration of the end joining repair mechanisms in fission yeast.","doi":"10.1016/j.dnarep.2011.10.011","authors":"Li P, Li J, Li M, Dou K, Zhang MJ, Suo F, Du LL","authors_abbrev":"Li P et al.","pubmed_publication_date":"01 Feb 2012","pubmed_entrez_date":"2011-11-19","publication_year":"2012","canto_session_key":"6d1a7154e047457b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun Li","canto_approved_date":"2015-01-09 03:21:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-30 05:42:18","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jun Li","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1183.05c","SPAC2F7.06c","SPCC126.02c","SPCC24B10.14c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-10-30"},{"uniquename":"PMID:19168988","title":"Characterization of a fission yeast P(5)-type ATPase homologue that is essential for Ca(2+)/Mn(2+ )homeostasis in the absence of P(2)-type ATPases.","citation":"Genes Genet Syst 2008 Oct;83(5):373-81","abstract":"In the fission yeast Schizosaccharomyces pombe, three P-type ATPases, namely Cta4p, Pmr1p, and Pmc1p, have been shown to be essential for Ca(2+) homeostasis and are required for specific cellular functions as well. Here, we show that the simultaneous deletion of pmc1(+) and SPAC29A4.19c, which encodes a putative P(5)-type ATPase, causes a hypersensitive growth to either high concentrations of Ca(2+) in a medium, or the antiarrhythmic drug amiodarone, which has been known to cause a disruption of Ca(2+) homeostasis. On the other hand, simultaneous deletion of pmr1(+) and SPAC29A4.19c causes a hypersensitive growth to Mn(2+) depletion in a medium. The green fluorescent protein-tagged SPAC29A4.19c protein reveals a typical localization pattern of the Golgi proteins, but the SPAC29A4.19c protein is not exchangeable in function with Pmr1p, which is required for Ca(2+)/Mn(2+) homeostasis in secretory pathways. These results suggest that the putative P(5)-type ATPase encoded by SPAC29A4.19c is essential for Ca(2+) and Mn(2+ )homeostasis in the absence of P(2)-type ATPases, Pmc1p or Pmr1p, respectively. According to the precedent nomenclature of calcium/cation transporting ATPase in fission yeast, SPAC29A4.19 was named cta5(+) in this study.","authors":"Furune T, Hashimoto K, Ishiguro J","authors_abbrev":"Furune T et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2009-01-27","publication_year":"2008","canto_session_key":"49018f5f84f23bb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-22 09:30:51","canto_approved_date":"2026-02-06 11:17:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-11 13:47:26","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31E1.02c","SPAC29A4.19c","SPBC1A4.10c","SPAPB2B4.04c","SPCC1672.11c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-07-22"},{"uniquename":"PMID:21832151","title":"Endocytosis is essential for dynamic translocation of a syntaxin 1 orthologue during fission yeast meiosis.","citation":"Mol Biol Cell 2011 Oct;22(19):3658-70","abstract":"Syntaxin is a component of the target soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex, which is responsible for fusion of membrane vesicles at the target membrane. The fission yeast syntaxin 1 orthologue Psy1 is essential for both vegetative growth and spore formation. During meiosis, Psy1 disappears from the plasma membrane (PM) and dramatically relocalizes on the nascent forespore membrane, which becomes the PM of the spore. Here we report the molecular details and biological significance of Psy1 relocalization. We find that, immediately after meiosis I, Psy1 is selectively internalized by endocytosis. In addition, a meiosis-specific signal induced by the transcription factor Mei4 seems to trigger this internalization. The internalization of many PM proteins is facilitated coincident with the initiation of meiosis, whereas Pma1, a P-type ATPase, persists on the PM even during the progression of meiosis II. Ergosterol on the PM is also important for the internalization of PM proteins in general during meiosis. We consider that during meiosis in Schizosaccharomyces pombe cells, the characteristics of endocytosis change, thereby facilitating internalization of Psy1 and accomplishing sporulation.","doi":"10.1091/mbc.E11-03-0255","authors":"Kashiwazaki J, Yamasaki Y, Itadani A, Teraguchi E, Maeda Y, Shimoda C, Nakamura T","authors_abbrev":"Kashiwazaki J et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-08-12","publication_year":"2011","canto_session_key":"6451b9d7a7729c14","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-16 14:00:16","canto_approved_date":"2026-01-25 10:17:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-09 10:27:38","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":45,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1142.05","SPAC57A7.08","SPBC26H8.02c","SPAC688.11","SPAC8C9.04","SPCC1235.13","SPBC839.06","SPBC4C3.06","SPBC1652.02","SPBC1778.06c","SPBC36.03c","SPCC23B6.04c","SPBC32H8.12c","SPAC1F3.06c","SPAC977.10","SPAC17A2.01","SPBC1347.06c","SPAC32A11.02c","SPCC825.03c","SPAC17G8.14c","SPAC1805.05","SPCC1739.10","SPBC30B4.01c","SPCC584.05","SPBC146.13c","SPAC17G6.02c","SPBC32F12.01c","SPAC1071.10c","SPCC663.03","SPAC20G8.07c"],"gene_count":30,"ltp_gene_count":26,"approved_date":"2017-09-16"},{"uniquename":"PMID:12905027","title":"Localization and functional characterization of metal-binding sites in phytochelatin synthases.","citation":"Planta 2003 Dec;218(2):300-8","abstract":"Metal-binding domains consisting of short, contiguous stretches of amino acids are found in many proteins mediating the transport, buffering, trafficking or detoxification of metal ions. Phytochelatin synthases are metal-activated enzymes that function in the detoxification of Cd(2+) and other toxic metal and metalloid ions. In order to localize Cd(2+)-binding sites, peptide libraries of two diverse phytochelatin synthases were synthesized and incubated with (109)Cd(2+). Distinct binding sites and binding motifs could be localized based on the patterns of Cd(2+)-binding. The number of binding sites was consistent with previous findings for recombinant protein. Positions of binding sites appeared to be conserved even among diverse phytochelatin synthases. Mutant peptide analysis was used to assess the contribution of exemplary amino acids to binding. Several binding motifs contain cysteines or glutamates. For cysteines a strong correlation was found between binding activity and degree of conservation among known phytochelatin synthases. These findings indicate the suitability of peptide scanning for the identification of metal-binding sites. The functional role of several cysteines was investigated by expression of hemagglutinin-tagged phytochelatin synthases in phytochelatin synthase-deficient, Cd(2+)-hypersensitive Schizosaccharomyces pombe cells. The data are consistent with a model suggesting functionally essential metal-binding activation sites in the N-terminal catalytic part of phytochelatin synthases and additional binding sites at the C-terminus not essential for activity.","authors":"Maier T, Yu C, Küllertz G, Clemens S","authors_abbrev":"Maier T et al.","pubmed_publication_date":"Dec 2003","pubmed_entrez_date":"2003-08-09","publication_year":"2003","canto_session_key":"d9eaa59234dc496a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-06-03 17:13:33","canto_approved_date":"2019-05-04 10:19:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-05-02 16:09:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H1.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-06-03"},{"uniquename":"PMID:33658433","title":"Single-Molecule Imaging Reveals the Mechanism Underlying Histone Loading of  Schizosaccharomyces pombe  AAA+ ATPase Abo1.","citation":"Mol Cells 2021 Feb 28;44(2):79-87","abstract":"Chromatin dynamics is essential for maintaining genomic integrity and regulating gene expression. Conserved bromodomain-containing AAA+ ATPases play important roles in nucleosome organization as histone chaperones. Recently, the high-resolution cryo-electron microscopy structures of  Schizosaccharomyces pombe  Abo1 revealed that it forms a hexameric ring and undergoes a conformational change upon ATP hydrolysis. In addition, single-molecule imaging demonstrated that Abo1 loads H3-H4 histones onto DNA in an ATP hydrolysis-dependent manner. However, the molecular mechanism by which Abo1 loads histones remains unknown. Here, we investigated the details concerning Abo1-mediated histone loading onto DNA and the Abo1- DNA interaction using single-molecule imaging techniques and biochemical assays. We show that Abo1 does not load H2A-H2B histones. Interestingly, Abo1 deposits multiple copies of H3-H4 histones as the DNA length increases and requires at least 80 bp DNA. Unexpectedly, Abo1 weakly binds DNA regardless of ATP, and neither histone nor DNA stimulates the ATP hydrolysis activity of Abo1. Based on our results, we propose an allosteric communication model in which the ATP hydrolysis of Abo1 changes the configuration of histones to facilitate their deposition onto DNA.","doi":"10.14348/molcells.2021.2242","authors":"Kang Y, Cho C, Lee KS, Song JJ, Lee JY","authors_abbrev":"Kang Y et al.","pubmed_publication_date":"28 Feb 2021","pubmed_entrez_date":"2021-03-04","publication_year":"2021","canto_session_key":"e3b972dfd12d8605","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-07-06 16:28:10","canto_approved_date":"2026-01-22 17:04:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-08 11:44:56","canto_added_date":"2021-03-06 01:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.19"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-07-06"},{"uniquename":"PMID:7926674","title":"Use of Yarrowia lipolytica hexokinase for the quantitative determination of trehalose 6-phosphate.","citation":"FEMS Microbiol Lett 1994 Aug 15;121(2):223-7","abstract":"This paper describes a procedure for the quantitative determination of trehalose 6-phosphate (T6P) based on its ability to inhibit hexokinase from Yarrowia lipolytica. The assay is linear between 1 nmol and at least 8 nmol. The concentration of T6P in wild-type Saccharomyces cerevisiae (0.15 mM) and in ras2 mutants (0.25 mM) remained unchanged in the exponential or stationary phase of growth or after heat shock. A tps1 mutant affected in T6P synthase did not show detectable T6P. Heat shock increased the concentration of T6P in Schizosaccharomyces pombe from 0.43 to 0.75 mM.","authors":"Blázquez MA, Gancedo JM, Gancedo C","authors_abbrev":"Blázquez MA et al.","pubmed_publication_date":"15 Aug 1994","pubmed_entrez_date":"1994-08-15","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SP21154","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2682634","title":"The adenylyl cyclase gene from Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1989 Oct;86(20):7989-93","abstract":"We cloned the adenylyl cyclase gene from the fission yeast Schizosaccharomyces pombe using low-stringency hybridization to the Saccharomyces cerevisiae adenylyl cyclase gene. The Sc. pombe gene encodes a 1692-amino acid-residue protein. The identity of this gene was confirmed by studies of its expression in Sa. cerevisiae. Expression of the carboxyl-terminal region of the Sc. pombe adenylyl cyclase protein will suppress a temperature-sensitive mutation in the Sa. cerevisiae adenylyl cyclase gene. Furthermore, Sa. cerevisiae that lack their endogenous adenylyl cyclase gene and express the carboxyl-terminal region of the Sc. pombe adenylyl cyclase protein have measurable adenylyl cyclase activity. The carboxyl-terminal region of this protein has strong homology with the catalytic domain of the Sa. cerevisiae adenylyl cyclase. Also, Sc. pombe adenylyl cyclase, like Sa. cerevisiae adenylyl cyclase, contains a tandemly repeated motif rich in leucine. Neither yeast protein is particularly homologous to the recently cloned Gs-responsive mammalian adenylyl cyclase [Krupinski, J., Coussen, F., Bakalyar, H. A., Tang, W.-J., Feinstein, P. G., Orth, K., Slaughter, C., Reed, R. R. & Gilman, A. G. (1989) Science 244, 1558-1564].","authors":"Young D, Riggs M, Field J, Vojtek A, Broek D, Wigler M","authors_abbrev":"Young D et al.","pubmed_publication_date":"Oct 1989","pubmed_entrez_date":"1989-10-01","publication_year":"1989","canto_session_key":"2be4410cf6f320fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-19 17:32:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-19 17:32:39","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-11-19"},{"uniquename":"PMID:3017714","title":"Isolation and characterization of mutants from Schyzosaccharomyces pombe defective in glycerol catabolism.","citation":"Eur J Biochem 1986 Aug 15;159(1):171-4","abstract":"Mutants unable to grow on glycerol were isolated from the fission yeast Schyzosaccharomyces pombe. Two types of mutants were obtained: one type was able to grow on dihydroxyacetone while the other one did not grow on this compound. The first type of mutants was defective in glycerol dehydrogenase while the second one was affected both in the glycerol dehydrogenase and in dihydroxyacetone kinase. It was found that the second type was defective in the derepression of several enzymes. The mutations were nuclear and monogenic and defined two complementation groups. Spontaneous revertants, able to grow on glycerol, were obtained from the first type of mutants. They have regained the glycerol dehydrogenase activity. The results presented provide genetic evidence for a pathway of glycerol catabolism in Sch. pombe involving dehydrogenation of glycerol as the first step followed by phosphorylation of the dihydroxyacetone formed.","authors":"Gancedo C, Llobell A, Ribas JC, Luchi F","authors_abbrev":"Gancedo C et al.","pubmed_publication_date":"15 Aug 1986","pubmed_entrez_date":"1986-08-15","publication_year":"1986","canto_session_key":"278fd9a9a5dcfc0a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-09-25 13:39:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 13:15:11","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.12c","SPAC13F5.03c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2013-09-24"},{"uniquename":"EMBL:AU008626","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11381104","title":"Cytokinesis in prokaryotes and eukaryotes: common principles and different solutions.","citation":"Microbiol Mol Biol Rev 2001 Jun;65(2):319-33 ; third page, table of contents","abstract":"Cytokinesis requires duplication of cellular structures followed by bipolarization of the predivisional cell. As a common principle, this applies to prokaryotes as well as eukaryotes. With respect to eukaryotes, the discussion has focused mainly on Saccharomyces cerevisiae and on Schizosaccharomyces pombe. Escherichia coli and to a lesser extent Bacillus subtilis have been used as prokaryotic examples. To establish a bipolar cell, duplication of a eukaryotic origin of DNA replication as well as its genome is not sufficient. Duplication of the microtubule-organizing center is required as a prelude to mitosis, and it is here that the dynamic cytoskeleton with all its associated proteins comes to the fore. In prokaryotes, a cytoskeleton that pervades the cytoplasm appears to be absent. DNA replication and the concomitant DNA segregation seem to occur without help from extensive cytosolic supramacromolecular assemblies but with help from the elongating cellular envelope. Prokaryotic cytokinesis proceeds through a contracting ring, which has a roughly 100-fold-smaller circumference than its eukaryotic counterpart. Although the ring contains proteins that can be considered as predecessors of actin, tubulin, and microtubule-associated proteins, its macromolecular composition is essentially different.","authors":"Nanninga N","authors_abbrev":"Nanninga N","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-05-31","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19844171","title":"Geometric control of the cell cycle.","citation":"Cell Cycle 2009 Nov 15;8(22):3643-7","abstract":"How do cells sense their own size and shape? And how does this information regulate progression of the cell cycle? Our group, in parallel to that of Paul Nurse, have recently demonstrated that fission yeast cells use a novel geometry-sensing mechanism to couple cell length perception with entry into mitosis. These rod-shaped cells measure their own length by using a medially-placed sensor, Cdr2, that reads a protein gradient emanating from cell tips, Pom1, to control entry into mitosis. Budding yeast cells use a similar molecular sensor to delay entry into mitosis in response to defects in bud morphogenesis. Metazoan cells also modulate cell proliferation in response to their own shape by sensing tension. Here I discuss the recent results obtained for the fission yeast system and compare them to the strategies used by these other organisms to perceive their own morphology.","authors":"Martin SG","authors_abbrev":"Martin SG","pubmed_publication_date":"15 Nov 2009","pubmed_entrez_date":"2009-10-22","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:979958","title":"Rearrangements at the mating type locus in fission yeast.","citation":"Mol Gen Genet 1976 Oct 18;148(2):149-58","abstract":"Crosses involving the partially defective mating type mutant B102 (functional in conjugation, defective in meiosis) have confirmed the notion that, in Schizosaccharomyces pombe, certain mating type mutations can arise by transposition. A copy of the mat2P segment (specifying + mating type) is transposed and inserted into the mat1M segment (usually specifying - mating type). The mat1M segment affected by the insertion loses its former - function entirely. The - function is, however, fully regained upon excision of the transposed and inserted mat2P segment. At either position, the mat2P segments can undergo inactivations to different states of residual activity. These events can occur about as frequent as other mutations of the mating type locus (ca. 10(-4) per cell division). In certain diploid strains, such inactivations were significantly correlated with recombination. Spontaneous reversions to full activity were also observed.","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"18 Oct 1976","pubmed_entrez_date":"1976-10-18","publication_year":"1976","canto_session_key":"c64b08a8bb9515e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-12-08 22:31:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-08 22:31:07","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-12-08"},{"uniquename":"PMID:14051481","title":"ON THE SENSITIVITY OF GERMINATING SPORES OF SCHIZOSACCHAROMYCES POMBE TO X-RAYS.","citation":"C R Trav Lab Carlsberg 1963;33:319-46","abstract":"","authors":"DITLEVSEN E, HARTELIUS V","authors_abbrev":"DITLEVSEN E et al.","pubmed_publication_date":"1963","pubmed_entrez_date":"1963-01-01","publication_year":"1963","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30445619","title":"GTRD: a database on gene transcription regulation-2019 update.","citation":"Nucleic Acids Res 2019 Jan 08;47(D1):D100-D105","abstract":"The current version of the Gene Transcription Regulation Database (GTRD; http://gtrd.biouml.org) contains information about: (i) transcription factor binding sites (TFBSs) and transcription coactivators identified by ChIP-seq experiments for Homo sapiens, Mus musculus, Rattus norvegicus, Danio rerio, Caenorhabditis elegans, Drosophila melanogaster, Saccharomyces cerevisiae, Schizosaccharomyces pombe and Arabidopsis thaliana; (ii) regions of open chromatin and TFBSs (DNase footprints) identified by DNase-seq; (iii) unmappable regions where TFBSs cannot be identified due to repeats; (iv) potential TFBSs for both human and mouse using position weight matrices from the HOCOMOCO database. Raw ChIP-seq and DNase-seq data were obtained from ENCODE and SRA, and uniformly processed. ChIP-seq peaks were called using four different methods: MACS, SISSRs, GEM and PICS. Moreover, peaks for the same factor and peak calling method, albeit using different experiment conditions (cell line, treatment, etc.), were merged into clusters. To reduce noise, such clusters for different peak calling methods were merged into meta-clusters; these were considered to be non-redundant TFBS sets. Moreover, extended quality control was applied to all ChIP-seq data. Web interface to access GTRD was developed using the BioUML platform. It provides browsing and displaying information, advanced search possibilities and an integrated genome browser.","doi":"10.1093/nar/gky1128","authors":"Yevshin I, Sharipov R, Kolmykov S, Kondrakhin Y, Kolpakov F","authors_abbrev":"Yevshin I et al.","pubmed_publication_date":"08 Jan 2019","pubmed_entrez_date":"2018-11-17","publication_year":"2019","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2018-11-19 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25501814","title":"The septation initiation network controls the assembly of nodes containing Cdr2p for cytokinesis in fission yeast.","citation":"J Cell Sci 2015 Feb 01;128(3):441-6","abstract":"In the fission yeast Schizosaccharomyces pombe, cortical protein structures called interphase nodes help to prepare the cell for cytokinesis by positioning precursors of the cytokinetic contractile ring, and the septation initiation network (SIN) regulates the onset of cytokinesis and septum formation. Previous work has noted that one type of interphase node disappears during mitosis providing SIN activity is high. Here, we used time-lapse fluorescence microscopy to provide evidence that SIN activity is necessary and sufficient to disperse the type 1 node proteins Cdr2p and Mid1p into the cytoplasm, so these nodes assemble only during interphase through early mitosis when SIN activity is low. Activating the SIN in interphase cells dispersed Cdr2p and anillin Mid1p from type 1 nodes a few min after the SIN kinase Cdc7p–GFP accumulated at spindle pole bodies. If the SIN was then turned off in interphase cells, Cdr2p and Mid1p reappeared in nodes in parallel with the decline in SIN activity. Hyperactivating SIN during mitosis dispersed type 1 nodes earlier than normal, and prolonged SIN activation prevented nodes from reforming at the end of mitosis.","authors":"Pu KM, Akamatsu M, Pollard TD","authors_abbrev":"Pu KM et al.","pubmed_publication_date":"01 Feb 2015","pubmed_entrez_date":"2014-12-16","publication_year":"2015","canto_session_key":"ba95f673c6553975","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-08 11:48:06","canto_approved_date":"2021-01-08 11:48:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-27 09:36:58","canto_added_date":"2014-12-18 01:15:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPAC6F6.08c","SPAC57A10.02","SPBC21.06c","SPAC19E9.02","SPAC24B11.11c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2021-01-08"},{"uniquename":"PMID:24224056","title":"The transcription factors Atf1 and Pcr1 are essential for transcriptional induction of the extracellular maltase Agl1 in fission yeast.","citation":"PLoS One 2013;8(11):e80572","abstract":"The fission yeast Schizosaccharomyces pombe secretes the extracellular maltase Agl1, which hydrolyzes maltose into glucose, thereby utilizing maltose as a carbon source. Whether other maltases contribute to efficient utilization of maltose and how Agl1 expression is regulated in response to switching of carbon sources are unknown. In this study, we show that three other possible maltases and the maltose transporter Sut1 are not required for efficient utilization of maltose. Transcription of agl1 was induced when the carbon source was changed from glucose to maltose. This was dependent on Atf1 and Pcr1, which are highly conserved transcription factors that regulate stress-responsive genes in various stress conditions. Atf1 and Pcr1 generally bind the TGACGT motif as a heterodimer. The agl1 gene lacks the exact motif, but has many degenerate TGACGT motifs in its promoter and coding region. When the carbon source was switched from glucose to maltose, Atf1 and Pcr1 associated with the promoters and coding regions of agl1, fbp1, and gpx1, indicating that the Atf1-Pcr1 heteromer binds a variety of regions in its target genes to induce their transcription. In addition, the association of Mediator with these genes was dependent on Atf1 and Pcr1. These data indicate that Atf1 and Pcr1 induce the transcription of agl1, which allows efficient utilization of extracellular maltose.","doi":"10.1371/journal.pone.0080572","authors":"Kato H, Kira S, Kawamukai M","authors_abbrev":"Kato H et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-11-14","publication_year":"2013","canto_session_key":"7857fadc3a2fd43a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroaki Kato","canto_first_approved_date":"2015-11-03 15:49:12","canto_approved_date":"2022-06-07 10:40:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-17 18:53:19","canto_added_date":"2013-11-20 09:00:24","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Hiroaki Kato","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC21E11.03c","SPAPB24D3.10c","SPBC1198.14c","SPBC14F5.08","SPAC1039.11c","SPAC30D11.01c","SPBC1683.07","SPBC29B5.01","SPAC2F3.08","SPAC24B11.06c","SPBC32F12.03c"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2015-11-03"},{"uniquename":"PMID:25908789","title":"A new transcription factor for mitosis: in Schizosaccharomyces pombe, the RFX transcription factor Sak1 works with forkhead factors to regulate mitotic expression.","citation":"Nucleic Acids Res 2015 Aug 18;43(14):6874-88","abstract":"Mitotic genes are one of the most strongly oscillating groups of genes in the eukaryotic cell cycle. Understanding the regulation of mitotic gene expression is a key issue in cell cycle control but is poorly understood in most organisms. Here, we find a new mitotic transcription factor, Sak1, in the fission yeast Schizosaccharomyces pombe. Sak1 belongs to the RFX family of transcription factors, which have not previously been connected to cell cycle control. Sak1 binds upstream of mitotic genes in close proximity to Fkh2, a forkhead transcription factor previously implicated in regulation of mitotic genes. We show that Sak1 is the major activator of mitotic gene expression and also confirm the role of Fkh2 as the opposing repressor. Sep1, another forkhead transcription factor, is an activator for a small subset of mitotic genes involved in septation. From yeasts to humans, forkhead transcription factors are involved in mitotic gene expression and it will be interesting to see whether RFX transcription factors may also be involved in other organisms.","doi":"10.1093/nar/gkv274","authors":"Garg A, Futcher B, Leatherwood J","authors_abbrev":"Garg A et al.","pubmed_publication_date":"18 Aug 2015","pubmed_entrez_date":"2015-04-25","publication_year":"2015","canto_session_key":"3784f6b1e100bfcc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-06 17:56:02","canto_approved_date":"2021-02-08 09:32:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-28 10:45:08","canto_added_date":"2015-04-26 00:19:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":49,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16G5.15c","SPAC3G9.14","SPAPB1E7.04c","SPBC4C3.12","SPCC825.03c","SPBC1E8.05","SPAC6G10.12c","SPAC20G8.05c","SPBC27.04","SPAC3F10.15c","SPCC306.11","SPAC1705.03c","SPAC821.08c","SPNCRNA.98","SPAPB1E7.05","SPBC1105.05","SPAC19B12.02c","SPAC24H6.05"],"gene_count":18,"ltp_gene_count":4,"approved_date":"2017-09-06"},{"uniquename":"InterPro:IPR026851","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8298187","title":"Fission yeast genes nda1+ and nda4+, mutations of which lead to S-phase block, chromatin alteration and Ca2+ suppression, are members of the CDC46/MCM2 family.","citation":"Mol Biol Cell 1993 Oct;4(10):1003-15","abstract":"Fission yeast cold-sensitive mutants nda1-376 and nda4-108 display a cell cycle block phenotype at the restrictive temperature (cell elongation with the single nucleus) accompanied by an alteration in the nuclear chromatin region. DNA content analysis shows that the onset of DNA synthesis is blocked or greatly delayed in both mutant cells, the block being reversible in nda4-108. Upon release to the permissive temperature, nda4-108 cells resumed replicating DNA, followed by mitosis and cytokinesis. The nda4 phenotype was partly rescued by the addition of Ca2+ to the medium; Ca2+ plays a positive role in the nda4+ function. The predicted protein sequences of nda1+ and nda4+ isolated by complementation are similar to each other and also, respectively, to those of the budding yeast, MCM2 and CDC46, both of which are members of the gene family required for the initiation of DNA replication. The central domains of these proteins are conserved, whereas the NH2- and COOH- domains are distinct. Results of the disruption of the nda1+ and nda4+ genes demonstrates that they are essential for viability.","authors":"Miyake S, Okishio N, Samejima I, Hiraoka Y, Toda T, Saitoh I, Yanagida M","authors_abbrev":"Miyake S et al.","pubmed_publication_date":"Oct 1993","pubmed_entrez_date":"1993-10-01","publication_year":"1993","canto_session_key":"f3b55c72c1d04ebc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-11-16 16:01:27","canto_approved_date":"2021-12-15 21:41:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-03 15:43:29","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPBC4.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-11-16"},{"uniquename":"PMID:1850698","title":"Cyclin promotes the tyrosine phosphorylation of p34cdc2 in a wee1+ dependent manner.","citation":"EMBO J 1991 May;10(5):1255-63","abstract":"The regulation of p34cdc2 was investigated by overproducing p34cdc2, cyclin (A and B) and the wee1+ gene product (p107wee1) using a baculoviral expression system. p34cdc2 formed a functional complex with both cyclins as judged by co-precipitation, phosphorylation of cyclin in vitro, and activation of p34cdc2 histone H1 kinase activity. Co-production of p34cdc2 and p107wee1 in insect cells resulted in a minor population of p34cdc2 that was phosphorylated on tyrosine and displayed an altered electrophoretic mobility. When p34cdc2 and p107wee1 were co-produced with cyclin (A or B) in insect cells, there was a dramatic increase in the population of p34cdc2 that was phosphorylated on tyrosine and that displayed a shift in electrophoretic mobility. The phosphorylation of p34cdc2 on tyrosine was absolutely dependent upon the presence of kinase-active p107wee1. Tyrosine-specific as well as serine/threonine-specific protein kinase activities co-immunoprecipitated with p107wee1. These results suggest that cyclin functions to facilitate tyrosine phosphorylation of p34cdc2 and that p107wee1 functions to regulate p34cdc2, either directly or indirectly, by tyrosine phosphorylation.","authors":"Parker LL, Atherton-Fessler S, Lee MS, Ogg S, Falk JL, Swenson KI, Piwnica-Worms H","authors_abbrev":"Parker LL et al.","pubmed_publication_date":"May 1991","pubmed_entrez_date":"1991-05-01","publication_year":"1991","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8121487","title":"Cell cycle. Rum tale of replication.","citation":"Nature 1994 Jan 20;367(6460):219-20","abstract":"","authors":"Murray AW","authors_abbrev":"Murray AW","pubmed_publication_date":"20 Jan 1994","pubmed_entrez_date":"1994-01-20","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF016222","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1481570","title":"Schizosaccharomyces pombe mitochondria: morphological, respiratory and protein import characteristics.","citation":"Yeast 1992 Nov;8(11):923-33","abstract":"A technique is described for the isolation and purification of intact, respiratory-competent mitochondria from Schizosaccharomyces pombe. The purified mitochondria are capable of oxidizing NADH and succinate as respiratory substrates, indicating the presence of succinate dehydrogenase and an NADH dehydrogenase located on the outer surface of the inner membrane. Mitochondria display good respiratory control with an ADP/O ratio of < 2. Respiratory activity is linearly dependent upon the redox poise of the quinone pool, suggesting the presence of an unbranched respiratory pathway to molecular oxygen. Immunogold labelling using antisera raised against mitochondrial HSP70 proteins (SSP1, SSC1 and PHSP1) from three different species, namely S. pombe, Saccharomyces cerevisiae and the plant Pisum sativum respectively, has been used to investigate the presence and ultrastructure of the mitochondria isolated by this procedure. The immunocytochemistry was carried out using cells containing wild-type levels of SSP1 protein and cells over-expressing the protein. These results also demonstrate the capacity of mitochondria to import increased levels of protein in vivo. In vitro import experiments using COXIV-DHFR indicate that purified S. pombe mitochondria can efficiently import this precursor, and that protein translocation is dependent upon an oxidizable substrate and a membrane potential.","authors":"Moore AL, Walters AJ, Thorpe J, Fricaud AC, Watts FZ","authors_abbrev":"Moore AL et al.","pubmed_publication_date":"Nov 1992","pubmed_entrez_date":"1992-11-01","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6288447","title":"Arrangement of the ribosomal RNA genes in Schizosaccharomyces pombe.","citation":"FEBS Lett 1982 Jun 21;143(1):129-32","abstract":"","authors":"Barnitz JT, Cramer JH, Rownd RH, Cooley L, Söll D","authors_abbrev":"Barnitz JT et al.","pubmed_publication_date":"21 Jun 1982","pubmed_entrez_date":"1982-06-21","publication_year":"1982","canto_session_key":"03af386c20f8ddb4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 18:08:51","canto_approved_date":"2019-01-31 18:08:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 18:08:45","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:34517959","title":"Facile detection of RNA phospho-methylation in cells and tissues.","citation":"Methods Enzymol 2021;658:49-72","abstract":"RNAs from various cells and tissues are modified in nearly 200 chemically distinct ways. These modifications can be deposited either on the 5' or 3' ends, or internally on the nucleobases or sugar backbone. 5'-end modifications are crucial for protecting RNAs from untimely degradation/processing, regulating their cellular functions, or discriminating endogenous RNAs from pathogenic RNAs. 5'-end phospho-methylation is a remarkable RNA modification that is enzymatically deposited either on the γ-phosphate of nascent triphosphorylated RNAs by human BCDIN3/MePCE, or on the α-phosphate of processed monophosphorylated RNAs by human BCDIN3D. These 5'-phospho-methyltransferases are part of the BIN3 family of O-methyltransferases conserved from S. pombe to humans and play important cellular and biological roles, many of which await further elucidation. Here, we quickly recapitulate historical methods for the detection of 5'-end phospho-methyl modifications, and focus more specifically on a method that can be used to detect and quantify α-monophosphate methylation from as low as 10-100ng of total RNA from cells or tissues. This method is important for deciphering the roles of BCDIN3D and its homologs across species, as well as serves as starting point for the development of new methods for detection of 5'-end modifications.","doi":"10.1016/bs.mie.2021.06.002","authors":"Devanathan SK, Debnath TK, Xhemalçe B","authors_abbrev":"Devanathan SK et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-09-14","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-09-16 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20531409","title":"Global coordination of transcriptional control and mRNA decay during cellular differentiation.","citation":"Mol Syst Biol 2010 Jun 08;6:380","abstract":"The function of transcription in dynamic gene expression programs has been extensively studied, but little is known about how it is integrated with RNA turnover at the genome-wide level. We investigated these questions using the meiotic gene expression program of Schizosaccharomyces pombe. We identified over 80 transcripts that co-purify with the meiotic-specific Meu5p RNA-binding protein. Their levels and half-lives were reduced in meu5 mutants, demonstrating that Meu5p stabilizes its targets. Most Meu5p-bound RNAs were also targets of the Mei4p transcription factor, which induces the transient expression of approximately 500 meiotic genes. Although many Mei4p targets showed sharp expression peaks, Meu5p targets had broad expression profiles. In the absence of meu5, all Mei4p targets were expressed with similar kinetics, indicating that Meu5p alters the global features of the gene expression program. As Mei4p activates meu5 transcription, Mei4p, Meu5p and their common targets form a feed-forward loop, a motif common in transcriptional networks but not studied in the context of mRNA decay. Our data provide insight into the topology of regulatory networks integrating transcriptional and posttranscriptional controls.","doi":"10.1038/msb.2010.38","authors":"Amorim MJ, Cotobal C, Duncan C, Mata J","authors_abbrev":"Amorim MJ et al.","pubmed_publication_date":"08 Jun 2010","pubmed_entrez_date":"2010-06-10","publication_year":"2010","canto_session_key":"ce2412aa4732ca7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-21 08:23:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-21 08:23:41","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13C5.06c","SPAC22A12.02c","SPAC17A5.04c","SPBC428.07","SPBC16A3.13","SPBC11G11.01","SPAC2E1P5.02c","SPBC32F12.10","SPBC3H7.09","SPBC649.04","SPCC1020.06c","SPBC1773.08c","SPBC18H10.08c","SPAC22A12.01c","SPAC3A12.03c","SPBC530.14c","SPCC1235.08c","SPCP1E11.05c","SPCC63.04","SPAC13F5.03c","SPAC4C5.02c","SPAC1610.03c","SPBC2G2.10c","SPAC4G9.05","SPBC646.06c","SPCC4G3.08","SPAC6F6.12","SPAC3F10.05c","SPCC1442.12","SPAC4G9.12","SPBC1348.01","SPCC191.07","SPAPYUG7.06","SPAC8C9.16c","SPBC1198.14c","SPAC212.04c","SPAC23D3.10c","SPAC25H1.09","SPAC56E4.05","SPCC31H12.06","SPCC645.03c","SPBC32H8.07","SPBC713.11c","SPAC1639.01c","SPAC24H6.04","SPAC959.05c","SPAC1F8.05","SPAC4F8.07c","SPACUNK4.10","SPBC3H7.15","SPAC750.06c","SPCC1183.09c","SPAC212.01c","SPBC32H8.11","SPBC83.11","SPBC8D2.01","SPAC3F10.06c","SPAC8C9.09c","SPBC19C2.05","SPCC736.04c","SPAC5D6.09c","SPBC146.11c","SPBC32H8.02c","SPAC13G6.08","SPAC144.12","SPAC6G9.11","SPAC630.09c","SPAC144.10c","SPAC1B2.03c","SPAC806.07","SPAC977.06","SPBP8B7.24c","SPCC11E10.09c","SPAC4F10.16c","SPBC27.03","SPCC297.03","SPBPB2B2.07c","SPCC1739.08c","SPCC1827.02c","SPAC3F10.07c","SPAC1A6.06c","SPCC1682.11c","SPAPB2B4.04c","SPBC3E7.15c","SPBC839.08c"],"gene_count":85,"ltp_gene_count":2,"approved_date":"2014-07-21"},{"uniquename":"PMID:25825517","title":"A formin-nucleated actin aster concentrates cell wall hydrolases for cell fusion in fission yeast.","citation":"J Cell Biol 2015 Mar 30;208(7):897-911","abstract":"Cell-cell fusion is essential for fertilization. For fusion of walled cells, the cell wall must be degraded at a precise location but maintained in surrounding regions to protect against lysis. In fission yeast cells, the formin Fus1, which nucleates linear actin filaments, is essential for this process. In this paper, we show that this formin organizes a specific actin structure-the actin fusion focus. Structured illumination microscopy and live-cell imaging of Fus1, actin, and type V myosins revealed an aster of actin filaments whose barbed ends are focalized near the plasma membrane. Focalization requires Fus1 and type V myosins and happens asynchronously always in the M cell first. Type V myosins are essential for fusion and concentrate cell wall hydrolases, but not cell wall synthases, at the fusion focus. Thus, the fusion focus focalizes cell wall dissolution within a broader cell wall synthesis zone to shift from cell growth to cell fusion.","doi":"10.1083/jcb.201411124","authors":"Dudin O, Bendezú FO, Groux R, Laroche T, Seitz A, Martin SG","authors_abbrev":"Dudin O et al.","pubmed_publication_date":"30 Mar 2015","pubmed_entrez_date":"2015-04-01","publication_year":"2015","canto_session_key":"1f490bc22fcecb5e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2015-09-09 19:57:09","canto_approved_date":"2026-04-07 16:08:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-27 15:36:24","canto_added_date":"2015-04-02 00:18:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.09","SPBC646.06c","SPAC29A4.05","SPBC2D10.05","SPAC14C4.09","SPAC20G8.05c","SPAC23D3.10c","SPAC4F10.15c","SPBC19G7.05c","SPCC1919.10c","SPBC2D10.14c","SPAC20G4.02c","SPBC1105.05","SPBC146.13c","SPAC17G8.04c","SPAC12B10.11","SPAC23C4.02","SPCC1840.02c","SPAC27F1.02c","SPCC895.05","SPBC24C6.10c"],"gene_count":21,"ltp_gene_count":21,"approved_date":"2015-09-09"},{"uniquename":"PMID:31380845","title":"Analysis of Lipid Droplet Content in Fission and Budding Yeasts using Automated Image Processing.","citation":"J Vis Exp 2019 Jul 17;(149)","abstract":"Lipid metabolism and its regulation are of interest to both basic and applied life sciences and biotechnology. In this regard, various yeast species are used as models in lipid metabolic research or for industrial lipid production. Lipid droplets are highly dynamic storage bodies and their cellular content represents a convenient readout of the lipid metabolic state. Fluorescence microscopy is a method of choice for quantitative analysis of cellular lipid droplets, as it relies on widely available equipment and allows analysis of individual lipid droplets. Furthermore, microscopic image analysis can be automated, greatly increasing overall analysis throughput. Here, we describe an experimental and analytical workflow for automated detection and quantitative description of individual lipid droplets in three different model yeast species: the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus, and the budding yeast Saccharomyces cerevisiae. Lipid droplets are visualized with BODIPY 493/503, and cell-impermeable fluorescent dextran is added to the culture media to help identify cell boundaries. Cells are subjected to 3D epifluorescence microscopy in green and blue channels and the resulting z-stack images are processed automatically by a MATLAB pipeline. The procedure outputs rich quantitative data on cellular lipid droplet content and individual lipid droplet characteristics in a tabular format suitable for downstream analyses in major spreadsheet or statistical packages. We provide example analyses of lipid droplet content under various conditions that affect cellular lipid metabolism.","doi":"10.3791/59889","authors":"Princová J, Schätz M, Ťupa O, Převorovský M","authors_abbrev":"Princová J et al.","pubmed_publication_date":"17 Jul 2019","pubmed_entrez_date":"2019-08-06","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-08-07 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26519308","title":"Visualization of Fission Yeast Cells by Transmission Electron Microscopy.","citation":"Methods Mol Biol 2016;1369:97-111","abstract":"This chapter deals with the preparation of fission yeast (Schizosaccharomyces) cells for ultrastructural examination. The structure of the cell must be preserved as close to the in vivo situation as possible. This can be achieved by either chemical or cryofixation; the latter will not be dealt with in this chapter. Aldehydes that cross-link proteins and permanganates that besides cross-linking also stain membranous and cell wall structures are used for chemical fixation. This step is followed by dehydration and embedding of the cells in epoxy or acrylic resin. Sectioning of the embedded material produces slices of the cells that have to be stained with heavy metals to increase contrast differences between different structures or can be used for immunodetection of antigens (polysaccharides or proteins) with specific primary antibodies and gold-conjugated secondary antibodies.","doi":"10.1007/978-1-4939-3145-3_8","authors":"Sipiczki M","authors_abbrev":"Sipiczki M","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-11-01","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-02 01:19:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7937765","title":"Schizosaccharomyces pombe glycosylation mutant with altered cell surface properties.","citation":"Proc Natl Acad Sci U S A 1994 Sep 27;91(20):9327-31","abstract":"Mutagenesis of Schizosaccharomyces pombe cells yielded a strain that made reduced amounts of invertase. A comparison of the O- and N-linked carbohydrate chains of the wild-type and mutant glycoproteins revealed that a single type of alpha 1-->2-linked mannose was missing in the mutant. Analysis of the wild-type galactomannoprotein showed that it contained a heterogeneous small \"core\" oligosaccharide fraction linked to asparagine with sugar compositions that ranged from Man9(GlcNAc)2- to Gal4Man10(GlcNAc)2-. The galactose units are in terminal positions of a Man10(GlcNAc)2- unit that is similar to the mannoprotein core of Saccharomyces cerevisiae. Attached to this core in a larger oligosaccharide fraction is an alpha 1-->6-linked polymannose chain that is substituted at position 2 with alpha-linked mannose and galactose. The O-linked sugars consist of mannose, alpha 1-->2-linked mannosylmannose and alpha 1-->2-linked galactosylmannose, along with small amounts of tri- and tetrasaccharides. The glycosylation mutant lacks alpha 1-->2-linked mannose on both the O-linked chains and the outer chain of the large N-linked chains, suggesting that it may be defective in regulation of an alpha 1,2-mannosyltransferase that adds mannose to glycoproteins in the Golgi.","authors":"Ballou CE, Ballou L, Ball G","authors_abbrev":"Ballou CE et al.","pubmed_publication_date":"27 Sep 1994","pubmed_entrez_date":"1994-09-27","publication_year":"1994","canto_session_key":"3bc1f7bd46c84bef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-09-30 13:44:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-09-30 13:44:26","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-09-30"},{"uniquename":"PMID:25883323","title":"Widespread exon skipping triggers degradation by nuclear RNA surveillance in fission yeast.","citation":"Genome Res 2015 Jun;25(6):884-96","abstract":"Exon skipping is considered a principal mechanism by which eukaryotic cells expand their transcriptome and proteome repertoires, creating different splice variants with distinct cellular functions. Here we analyze RNA-seq data from 116 transcriptomes in fission yeast (Schizosaccharomyces pombe), covering multiple physiological conditions as well as transcriptional and RNA processing mutants. We applied brute-force algorithms to detect all possible exon-skipping events, which were widespread but rare compared to normal splicing events. Exon-skipping events increased in cells deficient for the nuclear exosome or the 5'-3' exonuclease Dhp1, and also at late stages of meiotic differentiation when nuclear-exosome transcripts decreased. The pervasive exon-skipping transcripts were stochastic, did not increase in specific physiological conditions, and were mostly present at less than one copy per cell, even in the absence of nuclear RNA surveillance and during late meiosis. These exon-skipping transcripts are therefore unlikely to be functional and may reflect splicing errors that are actively removed by nuclear RNA surveillance. The average splicing rate by exon skipping was ∼ 0.24% in wild type and ∼ 1.75% in nuclear exonuclease mutants. We also detected approximately 250 circular RNAs derived from single or multiple exons. These circular RNAs were rare and stochastic, although a few became stabilized during quiescence and in splicing mutants. Using an exhaustive search algorithm, we also uncovered thousands of previously unknown splice sites, indicating pervasive splicing; yet most of these splicing variants were cryptic and increased in nuclear degradation mutants. This study highlights widespread but low frequency alternative or aberrant splicing events that are targeted by nuclear RNA surveillance.","doi":"10.1101/gr.185371.114","authors":"Bitton DA, Atkinson SR, Rallis C, Smith GC, Ellis DA, Chen YY, Malecki M, Codlin S, Lemay JF, Cotobal C, Bachand F, Marguerat S, Mata J, Bähler J","authors_abbrev":"Bitton DA et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-04-18","publication_year":"2015","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2015-04-19 00:19:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9G1.07","SPBP4H10.12","SPBC3B8.10"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:22359238","title":"Effect of the fungal mycotoxin patulin on the chromatin structure of fission yeast Schizosaccharomyces pombe.","citation":"J Basic Microbiol 2012 Dec;52(6):642-52","abstract":"The fungal mycotoxin patulin is produced by several molds, especially by Aspergillus and Penicillium. The aim of this study was to clarify whether patulin causes alterations in plasma membrane permeability of Schizosaccharomyces pombe lead to cellular shrinkage charateristic to apoptosis or increases cell size indicating necrosis in cells. Transmission and scanning electronmicroscopy revealed that lower concentrations of patulin induced cellular shrinkage and blebbing, higher concentration caused expansion without cellular disruption. Large-scale morphological changes of individual cells were followed by time lapse video microscopy. Patulin caused the elongation and stickiness of cells or rounded up their shapes. To visualize chromatin structures of S. pombe nuclei upon patulin treatment, protoplasts were isolated from S. pombe and subjected to fluorescent microscopy. Chromatin changes in the presence of 50 μM patulin concentration were characterized by elongated nuclei containing sticky fibrillary chromatin and enlarged round shaped nuclei trapped at the fibrillary stage of chromatin condensation. Short (60 min) incubation of S. pombe cells in the presence of high (500 μM) patulin concentration generated patches of condensed chromatin bodies inside the nucleus and caused nuclear expansion, with the rest of chromatin remaining in fibrillary form. Longer (90 min, 500 μM) incubation resulted in fewer highly condensed chromatin patches and in nuclear fragmentation. Although, high patulin concentration increased the size of S. pombe size, it did not lead to necrotic explosion of cells, neither did the fragmented nuclei resemble apoptotic bodies that would have indicated programmed cell death. All these morphological changes and the high rate of cell survival point to rapid adaptation and mixed type of fungistatic effects.","doi":"10.1002/jobm.201100515","authors":"Horvath E, Nagy G, Turani M, Balogh E, Papp G, Pollak E, Pocsi I, Pesti M, Banfalvi G","authors_abbrev":"Horvath E et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-02-24","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15920625","title":"Characterization of a second gene encoding gamma-glutamyl transpeptidase from Schizosaccharomyces pombe.","citation":"Can J Microbiol 2005 Mar;51(3):269-75","abstract":"The first gene encoding gamma-glutamyl transpeptidase (GGTI) of the fission yeast has previously been characterized, and its expression was found to be regulated by various oxidative stress-inducing agents. In this work, a second gene, encoding GGTII, was cloned and characterized from the fission yeast Schizosaccharomyces pombe. The structural gene encoding GGTII was amplified from the genomic DNA of the fission yeast and ligated into the shuttle vector pRS316 to generate the recombinant plasmid pPHJ02. The determined sequence contains 3040 bp and is able to encode the putative 611 amino acid sequence of GGTII, which resembles the counterparts of Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus, and Escherichia coli. The DNA sequence also contains 940-bp upstream and 289-bp downstream regions of the GGTII gene. The Schizosaccharomyces pombe cells harboring plasmid pPHJ02 showed about 4-fold higher GGT activity in the exponential phase than the cells harboring the vector only, indicating that the cloned GGTII gene is functional. The S. pombe cells containing the cloned GGTII gene were found to contain higher levels of both intracellular glutathione (GSH) content and GSH uptake. The S. pombe cells harboring plasmid pPHJ02 showed increased survival on solid media containing hydrogen peroxide, diethylmaleate, aluminum chloride, cadmium chloride, or mercuric chloride. The GGTII mRNA level was significantly elevated by treatment with GSH-depleting diethylmaleate. These results imply that the S. pombe GGTII gene produces functional GGTII protein and is involved in the response to oxidative stresses in S. pombe cells.","authors":"Park HJ, Moon JS, Kim HG, Kim IH, Kim K, Park EH, Lim CJ","authors_abbrev":"Park HJ et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-05-28","publication_year":"2005","canto_session_key":"75dadd0ae174dd58","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-05 14:45:53","canto_approved_date":"2025-11-24 13:34:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-27 15:19:29","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC56E4.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-07-05"},{"uniquename":"PMID:20226666","title":"Regulation of cytokinesis by the formin cdc12p.","citation":"Curr Biol 2010 Mar 23;20(6):561-6","abstract":"For successful cell division, cytokinesis must be properly timed to occur only after the segregation of chromosomes during mitosis. In the fission yeast Schizosaccharomyces pombe, contractile ring assembly initiates at the onset of mitosis, and ring contraction occurs concomitant with septation at the end of anaphase. Although many of the conserved factors necessary for ring assembly and regulation of cytokinesis have been characterized, still little is known about cell-cycle regulation of events that initiate cytokinesis. The formin cdc12p is an essential ring component with a well-characterized function in F-actin assembly. Here we show that overexpression of a cdc12p fragment bypasses normal cell-cycle controls and induces contractile ring assembly and sometimes even ring contraction and septation, all during interphase. Activation of cytokinesis occurs without the apparent activation of cell-cycle regulators such as polo kinase or the septation initiation network. For this effect, cdc12p contributes at least two separable activities: actin assembly and one or more additional functions in cytokinesis initiation. These observations suggest that the formin cdc12p participates downstream of cell-cycle regulators in a network that drives the initiation of cytokinesis.","doi":"10.1016/j.cub.2010.01.061","authors":"Yonetani A, Chang F","authors_abbrev":"Yonetani A et al.","pubmed_publication_date":"23 Mar 2010","pubmed_entrez_date":"2010-03-16","publication_year":"2010","canto_session_key":"e905a9d566f724ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-05-09 17:29:21","canto_approved_date":"2021-05-09 17:29:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-28 16:20:59","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-05-09"},{"uniquename":"PMID:28615445","title":"Iron-sulfur cluster biogenesis and trafficking in mitochondria.","citation":"J Biol Chem 2017 Aug 04;292(31):12754-12763","abstract":"The biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes is a multistage, multicompartment process that is essential for a broad range of cellular functions, including genome maintenance, protein translation, energy conversion, and the antiviral response. Genetic and cell biological studies over almost 2 decades have revealed some 30 proteins involved in the synthesis of cellular [2Fe-2S] and [4Fe-4S] clusters and their incorporation into numerous apoproteins. Mechanistic aspects of Fe/S protein biogenesis continue to be elucidated by biochemical and ultrastructural investigations. Here, we review recent developments in the pursuit of constructing a comprehensive model of Fe/S protein assembly in the mitochondrion.","doi":"10.1074/jbc.R117.787101","authors":"Braymer JJ, Lill R","authors_abbrev":"Braymer JJ et al.","pubmed_publication_date":"04 Aug 2017","pubmed_entrez_date":"2017-06-16","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10567589","title":"Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation.","citation":"Mol Cell Biol 1999 Dec;19(12):8660-72","abstract":"Unlike ubiquitin, the ubiquitin-like protein modifier SUMO-1 and its budding yeast homologue Smt3p have been shown to be more important for posttranslational protein modification than for protein degradation. Here we describe the identification of the SUMO-1 homologue of fission yeast, which we show to be required for a number of nuclear events including the control of telomere length and chromosome segregation. A disruption of the pmt3(+) gene, the Schizosaccharomyces pombe homologue of SMT3, was not lethal, but mutant cells carrying the disrupted gene grew more slowly. The pmt3Delta cells showed various phenotypes such as aberrant mitosis, sensitivity to various reagents, and high-frequency loss of minichromosomes. Interestingly, we found that pmt3(+) is required for telomere length maintenance. Loss of Pmt3p function caused a striking increase in telomere length. When Pmt3p synthesis was restored, the telomeres became gradually shorter. This is the first demonstration of involvement of one of the Smt3p/SUMO-1 family proteins in telomere length maintenance. Fusion of Pmt3p to green fluorescent protein (GFP) showed that Pmt3p was predominantly localized as intense spots in the nucleus. One of the spots was shown to correspond to the spindle pole body (SPB). During prometaphase- and metaphase, the bright GFP signals at the SPB disappeared. These observations suggest that Pmt3p is required for kinetochore and/or SPB functions involved in chromosome segregation. The multiple functions of Pmt3p described here suggest that several nuclear proteins are regulated by Pmt3p conjugation.","authors":"Tanaka K, Nishide J, Okazaki K, Kato H, Niwa O, Nakagawa T, Matsuda H, Kawamukai M, Murakami Y","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-11-24","publication_year":"1999","canto_session_key":"9bc7b364a9234861","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-02-22 20:22:16","canto_approved_date":"2019-02-22 20:22:16","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-02-22 20:22:08","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC18B5.11c","SPBC365.06"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-02-22"},{"uniquename":"PMID:18231579","title":"The CDK-activating kinase (CAK) Csk1 is required for normal levels of homologous recombination and resistance to DNA damage in fission yeast.","citation":"PLoS One 2008 Jan 30;3(1):e1492","abstract":"Cyclin-dependent kinases (CDKs) perform essential roles in cell division and gene expression in all eukaryotes. The requirement for an upstream CDK-activating kinase (CAK) is also universally conserved, but the fission yeast Schizosaccharomyces pombe appears to be unique in having two CAKs with both overlapping and specialized functions that can be dissected genetically. The Mcs6 complex--orthologous to metazoan Cdk7/cyclin H/Mat1--activates the cell-cycle CDK, Cdk1, but its non-redundant essential function appears to be in regulation of gene expression, as part of transcription factor TFIIH. The other CAK is Csk1, an ortholog of budding yeast Cak1, which activates all three essential CDKs in S. pombe--Cdk1, Mcs6 and Cdk9, the catalytic subunit of positive transcription elongation factor b (P-TEFb)--but is not itself essential.\nCells lacking csk1(+) are viable but hypersensitive to agents that damage DNA or block replication. Csk1 is required for normal levels of homologous recombination (HR), and interacts genetically with components of the HR pathway. Tests of damage sensitivity in csk1, mcs6 and cdk9 mutants indicate that Csk1 acts pleiotropically, through Cdk9 and at least one other target (but not through Mcs6) to preserve genomic integrity.\nThe two CAKs in fission yeast, which differ with respect to their substrate range and preferences for monomeric CDKs versus CDK/cyclin complexes as substrates, also support different functions of the CDK network in vivo. Csk1 plays a non-redundant role in safeguarding genomic integrity. We propose that specialized activation pathways dependent on different CAKs might insulate CDK functions important in DNA damage responses from those capable of triggering mitosis.","doi":"10.1371/journal.pone.0001492","authors":"Gerber HB, Pikman Y, Fisher RP","authors_abbrev":"Gerber HB et al.","pubmed_publication_date":"30 Jan 2008","pubmed_entrez_date":"2008-01-31","publication_year":"2008","canto_session_key":"71e1c4f7ef5de449","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-23 15:45:41","canto_approved_date":"2019-05-03 12:15:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-23 15:43:01","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.10","SPBC28F2.07","SPAC1D4.06c","SPAC644.14c","SPBC19F8.07","SPAC15A10.03c","SPBC216.05","SPBC3E7.08c","SPAC4H3.05","SPAC20H4.07"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-11-23"},{"uniquename":"PMID:8566770","title":"Cloning and characterization of the mitochondrial HSP60-encoding gene of Schizosaccharomyces pombe.","citation":"Gene 1995 Dec 29;167(1-2):163-6","abstract":"We report the isolation and characterization of a gene (designated mcp60) encoding the mitochondrial (mt) 60-kDa heat-shock protein (HSP60) in the fission yeast Schizosaccharomyces pombe. The deduced amino-acid sequence (582 aa) of this gene is highly similar to the known mt HSP60 from diverse organisms. When its sequence was related to the known functional domains of bacterial HSP60 (GroEL), the similarity was particularly high for the intermediate domains that connect the apical domain with the equatorial domain. The mRNA level of mcp60 increased several-fold upon temperature upshift (from 25 to 35 degrees C), while gradually decreased during sporulation. Gene disruption experiments revealed that mcp60 is essential for cell viability at all temperatures.","authors":"Yoshida H, Yanagi H, Yura T","authors_abbrev":"Yoshida H et al.","pubmed_publication_date":"29 Dec 1995","pubmed_entrez_date":"1995-12-29","publication_year":"1995","canto_session_key":"b522bc9d484ad0db","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-10-26 13:21:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-16 12:36:27","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC12G12.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-16"},{"uniquename":"EMBL:AU010538","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38562768","title":"Human CCDC51 and yeast Mdm33 are functionally conserved mitochondrial inner membrane proteins that demarcate a subset of organelle fission events.","citation":"bioRxiv 2024 Mar 22;","abstract":"Mitochondria are highly dynamic double membrane-bound organelles that exist in a semi-continuous network. Mitochondrial morphology arises from the complex interplay of numerous processes, including opposing fission and fusion dynamics and the formation of highly organized cristae invaginations of the inner membrane. While extensive work has examined the mechanisms of mitochondrial fission, it remains unclear how fission is coordinated across two membrane bilayers and how mitochondrial inner membrane organization is coupled with mitochondrial fission dynamics. Previously, the yeast protein Mdm33 was implicated in facilitating fission by coordinating with inner membrane homeostasis pathways. However, Mdm33 is not conserved outside fungal species and its precise mechanistic role remains unclear. Here, we use a bioinformatic approach to identify a putative structural ortholog of Mdm33 in humans, CCDC51 (also called MITOK). We find that the mitochondrial phenotypes associated with altered CCDC51 levels implicate the protein in mitochondrial fission dynamics. Further, using timelapse microscopy, we spatially and temporally resolve Mdm33 and CCDC51 to a subset of mitochondrial fission events. Finally, we show that CCDC51 can partially rescue yeast  Δmdm33  cells, indicating the proteins are functionally analogous. Our data reveal that Mdm33/CCDC51 are conserved mediators of mitochondrial morphology and suggest the proteins play a crucial role in maintaining normal mitochondrial dynamics and organelle homeostasis.","doi":"10.1101/2024.03.21.586162","authors":"Edington AR, Connor OM, Marlar-Pavey M, Friedman JR","authors_abbrev":"Edington AR et al.","pubmed_publication_date":"22 Mar 2024","pubmed_entrez_date":"2024-04-02","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC823.13c","HGNC:25714"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7431938","title":"Analyses of fission scars as permanent records of cell division in Schizosaccharomyces pombe.","citation":"J Theor Biol 1980 Jun 07;84(3):523-44","abstract":"","authors":"Calleja GB, Zuker M, Johnson BF, Yoo BY","authors_abbrev":"Calleja GB et al.","pubmed_publication_date":"07 Jun 1980","pubmed_entrez_date":"1980-06-07","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18252195","title":"Methylations of histone H3 lysine 9 and lysine 36 are functionally linked to DNA replication checkpoint control in fission yeast.","citation":"Biochem Biophys Res Commun 2008 Apr 04;368(2):419-25","abstract":"Recently, histone H4 lysine 20 and H3 lysine 79 methylations were functionally linked to DNA damage checkpoint. The crosstalk between histone methylation and the S-M checkpoint, however, has remained unclear. Here, we show that H3 lysine 9 (K9) and lysine 36 (K36) methylations catalyzed by two histone methyltransferases Clr4 and Set2 are involved in hydroxyurea (HU)-induced replication checkpoint. The clr4-set2 double mutants besides histone H3-K9 and K36 double mutants exhibited HU-sensitivity, a defective HU-induced S-M checkpoint, and a significant reduction of HU-induced phosphorylation of Cdc2. Intriguingly, the clr4-set2 double mutations impaired the HU-induced accumulation of a mitotic inhibitor Mik1. Double mutants in Alp13 and Swi6, which can specifically bind to H3-K36 and K9 methylations, exhibited phenotypes similar to those of the clr4-set2 mutants. Together, these findings suggest that methylations of histone H3-K9 and K36 by Clr4 and Set2 are functionally linked to DNA replication checkpoint via accumulation of Mik1.","doi":"10.1016/j.bbrc.2008.01.104","authors":"Kim HS, Rhee DK, Jang YK","authors_abbrev":"Kim HS et al.","pubmed_publication_date":"04 Apr 2008","pubmed_entrez_date":"2008-02-07","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.02c","SPAC664.01c","SPAC23H4.12","SPBC428.08c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:38701646","title":"The absence of the ribosomal protein Rpl2702 elicits the MAPK-mTOR signaling to modulate mitochondrial morphology and functions.","citation":"Redox Biol 2024 Apr 29;73:103174","abstract":"Ribosomes mediate protein synthesis, which is one of the most energy-demanding activities within the cell, and mitochondria are one of the main sources generating energy. How mitochondrial morphology and functions are adjusted to cope with ribosomal defects, which can impair protein synthesis and affect cell viability, is poorly understood. Here, we used the fission yeast Schizosaccharomyces Pombe as a model organism to investigate the interplay between ribosome and mitochondria. We found that a ribosomal insult, caused by the absence of Rpl2702, activates a signaling pathway involving Sty1/MAPK and mTOR to modulate mitochondrial morphology and functions. Specifically, we demonstrated that Sty1/MAPK induces mitochondrial fragmentation in a mTOR-independent manner while both Sty1/MAPK and mTOR increases the levels of mitochondrial membrane potential and mitochondrial reactive oxygen species (mROS). Moreover, we demonstrated that Sty1/MAPK acts upstream of Tor1/TORC2 and Tor1/TORC2 and is required to activate Tor2/TORC1. The enhancements of mitochondrial membrane potential and mROS function to promote proliferation of cells bearing ribosomal defects. Hence, our study reveals a previously uncharacterized Sty1/MAPK-mTOR signaling axis that regulates mitochondrial morphology and functions in response to ribosomal insults and provides new insights into the molecular and physiological adaptations of cells to impaired protein synthesis.","doi":"10.1016/j.redox.2024.103174","authors":"Liu L, Wu Y, Liu K, Zhu M, Guang S, Wang F, Liu X, Yao X, He J, Fu C","authors_abbrev":"Liu L et al.","pubmed_publication_date":"29 Apr 2024","pubmed_entrez_date":"2024-05-03","publication_year":"2024","canto_session_key":"c02a373d08fc2578","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-05-04 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11932440","title":"Potassium- or sodium-efflux ATPase, a key enzyme in the evolution of fungi.","citation":"Microbiology (Reading) 2002 Apr;148(Pt 4):933-941","abstract":"Potassium is the most abundant cation in cells. Therefore, plant-associated fungi and intracellular parasites are permanently or circumstantially exposed to high K(+) and must avoid excessive K(+) accumulation activating K(+) efflux systems. Because high K(+) and high pH are compatible in natural environments, free-living organisms cannot keep a permanent transmembrane DeltapH and cannot rely only on K(+)/H(+) antiporters, as do mitochondria. This study shows that the Schizosaccharomyces pombe CTA3 is a K(+)-efflux ATPase, and that other fungi are furnished with Na(+)-efflux ATPases, which also pump Na(+). All these fungal ATPases, including those pumping only Na(+), form a phylogenetic group, IID or ENA, among P-type ATPases. By searching in databases and partial cloning of ENA genes in species of Zygomycetes and Basidiomycetes, the authors conclude that probably all fungi have these genes. This study indicates that fungal K(+)- or Na(+)-ATPases evolved from an ancestral K(+)-ATPase, through processes of gene duplication. In yeast hemiascomycetes these duplications have occurred recently and produced bifunctional ATPases, whereas in Neurospora, and probably in other euascomycetes, they occurred earlier in evolution and produced specialized ATPases. In Schizosaccharomyces, adaptation to Na(+) did not involve the duplication of the K(+)-ATPase and thus it retains an enzyme which is probably close to the original one. The parasites Leishmania and Trypanosoma have ATPases phylogenetically related to fungal K(+)-ATPases, which are probably functional homologues of the fungal enzymes.","doi":"10.1099/00221287-148-4-933","authors":"Benito B, Garciadeblás B, Rodrı Guez-Navarro A","authors_abbrev":"Benito B et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-05","publication_year":"2002","canto_session_key":"e5443a1a620b404a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-19 10:09:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 15:17:18","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC839.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-06"},{"uniquename":"PMID:38163952","title":"REEPing the harvest of reticulophagy and nucleophagy.","citation":"Autophagy 2024 Jan 01;","abstract":"Under stress conditions, the endoplasmic reticulum and nucleus undergo turnover through selective macroautophagy/autophagy processes termed reticulophagy and nucleophagy, respectively. Our recent study has identified the protein Hva22/Rop1/Yep1, a member of the REEP1-REEP4 subfamily of the REEP protein family, as an essential factor for both processes in the fission yeast  Schizosaccharomyces pombe . In the absence of Hva22/Yep1, reticulophagy and nucleophagy cargos without surrounding autophagic membranes accumulate in the cytoplasm. Interestingly, human proteins in the REEP1-REEP4 subfamily can functionally substitute for Hva22/Yep1 to facilitate reticulophagy. Phylogenetic and synteny analyses further reveal that the budding yeast reticulophagy receptor Atg40 is also a REEP1-REEP4 subfamily member. Similar to human REEP1-REEP4 subfamily proteins, Atg40 can functionally replace Hva22/Yep1. Based on our findings, we propose that promoting reticulophagy is a conserved function of REEP1-REEP4 subfamily proteins.","doi":"10.1080/15548627.2023.2300915","authors":"Zou CX, Du LL","authors_abbrev":"Zou CX et al.","pubmed_publication_date":"01 Jan 2024","pubmed_entrez_date":"2024-01-02","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-01-03 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1361173","title":"Isolation and analysis of the fission yeast gene encoding polymerase delta accessory protein PCNA.","citation":"EMBO J 1992 Dec;11(13):5111-20","abstract":"Five monoclonal antibodies raised against rat PCNA cross-reacted with a similar protein in the fission yeast Schizosaccharomyces pombe. One of these was used to screen an S.pombe cDNA expression library. An incomplete cDNA was isolated and used to screen a genomic library, identifying a single gene, designated pcn1+ (proliferating cell nuclear antigen). The gene encodes a protein of 260 amino acids, with a deduced sequence 52% identical to human and rat PCNAs, which are 98.5% identical to each other. The budding yeast PCNA homologue POL30 is only 35% identical to the human and rat proteins. Pcn1 has a region near the C-terminus of particularly high homology to higher eukaryotic PCNA proteins. pcn1+ is essential for viability and delta pcn1 cells undergo aberrant DNA replication before cell cycle arrest. Overproduction of the protein leads to cell cycle delay in G2. Disruption of pcn1+ is complemented by the human PCNA gene, demonstrating that these genes are functional homologues.","authors":"Waseem NH, Labib K, Nurse P, Lane DP","authors_abbrev":"Waseem NH et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"68f20cc081d78bc5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 14:16:42","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-28 14:45:30","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-28"},{"uniquename":"PMID:41020877","title":"Checkpoint-Dependent Sensitivities to Nucleoside Analogues Uncover Specific Patterns of Genomic Instability.","citation":"Curr Issues Mol Biol 2025 Sep 12;47(9)","abstract":"Nucleoside analogues are used as drugs and as labels in laboratory-based research. However, the effect of different nucleoside analogue mechanism(s) on cell sensitivity or mutagenesis is unclear. This is particularly important in cancer treatments where checkpoint proteins and DNA damage factors are often mutated. We tested six nucleoside analogues in fission yeast,  Schizosaccharomyces pombe . We found that the mutations in the DNA replication checkpoint cause unique sensitivity profiles towards chemotherapeutic nucleoside analogues (gemcitabine, 5-fluorouracil, cytarabine) and the non-clinical analogue bromodeoxyuridine. Antiretroviral compounds, zidovudine and lamivudine, did not alter cell growth. We compared half-maximal inhibitory concentration (IC50) doses between checkpoint deficient yeast strains, examining culture growth and DNA mis-segregation. Intriguingly, gemcitabine and bromodeoxyuridine doses above the IC50 promoted better growth. Above each compound's IC50 dose we saw that cells were insensitive to nucleoside analogue re-exposure, particularly in DNA replication checkpoint mutants ( cds1∆ ,  rad3∆ ). Thus, pairing nucleoside analogue use with personal genomics may inform drug choice, dose, and schedule. Finally, these data indicate that resistance may be predictable, informing clinical strategy.","doi":"10.3390/cimb47090756","authors":"Kagalwala ZB, Chhipa MA, Kianfard Z, Karam E, Magalage SP, Sabatinos SA","authors_abbrev":"Kagalwala ZB et al.","pubmed_publication_date":"12 Sep 2025","pubmed_entrez_date":"2025-09-29","publication_year":"2025","canto_session_key":"f66a4cee258c5e1a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-29 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26624998","title":"Schizosaccharomyces pombe Homologs of Human DJ-1 Are Stationary Phase-Associated Proteins That Are Involved in Autophagy and Oxidative Stress Resistance.","citation":"PLoS One 2015;10(12):e0143888","abstract":"The Parkinson's disease protein DJ-1 is involved in various cellular functions including detoxification of dicarbonyl compounds, autophagy and oxidative stress response. DJ-1 homologs are widely found in both prokaryotes and eukaryotes, constituting a superfamily of proteins that appear to be involved in stress response. Schizosaccharomyces pombe contains six DJ-1 homologs, designated Hsp3101-Hsp3105 and Sdj1 (previously named SpDJ-1). Here we show that deletion of any one of these six genes somehow affects autophagy during prolonged stationary phase. Furthermore, deletions of each of these DJ-1 homologs result in reduced stationary phase survival. Deletion of sdj1 also increases the sensitivity of stationary-phase cells to oxidative stress induced by hydrogen peroxide (H2O2) whereas overexpression of sdj1 has the opposite effect. Consistent with their role in stationary phase, expression of hsp3101, hsp3102, hsp3105 and sdj1, and to a lesser extent hsp3103 and hsp3104, is increased in stationary phase. The induction of hsp3101, hsp3102, hsp3105 and sdj1 involves the Sty1-regulated transcription factor Atf1 but not the transcription factor Pap1. Our results firmly establish that S. pombe homologs of DJ-1 are stationary-phase associated proteins and are likely involved in autophagy and antioxidant defense in stationary phase of S. pombe cells.","doi":"10.1371/journal.pone.0143888","authors":"Su Y, Chen C, Huang L, Yan J, Huang Y","authors_abbrev":"Su Y et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-12-02","publication_year":"2015","canto_session_key":"3d98754ebb44d4fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-02-03 14:12:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-01-21 11:04:51","canto_added_date":"2015-12-03 01:19:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC757.03c","SPBC29B5.01","SPBC4B4.10c","SPAC22E12.03c","SPAC5H10.02c","SPAC11D3.13","SPBP8B7.24c","SPAC1F7.06","SPAC24B11.06c","SPBC947.09"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2016-01-21"},{"uniquename":"PMID:20634313","title":"Confining euchromatin/heterochromatin territory: jumonji crosses the line.","citation":"Genes Dev 2010 Jul 15;24(14):1465-78","abstract":"Heterochromatin is typically highly condensed, gene-poor, and transcriptionally silent, whereas euchromatin is less condensed, gene-rich, and more accessible to transcription. Besides acting as a graveyard for selfish mobile DNA repeats, heterochromatin contributes to important biological functions, such as chromosome segregation during cell division. Multiple features of heterochromatin-including the presence or absence of specific histone modifications, DNA methylation, and small RNAs-have been implicated in distinguishing heterochromatin from euchromatin in various organisms. Cells malfunction if the genome fails to restrict repressive chromatin marks within heterochromatin domains. How euchromatin and heterochromatin territories are confined remains poorly understood. Recent studies from the fission yeast Schizosaccharomyces pombe, the flowering plant Arabidopsis thaliana, and the filamentous fungus Neurospora crassa have revealed a new role for Jumonji C (JmjC) domain-containing proteins in protecting euchromatin from heterochromatin marks.","doi":"10.1101/gad.1941010","authors":"Tamaru H","authors_abbrev":"Tamaru H","pubmed_publication_date":"15 Jul 2010","pubmed_entrez_date":"2010-07-17","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733397","title":"Transformation of  Schizosaccharomyces pombe  in a 96-Well Format.","citation":"Cold Spring Harb Protoc 2018 Jan 02;2018(1)","abstract":"This protocol describes chemical transformation of  Schizosaccharomyces pombe  with linear DNA in a 96-well format. This procedure has been successfully used for large-scale strain construction in fission yeast.","doi":"10.1101/pdb.prot091942","authors":"Roguev A, Xu J, Krogan NJ","authors_abbrev":"Roguev A et al.","pubmed_publication_date":"02 Jan 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8464724","title":"Evolutionary conservation of excision repair in Schizosaccharomyces pombe: evidence for a family of sequences related to the Saccharomyces cerevisiae RAD2 gene.","citation":"Nucleic Acids Res 1993 Mar 25;21(6):1345-9","abstract":"Cells mutated at the rad13 locus in the fission yeast, Schizosaccharomyces pombe are deficient in excision-repair of UV damage. We have cloned the S.pombe rad13 gene by its ability to complement the UV sensitivity of a rad13 mutant. The gene is not essential for cell proliferation. Sequence analysis of the cloned gene revealed an open reading-frame of 1113 amino acids with structural homology to the RAD2 gene of the distantly related Saccharomyces cerevisiae. The sequence similarity is confined to three domains, two close to the N-terminus of the encoded protein, the third being close to the C-terminus. The central region of about 500 amino acids shows little similarity between the two organisms. The first and third domains are also found in a related yet distinct pair of homologous S.pombe/S.cerevisiae DNA repair genes (rad2/YKL510), which have only a very short region between these two conserved domains. Using the polymerase chain reaction with degenerate primers, we have isolated fragments from a gene homologous to rad13/RAD2 from Aspergillus nidulans. These findings define new functional domains involved in excision-repair, as well as identifying a conserved family of genes related to RAD2.","authors":"Carr AM, Sheldrick KS, Murray JM, al-Harithy R, Watts FZ, Lehmann AR","authors_abbrev":"Carr AM et al.","pubmed_publication_date":"25 Mar 1993","pubmed_entrez_date":"1993-03-25","publication_year":"1993","canto_session_key":"7c109baab1ed9c77","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-05-20 15:32:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-20 15:32:28","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-20"},{"uniquename":"PMID:35666203","title":"A yeast suppressor screen links Coa4 to the mitochondrial copper delivery pathway for cytochrome c oxidase.","citation":"Genetics 2022 Jul 30;221(4)","abstract":"Cytochrome c oxidase (CcO) is a multimeric copper-containing enzyme of the mitochondrial respiratory chain that powers cellular energy production. The two core subunits of cytochrome c oxidase, Cox1 and Cox2, harbor the catalytic CuB and CuA sites, respectively. Biogenesis of each copper site occurs separately and requires multiple proteins that constitute the mitochondrial copper delivery pathway. Currently, the identity of all the members of the pathway is not known, though several evolutionarily conserved twin CX9C motif-containing proteins have been implicated in this process. Here, we performed a targeted yeast suppressor screen that placed Coa4, a twin CX9C motif-containing protein, in the copper delivery pathway to the Cox1 subunit. Specifically, we show that overexpression of Cox11, a copper metallochaperone required for the formation of CuB site, can restore Cox1 abundance, cytochrome c oxidase assembly, and mitochondrial respiration in coa4Δ cells. This rescue is dependent on the copper-coordinating cysteines of Cox11. The abundance of Coa4 and Cox11 in mitochondria is reciprocally regulated, further linking Coa4 to the CuB site biogenesis. Additionally, we find that coa4Δ cells have reduced levels of copper and exogenous copper supplementation can partially ameliorate its respiratory-deficient phenotype, a finding that connects Coa4 to cellular copper homeostasis. Finally, we demonstrate that human COA4 can replace the function of yeast Coa4 indicating its evolutionarily conserved role. Our work provides genetic evidences for the role of Coa4 in the copper delivery pathway to the CuB site of cytochrome c oxidase.","doi":"10.1093/genetics/iyac090","authors":"Swaminathan AB, Soma S, Vicary AC, Zulkifli M, Kaur H, Gohil VM","authors_abbrev":"Swaminathan AB et al.","pubmed_publication_date":"30 Jul 2022","pubmed_entrez_date":"2022-06-06","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPMIT.01","SPCC550.01c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"EMBL:AU010352","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16593556","title":"Negative control for the initiation of meiosis in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1985 Apr;82(8):2447-51","abstract":"Temperature-sensitive mutants of the pat1 gene of Schizosaccharomyces pombe are able to produce poorly viable spores from the haploid state without the requirement for nitrogen starvation if exposed to the restrictive temperature. Three lines of evidence strongly suggest that this gene codes for a factor whose physiological role is inhibition of initiation of meiosis. First, pat1 haploids arrested in G(1) phase undergo apparent premeiotic DNA synthesis at the restrictive temperature. Second, the pat1 gene was found to exert its function at a specified stage of the meiotic pathway by comparison with other meiotic mutants. Third, meiotic recombination and chromosome segregation take place quite normally in pat1 diploids at the restrictive temperature, resulting in the production of highly viable spores. A negative control mechanism for meiosis is proposed.","authors":"Iino Y, Yamamoto M","authors_abbrev":"Iino Y et al.","pubmed_publication_date":"Apr 1985","pubmed_entrez_date":"1985-04-01","publication_year":"1985","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23185032","title":"Nonmedially assembled F-actin cables incorporate into the actomyosin ring in fission yeast.","citation":"J Cell Biol 2012 Nov 26;199(5):831-47","abstract":"In many eukaryotes, cytokinesis requires the assembly and constriction of an actomyosin-based contractile ring. Despite the central role of this ring in cytokinesis, the mechanism of F-actin assembly and accumulation in the ring is not fully understood. In this paper, we investigate the mechanism of F-actin assembly during cytokinesis in Schizosaccharomyces pombe using lifeact as a probe to monitor actin dynamics. Previous work has shown that F-actin in the actomyosin ring is assembled de novo at the division site. Surprisingly, we find that a significant fraction of F-actin in the ring was recruited from formin-Cdc12p nucleated long actin cables that were generated at multiple nonmedial locations and incorporated into the ring by a combination of myosin II and myosin V activities. Our results, together with findings in animal cells, suggest that de novo F-actin assembly at the division site and directed transport of F-actin cables assembled elsewhere can contribute to ring assembly.","doi":"10.1083/jcb.201209044","authors":"Huang J, Huang Y, Yu H, Subramanian D, Padmanabhan A, Thadani R, Tao Y, Tang X, Wedlich-Soldner R, Balasubramanian MK","authors_abbrev":"Huang J et al.","pubmed_publication_date":"26 Nov 2012","pubmed_entrez_date":"2012-11-28","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F5.04c","SPCC895.05","SPCC645.05c","SPBC2D10.14c","SPAC24H6.05"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:22645662","title":"Hexanucleotide motifs mediate recruitment of the RNA elimination machinery to silent meiotic genes.","citation":"Open Biol 2012 Mar;2(3):120014","abstract":"The selective elimination system blocks the accumulation of meiosis-specific mRNAs during the mitotic cell cycle in fission yeast. These mRNAs harbour a region, the determinant of selective removal (DSR), which is recognized by a YTH-family RNA-binding protein, Mmi1. Mmi1 directs target transcripts to destruction in association with nuclear exosomes. Hence, the interaction between DSR and Mmi1 is crucial to discriminate mitosis from meiosis. Here, we show that Mmi1 interacts with repeats of the hexanucleotide U(U/C)AAAC that are enriched in the DSR. Disruption of this 'DSR core motif' in a target mRNA inhibits its elimination. Tandem repeats of the motif can function as an artificial DSR. Mmi1 binds to it in vitro. Thus, a core motif cluster is responsible for the DSR activity. Furthermore, certain variant hexanucleotide motifs can augment the function of the DSR core motif. Notably, meiRNA, which composes the nuclear Mei2 dot required to suppress Mmi1 activity during meiosis, carries numerous copies of the core/augmenting motifs on its tail and is indeed degraded by the Mmi1/exosome system, indicating its likely role as decoy bait for Mmi1.","doi":"10.1098/rsob.120014","authors":"Yamashita A, Shichino Y, Tanaka H, Hiriart E, Touat-Todeschini L, Vavasseur A, Ding DQ, Hiraoka Y, Verdel A, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"Mar 2012","pubmed_entrez_date":"2012-05-31","publication_year":"2012","canto_session_key":"1b9f8877ac3cba92","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29423854","title":"Wide-band Electrical Impedance Spectroscopy (EIS) Measures S. pombe Cell Growth in vivo.","citation":"Methods Mol Biol 2018;1721:135-153","abstract":"This chapter describes a microfluidic device that enables immobilization and culturing of single rod-shaped S. pombe cells in a stand-up mode. The wide-band electrical impedance spectroscopy (EIS) has been integrated in the microfluidic device to continuously measure cell growth of single S. pombe cells. Cell growth curves showing cellular and intracellular features at high spatiotemporal resolution can be obtained from EIS signals. The features include longitudinal cell elongation in the G2 phase, mitosis, and cell division during an entire cell cycle of S. pombe cells. Microfluidics-based EIS systems provide, hence, a tool for dynamic single-cell studies.","doi":"10.1007/978-1-4939-7546-4_13","authors":"Zhu Z, Frey O, Hierlemann A","authors_abbrev":"Zhu Z et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35640578","title":"Ccr4-Not complex reduces transcription efficiency in heterochromatin.","citation":"Nucleic Acids Res 2022 Jun 10;50(10):5565-5576","abstract":"Heterochromatic silencing is thought to occur through a combination of transcriptional silencing and RNA degradation, but the relative contribution of each pathway is not known. In this study, we analyzed RNA Polymerase II (RNA Pol II) occupancy and levels of nascent and steady-state RNA in different mutants of Schizosaccharomyces pombe, in order to quantify the contribution of each pathway to heterochromatic silencing. We found that transcriptional silencing consists of two components, reduced RNA Pol II accessibility and, unexpectedly, reduced transcriptional efficiency. Heterochromatic loci showed lower transcriptional output compared to euchromatic loci, even when comparable amounts of RNA Pol II were present in both types of regions. We determined that the Ccr4-Not complex and H3K9 methylation are required for reduced transcriptional efficiency in heterochromatin and that a subset of heterochromatic RNA is degraded more rapidly than euchromatic RNA. Finally, we quantified the contribution of different chromatin modifiers, RNAi and RNA degradation to each silencing pathway. Our data show that several pathways contribute to heterochromatic silencing in a locus-specific manner and reveal transcriptional efficiency as a new mechanism of silencing.","doi":"10.1093/nar/gkac403","authors":"Monteagudo-Mesas P, Brönner C, Kohvaei P, Amedi H, Canzar S, Halic M","authors_abbrev":"Monteagudo-Mesas P et al.","pubmed_publication_date":"10 Jun 2022","pubmed_entrez_date":"2022-05-31","publication_year":"2022","canto_session_key":"057726752bcf5e6f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-06-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007333","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1828464","title":"Isolation and characterization of Schizosaccharomyces pombe mutants defective in cell wall (1-3)beta-D-glucan.","citation":"J Bacteriol 1991 Jun;173(11):3456-62","abstract":"Schizosaccharomyces pombe thermosensitive mutants requiring the presence of an osmotic stabilizer to survive and grow at a nonpermissive temperature were isolated. The mutants were genetically and biochemically characterized. In all of them, the phenotype segregated in Mendelian fashion as a single gene which coded for a recessive character. Fourteen loci were defined by complementation analysis. Studies of cell wall composition showed a reduction in the amount of cell wall beta-glucan in three strains (JCR1, JCR5, and JCR10) when growing at 37 degrees C. Galactomannan was diminished in two others. Strains JCR1 and JCR5, with mutant alleles cwg1-1 and cwg2-1, respectively, were further studied. The cwg1 locus was mapped on the right arm of chromosome III, 18.06 centimorgans (cM) to the left of the ade5 marker; cwg2 was located on the left arm of chromosome I, 34.6 cM away from the aro5 marker. (1-3)beta-D-Glucan synthase activities from cwg1-1 and cwg2-1 mutant strains grown at 37 degrees C were diminished, as measured in vitro, compared with the wild-type strain; however, Km values and activation by GTP were similar to the wild-type values. Mutant synthases behaved like the wild-type enzyme in terms of thermostability. Analyses of round shape, lytic behavior, and low (1-3)beta-D-glucan synthase activity in cultures derived from ascospores of the same tetrad showed cosegregation of all these characters. Detergent dissociation of (1-3)beta-D-glucan synthase into soluble and particulate fractions and subsequent reconstitution demonstrated that the cwg1-1 mutant was affected in the particulate fraction of the enzymatic activity while cwg2-1 was affected in the soluble component. The antifungal agents Papulacandin B and Aculeacin A had similar effects on the enzymatic activities of the wild type and the cwg2-1 mutant strain, whereas the cwg1-1 mutant, when growing at 37 degrees C, had a more inhibitor-resistant (1,3)beta-D-glucan synthase. It is concluded that the cwg1+ and cwg2+ genes are related to (1,3)beta-D-glucan biosynthesis.","authors":"Ribas JC, Diaz M, Duran A, Perez P","authors_abbrev":"Ribas JC et al.","pubmed_publication_date":"Jun 1991","pubmed_entrez_date":"1991-06-01","publication_year":"1991","canto_session_key":"1999a5fbfad09eed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-12-12 15:34:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-12 15:11:28","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.02c","SPAC2E1P5.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-06-12"},{"uniquename":"PMID:39054315","title":"Epigenetic memory is governed by an effector recruitment specificity toggle in Heterochromatin Protein 1.","citation":"Nat Commun 2024 Jul 25;15(1):6276","abstract":"HP1 proteins are essential for establishing and maintaining transcriptionally silent heterochromatin. They dimerize, forming a binding interface to recruit diverse chromatin-associated factors. Although HP1 proteins are known to rapidly evolve, the extent of variation required to achieve functional specialization is unknown. To investigate how changes in amino acid sequence impacts heterochromatin formation, we performed a targeted mutagenesis screen of the S. pombe HP1 homolog, Swi6. Substitutions within an auxiliary surface adjacent to the HP1 dimerization interface produce Swi6 variants with divergent maintenance properties. Remarkably, substitutions at a single amino acid position lead to the persistent gain or loss of epigenetic inheritance. These substitutions increase Swi6 chromatin occupancy in vivo and altered Swi6-protein interactions that reprogram H3K9me maintenance. We show how relatively minor changes in Swi6 amino acid composition in an auxiliary surface can lead to profound changes in epigenetic inheritance providing a redundant mechanism to evolve HP1-effector specificity.","doi":"10.1038/s41467-024-50538-z","authors":"Ames A, Seman M, Larkin A, Raiymbek G, Chen Z, Levashkevich A, Kim B, Biteen JS, Ragunathan K","authors_abbrev":"Ames A et al.","pubmed_publication_date":"25 Jul 2024","pubmed_entrez_date":"2024-07-25","publication_year":"2024","canto_session_key":"e6a5a918f3a3181a","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-07-26 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14968130","title":"eIF4E isoform 2 in Schizosaccharomyces pombe is a novel stress-response factor.","citation":"EMBO Rep 2004 Mar;5(3):311-6","abstract":"Cap-binding proteins of the elF4E family are generally involved in mediating ribosome recruitment to capped mRNA via an interaction with the initiation factor elF4G. However, Schizosaccharomyces pombe has two elF4E isoforms, one of which (elF4E2, encoded by tif452) has a relatively low affinity for elF4G. We show that tif452 is required for specific stress responses. An S. pombe, tif452delta mutant manifests slow growth under conditions of nutrient, temperature and salt stress. elF4E2 shows a distinct subcellular distribution to elF4E1, the cap-binding factor that is required for mainstream translation. In response to salt stress, the cellular level of elF4E2 increases, whereas the amount of intact elF4G decreases, leaving elF4E2 as the predominant elF4E isoform in a cell deficient in ElF4G. The presence of elF4E2 modifies the competence of S. pombe ribosomes to translate mRNAs with structured leaders in vivo. The tif452 promoter has putative stress-response (T-rich) motifs, whereas elF4E2 seems to be a new type of stress-response factor.","authors":"Ptushkina M, Malys N, McCarthy JE","authors_abbrev":"Ptushkina M et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-02-18","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16E8.15","SPBC1709.18"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"EMBL:SPAB1290","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18028193","title":"Biochemical characterization and structural prediction of a novel cytosolic leucyl aminopeptidase of the M17 family from Schizosaccharomyces pombe.","citation":"FEBS J 2007 Dec;274(23):6228-40","abstract":"A new leucyl aminopeptidase activity has been identified in the fission yeast Schizosaccharomyces pombe. The enzyme, which has been purified and named leucyl aminopeptidase yspII (LAP yspII), had a molecular mass of 320 and 54 kDa by gel filtration and SDS/PAGE, respectively, suggesting a homohexameric structure. The enzyme cleaved synthetic aminoacyl-4-nitroanilides at an optimum of pH 8.5, and preferred leucine and methionine as N-terminal amino acids. A clear dependence on Mn2+ concentration for activity was found, and an apparent association constant of 0.33 mM was calculated for the metal ion. Bestatin behaved as a competitive inhibitor of LAP yspII (K(i) = 0.14 microM), while chelating agents such as chloroquine, EDTA and 1,10-phenanthroline also reduced enzyme activity. A MALDI-MS analysis, followed by sequencing of two of the resulting peptides, showed that LAP yspII undoubtedly corresponds to the putative aminopeptidase C13A11.05 identified in the S. pombe genome project. The protein exhibited nearly 40% sequence identity to fungal and mammalian aminopeptidases belonging to the M17 family of metallopeptidases. Catalytic residues (Lys292 and Arg366), as well as those involved in coordination with the cocatalytic metal ions (Lys280, Asp285, Asp303, Asp362 and Glu364) and those forming the hydrophobic pocket for substrate binding (Met300, Asn360, Ala363, Thr390, Leu391, Ala483 and Met486), were perfectly conserved among all known aminopeptidases. The S. pombe enzyme is predicted to be formed two clearly distinguished domains with a well conserved C-terminal catalytic domain showing a characteristic topology of eight beta-sheets surrounded by alpha-helical segments in the form of a saddle.","authors":"Herrera-Camacho I, Rosas-Murrieta NH, Rojo-Domínguez A, Millán L, Reyes-Leyva J, Santos-López G, Suárez-Rendueles P","authors_abbrev":"Herrera-Camacho I et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-11-22","publication_year":"2007","canto_session_key":"d1588e24b70298cb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-05 13:53:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 10:03:22","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13A11.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-05"},{"uniquename":"PMID:10853365","title":"[Mechanism of interaction of ras with its effectors].","citation":"Seikagaku 2000 Apr;72(4):285-8","abstract":"","authors":"Kariya K, Kataoka T","authors_abbrev":"Kariya K et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-06-15","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2187435","title":"Purification and characterization of the invertase from Schizosaccharomyces pombe. A comparative analysis with the invertase from Saccharomyces cerevisiae.","citation":"Biochem J 1990 May 01;267(3):697-702","abstract":"Invertase (EC 3.2.1.26) was purified to homogeneity from exponentially growing cells of Schizosaccharomyces pombe fully de-repressed for synthesis of the enzyme, and was shown to be a high-molecular-mass glycoprotein that can be dissociated in the presence of 8 M-urea/1% SDS into identical subunits with an apparent molecular mass of 205 kDa. The carbohydrate moiety, accounting for 67% of the total mass, is composed of equimolar amounts of mannose and galactose. There is a small amount of glucosamine, which is probably involved in the linkage to the protein moiety, since the enzyme is sensitive to treatment with endoglycosidase H. The composition of the carbohydrate moiety resembles that found in higher-eukaryotic glycoproteins and differs from glycoproteins found in Saccharomyces cerevisiae. The protein portion of each subunit is a polypeptide of molecular mass 60 kDa, very similar to the invertase of Sacch. cerevisiae. Both proteins cross-react with antibodies raised against the protein fractions of the other, indicating that the two enzymes are similar.","authors":"Moreno S, Sanchez Y, Rodriguez L","authors_abbrev":"Moreno S et al.","pubmed_publication_date":"01 May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_session_key":"1ba5f0cb2104f77e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-01-28 17:41:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-26 14:03:31","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC191.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-26"},{"uniquename":"PMID:28684607","title":"Forces that shape fission yeast cells.","citation":"Mol Biol Cell 2017 Jul 07;28(14):1819-1824","abstract":"One of the major challenges of modern cell biology is to understand how cells are assembled from nanoscale components into micrometer-scale entities with a specific size and shape. Here I describe how our quest to understand the morphogenesis of the fission yeast  Schizosaccharomyces pombe  drove us to investigate cellular mechanics. These studies build on the view that cell shape arises from the physical properties of an elastic cell wall inflated by internal turgor pressure. Consideration of cellular mechanics provides new insights into not only mechanisms responsible for cell-shape determination and growth, but also cellular processes such as cytokinesis and endocytosis. Studies in yeast can help to illuminate approaches and mechanisms to study the mechanobiology of the cell surface in other cell types, including animal cells.","doi":"10.1091/mbc.E16-09-0671","authors":"Chang F","authors_abbrev":"Chang F","pubmed_publication_date":"07 Jul 2017","pubmed_entrez_date":"2017-07-08","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-07-09 00:15:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16093710","title":"The evolution of transposons in Schizosaccharomyces pombe.","citation":"Cytogenet Genome Res 2005;110(1-4):566-74","abstract":"Recent studies of the LTR-retrotransposons of Schizosaccharomyces pombe have shed considerable light on their evolution and function. The sequencing of the S. pombe genome allowed analysis of its transposon content. This analysis provides information about the maintenance and loss of transposons in the genome. The results of transposition assays and biochemical analyses demonstrate that the N-terminal protein of Tf1 is functionally equivalent to the Gag proteins of retroviruses and retrotransposons. Despite this conservation of function, the N-terminal protein of Tf1 lacks any sequence similarity to other known Gag proteins. Sequence analysis and experimental data also indicate that the Tf1 transposons of S. pombe target their integration into specific sites in the host genome. Transposition events resulting from the expression of Tf1 reveal a strong preference for intergenic regions, specifically at pol II promoters in a window 100-400 bp upstream of open reading frames. The complete and partial copies of Tf transposons in the sequenced genome of S. pombe show the same association of integration with promoter regions. This body of work explores how the transposon interacts with the host, the balance between the transposons propagation and loss, and how different families of transposons evolve.","authors":"Kelly FD, Levin HL","authors_abbrev":"Kelly FD et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-08-12","publication_year":"2005","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16258240","title":"The fission yeast gene encoding monothiol glutaredoxin 5 is regulated by nitrosative and osmotic stresses.","citation":"Mol Cells 2005 Aug 31;20(1):43-50","abstract":"Glutaredoxin (Grx) is a small, heat-stable redox protein acting as a multi-functional glutathione (GSH)-dependent disulfide oxidoreductase. We have cloned the monothiol Grx5 gene from the genomic DNA of the fission yeast Schizosaccharomyces pombe. It has 1,904 bp, with one intron, and encodes a putative protein of 146 amino acids with a molecular mass of 16.5 kDa. Recombinant Grx5 produced functional Grx in S. pombe cells. NO-generating sodium nitroprusside (SNP, 1.0 and 2.0 mM) and potassium chloride (KCl, 0.2 and 0.5 M) increased the synthesis of beta-galactosidase from a Grx5-lacZ fusion gene, and transcription of Grx5 was also enhanced by SNP and KCl. Synthesis of beta-galactosidase from the Grx5-lacZ fusion was lower in Pap1-negative TP108-3C cells than in wild type KP1 cells, and when Pap1 was overproduced in KP1 cells, the level of beta-galactosidase increased. We also found that Pap1 is involved in the induction of Grx5 by SNP and KCl. S. pombe Grx5 may play a crucial role in responses to nitrosative and osmotic stresses.","authors":"Kim HG, Park EH, Lim CJ","authors_abbrev":"Kim HG et al.","pubmed_publication_date":"31 Aug 2005","pubmed_entrez_date":"2005-11-01","publication_year":"2005","canto_session_key":"6faee029dd2c988c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:53:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-05 14:46:20","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAPB2B4.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-05"},{"uniquename":"PMID:36655493","title":"The kinesin-5 protein Cut7 moves bidirectionally on fission yeast spindles with activity that increases in anaphase.","citation":"J Cell Sci 2023 Mar 01;136(5)","abstract":"Kinesin-5 motors are essential to separate mitotic spindle poles and assemble a bipolar spindle in many organisms. These motors crosslink and slide apart antiparallel microtubules via microtubule plus-end-directed motility. However, kinesin-5 localization is enhanced away from antiparallel overlaps. Increasing evidence suggests this localization occurs due to bidirectional motility or trafficking. The purified fission-yeast kinesin-5 protein Cut7 moves bidirectionally, but bidirectionality has not been shown in cells, and the function of the minus-end-directed movement is unknown. Here, we characterized the motility of Cut7 on bipolar and monopolar spindles and observed movement toward both plus- and minus-ends of microtubules. Notably, the activity of the motor increased at anaphase B onset. Perturbations to microtubule dynamics only modestly changed Cut7 movement, whereas Cut7 mutation reduced movement. These results suggest that the directed motility of Cut7 contributes to the movement of the motor. Comparison of the Cut7 mutant and human Eg5 (also known as KIF11) localization suggest a new hypothesis for the function of minus-end-directed motility and spindle-pole localization of kinesin-5s.","doi":"10.1242/jcs.260474","authors":"Gergely ZR, Ansari S, Jones MH, Zhou B, Cash C, McIntosh R, Betterton MD","authors_abbrev":"Gergely ZR et al.","pubmed_publication_date":"01 Mar 2023","pubmed_entrez_date":"2023-01-19","publication_year":"2023","canto_session_key":"91cdd63cbc76d3f8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-01-20 01:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25G10.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU007152","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12773576","title":"A novel jmjC domain protein modulates heterochromatization in fission yeast.","citation":"Mol Cell Biol 2003 Jun;23(12):4356-70","abstract":"The heterochromatin domain at the mat locus of Schizosaccharomyces pombe is bounded by the IR-L and IR-R barriers. A genetic screen for mutations that promote silencing beyond IR-L revealed a novel gene named epe1, encoding a conserved nuclear protein with a jmjC domain. Disruption of epe1 promotes continuous spreading of heterochromatin-associated histone modifications and Swi6 binding to chromatin across heterochromatic barriers. It also enhances position effect variegation at heterochromatic domains, suppresses mutations in silencing genes, and stabilizes the repressed epigenetic state at the mat locus. However, it does not enhance silencing establishment. Our analysis suggests that the jmjC domain is essential for Epe1 activity and that Epe1 counteracts transcriptional silencing by negatively affecting heterochromatin stability. Consistent with this proposition, the meiotic stability of established heterochromatin beyond IR-L is diminished by Epe1 activity, and overexpression of Epe1 disrupts heterochromatin through acetylation of H3-K9 and H3-K14 and methylation of H3-K4. Furthermore, overexpression of Epe1 elevates the rate of chromosome loss. We propose that Epe1 helps control chromatin organization by down-regulating the stability of epigenetic marks that govern heterochromatization.","authors":"Ayoub N, Noma K, Isaac S, Kahan T, Grewal SI, Cohen A","authors_abbrev":"Ayoub N et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-05-30","publication_year":"2003","canto_session_key":"eaf06b3b341808fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-04-14 09:12:50","canto_approved_date":"2022-04-14 09:12:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-28 14:20:35","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.17","SPCC622.16c","SPBC800.03","SPBC2D10.17","SPBC36.05c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2022-04-14"},{"uniquename":"PMID:11042180","title":"The Cdc42p GTPase and its regulators Nrf1p and Scd1p are involved in endocytic trafficking in the fission yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 2001 Feb 02;276(5):3004-9","abstract":"Nrf1p was first identified in a screen for negative regulators of the Cdc42p GTPase. Overexpression of Nrf1p resulted in dose-dependent lethality, with cells exhibiting an ellipsoidal morphology and abnormal vacuolar phenotypes including an increase in vacuolar fusion. Green fluorescent protein (GFP)-Cdc42p and GFP-Nrf1p colocalized to vacuolar membranes and GFP-Nrf1p vacuolar localization depended on Scd1p, the Schizosaccharomyces pombe homolog of the Cdc24p guanine nucleotide exchange factor. In this study, site-directed mutagenesis was conducted on Nrf1p to determine its functional domains. Mutations in the three putative transmembrane domains resulted in mislocalization of GFP-Nrf1p and an inability to induce lethality, suggesting a loss of function. Mutations in the second extramembranous loop of Nrf1p also resulted in a loss of function and altered the ability of GFP-Nrf1p to localize to vacuolar membranes. Analysis of Deltanrf1 and Deltascd1 mutants revealed defects in endocytosis. In addition, overexpression of constitutively active Cdc42(G12V)p resulted in an increase in endocytosis and an ability to rescue the endocytic defects in Deltanrf1 and Deltascd1 cells. These data are consistent with Nrf1p and Scd1p being necessary for efficient endocytosis, possibly through the regulation of Cdc42p.","authors":"Murray JM, Johnson DI","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"02 Feb 2001","pubmed_entrez_date":"2000-10-24","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21B10.04c","SPAC110.03","SPAC16E8.09"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:19555350","title":"Functional conservation of tRNase ZL among Saccharomyces cerevisiae, Schizosaccharomyces pombe and humans.","citation":"Biochem J 2009 Aug 27;422(3):483-92","abstract":"Although tRNase Z from various organisms was shown to process nuclear tRNA 3' ends in vitro, only a very limited number of studies have reported its in vivo biological functions. tRNase Z is present in a short form, tRNase Z(S), and a long form, tRNase Z(L). Unlike Saccharomyces cerevisiae, which contains one tRNase Z(L) gene (scTRZ1) and humans, which contain one tRNase Z(L) encoded by the prostate-cancer susceptibility gene ELAC2 and one tRNase Z(S), Schizosaccharomyces pombe contains two tRNase Z(L) genes, designated sptrz1(+) and sptrz2(+). We report that both sptrz1(+) and sptrz2(+) are essential for growth. Moreover, sptrz1(+) is required for cell viability in the absence of Sla1p, which is thought to be required for endonuclease-mediated maturation of pre-tRNA 3' ends in yeast. Both scTRZ1 and ELAC2 can complement a temperature-sensitive allele of sptrz1(+), sptrz1-1, but not the sptrz1 null mutant, indicating that despite exhibiting species specificity, tRNase Z(L)s are functionally conserved among S. cerevisiae, S. pombe and humans. Overexpression of sptrz1(+), scTRZ1 and ELAC2 can increase suppression of the UGA nonsense mutation ade6-704 through facilitating 3' end processing of the defective suppressor tRNA that mediates suppression. Our findings reveal that 3' end processing is a limiting step for defective tRNA maturation and demonstrate that overexpression of sptrz1(+), scTRZ1 and ELAC2 can promote defective tRNA 3' processing in vivo. Our results also support the notion that yeast tRNase Z(L) is absolutely required for 3' end processing of at least a few pre-tRNAs even in the absence of Sla1p.","doi":"10.1042/BJ20090743","authors":"Zhao Z, Su W, Yuan S, Huang Y","authors_abbrev":"Zhao Z et al.","pubmed_publication_date":"27 Aug 2009","pubmed_entrez_date":"2009-06-27","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1D4.10"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:25308606","title":"Optimal conditions for mycelial growth of Schizosaccharomyces japonicus cells in liquid medium: it enables the molecular investigation of dimorphism.","citation":"Yeast 2014 Dec;31(12):475-82","abstract":"The non-pathogenic dimorphic fission yeast, Schizosaccharomyces japonicus, could be a suitable model organism for investigation of the genetic background of mycelial growth, as it has a haploid chromosome set and its genome is sequenced. Since earlier results have suggested that its morphological transition required solid substrates, but molecular biological experiments would require hyphae production in a liquid medium, we wanted to find circumstances which would enable hyphae production in liquid media. Several external conditions were investigated, but the strongest inducer was fetal bovine serum (FBS). Its positive effect could be hampered by heat and was dependent on pH, temperature and concentration of the serum. Other protein-containing compounds, such as peptone and bovine serum albumin or amino acids, proved to be ineffective or weak. Generally, the uninduced and induced mycelial growth of Sz. japonicus could be improved by lower external pH and higher temperature.","doi":"10.1002/yea.3048","authors":"Papp L, Sipiczki M, Holb IJ, Miklós I","authors_abbrev":"Papp L et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-10-14","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-10-15 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14602073","title":"Spatial and temporal pathway for assembly and constriction of the contractile ring in fission yeast cytokinesis.","citation":"Dev Cell 2003 Nov;5(5):723-34","abstract":"Microscopy of fluorescent fusion proteins and genetic dependencies show that fission yeast assemble and constrict a cytokinetic contractile ring in a precisely timed, sequential order. More than 90 min prior to separation of the spindle pole bodies (SPB), the anillin-like protein (Mid1p) migrates from the nucleus and specifies a broad band of cortex around the equator as the division site. Between 10 min before and 2 min after SPB separation, conventional myosin-II (Myo2p), IQGAP (Rng2p), PCH protein (Cdc15p), and formin (Cdc12p) join the broad band independent of actin filaments. Over the subsequent 10 min prior to anaphase B, this broad band of proteins condenses into a contractile ring including actin, tropomyosin (Cdc8p), and alpha-actinin (Ain1p). During anaphase B, unconventional myosin-II (Myp2p) joins the ring followed by the septin (Spn1p). Ring contraction and disassembly begin 37 min after SPB separation. This spatial and temporal hierarchy provides the framework for analysis of molecular mechanisms.","authors":"Wu JQ, Kuhn JR, Kovar DR, Pollard TD","authors_abbrev":"Wu JQ et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-11-07","publication_year":"2003","canto_session_key":"a3ae4b87ad040aa7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-03 15:32:41","canto_approved_date":"2019-11-26 20:49:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-03 15:32:30","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":38,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.13c","SPAC4A8.05c","SPAC4F10.11","SPAC27F1.02c","SPCC4B3.15","SPAC15A10.08","SPAP8A3.08","SPAC926.03","SPCC645.05c","SPAC1F5.04c","SPBC21.06c","SPAC20G8.05c","SPAC631.01c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2017-07-03"},{"uniquename":"PMID:22081013","title":"The Chp1-Tas3 core is a multifunctional platform critical for gene silencing by RITS.","citation":"Nat Struct Mol Biol 2011 Nov 13;18(12):1351-7","abstract":"RNA interference (RNAi) is critical for the assembly of heterochromatin at Schizosaccharomyces pombe centromeres. Central to this process is the RNA-induced initiation of transcriptional gene silencing (RITS) complex, which physically anchors small noncoding RNAs to chromatin. RITS includes Ago1, the chromodomain protein Chp1, and Tas3, which forms a bridge between Chp1 and Ago1. Chp1 is a large protein with no recognizable domains, apart from its chromodomain. Here we describe how the structured C-terminal half of Chp1 binds the Tas3 N-terminal domain, revealing the tight association of Chp1 and Tas3. The structure also shows a PIN domain at the C-terminal tip of Chp1 that controls subtelomeric transcripts through a post-transcriptional mechanism. We suggest that the Chp1-Tas3 complex provides a solid and versatile platform to recruit both RNAi-dependent and RNAi-independent gene-silencing pathways for locus-specific regulation of heterochromatin.","doi":"10.1038/nsmb.2151","authors":"Schalch T, Job G, Shanker S, Partridge JF, Joshua-Tor L","authors_abbrev":"Schalch T et al.","pubmed_publication_date":"13 Nov 2011","pubmed_entrez_date":"2011-11-15","publication_year":"2011","canto_session_key":"c3b81f2e0da5b138","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-16 16:25:55","canto_approved_date":"2023-02-16 16:25:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-16 16:19:29","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC212.11","SPAC18G6.02c","SPBC83.03c","SPBCPT2R1.08c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2023-02-16","pdb_entries":[{"pdb_id":"3tix","gene_chains":[{"gene_uniquename":"SPBC83.03c","chain":"A/A/C/C","position":"9-83"},{"gene_uniquename":"SPAC18G6.02c","chain":"B/D","position":"504-960"}],"title":"Crystal structure of the Chp1-Tas3 complex core","entry_authors":"Schalch T,Joshua-Tor L","entry_authors_abbrev":"Schalch T et al.","reference_uniquename":"PMID:22081013","experimental_method":"X-ray","resolution":"2.9001"}]},{"uniquename":"PMID:8945514","title":"Molecular mimicry in development: identification of ste11+ as a substrate and mei3+ as a pseudosubstrate inhibitor of ran1+ kinase.","citation":"Cell 1996 Nov 29;87(5):869-80","abstract":"ran1+ (pat1+) kinase inhibits exit from the mitotic cell cycle and entry into meiosis. Inactivation of ran1+ by mei3+ is sufficient to precipitate the entire meiotic developmental program. Here, we show that the ste11+ transcription factor is a substrate for ran1+ in vitro and that this reaction is directly inhibited by mei3+. Sequence comparison reveals that ste11+ contains two domains homologous to each other and to a domain of mei3+. Mutagenesis studies reveal that the regions of homology contain substrate specificity determinants. These results identify sequences critical for phosphorylation of ste11+ by ran1+ and suggest that mei3+ employs a pseudosubstrate mechanism for its inhibitory function.","authors":"Li P, McLeod M","authors_abbrev":"Li P et al.","pubmed_publication_date":"29 Nov 1996","pubmed_entrez_date":"1996-11-29","publication_year":"1996","canto_session_key":"871a9d64c37fd3c5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 09:40:26","canto_approved_date":"2026-04-08 11:02:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-05 19:28:57","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPBC119.04","SPBC19C2.05"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-06-10"},{"uniquename":"PMID:8631307","title":"Fission yeast cdc21, a member of the MCM protein family, is required for onset of S phase and is located in the nucleus throughout the cell cycle.","citation":"EMBO J 1996 Feb 15;15(4):861-72","abstract":"The fission yeast cdc21 protein belongs to the MCM family, implicated in the once per cell cycle regulation of chromosome replication. In budding yeast, proteins in this family are eliminated from the nucleus during S phase, which has led to the suggestion that they may serve to distinguish unreplicated from replicated DNA, as in the licensing factor model. We show here that, in contrast to the situation in budding yeast, cdc21 remains in the nucleus after S phase, as is found for related proteins in mammalian cells. We suggest that regulation of nuclear import of these proteins may not be an essential aspect of their function in chromosome replication. To determine the function of cdc21+, we have analysed the phenotype of a gene deletion. cdc21+ is required for entry into S phase and, unexpectedly, a proportion of cells depleted of the gene product are able to enter mitosis in the absence of DNA replication. These results are consistent with the view that individual proteins in the MCM family are required for all initiation events, and defective initiation may impair the coordination between mitosis and S phase.","authors":"Maiorano D, Van Assendelft GB, Kearsey SE","authors_abbrev":"Maiorano D et al.","pubmed_publication_date":"15 Feb 1996","pubmed_entrez_date":"1996-02-15","publication_year":"1996","canto_session_key":"602a4a67a16c36d5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-31 16:47:04","canto_approved_date":"2023-01-12 18:10:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-08 10:48:38","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07","SPBC11B10.09","SPCC16A11.17"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-01-31"},{"uniquename":"PMID:28096402","title":"Establishment of expression-state boundaries by Rif1 and Taz1 in fission yeast.","citation":"Proc Natl Acad Sci U S A 2017 Jan 31;114(5):1093-1098","abstract":"The Shelterin component Rif1 has emerged as a global regulator of the replication-timing program in all eukaryotes examined to date, possibly by modulating the 3D-organization of the genome. In fission yeast a second Shelterin component, Taz1, might share similar functions. Here, we identified unexpected properties for Rif1 and Taz1 by conducting high-throughput genetic screens designed to identify cis- and trans-acting factors capable of creating heterochromatin-euchromatin boundaries in fission yeast. The preponderance of cis-acting elements identified in the screens originated from genomic loci bound by Taz1 and associated with origins of replication whose firing is repressed by Taz1 and Rif1. Boundary formation and gene silencing by these elements required Taz1 and Rif1 and coincided with altered replication timing in the region. Thus, small chromosomal elements sensitive to Taz1 and Rif1 (STAR) could simultaneously regulate gene expression and DNA replication over a large domain, at the edge of which they established a heterochromatin-euchromatin boundary. Taz1, Rif1, and Rif1-associated protein phosphatases Sds21 and Dis2 were each sufficient to establish a boundary when tethered to DNA. Moreover, efficient boundary formation required the amino-terminal domain of the Mcm4 replicative helicase onto which the antagonistic activities of the replication-promoting Dbf4-dependent kinase and Rif1-recruited phosphatases are believed to converge to control replication origin firing. Altogether these observations provide an insight into a coordinated control of DNA replication and organization of the genome into expression domains.","doi":"10.1073/pnas.1614837114","authors":"Toteva T, Mason B, Kanoh Y, Brøgger P, Green D, Verhein-Hansen J, Masai H, Thon G","authors_abbrev":"Toteva T et al.","pubmed_publication_date":"31 Jan 2017","pubmed_entrez_date":"2017-01-19","publication_year":"2017","canto_session_key":"73e8cc4ec0f1e63c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-01-19 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1480481","title":"Cloning and characterization of rad21 an essential gene of Schizosaccharomyces pombe involved in DNA double-strand-break repair.","citation":"Nucleic Acids Res 1992 Dec 25;20(24):6605-11","abstract":"Analysis of the Schizosaccharomyces pombe chromosomes by pulsed field gel electrophoresis showed that the fission yeast has a very efficient DNA double-strand-break (dsb) repair system, which properly restores the three chromosomes after they are degraded by gamma-irradiation. The radiation-sensitive mutant rad21-45 is deficient in this repair pathway but is capable of cell-cycle arrest in G2 following DNA damage. We cloned the rad21 gene by complementing the radiation sensitivity of the rad21-45 mutant. The plasmid-borne gene completely reestablished the DNA dsb repair pathway. The rad21 gene was localized to chromosome III by hybridization. The transcript is 2.5 kb long and expressed at a moderate level. The 1884-bp open reading frame encodes a 628 amino acid, very acidic peptide with a calculated molecular mass of 67,854 D. The rad21 gene shows no significant homology to other known nucleotide or peptide sequences. The inability of the mutant to perform efficient DNA repair is caused by a single base substitution, which changes wild-type isoleucine67 into threonine in the mutant. Deletion of the genomic rad21 gene showed that it is essential for mitotic growth of S.pombe.","authors":"Birkenbihl RP, Subramani S","authors_abbrev":"Birkenbihl RP et al.","pubmed_publication_date":"25 Dec 1992","pubmed_entrez_date":"1992-12-25","publication_year":"1992","canto_session_key":"34e8b44e889fbf8e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-01-19 15:06:46","canto_approved_date":"2020-03-15 12:43:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-23 17:59:33","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-19"},{"uniquename":"PMID:12861001","title":"Identification of Cdc37 as a novel regulator of the stress-responsive mitogen-activated protein kinase.","citation":"Mol Cell Biol 2003 Aug;23(15):5132-42","abstract":"Eukaryotic cells utilize multiple mitogen-activated protein kinases (MAPKs) to transmit various extracellular stimuli to the nucleus. A subfamily of MAPKs that mediates environmental stress stimuli is also called stress-activated protein kinase (SAPK), which has crucial roles in cellular survival under stress conditions as well as inflammatory responses. Here we report that Cdc37, an evolutionarily conserved kinase-specific chaperone, is a positive regulator of Spc1 SAPK in the fission yeast Schizosaccharomyces pombe. Through a genetic screen, we have identified cdc37 as a mutation that compromises signaling through Spc1 SAPK. The Cdc37 protein physically interacts with Spc1, and the cdc37 mutation affects both the cellular level of the Spc1 protein and stress-induced Spc1 phosphorylation by Wis1 MAPK kinase (MAPKK). Consistently, expression of the stress response genes regulated by the Spc1 pathway is compromised in cdc37 mutant cells. On the other hand, a mutation in Hsp90, which often cooperates with Cdc37 in chaperoning protein kinases, does not affect Spc1 SAPK. These results suggest that Spc1 SAPK is a novel client protein for the Cdc37 chaperone, and the Cdc37 function is important to maintain the stability of the Spc1 protein and to facilitate stress signaling from Wis1 MAPKK to Spc1 SAPK.","authors":"Tatebe H, Shiozaki K","authors_abbrev":"Tatebe H et al.","pubmed_publication_date":"Aug 2003","pubmed_entrez_date":"2003-07-16","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC409.07c","SPBC9B6.10","SPAC24B11.06c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:26137436","title":"Uncleavable Nup98-Nup96 is functional in the fission yeast Schizosaccharomyces pombe.","citation":"FEBS Open Bio 2015;5:508-14","abstract":"Essential nucleoporins Nup98 and Nup96 are coded by a single open reading frame, and produced by autopeptidase cleavage. The autocleavage site of Nup98-Nup96 is highly conserved in a wide range of organisms. To understand the importance of autocleavage, we examined a mutant that produces the Nup98-Nup96 joint molecule as a sole protein product of the nup189 (+) gene in the fission yeast Schizosaccharomyces pombe. Cells expressing only the joint molecule were found to be viable. This result indicates that autocleavage of Nup98-Nup96 is dispensable for cell growth, at least under normal culture conditions in S. pombe.","doi":"10.1016/j.fob.2015.06.004","authors":"Asakawa H, Mori C, Ohtsuki C, Iwamoto M, Hiraoka Y, Haraguchi T","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-07-03","publication_year":"2015","canto_session_key":"8b8d3cc2e5f5c371","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Haruhiko Asakawa","canto_first_approved_date":"2019-11-27 15:25:41","canto_approved_date":"2021-10-21 16:03:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-11-21 15:17:28","canto_added_date":"2015-07-04 00:22:00","annotation_curators":[{"name":"Haruhiko Asakawa","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1486.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-27"},{"uniquename":"PMID:20427284","title":"The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain.","citation":"J Biol Chem 2010 Jun 25;285(26):20390-8","abstract":"Proteins containing ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains interact with various binding partners and function as hubs during ubiquitin-mediated protein degradation. A common interaction of the budding yeast UBL-UBA proteins Rad23 and Dsk2 with the E4 ubiquitin ligase Ufd2 has been described in endoplasmic reticulum-associated degradation among other pathways. The UBL domains of Rad23 and Dsk2 play a prominent role in this process by interacting with Ufd2 and different subunits of the 26 S proteasome. Here, we report crystal structures of Ufd2 in complex with the UBL domains of Rad23 and Dsk2. The N-terminal UBL-interacting region of Ufd2 exhibits a unique sequence pattern, which is distinct from any known ubiquitin- or UBL-binding domain identified so far. Residue-specific differences exist in the interactions of these UBL domains with Ufd2, which are coupled to subtle differences in their binding affinities. The molecular details of their differential interactions point to a role for adaptive evolution in shaping these interfaces.","doi":"10.1074/jbc.M110.112532","authors":"Hänzelmann P, Stingele J, Hofmann K, Schindelin H, Raasi S","authors_abbrev":"Hänzelmann P et al.","pubmed_publication_date":"25 Jun 2010","pubmed_entrez_date":"2010-04-30","publication_year":"2010","canto_session_key":"99afd303a35d63ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-09-30 11:05:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-30 11:04:57","canto_added_date":"2016-09-21 00:19:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4F6.15c","SPAC26A3.16","SPAC20H4.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-09-30"},{"uniquename":"PMID:30755408","title":"Short-Homology-Mediated CRISPR/Cas9-Based Method for Genome Editing in Fission Yeast.","citation":"G3 (Bethesda) 2019 Apr 09;9(4):1153-1163","abstract":"The CRISPR/Cas9 system enables the editing of genomes of numerous organisms through the induction of the double-strand breaks (DSB) at specific chromosomal targets. We improved the CRISPR/Cas9 system to ease the direct introduction of a point mutation or a tagging sequence into the chromosome by combining it with the noncanonical homology-directed DNA repair (HDR) based genome editing in fission yeast. We constructed convenient cloning vectors, which possessed a guide RNA (gRNA) expression module, or the humanized  Streptococcus pyogenes Cas9  gene that is expressed under the control of an inducible promoter to avoid the needless expression, or both a gRNA and Cas9 gene. Using this system, we attempted the short-homology-mediated genome editing and found that the HDR pathway provides high-frequency genome editing at target loci without the need of a long donor DNA. Using short oligonucleotides, we successfully introduced point mutations into two target genes at high frequency. We also precisely integrated the sequences for epitope and GFP tagging using donor DNA possessing short homology into the target loci, which enabled us to obtain cells expressing N-terminally tagged fusion proteins. This system could expedite genome editing in fission yeast, and could be applicable to other organisms.","doi":"10.1534/g3.118.200976","authors":"Hayashi A, Tanaka K","authors_abbrev":"Hayashi A et al.","pubmed_publication_date":"09 Apr 2019","pubmed_entrez_date":"2019-02-14","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-02-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8313888","title":"cdt1 is an essential target of the Cdc10/Sct1 transcription factor: requirement for DNA replication and inhibition of mitosis.","citation":"EMBO J 1994 Jan 15;13(2):425-34","abstract":"We have used an immunoprecipitation-PCR cycle to isolate physically genomic DNA sequences that are bound by the fission yeast cdc10 gene product in an attempt to identify novel target genes. An essential gene, cdt1, has been isolated whose expression is cell cycle regulated in a cdc10 dependent manner. The cdt1 promoter contains a recognition site for a sequence specific DNA binding factor. The cdc10 gene product is a component of this factor. Ectopic expression of cdt1 can complement a temperature sensitive mutation of cdc10 at semipermissive temperature. Cells carrying a null allele of cdt1 are defective in DNA replication but initiate mitotic events, suggesting that cdt1 is essential for the normal dependency relationship of S-phase and mitosis.","authors":"Hofmann JF, Beach D","authors_abbrev":"Hofmann JF et al.","pubmed_publication_date":"15 Jan 1994","pubmed_entrez_date":"1994-01-15","publication_year":"1994","canto_session_key":"a8c06beb35abbf7d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-02-09 17:53:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-18 15:46:55","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPAC17H9.19c","SPAC1F7.05","SPBC428.18"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2014-09-18"},{"uniquename":"PMID:10407266","title":"A systematic nomenclature for new translation initiation factor genes from S. pombe and other fungi.","citation":"Yeast 1999 Jul;15(10A):865-72","abstract":"Eukaryotic translation initiation factors and their corresponding genes have been characterized using biochemical and genetic methods from a variety of different organisms. The designations of the factors relate to their apparent roles in the biochemical process. Many gene names indicate genetic interactions with other genes or the functional attributes used to identify them. On the other hand, progress in systematic sequencing of the genomes of organisms like Saccharomyces cerevisiae and Schizosaccharomyces pombe has revealed many genes homologous to known translation initiation factor genes. The genes defined by the systematic sequencing approach are assigned numerical designations completely unrelated to their biological function. So far there have been publications on only three genes encoding translation initiation factors from Schizosaccharomyces pombe. We therefore see this an an ideal opportunity to propose a systematic and logical nomenclature for genes encoding translation initiation factor genes that can be applied to all further genes of this type that are characterized in this fission yeast.","authors":"Linder P, Vornlocher HP, Hershey JW, McCarthy JE","authors_abbrev":"Linder P et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-17","publication_year":"1999","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012436","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12058018","title":"The endoplasmic reticulum cation P-type ATPase Cta4p is required for control of cell shape and microtubule dynamics.","citation":"J Cell Biol 2002 Jun 10;157(6):1029-39","abstract":"Here we describe the phenotypic characterization of the cta4+ gene, encoding a novel member of the P4 family of P-type ATPases of fission yeast. The cta4Delta mutant is temperature sensitive and cold sensitive lethal and displays several morphological defects in cell polarity and cytokinesis. Microtubules are generally destabilized in cells lacking Cta4p. The microtubule length is decreased, and the number of microtubules per cell is increased. This is concomitant with an increase in the number of microtubule catastrophe events in the midzone of the cell. These defects are likely due to a general imbalance in cation homeostasis. Immunofluorescence microscopy and membrane fractionation experiments revealed that green fluorescent protein-tagged Cta4 localizes to the ER. Fluorescence resonance energy transfer experiments in living cells using the yellow cameleon indicator for Ca2+ indicated that Cta4p regulates the cellular Ca2+ concentration. Thus, our results reveal a link between cation homeostasis and the control of cell shape, microtubule dynamics, and cytokinesis, and appoint Ca2+ as a key ion in controlling these processes.","authors":"Façanha AL, Appelgren H, Tabish M, Okorokov L, Ekwall K","authors_abbrev":"Façanha AL et al.","pubmed_publication_date":"10 Jun 2002","pubmed_entrez_date":"2002-06-12","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPACUNK4.07c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:21421748","title":"Grx4 monothiol glutaredoxin is required for iron limitation-dependent inhibition of Fep1.","citation":"Eukaryot Cell 2011 May;10(5):629-45","abstract":"The expression of iron transport genes in Schizosaccharomyces pombe is controlled by the Fep1 transcription factor. When iron levels exceed those needed by the cells, Fep1 represses iron transport genes. In contrast, Fep1 is unable to bind chromatin under low-iron conditions, and that results in activation of genes involved in iron acquisition. Studies of fungi have revealed that monothiol glutaredoxins are required to inhibit iron-dependent transcription factors in response to high levels of iron. Here, we show that the monothiol glutaredoxin Grx4 plays an important role in the negative regulation of Fep1 activity in response to iron deficiency. Deletion of the grx4(+) gene led to constitutive promoter occupancy by Fep1 and caused an invariable repression of iron transport genes. We found that Grx4 and Fep1 physically interact with each other. Grx4 contains an N-terminal thioredoxin (TRX)-like domain and a C-terminal glutaredoxin (GRX)-like domain. Deletion mapping analysis revealed that the TRX domain interacts strongly and constitutively with the C-terminal region of Fep1. As opposed to the TRX domain, the GRX domain associates weakly and in an iron-dependent manner with the N-terminal region of Fep1. Further analysis showed that Cys35 of Grx4 is required for the interaction between the Fep1 C terminus and the TRX domain, whereas Grx4 Cys172 is necessary for the association between the Fep1 N terminus and the GRX domain. Our results describe the first example of a monothiol glutaredoxin that acts as an inhibitory partner for an iron-regulated transcription factor under conditions of low iron levels.","doi":"10.1128/EC.00015-11","authors":"Jbel M, Mercier A, Labbé S","authors_abbrev":"Jbel M et al.","pubmed_publication_date":"May 2011","pubmed_entrez_date":"2011-03-23","publication_year":"2011","canto_session_key":"27d5ac7a6911a381","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23E2.01","SPAC18B11.10","SPBC26H8.06"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:16111683","title":"Free uptake of cell-penetrating peptides by fission yeast.","citation":"FEBS Lett 2005 Aug 29;579(21):4873-8","abstract":"An increasing number of peptides translocate the plasma membrane of mammalian cells promising new avenues for drug delivery. However, only a few examples are known to penetrate the fungal cell wall. We compared the capacity of different fluorophore-labelled peptides to translocate into fission yeast and human cells and determined their intracellular distribution. Most of the 20 peptides tested were able to enter human cells, but only one, transportan 10 (TP10), efficiently penetrated fission yeast and was distributed uniformly inside the cells. The results show that the fungal cell wall may reduce, but does not block peptide uptake.","authors":"Parenteau J, Klinck R, Good L, Langel U, Wellinger RJ, Elela SA","authors_abbrev":"Parenteau J et al.","pubmed_publication_date":"29 Aug 2005","pubmed_entrez_date":"2005-08-23","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9683500","title":"Multicellular stalk-like structures in Saccharomyces cerevisiae.","citation":"J Bacteriol 1998 Aug;180(15):3992-6","abstract":"Stalk formation is a novel pattern of multicellular organization. Yeast cells which survive UV irradiation form colonies that grow vertically to form very long (0.5 to 3.0 cm) and thin (0.5 to 4 mm in diameter) multicellular structures. We describe the conditions required to obtain these stalk-like structures reproducibly in large numbers. Yeast mutants, mutated for control of cell polarity, developmental processes, UV response, and signal transduction cascades were tested and found capable of forming stalk-like structures. We suggest a model that explains the mechanism of stalk formation by mechanical environmental forces. We show that other microorganisms (Candida albicans, Schizosaccharomyces pombe, and Escherichia coli) also form stalks, suggesting that the ability to produce stalks may be a general property of microorganisms. Diploid yeast stalks sporulate at an elevated frequency, raising the possibility that the physiological role of stalks might be disseminating spores.","authors":"Engelberg D, Mimran A, Martinetto H, Otto J, Simchen G, Karin M, Fink GR","authors_abbrev":"Engelberg D et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-07-31","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34682285","title":"Genome Comparisons of the Fission Yeasts Reveal Ancient Collinear Loci Maintained by Natural Selection.","citation":"J Fungi (Basel) 2021 Oct 14;7(10)","abstract":"Fission yeasts have a unique life history and exhibit distinct evolutionary patterns from other yeasts. Besides, the species demonstrate stable genome structures despite the relatively fast evolution of their genomic sequences. To reveal what could be the reason for that, comparative genomic analyses were carried out. Our results provided evidence that the structural and sequence evolution of the fission yeasts were correlated. Moreover, we revealed ancestral locally collinear blocks (aLCBs), which could have been inherited from their last common ancestor. These aLCBs proved to be the most conserved regions of the genomes as the aLCBs contain almost eight genes/blocks on average in the same orientation and order across the species. Gene order of the aLCBs is mainly fission-yeast-specific but supports the idea of filamentous ancestors. Nevertheless, the sequences and gene structures within the aLCBs are as mutable as any sequences in other parts of the genomes. Although genes of certain Gene Ontology (GO) categories tend to cluster at the aLCBs, those GO enrichments are not related to biological functions or high co-expression rates, they are, rather, determined by the density of essential genes and Rec12 cleavage sites. These data and our simulations indicated that aLCBs might not only be remnants of ancestral gene order but are also maintained by natural selection.","doi":"10.3390/jof7100864","authors":"Acs-Szabo L, Papp LA, Sipiczki M, Miklos I","authors_abbrev":"Acs-Szabo L et al.","pubmed_publication_date":"14 Oct 2021","pubmed_entrez_date":"2021-10-23","publication_year":"2021","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-10-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23412655","title":"Release of chromosomes from the nuclear envelope: a universal mechanism for eukaryotic mitosis?","citation":"Nucleus 2013;4(2):100-4","abstract":"Multiple domains of chromosomes are associated with the nuclear envelope (NE) in interphase. The association between chromosomes and the NE is involved in a variety of chromosomal reactions, such as gene expression and DNA repair. However, efficient chromosome movements are required for the fidelity of chromosome segregation in mitosis. Most higher eukaryotes perform open mitosis, in which the NE is broken down, enabling chromosomes to be released from the NE as well as spindle microtubules to access to kinetochores. By contrast, lower eukaryotes, such as Schizosaccharomyces pombe, perform closed mitosis, during which NE breakdown does not occur. In S. pombe, telomeres are tethered to the NE in interphase. Phosphorylation of the telomere-binding protein Rap1 at M phase promotes transient dissociation of telomeres from the NE, facilitating the faithful chromosome segregation. These findings imply a common mechanism for genome stability via the dissociation of chromosomes from the NE in eukaryotic mitosis.","doi":"10.4161/nucl.23984","authors":"Kanoh J","authors_abbrev":"Kanoh J","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-02-16","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18657501","title":"siRNA-mediated heterochromatin establishment requires HP1 and is associated with antisense transcription.","citation":"Mol Cell 2008 Jul 25;31(2):178-89","abstract":"Heterochromatic gene silencing at the pericentromeric DNA repeats in fission yeast requires the RNA interference (RNAi) machinery. The RNA-induced transcriptional silencing (RITS) complex mediates histone H3 lysine 9 (H3K9) methylation and recruits the RNA-dependent RNA polymerase complex (RDRC) to promote double-stranded RNA (dsRNA) synthesis and siRNA generation. Here we show that ectopic expression of a long hairpin RNA bypasses the requirement for chromatin-dependent steps in siRNA generation. The ability of hairpin-produced siRNAs to silence homologous sequences in trans is subject to local chromatin structure, requires HP1, and correlates with antisense transcription at the target locus. Furthermore, although hairpin siRNAs can be produced in the absence of RDRC, trans-silencing of reporter genes by hairpin-produced siRNAs is completely dependent on the dsRNA synthesis activity of RDRC. These results provide insights into the regulation of siRNA action and reveal roles for cis-dsRNA synthesis and HP1 in siRNA-mediated heterochromatin assembly.","doi":"10.1016/j.molcel.2008.07.003","authors":"Iida T, Nakayama J, Moazed D","authors_abbrev":"Iida T et al.","pubmed_publication_date":"25 Jul 2008","pubmed_entrez_date":"2008-07-29","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30824572","title":"Seeing is believing: DNA zipping promotes DNA repair.","citation":"J Biol Chem 2019 Mar 01;294(9):3321-3322","abstract":"DNA double-strand break repair by homologous recombination is initiated by the Ctp1 protein together with the Mre11-Rad50-Nbs1 nuclease complex in  Schizosaccharomyces pombe , but the mechanism by which Ctp1 promotes this process has remained unknown. Andres  et al.  now use atomic force microscopy to image Ctp1-DNA complexes, demonstrating a striking capacity of Ctp1 filaments to bridge DNA molecules. This unanticipated role of Ctp1 might help explain how the processing of DNA ends is coordinated to facilitate DNA break repair.","doi":"10.1074/jbc.H119.007814","authors":"Cejka P","authors_abbrev":"Cejka P","pubmed_publication_date":"01 Mar 2019","pubmed_entrez_date":"2019-03-03","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-03-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10582241","title":"Control of metaphase-anaphase progression by proteolysis: cyclosome function regulated by the protein kinase A pathway, ubiquitination and localization.","citation":"Philos Trans R Soc Lond B Biol Sci 1999 Sep 29;354(1389):1559-69; discussion 1569-70","abstract":"Ubiquitin-mediated proteolysis is fundamental to cell cycle progression. In the fission yeast Schizosaccharomyces pombe, a mitotic cyclin (Cdc13), a key cell cycle regulator, is degraded for exiting mitosis, while Cut2 has to be destroyed for the onset of sister chromatid separation in anaphase. Ubiquitination of these proteins requires the special destruction box (DB) sequences locating in their N-termini and the large, 20S complex called the anaphase-promoting complex or cyclosome. Here we show that cyclosome function during metaphase-anaphase progression is regulated by the protein kinase A (PKA) inactivation pathway, ubiquitination of the cyclosome subunit, and cellular localization of the target substrates. Evidence is provided that the cyclosome plays pleiotropic roles in the cell cycle: mutations in the subunit genes show a common anaphase defect, but subunit-specific phenotypes such as in G1/S or G2/M transition, septation and cytokinesis, stress response and heavy metal sensitivity, are additionally produced, suggesting that different subunits take distinct parts of complex cyclosome functions. Inactivation of PKA is important for the activation of the cyclosome for promoting anaphase, perhaps through dephosphorylation of the subunits such as Cut9 (Apc6). Cut4 (Apc1), the largest subunit, plays an essential role in the assembly and functional regulation of the cyclosome in response to cell cycle arrest and stresses. Cut4 is highly modified, probably by ubiquitination, when it is not assembled into the 20S cyclosome. Sds23 is implicated in DB-mediated ubiquitination possibly through regulating de-ubiquitination, while Cut8 is necessary for efficient proteolysis of Cdc13 and Cut2 coupled with cytokinesis. Unexpectedly, the timing of proteolysis is dependent on cellular localization of the substrate. Cdc13 enriched along the spindle disappears first, followed by decay of the nuclear signal, whereas Cut2 in the nucleus disappears first, followed by decline in the spindle signal during metaphase-anaphase progression.","authors":"Yanagida M, Yamashita YM, Tatebe H, Ishii K, Kumada K, Nakaseko Y","authors_abbrev":"Yanagida M et al.","pubmed_publication_date":"29 Sep 1999","pubmed_entrez_date":"1999-12-03","publication_year":"1999","canto_session_key":"ad3e7504599b65c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-04-08 15:15:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-03 16:23:16","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC14C8.01c","SPAC688.13","SPATRNAALA.02","SPBC1A4.01","SPBC4.07c","SPBC776.02c","SPAC6F12.15c","SPAC144.13c","SPAC19G12.01c","SPAC23C11.12","SPAC17C9.13c","SPAC17C9.01c","SPAPB2B4.03","SPCC5E4.04","SPBC646.13","SPCC31H12.05c","SPAC821.08c","SPBC106.09","SPAC6F12.14","SPBC16G5.01"],"gene_count":21,"ltp_gene_count":0,"approved_date":"2015-12-03"},{"uniquename":"EMBL:AU011994","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF087836","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.70"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23618667","title":"Small RNA-directed silencing: the fly finds its inner fission yeast?","citation":"Curr Biol 2013 Apr 22;23(8):R318-20","abstract":"Several recent studies demonstrate that piRNAs guide Piwi protein to repress transposon transcription in fly ovaries, much as fission yeast use siRNAs to silence repeat sequences. Still mysterious though is how Piwi targets euchromatic transposons for silencing, but not the specialized heterochromatic loci that produce piRNA precursors.","doi":"10.1016/j.cub.2013.03.033","authors":"Ge DT, Zamore PD","authors_abbrev":"Ge DT et al.","pubmed_publication_date":"22 Apr 2013","pubmed_entrez_date":"2013-04-27","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32866412","title":"Epr1, a UPR-upregulated soluble autophagy receptor for reticulophagy.","citation":"Autophagy 2020 Nov;16(11):2112-2113","abstract":"The endoplasmic reticulum (ER) is a major site of protein folding. Perturbations in the folding capacity of the ER result in ER stress. ER stress triggers autophagic degradation of the ER (reticulophagy). Molecular mechanisms underlying ER stress-induced reticulophagy remain largely unknown. Our recent study identified a soluble protein, Epr1, as an autophagy receptor for ER stress-induced reticulophagy in the fission yeast  Schizosaccharomyces pombe . Epr1 can interact simultaneously with Atg8 and a VAP family integral ER membrane protein, and thereby act as a bridging molecule between them. VAP family proteins contribute to reticulophagy by not only connecting Atg8 to the ER membrane through Epr1, but also by supporting the ER-plasma membrane contact. The expression of Epr1 is upregulated during ER stress in a manner dependent on the unfolded protein response (UPR) regulator Ire1. Ire1 promotes reticulophagy by upregulating Epr1.","doi":"10.1080/15548627.2020.1816665","authors":"Zhao D, Du LL","authors_abbrev":"Zhao D et al.","pubmed_publication_date":"Nov 2020","pubmed_entrez_date":"2020-09-01","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-09-02 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC167.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:5111493","title":"Characterization of spontaneous mutations of mitotic and meiotic origin in the ad-I locus of Schizosaccharomyces pombe.","citation":"Mutat Res 1971 Apr;11(4):373-90","abstract":"","authors":"Friis J, Flury F, Leupold U","authors_abbrev":"Friis J et al.","pubmed_publication_date":"Apr 1971","pubmed_entrez_date":"1971-04-01","publication_year":"1971","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7548848","title":"Pheromone communication in the fission yeast Schizosaccharomyces pombe.","citation":"Semin Cell Biol 1995 Apr;6(2):95-104","abstract":"Conjugation between two haploid yeast cells is generally controlled by the reciprocal action of diffusible mating pheromones, cells of each mating type releasing pheromones that induce mating-specific changes in cells of the opposite type. Recent studies into pheromone signalling in the fission yeast Schizosaccharomyces pombe have revealed significant parallels with processes in higher eukaryotes and could provide the opportunity for investigating communication in an organism that is amenable to both biochemical and genetic manipulation.","authors":"Nielsen O, Davey J","authors_abbrev":"Nielsen O et al.","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ002494","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28659415","title":"Single-molecule imaging of the BAR-domain protein Pil1p reveals filament-end dynamics.","citation":"Mol Biol Cell 2017 Aug 15;28(17):2251-2259","abstract":"Molecular assemblies can have highly heterogeneous dynamics within the cell, but the limitations of conventional fluorescence microscopy can mask nanometer-scale features. Here we adapt a single-molecule strategy to perform single-molecule recovery after photobleaching (SRAP) within dense macromolecular assemblies to reveal and characterize binding and unbinding dynamics within such assemblies. We applied this method to study the eisosome, a stable assembly of BAR-domain proteins on the cytoplasmic face of the plasma membrane in fungi. By fluorescently labeling only a small fraction of cellular Pil1p, the main eisosome BAR-domain protein in fission yeast, we visualized whole eisosomes and, after photobleaching, localized recruitment of new Pil1p molecules with ∼30-nm precision. Comparing our data to computer simulations, we show that Pil1p exchange occurs specifically at eisosome ends and not along their core, supporting a new model of the eisosome as a dynamic filament. This result is the first direct observation of any BAR-domain protein dynamics in vivo under physiological conditions consistent with the oligomeric filaments reported from in vitro experiments.","doi":"10.1091/mbc.E17-04-0238","authors":"Lacy MM, Baddeley D, Berro J","authors_abbrev":"Lacy MM et al.","pubmed_publication_date":"15 Aug 2017","pubmed_entrez_date":"2017-06-30","publication_year":"2017","canto_session_key":"1d8bd8c589d2c2ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Julien Berro","canto_first_approved_date":"2017-10-20 14:47:13","canto_approved_date":"2017-10-20 14:47:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-10-12 19:19:36","canto_added_date":"2017-07-01 00:15:15","annotation_curators":[{"name":"Julien Berro","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-10-20"},{"uniquename":"PMID:10428498","title":"The cta3+ gene that encodes a cation-transporting P-type ATPase is induced by salt stress under control of the Wis1-Sty1 MAPKK-MAPK cascade in fission yeast.","citation":"FEBS Lett 1999 Jul 16;455(1-2):183-7","abstract":"In Schizosaccharomyces pombe, the Wis1-Sty1 MAP (mitogen-activated protein) kinase signaling cascade is known to play a major role in cellular adaptation to adverse external stimuli, including osmotic stress, oxidative stress, nutrient deprivation, DNA-damaging agents, and heat stress. Nonetheless, it is not known whether or not this particular MAPK cascade is also involved in response to the most common stress, salinity. In this study, we provide evidence that the Wis1-Sty1 MAP cascade is implicated in salt stress response through regulating expression of a salinity-inducible gene. The downstream target gene thus identified is the cta3+ gene, which encodes a cation-transporting P-type ATPase. The salt stress-responsive nature of cta3+ expression was characterized extensively. It was found that not only the Sty1 MAP kinase but also the Atf1 transcription factor is crucial for the inducible expression of cta3+. As far as we know, this is the first instance that the stress-activated Wis1-Sty1 MAPK cascade plays a role in salt stress response in S. pombe.","authors":"Nishikawa T, Aiba H, Mizuno T","authors_abbrev":"Nishikawa T et al.","pubmed_publication_date":"16 Jul 1999","pubmed_entrez_date":"1999-07-31","publication_year":"1999","canto_session_key":"bffb1444f51ef68c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-07-11 16:36:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-07-11 16:36:10","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPBC839.06","SPAC24B11.06c","SPBC409.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2013-07-11"},{"uniquename":"PMID:9343385","title":"The fission yeast protein p73res2 is an essential component of the mitotic MBF complex and a master regulator of meiosis.","citation":"Mol Cell Biol 1997 Nov;17(11):6246-54","abstract":"Depending on environmental conditions, Schizosaccharomyces pombe can remain in the stationary phase or enter into either premitotic or premeiotic DNA synthesis. This decision point is known as Start. In the mitotic cell cycle, regulation of G1/S-specific gene expression is dependent upon the MBF (Mlu1 binding factor) complex, known to contain p85cdc10 and p72res1. Here we demonstrate that p73res2 controls cell cycle progression via its participation in the MBF complex, interacting directly with both p85cdc10 and p72res1. In contrast, when cells enter into meiosis, the MBF complex is disrupted, and p73res2 shifts its regulatory function towards the transactivation of genes required for meiotic progression. These observations suggest that p73res2 plays a pivotal role at Start and constitutes an example of a transcription factor involved in the control of both mitotic and meiotic progression.","authors":"Ayté J, Leis JF, DeCaprio JA","authors_abbrev":"Ayté J et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1997-10-29","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14612233","title":"Characterization of gdp1+ as encoding a GDPase in the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 2003 Nov 07;228(1):33-8","abstract":"We have isolated the gdp1+ gene from Schizosaccharomyces pombe coding for a membrane protein with guanosine diphosphatase (GDPase) activity, which is highly homologous to Golgi GDPases isolated from other yeast species. The gdp1+ product, Gdp1p, displays both GDPase and uridine diphosphatase (UDPase) activities in vitro, with a strong dependence for calcium and manganese cations. The observation of a defect in N-glycosylation of invertase in S. pombe Deltagdp1 cells together with the ability of gdp1+ to functionally complement the defective O-mannosylation of chitinase in Saccharomyces cerevisiae cells disrupted in the GDA1 gene (gdp1+ homolog), suggests a main role for Gdp1p in protein glycosylation in fission yeast.","authors":"Sánchez R, Franco A, Gacto M, Notario V, Cansado J","authors_abbrev":"Sánchez R et al.","pubmed_publication_date":"07 Nov 2003","pubmed_entrez_date":"2003-11-13","publication_year":"2003","canto_session_key":"e73b6293989d19a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-24 22:35:46","canto_approved_date":"2025-10-07 06:54:11","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-09-24 16:13:00","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC824.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-01-24"},{"uniquename":"PMID:8381348","title":"A Schizosaccharomyces pombe gene that promotes sexual differentiation encodes a helix-loop-helix protein with homology to MyoD.","citation":"EMBO J 1993 Jan;12(1):135-43","abstract":"Nitrogen starvation of Schizosaccharomyces pombe induces a differentiated state in which haploid cells mate and sporulate. esc1+, a newly isolated S.pombe cDNA that promotes this sexual differentiation, encodes a putative transcription factor with a helix-loop-helix (HLH) motif similar to those of the human MyoD and Myf-5 myogenic differentiation inducers. Disruption of esc1+ in wild-type cells leads to a decrease in the efficiency of sexual conjugation, an early step in sexual differentiation. The disruption was also able partially to substitute for cAMP, an inhibitor of differentiation, to suppress the lethal, constitutive differentiation induced by the pat1 mutation. Conversely, overexpression of this cDNA conferred partial resistance to cAMP-mediated inhibition of differentiation. Transcription from this novel gene was induced early in response to nitrogen starvation and is largely independent of the ste11+ gene product, which is required for the differentiation-specific expression of other genes. Thus, this MyoD/Myf-5-like protein appears to promote sexual differentiation by modulating responses to decreases in cAMP, a part of the nitrogen starvation signal that induces differentiation.","authors":"Benton BK, Reid MS, Okayama H","authors_abbrev":"Benton BK et al.","pubmed_publication_date":"Jan 1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_session_key":"b478004f654223f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-11 09:07:39","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-04 15:29:10","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC56F8.16","SPBC19C2.05","SPBC32C12.02"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-08-04"},{"uniquename":"EMBL:D82574","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24963143","title":"Cheaters divide and conquer.","citation":"Elife 2014 Jun 24;3:e03371","abstract":"Three 'killer genes' in one species of fission yeast act selfishly and keep it reproductively isolated from a closely related species.","doi":"10.7554/eLife.03371","authors":"Bomblies K","authors_abbrev":"Bomblies K","pubmed_publication_date":"24 Jun 2014","pubmed_entrez_date":"2014-06-26","publication_year":"2014","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-06-28 00:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6942947","title":"Mating-type switching and mitotic crossing-over at the mating-type locus in fission yeast.","citation":"Cold Spring Harb Symp Quant Biol 1981;45 Pt 2:1003-7","abstract":"","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"1981","pubmed_entrez_date":"1981-01-01","publication_year":"1981","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR10989","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:21214","HGNC:21607","SPBPJ4664.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1587480","title":"A homologue of the ras-related CDC42 gene from Schizosaccharomyces pombe.","citation":"Gene 1992 May 01;114(1):153-4","abstract":"A cDNA was isolated from the fission yeast, Schizosaccharomyces pombe, using mixed oligodeoxyribonucleotides encoding part of the GTP-binding site of the ras superfamily. The encoded protein is the homologue of the budding yeast CDC42 gene product and the human proteins, CDC42Hs and G25K.","authors":"Fawell E, Bowden S, Armstrong J","authors_abbrev":"Fawell E et al.","pubmed_publication_date":"01 May 1992","pubmed_entrez_date":"1992-05-01","publication_year":"1992","canto_session_key":"dd2a589f518527e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-04-26 21:33:55","canto_approved_date":"2019-04-26 21:33:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-04-26 21:33:48","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-04-26"},{"uniquename":"PMID:8196617","title":"Protein phosphatase 2C, encoded by ptc1+, is important in the heat shock response of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1994 Jun;14(6):3742-51","abstract":"Protein phosphatase 2C (PP2C), an Mg(2+)-dependent enzyme that dephosphorylates serine and threonine residues, defines one of the three major families of structurally unrelated eukaryotic protein phosphatases. Members of the two other families of protein phosphatases are known to have important cellular roles, but very little is known about the biological functions of PP2C. In this report we describe a genetic investigation of a PP2C enzyme in the fission yeast Schizosaccharomyces pombe. We discovered ptc1+ (phosphatase two C) as a multicopy suppressor gene of swo1-26, a temperature-sensitive mutation of a gene encoding the heat shock protein hsp90. The ptc1+ gene product is a 40-kDa protein with approximately 24% identity to a rat PP2C protein. Purified Ptc1 has Mg(2+)-dependent casein phosphatase activity, confirming that it is a PP2C enzyme. A ptc1 deletion mutant is viable and has approximately normal levels of PP2C activity, observations consistent with the fact that ptc1+ is a member of a multigene family. Although a ptc1 deletion mutant is viable, it has a greatly reduced ability to survive brief exposure to elevated temperature. Moreover, ptc1+ mRNA levels increase 5- to 10-fold during heat shock. These data, demonstrating that Ptc1 activity is important for survival of heat shock, provide one of the first genetic clues as to the biological functions of PP2C.","authors":"Shiozaki K, Akhavan-Niaki H, McGowan CH, Russell P","authors_abbrev":"Shiozaki K et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_session_key":"bfae08ac6cac7fd9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-27 01:27:04","canto_approved_date":"2019-08-15 10:41:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 16:52:08","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4F11.02","SPAC926.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-10-27"},{"uniquename":"PMID:41068270","title":"Acrylamide-mediated errors in the cell cycle regulation are associated with altered TORC2 signaling in Schizosaccharomyces pombe.","citation":"Sci Rep 2025 Oct 09;15(1):35310","abstract":"Acrylamide (AA) poses a significant risk to living organisms as it is linked to serious health concerns. AA exposure triggers oxidative stress in cells through elevated ROS and modulation of antioxidant enzymes activities and expression of genes encoding antioxidant enzymes. AA-induced cell proliferation defects are linked to affected cell cycle regulation demonstrated by changes in the expression of genes encoding the major cell cycle regulators cdc2, cdc13, and cdc25, Additionally, cell division defects can be linked to changes in the expression of ark1 and cdc15, and AA-induced errors in chromosome segregation. The stress response involves signaling pathways like MAPKs (Mitogen-activated protein kinases) or the target of rapamycin (TOR) constituting two complexes TORC 1 and 2. As TORC2 manages the cell response to various stresses, its involvement in AA-mediated stress has been demonstrated by changes in the expression of tor1, wat1, ste20, sin1, bit61 encoding TORC2 members, and gad8 encoding a direct Tor1substrate, Gad8. To our surprise, AA has not affected the expression of sty1, which encodes the major stress-regulating kinase of the MAPK pathway in S. pombe. In the presented study we demonstrate, for the first time, that exposure to AA disrupts cellular homeostasis by altering TORC2 signaling and cell cycle regulation ultimately leading to carcinogenesis.","doi":"10.1038/s41598-025-19367-y","authors":"Navrátilová A, Kovár M, Klongová L, Bakošová A, Peťková M, Požgajová M","authors_abbrev":"Navrátilová A et al.","pubmed_publication_date":"09 Oct 2025","pubmed_entrez_date":"2025-10-09","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-10 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31748542","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2019-11-24 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17032733","title":"S. pombe FEAR protein orthologs are not required for release of Clp1/Flp1 phosphatase from the nucleolus during mitosis.","citation":"J Cell Sci 2006 Nov 01;119(Pt 21):4462-6","abstract":"Cdc14 family phosphatases are highly conserved regulators of cell-cycle progression. Two of the best studied members of this family are budding yeast Cdc14p and its fission yeast homolog Clp1p/Flp1p. The function of both Saccharomyces cerevisiae Cdc14p and Schizosaccharomyces pombe Clp1p/Flp1p are controlled in part by their regulated sequestration and release from the nucleolus. In the budding yeast S. cerevisiae a set of proteins collectively termed the FEAR network promote nucleolar and telomeric DNA segregation by triggering the release of the conserved Cdc14 phosphatase from the nucleolus. Here we show that FEAR homologs in S. pombe do not promote release of the Cdc14 homolog Clp1p/Flp1p from the nucleolus, and that Clp1p/Flp1p is not required for nucleolar and telomeric DNA segregation suggesting that this aspect of Cdc14 regulation and function may not be universally conserved.","authors":"Chen CT, Peli-Gulli MP, Simanis V, McCollum D","authors_abbrev":"Chen CT et al.","pubmed_publication_date":"01 Nov 2006","pubmed_entrez_date":"2006-10-13","publication_year":"2006","canto_session_key":"9a2551eef2dc7907","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-30 12:46:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-30 12:46:06","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.15c","SPAC1782.09c","SPCC5E4.04","SPAC890.02c","SPAC24B11.11c","SPAC23C11.16"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-01-30"},{"uniquename":"PMID:23039831","title":"The process of kinetochore assembly in yeasts.","citation":"FEMS Microbiol Lett 2013 Jan;338(2):107-17","abstract":"High fidelity chromosome segregation is essential for efficient transfer of the genetic material from the mother to daughter cells. The kinetochore (KT), which connects the centromere DNA to the spindle apparatus, plays a pivotal role in this process. In spite of considerable divergence in the centromere DNA sequence, basic architecture of a KT is evolutionarily conserved from yeast to humans. However, the identification of a large number of KT proteins paved the way of understanding conserved and diverged regulatory steps that lead to the formation of a multiprotein KT super-complex on the centromere DNA in different organisms. Because it is a daunting task to summarize the entire spectrum of information in a minireview, we focus here on the recent understanding in the process of KT assembly in three yeasts: Saccharomyces cerevisiae, Schizosaccharomyces pombe and Candida albicans. Studies in these unicellular organisms suggest that although the basic process of KT assembly remains the same, the dependence of a conserved protein for its KT localization may vary in these organisms.","doi":"10.1111/1574-6968.12019","authors":"Roy B, Varshney N, Yadav V, Sanyal K","authors_abbrev":"Roy B et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2012-10-09","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10101168","title":"The role of nucleotide binding and hydrolysis in the function of the fission yeast cdc18(+) gene product.","citation":"Genetics 1999 Apr;151(4):1445-57","abstract":"The fission yeast cdc18(+) gene is required for both initiation of DNA replication and the mitotic checkpoint that normally inhibits mitosis in the absence of DNA replication. The cdc18(+) gene product contains conserved Walker A and B box motifs. Studies of other ATPases have shown that these motifs are required for nucleotide binding and hydrolysis, respectively. We have observed that mutant strains in which either of these motifs is disrupted are inviable. The effects of these mutations were examined by determining the phenotypes of mutant strains following depletion of complementing wild-type Cdc18. In both synchronous and asynchronous cultures, the nucleotide-hydrolysis motif mutant (DE286AA) arrests with a 1C-2C DNA content, and thus exhibits no obvious defects in entry into S phase or in the mitotic checkpoint. In contrast, in cultures synchronized by hydroxyurea arrest and release, the nucleotide-binding motif mutant (K205A) exhibits the null phenotype, with 1C and <1C DNA content, indicating a block in entry into S phase and loss of checkpoint control. In asynchronous cultures this mutant exhibits a mixed phenotype: a percentage of the population displays the null phenotype, while the remaining fraction arrests with a 2C DNA content. Thus, the phenotype exhibited by the K205A mutant is dependent on the cell-cycle position at which wild-type Cdc18 is depleted. These data indicate that both nucleotide binding and hydrolysis are required for Cdc18 function. In addition, the difference in the phenotypes exhibited by the nucleotide-binding and hydrolysis motif mutants is consistent with a two-step model for Cdc18 function in which nucleotide binding and hydrolysis are required for distinct aspects of Cdc18 function that may be executed at different points in the cell cycle.","authors":"DeRyckere D, Smith CL, Martin GS","authors_abbrev":"DeRyckere D et al.","pubmed_publication_date":"Apr 1999","pubmed_entrez_date":"1999-04-02","publication_year":"1999","canto_session_key":"e88b60dcaac8ca59","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-05-09 14:40:41","canto_approved_date":"2022-03-13 12:33:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-09 14:40:34","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-05-09"},{"uniquename":"PMID:12951247","title":"High osmotic stress improves electro-transformation efficiency of fission yeast.","citation":"FEMS Microbiol Lett 2003 Aug 29;225(2):235-9","abstract":"A preincubation of fission yeast cells with hyperosmotic solution improved the electro-transformation efficiency. The efficiency increased approximately five-fold when the cells were preincubated with 2.0 M sorbitol and 1.5 M NaCl at 30 degrees C for 60 min before an applied high electric pulse. Losses in the efficiency of the cells after hyperosmotic stress above 2.5 M sorbitol and 2.0 M NaCl were directly related to the marked reduction of viability. The efficiency at 2.0 M sorbitol gradually increased until 60 min of the preincubation period, but longer exposure resulted in a gradual decrease. On the other hand, when the cells of the osmotic-sensitive mutant were preincubated with isosmotic solution of 0.5 M sorbitol, the efficiency was also dramatically increased by approximately 15-fold. These improvements in efficiency were observed in sublethal conditions of osmotic stress regardless of osmoticums and strains.","authors":"Suga M, Kusanagi I, Hatakeyama T","authors_abbrev":"Suga M et al.","pubmed_publication_date":"29 Aug 2003","pubmed_entrez_date":"2003-09-03","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18279662","title":"Molecular identification and characterization of peptide: N-glycanase from Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2008 Apr 18;368(4):907-12","abstract":"Peptide:N-glycanase (PNGase) is an enzyme responsible for deglycosylation of misfolded glycoproteins in so-called endoplasmic reticulum-associated degradation (ERAD) system. In this study, we reported the molecular identification and characterization of SpPNGase (Schizosaccharomyces pombe PNGase). Enzymatic analysis revealed that SpPNGase deglycosylated the misfolded glycoproteins and distinguished native and denatured high-mannose glycoproteins in vitro. The deglycosylation activity was lost with the addition of chelating agent EDTA and was not restored by re-addition of metal ions. By construction of deletion mutant, we confirmed that N-terminal alpha-helix of SpPNGase was responsible for the protein-protein interaction. Combining the results from ternary structure prediction and dendrogram analysis, we suggested that the N-terminal alpha-helices of PNGase are derived from evolutionary motif/peptide fusion.","doi":"10.1016/j.bbrc.2008.02.017","authors":"Xin F, Wang S, Song L, Liang Q, Qi Q","authors_abbrev":"Xin F et al.","pubmed_publication_date":"18 Apr 2008","pubmed_entrez_date":"2008-02-19","publication_year":"2008","canto_session_key":"9276d468f83256bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-03 20:06:18","canto_approved_date":"2023-11-30 17:40:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-03 16:51:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.15c","SPBC1709.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-07-03"},{"uniquename":"PMID:11884590","title":"Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs.","citation":"Mol Cell Biol 2002 Apr;22(7):2011-24","abstract":"Schizosaccharomyces pombe Cdc5p and its Saccharomyces cerevisiae ortholog, Cef1p, are essential Myb-related proteins implicated in pre-mRNA splicing and contained within large multiprotein complexes. Here we describe the tandem affinity purification (TAP) of Cdc5p- and Cef1p-associated complexes. Using transmission electron microscopy, we show that the purified Cdc5p complex is a discrete structure. The components of the S. pombe Cdc5p/S. cerevisiae Cef1p complexes (termed Cwfs or Cwcs, respectively) were identified using direct analysis of large protein complex (DALPC) mass spectrometry (A. J. Link et al., Nat. Biotechnol. 17:676-682, 1999). At least 26 proteins were detected in the Cdc5p/Cef1p complexes. Comparison of the polypeptides identified by S. pombe Cdc5p purification with those identified by S. cerevisiae Cef1p purification indicates that these two yeast complexes are nearly identical in composition. The majority of S. pombe Cwf proteins and S. cerevisiae Cwc proteins are known pre-mRNA splicing factors including core Sm and U2 and U5 snRNP components. In addition, the complex contains the U2, U5, and U6 snRNAs. Previously uncharacterized proteins were also identified, and we provide evidence that several of these novel factors are involved in pre-mRNA splicing. Our data represent the first comprehensive analysis of CDC5-associated proteins in yeasts, describe a discrete highly conserved complex containing novel pre-mRNA splicing factors, and demonstrate the power of DALPC for identification of components in multiprotein complexes.","authors":"Ohi MD, Link AJ, Ren L, Jennings JL, McDonald WH, Gould KL","authors_abbrev":"Ohi MD et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-03-09","publication_year":"2002","canto_session_key":"edb672200162a551","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-06-19 06:30:05","canto_approved_date":"2020-04-09 13:33:42","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-06-18 14:47:47","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.05c","SPBC28F2.04c","SPBC19C2.14","SPAC644.12","SPAC29A4.08c","SPBC24C6.11","SPBC31F10.11c","SPBC8D2.09c","SPBC3E7.13c","SPBC6B1.10","SPBC646.02","SPCC1840.10","SPBC211.02c","SPBC337.06c","SPAC9.03c","SPCC188.11","SPBC1289.11","SPCC4B3.14","SPAC2C4.03c","SPBC13E7.02","SPBC1861.08c","SPCC550.02c","SPAC9.13c","SPAC4F8.12c","SPAC3A12.11c","SPAC26A3.08","SPBC32F12.05c","SPAC30D11.09","SPCP1E11.07c","SPBC3E7.14","SPCC10H11.02","SPBP22H7.07","SPBC215.12"],"gene_count":33,"ltp_gene_count":33,"approved_date":"2017-06-19"},{"uniquename":"PMID:32896087","title":"Mitochondrial respiration is required to provide amino acids during fermentative proliferation of fission yeast.","citation":"EMBO Rep 2020 Nov 05;21(11):e50845","abstract":"When glucose is available, many organisms repress mitochondrial respiration in favour of aerobic glycolysis, or fermentation in yeast, that suffices for ATP production. Fission yeast cells, however, rely partially on respiration for rapid proliferation under fermentative conditions. Here, we determined the limiting factors that require respiratory function during fermentation. When inhibiting the electron transport chain, supplementation with arginine was necessary and sufficient to restore rapid proliferation. Accordingly, a systematic screen for mutants growing poorly without arginine identified mutants defective in mitochondrial oxidative metabolism. Genetic or pharmacological inhibition of respiration triggered a drop in intracellular levels of arginine and amino acids derived from the Krebs cycle metabolite alpha-ketoglutarate: glutamine, lysine and glutamic acid. Conversion of arginine into these amino acids was required for rapid proliferation when blocking the respiratory chain. The respiratory block triggered an immediate gene expression response diagnostic of TOR inhibition, which was muted by arginine supplementation or without the AMPK-activating kinase Ssp1. The TOR-controlled proteins featured biased composition of amino acids reflecting their shortage after respiratory inhibition. We conclude that respiration supports rapid proliferation in fermenting fission yeast cells by boosting the supply of Krebs cycle-derived amino acids.","doi":"10.15252/embr.202050845","authors":"Malecki M, Kamrad S, Ralser M, Bähler J","authors_abbrev":"Malecki M et al.","pubmed_publication_date":"05 Nov 2020","pubmed_entrez_date":"2020-09-08","publication_year":"2020","canto_session_key":"f33df0b48bb1431a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Michal Malecki","canto_first_approved_date":"2020-12-14 16:11:12","canto_approved_date":"2026-03-09 16:06:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-09 16:00:42","canto_added_date":"2020-09-10 00:15:21","annotation_curators":[{"name":"Michal Malecki","community_curator":true,"annotation_count":68,"orcid":"0000-0002-1525-5036","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11D3.17","SPAC1039.08","SPAC27E2.11c","SPCC777.09c","SPAC14C4.14","SPAC3H1.07","SPBC1652.02","SPAC1002.17c","SPCC1223.09","SPBPB2B2.01","SPBC1683.02","SPAC9.12c","SPAC1039.09","SPAC4G9.10","SPAC11D3.18c","SPCC4B3.17","SPBC1604.11","SPCPB1C11.01","SPBC83.09c","SPAC9E9.09c","SPBC23G7.13c","SPCC1393.08","SPBC1289.06c","SPCC18B5.10c","SPAC17G8.07","SPAC25B8.13c","SPBC428.05c","SPBC365.16","SPBC21C3.08c","SPBC16A3.03c","SPAC1039.02","SPCC306.09c","SPAPB8E5.05","SPAC11D3.14c","SPBC56F2.09c","SPBC725.01","SPAP27G11.06c","SPAC27E2.01","SPAC5H10.01","SPBC29B5.02c","SPAC222.05c","SPBC1271.14","SPBC215.08c","SPAC17H9.13c","SPAPB1E7.11c","SPBC12D12.07c","SPBC354.08c","SPAC4G8.11c","SPBC1539.03c","SPAC869.10c","SPAC227.17c","SPBC428.06c","SPAC17H9.08","SPAC22H10.09","SPAC11G7.03","SPAC323.01c","SPBC725.14","SPBC359.02","SPCC794.07","SPAP7G5.06","SPCC285.05","SPAC4G9.09c"],"gene_count":62,"ltp_gene_count":62,"approved_date":"2020-12-14"},{"uniquename":"PMID:19417002","title":"Fission yeast Tor1 functions as part of TORC1 to control mitotic entry through the stress MAPK pathway following nutrient stress.","citation":"J Cell Sci 2009 Jun 01;122(Pt 11):1737-46","abstract":"TOR signalling coordinates growth and division to control cell size. Inhibition of Schizosaccharomyces pombe Tor1, in response to a reduction in the quality of the nitrogen source (nutrient stress), promotes mitotic onset through activation of the mitogen-activated protein kinase (MAPK) Sty1 (also known as Spc1). Here we show that ;nutrient starvation' (complete withdrawal of nitrogen or leucine) blocks mitotic commitment by altering Sty1 signalling and that different degrees of Sty1 activation determine these differences in mitotic commitment decisions. Mammals contain one TOR kinase, whereas yeasts contain two. In each case, they comprise two distinct complexes: TORC1 and TORC2. We find that nutrient-stress-induced control of mitotic onset, through Tor1, is regulated through changes in TORC1 signalling. In minimal medium, Tor1 interacts with the TORC1 component Mip1 (raptor), and overexpression of tor1+ generates growth defects reminiscent of TORC1 mutants. Strains lacking the TORC2-specific components Sin1 and Ste20 (rictor) still advance mitotic onset in response to nutrient stress. By contrast, Mip1 and the downstream effector Gad8 (a S6K kinase homologue), like Tor1, are essential for nutrient stress to advance mitotic onset. We conclude that S. pombe Tor1 and Tor2 can both act in TORC1. However, it is the inhibition of Tor1 as part of TORC1 that promotes mitosis following nutrient stress.","doi":"10.1242/jcs.049387","authors":"Hartmuth S, Petersen J","authors_abbrev":"Hartmuth S et al.","pubmed_publication_date":"01 Jun 2009","pubmed_entrez_date":"2009-05-07","publication_year":"2009","canto_session_key":"6a5d03f63d343148","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-29 14:47:57","canto_approved_date":"2022-09-29 06:32:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-29 14:47:23","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":40,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC23C11.16","SPCC24B10.07","SPAC24B11.06c","SPBC409.07c","SPBC30D10.10c","SPAC57A7.11","SPAC19D5.01","SPCC1322.08","SPBC216.07c","SPBC12C2.02c","SPAPYUG7.02c"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2018-03-29"},{"uniquename":"PMID:17881729","title":"Atf1 is a target of the mitogen-activated protein kinase Pmk1 and regulates cell integrity in fission yeast.","citation":"Mol Biol Cell 2007 Dec;18(12):4794-802","abstract":"In fission yeast, knockout of the calcineurin gene resulted in hypersensitivity to Cl(-), and the overexpression of pmp1(+) encoding a dual-specificity phosphatase for Pmk1 mitogen-activated protein kinase (MAPK) or the knockout of the components of the Pmk1 pathway complemented the Cl(-) hypersensitivity of calcineurin deletion. Here, we showed that the overexpression of ptc1(+) and ptc3(+), both encoding type 2C protein phosphatase (PP2C), previously known to inactivate the Wis1-Spc1-Atf1 stress-activated MAPK signaling pathway, suppressed the Cl(-) hypersensitivity of calcineurin deletion. We also demonstrated that the mRNA levels of these two PP2Cs and pyp2(+), another negative regulator of Spc1, are dependent on Pmk1. Notably, the deletion of Atf1, but not that of Spc1, displayed hypersensitivity to the cell wall-damaging agents and also suppressed the Cl(-) hypersensitivity of calcineurin deletion, both of which are characteristic phenotypes shared by the mutation of the components of the Pmk1 MAPK pathway. Moreover, micafungin treatment induced Pmk1 hyperactivation that resulted in Atf1 hyperphosphorylation. Together, our results suggest that PP2C is involved in a negative feedback loop of the Pmk1 signaling, and results also demonstrate that Atf1 is a key component of the cell integrity signaling downstream of Pmk1 MAPK.","authors":"Takada H, Nishimura M, Asayama Y, Mannse Y, Ishiwata S, Kita A, Doi A, Nishida A, Kai N, Moriuchi S, Tohda H, Giga-Hama Y, Kuno T, Sugiura R","authors_abbrev":"Takada H et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-09-21","publication_year":"2007","canto_session_key":"be61b9ab28ac9d91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 17:56:09","canto_approved_date":"2022-03-14 07:39:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-10 14:39:23","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":69,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC543.07","SPBC839.08c","SPBP4H10.04","SPAC4A8.04","SPAC328.03","SPBC1685.01","SPBC119.08","SPAC2G11.07c","SPBC317.01","SPAC13G6.12c","SPCC1223.11","SPAC1783.07c","SPBC1709.01","SPBC29B5.01","SPCC4F11.02","SPAC19D5.01","SPBC409.07c","SPBC12D12.04c","SPAC24B11.06c"],"gene_count":19,"ltp_gene_count":14,"approved_date":"2019-01-30"},{"uniquename":"PMID:10593605","title":"Cloning of a Schizosaccharomyces pombe homologue of elongation factor 1 alpha by two-hybrid selection of calmodulin-binding proteins.","citation":"Biochem Cell Biol 1999;77(5):421-30","abstract":"This study reports the cloning and characterization of a cDNA encoding elongation factor 1-alpha (EF1alpha) from the yeast Schizosaccharomyces pombe. The cDNA was cloned from an Schizosaccharomyces pombe expression library by a two-hybrid selection for clones encoding calmodulin (CaM)-binding proteins. The predicted protein is highly homologous to mammalian EF1alpha, indicating a strong tendency towards conservation of the primary amino acid sequence. The protein was expressed as a glutathione S-transferase fusion in both bacteria and in Schizosaccharomyces pombe. The bacterial protein was shown by solution assay to compete with CaM kinase II for CaM. The CaM binding domain was localized to the C-terminus of the protein by this method. Expression of full-length EF1alpha in vivo caused an increase in cell cycle length and a decreased rate of growth as evidenced by a lack of elongated cells in slowly dividing cultures. This effect appears to involve CaM binding because a truncation mutant version of EF1alpha lacking the CaM binding domain did not cause cell cycle delay.","authors":"Rasmussen C, Wiebe C","authors_abbrev":"Rasmussen C et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-12-11","publication_year":"1999","canto_session_key":"99e6d0bdf0828d48","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-05-26 09:11:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-19 10:56:31","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23A1.10","SPCC794.09c","SPBC839.15c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-05-19"},{"uniquename":"PMID:12943532","title":"A role for calcium in the regulation of neutral trehalase activity in the fission yeast Schizosaccharomyces pombe.","citation":"Biochem J 2003 Nov 15;376(Pt 1):209-17","abstract":"Neutral trehalases mobilize trehalose accumulated by fungal cells as a protective and storage carbohydrate. A structural feature of these enzymes is the presence of an EF-like motif similar to that shown by many Ca2+-binding proteins. In this study we provide direct evidence for physical binding of Ca2+ to neutral trehalase (Ntp1p) of the fission yeast Schizosaccharomyces pombe, and show that aspartic residues at positions 97 and 108 in the conserved putative Ca2+-binding motif of Ntp1p appear to be responsible for this interaction. Mutations in these residues do not interfere with the ability of Ntp1p to associate in vivo with trehalose-6-phosphate synthase, but prevent activation of neutral trehalase triggered by the addition of glucose or by subjecting cells to stressing conditions. Strains expressing Ntp1p variants that are unable to bind Ca2+ partially resemble those devoid of the ntp1+ gene in terms of trehalose hyperaccumulation. Gel filtration of cell extracts from wild-type cells after EDTA treatment or from cells containing Ntp1p with mutations in aspartic acid residues within the Ca2+-binding site revealed that Ntp1p eluted mainly in an inactive conformation instead of the dimeric or trimeric active form of the enzyme. These results suggest that activation of S. pombe Ntp1p under different conditions depends upon Ca2+ binding through the Ca2+-binding motif as a prerequisite for correct enzyme oligomerization to its active form. Given the high degree of conservation of the Ca2+ accommodation site, this might be a general mechanism regulating neutral trehalase activity in other yeasts and filamentous fungi.","authors":"Franco A, Soto T, Vicente-Soler J, Paredes V, Madrid M, Gacto M, Cansado J","authors_abbrev":"Franco A et al.","pubmed_publication_date":"15 Nov 2003","pubmed_entrez_date":"2003-08-29","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.07"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:19378169","title":"Use of a reporter gene assay in yeast for genetic analysis of DNA-protein interactions.","citation":"Methods Mol Biol 2009;543:219-41","abstract":"We describe methods for the genetic analysis of a DNA-protein interaction from any species. The DNA-binding domain of the protein of interest is expressed in yeast cells as a fusion with a known transcriptional activation domain, and the target binding site is used as an artificial upstream activation sequence (UAS) in an engineered promoter driving expression of a reporter gene, such as beta-galactosidase. Expression of the reporter gene is dependent upon specific, high-affinity interaction between the DNA-binding domain of the artificial activator and the synthetic UAS. Error-prone PCR is used to introduce mutations into either member of this interacting pair, and homologous recombination is used to return the mutagenized sequences to their proper sequence contexts in vivo. Altered expression of the reporter gene is then used as a screen or selection for mutations conferring the desired phenotype, such as reductions or increases in the stability of the DNA-protein complex. Following identification of the relevant mutations, the mutant protein or binding site can be subjected to further analyses to confirm the expected biochemical basis of the selected phenotype. This approach has been used extensively in the analysis of the TFIIIA-5S rRNA gene interaction from both Xenopus laevis and Schizosaccharomyces pombe.","doi":"10.1007/978-1-60327-015-1_15","authors":"Setzer DR, Schulman DB, Gunther CV, Bumbulis MJ","authors_abbrev":"Setzer DR et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-04-21","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1645536","title":"Tetramethylthiuram disulfide or dimethyldithiocarbamate induces the synthesis of cadystins, heavy metal chelating peptides, in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 1991 May 15;176(3):1068-73","abstract":"Tetramethylthiuram disulfide (TMTD) or dimethyldithiocarbamate (DMDTC) induces the synthesis of cadystins, a family of heavy metal chelating isopeptides with the formula (gamma-Glu-Cys)n-Gly (n = 2,3,4,...), in the fission yeast Schizosaccharomyces pombe. Amount of cadystins synthesized in TMTD or DMDTC treated cells is less than that synthesized in CdCl2 treated cells but much more than that synthesized in ZnCl2 or CuSO4 treated cells.","authors":"Mutoh N, Kawabata M, Hayashi Y","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"15 May 1991","pubmed_entrez_date":"1991-05-15","publication_year":"1991","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11739777","title":"Structure-function analysis of fission yeast Hus1-Rad1-Rad9 checkpoint complex.","citation":"Mol Biol Cell 2001 Dec;12(12):3744-58","abstract":"Hus1, Rad1, and Rad9 are three evolutionarily conserved proteins required for checkpoint control in fission yeast. These proteins are known to form a stable complex in vivo. Recently, computational studies have predicted structural similarity between the individual proteins of Hus1-Rad1-Rad9 complex and the replication processivity factor proliferating cell nuclear antigen (PCNA). This has led to the proposal that the Hus1-Rad1-Rad9 complex may form a PCNA-like ring structure, and could function as a sliding clamp during checkpoint control. In the present study, we have attempted to test the predictions of this model by asking whether the PCNA alignment identifies functionally important residues or explains mutant phenotypes of hus1, rad1, or rad9 alleles. Although some of our results are consistent with the PCNA alignment, others indicate that the Hus1-Rad1-Rad9 complex possesses unique structural and functional features.","authors":"Kaur R, Kostrub CF, Enoch T","authors_abbrev":"Kaur R et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2001-12-12","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19412885","title":"The secret message of heterochromatin: new insights into the mechanisms and function of centromeric and pericentric repeat sequence transcription.","citation":"Int J Dev Biol 2009;53(2-3):259-68","abstract":"In the fission yeast, S. Pombe, small dsRNA generated by RNAi-dependent mechanisms are involved in the establishment and maintenance of heterochromatic regions. The existence of conserved features within the general organization of centromeric and pericentromeric repeats in yeast, mouse and human argues in favor of a conserved role for centromeric and pericentromeric-derived transcripts across these species. In support of this, evidence is accumulating that centromeric and pericentromeric sequences are transcriptionally competent in diverse biological contexts in mammalian cells. Given the importance of centromeric and pericentromeric regions, not only with respect to centromere function, but also to gene regulation, this review examines the biological contexts in which mouse and human centromeric and pericentromeric-specific transcripts have been observed. The structure of the transcripts generated, the molecular mechanisms underlying their expression and their supposed functions will be discussed.","doi":"10.1387/ijdb.082673ae","authors":"Eymery A, Callanan M, Vourc'h C","authors_abbrev":"Eymery A et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-05-05","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16793402","title":"Methods for studying mutagenesis and checkpoints in Schizosaccharomyces pombe.","citation":"Methods Enzymol 2006;409:183-94","abstract":"Mutations in genome caretaker genes can induce genomic instability, which are potentially early events in tumorigenesis. Cells have evolved biological processes to cope with the genomic insults. One is a multifaceted response, termed checkpoint, which is a network of signaling pathways to coordinate cell cycle transition with DNA repair, activation of transcriptional programs, and induction of tolerance of the genomic perturbations. When genomic perturbations are beyond repair, checkpoint responses can also induce apoptosis or senescence to eliminate those deleterious damaged cells. Fission yeast, Schizosaccharomyces pombe (S. pombe) has served as a valuable model organism for studies of the checkpoint signaling pathways. In this chapter, we describe methods used to analyze mutagenesis and recombinational repair induced by genomic perturbations, and methods used to detect the checkpoint responses to replication stress and DNA damage in fission yeast cells. In the first section, we present methods used to analyze the mutation rate, mutation spectra, and recombinational repair in fission yeast when replication is perturbed by either genotoxic agents or mutations in genomic caretaker gene such as DNA replication genes. In the second section, we describe methods used to examine checkpoint activation in response to chromosome replication stress and DNA damage. In the final section, we comment on how checkpoint activation regulates mutagenic synthesis by a translesion DNA polymerase in generating a mutator phenotype of small sequence alterations in cells, and how a checkpoint kinase appropriately regulates an endonuclease complex to either prevent or allow deletion of genomic sequences and recombinational repair when fission yeast cells experience genomic perturbation in order to avoid deleterious mutations and maintain cell growth.","authors":"Kai M, Taricani L, Wang TS","authors_abbrev":"Kai M et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-06-24","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30013016","title":"Genome Mining of Non-Conventional Yeasts: Search and Analysis of  MAL  Clusters and Proteins.","citation":"Genes (Basel) 2018 Jul 16;9(7)","abstract":"Genomic clustering of functionally related genes is rare in yeasts and other eukaryotes with only few examples available. Here, we summarize our data on a nontelomeric  MAL  cluster of a non-conventional methylotrophic yeast  Ogataea  ( Hansenula )  polymorpha  containing genes for α-glucosidase MAL1, α-glucoside permease MAL2 and two hypothetical transcriptional activators. Using genome mining, we detected  MAL  clusters of varied number, position and composition in many other maltose-assimilating non-conventional yeasts from different phylogenetic groups. The highest number of  MAL  clusters was detected in  Lipomyces starkeyi  while no  MAL  clusters were found in  Schizosaccharomyces pombe  and  Blastobotrys adeninivorans . Phylograms of α-glucosidases and α-glucoside transporters of yeasts agreed with phylogenesis of the respective yeast species. Substrate specificity of unstudied α-glucosidases was predicted from protein sequence analysis. Specific activities of  Scheffersomyces  stipitis  α-glucosidases MAL7, MAL8, and MAL9 heterologously expressed in  Escherichia coli  confirmed the correctness of the prediction-these proteins were verified promiscuous maltase-isomaltases. α-Glucosidases of earlier diverged yeasts  L. starkeyi ,  B. adeninivorans  and  S. pombe  showed sequence relatedness with α-glucosidases of filamentous fungi and bacilli.","doi":"10.3390/genes9070354","authors":"Viigand K, Põšnograjeva K, Visnapuu T, Alamäe T","authors_abbrev":"Viigand K et al.","pubmed_publication_date":"16 Jul 2018","pubmed_entrez_date":"2018-07-18","publication_year":"2018","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2018-07-19 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34984977","title":"Functional profiling of long intergenic non-coding RNAs in fission yeast.","citation":"Elife 2022 Jan 05;11","abstract":"Eukaryotic genomes express numerous long intergenic non-coding RNAs (lincRNAs) that do not overlap any coding genes. Some lincRNAs function in various aspects of gene regulation, but it is not clear in general to what extent lincRNAs contribute to the information flow from genotype to phenotype. To explore this question, we systematically analysed cellular roles of lincRNAs in  Schizosaccharomyces pombe . Using seamless CRISPR/Cas9-based genome editing, we deleted 141 lincRNA genes to broadly phenotype these mutants, together with 238 diverse coding-gene mutants for functional context. We applied high-throughput colony-based assays to determine mutant growth and viability in benign conditions and in response to 145 different nutrient, drug, and stress conditions. These analyses uncovered phenotypes for 47.5% of the lincRNAs and 96% of the protein-coding genes. For 110 lincRNA mutants, we also performed high-throughput microscopy and flow cytometry assays, linking 37% of these lincRNAs with cell-size and/or cell-cycle control. With all assays combined, we detected phenotypes for 84 (59.6%) of all lincRNA deletion mutants tested. For complementary functional inference, we analysed colony growth of strains ectopically overexpressing 113 lincRNA genes under 47 different conditions. Of these overexpression strains, 102 (90.3%) showed altered growth under certain conditions. Clustering analyses provided further functional clues and relationships for some of the lincRNAs. These rich phenomics datasets associate lincRNA mutants with hundreds of phenotypes, indicating that most of the lincRNAs analysed exert cellular functions in specific environmental or physiological contexts. This study provides groundwork to further dissect the roles of these lincRNAs in the relevant conditions.","doi":"10.7554/eLife.76000","authors":"Rodriguez-Lopez M, Anver S, Cotobal C, Kamrad S, Malecki M, Correia-Melo C, Hoti M, Townsend S, Marguerat S, Pong SK, Wu MY, Montemayor L, Howell M, Ralser M, Bähler J","authors_abbrev":"Rodriguez-Lopez M et al.","pubmed_publication_date":"05 Jan 2022","pubmed_entrez_date":"2022-01-05","publication_year":"2022","canto_session_key":"81652638903aecbc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-10-04 09:10:20","canto_approved_date":"2023-10-04 09:10:21","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-10-04 09:09:33","canto_added_date":"2022-01-07 01:15:04","annotation_curators":[],"file_curator_name":"Manuel Lera-Ramirez","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Manuel Lera-Ramirez","community_curator":false,"annotation_count":5066,"orcid":"0000-0002-8666-9746","file_type":"PHAF","file_name":"PMID_34984977_phaf.tsv"}],"genes":["SPAC13A11.06","SPNCRNA.7767","SPNCRNA.187","SPBC1778.07","SPNCRNA.79","SPCC24B10.18","SPBC21C3.03","SPCC1020.08","SPAC3G9.11c","SPNCRNA.5040","SPNCRNA.377","SPNCRNA.1119","SPNCRNA.90","SPNCRNA.1039","SPBC15C4.06c","SPAC688.13","SPBC15D4.10c","SPNCRNA.399","SPAC3H5.10","SPNCRNA.323","SPNCRNA.4320","SPNCRNA.1562","SPNCRNA.5041","SPAC1556.02c","SPAC1071.09c","SPBC365.20c","SPBC16H5.13","SPNCRNA.1501","SPAC25A8.03c","SPBC215.06c","SPNCRNA.401","SPBC646.09c","SPNCRNA.87","SPBC543.07","SPAC2F3.18c","SPBC725.11c","SPAC19B12.07c","SPNCRNA.189","SPAC227.17c","SPAC23A1.06c","SPAC56F8.02","SPAC3H1.11","SPNCRNA.1073","SPNCRNA.1064","SPNCRNA.1651","SPNCRNA.130","SPBC21C3.08c","SPNCRNA.974","SPCC338.04","SPNCRNA.115","SPNCRNA.352","SPBC28F2.03","SPNCRNA.394","SPNCRNA.51","SPBC21C3.14c","SPBC20F10.02c","SPNCRNA.389","SPCC63.03","SPNCRNA.1234","SPNCRNA.989","SPAC521.03","SPBC14F5.10c","SPAC16E8.01","SPBC30D10.10c","SPAC3A11.10c","SPAC20H4.03c","SPBP8B7.31","SPAC3H1.08c","SPAC1687.15","SPAC26F1.12c","SPNCRNA.7506","SPBC3B8.08","SPAC18B11.04","SPNCRNA.900","SPNCRNA.382","SPBC36.07","SPBC17G9.07","SPNCRNA.965","SPAC22F3.04","SPBC365.12c","SPAC637.07","SPBC1105.05","SPBC2D10.05","SPNCRNA.1097","SPBC649.04","SPBC21.03c","SPNCRNA.318","SPCC16C4.11","SPNCRNA.778","SPBC14C8.16c","SPNCRNA.4472","SPBC16E9.13","SPCC4G3.12c","SPNCRNA.475","SPBC25B2.04c","SPNCRNA.1460","SPBC409.07c","SPBC1539.02","SPAC3A12.13c","SPBC32F12.03c","SPNCRNA.177","SPAC20G4.05c","SPAC12G12.11c","SPNCRNA.383","SPNCRNA.6596","SPNCRNA.242","SPNCRNA.534","SPCC4G3.09c","SPBC646.13","SPNCRNA.650","SPCC553.01c","SPBC947.09","SPAC8C9.16c","SPBC119.03","SPNCRNA.452","SPNCRNA.1642","SPAC13F5.04c","SPNCRNA.1415","SPNCRNA.737","SPBC691.03c","SPNCRNA.12","SPBC17G9.09","SPNCRNA.1154","SPAC823.16c","SPAC57A7.09","SPNCRNA.93","SPNCRNA.07","SPCC16A11.08","SPNCRNA.6379","SPAC8C9.06c","SPBC1861.02","SPAC1071.07c","SPNCRNA.1255","SPBC3E7.07c","SPCC18B5.03","SPBC2G2.06c","SPNCRNA.311","SPAC694.06c","SPNCRNA.1343","SPAC13F5.03c","SPCC736.13","SPBC16H5.14c","SPNCRNA.819","SPNCRNA.414","SPAC1D4.03c","SPCC1259.02c","SPAC4H3.06","SPAC23G3.05c","SPNCRNA.463","SPAC3H8.03","SPBC1105.14","SPNCRNA.1303","SPBC106.10","SPBC18H10.02","SPAC683.02c","SPAC22A12.14c","SPNCRNA.388","SPBC1198.11c","SPBP22H7.04","SPNCRNA.1088","SPCC162.12","SPBC18H10.04c","SPNCRNA.1166","SPBC16E9.16c","SPBC14C8.15","SPBC428.08c","SPAPB1A11.02","SPBC32H8.03","SPNCRNA.29","SPACUNK4.16c","SPCC613.03","SPAC17H9.06c","SPAC1F3.09","SPBP35G2.11c","SPBPB21E7.04c","SPNCRNA.4302","SPNCRNA.1443","SPAP14E8.05c","SPBC16A3.08c","SPAC3A11.02","SPAP8A3.04c","SPNCRNA.31","SPCC1393.13","SPAC10F6.14c","SPCC13B11.01","SPNCRNA.5036","SPCC188.02","SPAC23H4.09","SPNCRNA.1670","SPAC3G6.05","SPBC215.05","SPAC21E11.04","SPNCRNA.628","SPNCRNA.993","SPAC823.09c","SPBC20F10.03","SPNCRNA.524","SPNCRNA.335","SPAC31G5.10","SPNCRNA.5296","SPBC9B6.03","SPBC25H2.14","SPAC694.02","SPAC1834.09","SPAC17A2.02c","SPAC16.01","SPCC320.07c","SPNCRNA.1559","SPBC21C3.18","SPAC22E12.14c","SPCC663.06c","SPAC29A4.20","SPAC3H1.03","SPAC1610.02c","SPAC23C4.09c","SPBC18H10.05","SPNCRNA.1164","SPNCRNA.1361","SPBC18E5.10","SPBC31E1.01c","SPNCRNA.405","SPBC1198.07c","SPAC3G6.03c","SPBC660.10","SPAC24H6.04","SPAC105.02c","SPNCRNA.256","SPNCRNA.784","SPNCRNA.188","SPAC4G9.14","SPAC1805.07c","SPAC23D3.04c","SPBC2D10.03c","SPNCRNA.284","SPAC821.05","SPCC1494.08c","SPBC119.16c","SPCC1235.03","SPAC32A11.03c","SPAC144.19","SPBC19C7.01","SPNCRNA.745","SPNCRNA.603","SPNCRNA.190","SPAC6G10.10c","SPAC23C11.08","SPAC6F12.02","SPAC1A6.04c","SPCC4G3.17","SPAC6F6.13c","SPNCRNA.781","SPCC962.05","SPAC589.07c","SPAC821.07c","SPAC5H10.06c","SPNCRNA.780","SPCC1620.03","SPNCRNA.26","SPNCRNA.1306","SPNCRNA.720","SPCC63.06","SPBC11B10.10c","SPAC652.01","SPAC1834.04","SPNCRNA.808","SPNCRNA.348","SPAC1705.02","SPNCRNA.738","SPNCRNA.1326","SPAP27G11.12","SPNCRNA.400","SPBC3H7.10","SPAC17A5.16","SPAC890.03","SPNCRNA.941","SPBP8B7.27","SPAC3H5.09c","SPNCRNA.1125","SPNCRNA.1533","SPNCRNA.3461","SPBC16C6.01c","SPNCRNA.1624","SPBC4F6.08c","SPCC320.03","SPNCRNA.1130","SPNCRNA.30","SPAC26F1.10c","SPAC19G12.15c","SPNCRNA.1425","SPNCRNA.1519","SPNCRNA.934","SPCC4B3.03c","SPNCRNA.1348","SPCC1753.02c","SPBC1709.09","SPAC22A12.06c","SPNCRNA.817","SPBC947.05c","SPNCRNA.1249","SPBC15D4.05","SPAC1B9.02c","SPCP31B10.02","SPNCRNA.253","SPAC8F11.03","SPAC688.03c","SPBC776.01","SPNCRNA.137","SPAC27E2.03c","SPBC16D10.08c","SPAC3A12.03c","SPBC18A7.01","SPCC126.12","SPNCRNA.1122","SPBC428.15","SPNCRNA.175","SPAC3A11.11c","SPNCRNA.942","SPNCRNA.37","SPNCRNA.412","SPNCRNA.1696","SPAC7D4.05","SPNCRNA.996","SPAC1F8.06","SPAC4H3.07c","SPAC1687.14c","SPACUNK4.17","SPBC1D7.03","SPNCRNA.282","SPAC140.01","SPAC15A10.10","SPACUNK4.13c","SPAC23D3.03c","SPAC694.04c","SPAPB2B4.07","SPCC4B3.12","SPAC806.04c","SPBC1198.14c","SPNCRNA.421","SPNCRNA.767","SPAC17H9.04c","SPBC3H7.03c","SPBC3B8.02","SPNCRNA.5916","SPAC4H3.04c","SPAPB24D3.08c","SPBC685.04c","SPAC25B8.08","SPNCRNA.627","SPCC965.12","SPAC11E3.12","SPNCRNA.103","SPAPB1E7.11c","SPNCRNA.7507","SPNCRNA.1530","SPBC16A3.02c","SPAC3H5.08c","SPAC806.07","SPNCRNA.194","SPBC30D10.13c","SPNCRNA.1165","SPNCRNA.159","SPCC5E4.10c","SPCC622.11","SPCC794.03"],"gene_count":364,"ltp_gene_count":0,"approved_date":"2023-10-04"},{"uniquename":"PMID:18600047","title":"Genome-wide identification of haploinsufficiency in fission yeast.","citation":"J Microbiol Biotechnol 2008 Jun;18(6):1059-63","abstract":"Abnormal phenotypes resulting from haploinsufficiency (HI) are due to the loss of one allele. Recent studies in budding yeast have shown that HI originates from insufficient protein levels or from a stoichiometric imbalance between subunits of protein complexes. In humans, however, HI often involves transcription factors. Therefore, the species differences in HI and the molecular mechanisms of species-specific HI remain under investigation. In this study, HI in fission yeast was systematically surveyed. HI in fission yeast affected genes related to signaling and to basic cellular processes, as observed in budding yeast. These results suggest that there are species differences in HI and that the HI that occurs in fission yeast is intermediate to and HI in budding yeast and humans.","authors":"Baek ST, Han S, Nam M, Kim YD, Kim L, Lee HJ, Heo KS, Lee H, Lee M, Park SK, Maeng PJ, Park Y, Lee S, Kim DU, Kim D, Hoe KL","authors_abbrev":"Baek ST et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-07-05","publication_year":"2008","canto_session_key":"d4d3284c2136475a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-06-27 16:19:35","canto_approved_date":"2019-06-27 16:19:35","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-06-27 16:19:29","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.04c","SPAC26A3.04","SPBC4F6.09","SPAC6G9.06c","SPBC25H2.03","SPBC1703.10","SPBC3F6.01c","SPBC365.03c","SPCC576.08c","SPAC4G9.03","SPBC11C11.07","SPCC191.07","SPCC74.09","SPBC16A3.15c","SPAC30.02c","SPBC1289.03c","SPAC694.05c","SPBC1198.09","SPBC19F8.08","SPBC11C11.03","SPCC1259.01c","SPCC1235.11"],"gene_count":22,"ltp_gene_count":22,"approved_date":"2019-06-27"},{"uniquename":"PMID:9837997","title":"The fission yeast prp10(+) gene involved in pre-mRNA splicing encodes a homologue of highly conserved splicing factor, SAP155.","citation":"Nucleic Acids Res 1998 Dec 15;26(24):5662-9","abstract":"In the fission yeast Schizosaccharomyces pombe, 14 prp (pre-mRNAprocessing) mutants have been isolated to date. We cloned the prp10(+) gene by complementation of the temperature-sensitive growth of prp10. Five types of transcripts were found that were alternatively spliced with respect to two possible introns located in the 5'-terminal region. Three of them are probably functional and code for putative proteins of approximately 1200 amino acids. Proteins highly homologous to Prp10p are present in other organisms, one of which is a human spliceosome-associated protein SAP155, a subunit of the splicing factor complex SF3. The C-terminal two-thirds of Prp10p is highly conserved among species, and contains consensus repeats for the regulatory subunit A of protein phosphatase PP2A. A gene disruption experiment indicated that the prp10(+) gene is essential for viability in S.pombe. Prp10p tagged with GFP is predominantly localized in the nuclear DNA region. A series of deletions showed that the less conserved N-terminal region of approximately 300 amino acids in Prp10p is dispensable, although the corresponding region was thought to play important roles in the mammalian splicing system.","authors":"Habara Y, Urushiyama S, Tani T, Ohshima Y","authors_abbrev":"Habara Y et al.","pubmed_publication_date":"15 Dec 1998","pubmed_entrez_date":"1998-12-05","publication_year":"1998","canto_session_key":"1088ee3f2681b5d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 13:45:35","canto_approved_date":"2024-01-11 20:15:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-07 18:31:15","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.09c","SPBC146.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-17"},{"uniquename":"PMID:25379379","title":"A new pma1 mutation identified in a chronologically long-lived fission yeast mutant.","citation":"FEBS Open Bio 2014;4:829-33","abstract":"We isolated a chronologically long-lived mutant of Schizosaccharomyces pombe and found a new mutation in pma1 (+) that encoded for an essential P-type proton ATPase. An Asp-138 to Asn mutation resulted in reduced Pma1 activity, concomitant with an increase in the chronological lifespan of this fission yeast. This study corroborates our previous report indicating Pma1 activity is crucial for the determination of life span of fission yeast, and offers information for better understanding of the enzyme, Pma1.","doi":"10.1016/j.fob.2014.09.006","authors":"Naito C, Ito H, Oshiro T, Ohtsuka H, Murakami H, Aiba H","authors_abbrev":"Naito C et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-11-08","publication_year":"2014","canto_session_key":"4ce4c5548434f3ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2020-03-15 12:57:34","canto_approved_date":"2020-03-15 12:57:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-10 06:02:44","canto_added_date":"2014-11-09 01:15:24","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":1,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-03-15"},{"uniquename":"PMID:29467252","title":"Yeast Aim21/Tda2 both regulates free actin by reducing barbed end assembly and forms a complex with Cap1/Cap2 to balance actin assembly between patches and cables.","citation":"Mol Biol Cell 2018 Apr 15;29(8):923-936","abstract":"Yeast Aim21 is recruited by the SH3-containing proteins Bbc1 and Abp1 to patches and, with Tda2, reduces barbed end assembly to balance the distribution of actin between patches and cables. Aim21/Tda2 also interacts with Cap1/Cap2, revealing a complex interplay between actin assembly regulators.","doi":"10.1091/mbc.E17-10-0592","authors":"Shin M, van Leeuwen J, Boone C, Bretscher A","authors_abbrev":"Shin M et al.","pubmed_publication_date":"15 Apr 2018","pubmed_entrez_date":"2018-02-23","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC18E5.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1396601","title":"Fission yeast and a plant have functional homologues of the Sar1 and Sec12 proteins involved in ER to Golgi traffic in budding yeast.","citation":"EMBO J 1992 Nov;11(11):4205-11","abstract":"Sec12p and Sar1p are required for the formation of transport vesicles generated from the endoplasmic reticulum (ER) in the yeast Saccharomyces cerevisiae. Sec12p is an ER type II membrane protein that mediates the membrane attachment of the GTP-binding Sar1 protein. The SAR1 gene is a multi-copy suppressor of a thermosensitive sec12 mutation. In an attempt to identify functional homologues of Sec12p and Sar1p from other eukaryotic organisms, we screened cDNA expression libraries derived from the fission yeast Schizosaccharomyces pombe and from the plant Arabidopsis thaliana for complementation of the sec12ts mutation. Four individual cDNAs were isolated, two of which encode the S. pombe and A. thaliana homologues of Sar1p. The three Sar1 proteins are 67% identical on average. The two other cDNAs encode type II membrane proteins which were designated Stl1p for the S. pombe protein and Stl2p for the A. thaliana protein (Stl stands for Sec12p-like). Both proteins have NH2-terminal cytoplasmic domains which resemble that of Sec12p: they are similar in size and present a significant degree of amino acid identity with the cytoplasmic domain of Sec12p. In contrast, the lumenal domains of Sec12p, Stl1p and Stl2p are very different in size and do not show any appreciable homology. That Stl1p and Stl2p are functional homologues of Sec12p was confirmed by showing that expression of either cloned gene complements a sec12 null mutation. Our results indicate that some of the mechanisms regulating vesicle formation at the ER are conserved not only in yeasts, but also in plants.","authors":"d'Enfert C, Gensse M, Gaillardin C","authors_abbrev":"d'Enfert C et al.","pubmed_publication_date":"Nov 1992","pubmed_entrez_date":"1992-11-01","publication_year":"1992","canto_session_key":"b4423eb16b5a9785","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-22 14:26:26","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-22 14:26:06","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC31F10.06c","SPBC3H7.01"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2012-11-22"},{"uniquename":"PMID:14328411","title":"METHIONINE AS AN ANTIMUTAGEN IN SCHIZOSACCHAROMYCES POMBE.","citation":"J Gen Microbiol 1965 Apr;39:21-31","abstract":"","authors":"CLARKE CH","authors_abbrev":"CLARKE CH","pubmed_publication_date":"Apr 1965","pubmed_entrez_date":"1965-04-01","publication_year":"1965","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16204093","title":"Fusing microarray experiments with multivariate regression.","citation":"Bioinformatics 2005 Sep 01;21 Suppl 2:ii137-43","abstract":"It is widely acknowledged that microarray data are subject to high noise levels and results are often platform dependent. Therefore, microarray experiments should be replicated several times and in several laboratories before the results can be relied upon. To make the best use of such extensive datasets, methods for microarray data fusion are required. Ideally, the fused data should distil important aspects of the data while suppressing unwanted sources of variation and be amenable to further informal and formal methods of analysis. Also, the variability in the quality of experimentation should be taken into account.\nWe present such an approach to data fusion, based on multivariate regression. We apply our methodology to data from a previous study on cell-cycle control in Schizosaccharomyces pombe.\nThe algorithm implemented in R is freely available from the authors on request.","authors":"Gilks WR, Tom BD, Brazma A","authors_abbrev":"Gilks WR et al.","pubmed_publication_date":"01 Sep 2005","pubmed_entrez_date":"2005-10-06","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28265724","title":"YLL056C from Saccharomyces cerevisiae encodes a novel protein with aldehyde reductase activity.","citation":"Appl Microbiol Biotechnol 2017 Jun;101(11):4507-4520","abstract":"The short-chain dehydrogenase/reductase (SDR) family, the largest family in dehydrogenase/reductase superfamily, is divided into \"classical,\" \"extended,\" \"intermediate,\" \"divergent,\" \"complex,\" and \"atypical\" groups. Recently, several open reading frames (ORFs) were characterized as intermediate SDR aldehyde reductase genes in Saccharomyces cerevisiae. However, no functional protein in the atypical group has been characterized in S. cerevisiae till now. Herein, we report that an uncharacterized ORF YLL056C from S. cerevisiae was significantly upregulated under high furfural (2-furaldehyde) or 5-(hydroxymethyl)-2-furaldehyde concentrations, and transcription factors Yap1p, Hsf1p, Pdr1/3p, Yrr1p, and Stb5p likely controlled its upregulated transcription. This ORF indeed encoded a protein (Yll056cp), which was grouped into the atypical subgroup 7 in the SDR family and localized to the cytoplasm. Enzyme activity assays showed that Yll056cp is not a quinone or ketone reductase but an NADH-dependent aldehyde reductase, which can reduce at least seven aldehyde compounds. This enzyme showed the best Vmax, Kcat, and Kcat/Km to glycolaldehyde, but the highest affinity (Km) to formaldehyde. The optimum pH and temperature of this enzyme was pH 6.5 for reduction of glycolaldehyde, furfural, formaldehyde, butyraldehyde, and propylaldehyde, and 30 °C for reduction of formaldehyde or 35 °C for reduction of glycolaldehyde, furfural, butyraldehyde, and propylaldehyde. Temperature and pH affected stability of this enzyme and this influence varied with aldehyde substrate. Metal ions, salts, and chemical protective additives, especially at high concentrations, had different influence on enzyme activities for reduction of different aldehydes. This research provided guidelines for study of more uncharacterized atypical SDR enzymes from S. cerevisiae and other organisms.","doi":"10.1007/s00253-017-8209-5","authors":"Wang HY, Xiao DF, Zhou C, Wang LL, Wu L, Lu YT, Xiang QJ, Zhao K, Li X, Ma M-","authors_abbrev":"Wang HY et al.","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2017-03-08","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2A9.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12447975","title":"The dynamics of cell cycle regulation.","citation":"Bioessays 2002 Dec;24(12):1095-109","abstract":"Major events of the cell cycle--DNA synthesis, mitosis and cell division-are regulated by a complex network of protein interactions that control the activities of cyclin-dependent kinases. The network can be modeled by a set of nonlinear differential equations and its behavior predicted by numerical simulation. Computer simulations are necessary for detailed quantitative comparisons between theory and experiment, but they give little insight into the qualitative dynamics of the control system and how molecular interactions determine the fundamental physiological properties of cell replication. To that end, bifurcation diagrams are a useful analytical tool, providing new views of the dynamical organization of the cell cycle, the role of checkpoints in assuring the integrity of the genome, and the abnormal regulation of cell cycle events in mutants. These claims are demonstrated by an analysis of cell cycle regulation in fission yeast.","authors":"Tyson JJ, Csikasz-Nagy A, Novak B","authors_abbrev":"Tyson JJ et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2002-11-26","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14514882","title":"Events at the end of mitosis in the budding and fission yeasts.","citation":"J Cell Sci 2003 Nov 01;116(Pt 21):4263-75","abstract":"The mitotic exit network (MEN) and the septation initiation network (SIN) control events at the end of mitosis in S. cerevisiae and S. pombe, respectively. SIN initiates contraction of the actin ring and synthesis of the division septum, thereby bringing about cytokinesis. The MEN is also required for cytokinesis, but its main role is to control inactivation of mitotic cyclin-dependent kinases (CDKs) at the end of mitosis, and thereby regulate mitotic exit. Each revolves around a Ras-family GTPase and involves several protein kinases, and SIN and MEN proteins are localised to the spindle pole body. In S. cerevisiae, a second network, known as FEAR, cooperates with the MEN to bring about mitotic exit, and a third, AMEN, contributes to switching the MEN off. Some of the central components of the FEAR, SIN and MEN have been conserved through evolution, which suggests that aspects of their function in controlling events at the end of mitosis might be conserved in higher eukaryotes.","authors":"Simanis V","authors_abbrev":"Simanis V","pubmed_publication_date":"01 Nov 2003","pubmed_entrez_date":"2003-09-30","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9291132","title":"Glutathione synthetase: similarities of the proteins from Schizosaccharomyces pombe and Arabidopsis thaliana.","citation":"Biochem J 1997 Sep 01;326 ( Pt 2)(Pt 2):563-6","abstract":"Glutathione synthetase predicted from the reported gene sequence from Schizosaccharomyces pombe is substantially smaller than the equivalent protein predicted from the cDNAs sequenced from Arabidopsis thaliana, Saccharomyces cerevisiae and other eukaryotes. Sequence alignments of the proteins encoded by the cDNA clones for glutathione synthetase from Arabidopsis and S. pombe show that the Arabidopsis protein contains 200 extra amino acids at the N-terminus. In order to test if this sequence is essential in the function of the protein, the full-length Arabidopsis protein and as two N-terminal deletions (Delta67-71 and Delta67-200) were expressed in S. pombe mutant MN101, which lacks endogenous glutathione synthetase activity. Although the wild-type plant cDNA could complement the yeast mutation, neither deletion mutant was able to restore glutathione-dependent cadmium resistance. When the three proteins were expressed as fusion proteins in Escherichia coli, they accumulated to the same level, but only the plasmid containing the full-length cDNA, pFLAG222, produced detectable enzyme activity in vitro. These results suggested that the N-terminus of the Arabidopsis glutathione synthetase is essential for its function and opened up the possibility that there was a sequencing error in the reported S. pombe sequence. Therefore the gsh2 sequence from wild-type S. pombe and the mutant strain MN101 were determined. The wild-type S. pombe gsh2 encodes a protein that is about the same length as that found in Arabidopsis, and the MN101 mutation involves a frameshift mutation early in the glutathione synthetase reading frame.","authors":"Wang CL, Oliver DJ","authors_abbrev":"Wang CL et al.","pubmed_publication_date":"01 Sep 1997","pubmed_entrez_date":"1997-09-18","publication_year":"1997","canto_session_key":"5814ffb8ad4a910f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-06-03 16:41:11","canto_approved_date":"2024-04-02 17:28:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-02 15:30:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-06-03"},{"uniquename":"PMID:9223280","title":"Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1997 Jul 22;94(15):7873-8","abstract":"Dolichol phosphate mannose (Dol-P-Man), formed upon transfer of Man from GDPMan to Dol-P, is a mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of protein. Dol-P-Man synthase is an essential protein in Saccharomyces cerevisiae. We have cloned cDNAs encoding human and Schizosaccharomyces pombe proteins that resemble S. cerevisiae Dol-P-Man synthase. Disruption of the gene for the S. pombe Dol-P-Man synthase homolog, dpm1(+), is lethal. The known Dol-P-Man synthase sequences can be divided into two classes. One contains the S. cerevisiae, Ustilago maydis, and Trypanosoma brucei enzymes, which have a COOH-terminal hydrophobic domain, and the other contains the human, S. pombe, and Caenorhabditis synthases, which lack a hydrophobic COOH-terminal domain. The two classes of synthase are functionally equivalent, because S. cerevisiae DPM1 and its human counterpart both complement the lethal null mutation in S. pombe dpm1(+). The findings that Dol-P-Man synthase is essential in yeast and that the Ustilago and Trypanosoma synthases are in a different class from the human enzyme raise the possibility that Dol-P-Man synthase could be exploited as a target for inhibitors of pathogenic eukaryotic microbes.","authors":"Colussi PA, Taron CH, Mack JC, Orlean P","authors_abbrev":"Colussi PA et al.","pubmed_publication_date":"22 Jul 1997","pubmed_entrez_date":"1997-07-22","publication_year":"1997","canto_session_key":"83089a83d5206564","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-05-06 08:18:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-05 22:19:17","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.16c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-05"},{"uniquename":"PMID:6275361","title":"Nucleotide sequences of the 5S ribosomal RNA genes and their adjacent regions in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1981 Dec 11;9(23):6429-37","abstract":"The organization of 5S ribosomal RNA (rRNA) genes in the genome of Schizosaccharomyces pombe has been investigated by restriction and hybridization analyses. The 5S rRNA genes were not linked to the other three species of rRNA genes which formed a repeating unit of 6.9 megadaltons, but located in other regions surrounded by heterogeneous sequences. The 5S rRNA gene organization in S. pombe is therefore different from those in other yeasts; Saccharomyces cerevisiae and Torulopsis utilis. Four restriction segments of different sizes each containing a single 5S rRNA gene were cloned on a bacterial plasmid, and the sequences in and around the RNA coding regions were determined. In the RNA coding regions, the sequences in four clones were identical with an exception that one residue has been substituted in one clone. In the flanking regions, the sequences were extremely rich in the AT-content and highly heterogeneous. The sequences were also markedly different from those in the corresponding regions of the other two yeasts. THe presence of T-clusters in the regions immediately after the RNA coding sequences was only notable homology among the four clones and the other two yeasts.","authors":"Tabata S","authors_abbrev":"Tabata S","pubmed_publication_date":"11 Dec 1981","pubmed_entrez_date":"1981-12-11","publication_year":"1981","canto_session_key":"b3efa25686cdbfcb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 17:44:12","canto_approved_date":"2019-01-31 17:44:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 17:44:04","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPRRNA.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:18180284","title":"Minichromosome maintenance proteins interact with checkpoint and recombination proteins to promote s-phase genome stability.","citation":"Mol Cell Biol 2008 Mar;28(5):1724-38","abstract":"The minichromosome maintenance (MCM) complex plays essential, conserved roles throughout DNA synthesis: first, as a component of the prereplication complex at origins and, then, as a helicase associated with replication forks. Here we use fission yeast (Schizosaccharomyces pombe) as a model to demonstrate a role for the MCM complex in protecting replication fork structure and promoting recovery from replication arrest. Loss of MCM function generates lethal double-strand breaks at sites of DNA synthesis during replication elongation, suggesting replication fork collapse. MCM function also maintains the stability of forks stalled by hydroxyurea that activate the replication checkpoint. In cells where the checkpoint is activated, Mcm4 binds the Cds1 kinase and undergoes Cds1-dependent phosphorylation. MCM proteins also interact with proteins involved in homologous recombination, which promotes recovery from arrest by ensuring normal mitosis. We suggest that the MCM complex links replication fork stabilization with checkpoint arrest and recovery through direct interactions with checkpoint and recombination proteins and that this role in S-phase genome stability is conserved from yeast to human cells.","doi":"10.1128/MCB.01717-07","authors":"Bailis JM, Luche DD, Hunter T, Forsburg SL","authors_abbrev":"Bailis JM et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-01-09","publication_year":"2008","canto_session_key":"56ce08f89dc9d46c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-11-27 11:14:38","canto_approved_date":"2023-11-28 14:13:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-27 11:14:31","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":67,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPBC776.12c","SPBC1734.02c","SPBC336.04","SPBC25D12.03c","SPAC1F7.05","SPCC1259.13","SPBC216.05","SPCC18B5.11c","SPBC4.04c","SPAC30D11.10","SPAC20G8.01","SPAC644.14c","SPBC211.04c"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2015-11-27"},{"uniquename":"PMID:10233158","title":"Ssp1 promotes actin depolymerization and is involved in stress response and new end take-off control in fission yeast.","citation":"Mol Biol Cell 1999 May;10(5):1495-510","abstract":"The ssp1 gene encodes a protein kinase involved in alteration of cell polarity in Schizosaccharomyces pombe. ssp1 deletion causes stress sensitivity, reminiscent of defects in the stress-activated MAP kinase, Spc1; however, the two protein kinases do not act through the same pathway. Ssp1 is localized mainly in the cytoplasm, but after a rise in external osmolarity it is rapidly recruited to the plasma membrane, preferentially to active growth zones and septa. Loss of Ssp1 function inhibits actin relocalization during osmotic stress, in cdc3 and cdc8 mutant backgrounds, and in the presence of latrunculin A, implicating Ssp1 in promotion of actin depolymerization. We propose a model in which Ssp1 can be activated independently of Spc1 and can partially compensate for its loss. The ssp1 deletion mutant exhibited monopolar actin distribution, but new end take-off (NETO) could be induced in these cells by exposure to KCl or to latrunculin A pulse treatment. This treatment induced NETO in cdc10 cells arrested in G1 but not in tea1 cells. This suggests that cells that contain intact cell end markers are competent to undergo NETO throughout interphase, and Ssp1 is involved in generating the NETO stimulus by enlarging the actin monomer pool.","authors":"Rupes I, Jia Z, Young PG","authors_abbrev":"Rupes I et al.","pubmed_publication_date":"May 1999","pubmed_entrez_date":"1999-05-08","publication_year":"1999","canto_session_key":"65a61f413b5b2a9f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-07 17:55:55","canto_approved_date":"2022-09-23 17:54:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-28 14:56:40","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC297.03","SPAC24B11.06c","SPAC24H6.05","SPAC4A8.15c","SPCC330.05c","SPAC26F1.10c","SPCC18B5.03","SPAC27F1.02c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2016-09-07"},{"uniquename":"PMID:22362333","title":"Mug20, a novel protein associated with linear elements in fission yeast meiosis.","citation":"Curr Genet 2012 Apr;58(2):119-27","abstract":"In the fission yeast, Schizosaccharomyces pombe, homologous chromosomes efficiently pair and recombine during meiotic prophase without forming a canonical synaptonemal complex (SC). Instead, it features simpler filamentous structures, the so-called linear elements (LinEs), which bear some resemblance to the axial/lateral element subunits of the SC. LinEs are required for wild-type recombination frequency. Here, we recognized Mug20, the product of a meiotically upregulated gene, as a LinE-associated protein. GFP-tagged Mug20 and anti-Mug20 antibody co-localized completely with Rec10, one of the major constituents of LinEs. In the absence of Mug20, LinEs failed to elongate beyond their initial state of nuclear dots. Foci of recombination protein Rad51 and genetic recombination were reduced. Since meiotic DNA double-strand breaks (DSBs), which initiate recombination, are induced at sites of preformed LinEs, we suggest that reduced recombination is a consequence of incomplete LinE extension. Therefore, we propose that Mug20 is required to extend LinEs from their sites of origin and thereby to increase DSB proficient regions on chromosomes.","doi":"10.1007/s00294-012-0369-3","authors":"Estreicher A, Lorenz A, Loidl J","authors_abbrev":"Estreicher A et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-02-25","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1718.02","SPBC36B7.06c","SPAC17A5.18c","SPAC25G10.04c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:30510058","title":"Both a Unique Motif at the C Terminus and an N-Terminal HEAT Repeat Contribute to G-Quadruplex Binding and Origin Regulation by the Rif1 Protein.","citation":"Mol Cell Biol 2019 Feb 15;39(4)","abstract":"Rif1 is a key factor for spatiotemporal regulation of DNA replication. Rif1 suppresses origin firing in the mid-late replication domains by generating replication-suppressive chromatin architecture and by recruiting a protein phosphatase. In fission yeast, the function of Hsk1, a kinase important for origin firing, can be bypassed by  rif1 Δ due to the loss of origin suppression. Rif1 specifically binds to G-quadruplex (G4)  in vitro  Here, we show both conserved N-terminal HEAT repeats and C-terminal nonconserved segments are required for origin suppression. The N-terminal 444 amino acids and the C-terminal 229 amino acids can each mediate specific G4 binding, although high-affinity G4 binding requires the presence of both N- and C-terminal segments. The C-terminal 91 amino acids, although not able to bind to G4, can form a multimer. Furthermore, genetic screening led to identification of two classes of  rif1  point mutations that can bypass Hsk1, one that fails to bind to chromatin and one that binds to chromatin. These results illustrate functional domains of Rif1 and indicate importance of both the N-terminal HEAT repeat segment and C-terminal G4 binding/oligomerization domain as well as other functionally unassigned segments of Rif1 in regulation of origin firing.","doi":"10.1128/MCB.00364-18","authors":"Kobayashi S, Fukatsu R, Kanoh Y, Kakusho N, Matsumoto S, Chaen S, Masai H","authors_abbrev":"Kobayashi S et al.","pubmed_publication_date":"15 Feb 2019","pubmed_entrez_date":"2018-12-05","publication_year":"2019","canto_session_key":"73e55178aa344af4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-12-06 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15040451","title":"Stress-dependent regulation of the gene encoding gamma-glutamylcysteine synthetase from the fission yeast.","citation":"Mol Biol Rep 2004 Mar;31(1):23-30","abstract":"Glutathione (GSH), an important antioxidant involved in stress response, is synthesized in two sequential reactions. Gamma-glutamylcysteine synthetase (GCS) catalyzes the first step in GSH biosynthesis, which is usually known to be rate-limiting. In this work, regulatory patterns of the GCS gene from the fission yeast Schizosaccharomyces pombe have been investigated. The 607 bp upstream region from the translational initiation point was amplified by the two synthetic primers. The amplified DNA was ligated into the BamHI/HindIII site of the shuttle vector YEp367R to generate the fusion plasmid pUGCS101. The GCS-lacZ fusion gene construct was confirmed by restriction mapping and nucleotide sequencing. The GCS-lacZ fusion gene was used to study effects of various agents on the transcription of the GCS gene. The synthesis of beta-galactosidase from the fusion plasmid pUGCS101 was enhanced by metals, oxidative and nitrosative stresses, and glutathione-depleting agents. The GCS mRNA level in the wildtype S. pombe cells was significantly elevated by the treatment with sodium nitroprusside or menadione, which was detected by RT-PCR. It was also induced by low concentrations of glucose and sucrose. These results suggest that the expression of S. pombe GCS gene is regulated by various stresses and carbon sources.","authors":"Kim SJ, Park EH, Lim CJ","authors_abbrev":"Kim SJ et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-03-26","publication_year":"2004","canto_session_key":"d43e515101fafb8e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-11-07 11:37:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-06 11:04:14","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F3.10c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-11-06"},{"uniquename":"PMID:6581157","title":"A meiotic mutant of the fission yeast Schizosaccharomyces pombe that produces mature asci containing two diploid spores.","citation":"J Bacteriol 1984 Jan;157(1):334-6","abstract":"A mutant of the fission yeast Schizosaccharomyces pombe grew normally in the mitotic cycle but produced two-spored asci in the meiosis cycle. These spores were diploid, and the segregation of centromere-linked markers in the dyads was mostly reductional. Only the first meiotic division appears to occur in this tws1 mutant, resulting in enclosure of diploid nuclei into spores.","authors":"Nakaseko Y, Niwa O, Yanagida M","authors_abbrev":"Nakaseko Y et al.","pubmed_publication_date":"Jan 1984","pubmed_entrez_date":"1984-01-01","publication_year":"1984","canto_session_key":"0f6b0a4f62f2c597","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-03-14 09:30:33","canto_approved_date":"2021-03-25 14:40:12","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-03-19 18:16:00","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-03-14"},{"uniquename":"Pfam:PF06131","canto_curator_role":"PomBase","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBPJ4664.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12077121","title":"YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins.","citation":"J Biol Chem 2002 Sep 20;277(38):35274-81","abstract":"The OS-9 gene maps to a region (q13-15) of chromosome 12 that is highly amplified in human osteosarcomas and encodes a protein of unknown function. Here we have characterized a homolog designated as YOS9 (YDR057w) from Saccharomyces cerevisiae. The yeast protein (Yos9) is a membrane-associated glycoprotein that localizes to the endoplasmic reticulum (ER). YOS9 interacts genetically with genes involved in ER-Golgi transport, particularly SEC34, whose temperature-sensitive mutant is rescued by YOS9 overexpression. Interestingly, Yos9 appears to play a direct role in the transport of glycosylphosphatidylinositol (GPI)-anchored proteins to the Golgi apparatus. Yos9 binds directly to Gas1 and Mkc7 and accelerates Gas1 transport and processing in cells overexpressing YOS9. Correspondingly, Gas1 processing is slowed in cells bearing a deletion in YOS9. No effect upon the transport and processing of non-GPI-anchored proteins (e.g. invertase and carboxypeptidase Y) was detected in cells either lacking or overexpressing Yos9. As Yos9 is not a component of the Emp24 complex, it may act as a novel escort factor for GPI-anchored proteins in ER-Golgi transport in yeast and possibly in mammals.","authors":"Friedmann E, Salzberg Y, Weinberger A, Shaltiel S, Gerst JE","authors_abbrev":"Friedmann E et al.","pubmed_publication_date":"20 Sep 2002","pubmed_entrez_date":"2002-06-22","publication_year":"2002","canto_curator_role":"PomBase","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC227.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8485317","title":"A mitotic role for a novel fission yeast protein kinase dsk1 with cell cycle stage dependent phosphorylation and localization.","citation":"Mol Biol Cell 1993 Mar;4(3):247-60","abstract":"The fission yeast dsk1+ gene, a multicopy suppressor for cold-sensitive dis1 mutants, encodes a novel 61-kd protein kinase. It is a phosphoprotein, and phosphoserine is the major phosphorylated amino acid. Hyperphosphorylation of dsk1 causes a mobility shift, resulting in two dsk1-specific protein bands. The phosphorylation pattern is strikingly altered when cell cycle progression is delayed or arrested. The slowly migrating phosphorylated form is prominent in mitotically arrested cells, and the fast migrating form is enriched in interphase-arrested cells. dsk1 is a protein kinase. It auto-phosphorylates as well as phosphorylates myelin basic protein (MBP). Phosphotyrosine as well as phosphoserine/threonine were found in autophosphorylation, but no tyrosine phosphorylation occurs when MBP was used as the substrate. The dsk1 immunoprecipitates from mitotically arrested cells have a several-fold higher kinase activity than that from wild type. The haploid gene disruptant is viable, indicating that the dsk1+ gene is non-essential for viability. High dosage of dsk1+, however, strongly delays the G2/M progression. Immunofluorescence microscopy using anti-dsk1 antibody shows that localization pattern of dsk1 protein strikingly alters depending on cell cycle stages. In G2-arrested cells, dsk1 locates in the cytoplasm, whereas in mitotically arrested cells, nuclear stain is intense. In wild-type cells, nuclear stain is seen only in mitotic cells. Hence dsk1 protein may play an important role in mitotic control by altering cellular location, degree of phosphorylation and kinase activity. We discuss possible roles of dsk1 kinase as an add-on regulator in mitosis.","authors":"Takeuchi M, Yanagida M","authors_abbrev":"Takeuchi M et al.","pubmed_publication_date":"Mar 1993","pubmed_entrez_date":"1993-03-01","publication_year":"1993","canto_session_key":"5a0095c9d74677e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-06-03 13:41:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-12-03 16:15:08","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC530.14c","SPCC736.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-12-03"},{"uniquename":"PMID:23771057","title":"Sir2 is required for Clr4 to initiate centromeric heterochromatin assembly in fission yeast.","citation":"EMBO J 2013 Aug 28;32(17):2321-35","abstract":"Heterochromatin assembly in fission yeast depends on the Clr4 histone methyltransferase, which targets H3K9. We show that the histone deacetylase Sir2 is required for Clr4 activity at telomeres, but acts redundantly with Clr3 histone deacetylase to maintain centromeric heterochromatin. However, Sir2 is critical for Clr4 function during de novo centromeric heterochromatin assembly. We identified new targets of Sir2 and tested if their deacetylation is necessary for Clr4-mediated heterochromatin establishment. Sir2 preferentially deacetylates H4K16Ac and H3K4Ac, but mutation of these residues to mimic acetylation did not prevent Clr4-mediated heterochromatin establishment. Sir2 also deacetylates H3K9Ac and H3K14Ac. Strains bearing H3K9 or H3K14 mutations exhibit heterochromatin defects. H3K9 mutation blocks Clr4 function, but why H3K14 mutation impacts heterochromatin was not known. Here, we demonstrate that recruitment of Clr4 to centromeres is blocked by mutation of H3K14. We suggest that Sir2 deacetylates H3K14 to target Clr4 to centromeres. Further, we demonstrate that Sir2 is critical for de novo accumulation of H3K9me2 in RNAi-deficient cells. These analyses place Sir2 and H3K14 deacetylation upstream of Clr4 recruitment during heterochromatin assembly.","doi":"10.1038/emboj.2013.143","authors":"Alper BJ, Job G, Yadav RK, Shanker S, Lowe BR, Partridge JF","authors_abbrev":"Alper BJ et al.","pubmed_publication_date":"28 Aug 2013","pubmed_entrez_date":"2013-06-18","publication_year":"2013","canto_session_key":"2649334dd5e29a0f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Janet Partridge","canto_first_approved_date":"2016-07-27 16:26:34","canto_approved_date":"2024-09-27 16:57:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-01-20 21:47:09","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Janet Partridge","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.03c","SPCC132.02","SPAC212.11","SPAC1783.04c","SPBC8D2.04","SPCC188.13c","SPBCPT2R1.08c","SPCC736.11","SPBC36.05c","SPCC330.05c","SPBC16D10.07c","SPBC428.08c","SPAC664.01c","SPBC800.03"],"gene_count":14,"ltp_gene_count":3,"approved_date":"2016-07-27"},{"uniquename":"PMID:15477092","title":"Purification, folding, and characterization of Rec12 (Spo11) meiotic recombinase of fission yeast.","citation":"Protein Expr Purif 2004 Nov;38(1):136-44","abstract":"Meiotic recombination is initiated by controlled dsDNA breaks (DSBs). Rec12 (Spo11) protein of fission yeast is essential for the formation of meiotic DSBs in vivo, for meiotic recombination, and for segregation of chromosomes during meiosis I. Rec12 is orthologous to Top6A topoisomerase of Archaea and is likely the catalytic subunit of a meiotic recombinase that introduces recombinogenic DSBs. However, despite intensive effort, it has not been possible to produce Rec12 protein in a soluble form required to permit biochemical analyses of function. To obtain purified Rec12 protein for in vitro studies, a rec12(+) cDNA was generated, cloned into vector pET15b(+), and expressed in Escherichia coli. Rec12 protein was produced at moderate levels and it partitioned into insoluble fractions of whole-cell extracts. The protein was enriched based upon its differential solubility in two different denaturants and was further purified by column chromatography. A combinatorial, fractional, factorial approach was used to identify conditions under which Rec12 protein could be refolded. Four parameters were most important and, following optimization, soluble Rec12 protein was obtained. Gel filtration demonstrated that refolded Rec12 protein exists as a monomer in solution, suggesting that additional proteins may be required to assemble biologically-active Rec12 dimers, as inferred previously from genetic data [Cell Chromosome 1 (2002) 1]. The production of refolded Rec12 in a soluble form will allow for characterization in vitro of this key meiotic recombination enzyme.","authors":"Wu H, Gao J, Sharif WD, Davidson MK, Wahls WP","authors_abbrev":"Wu H et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-13","publication_year":"2004","canto_session_key":"8b6be83d94a20403","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-10-06 09:15:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-06 09:15:08","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.11"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-10-06"},{"uniquename":"PMID:39476757","title":"Characterization of Ksg1 protein kinase-dependent phosphoproteome in the fission yeast S. pombe.","citation":"Biochem Biophys Res Commun 2024 Oct 25;736:150895","abstract":"Ksg1 is an essential protein kinase of the fission yeast S. pombe that belongs to the AGC kinase family and is homologous to the mammalian PDPK1 kinase. Previous studies have shown that Ksg1 functions in the nutrient-sensing TOR signaling pathway and is involved in the phosphorylation and activation of other AGC kinases, thereby affecting various downstream targets related to metabolism, cell division, stress response, and gene expression. To date, the molecular function of Ksg1 has been analyzed using its temperature sensitive mutants or mutants expressing its truncated isoforms, which are not always suitable for functional studies of Ksg1 and the identification of its targets. To overcome these limitations, we employed a chemical genetic strategy and used a conditional ksg1 as  mutant sensitive to an ATP analog. Combining this mutant with quantitative phosphoproteomics analysis, we identified 1986 phosphosites that were differentially phosphorylated when Ksg1 as  kinase was inhibited by an ATP analog. We found that proteins whose phosphorylation was dysregulated after inhibition of Ksg1 as  kinase were mainly represented by those involved in the regulation of cytokinesis, contractile ring contraction, cell division, septation initiation signaling cascade, intracellular protein kinase cascade, barrier septum formation, protein phosphorylation, intracellular signal transduction, cytoskeleton organization, cellular response to stimulus, or in RNA, ncRNA and rRNA processing. Importantly, proteins with significantly down-regulated phosphorylation were specifically enriched for R-X-X-S and R-X-R-X-X-S motifs, which are typical consensus substrate sequences for phosphorylation by the AGC family of kinases. The results of this study provide a basis for further analysis of the role of the Ksg1 kinase and its targets in S. pombe and may also be useful for studying Ksg1 orthologs in other organisms.","doi":"10.1016/j.bbrc.2024.150895","authors":"Cipak L, Sivakova B, Bellova J, Danchenko M, Jurcik J, Cipakova I, Lalakova LO, Gregan J, Barath P","authors_abbrev":"Cipak L et al.","pubmed_publication_date":"25 Oct 2024","pubmed_entrez_date":"2024-10-30","publication_year":"2024","canto_session_key":"2fe0a48657ba4f41","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-11-21 17:32:31","canto_approved_date":"2025-10-01 14:14:02","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-11-21 17:32:22","canto_added_date":"2024-11-01 00:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":32,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"file_curator_name":"Pascal Carme","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Pascal 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copper-sensing transcription factor regulates iron uptake genes in Schizosaccharomyces pombe.","citation":"J Biol Chem 1999 Dec 17;274(51):36252-60","abstract":"Copper and iron serve essential functions as catalytic co-factors in a wide variety of critical cellular enzymes. Studies in yeast have demonstrated an absolute dependence upon copper acquisition for proper assembly and function of the iron transport machinery. We have cloned genes for a high affinity copper transporter (Ctr4) and copper-sensing transcription factor (Cuf1) from Schizosaccharomyces pombe. Interestingly, the primary structure of Ctr4 and a putative human high affinity copper transport protein, hCtr1, suggests that they are derived from a fusion of the functionally redundant but structurally distinct Ctr1 and Ctr3 copper transporters from Saccharomyces cerevisiae. Furthermore, although Cuf1 activates ctr4(+) gene expression under copper starvation conditions, under these same conditions Cuf1 directly represses expression of genes encoding components of the iron transport machinery. These studies have identified an evolutionary step in which copper transport modules have been fused, and describe a mechanism by which a copper-sensing factor directly represses expression of the iron uptake genes under conditions in which the essential copper co-factor is scarce.","authors":"Labbé S, Peña MM, Fernandes AR, Thiele DJ","authors_abbrev":"Labbé S et al.","pubmed_publication_date":"17 Dec 1999","pubmed_entrez_date":"1999-12-14","publication_year":"1999","canto_session_key":"b020334f9d974ddf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-11-01 21:50:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-01 19:28:10","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.11c","SPAC1F7.07c","SPAC1F7.08","SPBC1683.09c","SPCC1393.10"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2014-12-01"},{"uniquename":"PMID:17035632","title":"Reconstruction of the kinetochore during meiosis in fission yeast Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2006 Dec;17(12):5173-84","abstract":"During the transition from mitosis to meiosis, the kinetochore undergoes significant reorganization, switching from a bipolar to a monopolar orientation. To examine the centromere proteins that are involved in fundamental reorganization in meiosis, we observed the localization of 22 mitotic and 2 meiotic protein components of the kinetochore during meiosis in living cells of the fission yeast. We found that the 22 mitotic proteins can be classified into three groups: the Mis6-like group, the NMS (Ndc80-Mis12-Spc7) group, and the DASH group, based on their meiotic behavior. Mis6-like group proteins remain at the centromere throughout meiosis. NMS group proteins disappear from the centromere at the onset of meiosis and reappear at the centromere in two steps in late prophase. DASH group proteins appear shortly before metaphase of meiosis I. These observations suggest that Mis6-like group proteins constitute the structural basis of the centromere and that the NMS and DASH group proteins reassemble to establish the functional metaphase kinetochore. On the other hand, the meiosis-specific protein Moa1, which plays an important role in forming the meiotic monopolar kinetochore, is loaded onto the centromere significantly earlier than the NMS group, whereas another meiosis-specific protein, Sgo1, is loaded at times similar to the NMS group.","authors":"Hayashi A, Asakawa H, Haraguchi T, Hiraoka Y","authors_abbrev":"Hayashi A et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-10-13","publication_year":"2006","canto_session_key":"f2debdcbb3120b09","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-05-19 06:11:34","canto_approved_date":"2023-05-19 06:11:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-05-18 17:34:10","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":79,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1861.01c","SPBC11C11.03","SPAC25B8.14","SPBC18E5.03c","SPAC589.08c","SPAC27F1.04c","SPAC1805.07c","SPAC1687.20c","SPAC23H4.11c","SPCC1020.02","SPBC1105.17","SPBC409.09c","SPBC27.02c","SPBP22H7.09c","SPCC1235.07","SPCC188.04c","SPAC16A10.05c","SPAC688.02c","SPBC336.08","SPAC29E6.04","SPBC409.04c","SPAC8C9.17c","SPAC15E1.07c","SPBP35G2.03c"],"gene_count":24,"ltp_gene_count":23,"approved_date":"2023-05-19"},{"uniquename":"PMID:2547758","title":"Mapping of the active site tyrosine of eukaryotic DNA topoisomerase I.","citation":"J Biol Chem 1989 Aug 15;264(23):13373-6","abstract":"DNA topoisomerase I from the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe was overproduced using the cloned genes. Extracts from cells overproducing DNA topoisomerase I were prepared and incubated with 32P-labeled DNA. Alkali was used to trap the topoisomerase I-DNA covalent intermediate. Most of the DNA was digested with nuclease, and the resultant 32P-labeled topoisomerase I was subjected to cleavage with cyanogen bromide or formic acid. From the molecular weights of the resultant labeled peptides and by comparison of the amino acid sequences derived from the cloned genes, we were able to deduce that the active site tyrosine of eukaryotic DNA topoisomerase I is very near the carboxyl terminus, at amino acid 771 for S. pombe and 727 for S. cerevisiae. Site-directed mutagenesis was used to change tyrosine 727 of S. cerevisiae topoisomerase I to a phenylalanine. The resulting mutant topoisomerase I protein lost all DNA relaxation activity and rendered cells resistant to the topoisomerase I inhibitor, camptothecin. The amino acid sequence of human topoisomerase I has significant similarity to the two yeast topoisomerase I sequences. Based on this similarity, we infer that tyrosine 723 is the active site tyrosine of human enzyme.","authors":"Eng WK, Pandit SD, Sternglanz R","authors_abbrev":"Eng WK et al.","pubmed_publication_date":"15 Aug 1989","pubmed_entrez_date":"1989-08-15","publication_year":"1989","canto_session_key":"9284968870a444a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-02-17 13:51:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-14 22:58:59","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1703.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-14"},{"uniquename":"PMID:17947404","title":"The hermes transposon of Musca domestica is an efficient tool for the mutagenesis of Schizosaccharomyces pombe.","citation":"Genetics 2007 Dec;177(4):2519-23","abstract":"Currently, no transposon-based method for the mutagenesis of Schizosaccharomyces pombe exists. We have developed such a system based on the introduction of the hermes transposon from the housefly into S. pombe. This system efficiently disrupts open reading frames and allows the insertion sites to be readily identified.","authors":"Evertts AG, Plymire C, Craig NL, Levin HL","authors_abbrev":"Evertts AG et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-10-20","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3536917","title":"Identification and characterization of thiamin repressible acid phosphatase in yeast.","citation":"J Biol Chem 1986 Dec 05;261(34):15877-82","abstract":"We have identified a genetic locus, pho4, in Schizosaccharomyces pombe which encodes a minor expressed cell surface acid phosphatase that is repressed by low concentrations (0.5 microM) of thiamin. The enzyme was purified from a strain that overproduces the enzyme. It is an Asn-linked glycoprotein. Removal of the carbohydrates by endoglycosidase H does not abolish enzymatic activity. The molecular mass of deglycosylated and unglycosylated enzyme that accumulates in membranes when cells are grown in the presence of tunicamycin is 56 kDa as determined by sodium dodecyl sulfate-gel electrophoresis. Thiamin regulation, at least in part, operates by reducing the level of pho4-mRNA. Pho4 is not genetically linked to the phosphate repressible acid phosphatase gene pho1. Phosphate and thiamin repressible acid phosphatase differ in their substrate specificity. Their protein moieties are immunologically related. Pho4 and pho1 are the only genes in S. pombe that express cell surface acid phosphatases being enzymatically active with nitrophenyl phosphate as substrate. S. pombe is not unique in having a thiamin repressible acid phosphatase. In Saccharomyces cerevisiae this enzyme is encoded by PHO3.","authors":"Schweingruber ME, Fluri R, Maundrell K, Schweingruber AM, Dumermuth E","authors_abbrev":"Schweingruber ME et al.","pubmed_publication_date":"05 Dec 1986","pubmed_entrez_date":"1986-12-05","publication_year":"1986","canto_session_key":"e55cf6a7fad0e08b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-10-31 14:30:52","canto_approved_date":"2019-10-31 14:30:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-10-31 14:30:47","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPBC428.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-10-31"},{"uniquename":"PMID:11859360","title":"The genome sequence of Schizosaccharomyces pombe.","citation":"Nature 2002 Feb 21;415(6874):871-80","abstract":"We have sequenced and annotated the genome of fission yeast (Schizosaccharomyces pombe), which contains the smallest number of protein-coding genes yet recorded for a eukaryote: 4,824. The centromeres are between 35 and 110 kilobases (kb) and contain related repeats including a highly conserved 1.8-kb element. Regions upstream of genes are longer than in budding yeast (Saccharomyces cerevisiae), possibly reflecting more-extended control regions. Some 43% of the genes contain introns, of which there are 4,730. Fifty genes have significant similarity with human disease genes; half of these are cancer related. We identify highly conserved genes important for eukaryotic cell organization including those required for the cytoskeleton, compartmentation, cell-cycle control, proteolysis, protein phosphorylation and RNA splicing. These genes may have originated with the appearance of eukaryotic life. Few similarly conserved genes that are important for multicellular organization were identified, suggesting that the transition from prokaryotes to eukaryotes required more new genes than did the transition from unicellular to multicellular organization.","authors":"Wood V, Gwilliam R, Rajandream MA, Lyne M, Lyne R, Stewart A, Sgouros J, Peat N, Hayles J, Baker S, Basham D, Bowman S, Brooks K, Brown D, Brown S, Chillingworth T, Churcher C, Collins M, Connor R, Cronin A, Davis P, Feltwell T, Fraser A, Gentles S, Goble A, Hamlin N, Harris D, Hidalgo J, Hodgson G, Holroyd S, Hornsby T, Howarth S, Huckle EJ, Hunt S, Jagels K, James K, Jones L, Jones M, Leather S, McDonald S, McLean J, Mooney P, Moule S, Mungall K, Murphy L, Niblett D, Odell C, Oliver K, O'Neil S, Pearson D, Quail MA, Rabbinowitsch E, Rutherford K, Rutter S, Saunders D, Seeger K, Sharp S, Skelton J, Simmonds M, Squares R, Squares S, Stevens K, Taylor K, Taylor RG, Tivey A, Walsh S, Warren T, Whitehead S, Woodward J, Volckaert G, Aert R, Robben J, Grymonprez B, Weltjens I, Vanstreels E, Rieger M, Schäfer M, Müller-Auer S, Gabel C, Fuchs M, Düsterhöft A, Fritzc C, Holzer E, Moestl D, Hilbert H, Borzym K, Langer I, Beck A, Lehrach H, Reinhardt R, Pohl TM, Eger P, Zimmermann W, Wedler H, Wambutt R, Purnelle B, Goffeau A, Cadieu E, Dréano S, Gloux S, Lelaure V, Mottier S, Galibert F, Aves SJ, Xiang Z, Hunt C, Moore K, Hurst SM, Lucas M, Rochet M, Gaillardin C, Tallada VA, Garzon A, Thode G, Daga RR, Cruzado L, Jimenez J, Sánchez M, del Rey F, Benito J, Domínguez A, Revuelta JL, Moreno S, Armstrong J, Forsburg SL, Cerutti L, Lowe T, McCombie WR, Paulsen I, Potashkin J, Shpakovski GV, Ussery D, Barrell BG, Nurse P","authors_abbrev":"Wood V et al.","pubmed_publication_date":"21 Feb 2002","pubmed_entrez_date":"2002-02-23","publication_year":"2002","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC27B12.08","SPBC27.02c","SPBC12C2.12c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23843946","title":"The role of the RACK1 ortholog Cpc2p in modulating pheromone-induced cell cycle arrest in fission yeast.","citation":"PLoS One 2013;8(7):e65927","abstract":"The detection and amplification of extracellular signals requires the involvement of multiple protein components. In mammalian cells the receptor of activated C kinase (RACK1) is an important scaffolding protein for signal transduction networks. Further, it also performs a critical function in regulating the cell cycle by modulating the G1/S transition. Many eukaryotic cells express RACK1 orthologs, with one example being Cpc2p in the fission yeast Schizosaccharomyces pombe. In contrast to RACK1, Cpc2p has been described to positively regulate, at the ribosomal level, cells entry into M phase. In addition, Cpc2p controls the stress response pathways through an interaction with Msa2p, and sexual development by modulating Ran1p/Pat1p. Here we describe investigations into the role, which Cpc2p performs in controlling the G protein-mediated mating response pathway. Despite structural similarity to Gβ-like subunits, Cpc2p appears not to function at the G protein level. However, upon pheromone stimulation, cells overexpressing Cpc2p display substantial cell morphology defects, disorientation of septum formation and a significantly protracted G1 arrest. Cpc2p has the potential to function at multiple positions within the pheromone response pathway. We provide a mechanistic interpretation of this novel data by linking Cpc2p function, during the mating response, with its previous described interactions with Ran1p/Pat1p. We suggest that overexpressing Cpc2p prolongs the stimulated state of pheromone-induced cells by increasing ste11 gene expression. These data indicate that Cpc2p regulates the pheromone-induced cell cycle arrest in fission yeast by delaying cells entry into S phase.","doi":"10.1371/journal.pone.0065927","authors":"Mos M, Esparza-Franco MA, Godfrey EL, Richardson K, Davey J, Ladds G","authors_abbrev":"Mos M et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-12","publication_year":"2013","canto_session_key":"cc66e41e7390e086","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-01 12:43:41","canto_approved_date":"2021-12-19 13:15:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-30 14:18:43","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPCC1020.09","SPBC32F12.09","SPAC6B12.15","SPBC24C6.06","SPAC19D5.01","SPBC1685.01"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-06-01"},{"uniquename":"EMBL:SPD228","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6347208","title":"Mutagenicity studies on tibezonium, a new oropharyngeal disinfectant.","citation":"Arzneimittelforschung 1983;33(3):369-72","abstract":"N,N-Diethyl-N-methyl-[2-[[4-(4-phenylthio) phenyl]-3H-1,5-benzodiazepin-2-yl]thio]-ethanaminium iodide) (tibezonium iodide; CAS-54663-47-7), a new oropharyngeal disinfectant, was tested, using the Ames procedure with and without metabolic activation, on five strains of Salmonella typhimurium and using the host mediated assay with Schizosaccharomyces pombe as microorganism test. In both tests the drug did not show any mutagenic activity when compared with mutagenic standards.","authors":"Veronese M, Barzaghi D, Bertoncini A","authors_abbrev":"Veronese M et al.","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-01-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10704216","title":"In vitro reconstitution of the Schizosaccharomyces pombe alternative excision repair pathway.","citation":"Biochemistry 2000 Mar 14;39(10):2659-66","abstract":"Schizosaccharomyces pombe alternative excision repair has been shown genetically and biochemically to be involved in the repair of a wide variety of DNA lesions. AER is initiated by a damage-specific endonuclease (Uve1p) that recognizes UV-induced photoproducts, base mispairs, abasic sites, and platinum G-G diadducts and cleaves the DNA phosphodiester backbone 5' to a lesion. Several models exist that employ various mechanisms for damage removal based on the activities of Rad2p, a nuclease thought to be responsible for damage excision in AER. This study represents the first report of the biochemical reconstitution of the AER pathway. A base mispair-containing substrate is repaired in a reaction requiring S. pombe Uve1p, Rad2p, DNA polymerase delta, replication factor C, proliferating cell nuclear antigen, and T4 DNA ligase. Surprisingly, damage is removed exclusively by the 5' to 3' exonuclease activity of Rad2p and not its \"flap endonuclease\" activity and is absolutely dependent upon the presence of the 5'-phosphoryl moiety at the Uve1p cleavage site.","authors":"Alleva JL, Zuo S, Hurwitz J, Doetsch PW","authors_abbrev":"Alleva JL et al.","pubmed_publication_date":"14 Mar 2000","pubmed_entrez_date":"2000-03-08","publication_year":"2000","canto_session_key":"cb1db2b36b725fd0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-05-07 14:09:36","canto_approved_date":"2022-11-21 10:29:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-07 14:09:29","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.06c","SPAC27E2.10c","SPAC23D3.02","SPBC12D12.02c","SPBC23E6.07c","SPBC83.14c","SPBC947.11c","SPBC16D10.09","SPBC1734.02c","SPAC1687.03c","SPAC27E2.05","SPBC336.04","SPBC19C7.09c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2015-05-07"},{"uniquename":"EMBL:AU008446","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38905307","title":"Replication stress response in fission yeast differentially depends on maintaining proper levels of Srs2 helicase and Rrp1, Rrp2 DNA translocases.","citation":"PLoS One 2024;19(6):e0300434","abstract":"Homologous recombination is a key process that governs the stability of eukaryotic genomes during DNA replication and repair. Multiple auxiliary factors regulate the choice of homologous recombination pathway in response to different types of replication stress. Using Schizosaccharomyces pombe we have previously suggested the role of DNA translocases Rrp1 and Rrp2, together with Srs2 helicase, in the common synthesis-dependent strand annealing sub-pathway of homologous recombination. Here we show that all three proteins are important for completion of replication after hydroxyurea exposure and provide data comparing the effect of overproduction of Srs2 with Rrp1 and Rrp2. We demonstrate that Srs2 localises to rDNA region and is required for proper replication of rDNA arrays. Upregulation of Srs2 protein levels leads to enhanced replication stress, chromosome instability and viability loss, as previously reported for Rrp1 and Rrp2. Interestingly, our data suggests that dysregulation of Srs2, Rrp1 and Rrp2 protein levels differentially affects checkpoint response: overproduction of Srs2 activates simultaneously DNA damage and replication stress response checkpoints, while cells overproducing Rrp1 mainly launch DNA damage checkpoint. On the other hand, upregulation of Rrp2 primarily leads to replication stress response checkpoint activation. Overall, we propose that Srs2, Rrp1 and Rrp2 have important and at least partially independent functions in the maintenance of distinct difficult to replicate regions of the genome.","doi":"10.1371/journal.pone.0300434","authors":"Baranowska G, Misiorna D, Białek W, Kramarz K, Dziadkowiec D","authors_abbrev":"Baranowska G et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-06-21","publication_year":"2024","canto_session_key":"684f78d5c32fa3f2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-06-21 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23395004","title":"Protein determinants of meiotic DNA break hot spots.","citation":"Mol Cell 2013 Mar 07;49(5):983-96","abstract":"Meiotic recombination, crucial for proper chromosome segregation and genome evolution, is initiated by programmed DNA double-strand breaks (DSBs) in yeasts and likely all sexually reproducing species. In fission yeast, DSBs occur up to hundreds of times more frequently at special sites, called hot spots, than in other regions of the genome. What distinguishes hot spots from cold regions is an unsolved problem, although transcription factors determine some hot spots. We report the discovery that three coiled-coil proteins-Rec25, Rec27, and Mug20-bind essentially all hot spots with great specificity even without DSB formation. These small proteins are components of linear elements, are related to synaptonemal complex proteins, and are essential for nearly all DSBs at most hot spots. Our results indicate these hot spot determinants activate or stabilize the DSB-forming protein Rec12 (Spo11 homolog) rather than promote its binding to hot spots. We propose a paradigm for hot spot determination and crossover control by linear element proteins.","doi":"10.1016/j.molcel.2013.01.008","authors":"Fowler KR, Gutiérrez-Velasco S, Martín-Castellanos C, Smith GR","authors_abbrev":"Fowler KR et al.","pubmed_publication_date":"07 Mar 2013","pubmed_entrez_date":"2013-02-12","publication_year":"2013","canto_session_key":"35aab4b08bf43fb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Randy Hyppa","canto_first_approved_date":"2021-02-26 14:43:23","canto_approved_date":"2025-12-23 12:30:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-19 17:28:15","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Randy Hyppa","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36B7.06c","SPAC17A5.18c","SPBC577.05c","SPBC29A10.14","SPCC4E9.01c","SPAC25G10.04c","SPAC17A5.11"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2021-02-26"},{"uniquename":"PMID:24223771","title":"New insights into the RNA-based mechanism of action of the anticancer drug 5'-fluorouracil in eukaryotic cells.","citation":"PLoS One 2013;8(11):e78172","abstract":"5-Fluorouracil (5FU) is a chemotherapeutic drug widely used in treating a range of advanced, solid tumours and, in particular, colorectal cancer. Here, we used high-density tiling DNA microarray technology to obtain the specific transcriptome-wide response induced by 5FU in the eukaryotic model Schizosaccharomyces pombe. This approach combined with real-time quantitative PCR analysis allowed us to detect splicing defects of a significant number of intron-containing mRNA, in addition to identify some rRNA and tRNA processing defects after 5FU treatment. Interestingly, our studies also revealed that 5FU specifically induced the expression of certain genes implicated in the processing of mRNA, tRNA and rRNA precursors, and in the post-transcriptional modification of uracil residues in RNA. The transcription of several tRNA genes was also significantly induced after drug exposure. These transcriptional changes might represent a cellular response mechanism to counteract 5FU damage since deletion strains for some of these up-regulated genes were hypersensitive to 5FU. Moreover, most of these RNA processing genes have human orthologs that participate in conserved pathways, suggesting that they could be novel targets to improve the efficacy of 5FU-based treatments.","doi":"10.1371/journal.pone.0078172","authors":"Mojardín L, Botet J, Quintales L, Moreno S, Salas M","authors_abbrev":"Mojardín L et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-11-14","publication_year":"2013","canto_session_key":"ba339daa4ef4e392","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-12-06 14:02:44","canto_approved_date":"2025-02-12 09:42:11","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-12-06 14:02:37","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":33,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.08","SPAC10F6.04","SPAC222.05c","SPAC16.04","SPCC757.08","SPCC126.03","SPAC23H3.02c","SPCC613.09","SPBC28E12.05","SPAC15E1.04","SPCC10H11.01","SPBC31E1.03","SPAC4G8.07c","SPBC19C2.13c","SPAC167.03c","SPCC4B3.01","SPBC2G5.03","SPAC227.02c","SPAC12B10.08c","SPAC1556.05c","SPBC30B4.06c","SPAP8A3.06","SPBC1861.05","SPBC713.05","SPAC31G5.01","SPBC2G2.15c","SPAC3H5.04"],"gene_count":27,"ltp_gene_count":27,"approved_date":"2024-12-06"},{"uniquename":"EMBL:AU011221","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012388","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8799823","title":"A nitrogen starvation-induced dormant G0 state in fission yeast: the establishment from uncommitted G1 state and its delay for return to proliferation.","citation":"J Cell Sci 1996 Jun;109 ( Pt 6):1347-57","abstract":"Fission yeast cells either remain in the mitotic cell cycle or exit to meiotic sporulation from an uncommitted G1 state dependent on the presence or absence of nitrogen source in the medium (Nurse and Bissett, 1981). We examined how heterothallic haploid cells, which cannot sporulate, behave under nitrogen-starvation for longer than 25 days at 26 degrees C. These cells were shown to enter a stable state (designated the dormant G0) with nearly full viability. Maintaining the dormant cells required glucose, suggesting that the cells remained metabolically active although cell division had ceased. They differed dramatically from mitotic and uncommitted G1 cells in heat resistance, and also in cytoplasmic and nuclear morphologies. After nitrogen replenishment, the initial responses of dormant G0 cells were investigated. The kinetics for reentry into the proliferative state were delayed considerably, and the changes in cell shape were enhanced particularly for those recovering from extended nitrogen starvation. A part of the delay could be accounted for by the duration of nuclear decondensation and cell elongation for the first cell division.","authors":"Su SS, Tanaka Y, Samejima I, Tanaka K, Yanagida M","authors_abbrev":"Su SS et al.","pubmed_publication_date":"Jun 1996","pubmed_entrez_date":"1996-06-01","publication_year":"1996","canto_session_key":"e398704ee4160f3a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-12-15 21:58:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-15 21:58:34","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-12-15"},{"uniquename":"EMBL:AU013453","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8462095","title":"A 13 kb resolution cosmid map of the 14 Mb fission yeast genome by nonrandom sequence-tagged site mapping.","citation":"Cell 1993 Apr 09;73(1):121-32","abstract":"We present the application of a nonrandom sequence-tagged site (STS) content detection method in mapping an entire genome, that of fission yeast. The novelty of our strategy is in the use of STS probes made from both ends of cosmid clones, selected on the basis of \"sample without replacement\" (only library clones that show no previous positive hybridization are selected and made into probes). We developed powerful techniques, based on consistency analysis, for error detection and contig assembly. In addition, we probed our library with genetically mapped markers and Notl or Sfil linking clones, thereby anchoring contigs onto chromosomes. Our map contains more than 1000 sites, including genes (most were previously unmapped), occurrences of known repetitive elements, and Notl-Sfil restriction sites.","authors":"Mizukami T, Chang WI, Garkavtsev I, Kaplan N, Lombardi D, Matsumoto T, Niwa O, Kounosu A, Yanagida M, Marr TG","authors_abbrev":"Mizukami T et al.","pubmed_publication_date":"09 Apr 1993","pubmed_entrez_date":"1993-04-09","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9343409","title":"Characterization of a Holliday junction-resolving enzyme from Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1997 Nov;17(11):6465-71","abstract":"The rearrangement and repair of DNA by homologous recombination involves the creation of Holliday junctions, which are cleaved by a class of junction-specific endonucleases to generate recombinant duplex DNA products. Only two cellular junction-resolving enzymes have been identified to date: RuvC in eubacteria and CCE1 from Saccharomyces cerevisiae mitochondria. We have identified a protein from Schizosaccharomyces pombe which has 28% sequence identity to CCE1. The YDC2 protein has been cloned and overexpressed in Escherichia coli, and the purified recombinant protein has been shown to be a Holliday junction-resolving enzyme. YDC2 has a high degree of specificity for the structure of the four-way junction, to which it binds as a dimer. The enzyme exhibits a sequence specificity for junction cleavage that differs from both CCE1 and RuvC, and it cleaves fixed junctions at the point of strand exchange. The conservation of the mechanism of Holliday junction cleavage between two organisms as diverse as S. cerevisiae and S. pombe suggests that there may be a common pathway for mitochondrial homologous recombination in fungi, plants, protists, and possibly higher eukaryotes.","authors":"White MF, Lilley DM","authors_abbrev":"White MF et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1997-10-29","publication_year":"1997","canto_session_key":"6363e0c80e2bc586","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-09-01 16:24:27","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-01 16:24:20","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-01"},{"uniquename":"PMID:24256276","title":"Use of PKA-mediated phenotypes for genetic and small-molecule screens in Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 2013 Dec;41(6):1692-5","abstract":"PKA (protein kinase A) in the fission yeast Schizosaccharomyces pombe controls transcription of genes involved in metabolism, cell growth and sexual development. In the present review, we discuss phenotypes associated with either high or low PKA activity in the context of how they can be used to carry out genetic or small-molecule screens that affect components of the PKA pathway. Although our recent research has focused on the study of heterologously expressed cyclic nucleotide PDEs (phosphodiesterases), these same methods can be used to target other S. pombe proteins or their functionally equivalent orthologues that act in the PKA pathway.","doi":"10.1042/BST20130159","authors":"de Medeiros AS, Magee A, Nelson K, Friedberg L, Trocka K, Hoffman CS","authors_abbrev":"de Medeiros AS et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11690648","title":"Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in Dictyostelium discoideum and Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2001 Oct 31;1521(1-3):146-51","abstract":"We screened the Dictyostelium discoideum two-hybrid cDNA library with the SNW/SKIP transcription coregulator SnwA and identified a novel cyclophilin CypE. Independently, the Schizosaccharomyces pombe cDNA library was screened with the SnwA ortholog Snw1 and the ortholog of CypE (named Cyp2) was found. Both cyclophilins bind the respective SNW protein in their autologous systems. The interaction was localized to the N-terminal part of SnwA as well as of Snw1. CypE was confirmed in vitro to be a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase. Remarkably, both SNW proteins bind the cyclophilins in a cyclosporin A independent manner, possibly serving as adaptors for these novel isomerases. These results are the first characterization of the members of a novel cyclophilin subfamily, which includes the human CGI-124/PPIL1 protein.","authors":"Skruzný M, Ambrozková M, Fuková I, Martínková K, Blahůsková A, Hamplová L, Půta F, Folk P","authors_abbrev":"Skruzný M et al.","pubmed_publication_date":"31 Oct 2001","pubmed_entrez_date":"2001-11-03","publication_year":"2001","canto_session_key":"68b41e3476ce7ef4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-04 19:14:19","canto_approved_date":"2022-11-14 17:03:24","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2016-10-04 19:13:46","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.03","SPCC188.11"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-10-04"},{"uniquename":"EMBL:SPHSP16","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24906232","title":"Comparative evolutionary analysis of cell cycle proteins networks in fission and budding yeast.","citation":"Cell Biochem Biophys 2014 Nov;70(2):1167-75","abstract":"Fission yeast and budding yeast are the two distantly related species with common ancestors. Various studies have shown significant differences in metabolic networks and regulatory networks. Cell cycle regulatory proteins in both species have differences in structural as well as in functional organization. Orthologous proteins in cell cycle regulatory protein networks seem to play contemporary role in both species during the evolution but little is known about non-orthologous proteins. Here, we used system biology approach to compare topological parameters of orthologous and non-orthologous proteins to find their contributions during the evolution to make an efficient cell cycle regulation. Observed results have shown a significant role of non-orthologous proteins in fission yeast in maintaining the efficiency of cell cycle regulation with less number of proteins as compared to budding yeast.","doi":"10.1007/s12013-014-0037-y","authors":"Singh PK, Shakya M","authors_abbrev":"Singh PK et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-06-08","publication_year":"2014","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27250943","title":"Staining Fission Yeast Filamentous Actin with Fluorescent Phalloidin Conjugates.","citation":"Cold Spring Harb Protoc 2016 Jun 01;2016(6)","abstract":"The Schizosaccharomyces pombe filamentous (F)-actin cytoskeleton drives cell growth, morphogenesis, endocytosis, and cytokinesis. The protocol described here reveals the distribution of F-actin in fixed cells through the use of fluorescently conjugated phalloidin. Simultaneous staining of cell wall landmarks (with calcofluor) and chromatin (with 4',6-diamidino-2-phenylindole, or DAPI) makes this rapid staining procedure highly effective for staging cell cycle progression, monitoring morphogenetic abnormalities, and assessing the impact of environmental and genetic changes on the integrity of the F-actin cytoskeleton.","doi":"10.1101/pdb.prot091033","authors":"Hagan IM","authors_abbrev":"Hagan IM","pubmed_publication_date":"01 Jun 2016","pubmed_entrez_date":"2016-06-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-06-04 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37939299","title":"Expected and Unexpected Products from the Biochemical Oxidation of Bacterial Alkylquinolones with CYP4F11.","citation":"J Nat Prod 2023 Nov 24;86(11):2502-2513","abstract":"2-Alkylquinolones are a class of microbial natural products primarily produced in the  Pseudomonas  and  Burkholderia  genera that play a key role in modulating quorum sensing. Bacterial alkylquinolones were synthesized and then subjected to oxidative biotransformation using human cytochrome P450 enzyme CYP4F11, heterologously expressed in the fission yeast  Schizosaccharomyces pombe . This yielded a range of hydroxylated and carboxylic acid derivatives which had undergone ω-oxidation of the 2-alkyl chain, the structures of which were determined by analysis of NMR and MS data. Oxidation efficiency depended on chain length, with a chain length of eight or nine carbon atoms proving optimal for high yields. Homology modeling suggested that Glu233 was relevant for binding, due to the formation of a hydrogen bond from the quinolone nitrogen to Glu233, and in this position only the longer alkyl chains could come close enough to the heme moiety for effective oxidation. In addition to the direct oxidation products, a number of esters were also isolated, which was attributed to the action of endogenous yeast enzymes on the newly formed ω-hydroxy-alkylquinolones. ω-Oxidation of the alkyl chain significantly reduced the antimicrobial and antibiofilm activity of the quinolones.","doi":"10.1021/acs.jnatprod.3c00689","authors":"Shi Y, Li J, Wolf CA, Liu S, Sharma SS, Wolber G, Bureik M, Clark BR","authors_abbrev":"Shi Y et al.","pubmed_publication_date":"24 Nov 2023","pubmed_entrez_date":"2023-11-08","publication_year":"2023","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2023-11-09 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22134091","title":"A mutation of the fission yeast EB1 overcomes negative regulation by phosphorylation and stabilizes microtubules.","citation":"Exp Cell Res 2012 Feb 01;318(3):262-75","abstract":"Mal3 is a fission yeast homolog of EB1, a plus-end tracking protein (+TIP). We have generated a mutation (89R) replacing glutamine with arginine in the calponin homology (CH) domain of Mal3. Analysis of the 89R mutant in vitro has revealed that the mutation confers a higher affinity to microtubules and enhances the intrinsic activity to promote the microtubule-assembly. The mutant Mal3 is no longer a +TIP, but binds strongly the microtubule lattice. Live cell imaging has revealed that while the wild type Mal3 proteins dissociate from the tip of the growing microtubules before the onset of shrinkage, the mutant Mal3 proteins persist on microtubules and reduces a rate of shrinkage after a longer pausing period. Consequently, the mutant Mal3 proteins cause abnormal elongation of microtubules composing the spindle and aster. Mal3 is phosphorylated at a cluster of serine/threonine residues in the linker connecting the CH and EB1-like C-terminal motif domains. The phosphorylation occurs in a microtubule-dependent manner and reduces the affinity of Mal3 to microtubules. We propose that because the 89R mutation is resistant to the effect of phosphorylation, it can associate persistently with microtubules and confers a stronger stability of microtubules likely by reinforcing the cylindrical structure.","doi":"10.1016/j.yexcr.2011.11.006","authors":"Iimori M, Ozaki K, Chikashige Y, Habu T, Hiraoka Y, Maki T, Hayashi I, Obuse C, Matsumoto T","authors_abbrev":"Iimori M et al.","pubmed_publication_date":"01 Feb 2012","pubmed_entrez_date":"2011-12-03","publication_year":"2012","canto_session_key":"1854edb1fb4a0e10","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-31 11:48:10","canto_approved_date":"2025-05-28 07:57:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-30 14:38:34","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-10-31"},{"uniquename":"PMID:714018","title":"Extrachromosomal inheritance in Schizosaccharomyces pombe. VIII. Extent of cytoplasmic mixing in zygotes estimated by tetrad analysis of crosses involving mitochondrial markers conferring resistance to antimycin, chloramphenicol, and erythromycin.","citation":"Mol Gen Genet 1978 Sep 08;164(3):321-9","abstract":"","authors":"Wolf K, Seitz-Mayr G, Kaudewitz F","authors_abbrev":"Wolf K et al.","pubmed_publication_date":"08 Sep 1978","pubmed_entrez_date":"1978-09-08","publication_year":"1978","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12442907","title":"A glucose-inducible gene in Schizosaccharomyces pombe, rrg1+, is involved in negative regulation of G2/M progression.","citation":"Mol Cells 2002 Oct 31;14(2):312-7","abstract":"A glucose-inducible gene in S. pombe is rrg1+. Its mRNA level is rapidly decreased and increased by glucose-depletion and readdition, respectively. The previous study revealed that the rrg1+ expression was regulated by glucose-dependent mRNA stability control. To understand the significance of the glucose-dependent expression of rrg1+, the cellular function of rrg1+ was explored. Deletion of the rrg1+ gene from the haploid chromosome of S. pombe cells did not lead to cell lethality but brought about cell size reduction, which was accompanied by fast cell proliferation. In accordance with this result, the overexpression of the Rrgl protein under the control of the nmt1 promoter produced elongated cells of G2 delay, and consequently resulted in the slowing-down of cell proliferation. In addition, the rrg1+ mRNA level showed cell-cycle dependent changes, peaking at G2/M. These results demonstrate that Rrg1 might be involved in the negative regulation of cell proliferation and G2/M progression for cell size control.","authors":"Kim MJ, Park EJ, Park SD","authors_abbrev":"Kim MJ et al.","pubmed_publication_date":"31 Oct 2002","pubmed_entrez_date":"2002-11-22","publication_year":"2002","canto_session_key":"5225c988b7cbf341","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-29 11:51:10","canto_approved_date":"2021-02-02 20:04:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-28 11:34:21","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-01-29"},{"uniquename":"TreeFam:TF300479","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.03c","YMR231W"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32306350","title":"Yeast Flocculin: Methods for Quantitative Analysis of Flocculation in Yeast Cells.","citation":"Methods Mol Biol 2020;2132:437-444","abstract":"Flocculation, the clump forming property of yeast, has long been appreciated in breweries and utilized as an off-cost method to enable the reuse of yeast cells. Members of the flocculin protein family were identified as the adherent proteins on the cell surface responsible for flocculation, and their properties have been investigated. Crystal structures of the adhesion domain of flocculins revealed their unique mode of ligand binding where a calcium ion is located in the middle of the interface between flocculin and the interacting sugar. Here we describe the most commonly used flocculation assay. The method is simple and easy, yet it is the most direct and reliable assay to evaluate the flocculation cellular phenotype.","doi":"10.1007/978-1-0716-0430-4_42","authors":"Maekawa H, Takegawa K","authors_abbrev":"Maekawa H et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-04-20","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-03-10 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:87335","title":"The cell cycle thermal-inactivation sensitive stage of Schizosaccharomyces pombe is independent of 2-phenylethanol-induced changes in S phase location.","citation":"Exp Cell Res 1979 Jul;121(2):441-5","abstract":"","authors":"Bullock JG, Coakley WT","authors_abbrev":"Bullock JG et al.","pubmed_publication_date":"Jul 1979","pubmed_entrez_date":"1979-07-01","publication_year":"1979","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23150603","title":"A mammalian-like DNA damage response of fission yeast to nucleoside analogs.","citation":"Genetics 2013 Jan;193(1):143-57","abstract":"Nucleoside analogs are frequently used to label newly synthesized DNA. These analogs are toxic in many cells, with the exception of the budding yeast. We show that Schizosaccharomyces pombe behaves similarly to metazoans in response to analogs 5-bromo-2'-deoxyuridine (BrdU) and 5-ethynyl-2'-deoxyuridine (EdU). Incorporation causes DNA damage that activates the damage checkpoint kinase Chk1 and sensitizes cells to UV light and other DNA-damaging drugs. Replication checkpoint mutant cds1Δ shows increased DNA damage response after exposure. Finally, we demonstrate that the response to BrdU is influenced by the ribonucleotide reductase inhibitor, Spd1, suggesting that BrdU causes dNTP pool imbalance in fission yeast, as in metazoans. Consistent with this, we show that excess thymidine induces G1 arrest in wild-type fission yeast expressing thymidine kinase. Thus, fission yeast responds to nucleoside analogs similarly to mammalian cells, which has implications for their use in replication and damage research, as well as for dNTP metabolism.","doi":"10.1534/genetics.112.145730","authors":"Sabatinos SA, Mastro TL, Green MD, Forsburg SL","authors_abbrev":"Sabatinos SA et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2012-11-15","publication_year":"2013","canto_session_key":"2e69b93dfb767faa","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28046110","title":"Network Centrality Analysis in Fungi Reveals Complex Regulation of Lost and Gained Genes.","citation":"PLoS One 2017;12(1):e0169459","abstract":"Gene gain and loss shape both proteomes and the networks they form. The increasing availability of closely related sequenced genomes and of genome-wide network data should enable a better understanding of the evolutionary forces driving gene gain, gene loss and evolutionary network rewiring. Using orthology mappings across 23 ascomycete fungi genomes, we identified proteins that were lost, gained or universally conserved across the tree, enabling us to compare genes across all stages of their life-cycle. Based on a collection of genome-wide network and gene expression datasets from baker's yeast, as well as a few from fission yeast, we found that gene loss is more strongly associated with network and expression features of closely related species than that of distant species, consistent with the evolutionary modulation of gene loss propensity through network rewiring. We also discovered that lost and gained genes, as compared to universally conserved \"core\" genes, have more regulators, more complex expression patterns and are much more likely to encode for transcription factors. Finally, we found that the relative rate of network integration of new genes into the different types of networks agrees with experimentally measured rates of network rewiring. This systems-level view of the life-cycle of eukaryotic genes suggests that the gain and loss of genes is tightly coupled to the gain and loss of network interactions, that lineage-specific adaptations drive regulatory complexity and that the relative rates of integration of new genes are consistent with network rewiring rates.","doi":"10.1371/journal.pone.0169459","authors":"Coulombe-Huntington J, Xia Y","authors_abbrev":"Coulombe-Huntington J et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-01-04","publication_year":"2017","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2017-01-05 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21776497","title":"In vivo multimode Raman imaging reveals concerted molecular composition and distribution changes during yeast cell cycle.","citation":"Chem Commun (Camb) 2011 Sep 07;47(33):9423-5","abstract":"In vivo time-lapse Raman imaging reveals highly dynamic and concerted changes in concentration and distribution of phospholipids and proteins during and after cell division of a single living Schizosaccharomyces pombe cell.","doi":"10.1039/c1cc12350e","authors":"Huang CK, Hamaguchi HO, Shigeto S","authors_abbrev":"Huang CK et al.","pubmed_publication_date":"07 Sep 2011","pubmed_entrez_date":"2011-07-22","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9315645","title":"Multiple regulatory domains on the Byr2 protein kinase.","citation":"Mol Cell Biol 1997 Oct;17(10):5876-87","abstract":"Byr2 protein kinase, a homolog of mammalian mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEKK) and Saccharomyces cerevisiae STE11, is required for pheromone-induced sexual differentiation in the fission yeast Schizosaccharomyces pombe. Byr2 functions downstream of Ste4, Ras1, and the membrane-associated receptor-coupled heterotrimeric G-protein alpha subunit, Gpa1. Byr2 has a distinctive N-terminal kinase regulatory domain and a characteristic C-terminal kinase catalytic domain. Ste4 and Ras1 interact with the regulatory domain of Byr2 directly. Here, we define the domains of Byr2 that bind Ste4 and Ras1 and show that the Byr2 regulatory domain binds to the catalytic domain in the two-hybrid system. Using Byr2 mutants, we demonstrate that these direct physical interactions are all required for proper signaling. In particular, the physical association between Byr2 regulatory and catalytic domains appears to result in autoinhibition, the loss of which results in kinase activation. Furthermore, we provide evidence that Shk1, the S. pombe homolog of the STE20 protein kinase, can directly antagonize the Byr2 intramolecular interaction, possibly by phosphorylating Byr2.","authors":"Tu H, Barr M, Dong DL, Wigler M","authors_abbrev":"Tu H et al.","pubmed_publication_date":"Oct 1997","pubmed_entrez_date":"1997-10-07","publication_year":"1997","canto_session_key":"c3f91b7bec8a34a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-05-10 12:30:56","canto_approved_date":"2025-12-14 19:08:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-10 12:30:36","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1565.04c","SPBC1604.14c","SPAC1D4.13","SPBC24C6.06","SPBC1D7.05","SPAC17H9.09c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-05-10"},{"uniquename":"PMID:23722945","title":"An expanded view of the eukaryotic cytoskeleton.","citation":"Mol Biol Cell 2013 Jun;24(11):1615-8","abstract":"A rich and ongoing history of cell biology research has defined the major polymer systems of the eukaryotic cytoskeleton. Recent studies have identified additional proteins that form filamentous structures in cells and can self-assemble into linear polymers when purified. This suggests that the eukaryotic cytoskeleton is an even more complex system than previously considered. In this essay, I examine the case for an expanded definition of the eukaryotic cytoskeleton and present a series of challenges for future work in this area.","doi":"10.1091/mbc.E12-10-0732","authors":"Moseley JB","authors_abbrev":"Moseley JB","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-06-01","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:47:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38415071","title":"The Cdc14 phosphatase, Clp1, does not affect genome expression.","citation":"MicroPubl Biol 2024;2024","abstract":" Schizosaccharomyces pombe  Clp1 is a Cdc14-family phosphatase that reverses mitotic Cdk1 phosphorylation. Despite evolutionary conservation, Clp1 's mammalian orthologs do not share this function. Rather, higher eukaryotic Cdc14 enzymes act in DNA repair, ciliogenesis, and gene regulation. To examine if Clp1 regulates gene expression, we compared the transcriptional profiles of cells lacking Clp1 function to that of wildtype. Because  clp1∆  cells are sensitive to the actin depolymerizing drug, LatrunculinA, we also investigated whether a transcriptional response was involved. Our results indicate that Clp1 does not detectably affect gene expression and highlight the organism-specific functions of this conserved phosphatase family.","doi":"10.17912/micropub.biology.001089","authors":"Lopez Maury L, Ren L, Hassan S, Bähler J, Gould KL","authors_abbrev":"Lopez Maury L et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-02-28","publication_year":"2024","canto_session_key":"26061630001e61e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-10-09 07:41:21","canto_approved_date":"2024-10-09 07:41:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-10-04 16:31:31","canto_added_date":"2024-02-29 00:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":22,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC513.03","SPAC212.11","SPAC139.05","SPBC16E9.16c","SPAC1782.09c","SPBC23G7.10c","SPBC1711.02","SPCC330.05c","SPAC186.05c","SPBC24C6.09c","SPAC23H3.15c","SPAC212.06c","SPBC21C3.19","SPBPB21E7.04c","SPAC27D7.03c"],"gene_count":15,"ltp_gene_count":6,"approved_date":"2024-10-09"},{"uniquename":"PMID:39727386","title":"Draft genome sequences of  Schizosaccharomyces pombe  strain I-540 isolated from grape must.","citation":"Microbiol Resour Announc 2024 Dec 27;:e0113524","abstract":" Schizosaccharomyces pombe  is a non-Saccharomyces yeast that is widely used in winemaking due to its ability to ferment malic acid, thus improving organoleptic properties of wine. We report the draft genome sequence of  S. pombe  strain I-540, isolated from grape must in Russia.","doi":"10.1128/mra.01135-24","authors":"Vasyagin EA, Beletsky AV, Ivanova EV, Shalamitskiy MY, Mardanov AV, Ravin NV","authors_abbrev":"Vasyagin EA et al.","pubmed_publication_date":"27 Dec 2024","pubmed_entrez_date":"2024-12-27","publication_year":"2024","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2024-12-28 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23293578","title":"Molecular genetics of charcot-marie-tooth disease: from genes to genomes.","citation":"Mol Syndromol 2012 Nov;3(5):204-14","abstract":"Charcot-Marie-Tooth disease (CMT) is a heterogeneous group of disorders of the peripheral nervous system, mainly characterized by distal muscle weakness and atrophy leading to motor handicap. With an estimated prevalence of 1 in 2,500, this condition is one of the most commonly inherited neurological disorders. Mutations in more than 30 genes affecting glial and/or neuronal functions have been associated with different forms of CMT leading to a substantial improvement in diagnostics of the disease and in the understanding of implicated pathophysiological mechanisms. However, recent data from systematic genetic screening performed in large cohorts of CMT patients indicated that molecular diagnosis could be established only in ∼50-70% of them, suggesting that additional genes are involved in this disease. In addition to providing an overview of genetic and functional data concerning various CMT forms, this review focuses on recent data generated through the use of highly parallel genetic technologies (SNP chips, sequence capture and next-generation DNA sequencing) in CMT families, and the current and future impact of these technologies on gene discovery and diagnostics of CMTs.","doi":"10.1159/000343487","authors":"Azzedine H, Senderek J, Rivolta C, Chrast R","authors_abbrev":"Azzedine H et al.","pubmed_publication_date":"Nov 2012","pubmed_entrez_date":"2013-01-08","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1A10.10c","SPAC3F10.03","SPCC1620.06c","SPBC3E7.02c","SPAC1093.03","SPBC3D6.06c","SPCC338.06c","SPAC23C11.09","SPBC1706.03"],"gene_count":9,"ltp_gene_count":0},{"uniquename":"PMID:34614242","title":"Fission yeast RNA-binding proteins Puf2 and Puf4 are involved in repression of ferrireductase Frp1 expression in response to iron.","citation":"Mol Microbiol 2021 Nov;116(5):1361-1377","abstract":"This study identifies a post-transcriptional mechanism of iron uptake regulation by Puf2 and Puf4 of the Pumilio and FBF (Puf) family of RNA-binding proteins in Schizosaccharomyces pombe. Cells expressing Puf2 and Puf4 stimulate decay of the frp1 +  mRNA encoding a key enzyme of the reductive iron uptake pathway. Results consistently showed that frp1 +  mRNA is stabilized in puf2Δ puf4Δ mutant cells under iron-replete conditions. As a result, puf2Δ puf4Δ cells exhibit an increased sensitivity to iron accompanied by enhanced ferrireductase activity. A pool of GFP-frp1 +  3'UTR RNAs was generated using a reporter gene containing the 3' untranslated region (UTR) of frp1 +  that was under the control of a regulatable promoter. Results showed that Puf2 and Puf4 accelerate the destabilization of mRNAs containing the frp1 +  3'UTR which harbors two Pumilio response elements (PREs). Binding studies revealed that the PUM-homology RNA-binding domain of Puf2 and Puf4 expressed in Escherichia coli specifically interacts with PREs in the frp1 +  3'UTR. Using RNA immunoprecipitation in combination with reverse transcription qPCR assays, results showed that Puf2 and Puf4 interact preferentially with frp1 +  mRNA under basal and iron-replete conditions, thereby contributing to inhibit Frp1 production and protecting cells against toxic levels of iron.","doi":"10.1111/mmi.14829","authors":"Beaudoin J, Normant V, Brault A, Henry DJ, Bachand F, Massé É, Chua G, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"Nov 2021","pubmed_entrez_date":"2021-10-06","publication_year":"2021","canto_session_key":"58e46bca55a217be","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-10-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17977837","title":"Identification and characterization of an essential telomeric repeat binding factor in fission yeast.","citation":"J Biol Chem 2008 Feb 01;283(5):2693-701","abstract":"Whereas mammalian cells harbor two double strand telomeric repeat binding factors, TRF1 and TRF2, the fission yeast Schizosaccharomyces pombe has been thought to harbor solely the TRF1/TRF2 ortholog Taz1p to perform comparable functions. Here we report the identification of telomeric repeat binding factor 1 (Tbf1), a second TRF1/TRF2 ortholog in S. pombe. Like the Taz1p, the identified Tbf1p shares amino acid sequence similarity, as well as structural and functional characteristics, with the mammalian TRF1 and TRF2 proteins. This family of proteins shares a common architecture with two separate structural domains. An N-terminal domain is necessary and sufficient for the formation of homodimers, and a C-terminal MYB/homeodomain mediates sequence specific recognition of double-stranded telomeric DNA. The identified Tbf1p binds S. pombe telomeric DNA with high sequence specificity in vitro. Targeted deletion of the tbf1 gene reveals that it is essential for survival, and overexpression of the tbf1 gene leads to telomere elongation in vivo, which is dependent upon the MYB domain. These data suggest that fission yeast, like mammals, have two factors that bind double-stranded telomeric DNA and perform distinct roles in telomere length regulation.","authors":"Pitt CW, Valente LP, Rhodes D, Simonsson T","authors_abbrev":"Pitt CW et al.","pubmed_publication_date":"01 Feb 2008","pubmed_entrez_date":"2007-11-06","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19G7.13"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:41087100","title":"Unique Role of Med8 in Ace2 Recruitment and Target Gene Expression in  Schizosaccharomyces pombe .","citation":"J Microbiol Biotechnol 2025 Oct 14;35:e2507055","abstract":"The Mediator, an essential RNA polymerase II coactivator, is a conserved multi-subunit protein complex present in organisms ranging from yeast to humans. Although its role in transcription is well-characterized, the distinct functions of its subunits remain largely unclear. In this study, we aimed to investigate the roles of Med8, Med14, and Med17 in Ace2-dependent transcriptional regulation in  Schizosaccharomyces pombe . Transcriptome analysis revealed that depletion of Med14 and Med17 caused widespread transcriptional repression, consistent with their structural roles in maintaining Mediator integrity. In contrast, depletion of Med8 specifically impaired the transcription of Ace2 target genes. Chromatin-binding analysis revealed that despite stable Ace2 protein levels, Med8 depletion led to a remarkable decrease in Ace2 occupancy at the target promoters, indicating that Med8 plays a crucial role in the recruitment of Ace2. In contrast, the binding of Ace2 was largely unaffected by the depletion of Med14 or Med17, underscoring their involvement in the transcriptional activation steps following Ace2 recruitment. Moreover, depletion of Med8 did not influence the expression or genome binding of Med14 and Med17, suggesting that Med8 plays a distinct role, rather than maintaining Mediator stability. Co-immunoprecipitation further revealed a physical association between Med8 and Ace2, suggesting that Med8 may be involved in Ace2-dependent transcriptional regulation. Overall, our findings highlighted that Med8 uniquely promotes Ace2-dependent transcriptional initiation by enhancing the recruitment of transcription factors. The study could advance our understanding of how individual Mediator subunits fine-tune gene expression through direct interactions with specific transcription factors.","doi":"10.4014/jmb.2507.07055","authors":"Kim JH, Kim KD","authors_abbrev":"Kim JH et al.","pubmed_publication_date":"14 Oct 2025","pubmed_entrez_date":"2025-10-14","publication_year":"2025","canto_session_key":"f69fab6edebc4ed3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-15 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6G10.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24192486","title":"The conserved Fanconi anemia nuclease Fan1 and the SUMO E3 ligase Pli1 act in two novel Pso2-independent pathways of DNA interstrand crosslink repair in yeast.","citation":"DNA Repair (Amst) 2013 Dec;12(12):1011-23","abstract":"DNA interstrand cross-links (ICLs) represent a physical barrier to the progression of cellular machinery involved in DNA metabolism. Thus, this type of adduct represents a serious threat to genomic stability and as such, several DNA repair pathways have evolved in both higher and lower eukaryotes to identify this type of damage and restore the integrity of the genetic material. Human cells possess a specialized ICL-repair system, the Fanconi anemia (FA) pathway. Conversely yeasts rely on the concerted action of several DNA repair systems. Recent work in higher eukaryotes identified and characterized a novel conserved FA component, FAN1 (Fanconi anemia-associated nuclease 1, or FANCD2/FANCI-associated nuclease 1). In this study, we characterize Fan1 in the yeast Schizosaccharomyces pombe. Using standard genetics, we demonstrate that Fan1 is a key component of a previously unidentified ICL-resolution pathway. Using high-throughput synthetic genetic arrays, we also demonstrate the existence of a third pathway of ICL repair, dependent on the SUMO E3 ligase Pli1. Finally, using sequence-threaded homology models, we predict and validate key residues essential for Fan1 activity in ICL repair.","doi":"10.1016/j.dnarep.2013.10.003","authors":"Fontebasso Y, Etheridge TJ, Oliver AW, Murray JM, Carr AM","authors_abbrev":"Fontebasso Y et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-07","publication_year":"2013","canto_session_key":"006084139334e409","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-02-02 16:32:57","canto_approved_date":"2024-05-13 06:05:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-15 12:19:47","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":123,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.10","SPBC146.06c","SPAC15A10.16","SPAC1D4.06c","SPAC11E3.04c","SPBC337.07c","SPBC1709.13c","SPAC1565.04c","SPAC13C5.03","SPBP4G3.02","SPAC3H5.07","SPAP7G5.05","SPAC9E9.14","SPAC25B8.18","SPAC15E1.10","SPAC1F12.02c","SPAC10F6.12c","SPCC18.17c","SPAC13G7.05","SPAC22A12.01c","SPBC1734.06","SPAC17A2.06c","SPCC970.01","SPAC644.14c","SPACUNK4.12c","SPBC1734.12c","SPCC1795.06","SPBPB2B2.10c","SPAC1D4.13","SPCC1235.09","SPAC15A10.15","SPAC20G4.04c","SPBC13E7.03c","SPBC24C6.06","SPBC2G2.10c","SPAC15A10.08","SPAC1952.07","SPAC14C4.13","SPAC15E1.05c","SPAC9.05","SPAC11D3.18c","SPAC24C9.14","SPBC3E7.08c","SPBC3B8.02","SPBP35G2.13c","SPBC19G7.04","SPBC428.14","SPCC1223.02","SPBC3E7.11c","SPAP7G5.04c","SPBC13E7.04","SPAC664.07c","SPAC1687.05","SPCC23B6.05c","SPBC216.05","SPBC21.05c","SPBC651.02","SPAC17A2.13c","SPBC29A3.21","SPAC6B12.12","SPAC24B11.12c","SPCC16C4.11","SPCC1393.10","SPBC1734.05c","SPAC23E2.03c","SPAC11G7.02","SPCC584.13","SPAC4D7.06c","SPBC1734.15","SPBC1921.05","SPAC17G8.13c","SPAC24H6.03","SPBC1D7.05","SPAC3C7.03c","SPBC18H10.06c","SPAC323.01c","SPAC12B10.05","SPCC126.11c","SPAC25A8.01c"],"gene_count":79,"ltp_gene_count":61,"approved_date":"2018-02-02"},{"uniquename":"PMID:20180855","title":"Different steps of sexual development are differentially regulated by the Sec8p and Exo70p exocyst subunits.","citation":"FEMS Microbiol Lett 2010 Apr;305(1):71-80","abstract":"In this paper we show that in Schizosaccharomyces pombe, mating-specific cell adhesion is dependent on the exocyst subunit Sec8p, but independent of the exocyst subunit Exo70p. In the absence of Exo70p, the forespore membrane does not develop properly and the leading edge protein Meu14p is abnormally distributed. Additionally, the spindle pole body is aberrant in a significant number of exo70Delta asci. In both the sec8-1 and the exo70Delta mutants, the development of the spore cell wall is impaired. These results show that different steps of sexual development are differentially regulated by the exocyst and suggest the existence of exocyst subcomplexes with distinct roles in mating.","doi":"10.1111/j.1574-6968.2010.01915.x","authors":"Sharifmoghadam MR, de Leon N, Hoya M, Curto MA, Valdivieso MH","authors_abbrev":"Sharifmoghadam MR et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-02-26","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23500374","title":"Scalable nano-bioprobes with sub-cellular resolution for cell detection.","citation":"Biosens Bioelectron 2013 Jul 15;45:267-73","abstract":"Here we present a carbon nanotube based device to noninvasively and quickly detect mobile single cells with the potential to maintain a high degree of spatial resolution. The device utilizes standard complementary metal oxide semiconductor (CMOS) technologies for fabrication, allowing it to be easily scalable (down to a few nanometers). Nanotubes are deposited using electrophoresis after fabrication in order to maintain CMOS compatibility. The devices are spaced by 6 μm which is the same size or smaller than a single cell. To demonstrate its capability to detect cells, we performed impedance spectroscopy on mobile human embryonic kidney (HEK) cells, neurons cells from mice, and yeast cells (S. pombe). Measurements were performed with and without cells and with and without nanotubes. Nanotubes were found to be crucial to successfully detect the presence of cells. The devices are also able to distinguish between cells with different characteristics.","doi":"10.1016/j.bios.2013.01.066","authors":"Kanwal A, Lakshmanan S, Bendiganavale A, Bot CT, Patlolla A, Raj R, Prodan C, Iqbal Z, Thomas GA, Farrow RC","authors_abbrev":"Kanwal A et al.","pubmed_publication_date":"15 Jul 2013","pubmed_entrez_date":"2013-03-19","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38514187","title":"The Rtf1/Prf1-dependent histone modification axis counteracts multi-drug resistance in fission yeast.","citation":"Life Sci Alliance 2024 Jun;7(6)","abstract":"RNA polymerase II transcription elongation directs an intricate pattern of histone modifications. This pattern includes a regulatory cascade initiated by the elongation factor Rtf1, leading to monoubiquitylation of histone H2B, and subsequent methylation of histone H3 on lysine 4. Previous studies have defined the molecular basis for these regulatory relationships, but it remains unclear how they regulate gene expression. To address this question, we investigated a drug resistance phenotype that characterizes defects in this axis in the model eukaryote  Schizosaccharomyces pombe  (fission yeast). The mutations caused resistance to the ribonucleotide reductase inhibitor hydroxyurea (HU) that correlated with a reduced effect of HU on dNTP pools, reduced requirement for the S-phase checkpoint, and blunting of the transcriptional response to HU treatment. Mutations in the C-terminal repeat domain of the RNA polymerase II large subunit Rpb1 led to similar phenotypes. Moreover, all the HU-resistant mutants also exhibited resistance to several azole-class antifungal agents. Our results suggest a novel, shared gene regulatory function of the Rtf1-H2Bub1-H3K4me axis and the Rpb1 C-terminal repeat domain in controlling fungal drug tolerance.","doi":"10.26508/lsa.202302494","authors":"Chen JJ, Moy C, Pagé V, Monnin C, El-Hajj ZW, Avizonis DZ, Reyes-Lamothe R, Tanny JC","authors_abbrev":"Chen JJ et al.","pubmed_publication_date":"Jun 2024","pubmed_entrez_date":"2024-03-21","publication_year":"2024","canto_session_key":"8a4ab759ddf88853","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-23 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26921917","title":"The linear and rotational motions of the fission yeast nucleus are governed by the stochastic dynamics of spatially distributed microtubules.","citation":"J Biomech 2016 May 03;49(7):1034-1041","abstract":"Dynamic nuclei are involved in a wide variety of fundamental biological processes including cell migration, cell division and fertilization. Here, we develop a mathematical model, in combination with live-cell imaging at high temporal resolution, to quantitatively elucidate how the linear and rotational motions of the nucleus are governed by the stochastic dynamics of the microtubule cytoskeleton. Our simulation and experimental results demonstrate that microtubule rescue and catastrophe frequencies are the decisive factors in regulating the nuclear movement. Lower rescue and catastrophe frequencies can lead to significantly larger angular and translational oscillations of the nucleus. In addition, our model also suggests that the stochastic dynamics of individual spatially distributed microtubules works collectively as a restoring force to maintain nuclear centering and hence ensures symmetric cell division, in excellent agreement with direct experimental observations.","doi":"10.1016/j.jbiomech.2016.02.017","authors":"Hui TH, Zheng F, Lin Y, Fu C","authors_abbrev":"Hui TH et al.","pubmed_publication_date":"03 May 2016","pubmed_entrez_date":"2016-02-29","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-03-01 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25786258","title":"Drug synergy drives conserved pathways to increase fission yeast lifespan.","citation":"PLoS One 2015;10(3):e0121877","abstract":"Aging occurs over time with gradual and progressive loss of physiological function. Strategies to reduce the rate of functional loss and mitigate the subsequent onset of deadly age-related diseases are being sought. We demonstrated previously that a combination of rapamycin and myriocin reduces age-related functional loss in the Baker's yeast Saccharomyces cerevisiae and produces a synergistic increase in lifespan. Here we show that the same drug combination also produces a synergistic increase in the lifespan of the fission yeast Schizosaccharomyces pombe and does so by controlling signal transduction pathways conserved across a wide evolutionary time span ranging from yeasts to mammals. Pathways include the target of rapamycin complex 1 (TORC1) protein kinase, the protein kinase A (PKA) and a stress response pathway, which in fission yeasts contains the Sty1 protein kinase, an ortholog of the mammalian p38 MAP kinase, a type of Stress Activated Protein Kinase (SAPK). These results along with previous studies in S. cerevisiae support the premise that the combination of rapamycin and myriocin enhances lifespan by regulating signaling pathways that couple nutrient and environmental conditions to cellular processes that fine-tune growth and stress protection in ways that foster long term survival. The molecular mechanisms for fine-tuning are probably species-specific, but since they are driven by conserved nutrient and stress sensing pathways, the drug combination may enhance survival in other organisms.","doi":"10.1371/journal.pone.0121877","authors":"Huang X, Leggas M, Dickson RC","authors_abbrev":"Huang X et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-19","publication_year":"2015","canto_session_key":"4adee07672de910f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-20 01:16:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26403204","title":"Eisosomes provide membrane reservoirs for rapid expansion of the yeast plasma membrane.","citation":"J Cell Sci 2015 Nov 15;128(22):4057-62","abstract":"Cell surface area rapidly increases during mechanical and hypoosmotic stresses. Such expansion of the plasma membrane requires 'membrane reservoirs' that provide surface area and buffer membrane tension, but the sources of this membrane remain poorly understood. In principle, the flattening of invaginations and buds within the plasma membrane could provide this additional surface area, as recently shown for caveolae in animal cells. Here, we used microfluidics to study the rapid expansion of the yeast plasma membrane in protoplasts, which lack the rigid cell wall. To survive hypoosmotic stress, yeast cell protoplasts required eisosomes, protein-based structures that generate long invaginations at the plasma membrane. Both budding yeast and fission yeast protoplasts lacking eisosomes were unable to expand like wild-type protoplasts during hypoosmotic stress, and subsequently lysed. By performing quantitative fluorescence microscopy on single protoplasts, we also found that eisosomes disassembled as surface area increased. During this process, invaginations generated by eisosomes at the plasma membrane became flattened, as visualized by scanning electron microscopy. We propose that eisosomes serve as tension-dependent membrane reservoirs for expansion of yeast cells in an analogous manner to caveolae in animal cells.","doi":"10.1242/jcs.176867","authors":"Kabeche R, Howard L, Moseley JB","authors_abbrev":"Kabeche R et al.","pubmed_publication_date":"15 Nov 2015","pubmed_entrez_date":"2015-09-26","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-09-27 00:18:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41436280","title":"The LINC complex component Kms1 and CENP-B protein Cbp1 cooperate to enforce faithful homology-directed DNA repair at the nuclear periphery in  S. pombe .","citation":"Genes Dev 2025 Dec 23;","abstract":"While homologous recombination (HR) is often considered to be an error-free DNA repair mechanism, the fidelity of this pathway depends on the cell's ability to engage the ideal template: the replicated sister chromatid. This is particularly challenging during repair of repetitive genome regions for which nonallelic sequences can errantly be used as templates. We developed a model to study spontaneous DNA damage and repair that occurs at repetitive protein-coding genes of the  Schizosaccharomyces pombe  flocculin family. We observed that genes encoding most members of this protein family constitutively reside at the nuclear periphery by virtue of their close proximity to binding sites for the CENP-B-like protein, Cbp1. Tethering via Cbp1 to the nuclear periphery enhances the stability of the flocculin genes against intragenic recombination and restrains intergenic recombination between homoeologous repeat-encoding sequences. The LINC complex component Kms1 also antagonizes both intragenic and intergenic recombination at the flocculin genes as well as microhomology-mediated end joining (MMEJ). Our observations suggest that  S. pombe  leverages nuclear compartmentalization to maintain the stability of repetitive genic regions at the nuclear periphery, while association of DSBs with Kms1-containing LINC complexes enforces stringency to avoid mutagenic end joining and use of the incorrect template during HR.","doi":"10.1101/gad.353167.125","authors":"Laffitte A, Lin D, Tian YJ, Liu N, Lusk CP, Mochrie SGJ, King MC","authors_abbrev":"Laffitte A et al.","pubmed_publication_date":"23 Dec 2025","pubmed_entrez_date":"2025-12-23","publication_year":"2025","canto_session_key":"68a2fcbc5c3342ec","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-25 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15744055","title":"Differential activation of M26-containing meiotic recombination hot spots in Schizosaccharomyces pombe.","citation":"Genetics 2005 May;170(1):95-106","abstract":"Certain genomic loci, termed hot spots, are predisposed to undergo genetic recombination during meiosis at higher levels relative to the rest of the genome. The factors that specify hot-spot potential are not well understood. The M26 hot spot of Schizosaccharomyces pombe is dependent on certain trans activators and a specific nucleotide sequence, which can function as a hot spot in a position- and orientation-independent fashion within ade6. In this report we demonstrate that a linear element (LE) component, Rec10, has a function that is required for activation of some, but not all, M26-containing hot spots and from this we propose that, with respect to hot-spot activity, there are three classes of M26-containing sequences. We demonstrate that the localized sequence context in which the M26 heptamer is embedded is a major factor governing whether or not this Rec10 function is required for full hot-spot activation. Furthermore, we show that the rec10-144 mutant, which is defective in full activation of ade6-M26, but proficient for activation of other M26-containing hot spots, is also defective in the formation of LEs, suggesting an intimate link between higher-order chromatin structure and local influences on hot-spot activation.","authors":"Pryce DW, Lorenz A, Smirnova JB, Loidl J, McFarlane RJ","authors_abbrev":"Pryce DW et al.","pubmed_publication_date":"May 2005","pubmed_entrez_date":"2005-03-04","publication_year":"2005","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36355349","title":"The Cdc42 GAP Rga6 promotes monopolar outgrowth of spores.","citation":"J Cell Biol 2023 Jan 02;222(1)","abstract":"The molecular mechanisms underlying the establishment of the monopolar growth of fission yeast spores have been less characterized. Here, we report that the Cdc42 GTPase-activating protein (GAP) Rga6 is required for promoting monopolar growth during spore germination. The absence of Rga6 increases the number of spores that grow in a bipolar fashion. Rga6 decorates the non-growing cortical region, binds phosphatidylinositol 4,5-bisphosphate, and colocalizes with the phosphatidylinositol 4,5-bisphosphate-binding protein Opy1. Overexpression of Opy1 diminishes the cortical localization of Rga6. The characteristic localization of Rga6 on the cell cortex depends on the C-terminal PBR region of Rga6. Moreover, engineered chimera composed of the Rga6 C-terminal PBR region fused to the GAP domain of Rga3 or Rga4 are sufficient to rescue the spore growth phenotype caused by the absence of Rga6. Hence, our work establishes a paradigm in which the lipid composition of the plasma membrane directs polarized cell growth by specifying the cortical localization of a GAP protein.","doi":"10.1083/jcb.202202064","authors":"Wei W, Zheng B, Zheng S, Wu D, Chu Y, Zhang S, Wang D, Ma X, Liu X, Yao X, Fu C","authors_abbrev":"Wei W et al.","pubmed_publication_date":"02 Jan 2023","pubmed_entrez_date":"2022-11-10","publication_year":"2023","canto_session_key":"f7b2aab28bb24422","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-11-15 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8192897","title":"Glutathione synthetase from the fission yeast. Purification and its unique heteromeric subunit structure.","citation":"Biochem Cell Biol 1993;71(9-10):447-53","abstract":"Glutathione (GSH) synthetase (EC 6.3.2.3) was purified from the fission yeast Schizosaccharomyces pombe L972h- and from the GSH synthetase deficient mutant MN101/pYS41, which harbors a plasmid containing the GSH synthetase gene of the fission yeast. GSH synthetase is expressed at 10 times higher the amount in MN101/pYS41 than in wild-type L972h-. The purified enzyme gave a single band on polyacrylamide gel electrophoresis in the absence of sodium dodecyl sulfate (native PAGE). The molecular weight of this enzyme was determined to be 1.2 x 10(5) by Sepharose CL-6B gel filtration. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE) revealed that this enzyme was composed of two kinds of subunits, A (M(r) = 33 x 10(3)) and B (M(r) = 26 x 10(3)), and existed as a heterotetramer (A2B2). The enzyme purified from the wild-type fission yeast, which did not harbor the plasmid, showed the same electrophoretic mobilities on both native PAGE and SDS-PAGE and similar catalytic properties under standard conditions. This enzyme is most active at 45 degrees C and pH 8.0-8.5 with 20 mM Mg2+ + 10 mM ATP and 50 mM K+. The strict requirement for the monovalent cation is rather specific for the enzymes from yeasts. The presence of sugar components in the enzyme is also observed, similar to that in the rat kidney enzyme.","authors":"Nakagawa CW, Mutoh N, Hayashi Y","authors_abbrev":"Nakagawa CW et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-09-01","publication_year":"1993","canto_session_key":"ad28f7b6025ae5d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-09-22 18:47:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-08 17:16:49","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-09-08"},{"uniquename":"PMID:6757737","title":"Mutagenic studies on the hair dye 2-(2',4'-diaminophenoxy)ethanol with different genetic systems.","citation":"Mutat Res 1982 Dec;102(4):331-46","abstract":"A new hair-dye coupler, 2-(2',4'-diaminophenoxy)ethanol was analyzed for its potential mutagenic activity in different genotoxic assays, namely gene reverse mutations in Salmonella typhimurium, forward mutations in the yeast Schizosaccharomyces pombe, and in the V79 Chinese hamster cell line grown in vitro (HGPRT forward mutation system). Two other genetic test systems, measuring the mitotic gene conversion in Saccharomyces cerevisiae (strain D4) and the unscheduled DNA-repair synthesis in a HeLa cell line grown in vitro, were also used. 2,4-Diaminoanisole, a mutagenic/carcinogenic structurally related hair-dye coupler, and a group of well-known mutagens, namely methyl methanesulfonate, ethyl methanesulfonate, cychlophosphamide, hycanthone and N-nitrosodimethylamine, were used as positive controls. The new aromatic amine, 2-(2',4'-diaminophenoxy)ethanol, was negative in all the assays performed, under the same treatment conditions as in the case of all the positive controls.","authors":"Loprieno N, Barale R, Mariani L, Zaccaro L","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"Dec 1982","pubmed_entrez_date":"1982-12-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9520266","title":"Isolation and characterization of hrp1+, a new member of the SNF2/SWI2 gene family from the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1998 Feb;257(3):319-29","abstract":"The SNF2/SWI2 ATPase/helicase family comprises proteins from a variety of species, which serve a number of functions, such as transcriptional regulation, maintenance of chromosome stability during mitosis, and various types of DNA repair. Several proteins with unknown functions are also included in this family. The number of genes that belong to this family is rapidly expanding, which makes it easier to analyze the common biological functions of the family members. This study was designed to clone the SNF2/SWI2 helicase-related genes from the fission yeast Schizosaccharomyces pombe in the hope that this would help to elucidate the common functions of the proteins in this family. The hrp1+ (helicase-related gene from S. pombe) gene was initially cloned by PCR amplification using degenerate primers based on conserved SNF2 motifs within the ERCC6 gene, which encodes a protein involved in DNA excision repair. The hrp1+ ORF codes for an 1373-amino acid polypeptide with a molecular mass of 159 kDa. Like other SNF2/SWI2 family proteins, the deduced amino acid sequence of Hrp1 contains DNA-dependent ATPase/7 helicase domains, as well as a chromodomain and a DNA-binding domain. This configuration is similar to that of mCHD1 (mouse chromo-ATPase/helicase-DNA-binding protein 1), suggesting that Hrp1 is a S. pombe homolog of mCHD1, which is thought to function in altering the chromatin structure to facilitate gene expression. Northern blot analysis showed that the hrp1+ gene produces a 4.6-kb transcript, which reaches its maximal level just before the cells enter the exponential growth phase, and then decreases gradually. DNA-damaging agents, such as MMS, MNNG and UV, decrease the rate of transcription of hrp1+. Deletion of the hrp1+ gene resulted in accelerated cell growth. On the other hand, overexpression of Hrp1 caused a reduction in growth rate. These results indicate that hrp1+ may act as a negative regulator of cellular growth.","authors":"Jin YH, Yoo EJ, Jang YK, Kim SH, Kim MJ, Shim YS, Lee JS, Choi IS, Seong RH, Hong SH, Park SD","authors_abbrev":"Jin YH et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-03-31","publication_year":"1998","canto_session_key":"d2197a514b8dbeb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-04-29 20:57:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 20:54:49","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-29"},{"uniquename":"PMID:16791824","title":"Proteome analysis of Schizosaccharomyces pombe by two-dimensional gel electrophoresis and mass spectrometry.","citation":"Proteomics 2006 Jul;6(14):4115-29","abstract":"The fission yeast Schizosaccharomyces pombe (S. pombe) is a unicellular eukaryote and contains many genes and regulatory mechanisms that are close to those of mammals. In this study, we performed a global proteomic analysis of the fission yeast S. pombe wild type h(-S) L 972 proteome. More than 1,500 protein spots were visualized on silver stained 2-D gels in the 3-10 pI range with a high resolution and high reproducibility. Protein identification was carried out by MALDI-TOF-MS and/or nanoLC-MS/MS. Advantage of the complementarity of these two MS approaches was used to enhance the identification quality. So far, 364 proteins (representing 157 different proteins) have been identified. We report here the identification of 117 new proteins on our 2-D reference map of this yeast compared to the first reference map. Of these identified proteins, 40.1% were involved in metabolism. The present work provides a very useful tool for all studies relying on S. pombe as a model organism and is a considerable complement to the first reference map of S. pombe published recently by Sun and coworkers (Sun, N., Jang, J., Lee, S., Kim, S. et al.., Proteomics 2005, 5, 1574-1579).","authors":"Hwang KH, Carapito C, Böhmer S, Leize E, Van Dorsselaer A, Bernhardt R","authors_abbrev":"Hwang KH et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-06-23","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000036","title":"Manual annotations that require more than one source of functional data to support the assignment of the associated GO term","abstract":"The Gene Ontology Consortium uses the IC (Inferred by Curator) evidence code when an annotation cannot be supported by any direct evidence, but can be inferred by GO annotations that have been annotated to the same gene/gene product identifier in conjunction with the curator's knowledge of biology (supporting GO annotations must not be IC-evidenced). In many cases an IC-evidenced annotation simply applies the same reference that was used in the supporting GO annotation.  The use of IC evidence code in an annotation with reference GO_REF:0000036 signifies a curator inferred the GO term based on evidence from multiple sources of evidence/GO annotations. The 'with/from' field in these annotations will therefore supply more than one GO identifier, obtained from the set of supporting GO annotations assigned to the same gene/gene product identifier which cite publicly-available references.","authors":"GO Annotation working group","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F5.07c","SPBC1347.01c","SPAC19G12.08","SPBC30D10.08","SPAC2E1P5.01c","SPAC607.09c","SPAPB1A10.15","SPBC30B4.06c","SPBC660.10","SPBC16D10.04c","SPAC688.10","SPAC23D3.10c","SPAPB17E12.10c","SPBC12D12.09","SPBC354.09c","SPBC21C3.03","SPMTR.01","SPBC8D2.12c","SPBC1306.01c","SPBC4C3.12","SPAC27E2.10c","SPAC1805.09c","SPAC31G5.02","SPAC20H4.11c","SPBP19A11.01","SPAC29B12.05c","SPAC1851.02","SPAC1002.09c","SPAC56E4.04c","SPBC16A3.10","SPAC23A1.05","SPBC11C11.05","SPAC31A2.06","SPBC1773.12","SPAC824.02","SPAC26H5.05","SPAC23C11.01","SPAC6G9.08","SPAC30D11.11","SPBC119.09c","SPBC1709.09","SPBP8B7.13","SPBC947.14c","SPAC5D6.12","SPAC31G5.14","SPAC22A12.10","SPBC2D10.15c","SPAC227.09","SPBC1773.16c","SPAC20G8.01","SPAC25B8.01","SPAC13G6.06c","SPAC16A10.01"],"gene_count":53,"ltp_gene_count":0},{"uniquename":"PMID:29423851","title":"Estimation of GFP-Nucleoporin Amount Based on Fluorescence Microscopy.","citation":"Methods Mol Biol 2018;1721:105-115","abstract":"Cellular structures and biomolecular complexes are not simply assemblies of proteins, but are organized with defined numbers of protein molecules in precise locations. Thus, evaluating the spatial localization and numbers of protein molecules is of fundamental importance in understanding cellular structures and functions. The amounts of proteins of interest have conventionally been determined by biochemical methods. However, biochemical measurements based on the population average have limitations: it is sometimes difficult to determine the amounts of insoluble proteins or low expression proteins localized in small portions of the cell. In contrast, microphotometric measurements using fluorescence microscopes enable us to detect the amounts of such proteins in situ in a particular subcellular region. Here, we describe a method to measure the amounts of fluorescently tagged proteins by fluorescence microscopy, and present an example of an application to nuclear pore proteins in the fission yeast Schizosaccharomyces pombe.","doi":"10.1007/978-1-4939-7546-4_10","authors":"Asakawa H, Hiraoka Y, Haraguchi T","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30679249","title":"Identification of Suppressor of Clathrin Deficiency-1 ( SCD1 ) and Its Connection to Clathrin-Mediated Endocytosis in  Saccharomyces cerevisiae .","citation":"G3 (Bethesda) 2019 Mar 07;9(3):867-877","abstract":"Clathrin is a major coat protein involved in vesicle formation during endocytosis and transport in the endosomal/trans Golgi system. Clathrin is required for normal growth of yeast  (Saccharomyces cerevisiae)  and in some genetic backgrounds deletion of the clathrin heavy chain gene ( CHC1 ) is lethal. Our lab defined a locus referred to as \"   s   uppressor of   c   lathrin   d   eficiency\" ( SCD1 ). In the presence of the  scd1-v  allele (\"v\" - viable), yeast cells lacking clathrin heavy chain survive but grow slowly, are morphologically abnormal and have many membrane trafficking defects. In the presence of  scd1-i  (\"i\"- inviable),  chc1∆  causes lethality. As a strategy to identify  SCD1 , we used pooled linkage analysis and whole genome sequencing. Here, we report that  PAL2  ( YHR097C ) is the  SCD1  locus.  pal2∆  is synthetic lethal with  chc1∆ ; whereas a deletion of its paralog,  PAL1 , is not synthetic lethal with clathrin deficiency. Like Pal1, Pal2 has two NPF motifs that are potential binding sites for EH domain proteins such as the early endocytic factor Ede1, and Pal2 associates with Ede1 Also, GFP-tagged Pal2p localizes to cortical patches containing other immobile phase endocytic coat factors. Overall, our data show that  PAL2  is the  SCD1  locus and the Pal2 protein has characteristics of an early factor involved in clathrin-mediated endocytosis.","doi":"10.1534/g3.118.200782","authors":"Moorthy BT, Sharma A, Boettner DR, Wilson TE, Lemmon SK","authors_abbrev":"Moorthy BT et al.","pubmed_publication_date":"07 Mar 2019","pubmed_entrez_date":"2019-01-26","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC6B1.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1897317","title":"Isolation and characterization of Schizosaccharomyces pombe mutants lacking aminopeptidase activity.","citation":"Yeast 1991 Jul;7(5):525-31","abstract":"A mutant strain of the fission yeast Schizosaccharomyces pombe defective in aminopeptidase I was isolated by screening for lack of activity against the chromogenic substrate lysine-beta-naphthylamide in isolated colonies. Tetrad dissection of sporulated diploids heterozygous for the wild-type and mutant allele resulted in a 2:2 segregation of mutant and wild-type phenotype indicating a single chromosomal gene mutation. Gene dosage experiments indicated that the mutation might reside in the structural gene of aminopeptidase I. No vital consequences of aminopeptidase I deficiency on cell life and sporulation could be detected. However, the enzyme seems to be involved in protein degradation under conditions of nutrient deprivation.","authors":"Arbesu MJ, Gascon S, Suarez-Rendueles P","authors_abbrev":"Arbesu MJ et al.","pubmed_publication_date":"Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23288360","title":"A popular engagement at the ends.","citation":"Nat Struct Mol Biol 2013 Jan;20(1):10-2","abstract":"Three recent studies converged on a specific protein-protein interface between TPP1 and telomerase as being crucial for the regulation of both telomerase recruitment and processivity in mammalian cells. An equivalent interaction appears to exist in budding yeast, making this a nearly universal means of telomerase regulation.","doi":"10.1038/nsmb.2483","authors":"Lue NF, Yu EY, Lei M","authors_abbrev":"Lue NF et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2013-01-05","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26787556","title":"Crystal structure and SUMO binding of Slx1-Slx4 complex.","citation":"Sci Rep 2016 Jan 20;6:19331","abstract":"The SLX1-SLX4 complex is a structure-specific endonuclease that cleaves branched DNA structures and plays significant roles in DNA recombination and repair in eukaryotic cells. The heterodimeric interaction between SLX1 and SLX4 is essential for the endonuclease activity of SLX1. Here, we present the crystal structure of Slx1 C-terminal zinc finger domain in complex with the C-terminal helix-turn-helix domain of Slx4 from Schizosaccharomyces pombe at 2.0 Å resolution. The structure reveals a conserved binding mechanism underling the Slx1-Slx4 interaction. Structural and sequence analyses indicate Slx1 C-terminal domain is actually an atypical C4HC3-type RING finger which normally possesses E3 ubiquitin ligase activity, but here is absolutely required for Slx1 interaction with Slx4. Furthermore, we found the C-terminal tail of S. pombe Slx1 contains a SUMO-interacting motif and can recognize Pmt3 (S. pombe SUMO), suggesting that Slx1-Slx4 complex could be recruited by SUMOylated protein targets to take part in replication associated DNA repair processes.","doi":"10.1038/srep19331","authors":"Lian FM, Xie S, Qian C","authors_abbrev":"Lian FM et al.","pubmed_publication_date":"20 Jan 2016","pubmed_entrez_date":"2016-01-21","publication_year":"2016","canto_session_key":"b37a05627466c42b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-05 15:56:07","canto_approved_date":"2022-02-07 16:50:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-05 15:55:58","canto_added_date":"2016-01-22 01:15:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.06","SPAC688.06c","SPAP27G11.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-04-05","pdb_entries":[{"pdb_id":"4zdt","gene_chains":[{"gene_uniquename":"SPAC688.06c","chain":"B/D","position":"352-419"},{"gene_uniquename":"SPAP27G11.15","chain":"A/C","position":"176-247"}],"title":"Crystal structure of the RING finger domain of Slx1 in complex with the C-terminal domain of Slx4","entry_authors":"Lian FM,Xie S,Qian CM","entry_authors_abbrev":"Lian FM et al.","reference_uniquename":"PMID:26787556","experimental_method":"X-ray","resolution":"2.0"}]},{"uniquename":"PMID:22209903","title":"Going in the right direction: mating-type switching of Schizosaccharomyces pombe is controlled by judicious expression of two different swi2 transcripts.","citation":"Genetics 2012 Mar;190(3):977-87","abstract":"Schizosaccharomyces pombe, the fission yeast, cells alternate between P- and M-mating type, controlled by the alternate alleles of the mating-type locus (mat1). The mat1 switching occurs by replacing mat1 with a copy derived from a silenced \"donor locus,\" mat2P or mat3M. The mechanism of donor choice ensuring that switching occurs primarily and productively to the opposite type, called directionality, is largely unknown. Here we identified the mat1-Mc gene, a mammalian sex-determination gene (SRY) homolog, as the primary gene that dictates directionality in M cells. A previously unrecognized, shorter swi2 mRNA, a truncated form of the swi2, was identified, and its expression requires the mat1-Mc function. We also found that the abp1 gene (human CENPB homolog) controls directionality through swi2 regulation. In addition, we implicated a cis-acting DNA sequence in mat2 utilization. Overall, we showed that switching directionality is controlled by judicious expression of two swi2 transcripts through a cell-type-regulated dual promoter. In this respect, this regulation mechanism resembles that of the Drosophila sex-determination Slx gene.","doi":"10.1534/genetics.111.137109","authors":"Yu C, Bonaduce MJ, Klar AJ","authors_abbrev":"Yu C et al.","pubmed_publication_date":"Mar 2012","pubmed_entrez_date":"2012-01-03","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9658169","title":"Identification of novel temperature-sensitive lethal alleles in essential beta-tubulin and nonessential alpha 2-tubulin genes as fission yeast polarity mutants.","citation":"Mol Biol Cell 1998 Jul;9(7):1757-71","abstract":"We have screened for temperature-sensitive (ts) fission yeast mutants with altered polarity (alp1-15). Genetic analysis indicates that alp2 is allelic to atb2 (one of two alpha-tubulin genes) and alp12 to nda3 (the single beta-tubulin gene). atb2(+) is nonessential, and the ts atb2 mutations we have isolated are dominant as expected. We sequenced two alleles of ts atb2 and one allele of ts nda3. In the ts atb2 mutants, the mutated residues (G246D and C356Y) are found at the longitudinal interface between alpha/beta-heterodimers, whereas in ts nda3 the mutated residue (Y422H) is situated in the domain located on the outer surface of the microtubule. The ts nda3 mutant is highly sensitive to altered gene dosage of atb2(+); overexpression of atb2(+) lowers the restrictive temperature, and, conversely, deletion rescues ts. Phenotypic analysis shows that contrary to undergoing mitotic arrest with high viability via the spindle assembly checkpoint as expected, ts nda3 mutants execute cytokinesis and septation and lose viability. Therefore, it appears that the ts nda3 mutant becomes temperature lethal because of irreversible progression through the cell cycle in the absence of activating the spindle assembly checkpoint pathway.","authors":"Radcliffe P, Hirata D, Childs D, Vardy L, Toda T","authors_abbrev":"Radcliffe P et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-07-11","publication_year":"1998","canto_session_key":"c4669f01934c07d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-07 17:11:26","canto_approved_date":"2026-04-05 16:44:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-13 07:23:27","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":55,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13D6.05","SPCC895.07","SPBP23A10.08","SPBC26H8.07c","SPCC70.07c","SPBC800.05c","SPAC890.02c","SPBC428.20c","SPAC23H4.12","SPBC16A3.15c","SPBC365.15","SPCC1223.06","SPBC11C11.04c"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2016-10-07"},{"uniquename":"PMID:11676915","title":"S. pombe cdc11p, together with sid4p, provides an anchor for septation initiation network proteins on the spindle pole body.","citation":"Curr Biol 2001 Oct 16;11(20):1559-68","abstract":"The signal for the onset of septum formation in the fission yeast Schizosaccharomyces pombe is transduced by the septation initiation network (SIN). Many of the components of the SIN are located on the spindle pole body during mitosis, from where it is presumed that the signal for septum formation is delivered. Cdc11 mutants are defective in SIN signaling, but the role of cdc11 in the pathway has remained enigmatic.\nWe have cloned the cdc11 gene by a combination of chromosome walking and transfection of cosmids into a cdc11 mutant. Cdc11p most closely resembles Saccharomyces cerevisiae Nud1p and is essential for septum formation. Cdc11p is a phosphoprotein, which becomes hyperphosphorylated during anaphase. It localizes to the spindle pole body at all stages of the cell cycle, in a sid4p-dependent manner, and cdc11p is required for the localization of all the known SIN components, except sid4p, to the SPB. Cdc11p and sid4p can be coimmunoprecipitated from cell extracts. Finally, like its S. cerevisiae ortholog Nud1p, cdc11p is involved in the proper organization of astral microtubules during mitosis.\nWe propose that cdc11p acts as a bridge between sid4p and the other SIN proteins, mediating their association with the spindle pole body.","authors":"Krapp A, Schmidt S, Cano E, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"16 Oct 2001","pubmed_entrez_date":"2001-10-26","publication_year":"2001","canto_session_key":"2a09c66cd3b7c486","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-29 08:56:50","canto_approved_date":"2026-02-19 16:19:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-12-29 08:51:24","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPAC23C11.16","SPBC428.13c","SPBC244.01c","SPAC1565.06c","SPAC222.10c","SPCC1739.11c","SPAC9G1.09","SPAC24B11.11c"],"gene_count":9,"ltp_gene_count":3,"approved_date":"2020-12-29"},{"uniquename":"PMID:9285594","title":"DNA renaturation activity of the SMC complex implicated in chromosome condensation.","citation":"Nature 1997 Aug 21;388(6644):798-801","abstract":"Chromosome condensation occurs in mitosis before the separation of sister chromatids, and requires DNA topoisomerase II and a group of proteins called SMCs. The resulting condensed chromosomes in metaphase have a complex hierarchical structure. SMCs, the components of condensed chromosomes, are also required for the separation of sister chromatids and gene dosage compensation, and are found in a range of organisms from yeasts to mammals. However, the mechanisms by which the SMCs contribute to chromosome condensation are unknown. We have studied chromosomes in fission-yeast SMC mutants cut3-477 and cut14-208, which remain largely non-condensed during mitosis at the restrictive temperature (36 degrees C). To test their role in DNA condensation, we isolated the proteins Cut3 and Cut14 as an oligomeric complex, and tested their interactions with isolated DNA. The complex efficiently promoted the DNA renaturation reactions (the winding up of single-strand DNAs into double helical DNA) as much as approximately 70-fold more efficiently than RecA, which is a bacterial protein with similar activity. The activity of the mutant complex was heat sensitive. As DNA winding by renaturation is a potential cause of supercoiling, the SMC complex may be implicated in promoting the higher-order DNA coiling found in condensed chromosomes.","authors":"Sutani T, Yanagida M","authors_abbrev":"Sutani T et al.","pubmed_publication_date":"21 Aug 1997","pubmed_entrez_date":"1997-08-21","publication_year":"1997","canto_session_key":"b365bd06b75ce0d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-11-25 13:01:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-01 15:36:24","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.06c","SPBC29A10.04","SPBC146.03c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2016-06-01"},{"uniquename":"PMID:21354177","title":"Transcriptional and cellular responses to defective mitochondrial proteolysis in fission yeast.","citation":"J Mol Biol 2011 Apr 29;408(2):222-37","abstract":"Lon and m-AAA are the principal, regulated proteases required for protein maturation and turnover in the mitochondrial matrix of diverse species. To understand their roles in fission yeast (Schizosaccharomyces pombe) mitochondria, we generated deletion strains lacking Lon and m-AAA, individually (Δlon1 and Δm-AAA) or together, Δlon1Δm-AAA (Δ/Δ). All three strains were viable but incapable of respiratory growth on a non-fermentable carbon source due to mitochondrial dysfunction. Confocal and electron microscopy revealed a decrease in membrane potential and ultrastructural changes in Δlon1, Δm-AAA and Δ/Δ mitochondria, consistent with a respiratory defect and aggregation of proteins in the mitochondrial matrix. To understand the global adaptations required for cell survival in the absence of Lon and m-AAA proteases, we compared genome-wide gene expression signatures of the deletion strains with the isogenic wild-type strain. Deletion of lon1 caused a distinctive transcriptional footprint of just 12 differentially expressed genes, 9 of which were up-regulated genes located on the proximal mitochondrial genome (mitochondrial DNA). In contrast, m-AAA deletion caused a much larger transcriptional response involving 268 almost exclusively nuclear genes. Genes ameliorating stress and iron assimilation were up-regulated, while diverse mitochondrial genes and other metabolic enzymes were down-regulated. The connection with iron dysregulation was further explored using biochemical, chemical and cellular assays. Although Δm-AAA and Δ/Δ contained more cellular iron than the wild-type strain, their transcriptomes strongly resembled a signature normally evoked by iron insufficiency or disrupted assembly of iron-sulfur clusters in mitochondria. Based on these findings, we posit that excess iron accumulation could contribute to the pathology of human neurodegenerative disorders arising from defects in m-AAA function.","doi":"10.1016/j.jmb.2011.02.044","authors":"Guha S, López-Maury L, Shaw M, Bähler J, Norbury CJ, Agashe VR","authors_abbrev":"Guha S et al.","pubmed_publication_date":"29 Apr 2011","pubmed_entrez_date":"2011-03-01","publication_year":"2011","canto_session_key":"226e465f7a422d15","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-06-20 08:39:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-05-16 08:39:12","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":40,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC543.09","SPAC22F3.06c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-05-16"},{"uniquename":"EMBL:AB084834","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.22"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU012909","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23091597","title":"Site directed mutagenesis of Schizosaccharomyces pombe glutathione synthetase produces an enzyme with homoglutathione synthetase activity.","citation":"PLoS One 2012;7(10):e46580","abstract":"Three different His-tagged, mutant forms of the fission yeast glutathione synthetase (GSH2) were derived by site-directed mutagenesis. The mutant and wild-type enzymes were expressed in E. coli DH5α and affinity purified in a two-step procedure. Analysis of enzyme activity showed that it was possible to shift the substrate specificity of GSH2 from Gly (k(m) 0,19; wild-type) to β-Ala or Ser. One mutation (substitution of Ile471, Cy472 to Met and Val and Ala 485 and Thr486 to Leu and Pro) increased the affinity of GSH2 for β-Ala (k(m) 0,07) and lowered the affinity for Gly (k(m) 0,83), which is a characteristic of the enzyme homoglutathione synthetase found in plants. Substitution of Ala485 and Thr486 to Leu and Pro only, increased instead the affinity of GSH2 for Ser (k(m) 0,23) as a substrate, while affinity to Gly was preserved (k(m) 0,12). This provides a new biosynthetic pathway for hydroxymethyl glutathione, which is known to be synthesized from glutathione and Ser in a reaction catalysed by carboxypeptidase Y. The reported findings provide further insight into how specific amino acids positioned in the GSH2 active site facilitate the recognition of different amino acid substrates, furthermore they support the evolutionary theory that homoglutathione synthetase evolved from glutathione synthetase by a single gene duplication event.","doi":"10.1371/journal.pone.0046580","authors":"Dworeck T, Zimmermann M","authors_abbrev":"Dworeck T et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-10-24","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17643314","title":"Structures of S. pombe phosphofructokinase in the F6P-bound and ATP-bound states.","citation":"J Struct Biol 2007 Sep;159(3):498-506","abstract":"Phosphofructokinase (Pfk1; EC 2.7.1.11) is the third enzyme of the glycolytic pathway catalyzing the formation of fructose-1,6-bisphosphate from fructose-6-phosphate (F6P) and ATP. Schizosaccharomyces pombe Pfk1 is a homo-octameric enzyme of 800 kDa molecular weight, distinct from its yeast counterparts which are mostly hetero-octameric enzymes composed of two different subunits. Having an \"open\" conformation and a tendency to aggregate into higher oligomeric structures, the S. pombe enzyme shows similarities to the mammalian muscle Pfk1. It has been proposed that due to the distinct N-terminal region of the S. pombe subunit, the oligomeric organization of subunits in this enzyme is different from other yeast phosphofructokinases. Electron microscopy studies were carried out to reveal the quaternary structure of the homo-octameric Pfk1 from S. pombe in the F6P-bound and in the ATP-bound state. Random conical tilt data sets have been collected from deep stain preparations of the enzyme in both states. The 0 degrees tilt images have been separated into different classes and a 3D reconstruction has been calculated for each class from the high tilt images. Our results confirm the presence of a variety of views of the particle, most of which can be interpreted as views of the molecule rotating around its long axis. Despite the biochemical differences, the structure of phosphofructokinase from S. pombe in the presence of either F6P or ATP is similar to the hetero-octameric structure of phosphofructokinase from Saccharomyces cerevisiae. The molecule can be described as composed of two subdomains, connected by two well-defined densities. We have been able to establish a correlation between the kinetic behavior and the structural conformation of Pfk1.","authors":"Benjamin S, Radermacher M, Bär J, Edelmann A, Ruiz T","authors_abbrev":"Benjamin S et al.","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-07-24","publication_year":"2007","canto_session_key":"02a6adf951874e01","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-30 23:57:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 23:57:14","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16H5.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-30"},{"uniquename":"PMID:17211518","title":"Characterisation of the nascent polypeptide-associated complex in fission yeast.","citation":"Mol Biol Rep 2007 Dec;34(4):275-81","abstract":"The nascent polypeptide-associated complex (NAC) is an abundant and phylogenetically conserved protein complex. It is composed of two subunits and interacts with nascent polypeptide chains emerging from the ribosome. It has been proposed to protect the nascent chains from premature interaction with other cell proteins, but has also been found to associate with DNA junctions, and to be involved in other processes including transcription regulation and mitochondrial protein import.Here, we characterize NAC in fission yeast. We find that NAC is associated with ribosomes, while a significant fraction remains in a free form. The NAC alpha subunit contains a ubiquitin-associated (UBA) domain, which is found in several proteins involved in the ubiquitin-proteasome pathway for protein degradation. However, NAC does not associate with ubiquitin chains and mutants lacking NAC did not exhibit any obvious defects in protein degradation. Accordingly, we find that the NAC UBA domain belongs to an ancient and distinct subgroup of the UBA family. In contrast to the situation with budding yeast, fission yeast cells devoid of NAC were not temperature sensitive. However, they displayed resistance to the amino acid analogue canavanine, in accordance with the idea that NAC is involved in protein quality control.","authors":"Andersen KM, Semple CA, Hartmann-Petersen R","authors_abbrev":"Andersen KM et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-01-11","publication_year":"2007","canto_session_key":"6ffedac206257aa0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-26 19:37:11","canto_approved_date":"2025-09-03 15:48:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-26 19:30:31","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.12","SPBC25H2.05","SPAC4F10.14c","SPBC337.08c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2020-11-26"},{"uniquename":"PMID:39880258","title":"Determination of enzyme kinetic parameters of fast-acting Schizosaccharomyces pombe Ulp1 catalytic domain using Forster resonance energy transfer (FRET) assay.","citation":"Int J Biol Macromol 2025 Jan 27;:140312","abstract":"The SUMO fusion technology has immensely contributed to the soluble production of therapeutics and other recombinant proteins in E. coli. The structure-based functionality of SUMO protease has remained the primary determinant for choosing SUMO as a solubility enhancer tag. This study details the quantification of kinetic parameters of commercially relevant S. pombe Ulp1 catalytic domain by employing a Forster resonance energy transfer (FRET) based assay. The energy transfer between the fluorophores allowed to elucidate the kinetic parameters precisely. For the FRET assay, the ECFP-SpSUMO-EYFP construct was successfully cloned in the pET28a vector. The fusion protein was efficaciously expressed and purified near homogeneity. The assay employed provided a real-time investigation of SpUlp1 catalysis. The enzyme turnover number (k cat ) was computed as 9.08 s -1 . The Michaelis-Menten constant, K M  was determined as 0.65 × 10 1  μM with a maximum velocity (V max ) of 0.045 μM/s. The substrate specificity ratio, k cat /K M  was calculated to be 1.39 × 10 6  M -1  s -1 . Using the FRET assay approach, the fast-acting nature of the SpUlp1 was analyzed in real-time at even 10 3  times higher molar substrate concentration. Thus, the kinetics of commercially relevant SpUlp1 was successfully demonstrated along with its large-scale production at 50 L bioreactor, where the maximum product concentration was 4.8 g/L. Additionally, the S. pombe SUMO used in the current study could potentially replace the S. cerevisiae SUMO as a solubility enhancer fusion tag.","doi":"10.1016/j.ijbiomac.2025.140312","authors":"Babbal SM, Khasa YP","authors_abbrev":"Babbal SM et al.","pubmed_publication_date":"27 Jan 2025","pubmed_entrez_date":"2025-01-29","publication_year":"2025","canto_session_key":"95faf941a4dcefab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-03-01 08:20:11","canto_approved_date":"2025-03-01 08:20:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-01 08:19:13","canto_added_date":"2025-01-31 00:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.06","SPBC19G7.09"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2025-03-01"},{"uniquename":"PMID:27371603","title":"Fixed-Cell Imaging of Schizosaccharomyces pombe.","citation":"Cold Spring Harb Protoc 2016 Jul 01;2016(7)","abstract":"The acknowledged genetic malleability of fission yeast has been matched by impressive cytology to drive major advances in our understanding of basic molecular cell biological processes. In many of the more recent studies, traditional approaches of fixation followed by processing to accommodate classical staining procedures have been superseded by live-cell imaging approaches that monitor the distribution of fusion proteins between a molecule of interest and a fluorescent protein. Although such live-cell imaging is uniquely informative for many questions, fixed-cell imaging remains the better option for others and is an important-sometimes critical-complement to the analysis of fluorescent fusion proteins by live-cell imaging. Here, we discuss the merits of fixed- and live-cell imaging as well as specific issues for fluorescence microscopy imaging of fission yeast.","doi":"10.1101/pdb.top079830","authors":"Hagan IM, Bagley S","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"01 Jul 2016","pubmed_entrez_date":"2016-07-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-07-04 00:15:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3887858","title":"Recovery, repair, and mutagenesis in Schizosaccharomyces pombe.","citation":"Adv Genet 1985;23:1-72","abstract":"","authors":"Phipps J, Nasim A, Miller DR","authors_abbrev":"Phipps J et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9211944","title":"Protein phosphatase 2C acts independently of stress-activated kinase cascade to regulate the stress response in fission yeast.","citation":"J Biol Chem 1997 Jul 11;272(28):17873-9","abstract":"Stress-activated signal transduction pathways, which are largely conserved among a broad spectrum of eukaryotic species, have a crucial role in the survival of many forms of stress. It is therefore important to discover how these pathways are both positively and negatively regulated. Recent genetic studies have implicated protein phosphatase 2C (PP2C) as a novel negative regulator of stress response pathways in both budding and fission yeasts. Moreover, it was hypothesized that PP2C dephosphorylates one or more components of protein kinase cascades that are at the core of stress-activated signal transduction pathways. Herein we present genetic and biochemical studies of the fission yeast Schizosaccharomyces pombe that disprove this hypothesis and indicate that PP2C instead negatively regulates a downstream element of the pathway. First, high expression of PP2C produces phenotypes that are inconsistent with negative regulation of the Wik1-Wis1-Spc1 stress-activated kinase cascade. Second, high expression of PP2C leads to sustained activating tyrosine phosphorylation of Spc1. Third, Spc1-dependent phosphorylation of Atf1, a transcription factor substrate of Spc1, is unaffected by high expression of PP2C. Fourth, high expression of PP2C suppresses Atf1-dependent transcription of a stress-response gene. These studies strongly suggest that PP2C acts downstream of Spc1 kinase in the stress-activated signal transduction pathway.","authors":"Gaits F, Shiozaki K, Russell P","authors_abbrev":"Gaits F et al.","pubmed_publication_date":"11 Jul 1997","pubmed_entrez_date":"1997-07-11","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4F11.02","SPAC2G11.07c","SPAC26F1.10c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:18692466","title":"A network of nuclear envelope membrane proteins linking centromeres to microtubules.","citation":"Cell 2008 Aug 08;134(3):427-38","abstract":"In the fission yeast S. pombe, nuclei are actively positioned at the cell center by microtubules. Here, we show that cytoplasmic microtubules are mechanically coupled to the nuclear heterochromatin through proteins embedded in the nuclear envelope. This includes an integral outer nuclear membrane protein of the KASH family (Kms2) and two integral inner nuclear membrane proteins, the SUN-domain protein Sad1 and the previously uncharacterized protein Ima1. Ima1 specifically binds to heterochromatic regions and promotes the tethering of centromeric DNA to the SUN-KASH complex. In the absence of Ima1, or in cells harboring mutations in the centromeric Ndc80 complex, inefficient coupling of centromeric heterochromatin to Sad1 leads to striking defects in the ability of the nucleus to tolerate microtubule-dependent forces, leading to changes in nuclear shape, loss of spindle pole body components from the nuclear envelope, and partial dissociation of SUN-KASH complexes. This work highlights a framework for communication between cytoplasmic microtubules and chromatin.","doi":"10.1016/j.cell.2008.06.022","authors":"King MC, Drivas TG, Blobel G","authors_abbrev":"King MC et al.","pubmed_publication_date":"08 Aug 2008","pubmed_entrez_date":"2008-08-12","publication_year":"2008","canto_session_key":"2bb2b3dd0c45b3a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-12-01 12:32:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-01 12:31:14","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC737.03c","SPAC18G6.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-12-01"},{"uniquename":"PMID:12034771","title":"Roles of fission yeast tea1p in the localization of polarity factors and in organizing the microtubular cytoskeleton.","citation":"J Cell Biol 2002 May 27;157(5):783-93","abstract":"The cylindrical shape of the fission yeast cell is generated by linear polarized growth from its cell ends. Using immunofluorescence and live imaging microscopy, we have investigated the roles of the cell end marker tea1p in generating linear polarized growth. We found that tea1p is primarily transported on plus ends of microtubules from the vicinity of the nucleus to the cell ends, and that its movement near the nucleus is independent of the kinesin tea2p. Deletion analysis identified a coiled-coil domain in tea1p essential for its retention at cell ends, and demonstrated that tea1p exerts different functions dependent on its location. On the tips of microtubules, tea1p prevents the curling of microtubules around the cell ends, whereas it is required for maintaining linear cell growth and for retention of polarity factors such as the Dyrk kinase pom1p, the CLIP170-like tip1p, and tea2p at the cell ends. We propose that tea1p has roles in organizing the microtubule cytoskeleton on the tips of microtubules, and in the retention of factors at the cell ends necessary for the cell to grow in a straight line.","authors":"Behrens R, Nurse P","authors_abbrev":"Behrens R et al.","pubmed_publication_date":"27 May 2002","pubmed_entrez_date":"2002-05-30","publication_year":"2002","canto_session_key":"f2b0ffda72370b22","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-03-26 10:13:53","canto_approved_date":"2025-07-22 15:44:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-17 17:18:48","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":23,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.03c","SPCC1223.06","SPAC3C7.12","SPBC1604.20c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2018-03-26"},{"uniquename":"PMID:21804323","title":"[Cell surface protein Ecm33 is involved in negative feedback regulation of MAP kinase signalling and development of the in vivo real-time monitoring of MAP kinase signalling].","citation":"Yakugaku Zasshi 2011;131(8):1195-200","abstract":"The mitogen-activated protein kinase (MAPK) pathways are signal transduction mechanisms that regulate many cellular processes in eukaryotic organisms, from yeasts to mammals. Multiple MAPKs regulate eukaryotic gene expression in response to various extracellular stimuli through phosphorylation of transcription factors. We have been studying the Pmk1 MAPK, a homologue of the mammalian ERK/MAPK in fission yeast. The Pmk1 MAPK regulates cell integrity and cell morphology. We have previously demonstrated that Atf1, a transcription factor downstream of the stress-activated MAPK pathway, serves also as a target of the Pmk1 MAPK signaling in fission yeast. Here, we identified ecm33⁺ gene, encoding a glycosyl-phosphatidylinositol (GPI)-anchored cell surface protein as a transcriptional target of Pmk1 and Atf1. The gene expression of ecm33⁺ is regulated by two transcription factors Atf1 and Mbx1. We also developed an in vivo real-time monitoring system of Atf1 or Mbx1 transcriptional activity, which enables to monitor the activation of the Pmk1 MAPK pathway by various stimuli. Finally, we demonstrated that Ecm33 is involved in the negative regulation of the Pmk1 MAPK signaling through the control of Ca²⁺ homeostasis. The ecm33 deleted cells displayed Ca²⁺ sensitivity and increased phosphorylation levels of Pmk1 MAPK. In addition, the Ecm33 overproducing cells displayed phenotypes closely similar to those of the pmk1 knockout cell. Collectively, Ecm33 plays a role in the negative feedback regulation of Pmk1 cell integrity signaling.","authors":"Takada H","authors_abbrev":"Takada H","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-08-02","publication_year":"2011","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8005439","title":"Efficient targeted integration at leu1-32 and ura4-294 in Schizosaccharomyces pombe.","citation":"Genetics 1994 Mar;136(3):849-56","abstract":"Homologous integration into the fission yeast Schizosaccharomyces pombe has not been well characterized. In this study, we have examined integration of plasmids carrying the leu1+ and ura4+ genes into their chromosomal loci. Genomic DNA blot analysis demonstrated that the majority of transformants have one or more copies of the plasmid vector integrated via homologous recombination with a much smaller fraction of gene conversion to leu1+ or ura4+. Non-homologous recombination events were not observed for either gene. We describe the construction of generally useful leu1+ and ura4+ plasmids for targeted integration at the leu1-32 and ura4-294 loci of S. pombe.","authors":"Keeney JB, Boeke JD","authors_abbrev":"Keeney JB et al.","pubmed_publication_date":"Mar 1994","pubmed_entrez_date":"1994-03-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10381387","title":"Asymmetry of the spindle pole bodies and spg1p GAP segregation during mitosis in fission yeast.","citation":"J Cell Sci 1999 Jul;112 ( Pt 14):2313-21","abstract":"In the fission yeast Schizosaccharomyces pombe, the onset of septum formation is induced by a signal transduction network involving several protein kinases and a GTPase switch. One of the roles of the spg1p GTPase is to localise the cdc7p protein kinase to the poles of the mitotic spindle, from where the onset of septation is thought to be signalled at the end of mitosis. Immunofluorescence studies have shown that cdc7p is located on both spindle pole bodies early in mitosis, but only on one during the later stages of anaphase. This is mediated by inactivation of spg1p on one pole before the other. The GAP for spg1p is a complex of two proteins, cdc16p and byr4p. Localisation of cdc16p and byr4p by indirect immunofluorescence during the mitotic cell cycle showed that both proteins are present on the spindle pole body in interphase cells. During mitosis, byr4p is seen first on both poles of the spindle, then on only one. This occurs prior to cdc7p becoming asymmetric. In contrast, the signal due to cdc16p decreases to a low level during early mitosis, before being seen strongly on the same pole as byr4p. Double staining indicates that this is the opposite pole to that which retains cdc7p in late anaphase. Examination of the effect of inactivating cdc16p at various stages of the cell cycle suggests that cdc16p, together with cdc2p plays a role in restraining septum formation during interphase. The asymmetric inactivation of spg1p is mediated by recruitment of the cdc16p-byr4p GAP to one of the poles of the spindle before the other, and the asymmetry of the spindle pole bodies may be established early during mitosis. Moreover, the spindle pole bodies appear to be non-equivalent even after division has been completed.","authors":"Cerutti L, Simanis V","authors_abbrev":"Cerutti L et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-06-25","publication_year":"1999","canto_session_key":"5219d3ee134bc21e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-02-26 17:58:58","canto_approved_date":"2024-10-18 09:33:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-26 17:58:52","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC222.10c","SPAC6F6.08c","SPAC1565.06c","SPBC21.06c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2021-02-26"},{"uniquename":"PMID:18093330","title":"Checkpoint independence of most DNA replication origins in fission yeast.","citation":"BMC Mol Biol 2007 Dec 19;8:112","abstract":"In budding yeast, the replication checkpoint slows progress through S phase by inhibiting replication origin firing. In mammals, the replication checkpoint inhibits both origin firing and replication fork movement. To find out which strategy is employed in the fission yeast, Schizosaccharomyces pombe, we used microarrays to investigate the use of origins by wild-type and checkpoint-mutant strains in the presence of hydroxyurea (HU), which limits the pool of deoxyribonucleoside triphosphates (dNTPs) and activates the replication checkpoint. The checkpoint-mutant cells carried deletions either of rad3 (which encodes the fission yeast homologue of ATR) or cds1 (which encodes the fission yeast homologue of Chk2).\nOur microarray results proved to be largely consistent with those independently obtained and recently published by three other laboratories. However, we were able to reconcile differences between the previous studies regarding the extent to which fission yeast replication origins are affected by the replication checkpoint. We found (consistent with the three previous studies after appropriate interpretation) that, in surprising contrast to budding yeast, most fission yeast origins, including both early- and late-firing origins, are not significantly affected by checkpoint mutations during replication in the presence of HU. A few origins (approximately 3%) behaved like those in budding yeast: they replicated earlier in the checkpoint mutants than in wild type. These were located primarily in the heterochromatic subtelomeric regions of chromosomes 1 and 2. Indeed, the subtelomeric regions defined by the strongest checkpoint restraint correspond precisely to previously mapped subtelomeric heterochromatin. This observation implies that subtelomeric heterochromatin in fission yeast differs from heterochromatin at centromeres, in the mating type region, and in ribosomal DNA, since these regions replicated at least as efficiently in wild-type cells as in checkpoint-mutant cells.\nThe fact that approximately 97% of fission yeast replication origins - both early and late - are not significantly affected by replication checkpoint mutations in HU-treated cells suggests that (i) most late-firing origins are restrained from firing in HU-treated cells by at least one checkpoint-independent mechanism, and (ii) checkpoint-dependent slowing of S phase in fission yeast when DNA is damaged may be accomplished primarily by the slowing of replication forks.","authors":"Mickle KL, Ramanathan S, Rosebrock A, Oliva A, Chaudari A, Yompakdee C, Scott D, Leatherwood J, Huberman JA","authors_abbrev":"Mickle KL et al.","pubmed_publication_date":"19 Dec 2007","pubmed_entrez_date":"2007-12-21","publication_year":"2007","canto_session_key":"ac12e0d42489768e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-08-28 13:38:02","canto_approved_date":"2019-08-28 13:38:03","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-08-16 10:40:20","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC216.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-08-28"},{"uniquename":"PMID:15470229","title":"The structure of cell wall alpha-glucan from fission yeast.","citation":"Glycobiology 2005 Mar;15(3):245-57","abstract":"Morphology and structural integrity of fungal cells depend on cell wall polysaccharides. The chemical structure and biosynthesis of two types of these polysaccharides, chitin and (1-->3)-beta-glucan, have been studied extensively, whereas little is known about alpha-glucan. Here we describe the chemical structure of alpha-glucan isolated from wild-type and mutant cell walls of the fission yeast Schizosaccharomyces pombe. Wild-type alpha-glucan was found to consist of a single population of linear glucose polymers, approximately 260 residues in length. These glucose polymers were composed of two interconnected linear chains, each consisting of approximately 120 (1-->3)-linked alpha-d-glucose residues and some (1-->4)-linked alpha-D-glucose residues at the reducing end. By contrast, alpha-glucan of an alpha-glucan synthase mutant with an aberrant cell morphology and reduced alpha-glucan levels consisted of a single chain only. We propose that alpha-glucan biosynthesis involves an ordered series of events, whereby two alpha-glucan chains are coupled to create mature cell wall alpha-glucan. This mature form of cell wall alpha-glucan is essential for fission-yeast morphogenesis.","authors":"Grün CH, Hochstenbach F, Humbel BM, Verkleij AJ, Sietsma JH, Klis FM, Kamerling JP, Vliegenthart JF","authors_abbrev":"Grün CH et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2004-10-08","publication_year":"2005","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20363118","title":"Multiple faces of the SAGA complex.","citation":"Curr Opin Cell Biol 2010 Jun;22(3):374-82","abstract":"The SAGA complex provides a paradigm for multisubunit histone modifying complexes. Although first characterized as a histone acetyltransferase, because of the Gcn5 subunit, SAGA is now known to contain a second activity, a histone deubiquitinase, as well as subunits important for interactions with transcriptional activators and the general transcription machinery. The functions of SAGA in transcriptional activation are well-established in Saccharomyces cerevisiae. Recent studies in S. pombe, Drosophila, and mammalian systems reveal that SAGA also has important roles in transcript elongation, the regulation of protein stability, and telomere maintenance. These functions are essential for normal embryo development in flies and mice, and mutations or altered expression of SAGA subunits correlate with neurological disease and aggressive cancers in humans.","doi":"10.1016/j.ceb.2010.03.005","authors":"Koutelou E, Hirsch CL, Dent SY","authors_abbrev":"Koutelou E et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-04-06","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7791776","title":"Characterization of fus1 of Schizosaccharomyces pombe: a developmentally controlled function needed for conjugation.","citation":"Mol Cell Biol 1995 Jul;15(7):3697-707","abstract":"In Schizosaccharomyces pombe, the fus1 mutation blocks conjugation at a point after cell contact and agglutination. The cell walls separating the mating partners are not degraded, which prevents cytoplasmic fusion. In order to investigate the molecular mechanism of conjugation, we cloned the fus1 gene and found that it is capable of encoding a 1,372-amino-acid protein with no significant similarities to other known proteins. Expression of the fus1 gene is regulated by the developmental state of the cells. Transcription is induced by nitrogen starvation and requires a pheromone signal in both P and M cell types. Consequently, mutants defective in the pheromone response pathway fail to induce fus1 expression. The ste11 gene, which encodes a transcription factor controlling expression of many genes involved in sexual differentiation, is also required for transcription of fus1. Furthermore, deletion of two potential Ste11 recognition sites in the fus1 promoter region abolished transcription, and expression could be restored when we inserted a different Ste11 site from the mat1-P promoter. Since this element was inverted relative to the fus1 element, we conclude that activation of transcription by Ste11 is independent of orientation. Although the fus1 mutant has a phenotype very similar to that of Saccharomyces cerevisiae fus1 mutants, the two proteins appear to have different roles in the process of cell fusion. Budding yeast Fus1 is a typical membrane protein and contains an SH3 domain. Fission yeast Fus1 has no features of a membrane protein, yet it appears to localize to the projection tip. A characteristic proline-rich potential SH3 binding site may mediate interaction with other proteins.","authors":"Petersen J, Weilguny D, Egel R, Nielsen O","authors_abbrev":"Petersen J et al.","pubmed_publication_date":"Jul 1995","pubmed_entrez_date":"1995-07-01","publication_year":"1995","canto_session_key":"ef2da839886aa260","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-07 16:14:17","canto_approved_date":"2026-02-20 16:15:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-03 12:34:19","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.02c","SPBC32C12.02","SPBC1D7.05","SPAC1D4.13"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-09-07"},{"uniquename":"PMID:20208336","title":"Simple and effective gap-repair cloning using short tracts of flanking homology in fission yeast.","citation":"Biosci Biotechnol Biochem 2010;74(3):685-9","abstract":"Gap-repair cloning for plasmid construction in budding yeast is very effective and often used. In contrast, the same method is not widely used in fission yeast, because of a shortage of information on it. Here we describe simple and effective gap-repair cloning for plasmid construction using short tracts of flanking homology. By this method, we combined concentrated DNA fragments with short (20 bp) tracts of flanking homology with the marker gene or the pre-existing gene module. In addition, we found that this method can be applied to one-step cloning of multiple DNA fragments to construct a fusion gene.","authors":"Matsuo Y, Kishimoto H, Horiuchi T, Tanae K, Kawamukai M","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-03-09","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1563351","title":"The ras1 function of Schizosaccharomyces pombe mediates pheromone-induced transcription.","citation":"EMBO J 1992 Apr;11(4):1391-5","abstract":"Loss of ras1+ function renders fission yeast cells unable to undergo morphological changes in response to mating pheromones, whereas cells carrying activated mutations in ras1 are hyper-responsive. This has led to the suggestion that the ras1 gene product plays a role in mating pheromone signal transduction. Using partially purified M factor we demonstrate that the mat1-Pm gene, which controls entry into meiosis, is transcribed in response to a pheromone signal. Strains mutated in the ras1 gene or in ste6, the fission yeast homologue of Ras protein GDP/GTP exchange factor, are unable to induce transcription of mat1-Pm in response to M factor. Furthermore, an activated ras1val17 mutant exhibits a stronger induction of the mat1-Pm transcript. However, transcription still depends on nitrogen deprivation as well as on the presence of pheromone, showing that activation of the Ras1 protein alone does not substitute for any of these signals. The pat1-114 mutant bypasses the ras1/ste6 checkpoint, suggesting that activation of ras1 contributes to inactivation of the pat1 protein kinase.","authors":"Nielsen O, Davey J, Egel R","authors_abbrev":"Nielsen O et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"17ddda6fd2aaf627","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-06 14:28:04","canto_approved_date":"2026-04-08 11:06:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-20 09:58:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMTR.02","SPAC17H9.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-09-06"},{"uniquename":"PMID:25062917","title":"Pogo-like transposases have been repeatedly domesticated into CENP-B-related proteins.","citation":"Genome Biol Evol 2014 Jul 24;6(8):2008-16","abstract":"The centromere is a chromatin region that is required for accurate inheritance of eukaryotic chromosomes during cell divisions. Among the different centromere-associated proteins (CENP) identified, CENP-B has been independently domesticated from a pogo-like transposase twice: Once in mammals and once in fission yeast. Recently, a third independent domestication restricted to holocentric lepidoptera has been described. In this work, we take advantage of the high-quality genome sequence and the wealth of functional information available for Drosophila melanogaster to further investigate the possibility of additional independent domestications of pogo-like transposases into host CENP-B related proteins. Our results showed that CENP-B related genes are not restricted to holocentric insects. Furthermore, we showed that at least three independent domestications of pogo-like transposases have occurred in metazoans. Our results highlight the importance of transposable elements as raw material for the recurrent evolution of important cellular functions.","doi":"10.1093/gbe/evu153","authors":"Mateo L, González J","authors_abbrev":"Mateo L et al.","pubmed_publication_date":"24 Jul 2014","pubmed_entrez_date":"2014-07-27","publication_year":"2014","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2014-07-28 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37128864","title":"CDK actively contributes to establishment of the stationary phase state in fission yeast.","citation":"J Cell Sci 2023 May 15;136(10)","abstract":"Upon exhaustion of essential environmental nutrients, unicellular organisms cease cell division and enter stationary phase, a metabolically repressed state essential for cell survival in stressful environments. In the fission yeast Schizosaccharomyces pombe, cell size is reduced by cell division before entry into stationary phase; thus cyclin-dependent kinase (CDK) must actively contribute to stationary phase establishment. However, the contribution of CDK to stationary phase remains largely uncharacterized. Here, we examine the role of the sole S. pombe CDK, Cdc2, in the establishment of stationary phase. We show that in stationary phase, nuclear and chromosomal volumes and the nucleus-to-cell volume ratio are reduced, and sister chromatid separation and chromosome fluctuation are repressed. Furthermore, Cdc2 accumulates in the nucleolus. Most of these changes are induced by glucose depletion. Reduction in Cdc2 activity before and upon stationary phase entry alleviates the changes and shortens the survival time of stationary phase cells, whereas Cdc2 inhibition represses nucleolar Cdc2 accumulation and glucose depletion-induced nuclear volume reduction. These results demonstrate that CDK actively regulates stationary phase, both before and upon stationary phase entry.","doi":"10.1242/jcs.260727","authors":"Hiraoka M, Kiyota Y, Kawai S, Notsu Y, Yamada K, Kurashima K, Chang JW, Shimazaki S, Yamamoto A","authors_abbrev":"Hiraoka M et al.","pubmed_publication_date":"15 May 2023","pubmed_entrez_date":"2023-05-02","publication_year":"2023","canto_session_key":"d34af2b4410c9977","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ayumu Yamamoto","canto_first_approved_date":"2023-06-29 11:11:54","canto_approved_date":"2025-09-02 22:31:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-06-19 14:57:15","canto_added_date":"2023-05-03 00:15:04","annotation_curators":[{"name":"Ayumu Yamamoto","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03","SPAC1782.09c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-06-29"},{"uniquename":"PMID:33131769","title":"Cell cycle-dependent phosphorylation of IQGAP is involved in assembly and stability of the contractile ring in fission yeast.","citation":"Biochem Biophys Res Commun 2021 Jan 01;534:1026-1032","abstract":"Cytokinesis is the final step in cell division and is driven by the constriction of the medial actomyosin-based contractile ring (CR) in many eukaryotic cells. In the fission yeast Schizosaccharomyces pombe, the IQGAP-like protein Rng2 is required for assembly and constriction of the CR, and specifically interacts with actin filaments (F-actin) in the CR after anaphase. However, the mechanism that timely activates Rng2 has not yet been elucidated. We herein tested the hypothesis that the cytokinetic function of Rng2 is regulated by phosphorylation by examining phenotypes of a series of non-phosphorylatable and phosphomimetic rng2 mutant strains. In phosphomimetic mutant cells, F-actin in the CR was unstable. Genetic analyses indicated that phosphorylated Rng2 was involved in CR assembly in cooperation with myosin-II, whereas the phosphomimetic mutation attenuated the localization of Rng2 to CR F-actin. The present results suggest that Rng2 is phosphorylated during CR assembly and then dephosphorylated, which enhances the interaction between Rng2 and CR F-actin to stabilize the ring, thereby ensuring secure cytokinesis.","doi":"10.1016/j.bbrc.2020.10.043","authors":"Morita R, Numata O, Nakano K, Takaine M","authors_abbrev":"Morita R et al.","pubmed_publication_date":"01 Jan 2021","pubmed_entrez_date":"2020-11-02","publication_year":"2021","canto_session_key":"d1ca5d873c81c5fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masak Takaine","canto_first_approved_date":"2021-01-04 17:55:23","canto_approved_date":"2023-09-27 17:53:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-31 09:24:26","canto_added_date":"2020-11-04 01:15:05","annotation_curators":[{"name":"Masak Takaine","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAC4F8.13c","SPAC15A10.08"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2021-01-04"},{"uniquename":"PMID:15269544","title":"Flow process for electroextraction of intracellular enzymes from the fission yeast, Schizosaccharomyces pombe.","citation":"Biotechnol Lett 2004 Jun;26(11):933-7","abstract":"Flow treatment of the yeast, Schizosaccharomyces pombe, with high intensity electric field pulses released intracellular enzymes such as glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase. Over 70% of the total activity was liberated within 4 h after pulse application. The optimal field intensities were considerably higher than that needed for irreversible plasma membrane permeabilization.","authors":"Ganeva V, Galutzov B, Teissié J","authors_abbrev":"Ganeva V et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-07-23","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19054124","title":"Promoter regulation in Candida albicans and related species.","citation":"FEMS Yeast Res 2009 Feb;9(1):2-15","abstract":"Regulation of gene expression has been studied extensively in Saccharomyces cerevisiae and Schizosaccharomyces pombe. Some, but by far not all, of the findings are also applicable to Candida albicans, an important ascomycete fungal pathogen of humans. Areas of research in C. albicans include the influence of key signal transduction cascades on morphology, and the response to host-generated influences, such as host immune effector cells, blood, pH or elevated carbon dioxide. The resistance to antifungal agents and response to stress are also well researched. Conditional gene expression and reporter genes adapted to the codon usage of C. albicans are now widely used in C. albicans. Here we present a comprehensive overview of the current techniques used to investigate regulation mechanisms for promoters in C. albicans and other Candida species. In addition, we discuss reporter genes used for the study of gene expression.","doi":"10.1111/j.1567-1364.2008.00455.x","authors":"Eckert SE, Mühlschlegel FA","authors_abbrev":"Eckert SE et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-12-05","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29975684","title":"Bases of antisense lncRNA-associated regulation of gene expression in fission yeast.","citation":"PLoS Genet 2018 Jul;14(7):e1007465","abstract":"Antisense (as)lncRNAs can regulate gene expression but the underlying mechanisms and the different cofactors involved remain unclear. Using Native Elongating Transcript sequencing, here we show that stabilization of antisense Exo2-sensitivite lncRNAs (XUTs) results in the attenuation, at the nascent transcription level, of a subset of highly expressed genes displaying prominent promoter-proximal nucleosome depletion and histone acetylation. Mechanistic investigations on the catalase gene ctt1 revealed that its induction following oxidative stress is impaired in Exo2-deficient cells, correlating with the accumulation of an asXUT. Interestingly, expression of this asXUT was also activated in wild-type cells upon oxidative stress, concomitant to ctt1 induction, indicating a potential attenuation feedback. This attenuation correlates with asXUT abundance, it is transcriptional, characterized by low RNAPII-ser5 phosphorylation, and it requires an histone deacetylase activity and the conserved Set2 histone methyltransferase. Finally, we identified Dicer as another RNA processing factor acting on ctt1 induction, but independently of Exo2. We propose that asXUTs could modulate the expression of their paired-sense genes when it exceeds a critical threshold, using a conserved mechanism independent of RNAi.","doi":"10.1371/journal.pgen.1007465","authors":"Wery M, Gautier C, Descrimes M, Yoda M, Migeot V, Hermand D, Morillon A","authors_abbrev":"Wery M et al.","pubmed_publication_date":"Jul 2018","pubmed_entrez_date":"2018-07-06","publication_year":"2018","canto_session_key":"560d35bee35f5de7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-07-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.14","SPCC188.13c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:8838655","title":"Fission yeast Nda1 and Nda4, MCM homologs required for DNA replication, are constitutive nuclear proteins.","citation":"J Cell Sci 1996 Feb;109 ( Pt 2):319-26","abstract":"The nda1+ and nda4+ genes of the fission yeast Schizosaccharomyces pombe encode proteins similar to budding yeast MCM2 and MCM5/CDC46, respectively, which are required for the early stages of DNA replication. The budding yeast Mcm proteins display cell-cycle dependent localization. They are present in the nucleus specifically from late M phase until the beginning of S phase, so that they were suggested to be components of a replication licensing factor, a positive factor for the onset of replication, which is thought to be inactivated after use, thus restricting replication to only once in a cell cycle. In the present study, we raised antibodies against Nda1 or Nda4 and identified 115 kDa and 80 kDa proteins, respectively. Their immunolocalization was examined in wild-type cells and in various cell-cycle mutants. Both Nda1 and Nda4 proteins remained primarily in the nucleus throughout the cell cycle. In mutants arrested in G1, S, and G2 phases, these proteins were also enriched in the nucleus. These results indicate that the dramatic change in subcellular localization as seen in budding yeast is not essential in fission yeast for the functions of Nda1 and Nda4 proteins to be executed. The histidine-tagged nda1+ gene was constructed and integrated into the chromosome to replace the wild-type nda1+ gene. The resulting His-tagged Nda1 protein was adsorbed to the Ni-affinity column, and co-eluted with the untagged Nda4 protein, suggesting that they formed a complex.","authors":"Okishio N, Adachi Y, Yanagida M","authors_abbrev":"Okishio N et al.","pubmed_publication_date":"Feb 1996","pubmed_entrez_date":"1996-02-01","publication_year":"1996","canto_session_key":"8168ae09cd9f4daa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-10 10:16:32","canto_approved_date":"2021-12-15 21:44:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-10-16 14:49:16","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPAC1F7.05","SPBC4.04c","SPAC24H6.05","SPBC336.12c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-06-10"},{"uniquename":"PMID:10200169","title":"Processing of UV damage in vitro by FEN-1 proteins as part of an alternative DNA excision repair pathway.","citation":"Biochemistry 1999 Apr 13;38(15):4809-17","abstract":"Ultraviolet (UV) irradiation induces predominantly cyclobutane and (6-4) pyrimidine dimer photoproducts in DNA. Several mechanisms for repairing these mutagenic UV-induced DNA lesions have been identified. Nucleotide excision repair is a major pathway, but mechanisms involving photolyases and DNA glycosylases have also been characterized. Recently, a novel UV damage endonuclease (UVDE) was identified that initiates an excision repair pathway different from previously established repair mechanisms. Homologues of UVDE have been found in eukaryotes as well as in bacteria. In this report, we have used oligonucleotide substrates containing site-specific cyclobutane pyrimidine dimers and (6-4) photoproducts for the characterization of this UV damage repair pathway. After introduction of single-strand breaks at the 5' sides of the photolesions by UVDE, these intermediates became substrates for cleavage by flap endonucleases (FEN-1 proteins). FEN-1 homologues from humans, Saccharomyces cerevisiae, and Schizosaccharomyces pombe all cleaved the UVDE-nicked substrates at similar positions 3' to the photolesions. T4 endonuclease V-incised DNA was processed in the same way. Both nicked and flapped DNA substrates with photolesions (the latter may be intermediates in DNA polymerase-catalyzed strand displacement synthesis) were cleaved by FEN-1. The data suggest that the two enzymatic activities, UVDE and FEN-1, are part of an alternative excision repair pathway for repair of UV photoproducts.","authors":"Yoon JH, Swiderski PM, Kaplan BE, Takao M, Yasui A, Shen B, Pfeifer GP","authors_abbrev":"Yoon JH et al.","pubmed_publication_date":"13 Apr 1999","pubmed_entrez_date":"1999-04-14","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38890877","title":"Improving Muscat Hamburg Wine Quality with Innovative Fermentation Strategies Using  Schizosaccharomyces pombe  Derived from Fermented Grains of Sauce-Flavor Baijiu.","citation":"Foods 2024 May 24;13(11)","abstract":"This study investigates innovative approaches to improve the quality and aroma characteristics of Muscat Hamburg wine production by substituting the conventional  Saccharomyces cerevisiae  yeast with an efficient fermentation strain of  Schizosaccharomyces pombe . The typical use of  S. cerevisiae  in Muscat Hamburg wine often leads to uniformity and prolonged processing times, requiring subsequent malolactic fermentation to degrade excessive malic acid. The study advocates for the replacement of  S. cerevisiae  with a specific  S. pombe  strain,  Sp-410 , isolated from the fermented grains of sauce-flavor Baijiu, a Chinese spirit. Muscat Hamburg wine fermented with the  S. pombe  strain demonstrates decreased malic acid levels, offering a potential alternative to malolactic fermentation. However, exclusive  S. pombe  fermentation may result in an overproduction of acetic acid metabolites, leading to a monotonous taste. In response, the study proposes a mixed fermentation approach, combining the  S. pombe  strain with a  Saccharomyces uvarum  strain and a non- Saccharomyces  yeast,  Torulaspora delbrueckii . The optimized mixed fermentation strategies (M:SP+TD and M60SP+TD) involve specific proportions and intervals of inoculation, aiming to enhance the quality and aroma complexity of Muscat Hamburg wine. In conclusion, this research contributes to advancing the production of high-quality Muscat Hamburg wines, utilizing  S. pombe  as the primary yeast strain and implementing mixed fermentation methodologies.","doi":"10.3390/foods13111648","authors":"Lyu X, Zhou Y, Li F, Zhou M, Wei C, Lin L, Li X, Zhang C","authors_abbrev":"Lyu X et al.","pubmed_publication_date":"24 May 2024","pubmed_entrez_date":"2024-06-19","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-06-19 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17969326","title":"[Roles of DNA replication and recombination factors in telomere maintenance].","citation":"Seikagaku 2007 Sep;79(9):868-71","abstract":"","authors":"Ueno M","authors_abbrev":"Ueno M","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-11-01","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8898367","title":"Fission yeast pkl1 is a kinesin-related protein involved in mitotic spindle function.","citation":"Mol Biol Cell 1996 Oct;7(10):1639-55","abstract":"We have used anti-peptide antibodies raised against highly conserved regions of the kinesin motor domain to identify kinesin-related proteins in the fission yeast Schizosaccharomyces pombe. Here we report the identification of a new kinesin-related protein, which we have named pkl1. Sequence homology and domain organization place pkl1 in the Kar3/ncd subfamily of kinesin-related proteins. Bacterially expressed pkl1 fusion proteins display microtubule-stimulated ATPase activity, nucleotide-sensitive binding, and bundling of microtubules. Immunofluorescence studies with affinity-purified antibodies indicate that the pkl1 protein localizes to the nucleus and the mitotic spindle. Pkl1 null mutants are viable but have increased sensitivity to microtubule-disrupting drugs. Disruption of pkl1+ suppresses mutations in another kinesin-related protein, cut7, which is known to act in the spindle. Overexpression of pkl1 to very high levels causes a similar phenotype to that seen in cut7 mutants: V-shaped and star-shaped microtubule structures are observed, which we interpret to be spindles with unseparated spindle poles. These observations suggest that pkl1 and cut7 provide opposing forces in the spindle. We propose that pkl1 functions as a microtubule-dependent motor that is involved in microtubule organization in the mitotic spindle.","authors":"Pidoux AL, LeDizet M, Cande WZ","authors_abbrev":"Pidoux AL et al.","pubmed_publication_date":"Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_session_key":"c82b945cd59f0caa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-02-28 12:11:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-01 08:04:41","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A11.14c","SPAC25G10.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-04-01"},{"uniquename":"PMID:32878942","title":"Phosphoregulation of the cytokinetic protein Fic1 contributes to fission yeast growth polarity establishment.","citation":"J Cell Sci 2020 Sep 17;133(18)","abstract":"Cellular polarization underlies many facets of cell behavior, including cell growth. The rod-shaped fission yeast  Schizosaccharomyces pombe  is a well-established, genetically tractable system for studying growth polarity regulation.  S. pombe  cells elongate at their two cell tips in a cell cycle-controlled manner, transitioning from monopolar to bipolar growth in interphase when new ends established by the most recent cell division begin to extend. We previously identified cytokinesis as a critical regulator of new end growth and demonstrated that Fic1, a cytokinetic factor, is required for normal polarized growth at new ends. Here, we report that Fic1 is phosphorylated on two C-terminal residues, which are each targeted by multiple protein kinases. Endogenously expressed Fic1 phosphomutants cannot support proper bipolar growth, and the resultant defects facilitate the switch into an invasive pseudohyphal state. Thus, phosphoregulation of Fic1 links the completion of cytokinesis to the re-establishment of polarized growth in the next cell cycle. These findings broaden the scope of signaling events that contribute to regulating  S. pombe  growth polarity, underscoring that cytokinetic factors constitute relevant targets of kinases affecting new end growth.This article has an associated First Person interview with Anthony M. Rossi, joint first author of the paper.","doi":"10.1242/jcs.244392","authors":"Bohnert KA, Rossi AM, Jin QW, Chen JS, Gould KL","authors_abbrev":"Bohnert KA et al.","pubmed_publication_date":"17 Sep 2020","pubmed_entrez_date":"2020-09-04","publication_year":"2020","canto_session_key":"5d8d5a6ec633fc68","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Anthony Rossi","canto_first_approved_date":"2020-10-12 19:59:12","canto_approved_date":"2024-01-29 21:15:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-10-07 15:49:30","canto_added_date":"2020-09-05 00:15:04","annotation_curators":[{"name":"Anthony Rossi","community_curator":true,"annotation_count":23,"orcid":"0000-0003-3787-8573","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC83.18c","SPAC24H6.05","SPBC11B10.09","SPAC23C11.11","SPAC20G8.05c","SPBC11C11.02","SPBP4H10.04","SPBC4F6.12"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2020-10-12"},{"uniquename":"PMID:25776556","title":"The Human RNA Polymerase I Transcription Terminator Complex Acts as a Replication Fork Barrier That Coordinates the Progress of Replication with rRNA Transcription Activity.","citation":"Mol Cell Biol 2015 May;35(10):1871-81","abstract":"In S phase, the replication and transcription of genomic DNA need to accommodate each other, otherwise their machineries collide, with chromosomal instability as a possible consequence. Here, we characterized the human replication fork barrier (RFB) that is present downstream from the 47S pre-rRNA gene (ribosomal DNA [rDNA]). We found that the most proximal transcription terminator, Sal box T1, acts as a polar RFB, while the other, Sal box T4/T5, arrests replication forks bidirectionally. The fork-arresting activity at these sites depends on polymerase I (Pol I) transcription termination factor 1 (TTF-1) and a replisome component, TIMELESS (TIM). We also found that the RFB activity was linked to rDNA copies with hypomethylated CpG and coincided with the time that actively transcribed rRNA genes are replicated. Failed fork arrest at RFB sites led to a slowdown of fork progression moving in the opposite direction to rRNA transcription. Chemical inhibition of transcription counteracted this deceleration of forks, indicating that rRNA transcription impedes replication in the absence of RFB activity. Thus, our results reveal a role of RFB for coordinating the progression of replication and transcription activity in highly transcribed rRNA genes.","doi":"10.1128/MCB.01521-14","authors":"Akamatsu Y, Kobayashi T","authors_abbrev":"Akamatsu Y et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-03-18","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:12397","SPAC22F8.07c","SPBC1198.11c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"EMBL:AU013275","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15265986","title":"The Clp1p/Flp1p phosphatase ensures completion of cytokinesis in response to minor perturbation of the cell division machinery in Schizosaccharomyces pombe.","citation":"J Cell Sci 2004 Aug 01;117(Pt 17):3897-910","abstract":"Fission yeast mutants defective in actomyosin ring formation and function exhibit a prolonged G2 delay following cytokinesis failure. This G2 delay depends on the SIN, a signaling network essential for cytokinesis, and the non-essential Cdc14p family phosphatase, Clp1p/Flp1p and has been proposed to signify a cytokinesis checkpoint mechanism. However, the physiological relevance of this proposed Clp1p/Flp1p-dependent checkpoint is unclear because all previous studies were carried out using mutations in essential actomyosin ring components under fully restrictive conditions and thus these cells would have died regardless of the presence of the checkpoint. Here we show that delays in cytokinesis caused by minor perturbations to different components of the cytokinetic machinery, which normally cause only mild defects, become lethal when Clp1p/Flp1p is inactivated. In addition, we show that Clp1p/Flp1p does not function simply to inhibit further rounds of nuclear division, but also allows damaged actomyosin rings to be maintained to facilitate completion of cell division. Ectopic activation of the SIN significantly bypasses the requirement of Clp1p/Flp1p for G2 delay as well as for completion of cytokinesis. We conclude that the Clp1p/Flp1p-dependent cytokinesis checkpoint provides a previously unrecognized cell survival advantage when the cell division apparatus is mildly perturbed.","authors":"Mishra M, Karagiannis J, Trautmann S, Wang H, McCollum D, Balasubramanian MK","authors_abbrev":"Mishra M et al.","pubmed_publication_date":"01 Aug 2004","pubmed_entrez_date":"2004-07-22","publication_year":"2004","canto_session_key":"b22f1157ab22d428","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-04-29 11:15:24","canto_approved_date":"2025-06-10 14:48:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-25 12:14:06","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPCC645.05c","SPAP8A3.08","SPAC24H6.05","SPAC20G8.05c","SPAC6F6.08c","SPBC19G7.05c","SPAC9G1.09","SPAC24B11.11c","SPAC4F8.13c","SPBC24C6.07","SPAC1782.09c"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2017-04-29"},{"uniquename":"PMID:18481965","title":"Co-ordination of cytokinesis with chromosome segregation.","citation":"Biochem Soc Trans 2008 Jun;36(Pt 3):387-90","abstract":"During anaphase, the spindle pulls the sister kinetochores apart until the sister chromatids are fully separated from each other. Subsequently, cytokinesis cleaves between the two separated chromosome masses to form two nucleated cells. Results from Schizosaccharomyces pombe suggested that cytokinesis and chromosome segregation are not co-ordinated with each other. However, recent studies indicate that, at least in budding yeast, a checkpoint called NoCut prevents abscission when spindle elongation is impaired, and might delay cytokinesis until all chromosomes are pulled out of the cleavage plane. Here, we discuss this possibility and summarize evidence suggesting that such a checkpoint is likely to be conserved in higher eukaryotes.","doi":"10.1042/BST0360387","authors":"Mendoza M, Barral Y","authors_abbrev":"Mendoza M et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-05-17","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25483073","title":"Chromosome segregation and organization are targets of 5'-Fluorouracil in eukaryotic cells.","citation":"Cell Cycle 2015;14(2):206-18","abstract":"The antimetabolite 5'-Fluorouracil (5FU) is an analog of uracil commonly employed as a chemotherapeutic agent in the treatment of a range of cancers including colorectal tumors. To assess the cellular effects of 5FU, we performed a genome-wide screening of the haploid deletion library of the eukaryotic model Schizosaccharomyces pombe. Our analysis validated previously characterized drug targets including RNA metabolism, but it also revealed unexpected mechanisms of action associated with chromosome segregation and organization (post-translational histone modification, histone exchange, heterochromatin). Further analysis showed that 5FU affects the heterochromatin structure (decreased levels of histone H3 lysine 9 methylation) and silencing (down-regulation of heterochromatic dg/dh transcripts). To our knowledge, this is the first time that defects in heterochromatin have been correlated with increased cytotoxicity to an anticancer drug. Moreover, the segregation of chromosomes, a process that requires an intact heterochromatin at centromeres, was impaired after drug exposure. These defects could be related to the induction of genes involved in chromatid cohesion and kinetochore assembly. Interestingly, we also observed that thiabendazole, a microtubule-destabilizing agent, synergistically enhanced the cytotoxic effects of 5FU. These findings point to new targets and drug combinations that could potentiate the effectiveness of 5FU-based treatments.","doi":"10.4161/15384101.2014.974425","authors":"Mojardín L, Botet J, Moreno S, Salas M","authors_abbrev":"Mojardín L et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2014-12-09","publication_year":"2015","canto_session_key":"ae7b1de4be92ec3f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-01-20 16:33:59","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-20 16:33:52","canto_added_date":"2014-12-10 01:16:42","annotation_curators":[],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":271,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_25483073_phaf.tsv"}],"genes":["SPCC4B3.08","SPBC609.05","SPAC10F6.16","SPBC32F12.01c","SPAC4F8.03","SPBC1734.05c","SPAC1D4.03c","SPBC651.10","SPBC19G7.10c","SPAC17G8.05","SPCC757.09c","SPBC13E7.11","SPAC222.04c","SPAC4G9.10","SPCC576.13","SPAC144.02","SPAC23H4.12","SPBC1198.11c","SPAPJ696.01c","SPBC16E9.09c","SPBC4F6.04","SPBC3E7.15c","SPAC19G12.08","SPBC17G9.07","SPAC22A12.07c","SPAPB17E12.13","SPAC4D7.10c","SPAC23C11.15","SPBC1734.11","SPAC977.17","SPBC31F10.09c","SPBC83.03c","SPCC553.08c","SPAC4G9.13c","SPBC1709.11c","SPBC29A10.16c","SPAC1610.02c","SPBC32C12.03c","SPCC790.02","SPBC31E1.02c","SPCC126.03","SPBC3H7.09","SPCC550.12","SPAC4G8.11c","SPAC4H3.02c","SPBC21C3.01c","SPBC30D10.04","SPCC645.02","SPAC4G9.14","SPBC16A3.19","SPBC4C3.12","SPAC18G6.10","SPAC9G1.02","SPBC13G1.08c","SPAC3G6.02","SPCP1E11.05c","SPBC530.14c","SPBC1539.08","SPBC1734.15","SPAC3G6.13c","SPAPYUG7.04c","SPCC1739.08c","SPAC3F10.16c","SPCC663.04","SPCC794.03","SPBC18H10.07","SPBC1271.12","SPAC13C5.04","SPBC365.14c","SPCC622.18","SPAC11E3.03","SPAC1805.03c","SPAC19A8.11c","SPAC4F10.11","SPAC19A8.01c","SPCC1672.04c","SPCC364.05","SPAC1610.01","SPAC16A10.05c","SPBC1861.05","SPAC3G9.07c","SPAC4C5.02c","SPAC6B12.07c","SPBC336.01","SPBC28F2.10c","SPBC32F12.11","SPAC1851.04c","SPAC3C7.12","SPAC1783.07c","SPBC29A10.01","SPBP35G2.13c","SPBC16G5.15c","SPAC30C2.02","SPBC1921.07c","SPCC285.13c","SPBC1306.02","SPAC644.14c","SPAC1F8.06","SPBC405.04c","SPBC685.07c","SPAC3A12.10","SPCC663.12","SPAC6B12.15","SPAC644.06c","SPAC3A12.12","SPAC15E1.06","SPBC4F6.12","SPBC1539.10","SPAC22F8.12c","SPBC336.03","SPBC27B12.03c","SPCC126.08c","SPBC1778.01c","SPAC22E12.11c","SPCC576.12c","SPAC637.07","SPAC22F3.03c","SPAC688.11","SPAC23D3.09","SPAC6F12.06","SPAC9G1.12","SPBC21D10.10","SPBC146.09c","SPBC19C7.02","SPBC2D10.16","SPAC1296.05c","SPBC409.18","SPAC19E9.01c","SPAC1783.05","SPCC736.11","SPAC17G6.04c","SPBC887.10","SPAP27G11.06c","SPCC1919.10c","SPAC12G12.12","SPAC664.01c","SPCC594.05c","SPBC4F6.11c","SPAC18B11.04","SPBC354.03","SPCC18.13","SPCC970.10c","SPAC23H3.05c","SPBC1734.12c","SPAC26A3.16","SPAC23C4.08","SPBC337.03","SPAC16.04","SPAC926.03","SPAC4F8.01","SPCC1393.08","SPCC663.11","SPBC32H8.02c","SPBC1685.09","SPAC2F7.04","SPBC16A3.03c","SPBC14C8.17c","SPBC725.06c","SPBC4F6.06","SPBC119.12","SPAC23E2.01","SPAC10F6.08c","SPBC14F5.13c","SPAC29A4.18","SPCC1223.15c","SPAC1783.02c","SPCC1919.15","SPCC24B10.11c","SPCC895.07","SPAPB17E12.08","SPBC6B1.04","SPBC11B10.10c","SPBC18H10.19","SPAC17A5.16","SPAC30D11.14c","SPAC17A5.14","SPBC1604.20c","SPBC16H5.07c","SPAC4F10.14c","SPBC4B4.10c","SPAC22H12.04c","SPBC428.08c","SPAC17H9.09c","SPAC6F6.01","SPAC589.07c","SPCC188.07","SPAC17A5.08","SPAC821.05","SPBC354.05c","SPBP4G3.02","SPAC1527.02","SPAC31G5.18c","SPAC18B11.07c","SPBC16C6.01c","SPCC1682.14","SPCC24B10.08c","SPAC31A2.14","SPAC3H1.12c","SPBC3H7.12","SPAC1952.05","SPAC1834.05","SPAC110.02","SPBC691.04","SPAC328.02","SPBP16F5.03c","SPBC215.03c","SPBC29A3.05","SPAC25A8.01c","SPAC2F7.07c","SPBC1703.12","SPCC11E10.07c","SPCC830.06","SPAC13G7.07","SPAC227.01c","SPAC2C4.05","SPAC140.03","SPAC24B11.12c","SPAC30C2.05","SPCC306.04c","SPBC4C3.08","SPAC27F1.08","SPBC1604.02c","SPCC1259.07","SPCC1223.06","SPBC106.07c","SPAC25B8.03","SPAC1071.02","SPAC17H9.10c","SPAC11E3.01c","SPAC1952.17c","SPCPB16A4.04c","SPAC17A2.06c","SPAC4A8.09c","SPBC16A3.17c","SPAC4G8.10","SPBC19C2.14","SPAC1851.03","SPAC22H10.11c","SPBC4B4.07c","SPCC297.05","SPCC74.02c","SPBC365.11","SPAC15E1.04","SPCC1450.02","SPCC550.14","SPAC22F3.09c","SPAC31A2.11c","SPBC11C11.07","SPBC17A3.05c","SPCC1259.03","SPCC11E10.08","SPAC6F12.09","SPAC57A10.02","SPAC6G10.12c","SPBC2G2.14","SPCC736.06","SPBC4B4.03","SPCC622.08c","SPBC32F12.08c","SPBC1D7.03","SPAC3H8.02","SPAC1142.08","SPCC613.12c","SPAC56F8.06c","SPCC188.02","SPBC887.06c","SPAC1486.08","SPAC144.06","SPCC364.03","SPAC14C4.16","SPBP16F5.05c"],"gene_count":271,"ltp_gene_count":0,"approved_date":"2015-01-20"},{"uniquename":"PMID:7489897","title":"Characterization of a new DNA polymerase from Schizosaccharomyces pombe: a probable homologue of the Saccharomyces cerevisiae DNA polymerase gamma.","citation":"Gene 1995 Nov 07;165(1):103-7","abstract":"Mitochondrial (mt) DNA replication is carried out by the nuclear-encoded DNA polymerase-gamma (Pol-gamma). We have cloned a new DNA polymerase-encoding gene from Schizosaccharomyces pombe (Sp), which we believe encodes the homologue of the Saccharomyces cerevisiae (Sc) mt DNA polymerase (MIP1). The putative Sp pol gamma gene expressed a transcript of approx. 4-kb that contained a 3-kb open reading frame encoding a polypeptide of 1018 amino acids (aa) (116 kDa). This Sp Pol-gamma is 48% identical to the Sc MIP1 and contains uniquely conserved regions not found in the bacterial PolI-type DNA polymerases. The most notable difference between these two proteins is that the MIP1 product has a 236-aa C-terminal region beyond motif C that is not found in Sp Pol-gamma. Chromosomal mapping and genomic sequencing of the Sp pol gamma places this gene on chromosome III downstream from the triose phosphate isomerase-encoding gene.","authors":"Ropp PA, Copeland WC","authors_abbrev":"Ropp PA et al.","pubmed_publication_date":"07 Nov 1995","pubmed_entrez_date":"1995-11-07","publication_year":"1995","canto_session_key":"7cd53fa3377c572a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-10-21 15:46:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-21 15:46:02","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.22"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-10-21"},{"uniquename":"PMID:7086393","title":"Cell cycle specificity of certain antimicrotubular drugs in Schizosaccharomyces pombe.","citation":"J Gen Microbiol 1982 Jan;128(1):61-71","abstract":"Of the seven antimicrotubular drugs tested, nocodazole, mebendazole and trifluralin at saturable concentrations failed to inhibit cell division in Schizosaccharomyces pombe, while carbendazim, thiabendazole and chloropropham each at 50 micrograms ml- and amiprophos methyl at 200 micrograms ml-1 completely arrested cell division. This inhibition was associated with striking morphological changes in which carbendazim- and thiabendazole-treated cells became elongated and pseudohyphal, whereas chloropropham- and amiprophos methyl-treated cells appeared small and rounded with occasional V-shaped pairs. Lomofungin staining revealed that nuclear division was also arrested by these drugs. Suspected blockage of defined cell cycle stages was confirmed by pulse-induction experiments which revealed that cells could be synchronized into division using exposure to a drug for one generation. Further experiments with synchronous cultures prepared by size selection showed that different drugs possessed different transition points; for example, carbendazim and thiabendazole were effective in blocking a late stage of the cell cycle just prior to division, whereas amiprophos methyl affected a very early stage. The results suggest that some of the drugs used exert cell cycle specificity in S. pombe either by impairing microtubule assembly mechanisms (as with carbendazim and thiabendazole) or by inhibiting synthesis of tubulin subunits (as with amiprophos methyl). These drugs could prove useful in studies of microtubule biogenesis during the cell cycle in yeast.","authors":"Walker GM","authors_abbrev":"Walker GM","pubmed_publication_date":"Jan 1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32788323","title":"A lncRNA-regulated gene expression system with rapid induction kinetics in the fission yeast  Schizosaccharomyces pombe .","citation":"RNA 2020 Nov;26(11):1743-1752","abstract":"The fission yeast  Schizosaccharomyces pombe  is an excellent model organism for the study of eukaryotic cellular physiology. The organism is genetically tractable and several tools to study the functions of individual genes are available. One such tool is regulatable gene expression and overproduction of proteins. Limitations of currently available overexpression systems include delay in expression after induction, narrow dynamic range, and system-wide changes due to induction conditions. Here I describe a new long noncoding RNA (lncRNA)-regulated, thiamine-inducible expression system that integrates lncRNA-based transcriptional interference at the fission yeast  tgp1  promoter with the fast repression kinetics of the thiamine-repressible  nmt1  promoter. This hybrid system has rapid induction kinetics, broad dynamic range, and tunable expression via thiamine concentration. The lncRNA-regulated thiamine-inducible system will be advantageous for the study of individual genes and for potential applications in the production of heterologous proteins in fission yeast.","doi":"10.1261/rna.076000.120","authors":"Garg A","authors_abbrev":"Garg A","pubmed_publication_date":"Nov 2020","pubmed_entrez_date":"2020-08-14","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-08-15 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC00839","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17727698","title":"Mitotic regulation by NIMA-related kinases.","citation":"Cell Div 2007 Aug 29;2:25","abstract":"The NIMA-related kinases represent a family of serine/threonine kinases implicated in cell cycle control. The founding member of this family, the NIMA kinase of Aspergillus nidulans, as well as the fission yeast homologue Fin1, contribute to multiple aspects of mitotic progression including the timing of mitotic entry, chromatin condensation, spindle organization and cytokinesis. Mammals contain a large family of eleven NIMA-related kinases, named Nek1 to Nek11. Of these, there is now substantial evidence that Nek2, Nek6, Nek7 and Nek9 also regulate mitotic events. At least three of these kinases, as well as NIMA and Fin1, have been localized to the microtubule organizing centre of their respective species, namely the centrosome or spindle pole body. Here, they have important functions in microtubule organization and mitotic spindle assembly. Other Nek kinases have been proposed to play microtubule-dependent roles in non-dividing cells, most notably in regulating the axonemal microtubules of cilia and flagella. In this review, we discuss the evidence that NIMA-related kinases make a significant contribution to the orchestration of mitotic progression and thereby protect cells from chromosome instability. Furthermore, we highlight their potential as novel chemotherapeutic targets.","authors":"O'regan L, Blot J, Fry AM","authors_abbrev":"O'regan L et al.","pubmed_publication_date":"29 Aug 2007","pubmed_entrez_date":"2007-08-31","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12442303","title":"Chromate sensitivity in fission yeast is caused by increased glutathione reductase activity and peroxide overproduction.","citation":"J Basic Microbiol 2002;42(6):408-19","abstract":"The Cr(VI)-sensitive mutant chr-51S of the Schizosaccharomyces pombe accumulated chromate (CrO(4) (2-)) and reduced Cr(V) to much greater extent, than did its parental strain 6 chr(+). Sublethal doses of K(2)Cr(2)O(7) did not induce any adaptive stress response, while H(2)O(2) or menadione pretreatment proved protective against the cell injuries caused by Cr(VI). The intracellular GSH concentration in chr-51S cells was approximately half of that for the 6 chr(+). Moreover, the glutathione disulfide reducing capacity of chr-51S was characterized by significantly increased glutathione reductase (GR) and glucose-6-phosphate dehydrogenase activities. These data strongly suggested that, instead of GSH, the NADPH/GR system was the major one-electron Cr(VI) reductant in vivo. The increased Cr(V) reduction in chr-51S mutant was accompanied by high intracellular superoxide and peroxide concentrations, required for formation of the hydroxyl radical ((*)OH). The decreased intracellular GSH levels and the Cr(VI)-sensitive phenotype of the chr-51S cells indicates that GSH might act effectively against chromate by scavenging (*)OH.","authors":"Pesti M, Gazdag Z, Emri T, Farkas N, Koósz Z, Belágyi J, Pócsi I","authors_abbrev":"Pesti M et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-11-21","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33419777","title":"Identification of mutants with increased variation in cell size at onset of mitosis in fission yeast.","citation":"J Cell Sci 2021 Feb 11;134(3)","abstract":"Fission yeast cells divide at a similar cell length with little variation about the mean. This is thought to be the result of a control mechanism that senses size and corrects for any deviations by advancing or delaying onset of mitosis. Gene deletions that advance cells into mitosis at a smaller size or delay cells entering mitosis have led to the identification of genes potentially involved in this mechanism. However, the molecular basis of this control is still not understood. In this work, we have screened for genes that when deleted increase the variability in size of dividing cells. The strongest candidate identified in this screen was  mga2  The  mga2  deletion strain shows a greater variation in cell length at division, with a coefficient of variation (CV) of 15-24%, while the wild-type strain has a CV of 5-8%. Furthermore, unlike wild-type cells, the  mga2  deletion cells are unable to correct cell size deviations within one cell cycle. We show that the  mga2  gene genetically interacts with  nem1  and influences the nuclear membrane and the nuclear-cytoplasmic transport of CDK regulators.","doi":"10.1242/jcs.251769","authors":"Scotchman E, Kume K, Navarro FJ, Nurse P","authors_abbrev":"Scotchman E et al.","pubmed_publication_date":"11 Feb 2021","pubmed_entrez_date":"2021-01-09","publication_year":"2021","canto_session_key":"848fdf36e609c892","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-03-03 17:15:11","canto_approved_date":"2024-04-03 10:16:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-05 18:14:45","canto_added_date":"2021-01-11 01:15:06","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":26,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPAC23C11.13c","SPBC543.07","SPAC31A2.13c","SPAC9E9.09c","SPBC215.03c","SPBC25D12.05","SPAC1B2.03c","SPBC582.03","SPAC14C4.16","SPCC18B5.03","SPAC13G6.14","SPAC869.03c","SPAC17G8.05","SPBC3B8.10c","SPAC26H5.05","SPBC11B10.09","SPCC663.12","SPAC1071.02","SPAC637.07","SPBC3B8.05","SPBC557.02c"],"gene_count":22,"ltp_gene_count":10,"approved_date":"2021-03-03"},{"uniquename":"PMID:7860624","title":"A novel cis-acting centromeric DNA element affects S. pombe centromeric chromatin structure at a distance.","citation":"J Cell Biol 1995 Feb;128(4):445-54","abstract":"The chromatin structure of the central core region of Schizosaccharomyces pombe centromeric DNA is unusual. This distinctive chromatin structure is associated only with central core sequences in a functional context and is modulated by a novel cis-acting DNA element (centromere enhancer) within the functionally critical K centromeric repeat, which is found in multiple copies in all three S. pombe centromeres. The centromere enhancer alters central core chromatin structure from a distance and in an orientation-independent manner without altering the nucleosomal packaging of sequences between the enhancer and the central core. These findings suggest a functionally relevant structural interaction between the enhancer and the centromeric central core brought about by DNA looping.","authors":"Marschall LG, Clarke L","authors_abbrev":"Marschall LG et al.","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_session_key":"964faa5ab64313a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-02-01 23:57:47","canto_approved_date":"2019-02-01 23:57:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-01 23:57:39","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-02-01"},{"uniquename":"EMBL:AU008592","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008985","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.96"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22172946","title":"The stress granule protein Vgl1 and poly(A)-binding protein Pab1 are required for doxorubicin resistance in the fission yeast Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2012 Jan 06;417(1):399-403","abstract":"Doxorubicin is an anthracycline antibiotic widely used for chemotherapy. Although doxorubicin is effective in the treatment of several cancers, including solid tumors and leukemias, the basis of its mechanism of action is not completely understood. Here, we describe the effects of doxorubicin and its relationship with stress granules formation in the fission yeast, Schizosaccharomyces pombe. We show that disruption of genes encoding the components of stress granules, including vgl1(+), which encodes a multi-KH type RNA-binding protein, and pab1(+), which encodes a poly(A)-binding protein, resulted in greater sensitivity to doxorubicin than seen in wild-type cells. Disruption of the vgl1(+) and pab1(+) genes did not confer sensitivity to other anti-cancer drugs such as cisplatin, 5-fluorouracil, and paclitaxel. We also showed that doxorubicin treatment promoted stress granule formation when combined with heat shock. Notably, doxorubicin treatment did not induce hyperphosphorylation of eIF2α, suggesting that doxorubicin is involved in stress granule assembly independent of eIF2α phosphorylation. Our results demonstrate the usefulness of fission yeast for elucidating the molecular targets of doxorubicin toxicity and suggest a novel drug-resistance mechanism involving stress granule assembly.","doi":"10.1016/j.bbrc.2011.11.127","authors":"Morita T, Satoh R, Umeda N, Kita A, Sugiura R","authors_abbrev":"Morita T et al.","pubmed_publication_date":"06 Jan 2012","pubmed_entrez_date":"2011-12-17","publication_year":"2012","canto_session_key":"3431227650f88754","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-10-27 13:18:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-27 13:18:07","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A7.04c","SPAC3G9.09c","SPCC550.14"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-10-27"},{"uniquename":"EMBL:AU011050","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.66"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20833892","title":"Schizosaccharomyces pombe calmodulin, Cam1, plays a crucial role in sporulation by recruiting and stabilizing the spindle pole body components responsible for assembly of the forespore membrane.","citation":"Eukaryot Cell 2010 Dec;9(12):1925-35","abstract":"Calmodulin in Schizosaccharomyces pombe is encoded by the cam1(+) gene, which is indispensable for both vegetative growth and sporulation. Here, we report how Cam1 functions in spore formation. We found that Cam1 preferentially localized to the spindle pole body (SPB) during meiosis and sporulation. Formation of the forespore membrane, a precursor of the plasma membrane in spores, was blocked in a missense cam1 mutant, which was viable but unable to sporulate. Three SPB proteins necessary for the onset of forespore membrane formation, Spo2, Spo13, and Spo15, were unable to localize to the SPB in the cam1 mutant although five core SPB components that were tested were present. Recruitment of Spo2 and Spo13 is known to require the presence of Spo15 in the SPB. Notably, Spo15 was unstable in the cam1 mutant, and as a result, SPB localization of Spo2 and Spo13 was lost. Overexpression of Spo15 partially alleviated the sporulation defect in the cam1 mutant. These results indicate that calmodulin plays an essential role in forespore membrane formation by stably maintaining Spo15, and thus Spo2 and Spo13, at the SPB in meiotic cells.","doi":"10.1128/EC.00022-10","authors":"Itadani A, Nakamura T, Hirata A, Shimoda C","authors_abbrev":"Itadani A et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-09-14","publication_year":"2010","canto_session_key":"170b4d4db77791d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-06-14 16:15:18","canto_approved_date":"2025-12-28 16:50:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-12 14:41:40","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.14","SPBC244.01c","SPBC649.05","SPBC12D12.01","SPBC365.15","SPCC1183.12","SPAC1F3.06c","SPBC16C6.14","SPAC6G9.06c"],"gene_count":9,"ltp_gene_count":2,"approved_date":"2016-06-14"},{"uniquename":"PMID:8825100","title":"Osmoregulation of fission yeast: cloning of two distinct genes encoding glycerol-3-phosphate dehydrogenase, one of which is responsible for osmotolerance for growth.","citation":"Mol Microbiol 1995 Dec;18(5):963-73","abstract":"Many types of microorganisms, including both prokaryotes and eukaryotes, have developed mechanisms to adapt to severe osmotic stress. In this study, we isolated multicopy suppressor genes for a Schizosaccharomyces pombe mutant, which exhibited the clear phenotype of being osmosensitive for growth (Osms) on agar plates containing high concentrations of either non-ionic or ionic osmotic solutes. Two genes were thus identified, and each was suggested to encode an NADH-dependent glycerol-3-phosphate dehydrogenase (GPD), which is required for glycerol synthesis. The nucleotide sequences, determined for these genes (named gpd1+ and gpd2+, respectively), revealed that S. pombe has two distinct GPD isozymes. They are only 60% identical to each other in their amino acid sequences. One such isozyme, GPD1, was shown to be directly involved in osmoregulation, based on the following observations. (i) Expression of gpd1+ was regulated at the mRNA level in response to osmotic upshift. (ii) It was demonstrated that wild-type cells markedly accumulated internal glycerol under high-osmolarity growth conditions. (iii) delta gpd1 mutants, however, failed to do so even in a high-osmolarity medium, and thus exhibited an Osms phenotype. On the other hand, the gpd2+ gene was constitutively expressed at a particular low level, regardless of the osmolarity of the medium.","authors":"Ohmiya R, Yamada H, Nakashima K, Aiba H, Mizuno T","authors_abbrev":"Ohmiya R et al.","pubmed_publication_date":"Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"40074c9a29f68732","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-10-30 22:58:00","canto_approved_date":"2024-07-12 09:04:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-23 16:12:32","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC215.05","SPAC23D3.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-10-30"},{"uniquename":"PMID:15157886","title":"Strategies for gene disruptions and plasmid constructions in fission yeast.","citation":"Methods 2004 Jul;33(3):199-205","abstract":"Molecular genetic analyses in Schizosaccharomyces pombe are greatly enhanced by our ability to delete chromosomal genes via homologous recombination and to introduce genes expressed from autonomous plasmids. In this paper, we describe a novel approach to generating marked deletion cassettes that bypasses the need for the long, PAGE-purified oligonucleotides required in the currently used PCR-based deletion approach. We also describe additional uses of this two-step PCR method for constructing chromosomal insertion cassettes. Finally, we describe how gap repair in S. pombe can facilitate plasmid constructions in a manner that circumvents the reliance on compatible restriction sites in the DNA molecules that are being joined. Several applications of this gap repair plasmid construction strategy are discussed.","authors":"Wang L, Kao R, Ivey FD, Hoffman CS","authors_abbrev":"Wang L et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR10562","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:25906","SPBC1921.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12519786","title":"Exposure of single-stranded telomeric DNA causes G2/M cell cycle arrest in Saccharomyces cerevisiae.","citation":"J Biol Chem 2003 Mar 14;278(11):9318-21","abstract":"In Saccharomyces cerevisiae, Cdc13p is a single-stranded TG(1-3) DNA binding protein that protects telomeres and maintains telomere length. A mutant allele of CDC13, cdc13-1, causes accumulation of single-stranded TG(1-3) DNA near telomeres along with a G(2)/M cell cycle arrest at non-permissive temperatures. We report here that when the single-stranded TG(1-3) DNA is masked by its binding proteins, such as S. cerevisiae Gbp2p or Schizosaccharomyces pombe Tcg1, the growth arrest phenotype of cdc13-1 is rescued. Mutations on Gbp2p that disrupt its binding to the single-stranded TG(1-3) DNA render the protein unable to complement the defects of cdc13-1. These results indicate that the presence of a single-stranded TG(1-3) tail in cdc13-1 cells serves as the signal for the cell cycle checkpoint. Moreover, the binding activity of Gbp2p to single-stranded TG(1-3) DNA appears to be associated with its ability to restore the telomere-lengthening phenotype in cdc13-1 cells. These results indicate that Gbp2p is involved in modulating telomere length.","authors":"Pang TL, Wang CY, Hsu CL, Chen MY, Lin JJ","authors_abbrev":"Pang TL et al.","pubmed_publication_date":"14 Mar 2003","pubmed_entrez_date":"2003-01-10","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ632015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.49"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20396879","title":"The gld1+ gene encoding glycerol dehydrogenase is required for glycerol metabolism in Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2010 Jun;87(2):715-27","abstract":"The budding yeast Saccharomyces cerevisiae is able to utilize glycerol as the sole carbon source via two pathways (glycerol 3-phosphate pathway and dihydroxyacetone [DHA] pathway). In contrast, the fission yeast Schizosaccharomyces pombe does not grow on media containing glycerol as the sole carbon source. However, in the presence of other carbon sources such as galactose and ethanol, S. pombe could assimilate glycerol and glycerol was preferentially utilized over ethanol and galactose. No equivalent of S. cerevisiae Gcy1/glycerol dehydrogenase has been identified in S. pombe. However, we identified a gene in S. pombe, SPAC13F5.03c (gld1 (+)), that is homologous to bacterial glycerol dehydrogenase. Deletion of gld1 caused a reduction in glycerol dehydrogenase activity and prevented glycerol assimilation. The gld1 Delta cells grew on 50 mM DHA as the sole carbon source, indicating that the glycerol dehydrogenase encoded by gld1 (+) is essential for glycerol assimilation in S. pombe. Strains of S. pombe deleted for dak1 (+) and dak2 (+) encoding DHA kinases could not grow on glycerol and showed sensitivity to a higher concentration of DHA. The dak1 Delta strain showed a more severe reduction of growth on glycerol and DHA than the dak2 Delta strain because the expression of dak1 (+) mRNA was higher than that of dak2 (+). In wild-type S. pombe, expression of the gld1 (+), dak1 (+), and dak2 (+) genes was repressed at a high concentration of glucose and was derepressed during glucose starvation. We found that gld1 (+) was regulated by glucose repression and that it was derepressed in scr1 Delta and tup12 Delta strains.","doi":"10.1007/s00253-010-2586-3","authors":"Matsuzawa T, Ohashi T, Hosomi A, Tanaka N, Tohda H, Takegawa K","authors_abbrev":"Matsuzawa T et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-04-17","publication_year":"2010","canto_session_key":"61ec82b0253ebca5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-15 08:00:47","canto_approved_date":"2026-05-27 12:25:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-04 09:15:19","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.11","SPAC977.16c","SPBC1D7.02c","SPAC18B11.10","SPAC630.14c","SPAC13F5.03c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-09-15"},{"uniquename":"PMID:32692956","title":"Bioinformatical dissection of fission yeast DNA replication origins.","citation":"Open Biol 2020 Jul;10(7):200052","abstract":"Replication origins in eukaryotes form a base for assembly of the pre-replication complex (pre-RC), thereby serving as an initiation site of DNA replication. Characteristics of replication origin vary among species. In fission yeast  Schizosaccharomyces pombe , DNA of high AT content is a distinct feature of replication origins; however, it remains to be understood what the general molecular architecture of fission yeast origin is. Here, we performed ChIP-seq mapping of Orc4 and Mcm2, two representative components of the pre-RC, and described the characteristics of their binding sites. The analysis revealed that fission yeast efficient origins are associated with two similar but independent features: a ≥15 bp-long motif with stretches of As and an AT-rich region of a few hundred bp. The A-rich motif was correlated with chromosomal binding of Orc, a DNA-binding component in the pre-RC, whereas the AT-rich region was associated with efficient binding of the DNA replicative helicase Mcm. These two features, in combination with the third feature, a transcription-poor region of approximately 1 kb, enabled to distinguish efficient replication origins from the rest of chromosome arms with high accuracy. This study, hence, provides a model that describes how multiple functional elements specify DNA replication origins in fission yeast genome.","doi":"10.1098/rsob.200052","authors":"Masuda K, Renard-Guillet C, Shirahige K, Sutani T","authors_abbrev":"Masuda K et al.","pubmed_publication_date":"Jul 2020","pubmed_entrez_date":"2020-07-22","publication_year":"2020","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2020-07-23 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9461438","title":"Fission yeast Slp1: an effector of the Mad2-dependent spindle checkpoint.","citation":"Science 1998 Feb 13;279(5353):1045-7","abstract":"Mad2 is a component of the spindle checkpoint, which delays the onset of anaphase until all chromosomes are attached to the spindle. Mad2 formed a complex with Slp1, a WD (tryptophan-aspartic acid)-repeat protein essential for the onset of anaphase. When the physical interaction between the two proteins was disrupted, the spindle checkpoint was no longer functional. Post-anaphase events such as chromosome decondensation and the next round of DNA replication were not delayed even when the spindle assembly was incomplete. This relief of dependence appears to be a result of deregulation of ubiquitin-dependent proteolysis mediated by the anaphase-promoting complex.","authors":"Kim SH, Lin DP, Matsumoto S, Kitazono A, Matsumoto T","authors_abbrev":"Kim SH et al.","pubmed_publication_date":"13 Feb 1998","pubmed_entrez_date":"1998-03-07","publication_year":"1998","canto_session_key":"3396ece82c387533","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPBC106.09","SPAC6F12.15c","SPAC821.08c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:4758902","title":"Rates of synthesis of ribosomal protein and total ribonucleic acid through the cell cycle of the fission yeast Schizosaccharomyces pombe.","citation":"Exp Cell Res 1973 Oct;81(2):269-78","abstract":"","authors":"Wain WH, Staatz WD","authors_abbrev":"Wain WH et al.","pubmed_publication_date":"Oct 1973","pubmed_entrez_date":"1973-10-01","publication_year":"1973","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17043220","title":"UV irradiation induces a postreplication DNA damage checkpoint.","citation":"Proc Natl Acad Sci U S A 2006 Oct 24;103(43):15877-82","abstract":"Eukaryotic cells irradiated with high doses of UV exhibit cell-cycle responses referred to as G(1)/S, intraS, and G(2)/M checkpoints. After a moderate UV dose that approximates sunlight exposure and is lethal to fission yeast checkpoint mutants, we found unexpectedly that these cell-cycle responses do not occur. Instead, cells at all stages of the cell cycle carry lesions into S phase and delay cell-cycle progression for hours after the completion of bulk DNA synthesis. Both DNA replication and the checkpoint kinase, Chk1, are required to generate this cell-cycle response. UV-irradiation of Deltachk1 cells causes chromosome damage and loss of viability only after cells have replicated irradiated DNA and entered mitosis. These data suggest that an important physiological role of the cell-cycle response to UV is to provide time for postreplication repair.","authors":"Callegari AJ, Kelly TJ","authors_abbrev":"Callegari AJ et al.","pubmed_publication_date":"24 Oct 2006","pubmed_entrez_date":"2006-10-18","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36253460","title":"Fold-change of chromatin condensation in yeast is a conserved property.","citation":"Sci Rep 2022 Oct 17;12(1):17393","abstract":"During mitosis, chromatin is condensed and organized into mitotic chromosomes. Condensation is critical for genome stability and dynamics, yet the degree of condensation is significantly different between multicellular and single-cell eukaryotes. What is less clear is whether there is a minimum degree of chromosome condensation in unicellular eukaryotes. Here, we exploited two-photon microscopy to analyze chromatin condensation in live and fixed cells, enabling studies of some organisms that are not readily amenable to genetic modification. This includes the yeasts Saccharomyces cerevisiae, Schizosaccharomyces pombe, Kluyveromyces lactis, and Candida albicans, as well as a protist Trypanosoma brucei. We found that mitotic chromosomes in this range of species are condensed about 1.5-fold relative to interphase chromatin. In addition, we used two-photon microscopy to reveal that chromatin reorganization in interphase human hepatoma cells infected by the hepatitis C virus is decondensed compared to uninfected cells, which correlates with the previously reported viral-induced changes in chromatin dynamics. This work demonstrates the power of two-photon microscopy to analyze chromatin in a broad range of cell types and conditions, including non-model single-cell eukaryotes. We suggest that similar condensation levels are an evolutionarily conserved property in unicellular eukaryotes and important for proper chromosome segregation. Furthermore, this provides new insights into the process of chromatin condensation during mitosis in unicellular organisms as well as the response of human cells to viral infection.","doi":"10.1038/s41598-022-22340-8","authors":"Yamin K, Bijlani S, Berman J, Soni A, Shlomai J, Buragohain BM, Werbner M, Gal-Tanamy M, Matityahu A, Onn I","authors_abbrev":"Yamin K et al.","pubmed_publication_date":"17 Oct 2022","pubmed_entrez_date":"2022-10-17","publication_year":"2022","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2022-10-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30867290","title":"Molecular basis of chromatin remodeling by Rhp26, a yeast CSB ortholog.","citation":"Proc Natl Acad Sci U S A 2019 Mar 26;116(13):6120-6129","abstract":"CSB/ERCC6 belongs to an orphan subfamily of SWI2/SNF2-related chromatin remodelers and plays crucial roles in gene expression, DNA damage repair, and the maintenance of genome integrity. The molecular basis of chromatin remodeling by Cockayne syndrome B protein (CSB) is not well understood. Here we investigate the molecular mechanism of chromatin remodeling by Rhp26, a  Schizosaccharomyces pombe  CSB ortholog. The molecular basis of chromatin remodeling and nucleosomal epitope recognition by Rhp26 is distinct from that of canonical chromatin remodelers, such as imitation switch protein (ISWI). We reveal that the remodeling activities are bidirectionally regulated by CSB-specific motifs: the N-terminal leucine-latch motif and the C-terminal coupling motif. Rhp26 remodeling activities depend mainly on H4 tails and to a lesser extent on H3 tails, but not on H2A and H2B tails. Rhp26 promotes the disruption of histone cores and the release of free DNA. Finally, we dissected the distinct contributions of two Rhp26 C-terminal regions to chromatin remodeling and DNA damage repair.","doi":"10.1073/pnas.1818163116","authors":"Wang W, Xu J, Limbo O, Fei J, Kassavetis GA, Chong J, Kadonaga JT, Russell P, Li B, Wang D","authors_abbrev":"Wang W et al.","pubmed_publication_date":"26 Mar 2019","pubmed_entrez_date":"2019-03-15","publication_year":"2019","canto_session_key":"2e077f148f258ebb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-03-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1852603","title":"Cloning and characterisation of the rad9 DNA repair gene from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1991 Jul 11;19(13):3525-31","abstract":"The rad9.192 DNA repair mutant from the fission yeast, Schizosaccharomyces pombe, is sensitive to both UV and ionising radiation. The rad9 gene has been cloned by complementation of the gamma-ray sensitivity of the mutant cell line. A 4.3 kb HindIII fragment was found to confer resistance to both types of radiation. The region of complementation was further localised to a 2.6 kb HindIII-EcoRV fragment, which, by DNA sequence analysis, was found to contain sequences capable of coding for a 427 amino acid protein, if three introns were postulated to remove stop codons. The introns were confirmed by sequence analysis of cDNA clones and PCR products derived from cDNA. The product of transcription is a 1.6 kb mRNA of low abundance. The putative rad9 protein shows no homology to any published sequence. A truncated protein is capable of complementing the radiation sensitivity of the rad9.192 mutant. Deletion of the gene is not lethal and the null allele has a similar phenotype to the rad9.192 mutant.","authors":"Murray JM, Carr AM, Lehmann AR, Watts FZ","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"11 Jul 1991","pubmed_entrez_date":"1991-07-11","publication_year":"1991","canto_session_key":"88c64b1e9fde06c2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-01-28 17:40:02","canto_approved_date":"2024-04-04 13:49:35","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-01-24 17:45:17","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-28"},{"uniquename":"PMID:26246046","title":"Nucleotide sequence composition adjacent to intronic splice sites improves splicing efficiency via its effect on pre-mRNA local folding in fungi.","citation":"RNA 2015 Oct;21(10):1704-18","abstract":"RNA splicing is the central process of intron removal in eukaryotes known to regulate various cellular functions such as growth, development, and response to external signals. The canonical sequences indicating the splicing sites needed for intronic boundary recognition are well known. However, the roles and evolution of the local folding of intronic and exonic sequence features adjacent to splice sites has yet to be thoroughly studied. Here, focusing on four fungi (Saccharomyces cerevisiae, Schizosaccharomyces pombe, Aspergillus nidulans, and Candida albicans), we performed for the first time a comprehensive high-resolution study aimed at characterizing the encoding of intronic splicing efficiency in pre-mRNA transcripts and its effect on intron evolution. Our analysis supports the conjecture that pre-mRNA local folding strength at intronic boundaries is under selective pressure, as it significantly affects splicing efficiency. Specifically, we show that in the immediate region of 12-30 nucleotides (nt) surrounding the intronic donor site there is a preference for weak pre-mRNA folding; similarly, in the region of 15-33 nt surrounding the acceptor and branch sites there is a preference for weak pre-mRNA folding. We also show that in most cases there is a preference for strong pre-mRNA folding further away from intronic splice sites. In addition, we demonstrate that these signals are not associated with gene-specific functions, and they correlate with splicing efficiency measurements (r = 0.77, P = 2.98 × 10(-21)) and with expression levels of the corresponding genes (P = 1.24 × 10(-19)). We suggest that pre-mRNA folding strength in the above-mentioned regions has a direct effect on splicing efficiency by improving the recognition of intronic boundaries. These new discoveries are contributory steps toward a broader understanding of splicing regulation and intronic/transcript evolution.","doi":"10.1261/rna.051268.115","authors":"Zafrir Z, Tuller T","authors_abbrev":"Zafrir Z et al.","pubmed_publication_date":"Oct 2015","pubmed_entrez_date":"2015-08-07","publication_year":"2015","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-08-09 00:19:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12074602","title":"Fibrillarin binds to a 3' cis-regulatory element in pre-mRNA of uvi15+ in fission yeast.","citation":"Biochem Biophys Res Commun 2002 Jun 28;294(5):1184-90","abstract":"uvi15+ is induced by various stresses including exposure to UV-light. Previously, we demonstrated that the UV-induction is mainly regulated at the post-transcriptional level through a cis-acting element in the pre-mRNA. Here we show that deletion analyses define an 18-nt element responsible for the UV-induction. RNA gel mobility shift assay showed that a specific protein(s) could form a complex with the 54-nt element but its binding ability is moderately decreased in response to UV-light. Using yeast three-hybrid screen, we isolated a homolog of fibrillarin as a protein interacting with the 54-nt element, which is a key nucleolar protein for pre-rRNA processing. We further showed that the recombinant fibrillarin specifically binds to the element in a sequence-specific manner. Thus, the data suggest that fission yeast fibrillarin might regulate uvi15+ mRNA stability via binding with the 54-nt element in the pre-mRNA, implying that fibrillarin is involved in both pre-mRNA and pre-rRNA processing.","authors":"Jang YK, Kim M, Dai Park S","authors_abbrev":"Jang YK et al.","pubmed_publication_date":"28 Jun 2002","pubmed_entrez_date":"2002-06-21","publication_year":"2002","canto_session_key":"d1e54bf1d660f4c8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-01-20 17:17:26","canto_approved_date":"2023-04-18 09:06:43","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-01-20 16:55:19","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.10c","SPBC649.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-01-20"},{"uniquename":"PMID:25401760","title":"RNase MRP cleaves pre-tRNASer-Met in the tRNA maturation pathway.","citation":"PLoS One 2014;9(11):e112488","abstract":"Ribonuclease mitochondrial RNA processing (RNase MRP) is a multifunctional ribonucleoprotein (RNP) complex that is involved in the maturation of various types of RNA including ribosomal RNA. RNase MRP consists of a potential catalytic RNA and several protein components, all of which are required for cell viability. We show here that the temperature-sensitive mutant of rmp1, the gene for a unique protein component of RNase MRP, accumulates the dimeric tRNA precursor, pre-tRNA(Ser-Met). To examine whether RNase MRP mediates tRNA maturation, we purified the RNase MRP holoenzyme from the fission yeast Schizosaccharomyces pombe and found that the enzyme directly and selectively cleaves pre-tRNA(Ser-Met), suggesting that RNase MRP participates in the maturation of specific tRNA in vivo. In addition, mass spectrometry-based ribonucleoproteomic analysis demonstrated that this RNase MRP consists of one RNA molecule and 11 protein components, including a previously unknown component Rpl701. Notably, limited nucleolysis of RNase MRP generated an active catalytic core consisting of partial mrp1 RNA fragments, which constitute \"Domain 1\" in the secondary structure of RNase MRP, and 8 proteins. Thus, the present study provides new insight into the structure and function of RNase MRP.","doi":"10.1371/journal.pone.0112488","authors":"Saito Y, Takeda J, Adachi K, Nobe Y, Kobayashi J, Hirota K, Oliveira DV, Taoka M, Isobe T","authors_abbrev":"Saito Y et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-11-18","publication_year":"2014","canto_session_key":"b843e3d2a1c6edd0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masato Taoka","canto_first_approved_date":"2018-02-13 15:11:18","canto_approved_date":"2023-04-14 16:23:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-13 16:25:37","canto_added_date":"2014-11-19 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":47,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Masato Taoka","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.04c","SPAC6C3.09","SPCC16C4.19","SPCC830.09c","SPBP8B7.01c","SPAC323.08","SPCC16C4.05","SPNCRNA.82","SPAC25B8.16","SPBC1709.20","SPBC1703.01c","SPBC18H10.12c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2018-02-13"},{"uniquename":"PMID:14988732","title":"Roles of histone acetylation and chromatin remodeling factor in a meiotic recombination hotspot.","citation":"EMBO J 2004 Apr 21;23(8):1792-803","abstract":"Histone acetyltransferases (HATs) and ATP-dependent chromatin remodeling factors (ADCRs) are involved in selective gene regulation via modulation of local chromatin configuration. Activation of the recombination hotspot ade6-M26 of Schizosaccharomyces pombe is mediated by a cAMP responsive element (CRE)-like sequence, M26, and a heterodimeric ATF/CREB transcription factor, Atf1.Pcr1. Chromatin remodeling occurs meiotically around M26. We examined the roles of HATs and ADCRs in chromatin remodeling around M26. Histones H3 and H4 around M26 were hyperacetylated in an M26- and Atf1-dependent manner early in meiosis. SpGcn5, the S. pombe homolog of Gcn5p, was required for the majority of histone H3 acetylation around M26 in vivo. Deletion of gcn5+ caused a significant delay in chromatin remodeling but only partial reduction of M26 meiotic recombination frequency. The snf22+ (a Swi2/Snf2-ADCR homologue) deletion and snf22+ gcn5+ double deletion abolished chromatin remodeling and significant reduction of meiotic recombination around M26. These results suggest that HATs and ADCRs cooperatively alter local chromatin structure, as in selective transcription activation, to activate meiotic recombination at M26 in a site-specific manner.","authors":"Yamada T, Mizuno K, Hirota K, Kon N, Wahls WP, Hartsuiker E, Murofushi H, Shibata T, Ohta K","authors_abbrev":"Yamada T et al.","pubmed_publication_date":"21 Apr 2004","pubmed_entrez_date":"2004-02-28","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.05"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:10617635","title":"Protein farnesylation is critical for maintaining normal cell morphology and canavanine resistance in Schizosaccharomyces pombe.","citation":"J Biol Chem 2000 Jan 07;275(1):429-38","abstract":"Protein farnesyltransferase (FTase) plays important roles in the growth and differentiation of eukaryotic cells. In this paper, we report the identification of the Schizosaccharomyces pombe gene cpp1(+) encoding the beta-subunit of FTase. The predicted amino acid sequence of the cpp1(+) gene product shares significant similarity with FTase beta-subunits from a variety of organisms. S. pombe FTase purified from E. coli exhibits high enzymatic activity toward the CAAX farnesylation motif substrates (where C represents cysteine, A represents aliphatic amino acid, and X is preferentially methionine, cysteine, serine, alanine, or glutamine) while showing little preference for CAAL geranylgeranylation motif substrates (where L represents leucine or phenylalanine). cpp1(+) is not essential for growth as shown by gene disruption; however, mutant cells exhibit rounded or irregular cell morphology. Expression of a geranylgeranylated mutant form, Ras1-CVIL, which can bypass farnesylation, rescues these morphological defects. We also identify a novel phenotype of cpp1(-) mutants, hypersensitivity to canavanine. This appears to be due to a 3-4-fold increase in the rate of arginine uptake as compared with wild-type cells. Expression of the geranylgeranylated mutant form of a novel farnesylated small GTPase, SpRheb, is able to suppress the elevated arginine uptake rate. These results demonstrate that protein farnesylation is critical for maintaining normal cell morphology through Ras1 and canavanine resistance through SpRheb.","authors":"Yang W, Urano J, Tamanoi F","authors_abbrev":"Yang W et al.","pubmed_publication_date":"07 Jan 2000","pubmed_entrez_date":"2000-01-05","publication_year":"2000","canto_session_key":"ca7148fa667c9c93","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-05 08:40:37","canto_approved_date":"2022-01-16 09:23:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-06 15:46:07","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.04c","SPAC23C4.08","SPAC17H9.09c","SPAC17G6.04c","SPBC428.16c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2015-05-05"},{"uniquename":"EMBL:SPD134","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37913773","title":"TOR inactivation triggers heterochromatin formation in rDNA during glucose starvation.","citation":"Cell Rep 2023 Nov 28;42(11):113320","abstract":"In response to environmental cues, such as nutrient starvation, living organisms modulate gene expression through mechanisms involving histone modifications. Specifically, nutrient depletion inactivates the TOR (target of rapamycin) pathway, leading to reduced expression of ribosomal genes. While these regulatory mechanisms are well elucidated in budding yeast Saccharomyces cerevisiae, their conservation across diverse organisms remains unclear. In this study, we demonstrate that fission yeast Schizosaccharomyces pombe cells repress ribosomal gene transcription through a different mechanism. TORC1, which accumulates in the rDNA region, dissociates upon starvation, resulting in enhanced methylation of H3K9 and heterochromatin formation, facilitated by dissociation of the stress-responsive transcription factor Atf1 and accumulation of the histone chaperone FACT. We propose that this mechanism might be adapted in mammals that possess Suv39H1 and HP1, which are absent in budding yeast.","doi":"10.1016/j.celrep.2023.113320","authors":"Hirai H, Sen Y, Tamura M, Ohta K","authors_abbrev":"Hirai H et al.","pubmed_publication_date":"28 Nov 2023","pubmed_entrez_date":"2023-11-01","publication_year":"2023","canto_session_key":"1c51e41628bda782","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hayato Hirai","canto_first_approved_date":"2024-01-18 14:33:36","canto_approved_date":"2024-04-02 15:09:56","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-01-16 02:07:32","canto_added_date":"2023-11-03 00:25:05","annotation_curators":[{"name":"Hayato Hirai","community_curator":true,"annotation_count":27,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.11","SPBC30D10.18c","SPAC1952.05","SPAC140.02","SPBC609.05","SPAC664.06","SPAC57A7.11","SPCC4G3.08","SPBC4C3.05c","SPBC216.07c","SPBC29B5.01","SPBC428.08c"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2024-01-18"},{"uniquename":"PMID:32101745","title":"Dense Transposon Integration Reveals Essential Cleavage and Polyadenylation Factors Promote Heterochromatin Formation.","citation":"Cell Rep 2020 Feb 25;30(8):2686-2698.e8","abstract":"Heterochromatin functions as a scaffold for factors responsible for gene silencing and chromosome segregation. Heterochromatin can be assembled by multiple pathways, including RNAi and RNA surveillance. We identified factors that form heterochromatin using dense profiles of transposable element integration in Schizosaccharomyces pombe. The candidates include a large number of essential proteins such as four canonical mRNA cleavage and polyadenylation factors. We find that Iss1, a subunit of the poly(A) polymerase module, plays a role in forming heterochromatin in centromere repeats that is independent of RNAi. Genome-wide maps reveal that Iss1 accumulates at genes regulated by RNA surveillance. Iss1 interacts with RNA surveillance factors Mmi1 and Rrp6, and importantly, Iss1 contributes to RNA elimination that forms heterochromatin at meiosis genes. Our profile of transposable element integration supports the model that a network of mRNA cleavage and polyadenylation factors coordinates RNA surveillance, including the mechanism that forms heterochromatin at meiotic genes.","doi":"10.1016/j.celrep.2020.01.094","authors":"Lee SY, Hung S, Esnault C, Pathak R, Johnson KR, Bankole O, Yamashita A, Zhang H, Levin HL","authors_abbrev":"Lee SY et al.","pubmed_publication_date":"25 Feb 2020","pubmed_entrez_date":"2020-02-27","publication_year":"2020","canto_session_key":"87f689d02b0fb234","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-08-25 11:04:05","canto_approved_date":"2024-02-04 10:40:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-08-04 20:21:53","canto_added_date":"2020-02-28 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":198,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_32101745_phaf.tsv"}],"genes":["SPBC4F6.06","SPAC1B3.14","SPBC83.07","SPAC959.08","SPAC694.06c","SPCC1827.04","SPBC30D10.16","SPAC17G6.16c","SPAC57A10.09c","SPAC3H1.04c","SPCP1E11.11","SPAC694.04c","SPAC23H3.09c","SPAC2G11.06","SPBC19G7.02","SPAC13F5.02c","SPAC6F12.09","SPAC1834.02","SPAC22F8.04","SPBC1D7.01","SPBC24C6.04","SPBC646.02","SPCC1494.07","SPCC4B3.17","SPAC16.03c","SPAC3F10.02c","SPAC1782.03","SPAC2C4.03c","SPAC31A2.12","SPCC16C4.19","SPBC23G7.12c","SPBC21D10.09c","SPAC12G12.15","SPAPB1A10.03","SPAC3A12.11c","SPAC6F12.17","SPAC890.06","SPAC17G8.02","SPCC1393.05","SPAC17H9.12c","SPCC1281.01","SPAC16E8.11c","SPCC364.03","SPAC1783.05","SPAC22H10.03c","SPAC16.02c","SPBC405.07","SPBC577.06c","SPAC2E1P5.05","SPBC28F2.12","SPAC2F7.04","SPAP8A3.07c","SPAC2G11.14","SPAC2F3.06c","SPAC29B12.02c","SPCC736.12c","SPAC57A10.12c","SPAC688.08","SPAC1F3.01","SPCC736.11","SPAC3H8.08c","SPCC188.04c","SPBP8B7.20c","SPAC1805.15c","SPAP8A3.06","SPAC22G7.02","SPAC1F12.05","SPBC691.02c","SPAC31G5.01","SPBC1198.04c","SPAC4G9.13c","SPBC16D10.07c","SPAC3H1.12c","SPAC14C4.11","SPBC902.05c","SPAC1751.03","SPAC18G6.02c","SPCC553.08c","SPAC19E9.03","SPBC776.01","SPAC13D6.02c","SPBC56F2.08c","SPBC6B1.06c","SPAC2F7.05c","SPCC31H12.05c","SPAC1039.10","SPAC3H5.07","SPAC144.05","SPBC29A10.10c","SPBP19A11.06","SPCC188.13c","SPAC29B12.01","SPAPB17E12.13","SPBP4G3.03","SPAC23G3.09","SPAC3G9.10c","SPBC28E12.04","SPBC1347.02","SPBC83.02c","SPCC569.05c","SPAC23E2.01","SPCC970.03","SPBC17G9.03c","SPAC11E3.04c","SPAC3G9.03","SPCC16C4.22","SPAC19D5.01","SPAC57A10.02","SPBC16A3.08c","SPAC6G9.09c","SPAC4F10.03c","SPBC4F6.14","SPCC63.06","SPCC1682.14","SPAC1093.05","SPAC1142.04","SPAC3F10.08c","SPCC11E10.08","SPBC11G11.03","SPBP8B7.21","SPBC839.04","SPBC582.04c","SPBC83.03c","SPCC1322.01","SPBC119.13c","SPAC140.02","SPAC29A4.18","SPAC27D7.13c","SPBC2A9.04c","SPAC26F1.04c","SPCC16C4.01","SPAC22G7.10","SPBPB8B6.04c","SPAC1F7.07c","SPAC26H5.03","SPCC1322.04","SPBC839.08c","SPAC24B11.05","SPAC806.06c","SPAC6B12.15","SPAC27F1.06c","SPAC1B3.17","SPBC11C11.09c","SPAC22F3.09c","SPBC27B12.13","SPBC660.15","SPAC23G3.06","SPAC57A10.14","SPAC16.04","SPAC22G7.09c","SPBC651.01c","SPAC9.02c","SPAC56E4.03","SPCC162.04c","SPAC22G7.06c","SPCC10H11.01","SPBP16F5.02","SPAC1D4.11c","SPBP8B7.03c","SPAC664.01c","SPBP8B7.19","SPAC26A3.01","SPBC13G1.09","SPBC577.03c","SPAC4F10.09c","SPBC609.05","SPAC1783.08c","SPAC13A11.04c","SPBC14C8.12","SPBP35G2.10","SPAP14E8.02","SPBC11C11.05","SPAC23C11.13c","SPAC589.06c","SPBC4.07c","SPBC32H8.11","SPAC19B12.13","SPBC4.05","SPAC19G12.06c","SPBC4F6.04","SPAC926.03","SPBC800.08","SPBC646.04","SPAC458.07","SPBC1921.03c","SPBPJ4664.04","SPCC613.01","SPAC644.06c","SPBC30D10.14","SPAC17G8.05","SPBC1306.01c","SPAC869.11","SPAC110.04c","SPAC27E2.09","SPBC1706.01","SPBC776.11","SPBC1604.05","SPAC1805.05","SPAC1250.07","SPCC16C4.08c","SPCC330.14c","SPAC1952.13","SPAC30D11.14c"],"gene_count":203,"ltp_gene_count":199,"approved_date":"2020-08-25"},{"uniquename":"PMID:28631611","title":"The gene family that cheats Mendel.","citation":"Elife 2017 Jun 20;6","abstract":"Some alleles of the  wtf  gene family can increase their chances of spreading by using poisons to kill other alleles, and antidotes to save themselves.","doi":"10.7554/eLife.28567","authors":"Shropshire JD, Rokas A","authors_abbrev":"Shropshire JD et al.","pubmed_publication_date":"20 Jun 2017","pubmed_entrez_date":"2017-06-21","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-06-22 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10226032","title":"Cdc2 activation in fission yeast depends on Mcs6 and Csk1, two partially redundant Cdk-activating kinases (CAKs).","citation":"Curr Biol 1999 Apr 22;9(8):441-4","abstract":"Cyclin-dependent kinases (Cdks) are fully active only when phosphorylated by a Cdk-activating kinase (CAK) [1]. Metazoan CAK is itself a Cdk, Cdk7, whereas the CAK of Saccharomyces cerevisiae is a distinct enzyme unrelated to Cdks [1]. The Mcs6-Mcs2 complex of Schizosaccharomyces pombe is a putative CAK related to the metazoan enzyme [2] [3]. Although the loss of Mcs6 is lethal, it results in a phenotype that is inconsistent with a failure to activate Cdc2, the major Cdk in S. pombe [3]. We therefore tested the ability of Csk1, a putative regulator of Mcs6 [4], to activate Cdk-cyclin complexes in vitro. Csk1 activated both the monomeric and the Mcs2-bound forms of Mcs6. Surprisingly, Csk1 also activated Cdc2 in complexes with either Cdc13 or Cig2 cyclins. When a double mutant carrying a csk1 deletion and a temperature-sensitive mcs6 allele was incubated at the restrictive temperature, Cdc2 was not activated and the cells underwent a cell division arrest prior to mitosis. Cdc2-cyclin complexes isolated from the arrested cells could be activated in vitro by recombinant CAK, whereas complexes from wild-type cells or either of the single mutants were refractory to activation. Thus, fission yeast contains two partially redundant CAKs: the Mcs6-Mcs2 complex and Csk1. Inactivation of both CAKs is necessary and sufficient to prevent Cdc2 activation and cause a cell-cycle arrest. Mcs6, which is essential, may therefore have required functions other than Cdk activation.","authors":"Lee KM, Saiz JE, Barton WA, Fisher RP","authors_abbrev":"Lee KM et al.","pubmed_publication_date":"22 Apr 1999","pubmed_entrez_date":"1999-05-05","publication_year":"1999","canto_session_key":"615084ae39833661","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-05-19 17:45:56","canto_approved_date":"2026-06-15 16:52:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-11 20:59:40","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.06c","SPBC11B10.09","SPBP16F5.02","SPBC19F8.07"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-05-19"},{"uniquename":"PMID:10512858","title":"The Schizosaccharomyces pombe hst4(+) gene is a SIR2 homologue with silencing and centromeric functions.","citation":"Mol Biol Cell 1999 Oct;10(10):3171-86","abstract":"Although silencing is a significant form of transcriptional regulation, the functional and mechanistic limits of its conservation have not yet been established. We have identified the Schizosaccharomyces pombe hst4(+) gene as a member of the SIR2/HST silencing gene family that is defined in organisms ranging from bacteria to humans. hst4Delta mutants grow more slowly than wild-type cells and have abnormal morphology and fragmented DNA. Mutant strains show decreased silencing of reporter genes at both telomeres and centromeres. hst4(+) appears to be important for centromere function as well because mutants have elevated chromosome-loss rates and are sensitive to a microtubule-destabilizing drug. Consistent with a role in chromatin structure, Hst4p localizes to the nucleus and appears concentrated in the nucleolus. hst4Delta mutant phenotypes, including growth and silencing phenotypes, are similar to those of the Saccharomyces cerevisiae HSTs, and at a molecular level, hst4(+) is most similar to HST4. Furthermore, hst4(+) is a functional homologue of S. cerevisiae HST3 and HST4 in that overexpression of hst4(+) rescues the temperature-sensitivity and telomeric silencing defects of an hst3Delta hst4Delta double mutant. These results together demonstrate that a SIR-like silencing mechanism is conserved in the distantly related yeasts and is likely to be found in other organisms from prokaryotes to mammals.","authors":"Freeman-Cook LL, Sherman JM, Brachmann CB, Allshire RC, Boeke JD, Pillus L","authors_abbrev":"Freeman-Cook LL et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-10-08","publication_year":"1999","canto_session_key":"823e9b738ae02f17","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-07-21 14:52:38","canto_approved_date":"2020-06-19 11:15:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-20 13:43:19","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-07-21"},{"uniquename":"PMID:1944266","title":"The fission yeast dis3+ gene encodes a 110-kDa essential protein implicated in mitotic control.","citation":"Mol Cell Biol 1991 Dec;11(12):5839-47","abstract":"The fission yeast mutant dis3-54 is defective in mitosis and fails in chromosome disjunction. Its phenotype is similar to that of dis2-11, a mutant with a mutation in the type 1 protein phosphatase gene. We cloned the dis3+ gene by transformation. Nucleotide sequencing predicts a coding region of 970 amino acids interrupted by a 164-bp intron at the 65th codon. The predicted dis3+ protein shares a weak but significant similarity with the budding yeast SSD1 or SRK1 gene product, the gene for which is a suppressor for the absence of a protein phosphatase SIT4 gene or the BCY1 regulatory subunit of cyclic AMP-dependent protein kinase. Anti-dis3 antibodies recognized the 110-kDa dis3+ gene product, which is part of a 250- to 350-kDa oligomer and is enriched in the nucleus. The cellular localization of the dis3+ protein is reminiscent of that of the dis2+ protein, but these two proteins do not form a complex. A type 1 protein phosphatase activity in the dis3-54 mutant extracts is apparently not affected. The dis3+ gene is essential for growth; gene disruptant cells do not germinate and fail in cell division. Increased dis3+ gene dosage reverses the Ts+ phenotype of a cdc25 wee1 strain, as does increased type 1 protein phosphatase gene dosage. Double mutant dis3 dis2 is lethal even at the permissive temperature, suggesting that the dis2+ and dis3+ genes may be functionally overlapped. The role of the dis3+ gene product in mitosis is unknown, but this gene product may be directly or indirectly involved in the regulation of mitosis.","authors":"Kinoshita N, Goebl M, Yanagida M","authors_abbrev":"Kinoshita N et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"35c498b7a5ea246c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-10-12 10:44:04","canto_approved_date":"2019-06-14 12:45:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-22 16:53:15","canto_added_date":"2012-02-24 05:55:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":43,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.12c","SPBC26H8.10","SPBC16H5.07c","SPCC31H12.05c","SPAC24H6.05","SPBC776.02c","SPCC736.14","SPCC18B5.03","SPBC646.13"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-10-12"},{"uniquename":"PMID:35770973","title":"Adaptor linked K63 di-ubiquitin activates Nedd4/Rsp5 E3 ligase.","citation":"Elife 2022 Jun 30;11","abstract":"Nedd4/Rsp5 family E3 ligases mediate numerous cellular processes, many of which require the E3 ligase to interact with PY motif containing adaptor proteins. Several arrestin-related trafficking adaptors (ARTs) of Rsp5 were self-ubiquitinated for activation, but the regulation mechanism remains elusive. Remarkably, we demonstrate that Art1, Art4, and Art5 undergo K63-linked di-ubiquitination by Rsp5. This modification enhances the plasma membrane recruitment of Rsp5 by Art1 or Art5 upon substrate induction, required for cargo protein ubiquitination. In agreement with these observations, we find that di-ubiquitin strengthens the interaction between the pombe orthologs of Rsp5 and Art1, Pub1, and Any1. Furthermore, we discover that the homologous to E6AP C-terminus (HECT) domain exosite protects the K63-linked di-ubiquitin on the adaptors from cleavage by the deubiquitination enzyme Ubp2. Together, our study uncovers a novel ubiquitination modification implemented by Rsp5 adaptor proteins, underscoring the regulatory mechanism of how adaptor proteins control the recruitment, and activity of Rsp5 for the turnover of membrane proteins.","doi":"10.7554/eLife.77424","authors":"Zhu L, Zhang Q, Cordeiro CD, Banjade S, Sardana R, Mao Y, Emr SD","authors_abbrev":"Zhu L et al.","pubmed_publication_date":"30 Jun 2022","pubmed_entrez_date":"2022-06-30","publication_year":"2022","canto_session_key":"bb777fbbcd84db01","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-07-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC18H10.20c","SPAC11G7.02"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:SPC08399","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7608113","title":"Molecular cloning and nucleotide sequencing of the gamma-glutamylcysteine synthetase gene of the fission yeast Schizosaccharomyces pombe.","citation":"J Biochem 1995 Feb;117(2):283-8","abstract":"A DNA fragment encoding gamma-glutamylcysteine synthetase [EC 6.3.2.2] of Schizosaccharomyces pombe was cloned by complementation of the cadmium hypersensitivity of a S. pombe mutant deficient in the enzyme. Sequence analysis of the cloned DNA revealed that the enzyme was consisted of 669 amino acid residues and was homologous to the enzymes of human liver, rat kidney, and Saccharomyces cerevisiae. The deduced amino acid sequence coincides with the amino acid sequences of the proteolytic peptides obtained from the purified enzyme. A cysteine residue was deduced to be important for catalytic activity by comparing the amino acid sequences of the enzymes of the four species. The gene contains one intron and the splicing point was confirmed by sequencing a cDNA amplified by PCR. Northern blot analysis showed an RNA of 2,200 bases hybridized with the cloned gene.","authors":"Mutoh N, Nakagawa CW, Hayashi Y","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_session_key":"4fbd51cd6dae75c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-10-21 13:18:50","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-05-25 16:15:11","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-05-25"},{"uniquename":"PMID:21764908","title":"Reinventing heterochromatin in budding yeasts: Sir2 and the origin recognition complex take center stage.","citation":"Eukaryot Cell 2011 Sep;10(9):1183-92","abstract":"The transcriptional silencing of the cryptic mating-type loci in Saccharomyces cerevisiae is one of the best-studied models of repressive heterochromatin. However, this type of heterochromatin, which is mediated by the Sir proteins, has a distinct molecular composition compared to the more ubiquitous type of heterochromatin found in Schizosaccharomyces pombe, other fungi, animals, and plants and characterized by the presence of HP1 (heterochromatin protein 1). This review discusses how the loss of important heterochromatin proteins, including HP1, in the budding yeast lineage presented an evolutionary opportunity for the development and diversification of alternative varieties of heterochromatin, in which the conserved deacetylase Sir2 and the replication protein Orc1 play key roles. In addition, we highlight how this diversification has been facilitated by gene duplications and has contributed to adaptations in lifestyle.","doi":"10.1128/EC.05123-11","authors":"Hickman MA, Froyd CA, Rusche LN","authors_abbrev":"Hickman MA et al.","pubmed_publication_date":"Sep 2011","pubmed_entrez_date":"2011-07-19","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34675074","title":"A rapidly reversible mutation generates subclonal genetic diversity and unstable drug resistance.","citation":"Proc Natl Acad Sci U S A 2021 Oct 26;118(43)","abstract":"Most genetic changes have negligible reversion rates. As most mutations that confer resistance to an adverse condition (e.g., drug treatment) also confer a growth defect in its absence, it is challenging for cells to genetically adapt to transient environmental changes. Here, we identify a set of rapidly reversible drug-resistance mutations in  Schizosaccharomyces pombe  that are caused by microhomology-mediated tandem duplication (MTD) and reversion back to the wild-type sequence. Using 10,000× coverage whole-genome sequencing, we identify nearly 6,000 subclonal MTDs in a single clonal population and determine, using machine learning, how MTD frequency is encoded in the genome. We find that sequences with the highest-predicted MTD rates tend to generate insertions that maintain the correct reading frame, suggesting that MTD formation has shaped the evolution of coding sequences. Our study reveals a common mechanism of reversible genetic variation that is beneficial for adaptation to environmental fluctuations and facilitates evolutionary divergence.","doi":"10.1073/pnas.2019060118","authors":"Dan L, Li Y, Chen S, Liu J, Wang Y, Li F, He X, Carey LB","authors_abbrev":"Dan L et al.","pubmed_publication_date":"26 Oct 2021","pubmed_entrez_date":"2021-10-22","publication_year":"2021","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-10-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007686","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3153181","title":"Yeast tubulin genes.","citation":"Microbiol Sci 1987 Apr;4(4):115-8","abstract":"There are two alpha-tubulin genes and one beta-tubulin gene in Schizosaccharomyces pombe and Saccharomyces cerevisiae. Detailed analyses employing tubulin mutants and cloned genes have revealed different cellular roles for the tubulin genes in these organisms.","authors":"Yanagida M","authors_abbrev":"Yanagida M","pubmed_publication_date":"Apr 1987","pubmed_entrez_date":"1987-04-01","publication_year":"1987","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21852501","title":"Aneuploidy drives genomic instability in yeast.","citation":"Science 2011 Aug 19;333(6045):1026-30","abstract":"Aneuploidy decreases cellular fitness, yet it is also associated with cancer, a disease of enhanced proliferative capacity. To investigate one mechanism by which aneuploidy could contribute to tumorigenesis, we examined the effects of aneuploidy on genomic stability. We analyzed 13 budding yeast strains that carry extra copies of single chromosomes and found that all aneuploid strains exhibited one or more forms of genomic instability. Most strains displayed increased chromosome loss and mitotic recombination, as well as defective DNA damage repair. Aneuploid fission yeast strains also exhibited defects in mitotic recombination. Aneuploidy-induced genomic instability could facilitate the development of genetic alterations that drive malignant growth in cancer.","doi":"10.1126/science.1206412","authors":"Sheltzer JM, Blank HM, Pfau SJ, Tange Y, George BM, Humpton TJ, Brito IL, Hiraoka Y, Niwa O, Amon A","authors_abbrev":"Sheltzer JM et al.","pubmed_publication_date":"19 Aug 2011","pubmed_entrez_date":"2011-08-20","publication_year":"2011","canto_session_key":"a3ba19ae15a1bb5d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-02-22 11:53:39","canto_approved_date":"2021-02-22 11:53:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-02-22 11:53:30","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-02-22"},{"uniquename":"PMID:25102102","title":"A metabolic strategy to enhance long-term survival by Phx1 through stationary phase-specific pyruvate decarboxylases in fission yeast.","citation":"Aging (Albany NY) 2014 Jul;6(7):587-601","abstract":"In the fission yeast Schizosaccharomyces pombe, the stationary phase-specific transcription factor Phx1 contributes to long-term survival, stress tolerance, and meiosis. We identified Phx1-dependent genes through transcriptome analysis, and further analyzed those related with carbohydrate and thiamine metabolism, whose expression decreased in ∆phx1. Consistent with mRNA changes, the level of thiamine pyrophosphate (TPP) and TPP-utilizing pyruvate decarboxylase activity that converts pyruvate to acetaldehyde were also reduced in the mutant. Therefore, Phx1 appears to shift metabolic flux by diverting pyruvate from the TCA cycle and respiration to ethanol fermentation. Among the four predicted genes for pyruvate decarboxylase, only the Phx1-dependent genes (pdc201+ and pdc202+) contributed to long-term survival as judged by mutation and overexpression studies. These findings indicate that the Phx1-mediated long-term survival is achieved primarily through increasing the synthesis and activity of pyruvate decarboxylase. Consistent with this hypothesis, we observed that Phx1 curtailed respiration when cells entered stationary phase. Introduction of Δphx1 mutation compromised the long-lived phenotypes of Δpka1 and Δsck2 mutants that are devoid of pro-aging kinases of nutrient-signalling pathways, and of the Δpyp1 mutant with constitutively activated stress-responsive kinase Sty1. Therefore, achievement of long-term viability through both nutrient limitation and anti-stress response appears to be dependent on Phx1.","authors":"Kim JY, Kim EJ, Lopez-Maury L, Bähler J, Roe JH","authors_abbrev":"Kim JY et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-08-08","publication_year":"2014","canto_session_key":"bcd1635bd0c34c02","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-20 02:17:57","canto_approved_date":"2025-01-15 15:35:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-08 15:18:24","canto_added_date":"2014-08-09 00:15:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F8.07c","SPAC32A11.03c","SPCC1223.02","SPBC106.10","SPAC3G9.11c","SPAC13A11.06","SPBC26H8.01","SPAC17A2.01","SPAC26F1.10c","SPAC186.09","SPAC22E12.14c"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2015-10-20"},{"uniquename":"PMID:14701811","title":"Schizosaccharomyces pombe carboxyl-terminal domain (CTD) phosphatase Fcp1: distributive mechanism, minimal CTD substrate, and active site mapping.","citation":"J Biol Chem 2004 Mar 19;279(12):10892-900","abstract":"Schizosaccharomyces pombe Fcp1 is an essential protein serine phosphatase that preferentially dephosphorylates Ser(2) of the RNA polymerase II C-terminal domain (CTD) heptad repeat Y(1)S(2)P(3)T(4)S(5)P(6)S(7). Here we show that: (i) Fcp1 acts distributively during the hydrolysis of substrates containing tandem Ser(2)-PO(4) heptads; (ii) the minimal optimal CTD substrate for Fcp1 is a single heptad of phasing S(5)P(6)S(7)Y(1)S(2)P(3)T(4); and (iii) single alanine mutations of flanking residues Tyr(1) or Pro(3) result in 6-fold decrements in CTD phosphatase activity. Fcp1 belongs to the DXDX(T/V) family of phosphotransferases that act via an acyl-phosphoenzyme intermediate. An alanine scan of 11 conserved positions of S. pombe Fcp1 identifies Thr(174), Tyr(237), Thr(243), and Tyr(249) as important for phosphatase activity. Structure-activity relationships at these positions were determined by introducing conservative substitutions. Our results, together with previous mutational studies, highlight a constellation of 11 amino acids that are conserved in all Fcp1 orthologs and likely comprise the active site.","authors":"Hausmann S, Erdjument-Bromage H, Shuman S","authors_abbrev":"Hausmann S et al.","pubmed_publication_date":"19 Mar 2004","pubmed_entrez_date":"2004-01-01","publication_year":"2004","canto_session_key":"e41d7b73c856910b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-22 11:54:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-22 11:54:36","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19B12.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-22"},{"uniquename":"PMID:30072443","title":"Involvement of the septation initiation network in events during cytokinesis in fission yeast.","citation":"J Cell Sci 2018 Aug 23;131(16)","abstract":"The septation initiation network (SIN), comprising a GTPase and a cascade of three protein kinases, regulates cell division in fission yeast  Schizosaccharomyces pombe , but questions remain about its influence on cytokinesis. Here, we made quantitative measurements of the numbers of Cdc7p kinase molecules (a marker for SIN activity) on spindle pole bodies (SPBs), and on the timing of assembly, maturation and constriction of contractile rings via six different proteins tagged with fluorescent proteins. When SIN activity is low in  spg1-106  mutant cells at 32°C, cytokinetic nodes formed contractile rings ∼3 min slower than wild-type cells. During the maturation period, these rings maintained normal levels of the myosin-II mEGFP-Myo2p but accumulated less of the F-BAR protein Cdc15p-GFP than in wild-type cells. The Cdc15p-GFP fluorescence then disintegrated into spots as mEGFP-Myo2p dissociated slowly. Some rings started to constrict at the normal time, but most failed to complete constriction. When high SIN activity persists far longer than normal on both SPBs in  cdc16-116  mutant cells at 32°C, contractile rings assembled and constricted normally, but disassembled slowly, delaying cell separation.","doi":"10.1242/jcs.216895","authors":"Dey SK, Pollard TD","authors_abbrev":"Dey SK et al.","pubmed_publication_date":"23 Aug 2018","pubmed_entrez_date":"2018-08-04","publication_year":"2018","canto_session_key":"d7acf88a8212c043","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-08-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6887244","title":"Cold-sensitive nuclear division arrest mutants of the fission yeast Schizosaccharomyces pombe.","citation":"J Mol Biol 1983 Aug 05;168(2):251-70","abstract":"Thirteen recessive cold sensitive nuclear division arrest mutants were isolated from the fission yeast Schizosaccharomyces pombe. Twelve unlinked genes were defined; six in chromosome I, three in chromosome II and two in chromosome III. The map positions of three nuclear division arrest genes (nda1, nda2 and nda3) in chromosome II were determined precisely. Together with the previously obtained temperature-sensitive cell division cycle mutations, at least 20 genes appear to control the nuclear division of the fission yeast. Physiological studies indicated that most cold sensitive nda mutants incubated previously at 22 degrees C proceeded with a synchronously normal cell-cycle after temperature shift-up. The morphology of the nuclei and nuclear chromatin region was studied by the 4',6-diamidino-2-phenylindole staining method and by electron microscopy. Each mutant exhibited characteristic nuclear morphology at 22 degrees C, showing the specific blockages. The nda genes seem to control a pathway of structural alterations in the nuclear chromatin region with the order hemisphere, condensed ellipsoid, segregating U-form and separating hemispheres. Two genes, nda2 and nda3, pleiotropically control nuclear division, nuclear location and cell shape. The terminal phenotype of nda2-KM52 is characterized by the nuclear displacement, the absence of a spindle and abnormal locations of spindle pole bodies. The cells of nda3-KM311 were aberrant in shape and contained a partially separated chromatin region with a long spindle. Together with the results of the accompanying paper, we conclude that nda2 and nda3 genes control nuclear and cytoplasmic microtubular organization.","authors":"Toda T, Umesono K, Hirata A, Yanagida M","authors_abbrev":"Toda T et al.","pubmed_publication_date":"05 Aug 1983","pubmed_entrez_date":"1983-08-05","publication_year":"1983","canto_session_key":"d8d04416bcc940b3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-03-20 16:24:43","canto_approved_date":"2026-01-31 15:46:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 18:07:56","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPBC4.04c","SPBC26H8.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-03-20"},{"uniquename":"PMID:8913338","title":"Isolation and characterization of a cisplatin-resistant strain of Schizosaccharomyces pombe.","citation":"Mol Pharmacol 1996 Nov;50(5):1080-6","abstract":"A cis-diamminedichloroplatinum [DDP (cisplatin)]-resistant population of Schizosaccharomyces pombe was developed through chronic exposure of the 972 h- strain to increasing concentrations of the drug. The resulting cells, designated wtr2, were 5.25-fold resistant to DDP, are resistance was retained by clone isolated from this population in the absence of drug for > or = 5 months. After backcrossing and isolation of a single clone, random spore analysis gave a segregation ratio close to 1:1 for DDP resistance and sensitivity. Tetrad analysis confirmed a mendelian 2:2 segregation, suggesting that a single nuclear gene was responsible for the DDP-resistant phenotype. Stable diploids obtained from the mating of a resistant spore carrying the ade6-216 marker with the mei2-102-ade6-210 meiosis-deficient mutant remained resistant, indicating that the resistant phenotype was expressed dominantly. There was no difference between the accumulation of the DDP analog [3H]dichloro(ethylenediamine)-platinum(II) into whole cells derived from the sensitive and the resistant spores obtained from the last backcross. The resistant clones from a single tetrad did not have an increased level of glutathione and were collaterally sensitive to cadmium and arsenite. We conclude that in S. pombe, a stable and dominant DDP-resistant phenotype can be mediated by a single allele, that the phenotype is not accompanied by cross-resistance to cadmium or arsenite, and that the mechanism is not associated with a significant alteration in glutathione level or DDP uptake.","authors":"Perego P, Jimenez G, Howell SB","authors_abbrev":"Perego P et al.","pubmed_publication_date":"Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_session_key":"6e2fe16566eb820f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-05-20 08:36:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-20 08:36:14","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-05-20"},{"uniquename":"PMID:22150589","title":"Solution structure of the Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNA.","citation":"Biochem J 2012 Mar 15;442(3):527-38","abstract":"Methylation of H4K20 (Lys(20) of histone H4) plays an important role in the regulation of diverse cellular processes. In fission yeast, all three states of H4K20 methylation are catalysed by Set9. Pdp1 is a PWWP (proline-tryptophan-tryptophan-proline) domain-containing protein, which associates with Set9 to regulate its chromatin localization and methyltransferase activity towards H4K20. The structure of the Pdp1 PWWP domain, which is the first PWWP domain identified which binds to methyl-lysine at the H4K20 site, was determined in the present study by solution NMR. The Pdp1 PWWP domain adopts a classical PWWP fold, with a five-strand antiparallel β-barrel followed by three α-helices. However, it differs significantly from other PWWP domains in some structural aspects that account, in part, for its molecular recognition. Moreover, we revealed a unique binding pattern of the PWWP domain, in that the PWWP domain of Pdp1 bound not only to H4K20me3 (trimethylated Lys(20) of histone H4), but also to dsDNA (double-stranded DNA) via an aromatic cage and a positively charged area respectively. EMSAs (electrophoretic mobility-shift assays) illustrated the ability of the Pdp1 PWWP domain to bind to the nucleosome core particle, and further mutagenesis experiments indicated the crucial role of this binding activity in histone H4K20 di- and tri-methylation in yeast cells. The present study may shed light on a novel mechanism of histone methylation regulation by the PWWP domain.","doi":"10.1042/BJ20111885","authors":"Qiu Y, Zhang W, Zhao C, Wang Y, Wang W, Zhang J, Zhang Z, Li G, Shi Y, Tu X, Wu J","authors_abbrev":"Qiu Y et al.","pubmed_publication_date":"15 Mar 2012","pubmed_entrez_date":"2011-12-14","publication_year":"2012","canto_session_key":"10205a1be0d30851","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-11 09:34:55","canto_approved_date":"2024-12-22 13:37:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-11 09:34:47","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.03c","SPBC8D2.03c","SPBC1105.12","SPBC29A3.13"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-11-11","pdb_entries":[{"pdb_id":"2l89","gene_chains":[{"gene_uniquename":"SPBC29A3.13","chain":"A","position":"45-152"}],"title":"Solution structure of Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNA","entry_authors":"Qiu Y,Zhang J,Zhang W","entry_authors_abbrev":"Qiu Y et al.","reference_uniquename":"PMID:22150589","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:9457075","title":"Ribosomal DNA replication in the fission yeast, Schizosaccharomyces pombe.","citation":"Exp Cell Res 1998 Jan 10;238(1):220-30","abstract":"We have employed genetic and two-dimensional (2D) gel electrophoretic methods to identify replication initiation, pausing, and termination sites in the tandem ribosomal DNA (rDNA) repeats of the fission yeast, Schizosaccharomyces pombe. An autonomously replicating sequence (ARS) element, ars3001, maps to a 2.3-kb restriction fragment spanning the junction between the nontranscribed spacer (NTS) and the external transcribed spacer upstream of the ribosomal RNA genes, and 2D gel analysis shows that replication initiates in the NTS portion of the same fragment. A pause region at the 3' end of the rRNA genes inhibits forks from entering these genes counter to the direction of transcription. Thus, most forks move through the genes in the same direction as transcription. In these respects, fission yeast rDNA replication resembles that in the budding yeast, Saccharomyces cerevisiae, and in multicellular eukaryotic organisms. A feature which, so far, has been detected only in fission yeast is the pausing of replication forks in a broad region near the 5.8S rRNA gene.","authors":"Sanchez JA, Kim SM, Huberman JA","authors_abbrev":"Sanchez JA et al.","pubmed_publication_date":"10 Jan 1998","pubmed_entrez_date":"1998-02-11","publication_year":"1998","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30237224","title":"Regulated reconstitution of spindle checkpoint arrest and silencing through chemically induced dimerisation  in vivo .","citation":"J Cell Sci 2018 Oct 04;132(4)","abstract":"Chemically induced dimerisation (CID) uses small molecules to control specific protein-protein interactions. We employed CID dependent on the plant hormone abscisic acid (ABA) to reconstitute spindle checkpoint signalling in fission yeast. The spindle checkpoint signal usually originates at unattached or inappropriately attached kinetochores. These are complex, multiprotein structures with several important functions. To bypass kinetochore complexity, we took a reductionist approach to studying checkpoint signalling. We generated a synthetic checkpoint arrest ectopically by inducing heterodimerisation of the checkpoint proteins Mph1 (the fission yeast homologue of Mps1) and Spc7 (the fission yeast homologue of KNL1). These proteins were engineered such that they cannot localise to kinetochores, and only form a complex in the presence of ABA. Using this novel assay we were able to checkpoint arrest a synchronous population of cells within 30 min of ABA addition. This assay allows detailed genetic dissection of checkpoint activation and, importantly, also provides a valuable tool for studying checkpoint silencing. To analyse silencing of the checkpoint and the ensuing mitotic exit, we simply washed out the ABA from arrested fission yeast cells. We show here that silencing is critically dependent on protein phosphatase 1 (PP1) recruitment to Mph1-Spc7 signalling platforms.","doi":"10.1242/jcs.219766","authors":"Amin P, Soper Ní Chafraidh S, Leontiou I, Hardwick KG","authors_abbrev":"Amin P et al.","pubmed_publication_date":"04 Oct 2018","pubmed_entrez_date":"2018-09-22","publication_year":"2018","canto_session_key":"db75ad7ade2d3c9d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-09-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29958536","title":"GrapHi-C: graph-based visualization of Hi-C datasets.","citation":"BMC Res Notes 2018 Jun 29;11(1):418","abstract":"Hi-C is a proximity-based ligation reaction used to detect regions of the genome that are close in 3D space (or \"interacting\"). Typically, results from Hi-C experiments (contact maps) are visualized as heatmaps or Circos plots. While informative, these visualizations do not directly represent genomic structure and folding, making the interpretation of the underlying 3D genomic organization obscured. Our objective was to generate a graph-based contact map representation that leads to a more intuitive structural visualization.\nNormalized contact maps were converted into undirected graphs where each vertex represented a genomic region and each edge represented a detected (intra- and inter-chromosomal) or known (linear) interaction between two regions. Each edge was weighted by the inverse of the linear distance (Hi-C experimental resolution) or the interaction frequency from the contact map. Graphs were generated based on this representation scheme for contact maps from existing fission yeast datasets. Originally, these datasets were used to (1) identify specific principles influencing fission yeast genome organization and (2) uncover changes in fission yeast genome organization during the cell cycle. When compared to the equivalent heatmaps and/or Circos plots, the graph-based visualizations more intuitively depicted the changes in genome organization described in the original studies.","doi":"10.1186/s13104-018-3507-2","authors":"MacKay K, Kusalik A, Eskiw CH","authors_abbrev":"MacKay K et al.","pubmed_publication_date":"29 Jun 2018","pubmed_entrez_date":"2018-07-01","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-07-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29937227","title":"The Inner Nuclear Membrane Is a Metabolically Active Territory that Generates Nuclear Lipid Droplets.","citation":"Cell 2018 Jul 26;174(3):700-715.e18","abstract":"The inner nuclear membrane (INM) encases the genome and is fused with the outer nuclear membrane (ONM) to form the nuclear envelope. The ONM is contiguous with the endoplasmic reticulum (ER), the main site of phospholipid synthesis. In contrast to the ER and ONM, evidence for a metabolic activity of the INM has been lacking. Here, we show that the INM is an adaptable membrane territory capable of lipid metabolism. S. cerevisiae cells target enzymes to the INM that can promote lipid storage. Lipid storage involves the synthesis of nuclear lipid droplets from the INM and is characterized by lipid exchange through Seipin-dependent membrane bridges. We identify the genetic circuit for nuclear lipid droplet synthesis and a role of these organelles in regulating this circuit by sequestration of a transcription factor. Our findings suggest a link between INM metabolism and genome regulation and have potential relevance for human lipodystrophy.","doi":"10.1016/j.cell.2018.05.047","authors":"Romanauska A, Köhler A","authors_abbrev":"Romanauska A et al.","pubmed_publication_date":"26 Jul 2018","pubmed_entrez_date":"2018-06-26","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YLR404W","SPAC3A11.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17202724","title":"Localization of type I myosin and F-actin to the leading edge region of the forespore membrane in Schizosaccharomyces pombe.","citation":"Cell Struct Funct 2006;31(2):181-95","abstract":"Myo1, a heavy chain of type I myosin of the fission yeast Schizosaccharomyces pombe, is essential for sporulation. Here we have analyzed the expression, localization and cellular function of the type I myosin light chain calmodulin, Cam2, encoded by cam2(+). Transcription of cam2(+) was constitutive and markedly enhanced in meiosis. The cam2 null mutant was viable and completed sporulation normally at 28 degrees C, but formed four-spored asci poorly at 34 degrees C. In those sporulation-defective cells, the forespore membrane was formed abnormally. A Cam2-GFP fusion protein accumulated at the cell poles in interphase cells and at the medial septation site in postmitotic cells, colocalizing with Myo1 and F-actin patches. During the mating process, a single Cam2-GFP dot was detected at the tip of the mating projection. During meiosis-I, the Cam2-GFP dots dispersed into the cell periphery and the cytoplasm. At metaphase-II, intense Cam2-GFP signals appeared near Meu14 rings which were formed at the leading edge of expanding forespore membranes. This localization of Cam2 was dependent upon Myo1; and sporulation defect of cam2Delta at 34 degrees C was alleviated by overexpressing Myo1DeltaIQ. These results suggest a close relationship between Cam2 and Myo1. In addition, both F-actin and Myo1 localized with Cam2 in the leading edge region. In summary, type I myosin and F-actin accumulate at the leading edge area of the forespore membrane and may play a pivotal role in its assembly.","authors":"Itadani A, Nakamura T, Shimoda C","authors_abbrev":"Itadani A et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-01-05","publication_year":"2006","canto_session_key":"24ad28da3d44573e","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29A4.05","SPBC32H8.12c","SPBC146.13c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:32231932","title":"Phytase produced using  Schizosaccharomyces pombe  ASP595-1 strain (Genetically Modified Feed Additives).","citation":"Food Saf (Tokyo) 2017 Jun;5(2):72-73","abstract":"Food Safety Commission of Japan (FSCJ) conducted two sets of risk assessment on phytase produced using  Schizosaccharomyces pombe  ASP595-1 strain. One is the safety assessment on feed additives produced using genetically modified microorganisms. None of new harmful substance is generated in the additive and thus not transferred to animal products, such as meat, milk and eggs. Components associated with genetic modification in the additive are unlikely to yield harmful substances to be accumulated in animal products. The components are unlikely to affect the metabolism of the target animals to generate new harmful substances. No safety concern is thus raised in the products from animals fed with this phytase. The other is the risk assessment related to the revision of the Standards and Specifications of Feeds and Feed Additives. The feed additive was considered to have no genotoxicity relevant to human health. No adverse effects were observed in 14-day and 90-day subacute toxicity studies in rats as well as in feeding trials in pigs and poultry. On the formulations with polyvinyl alcohol, human intake of polyvinyl alcohol via animal products was recognized to be negligible. Consequently, FSCJ judged that the risk on human health via food is negligible as long as the 6-phytase produced using  S. pombe  ASP595-1 strain is properly used as a feed additive.","doi":"10.14252/foodsafetyfscj.2017001s","authors":"Food Safety Commission of Japan","authors_abbrev":"Food Safety Commission of Japan","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2020-04-02","publication_year":"2017","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-04-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19037094","title":"The Rho1p exchange factor Rgf1p signals upstream from the Pmk1 mitogen-activated protein kinase pathway in fission yeast.","citation":"Mol Biol Cell 2009 Jan;20(2):721-31","abstract":"The Schizosaccharomyces pombe exchange factor Rgf1p specifically regulates Rho1p during polarized growth. Rgf1p activates the beta-glucan synthase (GS) complex containing the catalytic subunit Bgs4p and is involved in the activation of growth at the second end, a transition that requires actin reorganization. In this work, we investigated Rgf1p signaling and observed that Rgf1p acted upstream from the Pck2p-Pmk1p MAPK signaling pathway. We noted that Rgf1p and calcineurin play antagonistic roles in Cl(-) homeostasis; rgf1Delta cells showed the vic phenotype (viable in the presence of immunosuppressant and chlorine ion) and were unable to grow in the presence of high salt concentrations, both phenotypes being characteristic of knockouts of the MAPK components. In addition, mutations that perturb signaling through the MAPK pathway resulted in defective cell integrity (hypersensitivity to caspofungin and beta-glucanase). Rgf1p acts by positively regulating a subset of stimuli toward the Pmk1p-cell integrity pathway. After osmotic shock and cell wall damage HA-tagged Pmk1p was phosphorylated in wild-type cells but not in rgf1Delta cells. Finally, we provide evidence to show that Rgf1p regulates Pmk1p activation in a process that involves the activation of Rho1p and Pck2p, and we demonstrate that Rgf1p is unique in this signaling process, because Pmk1p activation was largely independent of the other two Rho1p-specific GEFs, Rgf2p and Rgf3p.","authors":"Garcia P, Tajadura V, Sanchez Y","authors_abbrev":"Garcia P et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2008-11-28","publication_year":"2009","canto_session_key":"50980b7b866ebd46","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Patricia Garcia","canto_first_approved_date":"2025-02-03 11:28:21","canto_approved_date":"2025-02-03 11:28:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-01-30 12:28:13","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":11,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Patricia Garcia","community_curator":true,"annotation_count":45,"orcid":"0000-0001-7513-1847","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.07","SPAC16.01","SPAC24B11.06c","SPBC12D12.04c","SPAC1F7.04","SPCC645.06c","SPBC119.08","SPAC1F3.02c","SPAC1006.06","SPAC31G5.09c","SPBC543.07","SPBC409.07c"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2025-02-03"},{"uniquename":"PMID:22573890","title":"Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis.","citation":"Mol Biol Cell 2012 Jul;23(13):2433-44","abstract":"Cell morphogenesis is a complex process that relies on a diverse array of proteins and pathways. We have identified a transglutaminase-like protein (Cyk3p) that functions in fission yeast morphogenesis. The phenotype of a cyk3 knockout strain indicates a primary role for Cyk3p in cytokinesis. Correspondingly, Cyk3p localizes both to the actomyosin contractile ring and the division septum, promoting ring constriction, septation, and subsequent cell separation following ring disassembly. In addition, Cyk3p localizes to polarized growth sites and plays a role in cell shape determination, and it also appears to contribute to cell integrity during stationary phase, given its accumulation as dynamic puncta at the cortex of such cells. Our results and the conservation of Cyk3p across fungi point to a role in cell wall synthesis and remodeling. Cyk3p possesses a transglutaminase domain that is essential for function, even though it lacks the catalytic active site. In a wider sense, our work illustrates the physiological importance of inactive members of the transglutaminase family, which are found throughout eukaryotes. We suggest that the proposed evolution of animal transglutaminase cross-linking activity from ancestral bacterial thiol proteases was accompanied by the emergence of a subclass whose function does not depend on enzymatic activity.","doi":"10.1091/mbc.E11-07-0656","authors":"Pollard LW, Onishi M, Pringle JR, Lord M","authors_abbrev":"Pollard LW et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-05-11","publication_year":"2012","canto_session_key":"cbc863c3c9dd38e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-07 22:00:12","canto_approved_date":"2024-03-22 16:56:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-29 21:30:53","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08","SPAC9G1.06c","SPBC1709.01","SPCC645.05c","SPAC1F5.04c","SPAC20G8.05c","SPAC4A8.05c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-06-07"},{"uniquename":"PMID:23382177","title":"Acetylated Histone H3K9 is associated with meiotic recombination hotspots, and plays a role in recombination redundantly with other factors including the H3K4 methylase Set1 in fission yeast.","citation":"Nucleic Acids Res 2013 Apr 01;41(6):3504-17","abstract":"Histone modifications are associated with meiotic recombination hotspots, discrete sites with augmented recombination frequency. For example, trimethylation of histone H3 lysine4 (H3K4me3) marks most hotspots in budding yeast and mouse. Modified histones are known to regulate meiotic recombination partly by promoting DNA double-strand break (DSB) formation at hotspots, but the role and precise landscape of involved modifications remain unclear. Here, we studied hotspot-associated modifications in fission yeast and found general features: acetylation of H3 lysine9 (H3K9ac) is elevated, and H3K4me3 is not significantly enriched. Mutating H3K9 to non-acetylatable alanine mildly reduced levels of the DSB-inducing protein Rec12 (the fission yeast homologue of Spo11) and DSB at hotspots, indicating that H3K9ac may be involved in DSB formation by enhancing the interaction between Rec12 and hotspots. In addition, we found that the lack of the H3K4 methyltransferase Set1 generally increased Rec12 binding to chromatin but partially reduced DSB formation at some loci, suggesting that Set1 is also involved in DSB formation. These results suggest that meiotic DSB formation is redundantly regulated by multiple chromatin-related factors including H3K9ac and Set1 in fission yeast.","doi":"10.1093/nar/gkt049","authors":"Yamada S, Ohta K, Yamada T","authors_abbrev":"Yamada S et al.","pubmed_publication_date":"01 Apr 2013","pubmed_entrez_date":"2013-02-06","publication_year":"2013","canto_session_key":"9df9cf21d582dbfc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000113","title":"Gene Ontology annotation of human sequence-specific DNA binding transcription factors (DbTFs) based on the TFClass database","abstract":"The TFClass (http://tfclass.bioinf.med.uni-goettingen.de/index.jsf) database provides a comprehensive classification of mammalian DNA binding transcription factors (DbTFs) based on their DNA binding domains (DBDs) (PMID:29087517). TFClass classifies mammalian DbTFs by a five-level classification in which the four highest levels represent groups defined by structural and sequence similarities (superclass, class, family, subfamily, and genera) (more details at http://www.edgar-wingender.de/TFClass_schema.html). This classification is based on the combination of background knowledge of the molecular structural features of DBDs (PMID:9340487, PMID:23427989) and phylogenetic trees constructed via multiple sequence alignment with hierarchical clustering of manually validated DBDs and/or full-length protein sequences retrieved from UniProt (PMID:23427989, PMID:23180794, PMID:23427989). ","authors":"Marcio Luis Acencio (1), George Georghiou (2), Sandra Orchard (2), Liv Thommensen (1), Martin Kuiper (1) and Astrid Lægreid (1). (1) Norwegian University of Science and Technology (NTNU), Trondheim, Norway; (2) European Bioinformatics Institute (EBI), Hinxton, Cambridgeshire, United Kingdom","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37586723","title":"Fission yeast poly(A) polymerase active site mutation Y86D alleviates the  rad24 Δ  asp1-H397A  synthetic growth defect and up-regulates mRNAs targeted by MTREC and Mmi1.","citation":"RNA 2023 Nov;29(11):1738-1753","abstract":"Expression of fission yeast Pho1 acid phosphatase is repressed under phosphate-replete conditions by transcription of an upstream  prt  lncRNA that interferes with the  pho1  mRNA promoter. lncRNA-mediated interference is alleviated by genetic perturbations that elicit precocious lncRNA 3'-processing and transcription termination, such as (i) the inositol pyrophosphate pyrophosphatase-defective  asp1-H397A  allele, which results in elevated levels of IP 8 , and (ii) absence of the 14-3-3 protein Rad24. Combining  rad24 Δ with  asp1-H397A  causes a severe synthetic growth defect. A forward genetic screen for  SRA  ( S uppressor of  R ad24  A sp1-H397A) mutations identified a novel missense mutation (Tyr86Asp) of Pla1, the essential poly(A) polymerase subunit of the fission yeast cleavage and polyadenylation factor (CPF) complex. The  pla1-Y86D  allele was viable but slow-growing in an otherwise wild-type background. Tyr86 is a conserved active site constituent that contacts the RNA primer 3' nt and the incoming ATP. The Y86D mutation elicits a severe catalytic defect in RNA-primed poly(A) synthesis in vitro and in binding to an RNA primer. Yet, analyses of specific mRNAs indicate that poly(A) tails in  pla1-Y86D  cells are not different in size than those in wild-type cells, suggesting that other RNA interactors within CPF compensate for the defects of isolated Pla1-Y86D. Transcriptome profiling of  pla1-Y86D  cells revealed the accumulation of multiple RNAs that are normally rapidly degraded by the nuclear exosome under the direction of the MTREC complex, with which Pla1 associates. We suggest that Pla1-Y86D is deficient in the hyperadenylation of MTREC targets that precedes their decay by the exosome.","doi":"10.1261/rna.079722.123","authors":"Garg A, Schwer B, Shuman S","authors_abbrev":"Garg A et al.","pubmed_publication_date":"Nov 2023","pubmed_entrez_date":"2023-08-16","publication_year":"2023","canto_session_key":"f22c677d597985b2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-08-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1340462","title":"Characterization of a fission yeast gene, gpa2, that encodes a G alpha subunit involved in the monitoring of nutrition.","citation":"Genes Dev 1992 Dec;6(12B):2455-62","abstract":"The Schizosaccharomyces pombe gpa2 gene was cloned by hybridization with a cDNA for Dictyostelium discoideum G alpha 1. It encodes a homolog of G-protein alpha-subunits with 354 amino acids and a predicted molecular mass of 40,522. Disruption of gpa2 slows cell growth but is not lethal. Cells defective in gpa2 mate and sporulate readily in the presence of plentiful nutrition, bypassing the requirement of nitrogen starvation for the initiation of sexual development. These phenotypes mimic those of cells defective in cyr1 encoding adenylyl cyclase. The level of cAMP in gpa2 null mutants is only one-third of the wild-type level. Mutations in gpa2 that are likely to inhibit the GTPase activity of the gene product cause a slight increase in intracellular cAMP levels and result in leaky sterility. The cAMP level reaches 20 times as high as the wild-type level if a cell carries both this type of gpa2 mutation and a null mutation in pde1 encoding phosphodiesterase. Cells defective in gpa2 fail to produce cAMP in response to glucose stimulation. These results suggest that Gpa2 is involved in the determination of the cAMP level according to nutritional conditions, most likely as a positive regulator of adenylyl cyclase.","authors":"Isshiki T, Mochizuki N, Maeda T, Yamamoto M","authors_abbrev":"Isshiki T et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"34d8f97a921167ba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 19:45:36","canto_approved_date":"2021-01-19 09:12:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-15 00:02:37","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H3.13c","SPCC285.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-10"},{"uniquename":"PMID:30108922","title":"Synthesis, characterization and biological application of 5-quinoline 1,3,5-trisubstituted pyrazole based platinum(ii) complexes.","citation":"Medchemcomm 2018 Feb 01;9(2):282-298","abstract":"Square planar mononuclear platinum(ii) complexes were synthesized in the presence of neutral bidentate heterocyclic (5-quinoline 1,3,5-tri-substituted pyrazole scaffold) ligands and K 2 PtCl 4  salt. The synthesized compounds were characterized by micro-elemental analysis, FT-IR, UV-vis,  1 H NMR,  13 C NMR, TGA, mass spectrometry and molar conductivity. Their biological activities were investigated by  in vitro  brine shrimp lethality bioassay,  in vitro  antimicrobial study against five different pathogens,  in vivo  cellular level cytotoxicity against  Schizosaccharomyces pombe  cells, and  in vitro  anti-proliferation assay. The binding constant  K  sv ,  K  b ,  K  a  values of the complexes were determined by DNA interaction studies. The gel electrophoresis assay was carried out to examine the effect of the complexes on the DNA nuclease of pUC19 plasmid DNA. The docking energies of the ligands ( L 1 -L 5   ) and complexes ( I-V ) were observed in the range of -265.14 to -284.33 kJ mol -1 . The synthesized Pt(ii) complexes ( I-V ) were screened against the MCF-7 (human breast adenocarcinoma) and HCT-116 (human colon carcinoma) cancer cell lines.","doi":"10.1039/c7md00472a","authors":"Lunagariya MV, Thakor KP, Varma RR, Waghela BN, Pathak C, Patel MN","authors_abbrev":"Lunagariya MV et al.","pubmed_publication_date":"01 Feb 2018","pubmed_entrez_date":"2018-08-16","publication_year":"2018","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2018-08-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22267499","title":"Characterization of ypa1 and ypa2, the Schizosaccharomyces pombe orthologs of the peptidyl proyl isomerases that activate PP2A, reveals a role for Ypa2p in the regulation of cytokinesis.","citation":"Genetics 2012 Apr;190(4):1235-50","abstract":"The Schizosaccharomyces pombe septation initiation network (SIN) regulates cytokinesis. Cdc7p is the first kinase in the core SIN; we have screened genetically for SIN regulators by isolating cold-sensitive suppressors of cdc7-24. Our screen yielded a mutant in SPAC1782.05, one of the two fission yeast orthologs of mammalian phosphotyrosyl phosphatase activator. We have characterized this gene and its ortholog SPAC4F10.04, which we have named ypa2 and ypa1, respectively. We find that Ypa2p is the major form of protein phosphatase type 2A activator in S. pombe. A double ypa1-Δ ypa2-Δ null mutant is inviable, indicating that the two gene products have at least one essential overlapping function. Individually, the ypa1 and ypa2 genes are essential for survival only at low temperatures. The ypa2-Δ mutant divides at a reduced cell size and displays aberrant cell morphology and cytokinesis. Genetic analysis implicates Ypa2p as an inhibitor of the septation initiation network. We also isolated a cold-sensitive allele of ppa2, the major protein phosphatase type 2A catalytic subunit, implicating this enzyme as a regulator of the septation initiation network.","doi":"10.1534/genetics.111.138040","authors":"Goyal A, Simanis V","authors_abbrev":"Goyal A et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-01-24","publication_year":"2012","canto_session_key":"291d614ef0c90bc4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-02-23 11:48:23","canto_approved_date":"2024-05-16 08:32:30","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-02-22 11:39:25","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC227.07c","SPBC24C6.07","SPBC16H5.07c","SPAC1006.08","SPAC1565.06c","SPAC6F6.08c","SPBC21.06c","SPAC4F10.04","SPCC188.02","SPAC24B11.11c","SPBC428.13c","SPCC18B5.03","SPAC823.15","SPAC23C11.16","SPCC1739.11c","SPAC1782.05"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2024-02-23"},{"uniquename":"PMID:20460254","title":"A genetic engineering solution to the \"arginine conversion problem\" in stable isotope labeling by amino acids in cell culture (SILAC).","citation":"Mol Cell Proteomics 2010 Jul;9(7):1567-77","abstract":"Stable isotope labeling by amino acids in cell culture (SILAC) provides a straightforward tool for quantitation in proteomics. However, one problem associated with SILAC is the in vivo conversion of labeled arginine to other amino acids, typically proline. We found that arginine conversion in the fission yeast Schizosaccharomyces pombe occurred at extremely high levels, such that labeling cells with heavy arginine led to undesired incorporation of label into essentially all of the proline pool as well as a substantial portion of glutamate, glutamine, and lysine pools. We found that this can be prevented by deleting genes involved in arginine catabolism using methods that are highly robust yet simple to implement. Deletion of both fission yeast arginase genes or of the single ornithine transaminase gene, together with a small modification to growth medium that improves arginine uptake in mutant strains, was sufficient to abolish essentially all arginine conversion. We demonstrated the usefulness of our approach in a large scale quantitative analysis of proteins before and after cell division; both up- and down-regulated proteins, including a novel protein involved in septation, were successfully identified. This strategy for addressing the \"arginine conversion problem\" may be more broadly applicable to organisms amenable to genetic manipulation.","doi":"10.1074/mcp.M110.000208","authors":"Bicho CC, de Lima Alves F, Chen ZA, Rappsilber J, Sawin KE","authors_abbrev":"Bicho CC et al.","pubmed_publication_date":"Jul 2010","pubmed_entrez_date":"2010-05-13","publication_year":"2010","canto_session_key":"6053b583675e98f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-09 17:56:45","canto_approved_date":"2026-01-15 18:39:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-25 21:57:52","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC777.09c","SPBP26C9.02c","SPAC227.18","SPBC27.04","SPAC3H1.07","SPBC21C3.08c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-01-09"},{"uniquename":"PMID:24691906","title":"DNA replication components as regulators of epigenetic inheritance--lesson from fission yeast centromere.","citation":"Protein Cell 2014 Jun;5(6):411-9","abstract":"Genetic information stored in DNA is accurately copied and transferred to subsequent generations through DNA replication. This process is accomplished through the concerted actions of highly conserved DNA replication components. Epigenetic information stored in the form of histone modifications and DNA methylation, constitutes a second layer of regulatory information important for many cellular processes, such as gene expression regulation, chromatin organization, and genome stability. During DNA replication, epigenetic information must also be faithfully transmitted to subsequent generations. How this monumental task is achieved remains poorly understood. In this review, we will discuss recent advances on the role of DNA replication components in the inheritance of epigenetic marks, with a particular focus on epigenetic regulation in fission yeast. Based on these findings, we propose that specific DNA replication components function as key regulators in the replication of epigenetic information across the genome.","doi":"10.1007/s13238-014-0049-9","authors":"He H, Gonzalez M, Zhang F, Li F","authors_abbrev":"He H et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-04-03","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12581158","title":"Overproduction of a conserved domain of fission yeast and mammalian translation initiation factor eIF4G causes aberrant cell morphology and results in disruption of the localization of F-actin and the organization of microtubules.","citation":"Genes Cells 2003 Feb;8(2):163-78","abstract":"The recruitment of mRNA for translation involves the assembly at the 5'cap of a complex of three initiation factors: the cap binding protein eIF4E, the ATP-dependent RNA helicase eIF4A and the scaffold protein eIF4G. eIF4G mediates the binding of this mRNA-protein complex to the 43S ribosomal preinitiation complex. There is growing recognition that the components of the translational apparatus interact functionally with cytoskeletal components. Here we report specific effects of the over-expression of human and fission yeast eIF4G domains on cell morphology in Schizosaccharomyces pombe.\nA single gene encoding fission yeast eIF4G was identified and demonstrated to be essential. We have over-expressed fragments corresponding to the conserved functional domains of eIF4G. At expression levels that did not disrupt rates of overall translation or protein accumulation, a fragment of S. pombe eIF4G, 4G-NOB, corresponding to the minimal region of human eIF4G required to support cap-independent mRNA recruitment, was found to impair cell proliferation in fission yeast. This resulted from defects in cytokinesis, and was associated with the disruption of both microtubules and actin microfilaments. The over-expressed fragment was itself localized to the cell ends, the nuclear periphery and the septum.\nThis is the first demonstration of a link between a translation initiation factor and mechanisms controlling cell morphology. The data suggest a direct or indirect interaction between the functional domains of eIF4G and cellular structures involved in cytokinesis.","authors":"Hashemzadeh-Bonehi L, Curtis PS, Morley SJ, Thorpe JR, Pain VM","authors_abbrev":"Hashemzadeh-Bonehi L et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-02-13","publication_year":"2003","canto_session_key":"047cab7e55967c39","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-09-11 16:04:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 16:04:47","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.03","SPAC16E8.15"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-09-11"},{"uniquename":"PMID:12921238","title":"Growth during the cell cycle.","citation":"Int Rev Cytol 2003;226:165-258","abstract":"During the cell cycle, major bulk parameters such as volume, dry mass, total protein, and total RNA double and such growth is a fundamental property of the cell cycle. The patterns of growth in volume and total protein or RNA provide an \"envelope\" that contains and may restrict the gear wheels. The main parameters of cell cycle growth were established in the earlier work when people moved from this field to the reductionist approaches of molecular biology, but very little is known on the patterns of metabolism. Most of the bulk properties of cells show a continuous increase during the cell cycle, although the exact pattern of this increase may vary. Since the earliest days, there have been two popular models, based on an exponential increase and linear increase. In the first, there is no sharp change in the rate of increase through the cycle but a smooth increase by a factor of two. In the second, the rate of increase stays constant through much of the cycle but it doubles sharply at a rate change point (RCP). It is thought that the exponential increase is caused by the steady growth of ribosome numbers and the linear pattern is caused by a doubling of the structural genes during the S period giving an RCP--a \"gene dosage\" effect. In budding yeast, there are experiments fitting both models but on balance slightly favoring \"gene dosage.\" In fission yeast, there is no good evidence of exponential increase. All the bulk properties, except O2 consumption, appear to follow linear patterns with an RCP during the short S period. In addition, there is in wild-type cells a minor RCP in G2 where the rate increases by 70%. In mammalian cells, there is good but not extensive evidence of exponential increase. In Escherichia coli, exponential increase appears to be the pattern. There are two important points: First, some proteins do not show peaks of periodic synthesis. If they show patterns of exponential increase both they and the total protein pattern will not be cell cycle regulated. However, if the total protein pattern is not exponential, then a majority of the individual proteins will be so regulated. If this majority pattern is linear, then it can be detected from rate measurements on total protein. However, it would be much harder at the level of individual proteins where the methods are at present not sensitive enough to detect a rate change by a factor of two. At a simple level, it is only the exponential increase that is not cell cycle regulated in a synchronous culture. The existence of a \"size control\" is well known and the control has been studied for a long time, but it has been remarkably resistant to molecular analysis. The attainment of a critical size triggers the periodic events of the cycle such as the S period and mitosis. This control acts as a homeostatic effector that maintains a constant \"average\" cell size at division through successive cycles in a growing culture. It is a vital link coordinating cell growth with periodic events of the cycle. A size control is present in all the systems and appears to operate near the start of S or of mitosis when the cell has reached a critical size, but the molecular mechanism by which size is measured remains both obscure and a challenge. A simple version might be for the cell to detect a critical concentration of a gene product.","authors":"Mitchison JM","authors_abbrev":"Mitchison JM","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-08-19","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15533439","title":"Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast.","citation":"J Mol Biol 2004 Nov 26;344(3):697-706","abstract":"Conjugation of proteins to ubiquitin plays a central role for a number of cellular processes including endocytosis, DNA repair and degradation by the 26S proteasome. However, ubiquitination is reversible as a number of deubiquitinating enzymes mediate the disassembly of ubiquitin-protein conjugates. Some deubiquitinating enzymes are associated with the 26S proteasome contributing to and regulating the particle's activity. Here, we characterise fission yeast Uch2 and Ubp6, two proteasome associated deubiquitinating enzymes. The human orthologues of these enzymes are known as Uch37 and Usp14, respectively. We report that the subunit Uch2/Uch37 is the major deubiquitinating enzyme associated with the fission yeast 26S proteasome. In contrast, the activity of Ubp6 appears to play a more regulatory and/or structural role involving the proteasome subunits Mts1/Rpn9, Mts2/Rpt2 and Mts3/Rpn12, as Ubp6 becomes essential when activity of these subunits is compromised by conditional mutations. Finally, when the genes encoding Uch2/Uch37 and Ubp6 are disrupted, the cells are viable without showing obvious signs of impaired ubiquitin-dependent proteolysis, indicating that other deubiquitinating enzymes may remedy for the redundancy of these enzymes.","authors":"Stone M, Hartmann-Petersen R, Seeger M, Bech-Otschir D, Wallace M, Gordon C","authors_abbrev":"Stone M et al.","pubmed_publication_date":"26 Nov 2004","pubmed_entrez_date":"2004-11-10","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP19A11.03c","SPBC409.06","SPBC29B5.01","SPAC31G5.13","SPBC4.07c","SPBC16G5.01","SPAC6G9.08","SPAC637.10c"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:27250942","title":"Chromatin and Cell Wall Staining of Schizosaccharomyces pombe.","citation":"Cold Spring Harb Protoc 2016 Jun 01;2016(6)","abstract":"Fission yeasts grow by tip extension, maintaining a constant width until they reach a critical size threshold and divide. Division by medial fission-which gives these yeast their name-generates a new end that arises from the site of cytokinesis. The old end, which was produced during the previous cell cycle, initiates progression of the new cell cycle, and in G2, the new end is activated in a process termed new-end takeoff (NETO). In this protocol, the fluorescent stains calcofluor and 4',6-diamidino-2-phenylindole (DAPI) are used to give a rapid and informative assessment of morphogenesis and cell-cycle progression in the fission yeast Schizosaccharomyces pombe Calcofluor reveals the timing of NETO because it stains the birth scars that are generated at new ends by cytokinesis less efficiently than the rest of the cell wall. Intense calcofluor staining of the septum and measurement of cell length are also widely used to identify dividing cells and to gauge the timing of mitotic commitment. Staining nuclei with DAPI identifies mono- and binucleated cells and complements the calcofluor staining procedure to evaluate the stages of the cell cycle and identify mitotic errors. Equally simple DAPI staining procedures reveal chromatin structure in higher resolution, facilitating more accurate staging of mitotic progression and characterization of mitotic errors.","doi":"10.1101/pdb.prot091025","authors":"Hagan IM","authors_abbrev":"Hagan IM","pubmed_publication_date":"01 Jun 2016","pubmed_entrez_date":"2016-06-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-06-04 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14871934","title":"ADAM family protein Mde10 is essential for development of spore envelopes in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2004 Feb;3(1):27-39","abstract":"We report the identification of Schizosaccharomyces pombe mde10+ as a gene possessing a FLEX element, which forms a binding site for the meiosis-specific transcription factor Mei4. In fact, mde10+ is transcribed only in diploid cells that are induced to meiosis in a Mei4-dependent manner. Western blot analysis indicated that the epitope-tagged Mde10 protein accumulates transiently during meiosis and then rapidly decreases. Mde10 is a multidomain protein containing a metalloprotease catalytic domain, a disintegrin domain, a cysteine-rich domain, and membrane-spanning regions, all of which are shared by members of the mammalian ADAM family. A fusion protein of Mde10 and green fluorescent protein localized to the endoplasmic reticulum during meiosis and was located at the peripheral region of spores at the end of meiosis. An mde10Delta deletion mutant showed no apparent defects in meiosis, sporulation, or spore germination. However, the mutant spores exhibited an aberrant surface appearance, in which the ragged outer spore wall was lost to a large extent. Furthermore, mde10Delta spores were found to be less tolerant to ethanol and diethyl ether than were wild-type spores. The mutagenic replacement of the conserved glutamic acid in the putative protease active site with an alanine residue did not affect the surface morphology or the resistance of spores to environmental stress. Our observations indicate that Mde10 is important in the development of the spore envelope, although this function of Mde10 seems to be independent of its metalloprotease activity.","authors":"Nakamura T, Abe H, Hirata A, Shimoda C","authors_abbrev":"Nakamura T et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2004-02-12","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.11","SPAC17A5.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12488447","title":"High conservation of the Set1/Rad6 axis of histone 3 lysine 4 methylation in budding and fission yeasts.","citation":"J Biol Chem 2003 Mar 07;278(10):8487-93","abstract":"Histone 3 lysine 4 (H3 Lys(4)) methylation in Saccharomyces cerevisiae is mediated by the Set1 complex (Set1C) and is dependent upon ubiquitinylation of H2B by Rad6. Mutually exclusive methylation of H3 at Lys(4) or Lys(9) is central to chromatin regulation; however, S. cerevisiae lacks Lys(9) methylation. Furthermore, a different H3 Lys(4) methylase, Set 7/9, has been identified in mammals, thereby questioning the relevance of the S. cerevisiae findings for eukaryotes in general. We report that the majority of Lys(4) methylation in Schizosaccharomyces pombe, like in S. cerevisiae, is mediated by Set1C and is Rad6-dependent. S. pombe Set1C mediates H3 Lys(4) methylation in vitro and contains the same eight subunits found in S. cerevisiae, including the homologue of the Drosophila trithorax Group protein, Ash2. Three additional features of S. pombe Set1C each involve PHD fingers. Notably, the Spp1 subunit is dispensable for H3 Lys(4) methylation in budding yeast but required in fission yeast, and Sp_Set1C has a novel proteomic hyperlink to a new complex that includes the homologue of another trithorax Group protein, Lid (little imaginal discs). Thus, we infer that Set1C is highly conserved in eukaryotes but observe that its links to the proteome are not.","authors":"Roguev A, Schaft D, Shevchenko A, Aasland R, Shevchenko A, Stewart AF","authors_abbrev":"Roguev A et al.","pubmed_publication_date":"07 Mar 2003","pubmed_entrez_date":"2002-12-19","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23H3.05c","SPBC13G1.08c","SPCC306.04c","SPBC354.03","SPAC3H1.12c","SPBP19A11.06","SPCC594.05c","SPAC17G8.09","SPBC18H10.06c","SPCC18.11c","SPBC83.07"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"GO_REF:0000088","title":"Representation of protein complex by molecular function in the Gene Ontology","abstract":"We have created a standard template for classes defining a protein complex by a molecular function as a cellular component. The underlying equivalence axiom template is \"GO:0043234 and 'capable_of' some ?A\", where A is a molecular function.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18422613","title":"A novel gene, ecl1(+), extends the chronological lifespan in fission yeast.","citation":"FEMS Yeast Res 2008 Jun;8(4):520-30","abstract":"We have identified a novel gene from Schizosaccharomyces pombe that we have named ecl1(+) (extender of the chronological lifespan). When ecl1(+) is provided on a high-copy number plasmid, it extends the viability of both the Deltasty1 MAP kinase mutant and the wild-type cells after entry into the stationary phase. ecl1(+) encodes an 80-amino acid polypeptide that had not been annotated in the current database. The ecl1(+)-mRNA increases transiently when the growth phase is changed from the log phase to the stationary phase. The Ecl1 protein is localized in the nucleus. Calorie restriction extends the chronological lifespan of wild-type and Deltaecl1 cells but not ecl1(+)-overproducing cells. The Deltapka1 mutant shows little, if any, additional extension of viability when Ecl1 is overproduced. The ste11(+) gene that is negatively controlled by Pka1 is up regulated when Ecl1 is overproduced. From these results we propose that the effect of Ecl1 overproduction may be mainly linked to and negatively affects the Pka1-dependent pathway.","doi":"10.1111/j.1567-1364.2008.00379.x","authors":"Ohtsuka H, Mita S, Ogawa Y, Azuma K, Ito H, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-22","publication_year":"2008","canto_session_key":"118ddd6c56f3dd56","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-07 17:13:12","canto_approved_date":"2023-07-10 17:34:37","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-12-19 14:20:18","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC22E12.14c","SPAC24B11.06c","SPBC106.10","SPCC70.12c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-12-07"},{"uniquename":"PMID:30102332","title":"Schizosaccharomyces pombe Pol II transcription elongation factor ELL functions as part of a rudimentary super elongation complex.","citation":"Nucleic Acids Res 2018 Nov 02;46(19):10095-10105","abstract":"ELL family transcription factors activate the overall rate of RNA polymerase II (Pol II) transcription elongation by binding directly to Pol II and suppressing its tendency to pause. In metazoa, ELL regulates Pol II transcription elongation as part of a large multisubunit complex referred to as the Super Elongation Complex (SEC), which includes P-TEFb and EAF, AF9 or ENL, and an AFF family protein. Although orthologs of ELL and EAF have been identified in lower eukaryotes including Schizosaccharomyces pombe, it has been unclear whether SEC-like complexes function in lower eukaryotes. In this report, we describe isolation from S. pombe of an ELL-containing complex with features of a rudimentary SEC. This complex includes S. pombe Ell1, Eaf1, and a previously uncharacterized protein we designate Ell1 binding protein 1 (Ebp1), which is distantly related to metazoan AFF family members. Like the metazoan SEC, this S. pombe ELL complex appears to function broadly in Pol II transcription. Interestingly, it appears to have a particularly important role in regulating genes involved in cell separation.","doi":"10.1093/nar/gky713","authors":"Gopalan S, Gibbon DM, Banks CA, Zhang Y, Florens LA, Washburn MP, Dabas P, Sharma N, Seidel CW, Conaway RC, Conaway JW","authors_abbrev":"Gopalan S et al.","pubmed_publication_date":"02 Nov 2018","pubmed_entrez_date":"2018-08-14","publication_year":"2018","canto_session_key":"ba41ae11a8a2c405","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Joan Conaway","canto_first_approved_date":"2019-04-30 12:53:16","canto_approved_date":"2025-09-03 12:42:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-04-14 18:18:28","canto_added_date":"2018-08-15 00:15:04","annotation_curators":[{"name":"Joan Conaway","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.10c","SPAC6G9.15c","SPBP23A10.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-04-30"},{"uniquename":"PMID:15937491","title":"TFIIH XPB mutants suggest a unified bacterial-like mechanism for promoter opening but not escape.","citation":"Nat Struct Mol Biol 2005 Jul;12(7):603-7","abstract":"DNA helicases open the duplex during DNA replication, repair and transcription. However, RNA polymerase II is the only member of its family with this requirement; RNA polymerases I and III and bacterial RNA polymerases open DNA without a helicase. In this report, characterization of XPB mutants indicates that its helicase activity is not used for RNA polymerase II promoter opening, which is instead driven by its ATPase activity. The mutants have parallels in sigma(54) bacterial transcription and this suggests a similar mode of opening DNA for both RNA polymerases, involving ATP-dependent enzyme conformational changes. Promoter escape is defective in these XPB mutants, suggesting that the XPB helicase acts as an ATP-driven motor to reorganize the tightly wrapped multiprotein eukaryotic preinitiation complex during the remodeling that precedes elongation and the coupling to RNA processing events.","authors":"Lin YC, Choi WS, Gralla JD","authors_abbrev":"Lin YC et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-06-07","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.06"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:30053106","title":"The Pif1 signature motif of Pfh1 is necessary for both protein displacement and helicase unwinding activities, but is dispensable for strand-annealing activity.","citation":"Nucleic Acids Res 2018 Sep 19;46(16):8516-8531","abstract":"Pfh1, the sole member of the Pif1 helicases in Schizosaccharomyces pombe, is multifunctional and essential for maintenance of both the nuclear and mitochondrial genomes. However, we lack mechanistic insights into the functions of Pfh1 and its different motifs. This paper is specifically concerned with the importance of the Pif1 signature motif (SM), a 23 amino acids motif unique to Pif1 helicases, because a single amino acid substitution in this motif is associated with increased risk of breast cancer in humans and inviability in S. pombe. Here we show that the nuclear isoform of Pfh1 (nPfh1) unwound RNA/DNA hybrids more efficiently than DNA/DNA, suggesting that Pfh1 resolves RNA/DNA structures like R-loops in vivo. In addition, nPfh1 displaced proteins from DNA and possessed strand-annealing activity. The unwinding and protein displacement activities were dependent on the SM because nPfh1 without a large portion of this motif (nPfh1-Δ21) or with the disease/inviability-linked mutation (nPfh1-L430P) lost these properties. Unexpectedly, both nPfh1-L430P and nPfh1-Δ21 still displayed binding to G-quadruplex DNA and demonstrated strand-annealing activity. Misregulated strand annealing and binding of nPfh1-L430P without unwinding are perhaps the reasons that cells expressing this allele are inviable.","doi":"10.1093/nar/gky654","authors":"Mohammad JB, Wallgren M, Sabouri N","authors_abbrev":"Mohammad JB et al.","pubmed_publication_date":"19 Sep 2018","pubmed_entrez_date":"2018-07-28","publication_year":"2018","canto_session_key":"f5f87c0cb83a3c7b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Nasim Sabouri","canto_first_approved_date":"2018-08-14 13:01:24","canto_approved_date":"2024-12-21 13:37:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-30 20:23:04","canto_added_date":"2018-07-29 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Nasim Sabouri","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-08-14"},{"uniquename":"PMID:18175921","title":"Cessation of cytokinesis in Schizosaccharomyces pombe during growth after release from high hydrostatic pressure treatment.","citation":"Biosci Biotechnol Biochem 2008 Jan;72(1):88-93","abstract":"On the basis of our previous study concerning the effect of high hydrostatic pressure treatment (HPT) on Escherichia coli FtsZ ring (bacterial cytoskeleton) formation, we aimed to determine the effect of HPT on the growth properties of a representative eukaryotic microbe, Schizosaccharomyces pombe, in relation to the behavior of genuine cytoskeletons. Microtubules were visualized with GFP-linked alpha-tubulin. Actin-related cytoskeletons were fluorescently stained with rhodamine-phalloidin. We observed growth retardation of about 10 h in post growth after HPT (75 MPa, 30 min, 28 degrees C), which caused only a little loss of viable cells. In accordance with the period of growth retardation, cessation of cytokinesis and disappearance of the contractile ring (composed of actin, myosin II, and other proteins), directly participates in cytokinesis, continued for 18 h after HPT. On the other hand, the microtubules disappeared only for 6 h after HPT. Based on these observations, the contractile ring was the site most sensitive to HPT resulting in the cessation of cytokinesis.","authors":"Arai S, Kawarai T, Arai R, Yoshida M, Furukawa S, Ogihara H, Yamasaki M","authors_abbrev":"Arai S et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2008-01-08","publication_year":"2008","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38382926","title":"A novel tracking and analysis system for time-lapse cellular imaging of Schizosaccharomyces pombe.","citation":"Genes Genet Syst 2024 Feb 21;","abstract":"The significance of employing the parent-progeny relationship tracking technique in single-cell analysis has grown with the passage of time. In this study, fundamental image processing techniques were amalgamated to develop software capable of inferring cell cycle alterations in fission yeasts exhibiting equipartition during division. These methods, exclusively relying on bright-field images as input, could track parent-progeny relationships after cellular division through the assessment of temporal morphological transformation of these cells. In the application of this technique, the software was employed for calculate the intracellular fluorescent dots during every stage of the cell cycle, leveraging the yeast strain GFP-fused Swi6, which is present in cells and binds to chromatin. The results obtained with this software were consistent with those of previous studies. This software facilitated the single-cell level tracking of parent-progeny relationships in cells exhibiting equipartition during division and enabled the monitoring of spatial fluctuations in cell cycle-dependent proteins. This method, expediting the analysis of extensive datasets, may also empower large-scale screening experiments that would be unfeasible to conduct manually.","doi":"10.1266/ggs.23-00239","authors":"Taniguchi K, Kajitani T, Ayano T, Yoshida T, Oki M","authors_abbrev":"Taniguchi K et al.","pubmed_publication_date":"21 Feb 2024","pubmed_entrez_date":"2024-02-21","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-02-23 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30278108","title":"The phenomenon of lipid metabolism \"cut\" mutants.","citation":"Yeast 2018 Dec;35(12):631-637","abstract":"Every cell cycle iteration culminates with the resolution of a mitotic nucleus into a pair of daughter nuclei, which are distributed between the two daughter cells. In the fission yeast Schizosaccharomyces pombe, the faithful division of a mitotic nucleus depends on unperturbed lipogenesis. Upon genetically or chemically induced perturbation of lipid anabolism, S. pombe cells fail to separate the two daughter nuclei and subsequently initiate lethal cytokinesis resulting in the so-called \"cut\" terminal phenotype. Evidence supporting a critical role of lipid biogenesis in successful mitosis in S. pombe has been accumulating for almost two decades, but the exact mechanism explaining the reported observations had been elusive. Recently, several studies established a functional link between biosynthesis of structural phospholipids, nuclear membrane growth, and the fidelity of \"closed\" mitosis in S. pombe. These novel insights suggest a mechanistic explanation for the mitotic defects characteristic for some S. pombe mutants deficient in lipid anabolism and extend our knowledge of metabolic modulation within the context of the cell cycle. In this review, we cover the essential role of lipogenesis in \"closed\" mitosis, focusing mainly on S. pombe as a model system.","doi":"10.1002/yea.3358","authors":"Zach R, Převorovský M","authors_abbrev":"Zach R et al.","pubmed_publication_date":"Dec 2018","pubmed_entrez_date":"2018-10-03","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-10-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17289922","title":"Cdk phosphorylation of the Ste11 transcription factor constrains differentiation-specific transcription to G1.","citation":"Genes Dev 2007 Feb 01;21(3):347-59","abstract":"Eukaryotic cells normally differentiate from G(1); here we investigate the mechanism preventing expression of differentiation-specific genes outside G(1). In fission yeast, induction of the transcription factor Ste11 triggers sexual differentiation. We find that Ste11 is only active in G(1) when Cdk activity is low. In the remaining part of the cell cycle, Ste11 becomes Cdk-phosphorylated at Thr 82 (T82), which inhibits its DNA-binding activity. Since the ste11 gene is autoregulated and the Ste11 protein is highly unstable, this Cdk switch rapidly extinguishes Ste11 activity when cells enter S phase. When we mutated T82 to aspartic acid, mimicking constant phosphorylation, cells no longer underwent differentiation. Conversely, changing T82 to alanine rendered Ste11-controlled transcription constitutive through the cell cycle, and allowed mating from S phase with increased frequency. Thus, Cdk phosphorylation mediates periodic expression of Ste11 and its target genes, and we suggest this to be part of the mechanism restricting differentiation to G(1).","authors":"Kjaerulff S, Andersen NR, Borup MT, Nielsen O","authors_abbrev":"Kjaerulff S et al.","pubmed_publication_date":"01 Feb 2007","pubmed_entrez_date":"2007-02-10","publication_year":"2007","canto_session_key":"c16da7bb96d51f56","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21118960","title":"The fission yeast rDNA-binding protein Reb1 regulates G1 phase under nutritional stress.","citation":"J Cell Sci 2011 Jan 01;124(Pt 1):25-34","abstract":"Yeast Reb1 and its mammalian ortholog TTF1 are conserved Myb-type DNA-binding proteins that bind to specific sites near the 3'-end of rRNA genes (rDNA). Here, they participate in the termination of transcription driven by RNA polymerase I and block DNA replication forks approaching in the opposite direction. We found that Schizosaccharomyces pombe Reb1 also upregulates transcription of the ste9(+) gene that is required for nitrogen-starvation-induced growth arrest with a G1 DNA content and sexual differentiation. Ste9 activates the anaphase-promoting complex or cyclosome ('APC/C') in G1, targeting B-cyclin for proteasomal degradation in response to nutritional stress. Reb1 binds in vivo and in vitro to a specific DNA sequence at the promoter of ste9(+), similar to the sequence recognized in the rDNA, and this binding is required for ste9(+) transcriptional activation and G1 arrest. This suggests that Reb1 acts as a link between rDNA metabolism and cell cycle control in response to nutritional stress. In agreement with this new role for Reb1 in the regulation of the G1-S transition, reb1Δ and wee1(ts) mutations are synthetically lethal owing to the inability of these cells to lengthen G1 before entering S phase. Similarly, reb1Δ cdc10(ts) cells are unable to arrest in G1 and die at the semi-permissive temperature.","doi":"10.1242/jcs.070987","authors":"Rodríguez-Sánchez L, Rodríguez-López M, García Z, Tenorio-Gómez M, Schvartzman JB, Krimer DB, Hernández P","authors_abbrev":"Rodríguez-Sánchez L et al.","pubmed_publication_date":"01 Jan 2011","pubmed_entrez_date":"2010-12-02","publication_year":"2011","canto_session_key":"f372ba194a5d127c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-19 16:46:27","canto_approved_date":"2022-06-01 15:25:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-17 14:19:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC1198.11c","SPAC144.13c","SPCC18B5.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-03-19"},{"uniquename":"PMID:11790253","title":"Computational prediction of membrane-tethered transcription factors.","citation":"Genome Biol 2001;2(12):RESEARCH0050","abstract":"Sequestration of transcription factors in the membrane is emerging as an important mechanism for the regulation of gene expression. A handful of membrane-spanning transcription factors has been previously identified whose access to the nucleus is regulated by proteolytic cleavage from the membrane. To investigate the existence of other transmembrane transcription factors, we analyzed computationally all proteins in SWISS-PROT/TrEMBL for the combined presence of a DNA-binding domain and a transmembrane segment.\nUsing Pfam hidden Markov models and four transmembrane-prediction programs, we identified with high confidence 76 membrane-spanning transcription factors in SWISS-PROT/TrEMBL. Analysis of the distribution of two proteins predicted by our method, MTJ1 and DMRT2, confirmed their localization to intracellular membrane compartments. Furthermore, elimination of the predicted transmembrane segment led to nuclear localization for each of these proteins.\nOur analysis uncovered a wealth of predicted membrane-spanning transcription factors that are structurally and taxonomically diverse, 56 of which lack experimental annotation. Seventy-five of the proteins are modular in structure, suggesting that a single proteolysis may be sufficient to liberate a DNA-binding domain from the membrane. This study provides grounds for investigations into the stimuli and mechanisms that release this intriguing class of transcription factors from membranes.","authors":"Zupicich J, Brenner SE, Skarnes WC","authors_abbrev":"Zupicich J et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2002-01-16","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:11:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP8B7.30c","SPBC19C2.09","SPBC354.05c","SPBC530.08"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:10855500","title":"Characterization of fission yeast meiotic mutants based on live observation of meiotic prophase nuclear movement.","citation":"Chromosoma 2000;109(1-2):103-9","abstract":"We characterized four meiotic mutants of the fission yeast Schizosaccharomyces pombe by live observation of nuclear movement. Nuclei were stained with either the DNA-specific fluorescent dye Hoechst 33342 or jellyfish green fluorescent protein (GFP) fused with the N-terminal portion of DNA polymerase alpha. We first followed nuclear dynamics in wild-type cells to determine the temporal sequence of meiotic events: nuclear fusion in the conjugated zygote is immediately followed by oscillatory nuclear movements that continue for 146 min; then, after coming to rest, the nucleus remains in the center of the cell for 26 min before the first meiotic division. Next we examined nuclear dynamics in four meiotic mutants: mei1 (also called mat2), mei4, dhc1, and taz1. Mei1 and mei4 both arrest during meiotic prophase; our observations, however, show that the timing of mei1 arrest is quite different from that of mei4: the mei1 mutant arrests after nuclear fusion but before starting the oscillatory nuclear movements, while the mei4 mutant arrests after the nucleus has completed the oscillatory movements but before the first meiotic division. We also show examples of the dynamic phenotypes of dhc1 and taz1, both of which complete meiosis but exhibit impaired nuclear movement and reduced frequencies of homologous recombination: the dhc1 mutant exhibits no nuclear movement after nuclear fusion, while the taz1 mutant exhibits severely impaired nuclear movement after nuclear fusion.","authors":"Hiraoka Y, Ding DQ, Yamamoto A, Tsutsumi C, Chikashige Y","authors_abbrev":"Hiraoka Y et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-06-16","publication_year":"2000","canto_session_key":"e77e5856b18646d5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-17 08:32:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-17 08:32:28","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPMTR.02","SPBC32H8.11","SPAC16A10.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-10-17"},{"uniquename":"PMID:40013339","title":"Macromolecular and cytological changes in fission yeast G0 nuclei.","citation":"J Cell Sci 2025 Feb 27;","abstract":"When starved of nitrogen, fission yeast Schizosaccharomyces pombe cells enter a quiescent \"G0\" state with smaller nuclei and transcriptional repression. The genomics of S. pombe G0 cells has been well studied, but much of its nuclear cell biology remains unknown. Here we use confocal microscopy, immunoblots, and electron cryotomography to investigate the cytological, biochemical, and ultrastructural differences between S. pombe proliferating, G1-arrested, and G0 cell nuclei, with an emphasis on the histone acetylation, RNA polymerase II fates, and macromolecular complex packing. Compared to proliferating cells, G0 cells have lower levels of histone acetylation, nuclear RNA polymerase II, and active transcription. The G0 nucleus has similar macromolecular crowding yet fewer chromatin-associated multi-megadalton globular complexes. Induced histone hyperacetylation during nitrogen starvation results in cells that have larger nuclei and therefore less compact chromatin. However, these histone-hyperacetylated cells remain transcriptionally repressed with similar nuclear crowding. Canonical nucleosomes - those that resemble the crystal structure - are rare in proliferating, G1-arrested, and G0 cells. Our study therefore shows that extreme changes in nucleus physiology are possible without extreme reorganisation at the macromolecular level.","doi":"10.1242/jcs.263654","authors":"Tan ZY, Cai S, Paithankar SA, Liu T, Nie X, Shi J, Gan L","authors_abbrev":"Tan ZY et al.","pubmed_publication_date":"27 Feb 2025","pubmed_entrez_date":"2025-02-27","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-02-28 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5139537","title":"Study of adenine aminohydrolase in the yeast, Schizosaccharomyces pombe.","citation":"J Bacteriol 1971 Dec;108(3):959-63","abstract":"Observation of the growth of some adenineless mutants of Schizosaccharomyces pombe on six substituted purine analogs leads to the hypothesis that an enzyme is present which catalyzes the conversion of these analogs into hypoxanthine. The enzyme adenase (adenine aminohydrolase, EC 3.5.4.2) has been found to be active in cell-free extracts of S. pombe. Results are reported which are in agreement with the hypothesis that this enzyme is responsible for the in vivo utilization of 6-chloropurine. This evidence comes mainly from a study of adenine aminohydrolase in two mutants selected for partial inability to grow on 6-chloropurine.","authors":"Abbondandolo A, Weyer A, Heslot H, Lambert M","authors_abbrev":"Abbondandolo A et al.","pubmed_publication_date":"Dec 1971","pubmed_entrez_date":"1971-12-01","publication_year":"1971","canto_session_key":"97212020adb41cb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-09 11:27:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-03 14:50:15","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC405.01","SPBC1198.02"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2013-09-03"},{"uniquename":"PMID:19373772","title":"The dynamin related protein Dnm1 fragments mitochondria in a microtubule-dependent manner during the fission yeast cell cycle.","citation":"Cell Motil Cytoskeleton 2009 Aug;66(8):509-23","abstract":"Mitochondria are dynamic organelles that undergo cycles of fission and fusion. In the fission yeast, Schizosaccharomyces pombe, mitochondria align with microtubules and mitochondrial integrity is dependent upon an intact microtubule cytoskeleton. Here we show that mitochondria re-organize during the cell cycle and that this process is both dynamin- and microtubule-dependent. Microtubule depolymerization results in mitochondrial fragmentation but only when the dynamin-related protein Dnm1 is present. Mitochondrial fusion is, on the other hand, microtubule-independent. dnm1Delta cells, besides showing extensively fused mitochondria, are specifically resistant to anti-microtubule drugs. Dnm1-YFP localizes to foci at sites of mitochondrial severing which occupy the interface between adjacent nucleoids, suggesting the existence of defined mitochondrial \"territories,\" each of which contains a nucleoid. Such territories are lost in dnm1Delta in which nucleoids become aggregated. Mitochondrial ends exhibit motile behavior, extending towards and retracting from the cell poles, independently of the cytoskeleton. We conclude that: (a) mitochondria are organized by microtubules in fission yeast but are not moved by them; (b) Dnm1 mediates mitochondrial fission during interphasic growth and at cell division; (c) the interaction between microtubules and mitochondria, either directly or indirectly via Dnm1, not only modifies the disposition of mitochondria it also modifies the behavior of microtubules. Cell Motil. Cytoskeleton 2009. (c) 2009 Wiley-Liss, Inc.","doi":"10.1002/cm.20351","authors":"Jourdain I, Gachet Y, Hyams JS","authors_abbrev":"Jourdain I et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-04-18","publication_year":"2009","canto_session_key":"fa7f755050797623","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-21 12:07:25","canto_approved_date":"2020-04-09 12:56:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-11 12:15:17","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.08","SPBC26H8.07c","SPAC767.01c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-04-21"},{"uniquename":"PMID:10373512","title":"Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals.","citation":"Mol Cell Biol 1999 Jul;19(7):4633-42","abstract":"Germ line mutations in the breast cancer susceptibility gene BRCA2 predispose to early-onset breast cancer, but the function of the nuclear protein encoded by the gene is ill defined. Using the yeast two-hybrid system with fragments of human BRCA2, we identified an interaction with the human DSS1 (deleted in split hand/split foot) gene. Yeast and mammalian two-hybrid assays showed that DSS1 can associate with BRCA2 in the region of amino acids 2472 to 2957 in the C terminus of the protein. Using coimmunoprecipitation of epitope-tagged BRCA2 and DSS1 cDNA constructs transiently expressed in COS cells, we were able to demonstrate an association. Furthermore, endogenous BRCA2 could be coimmunoprecipitated with endogenous DSS1 in MCF7 cells, demonstrating an in vivo association. Apparent orthologues of the mammalian DSS1 gene were identified in the genome of the yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae. Yeast strains in which these DSS1-like genes were deleted showed a temperature-sensitive growth phenotype, which was analyzed by flow cytometry. This provides evidence for a link between the BRCA2 tumor suppressor gene and a gene required for completion of the cell cycle.","authors":"Marston NJ, Richards WJ, Hughes D, Bertwistle D, Marshall CJ, Ashworth A","authors_abbrev":"Marston NJ et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-06-22","publication_year":"1999","canto_session_key":"c0eafe0487f4e960","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-05-21 12:51:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-04-25 06:35:42","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-04-25"},{"uniquename":"PMID:22968950","title":"A new versatile system for rapid control of gene expression in the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2012 Oct;29(10):425-34","abstract":"The ability to regulate the expression of a gene greatly aids the process of uncovering its functions. The fission yeast Schizosaccharomyces pombe has so far lacked a system for rapidly controlling the expression of chromosomal genes, hindering its full potential as a model organism. Although the widely used nmt1 promoter displays a wide dynamic range of activity, it takes > 14-15 h to derepress. The urg1 promoter also shows a large dynamic range and can be induced quickly (< 2 h), but its implementation requires laborious strain construction and it cannot be used to study meiosis. To overcome these limitations, we constructed a tetracycline-regulated system for inducible expression of chromosomal genes in fission yeast, which is easily established and implemented. In this system the promoter of a gene is replaced by simple one-step substitution techniques with a tetracycline-regulated promoter cassette (tetO(7) -TATA(CYC1) ) in cells where TetR/TetR'-based transcription activators/repressors are also produced. Using top1 and nse6 as reporter genes, we show that Top1 and Nse6 appear after just 30 min of activating tetO(7) -TATA(CYC1) and plateau after -4-6 h. The amount of synthesised protein is comparable to that produced from the attenuated nmt1 promoter P(nmt8) , which should be closer to wild-type levels for most genes than those generated from excessively strong promoters and can be controlled by changing the concentration of the effector antibiotic. This system also works efficiently during meiosis, thus making it a useful addition to the toolkit of the fission yeast community.","doi":"10.1002/yea.2920","authors":"Zilio N, Wehrkamp-Richter S, Boddy MN","authors_abbrev":"Zilio N et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-09-13","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23934111","title":"De novo mutations in epileptic encephalopathies.","citation":"Nature 2013 Sep 12;501(7466):217-21","abstract":"Epileptic encephalopathies are a devastating group of severe childhood epilepsy disorders for which the cause is often unknown. Here we report a screen for de novo mutations in patients with two classical epileptic encephalopathies: infantile spasms (n = 149) and Lennox-Gastaut syndrome (n = 115). We sequenced the exomes of 264 probands, and their parents, and confirmed 329 de novo mutations. A likelihood analysis showed a significant excess of de novo mutations in the ∼4,000 genes that are the most intolerant to functional genetic variation in the human population (P = 2.9 × 10(-3)). Among these are GABRB3, with de novo mutations in four patients, and ALG13, with the same de novo mutation in two patients; both genes show clear statistical evidence of association with epileptic encephalopathy. Given the relevant site-specific mutation rates, the probabilities of these outcomes occurring by chance are P = 4.1 × 10(-10) and P = 7.8 × 10(-12), respectively. Other genes with de novo mutations in this cohort include CACNA1A, CHD2, FLNA, GABRA1, GRIN1, GRIN2B, HNRNPU, IQSEC2, MTOR and NEDD4L. Finally, we show that the de novo mutations observed are enriched in specific gene sets including genes regulated by the fragile X protein (P < 10(-8)), as has been reported previously for autism spectrum disorders.","doi":"10.1038/nature12439","authors":"Epi4K Consortium, Epilepsy Phenome/Genome Project, Allen AS, Berkovic SF, Cossette P, Delanty N, Dlugos D, Eichler EE, Epstein MP, Glauser T, Goldstein DB, Han Y, Heinzen EL, Hitomi Y, Howell KB, Johnson MR, Kuzniecky R, Lowenstein DH, Lu YF, Madou MR, Marson AG, Mefford HC, Esmaeeli Nieh S, O'Brien TJ, Ottman R, Petrovski S, Poduri A, Ruzzo EK, Scheffer IE, Sherr EH, Yuskaitis CJ, Abou-Khalil B, Alldredge BK, Bautista JF, Berkovic SF, Boro A, Cascino GD, Consalvo D, Crumrine P, Devinsky O, Dlugos D, Epstein MP, Fiol M, Fountain NB, French J, Friedman D, Geller EB, Glauser T, Glynn S, Haut SR, Hayward J, Helmers SL, Joshi S, Kanner A, Kirsch HE, Knowlton RC, Kossoff EH, Kuperman R, Kuzniecky R, Lowenstein DH, McGuire SM, Motika PV, Novotny EJ, Ottman R, Paolicchi JM, Parent JM, Park K, Poduri A, Scheffer IE, Shellhaas RA, Sherr EH, Shih JJ, Singh R, Sirven J, Smith MC, Sullivan J, Lin Thio L, Venkat A, Vining EP, Von Allmen GK, Weisenberg JL, Widdess-Walsh P, Winawer MR","authors_abbrev":"Epi4K Consortium et al.","pubmed_publication_date":"12 Sep 2013","pubmed_entrez_date":"2013-08-13","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC56E4.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17440621","title":"Genome-wide studies of histone demethylation catalysed by the fission yeast homologues of mammalian LSD1.","citation":"PLoS One 2007 Apr 18;2(4):e386","abstract":"In order to gain a more global view of the activity of histone demethylases, we report here genome-wide studies of the fission yeast SWIRM and polyamine oxidase (PAO) domain homologues of mammalian LSD1. Consistent with previous work we find that the two S. pombe proteins, which we name Swm1 and Swm2 (after SWIRM1 and SWIRM2), associate together in a complex. However, we find that this complex specifically demethylates lysine 9 in histone H3 (H3K9) and both up- and down-regulates expression of different groups of genes. Using chromatin-immunoprecipitation, to isolate fragments of chromatin containing either H3K4me2 or H3K9me2, and DNA microarray analysis (ChIP-chip), we have studied genome-wide changes in patterns of histone methylation, and their correlation with gene expression, upon deletion of the swm1(+) gene. Using hyper-geometric probability comparisons we uncover genetic links between lysine-specific demethylases, the histone deacetylase Clr6, and the chromatin remodeller Hrp1. The data presented here demonstrate that in fission yeast the SWIRM/PAO domain proteins Swm1 and Swm2 are associated in complexes that can remove methyl groups from lysine 9 methylated histone H3. In vitro, we show that bacterially expressed Swm1 also possesses lysine 9 demethylase activity. In vivo, loss of Swm1 increases the global levels of both H3K9me2 and H3K4me2. A significant accumulation of H3K4me2 is observed at genes that are up-regulated in a swm1 deletion strain. In addition, H3K9me2 accumulates at some genes known to be direct Swm1/2 targets that are down-regulated in the swm1Delta strain. The in vivo data indicate that Swm1 acts in concert with the HDAC Clr6 and the chromatin remodeller Hrp1 to repress gene expression. In addition, our in vitro analyses suggest that the H3K9 demethylase activity requires an unidentified post-translational modification to allow it to act. Thus, our results highlight complex interactions between histone demethylase, deacetylase and chromatin remodelling activities in the regulation of gene expression.","authors":"Opel M, Lando D, Bonilla C, Trewick SC, Boukaba A, Walfridsson J, Cauwood J, Werler PJ, Carr AM, Kouzarides T, Murzina NV, Allshire RC, Ekwall K, Laue ED","authors_abbrev":"Opel M et al.","pubmed_publication_date":"18 Apr 2007","pubmed_entrez_date":"2007-04-19","publication_year":"2007","canto_session_key":"628c4060d26880cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-06 22:31:49","canto_approved_date":"2023-04-17 08:50:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-27 10:52:51","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23E2.02","SPCC4G3.07c","SPAC30D11.08c","SPBC146.09c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-03-06"},{"uniquename":"PMID:10947840","title":"Mis3 with a conserved RNA binding motif is essential for ribosome biogenesis and implicated in the start of cell growth and S phase checkpoint.","citation":"Genes Cells 2000 Jul;5(7):525-41","abstract":"In normal somatic cell cycle, growth and cell cycle are properly coupled. Although CDK (cyclin-dependent kinase) activity is known to be essential for cell cycle control, the mechanism to ensure the coupling has been little understood.\nWe here show that fission yeast Mis3, a novel evolutionarily highly conserved protein with the RNA-interacting KH motif, is essential for ribosome RNA processing, and implicated in initiating the cell growth. Growth arrest of mis3-224, a temperature sensitive mutant at the restrictive temperature, coincides with the early G2 block in the complete medium or the G1/S block in the release from nitrogen starvation, reflecting coupling of cell growth and division. Genetic interactions indicated that Mis3 shares functions with cell cycle regulators and RNA processing proteins, and is under the control of Dsk1 kinase and PP1 phosphatase. Mis3 is needed for the formation of 18S ribosome RNA, and may hence direct the level of proteins required for the coupling. One such candidate is Mik1 kinase. mis3-224 is sensitive to hydroxyurea, and the level of Mik1 protein increases during replication checkpoint in a manner dependent upon the presence of Mis3 and Cds1.\nMis3 is essential for ribosome biogenesis, supports S phase checkpoint, and is needed for the coupling between growth and cell cycle. Whether Mis3 interacts solely with ribosomal precursor RNA remains to be determined.","authors":"Kondoh H, Yuasa T, Yanagida M","authors_abbrev":"Kondoh H et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-08-18","publication_year":"2000","canto_session_key":"388045986ed63280","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-05-22 07:03:01","canto_approved_date":"2024-05-22 07:03:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-17 15:38:18","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.10","SPCC18B5.11c","SPBC25B2.05","SPBC582.03","SPAC24H6.05","SPBC776.02c","SPCC18B5.03","SPBC660.14","SPBC530.14c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2024-05-22"},{"uniquename":"PMID:26263485","title":"Comparative biology of cell division in the fission yeast clade.","citation":"Curr Opin Microbiol 2015 Dec;28:18-25","abstract":"Cytokinesis must be regulated in time and space in order to preserve genome integrity during cell proliferation and to allow daughter cells to adopt distinct fates and geometries during differentiation. The fission yeast Schizosaccharomyces pombe has been a popular model organism for understanding spatiotemporal regulation of cytokinesis in a symmetrically dividing cell. Recent work on another member of the same genus, Schisozaccharomyces japonicus, suggests that S. pombe may have evolved an unusual division site placement mechanism based on a recently duplicated anillin paralog. Here we discuss an extraordinary evolutionary plasticity of cytokinesis within the fission yeast clade and argue that the comparative cell biology approach may provide functional insights beyond those afforded by scrutinizing individual model species.","doi":"10.1016/j.mib.2015.07.011","authors":"Gu Y, Oliferenko S","authors_abbrev":"Gu Y et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-08-12","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-08-13 00:20:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33670267","title":"The Role of Non-Catalytic Domains of Hrp3 in Nucleosome Remodeling.","citation":"Int J Mol Sci 2021 Feb 11;22(4)","abstract":"The Helicase-related protein 3 (Hrp3), an ATP-dependent chromatin remodeling enzyme from the CHD family, is crucial for maintaining global nucleosome occupancy in  Schizosaccharomyces pombe  ( S. pombe) . Although the ATPase domain of Hrp3 is essential for chromatin remodeling, the contribution of non-ATPase domains of Hrp3 is still unclear. Here, we investigated the role of non-ATPase domains using in vitro methods. In our study, we expressed and purified recombinant  S. pombe  histone proteins, reconstituted them into histone octamers, and assembled nucleosome core particles. Using reconstituted nucleosomes and affinity-purified wild type and mutant Hrp3 from  S. pombe  we created a homogeneous in vitro system to evaluate the ATP hydrolyzing capacity of truncated Hrp3 proteins. We found that all non-ATPase domain deletions (∆chromo, ∆SANT, ∆SLIDE, and ∆coupling region) lead to reduced ATP hydrolyzing activities in vitro with DNA or nucleosome substrates. Only the coupling region deletion showed moderate stimulation of ATPase activity with the nucleosome. Interestingly, affinity-purified Hrp3 showed co-purification with all core histones suggesting a strong association with the nucleosomes in vivo. However, affinity-purified Hrp3 mutant with SANT and coupling regions deletion showed complete loss of interactions with the nucleosomes, while SLIDE and chromodomain deletions reduced Hrp3 interactions with the nucleosomes. Taken together, nucleosome association and ATPase stimulation by DNA or nucleosomes substrate suggest that the enzymatic activity of Hrp3 is fine-tuned by unique contributions of all four non-catalytic domains.","doi":"10.3390/ijms22041793","authors":"Dong W, Prasad P, Lennartsson A, Ekwall K","authors_abbrev":"Dong W et al.","pubmed_publication_date":"11 Feb 2021","pubmed_entrez_date":"2021-03-06","publication_year":"2021","canto_session_key":"4ca3e303dba088f4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Karl Ekwall","canto_first_approved_date":"2021-04-14 09:59:02","canto_approved_date":"2025-05-28 12:58:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-08 08:38:53","canto_added_date":"2021-03-08 01:15:08","annotation_curators":[{"name":"Karl Ekwall","community_curator":true,"annotation_count":8,"orcid":"0000-0002-3029-4041","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.01","SPAC19G12.06c","SPAC1834.03c","SPBC1105.12","SPAC1834.04","SPBC8D2.04","SPCC622.08c","SPBC1105.11c","SPBC8D2.03c","SPCC622.09"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2021-04-14"},{"uniquename":"PMID:22586155","title":"tRNAomics: tRNA gene copy number variation and codon use provide bioinformatic evidence of a new anticodon:codon wobble pair in a eukaryote.","citation":"RNA 2012 Jul;18(7):1358-72","abstract":"tRNA genes are interspersed throughout eukaryotic DNA, contributing to genome architecture and evolution in addition to translation of the transcriptome. Codon use correlates with tRNA gene copy number in noncomplex organisms including yeasts. Synonymous codons impact translation with various outcomes, dependent on relative tRNA abundances. Availability of whole-genome sequences allowed us to examine tRNA gene copy number variation (tgCNV) and codon use in four Schizosaccharomyces species and Saccharomyces cerevisiae. tRNA gene numbers vary from 171 to 322 in the four Schizosaccharomyces despite very high similarity in other features of their genomes. In addition, we performed whole-genome sequencing of several related laboratory strains of Schizosaccharomyces pombe and found tgCNV at a cluster of tRNA genes. We examined for the first time effects of wobble rules on correlation of tRNA gene number and codon use and showed improvement for S. cerevisiae and three of the Schizosaccharomyces species. In contrast, correlation in Schizosaccharomyces japonicus is poor due to markedly divergent tRNA gene content, and much worsened by the wobble rules. In japonicus, some tRNA iso-acceptor genes are absent and others are greatly reduced relative to the other yeasts, while genes for synonymous wobble iso-acceptors are amplified, indicating wobble use not apparent in any other eukaryote. We identified a subset of japonicus-specific wobbles that improves correlation of codon use and tRNA gene content in japonicus. We conclude that tgCNV is high among Schizo species and occurs in related laboratory strains of S. pombe (and expectedly other species), and tRNAome-codon analyses can provide insight into species-specific wobble decoding.","doi":"10.1261/rna.032151.111","authors":"Iben JR, Maraia RJ","authors_abbrev":"Iben JR et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-05-16","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24642412","title":"Cortical regulation of cell size by a sizer cdr2p.","citation":"Elife 2014 Mar 18;3:e02040","abstract":"Cells can, in principle, control their size by growing to a specified size before commencing cell division. How any cell actually senses its own size remains poorly understood. The fission yeast Schizosaccharomyces pombe are rod-shaped cells that grow to ∼14 µm in length before entering mitosis. In this study, we provide evidence that these cells sense their surface area as part of this size control mechanism. We show that cells enter mitosis at a certain surface area, as opposed to a certain volume or length. A peripheral membrane protein kinase cdr2p has properties of a dose-dependent 'sizer' that controls mitotic entry. As cells grow, the local cdr2p concentration in nodes at the medial cortex accumulates as a measure of cell surface area. Our findings, which challenge a previously proposed pom1p gradient model, lead to a new model in which cells sense their size by using cdr2p to probe the surface area over the whole cell and relay this information to the medial cortex. DOI: http://dx.doi.org/10.7554/eLife.02040.001.","doi":"10.7554/eLife.02040","authors":"Pan KZ, Saunders TE, Flor-Parra I, Howard M, Chang F","authors_abbrev":"Pan KZ et al.","pubmed_publication_date":"18 Mar 2014","pubmed_entrez_date":"2014-03-20","publication_year":"2014","canto_session_key":"748a82c3d2466430","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18285637","title":"Gene expression and distribution of Swi6 in partial aneuploids of the fission yeast Schizosaccharomyces pombe.","citation":"Cell Struct Funct 2007;32(2):149-61","abstract":"Imbalances of gene expression in aneuploids, which contain an abnormal number of chromosomes, cause a variety of growth and developmental defects. Aneuploid cells of the fission yeast Schizosaccharomyces pombe are inviable, or very unstable, during mitotic growth. However, S. pombe haploid cells bearing minichromosomes derived from the chromosome 3 can grow stably as a partial aneuploid. To address biological consequences of aneuploidy, we examined the gene expression profiles of partial aneuploid strains using DNA microarray analysis. The expression of genes in disomic or trisomic cells was found to increase approximately in proportion to their copy number. We also found that some genes in the monosomic regions of partial aneuploid strains increased their expression level despite there being no change in copy number. This change in gene expression can be attributed to increased expression of the genes in the disomic or trisomic regions. However, even in an aneuploid strain that bears a minichromosome containing no protein coding genes, genes located within about 50 kb of the telomere showed similar increases in expression, indicating that these changes are not a secondary effect of the increased gene dosage. Examining the distribution of the heterochromoatin protein Swi6 using DNA microarray analysis, we found that binding of Swi6 within ~50 kb from the telomere occurred less in partial aneuploid strains compared to euploid strains. These results suggest that additional chromosomes in aneuploids could lead to imbalances in gene expression through changes in distribution of heterochromatin as well as in gene dosage.","authors":"Chikashige Y, Tsutsumi C, Okamasa K, Yamane M, Nakayama J, Niwa O, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2008-02-21","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10467004","title":"A novel group-II intron in the cox1 gene of the fission yeast Schizosaccharomyces pombe is inserted in the same codon as the mobile group-II intron aI2 in the Saccharomyces cerevisiae cox1 homologue.","citation":"Curr Genet 1999 Jul;35(6):602-8","abstract":"We describe herein a large group-II intron which is inserted in the mitochondrial cox1 gene of the Schizosaccharomyces pombe strain EF2. The intron RNA consists of 2492 nucleotides which can be folded into a secondary structure with all the expected sequence motifs of subgroup-IIA1 introns (Michel et al. 1989). Determination of the exact splice point revealed that the intron is inserted in the same codon, but 1 bp downstream, as the mobile intron aI2 in the Saccharomyces cerevisiae cox1 homologue. A total of nine nucleotide changes was observed around the insertion site of the intron in the cox1 gene of strain EF2 compared with the reference strain ade7-50h(-). Seven of these changes are clustered within the 51 bp upstream of the splice point. Only one sequence deviation was found in the downstream exon. The intron is capable of splicing despite the fact that both the EBS1/IBS1 and the EBS2/IBS2 sequence motifs, thought to be necessary for correct splicing, extend over 5 instead of 6 bp. The maturase, endonuclease and reverse transcriptase domains of the putative protein encoded by the newly described S. pombe group-II intron were not closer to those encoded by the other two, cobI and cox2I, S. pombe group-II introns than to the group-II intron-encoded proteins in Allomyces, Marchantia, Podospora and Saccharomyces.","authors":"Schäfer B, Wolf K","authors_abbrev":"Schäfer B et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-08-31","publication_year":"1999","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32474823","title":"Ends and middle: Global force balance and septum location in fission yeast.","citation":"Eur Phys J E Soft Matter 2020 May 29;43(5):31","abstract":"The fission yeast cell is shaped as a very regular cylinder ending by hemi-spheres at both cell ends. Its conserved phenotypes are often used as read-outs for classifying interacting genes and protein networks. Using Pascal and Young-Laplace laws, we proposed a framework where scaling arguments predicted shapes. Here we probed quantitatively one of these relations which predicts that the division site would be located closer to the cell end with the larger radius of curvature. By combining genetics and quantitative imaging, we tested experimentally whether altered shapes of cell end correlate with a displaced division site, leading to asymmetric cell division. Our results show that the division site position depends on the radii of curvatures of both ends. This new geometrical mechanism for the proper division plane positioning could be essential to achieve even partitioning of cellular material at each cell division.","doi":"10.1140/epje/i2020-11955-x","authors":"Le Goff X, Comelles J, Kervrann C, Riveline D","authors_abbrev":"Le Goff X et al.","pubmed_publication_date":"29 May 2020","pubmed_entrez_date":"2020-06-01","publication_year":"2020","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2020-06-02 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22683269","title":"HP1(Swi6) mediates the recognition and destruction of heterochromatic RNA transcripts.","citation":"Mol Cell 2012 Jul 27;47(2):215-27","abstract":"HP1 proteins are major components of heterochromatin, which is generally perceived to be an inert and transcriptionally inactive chromatin structure. Yet, HP1 binding to chromatin is highly dynamic and robust silencing of heterochromatic genes can involve RNA processing. Here, we demonstrate by a combination of in vivo and in vitro experiments that the fission yeast HP1(Swi6) protein guarantees tight repression of heterochromatic genes through RNA sequestration and degradation. Stimulated by positively charged residues in the hinge region, RNA competes with methylated histone H3K9 for binding to the chromodomain of HP1(Swi6). Hence, HP1(Swi6) binding to RNA is incompatible with stable heterochromatin association. We propose a model in which an ensemble of HP1(Swi6) proteins functions as a heterochromatin-specific checkpoint, capturing and priming heterochromatic RNAs for the RNA degradation machinery. Sustaining a functional checkpoint requires continuous exchange of HP1(Swi6) within heterochromatin, which explains the dynamic localization of HP1 proteins on heterochromatin.","doi":"10.1016/j.molcel.2012.05.009","authors":"Keller C, Adaixo R, Stunnenberg R, Woolcock KJ, Hiller S, Bühler M","authors_abbrev":"Keller C et al.","pubmed_publication_date":"27 Jul 2012","pubmed_entrez_date":"2012-06-12","publication_year":"2012","canto_session_key":"5bf20875f2c283f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-02-08 17:45:31","canto_approved_date":"2025-09-04 06:26:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-11 16:10:15","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.11c","SPBC8D2.04","SPAC1834.04","SPAC12G12.13c","SPAC664.01c","SPBC428.08c","SPCC188.13c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-02-08"},{"uniquename":"PMID:9923681","title":"Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein.","citation":"Nature 1999 Jan 14;397(6715):172-5","abstract":"DNA damage activates a cell-cycle checkpoint that prevents mitosis while DNA repair is under way. The protein Chk1 enforces this checkpoint by phosphorylating the mitotic inducer Cdc25. Phosphorylation of Cdc25 by Chk1 creates a binding site in Cdc25 for 14-3-3 proteins, but it is not known how 14-3-3 proteins regulate Cdc25. Rad24 is a 14-3-3 protein that is important in the DNA-damage checkpoint in fission yeast. Here we show that Rad24 controls the intracellular distribution of Cdc25. Elimination of Rad24 causes nuclear accumulation of Cdc25. Activation of the DNA-damage checkpoint causes the net nuclear export of Cdc25 by a process that requires Chk1, Rad24 and nuclear-export machinery. Mutation of a putative nuclear-export signal in Rad24 impairs the nuclear exclusion of Rad24, the damage-induced nuclear export of Cdc25 and the damage checkpoint. Thus, Rad24 appears to function as an attachable nuclear-export signal that enhances the nuclear export of Cdc25 in response to DNA damage.","authors":"Lopez-Girona A, Furnari B, Mondesert O, Russell P","authors_abbrev":"Lopez-Girona A et al.","pubmed_publication_date":"14 Jan 1999","pubmed_entrez_date":"1999-01-29","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPAC24H6.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:20175747","title":"Rho GTPases: regulation of cell polarity and growth in yeasts.","citation":"Biochem J 2010 Feb 24;426(3):243-53","abstract":"Eukaryotic cells display a wide range of morphologies important for cellular function and development. A particular cell shape is made via the generation of asymmetry in the organization of cytoskeletal elements, usually leading to actin localization at sites of growth. The Rho family of GTPases is present in all eukaryotic cells, from yeast to mammals, and their role as key regulators in the signalling pathways that control actin organization and morphogenetic processes is well known. In the present review we will discuss the role of Rho GTPases as regulators of yeasts' polarized growth, their mechanism of activation and signalling pathways in Saccharomyces cerevisiae and Schizosaccharomyces pombe. These two model yeasts have been very useful in the study of the molecular mechanisms responsible for cell polarity. As in other organisms with cell walls, yeast's polarized growth is closely related to cell-wall biosynthesis, and Rho GTPases are critical modulators of this process. They provide the co-ordinated regulation of cell-wall biosynthetic enzymes and actin organization required to maintain cell integrity during vegetative growth.","doi":"10.1042/BJ20091823","authors":"Perez P, Rincón SA","authors_abbrev":"Perez P et al.","pubmed_publication_date":"24 Feb 2010","pubmed_entrez_date":"2010-02-24","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB191155","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8842148","title":"Cell cycle, DNA damage and heat shock regulate suc22+ expression in fission yeast.","citation":"Mol Gen Genet 1996 Sep 13;252(3):284-91","abstract":"The suc22+ gene of Schizosaccharomyces pombe encodes the small subunit of ribonucleotide reductase. Two transcripts that hybridise to suc22+ have previously been described: a constitutive transcript of 1.5 kb, and a transcript of approximately 1.9 kb that is induced when DNA replication is blocked by hydroxyurea. In this paper we show that both transcripts derive from the suc22+ gene, are polyadenylated, and have transcription initiation sites separated by approximately 550 nucleotides. The absence of translation initiation codons and predicted intron splice sites within this 550 nucleotide region suggests strongly that both transcripts encode the same protein. Under normal growth conditions, the larger suc22+ transcript is present at a very low level. This low level expression is periodic during the cell cycle, showing a pattern similar to that of other genes under regulation by MCB elements with a maximum in G1/S phase. Consistent with this, there are MCB elements upstream of the initiation site of the transcript. This pattern of expression contrasts with the continuous expression, at a much higher level, of the smaller suc22+ transcript. The larger suc22+ transcript is induced by exposure of cells to 4-nitroquinoline oxide (4-NQO),a UV-mimetic agent that causes DNA damage. The transcriptional response to 4-NQO is observed in cells previously arrested in G2 by a cdc2ts mutation, demonstrating that induction can occur outside S phase. We show that the rad1+ gene, part of the mitotic checkpoint, is required for induction of the large transcript. Exposure of cells to heat shock also induces the suc22+ large transcript: a consensus heat shock element has been identified upstream of the large transcript start site.","authors":"Harris P, Kersey PJ, McInerny CJ, Fantes PA","authors_abbrev":"Harris P et al.","pubmed_publication_date":"13 Sep 1996","pubmed_entrez_date":"1996-09-13","publication_year":"1996","canto_session_key":"037ecacfc05e7bdd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-06-24 12:10:37","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-23 17:33:41","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPAC1952.07","SPBC25D12.04"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2014-06-23"},{"uniquename":"PMID:18430926","title":"Schizosaccharomyces pombe Hsp90/Git10 is required for glucose/cAMP signaling.","citation":"Genetics 2008 Apr;178(4):1927-36","abstract":"The fission yeast Schizosaccharomyces pombe senses environmental glucose through a cAMP-signaling pathway. Elevated cAMP levels activate protein kinase A (PKA) to inhibit transcription of genes involved in sexual development and gluconeogenesis, including the fbp1(+) gene, which encodes fructose-1,6-bisphosphatase. Glucose-mediated activation of PKA requires the function of nine glucose-insensitive transcription (git) genes, encoding adenylate cyclase, the PKA catalytic subunit, and seven \"upstream\" proteins required for glucose-triggered adenylate cyclase activation. We describe the cloning and characterization of the git10(+) gene, which is identical to swo1(+) and encodes the S. pombe Hsp90 chaperone protein. Glucose repression of fbp1(+) transcription is impaired by both git10(-) and swo1(-) mutant alleles of the hsp90(+) gene, as well as by chemical inhibition of Hsp90 activity and temperature stress to wild-type cells. Unlike the swo1(-) mutant alleles, the git10-201 allele supports cell growth at 37 degrees , while severely reducing glucose repression of an fbp1-lacZ reporter, suggesting a separation-of-function defect. Sequence analyses of three swo1(-) alleles and the one git10(-) allele indicate that swo1(-) mutations alter core functional domains of Hsp90, while the git10(-) mutation affects the Hsp90 central domain involved in client protein binding. These results suggest that Hsp90 plays a specific role in the S. pombe glucose/cAMP pathway.","doi":"10.1534/genetics.107.086165","authors":"Alaamery MA, Hoffman CS","authors_abbrev":"Alaamery MA et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-04-24","publication_year":"2008","canto_session_key":"40c52ec90ce2de0e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Charlie Hoffman","canto_first_approved_date":"2016-02-25 16:48:27","canto_approved_date":"2021-11-04 13:48:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-18 17:10:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Charlie Hoffman","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.07","SPBC21C3.20c","SPBC36.12c","SPBC1198.14c","SPAC926.04c","SPBC19C7.03"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2016-02-25"},{"uniquename":"PMID:10911361","title":"Transcriptional silencing in fission yeast.","citation":"J Cell Physiol 2000 Sep;184(3):311-8","abstract":"In eukaryotes, epigenetic events govern diverse processes, ranging from gene expression to other aspects of global chromosome architecture essential for preserving the integrity of the genome. Transcriptional silencing at the mating-type locus, centromeres, and telomeres of the fission yeast is regulated by epigenetic mechanisms. Epigenetic states are inherited in cis during mitosis and, remarkably, even through meiosis. Several trans-acting genes that affect silencing are found to encode either chromatin proteins such as chromodomain proteins Swi6 and Clr4 or the factors that affect chromatin assembly, including histone deacetylase homologs Clr3 and Clr6. A recent study showed that Swi6 is involved in imprinting at the mating-type locus and contributes to the cellular memory responsible for maintenance of the silenced state. The \"gene\" in this instance thus comprises DNA plus the associated Swi6-containing protein complex.","authors":"Grewal SI","authors_abbrev":"Grewal SI","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-07-27","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10574765","title":"Mis-specification of cortical identity in a fission yeast PAK mutant.","citation":"Curr Biol 1999 Nov 18;9(22):1335-8","abstract":"The regulation of cell polarity in the fission yeast Schizosaccharomyces pombe is apparent in the restriction of extensile growth to the two ends of a cylindrically shaped cell, and in a specific transition - termed 'new-end take-off' (NETO) - between monopolar and bipolar growth mid-way through the cell cycle [1]. Several genes have been identified that affect one or more aspects of cell polarity (reviewed in [2] [3]), and the molecular pathways regulating cell polarity in fission yeast appear to be conserved among eukaryotes [3] [4] [5] [6] [7] [8] [9], but it is less clear how the proteins involved organize polarity at the level of the entire cell. Here, we describe novel cytological markers of cell polarity in fission yeast and their unusual localization in the monopolar growth mutant orb2-34, which carries a non-lethal mutation in the essential gene shk1(+)/pak1(+)/orb2(+), which encodes a p21-activated kinase (PAK) family member [8] [9] [10] [11] [12]. Our results suggest that, in contrast to other monopolar-growing mutants, the monopolar phenotype of the orb2-34 mutant might not be due to a defect in activating end growth per se, but rather reflects a failure of one of the cell ends to maintain the molecular properties that identify an end. Thus, one role of the Shk1/Pak1 kinase in vivo might be to contribute to how a cell recognizes its ends as sites for growth.","authors":"Sawin KE, Hajibagheri MA, Nurse P","authors_abbrev":"Sawin KE et al.","pubmed_publication_date":"18 Nov 1999","pubmed_entrez_date":"1999-11-27","publication_year":"1999","canto_session_key":"88d2e1acdc9993bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-03-26 10:30:45","canto_approved_date":"2024-03-28 17:58:50","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-04-13 08:44:51","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":8,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC297.03","SPAC22H10.07","SPBC336.12c","SPAC11E3.08c","SPBC1604.14c","SPAC2C4.05"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-03-26"},{"uniquename":"PMID:25452419","title":"Parallel profiling of fission yeast deletion mutants for proliferation and for lifespan during long-term quiescence.","citation":"G3 (Bethesda) 2014 Dec 01;5(1):145-55","abstract":"Genetic factors underlying aging are remarkably conserved from yeast to human. The fission yeast Schizosaccharomyces pombe is an emerging genetic model to analyze cellular aging. Chronological lifespan (CLS) has been studied in stationary-phase yeast cells depleted for glucose, which only survive for a few days. Here, we analyzed CLS in quiescent S. pombe cells deprived of nitrogen, which arrest in a differentiated, G0-like state and survive for more than 2 months. We applied parallel mutant phenotyping by barcode sequencing (Bar-seq) to assay pooled haploid deletion mutants as they aged together during long-term quiescence. As expected, mutants with defects in autophagy or quiescence were under-represented or not detected. Lifespan scores could be calculated for 1199 mutants. We focus the discussion on the 48 most long-lived mutants, including both known aging genes in other model systems and genes not previously implicated in aging. Genes encoding membrane proteins were particularly prominent as pro-aging factors. We independently verified the extended CLS in individual assays for 30 selected mutants, showing the efficacy of the screen. We also applied Bar-seq to profile all pooled deletion mutants for proliferation under a standard growth condition. Unlike for stationary-phase cells, no inverse correlation between growth and CLS of quiescent cells was evident. These screens provide a rich resource for further studies, and they suggest that the quiescence model can provide unique, complementary insights into cellular aging.","doi":"10.1534/g3.114.014415","authors":"Sideri T, Rallis C, Bitton DA, Lages BM, Suo F, Rodríguez-López M, Du LL, Bähler J","authors_abbrev":"Sideri T et al.","pubmed_publication_date":"01 Dec 2014","pubmed_entrez_date":"2014-12-03","publication_year":"2014","canto_session_key":"4d77205831109bda","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-24 09:38:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-02-24 09:38:05","canto_added_date":"2014-12-04 01:15:35","annotation_curators":[],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":553,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_25452419_phaf.tsv"}],"genes":["SPCC4G3.19","SPAC1805.11c","SPAC1071.09c","SPBC428.08c","SPBC17G9.10","SPAC26H5.07c","SPCC970.05","SPAC23H3.14","SPAC2C4.16c","SPBC13E7.07","SPAC1B3.03c","SPCC622.17","SPCC4G3.04c","SPCC162.04c","SPBC36.11","SPAC2E1P3.04","SPCC1795.06","SPAC1834.10c","SPAC5H10.06c","SPAC18B11.03c","SPBC12C2.09c","SPBC15C4.04c","SPCC794.10","SPAC31G5.07","SPBC23G7.04c","SPAC1B3.11c","SPAC25B8.11","SPAC926.03","SPAC15F9.01c","SPCC1450.16c","SPBC646.13","SPBC8D2.10c","SPCC297.04c","SPCC569.02c","SPCC736.09c","SPAP7G5.05","SPBC16E9.15","SPAC4G9.02","SPCC550.07","SPAC1687.08","SPBC16E9.12c","SPAC5D6.02c","SPBC354.03","SPAC1783.05","SPAC1F8.08","SPCC188.08c","SPBC1683.12","SPCC16C4.17","SPAP32A8.03c","SPBC2G5.04c","SPAC30C2.05","SPAC31F12.01","SPAC3H8.07c","SPCC1235.12c","SPCC645.12c","SPBC25B2.08","SPCC1450.05c","SPBC21H7.04","SPAC13A11.05","SPBPB2B2.13","SPAC22F3.02","SPBC24C6.04","SPAC17A5.18c","SPAC17H9.14c","SPBC646.08c","SPBC11C11.11c","SPAC1B3.02c","SPAC15E1.05c","SPCC31H12.05c","SPCC663.06c","SPAC1851.02","SPAC17D4.04","SPAC22G7.11c","SPBC19G7.17","SPBC1734.07c","SPAC17G6.06","SPAC23C4.03","SPAC56F8.05c","SPAC17C9.16c","SPBC27B12.10c","SPAC26H5.04","SPBC3B9.13c","SPAC1F12.04c","SPAC9G1.02","SPAC1A6.06c","SPAC823.15","SPBC1347.13c","SPCC584.16c","SPAC1783.02c","SPBC3E7.02c","SPCC965.11c","SPBC1683.13c","SPAC1952.06c","SPCC1620.12c","SPAC29A4.06c","SPAC25B8.09","SPAC8E11.05c","SPCC191.05c","SPAC30D11.14c","SPAPYUG7.03c","SPBC947.09","SPAC20H4.08","SPAC31A2.16","SPAC1B1.04c","SPCC285.16c","SPAC212.01c","SPBC31F10.10c","SPCC965.08c","SPAPYUG7.06","SPAC23A1.06c","SPAC19D5.01","SPBC1198.11c","SPBC106.11c","SPCC1840.09","SPAC31G5.17c","SPAC23C11.13c","SPAC3A11.04","SPCC1020.08","SPBC8E4.01c","SPAC222.13c","SPAC1687.15","SPBC1773.02c","SPAC3H8.09c","SPAC9G1.12","SPAC6G10.12c","SPAC26H5.10c","SPAC343.12","SPAC1565.01","SPBC25B2.06c","SPAC27F1.10","SPAC9.11","SPBC26H8.01","SPCC31H12.03c","SPAC688.10","SPAC23D3.03c","SPBC19C2.06c","SPAC1039.03","SPAC27D7.13c","SPCC622.16c","SPBC12C2.05c","SPAC17A5.16","SPAC6G10.03c","SPAC56F8.02","SPAC869.10c","SPAC6F6.04c","SPAC1952.12c","SPBC1709.14","SPAC824.05","SPAC31A2.14","SPCC622.12c","SPCC70.08c","SPAC23H3.04","SPAC3A12.13c","SPCC1795.10c","SPBC20F10.10","SPAC29A4.09","SPBC839.02","SPNCRNA.9001","SPBP16F5.08c","SPCC1450.03","SPAC3C7.07c","SPAC227.01c","SPAC13F5.04c","SPCC1020.10","SPBC1105.09","SPBC2D10.16","SPAC607.10","SPAC25G10.06","SPAC694.06c","SPBC365.16","SPAC25B8.01","SPBC1709.13c","SPAC2E1P5.03","SPCC1393.08","SPAC11D3.09","SPBC12C2.07c","SPAC664.13","SPACUNK4.16c","SPCC1393.07c","SPAC4G9.11c","SPBC3B9.05","SPBC29A10.05","SPCC31H12.04c","SPCC1739.07","SPAC1F12.02c","SPAC22H12.05c","SPCC576.12c","SPAC16.01","SPCC417.06c","SPBP8B7.04","SPAC17G6.15c","SPCC1020.12c","SPBC19C7.01","SPAC19A8.10","SPBC16D10.07c","SPBC2D10.17","SPAC9G1.07","SPAC25H1.03","SPAC3C7.13c","SPBC839.13c","SPCC737.06c","SPCC23B6.02c","SPAC24C9.15c","SPBC685.04c","SPBC28F2.05c","SPCC16C4.10","SPBC21B10.07","SPCC364.03","SPBC21C3.18","SPAC328.10c","SPBC1773.16c","SPAC1002.14","SPCC584.03c","SPCC63.13","SPBC947.08c","SPBC13G1.02","SPBC15D4.05","SPBC1734.12c","SPAC57A10.06","SPBC691.03c","SPAC3G9.01","SPAC23C11.14","SPBC3B8.05","SPBC21C3.08c","SPAC23G3.07c","SPCP1E11.10","SPCC1223.11","SPBC32F12.03c","SPCC417.05c","SPAC890.03","SPBC543.07","SPBC1734.15","SPAC1F5.07c","SPBC1921.04c","SPAC16A10.04","SPBC23G7.13c","SPAC227.17c","SPAC2C4.15c","SPBC215.06c","SPAC6G9.13c","SPAC1834.04","SPBP8B7.18c","SPAC212.02","SPAC24B11.12c","SPCC613.06","SPAC26A3.07c","SPCC663.11","SPCC306.11","SPCC4B3.12","SPAC25B8.15c","SPAPB1A10.05","SPCC1494.08c","SPBC26H8.03","SPAC1B3.17","SPAC13D6.02c","SPBC365.14c","SPAC1071.11","SPAC1486.02c","SPBC13E7.08c","SPAC6B12.08","SPBC16H5.08c","SPAC16E8.06c","SPAC144.04c","SPAC17A5.09c","SPAC17C9.05c","SPAC23C11.02c","SPBC2G2.06c","SPCC1450.12","SPAC30D11.09","SPCC4G3.09c","SPBC25H2.15","SPCC16A11.15c","SPAC23H4.09","SPBC11C11.06c","SPAC5D6.08c","SPAC3H1.06c","SPBC359.01","SPBC577.06c","SPAC29A4.10","SPAC11E3.13c","SPBC106.10","SPAC1952.02","SPBC713.11c","SPAC14C4.05c","SPBC947.15c","SPBC1198.07c","SPAC17G8.11c","SPCC1322.07c","SPAC1F3.09","SPBC12D12.07c","SPAPB21F2.03","SPAC1F8.06","SPCC74.04","SPBC16H5.11c","SPCC24B10.02c","SPAC23H4.10c","SPBC1539.10","SPBC17G9.05","SPBC14C8.04","SPAC15A10.08","SPAC1B1.02c","SPAC3A12.17c","SPAC22A12.17c","SPAPB8E5.05","SPCC4B3.15","SPAC11E3.14","SPBC12C2.04","SPBC713.03","SPCC126.10","SPAC977.14c","SPAC15E1.09","SPAC11G7.01","SPBC15D4.09c","SPAC6B12.12","SPAC212.08c","SPCC594.01","SPBC15C4.05","SPCC61.03","SPBC800.02","SPBC25B2.02c","SPBP8B7.23","SPAC323.05c","SPAC19G12.03","SPBC947.03c","SPBC30D10.09c","SPAC2G11.04","SPBC26H8.05c","SPAC17G8.08c","SPBC23E6.02","SPBC31F10.07","SPCPB16A4.02c","SPBC1685.01","SPAC6F6.13c","SPCC737.04","SPAC17H9.12c","SPAC26H5.03","SPAC1635.01","SPBC1105.14","SPBC4B4.06","SPBC19F8.04c","SPAC4F10.18","SPBC3B8.07c","SPAC24B11.05","SPBC106.01","SPAC19D5.03","SPBC16E9.16c","SPAC15A10.16","SPAC1565.07c","SPCC825.05c","SPAC29B12.12","SPBC359.05","SPAC3A11.09","SPAC823.03","SPCC188.07","SPAC2F3.08","SPBC365.20c","SPBC21B10.13c","SPAPB1A10.15","SPBC577.13","SPCC364.07","SPAC14C4.01c","SPBC19C2.14","SPCC338.11c","SPAC2F7.08c","SPAC10F6.16","SPBC27B12.14","SPAC20H4.09","SPAC3H1.11","SPAPB1A10.03","SPAC688.11","SPAC1142.03c","SPBC23G7.11","SPBC336.13c","SPAP7G5.03","SPCC576.17c","SPAC23G3.08c","SPCC613.03","SPBP4H10.13","SPAC105.02c","SPBC4F6.09","SPBC354.02c","SPAC23H3.06","SPBC18H10.18c","SPCC364.02c","SPBC336.01","SPCC794.03","SPAC3F10.04","SPAC13G6.02c","SPAC23D3.10c","SPAC18G6.02c","SPAC31G5.14","SPBC56F2.05c","SPBC1921.01c","SPAPB24D3.08c","SPBC29A3.08","SPBC19C2.04c","SPCC622.15c","SPBC27B12.08","SPAC144.17c","SPAC1805.07c","SPCC1393.02c","SPCC1827.04","SPAC13G6.01c","SPBC4B4.12c","SPAC2F3.07c","SPCC663.08c","SPAC11D3.16c","SPAC23C11.06c","SPAC23G3.05c","SPBC106.03","SPCC1450.11c","SPAC17G8.09","SPBC354.08c","SPCC13B11.03c","SPAC977.16c","SPAC31G5.11","SPBC25B2.10","SPCC24B10.13","SPBC1718.03","SPAC3C7.08c","SPAC20H4.02","SPBC1D7.03","SPAC637.13c","SPAC24C9.12c","SPAC16C9.07","SPBC12C2.12c","SPCPB1C11.03","SPAC607.06c","SPCC320.03","SPBC3D6.04c","SPCC663.09c","SPCC1442.04c","SPCC4B3.01","SPBC17D1.06","SPAC15A10.10","SPBC21B10.12","SPBC4B4.10c","SPBP8B7.28c","SPAC20G4.08","SPAC630.04c","SPAC1A6.04c","SPBC17G9.09","SPBC1711.04","SPAC1039.07c","SPBC1271.07c","SPCC24B10.09","SPAPB1A11.03","SPAC2F3.05c","SPBC337.04","SPCC1919.07","SPAC26A3.04","SPAC17A2.01","SPAC18B11.04","SPBC685.06","SPAP8A3.12c","SPCC1753.02c","SPAC3F10.02c","SPCC962.04","SPAC1071.07c","SPCC1393.05","SPAC16E8.17c","SPAC12G12.03","SPBC119.03","SPBC119.14","SPBP4G3.03","SPAC227.10","SPCC550.01c","SPBC1703.14c","SPBC839.03c","SPAC8F11.03","SPCC1739.08c","SPBC4F6.16c","SPAC9.02c","SPBC106.08c","SPBC18E5.14c","SPBC14C8.15","SPAC20H4.03c","SPBC23G7.14","SPBC36B7.05c","SPCC364.04c","SPBC1734.05c","SPAC26H5.09c","SPBC36.06c","SPAC521.05","SPAP7G5.04c","SPCC330.02","SPAC227.15","SPBC354.15","SPBC1861.02","SPBC1539.03c","SPBP8B7.25","SPCC1223.05c","SPAC589.07c","SPAC144.14","SPBC215.05","SPAPB24D3.04c","SPAC26A3.17c","SPAC1751.04","SPBC16G5.15c","SPCC576.01c","SPAC22F3.08c","SPBC20F10.07","SPBC11C11.09c","SPBC3B9.04","SPAC12G12.09","SPAC1952.10c","SPCC594.02c","SPCC1682.12c","SPBC947.05c","SPAC3F10.05c","SPBC336.05c"],"gene_count":511,"ltp_gene_count":0,"approved_date":"2016-02-24"},{"uniquename":"PMID:4156830","title":"Changes in respiratory activities during the cell-cycle of the fission yeast Schizosaccharomyces pompe 972h--growing in the presence of glycerol.","citation":"Biochem J 1974 Oct;144(1):141-8","abstract":"1. The specific activities of cytochrome c oxidase, catalase, succinate dehydrogenase, succinate-cytochrome c oxidoreductase, NADH-cytochrome c oxidoreductase, and NADPH-cytochrome c oxidoreductase in mid-exponential-phase batch cultures of glycerol-grown Schizosaccharomyces pombe indicated that the organisms were catabolite-de-repressed. 2. In cultures growing synchronously in the presence of glycerol as sole carbon source, the respiration rate showed two abrupt increases at about 0.45 and 0.95 of the cell-cycle and remained constant in the periods between successive rises. 3. Catalase, succinate dehydrogenase, NADH-cytochrome c oxidoreductase and acid p-nitrophenyl-phosphatase all showed peak patterns of expression in synchronous cultures. 4. Cytochrome c oxidase and cytochromes a+a(3) both showed step patterns of expression with two rises per cell-cycle. 5. Cytochromes c(548), b(554) and b(560) all followed similar time-courses in step patterns of expression, but these were distinct from, and more complex than, that of cytochromes a+a(3). 6. These results are compared with those previously obtained with glucose-grown cultures, and the part played by catabolite repression in the expression of respiratory activities in the cell-cycle is assessed.","authors":"Poole RK, Lloyd D","authors_abbrev":"Poole RK et al.","pubmed_publication_date":"Oct 1974","pubmed_entrez_date":"1974-10-01","publication_year":"1974","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9420333","title":"Asymmetric segregation on spindle poles of the Schizosaccharomyces pombe septum-inducing protein kinase Cdc7p.","citation":"Genes Dev 1998 Jan 01;12(1):84-94","abstract":"Schizosaccharomyces pombe divides by means of a centrally placed division septum. The initiation of septation must be tightly coordinated with events in mitosis, as premature formation of the septum can lethally cut the undivided nucleus. The Spg1p GTPase and the Cdc7p kinase, with which it interacts, play a central role in signaling the initiation of septum formation. Loss-of-function mutations in either gene prevent septation, whereas inappropriate activation of Spg1p can induce septum formation from G1 or G2 interphase cells. Increased expression of either gene leads to multiple rounds of septation without cell cleavage, emphasizing the need for precise cell cycle regulation of their activity. To understand the mechanisms underlying this regulation, we have investigated whether these key initiators of septum formation are controlled by changes in their activity and/or location during mitosis and cytokinesis. We demonstrate that Spg1p localizes to the spindle pole body in interphase and to both spindle poles during mitosis. In contrast, Cdc7p shows no discrete localization during interphase, but early in mitosis it associates with both spindle pole bodies and, as the spindle extends, is seen on only one pole of the spindle during anaphase B. Spg1p activity is required for localization of Cdc7p in vivo but not for its kinase activity in vitro. Staining with an antiserum that recognizes preferentially GDP-Spg1p indicates that activated GTP-Spg1p predominates during mitosis when Cdc7p is associated with the spindle pole body. Furthermore, staining with this antibody shows that asymmetric distribution of Cdc7p may be mediated by inactivation of Spg1p on one spindle pole. Deregulated septation in mutant cells correlates with segregation of Cdc7p to both spindle poles.","authors":"Sohrmann M, Schmidt S, Hagan I, Simanis V","authors_abbrev":"Sohrmann M et al.","pubmed_publication_date":"01 Jan 1998","pubmed_entrez_date":"1998-02-21","publication_year":"1998","canto_session_key":"709eb266115f50d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-05-09 17:39:29","canto_approved_date":"2025-09-04 11:30:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-05 08:52:40","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":10,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPAC1565.06c","SPBC12D12.01","SPAC6F6.08c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2021-05-09"},{"uniquename":"PMID:17377067","title":"Regulation of cell diameter, For3p localization, and cell symmetry by fission yeast Rho-GAP Rga4p.","citation":"Mol Biol Cell 2007 Jun;18(6):2090-101","abstract":"Control of cellular dimensions and cell symmetry are critical for development and differentiation. Here we provide evidence that the putative Rho-GAP Rga4p of Schizosaccharomyces pombe controls cellular dimensions. rga4 Delta cells are wider in diameter and shorter in length, whereas Rga4p overexpression leads to reduced diameter of the growing cell tip. Consistent with a negative role in cell growth control, Rga4p protein localizes to the cell sides in a \"corset\" pattern, and to the nongrowing cell tips. Additionally, rga4 Delta cells show an altered growth pattern similar to that observed in mutants of the formin homology protein For3p. Consistent with these observations, Rga4p is required for normal localization of For3p and for normal distribution of the actin cytoskeleton. We show that different domains of the Rga4p protein mediate diverse morphological functions. The C-terminal GAP domain mediates For3p localization to the cell tips and maintains cell diameter. Conversely, overexpression of the N-terminal LIM homology domain of Rga4p promotes actin cable formation in a For3p-dependent manner. Our studies indicate that Rga4p functionally interacts with For3p and has a novel function in the control of cell diameter and cell growth.","authors":"Das M, Wiley DJ, Medina S, Vincent HA, Larrea M, Oriolo A, Verde F","authors_abbrev":"Das M et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-03-23","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.12","SPBC28E12.03","SPCC895.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:19592249","title":"A novel protein phosphatase 1-dependent spindle checkpoint silencing mechanism.","citation":"Curr Biol 2009 Jul 28;19(14):1176-81","abstract":"The spindle checkpoint is a surveillance system acting in mitosis to delay anaphase onset until all chromosomes are properly attached to the mitotic spindle. When the checkpoint is activated, the Mad2 and Mad3 proteins directly bind and inhibit Cdc20, which is an essential activator of an E3 ubiquitin ligase known as the anaphase-promoting complex (APC). When the checkpoint is satisfied, Cdc20-APC is activated and polyubiquitinates securin and cyclin, leading to the dissolution of sister chromatid cohesion and mitotic progression. Several protein kinases play critical roles in spindle checkpoint signaling, but the mechanism (or mechanisms) by which they inhibit mitotic progression remains unclear. Furthermore, it is not known whether their activity needs to be reversed by protein phosphatases before anaphase onset can occur. Here we employ fission yeast to show that Aurora (Ark1) kinase activity is directly required to maintain spindle checkpoint arrest, even in the presence of many unattached kinetochores. Upon Ark1 inhibition, checkpoint complexes are disassembled and cyclin B is rapidly degraded. Importantly, checkpoint silencing and cyclin B degradation require the kinetochore-localized isoform of protein phosphatase 1 (PP1(Dis2)). We propose that PP1(Dis2)-mediated dephosphorylation of checkpoint components forms a novel spindle checkpoint silencing mechanism.","doi":"10.1016/j.cub.2009.05.060","authors":"Vanoosthuyse V, Hardwick KG","authors_abbrev":"Vanoosthuyse V et al.","pubmed_publication_date":"28 Jul 2009","pubmed_entrez_date":"2009-07-14","publication_year":"2009","canto_session_key":"50ae65179f9a18da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-11-22 17:29:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-17 16:53:01","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.01c","SPBC582.03","SPBC20F10.06","SPCC320.13c","SPBC776.02c","SPAC19G12.01c","SPBC26H8.07c","SPCC31H12.05c"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2016-10-17"},{"uniquename":"PMID:18198019","title":"Behaviors of the \"raman spectroscopic signature of life\" in single living fission yeast cells under different nutrient, stress, and atmospheric conditions.","citation":"Appl Spectrosc 2007 Dec;61(12):1290-4","abstract":"Time- and space-resolved Raman spectra of mitochondria in single living fission yeast cells have been measured under various nutrient, stress, and atmospheric conditions. A focus is placed on the behavior of the Raman band located at 1602 cm(-1), which sensitively reflects the metabolic activity in mitochondria and which has been called by us the \"Raman spectroscopic signature of life\". Addition of nutrients increases the intensity of this band by approximately 1.5 times, confirming its correlation with the metabolic activity in mitochondria. The spectra of cells cultured under 100% N(2), 100% O(2), and N(2)/O(2) (V(N2):V(O2) congruent with approximately = 4:1) atmospheres have been measured for both (16)O(2) and (18)O(2). Yeast cells have been found to lose their metabolic activity after the culture under 100% N(2) and 100% O(2) atmospheres. Cells cultured under a N(2)/(16)O(2) ((16)O(2) = 20%) atmosphere show strong \"Raman spectroscopic signature of life\". No (18)O isotopic shift has been found for the wavenumber 1602 cm(-1), indicating that the origin of this signature is neither O(2) nor an O-containing small molecule. Addition of H(2)O(2) causes a quick decrease of the \"Raman spectroscopic signature of life\", followed by the cis-trans isomerization in the unsaturated phospholipid chain. The \"Raman spectroscopic signature of life\" has thus been proved to be a reliable real-time and in vivo indicator for monitoring the metabolic activity in living cells.","doi":"10.1366/000370207783292082","authors":"Huang YS, Nakatsuka T, Hamaguchi HO","authors_abbrev":"Huang YS et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2008-01-17","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35857444","title":"HP1 oligomerization compensates for low-affinity H3K9me recognition and provides a tunable mechanism for heterochromatin-specific localization.","citation":"Sci Adv 2022 Jul 08;8(27):eabk0793","abstract":"HP1 proteins traverse a complex and crowded chromatin landscape to bind with low affinity but high specificity to histone H3K9 methylation (H3K9me) and form transcriptionally inactive genomic compartments called heterochromatin. Here, we visualize single-molecule dynamics of an HP1 homolog, the fission yeast Swi6, in its native chromatin environment. By tracking single Swi6 molecules, we identify mobility states that map to discrete biochemical intermediates. Using Swi6 mutants that perturb H3K9me recognition, oligomerization, or nucleic acid binding, we determine how each biochemical property affects protein dynamics. We estimate that Swi6 recognizes H3K9me3 with ~94-fold specificity relative to unmodified nucleosomes in living cells. While nucleic acid binding competes with Swi6 oligomerization, as few as four tandem chromodomains can overcome these inhibitory effects to facilitate Swi6 localization at heterochromatin formation sites. Our studies indicate that HP1 oligomerization is essential to form dynamic, higher-order complexes that outcompete nucleic acid binding to enable specific H3K9me recognition.","doi":"10.1126/sciadv.abk0793","authors":"Biswas S, Chen Z, Karslake JD, Farhat A, Ames A, Raiymbek G, Freddolino PL, Biteen JS, Ragunathan K","authors_abbrev":"Biswas S et al.","pubmed_publication_date":"08 Jul 2022","pubmed_entrez_date":"2022-07-20","publication_year":"2022","canto_session_key":"179878b283512d8e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-07-23 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22033972","title":"Fission yeast Swi5-Sfr1 protein complex, an activator of Rad51 recombinase, forms an extremely elongated dogleg-shaped structure.","citation":"J Biol Chem 2011 Dec 16;286(50):43569-76","abstract":"In eukaryotes, DNA strand exchange is the central reaction of homologous recombination, which is promoted by Rad51 recombinases forming a right-handed nucleoprotein filament on single-stranded DNA, also known as a presynaptic filament. Accessory proteins known as recombination mediators are required for the formation of the active presynaptic filament. One such mediator in the fission yeast Schizosaccharomyces pombe is the Swi5-Sfr1 complex, which has been identified as an activator of Rad51 that assists in presynaptic filament formation and stimulates its strand exchange reaction. Here, we determined the 1:1 binding stoichiometry between the two subunits of the Swi5-Sfr1 complex using analytical ultracentrifugation and electrospray ionization mass spectrometry. Small-angle x-ray scattering experiments revealed that the Swi5-Sfr1 complex displays an extremely elongated dogleg-shaped structure in solution, which is consistent with its exceptionally high frictional ratio (f/f(0)) of 2.0 ± 0.2 obtained by analytical ultracentrifugation. Furthermore, we determined a rough topology of the complex by comparing the small-angle x-ray scattering-based structures of the Swi5-Sfr1 complex and four Swi5-Sfr1-Fab complexes, in which the Fab fragments of monoclonal antibodies were specifically bound to experimentally determined sites of Sfr1. We propose a model for how the Swi5-Sfr1 complex binds to the Rad51 filament, in which the Swi5-Sfr1 complex fits into the groove of the Rad51 filament, leading to an active and stable presynaptic filament.","doi":"10.1074/jbc.M111.303339","authors":"Kokabu Y, Murayama Y, Kuwabara N, Oroguchi T, Hashimoto H, Tsutsui Y, Nozaki N, Akashi S, Unzai S, Shimizu T, Iwasaki H, Sato M, Ikeguchi M","authors_abbrev":"Kokabu Y et al.","pubmed_publication_date":"16 Dec 2011","pubmed_entrez_date":"2011-10-29","publication_year":"2011","canto_session_key":"f23547b9f5114991","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-10-01 07:16:19","canto_approved_date":"2021-10-01 07:16:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-10-01 07:16:12","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.07","SPBC409.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-10-01"},{"uniquename":"PMID:23145069","title":"Identification and functional analysis of the erh1(+) gene encoding enhancer of rudimentary homolog from the fission yeast Schizosaccharomyces pombe.","citation":"PLoS One 2012;7(11):e49059","abstract":"The ERH gene encodes a highly conserved small nuclear protein with a unique amino acid sequence and three-dimensional structure but unknown function. The gene is present in animals, plants, and protists but to date has only been found in few fungi. Here we report that ERH homologs are also present in all four species from the genus Schizosaccharomyces, S. pombe, S. octosporus, S. cryophilus, and S. japonicus, which, however, are an exception in this respect among Ascomycota and Basidiomycota. The ERH protein sequence is moderately conserved within the genus (58% identity between S. pombe and S.japonicus), but the intron-rich genes have almost identical intron-exon organizations in all four species. In S. pombe, erh1(+) is expressed at a roughly constant level during vegetative growth and adaptation to unfavorable conditions such as nutrient limitation and hyperosmotic stress caused by sorbitol. Erh1p localizes preferentially to the nucleus with the exception of the nucleolus, but is also present in the cytoplasm. Cells lacking erh1(+) have an aberrant cell morphology and a comma-like shape when cultured to the stationary phase, and exhibit a delayed recovery from this phase followed by slower growth. Loss of erh1(+) in an auxotrophic background results in enhanced arrest in the G1 phase following nutritional stress, and also leads to hypersensitivity to agents inducing hyperosmotic stress (sorbitol), inhibiting DNA replication (hydroxyurea), and destabilizing the plasma membrane (SDS); this hypersensitivity can be abolished by expression of S. pombe erh1(+) and, to a lesser extent, S. japonicus erh1(+) or human ERH. Erh1p fails to interact with the human Ciz1 and PDIP46/SKAR proteins, known molecular partners of human ERH. Our data suggest that in Schizosaccharomyces sp. erh1(+) is non-essential for normal growth and Erh1p could play a role in response to adverse environmental conditions and in cell cycle regulation.","doi":"10.1371/journal.pone.0049059","authors":"Krzyzanowski MK, Kozlowska E, Kozlowski P","authors_abbrev":"Krzyzanowski MK et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-11-13","publication_year":"2012","canto_session_key":"0bd070642c31ebd4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-21 10:18:09","canto_approved_date":"2024-07-15 11:43:35","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-06-12 11:03:09","canto_added_date":"2012-11-14 14:56:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.02c","SPAC19G12.17","SPCC1322.13","SPCC330.05c","SPAC144.03"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2015-09-21"},{"uniquename":"PMID:10049914","title":"Localization and properties of a silencing element near the mat3-M mating-type cassette of Schizosaccharomyces pombe.","citation":"Genetics 1999 Mar;151(3):945-63","abstract":"Transcription is repressed in a segment of Schizosaccharomyces pombe chromosome II that encompasses the mat2-P and mat3-M mating-type cassettes. Chromosomal deletion analysis revealed the presence of a repressor element within 500 bp of mat3-M. This element acted in synergy with the trans-acting factors Swi6, Clr1, Clr2, Clr3, and Clr4 and had several properties characteristic of silencers: it did not display promoter specificity, being able to silence not only the M mating-type genes but also the S. pombe ura4 and ade6 genes placed on the centromere-distal side of the mat3-M cassette; it could repress a gene when placed further than 2.6 kb from the promoter and it acted in both orientations, although with different efficiencies, the natural orientation repressing more stringently than the reverse. Following deletion of this element, two semistable states of expression of the mat3-M region were observed and these two states could interconvert. The deletion did not affect gene expression in the vicinity of the mat2-P cassette, 11 kb away from mat3-M. Conversely, deleting 1.5 kb on the centromere-proximal side of the mat2-P cassette, which was previously shown to partially derepress transcription around mat2-P, had no effect on gene expression near mat3-M. A double deletion removing the mat2-P and mat3-M repressor elements had the same effect as the single deletions on their respective cassettes when assayed in cells of the M mating type. These observations allow us to refine a model proposing that redundant pathways silence the mating type region of S. pombe.","authors":"Thon G, Bjerling KP, Nielsen IS","authors_abbrev":"Thon G et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-03-02","publication_year":"1999","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007223","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14742702","title":"Interdependency of fission yeast Alp14/TOG and coiled coil protein Alp7 in microtubule localization and bipolar spindle formation.","citation":"Mol Biol Cell 2004 Apr;15(4):1609-22","abstract":"The Dis1/TOG family plays a pivotal role in microtubule organization. In fission yeast, Alp14 and Dis1 share an essential function in bipolar spindle formation. Here, we characterize Alp7, a novel coiled-coil protein that is required for organization of bipolar spindles. Both Alp7 and Alp14 colocalize to the spindle pole body (SPB) and mitotic spindles. Alp14 localization to these sites is fully dependent upon Alp7. Conversely, in the absence of Alp14, Alp7 localizes to the SPBs, but not mitotic spindles. Alp7 forms a complex with Alp14, where the C-terminal region of Alp14 interacts with the coiled-coil domain of Alp7. Intriguingly, this Alp14 C terminus is necessary and sufficient for mitotic spindle localization. Overproduction of either full-length or coiled-coil region of Alp7 results in abnormal V-shaped spindles and stabilization of interphase microtubules, which is induced independent of Alp14. Alp7 may be a functional homologue of animal TACC. Our results shed light on an interdependent relationship between Alp14/TOG and Alp7. We propose a two-step model that accounts for the recruitment of Alp7 and Alp14 to the SPB and microtubules.","authors":"Sato M, Vardy L, Angel Garcia M, Koonrugsa N, Toda T","authors_abbrev":"Sato M et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-01-27","publication_year":"2004","canto_session_key":"a39841010d3ec10f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-02-01 17:28:48","canto_approved_date":"2022-07-22 14:25:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-16 09:16:36","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":39,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPAC890.02c","SPBC2F12.13","SPCC895.07","SPCC736.14"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-02-01"},{"uniquename":"PMID:11598266","title":"Requirement of heterochromatin for cohesion at centromeres.","citation":"Science 2001 Dec 21;294(5551):2539-42","abstract":"Centromeres are heterochromatic in many organisms, but the mitotic function of this silent chromatin remains unknown. During cell division, newly replicated sister chromatids must cohere until anaphase when Scc1/Rad21-mediated cohesion is destroyed. In metazoans, chromosome arm cohesins dissociate during prophase, leaving centromeres as the only linkage before anaphase. It is not known what distinguishes centromere cohesion from arm cohesion. Fission yeast Swi6 (a Heterochromatin protein 1 counterpart) is a component of silent heterochromatin. Here we show that this heterochromatin is specifically required for cohesion between sister centromeres. Swi6 is required for association of Rad21-cohesin with centromeres but not along chromosome arms and, thus, acts to distinguish centromere from arm cohesion. Therefore, one function of centromeric heterochromatin is to attract cohesin, thereby ensuring sister centromere cohesion and proper chromosome segregation.","authors":"Bernard P, Maure JF, Partridge JF, Genier S, Javerzat JP, Allshire RC","authors_abbrev":"Bernard P et al.","pubmed_publication_date":"21 Dec 2001","pubmed_entrez_date":"2001-10-13","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.01c","SPCC338.17c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:33977597","title":"Extension of chronological lifespan in Schizosaccharomyces pombe.","citation":"Genes Cells 2021 Jul;26(7):459-473","abstract":"There are several examples in the nature wherein the mechanism of longevity control of unicellular organisms is evolutionarily conserved with that of higher multicellular organisms. The present microreview focuses on aging and longevity studies, particularly on chronological lifespan (CLS) concerning the unicellular eukaryotic fission yeast Schizosaccharomyces pombe. In S. pombe, >30 compounds, 8 types of nutrient restriction, and >80 genes that extend CLS have been reported. Several CLS control mechanisms are known to be involved in nutritional response, energy utilization, stress responses, translation, autophagy, and sexual differentiation. In unicellular organisms, the control of CLS is directly linked to the mechanism by which cells are maintained in limited-resource environments, and their genetic information is left to posterity. We believe that this important mechanism may have been preserved as a lifespan control mechanism for higher organisms.","doi":"10.1111/gtc.12854","authors":"Ohtsuka H, Shimasaki T, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Jul 2021","pubmed_entrez_date":"2021-05-12","publication_year":"2021","canto_session_key":"7a8b139455854980","canto_annotation_status":"APPROVED","canto_triage_status":"Review or comment","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2021-08-04 16:50:06","canto_approved_date":"2021-08-04 16:50:06","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-08-03 03:41:54","canto_added_date":"2021-05-14 00:15:03","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":1,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11D3.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-08-04"},{"uniquename":"PMID:9774107","title":"Replication checkpoint requires phosphorylation of the phosphatase Cdc25 by Cds1 or Chk1.","citation":"Nature 1998 Oct 01;395(6701):507-10","abstract":"Checkpoints maintain the order and fidelity of events of the cell cycle by blocking mitosis in response to unreplicated or damaged DNA. In most species this is accomplished by preventing activation of the cell-division kinase Cdc2, which regulates entry into mitosis. The Chk1 kinase, an effector of the DNA-damage checkpoint, phosphorylates Cdc25, an activator of Cdc2. Phosphorylation of Cdc25 promotes its binding to 14-3-3 proteins, preventing it from activating Cdc2. Here we propose that a similar pathway is required for mitotic arrest in the presence of unreplicated DNA (that is, in the replication checkpoint) in fission yeast. We show by mutagenesis that Chk1 functions redundantly with the kinase Cds1 at the replication checkpoint and that both kinases phosphorylate Cdc25 on the same sites, which include serine residues at positions 99, 192 and 359. Mutation of these residues reduces binding of 14-3-3 proteins to Cdc25 in vitro and disrupts the replication checkpoint in vivo. We conclude that both Cds1 and Chk1 regulate the binding of Cdc25 to 14-3-3 proteins as part of the checkpoint response to unreplicated DNA.","authors":"Zeng Y, Forbes KC, Wu Z, Moreno S, Piwnica-Worms H, Enoch T","authors_abbrev":"Zeng Y et al.","pubmed_publication_date":"01 Oct 1998","pubmed_entrez_date":"1998-10-17","publication_year":"1998","canto_session_key":"a8a2700cbe528751","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-04-17 11:06:20","canto_approved_date":"2021-01-05 16:39:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-09-21 09:45:17","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC1259.13","SPAC8E11.02c","SPAC24H6.05","SPBC660.14","SPAC17A2.13c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-04-17"},{"uniquename":"PMID:9193713","title":"A microtiter-based fluorescence assay for (1,3)-beta-glucan synthases.","citation":"Anal Biochem 1997 Jun 15;249(1):88-93","abstract":"A high-throughput assay for UDP-Glc:(1,3)-beta-glucan synthase(EC 2.4.1.34, UDP-glucose:1,3-beta-D-glucan, 3-beta-glucosyltransferase) from fungi and higher plants is described. The assay is performed in microtiter plates and is extremely inexpensive compared to other standard assays for these enzymes. The reduction in price is achieved by replacing the conventional substrate UDP-[14C]Glc with its nonradioactive counterpart, and the nonradioactive glucan produced is quantified as a fluorescent complex following specific interaction with the fluorochrome present in commercial aniline blue. In addition to a > 100-fold reduction in cost, the assay is highly reproducible and nearly as sensitive as radioactive assays and has the additional advantages of increased safety and avoidance of the need for filtration and washing steps to collect the glucan product. As such, the assay is highly suitable for high-throughput screening for inhibitors of these enzymes.","authors":"Shedletzky E, Unger C, Delmer DP","authors_abbrev":"Shedletzky E et al.","pubmed_publication_date":"15 Jun 1997","pubmed_entrez_date":"1997-06-15","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36548389","title":"PTMint database of experimentally verified PTM regulation on protein-protein interaction.","citation":"Bioinformatics 2023 Jan 01;39(1)","abstract":"Post-translational modification (PTM) is an important biochemical process. which includes six most well-studied types: phosphorylation, acetylation, methylation, sumoylation, ubiquitylation and glycosylation. PTM is involved in various cell signaling pathways and biological processes. Abnormal PTM status is closely associated with severe diseases (such as cancer and neurologic diseases) by regulating protein functions, such as protein-protein interactions (PPIs). A set of databases was constructed separately for PTM sites and PPI; however, the resource of regulation for PTM on PPI is still unsolved.\nHere, we firstly constructed a public accessible database of PTMint (PTMs that are associated with PPIs) (https://ptmint.sjtu.edu.cn/) that contains manually curated complete experimental evidence of the PTM regulation on PPIs in multiple organisms, including Homo sapiens, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Saccharomyces cerevisiae and Schizosaccharomyces pombe. Currently, the first version of PTMint encompassed 2477 non-redundant PTM sites in 1169 proteins affecting 2371 protein-protein pairs involving 357 diseases. Various annotations were systematically integrated, such as protein sequence, structure properties and protein complex analysis. PTMint database can help to insight into disease mechanism, disease diagnosis and drug discovery associated with PTM and PPI.\nPTMint is freely available at: https://ptmint.sjtu.edu.cn/.\nSupplementary data are available at Bioinformatics online.","doi":"10.1093/bioinformatics/btac823","authors":"Hong X, Li N, Lv J, Zhang Y, Li J, Zhang J, Chen HF","authors_abbrev":"Hong X et al.","pubmed_publication_date":"01 Jan 2023","pubmed_entrez_date":"2022-12-22","publication_year":"2023","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2022-12-23 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8021171","title":"Trehalose-6-P synthase is dispensable for growth on glucose but not for spore germination in Schizosaccharomyces pombe.","citation":"J Bacteriol 1994 Jul;176(13):3895-902","abstract":"Trehalose-6-P inhibits hexokinases in Saccharomyces cerevisiae (M. A. Blázquez, R. Lagunas, C. Gancedo, and J. M. Gancedo, FEBS Lett. 329:51-54, 1993), and disruption of the TPS1 gene (formerly named CIF1 or FDP1) encoding trehalose-6-P synthase prevents growth in glucose. We have found that the hexokinase from Schizosaccharomyces pombe is not inhibited by trehalose-6-P even at a concentration of 3 mM. The highest internal concentration of trehalose-6-P that we measured in S. pombe was 0.75 mM after heat shock. We have isolated from S. pombe the tps1+ gene, which is homologous to the Saccharomyces cerevisiae TPS1 gene. The DNA sequence from tps1+ predicts a protein of 479 amino acids with 65% identity with the protein of S. cerevisiae. The tps1+ gene expressed from its own promoter could complement the lack of trehalose-6-P synthase in S. cerevisiae tps1 mutants. The TPS1 gene from S. cerevisiae could also restore trehalose synthesis in S. pombe tps1 mutants. A chromosomal disruption of the tps1+ gene in S. pombe did not have a noticeable effect on growth in glucose, in contrast with the disruption of TPS1 in S. cerevisiae. However, the disruption prevented germination of spores carrying it. The level of an RNA hybridizing with an internal probe of the tps1+ gene reached a maximum after 20 min of heat shock treatment. The results presented support the idea that trehalose-6-P plays a role in the control of glycolysis in S. cerevisiae but not in S. pombe and show that the trehalose pathway has different roles in the two yeast species.","authors":"Blázquez MA, Stucka R, Feldmann H, Gancedo C","authors_abbrev":"Blázquez MA et al.","pubmed_publication_date":"Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_session_key":"e980040aaa685a70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-20 13:23:33","canto_approved_date":"2019-10-26 12:21:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-20 10:13:24","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC328.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-20"},{"uniquename":"PMID:1923816","title":"Dual modes of transcriptional and translational initiation of SSP1, the gene for a mitochondrial HSP70, responding to heat-shock in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1991 Oct 11;19(19):5331-7","abstract":"The SSP1 gene of Schizosaccharomyces pombe which is homologous to the SSC1 gene of Saccharomyces cerevisiae was cloned and its nucleotide sequence determined. A heat-shock element and three possible TATA boxes were found upstream of the coding region. Dual modes of transcriptional initiation were observed in primer extension analyses using as templates the mRNAs prepared from cells before and after heat-shock. Initiation sites situated 50 to 60 nucleotides downstream of the normal one were found to be additionally used in cells after heat-shock. Thus, the mode of transcription in heat-shocked cells of S. pombe appears to be more similar to the one observed in higher eukaryotes than that in S. cerevisiae. The SSP1 gene contains two methionine codons in the region predicted to encode a mitochondrial targeting signal sequence of its protein (Ssp1) and the stretch between the two methionine codons is capable of forming stem-loop structures. Both of the two methionine codons were confirmed to function as translational initiators in vitro. A possible mechanism is proposed for the response of the SSP1 gene towards heat-shock by the differential initiation of its transcription and translation.","authors":"Kasai H, Isono K","authors_abbrev":"Kasai H et al.","pubmed_publication_date":"11 Oct 1991","pubmed_entrez_date":"1991-10-11","publication_year":"1991","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:3442827","title":"Transformation of Schizosaccharomyces pombe by non-homologous, unstable integration of plasmids in the genome.","citation":"Curr Genet 1986;10(7):503-8","abstract":"In the fission yeast, Schizosaccharomyces pombe, transformation with recombinant plasmids always results in a high proportion of mitotically unstable transformants. This suggested that specialised (ARS) sequences might not be required for autonomous replication of plasmids in S. pombe, contrary to the situation in Saccharomyces cerevisiae. We have shown that specialised ARS sequences, analogous to those in S. cerevisiae, do exist in S. pombe, supporting the view that ARS elements are a general feature of eukaryotes. In addition, there is a further mechanism of plasmid maintenance which involves homologous and non-homologous integration into, and excision from the genome.","authors":"Wright AP, Maundrell K, Shall S","authors_abbrev":"Wright AP et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:853033","title":"Conjugation-induced lysis of Schizosaccharomyces pombe.","citation":"J Bacteriol 1977 Apr;130(1):512-5","abstract":"About 15% of the conjugating cells of Schizosaccharomyces pombe were observed to lyse spontaneously during the conjugation process. Lysis occurred at the site of union.","authors":"Calleja GB, Yoo BY, Johnson BF","authors_abbrev":"Calleja GB et al.","pubmed_publication_date":"Apr 1977","pubmed_entrez_date":"1977-04-01","publication_year":"1977","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36426865","title":"The role of anillin/Mid1p during medial division and cytokinesis: from fission yeast to cancer cells.","citation":"Cell Cycle 2023;22(6):633-644","abstract":"Cytokinesis is the final stage of cell division cycle when cellular constituents are separated to produce two daughter cells. This process is driven by the formation and constriction of a contractile ring. Progression of these events is controlled by mechanisms and proteins that are evolutionary conserved in eukaryotes from fungi to humans. Genetic and molecular studies in different model organisms identified essential cytokinesis genes, with several conserved proteins, including the anillin/Mid1p proteins, constituting the core cytokinetic machinery. The fission yeast  Schizosaccharomyces pombe  represents a well-established model organism to study eukaryotic cell cycle regulation. Cytokinesis in fission yeast and mammalian cells depends on the placement, assembly, maturation, and constriction of a medially located actin-myosin contractile ring (ACR). Here, we review aspects of the ACR assembly and cytokinesis process in fission yeast and consider the regulation of such events in mammalian cells. First, we briefly describe the role of anillin during mammalian ACR assembly and cytokinesis. Second, we describe different aspects of the anillin-like protein Mid1p regulation during the  S. pombe  cell cycle, including its structure, function, and phospho-regulation. Third, we briefly discuss Mid1pindependent ACR assembly in  S. pombe . Fourth, we highlight emerging studies demonstrating the roles of anillin in human tumourigenesis introducing anillin as a potential drug target for cancer treatment. Collectively, we provide an overview of the current understanding of medial division and cytokinesis in  S. pombe  and suggest the implications of these observations in other eukaryotic organisms, including humans.","doi":"10.1080/15384101.2022.2147655","authors":"Rezig IM, Yaduma WG, Gould GW, McInerny CJ","authors_abbrev":"Rezig IM et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2022-11-25","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-11-26 01:15:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4B3.15"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21660689","title":"Detection of covalent DNA-bound Spo11 and topoisomerase complexes.","citation":"Methods Mol Biol 2011;745:65-77","abstract":"Topoisomerases can release topological stress and resolve DNA catenanes by a DNA strand breakage and re-ligation mechanism. During the lifetime of the DNA break, the topoisomerase remains covalently linked to the DNA and removes itself when the break is re-ligated. While the lifetime of a covalent topoisomerase-DNA complex is usually short, several clinically important cancer drugs kill cancer cells by inhibiting the removal of covalently linked topoisomerases. The topoisomerase-like protein Spo11 is responsible for meiotic double strand break formation. Spo11 is not able to remove itself and is removed by nucleolytic cleavage. This chapter describes a method which allows the reproducible and quantitative detection of proteins covalently bound to the DNA.","doi":"10.1007/978-1-61779-129-1_5","authors":"Hartsuiker E","authors_abbrev":"Hartsuiker E","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-06-11","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29686279","title":"Iron homeostasis regulates facultative heterochromatin assembly in adaptive genome control.","citation":"Nat Struct Mol Biol 2018 May;25(5):372-383","abstract":"Iron metabolism is critical for sustaining life and maintaining human health. Here, we find that iron homeostasis is linked to facultative heterochromatin assembly and regulation of gene expression during adaptive genome control. We show that the fission yeast Clr4/Suv39h histone methyltransferase is part of a rheostat-like mechanism in which transcriptional upregulation of mRNAs in response to environmental change provides feedback to prevent their uncontrolled expression through heterochromatin assembly. Interestingly, proper iron homeostasis is required, as iron depletion or downregulation of iron transporters causes defects in heterochromatin assembly and unrestrained upregulation of gene expression. Remarkably, an unbiased genetic screen revealed that restoration of iron homeostasis is sufficient to re-establish facultative heterochromatin and proper gene control genome-wide. These results establish a role for iron homeostasis in facultative heterochromatin assembly and reveal a dynamic mechanism for reprogramming the genome in response to environmental changes.","doi":"10.1038/s41594-018-0056-2","authors":"Gallagher PS, Larkin M, Thillainadesan G, Dhakshnamoorthy J, Balachandran V, Xiao H, Wellman C, Chatterjee R, Wheeler D, Grewal SIS","authors_abbrev":"Gallagher PS et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-04-25","publication_year":"2018","canto_session_key":"512da903984f030c","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-04-26 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23E2.01","SPBC428.08c","SPBC23E6.09","SPCC31H12.08c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:27851952","title":"Shape Transformation of the Nuclear Envelope during Closed Mitosis.","citation":"Biophys J 2016 Nov 15;111(10):2309-2316","abstract":"The nuclear envelope (NE) in lower eukaryotes such as Schizosaccharomyces pombe undergoes large morphology changes during closed mitosis. However, which physical parameters are important in governing the shape evolution of the NE, and how defects in the dividing chromosomes/microtubules are reflected in those parameters, are fundamental questions that remain unresolved. In this study, we show that improper separation of chromosomes in genetically deficient cells leads to membrane tethering or asymmetric division in contrast to the formation of two equal-sized daughter nuclei in wild-type cells. We hypothesize that the poleward force is transmitted to the nuclear membrane through its physical contact with the separated sister chromatids at the two spindle poles. A theoretical model is developed to predict the morphology evolution of the NE where key factors such as the work done by the poleward force and bending and surface energies stored in the membrane have been taken into account. Interestingly, the predicted phase diagram, summarizing the dependence of nuclear shape on the size of the load transmission regions, and the pole-to-pole distance versus surface area relationship all quantitatively agree well with our experimental observations, suggesting that this model captures the essential physics involved in closed mitosis.","doi":"10.1016/j.bpj.2016.10.004","authors":"Zhu Q, Zheng F, Liu AP, Qian J, Fu C, Lin Y","authors_abbrev":"Zhu Q et al.","pubmed_publication_date":"15 Nov 2016","pubmed_entrez_date":"2016-11-17","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-11-18 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11369198","title":"M phase-specific kinetochore proteins in fission yeast: microtubule-associating Dis1 and Mtc1 display rapid separation and segregation during anaphase.","citation":"Curr Biol 2001 Apr 17;11(8):537-49","abstract":"Kinetochore microtubules are made early in mitosis and link chromosomal kinetochores to the spindle poles. They are required later to move the separated sister chromatids toward the opposite poles upon the onset of anaphase. Very little is known about proteins that are responsible for the connection between kinetochores and mitotic microtubules.\nWe here show that fission yeast Dis1 and the related protein Mtc1/Alp14 are both able to bind microtubules in vitro and share an essential function for viability in vivo. The deletion of mtc1+ results in an instability of cytoplasmic microtubules that can be suppressed by the ectopic expression of dis1+. Dis1 and Mtc1 are localized along interphase cytoplasmic microtubules and are mobilized onto the spindle upon mitotic commitment. In chromatin immunoprecipitation (CHIP) experiments Dis1 coprecipitated with the central centromeric DNA in an M phase-specific manner. Consistently, observations of both living cells in which the native, genomic copy of dis1+ tagged with GFP and cells fixed by immunostaining established that Dis1 behaves as a kinetochore protein during the progression from metaphase to anaphase. The central and C-terminal regions of Dis1 are sufficient for interactions with microtubules and the kinetochore, respectively. In anaphase, the GFP signals of both Dis1 and Mtc1 suddenly separate and move quickly toward opposite spindle poles.\nFission yeast Dis1 and Mtc1 are members of an evolutionarily conserved microtubule binding protein family that includes frog XMAP215. Dis1 and Mtc1 are implicated in stabilizing kinetochore microtubules in metaphase and so counteract the action of microtubule destabilizing factors that dominate in anaphase. Dis1 may play a dual role by becoming a part of the kinetochores in an M phase-specific manner, and it may possibly generate connections between kinetochores and microtubules.","authors":"Nakaseko Y, Goshima G, Morishita J, Yanagida M","authors_abbrev":"Nakaseko Y et al.","pubmed_publication_date":"17 Apr 2001","pubmed_entrez_date":"2001-05-23","publication_year":"2001","canto_session_key":"4d9c10ab5ce2986c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-08-18 15:57:25","canto_approved_date":"2021-04-19 10:58:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-17 16:41:36","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.04c","SPCC736.14","SPCC895.07"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-08-18"},{"uniquename":"PMID:33946513","title":"The Putative RNA-Binding Protein Dri1 Promotes the Loading of Kinesin-14/Klp2 to the Mitotic Spindle and Is Sequestered into Heat-Induced Protein Aggregates in Fission Yeast.","citation":"Int J Mol Sci 2021 Apr 30;22(9)","abstract":"Cells form a bipolar spindle during mitosis to ensure accurate chromosome segregation. Proper spindle architecture is established by a set of kinesin motors and microtubule-associated proteins. In most eukaryotes, kinesin-5 motors are essential for this process, and genetic or chemical inhibition of their activity leads to the emergence of monopolar spindles and cell death. However, these deficiencies can be rescued by simultaneous inactivation of kinesin-14 motors, as they counteract kinesin-5. We conducted detailed genetic analyses in fission yeast to understand the mechanisms driving spindle assembly in the absence of kinesin-5. Here, we show that deletion of the  dri1  gene, which encodes a putative RNA-binding protein, can rescue temperature sensitivity caused by  cut7-22 , a fission yeast kinesin-5 mutant. Interestingly, kinesin-14/Klp2 levels on the spindles in the  cut7  mutants were significantly reduced by the  dri1  deletion, although the total levels of Klp2 and the stability of spindle microtubules remained unaffected. Moreover, RNA-binding motifs of Dri1 are essential for its cytoplasmic localization and function. We have also found that a portion of Dri1 is spatially and functionally sequestered by chaperone-based protein aggregates upon mild heat stress and limits cell division at high temperatures. We propose that Dri1 might be involved in post-transcriptional regulation through its RNA-binding ability to promote the loading of Klp2 on the spindle microtubules.","doi":"10.3390/ijms22094795","authors":"Yukawa M, Ohishi M, Yamada Y, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"30 Apr 2021","pubmed_entrez_date":"2021-05-05","publication_year":"2021","canto_session_key":"297469ade6812e26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masashi Yukawa","canto_first_approved_date":"2021-06-08 08:28:11","canto_approved_date":"2023-01-26 07:24:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-18 00:28:40","canto_added_date":"2021-05-07 00:15:18","annotation_curators":[{"name":"Masashi Yukawa","community_curator":true,"annotation_count":35,"orcid":"0000-0002-1723-890X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.02c","SPAC13G7.02c","SPAC926.04c","SPAC18G6.15","SPBC16D10.08c","SPBC16A3.05c","SPBC3B9.21","SPCC1739.13","SPAC57A7.04c","SPBC1734.11","SPAC664.10","SPAC25G10.07c","SPCC830.07c","SPAC17H9.04c"],"gene_count":14,"ltp_gene_count":6,"approved_date":"2021-06-08"},{"uniquename":"PMID:36202103","title":"Condensation of the fusion focus by the intrinsically disordered region of the formin Fus1 is essential for cell-cell fusion.","citation":"Curr Biol 2022 Nov 07;32(21):4752-4761.e10","abstract":"Secretory vesicle clusters transported on actin filaments by myosin V motors for local secretion underlie various cellular processes, such as neurotransmitter release at neuronal synapses, 1  hyphal steering in filamentous fungi, 2  ,  3  and local cell wall digestion preceding the fusion of yeast gametes. 4  During fission yeast Schizosaccharomyces pombe gamete fusion, the actin fusion focus assembled by the formin Fus1 concentrates secretory vesicles carrying cell wall digestive enzymes. 5  ,  6  ,  7  The position and coalescence of the vesicle focus are controlled by local signaling and actin-binding proteins to prevent inappropriate cell wall digestion that would cause lysis, 6  ,  8  ,  9  ,  10  but the mechanisms of focusing have been elusive. Here, we show that the regulatory N terminus of Fus1 contains an intrinsically disordered region (IDR) that mediates Fus1 condensation in vivo and forms dense assemblies that exclude ribosomes. Fus1 lacking its IDR fails to concentrate in a tight focus and causes cell lysis during attempted cell fusion. Remarkably, the replacement of Fus1 IDR with a heterologous low-complexity region that forms molecular condensates fully restores Fus1 focusing and function. By contrast, the replacement of Fus1 IDR with a domain that forms more stable oligomers restores focusing but poorly supports cell fusion, suggesting that condensation is tuned to yield a selectively permeable structure. We propose that condensation of actin structures by an IDR may be a general mechanism for actin network organization and the selective local concentration of secretory vesicles.","doi":"10.1016/j.cub.2022.09.026","authors":"Billault-Chaumartin I, Muriel O, Michon L, Martin SG","authors_abbrev":"Billault-Chaumartin I et al.","pubmed_publication_date":"07 Nov 2022","pubmed_entrez_date":"2022-10-06","publication_year":"2022","canto_session_key":"d8f932ddae176e0b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2025-04-10 07:35:54","canto_approved_date":"2026-04-24 14:09:50","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-01 06:26:54","canto_added_date":"2022-10-08 00:15:04","annotation_curators":[{"name":"Sophie Martin","community_curator":true,"annotation_count":57,"orcid":"0000-0002-5317-2557","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPAC20G4.02c","SPCC1223.06","SPBC2D10.14c","SPAC631.01c","SPCC1919.10c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2025-04-10"},{"uniquename":"PMID:26389686","title":"Open and closed HORMAs regulate autophagy initiation.","citation":"Autophagy 2015 Nov 02;11(11):2123-2124","abstract":"The Atg1/ULK complex functions as the most upstream factor among Atg proteins to initiate autophagy. ATG101 is a constitutive component of the Atg1/ULK complex in most eukaryotes except for budding yeast, and plays an essential role in autophagy; however, the structure and functions of ATG101 were largely unknown. Recently, we determined the crystal structure of fission yeast Atg101 in complex with the closed HORMA domain of Atg13, revealing that Atg101 is also a HORMA protein with an open conformation. These 2 HORMA proteins play essential roles in autophagy initiation through recruiting downstream factors to the autophagosome formation site.","doi":"10.1080/15548627.2015.1091144","authors":"Suzuki H, Kaizuka T, Mizushima N, Noda NN","authors_abbrev":"Suzuki H et al.","pubmed_publication_date":"02 Nov 2015","pubmed_entrez_date":"2015-09-22","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-09-23 00:19:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25H1.03","SPAC4F10.07c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:7588609","title":"Fission yeast Rep2 is a putative transcriptional activator subunit for the cell cycle 'start' function of Res2-Cdc10.","citation":"EMBO J 1995 Oct 02;14(19):4794-802","abstract":"In the yeast cell cycle 'start' requires sets of the Cdc10/ SWI family of transcriptional factors which activate the MCB cis elements contained in genes essential for S phase progression. Fission yeast possess two such overlapping systems, Res1-Cdc10 and Res2-Cdc10, both of which act to start the mitotic and meiotic cycles. We have recently isolated rep2+ as a multicopy suppressor of a temperature-sensitive cdc10 mutant which encodes a zinc finger protein. Here we show that the Rep2 zinc finger protein is an essential component of the active Res2-Cdc10 transcriptional regulator complex and likely to play a role in the control of cell cycle 'start'. Our data suggest that Rep2 is a transcriptional activator subunit which interacts with the MCB binding subunit complex formed by Res2 and Cdc10.","authors":"Nakashima N, Tanaka K, Sturm S, Okayama H","authors_abbrev":"Nakashima N et al.","pubmed_publication_date":"02 Oct 1995","pubmed_entrez_date":"1995-10-02","publication_year":"1995","canto_session_key":"fb7a0a2c9bb5df54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-02-01 17:30:06","canto_approved_date":"2024-06-28 11:04:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-03-13 17:32:26","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.11c","SPAC22F3.09c","SPBC725.16","SPBC2D10.06","SPBC336.12c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-02-01"},{"uniquename":"PMID:17571595","title":"[Recombination mediators].","citation":"Seikagaku 2007 May;79(5):449-53","abstract":"","authors":"Haruta-Takahashi N, Iwasaki H","authors_abbrev":"Haruta-Takahashi N et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-06-19","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38575358","title":"Acetylation of Rec8 cohesin complexes regulates reductional chromosome segregation in meiosis.","citation":"Life Sci Alliance 2024 Jun;7(6)","abstract":"For establishing sister chromatid cohesion and proper chromosome segregation in mitosis in fission yeast, the acetyltransferase Eso1 plays a key role. Eso1 acetylates cohesin complexes, at two conserved lysine residues K105 and K106 of the cohesin subunit Psm3. Although Eso1 also contributes to reductional chromosome segregation in meiosis, the underlying molecular mechanisms have remained elusive. Here, we purified meiosis-specific Rec8 cohesin complexes localized at centromeres and identified a new acetylation at Psm3-K1013, which largely depends on the meiotic kinetochore factor meikin (Moa1). Our molecular genetic analyses indicate that Psm3-K1013 acetylation cooperates with canonical acetylation at Psm3-K105 and K106, and plays a crucial role in establishing reductional chromosome segregation in meiosis.","doi":"10.26508/lsa.202402606","authors":"Li Z, Liu Y, Jones AW, Watanabe Y","authors_abbrev":"Li Z et al.","pubmed_publication_date":"Jun 2024","pubmed_entrez_date":"2024-04-04","publication_year":"2024","canto_session_key":"71258840c50eb005","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-04-05 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14511667","title":"A mutation in the gene involved in sister chromatid separation causes a defect in nuclear mRNA export in fission yeast.","citation":"Biochem Biophys Res Commun 2003 Oct 10;310(1):176-81","abstract":"Fission yeast ptr4-1 is one of the mRNA transport mutants that accumulate poly(A)(+) RNA in the nuclei at the nonpermissive temperature. We cloned the ptr4(+) gene and found that it is identical with the cut1(+) gene essential for chromosome segregation during mitosis. ptr4/cut1 has no defects in nucleocytoplasmic transport of a protein, indicative of a specific blockage of mRNA export by this mutation. A mutant of Cut2p cooperating with Cut1p in sister chromatid separation also showed defective mRNA export at the nonpermissive temperature. Our results suggest a novel linkage between the cell division cycle and nuclear mRNA export in eukaryotic cells.","authors":"Kalam Azad A, Ideue T, Ohshima Y, Tani T","authors_abbrev":"Kalam Azad A et al.","pubmed_publication_date":"10 Oct 2003","pubmed_entrez_date":"2003-09-27","publication_year":"2003","canto_session_key":"a4b01302c184e336","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-02-10 09:21:28","canto_approved_date":"2021-02-26 15:36:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-16 10:58:30","canto_added_date":"2012-02-24 05:50:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.01c","SPCC5E4.04"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2016-02-10"},{"uniquename":"EMBL:AB084831","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.19"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15797925","title":"The nuclear rim protein Amo1 is required for proper microtubule cytoskeleton organisation in fission yeast.","citation":"J Cell Sci 2005 Apr 15;118(Pt 8):1705-14","abstract":"Microtubules have a central role in cell division and cell polarity in eukaryotic cells. The fission yeast is a useful organism for studying microtubule regulation owing to the highly organised nature of its microtubular arrays. To better understand microtubule dynamics and organisation we carried out a screen that identified over 30 genes whose overexpression resulted in microtubule cytoskeleton abnormalities. Here we describe a novel nucleoporin-like protein, Amo1, identified in this screen. Amo1 localises to the nuclear rim in a punctate pattern that does not overlap with nuclear pore complex components. Amo1Delta cells are bent, and they have fewer microtubule bundles that curl around the cell ends. The microtubules in amo1Delta cells have longer dwelling times at the cell tips, and grow in an uncoordinated fashion. Lack of Amo1 also causes a polarity defect. Amo1 is not required for the microtubule loading of several factors affecting microtubule dynamics, and does not seem to be required for nuclear pore function.","authors":"Pardo M, Nurse P","authors_abbrev":"Pardo M et al.","pubmed_publication_date":"15 Apr 2005","pubmed_entrez_date":"2005-03-31","publication_year":"2005","canto_session_key":"55601848bf58a3e9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-19 10:53:16","canto_approved_date":"2026-01-25 05:13:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-09-17 06:23:18","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":283,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_15797925_phaf.tsv"}],"genes":["SPBC336.11","SPBC3B8.04c","SPCC1223.06","SPBC16H5.07c","SPBC543.02c","SPBC6B1.10","SPAC19E9.02","SPBC887.17","SPBC359.03c","SPBP4H10.07","SPCC1827.03c","SPCC825.02","SPCC417.07c","SPBC3H7.03c","SPBC14C8.05c","SPBC1347.02","SPAC10F6.14c","SPBC26H8.07c","SPBC11B10.05c","SPAC18G6.07c","SPCC306.06c","SPBC21D10.05c","SPCC1682.12c","SPBPJ4664.04","SPAC1687.10","SPAC23C4.12","SPAC1F8.05","SPBC16E9.02c","SPAC24C9.05c","SPBC146.11c","SPAC26A3.16","SPBC25B2.07c","SPAC22G7.09c","SPBC2F12.05c","SPAC23G3.06","SPCC1840.04","SPBC365.15","SPAC3A11.02","SPBC1734.11","SPAC21E11.03c","SPAC17G6.13","SPAC3C7.12","SPCC4G3.19","SPBC2F12.13","SPBC15D4.10c"],"gene_count":45,"ltp_gene_count":40,"approved_date":"2017-07-19"},{"uniquename":"PMID:3446375","title":"Distribution of mitochondrial introns in the species Schizosaccharomyces pombe and the origin of the group II intron in the gene encoding apocytochrome b.","citation":"Curr Genet 1987;12(5):329-36","abstract":"The mitochondrial genome size of 26 different Schizosaccharomyces pombe strains varies between 17.6 and 24.6 kilobase pairs due to the presence or absence of introns. One of these is the group II intron in the gene encoding apocytochrome b (cob: intron cobI1). Partial DNA sequences of continuous cob genes from six strains (including strain EF1: Trinkl et al. 1985) revealed identical nucleotide sequence in the region where the group II intron is inserted in the mosaic form of the gene. In contrast, analysis of the mosaic cob gene in strain UCD-FstI revealed several base pair changes in the exon regions flanking the splice point, compared with the continuous genes and with the mosaic cob gene in strain 50 (Lang et al. 1985). The base pair differences between the exons of the two mosaic cob genes and the identity of exons in all continuous cob genes argue in favour of the two cob introns in strains 50 and UCD-FstI as independent later acquisitions of the genes, rather than loss of the intron from a common mosaic ancestor of all strains. Other introns present in some but not all strain include two group I introns without open reading frame in the gene encoding subunit 1 of cytochrome c oxidase (cox1: introns cox1I2a and cox1I3), and two group I introns with open reading frames in the same gene (introns cox1I1 and cox1I2b).","authors":"Zimmer M, Welser F, Oraler G, Wolf K","authors_abbrev":"Zimmer M et al.","pubmed_publication_date":"1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26424849","title":"Dynamic modulation of Dnmt2-dependent tRNA methylation by the micronutrient queuine.","citation":"Nucleic Acids Res 2015 Dec 15;43(22):10952-62","abstract":"Dnmt2 enzymes are cytosine-5 methyltransferases that methylate C38 of several tRNAs. We report here that the activities of two Dnmt2 homologs, Pmt1 from Schizosaccharomyces pombe and DnmA from Dictyostelium discoideum, are strongly stimulated by prior queuosine (Q) modification of the substrate tRNA. In vivo tRNA methylation levels were stimulated by growth of cells in queuine-containing medium; in vitro Pmt1 activity was enhanced on Q-containing RNA; and queuine-stimulated in vivo methylation was abrogated by the absence of the enzyme that inserts queuine into tRNA, eukaryotic tRNA-guanine transglycosylase. Global analysis of tRNA methylation in S. pombe showed a striking selectivity of Pmt1 for tRNA(Asp) methylation, which distinguishes Pmt1 from other Dnmt2 homologs. The present analysis also revealed a novel Pmt1- and Q-independent tRNA methylation site in S. pombe, C34 of tRNA(Pro). Notably, queuine is a micronutrient that is scavenged by higher eukaryotes from the diet and gut microflora. This work therefore reveals an unanticipated route by which the environment can modulate tRNA modification in an organism.","doi":"10.1093/nar/gkv980","authors":"Müller M, Hartmann M, Schuster I, Bender S, Thüring KL, Helm M, Katze JR, Nellen W, Lyko F, Ehrenhofer-Murray AE","authors_abbrev":"Müller M et al.","pubmed_publication_date":"15 Dec 2015","pubmed_entrez_date":"2015-10-02","publication_year":"2015","canto_session_key":"466ed4e946c15c3f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ann Ehrenhofer-Murray","canto_first_approved_date":"2017-03-30 05:51:32","canto_approved_date":"2025-03-13 18:38:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-12 13:16:49","canto_added_date":"2015-10-03 00:19:00","annotation_curators":[{"name":"Ann Ehrenhofer-Murray","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPATRNAASP.01","SPAC2F3.13c","SPBC19C2.02","SPAC1687.19c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-03-30"},{"uniquename":"PMID:12678777","title":"Nucleo-cytoplasmic transport of proteins as a target for therapeutic drugs.","citation":"Curr Med Chem 2003 May;10(9):741-8","abstract":"Recruitment of cytoplasmic signaling proteins into the nucleus is an essential step in the activation of gene expression in response to an extracellular signal. Nucleo-cytoplasmic transport of macromolecules is mediated by the transport receptors of an importin beta family. Post-translational modifications and masking/unmasking of specific signal sequences responsible for nuclear import and export are important for the coordinated control of the nucleo-cytoplasmic transport. Malfunctioning of the nucleo-cytoplasmic transport is profoundly involved in a number of diseases including cancer. Leptomycin B (LMB) is a Streptomyces metabolite that causes specific inhibition of the cell cycle of fission yeast and mammalian cells. The target molecule of LMB has been shown by genetic and biochemical analyses to be CRM1, a highly conserved protein in eukaryotes. CRM1 was shown to be a member of the importin beta family and a receptor for the nuclear export signal (NES) of proteins in both yeast and mammalian cells. LMB binds directly to CRM1, which results in dissociation of the NES from the nuclear export machinery containing CRM1. Thus, LMB serves as a potent tool for understanding the molecular mechanisms of nucleo-cytoplasmic transport of proteins and a potential therapeutic drug for diseases caused by mislocalization of regulatory proteins.","authors":"Yashiroda Y, Yoshida M","authors_abbrev":"Yashiroda Y et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-04-08","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8614629","title":"Characterization of a UV endonuclease gene from the fission yeast Schizosaccharomyces pombe and its bacterial homolog.","citation":"Nucleic Acids Res 1996 Apr 01;24(7):1267-71","abstract":"From the fission yeast Schizosaccharomyces pombe, a cDNA fragment was isolated, which confers UV resistance on repair deficient Escherichia coli host cells. The cloned cDNA encodes a protein of 68,815 Da, which has a 36.6% identity of amino acid sequence with the previously identified 74 kDa UV endonuclease of the filamentous fungus Neurospora crassa. Analysis of several truncated gene constructs shows that only the C-terminal two thirds region, which has 54% identity of amino acid sequence with the C-terminal region of the Neurospora homolog, is necessary for complementing activity of UV-sensitivity in the E. coli host cells. Purified recombinant protein from E. coli host cells incises both UV-induced cyclobutane pyrimidine dimers and (6-4) photoproducts at the sites immediately 5' to the DNA damage in the same fashion as the Neurospora protein. Furthermore, a bacterial homologous sequence was isolated from Bacillus subtilis and shows a similar complementing activity of UV sensitivity in E. coli host cells, indicating a wide distribution of this alternative excision repair mechanism in life.","authors":"Takao M, Yonemasu R, Yamamoto K, Yasui A","authors_abbrev":"Takao M et al.","pubmed_publication_date":"01 Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_session_key":"e0a628fa3c3b15cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-01 11:36:35","canto_approved_date":"2025-03-12 06:58:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-01 11:36:29","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-01"},{"uniquename":"PMID:17673174","title":"Translation initiation factor eIF1A possesses RNA annealing activity in its oligonucleotide-binding fold.","citation":"Biochem Biophys Res Commun 2007 Sep 28;361(3):681-6","abstract":"Translation initiation factor eIF1A is highly conserved among all eukaryotes, and performs essential functions in the formation of 43S preinitiation complex and mRNA scanning. In this study, we found that RNA annealing activity is intrinsically associated with eIF1A. Schizosaccharomyces pombe, Saccharomyces cerevisiae, and human eIF1As were isolated in their recombinant forms in order to determine their RNA annealing activities. A truncated eIF1A devoid of both N- and C-terminal domains proved most active, indicating that the activity is localized in the OB-fold domain. Some N- or C-terminal His tag fusions were shown to make the proteins inactive. This is probably caused by shielding of the RNA binding surface, as the proteins were activated via partial proteolytic digestion. We also found that eIF1A formed a stable complex with a short double-stranded RNA in gel mobility shift assays. Our results indicate that eIF1A may function as an RNA chaperone, inducing conformational changes in rRNA in the 43S preinitiation complex.","authors":"Kwon SH, Lee IH, Kim NY, Choi DH, Oh YM, Bae SH","authors_abbrev":"Kwon SH et al.","pubmed_publication_date":"28 Sep 2007","pubmed_entrez_date":"2007-08-04","publication_year":"2007","canto_session_key":"eecef90e41dfa02e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-01-10 16:49:03","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-01-10 16:38:22","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-01-10"},{"uniquename":"PMID:10526238","title":"Overproduction of elongation factor 1alpha, an essential translational component, causes aberrant cell morphology by affecting the control of growth polarity in fission yeast.","citation":"Genes Cells 1999 Sep;4(9):517-27","abstract":"Elongation factor 1alpha (EF1alpha), an essential component of the eukaryotic translational machinery, has been shown to possess various biochemical and biological activities, including F-actin-binding and -bundling, microtubule- severing, and the activity of making fibroblasts highly susceptible to transformation. However, our understanding of the biological significance of EF1alpha with respect to these various biochemical or biological activities remains limited. Here we report the identification of EF1alpha-encoding genes as genes whose over-expression causes aberrant cell morphology in fission yeast.\nOverproduction of EF1alpha caused aberrant cell morphology-elliptic, curved or branched-and growth defects in yeast cells at high temperatures. EF1alpha-overproducing cells showed a supersensitivity to the actin inhibitor cytochalasin D and to the tubulin inhibitor thiabendazole. Genetic analyses using cdc mutants suggested that excess EF1alpha disturbed the establishment and the maintenance of growth polarity in the G1 phase by pre- venting the localization of F-actin to the polarized growing site and the organization of microtubules. Results from DNase I column chromatography indicated that EF1alpha was bound to G-actin. Indeed, the fission yeast actin was immunoprecipitated along with EF1alpha. Moreover, the temperature sensitivity caused by the overproduction of EF1alpha was restored by co-overproduction of actin.\nFission yeast EF1alpha has the ability to alter the cell morphology of yeast by affecting the control of actin and microtubule cytoskeletons.","authors":"Suda M, Fukui M, Sogabe Y, Sato K, Morimatsu A, Arai R, Motegi F, Miyakawa T, Mabuchi I, Hirata D","authors_abbrev":"Suda M et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-10-20","publication_year":"1999","canto_session_key":"556cdf2a4ce24e23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-01 18:25:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-07 13:30:50","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPCC794.09c","SPAC23A1.10","SPBC839.15c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-08-07"},{"uniquename":"PMID:5796945","title":"Evaluation of the genetic alterations induced by chemical mutagens in Schizosaccharomyces pombe.","citation":"Mutat Res 1969;8(1):65-71","abstract":"","authors":"Loprieno N, Guglielminetti R, Bonatti S, Abbondandolo A","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"1969","pubmed_entrez_date":"1969-07-01","publication_year":"1969","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PB_REF:0000003","title":"Disease Association Curation","abstract":"PomBase curators manually curate \"disease association\" annotations for S. pombe genes that have human orthologs, where the ortholog is implicated in disease. Disease descriptions are manually mapped to Monarch Disease Ontology (MONDO) terms via MONDO IDs.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.14c","SPAC1D4.12","SPBC83.01","SPBC1706.03","SPAC1F5.07c","SPBC1539.03c","SPAC343.10","SPAC22A12.12c","SPAC21E11.06","SPAC4G9.02","SPBC12D12.05c","SPAC664.12c","SPAC2G11.08c","SPBC17G9.11c","SPAC977.17","SPAC22A12.04c","SPBC19G7.01c","SPAC3F10.04","SPBC16C6.09","SPBC577.09","SPBPB2B2.13","SPBC365.14c","SPCC830.08c","SPBC115.01c","SPCC18.09c","SPBC1718.06","SPBC2D10.14c","SPAC1556.02c","SPAC29A4.15","SPBC354.02c","SPAC17A5.01","SPAC1296.05c","SPBC25H2.02","SPBC3B9.02c","SPAC607.09c","SPCC338.17c","SPBC725.14","SPBP26C9.02c","SPCC417.10","SPBC713.07c","SPAC19B12.12c","SPAC10F6.09c","SPCC4B3.05c","SPAC6G9.10c","SPBC17D1.03c","SPCC330.08","SPBC691.02c","SPMIT.07","SPAC823.07","SPBC887.19","SPAC589.07c","SPAC12G12.16c","SPBC646.15c","SPBC2G2.15c","SPAC26F1.03","SPCC285.04","SPAC13C5.07","SPAC17H9.09c","SPAC1687.12c","SPCC364.07","SPBC1306.01c","SPAC4F8.12c","SPBC9B6.04c","SPAC16E8.17c","SPAPB1E7.09","SPAC9.12c","SPBC2A9.06c","SPCC1795.05c","SPAC3F10.11c","SPBC17G9.04c","SPAC13G6.06c","SPBC1703.15c","SPAC890.06","SPAC1783.01","SPBP23A10.15c","SPAC24C9.11","SPCP25A2.02c","SPBP23A10.16","SPBC119.06","SPCC613.10","SPBC1347.04","SPAC821.10c","SPBC4F6.05c","SPAC5D6.01","SPAC31G5.14","SPMIT.05","SPAC17G6.08","SPBC713.02c","SPBC13E7.09","SPBPB2B2.12c","SPCC18B5.03","SPBC725.07","SPAC24B11.13","SPAC11D3.18c","SPBPB10D8.02c","SPAC869.10c","SPAC23C11.09","SPAC1071.06","SPAC13G6.04","SPAC23C11.13c","SPCC757.08","SPAC4F10.18","SPAC22E12.10c","SPBC16A3.16","SPBC3E7.08c","SPAC16E8.10c","SPBC342.01c","SPAC13A11.02c","SPAC1006.01","SPAC4A8.04","SPAC12B10.06c","SPAC17G8.08c","SPAC31G5.08","SPBC17A3.10","SPBC29A10.04","SPCC16C4.01","SPBC3B8.03","SPBC1683.12","SPBC776.15c","SPAC23C4.14","SPBC800.10c","SPAC1687.09","SPAC17C9.14","SPBC16H5.06","SPAC4G9.09c","SPCC970.03","SPCC1183.01","SPBC29A3.17","SPAC20G8.04c","SPBC1734.12c","SPAC688.03c","SPCC417.07c","SPACUNK4.10","SPBC530.12c","SPBC3B8.08","SPAC1002.09c","SPBC17F3.01c","SPAC1834.04","SPBC1703.11","SPAC27D7.13c","SPBC543.10","SPCC1442.05c","SPAC4G9.10","SPAC22E12.03c","SPAC1687.01","SPAC18B11.11","SPAC22E12.11c","SPAC3A11.02","SPBC13G1.03c","SPAC637.04","SPBC11B10.01","SPBP23A10.08","SPAC19G12.11","SPAC824.07","SPCC1672.07","SPCC16A11.10c","SPBC30D10.05c","SPAC1A6.10","SPCC794.07","SPBC30D10.07c","SPAC8C9.15c","SPAC227.18","SPCC320.09","SPBC16C6.02c","SPAPB17E12.02","SPCC645.05c","SPBC660.16","SPBC30D10.21","SPAC19A8.14","SPAPB2B4.04c","SPCC1259.09c","SPAC17D4.01","SPCC330.12c","SPBC2G5.02c","SPBC11G11.04","SPBC24C6.03","SPBC354.06","SPBC1685.06","SPCC13B11.03c","SPCC338.14","SPAPB1A10.11c","SPAC1486.08","SPBC19C7.11","SPAC186.05c","SPBC1105.11c","SPBC336.04","SPBC4C3.08","SPBC3H7.03c","SPBC1773.17c","SPCC18.08","SPCP31B10.05","SPCC18B5.11c","SPAC1782.07","SPAC1039.11c","SPAC22H10.12c","SPCC757.07c","SPAC6G9.06c","SPBC839.19","SPAC26A3.15c","SPCC338.15","SPBC3B9.14c","SPBC2A9.12","SPAC7D4.09c","SPAC3C7.13c","SPAP8A3.03","SPBC8D2.04","SPBC12C2.03c","SPAC20G8.01","SPAC1F5.09c","SPAC12G12.15","SPAC31G5.16c","SPAP27G11.13c","SPCC1795.03","SPBC4B4.01c","SPBC947.02","SPAC4G9.14","SPAPB18E9.01","SPBC19G7.17","SPBPB2B2.10c","SPAC637.05c","SPBC2G2.12","SPAC23A1.19c","SPAC23H4.04","SPBC14F5.13c","SPAC12B10.12c","SPBC16H5.02","SPAC26F1.04c","SPCC794.01c","SPCPB1C11.03","SPAC29A4.04c","SPCC757.13","SPAC3H5.06c","SPAC6G10.08","SPBC83.07","SPBC119.05c","SPCC364.04c","SPBC1778.06c","SPAC17A5.06","SPBC36B7.09","SPAC27F1.06c","SPBC3D6.06c","SPBC25D12.05","SPBC21C3.08c","SPAPB17E12.03","SPAC2C4.05","SPBC11G11.02c","SPBC18E5.12c","SPBC1604.05","SPAC25G10.01","SPAC4D7.09","SPCC4B3.11c","SPAC18B11.05","SPAC2C4.07c","SPCC63.10c","SPAC7D4.06c","SPAC144.14","SPBC16A3.15c","SPAC343.14c","SPAC22F3.13","SPAC1834.10c","SPBC887.12","SPAC1952.13","SPBC30D10.13c","SPAC140.01","SPBC8D2.18c","SPAC57A7.07c","SPCC1827.07c","SPBC15D4.04","SPAC27D7.06","SPAC343.15","SPBC24C6.04","SPBC16G5.09","SPAC2C4.06c","SPAC17C9.07","SPAC30D11.01c","SPAC1851.03","SPBC30B4.06c","SPBC16A3.12c","SPBC29A3.18","SPCC11E10.07c","SPBC649.02","SPAC25H1.10c","SPBC460.05","SPCC191.07","SPCC1281.02c","SPBC1677.02","SPAC1D4.14","SPAC2G11.03c","SPBC21C3.13","SPBC1773.15","SPAC328.04","SPBC15C4.03","SPAC823.16c","SPCC584.14","SPAC1805.06c","SPBC14F5.05c","SPBP19A11.01","SPBC4F6.18c","SPBC17G9.02c","SPAC24H6.04","SPCC1183.03c","SPAC4G9.11c","SPBC13A2.02","SPAC23C11.04c","SPBC215.09c","SPAC328.08c","SPAC1805.15c","SPBP23A10.12","SPAC4F8.03","SPAC644.14c","SPAC3C7.10","SPBC26H8.12","SPCC825.02","SPBC947.01","SPAPB24D3.10c","SPAC26A3.02","SPAPB8E5.04c","SPAC22A12.07c","SPAC30C2.04","SPAC1296.04","SPBC14C8.15","SPAC17G6.10","SPBC31F10.04c","SPAC16E8.07c","SPAC4F8.07c","SPAC4A8.03c","SPCC553.03","SPBC1198.02","SPAC23G3.08c","SPBC16A3.02c","SPBC530.09c","SPBC16A3.11","SPBPJ4664.06","SPCC1494.07","SPNCRNA.214","SPAC644.07","SPAP27G11.05c","SPBC28E12.06c","SPAC1002.16c","SPBC21B10.11","SPBC428.05c","SPAC56F8.04c","SPAC3A12.18","SPAC6F6.16c","SPBPB10D8.01","SPBC336.06c","SPAC17H9.08","SPBC2G2.16","SPAC1556.08c","SPBC16E9.11c","SPAC15A10.05c","SPAC4D7.04c","SPBC660.14","SPBC36.04","SPAC29A4.14c","SPAC6C3.08","SPBC16H5.05c","SPBC21C3.19","SPBC800.07c","SPAPB17E12.11","SPAC2F7.16c","SPBP16F5.08c","SPCC1795.11","SPAC869.07c","SPBC2G5.07c","SPAC323.06c","SPAC23H3.07c","SPBC1711.17","SPAC1039.04","SPBC11C11.08","SPCC188.08c","SPAC1556.07","SPBC31E1.05","SPCC1672.06c","SPAC1782.10c","SPCC737.02c","SPBC2G2.01c","SPCC24B10.21","SPCC1672.09","SPAC630.13c","SPAC1834.05","SPAC824.02","SPAC23D3.09","SPAC26F1.06","SPBC1604.14c","SPCC126.04c","SPBC543.04","SPAC688.06c"],"gene_count":388,"ltp_gene_count":0},{"uniquename":"EMBL:AU006574","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9914167","title":"Reduced dosage of a single fission yeast MCM protein causes genetic instability and S phase delay.","citation":"J Cell Sci 1999 Feb;112 ( Pt 4):559-67","abstract":"MCM proteins are a conserved family of eukaryotic replication factors implicated in the initiation of DNA replication and in the discrimination between replicated and unreplicated chromatin. However, most mcm mutants in yeast arrest the cell cycle after bulk DNA synthesis has occurred. We investigated the basis for this late S phase arrest by analyzing the effects of a temperature-sensitive mutation in fission yeast cdc19(+ )(mcm2(+)). cdc19-P1 cells show a dramatic loss of viability at the restrictive temperature, which is not typical of all S phase mutants. The cdc19-P1 cell cycle arrest requires an intact damage-response checkpoint and is accompanied by increased rates of chromosome loss and mitotic recombination. Chromosomes from cdc19-P1 cells migrate aberrantly in pulsed-field gels, typical of strains arrested with unresolved replication intermediates. The cdc19-P1 mutation reduces the level of the Cdc19 protein at all temperatures. We compared the effects of disruptions of cdc19(+ )(mcm2(+)), cdc21(+ )(mcm4(+)), nda4(+ )(mcm5(+)) and mis5(+ )(mcm6(+)); in all cases, the null mutants underwent delayed S phase but were unable to proceed through the cell cycle. Examination of protein levels suggests that this delayed S phase reflects limiting, but not absent, MCM proteins. Thus, reduced dosage of MCM proteins allows replication initiation, but is insufficient for completion of S phase and cell cycle progression.","authors":"Liang DT, Hodson JA, Forsburg SL","authors_abbrev":"Liang DT et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-01-23","publication_year":"1999","canto_session_key":"6998329e8f9ad0bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2012-10-31 14:40:52","canto_approved_date":"2026-02-01 09:22:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-10-31 14:40:18","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPCC18B5.11c","SPBC29A10.15","SPBC4.04c","SPCC16A11.17","SPBC211.04c","SPCC1259.13"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2012-10-31"},{"uniquename":"PMID:15109785","title":"Genetic aspects of targeted insertion mutagenesis in yeasts.","citation":"FEMS Microbiol Rev 2004 May;28(2):201-23","abstract":"Targeted insertion mutagenesis is a main molecular tool of yeast science initially applied in Saccharomyces cerevisiae. The method was extended to fission yeast Schizosaccharomyces pombe and to \"non-conventional\" yeast species, which show specific properties of special interest to both basic and applied research. Consequently, the behaviour of such non-Saccharomyces yeasts is reviewed against the background of the knowledge of targeted insertion mutagenesis in S. cerevisiae. Data of homologous integration efficiencies obtained with circular, ends-in or ends-out vectors in several yeasts are compared. We follow details of targeted insertion mutagenesis in order to recognize possible rate-limiting steps. The route of the vector to the target and possible mechanisms of its integration into chromosomal genes are considered. Specific features of some yeast species are discussed. In addition, similar approaches based on homologous recombination that have been established for the mitochondrial genome of S. cerevisiae are described.","authors":"Klinner U, Schäfer B","authors_abbrev":"Klinner U et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-04-28","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30116786","title":"Genetic regulation of mitotic competence in G 0  quiescent cells.","citation":"Sci Adv 2018 Aug;4(8):eaat5685","abstract":"Quiescent (G 0  phase) cells must maintain mitotic competence (MC) to restart the cell cycle. This is essential for reproduction in unicellular organisms and also for development and cell replacement in higher organisms. Recently, suppression of MC has gained attention as a possible therapeutic strategy for cancer. Using a  Schizosaccharomyces pombe  deletion-mutant library, we identified 85 genes required to maintain MC during the G 0  phase induced by nitrogen deprivation. G 0  cells must recycle proteins and RNA, governed by anabolism, catabolism, transport, and availability of small molecules such as antioxidants. Protein phosphatases are also essential to maintain MC. In particular, Nem1-Spo7 protects the nucleus from autophagy by regulating Ned1, a lipin. These genes, designated GZE (G-Zero Essential) genes, reveal the landscape of genetic regulation of MC.","doi":"10.1126/sciadv.aat5685","authors":"Sajiki K, Tahara Y, Uehara L, Sasaki T, Pluskal T, Yanagida M","authors_abbrev":"Sajiki K et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-08-18","publication_year":"2018","canto_session_key":"1719104d313ca4be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mitsuhiro Yanagida","canto_first_approved_date":"2018-08-27 06:23:57","canto_approved_date":"2024-05-16 13:21:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-23 03:20:11","canto_added_date":"2018-08-19 00:15:04","annotation_curators":[{"name":"Mitsuhiro Yanagida","community_curator":true,"annotation_count":85,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":120,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC74.02c","SPCC757.09c","SPAC694.04c","SPBC1711.04","SPBC4B4.10c","SPAC3A12.13c","SPCC1672.06c","SPCP1E11.05c","SPAC22H12.02","SPBC2D10.16","SPAC17G8.05","SPAC4F10.07c","SPAC8F11.02c","SPBC1685.01","SPAC20G8.10c","SPBC902.03","SPAPJ691.02","SPAC23D3.09","SPAC4F10.04","SPBC725.01","SPBC13G1.12","SPAC1B3.16c","SPBC18H10.07","SPBP8B7.13","SPCC11E10.06c","SPBC947.15c","SPAC10F6.16","SPBC16C6.11","SPBC3B9.06c","SPCC11E10.08","SPBC18E5.04","SPAPB1A10.14","SPCC24B10.11c","SPCC622.12c","SPBC4F6.06","SPCC188.02","SPCC1393.08","SPBC3B9.13c","SPBC2G2.03c","SPBC215.14c","SPAC589.07c","SPAC4F8.01","SPBC21C3.02c","SPBC13G1.08c","SPCC663.14c","SPAC1952.13","SPAC25A8.02","SPBC6B1.05c","SPAC664.02c","SPBC21C3.03","SPAC57A7.12","SPAC11H11.01","SPBC56F2.11","SPAC637.09","SPAC31G5.04","SPCC1739.07","SPBC1718.03","SPAC144.04c","SPBC428.04","SPAC17G8.06c","SPAC22F8.12c","SPAC9.13c","SPCC4G3.04c","SPAC57A10.14","SPAC25A8.01c","SPBP8B7.16c","SPAC11D3.15","SPBC3B9.11c","SPAC17A5.14","SPAC144.02","SPBC365.16","SPBC3B8.10c","SPAC1D4.03c","SPAC630.05","SPAC4G9.13c","SPAC17G6.05c","SPAC31F12.01","SPBC577.04","SPBC646.13","SPCC777.13","SPCC16C4.20c","SPAC1486.01","SPBC83.16c","SPCC970.05","SPBC83.19c","SPCC364.05","SPAC26A3.04"],"gene_count":87,"ltp_gene_count":86,"approved_date":"2018-08-27"},{"uniquename":"PMID:6772655","title":"Magnesium ions and the control of the cell cycle in yeast.","citation":"J Cell Sci 1980 Apr;42:329-56","abstract":"A study has been made of the role of magnesium ions in cell division cycle control in the fission yeast, Schizosaccharomyces pombe, and the budding yeast, Kluyveromyces fraglis. Synchronization of cell division in these organismms can be induced by restoring magnesium to magnesium-exhausted cultures. In S. pombe, a correlation exists between the time taken for cells to enter the first synchronous division and the period of magnesium exhaustion. During short-term incubation in magnesium-deficient media, S. pombe cells are observed to continue growth in length, but they fail to make a cell plate and divide; long-term magnesium deficiency results in the production of aberrant cell forms, and a reduction in viability. Analysis of total cell magnesium in cultures of both S. pombe and K. fragilis, synchronized by various induction and selection procedures, revealed that there is a fairly steady fall in magnesium concentration as cells grow, terminating in a rapid influx of magnesium just before cell division. This leads to the hypothesis that falling magnesium concentration may act as a transducer of cell size, eventually triggering spindle formation and a membrane change which permits rapid uptake of magnesium to a concentration which brings about spindle breakdown. The hypothesis was tested directly using the divalent cation ionophore, A23187, in the absence of calcium ions; the results obtained showed that a short pulse of A23187, very late in the cell cycle, accelerated cells into division and shortened the subsequent cycle. The hypothesis is discussed in relation to current models of cell cycle regulation.","authors":"Walker GM, Duffus JH","authors_abbrev":"Walker GM et al.","pubmed_publication_date":"Apr 1980","pubmed_entrez_date":"1980-04-01","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8552043","title":"Fission yeast sta mutations that stabilize an unstable minichromosome are novel cdc2-interacting suppressors and are involved in regulation of spindle dynamics.","citation":"Mol Gen Genet 1995 Dec 10;249(4):391-9","abstract":"Cytological observations have shown that the presence of unstable minichromosomes can delay progression through the early stages of mitosis in fission yeast (Schizosaccharomyces pombe), suggesting that such minichromosomes may provide a useful tool for examining the system that regulates the coordinated segregation of chromosomes. One such unstable minichromosome is a large circular minichromosome. We previously showed that the mitotic instability of this minichromosome is probably due to the frequent occurrence of catenated forms of DNA after replication. To identify genes involved in the regulation of chromosome behavior in mitosis, we isolated mutants which stabilized this minichromosome. Three loci (sta1, sta2, and sta3) were identified. Two of them were found to be suppressors of temperature-sensitive mutations in cdc2, which encodes the catalytic subunit of muturation promoting factor (MPF). They show no linkage to, and are thus different from, suc1, and cdc13, previously identified as genes that interact with cdc2. The other mutation mapped to a gene previously identified as being required for the correct formation of the mitotic spindle. Data provided in this study suggest that the sta genes are involved in the regulation of spindle dynamics to ensure proper chromosome segregation during mitosis.","authors":"Murakami S, Niwa O","authors_abbrev":"Murakami S et al.","pubmed_publication_date":"10 Dec 1995","pubmed_entrez_date":"1995-12-10","publication_year":"1995","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37854101","title":"Multiple DNA repair pathways contribute to MMS-induced post-replicative DNA synthesis in  S. pombe  .","citation":"MicroPubl Biol 2023;2023","abstract":"Replication stress can induce DNA synthesis outside of replicative S-phase. We have previously demonstrated that fission yeast cells stimulate DNA synthesis in G2-phase but not in M-phase in response to DNA alkylating agent MMS. In this study, we show that various DNA repair pathways, including translesion synthesis and break-induced replication contribute to post-replicative DNA synthesis. Checkpoint kinases, various repair and resection proteins, and multiple polymerases are also involved.","doi":"10.17912/micropub.biology.000974","authors":"Kim SM, Forsburg SL","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-10-19","publication_year":"2023","canto_session_key":"5cdd22eeb18ae2b2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-10-19 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10628857","title":"Isolation and characterization of the fission yeast gene rpa42+, which encodes a subunit shared by RNA polymerases I and III.","citation":"Mol Gen Genet 1999 Dec;262(4-5):749-57","abstract":"Eukaryotic RNA polymerases I and III share two distinct alpha-related subunits that show limited homology to the alpha subunit of Escherichia coli RNA polymerase, which forms a homodimer to nucleate the assembly of prokaryotic RNA polymerase. To gain insight into the functions of alpha-related subunits in eukaryotes, we have previously identified the alpha-related small subunit RPA17 of RNA polymerase I (and III) in Schizosaccharomyces pombe, and have shown that it is a functional homolog of Saccharomyces cerevisiae AC19. In an extension of that study, we have now isolated and characterized rpa42+, which encodes the alpha-related large subunit RPA42 of S. pombe RNA polymerase I, by virtue of the fact that its product interacts with RPA17 in the yeast two-hybrid system. We have found that rpa42+ encodes a polypeptide with an apparent molecular mass of 42 kDa, which shows 58% identity to the AC40 subunit shared by RNA polymerases I and III in S. cerevisiae. Furthermore, we have shown that rpa42+ complements a temperature-sensitive mutation in RPC40 the gene that encodes AC40 in S. cerevisiae and which is essential for cell growth. Finally, we have shown that neither RPA42 nor RPA17 can self-associate. These results provide evidence that the two distinct alpha-related subunits, RPA42 and RPA17, of RNA polymerases I and III are functionally conserved between S. pombe and S. cerevisiae, and suggest that heterodimer formation between them is essential for the assembly of RNA polymerases I and III in eukaryotes.","authors":"Imazawa Y, Imai K, Fukushima A, Hisatake K, Muramatsu M, Nogi Y","authors_abbrev":"Imazawa Y et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"2000-01-11","publication_year":"1999","canto_session_key":"afe3d414d33758a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-02 15:46:42","canto_approved_date":"2024-12-19 16:51:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 13:49:37","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1289.07c","SPAC1687.01"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-04-02"},{"uniquename":"EMBL:AU013235","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14758541","title":"The transcription factor Pap1/Caf3 plays a central role in the determination of caffeine resistance in Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2004 Mar;271(2):161-70","abstract":"We previously identified four nuclear genes (caf1+-caf4+) in Schizosaccharomyces pombe, mutations in which confer resistance to caffeine and brefeldin A. caf1+, caf2+ and caf4+ were sequenced and found to be identical to the multidrug-resistance/stress-response genes hba1, crm1 and trr1, respectively. Here we show that caf3 is allelic to pap1, which encodes an AP-1-like transcription factor. The allele associated with caffeine resistance, caf3-89, contains a single-nucleotide exchange that results in a Leu-->Ser exchange in the NES (nuclear export signal) domain of the gene product. Due to this alteration, the modified protein can not be exported from the nucleus back into the cytoplasm, and thus accumulates in the nucleus. The activity of pap1/caf3 is shown to be necessary for manifestation of the caffeine resistance caused by mutations in the genes hba1/caf1 and crm1/caf2. We also cloned two genes that confer caffeine resistance when carried on a multicopy plasmid. One of them turned out to be a truncated allele of pad1/bfr2/sks1, which codes for a subunit of the 26 S proteosome. The putative product of the other gene, designated caf5, has a structure highly similar to that of MFS permeases. It contains two groups of six transmembrane spanning domains each, with the conserved motifs WRW, PET and GAIGGPVLGP in the fifth and sixth domains. These results are all consistent with our earlier hypothesis, which suggested that the caf genes are functionally interlinked in a complex detoxification mechanism. caf5 and pad1 may also encode parts of this mechanism.","authors":"Benko Z, Fenyvesvolgyi C, Pesti M, Sipiczki M","authors_abbrev":"Benko Z et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-02-06","publication_year":"2004","canto_session_key":"d2a1d493dc361259","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-28 10:38:31","canto_approved_date":"2022-02-24 12:09:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-28 10:38:23","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC1805.17","SPBC365.13c","SPBC609.04","SPAC31G5.13","SPBC3F6.03"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-06-28"},{"uniquename":"EMBL:AU008824","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17336902","title":"Organization of interphase microtubules in fission yeast analyzed by electron tomography.","citation":"Dev Cell 2007 Mar;12(3):349-61","abstract":"Polarized cells, such as neuronal, epithelial, and fungal cells, all display a specialized organization of their microtubules (MTs). The interphase MT cytoskeleton of the rod-shaped fission yeast, Schizosaccharomyces pombe, has been extensively described by fluorescence microscopy. Here, we describe a large-scale, electron tomography investigation of S. pombe, including a 3D reconstruction of a complete eukaryotic cell volume at sufficient resolution to show both how many MTs there are in a bundle and their detailed architecture. Most cytoplasmic MTs are open at one end and capped at the other, providing evidence about their polarity. Electron-dense bridges between the MTs themselves and between MTs and the nuclear envelope were frequently observed. Finally, we have investigated structure/function relationships between MTs and both mitochondria and vesicles. Our analysis shows that electron tomography of well-preserved cells is ideally suited for describing fine ultrastructural details that were not visible with previous techniques.","authors":"Höög JL, Schwartz C, Noon AT, O'Toole ET, Mastronarde DN, McIntosh JR, Antony C","authors_abbrev":"Höög JL et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-03-06","publication_year":"2007","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29423848","title":"Analysis of Reverse Transcribed mRNA Using PCR and Polyacrylamide Gel Electrophoresis.","citation":"Methods Mol Biol 2018;1721:73-87","abstract":"The patterns of gene expression in the fission yeast Schizosaccharomyces pombe under various experimental conditions form the basis of any transcriptomic study. We describe a method involving reverse transcription of the mRNA, Polymerase Chain Reaction (PCR), and the subsequent separation of the products onto Urea-Polyacrylamide gel that can be used to study the gene expression patterns in the fission yeast. The method described is cost effective and reproducible with satisfactory resolution of expressed transcripts in the gel. The method has the following essential steps: total RNA isolation and purification, cDNA synthesis from mRNAs, PCR amplification of cDNAs, visualization of PCR products, re-amplification and cloning of the differentially expressed PCR products, sequencing the confirmed clones, and finally cDNA library screening to isolate the genes of interest. The technique is also popularly known as Differential Display Reverse Transcription (DDRT-PCR). After its invention in 1992, a number of modifications have been introduced to optimize the technique and specifically to reduce the major problem of \"false positives.\" Since understanding of specific gene expression patterns that regulate developmental and stress responses is a major concern of biology, DDRT-PCR has become a very popular molecular technique during the past two decades.","doi":"10.1007/978-1-4939-7546-4_7","authors":"Biswas P, Majumdar U, Ghosh S","authors_abbrev":"Biswas P et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41817770","title":"Decoding Cdk1 control: from mitotic thresholds to meiotic specificity.","citation":"Chromosome Res 2026 Mar 12;34(1)","abstract":"The eukaryotic cell cycle is one of the most fundamental biological processes, ensuring the accurate duplication and segregation of the genome during mitosis. Decades of research across model systems have shown that this process is orchestrated by a family of protein kinases known as cyclin-dependent kinases (Cdks). Together with their cyclin partners, Cdks act as master regulators of cell division, coordinating DNA replication, chromosome segregation, and cytokinesis with remarkable precision. The discovery of Cdks and cyclins in yeast and sea urchins, celebrated with the Nobel Prize of Hartwell, Hunt, and Nurse (awarded in 2001), established the conceptual framework for understanding how oscillations in kinase activities drive cell cycle progression in a unidirectional and irreversible manner. Over the past thirty years, a central question has been whether cell cycle control relies primarily on the quantitative level of Cdk1 activity or whether distinct qualitative functions of cyclin-Cdk1 complexes ensure the correct ordering of events. Addressing this question required new genetic and biochemical tools capable of controlling Cdk1 activity with high temporal resolution and specificity. A turning point came in 2000 with the development of the analogue-sensitive Cdk1 allele by the Shokat laboratory. This approach replaced classical temperature-sensitive alleles with a version of Cdk1 that can be selectively inhibited by bulky ATP analogues. Beyond specific inhibition, the system was soon adapted to directly label and identify Cdk1 substrates, coupling chemical genetics with the emerging power of mass spectrometry. This review outlines the conceptual frameworks of quantitative and qualitative models of Cdk1 control. It also highlights how these ideas have been experimentally dissected, tracing the development of the Cdk1 Shokat system and advances from synthetic biology and phosphoproteomics in decoding phosphorylation logic, and how these concepts apply to meiosis. These studies draw primarily on budding yeast and fission yeast which have a single Cdk, making them convenient models for studying core principles of cell cycle regulation. Key insights from vertebrates are also integrated to illustrate principles that extend to other eukaryotes.","doi":"10.1007/s10577-026-09796-4","authors":"Touati SA","authors_abbrev":"Touati SA","pubmed_publication_date":"12 Mar 2026","pubmed_entrez_date":"2026-03-12","publication_year":"2026","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2026-03-13 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23000638","title":"TFIIIC bound DNA elements in nuclear organization and insulation.","citation":"Biochim Biophys Acta 2013;1829(3-4):418-24","abstract":"tRNA genes (tDNAs) have been known to have barrier insulator function in budding yeast, Saccharomyces cerevisiae, for over a decade. tDNAs also play a role in genome organization by clustering at sites in the nucleus and both of these functions are dependent on the transcription factor TFIIIC. More recently TFIIIC bound sites devoid of pol III, termed Extra-TFIIIC sites (ETC) have been identified in budding yeast and these sites also function as insulators and affect genome organization. Subsequent studies in Schizosaccharomyces pombe showed that TFIIIC bound sites were insulators and also functioned as Chromosome Organization Clamps (COC); tethering the sites to the nuclear periphery. Very recently studies have moved to mammalian systems where pol III genes and their associated factors have been investigated in both mouse and human cells. Short interspersed nuclear elements (SINEs) that bind TFIIIC, function as insulator elements and tDNAs can also function as both enhancer - blocking and barrier insulators in these organisms. It was also recently shown that tDNAs cluster with other tDNAs and with ETCs but not with pol II transcribed genes. Intriguingly, TFIIIC is often found near pol II transcription start sites and it remains unclear what the consequences of TFIIIC based genomic organization are and what influence pol III factors have on pol II transcribed genes and vice versa. In this review we provide a comprehensive overview of the known data on pol III factors in insulation and genome organization and identify the many open questions that require further investigation. This article is part of a Special Issue entitled: Transcription by Odd Pols.","doi":"10.1016/j.bbagrm.2012.09.006","authors":"Kirkland JG, Raab JR, Kamakaka RT","authors_abbrev":"Kirkland JG et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2012-09-25","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR21286","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:18017","SPBC3B9.16c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17611416","title":"Bin1 homolog hob1 supports a Rad6-Set1 pathway of transcriptional repression in fission yeast.","citation":"Cell Cycle 2007 Jul 01;6(13):1655-62","abstract":"Bin1 encodes a mammalian BAR adapter protein with a nuclear anti-oncogenic function that is poorly understood. To gain functional insights, we investigated the role of the fission yeast homolog hob1+ in growth arrest and survival of cells treated with phleomycin, a DNA damaging drug. Unlike wild-type cells, hob1delta cells treated with phleomycin displayed a defective growth arrest phenotype, elongating abnormally without septation or cytokinesis and eventually losing viability. Genetic investigations suggested that the survival defect in hob1delta cells reflected a deficiency in a Rad6 pathway involving histone methyltransferase Set1 that leads to transcriptional repression. In support of this connection, transcription of telomeric and centromeric heterochromatin that is normally silenced by a Rad6/Set1-dependent mechanism was aberrantly activated in hob1delta cells. Taken together, these findings suggest that hob1+ may support a mechanism of transcriptional repression possibly relevant to the role of Bin1 in cancer suppression.","authors":"Ramalingam A, Prendergast GC","authors_abbrev":"Ramalingam A et al.","pubmed_publication_date":"01 Jul 2007","pubmed_entrez_date":"2007-07-06","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21D10.12","SPAC18B11.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:25154415","title":"Mediator can regulate mitotic entry and direct periodic transcription in fission yeast.","citation":"Mol Cell Biol 2014 Nov;34(21):4008-18","abstract":"Cdk8 is required for correct timing of mitotic progression in fission yeast. How the activity of Cdk8 is regulated is unclear, since the kinase is not activated by T-loop phosphorylation and its partner, CycC, does not oscillate. Cdk8 is, however, a component of the multiprotein Mediator complex, a conserved coregulator of eukaryotic transcription that is connected to a number of intracellular signaling pathways. We demonstrate here that other Mediator components regulate the activity of Cdk8 in vivo and thereby direct the timing of mitotic entry. Deletion of Mediator components Med12 and Med13 leads to higher cellular Cdk8 protein levels, premature phosphorylation of the Cdk8 target Fkh2, and earlier entry into mitosis. We also demonstrate that Mediator is recruited to clusters of mitotic genes in a periodic fashion and that the complex is required for the transcription of these genes. We suggest that Mediator functions as a hub for coordinated regulation of mitotic progression and cell cycle-dependent transcription. The many signaling pathways and activator proteins shown to function via Mediator may influence the timing of these cell cycle events.","doi":"10.1128/MCB.00819-14","authors":"Banyai G, Lopez MD, Szilagyi Z, Gustafsson CM","authors_abbrev":"Banyai G et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-08-27","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-08-28 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC589.02c","SPAC688.08","SPAC23H4.17c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:16598261","title":"Semi-conservative DNA replication through telomeres requires Taz1.","citation":"Nature 2006 Apr 06;440(7085):824-8","abstract":"Telomere replication is achieved through the combined action of the conventional DNA replication machinery and the reverse transcriptase, telomerase. Telomere-binding proteins have crucial roles in controlling telomerase activity; however, little is known about their role in controlling semi-conservative replication, which synthesizes the bulk of telomeric DNA. Telomere repeats in the fission yeast Schizosaccharomyces pombe are bound by Taz1, a regulator of diverse telomere functions. It is generally assumed that telomere-binding proteins impede replication fork progression. Here we show that, on the contrary, Taz1 is crucial for efficient replication fork progression through the telomere. Using two-dimensional gel electrophoresis, we find that loss of Taz1 leads to stalled replication forks at telomeres and internally placed telomere sequences, regardless of whether the telomeric G-rich strand is replicated by leading- or lagging-strand synthesis. In contrast, the Taz1-interacting protein Rap1 is dispensable for efficient telomeric fork progression. Upon loss of telomerase, taz1Delta telomeres are lost precipitously, suggesting that maintenance of taz1Delta telomere repeats cannot be sustained through semi-conservative replication. As the human telomere proteins TRF1 and TRF2 are Taz1 orthologues, we predict that one or both of the human TRFs may orchestrate fork passage through human telomeres. Stalled forks at dysfunctional human telomeres are likely to accelerate the genomic instability that drives tumorigenesis.","authors":"Miller KM, Rog O, Cooper JP","authors_abbrev":"Miller KM et al.","pubmed_publication_date":"06 Apr 2006","pubmed_entrez_date":"2006-04-07","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20505337","title":"Roles of the checkpoint sensor clamp Rad9-Rad1-Hus1 (911)-complex and the clamp loaders Rad17-RFC and Ctf18-RFC in Schizosaccharomyces pombe telomere maintenance.","citation":"Cell Cycle 2010 Jun 01;9(11):2237-48","abstract":"While telomeres must provide mechanisms to prevent DNA repair and DNA damage checkpoint factors from fusing chromosome ends and causing permanent cell cycle arrest, these factors associate with functional telomeres and play critical roles in the maintenance of telomeres. Previous studies have established that Tel1 (ATM) and Rad3 (ATR) kinases play redundant but essential roles for telomere maintenance in fission yeast. In addition, the Rad9-Rad1-Hus1 (911) and Rad17-RFC complexes work downstream of Rad3 (ATR) in fission yeast telomere maintenance. Here, we investigated how 911, Rad17-RFC and another RFC-like complex Ctf18-RFC contribute to telomere maintenance in fission yeast cells lacking Tel1 and carrying a novel hypomorphic allele of rad3 (DBD-rad3), generated by the fusion between the DNA binding domain (DBD) of the fission yeast telomere capping protein Pot1 and Rad3. Our investigations have uncovered a surprising redundancy for Rad9 and Hus1 in allowing Rad1 to contribute to telomere maintenance in DBD-rad3 tel1 cells. In addition, we found that Rad17-RFC and Ctf18-RFC carry out redundant telomere maintenance functions in DBD-rad3 tel1 cells. Since checkpoint sensor proteins are highly conserved, genetic redundancies uncovered here may be relevant to telomere maintenance and detection of DNA damage in other eukaryotes.","authors":"Khair L, Chang YT, Subramanian L, Russell P, Nakamura TM","authors_abbrev":"Khair L et al.","pubmed_publication_date":"01 Jun 2010","pubmed_entrez_date":"2010-05-28","publication_year":"2010","canto_session_key":"3ef85081ea5a83a3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC1952.07","SPBC29A3.14c","SPBC902.02c","SPAC9E9.08","SPAC14C4.13","SPCC23B6.03c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:9693384","title":"The fission yeast mitotic regulator win1+ encodes an MAP kinase kinase kinase that phosphorylates and activates Wis1 MAP kinase kinase in response to high osmolarity.","citation":"Mol Biol Cell 1998 Aug;9(8):2325-35","abstract":"The Schizosaccharomyces pombe win1-1 mutant has a defect in the G2-M transition of the cell cycle. Although the defect is suppressed by wis1+ and wis4+, which are components of a stress-activated MAP kinase pathway that links stress response and cell cycle control, the molecular identity of Win1 has not been known. We show here that win1+ encodes a polypeptide of 1436 residues with an apparent molecular size of 180 kDa and demonstrate that Win1 is a MAP kinase kinase kinase that phosphorylates and activates Wis1. Despite extensive similarities between Win1 and Wis4, the two MAP kinase kinase kinases have distinct functions. Wis4 is able to compensate for loss of Win1 only under unstressed conditions to maintain basal Wis1 activity, but it fails to suppress the osmosignaling defect conferred by win1 mutations. The win1-1 mutation is a spontaneous duplication of 16 nucleotides, which leads to a frameshift and production of a truncated protein lacking the kinase domain. We discuss the cell cycle phenotype of the win1-1 cdc25-22 wee1-50 mutant and its suppression by wis genes.","authors":"Samejima I, Mackie S, Warbrick E, Weisman R, Fantes PA","authors_abbrev":"Samejima I et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-08-07","publication_year":"1998","canto_session_key":"4436cb3ee9a644ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-21 15:48:34","canto_approved_date":"2022-04-02 13:15:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-29 13:54:32","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC409.07c","SPAC1006.09","SPAC9G1.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-08-21"},{"uniquename":"PMID:8590485","title":"The Saccharomyces cerevisiae HIS3 and LYS2 genes complement the Schizosaccharomyces pombe his5-303 and lys1-131 mutations, respectively: new selectable markers and new multi-purpose multicopy shuttle vectors, pSP3 and pSP4.","citation":"Curr Genet 1995 Sep;28(4):380-3","abstract":"Three new S. pombe plasmids are described. Plasmids pSP3 and pSP4 are two Schizosaccharomyces pombe ars1 multicopy vectors with the Saccharomyces cerevisiae HIS3 or LYS2 genes as selectable markers. They complement the S. pombe his5-303 or lys1-131 mutations, respectively. Plasmid pSPars1 is a vector carrying the S. pombe ars1 and a unique NdeI site which allows the introduction of any selectable marker therefore bringing a unified vector backbone for the construction of new S. pombe/S. cerevisiae/E. coli shuttle vectors. These plasmids permit classical molecular genetic techniques to be performed directly.","authors":"Cottarel G","authors_abbrev":"Cottarel G","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_session_key":"24fa84d701b6993c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-09-25 10:59:02","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-25 10:58:55","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP7G5.04c","SPBC21H7.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-09-25"},{"uniquename":"PMID:24256266","title":"Influence of long terminal repeat retrotransposons in the genomes of fission yeasts.","citation":"Biochem Soc Trans 2013 Dec;41(6):1629-33","abstract":"LTR (long terminal repeat) RTs (retrotransposons) are almost ubiquitous in eukaryotic genomes. Their abundance and selfish properties make them a major influence in the regulation and evolution of their host genome. Recently, several striking properties of the LTR RTs of fission yeast have been uncovered, affecting important cellular processes such as gene regulation, nuclear architecture and genome integrity. The present review summarizes the current information and puts it in the context of the wider search for understanding the influence of transposable elements on the host genome.","doi":"10.1042/BST20130207","authors":"Zaratiegui M","authors_abbrev":"Zaratiegui M","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24095860","title":"Specification of DNA replication origins and genomic base composition in fission yeasts.","citation":"J Mol Biol 2013 Nov 29;425(23):4706-13","abstract":"In the \"Replicon Theory\", Jacob, Brenner and Cuzin proposed the existence of replicators and initiators as the two major actors in DNA replication. Over the years, many protein components of initiators have been shown to be conserved in different organisms during evolution. By contrast, replicator DNA sequences (often referred to as replication origins) have diverged beyond possible comparison between eukaryotic genomes. Replication origins in the fission yeast Schizosaccharomyces pombe are made up of A+T-rich sequences that do not share any consensus elements. The information encoded in these replicators is interpreted by the Orc4 subunit of the ORC (origin recognition complex), which is unique among eukaryotes in that it contains a large domain harboring nine AT-hook subdomains that target ORC to a great variety of A+T-rich sequences along the chromosomes. Recently, the genomes of other Schizosaccharomyces species have been sequenced and the regions encompassing their replication origins have been identified. DNA sequence analysis and comparison of the organization of their Orc4 proteins have revealed species-specific differences that contribute to our understanding of how the specification of replication origins has evolved during the phylogenetic divergence of fission yeasts.","doi":"10.1016/j.jmb.2013.09.023","authors":"Mojardín L, Vázquez E, Antequera F","authors_abbrev":"Mojardín L et al.","pubmed_publication_date":"29 Nov 2013","pubmed_entrez_date":"2013-10-08","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1934132","title":"Mapping of four ras superfamily genes by physical and genetic means in Schizosaccharomyces pombe.","citation":"Curr Genet 1991 Sep;20(4):277-81","abstract":"Four ras superfamily genes, namely ypt1, ypt2, ypt3 and ryh1, have been located on the S. pombe linkage map. This was achieved by constructing strains carrying a new NotI cutting site and the S. cerevisiae LEU2 gene integrated next to the respective gene. The physical location of these genes of the chromosomes was then determined by NotI restriction analysis of the DNA prepared from each strain. Fine genetic mapping was carried out by conventional tetrad analysis using the integrated LEU2 gene as a marker. The results indicated that ypt1 is tightly linked to top1 on the right arm of chromosome II; that ypt2 is 2.5 cM apart from ura2 on the right arm of chromosome I; that ypt3 is tightly linked to arg3 on the left arm of chromosome I; and that rhy1 is located approximately 20 cM from ade3 on the left arm of chromosome I.","authors":"Miyake S, Tanaka A, Yamamoto M","authors_abbrev":"Miyake S et al.","pubmed_publication_date":"Sep 1991","pubmed_entrez_date":"1991-09-01","publication_year":"1991","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33540829","title":"Crosstalk between the mTOR and DNA Damage Response Pathways in Fission Yeast.","citation":"Cells 2021 Feb 02;10(2)","abstract":"Cells have developed response systems to constantly monitor environmental changes and accordingly adjust growth, differentiation, and cellular stress programs. The evolutionarily conserved, nutrient-responsive, mechanistic target of rapamycin signaling (mTOR) pathway coordinates basic anabolic and catabolic cellular processes such as gene transcription, protein translation, autophagy, and metabolism, and is directly implicated in cellular and organismal aging as well as age-related diseases. mTOR mediates these processes in response to a broad range of inputs such as oxygen, amino acids, hormones, and energy levels, as well as stresses, including DNA damage. Here, we briefly summarize data relating to the interplays of the mTOR pathway with DNA damage response pathways in fission yeast, a favorite model in cell biology, and how these interactions shape cell decisions, growth, and cell-cycle progression. We, especially, comment on the roles of caffeine-mediated DNA-damage override. Understanding the biology of nutrient response, DNA damage and related pharmacological treatments can lead to the design of interventions towards improved cellular and organismal fitness, health, and survival.","doi":"10.3390/cells10020305","authors":"Alao JP, Legon L, Rallis C","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"02 Feb 2021","pubmed_entrez_date":"2021-02-05","publication_year":"2021","canto_session_key":"5ee45f483704840e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-02-07 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7958346","title":"The ypt proteins of Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1994 May;22(2):460-3","abstract":"","authors":"Armstrong J, Pidoux A, Bowden S, Craighead M, Bone N, Robinson E","authors_abbrev":"Armstrong J et al.","pubmed_publication_date":"May 1994","pubmed_entrez_date":"1994-05-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17429064","title":"Fission yeast Taz1 and RPA are synergistically required to prevent rapid telomere loss.","citation":"Mol Biol Cell 2007 Jun;18(6):2378-87","abstract":"The telomere complex must allow nucleases and helicases to process chromosome ends to make them substrates for telomerase, while preventing these same activities from disrupting chromosome end-protection. Replication protein A (RPA) binds to single-stranded DNA and is required for DNA replication, recombination, repair, and telomere maintenance. In fission yeast, the telomere binding protein Taz1 protects telomeres and negatively regulates telomerase. Here, we show that taz1-d rad11-D223Y double mutants lose their telomeric DNA, indicating that RPA (Rad11) and Taz1 are synergistically required to prevent telomere loss. Telomere loss in the taz1-d rad11-D223Y double mutants was suppressed by additional mutation of the helicase domain in a RecQ helicase (Rqh1), or by overexpression of Pot1, a single-strand telomere binding protein that is essential for protection of chromosome ends. From our results, we propose that in the absence of Taz1 and functional RPA, Pot1 cannot function properly and the helicase activity of Rqh1 promotes telomere loss. Our results suggest that controlling the activity of Rqh1 at telomeres is critical for the prevention of genomic instability.","authors":"Kibe T, Ono Y, Sato K, Ueno M","authors_abbrev":"Kibe T et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-04-13","publication_year":"2007","canto_session_key":"29ac2c8c97f2cc6c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-24 14:22:10","canto_approved_date":"2020-07-13 13:37:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-06-24 14:22:04","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16A10.07c","SPBC29A3.14c","SPBC1778.02","SPAC2G11.12","SPBC660.13c","SPAC26H5.06","SPAC1556.01c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-06-24"},{"uniquename":"PMID:30289413","title":"Structural insights into the recognition of phosphorylated Hop1 by Mek1.","citation":"Acta Crystallogr D Struct Biol 2018 Oct 01;74(Pt 10):1027-1038","abstract":"The FHA domain-containing protein Mek1 is a meiosis-specific kinase that is involved in the regulation of interhomolog recombination in meiosis in Saccharomyces cerevisiae. The recruitment and activation of Mek1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the Mek1 FHA domain. Here, crystal structures of the Mek1 FHA domain in the apo state and in complex with the Hop1 pT318 peptide are presented, demonstrating that the hydrophobic residues Phe320 and Val321 at the pT+2 and pT+3 positions in the ligand contribute to the preferential recognition. It was further found that in Schizosaccharomyces pombe Mek1 FHA binds both pT15 in its N-terminal SQ/TQ cluster domain (SCD) and pT270 in the Hop1 SCD. The results revealed the structural basis for the preferential recognition of phosphorylated Hop1 by Mek1 in S. cerevisiae and facilitate the understanding of the interaction between the S. pombe Mek1 FHA domain and its binding targets.","doi":"10.1107/S2059798318011993","authors":"Xie C, He C, Jiang Y, Yu H, Cheng L, Nshogoza G, Ala MS, Tian C, Wu J, Shi Y, Li F","authors_abbrev":"Xie C et al.","pubmed_publication_date":"01 Oct 2018","pubmed_entrez_date":"2018-10-06","publication_year":"2018","canto_session_key":"42ca6f48738fdf35","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-01 20:30:04","canto_approved_date":"2023-03-01 20:30:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-01 20:29:57","canto_added_date":"2018-10-07 00:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.02","SPAC14C4.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-03-01"},{"uniquename":"PMID:22768263","title":"Fission yeast Sec3 and Exo70 are transported on actin cables and localize the exocyst complex to cell poles.","citation":"PLoS One 2012;7(6):e40248","abstract":"The exocyst complex is essential for many exocytic events, by tethering vesicles at the plasma membrane for fusion. In fission yeast, polarized exocytosis for growth relies on the combined action of the exocyst at cell poles and myosin-driven transport along actin cables. We report here the identification of fission yeast Schizosaccharomyces pombe Sec3 protein, which we identified through sequence homology of its PH-like domain. Like other exocyst subunits, sec3 is required for secretion and cell division. Cells deleted for sec3 are only conditionally lethal and can proliferate when osmotically stabilized. Sec3 is redundant with Exo70 for viability and for the localization of other exocyst subunits, suggesting these components act as exocyst tethers at the plasma membrane. Consistently, Sec3 localizes to zones of growth independently of other exocyst subunits but depends on PIP(2) and functional Cdc42. FRAP analysis shows that Sec3, like all other exocyst subunits, localizes to cell poles largely independently of the actin cytoskeleton. However, we show that Sec3, Exo70 and Sec5 are transported by the myosin V Myo52 along actin cables. These data suggest that the exocyst holocomplex, including Sec3 and Exo70, is present on exocytic vesicles, which can reach cell poles by either myosin-driven transport or random walk.","doi":"10.1371/journal.pone.0040248","authors":"Bendezú FO, Vincenzetti V, Martin SG","authors_abbrev":"Bendezú FO et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-07-07","publication_year":"2012","canto_session_key":"c9cf7fe37e5e89fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2017-08-14 13:47:16","canto_approved_date":"2026-04-16 06:15:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-02 10:37:49","canto_added_date":"2012-07-16 10:48:28","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":26,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["YER008C","SPAC6F12.08c","SPCC895.05","SPAC17G8.12","SPCC1919.10c","SPAC110.03","SPBC106.20","SPCC622.10c","SPAC19G12.14"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2017-08-14"},{"uniquename":"PMID:24115772","title":"SIN-dependent phosphoinhibition of formin multimerization controls fission yeast cytokinesis.","citation":"Genes Dev 2013 Oct 01;27(19):2164-77","abstract":"Many eukaryotes accomplish cell division by building and constricting a medial actomyosin-based cytokinetic ring (CR). In Schizosaccharomyces pombe, a Hippo-related signaling pathway termed the septation initiation network (SIN) controls CR formation, maintenance, and constriction. However, how the SIN regulates integral CR components was unknown. Here, we identify the essential cytokinetic formin Cdc12 as a key CR substrate of SIN kinase Sid2. Eliminating Sid2-mediated Cdc12 phosphorylation leads to persistent Cdc12 clustering, which prevents CR assembly in the absence of anillin-like Mid1 and causes CRs to collapse when cytokinesis is delayed. Molecularly, Sid2 phosphorylation of Cdc12 abrogates multimerization of a previously unrecognized Cdc12 domain that confers F-actin bundling activity. Taken together, our findings identify a SIN-triggered oligomeric switch that modulates cytokinetic formin function, revealing a novel mechanism of actin cytoskeleton regulation during cell division.","doi":"10.1101/gad.224154.113","authors":"Bohnert KA, Grzegorzewska AP, Willet AH, Vander Kooi CW, Kovar DR, Gould KL","authors_abbrev":"Bohnert KA et al.","pubmed_publication_date":"01 Oct 2013","pubmed_entrez_date":"2013-10-12","publication_year":"2013","canto_session_key":"b42a7324f08b6a24","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2018-01-30 20:00:27","canto_approved_date":"2026-04-17 17:04:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-28 14:47:49","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.04c","SPCC4B3.15","SPBC1778.06c","SPBC19G7.05c","SPAC24B11.11c","SPCC645.05c","SPAC20G8.05c","SPBC32H8.12c","SPAC926.03","SPAC1782.09c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2018-01-30"},{"uniquename":"PMID:22989756","title":"RNA interference regulates the cell cycle checkpoint through the RNA export factor, Ptr1, in fission yeast.","citation":"Biochem Biophys Res Commun 2012 Oct 12;427(1):143-7","abstract":"Ago1, an effector protein of RNA interference (RNAi), regulates heterochromatin silencing and cell cycle arrest in fission yeast. However, the mechanism by which Ago1 controls cell cycle checkpoint following hydroxyurea (HU) treatment has not been elucidated. In this study, we show that Ago1 and other RNAi factors control cell cycle checkpoint following HU treatment via a mechanism independent of silencing. While silencing requires dcr1(+), the overexpression of ago1(+) alleviated the cell cycle defect in dcr1Δ. Ago1 interacted with the mRNA export factor, Ptr1. The ptr1-1 mutation impaired cell cycle checkpoint but gene silencing was unaffected. Genetic analysis revealed that the regulation of cell cycle checkpoint by ago1(+) is dependent on ptr1(+). Nuclear accumulation of poly(A)(+) RNAs was detected in mutants of ago1(+) and ptr1(+), suggesting there is a functional link between the cell cycle checkpoint and RNAi-mediated RNA quality control.","doi":"10.1016/j.bbrc.2012.09.027","authors":"Iida T, Iida N, Tsutsui Y, Yamao F, Kobayashi T","authors_abbrev":"Iida T et al.","pubmed_publication_date":"12 Oct 2012","pubmed_entrez_date":"2012-09-20","publication_year":"2012","canto_session_key":"7783d384917d0871","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.11","SPAC13G7.07","SPAC140.03","SPAC19D5.04","SPCC188.13c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"EMBL:SP26739","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23551936","title":"TORC1 signaling inhibition by rapamycin and caffeine affect lifespan, global gene expression, and cell proliferation of fission yeast.","citation":"Aging Cell 2013 Aug;12(4):563-73","abstract":"Target of rapamycin complex 1 (TORC1) is implicated in growth control and aging from yeast to humans. Fission yeast is emerging as a popular model organism to study TOR signaling, although rapamycin has been thought to not affect cell growth in this organism. Here, we analyzed the effects of rapamycin and caffeine, singly and combined, on multiple cellular processes in fission yeast. The two drugs led to diverse and specific phenotypes that depended on TORC1 inhibition, including prolonged chronological lifespan, inhibition of global translation, inhibition of cell growth and division, and reprograming of global gene expression mimicking nitrogen starvation. Rapamycin and caffeine differentially affected these various TORC1-dependent processes. Combined drug treatment augmented most phenotypes and effectively blocked cell growth. Rapamycin showed a much more subtle effect on global translation than did caffeine, while both drugs were effective in prolonging chronological lifespan. Rapamycin and caffeine did not affect the lifespan via the pH of the growth media. Rapamycin prolonged the lifespan of nongrowing cells only when applied during the growth phase but not when applied after cells had stopped proliferation. The doses of rapamycin and caffeine strongly correlated with growth inhibition and with lifespan extension. This comprehensive analysis will inform future studies into TORC1 function and cellular aging in fission yeast and beyond.","doi":"10.1111/acel.12080","authors":"Rallis C, Codlin S, Bähler J","authors_abbrev":"Rallis C et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-04-05","publication_year":"2013","canto_session_key":"02ba9b750a49128f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Charalampos Rallis","canto_first_approved_date":"2014-02-25 10:33:33","canto_approved_date":"2025-05-28 22:27:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-07 14:01:54","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Charalampos Rallis","community_curator":true,"annotation_count":9,"orcid":"0000-0002-4390-0266","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC162.12","SPBC106.10","SPBC30D10.10c","SPBC839.17c","SPCC24B10.07"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-02-25"},{"uniquename":"PMID:27555098","title":"The amino-terminal hydrophilic region of the vacuolar transporter Avt3p is dispensable for the vacuolar amino acid compartmentalization of Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2016 Dec;80(12):2291-2297","abstract":"Avt3p, a vacuolar amino acid exporter (656 amino acid residues) that is important for vacuolar amino acid compartmentalization as well as spore formation in Schizosaccharomyces pombe, has an extremely long hydrophilic region (approximately 290 amino acid residues) at its N-terminus. Because known functional domains have not been found in this region, its functional role was examined with a deletion mutant avt3 (∆1-270)  expressed in S. pombe avt3∆ cells. The deletion of this region did not affect its intracellular localization or vacuolar contents of basic amino acids as well as neutral ones. The defect of avt3Δ cells in spore formation was rescued by the expression of avt3 +  but was not completely rescued by the expression of avt3 (∆1-270) . The N-terminal region is thus dispensable for the function of Avt3p as an amino acid exporter, but it is likely to be involved in the role of Avt3p under nutritional starvation conditions.","authors":"Kawano-Kawada M, Chardwiriyapreecha S, Manabe K, Sekito T, Akiyama K, Takegawa K, Kakinuma Y","authors_abbrev":"Kawano-Kawada M et al.","pubmed_publication_date":"Dec 2016","pubmed_entrez_date":"2016-08-25","publication_year":"2016","canto_session_key":"80cc37348b1dba98","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-08-26 00:16:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27194449","title":"A rationally engineered yeast pyruvyltransferase Pvg1p introduces sialylation-like properties in neo-human-type complex oligosaccharide.","citation":"Sci Rep 2016 May 19;6:26349","abstract":"Pyruvylation onto the terminus of oligosaccharide, widely seen from prokaryote to eukaryote, confers negative charges on the cell surface and seems to be functionally similar to sialylation, which is found at the end of human-type complex oligosaccharide. However, detailed molecular mechanisms underlying pyruvylation have not been clarified well. Here, we first determined the crystal structure of fission yeast pyruvyltransferase Pvg1p at a resolution of 2.46 Å. Subsequently, by combining molecular modeling with mutational analysis of active site residues, we obtained a Pvg1p mutant (Pvg1p(H168C)) that efficiently transferred pyruvyl moiety onto a human-type complex glycopeptide. The resultant pyruvylated human-type complex glycopeptide recognized similar lectins on lectin arrays as the α2,6-sialyl glycopeptides. This newly-generated pyruvylation of human-type complex oligosaccharides would provide a novel method for glyco-bioengineering.","doi":"10.1038/srep26349","authors":"Higuchi Y, Yoshinaga S, Yoritsune K, Tateno H, Hirabayashi J, Nakakita S, Kanekiyo M, Kakuta Y, Takegawa K","authors_abbrev":"Higuchi Y et al.","pubmed_publication_date":"19 May 2016","pubmed_entrez_date":"2016-05-20","publication_year":"2016","canto_session_key":"66d0d6609144ac64","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-07-01 16:18:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-01 16:17:46","canto_added_date":"2016-05-21 00:15:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8F11.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-07-01","pdb_entries":[{"pdb_id":"5ax7","gene_chains":[{"gene_uniquename":"SPAC8F11.10c","chain":"A/B","position":"54-401"}],"title":"yeast pyruvyltransferase Pvg1p","entry_authors":"Kanekiyo M,Yoritsune K,Yoshinaga S,Higuchi Y,Takegawa K,Kakuta Y","entry_authors_abbrev":"Kanekiyo M et al.","reference_uniquename":"PMID:27194449","experimental_method":"X-ray","resolution":"2.46"}]},{"uniquename":"PMID:22384373","title":"A Geographically Diverse Collection of Schizosaccharomyces pombe Isolates Shows Limited Phenotypic Variation but Extensive Karyotypic Diversity.","citation":"G3 (Bethesda) 2011 Dec;1(7):615-26","abstract":"The fission yeast Schizosaccharomyces pombe has been widely used to study eukaryotic cell biology, but almost all of this work has used derivatives of a single strain. We have studied 81 independent natural isolates and 3 designated laboratory strains of Schizosaccharomyces pombe. Schizosaccharomyces pombe varies significantly in size but shows only limited variation in proliferation in different environments compared with Saccharomyces cerevisiae. Nucleotide diversity, π, at a near neutral site, the central core of the centromere of chromosome II is approximately 0.7%. Approximately 20% of the isolates showed karyotypic rearrangements as detected by pulsed field gel electrophoresis and filter hybridization analysis. One translocation, found in 6 different isolates, including the type strain, has a geographically widespread distribution and a unique haplotype and may be a marker of an incipient speciation event. All of the other translocations are unique. Exploitation of this karyotypic diversity may cast new light on both the biology of telomeres and centromeres and on isolating mechanisms in single-celled eukaryotes.","doi":"10.1534/g3.111.001123","authors":"Brown WR, Liti G, Rosa C, James S, Roberts I, Robert V, Jolly N, Tang W, Baumann P, Green C, Schlegel K, Young J, Hirchaud F, Leek S, Thomas G, Blomberg A, Warringer J","authors_abbrev":"Brown WR et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2012-03-03","publication_year":"2011","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1779795","title":"Cadystins: small metal-binding peptides.","citation":"Methods Enzymol 1991;205:348-58","abstract":"","authors":"Hayashi Y, Isobe M, Mutoh N, Nakagawa CW, Kawabata M","authors_abbrev":"Hayashi Y et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1597422","title":"Mutant enrichment of Schizosaccharomyces pombe by inositol-less death.","citation":"J Bacteriol 1992 Jun;174(12):4078-85","abstract":"Enrichment procedures, such as those utilizing inositol-less death, have proven to be extremely powerful for increasing the efficiency of identification of spontaneous mutants in a variety of procaryotic and eucaryotic organisms. We characterized inositol-less death in several widely used strains of the inositol-requiring yeast Schizosaccharomyces pombe and determined conditions under which this phenomenon can be used to enrich for mutants. Conflicting reports in the literature on the effects of inositol starvation upon viability of S. pombe had cast doubt on the suitability of using inositol-less death in a mutant enrichment procedure for this organism. We determined that inositol-less death was strain dependent, with differences in viability of up to 5 orders of magnitude observed between the most-sensitive strain, 972, and the least-sensitive strain, SP837. Inositol-less death was also dependent upon the cell concentration at the time of initiation of starvation. While inositol-less death occurred at all four temperatures tested, the kinetics of death was slower at 16 degrees C than at 23, 30, or 37 degrees C. Inositol-less death was observed during growth in fermentable and nonfermentable carbon sources, although loss of viability in glycerol-ethanol was significantly slower than that in glucose, sucrose, or raffinose. The feasibility of exploiting inositol-less death to enrich for spontaneous mutants was demonstrated by the identification of amino acid auxotrophs, nucleotide auxotrophs, carbon source utilization mutants, and temperature-sensitive mutants. By varying starvation conditions, some mutants were recovered at frequencies as high as 5.7 x 10(-2), orders of magnitude higher than the spontaneous mutation rate.","authors":"Minskoff SA, Gaynor PM, Greenberg ML","authors_abbrev":"Minskoff SA et al.","pubmed_publication_date":"Jun 1992","pubmed_entrez_date":"1992-06-01","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25712096","title":"Structural plasticity of Cid1 provides a basis for its distributive RNA terminal uridylyl transferase activity.","citation":"Nucleic Acids Res 2015 Mar 11;43(5):2968-79","abstract":"Terminal uridylyl transferases (TUTs) are responsible for the post-transcriptional addition of uridyl residues to RNA 3' ends, leading in some cases to altered stability. The Schizosaccharomyces pombe TUT Cid1 is a model enzyme that has been characterized structurally at moderate resolution and provides insights into the larger and more complex mammalian TUTs, ZCCHC6 and ZCCHC11. Here, we report a higher resolution (1.74 Å) crystal structure of Cid1 that provides detailed evidence for uracil selection via the dynamic flipping of a single histidine residue. We also describe a novel closed conformation of the enzyme that may represent an intermediate stage in a proposed product ejection mechanism. The structural insights gained, combined with normal mode analysis and biochemical studies, demonstrate that the plasticity of Cid1, particularly about a hinge region (N164-N165), is essential for catalytic activity, and provide an explanation for its distributive uridylyl transferase activity. We propose a model clarifying observed differences between the in vitro apparently processive activity and in vivo distributive monouridylylation activity of Cid1. We suggest that modulating the flexibility of such enzymes-for example by the binding of protein co-factors-may allow them alternatively to add single or multiple uridyl residues to the 3' termini of RNA molecules.","doi":"10.1093/nar/gkv122","authors":"Yates LA, Durrant BP, Fleurdépine S, Harlos K, Norbury CJ, Gilbert RJ","authors_abbrev":"Yates LA et al.","pubmed_publication_date":"11 Mar 2015","pubmed_entrez_date":"2015-02-26","publication_year":"2015","canto_session_key":"ce72b923bb5a139e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-27 16:40:55","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-27 16:40:48","canto_added_date":"2015-02-27 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19D5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-03-27","pdb_entries":[{"pdb_id":"4ud4","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A/B","position":"40-405"}],"title":"Structural Plasticity of Cid1 Provides a Basis for its RNA Terminal Uridylyl Transferase Activity","entry_authors":"Yates LA,Durrant BP,Fleurdepine S,Harlos K,Norbury CJ,Gilbert RJC","entry_authors_abbrev":"Yates LA et al.","reference_uniquename":"PMID:25712096","experimental_method":"X-ray","resolution":"1.74"},{"pdb_id":"4ud5","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A/B","position":"40-405"}],"title":"Structural Plasticity of Cid1 Provides a Basis for its RNA Terminal Uridylyl Transferase Activity","entry_authors":"Yates LA,Durrant BP,Fleurdepine S,Harlos K,Norbury CJ,Gilbert RJC","entry_authors_abbrev":"Yates LA et al.","reference_uniquename":"PMID:25712096","experimental_method":"X-ray","resolution":"2.52"}]},{"uniquename":"PMID:28679703","title":"Spore Analysis and Tetrad Dissection of  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2017 Jul 05;2017(7):pdb.prot091710","abstract":"Here we describe the processing of  Schizosaccharomyces pombe  spores in batches (random spore analysis) or through tetrad dissections. Spores are usually prepared from matings between haploid strains (producing zygotic asci) or from sporulating diploids (producing azygotic asci). In random spore analysis, a snail enzyme preparation is used to digest the walls of asci to release free spores that are diluted and plated to form colonies. In tetrad dissection, a needle attached to a micromanipulator is used to pick asci and separate spores. Tetrad dissection has traditionally been the method of choice for genetic mapping and is very useful in the study of genetic interactions (e.g., suppressor analysis). It is also the preferred method for routine crosses because it ensures that every colony stems from a single spore. This can never be certain in random spore analysis.","doi":"10.1101/pdb.prot091710","authors":"Ekwall K, Thon G","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"05 Jul 2017","pubmed_entrez_date":"2017-07-07","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-08 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17382883","title":"Identification of a targeting factor for posttranslational membrane protein insertion into the ER.","citation":"Cell 2007 Mar 23;128(6):1147-59","abstract":"Hundreds of proteins are anchored in intracellular membranes by a single transmembrane domain (TMD) close to the C terminus. Although these tail-anchored (TA) proteins serve numerous essential roles in cells, components of their targeting and insertion pathways have long remained elusive. Here we reveal a cytosolic TMD recognition complex (TRC) that targets TA proteins for insertion into the ER membrane. The highly conserved, 40 kDa ATPase subunit of TRC (which we termed TRC40) was identified as Asna-1. TRC40/Asna-1 interacts posttranslationally with TA proteins in a TMD-dependent manner for delivery to a proteinaceous receptor at the ER membrane. Subsequent release from TRC40/Asna-1 and insertion into the membrane depends on ATP hydrolysis. Consequently, an ATPase-deficient mutant of TRC40/Asna-1 dominantly inhibited TA protein insertion selectively without influencing other translocation pathways. Thus, TRC40/Asna-1 represents an integral component of a posttranslational pathway of membrane protein insertion whose targeting is mediated by TRC.","authors":"Stefanovic S, Hegde RS","authors_abbrev":"Stefanovic S et al.","pubmed_publication_date":"23 Mar 2007","pubmed_entrez_date":"2007-03-27","publication_year":"2007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1142.06"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37108917","title":" Amesia hispanica  sp. nov., Producer of the Antifungal Class of Antibiotics Dactylfungins.","citation":"J Fungi (Basel) 2023 Apr 12;9(4)","abstract":"During a study of the diversity of soilborne fungi from Spain, a strain belonging to the family Chaetomiaceae (Sordariales) was isolated. The multigene phylogenetic inference using five DNA loci showed that this strain represents an undescribed species of the genus  Amesia , herein introduced as  A. hispanica  sp. nov. Investigation of its secondary metabolome led to the isolation of two new derivatives ( 2  and  3 ) of the known antifungal antibiotic dactylfungin A ( 1 ), together with the known compound cochliodinol ( 4 ). The planar structures of  1 - 4  were determined by ultrahigh performance liquid chromatography coupled with diode array detection and ion mobility tandem mass spectrometry (UHPLC-DAD-IM-MS/MS) and extensive 1D and 2D nuclear magnetic resonance (NMR) spectroscopy after isolation by HPLC. All isolated secondary metabolites were tested for their antimicrobial and cytotoxic activities. Dactylfungin A ( 1 ) showed selective and strong antifungal activity against some of the tested human pathogens ( Aspergillus fumigatus  and  Cryptococcus neoformans ). The additional hydroxyl group in  2  resulted in the loss of activity against  C. neoformans  but still retained the inhibition of  As. fumigatus  in a lower concentration than that of the respective control, without showing any cytotoxic effects. In contrast, 25″-dehydroxy-dactylfungin A ( 3 ) exhibited improved activity against yeasts ( Schizosaccharomyces pombe  and  Rhodotorula glutinis ) than  1  and  2 , but resulted in the appearance of slight cytotoxicity. The present study exemplifies how even in a well-studied taxonomic group such as the Chaetomiaceae, the investigation of novel taxa still brings chemistry novelty, as demonstrated in this first report of this antibiotic class for chaetomiaceous and sordarialean taxa.","doi":"10.3390/jof9040463","authors":"Charria-Girón E, Stchigel AM, Čmoková A, Kolařík M, Surup F, Marin-Felix Y","authors_abbrev":"Charria-Girón E et al.","pubmed_publication_date":"12 Apr 2023","pubmed_entrez_date":"2023-04-28","publication_year":"2023","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2023-04-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3481018","title":"Mapping of the ras1 gene of Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1987 Oct;209(3):627-9","abstract":"The ras1 gene, an oncogene homologue, is known to be essential for recognition of the mating pheromone and hence for conjugation but not for vegetative growth in Schizosaccharomyces pombe. To facilitate further characterization and genetic manipulation of this gene, we have mapped it by using S. pombe strains which carry the Saccharomyces cerevisiae LEU2 gene inserted next to ras1 on the chromosome. Crosses with tester strains revealed that ras1 is tightly linked to pro2 on chromosome I. Furthermore, we have shown that ras1 is allelic with ste5, one of the sterility genes described by O. Girgsdies. The map position previously reported for ste5 eventually turned out to be false.","authors":"Lund PM, Hasegawa Y, Kitamura K, Shimoda C, Fukui Y, Yamamoto M","authors_abbrev":"Lund PM et al.","pubmed_publication_date":"Oct 1987","pubmed_entrez_date":"1987-10-01","publication_year":"1987","canto_session_key":"a9dcefd5cf94c7fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-04-28 23:34:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-31 12:12:39","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-31"},{"uniquename":"PMID:15007098","title":"Eukaryotic MCM proteins: beyond replication initiation.","citation":"Microbiol Mol Biol Rev 2004 Mar;68(1):109-31","abstract":"The minichromosome maintenance (or MCM) protein family is composed of six related proteins that are conserved in all eukaryotes. They were first identified by genetic screens in yeast and subsequently analyzed in other experimental systems using molecular and biochemical methods. Early data led to the identification of MCMs as central players in the initiation of DNA replication. More recent studies have shown that MCM proteins also function in replication elongation, probably as a DNA helicase. This is consistent with structural analysis showing that the proteins interact together in a heterohexameric ring. However, MCMs are strikingly abundant and far exceed the stoichiometry of replication origins; they are widely distributed on unreplicated chromatin. Analysis of mcm mutant phenotypes and interactions with other factors have now implicated the MCM proteins in other chromosome transactions including damage response, transcription, and chromatin structure. These experiments indicate that the MCMs are central players in many aspects of genome stability.","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-03-10","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:12:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10329722","title":"A novel nuclear export signal sensitive to oxidative stress in the fission yeast transcription factor Pap1.","citation":"J Biol Chem 1999 May 21;274(21):15151-8","abstract":"Pap1, a fission yeast AP-1-like transcription factor, is negatively regulated by CRM1/exportin 1, the nuclear export factor. Pap1 was localized normally in the cytoplasm but was accumulated in the nucleus when Crm1 was inactivated by a temperature-sensitive mutation or by treatment with leptomycin B, a specific export inhibitor. Deletion of the C-terminal cysteine-rich domain (CRD) resulted in nuclear accumulation of Pap1, while a glutathione S-transferase-green fluorescent protein-CRD fusion protein was localized in the cytoplasm in a Crm1-dependent manner. Deletion and mutational analyses identified several important amino acids in a 19-amino acid region in the CRD as a nuclear export signal (NES). Strikingly, a cysteine residue (Cys-532), in addition to two leucines and an isoleucine, was important for the NES function and the presence of at least one of the two cysteine residues was essential. Unlike classical NESs such as the human immunodeficiency virus Rev NES, the Pap1 NES lost the function upon treatment with oxidants such as diethyl maleate. The oxidative stress response is conserved through evolution, as green fluorescent protein-fused proteins bearing the Pap1 NES expressed in mammalian cells responded to diethyl maleate. These results show that the hydrophobic amino acid-rich region containing two important cysteines in Pap1 serves as a novel NES, which is sensitive to oxidative stress.","authors":"Kudo N, Taoka H, Toda T, Yoshida M, Horinouchi S","authors_abbrev":"Kudo N et al.","pubmed_publication_date":"21 May 1999","pubmed_entrez_date":"1999-05-18","publication_year":"1999","canto_session_key":"b8e0e1e996db9660","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-24 14:52:36","canto_approved_date":"2022-02-02 14:41:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-24 14:52:29","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.17","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-24"},{"uniquename":"PMID:8811082","title":"Molecular cloning and functional analysis of a Schizosaccharomyces pombe homologue of Escherichia coli endonuclease III.","citation":"Nucleic Acids Res 1996 Sep 01;24(17):3307-12","abstract":"The Escherichia coli endonuclease III (Nth-Eco) protein is involved in the removal of damaged pyrimidine residues from DNA by base excision repair. It is an iron-sulphur enzyme possessing both DNA glycosylase and apurinic/apyrimidinic lyase activities. A database homology search identified an open reading frame in genomic sequences of Schizosaccharomyces pombe which encodes a protein highly similar to Nth-Eco. The gene has been subcloned in an expression vector and the protein purified to apparent homogeneity. The S.pombe Nth homologue (Nth-Spo) is a 40.2 kDa protein of 355 amino acids. Nth-Spo possesses glycosylase activity on different types of DNA substrates with pyrimidine damage, being able to release both urea and thymine glycol from double-stranded polymers. The eukaryotic protein removes urea more efficiently than the prokaryotic enzyme, whereas its efficiency in excising thymine glycol is lower. A nicking assay was used to show that the enzyme also exhibits an AP lyase activity on UV- and gamma-irradiated DNA substrates. These findings show that Nth protein is structurally and functionally conserved from bacteria to fission yeast.","authors":"Roldán-Arjona T, Anselmino C, Lindahl T","authors_abbrev":"Roldán-Arjona T et al.","pubmed_publication_date":"01 Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_session_key":"9598b4bb67597469","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-06 16:51:07","canto_approved_date":"2019-11-06 16:51:07","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-06 16:51:02","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC30D11.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-11-06"},{"uniquename":"PMID:9335279","title":"Rapamycin specifically interferes with the developmental response of fission yeast to starvation.","citation":"J Bacteriol 1997 Oct;179(20):6325-34","abstract":"Rapamycin is a microbial macrolide which belongs to a family of immunosuppressive drugs that suppress the immune system by blocking stages of signal transduction in T lymphocytes. In Saccharomyces cerevisiae cells, as in T lymphocytes, rapamycin inhibits growth and cells become arrested at the G1 stage of the cell cycle. Rapamycin is also an effective antifungal agent, affecting the growth of yeast and filamentous fungi. Unexpectedly, we observed that rapamycin has no apparent effect on the vegetative growth of Schizosaccharomyces pombe. Instead, the drug becomes effective only when cells experience starvation. Under such conditions, homothallic wild-type cells will normally mate and undergo sporulation. In the presence of rapamycin, this sexual development process is strongly inhibited and cells adopt an alternative physiological option and enter stationary phase. Rapamycin strongly inhibits sexual development of haploid cells prior to the stage of sexual conjugation. In contrast, the drug has only a slight inhibitory effect on the sporulation of diploid cells. A genetic approach was applied to identify the signal transduction pathway that is inhibited by rapamycin. The results indicate that either rapamycin did not suppress the derepression of sexual development of strains in which adenylate cyclase was deleted or the cyclic AMP-dependent protein kinase encoded by pka1 was mutated. Nor did rapamycin inhibit the unscheduled meiosis observed in pat1-114 mutants. Overexpression of ras1+, an essential gene for sexual development, did not rescue the sterility of rapamycin-treated cells. However, expression of the activated allele, ras1Val17, antagonized the effect of rapamycin and restored the ability of the cells to respond to mating signals in the presence of the drug. We discuss possible mechanisms for the inhibitory effect of rapamycin on sexual development in S. pombe.","authors":"Weisman R, Choder M, Koltin Y","authors_abbrev":"Weisman R et al.","pubmed_publication_date":"Oct 1997","pubmed_entrez_date":"1997-10-23","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16890530","title":"Asymmetric microtubule pushing forces in nuclear centering.","citation":"Curr Biol 2006 Aug 08;16(15):1544-50","abstract":"Dynamic properties of microtubules contribute to the establishment of spatial order within cells. In the fission yeast Schizosaccharomyces pombe, interphase cytoplasmic microtubules are organized into antiparallel bundles that attach to the nuclear envelope and are needed to position the nucleus at the geometric center of the cell. Here, we show that after the nucleus is displaced by cell centrifugation, these microtubule bundles efficiently push the nucleus back to the center. Asymmetry in microtubule number, length, and dynamics contributes to the generation of force responsible for this unidirectional movement. Notably, microtubules facing the distal cell tip are destabilized when the microtubules in the same bundle are pushing from the proximal cell tip. The CLIP-170-like protein tip1p and the microtubule-bundling protein ase1p are required for this asymmetric regulation of microtubule dynamics, indicating contributions of factors both at microtubule plus ends and within the microtubule bundle. Mutants in these factors are defective in nuclear movement. Thus, cells possess an efficient microtubule-based engine that produces and senses forces for centering the nucleus. These studies may provide insights into mechanisms of asymmetric microtubule behaviors and force sensing in other processes such as chromosome segregation and cell polarization.","authors":"Daga RR, Yonetani A, Chang F","authors_abbrev":"Daga RR et al.","pubmed_publication_date":"08 Aug 2006","pubmed_entrez_date":"2006-08-08","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17596513","title":"Geranylgeranyl diphosphate synthase in fission yeast is a heteromer of farnesyl diphosphate synthase (FPS), Fps1, and an FPS-like protein, Spo9, essential for sporulation.","citation":"Mol Biol Cell 2007 Sep;18(9):3568-81","abstract":"Both farnesyl diphosphate synthase (FPS) and geranylgeranyl diphosphate synthase (GGPS) are key enzymes in the synthesis of various isoprenoid-containing compounds and proteins. Here, we describe two novel Schizosaccharomyces pombe genes, fps1(+) and spo9(+), whose products are similar to FPS in primary structure, but whose functions differ from one another. Fps1 is essential for vegetative growth, whereas, a spo9 null mutant exhibits temperature-sensitive growth. Expression of fps1(+), but not spo9(+), suppresses the lethality of a Saccharomyces cerevisiae FPS-deficient mutant and also restores ubiquinone synthesis in an Escherichia coli ispA mutant, which lacks FPS activity, indicating that S. pombe Fps1 in fact functions as an FPS. In contrast to a typical FPS gene, no apparent GGPS homologues have been found in the S. pombe genome. Interestingly, although neither fps1(+) nor spo9(+) expression alone in E. coli confers clear GGPS activity, coexpression of both genes induces such activity. Moreover, the GGPS activity is significantly reduced in the spo9 mutant. In addition, the spo9 mutation perturbs the membrane association of a geranylgeranylated protein, but not that of a farnesylated protein. Yeast two-hybrid and coimmunoprecipitation analyses indicate that Fps1 and Spo9 physically interact. Thus, neither Fps1 nor Spo9 alone functions as a GGPS, but the two proteins together form a complex with GGPS activity. Because spo9 was originally identified as a sporulation-deficient mutant, we show here that expansion of the forespore membrane is severely inhibited in spo9Delta cells. Electron microscopy revealed significant accumulation membrane vesicles in spo9Delta cells. We suggest that lack of GGPS activity in a spo9 mutant results in impaired protein prenylation in certain proteins responsible for secretory function, thereby inhibiting forespore membrane formation.","authors":"Ye Y, Fujii M, Hirata A, Kawamukai M, Shimoda C, Nakamura T","authors_abbrev":"Ye Y et al.","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-06-29","publication_year":"2007","canto_session_key":"2e5593fd20311c48","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-08-04 13:02:03","canto_approved_date":"2026-06-13 13:41:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-04 13:01:58","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.16c","SPBC36.06c","SPAC6F12.13c","SPBC405.04c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2015-08-04"},{"uniquename":"PMID:10359668","title":"Interaction of mammalian neprilysin with binding protein and calnexin in Schizosaccharomyces pombe.","citation":"Biochem J 1999 Jun 15;340 ( Pt 3)(Pt 3):813-9","abstract":"Neutral endopeptidase (neprilysin or NEP, EC 3.4.24.11) is a zinc metallo-endopeptidase expressed in many eukaryotic cell types and displaying several important physiological roles. In the brain (and central nervous system), this enzyme is involved in the molecular mechanism of pain by its action in the degradation of enkephalin molecules. In the kidney, NEP is implicated in the degradation of regulatory factors involved in the control of arterial pressure, including atrial natriuretic peptide and bradykinin. In this study we assessed the potential of the fission yeast Schizosaccharomyces pombe to overproduce rabbit NEP and secreted NEP (sNEP, a soluble derivative of this integral membrane protein). Both recombinant NEP and sNEP were produced at high levels (5 mg/l) in this system. Enzymic studies revealed that these recombinant proteins were fully active and exhibit kinetic parameters similar to those of the bona fide enzyme. Immunofluorescence microscopy and enzymic assays demonstrated that recombinant NEP is correctly targeted to the cell membrane. Furthermore, co-immunoprecipitation studies showed that folding intermediates of NEP and sNEP, produced in S. pombe, interact in the endoplasmic reticulum (ER) with binding protein (BiP) and calnexin (Cnx1p). The amount of sNEP coprecipitated with both BiP and Cnx1p augmented when cells were subjected to various stresses causing the accumulation of unfolded proteins in the ER. The interactions of NEP with BiP and Cnx1p were, however, more refractive to the same stresses.","authors":"Beaulieu H, Elagöz A, Crine P, Rokeach LA","authors_abbrev":"Beaulieu H et al.","pubmed_publication_date":"15 Jun 1999","pubmed_entrez_date":"1999-06-09","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2172964","title":"Adenylyl cyclase is dispensable for vegetative cell growth in the fission yeast Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1990 Oct;87(20):7814-8","abstract":"Disruption of the cyr1 gene of Schizosaccharomyces pombe, which encodes adenylyl cyclase, did not confer lethality to fission yeast cells, although they grew 40% slower than wild-type strains in complete medium. These cells contained no measurable amount of cAMP and no adenylyl cyclase activity. When h+ and h- cyr1 disruptants were mixed, they underwent mating even in rich medium. Propagation of homothallic cyr1 disruptants was difficult, probably because such cells readily mate and produce asci and thus stop growing. A greater than 10-fold increase in the amount of cyr1 mRNA was observed when cloned cyr1+ was introduced into Sch. pombe cells on a multicopy plasmid. The total adenylyl cyclase activity was similarly high in these transformants. However, the level of intracellular cAMP was hardly affected. Evidence suggests that this was not due to increased phosphodiesterase activity. Thus, cAMP level in growing fission yeast cells appears to be regulated not by the amount of adenylyl cyclase protein but by a feedback mechanism at the enzyme level. The cAMP level fell by approximately 50% under nitrogen starvation, which triggers sexual development in Sch. pombe. We suggest that fission yeast controls the level of intracellular cAMP primarily to regulate sexual development rather than to drive or arrest the cell cycle.","authors":"Maeda T, Mochizuki N, Yamamoto M","authors_abbrev":"Maeda T et al.","pubmed_publication_date":"Oct 1990","pubmed_entrez_date":"1990-10-01","publication_year":"1990","canto_session_key":"fc07dc88b6ff742e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2013-02-05 16:30:05","canto_approved_date":"2021-04-16 15:55:07","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-02-05 16:27:35","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-05"},{"uniquename":"PMID:11972332","title":"Identification of histone H4-like TAF in Schizosaccharomyces pombe as a protein that interacts with WD repeat-containing TAF.","citation":"Nucleic Acids Res 2002 May 01;30(9):1952-8","abstract":"The general transcription factor TFIID consists of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). We previously identified two distinct WD repeat-containing TAFs, spTAF72 and spTAF73, in the fission yeast Schizosaccharomyces pombe. Here we report the identification of another S.pombe TAF, spTAF50, which is the S.pombe homolog of histone H4-like TAFs such as human TAF80, Drosophila TAF60 and Saccharomyces cerevisiae TAF60. spTAF50 was identified in a two-hybrid screen as a protein that interacts with the C-terminal WD repeat-containing region of spTAF72. Gene disruption revealed that spTAF50 is essential for cell viability. In vitro, spTAF50 bound to spTAF72 but less efficiently to spTAF73. In S.pombe cells, spTAF50 was detected as a protein with an apparent molecular mass of approximately 50 kDa. Immunoprecipitation experiments demonstrated that spTAF50 is present in both the TFIID and SAGA-like complexes as in the case of spTAF72. These results indicate that the C-terminal region of spTAF72, which largely consists of WD repeats, interacts with spTAF50 in the TFIID and SAGA-like complexes, suggesting a role for the WD repeat domain in the interaction between TAFs.","authors":"Mitsuzawa H, Ishihama A","authors_abbrev":"Mitsuzawa H et al.","pubmed_publication_date":"01 May 2002","pubmed_entrez_date":"2002-04-25","publication_year":"2002","canto_session_key":"5e17d086a1ce0097","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-03 18:04:13","canto_approved_date":"2023-07-03 18:04:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-03 18:02:51","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC15D4.14","SPCC5E4.03c","SPAC13F5.02c","SPAC29E6.08","SPAC2G11.14","SPCC16C4.18c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2023-07-03"},{"uniquename":"PMID:4664533","title":"Cell wall growth during the cell cycle of Schizosaccharomyces pombe.","citation":"Z Allg Mikrobiol 1972;12(8):673-84","abstract":"","authors":"Streiblová E, Wolf A","authors_abbrev":"Streiblová E et al.","pubmed_publication_date":"1972","pubmed_entrez_date":"1972-01-01","publication_year":"1972","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25015293","title":"Septin ring assembly is regulated by Spt20, a structural subunit of the SAGA complex.","citation":"J Cell Sci 2014 Sep 15;127(Pt 18):4024-36","abstract":"Accurate cell division requires the proper assembly of high-order septin structures. In fission yeast (Schizosaccharomyces pombe), Spn1-Spn4 are assembled into a primary septin ring at the division site, and the subsequent recruitment of Mid2 to the structure results in a stable septin ring. However, not much is known about the regulation of this key process. Here, we found that deletion of Spt20, a structural subunit of the Spt-Ada-Gcn5-acetyltransferase (SAGA) transcriptional activation complex, caused a severe cell separation defect. The defect was mainly due to impaired septin ring assembly, as 80% of spt20Δ cells lost septin rings at the division sites. Spt20 regulates septin ring assembly partially through the transcriptional activation of mid2(+). Spt20 also interacted with Spn2 and Mid2 in vitro and was associated with other components of the ring in vivo. Spt20 colocalized with the septin ring, but did not separate when the septin ring split. Importantly, Spt20 regulated the stability of the septin ring and was required for the recruitment of Mid2. The transcription-dependent and -independent roles of Spt20 in septin ring assembly highlight a multifaceted regulation of one process by a SAGA subunit.","doi":"10.1242/jcs.151910","authors":"Lei B, Zhou N, Guo Y, Zhao W, Tan YW, Yu Y, Lu H","authors_abbrev":"Lei B et al.","pubmed_publication_date":"15 Sep 2014","pubmed_entrez_date":"2014-07-13","publication_year":"2014","canto_session_key":"9fbdcdc0e32c2c2c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-02-20 16:52:09","canto_approved_date":"2025-12-10 10:07:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-29 01:38:45","canto_added_date":"2014-07-14 00:15:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":63,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F10.11","SPAC1952.05","SPBC16A3.01","SPAC13A11.04c","SPBC14C8.17c","SPAPYUG7.03c","SPAC6G10.12c","SPAC9G1.11c","SPAC821.06","SPAC14C4.09","SPBC25H2.11c","SPAC821.09","SPAC4D7.10c"],"gene_count":13,"ltp_gene_count":11,"approved_date":"2018-02-20"},{"uniquename":"PMID:17277801","title":"Tudor hooks up with DNA repair.","citation":"Nat Struct Mol Biol 2007 Feb;14(2):98-9","abstract":"","authors":"Corsini L, Sattler M","authors_abbrev":"Corsini L et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-02-06","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24954111","title":"Chromosomes rein back the spindle pole body during horsetail movement in fission yeast meiosis.","citation":"Cell Struct Funct 2014;39(2):93-100","abstract":"In meiosis, pairing and recombination of homologous chromosomes are crucial for the correct segregation of chromosomes, and substantial movements of chromosomes are required to achieve homolog pairing. During this process, it is known that telomeres cluster to form a bouquet arrangement of chromosomes. The fission yeast Schizosaccharomyces pombe provides a striking example of bouquet formation, after which the entire nucleus oscillates between the cell poles (these oscillations are generally called horsetail nuclear movements) while the telomeres remain clustered to the spindle pole body (SPB; a centrosome-equivalent structure in fungi) at the leading edge of the moving nucleus. S. pombe mutants defective in telomere clustering frequently form aberrant spindles, such as monopolar or nonpolar spindles, leading to missegregation of the chromosomes at the subsequent meiotic divisions. Here we demonstrate that such defects in meiotic spindle formation caused by loss of meiotic telomere clustering are rescued when nuclear movement is prevented. On the other hand, stopping nuclear movement does not rescue defects in telomere clustering, nor chromosome missgregation even in cells that have formed a bipolar spindle. These results suggest that movement of the SPB without attachment of telomeres leads to the formation of aberrant spindles, but that recovering bipolar spindles is not sufficient for rescue of chromosome missegregation in mutants lacking telomere clustering.","authors":"Chikashige Y, Yamane M, Okamasa K, Mori C, Fukuta N, Matsuda A, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-06-24","publication_year":"2014","canto_session_key":"d64f1fadd832246e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yuji Chikashige","canto_first_approved_date":"2018-02-09 12:40:15","canto_approved_date":"2018-02-09 12:40:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-29 05:26:58","canto_added_date":"2014-06-25 00:15:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yuji Chikashige","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.06c","SPAC1002.06c","SPAC1093.06c","SPBC2G2.12"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-02-09"},{"uniquename":"PMID:30476445","title":"The Smc5/6 Complex: New and Old Functions of the Enigmatic Long-Distance Relative.","citation":"Annu Rev Genet 2018 Nov 23;52:89-107","abstract":"Smc5 and Smc6, together with the kleisin Nse4, form the heart of the enigmatic and poorly understood Smc5/6 complex, which is frequently viewed as a cousin of cohesin and condensin with functions in DNA repair. As novel functions for cohesin and condensin complexes in the organization of long-range chromatin architecture have recently emerged, new unsuspected roles for Smc5/6 have also surfaced. Here, I aim to provide a comprehensive overview of our current knowledge of the Smc5/6 complex, including its long-established function in genome stability, its multiple roles in DNA repair, and its recently discovered connection to the transcription inhibition of hepatitis B virus genomes. In addition, I summarize new research that is beginning to tease out the molecular details of Smc5/6 structure and function, knowledge that will illuminate the nuclear activities of Smc5/6 in the stability and dynamics of eukaryotic genomes.","doi":"10.1146/annurev-genet-120417-031353","authors":"Aragón L","authors_abbrev":"Aragón L","pubmed_publication_date":"23 Nov 2018","pubmed_entrez_date":"2018-11-27","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-07-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33881756","title":"Screening and Purification of Natural Products from Actinomycetes that Induce a \"Rounded\" Morphological Phenotype in Fission Yeast.","citation":"Nat Prod Bioprospect 2021 Aug;11(4):431-445","abstract":"This study was designed to identify and investigate bioactive natural product compounds that alter the cellular shape of the fission yeast Schizosaccharomyces pombe and induce a \"rounded\" or \"small\" cellular morphological phenotype. Bioassays using a range of antifungal agents against a multidrug-sensitive fission yeast strain, SAK950 showed that many induced a \"rounded\" phenotype. We then investigated whether 46 of the actinomycete strains identified in our previous study as inducing a similar phenotype produced antifungal agents of similar classes. We show that five of the strains produced streptothricin and that 26 strains produced polyenes, including fungichromin, filipin and candicidin, the last of which was produced by 24 strains. A taxonomic study of the strains indicated that the majority of the candicidin only producers were Streptomyces hydrogenans and S. albidoflavus whilst those that additionally produced streptothricin were related to S. enissocaesilis. A follow-up study to investigate the natural products made by related strains indicated that they followed a similar pattern. The identification of several compounds from the actinomycete strains similar to the antifungal agents initially tested confirm the validity of an approach using the S. pombe morphological phenotype and actinomycete taxonomy as a predictive tool for natural product identification.","doi":"10.1007/s13659-021-00304-1","authors":"Lewis RA, Devi J, Green K, Li J, Hopkins A, Hayles J, Nurse P, Errington J, Allenby NEE","authors_abbrev":"Lewis RA et al.","pubmed_publication_date":"Aug 2021","pubmed_entrez_date":"2021-04-21","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-04-23 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18606828","title":"Schizosaccharomyces pombe Noc3 is essential for ribosome biogenesis and cell division but not DNA replication.","citation":"Eukaryot Cell 2008 Sep;7(9):1433-40","abstract":"The initiation of eukaryotic DNA replication is preceded by the assembly of prereplication complexes (pre-RCs) at chromosomal origins of DNA replication. Pre-RC assembly requires the essential DNA replication proteins ORC, Cdc6, and Cdt1 to load the MCM DNA helicase onto chromatin. Saccharomyces cerevisiae Noc3 (ScNoc3), an evolutionarily conserved protein originally implicated in 60S ribosomal subunit trafficking, has been proposed to be an essential regulator of DNA replication that plays a direct role during pre-RC formation in budding yeast. We have cloned Schizosaccharomyces pombe noc3(+) (Spnoc3(+)), the S. pombe homolog of the budding yeast ScNOC3 gene, and functionally characterized the requirement for the SpNoc3 protein during ribosome biogenesis, cell cycle progression, and DNA replication in fission yeast. We showed that fission yeast SpNoc3 is a functional homolog of budding yeast ScNoc3 that is essential for cell viability and ribosome biogenesis. We also showed that SpNoc3 is required for the normal completion of cell division in fission yeast. However, in contrast to the proposal that ScNoc3 plays an essential role during DNA replication in budding yeast, we demonstrated that fission yeast cells do enter and complete S phase in the absence of SpNoc3, suggesting that SpNoc3 is not essential for DNA replication in fission yeast.","doi":"10.1128/EC.00119-08","authors":"Houchens CR, Perreault A, Bachand F, Kelly TJ","authors_abbrev":"Houchens CR et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-07-09","publication_year":"2008","canto_session_key":"20c07bfb2824ebe6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-10 09:44:00","canto_approved_date":"2024-04-04 11:13:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-06-10 09:43:54","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-06-10"},{"uniquename":"PMID:2977067","title":"Dot-blot assays and their use as a direct antigen-binding method to screen monoclonal antibodies to 1,4-beta- and 1,3-beta-glucan synthases.","citation":"Anal Biochem 1988 Nov 01;174(2):662-5","abstract":"A rapid method has been developed to assay beta-glucan synthases spotted on a nitrocellulose sheet. The sensitivity of this method allows screening of hybridoma-making monoclonal antibodies in a direct antigen-binding assay by measurement of the activity of the enzymes retained by the antibodies previously fixed on nitrocellulose.","authors":"Nodet P, Grange J, Fevre M","authors_abbrev":"Nodet P et al.","pubmed_publication_date":"01 Nov 1988","pubmed_entrez_date":"1988-11-01","publication_year":"1988","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35058438","title":"A structural basis for the diverse linkage specificities within the ZUFSP deubiquitinase family.","citation":"Nat Commun 2022 Jan 20;13(1):401","abstract":"Eukaryotic deubiquitinases are important regulators of ubiquitin signaling and can be subdivided into several structurally distinct classes. The ZUFSP family, with ZUP1 as its sole human member, has a modular architecture with a core catalytic domain highly active against the ubiquitin-derived peptide RLRGG, but not against ubiquitin itself. Ubiquitin recognition is conferred by additional non-catalytic domains, making full-length ZUP1 active against long K63-linked chains. However, non-mammalian ZUFSP family members contain different ubiquitin-binding domains in their N-terminal regions, despite their high conservation within the catalytic domain. Here, by working with representative ZUFSP family members from insects, fungi and plants, we show that different N-terminal domains are associated with different linkage preferences. Biochemical and structural studies suggest that the acquisition of two family-specific proximal domains have changed the default K48 preference of the ZUFSP family to the K63 preference observed in ZUP1 and its insect homolog. Additional N-terminal zinc finger domains promote chain cleavage without changing linkage-specificity.","doi":"10.1038/s41467-022-28049-6","authors":"Hermanns T, Pichlo C, Baumann U, Hofmann K","authors_abbrev":"Hermanns T et al.","pubmed_publication_date":"20 Jan 2022","pubmed_entrez_date":"2022-01-21","publication_year":"2022","canto_session_key":"b2a1e8f079c67607","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-04-21 10:13:44","canto_approved_date":"2024-05-15 17:40:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-21 10:12:46","canto_added_date":"2022-02-17 01:15:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["HGNC:21224","SPAC25H1.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-04-21","pdb_entries":[{"pdb_id":"7oiy","gene_chains":[{"gene_uniquename":"SPAC25H1.04","chain":"A/B","position":"1-244"}],"title":"Crystal structure of the ZUFSP family member Mug105","entry_authors":"Pichlo C,Hermanns T,Hofmann K,Baumann U","entry_authors_abbrev":"Pichlo C et al.","reference_uniquename":"PMID:35058438","experimental_method":"X-ray","resolution":"2.05"}]},{"uniquename":"PMID:9878760","title":"The dolichol pathway of N-linked glycosylation.","citation":"Biochim Biophys Acta 1999 Jan 06;1426(2):239-57","abstract":"The oligosaccharide substrate for the N-linked protein glycosylation is assembled at the membrane of the endoplasmic reticulum. Dolichyl pyrophosphate serves as a carrier in this biosynthetic pathway. In this review, we discuss the function of the lipid carrier dolichol in oligosaccharide assembly and give an overview of the biosynthesis of the different sugar donors required for the building of the oligosaccharide. Yeast genetic techniques have made it possible to identify many different loci encoding specific glycosyltransferases required for the precise and ordered assembly of the dolichyl pyrophosphate-linked oligosaccharide. Based on the knowledge obtained from studying this pathway in yeast, we compare it to the process of N-linked protein glycosylation in archaea. We suggest that N-linked glycosylation in eukaryotes and in archaea share a common evolutionary origin.","authors":"Burda P, Aebi M","authors_abbrev":"Burda P et al.","pubmed_publication_date":"06 Jan 1999","pubmed_entrez_date":"1999-01-08","publication_year":"1999","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC7D4.06c","SPAC17C9.07","SPCC330.08","SPAC5D6.06c","SPBC11B10.01","SPBC1734.12c","SPAC56E4.02c","SPAC56F8.06c","SPBC342.01c","SPAC1834.05"],"gene_count":10,"ltp_gene_count":0},{"uniquename":"EMBL:SPC00707","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22050224","title":"S-Glucuronidation of 7-mercapto-4-methylcoumarin by human UDP glycosyltransferases in genetically engineered fission yeast cells.","citation":"Biol Chem 2011 Dec;392(12):1089-95","abstract":"Human UDP glycosyltransferases (UGTs) play an important role in xenobiotic detoxification. They increase the solubility of their substrates by adding a sugar moiety (such as glucuronic acid) to different functional entities (such as hydroxyl groups). The aim of this study was to investigate how glucuronidation of a standard substrate is affected by a change of the hetero-atom at the conjugation site. For this purpose, we compared the in vitro glucuronidation rates of 4-methylumbelliferone and 7-mercapto-4-methylcoumarin, respectively. Human liver microsomes catalyzed the S-glucuronidation of 7-mercapto-4--methylcoumarin almost as efficient as the O-glucuronidation of 4-methylumbelliferone. When testing isoenzyme specificity by whole cell biotransformation with fission yeast strains that recombinantly express all 19 human members of the UGT1 and UGT2 families, it was found that 13 isoenzymes were able to glucuronidate 7-mercapto-4-methylcoumarin, with five of them being specific for this substrate and the other eight also converting 4-methylumbelliferone under these conditions. The remaining six UGTs did not accept either substrate. Out of the eight isoenzymes that glucuronidated both substrates, four catalyzed both reactions approximately to the same extent, while three displayed higher conversion rates towards 4-methylumbelliferone and one preferred 7-mercapto-4-methylcoumarin. These data suggest that 7-mercapto-4-methylcoumarin is a convenient new standard substrate for monitoring S-glucuronidation.","doi":"10.1515/BC.2011.194","authors":"Buchheit D, Schmitt EI, Bischoff D, Ebner T, Bureik M","authors_abbrev":"Buchheit D et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-11-05","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7926829","title":"The Schizosaccharomyces pombe rad1 gene consists of three exons and the cDNA sequence is partially homologous to the Ustilago maydis REC1 cDNA.","citation":"Gene 1994 Oct 11;148(1):155-9","abstract":"We show that the rad1 gene of Schizosaccharomyces pombe is comprised of three exons and encodes a protein of 37 kDa. A cDNA clone containing these three exons complements the sensitivity of the rad1-1 mutant to ultraviolet and gamma-radiation and to hydroxyurea. The newly identified ORF of the rad1 gene was found to exhibit partial homology to the REC1 gene of Ustilago maydis. These two genes share putative functional similarities in their respective organisms.","authors":"Long KE, Sunnerhagen P, Subramani S","authors_abbrev":"Long KE et al.","pubmed_publication_date":"11 Oct 1994","pubmed_entrez_date":"1994-10-11","publication_year":"1994","canto_session_key":"f7994126dc65670a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-02-01 23:55:24","canto_approved_date":"2019-02-01 23:55:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-01 23:55:10","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-02-01"},{"uniquename":"PMID:29061993","title":"Live cell X-ray imaging of autophagic vacuoles formation and chromatin dynamics in fission yeast.","citation":"Sci Rep 2017 Oct 23;7(1):13775","abstract":"Seeing physiological processes at the nanoscale in living organisms without labeling is an ultimate goal in life sciences. Using X-ray ptychography, we explored in situ the dynamics of unstained, living fission yeast Schizosaccharomyces pombe cells in natural, aqueous environment at the nanoscale. In contrast to previous X-ray imaging studies on biological matter, in this work the eukaryotic cells were alive even after several ptychographic X-ray scans, which allowed us to visualize the chromatin motion as well as the autophagic cell death induced by the ionizing radiation. The accumulated radiation of the sequential scans allowed for the determination of a characteristic dose of autophagic vacuole formation and the lethal dose for fission yeast. The presented results demonstrate a practical method that opens another way of looking at living biological specimens and processes in a time-resolved label-free setting.","doi":"10.1038/s41598-017-13175-9","authors":"Strelnikova N, Sauter N, Guizar-Sicairos M, Göllner M, Diaz A, Delivani P, Chacón M, Tolić IM, Zaburdaev V, Pfohl T","authors_abbrev":"Strelnikova N et al.","pubmed_publication_date":"23 Oct 2017","pubmed_entrez_date":"2017-10-25","publication_year":"2017","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2017-10-26 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16085494","title":"PtdIns(4,5)P2 functions at the cleavage furrow during cytokinesis.","citation":"Curr Biol 2005 Aug 09;15(15):1407-12","abstract":"Phosphoinositides play important roles in regulating the cytoskeleton and vesicle trafficking, potentially important processes at the cleavage furrow. However, it remains unclear which, if any, of the phosphoinositides play a role during cytokinesis. A systematic analysis to determine if any of the phosphoinositides might be present or of functional importance at the cleavage furrow has not been published. Several studies hint at a possible role for one or more phosphoinositides at the cleavage furrow. The best of these are genetic data identifying mutations in phosphoinositide-modifying enzymes (a PtdIns(4)P-5-kinase in S. pombe and a PI-4-kinase in D. melanogaster) that interfere with cytokinesis. The genetic nature of these experiments leaves questions as to how direct may be their contribution to cytokinesis. Here we show that a single phosphoinositide, PtdIns(4,5)P2, specifically accumulates at the furrow. Interference with PtdIns(4,5)P2 interferes with adhesion of the plasma membrane to the contractile ring at the furrow. Finally, four distinct interventions to specifically interfere with PtdIns(4,5)P2 each impair cytokinesis. We conclude that PtdIns(4,5)P2 is present at the cleavage furrow and is required for normal cytokinesis at least in part because of a role in adhesion between the contractile ring and the plasma membrane.","authors":"Field SJ, Madson N, Kerr ML, Galbraith KA, Kennedy CE, Tahiliani M, Wilkins A, Cantley LC","authors_abbrev":"Field SJ et al.","pubmed_publication_date":"09 Aug 2005","pubmed_entrez_date":"2005-08-09","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31260531","title":"Gcn5-mediated acetylation at MBF-regulated promoters induces the G1/S transcriptional wave.","citation":"Nucleic Acids Res 2019 Sep 19;47(16):8439-8451","abstract":"In fission yeast, MBF-dependent transcription is inactivated at the end of S phase through a negative feedback loop that involves the co-repressors, Yox1 and Nrm1. Although this repression system is well known, the molecular mechanisms involved in MBF activation remain largely unknown. Compacted chromatin constitutes a barrier to activators accessing promoters. Here, we show that chromatin regulation plays a key role in activating MBF-dependent transcription. Gcn5, a part of the SAGA complex, binds to MBF-regulated promoters through the MBF co-activator Rep2 in a cell cycle-dependent manner and in a reverse correlation to the binding of the MBF co-repressors, Nrm1 or Yox1. We propose that the co-repressors function as physical barriers to SAGA recruitment onto MBF promoters. We also show that Gcn5 acetylates specific lysine residues on histone H3 in a cell cycle-regulated manner. Furthermore, either in a gcn5 mutant or in a strain in which histone H3 is kept in an unacetylated form, MBF-dependent transcription is downregulated. In summary, Gcn5 is required for the full activation and correct timing of MBF-regulated gene transcription.","doi":"10.1093/nar/gkz561","authors":"González-Medina A, Hidalgo E, Ayté J","authors_abbrev":"González-Medina A et al.","pubmed_publication_date":"19 Sep 2019","pubmed_entrez_date":"2019-07-02","publication_year":"2019","canto_session_key":"3bc471528952a5da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alberto Gonzalez-Medina","canto_first_approved_date":"2020-01-08 14:49:25","canto_approved_date":"2022-01-15 09:59:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-01-01 22:09:21","canto_added_date":"2019-07-03 00:15:04","annotation_curators":[{"name":"Alberto Gonzalez-Medina","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPBC21B10.13c","SPAC1952.05","SPBC428.18","SPBC16A3.07c","SPBC342.06c","SPCC1259.13","SPAC1783.04c","SPAC17G8.13c","SPAC1F7.05","SPBC1105.11c","SPBC2F12.11c","SPAC17H9.19c","SPBC660.13c","SPAC1834.04","SPBC8D2.04","SPBP16F5.03c"],"gene_count":17,"ltp_gene_count":8,"approved_date":"2020-01-08"},{"uniquename":"PMID:36774373","title":"Mechanistic insights into RNA surveillance by the canonical poly(A) polymerase Pla1 of the MTREC complex.","citation":"Nat Commun 2023 Feb 11;14(1):772","abstract":"The S. pombe orthologue of the human PAXT connection, Mtl1-Red1 Core (MTREC), is an eleven-subunit complex that targets cryptic unstable transcripts (CUTs) to the nuclear RNA exosome for degradation. It encompasses the canonical poly(A) polymerase Pla1, responsible for polyadenylation of nascent RNA transcripts as part of the cleavage and polyadenylation factor (CPF/CPSF). In this study we identify and characterise the interaction between Pla1 and the MTREC complex core component Red1 and analyse the functional relevance of this interaction in vivo. Our crystal structure of the Pla1-Red1 complex shows that a 58-residue fragment in Red1 binds to the RNA recognition motif domain of Pla1 and tethers it to the MTREC complex. Structure-based Pla1-Red1 interaction mutations show that Pla1, as part of MTREC complex, hyper-adenylates CUTs for their efficient degradation. Interestingly, the Red1-Pla1 interaction is also required for the efficient assembly of the fission yeast facultative heterochromatic islands. Together, our data suggest a complex interplay between the RNA surveillance and 3'-end processing machineries.","doi":"10.1038/s41467-023-36402-6","authors":"Soni K, Sivadas A, Horvath A, Dobrev N, Hayashi R, Kiss L, Simon B, Wild K, Sinning I, Fischer T","authors_abbrev":"Soni K et al.","pubmed_publication_date":"11 Feb 2023","pubmed_entrez_date":"2023-02-11","publication_year":"2023","canto_session_key":"6995981c6f4c4090","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-02-13 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC646.04","SPAC1006.03c"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"7q73","gene_chains":[{"gene_uniquename":"SPBC646.04","chain":"A","position":"1-566"}],"title":"Structure of Pla1 apo","entry_authors":"Soni K,Wild K,Sinning I","entry_authors_abbrev":"Soni K et al.","reference_uniquename":"PMID:36774373","experimental_method":"X-ray","resolution":"1.9"},{"pdb_id":"7q72","gene_chains":[{"gene_uniquename":"SPBC646.04","chain":"A/B","position":"1-566"},{"gene_uniquename":"SPAC1006.03c","chain":"C/D","position":"288-345"}],"title":"Structure of Pla1 in complex with Red1","entry_authors":"Soni K,Wild K,Sinning I","entry_authors_abbrev":"Soni K et al.","reference_uniquename":"PMID:36774373","experimental_method":"X-ray","resolution":"2.8"},{"pdb_id":"7q74","gene_chains":[{"gene_uniquename":"SPBC646.04","chain":"A/B","position":"1-542"}],"title":"Structure of Pla1 apo, with a C-terminal deletion","entry_authors":"Soni K,Wild K,Sinning I","entry_authors_abbrev":"Soni K et al.","reference_uniquename":"PMID:36774373","experimental_method":"X-ray","resolution":"2.599"}]},{"uniquename":"PMID:28273166","title":"Ste12/Fab1 phosphatidylinositol-3-phosphate 5-kinase is required for nitrogen-regulated mitotic commitment and cell size control.","citation":"PLoS One 2017;12(3):e0172740","abstract":"Tight coupling of cell growth and cell cycle progression enable cells to adjust their rate of division, and therefore size, to the demands of proliferation in varying nutritional environments. Nutrient stress promotes inhibition of Target Of Rapamycin Complex 1 (TORC1) activity. In fission yeast, reduced TORC1 activity advances mitotic onset and switches growth to a sustained proliferation at reduced cell size. A screen for mutants, that failed to advance mitosis upon nitrogen stress, identified a mutant in the PIKFYVE 1-phosphatidylinositol-3-phosphate 5-kinase fission yeast homolog Ste12. Ste12PIKFYVE deficient mutants were unable to advance the cell cycle to reduce cell size after a nitrogen downshift to poor nitrogen (proline) growth conditions. While it is well established that PI(3,5)P2 signalling is required for autophagy and that Ste12PIKFYVE mutants have enlarged vacuoles (yeast lysosomes), neither a block to autophagy or mutants that independently have enlarged vacuoles had any impact upon nitrogen control of mitotic commitment. The addition of rapamycin to Ste12PIKFYVE deficient mutants reduced cell size at division to suggest that Ste12PIKFYVE possibly functions upstream of TORC1. ste12 mutants display increased Torin1 (TOR inhibitor) sensitivity. However, no major impact on TORC1 or TORC2 activity was observed in the ste12 deficient mutants. In summary, Ste12PIKFYVE is required for nitrogen-stress mediated advancement of mitosis to reduce cell size at division.","doi":"10.1371/journal.pone.0172740","authors":"Cobley D, Hálová L, Schauries M, Kaczmarek A, Franz-Wachtel M, Du W, Krug K, Maček B, Petersen J","authors_abbrev":"Cobley D et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-03-09","publication_year":"2017","canto_session_key":"8e7208f625e25c0f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-10 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23103209","title":"End-binding proteins and Ase1/PRC1 define local functionality of structurally distinct parts of the microtubule cytoskeleton.","citation":"Trends Cell Biol 2013 Feb;23(2):54-63","abstract":"The microtubule cytoskeleton is crucial for the intracellular organization of eukaryotic cells. It is a dynamic scaffold that has to perform a variety of very different functions. This multitasking is achieved through the activity of numerous microtubule-associated proteins. Two prominent classes of proteins are central to the selective recognition of distinct transiently existing structural features of the microtubule cytoskeleton. They define local functionality through tightly regulated protein recruitment. Here we summarize the recent developments in elucidating the molecular mechanism underlying the action of microtubule end-binding proteins (EBs) and antiparallel microtubule crosslinkers of the Ase1/PRC1 family that represent the core of these two recruitment modules. Despite their fundamentally different activities, these conserved families share several common features.","doi":"10.1016/j.tcb.2012.10.003","authors":"Duellberg C, Fourniol FJ, Maurer SP, Roostalu J, Surrey T","authors_abbrev":"Duellberg C et al.","pubmed_publication_date":"Feb 2013","pubmed_entrez_date":"2012-10-30","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17651922","title":"Identification of novel suppressors for Mog1 implies its involvement in RNA metabolism, lipid metabolism and signal transduction.","citation":"Gene 2007 Oct 01;400(1-2):114-21","abstract":"Mog1 is conserved from yeast to mammal, but its function is obscure. We isolated yeast genes that rescued a temperature-sensitive death of S. cerevisiae Scmog1Delta, and of S. pombe Spmog1(ts). Scmog1Delta was rescued by Opi3p, a phospholipid N-methyltransferase, in addition to S. cerevisiae Ran-homologue Gsp1p, and a RanGDP binding protein Ntf2p. On the other hand, Spmog1(ts) was rescued by Cid13 that is a poly (A) polymerase specific for suc22(+) mRNA encoding a subunit of ribonucleotide reductase, Ssp1 that is a protein kinase involved in stress response pathway, and Crp79 that is required for mRNA export, in addition to Spi1, S. pombe Ran-homologue, and Nxt2, S. pombe homologue of Ntf2p. Consistent with the identification of those suppressors, lack of ScMog1p dislocates Opi3p from the nuclear membrane and all of Spmog1(ts) showed the nuclear accumulation of mRNA. Furthermore, SpMog1 was co-precipitated with Nxt2 and Cid13.","authors":"Oki M, Ma L, Wang Y, Hatanaka A, Miyazato C, Tatebayashi K, Nishitani H, Uchida H, Nishimoto T","authors_abbrev":"Oki M et al.","pubmed_publication_date":"01 Oct 2007","pubmed_entrez_date":"2007-07-27","publication_year":"2007","canto_session_key":"82089b771a013b06","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-23 14:36:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-02-23 14:36:27","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.01c","SPBC1289.03c","SPAC1610.03c","SPCC297.03","SPAC15F9.03c","SPBC354.10","SPAC821.04c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-02-23"},{"uniquename":"PMID:15489526","title":"The meiotic recombination hot spot ura4A in Schizosaccharomyces pombe.","citation":"Genetics 2005 Feb;169(2):551-61","abstract":"The meiotic recombination hot spot ura4A (formerly ura4-aim) of Schizosaccharomyces pombe was observed at the insertion of the ura4+ gene 15 kb centromere-proximal to ade6 on chromosome III. Crosses heterozygous for the insertion showed frequent conversion at the heterology with preferential loss of the insertion. This report concerns the characterization of 12 spontaneous ura4A mutants. A gradient of conversion ranging from 18% at the 5' end to 6% at the 3' end was detected. A novel phenomenon also was discovered: a mating-type-related bias of conversion. The allele entering with the h+ parent acts preferentially as the acceptor for conversion (ratio of 3:2). Tetrad analysis of two-factor crosses showed that heteroduplex DNA is predominantly asymmetrical, enters from the 5' end, and more often than not covers the entire gene. Restoration repair of markers at the 5' end was inferred. Random spore analyses of two-factor crosses and normalization of prototroph-recombinant frequencies to physical distance led to the demonstration of map expansion: Crosses involving distant markers yielded recombinant frequencies higher than the sum of the frequencies measured in the subintervals. Finally, marker effects on recombination were defined for two of the ura4A mutations.","authors":"Baur M, Hartsuiker E, Lehmann E, Ludin K, Munz P, Kohli J","authors_abbrev":"Baur M et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2004-10-19","publication_year":"2005","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011330","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32179107","title":"Pattern formation in a coupled membrane-bulk reaction-diffusion model for intracellular polarization and oscillations.","citation":"J Theor Biol 2020 Jul 21;497:110242","abstract":"Reaction-diffusion systems have been widely used to study spatio-temporal phenomena in cell biology, such as cell polarization. Coupled bulk-surface models naturally include compartmentalization of cytosolic and membrane-bound polarity molecules. Here we study the distribution of the polarity protein Cdc42 in a mass-conserved membrane-bulk model, and explore the effects of diffusion and spatial dimensionality on spatio-temporal pattern formation. We first analyze a one-dimensional (1-D) model for Cdc42 oscillations in fission yeast, consisting of two diffusion equations in the bulk domain coupled to nonlinear ODEs for binding kinetics at each end of the cell. In 1-D, our analysis reveals the existence of symmetric and asymmetric steady states, as well as anti-phase relaxation oscillations typical of slow-fast systems. We then extend our analysis to a two-dimensional (2-D) model with circular bulk geometry, for which species can either diffuse inside the cell or become bound to the membrane and undergo a nonlinear reaction-diffusion process. We also consider a nonlocal system of PDEs approximating the dynamics of the 2-D membrane-bulk model in the limit of fast bulk diffusion. In all three model variants we find that mass conservation selects perturbations of spatial modes that simply redistribute mass. In 1-D, only anti-phase oscillations between the two ends of the cell can occur, and in-phase oscillations are excluded. In higher dimensions, no radially symmetric oscillations are observed. Instead, the only instabilities are symmetry-breaking, either corresponding to stationary Turing instabilities, leading to the formation of stationary patterns, or to oscillatory Turing instabilities, leading to traveling and standing waves. Codimension-two Bogdanov-Takens bifurcations occur when the two distinct instabilities coincide, causing traveling waves to slow down and to eventually become stationary patterns. Our work clarifies the effect of geometry and dimensionality on behaviors observed in mass-conserved cell polarity models.","doi":"10.1016/j.jtbi.2020.110242","authors":"Paquin-Lefebvre F, Xu B, DiPietro KL, Lindsay AE, Jilkine A","authors_abbrev":"Paquin-Lefebvre F et al.","pubmed_publication_date":"21 Jul 2020","pubmed_entrez_date":"2020-03-18","publication_year":"2020","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2020-03-19 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:4006903","title":"Molecular cloning and sequence analysis of a ras gene from Schizosaccharomyces pombe.","citation":"EMBO J 1985 Mar;4(3):687-91","abstract":"We have cloned a ras gene homologue from fission yeast Schizosaccharomyces pombe and determined its nucleotide sequence. A putative coding sequence for 219 amino acids was found. The sequence contained one set of splicing signals: GTAAGT for a donor sequence, ACTAA for a unique sequence found in introns of yeast genes and TAG for an acceptor sequence, indicating the existence of an intron. The amino-terminal one third of the predicted S. pombe ras protein was nearly perfectly homologous and the next one third moderately homologous to those of mammalian ras proteins. The carboxy-terminal one third showed no homology but terminated with a short conserved sequence Cys-X-X-Z (X being a hydrophobic amino acid) as in other ras proteins. The result of Southern analysis of S. pombe DNA under nonstringent hybridization conditions using our clone as a probe indicated that no other closely related gene may be present in the S. pombe genome. The transcript of this gene could be detected by Northern analysis.","authors":"Fukui Y, Kaziro Y","authors_abbrev":"Fukui Y et al.","pubmed_publication_date":"Mar 1985","pubmed_entrez_date":"1985-03-01","publication_year":"1985","canto_session_key":"5bbefeb215da190b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:23:35","canto_approved_date":"2018-12-22 20:23:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 19:16:24","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:1297355","title":"Regulation of the G2-mitosis transition.","citation":"Biochem Cell Biol 1992;70(10-11):954-71","abstract":"The cell cycle is regulated by pathways composed of a dependent series of steps, by timers, and by checkpoint controls which ensure the completion of one event before the initiation of another. This review focuses on the regulation of the initiation of mitosis, with particular emphasis on the regulation of p34cdc2 activity at this point in the cell cycle. The review draws on data from various organisms, but strongly emphasizes the genetic framework as seen in the fission yeast Schizosaccharomyces pombe and the biology and biochemistry of maturation promoting factor in frog oocytes. An attempt is made to include all known genes and proteins where a link can be made to the initiation event. The nutritional size control and its major known controlling elements, the wee1/mik1 protein kinases, and cdc25 protein tyrosine phosphatase are considered in detail along with their regulation. In addition, the checkpoint control pathways which mediate G2 delay in response to failure of DNA replication or DNA damage are examined.","authors":"Feilotter H, Lingner C, Rowley R, Young PG","authors_abbrev":"Feilotter H et al.","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16618806","title":"Two-stage mechanism for activation of the DNA replication checkpoint kinase Cds1 in fission yeast.","citation":"Genes Dev 2006 Apr 15;20(8):990-1003","abstract":"The DNA replication checkpoint is a complex signal transduction pathway, present in all eukaryotic cells, that functions to maintain genomic integrity and cell viability when DNA replication is perturbed. In Schizosaccharomyces pombe the major effector of the replication checkpoint is the protein kinase Cds1. Activation of Cds1 is known to require the upstream kinase Rad3 and the mediator Mrc1, but the biochemical mechanism of activation is not well understood. We report that the replication checkpoint is activated in two stages. In the first stage, Mrc1 recruits Cds1 to stalled replication forks by interactions between the FHA domain of Cds1 and specific phosphorylated Rad3 consensus sites in Mrc1. Cds1 is then primed for activation by Rad3-dependent phosphorylation. In the second stage, primed Cds1 molecules dimerize via phospho-specific interactions mediated by the FHA domains and are activated by autophosphorylation. This two-stage activation mechanism for the replication checkpoint allows for rapid activation with a high signal-to-noise ratio.","authors":"Xu YJ, Davenport M, Kelly TJ","authors_abbrev":"Xu YJ et al.","pubmed_publication_date":"15 Apr 2006","pubmed_entrez_date":"2006-04-19","publication_year":"2006","canto_session_key":"459a6e9d469b1af5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-04-11 14:53:33","canto_approved_date":"2025-09-03 18:24:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-11 14:51:01","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":33,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":58,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_16618806_phaf.tsv"}],"genes":["SPCC18B5.11c","SPAP14E8.02","SPAC694.06c","SPCC1259.13","SPBC216.05","SPCC23B6.03c","SPBC336.12c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-04-11"},{"uniquename":"PMID:11781565","title":"Feedback regulation of the MBF transcription factor by cyclin Cig2.","citation":"Nat Cell Biol 2001 Dec;3(12):1043-50","abstract":"The Mlu1-binding factor (MBF) from the fission yeast Schizosaccharomyces pombe contains the proteins Res1p and Res2p and binds to the Mlu1 cell-cycle box (MCB) element in DNA, activating the transcription of genes required for S phase. We report here that the cell-cycle-regulated expression of the cyclin cig2 gene is dependent on MBF. Deletion of MCB elements in the cig2 promoter perturbed the expression not only of cig2 but also of other MBF-dependent genes, indicating that Cig2p could regulate MBF activity. Cig2p can bind to Res2p, promote the phosphorylation of Res1p and inhibit MBF-dependent gene transcription. Cig2p thus forms an autoregulating feedback-inhibition loop with MBF which is important for normal regulation of the cell cycle.","authors":"Ayté J, Schweitzer C, Zarzov P, Nurse P, DeCaprio JA","authors_abbrev":"Ayté J et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2002-01-10","publication_year":"2001","canto_session_key":"4fc60b01472378b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-09-05 13:46:20","canto_approved_date":"2024-04-05 07:28:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-04 09:31:22","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jacky Hayles","community_curator":true,"annotation_count":32,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPBC336.12c","SPBC725.16","SPBC11B10.09","SPBC14C8.07c","SPBC19C2.05","SPAC24H6.05","SPBC428.18","SPAC22F3.09c","SPAPB2B4.03","SPBC32F12.09"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2018-09-05"},{"uniquename":"PMID:27082518","title":"Roles of the TRAPP-II Complex and the Exocyst in Membrane Deposition during Fission Yeast Cytokinesis.","citation":"PLoS Biol 2016 Apr;14(4):e1002437","abstract":"The cleavage-furrow tip adjacent to the actomyosin contractile ring is believed to be the predominant site for plasma-membrane insertion through exocyst-tethered vesicles during cytokinesis. Here we found that most secretory vesicles are delivered by myosin-V on linear actin cables in fission yeast cytokinesis. Surprisingly, by tracking individual exocytic and endocytic events, we found that vesicles with new membrane are deposited to the cleavage furrow relatively evenly during contractile-ring constriction, but the rim of the cleavage furrow is the main site for endocytosis. Fusion of vesicles with the plasma membrane requires vesicle tethers. Our data suggest that the transport particle protein II (TRAPP-II) complex and Rab11 GTPase Ypt3 help to tether secretory vesicles or tubulovesicular structures along the cleavage furrow while the exocyst tethers vesicles at the rim of the division plane. We conclude that the exocyst and TRAPP-II complex have distinct localizations at the division site, but both are important for membrane expansion and exocytosis during cytokinesis.","doi":"10.1371/journal.pbio.1002437","authors":"Wang N, Lee IJ, Rask G, Wu JQ","authors_abbrev":"Wang N et al.","pubmed_publication_date":"Apr 2016","pubmed_entrez_date":"2016-04-16","publication_year":"2016","canto_session_key":"4f2995b7c74f1360","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jian-Qiu Wu","canto_first_approved_date":"2016-11-07 23:23:13","canto_approved_date":"2026-02-16 14:30:27","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-07-26 15:02:08","canto_added_date":"2016-04-17 00:15:19","annotation_curators":[{"name":"Jian-Qiu Wu","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1919.10c","SPCC895.05","SPCC825.03c","SPAC6G10.05c","SPAC18G6.03","SPBC106.20","SPBC19G7.05c","SPAC6G9.11","SPAC821.09","SPCC970.09"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2016-11-07"},{"uniquename":"EMBL:AU009650","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29699848","title":"Phosphorylation of Wat1, human Lst8 homolog is critical for the regulation of TORC2 -Gad8 dependent pathway in fission yeast Schizosacchromyces pombe.","citation":"Eur J Cell Biol 2018 May;97(4):300-307","abstract":"Mammalian Lst8 interacts with the kinase domain of mTOR and stabilizes its interaction with Raptor regulating cell growth through the mTOR-S6K1 signalling pathway. Fission yeast Wat1, an ortholog of mammalian Lst8 is also an essential component of TOR complex 1 (TORC1) and TOR Complex 2 (TORC2) that control protein kinases essential for metabolic pathways. Here, we show that in response to osmotic stress, the Wat1 protein undergoes hyper-phosphorylation at S116 position. Wat1 interacts with the C-terminal region of Tor1 that also contain kinase domain. Co-immunoprecipitation and molecular modelling studies suggest that Wat1-Tor1 interaction is stabilized by FATC domain of Tor1 protein present at the C-terminal region. We have also demonstrated a physical interaction of Wat1 with Gad8, an AGC family protein kinase that is dependent on phosphorylation of Wat1 at S116 residue. Wat1 phosphorylation is required for the maintenance of vacuolar integrity and sexual differentiation. Collectively, our study reveals Wat1 phosphorylation regulates Gad8 function in a manner dependent on Tor1 interaction.","doi":"10.1016/j.ejcb.2018.04.006","authors":"Ahamad N, Sharma T, Khan S, Siddiqi MI, Ahmed S","authors_abbrev":"Ahamad N et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-04-28","publication_year":"2018","canto_session_key":"0afd82c6e0085a3f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shakil Ahmed","canto_first_approved_date":"2019-04-03 17:39:47","canto_approved_date":"2025-05-27 13:11:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-07 07:17:23","canto_added_date":"2018-04-29 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Shakil Ahmed","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21B10.05c","SPBC30D10.10c","SPCC24B10.07"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-04-03"},{"uniquename":"PMID:8663290","title":"Heterologous complementation of a Rieske iron-sulfur protein-deficient Saccharomyces cerevisiae by the Rip1 gene of Schizosaccharomyces pombe.","citation":"J Biol Chem 1996 Jun 28;271(26):15341-5","abstract":"A cDNA carrying the Rip1 gene, which encodes the Rieske iron-sulfur protein of Schizosaccharomyces pombe, has been cloned by complementing the respiratory deficiency of a Saccharomyces cerevisiae strain in which the endogenous copy of the RIP1 gene has been deleted. The deduced amino acid sequences of the S. pombe and S. cerevisiae iron-sulfur proteins are 50% identical, with the highest region of identity being in the C termini of the proteins, where the 2Fe:2S cluster is bound. When expressed in the S. cerevisiae deletion strain, the S. pombe iron-sulfur protein restores 25-30% of the ubiquinol-cytochrome c reductase activity. The kinetics of cytochrome c reduction, the effects of inhibitors which act at defined sites in the cytochrome bc1 complex, and the optical properties of cytochrome b in membranes from the S. cerevisiae deletion strain complemented with S. pombe iron-sulfur protein indicate that the S. pombe protein interacts with cytochrome b to restore an apparently normal ubiquinol oxidase site, but that interaction between the iron-sulfur protein and cytochrome c1 is partially impaired. This is the first heterologous replacement of an electron transfer protein in a respiratory enzyme complex in S. cerevisiae.","authors":"di Rago JP, Bruel C, Graham LA, Slonimski P, Trumpower BL","authors_abbrev":"di Rago JP et al.","pubmed_publication_date":"28 Jun 1996","pubmed_entrez_date":"1996-06-28","publication_year":"1996","canto_session_key":"33532b8ce078a4a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-05-17 08:34:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-06-22 15:40:28","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16H5.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-06-22"},{"uniquename":"PMID:25801050","title":"An IPTG-inducible derivative of the fission yeast nmt promoter.","citation":"Yeast 2015 Jun;32(6):469-78","abstract":"We here describe an IPTG-inducible system that reveals that the lac repressor alone can function as a potent transmodulator to regulate gene expression in the fission yeast, Schizosaccharomyces pombe. This expression system is a derivative of the Sz. pombe nmt promoter, which normally is strongly repressed by thiamine. With appropriate positioning of a lac operator site (lacO) downstream of the TATA-box, we show that gene expression from a chimeric nmt::lacO promoter can be regulated by the lac repressor up to two orders of magnitude in response to IPTG. The chimeric nmt::lacO promoter is rapidly induced and when GFP is used as a reporter; almost full induction is achieved 40 min after the addition of IPTG. Like the wild-type nmt promoter, the chimeric nmt::lacO is repressed by thiamine. This allows expression in a short and defined window, e.g. the S-phase of a synchronized cell population, by first adding IPTG to turn on expression, followed by addition of thiamine to switch off expression.","doi":"10.1002/yea.3073","authors":"Kjaerulff S, Nielsen O","authors_abbrev":"Kjaerulff S et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-03-25","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-03-26 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36635051","title":"Silver nanoparticles elevate mutagenesis of eukaryotic genomes.","citation":"G3 (Bethesda) 2023 Mar 09;13(3)","abstract":"Metal nanoparticles, especially silver, have been used in various medical scenarios, due to their excellent antimicrobial effects. Recent studies have shown that AgNPs do not exert mutagenic effects on target bacteria, but the degree to which they compromise eukaryotic genomes remains unclear. To study this, we evaluated the mutagenic effects of AgNPs on the fission yeast Schizosaccharomyces pombe ATCC-16979, of which ∼23% genes are homologous to human ones, at single-nucleotide resolution, and whole-genome scale by running 283 mutation accumulation lines for ∼260,000 cell divisions in total. We also explored the action and mutagenesis mechanisms using differential gene-expression analysis based on RNAseq. Upon AgNPs treatment, the genomic base-substitution mutation rate of S. pombe at four-fold degenerate sites increased by 3.46×, and small indels were prone to occur in genomic regions that are not simple sequence repeats. The G:C → T:A transversion rate was also significantly increased, likely mostly from oxidative damage. Thus, in addition to their antimicrobial potency, AgNPs might pose slight genotoxicity threats to eukaryotic and possibly human genomes, though at a low magnitude.","doi":"10.1093/g3journal/jkad008","authors":"Wu K, Li H, Wang Y, Liu D, Li H, Zhang Y, Lynch M, Long H","authors_abbrev":"Wu K et al.","pubmed_publication_date":"09 Mar 2023","pubmed_entrez_date":"2023-01-12","publication_year":"2023","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2023-01-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38485050","title":"Fungal microtubule organizing centers are evolutionarily unstable structures.","citation":"Fungal Genet Biol 2024 Mar 12;:103885","abstract":"For most Eukaryotic species the requirements of cilia formation dictate the structure of microtubule organizing centers (MTOCs). In this study we find that loss of cilia corresponds to loss of evolutionary stability for fungal MTOCs. We used iterative search algorithms to identify proteins homologous to those found in saccharomyces cerevisiae, and schizosaccharomyces pombe MTOCs, and calculated site-specific rates of change for those proteins that were broadly phylogenetically distributed. Our results indicate that both the protein composition of MTOCs as well as the sequence of MTOC proteins are poorly conserved throughout the fungal kingdom. To begin to reconcile this rapid evolutionary change with the rigid structure and essential function of the s. cerevisiae MTOC we further analyzed how structural interfaces among proteins influence the rates of change for specific residues within a protein. We find that a more stable protein may stabilize portions of an interacting partner where the two proteins are in contact. In summary, while the protein composition and sequences of the MTOC may be rapidly changing the proteins within the structure have a stabilizing effect on one another. Further exploration of fungal MTOCs will expand our understanding of how changes in the functional needs of a cell have affected physical structures, proteomes, and protein sequences throughout fungal evolution.","doi":"10.1016/j.fgb.2024.103885","authors":"Grazzini A, Cavanaugh AM","authors_abbrev":"Grazzini A et al.","pubmed_publication_date":"12 Mar 2024","pubmed_entrez_date":"2024-03-14","publication_year":"2024","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2024-03-16 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9878790","title":"Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells.","citation":"Biochim Biophys Acta 1999 Jan 06;1426(2):287-95","abstract":"Proteins entering the secretory pathway may be glycosylated upon transfer of an oligosaccharide (Glc3Man9GlcNAc2) from a dolichol-P-P derivative to nascent polypeptide chains in the lumen of the endoplasmic reticulum (ER). Oligosaccharides are then deglucosylated by glucosidases I and II (GII). Also in the ER, glycoproteins acquire their final tertiary structures, and species that fail to fold properly are retained and eventually degraded in the proteasome. It has been proposed that in mammalian cells the monoglucosylated oligosaccharides generated either by partial deglucosylation of the transferred compound or by reglucosylation of glucose-free oligosaccharides by the UDP-Glc:glycoprotein glucosyltransferase (GT) are recognized by ER resident lectins (calnexin and/or calreticulin). GT is a sensor of glycoprotein conformation as it only glucosylates misfolded species. The lectin-monoglucosylated oligosaccharide interaction would retain glycoproteins in the ER until correctly folded, and also facilitate their acquisition of proper tertiary structures by preventing aggregation. GII would liberate glycoproteins from the calnexin/calreticulin anchor, but species not properly folded would be reglucosylated by GT, and so continue to be retained by the lectins. Only when the protein becomes properly folded would it cease to be retained by the lectins. This review presents evidence suggesting that a similar quality control mechanism of glycoprotein folding is operative in Schizosaccharomyces pombe and that the mechanism in Saccharomyces cerevisiae probably differs substantially from that occurring in mammalian and Sch. pombe cells.","authors":"Parodi AJ","authors_abbrev":"Parodi AJ","pubmed_publication_date":"06 Jan 1999","pubmed_entrez_date":"1999-01-08","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22639641","title":"Evolution of plant sucrose uptake transporters.","citation":"Front Plant Sci 2012;3:22","abstract":"In angiosperms, sucrose uptake transporters (SUTs) have important functions especially in vascular tissue. Here we explore the evolutionary origins of SUTs by analysis of angiosperm SUTs and homologous transporters in a vascular early land plant, Selaginella moellendorffii, and a non-vascular plant, the bryophyte Physcomitrella patens, the charophyte algae Chlorokybus atmosphyticus, several red algae and fission yeast, Schizosaccharomyces pombe. Plant SUTs cluster into three types by phylogenetic analysis. Previous studies using angiosperms had shown that types I and II are localized to the plasma membrane while type III SUTs are associated with vacuolar membrane. SUT homologs were not found in the chlorophyte algae Chlamydomonas reinhardtii and Volvox carterii. However, the characean algae Chlorokybus atmosphyticus contains a SUT homolog (CaSUT1) and phylogenetic analysis indicated that it is basal to all other streptophyte SUTs analyzed. SUTs are present in both red algae and S. pombe but they are less related to plant SUTs than CaSUT1. Both Selaginella and Physcomitrella encode type II and III SUTs suggesting that both plasma membrane and vacuolar sucrose transporter activities were present in early land plants. It is likely that SUT transporters are important for scavenging sucrose from the environment and intracellular compartments in charophyte and non-vascular plants. Type I SUTs were only found in eudicots and we conclude that they evolved from type III SUTs, possibly through loss of a vacuolar targeting sequence. Eudicots utilize type I SUTs for phloem (vascular tissue) loading while monocots use type II SUTs for phloem loading. We show that HvSUT1 from barley, a type II SUT, reverted the growth defect of the Arabidopsis atsuc2 (type I) mutant. This indicates that type I and II SUTs evolved similar (and interchangeable) phloem loading transporter capabilities independently.","doi":"10.3389/fpls.2012.00022","authors":"Reinders A, Sivitz AB, Ward JM","authors_abbrev":"Reinders A et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-05-29","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC01576","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23133674","title":"Identification of the functional domains of the telomere protein Rap1 in Schizosaccharomyces pombe.","citation":"PLoS One 2012;7(11):e49151","abstract":"The telomere at the end of a linear chromosome plays crucial roles in genome stability. In the fission yeast Schizosaccharomyces pombe, the Rap1 protein, one of the central players at the telomeres, associates with multiple proteins to regulate various telomere functions, such as the maintenance of telomere DNA length, telomere end protection, maintenance of telomere heterochromatin, and telomere clustering in meiosis. The molecular bases of the interactions between Rap1 and its partners, however, remain largely unknown. Here, we describe the identification of the interaction domains of Rap1 with its partners. The Bqt1/Bqt2 complex, which is required for normal meiotic progression, Poz1, which is required for telomere length control, and Taz1, which is required for the recruitment of Rap1 to telomeres, bind to distinct domains in the C-terminal half of Rap1. Intriguingly, analyses of a series of deletion mutants for rap1(+) have revealed that the long N-terminal region (1-456 a.a. [amino acids]) of Rap1 (full length: 693 a.a.) is not required for telomere DNA length control, telomere end protection, and telomere gene silencing, whereas the C-terminal region (457-693 a.a.) containing Poz1- and Taz1-binding domains plays important roles in those functions. Furthermore, the Bqt1/Bqt2- and Taz1-binding domains are essential for normal spore formation after meiosis. Our results suggest that the C-terminal half of Rap1 is critical for the primary telomere functions, whereas the N-terminal region containing the BRCT (BRCA1 C-terminus) and Myb domains, which are evolutionally conserved among the Rap1 family proteins, does not play a major role at the telomeres.","doi":"10.1371/journal.pone.0049151","authors":"Fujita I, Tanaka M, Kanoh J","authors_abbrev":"Fujita I et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-11-08","publication_year":"2012","canto_session_key":"cafc26135a141916","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-13 09:51:35","canto_approved_date":"2026-02-15 12:33:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-13 09:51:27","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.13c","SPBC1778.02","SPAC212.11","SPBC19C7.10","SPAC16A10.07c","SPAC1002.06c","SPBCPT2R1.08c","SPAC19G12.13c"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2017-11-13"},{"uniquename":"PMID:18533101","title":"[RNAi and the formation of heterochromatin in Schizosaccharomyces pombe.].","citation":"J Soc Biol 2007;201(4):401-10","abstract":"In the fission yeast Schizosaccharomyces pombe, formation of pericentromeric heterochromatin involves RNA interference (RNAi). Recent data indicate that two RNAi complexes, RITS (RNA-induced transcriptional silencing complex) and RDRC (RNA-directed RNA polymerase complex), their respective enzymatic activity, and RNA polymerase II are essential for RNAi-mediated heterochromatin formation. At the site where heterochromatin formation takes place, RNA polymerase II synthesizes an RNA that would serve as an RNA platform to recruit in a siRNA-dependent manner RITS and RDRC, and thereby initiate heterochromatin assembly. Once recruited, RITS and RDRC seem to also contribute to the processing of the RNA platform. Therefore, RNAi-driven heterochromatin assembly appears to take place through a dynamic process of RNA synthesis, RNA-dependant recruitment of RNAi complexes and RNA degradation that all occur in cis.","doi":"10.1051/jbio:2007901","authors":"Barral S, Vavasseur A, Verdel A","authors_abbrev":"Barral S et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2008-06-06","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7596819","title":"Site-specific cleavage of chromosomes in vitro through Cre-lox recombination.","citation":"Nucleic Acids Res 1995 Jun 11;23(11):1923-7","abstract":"Site-specific recombination systems are useful tools for chromosome engineering in vivo and site-specific DNA cleavage methods have applications in genome analysis and gene isolation. Here, we report a new method to fragment chromosomes in vitro using the Cre-lox site-specific recombination system. Two lox sites were targeted into the 5.7 Mb chromosomes I of Schizosaccharomyces pombe. In vitro recombination between chromosomal lox sites and exogenously provided lox oligonucleotides 'cleaved' the chromosome at the defined lox sequences. Site-specific cleavage of lox sites in the tobacco genome was also demonstrated. This recombination-based cleavage method provides a novel approach for structural and functional analyses of eukaryotic chromosomes as it allows direct isolation of chromosome regions that correspond to phenotypes revealed through Cre-lox mediated chromosome rearrangements in vivo. Moreover, recombination with end-labeled lox oligonucleotides would permit the specific end-labeling of chromosome segments to facilitate the long range mapping of chromosomes.","authors":"Qin M, Lee E, Zankel T, Ow DW","authors_abbrev":"Qin M et al.","pubmed_publication_date":"11 Jun 1995","pubmed_entrez_date":"1995-06-11","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28475613","title":"SUMO-targeted ubiquitin ligase activity can either suppress or promote genome instability, depending on the nature of the DNA lesion.","citation":"PLoS Genet 2017 May;13(5):e1006776","abstract":"The posttranslational modifiers SUMO and ubiquitin critically regulate the DNA damage response (DDR). Important crosstalk between these modifiers at DNA lesions is mediated by the SUMO-targeted ubiquitin ligase (STUbL), which ubiquitinates SUMO chains to generate SUMO-ubiquitin hybrids. These SUMO-ubiquitin hybrids attract DDR proteins able to bind both modifiers, and/or are degraded at the proteasome. Despite these insights, specific roles for SUMO chains and STUbL in the DDR remain poorly defined. Notably, fission yeast defective in SUMO chain formation exhibit near wild-type resistance to genotoxins and moreover, have a greatly reduced dependency on STUbL activity for DNA repair. Based on these and other data, we propose that a critical role of STUbL is to antagonize DDR-inhibitory SUMO chain formation at DNA lesions. In this regard, we identify a SUMO-binding Swi2/Snf2 translocase called Rrp2 (ScUls1) as a mediator of the DDR defects in STUbL mutant cells. Therefore, in support of our proposal, SUMO chains attract activities that can antagonize STUbL and other DNA repair factors. Finally, we find that Taz1TRF1/TRF2-deficiency triggers extensive telomeric poly-SUMOylation. In this setting STUbL, together with its cofactor Cdc48p97, actually promotes genomic instability caused by the aberrant processing of taz1Δ telomeres by DNA repair factors. In summary, depending on the nature of the initiating DNA lesion, STUbL activity can either be beneficial or harmful.","doi":"10.1371/journal.pgen.1006776","authors":"Nie M, Moser BA, Nakamura TM, Boddy MN","authors_abbrev":"Nie M et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2017-05-06","publication_year":"2017","canto_session_key":"5b3ca07af37ba633","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-05-08 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.09c","SPCP31B10.05","SPBC3D6.11c","SPAC16A10.07c","SPBC365.06","SPBC23E6.02","SPAC1805.04","SPAC1687.05"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:9774697","title":"Schizosaccharomyces pombe retrotransposon Tf2 mobilizes primarily through homologous cDNA recombination.","citation":"Mol Cell Biol 1998 Nov;18(11):6839-52","abstract":"The Tf2 retrotransposon, found in the fission yeast Schizosaccharomyces pombe, is nearly identical to its sister element, Tf1, in its reverse transcriptase-RNase H and integrase domains but is very divergent in the gag domain, the protease, the 5' untranslated region, and the U3 domain of the long terminal repeats. It has now been demonstrated that a neo-marked copy of Tf2 overexpressed from a heterologous promoter can mobilize into the S. pombe genome and produce true transposition events. However, the Tf2-neo mobilization frequency is 10- to 20-fold lower than that of Tf1-neo, and 70% of the Tf2-neo events are homologous recombination events generated independently of a functional Tf2 integrase. Thus, the Tf2 element is primarily dependent on homologous recombination with preexisting copies of Tf2 for its propagation. Finally, production of Tf2-neo proteins and cDNA was also analyzed; surprisingly, Tf2 was found to produce its reverse transcriptase as a single species in which it is fused to protease, unlike all other retroviruses and retrotransposons.","authors":"Hoff EF, Levin HL, Boeke JD","authors_abbrev":"Hoff EF et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1998-10-17","publication_year":"1998","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7499352","title":"Schizosaccharomyces pombe thiamine pyrophosphokinase is encoded by gene tnr3 and is a regulator of thiamine metabolism, phosphate metabolism, mating, and growth.","citation":"J Biol Chem 1995 Nov 24;270(47):28457-62","abstract":"The Schizosaccharomyces pombe gene tnr3 has been genetically defined as a negative regulator of genes involved in thiamine metabolism (Schweingruber, A. M., Frankhauser, H., Dlugonski, J., Steinmann-Loss, C., and Schweingruber, M. E. (1992) Genetics 130, 445-449). We have isolated and sequenced the gene and show that it codes for a putative protein of 569 amino acids which exhibits, in its carboxyl-terminal half, good homology to Saccharomyces cerevisiae thiamine pyrophosphokinase (TPK). tnr3 mutants have reduced levels of intracellular thiamine diphosphate, show impaired TPK activity, which is enhanced by introducing the tnr3 wild type gene on a plasmid, and can be complemented by the S. cerevisiae TPK-encoding gene TH180. These data strongly suggest that tnr3 encodes S. pombe TPK. We present evidence that TPK also acts as a negative regulator for gene pho1, which is derepressed when cells are starved for phosphate and show that in contrast to wild type cells, tnr3 mutants mate constitutively in response to thiamine, indicating that TPK is also involved in regulation of mating. Disruption of the tnr3 gene is lethal, and a tnr3 mutant expressing only residual TPK activity grows slowly and shows aberrant morphology.","authors":"Fankhauser H, Zurlinden A, Schweingruber AM, Edenharter E, Schweingruber ME","authors_abbrev":"Fankhauser H et al.","pubmed_publication_date":"24 Nov 1995","pubmed_entrez_date":"1995-11-24","publication_year":"1995","canto_session_key":"5cbe479087353d2f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-03-27 14:36:14","canto_approved_date":"2020-01-23 13:43:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-10 13:38:33","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPAC6F12.05c","SPBC428.03c","SPAC23H4.10c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2015-03-27"},{"uniquename":"PMID:25891897","title":"A single cyclin-CDK complex is sufficient for both mitotic and meiotic progression in fission yeast.","citation":"Nat Commun 2015 Apr 20;6:6871","abstract":"The dominant model for eukaryotic cell cycle control proposes that cell cycle progression is driven by a succession of CDK complexes with different substrate specificities. However, in fission yeast it has been shown that a single CDK complex generated by the fusion of the Cdc13 cyclin with the CDK protein Cdc2 can drive the mitotic cell cycle. Meiosis is a modified cell cycle programme in which a single S-phase is followed by two consecutive rounds of chromosome segregation. Here we systematically analyse the requirements of the different fission yeast cyclins for meiotic cell cycle progression. We also show that a single Cdc13-Cdc2 complex, in the absence of the other cyclins, can drive the meiotic cell cycle. We propose that qualitatively different CDK complexes are not absolutely required for cell cycle progression either during mitosis or meiosis, and that a single CDK complex can drive both cell cycle programmes.","doi":"10.1038/ncomms7871","authors":"Gutiérrez-Escribano P, Nurse P","authors_abbrev":"Gutiérrez-Escribano P et al.","pubmed_publication_date":"20 Apr 2015","pubmed_entrez_date":"2015-04-21","publication_year":"2015","canto_session_key":"9f25f26d17f2ec78","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-26 14:38:31","canto_approved_date":"2025-09-03 16:37:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-16 16:05:08","canto_added_date":"2015-04-23 00:19:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jacky Hayles","community_curator":false,"annotation_count":33,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19F5.01c","SPBC16E9.17c","SPBC2G2.09c","SPAPB2B4.03","SPBC11B10.09","SPBC19C2.05","SPBC582.03","SPCC4E9.02"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2018-03-26"},{"uniquename":"PMID:14766577","title":"Viral preprotoxin signal sequence allows efficient secretion of green fluorescent protein by Candida glabrata, Pichia pastoris, Saccharomyces cerevisiae, and Schizosaccharomyces pombe.","citation":"Appl Environ Microbiol 2004 Feb;70(2):961-6","abstract":"Besides its importance as model organism in eukaryotic cell biology, yeast species have also developed into an attractive host for the expression, processing, and secretion of recombinant proteins. Here we investigated foreign protein secretion in four distantly related yeasts (Candida glabrata, Pichia pastoris, Saccharomyces cerevisiae, and Schizosaccharomyces pombe) by using green fluorescent protein (GFP) as a reporter and a viral secretion signal sequence derived from the K28 preprotoxin (pptox), the precursor of the yeast K28 virus toxin. In vivo expression of GFP fused to the N-terminal pptox leader sequence and/or expression of the entire pptox gene was driven either from constitutive (PGK1 and TPI1) or from inducible and/or repressible (GAL1, AOX1, and NMT1) yeast promoters. In each case, GFP entered the secretory pathway of the corresponding host cell; confocal fluorescence microscopy as well as sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western analysis of cell-free culture supernatants confirmed that GFP was efficiently secreted into the culture medium. In addition to the results seen with GFP, the full-length viral pptox was correctly processed in all four yeast genera, leading to the secretion of a biologically active virus toxin. Taken together, our data indicate that the viral K28 pptox signal sequence has the potential for being used as a unique tool in recombinant protein production to ensure efficient protein secretion in yeast.","authors":"Eiden-Plach A, Zagorc T, Heintel T, Carius Y, Breinig F, Schmitt MJ","authors_abbrev":"Eiden-Plach A et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2004-02-10","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18504300","title":"Reversible cytoplasmic localization of the proteasome in quiescent yeast cells.","citation":"J Cell Biol 2008 Jun 02;181(5):737-45","abstract":"The 26S proteasome is responsible for the controlled proteolysis of a vast number of proteins, including crucial cell cycle regulators. Accordingly, in Saccharomyces cerevisiae, 26S proteasome function is mandatory for cell cycle progression. In budding yeast, the 26S proteasome is assembled in the nucleus, where it is localized throughout the cell cycle. We report that upon cell entry into quiescence, proteasome subunits massively relocalize from the nucleus into motile cytoplasmic structures. We further demonstrate that these structures are proteasome cytoplasmic reservoirs that are rapidly mobilized upon exit from quiescence. Therefore, we have named these previously unknown structures proteasome storage granules (PSGs). Finally, we observe conserved formation and mobilization of these PSGs in the evolutionary distant yeast Schizosaccharomyces pombe. This conservation implies a broad significance for these proteasome reserves.","doi":"10.1083/jcb.200711154","authors":"Laporte D, Salin B, Daignan-Fornier B, Sagot I","authors_abbrev":"Laporte D et al.","pubmed_publication_date":"02 Jun 2008","pubmed_entrez_date":"2008-05-28","publication_year":"2008","canto_session_key":"6f7cf08e7e6712ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-04-17 12:47:54","canto_approved_date":"2024-04-17 12:47:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-04-17 12:47:44","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":4,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-04-17"},{"uniquename":"PMID:12815070","title":"Physical and functional interactions between polo kinase and the spindle pole component Cut12 regulate mitotic commitment in S. pombe.","citation":"Genes Dev 2003 Jun 15;17(12):1507-23","abstract":"Commitment to mitosis is regulated by a protein kinase complex called MPF. MPF is inhibited by Wee1-related kinases and activated by Cdc25 phosphatase. MPF activation further boosts Cdc25 and represses Wee1. This feedback control probably involves polo kinase. A dominant cut12.s11 mutation in the Schizosaccharomyces pombe spindle pole body (SPB) component Cut12 both suppresses the conditional lethal mitotic commitment defect of cdc25.22 and promotes premature association of the S. pombe polo kinase, Plo1, with the SPB. We now show that Cut12 associated with Plo1 in two hybrid and immunoprecipitation assays. Plo1 function was required for recognition of the mitotic SPB by the phospho-specific antibody MPM-2. In vivo MPM-2 staining and in vitro kinase assays established that the loss-of-function mutation, cut12.1, reduced mitotic activation of Plo1, whereas the gain-of-function mutation, cut12.s11, promoted higher levels of Plo1 activity than were normally seen in interphase. cut12.s11 could not promote mitotic commitment of cdc25.22 cells when Plo1 function was compromised. Expression of a constitutively active plo1 allele suppressed the mitotic commitment defect of cdc25.22. These data suggest that cut12.s11 suppresses cdc25.22 by promoting Plo1 activity. Furthermore, the delayed mitotic commitment of plo1.ts2 cells suggests that Plo1 is an integral part of the core controls that modulate MPF activation in S. pombe.","authors":"MacIver FH, Tanaka K, Robertson AM, Hagan IM","authors_abbrev":"MacIver FH et al.","pubmed_publication_date":"15 Jun 2003","pubmed_entrez_date":"2003-06-20","publication_year":"2003","canto_session_key":"6356242fe0e335bd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-12-10 18:08:18","canto_approved_date":"2026-01-31 11:58:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-01-31 11:58:06","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC649.05","SPAC25G10.07c","SPAC23C11.16","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-12-10"},{"uniquename":"PMID:32908306","title":"Epigenetic gene silencing by heterochromatin primes fungal resistance.","citation":"Nature 2020 Sep;585(7825):453-458","abstract":"Heterochromatin that depends on histone H3 lysine 9 methylation (H3K9me) renders embedded genes transcriptionally silent 1-3 . In the fission yeast Schizosaccharomyces pombe, H3K9me heterochromatin can be transmitted through cell division provided the counteracting demethylase Epe1 is absent 4,5 . Heterochromatin heritability might allow wild-type cells under certain conditions to acquire epimutations, which could influence phenotype through unstable gene silencing rather than DNA change 6,7 . Here we show that heterochromatin-dependent epimutants resistant to caffeine arise in fission yeast grown with threshold levels of caffeine. Isolates with unstable resistance have distinct heterochromatin islands with reduced expression of embedded genes, including some whose mutation confers caffeine resistance. Forced heterochromatin formation at implicated loci confirms that resistance results from heterochromatin-mediated silencing. Our analyses reveal that epigenetic processes promote phenotypic plasticity, letting wild-type cells adapt to unfavourable environments without genetic alteration. In some isolates, subsequent or coincident gene-amplification events augment resistance. Caffeine affects two anti-silencing factors: Epe1 is downregulated, reducing its chromatin association, and a shortened isoform of Mst2 histone acetyltransferase is expressed. Thus, heterochromatin-dependent epimutation provides a bet-hedging strategy allowing cells to adapt transiently to insults while remaining genetically wild type. Isolates with unstable caffeine resistance show cross-resistance to antifungal agents, suggesting that related heterochromatin-dependent processes may contribute to resistance of plant and human fungal pathogens to such agents.","doi":"10.1038/s41586-020-2706-x","authors":"Torres-Garcia S, Yaseen I, Shukla M, Audergon PNCB, White SA, Pidoux AL, Allshire RC","authors_abbrev":"Torres-Garcia S et al.","pubmed_publication_date":"Sep 2020","pubmed_entrez_date":"2020-09-10","publication_year":"2020","canto_session_key":"c2cd1d8a4d29ba93","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sito Torres-Garcia","canto_first_approved_date":"2021-04-13 15:13:24","canto_approved_date":"2024-04-04 07:07:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-03 13:52:14","canto_added_date":"2020-09-13 00:15:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sito Torres-Garcia","community_curator":true,"annotation_count":27,"orcid":"0000-0003-1029-8325","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.394","SPCC622.16c","SPNCRNA.393","SPBC17G9.13c","SPAC1783.07c","SPBC1815.01","SPBC17G9.12c","SPBC365.13c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2021-04-13"},{"uniquename":"PMID:24562612","title":"When Mad met Bub.","citation":"EMBO Rep 2014 Apr;15(4):326-8","abstract":"The faithful segregation of chromosomes into daughter cells is essential for cellular and organismal viability. Errors in this process cause aneuploidy, a hallmark of cancer and several congenital diseases. For proper separation, chromosomes attach to microtubules of the mitotic spindle via their kinetochores, large protein structures assembled on centromeric chromatin. Kinetochores are also crucial for a cell cycle feedback mechanism known as the spindle assembly checkpoint (SAC). The SAC forces cells to remain in mitosis until all chromosomes are properly attached to microtubules. At the beginning of mitosis, the SAC proteins--Mad1, Mad2, Bub1, Bub3, BubR1, Mps1, and Cdc20--are recruited to kinetochores in a hierarchical and interdependent fashion (Fig 1A). There they monitor, in ways that are not fully clarified, the formation of kinetochore-microtubule attachments. Two studies recently published in EMBO reports by the groups of Silke Hauf and Jakob Nilsson, and a recent study by London and Biggins in Genes & Development, shed new light on the conserved SAC protein Mad1.","doi":"10.1002/embr.201438574","authors":"Overlack K, Krenn V, Musacchio A","authors_abbrev":"Overlack K et al.","pubmed_publication_date":"Apr 2014","pubmed_entrez_date":"2014-02-25","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-12-16 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2204030","title":"The gene for cyclophilin (peptidyl-prolyl cis-trans isomerase) from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1990 Aug 25;18(16):4917","abstract":"","authors":"de Martin R, Philipson L","authors_abbrev":"de Martin R et al.","pubmed_publication_date":"25 Aug 1990","pubmed_entrez_date":"1990-08-25","publication_year":"1990","canto_session_key":"c052661320b11da4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 14:22:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-28 14:22:19","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-28"},{"uniquename":"PMID:1868575","title":"Sequence analysis of the ARG7 gene of Schizosaccharomyces pombe coding for argininosuccinate lyase. Expression of the gene in Saccharomyces cerevisiae.","citation":"Curr Genet 1991 Apr;19(4):255-60","abstract":"The complete nucleotide sequence of the ARG7 gene, coding for argininosuccinate lyase (EC 4.3.2.1), in the fission yeast (Schizosaccharomyces pombe) has been determined. It consists of an open reading frame of 461 codons. The deduced protein has a molecular weight of 51,200 Da. The gene is devoid of introns which is confirmed by the fact that it is expressed in Escherichia coli after spontaneous insertion of a bacterial sequence probably bearing a prokaryotic promoter. A perfect \"TATA\" box is found at -72 and the major transcription initiation site in Saccharomyces cerevisiae is located at -11 as shown by primer extension experiments. Comparison of the S. pombe lyase with related proteins from other organisms reveals an important degree of conservation except in the carboxyterminal part of the polypeptide. Additionally, a deletion removing 66 amino acids of the carboxy terminus yields an enzyme exhibiting some biological activity. A unique 1,500 b transcript was found in S. cerevisiae when the intact gene was present, but the deleted version of the gene gave rise to at least three transcripts of 1,800, 2,800 and 3,900 b.","authors":"Loppes R, Michels R, Decroupette I, Joris B","authors_abbrev":"Loppes R et al.","pubmed_publication_date":"Apr 1991","pubmed_entrez_date":"1991-04-01","publication_year":"1991","canto_session_key":"0fa147f6c25aba85","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-01-28 17:31:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 17:18:12","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1773.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-25"},{"uniquename":"PMID:10835379","title":"Schizosaccharomyces pombe Ste7p is required for both promotion and withholding of the entry to meiosis.","citation":"Genetics 2000 Jun;155(2):539-49","abstract":"The fission yeast ste7 mutant cannot mate and undergo meiosis, but shows no defect in vegetative growth. We cloned and characterized the ste7 gene. The deduced ste7 gene product (Ste7p) was a protein of 569 amino acids with no significant similarity to other proteins. Transcription of ste7 was induced by nutrient starvation via the function of the transcription factor Ste11p. Disruption of the ste7 gene blocked both conjugation and meiosis, showing that Ste7p plays a positive role in these two processes, probably activating the pheromone signal pathway. Unexpectedly, overexpression of ste7(+) promoted conjugation but inhibited meiosis in wild-type cells. The temperature-sensitive pat1-114 mutant underwent ectopic conjugation at the semirestrictive temperature when its genetic background was ste7(+), whereas the same mutant initiated haploid meiosis when its genetic background was ste7Delta. Two-hybrid analysis suggested that Ste7p interacts physically with both Pat1p and Mei2p, which together constitute the major switch to initiate meiosis. Ste7p tagged with green fluorescent protein accumulated in haploid cells under nutrient starvation until they completed conjugation, but this protein disappeared when they were to enter meiosis. These observations suggest that Ste7p may have a function to suppress the onset of meiosis until the conjugation process has been duly completed.","authors":"Matsuyama A, Yabana N, Watanabe Y, Yamamoto M","authors_abbrev":"Matsuyama A et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-06-03","publication_year":"2000","canto_session_key":"34e3d6fc4ce28886","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-23 15:04:04","canto_approved_date":"2026-04-11 08:07:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-02 14:32:35","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC23E2.03c","SPBC19C2.05","SPAC27D7.03c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-09-23"},{"uniquename":"PMID:9184215","title":"rqh1+, a fission yeast gene related to the Bloom's and Werner's syndrome genes, is required for reversible S phase arrest.","citation":"EMBO J 1997 May 15;16(10):2682-92","abstract":"In eukaryotic cells, S phase can be reversibly arrested by drugs that inhibit DNA synthesis or DNA damage. Here we show that recovery from such treatments is under genetic control and is defective in fission yeast rqh1 mutants. rqh1+, previously known as hus2+, encodes a putative DNA helicase related to the Escherichia coli RecQ helicase, with particular homology to the gene products of the human BLM and WRN genes and the Saccharomyces cerevisiae SGS1 gene. BLM and WRN are mutated in patients with Bloom's syndrome and Werner's syndrome respectively. Both syndromes are associated with genomic instability and cancer susceptibility. We show that, like BLM and SGS1, rqh1+ is required to prevent recombination and that in fission yeast suppression of inappropriate recombination is essential for reversible S phase arrest.","authors":"Stewart E, Chapman CR, Al-Khodairy F, Carr AM, Enoch T","authors_abbrev":"Stewart E et al.","pubmed_publication_date":"15 May 1997","pubmed_entrez_date":"1997-05-15","publication_year":"1997","canto_session_key":"bcfdccafeb565e24","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-11-26 17:33:11","canto_approved_date":"2021-01-06 17:28:11","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-26 17:33:03","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-26"},{"uniquename":"EMBL:SPD1691","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26697385","title":"Genome wide transcription profiling of the effects of overexpression of Spc1 and its kinase dead mutant in Schizosaccharomyces pombe.","citation":"Genom Data 2015 Dec;6:241-4","abstract":"The Mitogen Activated Protein Kinase Spc1 (p38 homolog) is a major player in stress responses of the unicellular fission yeast Schizosaccharomyces pombe. This pathway is therefore also known as the SAPK or Stress Activated Protein Kinase pathway. Spc1 is a known activator of transcription factors that control gene expression in response to extracellular stimuli and is also known to interact with the translation machinery [1], [2], [3], [4], [5], [6], [7], [8]. Spc1 has also been implicated in cell cycle regulation and meiosis in S. pombe[1], [2], [9], [10]. Given its documented role in modulating gene expression, we performed a microarray based identification of genes whose expression in unperturbed cells (absence of stress stimuli) is dependent on Spc1. For this we overexpressed Spc1 in S. pombe. Additionally we also overexpressed Spc1K49R (a kinase dead mutant of Spc1) to understand the contribution of Spc1's kinase activity towards the observed gene expression changes. The microarray data are available at NCBI's Gene Expression Omnibus (GEO) Series (accession number GSE73618). Here we report the annotation of the genes whose expression get altered by Spc1/Spc1K49R overexpression and also provide details related to sample processing and statistical analysis of our microarray data.","doi":"10.1016/j.gdata.2015.10.007","authors":"Paul M, Sanyal S, Sundaram G","authors_abbrev":"Paul M et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-12-24","publication_year":"2015","canto_session_key":"05f817bdcfed2bfa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-07 15:30:58","canto_approved_date":"2021-10-19 16:03:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-02-05 03:25:58","canto_added_date":"2015-12-25 01:19:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.22","SPAC24B11.06c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2018-02-07"},{"uniquename":"PMID:34747981","title":"Pcp1/pericentrin controls the SPB number in fission yeast meiosis and ploidy homeostasis.","citation":"J Cell Biol 2022 Jan 03;221(1)","abstract":"During sexual reproduction, the zygote must inherit exactly one centrosome (spindle pole body [SPB] in yeasts) from the gametes, which then duplicates and assembles a bipolar spindle that supports the subsequent cell division. Here, we show that in the fission yeast Schizosaccharomyces pombe, the fusion of SPBs from the gametes is blocked in polyploid zygotes. As a result, the polyploid zygotes cannot proliferate mitotically and frequently form supernumerary SPBs during subsequent meiosis, which leads to multipolar nuclear divisions and the generation of extra spores. The blockage of SPB fusion is caused by persistent SPB localization of Pcp1, which, in normal diploid zygotic meiosis, exhibits a dynamic association with the SPB. Artificially induced constitutive localization of Pcp1 on the SPB is sufficient to cause blockage of SPB fusion and formation of extra spores in diploids. Thus, Pcp1-dependent SPB quantity control is crucial for sexual reproduction and ploidy homeostasis in fission yeast.","doi":"10.1083/jcb.202104099","authors":"Zhu Q, Jiang Z, He X","authors_abbrev":"Zhu Q et al.","pubmed_publication_date":"03 Jan 2022","pubmed_entrez_date":"2021-11-08","publication_year":"2022","canto_session_key":"a9267c409961f4d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-11-10 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33164662","title":"Atg11-mediated activation of Atg1 kinase in fission yeast.","citation":"Autophagy 2021 Feb;17(2):584-585","abstract":"The protein kinase Atg1 is a key player in macroautophagy/autophagy, but how its activity is regulated in various organisms is inadequately understood. Our recent study showed that in the fission yeast  Schizosaccharomyces pombe , Atg1 kinase activity depends on Atg11, but not Atg13, Atg17, or Atg101. Notably, a 62 amino acid region of  S. pombe  Atg11 is sufficient for activating Atg1. This region is composed of two parts: an Atg1-binding domain and a homodimerization domain. Atg11 uses this region to dimerize Atg1. Dimerized Atg1 is activated through cis-autophosphorylation.","doi":"10.1080/15548627.2020.1846303","authors":"Pan ZQ, Du LL","authors_abbrev":"Pan ZQ et al.","pubmed_publication_date":"Feb 2021","pubmed_entrez_date":"2020-11-09","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-11-12 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC63.08c","SPAC7D4.04"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:16055437","title":"Interaction of a small heat shock protein of the fission yeast, Schizosaccharomyces pombe, with a denatured protein at elevated temperature.","citation":"J Biol Chem 2005 Sep 23;280(38):32586-93","abstract":"We have expressed, purified, and characterized one small heat shock protein of the fission yeast Schizosaccharomyces pombe, SpHsp16.0. SpHsp16.0 was able to protect citrate synthase from thermal aggregation at 45 degrees C with high efficiency. It existed as a hexadecameric globular oligomer near the physiological growth temperature. At elevated temperatures, the oligomer dissociated into small species, probably dimers. The dissociation was completely reversible, and the original oligomer reformed immediately after the temperature dropped. Large complexes of SpHsp16.0 and denatured citrate synthase were observed by size exclusion chromatography and electron microscopy following incubation at 45 degrees C and then cooling. However, such large complexes did not elute from the size exclusion column incubated at 45 degrees C. The denatured citrate synthase protected from aggregation was trapped by a GroEL trap mutant at 45 degrees C. These results suggest that the complex of SpHsp16.0 and denatured citrate synthase at elevated temperatures is in the transient state and has a hydrophobic nature. Analyses of the interaction between SpHsp16.0 and denatured citrate synthase by fluorescence cross-correlation spectrometry have also shown that the characteristics of SpHsp16.0-denatured citrate synthase complex at the elevated temperature are different from those of the large complex obtained after the shift to lowered temperatures.","authors":"Hirose M, Tohda H, Giga-Hama Y, Tsushima R, Zako T, Iizuka R, Pack C, Kinjo M, Ishii N, Yohda M","authors_abbrev":"Hirose M et al.","pubmed_publication_date":"23 Sep 2005","pubmed_entrez_date":"2005-08-02","publication_year":"2005","canto_session_key":"09f311273c61ffe7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-02 18:09:44","canto_approved_date":"2026-02-21 14:18:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-02 18:09:38","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-07-02"},{"uniquename":"PMID:9852944","title":"Identification of the gene and the protein of RNA polymerase II subunit 9 (Rpb9) from the fission yeast Schizosacharomyces pombe.","citation":"Gene 1998 Oct 09;221(1):11-6","abstract":"Both the rpb9 gene and its cDNA encoding the subunit 9 of RNA polymerase II were cloned from the fission yeast Schizosaccharomyces pombe. From the DNA sequences, Rpb9 was predicted to consist of 113 amino acid residues with a molecular mass of 13,175. S. pombe Rpb9 is 47, 40 and 36% identical in amino acid sequence to the corresponding subunits from Saccharomyces cerevisiae, human and Drosophila melanogaster, respectively. Previously, we failed to detect Rpb9 in the purified RNA polymerase II by amino-terminal micro-sequencing of proteolytic fragments of subunits separated by SDS-gel electrophoresis. After Western blot analysis using antibodies raised against the protein product of the newly isolated rpb9 gene, we found that the purified RNA polymerase II contains Rpb9.","authors":"Sakurai H, Kimura M, Ishihama A","authors_abbrev":"Sakurai H et al.","pubmed_publication_date":"09 Oct 1998","pubmed_entrez_date":"1998-12-16","publication_year":"1998","canto_session_key":"9c262ab39c68163e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-04 12:56:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 12:15:06","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPYUG7.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:38878203","title":"Unravelling bacterial virulence factors in yeast: From identification to the elucidation of their mechanisms of action.","citation":"Arch Microbiol 2024 Jun 15;206(7):303","abstract":"Pathogenic bacteria employ virulence factors (VF) to establish infection and cause disease in their host. Yeasts, Saccharomyces cerevisiae and Saccharomyces pombe, are useful model organisms to study the functions of bacterial VFs and their interaction with targeted cellular processes because yeast processes and organelle structures are highly conserved and similar to higher eukaryotes. In this review, we describe the principles and applications of the yeast model for the identification and functional characterisation of bacterial VFs to investigate bacterial pathogenesis. The growth inhibition phenotype caused by the heterologous expression of bacterial VFs in yeast is commonly used to identify candidate VFs. Then, subcellular localisation patterns of bacterial VFs can provide further clues about their target molecules and functions during infection. Yeast knockout and overexpression libraries are also used to investigate VF interactions with conserved eukaryotic cell structures (e.g., cytoskeleton and plasma membrane), and cellular processes (e.g., vesicle trafficking, signalling pathways, and programmed cell death). In addition, the yeast growth inhibition phenotype is also useful for screening new drug leads that target and inhibit bacterial VFs. This review provides an updated overview of new tools, principles and applications to study bacterial VFs in yeast.","doi":"10.1007/s00203-024-04023-2","authors":"Ong ZWEBB","authors_abbrev":"Ong ZWEBB","pubmed_publication_date":"15 Jun 2024","pubmed_entrez_date":"2024-06-15","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-06-15 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25686494","title":"Coordinated regulation by two VPS9 domain-containing guanine nucleotide exchange factors in small GTPase Rab5 signaling pathways in fission yeast.","citation":"Biochem Biophys Res Commun 2015 Mar 20;458(4):802-9","abstract":"The small GTPase Rab5 is reported to regulate various cellular functions, such as vesicular transport and endocytosis. VPS9 domain-containing proteins are thought to activate Rab5(s) by their guanine-nucleotide exchange activities. Numerous VPS9 proteins have been identified and are structurally conserved from yeast to mammalian cells. However, the functional relationships among VPS9 proteins in cells remain unclear. Only one Rab5 and two VPS9 proteins were identified in the Schizosaccharomyces pombe genome. Here, we examined the cellular function of two VPS9 proteins and the relationship between these proteins in cellular functions. Vps901-GFP and Vps902-GFP exhibited dotted signals in vegetative and differentiated cells. vps901 deletion mutant (Δvps901) cells exhibited a phenotype deficient in the mating process and responses to high concentrations of ions, such as calcium and metals, and Δvps901Δvps902 double mutant cells exhibited round cell shapes similar to ypt5-909 (Rab5 mutant allele) cells. Deletion of both vps901 and vps902 genes completely abolished the mating process and responses to various stresses. A lack of vacuole formation and aberrant inner cell membrane structures were also observed in Δvps901Δvps902 cells by electron microscopy. These data strongly suggest that Vps901 and Vps902 are cooperatively involved in the regulation of cellular functions, such as cell morphology, sexual development, response to ion stresses, and vacuole formation, via Rab5 signaling pathways in fission yeast cells.","doi":"10.1016/j.bbrc.2015.02.031","authors":"Tsukamoto Y, Kagiwada S, Shimazu S, Takegawa K, Noguchi T, Miyamoto M","authors_abbrev":"Tsukamoto Y et al.","pubmed_publication_date":"20 Mar 2015","pubmed_entrez_date":"2015-02-18","publication_year":"2015","canto_session_key":"3b9c4f119c698369","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-02-19 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4F6.10","SPBC29A10.11c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7749325","title":"The genetics of cell cycle checkpoints.","citation":"Curr Opin Genet Dev 1995 Feb;5(1):5-11","abstract":"Checkpoints help in the prevention of genetic damage by giving cells time to repair damaged structures before proceeding in the cell cycle. Genetic analyses in budding and fission yeast have identified a large number of cell cycle checkpoint genes. Several of these encode proteins related to components of other signal transduction pathways, including protein kinases, lipid kinases, and 14-3-3 proteins. In fission yeast, checkpoints play an important role in keeping cells from entering mitosis before they pass Start.","authors":"Murray AW","authors_abbrev":"Murray AW","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19783819","title":"MiCroKit 3.0: an integrated database of midbody, centrosome and kinetochore.","citation":"Nucleic Acids Res 2010 Jan;38(Database issue):D155-60","abstract":"During cell division/mitosis, a specific subset of proteins is spatially and temporally assembled into protein super complexes in three distinct regions, i.e. centrosome/spindle pole, kinetochore/centromere and midbody/cleavage furrow/phragmoplast/bud neck, and modulates cell division process faithfully. Although many experimental efforts have been carried out to investigate the characteristics of these proteins, no integrated database was available. Here, we present the MiCroKit database (http://microkit.biocuckoo.org) of proteins that localize in midbody, centrosome and/or kinetochore. We collected into the MiCroKit database experimentally verified microkit proteins from the scientific literature that have unambiguous supportive evidence for subcellular localization under fluorescent microscope. The current version of MiCroKit 3.0 provides detailed information for 1489 microkit proteins from seven model organisms, including Saccharomyces cerevisiae, Schizasaccharomyces pombe, Caenorhabditis elegans, Drosophila melanogaster, Xenopus laevis, Mus musculus and Homo sapiens. Moreover, the orthologous information was provided for these microkit proteins, and could be a useful resource for further experimental identification. The online service of MiCroKit database was implemented in PHP + MySQL + JavaScript, while the local packages were developed in JAVA 1.5 (J2SE 5.0).","doi":"10.1093/nar/gkp784","authors":"Ren J, Liu Z, Gao X, Jin C, Ye M, Zou H, Wen L, Zhang Z, Xue Y, Yao X","authors_abbrev":"Ren J et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-09-29","publication_year":"2010","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24939935","title":"How an mRNA capping enzyme reads distinct RNA polymerase II and Spt5 CTD phosphorylation codes.","citation":"Genes Dev 2014 Jun 15;28(12):1323-36","abstract":"Interactions between RNA guanylyltransferase (GTase) and the C-terminal domain (CTD) repeats of RNA polymerase II (Pol2) and elongation factor Spt5 are thought to orchestrate cotranscriptional capping of nascent mRNAs. The crystal structure of a fission yeast GTase•Pol2 CTD complex reveals a unique docking site on the nucleotidyl transferase domain for an 8-amino-acid Pol2 CTD segment, S5PPSYSPTS5P, bracketed by two Ser5-PO4 marks. Analysis of GTase mutations that disrupt the Pol2 CTD interface shows that at least one of the two Ser5-PO4-binding sites is required for cell viability and that each site is important for cell growth at 37°C. Fission yeast GTase binds the Spt5 CTD at a separate docking site in the OB-fold domain that captures the Trp4 residue of the Spt5 nonapeptide repeat T(1)PAW(4)NSGSK. A disruptive mutation in the Spt5 CTD-binding site of GTase is synthetically lethal with mutations in the Pol2 CTD-binding site, signifying that the Spt5 and Pol2 CTDs cooperate to recruit capping enzyme in vivo. CTD phosphorylation has opposite effects on the interaction of GTase with Pol2 (Ser5-PO4 is required for binding) versus Spt5 (Thr1-PO4 inhibits binding). We propose that the state of Thr1 phosphorylation comprises a binary \"Spt5 CTD code\" that is read by capping enzyme independent of and parallel to its response to the state of the Pol2 CTD.","doi":"10.1101/gad.242768.114","authors":"Doamekpor SK, Sanchez AM, Schwer B, Shuman S, Lima CD","authors_abbrev":"Doamekpor SK et al.","pubmed_publication_date":"15 Jun 2014","pubmed_entrez_date":"2014-06-19","publication_year":"2014","canto_session_key":"43659e6aa472ef94","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2024-03-21 08:10:53","canto_approved_date":"2024-05-13 12:40:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-27 15:15:32","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":26,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.08c","SPBC28F2.12","SPAC23C4.19"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2024-03-21","pdb_entries":[{"pdb_id":"4pz6","gene_chains":[{"gene_uniquename":"SPBC28F2.12","chain":"P/Q","position":"1732-1752"},{"gene_uniquename":"SPBC2F12.08c","chain":"A/B","position":"1-402"}],"title":"PCE1 guanylyltransferase bound to SER2/SER5 phosphorylated RNA pol II CTD","entry_authors":"Doamekpor SK,Lima CD","entry_authors_abbrev":"Doamekpor SK et al.","reference_uniquename":"PMID:24939935","experimental_method":"X-ray","resolution":"2.406"},{"pdb_id":"4pz8","gene_chains":[{"gene_uniquename":"SPAC23C4.19","chain":"B","position":"827-844"},{"gene_uniquename":"SPBC2F12.08c","chain":"A","position":"1-402"}],"title":"PCE1 guanylyltransferase bound to SPT5 CTD","entry_authors":"Doamekpor SK,Lima CD","entry_authors_abbrev":"Doamekpor SK et al.","reference_uniquename":"PMID:24939935","experimental_method":"X-ray","resolution":"3.1"},{"pdb_id":"4pz7","gene_chains":[{"gene_uniquename":"SPBC2F12.08c","chain":"A/B","position":"1-402"}],"title":"PCE1 guanylyltransferase","entry_authors":"Doamekpor SK,Lima CD","entry_authors_abbrev":"Doamekpor SK et al.","reference_uniquename":"PMID:24939935","experimental_method":"X-ray","resolution":"2.109"}]},{"uniquename":"PMID:32053104","title":"Mechanisms of chromosome biorientation and bipolar spindle assembly analyzed by computational modeling.","citation":"Elife 2020 Feb 13;9","abstract":"The essential functions required for mitotic spindle assembly and chromosome biorientation and segregation are not fully understood, despite extensive study. To illuminate the combinations of ingredients most important to align and segregate chromosomes and simultaneously assemble a bipolar spindle, we developed a computational model of fission-yeast mitosis. Robust chromosome biorientation requires progressive restriction of attachment geometry, destabilization of misaligned attachments, and attachment force dependence. Large spindle length fluctuations can occur when the kinetochore-microtubule attachment lifetime is long. The primary spindle force generators are kinesin-5 motors and crosslinkers in early mitosis, while interkinetochore stretch becomes important after biorientation. The same mechanisms that contribute to persistent biorientation lead to segregation of chromosomes to the poles after anaphase onset. This model therefore provides a framework to interrogate key requirements for robust chromosome biorientation, spindle length regulation, and force generation in the spindle.","doi":"10.7554/eLife.48787","authors":"Edelmaier C, Lamson AR, Gergely ZR, Ansari S, Blackwell R, McIntosh JR, Glaser MA, Betterton MD","authors_abbrev":"Edelmaier C et al.","pubmed_publication_date":"13 Feb 2020","pubmed_entrez_date":"2020-02-14","publication_year":"2020","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12018857","title":"Fission yeast Rap1 homolog is a telomere-specific silencing factor and interacts with Taz1p.","citation":"Mol Cells 2002 Apr 30;13(2):327-33","abstract":"Taz1p is the fission yeast orthologue of human TRF2, a telomeric repeat-binding protein. Delta(taz1) mutants are defective in telomeric silencing, telomere length control, and meiotic recombination events. A recent report demonstrated that the human Rap1p homolog (hRap1) is recruited to telomere by interaction with TRF2, arguing that the telomere control mechanism of higher eukaryotes is distinct from that of the budding yeast. Taz1p showed a significant similarity to human TRF2, but not with the budding yeast Rap1p (scRap1p). This suggests that Taz1p and TRF2 share common features in telomere regulation. To assess the roles of Taz1p in telomere-related functions in detail, we attempted to identify a protein(s) that interacts with Taz1p by using two-hybrid screening. Interestingly, the sequence analysis of a positive clone revealed a perfect match with a Rap1 homolog in S. pombe (spRap1), which showed a significant homology with scRap1p and hRap1p. Here we show that the spRap1 deficiency in haploid cells is viable, which results in increased telomere length regulation, disruption of telomere silencing, and aberrant meiosis (like the delta(taz1) mutant). This suggests that spRap1p might be recruited to the telomere by Taz1p and play crucial roles in telomere function. Interestingly, the delta(rap1) mutants in fission yeast are defective only for telomere silencing. Therefore, the role of spRap1p may be distinct from that of scRap1p, which is involved in the silencing at both the telomere and mating type locus. Our data, therefore, suggest that the regulation mechanisms of telomere in fission yeast resemble that of higher eukaryotic cells rather than the budding yeast.","authors":"Park MJ, Jang YK, Choi ES, Kim HS, Park SD","authors_abbrev":"Park MJ et al.","pubmed_publication_date":"30 Apr 2002","pubmed_entrez_date":"2002-05-23","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1778.02","SPAC16A10.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:X15220","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.98"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24478458","title":"The checkpoint-dependent nuclear accumulation of Rho1p exchange factor Rgf1p is important for tolerance to chronic replication stress.","citation":"Mol Biol Cell 2014 Apr;25(7):1137-50","abstract":"Guanine nucleotide exchange factors control many aspects of cell morphogenesis by turning on Rho-GTPases. The fission yeast exchange factor Rgf1p (Rho gef1) specifically regulates Rho1p during polarized growth and localizes to cortical sites. Here we report that Rgf1p is relocalized to the cell nucleus during the stalled replication caused by hydroxyurea (HU). Import to the nucleus is mediated by a nuclear localization sequence at the N-terminus of Rgf1p, whereas release into the cytoplasm requires two leucine-rich nuclear export sequences at the C-terminus. Moreover, Rgf1p nuclear accumulation during replication arrest depends on the 14-3-3 chaperone Rad24p and the DNA replication checkpoint kinase Cds1p. Both proteins control the nuclear accumulation of Rgf1p by inhibition of its nuclear export. A mutant, Rgf1p-9A, that substitutes nine serine potential phosphorylation Cds1p sites for alanine fails to accumulate in the nucleus in response to replication stress, and this correlates with a severe defect in survival in the presence of HU. In conclusion, we propose that the regulation of Rgf1p could be part of the mechanism by which Cds1p and Rad24p promote survival in the presence of chronic replication stress. It will be of general interest to understand whether the same is true for homologues of Rgf1p in budding yeast and higher eukaryotes.","doi":"10.1091/mbc.E13-11-0689","authors":"Muñoz S, Manjón E, García P, Sunnerhagen P, Sánchez Y","authors_abbrev":"Muñoz S et al.","pubmed_publication_date":"Apr 2014","pubmed_entrez_date":"2014-01-31","publication_year":"2014","canto_session_key":"7b30a1cc7d87ace2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-15 15:34:18","canto_approved_date":"2023-04-08 18:21:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-08-22 11:27:13","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":61,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.06c","SPBC216.05","SPAC1805.17","SPCC18B5.11c","SPCC645.07","SPAC8E11.02c","SPAC1006.06","SPAC1F7.04","SPCC1259.13"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2018-02-15"},{"uniquename":"PMID:2417640","title":"Probing fungal mitochondrial evolution with tRNA.","citation":"Biosystems 1985;18(3-4):263-7","abstract":"Sequence data are now available for almost the entire complement of mitochondrial rRNAs from five fungi: Schizosaccharomyces pombe, Saccharomyces cerevisiae, Toropulis glabrata, Aspergillus nidulans and Neurospora crassa. Analysis of these data show that the five mitochondria can be related to a common ancestor. The unusually high similarity between some S. pombe mt tRNAs may be due to a process similar to gene conversion. Using the number of differences between tRNA pairs as a measure of the evolutionary rate the yeast-S. pombe branch has paradoxically a high nuclear rate and a low mt rate of evolution as compared with other branches in the phylogenetic tree. Finally the position of mt tRNA genes in S. pombe is abnormally distinct from gene orders in other mitochondria. All of the above factors must be taken into account when describing the relationship between these mitochondria.","authors":"Cedergren R, Lang BF","authors_abbrev":"Cedergren R et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20152173","title":"Dcr1 tracked down.","citation":"Dev Cell 2010 Jan 19;18(1):6-7","abstract":"RNAi is essential for pericentromeric heterochromatic formation in S. pombe, and although Dcr1, the initiator protein of this process, has been biochemically well described, its subcellular localization has remained elusive. In this issue of Developmental Cell, Emmerth et al. now show that Dcr1 is dynamically shuttling between nucleus and cytoplasm, adding new insight into the subcellular mechanics of RNAi.","doi":"10.1016/j.devcel.2010.01.001","authors":"Kaaij LJ, Ketting RF","authors_abbrev":"Kaaij LJ et al.","pubmed_publication_date":"19 Jan 2010","pubmed_entrez_date":"2010-02-16","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25763975","title":"Kinesin-8 motors improve nuclear centering by promoting microtubule catastrophe.","citation":"Phys Rev Lett 2015 Feb 20;114(7):078103","abstract":"In fission yeast, microtubules push against the cell edge, thereby positioning the nucleus in the cell center. Kinesin-8 motors regulate microtubule catastrophe; however, their role in nuclear positioning is not known. Here we develop a physical model that describes how kinesin-8 motors affect nuclear centering by promoting a microtubule catastrophe. Our model predicts the improved centering of the nucleus in the presence of motors, which we confirmed experimentally in living cells. The model also predicts a characteristic time for the recentering of a displaced nucleus, which is supported by our experiments where we displaced the nucleus using optical tweezers.","authors":"Glunčić M, Maghelli N, Krull A, Krstić V, Ramunno-Johnson D, Pavin N, Tolić IM","authors_abbrev":"Glunčić M et al.","pubmed_publication_date":"20 Feb 2015","pubmed_entrez_date":"2015-03-13","publication_year":"2015","canto_session_key":"46ad29ab22f1f5e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-12 05:34:40","canto_approved_date":"2024-06-12 05:34:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-11 15:15:54","canto_added_date":"2015-03-14 01:15:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-06-12"},{"uniquename":"PMID:29084823","title":"Phosphorylation of the RNA-binding protein Zfs1 modulates sexual differentiation in fission yeast.","citation":"J Cell Sci 2017 Dec 15;130(24):4144-4154","abstract":"Sexual differentiation in the fission yeast  Schizosaccharomyces pombe  promotes cell cycle arrest and extensive changes in gene expression, resulting in cell-to-cell fusion, the exchange of hereditary material and specialized cell division. These events are detrimental to the cell if they are triggered in inappropriate conditions, and therefore the decision to differentiate must be precisely controlled. Here, we investigated the role of the RNA-binding protein Zfs1 in this process by identifying its targets and characterizing novel post-translational regulatory mechanisms. We found that Zfs1 negatively regulates the G1 cyclin Puc1, and deregulated Puc1 levels inhibit differentiation in the  zfs1 Δ mutant. We also found that Zfs1 undergoes phosphorylation, which is stimulated upon nitrogen depletion or inhibition of the TOR pathway. Phosphorylation of Zfs1 modulates accumulation of Puc1 and plays an important role in the response of the cell to sexual differentiation signals. We propose that Zfs1 functions as an integrator of nutrient information to modulate sexual differentiation, contributing to the establishment of the differentiation-activating threshold.","doi":"10.1242/jcs.208066","authors":"Navarro FJ, Chakravarty P, Nurse P","authors_abbrev":"Navarro FJ et al.","pubmed_publication_date":"15 Dec 2017","pubmed_entrez_date":"2017-11-01","publication_year":"2017","canto_session_key":"efc5a5e85ec7f642","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-02-24 14:39:32","canto_approved_date":"2023-03-14 18:06:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-12 11:57:55","canto_added_date":"2017-11-02 01:15:16","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":42,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.04c","SPBC13E7.02","SPAC3H8.09c","SPBC1347.12","SPAC13G7.04c","SPCC24B10.07","SPAC688.10","SPBC30B4.09","SPBC36.02c","SPCC576.16c","SPCC594.04c","SPNCRNA.1197","SPAPB2B4.03","SPAC23H3.13c","SPCC895.05","SPAC3H1.11","SPBC14F5.10c","SPAC24H6.11c","SPAPB1A10.05","SPNCRNA.1367","SPCC330.02","SPNCRNA.570","SPAC14C4.10c","SPAC1399.01c","SPBC32F12.07c","SPAC328.04","SPCC1235.03","SPAC1B3.11c","SPAC24B11.09","SPBC32C12.02","SPAC959.11","SPBC337.12","SPBC651.04","SPCC1450.05c","SPCC70.09c","SPNCRNA.1299","SPAC19D5.01","SPBC11B10.09","SPBC16D10.04c","SPCC290.04","SPBC32H8.11","SPCC736.15","SPAC1F3.02c","SPAC16A10.01","SPAC3C7.06c","SPBC18H10.09","SPBC19G7.06","SPBC30B4.07c","SPAC31F12.01","SPBC649.03","SPCC162.04c","SPCC1906.03","SPCC548.03c","SPCC553.09c","SPCC4E9.02","SPBC56F2.05c","SPBC17D11.01","SPNCRNA.1678","SPAC31A2.13c","SPAC806.06c","SPAC977.17","SPAPB24D3.10c","SPBC1685.07c","SPBC19G7.08c","SPBC530.11c","SPBC30B4.01c","SPAC13G6.12c","SPBC36B7.02","SPBC4B4.08","SPNCRNA.1059","SPNCRNA.1427","SPNCRNA.1467","SPBC19C2.04c","SPNCRNA.1366","SPNCRNA.1475","SPAC458.03","SPAC24H6.13","SPNCRNA.1044","SPAC26A3.01","SPBC21C3.03","SPAC31G5.11","SPBC1289.13c","SPAC11E3.14","SPBC12D12.06","SPBC28F2.02","SPBC3H7.02","SPBC336.03","SPBC3H7.14","SPBC428.10","SPAC3C7.02c","SPCC1020.10","SPAC323.08","SPAC4D7.03","SPBC19C2.13c","SPBC25B2.08","SPCC191.09c","SPAC3A12.19","SPBC354.09c","SPAC31A2.12","SPAC17H9.08","SPBC20F10.03","SPCC569.05c","SPCC584.16c","SPBC20F10.10","SPCC830.02","SPNCRNA.1157","SPBC1718.07c","SPBC2G5.02c","SPAC3F10.12c","SPBC23G7.06c","SPAC343.18","SPBC19F5.01c","SPAC23H4.16c","SPAC6G10.10c","SPBC30B4.02c","SPBC649.04","SPAC959.10","SPBP4H10.10","SPCC1450.08c","SPAC227.03c","SPCC1494.03","SPCC553.05c","SPNCRNA.1518","SPNCRNA.846","SPBC106.08c","SPAC18G6.09c","SPBC691.01","SPBC1348.02","SPNCRNA.865","SPAC6F12.12","SPBC29A10.02","SPBC660.14","SPAC343.15","SPCP25A2.02c","SPNCRNA.866","SPNCRNA.1391","SPBC428.08c","SPAC17G6.02c","SPAC1B3.15c","SPAC110.01","SPAC589.03c","SPBC36.03c","SPBC1685.13","SPAC9E9.02","SPAC821.08c","SPAPB1A10.08","SPBC2A9.04c","SPBC16A3.17c","SPAC8C9.16c","SPCC1442.07c","SPCC622.01c","SPAC23H4.17c","SPAC19E9.03","SPAC15E1.07c","SPAC27E2.11c","SPBC3B9.06c","SPCC320.05","SPAC2H10.01","SPBC8E4.12c","SPAC1002.05c","SPAC22G7.08","SPBC342.05","SPCC1235.06","SPAC23H3.04","SPCC285.07c","SPNCRNA.752","SPAC167.03c","SPBC19G7.01c","SPAC31G5.09c","SPAC644.06c","SPAC13G7.02c","SPNCRNA.1273","SPAC637.11","SPAC32A11.01","SPAPB1A10.14","SPNCRNA.873","SPAC2F3.01","SPBC8D2.11","SPAC14C4.03","SPNCRNA.1297","SPCC162.11c","SPCC1223.13","SPCC1620.02","SPAC343.06c","SPBC2D10.04","SPBC16G5.16","SPBC19C2.05","SPBC27B12.09c","SPAC22F8.02c","SPCC1682.12c","SPCC4G3.05c","SPNCRNA.1480","SPBC36.01c","SPNCRNA.1689","SPBC530.05","SPBC800.05c","SPBC1773.15","SPAC20G4.04c","SPAC823.06","SPAC6B12.02c","SPCC1739.08c","SPCC188.09c","SPCC645.06c","SPAC6G9.05","SPCC1494.08c","SPAC607.10","SPAC222.19","SPAC8C9.09c","SPAC3A11.09","SPAC11D3.17","SPBC16E9.16c","SPBC215.04","SPCC1795.09","SPCC285.10c","SPBC32H8.12c","SPNCRNA.1201","SPBC3B9.21","SPCC553.04","SPCC4G3.10c","SPNCRNA.1356"],"gene_count":220,"ltp_gene_count":10,"approved_date":"2021-02-24"},{"uniquename":"PMID:24656819","title":"Protein phosphatase 1 recruitment by Rif1 regulates DNA replication origin firing by counteracting DDK activity.","citation":"Cell Rep 2014 Apr 10;7(1):53-61","abstract":"The firing of eukaryotic origins of DNA replication requires CDK and DDK kinase activities. DDK, in particular, is involved in setting the temporal program of origin activation, a conserved feature of eukaryotes. Rif1, originally identified as a telomeric protein, was recently implicated in specifying replication timing in yeast and mammals. We show that this function of Rif1 depends on its interaction with PP1 phosphatases. Mutations of two PP1 docking motifs in Rif1 lead to early replication of telomeres in budding yeast and misregulation of origin firing in fission yeast. Several lines of evidence indicate that Rif1/PP1 counteract DDK activity on the replicative MCM helicase. Our data suggest that the PP1/Rif1 interaction is downregulated by the phosphorylation of Rif1, most likely by CDK/DDK. These findings elucidate the mechanism of action of Rif1 in the control of DNA replication and demonstrate a role of PP1 phosphatases in the regulation of origin firing.","doi":"10.1016/j.celrep.2014.02.019","authors":"Davé A, Cooley C, Garg M, Bianchi A","authors_abbrev":"Davé A et al.","pubmed_publication_date":"10 Apr 2014","pubmed_entrez_date":"2014-03-25","publication_year":"2014","canto_session_key":"d3d1c8398672c5ba","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-02-21 17:28:46","canto_approved_date":"2022-09-29 15:27:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-07 19:57:30","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":48,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.17","SPBC776.12c","SPBC776.02c","SPBC11B10.09","SPCC31H12.05c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-02-21"},{"uniquename":"PMID:8602505","title":"Cell shape determination: a pivotal role for Rho.","citation":"Science 1996 Apr 12;272(5259):224-5","abstract":"","authors":"Bussey H","authors_abbrev":"Bussey H","pubmed_publication_date":"12 Apr 1996","pubmed_entrez_date":"1996-04-12","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18303049","title":"Chemical genetic analysis of the regulatory role of Cdc2p in the S. pombe septation initiation network.","citation":"J Cell Sci 2008 Mar 15;121(Pt 6):843-53","abstract":"The protein kinase Cdc2p is the master regulator of cell cycle progression in the fission yeast Schizosaccharomyces pombe. It is required both for entry into mitosis and for onset of DNA replication. Cdc2p must be inactivated to permit exit from mitosis, licensing of replication origins and cytokinesis. To study the role of Cdc2p in greater detail, we generated a cdc2 allele that is sensitive to an inhibitory ATP analogue. We show that the inhibitor-induced cell cycle arrest is reversible and examine the effect of inhibiting Cdc2p on the regulation of the septation initiation network (SIN), which controls the initiation of cytokinesis in S. pombe. We found that specific inactivation of Cdc2p in a mitotically arrested cell promotes the asymmetrical recruitment of SIN proteins to the spindle poles and the recruitment of the most downstream SIN components and beta-(1,3) glucan synthase to the contractile ring. Thus, we conclude that inactivation of Cdc2p is sufficient to activate the SIN and promote cytokinesis.","doi":"10.1242/jcs.021584","authors":"Dischinger S, Krapp A, Xie L, Paulson JR, Simanis V","authors_abbrev":"Dischinger S et al.","pubmed_publication_date":"15 Mar 2008","pubmed_entrez_date":"2008-02-28","publication_year":"2008","canto_session_key":"4bc8f8330173e8e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-08-12 17:27:53","canto_approved_date":"2024-08-13 16:10:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-12 17:27:48","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":17,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC11B10.09","SPBC428.13c","SPAC23C11.16","SPBC19G7.05c","SPAC1782.09c","SPAC9G1.09","SPBC21.06c"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2024-08-12"},{"uniquename":"PMID:18077559","title":"Biphasic incorporation of centromeric histone CENP-A in fission yeast.","citation":"Mol Biol Cell 2008 Feb;19(2):682-90","abstract":"CENP-A is a centromere-specific histone H3 variant that is essential for kinetochore formation. Here, we report that the fission yeast Schizosaccharomyces pombe has at least two distinct CENP-A deposition phases across the cell cycle: S and G2. The S phase deposition requires Ams2 GATA factor, which promotes histone gene activation. In Delta ams2, CENP-A fails to retain during S, but it reaccumulates onto centromeres via the G2 deposition pathway, which is down-regulated by Hip1, a homologue of HIRA histone chaperon. Reducing the length of G2 in Delta ams2 results in failure of CENP-A accumulation, leading to chromosome missegregation. N-terminal green fluorescent protein-tagging reduces the centromeric association of CENP-A, causing cell death in Delta ams2 but not in wild-type cells, suggesting that the N-terminal tail of CENP-A may play a pivotal role in the formation of centromeric nucleosomes at G2. These observations imply that CENP-A is normally localized to centromeres in S phase in an Ams2-dependent manner and that the G2 pathway may salvage CENP-A assembly to promote genome stability. The flexibility of CENP-A incorporation during the cell cycle may account for the plasticity of kinetochore formation when the authentic centromere is damaged.","authors":"Takayama Y, Sato H, Saitoh S, Ogiyama Y, Masuda F, Takahashi K","authors_abbrev":"Takayama Y et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2007-12-14","publication_year":"2008","canto_session_key":"440ff0786082ec49","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-01 22:46:56","canto_approved_date":"2022-11-10 17:35:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-16 17:17:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31F10.13c","SPCC290.04","SPBC4.04c","SPBC1105.17","SPCC18B5.03","SPAC24H6.05"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-03-01"},{"uniquename":"PMID:38482739","title":"Critical importance of DNA binding for CSL protein functions in fission yeast.","citation":"J Cell Sci 2024 Mar 14;","abstract":"CSL (CBF1/RBP-Jκ/Suppressor of Hairless/LAG-1) proteins are conserved transcription factors found in animals and fungi. In fission yeast, they regulate various cellular processes, including cell cycle progression, lipid metabolism, and cell adhesion. CSL proteins bind to DNA through their N-terminal Rel-like domain and central beta-trefoil domain. Here, we investigated the importance of DNA binding for CSL functions in the fission yeast Schizosaccharomyces pombe. We created CSL mutants with disrupted DNA binding and found that the vast majority of CSL functions depend on intact DNA binding. Specifically, DNA binding is crucial for the regulation of cell adhesion, lipid metabolism, cell cycle progression, long non-coding RNA expression, and genome integrity maintenance. Interestingly, perturbed lipid metabolism leads to chromatin structure changes, potentially linking lipid metabolism to the diverse CSL-associated phenotypes. Our study highlights the critical role of DNA binding for CSL protein functions in fission yeast.","doi":"10.1242/jcs.261568","authors":"Marešová A, Oravcová M, Rodríguez-López M, Hradilová M, Zemlianski V, Häsler R, Hernández P, Bähler J, Převorovský M","authors_abbrev":"Marešová A et al.","pubmed_publication_date":"14 Mar 2024","pubmed_entrez_date":"2024-03-14","publication_year":"2024","canto_session_key":"3b3bb128e7747bc0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Anna Marešová","canto_first_approved_date":"2024-08-02 09:36:06","canto_approved_date":"2024-08-15 14:53:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-30 15:08:19","canto_added_date":"2024-03-15 00:25:05","annotation_curators":[{"name":"Anna Marešová","community_curator":true,"annotation_count":48,"orcid":"0000-0003-0864-7231","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":30,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1281.06c","SPAC22A12.06c","SPCC736.08","SPAC1B3.16c","SPBC359.04c","SPCC1450.16c","SPBP4H10.11c","SPCC1742.01","SPCC1235.02","SPAC56E4.04c","SPCC1223.13","SPBC18H10.02","SPBC1198.11c","SPAC4A8.11c","SPAPB15E9.01c"],"gene_count":15,"ltp_gene_count":4,"approved_date":"2024-08-02"},{"uniquename":"PMID:23755176","title":"Proper microtubule structure is vital for timely progression through meiosis in fission yeast.","citation":"PLoS One 2013;8(6):e65082","abstract":"Cells of the fission yeast Schizosaccharomyces pombe normally reproduce by mitotic division in the haploid state. When subjected to nutrient starvation, two haploid cells fuse and undergo karyogamy, forming a diploid cell that initiates meiosis to form four haploid spores. Here, we show that deletion of the mal3 gene, which encodes a homolog of microtubule regulator EB1, produces aberrant asci carrying more than four spores. The mal3 deletion mutant cells have a disordered cytoplasmic microtubule structure during karyogamy and initiate meiosis before completion of karyogamy, resulting in twin haploid meiosis in the zygote. Treatment with anti-microtubule drugs mimics this phenotype. Mutants defective in karyogamy or mutants prone to initiate haploid meiosis exaggerate the phenotype of the mal3 deletion mutant. Our results indicate that proper microtubule structure is required for ordered progression through the meiotic cycle. Furthermore, the results of our study suggest that fission yeast do not monitor ploidy during meiosis.","doi":"10.1371/journal.pone.0065082","authors":"Yamashita A, Fujita Y, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-06-12","publication_year":"2013","canto_session_key":"0909a015627ab393","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-09-08 15:34:23","canto_approved_date":"2022-07-15 08:26:05","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2013-12-28 13:09:15","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPAC27D7.13c","SPAC18G6.15","SPCC417.07c","SPBC19C2.05"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-09-08"},{"uniquename":"PMID:31533287","title":"meiRNA, A Polyvalent Player in Fission Yeast Meiosis.","citation":"Noncoding RNA 2019 Sep 17;5(3)","abstract":"A growing number of recent studies have revealed that non-coding RNAs play a wide variety of roles beyond expectation. A lot of non-coding RNAs have been shown to function by forming intracellular structures either in the nucleus or the cytoplasm. In the fission yeast  Schizosaccharomyces pombe , a non-coding RNA termed meiRNA has been shown to play multiple vital roles in the course of meiosis. meiRNA is tethered to its genetic locus after transcription and forms a peculiar intranuclear dot structure. It ensures stable expression of meiotic genes in cooperation with an RNA-binding protein Mei2. Chromosome-associated meiRNA also facilitates recognition of homologous chromosome loci and induces robust pairing. In this review, the quarter-century history of meiRNA, from its identification to functional characterization, will be outlined.","doi":"10.3390/ncrna5030045","authors":"Yamashita A","authors_abbrev":"Yamashita A","pubmed_publication_date":"17 Sep 2019","pubmed_entrez_date":"2019-09-20","publication_year":"2019","canto_session_key":"219aab1033a5c38b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-08 12:04:15","canto_approved_date":"2019-11-08 12:04:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-08 12:04:09","canto_added_date":"2019-09-21 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPNCRNA.103"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-11-08"},{"uniquename":"PMID:26122634","title":"The essential function of Rrs1 in ribosome biogenesis is conserved in budding and fission yeasts.","citation":"Yeast 2015 Sep;32(9):607-14","abstract":"The Rrs1 protein plays an essential role in the biogenesis of 60S ribosomal subunits in budding yeast (Saccharomyces cerevisiae). Here, we examined whether the fission yeast (Schizosaccharomyces pombe) homologue of Rrs1 also plays a role in ribosome biogenesis. To this end, we constructed two temperature-sensitive fission yeast strains, rrs1-D14/22G and rrs1-L51P, which had amino acid substitutions corresponding to those of the previously characterized budding yeast rrs1-84 (D22/30G) and rrs1-124 (L61P) strains, respectively. The fission yeast mutants exhibited severe defects in growth and 60S ribosomal subunit biogenesis at high temperatures. In addition, expression of the Rrs1 protein of fission yeast suppressed the growth defects of the budding yeast rrs1 mutants at high temperatures. Yeast two-hybrid analyses revealed that the interactions of Rrs1 with the Rfp2 and Ebp2 proteins were conserved in budding and fission yeasts. These results suggest that the essential function of Rrs1 in ribosome biogenesis may be conserved in budding and fission yeasts.","doi":"10.1002/yea.3083","authors":"Wan K, Kawara H, Yamamoto T, Kume K, Yabuki Y, Goshima T, Kitamura K, Ueno M, Kanai M, Hirata D, Funato K, Mizuta K","authors_abbrev":"Wan K et al.","pubmed_publication_date":"Sep 2015","pubmed_entrez_date":"2015-07-01","publication_year":"2015","canto_session_key":"1ae670cde3faca1e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-07-23 09:10:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-20 11:02:53","canto_added_date":"2015-07-02 00:20:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.16","SPAC926.08c","SPBC800.06","SPAC17H9.05"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-07-20"},{"uniquename":"PMID:22110027","title":"DNAtraffic--a new database for systems biology of DNA dynamics during the cell life.","citation":"Nucleic Acids Res 2012 Jan;40(Database issue):D1235-40","abstract":"DNAtraffic (http://dnatraffic.ibb.waw.pl/) is dedicated to be a unique comprehensive and richly annotated database of genome dynamics during the cell life. It contains extensive data on the nomenclature, ontology, structure and function of proteins related to the DNA integrity mechanisms such as chromatin remodeling, histone modifications, DNA repair and damage response from eight organisms: Homo sapiens, Mus musculus, Drosophila melanogaster, Caenorhabditis elegans, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Escherichia coli and Arabidopsis thaliana. DNAtraffic contains comprehensive information on the diseases related to the assembled human proteins. DNAtraffic is richly annotated in the systemic information on the nomenclature, chemistry and structure of DNA damage and their sources, including environmental agents or commonly used drugs targeting nucleic acids and/or proteins involved in the maintenance of genome stability. One of the DNAtraffic database aim is to create the first platform of the combinatorial complexity of DNA network analysis. Database includes illustrations of pathways, damage, proteins and drugs. Since DNAtraffic is designed to cover a broad spectrum of scientific disciplines, it has to be extensively linked to numerous external data sources. Our database represents the result of the manual annotation work aimed at making the DNAtraffic much more useful for a wide range of systems biology applications.","doi":"10.1093/nar/gkr962","authors":"Kuchta K, Barszcz D, Grzesiuk E, Pomorski P, Krwawicz J","authors_abbrev":"Kuchta K et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2011-11-24","publication_year":"2012","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12109879","title":"Physiological diversity and trehalose accumulation in Schizosaccharomyces pombe strains isolated from spontaneous fermentations during the production of the artisanal Brazilian cachaça.","citation":"Can J Microbiol 2002 May;48(5):399-406","abstract":"Twenty-seven Schizosaccharomyces pombe isolates from seven cachaça distilleries were tested for maximum temperature of growth and fermentation, osmotolerance, ethanol resistance, invertase production, and trehalose accumulation. Two isolates were selected for studies of trehalose accumulation under heat shock and ethanol stress. The S. pombe isolates were also characterized by RAPD-PCR. The isolates were able to grow and ferment at 41 degrees C, resisted concentrations of 10% ethanol, and grew on 50% glucose medium. Four isolates yielded invertase activity of more than 100 micromol of reducing sugar x mg(-1) x min(-1). The S. pombe isolates were able to accumulate trehalose during stationary phase. Two isolates, strains UFMG-A533 and UFMG-A1000, submitted to a 15 min heat shock, were able to accumulate high trehalose levels. Strain UFMG-A533 had a marked reduction in viability during heat shock, but strain UFMG-A1000 preserved a viability rate of almost 20% after 15 min at 48 degrees C. No clear correlation was observed between trehalose accumulation and cell survival during ethanol stress. Strain UFMG-A1000 had higher trehalose accumulation levels than strain UFMG-A533 under conditions of combined heat treatment and ethanol stress. Molecular analysis showed that some strains are maintained during the whole cachaça production period; using the RAPD-PCR profiles, it was possible to group the isolates according to their isolation sites.","authors":"Gomes FC, Pataro C, Guerra JB, Neves MJ, Corrêa SR, Moreira ES, Rosa CA","authors_abbrev":"Gomes FC et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-07-12","publication_year":"2002","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11809834","title":"Fission yeast F-box protein Pof3 is required for genome integrity and telomere function.","citation":"Mol Biol Cell 2002 Jan;13(1):211-24","abstract":"The Skp1-Cullin-1/Cdc53-F-box protein (SCF) ubiquitin ligase plays an important role in various biological processes. In this enzyme complex, a variety of F-box proteins act as receptors that recruit substrates. We have identified a fission yeast gene encoding a novel F-box protein Pof3, which contains, in addition to the F-box, a tetratricopeptide repeat motif in its N terminus and a leucine-rich-repeat motif in the C terminus, two ubiquitous protein-protein interaction domains. Pof3 forms a complex with Skp1 and Pcu1 (fission yeast cullin-1), suggesting that Pof3 functions as an adaptor for specific substrates. In the absence of Pof3, cells exhibit a number of phenotypes reminiscent of genome integrity defects. These include G2 cell cycle delay, hypersensitivity to UV, appearance of lagging chromosomes, and a high rate of chromosome loss. pof3 deletion strains are viable because the DNA damage checkpoint is continuously activated in the mutant, and this leads to G2 cell cycle delay, thereby preventing the mutant from committing lethal mitosis. Pof3 localizes to the nucleus during the cell cycle. Molecular analysis reveals that in this mutant the telomere is substantially shortened and furthermore transcriptional silencing at the telomere is alleviated. The results highlight a role of the SCF(Pof3) ubiquitin ligase in genome integrity via maintaining chromatin structures.","authors":"Katayama S, Kitamura K, Lehmann A, Nikaido O, Toda T","authors_abbrev":"Katayama S et al.","pubmed_publication_date":"Jan 2002","pubmed_entrez_date":"2002-01-26","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC14C4.13","SPAC17G6.12","SPBC409.05","SPBC216.05","SPBC660.14","SPCC338.16","SPAC9E9.08","SPCC18B5.03","SPBC342.05","SPCC18B5.11c","SPAC1952.07","SPCC1259.13"],"gene_count":13,"ltp_gene_count":13},{"uniquename":"PMID:958201","title":"Genetic control of the cell division cycle in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1976 Jul 23;146(2):167-78","abstract":"Twenty seven recessive temperature sensitive mutants have been isolated in Schizosaccharomyces pombe which are unable to complete the cell division cycle at the restrictive temperature. These mutants define 14 unlinked genes which are involved in DNA synthesis, nuclear division and cell plate formation. The products from most of these genes complete their function just before the cell cycle event in which they are involved. Physiological characterisation of the mutants has shown that DNA synthesis and nuclear division form a cycle of mutually dependent events which can operate in the absence of cell plate formation. Cell plate formation itself is usually dependent upon the completion of nuclear division.","authors":"Nurse P, Thuriaux P, Nasmyth K","authors_abbrev":"Nurse P et al.","pubmed_publication_date":"23 Jul 1976","pubmed_entrez_date":"1976-07-23","publication_year":"1976","canto_session_key":"2598fac4f5efa38a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ryoko Mandeville","canto_first_approved_date":"2015-09-16 13:24:47","canto_approved_date":"2026-01-30 15:00:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-15 16:22:47","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[{"name":"Ryoko Mandeville","community_curator":true,"annotation_count":23,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.11c","SPAC4A8.15c","SPBC336.04","SPBC336.12c","SPAC644.12","SPAC20G8.05c","SPAP8A3.08","SPAC27F1.02c","SPBC21B10.05c","SPBC24C6.07","SPAC27E2.05","SPAC1F5.04c","SPBC11B10.09","SPBC582.03"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2015-09-16"},{"uniquename":"PMID:16420355","title":"Synthesis of alpha-glucans in fission yeast spores is carried out by three alpha-glucan synthase paralogues, Mok12p, Mok13p and Mok14p.","citation":"Mol Microbiol 2006 Feb;59(3):836-53","abstract":"Fission yeast possesses a family of (1,3)-alpha-glucan synthase-related genes; one of them, mok1+/ags1+, plays an essential function in morphogenesis during vegetative growth. Here we show that three mok1+ paralogues -mok12+, mok13+ and mok14+- are required for sporulation to succeed, acting at different stages of the spore wall maturation process. Mutation of mok12+ affected the efficiency of spore formation and spore viability. Deletion of mok13+ does not affect spore viability but the spores showed reduced resistance to stress conditions. mok14Delta mutant spores failed to accumulate the amylose-like spore wall-specific polymer. mok12+, mok13+ and mok14+ expression was restricted to sporulating cells and the proteins localized to the spore envelope but with different timing. mok11+ was also induced during the sporulation process although its deletion did not show apparently a sporulation defect. In vegetative cells, beta-glucans are more abundant than alpha-glucans (55% versus 28%). In spores, the situation was the opposite, alpha-glucans accounted for 46% while beta-glucans were approximately 38% of the total polysaccharides. We found at least two types of alpha-glucan polymers, Mok12p and Mok13p, were involved in the synthesis of the greater part of alpha-glucan in the spores envelope, a polymer that is mainly digested with alpha-1,3 glucanase, while Mok14p, homologous to starch synthases, was required for the synthesis of the iodine-reactive polymer that is made of alpha-1,4 glucose residues.","authors":"García I, Tajadura V, Martín V, Toda T, Sánchez Y","authors_abbrev":"García I et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-01-20","publication_year":"2006","canto_session_key":"5e96383ce64d7245","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-10-21 14:16:37","canto_approved_date":"2026-01-03 19:50:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-04 17:56:32","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":76,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.05","SPCC63.04","SPCC1281.01","SPAC1527.01","SPBC32H8.13c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-10-21"},{"uniquename":"PMID:33404291","title":"Did evolution choose Atg11 as the scaffolding platform beyond selective autophagy?","citation":"Autophagy 2021 Apr;17(4):835-836","abstract":"It has been well established that Atg11 plays a critical role in selective macroautophagy/autophagy, but not in nonselective autophagy in the budding yeast  Saccharomyces cerevisiae . However, its mammalian ortholog RB1CC1/FIP200 is indispensable for both types of autophagy, and the molecular mechanism behind its function is a mystery. Recently, Pan et al. showed that in the fission yeast  Schizosaccharomyces pombe , Atg11 could also promote nonselective autophagy via activation of Atg1 kinase. These results prompt an interesting idea that Atg11 might have gained an additional ability to mediate nonselective autophagy through evolution.","doi":"10.1080/15548627.2021.1872176","authors":"Huang YJ, Klionsky DJ","authors_abbrev":"Huang YJ et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2021-01-06","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-01-08 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8918598","title":"Characteristics of 26 S proteases from fission yeast mutants, which arrest in mitosis.","citation":"J Mol Biol 1996 Nov 01;263(3):423-31","abstract":"We have isolated the 26 S protease from the fission yeast Schizosaccharomyces pombe. The affinity-purified enzyme contains the two regulatory ATPases mts2+, a homolog of human S4, and CIM5, a homolog of human MSS1 = S7. We show that mts3+, a homolog of the budding yeast NIN1 protein and human S14, is a true component of the 19 S regulatory complex from the fission yeast. The 26 S proteases purified from two thermosensitive mutants, mts2-1 and mts3-1, which arrest in cell cycle at the restrictive temperature (37 degrees C), have been compared with the wild-type enzyme after growing cells at permissive (25 degrees C) and non-permissive temperatures. We demonstrate that mutated mts2 protein is integrated into the protease complex prepared from mts2 cells, whereas mutated mts3 is not present in the 19 S regulatory complex from mts3 cells. The two mutant 26 S proteases isolated after growing cells at 37 degrees C remain stable for two hours at 37 degrees C as measured by ATP-dependent cleavage of the fluorogenic peptide sucLLVY-MCA. At the restrictive temperature, the mutant 26 S proteases do not degrade ubiquitin-[125I]lysozyme conjugates in an ATP-dependent manner, indicating that mts2+ and mts3+ are essential for ubiquitin conjugate degradation. This explains the conditional lethality of the mutants and the cell-cycle arrest in metaphase to anaphase transition. In addition, our data demonstrate that the ATPases of the 26 S enzyme are not redundant.","authors":"Seeger M, Gordon C, Ferrell K, Dubiel W","authors_abbrev":"Seeger M et al.","pubmed_publication_date":"01 Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_session_key":"6f2c464590b4ee1b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-05-18 15:18:08","canto_approved_date":"2019-05-18 15:18:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-17 19:31:38","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16G5.01","SPBC4.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-05-18"},{"uniquename":"PMID:17464066","title":"Transduction of centrifugation-induced gravity forces through mitogen-activated protein kinase pathways in the fission yeast Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 2007 May;153(Pt 5):1519-1529","abstract":"Centrifugation of cells of Schizosaccharomyces pombe in liquid medium prompted a marked activation of Sty1 and Pmk1, which are the effector mitogen-activated protein kinases (MAPKs) of the stress-activated protein kinase pathway and the cell-integrity pathway, respectively. Transduction of the centrifugation signals showed a sensitivity threshold above which the response was dependent on time and temperature. Centrifugation-induced phosphorylation of Sty1 and Pmk1 required the presence of the main functional components of the respective signalling cascades, i.e. Wak1 or Win1 plus Wis1, and Mkh1 plus Pek1. The transcription factor Atf1 also became phosphorylated in a Sty1-dependent way upon centrifugation. Hypergravity was an important factor in the activation of Sty1 induced by centrifugation, whilst activation of Pmk1 was mostly due to gravity-associated shear forces. Centrifugation did not increase cell survival against other stresses. Rather, the increased gravitational forces produced a delay in the cell cycle, probably related to alterations in the actin-polarization pattern. Phosphorylation of the MAPK Sty1 was needed for the depolarization of actin patches induced by the centrifugation stress.","doi":"10.1099/mic.0.2006/004283-0","authors":"Soto T, Núñez A, Madrid M, Vicente J, Gacto M, Cansado J","authors_abbrev":"Soto T et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-04-28","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:13992377","title":"[Nuclear division in Schizosaccharomyces pombe].","citation":"Arch Mikrobiol 1963;45:304-13","abstract":"","authors":"SCHOPFER WH, WUSTENFELD D, TURIAN G","authors_abbrev":"SCHOPFER WH et al.","pubmed_publication_date":"1963","pubmed_entrez_date":"1963-01-01","publication_year":"1963","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33113963","title":"Transient Breakage of the Nucleocytoplasmic Barrier Controls Spore Maturation via Mobilizing the Proteasome Subunit Rpn11 in the Fission Yeast  Schizosaccharomyces pombe .","citation":"J Fungi (Basel) 2020 Oct 23;6(4)","abstract":"Forespore membrane (FSM) closure is a process of specialized cytokinesis in yeast meiosis. FSM closure begins with the contraction of the FSM opening and finishes with the disassembly of the leading-edge proteins (LEPs) from the FSM opening. Here, we show that the FSM opening starts to contract when the event of virtual nuclear envelope breakdown (vNEBD) occurs in anaphase II of the fission yeast  Schizosaccharomyces pombe . The occurrence of vNEBD controls the redistribution of the proteasomal subunit Rpn11 from the nucleus to the cytosol. To investigate the importance of Rpn11 re-localization during vNEBD, Rpn11 was sequestered at the inner nuclear membrane by fusion with the transmembrane region of Bqt4 (Rpn11-GFP-INM). Remarkably, in the absence of endogenous  rpn11  + , the cells carrying Rpn11-GFP-INM had abnormal or no spore formation. Live-cell imaging analysis further reveals that the FSM opening failed to contract when vNEBD occurred, and the LEP Meu14 was persistently present at the FSM in the  rpn11-gfp- INM cells. The results suggest that the dynamic localization of Rpn11 during vNEBD is essential for spore development.","doi":"10.3390/jof6040242","authors":"Yang HJ, Asakawa H, Ohtsuki C, Haraguchi T, Hiraoka Y","authors_abbrev":"Yang HJ et al.","pubmed_publication_date":"23 Oct 2020","pubmed_entrez_date":"2020-10-29","publication_year":"2020","canto_session_key":"6b80d639d6d96756","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-10-31 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1347.03","SPAC31G5.13"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:22167310","title":"Synthesis and bioactive studies of complex 8-hydroxyquinolinato-bis-(salicylato) yttrium (III).","citation":"Biol Trace Elem Res 2012 Jun;147(1-3):366-73","abstract":"This paper reports the synthesis of a new bioactive complex, 8-hydroxyquinolinato-bis-(salicylato) yttrium (III) (HSAY), whose composition and structure were characterized by elemental analysis, IR spectra, thermogravimetric analysis, and X-ray diffraction. The power-time curves of the compounds HSAY, C(7)H(6)O(3), C(9)H(7)NO, and YCl(3)·6H(2)O on the growth metabolism of Schizosaccharomyces pombe (S. pombe) were determined at 32.00°C, respectively. The corresponding thermokinetics parameters, which include the microbial growth rate constant (κ), inhibition ratio (I), and half inhibition concentration (IC(50)), were also derived. The results showed that the generation time was 168.2 min, and all the compounds HSAY, C(7)H(6)O(3), C(9)H(7)NO, and YCl(3)·6H(2)O possessed good bioactivities on the growth metabolism of S. pombe, with the values of IC(50) being 0.055, 3.57, 0.057, and 1.35 mmol L(-1), respectively. The inhibition ability of these compounds above on the growth of the S. pombe has been observed to decrease in the order HSAY>C(9)H(7)NO>YCl(3)·6H(2)O>C(7)H(6)O(3).","doi":"10.1007/s12011-011-9297-1","authors":"Li X, Li QG, Zhang H, Hu JL, Yao FH, Yang DJ, Xiao SX, Ye LJ, Huang Y, Guo DC","authors_abbrev":"Li X et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2011-12-15","publication_year":"2012","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28208632","title":"Cross-Talk between Dnmt2-Dependent tRNA Methylation and Queuosine Modification.","citation":"Biomolecules 2017 Feb 10;7(1)","abstract":"Enzymes of the Dnmt2 family of methyltransferases have yielded a number of unexpected discoveries. The first surprise came more than ten years ago when it was realized that, rather than being DNA methyltransferases, Dnmt2 enzymes actually are transfer RNA (tRNA) methyltransferases for cytosine-5 methylation, foremost C38 (m5C38) of tRNAAsp. The second unanticipated finding was our recent discovery of a nutritional regulation of Dnmt2 in the fission yeast Schizosaccharomyces pombe. Significantly, the presence of the nucleotide queuosine in tRNAAsp strongly stimulates Dnmt2 activity both in vivo and in vitro in S. pombe. Queuine, the respective base, is a hypermodified guanine analog that is synthesized from guanosine-5'-triphosphate (GTP) by bacteria. Interestingly, most eukaryotes have queuosine in their tRNA. However, they cannot synthesize it themselves, but rather salvage it from food or from gut microbes. The queuine obtained from these sources comes from the breakdown of tRNAs, where the queuine ultimately was synthesized by bacteria. Queuine thus has been termed a micronutrient. This review summarizes the current knowledge of Dnmt2 methylation and queuosine modification with respect to translation as well as the organismal consequences of the absence of these modifications. Models for the functional cooperation between these modifications and its wider implications are discussed.","doi":"10.3390/biom7010014","authors":"Ehrenhofer-Murray AE","authors_abbrev":"Ehrenhofer-Murray AE","pubmed_publication_date":"10 Feb 2017","pubmed_entrez_date":"2017-02-18","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-02-19 01:15:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9671485","title":"A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site.","citation":"Mol Cell Biol 1998 Aug;18(8):4752-60","abstract":"Base pairing between U2 snRNA and the branchpoint sequence (BPS) is essential for pre-mRNA splicing. Because the metazoan BPS is short and highly degenerate, this interaction alone is insufficient for specific binding of U2 snRNP. The splicing factor U2AF binds to the pyrimidine tract at the 3' splice site in the earliest spliceosomal complex, E, and is essential for U2 snRNP binding in the spliceosomal complex A. We show that the U2 snRNP protein SAP 155 UV cross-links to pre-mRNA on both sides of the BPS in the A complex. SAP 155's downstream cross-linking site is immediately adjacent to the U2AF binding site, and the two proteins interact directly in protein-protein interaction assays. Using UV cross-linking, together with functional analyses of pre-mRNAs containing duplicated BPSs, we show a direct correlation between BPS selection and UV cross-linking of SAP 155 on both sides of the BPS. Together, our data are consistent with a model in which U2AF binds to the pyrimidine tract in the E complex and then interacts with SAP 155 to recruit U2 snRNP to the BPS.","authors":"Gozani O, Potashkin J, Reed R","authors_abbrev":"Gozani O et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-07-22","publication_year":"1998","canto_session_key":"7924e321b376a76c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-07-02 16:49:07","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-02 16:48:21","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.09c","SPAP8A3.06","SPBC146.07"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-07-02"},{"uniquename":"PMID:22796319","title":"Regulation of patulin-induced oxidative stress processes in the fission yeast Schizosaccharomyces pombe.","citation":"Food Chem Toxicol 2012 Oct;50(10):3792-8","abstract":"Patulin (PAT), is one of the most widely disseminated mycotoxins found in agricultural products. In this study the PAT-induced accumulation of reactive oxygen species (ROS) and the regulation of the specific activities of antioxidant enzymes were investigated in the single cell eukaryotic organism Schizosaccharomyces pombe. In comparison with the untreated cells, 500 μM PAT treatment caused a 43% decrease in the concentration of the main intracellular antioxidant, glutathione (GSH); this depletion of GSH initiated a 2.44- and a 2.6-fold accumulation of superoxide anion and hydrogen peroxide, respectively, but did not increase the concentration of hydroxyl radicals; the reduction of ROS-induced adaptation processes via the activation of Pap1 transcription factor resulted in significantly increased specific activities of Cu/Zn superoxide dismutase, catalase and glutathione S-transferase to protect the cells against the ROS-induced unbalanced redox state. However, no change was measured in the activities of glutathione reductase, glutathione peroxidase and glucose-6-phosphate dehydrogenase. It seems reasonable to assume that the temporary PAT-induced ROS accumulation plays a crucial role in adaptation processes. The adverse effects of PAT may be exerted mainly through the destruction of cellular membranes and protein/enzyme functions.","doi":"10.1016/j.fct.2012.07.001","authors":"Papp G, Horváth E, Mike N, Gazdag Z, Belágyi J, Gyöngyi Z, Bánfalvi G, Hornok L, Pesti M","authors_abbrev":"Papp G et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-07-17","publication_year":"2012","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29146263","title":"Transcription factors Atf1 and Sty1 promote stress tolerance under nitrosative stress in Schizosaccharomyces pombe.","citation":"Microbiol Res 2018 Jan;206:82-90","abstract":"Nitric Oxide (NO) and its associated reactive nitrogen species (RNS) produce nitrosative stress under various pathophysiological conditions in eukaryotes. The fission yeast Schizosaccharomyces pombe regulates stress response mainly through the Sty1-Atf1 MAP Kinase pathway. The present study deals with the role of transcription factor Atf1 and Sty1 in S. pombe under nitrosative stress. In this study, exposure to an NO donor resulted in S-phase slowdown with associated mitotic block in S. pombe. Deletion of sty1 and atf1 in S. pombe had differential growth sensitivity towards NO donor. Both Sty1 and Atf1 were involved in regulating mitotic slowdown in S. pombe under nitrosative stress. Experimental data obtained in this study reveals a novel role of Atf1 in initiating the replication slowdown in S. pombe under nitrosative stress. Both Sty1 and Atf1 were accumulated in the nucleus in S. pombe under nitrosative stress in a concentration and time dependent manner. Atf1 is also found to be nuclear delocalized under longer nitrosative stress.","doi":"10.1016/j.micres.2017.10.002","authors":"Kar P, Biswas P, Patra SK, Ghosh S","authors_abbrev":"Kar P et al.","pubmed_publication_date":"Jan 2018","pubmed_entrez_date":"2017-11-18","publication_year":"2018","canto_session_key":"1746cf4459230be3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-11-19 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC24B11.06c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"GO_REF:0000083","title":"Representation of plant morphogenesis as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the morphogenesis of a plant structure as a biological process. The underlying equivalence axiom template is \"'anatomical structure morphogenesis' and 'results in morphogenesis of' some P\", where P is a plant anatomical entity (PO:0025131).","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18280239","title":"Structural basis of dcp2 recognition and activation by dcp1.","citation":"Mol Cell 2008 Feb 15;29(3):337-49","abstract":"A critical step in mRNA degradation is the removal of the 5' cap structure, which is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of an S. pombe Dcp1p-Dcp2n complex combined with small-angle X-ray scattering analysis (SAXS) reveals that Dcp2p exists in open and closed conformations, with the closed complex being, or closely resembling, the catalytically more active form. This suggests that a conformational change between these open and closed complexes might control decapping. A bipartite RNA-binding channel containing the catalytic site and Box B motif is identified with a bound ATP located in the catalytic pocket in the closed complex, suggesting possible interactions that facilitate substrate binding. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. Notably, the interface of Dcp1 and Dcp2 is not fully conserved, explaining why the Dcp1-Dcp2 interaction in higher eukaryotes requires an additional factor.","doi":"10.1016/j.molcel.2008.01.002","authors":"She M, Decker CJ, Svergun DI, Round A, Chen N, Muhlrad D, Parker R, Song H","authors_abbrev":"She M et al.","pubmed_publication_date":"15 Feb 2008","pubmed_entrez_date":"2008-02-19","publication_year":"2008","canto_session_key":"9787081c65c1aca3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-15 15:09:25","canto_approved_date":"2023-07-05 11:16:40","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2015-10-16 17:44:35","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19A8.12","SPBC3B9.21"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-02-15","pdb_entries":[{"pdb_id":"2qkm","gene_chains":[{"gene_uniquename":"SPAC19A8.12","chain":"B/D/F/H","position":"1-266"},{"gene_uniquename":"SPBC3B9.21","chain":"A/C/E/G","position":"1-127"}],"title":"The crystal structure of fission yeast mRNA decapping enzyme Dcp1-Dcp2 complex","entry_authors":"She M,Song H","entry_authors_abbrev":"She M et al.","reference_uniquename":"PMID:18280239","experimental_method":"X-ray","resolution":"2.8"},{"pdb_id":"2qkl","gene_chains":[{"gene_uniquename":"SPAC19A8.12","chain":"B","position":"1-95"},{"gene_uniquename":"SPBC3B9.21","chain":"A","position":"1-127"}],"title":"The crystal structure of fission yeast mRNA decapping enzyme Dcp1-Dcp2 complex","entry_authors":"She M,Chen N,Song H","entry_authors_abbrev":"She M et al.","reference_uniquename":"PMID:18280239","experimental_method":"X-ray","resolution":"2.33"}]},{"uniquename":"PMID:16835444","title":"Sequential processing of a mitochondrial tandem protein: insights into protein import in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2006 Jul;5(7):997-1006","abstract":"The sequencing of the genome of Schizosaccharomyces pombe revealed the presence of a number of genes encoding tandem proteins, some of which are mitochondrial components. One of these proteins (pre-Rsm22-Cox11) consists of a fusion of Rsm22, a component of the mitochondrial ribosome, and Cox11, a factor required for copper insertion into cytochrome oxidase. Since in Saccharomyces cerevisiae, Cox11 is physically attached to the mitochondrial ribosome, it was suggested that the tandem organization of Rsm22-Cox11 is used to covalently tie the mitochondrial ribosome to Cox11 in S. pombe. We report here that pre-Rsm22-Cox11 is matured in two subsequent processing events. First, the mitochondrial presequence is removed. At a later stage of the import process, the Rsm22 and Cox11 domains are separated by cleavage of the mitochondrial processing peptidase at an internal processing site. In vivo data obtained using a tagged version of pre-Rsm22-Cox11 confirmed the proteolytic separation of Cox11 from the Rsm22 domain. Hence, the tandem organization of pre-Rsm22-Cox11 does not give rise to a persistent fusion protein but rather might be used to increase the import efficiency of Cox11 and/or to coordinate expression levels of Rsm22 and Cox11 in S. pombe.","authors":"Khalimonchuk O, Ott M, Funes S, Ostermann K, Rödel G, Herrmann JM","authors_abbrev":"Khalimonchuk O et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-07-13","publication_year":"2006","canto_session_key":"ec8a5d32e6f2e4be","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1420.04c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:41040388","title":"Discrete Subdomains Establish Epigenetic Diversity in Subtelomeric Heterochromatin.","citation":"bioRxiv 2025 Sep 25;","abstract":"Subtelomeres are imperfect repeats adjacent to telomeres that are repressed by heterochromatin. Although essential for genome integrity, their repetitive nature has thwarted dissection of local heterochromatin assembly and maintenance mechanisms. Here, we engineered  Schizosaccharomyces pombe  strains carrying fluorescent reporters at a single subtelomere. We find that subtelomeric heterochromatin is organized into discrete subdomains that nucleate at telomere-proximal and cryptic internal sites. Telomere-proximal regions depend on canonical shelterin or RNA interference nucleation pathways, while telomere-distal regions require nucleosome remodelers, histone chaperones, and boundary-associated factors. Using multi-generational live imaging and targeted perturbations, we show that subtelomeric subdomains display position-specific, clonally variable silencing across a spectrum of robust to fragile epigenetic states. This clonal variegation is also induced by naturally occurring subtelomeric structural variants. These findings demonstrate that subtelomeric heterochromatin maintenance is not uniform but rather governed by local chromatin context and architecture.","doi":"10.1101/2025.09.25.678047","authors":"Mazumder A, Cooper J, Goksal C, Khanduja JS, Joh RI, Groos JJ, Brockhausen RYJ, Kanoh J, Motamedi M, Finkelstein IJ, Al-Sady B, Braun S","authors_abbrev":"Mazumder A et al.","pubmed_publication_date":"25 Sep 2025","pubmed_entrez_date":"2025-10-03","publication_year":"2025","canto_session_key":"e954588c1f5f277a","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-03 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000090","title":"Automatic creation of relationships between ontology branches in the Gene Ontology","abstract":"We have created a rule-based approach to create relations between the branches of the Gene Ontology. The approach uses the equivalence axioms and a given pattern to create non-subClassOf relationships between the three different branches of the Gene Ontology (biological process, molecular function, cellular component). Currently, there are the following rules: \"'transporter activity' and 'transports_or_maintains_localization_of' some X' -part_of-> \"transport and 'transports_or_maintains_localization_of' some X\"; \"'transmembrane transporter activity' and 'transports_or_maintains_localization_of' some X -part_of-> 'transmembrane transport' and 'transports_or_maintains_localization_of' some X\"","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11274158","title":"Human BIN3 complements the F-actin localization defects caused by loss of Hob3p, the fission yeast homolog of Rvs161p.","citation":"J Biol Chem 2001 Jun 15;276(24):21670-7","abstract":"The BAR adaptor proteins encoded by the RVS167 and RVS161 genes from Saccharomyces cerevisiae form a complex that regulates actin, endocytosis, and viability following starvation or osmotic stress. In this study, we identified a human homolog of RVS161, termed BIN3 (bridging integrator-3), and a Schizosaccharomyces pombe homolog of RVS161, termed hob3+ (homolog of Bin3). In human tissues, the BIN3 gene was expressed ubiquitously except for brain. S. pombe cells lacking Hob3p were often multinucleate and characterized by increased amounts of calcofluor-stained material and mislocalized F-actin. For example, while wild-type cells localized F-actin to cell ends during interphase, hob3Delta mutants had F-actin patches distributed randomly around the cell. In addition, medial F-actin rings were rarely found in hob3Delta mutants. Notably, in contrast to S. cerevisiae rvs161Delta mutants, hob3Delta mutants showed no measurable defects in endocytosis or response to osmotic stress, yet hob3+ complemented the osmosensitivity of a rvs161Delta mutant. BIN3 failed to rescue the osmosensitivity of rvs161Delta, but the actin localization defects of hob3Delta mutants were completely rescued by BIN3 and partially rescued by RVS161. These findings suggest that hob3+ and BIN3 regulate F-actin localization, like RVS161, but that other roles for this gene have diverged somewhat during evolution.","authors":"Routhier EL, Burn TC, Abbaszade I, Summers M, Albright CF, Prendergast GC","authors_abbrev":"Routhier EL et al.","pubmed_publication_date":"15 Jun 2001","pubmed_entrez_date":"2001-03-29","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC725.09c","HGNC:1054"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:1302023","title":"Complete coverage of the Schizosaccharomyces pombe genome in yeast artificial chromosomes.","citation":"Nat Genet 1992 Jul;1(4):273-7","abstract":"The genome of the fission yeast, Schizosaccharomyces pombe, consists of some 14 million base pairs of DNA contained in three chromosomes. On account of its excellent genetics we used it as a test system for a strategy designed to map mammalian chromosomes and genomes. Data obtained from hybridization fingerprinting established an ordered library of 1,248 yeast artificial chromosome clones with an average size of 535 kilobases. The clones fall into three contigs completely representing the three chromosomes of the organism. This work provides a high resolution physical and clone map of the genome, which has been related to available genetic and physical map information.","authors":"Maier E, Hoheisel JD, McCarthy L, Mott R, Grigoriev AV, Monaco AP, Larin Z, Lehrach H","authors_abbrev":"Maier E et al.","pubmed_publication_date":"Jul 1992","pubmed_entrez_date":"1992-07-01","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8423799","title":"Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1993 Feb;13(2):749-61","abstract":"Schizosaccharomyces pombe is becoming an increasingly useful organism for the study of cellular processes, since in certain respects, such as the cell cycle and splicing, it is similar to metazoans. Previous biochemical studies have shown that the DNA binding ability of S. pombe heat shock factor (HSF) is fully induced only under stressed conditions, in a manner similar to that of Drosophila melanogaster and humans but differing from the constitutive binding by HSF in the budding yeasts. We report the isolation of the cDNA and gene for the HSF from S. pombe. S. pombe HSF has a domain structure that is more closely related to the structure of human and D. melanogaster HSFs than to the structure of the budding yeast HSFs, further arguing that regulation of HSF in S. pombe is likely to reflect regulation in metazoans. Surprisingly, the S. pombe HSF gene is required for growth at normal temperatures. We show that the S. pombe HSF gene can be replaced by the D. melanogaster HSF gene and that strains containing either of these genes behave similarly to transiently heat-shocked strains with respect to viability and the level of heat-induced transcripts from heat shock promoters. Strains containing the D. melanogaster HSF gene, however, have lower growth rates and show altered morphology at normal growth temperatures. These data demonstrate the functional conservation of domains of HSF that are required for response to heat shock. They further suggest a general role for HSF in growth of eukaryotic cells under normal (nonstressed) growth conditions.","authors":"Gallo GJ, Prentice H, Kingston RE","authors_abbrev":"Gallo GJ et al.","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_session_key":"fcb4f20b3fcb6424","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-28 13:54:25","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-04 13:38:29","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2E12.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:1849659","title":"A fission-yeast gene encoding a protein with features of protein-tyrosine-phosphatases.","citation":"Proc Natl Acad Sci U S A 1991 Apr 15;88(8):3455-9","abstract":"Degenerate oligonucleotide probes encoding sequences conserved among mammalian protein-tyrosine-phosphatases (PTPases) were used to amplify DNA fragments from a Schizosaccharomyces pombe cDNA library by polymerase chain reaction (PCR) methods. A cloned PCR product predicted peptide sequences similar to those found in PTPases but not identical to any published sequences. A S. pombe gene, designated pyp1+, was identified in a cDNA library with this PCR probe, cloned, and sequenced. The sequence of the gene predicted a 550-amino acid protein with Mr 61,586, which includes amino acid sequences that are highly conserved in mammalian PTPases. Disruption of the pyp1+ gene resulted in viable cells. Overexpression of the pyp1+ gene in S. pombe permitted detection of a protein of apparent Mr 63,000.","authors":"Ottilie S, Chernoff J, Hannig G, Hoffman CS, Erikson RL","authors_abbrev":"Ottilie S et al.","pubmed_publication_date":"15 Apr 1991","pubmed_entrez_date":"1991-04-15","publication_year":"1991","canto_session_key":"7cf72508fd0e1dcb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-20 15:53:14","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-02-16 21:55:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26F1.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-02-16"},{"uniquename":"PMID:20946835","title":"Molecular genetics of Schizosaccharomyces pombe.","citation":"Methods Enzymol 2010;470:759-95","abstract":"In this chapter we present basic protocols for the use of Schizosaccharomyces pombe, commonly known as fission yeast, in molecular biology and genetics research. Fission yeast is an increasingly popular model organism for the study of biological pathways because of its genetic tractability and as a model for metazoan biology. It provides an alternative and complimentary approach to Saccharomyces cerevisiae for addressing questions of cell biology, physiology, genetics, and genomics/proteomics. We include details and considerations for growing fission yeast, information on crosses and genetics, gene targeting and transformation, cell synchrony and analysis, and molecular biology protocols.","doi":"10.1016/S0076-6879(10)70032-X","authors":"Sabatinos SA, Forsburg SL","authors_abbrev":"Sabatinos SA et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2010-10-16","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7926774","title":"pct1+, which encodes a new DNA-binding partner of p85cdc10, is required for meiosis in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Dev 1994 Apr 15;8(8):885-98","abstract":"The transcriptional activation of genes at late G1 is an important regulatory step in the commitment to a new cell division cycle. In Schizosaccharomyces pombe, this regulation is mediated by MCB elements that serve as binding sites for the MBF/DSC-1 complex. The cdc10(+)-encoded protein is a component of this complex. We report the cloning of a new gene, pct1+, encoding a 73-kD protein that interacts with p85cdc10 to form an MCB-binding heteromer. Pct1+ is related to, but distinct from, the res1+/sct1+ gene that also encodes a p85cdc10 partner. p73pct1 has centrally located ankyrin repeats and a putative amino-terminal DNA-binding domain that has extensive sequence similarity to the DNA-binding domains of the Saccharomyces cerevisiae SWI4 and MBP1 proteins. The p73pct1/p85cdc10 complex binds both in vitro and in vivo to MCB but not SCB or E2F sites. Overexpression of pct1+ is sufficient to rescue the growth of the cdc10-129 temperature-sensitive mutant at the restrictive temperature, although it is unable to rescue a cdc10 null mutation. A deletion of pct1+ is not lethal but does result in a severe meiotic defect. Our results indicate that there are two cdc10-containing heteromeric complexes that bind to MCB elements and play differential roles in mitotic division and meiosis.","authors":"Zhu Y, Takeda T, Nasmyth K, Jones N","authors_abbrev":"Zhu Y et al.","pubmed_publication_date":"15 Apr 1994","pubmed_entrez_date":"1994-04-15","publication_year":"1994","canto_session_key":"946a007531b934a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-03 12:04:56","canto_approved_date":"2019-05-27 21:06:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-05 13:57:47","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPAC22F3.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-06-03"},{"uniquename":"PMID:38041528","title":"GetPrimers: A generalized PCR-based genetic targeting primer designer enabling easy and standardized targeted gene modification across multiple systems.","citation":"Yeast 2023 Dec 02;","abstract":"Genetic targeting (e.g., gene knockout and tagging) based on polymerase chain reaction (PCR) is a simple yet powerful approach for studying gene functions. Although originally developed in classic budding and fission yeast models, the same principle applies to other eukaryotic systems with efficient homologous recombination. One-step PCR-based genetic targeting is conventionally used but the sizes of the homologous arms that it generates for recombination-mediated genetic targeting are usually limited. Alternatively, gene targeting can also be performed via fusion PCR, which can create homologous arms that are orders of magnitude larger, therefore substantially increasing the efficiency of recombination-mediated genetic targeting. Here, we present GetPrimers (https://www.evomicslab.org/app/getprimers/), a generalized computational framework and web tool to assist automatic targeting and verification primer design for both one-step PCR-based and fusion PCR-based genetic targeting experiments. Moreover, GetPrimers by design runs for any given genetic background of any species with full genome scalability. Therefore, GetPrimers is capable of empowering high-throughput functional genomic assays at multipopulation and multispecies levels. Comprehensive experimental validations have been performed for targeting and verification primers designed by GetPrimers across multiple organism systems and experimental setups. We anticipate GetPrimers to become a highly useful and popular tool to facilitate easy and standardized gene modification across multiple systems.","doi":"10.1002/yea.3916","authors":"Miao Z, Wang H, Tu X, Huang Z, Huang S, Zhang X, Wang F, Huang Z, Li H, Jiao Y, Gao S, Zhou Z, Shan CM, Li J, Yue JX","authors_abbrev":"Miao Z et al.","pubmed_publication_date":"02 Dec 2023","pubmed_entrez_date":"2023-12-02","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-12-03 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10503548","title":"Analysis of the cps1 gene provides evidence for a septation checkpoint in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1999 Aug;262(1):163-72","abstract":"The fission yeast gene cps1, which encodes the catalytic subunit of beta-glucan synthase, was isolated in a screen for mutants that show an increase in ploidy at the restrictive temperature. cps1 mutants display defects in both polarity and septation at the permissive temperature, and become swollen and multinucleate at the restrictive temperature. Analysis of the interaction of cps1 with other mutations suggests the existence of a septation checkpoint, which requires the activity of the protein kinase weel for function.","authors":"Le Goff X, Woollard A, Simanis V","authors_abbrev":"Le Goff X et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-09-30","publication_year":"1999","canto_session_key":"5205450d9019e784","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-23 10:26:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-02-23 10:26:39","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAP8A3.08","SPBC21.06c","SPAC20G8.05c","SPAC1565.06c","SPBC11B10.09","SPCC1223.06","SPAC27F1.02c","SPBC24C6.07","SPBC19G7.05c","SPCC1739.11c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2015-02-23"},{"uniquename":"PMID:27604537","title":"Genetic Interactions among AMPK Catalytic Subunit Ssp2 and Glycogen Synthase Kinases Gsk3 and Gsk31 in Schizosaccharomyces Pombe.","citation":"Kobe J Med Sci 2016 Aug 03;62(3):E70-8","abstract":"In Schizosaccharomyces pombe, Ssp2, an ortholog of AMP-activated protein kinase (AMPK), is critical for cell growth at restrictive temperatures and under glucose depletion as well as sexual differentiation under nitrogen depletion. To identify genes genetically related to Ssp2, we performed a genetic screening to search for the genes whose overexpression rescued the growth defects in Δssp2 cells at restrictive temperatures, and identified 35 cosmids as multicopy suppressor genes. In Southern blot analyses, 22 out of these cosmids were hybridized to an ssp2+ probe. Using nucleotide sequencing, we identified the gsk3+ gene in one of the cosmids, and the remaining 12 cosmids were hybridized to a gsk3+ probe. Overexpression of the gsk3+ gene or the gsk31+ gene, another GSK3 member, rescues defective growth of Δssp2 cells at restrictive temperatures and under glucose depletion as well as sexual differentiation under nitrogen depletion. Δgsk3Δgsk31 double knockout cells, but neither Δgsk3 nor Δgsk31 single knockout cells, phenocopy Δssp2 cells. The deletion of the gsk3+ or gsk31+ gene augments the phenotypes of Δssp2 cells. These findings suggest that Gsk3 and Gsk31 are critical and interact with Ssp2 in multiple cellular functions.","authors":"Qingyun, Ma Y, Kato T, Furuyashiki T","authors_abbrev":"Qingyun et al.","pubmed_publication_date":"03 Aug 2016","pubmed_entrez_date":"2016-09-09","publication_year":"2016","canto_session_key":"194ff7f0202bb8f7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-10-31 12:19:57","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-01-10 20:33:04","canto_added_date":"2016-09-10 00:15:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.01","SPCC74.03c","SPAC1687.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-01-10"},{"uniquename":"EMBL:AU009216","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9009280","title":"Meiotic nuclear reorganization: switching the position of centromeres and telomeres in the fission yeast Schizosaccharomyces pombe.","citation":"EMBO J 1997 Jan 02;16(1):193-202","abstract":"In fission yeast meiotic prophase, telomeres are clustered near the spindle pole body (SPB; a centrosome-equivalent structure in fungi) and take the leading position in chromosome movement, while centromeres are separated from the SPB. This telomere position contrasts with mitotic nuclear organization, in which centromeres remain clustered near the SPB and lead chromosome movement. Thus, nuclear reorganization switching the position of centromeres and telomeres must take place upon entering meiosis. In this report, we analyze the nuclear location of centromeres and telomeres in genetically well-characterized meiotic mutant strains. An intermediate structure for telomere-centromere switching was observed in haploid cells induced to undergo meiosis by synthetic mating pheromone; fluorescence in situ hybridization revealed that in these cells, both telomeres and centromeres were clustered near the SPB. Further analyses in a series of mutants showed that telomere-centromere switching takes place in two steps; first, association of telomeres with the SPB and, second, dissociation of centromeres from the SPB. The first step can take place in the haploid state in response to mating pheromone, but the second step does not take place in haploid cells and probably depends on conjugation-related events. In addition, a linear minichromosome was also co-localized with authentic telomeres instead of centromeres, suggesting that telomere clustering plays a role in organizing chromosomes within a meiotic prophase nucleus.","authors":"Chikashige Y, Ding DQ, Imai Y, Yamamoto M, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"02 Jan 1997","pubmed_entrez_date":"1997-01-02","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4336550","title":"Dictyosomes in the yeast Schizosaccharomyces pombe.","citation":"Antonie Van Leeuwenhoek 1972;38(1):27-31","abstract":"","authors":"Kopecka M","authors_abbrev":"Kopecka M","pubmed_publication_date":"1972","pubmed_entrez_date":"1972-01-01","publication_year":"1972","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013314","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8193545","title":"MAP kinase kinase kinase, MAP kinase kinase and MAP kinase.","citation":"Curr Opin Genet Dev 1994 Feb;4(1):82-9","abstract":"Signal transduction pathways that respond to external signals through the MAP kinase family of protein kinases are involved in diverse responses in eukaryotic cells. MAP kinases are one element in a series of kinases that serve to connect the plasma membrane with cytoplasmic and nuclear events. MAP kinases have the unusual feature that their activation requires threonine and tyrosine phosphorylation carried out by a dual specificity protein kinase. Recent advances have shown that in two MAP kinase pathways (the mating response pathway in the fission yeast Schizosaccharomyces pombe, and receptor tyrosine kinase signalling), the small GTP binding protein ras p21 links membrane events to kinase pathway activation.","authors":"Marshall CJ","authors_abbrev":"Marshall CJ","pubmed_publication_date":"Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18682565","title":"DNA replication checkpoint promotes G1-S transcription by inactivating the MBF repressor Nrm1.","citation":"Proc Natl Acad Sci U S A 2008 Aug 12;105(32):11230-5","abstract":"The cell cycle transcriptional program imposes order on events of the cell-cycle and is a target for signals that regulate cell-cycle progression, including checkpoints required to maintain genome integrity. Neither the mechanism nor functional significance of checkpoint regulation of the cell-cycle transcription program are established. We show that Nrm1, an MBF-specific transcriptional repressor acting at the transition from G(1) to S phase of the cell cycle, is at the nexus between the cell cycle transcriptional program and the DNA replication checkpoint in fission yeast. Phosphorylation of Nrm1 by the Cds1 (Chk2) checkpoint protein kinase, which is activated in response to DNA replication stress, promotes its dissociation from the MBF transcription factor. This leads to the expression of genes encoding components that function in DNA replication and repair pathways important for cell survival in response to arrested DNA replication.","doi":"10.1073/pnas.0801106105","authors":"de Bruin RA, Kalashnikova TI, Aslanian A, Wohlschlegel J, Chahwan C, Yates JR, Russell P, Wittenberg C","authors_abbrev":"de Bruin RA et al.","pubmed_publication_date":"12 Aug 2008","pubmed_entrez_date":"2008-08-07","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC16A3.07c","SPBC216.05","SPBC336.12c","SPAC22F3.09c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:29735745","title":"Control of mitotic chromosome condensation by the fission yeast transcription factor Zas1.","citation":"J Cell Biol 2018 Jul 02;217(7):2383-2401","abstract":"Although the formation of rod-shaped chromosomes is vital for the correct segregation of eukaryotic genomes during cell divisions, the molecular mechanisms that control the chromosome condensation process have remained largely unknown. Here, we identify the C 2 H 2  zinc-finger transcription factor Zas1 as a key regulator of mitotic condensation dynamics in a quantitative live-cell microscopy screen of the fission yeast  Schizosaccharomyces pombe  By binding to specific DNA target sequences in their promoter regions, Zas1 controls expression of the Cnd1 subunit of the condensin protein complex and several other target genes, whose combined misregulation in  zas1  mutants results in defects in chromosome condensation and segregation. Genetic and biochemical analysis reveals an evolutionarily conserved transactivation domain motif in Zas1 that is pivotal to its function in gene regulation. Our results suggest that this motif, together with the Zas1 C-terminal helical domain to which it binds, creates a cis/trans switch module for transcriptional regulation of genes that control chromosome condensation.","doi":"10.1083/jcb.201711097","authors":"Schiklenk C, Petrova B, Kschonsak M, Hassler M, Klein C, Gibson TJ, Haering CH","authors_abbrev":"Schiklenk C et al.","pubmed_publication_date":"02 Jul 2018","pubmed_entrez_date":"2018-05-09","publication_year":"2018","canto_session_key":"f5cfe860f60d0109","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Christoph Schiklenk","canto_first_approved_date":"2018-06-15 16:43:07","canto_approved_date":"2026-01-29 19:32:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-07-28 19:15:33","canto_added_date":"2018-05-09 00:15:04","annotation_curators":[{"name":"Christoph Schiklenk","community_curator":true,"annotation_count":77,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.06c","SPBC1652.02","SPBC19F5.01c","SPBC13E7.10c","SPAC1565.03","SPBC146.03c","SPBC1198.04c","SPAC6G10.04c","SPBC776.13","SPAC13G7.10","SPBC1289.04c","SPBC609.01","SPAC1B9.03c","SPCC306.03c","SPNCRNA.1321","SPNCRNA.244","SPAC18B11.08c","SPAC644.09","SPBC713.14c","SPAC1039.05c","SPBC887.16","SPAC17H9.16","SPCC188.03","SPAC11E3.09","SPAC3G9.12"],"gene_count":25,"ltp_gene_count":14,"approved_date":"2018-06-15"},{"uniquename":"PMID:10735851","title":"Contribution of base excision repair, nucleotide excision repair, and DNA recombination to alkylation resistance of the fission yeast Schizosaccharomyces pombe.","citation":"J Bacteriol 2000 Apr;182(8):2104-12","abstract":"DNA damage is unavoidable, and organisms across the evolutionary spectrum possess DNA repair pathways that are critical for cell viability and genomic stability. To understand the role of base excision repair (BER) in protecting eukaryotic cells against alkylating agents, we generated Schizosaccharomyces pombe strains mutant for the mag1 3-methyladenine DNA glycosylase gene. We report that S. pombe mag1 mutants have only a slightly increased sensitivity to methylation damage, suggesting that Mag1-initiated BER plays a surprisingly minor role in alkylation resistance in this organism. We go on to show that other DNA repair pathways play a larger role than BER in alkylation resistance. Mutations in genes involved in nucleotide excision repair (rad13) and recombinational repair (rhp51) are much more alkylation sensitive than mag1 mutants. In addition, S. pombe mutant for the flap endonuclease rad2 gene, whose precise function in DNA repair is unclear, were also more alkylation sensitive than mag1 mutants. Further, mag1 and rad13 interact synergistically for alkylation resistance, and mag1 and rhp51 display a surprisingly complex genetic interaction. A model for the role of BER in the generation of alkylation-induced DNA strand breaks in S. pombe is discussed.","authors":"Memisoglu A, Samson L","authors_abbrev":"Memisoglu A et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-03-29","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3E7.08c","SPAPB24D3.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:27325172","title":"A replication-time-controlling sequence element in Schizosaccharomyces pombe.","citation":"Chromosoma 2017 Aug;126(4):465-471","abstract":"Eukaryotic replication origins are highly variable in their activity and replication timing. The nature and role of cis-acting regulatory sequences that control chromosomal replication timing is not well defined. In the fission yeast, Schizosaccharomyces pombe, a 200-bp late-replication-enforcing element (LRE), has been shown to enforce late replication of ARS elements in plasmids. Here, we show that a short (133-bp) fragment of the LRE (shLRE) is required for causing late replication of adjoining origins in its native as well as in an ectopic early-replicating chromosomal location. Active from both sides of an early-replicating origin, the shLRE is a bona fide cis-acting regulatory element that imposes late replication timing in the chromosome.","doi":"10.1007/s00412-016-0606-5","authors":"Tripathi VP, Dubey DD","authors_abbrev":"Tripathi VP et al.","pubmed_publication_date":"Aug 2017","pubmed_entrez_date":"2016-06-22","publication_year":"2017","canto_session_key":"4dffe39683cc9b13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-16 16:57:15","canto_approved_date":"2019-01-16 16:57:15","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-01-11 22:46:03","canto_added_date":"2016-06-23 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-16"},{"uniquename":"PMID:762020","title":"Uncontrolled septation in a cell division cycle mutant of the fission yeast Schizosaccharomyces pombe.","citation":"J Bacteriol 1979 Jan;137(1):440-6","abstract":"A temperature-sensitive Schizosaccharomyces pombe mutant, cdc16-116, has been isolated which undergoes uncontrolled septation during its cell division cycle. The mutant accumulates two types of cells after 3 h of growth at the restrictive temperature: (i) type I cells (85% of the population), which complete nuclear division and then form up to five septa between the divided nuclei; and (ii) type II cells (15% of the population), which form an asymmetrically situated septum in the absence of any nuclear division. cdc16-116 is a monogenic recessive mutation unlinked to any previously known cdc gene of S. pombe. It is not affected in a previously reported control by which septation is dependent upon completion of nuclear division. We propose the cdc16-116 is unable to complete septum formation and proceed to cell separation and is also defective in a control which prevents the manufacture of more than one septum in each cell cycle.","authors":"Minet M, Nurse P, Thuriaux P, Mitchison JM","authors_abbrev":"Minet M et al.","pubmed_publication_date":"Jan 1979","pubmed_entrez_date":"1979-01-01","publication_year":"1979","canto_session_key":"e790f3050bf01b42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ryoko Mandeville","canto_approved_date":"2016-02-09 17:48:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-04-30 12:57:08","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[{"name":"Ryoko Mandeville","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.05c","SPBC11B10.09","SPAC6F6.08c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2013-04-30"},{"uniquename":"PMID:24997422","title":"The role of frataxin in fission yeast iron metabolism: implications for Friedreich's ataxia.","citation":"Biochim Biophys Acta 2014 Oct;1840(10):3022-33","abstract":"The neurodegenerative disease Friedreich's ataxia is the result of frataxin deficiency. Frataxin is a mitochondrial protein involved in iron-sulfur cluster (Fe-S) cofactor biogenesis, but its functional role in this pathway is debated. This is due to the interconnectivity of iron metabolic and oxidative stress response pathways that make distinguishing primary effects of frataxin deficiency challenging. Since Fe-S cluster assembly is conserved, frataxin overexpression phenotypes in a simple eukaryotic organism will provide additional insight into frataxin function.\nThe Schizosaccharomyces pombe frataxin homologue (fxn1) was overexpressed from a plasmid under a thiamine repressible promoter. The S. pombe transformants were characterized at several expression strengths for cellular growth, mitochondrial organization, iron levels, oxidative stress, and activities of Fe-S cluster containing enzymes.\nObserved phenotypes were dependent on the amount of Fxn1 overexpression. High Fxn1 overexpression severely inhibited S. pombe growth, impaired mitochondrial membrane integrity and cellular respiration, and led to Fxn1 aggregation. Cellular iron accumulation was observed at moderate Fxn1 overexpression but was most pronounced at high levels of Fxn1. All levels of Fxn1 overexpression up-regulated oxidative stress defense and mitochondrial Fe-S cluster containing enzyme activities.\nDespite the presence of oxidative stress and accumulated iron, activation of Fe-S cluster enzymes was common to all levels of Fxn1 overexpression; therefore, Fxn1 may regulate the efficiency of Fe-S cluster biogenesis in S. pombe.\nWe provide evidence that suggests that dysregulated Fe-S cluster biogenesis is a primary effect of both frataxin overexpression and deficiency as in Friedreich's ataxia.","doi":"10.1016/j.bbagen.2014.06.017","authors":"Wang Y, Wang Y, Marcus S, Busenlehner LS","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-07-06","publication_year":"2014","canto_session_key":"d8f2845f7d04fc0b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-20 17:30:21","canto_approved_date":"2022-02-07 15:19:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-20 17:30:08","canto_added_date":"2014-07-07 00:15:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21D10.11c","SPAC140.01","SPAC24C9.06c","SPCC1183.03c","SPBC13G1.06c","SPAC821.10c","SPAC227.13c"],"gene_count":7,"ltp_gene_count":1,"approved_date":"2016-01-20"},{"uniquename":"PMID:7548843","title":"Elements of chromosome structure and function in fission yeast.","citation":"Semin Cell Biol 1995 Apr;6(2):55-64","abstract":"The investigation of fission yeast chromosome structure and function has moved rapidly over the past 10 years. The isolation of replication origins, telomeres and centromeres has allowed the development of minichromosomes, a yeast artificial chromosome (YAC)-like cloning system and investigations into chromosome segregation and behaviour during mitosis and meiosis. Many mutants have been isolated which are defective in chromosome segregation. The development of the fluorescent in-situ hybridization (FISH) technique for use in S. pombe has allowed the localization of centromeres and telomeres throughout mitosis and meiosis. In combination with indirect immunofluorescence to detect spindle and chromosomal proteins, the FISH technique should further advance our understanding of fission yeast chromosome structure and function. The recent discovery of a heterochromatin-like structure mediating transcriptional repression at centromeres reinforces the notion that fission yeast centromeres are similar to those of larger eukaryotes. Further characterization of such phenomena will accelerate the genetic dissection of this important chromosomal element.","authors":"Allshire RC","authors_abbrev":"Allshire RC","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8688826","title":"Cyclin B (p56cdc13) localization in the yeast Schizosaccharomyces pombe: an ultrastructural and immunocytochemical study.","citation":"Biol Cell 1996;86(1):1-10","abstract":"The eucaryote cell cycle is driven by a set of cyclin dependent kinases (CDKs) associated to cyclins, which confer not only the activity but also the substrate specificity and the proper localization of the kinase activity. In the fission yeast Schizosaccharomyces pombe, only one cyclin, the product of the cdc13 gene (p56cdc13), is required to be associated with p34cdc2, to control the complete cell cycle. Earlier studies have localized this complex mainly in the nucleus and its periphery. Using new improved electron microscopy (EM) technologies, based on high pressure freezing fixation, we refined previous studies, evidencing cytoplasmic localization of p56cdc13, in addition to the nuclear localization previously observed. Further immunofluorescence studies, performed on aldehydically fixed cells, confirmed our EM results, emphasizing the major cytoplasmic localization of p56cdc13 in interphase cells and the relocalization towards the nucleus in mitotic cells, suggesting that the S pombe cyclin B localization is cell cycle-regulated.","authors":"Audit M, Barbier M, Soyer-Gobillard MO, Albert M, Géraud ML, Nicolas G, Lenaers G","authors_abbrev":"Audit M et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"a0eb5775b3ce7599","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-21 18:24:47","canto_approved_date":"2025-09-02 21:22:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-06 17:47:25","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-04-21"},{"uniquename":"PMID:11309419","title":"A mechanism for nuclear positioning in fission yeast based on microtubule pushing.","citation":"J Cell Biol 2001 Apr 16;153(2):397-411","abstract":"The correct positioning of the nucleus is often important in defining the spatial organization of the cell, for example, in determining the cell division plane. In interphase Schizosaccharomyces pombe cells, the nucleus is positioned in the middle of the cylindrical cell in an active microtubule (MT)-dependent process. Here, we used green fluorescent protein markers to examine the dynamics of MTs, spindle pole body, and the nuclear envelope in living cells. We find that interphase MTs are organized in three to four antiparallel MT bundles arranged along the long axis of the cell, with MT plus ends facing both the cell tips and minus ends near the middle of the cell. The MT bundles are organized from medial MT-organizing centers that may function as nuclear attachment sites. When MTs grow to the cell tips, they exert transient forces produced by plus end MT polymerization that push the nucleus. After an average of 1.5 min of growth at the cell tip, MT plus ends exhibit catastrophe and shrink back to the nuclear region before growing back to the cell tip. Computer modeling suggests that a balance of these pushing MT forces can provide a mechanism to position the nucleus at the middle of the cell.","authors":"Tran PT, Marsh L, Doye V, Inoué S, Chang F","authors_abbrev":"Tran PT et al.","pubmed_publication_date":"16 Apr 2001","pubmed_entrez_date":"2001-04-20","publication_year":"2001","canto_session_key":"9910aceebe8f3bcc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-10-04 18:35:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-04 18:35:01","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16A3.15c","SPBC800.05c","SPBC26H8.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-10-04"},{"uniquename":"PMID:15889139","title":"RMI1/NCE4, a suppressor of genome instability, encodes a member of the RecQ helicase/Topo III complex.","citation":"EMBO J 2005 Jun 01;24(11):2024-33","abstract":"SGS1 encodes a DNA helicase whose homologues in human cells include the BLM, WRN, and RECQ4 genes, mutations in which lead to cancer-predisposition syndromes. Clustering of synthetic genetic interactions identified by large-scale genetic network analysis revealed that the genetic interaction profile of the gene RMI1 (RecQ-mediated genome instability, also known as NCE4 and YPL024W) was highly similar to that of SGS1 and TOP3, suggesting a functional relationship between Rmi1 and the Sgs1/Top3 complex. We show that Rmi1 physically interacts with Sgs1 and Top3 and is a third member of this complex. Cells lacking RMI1 activate the Rad53 checkpoint kinase, undergo a mitotic delay, and display increased relocalization of the recombination repair protein Rad52, indicating the presence of spontaneous DNA damage. Consistent with a role for RMI1 in maintaining genome integrity, rmi1Delta cells exhibit increased recombination frequency and increased frequency of gross chromosomal rearrangements. In addition, rmi1Delta strains fail to fully activate Rad53 upon exposure to DNA-damaging agents, suggesting that Rmi1 is also an important part of the Rad53-dependent DNA damage response.","authors":"Chang M, Bellaoui M, Zhang C, Desai R, Morozov P, Delgado-Cruzata L, Rothstein R, Freyer GA, Boone C, Brown GW","authors_abbrev":"Chang M et al.","pubmed_publication_date":"01 Jun 2005","pubmed_entrez_date":"2005-05-13","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.03c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:1315954","title":"Random mutagenesis of Schizosaccharomyces pombe SRP RNA: lethal and conditional lesions cluster in presumptive protein binding sites.","citation":"Nucleic Acids Res 1992 Apr 11;20(7):1607-15","abstract":"Signal recognition particle (SRP), a ribonucleoprotein composed of six polypeptides and one RNA subunit, serves as an adaptor between the cytoplasmic protein synthetic machinery and the translocation apparatus of the endoplasmic reticulum. To begin constructing a functional map of the 7SL RNA component of SRP, we extensively mutagenized the Schizosaccharomyces pombe SRP7 gene. Phenotypes are reported for fifty-two mutant alleles derived from random point mutagenesis, seven alleles created by site-directed mutagenesis to introduce restriction sites into the SRP7 gene, nine alleles designed to pinpoint conditional lesions, and three alleles with extra nucleotides inserted at position 84. Our data indicate that virtually all single nucleotide changes as well as many multiple substitutions in this highly structured RNA are phenotypically silent. Six lethal alleles and eleven which result in sensitivity to the combination of high temperature and elevated osmotic strength were identified. These mutations cluster in conserved regions which, in the mammalian RNA, are protected from nucleolytic agents by SRP proteins. The effects of mutations in the presumptive binding site for a fission yeast SRP 9/14 homolog indicate that both the identity of a conserved residue and the secondary structure within which it is embedded are functionally important. The phenotypes of mutations in Domain IV suggest particular residues as base-specific contacts for the fission yeast SRP54 protein. A single allele which confers temperature-sensitivity in the absence of osmotic perturbants was identified in this study; the growth properties of the mutant strain suggest that the encoded RNA is somewhat defective even at the permissive temperature, and is most likely unable to correctly assemble with SRP proteins at the nonpermissive temperature.","authors":"Liao X, Selinger D, Althoff S, Chiang A, Hamilton D, Ma M, Wise JA","authors_abbrev":"Liao X et al.","pubmed_publication_date":"11 Apr 1992","pubmed_entrez_date":"1992-04-11","publication_year":"1992","canto_session_key":"ea830c655401d75d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-09 13:03:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-09 13:03:17","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":139,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_1315954_phaf.tsv"}],"genes":["SPNCRNA.98"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-09"},{"uniquename":"EMBL:AF087837","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19452197","title":"What was the set of ubiquitin and ubiquitin-like conjugating enzymes in the eukaryote common ancestor?","citation":"J Mol Evol 2009 Jun;68(6):616-28","abstract":"Ubiquitin (Ub)-conjugating enzymes (E2) are key enzymes in ubiquitination or Ub-like modifications of proteins. We searched for all proteins belonging to the E2 enzyme super-family in seven species (Homo sapiens, Mus musculus, Drosophila melanogaster, Caenorhabditis elegans, Schizosaccharomyces pombe, Saccharomyces cerevisiae, and Arabidopsis thaliana) to identify families and to reconstruct each family's phylogeny. Our phylogenetic analysis of 207 genes led us to define 17 E2 families, with 37 E2 genes, in the human genome. The subdivision of E2 into four classes did not correspond to the phylogenetic tree. The sequence signature HPN (histidine-proline-asparagine), followed by a tryptophan residue at 16 (up to 29) amino acids, was highly conserved. When present, the active cysteine was found 7 to 8 amino acids from the C-terminal end of HPN. The secondary structures were characterized by a canonical alpha/beta fold. Only family 10 deviated from the common organization because the proteins were devoid of enzymatic activity. Family 7 had an insertion between beta strands 1 and 2; families 3, 5 and 14 had an insertion between the active cysteine and the conserved tryptophan. The three-dimensional data of these proteins highlight a strong structural conservation of the core domain. Our analysis shows that the primitive eukaryote ancestor possessed a diversified set of E2 enzymes, thus emphasizing the importance of the Ub pathway. This comprehensive overview of E2 enzymes emphasizes the diversity and evolution of this superfamily and helps clarify the nomenclature and true orthologies. A better understanding of the functions of these enzymes is necessary to decipher several human diseases.","doi":"10.1007/s00239-009-9225-6","authors":"Michelle C, Vourc'h P, Mignon L, Andres CR","authors_abbrev":"Michelle C et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-05-20","publication_year":"2009","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28631610","title":"A large gene family in fission yeast encodes spore killers that subvert Mendel's law.","citation":"Elife 2017 Jun 20;6","abstract":"Spore killers in fungi are selfish genetic elements that distort Mendelian segregation in their favor. It remains unclear how many species harbor them and how diverse their mechanisms are. Here, we discover two spore killers from a natural isolate of the fission yeast  Schizosaccharomyces pombe . Both killers belong to the previously uncharacterized  wtf  gene family with 25 members in the reference genome. These two killers act in strain-background-independent and genome-location-independent manners to perturb the maturation of spores not inheriting them. Spores carrying one killer are protected from its killing effect but not that of the other killer. The killing and protecting activities can be uncoupled by mutation. The numbers and sequences of  wtf  genes vary considerably between  S. pombe  isolates, indicating rapid divergence. We propose that  wtf  genes contribute to the extensive intraspecific reproductive isolation in  S. pombe , and represent ideal models for understanding how segregation-distorting elements act and evolve.","doi":"10.7554/eLife.26057","authors":"Hu W, Jiang ZD, Suo F, Zheng JX, He WZ, Du LL","authors_abbrev":"Hu W et al.","pubmed_publication_date":"20 Jun 2017","pubmed_entrez_date":"2017-06-21","publication_year":"2017","canto_session_key":"4cec0b8a65f82274","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-01-14 21:22:38","canto_approved_date":"2018-01-14 21:22:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-14 21:22:31","canto_added_date":"2017-06-22 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2E12.05","SPCC553.05c","SPCC1620.02","SPCC162.04c","SPCC306.10","SPCC830.02","SPCC576.16c","SPBC1706.02c","SPCC736.05","SPCC548.02c","SPCC548.03c","SPCC285.07c","SPCC1906.03","SPCC285.06c","SPCC794.02"],"gene_count":15,"ltp_gene_count":0,"approved_date":"2018-01-14"},{"uniquename":"PMID:12760062","title":"A conserved role for the Hus1 checkpoint protein in eukaryotic genome maintenance.","citation":"Cold Spring Harb Symp Quant Biol 2000;65:457-66","abstract":"","authors":"Weiss RS, Leder P, Enoch T","authors_abbrev":"Weiss RS et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2003-05-23","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18854158","title":"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair.","citation":"Cell 2008 Oct 03;135(1):97-109","abstract":"Mre11 forms the core of the multifunctional Mre11-Rad50-Nbs1 (MRN) complex that detects DNA double-strand breaks (DSBs), activates the ATM checkpoint kinase, and initiates homologous recombination (HR) repair of DSBs. To define the roles of Mre11 in both DNA bridging and nucleolytic processing during initiation of DSB repair, we combined small-angle X-ray scattering (SAXS) and crystal structures of Pyrococcus furiosus Mre11 dimers bound to DNA with mutational analyses of fission yeast Mre11. The Mre11 dimer adopts a four-lobed U-shaped structure that is critical for proper MRN complex assembly and for binding and aligning DNA ends. Further, mutations blocking Mre11 endonuclease activity impair cell survival after DSB induction without compromising MRN complex assembly or Mre11-dependant recruitment of Ctp1, an HR factor, to DSBs. These results show how Mre11 dimerization and nuclease activities initiate repair of DSBs and collapsed replication forks, as well as provide a molecular foundation for understanding cancer-causing Mre11 mutations in ataxia telangiectasia-like disorder (ATLD).","doi":"10.1016/j.cell.2008.08.017","authors":"Williams RS, Moncalian G, Williams JS, Yamada Y, Limbo O, Shin DS, Groocock LM, Cahill D, Hitomi C, Guenther G, Moiani D, Carney JP, Russell P, Tainer JA","authors_abbrev":"Williams RS et al.","pubmed_publication_date":"03 Oct 2008","pubmed_entrez_date":"2008-10-16","publication_year":"2008","canto_session_key":"4dd289ca048623e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-27 16:36:49","canto_approved_date":"2021-04-29 15:59:01","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-01-27 16:36:40","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":76,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPBC6B1.09c","SPAC13C5.07","SPCC338.08","SPBC29A10.05","SPBC543.03c"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2017-01-27"},{"uniquename":"PMID:463","title":"Protoplasts of Schizosaccharomyces pombe: an improved method for their preparation and the study of their guanine uptake.","citation":"J Gen Microbiol 1975 Oct;90(2):260-4","abstract":"A new method is described for the efficient conversion of Schizosaccharomyces pombe cells into protoplasts. The following parameters of guanine uptake determined in whole cells were unchanged in protoplasts: Km value, requirement for an energy source, sensitivity to competitive inhibitors, pH optimum, as well as the typical variation of the initial velocity of uptake observed during the growth phase.","authors":"Housset P, Nagy M, Schwencke J","authors_abbrev":"Housset P et al.","pubmed_publication_date":"Oct 1975","pubmed_entrez_date":"1975-10-01","publication_year":"1975","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20303984","title":"A mathematical model for cell size control in fission yeast.","citation":"J Theor Biol 2010 Jun 07;264(3):771-81","abstract":"Experimental investigations of cell size control in fission yeast Schizosaccharomyces pombe have illustrated that the cell cycle features 'sizer' and 'timer' phases which are distinguished by a growth rate changing point. Based on current biological knowledge of fission yeast size control, we propose here a model of ordinary differential equations (ODEs) for a possible explanation of the facts and control mechanism which is coupled with the cell cycle. Simulation results of the ODE model are demonstrated to agree with experimental data for the wild type and the cdc2-33 mutant. We show that the coupling of cell growth to cell division by translational control may account for observed properties of size control in fission yeast. As the translational control in the expression of cycle proteins Cdc13 and Cdc25 constructs positive feedback loops, the dynamical activities of the key components undergoes a rapid rising after a preliminary stage of slow increase. The coupling of this dynamical behavior to the elongation of the cell naturally gives rise to a rate change point and to 'sizer' and 'timer' phases, which characterize the cell cycle of fission yeast.","doi":"10.1016/j.jtbi.2010.03.023","authors":"Li B, Shao B, Yu C, Ouyang Q, Wang H","authors_abbrev":"Li B et al.","pubmed_publication_date":"07 Jun 2010","pubmed_entrez_date":"2010-03-23","publication_year":"2010","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28805495","title":"Shushing histone turnover: It's FUN protecting epigenome-genome.","citation":"Cell Cycle 2017 Oct 02;16(19):1731-1732","abstract":"","doi":"10.1080/15384101.2017.1360651","authors":"Taneja N, Grewal SIS","authors_abbrev":"Taneja N et al.","pubmed_publication_date":"02 Oct 2017","pubmed_entrez_date":"2017-08-15","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25A8.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU013380","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006482","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18391219","title":"The conserved Wobble uridine tRNA thiolase Ctu1-Ctu2 is required to maintain genome integrity.","citation":"Proc Natl Acad Sci U S A 2008 Apr 08;105(14):5459-64","abstract":"Modified nucleosides close to the anticodon are important for the proper decoding of mRNA by the ribosome. Particularly, the uridine at the first anticodon position (U34) of glutamate, lysine, and glutamine tRNAs is universally thiolated (S(2)U34), which is proposed to be crucial for both restriction of wobble in the corresponding split codon box and efficient codon-anticodon interaction. Here we show that the highly conserved complex Ctu1-Ctu2 (cytosolic thiouridylase) is responsible for the 2-thiolation of cytosolic tRNAs in the nematode and fission yeast. In both species, inactivation of the complex leads to loss of thiolation on tRNAs and to a thermosensitive decrease of viability associated with marked ploidy abnormalities and aberrant development. Increased level of the corresponding tRNAs suppresses the fission yeast defects, and our data suggest that these defects could result from both misreading and frame shifting during translation. Thus, a translation defect due to unmodified tRNAs results in severe genome instability.","doi":"10.1073/pnas.0709404105","authors":"Dewez M, Bauer F, Dieu M, Raes M, Vandenhaute J, Hermand D","authors_abbrev":"Dewez M et al.","pubmed_publication_date":"08 Apr 2008","pubmed_entrez_date":"2008-04-09","publication_year":"2008","canto_session_key":"7363f18fe5e26614","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-20 13:52:55","canto_approved_date":"2025-12-03 12:19:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-20 23:19:43","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPATRNALYS.03","SPATRNALYS.04","SPAC23A1.10","SPBC21D10.11c","SPATRNALYS.02","SPBC2G5.03","SPBC19C2.13c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2017-01-20"},{"uniquename":"PMID:32178677","title":"Robust microorganisms for biofuel and chemical production from municipal solid waste.","citation":"Microb Cell Fact 2020 Mar 16;19(1):68","abstract":"Worldwide 3.4 billion tonnes of municipal solid waste (MSW) will be produced annually by 2050, however, current approaches to MSW management predominantly involve unsustainable practices like landfilling and incineration. The organic fraction of MSW (OMSW) typically comprises ~ 50% lignocellulose-rich material but is underexplored as a biomanufacturing feedstock due to its highly inconsistent and heterogeneous composition. This study sought to overcome the limitations associated with studying MSW-derived feedstocks by using OMSW produced from a realistic and reproducible MSW mixture on a commercial autoclave system. The resulting OMSW fibre was enzymatically hydrolysed and used to screen diverse microorganisms of biotechnological interest to identify robust species capable of fermenting this complex feedstock.\nThe autoclave pre-treated OMSW fibre contained a polysaccharide fraction comprising 38% cellulose and 4% hemicellulose. Enzymatic hydrolysate of OMSW fibre was high in D-glucose (5.5% w/v) and D-xylose (1.8%w/v) but deficient in nitrogen and phosphate. Although relatively low levels of levulinic acid (30 mM) and vanillin (2 mM) were detected and furfural and 5-hydroxymethylfurfural were absent, the hydrolysate contained an abundance of potentially toxic metals (0.6% w/v). Hydrolysate supplemented with 1% yeast extract to alleviate nutrient limitation was used in a substrate-oriented shake-flask screen with eight biotechnologically useful microorganisms (Clostridium saccharoperbutylacetonicum, Escherichia coli, Geobacillus thermoglucosidasius, Pseudomonas putida, Rhodococcus opacus, Saccharomyces cerevisiae, Schizosaccharomyces pombe and Zymomonas mobilis). Each species' growth and productivity were characterised and three species were identified that robustly and efficiently fermented OMSW fibre hydrolysate without significant substrate inhibition: Z. mobilis, S. cerevisiae and R. opacus, respectively produced product to 69%, 70% and 72% of the maximum theoretical fermentation yield and could theoretically produce 136 kg and 139 kg of ethanol and 91 kg of triacylglycerol (TAG) per tonne of OMSW.\nDeveloping an integrated biorefinery around MSW has the potential to significantly alleviate the environmental burden of current waste management practices. Substrate-oriented screening of a representative and reproducible OMSW-derived fibre identified microorganisms intrinsically suited to growth on OMSW hydrolysates. These species are promising candidates for developing an MSW biorefining platform and provide a foundation for future studies aiming to valorise this underexplored feedstock.","doi":"10.1186/s12934-020-01325-0","authors":"Dornau A, Robson JF, Thomas GH, McQueen-Mason SJ","authors_abbrev":"Dornau A et al.","pubmed_publication_date":"16 Mar 2020","pubmed_entrez_date":"2020-03-18","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-03-19 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35807551","title":"Acrylamide-Derived Ionome, Metabolic, and Cell Cycle Alterations Are Alleviated by Ascorbic Acid in the Fission Yeast.","citation":"Molecules 2022 Jul 05;27(13)","abstract":"Acrylamide (AA), is a chemical with multiple industrial applications, however, it can be found in foods that are rich in carbohydrates. Due to its genotoxic and cytotoxic effects, AA has been classified as a potential carcinogen. With the use of spectrophotometry, ICP-OES, fluorescence spectroscopy, and microscopy cell growth, metabolic activity, apoptosis, ROS production, MDA formation, CAT and SOD activity, ionome balance, and chromosome segregation were determined in  Schizosaccharomyces pombe . AA caused growth and metabolic activity retardation, enhanced ROS and MDA production, and modulated antioxidant enzyme activity. This led to damage to the cell homeostasis due to ionome balance disruption. Moreover, AA-induced oxidative stress caused alterations in the cell cycle regulation resulting in chromosome segregation errors, as 4.07% of cells displayed sister chromatid non-disjunction during mitosis. Ascorbic acid (AsA, Vitamin C), a strong natural antioxidant, was used to alleviate the negative impact of AA. Cell pre-treatment with AsA significantly improved AA impaired growth, and antioxidant capacity, and supported ionome balance maintenance mainly due to the promotion of calcium uptake. Chromosome missegregation was reduced to 1.79% (44% improvement) by AsA pre-incubation. Results of our multiapproach analyses suggest that AA-induced oxidative stress is the major cause of alteration to cell homeostasis and cell cycle regulation.","doi":"10.3390/molecules27134307","authors":"Kovár M, Navrátilová A, Kolláthová R, Trakovická A, Požgajová M","authors_abbrev":"Kovár M et al.","pubmed_publication_date":"05 Jul 2022","pubmed_entrez_date":"2022-07-09","publication_year":"2022","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2022-07-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8264644","title":"Interaction between the Cig1 and Cig2 B-type cyclins in the fission yeast cell cycle.","citation":"Mol Cell Biol 1994 Jan;14(1):768-76","abstract":"In this report, we describe the cloning and characterization of a B-type cyclin, Cig2 from the fission yeast Schizosaccharomyces pombe. The cig2 gene encodes a 45-kDa protein that is most similar to a previously identified B-type cyclin in S. pombe, Cdc13. Deletion of cig2 had no observable effect on cell viability or progression through the cell cycle. Strains carrying the cig2 null allele do, however, exhibit an enhanced ability to undergo conjugation relative to a wild-type strain. The cig2 transcript was found to undergo periodic oscillation during the cell cycle, peaking at the G1/S-phase boundary. We have investigated the relationship between Cig2 and the other B-type cyclins, Cig1 and Cdc13, in the fission yeast. We found that cells carrying disruptions of both the cig1 and cig2 genes contain multiple nuclei with a 1C DNA content, suggesting that they are delayed in progression through the G1 phase of the cell cycle. The phenotype of this double mutant suggests that there is a delay in septum formation, possibly as a result of defective nuclear separation.","authors":"Connolly T, Beach D","authors_abbrev":"Connolly T et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_session_key":"c64c51b827f40f47","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-06-25 11:42:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-20 13:12:45","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4E9.02","SPAPB2B4.03"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-06-20"},{"uniquename":"PMID:29539401","title":"Characterization of Cell Boundary and Confocal Effects Improves Quantitative FRAP Analysis.","citation":"Biophys J 2018 Mar 13;114(5):1153-1164","abstract":"Fluorescence recovery after photobleaching (FRAP) is an important tool used by cell biologists to study the diffusion and binding kinetics of vesicles, proteins, and other molecules in the cytoplasm, nucleus, or cell membrane. Although many FRAP models have been developed over the past decades, the influence of the complex boundaries of 3D cellular geometries on the recovery curves, in conjunction with regions of interest and optical effects (imaging, photobleaching, photoswitching, and scanning), has not been well studied. Here, we developed a 3D computational model of the FRAP process that incorporates particle diffusion, cell boundary effects, and the optical properties of the scanning confocal microscope, and validated this model using the tip-growing cells of Physcomitrella patens. We then show how these cell boundary and optical effects confound the interpretation of FRAP recovery curves, including the number of dynamic states of a given fluorophore, in a wide range of cellular geometries-both in two and three dimensions-namely nuclei, filopodia, and lamellipodia of mammalian cells, and in cell types such as the budding yeast, Saccharomyces pombe, and tip-growing plant cells. We explored the performance of existing analytical and algorithmic FRAP models in these various cellular geometries, and determined that the VCell VirtualFRAP tool provides the best accuracy to measure diffusion coefficients. Our computational model is not limited only to these cells types, but can easily be extended to other cellular geometries via the graphical Java-based application we also provide. This particle-based simulation-called the Digital Confocal Microscopy Suite or DCMS-can also perform fluorescence dynamics assays, such as number and brightness, fluorescence correlation spectroscopy, and raster image correlation spectroscopy, and could help shape the way these techniques are interpreted.","doi":"10.1016/j.bpj.2018.01.013","authors":"Kingsley JL, Bibeau JP, Mousavi SI, Unsal C, Chen Z, Huang X, Vidali L, Tüzel E","authors_abbrev":"Kingsley JL et al.","pubmed_publication_date":"13 Mar 2018","pubmed_entrez_date":"2018-03-15","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-03-16 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12529446","title":"Gef1p, a new guanine nucleotide exchange factor for Cdc42p, regulates polarity in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2003 Jan;14(1):313-23","abstract":"Schizosaccharomyces pombe cdc42(+) regulates cell morphology and polarization of the actin cytoskeleton. Scd1p/Ral1p is the only described guanine nucleotide exchange factor (GEF) for Cdc42p in S. pombe. We have identified a new GEF, named Gef1p, specifically regulating Cdc42p. Gef1p binds to inactive Cdc42p but not to other Rho GTPases in two-hybrid assays. Overexpression of gef1(+) increases specifically the GTP-bound Cdc42p, and Gef1p is capable of stimulating guanine nucleotide exchange of Cdc42p in vitro. Overexpression of gef1(+) causes changes in cell morphology similar to those caused by overexpression of the constitutively active cdc42G12V allele. Gef1p localizes to the septum. gef1(+) deletion is viable but causes a mild cell elongation and defects in bipolar growth and septum formation, suggesting a role for Gef1p in the control of cell polarity and cytokinesis. The double mutant gef1delta scd1delta is not viable, indicating that they share an essential function as Cdc42p activators. However, both deletion and overexpression of either gef1(+) or scd1(+) causes different morphological phenotypes, which suggest different functions. Genetic evidence revealed a link between Gef1p and the signaling pathway of Shk1/Orb2p and Orb6p. In contrast, no genetic interaction between Gef1p and Shk2p-Mkh1p pathway was observed.","authors":"Coll PM, Trillo Y, Ametzazurra A, Perez P","authors_abbrev":"Coll PM et al.","pubmed_publication_date":"Jan 2003","pubmed_entrez_date":"2003-01-17","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.12","SPAC24H6.09","SPAC16E8.09","SPBC1604.14c","SPAC110.03"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:3732265","title":"Glycosylation and secretion of acid phosphatase in Schizosaccharomyces pombe.","citation":"Eur J Biochem 1986 Jul 01;158(1):133-40","abstract":"We have purified secreted acid phosphatase of Schizosaccharomyces pombe. The enzyme is N-glycosylated, the associated carbohydrate accounts for 90% of the total molecular mass and the protein moiety has a molecular mass of 54 kDa. The deglycosylated enzyme still exhibits enzymatic activity. Using antibodies recognizing the protein moiety of the enzyme we have identified two intracellular precursors of acid phosphatase: an unglycosylated membrane-bound 54-kDa form that accumulates in the presence of tunicamycin and a partially glycosylated 72-kDa form that accumulates mostly in membranes of cells grown in rich medium. We further showed that the conversion of the 54-kDa and 72-kDa forms to partially glycosylated and fully glycosylated acid phosphatase is a regulated process. Growth conditions determine how much of translated 54-kDa acid phosphatase is glycosylated to the 72-kDa form and how much remains unglycosylated in membranes. When cells are grown in a rich medium, 5% of the total acid phosphatase protein remains as unglycosylated enzyme and 8% as partially glycosylated 72-kDa form. In cells grown in the minimal medium, however, all of the 54-kDa and 72-kDa forms of acid phosphatase are rapidly processed to fully glycosylated enzyme. The 72-kDa form and the unglycosylated form of acid phosphatase are not secreted or transported to the plasma membrane.","authors":"Schweingruber AM, Schoenholzer F, Keller L, Schwaninger R, Trachsel H, Schweingruber ME","authors_abbrev":"Schweingruber AM et al.","pubmed_publication_date":"01 Jul 1986","pubmed_entrez_date":"1986-07-01","publication_year":"1986","canto_session_key":"47419e0c2f2a5f42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-05 16:04:27","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-05-18 13:43:42","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-05-18"},{"uniquename":"PMID:23760507","title":"Subunit architecture of the Golgi Dsc E3 ligase required for sterol regulatory element-binding protein (SREBP) cleavage in fission yeast.","citation":"J Biol Chem 2013 Jul 19;288(29):21043-21054","abstract":"The membrane-bound sterol regulatory element-binding protein (SREBP) transcription factors regulate lipogenesis in mammalian cells and are activated through sequential cleavage by the Golgi-localized Site-1 and Site-2 proteases. The mechanism of fission yeast SREBP cleavage is less well defined and, in contrast, requires the Golgi-localized Dsc E3 ligase complex. The Dsc E3 ligase consists of five integral membrane subunits, Dsc1 through Dsc5, and resembles membrane E3 ligases that function in endoplasmic reticulum-associated degradation. Using immunoprecipitation assays and blue native electrophoresis, we determined the subunit architecture for the complex of Dsc1 through Dsc5, showing that the Dsc proteins form subcomplexes and display defined connectivity. Dsc2 is a rhomboid pseudoprotease family member homologous to mammalian UBAC2 and a central component of the Dsc E3 ligase. We identified conservation in the architecture of the Dsc E3 ligase and the multisubunit E3 ligase gp78 in mammals. Specifically, Dsc1-Dsc2-Dsc5 forms a complex resembling gp78-UBAC2-UBXD8. Further characterization of Dsc2 revealed that its C-terminal UBA domain can bind to ubiquitin chains but that the Dsc2 UBA domain is not essential for yeast SREBP cleavage. Based on the ability of rhomboid superfamily members to bind transmembrane proteins, we speculate that Dsc2 functions in SREBP recognition and binding. Homologs of Dsc1 through Dsc4 are required for SREBP cleavage and virulence in the human opportunistic pathogen Aspergillus fumigatus. Thus, these studies advance our organizational understanding of multisubunit E3 ligases involved in endoplasmic reticulum-associated degradation and fungal pathogenesis.","doi":"10.1074/jbc.M113.468215","authors":"Lloyd SJ, Raychaudhuri S, Espenshade PJ","authors_abbrev":"Lloyd SJ et al.","pubmed_publication_date":"19 Jul 2013","pubmed_entrez_date":"2013-06-14","publication_year":"2013","canto_session_key":"0197357ea7803731","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rocky Cheung","canto_first_approved_date":"2015-04-27 15:08:22","canto_approved_date":"2022-11-09 19:21:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-26 18:15:32","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Rocky Cheung","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20H4.02","SPBC337.08c","SPBC19C2.09","SPAC1565.08","SPBC947.10","SPCC285.11","SPAC4D7.11","SPBC354.05c","SPBC119.02","SPAC1486.02c"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2015-04-27"},{"uniquename":"PMID:39752482","title":"Klp2-mediated Rsp1-Mto1 colocalization inhibits microtubule-dependent microtubule assembly in fission yeast.","citation":"Sci Adv 2025 Jan 03;11(1):eadq0670","abstract":"Microtubule assembly takes place at the centrosome and noncentrosomal microtubule-organizing centers (MTOCs). However, the mechanisms controlling the activity of noncentrosomal MTOCs are poorly understood. Here, using the fission yeast  Schizosaccharomyces pombe  as a model organism, we demonstrate that the kinesin-14 motor Klp2 interacts with the J-domain Hsp70/Ssa1 cochaperone Rsp1, an inhibitory factor of microtubule assembly, and that Klp2 is required for the proper localization of Rsp1 to microtubules. In addition, we demonstrate that Klp2 is not required for the localization of Mto1, a factor promoting microtubule assembly, to microtubules. Moreover, Rsp1-Ssa1 inhibits the interaction of Mto1-Mto2 with the gamma-tubulin small complex. The absence of Klp2 reduces the colocalization of Rsp1 and Mto1 foci on preexisting microtubules, resulting in an increased microtubule-dependent microtubule assembly. Our results suggest that Klp2 regulates the activity of noncentrosomal MTOCs by targeting Rsp1 to the sites of Mto1 activity and reveal a mechanism for the inhibition of noncentrosomal microtubule assembly by a kinesin-14 motor.","doi":"10.1126/sciadv.adq0670","authors":"Nie L, Liu W, Liang Z, Zheng F, Liu X, Yao X, Xiang S, Jiang K, Zheng S, Fu C","authors_abbrev":"Nie L et al.","pubmed_publication_date":"03 Jan 2025","pubmed_entrez_date":"2025-01-03","publication_year":"2025","canto_session_key":"8625aa489d4b8db9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-01-04 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17408088","title":"[Receptors of the serpentine type and heterotrimeric G-proteins of the yeasts: structural-functional organization and molecular action mechanisms].","citation":"Zh Evol Biokhim Fiziol 2007;43(1):3-23","abstract":"The signal systems of the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, coupled to heterotrimeric G-proteins and sensitive to pheromones and alimentary molecules, are prototypes of hormonal signal systems of the higher vertebrate animals and are widely used in studies on molecular mechanisms of their functioning. This review summarizes and analyzes data on structural-functional organization of the first two components of these systems - receptors of the serpentine type and heterotrimeric G-proteins; mechanisms of functional coupling of receptors and G-proteins both between each other and to other signal proteins are discussed. It has been shown that at the early stages of evolution of signal systems, at the yeast level, various models of transduction of signals into the cell were tested; many of them differ essentially from the classic model of the three-component, G-protein-coupled signal system of the higher vertebrates.","authors":"Shpakov AO","authors_abbrev":"Shpakov AO","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-04-06","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26771498","title":"A Proteome-wide Fission Yeast Interactome Reveals Network Evolution Principles from Yeasts to Human.","citation":"Cell 2016 Jan 14;164(1-2):310-323","abstract":"Here, we present FissionNet, a proteome-wide binary protein interactome for S. pombe, comprising 2,278 high-quality interactions, of which ∼ 50% were previously not reported in any species. FissionNet unravels previously unreported interactions implicated in processes such as gene silencing and pre-mRNA splicing. We developed a rigorous network comparison framework that accounts for assay sensitivity and specificity, revealing extensive species-specific network rewiring between fission yeast, budding yeast, and human. Surprisingly, although genes are better conserved between the yeasts, S. pombe interactions are significantly better conserved in human than in S. cerevisiae. Our framework also reveals that different modes of gene duplication influence the extent to which paralogous proteins are functionally repurposed. Finally, cross-species interactome mapping demonstrates that coevolution of interacting proteins is remarkably prevalent, a result with important implications for studying human disease in model organisms. Overall, FissionNet is a valuable resource for understanding protein functions and their evolution.","doi":"10.1016/j.cell.2015.11.037","authors":"Vo TV, Das J, Meyer MJ, Cordero NA, Akturk N, Wei X, Fair BJ, Degatano AG, Fragoza R, Liu LG, Matsuyama A, Trickey M, Horibata S, Grimson A, Yamano H, Yoshida M, Roth FP, Pleiss JA, Xia Y, Yu H","authors_abbrev":"Vo TV et al.","pubmed_publication_date":"14 Jan 2016","pubmed_entrez_date":"2016-01-16","publication_year":"2016","canto_session_key":"0517517c992c8525","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-06-29 17:35:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-29 14:37:16","canto_added_date":"2016-01-21 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of Ran1/Pat1 kinase bypasses the requirement for high-level expression of mei2 during fission yeast meiosis.","citation":"Curr Genet 2003 Jun;43(3):178-85","abstract":"Ran1/Pat1 kinase and cAMP-dependent protein kinase (PKA) regulate sexual differentiation in Schizosaccharomyces pombe. A reduction in the activity of both enzymes is a prerequisite for meiosis. Together, PKA and Pat1 control the level of expression of the Mei2 RNA-binding protein. Pat1 further regulates the activity of Mei2 by phosphorylation. Phosphorylation inactivates Mei2 by interfering with its cellular localization and by causing degradation of the protein via the ubiquitin-proteasome pathway. The inhibitor of Pat1, Mei3, is found only in diploid cells undergoing meiosis. Expression of mei3 is sufficient to induce meiosis. Here, we examine the relationship between Pat1, PKA and Mei3. We demonstrate that Mei3 is an in vitro substrate for PKA. Using site-specific mutagenesis, the major PKA phosphorylation site is identified. In vivo assays indicate that phosphorylation of Mei3 by PKA does not significantly alter the ability of the inhibitor to regulate Pat1. Although it does not function as an inhibitor for PKA, ectopic expression of Mei3 causes cells containing high PKA levels to undergo meiosis. Expression of various mei3 alleles in cells containing unregulated PKA activity shows that the ability to undergo meiosis correlates with Pat1 activity. Notably, induced levels of mei2 are not a prerequisite for meiotic differentiation, as previously thought. The implications of this result to developmental regulation are discussed.","authors":"Peng Z, Wang W, Schettino A, Leung B, McLeod M","authors_abbrev":"Peng Z et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-03-29","publication_year":"2003","canto_session_key":"65343c9ec44111ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 23:04:15","canto_approved_date":"2023-08-10 16:03:32","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2017-08-03 08:32:04","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC27D7.03c","SPBC119.04","SPBC106.10","SPAC8C9.03"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2018-06-10"},{"uniquename":"EMBL:SPC05768","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17476213","title":"Alp7/TACC is a crucial target in Ran-GTPase-dependent spindle formation in fission yeast.","citation":"Nature 2007 May 17;447(7142):334-7","abstract":"Microtubules are essential intracellular structures involved in several cellular phenomena, including polarity establishment and chromosome segregation. Because the nuclear envelope persists during mitosis (closed mitosis) in fission yeast (Schizosaccharomyces pombe), cytoplasmic microtubules must be reorganized into the spindle in the compartmentalized nucleus on mitotic entry. An ideal mechanism might be to take advantage of an evolutionarily conserved microtubule formation system that uses the Ran-GTPase nuclear transport machinery, but no targets of Ran for spindle formation have been identified in yeast. Here we show that a microtubule-associated protein, Alp7, which forms a complex with Alp14, is a target of Ran in yeast for spindle formation. The Ran-deficient pim1 mutant (pim1-F201S) failed to show mitosis-specific nuclear accumulation of Alp7. Moreover, this mutant exhibited compromised spindle formation and early mitotic delay. Importantly, these defects were suppressed by Alp7 that was artificially targeted to the nucleus by a Ran-independent and importin-alpha-mediated system. Thus, Ran targets Alp7-Alp14 to achieve nuclear spindle formation, and might differentiate its targets depending on whether the organism undergoes closed or open mitosis.","authors":"Sato M, Toda T","authors_abbrev":"Sato M et al.","pubmed_publication_date":"17 May 2007","pubmed_entrez_date":"2007-05-04","publication_year":"2007","canto_session_key":"c188e14b529e8e3d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-08-28 15:14:45","canto_approved_date":"2024-04-03 12:22:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-24 14:30:14","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.08c","SPBC1289.03c","SPBC557.03c","SPAC890.02c","SPCC895.07"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-08-28"},{"uniquename":"PMID:33171978","title":"Functional Expression of All Human Sulfotransferases in Fission Yeast, Assay Development, and Structural Models for Isoforms SULT4A1 and SULT6B1.","citation":"Biomolecules 2020 Nov 06;10(11)","abstract":"Cytosolic sulfotransferases (SULTs) catalyze phase II (conjugation) reactions of drugs and endogenous compounds. A complete set of recombinant fission yeast strains each expressing one of the 14 human SULTs was generated, including SULT4A1 and SULT6B1. Sulfation of test substrates by whole-cell biotransformation was successfully demonstrated for all enzymes for which substrates were previously known. The results proved that the intracellular production of the cofactor 3'-phosphoadenosine 5'-phosphosulfate (PAPS) necessary for SULT activity in fission yeast is sufficiently high to support metabolite production. A modified variant of sulfotransferase assay was also developed that employs permeabilized fission yeast cells (enzyme bags). Using this approach, SULT4A1-dependent sulfation of 1-naphthol was observed. Additionally, a new and convenient SULT activity assay is presented. It is based on the sulfation of a proluciferin compound, which was catalyzed by SULT1E1, SULT2A1, SULT4A1, and SULT6B1. For the latter two enzymes this study represents the first demonstration of their enzymatic functionality. Furthermore, the first catalytically competent homology models for SULT4A1 and SULT6B1 in complex with PAPS are reported. Through mechanistic molecular modeling driven by substrate docking, we pinned down the increased activity levels of these two isoforms to optimized substrate binding.","doi":"10.3390/biom10111517","authors":"Sun Y, Machalz D, Wolber G, Parr MK, Bureik M","authors_abbrev":"Sun Y et al.","pubmed_publication_date":"06 Nov 2020","pubmed_entrez_date":"2020-11-11","publication_year":"2020","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-11-13 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25814783","title":"Conservation of the Tsc/Rheb/TORC1/S6K/S6 Signaling in Fission Yeast.","citation":"Enzymes 2010;28:167-187","abstract":"The TSC/Rheb/TORC1/S6K/S6 signaling pathway plays critical roles in regulating protein synthesis and growth in eukaryotes. Our recent work using fission yeast  Schizosaccharomyces pombe  revealed that this signaling pathway is conserved from humans to fission yeast. In addition to target of rapamycin (TOR) homologsand tuberous sclerosis complex (TSC) homologs, fission yeast but not budding yeast, has a functional homolog of Rheb, a small G-protein acting as an activator of TOR complex 1 (TORC1). Several lines of genetic evidence suggest that the Tsc1-Tsc2 complex and Rheb act as upstream players of TORC1 in fission yeast. We have recently demonstrated that TORC1, but not TORC2, regulates phosphorylation of ribosomal protein S6 in response to nutrient availability. Candidate S6 kinase (S6K) protein has been identified. In addition, we find that rapamycin prevents a subset of TORC1 activity to regulate S6 phosphorylation in fission yeast.","authors":"Nakashima A, Tamanoi F","authors_abbrev":"Nakashima A et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2015-03-28","publication_year":"2010","canto_session_key":"6a434febaf336782","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-16 17:58:06","canto_approved_date":"2024-01-01 11:36:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-16 17:57:58","canto_added_date":"2015-04-01 01:00:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC839.17c","SPAPB1E7.12","SPAC630.13c","SPBC428.16c","SPBC216.07c","SPAC13G6.07c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-10-16"},{"uniquename":"PMID:24344203","title":"Isp7 is a novel regulator of amino acid uptake in the TOR signaling pathway.","citation":"Mol Cell Biol 2014 Mar;34(5):794-806","abstract":"TOR proteins reside in two distinct complexes, TOR complexes 1 and 2 (TORC1 and TORC2), that are central for the regulation of cellular growth, proliferation, and survival. TOR is also the target for the immunosuppressive and anticancer drug rapamycin. In Schizosaccharomyces pombe, disruption of the TSC complex, mutations in which can lead to the tuberous sclerosis syndrome in humans, results in a rapamycin-sensitive phenotype under poor nitrogen conditions. We show here that the sensitivity to rapamycin is mediated via inhibition of TORC1 and suppressed by overexpression of isp7(+), a member of the family of 2-oxoglutarate-Fe(II)-dependent oxygenase genes. The transcript level of isp7(+) is negatively regulated by TORC1 but positively regulated by TORC2. Yet we find extensive similarity between the transcriptome of cells disrupted for isp7(+) and cells mutated in the catalytic subunit of TORC1. Moreover, Isp7 regulates amino acid permease expression in a fashion similar to that of TORC1 and opposite that of TORC2. Overexpression of isp7(+) induces TORC1-dependent phosphorylation of ribosomal protein Rps6 while inhibiting TORC2-dependent phosphorylation and activation of the AGC-like kinase Gad8. Taken together, our findings suggest a central role for Isp7 in amino acid homeostasis and the presence of isp7(+)-dependent regulatory loops that affect both TORC1 and TORC2.","doi":"10.1128/MCB.01473-13","authors":"Laor D, Cohen A, Pasmanik-Chor M, Oron-Karni V, Kupiec M, Weisman R","authors_abbrev":"Laor D et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2013-12-18","publication_year":"2014","canto_session_key":"72f780a0a113152a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronitt Weisman","canto_first_approved_date":"2018-05-02 16:30:25","canto_approved_date":"2025-09-03 18:21:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-30 16:02:38","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":48,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Ronit Weisman","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Ronitt Weisman","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC869.10c","SPBC337.13c","SPAPYUG7.02c","SPBC30D10.10c","SPBC428.16c","SPAC22F3.13","SPCC24B10.07","SPAP7G5.06","SPAC630.13c","SPAPB1E7.12","SPAC1039.09","SPCC777.05","SPAC25B8.13c","SPAC869.11","SPBC12C2.02c","SPBC16G5.15c","SPBC216.07c"],"gene_count":17,"ltp_gene_count":12,"approved_date":"2018-05-02"},{"uniquename":"PMID:12237855","title":"Genome-wide search of Schizosaccharomyces pombe genes causing overexpression-mediated cell cycle defects.","citation":"Yeast 2002 Sep 30;19(13):1139-51","abstract":"Genetic studies in yeasts enable an in vivo analysis of gene functions required for the cell division cycle (cdc genes) in eukaryotes. In order to characterize new functions involved in cell cycle regulation, we searched for genes causing cell division defects by overexpression in the fission yeast Schizosaccharomyces pombe. By using this dominant genetic strategy, 26 independent clones were isolated from a Sz. pombe cDNA library. The cloned cDNAs were partially sequenced and identified by computer analysis. The 26 clones isolated corresponded to 21 different genes. Among them, six were genes previously characterized in Sz. pombe, 11 were homologues to genes identified and characterized in other organisms, and four represented genes with unknown functions. In addition to known cell cycle regulators encoding inhibitory protein kinases (wee1, pka1) and DNA checkpoint proteins (Pcna, rad24), we have identified genes that are involved in a number of cellular processes. This includes protein synthesis (ribosomal proteins L7, L10, L29, L41, S6, S11, S17 and the PolyA-Binding Protein PABP), protein degradation (UBI3), nucleolar rRNA expression (fib, imp1, dbp2), cell cytoskeleton (act1) and glycolysis (pfk1). The interference caused in the cell cycle by overexpression of these genes may elucidate novel mechanisms coupling different cellular processes with the control of the cell division. The effect caused by some of them is described in more detail.","authors":"Tallada VA, Daga RR, Palomeque C, Garzón A, Jimenez J","authors_abbrev":"Tallada VA et al.","pubmed_publication_date":"30 Sep 2002","pubmed_entrez_date":"2002-09-19","publication_year":"2002","canto_session_key":"18a27420dc89982d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-09-22 18:11:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-20 10:27:43","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC13G6.07c","SPBC16H5.02","SPAC6G10.11c","SPBC29A3.12","SPBC106.10","SPCC1020.10","SPBC2F12.04","SPBC15C4.01c","SPBC2D10.10c","SPCC74.05","SPCC16A11.10c","SPCC364.03","SPAC57A7.04c","SPBP8B7.16c","SPBC1604.08c","SPAC8E11.02c","SPCC18B5.03","SPCC24B10.09","SPAC15E1.03","SPBC16D10.09","SPCC5E4.07"],"gene_count":22,"ltp_gene_count":22,"approved_date":"2014-02-20"},{"uniquename":"EMBL:AU007054","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7985416","title":"A fission yeast gene encoding a protein that preferentially associates with curved DNA.","citation":"Yeast 1994 Jul;10(7):883-94","abstract":"We searched for fission yeast (Schizosaccharomyces pombe) proteins that preferentially bind to a synthetic curved DNA sequence, by means of a DNA-binding gel shift assay in the presence of an excess amount of a non-curved DNA sequence as a competitor. We identified such a protein in S. pombe. The protein, thus purified, has an apparent molecular weight of 42,000, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It was suggested that this protein (42 K-protein) recognizes and binds to a curved DNA structure in a given nucleotide sequence, although it also binds to a non-curved DNA sequence with lower affinity. As its putative coding sequence, a 1.9-kilobase genomic DNA from S. pombe was cloned and sequenced. Sequencing of a cDNA clone also revealed the existence of an open reading frame, with no intron, encoding a 381-amino-acid protein with a calculated molecular mass, 41,597. This protein appears to be located in the nucleus. The predicted protein sequence revealed that the 42 K-protein exhibits no significant similarity to any other known proteins, except to a hypothetical protein of Caenorhabditis elegans.","authors":"Yamada H, Mori H, Momoi H, Nakagawa Y, Ueguchi C, Mizuno T","authors_abbrev":"Yamada H et al.","pubmed_publication_date":"Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_session_key":"57ce3f9bb7bd9343","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-30 10:30:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-27 17:19:16","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23H4.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-27"},{"uniquename":"PMID:2079623","title":"The occurrence of glucosaminoglycan in the wall of Schizosaccharomyces pombe.","citation":"J Gen Microbiol 1990 Nov;136(11):2261-5","abstract":"The major part of the wall of Schizosaccharomyces pombe consists of (1----3)-alpha-glucan and (1----3)-beta-glucan with some (1----6)-beta-linkages. Although in hydrolysed samples only a minute amount of glucosamine could be detected, this amino sugar may play an essential role as an integral part of a glucosaminoglycan/glucan complex. Treatment of the wall with either nitrous acid or chitinase changed the solubility properties of the beta-glucan, which suggests that the glucosaminoglycan/glucan complex is essentially similar to that found in walls of other fungi. An enzyme with properties similar to that of chitin synthase of other fungi, and probably responsible for the synthesis of the glucosaminoglycan, was detected in a mixed-membrane fraction.","authors":"Sietsma JH, Wessels JG","authors_abbrev":"Sietsma JH et al.","pubmed_publication_date":"Nov 1990","pubmed_entrez_date":"1990-11-01","publication_year":"1990","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30930628","title":"Oxidative Stress Upregulates the Transcription of Genes Involved in Thiamine Metabolism.","citation":"Turk J Biol 2018;42(5):447-452","abstract":"Thiamine is a major vitamin that acts as a cofactor in energy metabolism in all organisms, as well as in lipid and amino acid metabolisms, and is associated with many diseases. It is known that glucose starvation decreases the intracellular thiamine pool while increasing oxidative stress tolerance. Earlier, in whole genome analysis, we detected major differences in the expression of genes related to thiamine pathway against oxidative stress in Schizosaccharomyces pombe. We investigated the effects of oxidative stress and glucose repression to thiamine pathway in S. pombe by comparing some genes encoding key enzymes of each related pathway at the transcription level. In the present study, we found that the expression of genes related to thiamine biosynthesis and transport (thi2, thi3, and pho1) increased in wild type and ird11 cells grown in thiamine-rich media under oxidative stress induced by H2O2. Based on our findings, we suggested that there might be an important effect of oxidative stress on thiamine biosynthesis and transport.","doi":"10.3906/biy-1801-51","authors":"Kartal B, Akçay A, Palabiyik B","authors_abbrev":"Kartal B et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2019-04-02","publication_year":"2018","canto_session_key":"9845e2430ee0ff58","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-04-03 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12664930","title":"[Structure of fungi and the action mechanism of antifungal agents].","citation":"Jpn J Antibiot 2002 Dec;55(6):902-6","abstract":"","authors":"Nishiyama Y","authors_abbrev":"Nishiyama Y","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2003-04-01","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15278909","title":"The regulation of competence to replicate in meiosis by Cdc6 is conserved during evolution.","citation":"Mol Reprod Dev 2004 Sep;69(1):94-100","abstract":"DNA replication licensing is an important step in the cell cycle at which cells become competent for DNA replication. When the cell cycle is arrested for long periods of time, this competence is lost. This is the case for somatic cells arrested in G0 or vertebrate oocytes arrested in G2. CDC6 is a factor involved in replication initiation competence which is necessary for the recruitment of the MCM helicase complex to DNA replication origins. In Xenopus, we have previously shown that CDC6 is the only missing replication factor in the oocyte whose translation during meiotic maturation is necessary and sufficient to confer DNA replication competence to the egg before fertilization (Lemaitre et al., 2002: Mol Biol Cell 13:435-444; Whitmire et al., 2002: Nature 419:722-725). Here, we report that this oogenesis control has been acquired by metazoans during evolution and conserved up to mammals. We also show that, contrary to eukaryotic metazoans, in S. pombe cdc18 (the S. pombe CDC6 homologue), CDC6 protein synthesis is down regulated during meiosis. As such, the lack of cdc18 prevents DNA replication from occurring in spores, whereas the presence of cdc6 makes eggs competent for DNA replication.","authors":"Lemaître JM, Bocquet S, Terret ME, Namdar M, Aït-Ahmed O, Kearsey S, Verlhac MH, Méchali M","authors_abbrev":"Lemaître JM et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-07-28","publication_year":"2004","canto_session_key":"273401965d727d19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-23 16:45:08","canto_approved_date":"2019-12-05 17:19:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-23 16:45:01","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-23"},{"uniquename":"GO_REF:0000067","title":"Representation of binding to a chemical entity as molecular function in the Gene Ontology","abstract":"We have created a standard template for classes describing the binding to a chemical entity (ChEBI) as a molecular function. The underlying equivalence axiom template is \"GO:0005488 and 'has input' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20587778","title":"Quantitative analysis of the mechanism of endocytic actin patch assembly and disassembly in fission yeast.","citation":"Mol Biol Cell 2010 Aug 15;21(16):2894-904","abstract":"We used quantitative confocal microscopy to measure the numbers of 16 proteins tagged with fluorescent proteins during assembly and disassembly of endocytic actin patches in fission yeast. The peak numbers of each molecule that accumulate in patches varied <30-50% between individual patches. The pathway begins with accumulation of 30-40 clathrin molecules, sufficient to build a hemisphere at the tip of a plasma membrane invagination. Thereafter precisely timed waves of proteins reach characteristic peak numbers: endocytic adaptor proteins (approximately 120 End4p and approximately 230 Pan1p), activators of Arp2/3 complex (approximately 200 Wsp1p and approximately 340 Myo1p) and approximately 300 Arp2/3 complexes just ahead of a burst of actin assembly into short, capped and highly cross-linked filaments (approximately 7000 actins, approximately 200 capping proteins, and approximately 900 fimbrins). Coronin arrives last as all other components disperse upon patch internalization and movement over approximately 10 s. Patch internalization occurs without recruitment of dynamins. Mathematical modeling, described in the accompanying paper (Berro et al., 2010, MBoC 21: 2803-2813), shows that the dendritic nucleation hypothesis can account for the time course of actin assembly into a branched network of several hundred filaments 100-200 nm long and that patch disassembly requires actin filament fragmentation in addition to depolymerization from the ends.","doi":"10.1091/mbc.E10-02-0157","authors":"Sirotkin V, Berro J, Macmillan K, Zhao L, Pollard TD","authors_abbrev":"Sirotkin V et al.","pubmed_publication_date":"15 Aug 2010","pubmed_entrez_date":"2010-07-01","publication_year":"2010","canto_session_key":"6eeb7666f8d6b4bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-09-07 15:50:53","canto_approved_date":"2024-03-24 07:22:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-07 15:50:44","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.05","SPBC13E7.09","SPAC630.03","SPBC9B6.08","SPBC1778.06c","SPAC17G8.04c","SPAC631.01c","SPCC126.06","SPBC146.13c","SPAPJ760.02c","SPAC25G10.09c","SPBC32H8.12c","SPAC688.11","SPAC11H11.06","SPAC4F10.15c","SPBC12C2.08","SPAC767.01c","SPAC23C4.02"],"gene_count":18,"ltp_gene_count":18,"approved_date":"2017-09-07"},{"uniquename":"PMID:10607571","title":"The COP9/signalosome complex is conserved in fission yeast and has a role in S phase.","citation":"Curr Biol 1999 Dec 02;9(23):1427-30","abstract":"The COP9/signalosome complex is conserved from plant to mammalian cells. In Arabidopsis, it regulates the nuclear abundance of COP1, a transcriptional repressor of photomorphogenic development [1] [2]. All COP (constitutive photomorphogenesis) mutants inappropriately express genes that are normally repressed in the dark. Eight subunits (Sgn1-Sgn8) of the homologous mammalian complex have been purified [3] [4]. Several of these have been previously identified through genetic or protein interaction screens. No coherent model for COP9/signalosome function has yet emerged, but a relationship with cell-cycle progression by transcriptional regulation, protein localisation or protein stability is possible. Interestingly, the COP9/signalosome subunits possess domain homology to subunits of the proteasome regulatory lid complex [5] [6]. Database searches indicate that only Sgn5/JAB1 is present in Saccharomyces cerevisiae, precluding genetic analysis of the complex in cell-cycle regulation. Here we identify a subunit of the signalosome in the fission yeast Schizosaccharomyces pombe through an analysis of the DNA-integrity checkpoint. We provide evidence for the conservation of the COP9/signalosome complex in fission yeast and demonstrate that it functions during S-phase progression.","authors":"Mundt KE, Porte J, Murray JM, Brikos C, Christensen PU, Caspari T, Hagan IM, Millar JB, Simanis V, Hofmann K, Carr AM","authors_abbrev":"Mundt KE et al.","pubmed_publication_date":"02 Dec 1999","pubmed_entrez_date":"1999-12-23","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8887552","title":"A novel S phase inhibitor in fission yeast.","citation":"EMBO J 1996 Sep 02;15(17):4603-12","abstract":"We have cloned a novel fission yeast gene, spd1, which causes G1 arrest when overexpressed. Deleting the gene results in cells being accelerated through G1 into S phase in certain circumstances when the G1-->S phase control is compromised. We have found that the encoded 14 kDa protein is cell cycle regulated, declining in level during S phase, and that p14spd1 physically associates with p34cdc2 in vivo when overexpressed, suggesting that p14spd1 may regulate S phase progression via an interaction with p34cdc2. We conclude that p14spd1 is a negative regulator of S phase, and that it may be part of the control ensuring an orderly onset of S phase or part of a G1-->S phase checkpoint control.","authors":"Woollard A, Basi G, Nurse P","authors_abbrev":"Woollard A et al.","pubmed_publication_date":"02 Sep 1996","pubmed_entrez_date":"1996-09-02","publication_year":"1996","canto_session_key":"f1afdd21aae916be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-03-03 20:25:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-15 18:39:11","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB2B4.03","SPBC336.12c","SPAC29B12.03","SPBC14C8.07c","SPBC11B10.09","SPBC582.03"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2014-02-15"},{"uniquename":"PMID:8631367","title":"The molecular basis for the natural resistance of the cytochrome bc1 complex from strobilurin-producing basidiomycetes to center Qp inhibitors.","citation":"Eur J Biochem 1996 Jan 15;235(1-2):54-63","abstract":"Mitochondria from the strobilurin A producing basidiomycetes Strobilurus tenacellus and Mycena galopoda exhibit natural resistance to (E)-beta-methoxyacrylate inhibitors of the ubiquinol oxidation center(center Qp) of the cytochrome bc1 complex. Isolated cytochrome bc1 complex from S. tenacellus was found to be highly similar to that of Saccharomyces cerevisiae with respect to subunit composition, as well as spectral characteristics and midpoint potentials of the heme centers. To understand the molecular basis of natural resistance, we determined the exon/intron organization and deduced the sequences of cytochromes b from S. tenacellus, M. galopoda and a third basidiomycete, Mycena viridimarginata, which produces no strobilurin A. Comparative sequence analysis of two regions of cytochrome b known to contribute to the formation of center Qp suggested that the generally lower sensitivity of all three basidiomycetes was due to the replacement of a small amino acid residue in position 127 by isoleucine. For M. galopoda replacement of Gly143 by alanine and Gly153 by serine, for S. tenacellus replacement of a small residue in position 254 by glutamine and Asn261 by aspartate was found to be the likely causes for resistance to (E)-beta-methoxyacrylates. The latter exchange is also found in Schizosaccharomyces pombe, which we found also to be naturally resistant to (E)-beta-methoxyacrylates.","authors":"Kraiczy P, Haase U, Gencic S, Flindt S, Anke T, Brandt U, Von Jagow G","authors_abbrev":"Kraiczy P et al.","pubmed_publication_date":"15 Jan 1996","pubmed_entrez_date":"1996-01-15","publication_year":"1996","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7813430","title":"Isolation and characterization of krp, a dibasic endopeptidase required for cell viability in the fission yeast Schizosaccharomyces pombe.","citation":"EMBO J 1994 Dec 15;13(24):5910-21","abstract":"The activation of pro-hormones and many precursor proteins involves cleavage by endopeptidases belonging to the subtilisin-like family of enzymes. Here we describe the isolation and characterization of the first member of this family from the fission yeast Schizosaccharomyces pombe. The enzyme, which has been named krp for KEX2-related protease, is a type I membrane-bound endopeptidase that cleaves substrates after pairs of dibasic residues. It appears to be synthesized as a pre-pro-protein that is likely to undergo processing following translocation into the endoplasmic reticulum. Processing has been characterized in a cell-free translation/translocation system prepared from Xenopus eggs. Krp is N-glycosylated on all five of its potential sites and both the pre-sequence and the pro-sequence are quickly removed following translocation, the latter probably by autocatalytic cleavage. The inhibitor profile of krp broadly reflects the known properties of the eukaryotic subtilisin proteases, while its pH and Ca2+ dependence are consistent with it being active within the secretory pathway. One of its physiological substrates is likely to be the pheromone precursor pro-P-factor, which it is shown to process in an in vitro system, but identification of other substrates is complicated because, unlike other members of this family, krp is essential for cell viability.","authors":"Davey J, Davis K, Imai Y, Yamamoto M, Matthews G","authors_abbrev":"Davey J et al.","pubmed_publication_date":"15 Dec 1994","pubmed_entrez_date":"1994-12-15","publication_year":"1994","canto_session_key":"8ccb3c8f2d46fe8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-03-20 15:59:00","canto_approved_date":"2025-12-29 06:31:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-03-22 18:36:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.06","SPAC22E12.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-03-20"},{"uniquename":"PMID:18411404","title":"A high-resolution map of nucleosome positioning on a fission yeast centromere.","citation":"Genome Res 2008 Jul;18(7):1064-72","abstract":"A key element for defining the centromere identity is the incorporation of a specific histone H3, CENPA, known as Cnp1p in Schizosaccharomyces pombe. Previous studies have suggested that functional S. pombe centromeres lack regularly positioned nucleosomes and may involve chromatin remodeling as a key step of kinetochore assembly. We used tiling microarrays to show that nucleosomes are, in fact, positioned in regular intervals in the core of centromere 2, providing the first high-resolution map of regional centromere chromatin. Nucleosome locations are not disrupted by mutations in kinetochore protein genes cnp1, mis18, mis12, nuf2, mal2; overexpression of cnp1; or the deletion of ams2, which encodes a GATA-like factor participating in CENPA incorporation. Bioinformatics analysis of the centromere sequence indicates certain enriched motifs in linker regions between nucleosomes and reveals a sequence bias in nucleosome positioning. In addition, sequence analysis of nucleosome-free regions identifies novel binding sites of Ams2p. We conclude that centromeric nucleosome positions are stable and may be derived from the underlying DNA sequence.","doi":"10.1101/gr.075374.107","authors":"Song JS, Liu X, Liu XS, He X","authors_abbrev":"Song JS et al.","pubmed_publication_date":"Jul 2008","pubmed_entrez_date":"2008-04-16","publication_year":"2008","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18272791","title":"Activation of Srk1 by the mitogen-activated protein kinase Sty1/Spc1 precedes its dissociation from the kinase and signals its degradation.","citation":"Mol Biol Cell 2008 Apr;19(4):1670-9","abstract":"Control of cell cycle progression by stress-activated protein kinases (SAPKs) is essential for cell adaptation to extracellular stimuli. The Schizosaccharomyces pombe SAPK Sty1/Spc1 orchestrates general changes in gene expression in response to diverse forms of cytotoxic stress. Here we show that Sty1/Spc1 is bound to its target, the Srk1 kinase, when the signaling pathway is inactive. In response to stress, Sty1/Spc1 phosphorylates Srk1 at threonine 463 of the regulatory domain, inducing both activation of Srk1 kinase, which negatively regulates cell cycle progression by inhibiting Cdc25, and dissociation of Srk1 from the SAPK, which leads to Srk1 degradation by the proteasome.","authors":"López-Avilés S, Lambea E, Moldón A, Grande M, Fajardo A, Rodríguez-Gabriel MA, Hidalgo E, Aligue R","authors_abbrev":"López-Avilés S et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-02-15","publication_year":"2008","canto_session_key":"8ee3edf9b1bcb1d5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-19 09:35:46","canto_approved_date":"2026-01-27 14:46:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-19 09:34:57","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC24B11.06c","SPAC24H6.05","SPCC1322.08","SPBC409.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-10-19"},{"uniquename":"PMID:12399381","title":"The sal3(+) gene encodes an importin-beta implicated in the nuclear import of Cdc25 in Schizosaccharomyces pombe.","citation":"Genetics 2002 Oct;162(2):689-703","abstract":"In Schizosaccharomyces pombe, the nuclear accumulation of Cdc25 peaks in G2 and is necessary for the proper timing of mitotic entry. Here, we identify the sal3(+) gene product as an importin-beta homolog that participates in the nuclear import of Cdc25. Loss of sal3(+) results in a cell cycle delay, failure to undergo G1 arrest under nitrogen-starvation conditions, and mislocalization of Cdc25 to the cytosol. Fusion of an exogenous classical nuclear localization sequence (cNLS) to Cdc25 restores its nuclear accumulation in a sal3 disruptant and suppresses the sal3 mutant phenotypes. In addition, we show that enhanced nuclear localization of Cdc25 at endogenous levels of expression advances the onset of mitosis. These results demonstrate that the nuclear translocation of Cdc25 is important for the timing of mitotic entry and that Sal3 plays an important role in this process.","authors":"Chua G, Lingner C, Frazer C, Young PG","authors_abbrev":"Chua G et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-10-26","publication_year":"2002","canto_session_key":"8fe26054c4dd9003","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-30 14:33:24","canto_approved_date":"2024-04-02 17:27:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-13 12:51:35","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.03","SPAC24H6.05","SPAC644.06c","SPAC8E11.02c","SPAC22F3.09c","SPAC11E3.09","SPAC57A10.02","SPAC6B12.10c","SPAC24B11.06c","SPBC582.03"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2016-09-30"},{"uniquename":"PMID:17761670","title":"Isolation of the Schizosaccharomyces pombe proteasome subunit Rpn7 and a structure-function study of the proteasome-COP9-initiation factor domain.","citation":"J Biol Chem 2007 Nov 02;282(44):32414-23","abstract":"Proper assembly of the 26 S proteasome is required to efficiently degrade polyubiquitinated proteins. Many proteasome subunits contain the proteasome-COP9-initiation factor (PCI) domain, thus raising the possibility that the PCI domain may play a role in mediating proteasome assembly. We have previously characterized the PCI protein Yin6, a fission yeast ortholog of the mammalian Int6 that has been implicated in breast oncogenesis, and demonstrated that it binds and regulates the assembly of the proteasome. In this study, we isolated another PCI proteasome subunit, Rpn7, as a high copy suppressor that rescued the proteasome defects in yin6 null cells. To better define the function of the PCI domain, we aligned protein sequences to identify a conserved leucine residue that is present in nearly all known PCI domains. Replacing it with aspartate in yeast Rpn7, Yin6, and Rpn5 inactivated these proteins, and mutant human Int6 mislocalized in HeLa cells. Rpn7 and Rpn5 bind Rpn9 with high affinity, but their mutant versions do not. Our data suggest that this leucine may interact with several hydrophobic amino acid residues to influence the spatial arrangement either within the N-terminal tandem alpha-helical repeats or between these repeats and the more C-terminal winged helix subdomain. Disruption of such an arrangement in the PCI domain may substantially inactivate many PCI proteins and block their binding to other proteins.","authors":"Sha Z, Yen HC, Scheel H, Suo J, Hofmann K, Chang EC","authors_abbrev":"Sha Z et al.","pubmed_publication_date":"02 Nov 2007","pubmed_entrez_date":"2007-09-01","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC607.05","SPBC582.07c","SPAC637.10c","SPBC16G5.01","SPAPB8E5.02c","SPAC1420.03"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:24531330","title":"Getting myosin-V on the right track: tropomyosin sorts transport in yeast.","citation":"Bioarchitecture 2014;4(1):35-8","abstract":"Recent studies have revealed a novel mechanism of myosin regulation in which the actin-binding protein tropomyosin converts atypical type-V myosins into processive cargo transporters. To achieve this, tropomyosin's primary role appears to lie in its ability to influence myosin's enzyme kinetics, prolonging the strong actin-bound ADP/apo state to enable hand-over-hand walking of myosin-V dimers along actin tracks. Activation of myosin-V mediated transport by tropomyosin underscores its function in helping to direct cargos to specific actin tracks and subcellular destinations. This type of regulation supports the broader notion that tropomyosin plays a key role in actomyosin sorting.","doi":"10.4161/bioa.28204","authors":"Pollard LW, Lord M","authors_abbrev":"Pollard LW et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-18","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-11-09 01:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1919.10c","SPBC2D10.14c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:7956071","title":"RecA-like recombination proteins in eukaryotes: functions and structures of RAD51 genes.","citation":"Cold Spring Harb Symp Quant Biol 1993;58:567-76","abstract":"","authors":"Ogawa T, Shinohara A, Nabetani A, Ikeya T, Yu X, Egelman EH, Ogawa H","authors_abbrev":"Ogawa T et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9383051","title":"Mcs4, a two-component system response regulator homologue, regulates the Schizosaccharomyces pombe cell cycle control.","citation":"Genetics 1997 Nov;147(3):1043-51","abstract":"The Schizosaccharomyces pombe cdc2-3w wee1-50 double mutant displays a temperature-sensitive lethal phenotype termed mitotic catastrophe. Six mitotic catastrophe suppressor (mcs1-6) genes were identified in a genetic screen designed to identify regulators of cdc2. Mutations in mcs1-6 suppress the cdc2-3w wee1-50 temperature-sensitive growth defect. Here, the cloning of mcs4 is described. The mcs4 gene product displays significant sequence homology to members of the two-component system response regulator protein family. Strains carrying the mcs4 and cdc25 mutations display a synthetic osmotic lethal phenotype along with an inability to grow on minimal synthetic medium. These phenotypes are suppressed by a mutation in wee1. In addition, the wis1 gene, encoding a stress-activated mitogen-activated protein kinase kinase, was identified as a dosage suppressor in this screen. These findings link the two-component signal transduction system to stress response and cell cycle control in S. pombe.","authors":"Cottarel G","authors_abbrev":"Cottarel G","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-02-07","publication_year":"1997","canto_session_key":"0b8d0d593c3d5404","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-07 19:45:04","canto_approved_date":"2021-02-08 09:44:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-07 19:44:54","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.10","SPBC19F8.07","SPBC409.07c","SPCC18B5.03","SPBC11B10.09","SPAC24H6.05"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-06-07"},{"uniquename":"PMID:18936951","title":"Reorganization of chromatin is an early response to nitrogen starvation in Schizosaccharomyces pombe.","citation":"Chromosoma 2009 Feb;118(1):99-112","abstract":"There are several documented events of changes in subnuclear localization during gene activation. However, there are conflicting data on whether the nuclear periphery is a compartment for gene repression or activation and whether genes are moved to the pores at the nuclear membrane (NM) or not during gene activation. Nitrogen starvation of fission yeast serves as a good model system for studying gene induction, as it causes fast regulation of hundreds of genes. In this study, the subnuclear localization of two gene clusters repressed by nitrogen was investigated. During normal growth conditions, the gene clusters localized to the nuclear periphery at the opposite side of the nucleus as compared to the spindle pole body. This constrained localization was dependent on the histone deacetylase Clr3, known to transcriptionally repress genes in these clusters. Already 20 min after nitrogen depletion, drastic changes in subnuclear localization of the two loci were observed, away from the NM toward the nuclear interior. At least for one of the clusters, the movement was clearly transcription dependent. Data presented in this paper illustrates how interconnected events of gene activation and nuclear reorganization are as well as provides a suggestion of how nuclear organization might be maintained.","doi":"10.1007/s00412-008-0180-6","authors":"Alfredsson-Timmins J, Kristell C, Henningson F, Lyckman S, Bjerling P","authors_abbrev":"Alfredsson-Timmins J et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2008-10-22","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27834216","title":"Schizosaccharomyces pombe kinesin-5 switches direction using a steric blocking mechanism.","citation":"Proc Natl Acad Sci U S A 2016 Nov 22;113(47):E7483-E7489","abstract":"Cut7, the sole kinesin-5 in Schizosaccharomyces pombe, is essential for mitosis. Like other yeast kinesin-5 motors, Cut7 can reverse its stepping direction, by mechanisms that are currently unclear. Here we show that for full-length Cut7, the key determinant of stepping direction is the degree of motor crowding on the microtubule lattice, with greater crowding converting the motor from minus end-directed to plus end-directed stepping. To explain how high Cut7 occupancy causes this reversal, we postulate a simple proximity sensing mechanism that operates via steric blocking. We propose that the minus end-directed stepping action of Cut7 is selectively inhibited by collisions with neighbors under crowded conditions, whereas its plus end-directed action, being less space-hungry, is not. In support of this idea, we show that the direction of Cut7-driven microtubule sliding can be reversed by crowding it with non-Cut7 proteins. Thus, crowding by either dynein microtubule binding domain or Klp2, a kinesin-14, converts Cut7 from net minus end-directed to net plus end-directed stepping. Biochemical assays confirm that the Cut7 N terminus increases Cut7 occupancy by binding directly to microtubules. Direct observation by cryoEM reveals that this occupancy-enhancing N-terminal domain is partially ordered. Overall, our data point to a steric blocking mechanism for directional reversal through which collisions of Cut7 motor domains with their neighbors inhibit their minus end-directed stepping action, but not their plus end-directed stepping action. Our model can potentially reconcile a number of previous, apparently conflicting, observations and proposals for the reversal mechanism of yeast kinesins-5.","authors":"Britto M, Goulet A, Rizvi S, von Loeffelholz O, Moores CA, Cross RA","authors_abbrev":"Britto M et al.","pubmed_publication_date":"22 Nov 2016","pubmed_entrez_date":"2016-11-12","publication_year":"2016","canto_session_key":"bbca19399d458107","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-05-16 10:23:41","canto_approved_date":"2022-05-16 11:03:07","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-05-16 10:23:19","canto_added_date":"2016-11-13 01:15:11","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":2,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPAC25G10.07c","SPBC16A3.15c","SPAC664.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2022-05-16","pdb_entries":[{"pdb_id":"5m5m","gene_chains":[{"gene_uniquename":"SPAC25G10.07c","chain":"C","position":"64-432"}],"title":"Pseudo-atomic model of microtubule-bound S.pombe kinesin-5 motor domain in the AMPPNP state (based on cryo-electron microscopy experiment): the N-terminus adopts multiple conformations.","entry_authors":"Goulet A,Moores CA,Cross RA","entry_authors_abbrev":"Goulet A et al.","reference_uniquename":"PMID:27834216","experimental_method":"EM","resolution":"9.3"},{"pdb_id":"5m5n","gene_chains":[{"gene_uniquename":"SPAC25G10.07c","chain":"C","position":"64-432"}],"title":"Pseudo-atomic model of microtubule-bound S.pombe kinesin-5 motor domain in the AMPPNP state (based on cryo-electron microscopy experiment): the N-terminus adopts multiple conformations.","entry_authors":"Goulet A,Moores CA,Cross RA","entry_authors_abbrev":"Goulet A et al.","reference_uniquename":"PMID:27834216","experimental_method":"EM","resolution":"9.3"},{"pdb_id":"5m5o","gene_chains":[{"gene_uniquename":"SPAC25G10.07c","chain":"C","position":"64-432"}],"title":"Pseudo-atomic model of microtubule-bound S.pombe kinesin-5 motor domain in the AMPPNP state (based on cryo-electron microscopy experiment): the N-terminus adopts multiple conformations.","entry_authors":"Goulet A,Moores CA,Cross RA","entry_authors_abbrev":"Goulet A et al.","reference_uniquename":"PMID:27834216","experimental_method":"EM","resolution":"9.3"},{"pdb_id":"5m5l","gene_chains":[{"gene_uniquename":"SPAC25G10.07c","chain":"C","position":"64-432"}],"title":"Pseudo-atomic model of microtubule-bound S. pombe kinesin-5 motor domain in the AMPPNP state (based on cryo-electron microscopy experiment): the N-terminus adopts multiple conformations","entry_authors":"Goulet A,Moores CA,Cross RA","entry_authors_abbrev":"Goulet A et al.","reference_uniquename":"PMID:27834216","experimental_method":"EM","resolution":"9.3"},{"pdb_id":"5m5i","gene_chains":[{"gene_uniquename":"SPAC25G10.07c","chain":"C","position":"64-432"}],"title":"Pseudo-atomic model of microtubule-bound S.pombe kinesin-5 motor domain in the AMPPNP state (based on cryo-electron microscopy experiment): the N-terminus conformation allows formation of a cover neck bundle.","entry_authors":"Goulet A,Moores CA,Cross RA","entry_authors_abbrev":"Goulet A et al.","reference_uniquename":"PMID:27834216","experimental_method":"EM","resolution":"9.3"}]},{"uniquename":"PMID:8590481","title":"Nucleotide sequence of the Schizosaccharomyces japonicus var. versatilis ribosomal RNA gene cluster and its phylogenetic implications.","citation":"Curr Genet 1995 Sep;28(4):353-9","abstract":"Fission yeasts form a small but heterogeneous group of ascomycetes and it is still unclear whether they should be subdivided into three genera (Schizosaccharomyces, Octosporomyces, Hasegawaea) or remain a single genus (Schizosaccharomyces). In order to decide whether a new genus Hasegawaea should be established for the species Schizosaccharomyces japonicus and Schizosaccharomyces versatilis, we have characterized the entire rDNA cluster in Schizosaccharomyces japonicus var. versatilis and compared it with the homologous region from Schizosaccharomyces pombe and with complete rRNA gene sequences from other yeast genera. From a phage genomic library a recombinant lambda phage containing the entire rDNA repeat unit was isolated. In this paper we report the primary sequence of the 18s, 5.8s and 25s rRNA coding regions. The S. japonicus var. versatilis rRNA genes are 1823 (18s), 158 (5.8s) and 3422 (25s) nucleotides long. The two sequences of the larger rRNA genes exhibit 95.7% (18s) and 93% (25s) similarity with the homologous genes from S. pombe. The differences between the rRNA genes of S. japonicus and S. pombe, however, are much smaller than the intrageneric differences within the rDNA sequences of other yeast genera. Therefore, subdivision of fission yeasts into the genera Schizosaccharomyces and Hasegawaea does not to seem to be justified.","authors":"Naehring J, Kiefer S, Wolf K","authors_abbrev":"Naehring J et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8549830","title":"Schizosaccharomyces pombe possesses an unusual and a conventional hexokinase: biochemical and molecular characterization of both hexokinases.","citation":"FEBS Lett 1996 Jan 08;378(2):185-9","abstract":"Two hexokinases were characterized in Schizosaccharomyces pombe: hexokinase 1, with a low phosphorylation coefficient on glucose (Km 8.5 mM) and hexokinase 2, a kinetically conventional hexokinase. Genes hxk1+ and hxk2+ encoding these enzymes were cloned and sequenced. Disruption of hxk1+ had no effect on growth but disruption of hxk2+ doubled the generation time in glucose. Spores carrying the double disruption hxk1+ hxk2+ did not grow on glucose or fructose after one week. Expression of hxk1+ increased strongly during growth in fructose or glycerol. Expression of hxk2+ was highest during growth in glycerol. A NADP-dependent glucose dehydrogenase was detected, but not a glucokinase.","authors":"Petit T, Blázquez MA, Gancedo C","authors_abbrev":"Petit T et al.","pubmed_publication_date":"08 Jan 1996","pubmed_entrez_date":"1996-01-08","publication_year":"1996","canto_session_key":"78253143f2002b71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-06-21 14:54:44","canto_session_submitted_date":"2012-06-20 21:21:22","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.04","SPAC4F8.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-06-20"},{"uniquename":"PMID:40908147","title":"Genetic suppression of precocious transcription termination identifies mutations in essential subunits of the fission yeast cleavage and polyadenylation machinery.","citation":"RNA 2025 Sep 04;","abstract":"The fission yeast phosphate acquisition (PHO) regulon is repressed under phosphate-replete conditions by upstream lncRNA-mediated transcriptional interference. Inositol-1-pyrophosphates control phosphate homeostasis via their action as agonists of precocious PHO lncRNA 3'-processing/termination. Inositol pyrophosphatase-inactivating mutations that increase inositol-1-pyrophosphates elicit derepression of the PHO genes and a severe growth defect in YES medium. Previous studies demonstrated suppression of inositol pyrophosphate toxicosis by targeted deletion or loss-of-function mutations in the nonessential Ssu72, Ppn1, Swd22, and Ctf1 subunits of the fission yeast Cleavage and Polyadenylation Factor (CPF) complex. Here we conducted a screen for spontaneous mutations that suppress the precocious PHO lncRNA termination underlying the sickness of asp1-STF pyrophosphatase mutants. We thereby recovered and characterized novel hypomorphic missense mutations in five essential CPF subunits: Ysh1 (the cleavage endonuclease), Pta1 (an Armadillo/HEAT-repeat protein), Pfs2 (a WD repeat protein), Cft1 (a WD repeat protein), and Msi2 (a tandem RRM RNA-binding protein). The screen also yielded an intron branchpoint mutation in the gene encoding essential CPF subunit Iss1. In addition, we found that asp1-STF toxicosis was suppressed by a missense mutation in the active site of Pla1, the essential poly(A) polymerase subunit of CPF. Genetic crosses revealed a hierarchy of mutational synergies between the essential CPF subunits, the inessential CPF subunits, termination factor Rhn1, the Thr4 \"letter\" of the RNA polymerase II CTD code, and the Asp1 kinase that synthesizes inositol-1-pyrophosphates. The synthetic lethality of msi2-G252E with ctf1∆, swd22∆, ppn1∆, ssu72-C13S, rpb1-CTD-T4A, and asp1∆ establishes Msi2 as a central agent of 3'-processing/termination, functioning in parallel to inositol-1-pyrophosphates.","doi":"10.1261/rna.080664.125","authors":"Innokentev A, Sanchez AM, Bednor L, Babor J, Schwer B, Shuman S","authors_abbrev":"Innokentev A et al.","pubmed_publication_date":"04 Sep 2025","pubmed_entrez_date":"2025-09-04","publication_year":"2025","canto_session_key":"933aac2cf6e3b3ed","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-05 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.15"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2583093","title":"Characterization of Schizosaccharomyces pombe minichromosome deletion derivatives and a functional allocation of their centromere.","citation":"EMBO J 1989 Oct;8(10):3045-52","abstract":"A 530 kb long Schizosaccharomyces pombe linear minichromosome, Ch16, containing a centric region of chromosome III, has previously been made. In the present study, we constructed a number of deletions in the right and/or left arms of Ch16, and compared their structure and behaviour with Ch16. The functional centromere, cen3, is allocated within a 120 kb long region which is covered by the shortest derivative, Ch10, and is comprised mostly of centromeric repeating sequences. The shortest minichromosome is stable in mitosis and the copy number control is apparently precise. In monosomic meiosis it segregates normally. In disomic meioses, however, the frequency of non-disjunction is very high, suggesting that it may not form a pair. The mitotic loss rate of one of the left-arm deletions, ChR32, which lacks a part of the centromeric repeating sequence, is the highest of all the deletions. This deletion also exhibits the highest precocious sister chromatid separation in meiosis I, suggesting that sister chromatid association might become weakened in ChR32. Our results indicate that the proper meiotic segregation of S.pombe minichromosomes is dependent upon the formation of a bivalent. S.pombe may not have the 'distributive segregation' found with Saccharomyces cerevisiae minichromosomes.","authors":"Niwa O, Matsumoto T, Chikashige Y, Yanagida M","authors_abbrev":"Niwa O et al.","pubmed_publication_date":"Oct 1989","pubmed_entrez_date":"1989-10-01","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10872838","title":"Identification of a 26S proteasome-associated UCH in fission yeast.","citation":"Biochem Biophys Res Commun 2000 May 27;272(1):270-5","abstract":"We have identified a 26S proteasome-associated ubiquitin carboxyl-terminal hydrolase (UCH) in Schizosaccharomyces pombe. The gene (designated uch2+) encodes a protein containing a UCH catalytic domain at its N-terminus and a short extension at its C-terminus. uch2+ is nonessential as the uch2 null mutant strain showed no significant difference from the wild-type strain. The GFP-tagged Uch2p is localized predominantly to the nuclear periphery, which is similar to the 26S proteasome localization. Deletion of the C-terminal extension of Uch2p resulted in a drastic change of its subcellular localization: it showed a generally diffused distribution instead of a perinuclear pattern. Glycerol gradient centrifugation analysis and coimmunoprecipitation studies of fission yeast extracts using anti-Mts4p antiserum suggest that Uch2p is associated with the 26S proteasome and the association of Uch2p with the 26S proteasome is mediated by its C-terminal extension.","authors":"Li T, Naqvi NI, Yang H, Teo TS","authors_abbrev":"Li T et al.","pubmed_publication_date":"27 May 2000","pubmed_entrez_date":"2000-06-29","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC409.06","SPBP19A11.03c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:23900342","title":"Genome-wide mapping of polyadenylation sites in fission yeast reveals widespread alternative polyadenylation.","citation":"RNA Biol 2013 Aug;10(8):1407-14","abstract":"Regulatory elements in the 3' untranslated regions (UTRs) of eukaryotic mRNAs influence mRNA localization, translation, and stability. 3'-UTR length is determined by the location at which mRNAs are cleaved and polyadenylated. The use of alternative polyadenylation sites is common, and can be regulated in different situations. I present a new method to identify cleavage and polyadenylation sites (CSs) at the genome-wide level. The approach is strand-specific, avoids RNA enzymatic modification steps that can introduce sequence-specific biases, and uses unique molecular identifiers to ensure that all identified CS originates from individual RNA molecules. I applied this method to create the first comprehensive genome-wide map of polyadenylation sites of the fission yeast Schizosaccharomyces pombe, comprising the analysis of 2,021,000 individual mRNAs that defined 8,883 CSs. CSs were identified for 90% of coding genes and 50% of ncRNAs. Alternative polyadenylation was prevalent in both groups, with 41% and 45% of all detected genes, respectively, displaying more than one CS. The specificity of the cleavage reaction was gene-specific, resulting in highly variable levels of heterogeneity in 3'-UTR lengths. Finally, I show that for both coding and non-coding genes, the most common regulatory motif associated with CSs in fission yeast is the canonical human AAUAAA sequence.","doi":"10.4161/rna.25758","authors":"Mata J","authors_abbrev":"Mata J","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-08-01","publication_year":"2013","canto_session_key":"74671fa2ad03afa3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-11 07:28:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-10 12:34:52","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-09-10"},{"uniquename":"PMID:8159161","title":"Cloning of the blasticidin S deaminase gene (BSD) from Aspergillus terreus and its use as a selectable marker for Schizosaccharomyces pombe and Pyricularia oryzae.","citation":"Mol Gen Genet 1994 Jan;242(2):121-9","abstract":"Aspergillus terreus produces a unique enzyme, blasticidin S deaminase, which catalyzes the deamination of blasticidin S (BS), and in consequence confers high resistance to the antibiotic. A cDNA clone derived from the structural gene for BS deaminase (BSD) was isolated by transforming Escherichia coli with an Aspergillus cDNA expression library and directly selecting for the ability to grow in the presence of the antibiotic. The complete nucleotide sequence of BSD was determined and proved to contain an open reading frame of 393 bp, encoding a polypeptide of 130 amino acids. Comparison of its nucleotide sequence with that of bsr, the BS deaminase gene isolated from Bacillus cereus, indicated no homology and a large difference in codon usage. The activity of BSD expressed in E. coli was easily quantified by an assay based on spectrophotometric recording. The BSD gene was placed in a shuttle vector for Schizosaccharomyces pombe, downstream of the SV40 early region promoter, and this allowed direct selection with BS at high frequency, following transformation into the yeast. The BSD gene was also employed as a selectable marker for Pyricularia oryzae, which could not be transformed to BS resistance by bsr. These result promise that the BSD gene will be useful as a new dominant selectable marker for eukaryotes.","authors":"Kimura M, Kamakura T, Tao QZ, Kaneko I, Yamaguchi I","authors_abbrev":"Kimura M et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12747847","title":"Chromosome segregation: clamping down on deviant orientations.","citation":"Curr Biol 2003 May 13;13(10):R385-7","abstract":"Chromosome segregation depends on proper orientation of sister kinetochores. The protein Csm1 is required for mono-orientation of sister kinetochores at meiosis I in budding yeast. Surprisingly, its homologue in fission yeast appears instead of clamp micro-tubule binding sites together on single mitotic kinetochores so that they all face one spindle pole.","authors":"Pidoux A, Allshire R","authors_abbrev":"Pidoux A et al.","pubmed_publication_date":"13 May 2003","pubmed_entrez_date":"2003-05-16","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31615768","title":"CLASP promotes microtubule bundling in metaphase spindle independently of Ase1/PRC1 in fission yeast.","citation":"Biol Open 2019 Oct 24;8(10)","abstract":"Microtubules in the mitotic spindle are organised by microtubule-associated proteins. In the late stage of mitosis, spindle microtubules are robustly organised through bundling by the antiparallel microtubule bundler Ase1/PRC1. In early mitosis, however, it is not well characterised as to whether spindle microtubules are actively bundled, as Ase1 does not particularly localise to the spindle at that stage. Here we show that the conserved microtubule-associated protein CLASP (fission yeast Peg1/Cls1) facilitates bundling of spindle microtubules in early mitosis. The  peg1  mutant displayed a fragile spindle with unbundled microtubules, which eventually resulted in collapse of the metaphase spindle and abnormal segregation of chromosomes. Peg1 is known to be recruited to the spindle by Ase1 to stabilise antiparallel microtubules in late mitosis. However, we demonstrate that the function of Peg1 in early mitosis does not rely on Ase1. The unbundled spindle phenotype of the  peg1  mutant was not seen in the  ase1  mutant, and Peg1 preferentially localised to the spindle even in early mitosis unlike Ase1. Moreover, artificial overexpression of Ase1 in the  peg1  mutant partially suppressed unbundled microtubules. We thus conclude that Peg1 bundles microtubules in early mitosis, in a distinct manner from its conventional Ase1-dependent functions in other cell cycle stages.","doi":"10.1242/bio.045716","authors":"Ebina H, Ji L, Sato M","authors_abbrev":"Ebina H et al.","pubmed_publication_date":"24 Oct 2019","pubmed_entrez_date":"2019-10-17","publication_year":"2019","canto_session_key":"25e3a75033029bd6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2019-11-05 08:06:10","canto_approved_date":"2026-02-06 15:57:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-24 09:32:41","canto_added_date":"2019-10-18 00:15:04","annotation_curators":[{"name":"Masamitsu Sato","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPAPB1A10.09","SPAC3G9.12"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-11-05"},{"uniquename":"PMID:24189723","title":"The origin of a centromere effect on mitotic recombination : A study in the fission yeast Schizosaccharomyces pombe.","citation":"Curr Genet 1980 Jul;2(1):53-60","abstract":"Spontaneous meiotic and mitotic rates of recombination were measured for 50 intragenic intervals in 9 genes of Schizosaccharomyces pombe. A much smaller mitotic/meiotic recombination ratio is observed for genes unlinked to the centromere (average ratio: 0.005) than for genes close to the centromere (up to 0.17). The high ratio observed for the latter genes is due to a high rate of mitotic recombination rather than to a centromeric inhibition of meiotic recombination, since there was no meiotic inhibition in the genes considered. As already reported for one pair of genes in Saccharomyces cerevisiae (Hénaut et Luzzati, 1972), cells that have recombined at one locus have a meiotic rate of coincident recombination at an unlinked locus, even if the latter is not on the same chromosome. This coincidence is much lower when intragenic recombinants are selected in the centromere-linked gene lys1. In modification of an earlier hypothesis (Hurst and Fogel, 1964), we propose that: (a) pairing between homologous chromosomes is the major rate-limiting factor in mitotic recombination; (b) mitotic pairing of homologous chromosomes is frequent, possibly occuring in all vegetative cells, but is usually restricted to the centromere region; and (c) pairing along the whole genome is restricted to a small subpopulation among the mitotically dividing cells.","doi":"10.1007/BF00445694","authors":"Minet M, Grossenbacher-Grunder AM, Thuriaux P","authors_abbrev":"Minet M et al.","pubmed_publication_date":"Jul 1980","pubmed_entrez_date":"2013-11-06","publication_year":"1980","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 06:09:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPO251329","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30523155","title":"Adaptor protein complex-1 (AP-1) is recruited by the HEATR5 protein Laa1 and its co-factor Laa2 in yeast.","citation":"J Biol Chem 2019 Jan 25;294(4):1410-1419","abstract":"Cellular membrane trafficking mediated by the clathrin adaptor protein complex-1 (AP-1) is important for the proper composition and function of organelles of the endolysosomal system. Normal AP-1 function requires proteins of the HEAT repeat-containing 5 (HEATR5) family. Although HEATR5 proteins were first identified based on their ability to interact with AP-1, the functional significance of this interaction was unknown. We used bioinformatics-based phenotypic profiling and information from genome-wide fluorescence microscopy studies in the budding yeast  Saccharomyces cerevisiae  to identify a protein, Laa2, that mediates the interaction between AP-1 and the yeast HEATR5 protein Laa1. Further characterization of Laa2 revealed that it binds to both Laa1 and AP-1. Laa2 contains a motif similar to the characterized γ-ear-binding sites found in other AP-1-binding proteins. This motif in Laa2 is essential for the Laa1-AP-1 interaction. Moreover, mutation of this motif disrupted AP-1 localization and function and caused effects similar to mutations that remove the γ-ear of AP-1. These results indicate that Laa2 mediates the interaction between Laa1 and AP-1 and reveal that this interaction promotes the stable association of AP-1 with membranes in yeast.","doi":"10.1074/jbc.RA118.005253","authors":"Zysnarski CJ, Lahiri S, Javed FT, Martínez-Márquez JY, Trowbridge JW, Duncan MC","authors_abbrev":"Zysnarski CJ et al.","pubmed_publication_date":"25 Jan 2019","pubmed_entrez_date":"2018-12-08","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.05c","SPBC27B12.08"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8750236","title":"The mae1 gene of Schizosaccharomyces pombe encodes a permease for malate and other C4 dicarboxylic acids.","citation":"Yeast 1995 Dec;11(15):1485-91","abstract":"The mae1 gene of the yeast Schizosaccharomyces pombe was identified on the basis of its ability to complement a mutant defective in the transport of malic acid. Analysis of the DNA sequence revealed an open reading frame of 1314 base pairs, encoding a polypeptide of 438 amino acids with a predicted molecular weight of 49 kDa. A hydropathy profile of the predicted amino acid sequence revealed a protein with ten membrane-spanning or associated domains and hydrophilic N- and C- termini. The predicted secondary structure of the protein in similar to models proposed for other integral membrane proteins from both prokaryotes and eukaryotes. The S. pombe mae1 gene encodes a single mRNA of 1.5 kb. The mea1 gene is expressed constitutively and is not subject to catabolite repression as was previously reported for the malate permease systems of Candida utilis and Hansenula anomala. The mae1 gene was mapped 2842 bp 5' to the MFml gene on chromosome I. Transport assays revealed that the mae1 gene encodes a permease involved in the uptake of L-malate, succinate and malonic acid.","authors":"Grobler J, Bauer F, Subden RE, Van Vuuren HJ","authors_abbrev":"Grobler J et al.","pubmed_publication_date":"Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"a832c3b98a842c37","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-07 16:21:36","canto_approved_date":"2017-11-07 16:21:36","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-05-30 13:54:30","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB8E5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-11-07"},{"uniquename":"PMID:28289220","title":"Phytosphingosine degradation pathway includes fatty acid α-oxidation reactions in the endoplasmic reticulum.","citation":"Proc Natl Acad Sci U S A 2017 Mar 28;114(13):E2616-E2623","abstract":"Although normal fatty acids (FAs) are degraded via β-oxidation, unusual FAs such as 2-hydroxy (2-OH) FAs and 3-methyl-branched FAs are degraded via α-oxidation. Phytosphingosine (PHS) is one of the long-chain bases (the sphingolipid components) and exists in specific tissues, including the epidermis and small intestine in mammals. In the degradation pathway, PHS is converted to 2-OH palmitic acid and then to pentadecanoic acid (C15:0-COOH) via FA α-oxidation. However, the detailed reactions and genes involved in the α-oxidation reactions of the PHS degradation pathway have yet to be determined. In the present study, we reveal the entire PHS degradation pathway: PHS is converted to C15:0-COOH via six reactions [phosphorylation, cleavage, oxidation, CoA addition, cleavage (C1 removal), and oxidation], in which the last three reactions correspond to the α-oxidation. The aldehyde dehydrogenase ALDH3A2 catalyzes both the first and second oxidation reactions (fatty aldehydes to FAs). In  Aldh3a2 -deficient cells, the unmetabolized fatty aldehydes are reduced to fatty alcohols and are incorporated into ether-linked glycerolipids. We also identify HACL2 (2-hydroxyacyl-CoA lyase 2) [previous name, ILVBL; ilvB (bacterial acetolactate synthase)-like] as the major 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the FA α-oxidation of the PHS degradation pathway. HACL2 is localized in the endoplasmic reticulum. Thus, in addition to the already-known FA α-oxidation in the peroxisomes, we have revealed the existence of FA α-oxidation in the endoplasmic reticulum in mammals.","doi":"10.1073/pnas.1700138114","authors":"Kitamura T, Seki N, Kihara A","authors_abbrev":"Kitamura T et al.","pubmed_publication_date":"28 Mar 2017","pubmed_entrez_date":"2017-03-15","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007918","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22132734","title":"The yeast Golgi apparatus.","citation":"Traffic 2012 Apr;13(4):505-10","abstract":"The Golgi apparatus is an organelle that has been extensively studied in the model eukaryote, yeast. Its morphology varies among yeast species; the Golgi exists as a system of dispersed cisternae in the case of the budding yeast Saccharomyces cerevisiae, whereas the Golgi cisternae in Pichia pastoris and Schizosaccharomyces pombe are organized into stacks. In spite of the different organization, the mechanism of trafficking through the Golgi apparatus is believed to be similar, involving cisternal maturation, in which the resident Golgi proteins are transported backwards while secretory cargo proteins can stay in the cisternae. Questions remain regarding the organization of the yeast Golgi, the regulatory mechanisms that underlie cisternal maturation of the Golgi and transport machinery of cargo proteins through this organelle. Studies using different yeast species have provided hints to these mechanisms.","doi":"10.1111/j.1600-0854.2011.01316.x","authors":"Suda Y, Nakano A","authors_abbrev":"Suda Y et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2011-12-03","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38097187","title":"Phosphorylation of Bub1 by Mph1 promotes the Bub1 signaling at the kinetochore to ensure accurate chromosome segregation.","citation":"J Biol Chem 2023 Dec 12;:105559","abstract":"Bub1 is a conserved mitotic kinase involved in signaling of the spindle assembly checkpoint (SAC). Multiple phosphorylation sites on Bub1 have been characterized, yet it is challenging to understand the interplay between the multiple phosphorylation sites due to the limited availability of phospho-specific antibodies. In addition, phospho-regulation of Bub1 in Schizosaccharomyces Pombe is poorly understood. Here we report the identification of a new Mph1/Mps1-mediated phosphorylation site, i.e., Ser532, of Bub1 in Schizosaccharomyces Pombe. A phospho-specific antibody against phosphorylated Bub1-Ser532 was developed. Using the phospho-specific antibody, we demonstrated that phosphorylation of Bub1-Ser352 was mediated specifically by Mph1/Mps1 and took place during early mitosis. Moreover, live-cell microscopy showed that inhibition of the phosphorylation of Bub1 at Ser532 impaired the localization of Bub1, Mad1, and Mad2 to the kinetochore. In addition, inhibition of the phosphorylation of Bub1 at Ser532 caused anaphase B lagging chromosomes. Hence, our study constitutes a model in which Mph1/Mps1-mediated phosphorylation of fission yeast Bub1 promotes proper kinetochore localization of Bub1 and faithful chromosome segregation.","doi":"10.1016/j.jbc.2023.105559","authors":"Jian Y, Jiang Y, Nie L, Dou Z, Liu X, Fu C","authors_abbrev":"Jian Y et al.","pubmed_publication_date":"12 Dec 2023","pubmed_entrez_date":"2023-12-14","publication_year":"2023","canto_session_key":"49d7370636fa5c85","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-12-16 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1322.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7479758","title":"Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch.","citation":"Proc Natl Acad Sci U S A 1995 Oct 24;92(22):10232-6","abstract":"The Schizosaccharomyces pombe cell cycle-regulatory protein suc1, named as the suppressor of cdc2 temperature-sensitive mutations, is essential for cell cycle progression. To understand suc1 structure-function relationships and to help resolve conflicting interpretations of suc1 function based on genetic studies of suc1 and its functional homologs in both lower and higher eukaryotes, we have determined the crystal structure of the beta-interchanged suc1 dimer. Each domain consists of three alpha-helices and a four-stranded beta-sheet, completed by the interchange of terminal beta-strands between the two subunits. This beta-interchanged suc1 dimer, when compared with the beta-hairpin single-domain folds of suc1, reveals a beta-hinge motif formed by the conserved amino acid sequence HVPEPH. This beta-hinge mediates the subunit conformation and assembly of suc1: closing produces the intrasubunit beta-hairpin and single-domain fold, whereas opening leads to the intersubunit beta-strand interchange and interlocked dimer assembly reported here. This conformational switch markedly changes the surface accessibility of sequence-conserved residues available for recognition of cyclin-dependent kinase, suggesting a structural mechanism for beta-hinge-mediated regulation of suc1 biological function. Thus, suc1 belongs to the family of domain-swapping proteins, consisting of intertwined and dimeric protein structures in which the dual assembly modes regulate their function.","authors":"Bourne Y, Arvai AS, Bernstein SL, Watson MH, Reed SI, Endicott JE, Noble ME, Johnson LN, Tainer JA","authors_abbrev":"Bourne Y et al.","pubmed_publication_date":"24 Oct 1995","pubmed_entrez_date":"1995-10-24","publication_year":"1995","canto_session_key":"3f3c8437c4b836e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-21 16:01:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-21 16:01:18","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-21","pdb_entries":[{"pdb_id":"1sce","gene_chains":[{"gene_uniquename":"SPBC1734.14c","chain":"A/B/C/D","position":"1-113"}],"title":"CRYSTAL STRUCTURE OF THE CELL CYCLE REGULATORY PROTEIN SUC1 REVEALS A NOVEL BETA-HINGE CONFORMATIONAL SWITCH","entry_authors":"Bourne Y,Tainer JA","entry_authors_abbrev":"Bourne Y et al.","reference_uniquename":"PMID:7479758","experimental_method":"X-ray","resolution":"2.2"}]},{"uniquename":"PMID:38320620","title":"Combining single-molecule and expansion microscopy in fission yeast to visualize protein structures at the nanostructural level.","citation":"Open Biol 2024 Feb;14(2):230414","abstract":"In this work, we have developed an expansion microscopy (ExM) protocol that combines ExM with photoactivated localization microscopy (ExPALM) for yeast cell imaging, and report a robust protocol for single-molecule and expansion microscopy of fission yeast, abbreviated as SExY. Our optimized SExY protocol retains about 50% of the fluorescent protein signal, doubling the amount obtained compared to the original protein retention ExM (proExM) protocol. It allows for a fivefold, highly isotropic expansion of fission yeast cells, which we carefully controlled while optimizing protein yield. We demonstrate the SExY method on several exemplary molecular targets and explicitly introduce low-abundant protein targets (e.g. nuclear proteins such as cbp1 and mis16, and the centromere-specific histone protein cnp1). The SExY protocol optimizations increasing protein yield could be beneficial for many studies, when targeting low abundance proteins, or for studies that rely on genetic labelling for various reasons (e.g. for proteins that cannot be easily targeted by extrinsic staining or in case artefacts introduced by unspecific staining interfere with data quality).","doi":"10.1098/rsob.230414","authors":"Vojnovic I, Caspari OD, Hoşkan MA, Endesfelder U","authors_abbrev":"Vojnovic I et al.","pubmed_publication_date":"Feb 2024","pubmed_entrez_date":"2024-02-06","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-02-08 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42102264","title":"Pseudogene revival drives repeated adaptation in fission yeast.","citation":"Mol Biol Evol 2026 May 01;43(5)","abstract":"Repeated (parallel or convergent) evolution is often taken as evidence of adaptation and is relevant to the predictability of evolution. However, much remains unknown about the genetic basis of repeated evolution. Here, we use genome editing to progressively knock out all the complete transposable elements, a rich source of mutations, in the fission yeast Schizosaccharomyces pombe. While progressive knockout has no apparent effect on the biology or fitness of S. pombe under normal conditions, certain transposable element knockout strains exhibit growth arrest under acid challenge. We next perform parallel replay experiments by evolving S. pombe strains with a single transposable element and without transposable element under acid stress. Adaptation occurs rapidly and repeatedly. We do not detect any new transposable element insertions at appreciable frequencies, indicating that the observed repeated adaptation is not driven by transposable element insertions. Instead, revival mutations in SPBC409.08, a pseudogene that encodes a putative transporter of the major facilitator superfamily, repeatedly undergo hard or soft selective sweeps and drive adaptation in all the replicates. Although the revival mutations exhibit a trend of diminishing returns, they also repeatedly become fixed in all evolved wild-type populations. This work unveils the significance of pseudogene revival on repeated evolution and thus evolutionary predictability.","doi":"10.1093/molbev/msag120","authors":"Wu Z, Liu X, Xu H, Han GZ","authors_abbrev":"Wu Z et al.","pubmed_publication_date":"01 May 2026","pubmed_entrez_date":"2026-05-08","publication_year":"2026","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2026-05-08 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31719163","title":"A novel interplay between GEFs orchestrates Cdc42 activity during cell polarity and cytokinesis in fission yeast.","citation":"J Cell Sci 2019 Dec 03;132(23)","abstract":"Cdc42, a conserved regulator of cell polarity, is activated by two GEFs, Gef1 and Scd1, in fission yeast. Why the cell needs two GEFs is unclear, given that they are partially redundant and activate the same GTPase. Using the GEF localization pattern during cytokinesis as a paradigm, we report a novel interplay between Gef1 and Scd1 that spatially modulates Cdc42. We find that Gef1 promotes Scd1 localization to the division site during cytokinesis through recruitment of the scaffold protein Scd2, via a Cdc42 feedforward pathway. Similarly, during interphase Gef1 promotes Scd1 recruitment at the new end to enable the transition from monopolar to bipolar growth. Reciprocally, Scd1 restricts Gef1 localization to prevent ectopic Cdc42 activation during cytokinesis to promote cell separation, and to maintain cell shape during interphase. Our findings reveal an elegant regulatory pattern in which Gef1 primes Cdc42 activation at new sites to initiate Scd1-dependent polarized growth, while Scd1 restricts Gef1 to sites of polarization. We propose that crosstalk between GEFs is a conserved mechanism that orchestrates Cdc42 activation during complex cellular processes.This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.236018","authors":"Hercyk BS, Rich-Robinson J, Mitoubsi AS, Harrell MA, Das ME","authors_abbrev":"Hercyk BS et al.","pubmed_publication_date":"03 Dec 2019","pubmed_entrez_date":"2019-11-14","publication_year":"2019","canto_session_key":"721bf4355105bfb4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maitreyi Das","canto_first_approved_date":"2020-02-12 15:26:34","canto_approved_date":"2026-04-02 15:30:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-01-31 19:09:02","canto_added_date":"2019-11-15 01:15:05","annotation_curators":[{"name":"Maitreyi Das","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.14c","SPAC24H6.09","SPAC22H10.07","SPBC336.12c","SPAC16E8.09","SPAC110.03"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2020-02-12"},{"uniquename":"GO_REF:0000012","title":"Pairwise alignment (TIGR)","abstract":"Pairwise alignments are generated by taking two sequences and aligning them so that the maximum number of amino acids in each protein match, or are similar to, each other. Tools such as BLAST work by comparing a protein-of-interest individually with every protein in a database of known protein sequences and retaining only those matches with a high probability of being significant. Basic BLAST generates local alignments between proteins for regions of high similarity. Other pairwise alignment tools attempt to generate global (full-length) protein alignments. A tool called Blast_Extend_repraze (BER, http://ber.sourceforge.net) has some benefits over basic BLAST. Input into the BER tool includes the underlying DNA sequence for each protein as well as 300 nucleotides upstream and downstream of the predicted boundaries of the protein coding sequence. This allows annotators to see the DNA sequence that underlies the query protein as part of the alignment. In addition, the BER tool is able to look for continuation of regions of similarity through frameshifts and in-frame stop codons.  If such regions are found the alignment is continued. BER searches are done in a two-step process: step one is a BLAST search against a non-redundant protein database, significant BLAST hits are stored in a mini-database for each query protein; step two is a modified Smith-Waterman alignment between the query and the proteins in its mini-database. In order to assess whether a given BER alignment is good enough to assert that the query shares the function of the match protein, one must look at a several factors. First of all, the match protein must itself be experimentally characterized in order to avoid transitive annotation errors. In addition, any residues or secondary structures known to be important for function in the match protein must be conserved in the query. The alignment should be visually inspected to look for any areas of lesser quality that might indicate the two proteins do not share the same function. Although it is impossible to set cutoff values for percent identity and length of match that will apply for every alignment, there are some guidelines. In general at least 40% identity that extends over the full lengths of both proteins is required in order to even consider functional equivalence. However, this percentage is highly dependent on the length and complexity of the proteins. 40% identity between two proteins 500 amino acids long is much more significant that 40% identity between two proteins that are only 100 amino acids long. Therefore, the annotator's experience and knowledge of what is considered significant for the organism and protein family in question is very important. Some sets of proteins are much more highly conserved than others and therefore tolerances for percent identity may have to be adjusted. Finally, the alignment must be considered in the context of what else is known about the query protein and the organism as a whole.","authors":"Michelle Gwinn, TIGR curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22084378","title":"Nutrient limitations alter cell division control and chromosome segregation through growth-related kinases and phosphatases.","citation":"Philos Trans R Soc Lond B Biol Sci 2011 Dec 27;366(1584):3508-20","abstract":"In dividing fission yeast Schizosaccharomyces pombe cells, the balance between Wee1 kinase and Cdc25 phosphatase which control the cyclin-dependent kinase (CDK) at the G2-M transition determines the rod-shaped cell length. Under nitrogen source starvation or glucose limitation, however, cell size determination is considerably modulated, and cell size shortening occurs for wild-type cells. For several mutants of kinases or phosphatases, including CDK, target of rapamycin complex (TORC) 1 and 2, stress-responsive mitogen-activated protein kinase (MAPK) Sty1/Spc1, MAPK kinase Wis1, calcium- and calmodulin-dependent protein kinase kinase-like Ssp1, and type 2A and 2A-related phosphatases inhibitor Sds23, this cell shortening does not normally occur. In tor1 and ssp1 mutants, cell elongation is observed. Sds23 that binds to and inhibits 2A and 2A-related phosphatases is synergistic with Ssp1 in the cell size determination and survival under low glucose and nitrogen source. Tor2 (TORC1) is required for growth, whereas Tor1 (TORC2) is needed for determining division size according to different nutrient conditions. Surprisingly, in growth-diminished tor2 mutant or rapamycin-treated cells, the requirement of separase/Cut1-securin/Cut2 essential for chromosome segregation is greatly alleviated. By contrast, defects of tor1 with secruin/cut2 or overproduction of Cut1 are additive. While Tor1 and Tor2 are opposite in their apparent functions, both may actually coordinate cell division with growth in response to the changes in nutrients.","doi":"10.1098/rstb.2011.0124","authors":"Yanagida M, Ikai N, Shimanuki M, Sajiki K","authors_abbrev":"Yanagida M et al.","pubmed_publication_date":"27 Dec 2011","pubmed_entrez_date":"2011-11-16","publication_year":"2011","canto_session_key":"6d612ce099b2b02a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-16 10:40:18","canto_approved_date":"2021-10-31 16:58:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-16 10:40:09","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC11B10.09","SPCC297.03","SPAC24B11.06c","SPBC216.07c","SPBC409.07c","SPBC14C8.01c","SPBC30D10.10c","SPCC5E4.04","SPBC27B12.04c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2015-02-16"},{"uniquename":"PMID:21099360","title":"Hsk1 kinase and Cdc45 regulate replication stress-induced checkpoint responses in fission yeast.","citation":"Cell Cycle 2010 Dec 01;9(23):4627-37","abstract":"In fission yeast, replication fork arrest activates the replication checkpoint effector kinase Cds1(Chk2/Rad53) through the Rad3(ATR/Mec1)-Mrc1(Claspin) pathway. Hsk1, the Cdc7 homologue of fission yeast required for efficient initiation of DNA replication, is also required for Cds1 activation. Hsk1 kinase activity is required for induction and maintenance of Mrc1 hyperphosphorylation, which is induced by replication fork block and mediated by Rad3. Rad3 kinase activity does not change in an hsk1 temperature-sensitive mutant, and Hsk1 kinase activity is not affected by rad3 mutation. Hsk1 kinase vigorously phosphorylates Mrc1 in vitro, predominantly at non-SQ/TQ sites, but this phosphorylation does not seem to affect the Rad3 action on Mrc1. Interestingly, the replication stress-induced activation of Cds1 and hyperphosphorylation of Mrc1 is almost completely abrogated in an initiation-defective mutant of cdc45, but not in an mcm2 or polε mutant. The results suggest that Hsk1-mediated loading of Cdc45 onto replication origins may play important roles in replication stress-induced checkpoint.","authors":"Matsumoto S, Shimmoto M, Kakusho N, Yokoyama M, Kanoh Y, Hayano M, Russell P, Masai H","authors_abbrev":"Matsumoto S et al.","pubmed_publication_date":"01 Dec 2010","pubmed_entrez_date":"2010-11-25","publication_year":"2010","canto_session_key":"5da0f1305d21c994","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-01-21 23:43:21","canto_approved_date":"2020-01-23 13:32:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-03 17:00:04","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":51,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC694.06c","SPBC776.12c","SPCC18B5.11c","SPBC216.06c","SPAC17D4.02","SPBC4.04c","SPCC18B5.03","SPBC216.05","SPBC25H2.13c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-01-21"},{"uniquename":"PMID:17150956","title":"Identification and Characterization of a Schizosaccharomyces pombe RNA Polymerase II Elongation Factor with Similarity to the Metazoan Transcription Factor ELL.","citation":"J Biol Chem 2007 Feb 23;282(8):5761-9","abstract":"ELL family transcription factors activate the rate of transcript elongation by suppressing transient pausing by RNA polymerase II at many sites along the DNA. ELL-associated factors 1 and 2 (EAF1 and EAF2) bind stably to ELL family members and act as strong positive regulators of their transcription activities. Orthologs of ELL and EAF have been identified in metazoa, but it has been unclear whether such RNA polymerase II elongation factors are utilized in lower eukaryotes. Using bioinformatic and biochemical approaches, we have identified a new Schizosaccharomyces pombe RNA polymerase II elongation factor that is composed of two subunits designated SpELL and SpEAF, which share weak sequence similarity with members of the metazoan ELL and EAF families. Like mammalian ELL-EAF, SpELL-SpEAF stimulates RNA polymerase II transcription elongation and pyrophosphorolysis. In addition, like many yeast RNA polymerase II elongation factors, deletion of the SpELL gene renders S. pombe sensitive to the drug 6-azauracil. Finally, phylogenetic analyses suggest that the SpELL and SpEAF proteins are evolutionarily conserved in many fungi but not in Saccharomyces cerevisiae.","authors":"Banks CA, Kong SE, Spahr H, Florens L, Martin-Brown S, Washburn MP, Conaway JW, Mushegian A, Conaway RC","authors_abbrev":"Banks CA et al.","pubmed_publication_date":"23 Feb 2007","pubmed_entrez_date":"2006-12-08","publication_year":"2007","canto_session_key":"20f5e1ab06f9d016","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-12-18 16:52:43","canto_approved_date":"2022-06-06 18:13:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-15 16:52:15","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP23A10.14c","SPCC1223.10c","SPBC28F2.12"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-12-18"},{"uniquename":"PMID:23851147","title":"Citrinin-induced fluidization of the plasma membrane of the fission yeast Schizosaccharomyces pombe.","citation":"Food Chem Toxicol 2013 Sep;59:636-42","abstract":"Citrinin (CTN) is a toxic fungal metabolite that is a hazardous contaminant of foods and feeds. In the present study, its acute toxicity and effects on the plasma membrane of Schizosaccharomyces pombe were investigated. The minimum inhibitory concentration of CTN against the yeast cells proved to be 500 μM. Treatment with 0, 250, 500 or 1000 μM CTN for 60 min resulted in a 0%, 2%, 21% or 100% decrease, respectively, in the survival rate of the cell population. Treatment of cells with 0, 100, 500 or 1000 μM CTN for 20 min induced decrease in the phase-transition temperature of the 5-doxylstearic acid-labeled plasma membrane to 16.51, 16.04, 14.18 or 13.98°C, respectively as measured by electron paramagnetic resonance spectroscopy. This perturbation was accompanied by the efflux of essential K⁺ from the cells. The existence of an interaction between CTN and glutathione was detected for the first time by spectrofluorometry. Our observations may suggest a direct interaction of CTN with the free sulfhydryl groups of the integral proteins of the plasma membrane, leading to dose-dependent membrane fluidization. The change in fluidity disturbed the ionic homeostasis, contributing to the death of the cells, which is a novel aspect of CTN cytotoxicity.","doi":"10.1016/j.fct.2013.07.006","authors":"Blaskó Á, Mike N, Gróf P, Gazdag Z, Czibulya Z, Nagy L, Kunsági-Máté S, Pesti M","authors_abbrev":"Blaskó Á et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-07-16","publication_year":"2013","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14704204","title":"Fission yeast Mus81.Eme1 Holliday junction resolvase is required for meiotic crossing over but not for gene conversion.","citation":"Genetics 2003 Dec;165(4):2289-93","abstract":"Most models of homologous recombination invoke cleavage of Holliday junctions to explain crossing over. The Mus81.Eme1 endonuclease from fission yeast and humans cleaves Holliday junctions and other branched DNA structures, leaving its physiological substrate uncertain. We report here that Schizosaccharomyces pombe mus81 mutants have normal or elevated frequencies of gene conversion but 20- to 100-fold reduced frequencies of crossing over. Thus, gene conversion and crossing over can be genetically separated, and Mus81 is required for crossing over, supporting the hypothesis that the fission yeast Mus81.Eme1 protein complex resolves Holliday junctions in meiotic cells.","authors":"Smith GR, Boddy MN, Shanahan P, Russell P","authors_abbrev":"Smith GR et al.","pubmed_publication_date":"Dec 2003","pubmed_entrez_date":"2004-01-06","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1E7.06c","SPCC4G3.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:24866294","title":"Is there a universal rule for cellular growth?--Problems in studying and interpreting this phenomenon.","citation":"FEMS Yeast Res 2014 Aug;14(5):679-82","abstract":"","doi":"10.1111/1567-1364.12168","authors":"Sveiczer Á, Horváth A, Buchwald P","authors_abbrev":"Sveiczer Á et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-05-29","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32930427","title":"Metabolism of Storage Lipids and the Role of Lipid Droplets in the Yeast Schizosaccharomyces pombe.","citation":"Lipids 2020 Sep;55(5):513-535","abstract":"Storage lipids, triacylglycerols (TAG), and steryl esters (SE), are predominant constituents of lipid droplets (LD) in fungi. In several yeast species, metabolism of TAG and SE is linked to various cellular processes, including cell division, sporulation, apoptosis, response to stress, and lipotoxicity. In addition, TAG are an important source for the generation of value-added lipids for industrial and biomedical applications. The fission yeast Schizosaccharomyces pombe is a widely used unicellular eukaryotic model organism. It is a powerful tractable system used to study various aspects of eukaryotic cellular and molecular biology. However, the knowledge of S. pombe neutral lipids metabolism is quite limited. In this review, we summarize and discuss the current knowledge of the homeostasis of storage lipids and of the role of LD in the fission yeast S. pombe with the aim to stimulate research of lipid metabolism and its connection with other essential cellular processes. We also discuss the advantages and disadvantages of fission yeast in lipid biotechnology and recent achievements in the use of S. pombe in the biotechnological production of valuable lipid compounds.","doi":"10.1002/lipd.12275","authors":"Hapala I, Griac P, Holic R","authors_abbrev":"Hapala I et al.","pubmed_publication_date":"Sep 2020","pubmed_entrez_date":"2020-09-15","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-09-17 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1718.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU013721","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7706319","title":"The rad21 gene product of Schizosaccharomyces pombe is a nuclear, cell cycle-regulated phosphoprotein.","citation":"J Biol Chem 1995 Mar 31;270(13):7703-11","abstract":"The rad21 gene of Schizosaccharomyces pombe is involved in the repair of double-strand breaks in DNA and is essential for mitotic growth (Birkenbihl, R. P., and Subramani, S. (1992) Nucleic Acids Res. 20, 6605-6611). We show that the Rad21 protein migrates with an aberrantly slow mobility, has a thrombin cleavage site, and is multiply phosphorylated mainly at serine residues. The expression of the rad21 mRNA and the Rad21 protein is cell cycle-regulated, with the peak of mRNA and protein expression occurring near the G1 to S transition. Following translation of the protein, hypophosphorylated forms of the protein appear. However, the most phosphorylated form of Rad21 appears only later in the cell cycle (in S to G2). Analysis of the radiosensitive mutant rad21-45 revealed that the mutant protein is permanently hypophosphorylated. The Rad21 protein is nuclear during the cell cycle. The nuclear localization signal was identified in the C-terminal third of the protein. Upon repression of the Rad21 protein expressed from the repressible nmt1 promoter, the unphosphorylated and hypophosphorylated forms of Rad21 disappeared first. When the concentration of the most highly phosphorylated form of Rad21 sank under a critical level, the cells underwent aberrant mitoses. They exhibited loss of proper nuclear organization and abnormal septation.","authors":"Birkenbihl RP, Subramani S","authors_abbrev":"Birkenbihl RP et al.","pubmed_publication_date":"31 Mar 1995","pubmed_entrez_date":"1995-03-31","publication_year":"1995","canto_session_key":"394a9becc3abea7c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-12-22 16:12:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-20 13:12:03","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-20"},{"uniquename":"PMID:18334479","title":"Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus.","citation":"J Biol Chem 2008 May 16;283(20):14022-31","abstract":"The assembly of core histones onto eukaryotic DNA is modulated by several histone chaperone complexes, including Asf1, CAF-1, and HIRA. Asf1 is a unique histone chaperone that participates in both the replication-dependent and replication-independent pathways. Here we report the crystal structures of the apo-form of fission yeast Asf1/Cia1 (SpAsf1N; residues 1-161) as well as its complexes with the B-domain of the fission yeast HIRA orthologue Hip1 (Hip1B) and the C-terminal region of the Cac2 subunit of CAF-1 (Cac2C). The mode of the fission yeast Asf1N-Hip1B recognition is similar to that of the human Asf1-HIRA recognition, suggesting that Asf1N recognition of Hip1B/HIRA is conserved from yeast to mammals. Interestingly, Hip1B and Cac2C show remarkably similar interaction modes with Asf1. The binding between Asf1N and Hip1B was almost completely abolished by the D37A and L60A/V62A mutations in Asf1N, indicating the critical role of salt bridge and van der Waals contacts in the complex formation. Consistently, both of the aforementioned Asf1 mutations also drastically reduced the binding to Cac2C. These results provide a structural basis for a mutually exclusive Asf1-binding model of CAF-1 and HIRA/Hip1, in which Asf1 and CAF-1 assemble histones H3/H4 (H3.1/H4 in vertebrates) in a replication-dependent pathway, whereas Asf1 and HIRA/Hip1 assemble histones H3/H4 (H3.3/H4 in vertebrates) in a replication-independent pathway.","doi":"10.1074/jbc.M800594200","authors":"Malay AD, Umehara T, Matsubara-Malay K, Padmanabhan B, Yokoyama S","authors_abbrev":"Malay AD et al.","pubmed_publication_date":"16 May 2008","pubmed_entrez_date":"2008-03-13","publication_year":"2008","canto_session_key":"a1a1f5556ca099b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-06 15:07:46","canto_approved_date":"2024-01-19 15:07:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-06 15:07:39","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC663.05c","SPAC26H5.03","SPBC31F10.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-10-06","pdb_entries":[{"pdb_id":"2cu9","gene_chains":[{"gene_uniquename":"SPCC663.05c","chain":"A","position":"1-161"}],"title":"Crystal structure of Histone chaperone cia1","entry_authors":"Padmanabhan B,Yokoyama S,RIKEN Structural Genomics/Proteomics Initiative (RSGI)","entry_authors_abbrev":"Padmanabhan B et al.","reference_uniquename":"PMID:18334479","experimental_method":"X-ray","resolution":"1.8"},{"pdb_id":"2z34","gene_chains":[{"gene_uniquename":"SPCC663.05c","chain":"A/B","position":"1-161"},{"gene_uniquename":"SPBC31F10.13c","chain":"C/D","position":"469-497"}],"title":"Crystal structure of SpCia1/Asf1 complex with Hip1","entry_authors":"Malay AD,Padmanabhan B,Yokoyama S,RIKEN Structural Genomics/Proteomics Initiative (RSGI)","entry_authors_abbrev":"Malay AD et al.","reference_uniquename":"PMID:18334479","experimental_method":"X-ray","resolution":"2.4"},{"pdb_id":"2z3f","gene_chains":[{"gene_uniquename":"SPAC26H5.03","chain":"I/J/K/L/M/N/O/P/Q/R/T","position":"493-512"},{"gene_uniquename":"SPCC663.05c","chain":"A/B/C/D/E/F/G/H","position":"1-161"}],"title":"Crystal structure of spCia1/Asf1 complexed with Cac2 peptide","entry_authors":"Malay AD,Padmanabhan B,Yokoyama S,RIKEN Structural Genomics/Proteomics Initiative (RSGI)","entry_authors_abbrev":"Malay AD et al.","reference_uniquename":"PMID:18334479","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:28600551","title":"Epe1 contributes to activation of AMPK by promoting phosphorylation of AMPK alpha subunit, Ssp2.","citation":"Sci Rep 2017 Jun 09;7(1):3208","abstract":"AMP-activated protein kinase (AMPK) is a pivotal cellular energy sensor. It is activated by stresses that cause depletion of energy and initiates adaptive responses by regulating metabolism balance. AMPK forms αβγ heterotrimer. In fission yeast, activation of AMPK mainly depends on the phosphorylation of AMPKα subunit Ssp2 at Thr 189  by upstream kinase Ssp1. However, not much is known about the regulation of this process. In this study, we identified Epe1 as a novel positive regulator of AMPK. Epe1, a jmjC-domain-containing protein, is best-known as a negative regulator of heterochromatin spreading. Although the novel role of Epe1 in regulation of AMPK relies on predicted iron- and 2-oxyglutarate-binding residues inside jmjC domain, it seems to be irrelevant to inhibition of heterochromatin spreading. Epe1 is associated with Ssp2 directly and promotes phosphorylation of Ssp2 upon various environmental stresses, including low-glucose, high-sodium, high-pH and oxidative conditions. Similar to Epe1, Jmj1 and Msc1 also contribute to phosphorylation of Ssp2. Deletion of epe1  +  impairs downstream events following phosphorylation of Ssp2, including nuclear translocation of Ssp2, sexual differentiation and inhibition of fatty acid synthesis. Our study reveals a novel way in which a jmjC-domain-containing protein regulates adaptive response by directly binding to a principal sensor.","doi":"10.1038/s41598-017-03442-0","authors":"Chen Y, Hu X, Guo C, Yu Y, Lu H","authors_abbrev":"Chen Y et al.","pubmed_publication_date":"09 Jun 2017","pubmed_entrez_date":"2017-06-11","publication_year":"2017","canto_session_key":"d150d3eeabbfefdd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-14 15:56:17","canto_approved_date":"2022-01-16 08:50:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-11-14 15:55:53","canto_added_date":"2017-06-12 00:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":63,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC74.03c","SPCC622.16c","SPCC297.03","SPAC343.11c","SPAC17G8.13c","SPAC1002.05c","SPCC622.19","SPAC25H1.02","SPCC1919.03c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2018-11-14"},{"uniquename":"PMID:12032307","title":"A single unbranched S-phase DNA damage and replication fork blockage checkpoint pathway.","citation":"Proc Natl Acad Sci U S A 2002 May 28;99(11):7472-7","abstract":"The eukaryotic intra-S-phase checkpoint, which slows DNA synthesis in response to DNA damage, is poorly understood. Is DNA damage recognized directly, or indirectly through its effects on replication forks? Is the slowing of S phase in part because of competition between DNA synthesis and recombination/repair processes? The results of our genetic analyses of the intra-S-phase checkpoint in the fission yeast, Schizosaccharomyces pombe, suggest that the slowing of S phase depends weakly on the helicases Rqh1 and Srs2 but not on other recombination/repair pathways. The slowing of S phase depends strongly on the six checkpoint-Rad proteins, on Cds1, and on Rad4/Cut5 (similar to budding yeast Dpb11, which interacts with DNA polymerase epsilon) but not on Rhp9 (similar to budding yeast Rad9, necessary for direct damage recognition). These results suggest that, in fission yeast, the signal activating the intra-S-phase checkpoint is generated only when replication forks encounter DNA damage.","authors":"Marchetti MA, Kumar S, Hartsuiker E, Maftahi M, Carr AM, Freyer GA, Burhans WC, Huberman JA","authors_abbrev":"Marchetti MA et al.","pubmed_publication_date":"28 May 2002","pubmed_entrez_date":"2002-05-29","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.05","SPAC20G4.04c","SPAC1952.07","SPAC664.07c","SPCC18B5.11c","SPAC9E9.08","SPAC14C4.13"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:17446861","title":"Specific functions for the fission yeast Sirtuins Hst2 and Hst4 in gene regulation and retrotransposon silencing.","citation":"EMBO J 2007 May 16;26(10):2477-88","abstract":"Expression profiling, ChiP-CHIP and phenotypic analysis were used to investigate the functional relationships of class III NAD(+)-dependent HDACs (Sirtuins) in fission yeast. We detected significant histone acetylation increases in Sirtuin mutants at their specific genomic binding targets and were thus able to identify an in vivo substrate preference for each Sirtuin. At heterochromatic loci, we demonstrate that although Hst2 is mainly cytoplasmic, a nuclear pool of Hst2 colocalizes with the other Sirtuins at silent regions (cen, mat, tel, rDNA), and that like the other Sirtuins, Hst2 is required for rDNA and centromeric silencing. Interestingly we found specific functions for the fission yeast Sirtuins Hst2 and Hst4 in gene regulation. Hst2 directly represses genes involved in transport and membrane function, whereas Hst4 represses amino-acid biosynthesis genes and Tf2 retrotransposons. A specific role for Hst4 in Tf2 5' mRNA processing was revealed. Thus, Sirtuins share functions at many genomic targets, but Hst2 and Hst4 have also evolved unique functions in gene regulation.","authors":"Durand-Dubief M, Sinha I, Fagerström-Billai F, Bonilla C, Wright A, Grunstein M, Ekwall K","authors_abbrev":"Durand-Dubief M et al.","pubmed_publication_date":"16 May 2007","pubmed_entrez_date":"2007-04-21","publication_year":"2007","canto_session_key":"e94ce18ecdb1e796","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-09-16 13:20:20","canto_approved_date":"2022-01-18 15:29:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 17:03:17","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":47,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.07c","SPBC29A10.07","SPAC1783.04c","SPCC132.02"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-09-16"},{"uniquename":"PMID:19528228","title":"Smc5-Smc6-dependent removal of cohesin from mitotic chromosomes.","citation":"Mol Cell Biol 2009 Aug;29(16):4363-75","abstract":"The function of the essential cohesin-related Smc5-Smc6 complex has remained elusive, though hypomorphic mutants have defects late in recombination, in checkpoint maintenance, and in chromosome segregation. Recombination and checkpoints are not essential for viability, and Smc5-Smc6-null mutants die in lethal mitoses. This suggests that the chromosome segregation defects may be the source of lethality in irradiated Smc5-Smc6 hypomorphs. We show that in smc6 mutants, following DNA damage in interphase, chromosome arm segregation fails due to an aberrant persistence of cohesin, which is normally removed by the Separase-independent pathway. This postanaphase persistence of cohesin is not dependent on DNA damage, since the synthetic lethality of smc6 hypomorphs with a topoisomerase II mutant, defective in mitotic chromosome structure, is also due to the retention of cohesin on undamaged chromosome arms. In both cases, Separase overexpression bypasses the defect and restores cell viability, showing that defective cohesin removal is a major determinant of the mitotic lethality of Smc5-Smc6 mutants.","doi":"10.1128/MCB.00377-09","authors":"Outwin EA, Irmisch A, Murray JM, O'Connell MJ","authors_abbrev":"Outwin EA et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-06-17","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC5E4.04","SPBC1A4.03c","SPCC5E4.06","SPAC16A10.06c","SPBC1921.02","SPBC582.05c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:12477395","title":"Proteomics analysis identifies new components of the fission and budding yeast anaphase-promoting complexes.","citation":"Curr Biol 2002 Dec 10;12(23):2048-54","abstract":"The anaphase-promoting complex (APC) is a conserved multisubunit ubiquitin ligase required for the degradation of key cell cycle regulators. Components of the APC have been identified through genetic screens in both Schizosaccharomyces pombe and Saccharomyces cerevisiae as well as through biochemical purification coupled with mass spectrometric protein identification. With these approaches, 11 subunits of the core S. cerevisiae APC have been identified. Here, we have applied a tandem affinity purification approach coupled with direct analysis of the purified complexes by mass spectrometry (DALPC) to reveal additional subunits of both the S. pombe and S. cerevisiae APCs. Our data increase the total number of identified APC subunits to 13 in both yeasts and indicate that previous approaches were biased against the identification of small subunits. These results underscore the power of direct analysis of protein complexes by mass spectrometry and set the foundation for further functional and structural studies of the APC.","authors":"Yoon HJ, Feoktistova A, Wolfe BA, Jennings JL, Link AJ, Gould KL","authors_abbrev":"Yoon HJ et al.","pubmed_publication_date":"10 Dec 2002","pubmed_entrez_date":"2002-12-13","publication_year":"2002","canto_session_key":"934d34f3696c1f31","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-09 09:13:59","canto_approved_date":"2021-11-29 21:21:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-28 14:27:14","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.09","SPBC1A4.01","SPAC959.09c","SPBC83.04","SPBP23A10.04","SPAC23C11.12","SPAC343.03","SPBC28E12.01c","SPAC19G12.01c","SPAC6F12.14","SPAC17C9.01c","SPAC6F12.15c","SPAC27D7.05c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2015-06-09"},{"uniquename":"PMID:3068351","title":"Genetic manipulation of non-conventional yeasts by conventional and non-conventional methods.","citation":"J Basic Microbiol 1988;28(5):321-33","abstract":"In recent years, yeasts other than those belonging to the species Saccharomyces cerevisiae and Schizosaccharomyces pombe have become increasingly important in industrial processes. Species such as Pichia stipitis, Hansenula polymorpha, Zygosaccharomyces rouxii, Saccharomyces exiguus, Torulaspora delbrueckii, Yarrowia lipolytica and others whose perfect stage is known, can be manipulated genetically by classical methods, but those belonging to the genera Candida (C. utilis, C. tropicalis, C. bombicola, C. zeylanoides, C. boidinii, etc.), Brettanomyces, Cryptococcus, Rhodotorula, and others of the different form genera, cannot be treated in this way. Some, such as Schwanniomyces and Debaryomyces spp., which have a perfect stage, are still difficult to manipulate by conventional means. Genetic manipulation of these yeasts can be approached from two points of view; the first involving improvement of strains by cross-breeding within one species, and the second, the introduction of desirable genes from unrelated species and even from plants or animals. Two techniques are available for construction of industrially-useful strains from these yeasts: protoplast fusion and transformation with chimaeric plasmids containing the gene(s) it is desired to introduce into the recipient strain. The methods for the latter procedure are well known but can be laborious and time-consuming, especially if it is desired to introduce genes from plant or animal sources for production of enzymes, hormones, vaccines and similar products. Protoplast fusion is a simple technique which can be utilized in most laboratories and used for construction of improved yeast strains for brewing, baking, ethanol production and wine-making, either by the fusion of desirable strains of the same species which do not sporulate, or by introduction of genes from non-Saccharomyces species. Methods for fusion of species from different genera and isolation of the desired hybrids have been improved considerably in recent years. We have developed a method for isolation of strains carrying the desired genes by fusing a non-Saccharomyces species with an auxotrophic strain of Saccharomyces cerevisiae and selecting hybrids having the desired characteristics on appropriate media, after which the genes are transferred to the industrial strain by rare-mating, repeated protoplast fusion, or classical mating as required. The advantages and limitations of the method are under investigation.","authors":"Spencer JF, Spencer DM, Reynolds N","authors_abbrev":"Spencer JF et al.","pubmed_publication_date":"1988","pubmed_entrez_date":"1988-01-01","publication_year":"1988","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11069779","title":"The SHR3 homologue from S. pombe demonstrates a conserved function of ER packaging chaperones.","citation":"J Cell Sci 2000 Dec;113 Pt 23:4351-62","abstract":"In Saccharomyces cerevisiae cells lacking SHR3, amino acid permeases do not enter into COPII transport vesicles and specifically accumulate in the membrane of the endoplasmic reticulum. Shr3p functions as a packaging chaperone to prime transport vesicle formation in the proximity of amino acid permeases. A genetic screen was developed that enabled the Schizosaccharomyces pombe SHR3 functional homologue, designated psh3(+) (pombe SHR3), to be cloned. The psh3(+) gene encodes a protein of 215 amino acids, which shares a high degree of structural and functional similarity with Shr3p. The heterologous expression of psh3(+) complements many, but not all, shr3 null mutant phenotypes in S. cerevisiae in a temperature-dependent manner. Psh3p is localised to the endoplasmic reticulum of S. pombe cells, and strains lacking the psh3(+ )gene exhibit decreased rates of amino acid uptake due to reduced levels of functional permeases in the plasma membrane. No packaging chaperones, or proteins exhibiting homology with packaging chaperones, have so far been identified in other eukayotic organisms. The findings reported here are the first to establish that specific packaging chaperones exist in divergent organisms, and demonstrate a conserved function of packaging chaperones in facilitating the export of large polytopic membrane proteins from the endoplasmic reticulum.","authors":"Martínez P, Ljungdahl PO","authors_abbrev":"Martínez P et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-09","publication_year":"2000","canto_session_key":"7186b912b1fbca8b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-18 16:51:52","canto_approved_date":"2023-07-22 08:38:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-18 16:44:53","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.20c","SPBC1A4.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-09-18"},{"uniquename":"PMID:34980915","title":"SignalP 6.0 predicts all five types of signal peptides using protein language models.","citation":"Nat Biotechnol 2022 Jul;40(7):1023-1025","abstract":"Signal peptides (SPs) are short amino acid sequences that control protein secretion and translocation in all living organisms. SPs can be predicted from sequence data, but existing algorithms are unable to detect all known types of SPs. We introduce SignalP 6.0, a machine learning model that detects all five SP types and is applicable to metagenomic data.","doi":"10.1038/s41587-021-01156-3","authors":"Teufel F, Almagro Armenteros JJ, Johansen AR, Gíslason MH, Pihl SI, Tsirigos KD, Winther O, Brunak S, von Heijne G, Nielsen H","authors_abbrev":"Teufel F et al.","pubmed_publication_date":"Jul 2022","pubmed_entrez_date":"2022-01-04","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6G10.09","SPAPB2B4.01c","SPBC1683.08","SPAC4A8.04","SPAC926.10","SPBC14C8.11c","SPCC548.07c","SPAC1F8.01","SPBC1347.05c","SPBC4B4.08","SPCC1235.13","SPAC17G6.03","SPBC2G5.01","SPAC4G8.12c","SPBC3D6.05","SPBC21C3.16c","SPBPB2B2.18","SPCC1235.14","SPCC330.21"],"gene_count":19,"ltp_gene_count":0},{"uniquename":"PMID:24652833","title":"Spd2 assists Spd1 in the modulation of ribonucleotide reductase architecture but does not regulate deoxynucleotide pools.","citation":"J Cell Sci 2014 Jun 01;127(Pt 11):2460-70","abstract":"In yeasts, small intrinsically disordered proteins (IDPs) modulate ribonucleotide reductase (RNR) activity to ensure an optimal supply of dNTPs for DNA synthesis. The Schizosaccharomyces pombe Spd1 protein can directly inhibit the large RNR subunit (R1), import the small subunit (R2) into the nucleus and induce an architectural change in the R1-R2 holocomplex. Here, we report the characterization of Spd2, a protein with sequence similarity to Spd1. We show that Spd2 is a CRL4(Cdt2)-controlled IDP that functions together with Spd1 in the DNA damage response and in modulation of RNR architecture. However, Spd2 does not regulate dNTP pools and R2 nuclear import. Furthermore, deletion of spd2 only weakly suppresses the Rad3(ATR) checkpoint dependency of CRL4(Cdt2) mutants. However, when we raised intracellular dNTP pools by inactivation of RNR feedback inhibition, deletion of spd2 could suppress the checkpoint dependency of CRL4(Cdt2) mutant cells to the same extent as deletion of spd1. Collectively, these observations suggest that Spd1 on its own regulates dNTP pools, whereas in combination with Spd2 it modulates RNR architecture and sensitizes cells to DNA damage.","doi":"10.1242/jcs.139816","authors":"Vejrup-Hansen R, Fleck O, Landvad K, Fahnøe U, Broendum SS, Schreurs AS, Kragelund BB, Carr AM, Holmberg C, Nielsen O","authors_abbrev":"Vejrup-Hansen R et al.","pubmed_publication_date":"01 Jun 2014","pubmed_entrez_date":"2014-03-22","publication_year":"2014","canto_session_key":"d00159ad077f1b3c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-12-19 20:16:35","canto_approved_date":"2022-08-31 19:25:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-19 20:16:17","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":69,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPAC17H9.19c","SPAC3F10.19","SPBC215.03c","SPAC17H9.10c","SPBC25D12.04","SPAC29B12.03","SPBC216.05"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-12-19"},{"uniquename":"PMID:37156397","title":"Identification of novel coenzyme Q 10  biosynthetic proteins Coq11 and Coq12 in Schizosaccharomyces pombe.","citation":"J Biol Chem 2023 Jun;299(6):104797","abstract":"Coenzyme Q (CoQ) is an essential component of the electron transport system in aerobic organisms. CoQ 10  has ten isoprene units in its quinone structure and is especially valuable as a food supplement. However, the CoQ biosynthetic pathway has not been fully elucidated, including synthesis of the p-hydroxybenzoic acid (PHB) precursor to form a quinone backbone. To identify the novel components of CoQ 10  synthesis, we investigated CoQ 10  production in 400 Schizosaccharomyces pombe gene-deleted strains in which individual mitochondrial proteins were lost. We found that deletion of coq11 (an S. cerevisiae COQ11 homolog) and a novel gene designated coq12 lowered CoQ levels to ∼4% of that of the WT strain. Addition of PHB or p-hydroxybenzaldehyde restored the CoQ content and growth and lowered hydrogen sulfide production of the Δcoq12 strain, but these compounds did not affect the Δcoq11 strain. The primary structure of Coq12 has a flavin reductase motif coupled with an NAD +  reductase domain. We determined that purified Coq12 protein from S. pombe displayed NAD +  reductase activity when incubated with ethanol-extracted substrate of S. pombe. Because purified Coq12 from Escherichia coli did not exhibit reductase activity under the same conditions, an extra protein is thought to be necessary for its activity. Analysis of Coq12-interacting proteins by LC-MS/MS revealed interactions with other Coq proteins, suggesting formation of a complex. Thus, our analysis indicates that Coq12 is required for PHB synthesis, and it has diverged among species.","doi":"10.1016/j.jbc.2023.104797","authors":"Nishida I, Ohmori Y, Yanai R, Nishihara S, Matsuo Y, Kaino T, Hirata D, Kawamukai M","authors_abbrev":"Nishida I et al.","pubmed_publication_date":"Jun 2023","pubmed_entrez_date":"2023-05-08","publication_year":"2023","canto_session_key":"0163a412b84512b3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_first_approved_date":"2023-06-07 11:30:52","canto_approved_date":"2024-05-16 14:17:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-05-24 02:31:23","canto_added_date":"2023-05-10 00:15:04","annotation_curators":[{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":36,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.01c","SPCC622.06c","SPCC4G3.04c","SPBC146.12","SPBC16E9.12c","SPAC1071.11","SPCC162.05","SPAC630.13c","SPBC2F12.10","SPBC947.14c","SPCC1442.16c","SPCC338.10c","SPAC9.12c","SPAC19G12.11","SPBC1271.12","SPAC1687.12c","SPBC3E7.16c","SPAC1635.01","SPBC2D10.18","SPAC12G12.04","SPAC1F3.09","SPBC337.15c","SPBC23E6.04c","SPCC1840.09","SPBC1718.06","SPBC17D11.02c","SPAC17G8.03c","SPAC19G12.12","SPAC9E9.09c","SPAPB1E7.11c","SPCC11E10.04","SPCC1682.01","SPAC22E12.17c","SPBC3B9.17","SPCC126.03","SPCC4B3.11c","SPBP8B7.08c","SPBC18E5.12c","SPAC56F8.04c","SPCC645.03c","SPBPJ4664.01","SPAC10F6.01c"],"gene_count":42,"ltp_gene_count":42,"approved_date":"2023-06-07"},{"uniquename":"PMID:24356711","title":"Non-destructive handling of individual chromatin fibers isolated from single cells in a microfluidic device utilizing an optically driven microtool.","citation":"Lab Chip 2014 Feb 21;14(4):696-704","abstract":"We report a novel method for the non-destructive handling of, and biochemical experiments with, individual intact chromatin fibers, as well as their isolation from single cells, utilizing a specifically designed microfluidic device with an optically driven microtool under the microscope. Spheroplasts of recombinant fission yeast cells expressing fluorescent protein-tagged core histones were employed, and isolation of chromatin fibers was conducted by cell bursting via changing from isotonic conditions to hypotonic conditions in the microfluidic device. The isolation of chromatin fibers was confirmed by the fluorescent protein-tagged core histones involved in the chromatin fibers. For the non-destructive handling of the isolated chromatin fibers in the microfluidic device, we developed antibody-conjugated microspheres, which had affinity to the fluorescent protein-tagged core histones, and the microspheres were manipulated using optical tweezers, which functioned as optically driven microtools. With the aid of the microtool, isolated chromatin fibers were handled non-destructively and were tethered at the microstructures fabricated in the microfluidic device with straightened conformation by the flow. Immunofluorescence staining was carried out as a demonstrative biochemical experiment with the individual native chromatin fibers isolated in the microfluidic device, and specific fluorescent spots were visualized along the tethered chromatin fibers. Thus, the potential application of this method for epigenetic analyses of intact chromatin fibers isolated from single cells is demonstrated.","doi":"10.1039/c3lc51111a","authors":"Oana H, Nishikawa K, Matsuhara H, Yamamoto A, Yamamoto TG, Haraguchi T, Hiraoka Y, Washizu M","authors_abbrev":"Oana H et al.","pubmed_publication_date":"21 Feb 2014","pubmed_entrez_date":"2013-12-21","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8621070","title":"Schizosaccharomyces pombe rad23 is allelic with swi10, a mating-type switching/radioresistance gene that shares sequence homology with human and mouse ERCC1.","citation":"Gene 1996 Apr 17;170(1):113-7","abstract":"Schizosaccharomyces pombe (Sp) rad23-1 mutant cells are extremely sensitive to UV light and ionizing radiation. A genomic DNA fragment that contains wild-type (wt) rad23 has been cloned. The DNA sequence of this cloned gene has been determined and was found to be identical to the previously characterized mating-type switching/radioresistance gene, swi10. Complementation tests between rad23-1 and swi10-154 mutant cells exclusively produce UV-sensitive progeny and confirm that these two genes are allelic. The DNA sequences of rad23-1 and swi10-154 reveal that each contains a single, unique point mutation. In rad23-1, Glu231 changes to a stop codon, resulting in the production of a truncated protein. In swi10-154, a G to A transition mutation is within a splice consensus sequence for intron 1. Therefore, the corresponding mRNA is incapable of being processed appropriately.","authors":"Hang H, Hager DN, Goriparthi L, Hopkins KM, Shih H, Lieberman HB","authors_abbrev":"Hang H et al.","pubmed_publication_date":"17 Apr 1996","pubmed_entrez_date":"1996-04-17","publication_year":"1996","canto_session_key":"1db37277d7f4d8d8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-09-24 15:07:19","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-24 15:07:10","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.15c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-24"},{"uniquename":"PMID:34572495","title":"Comparative Genomic Analysis of the DUF34 Protein Family Suggests Role as a Metal Ion Chaperone or Insertase.","citation":"Biomolecules 2021 Aug 27;11(9)","abstract":"Members of the DUF34 (domain of unknown function 34) family, also known as the NIF3 protein superfamily, are ubiquitous across superkingdoms. Proteins of this family have been widely annotated as \"GTP cyclohydrolase I type 2\" through electronic propagation based on one study. Here, the annotation status of this protein family was examined through a comprehensive literature review and integrative bioinformatic analyses that revealed varied pleiotropic associations and phenotypes. This analysis combined with functional complementation studies strongly challenges the current annotation and suggests that DUF34 family members may serve as metal ion insertases, chaperones, or metallocofactor maturases. This general molecular function could explain how DUF34 subgroups participate in highly diversified pathways such as cell differentiation, metal ion homeostasis, pathogen virulence, redox, and universal stress responses.","doi":"10.3390/biom11091282","authors":"Reed CJ, Hutinet G, de Crécy-Lagard V","authors_abbrev":"Reed CJ et al.","pubmed_publication_date":"27 Aug 2021","pubmed_entrez_date":"2021-09-28","publication_year":"2021","canto_session_key":"1bd55421bff92cdb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2022-02-20 09:39:11","canto_approved_date":"2022-02-20 09:39:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-02-20 09:32:42","canto_added_date":"2022-02-20 09:31:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC126.12"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2022-02-20"},{"uniquename":"PMID:22194800","title":"De novo growth zone formation from fission yeast spheroplasts.","citation":"PLoS One 2011;6(12):e27977","abstract":"Eukaryotic cells often form polarized growth zones in response to internal or external cues. To understand the establishment of growth zones with specific dimensions we used fission yeast, which grows as a rod-shaped cell of near-constant width from growth zones located at the cell tips. Removing the cell wall creates a round spheroplast with a disorganized cytoskeleton and depolarized growth proteins. As spheroplasts recover, new growth zones form that resemble normal growing cell tips in shape and width, and polarized growth resumes. Regulators of the GTPase Cdc42, which control width in exponentially growing cells, also control spheroplast growth zone width. During recovery the Cdc42 scaffold Scd2 forms a polarized patch in the rounded spheroplast, demonstrating that a growth zone protein can organize independent of cell shape. Rga4, a Cdc42 GTPase activating protein (GAP) that is excluded from cell tips, is initially distributed throughout the spheroplast membrane, but is excluded from the growth zone after a stable patch of Scd2 forms. These results provide evidence that growth zones with normal width and protein localization can form de novo through sequential organization of cellular domains, and that the size of these growth zones is genetically controlled, independent of preexisting cell shape.","doi":"10.1371/journal.pone.0027977","authors":"Kelly FD, Nurse P","authors_abbrev":"Kelly FD et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-12-24","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15157890","title":"Nucleocytoplasmic transport and nuclear envelope integrity in the fission yeast Schizosaccharomyces pombe.","citation":"Methods 2004 Jul;33(3):226-38","abstract":"The nuclear envelope is essential for compartmentalizing the nucleus from the cytoplasm in all eukaryotic cells. There is a tremendous flux of both RNA and proteins across the nuclear envelope, which is intact throughout the entire cell cycle of yeasts but breaks down during mitosis of animal cells. Transport across the nuclear envelope requires the recognition of cargo molecules by receptors, docking at the nuclear pore, transit through the nuclear pore, and then dissociation of the cargo from the receptor. This process depends on the RanGTPase system, transport receptors, and the nuclear pore complex. We provide an overview of the nuclear transport process, with particular emphasis on the fission yeast Schizosaccharomyces pombe, including strategies for predicting and experimentally verifying the signals that determine the sub-cellular localization of a protein of interest. We also describe a variety of reagents and experimental strategies, including the use of mutants and chemical inhibitors, to study nuclear protein import, nuclear protein export, nucleocytoplasmic protein shuttling, and mRNA export in fission yeast. The RanGTPase and its regulators also play an essential transport independent role in nuclear envelope re-assembly after mitosis in animal cells and in the maintenance of nuclear envelope integrity at mitosis in S. pombe. Several experimental strategies and reagents for studying nuclear size, nuclear shape, the localization of nuclear pores, and the integrity of the nuclear envelope in living fission yeast cells are described.","authors":"Yoshida M, Sazer S","authors_abbrev":"Yoshida M et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.15c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:24177528","title":"Drug resistance in the fission yeast Schizosaccharomyces pombe: pleiotropic mutations affecting the oleic acid and sterol composition of cell membranes.","citation":"Curr Genet 1984 Jan;8(1):37-43","abstract":"The whole cell lipid and sterol content of the drug resistant strains cyh1, cyh3 and cyh4 was compared with that of wild type by thin layer and gas liquid chromatography and by UV spectrophotometric analysis. The cyh3 and cyh4 strains had a decreased content of the unsaturated 18:1 fatty acid oleic acid, a decreased content of ergosterol and an increased content of 24,28 dehydroergosterol with respect to wild type. The cyh1 strain, however, only showed a decreased content of ergosterol and an increased content of 24,28 dehydro-ergosterol when compared to wild type.","doi":"10.1007/BF00405430","authors":"Johnston PA, Coddington A","authors_abbrev":"Johnston PA et al.","pubmed_publication_date":"Jan 1984","pubmed_entrez_date":"2013-11-02","publication_year":"1984","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10775274","title":"Conservation of polyamine regulation by translational frameshifting from yeast to mammals.","citation":"EMBO J 2000 Apr 17;19(8):1907-17","abstract":"Regulation of ornithine decarboxylase in vertebrates involves a negative feedback mechanism requiring the protein antizyme. Here we show that a similar mechanism exists in the fission yeast Schizosaccharomyces pombe. The expression of mammalian antizyme genes requires a specific +1 translational frameshift. The efficiency of the frameshift event reflects cellular polyamine levels creating the autoregulatory feedback loop. As shown here, the yeast antizyme gene and several newly identified antizyme genes from different nematodes also require a ribosomal frameshift event for their expression. Twelve nucleotides around the frameshift site are identical between S.pombe and the mammalian counterparts. The core element for this frameshifting is likely to have been present in the last common ancestor of yeast, nematodes and mammals.","authors":"Ivanov IP, Matsufuji S, Murakami Y, Gesteland RF, Atkins JF","authors_abbrev":"Ivanov IP et al.","pubmed_publication_date":"17 Apr 2000","pubmed_entrez_date":"2000-04-25","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010556","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19475393","title":"The spindle checkpoint: assays for the analysis of spindle checkpoint arrest and recovery.","citation":"Methods Mol Biol 2009;545:243-58","abstract":"The spindle checkpoint is a surveillance mechanism that ensures the fidelity of chromosome segregation by inhibiting anaphase onset until all chromosomes have established stable bipolar attachments. Here we describe a number of protocols that can be used to assay the ability of budding and fission yeast cells to (1) establish and maintain a spindle checkpoint arrest, and (2) segregate chromosomes efficiently upon recovery from mitotic arrest. We focus on experimental detail of the budding yeast protocols, but also point out important differences between budding and fission yeast assays.","doi":"10.1007/978-1-60327-993-2_15","authors":"Fernius J, Hardwick KG","authors_abbrev":"Fernius J et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-05-29","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22582262","title":"Meiosis-specific noncoding RNA mediates robust pairing of homologous chromosomes in meiosis.","citation":"Science 2012 May 11;336(6082):732-6","abstract":"Pairing and recombination of homologous chromosomes are essential for ensuring reductional segregation in meiosis. However, the mechanisms by which chromosomes recognize their homologous partners are poorly understood. Here, we report that the sme2 gene encodes a meiosis-specific noncoding RNA that mediates homologous recognition in the fission yeast Schizosaccharomyces pombe. The sme2 locus shows robust pairing from early in meiotic prophase. The sme2 RNA transcripts accumulate at their respective gene loci and greatly enhance pairing of homologous loci: Deletion of the sme2 sequence eliminates this robust pairing, whereas transposition to other chromosomal sites confers robust pairing at those ectopic sites. Thus, we propose that RNA transcripts retained on the chromosome play an active role in recognition of homologous chromosomes for pairing.","doi":"10.1126/science.1219518","authors":"Ding DQ, Okamasa K, Yamane M, Tsutsumi C, Haraguchi T, Yamamoto M, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"11 May 2012","pubmed_entrez_date":"2012-05-15","publication_year":"2012","canto_session_key":"e3c8313e9bd1dabc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-26 12:28:22","canto_approved_date":"2023-04-20 11:52:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-10 13:58:27","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPNCRNA.103","SPAC6G9.13c","SPCC736.12c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-10-26"},{"uniquename":"PMID:10871352","title":"Insertional mutagenesis based on illegitimate recombination in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2000 Jun 01;28(11):E53","abstract":"An efficient insertional mutagenesis system has been developed for Schizosaccharomyces pombe based on linear PCR-generated cassettes containing selectable markers. It depends upon illegitimate recombination for integration into the genome. Various selectable markers of different sizes can be used to obtain sufficiently high transformation and integration frequencies. Based on Southern blotting, a single insertion is found in each strain and integration sites are broadly distributed in the genome. Sequence analysis of the insert junctions frequently reveals small regions of homology (4-10 bp) between the ends of the integrated cassette and the disrupted gene. The system has been used for simple genetic screens of various types and as a promoter trap for in-frame GFP fusions.","authors":"Chua G, Taricani L, Stangle W, Young PG","authors_abbrev":"Chua G et al.","pubmed_publication_date":"01 Jun 2000","pubmed_entrez_date":"2000-06-28","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22403715","title":"Regulation of fission yeast morphogenesis by PP2A activator pta2.","citation":"PLoS One 2012;7(3):e32823","abstract":"Cell polarization is key for the function of most eukaryotic cells, and regulates cell shape, migration and tissue architecture. Fission yeast, Schizosaccharomyces pombe cells are cylindrical and polarize cell growth to one or both cell tips dependent on the cell cycle stage. Whereas microtubule cytoskeleton contributes to the positioning of the growth sites by delivering polarity factors to the cell ends, the Cdc42 GTPase polarizes secretion via actin-dependent delivery and tethering of secretory vesicles to plasma membrane. How growth is restricted to cell tips and how re-initiation of tip growth is regulated in the cell cycle remains poorly understood. In this work we investigated the function of protein phosphatase type 2A (PP2A) in S. pombe morphogenesis by deleting the evolutionary conserved PTPA-type regulatory subunit that we named pta2. pta2-deleted cells showed morphological defects and altered growth pattern. Consistent with this, actin patches and active Cdc42 were mislocalized in the pta2 deletion. These defects were additive to the lack of Cdc42-GAP Rga4. pta2Δ cells show upregulated Cdc42 activity and pta2 interacts genetically with polarisome components Tea1, Tea4 and For3 leading to complete loss of cell polarity and rounded morphology. Thus, regulation of polarity by PP2A requires the polarisome and involves Pta2-dependent control of Cdc42 activity.","doi":"10.1371/journal.pone.0032823","authors":"Bernal M, Sanchez-Romero MA, Salas-Pino S, Daga RR","authors_abbrev":"Bernal M et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-03-10","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP8A3.09c","SPCC13B11.01","SPBC32F12.11","SPAC140.02","SPBP8B7.08c","SPBC16H5.07c","SPAC823.15","SPAC1782.05","SPCC188.02","SPBC2D10.10c","SPBC19C2.07"],"gene_count":11,"ltp_gene_count":0},{"uniquename":"PMID:6835257","title":"Mutagenicity of some organophosphorus compounds at the ade6 locus of Schizosaccharomyces pombe.","citation":"Mutat Res 1983 Apr;117(1-2):139-48","abstract":"12 organophosphorus insecticides were tested for toxicity and mutagenicity in the forward mutation test system ade6 of the yeast Schizosaccharomyces pombe. EMS and MMS were selected as positive controls. 3 compounds, dichlorvos, trichlorfon and paraoxon, showed a linear dose-response relationship. Among the other compounds investigated, methyl derivatives, though in general more toxic than ethyl derivatives, did not significantly increase the mutation frequency. Trichlorfon, tested in combination with malathion, methylparathion or methylazinphos (guthion), produced clearly synergistic effects for both toxicity and mutagenicity. The addition of S9 microsomal liver fraction decreased the efficiency of both single and combined treatments only where a dose-response relationship or a synergistic effect was obtained.","authors":"Gilot-Delhalle J, Colizzi A, Moutschen J, Moutschen-Dahmen M","authors_abbrev":"Gilot-Delhalle J et al.","pubmed_publication_date":"Apr 1983","pubmed_entrez_date":"1983-04-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19759825","title":"The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.","citation":"PLoS One 2009 Sep 11;4(9):e6939","abstract":"The molecular chaperone Hsp104 is a crucial factor in the acquisition of thermotolerance in yeast. Under stress conditions, the disaggregase activity of Hsp104 facilitates the reactivation of misfolded proteins. Hsp104 is also involved in the propagation of fungal prions. For instance, the well-characterized [PSI(+)] prion of Saccharomyces cerevisiae does not propagate in Deltahsp104 cells or in cells overexpressing Hsp104. In this study, we characterized the functional homolog of Hsp104 from Schizosaccharomyces pombe (Sp_Hsp104). As its S. cerevisiae counterpart, Sp_hsp104(+) is heat-inducible and required for thermotolerance in S. pombe. Sp_Hsp104 displays low disaggregase activity and cannot propagate the [PSI(+)] prion in S. cerevisiae. When overexpressed in S. cerevisiae, Sp_Hsp104 confers thermotolerance to Deltahsp104 cells and reactivates heat-aggregated proteins. However, overexpression of Sp_Hsp104 does not propagate nor eliminate [PSI(+)]. Strikingly, [PSI(+)] was cured by overexpression of a chimeric chaperone bearing the C-terminal domain (CTD) of the S. cerevisiae Hsp104 protein. Our study demonstrates that the ability to untangle aggregated proteins is conserved between the S. pombe and S. cerevisiae Hsp104 homologs, and points to a role of the CTD in the propagation of the S. cerevisiae [PSI(+)] prion.","doi":"10.1371/journal.pone.0006939","authors":"Sénéchal P, Arseneault G, Leroux A, Lindquist S, Rokeach LA","authors_abbrev":"Sénéchal P et al.","pubmed_publication_date":"11 Sep 2009","pubmed_entrez_date":"2009-09-18","publication_year":"2009","canto_session_key":"5b36d74c349d9860","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-11-24 15:12:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-24 15:12:39","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-24"},{"uniquename":"PMID:9552380","title":"Regulation of G1 progression in fission yeast by the rum1+ gene product.","citation":"Prog Cell Cycle Res 1996;2:29-35","abstract":"Recently it has been found that B-type cyclins in fission yeast regulate the activation of the cdc2 kinase to promote the onset of both DNA replication and mitosis. cig2 is the major G1 cyclin while cdc13 is the principal mitotic cyclin. cdc13 also has an additional function in G2 phase, preventing more than one round of DNA replication per cell cycle. In opposition to these cyclins the rum1 inhibitor, a protein present exclusively in G1, prevents premature activation of the cdc2/cig2 and the cdc2/cdc13 complexes until cells have reached the critical cell size required to pass Start and initiate a new cell cycle.","authors":"Martín-Castellanos C, Moreno S","authors_abbrev":"Martín-Castellanos C et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"0cd9347bf6391fc3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-13 15:19:29","canto_approved_date":"2022-06-06 07:08:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-24 12:14:00","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAPB2B4.03","SPBC582.03","SPCC18B5.03","SPBC32F12.09"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2017-07-13"},{"uniquename":"PMID:22570876","title":"DNA repair, DNA replication and human disorders: a personal journey.","citation":"DNA Repair (Amst) 2012 Apr 01;11(4):328-34","abstract":"","authors":"Lehmann AR","authors_abbrev":"Lehmann AR","pubmed_publication_date":"01 Apr 2012","pubmed_entrez_date":"2012-05-10","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21148300","title":"Actin cables and the exocyst form two independent morphogenesis pathways in the fission yeast.","citation":"Mol Biol Cell 2011 Jan 01;22(1):44-53","abstract":"Cell morphogenesis depends on polarized exocytosis. One widely held model posits that long-range transport and exocyst-dependent tethering of exocytic vesicles at the plasma membrane sequentially drive this process. Here, we describe that disruption of either actin-based long-range transport and microtubules or the exocyst did not abolish polarized growth in rod-shaped fission yeast cells. However, disruption of both actin cables and exocyst led to isotropic growth. Exocytic vesicles localized to cell tips in single mutants but were dispersed in double mutants. In contrast, a marker for active Cdc42, a major polarity landmark, localized to discreet cortical sites even in double mutants. Localization and photobleaching studies show that the exocyst subunits Sec6 and Sec8 localize to cell tips largely independently of the actin cytoskeleton, but in a cdc42 and phospholipid phosphatidylinositol 4,5-bisphosphate (PIP₂)-dependent manner. Thus in fission yeast long-range cytoskeletal transport and PIP₂-dependent exocyst represent parallel morphogenetic modules downstream of Cdc42, raising the possibility of similar mechanisms in other cell types.","doi":"10.1091/mbc.E10-08-0720","authors":"Bendezú FO, Martin SG","authors_abbrev":"Bendezú FO et al.","pubmed_publication_date":"01 Jan 2011","pubmed_entrez_date":"2010-12-15","publication_year":"2011","canto_session_key":"50905b15a05554bd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2021-03-24 15:42:37","canto_approved_date":"2022-09-02 16:58:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-10 11:54:28","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.11","SPAC4A8.15c","SPAC110.03","SPAC1F5.04c","SPCC895.05","SPCC970.09","SPAC19G12.14","SPBC2D10.14c","SPCC1919.10c","SPCC1840.02c","SPBC19G7.05c","SPBC106.20","SPAC20G4.02c","SPCC1235.10c"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2021-03-24"},{"uniquename":"PMID:23209589","title":"Mathematical model for growth regulation of fission yeast Schizosaccharomyces pombe.","citation":"PLoS One 2012;7(11):e49675","abstract":"Regulation of polarised cell growth is essential for many cellular processes including spatial coordination of cell morphology changes during the division cycle. We present a mathematical model of the core mechanism responsible for the regulation of polarised growth dynamics during the fission yeast cell cycle. The model is based on the competition of growth zones localised at the cell tips for a common substrate distributed uniformly in the cytosol. We analyse the bifurcations in this model as the cell length increases, and show that the growth activation dynamics provides an explanation for the new-end take-off (NETO) as a saddle-node bifurcation at which the cell sharply switches from monopolar to bipolar growth. We study the parameter sensitivity of the bifurcation diagram and relate qualitative changes of the growth pattern, e.g. delayed or absent NETO, to previously observed mutant phenotypes. We investigate the effects of imperfect asymmetric cell division, and show that this leads to distinct growth patterns that provide experimentally testable predictions for validating the presented competitive growth zone activation model. Finally we discuss extension of the model for describing mutant cells with more than two growth zones.","doi":"10.1371/journal.pone.0049675","authors":"Cerone L, Novák B, Neufeld Z","authors_abbrev":"Cerone L et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-12-05","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3522614","title":"Mitosis in the fission yeast Schizosaccharomyces pombe as revealed by freeze-substitution electron microscopy.","citation":"J Cell Sci 1986 Feb;80:253-68","abstract":"Nuclear division in Schizosaccharomyces pombe has been studied in transmission electron micrographs of sections of cells fixed by a method of freeze-substitution. We have found cytoplasmic microtubules in the vicinity of the spindle pole bodies and two kinds of microtubules, short discontinuous ones and long, parallel ones in the intranuclear mitotic spindle. For most of the time taken by nuclear division the spindle pole bodies face each other squarely across the nuclear space but early in mitosis they briefly appear twisted out of alignment with each other, thereby imparting a sigmoidal shape to the bundle of spindle microtubules extending between them. This configuration is interpreted as indicating active participation of the spindle in the initial elongation of the dividing nucleus. It is proposed that mitosis is accompanied by the shortening of chromosomal microtubules simultaneously with the elongation of the central pole-to-pole bundle of microtubules of the intranuclear spindle. Daughter nuclei are separated by the sliding apart of interdigitating microtubules of the spindle at telophase. Some of the latter bear dense knobs at their ends.","authors":"Tanaka K, Kanbe T","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"Feb 1986","pubmed_entrez_date":"1986-02-01","publication_year":"1986","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21035342","title":"Rab-family GTPase regulates TOR complex 2 signaling in fission yeast.","citation":"Curr Biol 2010 Nov 23;20(22):1975-82","abstract":"From yeast to human, TOR (target of rapamycin) kinase plays pivotal roles in coupling extracellular stimuli to cell growth and metabolism. TOR kinase functions in two distinct protein complexes, TOR complex 1 (TORC1) and 2 (TORC2), which phosphorylate and activate different AGC-family protein kinases. TORC1 is controlled by the small GTPase Rheb, but little is known about TORC2 regulators.\nWe have identified the Ryh1 GTPase, a human Rab6 ortholog, as an activator of TORC2 signaling in the fission yeast Schizosaccharomyces pombe. Mutational inactivation of Ryh1 or its guanine nucleotide exchange factor compromises the TORC2-dependent phosphorylation of the AGC-family Gad8 kinase. In addition, the effector domain of Ryh1 is important for its physical interaction with TORC2 and for stimulation of TORC2 signaling. Thus, GTP-bound Ryh1 is likely to be the active form stimulatory to TORC2-Gad8 signaling. Consistently, expression of the GTP-locked mutant Ryh1 is sufficient to promote interaction between TORC2 and Gad8 and to induce Gad8 hyperphosphorylation. The loss of functional Ryh1, TORC2, or Gad8 brings about similar vacuolar fragmentation and stress sensitivity, further corroborating their involvement in a common cellular process. Human Rab6 can substitute Ryh1 in S. pombe, and therefore Rab6 may be a potential activator of TORC2 in mammals.\nIn its GTP-bound form, Ryh1, an evolutionarily conserved Rab GTPase, activates TORC2 signaling to the AGC kinase Gad8. The Ryh1 GTPase and the TORC2-Gad8 pathway are required for vacuolar integrity and cellular stress resistance in S. pombe.","doi":"10.1016/j.cub.2010.10.026","authors":"Tatebe H, Morigasaki S, Murayama S, Zeng CT, Shiozaki K","authors_abbrev":"Tatebe H et al.","pubmed_publication_date":"23 Nov 2010","pubmed_entrez_date":"2010-11-02","publication_year":"2010","canto_session_key":"54af20fd9bd9f581","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaz Shiozaki","canto_first_approved_date":"2016-08-03 08:29:52","canto_approved_date":"2024-03-11 16:28:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-07 09:00:02","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kaz Shiozaki","community_curator":true,"annotation_count":38,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC24B10.07","SPBC16G5.15c","SPBC23E6.08","SPCC777.08c","SPBC12C2.02c","SPAC4C5.02c","SPAC1851.04c","SPBC30D10.10c","SPAPYUG7.02c","SPAC18G6.03","SPBC21B10.05c"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2016-08-03"},{"uniquename":"PMID:39813093","title":"Fission yeast GPI inositol deacylase Bst1 regulates ER-Golgi transport and functions in late stages of cytokinesis.","citation":"Mol Biol Cell 2025 Jan 15;:mbcE24080375","abstract":"The Munc13/UNC-13 family protein Ync13 is essential for septum integrity and cytokinesis in fission yeast. To further explore the mechanism of Ync13 functions, spontaneous suppressors of  ync13  mutants, which can suppress the colony-formation defects and lysis phenotype of  ync13  mutant cells, are isolated and characterized. One of the suppressor mutants,  bst1 - s27 , shows defects in the cytokinetic contractile ring constriction, septation, and daughter-cell separation, similar to  bst1Δ  mutant. Bst1, a predicted GPI inositol deacylase, was an uncharacterized protein in fission yeast. It localizes to the nuclear ER and puncta structures in the cytoplasm. The Bst1 puncta overlaps frequently with Anp1, which is a marker of ER-Golgi transport, but rarely with trans-Golgi marker Sec72. The nuclear ER signal of Anp1 increases in  bst1Δ  mutant, whereas Sec72 localization shows no obvious changes. In addition, more cytoplasmic puncta structures of COPII subunits, Sec13 and Sec24, are observed in  bst1Δ  mutant, and acid phosphatase secretion is compromised without Bst1. Consistently, the division site targeting of the β-glucanase Eng1 and α-glucanase Agn1 is reduced in  bst1Δ  and  bst1Δ ync13Δ  mutant. Taken together, our results suggest that Bst1 regulates ER-Golgi transport and is involved in cytokinesis through regulating the secretion of glucanases.","doi":"10.1091/mbc.E24-08-0375","authors":"Ye Y, Osmani AH, Liu ZR, Kern A, Wu JQ","authors_abbrev":"Ye Y et al.","pubmed_publication_date":"15 Jan 2025","pubmed_entrez_date":"2025-01-15","publication_year":"2025","canto_session_key":"a364ad7e70b0ff67","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-01-16 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26099175","title":"The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron-sulfur proteins.","citation":"Eur J Cell Biol 2015;94(7-9):280-91","abstract":"Mitochondria have been derived from alpha-bacterial endosymbionts during the evolution of eukaryotes. Numerous bacterial functions have been maintained inside the organelles including fatty acid degradation, citric acid cycle, oxidative phosphorylation, and the synthesis of heme or lipoic acid cofactors. Additionally, mitochondria have inherited the bacterial iron-sulfur cluster assembly (ISC) machinery. Many of the ISC components are essential for cell viability because they generate a still unknown, sulfur-containing compound for the assembly of cytosolic and nuclear Fe/S proteins that perform important functions in, e.g., protein translation, DNA synthesis and repair, and chromosome segregation. The sulfur-containing compound is exported by the mitochondrial ABC transporter Atm1 (human ABCB7) and utilized by components of the cytosolic iron-sulfur protein assembly (CIA) machinery. An appealing minimal model for the striking compartmentation of eukaryotic Fe/S protein biogenesis is provided by organisms that contain mitosomes instead of mitochondria. Mitosomes have been derived from mitochondria by reductive evolution, during which they have lost virtually all classical mitochondrial tasks. Nevertheless, mitosomes harbor all core ISC components which presumably have been maintained for assisting the maturation of cytosolic-nuclear Fe/S proteins. The current review is centered around the Atm1 export process. We present an overview on the mitochondrial requirements for the export reaction, summarize recent insights into the 3D structure and potential mechanism of Atm1, and explain how the CIA machinery uses the mitochondrial export product for the assembly of cytosolic and nuclear Fe/S proteins.","doi":"10.1016/j.ejcb.2015.05.002","authors":"Lill R, Dutkiewicz R, Freibert SA, Heidenreich T, Mascarenhas J, Netz DJ, Paul VD, Pierik AJ, Richter N, Stümpfig M, Srinivasan V, Stehling O, Mühlenhoff U","authors_abbrev":"Lill R et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-06-24","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC637.08","SPAC15A10.01","SPAC1296.06","SPBC337.10c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:15576932","title":"In situ assay for analyzing the chromatin binding of proteins in fission yeast.","citation":"Methods Mol Biol 2005;296:181-8","abstract":"An in situ technique for studying the chromatin binding of proteins in single fission yeast cells (Schizosaccharomyces pombe) is described. Cells are permeabilized by enzymatic digestion and extracted with a detergent-containing buffer. This procedure removes soluble proteins, but proteins that are bound to insoluble cell structures such as chromatin are retained, and overall cell morphology is maintained. Extraction of proteins is monitored by fluorescence microscopy, either using fluorescently tagged proteins or by indirect immunofluorescence. This method allows the chromatin association of proteins to be correlated with other cell cycle events without the need for cell synchronization.","authors":"Kearsey SE, Brimage L, Namdar M, Ralph E, Yang X","authors_abbrev":"Kearsey SE et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2004-12-04","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25647499","title":"Production of CoQ10 in fission yeast by expression of genes responsible for CoQ10 biosynthesis.","citation":"Biosci Biotechnol Biochem 2015;79(6):1026-33","abstract":"Coenzyme Q10 (CoQ10) is essential for energy production and has become a popular supplement in recent years. In this study, CoQ10 productivity was improved in the fission yeast Schizosaccharomyces pombe. Ten CoQ biosynthetic genes were cloned and overexpressed in S. pombe. Strains expressing individual CoQ biosynthetic genes did not produce higher than a 10% increase in CoQ10 production. In addition, simultaneous expression of all ten coq genes did not result in yield improvements. Genes responsible for the biosynthesis of p-hydroxybenzoate and decaprenyl diphosphate, both of which are CoQ biosynthesis precursors, were also overexpressed. CoQ10 production was increased by overexpression of Eco_ubiC (encoding chorismate lyase), Eco_aroF(FBR) (encoding 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase), or Sce_thmgr1 (encoding truncated HMG-CoA reductase). Furthermore, simultaneous expression of these precursor genes resulted in two fold increases in CoQ10 production.","doi":"10.1080/09168451.2015.1006573","authors":"Moriyama D, Hosono K, Fujii M, Washida M, Nanba H, Kaino T, Kawamukai M","authors_abbrev":"Moriyama D et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-02-04","publication_year":"2015","canto_session_key":"9ea27909f0fa0017","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-03 22:42:06","canto_approved_date":"2026-01-12 17:05:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-03 22:41:58","canto_added_date":"2015-02-05 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.18","SPAC56F8.04c","SPBC146.12","SPAC19G12.12","SPAC1687.12c","SPBC337.15c","SPAC16E8.04c","SPCC4G3.04c","SPAC24C9.03","SPAC343.01c","SPCC162.09c","SPBPJ4664.01","SPAC19G12.11","SPCC162.05"],"gene_count":14,"ltp_gene_count":12,"approved_date":"2015-11-03"},{"uniquename":"PMID:30148840","title":"Tdp1 processes chromate-induced single-strand DNA breaks that collapse replication forks.","citation":"PLoS Genet 2018 Aug;14(8):e1007595","abstract":"Hexavalent chromium [Cr(VI)] damages DNA and causes cancer, but it is unclear which DNA damage responses (DDRs) most critically protect cells from chromate toxicity. Here, genome-wide quantitative functional profiling, DDR measurements and genetic interaction assays in Schizosaccharomyces pombe reveal a chromate toxicogenomic profile that closely resembles the cancer chemotherapeutic drug camptothecin (CPT), which traps Topoisomerase 1 (Top1)-DNA covalent complex (Top1cc) at the 3' end of single-stand breaks (SSBs), resulting in replication fork collapse. ATR/Rad3-dependent checkpoints that detect stalled and collapsed replication forks are crucial in Cr(VI)-treated cells, as is Mus81-dependent sister chromatid recombination (SCR) that repairs single-ended double-strand breaks (seDSBs) at broken replication forks. Surprisingly, chromate resistance does not require base excision repair (BER) or interstrand crosslink (ICL) repair, nor does co-elimination of XPA-dependent nucleotide excision repair (NER) and Rad18-mediated post-replication repair (PRR) confer chromate sensitivity in fission yeast. However, co-elimination of Tdp1 tyrosyl-DNA phosphodiesterase and Rad16-Swi10 (XPF-ERCC1) NER endonuclease synergistically enhances chromate toxicity in top1Δ cells. Pnk1 polynucleotide kinase phosphatase (PNKP), which restores 3'-hydroxyl ends to SSBs processed by Tdp1, is also critical for chromate resistance. Loss of Tdp1 ameliorates pnk1Δ chromate sensitivity while enhancing the requirement for Mus81. Thus, Tdp1 and PNKP, which prevent neurodegeneration in humans, repair an important class of Cr-induced SSBs that collapse replication forks.","doi":"10.1371/journal.pgen.1007595","authors":"Ganguly A, Guo L, Sun L, Suo F, Du LL, Russell P","authors_abbrev":"Ganguly A et al.","pubmed_publication_date":"Aug 2018","pubmed_entrez_date":"2018-08-28","publication_year":"2018","canto_session_key":"54db84e4ca91c654","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2018-09-18 13:10:49","canto_approved_date":"2025-05-28 14:50:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-09-04 23:30:07","canto_added_date":"2018-08-29 00:15:04","annotation_curators":[{"name":"Paul Russell","community_curator":true,"annotation_count":184,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC56F2.11","SPAC26F1.10c","SPAC8E11.02c","SPBC28F2.10c","SPBC609.02","SPCC338.08","SPBC1703.14c","SPBC660.11","SPBC14C8.03","SPAC20H4.07","SPAC30D11.07","SPAC2G11.12","SPAC20G4.04c","SPCC4G3.05c","SPAC664.02c","SPBC29A10.07","SPAC1B3.07c","SPAC144.06","SPBC582.05c","SPBC16H5.13","SPCC594.06c","SPAC23A1.19c","SPAC17H9.08","SPAC11E3.04c","SPAC26H5.07c","SPCC622.12c","SPCC126.04c","SPCC285.09c","SPCC794.11c","SPBC106.10","SPBC4F6.15c","SPBC30D10.04","SPAC6G9.08","SPAC23C11.04c","SPAC9G1.07","SPAC21E11.03c","SPAC4G9.11c","SPAC105.01c","SPBC215.03c","SPAC19A8.05c","SPAC1486.01","SPBC36.04","SPBC106.17c","SPAC22F8.02c","SPBPJ4664.01","SPBC342.06c","SPCC757.10","SPCC970.01","SPCC162.05","SPBC216.06c","SPAC23H3.06","SPBC1734.06","SPAC19G12.11","SPBC216.05","SPBC660.10","SPAC24C9.05c","SPCC18B5.11c","SPBC3H7.12","SPBC651.11c","SPBC1105.10","SPCC1259.13","SPBC342.05","SPAC644.14c","SPCC16C4.20c","SPAC9E9.08","SPAC10F6.08c","SPBC3D6.10","SPBC2D10.13","SPBC3E7.08c","SPCC1442.04c","SPAC23E2.01","SPCC1739.06c","SPAC688.10","SPCP31B10.05","SPAC13C5.07","SPBC2G5.06c","SPAC1952.07","SPAC664.07c","SPAC14C4.13","SPAC13A11.04c","SPBC649.03","SPAC694.06c","SPAC31A2.11c","SPAC17H9.10c","SPAC4D7.06c","SPBC29A3.14c","SPAC17A2.09c","SPBC365.14c","SPAC22A12.01c","SPBC354.03","SPBC1703.12","SPBC215.14c"],"gene_count":92,"ltp_gene_count":90,"approved_date":"2018-09-18"},{"uniquename":"PMID:12387729","title":"Disruption and overexpression of the Schizosaccharomyces pombe aps1 gene, and effects on growth rate, morphology and intracellular diadenosine 5',5\"'-P1,P5-pentaphosphate and diphosphoinositol polyphosphate concentrations.","citation":"Biochem J 2003 Feb 01;369(Pt 3):519-28","abstract":"Schizosaccharomyces pombe Aps1 is an enzyme that degrades both diadenosine oligophosphates (Ap(n)A, n =5 or 6) and diphosphoinositol polyphosphates [diphosphoinositol pentakisphosphate (PP-InsP(5)) and bisdiphosphoinositol tetrakisphosphate ([PP](2)-InsP(4))] in vitro. The in vivo substrates of Aps1 are unknown. We report here the identification of Ap(5)A, PP-InsP(5), [PP](2)-InsP(4) and a novel diphosphoinositol polyphosphate ([PP](x)-InsP(x)) in S. pombe using HPLC methods. Ap(5)A was present at 0.06 pmol/mg of protein (approx. 4 nM). PP-InsP(5), [PP](x)-InsP(x) and [PP](2)-InsP(4) were present at 15 pmol/mg (approx. 1.1 microM), 15 pmol/mg (approx. 1.1 microM) and 30 pmol/mg (approx. 2.2 microM) respectively, while the intracellular concentration of InsP(6) was 0.5 nmol/mg of protein (approx. 36 microM). Disruption of aps1 resulted in a 52% decrease in Ap(6)A hydrolase activity in vitro, no detectable change in the intracellular Ap(5)A concentration, and 3-fold increased intracellular concentrations of PP-Ins P(5) and [PP](x)-InsP(x). Disruption of aps1 resulted in no detectable change in morphology or growth rate in minimal or rich media at 30 degrees C. Overexpression of aps1 via two different plasmids that resulted in 60% and 6-fold increases above wild-type enzymic activity in vitro caused no detectable changes in the intracellular concentrations of [PP](2)-InsP(4), [PP](x)-InsP(x) or PP-InsP(5), but paradoxical increases of approx. 2.5- and 55-fold respectively in the intracellular Ap(5)A concentration. Overexpression of aps1 also resulted in a reduced growth rate and in morphological changes, including swollen, rounded and multiseptate cells. No phenotypic changes or changes in intracellular Ap(5)A occurred upon overexpression of aps1 E93Q, which encodes a mutated Aps1 lacking significant enzymic activity. We conclude that Aps1 degrades PP-InsP(5) and [PP](x)-InsP(x) in vivo.","authors":"Ingram SW, Safrany ST, Barnes LD","authors_abbrev":"Ingram SW et al.","pubmed_publication_date":"01 Feb 2003","pubmed_entrez_date":"2002-10-22","publication_year":"2003","canto_session_key":"de26237c46b6b072","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-29 08:26:40","canto_approved_date":"2022-10-25 14:17:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-29 08:26:34","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G6.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-29"},{"uniquename":"PMID:7926667","title":"Sulfur amino acid metabolism in Schizosaccharomyces pombe: occurrence of two O-acetylhomoserine sulfhydrylases and the lack of the reverse transsulfuration pathway.","citation":"FEMS Microbiol Lett 1994 Aug 15;121(2):171-4","abstract":"The fission yeast Schizosaccharomyces pombe has a unique organization of sulfur amino acid metabolism: it has two distinct O-acetylhomoserine sulfhydrylases (homocysteine synthases). Similar to Enterobacteriaceae, S. pombe lacks cystathionine beta-synthase and cystathionine gamma-lyase-the enzymes of the reverse transsulfuration pathway, by which methionine is readily metabolized to cysteine-a likely effector in the sulfur metabolite repression system. Consequently no repression of sulfate assimilation is observed when methionine is added to the growth medium.","authors":"Brzywczy J, Paszewski A","authors_abbrev":"Brzywczy J et al.","pubmed_publication_date":"15 Aug 1994","pubmed_entrez_date":"1994-08-15","publication_year":"1994","canto_session_key":"8e2abb504c036182","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-11-27 11:58:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-27 11:58:46","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-11-27"},{"uniquename":"PMID:15601840","title":"Composition and architecture of the Schizosaccharomyces pombe Rad18 (Smc5-6) complex.","citation":"Mol Cell Biol 2005 Jan;25(1):172-84","abstract":"The rad18 gene of Schizosaccharomyces pombe is an essential gene that is involved in several different DNA repair processes. Rad18 (Smc6) is a member of the structural maintenance of chromosomes (SMC) family and, together with its SMC partner Spr18 (Smc5), forms the core of a high-molecular-weight complex. We show here that both S. pombe and human Smc5 and -6 interact through their hinge domains and that four independent temperature-sensitive mutants of Rad18 (Smc6) are all mutated at the same glycine residue in the hinge region. This mutation abolishes the interactions between the hinge regions of Rad18 (Smc6) and Spr18 (Smc5), as does mutation of a conserved glycine in the hinge region of Spr18 (Smc5). We purified the Smc5-6 complex from S. pombe and identified four non-SMC components, Nse1, Nse2, Nse3, and Rad62. Nse3 is a novel protein which is related to the mammalian MAGE protein family, many members of which are specifically expressed in cancer tissue. In initial steps to understand the architecture of the complex, we identified two subcomplexes containing Rad18-Spr18-Nse2 and Nse1-Nse3-Rad62. The subcomplexes are probably bridged by a weaker interaction between Nse2 and Nse3.","authors":"Sergeant J, Taylor E, Palecek J, Fousteri M, Andrews EA, Sweeney S, Shinagawa H, Watts FZ, Lehmann AR","authors_abbrev":"Sergeant J et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-12-17","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC645.04","SPCC550.05","SPCC5E4.06","SPBC20F10.04c","SPAC14C4.02c","SPAC16A10.06c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:3434730","title":"Brain stem and spinal cord impairment in Rett syndrome: somatosensory and auditory evoked responses investigations.","citation":"Brain Dev 1987;9(5):517-22","abstract":"Six females with Rett syndrome (RS)--all seriously motor disabled with clinical symptomatology indicating not only brain but also spinal cord impairment--were investigated using auditory and somatosensory evoked responses techniques. In all patients the responses representing the pathways through the upper spinal cord were delayed suggesting an impairment of the central conduction time. The findings mean an involvement of the sub-cortical structures, the brain stem and the cervical spinal cord in the disease process. From the natural clinical course and the present findings, it is concluded that RS is also characterized by spinal cord impairment appearing with increasing age and stage of diseases.","authors":"Badr GG, Witt-Engerström I, Hagberg B","authors_abbrev":"Badr GG et al.","pubmed_publication_date":"1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP8B7.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:27792454","title":"Gene dosis and the timing of mitosis.","citation":"Cell Cycle 2016 Nov 16;15(22):3022-3023","abstract":"","authors":"Tallada VA, Bähler J","authors_abbrev":"Tallada VA et al.","pubmed_publication_date":"16 Nov 2016","pubmed_entrez_date":"2016-10-30","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-10-31 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19470220","title":"Biotechnological synthesis of the designer drug metabolite 4'-hydroxymethyl-alpha-pyrrolidinohexanophenone in fission yeast heterologously expressing human cytochrome P450 2D6--a versatile alternative to multistep chemical synthesis.","citation":"J Anal Toxicol 2009 May;33(4):190-7","abstract":"1-(4-Methylphenyl)-2-pyrrolidin-1-ylhexan-1-one (4'-methyl-alpha-pyrrolidinohexanophenone, MPHP) is a new designer drug that appeared on the illicit drug market. It is mainly metabolized to 4'-hydroxymethyl-alpha-pyrrolidinohexanophenone (HO-MPHP) followed by oxidation to the respective carboxylic acid. For studies on the quantitative involvement of human cytochrome P450 (CYP) isoenzymes in the initial hydroxylation, a reference standard of HO-MPHP was needed. Therefore, the aim of this study was to synthesize this metabolite using a biotechnological approach. MPHP.HNO(3) (250 micromol) was incubated with 1 L culture of the fission yeast (Schizosaccharomyces pombe) strain CAD64 heterologously co-expressing human CYP reductase and CYP2D6. After centrifugation, the product was isolated from the incubation supernatants by solid-phase extraction. Further product cleanup was achieved by semi-preparative high-performance liquid chromatography (HPLC). After extraction of HO-MPHP from the respective eluent fractions, it was precipitated as its hydrochloric salt. The final product HO-MPHP.HCl was obtained in a yield of 138 micromol (43 mg, 55%). Its identity was confirmed by full scan gas chromatography-mass spectrometry (after trimethylsilylation), (1)H-NMR, and (13)C-NMR. The product purity as estimated from HPLC-ultraviolet analysis was greater than 99%. The described biotechnological approach proved to be a versatile alternative to the chemical synthesis of HO-MPHP.","authors":"Peters FT, Dragan CA, Kauffels A, Schwaninger AE, Zapp J, Bureik M, Maurer HH","authors_abbrev":"Peters FT et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-05-28","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28513584","title":"Kinesin-5-independent mitotic spindle assembly requires the antiparallel microtubule crosslinker Ase1 in fission yeast.","citation":"Nat Commun 2017 May 17;8:15286","abstract":"Bipolar spindle assembly requires a balance of forces where kinesin-5 produces outward pushing forces to antagonize the inward pulling forces from kinesin-14 or dynein. Accordingly, Kinesin-5 inactivation results in force imbalance leading to monopolar spindle and chromosome segregation failure. In fission yeast, force balance is restored when both kinesin-5 Cut7 and kinesin-14 Pkl1 are deleted, restoring spindle bipolarity. Here we show that the cut7Δpkl1Δ spindle is fully competent for chromosome segregation independently of motor activity, except for kinesin-6 Klp9, which is required for anaphase spindle elongation. We demonstrate that cut7Δpkl1Δ spindle bipolarity requires the microtubule antiparallel bundler PRC1/Ase1 to recruit CLASP/Cls1 to stabilize microtubules. Brownian dynamics-kinetic Monte Carlo simulations show that Ase1 and Cls1 activity are sufficient for initial bipolar spindle formation. We conclude that pushing forces generated by microtubule polymerization are sufficient to promote spindle pole separation and the assembly of bipolar spindle in the absence of molecular motors.","doi":"10.1038/ncomms15286","authors":"Rincon SA, Lamson A, Blackwell R, Syrovatkina V, Fraisier V, Paoletti A, Betterton MD, Tran PT","authors_abbrev":"Rincon SA et al.","pubmed_publication_date":"17 May 2017","pubmed_entrez_date":"2017-05-18","publication_year":"2017","canto_session_key":"c833cf237c7875e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-05-18 09:31:40","canto_approved_date":"2022-05-18 15:03:24","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-05-18 09:31:31","canto_added_date":"2017-05-19 00:15:14","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":27,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC15D4.01c","SPBC20F10.06","SPAPB1A10.09","SPBC2F12.13","SPBC106.10","SPAC25G10.07c","SPAC3A11.14c","SPAC664.10","SPAC3G9.12","SPBC1685.15c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2022-05-18"},{"uniquename":"PMID:23661703","title":"Plasticity and epigenetic inheritance of centromere-specific histone H3 (CENP-A)-containing nucleosome positioning in the fission yeast.","citation":"J Biol Chem 2013 Jun 28;288(26):19184-96","abstract":"Nucleosomes containing the specific histone H3 variant CENP-A mark the centromere locus on each chromatin and initiate kinetochore assembly. For the common type of regional centromeres, little is known in molecular detail of centromeric chromatin organization, its propagation through cell division, and how distinct organization patterns may facilitate kinetochore assembly. Here, we show that in the fission yeast S. pombe, a relatively small number of CENP-A/Cnp1 nucleosomes are found within the centromeric core and that their positioning relative to underlying DNA varies among genetically homogenous cells. Consistent with the flexible positioning of Cnp1 nucleosomes, a large portion of the endogenous centromere is dispensable for its essential activity in mediating chromosome segregation. We present biochemical evidence that Cnp1 occupancy directly correlates with silencing of the underlying reporter genes. Furthermore, using a newly developed pedigree analysis assay, we demonstrated the epigenetic inheritance of Cnp1 positioning and quantified the rate of occasional repositioning of Cnp1 nucleosomes throughout cell generations. Together, our results reveal the plasticity and the epigenetically inheritable nature of centromeric chromatin organization.","doi":"10.1074/jbc.M113.471276","authors":"Yao J, Liu X, Sakuno T, Li W, Xi Y, Aravamudhan P, Joglekar A, Li W, Watanabe Y, He X","authors_abbrev":"Yao J et al.","pubmed_publication_date":"28 Jun 2013","pubmed_entrez_date":"2013-05-11","publication_year":"2013","canto_session_key":"232ff8074cf53fae","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7660977","title":"Evolution of the GATase, CPSase, DHOase-like, ATCase multifunctional protein in eukaryotes: genetic and molecular approaches with yeasts S. cerevisiae and S. pombe.","citation":"Adv Exp Med Biol 1994;370:603-6","abstract":"","authors":"Lollier M, Jaquet L, Nedeva T, Lacroute F, Potier S, Souciet JL","authors_abbrev":"Lollier M et al.","pubmed_publication_date":"1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17381331","title":"RNAi-mediated heterochromatin assembly in fission yeast.","citation":"Cold Spring Harb Symp Quant Biol 2006;71:487-96","abstract":"The organization of DNA into heterochromatin domains is critical for a variety of chromosomal functions, including gene silencing, recombination suppression, and chromosome segregation. In fission yeast, factors involved in the RNAi pathway such as Argonaute, Dicer, and RNA-dependent RNA polymerase are required for assembly of heterochromatin structures. The RNAi Argonaute-containing RITS complex and RNA-dependent RNA polymerase localize throughout heterochromatin domains. These factors are important components of a self-reinforcing loop mechanism operating in cis to process repeat transcripts into siRNAs, which involve in heterochromatin assembly. In this paper, we describe our results suggesting that slicing of repeat transcripts by the Argonaute is an important step in their conversion into siRNAs and heterochromatic silencing. Mutations in conserved residues known to be essential for slicer activity of Argonautes result in loss of siRNAs corresponding to centromeric repeats, accumulation of repeat transcripts, and defects in heterochromatin assembly. We also discuss our recent finding that heterochromatin proteins such as Swi6/HP1 serve as a platform that could recruit both silencing and antisilencing factors to heterochromatic loci.","authors":"Zofall M, Grewal SI","authors_abbrev":"Zofall M et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-03-27","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42275217","title":"Rapid aging and disassembly of actin filaments from two evolutionary distant yeasts.","citation":"Cell Rep 2026 Jun 10;45(6):117473","abstract":"Similarities and differences in the self-assembly of actin filaments from different species inform our understanding of its evolution. However, this basic knowledge is largely incomplete. Here, we systematically characterize assembly kinetics for actin from two yeast species that are five hundred million years apart in evolution, Saccharomyces cerevisiae and Schizosaccharomyces pombe, and compare them to the well-studied rabbit muscle actin from which they diverged a billion years ago. We find that, in the ATP state, both yeast actins behave strikingly like mammalian actin at filament barbed ends. In contrast, yeast actin filaments in both the ADP·Pi and the ADP states depolymerize several-fold faster than their mammalian counterparts, and they release inorganic phosphate over 20-fold faster. We show that the absence of methylation on histidine 73 largely accounts for this faster aging of yeast actin filaments. We also reveal biochemical and mechanical differences between the actins of the two yeasts. Our findings suggest that actins are more diverse and biochemically specialized across species than previously recognized.","doi":"10.1016/j.celrep.2026.117473","authors":"Billault-Chaumartin I, Wioland H, Guillotin A, Michelot A, Jégou A, Romet-Lemonne G","authors_abbrev":"Billault-Chaumartin I et al.","pubmed_publication_date":"10 Jun 2026","pubmed_entrez_date":"2026-06-11","publication_year":"2026","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2026-06-11 23:25:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33970532","title":"Magnesium depletion extends fission yeast lifespan via general amino acid control activation.","citation":"Microbiologyopen 2021 Mar;10(2):e1176","abstract":"Nutrients including glucose, nitrogen, sulfur, zinc, and iron are involved in the regulation of chronological lifespan (CLS) of yeast, which serves as a model of the lifespan of differentiated cells of higher organisms. Herein, we show that magnesium (Mg 2+  ) depletion extends CLS of the fission yeast Schizosaccharomyces pombe through a mechanism involving the Ecl1 gene family. We discovered that ecl1 +  expression, which extends CLS, responds to Mg 2+  depletion. Therefore, we investigated the underlying intracellular responses. In amino acid auxotrophic strains, Mg 2+  depletion robustly induces ecl1 +  expression through the activation of the general amino acid control (GAAC) pathway-the equivalent of the amino acid response of mammals. Polysome analysis indicated that the expression of Ecl1 family genes was required for regulating ribosome amount when cells were starved, suggesting that Ecl1 family gene products control the abundance of ribosomes, which contributes to longevity through the activation of the evolutionarily conserved GAAC pathway. The present study extends our understanding of the cellular response to Mg 2+  depletion and its influence on the mechanism controlling longevity.","doi":"10.1002/mbo3.1176","authors":"Ohtsuka H, Kobayashi M, Shimasaki T, Sato T, Akanuma G, Kitaura Y, Otsubo Y, Yamashita A, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2021-05-10","publication_year":"2021","canto_session_key":"7d41b40fbc72d8a6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hokuto Ohtsuka","canto_first_approved_date":"2021-06-10 07:38:34","canto_approved_date":"2023-03-01 16:19:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-21 02:17:45","canto_added_date":"2021-05-12 00:15:04","annotation_curators":[{"name":"Hokuto Ohtsuka","community_curator":true,"annotation_count":4,"orcid":"0000-0001-7843-2602","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1393.08","SPCC70.12c","SPBC36B7.09","SPBP35G2.16c","SPAC18G6.05c","SPBC8E4.12c","SPAC3G9.09c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2021-06-10"},{"uniquename":"PMID:29635344","title":"Histone H3 lysine 36 methyltransferase mobilizes NER factors to regulate tolerance against alkylation damage in fission yeast.","citation":"Nucleic Acids Res 2018 Jun 01;46(10):5061-5074","abstract":"The Set2 methyltransferase and its target, histone H3 lysine 36 (H3K36), affect chromatin architecture during the transcription and repair of DNA double-stranded breaks. Set2 also confers resistance against the alkylating agent, methyl methanesulfonate (MMS), through an unknown mechanism. Here, we show that Schizosaccharomyces pombe (S. pombe) exhibit MMS hypersensitivity when expressing a set2 mutant lacking the catalytic histone methyltransferase domain or a H3K36R mutant (reminiscent of a set2-null mutant). Set2 acts synergistically with base excision repair factors but epistatically with nucleotide excision repair (NER) factors, and determines the timely nuclear accumulation of the NER initiator, Rhp23, in response to MMS. Set2 facilitates Rhp23 recruitment to chromatin at the brc1 locus, presumably to repair alkylating damage and regulate the expression of brc1+ in response to MMS. Set2 also show epistasis with DNA damage checkpoint proteins; regulates the activation of Chk1, a DNA damage response effector kinase; and acts in a similar functional group as proteins involved in homologous recombination. Consistently, Set2 and H3K36 ensure the dynamicity of Rhp54 in DNA repair foci formation after MMS treatment. Overall, our results indicate a novel role for Set2/H3K36me in coordinating the recruitment of DNA repair machineries to timely manage alkylating damage.","doi":"10.1093/nar/gky245","authors":"Lim KK, Nguyen TTT, Li AY, Yeo YP, Chen ES","authors_abbrev":"Lim KK et al.","pubmed_publication_date":"01 Jun 2018","pubmed_entrez_date":"2018-04-11","publication_year":"2018","canto_session_key":"01d2c395653a1af8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-04-12 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1834.04","SPCC18B5.11c","SPAC30D11.07","SPBC543.03c","SPAC29B12.02c","SPBC3D6.10","SPCC330.02","SPBC216.05","SPAC13C5.07"],"gene_count":9,"ltp_gene_count":9},{"uniquename":"PMID:1369064","title":"Inhibition of protein translocation in permeabilized cells of Schizosaccharomyces pombe by puromycin.","citation":"Biosci Biotechnol Biochem 1992 Oct;56(10):1649-54","abstract":"To investigate protein translocation in eukaryotes, we reconstituted a protein translocation system using the permeabilized spheroplasts (P-cells) of the fission yeast Schizosaccharomyces pombe. The precursor of a sex pheromone of Saccharomyces cerevisiae, prepro-alpha-factor, was translocated across the endoplasmic reticulum (ER) of S. pombe posttranslationally, and glycosylated to the same extent as in the ER of S. cerevisiae. This suggested that the size of N-linked core-oligosaccharide in the ER of S. pombe is similar to that in S. cerevisiae. This translocation into the ER of S. pombe was inhibited by puromycin, but the translocation in the P-cells of S. cerevisiae was not inhibited. This difference in sensitivity to puromycin was due to the membrane but not the cytosolic fraction. Our results suggested that the translocation machinery of S. pombe was sensitive to puromycin and different from that of S. cerevisiae.","authors":"Kambe-Honjoh H, Yoda K, Yamasaki M","authors_abbrev":"Kambe-Honjoh H et al.","pubmed_publication_date":"Oct 1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10740815","title":"A Cdc7p-Dbf4p protein kinase activity is conserved from yeast to humans.","citation":"Prog Cell Cycle Res 2000;4:61-9","abstract":"DBF4 and CDC7 were identified as budding yeast cell cycle mutants that arrest immediately before S phase. The Dbf4p and Cdc7p proteins interact to form a protein kinase, Cdc7p being the catalytic subunit and Dbf4p is a cyclin-like molecule that activates the kinase in late G1. Dbf4p also targets Cdc7p to origins of replication where likely substrates include the Mcm proteins. Dbf4p and Cdc7p related proteins occur in the fission yeast and in metazoans. These also phosphorylate Mcm proteins and preliminary evidence indicates a similar function to Dbf4p/Cdc7p in budding yeast. The Dbf4p/Cdc7p activity will therefore very likely be conserved in all eukaryotes.","authors":"Johnston LH, Masai H, Sugino A","authors_abbrev":"Johnston LH et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2000-03-31","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18305104","title":"Regulation and targeting of the fission yeast formin cdc12p in cytokinesis.","citation":"Mol Biol Cell 2008 May;19(5):2208-19","abstract":"Formins are conserved actin nucleators which promote the assembly of actin filaments for the formation of diverse actin structures. In fission yeast Schizosaccharomyces pombe, the formin cdc12p is required specifically in assembly of the actin-based contractile ring during cytokinesis. Here, using a mutational analysis of cdc12p, we identify regions of cdc12p responsible for ring assembly and localization. Profilin-binding residues of the FH1 domain regulate actin assembly and processive barbed-end capping by the FH2 domain. Studies using photobleaching (FRAP) and sensitivity to latrunculin A treatment show that profilin binding modulates the rapid dynamics of actin and cdc12p within the ring in vivo. Visualized by functional GFP-fusion constructs expressed from the endogenous promoter, cdc12p appears in a small number of cytoplasmic motile spot structures that deliver the formin to the ring assembly site, without detectable formation of an intermediate band of \"nodes.\" The FH3/DID region directs interphase spot localization, while an N-terminal region and the FH1-FH2 domains of cdc12p can target its localization to the ring. Mutations in putative DID and DAD regions do not alter regulation, suggesting that cdc12p is not regulated by a canonical autoinhibition mechanism. Our findings provide insights into the regulation of formin activity and the mechanisms of contractile ring dynamics and assembly.","authors":"Yonetani A, Lustig RJ, Moseley JB, Takeda T, Goode BL, Chang F","authors_abbrev":"Yonetani A et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-02-29","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4A8.15c","SPAC1F5.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:33862686","title":"Covariance distributions in single particle tracking.","citation":"Phys Rev E 2021 Mar;103(3-1):032405","abstract":"Several recent experiments, including our own experiments in the fission yeast, Schizosaccharomyces pombe, have characterized the motions of gene loci within living nuclei by measuring the locus position over time, then proceeding to obtain the statistical properties of this motion. To address the question of whether a population of such single-particle tracks, obtained from many different cells, corresponds to a single mode of diffusion, we derive theoretical equations describing the probability distribution of the displacement covariance, assuming the displacement itself is a zero-mean multivariate Gaussian random variable. We also determine the corresponding theoretical means, variances, and third central moments. Bolstering the theory is good agreement between its predictions and the results obtained for various simulated and measured data sets, including simulated particle trajectories undergoing simple and anomalous diffusion, and the measured trajectories of an optically trapped bead in water, and in a viscoelastic polymer solution. We also show that, for sufficiently long tracks, each covariance distribution in all of these examples is well-described by a skew-normal distribution with mean, variance, and skewness given by the theory. However, for the experimentally measured motion of a gene locus in S. pombe, we find that the first two covariance distributions are wider than predicted, although the third and subsequent covariance distributions are well-described by theory. This observation suggests that the origin of the theory-experiment discrepancy in this case is associated with localization noise, which influences only the first two covariances. Thus, we hypothesized that the discrepancy is caused by locus-to-locus heterogeneity in the localization noise, of independent measurements of the same tagged site. Indeed, simulations implementing heterogeneous localization noise revealed that the excess covariance widths can be largely recreated on the basis of heterogeneous noise. Thus, we conclude that the motion of gene loci in fission yeast is consistent with a single mode of diffusion.","doi":"10.1103/PhysRevE.103.032405","authors":"Bailey MLP, Yan H, Surovtsev I, Williams JF, King MC, Mochrie SGJ","authors_abbrev":"Bailey MLP et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2021-04-17","publication_year":"2021","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2021-04-19 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7538479","title":"A rapid permeabilization procedure for accurate quantitative determination of beta-galactosidase activity in yeast cells.","citation":"FEMS Microbiol Lett 1995 May 01;128(2):201-6","abstract":"A procedure is described which allows the rapid permeabilization of yeast cells, Schizosaccharomyces pombe and Saccharomyces cerevisiae, for quantitative in situ assays of beta-galactosidase activity. Yeast cells are permeabilized by incubation in buffer containing 0.2% of the detergent sodium lauroyl sarcosinate without any need for washing or vortexing. This procedure is equally applicable to fresh and frozen samples. It is compared to earlier reported methods and found to be superior by being more accurate and less time-consuming.","authors":"Kippert F","authors_abbrev":"Kippert F","pubmed_publication_date":"01 May 1995","pubmed_entrez_date":"1995-05-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12665550","title":"The endo-beta-1,3-glucanase eng1p is required for dissolution of the primary septum during cell separation in Schizosaccharomyces pombe.","citation":"J Cell Sci 2003 May 01;116(Pt 9):1689-98","abstract":"Schizosaccharomyces pombe cells divide by medial fission throughout contraction of an actomyosin ring and deposition of a multilayered division septum that must be cleaved to release the two daughter cells. Although many studies have focused on the actomoysin ring and septum assembly, little information is available concerning the mechanism of cell separation. Here we describe the characterization of eng1+, a new gene that encodes a protein with detectable endo-beta-1,3-glucanase activity and whose deletion is not lethal to the cells but does interfere in their separation. Electron microscopic observation of mutant cells indicated that this defect is mainly due to the failure of the cells to degrade the primary septum, a structure rich in beta-1,3-glucans, that separates the two sisters cells. Expression of eng1+ varies during the cell cycle, maximum expression being observed before septation, and the protein localizes to a ring-like structure that surrounds the septum region during cell separation. This suggests that it could also be involved in the cleavage of the cylinder of the cell wall that covers the division septum. The expression of eng1+ during vegetative growth is regulated by a C2H2 zinc-finger protein (encoded by the SPAC6G10.12c ORF), which shows significant sequence similarity to the Saccharomyces cerevisiae ScAce2p, especially in the zinc-finger region. Mutants lacking this transcriptional regulator (which we have named ace2+) show a severe cell separation defect, hyphal growth being observed. Thus, ace2p may regulate the expression of the eng1+ gene together with that of other genes whose products are also involved in cell separation.","authors":"Martín-Cuadrado AB, Dueñas E, Sipiczki M, Vázquez de Aldana CR, del Rey F","authors_abbrev":"Martín-Cuadrado AB et al.","pubmed_publication_date":"01 May 2003","pubmed_entrez_date":"2003-04-01","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.09"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:15824112","title":"Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular switch controlling the transcriptional response to increasing levels of hydrogen peroxide.","citation":"J Biol Chem 2005 Jun 17;280(24):23319-27","abstract":"Although activation of the AP-1-like transcription factor Pap1 in Schizosaccharomyces pombe is important for oxidative stress-induced gene expression, this activation is delayed at higher concentrations of peroxide. Here, we reveal that the 2-Cys peroxiredoxin (2-Cys Prx) Tpx1 is required for the peroxide-induced activation of Pap1. Tpx1, like other eukaryotic 2-Cys Prxs, is highly sensitive to oxidation, which inactivates its thioredoxin peroxidase activity. Our data suggest that the reduced thioredoxin peroxidase-active form of Tpx1 is required for the peroxide-induced oxidation and nuclear accumulation of Pap1. Indeed, in contrast to the previously described role for Tpx1 in the activation of the Sty1 stress-activated protein kinase by peroxide, we find that both catalytic cysteines of Tpx1 are required for Pap1 activation. Moreover, overexpression of the conserved sulfiredoxin Srx1, which interacts with and reduces Tpx1, allows rapid activation of Pap1 at higher concentrations of H(2)O(2). Conversely, loss of Srx1 prevents the reduction of oxidized Tpx1 and prolongs the inhibition of Pap1 activation. Collectively, these data suggest that redox regulation of the thioredoxin peroxidase activity of Tpx1 acts as a molecular switch controlling the transcriptional response to H(2)O(2). Furthermore, they reveal that a single eukaryotic 2-Cys Prx regulates peroxide signaling by multiple independent mechanisms.","authors":"Bozonet SM, Findlay VJ, Day AM, Cameron J, Veal EA, Morgan BA","authors_abbrev":"Bozonet SM et al.","pubmed_publication_date":"17 Jun 2005","pubmed_entrez_date":"2005-04-13","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC106.02c","SPCC576.03c","SPAC1783.07c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:1264064","title":"Extrachromosomal inheritance in Schizosaccharomyces pombe. II. Evidence for extrakaryotically inherited respiratory deficient mutants.","citation":"Mol Gen Genet 1976 Feb 27;144(1):75-81","abstract":"In contrast to the wild-type, mutant [ANTr8] is able spontaneously to throw off stable respiratory deficient mutants. The frequency of these mutants is considerably enhanced by treatment with ethidium bromide (EB) or the azo-dye Janus green (JG). An unstable cell state with a petite-like phenotype is found in both mutant [ANTr8] and wild-type after EB-treatment. However, only in the mutant is this unstable cell state followed by the appearance of stable respiratory deficient (RD) mutants. Formation of microcolonies is observed both in [ANTr8] and wild-type. RD mutants were isolated after EB treatment. Three of them (mit-12, mit-25, and mit-30) were analyzed and mit-25 characterized in more detail.","authors":"Wolf K, Lang B, Burger G, Kaudewitz F","authors_abbrev":"Wolf K et al.","pubmed_publication_date":"27 Feb 1976","pubmed_entrez_date":"1976-02-27","publication_year":"1976","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32365869","title":"Combined Use of  Lachancea thermotolerans  and  Schizosaccharomyces pombe  in Winemaking: A Review.","citation":"Microorganisms 2020 Apr 30;8(5)","abstract":"The combined use of  Lachancea thermotolerans  and  Schizosaccharomyces pombe  is a new winemaking biotechnology that aims to solve some modern industrial oenology problems related to warm viticulture regions. These areas are characterized for producing musts with high levels of sugar that can potentially be converted into wines with elevated ethanol contents, which are usually associated with high pH levels. This biotechnology was reported for the first time in 2015, and since then, several scientific articles have been published regarding this topic. These reported scientific studies follow an evolution similar to that performed in the past for  Saccharomyces cerevisiae  and  Oenococcus oeni ; they start by reporting results for basic winemaking parameters at the beginning, later continuing with more advanced parameters. This review compares the results of different researchers that have applied this new biotechnology and have studied wine quality parameters such as ethanol, glycerol, malic acid, lactic acid, amino acids, aroma compounds, or anthocyanins. It is shown that the new biotechnology is repeatedly reported to solve specific winemaking problems such as the lack of acidity, biogenic amines, ethyl carbamate, or undesirable color losses. Such results highlight this biotechnology as a promising option for warm viticulture areas.","doi":"10.3390/microorganisms8050655","authors":"Benito S","authors_abbrev":"Benito S","pubmed_publication_date":"30 Apr 2020","pubmed_entrez_date":"2020-05-06","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-05-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2621446","title":"Purification and properties of glycerol:NADP+ 2-oxidoreductase from Schizosaccharomyces pombe.","citation":"J Gen Microbiol 1989 Mar;135(3):697-701","abstract":"Glycerol:NADP+ 2-oxidoreductase (EC 1.1.1.156) was isolated from Schizosaccharomyces pombe, purified and characterized. It had an Mr of 57,000, and SDS-PAGE revealed two polypeptides, of Mr 25,000 and 30,000. Its coenzyme requirement was satisfied exclusively by NADP. The pH optimum for glycerol oxidation was 9.5, for dihydroxyacetone reduction 6.0. Rates of oxidation with some structurally related diols were three- to six-fold lower than for glycerol, while glyceraldehyde and other carbonyl compounds showed negligible rates of reduction. Neither monovalent nor divalent cations activated the enzyme. Apparent Km and Vmax values were determined. The enzyme is similar to glycerol dehydrogenases isolated from Mucor javanicus and from Dunaliella parva but differs considerably from the glycerol:NAD+ 2-oxidoreductase of S. pombe.","authors":"Marshall JH, Kong YC, Sloan J, May JW","authors_abbrev":"Marshall JH et al.","pubmed_publication_date":"Mar 1989","pubmed_entrez_date":"1989-03-01","publication_year":"1989","canto_session_key":"cee066746e264cd2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-02-08 19:21:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 16:03:45","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-02-08"},{"uniquename":"EMBL:AJ632019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.52"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28545058","title":"A systematic genomic screen implicates nucleocytoplasmic transport and membrane growth in nuclear size control.","citation":"PLoS Genet 2017 May;13(5):e1006767","abstract":"How cells control the overall size and growth of membrane-bound organelles is an important unanswered question of cell biology. Fission yeast cells maintain a nuclear size proportional to cellular size, resulting in a constant ratio between nuclear and cellular volumes (N/C ratio). We have conducted a genome-wide visual screen of a fission yeast gene deletion collection for viable mutants altered in their N/C ratio, and have found that defects in both nucleocytoplasmic mRNA transport and lipid synthesis alter the N/C ratio. Perturbing nuclear mRNA export results in accumulation of both mRNA and protein within the nucleus, and leads to an increase in the N/C ratio which is dependent on new membrane synthesis. Disruption of lipid synthesis dysregulates nuclear membrane growth and results in an enlarged N/C ratio. We propose that both properly regulated nucleocytoplasmic transport and nuclear membrane growth are central to the control of nuclear growth and size.","doi":"10.1371/journal.pgen.1006767","authors":"Kume K, Cantwell H, Neumann FR, Jones AW, Snijders AP, Nurse P","authors_abbrev":"Kume K et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2017-05-26","publication_year":"2017","canto_session_key":"e0fb6894384ffb7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2019-06-29 18:38:05","canto_approved_date":"2024-08-14 08:27:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-27 15:06:17","canto_added_date":"2017-05-27 00:15:14","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":51,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F8.02c","SPBC902.03","SPAC22H10.11c","SPBC32H8.11","SPCC18.06c","SPBC21C3.08c","SPBC21B10.13c","SPAC3G6.02","SPBC106.20","SPBC29B5.01","SPAC31A2.02","SPAC1782.05","SPAC24H6.05","SPAC13G7.03","SPBC3B8.10c","SPAC57A7.04c","SPAC56E4.04c","SPBC16A3.05c","SPAC17C9.13c","SPBC2G2.13c","SPBC1D7.04"],"gene_count":21,"ltp_gene_count":20,"approved_date":"2019-06-29"},{"uniquename":"PMID:29080743","title":"Temperature sensitive point mutations in fission yeast tropomyosin have long range effects on the stability and function of the actin-tropomyosin copolymer.","citation":"Biochem Biophys Res Commun 2018 Nov 25;506(2):339-346","abstract":"The actin cytoskeleton is modulated by regulatory actin-binding proteins which fine-tune the dynamic properties of the actin polymer to regulate function. One such actin-binding protein is tropomyosin (Tpm), a highly-conserved alpha-helical dimer which stabilises actin and regulates interactions with other proteins. Temperature sensitive mutants of Tpm are invaluable tools in the study of actin filament dependent processes, critical to the viability of a cell. Here we investigated the molecular basis of the temperature sensitivity of fission yeast Tpm mutants which fail to undergo cytokinesis at the restrictive temperatures. Comparison of Contractile Actomyosin Ring (CAR) constriction as well as cell shape and size revealed the cdc8.110 or cdc8.27 mutant alleles displayed significant differences in their temperature sensitivity and impact upon actin dependent functions during the cell cycle. In vitro analysis revealed the mutant proteins displayed a different reduction in thermostability, and unexpectedly yield two discrete unfolding domains when acetylated on their amino-termini. Our findings demonstrate how subtle changes in structure (point mutations or acetylation) alter the stability not simply of discrete regions of this conserved cytoskeletal protein but of the whole molecule. This differentially impacts the stability and cellular organisation of this essential cytoskeletal protein.","doi":"10.1016/j.bbrc.2017.10.109","authors":"Johnson CA, Brooker HR, Gyamfi I, O'Brien J, Ashley B, Brazier JE, Dean A, Embling J, Grimsey E, Tomlinson AC, Wilson EG, Geeves MA, Mulvihill DP","authors_abbrev":"Johnson CA et al.","pubmed_publication_date":"25 Nov 2018","pubmed_entrez_date":"2017-10-30","publication_year":"2018","canto_session_key":"f899f218fbb2015e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-11-02 01:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27F1.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9191269","title":"Characterisation of a phospholipase C delta from Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1997 May;25(2):225S","abstract":"","authors":"Slaaby R, Knott T, Davey J","authors_abbrev":"Slaaby R et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"52d277da6d0f8b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-08 16:00:40","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-08-03 13:05:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F8.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-08-03"},{"uniquename":"PMID:9034181","title":"Telomeres. Different means to common ends.","citation":"Nature 1997 Feb 20;385(6618):676-7","abstract":"","authors":"Shore D","authors_abbrev":"Shore D","pubmed_publication_date":"20 Feb 1997","pubmed_entrez_date":"1997-02-20","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19464966","title":"A tale of two tails: activation of DNA damage checkpoint kinase Mec1/ATR by the 9-1-1 clamp and by Dpb11/TopBP1.","citation":"DNA Repair (Amst) 2009 Sep 02;8(9):996-1003","abstract":"The DNA damage and replication checkpoint kinase Mec1/ATR is a member of the PI3-kinase related kinases that function in response to various genotoxic stresses. The checkpoint clamp 9-1-1 (Rad9-Rad1-Hus1 in S. pombe and mammals; Ddc1-Rad17-Mec3 in S. cerevisiae) executes two distinct checkpoint functions. In S. cerevisiae, DNA-bound 9-1-1 directly activates Mec1 kinase activity, a function that has not been demonstrated in other organisms. A second, conserved activity of 9-1-1 is that of TopBP1/Cut5/Dpb11 recruitment to stalled replication sites; subsequent activation of Mec1/ATR is carried out by TopBP1/Cut5/Dpb11. Biochemical studies indicate that the mode of Mec1/ATR activation by S. cerevisiae 9-1-1 is analogous to activation by S. cerevisiae Dpb11 or by vertebrate TopBP1: activation is mediated by the intrinsically disordered C-terminal tail of each activator. The relative contributions made by multiple activators of Mec1/ATR are discussed.","doi":"10.1016/j.dnarep.2009.03.011","authors":"Navadgi-Patil VM, Burgers PM","authors_abbrev":"Navadgi-Patil VM et al.","pubmed_publication_date":"02 Sep 2009","pubmed_entrez_date":"2009-05-26","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15689488","title":"Meiotic S-phase damage activates recombination without checkpoint arrest.","citation":"Mol Biol Cell 2005 Apr;16(4):1651-60","abstract":"Checkpoints operate during meiosis to ensure the completion of DNA synthesis and programmed recombination before the initiation of meiotic divisions. Studies in the fission yeast Schizosaccharomyces pombe suggest that the meiotic response to DNA damage due to a failed replication checkpoint response differs substantially from the vegetative response, and may be influenced by the presence of homologous chromosomes. The checkpoint responses to DNA damage during fission yeast meiosis are not well characterized. Here we report that DNA damage induced during meiotic S-phase does not activate checkpoint arrest. We also find that in wild-type cells, markers for DNA breaks can persist at least to the first meiotic division. We also observe increased spontaneous S-phase damage in checkpoint mutants, which is repaired by recombination without activating checkpoint arrest. Our results suggest that fission yeast meiosis is exceptionally tolerant of DNA damage, and that some forms of spontaneous S-phase damage can be repaired by recombination without activating checkpoint arrest.","authors":"Pankratz DG, Forsburg SL","authors_abbrev":"Pankratz DG et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-02-04","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPCC1259.13","SPBC216.05","SPCC18B5.11c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:42016605","title":"Effects of  rok1  gene deletion on mitosis in fission yeast at appropriate and stressful temperatures and the molecular mechanisms.","citation":"Exp Ther Med 2026 Jun;31(6):151","abstract":"The  rok1  gene encodes the ATP-dependent RNA helicase Rok1, which is involved in regulating the maturation of small subunit ribosomal RNA and thus ribosome biogenesis. However, the regulation of cellular mitotic dynamics by the  rok1  gene deletion is currently unclear. In the present study, fluorescent protein labeling and live cell imaging techniques were used to investigate the effects of  rok 1 deletion on the dynamics of microtubules, actin and kinetochores during mitosis at 25 and 37˚C, and RNA-sequencing and bioinformatics analyses were used to reveal the key genes. Analysis of the live cell imaging results revealed that, in mitosis, the initiation length and contraction length of actin rings were both shortened and the contraction rate was decreased at 25 and 37˚C. The separation process of kinetochores was inhibited at 25 and 37˚C, and the inhibition was more severe at the higher temperature of 37˚C. Analysis of RNA sequencing results showed that upregulation of  myo51  and  blt1  resulted in delayed actin ring assembly and slowed actin ring contraction in the  rok1 Δ strain. In addition,  psm1  and  psc3  were upregulated and are key genes affecting the ability of kinetochores to move on the spindle and the cohesion of sister chromatids. The present study revealed that the Rok1 protein not only influences the actin polymerization process, participate in the regulation of actin ring assembly and contraction, and cytoplasmic division, but also affects the migration ability of kinetochores on the spindle and participate in the regulation of the formation and maintenance of cohesion between sister chromatids, which provides a certain scientific basis for further exploring the function of the Rok1 protein in cell division.","doi":"10.3892/etm.2026.13145","authors":"He J, Liu M, Xu J, Ding X, Hou Y","authors_abbrev":"He J et al.","pubmed_publication_date":"Jun 2026","pubmed_entrez_date":"2026-04-22","publication_year":"2026","canto_session_key":"fec3c53f99c81aac","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-04-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14681424","title":"yMGV: a cross-species expression data mining tool.","citation":"Nucleic Acids Res 2004 Jan 01;32(Database issue):D323-5","abstract":"The yeast Microarray Global Viewer (yMGV @ http://transcriptome.ens.fr/ymgv) was created 3 years ago as a database that houses a collection of Saccharomyces cerevisiae and Schizosaccharo myces pombe microarray data sets published in 82 different articles. yMGV couples data mining tools with a user-friendly web interface so that, with a few mouse clicks, one can identify the conditions that affect the expression of a gene or list of genes regulated in a set of experiments. One of the major new features we present here is a set of tools that allows for inter-organism comparisons. This should enable the fission yeast community to take advantage of the large amount of available information on budding yeast transcriptome. New tools and ongoing developments are also presented here.","authors":"Lelandais G, Le Crom S, Devaux F, Vialette S, Church GM, Jacq C, Marc P","authors_abbrev":"Lelandais G et al.","pubmed_publication_date":"01 Jan 2004","pubmed_entrez_date":"2003-12-19","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32101481","title":"DYRK kinase Pom1 drives F-BAR protein Cdc15 from the membrane to promote medial division.","citation":"Mol Biol Cell 2020 Apr 15;31(9):917-929","abstract":"In many organisms, positive and negative signals cooperate to position the division site for cytokinesis. In the rod-shaped fission yeast  Schizosaccharomyces pombe , symmetric division is achieved through anillin/Mid1-dependent positive cues released from the central nucleus and negative signals from the DYRK-family polarity kinase Pom1 at cell tips. Here we establish that Pom1's kinase activity prevents septation at cell tips even if Mid1 is absent or mislocalized. We also find that Pom1 phosphorylation of F-BAR protein Cdc15, a major scaffold of the division apparatus, disrupts Cdc15's ability to bind membranes and paxillin, Pxl1, thereby inhibiting Cdc15's function in cytokinesis. A Cdc15 mutant carrying phosphomimetic versions of Pom1 sites or deletion of Cdc15 binding partners suppresses division at cell tips in cells lacking both Mid1 and Pom1 signals. Thus, inhibition of Cdc15-scaffolded septum formation at cell poles is a key Pom1 mechanism that ensures medial division.","doi":"10.1091/mbc.E20-01-0026","authors":"Bhattacharjee R, Mangione MC, Wos M, Chen JS, Snider CE, Roberts-Galbraith RH, McDonald NA, Presti LL, Martin SG, Gould KL","authors_abbrev":"Bhattacharjee R et al.","pubmed_publication_date":"15 Apr 2020","pubmed_entrez_date":"2020-02-27","publication_year":"2020","canto_session_key":"1de58f8a4e93861a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rahul Bhattacharjee","canto_first_approved_date":"2020-06-16 19:05:11","canto_approved_date":"2024-04-02 15:39:00","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-06-03 21:51:30","canto_added_date":"2020-02-28 01:15:04","annotation_curators":[{"name":"Rahul Bhattacharjee","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC83.18c","SPAC20G8.05c","SPCC4B3.15","SPCC1919.10c","SPAC23D3.06c","SPAC2F7.03c","SPBC4F6.12"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2020-06-16"},{"uniquename":"PMID:27647921","title":"Molecular organization of cytokinesis nodes and contractile rings by super-resolution fluorescence microscopy of live fission yeast.","citation":"Proc Natl Acad Sci U S A 2016 Oct 04;113(40):E5876-E5885","abstract":"Cytokinesis in animals, fungi, and amoebas depends on the constriction of a contractile ring built from a common set of conserved proteins. Many fundamental questions remain about how these proteins organize to generate the necessary tension for cytokinesis. Using quantitative high-speed fluorescence photoactivation localization microscopy (FPALM), we probed this question in live fission yeast cells at unprecedented resolution. We show that nodes, protein assembly precursors to the contractile ring, are discrete structural units with stoichiometric ratios and distinct distributions of constituent proteins. Anillin Mid1p, Fes/CIP4 homology-Bin/amphiphysin/Rvs (F-BAR) Cdc15p, IQ motif containing GTPase-activating protein (IQGAP) Rng2p, and formin Cdc12p form the base of the node that anchors the ends of myosin II tails to the plasma membrane, with myosin II heads extending into the cytoplasm. This general node organization persists in the contractile ring where nodes move bidirectionally during constriction. We observed the dynamics of the actin network during cytokinesis, starting with the extension of short actin strands from nodes, which sometimes connected neighboring nodes. Later in cytokinesis, a broad network of thick bundles coalesced into a tight ring around the equator of the cell. The actin ring was ∼125 nm wide and ∼125 nm thick. These observations establish the organization of the proteins in the functional units of a cytokinetic contractile ring.","authors":"Laplante C, Huang F, Tebbs IR, Bewersdorf J, Pollard TD","authors_abbrev":"Laplante C et al.","pubmed_publication_date":"04 Oct 2016","pubmed_entrez_date":"2016-09-21","publication_year":"2016","canto_session_key":"568a1bdad3bc0736","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-09-22 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29149173","title":"Trade-off and flexibility in the dynamic regulation of the cullin-RING ubiquitin ligase repertoire.","citation":"PLoS Comput Biol 2017 Nov;13(11):e1005869","abstract":"Cullin-RING ubiquitin ligases (CRLs) catalyze the ubiquitylation of substrates many of which are degraded by the 26S proteasome. Their modular architecture enables recognition of numerous substrates via exchangeable substrate receptors that competitively bind to a cullin scaffold with high affinity. Due to the plasticity of these interactions there is ongoing uncertainty how cells maintain a flexible CRL repertoire in view of changing substrate loads. Based on a series of in vivo and in vitro studies, different groups proposed that the exchange of substrate receptors is mediated by a protein exchange factor named Cand1. Here, we have performed mathematical modeling to provide a quantitative underpinning of this hypothesis. First we show that the exchange activity of Cand1 necessarily leads to a trade-off between high ligase activity and fast receptor exchange. Supported by measurements we argue that this trade-off yields an optimal Cand1 concentration in cells where the time scale for substrate degradation becomes minimal. In a second step we show through simulations that (i) substrates bias the CRL repertoire leading to preferential assembly of ligases for which substrates are available and (ii) differences in binding affinities or substrate receptor abundances create a temporal hierarchy for the degradation of substrates. Finally, we compare the Cand1-mediated exchange cycle with an alternative architecture lacking Cand1 which indicates superiority of a system with exchange factor if substrate receptors bind substrates and the cullin scaffold in a random order. Together, our results provide general constraints for the operating regimes of molecular exchange systems and suggest that Cand1 endows the CRL network with the properties of an \"on demand\" system allowing cells to dynamically adjust their CRL repertoire to fluctuating substrate abundances.","doi":"10.1371/journal.pcbi.1005869","authors":"Straube R, Shah M, Flockerzi D, Wolf DA","authors_abbrev":"Straube R et al.","pubmed_publication_date":"Nov 2017","pubmed_entrez_date":"2017-11-18","publication_year":"2017","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2017-12-15 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G6.12","SPAC1565.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11907681","title":"Inositol is specifically involved in the sexual program of the fission yeast Schizosaccharomyces pombe.","citation":"Arch Microbiol 2002 Mar;177(3):251-8","abstract":"The fission yeast Schizosaccharomyces pombe is a natural auxotroph for inositol and fails to grow in the complete absence of it. It was previously reported that a small concentration of inositol in the culture medium supports vegetative growth, but not mating and sporulation, and a tenfold of that concentration also supports mating and sporulation. The purpose of the present work was to investigate whether a moderate inositol starvation specifically affected events of the sexual program of development. A homothallic culture grown to the stationary phase in medium with a small inositol concentration was sterile but cells in the stationary phase of growth synchronously entered and completed the sexual cycle when inositol was added, without need of previous cell divisions. This suggests the involvement of inositol in a mechanism (or mechanisms) of the sexual program. The events of the program that were affected by inositol starvation were investigated. Commitment to mating and production of pheromone M were shown not to be inositol-dependent. A diploid strain homozygous at the mating-type locus and carrying a pat1-114 temperature-sensitive mutation in homozygous configuration sporulated under inositol starvation at the restrictive temperature; therefore starvation did not directly affect meiosis or sporulation. In contrast, production of pheromone P and the response of cells to pheromones were found to be inositol-dependent. The possibility that inositol or one of its derivative compounds is involved in pheromone P secretion and in pheromone signal reception is discussed.","authors":"Voicu PM, Poitelea M, Schweingruber E, Rusu M","authors_abbrev":"Voicu PM et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-22","publication_year":"2002","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40861011","title":"Faithful inheritance: Parental histone recycling and epigenetic memory in fission yeast.","citation":"Cell Insight 2025 Oct;4(5):100275","abstract":"Accurate transmission of chromatin states during DNA replication is central to epigenetic inheritance. Recent advances have illuminated mechanisms by which parental histones, which carry key post-translational modifications, are recycled and redistributed to daughter strands. This review synthesizes emerging insights into the molecular machinery that mediates histone recycling during replication. It highlights the interplay between histone chaperones and replication factors and examines how perturbations in these pathways influence heterochromatin inheritance. The fission yeast serves as a powerful model for recent investigations, revealing new principles that are conserved across eukaryotes.","doi":"10.1016/j.cellin.2025.100275","authors":"Fang Y, Toda T, Jia S","authors_abbrev":"Fang Y et al.","pubmed_publication_date":"Oct 2025","pubmed_entrez_date":"2025-08-27","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-08-27 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3D6.09","SPAC694.06c","SPBC4.04c","SPCC16C4.22"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:20453258","title":"Living on the edge: stress and activation of stress responses promote lifespan extension.","citation":"Aging (Albany NY) 2010 Apr;2(4):231-7","abstract":"Oxidative stress constitutes the basis of physio-pathological situations such as neurodegenerative diseases and aging. However, sublethal exposure to toxic molecules such as reactive oxygen species can induce cellular responses that result in stress fitness. Studies in Schizosaccharomyces pombe have recently showed that the Sty1 MAP kinase, known to be activated by hydrogen peroxide and other cellular stressors, plays a pivotal role in promoting fitness and longevity when it becomes activated by calorie restriction, a situation which induces oxidative metabolism and reactive oxygen species production. Activation of the MAP kinase by calorie restriction during logarithmic growth induces a transcriptional anti-stress response including genes essential to promote lifespan extension. Importantly enough, the lifespan promotion exerted by deletion of the pka1 or sck2 genes, inactivating the two main nutrient-responsive pathways, is dependent on the presence of a functional Sty1 stress pathway, since double mutants also lacking Sty1 or its main substrate Atf1 do not display extended viability. In this Research Perspective, we review these findings in relation to previous reports and extend important aspects of the original study. We propose that moderate stress levels that are not harmful for cells can make them stronger.","authors":"Zuin A, Castellano-Esteve D, Ayté J, Hidalgo E","authors_abbrev":"Zuin A et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-05-11","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26F1.10c","SPBC29B5.01","SPAC8C9.03","SPAC24B11.06c","SPAC22E12.14c","SPBC106.10"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:18583929","title":"An old HAT in human p300/CBP and yeast Rtt109.","citation":"Cell Cycle 2008 Jun 15;7(12):1884-6","abstract":"The crystal structure of the human p300 histone acetyltransferase (HAT) domain reveals a familiar alpha + beta fold with unique structural elaborations that merit its classification as a third divergent HAT branch alongside the GCN5-related N-acetyltransferase (GNAT) and MYST (MOZ, Ybf2/Sas3, Sas2, Tip60) families. Two key departures from the core GNAT/MYST HAT fold--a long unstructured chain (or \"flap\") overlaying the acetyl-CoA (AcCoA) binding groove, and a four-alpha-helix \"tower\" excursion from the main beta-sheet--critically contribute to the recognition and presumptive catalytic machinery of p300/CBP HAT enzymes. Kinetic and mutant analysis of this enlarged residue constellation in p300 (which is distinct from functional fingerprints drawn from GNAT or MYST complexes) led Liu et al., to suggest that p300/CBP works with an unorthodox \"hit and run\" mechanism that enlists Tyr1467 as the critical catalytic residue. In order to extend the evolutionary testbed for this variant HAT mechanism beyond the thin roll of p300/CBP orthologs, I propose that Rtt109, a novel yeast HAT that has so far eluded classification, is the prototype of a fungal clan of p300-related enzymes that preserve the embellished HAT fold, but further diversify its catalytic options.","authors":"Bazan JF","authors_abbrev":"Bazan JF","pubmed_publication_date":"15 Jun 2008","pubmed_entrez_date":"2008-06-28","publication_year":"2008","canto_session_key":"c846a1d0d31488c6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 10:03:41","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-20 09:55:46","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC342.06c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:5903108","title":"Structural changes in the cell wall of Schizosaccharomyces pombe during cell division.","citation":"J Bacteriol 1966 Jan;91(1):428-35","abstract":"Streiblová, Eva (Czechoslovak Academy of Sciences, Prague, Czechoslovakia), I. Málek, and K. Beran. Structural changes in the cell wall of Schizosaccharomyces pombe during cell division. J. Bacteriol. 91:428-435. 1966.-Individual stages of growing and dividing cells of Schizosaccharomyces pombe were studied by means of fluorescence and electron microscopy with the use of metal-shadowed isolated walls, replicas, and ultrathin sections. Vegetative cells were found to contain division scars (six at the most); their formation and structure are described. More data on the growth of arthrospores were obtained. New structural observations were made on the architecture of the cell wall (original wall ring, polar cell wall, plug wall band, additional wall ring). Structural changes of cell surfaces and lateral walls during fission are represented schematically to the fourth generation. The question of origin of the septum is discussed, and on this basis the entire structure of the cell wall is interpreted.","authors":"Streiblová E, Málek I, Beran K","authors_abbrev":"Streiblová E et al.","pubmed_publication_date":"Jan 1966","pubmed_entrez_date":"1966-01-01","publication_year":"1966","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16940755","title":"Stress-induced switch to pseudohyphal growth in S. pombe.","citation":"Cell Cycle 2006 Sep;5(18):2138-45","abstract":"Several genetic mutants of fission yeast (Schizosaccharomyces pombe) that form multiple septa and pseudohyphae (i.e., branching growth) have been isolated.(1-15) The current understanding of these mutants is that they lack the ability to separate the two sister cells after formation of the septum. Here it is shown that switching to multisepta and pseudohyphal growth can be induced in a reversible manner in wild-type S. pombe cells by changing the growth conditions, thus indicating an inherent cellular switch. Flow cytometry profiles of exponentially growing cultures of both wild-type and mutant cells further support that a bi-stable switch is controlling the morphological state of the cell in a stress-dependent manner.","authors":"Borup MT","authors_abbrev":"Borup MT","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-08-31","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17477863","title":"Global transcriptional responses of fission and budding yeast to changes in copper and iron levels: a comparative study.","citation":"Genome Biol 2007;8(5):R73","abstract":"Recent studies in comparative genomics demonstrate that interspecies comparison represents a powerful tool for identifying both conserved and specialized biologic processes across large evolutionary distances. All cells must adjust to environmental fluctuations in metal levels, because levels that are too low or too high can be detrimental. Here we explore the conservation of metal homoeostasis in two distantly related yeasts.\nWe examined genome-wide gene expression responses to changing copper and iron levels in budding and fission yeast using DNA microarrays. The comparison reveals conservation of only a small core set of genes, defining the copper and iron regulons, with a larger number of additional genes being specific for each species. Novel regulatory targets were identified in Schizosaccharomyces pombe for Cuf1p (pex7 and SPAC3G6.05) and Fep1p (srx1, sib1, sib2, rds1, isu1, SPBC27B12.03c, SPAC1F8.02c, and SPBC947.05c). We also present evidence refuting a direct role of Cuf1p in the repression of genes involved in iron uptake. Remarkable differences were detected in responses of the two yeasts to excess copper, probably reflecting evolutionary adaptation to different environments.\nThe considerable evolutionary distance between budding and fission yeast resulted in substantial diversion in the regulation of copper and iron homeostasis. Despite these differences, the conserved regulation of a core set of genes involved in the uptake of these metals provides valuable clues to key features of metal metabolism.","authors":"Rustici G, van Bakel H, Lackner DH, Holstege FC, Wijmenga C, Bähler J, Brazma A","authors_abbrev":"Rustici G et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-05-05","publication_year":"2007","canto_session_key":"c696c92aed57f6fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-08-25 14:37:55","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-08-25 14:17:34","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.08","SPAC3G6.05","SPAC227.13c","SPAC1F8.03c","SPBC4F6.09","SPBC27B12.03c","SPBC23G7.16","SPAC1F7.07c","SPAC1142.05","SPAC1F8.02c","SPBC1683.09c","SPAC23G3.03","SPAC343.12","SPAC23E2.01","SPBC947.05c","SPBC106.02c","SPAC17D4.01","SPAC23G3.02c","SPAC31A2.11c","SPCC1393.10"],"gene_count":20,"ltp_gene_count":2,"approved_date":"2016-08-25"},{"uniquename":"PMID:25109978","title":"The fission yeast Schizosaccharomyces pombe as a model to understand how peroxiredoxins influence cell responses to hydrogen peroxide.","citation":"Biochem Soc Trans 2014 Aug;42(4):909-16","abstract":"As a more selectively reactive oxygen species, H2O2 (hydrogen peroxide) has been co-opted as a signalling molecule, but high levels can still lead to lethal amounts of cell damage. 2-Cys Prxs (peroxiredoxins) are ubiquitous thioredoxin peroxidases which utilize reversibly oxidized catalytic cysteine residues to reduce peroxides. As such, Prxs potentially make an important contribution to the repertoire of cell defences against oxidative damage. Although the abundance of eukaryotic 2-Cys Prxs suggests an important role in maintaining cell redox, the surprising sensitivity of their thioredoxin peroxidase activity to inactivation by H2O2 has raised questions as to their role as an oxidative stress defence. Indeed, work in model yeast has led the way in revealing that Prxs do much more than simply remove peroxides and have even uncovered circumstances where their thioredoxin peroxidase activity is detrimental. In the present paper, we focus on what we have learned from studies in the fission yeast Schizosaccharomyces pombe about the different roles of 2-Cys Prxs in responses to H2O2 and discuss the general implications of these findings for other systems.","doi":"10.1042/BST20140059","authors":"Veal EA, Tomalin LE, Morgan BA, Day AM","authors_abbrev":"Veal EA et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-08-12","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-08-13 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6559822","title":"An antisuppressor mutation of Schizosaccharomyces pombe affects the post-transcriptional modification of the \"wobble\" base in the anticodon of tRNAs.","citation":"J Biol Chem 1984 Mar 10;259(5):2856-62","abstract":"The screening of antisuppressor mutants of the yeast Schizosaccharomyces pombe has been successfully accomplished with high resolution liquid chromatographic methods for the analysis of tRNA nucleosides. Antisuppressor mutations reduce or abolish the function of nonsense suppressor-tRNAs or other informational suppressors. Nonradioactive or 35S-labeled unfractionated tRNA from various strains was digested to nucleosides and analyzed by high performance liquid chromatography. The mutant sin3 has lost the nucleoside 5-(methoxycarbonylmethyl)-2-thiouridine from its tRNA in comparison to parental strains. In eukaryotes this nucleoside is found at the first position of the anticodon (wobble position) in several isoacceptor tRNAs that preferentially recognize codons ending with adenosine. The sin3 mutation reduces the efficiency of UGA and UAA suppressor tRNASer and suppressor tRNALeu. The genetic cosegregation of modification loss, antisuppressor phenotype, and a change in cell size is demonstrated. This indicates that a single mutation in the structural gene for a tRNA modification enzyme causes the three different phenotypes.","authors":"Heyer WD, Thuriaux P, Kohli J, Ebert P, Kersten H, Gehrke C, Kuo KC, Agris PF","authors_abbrev":"Heyer WD et al.","pubmed_publication_date":"10 Mar 1984","pubmed_entrez_date":"1984-03-10","publication_year":"1984","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21127511","title":"Understanding of the Hsp90 molecular chaperone reaches new heights.","citation":"Nat Struct Mol Biol 2010 Dec;17(12):1400-4","abstract":"Heat shock protein 90 (Hsp90) was the focus of a recent meeting in the Swiss Alps, where the Hsp90 community met to discuss the operation and functions of this ubiquitous and essential molecular chaperone.","doi":"10.1038/nsmb1210-1400","authors":"Vaughan CK, Neckers L, Piper PW","authors_abbrev":"Vaughan CK et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-12-04","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC926.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10712694","title":"The respiratory gene OXA1 has two fission yeast orthologues which together encode a function essential for cellular viability.","citation":"Mol Microbiol 2000 Mar;35(5):1135-45","abstract":"The Saccharomyces cerevisiae nuclear gene OXA1, which is conserved from prokaryotes to human, was shown to be essential for cytochrome c oxidase and F1F0-ATP synthase biogenesis. We have searched for an orthologue of OXA1 in Schizosaccharomyces pombe, another yeast that is highly diverged from S. cerevisiae and which could more closely model higher eukaryotes. In particular, S. pombe exhibits a limited growth under anaerobic conditions and is petite negative, that is it does not tolerate large deletions of its mitochondrial DNA. Surprisingly, two S. pombe cDNAs able to complement an S. cerevisiae oxa1 mutation were isolated. The corresponding genes have different chromosomal locations and intron contents. They encode distinct proteins, both sharing a weak sequence identity one with the other and with Oxa1p. A phenotypic analysis of both single inactivations demonstrates that only one gene is essential for respiration in S. pombe. However, the double inactivation is lethal. This work gives new insight into the dependence of S. pombe viability upon oxa1 function, providing evidence of a connection between petite negativity, a functional respiratory chain and F1F0-ATP synthase complex in S. pombe.","authors":"Bonnefoy N, Kermorgant M, Groudinsky O, Dujardin G","authors_abbrev":"Bonnefoy N et al.","pubmed_publication_date":"Mar 2000","pubmed_entrez_date":"2000-03-11","publication_year":"2000","canto_session_key":"fea2937498c01faf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-21 14:28:26","canto_approved_date":"2023-08-03 09:41:27","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-10-21 14:28:02","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.03","SPAC9G1.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-10-21"},{"uniquename":"EMBL:SPD225","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41426960","title":"Localizations of the septin Spn4 tagged with GFP and mEGFP in fission yeast.","citation":"MicroPubl Biol 2025;2025","abstract":"Septins are cytoskeletal proteins crucial for cell division and many other processes. In fission yeast, septins localize to the division site during septum formation. Recently, we conducted a study that elucidates the localizations and functionalities of epitope-tagged septins. However, some questions remain outstanding. Here we assessed the impacts of monomeric mEGFP and dimeric GFP(S65T) on the septin Spn4 tagged at either of its terminus. We found that septin levels were important for its function, Spn4-mEGFP localized normally to the division site, but GFP(S65T)-Spn4 formed elongated structures ectopically, further highlighting that dimeric tags are more disruptive to septin localizations.","doi":"10.17912/micropub.biology.001930","authors":"Gregory JR, Ricottilli NJ, Wu JQ","authors_abbrev":"Gregory JR et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-12-22","publication_year":"2025","canto_session_key":"e088e70b17f84f2c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-23 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35602970","title":"Chl1 coordinates with H3K9 methyltransferase Clr4 to reduce the accumulation of RNA-DNA hybrids and maintain genome stability.","citation":"iScience 2022 May 20;25(5):104313","abstract":"A genome-wide analysis in  Schizosaccharomyces pombe  indicated that double-deletion mutants of Chl1 and histone H3K9 methyltransferase complex factors are synthetically sick. Here, we show that loss of Chl1 increases the accumulation of RNA-DNA hybrids at pericentromeric dg and dh repeats in the absence of the H3K9 methyltransferase Clr4, which leads to genome instability, including more severe defects in chromosome segregation and increased chromatin accessibility. Localization of Chl1 at pericentromeric regions depends on a subunit of replication protein A (RPA), Ssb1. In wild-type (WT) cells, transcriptionally repressed heterochromatin prevents the formation of RNA-DNA hybrids. When Clr4 is deleted, dg and dh repeats are highly transcribed. Then Ssb1 associates with the displaced single-stranded DNA (ssDNA) and recruits Chl1 to resolve the RNA-DNA hybrids. Together, our data suggest that Chl1 coordinates with Clr4 to eliminate RNA-DNA hybrids, which contributes to the maintenance of genome integrity.","doi":"10.1016/j.isci.2022.104313","authors":"He D, Guo Y, Cheng J, Wang Y","authors_abbrev":"He D et al.","pubmed_publication_date":"20 May 2022","pubmed_entrez_date":"2022-05-23","publication_year":"2022","canto_session_key":"d0cd9cd405be4a5a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-05-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18059460","title":"Reconstitution of a microtubule plus-end tracking system in vitro.","citation":"Nature 2007 Dec 13;450(7172):1100-5","abstract":"The microtubule cytoskeleton is essential to cell morphogenesis. Growing microtubule plus ends have emerged as dynamic regulatory sites in which specialized proteins, called plus-end-binding proteins (+TIPs), bind and regulate the proper functioning of microtubules. However, the molecular mechanism of plus-end association by +TIPs and their ability to track the growing end are not well understood. Here we report the in vitro reconstitution of a minimal plus-end tracking system consisting of the three fission yeast proteins Mal3, Tip1 and the kinesin Tea2. Using time-lapse total internal reflection fluorescence microscopy, we show that the EB1 homologue Mal3 has an enhanced affinity for growing microtubule end structures as opposed to the microtubule lattice. This allows it to track growing microtubule ends autonomously by an end recognition mechanism. In addition, Mal3 acts as a factor that mediates loading of the processive motor Tea2 and its cargo, the Clip170 homologue Tip1, onto the microtubule lattice. The interaction of all three proteins is required for the selective tracking of growing microtubule plus ends by both Tea2 and Tip1. Our results dissect the collective interactions of the constituents of this plus-end tracking system and show how these interactions lead to the emergence of its dynamic behaviour. We expect that such in vitro reconstitutions will also be essential for the mechanistic dissection of other plus-end tracking systems.","authors":"Bieling P, Laan L, Schek H, Munteanu EL, Sandblad L, Dogterom M, Brunner D, Surrey T","authors_abbrev":"Bieling P et al.","pubmed_publication_date":"13 Dec 2007","pubmed_entrez_date":"2007-12-07","publication_year":"2007","canto_session_key":"af3180f6af4fa627","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-05-30 18:04:17","canto_approved_date":"2022-05-30 18:04:17","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-05-30 18:04:09","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":1,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.20c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-05-30"},{"uniquename":"PMID:34217291","title":"Analysis and application of a suite of recombinant endo-β(1,3)-D-glucanases for studying fungal cell walls.","citation":"Microb Cell Fact 2021 Jul 03;20(1):126","abstract":"The fungal cell wall is an essential and robust external structure that protects the cell from the environment. It is mainly composed of polysaccharides with different functions, some of which are necessary for cell integrity. Thus, the process of fractionation and analysis of cell wall polysaccharides is useful for studying the function and relevance of each polysaccharide, as well as for developing a variety of practical and commercial applications. This method can be used to study the mechanisms that regulate cell morphogenesis and integrity, giving rise to information that could be applied in the design of new antifungal drugs. Nonetheless, for this method to be reliable, the availability of trustworthy commercial recombinant cell wall degrading enzymes with non-contaminating activities is vital.\nHere we examined the efficiency and reproducibility of 12 recombinant endo-β(1,3)-D-glucanases for specifically degrading the cell wall β(1,3)-D-glucan by using a fast and reliable protocol of fractionation and analysis of the fission yeast cell wall. This protocol combines enzymatic and chemical degradation to fractionate the cell wall into the four main polymers: galactomannoproteins, α-glucan, β(1,3)-D-glucan and β(1,6)-D-glucan. We found that the GH16 endo-β(1,3)-D-glucanase PfLam16A from Pyrococcus furiosus was able to completely and reproducibly degrade β(1,3)-D-glucan without causing the release of other polymers. The cell wall degradation caused by PfLam16A was similar to that of Quantazyme, a recombinant endo-β(1,3)-D-glucanase no longer commercially available. Moreover, other recombinant β(1,3)-D-glucanases caused either incomplete or excessive degradation, suggesting deficient access to the substrate or release of other polysaccharides.\nThe discovery of a reliable and efficient recombinant endo-β(1,3)-D-glucanase, capable of replacing the previously mentioned enzyme, will be useful for carrying out studies requiring the digestion of the fungal cell wall β(1,3)-D-glucan. This new commercial endo-β(1,3)-D-glucanase will allow the study of the cell wall composition under different conditions, along the cell cycle, in response to environmental changes or in cell wall mutants. Furthermore, this enzyme will also be greatly valuable for other practical and commercial applications such as genome research, chromosomes extraction, cell transformation, protoplast formation, cell fusion, cell disruption, industrial processes and studies of new antifungals that specifically target cell wall synthesis.","doi":"10.1186/s12934-021-01616-0","authors":"Carvalho VSD, Gómez-Delgado L, Curto MÁ, Moreno MB, Pérez P, Ribas JC, Cortés JCG","authors_abbrev":"Carvalho VSD et al.","pubmed_publication_date":"03 Jul 2021","pubmed_entrez_date":"2021-07-04","publication_year":"2021","canto_session_key":"68bc2f11f0f9f139","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-07-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34849842","title":"The sixth transmembrane region of a pheromone G-protein coupled receptor, Map3, is implicated in discrimination of closely related pheromones in Schizosaccharomyces pombe.","citation":"Genetics 2021 Dec 10;219(4)","abstract":"Most sexually reproducing organisms have the ability to recognize individuals of the same species. In ascomycete fungi including yeasts, mating between cells of opposite mating type depends on the molecular recognition of two peptidyl mating pheromones by their corresponding G-protein coupled receptors (GPCRs). Although such pheromone/receptor systems are likely to function in both mate choice and prezygotic isolation, very few studies have focused on the stringency of pheromone receptors. The fission yeast Schizosaccharomyces pombe has two mating types, Plus (P) and Minus (M). Here, we investigated the stringency of the two GPCRs, Mam2 and Map3, for their respective pheromones, P-factor and M-factor, in fission yeast. First, we switched GPCRs between S. pombe and the closely related species Schizosaccharomyces octosporus, which showed that SoMam2 (Mam2 of S. octosporus) is partially functional in S. pombe, whereas SoMap3 (Map3 of S. octosporus) is not interchangeable. Next, we swapped individual domains of Mam2 and Map3 with the respective domains in SoMam2 and SoMap3, which revealed differences between the receptors both in the intracellular regions that regulate the downstream signaling of pheromones and in the activation by the pheromone. In particular, we demonstrated that two amino acid residues of Map3, F214 and F215, are key residues important for discrimination of closely related M-factors. Thus, the differences in these two GPCRs might reflect the significantly distinct stringency/flexibility of their respective pheromone/receptor systems; nevertheless, species-specific pheromone recognition remains incomplete.","doi":"10.1093/genetics/iyab150","authors":"Seike T, Sakata N, Shimoda C, Niki H, Furusawa C","authors_abbrev":"Seike T et al.","pubmed_publication_date":"10 Dec 2021","pubmed_entrez_date":"2021-12-01","publication_year":"2021","canto_session_key":"97737842b82bf29d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-03 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17333280","title":"Cytoplasmatic post-transcriptional regulation and intracellular signalling.","citation":"Mol Genet Genomics 2007 Apr;277(4):341-55","abstract":"Studies of intracellular signalling have traditionally focused on regulation at the levels of initiation of transcription on one hand, and post-translational regulation on the other. More recently, it is becoming apparent that the post-transcriptional level of gene expression is also subject to regulation by signalling pathways. The emphasis in this review is on short-term regulation of mRNAs at the levels of degradation and frequency of translation. Interplay between the mRNA translation and degradation machineries and mainly the TOR, stress-induced MAP kinase (SAPK), and DNA damage checkpoint pathways is discussed. Since a large fraction of the molecular mechanisms has been dissected using molecular genetics methods in yeast, most of the examples in this review are from budding and fission yeast. Some parallels are drawn to plant and animal cells. This review is intended for those more familiar with intracellular signalling, and who realise that post-transcriptional regulation may be an underemphasised level of signalling output.","authors":"Sunnerhagen P","authors_abbrev":"Sunnerhagen P","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-03-03","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084833","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.21"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:12000947","title":"Cell biology: keeping the genome in shape.","citation":"Nature 2002 May 09;417(6885):135-6","abstract":"","authors":"Uhlmann F","authors_abbrev":"Uhlmann F","pubmed_publication_date":"09 May 2002","pubmed_entrez_date":"2002-05-10","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC306.03c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:12535531","title":"A cell cycle-regulated GATA factor promotes centromeric localization of CENP-A in fission yeast.","citation":"Mol Cell 2003 Jan;11(1):175-87","abstract":"CENP-A, the centromere-specific histone H3 variant, plays a crucial role in organizing kinetochore chromatin for precise chromosome segregation. We have isolated Ams2, a Daxx-like motif-containing GATA factor, and histone H4, as multicopy suppressors of cnp1-1, an S. pombe CENP-A mutant. While depletion of Ams2 results in the reduction of CENP-A binding to the centromere and chromosome missegregation, increasing its dosage restores association of a CENP-A mutant protein with centromeres. Conversely, overexpression of CENP-A or histone H4 suppresses an ams2 disruptant. The intracellular amount of Ams2 thus affects centromeric nucleosomal constituents. Ams2 is abundant in S phase and associates with chromatin, including the central centromeres through binding to GATA-core sequences. Ams2 is thus a cell cycle-regulated GATA factor that is required for centromere function.","authors":"Chen ES, Saitoh S, Yanagida M, Takahashi K","authors_abbrev":"Chen ES et al.","pubmed_publication_date":"Jan 2003","pubmed_entrez_date":"2003-01-22","publication_year":"2003","canto_session_key":"e6c2537c546c8b20","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-28 18:18:43","canto_approved_date":"2026-01-12 17:06:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-28 18:18:32","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.17","SPCC290.04","SPBC14C8.07c","SPBC1105.12","SPAC1687.20c","SPBC8D2.03c","SPBC409.04c","SPAC1834.03c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2018-02-28"},{"uniquename":"PMID:30212894","title":"Distinctive structural basis for DNA recognition by the fission yeast Zn2Cys6 transcription factor Pho7 and its role in phosphate homeostasis.","citation":"Nucleic Acids Res 2018 Nov 30;46(21):11262-11273","abstract":"Pho7, a member of the Zn2Cys6 family of fungal transcription factors, is the key transcriptional activator underlying fission yeast phosphate homeostasis, a physiological response to phosphate starvation in which the pho1, pho84 and tgp1 genes are upregulated. Here, we delineated a minimized 61-amino-acid Pho7 DNA-binding domain (DBD) and determined the 1.7 Å crystal structure of the DBD at its target site in the tgp1 promoter. Two distinctive features of the Pho7 DBD are: it binds DNA as a monomer, unlike most other fungal zinc-cluster factors that bind as homodimers; and it makes extensive interactions with its asymmetric target sequence over a 14-bp footprint that entails hydrogen bonding to 13 individual bases within, and remote from, the CGG triplet typically recognized by other Zn2Cys6 DBDs. Base pair substitutions at Pho7 sites in the tgp1 and pho1 promoters highlight the importance of the 5'-CGG triplet for Pho7 binding in vitro and Pho7-dependent gene expression in vivo. We identify several DBD amino acids at which alanine substitution effaced or attenuated the pho1 phosphate starvation response and concordantly reduced Pho7 binding to a pho1 promoter site.","doi":"10.1093/nar/gky827","authors":"Garg A, Goldgur Y, Schwer B, Shuman S","authors_abbrev":"Garg A et al.","pubmed_publication_date":"30 Nov 2018","pubmed_entrez_date":"2018-09-14","publication_year":"2018","canto_session_key":"a3a97d79735bef9a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Angad Garg","canto_first_approved_date":"2018-10-29 16:30:04","canto_approved_date":"2025-09-02 18:36:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-10 19:40:15","canto_added_date":"2018-09-15 00:15:04","annotation_curators":[{"name":"Angad Garg","community_curator":true,"annotation_count":45,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPBC27B12.11c","SPBC1271.09"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2018-10-29","pdb_entries":[{"pdb_id":"6e33","gene_chains":[{"gene_uniquename":"SPBC27B12.11c","chain":"A","position":"279-339"}],"title":"Crystal Structure of Pho7-DNA complex","entry_authors":"Garg A,Goldgur Y,Shuman S","entry_authors_abbrev":"Garg A et al.","reference_uniquename":"PMID:30212894","experimental_method":"X-ray","resolution":"1.705"}]},{"uniquename":"PMID:21422229","title":"Assembly and architecture of precursor nodes during fission yeast cytokinesis.","citation":"J Cell Biol 2011 Mar 21;192(6):1005-21","abstract":"The contractile ring is essential for cytokinesis in most fungal and animal cells. In fission yeast, cytokinesis nodes are precursors of the contractile ring and mark the future cleavage site. However, their assembly and architecture have not been well described. We found that nodes are assembled stoichiometrically in a hierarchical order with two modules linked by the positional marker anillin Mid1. Mid1 first recruits Cdc4 and IQGAP Rng2 to form module I. Rng2 subsequently recruits the myosin-II subunits Myo2 and Rlc1. Mid1 then independently recruits the F-BAR protein Cdc15 to form module II. Mid1, Rng2, Cdc4, and Cdc15 are stable node components that accumulate close to the plasma membrane. Both modules recruit the formin Cdc12 to nucleate actin filaments. Myo2 heads point into the cell interior, where they efficiently capture actin filaments to condense nodes into the contractile ring. Collectively, our work characterizing the assembly and architecture of precursor nodes defines important steps and molecular players for contractile ring assembly.","doi":"10.1083/jcb.201008171","authors":"Laporte D, Coffman VC, Lee IJ, Wu JQ","authors_abbrev":"Laporte D et al.","pubmed_publication_date":"21 Mar 2011","pubmed_entrez_date":"2011-03-23","publication_year":"2011","canto_session_key":"42e301a20297a109","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-02-21 14:15:37","canto_approved_date":"2025-05-02 16:11:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-06 15:59:01","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":64,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08","SPAC57A10.02","SPCC645.05c","SPAC1F5.04c","SPCC4B3.15","SPAC20G8.05c","SPAC926.03","SPAC4F8.13c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-02-21"},{"uniquename":"PMID:10467001","title":"Controlling septation in fission yeast: finding the middle, and timing it right.","citation":"Curr Genet 1999 Jul;35(6):571-84","abstract":"The fission yeast Schizosaccharomyces pombe provides a simple eukaryotic model for the study of cytokinesis. S. pombe cells are rod-shaped, grow mainly by elongation at their tips, and divide by binary fission after forming a centrally placed division septum. Analysis of mutants has begun to shed light upon how septum formation and cytokinesis are regulated both spatially and temporally. Some of the proteins involved in these events have been functionally conserved throughout eukaryotic evolution, suggesting that aspects of this control will be common to all eukaryotic cells.","authors":"Le Goff X, Utzig S, Simanis V","authors_abbrev":"Le Goff X et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-08-31","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7548846","title":"The control of septum formation and cytokinesis in fission yeast.","citation":"Semin Cell Biol 1995 Apr;6(2):79-87","abstract":"Our understanding of the control of cytokinesis is limited in comparison with our knowledge of the controls over the initiation of S phase or mitosis. Study of genetically tractable systems such as Schizosaccharomyces pombe are a useful way to address this problem, since mutants defective in regulation of cytokinesis have been identified. Cloning and analysis of the proteins they encode has begun to shed light upon how formation of the division septum is initiated and directed to the correct place in the cell. Some of these mutants may also be implicated in coordinating mitosis and cytokinesis.","authors":"Simanis V","authors_abbrev":"Simanis V","pubmed_publication_date":"Apr 1995","pubmed_entrez_date":"1995-04-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23872991","title":"Noncoding RNAs prevent spreading of a repressive histone mark.","citation":"Nat Struct Mol Biol 2013 Aug;20(8):994-1000","abstract":"Transcription of eukaryotic genomes is more widespread than was previously anticipated and results in the production of many non-protein-coding RNAs (ncRNAs) whose functional relevance is poorly understood. Here we demonstrate that ncRNAs can counteract the encroachment of heterochromatin into neighboring euchromatin. We have identified a long ncRNA (termed BORDERLINE) that prevents spreading of the HP1 protein Swi6 and histone H3 Lys9 methylation beyond the pericentromeric repeat region of Schizosaccharomyces pombe chromosome 1. BORDERLINE RNAs act in a sequence-independent but locus-dependent manner and are processed by Dicer into short RNAs referred to as brdrRNAs. In contrast to canonical centromeric short interfering RNAs, brdrRNAs are rarely loaded onto Argonaute. Our analyses reveal an unexpected regulatory activity of ncRNAs in demarcating an epigenetically distinct chromosomal domain that could also be operational in other eukaryotes.","doi":"10.1038/nsmb.2619","authors":"Keller C, Kulasegaran-Shylini R, Shimada Y, Hotz HR, Bühler M","authors_abbrev":"Keller C et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-07-23","publication_year":"2013","canto_session_key":"06e96fbe88cfa787","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.84","SPNCRNA.95"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:25074378","title":"The telomeric protein Pot1 from Schizosaccharomyces pombe binds ssDNA in two modes with differing 3' end availability.","citation":"Nucleic Acids Res 2014 Sep;42(15):9656-65","abstract":"Telomere protection and length regulation are important processes for aging, cancer and several other diseases. At the heart of these processes lies the single-stranded DNA (ssDNA)-binding protein Pot1, a component of the telomere maintenance complex shelterin, which is present in species ranging from fission yeast to humans. Pot1 contains a dual OB-fold DNA-binding domain (DBD) that fully confers its high affinity for telomeric ssDNA. Studies of S. pombe Pot1-DBD and its individual OB-fold domains revealed a complex non-additive behavior of the two OB-folds in the context of the complete Pot1 protein. This behavior includes the use of multiple distinct binding modes and an ability to form higher order complexes. Here we use NMR and biochemical techniques to investigate the structural features of the complete Pot1-DBD. These experiments reveal one binding mode characterized by only subtle alternations to the individual OB-fold subdomain structures, resulting in an inaccessible 3' end of the ssDNA. The second binding mode, which has equivalent affinity, interacts differently with the 3' end, rendering it available for interaction with other proteins. These findings suggest a structural switch that contributes to telomere end-protection and length regulation.","doi":"10.1093/nar/gku680","authors":"Dickey TH, Wuttke DS","authors_abbrev":"Dickey TH et al.","pubmed_publication_date":"Sep 2014","pubmed_entrez_date":"2014-07-31","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-08-01 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:42257267","title":"Methods to Study Mitochondrial Metabolism and Homeostasis in Fission Yeast.","citation":"Yeast 2026 Jun 08;","abstract":"","doi":"10.1002/yea.70030","authors":"Gómez-Armengol F, Hidalgo E, Vega M","authors_abbrev":"Gómez-Armengol F et al.","pubmed_publication_date":"08 Jun 2026","pubmed_entrez_date":"2026-06-08","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-06-08 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010910","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28241144","title":"Mediator structure and rearrangements required for holoenzyme formation.","citation":"Nature 2017 Apr 13;544(7649):196-201","abstract":"The conserved Mediator co-activator complex has an essential role in the regulation of RNA polymerase II transcription in all eukaryotes. Understanding the structure and interactions of Mediator is crucial for determining how the complex influences transcription initiation and conveys regulatory information to the basal transcription machinery. Here we present a 4.4 Å resolution cryo-electron microscopy map of Schizosaccharomyces pombe Mediator in which conserved Mediator subunits are individually resolved. The essential Med14 subunit works as a central backbone that connects the Mediator head, middle and tail modules. Comparison with a 7.8 Å resolution cryo-electron microscopy map of a Mediator-RNA polymerase II holoenzyme reveals that changes in the structure of Med14 facilitate a large-scale Mediator rearrangement that is essential for holoenzyme formation. Our study suggests that access to different conformations and crosstalk between structural elements are essential for the Mediator regulation mechanism, and could explain the capacity of the complex to integrate multiple regulatory signals.","doi":"10.1038/nature21393","authors":"Tsai KL, Yu X, Gopalan S, Chao TC, Zhang Y, Florens L, Washburn MP, Murakami K, Conaway RC, Conaway JW, Asturias FJ","authors_abbrev":"Tsai KL et al.","pubmed_publication_date":"13 Apr 2017","pubmed_entrez_date":"2017-02-28","publication_year":"2017","canto_session_key":"6034e5e0655e1575","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-01 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1A4.10c","SPAC1B3.12c","SPACUNK4.06c","SPBC337.14","SPBC14C8.12","SPBC31F10.04c","SPBC21.04","SPBC1604.10","SPAPYUG7.04c","SPCC1442.10c","SPAC17C9.05c","SPAC24C9.04","SPBC28F2.12","SPCC1020.04c","SPBC14F5.08","SPAC3A12.07","SPAC29A4.07","SPAC644.10","SPAC23C4.15","SPCP31B10.03c","SPAC1002.15c","SPBC19C2.03","SPAC23G3.01","SPAC17G8.05","SPAC5D6.05"],"gene_count":25,"ltp_gene_count":25,"pdb_entries":[{"pdb_id":"5u0p","gene_chains":[{"gene_uniquename":"SPAC24C9.04","chain":"I","position":"1-121"},{"gene_uniquename":"SPAC29A4.07","chain":"V","position":"1-136"},{"gene_uniquename":"SPAC5D6.05","chain":"R","position":"1-207"},{"gene_uniquename":"SPBC14F5.08","chain":"G","position":"1-376"},{"gene_uniquename":"SPBC1604.10","chain":"U","position":"1-138"},{"gene_uniquename":"SPBC21.04","chain":"H","position":"1-200"},{"gene_uniquename":"SPBC31F10.04c","chain":"Q","position":"1-545"},{"gene_uniquename":"SPAC17G8.05","chain":"T","position":"1-193"},{"gene_uniquename":"SPAC17C9.05c","chain":"2","position":"1-273"},{"gene_uniquename":"SPAC644.10","chain":"K","position":"1-112"},{"gene_uniquename":"SPBC1A4.10c","chain":"N","position":"1-879"},{"gene_uniquename":"SPAC1002.15c","chain":"F","position":"1-216"},{"gene_uniquename":"SPCP31B10.03c","chain":"3","position":"1-139"}],"title":"Cryo-EM structure of the transcriptional Mediator","entry_authors":"Tsai K-L,Yu X,Gopalan S,Chao T-C,Zhang Y,Florens L,Washburn MP,Murakami K,Conaway RC,Conaway JW,Asturias F","entry_authors_abbrev":"Tsai K-L et al.","reference_uniquename":"PMID:28241144","experimental_method":"EM","resolution":"4.4"},{"pdb_id":"5u0s","gene_chains":[{"gene_uniquename":"SPAC1B3.12c","chain":"j","position":"1-71"},{"gene_uniquename":"SPAC24C9.04","chain":"I","position":"1-121"},{"gene_uniquename":"SPAC29A4.07","chain":"V","position":"1-136"},{"gene_uniquename":"SPAC5D6.05","chain":"R","position":"1-207"},{"gene_uniquename":"SPACUNK4.06c","chain":"g","position":"1-172"},{"gene_uniquename":"SPBC14F5.08","chain":"G","position":"1-376"},{"gene_uniquename":"SPAPYUG7.04c","chain":"i","position":"1-113"},{"gene_uniquename":"SPBC337.14","chain":"d","position":"1-135"},{"gene_uniquename":"SPBC1604.10","chain":"U","position":"1-138"},{"gene_uniquename":"SPBC21.04","chain":"H","position":"1-200"},{"gene_uniquename":"SPBC28F2.12","chain":"a","position":"1-1752"},{"gene_uniquename":"SPCC1020.04c","chain":"f","position":"1-142"},{"gene_uniquename":"SPCC1442.10c","chain":"c","position":"1-297"},{"gene_uniquename":"SPBC19C2.03","chain":"l","position":"1-63"},{"gene_uniquename":"SPAC3A12.07","chain":"k","position":"1-123"},{"gene_uniquename":"SPBC31F10.04c","chain":"Q","position":"1-545"},{"gene_uniquename":"SPAC23G3.01","chain":"b","position":"1-1210"},{"gene_uniquename":"SPAC23C4.15","chain":"e","position":"1-210"},{"gene_uniquename":"SPAC17G8.05","chain":"T","position":"1-193"},{"gene_uniquename":"SPAC17C9.05c","chain":"2","position":"1-273"},{"gene_uniquename":"SPBC14C8.12","chain":"h","position":"1-125"},{"gene_uniquename":"SPAC644.10","chain":"K","position":"1-112"},{"gene_uniquename":"SPBC1A4.10c","chain":"N","position":"1-879"},{"gene_uniquename":"SPAC1002.15c","chain":"F","position":"1-216"},{"gene_uniquename":"SPCP31B10.03c","chain":"3","position":"1-139"}],"title":"Cryo-EM structure of the Mediator-RNAPII complex","entry_authors":"Tsai K-L,Yu X,Gopalan S,Chao T-C,Zhang Y,Florens L,Washburn MP,Murakami K,Conaway RC,Conaway JW,Asturias F","entry_authors_abbrev":"Tsai K-L et al.","reference_uniquename":"PMID:28241144","experimental_method":"EM","resolution":"7.8"}]},{"uniquename":"PMID:34660592","title":"Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.","citation":"Front Cell Dev Biol 2021;9:735678","abstract":"Iron-sulfur (Fe/S) clusters (ISCs) are redox-active protein cofactors that their synthesis, transfer, and insertion into target proteins require many components. Mitochondrial ISC assembly is the foundation of all cellular ISCs in eukaryotic cells. The mitochondrial ISC cooperates with the cytosolic Fe/S protein assembly (CIA) systems to accomplish the cytosolic and nuclear Fe/S clusters maturation. ISCs are needed for diverse cellular functions, including nitrogen fixation, oxidative phosphorylation, mitochondrial respiratory pathways, and ribosome assembly. Recent research advances have confirmed the existence of different ISCs in enzymes that regulate DNA metabolism, including helicases, nucleases, primases, DNA polymerases, and glycosylases. Here we outline the synthesis of mitochondrial, cytosolic and nuclear ISCs and highlight their functions in DNA metabolism.","doi":"10.3389/fcell.2021.735678","authors":"Shi R, Hou W, Wang ZQ, Xu X","authors_abbrev":"Shi R et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-10-18","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC21E11.07","SPAC227.13c","SPAC144.16","SPAC637.08","SPBC13G1.06c","SPAC4H3.09","SPAC22E12.10c","SPBC21D10.11c","SPCC1183.03c","SPBC1709.19c","SPBC3B9.17","SPAC806.02c","SPBC3B8.01c","SPCC645.03c"],"gene_count":14,"ltp_gene_count":0},{"uniquename":"PMID:11526017","title":"Characterization of Schizosaccharomyces pombe malate permease by expression in Saccharomyces cerevisiae.","citation":"Appl Environ Microbiol 2001 Sep;67(9):4144-51","abstract":"In Saccharomyces cerevisiae, L-malic acid transport is not carrier mediated and is limited to slow, simple diffusion of the undissociated acid. Expression in S. cerevisiae of the MAE1 gene, encoding Schizosaccharomyces pombe malate permease, markedly increased L-malic acid uptake in this yeast. In this strain, at pH 3.5 (encountered in industrial processes), L-malic acid uptake involves Mae1p-mediated transport of the monoanionic form of the acid (apparent kinetic parameters: Vmax = 8.7 nmol/mg/min; Km = 1.6 mM) and some simple diffusion of the undissociated L-malic acid (Kd = 0.057 min(-1)). As total L-malic acid transport involved only low levels of diffusion, the Mae1p permease was further characterized in the recombinant strain. L-Malic acid transport was reversible and accumulative and depended on both the transmembrane gradient of the monoanionic acid form and the DeltapH component of the proton motive force. Dicarboxylic acids with stearic occupation closely related to L-malic acid, such as maleic, oxaloacetic, malonic, succinic and fumaric acids, inhibited L-malic acid uptake, suggesting that these compounds use the same carrier. We found that increasing external pH directly inhibited malate uptake, resulting in a lower initial rate of uptake and a lower level of substrate accumulation. In S. pombe, proton movements, as shown by internal acidification, accompanied malate uptake, consistent with the proton/dicarboxylate mechanism previously proposed. Surprisingly, no proton fluxes were observed during Mae1p-mediated L-malic acid import in S. cerevisiae, and intracellular pH remained constant. This suggests that, in S. cerevisiae, either there is a proton counterflow or the Mae1p permease functions differently from a proton/dicarboxylate symport.","authors":"Camarasa C, Bidard F, Bony M, Barre P, Dequin S","authors_abbrev":"Camarasa C et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-08-30","publication_year":"2001","canto_session_key":"39a9ab38c73c2829","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-08-06 16:36:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 16:36:02","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB8E5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-06"},{"uniquename":"PMID:11473261","title":"Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones.","citation":"Nat Struct Biol 2001 Aug;8(8):701-4","abstract":"The translationally controlled tumor-associated proteins (TCTPs) are a highly conserved and abundantly expressed family of eukaryotic proteins that are implicated in both cell growth and the human acute allergic response but whose intracellular biochemical function has remained elusive. We report here the solution structure of the TCTP from Schizosaccharomyces pombe, which, on the basis of sequence homology, defines the fold of the entire family. We show that TCTPs form a structural superfamily with the Mss4/Dss4 family of proteins, which bind to the GDP/GTP free form of Rab proteins (members of the Ras superfamily) and have been termed guanine nucleotide-free chaperones (GFCs). Mss4 also acts as a relatively inefficient guanine nucleotide exchange factor (GEF). We further show that the Rab protein binding site on Mss4 coincides with the region of highest sequence conservation in the TCTP family. This is the first link to any other family of proteins that has been established for the TCTP family and suggests the presence of a GFC/GEF at extremely high abundance in eukaryotic cells.","authors":"Thaw P, Baxter NJ, Hounslow AM, Price C, Waltho JP, Craven CJ","authors_abbrev":"Thaw P et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-07-27","publication_year":"2001","canto_session_key":"83860afc6d9127b5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2022-09-18 17:31:15","canto_approved_date":"2022-11-04 18:52:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-18 17:31:08","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F12.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-09-18","pdb_entries":[{"pdb_id":"1h6q","gene_chains":[{"gene_uniquename":"SPAC1F12.02c","chain":"A","position":"1-168"}],"title":"Translationally Controlled Tumor-associated Protein p23fyp from Schizosaccharomyces pombe","entry_authors":"Thaw P,Baxter NJ,Sedelnikova SE,Price C,Waltho JP,Craven CJ","entry_authors_abbrev":"Thaw P et al.","reference_uniquename":"PMID:11473261","experimental_method":"NMR","resolution":""},{"pdb_id":"1h7y","gene_chains":[{"gene_uniquename":"SPAC1F12.02c","chain":"A","position":"1-168"}],"title":"Translationally Controlled Tumor-associated Protein p23fyp from Schizosaccharomyces pombe","entry_authors":"Thaw P,Baxter NJ,Sedelnikova SE,Price C,Waltho JP,Craven CJ","entry_authors_abbrev":"Thaw P et al.","reference_uniquename":"PMID:11473261","experimental_method":"NMR","resolution":""}]},{"uniquename":"EMBL:AU012082","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8078473","title":"The ste13+ gene encoding a putative RNA helicase is essential for nitrogen starvation-induced G1 arrest and initiation of sexual development in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1994 Sep 01;244(5):456-64","abstract":"When the fission yeast Schizosaccharomyces pombe is starved for nitrogen, the cells are arrested in the G1 phase, enter the G0 phase and initiate sexual development. The ste13 mutant, however, fails to undergo a G1 arrest when starved for nitrogen and since this mutant phenotype is not suppressed by a mutation in adenylyl cyclase (cyr1), it would appear that ste13+ either acts independently of the decrease in the cellular cAMP level induced by starvation for nitrogen, or functions downstream of this controlling event. We have used functional complementation to clone the ste13+ gene from an S. pombe genomic library and show that its disruption is not lethal, indicating that, while the gene is required for sexual development, it is not essential for cell growth. Nucleotide sequencing predicts that ste13+ should encode a protein of 485 amino acids in which the consensus motifs of ATP-dependent RNA helicases of the DEAD box family are completely conserved. Point mutations introduced into these consensus motifs abolished the ste13+ functions. The predicted Ste13 protein is 72% identical to the Drosophila melanogaster Me31B protein over a stretch of 391 amino acids. ME31B is a developmentally regulated gene that is expressed preferentially in the female germline and may be required for oogenesis. Expression of ME31B cDNA in S. pombe suppresses the ste13 mutation. These two evolutionarily conserved genes encoding putative RNA helicases may play a pivotal role in sexual development.","authors":"Maekawa H, Nakagawa T, Uno Y, Kitamura K, Shimoda C","authors_abbrev":"Maekawa H et al.","pubmed_publication_date":"01 Sep 1994","pubmed_entrez_date":"1994-09-01","publication_year":"1994","canto_session_key":"e8aedfc4412e4268","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-05-14 10:02:04","canto_approved_date":"2019-06-14 09:13:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-08 15:02:08","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-14"},{"uniquename":"PMID:19243129","title":"Use of a Schizosaccharomyces pombe mutant to reduce the content in gluconic acid of must obtained from rotten grapes.","citation":"J Agric Food Chem 2009 Mar 25;57(6):2368-77","abstract":"Schizosaccharomyces pombe YGS-5 and Saccharomyces cerevisiae G1 strains were used in order to develop an effective method for reducing the gluconic acid content of musts without altering the development of alcoholic fermentation or detracting from quality in the resulting wines. The best results in synthetic media were obtained by using a temperature of 24 degrees C and a sulfur dioxide rate below 100 mg/L under semiaerobic conditions. Sequential inoculation of the musts with YGS-5 first and fermentative G1 yeasts then reduced their gluconic acid content by 85% within 43 h; by contrast, simultaneous inoculation with YGS-5 and G1 provided a reduction of only 40%. The wines with the best sensory and analytical properties were obtained by sequentially inoculating the musts with YGS-5 and, once gluconic acid was removed, G1. The wine obtained by sequential inoculation without removing YGS-5 was that exhibiting the highest odorant activity value (OAV) for the volatile compounds in the floral odor series. A protocol for treating musts containing gluconic acid was developed and tested at the pilot plant scale. The treatment reduced the gluconic acid content by 70% within 46 h with no adverse effect on the analytical or sensory quality of the resulting wines.","doi":"10.1021/jf803479r","authors":"Peinado RA, Maestre O, Mauricio JC, Moreno JJ","authors_abbrev":"Peinado RA et al.","pubmed_publication_date":"25 Mar 2009","pubmed_entrez_date":"2009-02-27","publication_year":"2009","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6828164","title":"Control of timing of cell cycle events in fission yeast by the wee 1+ gene.","citation":"Nature 1983 Mar 10;302(5904):153-5","abstract":"","authors":"Fantes PA","authors_abbrev":"Fantes PA","pubmed_publication_date":"10 Mar 1983","pubmed_entrez_date":"1983-03-10","publication_year":"1983","canto_session_key":"ef61ac1ac91c951e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-12-05 15:32:53","canto_approved_date":"2026-01-30 12:13:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-06 11:09:15","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":10,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC336.04","SPAC27E2.05","SPCC18B5.03","SPBC11B10.09","SPBC1734.02c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-12-05"},{"uniquename":"PMID:15767681","title":"Schizosaccharomyces pombe Swi1, Swi3, and Hsk1 are components of a novel S-phase response pathway to alkylation damage.","citation":"Mol Cell Biol 2005 Apr;25(7):2770-84","abstract":"The Swi1 and Swi3 proteins are required for mat1 imprinting and mating-type switching in Schizosaccharomyces pombe, where they mediate a pause of leading-strand replication in response to a lagging-strand signal. In addition, Swi1 has been demonstrated to be involved in the checkpoint response to stalled replication forks, as was described for the Saccharomyces cerevisiae homologue Tof1. This study addresses the roles of Swi1 and Swi3 during a replication process perturbed by the presence of template bases alkylated by methyl methanesulfonate (MMS). Both the swi1 and swi3 mutations have additive effects on MMS sensitivity and on the MMS-induced damage checkpoint response when combined with chk1 and cds1, but they are nonadditive with hsk1. Cells with swi1, swi3, or hsk1 mutations are also defective in slowing progression through S phase in response to MMS damage. Moreover, swi1 and swi3 strains show increased levels of genomic instability even in the absence of exogenously induced DNA damage. Chromosome fragmentation, increased levels of single-stranded DNA, increased recombination, and instability of replication forks stalled in the presence of hydroxyurea are observed, consistent with the possibility that the replication process is affected in these mutants. In conclusion, Swi1, Swi3, and Hsk1 act in a novel S-phase checkpoint pathway that contributes to replication fork maintenance and to survival of alkylation damage.","authors":"Sommariva E, Pellny TK, Karahan N, Kumar S, Huberman JA, Dalgaard JZ","authors_abbrev":"Sommariva E et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-03-16","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC30D10.04","SPCC1259.13","SPCC550.13","SPCC18B5.11c","SPBC216.06c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:40112985","title":"Balance of polo-like kinase Plo1 and monopolar attachment protein 1 (Moa1) regulates fission yeast meiosis.","citation":"Int J Biol Macromol 2025 Mar 18;307(Pt 4):142189","abstract":"During meiosis, diploid germ cells undergo two successive rounds of chromosome segregation requiring key changes that sister chromatids co-orient in meiosis I and bi-orient in meiosis II. The kinetochore protein MEIKIN/Moa1 is restricted to meiosis I, has the function to properly co-orient sister kinetochores and maintain pericentrometic cohesion. However, the mechanisms governing the Moa1 activity throughout meiosis remain elusive in Schizosaccharomyces pombe. Here, we demonstrate that fission yeast Moa1 is degraded by the APC/C at anaphase I and blocking Moa1 degradation has no effect on cohesin protection and chromosome segregation during meiosis. Blocking Moa1 degradation can be prevented by the elimination of kinetochore Plo1. Conversely, the removal of Plo1 from the kinetochore, which leads to chromosome mis-segregation, can be reversed by maintaining kinetochore Moa1 levels. Therefore, we have observed a feedback relationship between reduced Plo1 enrichment at kinetochores and inhibited Moa1 degradation.","doi":"10.1016/j.ijbiomac.2025.142189","authors":"Zhou KD, Wang YJ, Ma PY, Fang SY, Ma W","authors_abbrev":"Zhou KD et al.","pubmed_publication_date":"18 Mar 2025","pubmed_entrez_date":"2025-03-20","publication_year":"2025","canto_session_key":"aa16114bf87c5477","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-03-22 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR38645","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YJR056C","SPAC6B12.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25651869","title":"Chemical genomics approach to identify genes associated with sensitivity to rapamycin in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Cells 2015 Apr;20(4):292-309","abstract":"Rapamycin and its derivatives have now emerged as an attractive therapeutic strategy with both immunosuppressant and antitumor properties. In addition, rapamycin has been proposed as a calorie restriction mimetic to extend the life span of various organisms. The fission yeast Schizosaccharomyces pombe (S. pombe) serves as a valuable genetic model system to study the mechanism(s) of drug action as well as to determine genetic contexts associated with drug sensitivity or resistance. Here, we identified genes that when deleted modulate the rapamycin-sensitive strains in S. pombe. We carried out a chemical genomics screen for rapamycin-sensitive mutants using the genome-deletion library which covers 95.3% of all nonessential fission yeast genes and confirmed 59 genes to be rapamycin sensitive. Gene Ontology (GO) enrichment analysis showed that strains sensitive to rapamycin are highly enriched in processes regulating tRNA modification and mitochondria as well as other ontologies, including cellular metabolic process, chromatin organization, cell cycle, signaling, translation, transport and other cellular processes. Analysis also showed that components of the Elongator complex are overrepresented in the sensitive strains. Here, the data obtained will provide valuable information for speculation on the actions of rapamycin as well as on TORC signaling, thereby presenting a strategy to enhance sensitivity to rapamycin.","doi":"10.1111/gtc.12223","authors":"Doi A, Fujimoto A, Sato S, Uno T, Kanda Y, Asami K, Tanaka Y, Kita A, Satoh R, Sugiura R","authors_abbrev":"Doi A et al.","pubmed_publication_date":"Apr 2015","pubmed_entrez_date":"2015-02-06","publication_year":"2015","canto_session_key":"ac620ded0e797706","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-23 10:34:56","canto_approved_date":"2026-01-23 08:50:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-23 10:34:48","canto_added_date":"2015-02-07 01:15:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":94,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_25651869_phaf.tsv"}],"genes":["SPBC16G5.11c","SPBC36.07","SPAC30C2.04","SPCC1919.10c","SPAC23H3.13c","SPBC1778.05c","SPBC660.11","SPBC3H7.03c","SPAC57A10.10c","SPBC2G5.03","SPBC2D10.18","SPCC188.08c","SPBC146.12","SPAC513.03","SPAC4C5.02c","SPCC16C4.11","SPBC25H2.16c","SPAC26F1.04c","SPCC1259.07","SPCC1902.02","SPAC23H3.09c","SPBC24C6.11","SPBC106.04","SPAC22E12.04","SPBC31F10.15c","SPAC23H4.12","SPAC323.01c","SPBC29A10.01","SPBP8B7.09c","SPAC2G11.03c","SPAC29A4.20","SPAC821.11","SPBC1105.04c","SPAC30.02c","SPCC1393.13","SPBC216.07c","SPCC11E10.06c","SPAC27E2.11c","SPBPB2B2.01","SPAC15A10.06","SPBC725.10","SPBC577.15c","SPBC4B4.07c","SPAC29B12.08","SPAC824.02","SPCC794.12c","SPAC664.03","SPBC106.07c","SPAC4F10.04","SPAC637.07","SPAC25B8.05","SPBC337.15c","SPBC3B8.02","SPAC1142.05","SPBC3H7.10","SPCC4B3.10c","SPCC16C4.10","SPAC1D4.06c","SPBC1271.12","SPAC20G4.07c"],"gene_count":60,"ltp_gene_count":14,"approved_date":"2015-02-23"},{"uniquename":"PMID:21849474","title":"Spatial control of Cdc42 activation determines cell width in fission yeast.","citation":"Mol Biol Cell 2011 Oct;22(20):3801-11","abstract":"The fission yeast Schizosaccharomyces pombe is a rod-shaped cell that grows by linear extension at the cell tips, with a nearly constant width throughout the cell cycle. This simple geometry makes it an ideal system for studying the control of cellular dimensions. In this study, we carried out a near-genome-wide screen for mutants wider than wild-type cells. We found 11 deletion mutants that were wider; seven of the deleted genes are implicated in the control of the small GTPase Cdc42, including the Cdc42 guanine nucleotide exchange factor (GEF) Scd1 and the Cdc42 GTPase-activating protein (GAP) Rga4. Deletions of rga4 and scd1 had additive effects on cell width, and the proteins localized independently of one another, with Rga4 located at the cell sides and Scd1 at the cell tips. Activated Cdc42 localization is altered in rga4Δ, scd1Δ, and scd2Δ mutants. Delocalization and ectopic retargeting experiments showed that the localizations of Rga4 and Scd1 are crucial for their roles in determining cell width. We propose that the GAP Rga4 and the GEF Scd1 establish a gradient of activated Cdc42 within the cellular tip plasma membrane, and it is this gradient that determines cell growth-zone size and normal cell width.","doi":"10.1091/mbc.E11-01-0057","authors":"Kelly FD, Nurse P","authors_abbrev":"Kelly FD et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-08-19","publication_year":"2011","canto_session_key":"c480fb02b530ca54","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-07-18 10:02:49","canto_approved_date":"2025-03-17 15:05:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-17 13:20:56","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":62,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPAC17G6.04c","SPBC1604.14c","SPAC22H10.07","SPBC28E12.03","SPCC1672.06c","SPAC13G6.10c","SPCC1919.10c","SPAC110.03","SPAC24H6.09","SPBC1A4.05","SPBC725.02","SPAC16E8.09","SPBC21.05c","SPBC336.03"],"gene_count":15,"ltp_gene_count":14,"approved_date":"2018-07-18"},{"uniquename":"PMID:14576334","title":"Efficient labeling of fission yeast Schizosaccharomyces pombe with thymidine and BUdR.","citation":"Nucleic Acids Res 2003 Nov 01;31(21):e134","abstract":"In this paper we report the construction of a Schizosaccharomyces pombe strain that facilitates analysis of replicating DNA. The strain co-expresses the Herpes simplex virus thymidine kinase gene (hsv-tk) and a human equilibrative nucleoside transporter (hENT1). The double integrant efficiently incorporates 3H-thymidine into nuclear DNA as monitored by scintillation counting. These strains also incorporate the thymidine analog Bromodeoxy uridine (BUdR) into newly replicated DNA, which can be detected by immunofluorescence and flow cytometry. This strain provides a valuable tool for direct study of DNA replication in S.pombe.","authors":"Hodson JA, Bailis JM, Forsburg SL","authors_abbrev":"Hodson JA et al.","pubmed_publication_date":"01 Nov 2003","pubmed_entrez_date":"2003-10-25","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11238404","title":"Functional redundancies, distinct localizations and interactions among three fission yeast homologs of centromere protein-B.","citation":"Genetics 2001 Mar;157(3):1191-203","abstract":"Several members of protein families that are conserved in higher eukaryotes are known to play a role in centromere function in the fission yeast Schizosaccharomyces pombe, including two homologs of the mammalian centromere protein CENP-B, Abp1p and Cbh1p. Here we characterize a third S. pombe CENP-B homolog, Cbh2p (CENP-B homolog 2). cbh2Delta strains exhibited a modest elevation in minichromosome loss, similar to cbh1Delta or abp1Delta strains. cbh2Delta cbh1Delta strains showed little difference in growth or minichromosome loss rate when compared to single deletion strains. In contrast, cbh2Delta abp1Delta strains displayed dramatic morphological and chromosome segregation defects, as well as enhancement of the slow-growth phenotype of abp1Delta strains, indicating partial functional redundancy between these proteins. Both cbh2Delta abp1Delta and cbh1Delta abp1Delta strains also showed strongly enhanced sensitivity to a microtubule-destabilizing drug, consistent with a mitotic function for these proteins. Cbh2p was localized to the central core and core-associated repeat regions of centromeric heterochromatin, but not at several other centromeric and arm locations tested. Thus, like its mammalian counterpart, Cbh2p appeared to be localized exclusively to a portion of centromeric heterochromatin. In contrast, Abp1p was detected in both centromeric heterochromatin and in chromatin at two of three replication origins tested. Cbh2p and Abp1p homodimerized in the budding yeast two-hybrid assay, but did not interact with each other. These results suggest that indirect cooperation between different CENP-B-like DNA binding proteins with partially overlapping chromatin distributions helps to establish a functional centromere.","authors":"Irelan JT, Gutkin GI, Clarke L","authors_abbrev":"Irelan JT et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-03-10","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14F5.12c","SPBC1105.04c","SPAC9E9.10c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:29214404","title":"The 19S proteasome regulates subtelomere silencing and facultative heterochromatin formation in fission yeast.","citation":"Curr Genet 2018 Jun;64(3):741-752","abstract":"Accumulating evidence shows that non-proteolytic functions of the proteasome are as crucial as its well-known proteolytic function in regulating cellular activities. In our recent work, we showed that the 19S proteasome mediates the heterochromatin spreading of centromeric heterochromatin in non-proteolytic manner. However, the involvement of the proteasome in other heterochromatin regions remained largely unknown. In the present study, we investigated the non-proteolytic role of the 19S proteasome in subtelomere and facultative heterochromatin regions. Using the non-proteolytic mutant, rpt4-1, we show that the 19S proteasome is involved in regulating subtelomere silencing and facultative heterochromatin formation in fission yeast. In addition to this proteasome-related regulation, we also observed a distinct pathway that regulates subtelomere silencing and facultative heterochromatin formation through the Paf1 complex subunit, Leo1. Our comparison of the two pathways revealed a new group of heterochromatin domains that are regulated exclusively by the proteasome pathway. Taken together, our findings reveal that the proteasome is involved in the global regulation of facultative and constitutive heterochromatin.","doi":"10.1007/s00294-017-0792-6","authors":"Seo HD, Kwon CS, Lee D","authors_abbrev":"Seo HD et al.","pubmed_publication_date":"Jun 2018","pubmed_entrez_date":"2017-12-08","publication_year":"2018","canto_session_key":"1dd1a72244ca3e99","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hogyu David Seo","canto_first_approved_date":"2018-02-15 16:16:48","canto_approved_date":"2020-04-09 15:23:00","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-02-05 04:35:51","canto_added_date":"2017-12-09 01:15:56","annotation_curators":[{"name":"Hogyu David Seo","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":28,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.03c","SPAC9E9.09c","SPCC548.06c","SPBC428.08c","SPBC1D7.02c","SPAC27D7.03c","SPAC212.11","SPAC23C11.09","SPAC29E6.08","SPCC1682.16","SPBC13E7.08c","SPCC736.11","SPCC188.13c","SPBC1685.13","SPAC1782.06c","SPBC713.12","SPNCRNA.133","SPCC1795.11","SPAC144.02","SPAC664.01c","SPBC4B4.08","SPAC13G7.13c","SPCC191.02c","SPAPB15E9.01c","SPCC13B11.04c","SPBPB21E7.09","SPAC1834.05","SPNCRNA.1169","SPCC622.16c","SPBC1539.07c","SPBCPT2R1.08c","SPCC1742.01"],"gene_count":32,"ltp_gene_count":6,"approved_date":"2018-02-15"},{"uniquename":"PMID:16874521","title":"Joint regulation of the nmt1 promoter and sporulation by Thi1 and Thi5 in Schizosaccharomyces pombe.","citation":"Curr Genet 2006 Oct;50(4):269-79","abstract":"nmt1 in fission yeast is essential for thiamine biosynthesis and is regulated by the thi1 transcription factor. The thiamine-repressible nmt1 promoter is the most widely used promoter construct for gene expression studies in fission yeast. We show that in addition to thi1, thi5 also regulates the nmt1 promoter and its expression is undetectable in a thi1 thi5 double deletion. Thi5 over-expression relieves the repression of nmt1 by thiamine and rescues the thiamine auxotrophy in thi1 deletions. Thi5 may also work to regulate Thi1 activity. Sporulation defects and decreased conjugation were observed in a thi1 disruption; deleting thi5 did not affect conjugation, but resulted in decreased sensitivity to exogenous thiamine. The thi5 deletion is epistatic to thi1 with respect to the failure of the thi1 disruption to produce spores. Thi5 negatively regulates some stages of meiosis. Over-expressing Thi1 from its native promoter results in increased thiamine-insensitive conjugation in all genetic backgrounds, suggesting that Thi1 positively regulates meiosis and that thiamine inhibition of conjugation is a result of Thi1 repression. Thi5 and Thi1 work in the same pathway to positively regulate nmt1 promoter activity. In conjugation, Thi5 and Thi1 operate in different pathways to transcribe antagonists involved in the completion of meiosis.","authors":"McQuire TA, Young PG","authors_abbrev":"McQuire TA et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-07-29","publication_year":"2006","canto_session_key":"c0b99491ed09bf31","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-28 18:26:56","canto_approved_date":"2024-01-05 09:39:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-08 11:41:02","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1486.10","SPCC1223.02","SPBP8B7.30c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2018-01-28"},{"uniquename":"PMID:4029277","title":"Changes in phosphoprotein pattern in Schizosaccharomyces pombe.","citation":"Exp Cell Res 1985 Aug;159(2):495-509","abstract":"A variety of evidence suggests that protein phosphorylation (pp) may be important in cell-cycle control. Phosphorylated proteins from S. pombe have been examined for phosphorylation changes under several conditions: known triggers of the division control (low nitrogen, low phosphate), cell size mutants (WEE1 and CDC2 alleles) and cell cycle mutants (CDC2, CDC10, CDC17, CDC25 alleles). Three major phosphorylated proteins (pp38, pp45 and pp54) showed the greatest response to nutritional shifts. The changes in the phosphorylated states of these proteins correlated with growth rate. Some phosphorylations (e.g. pp53) occurred transiently following a stimulus to cell division suggesting a possible involvement with the division mechanism. An allele-specific alteration of charge was noted for pp45 suggesting that this protein is the product of the CDC2 gene. The wee1-6 phosphoprotein pattern is similar to wild-type indicating that this mutant cell line accurately senses its nutritional environment and that the mutation likely affects the transfer of this information to the division control. Cells blocked by various temperature-sensitive cell cycle mutants did not show an alteration of phosphoprotein pattern.","authors":"Querengesser LD, Young PG","authors_abbrev":"Querengesser LD et al.","pubmed_publication_date":"Aug 1985","pubmed_entrez_date":"1985-08-01","publication_year":"1985","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14669918","title":"Hierarchical chromatin structure of Schizosaccharomyces pombe revealed by atomic force microscopy.","citation":"Curr Microbiol 2003 Nov;47(5):404-7","abstract":"Many structural studies on higher eukaryotic chromatin have been carried out, but chromatin structure in fungi remains unclear. Schizosaccharomyces pombe has been used for investigations of chromosome function; however, the structural details of S. pombe chromatin have not been clarified owing to its small nucleus. We used atomic force microscopy for nano-scale imaging of chromatin isolated from S. pombe. Topographic images indicated that nuclear chromatin contained at least three hierarchical structures: large-scale chromatin fibers, spherical domains in the fibers, and nodules in the domains. The average diameters of the domain and the nodule were 363 +/- 85.2 nm and 46.2 +/- 9.30 nm. Each structure comprising the hierarchy was similar to higher eukaryotic chromatin thus far observed, despite definite differences in chromatin organization at the nucleosomal level. The presence of histone H1 suggested that there might be an alternative to compensate for histone H1 lacking in S. pombe.","authors":"Kobori T, Yoshino T, Sugiyama S, Ohtani T","authors_abbrev":"Kobori T et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-12-13","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19948483","title":"Ase1/Prc1-dependent spindle elongation corrects merotely during anaphase in fission yeast.","citation":"J Cell Biol 2009 Nov 02;187(3):399-412","abstract":"Faithful segregation of sister chromatids requires the attachment of each kinetochore (Kt) to microtubules (MTs) that extend from opposite spindle poles. Merotelic Kt orientation is a Kt-MT misattachment in which a single Kt binds MTs from both spindle poles rather than just one. Genetic induction of merotelic Kt attachment during anaphase in fission yeast resulted in intra-Kt stretching followed by either correction or Kt disruption. Laser ablation of spindle MTs revealed that intra-Kt stretching and merotelic correction were dependent on MT forces. The presence of multiple merotelic chromosomes linearly antagonized the spindle elongation rate, and this phenomenon could be solved numerically using a simple force balance model. Based on the predictions of our mechanical model, we provide in vivo evidence that correction of merotelic attachment in anaphase is tension dependent and requires an Ase1/Prc1-dependent mechanism that prevents spindle collapse and thus asymmetric division and/or the appearance of the cut phenotype.","doi":"10.1083/jcb.200902093","authors":"Courtheoux T, Gay G, Gachet Y, Tournier S","authors_abbrev":"Courtheoux T et al.","pubmed_publication_date":"02 Nov 2009","pubmed_entrez_date":"2009-12-02","publication_year":"2009","canto_session_key":"deaffb81d6a5dd3d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-08-25 09:57:39","canto_approved_date":"2022-08-25 09:57:39","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-08-25 09:57:12","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":6,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPAPB1A10.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-08-25"},{"uniquename":"PMID:21423720","title":"Identification of a novel type of spacer element required for imprinting in fission yeast.","citation":"PLoS Genet 2011 Mar;7(3):e1001328","abstract":"Asymmetrical segregation of differentiated sister chromatids is thought to be important for cellular differentiation in higher eukaryotes. Similarly, in fission yeast, cellular differentiation involves the asymmetrical segregation of a chromosomal imprint. This imprint has been shown to consist of two ribonucleotides that are incorporated into the DNA during lagging-strand synthesis in response to a replication pause, but the underlying mechanism remains unknown. Here we present key novel discoveries important for unravelling this process. Our data show that cis-acting sequences within the mat1 cassette mediate pausing of replication forks at the proximity of the imprinting site, and the results suggest that this pause dictates specific priming at the position of imprinting in a sequence-independent manner. Also, we identify a novel type of cis-acting spacer region important for the imprinting process that affects where subsequent primers are put down after the replication fork is released from the pause. Thus, our data suggest that the imprint is formed by ligation of a not-fully-processed Okazaki fragment to the subsequent fragment. The presented work addresses how differentiated sister chromatids are established during DNA replication through the involvement of replication barriers.","doi":"10.1371/journal.pgen.1001328","authors":"Sayrac S, Vengrova S, Godfrey EL, Dalgaard JZ","authors_abbrev":"Sayrac S et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-03-23","publication_year":"2011","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14989084","title":"Electroporation of Schizosaccharomyces pombe by hyperosmotic post-pulse incubation.","citation":"Biotechniques 2004 Feb;36(2):218-20","abstract":"","authors":"Suga M, Kusanagi I, Hatakeyama T","authors_abbrev":"Suga M et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2004-03-03","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18328707","title":"Pom1 DYRK regulates localization of the Rga4 GAP to ensure bipolar activation of Cdc42 in fission yeast.","citation":"Curr Biol 2008 Mar 11;18(5):322-30","abstract":"In the fission yeast Schizosaccharomyces pombe, cell growth takes place exclusively at both ends of the cylindrical cell. During this highly polarized growth, microtubules are responsible for the placement of the cell-end marker proteins, the Tea1-Tea4/Wsh3 complex, which recruits the Pom1 DYRK-family protein kinase. Pom1 is required for proper positioning of growth sites, and the Deltapom1 mutation brings about monopolar cell growth.\nPom1 kinase physically interacts with Rga4, which has a GAP (GTPase-activating protein) domain for Rho-family GTPase. Genetic and biochemical evidence indicates that Rga4 functions as GAP for the Cdc42 GTPase, an evolutionarily conserved regulator of F-actin. CRIB (Cdc42/Rac interactive binding)-GFP microscopy has revealed that GTP-bound, active Cdc42 is concentrated to growing cell ends accompanied by developed F-actin structures, where the Rga4 GAP is excluded. The monopolar Deltapom1 mutant fails to eliminate Rga4 from the nongrowing cell end, resulting in monopolar distribution of GTP-Cdc42 to the growing cell end. However, mutational inactivation of Rga4 allows Cdc42 to be active at both ends of Deltapom1 cells, suggesting that mislocalization of Rga4 in the Deltapom1 mutant contributes to its monopolar phenotype.\nPom1 kinase recruited to cell ends by the Tea1-Tea4/Wsh3 complex is essential for proper localization of a GAP for Cdc42, Rga4, which ensures bipolar localization of GTP-bound, active Cdc42. Because of the established role of Cdc42 in F-actin formation, these observations provide a new insight into how the microtubule system achieves localized formation of F-actin to generate cell polarity.","doi":"10.1016/j.cub.2008.02.005","authors":"Tatebe H, Nakano K, Maximo R, Shiozaki K","authors_abbrev":"Tatebe H et al.","pubmed_publication_date":"11 Mar 2008","pubmed_entrez_date":"2008-03-11","publication_year":"2008","canto_session_key":"f46092d2d0683328","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-02-05 15:11:15","canto_approved_date":"2026-04-24 06:39:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-01 16:59:58","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.06","SPBC3F6.05","SPAC110.03","SPAC2F7.03c","SPAC16E8.09","SPBC28E12.03"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2019-02-05"},{"uniquename":"PMID:7411631","title":"The antisuppressor strain sin1 of Schizosaccharomyces pombe lacks the modification isopentenyladenosine in transfer RNA.","citation":"J Mol Biol 1980 May 15;139(2):207-19","abstract":"","authors":"Janner F, Vögeli G, Fluri R","authors_abbrev":"Janner F et al.","pubmed_publication_date":"15 May 1980","pubmed_entrez_date":"1980-05-15","publication_year":"1980","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011644","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18629211","title":"Identification and comparative analysis of the peptidyl-prolyl cis/trans isomerase repertoires of H. sapiens, D. melanogaster, C. elegans, S. cerevisiae and Sz. pombe.","citation":"Comp Funct Genomics 2005;6(5-6):277-300","abstract":"The peptidyl-prolyl cis/trans isomerase (PPIase) class of proteins comprises three member families that are found throughout nature and are present in all the major compartments of the cell. Their numbers appear to be linked to the number of genes in their respective genomes, although we have found the human repertoire to be smaller than expected due to a reduced cyclophilin repertoire. We show here that whilst the members of the cyclophilin family (which are predominantly found in the nucleus and cytoplasm) and the parvulin family (which are predominantly nuclear) are largely conserved between different repertoires, the FKBPs (which are predominantly found in the cytoplasm and endoplasmic reticulum) are not. It therefore appears that the cyclophilins and parvulins have evolved to perform conserved functions, while the FKBPs have evolved to fill ever-changing niches within the constantly evolving organisms. Many orthologous subgroups within the different PPIase families appear to have evolved from a distinct common ancestor, whereas others, such as the mitochondrial cyclophilins, appear to have evolved independently of one another. We have also identified a novel parvulin within Drosophila melanogaster that is unique to the fruit fly, indicating a recent evolutionary emergence. Interestingly, the fission yeast repertoire, which contains no unique cyclophilins and parvulins, shares no PPIases solely with the budding yeast but it does share a majority with the higher eukaryotes in this study, unlike the budding yeast. It therefore appears that, in comparison with Schizosaccharomyces pombe, Saccharomyces cerevisiae is a poor representation of the higher eukaryotes for the study of PPIases.","doi":"10.1002/cfg.482","authors":"Pemberton TJ, Kay JE","authors_abbrev":"Pemberton TJ et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2008-07-17","publication_year":"2005","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17512413","title":"Theoretical analysis of epigenetic cell memory by nucleosome modification.","citation":"Cell 2007 May 18;129(4):813-22","abstract":"Chromosomal regions can adopt stable and heritable alternative states resulting in bistable gene expression without changes to the DNA sequence. Such epigenetic control is often associated with alternative covalent modifications of histones. The stability and heritability of the states are thought to involve positive feedback where modified nucleosomes recruit enzymes that similarly modify nearby nucleosomes. We developed a simplified stochastic model for dynamic nucleosome modification based on the silent mating-type region of the yeast Schizosaccharomyces pombe. We show that the mechanism can give strong bistability that is resistant both to high noise due to random gain or loss of nucleosome modifications and to random partitioning upon DNA replication. However, robust bistability required: (1) cooperativity, the activity of more than one modified nucleosome, in the modification reactions and (2) that nucleosomes occasionally stimulate modification beyond their neighbor nucleosomes, arguing against a simple continuous spreading of nucleosome modification.","authors":"Dodd IB, Micheelsen MA, Sneppen K, Thon G","authors_abbrev":"Dodd IB et al.","pubmed_publication_date":"18 May 2007","pubmed_entrez_date":"2007-05-22","publication_year":"2007","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6214161","title":"Yeast cell-wall glucans.","citation":"Adv Microb Physiol 1982;23:151-81","abstract":"","authors":"Duffus JH, Levi C, Manners DJ","authors_abbrev":"Duffus JH et al.","pubmed_publication_date":"1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8887563","title":"A functional dominant mutation in Schizosaccharomyces pombe RNase MRP RNA affects nuclear RNA processing and requires the mitochondrial-associated nuclear mutation ptp1-1 for viability.","citation":"EMBO J 1996 Sep 02;15(17):4723-33","abstract":"The essential gene for RNase MRP RNA, mrp1, was identified previously in Schizosaccharomyces pombe by homology to mammalian RNase MRP RNAs. Here we describe distinct site-specific mutations in RNase MRP RNA that support a conserved role for this ribonucleoprotein in nucleolar 5.8S rRNA processing. One characterized mutation, mrp1-ND90, displays dominance and results in accumulation of unspliced precursor RNAs of dimeric tRNA(Ser)-tRNA(Met)i, suggesting a novel nuclear role for RNase MRP in tRNA processing. Cells carrying the mrp1-ND90 mutation, in the absence of a wild-type copy of mrp1, additionally require the mitochondrially associated nuclear mutation ptp1-1 for viability. Analysis of this mrp1 mutation reinforces previous biochemical evidence suggesting a role for RNase MRP in mitochondrial DNA replication. Several mutations in mrp1 result in unusual cellular morphology, including alterated nuclear organization, and are consistent with a broader nuclear role for RNase MRP in regulating a nuclear signal for septation; these results are a further indication of the multifunctional nature of this ribonucleoprotein.","authors":"Paluh JL, Clayton DA","authors_abbrev":"Paluh JL et al.","pubmed_publication_date":"02 Sep 1996","pubmed_entrez_date":"1996-09-02","publication_year":"1996","canto_session_key":"9745b103c44cf72d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-14 12:37:50","canto_approved_date":"2024-04-02 16:58:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-15 12:05:21","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.82"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-06-14"},{"uniquename":"PMID:11517666","title":"[Internal symmetry in nucleotide sequences of genes encoding the dolichol cycle enzymes].","citation":"Tsitologiia 2001;43(5):491-500","abstract":"In genes alg5, alg8 and swp1 of Saccharomyces cerevisiae, gpt of Schizosaccharomyces pombe and human gene alg6, encoding the dolichol cycle enzymes, a mirror type internal symmetry was found. The symmetry was detected in both complete nucleotide sequences and sequences of the first, second and third nucleotide bases of codons. In the encoding gene regions the density of single- and double-point centres of the internal symmetry for sequences of the second bases was higher in comparison with the sequences of the first and third bases of codons, whereas in the noncoding regions degrees of symmetry of the first, second and third bases sequences did not differ significantly. A clear positive correlation was revealed in the internal symmetry distribution in the second base sequences of codons in genes, on the one hand, and in the gene encoded amino acid sequences, on the other hand. The maximum internal symmetry of gene segments encoding the functionally important regions of proteins was found at the level of the second base sequences. The obtained results corroborate a hypothesis about the determining role of the second bases of codons in encoding amino acid residues. The investigation of internal symmetry in nucleotide sequences has first shown the existence of internal symmetry at the level of gene primary structure.","authors":"Shpakov AO","authors_abbrev":"Shpakov AO","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-08-24","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36194626","title":"Concentration fluctuations in growing and dividing cells: Insights into the emergence of concentration homeostasis.","citation":"PLoS Comput Biol 2022 Oct;18(10):e1010574","abstract":"Intracellular reaction rates depend on concentrations and hence their levels are often regulated. However classical models of stochastic gene expression lack a cell size description and cannot be used to predict noise in concentrations. Here, we construct a model of gene product dynamics that includes a description of cell growth, cell division, size-dependent gene expression, gene dosage compensation, and size control mechanisms that can vary with the cell cycle phase. We obtain expressions for the approximate distributions and power spectra of concentration fluctuations which lead to insight into the emergence of concentration homeostasis. We find that (i) the conditions necessary to suppress cell division-induced concentration oscillations are difficult to achieve; (ii) mRNA concentration and number distributions can have different number of modes; (iii) two-layer size control strategies such as sizer-timer or adder-timer are ideal because they maintain constant mean concentrations whilst minimising concentration noise; (iv) accurate concentration homeostasis requires a fine tuning of dosage compensation, replication timing, and size-dependent gene expression; (v) deviations from perfect concentration homeostasis show up as deviations of the concentration distribution from a gamma distribution. Some of these predictions are confirmed using data for E. coli, fission yeast, and budding yeast.","doi":"10.1371/journal.pcbi.1010574","authors":"Jia C, Singh A, Grima R","authors_abbrev":"Jia C et al.","pubmed_publication_date":"Oct 2022","pubmed_entrez_date":"2022-10-04","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-10-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28678660","title":"The functionally elusive RabI chromosome configuration directly regulates nuclear membrane remodeling at mitotic onset.","citation":"Cell Cycle 2017 Aug 03;16(15):1392-1396","abstract":"Despite its ubiquity in interphase eukaryotic nuclei, the functional significance of the RabI configuration, in which interphase centromeres are clustered at the nuclear envelope (NE) near the centrosome and telomeres localize at the opposite end of the nucleus, has remained mysterious. In a broad variety of organisms, including Schizosaccharomyces pombe, the RabI configuration is maintained throughout mitotic interphase. The fission yeast linker of nucleoskeleton and cytoskeleton (LINC) complex mediates this centromere association. The functional significance of centromere positioning during interphase has been recently revealed using a conditionally inactivated LINC allele that maintains LINC stability but releases interphase centromere-LINC contacts. Remarkably, this interphase release abolishes mitotic spindle formation. Here, we confirm these observations using an alternative strategy to explore the role of centromere-NE association without modifying the LINC complex. We analyze spindle dynamics in cells lacking Csi1, a stabilizer of centromere-LINC associations, and Lem2, a NE protein harboring lamin interacting domains. We recapitulate these observations and their implications for the functional significance of centromere positioning for cell cycle progression in fission yeast and most likely, a wide range of eukaryotes.","doi":"10.1080/15384101.2017.1338986","authors":"Fernández-Álvarez A, Cooper JP","authors_abbrev":"Fernández-Álvarez A et al.","pubmed_publication_date":"03 Aug 2017","pubmed_entrez_date":"2017-07-06","publication_year":"2017","canto_session_key":"6becd9cff464a1f3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-07-07 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.10","SPBC2G2.14"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:42136753","title":"Love-thy-neighbor: neural networks for tracking and lineage tracing in budding yeast.","citation":"Bioinform Adv 2026;6(1):vbag067","abstract":"Tracking and lineage tracing are widely needed tasks in biological image analysis. For cells that grow and divide, tracking is challenging because cells change in number, shape, and size throughout a recording. Longer intervals between images make tracking more difficult. Consequently, tracking has to be performed between consecutive or temporally close images, which leads to exponentially decreasing tracking accuracy and high sensitivity to error rates. For budding yeast, this challenge is further heightened by the similarity of cells in colonies, their dense packing, asymmetric cell divisions, and movement due to colony growth. A related task, lineage tracing, is similarly challenging without fluorescent markers since a new daughter cell can be surrounded by multiple potential mother cells. Here, we present neural networks for budding yeast tracking and lineage tracing, named LYN-track and LYN-trace, respectively, which leverage fine geometric features of cells and their neighborhoods. To train and test the algorithms, we recorded and annotated budding and fission yeast timelapse microscopy movies (78 852 frame-to-frame tracklets, 2512 images), which we make available. On these and existing datasets, our neural network-based methods demonstrate robust, above state-of-the-art performance. Both tools are integrated into graphical user interfaces (GUIs) and can be retrained with custom data.","doi":"10.1093/bioadv/vbag067","authors":"Zelic M, Gligorovski V, Labbaf F, Labagnara M, Oesterle R, Brenna G, Massard F, Chethan SG, Li W, Martin SG, Hauf S, Rahi SJ","authors_abbrev":"Zelic M et al.","pubmed_publication_date":"2026","pubmed_entrez_date":"2026-05-15","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-05-15 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27671940","title":"Gene Deletion by Synthesis in Yeast.","citation":"Methods Mol Biol 2017;1472:169-85","abstract":"Targeted gene deletion is a useful tool for understanding the function of a gene and its protein product. We have developed an efficient and robust gene deletion approach in yeast that employs oligonucleotide-based gene synthesis. This approach requires a deletion cassette composed of three modules: a central 1397-bp KanMX4 selection marker module and two 366-bp gene-specific flanking modules. The invariable KanMX4 module can be used in combination with different pairs of flanking modules targeting different genes. The two flanking modules consist of both sequences unique to each cassette (chromosomal homologous regions and barcodes) and those common to all deletion constructs (artificial linkers and restriction enzyme sites). Oligonucleotides for each module and junction regions are designed using the BatchBlock2Oligo program and are synthesized on a 96-well basis. The oligonucleotides are ligated into a single deletion cassette by ligase chain reaction, which is then amplified through two rounds of nested PCR to obtain sufficient quantities for yeast transformation. After removal of the artificial linkers, the deletion cassettes are transformed into wild-type diploid fission yeast SP286 cells. Verification of correct clone and gene deletion is achieved by performing check PCR and tetrad analysis. This method with proven effectiveness, as evidenced by a high success rate of gene deletion, can be potentially applicable to create systematic gene deletion libraries in a variety of yeast species.","doi":"10.1007/978-1-4939-6343-0_13","authors":"Kim J, Kim DU, Hoe KL","authors_abbrev":"Kim J et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2016-09-28","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-09-29 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10628977","title":"Isolation and characterization of Nrf1p, a novel negative regulator of the Cdc42p GTPase in Schizosaccharomyces pombe.","citation":"Genetics 2000 Jan;154(1):155-65","abstract":"The Cdc42p GTPase and its regulators, such as the Saccharomyces cerevisiae Cdc24p guanine-nucleotide exchange factor, control signal-transduction pathways in eukaryotic cells leading to actin rearrangements. A cross-species genetic screen was initiated based on the ability of negative regulators of Cdc42p to reverse the Schizosaccharomyces pombe Cdc42p suppression of a S. cerevisiae cdc24(ts) mutant. A total of 32 S. pombe nrf (negative regulator of Cdc forty two) cDNAs were isolated that reversed the suppression. One cDNA, nrf1(+), encoded an approximately 15 kD protein with three potential transmembrane domains and 78% amino-acid identity to a S. cerevisiae gene, designated NRF1. A S. pombe Deltanrf1 mutant was viable but overexpression of nrf1(+) in S. pombe resulted in dose-dependent lethality, with cells exhibiting an ellipsoidal morphology indicative of loss of polarized cell growth along with partially delocalized cortical actin and large vacuoles. nrf1(+) also displayed synthetic overdose phenotypes with cdc42 and pak1 alleles. Green fluorescent protein (GFP)-Cdc42p and GFP-Nrf1p colocalized to intracellular membranes, including vacuolar membranes, and to sites of septum formation during cytokinesis. GFP-Nrf1p vacuolar localization depended on the S. pombe Cdc24p homolog Scd1p. Taken together, these data are consistent with Nrf1p functioning as a negative regulator of Cdc42p within the cell polarity pathway.","authors":"Murray JM, Johnson DI","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-11","publication_year":"2000","canto_session_key":"08119406299f6235","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-14 17:11:45","canto_approved_date":"2024-05-08 08:32:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-14 17:11:38","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.14c","SPBC3F6.03","SPAP8A3.04c","SPBC23G7.12c","SPAC16E8.09","SPCC962.04","SPAC26A3.07c","SPAC8F11.07c","SPAC7D4.07c","SPBC119.02","SPBC1685.10","SPBC405.07","SPAC6F6.07c","SPAC4F8.07c","SPAC110.03","SPBC21B10.04c"],"gene_count":16,"ltp_gene_count":16,"approved_date":"2019-06-14"},{"uniquename":"PMID:21575587","title":"Fully hydrated yeast cells imaged with electron microscopy.","citation":"Biophys J 2011 May 18;100(10):2522-9","abstract":"We demonstrate electron microscopy of fully hydrated eukaryotic cells with nanometer resolution. Living Schizosaccharomyces pombe cells were loaded in a microfluidic chamber and imaged in liquid with scanning transmission electron microscopy (STEM). The native intracellular (ultra)structures of wild-type cells and three different mutants were studied without prior labeling, fixation, or staining. The STEM images revealed various intracellular components that were identified on the basis of their shape, size, location, and mass density. The maximal achieved spatial resolution in this initial study was 32 ± 8 nm, an order of magnitude better than achievable with light microscopy on pristine cells. Light-microscopy images of the same samples were correlated with the corresponding electron-microscopy images. Achieving synergy between the capabilities of light and electron microscopy, we anticipate that liquid STEM will be broadly applied to explore the ultrastructure of live cells.","doi":"10.1016/j.bpj.2011.03.045","authors":"Peckys DB, Mazur P, Gould KL, de Jonge N","authors_abbrev":"Peckys DB et al.","pubmed_publication_date":"18 May 2011","pubmed_entrez_date":"2011-05-18","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084842","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.587"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15847583","title":"Combined intracellular three-dimensional imaging and selective nanosurgery by a nonlinear microscope.","citation":"J Biomed Opt 2005;10(1):14002","abstract":"We use near-IR femtosecond laser pulses for a combination of microscopy and nanosurgery on fluorescently labeled structures within living cells. Three-dimensional reconstructions of microtubule structures tagged with green fluorescent protein (GFP) are made during different phases of the cell cycle. Further, the microtubules are dissected using the same laser beam but with a higher laser power than for microscopy. We establish the viability of this technique for the cells of a fission yeast, which is a common model to study the mechanics of cell division. We show that nanosurgery can be performed with submicrometer precision and without visible collateral damage to the cell. The energy is primarily absorbed by the GFP molecules, and not by other native structures in the cell. GFP is particularly suitable for multiphoton excitation, as its excitation wavelength near 900 nm is benign for most cellular structures. The ability to use GFP to label structures for destruction by multiphoton excitation may be a valuable tool in cell biology.","authors":"Sacconi L, Tolić-Nørrelykke IM, Antolini R, Pavone FS","authors_abbrev":"Sacconi L et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-04-26","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31350787","title":"Schizosaccharomyces pombe Mti2 and Mti3 act in conjunction during mitochondrial translation initiation.","citation":"FEBS J 2019 Nov;286(22):4542-4553","abstract":"Mitochondrial DNA encodes key subunits of the oxidative phosphorylation complexes essential for ATP production. Translation initiation in mitochondria requires two general factors, mtIF2 and mtIF3, whose counterparts in bacteria are essential for protein synthesis. In this study, we report the characterization of the fission yeast Schizosaccharomyces pombe mtIF2 (Mti2) and mtIF3 (Mti3). Deletion of mti2 impairs cell growth on the respiratory medium. The growth defect of the mti2 deletion mutant can be suppressed by expressing IFM1, the Saccharomyces cerevisiae homolog of Mti2, demonstrating functional conservation between the two proteins. Deletion of mti2 also impairs mitochondrial protein synthesis. Unlike mti2, deletion of mti3 does not affect cell growth on respiratory media and mitochondrial translation. However, deletion of mti3 exacerbates the growth defect of the Δmti2 mutant, suggesting that the two proteins have distinct, but partially overlapping functions during the process of mitochondrial translation initiation in S. pombe. Both Mti2 and Mti3 are associated with the small subunit of the mitochondrial ribosome (mitoribosome). Disruption of mti2, but not mti3, causes dissociation of the mitoribosome and also abolishes Mti3 binding to the small subunit of the mitoribosome. Our results suggest that Mti2 and Mti3 bind in a sequential manner to the small subunit of the mitoribosome and that Mti3 facilitates the function of Mti2 in mitochondrial translation initiation. Our findings also support the view that the importance of the mitochondrial translation initiation factors varies among the organisms.","doi":"10.1111/febs.15021","authors":"Luo Y, Su R, Wang Y, Xie W, Liu Z, Huang Y","authors_abbrev":"Luo Y et al.","pubmed_publication_date":"Nov 2019","pubmed_entrez_date":"2019-07-28","publication_year":"2019","canto_session_key":"1ac71137f0c65839","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2019-10-31 11:26:02","canto_approved_date":"2019-10-31 11:26:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-22 01:26:05","canto_added_date":"2019-07-29 00:15:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18E5.13","SPBC1271.15c","YJL131C"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-10-31"},{"uniquename":"PMID:31744872","title":"Branched unwinding mechanism of the Pif1 family of DNA helicases.","citation":"Proc Natl Acad Sci U S A 2019 Dec 03;116(49):24533-24541","abstract":"Members of the Pif1 family of helicases function in multiple pathways that involve DNA synthesis: DNA replication across G-quadruplexes; break-induced replication; and processing of long flaps during Okazaki fragment maturation. Furthermore, Pif1 increases strand-displacement DNA synthesis by DNA polymerase δ and allows DNA replication across arrays of proteins tightly bound to DNA. This is a surprising feat since DNA rewinding or annealing activities limit the amount of single-stranded DNA product that Pif1 can generate, leading to an apparently poorly processive helicase. In this work, using single-molecule Förster resonance energy transfer approaches, we show that 2 members of the Pif1 family of helicases, Pif1 from  Saccharomyces cerevisiae  and Pfh1 from  Schizosaccharomyces pombe , unwind double-stranded DNA by a branched mechanism with 2 modes of activity. In the dominant mode, only short stretches of DNA can be processively and repetitively opened, with reclosure of the DNA occurring by mechanisms other than strand-switching. In the other less frequent mode, longer stretches of DNA are unwound via a path that is separate from the one leading to repetitive unwinding. Analysis of the kinetic partitioning between the 2 different modes suggests that the branching point in the mechanism is established by conformational selection, controlled by the interaction of the helicase with the 3' nontranslocating strand. The data suggest that the dominant and repetitive mode of DNA opening of the helicase can be used to allow efficient DNA replication, with DNA synthesis on the nontranslocating strand rectifying the DNA unwinding activity.","doi":"10.1073/pnas.1915654116","authors":"Singh SP, Soranno A, Sparks MA, Galletto R","authors_abbrev":"Singh SP et al.","pubmed_publication_date":"03 Dec 2019","pubmed_entrez_date":"2019-11-21","publication_year":"2019","canto_session_key":"22b3ba524d1dfe01","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-11-22 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18206786","title":"Evaluation of the inhibitory effect of dimethyl dicarbonate (DMDC) against wine microorganisms.","citation":"Food Microbiol 2008 Apr;25(2):422-7","abstract":"Several microbial species associated with wine were challenged against increasing concentrations of dimethyl dicarbonate (DMDC). The concentration inducing complete cell death upon addition to red wine was regarded as the minimum inhibitory concentration (MIC). In dry red wines with 12% (v/v) ethanol and pH 3.50, the inactivation depended on the initial cell concentration. For an initial inoculum of 500 CFU/ml, the MIC of the yeasts species Schizosaccharomyces pombe, Dekkera bruxellensis, Saccharomyces cerevisiae and Pichia guilliermondii was 100mg/l. The most sensitive strains belong to Zygosaccharomyces bailii, Zygoascus hellenicus and Lachancea thermotolerans, with MIC of 25mg/l DMDC. For inoculation rates of about 10(6)CFU/ml, the maximum dose of DMDC legally authorized (200mg/l) was not effective against the most resistant species. The addition of 100mg/l potassium metabisulphite (PMB), equivalent to 1mg/l molecular sulphur dioxide, increased the inactivation effect of 100mg/l DMDC over initial yeast populations of 10(6)CFU/ml but did not fully kill S. pombe and S. cerevisiae. Lactic acid and acetic acid bacteria were not killed by the addition of 300 mg/l of DMDC. Trials performed in wines before bottling showed that in most samples indigenous bacterial populations were not affected by 200mg/l DMDC. Therefore, under winery practice, DMDC at the maximum dose legally permitted may be regarded as an efficient preservative to control low contamination rates of yeasts but ineffective against lactic acid and acetic acid bacteria.","doi":"10.1016/j.fm.2007.10.003","authors":"Costa A, Barata A, Malfeito-Ferreira M, Loureiro V","authors_abbrev":"Costa A et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-01-22","publication_year":"2008","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14599746","title":"Fission yeast Uve1 and Apn2 function in distinct oxidative damage repair pathways in vivo.","citation":"DNA Repair (Amst) 2003 Nov 21;2(11):1253-67","abstract":"In Schizosaccharomyces pombe, the endonuclease Uve1 functions as the first step in an alternate UV photo-product repair pathway that is distinct from nucleotide excision repair (NER). Based upon the broad substrate specificity of Uve1 in vitro, and the observation that Uve1 mutants accumulate spontaneous mutations at an elevated rate in vivo, we and others have hypothesized that this protein might have a function in a mutation avoidance pathway other than UV photo-product repair. We show here that fission yeast Uve1 also functions in oxidative damage repair in vivo. We have determined the spectrum of spontaneous mutations that arise in uve1 null (uve1 degrees ) cells and have observed that both G-->T(C-->A) and T-->G(A-->C) transversions occur at an increased rate relative to wildtype cells. These mutations are indicative of unrepaired oxidative DNA damage and are very similar to the mutation spectrum observed in 8-oxoguanine glycosylase (OGG1) mutants in Saccharomyces cerevisiae. We have generated an apn2 null (apn2 degrees ) strain and shown that it is mildly sensitive to H(2)O(2). Furthermore we have also shown that apn2 degrees cells have an elevated rate of spontaneous mutation that is similar to uve1 degrees. The phenotype of apn2 degrees uve1 degrees double mutants indicates that these genes define distinct spontaneous mutation avoidance pathways. While uve1 degrees cells show only a modest sensitivity to the oxidizing agent hydrogen peroxide (H(2)O(2)), both uve1 degrees and apn2 degrees cells also display a marked increased in mutation rate following exposure to H(2)O(2) doses. Collectively these data demonstrate that Uve1 is a component of multiple alternate repair pathways in fission yeast and suggest a possible role for Uve1 in a general alternate incision repair pathway in eukaryotes.","authors":"Fraser JL, Neill E, Davey S","authors_abbrev":"Fraser JL et al.","pubmed_publication_date":"21 Nov 2003","pubmed_entrez_date":"2003-11-06","publication_year":"2003","canto_session_key":"4b1bf8c741c5b2a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-10-15 15:01:16","canto_approved_date":"2026-02-17 15:38:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-15 15:01:09","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.10","SPAC19G12.02c","SPBC19C7.09c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-10-15"},{"uniquename":"PMID:21481773","title":"The hypoxic regulator of sterol synthesis nro1 is a nuclear import adaptor.","citation":"Structure 2011 Apr 13;19(4):503-14","abstract":"Fission yeast protein Sre1, the homolog of the mammalian sterol regulatory element-binding protein (SREBP), is a hypoxic transcription factor required for sterol homeostasis and low-oxygen growth. Nro1 regulates the stability of the N-terminal transcription factor domain of Sre1 (Sre1N) by inhibiting the action of the prolyl 4-hydroxylase-like Ofd1 in an oxygen-dependent manner. The crystal structure of Nro1 determined at 2.2 Å resolution shows an all-α-helical fold that can be divided into two domains: a small N-terminal domain, and a larger C-terminal HEAT-repeat domain. Follow-up studies showed that Nro1 defines a new class of nuclear import adaptor that functions both in Ofd1 nuclear localization and in the oxygen-dependent inhibition of Ofd1 to control the hypoxic response.","doi":"10.1016/j.str.2011.01.017","authors":"Yeh TL, Lee CY, Amzel LM, Espenshade PJ, Bianchet MA","authors_abbrev":"Yeh TL et al.","pubmed_publication_date":"13 Apr 2011","pubmed_entrez_date":"2011-04-13","publication_year":"2011","canto_session_key":"f76dbfe807197d79","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-05-07 16:29:11","canto_approved_date":"2024-05-17 11:19:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-29 11:48:59","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.08c","SPCC4B3.07","SPBC19C2.09","SPBC14F5.03c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-05-07","pdb_entries":[{"pdb_id":"6e0t","gene_chains":[{"gene_uniquename":"SPBC6B1.08c","chain":"X","position":"255-515"}],"title":"C-terminal domain of Fission Yeast OFD1","entry_authors":"Bianchet MA,Amzel LM,Espenshade PJ,Yeh T","entry_authors_abbrev":"Bianchet MA et al.","reference_uniquename":"PMID:21481773","experimental_method":"X-ray","resolution":"2.02"},{"pdb_id":"3msv","gene_chains":[{"gene_uniquename":"SPCC4B3.07","chain":"A/B","position":"1-393"}],"title":"The hypoxic regulator of sterol synthesis Nro1 is a nuclear import adaptor","entry_authors":"Yeh TL,Amzel LM,Bianchet MA","entry_authors_abbrev":"Yeh TL et al.","reference_uniquename":"PMID:21481773","experimental_method":"X-ray","resolution":"2.18"}]},{"uniquename":"PMID:8056292","title":"Dipeptidyl aminopeptidase yspI mutants of Schizosaccharomyces pombe: genetic mapping of dpa1+ on chromosome III.","citation":"FEMS Microbiol Lett 1994 Jul 01;120(1-2):211-6","abstract":"A mutant strain of Schizosaccharomyces pombe lacking dipeptidyl aminopeptidase yspI was isolated from a strain already defective in aminopeptidase activity by means of a staining technique with the chromogenic substrate ala-pro-4-methoxy-beta-naph-thylamide to screen colonies for the absence of the enzyme. The defect segregated 2+:2- in meiotic tetrads, indicating a single chromosomal gene mutation, which was shown to be recessive. Gene dosage experiments indicated that the mutation resides in the structural gene of dipeptidyl aminopeptidase yspI, dpa1+. The dpa1+ gene was located on chromosome III by using m-fluorophenylalanine-induced haploidization and mitotic analysis. dpa1 mutants did not show any obvious phenotype under a variety of conditions tested.","authors":"Villa L, Suárez-Rendueles P","authors_abbrev":"Villa L et al.","pubmed_publication_date":"01 Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20647746","title":"Schizosaccharoomyces pombe gene deletion library nearing completion: new perspectives for cell cycle research.","citation":"Cell Cycle 2010 Jul 01;9(13):2492","abstract":"","authors":"Sipiczki M","authors_abbrev":"Sipiczki M","pubmed_publication_date":"01 Jul 2010","pubmed_entrez_date":"2010-07-22","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34208949","title":"Mapping and Analysis of Swi5 and Sfr1 Phosphorylation Sites.","citation":"Genes (Basel) 2021 Jun 30;12(7)","abstract":"The evolutionarily conserved Swi5-Sfr1 complex plays an important role in homologous recombination, a process crucial for the maintenance of genomic integrity. Here, we purified  Schizosaccharomyces pombe  Swi5-Sfr1 complex from meiotic cells and analyzed it by mass spectrometry. Our analysis revealed new phosphorylation sites on Swi5 and Sfr1. We found that mutations that prevent phosphorylation of Swi5 and Sfr1 do not impair their function but  swi5  and  sfr1  mutants encoding phosphomimetic aspartate at the identified phosphorylation sites are only partially functional. We concluded that during meiosis, Swi5 associates with Sfr1 and both Swi5 and Sfr1 proteins are phosphorylated. However, the functional relevance of Swi5 and Sfr1 phosphorylation remains to be determined.","doi":"10.3390/genes12071014","authors":"Sevcovicova A, Plava J, Gazdarica M, Szabova E, Huraiova B, Gaplovska-Kysela K, Cipakova I, Cipak L, Gregan J","authors_abbrev":"Sevcovicova A et al.","pubmed_publication_date":"30 Jun 2021","pubmed_entrez_date":"2021-07-02","publication_year":"2021","canto_session_key":"7f89392aaf70c882","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Juraj Gregan","canto_first_approved_date":"2021-07-15 15:24:30","canto_approved_date":"2024-02-21 14:56:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-07-06 08:35:21","canto_added_date":"2021-07-04 00:15:05","annotation_curators":[{"name":"Juraj Gregan","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.07","SPAC8E11.03c","SPBC409.03"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2021-07-15"},{"uniquename":"EMBL:AU006641","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12471450","title":"Activation of the urease of Schizosaccharomyces pombe by the UreF accessory protein from soybean.","citation":"Mol Genet Genomics 2002 Dec;268(4):525-34","abstract":"Plant orthologs of the bacterial urease accessory genes ureD and ureF, which are required for the insertion of the nickel ion at the active site, have been isolated from soybean ( Glycine max L. Merr.), tomato ( Lycopersicon esculentum) and Arabidopsis thaliana. The functionality of soybean UreD and UreF was tested by measuring their ability to complement urease-negative mutants of Schizosaccharomyces pombe, a eukaryote which produces a \"plant-like\" urease of ~90 kDa. The S. pombe ure4 mutant was complemented by a 12-kb fragment of S. pombe genomic DNA, which was shown by PCR to contain a putative ureD gene. However, ure4 was not complemented by a UreD cDNA soybean, expressed under the control of a strong promoter. In contrast, an S. pombe ure3 mutation was complemented by both a 10-kb fragment of S. pombe DNA containing ureF and the UreF cDNA from soybean. Soybean Eu2 is a candidate urease accessory gene; its product cooperates with the Eu3 protein in activating apourease in vitro. However, the sequences of UreD and UreF transcripts from two eu2/eu2 mutants, recovered as RT-PCR products, revealed no mutational alteration, suggesting that Eu2 encodes neither UreD nor UreF.","authors":"Bacanamwo M, Witte CP, Lubbers MW, Polacco JC","authors_abbrev":"Bacanamwo M et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2002-12-10","publication_year":"2002","canto_session_key":"7a743f10d923be4a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-12-18 16:51:11","canto_approved_date":"2019-05-21 22:07:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-12-15 14:58:00","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.09c","SPAC29A4.13","SPCPB16A4.05c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-12-18"},{"uniquename":"PMID:22143918","title":"Uncoupling of genomic and epigenetic signals in the maintenance and inheritance of heterochromatin domains in fission yeast.","citation":"Genetics 2012 Feb;190(2):549-57","abstract":"Many essential aspects of genome function, including gene expression and chromosome segregation, are mediated throughout development and differentiation by changes in the chromatin state. Along with genomic signals encoded in the DNA, epigenetic processes regulate heritable gene expression patterns. Genomic signals such as enhancers, silencers, and repetitive DNA, while required for the establishment of alternative chromatin states, have an unclear role in epigenetic processes that underlie the persistence of chromatin states throughout development. Here, we demonstrate in fission yeast that the maintenance and inheritance of ectopic heterochromatin domains are independent of the genomic sequences necessary for their de novo establishment. We find that both structural heterochromatin and gene silencing can be stably maintained over an ~10-kb domain for up to hundreds of cell divisions in the absence of genomic sequences required for heterochromatin establishment, demonstrating the long-term persistence and stability of this chromatin state. The de novo heterochromatin, despite the absence of nucleation sequences, is also stably inherited through meiosis. Together, these studies provide evidence for chromatin-dependent, epigenetic control of gene silencing that is heritable, stable, and self-sustaining, even in the absence of the originating genomic signals.","doi":"10.1534/genetics.111.137083","authors":"Wheeler BS, Ruderman BT, Willard HF, Scott KC","authors_abbrev":"Wheeler BS et al.","pubmed_publication_date":"Feb 2012","pubmed_entrez_date":"2011-12-07","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10978275","title":"A family of cAMP-response-element-related DNA sequences with meiotic recombination hotspot activity in Schizosaccharomyces pombe.","citation":"Genetics 2000 Sep;156(1):59-68","abstract":"The heptamer sequence ATGACGT is essential for activity of the M26 meiotic recombination hotspot in the ade6 gene of Schizosaccharomyces pombe. Hotspot activity is associated with binding of the heterodimeric transcription factor Atf1.Pcr1 to M26. We have found that the sequences (C/T/G) TGACGT also bound Atf1.Pcr1 and acted as meiotic hotspots, but unlike M26 they must be followed by A or C for Atf1.Pcr1 binding and hotspot activity. The basis of the hotspot activity of CTGACGTA (ade6-3013) appears to be identical to that of M26: hotspot activity of both sequences was abolished in cells mutant for atf1, pcr1, spc1, or wis1 and was undetectable in mitotic recombination and in meiotic recombination when located on a plasmid. Both hotspot sequences were sites of micrococcal nuclease hypersensitivity in meiotic chromatin, suggesting that they create an open chromatin structure during meiosis at the site of the hotspots. The newly identified hotspot sequences (C/T/G)TGACGT(A/C) and M26 are closely related to the cAMP response element (CRE) consensus sequence for binding of cAMP-responsive transcription factors such as Atf1.Pcr1, suggesting a link between transcription and meiotic recombination. These results significantly expand the list of identified sequences with meiotic recombination hotspot activity in S. pombe from a single sequence to a family of CRE-related sequences.","authors":"Fox ME, Yamada T, Ohta K, Smith GR","authors_abbrev":"Fox ME et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-09-09","publication_year":"2000","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2080665","title":"An assay of relative cell wall porosity in Saccharomyces cerevisiae, Kluyveromyces lactis and Schizosaccharomyces pombe.","citation":"Yeast 1990;6(6):483-90","abstract":"We have developed a new assay to determine relative cell wall porosity in yeasts, which is based on polycation-induced leakage of UV-absorbing compounds. Polycations with a small hydrodynamic radius as measured by gel filtration (poly-L-lysine) caused cell leakage independent of cell wall porosity whereas polycations with a large hydrodynamic radius (DEAE-dextrans) caused only limited cell leakage due to limited passage through the cell wall. This allowed the ratio between DEAE-dextran- and poly-L-lysine-induced cell leakage to be used as a measure of cell wall porosity in Saccharomyces cerevisiae, Kluyveromyces lactis and Schizosaccharomyces pombe. Using this assay, we found that the composition of the growth medium affected cell wall porosity in S. cerevisiae. In addition, we could show that cell wall porosity is limited by the number of disulphide bridges in the wall and is dependent on cell turgor. It is argued that earlier methods to estimate cell wall porosity in S. cerevisiae resulted in large underestimations.","authors":"De Nobel JG, Klis FM, Munnik T, Priem J, van den Ende H","authors_abbrev":"De Nobel JG et al.","pubmed_publication_date":"1990","pubmed_entrez_date":"1990-11-01","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40899782","title":"Golgi_traff phylogeny reveals ancient eukaryotic genes with recent surprises: replication and diversification of HID1 Domain-Containing Protein unique to Schizosaccharomyces.","citation":"FEMS Microbiol Lett 2025 Sep 03;","abstract":"Golgi_traff is a Pfam clan containing two members, Dymeclin and HID1 domain-containing protein. Interrogation of over 900 eukaryotic genomes with sequence models showed that both are ancient eukaryotic genes, which have exhibited different paths of gene loss, including from major taxonomic groups. For example, the Metazoa have both genes, whereas the Viridiplantae and Dikarya have lost HID and DYM, respectively. A unique replication event occurred within the genus Schizosaccharomyces in that all sequenced species possess three HID-encoding paralogs, whereas its nearest fungal relatives and other eukaryotes are almost exclusively monogenic. A phylogenetic analysis of yeasts revealed that the Golgi-resident paralog Human ortholog 3 (SPAC17A5.16) is more similar to the HID of other yeasts than to its paralogs. Transmission electron microscopy revealed that the SPAC17A5.16 mutant lacks a stacked Golgi apparatus (GA) form, suggesting a role in maintaining GA structure. Altered proliferation of the SPAC17A5.16 mutant in response to GA disrupting chemical agents indicated a perturbation of GA-related functions. Structural models suggest SPAC17A5.16 has a long, disordered N-terminal region that may facilitate anchoring to GA membranes. A modification to Schizosaccharomyces HID nomenclature is proposed to reflect their evolutionary and functional characteristics. The potential of the Golgi_traff clan to serve as a model for the diversification of protein function according to the concepts of sub/neofunctionalization is discussed.","doi":"10.1093/femsle/fnaf088","authors":"Hooks MA, Alasmari A, Alshehri M, Brocard L, Hooks KB, Julien M, McFarlane RJ","authors_abbrev":"Hooks MA et al.","pubmed_publication_date":"03 Sep 2025","pubmed_entrez_date":"2025-09-03","publication_year":"2025","canto_session_key":"08bebfeb282a3936","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mark Hooks","canto_first_approved_date":"2025-09-28 11:15:46","canto_approved_date":"2025-09-28 11:15:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-09-10 13:38:27","canto_added_date":"2025-09-03 23:25:05","annotation_curators":[{"name":"Mark Hooks","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.16","SPAP27G11.12","SPBP19A11.07c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2025-09-28"},{"uniquename":"PMID:9057003","title":"The inositol 1,4,5-trisphosphate 6-kinase of Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1997 Feb;25(1):105S","abstract":"","authors":"Ongusaha PP, Hughes PJ, Hirata M, Davey J, Michell RH","authors_abbrev":"Ongusaha PP et al.","pubmed_publication_date":"Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_session_key":"3546a54b6fca3ca1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:47:32","canto_session_submitted_date":"2012-02-27 11:05:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:16998477","title":"Self-organization of interphase microtubule arrays in fission yeast.","citation":"Nat Cell Biol 2006 Oct;8(10):1102-7","abstract":"Microtubule organization is key to eukaryotic cell structure and function. In most animal cells, interphase microtubules organize around the centrosome, the major microtubule organizing centre (MTOC). Interphase microtubules can also become organized independently of a centrosome, but how acentrosomal microtubules arrays form and whether they are functionally equivalent to centrosomal arrays remains poorly understood. Here, we show that the interphase microtubule arrays of fission yeast cells can persist independently of nuclear-associated MTOCs, including the spindle pole body (SPB)--the centrosomal equivalent. By artificially enucleating cells, we show that arrays can form de novo (self-organize) without nuclear-associated MTOCs, but require the microtubule nucleator mod20-mbo1-mto1 (refs 3-5), the bundling factor ase1 (refs 6,7), and the kinesin klp2 (refs 8,9). Microtubule arrays in enucleated and nucleated cells are morphologically indistinguishable and similarly locate to the cellular axis and centre. By simultaneously tracking nuclear-independent and SPB-associated microtubule arrays within individual nucleated cells, we show that both define the cell centre with comparable precision. We propose that in fission yeast, nuclear-independent, self-organized, acentrosomal microtubule arrays are structurally and functionally equivalent to centrosomal arrays.","authors":"Carazo-Salas RE, Nurse P","authors_abbrev":"Carazo-Salas RE et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-09-26","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19423874","title":"Mapping epigenetic mutations in fission yeast using whole-genome next-generation sequencing.","citation":"Genome Res 2009 Jun;19(6):1077-83","abstract":"Fission yeast is an important model for epigenetic studies due to the ease with which genetic mutants can be isolated. However, it can be difficult to complement epigenetic phenotypes with genomic libraries in order to identify the genes responsible. This is because epigenetic phenotypes are typically unstable, and can prohibit complementation if silencing cannot be reestablished. Here we have resequenced the fission yeast genome following mutagenesis to readily identify a novel mutant involved in heterochromatic silencing. Candidate genes were identified as functional single base changes linked to the mutation, which were then reconstituted in a wild-type strain to recapitulate the mutant phenotype. By this procedure we identified a weak allele of ubc4, which encodes an essential E2 ubiquitin ligase, as responsible for the swi*603 mutant phenotype. In combination with a large collection of mutants and suppressor plasmids, next-generation genomic resequencing promises to dramatically enhance the power of yeast genetics, permitting the isolation of subtle alleles of essential genes, alleles with quantitative effects, and enhancers and suppressors of heterochromatic silencing.","doi":"10.1101/gr.089318.108","authors":"Irvine DV, Goto DB, Vaughn MW, Nakaseko Y, McCombie WR, Yanagida M, Martienssen R","authors_abbrev":"Irvine DV et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-05-09","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31454352","title":"Telomere-binding proteins Taz1 and Rap1 regulate DSB repair and suppress gross chromosomal rearrangements in fission yeast.","citation":"PLoS Genet 2019 Aug;15(8):e1008335","abstract":"Genomic rearrangements (gross chromosomal rearrangements, GCRs) threatens genome integrity and cause cell death or tumor formation. At the terminus of linear chromosomes, a telomere-binding protein complex, called shelterin, ensures chromosome stability by preventing chromosome end-to-end fusions and regulating telomere length homeostasis. As such, shelterin-mediated telomere functions play a pivotal role in suppressing GCR formation. However, it remains unclear whether the shelterin proteins play any direct role in inhibiting GCR at non-telomeric regions. Here, we have established a GCR assay for the first time in fission yeast and measured GCR rates in various mutants. We found that fission yeast cells lacking shelterin components Taz1 or Rap1 (mammalian TRF1/2 or RAP1 homologues, respectively) showed higher GCR rates compared to wild-type, accumulating large chromosome deletions. Genetic dissection of Rap1 revealed that Rap1 contributes to inhibiting GCRs via two independent pathways. The N-terminal BRCT-domain promotes faithful DSB repair, as determined by I-SceI-mediated DSB-induction experiments; moreover, association with Poz1 mediated by the central Poz1-binding domain regulates telomerase accessibility to DSBs, leading to suppression of de novo telomere additions. Our data highlight unappreciated functions of the shelterin components Taz1 and Rap1 in maintaining genome stability, specifically by preventing non-telomeric GCRs.","doi":"10.1371/journal.pgen.1008335","authors":"Irie H, Yamamoto I, Tarumoto Y, Tashiro S, Runge KW, Ishikawa F","authors_abbrev":"Irie H et al.","pubmed_publication_date":"Aug 2019","pubmed_entrez_date":"2019-08-28","publication_year":"2019","canto_session_key":"6bfb7a847a0fc3fe","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-08-29 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29083304","title":"Prolyl dihydroxylation of unassembled uS12/Rps23 regulates fungal hypoxic adaptation.","citation":"Elife 2017 Oct 30;6","abstract":"The prolyl-3,4-dihydroxylase Ofd1 and nuclear import adaptor Nro1 regulate the hypoxic response in fission yeast by controlling activity of the sterol regulatory element-binding protein transcription factor Sre1. Here, we identify an extra-ribosomal function for uS12/Rps23 central to this regulatory system. Nro1 binds Rps23, and Ofd1 dihydroxylates Rps23 P62 in complex with Nro1. Concurrently, Nro1 imports Rps23 into the nucleus for assembly into 40S ribosomes. Low oxygen inhibits Ofd1 hydroxylase activity and stabilizes the Ofd1-Rps23-Nro1 complex, thereby sequestering Ofd1 from binding Sre1, which is then free to activate hypoxic gene expression. In vitro studies demonstrate that Ofd1 directly binds Rps23, Nro1, and Sre1 through a consensus binding sequence. Interestingly, Rps23 expression modulates Sre1 activity by changing the Rps23 substrate pool available to Ofd1. To date, oxygen is the only known signal to Sre1, but additional nutrient signals may tune the hypoxic response through control of unassembled Rps23 or Ofd1 activity.","doi":"10.7554/eLife.28563","authors":"Clasen SJ, Shao W, Gu H, Espenshade PJ","authors_abbrev":"Clasen SJ et al.","pubmed_publication_date":"30 Oct 2017","pubmed_entrez_date":"2017-10-31","publication_year":"2017","canto_session_key":"54b4f3fa56c4718d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sara Clasen","canto_first_approved_date":"2017-12-01 09:25:10","canto_approved_date":"2024-12-28 13:17:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-09 04:59:10","canto_added_date":"2017-11-02 01:15:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":102,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Sara Clasen","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.08c","SPCC4B3.07","SPBC19C2.09","SPAC1805.17","SPAC23C11.02c","SPBP4H10.13"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-12-01"},{"uniquename":"PMID:10454621","title":"Intron-exon structures of eukaryotic model organisms.","citation":"Nucleic Acids Res 1999 Aug 01;27(15):3219-28","abstract":"To investigate the distribution of intron-exon structures of eukaryotic genes, we have constructed a general exon database comprising all available intron-containing genes and exon databases from 10 eukaryotic model organisms: Homo sapiens, Mus musculus, Gallus gallus, Rattus norvegicus, Arabidopsis thaliana, Zea mays, Schizosaccharomyces pombe, Aspergillus, Caenorhabditis elegans and Drosophila. We purged redundant genes to avoid the possible bias brought about by redundancy in the databases. After discarding those questionable introns that do not contain correct splice sites, the final database contained 17 102 introns, 21 019 exons and 2903 independent or quasi-independent genes. On average, a eukaryotic gene contains 3.7 introns per kb protein coding region. The exon distribution peaks around 30-40 residues and most introns are 40-125 nt long. The variable intron-exon structures of the 10 model organisms reveal two interesting statistical phenomena, which cast light on some previous speculations. (i) Genome size seems to be correlated with total intron length per gene. For example, invertebrate introns are smaller than those of human genes, while yeast introns are shorter than invertebrate introns. However, this correlation is weak, suggesting that other factors besides genome size may also affect intron size. (ii) Introns smaller than 50 nt are significantly less frequent than longer introns, possibly resulting from a minimum intron size requirement for intron splicing.","authors":"Deutsch M, Long M","authors_abbrev":"Deutsch M et al.","pubmed_publication_date":"01 Aug 1999","pubmed_entrez_date":"1999-08-24","publication_year":"1999","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16314302","title":"Simulation of non-specific protein-mRNA interactions.","citation":"Nucleic Acids Res 2005;33(21):6694-9","abstract":"Protein-nucleic acid interactions exhibit varying degrees of specificity. Relatively high affinity, sequence-specific interactions, can be studied with structure determination, but lower affinity, non-specific interactions are also of biological importance. We report simulations that predict the population of nucleic acid paths around protein surfaces, and give binding constant differences for changes in the protein scaffold. The method is applied to the non-specific component of interactions between eIF4Es and messenger RNAs that are bound tightly at the cap site. Adding a fragment of eIF4G to the system changes both the population of mRNA paths and the protein-mRNA binding affinity, suggesting a potential role for non-specific interactions in modulating translational properties. Generally, the free energy simulation technique could work in harness with characterized tethering points to extend analysis of nucleic acid conformation, and its modulation by protein scaffolds.","authors":"Magee J, Warwicker J","authors_abbrev":"Magee J et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-11-30","publication_year":"2005","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40237466","title":"Tandem inactivation of inositol pyrophosphatases Asp1, Siw14, and Aps1 illuminates functional redundancies in inositol pyrophosphate catabolism in fission yeast.","citation":"mBio 2025 Apr 16;:e0038925","abstract":"Inositol pyrophosphates 5-IP 7 , 1-IP 7 , and 1,5-IP 8  are eukaryal signaling molecules that influence cell physiology, especially phosphate homeostasis. In fission yeast, 1,5-IP 8  and 1-IP 7  impact gene expression by acting as agonists of RNA 3'-processing and transcription termination. 1,5-IP 8  is synthesized by position-specific kinases Kcs1 and Asp1 that convert IP 6  to 5-IP 7  and 5-IP 7  to 1,5-IP 8 , respectively. Inositol pyrophosphatase enzymes Asp1 (a histidine acid phosphatase), Siw14 (a cysteinyl phosphatase), and Aps1 (a Nudix hydrolase) are agents of inositol pyrophosphate catabolism in fission yeast. Whereas Asp1, Siw14, and Aps1 are individually inessential, double pyrophosphatase mutants  asp1-H397A aps1 ∆ and  siw14 ∆  aps1 ∆ display severe growth defects caused by overzealous 3'-processing/termination. By applying CE-ESI-MS to profile the inositol pyrophosphate content of fission yeast mutants in which inositol pyrophosphate toxicity is genetically suppressed, we elucidated the functional redundancies of the Asp1, Siw14, and Aps1 pyrophosphatases. Asp1, which exclusively cleaves the 1-β-phosphate, and Aps1, which prefers to cleave the 1-β-phosphate, play essential overlapping roles in guarding against the accumulation of toxic levels of 1-IP 7 . Aps1 and Siw14 together catabolize the inositol-5-pyrophosphates, and their simultaneous inactivation results in overaccumulation of 5-IP 7 . Cells lacking all three pyrophosphatases amass high levels of 1,5-IP 8  and 1-IP 7 , with concomitant depletion of IP 6 . A genetic screen identified three missense mutations in the catalytic domain of Kcs1 kinase that suppressed inositol-1-pyrophosphate toxicosis. The screen also implicated the 3'-processing factor Swd22, the inositol pyrophosphate sensor Spx1, and the nuclear poly(A)-binding protein Nab2 as mediators of inositol-1-pyrophosphate toxicity.IMPORTANCEInositol pyrophosphates are key effectors of eukaryal cellular phosphate homeostasis. They are synthesized by kinases that add a β-phosphate to the 5- or 1-phosphate groups of IP 6  and catabolized by three classes of pyrophosphatases that hydrolyze the β-phosphates of 5-IP 7 , 1-IP 7 , or 1,5-IP 8 . Whereas the fission yeast inositol pyrophosphatases-Asp1 (histidine acid phosphatase), Siw14 (cysteinyl phosphatase), and Aps1 (Nudix hydrolase)-are inessential for growth, Asp1/Aps1 and Aps1/Siw14 double mutations and Asp1/Siw14/Aps1 triple mutations elicit severe or lethal growth defects. By profiling the inositol pyrophosphate content of pyrophosphatase mutants in which this toxicity is genetically suppressed, we reveal the functional redundancies of the Asp1, Siw14, and Aps1 pyrophosphatases. Their synergies are manifested as excess accumulation of 1-IP 7  upon dual inactivation of Asp1 and Aps1 or an excess of 5-IP 7  in  aps1 ∆  siw14 ∆ cells. In the absence of all three pyrophosphatases, cells accrue high levels of 1,5-IP 8  and 1-IP 7  while IP 6  declines.","doi":"10.1128/mbio.00389-25","authors":"Schwer B, Prucker I, Sanchez AM, Babor J, Jessen HJ, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"16 Apr 2025","pubmed_entrez_date":"2025-04-16","publication_year":"2025","canto_session_key":"07045d4ea97ee86e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-04-16 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084874","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.62"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:41654523","title":"A role for condensin-mediator interaction in mitotic chromosome organization.","citation":"Nat Commun 2026 Feb 08;","abstract":"Condensin organizes eukaryotic genomes into three-dimensional (3D) chromosome architectures that support accurate chromosome segregation during mitosis. However, the molecular mechanisms underlying this organization remain unclear. Here, we identify a previously unrecognized interaction between the condensin subunit Cnd1 and the mediator subunit Pmc4 in fission yeast, Schizosaccharomyces pombe. We characterize a condensin mutation, cnd1-K658E, which disrupts this interaction and observe that it impairs the formation of condensin-mediated chromatin domains during mitosis, resulting in chromosome segregation defects. This condensin-mediator interaction facilitates condensin recruitment to highly transcribed genes and mitotically activated genes, the latter of which demarcate condensin-mediated domains. Moreover, 1,6-hexanediol treatment and Pmc4 mediator depletion impair expression of mitotically activated genes, diminish condensin enrichment at those boundary genes, and disrupt domain boundaries, suggesting that mediator contributes to mitotic gene expression and chromosome architecture via phase separation. Together, these results reveal a mechanism by which mitotic gene expression patterns shape condensin-mediated chromosome architecture to ensure faithful chromosome segregation.","doi":"10.1038/s41467-026-69270-x","authors":"Iwasaki O, Tashiro S, Chung CY, Hayashi T, Tanizawa H, Wang X, Ohta S, Fujioka Y, Han J, Tabor G, Kawagoe M, Marmorstein R, Noda NN, Noma KI","authors_abbrev":"Iwasaki O et al.","pubmed_publication_date":"08 Feb 2026","pubmed_entrez_date":"2026-02-07","publication_year":"2026","canto_session_key":"015af2ef93b741f1","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-02-09 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40210446","title":"Shedding Light on Telomere Replication, Insights from the Fission Yeast  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Perspect Biol 2025 Apr 10;","abstract":"Over the years, the fission yeast has become a reference model for telomere biology studies as this organism shares with mammals a highly conserved telomere composition. Here, we highlight the latest discoveries in telomere replication in fission yeast and show how this research brings new insights into the understanding of the replication and maintenance of mammalian telomeres.","doi":"10.1101/cshperspect.a041704","authors":"Coulon S","authors_abbrev":"Coulon S","pubmed_publication_date":"10 Apr 2025","pubmed_entrez_date":"2025-04-10","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-04-11 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12007420","title":"Tea3p is a cell end marker activating polarized growth in Schizosaccharomyces pombe.","citation":"Curr Biol 2002 Apr 30;12(9):751-6","abstract":"Eukaryotic cells are often polarized in their cytoplasmic structures, and this can be important for their function. The fission yeast Schizosaccharomyces pombe is a highly polarized cell that extends bipolarly along a single axis to generate a rod-shaped cell. It divides by medial fission to generate two equal-sized daughter cells that resume growth only at the old end. Once these cells have reached a particular length, they undergo NETO, new end take-off, whereby growth is activated at the other end to generate bipolarly extending cells. The activation and positioning of these growth zones are essential for maintaining growth in a straight line. Genetic analyses have identified many proteins involved in this process, like the cell end markers Tea1p and Pom1p and the kinases Orb2p/Shk1p/Pak1, Ssp1p, and Wee1p. Here, we describe tea3, a gene encoding a tea1-like protein with some similarities to ERM proteins. Tea3p is required for efficient NETO and for the proper placement of the septum. Like Pom1p, Tea3p localizes to cell ends, and its localization depends on microtubules and Tea1p. We propose that Tea3p is a novel cell end marker required specifically to activate polarized cell growth at the second end during NETO.","authors":"Arellano M, Niccoli T, Nurse P","authors_abbrev":"Arellano M et al.","pubmed_publication_date":"30 Apr 2002","pubmed_entrez_date":"2002-05-15","publication_year":"2002","canto_session_key":"49c4f596e9b38eb7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2020-06-05 10:21:35","canto_approved_date":"2025-05-19 15:57:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-05-11 13:07:35","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":16,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.11c","SPCC1223.06","SPAC6G10.02c","SPBC26H8.07c","SPCC297.03","SPCC18B5.03","SPBC1604.20c","SPBC1604.14c","SPBC336.12c","SPAC2F7.03c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2020-06-05"},{"uniquename":"PMID:19308696","title":"Condensin: Architect of mitotic chromosomes.","citation":"Chromosome Res 2009;17(2):131-44","abstract":"Condensin is a highly conserved pentameric complex consisting of two structural maintenance of chromosome (SMC) ATPase subunits and three auxiliary components. While initially regarded as a key driver of mitotic chromosome condensation, condensin is increasingly viewed as having a more subtle influence on chromosome architecture. The two condensin complexes are required to direct the correct folding and organization of chromosomes prior to anaphase and for keeping the chromosomes compact as they separate to the poles. This ancient complex is essential in mitosis and meiosis and has additional roles in gene regulation and DNA repair. The wide variety of biochemical and genetic tools available are gradually unravelling the numerous roles condensin plays during the cell cycle and shedding light on its mechanism of action.","doi":"10.1007/s10577-008-9009-7","authors":"Hudson DF, Marshall KM, Earnshaw WC","authors_abbrev":"Hudson DF et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-03-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11329175","title":"Vectors and gene targeting modules for tandem affinity purification in Schizosaccharomyces pombe.","citation":"Yeast 2001 May;18(7):657-62","abstract":"We describe the construction of tagging cassettes and plasmids for tandem affinity purification (TAP) of proteins in Schizosaccharomyces pombe. The tagging cassettes are designed for either carboxy- or amino-terminal tagging of proteins. The carboxyl terminal tags differ in that they contain either two or four repeats of IgG binding units. For tagging endogenous loci, the cassettes contain the kan MX6 module to allow for selection of G418-resistant cells. The amino-terminal tagging vectors allow for the regulated expression of proteins. Sz. pombe Cdc2p was chosen to test these new affinity tags. Several known binding proteins co-purified with both Cdc2p-CTAP and N-TAP-Cdc2p, indicating the usefulness of these tags for the rapid purification of stable protein complexes from Sz. pombe.","authors":"Tasto JJ, Carnahan RH, McDonald WH, Gould KL","authors_abbrev":"Tasto JJ et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-05-01","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC32F12.09","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU011690","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD209","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19838064","title":"Distinct Kinesin-14 mitotic mechanisms in spindle bipolarity.","citation":"Cell Cycle 2009 Nov 01;8(21):3571-83","abstract":"Kinesin-like proteins are integral to formation and function of a conserved mitotic spindle apparatus that directs chromosome segregation and precedes cell division. Ubiquitous to the mechanism of spindle assembly and stability are balanced Kinesin-5 promoting and Kinesin-14 opposing forces. Distinct Kinesin-14 roles in bipolarity in eukaryotes have not been shown, but are suggested by gamma-tubulin-based pole interactions that affect establishment and by microtubule cross-linking and sliding that maintain bipolarity and spindle length. Distinct roles also imply specialized functional domains. By cross-species analysis of compatible mechanisms in establishing mitotic bipolarity we demonstrate that Kinesin-14 human HSET (HsHSET) functionally replaces Schizosaccharomyces pombe Pkl1 and its action is similarly blocked by mutation in a Kinesin-14 binding site on gamma-tubulin. Drosophila DmNcd localizes preferentially to bundled interpolar microtubules in fission yeast and does not replace SpPkl1. Analysis of twenty-six Kinesin-14 derivatives, including Tail, Stalk or Neck-Motor chimeras, for spindle localization, spindle assembly and mitotic progression defined critical domains. The Tail of SpPkl1 contains functional elements enabling its role in spindle assembly that are distinct from but transferable to DmNcd, whereas HsHSET function utilizes both Tail and Stalk features. Our analysis is the first to demonstrate distinct mechanisms between SpPkl1 and DmNcd, and reveal that HsHSET shares functional overlap in spindle pole mechanisms.","authors":"Simeonov DR, Kenny K, Seo L, Moyer A, Allen J, Paluh JL","authors_abbrev":"Simeonov DR et al.","pubmed_publication_date":"01 Nov 2009","pubmed_entrez_date":"2009-10-20","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPAC3A11.14c"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:37542144","title":"Polymeric nature of tandemly repeated genes enhances assembly of constitutive heterochromatin in fission yeast.","citation":"Commun Biol 2023 Aug 04;6(1):796","abstract":"Motivated by our recent experiments that demonstrate that the tandemly repeated genes become heterochromatin, here we show a theory of heterochromatin assembly by taking into account the connectivity of these genes along the chromatin in the kinetic equations of small RNA production and histone methylation, which are the key biochemical reactions involved in the heterochromatin assembly. Our theory predicts that the polymeric nature of the tandemly repeated genes ensures the steady production of small RNAs because of the stable binding of nascent RNAs produced from the genes to RDRC/Dicers at the surface of nuclear membrane. This theory also predicts that the compaction of the tandemly repeated genes suppresses the production of small RNAs, consistent with our recent experiments. This theory can be extended to the small RNA-dependent gene silencing in higher organisms.","doi":"10.1038/s42003-023-05154-w","authors":"Yamamoto T, Asanuma T, Murakami Y","authors_abbrev":"Yamamoto T et al.","pubmed_publication_date":"04 Aug 2023","pubmed_entrez_date":"2023-08-04","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-08-06 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3025190","title":"Cloning and analysis of transcription of the mei2 gene responsible for initiation of meiosis in the fission yeast Schizosaccharomyces pombe.","citation":"J Bacteriol 1987 Jan;169(1):93-6","abstract":"We have isolated a hybrid plasmid, pDB(mei2)2, containing a 7.4-kilobases (kb) DNA fragment from a Schizosaccharomyces pombe genomic library which is able to complement the mei2 mutation of S. pombe. Integration of the cloned DNA sequence at the mei2 site on chromosome I demonstrated that it contained the mei2 gene. This gene was localized on a 4.7-kb HindIII-PvuII fragment in the subclone pFMV402. Transcriptional regulation was studied by Northern blot analysis in which polyadenylated RNA was prepared from a heterozygous (h+N/h-S) diploid strain cultured either in nitrogen-rich growth medium or in nitrogen-free sporulation medium. The size of the major mei2 mRNA, which always gave a broad band, was estimated to be 4.2 +/- 0.2 kb, and a few minor bands (e.g., 3.2 and 1.8 kb) appeared as well. These transcripts appeared more abundantly in sporulating cells than in growing cells. Neither the mating type genes (mat) nor the mei3 gene was essential for transcription of the mei2 gene, since ample mei2 mRNA was detected in sporulation-deficient cells transferred to sporulation medium, such as h+N/h+N and h-S/h-S homozygotes, as well as mei1 and mei3 mutants.","authors":"Shimoda C, Uehira M, Kishida M, Fujioka H, Iino Y, Watanabe Y, Yamamoto M","authors_abbrev":"Shimoda C et al.","pubmed_publication_date":"Jan 1987","pubmed_entrez_date":"1987-01-01","publication_year":"1987","canto_session_key":"f1fd9ea373dc0e13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-03-16 13:59:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-03-08 08:48:54","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.04","SPMTR.02","SPAC27D7.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-03-08"},{"uniquename":"PMID:25411338","title":"Mechanisms of expression and translocation of major fission yeast glucose transporters regulated by CaMKK/phosphatases, nuclear shuttling, and TOR.","citation":"Mol Biol Cell 2015 Jan 15;26(2):373-86","abstract":"Hexose transporters are required for cellular glucose uptake; thus they play a pivotal role in glucose homeostasis in multicellular organisms. Using fission yeast, we explored hexose transporter regulation in response to extracellular glucose concentrations. The high-affinity transporter Ght5 is regulated with regard to transcription and localization, much like the human GLUT transporters, which are implicated in diabetes. When restricted to a glucose concentration equivalent to that of human blood, the fission yeast transcriptional regulator Scr1, which represses Ght5 transcription in the presence of high glucose, is displaced from the nucleus. Its displacement is dependent on Ca(2+)/calmodulin-dependent kinase kinase, Ssp1, and Sds23 inhibition of PP2A/PP6-like protein phosphatases. Newly synthesized Ght5 locates preferentially at the cell tips with the aid of the target of rapamycin (TOR) complex 2 signaling. These results clarify the evolutionarily conserved molecular mechanisms underlying glucose homeostasis, which are essential for preventing hyperglycemia in humans.","doi":"10.1091/mbc.E14-11-1503","authors":"Saitoh S, Mori A, Uehara L, Masuda F, Soejima S, Yanagida M","authors_abbrev":"Saitoh S et al.","pubmed_publication_date":"15 Jan 2015","pubmed_entrez_date":"2014-11-21","publication_year":"2015","canto_session_key":"e2d5c2adaa68d91d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shigeaki Saitoh","canto_first_approved_date":"2017-10-20 16:57:10","canto_approved_date":"2023-11-14 13:50:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-13 17:59:28","canto_added_date":"2014-11-22 01:16:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Shigeaki Saitoh","community_curator":true,"annotation_count":18,"orcid":"0000-0001-5408-296X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4H10.09","SPBC12C2.02c","SPAC1556.08c","SPCC1235.14","SPAC1F8.01","SPCC576.15c","SPBC1D7.02c","SPBC21B10.05c","SPCC297.03","SPBC646.13","SPCC548.07c","SPCC24B10.07","SPBC30D10.10c","SPBC1683.08","SPCC548.06c","SPBC4B4.08","SPCC1235.13","SPBC1348.14c"],"gene_count":18,"ltp_gene_count":17,"approved_date":"2017-10-20"},{"uniquename":"PMID:17699595","title":"Regulation of the formin for3p by cdc42p and bud6p.","citation":"Mol Biol Cell 2007 Oct;18(10):4155-67","abstract":"Formins are conserved actin nucleators responsible for the assembly of diverse actin structures. Many formins are controlled through an autoinhibitory mechanism involving the interaction of a C-terminal DAD sequence with an N-terminal DID sequence. Here, we show that the fission yeast formin for3p, which mediates actin cable assembly and polarized cell growth, is regulated by a similar autoinhibitory mechanism in vivo. Multiple sites govern for3p localization to cell tips. The localization and activity of for3p are inhibited by an intramolecular interaction of divergent DAD and DID-like sequences. A for3p DAD mutant expressed at endogenous levels produces more robust actin cables, which appear to have normal organization and dynamics. We identify cdc42p as the primary Rho GTPase involved in actin cable assembly and for3p regulation. Both cdc42p, which binds at the N terminus of for3p, and bud6p, which binds near the C-terminal DAD-like sequence, are needed for for3p localization and full activity, but a mutation in the for3p DAD restores for3p localization and other phenotypes of cdc42 and bud6 mutants. In particular, the for3p DAD mutation suppresses the bipolar growth (NETO) defect of bud6Delta cells. These findings suggest that cdc42p and bud6p activate for3p by relieving autoinhibition.","authors":"Martin SG, Rincón SA, Basu R, Pérez P, Chang F","authors_abbrev":"Martin SG et al.","pubmed_publication_date":"Oct 2007","pubmed_entrez_date":"2007-08-19","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11057691","title":"Yeasts as a model for assessing the toxicity of the fungicides Penconazol, Cymoxanil and Dichlofluanid.","citation":"Chemosphere 2000 Nov;41(10):1637-42","abstract":"In the present work the sensitivity of yeast strains of Kluyveromyces marxianus, Pichia anomala, Candida utilis, Schizosaccharomyces pombe and Saccharomyces cerevisiae, to the fungicides cymoxanil, penconazol, and dichlofluanid, was evaluated. Dichlofluanid induced the most negative effects, whereas penconazol in general was not very toxic. Overall, our results show that the parameters IC50 for specific respiration rates of C. utilis and S. cerevisiae and C(D) for cell viability of S. cerevisiae can be applied to quantify the toxicity level of the above compounds in yeast. Hence, could be explored as an alternative or at least as a complementary test in toxicity studies and, therefore, its potential for inclusion in a tier testing toxicity test battery merits further research.","authors":"Ribeiro IC, Veríssimo I, Moniz L, Cardoso H, Sousa MJ, Soares AM, Leão C","authors_abbrev":"Ribeiro IC et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-11-01","publication_year":"2000","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33397181","title":"Connecting cell polarity signals to the cytokinetic machinery in yeast and metazoan cells.","citation":"Cell Cycle 2021 Jan;20(1):1-10","abstract":"Polarized growth and cytokinesis are two fundamental cellular processes that exist in virtually all cell types. Mechanisms for asymmetric distribution of materials allow for cells to grow in a polarized manner. This gives rise to a variety of cell shapes seen throughout all cell types. Following polarized growth during interphase, dividing cells assemble a cytokinetic ring containing the protein machinery to constrict and separate daughter cells. Here, we discuss how cell polarity signaling pathways act on cytokinesis, with a focus on direct regulation of the contractile actomyosin ring (CAR). Recent studies have exploited phosphoproteomics to identify new connections between cell polarity kinases and CAR proteins. Existing evidence suggests that some polarity kinases guide the local organization of CAR proteins and structures while also contributing to global organization of the division plane within a cell. We provide several examples of this regulation from budding yeast, fission yeast, and metazoan cells. In some cases, kinase-substrate connections point to conserved processes in these different organisms. We point to several examples where future work can indicate the degree of conservation and divergence in the cell division process of these different organisms.","doi":"10.1080/15384101.2020.1864941","authors":"Magliozzi JO, Moseley JB","authors_abbrev":"Magliozzi JO et al.","pubmed_publication_date":"Jan 2021","pubmed_entrez_date":"2021-01-05","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-01-07 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29348205","title":"Structure of the fission yeast actomyosin ring during constriction.","citation":"Proc Natl Acad Sci U S A 2018 Feb 13;115(7):E1455-E1464","abstract":"Cell division in many eukaryotes is driven by a ring containing actin and myosin. While much is known about the main proteins involved, the precise arrangement of actin filaments within the contractile machinery, and how force is transmitted to the membrane, remains unclear. Here we use cryosectioning and cryofocused ion beam milling to gain access to cryopreserved actomyosin rings in  Schizosaccharomyces pombe  for direct 3D imaging by electron cryotomography. Our results show that straight, overlapping actin filaments, running nearly parallel to each other and to the membrane, form a loose bundle of ∼150 nm in diameter that \"saddles\" the inward-bending membrane at the leading edge of the division septum. The filaments do not make direct contact with the membrane. Our analysis of the actin filaments reveals the variability in filament number, nearest-neighbor distances between filaments within the bundle, their distance from the membrane, and angular distribution with respect to the membrane.","doi":"10.1073/pnas.1711218115","authors":"Swulius MT, Nguyen LT, Ladinsky MS, Ortega DR, Aich S, Mishra M, Jensen GJ","authors_abbrev":"Swulius MT et al.","pubmed_publication_date":"13 Feb 2018","pubmed_entrez_date":"2018-01-20","publication_year":"2018","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2018-01-21 01:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2123810","title":"Isolation of a gene encoding a mitochondrial HSP70 protein from Schizosaccharomyces pombe.","citation":"Gene 1990 Oct 30;95(1):105-10","abstract":"We have isolated cDNA and genomic clones encoding a mitochondrial HSP70 protein from Schizosaccharomyces pombe. Nucleotide sequence analysis indicates that the encoded protein is homologous to the HSP70s of other organisms. The highest degree of amino acid conservation is with the proteins encoded by the Escherichia coli dnaK gene, the SSC1 gene of Saccharomyces cerevisiae and the MTP70 gene of Trypanosoma cruzi, the latter two having recently been shown to be located in the mitochondria. Western-blot analysis with immunoglobulin G raised against a peptide corresponding to the C terminus of the SSP1 protein indicates a 70-kDa protein which is associated with the mitochondria.","authors":"Powell MJ, Watts FZ","authors_abbrev":"Powell MJ et al.","pubmed_publication_date":"30 Oct 1990","pubmed_entrez_date":"1990-10-30","publication_year":"1990","canto_session_key":"ba1db8bd22527c63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-02-07 18:50:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-31 09:33:42","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-31"},{"uniquename":"EMBL:SPC03245","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8336703","title":"Centromeres of the fission yeast Schizosaccharomyces pombe are highly variable genetic loci.","citation":"Mol Cell Biol 1993 Aug;13(8):4578-87","abstract":"Gross variations in the structure of the centromere of Schizosaccharomyces pombe chromosome III (cen3) were apparent following characterization of this centromeric DNA in strain Sp223 and comparison of the structure with that of cen3 in three other commonly used laboratory strains. Further differences in centromere structure were revealed when the structure of the centromere of S. pombe chromosome II (cen2) was compared among common laboratory strains and when the structures of cen2 and cen3 from our laboratory strains were compared with those reported from other laboratories. Differences observed in cen3 structure include variations in the arrangement of the centromeric K repeats and an inverted orientation of the conserved centromeric central core. In addition, we have identified two laboratory strains that contain a minimal cen2 repeat structure that lacks the tandem copies of the cen2-specific block of K-L-B-J repeats characteristic of Sp223 cen2. We have also determined that certain centromeric DNA structural motifs are relatively conserved among the four laboratory strains and eight additional wild-type S. pombe strains isolated from various food and beverage sources. We conclude that in S. pombe, as in higher eukaryotes, the centromere of a particular chromosome is not a defined genetic locus but can contain significant variability. However, the basic DNA structural motif of a central core immediately flanked by inverted repeats is a common parameter of the S. pombe centromere.","authors":"Steiner NC, Hahnenberger KM, Clarke L","authors_abbrev":"Steiner NC et al.","pubmed_publication_date":"Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5848718","title":"Mutagen specificity among reversions of ultraviolet-induced adenine-1 mutants of Schizosaccharomyces pombe.","citation":"Genet Res 1965 Nov;6(3):433-41","abstract":"","authors":"Clarke CH","authors_abbrev":"Clarke CH","pubmed_publication_date":"Nov 1965","pubmed_entrez_date":"1965-11-01","publication_year":"1965","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24069453","title":"A reverse engineering approach to optimize experiments for the construction of biological regulatory networks.","citation":"PLoS One 2013;8(9):e75931","abstract":"One of the major objectives in systems biology is to understand the relation between the topological structures and the dynamics of biological regulatory networks. In this context, various mathematical tools have been developed to deduct structures of regulatory networks from microarray expression data. In general, from a single data set, one cannot deduct the whole network structure; additional expression data are usually needed. Thus how to design a microarray expression experiment in order to get the most information is a practical problem in systems biology. Here we propose three methods, namely, maximum distance method, trajectory entropy method, and sampling method, to derive the optimal initial conditions for experiments. The performance of these methods is tested and evaluated in three well-known regulatory networks (budding yeast cell cycle, fission yeast cell cycle, and E. coli. SOS network). Based on the evaluation, we propose an efficient strategy for the design of microarray expression experiments.","doi":"10.1371/journal.pone.0075931","authors":"Zhang X, Shao B, Wu Y, Qi O","authors_abbrev":"Zhang X et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-09-27","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10487925","title":"Gene disruption in Schizosaccharomyces pombe using a temperature-sensitive Ura4p.","citation":"Yeast 1999 Sep 15;15(12):1231-6","abstract":"We have generated a temperature-sensitive form of the Ura4p protein from the fission yeast Schizosaccharomyces pombe. A single T-to-C mutation at nucleotide 782 (relative to the initiator ATG codon of ura4) changes the leucine residue at position 261 in Ura4p to a proline. The mutant Ura4p(ts) supports growth at 30 degrees C but is unable to allow growth at 37 degrees C in the absence of uracil when a single copy of the gene is integrated into the host chromosome. Using the ura4(ts) cassette for gene replacements simplifies the identification of transformants in which the disruption construct has undergone homologous integration into the host chromosome, as these individuals contain a single copy of the ura4(ts) gene and fail to grow when replicated to 37 degrees C in the absence of uracil.","authors":"Davis K, Pateman C, Davey J","authors_abbrev":"Davis K et al.","pubmed_publication_date":"15 Sep 1999","pubmed_entrez_date":"1999-09-17","publication_year":"1999","canto_session_key":"787c309b6034127","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-17 15:30:22","canto_approved_date":"2024-04-04 11:51:01","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-02-16 21:54:15","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-17"},{"uniquename":"PMID:37220133","title":"Pervasive mRNA uridylation in fission yeast is catalysed by both Cid1 and Cid16 terminal uridyltransferases.","citation":"PLoS One 2023;18(5):e0285576","abstract":"Messenger RNA uridylation is pervasive and conserved among eukaryotes, but the consequences of this modification for mRNA fate are still under debate. Utilising a simple model organism to study uridylation may facilitate efforts to understand the cellular function of this process. Here we demonstrate that uridylation can be detected using simple bioinformatics approach. We utilise it to unravel widespread transcript uridylation in fission yeast and demonstrate the contribution of both Cid1 and Cid16, the only two annotated terminal uridyltransferases (TUT-ases) in this yeast. To detect uridylation in transcriptome data, we used a RNA-sequencing (RNA-seq) library preparation protocol involving initial linker ligation to fragmented RNA-an approach borrowed from small RNA sequencing that was commonly used in older RNA-seq protocols. We next explored the data to detect uridylation marks. Our analysis show that uridylation in yeast is pervasive, similarly to the one in multicellular organisms. Importantly, our results confirm the role of the cytoplasmic uridyltransferase Cid1 as the primary uridylation catalyst. However, we also observed an auxiliary role of the second uridyltransferase, Cid16. Thus both fission yeast uridyltransferases are involved in mRNA uridylation. Intriguingly, we found no physiological phenotype of the single and double deletion mutants of cid1 and cid16 and only minimal impact of uridylation on steady-state mRNA levels. Our work establishes fission yeast as a potent model to study uridylation in a simple eukaryote, and we demonstrate that it is possible to detect uridylation marks in RNA-seq data without the need for specific methodologies.","doi":"10.1371/journal.pone.0285576","authors":"Lipińska-Zubrycka L, Grochowski M, Bähler J, Małecki M","authors_abbrev":"Lipińska-Zubrycka L et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-05-23","publication_year":"2023","canto_session_key":"be9e49f919365c2d","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-05-24 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24350606","title":"Functional link between Rab GTPase-mediated membrane trafficking and PI4,5P2 signaling.","citation":"Genes Cells 2014 Mar;19(3):177-97","abstract":"Fission yeast its3(+) encodes an essential phosphatidylinositol-4-phosphate 5-kinase (PI4P5K) that regulates cell integrity and cytokinesis. We performed a genetic screen to identify genes that function in PI4P5K-mediated signaling, and identified gyp10(+) encoding a Rab GTPase-activating protein (GAP), a negative regulator for Rab GTPase signaling. Its3 overproduction caused growth defects and abnormal cytoplasmic accumulation of the Its3 protein, which can be stained by calcofluor. Notably, Its3 overproducing cells displayed abnormal membranous structures, multilamella Golgi and fragmented vacuoles showed by Electron microscopy. Furthermore, the excess cytoplasmic Its3 structure partly colocalized with the fluorescence of FM4-64. Gyp10 rescued both growth defects and abnormal Its3 localization when it was over-expressed. Gyp10 functionally interacted with the Rab GTPases Ypt3 and Ryh1, both of which regulate Golgi membrane trafficking. Consistently, mutation or deletion of Ypt3 and Ryh1 suppressed phenotypes associated with Its3 overproduction. Importantly, the plasma membrane localization of Its3 was also affected by the impairment of the Ypt3/Ryh1 Rab membrane trafficking, thus suggesting that membrane trafficking events regulated by two Rab GTPases functionally interacts with PI4,5P2 signaling. These results suggest a mechanism whereby PI4P5K signaling/localization is affected by Golgi membrane trafficking, thus provide a functional link between the PI4,5P2 signaling and Rab-mediated trafficking.","doi":"10.1111/gtc.12123","authors":"Li C, Kita A, Hashimoto Y, Ihara M, Kato A, Ogura N, Doi A, Oku M, Itoh T, Sakai Y, Sugiura R","authors_abbrev":"Li C et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2013-12-20","publication_year":"2014","canto_session_key":"afbaeadf37a5ea81","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.03","SPBC651.03c","SPAC4C5.02c","SPAC19G12.14"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:16787941","title":"The Schizosaccharomyces pombe septation initiation network (SIN) is required for spore formation in meiosis.","citation":"J Cell Sci 2006 Jul 15;119(Pt 14):2882-91","abstract":"When nutrients are abundant, S. pombe cells grow as rods, dividing by fission after formation of a medially placed cell wall or division septum. Septum formation is triggered by a group of proteins, called the septation initiation network or SIN, that trigger contraction of the acto-myosin contractile ring at the end of mitosis. Ectopic activation of the SIN can uncouple septum formation from other cell-cycle events, whereas loss of SIN signalling gives rise to multinucleated cells due to the failure of cytokinesis. When starved, S. pombe cells of opposite mating types fuse to form a diploid zygote that undergoes meiosis and produces four spores. No septa or contractile rings are formed during meiosis. In this study, we have investigated the role of the SIN in meiosis. Our data show that, whereas the meiotic divisions appear normal, SIN mutants cannot form spores. Forespore membrane formation is initiated, but the nuclei are not encapsulated properly. The SIN proteins localise to the spindle pole body in meiosis. The protein kinases Sid1p and Cdc7p do not associate with the spindle pole body until meiosis II, when forespore membrane deposition begins. These data indicate a role for the SIN in regulating spore formation during meiosis.","authors":"Krapp A, Collin P, Cokoja A, Dischinger S, Cano E, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"15 Jul 2006","pubmed_entrez_date":"2006-06-22","publication_year":"2006","canto_session_key":"eec560c358000716","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-04-22 11:08:43","canto_approved_date":"2025-04-22 11:08:43","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-22 11:07:47","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":26,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1565.06c","SPBC21.06c","SPCC1739.11c","SPAC9G1.09","SPBC244.01c","SPAC6F6.08c","SPBC19C2.05","SPBC428.13c","SPAC24B11.11c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2025-04-22"},{"uniquename":"PMID:12511578","title":"Identification of Uhp1, a ubiquitinated histone-like protein, as a target/mediator of Rhp6 in mating-type silencing in fission yeast.","citation":"J Biol Chem 2003 Mar 14;278(11):9185-94","abstract":"Mating-type silencing in Schizosaccharomyces pombe is brought about by cooperative interactions between cis-acting DNA sequences flanking mat2P and mat3M and the trans-acting factors, namely Swi6, Clr1-Clr4, Clr6, and Rik1. In addition, DNA repair gene rhp6, which plays a role in post-replication DNA repair and ubiquitination of proteins including histones, is also involved in silencing, albeit in a unique way; its effect on silencing and chromatin structure of the donor loci is dependent on their switching competence. Earlier, we hypothesized the existence of a mediator of Rhp6 that plays a role in reestablishment of the chromatin structure coincidentally with DNA replication associated with mating-type switching. Here we report the identification of a 22-kDa protein as an in vivo target and mediator of Rhp6 in mating-type silencing. The level of this protein is greatly elevated in sng1-1/rhp6(-) mutant and rhp6Delta as compared with wild type strain. Both the deletion and overexpression of the gene encoding this protein elicit switching-dependent loss of silencing. Furthermore, the 22-kDa protein undergoes Rhp6-dependent multiubiquitination and associates with mat2 locus during S phase in wild type cells. Interestingly, it contains a histone-fold motif similar to that of histone H2A, and like histone H2A, it interacts strongly with histone H2B in vitro. These results indicate that the 22-kDa protein, renamed as the ubiquitinated histone-like protein Uhp1, is an in vivo target/mediator of Rhp6 in silencing. Thus, regulation of association of Uhp1 with chromatin and ubiquitination followed by degradation may play a role in reestablishment of inactive chromatin structure at the silent mating-type loci.","authors":"Naresh A, Saini S, Singh J","authors_abbrev":"Naresh A et al.","pubmed_publication_date":"14 Mar 2003","pubmed_entrez_date":"2003-01-04","publication_year":"2003","canto_session_key":"7db550beef61d55f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-10 14:17:07","canto_approved_date":"2022-02-07 16:28:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-10 14:16:56","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.09","SPBC16G5.01","SPAC18B11.07c","SPMTR.01","SPBC1711.01c","SPAC3C7.14c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2016-02-10"},{"uniquename":"PMID:16611238","title":"The carboxy-terminus of Alp4 alters microtubule dynamics to induce oscillatory nuclear movement led by the spindle pole body in Schizosaccharomyces pombe.","citation":"Genes Cells 2006 Apr;11(4):337-52","abstract":"Alp4 is an essential component of the S. pombe gamma-tubulin complex. Overproduction of the carboxy-terminus of Alp4 induces oscillatory nuclear movement led by the spindle pole body (SPB). The movement is not dependent on cytoplasmic dynein dhc1, or kinesin-related proteins pkl1 and klp2. Rates of SPB movement correlate with elongation rates of microtubules (MTs) extending backwards from the moving SPB (backward-extending MTs), showing that pushing forces exerted by backward-extending MTs move the nucleus via the SPB. These backward-extending MTs are more stable than those of control cells and, thus, are able to push the SPB further towards the cell end, inducing nuclear oscillation with larger amplitudes than in control cells. SPB movement is biased towards the new end of the cell where levels of the CLIP170 homolog Tip1 increase, suggesting that the movement is related to MT-mediated cell polarity control. These results demonstrate that the carboxy-terminus of Alp4 alters MT dynamics and induces nuclear oscillation by modulating a nuclear positioning mechanism based on the balance of MT pushing forces, and suggest that regulation of gamma-tubulin complex activity is important for controlling MT dynamics and nuclear positioning.","authors":"Masuda H, Miyamoto R, Haraguchi T, Hiraoka Y","authors_abbrev":"Masuda H et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-04-14","publication_year":"2006","canto_session_key":"80821af8a094ff52","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-03 06:43:47","canto_approved_date":"2021-10-15 13:10:55","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-10-19 15:52:25","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPAC664.10","SPAC1805.08","SPAC3A11.14c","SPBC365.15","SPAC3C7.12"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2015-11-03"},{"uniquename":"PMID:18845847","title":"The mating-type-related bias of gene conversion in Schizosaccharomyces pombe.","citation":"Genetics 2008 Dec;180(4):1859-68","abstract":"The mating-type bias (mat-bias) of gene conversion was previously described as a phenomenon in which the number of prototrophic recombinants in an ura4A heteroallelic two-factor cross relates to the mating types of the parents. We show now that the mat-bias is restricted neither to ura4A nor to recombination hotspots, but occurs at other genomic loci, too. It is specific for gene conversion and absent in azygotic meiosis. Thus, the mat-bias must originate from mating-type-specific \"imprinting\" events before karyogamy takes place. Structural variations of the mating-type locus, such as h(+N), h(+S), h(-S), h(+smtDelta), or h(-smtDelta), showed mat-bias manifestation. Mutations in genes coding for histone acetylase (gcn5, ada2) and histone deacetylase (hos2, clr6) activities smooth or abolish the mat-bias. In addition, the mat-bias depends on the presence of Swi5. We propose a new role for Swi5 and the histone acetylation status in mat-bias establishment through directionality of repair from the intact chromatid to the broken chromatid.","doi":"10.1534/genetics.108.093005","authors":"Parvanov E, Kohli J, Ludin K","authors_abbrev":"Parvanov E et al.","pubmed_publication_date":"Dec 2008","pubmed_entrez_date":"2008-10-11","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11856310","title":"Biosynthesis of riboflavin: 6,7-dimethyl-8-ribityllumazine synthase of Schizosaccharomyces pombe.","citation":"Eur J Biochem 2002 Jan;269(2):519-26","abstract":"A cDNA sequence from Schizosaccharomyces pombe with similarity to 6,7-dimethyl-8-ribityllumazine synthase was expressed in a recombinant Escherichia coli strain. The recombinant protein is a homopentamer of 17-kDa subunits with an apparent molecular mass of 87 kDa as determined by sedimentation equilibrium centrifugation (it sediments at an apparent velocity of 5.0 S at 20 degrees C). The protein has been crystallized in space group C2221. The crystals diffract to a resolution of 2.4 A. The enzyme catalyses the formation of 6,7-dimethyl-8-ribityllumazine from 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione and 3,4-dihydroxy- 2-butanone 4-phosphate. Steady-state kinetic analysis afforded a vmax value of 13 000 nmol.mg-1.h-1 and Km values of 5 and 67 microm for 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione and 3,4-dihydroxy-2-butanone 4-phosphate, respectively. The enzyme binds riboflavin with a Kd of 1.2 microm. The fluorescence quantum yield of enzyme-bound riboflavin is < 2% as compared with that of free riboflavin. The protein/riboflavin complex displays an optical transition centered around 530 nm as shown by absorbance and CD spectrometry which may indicate a charge transfer complex. Replacement of tryptophan 27 by tyrosine or phenylalanine had only minor effects on the kinetic properties, but complexes of the mutant proteins did not show the anomalous long wavelength absorbance of the wild-type protein. The replacement of tryptophan 27 by aliphatic amino acids substantially reduced the affinity of the enzyme for riboflavin and for the substrate, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione.","authors":"Fischer M, Haase I, Feicht R, Richter G, Gerhardt S, Changeux JP, Huber R, Bacher A","authors_abbrev":"Fischer M et al.","pubmed_publication_date":"Jan 2002","pubmed_entrez_date":"2002-02-22","publication_year":"2002","canto_session_key":"bdba5857d73a0512","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-11-23 00:11:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-25 14:10:54","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-25"},{"uniquename":"PMID:16448511","title":"Atomic force microscopic study of the effects of ethanol on yeast cell surface morphology.","citation":"FEMS Microbiol Lett 2006 Feb;255(2):308-15","abstract":"The detrimental effects of ethanol toxicity on the cell surface morphology of Saccharomyces cerevisiae (strain NCYC 1681) and Schizosaccharomyces pombe (strain DVPB 1354) were investigated using an atomic force microscope (AFM). In combination with culture viability and mean cell volume measurements AFM studies allowed us to relate the cell surface morphological changes, observed on nanometer lateral resolution, with the cellular stress physiology. Exposing yeasts to increasing stressful concentrations of ethanol led to decreased cell viabilities and mean cell volumes. Together with the roughness and bearing volume analyses of the AFM images, the results provided novel insight into the relative ethanol tolerance of S. cerevisiae and Sc. pombe.","authors":"Canetta E, Adya AK, Walker GM","authors_abbrev":"Canetta E et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-02-02","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16153738","title":"Genome-wide analysis of HDAC function.","citation":"Trends Genet 2005 Nov;21(11):608-15","abstract":"This article focuses on new developments in the genome-wide analysis of histone deacetylase (HDAC) function in yeast. HDACs are highly conserved in many organisms; therefore, their basic functions can be investigated using experimentally tractable model organisms, such as the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe. New microarray techniques have enabled the systematic study of HDACs by identifying their direct and indirect gene targets in addition to their physiological functions and enzymatic specificity. These new approaches have already provided new surprising insights into the basic function of HDACs.","authors":"Ekwall K","authors_abbrev":"Ekwall K","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-09-13","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28855376","title":"Destabilization of the replication fork protection complex disrupts meiotic chromosome segregation.","citation":"Mol Biol Cell 2017 Nov 01;28(22):2978-2997","abstract":"The replication fork protection complex (FPC) coordinates multiple processes that are crucial for unimpeded passage of the replisome through various barriers and difficult to replicate areas of the genome. We examine the function of Swi1 and Swi3, fission yeast's primary FPC components, to elucidate how replication fork stability contributes to DNA integrity in meiosis. We report that destabilization of the FPC results in reduced spore viability, delayed replication, changes in recombination, and chromosome missegregation in meiosis I and meiosis II. These phenotypes are linked to accumulation and persistence of DNA damage markers in meiosis and to problems with cohesion stability at the centromere. These findings reveal an important connection between meiotic replication fork stability and chromosome segregation, two processes with major implications to human reproductive health.","doi":"10.1091/mbc.E17-02-0101","authors":"Escorcia W, Forsburg SL","authors_abbrev":"Escorcia W et al.","pubmed_publication_date":"01 Nov 2017","pubmed_entrez_date":"2017-09-01","publication_year":"2017","canto_session_key":"7cdc2aa6da93d713","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-03-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8334988","title":"The S. pombe cdc16 gene is required both for maintenance of p34cdc2 kinase activity and regulation of septum formation: a link between mitosis and cytokinesis?","citation":"EMBO J 1993 Jul;12(7):2697-704","abstract":"In the fission yeast Schizosaccharomyces pombe, septum formation and cytokinesis are dependent upon the initiation, though not the completion of mitosis. A number of cell cycle mutants which show phenotypes consistent with a defect in the regulation of septum formation have been isolated. A mutation in the S. pombe cdc16 gene leads to the formation of multiple septa without cytokinesis, suggesting that the normal mechanisms that limit the cell to the formation of a single septum in each cycle do not operate. Mutations in the S. pombe early septation mutants cdc7, cdc11, cdc14 and cdc15 lead to the formation of elongated, multinucleate cells, as a result of S phase and mitosis continuing in the absence of cytokinesis. This suggests that in these cells, the normal mechanisms which initiate cytokinesis are defective and that they are unable to respond to this by preventing further nuclear cycles. Genetic analysis has implied that the products of some of these genes may interact with that of the cdc16 gene. To understand how the processes of septation and cytokinesis are regulated and coordinated with mitosis we are studying the early septation mutants and cdc16. In this paper, we present the cloning and analysis of the cdc16 gene. Deletion of the gene shows that it is essential for cell proliferation: spores lacking a functional cdc16 gene germinate, complete mitosis and form multiple septa without undergoing cell cleavage.(ABSTRACT TRUNCATED AT 250 WORDS)","authors":"Fankhauser C, Marks J, Reymond A, Simanis V","authors_abbrev":"Fankhauser C et al.","pubmed_publication_date":"Jul 1993","pubmed_entrez_date":"1993-07-01","publication_year":"1993","canto_session_key":"670e6db747c0dacb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-04-04 13:01:34","canto_approved_date":"2025-09-03 10:35:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-26 16:59:47","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2018-04-04"},{"uniquename":"PMID:40931865","title":"Evolutionary diversification of the autophagy initiation complex: reduced Atg101 dependency and changes in Atg9 binding to Atg13.","citation":"Autophagy 2025 Sep 18;:1-18","abstract":"Macroautophagy/autophagy is an evolutionarily conserved process through which cells degrade cytoplasmic substances via autophagosomes. During the initiation of autophagosome formation, the ULK/Atg1 complex serves as a scaffold that recruits and regulates downstream ATG/Atg proteins and ATG9/Atg9-containing vesicles. Despite the essential role of the ULK/Atg1 complex, its components have changed during evolution; the ULK complex in mammals consists of ULK1 (or ULK2), RB1CC1, ATG13, and ATG101, whereas the Atg1 complex in the yeast  Saccharomyces cerevisiae  lacks Atg101 but instead has Atg29 and Atg31 along with Atg17. In this study, we investigated how such changes have evolved. A BLAST analysis across the major eukaryotic clades revealed that  ATG101 , which is essential for autophagy in mammals, was lost in some Holomycota lineages after acquisition of  ATG29  and  ATG31  by their common ancestor. Additionally, the acquisition of a cap structure in Atg13 preceded the loss of  ATG101 . However, some Holomycota species have both  ATG101  and  ATG29-ATG31 , including  Aspergillus oryzae  and  Komagataella phaffii . Yeast two-hybrid assays showed that ATG101 is required for ATG13-ATG9 interaction in mammals but dispensable in  A. oryzae , probably because of a shift in the  Ao Atg9-binding site in  Ao Atg13. We found an additive effect between  atg101  and  atg31  deletions in starvation-induced autophagy in  K. phaffii . Furthermore, both  Kp Atg101 and  Kp Atg31 are involved in Atg1 complex assembly in  K. phaffii . These findings suggest that the reduced importance of Atg101 in the Atg13-Atg9 interaction and Atg1 complex assembly enabled the eventual loss of  ATG101  in some Holomycota species, including  S. cerevisiae .","doi":"10.1080/15548627.2025.2559683","authors":"Lai Z, Hama Y, Oku M, Zhang S, Sakai Y, Yamamoto H, Mizushima N","authors_abbrev":"Lai Z et al.","pubmed_publication_date":"18 Sep 2025","pubmed_entrez_date":"2025-09-11","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC15D4.07c","SPAC4F10.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:25486473","title":"Regulation of wee1(+) expression during meiosis in fission yeast.","citation":"Cell Cycle 2014;13(18):2853-8","abstract":"In eukaryotes, the cyclin-dependent kinase Cdk1p (Cdc2p) plays a central role in entry into and progression through nuclear division during mitosis and meiosis. Cdk1p is activated during meiotic nuclear divisions by dephosphorylation of its tyrosine-15 residue. The phosphorylation status of this residue is largely determined by the Wee1p kinase and the Cdc25p phosphatase. In fission yeast, the forkhead-type transcription factor Mei4p is essential for entry into the first meiotic nuclear division. We recently identified cdc25(+) as an essential target of Mei4p in the control of entry into meiosis I. Here, we show that wee1(+) is another important target of Mei4p in the control of entry into meiosis I. Mei4p bound to the upstream region of wee1(+) in vivo and in vitro and inhibited expression of wee1(+), whereas Mei4p positively regulated expression of the adjacent pseudogene. Overexpression of Mei4p inhibited expression of wee1(+) and induced that of the pseudogene. Conversely, deletion of Mei4p did not decrease expression of wee1(+) but inhibited that of the pseudogene. In addition, deletion of Mei4p-binding regions delayed repression of wee1(+) expression as well as induction of expression of the pseudogene. These results suggest that repression of wee1(+) expression is primarily owing to Mei4p-mediated transcriptional interference.","doi":"10.4161/15384101.2014.946807","authors":"Murakami-Tonami Y, Ohtsuka H, Aiba H, Murakami H","authors_abbrev":"Murakami-Tonami Y et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-12-09","publication_year":"2014","canto_session_key":"90cdac452fc43744","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-12-10 01:16:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC32H8.11"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8313892","title":"The Schizosaccharomyces pombe cdc5+ gene encodes an essential protein with homology to c-Myb.","citation":"EMBO J 1994 Jan 15;13(2):471-83","abstract":"The Schizosaccharomyces pombe cdc5+ gene was identified in the first screen for cell division cycle mutants in this yeast. The cdc5+ gene was reported to be required for nuclear division but because of its modest elongation and leaky nature at the non-permissive temperature, it was not investigated further. Here, we report the characterization of the single allele of this gene, cdc5-120, in more detail. The mutant arrests with a 2N DNA content and a single interphase nucleus. Further genetic analyses suggest that cdc5+ gene function is essential in the G2 phase of the cell cycle. We have cloned and sequenced the cdc5+ gene. The deduced protein sequence predicts that Cdc5 is an 87 kDa protein and contains a region sharing significant homology with the DNA binding domain of the Myb family of transcription factors. Deletion mapping of the cdc5+ gene has shown that the N-terminal 232 amino acids of the protein, which contain the Myb-related region, are sufficient to complement the cdc5ts strain. A cdc5 null mutant was generated by homologous recombination. Haploid cells lacking cdc5+ are inviable, indicating that cdc5+ is an essential gene. A fusion protein consisting of bacterial glutathione S-transferase joined in-frame to the N-terminal 127 amino acids of the Cdc5 protein is able to bind to DNA cellulose at low salt concentrations. This evidence suggests that cdc5+ might encode a transcription factor whose activity is required for cell cycle progression and growth during G2.","authors":"Ohi R, McCollum D, Hirani B, Den Haese GJ, Zhang X, Burke JD, Turner K, Gould KL","authors_abbrev":"Ohi R et al.","pubmed_publication_date":"15 Jan 1994","pubmed_entrez_date":"1994-01-15","publication_year":"1994","canto_session_key":"bd263441cf8ed949","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-30 16:09:18","canto_approved_date":"2026-01-29 21:49:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-21 16:25:14","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC16A11.17","SPCC1739.11c","SPAC644.12","SPAC1952.07","SPBC336.12c","SPAC24H6.05"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2015-04-30"},{"uniquename":"PMID:18176550","title":"Stuttering against marginotomy.","citation":"Nat Struct Mol Biol 2008 Jan;15(1):18-9","abstract":"Stuttering by telomerase contributes to the natural heterogeneity of fission yeast telomeric repeat sequences.","doi":"10.1038/nsmb0108-18","authors":"Ares M, Chakrabarti K","authors_abbrev":"Ares M et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2008-01-08","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23231852","title":"Visualization of yeast cells by electron microscopy.","citation":"J Electron Microsc (Tokyo) 2012;61(6):343-65","abstract":"In the 1970s, hydrocarbon or methanol utilizable yeasts were considered as a material for foods and ethanol production. During the course of studies into the physiology of yeasts, we found that these systems provide a suitable model for the biogenesis and ultrastructure research of microbodies (peroxisomes). Microbodies of hydrocarbon utilizing Candida tropicalis multiply profusely from the preexisting microbody. β oxidation enzymes in the microbody were determined by means of immunoelectron microscopy. We examined the ultrastructure of Candida boidinii microbodies grown on methanol, and found a composite crystalloid of two enzymes, alcohol oxidase and catalase, by analyzing using the optical diffraction and filtering technique and computer simulation. We established methods for preparing the protoplasts of Schizosaccharomyces pombe and conditions for the complete regeneration of the cell wall. The dynamic process of cell wall formation was clarified through our study of the protoplasts, using an improved ultra high resolution (UHR) FESEM S-900 and an S-900LV. It was found that β-1,3-glucan, β-1,6-glucan and α-1,3-glucan, as well as α-galactomannan, are ingredients of the cell wall. The process of septum formation during cell division was examined after cryo-fixation by high pressure freezing (HPF). It was also found that α-1,3- and β-1,3-glucans were located in the invaginating nascent septum, and later, highly branched β-1,6-glucan also appeared on the second septum. The micro-sampling method, using a focused ion beam (FIB), has been applied to our yeast cell wall research. A combination of FIB and scanning transmission electron microscopy is useful in constructing 3D images and analyzing the molecular architecture of cells, as well as for electron tomography of thick sections of biological specimens.","doi":"10.1093/jmicro/dfs082","authors":"Osumi M","authors_abbrev":"Osumi M","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-12-13","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39565210","title":"[SNG2], a prion form of Cut4/Apc1, confers non-Mendelian inheritance of heterochromatin silencing defect in fission yeast.","citation":"Nucleic Acids Res 2024 Nov 20;","abstract":"Prions represent epigenetic regulator proteins that can self-propagate their structure and confer their misfolded structure and function on normally folded proteins. Like the mammalian prion PrPSc, prions also occur in fungi. While a few prions, like Swi1, affect gene expression, none are shown to affect heterochromatin structure and function. In fission yeast and metazoans, histone methyltransferase Clr4/Suv39 causes H3-Lys9 methylation, which is bound by the chromodomain protein Swi6/HP1 to assemble heterochromatin. Earlier, we showed that sng2-1 mutation in the Cut4 subunit of anaphase-promoting complex abrogates heterochromatin structure due to defective binding and recruitment of Swi6. Here, we demonstrate that the Cut4p forms a non-canonical prion form, designated as [SNG2], which abrogates heterochromatin silencing. [SNG2] exhibits various prion-like properties, e.g. non-Mendelian inheritance, requirement of Hsp proteins for its propagation, de novo generation upon cut4 overexpression, reversible curing by guanidine, cytoplasmic inheritance and formation of infectious protein aggregates, which are dissolved upon overexpression of hsp genes. Interestingly, [SNG2] prion imparts an enhanced tolerance to stress conditions, supporting its role in promoting cell survival under environmental stress during evolution.","doi":"10.1093/nar/gkae1136","authors":"Sharma S, Srivastava S, Dubey RN, Mishra P, Singh J","authors_abbrev":"Sharma S et al.","pubmed_publication_date":"20 Nov 2024","pubmed_entrez_date":"2024-11-20","publication_year":"2024","canto_session_key":"7ffaa76513b2dd45","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-11-22 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19056897","title":"Mid1p/anillin and the septation initiation network orchestrate contractile ring assembly for cytokinesis.","citation":"Genes Dev 2008 Nov 15;22(22):3205-16","abstract":"In both animal cells and fungi, cytokinesis proceeds via a contractile actomyosin ring (CAR). Many CAR components and regulators are evolutionarily conserved. In Schizosaccharomyces pombe, the spatial cue for cytokinesis is provided by Mid1p/Anillin, whereas temporal coordination is ensured by the septation initiation network (SIN). However, neither Mid1p nor the SIN is considered to be essential for CAR assembly per se. Here, using 4D imaging, we reveal an unanticipated, novel role for the SIN in CAR assembly. We demonstrate that CAR assembly involves three, genetically separable steps: establishment of a cortical network of CAR proteins, its lateral condensation, and finally, the formation of a homogeneous CAR. We show that SIN mutants fail to form a homogeneous CAR; we identify hypophosphorylation and recruitment of the conserved PCH-family protein Cdc15p to the CAR as critical steps requiring SIN function. Furthermore, we show that in the absence of Mid1p, CAR assembly proceeds via an actomyosin filament, rather than a cortical network of CAR proteins. This mode of assembly is totally dependent on SIN signaling, thereby demonstrating a direct role for the SIN in CAR formation. Taken together, these data establish that Mid1p and the SIN are the key regulators that orchestrate CAR assembly.","doi":"10.1101/gad.1697208","authors":"Hachet O, Simanis V","authors_abbrev":"Hachet O et al.","pubmed_publication_date":"15 Nov 2008","pubmed_entrez_date":"2008-12-06","publication_year":"2008","canto_session_key":"26d858917c4231c8","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33268381","title":"Endophilin recruitment drives membrane curvature generation through coincidence detection of GPCR loop interactions and negative lipid charge.","citation":"J Biol Chem 2021;296:100140","abstract":"Endophilin plays key roles during endocytosis of cellular receptors, including generating membrane curvature to drive internalization. Electrostatic interactions between endophilin's BIN/Amphiphysin/Rvs domain and anionic membrane lipids have been considered the major driving force in curvature generation. However, the SH3 domain of endophilin also interacts with the proline-rich third intracellular loop (TIL) of various G-protein-coupled receptors (GPCRs), and it is unclear whether this interaction has a direct role in generating membrane curvature during endocytosis. To examine this, we designed model membranes with a membrane density of 1400 receptors per μm 2  represented by a covalently conjugated TIL region from the β1-adrenergic receptor. We observed that TIL recruits endophilin to membranes composed of 95 mol% of zwitterionic lipids via the SH3 domain. More importantly, endophilin recruited via TIL tubulates vesicles and gets sorted onto highly curved membrane tubules. These observations indicate that the cellular membrane bending and curvature sensing activities of endophilin can be facilitated through detection of the TIL of activated GPCRs in addition to binding to anionic lipids. Furthermore, we show that TIL electrostatically interacts with membranes composed of anionic lipids. Therefore, anionic lipids can modulate TIL/SH3 domain binding. Overall, our findings imply that an interplay between TIL, charged membrane lipids, BAR domain, and SH3 domain could exist in the biological system and that these components may act in coordination to regulate the internalization of cellular receptors.","doi":"10.1074/jbc.RA120.016118","authors":"Mondal S, Narayan KB, Powers I, Botterbusch S, Baumgart T","authors_abbrev":"Mondal S et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2020-12-03","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1919.11","SPBC19C2.10"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:25471935","title":"The essential Schizosaccharomyces pombe Pfh1 DNA helicase promotes fork movement past G-quadruplex motifs to prevent DNA damage.","citation":"BMC Biol 2014 Dec 04;12:101","abstract":"G-quadruplexes (G4s) are stable non-canonical DNA secondary structures consisting of stacked arrays of four guanines, each held together by Hoogsteen hydrogen bonds. Sequences with the ability to form these structures in vitro, G4 motifs, are found throughout bacterial and eukaryotic genomes. The budding yeast Pif1 DNA helicase, as well as several bacterial Pif1 family helicases, unwind G4 structures robustly in vitro and suppress G4-induced DNA damage in S. cerevisiae in vivo.\nWe determined the genomic distribution and evolutionary conservation of G4 motifs in four fission yeast species and investigated the relationship between G4 motifs and Pfh1, the sole S. pombe Pif1 family helicase. Using chromatin immunoprecipitation combined with deep sequencing, we found that many G4 motifs in the S. pombe genome were associated with Pfh1. Cells depleted of Pfh1 had increased fork pausing and DNA damage near G4 motifs, as indicated by high DNA polymerase occupancy and phosphorylated histone H2A, respectively. In general, G4 motifs were underrepresented in genes. However, Pfh1-associated G4 motifs were located on the transcribed strand of highly transcribed genes significantly more often than expected, suggesting that Pfh1 has a function in replication or transcription at these sites.\nIn the absence of functional Pfh1, unresolved G4 structures cause fork pausing and DNA damage of the sort associated with human tumors.","doi":"10.1186/s12915-014-0101-5","authors":"Sabouri N, Capra JA, Zakian VA","authors_abbrev":"Sabouri N et al.","pubmed_publication_date":"04 Dec 2014","pubmed_entrez_date":"2014-12-05","publication_year":"2014","canto_session_key":"bcce385e477241ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-11-10 11:30:00","canto_approved_date":"2024-12-21 12:16:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-04 09:35:42","canto_added_date":"2014-12-06 01:15:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-11-10"},{"uniquename":"PMID:27509904","title":"The nucleolytic resolution of recombination intermediates in yeast mitotic cells.","citation":"FEMS Yeast Res 2016 Sep;16(6)","abstract":"In mitotic cells, the repair of double-strand breaks by homologous recombination (HR) is important for genome integrity. HR requires the orchestration of a subset of pathways for timely removal of joint-molecule intermediates that would otherwise prevent segregation of chromosomes in mitosis. The use of nucleases to resolve recombination intermediates is important for chromosome segregation, but is hazardous because crossovers can result in loss of heterozygosity or chromosome rearrangements. Unregulated use of the nucleases involved in the resolution of recombination intermediates could also be a risk during replication. The yeast models (Saccharomyces cerevisae and Schizosaccharomyces pombe) have proven effective in determining the major nucleases involved in the processing of such intermediates: Mus81-Mms4 and Yen1. Mus81-Mms4 and Yen1 are regulated by the cell cycle in a gradual activation during G2/M to keep the crossing-over risk low while ensuring proper removal of HJ intermediates.","doi":"10.1093/femsyr/fow065","authors":"Talhaoui I, Bernal M, Mazón G","authors_abbrev":"Talhaoui I et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-08-12","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-08-13 00:15:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11266451","title":"The Ndc80p complex from Saccharomyces cerevisiae contains conserved centromere components and has a function in chromosome segregation.","citation":"J Cell Biol 2001 Jan 22;152(2):349-60","abstract":"We have purified a complex from Saccharomyces cerevisiae containing the spindle components Ndc80p, Nuf2p, Spc25p, and Spc24p. Temperature-sensitive mutants in NDC80, SPC25, and SPC24 show defects in chromosome segregation. In spc24-1 cells, green fluorescence protein (GFP)-labeled centromeres fail to split during spindle elongation, and in addition some centromeres may detach from the spindle. Chromatin immunoprecipitation assays show an association of all four components of the complex with the yeast centromere. Homologues of Ndc80p, Nuf2p, and Spc24p were found in Schizosaccharomyces pombe and GFP tagging showed they were located at the centromere. A human homologue of Nuf2p was identified in the expressed sequence tag database. Immunofluorescent staining with anti-human Nuf2p and with anti-HEC, the human homologue of Ndc80p, showed that both proteins are at the centromeres of mitotic HeLa cells. Thus the Ndc80p complex contains centromere-associated components conserved between yeasts and vertebrates.","authors":"Wigge PA, Kilmartin JV","authors_abbrev":"Wigge PA et al.","pubmed_publication_date":"22 Jan 2001","pubmed_entrez_date":"2001-03-27","publication_year":"2001","canto_session_key":"7555bfbc9293149b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-12-19 17:21:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-19 17:21:13","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.08","SPAC27F1.04c","SPBC11C11.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-12-19"},{"uniquename":"PMID:14508607","title":"Ibp1p, a novel Cdc25-related phosphatase, suppresses Schizosaccharomyces pombe hsk1 ( cdc7).","citation":"Curr Genet 2003 Oct;44(1):38-48","abstract":"We report the identification of a novel Cdc25-like protein phosphatase, Ibp1, in the fission yeast Schizosaccharomyces pombe. Ibp1 is closely related to the catalytic subunit of the Cdc25 dual-specificity phosphatases and has phosphatase activity in vitro. Over-production of catalytically active Ibp1 robustly suppresses a mutation in the replication initiation kinase Hsk1p, a member of the Cdc7 family of protein kinases and weakly suppresses mutation of Rad4/Cut5, a DNA polymerase epsilon-associated factor. Ibp1 is not required for viability, suggesting it may be a non-essential regulator of DNA replication or chromosome structure during S phase.","authors":"Snaith HA, Marlett J, Forsburg SL","authors_abbrev":"Snaith HA et al.","pubmed_publication_date":"Oct 2003","pubmed_entrez_date":"2003-09-26","publication_year":"2003","canto_session_key":"56085db14afabbf3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-09-05 08:58:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-15 12:50:58","canto_added_date":"2012-02-24 05:50:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC839.07","SPCC338.17c","SPBC4.04c","SPCC18B5.11c","SPBC776.12c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-01-15"},{"uniquename":"PMID:22297579","title":"Quantitative live cell fluorescence-microscopy analysis of fission yeast.","citation":"J Vis Exp 2012 Jan 23;(59)","abstract":"Several microscopy techniques are available today that can detect a specific protein within the cell. During the last decade live cell imaging using fluorochromes like Green Fluorescent Protein (GFP) directly attached to the protein of interest has become increasingly popular. Using GFP and similar fluorochromes the subcellular localisations and movements of proteins can be detected in a fluorescent microscope. Moreover, also the subnuclear localisation of a certain region of a chromosome can be studied using this technique. GFP is fused to the Lac Repressor protein (LacR) and ectopically expressed in the cell where tandem repeats of the lacO sequence has been inserted into the region of interest on the chromosome. The LacR-GFP will bind to the lacO repeats and that area of the genome will be visible as a green dot in the fluorescence microscope. Yeast is especially suited for this type of manipulation since homologous recombination is very efficient and thereby enables targeted integration of the lacO repeats and engineered fusion proteins with GFP. Here we describe a quantitative method for live cell analysis of fission yeast. Additional protocols for live cell analysis of fission yeast can be found, for example on how to make a movie of the meiotic chromosomal behaviour. In this particular experiment we focus on subnuclear organisation and how it is affected during gene induction. We have labelled a gene cluster, named Chr1, by the introduction of lacO binding sites in the vicinity of the genes. The gene cluster is enriched for genes that are induced early during nitrogen starvation of fission yeast. In the strain the nuclear membrane (NM) is labelled by the attachment of mCherry to the NM protein Cut11 giving rise to a red fluorescent signal. The Spindle Pole body (SPB) compound Sid4 is fused to Red Fluorescent Protein (Sid4-mRFP). In vegetatively growing yeast cells the centromeres are always attached to the SPB that is embedded in the NM. The SPB is identified as a large round structure in the NM. By imaging before and 20 minutes after depletion of the nitrogen source we can determine the distance between the gene cluster (GFP) and the NM/SPB. The mean or median distances before and after nitrogen depletion are compared and we can thus quantify whether or not there is a shift in subcellular localisation of the gene cluster after nitrogen depletion.","doi":"10.3791/3454","authors":"Bjerling P, Olsson I, Meng X","authors_abbrev":"Bjerling P et al.","pubmed_publication_date":"23 Jan 2012","pubmed_entrez_date":"2012-02-03","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8163511","title":"p-nitrophenylphosphatase activity of plasma membrane H(+)-ATPase from yeast. Implications for the regulation of the catalytic cycle by H+.","citation":"J Biol Chem 1994 Apr 22;269(16):12074-9","abstract":"The H(+)-ATPase from Schizosaccharomyces pombe belongs to the group of transport ATPases which displays two main conformational states, E1 and E2 (P-type ATPase). In this report, we show that, as in the case of other P-type ATPase, the purified enzyme exhibits a p-nitrophenylphosphatase activity which can be completely inhibited by vanadate. In aqueous medium, p-nitrophenyl phosphate hydrolysis proceeds at only 0.5% of the rate of ATP hydrolysis, and both activities can be stimulated 3- to 4-fold by decreasing the pH from 7.5 to 6.5. Addition of the organic solvent dimethyl sulfoxide (10-40%), which has been shown to favor the E2 conformation, stimulates the p-nitrophenylphosphatase activity but inhibits the ATPase activity. At pH 7.5, the Km for p-nitrophenyl phosphate decreases when dimethyl sulfoxide is present. In the presence of 30% (v/v) dimethyl sulfoxide, the phosphatase activity can be inhibited by ATP (K(i) 300 microM) or by P(i) (K(i) 1 mM). The H(+)-ATPase incorporated into liposomes retains pNPPase activity, but it does not support H+ transport. Gel electrophoresis reveals that the pattern of H(+)-ATPase cleavage by trypsin changes when vanadate, Me2SO, or both compounds are present in the medium, regardless of the pH used during trypsinization. We propose that p-nitrophenyl phosphate is hydrolyzed by a H(+)-ATPase conformation distinct from that which hydrolyzes ATP, most probably an E2-like form. We also suggest that, in addition to the E1-E2 transition, the enzyme activity can be regulated by protons at another step of the catalytic cycle.","authors":"Ferreira-Pereira A, Alves-Ferreira M, de Carvalho-Alves PC","authors_abbrev":"Ferreira-Pereira A et al.","pubmed_publication_date":"22 Apr 1994","pubmed_entrez_date":"1994-04-22","publication_year":"1994","canto_session_key":"1c7c91f813b7b13b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-12-15 12:42:36","canto_approved_date":"2023-12-15 12:42:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-13 13:57:46","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2023-12-15"},{"uniquename":"PMID:12161753","title":"The transcriptional program of meiosis and sporulation in fission yeast.","citation":"Nat Genet 2002 Sep;32(1):143-7","abstract":"Sexual reproduction requires meiosis to produce haploid gametes, which in turn can fuse to regenerate a diploid organism. We have studied the transcriptional program that drives this developmental process in Schizosaccharomyces pombe using DNA microarrays. Here we show that hundreds of genes are regulated in successive waves of transcription that correlate with major biological events of meiosis and sporulation. Each wave is associated with specific promoter motifs. Clusters of neighboring genes (mostly close to telomeres) are co-expressed early in the process, which reflects a more global control of these genes. We find that two Atf-like transcription factors are essential for the expression of late genes and formation of spores, and identify dozens of potential Atf target genes. Comparison with the meiotic program of the distantly related Saccharomyces cerevisiae reveals an unexpectedly small shared meiotic transcriptome, suggesting that the transcriptional regulation of meiosis evolved independently in both species.","authors":"Mata J, Lyne R, Burns G, Bähler J","authors_abbrev":"Mata J et al.","pubmed_publication_date":"Sep 2002","pubmed_entrez_date":"2002-08-06","publication_year":"2002","canto_session_key":"27be9205854f1f5b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-12-16 11:13:26","canto_approved_date":"2025-12-16 11:13:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-12-16 11:13:19","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":4,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"file_curator_name":"Pascal Carme","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1000,"orcid":"0009-0003-9059-1333","file_type":"qualitative_gene_expression","file_name":"PMID_12161753_Mata_qualitative_expression.txt"}],"genes":["SPAC22A12.02c","SPAC869.06c","SPAC1039.07c","SPAC3H5.08c","SPAC10F6.15","SPAC823.16c","SPBC685.03","SPBC21C3.17c","SPCC306.03c","SPCC63.14","SPBC16G5.02c","SPBP8B7.24c","SPAC25G10.04c","SPNCRNA.587","SPAC6C3.05","SPCC1259.15c","SPCC1223.03c","SPAC23C4.12","SPAC17H9.09c","SPAC343.11c","SPCC1739.15","SPBC31F10.17c","SPCC1795.08c","SPAC1565.04c","SPBC557.03c","SPBC19C2.05","SPAC23H3.05c","SPAC3H1.03","SPBC1683.08","SPCC126.07c","SPBC1348.01","SPBC3B9.17","SPAC11D3.16c","SPBC2G2.09c","SPCC338.02","SPAC144.13c","SPBC3H7.08c","SPBC409.03","SPAC15A10.07","SPCC584.14","SPAC2E1P3.01","SPAC24H6.08","SPBC19F8.07","SPAC2H10.01","SPAC589.07c","SPAC13G7.02c","SPAC869.04","SPAC6C3.06c","SPBC56F2.06","SPAC1006.01","SPAC17C9.16c","SPBC30D10.11","SPBC1347.11","SPAC4G8.04","SPAC3G6.03c","SPCC18.01c","SPAC17A5.14","SPBC365.15","SPBPB2B2.13","SPCC1739.08c","SPAC1A6.08c","SPBC36B7.06c","SPCC663.14c","SPAC11G7.03","SPAC3A12.06c","SPBC660.11","SPCC1322.10","SPAC22G7.11c","SPCC737.04","SPBC106.08c","SPBC609.01","SPBC21B10.13c","SPAC4F10.16c","SPAPB8E5.05","SPBC3E7.12c","SPAC23H3.15c","SPBC31F10.05","SPBC17F3.01c","SPBC1105.17","SPBP19A11.02c","SPCC1450.07c","SPAC22F8.05","SPCC1322.08","SPCC1906.04","SPBC1778.10c","SPAC212.01c","SPBPB2B2.19c","SPCC285.16c","SPCC1919.06c","SPAC18G6.03","SPAC1F7.10","SPAC27E2.11c","SPAC27D7.12c","SPAC343.20","SPCC4F11.04c","SPAC1639.01c","SPCC1620.03","SPBC31A8.02","SPCC417.10","SPAC589.12","SPAC19G12.04","SPCC162.11c","SPCC553.07c","SPBP4H10.10","SPAC5D6.02c","SPAC29B12.03","SPAC4A8.02c","SPAC23C11.16","SPCC4G3.07c","SPAC922.07c","SPBC2D10.12","SPCC1902.02","SPCC4B3.13","SPAC26F1.05","SPAC3G6.07","SPAPB8E5.04c","SPBC8E4.05c","SPAC589.09","SPAC25H1.03","SPBC17D1.01","SPAC27D7.13c","SPAC29B12.13","SPCC4G3.08","SPAC3H8.09c","SPACUNK4.17","SPCC285.11","SPBC27.03","SPBC146.02","SPNCRNA.9001","SPBC13E7.06","SPCC1682.11c","SPCC1281.07c","SPBC1539.02","SPBC11C11.06c","SPCC320.07c","SPCC622.11","SPACUNK12.02c","SPBC32H8.11","SPAC23H3.11c","SPBC106.09","SPCC757.03c","SPCC330.02","SPAC212.02","SPAC186.02c","SPAC1039.03","SPAC31G5.07","SPAC2G11.04","SPCC1223.04c","SPAC750.06c","SPBC4.01","SPAC4H3.04c","SPAC959.09c","SPBC16D10.05","SPAC3A12.14","SPCC338.04","SPAC1399.02","SPAC1002.02","SPBPB2B2.10c","SPBC21.06c","SPBC1198.14c","SPBC16G5.15c","SPAC328.04","SPAC212.05c","SPCC1620.04c","SPBC660.16","SPAC24B11.05","SPAC15A10.10","SPAC1250.02","SPAC2F3.05c","SPAC30D11.01c","SPAC25B8.13c","SPAC14C4.10c","SPBC146.03c","SPAC1006.04c","SPBC1105.14","SPCC1840.05c","SPBC660.14","SPAC22F3.12c","SPBC646.03","SPBC30D10.08","SPBC651.06","SPAC3C7.13c","SPAC688.03c","SPBC36B7.02","SPCC1281.04","SPBC660.07","SPBC1289.16c","SPCC645.11c","SPAC31F12.01","SPAC22A12.13","SPAC3A11.02","SPAC1039.08","SPAC17A5.04c","SPAPB24D3.10c","SPAC630.05","SPBC119.05c","SPAC343.09","SPAC7D4.11c","SPCC16A11.04","SPBC359.06","SPAC23C11.12","SPAC29A4.12c","SPBC2G2.07c","SPCC1919.11","SPAC5D6.08c","SPAC750.02c","SPBC725.10","SPAC869.07c","SPAC1006.08","SPCC1450.01c","SPAC56E4.05","SPBC119.14","SPBC649.04","SPMIT.07","SPAC1093.06c","SPAC630.07c","SPCC1739.11c","SPBC16E9.17c","SPBC106.13","SPAC11H11.04","SPAC959.05c","SPAC1039.11c","SPAC17H9.18c","SPAC222.14c","SPAC24C9.07c","SPAPB1A11.04c","SPAC29B12.07","SPBC14F5.11c","SPBC800.14c","SPAC22F3.09c","SPAC2E1P5.02c","SPBC32H8.04c","SPAC1F8.01","SPCC306.05c","SPAC1039.06","SPBC3E7.02c","SPAC1952.09c","SPAC4F10.08","SPBC354.14c","SPCC548.06c","SPBC119.12","SPCC1442.12","SPAC1F3.09","SPCC188.03","SPAC13G7.10","SPCP31B10.06","SPBC8D2.01","SPAC22H12.01c","SPCC191.06","SPAC806.07","SPAP14E8.05c","SPAP14E8.04","SPNCRNA.17","SPBC1861.05","SPAC15A10.05c","SPBC36B7.03","SPBC21D10.08c","SPAC8F11.06","SPBC1778.03c","SPAC1002.18","SPAC458.06","SPAC1687.20c","SPAC186.04c","SPAC20G4.02c","SPAC27E2.07","SPBC1711.02","SPAC11D3.09","SPCC736.13","SPBC947.09","SPAC17G8.12","SPBP35G2.03c","SPCPJ732.02c","SPBC21D10.06c","SPBC83.11","SPCC757.07c","SPBC776.13","SPBC15D4.12c","SPAC343.12","SPBC216.02","SPAC16C9.07","SPAC22F3.02","SPBC725.12","SPCC1682.15","SPCC4F11.03c","SPBC725.02","SPBP8B7.30c","SPCC1672.03c","SPBPB2B2.01","SPAC1527.01","SPAC25B8.01","SPBC32F12.10","SPBC15C4.06c","SPAC8C9.09c","SPAC977.01","SPAC4D7.02c","SPAC11D3.17","SPMIT.05","SPAC821.08c","SPBC1683.07","SPAC29A4.05","SPBC1921.05","SPBC25B2.07c","SPBC887.12","SPAC31G5.12c","SPAC4H3.03c","SPBC27B12.06","SPAPB1A10.02","SPAC688.06c","SPAC6F6.16c","SPAC6B12.09","SPAC513.02","SPAC22F8.02c","SPAC3F10.05c","SPCC794.02","SPCC24B10.16c","SPBC1198.01","SPAPB1A10.14","SPAC31A2.03","SPAC20G4.03c","SPBC725.06c","SPCC4E9.01c","SPCC548.07c","SPBC32F12.03c","SPBP8B7.04","SPAC13C5.05c","SPCC1795.06","SPBC1685.05","SPBC2F12.15c","SPBC342.03","SPCC306.02c","SPAC105.02c","SPBC36B7.05c","SPAC24C9.15c","SPBC14C8.01c","SPCC70.04c","SPBC146.11c","SPCC1682.06","SPCC11E10.01","SPBC32H8.13c"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Tpx1 interacts with cell-surface heme transporter Str3 in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2021 Apr;115(4):699-722","abstract":"Str3 is a transmembrane protein that mediates low-affinity heme uptake in Schizosaccharomyces pombe. Under iron-limiting conditions, Str3 remains at the cell surface in the presence of increasing hemin concentrations. Using a proximity-dependent biotinylation approach coupled to mass spectrometry and coimmunoprecipitation assays, we report that the peroxiredoxin Tpx1 is a binding partner of Str3. Under microaerobic conditions, cells deficient in heme biosynthesis and lacking the heme receptor Shu1 exhibit poor hemin-dependent growth in the absence of Tpx1. Analysis of membrane protein preparations from iron-starved hem1Δ shu1Δ str3Δ tpx1Δ cells coexpressing Str3-GFP and TAP-Tpx1 showed that TAP-Tpx1 is enriched in membrane protein fractions in response to hemin. Bimolecular fluorescence complementation assays brought additional evidence that an interaction between Tpx1 and Str3 occurs at the plasma membrane. Results showed that Tpx1 exhibits an equilibrium constant value of 0.26 μM for hemin. The association of Tpx1 with hemin protects hemin from degradation by H 2  O 2  . The peroxidase activity of hemin is lowered when it is bound to Tpx1. Taken together, these results revealed that Tpx1 is a novel interacting partner of Str3. Our data are the first example of an interaction between a cytoplasmic heme-binding protein and a cell-surface heme transporter.","doi":"10.1111/mmi.14638","authors":"Normant V, Brault A, Avino M, Mourer T, Vahsen T, Beaudoin J, Labbé S","authors_abbrev":"Normant V et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2020-11-03","publication_year":"2021","canto_session_key":"c07ab0ccb8c2acb4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-11-05 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12672455","title":"UBA domain containing proteins in fission yeast.","citation":"Int J Biochem Cell Biol 2003 May;35(5):629-36","abstract":"The ubiquitin-proteasome pathway for intracellular proteolysis is involved in a series of cellular and molecular functions, including the degradation of bulk proteins, cell cycle control, DNA repair, antigen presentation, vesicle transport and the regulation of signal transudation pathways and transcription. Considering this variety of cell biological processes, it is puzzling that until recently only very few proteins were known to possess the ability to interact specifically with ubiquitin chains. However, several ubiquitin binding proteins have now been identified and the binding domains have been characterised on both the functional and structural levels. One example of a widespread ubiquitin binding module is the ubiquitin associated (UBA) domain. Here, we discuss the approximately 15 UBA domain containing proteins encoded in the relatively small genome of the fission yeast Schizosaccharomyces pombe. The proteins display remarkable differences in their domain organisation, indicating that these potential ubiquitin binding proteins are involved in various cell activities.","authors":"Hartmann-Petersen R, Semple CA, Ponting CP, Hendil KB, Gordon C","authors_abbrev":"Hartmann-Petersen R et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-04-04","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26A3.16","SPAC56F8.08","SPAC3F10.13","SPBC21D10.05c","SPAC17A5.12","SPBC83.01"],"gene_count":6,"ltp_gene_count":0},{"uniquename":"PMID:27140917","title":"Identifying Products of Recombinase-Mediated Cassette Exchange (RMCE) in Schizosaccharomyces pombe.","citation":"Cold Spring Harb Protoc 2016 May 02;2016(5)","abstract":"Homologous recombination is highly efficient when mediated between two identical target sequences by recombination enzymes such as Cre. Exploiting this, recombinase-mediated cassette exchange (RMCE) was developed for the genetic manipulation of eukaryotic cells, including those of Schizosaccharomyces pombe RMCE can be summarized in three stages: (1) A loxP-ura4(+)-loxM3 cassette is introduced into the genome using standard homologous recombination techniques to create a \"base strain.\" (2) A Cre-expression plasmid carrying a protein tag or replacement gene flanked by loxP and loxM3 is introduced into the cell. (3) Cassette exchange between the chromosomal cassette and the plasmid cassette results in either gene tagging or gene replacement. This is selected for by loss of the marker. This protocol explains how to identify the products of the exchange events in the last stage.","doi":"10.1101/pdb.prot090944","authors":"Murray JM, Watson AT, Carr AM","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"02 May 2016","pubmed_entrez_date":"2016-05-04","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-05-05 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008365","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:X04013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.128"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8643672","title":"cdc18+ regulates initiation of DNA replication in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1996 Feb 20;93(4):1566-70","abstract":"In the fission yeast Schizosaccharomyces pombe the cdc18'+gene is required both for initiation of DNA replication and for coupling mitosis to the completion of S phase. Cells lacking Cdc18 fail to enter S phase but still undergo nuclear division. Expression of cdc18+ is sufficient to drive a G1-arrested cdc10ts mutant into the S phase of the cell cycle, indicating that cdc18+ represents a critical link between passage through START and the initiation of DNA replication. Here we show that Cdcl8 is a highly unstable protein that is expressed only once per cell cycle at the boundary between GI and S phase. De novo synthesis of Cdc18 is required before, but not after, the initiation of DNA replication, indicating that Cdc18 function is not necessary once the initiation event has occurred. Overproduction of the protein results in an accumulation of cells with DNA content of greater than 2C and delays mitosis, suggesting that Cdc18 is sufficient to cause reinitiation of DNA replication within a given cell cycle. Our data indicate that the synthesis of Cdc18 protein is a critical rate-limiting step in the initiation of DNA replication during each cell cycle. The extreme lability of the protein may contribute to the prevention of reinitiation.","authors":"Muzi Falconi M, Brown GW, Kelly TJ","authors_abbrev":"Muzi Falconi M et al.","pubmed_publication_date":"20 Feb 1996","pubmed_entrez_date":"1996-02-20","publication_year":"1996","canto_session_key":"4bc1b46208b0fefe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-09-19 14:35:35","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-19 14:35:30","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-19"},{"uniquename":"EMBL:AU009232","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16469735","title":"Identification of functional domains within the septation initiation network kinase, Cdc7.","citation":"J Biol Chem 2006 Apr 14;281(15):9935-41","abstract":"The septation initiation network (SIN) serves to coordinate cytokinesis with mitotic exit in the fission yeast Schizosaccharomyces pombe. SIN components Spg1 and Cdc7 together play a central role in regulating the onset of septation and cytokinesis. Spg1, a Ras-like GTPase, localizes to the spindle pole bodies (SPBs) throughout the cell cycle. It is converted to its GTP-bound (active) state during mitosis, only to become inactivated at one SPB during anaphase and at both SPBs as cells exit mitosis. Cdc7 functions as an effector kinase for Spg1, binding to Spg1 in its GTP-bound state, and therefore is present at both SPBs during mitosis and asymmetrically at only one during anaphase. Interestingly, the kinase activity of Cdc7 does not vary across the cell cycle, suggesting the possibility that Cdc7 kinase activity is independent of Spg1 binding. Consistent with this, we found that Cdc7 associates with Spg1 only during mitosis. To learn more about the essential role of Cdc7 kinase in the SIN and its regulation, we undertook a structure/function analysis and identified independent functional domains within Cdc7. We found that a region adjacent to the kinase domain is responsible for Spg1 association and identified an overlapping but distinct SPB localization domain. In addition Cdc7 associates with itself and exists as a dimer in vivo.","authors":"Mehta S, Gould KL","authors_abbrev":"Mehta S et al.","pubmed_publication_date":"14 Apr 2006","pubmed_entrez_date":"2006-02-14","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21.06c","SPAC1565.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:29514954","title":"Assembling the mitochondrial ATP synthase.","citation":"Proc Natl Acad Sci U S A 2018 Mar 20;115(12):2850-2852","abstract":"","doi":"10.1073/pnas.1801697115","authors":"Song J, Pfanner N, Becker T","authors_abbrev":"Song J et al.","pubmed_publication_date":"20 Mar 2018","pubmed_entrez_date":"2018-03-09","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1604.11","HGNC:1188","HGNC:848","SPAC23C4.11"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8256510","title":"Comparison of the biochemical and biological functions of tyrosine phosphatases from fission yeast, budding yeast and animal cells.","citation":"Yeast 1993 Oct;9(10):1039-52","abstract":"In a previous communication, we have shown that two protein tyrosine tyrosine phosphatases (PTPases) from fission yeast, pyp1+ and pyp2+, act as novel inhibitors of mitosis upstream of the wee1+/mik1+ pathway (Ottilie et al., 1992). Here we describe that both genes possess intrinsic PTPase activity as judged by in vitro PTPase assays using 32P-labeled Raytide as a substrate, and that 32P-labeled p107wee1 is an in vitro substrate for pyp1. To compare the biological activity of pyp1 and pyp2 to that of other known PTPases, we expressed the budding yeast PTP1 and human placental phosphatase 1B (PTP1B) genes in either a cdc25-22 or wee1-50 genetic background and established that, in contrast to pyp1+ and pyp2+, Saccharomyces cerevisiae PTP1 and human PTP1B complement the cdc25 mutant, opposing the wee1+/mik1+ pathway.","authors":"Hannig G, Ottilie S, Schievella AR, Erikson RL","authors_abbrev":"Hannig G et al.","pubmed_publication_date":"Oct 1993","pubmed_entrez_date":"1993-10-01","publication_year":"1993","canto_session_key":"f0d5b32ce5baf146","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-11 19:15:35","canto_approved_date":"2020-03-06 16:49:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-04 15:50:53","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC19D5.01","SPAC26F1.10c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-12-11"},{"uniquename":"EMBL:AU013795","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29395921","title":"Repression of Cell Differentiation by a cis-Acting lincRNA in Fission Yeast.","citation":"Curr Biol 2018 Feb 05;28(3):383-391.e3","abstract":"The cell fate decision leading to gametogenesis requires the convergence of multiple signals on the promoter of a master regulator. In fission yeast, starvation-induced signaling leads to the transcriptional induction of the ste11 gene, which encodes the central inducer of mating and gametogenesis, known as sporulation. We find that the long intergenic non-coding (linc) RNA rse1 is transcribed divergently upstream of the ste11 gene. During vegetative growth, rse1 directly recruits a Mug187-Lid2-Set1 complex that mediates cis repression at the ste11 promoter through SET3C-dependent histone deacetylation. The absence of rse1 bypasses the starvation-induced signaling and induces gametogenesis in the presence of nutrients. Our data reveal that the remodeling of chromatin through ncRNA scaffolding of repressive complexes that is observed in higher eukaryotes is a conserved, likely very ancient mechanism for tight control of cell differentiation.","doi":"10.1016/j.cub.2017.12.048","authors":"Fauquenoy S, Migeot V, Finet O, Yague-Sanz C, Khorosjutina O, Ekwall K, Hermand D","authors_abbrev":"Fauquenoy S et al.","pubmed_publication_date":"05 Feb 2018","pubmed_entrez_date":"2018-02-04","publication_year":"2018","canto_session_key":"18f098a4f1ecba9a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-02-07 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.111"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11242054","title":"Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.","citation":"Nature 2001 Mar 01;410(6824):120-4","abstract":"Heterochromatin protein 1 (HP1) is localized at heterochromatin sites where it mediates gene silencing. The chromo domain of HP1 is necessary for both targeting and transcriptional repression. In the fission yeast Schizosaccharomyces pombe, the correct localization of Swi6 (the HP1 equivalent) depends on Clr4, a homologue of the mammalian SUV39H1 histone methylase. Both Clr4 and SUV39H1 methylate specifically lysine 9 of histone H3 (ref. 6). Here we show that HP1 can bind with high affinity to histone H3 methylated at lysine 9 but not at lysine 4. The chromo domain of HP1 is identified as its methyl-lysine-binding domain. A point mutation in the chromo domain, which destroys the gene silencing activity of HP1 in Drosophila, abolishes methyl-lysine-binding activity. Genetic and biochemical analysis in S. pombe shows that the methylase activity of Clr4 is necessary for the correct localization of Swi6 at centromeric heterochromatin and for gene silencing. These results provide a stepwise model for the formation of a transcriptionally silent heterochromatin: SUV39H1 places a 'methyl marker' on histone H3, which is then recognized by HP1 through its chromo domain. This model may also explain the stable inheritance of the heterochromatic state.","authors":"Bannister AJ, Zegerman P, Partridge JF, Miska EA, Thomas JO, Allshire RC, Kouzarides T","authors_abbrev":"Bannister AJ et al.","pubmed_publication_date":"01 Mar 2001","pubmed_entrez_date":"2001-03-10","publication_year":"2001","canto_session_key":"238989fa4ca1c956","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-30 15:21:39","canto_approved_date":"2025-04-17 12:49:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-28 16:37:33","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.04","SPBC1105.11c","SPAC664.01c","SPBC8D2.04","SPBC428.08c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-01-30"},{"uniquename":"PMID:22135306","title":"Identification of a core set of signature cell cycle genes whose relative order of time to peak expression is conserved across species.","citation":"Nucleic Acids Res 2012 Apr;40(7):2823-32","abstract":"A cell division cycle is a well-coordinated process in eukaryotes with cell cycle genes exhibiting a periodic expression over time. There is considerable interest among cell biologists to determine genes that are periodic in multiple organisms and whether such genes are also evolutionarily conserved in their relative order of time to peak expression. Interestingly, periodicity is not well-conserved evolutionarily. A conservative estimate of a number of periodic genes common to fission yeast (Schizosaccharomyces pombe) and budding yeast (Saccharomyces cerevisiae) ('core set FB') is 35, while those common to fission yeast and humans (Homo sapiens) ('core set FH') is 24. Using a novel statistical methodology, we discover that the relative order of peak expression is conserved in ∼80% of FB genes and in ∼40% of FH genes. We also discover that the order is evolutionarily conserved in six genes which are potentially the core set of signature cell cycle genes. These include ace2 (a transcription factor) and polo-kinase plo1, which are well-known hubs of early M-phase clusters, cdc18 a key component of pre-replication complexes, mik1 which is critical for the establishment and maintenance of DNA damage check point, and histones hhf1 and hta2.","doi":"10.1093/nar/gkr1077","authors":"Fernández MA, Rueda C, Peddada SD","authors_abbrev":"Fernández MA et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2011-12-03","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19808887","title":"Ste20-kinase-dependent TEDS-site phosphorylation modulates the dynamic localisation and endocytic function of the fission yeast class I myosin, Myo1.","citation":"J Cell Sci 2009 Nov 01;122(Pt 21):3856-61","abstract":"Type I myosins are monomeric motors involved in a range of motile and sensory activities in different cell types. In simple unicellular eukaryotes, motor activity of class I myosins is regulated by phosphorylation of a conserved 'TEDS site' residue within the motor domain. The mechanism by which this phosphorylation event affects the cellular function of each myosin I remains unclear. The fission yeast myosin I, Myo1, activates Arp2/3-dependent polymerisation of cortical actin patches and also regulates endocytosis. Using mutants and Myo1-specific antibodies, we show that the phosphorylation of the Myo1 TEDS site (serine 361) plays a crucial role in regulating this protein's dynamic localisation and cellular function. We conclude that although phosphorylation of serine 361 does not affect the ability of this motor protein to promote actin polymerisation, it is required for Myo1 to recruit to sites of endocytosis and function during this process.","doi":"10.1242/jcs.053959","authors":"Attanapola SL, Alexander CJ, Mulvihill DP","authors_abbrev":"Attanapola SL et al.","pubmed_publication_date":"01 Nov 2009","pubmed_entrez_date":"2009-10-08","publication_year":"2009","canto_session_key":"d500f4aa2dcb1642","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-31 14:25:07","canto_approved_date":"2025-12-21 11:14:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-31 14:25:02","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.13c","SPAC688.11","SPBC1604.14c","SPBC17F3.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-07-31"},{"uniquename":"PMID:28053344","title":"Histone chaperone networks shaping chromatin function.","citation":"Nat Rev Mol Cell Biol 2017 Mar;18(3):141-158","abstract":"The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational modification, nuclear import, stability, assembly and genomic localization. In this way, the chaperoning of soluble histones is a key determinant of histone availability and fate, which affects all chromosomal processes, including gene expression, chromosome segregation and genome replication and repair. Here, we review the distinct structural and functional properties of the expanding network of histone chaperones. We emphasize how chaperones cooperate in the histone chaperone network and via co-chaperone complexes to match histone supply with demand, thereby promoting proper nucleosome assembly and maintaining epigenetic information by recycling modified histones evicted from chromatin.","doi":"10.1038/nrm.2016.159","authors":"Hammond CM, Strømme CB, Huang H, Patel DJ, Groth A","authors_abbrev":"Hammond CM et al.","pubmed_publication_date":"Mar 2017","pubmed_entrez_date":"2017-01-06","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPCC364.06"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:31396577","title":"Tpz1 TPP1  prevents telomerase activation and protects telomeres by modulating the Stn1-Ten1 complex in fission yeast.","citation":"Commun Biol 2019;2:297","abstract":"In both mammalian and fission yeast cells, conserved shelterin and CST (CTC1-STN1-TEN1) complexes play critical roles in protection of telomeres and regulation of telomerase, an enzyme required to overcome the end replication problem. However, molecular details that govern proper coordination among shelterin, CST, and telomerase have not yet been fully understood. Here, we establish a conserved SWSSS motif, located adjacent to the Lys242 SUMOylation site in the fission yeast shelterin subunit Tpz1, as a new functional regulatory element for telomere protection and telomere length homeostasis. The SWSSS motif works redundantly with Lys242 SUMOylation to promote binding of Stn1-Ten1 at telomere and sub-telomere regions to protect against single-strand annealing (SSA)-dependent telomere fusions, and to prevent telomerase accumulation at telomeres. In addition, we provide evidence that the SWSSS motif defines an unanticipated role of Tpz1 in limiting telomerase activation at telomeres to prevent uncontrolled telomere elongation.","doi":"10.1038/s42003-019-0546-8","authors":"Mennie AK, Moser BA, Hoyle A, Low RS, Tanaka K, Nakamura TM","authors_abbrev":"Mennie AK et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-08-10","publication_year":"2019","canto_session_key":"b5216ed829799873","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-08-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31495586","title":"Capping Protein Insulates Arp2/3-Assembled Actin Patches from Formins.","citation":"Curr Biol 2019 Oct 07;29(19):3165-3176.e6","abstract":"How actin structures of distinct identities and functions coexist within the same environment is a critical self-organization question. Fission yeast cells have a simple actin cytoskeleton made of four structures: Arp2/3 assembles actin patches around endocytic pits, and the formins For3, Cdc12, and Fus1 assemble actin cables, the cytokinetic ring during division, and the fusion focus during sexual reproduction, respectively. The focus concentrates the delivery of hydrolases by myosin V to digest the cell wall for cell fusion. We discovered that cells lacking capping protein (CP), a heterodimer that blocks barbed-end dynamics and associates with actin patches, exhibit a delay in fusion. Consistent with CP-formin competition for barbed-end binding, Fus1, F-actin, and the linear filament marker tropomyosin hyper-accumulate at the fusion focus in cells lacking CP. CP deletion also rescues the fusion defect of a mutation in the Fus1 knob region. However, myosin V and exocytic cargoes are reduced at the fusion focus and diverted to ectopic foci, which underlies the fusion defect. Remarkably, the ectopic foci coincide with Arp2/3-assembled actin patches, which now contain low levels of Fus1. We further show that CP localization to actin patches is required to prevent the formation of ectopic foci and promote efficient cell fusion. During mitotic growth, actin patches lacking CP similarly display a dual identity, as they accumulate the formins For3 and Cdc12, normally absent from patches, and are co-decorated by the linear filament-binding protein tropomyosin and the patch marker fimbrin. Thus, CP serves to protect Arp2/3-nucleated structures from formin activity.","doi":"10.1016/j.cub.2019.07.088","authors":"Billault-Chaumartin I, Martin SG","authors_abbrev":"Billault-Chaumartin I et al.","pubmed_publication_date":"07 Oct 2019","pubmed_entrez_date":"2019-09-10","publication_year":"2019","canto_session_key":"a983b01258f7c025","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2019-10-14 14:23:19","canto_approved_date":"2022-09-23 08:11:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-21 20:42:42","canto_added_date":"2019-09-11 00:15:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":23,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":41,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.14c","SPAC27F1.02c","SPAC6F12.08c","SPAC20G4.02c","SPAC18G6.03","SPBC106.20","SPAC23D3.10c","SPBC646.06c","SPAC1F5.04c","SPAC631.01c","SPAC12B10.07","SPBC1778.06c","SPCC1919.10c","SPCC895.05"],"gene_count":14,"ltp_gene_count":6,"approved_date":"2019-10-14"},{"uniquename":"PMID:11850415","title":"Purification and characterization of the Schizosaccharomyces pombe origin recognition complex: interaction with origin DNA and Cdc18 protein.","citation":"J Biol Chem 2002 May 10;277(19):16920-7","abstract":"The origin recognition complex (ORC) plays a central role in the initiation of DNA replication in eukaryotic cells. It interacts with origins of DNA replication in chromosomal DNA and recruits additional replication proteins to form functional initiation complexes. These processes have not been well characterized at the biochemical level except in the case of Saccharomyces cerevisiae ORC. We report here the expression, purification, and initial characterization of Schizosaccharomyces pombe ORC (SpORC) containing six recombinant subunits. Purified SpORC binds efficiently to the ars1 origin of DNA replication via the essential Nterminal domain of the SpOrc4 subunit which contains nine AT-hook motifs. Competition binding experiments demonstrated that SpORC binds preferentially to DNA molecules rich in AT-tracts, but does not otherwise exhibit a high degree of sequence specificity. The complex is capable of binding to multiple sites within the ars1 origin of DNA replication with similar affinities, indicating that the sequence requirements for origin recognition in S. pombe are significantly less stringent than in S. cerevisiae. We have also demonstrated that SpORC interacts directly with Cdc18p, an essential fission yeast initiation protein, and recruits it to the ars1 origin in vitro. Recruitment of Cdc18p to chromosomal origins is a likely early step in the initiation of DNA replication in vivo. These data indicate that the purified recombinant SpORC retains at least two of its primary biological functions and that it will be useful for the eventual reconstitution of the initiation reaction with purified proteins.","authors":"Chuang RY, Chretien L, Dai J, Kelly TJ","authors_abbrev":"Chuang RY et al.","pubmed_publication_date":"10 May 2002","pubmed_entrez_date":"2002-02-19","publication_year":"2002","canto_session_key":"5a267592b8c97764","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2013-12-23 12:19:51","canto_approved_date":"2022-08-02 12:06:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-23 12:15:21","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.14c","SPBP23A10.13","SPAC3H1.01c","SPBC29A10.15","SPBC2A9.12","SPBC685.09","SPBC14C8.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2013-12-23"},{"uniquename":"PMID:28142187","title":"Spatial regulation of the KH domain RNA-binding protein Rnc1 mediated by a Crm1-independent nuclear export system in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2017 May;104(3):428-448","abstract":"RNA-binding proteins (RBPs) play important roles in the posttranscriptional regulation of gene expression, including mRNA stability, transport and translation. Fission yeast rnc1 +  encodes a K Homology (KH)-type RBP, which binds and stabilizes the Pmp1 MAPK phosphatase mRNA thereby suppressing the Cl -  hypersensitivity of calcineurin deletion and MAPK signaling mutants. Here, we analyzed the spatial regulation of Rnc1 and discovered a putative nuclear export signal (NES) Rnc1  , which dictates the cytoplasmic localization of Rnc1 in a Crm1-independent manner. Notably, mutations in the NES Rnc1  altered nucleocytoplasmic distribution of Rnc1 and abolished its function to suppress calcineurin deletion, although the Rnc1 NES mutant maintains the ability to bind Pmp1 mRNA. Intriguingly, the Rnc1 NES mutant destabilized Pmp1 mRNA, suggesting the functional importance of the Rnc1 cytoplasmic localization. Mutation in Rae1, but not Mex67 deletion or overproduction, induced Rnc1 accumulation in the nucleus, suggesting that Rnc1 is exported from the nucleus to the cytoplasm via the mRNA export pathway involving Rae1. Importantly, mutations in the Rnc1 KH-domains abolished the mRNA-binding ability and induced nuclear localization, suggesting that Rnc1 may be exported from the nucleus together with its target mRNAs. Collectively, the functional Rae1-dependent mRNA export system may influence the cytoplasmic localization and function of Rnc1.","doi":"10.1111/mmi.13636","authors":"Satoh R, Matsumura Y, Tanaka A, Takada M, Ito Y, Hagihara K, Inari M, Kita A, Fukao A, Fujiwara T, Hirai S, Tani T, Sugiura R","authors_abbrev":"Satoh R et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2017-02-01","publication_year":"2017","canto_session_key":"94b0e03380a325a5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-02 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29361524","title":"F-box proteins Pof3 and Pof1 regulate Wee1 degradation and mitotic entry in fission yeast.","citation":"J Cell Sci 2018 Feb 02;131(3)","abstract":"The key cyclin-dependent kinase Cdk1 (Cdc2) promotes irreversible mitotic entry, mainly by activating the phosphatase Cdc25 while suppressing the tyrosine kinase Wee1. Wee1 needs to be downregulated at the onset of mitosis to ensure rapid activation of Cdk1. In human somatic cells, one mechanism of suppressing Wee1 activity is mediated by ubiquitylation-dependent proteolysis through the Skp1/Cul1/F-box protein (SCF) ubiquitin E3 ligase complex. This mechanism is believed to be conserved from yeasts to humans. So far, the best-characterized human F-box proteins involved in recognition of Wee1 are β-TrCP (BTRCP) and Tome-1 (CDCA3). Although fission yeast Wee1 was the first identified member of its conserved kinase family, the F-box proteins involved in recognition and ubiquitylation of Wee1 have not been identified in this organism. In this study, our screen using Wee1- Renilla  luciferase as the reporter revealed that two F-box proteins, Pof1 and Pof3, are required for downregulating Wee1 and are possibly responsible for recruiting Wee1 to SCF. Our genetic analyses supported a functional relevance between Pof1 and Pof3 and the rate of mitotic entry, and Pof3 might play a major role in this process.","doi":"10.1242/jcs.202895","authors":"Qiu C, Yi YY, Lucena R, Wu MJ, Sun JH, Wang X, Jin QW, Wang Y","authors_abbrev":"Qiu C et al.","pubmed_publication_date":"02 Feb 2018","pubmed_entrez_date":"2018-01-24","publication_year":"2018","canto_session_key":"b48fa0fb6cc991c0","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-01-25 01:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC57A10.05c","SPCC338.16","SPBC409.05","SPAC24H6.05"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:28645196","title":"Antagonistic regulation of cyclin expression by the bZIP transcription factors Pcr1 and Atf1 during G2/M transition.","citation":"FEMS Microbiol Lett 2017 Aug 01;364(14)","abstract":"The transcription factor Atf1 is known to promote cell survival during various stress conditions in Schizosaccharomyces pombe by activating the expression of appropriate genes. It can also activate transcription of other important genes responsible for cell cycle progression. An Atf1-dependent increase in the expression of cell division promoting genes will oppose activation of checkpoints necessary to ensure repairs and cell survival during stress. Hence, selective inhibition of the cell cycle-related functions of Atf1 would be indispensable for cellular survival during stress. Here we present evidence in favour of selective inhibition of Atf1's ability to activate cdc13+ transcription. We show that the transcription factor Pcr1 can specifically inhibit the recruitment of Atf1 on cdc13 promoter and thereby prevent Atf1-mediated mitotic acceleration. We also show that this opposition of Atf1 functions by Pcr1 extends to the G1-S transition event as well. Altogether these results suggest a previously unknown antagonistic function of Atf1 and Pcr1 in regulating Cdc13 expression during cell cycle progression.","doi":"10.1093/femsle/fnx132","authors":"Bandyopadhyay S, Ghosh PM, Basu S, Paul M, Alam SB, Das E, Sundaram G","authors_abbrev":"Bandyopadhyay S et al.","pubmed_publication_date":"01 Aug 2017","pubmed_entrez_date":"2017-06-25","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC21E11.03c","SPAC24H6.05","SPBC29B5.01","SPCC18B5.03"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"EMBL:AU006959","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29205883","title":"Fission yeast Myo2: Molecular organization and diffusion in the cytoplasm.","citation":"Cytoskeleton (Hoboken) 2018 Apr;75(4):164-173","abstract":"Myosin-II is required for the assembly and constriction of cytokinetic contractile rings in fungi and animals. We used electron microscopy, fluorescence recovery after photobleaching (FRAP), and fluorescence correlation spectroscopy (FCS) to characterize the physical properties of Myo2 from fission yeast Schizosaccharomyces pombe. By electron microscopy, Myo2 has two heads and a coiled-coiled tail like myosin-II from other species. The first 65 nm of the tail is a stiff rod, followed by a flexible, less-ordered region up to 30 nm long. Myo2 sediments as a 7 S molecule in high salt, but aggregates rather than forming minifilaments at lower salt concentrations; this is unaffected by heavy chain phosphorylation. We used FRAP and FCS to observe the dynamics of Myo2 in live S. pombe cells and in cell extracts at different salt concentrations; both show that Myo2 with an N-terminal mEGFP tag has a diffusion coefficient of ∼ 3 µm 2  s -1  in the cytoplasm of live cells during interphase and mitosis. Photon counting histogram analysis of the FCS data confirmed that Myo2 diffuses as doubled-headed molecules in the cytoplasm. FCS measurements on diluted cell extracts showed that mEGFP-Myo2 has a diffusion coefficient of ∼ 30 µm 2  s -1  in 50 to 400 mM KCl concentrations.","doi":"10.1002/cm.21425","authors":"Friend JE, Sayyad WA, Arasada R, McCormick CD, Heuser JE, Pollard TD","authors_abbrev":"Friend JE et al.","pubmed_publication_date":"Apr 2018","pubmed_entrez_date":"2017-12-06","publication_year":"2018","canto_session_key":"43c0e5dc9544d3a4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-12-07 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40452482","title":"Aqueous Two-Phase System (ATPS)-Based Spore Isolation in Schizosaccharomyces pombe Requires Isp3-Dependent Surface Hydrophobicity.","citation":"Genes Cells 2025 Jul;30(4):e70029","abstract":"The fission yeast Schizosaccharomyces pombe is a valuable unicellular model organism that proliferates predominantly in the haploid state. Under nitrogen starvation, sexual reproduction occurs, resulting in the formation of a diploid zygote and subsequent meiosis, producing four haploid ascospores. The genetic tractability of yeast, particularly, its ability to produce offspring through sexual reproduction, makes it a widely used model organism. Spores also serve as a model for dormant cells. In this study, I present a highly efficient and low-cost method for purifying S. pombe spores using an aqueous two-phase system (ATPS). Using polyethylene glycol (PEG)-salt (e.g., phosphate)-based ATPS, free spores were found to partition exclusively into the upper (PEG-rich) phase. In contrast, spores lacking Isp3, which forms the outermost spore wall layer, partitioned into the lower (salt-rich) phase, like vegetative cells. This suggests that the Isp3 layer imparts hydrophobicity to the spore surface, facilitating efficient separation in ATPS. This unique surface property may also reflect differences in ecological adaptation and spore dispersal strategies between S. pombe and other fission yeast species.","doi":"10.1111/gtc.70029","authors":"Imada K","authors_abbrev":"Imada K","pubmed_publication_date":"Jul 2025","pubmed_entrez_date":"2025-06-02","publication_year":"2025","canto_session_key":"548ba87274da9df2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kazuki Imada","canto_first_approved_date":"2025-06-19 07:10:00","canto_approved_date":"2025-06-19 07:10:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-06-18 12:33:07","canto_added_date":"2025-06-02 23:25:04","annotation_curators":[{"name":"Kazuki Imada","community_curator":true,"annotation_count":2,"orcid":"0000-0002-9894-6579","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F8.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-06-19"},{"uniquename":"PMID:18321857","title":"Nonpolyadenylated RNA polymerase II termination is induced by transcript cleavage.","citation":"J Biol Chem 2008 May 16;283(20):13601-10","abstract":"Although the termination of transcription and 3' RNA processing of the eukaryotic mRNA has been linked to a polyadenylation signal and a transcript cleavage process, much less is known about the termination or processing of nonpolyadenylated RNA polymerase II transcripts. An efficiently expressed plasmid-based expression system was used to study the termination and processing of Schizosaccharomyces pombe U3 small nucleolar RNA (snoRNA) transcripts in vivo. The termination assay was linked to cell transformation, and restriction fragment length polymorphism was used to determine levels of plasmid-derived U3 snoRNA. Mutation analyses in vivo indicate that the maturation of the 3' end is not directly dependent on an external cis-acting sequence or structure; rather, it is dependent on a transcript cleavage that can occur hundreds or even thousands of nucleotides downstream of the mature U3 snoRNA sequence. Similarly, termination is dependent on the same transcript cleavage that is localized in a hairpin structure that normally follows the 3' end of the U3 snoRNA but that also can be moved hundreds or thousands of nucleotides downstream. Both processes, however, can be induced simultaneously and equally efficiently with a single unrelated Pac1 endonuclease-labile structure. The results support a \"reversed torpedoes\" model in which a single cleavage allows exonucleases and/or other protein factors access to the transcript leading to transcription termination in one direction and RNA maturation in the other direction.","doi":"10.1074/jbc.M710125200","authors":"Nabavi S, Nazar RN","authors_abbrev":"Nabavi S et al.","pubmed_publication_date":"16 May 2008","pubmed_entrez_date":"2008-03-07","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23658693","title":"Mutations disrupting histone methylation have different effects on replication timing in S. pombe centromere.","citation":"PLoS One 2013;8(5):e61464","abstract":"The fission yeast pericentromere comprises repetitive sequence elements packaged into heterchromatin marked by histone H3K9 methylation and Swi6 binding. Transient disruption of Swi6 during S phase allows a period of RNA synthesis which programs the RNAi machinery to maintain histone methylation. However, Swi6 is also required for early replication timing. We show that not only Swi6 but also the chromodomain protein Chp1 are delocalized during S phase. Different from loss of swi6, mutations that disrupt histone methylation in the centromere, chp1Δ and clr4Δ, undergo early DNA replication. However, timing is modestly delayed in RNAi mutants dcr1Δ or rdp1Δ, while hrr1Δ mutants resemble swi6Δ in their replication delay. Finally, we show that recruitment of RNA polymerase II in the centromere occurs independently of replication. These different effects indicate that replication timing is not simply linked to histone methylation.","doi":"10.1371/journal.pone.0061464","authors":"Li PC, Green MD, Forsburg SL","authors_abbrev":"Li PC et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-05-10","publication_year":"2013","canto_session_key":"370a6eba944c65e8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7748888","title":"cDNA sequence of subunit VIII of ubiquinol-cytochrome-c oxidoreductase from Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1995 May 10;1229(3):386-8","abstract":"We have cloned a cDNA coding for subunit VIII of the ubiquinol-cytochrome-c oxidoreductase of Schizosaccharomyces pombe by functional complementation of the null mutant in the QCR8 gene of Saccharomyces cerevisiae. DNA sequence analysis reveals an open-reading frame of 276 bp encoding a 10.5 kDa protein with 51% amino acid sequence identity to its counterpart in S. cerevisiae.","authors":"Boumans H, Berden JA, Grivell LA","authors_abbrev":"Boumans H et al.","pubmed_publication_date":"10 May 1995","pubmed_entrez_date":"1995-05-10","publication_year":"1995","canto_session_key":"f8bf4079ee28033f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:24:09","canto_approved_date":"2018-12-22 20:24:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 19:13:52","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1782.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:18165685","title":"Pathway of actin filament branch formation by Arp2/3 complex.","citation":"J Biol Chem 2008 Mar 14;283(11):7135-44","abstract":"A spectroscopic assay using pyrene-labeled fission yeast Arp2/3 complex revealed that the complex binds to and dissociates from actin filaments extremely slowly with or without the nucleation-promoting factor fission yeast Wsp1-VCA. Wsp1-VCA binds both Arp2/3 complex and actin monomers with high affinity. These two ligands have only modest impacts on the interaction of the other ligand with VCA. Simulations of a mathematical model based on the kinetic parameters determined in this study and elsewhere account for the full time course of actin polymerization in the presence of Arp2/3 complex and Wsp1-VCA and show that an activation step, postulated to follow binding of a ternary complex of Arp2/3 complex, a bound nucleation-promoting factor, and an actin monomer to an actin filament, has a rate constant at least 0.15 s(-1). Kinetic parameters determined in this study constrain the process of actin filament branch formation during cellular motility to one main pathway.","doi":"10.1074/jbc.M705894200","authors":"Beltzner CC, Pollard TD","authors_abbrev":"Beltzner CC et al.","pubmed_publication_date":"14 Mar 2008","pubmed_entrez_date":"2008-01-01","publication_year":"2008","canto_session_key":"8f47d042c3550bb8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-08-21 15:29:55","canto_approved_date":"2019-08-21 15:29:55","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-08-21 15:29:40","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.08c","SPAC17G8.04c","SPAC6F6.10c","SPAC11H11.06","SPAC630.03","SPAC4F10.15c","SPAC6G9.07c","SPBC14C8.06"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2019-08-21"},{"uniquename":"PMID:21813639","title":"Schizosaccharomyces pombe minichromosome maintenance-binding protein (MCM-BP) antagonizes MCM helicase.","citation":"J Biol Chem 2011 Sep 23;286(38):32918-30","abstract":"The minichromosome maintenance (MCM) complex, a replicative helicase, is a heterohexamer essential for DNA duplication and genome stability. We identified Schizosaccharomyces pombe mcb1(+) (Mcm-binding protein 1), an apparent orthologue of the human MCM-binding protein that associates with a subset of MCM complex proteins. mcb1(+) is an essential gene. Deletion of mcb1(+) caused cell cycle arrest after several generations with a cdc phenotype and disrupted nuclear structure. Mcb1 is an abundant protein, constitutively present across the cell cycle. It is widely distributed in cytoplasm and nucleoplasm and bound to chromatin. Co-immunoprecipitation suggested that Mcb1 interacts robustly with Mcm3-7 but not Mcm2. Overproduction of Mcb1 disrupted the association of Mcm2 with other MCM proteins, resulting in inhibition of DNA replication, DNA damage, and activation of the checkpoint kinase Chk1. Thus, Mcb1 appears to antagonize the function of MCM helicase.","doi":"10.1074/jbc.M111.282541","authors":"Ding L, Forsburg SL","authors_abbrev":"Ding L et al.","pubmed_publication_date":"23 Sep 2011","pubmed_entrez_date":"2011-08-05","publication_year":"2011","canto_session_key":"db0ab2817f38d5f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-02 11:37:27","canto_approved_date":"2024-11-14 09:44:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-20 09:35:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25D12.03c","SPCC1682.02c","SPBC4.04c","SPCC1259.13","SPBC211.04c","SPBC216.05","SPCC16A11.17","SPAC1B2.05","SPAC1687.04"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2017-06-02"},{"uniquename":"PMID:38132788","title":"Exploring the Molecular Underpinnings of Cancer-Causing Oncohistone Mutants Using Yeast as a Model.","citation":"J Fungi (Basel) 2023 Dec 11;9(12)","abstract":"Understanding the molecular basis of cancer initiation and progression is critical in developing effective treatment strategies. Recently, mutations in genes encoding histone proteins that drive oncogenesis have been identified, converting these essential proteins into \"oncohistones\". Understanding how oncohistone mutants, which are commonly single missense mutations, subvert the normal function of histones to drive oncogenesis requires defining the functional consequences of such changes. Histones genes are present in multiple copies in the human genome with 15 genes encoding histone H3 isoforms, the histone for which the majority of oncohistone variants have been analyzed thus far. With so many wildtype histone proteins being expressed simultaneously within the oncohistone, it can be difficult to decipher the precise mechanistic consequences of the mutant protein. In contrast to humans, budding and fission yeast contain only two or three histone H3 genes, respectively. Furthermore, yeast histones share ~90% sequence identity with human H3 protein. Its genetic simplicity and evolutionary conservation make yeast an excellent model for characterizing oncohistones. The power of genetic approaches can also be exploited in yeast models to define cellular signaling pathways that could serve as actionable therapeutic targets. In this review, we focus on the value of yeast models to serve as a discovery tool that can provide mechanistic insights and inform subsequent translational studies in humans.","doi":"10.3390/jof9121187","authors":"Zhang X, Fawwal DV, Spangle JM, Corbett AH, Jones CY","authors_abbrev":"Zhang X et al.","pubmed_publication_date":"11 Dec 2023","pubmed_entrez_date":"2023-12-22","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-12-23 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10648552","title":"The tails of two myosins.","citation":"J Cell Biol 2000 Jan 24;148(2):219-21","abstract":"","authors":"Machesky LM","authors_abbrev":"Machesky LM","pubmed_publication_date":"24 Jan 2000","pubmed_entrez_date":"2000-01-29","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28132884","title":"Novel mutation in mitochondrial Elongation Factor EF-Tu associated to dysplastic leukoencephalopathy and defective mitochondrial DNA translation.","citation":"Biochim Biophys Acta Mol Basis Dis 2017 Apr;1863(4):961-967","abstract":"The mitochondrial Elongation Factor Tu (EF-Tu), encoded by the TUFM gene, is a highly conserved GTPase, which is part of the mitochondrial protein translation machinery. In its activated form it delivers the aminoacyl-tRNAs to the A site of the mitochondrial ribosome. We report here on a baby girl with severe infantile macrocystic leukodystrophy with micropolygyria and a combined defect of complexes I and IV in muscle biopsy, caused by a novel mutation identified in TUFM. Using human mutant cells and the yeast model, we demonstrate the pathological role of the novel variant. Moreover, results of a molecular modeling study suggest that the mutant is inactive in mitochondrial polypeptide chain elongation, probably as a consequence of its reduced ability to bind mitochondrial aa-tRNAs. Four patients have so far been described with mutations in TUFM, and, following the first description of the disease in a single patient, we describe similar clinical and neuroradiological features in an additional patient.","doi":"10.1016/j.bbadis.2017.01.022","authors":"Di Nottia M, Montanari A, Verrigni D, Oliva R, Torraco A, Fernandez-Vizarra E, Diodato D, Rizza T, Bianchi M, Catteruccia M, Zeviani M, Dionisi-Vici C, Francisci S, Bertini E, Carrozzo R","authors_abbrev":"Di Nottia M et al.","pubmed_publication_date":"Apr 2017","pubmed_entrez_date":"2017-01-31","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC9B6.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38895319","title":"Laboratory horror stories: Poison in the agars.","citation":"bioRxiv 2024 Jun 06;","abstract":"","doi":"10.1101/2024.06.06.597796","authors":"Davidson MK, Protacio RU, Helmlinger D, Wahls WP","authors_abbrev":"Davidson MK et al.","pubmed_publication_date":"06 Jun 2024","pubmed_entrez_date":"2024-06-19","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-06-19 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22292001","title":"SCF ensures meiotic chromosome segregation through a resolution of meiotic recombination intermediates.","citation":"PLoS One 2012;7(1):e30622","abstract":"The SCF (Skp1-Cul1-F-box) complex contributes to a variety of cellular events including meiotic cell cycle control, but its function during meiosis is not understood well. Here we describe a novel function of SCF/Skp1 in meiotic recombination and subsequent chromosome segregation. The skp1 temperature-sensitive mutant exhibited abnormal distribution of spindle microtubules in meiosis II, which turned out to originate from abnormal bending of the spindle in meiosis I. Bent spindles were reported in mitosis of this mutant, but it remained unknown how SCF could affect spindle morphology. We found that the meiotic bent spindle in skp1 cells was due to a hypertension generated by chromosome entanglement. The spindle bending was suppressed by inhibiting double strand break (DSB) formation, indicating that the entanglement was generated by the meiotic recombination machinery. Consistently, Rhp51/Rad51-Rad22/Rad52 foci persisted until meiosis I in skp1 cells, proving accumulation of recombination intermediates. Intriguingly bent spindles were also observed in the mutant of Fbh1, an F-box protein containing the DNA helicase domain, which is involved in meiotic recombination. Genetic evidence suggested its cooperation with SCF/Skp1. Thus, SCF/Skp1 together with Fbh1 is likely to function in the resolution of meiotic recombination intermediates, thereby ensuring proper chromosome segregation.","doi":"10.1371/journal.pone.0030622","authors":"Okamoto SY, Sato M, Toda T, Yamamoto M","authors_abbrev":"Okamoto SY et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-02-01","publication_year":"2012","canto_session_key":"7c5c740e8a4e0e0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2020-02-04 10:33:12","canto_approved_date":"2026-01-31 12:34:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-03 13:20:33","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":39,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Masamitsu Sato","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.05","SPBC216.05","SPBC336.01","SPBC29A10.14","SPAC17A5.11"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-02-04"},{"uniquename":"PMID:31257143","title":"The Bub1-TPR Domain Interacts Directly with Mad3 to Generate Robust Spindle Checkpoint Arrest.","citation":"Curr Biol 2019 Jul 22;29(14):2407-2414.e7","abstract":"The spindle checkpoint monitors kinetochore-microtubule interactions and generates a \"wait anaphase\" delay when any defects are apparent [1-3]. This provides time for cells to correct chromosome attachment errors and ensure high-fidelity chromosome segregation. Checkpoint signals are generated at unattached chromosomes during mitosis. To activate the checkpoint, Mps1 Mph1  kinase phosphorylates the kinetochore component KNL1 Spc105/Spc7  on conserved MELT motifs to recruit Bub3-Bub1 complexes [4-6] via a direct Bub3 interaction with phospho-MELT motifs [7, 8]. Mps1 Mph1  then phosphorylates Bub1, which strengthens its interaction with Mad1-Mad2 complexes to produce a signaling platform [9, 10]. The Bub1-Mad1 platform is thought to recruit Mad3, Cdc20, and Mad2 to produce the mitotic checkpoint complex (MCC), which is the diffusible wait anaphase signal [9, 11, 12]. The MCC binds and inhibits the mitotic E3 ubiquitin ligase, known as Cdc20-anaphase promoting complex/cyclosome (APC/C), and stabilizes securin and cyclin to delay anaphase onset [13-17]. Here we demonstrate, in both budding and fission yeast, that kinetochores and KNL1 Spc105/Spc7  can be bypassed; simply inducing heterodimers of Mps1 Mph1  kinase and Bub1 is sufficient to trigger metaphase arrest that is dependent on Mad1, Mad2, and Mad3. We use this to dissect the domains of Bub1 necessary for arrest, highlighting the need for Bub1-CD1, which binds Mad1 [9], and Bub1's highly conserved N-terminal tetratricopeptide repeat (TPR) domain [18, 19]. We demonstrate that the Bub1 TPR domain is both necessary and sufficient to bind and recruit Mad3. We propose that this brings Mad3 into close proximity to Mad1-Mad2 and Mps1 Mph1  kinase, enabling efficient generation of MCC complexes.","doi":"10.1016/j.cub.2019.06.011","authors":"Leontiou I, London N, May KM, Ma Y, Grzesiak L, Medina-Pritchard B, Amin P, Jeyaprakash AA, Biggins S, Hardwick KG","authors_abbrev":"Leontiou I et al.","pubmed_publication_date":"22 Jul 2019","pubmed_entrez_date":"2019-07-02","publication_year":"2019","canto_session_key":"0cfe17c3c16e2b0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kevin Hardwick","canto_first_approved_date":"2019-11-14 14:03:12","canto_approved_date":"2024-04-04 17:41:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-01-18 09:08:30","canto_added_date":"2019-07-03 00:15:04","annotation_curators":[{"name":"Kevin Hardwick","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1020.02","SPBC3D6.04c","SPCC1795.01c","SPCC1322.12c","SPBC106.01","SPAC23H3.08c","SPBC14C8.01c","SPBC20F10.06"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2019-11-14"},{"uniquename":"PMID:16444015","title":"Nickel resistance in fission yeast associated with the magnesium transport system.","citation":"Mol Biotechnol 2006 Feb;32(2):139-46","abstract":"We isolated and characterized a nickel (Ni2+)-resistant mutant (GA1) of Schizosaccharomyces pombe. This mutant strain displayed resistance to both Ni2+ and Zn2+, but not to Cd2+, Co2+, and Cu2+. The growth rate of GA1 increased proportionally with increasing Mg2+ concentrations until 50 mM Mg2+. The GA1 mutation phenotype suggests a defect in Mg2+ uptake. Sequence analysis of the GA1 open reading frame (ORF) O13779, which is homologous to the prokaryotic and eukaryotic CorA Mg2+ transport systems, revealed a point mutation at codon 153 (ccc to acc) resulting in a Pro153Thr substitution in the N-terminus of the CorA domain. Our results provide novel genetic information about Ni2+ resistance in fission yeast. Specifically, that reducing Mg2+ influx through the CorA Mg2+ transport membrane protein confers Ni2+ resistance in S. pombe. We also report that Ni2+ ion detoxification of the fission yeast is related to histidine metabolism and pH.","authors":"Sarikaya AT, Akman G, Temizkan G","authors_abbrev":"Sarikaya AT et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-01-31","publication_year":"2006","canto_session_key":"affec7759847d81d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-05 17:18:41","canto_approved_date":"2023-01-26 10:28:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-29 08:40:48","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A2.14","SPBC11B10.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-09-05"},{"uniquename":"PMID:8319314","title":"Two new multi-purpose multicopy Schizosaccharomyces pombe shuttle vectors, pSP1 and pSP2.","citation":"Curr Genet 1993;23(5-6):547-8","abstract":"Plasmids pSP1 and pSP2 are two new Schizosaccharomyces pombe ars1 multicopy vectors with the Saccharomyces cerevisiae LEU2 and URA3 genes as selectable markers. They are derivatives of S. cerevisiae integrative plasmids. These plasmids allow classical molecular genetic techniques, such as mutagenesis, nested deletions and sequencing, to be performed directly.","authors":"Cottarel G, Beach D, Deuschle U","authors_abbrev":"Cottarel G et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-05-01","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38084929","title":"The cysteine-rich domain in CENP-A chaperone Scm3HJURP ensures centromere targeting and kinetochore integrity.","citation":"Nucleic Acids Res 2023 Dec 12;","abstract":"Centromeric chromatin plays a crucial role in kinetochore assembly and chromosome segregation. Centromeres are specified through the loading of the histone H3 variant CENP-A by the conserved chaperone Scm3/HJURP. The N-terminus of Scm3/HJURP interacts with CENP-A, while the C-terminus facilitates centromere localization by interacting with the Mis18 holocomplex via a small domain, called the Mis16-binding domain (Mis16-BD) in fission yeast. Fungal Scm3 proteins contain an additional conserved cysteine-rich domain (CYS) of unknown function. Here, we find that CYS binds zinc in vitro and is essential for the localization and function of fission yeast Scm3. Disrupting CYS by deletion or introduction of point mutations within its zinc-binding motif prevents Scm3 centromere localization and compromises kinetochore integrity. Interestingly, CYS alone can localize to the centromere, albeit weakly, but its targeting is greatly enhanced when combined with Mis16-BD. Expressing a truncated protein containing both Mis16-BD and CYS, but lacking the CENP-A binding domain, causes toxicity and is accompanied by considerable chromosome missegregation and kinetochore loss. These effects can be mitigated by mutating the CYS zinc-binding motif. Collectively, our findings establish the essential role of the cysteine-rich domain in fungal Scm3 proteins and provide valuable insights into the mechanism of Scm3 centromere targeting.","doi":"10.1093/nar/gkad1182","authors":"Folco HD, Xiao H, Wheeler D, Feng H, Bai Y, Grewal SIS","authors_abbrev":"Folco HD et al.","pubmed_publication_date":"12 Dec 2023","pubmed_entrez_date":"2023-12-12","publication_year":"2023","canto_session_key":"3f3654fdecbe9700","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Diego Folco","canto_first_approved_date":"2025-11-19 10:46:32","canto_approved_date":"2025-12-17 09:14:13","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-10-28 21:02:31","canto_added_date":"2023-12-13 00:25:05","annotation_curators":[{"name":"Diego Folco","community_curator":true,"annotation_count":28,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":15,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1861.01c","SPCC1672.10","SPBC18E5.03c","SPAPB1A10.02","SPBC1105.17"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2025-11-19"},{"uniquename":"PMID:40606259","title":"Comparison of Telomere Structure in Eukaryotes.","citation":"Arch Razi Inst 2024 Dec;79(6):1365-1374","abstract":"Telomeres are DNA-protein complexes that are located at the ends of eukaryotic chromosomes. The fusion of broken chromosome ends is prevented by the presence of telomeres, which act to inhibit this process. This specific function of telomeres serves to distinguish normal chromosome ends from double-stranded breaks in DNA. Telomeres contain a series of short, repeated sequences arranged in a tandem array. The number of repeats varies between different organisms, with a range of 20 to 1,000 repeats being typical. A G-rich strand is replicated by lagging strand synthesis, which creates a 3' overhang. In addition, a complementary C-rich strand is replicated by leading strand synthesis. The objective of this study is to undertake a comparative analysis of the structure of telomeres in Saccharomyces cerevisiae, Saccharomyces pombe and mammals. In Saccharomyces cerevisiae, the Rap1 protein binds to the double-stranded telomeric sequences, as well as to the Rif1 and Rif2 proteins, which regulate telomere length. Cdc13 and the Cdc13-interacting factors Ten1 and Stn1 bind to the single-stranded overhang. In Saccharomyces pombe telomeres, Taz1 binds to the double-stranded DNA (dsDNA), and Rap1 and Rif1 also bind to the ds region via Taz1. Pot1 interacts with Tpz1, forming a complex that binds to the 3' overhang. The protein Poz1 serves to connect the dsDNA binding complex, comprising Taz1 and Rap1, to the ssDNA binding complex, which includes Pot1 and Tpz1. Furthermore, Ccq1 interacts with Tpz1 and facilitates the recruitment of telomerase. The Stn1/Ten1 complex exhibits a binding affinity for a single-stranded telomere. In mammalian telomeres, the shelterin complex that binds double-stranded telomeric DNA is composed of six subunits. The double-stranded telomeric DNA is bound by TRF1 and TRF2. TPP1 and POT1 are capable of binding single-stranded DNA. TIN2 serves to connect the dsDNA binding complex TRF1/TRF2 to the ssDNA binding complex POT1/TPP1. Rap1 binds to the telomere by interacting with TRF1 and TRF2. Moreover, this study will address the regulation and comparison of the shelterin complex. Additionally, in mammals, the activation of DNA damage response pathways is necessary when double-strand DNA is broken. This, in turn, elucidates the specific repair pathways that are employed. We conclude by discussing the T-loop structure, as telomeres in several species have been shown to fold back into a structure called a T-loop, which is believed to mediate telomere protection.","doi":"10.32592/ARI.2024.79.6.1365","authors":"Mansoubi S, Mohsenpour M","authors_abbrev":"Mansoubi S et al.","pubmed_publication_date":"Dec 2024","pubmed_entrez_date":"2025-07-03","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-07-03 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7518718","title":"RNA associated with a heterodimeric protein that activates a meiotic homologous recombination hot spot: RL/RT/PCR strategy for cloning any unknown RNA or DNA.","citation":"PCR Methods Appl 1994 Apr;3(5):272-7","abstract":"The ade6-M26 mutation in the fission yeast Schizosaccharomyces pombe creates a meiotic homologous recombination hot spot. We have achieved 40,000-fold purification of a heterodimeric DNA-binding protein, Mts1/Mts2, that activates the recombination hot spot. Physical studies suggested the presence of a third subunit. It is demonstrated here that RNA molecules of approximately 210 nucleotides copurified with the heterodimer. To characterize the RNA component, it was necessary to develop a new strategy for cloning of the unknown, low-abundance, partially degraded RNAs that were present in purified Mts1/Mts2 protein preparations. The strategy uses RNA ligase to add DNA oligonucleotide priming sites to the RNA for subsequent reverse transcription and PCR (RNA ligase, reverse transcription-PCR, or RL/RT/PCR). This cloning procedure could be applied to the cloning of any unknown RNA or DNA molecules. Because the cDNA clones obtained from Mts1/Mts2 were largely heterogeneous, it seems likely that the RNAs copurified as a result of tight but nonspecific interactions with the heterodimeric protein.","authors":"Wahls WP","authors_abbrev":"Wahls WP","pubmed_publication_date":"Apr 1994","pubmed_entrez_date":"1994-04-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:16775007","title":"Ppc89 links multiple proteins, including the septation initiation network, to the core of the fission yeast spindle-pole body.","citation":"Mol Biol Cell 2006 Sep;17(9):3793-805","abstract":"The spindle-pole body (SPB), the yeast analog of the centrosome, serves as the major microtubule (MT) organizing center in the yeast cell. In addition to this central function, the SPB organizes and concentrates proteins required for proper coordination between the nuclear-division cycle and cytokinesis. For example, the Schizosaccharomyces pombe septation-initiation network (SIN), which is responsible for initiating actomyosin ring constriction and septation, is assembled at the SPB through its two scaffolding components, Sid4 and Cdc11. In an effort to identify novel SIN interactors, we purified Cdc11 and identified by mass spectrometry a previously uncharacterized protein associated with it, Ppc89. Ppc89 localizes constitutively to the SPB and interacts directly with Sid4. A fusion between the N-terminal 300 amino acids of Sid4 and a SPB targeting domain of Ppc89 supplies the essential function of Sid4 in anchoring the SIN. ppc89Delta cells are inviable and exhibit defects in SPB integrity, and hence in spindle formation, chromosome segregation, and SIN localization. Ppc89 overproduction is lethal, resulting primarily in a G2 arrest accompanied by massive enlargement of the SPB and increased SPB MT nucleation. These results suggest a fundamental role for Ppc89 in organization of the S. pombe SPB.","authors":"Rosenberg JA, Tomlin GC, McDonald WH, Snydsman BE, Muller EG, Yates JR, Gould KL","authors_abbrev":"Rosenberg JA et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-06-16","publication_year":"2006","canto_session_key":"574df5dbdb6edf7f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-12 18:23:02","canto_approved_date":"2020-12-29 07:40:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-07 14:15:55","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPAC4H3.11c","SPCC1739.11c","SPAC6G9.06c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-03-12"},{"uniquename":"PMID:18162174","title":"Gpx1 is a stationary phase-specific thioredoxin peroxidase in fission yeast.","citation":"Biochem Biophys Res Commun 2008 Feb 29;367(1):67-71","abstract":"The genome sequence of Schizosaccharomyces pombe reveals only one gene for a putative glutathione peroxidase (gpx1(+)). The Gpx1 protein has a peroxidase activity but preferred thioredoxin to glutathione as an electron donor when examined in vitro and in vivo, and therefore is a thioredoxin peroxidase. Besides H(2)O(2), it can reduce alkyl and phospholipid hydroperoxides. Expression of the gpx1 gene was elevated at the stationary phase, and we found that it supported long-term survival of S. pombe. The mutant also exhibited some defect in the activity of aconitase, an oxidation-labile Fe-S enzyme in mitochondria. Activity of sulfite reductase, a labile Fe-S enzyme in the cytosol, was also dramatically lowered in the mutant in the stationary phase. The Gpx1 protein, without any obvious targeting sequence, was localized in mitochondria as well as in the cytosol. Therefore, Gpx1 must serve to ensure optimal mitochondrial function and cytosolic environment, especially in the stationary phase.","authors":"Lee SY, Song JY, Kwon ES, Roe JH","authors_abbrev":"Lee SY et al.","pubmed_publication_date":"29 Feb 2008","pubmed_entrez_date":"2007-12-29","publication_year":"2008","canto_session_key":"50906198d7f94a7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-07-27 07:48:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-30 10:17:04","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.03c","SPBC12D12.07c","SPAC7D4.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-10-30"},{"uniquename":"EMBL:AU007197","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17304215","title":"Fission yeast Swi5/Sfr1 and Rhp55/Rhp57 differentially regulate Rhp51-dependent recombination outcomes.","citation":"EMBO J 2007 Mar 07;26(5):1352-62","abstract":"Several accessory proteins referred to as mediators are required for the full activity of the Rad51 (Rhp51 in fission yeast) recombinase. In this study, we analyzed in vivo functions of the recently discovered Swi5/Sfr1 complex from fission yeast. In normally growing cells, the Swi5-GFP protein localizes to the nucleus, where it forms a diffuse nuclear staining pattern with a few distinct foci. These spontaneous foci do not form in swi2Delta mutants. Upon UV irradiation, Swi5 focus formation is induced in swi2Delta mutants, a response that depends on Sfr1 function, and Sfr1 also forms foci that colocalize with damage-induced Rhp51 foci. The number of UV-induced Rhp51 foci is partially reduced in swi5Delta and rhp57Delta mutants and completely abolished in an swi5Delta rhp57Delta double mutant. An assay for products generated by HO endonuclease-induced DNA double-strand breaks (DSBs) reveals that Rhp51 and Rhp57, but not Swi5/Sfr1, are essential for crossover production. These results suggest that Swi5/Sfr1 functions as an Rhp51 mediator but processes DSBs in a manner different from that of the Rhp55/57 mediator.","authors":"Akamatsu Y, Tsutsui Y, Morishita T, Siddique MS, Kurokawa Y, Ikeguchi M, Yamao F, Arcangioli B, Iwasaki H","authors_abbrev":"Akamatsu Y et al.","pubmed_publication_date":"07 Mar 2007","pubmed_entrez_date":"2007-02-17","publication_year":"2007","canto_session_key":"c1083ee2230b687c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-03-21 08:00:14","canto_approved_date":"2024-03-21 08:00:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-15 18:02:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC144.13c","SPAC1142.03c","SPAC20H4.07","SPBC28F2.07","SPAC15A10.03c","SPBC409.03"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2024-03-21"},{"uniquename":"PMID:41717013","title":"The microcephaly-associated protein YIPF5 differentially regulates ER export.","citation":"iScience 2026 Feb 20;29(2):114791","abstract":"YIPF5 is an ER-membrane protein implicated in ER-Golgi transport. Mutations in YIPF5 cause MEDS2 (microcephaly, epilepsy, and neonatal diabetes syndrome), a fatal disorder manifesting in early childhood. We demonstrate that YIPF5 is involved in ER export of a subset of proteins, including cargoes of the ER export receptor SURF4, with which it directly interacts. YIPF5 knockout cells display altered cell surface and secretome profiles, with reduced neuronal adhesion molecules and increased secretion of ER chaperones affecting migration. YIPF5 depletion enhances cell migration in a wound-healing assay and alters SURF4 localization, causing elongated ERGIC53- and Rab1-positive tubules from ER exit sites. Kinetic analysis suggests that YIPF5 negatively regulates SURF4-mediated ER export.  In utero  knockdown of  Yipf5  in embryonic mouse brains induces premature neuronal migration and abnormal neuronal morphology. Our findings suggest that YIPF5 and SURF4 coordinate ER export of key proteins and disruption may underlie cortical development defects leading to microcephaly.","doi":"10.1016/j.isci.2026.114791","authors":"Bruno F, Anitei M, Di Fraia D, Durso W, Dau T, Cirri E, Sannai M, Valkova C, Maldutyte J, Miller EA, Rubio I, Garloff V, Kersten N, Farias GG, Ori A, Mestres I, Calegari F, Kaether C","authors_abbrev":"Bruno F et al.","pubmed_publication_date":"20 Feb 2026","pubmed_entrez_date":"2026-02-20","publication_year":"2026","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC61.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU010333","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18692073","title":"The transition from differential equations to Boolean networks: a case study in simplifying a regulatory network model.","citation":"J Theor Biol 2008 Dec 07;255(3):269-77","abstract":"Methods for modeling cellular regulatory networks as diverse as differential equations and Boolean networks co-exist, however, without much closer correspondence to each other. With the example system of the fission yeast cell cycle control network, we here discuss these two approaches with respect to each other. We find that a Boolean network model can be formulated as a specific coarse-grained limit of the more detailed differential equations model for this system. This demonstrates the mathematical foundation on which Boolean networks can be applied to biological regulatory networks in a controlled way.","doi":"10.1016/j.jtbi.2008.07.020","authors":"Davidich M, Bornholdt S","authors_abbrev":"Davidich M et al.","pubmed_publication_date":"07 Dec 2008","pubmed_entrez_date":"2008-08-12","publication_year":"2008","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40162989","title":"Phosphorylation of the Aly3 C-terminus impedes aberrant endocytosis of Schizosaccharomyces pombe hexose transporter Ght5.","citation":"J Cell Sci 2025 Mar 31;","abstract":"In fission yeast, Schizosaccharomyces pombe, transcriptional upregulation and cell-surface localization of the hexose transporter, Ght5, are required for cell proliferation in low glucose. As the target of rapamycin complex 2 (TORC2) signaling pathway inhibits α-arrestin Aly3-dependent endocytosis of Ght5, we hypothesized that phosphorylation inhibits this endocytosis. To identify phosphorylation sites required for proliferation in low glucose, putatively phosphorylated serine/threonine residues of Aly3 and Ght5 were replaced with alanine. C-terminal serine residues of Aly3, but not Ght5, were necessary for proliferation in low glucose. Expression of Aly3 unphosphorylated at the C-terminus led to increased ubiquitination and vacuolar accumulation of Ght5 in low glucose, but reversion of one of the alanine residues to serine reversed those defects. Also, Aly3 physically interacted with the HECT-type ubiquitin ligases, Pub1 and Pub3, and these interactions were required for surface localization of Ght5 and proliferation in low glucose. This study reveals mechanisms by which Aly3 is regulated so that fission yeast can adapt to nutritional stress.","doi":"10.1242/jcs.263572","authors":"Toyoda Y, Masuda F, Saitoh S","authors_abbrev":"Toyoda Y et al.","pubmed_publication_date":"31 Mar 2025","pubmed_entrez_date":"2025-03-31","publication_year":"2025","canto_session_key":"f071e3683fe60802","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-04-01 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008736","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32053662","title":"AMPKα Subunit Ssp2 and Glycogen Synthase Kinases Gsk3/Gsk31 are involved in regulation of sterol regulatory element-binding protein (SREBP) activity in fission yeast.","citation":"PLoS One 2020;15(2):e0228845","abstract":"Sterol regulatory element-binding protein (SREBP), a highly conserved family of membrane-bound transcription factors, is an essential regulator for cellular cholesterol and lipid homeostasis in mammalian cells. Sre1, the homolog of SREBP in the fission yeast Schizosaccharomyces pombe (S. pombe), regulates genes involved in the transcriptional responses to low sterol as well as low oxygen. Previous study reported that casein kinase 1 family member Hhp2 phosphorylated the Sre1 N-terminal transcriptional factor domain (Sre1N) and accelerated Sre1N degradation, and other kinases might exist for regulating the Sre1 function. To gain insight into the mechanisms underlying the Sre1 activity and to identify additional kinases involved in regulation of Sre1 function, we developed a luciferase reporter system to monitor the Sre1 activity through its binding site called SRE2 in living yeast cells. Here we showed that both ergosterol biosynthesis inhibitors and hypoxia-mimic CoCl2 caused a dose-dependent increase in the Sre1 transcription activity, concurrently, these induced transcription activities were almost abolished in Δsre1 cells. Surprisingly, either AMPKα Subunit Ssp2 deletion or Glycogen Synthase Kinases Gsk3/Gsk31 double deletion significantly suppressed ergosterol biosynthesis inhibitors- or CoCl2-induced Sre1 activity. Notably, the Δssp2Δgsk3Δgsk31 mutant showed further decreased Sre1 activity when compared with their single or double deletion. Consistently, the Δssp2Δgsk3Δgsk31 mutant showed more marked temperature sensitivity than any of their single or double deletion. Moreover, the fluorescence of GFP-Sre1N localized at the nucleus in wild-type cells, but significantly weaker nuclear fluorescence of GFP-Sre1N was observed in Δssp2, Δgsk3Δgsk31, Δssp2Δgsk3, Δssp2Δgsk31 or Δssp2Δgsk3Δgsk31 cells. On the other hand, the immunoblot showed a dramatic decrease in GST-Sre1N levels in the Δgsk3Δgsk31 or the Δssp2Δgsk3Δgsk31 cells but not in the Δssp2 cells. Altogether, our findings suggest that Gsk3/Gsk31 may regulate Sre1N degradation, while Ssp2 may regulate not only the degradation of Sre1N but also its translocation to the nucleus.","doi":"10.1371/journal.pone.0228845","authors":"Miao H, Liu Q, Jiang G, Zhang W, Liu K, Gao X, Huo Y, Chen S, Kato T, Sakamoto N, Kuno T, Fang Y","authors_abbrev":"Miao H et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-02-14","publication_year":"2020","canto_session_key":"b8a8ea77ee8fb109","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yue Fang","canto_first_approved_date":"2020-04-08 15:11:13","canto_approved_date":"2020-04-08 15:11:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-23 18:05:08","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yue Fang","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.12","SPBC8D2.01","SPCC74.03c","SPAC1687.15","SPBC19C2.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2020-04-08"},{"uniquename":"PMID:28049777","title":"Preparing Fission Yeast for Electron Microscopy.","citation":"Cold Spring Harb Protoc 2017 Jan 03;2017(1)","abstract":"Freezing samples while simultaneously subjecting them to a rapid increase in pressure, which inhibits ice crystal formation, is a reliable method for cryofixing fission yeast. The procedure consists simply of harvesting cells and loading them into a high-pressure freezer (HPF), and then operating the device. If equipment for high-pressure freezing is not available, fission yeast can be frozen by plunging a monolayer of cells into a liquid cryogen, usually ethane or propane. Unlike the HPF, where relatively large volumes of cells can be frozen in a single run, plunge freezing requires cells to be dispersed in a layer <20 µm thick. Unless frozen cells are to be imaged in the vitreous state, they must be fixed, dehydrated, and embedded for subsequent study by transmission electron microscopy; warming frozen cells without fixation badly damages cell structure. Fixation is best accomplished by freeze-substitution, a process in which frozen water is removed from samples by a water-miscible solvent that is liquid at a temperature low enough to prevent the cellular water from recrystallizing. Low concentrations of chemical fixatives and stains are generally added to this solvent such that they permeate the cells as the water is replaced. The activity of these additives is quite limited at the low temperatures required for minimizing ice crystal formation, but they are in the right place to react effectively as the cells warm up. Step-by-step protocols for HPF, plunge freezing, and freeze-substitution are provided here.","doi":"10.1101/pdb.prot091314","authors":"Giddings TH, Morphew MK, McIntosh JR","authors_abbrev":"Giddings TH et al.","pubmed_publication_date":"03 Jan 2017","pubmed_entrez_date":"2017-01-05","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-01-06 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38603491","title":"Molecular mechanism of actin filament elongation by formins.","citation":"Science 2024 Apr 12;384(6692):eadn9560","abstract":"Formins control the assembly of actin filaments (F-actin) that drive cell morphogenesis and motility in eukaryotes. However, their molecular interaction with F-actin and their mechanism of action remain unclear. In this work, we present high-resolution cryo-electron microscopy structures of F-actin barbed ends bound by three distinct formins, revealing a common asymmetric formin conformation imposed by the filament. Formation of new intersubunit contacts during actin polymerization sterically displaces formin and triggers its translocation. This \"undock-and-lock\" mechanism explains how actin-filament growth is coordinated with formin movement. Filament elongation speeds are controlled by the positioning and stability of actin-formin interfaces, which distinguish fast and slow formins. Furthermore, we provide a structure of the actin-formin-profilin ring complex, which resolves how profilin is rapidly released from the barbed end during filament elongation.","doi":"10.1126/science.adn9560","authors":"Oosterheert W, Boiero Sanders M, Funk J, Prumbaum D, Raunser S, Bieling P","authors_abbrev":"Oosterheert W et al.","pubmed_publication_date":"12 Apr 2024","pubmed_entrez_date":"2024-04-11","publication_year":"2024","canto_session_key":"71f087298d9fd36b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-15 20:57:05","canto_approved_date":"2024-06-15 20:57:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-15 07:59:18","canto_added_date":"2024-06-15 06:57:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-06-15","pdb_entries":[{"pdb_id":"8rty","gene_chains":[{"gene_uniquename":"SPAC1F5.04c","chain":"E/E/F/F","position":"881-1390"}],"title":"Structure of the F-actin barbed end bound by Cdc12 and profilin (ring complex) at a resolution of 6.3 Angstrom","entry_authors":"Oosterheert W,Boiero Sanders M,Funk J,Prumbaum D,Raunser S,Bieling P","entry_authors_abbrev":"Oosterheert W et al.","reference_uniquename":"PMID:38603491","experimental_method":"EM","resolution":"6.25"},{"pdb_id":"8rtt","gene_chains":[{"gene_uniquename":"SPAC1F5.04c","chain":"E/F","position":"972-1390"}],"title":"Structure of the formin Cdc12 bound to the barbed end of phalloidin-stabilized F-actin.","entry_authors":"Oosterheert W,Boiero Sanders M,Funk J,Prumbaum D,Raunser S,Bieling P","entry_authors_abbrev":"Oosterheert W et al.","reference_uniquename":"PMID:38603491","experimental_method":"EM","resolution":"3.56"}]},{"uniquename":"PMID:22203678","title":"RNA chaperone activity of human La protein is mediated by variant RNA recognition motif.","citation":"J Biol Chem 2012 Feb 17;287(8):5472-82","abstract":"La proteins are conserved factors in eukaryotes that bind and protect the 3' trailers of pre-tRNAs from exonuclease digestion via sequence-specific recognition of UUU-3'OH. La has also been hypothesized to assist pre-tRNAs in attaining their native fold through RNA chaperone activity. In addition to binding polymerase III transcripts, human La has also been shown to enhance the translation of several internal ribosome entry sites and upstream ORF-containing mRNA targets, also potentially through RNA chaperone activity. Using in vitro FRET-based assays, we show that human and Schizosaccharomyces pombe La proteins harbor RNA chaperone activity by enhancing RNA strand annealing and strand dissociation. We use various RNA substrates and La mutants to show that UUU-3'OH-dependent La-RNA binding is not required for this function, and we map RNA chaperone activity to its RRM1 motif including a noncanonical α3-helix. We validate the importance of this α3-helix by appending it to the RRM of the unrelated U1A protein and show that this fusion protein acquires significant strand annealing activity. Finally, we show that residues required for La-mediated RNA chaperone activity in vitro are required for La-dependent rescue of tRNA-mediated suppression via a mutated suppressor tRNA in vivo. This work delineates the structural elements required for La-mediated RNA chaperone activity and provides a basis for understanding how La can enhance the folding of its various RNA targets.","doi":"10.1074/jbc.M111.276071","authors":"Naeeni AR, Conte MR, Bayfield MA","authors_abbrev":"Naeeni AR et al.","pubmed_publication_date":"17 Feb 2012","pubmed_entrez_date":"2011-12-29","publication_year":"2012","canto_session_key":"70d3bc356eb9b749","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-10-25 14:46:16","canto_approved_date":"2023-10-23 19:56:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-19 16:13:39","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-10-25"},{"uniquename":"PMID:7705612","title":"Effects of ethanol and acetic acid on the transport of malic acid and glucose in the yeast Schizosaccharomyces pombe: implications in wine deacidification.","citation":"FEMS Microbiol Lett 1995 Feb 15;126(2):197-202","abstract":"Ethanol and acetic acid, at concentrations which may occur during wine-making, inhibited the transport of L-malic acid in Schizosaccharomyces pombe. The inhibition was non-competitive, the decrease of the maximum initial velocity following exponential kinetics. Glucose transport was not significantly affected either by ethanol (up to 13%, w/v) or by acetic acid (up to 1.5%, w/v). The uptake of labelled acetic acid followed simple diffusion kinetics, indicating that a carrier was not involved in its transport. Therefore, the undissociated acid appears to be the only form that enters the cells and is probably responsible for the toxic effects. Accordingly, deacidification by Ss. pombe during wine fermentation should take place before, rather than after, the main alcoholic fermentation by Saccharomyces cerevisiae.","authors":"Sousa MJ, Mota M, Leão C","authors_abbrev":"Sousa MJ et al.","pubmed_publication_date":"15 Feb 1995","pubmed_entrez_date":"1995-02-15","publication_year":"1995","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28974540","title":"The fission yeast nucleoporin Alm1 is required for proteasomal degradation of kinetochore components.","citation":"J Cell Biol 2017 Nov 06;216(11):3591-3608","abstract":"Kinetochores (KTs) are large multiprotein complexes that constitute the interface between centromeric chromatin and the mitotic spindle during chromosome segregation. In spite of their essential role, little is known about how centromeres and KTs are assembled and how their precise stoichiometry is regulated. In this study, we show that the nuclear pore basket component Alm1 is required to maintain both the proteasome and its anchor, Cut8, at the nuclear envelope, which in turn regulates proteostasis of certain inner KT components. Consistently,  alm1 -deleted cells show increased levels of KT proteins, including CENP-C Cnp3 , spindle assembly checkpoint activation, and chromosome segregation defects. Our data demonstrate a novel function of the nucleoporin Alm1 in proteasome localization required for KT homeostasis.","doi":"10.1083/jcb.201612194","authors":"Salas-Pino S, Gallardo P, Barrales RR, Braun S, Daga RR","authors_abbrev":"Salas-Pino S et al.","pubmed_publication_date":"06 Nov 2017","pubmed_entrez_date":"2017-10-05","publication_year":"2017","canto_session_key":"fe7a0f32d4e76d5d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rafael Daga","canto_first_approved_date":"2018-06-25 04:20:59","canto_approved_date":"2024-04-02 12:54:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-01-03 09:06:35","canto_added_date":"2017-10-06 00:15:15","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Rafael Daga","community_curator":true,"annotation_count":185,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G10.02c","SPCC364.05","SPAC6F6.09","SPAC11E3.03","SPBC25B2.07c","SPAC15E1.10","SPAC1B1.04c","SPAC3A11.13","SPAC9.13c","SPAC589.12","SPAC1486.04c","SPBC1604.18c","SPBC1105.05","SPAC4H3.02c","SPAC17A5.14","SPAC3F10.10c","SPCC24B10.14c","SPCC14G10.03c","SPBC725.02","SPAPYUG7.04c","SPAC4H3.01","SPBC17A3.03c","SPBC13G1.12","SPBC902.03","SPAC19A8.01c","SPBPJ4664.06","SPAC20H4.06c","SPAC1071.05","SPBC4.07c","SPBC1703.14c","SPAC19G12.13c","SPAC9E9.05","SPCC1322.12c","SPBC557.02c","SPAC4G8.07c","SPCC74.09","SPAC521.05","SPAC821.03c","SPBC13E7.06","SPAC664.15","SPAC1F7.01c","SPAC9.02c","SPAC27E2.01","SPAC17G8.14c","SPBC4C3.08","SPBC25B2.11","SPAC1805.03c","SPAC328.06","SPBC776.02c","SPBC11B10.07c","SPCC1223.15c","SPBC18E5.03c","SPAC15E1.05c","SPCC576.01c","SPAC22G7.02","SPAC16A10.03c","SPBC20F10.06","SPCC24B10.11c","SPBC800.13","SPBC577.15c","SPBC2A9.03","SPAC688.10","SPBC6B1.04","SPBC15D4.03","SPBC19G7.02","SPAPB1E7.05","SPAC3C7.12","SPBC17D11.02c","SPAC4F10.14c","SPAC6F6.03c","SPBC342.01c","SPAC1F5.08c","SPBC409.04c","SPAC1851.03","SPAC926.05c","SPCC663.11","SPBC3B9.05","SPAC25A8.01c","SPAC6G9.01c","SPAC23C11.14","SPAC8C9.09c","SPBC651.02","SPCC576.12c","SPCC1020.12c","SPAC8E11.04c","SPBC16G5.17","SPBC1198.11c","SPCC1223.02","SPBC2D10.16","SPAC1B3.07c","SPCC1494.08c","SPAC17A2.13c","SPBC530.11c","SPAC57A7.09","SPAC17C9.13c","SPBC887.06c","SPBC3H7.09","SPBC530.14c","SPCC576.13","SPBC1861.01c","SPCC417.07c","SPBC27B12.08","SPAC4H3.07c","SPAC6G9.13c","SPAC1002.03c","SPBC354.10","SPAC1687.22c","SPAC23D3.01","SPAPB1E7.02c","SPBC1105.17","SPBP22H7.05c","SPAC57A7.08","SPBC11C11.03","SPCC970.12","SPAC823.05c","SPBC13G1.08c","SPAC1071.03c","SPBC1734.13","SPAC1142.03c","SPAC15A10.06","SPCC18.09c","SPCC965.11c","SPBC26H8.09c","SPAC27F1.04c","SPCC18B5.03","SPCC794.10","SPCC1259.07","SPBC336.03","SPAC1687.20c","SPBC1685.07c","SPCC16C4.01","SPCC4G3.15c","SPCC320.13c","SPBC119.08","SPBC1921.03c","SPAC30.01c","SPBP19A11.03c","SPBC530.06c","SPCC162.08c","SPAC29A4.18","SPCC1919.15","SPAC683.02c","SPAC22E12.04","SPAC6G9.10c","SPBC27.02c","SPAC22F8.07c","SPAC1952.02","SPBC30B4.04c","SPCC1672.10","SPAC3G6.02","SPBC887.10","SPAC6B12.07c","SPAPB1A10.02","SPBC1271.14","SPBC32F12.05c","SPBC354.03","SPAC1002.01","SPAC3G9.01","SPCC965.05c","SPAC4F10.12","SPAC2F3.15","SPAC3A11.03","SPBC3D6.04c","SPBC29A10.06c","SPCC4B3.08"],"gene_count":165,"ltp_gene_count":156,"approved_date":"2018-06-25"},{"uniquename":"PMID:28733407","title":"Fission Yeast Cell Wall Analysis.","citation":"Cold Spring Harb Protoc 2017 Nov 01;2017(11):pdb.top079897","abstract":"The  Schizosaccharomyces pombe  cell wall is a rigid exoskeletal structure mainly composed of interlinked glucose polysaccharides and galactomannoproteins. It is essential for survival of the fission yeast, as it prevents cells from bursting from internal turgor pressure and protects them from mechanical injuries. Additionally, the cell wall determines the cell shape and, therefore, a better knowledge of cell wall structure and composition could provide valuable data in  S. pombe  morphogenetic studies. Here, we provide information about this structure and the current reliable methods for rapid analysis of the cell wall polymers by specific enzymatic and chemical degradations of purified cell walls.","doi":"10.1101/pdb.top079897","authors":"Pérez P, Ribas JC","authors_abbrev":"Pérez P et al.","pubmed_publication_date":"01 Nov 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10675040","title":"Investigation of Schizosaccharomyces pombe as a cloning host for human telomere and alphoid DNA.","citation":"Gene 2000 Jan 11;241(2):275-85","abstract":"The fission yeast Schizosaccharomyces pombe (Sch. pombe) has been proposed as a possible cloning host for both mammalian artificial chromosomes (MACs) and mammalian genomic libraries, due to the large size of its chromosomes and its similarity to higher eukaryotic cells. Here, it was investigated for its ability to form telomeres from human telomere sequence and to stably maintain long stretches of alphoid DNA. Using linear constructs terminating in the telomere repeat, T2AG3, human telomere DNA was shown to efficiently seed telomere formation in Sch. pombe. Much of the human telomeric sequence was removed on addition of Sch. pombe telomeric sequence, a process similar to that described in S. cerevisiae. To investigate the stability of alphoid DNA in fission yeast, bacterial artificial chromosomes (BACs) containing 130 and 173 kb of alphoid DNA were retrofitted with the Sch. pombe ars1 element and ura4+ marker using Cre-lox recombination. These alphoid BACs were found to be highly unstable in Sch. pombe deleting down to less than 40 kb, whilst control BACs of 96 and 202 kb, containing non-repetitive DNA, were unrearranged. Alphoid DNA has been shown to be sufficient for human centromere function, and this marked instability excludes Sch. pombe as a useful cloning host for mammalian artificial chromosomes. In addition, regions containing repetitive DNA from mammalian genomes may not be truly represented in libraries constructed in Sch. pombe.","authors":"Mann KL, Huxley C","authors_abbrev":"Mann KL et al.","pubmed_publication_date":"11 Jan 2000","pubmed_entrez_date":"2000-02-16","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9245353","title":"Parallel Processing in Genome Mapping and Sequencing.","citation":"Methods 1996 Feb;9(1):136-44","abstract":"Conventional genome mapping and sequencing involves the analysis and processing of individual samples and pieces of experimental data. Although these methods work, it is quite clear that more efficient and less expensive methods are needed. Our top down physical mapping experiments have focused on the parallel processing of information from multiple samples at one time. This approach has aided the construction of genomic restriction maps and allowed us to assess the degree of large-scale conservation across wide regions of the human genome. The principles of parallel processing were applied in top down experiments that ordered an overlapping cosmid library from the 14-Mb Schizosaccharomyces pombe genome. This approach produced an eight-fold increase in efficiency in clone ordering over similar efforts. Recently, we have developed an enhanced sequencing by hybridization protocol that allows DNA sequence information to be collected on a large number of samples at once. Our current research focuses on applying parallel processing principles to make genome-wide comparisons between pairs of samples for analyzing disease states.","authors":"Smith CL, Wang D, Broude N, Bukanov N, Monastyrskaya GS, Sverdlov E","authors_abbrev":"Smith CL et al.","pubmed_publication_date":"Feb 1996","pubmed_entrez_date":"1996-02-01","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9111914","title":"Sexual co-flocculation by heterothallic cells of the fission yeast Schizosaccharomyces pombe modulated by medium constituents.","citation":"Antonie Van Leeuwenhoek 1997 Mar;71(3):207-15","abstract":"Novel simple synthetic media for inducing sexual co-flocculation in a short time after mixing heterothallic fission-yeast (Schizosaccharomyces pombe) cells of h- and h+ were devised; The most effective of these, mannose synthetic medium (MSM), contains 0.4% mannose as a carbon source in addition to galactose, KH2PO4 (pH4.0) and 4 vitamins. The addition of galactose to the medium suppressed the asexual self-flocculation but rather promoted the sexual co-flocculation. By transferring and mixing h- and h+ cells grown in malt-extract broth plus galactose into MSM, these heterothallic strains were revealed to be sexually ready through a long period of the log to stationary phases. Furthermore, a variety of C sources and NH4Cl at various concentrations in various media were examined for their effects upon sexual co-flocculation, conjugation and sporulation; it was found that the sugar concentration strictly affected the progress of the sequence of sexual reproduction at 26 degrees C but not 30 degrees C and that sexual co-flocculation of the heterothallic strains was induced only under lower concentrations of C and N source than that for the homothallic one.","authors":"Miyata M, Doi H, Miyata H, Johnson BF","authors_abbrev":"Miyata M et al.","pubmed_publication_date":"Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC00233","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7805886","title":"Recombinant expression and domain structure of the Rna1 protein from Schizosaccharomyces pombe.","citation":"FEBS Lett 1995 Jan 03;357(2):173-7","abstract":"The amino acid sequence of Rna1p, a yeast protein implicated in the maturation and/or nucleocytoplasmic transport of RNA, is characterised by the presence of eight leucine-rich repeats (LLRs) as well as two intervening repeats of a different type and a highly acidic C-terminal region. Limited proteolysis of purified Rna1p expressed recombinantly in bacteria reveals that the C-terminal extension but not the region containing the two types of repeats is highly accessible to proteolytic attack and that the C-terminal region most likely harbours (a) low affinity Ca(2+)-binding site(s). These results are indicative of the domain structure of the Rna1p molecule, with the repeats and the C-terminal region being accessible for different interactions.","authors":"Haberland J, Gerke V","authors_abbrev":"Haberland J et al.","pubmed_publication_date":"03 Jan 1995","pubmed_entrez_date":"1995-01-03","publication_year":"1995","canto_session_key":"a13bb32b9de9e502","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-25 10:17:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-24 10:35:54","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22E12.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-04-24"},{"uniquename":"PMID:12807767","title":"Repair of damaged and mismatched DNA by the XPC homologues Rhp41 and Rhp42 of fission yeast.","citation":"Genetics 2003 Jun;164(2):457-67","abstract":"Rhp41 and Rhp42 of Schizosaccharomyces pombe are homologues of human XPC, which is involved in nucleotide excision repair (NER) of damaged DNA. Inactivation of rhp41 caused moderate sensitivity to ultraviolet (UV) radiation. In addition, an increase of mitotic mutation rates was observed in the rhp41 mutant, which was dependent on active translesion polymerase Z. UV sensitivity and mutation rates were not different between rhp42 and wild type, but compared to rhp41 were further increased in rhp41 rhp42 cells. Transcription of the fbp1 gene (induced in vegetative cells) and of the SPBC1289.14 gene (induced during meiosis) was strongly blocked by UV-induced damages in the rhp41 mutant, but not, or only slightly, reduced in rhp42 background. NER-dependent short-patch repair of mismatches formed during meiosis was slightly affected in rhp41, moderately affected in rhp42, and absent in rhp41 rhp42. Epistasis analysis with rhp7 and rhp26 indicates that Rhp41 and Rhp42 are both involved in the global genome and transcription-coupled repair subpathways of NER. Rhp41 plays a major role in damage repair and Rhp42 in mismatch repair.","authors":"Marti TM, Kunz C, Fleck O","authors_abbrev":"Marti TM et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-06-17","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC12B10.12c","SPAC688.10","SPBC19C7.09c","SPCP25A2.02c","SPCC330.02","SPBC4F6.15c","SPBC19G7.01c","SPCC4G3.10c"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:2611011","title":"[Various sensitivities of yeasts to lycorine].","citation":"Boll Soc Ital Biol Sper 1989 Jun;65(6):501-8","abstract":"Lycorine, an Amaryllidaceae alkaloid, is a powerful inhibitor of growth in higher plants and algae. Thirty-one strains of yeasts, belonging to different genera and species, were screened to study the effect of lycorine on their growth. The strains were incubated at 25 degrees C in a 2% glucose medium with different concentrations of lycorine (10, 50 and 100 microM), and their growth after 72 hours was evaluated. Most of the strains showed no sensitivity to lycorine. However, in Schizosaccharomyces pombe (IMAT-V Pbx) and Aureobasidium pullulans (DBV A77) lycorine significantly inhibited growth (59-73%), while, on the contrary, in Saccharomycopsis fibuligera (DBV 3812) and Cryptococcus terreus (CBS 1895) it was clearly stimulated (76-140%). The fact that lycorine inhibits growth in some yeasts while it stimulates it in others means that neither of the two previously formulated interpretations on the molecular mechanism of action of alkaloid can explain all cases. In other words, it does not seem that lycorine just inhibits protein synthesis, as claimed by Kukhanova et al. (1983), nor, on the other hand, do the data presented here prove that lycorine specifically inhibits ascorbic acid biosynthesis (Arrigoni et al., 1975). We must now check the ability of yeasts to split lycorine and study whether yeasts do actually have an ascorbic acid system.","authors":"Garuccio I, Arrigoni O","authors_abbrev":"Garuccio I et al.","pubmed_publication_date":"Jun 1989","pubmed_entrez_date":"1989-06-01","publication_year":"1989","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8395535","title":"Identification of seven new cut genes involved in Schizosaccharomyces pombe mitosis.","citation":"J Cell Sci 1993 May;105 ( Pt 1):135-43","abstract":"Fission yeast cut mutants cause cytokinesis in the absence of normal nuclear division. These mutants show abnormal uncoupled mitosis and are known to be the result of mutations in the genes encoding DNA topoisomerase II, proteins related to spindle pole duplication, and a kinesin-related mitotic motor. We have screened 717 temperature-sensitive (ts) mutants by individually observing their cytological phenotypes at the restrictive temperature, and have newly isolated 25 cut mutants. Genetic analyses indicate that 14 of them fall into five previously identified loci, namely, top2, cut1, cut5, cut7 and cut9, whereas nine have been mapped onto seven new loci, designated cut13 to cut19. The cytological phenotypes of the newly identified cut mutants can be classified into three groups. One group consists of mutants in which a portion of the nuclear chromatin is stretched by the elongated spindle but the entire nucleus is not separated, reminiscent of, but not identical to, the phenotypes of top2 and cut1; mutants cut14-208, cut15-85, cut16-267 and cut17-275 display such a phenotype. Another group exhibits non-disjunctioned and condensed chromosomes in the presence of the spindle; cut13-131 belongs to this group. The cut19-708 mutant has also been found to have condensed chromosomes. The remaining group has a mixed phenotype of the above two groups; namely, stretched chromatin and condensed chromosomes; cut18-447 exhibits such a phenotype. The isolation and characterization of the mutated genes will be the subjects of future investigations.","authors":"Samejima I, Matsumoto T, Nakaseko Y, Beach D, Yanagida M","authors_abbrev":"Samejima I et al.","pubmed_publication_date":"May 1993","pubmed_entrez_date":"1993-05-01","publication_year":"1993","canto_session_key":"19290aa093475d5e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-02 15:58:42","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-10-30 18:23:27","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.04","SPAC23C4.18c","SPBP4H10.06c","SPCC962.02c","SPAC25G10.07c","SPCC962.03c","SPAC6F12.15c","SPBC1A4.03c","SPBC14C8.01c"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2014-10-30"},{"uniquename":"PMID:22987637","title":"Telomere-binding protein Taz1 controls global replication timing through its localization near late replication origins in fission yeast.","citation":"Genes Dev 2012 Sep 15;26(18):2050-62","abstract":"In eukaryotes, the replication of chromosome DNA is coordinated by a replication timing program that temporally regulates the firing of individual replication origins. However, the molecular mechanism underlying the program remains elusive. Here, we report that the telomere-binding protein Taz1 plays a crucial role in the control of replication timing in fission yeast. A DNA element located proximal to a late origin in the chromosome arm represses initiation from the origin in early S phase. Systematic deletion and substitution experiments demonstrated that two tandem telomeric repeats are essential for this repression. The telomeric repeats recruit Taz1, a counterpart of human TRF1 and TRF2, to the locus. Genome-wide analysis revealed that Taz1 regulates about half of chromosomal late origins, including those in subtelomeres. The Taz1-mediated mechanism prevents Dbf4-dependent kinase (DDK)-dependent Sld3 loading onto the origins. Our results demonstrate that the replication timing program in fission yeast uses the internal telomeric repeats and binding of Taz1.","doi":"10.1101/gad.194282.112","authors":"Tazumi A, Fukuura M, Nakato R, Kishimoto A, Takenaka T, Ogawa S, Song JH, Takahashi TS, Nakagawa T, Shirahige K, Masukata H","authors_abbrev":"Tazumi A et al.","pubmed_publication_date":"15 Sep 2012","pubmed_entrez_date":"2012-09-19","publication_year":"2012","canto_session_key":"d505f490197e7842","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hisao Masukata","canto_first_approved_date":"2016-11-10 11:20:26","canto_approved_date":"2022-10-05 22:24:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-03 09:03:42","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Hisao Masukata","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.17","SPBC211.04c","SPAC24H6.06","SPAC16A10.07c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2016-11-10"},{"uniquename":"PMID:7898433","title":"Characterization of uvi15+, a stress-inducible gene from Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1995 Mar 20;246(6):663-70","abstract":"The uvi15+ gene of Schizosaccharomyces pombe is a member of a group of stress-inducible genes transcription levels of which increase in response to DNA-damaging agents or heat shock. It encodes a polypeptide of calculated molecular mass 11641 Da, with no significant sequence similarity to other known heat shock proteins. The steady-state level of the uvi15+ gene product of about 12 kDa was increased by heat shock and canavanine, an amino acid analog. This gene also showed a transient increase in expression as cells moved into diauxic shift phase. Although deletion of the uvi15+ gene did not affect the mitotic growth or thermotolerance of cells, the mutant cells rapidly lost viability in stationary phase and under starvation conditions. These cells also showed a defect in sporulation ability. These results suggest that the uvi15+ gene encodes a stress response protein involved in the maintenance of cell viability during entry into stationary phase or under starvation conditions.","authors":"Lee JK, Kim M, Choe J, Seong RH, Hong SH, Park SD","authors_abbrev":"Lee JK et al.","pubmed_publication_date":"20 Mar 1995","pubmed_entrez_date":"1995-03-20","publication_year":"1995","canto_session_key":"5964257cca6cfa69","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-06-30 09:06:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-07-17 14:26:37","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC649.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-07-17"},{"uniquename":"EMBL:AU010044","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012446","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11486016","title":"Control of DNA rereplication via Cdc2 phosphorylation sites in the origin recognition complex.","citation":"Mol Cell Biol 2001 Sep;21(17):5767-77","abstract":"Cdc2 kinase is a master regulator of cell cycle progression in the fission yeast Schizosaccharomyces pombe. Our data indicate that Cdc2 phosphorylates replication factor Orp2, a subunit of the origin recognition complex (ORC). Cdc2 phosphorylation of Orp2 appears to be one of multiple mechanisms by which Cdc2 prevents DNA rereplication in a single cell cycle. Cdc2 phosphorylation of Orp2 is not required for Cdc2 to activate DNA replication initiation. Phosphorylation of Orp2 appears first in S phase and becomes maximal in G(2) and M when Cdc2 kinase activity is required to prevent reinitiation of DNA replication. A mutant lacking Cdc2 phosphorylation sites in Orp2 (orp2-T4A) allowed greater rereplication of DNA than congenic orp2 wild-type strains when the limiting replication initiation factor Cdc18 was deregulated. Thus, Cdc2 phosphorylation of Orp2 may be redundant with regulation of Cdc18 for preventing reinitiation of DNA synthesis. Since Cdc2 phosphorylation sites are present in Orp2 (also known as Orc2) from yeasts to metazoans, we propose that cell cycle-regulated phosphorylation of the ORC provides a safety net to prevent DNA rereplication and resulting genetic instability.","authors":"Vas A, Mok W, Leatherwood J","authors_abbrev":"Vas A et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-08-04","publication_year":"2001","canto_session_key":"d4ae29a798ec94dd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-02-24 15:33:43","canto_approved_date":"2024-01-11 17:19:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-01 13:03:23","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC685.09","SPBC14C8.07c","SPBC582.03","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-02-24"},{"uniquename":"PMID:39527195","title":"Pil1 Co-tethering Assay to Detect Protein-Protein Interactions in the Fission Yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2025;2862:93-102","abstract":"Protein-protein interactions play critical roles in biological processes. We previously developed the Pil1 co-tethering assay, an imaging-based method to detect protein-protein interactions in living Schizosaccharomyces pombe cells. This assay leverages the distinct localization pattern of the Pil1 protein by fusing a bait protein to Pil1 and examining whether a prey protein co-localize with the Pil1-fused bait. Here, we present an improved protocol of the Pil1 co-tethering assay. In this protocol, modified stable integration vectors (SIVs) with a NotI site as the linearization site are used to express bait and prey proteins. We expect that this protocol will enhance the application of the Pil1 co-tethering assay for studying protein-protein interactions.","doi":"10.1007/978-1-0716-4168-2_7","authors":"Pan ZQ, Yang YS, Du LL","authors_abbrev":"Pan ZQ et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084878","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.66"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1316996","title":"Cold-sensitive mutants of p34cdc2 that suppress a mitotic catastrophe phenotype in fission yeast.","citation":"Mol Gen Genet 1992 Apr;232(3):344-50","abstract":"The p34cdc2 protein kinase plays a central role in the regulation of the eukaryotic cell cycle, being required both in late G1 for the commitment to S-phase and in late G2 for the initiation of mitosis. p34cdc2 also determines the precise timing of entry into mitosis in fission yeast, where a number of gene products that regulate p34cdc2 activity have been identified and characterised. To investigate further the mitotic role of p34cdc2 in this organism we have isolated new cold-sensitive p34cdc2 mutants. These are defective only in their G2 function and are extragenic suppressors of the lethal premature entry into mitosis brought about by mutating the mitotic inhibitor p107wee1 and overproducing the mitotic activator p80cdc25. One of the mutant proteins p34cdc2-E8 is only functional in the absence of p107wee1, and all the mutant strains have reduced histone H1 kinase activity in vitro. Each mutant allele has been cloned and sequenced, and the lesions responsible for the cold-sensitive phenotypes identified. All the mutations were found to map to regions that are conserved between the fission yeast p34cdc2 and functional homologues from higher eukaryotes.","authors":"Ayscough K, Hayles J, MacNeill SA, Nurse P","authors_abbrev":"Ayscough K et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"31390a94c8f8643a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-07-05 15:14:24","canto_approved_date":"2025-12-23 13:14:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-28 14:28:38","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Jacky Hayles","community_curator":false,"annotation_count":9,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPCC18B5.03","SPBC11B10.09","SPCC70.07c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-07-05"},{"uniquename":"PMID:12450137","title":"Involvement of a CCAAT-binding complex in the expression of a nitrogen-starvation-specific gene, isp6+, in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2002 Oct;66(10):2224-7","abstract":"The fission yeast gene isp6+ is needed in nitrogen-starvation response but its transcriptional regulation has been unclear. isp6+ was repressed under nutrient conditions, in which cAMP-dependent protein kinase A, the stress-activated protein kinase cascade, and the CCAAT-binding complex were concerned. The CCAAT-binding complex also was involved in the induction of isp6+ during nitrogen starvation.","authors":"Nakashima A, Ueno M, Ushimaru T, Uritani M","authors_abbrev":"Nakashima A et al.","pubmed_publication_date":"Oct 2002","pubmed_entrez_date":"2002-11-27","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11511538","title":"A DNA replication-arrest site RTS1 regulates imprinting by determining the direction of replication at mat1 in S. pombe.","citation":"Genes Dev 2001 Aug 15;15(16):2060-8","abstract":"Mating-type switching in Schizosaccharomyces pombe involves a strand-specific, alkali-labile imprint at the mat1 (mating-type) locus. The imprint is synthesized during replication in a swi1, swi3, and polymerase alpha (swi7) dependent manner and is dependent on mat1 being replicated in a specific direction. Here we show that the direction of replication at mat1 is controlled by a cis-acting polar terminator of replication (RTS1). Two-dimensional gel analysis of replication intermediates reveals that RTS1 only terminates replication forks moving in the centromere-distal direction. A genetic analysis shows that RTS1 optimizes the imprinting process. Transposing the RTS1 element to the distal side of mat1 abolishes imprinting of the native mat1 allele but restores imprinting of an otherwise unimprinted inverted mat1 allele. These data provide conclusive evidence for the \"direction of replication model\" that explains the asymmetrical switching pattern of S. pombe, and identify a DNA replication-arrest element implicated in a developmental process. Such elements could play a more general role during development and differentiation in higher eukaryotes by regulating the direction of DNA replication at key loci.","authors":"Dalgaard JZ, Klar AJ","authors_abbrev":"Dalgaard JZ et al.","pubmed_publication_date":"15 Aug 2001","pubmed_entrez_date":"2001-08-21","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25131669","title":"Telomerase activation after recruitment in fission yeast.","citation":"Curr Biol 2014 Sep 08;24(17):2006-11","abstract":"Current models depict that telomerase recruitment equates to activation. Telomeric DNA-binding proteins and the telomerase accessory proteins coordinate the recruitment of telomerase to the ends of chromosomes in a telomere length- and cell-cycle-dependent manner [1-4]. Recent studies have demonstrated that the telomeric protein TPP1 and its binding protein TIN2 are key proteins for both telomerase recruitment and processivity in mammalian cells [5-7]. Although the precise molecular mechanism of telomerase recruitment has not yet been established, targeted point mutations within the oligonucleotide/oligosaccharide-binding (OB)-fold domain of TPP1 have been shown to impair telomerase association and processivity [8-10]. In fission yeast, telomerase is recruited through an interaction between the telomerase subunit Est1 and Ccq1, a component of the Pot1-Tpz1 telomere complex (POT1-TPP1 orthologs) [11-15]. Here, we demonstrate that association of telomerase with telomeres does not engage activity. We describe a mutation of Tpz1 that causes critical telomere shortening despite telomeric accumulation of the telomerase catalytic subunit, Trt1. Furthermore, Est1-directed telomerase association with Ccq1 is transient, and the Est1-Ccq1 interaction does not remain the bridge between telomeres and telomerase. Rather, direct interaction of Trt1 with Tpz1 is critical for telomere elongation. Moreover, Ccq1, which has been well characterized as a telomerase recruiter, is also required for the activation of telomere-associated telomerase. Our findings reveal a layer of telomerase regulation that controls activity after recruitment.","doi":"10.1016/j.cub.2014.07.035","authors":"Armstrong CA, Pearson SR, Amelina H, Moiseeva V, Tomita K","authors_abbrev":"Armstrong CA et al.","pubmed_publication_date":"08 Sep 2014","pubmed_entrez_date":"2014-08-19","publication_year":"2014","canto_session_key":"20a764f2e6d7485e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kazunori Tomita","canto_first_approved_date":"2017-11-01 16:46:59","canto_approved_date":"2021-02-14 18:59:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-27 14:12:01","canto_added_date":"2014-08-20 00:15:24","annotation_curators":[{"name":"Kazunori Tomita","community_curator":true,"annotation_count":1,"orcid":"0000-0003-1096-6725","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":59,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.02","SPCC188.07","SPAC26H5.06","SPAC19G12.13c","SPAC6F6.16c","SPBC29A3.14c","SPAC16A10.07c","SPBC2D10.13","SPNCRNA.214"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2017-11-01"},{"uniquename":"PMID:15915339","title":"Genetic and physical interactions between Schizosaccharomyces pombe Mcl1 and Rad2, Dna2 and DNA polymerase alpha: evidence for a multifunctional role of Mcl1 in DNA replication and repair.","citation":"Curr Genet 2005 Jul;48(1):34-43","abstract":"Schizosaccharomyces pombe rad2 is involved in Okazaki fragments processing during lagging-strand DNA replication. Previous studies identified several slr mutants that are co-lethal with rad2Delta and sensitive to methyl methanesulfonate as single mutants. One of these mutants, slr3-1, is characterized here. Complementation and sequence analyses show that slr3-1 (mcl1-101) is allelic to mcl1(+), which is required for chromosome replication, cohesion and segregation. mcl1-101 is temperature-sensitive for growth and is highly sensitive to DNA damage. mcl1 cells arrest with 2C DNA content and chromosomal DNA double-strand breaks accumulate at the restrictive temperature. Mcl1p, which belongs to the Ctf4p/SepBp family, interacts both genetically and physically with DNA polymerase alpha. Mutations in rhp51 and dna2 enhance the growth defect of the mcl1-101 mutant. These results strongly suggest that Mcl1p is a functional homologue of Saccharomyces cerevisiae Ctf4p and plays a role in lagging-strand synthesis and Okazaki fragment processing, in addition to DNA repair.","authors":"Tsutsui Y, Morishita T, Natsume T, Yamashita K, Iwasaki H, Yamao F, Shinagawa H","authors_abbrev":"Tsutsui Y et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-05-26","publication_year":"2005","canto_session_key":"a28d9f4e4dcc8ef3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-07-22 14:40:28","canto_approved_date":"2025-09-03 14:18:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-13 17:48:33","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c","SPAPB1E7.02c","SPBC16D10.04c","SPAC3G6.06c","SPAC644.14c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-07-22"},{"uniquename":"PMID:24191010","title":"Subnuclear relocalization and silencing of a chromosomal region by an ectopic ribosomal DNA repeat.","citation":"Proc Natl Acad Sci U S A 2013 Nov 19;110(47):E4465-73","abstract":"Our research addresses the relationship between subnuclear localization and gene expression in fission yeast. We observed the relocalization of a heterochromatic region, the mating-type region, from its natural location at the spindle-pole body to the immediate vicinity of the nucleolus. Relocalization occurred in response to a DNA rearrangement replacing a boundary element (IR-R) with a ribosomal DNA repeat (rDNA-R). Gene expression was strongly silenced in the relocalized mating-type region through mechanisms that differ from those operating in wild type. Also different from the wild-type situation, programmed recombination events failed to take place in the rDNA-R mutant. Increased silencing and perinucleolar localization depended on Reb1, a DNA-binding protein with cognate sites in the rDNA. Reb1 was recently shown to mediate long-range interchromosomal interactions in the nucleus through dimerization, providing a mechanism for the observed relocalization. Replacing the full rDNA repeat with Reb1-binding sites, and using mutants lacking the histone H3K9 methyltransferase Clr4, indicated that the relocalized region was silenced redundantly by heterochromatin and another mechanism, plausibly antisense transcription, achieving a high degree of repression in the rDNA-R strain.","doi":"10.1073/pnas.1315581110","authors":"Jakociunas T, Domange Jordö M, Aït Mebarek M, Bünner CM, Verhein-Hansen J, Oddershede LB, Thon G","authors_abbrev":"Jakociunas T et al.","pubmed_publication_date":"19 Nov 2013","pubmed_entrez_date":"2013-11-06","publication_year":"2013","canto_session_key":"24545814754c29b5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27002055","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:20:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7698654","title":"Isolation and sequencing of two cDNA clones encoding Rho proteins from the fission yeast Schizosaccharomyces pombe.","citation":"Gene 1995 Mar 21;155(1):119-22","abstract":"The rho genes encode a group of low-molecular-weight GTP-binding proteins that show about 30% identity in the amino-acid sequence to the ras gene product. Two cDNA clones, both of which are similar to the rho genes, were isolated from a cDNA library of the fission yeast Schizosaccharomyces pombe, using the human rhoA cDNA as a probe. These genes were called rho1+ and rho2+. The encoded Rho1 protein showed 72.7% identity to the budding yeast RHO1 and 66.8% to human RhoA, and the encoded Rho2 protein showed 53.2% identity to the budding yeast RHO2 and RhoA.","authors":"Nakano K, Mabuchi I","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"21 Mar 1995","pubmed_entrez_date":"1995-03-21","publication_year":"1995","canto_session_key":"a3bff2e2b0c51abc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 18:10:01","canto_approved_date":"2019-01-31 18:10:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 18:09:54","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16.01","SPAC1F7.04"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:16322512","title":"zds1, a novel gene encoding an ortholog of Zds1 and Zds2, controls sexual differentiation, cell wall integrity and cell morphology in fission yeast.","citation":"Genetics 2006 Feb;172(2):811-25","abstract":"While screening for genes that reverse the sporulation-deficient phenotype of the ras1delta diploid Schizosaccharomyces pombe strain, we identified zds1. This gene shares sequence homology with the ZDS1 and ZDS2 genes from Saccharomyces cerevisiae, which appear to be involved in multiple cellular events. Expression of Zds1 in ras1delta diploid cells elevated their sporulation rate from 0.3 to 11.2%. Expression of the Zds1 C-terminal region increased the sporulation rate further (to 21.9%) while introduction of the Zds1 N-terminal region had no effect. zds1 expression did not induce sporulation in strains with mutations in genes participating in the downstream MAP kinase cascade. The zds1-disrupted strain is sensitive to CaCl2, and this effect is suppressed by the C-terminal region of Zds1. The growth of the zds1delta strain is markedly inhibited by cold temperatures, while its viability decreased in the stationary phase. Moreover, the zds1delta strain is round in shape and very sensitive to zymolyase, and its cell wall becomes thicker than that of wild type. Thus, zds1 must be required to maintain cell wall integrity. The Zds1-GFP fusion protein localized to the cytosol, the septum, and the cell cortex. Its localization in the septum was dependent on its C-terminal region. Overexpression of the C-terminal region of Zds1 induced multi-septa and abnormal zygotes. We propose that the C-terminal region is the functional domain of Zds1 while the N-terminal region is a negative regulatory region. Thus, Zds1 is involved in multiple cellular events in fission yeast, including sexual differentiation, Ca2+ tolerance, cell wall integrity, viability in the stationary phase, and cell morphology.","authors":"Yakura M, Ozoe F, Ishida H, Nakagawa T, Tanaka K, Matsuda H, Kawamukai M","authors_abbrev":"Yakura M et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2005-12-03","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPAC31F12.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:16936832","title":"Epigenetic regulation of centromere formation and kinetochore function.","citation":"Biochem Cell Biol 2006 Aug;84(4):605-18","abstract":"In the midst of an increasingly detailed understanding of the molecular basis of genome regulation, we still only vaguely understand the relationship between molecular biochemistry and the structure of the chromatin inside of cells. The centromere is a structurally and functionally unique region of each chromosome and provides an example in which the molecular understanding far exceeds the understanding of the structure and function relationships that emerge on the chromosomal scale. The centromere is located at the primary constriction of the chromosome. During entry into mitosis, the centromere specifies the assembly site of the kinetochore, the structure that binds to microtubules to enable transport of the chromosomes into daughter cells. The epigenetic contributions to the molecular organization and function of the centromere are reviewed in the context of structural mechanisms of chromatin function.","authors":"Heit R, Underhill DA, Chan G, Hendzel MJ","authors_abbrev":"Heit R et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-08-29","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12845604","title":"Genome-wide identification of fungal GPI proteins.","citation":"Yeast 2003 Jul 15;20(9):781-96","abstract":"Glycosylphosphatidylinositol-modified (GPI) proteins share structural features that allow their identification using a genomic approach. From the known S. cerevisiae and C. albicans GPI proteins, the following consensus sequence for the GPI attachment site and its downstream region was derived: [NSGDAC]-[GASVIETKDLF]-[GASV]-X(4,19)-[FILMVAGPSTCYWN](10)>, where > indicates the C-terminal end of the protein. This consensus sequence, which recognized known GPI proteins from various fungi, was used to screen the genomes of the yeasts S. cerevisiae, C. albicans, Sz. pombe and the filamentous fungus N. crassa for putative GPI proteins. The subsets of proteins so obtained were further screened for the presence of an N-terminal signal sequence for the secretion and absence of internal transmembrane domains. In this way, we identified 66 putative GPI proteins in S. cerevisiae. Some of these are known GPI proteins that were not identified by earlier genomic analyses, indicating that this selection procedure renders a more complete image of the S. cerevisiae GPI proteome. Using the same approach, 104 putative GPI proteins were identified in the human pathogen C. albicans. Among these were the proteins Gas/Phr, Ecm33, Crh and Plb, all members of GPI protein families that are also present in S. cerevisiae. In addition, several proteins and protein families with no significant homology to S. cerevisiae proteins were identified, including the cell wall-associated Als, Csa1/Rbt5, Hwp1/Rbt1 and Hyr1 protein families. In Sz. pombe, which has a low level of (galacto)mannan in the cell wall compared to C. albicans and S. cerevisiae, only 33 GPI candidates were identified and in N. crassa 97. BLAST searches revealed that about half of the putative GPI proteins that were identified in Sz. pombe and N. crassa are homologous to known or putative GPI proteins from other fungi. We conclude that our algorithm is selective and can also be used for GPI protein identification in other fungi.","authors":"De Groot PW, Hellingwerf KJ, Klis FM","authors_abbrev":"De Groot PW et al.","pubmed_publication_date":"15 Jul 2003","pubmed_entrez_date":"2003-07-08","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBP4G3.02","SPCC970.02","SPAC19G12.16c","SPAC212.08c","SPAC1A6.03c","SPAPB15E9.01c","SPAC1786.02","SPBP19A11.02c","SPBPJ4664.02","SPBPB7E8.01","SPCC1795.09","SPAC19B12.02c","SPAC26A3.01","SPAC27E2.11c","SPAC1F5.08c","SPCC553.10","SPAC23D3.14c","SPAC2E1P3.05c","SPCC24B10.06","SPBC29A10.08","SPAC1F8.02c","SPBC1E8.05","SPBC342.03","SPBC16A3.13","SPAC17A5.04c","SPBC215.13","SPAC821.09","SPCC63.02c","SPCC757.12"],"gene_count":29,"ltp_gene_count":1},{"uniquename":"PMID:30674555","title":"An essential role for dNTP homeostasis following CDK-induced replication stress.","citation":"J Cell Sci 2019 Mar 25;132(6)","abstract":"Replication stress is a common feature of cancer cells, and thus a potentially important therapeutic target. Here, we show that cyclin-dependent kinase (CDK)-induced replication stress, resulting from Wee1 inactivation, is synthetic lethal with mutations disrupting dNTP homeostasis in fission yeast. Wee1 inactivation leads to increased dNTP demand and replication stress through CDK-induced firing of dormant replication origins. Subsequent dNTP depletion leads to inefficient DNA replication, DNA damage and to genome instability. Cells respond to this replication stress by increasing dNTP supply through histone methyltransferase Set2-dependent MBF-induced expression of Cdc22, the catalytic subunit of ribonucleotide reductase (RNR). Disrupting dNTP synthesis following Wee1 inactivation, through abrogating Set2-dependent H3K36 tri-methylation or DNA integrity checkpoint inactivation results in critically low dNTP levels, replication collapse and cell death, which can be rescued by increasing dNTP levels. These findings support a 'dNTP supply and demand' model in which maintaining dNTP homeostasis is essential to prevent replication catastrophe in response to CDK-induced replication stress.","doi":"10.1242/jcs.226969","authors":"Pai CC, Hsu KF, Durley SC, Keszthelyi A, Kearsey SE, Rallis C, Folkes LK, Deegan R, Wilkins SE, Pfister SX, De León N, Schofield CJ, Bähler J, Carr AM, Humphrey TC","authors_abbrev":"Pai CC et al.","pubmed_publication_date":"25 Mar 2019","pubmed_entrez_date":"2019-01-25","publication_year":"2019","canto_session_key":"2d68ca2dceefb4d6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-01-26 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC29B12.02c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:17623900","title":"Function of recQ family helicase in genome stability.","citation":"Subcell Biochem 2006;40:49-73","abstract":"The recQ gene of Escherichia coli is the founding member of the RecQ family of helicases. Like E. coli, lower eukaryotic species also possess single RecQ proteins, such as Sgs1 and Rqh1 in budding and fission yeast, respectively. However, there are five RecQ helicases in human as well as in chicken cells. Three of the human RecQ helicases are encoded by BLM, WRN and RECQL4 genes, defects of which give rise to the cancer predisposition disorders known as Bloom syndrome (BS), Werner syndrome (WS) and Rothmund-Thomson syndrome (RTS), respectively. The other two, RECQL1 and RECQL5, have not been associated with human diseases. Characterization of RecQ family proteins in unicellular organisms has revealed that their defects confer genomic instability and impairment of homologous recombination. Although systematic genetic analysis of human BS, WS, and RTS cells must be useful to understand their functions, such approach is hampered by the difficulty of making cell lines with double gene disruptions. In this context, the chicken DT40 cell line is an ideal experimental tool for sophisticated approaches that illuminate the functions of vertebrate RecQ helicases. Here, we briefly review general features of RecQ helicases and describe their functions as revealed by analysis of DT40 cells.","authors":"Seki M, Tada S, Enomoto T","authors_abbrev":"Seki M et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-07-13","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17380189","title":"Ribonuclease activity of Dis3 is required for mitotic progression and provides a possible link between heterochromatin and kinetochore function.","citation":"PLoS One 2007 Mar 21;2(3):e317","abstract":"Cellular RNA metabolism has a broad range of functional aspects in cell growth and division, but its role in chromosome segregation during mitosis is only poorly understood. The Dis3 ribonuclease is a key component of the RNA-processing exosome complex. Previous isolation of the dis3-54 cold-sensitive mutant of fission yeast Schizosaccharomyces pombe suggested that Dis3 is also required for correct chromosome segregation.\nWe show here that the progression of mitosis is arrested in dis3-54, and that segregation of the chromosomes is blocked by activation of the mitotic checkpoint control. This block is dependent on the Mad2 checkpoint protein. Double mutant and inhibitor analyses revealed that Dis3 is required for correct kinetochore formation and function, and that this activity is monitored by the Mad2 checkpoint. Dis3 is a member of the highly conserved RNase II family and is known to be an essential subunit of the exosome complex. The dis3-54 mutation was found to alter the RNaseII domain of Dis3, which caused a reduction in ribonuclease activity in vitro. This was associated with loss of silencing of an ura4(+) reporter gene inserted into the outer repeats (otr) and central core (cnt and imr) regions of the centromere. On the other hand, centromeric siRNA maturation and formation of the RITS RNAi effector complex was normal in the dis3-54 mutant. Micrococcal nuclease assay also suggested the overall chromatin structure of the centromere was not affected in dis3-54 mutant.\nRNase activity of Dis3, a core subunit of exosome, was found to be required for proper kinetochore formation and establishment of kinetochore-microtubule interactions. Moreover, Dis3 was suggested to contribute to kinetochore formation through an involvement in heterochromatic silencing at both outer centromeric repeats and within the central core region. This activity is likely monitored by the mitotic checkpoint, and distinct from that of RNAi-mediated heterochromatin formation directly targeting outer centromeric repeats.","authors":"Murakami H, Goto DB, Toda T, Chen ES, Grewal SI, Martienssen RA, Yanagida M","authors_abbrev":"Murakami H et al.","pubmed_publication_date":"21 Mar 2007","pubmed_entrez_date":"2007-03-24","publication_year":"2007","canto_session_key":"c0d2e41f4397cf86","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-05-10 14:59:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-12 12:41:42","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.10","SPCC1322.12c","SPAC664.01c","SPBC20F10.06","SPCC188.13c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2014-09-12"},{"uniquename":"PMID:12000964","title":"Cnd2 has dual roles in mitotic condensation and interphase.","citation":"Nature 2002 May 09;417(6885):197-202","abstract":"Chromosome condensation requires condensin, which comprises five subunits. Two of these subunits--both being structural maintenance of chromosome (SMC) proteins-are coiled-coils with globular terminal domains that interact with ATP and DNA. The remaining three, non-SMC subunits also have essential, albeit undefined, roles in condensation. Here we report that Cnd2 (ref. 6), a non-SMC subunit of fission yeast similar to Drosophila Barren and the budding yeast protein Brn1 (refs 8, 9), is required for both interphase and mitotic condensation. In cnd2-1 mutants, ultraviolet-induced DNA damage is not repaired, and cells arrested by hydroxyurea do not recover. A definitive defect of interphase is abolishment of Cds1 (a checkpoint kinase) activation in the presence of hydroxyurea in both cnd2-1 mutant cells and in cells where other condensin subunits have been genetically disrupted. In the absence of hydroxyurea, a G2 checkpoint delay occurred in cnd2-1 mutants in a manner dependent on Cds1 and ATM-like Rad3, but not Chk1 (refs 10-13), before the mitotic condensation defect. Furthermore, cnd2-1 was synthetic-lethal with mutations of excision repair, RecQ helicase and DNA replication enzymes. These interphase and mitotic defects provide insight into the mechanistic role of non-SMC subunits that interact with the globular SMC domains in the heteropentameric holocomplex.","authors":"Aono N, Sutani T, Tomonaga T, Mochida S, Yanagida M","authors_abbrev":"Aono N et al.","pubmed_publication_date":"09 May 2002","pubmed_entrez_date":"2002-05-10","publication_year":"2002","canto_session_key":"c2d743509dce790c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-24 08:37:37","canto_approved_date":"2026-01-29 14:54:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-01 14:03:45","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":48,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.14","SPCC306.03c","SPBC216.05","SPAC20G8.01","SPBC3E7.08c","SPBC776.13","SPBC146.03c","SPBP4H10.06c","SPBC19C7.09c","SPBC342.05","SPAC2G11.12","SPCC1259.13","SPCC18B5.11c","SPAC1F7.05","SPCC188.03"],"gene_count":15,"ltp_gene_count":14,"approved_date":"2019-01-24"},{"uniquename":"PMID:2398900","title":"Evolutionary origin of the U6 small nuclear RNA intron.","citation":"Mol Cell Biol 1990 Oct;10(10):5548-52","abstract":"U6 is the most conserved of the five small nuclear RNAs known to participate in pre-mRNA splicing. In the fission yeast Schizosaccharomyces pombe, the single-copy gene encoding this RNA is itself interrupted by an intron (T. Tani and Y. Ohshima, Nature (London) 337:87-90, 1989). Here we report analysis of the U6 genes from all four Schizosaccharomyces species, revealing that each is interrupted at an identical position by a homologous intron; in other groups, including ascomycete and basidiomycete fungi, as well as more distantly related organisms, the U6 gene is colinear with the RNA. The most parsimonious interpretation of our data is that the ancestral U6 gene did not contain an intron, but rather, it was acquired via a single relatively recent insertional event.","authors":"Reich C, Wise JA","authors_abbrev":"Reich C et al.","pubmed_publication_date":"Oct 1990","pubmed_entrez_date":"1990-10-01","publication_year":"1990","canto_session_key":"651f8e17316a44f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-12-05 09:45:53","canto_approved_date":"2019-12-05 09:45:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-05 09:45:43","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-12-05"},{"uniquename":"PMID:9016592","title":"Identification of a predominant replication origin in fission yeast.","citation":"Nucleic Acids Res 1997 Feb 01;25(3):530-7","abstract":"We have identified five autonomously replicating sequences (ARSs) in a 100 kbp region of the Schizosaccharomyces pombe chromosome II. Analyses of replicative intermediates of the chromosome DNA by neutral/neutral two-dimensional gel electrophoresis demonstrated that at least three of these ARS loci operate as chromosomal replication origins. One of the loci,ori2004, was utilized in almost every cell cycle, while the others were used less frequently. The frequency of initiation from the respective chromosomal replication origin was found to be roughly proportional to the efficiency of autonomous replication of the corresponding ARS plasmid. Replication from ori2004 was initiated within a distinct region almost the same as that for replication of the ARS plasmid. These results showed that the ori2004 region of approximately 3 kbp contains all the cis elements essential for initiation of chromosome replication.","authors":"Okuno Y, Okazaki T, Masukata H","authors_abbrev":"Okuno Y et al.","pubmed_publication_date":"01 Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1943699","title":"Thirty-three nucleotides of 5' flanking sequence including the 'TATA' box are necessary and sufficient for efficient U2 snRNA transcription in Schizosaccharomyces pombe.","citation":"Mol Microbiol 1991 Jul;5(7):1621-5","abstract":"We have sequenced the 5' flanking region of the U2 gene and compared this with the 5' flanking sequences of other snRNA genes from Schizosaccharomyces pombe. This revealed no regions of clear homology 5' to a region surrounding the 'TATA' box at -32 to -29. Deletion analysis shows that a 5' flanking region extending to only -33 is sufficient for accurate and efficient transcription of U2 in Schizosaccharomyces pombe.","authors":"Dandekar T, Tollervey D","authors_abbrev":"Dandekar T et al.","pubmed_publication_date":"Jul 1991","pubmed_entrez_date":"1991-07-01","publication_year":"1991","canto_session_key":"6486be0c077d9f0b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-12-22 13:14:00","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-23 15:30:23","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-23"},{"uniquename":"PMID:27630562","title":"Cerebral Blood Flow Alterations as Assessed by 3D ASL in Cognitive Impairment in Patients with Subcortical Vascular Cognitive Impairment: A Marker for Disease Severity.","citation":"Front Aging Neurosci 2016;8:211","abstract":"Abnormal reductions in cortical cerebral blood flow (CBF) have been identified in subcortical vascular cognitive impairment (SVCI). However, little is known about the pattern of CBF reduction in relation with the degree of cognitive impairment. CBF measured with three-dimensional (3D) Arterial Spin Labeling (ASL) perfusion magnetic resonance imaging (MRI) helps detect functional changes in subjects with SVCI. We aimed to compare CBF maps in subcortical ischemic vascular disease (SIVD) subjects with and without cognitive impairment and to detect the relationship of the regions of CBF reduction in the brain with the degree of cognitive impairment according to the z-score. A total of 53 subjects with SVCI and 23 matched SIVD subjects without cognitive impairment (controls), underwent a whole-brain 3D ASL MRI in the resting state. Regional CBF (rCBF) was compared voxel wise by using an analysis of variance design in a statistical parametric mapping program, with patient age and sex as covariates. Correlations were calculated between the rCBF value in the whole brain and the z-score in the 53 subjects with SVCI. Compared with the control subjects, SVCI group demonstrated diffuse decreased CBF in the brain. Significant positive correlations were determined in the rCBF values in the left hippocampus, left superior temporal pole gyrus, right superior frontal orbital lobe, right medial frontal orbital lobe, right middle temporal lobe, left thalamus and right insula with the z-scores in SVCI group. The noninvasively quantified resting CBF demonstrated altered CBF distributions in the SVCI brain. The deficit brain perfusions in the temporal and frontal lobe, hippocampus, thalamus and insula was related to the degree of cognitive impairment. Its relationship to cognition indicates the clinical relevance of this functional marker. Thus, our results provide further evidence for the mechanisms underlying the cognitive deficit in patients with SVCI.","doi":"10.3389/fnagi.2016.00211","authors":"Sun Y, Cao W, Ding W, Wang Y, Han X, Zhou Y, Xu Q, Zhang Y, Xu J","authors_abbrev":"Sun Y et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-09-16","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.10"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:16751090","title":"TFIIIC boxes in the genome.","citation":"Cell 2006 Jun 02;125(5):829-31","abstract":"In this issue of Cell, Noma et al. (2006) show that B-boxes and TFIIIC limit the spread of heterochromatin at the silent mat region in the fission yeast genome. Global analysis of TFIIIC distribution revealed dispersed sites of association that coalesce at the nuclear periphery, suggesting that TFIIIC may act as a barrier throughout the genome.","authors":"Wallrath LL, Geyer PK","authors_abbrev":"Wallrath LL et al.","pubmed_publication_date":"02 Jun 2006","pubmed_entrez_date":"2006-06-06","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37813972","title":"Hem25p is required for mitochondrial IPP transport in fungi.","citation":"Nat Cell Biol 2023 Nov;25(11):1616-1624","abstract":"Coenzyme Q (CoQ, ubiquinone) is an essential cellular cofactor composed of a redox-active quinone head group and a long hydrophobic polyisoprene tail. How mitochondria access cytosolic isoprenoids for CoQ biosynthesis is a longstanding mystery. Here, via a combination of genetic screening, metabolic tracing and targeted uptake assays, we reveal that Hem25p-a mitochondrial glycine transporter required for haem biosynthesis-doubles as an isopentenyl pyrophosphate (IPP) transporter in Saccharomyces cerevisiae. Mitochondria lacking Hem25p failed to efficiently incorporate IPP into early CoQ precursors, leading to loss of CoQ and turnover of CoQ biosynthetic proteins. Expression of Hem25p in Escherichia coli enabled robust IPP uptake and incorporation into the CoQ biosynthetic pathway. HEM25 orthologues from diverse fungi, but not from metazoans, were able to rescue hem25∆ CoQ deficiency. Collectively, our work reveals that Hem25p drives the bulk of mitochondrial isoprenoid transport for CoQ biosynthesis in fungi.","doi":"10.1038/s41556-023-01250-5","authors":"Tai J, Guerra RM, Rogers SW, Fang Z, Muehlbauer LK, Shishkova E, Overmyer KA, Coon JJ, Pagliarini DJ","authors_abbrev":"Tai J et al.","pubmed_publication_date":"Nov 2023","pubmed_entrez_date":"2023-10-09","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC823.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28799069","title":"Rae1-mediated nuclear export of Rnc1 is an important determinant in controlling MAPK signaling.","citation":"Curr Genet 2018 Feb;64(1):103-108","abstract":"In eukaryotic cells, RNA binding proteins (RBPs) play critical roles in regulating almost every aspect of gene expression, often shuttling between the nucleus and the cytoplasm. They are also key determinants in cell fate via controlling the target mRNAs under the regulation of various signaling pathways in response to environmental stresses. Therefore, understanding the mechanisms that couple the location of mRNA and RBPs is a major challenge in the field of gene expression and signal responses. In fission yeast, a KH-type RBP Rnc1 negatively regulates MAPK signaling activation via mRNA stabilization of the dual-specificity MAPK phosphatase Pmp1, which dephosphorylates MAPK Pmk1. Rnc1 also serves as a target of MAPK phosphorylation, which makes a feedback loop mediated by an RBP. We recently discovered that the nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. This strongly suggested the presence of an mRNA-export system, which recognizes the mRNA/RBP complex and dictates the location and post-transcriptional regulation of mRNA cargo. Here, we briefly review the known mechanisms of general nuclear transporting systems, with an emphasis on our recent findings on the spatial regulation of Rnc1 and its impact on the regulation of the MAPK signal transduction cascade.","doi":"10.1007/s00294-017-0732-5","authors":"Satoh R, Hagihara K, Sugiura R","authors_abbrev":"Satoh R et al.","pubmed_publication_date":"Feb 2018","pubmed_entrez_date":"2017-08-12","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-08-13 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16A3.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26774782","title":"Temporal Regulation of Lipin Activity Diverged to Account for Differences in Mitotic Programs.","citation":"Curr Biol 2016 Jan 25;26(2):237-243","abstract":"Eukaryotes remodel the nucleus during mitosis using a variety of mechanisms that differ in the timing and the extent of nuclear envelope (NE) breakdown. Here, we probe the principles enabling this functional diversity by exploiting the natural divergence in NE management strategies between the related fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus [1-3]. We show that inactivation of Ned1, the phosphatidic acid phosphatase of the lipin family, by CDK phosphorylation is both necessary and sufficient to promote NE expansion required for \"closed\" mitosis in S. pombe. In contrast, Ned1 is not regulated during division in S. japonicus, thus limiting membrane availability and necessitating NE breakage. Interspecies gene swaps result in phenotypically normal divisions with the S. japonicus lipin acquiring an S. pombe-like mitotic phosphorylation pattern. Our results provide experimental evidence for the mitotic regulation of phosphatidic acid flux and suggest that the regulatory networks governing lipin activity diverged in evolution to give rise to strikingly dissimilar mitotic programs.","doi":"10.1016/j.cub.2015.11.061","authors":"Makarova M, Gu Y, Chen JS, Beckley JR, Gould KL, Oliferenko S","authors_abbrev":"Makarova M et al.","pubmed_publication_date":"25 Jan 2016","pubmed_entrez_date":"2016-01-18","publication_year":"2016","canto_session_key":"59369ed763d96a6b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16200506","title":"Additional vectors for PCR-based gene tagging in Saccharomyces cerevisiae and Schizosaccharomyces pombe using nourseothricin resistance.","citation":"Yeast 2005 Oct 15;22(13):1061-8","abstract":"The one-step PCR-mediated technique used for modification of chromosomal loci is a powerful tool for functional analysis in yeast. Both Saccharomyces cerevisiae and Schizosaccharomyces pombe are amenable to this technique. However, the scarce availability of selectable markers for Sz. pombe hampers the easy use of this technique in this species. Here, we describe the construction of new vectors deriving from the pFA6a family, which are suitable for tagging in both yeasts owing to the presence of a nourseothricin-resistance cassette. These plasmids allow various gene manipulations at chromosomal loci, viz. N- and C-terminal tagging with 3HA (haemagglutinin) or 13Myc epitopes, GST (glutathione S-transferase), 4TAP (tandem affinity purification) and several GFP (green fluorescent protein) isoforms. For N-terminal modifications, the use of different promoters allows constitutive (PADH1) or regulatable (PGAL1) promoters for S. cerevisiae and derivatives of Pnmt1 for Sz. pombe expression.","authors":"Van Driessche B, Tafforeau L, Hentges P, Carr AM, Vandenhaute J","authors_abbrev":"Van Driessche B et al.","pubmed_publication_date":"15 Oct 2005","pubmed_entrez_date":"2005-10-04","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32826315","title":"The intermembrane space protein Mix23 is a novel stress-induced mitochondrial import factor.","citation":"J Biol Chem 2020 Oct 23;295(43):14686-14697","abstract":"The biogenesis of mitochondria requires the import of hundreds of precursor proteins. These proteins are transported post-translationally with the help of chaperones, meaning that the overproduction of mitochondrial proteins or the limited availability of chaperones can lead to the accumulation of cytosolic precursor proteins. This imposes a severe challenge to cytosolic proteostasis and triggers a specific transcription program called the mitoprotein-induced stress response, which activates the proteasome system. This coincides with the repression of mitochondrial proteins, including many proteins of the intermembrane space. In contrast, herein we report that the so-far-uncharacterized intermembrane space protein Mix23 is considerably up-regulated when mitochondrial import is perturbed. Mix23 is evolutionarily conserved and a homolog of the human protein CCDC58. We found that, like the subunits of the proteasome, Mix23 is under control of the transcription factor Rpn4. It is imported into mitochondria by the mitochondrial disulfide relay. Mix23 is critical for the efficient import of proteins into the mitochondrial matrix, particularly if the function of the translocase of the inner membrane 23 is compromised such as in temperature-sensitive mutants of Tim17. Our observations identify Mix23 as a novel regulator or stabilizer of the mitochondrial protein import machinery that is specifically up-regulated upon mitoprotein-induced stress conditions.","doi":"10.1074/jbc.RA120.014247","authors":"Zöller E, Laborenz J, Krämer L, Boos F, Räschle M, Alexander RT, Herrmann JM","authors_abbrev":"Zöller E et al.","pubmed_publication_date":"23 Oct 2020","pubmed_entrez_date":"2020-08-23","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC338.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21247416","title":"Ubiquitin-proteasome genes as targets for modulation of cisplatin sensitivity in fission yeast.","citation":"BMC Genomics 2011 Jan 19;12:44","abstract":"The ubiquitin(Ub)-proteasome pathway is implicated in the regulation of a variety of cellular functions and plays a major role in stress response in eukaryotic cells, by targeting misfolded and damaged proteins for degradation. In addition, in the presence of DNA damage, the Ub-proteasome system regulates proteins involved in sensing, repairing, and/or tolerating the damage. Antitumor agents such as cisplatin can activate the pathway, but the role of specific pathway components in cell sensitivity/response to the drug is not known. Since platinum compounds represent clinically relevant antitumor agents and a major limitation to their use is the development of drug resistance, there is an urgent need for identifying targets for improving their efficacy.\nIn the present study, we performed a genome-wide screening for sensitivity to cisplatin using non-essential haploid deletion mutants of the fission yeast Schizosaccharomyces pombe, belonging to a collection of haploid strains constructed through homologous recombination. Using this approach, we identified three Ub-proteasome mutants exhibiting hypersensitivity to cisplatin (ubp16, ubc13 and pmt3) and ten mutants (including ufd2, beta7 20S, rpt6/let1) resistant to the drug. In addition, the importance of lub1 gene emerged from the comparison between the present screening and gene expression profile data previously obtained in fission yeast.\nThe factors identified in the present study allowed us to highlight most finely the close relationship between the Ub-proteasome system and DNA damage response mechanisms, thus establishing a comprehensive framework of regulators likely relevant also in higher eukaryotes. Our results provide the proof of principle of the involvement of specific genes modulated by cisplatin treatment in cell response to the drug, suggesting their potential role as targets for modulating cisplatin sensitivity. In this regard, the prospective identification of novel targets for modulation of cisplatin sensitivity in an eukaryotic model organism appears particularly intriguing towards the discovery of strategies to overcome cisplatin resistance in human tumors.","doi":"10.1186/1471-2164-12-44","authors":"Gatti L, Hoe KL, Hayles J, Righetti SC, Carenini N, Bo LD, Kim DU, Park HO, Perego P","authors_abbrev":"Gatti L et al.","pubmed_publication_date":"19 Jan 2011","pubmed_entrez_date":"2011-01-21","publication_year":"2011","canto_session_key":"ac31b02402fe243c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-24 12:15:22","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-24 12:15:06","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":47,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_21247416_phaf.tsv"}],"genes":["SPBC2D10.20","SPBP8B7.27","SPBP8B7.21","SPBC409.06","SPBC800.12c","SPBC2A9.04c","SPBC15C4.06c","SPBC6B1.06c","SPAC1805.15c","SPBC1198.09","SPBC19C2.04c","SPAC17G8.10c","SPCC790.02","SPBC19C7.02","SPCC1442.07c","SPBC16E9.11c","SPAC17C9.13c","SPAC6G9.08","SPBC530.03c","SPAC6G10.11c","SPAC31G5.18c","SPAC10F6.07c","SPBC23G7.12c","SPBC365.06","SPAC11E3.04c","SPAC15A10.11","SPCC1682.16","SPAC13A11.04c","SPAC167.07c","SPCC1919.15","SPCC1682.12c","SPBC106.16","SPAC1250.03","SPBC216.05","SPBC887.04c","SPAC12B10.01c","SPAC20H4.10","SPBC577.10","SPBC19G7.09","SPBC18H10.08c","SPAC24H6.03","SPAC26A3.16","SPAC27F1.03c","SPBC16G5.03","SPBC6B1.05c","SPAC23G3.08c","SPCC188.08c"],"gene_count":47,"ltp_gene_count":0,"approved_date":"2014-07-24"},{"uniquename":"PMID:23456716","title":"Clades of γ-glutamyltransferases (GGTs) in the ascomycota and heterologous expression of Colletotrichum graminicola CgGGT1, a member of the pezizomycotina-only GGT clade.","citation":"J Microbiol 2013 Feb;51(1):88-99","abstract":"Gamma-glutamyltransferase (GGT, EC 2.3.2.2) cleaves the γ-glutamyl linkage in glutathione (GSH). Ascomycetes in either the Saccharomycotina or the Taphrinomycotina have one to three GGTs, whereas members of the Pezizomycotina have two to four GGTs. A Bayesian analysis indicates there are three well-supported main clades of GGTs in the Ascomycota. 1) A Saccharomycotina and a Taphrinomycotina-specific GGT sub-clade form a yeast main clade. This clade has the three relatively well-characterized fungal GGTs: (Saccharomyces cerevisiae CIS2 and Schizosaccharomyces pombe Ggt1 and Ggt2) and most of its members have all 14 of the highly conserved and critical amino acids that are found in GGTs in the other kingdoms. 2) In contrast, a main clade (GGT3) differs in 11 of the 14 highly conserved amino acids that are found in GGTs in the other kingdoms. All of the 44 Pezizomycotina analyzed have either one or two GGT3s. 3) There is a Pezizomycotina-only GGT clade that has two well-supported sub-clades (GGT1 and GGT2); this clade differs in only two of the 14 highly conserved amino acids found in GGTs in the other kingdoms. Because the Pezizomycotina GGTs differ in apparently critical amino acids from the cross-kingdom consensus, a putative GGT from Colletotrichum graminicola, a member of the Pezizomycotina, was cloned and the protein product was expressed as a secreted protein in Pichia pastoris. A GGT enzyme assay of the P. pastoris supernatant showed that the recombinant protein was active, thereby demonstrating that CgGGT1 is a bona fide GGT.","doi":"10.1007/s12275-013-2434-0","authors":"Bello MH, Epstein L","authors_abbrev":"Bello MH et al.","pubmed_publication_date":"Feb 2013","pubmed_entrez_date":"2013-03-05","publication_year":"2013","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000021","title":"Improving the representation of central nervous system development in the biological process ontology","abstract":"Current genetic and molecular studies in many model organisms are aimed at understanding formation and development of the nervous system. Up until this point, the GO has had a very shallow representation of processes pertaining to the nervous system. In June 2006, curators from MGI and ZFIN met with researchers studying central nervous system development to improve the representation of these processes in GO. In particular, emphasis was placed on three areas that are being addressed actively in current research: forebrain development, hindbrain development and neural tube development. This collaboration resulted in the addition of over 500 terms that reflect the development of the forebrain, the hindbrain, and the neural tube from the perspective of biological process and anatomical structure.","authors":"Judith Blake (1, 2), William Bug (3), Rex Chisholm (1, 4), Jennifer Clark (1, 5), Erika Feltrin (6), Jacqueline Finger (2), David Hill (1, 2), Midori Harris (1, 5), Terry Hayamizu (2), Doug Howe (9), Maryanne Martone (7), Kathleen Millen (8), Francis Sele (4) (1. The Gene Ontology Consortium, 2. Mouse Genome Informatics, Bar Harbor, ME, 3. Drexel University, Philadelphia, PA, 4. Northwestern University, Chicago, IL, 5. EMBL-EBI, Hinxton, Cambridgeshire, UK, 6. The University of Padua, Padua, Italy, 7. The University of California at San Diego, San Diego, CA, 8. The University of Chicago, Chicago, IL, 9. The Zebrafish Information Network, University of Oregon, Eugene, OR)","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28752814","title":"A Matter of Scale and Dimensions: Chromatin of Chromosome Landmarks in the Fungi.","citation":"Microbiol Spectr 2017 Jul;5(4)","abstract":"Chromatin and chromosomes of fungi are highly diverse and dynamic, even within species. Much of what we know about histone modification enzymes, RNA interference, DNA methylation, and cell cycle control was first addressed in  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe ,  Aspergillus nidulans , and  Neurospora crassa . Here, we examine the three landmark regions that are required for maintenance of stable chromosomes and their faithful inheritance, namely, origins of DNA replication, telomeres and centromeres. We summarize the state of recent chromatin research that explains what is required for normal function of these specialized chromosomal regions in different fungi, with an emphasis on the silencing mechanism associated with subtelomeric regions, initiated by sirtuin histone deacetylases and histone H3 lysine 27 (H3K27) methyltransferases. We explore mechanisms for the appearance of \"accessory\" or \"conditionally dispensable\" chromosomes and contrast what has been learned from studies on genome-wide chromosome conformation capture in  S. cerevisiae ,  S. pombe ,  N. crassa , and  Trichoderma reesei . While most of the current knowledge is based on work in a handful of genetically and biochemically tractable model organisms, we suggest where major knowledge gaps remain to be closed. Fungi will continue to serve as facile organisms to uncover the basic processes of life because they make excellent model organisms for genetics, biochemistry, cell biology, and evolutionary biology.","doi":"10.1128/microbiolspec.FUNK-0054-2017","authors":"Erlendson AA, Friedman S, Freitag M","authors_abbrev":"Erlendson AA et al.","pubmed_publication_date":"Jul 2017","pubmed_entrez_date":"2017-07-29","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-07-30 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1988457","title":"The chromatin structure of centromeres from fission yeast: differentiation of the central core that correlates with function.","citation":"J Cell Biol 1991 Jan;112(2):191-201","abstract":"We have examined the chromatin structure of centromere regions from the fission yeast Schizosaccharomyces pombe. The large and complex centromere regions of the S. pombe chromosomes encompass many kilobase pairs of DNA and contain several classes of tandemly repeated DNA sequences. The repeated sequences are further organized into a large inverted repeat flanking a central core, a conserved structural feature among all three centromeres in S. pombe. The nucleosomal configuration of the centromere regions is nonuniform and highly varied. Most of the centromere-specific repeated DNA sequences are packaged into nucleosomes typical of bulk chromatin. However, the central core and core-associated repeated sequences from the centromere regions of chromosomes I (cen1) and II (cen2), when present in S. pombe, show an altered chromatin structure, with little or no evidence of regular nucleosomal packaging. The atypical chromatin organization of the cen2 central core is not due to transcription, as no transcripts from this region were detected. These same DNA sequences, however, are packaged into nucleosomes typical of bulk chromatin when present in a nonfunctional environment on a minichromosome in the budding yeast Saccharomyces cerevisiae. Because the cen2 central core sequences themselves do not preclude regular nucleosomal packaging, we speculate that in S. pombe they constitute a specialized site of kinetochore protein assembly. The atypical nucleosomal pattern of the cen2 central core remains constant during the cell cycle, with only minor differences observed for some sequences. We propose that the unusual chromatin organization of the core region forms the basis of a higher order structural differentiation that distinguishes the centromere from the chromosome arms and specifies the essential structure for centromere function.","authors":"Polizzi C, Clarke L","authors_abbrev":"Polizzi C et al.","pubmed_publication_date":"Jan 1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_session_key":"2a555c6a69300e78","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-02 13:45:12","canto_approved_date":"2019-01-02 13:45:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 21:57:01","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-02"},{"uniquename":"PMID:8898110","title":"The activity of the gluconate-H+ symporter of Schizosaccharomyces pombe cells is down-regulated by D-glucose and exogenous cAMP.","citation":"FEBS Lett 1996 Oct 21;395(2-3):272-6","abstract":"Schizosaccharomyces pombe cells take up D-gluconate, as an alternative carbon source for growth, during glucose starvation or when cultured on glycerol-containing medium. Gluconate uptake is not detectable while cells are growing logarithmically on glucose. The addition of D-glucose as well as its non-metabolizable analogues to glycerol-grown cells causes an immediate loss of gluconate transport within 1 min. The reversible down-regulation of the gluconate carrier occurs after glucose has been internalized. This regulation is triggered not only by D-glucose but also by extracellular cAMP even in the absence of the cAMP-dependent protein kinase (PKA1).","authors":"Caspari T, Urlinger S","authors_abbrev":"Caspari T et al.","pubmed_publication_date":"21 Oct 1996","pubmed_entrez_date":"1996-10-21","publication_year":"1996","canto_session_key":"224fc1be175a11d5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-12-06 11:31:21","canto_approved_date":"2024-12-06 11:31:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-12-06 11:31:16","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":2,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-12-06"},{"uniquename":"PMID:18096621","title":"Site-specific recombination in Schizosaccharomyces pombe and systematic assembly of a 400kb transgene array in mammalian cells using the integrase of Streptomyces phage phiBT1.","citation":"Nucleic Acids Res 2008 Jan;36(1):e9","abstract":"We have established the integrase of the Streptomyces phage phiBT1 as a tool for eukaryotic genome manipulation. We show that the phiBT1 integrase promotes efficient reciprocal and conservative site-specific recombination in vertebrate cells and in Schizosaccharomyces pombe, thus establishing the utility of this protein for genome manipulation in a wide range of eukaryotes. We show that the phiBT1 integrase can be used in conjunction with Cre recombinase to promote the iterative integration of transgenic DNA. We describe five cycles of iterative integration of a candidate mouse centromeric sequence 80 kb in length into a human mini-chromosome within a human-Chinese hamster hybrid cell line. These results establish the generality of the iterative site-specific integration technique.","authors":"Xu Z, Lee NC, Dafhnis-Calas F, Malla S, Smith MC, Brown WR","authors_abbrev":"Xu Z et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-12-22","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35286671","title":"Methods to Assess Phosphodiesterase and/or Adenylyl Cyclase Activity Via Heterologous Expression in Fission Yeast.","citation":"Methods Mol Biol 2022;2483:93-104","abstract":"Heterologous expression of cyclic nucleotide phosphodiesterases (PDEs) and adenylyl cyclases (ACs) in the fission yeast Schizosaccharomyces pombe can be used in combination with PKA-repressed reporters to either carry out high throughput screens for small molecule inhibitors of these target enzymes or to assess hit compounds and their analogs from such screens. Here, we describe two methods for testing panels of such compounds. The first uses a growth assay for which growth in medium containing the pyrimidine analog 5-fluoro orotic acid (5FOA) occurs in response to inhibiting PDE activity to activate PKA. The second uses mass spectrometry to directly measure the impact of compound treatment to study compounds that modulate either PDE or AC activity.","doi":"10.1007/978-1-0716-2245-2_6","authors":"Domin M, Hoffman CS","authors_abbrev":"Domin M et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-03-14","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-03-16 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1198.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU010355","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"TreeFam:TF329173","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9E9.11","HGNC:390","HGNC:24056","HGNC:389"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:31276301","title":"A unique kinesin-like protein, Klp8, is involved in mitosis and cell morphology through microtubule stabilization.","citation":"Cytoskeleton (Hoboken) 2019 May;76(5):355-367","abstract":"Kinesins are microtubule (MT)-based motors involved in various cellular functions including intracellular transport of vesicles and organelles, and dynamics of chromosomes during cell division. The fission yeast Schizosaccharomyces pombe expresses nine kinesin-like proteins (klps). Klp8 is one of them and has not been characterized yet though it has been reported to localize at the division site. Here, we studied function and localization of Klp8 in S. pombe cells. The gene klp8 +  was not essential for both viability and cytoskeletal organization. Klp8-YFP was concentrated as medial cortical dots during interphase, and organized into a ring at the division site during mitosis. The Klp8 ring seemed to be localized in the space between the actomyosin contractile ring and the plasma membrane. The Klp8 ring shrank as cytokinesis proceeded. In klp8-deleted (Δ) cells, the speed of spindle elongation during anaphase B was slowed down. Overproduction of Klp8 caused bent or elongated cells, in which MTs were abnormally elongated and less dynamic than those in normal cells. Deletion of klp8 +  gene suppressed the delay in mitotic entry in blt1Δ cells. These results suggest that Klp8 is involved in mitosis and cell morphology through MT stabilization.","doi":"10.1002/cm.21551","authors":"Kashiwazaki J, Yoneda Y, Mutoh T, Arai R, Yoshida M, Mabuchi I","authors_abbrev":"Kashiwazaki J et al.","pubmed_publication_date":"May 2019","pubmed_entrez_date":"2019-07-06","publication_year":"2019","canto_session_key":"38c6b56f199ef8a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun Kashiwazaki","canto_first_approved_date":"2019-12-10 18:15:46","canto_approved_date":"2023-05-03 21:40:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-25 11:32:34","canto_added_date":"2019-07-07 00:15:04","annotation_curators":[{"name":"Jun Kashiwazaki","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.05c","SPBC1A4.05","SPAC144.14"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-12-10"},{"uniquename":"PMID:27723196","title":"RNA decay systems enhance reciprocal switching of sense and antisense transcripts in response to glucose starvation.","citation":"Genes Cells 2016 Dec;21(12):1276-1289","abstract":"Antisense RNA has emerged as a crucial regulator of opposite-strand protein-coding genes in the long noncoding RNA (lncRNA) category, but little is known about their dynamics and decay process in the context of a stress response. Antisense transcripts from the fission yeast fbp1 locus (fbp1-as) are expressed in glucose-rich conditions and anticorrelated with transcription of metabolic stress-induced lncRNA (mlonRNA) and mRNA on the sense strand during glucose starvation. Here, we investigate the localization and decay of antisense RNAs at fbp1 and other loci, and propose a model to explain the rapid switch between antisense and sense mlonRNA/mRNA transcription triggered by glucose starvation. We show that fbp1-as shares many features with mRNAs, such as a 5'-cap and poly(A)-tail, and that its decay partially depends upon Rrp6, a cofactor of the nuclear exosome complex involved in 3'-5' degradation of RNA. Fluorescence in situ hybridization and polysome fractionation show that the majority of remaining fbp1-as localizes to the cytoplasm and binds to polyribosomes in glucose-rich conditions. Furthermore, fbp1-as and antisense RNA at other stress-responsive loci are promptly degraded via the cotranslational nonsense-mediated decay (NMD) pathway. These results suggest NMD may potentiate the swift disappearance of antisense RNAs in response to cellular stress.","doi":"10.1111/gtc.12443","authors":"Miki A, Galipon J, Sawai S, Inada T, Ohta K","authors_abbrev":"Miki A et al.","pubmed_publication_date":"Dec 2016","pubmed_entrez_date":"2016-10-11","publication_year":"2016","canto_session_key":"c95c5a109b7d8df9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-10-12 00:15:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28441348","title":"Deoxynucleoside Salvage in Fission Yeast Allows Rescue of Ribonucleotide Reductase Deficiency but Not Spd1-Mediated Inhibition of Replication.","citation":"Genes (Basel) 2017 Apr 25;8(5)","abstract":"In fission yeast, the small, intrinsically disordered protein S-phase delaying protein 1 (Spd1) blocks DNA replication and causes checkpoint activation at least in part, by inhibiting the enzyme ribonucleotide reductase, which is responsible for the synthesis of DNA. The CRL4 Cdt2  E3 ubiquitin ligase mediates degradation of Spd1 and the related protein Spd2 at S phase of the cell cycle. We have generated a conditional allele of CRL4 Cdt2 , by expressing the highly unstable substrate-recruiting protein Cdt2 from a repressible promoter. Unlike Spd1, Spd2 does not regulate deoxynucleotide triphosphate (dNTP) pools; yet we find that Spd1 and Spd2 together inhibit DNA replication upon Cdt2 depletion. To directly test whether this block of replication was solely due to insufficient dNTP levels, we established a deoxy-nucleotide salvage pathway in fission yeast by expressing the human nucleoside transporter human equilibrative nucleoside transporter 1 (hENT1) and the Drosophila deoxynucleoside kinase. We present evidence that this salvage pathway is functional, as 2 µM of deoxynucleosides in the culture medium is able to rescue the growth of two different temperature-sensitive alleles controlling ribonucleotide reductase. However, salvage completely failed to rescue S phase delay, checkpoint activation, and damage sensitivity, which was caused by CRL4 Cdt2  inactivation, suggesting that Spd1-in addition to repressing dNTP synthesis-together with Spd2, can inhibit other replication functions. We propose that this inhibition works at the point of the replication clamp proliferating cell nuclear antigen, a co-factor for DNA replication.","doi":"10.3390/genes8050128","authors":"Fleck O, Fahnøe U, Løvschal KV, Gasasira MU, Marinova IN, Kragelund BB, Carr AM, Hartsuiker E, Holmberg C, Nielsen O","authors_abbrev":"Fleck O et al.","pubmed_publication_date":"25 Apr 2017","pubmed_entrez_date":"2017-04-26","publication_year":"2017","canto_session_key":"a13aff557a7c3ff7","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_session_submitted_date":"2020-12-15 10:10:45","canto_added_date":"2017-04-27 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPAC9E9.08","SPCC1259.13","SPAC29B12.03","SPBC25D12.04","SPAC1952.07","SPAC17H9.19c","SPBC216.05","SPAC664.07c","SPCC18B5.11c","SPAC14C4.13"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:30447028","title":"The plasma membrane H +  -ATPase, a simple polypeptide with a long history.","citation":"Yeast 2019 Apr;36(4):201-210","abstract":"The plasma membrane H +  -ATPase of fungi and plants is a single polypeptide of fewer than 1,000 residues that extrudes protons from the cell against a large electric and concentration gradient. The minimalist structure of this nanomachine is in stark contrast to that of the large multi-subunit F O  F 1  ATPase of mitochondria, which is also a proton pump, but under physiological conditions runs in the reverse direction to act as an ATP synthase. The plasma membrane H +  -ATPase is a P-type ATPase, defined by having an obligatory phosphorylated reaction cycle intermediate, like cation pumps of animal membranes, and thus, this pump has a completely different mechanism to that of F O  F 1  ATPases, which operates by rotary catalysis. The work that led to these insights in plasma membrane H +  -ATPases of fungi and plants has a long history, which is briefly summarized in this review.","doi":"10.1002/yea.3365","authors":"Palmgren M, Morsomme P","authors_abbrev":"Palmgren M et al.","pubmed_publication_date":"Apr 2019","pubmed_entrez_date":"2018-11-18","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-19 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28239447","title":"Yeast help identify cytopathic factors of Zika virus.","citation":"Cell Biosci 2017;7:12","abstract":"Accumulating evidence implicates Zika virus (ZIKV) in pathogenesis of microcephaly in newborns and Guillain-Barré syndrome in adults. However, it remains unclear which viral proteins are responsible for these effects and what are the underlying mechanisms of their pathogenic activity. A recent paper by Drs. Zhao and Gallo, and their colleagues at University of Maryland in Baltimore used fission yeast for genome-wide analysis of ZIKV proteins. They demonstrated cytopathogenic activity for seven ZIKV proteins, anaC, C, prM, M, E, NS2B and NS4A. This activity was shown to be dependent on oxidative stress, and for NS4A they demonstrated involvement of the TOR stress-response pathway. Taken together, the findings presented in this paper provide the basis for further mechanistic studies that potentially can identify therapeutic means to treat neuro and immune complications of ZIKV infection.","doi":"10.1186/s13578-017-0139-5","authors":"Bukrinsky M","authors_abbrev":"Bukrinsky M","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-02-28","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-03-01 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27236021","title":"Quantitative PCR for detection of DNA damage in mitochondrial DNA of the fission yeast Schizosaccharomyces pombe.","citation":"J Microbiol Methods 2016 Aug;127:77-81","abstract":"Quantitative polymerase chain reaction (QPCR) has been employed to detect DNA damage and repair in mitochondrial DNA (mtDNA) of human and several model organisms. The assay also permits the quantitation of relative mtDNA copy number in cells. Here, we developed the QPCR assay primers and reaction conditions for the fission yeast Schizosaccharomyces pombe, an important model of eukaryote biology, not previously described. Under these conditions, long targets (approximately 10kb) in mtDNA were quantitatively amplified using 0.1ng of crude DNA templates without isolation of mitochondria and mtDNA. Quantitative detection of oxidative DNA damage in mtDNA was illustrated by using a DNA template irradiated with UVA in the presence of riboflavin. The damage to mtDNA in S. pombe cells treated with hydrogen peroxide and paraquat was also quantitatively measured. Finally, we found that mtDNA copy number in S. pombe cells increased after transition into a stationary phase and that the damage to mtDNA due to endogenous cellular processes accumulated during chronological aging.","doi":"10.1016/j.mimet.2016.05.023","authors":"Senoo T, Yamanaka M, Nakamura A, Terashita T, Kawano S, Ikeda S","authors_abbrev":"Senoo T et al.","pubmed_publication_date":"Aug 2016","pubmed_entrez_date":"2016-05-29","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-05-30 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35639710","title":"Characterization of canavanine-resistance of cat1 and vhc1 deletions and a dominant any1 mutation in fission yeast.","citation":"PLoS One 2022;17(5):e0269276","abstract":"Positive and counter-selectable markers have been successfully integrated as a part of numerous genetic assays in many model organisms. In this study, we investigate the mechanism of resistance to arginine analog canavanine and its applicability for genetic selection in Schizosaccharomyces pombe. Deletion of both the arginine permease gene cat1 and SPBC18H10.16/vhc1 (formerly mistakenly called can1) provides strong drug resistance, while the single SPBC18H10.16/vhc1 deletion does not have an impact on canavanine resistance. Surprisingly, the widely used can1-1 allele does not encode for a defective arginine permease but rather corresponds to the any1-523C>T allele. The strong canavanine-resistance conferred by this allele arises from an inability to deposit basic amino acid transporters on the cellular membrane. any1-523C>T leads to reduced post-translational modifications of Any1 regulated by the Tor2 kinase. We also demonstrate that any1-523C>T is a dominate allele. Our results uncover the mechanisms of canavanine-resistance in fission yeast and open the opportunity of using cat1, vhc1 and any1 mutant alleles in genetic assays.","doi":"10.1371/journal.pone.0269276","authors":"Ait Saada A, Costa AB, Lobachev KS","authors_abbrev":"Ait Saada A et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-05-31","publication_year":"2022","canto_session_key":"44791e9e5116fe71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Anissia Ait Saada","canto_first_approved_date":"2022-07-01 10:49:14","canto_approved_date":"2022-07-01 10:49:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-06-14 22:39:05","canto_added_date":"2022-06-02 00:15:04","annotation_curators":[{"name":"Anissia Ait Saada","community_curator":true,"annotation_count":7,"orcid":"0000-0002-1302-9246","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18H10.16","SPBC18H10.20c","SPBC216.07c","SPAC869.11"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2022-07-01"},{"uniquename":"PMID:19335619","title":"Codon usage bias is correlated with gene expression levels in the fission yeast Schizosaccharomyces pombe.","citation":"Genes Cells 2009 Apr;14(4):499-509","abstract":"Usage of synonymous codons represents a characteristic pattern of preference in each organism. It has been inferred that such bias of codon usage has evolved as a result of adaptation for efficient synthesis of proteins. Here we examined synonymous codon usage in genes of the fission yeast Schizosaccharomyces pombe, and compared codon usage bias with expression levels of the gene. In this organism, synonymous codon usage bias was correlated with expression levels of the gene; the bias was most obvious in two-codon amino acids. A similar pattern of the codon usage bias was also observed in Saccharomyces cerevisiae, Arabidopsis thaliana and Caenorhabditis elegans, but was not obvious in Oryza sativa, Drosophila melanogaster, Takifugu rubripes and Homo sapiens. As codons of the highly expressed genes have greater influence on translational efficiency than codons of genes expressed at lower levels, it is likely that codon usage in the S. pombe genome has been optimized by translational selection through evolution.","doi":"10.1111/j.1365-2443.2009.01284.x","authors":"Hiraoka Y, Kawamata K, Haraguchi T, Chikashige Y","authors_abbrev":"Hiraoka Y et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-04-02","publication_year":"2009","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12049746","title":"Aberrant nuclear trafficking of La protein leads to disordered processing of associated precursor tRNAs.","citation":"Mol Cell 2002 May;9(5):1113-23","abstract":"Eukaryotic precursor tRNAs undergo extensive processing prior to nuclear export. The first of multiple factors to interact with pre-tRNAs and other nascent transcripts is the La protein. Using suppressor and wild-type tRNAs, we demonstrate that the normal distribution of cellular end-processed and spliced tRNA species is disordered by La proteins that lack a conserved nuclear retention element. Fission yeast or human La mutants that lack this element enter nuclei and stabilize nascent pre-tRNA but are aberrantly exported and fail to support normal tRNA processing. Instead, anomalous 5' and 3' end-containing, spliced tRNAs accumulate, complexed with the mutant La protein. Thus, appropriate nuclear trafficking by La affects the normal order of pre-tRNA processing.","authors":"Intine RV, Dundr M, Misteli T, Maraia RJ","authors_abbrev":"Intine RV et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-06-07","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41339091","title":"Fission yeast Tpt1 is composed of tandem RNA 2'-phosphotransferase and Yae1 domains, both of which are essential for viability.","citation":"RNA 2025 Dec 03;","abstract":"RNA 2'-phosphotransferase Tpt1 is a widely distributed enzyme that removes an internal RNA 2'-phosphate by transfer to NAD+. Tpt1 is essential in fungi, where it erases the 2'-PO4 mark installed by tRNA ligase during tRNA splicing. Tpt1 executes a two-step reaction in which: (i) the RNA 2'-PO4 attacks NAD+ to form an RNA-2'-phospho-(ADP-ribose) intermediate and expel nicotinamide; and (ii) the ADP-ribose O2'' attacks the RNA 2'-phosphodiester to form 2'-OH RNA and ADP-ribose-1'',2''-cyclic phosphate products. All Tpt1 enzymes studied to date are monofunctional units comprising a single bilobed fold composed of an RNA-binding lobe and an NAD+-binding lobe. We now find that fission yeast Tpt1 is an exception to this rule. Schizosaccharomyces pombe Tpt1 (SpTpt1) consists of an N-terminal RNA 2'-phosphotransferase catalytic domain (aa 1-237) linked to a C-terminal domain (aa 238-365) homologous to budding yeast iron-sulfur cluster assembly factor Yae1. The SpTpt1 catalytic domain and the Yae1 domain are both essential for S. pombe growth, though they need not be linked within the same polypeptide. A mutational analysis of the 2'-phosphotransferase domain illuminates the distinct contributions of essential active site constituents Arg50 and Arg96 during the two chemical steps of the Tpt1 pathway.","doi":"10.1261/rna.080827.125","authors":"Sarkar A, Schwer B, Shuman S","authors_abbrev":"Sarkar A et al.","pubmed_publication_date":"03 Dec 2025","pubmed_entrez_date":"2025-12-03","publication_year":"2025","canto_session_key":"e372f6e04bf73a52","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-05 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2C4.12c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:14067863","title":"PATTERNS OF SYNTHESIS OF RNA AND OTHER CELL COMPONENTS DURING THE CELL CYCLE OF SCHIZOSACCHAROMYCES POMBE.","citation":"J Cell Comp Physiol 1963 Oct;62:SUPPL1:1-13","abstract":"","authors":"MITCHISON JM","authors_abbrev":"MITCHISON JM","pubmed_publication_date":"Oct 1963","pubmed_entrez_date":"1963-10-01","publication_year":"1963","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9572142","title":"Defective meiosis in telomere-silencing mutants of Schizosaccharomyces pombe.","citation":"Nature 1998 Apr 23;392(6678):825-8","abstract":"During meiotic prophase, chromosomes frequently adopt a bouquet-like arrangement, with their telomeres clustered close to the nuclear periphery. A dramatic example of this occurs in the fission yeast, Schizosaccharomyces pombe, where all telomeres aggregate adjacent to the spindle pole body (SPB). Nuclei then undergo rapid traverses of the cell, known as 'horsetail' movement, which is led by the SPB dragging telomeres and chromosomes behind. This process may initiate or facilitate chromosome pairing before recombination and meiosis. With the aim of identifying components involved in telomere structure and function, we report here the isolation of S. pombe mutants defective in the ability to impose transcriptional silencing on genes placed near telomeres. Two of these mutants, lot2-s17 and lot3-uv3, also display a dramatic lengthening of telomeric repeats. lot3-uv3 carries a mutation in Taz1, a telomere-binding protein containing a Myb-like motif similar to two human telomere-binding proteins. Meiosis is aberrant in these mutant yeast strains, and our analysis demonstrates a decreased association of telomeres with the SPB in meiotic prophase. This results in defective 'horsetail' movement, a significant reduction in recombination, low spore viability and chromosome missegregation through meiosis.","authors":"Nimmo ER, Pidoux AL, Perry PE, Allshire RC","authors_abbrev":"Nimmo ER et al.","pubmed_publication_date":"23 Apr 1998","pubmed_entrez_date":"1998-05-08","publication_year":"1998","canto_session_key":"1d71de220594955f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-11 15:42:57","canto_approved_date":"2022-06-22 16:20:44","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2015-05-11 15:42:50","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.02","SPAC16A10.07c","SPBC428.08c","SPAC26A3.12c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-05-11"},{"uniquename":"PMID:10490657","title":"Association of fission yeast Orp1 and Mcm6 proteins with chromosomal replication origins.","citation":"Mol Cell Biol 1999 Oct;19(10):7228-36","abstract":"We have previously shown that replication of fission yeast chromosomes is initiated in distinct regions. Analyses of autonomous replicating sequences have suggested that regions required for replication are very different from those in budding yeast. Here, we present evidence that fission yeast replication origins are specifically associated with proteins that participate in initiation of replication. Most Orp1p, a putative subunit of the fission yeast origin recognition complex (ORC), was found to be associated with chromatin-enriched insoluble components throughout the cell cycle. In contrast, the minichromosome maintenance (Mcm) proteins, SpMcm2p and SpMcm6p, encoded by the nda1(+)/cdc19(+) and mis5(+) genes, respectively, were associated with chromatin DNA only during the G(1) and S phases. Immunostaining of spread nuclei showed SpMcm6p to be localized at discrete foci on chromatin during the G(1) and S phases. A chromatin immunoprecipitation assay demonstrated that Orp1p was preferentially localized at the ars2004 and ars3002 origins of the chromosome throughout the cell cycle, while SpMcm6p was associated with these origins only in the G(1) and S phases. Both Orp1p and SpMcm6p were associated with a 1-kb region that contains elements required for autonomous replication of ars2004. The results suggest that the fission yeast ORC specifically interacts with chromosomal replication origins and that Mcm proteins are loaded onto the origins to play a role in initiation of replication.","authors":"Ogawa Y, Takahashi T, Masukata H","authors_abbrev":"Ogawa Y et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-09-22","publication_year":"1999","canto_session_key":"0b716f65793f53f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-06-10 15:05:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-09-05 13:51:12","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPBC211.04c","SPBC29A10.15","SPBC14C8.07c","SPBC4.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2012-09-05"},{"uniquename":"PMID:17178839","title":"Fission yeast Cut8 is required for the repair of DNA double-strand breaks, ribosomal DNA maintenance, and cell survival in the absence of Rqh1 helicase.","citation":"Mol Cell Biol 2007 Mar;27(5):1558-67","abstract":"Schizosaccharomyces pombe Rqh1 is a member of the RecQ DNA helicase family. Members of this protein family are mutated in cancer predisposition diseases, causing Bloom's, Werner, and Rothmund-Thomson syndromes. Rqh1 forms a complex with topoisomerase III and is proposed to process or disrupt aberrant recombination structures that arise during S phase to allow proper chromosome segregation during mitosis. Intriguingly, in the absence of Rqh1, processing of these structures appears to be dependent on Rad3 (human ATR) in a manner that is distinct from its role in checkpoint control. Here, we show that rad3 rqh1 mutants are normally committed to a lethal pathway of DNA repair requiring homologous recombination, but blocking this pathway by Rhp51 inactivation restores viability. Remarkably, viability is also restored by overexpression of Cut8, a nuclear envelope protein involved in tethering and proper function of the proteasome. In keeping with a recently described function of the proteasome in the repair of DNA double-strand breaks, we found that Cut8 is also required for DNA double-strand break repair and is essential for proper chromosome segregation in the absence of Rqh1, suggesting that these proteins might function in a common pathway in homologous recombination repair to ensure accurate nuclear division in S. pombe.","authors":"Kearsey SE, Stevenson AL, Toda T, Wang SW","authors_abbrev":"Kearsey SE et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2006-12-21","publication_year":"2007","canto_session_key":"5da5597d14f0cc49","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-08-22 22:29:24","canto_approved_date":"2021-06-01 18:07:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-13 15:21:42","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPAC15A10.03c","SPAC17C9.13c","SPBC216.05","SPCC5E4.04","SPBC14C8.01c","SPAC3C7.03c","SPCC1259.13","SPBC582.03","SPAP27G11.15","SPBC16G5.12c","SPAC644.14c","SPCC18B5.11c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2016-08-22"},{"uniquename":"EMBL:AU010290","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006773","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10395922","title":"Isolation of a novel gene, moc2, encoding a putative RNA helicase as a suppressor of sterile strains in Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1999 Jul 07;1446(1-2):93-101","abstract":"A novel gene designated moc2, which encodes a putative RNA helicase, was isolated from Schizosaccharomyces pombe on the basis of its suppression of the sterility of two different mutant strains, one of which had elevated levels of cAMP and the other deregulated Ras functioning as a result of an ectopic expression of dominant negative RAS2. Moc2 is highly homologous to the RNA helicase DED1 of Saccharomyces cerevisiae (58% identity) and PL10 of mouse (50% identity). Disruption of the moc2 gene indicated that moc2 is essential for cell growth. The moc2 gene seems to have roles in both sexual differentiation and cell growth.","authors":"Kawamukai M","authors_abbrev":"Kawamukai M","pubmed_publication_date":"07 Jul 1999","pubmed_entrez_date":"1999-07-09","publication_year":"1999","canto_session_key":"26e518793dc105a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-30 14:39:36","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 12:23:44","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC19C7.03","SPBC1D7.05","SPAC1D4.13","SPCC1795.11"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2014-06-30"},{"uniquename":"PANTHER:PTHR11560","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:14055","SPAC31A2.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:27723753","title":"Micro-C XL: assaying chromosome conformation from the nucleosome to the entire genome.","citation":"Nat Methods 2016 Dec;13(12):1009-1011","abstract":"We present Micro-C XL, an improved method for analysis of chromosome folding at mononucleosome resolution. Using long crosslinkers and isolation of insoluble chromatin, Micro-C XL increases signal-to-noise ratio. Micro-C XL maps of budding and fission yeast genomes capture both short-range chromosome fiber features such as chromosomally interacting domains and higher order features such as centromere clustering. Micro-C XL provides a single assay to interrogate chromosome folding at length scales from the nucleosome to the full genome.","doi":"10.1038/nmeth.4025","authors":"Hsieh TS, Fudenberg G, Goloborodko A, Rando OJ","authors_abbrev":"Hsieh TS et al.","pubmed_publication_date":"Dec 2016","pubmed_entrez_date":"2016-11-08","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-10-12 00:15:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27881299","title":"Transient RNA-DNA Hybrids Are Required for Efficient Double-Strand Break Repair.","citation":"Cell 2016 Nov 03;167(4):1001-1013.e7","abstract":"RNA-DNA hybrids are a major internal cause of DNA damage within cells, and their degradation by RNase H enzymes is important for maintaining genomic stability. Here, we identified an unexpected role for RNA-DNA hybrids and RNase H enzymes in DNA repair. Using a site-specific DNA double-strand break (DSB) system in Schizosaccharomyces pombe, we showed that RNA-DNA hybrids form as part of the homologous-recombination (HR)-mediated DSB repair process and that RNase H enzymes are essential for their degradation and efficient completion of DNA repair. Deleting RNase H stabilizes RNA-DNA hybrids around DSB sites and strongly impairs recruitment of the ssDNA-binding RPA complex. In contrast, overexpressing RNase H1 destabilizes these hybrids, leading to excessive strand resection and RPA recruitment and to severe loss of repeat regions around DSBs. Our study challenges the existing model of HR-mediated DSB repair and reveals a surprising role for RNA-DNA hybrids in maintaining genomic stability.","doi":"10.1016/j.cell.2016.10.001","authors":"Ohle C, Tesorero R, Schermann G, Dobrev N, Sinning I, Fischer T","authors_abbrev":"Ohle C et al.","pubmed_publication_date":"03 Nov 2016","pubmed_entrez_date":"2016-11-25","publication_year":"2016","canto_session_key":"e211ad5d6e3a443c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-11-26 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.06c","SPAC4G9.02"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:20154645","title":"Silencing in trans: position matters in fission yeast.","citation":"EMBO Rep 2010 Mar;11(3):145-6","abstract":"The distinction in RNAi-mediated gene silencing between metazoans —which mostly use a post-transcriptional RNAi mechanism— and fission yeast —which use a transcriptional RNAi mechanism— seems to be less clear-cut than previously thought. Robin Allshire's group has recently published in  EMBO reports  that  S. pombe  can repress gene expression in  trans , which is reminiscent of mammalian post-transcriptional gene silencing.","doi":"10.1038/embor.2010.24","authors":"Gullerova M, Proudfoot NJ","authors_abbrev":"Gullerova M et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2010-02-16","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22438796","title":"Network evolution: rewiring and signatures of conservation in signaling.","citation":"PLoS Comput Biol 2012;8(3):e1002411","abstract":"The analysis of network evolution has been hampered by limited availability of protein interaction data for different organisms. In this study, we investigate evolutionary mechanisms in Src Homology 3 (SH3) domain and kinase interaction networks using high-resolution specificity profiles. We constructed and examined networks for 23 fungal species ranging from Saccharomyces cerevisiae to Schizosaccharomyces pombe. We quantify rates of different rewiring mechanisms and show that interaction change through binding site evolution is faster than through gene gain or loss. We found that SH3 interactions evolve swiftly, at rates similar to those found in phosphoregulation evolution. Importantly, we show that interaction changes are sufficiently rapid to exhibit saturation phenomena at the observed timescales. Finally, focusing on the SH3 interaction network, we observe extensive clustering of binding sites on target proteins by SH3 domains and a strong correlation between the number of domains that bind a target protein (target in-degree) and interaction conservation. The relationship between in-degree and interaction conservation is driven by two different effects, namely the number of clusters that correspond to interaction interfaces and the number of domains that bind to each cluster leads to sequence specific conservation, which in turn results in interaction conservation. In summary, we uncover several network evolution mechanisms likely to generalize across peptide recognition modules.","doi":"10.1371/journal.pcbi.1002411","authors":"Sun MG, Sikora M, Costanzo M, Boone C, Kim PM","authors_abbrev":"Sun MG et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-03-23","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39509469","title":"Rho1 and Rgf1 establish a new actin-dependent signal to determine growth poles in yeast independently of microtubules and the Tea1-Tea4 complex.","citation":"PLoS Biol 2024 Nov 07;22(11):e3002491","abstract":"Cellular asymmetry begins with the selection of a discrete point on the cell surface that triggers Rho-GTPases activation and localized assembly of the cytoskeleton to establish new growth zones. The cylindrical shape of fission yeast is organized by microtubules (MT) that deliver the landmark Tea1-Tea4 complex at the cell tips to define the growth poles. However, only a few tea1Δ cells mistaken the direction of growth, indicating that they manage to detect their growth sites. Here, we show that Rgf1 (Rho1-GEF) and Tea4 are components of the same complex and that Rgf1 activity toward Rho1 is required for strengthen Tea4 at the cell tips. Moreover, in cells lacking Tea1, selection of the correct growth site depends on Rgf1 and on a correctly polarized actin cytoskeleton, both necessary for Rho1 activation at the pole. We propose an actin-dependent mechanism driven by Rgf1-Rho1 that marks the poles independently of MTs and the Tea1-Tea4 complex.","doi":"10.1371/journal.pbio.3002491","authors":"Garcia P, Celador R, Edreira T, Sanchez Y","authors_abbrev":"Garcia P et al.","pubmed_publication_date":"07 Nov 2024","pubmed_entrez_date":"2024-11-07","publication_year":"2024","canto_session_key":"4b91e1b64edf570f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Patricia Garcia","canto_first_approved_date":"2025-01-31 13:50:41","canto_approved_date":"2025-01-31 13:50:41","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-01-28 10:02:49","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":29,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Patricia Garcia","community_curator":true,"annotation_count":31,"orcid":"0000-0001-7513-1847","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPCC1223.06","SPAC24H6.09","SPBC29B5.01","SPCC1739.11c","SPBC1706.01","SPAC1F7.04","SPCC794.08","SPBC530.04","SPCC645.07"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2025-01-31"},{"uniquename":"PMID:9023111","title":"The fission yeast UVDR DNA repair pathway is inducible.","citation":"Nucleic Acids Res 1997 Mar 01;25(5):1002-8","abstract":"In addition to nucleotide excision repair (NER), the fission yeast Schizosaccharomyces pombe possesses a UV damage endonuclease (UVDE) for the excision of cyclobutane pyrimidine dimers and 6-4 pyrimidine pyrimidones. We have previously described UVDE as part of an alternative excision repair pathway, UVDR, for UV damage repair. The existence of two excision repair processes has long been postulated to exist in S.pombe, as NER-deficient mutants are still proficient in the excision of UV photoproducts. UVDE recognizes the phosphodiester bond immediately 5'of the UV photoproducts as the initiating event in this process. We show here that UVDE activity is inducible at both the level of uve1+ mRNA and UVDE enzyme activity. Further, we show that UVDE activity is regulated by the product of the rad12 gene.","authors":"Davey S, Nass ML, Ferrer JV, Sidik K, Eisenberger A, Mitchell DL, Freyer GA","authors_abbrev":"Davey S et al.","pubmed_publication_date":"01 Mar 1997","pubmed_entrez_date":"1997-03-01","publication_year":"1997","canto_session_key":"0affa773d31418b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-09 11:40:22","canto_approved_date":"2018-06-09 11:40:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-06-09 11:40:14","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.08c","SPBC19C7.09c","SPAC2G11.12","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2018-06-09"},{"uniquename":"PMID:15517003","title":"Organization of a sterol-rich membrane domain by cdc15p during cytokinesis in fission yeast.","citation":"Nat Cell Biol 2004 Nov;6(11):1142-4","abstract":"Many membrane processes occur in discrete membrane domains containing lipid rafts, but little is known about how these domains are organized and positioned. In the fission yeast Schizosaccharomyces pombe, a sterol-rich membrane domain forms at the cell-division site. Here, we show that formation of this membrane domain is independent of the contractile actin ring, septation, mid1p and the septins, and also requires cdc15p, an essential contractile ring protein that associates with lipid rafts. cdc15 mutants have membrane domains in the shape of spirals. Overexpression of cdc15p in interphase cells induces abnormal membrane domain formation in an actin-independent manner. We propose that cdc15p functions to organize lipid rafts at the cleavage site for cytokinesis.","authors":"Takeda T, Kawate T, Chang F","authors_abbrev":"Takeda T et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-11-02","publication_year":"2004","canto_session_key":"19eeb17f636dc21f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-08 11:56:50","canto_approved_date":"2021-10-30 17:08:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-30 17:53:16","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9G1.11c","SPBC24C6.07","SPCC4B3.15","SPBC11C11.02","SPAC11H11.06","SPAC20G8.05c","SPCC1739.11c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2021-01-08"},{"uniquename":"PMID:29852001","title":"New insights into donor directionality of mating-type switching in Schizosaccharomyces pombe.","citation":"PLoS Genet 2018 May;14(5):e1007424","abstract":"Mating-type switching in Schizosaccharomyces pombe entails programmed gene conversion events regulated by DNA replication, heterochromatin, and the HP1-like chromodomain protein Swi6. The whole mechanism remains to be fully understood. Using a gene deletion library, we screened ~ 3400 mutants for defects in the donor selection step where a heterochromatic locus, mat2-P or mat3-M, is chosen to convert the expressed mat1 locus. By measuring the biases in mat1 content that result from faulty directionality, we identified in total 20 factors required for donor selection. Unexpectedly, these included the histone H3 lysine 4 (H3K4) methyltransferase complex subunits Set1, Swd1, Swd2, Swd3, Spf1 and Ash2, the BRE1-like ubiquitin ligase Brl2 and the Elongator complex subunit Elp6. The mutant defects were investigated in strains with reversed donor loci (mat2-M mat3-P) or when the SRE2 and SRE3 recombination enhancers, adjacent to the donors, were deleted or transposed. Mutants in Set1C, Brl2 or Elp6 altered balanced donor usage away from mat2 and the SRE2 enhancer, towards mat3 and the SRE3 enhancer. The defects in these mutants were qualitatively similar to heterochromatin mutants lacking Swi6, the NAD+-dependent histone deacetylase Sir2, or the Clr4, Raf1 or Rik1 subunits of the histone H3 lysine 9 (H3K9) methyltransferase complex, albeit not as extreme. Other mutants showed clonal biases in switching. This was the case for mutants in the NAD+-independent deacetylase complex subunits Clr1, Clr2 and Clr3, the casein kinase CK2 subunit Ckb1, the ubiquitin ligase component Pof3, and the CENP-B homologue Cbp1, as well as for double mutants lacking Swi6 and Brl2, Pof3, or Cbp1. Thus, we propose that Set1C cooperates with Swi6 and heterochromatin to direct donor choice to mat2-P in M cells, perhaps by inhibiting the SRE3 recombination enhancer, and that in the absence of Swi6 other factors are still capable of imposing biases to donor choice.","doi":"10.1371/journal.pgen.1007424","authors":"Maki T, Ogura N, Haber JE, Iwasaki H, Thon G","authors_abbrev":"Maki T et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-06-01","publication_year":"2018","canto_session_key":"bd5224d294af5974","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-10 10:04:42","canto_approved_date":"2024-07-10 10:10:46","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-10 09:29:11","canto_added_date":"2018-06-02 00:15:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":273,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.15","SPBC543.03c","SPCC895.06","SPBC32F12.05c","SPBC354.08c","SPAC20G4.08","SPAC2F7.07c","SPCC320.03","SPAC1F7.01c","SPAC17G8.05","SPAC26A3.04","SPBC839.13c","SPBC17G9.08c","SPAC14C4.06c","SPAC8C9.07","SPAC3G9.07c","SPAC11G7.04","SPAC1142.03c","SPAPB18E9.01","SPAC26A3.07c","SPBC3B8.02","SPBC800.03","SPCC594.05c","SPBC337.16","SPCC338.10c","SPBC14C8.04","SPAC1556.05c","SPBC12C2.07c","SPBC19G7.01c","SPBC19C7.02","SPBC32F12.11","SPAC29B12.02c","SPAC26A3.01","SPCC4B3.17","SPAC5H10.06c","SPAC664.02c","SPBC713.08","SPBC365.03c","SPBC646.12c","SPBC30D10.13c","SPBC1685.07c","SPAC20G4.07c","SPAC2F3.15","SPBC6B1.06c","SPAC3H8.03","SPCC11E10.07c","SPAC824.02","SPAC13C5.07","SPAC1B3.17","SPAC644.15","SPCC188.02","SPBP8B7.22","SPBC337.08c","SPAC6C3.03c","SPBC29A10.03c","SPBP35G2.03c","SPAC14C4.14","SPBC83.13","SPBC16D10.07c","SPCC1450.06c","SPAC3H5.12c","SPBC2D10.07c","SPAC23H4.12","SPAC11E3.06","SPCC4B3.08","SPAC644.07","SPCC613.12c","SPBC16H5.08c","SPAC16C9.05","SPBC947.08c","SPCC338.16","SPAC1556.02c","SPAC29A4.20","SPAC664.01c","SPCC1223.05c","SPBC29A3.02c","SPAC664.03","SPBC16E9.09c","SPBC577.15c","SPBC9B6.07","SPAC4D7.01c","SPAC23C11.10","SPBP22H7.08","SPAPB17E12.05","SPAC25G10.01","SPCC11E10.08","SPCC1259.07","SPAC20H4.10","SPBC16G5.15c","SPBC800.02","SPCC970.05","SPBC2D10.17","SPAC6G9.09c","SPBC651.02","SPAC1F7.13c","SPBC776.02c","SPBC11C11.09c","SPAPB1E7.04c","SPAC13G6.09","SPBC25D12.06","SPBC646.13","SPAC12B10.05","SPCC1906.02c","SPBC1685.02c","SPAC23C4.08","SPCC663.04","SPAC22E12.18","SPAC20H4.07","SPAC30D11.13","SPBC3B9.13c","SPAC19B12.11c","SPBC25H2.09","SPAC3F10.17","SPBC19F5.01c","SPBC31F10.14c","SPBC30D10.10c","SPAC21E11.05c","SPBC2G2.03c","SPBC1306.02","SPCC297.03","SPBC839.17c","SPBC18H10.06c","SPAC694.06c","SPAC23H3.05c","SPAC959.08","SPBC21C3.16c","SPCC1840.06","SPBC651.05c","SPAC5D6.12","SPAC25G10.06","SPBC4C3.12","SPBC839.03c","SPBC14C8.05c","SPAC23C11.02c","SPAC17H9.01","SPBC30D10.04","SPBC15D4.02","SPAC10F6.12c","SPAC3H8.05c","SPAC23H4.17c","SPCC1739.07","SPAC23A1.11","SPAC22A12.04c","SPCC11E10.06c","SPAC144.04c","SPAPB8E5.06c","SPAC31G5.07","SPBC428.08c","SPAC23C4.09c","SPBC1778.01c","SPBC23E6.08","SPAC3H5.07","SPBC660.09","SPAC9G1.03c","SPBC651.12c","SPAC1556.08c","SPAC26H5.09c","SPBC428.15","SPBC409.07c","SPAC4F10.05c","SPAC8F11.03","SPAC23C11.08","SPCC970.10c","SPBC577.02","SPBC3B9.06c","SPAPB1E7.06c","SPAC140.02","SPBC119.06","SPBC1718.07c","SPBC3E7.01","SPBP4H10.05c","SPAC1565.01","SPAC227.17c","SPAC222.12c","SPCC645.07","SPBC1604.07","SPBC21C3.07c","SPAC3G6.02","SPCC970.02","SPAC1952.02","SPCC777.10c","SPAPJ695.01c","SPAPB24D3.08c","SPCC594.06c","SPBC13E7.04","SPAC11E3.03","SPAC17H9.19c","SPAC11D3.15","SPCC74.02c","SPAC31A2.06","SPBC3H7.10","SPAC23C11.06c","SPCC970.01","SPCC1322.02","SPBC1105.04c","SPCC16C4.13c","SPBC1604.20c","SPAC8E11.01c","SPBC16A3.07c","SPAPJ698.02c","SPBC19G7.08c","SPBC29A10.13","SPAC24H6.07","SPBC30D10.09c","SPAC4F10.19c","SPAC11D3.10","SPAC1851.04c","SPAC630.09c","SPBC1711.14","SPAC2F7.02c","SPAC13G7.06","SPAPB1E7.12","SPAC3H1.11","SPCC613.06","SPAC890.05","SPAC167.07c","SPBC16A3.02c","SPBC1604.11","SPBC115.02c","SPBC800.04c","SPAC17H9.14c","SPBC1778.06c","SPAC8C9.10c","SPAC6F6.12","SPAC343.09","SPAC29A4.09","SPAC1786.04","SPBC1861.01c","SPAC1851.03"],"gene_count":229,"ltp_gene_count":229,"approved_date":"2024-07-10"},{"uniquename":"PMID:859590","title":"Frequency of mating-type switching in homothallic fission yeast.","citation":"Nature 1977 Mar 10;266(5598):172-4","abstract":"","authors":"Egel R","authors_abbrev":"Egel R","pubmed_publication_date":"10 Mar 1977","pubmed_entrez_date":"1977-03-10","publication_year":"1977","canto_session_key":"89113516f92bffb5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-24 11:24:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-24 11:24:18","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-24"},{"uniquename":"PMID:1441744","title":"Mutational analysis of Schizosaccharomyces pombe U4 snRNA by plasmid exchange.","citation":"Yeast 1992 Aug;8(8):647-53","abstract":"We have developed a system for testing mutations by plasmid exchange in the fission yeast Schizosaccharomyces pombe. This system has been used to test the requirement for different regions of the small nuclear RNA U4 in S. pombe. Surprisingly, five of seven deletion and substitution mutations tested in different regions of U4 prevent the accumulation of the mutant RNA. Substitution of the U4 sequence in stem 1 of the U4/U6 interaction domain allows accumulation of the mutant U4, but does not support viability. Two sequences with homology to the Sm binding site are found in the 3' region of S. pombe U4; substitution of the 3' sequence of the two does not interfere with accumulation or function of U4, indicating that the 5' sequence is the functional Sm-binding site.","authors":"Dandekar T, Tollervey D","authors_abbrev":"Dandekar T et al.","pubmed_publication_date":"Aug 1992","pubmed_entrez_date":"1992-08-01","publication_year":"1992","canto_session_key":"0704cc17d3874f7f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-06-19 14:20:23","canto_approved_date":"2022-02-23 12:11:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-19 14:20:17","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-19"},{"uniquename":"PMID:6327308","title":"Catabolite repression in yeasts is not associated with low levels of cAMP.","citation":"Eur J Biochem 1984 May 15;141(1):195-8","abstract":"relationship between levels of cAMP and catabolite repression in yeasts has been investigated. Strains of Saccharomyces cerevisiae, Schizosaccharomyces pombe and Kluyveromyces fragilis were used. The yeasts were grown on different carbon sources to attain various degrees of repression. Galactose repressed as much as glucose, while maltose was less effective. Full derepression was achieved with ethanol. The enzymes tested were fructose-bisphosphatase, malate dehydrogenase, glutamate dehydrogenase (NAD dependent), cytochrome oxidase and isocitrate lyase (this last enzyme was found to be absent in Schizosaccharomyces). The levels of cAMP were 2-3 times higher in the repressed conditions than in the derepressed ones. It is therefore concluded that in yeasts catabolite repression is not mediated by a lowering of the intracellular concentration of cAMP.","authors":"Eraso P, Gancedo JM","authors_abbrev":"Eraso P et al.","pubmed_publication_date":"15 May 1984","pubmed_entrez_date":"1984-05-15","publication_year":"1984","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15979554","title":"An agarose-acrylamide composite native gel system suitable for separating ultra-large protein complexes.","citation":"Anal Biochem 2005 Aug 01;343(1):166-75","abstract":"An agarose-acrylamide composite native gel (CNG) system has been developed for separating protein complexes of ultra-large molecular sizes (over 500kDa) and for analyzing protein-protein interactions in their native states. Various native gel conditions were explored and techniques were improved to facilitate the formation and performance of the CNG system. We demonstrate here that the CNG technique is capable of resolving a complex of RNA polymerase II and an associated factor from the free components, which had not been previously achieved with other methods. Furthermore, this CNG electrophoresis can be conveniently coupled to second-dimension sodium dodecyl sulfate-polyacrylamide gel electrophoresis for identification of protein components within discrete complexes separated during the CNG run. The CNG technique is particularly suitable for capturing dynamic protein-protein interactions as exemplified here by the formation and demonstration of RNA polymerase II-Fcp1 complex.","authors":"Suh MH, Ye P, Datta AB, Zhang M, Fu J","authors_abbrev":"Suh MH et al.","pubmed_publication_date":"01 Aug 2005","pubmed_entrez_date":"2005-06-28","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18305313","title":"Thematic review series: sphingolipids. ISC1 (inositol phosphosphingolipid-phospholipase C), the yeast homologue of neutral sphingomyelinases.","citation":"J Lipid Res 2008 May;49(5):922-8","abstract":"Sphingolipid biosynthesis and breakdown in yeast share many homologies in their pathways with higher eukaryotes (Dickson, R. C. 1998. Sphingolipid functions in Saccharomyces cerevisiae: comparison to mammals. Annu. Rev. Biochem. 67: 27-48). In mammals, ceramide can be generated through hydrolysis of sphingomyelin catalyzed by sphingomyelinase (SMase). To date, as many as five SMases have been identified molecularly, separated into three main groups: acid, alkaline, and neutral SMases (nSMases) (Marchesini, N., and Y. Hannun. 2004. Acid and neutral sphingomyelinases: roles and mechanisms of regulation. Biochem. Cell Biol. 82: 27-44). nSMase in mammals is represented by its homolog, inositol phosphosphingolipase C, codified by ISC1 in Saccharomyces cerevisiae (Sc) and Cryptococcus neoformans (Cn) and by CSS1 (Can't Stop Synthesizing cell wall) in Schizosaccharomyces pombe (Sp). Yeasts do not have sphingomyelin but instead have inositol phosphosphingolipids, which may function as orthologs of mammalian sphingomyelin. In this review, we will describe findings related to the function of ISC1, its localization, mechanisms, and its roles in cell response to different types of stresses. These studies serve as a foundation for the elucidation of the properties and functions of the extended family of nSMases.","doi":"10.1194/jlr.R800004-JLR200","authors":"Matmati N, Hannun YA","authors_abbrev":"Matmati N et al.","pubmed_publication_date":"May 2008","pubmed_entrez_date":"2008-02-29","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36068165","title":"Cdc42 GTPase activating proteins Rga4 and Rga6 coordinate septum synthesis and membrane trafficking at the division plane during cytokinesis.","citation":"Traffic 2022 Oct;23(10):478-495","abstract":"Fission yeast cytokinesis is driven by simultaneous septum synthesis, membrane furrowing and actomyosin ring constriction. The septum consists of a primary septum flanked by secondary septa. First, delivery of the glucan synthase Bgs1 and membrane vesicles initiate primary septum synthesis and furrowing. Next, Bgs4 is delivered for secondary septum formation. It is unclear how septum synthesis is coordinated with membrane furrowing. Cdc42 promotes delivery of Bgs1 but not Bgs4. We find that after primary septum initiation, Cdc42 inactivators Rga4 and Rga6 localize to the division site. In rga4Δrga6Δ mutants, Cdc42 activity is enhanced during late cytokinesis and cells take longer to separate. Electron micrographs of the division site in these mutants exhibit malformed septum with irregular membrane structures. These mutants have a larger division plane with enhanced Bgs1 delivery but fail to enhance accumulation of Bgs4 and several exocytic proteins. Additionally, these mutants show endocytic defects at the division site. This suggests that Cdc42 regulates primary septum formation and only certain membrane trafficking events. As cytokinesis progresses Rga4 and Rga6 localize to the division site to decrease Cdc42 activity to allow coupling of Cdc42-independent membrane trafficking events with septum formation for proper septum morphology.","doi":"10.1111/tra.12864","authors":"Campbell BF, Hercyk BS, Williams AR, San Miguel E, Young HG, Das ME","authors_abbrev":"Campbell BF et al.","pubmed_publication_date":"Oct 2022","pubmed_entrez_date":"2022-09-06","publication_year":"2022","canto_session_key":"bab7a8e298726abc","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-09 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:31076844","title":"RNA insertion in DNA as the imprint moiety: the fission yeast paradigm.","citation":"Curr Genet 2019 Dec;65(6):1301-1306","abstract":"This review elaborates on the findings of a new report which possibly resolves the biochemical nature of a novel type of DNA imprint as ribonucleotide and the mechanism of its formation during cell differentiation in fission yeast. The process of mating-type switching in fission yeast, Schizosaccharomyces pombe, displays characteristics of a typical mammalian stem cell lineage, wherein a cell divides to produce an identical cell and a differentiated cell after every two cell divisions. This developmental asymmetry has been ascribed to play a role in generation of a DNA strand-specific imprint at the mat1 locus during lagging strand synthesis and its segregation to one of the two daughter cells by the process of asymmetric, semi-conservative DNA replication. The nature of this imprint and mechanisms of its generation have been a subject of research and debate. A recent report by Singh et al. (Nucleic Acids Res 47:3422-3433. https://doi.org/10.1093/nar/gkz092 , 2019) provides compelling evidence in support of a ribonucleotide as the imprint moiety within the mat1 DNA and demonstrates the role of Mcm10/Cdc23, an important, evolutionarily conserved component of DNA replication machinery in eukaryotes, in installing the imprint through a non-canonical primase activity and interaction with DNA Polα and Swi1. The high degree of conservation of DNA replication machinery, especially the presence of the T7 gene 4 helicase/primase domain in the mammalian orthologs of Mcm10 suggests that similar mechanisms of DNA imprinting may play a role during cell differentiation in metazoans.","doi":"10.1007/s00294-019-00991-x","authors":"Singh J","authors_abbrev":"Singh J","pubmed_publication_date":"Dec 2019","pubmed_entrez_date":"2019-05-12","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-05-13 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39094565","title":"Mapping the dynamics of epigenetic adaptation in S. pombe during heterochromatin misregulation.","citation":"Dev Cell 2024 Jul 26;","abstract":"Epigenetic mechanisms enable cells to develop novel adaptive phenotypes without altering their genetic blueprint. Recent studies show histone modifications, such as heterochromatin-defining H3K9 methylation (H3K9me), can be redistributed to establish adaptive phenotypes. We developed a precision-engineered genetic approach to trigger heterochromatin misregulation on-demand in fission yeast. This enabled us to trace genome-scale RNA and H3K9me changes over time in long-term, continuous cultures. Adaptive H3K9me establishes over remarkably slow timescales relative to the initiating stress. We captured dynamic H3K9me redistribution events which depend on an RNA binding complex MTREC, ultimately leading to cells converging on an optimal adaptive solution. Upon stress removal, cells relax to new transcriptional and chromatin states, establishing memory that is tunable and primed for future adaptive epigenetic responses. Collectively, we identify the slow kinetics of epigenetic adaptation that allow cells to discover and heritably encode novel adaptive solutions, with implications for drug resistance and response to infection.","doi":"10.1016/j.devcel.2024.07.006","authors":"Larkin A, Kunze C, Seman M, Levashkevich A, Curran J, Morris-Evans D, Lemieux S, Khalil AS, Ragunathan K","authors_abbrev":"Larkin A et al.","pubmed_publication_date":"26 Jul 2024","pubmed_entrez_date":"2024-08-02","publication_year":"2024","canto_session_key":"8c76b5840b281ac1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaushik Ragunathan","canto_first_approved_date":"2024-11-14 15:14:39","canto_approved_date":"2025-03-03 16:42:32","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-10-25 19:30:38","canto_added_date":"2024-08-03 23:25:05","annotation_curators":[{"name":"Kaushik Ragunathan","community_curator":true,"annotation_count":20,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":31,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.05","SPBC1711.02","SPBC25B2.02c","SPAC1F8.05","SPBC428.08c","SPAC17G8.13c","SPAC1006.03c","SPBC23G7.13c","SPAC24B11.06c","SPBC23G7.10c","SPAC11H11.04","SPCC622.16c","SPNCRNA.1488","SPCC1494.11c","SPAC513.03","SPAC10F6.12c","SPNCRNA.606","SPCC736.11","SPBC32H8.10","SPAPB8E5.05","SPCC188.13c","SPBC17G9.13c","SPAC513.04"],"gene_count":23,"ltp_gene_count":9,"approved_date":"2024-11-14"},{"uniquename":"PMID:17297868","title":"[Telomere bouquet of meiotic chromosomes].","citation":"Tanpakushitsu Kakusan Koso 2007 Feb;52(2):145-50","abstract":"","authors":"Hiraoka Y","authors_abbrev":"Hiraoka Y","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-02-15","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7744248","title":"The conserved Schizosaccharomyces pombe kinase plo1, required to form a bipolar spindle, the actin ring, and septum, can drive septum formation in G1 and G2 cells.","citation":"Genes Dev 1995 May 01;9(9):1059-73","abstract":"We have identified a Schizosaccharomyces pombe gene with homology to the budding yeast gene CDC5, the Drosophila gene polo, and the mammalian family of genes encoding polo-like kinases. Disruption of this gene, plo1+, indicates that it is essential. Loss of plo1+ function leads to a mitotic arrest in which condensed chromosomes are associated with a monopolar spindle or to the failure of septation following the completion of nuclear division. In the latter case, cells show a failure both in the formation of an F-actin ring and in the deposition of septal material, suggesting that plo1+ function is required high in the regulatory cascade that controls septation. The overexpression of plo1+ in wild-type cells also results in the formation of monopolar spindles but also induces the formation of multiple septa without nuclear division. Septation can also be induced in the absence of mitotic commitment and concomitant spindle formation by the overexpression of plo1+ in cdc25-22 or cdc2-33 cells arrested in G2; in G1 cells arrested at Start by the cdc10-V50 mutation, or in cells lacking the cyclin B homolog cdc13 that undergo repeated S phases in the absence of mitosis.","authors":"Ohkura H, Hagan IM, Glover DM","authors_abbrev":"Ohkura H et al.","pubmed_publication_date":"01 May 1995","pubmed_entrez_date":"1995-05-01","publication_year":"1995","canto_session_key":"9b5adb5a089069ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-09-02 18:04:54","canto_approved_date":"2026-02-17 08:59:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-29 15:23:43","canto_added_date":"2012-02-24 05:54:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-09-02"},{"uniquename":"PMID:1734281","title":"Control of DNA synthesis genes in fission yeast by the cell-cycle gene cdc10+.","citation":"Nature 1992 Jan 30;355(6359):449-53","abstract":"In the budding yeast Saccharomyces cerevisiae, cell-cycle control over DNA synthesis occurs partly through the coordinate expression in late G1 phase of many, if not all, of the genes required for DNA synthesis. A cis-acting hexamer element ACGCGT (an MluI restriction site) is responsible for coordinating transcriptional regulation of these genes at the G1/S phase boundary and we have identified a binding activity, DSC1, that recognizes these sequences in a cell-cycle-dependent manner. In the distantly related fission yeast Schizosaccharomyces pombe, only one of the known DNA synthesis genes, cdc22+, which encodes a subunit of ribonucleotide reductase, is periodically expressed in late G1 (ref. 6). The promoter region of cdc22+ has two MluI sites and five related sequences, suggesting that similar controls over DNA synthesis genes could occur in fission yeast. We report here a binding activity in fission yeast that is very similar to DSC1 in budding yeast. We also show that the fission yeast cdc10+ gene product, which is required for Start and entry into S phase, is a component of this binding activity.","authors":"Lowndes NF, McInerny CJ, Johnson AL, Fantes PA, Johnston LH","authors_abbrev":"Lowndes NF et al.","pubmed_publication_date":"30 Jan 1992","pubmed_entrez_date":"1992-01-30","publication_year":"1992","canto_session_key":"770c340acda1b033","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-04-26 22:50:48","canto_approved_date":"2021-06-11 15:22:52","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-04-26 22:50:43","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPBC336.12c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-04-26"},{"uniquename":"PMID:8628672","title":"DNA-protein interactions at the telomeric repeats of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1996 Apr 15;24(8):1412-9","abstract":"Gel retardation assays using a probe containing the repeat region of a Schizosaccharomyces pombe chromosomal telomere identified four specific DNA- protein complexes in S. pombe total protein extracts (I, I', IIa and IIb). The proteins responsible for these complexes bound to the telomeric repeat region irrespective of whether or not the repeats were in close proximity to the end of a DNA molecule, and none of them bound strongly to single-stranded DNA. The protein responsible for complex I (TeRF I) was separated from the activity responsible for complexes IIa and IIb (TeRF II) using heparin-Sepharose chromatography. Both factors were efficiently cross-competed by an oligonucleotide containing the 18 bp sequence 5'-GGTTACAGGTTACAGGTT-3', which corresponds to two complete telomeric repeat units. Mutation of the T residues at positions 4 and 11 in the oligonucleotide dramatically reduced binding by TeRF II, but had no affect on binding by TeRF I. The protein responsible for complex I' did not bind strongly to either the wild-type or mutant oligonucleotide.","authors":"Duffy M, Chambers A","authors_abbrev":"Duffy M et al.","pubmed_publication_date":"15 Apr 1996","pubmed_entrez_date":"1996-04-15","publication_year":"1996","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD214","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19431238","title":"Fission yeast syt22 protein, a putative Arf guanine nucleotide exchange factor, is necessary for new end take off.","citation":"FEMS Microbiol Lett 2009 May;294(2):191-7","abstract":"In fission yeast Schizosaccharomyces pombe, the directions of cell growth change from monopolar to bipolar in character, which is known as 'new end take off ' (NETO). We previously found that arf6p, a member (class III) of the ADP-ribosylation factor (Arf) family, is necessary for NETO in fission yeast. Here we report the characterization of an S. pombe gene, syt22(+), encoding a putative Arf guanine nucleotide exchange factor (GEF). The syt22 protein contains a Sec7 domain and a PH domain conserved in the mammalian EFA6 GEF family, and has high similarity to Yel1p, which was identified as a GEF for Arf3p (class III Arf) in Saccharomyces cerevisiae. syt22Delta cells, like arf6Delta cells, completely failed to undergo NETO. Syt22p uniformly localizes to the cell periphery. Its localization is not dependent on microtubules, actin cytoskeletons or arf6p. We hypothesize that syt22p functions as a GEF for arf6p.","authors":"Fujita A, Misumi Y","authors_abbrev":"Fujita A et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-05-12","publication_year":"2009","canto_session_key":"c2a157dbb0ccbaa8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-09-07 17:53:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-12 16:21:07","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.11c","SPBC1539.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-07-12"},{"uniquename":"PMID:32777371","title":"Pathways of heme utilization in fungi.","citation":"Biochim Biophys Acta Mol Cell Res 2020 Nov;1867(11):118817","abstract":"Iron acquisition is challenging in most environments. As an alternative to elemental iron, organisms can take up iron-protoporphyrin IX, or heme. Heme can be found in decaying organic matter and is particularly prevalent in animal hosts. Fungi have evolved at least three distinct endocytosis-mediated heme uptake systems, which have been studied in detail in the organisms Candida albicans, Cryptococcus neoformans and Schizosaccharomyces pombe. Here we summarize the known molecular details of these three uptake systems that enable parasitic and saprophytic fungi to take advantage of external heme as either cellular iron or heme sources.","doi":"10.1016/j.bbamcr.2020.118817","authors":"Kornitzer D, Roy U","authors_abbrev":"Kornitzer D et al.","pubmed_publication_date":"Nov 2020","pubmed_entrez_date":"2020-08-11","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-08-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ627891","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F8.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17476701","title":"The txl1+ gene from Schizosaccharomyces pombe encodes a new thioredoxin-like 1 protein that participates in the antioxidant defence against tert-butyl hydroperoxide.","citation":"Yeast 2007 Jun;24(6):481-90","abstract":"Yeasts are equipped with several putative single-domain thioredoxins located in different subcellular compartments. However, additional proteins containing thioredoxin domains are also encoded by the yeast genomes as described for mammals and other eukaryotic organisms. We report here the characterization of the fission yeast orthologue thioredoxin-like 1 (txl1(+)), which has been previously identified in mammals. Similarly to the human protein, the fission yeast Txl1 is a two-domain protein comprising an N-terminal thioredoxin-like domain and a C-terminal domain of unknown function. Many other yeasts and fungi species contain homologues of txl1(+); however, there is no evidence of txl1(+) orthologues in either Saccharomyces cerevisiae or plants. Txl1 is found in both the nucleus and the cytoplasm of Schizosaccharomyces pombe cells and exhibits a strong reducing activity coupled to thioredoxin reductase. In humans, TXL1 expression is induced by glucose deprivation and overexpression of TXL1 confers resistance against this stress. In contrast, a Sz. pombe Deltatxl1 mutant was not affected in the response against glucose starvation but the Deltatxl1 mutant strain showed a clear hypersensitivity to alkyl hydroperoxide. The mRNA levels of txl1(+) in a h20 strain did not change in response to any oxidative insult (hydrogen peroxide or alkyl hydroperoxide) and the overexpression of an integrated copy of the wild-type txl1(+) gene did not confer a significant increased resistance against alkyl hydroperoxide. Overall, these results indicate that the Txl1 role in the cellular detoxification of alkyl hydroperoxide is exerted through a constitutive transcription of txl1(+).","authors":"Jiménez A, Mateos L, Pedrajas JR, Miranda-Vizuete A, Revuelta JL","authors_abbrev":"Jiménez A et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-05-04","publication_year":"2007","canto_session_key":"45a9c137e360e9a6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-27 17:09:23","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-27 17:09:15","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC577.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-27"},{"uniquename":"PMID:26057668","title":"Structural analysis of Dis3l2, an exosome-independent exonuclease from Schizosaccharomyces pombe.","citation":"Acta Crystallogr D Biol Crystallogr 2015 Jun;71(Pt 6):1284-94","abstract":"After deadenylation and decapping, cytoplasmic mRNA can be digested in two opposite directions: in the 5'-3' direction by Xrn1 or in the 3'-5' direction by the exosome complex. Recently, a novel 3'-5' RNA-decay pathway involving Dis3l2 has been described that differs from degradation by Xrn1 and the exosome. The product of the Schizosaccharomyces pombe gene SPAC2C4.07c was identified as a homologue of human Dis3l2. In this work, the 2.8 Å resolution X-ray crystal structure of S. pombe Dis3l2 (SpDis3l2) is reported, the conformation of which is obviously different from that in the homologous mouse Dis3l2-RNA complex. Fluorescence polarization assay experiments showed that RNB and S1 are the primary RNA-binding domains and that the CSDs (CSD1 and CSD2) play an indispensable role in the RNA-binding process of SpDis3l2. Taking the structure comparison and mutagenic experiments together, it can be inferred that the RNA-recognition pattern of SpDis3l2 resembles that of its mouse homologue rather than that of the Escherichia coli RNase II-RNA complex. Furthermore, a drastic conformation change could occur following the binding of the RNA substrate to SpDis3l2.","doi":"10.1107/S1399004715005805","authors":"Lv H, Zhu Y, Qiu Y, Niu L, Teng M, Li X","authors_abbrev":"Lv H et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-06-10","publication_year":"2015","canto_session_key":"4adda085ff88928f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-04-04 12:39:36","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-04-04 12:39:28","canto_added_date":"2015-06-11 00:20:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2C4.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-04-04","pdb_entries":[{"pdb_id":"4ro1","gene_chains":[{"gene_uniquename":"SPAC2C4.07c","chain":"A/B","position":"170-927"}],"title":"An 3'-5'-exoribonuclease that specifically recognizes RNAs.","entry_authors":"Lv H,Zhu Y,Teng M","entry_authors_abbrev":"Lv H et al.","reference_uniquename":"PMID:26057668","experimental_method":"X-ray","resolution":"2.803"}]},{"uniquename":"PMID:8834801","title":"Role of gamma-tubulin in mitosis-specific microtubule nucleation from the Schizosaccharomyces pombe spindle pole body.","citation":"J Cell Sci 1996 Jan;109 ( Pt 1):165-77","abstract":"The ability of the Schizosacchromyces pombe spindle pole body to nucleate microtubules is activated at the onset of mitosis for forming a mitotic spindle, but it is inactivated during interphase. We have previously developed an in vitro assay for studying the molecular mechanism of spindle pole body activation using permeabilized interphase S. pombe cells and Xenopus mitotic extracts. We have shown that the interphase spindle pole body is activated indirectly by p34cdc2 protein kinase in Xenopus mitotic extracts. In this study we examined the role of gamma-tubulin, a component of both interphase and mitotic spindle pole body, in formation of the microtubule nucleating complex at the mitotic spindle pole body. A polyclonal antibody specific to S. pombe gamma-tubulin inhibited both activation of the interphase spindle pole body and microtubule nucleation from the mitotic spindle pole body. Addition of bacterially expressed S. pombe gamma-tubulin or its amino-terminal fragments to Xenopus mitotic extracts inhibited spindle pole body activation. Affinity chromatography of partially fractionated Xenopus mitotic extracts with the amino-terminal fragment of S. pombe gamma-tubulin showed that fractions bound to the fragment supported the activation. The fractions did not contain Xenopus gamma-tubulin, showing that activation of the spindle pole body is not due to recruitment of Xenopus gamma-tubulin to the spindle pole body. The spindle pole body activation occurred in extracts depleted of p34cdc2 protein kinase or MAP kinase. The activity of the fractions bound to the fragment was inhibited by a protein kinase inhibitor, staurosporine. These results suggest that S. pombe gamma-tubulin is a component of the microtubule nucleating complex, and that the function of proteins that interact with gamma-tubulin is required for activation of the spindle pole body. We present possible models for the activation that convert the immature microtubule nucleating complex at interphase into the mature microtubule nucleating complex at mitosis.","authors":"Masuda H, Shibata T","authors_abbrev":"Masuda H et al.","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"35e854953c18ed20","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-26 17:36:01","canto_approved_date":"2022-07-28 07:11:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-22 13:23:07","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-01-26"},{"uniquename":"PMID:8048925","title":"Isolation of UV-inducible transcripts from Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 1994 Jul 29;202(2):1113-9","abstract":"Four UV-inducible cDNA clones, UVI15, UVI18, UVI22 and UVI31, were isolated from Schizosaccharomyces pombe by subtraction hybridization. All transcripts of these clones were rapidly induced about 5 to 10 fold within 1 hour after UV-irradiation and the nucleotide sequences of these clones did not showed any significant sequence homology to the known genes in the data bases. Transcripts of UVI18 and UVI31 were induced only by UV-irradiation and those of UVI22 were also induced by alkylating agents, suggesting that inductions of these transcripts are specific responses to DNA damages. However, transcript levels of UVI15 were also increased by other cytotoxic agents including heat shock. These results indicate that UVI15 might be a stress responsive gene.","authors":"Lee JK, Park EJ, Chung HK, Hong SH, Joe CO, Park SD","authors_abbrev":"Lee JK et al.","pubmed_publication_date":"29 Jul 1994","pubmed_entrez_date":"1994-07-29","publication_year":"1994","canto_session_key":"4946a3cf5e618fb4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-04-27 00:01:31","canto_approved_date":"2019-04-27 00:01:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-04-27 00:01:24","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC649.04","SPBC16E9.06c","SPCC338.11c"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2019-04-27"},{"uniquename":"PMID:2038319","title":"Identification of a GTPase-activating protein homolog in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1991 Jun;11(6):3088-94","abstract":"Loss of function of the Schizosaccharomyces pombe gap1 gene results in the same phenotypes as those caused by an activated ras1 mutation, i.e., hypersensitivity to the mating factor and inability to perform efficient mating. Sequence analysis of gap1 indicates that it encodes a homolog of the mammalian Ras GTPase-activating protein (GAP). The predicted gap1 gene product has 766 amino acids with relatively short N- and C-terminal regions flanking the conserved core sequence of GAP. Genetic analysis suggests that S. pombe Gap1 functions primarily as a negative regulator of Ras1, like S. cerevisiae GAP homologs encoded by IRA1 and IRA2, but is unlikely to be a downstream effector of the Ras protein, a role proposed for mammalian GAP. Thus, Gap1 and Ste6, a putative GDP-GTP-exchanging protein for Ras1 previously identified, appear to play antagonistic roles in the Ras-GTPase cycle in S. pombe. Furthermore, we suggest that this Ras-GTPase cycle involves the ra12 gene product, another positive regulator of Ras1 whose homologs have not been identified in other organisms, which could function either as a second GDP-GTP-exchanging protein or as a factor that negatively regulates Gap1 activity.","authors":"Imai Y, Miyake S, Hughes DA, Yamamoto M","authors_abbrev":"Imai Y et al.","pubmed_publication_date":"Jun 1991","pubmed_entrez_date":"1991-06-01","publication_year":"1991","canto_session_key":"468db0c3950bdbf6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-18 15:44:26","canto_approved_date":"2023-11-29 08:45:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 14:12:14","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.12c","SPBC21.05c","SPAC17H9.09c","SPCC1442.01"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-04-18"},{"uniquename":"PMID:12597869","title":"DNA-RNA-protein gang together in silence.","citation":"Trends Plant Sci 2003 Feb;8(2):53-5","abstract":"Two recent reports demonstrate interdependence between DNA and histone methylation in Arabidopsis. ddm1 (decrease in DNA methylation 1) mutants switch histone methylation from a form associated with inactive chromatin to a form connected to actively transcribed genomic regions. The loss of DNA methylation and shift in histone methylation cause transcriptional derepression of heterochromatic regions. In a related report, small RNAs in Schizosaccharomyces pombe mark histone methylation to form heterochromatin, suggesting that methylation systems work alongside RNA metabolism.","authors":"Stokes T","authors_abbrev":"Stokes T","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-02-25","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40519641","title":"A Chromosome End Without Terminal Telomere Repeats is Stable for Multiple Cell Divisions.","citation":"MicroPubl Biol 2025;2025","abstract":"We have formed new short telomeres in  Schizosaccharomyces pombe  using an inducible nuclease that cuts near telomere repeats in cells that lack, cannot recruit or cannot fully activate telomerase. Sequencing these new telomeres showed that cells can divide at least 4 times with ~30 bp of non-telomeric sequence at the chromosome end in cells lacking telomerase, which contrasts with current models for the roles of terminal single-stranded telomere repeats and the telomere proteins in telomere protection and replication. Cells that cannot recruit or activate telomerase had similar results, with additional terminal truncations or telomere repeat addition.","doi":"10.17912/micropub.biology.001622","authors":"Zhang H, Audry J, Runge KW","authors_abbrev":"Zhang H et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-06-16","publication_year":"2025","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2025-06-16 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8552670","title":"Identification, purification, and molecular cloning of autonomously replicating sequence-binding protein 1 from fission yeast Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1996 Jan 09;93(1):502-7","abstract":"Autonomously replicating sequence (ARS) elements of the fission yeast Schizosaccharomyces pombe contain multiple imperfect copies of the consensus sequence reported by Maundrell et al. [Maundrell K., Hutchison, A. & Shall, S. (1988) EMBO J. 7, 2203-2209]. When cell free extracts of S. pombe were incubated with a dimer or tetramer of an oligonucleotide containing the ARS consensus sequence, several complexes were detected using a gel mobility-shift assay. The proteins forming these complexes also bind ars3002, which is the most active origin in the ura4 region of chromosome III of S. pombe. One protein, partly responsible for the binding activity observed with crude extracts, was purified to near homogeneity. It is a 60-kDa protein and was named ARS-binding protein 1 (Abp1). Abp1 preferentially binds to multiple sites in ARS 3002 and to the DNA polymer poly[d(A.T)]. The cloning and sequence of the gene coding for Abp1 revealed that it encodes a protein of 59.8 kDa (522 amino acids). Abp1 has significant homology (25% identity, 50% similarity) to the N-terminal region (approximately 300 amino acids) of the human and mouse centromere DNA-binding protein CENP-B. Because centromeres of S. pombe contain a high density of ARS elements, Abp1 may play a role connecting DNA replication and chromosome segregation.","authors":"Murakami Y, Huberman JA, Hurwitz J","authors_abbrev":"Murakami Y et al.","pubmed_publication_date":"09 Jan 1996","pubmed_entrez_date":"1996-01-09","publication_year":"1996","canto_session_key":"f55fcc98c5e448a0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-28 14:02:01","canto_approved_date":"2020-01-23 13:38:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-01 11:22:57","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-28"},{"uniquename":"PMID:3116005","title":"Periodic cell cycle changes in the rate of CO2 production in the fission yeast Schizosaccharomyces pombe persist after a block to protein synthesis.","citation":"J Cell Sci 1987 Mar;87 ( Pt 2):323-5","abstract":"CO2 production has been followed by manometry in synchronous and asynchronous control cultures of Schizosaccharomyces pombe prepared by elutriation from the same initial culture. Earlier results showed a periodic change in the rate of production, which took place once per cell cycle. These changes were most clearly shown as oscillations in the difference between values of the second differential (acceleration) for the synchronous and asynchronous cultures. This paper shows that the oscillations continue for at least three cycles in the presence of cycloheximide (with and without chloramphenicol). Protein synthesis is virtually absent and there is no cell division. The control of this metabolic oscillation is therefore not directly dependent on translation. The period of the oscillation under these conditions is about 60% of the normal cycle time.","authors":"Novak B, Mitchison JM","authors_abbrev":"Novak B et al.","pubmed_publication_date":"Mar 1987","pubmed_entrez_date":"1987-03-01","publication_year":"1987","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34576871","title":"Subtelomeric Chromatin in the Fission Yeast  S. pombe .","citation":"Microorganisms 2021 Sep 17;9(9)","abstract":"Telomeres play important roles in safeguarding the genome. The specialized repressive chromatin that assembles at telomeres and subtelomeric domains is key to this protective role. However, in many organisms, the repetitive nature of telomeric and subtelomeric sequences has hindered research efforts. The fission yeast  S. pombe  has provided an important model system for dissection of chromatin biology due to the relative ease of genetic manipulation and strong conservation of important regulatory proteins with higher eukaryotes. Telomeres and the telomere-binding shelterin complex are highly conserved with mammals, as is the assembly of constitutive heterochromatin at subtelomeres. In this review, we seek to summarize recent work detailing the assembly of distinct chromatin structures within subtelomeric domains in fission yeast. These include the heterochromatic SH subtelomeric domains, the telomere-associated sequences (TAS), and ST chromatin domains that assemble highly condensed chromatin clusters called knobs. Specifically, we review new insights into the sequence of subtelomeric domains, the distinct types of chromatin that assemble on these sequences and how histone H3 K36 modifications influence these chromatin structures. We address the interplay between the subdomains of chromatin structure and how subtelomeric chromatin is influenced by both the telomere-bound shelterin complexes and by euchromatic chromatin regulators internal to the subtelomeric domain. Finally, we demonstrate that telomere clustering, which is mediated via the condensed ST chromatin knob domains, does not depend on knob assembly within these domains but on Set2, which mediates H3K36 methylation.","doi":"10.3390/microorganisms9091977","authors":"Yadav RK, Matsuda A, Lowe BR, Hiraoka Y, Partridge JF","authors_abbrev":"Yadav RK et al.","pubmed_publication_date":"17 Sep 2021","pubmed_entrez_date":"2021-09-28","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-09-30 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7217063","title":"Molecular properties and active form of nonspecific acid phosphatase from Schizosaccharomyces pombe.","citation":"J Biol Chem 1981 Apr 25;256(8):3926-30","abstract":"Equilibrium sedimentation experiments of the native acid phosphatase indicate a dimer-tetramer dissociating nonequilibrating system with a dimer Mr = 180,000 g/mol. The hydrolysis of nitrophenylphosphate was used to determine the sedimentation coefficient of the active species. The s20,w value for the species which degrades nitrophenylphosphate is 13.52 +/- 0.46 S in 1% sucrose and 13.72 +/- 0.11 S in 1.3 M sodium chloride, corresponding to the Svedberg value of the tetramer species. Several lines of evidence are presented which, together with previous data, indicate that the Schizosaccharomyces pombe nonspecific acid phosphatase is composed of 4 identical or nearly identical polypeptide chains: a, equilibrium sedimentation analysis of the enzyme in denaturing agents indicates the presence of homogeneous material having Mr = 90,800 g/mol; b, digestion with carboxypeptidase A releases 0.82 mol of tyrosine/monomer molecular weight. Concomitant phosphatase inactivation occurred during the splitting off of the tyrosyl terminal residue. Furthermore, a unique NH2-terminal residue (histidine) was determined.","authors":"Dibenedetto G, Teller DC","authors_abbrev":"Dibenedetto G et al.","pubmed_publication_date":"25 Apr 1981","pubmed_entrez_date":"1981-04-25","publication_year":"1981","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ632011","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.45"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU013722","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9117998","title":"Extracellular Mg2+ regulates intracellular Mg2+ and its subcellular compartmentation in fission yeast, Schizosaccharomyces pombe.","citation":"Cell Mol Life Sci 1997 Jan;53(1):69-72","abstract":"Effects of extracellular magnesium ions ([Mg2+]o) on intracellular free Mg2+ ([Mg2+]i) and its subcellular distribution in single fission yeast cells, Schizosaccharomyces pombe, were studied with digital-imaging microscopy and an Mg2+ fluorescent probe (mag-fura-2). Using 0.44 mM [Mg2+]o, [Mg2+]i in yeast cells was 0.91 +/- 0.08 mM. Elevation of [Mg2+]o to 1.97 mM induced rapid (within 5 min) increments in [Mg2+]i (2.18 +/- 0.11 mM). Lowering [Mg2+]o to 0.06 mM, however, exerted no significant effects on [Mg2+]i (0.93 +/- 0.14 mM), at least for periods of up to 30 min. Irrespective of the [Mg2+]o used, the subcellular distribution of [Mg2+]i remained heterogeneous, i.e. where the sub-plasma membrane region > cytoplasm > nucleus. [Mg2+] in all three subcellular compartments increased significantly, two- to threefold, concomitant with [Mg2+] when placed in 1.97 mM [Mg2+]o. We conclude that [Mg2+]i in fission yeast is maintained at a physiologic level when [Mg2+]o is low, but intracellular free Mg2+ rapidly rises when [Mg2+]o is elevated. Like most eukaryotic cells, yeast may have a Mg2+ transport system(s) which functions to maintain gradients of Mg2+ from the outside to inside the cell and among its subcellular compartments.","authors":"Zhang A, Cheng TP, Wu XY, Altura BT, Altura BM","authors_abbrev":"Zhang A et al.","pubmed_publication_date":"Jan 1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39527198","title":"Fast Fission Yeast Genome Editing by CRISPR/Cas9 Using Gap Repair and Fluoride Selection.","citation":"Methods Mol Biol 2025;2862:141-154","abstract":"We present a protocol to perform CRISPR/Cas9-mediated genome editing in the fission yeast Schizosaccharomyces pombe that does not require cloning and uses the fluoride exporter channel Fex1 as the selection marker. Transformation is typically carried out on the same day of PCR primer arrival and successfully edited strains are selected 5 days after transformation. We expect the adoption of this protocol to further accelerate the throughput of genome editing in S. pombe.","doi":"10.1007/978-1-0716-4168-2_10","authors":"Ren Y, Fernandez R, Saito T, Fujita B, Mousavi I, Berro J","authors_abbrev":"Ren Y et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10790689","title":"Cyclic AMP regulates cell size of Schizosaccharomyces pombe through Cdc25 mitotic inducer.","citation":"Yeast 2000 Apr;16(6):523-9","abstract":"Nutritional state modulates the cell size of the fission yeast Schizosaccharomyces pombe, such that cells grown in rich medium are larger in size than those in poor medium. This signal is transduced partly through the cyclic AMP-dependent protein kinase cascade. However, little is known about how cyclic AMP interacts with the central cell cycle machinery, Cdc2, the cyclin-dependent kinase that induces mitosis. We show here that cyclic AMP regulates mitosis and cell size, in part, through regulation of protein stability of the Cdc2-activating phosphatase, Cdc25. However, our analysis demonstrates that cyclic AMP can negatively regulate mitosis independently of dephosphorylation of Cdc2 at Tyr(15).","authors":"Kishimoto N, Yamashita I","authors_abbrev":"Kishimoto N et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-05-03","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22762302","title":"TORC1 of fission yeast is rapamycin-sensitive.","citation":"Genes Cells 2012 Aug;17(8):698-708","abstract":"The target of rapamycin (TOR) protein kinase plays central roles in the regulation of cell growth in response to nutritional availability. TOR forms two distinct multiprotein complexes termed TOR complex 1 (TORC1) and TORC2. Typically, only the activity of TORC1 is inhibited by the immunosuppressant rapamycin. Although rapamycin strongly inhibits cell growth of the budding yeast Saccharomyces cerevisiae through inhibition of TORC1, growth of the fission yeast Schizosaccharomyces pombe appears to be resistant to rapamycin. Here, we demonstrate that rapamycin inhibits the kinase activity of S. pombe TORC1 in vitro in a similar manner to TORC1 of other organisms. We furthermore show that incomplete inhibition of TORC1 by rapamycin underlies the apparent rapamycin resistance of S. pombe. In the presence of caffeine, which potentially lowers TORC1 activity, the growth of wild-type S. pombe cells is sensitive to rapamycin in a TORC1-dependent manner. Moreover, treatment of S. pombe cells with rapamycin plus caffeine induces starvation-specific gene expression and autophagy, similarly to cells with reduced TORC1 activity. These results indicate that rapamycin does inhibit TORC1 in S. pombe, but the inhibition is not sufficient to cause a growth defect. These findings establish a universal action of rapamycin on TORC1 inhibition.","doi":"10.1111/j.1365-2443.2012.01618.x","authors":"Takahara T, Maeda T","authors_abbrev":"Takahara T et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-07-06","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A7.11","SPBC216.07c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12167173","title":"Combinatorial diversity of fission yeast SCF ubiquitin ligases by homo- and heterooligomeric assemblies of the F-box proteins Pop1p and Pop2p.","citation":"BMC Biochem 2002 Aug 07;3:22","abstract":"SCF ubiquitin ligases share the core subunits cullin 1, SKP1, and HRT1/RBX1/ROC1, which associate with different F-box proteins. F-box proteins bind substrates following their phosphorylation upon stimulation of various signaling pathways. Ubiquitin-mediated destruction of the fission yeast cyclin-dependent kinase inhibitor Rum1p depends on two heterooligomerizing F-box proteins, Pop1p and Pop2p. Both proteins interact with the cullin Pcu1p when overexpressed, but it is unknown whether this reflects their co-assembly into bona fide SCF complexes.\nWe have identified Psh1p and Pip1p, the fission yeast homologues of human SKP1 and HRT1/RBX1/ROC1, and show that both associate with Pop1p, Pop2p, and Pcu1p into a ~500 kDa SCFPop1p-Pop2p complex, which supports polyubiquitylation of Rum1p. Only the F-box of Pop1p is required for SCFPop1p-Pop2p function, while Pop2p seems to be attracted into the complex through binding to Pop1p. Since all SCFPop1p-Pop2p subunits, except for Pop1p, which is exclusively nuclear, localize to both the nucleus and the cytoplasm, the F-box of Pop2p may be critical for the assembly of cytoplasmic SCFPop2p complexes. In support of this notion, we demonstrate individual SCFPop1p and SCFPop2p complexes bearing ubiquitin ligase activity.\nOur data suggest that distinct homo- and heterooligomeric assemblies of Pop1p and Pop2p generate combinatorial diversity of SCFPop function in fission yeast. Whereas a heterooligomeric SCFPop1p-Pop2p complex mediates polyubiquitylation of Rum1p, homooligomeric SCFPop1p and SCFPop2p complexes may target unknown nuclear and cytoplasmic substrates.","authors":"Seibert V, Prohl C, Schoultz I, Rhee E, Lopez R, Abderazzaq K, Zhou C, Wolf DA","authors_abbrev":"Seibert V et al.","pubmed_publication_date":"07 Aug 2002","pubmed_entrez_date":"2002-08-09","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4D7.03","SPBC11B10.09","SPAC23H4.18c","SPAC17G6.12","SPBC32F12.09","SPBC409.05","SPBC1718.01"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:11114532","title":"Microtubule dynamics: the view from the tip.","citation":"Curr Biol 2000 Nov 30;10(23):R860-2","abstract":"Recent studies have suggested that proteins found at the tips of microtubules in vertebrate cells may play an important role in intracellular membrane transport processes. Evidence from fission yeast indicates that such proteins can also regulate microtubule dynamics.","authors":"Sawin KE","authors_abbrev":"Sawin KE","pubmed_publication_date":"30 Nov 2000","pubmed_entrez_date":"2000-12-15","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9301023","title":"Advancement through mitosis requires rae1 gene function in fission yeast.","citation":"Yeast 1997 Sep 30;13(12):1167-79","abstract":"Growth of the rae1-1 mutant of Schizosaccharomyces pombe at restrictive temperature results in accumulation of poly(A)+ RNA in the nucleus and a cell cycle arrest at the G2/M boundary. We demonstrate here that rae1 function is required for a process other than mRNA export which is essential for advancement through mitosis. Cells lacking rae1 function arrest with elevated Cdc2p kinase levels at a step before the formation of a mitotic spindle and without separation of the spindle pole bodies. Rae1p was localized to the nuclear periphery, consistent with a role in nucleocytoplasmic trafficking, which could include protein import. We propose a model where rae1 functions in cell cycle progression through trafficking of proteins required for mitosis.","authors":"Whalen WA, Bharathi A, Danielewicz D, Dhar R","authors_abbrev":"Whalen WA et al.","pubmed_publication_date":"30 Sep 1997","pubmed_entrez_date":"1997-09-25","publication_year":"1997","canto_session_key":"493636e956e2fa13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-07 01:01:39","canto_approved_date":"2023-05-03 16:27:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-07 01:01:29","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC16A3.05c","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2018-06-07"},{"uniquename":"PMID:8594339","title":"Structural and functional similarities between the SbcCD proteins of Escherichia coli and the RAD50 and MRE11 (RAD32) recombination and repair proteins of yeast.","citation":"Mol Microbiol 1995 Sep;17(6):1215-7","abstract":"","authors":"Sharples GJ, Leach DR","authors_abbrev":"Sharples GJ et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_session_key":"79dea8c7b78b97e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 10:48:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-20 10:48:44","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13C5.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:7476866","title":"A selection system for diploid and against haploid cells in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1995 Oct 25;248(6):644-8","abstract":"We have isolated a mutant of Schizosaccharomyces pombe whose growth is temperature sensitive when it is haploid but not when it is diploid. This mutant may provide a useful system for selecting nonconditional mutants which are defective in diploid formation upon conjugation.","authors":"Tange Y, Niwa O","authors_abbrev":"Tange Y et al.","pubmed_publication_date":"25 Oct 1995","pubmed_entrez_date":"1995-10-25","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:830640","title":"Colcemid sensitivity of fission yeast: permeability and detoxification properties of resistant mutants.","citation":"J Bacteriol 1977 Jan;129(1):198-201","abstract":"Mutants of Schizosaccharomyces pombe, which were resistant to concentrations of colcemid inhibitory to the wild-type parent, were not diminished in their permeability to colcemid or colchicine. They also did not modify colcemid to a detectable derivative or to a product that was incapable of binding to brain tubulin. The resistance of these mutants was therefore via mechanisms different from those of permeability and detoxification known for animal cells.","authors":"Lederberg S, Gourse RL, Sackett DL","authors_abbrev":"Lederberg S et al.","pubmed_publication_date":"Jan 1977","pubmed_entrez_date":"1977-01-01","publication_year":"1977","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9551201","title":"[Exon-intron structure of the fet5+ gene of Schizosaccharomyces pombe and physical mapping of genome encompassing regions].","citation":"Bioorg Khim 1998 Jan;24(1):42-7","abstract":"Plasmid pYUK3 bearing the fet5+ gene of Schizosaccharomyces pombe was isolated from a genomic library of the fission yeast, and a detailed physical map of the whole genomic insert (ca. 9.6 Kbp) was constructed. The primary structure of the fet5+ gene and its flanking regions is established. The gene contains a single 45-bp intron in its distal part. A typical TATA-box (TATAAG) was found in the 5'-noncoding region ca. 50 bp upstream of the putative start of transcription, and the 3'-noncoding region contains AT-rich palindromes, which are probably involved in termination of the fet5+ transcription. A previously unidentified gene of Sz. pombe encoding a protein with some similarity to one of the transcriptional activators from the TBP (TATA-binding protein) group of SPT factors of transcription was found in the vicinity of the fet5+ gene. Taking into account that cDNA of the fet5(+)-gene was isolated as a suppressor of the genetic-defect of nuclear RNA polymerases I-III (Bioorg. Khim., 1997, vol. 23, No 3, pp. 234-237), this vicinity may be the first evidence of possible clustering, in the genome of the fission yeast, of genes participating in transcription regulation.","authors":"Shpakovskiĭ GV, Lebedenko EN","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Jan 1998","pubmed_entrez_date":"1998-04-29","publication_year":"1998","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15608241","title":"Inparanoid: a comprehensive database of eukaryotic orthologs.","citation":"Nucleic Acids Res 2005 Jan 01;33(Database issue):D476-80","abstract":"The Inparanoid eukaryotic ortholog database (http://inparanoid.cgb.ki.se/) is a collection of pairwise ortholog groups between 17 whole genomes; Anopheles gambiae, Caenorhabditis briggsae, Caenorhabditis elegans, Drosophila melanogaster, Danio rerio, Takifugu rubripes, Gallus gallus, Homo sapiens, Mus musculus, Pan troglodytes, Rattus norvegicus, Oryza sativa, Plasmodium falciparum, Arabidopsis thaliana, Escherichia coli, Saccharomyces cerevisiae and Schizosaccharomyces pombe. Complete proteomes for these genomes were derived from Ensembl and UniProt and compared pairwise using Blast, followed by a clustering step using the Inparanoid program. An Inparanoid cluster is seeded by a reciprocally best-matching ortholog pair, around which inparalogs (should they exist) are gathered independently, while outparalogs are excluded. The ortholog clusters can be searched on the website using Ensembl gene/protein or UniProt identifiers, annotation text or by Blast alignment against our protein datasets. The entire dataset can be downloaded, as can the Inparanoid program itself.","authors":"O'Brien KP, Remm M, Sonnhammer EL","authors_abbrev":"O'Brien KP et al.","pubmed_publication_date":"01 Jan 2005","pubmed_entrez_date":"2004-12-21","publication_year":"2005","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19542306","title":"{beta}-glucanase Eng2 is required for ascus wall endolysis after sporulation in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2009 Aug;8(8):1278-86","abstract":"Meiosis is the developmental program by which sexually reproducing diploid organisms generate haploid gametes. In yeast, meiosis is followed by spore morphogenesis. When Schizosaccharomyces pombe diploid cells undergo meiosis, they differentiate into asci containing four haploid ascospores that are highly resistant to environmental stress. The formation of the ascospore wall requires the activity of several enzymes involved in the biosynthesis and modification of its components, such as alpha- and beta-glucan synthases. Once the spores are completely mature, the wall of the ascus undergoes an endolytic process that results in the release of ascospores from the ascus, allowing their dispersal into the environment. This process requires the activity of the endo-alpha-1,3-glucanase Agn2. Here, we focus on the characterization of the endo-beta-1,3-glucanase Eng2, which is also required for ascospore release from the ascus. Although Eng2 is present during the mitotic cycle, the protein accumulates after meiosis II. The expression of eng2(+) is required for the efficient release of ascospores, as shown by placing eng2(+) under the control of a repressible promoter. Furthermore, a point mutation that destroys the catalytic activity of the protein results in a phenotype similar to that of the mutant strain. Finally, we demonstrate that exogenous addition of purified Eng2 releases the ascospores from asci generated by an eng2Delta mutant. We propose that Eng2 would act together with Agn2 to completely hydrolyze the ascus wall, thereby assisting in the release of ascospores in S. pombe.","doi":"10.1128/EC.00148-09","authors":"Encinar del Dedo J, Dueñas E, Arnáiz Y, del Rey F, Vázquez de Aldana CR","authors_abbrev":"Encinar del Dedo J et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-06-23","publication_year":"2009","canto_session_key":"56bbe992fbfce4f2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-11-30 16:22:53","canto_approved_date":"2024-10-08 12:48:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-30 16:22:48","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.06c","SPAC23D3.10c","SPAC821.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-11-30"},{"uniquename":"PMID:15612920","title":"Rpc25, a conserved RNA polymerase III subunit, is critical for transcription initiation.","citation":"Mol Microbiol 2005 Jan;55(1):104-14","abstract":"Rpc25 is a strongly conserved subunit of RNA polymerase III with homology to Rpa43 in RNA polymerase I, Rpb7 in RNA polymerase II and the archaeal RpoE subunit. A central domain of Rpc25 can replaced the corresponding region of Rpb7 with little or no growth defect, underscoring the functional relatedness of these proteins. Rpc25 forms a heterodimer with Rpc17, another conserved component of RNA polymerase III. A conditional mutant (rpc25-S100P) impairs this interaction. rpc25-S100P and another conditional mutant obtained by complementation with the Schizosaccharomyces pombe subunit (rpc25-Sp) were investigated for the properties of their purified RNA polymerase III. The mutant enzymes were defective in the specific synthesis of pre-tRNA transcripts but acted at a wild-type level on poly[d(A-T)] templates. They were also indistinguishable from wild type in transcript elongation, cleavage and termination. These data indicate that Rpc25 is needed for transcription initiation but is not critical for the elongating properties of RNA polymerase III.","authors":"Zaros C, Thuriaux P","authors_abbrev":"Zaros C et al.","pubmed_publication_date":"Jan 2005","pubmed_entrez_date":"2004-12-23","publication_year":"2005","canto_session_key":"64894c9f23d8198a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-06-08 08:52:40","canto_approved_date":"2023-03-14 17:58:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 11:41:38","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1E7.10","SPBC2G5.07c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2017-06-08"},{"uniquename":"PMID:1657594","title":"Interaction between ran1+ protein kinase and cAMP dependent protein kinase as negative regulators of fission yeast meiosis.","citation":"EMBO J 1991 Dec;10(12):3759-68","abstract":"In fission yeast, meiosis is initiated by transcriptional activation of the mei3+ gene under the combined influence of the four mating type genes. The mei3+ gene product acts as a meiotic inducer by binding to and inhibiting the ran1+ protein kinase. Inactivation of ran1+ kinase is both necessary and sufficient to allow meiotic differentiation. We describe a class of mutants which are unable to undergo both normal meiosis and meiosis induced by inactivation of ran1+. In addition to these defects, the cells are sterile and unable to enter stationary phase. We have determined that the mutants define two complementation groups, designated cgs1+ and cgs2+ (continues to grow in stationary). The wild type allele of each gene has been isolated and sequence analysis of cgs1+ shows that it encodes a protein homologous to the regulatory subunit of cyclic AMP dependent protein kinase (cAPK). Biochemical studies demonstrate that in cgs1-1 containing cells, cAPK activity is unregulated by cyclic AMP (cAMP). Sequence analysis of cgs2+ shows that the predicted protein it encodes shares homology with a phosphodiesterase from Dictyostelium discoideum and biochemical studies demonstrate that cells containing a mutant allele of cgs2+ have elevated levels of cAMP. Thus, both genes encode proteins that regulate the activity of cAPK. We have previously shown that cells overproducing ran1+ kinase are meiotically defective. Here, we provide direct evidence that the meiotic defect caused by either unregulated cAPK activity or unregulated ran1+ kinase activity is due to inability to induce transcription of the mei2+ gene, which is required for meiotic initiation. We propose that the switch from vegetative growth to meiosis in fission yeast requires inactivation of ran1+ kinase and is prevented by unregulated levels of cAPK.","authors":"DeVoti J, Seydoux G, Beach D, McLeod M","authors_abbrev":"DeVoti J et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"0c872033a21c238e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 21:59:53","canto_approved_date":"2022-06-06 07:02:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-08 15:08:38","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.03","SPBC19C2.05","SPBC106.10","SPBC119.04","SPCC285.09c","SPAC27D7.03c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2018-06-10"},{"uniquename":"PMID:32790622","title":"Atypical meiosis can be adaptive in outcrossed  Schizosaccharomyces pombe  due to  wtf  meiotic drivers.","citation":"Elife 2020 Aug 13;9","abstract":"Killer meiotic drivers are genetic parasites that destroy 'sibling' gametes lacking the driver allele. The fitness costs of drive can lead to selection of unlinked suppressors. This suppression could involve evolutionary tradeoffs that compromise gametogenesis and contribute to infertility.  Schizosaccharomyces pombe , an organism containing numerous gamete (spore)-killing  wtf  drivers, offers a tractable system to test this hypothesis. Here, we demonstrate that in scenarios analogous to outcrossing,  wtf  drivers generate a fitness landscape in which atypical spores, such as aneuploids and diploids, are advantageous. In this context,  wtf  drivers can decrease the fitness costs of mutations that disrupt meiotic fidelity and, in some circumstances, can even make such mutations beneficial. Moreover, we find that  S. pombe  isolates vary greatly in their ability to make haploid spores, with some isolates generating up to 46% aneuploid or diploid spores. This work empirically demonstrates the potential for meiotic drivers to shape the evolution of gametogenesis.","doi":"10.7554/eLife.57936","authors":"Bravo Núñez MA, Sabbarini IM, Eide LE, Unckless RL, Zanders SE","authors_abbrev":"Bravo Núñez MA et al.","pubmed_publication_date":"13 Aug 2020","pubmed_entrez_date":"2020-08-14","publication_year":"2020","canto_session_key":"99e9b5b486ebd287","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maria Angelica Bravo Nunez","canto_first_approved_date":"2020-09-22 15:31:34","canto_approved_date":"2025-09-03 11:17:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-16 01:42:48","canto_added_date":"2020-08-15 00:15:06","annotation_curators":[{"name":"Maria Angelica Bravo Nunez","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14","SPAC15E1.07c","SPCC162.04c","SPAC25G10.04c","SPBP35G2.03c","SPAC17A5.11"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2020-09-22"},{"uniquename":"PMID:39676666","title":"Abo1 ATPase facilitates the dissociation of FACT from chromatin.","citation":"Nucleic Acids Res 2024 Dec 16;","abstract":"The histone chaperone FAcilitates Chromatin Transcription (FACT) is a heterodimeric complex consisting of Spt16 and Pob3, crucial for preserving nucleosome integrity during transcription and DNA replication. Loss of FACT leads to cryptic transcription and heterochromatin defects. FACT was shown to interact with Abo1, an AAA + family histone chaperone involved in nucleosome dynamics. Depletion of Abo1 causes FACT to stall at transcription start sites and mimics FACT mutants, indicating a functional association between Abo1 and FACT. However, the precise role of Abo1 in FACT function remains poorly understood. Here, we reveal that Abo1 directly interacts with FACT and facilitates the dissociation of FACT from nucleosome. Specifically, the N-terminal region of Abo1 utilizes its FACT-interacting helix to bind to the N-terminal domain of Spt16. In addition, using single-molecule fluorescence imaging, we discovered that Abo1 facilitates the ATP-dependent dissociation of FACT from nucleosomes. Furthermore, we demonstrate that the interaction between Abo1 and FACT is essential for maintaining heterochromatin in fission yeast. In summary, our findings suggest that Abo1 regulates FACT turnover in an ATP-dependent manner, proposing a model of histone chaperone recycling driven by inter-chaperone interactions.","doi":"10.1093/nar/gkae1229","authors":"Jang J, Kang Y, Zofall M, Woo S, An S, Cho C, Grewal S, Lee JY, Song JJ","authors_abbrev":"Jang J et al.","pubmed_publication_date":"16 Dec 2024","pubmed_entrez_date":"2024-12-16","publication_year":"2024","canto_session_key":"44461dcced36c653","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-12-17 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31G5.19","SPBC609.05","SPBP8B7.19"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:29326669","title":"Yeast Monitoring of Wine Mixed or Sequential Fermentations Made by Native Strains from D.O. \"Vinos de Madrid\" Using Real-Time Quantitative PCR.","citation":"Front Microbiol 2017;8:2520","abstract":"There is an increasing trend toward understanding the impact of non- Saccharomyces  yeasts on the winemaking process. Although  Saccharomyces cerevisiae  is the predominant species at the end of fermentation, it has been recognized that the presence of non- Saccharomyces  species during alcoholic fermentation can produce an improvement in the quality and complexity of the final wines. A previous work was developed for selecting the best combinations between  S. cerevisiae  and five non- Saccharomyces  ( Torulaspora delbrueckii, Schizosaccharomyces pombe, Candida stellata, Metschnikowia pulcherrima , and  Lachancea thermotolorans ) native yeast strains from D.O. \"Vinos de Madrid\" at the laboratory scale. The best inoculation strategies between  S. cerevisiae  and non- Saccharomyces  strains were chosen to analyze, by real-time quantitative PCR (qPCR) combined with the use of specific primers, the dynamics of inoculated populations throughout the fermentation process at the pilot scale using the Malvar white grape variety. The efficiency of the qPCR system was verified independently of the samples matrix, founding the inoculated yeast species throughout alcoholic fermentation. Finally, we can validate the positive effect of selected co-cultures in the Malvar wine quality, highlighting the sequential cultures of  T. delbrueckii  CLI 918/ S. cerevisiae  CLI 889 and  C. stellata  CLI 920/ S. cerevisiae  CLI 889 and, mixed and sequential cultures of  L. thermotolerans  9-6C combined with  S. cerevisiae  CLI 889.","doi":"10.3389/fmicb.2017.02520","authors":"García M, Esteve-Zarzoso B, Crespo J, Cabellos JM, Arroyo T","authors_abbrev":"García M et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2018-01-13","publication_year":"2017","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2018-01-14 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16935874","title":"Roles of Pif1-like helicases in the maintenance of genomic stability.","citation":"Nucleic Acids Res 2006;34(15):4147-53","abstract":"The Pif1p family of DNA helicases is conserved from yeast to humans. To date, four members of this family have been analyzed in some detail by in vitro and in vivo assays: the two baker's yeast helicases, ScPif1p and Rrm3p, the fission yeast Pfh1p and the human enzyme hPif1p. In vitro, these enzymes are 5' to 3' DNA helicase and show little processivity. In vivo, ScPif1p, Rrm3p and probably Pfh1p, function in both the nucleus at specific genomic loci and in mitochondria, where they are needed for the stable maintenance of the genome as accessory helicases to the replication machinery. Interestingly, they act on common DNA substrates but appear to have largely non-overlapping cellular functions, ranging from Okazaki fragment processing, telomerase inhibition, to helping the replication fork progress through non-nucleosomal protein-DNA complexes. For example, both ScPif1p and Rrm3p affect the replication of telomeres, but in a different way: Pif1p inhibits telomerase-mediated telomere elongation by directly removing telomerase from a DNA end, whereas Rrm3p facilitates replication through telomeric DNA. Here we review the current knowledge on the Pif1-like helicases, as a first step towards understanding the basis of their functional specialization and mechanism of action.","authors":"Boulé JB, Zakian VA","authors_abbrev":"Boulé JB et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-08-29","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:478290","title":"Estimation of meiosis and sporulation efficiencies in the fission yeast by ascus analysis.","citation":"Genet Res 1979 Apr;33(2):109-19","abstract":"","authors":"Calleja GB, Zuker M, Johnson BF","authors_abbrev":"Calleja GB et al.","pubmed_publication_date":"Apr 1979","pubmed_entrez_date":"1979-04-01","publication_year":"1979","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19269359","title":"In DNA replication, the early bird catches the worm.","citation":"Cell 2009 Mar 06;136(5):812-4","abstract":"The initiation of DNA replication is a complex, multistep process with important implications for genomic stability. In this issue, Wu and Nurse (2009) find that initiation factors are differentially recruited to replication origins. They uncover evidence suggesting that the efficiency of this recruitment may determine whether and when an origin is used to initiate DNA replication in S phase.","doi":"10.1016/j.cell.2009.02.023","authors":"Boye E, Grallert B","authors_abbrev":"Boye E et al.","pubmed_publication_date":"06 Mar 2009","pubmed_entrez_date":"2009-03-10","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41556658","title":"p24 family proteins are critical for cell wall integrity, protein secretion, and virulence in  Candida albicans .","citation":"mSphere 2026 Feb 24;11(2):e0082725","abstract":" Candida albicans  is a fungal commensal and also a prevalent pathogen of humans. p24 proteins are a family of type I membrane proteins regarded as cargo receptors for endoplasmic reticulum (ER) to Golgi transport and are thought to be involved in regulating secretion. Here, we sought to explore the impact of this family of proteins on  C. albicans  pathogenicity. The expression of all four members of the p24 family is upregulated during invasive candidiasis. Their expression is independent of yeast-to-hypha transition but is highly induced by tissue culture conditions. We then generated single deletion mutants for each member of the p24 family for phenotypic characterization. All these mutants exhibit significantly attenuated virulence in a mouse model of systemic infection and reduced survival in macrophages but are dispensable for vegetative growth and morphogenesis. They also show lower abundance of chitin and phosphomannan in the cell wall and enhanced sensitivity to fluconazole, an azole antifungal drug. Importantly, the absence of p24 proteins leads to defective protein secretion in  C. albicans , including pathogenicity-related effectors and lipases, and reduces commensal fitness. These results suggest that p24 proteins are critical for cell wall integrity, secretion of virulence factors, and virulence in  C. albicans .IMPORTANCE Candida albicans  is an important opportunistic fungal pathogen of immunocompromised individuals and a top-ranking WHO fungal priority pathogen due to the high frequency and mortality of invasive candidiasis. The eukaryotic p24 family of proteins has long been known to be key regulators of protein trafficking along the secretory pathway, but their potential roles regarding pathogenesis in  C. albicans  remain unknown. Here, we discover that all members of the p24 family are required for cell wall integrity, proper secretion of virulence factors, survival in macrophages, and virulence in a systemic infection model. However, they are dispensable for vegetative growth and yeast-to-hypha transition, the best-known virulence attribute. Our study systematically investigates  C. albicans  p24 proteins and highlights the critical role that the early secretory pathway plays in fungal pathogenicity.","doi":"10.1128/msphere.00827-25","authors":"Yu X, Cui H, Liu Y, Yin J, Zhang J, Luo G, Lu Y, Su C","authors_abbrev":"Yu X et al.","pubmed_publication_date":"24 Feb 2026","pubmed_entrez_date":"2026-01-20","publication_year":"2026","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41990136","title":"Repurposing extracellular phosphatases to enhance thiamine biosynthesis and refine a genetic tool in Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 2026 Apr 16;","abstract":"Thiamine (Vitamin B1) and its active form, thiamine pyrophosphate (TPP), are essential cofactors in all living organisms. However, industrial thiamine production in prokaryotes has been hindered by tight feedback regulation, such as that imposed by TPP riboswitches. This study explores the fission yeast Schizosaccharomyces pombe-which naturally lacks TPP riboswitches-as an alternative production host. We identified the extracellular phosphatases Pho1 and Pho4 as key redundant enzymes that hydrolyze thiamine monophosphate (TMP) to support the growth of thiamine auxotrophic strains. Intracellular retention of Pho1 and Pho4, engineered by signal peptide deletion, enhanced intracellular thiamine synthesis, as evidenced by strengthened TPP-mediated repression of nmt1+ gene. This modification effectively reduced the leaky basal expression of heterologous genes driven by the thiamine-repressible nmt1 promoter without compromising its strong inducibility, resulting in an improved gene expression system for S. pombe. Our work provides novel insights into thiamine metabolism and an effective engineering strategy for optimizing eukaryotic expression systems.","doi":"10.1093/femsle/fnag044","authors":"Huang X, Bai H, Sun L, Meng G, Ma L, Hou H","authors_abbrev":"Huang X et al.","pubmed_publication_date":"16 Apr 2026","pubmed_entrez_date":"2026-04-16","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-04-16 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012172","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41526646","title":"Development of a global screening system for detecting protein-protein interactions by luminescence complementation in fission yeast.","citation":"Sci Rep 2026 Jan 12;","abstract":"Deciphering protein-protein interactions (PPIs) is crucial for a comprehensive understanding of biological processes, yet current methodologies often provide incomplete interactome maps. Here, we present a sensitive bimolecular NanoBiT-based protein complementation assay platform for robust PPI detection in the fission yeast Schizosaccharomyces pombe. Our platform utilizes two NanoLuc moieties, SmBiT and LgBiT, fused to interacting protein partners, generating a quantifiable luminescent signal upon interaction. To maximize the chances of detection and mitigate potential issues arising from tag position-dependent inactivation of bait proteins, our system enables simultaneous expression of two distinct bait constructs within a single cell: one with the LgBiT-tag fused at its N-terminus and another at its C-terminus. For the prey, we constructed a comprehensive ORFeome library of fission yeast proteins, each fused with SmBiT at its C-terminus, leveraging homologous recombination tools. We established efficient high-throughput methods for cloning and selection of single-copy integrants, enabling the rapid construction of the prey library and reliable identification of true yeast transformants. Validating the platform, high-throughput screening using the general transcription elongation factor Tfs1 successfully identified previously undetectable interactors. This versatile platform not only significantly expands the scope of interactome discovery but also offers a powerful tool for future protein-compound interaction studies.","doi":"10.1038/s41598-026-35430-8","authors":"Azadeh F, Hashimoto A, Nishimura S, Arioka M, Yoshida M, Matsuyama A","authors_abbrev":"Azadeh F et al.","pubmed_publication_date":"12 Jan 2026","pubmed_entrez_date":"2026-01-12","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-01-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1652.02","SPAC29B12.05c","SPAC17A2.08c","SPAC15A10.05c","SPCC338.05c","SPAC222.04c","SPAC25B8.11","SPAC2F3.17c","SPBC839.17c","SPAC27D7.04","SPBP23A10.11c","SPAC8E11.02c","SPAC105.03c","SPCC1795.04c","SPAC25A8.01c","SPAC1039.09","SPAC806.07","SPAC22F8.11","SPBC20F10.10","SPAC11E3.04c","SPBC1773.16c","SPAC20H4.03c","SPCC338.07c","SPAC11G7.02","SPAC1142.06","SPAC644.05c","SPBC2D10.20","SPAC869.11","SPAC3G6.02","SPAC5H10.09c","SPCC126.01c","SPCC576.02","SPAC652.01","SPAC227.17c","SPBC19C2.14","SPCC830.08c","SPBC215.14c","SPAC6F12.04","SPBC2G5.05","SPAC1F7.10","SPAC4G8.13c","SPBC418.02","SPAC1786.03","SPBC359.03c","SPAC1B9.02c","SPAC343.09"],"gene_count":46,"ltp_gene_count":46},{"uniquename":"PMID:16204182","title":"RNA Pol II subunit Rpb7 promotes centromeric transcription and RNAi-directed chromatin silencing.","citation":"Genes Dev 2005 Oct 01;19(19):2301-6","abstract":"Fission yeast centromeric repeats are transcribed into small interfering RNA (siRNA) precursors (pre-siRNAs), which are processed by Dicer to direct heterochromatin formation. Recently, Rpb1 and Rpb2 subunits of RNA polymerase II (RNA Pol II) were shown to mediate RNA interference (RNAi)-directed chromatin modification but did not affect pre-siRNA levels. Here we show that another Pol II subunit, Rpb7 has a specific role in pre-siRNA transcription. We define a centromeric pre-siRNA promoter from which initiation is exquisitely sensitive to the rpb7-G150D mutation. In contrast to other Pol II subunits, Rpb7 promotes pre-siRNA transcription required for RNAi-directed chromatin silencing.","authors":"Djupedal I, Portoso M, Spåhr H, Bonilla C, Gustafsson CM, Allshire RC, Ekwall K","authors_abbrev":"Djupedal I et al.","pubmed_publication_date":"01 Oct 2005","pubmed_entrez_date":"2005-10-06","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1B3.12c","SPBC14C8.12","SPACUNK4.06c","SPAC23G3.01","SPBC28F2.12","SPAC23C4.15","SPAC3A12.07","SPCC1442.10c","SPBC19C2.03","SPBC337.14"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"EMBL:SPD136","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15148393","title":"Cti1/C1D interacts with condensin SMC hinge and supports the DNA repair function of condensin.","citation":"Proc Natl Acad Sci U S A 2004 May 25;101(21):8078-83","abstract":"Condensin is a conserved five-subunit complex containing two SMC (structural maintenance of chromosomes) and three non-SMC subunits and plays a major role in mitotic chromosome condensation. Condensin also acts in interphase and is required for DNA repair and replication checkpoint control. We attempted to study the function of the condensin in greater detail by means of the isolation of interacting proteins with the two-hybrid system. Using the hinge domain of Cut3/SMC4 as bait, we found one Cut three-interacting (Cti) 14-kDa nuclear protein, Cti1. GST pull-down assay and immunoprecipitation supported physical interaction between Cti1 and condensin. Cti1 is similar to human C1D, which associates tightly with genomic DNA and functions to activate DNA protein kinase. SpC1D is essential for viability. The null mutant could germinate but arrest after replication, indicating that it is required for interphase growth. Importantly, an elevated dosage of spC1D suppressed the temperature, UV irradiation, and hydroxyurea sensitivity of the mutant of Cnd2, a non-SMC subunit of condensin. Upon exposure to hydroxyurea, spC1D accumulated on the nuclear chromatin, and the fraction of spC1D that was chromatin-bound increased. Cti1 is the first example of the protein that interacts with the hinge domain of SMC. Cti1 may have a supporting role for the DNA repair function of condensin.","authors":"Chen ES, Sutani T, Yanagida M","authors_abbrev":"Chen ES et al.","pubmed_publication_date":"25 May 2004","pubmed_entrez_date":"2004-05-19","publication_year":"2004","canto_session_key":"c270fbd238027d44","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-03-02 08:11:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-01 15:02:41","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC306.03c","HGNC:29911","SPCC1739.07","SPBC146.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-03-01"},{"uniquename":"PMID:26144970","title":"Three myosins contribute uniquely to the assembly and constriction of the fission yeast cytokinetic contractile ring.","citation":"Curr Biol 2015 Aug 03;25(15):1955-65","abstract":"Cytokinesis in fission yeast cells depends on conventional myosin-II (Myo2) to assemble and constrict a contractile ring of actin filaments. Less is known about the functions of an unconventional myosin-II (Myp2) and a myosin-V (Myo51) that are also present in the contractile ring. Myo2 appears in cytokinetic nodes around the equator 10 min before spindle pole body separation (cell-cycle time, -10 min) independent of actin filaments, followed by Myo51 at time zero and Myp2 at time +20 min, both located between nodes and dependent on actin filaments. We investigated the contributions of these three myosins to cytokinesis using a severely disabled mutation of the essential myosin-II heavy-chain gene (myo2-E1) and deletion mutations of the other myosin heavy-chain genes. Cells with only Myo2 assemble contractile rings normally. Cells with either Myp2 or Myo51 alone can assemble nodes and actin filaments into contractile rings but complete assembly later than normal. Both Myp2 and Myo2 contribute to constriction of fully assembled rings at rates 55% that of normal in cells relying on Myp2 alone and 25% that of normal in cells with Myo2 alone. Myo51 alone cannot constrict rings but increases the constriction rate by Myo2 in Δmyp2 cells or Myp2 in myo2-E1 cells. Three myosins function in a hierarchal, complementary manner to accomplish cytokinesis, with Myo2 and Myo51 taking the lead during contractile ring assembly and Myp2 making the greatest contribution to constriction.","doi":"10.1016/j.cub.2015.06.018","authors":"Laplante C, Berro J, Karatekin E, Hernandez-Leyva A, Lee R, Pollard TD","authors_abbrev":"Laplante C et al.","pubmed_publication_date":"03 Aug 2015","pubmed_entrez_date":"2015-07-07","publication_year":"2015","canto_session_key":"6ed88ec53b8a937a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-07-08 00:22:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1779794","title":"Sulfur-containing cadystin-cadmium complexes.","citation":"Methods Enzymol 1991;205:341-7","abstract":"","authors":"Mutoh N, Hayashi Y","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8143797","title":"Hotspots of homologous recombination.","citation":"Experientia 1994 Mar 15;50(3):234-41","abstract":"Homologous recombination occurs at higher than average frequency at and near hotspots. Hotspots are special nucleotide sequences recognized by proteins that promote, directly or indirectly, a rate limiting step of recombination. This review focuses on two well-studied examples, the Chi sites of the bacterium Escherichia coli and the M26 site of the fission yeast Schizosaccharomyces pombe. Chi, 5' G-C-T-G-G-T-G-G 3', is recognized by the RecBCD enzyme, which nicks the DNA near Chi and produces a 3'-ended single-stranded DNA 'tail'; this tail is a potent substrate for homologous pairing by RecA and single-stranded DNA binding proteins. M26, 5' A-T-G-A-C-G-T 3', is recognized by a heterodimeric protein and stimulates, by an as-yet-unknown mechanism, meiotic recombination at and near the ade6 gene. Additional hotspots in bacteria, fungi, and mammals enhance recombination directly or indirectly via a variety of mechanisms. Although hotspots are widespread among organisms, the biological role of their localized enhancement of recombination remains a matter of speculation.","authors":"Smith GR","authors_abbrev":"Smith GR","pubmed_publication_date":"15 Mar 1994","pubmed_entrez_date":"1994-03-15","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4903939","title":"[Production and features of protoplasts from Schizosaccharomyces pombe].","citation":"Z Allg Mikrobiol 1969;9(4):290-5","abstract":"","authors":"Rost K","authors_abbrev":"Rost K","pubmed_publication_date":"1969","pubmed_entrez_date":"1969-01-01","publication_year":"1969","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17189861","title":"Silence is golden: combining RNAi and live cell imaging to study cell cycle regulatory genes during Caenorhabditis elegans development.","citation":"Methods 2007 Feb;41(2):190-7","abstract":"Much of the pioneering work on the genetics of cell cycle regulation was accomplished using budding and fission yeast. The relative simplicity of these single-celled organisms allowed investigators to readily identify and assign roles to individual genes. While the molecular mechanisms worked out in yeast are more or less identical to those operating in higher organisms, additional layers of control must exist in multicellular organisms to coordinate the timing of developmental events occurring in different cells and tissues. Here we discuss experimental approaches for studying cell cycle processes in the nematode Caenorhabditis elegans.","authors":"Golden A, O'Connell KF","authors_abbrev":"Golden A et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2006-12-27","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9200612","title":"tea1 and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell.","citation":"Cell 1997 Jun 13;89(6):939-49","abstract":"Fission yeast cells identify and maintain growing regions exactly opposed at the ends of a cylindrical cell. tea1 mutants disrupt this organization, producing bent and T-shaped cells. We have cloned tea1 and shown that tea1 is located at the cell poles. Microtubules are continuously required to transfer tea1 to the cell ends, and tea1 is located at the ends of microtubules growing toward the cell poles. We suggest that tea1 acts as an end marker, directing the growth machinery to the cell poles. tea1 is down-regulated in cells treated with pheromone that grow toward a mating partner and no longer maintain their ends exactly opposed. tea1 may also influence microtubular organization, affecting the maintenance of a single central axis.","authors":"Mata J, Nurse P","authors_abbrev":"Mata J et al.","pubmed_publication_date":"13 Jun 1997","pubmed_entrez_date":"1997-06-13","publication_year":"1997","canto_session_key":"f6b6af4b58d157ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-04-30 13:19:03","canto_approved_date":"2024-04-03 16:45:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-30 13:18:36","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":24,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPAC27F1.02c","SPBC776.02c","SPBC26H8.07c","SPAC24H6.05","SPBC1604.14c","SPCC1223.06","SPAC4A8.15c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-04-30"},{"uniquename":"PMID:7816618","title":"Identification of two mismatch-binding activities in protein extracts of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1994 Dec 11;22(24):5289-95","abstract":"We have performed band-shift assays to identify mismatch-binding proteins in cell extracts of Schizosaccharomyces pombe. By testing heteroduplex DNA containing either a T/G or a C/C mismatch, two distinct band shifts were produced in the gels. A low mobility complex was observed with the T/G substrate, while a high mobility complex was present with C/C. Further analysis of the mismatch-binding specificities revealed that the T/G binding activity also binds to T/C, C/T, T/T, T/-, A/-, C/-, G/-, G/G, A/A, A/C, A/G, G/T, G/A, and C/A substrates with varying efficiencies, but not binds to C/C. The C/C binding activity efficiently binds to C/C, T/C, C/T, C/A, A/C, C/-, and weakly also to T/T, while all other mispairs are not recognized. Protein extracts of a mutant strain, defective in the mutS homologue swi4, displayed both mismatch-binding activities. Thus, swi4 does not encode for either one of the mismatch-binding proteins.","authors":"Fleck O, Schär P, Kohli J","authors_abbrev":"Fleck O et al.","pubmed_publication_date":"11 Dec 1994","pubmed_entrez_date":"1994-12-11","publication_year":"1994","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27022830","title":"Microscopy of Fission Yeast Sexual Lifecycle.","citation":"J Vis Exp 2016 Mar 09;(109)","abstract":"The fission yeast Schizosaccharomyces pombe has been an invaluable model system in studying the regulation of the mitotic cell cycle progression, the mechanics of cell division and cell polarity. Furthermore, classical experiments on its sexual reproduction have yielded results pivotal to current understanding of DNA recombination and meiosis. More recent analysis of fission yeast mating has raised interesting questions on extrinsic stimuli response mechanisms, polarized cell growth and cell-cell fusion. To study these topics in detail we have developed a simple protocol for microscopy of the entire sexual lifecycle. The method described here is easily adjusted to study specific mating stages. Briefly, after being grown to exponential phase in a nitrogen-rich medium, cell cultures are shifted to a nitrogen-deprived medium for periods of time suited to the stage of the sexual lifecycle that will be explored. Cells are then mounted on custom, easily built agarose pad chambers for imaging. This approach allows cells to be monitored from the onset of mating to the final formation of spores.","doi":"10.3791/53801","authors":"Vjestica A, Merlini L, Dudin O, Bendezu FO, Martin SG","authors_abbrev":"Vjestica A et al.","pubmed_publication_date":"09 Mar 2016","pubmed_entrez_date":"2016-03-30","publication_year":"2016","canto_session_key":"3c92e360a9269bd5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_approved_date":"2017-01-09 19:40:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-15 16:13:12","canto_added_date":"2016-03-31 00:15:22","annotation_curators":[{"name":"Sophie Martin","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1919.10c","SPAC1296.03c","SPAC22H10.07"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2016-11-15"},{"uniquename":"PMID:29222069","title":"Cooperativity between different tRNA modifications and their modification pathways.","citation":"Biochim Biophys Acta Gene Regul Mech 2018 Apr;1861(4):409-418","abstract":"Ribonucleotide modifications perform a wide variety of roles in synthesis, turnover and functionality of tRNA molecules. The presence of particular chemical moieties can refine the internal interaction network within a tRNA molecule, influence its thermodynamic stability, contribute novel chemical properties and affect its decoding behavior during mRNA translation. As the lack of specific modifications in the anticodon stem and loop causes disrupted proteome homeostasis, diminished response to stress conditions, and the onset of human diseases, the underlying modification cascades have recently gained particular scientific and clinical interest. Nowadays, a complicated but conclusive image of the interconnectivity between different enzymatic modification cascades and their resulting tRNA modifications emerges. Here we summarize the current knowledge in the field, focusing on the known instances of cross talk among the enzymatic tRNA modification pathways and the consequences on the dynamic regulation of the tRNA modificome by various factors. This article is part of a Special Issue entitled: SI: Regulation of tRNA synthesis and modification in physiological conditions and disease edited by Dr. Boguta Magdalena.","doi":"10.1016/j.bbagrm.2017.12.003","authors":"Sokołowski M, Klassen R, Bruch A, Schaffrath R, Glatt S","authors_abbrev":"Sokołowski M et al.","pubmed_publication_date":"Apr 2018","pubmed_entrez_date":"2017-12-10","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-08-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011806","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.1674"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"Pfam:PF02330","canto_curator_role":"PomBase","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC15D4.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28581482","title":"Parallel evolution of non-homologous isofunctional enzymes in methionine biosynthesis.","citation":"Nat Chem Biol 2017 Aug;13(8):858-866","abstract":"Experimental validation of enzyme function is crucial for genome interpretation, but it remains challenging because it cannot be scaled up to accommodate the constant accumulation of genome sequences. We tackled this issue for the MetA and MetX enzyme families, phylogenetically unrelated families of acyl-L-homoserine transferases involved in L-methionine biosynthesis. Members of these families are prone to incorrect annotation because MetX and MetA enzymes are assumed to always use acetyl-CoA and succinyl-CoA, respectively. We determined the enzymatic activities of 100 enzymes from diverse species, and interpreted the results by structural classification of active sites based on protein structure modeling. We predict that >60% of the 10,000 sequences from these families currently present in databases are incorrectly annotated, and suggest that acetyl-CoA was originally the sole substrate of these isofunctional enzymes, which evolved to use exclusively succinyl-CoA in the most recent bacteria. We also uncovered a divergent subgroup of MetX enzymes in fungi that participate only in L-cysteine biosynthesis as O-succinyl-L-serine transferases.","doi":"10.1038/nchembio.2397","authors":"Bastard K, Perret A, Mariage A, Bessonnet T, Pinet-Turpault A, Petit JL, Darii E, Bazire P, Vergne-Vaxelaire C, Brewee C, Debard A, Pellouin V, Besnard-Gonnet M, Artiguenave F, Médigue C, Vallenet D, Danchin A, Zaparucha A, Weissenbach J, Salanoubat M, de Berardinis V","authors_abbrev":"Bastard K et al.","pubmed_publication_date":"Aug 2017","pubmed_entrez_date":"2017-06-06","publication_year":"2017","canto_session_key":"ab984683b908067b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-09-25 17:17:34","canto_approved_date":"2026-02-12 11:52:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-09-06 06:51:00","canto_added_date":"2024-09-06 06:47:46","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.04","SPBC106.17c","SPBC428.11"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2024-09-25"},{"uniquename":"PMID:22540037","title":"Predicting the fission yeast protein interaction network.","citation":"G3 (Bethesda) 2012 Apr;2(4):453-67","abstract":"A systems-level understanding of biological processes and information flow requires the mapping of cellular component interactions, among which protein-protein interactions are particularly important. Fission yeast (Schizosaccharomyces pombe) is a valuable model organism for which no systematic protein-interaction data are available. We exploited gene and protein properties, global genome regulation datasets, and conservation of interactions between budding and fission yeast to predict fission yeast protein interactions in silico. We have extensively tested our method in three ways: first, by predicting with 70-80% accuracy a selected high-confidence test set; second, by recapitulating interactions between members of the well-characterized SAGA co-activator complex; and third, by verifying predicted interactions of the Cbf11 transcription factor using mass spectrometry of TAP-purified protein complexes. Given the importance of the pathway in cell physiology and human disease, we explore the predicted sub-networks centered on the Tor1/2 kinases. Moreover, we predict the histidine kinases Mak1/2/3 to be vital hubs in the fission yeast stress response network, and we suggest interactors of argonaute 1, the principal component of the siRNA-mediated gene silencing pathway, lost in budding yeast but preserved in S. pombe. Of the new high-quality interactions that were discovered after we started this work, 73% were found in our predictions. Even though any predicted interactome is imperfect, the protein network presented here can provide a valuable basis to explore biological processes and to guide wet-lab experiments in fission yeast and beyond. Our predicted protein interactions are freely available through PInt, an online resource on our website (www.bahlerlab.info/PInt).","doi":"10.1534/g3.111.001560","authors":"Pancaldi V, Saraç OS, Rallis C, McLean JR, Převorovský M, Gould K, Beyer A, Bähler J","authors_abbrev":"Pancaldi V et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2012-04-28","publication_year":"2012","canto_session_key":"6dcb87ba6a1fc262","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-23 18:39:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-23 18:39:11","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1783.05","SPAPB1A11.04c","SPBC106.06","SPAC1F7.11c","SPBC18E5.12c","SPAC222.12c","SPAC959.08","SPAC23E2.01","SPBC1773.10c","SPAC4G9.11c","SPAPB1E7.10","SPBC14F5.03c","SPBC1A4.03c","SPBC12C2.08","SPBC3B9.19","SPCC1223.09","SPAC17G8.06c","SPAC23G3.10c","SPBC26H8.07c","SPAC4D7.10c","SPBC1105.11c","SPAC2E1P3.04","SPAC6G10.02c","SPAC9.09","SPAC15A10.11","SPBC11G11.02c","SPBC16A3.15c","SPBC16D10.11c","SPBC17D11.07c","SPBC21C3.08c","SPCC16C4.14c","SPAC8C9.14","SPBC1105.12","SPCC16C4.09","SPAC6B12.05c","SPBC16H5.11c","SPBC1105.04c","SPAC17A2.13c","SPBC336.10c","SPCC285.08","SPAPB17E12.14c","SPAC3H8.08c","SPBC646.11","SPCC338.12","SPBC215.09c","SPBC16C6.02c","SPBC2A9.07c","SPBP23A10.15c","SPBC1703.02","SPAC23G3.09","SPCC5E4.03c","SPBC660.16","SPBP4H10.06c","SPAC922.07c","SPAC1327.01c","SPAC12G12.04","SPAC2F3.16","SPBC1718.03","SPAC25B8.11","SPBC29B5.01","SPAC2F3.04c","SPBC23G7.07c","SPCC285.16c","SPAC16E8.11c","SPCC736.08","SPAC17A5.13","SPBC1703.14c","SPAC15A10.02","SPAC22H12.02","SPAC139.01c","SPAC19A8.15","SPAC13D6.02c","SPAC26A3.16","SPBP4H10.11c","SPCC188.03","SPCC1919.14c","SPBC211.07c","SPAC29A4.15","SPAC139.03","SPAC8C9.08","SPAC13G7.13c","SPAC9E9.10c","SPAC1952.05","SPBC8D2.06","SPAC17H9.02","SPBC30D10.13c","SPAC1420.02c","SPBC36.05c","SPCC962.04","SPAC821.11","SPAC9E9.09c","SPAC17G8.03c","SPAC18G6.05c","SPBC19G7.01c","SPBC4F6.18c","SPBC887.01","SPBC17D1.06","SPBC646.13","SPCC553.11c","SPBC11G11.05","SPAC637.05c","SPAC2F3.09","SPBC21D10.11c","SPBC31F10.14c","SPBP16F5.03c","SPAC10F6.08c","SPAC1006.07","SPCC1795.04c","SPBC1198.02","SPBC1826.01c","SPAC343.11c","SPBC336.04","SPBC902.04","SPBP19A11.03c","SPCC1620.06c","SPCC330.03c","SPAC1F7.09c","SPCC1620.08","SPAC3G6.01","SPAC1006.03c","SPBC16H5.07c","SPBC12C2.06","SPCC16A11.14","SPAC6F6.10c","SPBC660.13c","SPAC17A5.06","SPBC23E6.02","SPCC306.03c","SPAC11E3.01c","SPAC9.05","SPCC1442.02","SPBC1734.16c","SPBC30D10.08","SPAC767.01c","SPBC27B12.11c","SPBC8D2.03c","SPBC1347.02","SPBC30D10.02","SPBC31F10.13c","SPBC887.14c","SPBC13E7.10c","SPBC947.08c","SPBC1198.04c","SPBP8B7.17c","SPAC21E11.03c","SPAC1399.05c","SPBC9B6.04c","SPBC543.03c","SPAC25G10.09c","SPAC1B3.12c","SPAC25G10.07c","SPBC1A4.08c","SPAC4G9.08c","SPAC16E8.01","SPAC12G12.05c","SPAC9G1.05","SPAC10F6.01c","SPBP23A10.13","SPBC1861.02","SPAC7D4.14c","SPBC337.08c","SPAC222.04c","SPAC1834.04","SPBC23E6.09","SPAC664.11","SPAC664.02c","SPAC31G5.19","SPBC28F2.09","SPBC409.06","SPCC576.03c","SPBC543.09","SPCC794.12c","SPAC31G5.03","SPAC26H5.12","SPAC4D7.08c","SPAC23G3.11","SPBC336.07","SPCC18.07","SPAC17H9.01","SPAC1783.07c","SPBC1289.04c","SPBC8D2.04","SPAC1565.08","SPAC14C4.14","SPCC1840.09","SPCC622.10c","SPBC25H2.11c","SPCC1259.04","SPBC800.05c","SPBC365.10","SPCC1682.10","SPAC11G7.04","SPAC110.04c","SPAC1B1.03c","SPAC23G3.01","SPAC1F7.05","SPCC1620.14c","SPCC1739.12","SPBC16C6.13c","SPAC17H9.14c","SPAC1556.02c","SPBP35G2.03c","SPAC1687.01","SPAC1250.01","SPAPB1E7.14","SPBC354.12","SPAC3G9.14","SPAC644.16","SPBC2G5.05","SPAC637.04","SPAC13G6.07c","SPBC651.08c","SPAC24C9.12c","SPAC23H3.09c","SPBC530.08","SPBC28F2.10c","SPAC23D3.09","SPAC26H5.05","SPAC3G9.06","SPBC4B4.03","SPAC13G7.12c","SPAC1486.10","SPBC14F5.12c","SPCC330.02","SPAC31G5.13","SPBC530.05","SPCC550.11","SPBC16D10.09","SPAC30.01c","SPCC736.15","SPAC1071.10c","SPBC30B4.04c","SPAC22G7.09c","SPAC1F3.06c","SPAC328.10c","SPBC1105.17","SPAC25B8.16","SPBC12C2.10c","SPAC1D4.04","SPBC146.14c","SPCC1672.02c","SPAC18B11.10","SPAC1834.03c","SPBC19C7.06","SPAC144.04c","SPAC23H3.10","SPBC146.03c","SPCC320.03","SPBC11B10.09","SPBC16G5.16","SPAC19G12.10c","SPAC630.14c","SPBC28F2.03","SPAC1F3.07c","SPAC589.10c","SPBC337.05c","SPBC28F2.12","SPCC126.02c","SPCC24B10.22","SPCC23B6.05c","SPBC609.05","SPAC17G6.10","SPAC821.07c","SPBC1734.15","SPBP23A10.05","SPCC290.02","SPAC6F12.11c","SPAC20G8.06","SPAC4H3.09","SPCC965.10","SPAC1751.01c","SPAC4F8.12c","SPCC1281.05","SPAC3A11.12c","SPAC13G7.02c","SPAC1071.06","SPBC713.03","SPBP8B7.30c","SPAC144.11","SPBC354.05c","SPAC29A4.02c","SPAC29E6.08","SPAPB24D3.01","SPAC144.02","SPBC660.11","SPBPJ4664.04","SPAC30D11.08c","SPAC26A3.15c","SPCC330.13","SPAC25A8.01c","SPBC56F2.09c","SPAC30D11.10","SPAC977.14c","SPBC1198.11c","SPBC29A10.10c","SPAC140.02","SPBC8D2.07c","SPCC965.05c","SPBC2G5.07c"],"gene_count":299,"ltp_gene_count":0,"approved_date":"2016-02-23"},{"uniquename":"PMID:28218250","title":"Chromatin remodeller Fun30 Fft3  induces nucleosome disassembly to facilitate RNA polymerase II elongation.","citation":"Nat Commun 2017 Feb 20;8:14527","abstract":"Previous studies have revealed that nucleosomes impede elongation of RNA polymerase II (RNAPII). Recent observations suggest a role for ATP-dependent chromatin remodellers in modulating this process, but direct in vivo evidence for this is unknown. Here using fission yeast, we identify Fun30 Fft3  as a chromatin remodeller, which localizes at transcribing regions to promote RNAPII transcription. Fun30 Fft3  associates with RNAPII and collaborates with the histone chaperone, FACT, which facilitates RNAPII elongation through chromatin, to induce nucleosome disassembly at transcribing regions during RNAPII transcription. Mutants, resulting in reduced nucleosome-barrier, such as deletion mutants of histones H3/H4 themselves and the genes encoding components of histone deacetylase Clr6 complex II suppress the defects in growth and RNAPII occupancy of cells lacking Fun30 Fft3 . These data suggest that RNAPII utilizes the chromatin remodeller, Fun30 Fft3 , to overcome the nucleosome barrier to transcription elongation.","doi":"10.1038/ncomms14527","authors":"Lee J, Choi ES, Seo HD, Kang K, Gilmore JM, Florens L, Washburn MP, Choe J, Workman JL, Lee D","authors_abbrev":"Lee J et al.","pubmed_publication_date":"20 Feb 2017","pubmed_entrez_date":"2017-02-21","publication_year":"2017","canto_session_key":"ec5bea036f16d96e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junwoo Lee","canto_first_approved_date":"2018-01-29 20:43:25","canto_approved_date":"2022-11-04 08:40:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-29 20:43:06","canto_added_date":"2017-02-23 01:15:14","annotation_curators":[{"name":"Junwoo Lee","community_curator":true,"annotation_count":1525,"orcid":"0000-0001-5821-2274","file_type":null,"file_name":null},{"name":"Midori 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of chronological aging in Schizosaccharomyces pombe by the protein kinases Pka1 and Sck2.","citation":"Aging Cell 2006 Aug;5(4):345-57","abstract":"Budding yeast shows a progressive decline in viability after entering stationary phase, a phenomenon known as chronological aging. We show here that the fission yeast Schizosaccharomyces pombe also undergoes chronological aging and that the process is regulated by genes controlling two related nutrient signalling pathways. The first pathway includes the serine/threonine cAMP-activated protein kinase Pka1 and the second pathway comprises the serine/threonine kinase Sck2, a homologue of Saccharomyces cerevisiae SCH9. A double mutant for pka1 and sck2 displayed an additive effect on prolonging the fission yeast lifespan, suggesting that these genes regulate related but independent pathways. These long-lived mutants also accumulated less reactive oxygen species and had a delayed initiation of apoptosis compared with wild-type cells. We also found that strains carrying pka1 deletion but not those with sck2 deletion gained resistance to oxidative stress due to exposure to H(2)O(2) or menadione. On the other hand, the additional increase in lifespan shown by the Deltapka1Deltasck2 double-mutant strain correlated with an increased resistance to both oxidative stress and heat shock. These results underscore the importance of nutrient signalling pathways and reactive oxygen species on organismal lifespan and establish S. pombe as a new model organism to study the molecular mechanisms underlying aging.","authors":"Roux AE, Quissac A, Chartrand P, Ferbeyre G, Rokeach LA","authors_abbrev":"Roux AE et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-07-11","publication_year":"2006","canto_session_key":"1900a00e16aa4080","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-23 10:56:09","canto_approved_date":"2019-12-11 16:35:29","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-11-20 14:41:41","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.14c","SPAC1B9.02c","SPBC106.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-11-23"},{"uniquename":"PMID:20400941","title":"Specific splicing defects in S. pombe carrying a degron allele of the Survival of Motor Neuron gene.","citation":"EMBO J 2010 Jun 02;29(11):1817-29","abstract":"Spinal muscular atrophy results from deletions or mutations in the survival of motor neuron (SMN1) gene. The SMN protein has an essential role in the biogenesis of spliceosomal snRNPs, but the link between a defect in this process and specific splicing inhibition of pre-mRNAs has not been established. In this study, we report the construction of a temperature-degron (td) allele of the Schizosaccharomyces pombe SMN protein and show that its depletion at 37 degrees C affects splicing and formation of U1, U2, U4 and U5 snRNPs, but not of U6 and U3 ribonucleoproteins. The function of the tdSMN allele in snRNP assembly is already perturbed at 25 degrees C, suggesting a deleterious effect of the tag at this temperature. Using a genome-wide approach, we report that introns react unequally to lower levels of snRNPs in tdSMN cells and that increasing the length of the polypyrimidine tract can improve the splicing efficiency of some, but not all, affected introns. Altogether, our results suggest that the defects observed in tdSMN fission yeast cells mimic splicing deficits observed in SMN-deficient metazoan cells.","doi":"10.1038/emboj.2010.70","authors":"Campion Y, Neel H, Gostan T, Soret J, Bordonné R","authors_abbrev":"Campion Y et al.","pubmed_publication_date":"02 Jun 2010","pubmed_entrez_date":"2010-04-20","publication_year":"2010","canto_session_key":"4da586afa92f17fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-12-22 13:14:44","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-19 08:50:49","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.08c","SPSNRNA.01","SPSNRNA.05","SPSNRNA.04","SPSNRNA.02","SPSNRNA.03","SPAC644.12","SPSNRNA.06"],"gene_count":8,"ltp_gene_count":1,"approved_date":"2014-08-19"},{"uniquename":"EMBL:AB084867","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6B12.18"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"GO_REF:0000054","title":"Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells.","abstract":"LIFEdb is a database that was created to manage the experimental data produced by the German Cancer Research Institute (DKFZ) and its collaborators, from work on cDNAs contained in the German cDNA Consortium collection. <br>A novel cloning technology was used to rapidly generate N- and C-terminal green fluorescent protein fusions of cDNAs to examine the intracellular localizations of expressed fusion proteins in living cells. GO Cellular Component terms are manually assigned by curators studying fluorescence microscope images of cells labelled with GFP-fused cDNAs. Protein coding regions of novel full length cDNAs are tagged with the coding sequence of the green fluorescent protein, the fusion proteins are then expressed and analyzed for their subcellular localization. <br>Prior to February 2013, all LIFEdb annotations were referenced by PMID: 11256614 (Simpson et al. 2000 EMBO Rep. 1:287-292), a paper describing the protein subcellular localization pilot study and methodology used by LIFEdb. However, it has been decided that these annotations are more correctly described by a GO reference. <br>Resource URL: http://www.dkfz.de/en/mga/Groups/LIFEdb-Database.html <br>Protein subcellular localization images can be viewed on the LIFEdb website, http://www.dkfz.de/gpcf/lifedb.php","authors":"LIFEdb","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27558664","title":"Global Fitness Profiling Identifies Arsenic and Cadmium Tolerance Mechanisms in Fission Yeast.","citation":"G3 (Bethesda) 2016 Oct 13;6(10):3317-3333","abstract":"Heavy metals and metalloids such as cadmium [Cd(II)] and arsenic [As(III)] are widespread environmental toxicants responsible for multiple adverse health effects in humans. However, the molecular mechanisms underlying metal-induced cytotoxicity and carcinogenesis, as well as the detoxification and tolerance pathways, are incompletely understood. Here, we use global fitness profiling by barcode sequencing to quantitatively survey the Schizosaccharomyces pombe haploid deletome for genes that confer tolerance of cadmium or arsenic. We identified 106 genes required for cadmium resistance and 110 genes required for arsenic resistance, with a highly significant overlap of 36 genes. A subset of these 36 genes account for almost all proteins required for incorporating sulfur into the cysteine-rich glutathione and phytochelatin peptides that chelate cadmium and arsenic. A requirement for Mms19 is explained by its role in directing iron-sulfur cluster assembly into sulfite reductase as opposed to promoting DNA repair, as DNA damage response genes were not enriched among those required for cadmium or arsenic tolerance. Ubiquinone, siroheme, and pyridoxal 5'-phosphate biosynthesis were also identified as critical for Cd/As tolerance. Arsenic-specific pathways included prefoldin-mediated assembly of unfolded proteins and protein targeting to the peroxisome, whereas cadmium-specific pathways included plasma membrane and vacuolar transporters, as well as Spt-Ada-Gcn5-acetyltransferase (SAGA) transcriptional coactivator that controls expression of key genes required for cadmium tolerance. Notable differences are apparent with corresponding screens in the budding yeast Saccharomyces cerevisiae, underscoring the utility of analyzing toxic metal defense mechanisms in both organisms.","doi":"10.1534/g3.116.033829","authors":"Guo L, Ganguly A, Sun L, Suo F, Du LL, Russell P","authors_abbrev":"Guo L et al.","pubmed_publication_date":"13 Oct 2016","pubmed_entrez_date":"2016-08-26","publication_year":"2016","canto_session_key":"987e13c5387ab8d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Abantika Ganguly","canto_first_approved_date":"2016-10-17 13:55:47","canto_approved_date":"2026-03-17 08:11:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-11 18:12:23","canto_added_date":"2016-08-27 00:15:21","annotation_curators":[{"name":"Abantika Ganguly","community_curator":true,"annotation_count":12,"orcid":"0000-0003-3037-7231","file_type":null,"file_name":null},{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Abantika Ganguly","file_curator_role":"community","annotation_file_curators":[{"name":"Abantika Ganguly","community_curator":true,"annotation_count":216,"orcid":"0000-0003-3037-7231","file_type":"PHAF","file_name":"PMID_27558664_phaf.tsv"}],"genes":["SPBC428.02c","SPBC1A4.04","SPCC24B10.08c","SPBC409.20c","SPBC16D10.07c","SPCC306.08c","SPAC1783.05","SPBC2G2.10c","SPBC1604.03c","SPAC6C3.04","SPAC11E3.11c","SPBC1861.05","SPBC106.17c","SPAC6B12.12","SPBC1D7.01","SPCC1682.01","SPAC4D7.06c","SPBC3B9.05","SPBC13E7.03c","SPAC24H6.03","SPBC3H7.03c","SPAC24B11.06c","SPAC222.08c","SPBPJ4664.01","SPBC337.15c","SPAC1250.05","SPAC222.12c","SPAC29E6.10c","SPAC3H1.10","SPAC17C9.14","SPAC22H10.07","SPBC2D10.18","SPAC25H1.05","SPBC215.02","SPAC1D4.03c","SPBC1D7.03","SPAC6F12.06","SPAC17H9.10c","SPAC227.05","SPBC28F2.10c","SPAC29A4.14c","SPAC824.02","SPCC1840.09","SPCC16A11.07","SPCC737.09c","SPAC17H9.11","SPAC11E3.05","SPCC737.06c","SPAC23D3.09","SPBC119.08","SPBC4F6.06","SPCC18.04","SPBC609.02","SPAC4D7.10c","SPAC1486.01","SPAC1071.11","SPAC1610.02c","SPBC725.07","SPBC16A3.03c","SPAC1F7.08","SPAC4A8.10","SPAC323.01c","SPBC24C6.08c","SPAC9.02c","SPCC63.02c","SPBC1778.05c","SPAC9G1.07","SPCC417.02","SPAC57A10.14","SPAC12B10.13","SPAC1952.05","SPAC3H8.07c","SPBC36.04","SPBP16F5.03c","SPAPJ696.01c","SPAC13A11.05","SPCC24B10.11c","SPAC10F6.13c","SPBC651.11c","SPAC1952.03","SPBC31F10.16","SPAC1783.07c","SPAC17H9.09c","SPCC31H12.05c","SPCC1442.04c","SPAC823.05c","SPBC1921.07c","SPAC4G9.13c","SPBC660.10","SPAC15E1.06","SPBC27B12.10c","SPBC887.13c","SPAC23A1.07","SPBC14C8.17c","SPAC5H10.11","SPCC777.13","SPCC1739.06c","SPCC11E10.06c","SPAC227.17c","SPAC17C9.13c","SPBC691.04","SPBC2G5.02c","SPAC19G12.11","SPAC31A2.11c","SPAC29B12.04","SPCC11E10.04","SPBC1539.08","SPAC4G8.11c","SPBC1271.12","SPBC30B4.03c","SPAC2F7.10","SPAC10F6.06","SPAC3H5.11","SPCC338.14","SPBC1198.08","SPAC1782.11","SPBC1734.15","SPBC15C4.04c","SPAC1687.12c","SPCC1827.02c","SPAC631.01c","SPAC1556.03","SPBC13G1.08c","SPAC13G7.06","SPBC29A3.10c","SPBC36.06c","SPBC2G2.02","SPBC660.11","SPCC965.07c","SPAC823.10c","SPAC25G10.03","SPCC553.03","SPAPB1A11.04c","SPAC25H1.07","SPCC126.04c","SPAC6F12.03c","SPAC3A11.07","SPAC3A11.13","SPBC336.13c","SPAPB17E12.03","SPAC3F10.04","SPAC17A5.01","SPAC3A12.12","SPBC3B8.02","SPAC1071.12c","SPAC29B12.03","SPAC27D7.02c","SPCC162.05","SPBC365.16","SPBC12D12.07c","SPAC1F8.06","SPBC23E6.08","SPBC215.05","SPCC594.06c","SPAC30D11.13","SPAPB21F2.02","SPBC27.08c","SPBC2G5.06c","SPAC22E12.04","SPAC227.10","SPAC24B11.09","SPAC14C4.14","SPAC6F6.01","SPAC30C2.02","SPAC23C4.09c","SPBC30B4.04c","SPBC365.11","SPBC106.07c","SPAPB1A11.01","SPBC31E1.02c","SPAC17H9.13c","SPAC3C7.10","SPCC188.07","SPCC1620.11","SPAC20G4.07c","SPAC17A5.10","SPBC1685.06","SPBC17A3.10","SPBP35G2.07","SPCC4G3.04c","SPAC144.06","SPBC12C2.02c","SPAC1071.02"],"gene_count":183,"ltp_gene_count":8,"approved_date":"2016-10-17"},{"uniquename":"PMID:19533117","title":"Fine-structured multi-scaling long-range correlations in completely sequenced genomes--features, origin, and classification.","citation":"Eur Biophys J 2009 Jul;38(6):757-79","abstract":"The sequential organization of genomes, i.e. the relations between distant base pairs and regions within sequences, and its connection to the three-dimensional organization of genomes is still a largely unresolved problem. Long-range power-law correlations were found using correlation analysis on almost the entire observable scale of 132 completely sequenced chromosomes of 0.5 x 10(6) to 3.0 x 10(7) bp from Archaea, Bacteria, Arabidopsis thaliana, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melanogaster, and Homo sapiens. The local correlation coefficients show a species-specific multi-scaling behaviour: close to random correlations on the scale of a few base pairs, a first maximum from 40 to 3,400 bp (for Arabidopsis thaliana and Drosophila melanogaster divided in two submaxima), and often a region of one or more second maxima from 10(5) to 3 x 10(5) bp. Within this multi-scaling behaviour, an additional fine-structure is present and attributable to codon usage in all except the human sequences, where it is related to nucleosomal binding. Computer-generated random sequences assuming a block organization of genomes, the codon usage, and nucleosomal binding explain these results. Mutation by sequence reshuffling destroyed all correlations. Thus, the stability of correlations seems to be evolutionarily tightly controlled and connected to the spatial genome organization, especially on large scales. In summary, genomes show a complex sequential organization related closely to their three-dimensional organization.","doi":"10.1007/s00249-009-0489-y","authors":"Knoch TA, Göker M, Lohner R, Abuseiris A, Grosveld FG","authors_abbrev":"Knoch TA et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-06-18","publication_year":"2009","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17039252","title":"DNA damage induces Cdt1 proteolysis in fission yeast through a pathway dependent on Cdt2 and Ddb1.","citation":"EMBO Rep 2006 Nov;7(11):1134-9","abstract":"Cdt1 is an essential protein required for licensing of replication origins. Here, we show that in Schizosaccharomyces pombe, Cdt1 is proteolysed in M and G1 phases in response to DNA damage and that this mechanism seems to be conserved from yeast to Metazoa. This degradation does not require Rad3 and Cds1, indicating that it is independent of classic DNA damage and replication checkpoint pathways. Damage-induced degradation of Cdt1 is dependent on Cdt2 and Ddb1, which are components of a Cul4 ubiquitin ligase. We also show that Cdt2 and Ddb1 are needed for cell-cycle changes in Cdt1 levels in the absence of DNA damage. Cdt2 and Ddb1 have been shown to be involved in the degradation of the Spd1 inhibitor of ribonucleotide reductase after DNA damage, and we speculate that Cdt1 downregulation might contribute to genome stability by reducing demand on dNTP pools during DNA repair.","authors":"Ralph E, Boye E, Kearsey SE","authors_abbrev":"Ralph E et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-10-14","publication_year":"2006","canto_session_key":"3a8dc608ff891ebb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-01-18 15:46:32","canto_approved_date":"2021-10-13 13:35:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-18 15:46:14","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.10c","SPAC17H9.19c","SPCC18B5.11c","SPBC216.05","SPBC428.18"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2016-01-18"},{"uniquename":"PMID:22235339","title":"The S. pombe histone H2A dioxygenase Ofd2 regulates gene expression during hypoxia.","citation":"PLoS One 2012;7(1):e29765","abstract":"Post-translational modification of histone proteins are known to play an important role in regulating chromatin structure. In an effort to find additional histone modifications we set out to screen enzymes of the 2-oxoglutarate and Fe(II)-dependent (2-OG-Fe(II)) dioxygenase family for activity towards histones. Here we show that the Schizosaccharomyces pombe 2-OG-Fe(II) dioxygenase domain containing protein-2 (Ofd2) is a histone H2A dioxygenase enzyme. Using a combination of peptide screening and alanine scanning substitution analysis, we identify an HxxLR motif in H2A as a substrate for Ofd2 activity. Transcriptional profiling indicates that Ofd2 regulates the repression of oxidative phosphorylation genes during hypoxic stress. We show that Ofd2 is recruited to the 5' end of oxidative phosphorylation genes specifically during hypoxia and that it uses its dioxygenase activity to regulate their transcription. Together, these data uncover a novel histone H2A modifying activity involved in the regulation of gene expression during hypoxia.","doi":"10.1371/journal.pone.0029765","authors":"Lando D, Balmer J, Laue ED, Kouzarides T","authors_abbrev":"Lando D et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-01-12","publication_year":"2012","canto_session_key":"7dda9fd3efb63699","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-10-20 02:25:00","canto_approved_date":"2022-06-01 15:42:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-29 15:43:17","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":54,"orcid":"0000-0003-4148-4606","file_type":"qualitative_gene_expression","file_name":"PMID_22235339_Lando_qualitative_expression.txt"}],"genes":["SPBC19C2.09","SPBC1711.14","SPAC1687.16c","SPCC1840.06","SPAC17H9.12c","SPCC4F11.04c","SPCC191.07","SPCC613.10","SPAC1F12.10c","SPBC11C11.06c","SPAC4F8.08","SPCC320.09","SPCC548.07c","SPAC977.17","SPBC1306.01c","SPAC222.11","SPBC713.12","SPBC1703.11","SPCC1235.14","SPBC25H2.09","SPAC630.08c","SPBPB2B2.06c","SPBC1711.15c","SPCC70.02c","SPBP4H10.08","SPCC1442.05c","SPBC887.15c","SPBP4H10.11c","SPAC30C2.02","SPBC29A3.10c","SPBC215.11c","SPAC19A8.04","SPAC19G12.06c","SPAC1782.07","SPBC106.02c","SPAP8A3.02c","SPCC191.04c","SPAC17A2.05","SPBPB10D8.01","SPAC589.08c","SPAC977.16c","SPBC215.05","SPBC13E7.04","SPBC17F3.01c","SPAC3A11.07","SPBC31F10.05","SPAC869.02c","SPBC4F6.09","SPAC16A10.01","SPAC18G6.01c","SPBPB2B2.01","SPCC737.02c","SPAC25B8.01","SPBC359.02","SPAC13A11.02c","SPCC162.10","SPCC330.06c","SPAC1002.16c","SPBC530.02","SPAC22A12.06c","SPAC6B12.16","SPCC622.08c"],"gene_count":62,"ltp_gene_count":1,"approved_date":"2015-10-20"},{"uniquename":"PMID:39110593","title":"VAP-mediated membrane-tethering mechanisms implicate ER-PM contact function in pH homeostasis.","citation":"Cell Rep 2024 Aug 05;43(8):114592","abstract":"Vesicle-associated membrane protein (VAMP)-associated proteins (VAPs) are highly conserved endoplasmic reticulum (ER)-resident proteins that establish ER contacts with multiple membrane compartments in many eukaryotes. However, VAP-mediated membrane-tethering mechanisms remain ambiguous. Here, focusing on fission yeast ER-plasma membrane (PM) contact formation, using systematic interactome analyses and quantitative microscopy, we predict a non-VAP-protein direct binding-based ER-PM coupling. We further reveal that VAP-anionic phospholipid interactions may underlie ER-PM association and define the pH-responsive nature of VAP-tethered membrane contacts. Such conserved interactions with anionic phospholipids are generally defective in amyotrophic lateral sclerosis-associated human VAPB mutant. Moreover, we identify a conserved FFAT-like motif locating at the autoinhibitory hotspot of the essential PM proton pump Pma1. This modulatory VAP-Pma1 interaction appears crucial for pH homeostasis. We thus propose an ingenious strategy for maintaining intracellular pH by coupling Pma1 modulation with pH-sensory ER-PM contacts via VAP-mediated interactions.","doi":"10.1016/j.celrep.2024.114592","authors":"Hoh KL, Mu B, See T, Ng AYE, Ng AQE, Zhang D","authors_abbrev":"Hoh KL et al.","pubmed_publication_date":"05 Aug 2024","pubmed_entrez_date":"2024-08-07","publication_year":"2024","canto_session_key":"6673f828e280c8b9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dan Zhang","canto_first_approved_date":"2024-11-13 11:07:00","canto_approved_date":"2026-04-22 15:37:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-01 05:40:15","canto_added_date":"2024-08-07 23:25:04","annotation_curators":[{"name":"Dan Zhang","community_curator":true,"annotation_count":57,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H8.02","SPCC23B6.04c","SPAPJ696.02","SPAC15A10.16","SPBC146.14c","SPCC736.15","SPAC19A8.04","SPAC3H8.10","SPCC1442.12","SPAC2F7.03c","SPBC4F6.06","SPAC6B12.12","SPCC1223.06","SPAC17C9.12","SPAC13A11.02c","SPBC16G5.05c","SPAC3G9.05","SPBC1604.14c","SPBC19F5.03","SPAC1834.11c","SPAC57A7.10c","SPAC1071.10c","SPCC584.05","SPBC146.13c"],"gene_count":24,"ltp_gene_count":24,"approved_date":"2024-11-13"},{"uniquename":"PMID:32093266","title":"Yeast Genome Maintenance by the Multifunctional PIF1 DNA Helicase Family.","citation":"Genes (Basel) 2020 Feb 20;11(2)","abstract":"The two PIF1 family helicases in  Saccharomyces cerevisiae,  Rrm3, and ScPif1, associate with thousands of sites throughout the genome where they perform overlapping and distinct roles in telomere length maintenance, replication through non-histone proteins and G4 structures, lagging strand replication, replication fork convergence, the repair of DNA double-strand break ends, and transposable element mobility. ScPif1 and its fission yeast homolog Pfh1 also localize to mitochondria where they protect mitochondrial genome integrity. In addition to yeast serving as a model system for the rapid functional evaluation of human Pif1 variants, yeast cells lacking Rrm3 have proven useful for elucidating the cellular response to replication fork pausing at endogenous sites. Here, we review the increasingly important cellular functions of the yeast PIF1 helicases in maintaining genome integrity, and highlight recent advances in our understanding of their roles in facilitating fork progression through replisome barriers, their functional interactions with DNA repair, and replication stress response pathways.","doi":"10.3390/genes11020224","authors":"Muellner J, Schmidt KH","authors_abbrev":"Muellner J et al.","pubmed_publication_date":"20 Feb 2020","pubmed_entrez_date":"2020-02-26","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-02-27 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC887.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9003326","title":"The Schizosaccharomyces pombe map1 gene encodes an SRF/MCM1-related protein required for P-cell specific gene expression.","citation":"Mol Gen Genet 1996 Dec 13;253(3):387-92","abstract":"Cells of Schizosaccharomyces pombe undergo mating and meiosis when starved for a nitrogen source. In this process a P and and M cell first mate to generate a diploid zygote, which subsequently enters meiosis and sporulates. The P mating type is controlled by the mat1-Pc gene at the mating type locus, together with a gene called map1. We show that these two functions are required for expression of the P-specific gene map3. We have cloned the map1 gene and show that it encodes a putative MADS-box containing transcription factor related to mammalian Serum Response Factor (SRF) and Saccharomyces cerevisiae MCM1. The Mat1-Pc protein contains a motif characteristic for proteins that interact with MADS-box factors, suggesting that Mat-Pc and Map1 may form a heterodimer that activates the P-specific map3 gene.","authors":"Nielsen O, Friis T, Kjaerulff S","authors_abbrev":"Nielsen O et al.","pubmed_publication_date":"13 Dec 1996","pubmed_entrez_date":"1996-12-13","publication_year":"1996","canto_session_key":"621ee5f0491cf6af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-18 16:23:13","canto_approved_date":"2024-04-03 16:23:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-12-18 16:23:05","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11E3.06","SPAC3F10.10c","SPMTR.01"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2014-12-18"},{"uniquename":"PMID:5306879","title":"The growth-duplication cycle. VII. Further evidence for linear growth of a fission yeast. ANL-7535.","citation":"ANL Rep 1968 Dec;:7","abstract":"","authors":"Kubitschek HE, Clayman R","authors_abbrev":"Kubitschek HE et al.","pubmed_publication_date":"Dec 1968","pubmed_entrez_date":"1968-12-01","publication_year":"1968","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32612874","title":"Screening of the whole human cytochrome P450 complement (CYPome) with enzyme bag cocktails.","citation":"J Pharm Anal 2020 Jun;10(3):271-276","abstract":"We have previously introduced the use of permeabilized fission yeast cells (enzyme bags) that recombinantly express full-length CYPs for drug metabolism studies. Such enzyme bags are cells with pores that function as enzymes  in situ . They can easily be prepared without a need for ultracentrifugation and may be used in similar protocols as microsomes. In this study we report the preparation of enzyme bag cocktails that permit the testing of multiple CYPs in a single enzyme bag reaction. Moreover, we established a convenient testing scheme that permits a rapid screen of all human CYPs for activity towards any given candidate substrate. An important aspect of this approach is the reduction of individual CYP test assays. If a cocktail containing many CYPs tests negative, it follows that all CYPs included in that cocktail need not be tested individually, thus saving time and resources. The new protocol was validated using two probe substrates.","doi":"10.1016/j.jpha.2020.05.003","authors":"Sharma SS, Sharma S, Bureik M","authors_abbrev":"Sharma SS et al.","pubmed_publication_date":"Jun 2020","pubmed_entrez_date":"2020-07-03","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-07-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27575340","title":"Tying up the Ends: Plasticity in the Recognition of Single-Stranded DNA at Telomeres.","citation":"Biochemistry 2016 Sep 27;55(38):5326-40","abstract":"Telomeres terminate nearly exclusively in single-stranded DNA (ssDNA) overhangs comprised of the G-rich 3' end. This overhang varies widely in length from species to species, ranging from just a few bases to several hundred nucleotides. These overhangs are not merely a remnant of DNA replication but rather are the result of complex further processing. Proper management of the telomeric overhang is required both to deter the action of the DNA damage machinery and to present the ends properly to the replicative enzyme telomerase. This Current Topic addresses the biochemical and structural features used by the proteins that manage these variable telomeric overhangs. The Pot1 protein tightly binds the single-stranded overhang, preventing DNA damage sensors from binding. Pot1 also orchestrates the access of telomerase to that same substrate. The remarkable plasticity of the binding interface exhibited by the Schizosaccharomyces pombe Pot1 provides mechanistic insight into how these roles may be accomplished, and disease-associated mutations clustered around the DNA-binding interface in the hPOT1 highlight the importance of this function. The budding yeast Cdc13-Stn1-Ten1, a telomeric RPA complex closely associated with telomere function, also interacts with ssDNA in a fashion that allows degenerate sequences to be recognized. A related human complex composed of hCTC1, hSTN1, and hTEN1 has recently emerged with links to both telomere maintenance and general DNA replication and also exhibits mutations associated with telomere pathologies. Overall, these sequence-specific ssDNA binders exhibit a range of recognition properties that allow them to perform their unique biological functions.","doi":"10.1021/acs.biochem.6b00496","authors":"Lloyd NR, Dickey TH, Hom RA, Wuttke DS","authors_abbrev":"Lloyd NR et al.","pubmed_publication_date":"27 Sep 2016","pubmed_entrez_date":"2016-08-31","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-09-01 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15372378","title":"A mutation in the vesicle-trafficking protein VAPB causes late-onset spinal muscular atrophy and amyotrophic lateral sclerosis.","citation":"Am J Hum Genet 2004 Nov;75(5):822-31","abstract":"Motor neuron diseases (MNDs) are a group of neurodegenerative disorders with involvement of upper and/or lower motor neurons, such as amyotrophic lateral sclerosis (ALS), spinal muscular atrophy (SMA), progressive bulbar palsy, and primary lateral sclerosis. Recently, we have mapped a new locus for an atypical form of ALS/MND (atypical amyotrophic lateral sclerosis [ALS8]) at 20q13.3 in a large white Brazilian family. Here, we report the finding of a novel missense mutation in the vesicle-associated membrane protein/synaptobrevin-associated membrane protein B (VAPB) gene in patients from this family. Subsequently, the same mutation was identified in patients from six additional kindreds but with different clinical courses, such as ALS8, late-onset SMA, and typical severe ALS with rapid progression. Although it was not possible to link all these families, haplotype analysis suggests a founder effect. Members of the vesicle-associated proteins are intracellular membrane proteins that can associate with microtubules and that have been shown to have a function in membrane transport. These data suggest that clinically variable MNDs may be caused by a dysfunction in intracellular membrane trafficking.","authors":"Nishimura AL, Mitne-Neto M, Silva HC, Richieri-Costa A, Middleton S, Cascio D, Kok F, Oliveira JR, Gillingwater T, Webb J, Skehel P, Zatz M","authors_abbrev":"Nishimura AL et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-09-17","publication_year":"2004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16G5.05c","SPAC17C9.12"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:11210133","title":"Efflux system for pyridoxine in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2000 Dec;64(12):2675-9","abstract":"Pyridoxine-charged Schizosaccharomyces pombe released pyridoxine rapidly at 30 degrees C: very low amounts of three other B6 vitamers were also released. The rate of efflux was temperature-dependent. The initial rate of efflux was dependent on the concentration of pyridoxine in the cells: the rate was almost zero at lower than 0.02 mM and became saturated at higher than 0.2 mM. Na+, sodium azide, and dinitrophenol increased the rate in both the presence and absence of D-glucose. Mg++, thiamine, and menadione inhibited the efflux. The intracellular concentration of ATP did not significantly affect the efflux rate. The system may be dependent on a membrane potential of the yeast cells. It was found that the fission yeast cells have a gate or carrier system for efflux of pyridoxine, which was distinct from that in Saccharomyces cerevisiae.","authors":"Hirose K, Chumnantana R, Nakashima T, Ashiuchi M, Yagi T","authors_abbrev":"Hirose K et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2001-02-24","publication_year":"2000","canto_session_key":"e960dff00e13815f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-10-14 14:02:03","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-11 14:34:07","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-10-11"},{"uniquename":"PMID:39437723","title":"Actomyosin clusters as active units shaping living matter.","citation":"Curr Biol 2024 Oct 21;34(20):R1045-R1058","abstract":"Stress generation by the actin cytoskeleton shapes cells and tissues. Despite impressive progress in live imaging and quantitative physical descriptions of cytoskeletal network dynamics, the connection between processes at molecular scales and spatiotemporal patterns at the cellular scale is still unclear. Here, we review studies reporting actomyosin clusters of micrometre size and with lifetimes of several minutes in a large number of organisms, ranging from fission yeast to humans. Such structures have also been found in reconstituted systems in vitro and in theoretical analyses of cytoskeletal dynamics. We propose that tracking these clusters could provide a simple readout for characterising living matter. Spatiotemporal patterns of clusters could serve as determinants of morphogenetic processes that have similar roles in diverse organisms.","doi":"10.1016/j.cub.2024.08.043","authors":"Kruse K, Berthoz R, Barberi L, Reymann AC, Riveline D","authors_abbrev":"Kruse K et al.","pubmed_publication_date":"21 Oct 2024","pubmed_entrez_date":"2024-10-22","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-10-23 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31071203","title":"The concerted actions of Tip1/CLIP-170, Klp5/Kinesin-8, and Alp14/XMAP215 regulate microtubule catastrophe at the cell end.","citation":"J Mol Cell Biol 2019 Dec 23;11(11):956-966","abstract":"Spatial regulation of microtubule catastrophe is important for controlling microtubule length and consequently contributes to the proper establishment of cell polarity and cell growth. The +TIP proteins including Tip1/CLIP-170, Klp5/Kinesin-8, and Alp14/XMAP215 reside at microtubule plus ends to regulate microtubule dynamics. In the fission yeast Schizosaccharomyces pombe, Tip1 and Alp14 serve as microtubule-stabilizing factors, while Klp5 functions oppositely as a catastrophe-promoting factor. Despite that Tip1 has been shown to play a key role in restricting microtubule catastrophe to the cell end, how Tip1 fulfills the role remains to be determined. Employing live-cell microscopy, we showed that the absence of Tip1 impairs the localization of both Klp5 and Alp14 at microtubule plus ends, but the absence of Klp5 prolongs the residence time of Tip1 at microtubule plus ends. We further revealed that Klp5 accumulates behind Tip1 at microtubule plus ends in a Tip1-dependent manner. In addition, artificially tethering Klp5 to microtubule plus ends promotes premature microtubule catastrophe, while tethering Alp14 to microtubule plus ends in the cells lacking Tip1 rescues the phenotype of short microtubules. These findings establish that Tip1 restricts microtubule catastrophe to the cell end likely by spatially restricting the microtubule catastrophe activity of Klp5 and stabilizing Alp14 at microtubule plus ends. Thus, the work demonstrates the orchestration of Tip1, Alp14, and Klp5 in ensuring microtubule catastrophe at the cell end.","doi":"10.1093/jmcb/mjz039","authors":"Niu X, Zheng F, Fu C","authors_abbrev":"Niu X et al.","pubmed_publication_date":"23 Dec 2019","pubmed_entrez_date":"2019-05-10","publication_year":"2019","canto_session_key":"6abc88522f5d2473","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-05-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.12","SPCC895.07"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:21183410","title":"Schizosaccharomyces pombe Mms1 channels repair of perturbed replication into Rhp51 independent homologous recombination.","citation":"DNA Repair (Amst) 2011 Mar 07;10(3):283-95","abstract":"In both Schizosaccharomyces pombe and Saccharomyces cerevisiae, Mms22 and Mms1 form a complex with important functions in the response to DNA damage, loss of which leads to perturbations during replication. Furthermore, in S. cerevisiae, Mms1 has been suggested to function in concert with a Cullin-like protein, Rtt101/Cul8, a potential paralog of Cullin 4. We performed epistasis analysis between Δmms1 and mutants of pathways with known functions in genome integrity, and measured the recruitment of homologous recombination proteins to blocked replication forks and recombination frequencies. We show that, in S. pombe, the functions of Mms1 and the conserved components of the Cullin 4 ubiquitin ligase, Pcu4 and Ddb1, do not significantly overlap. Furthermore, unlike in S. cerevisiae, the function of the H3K56 acetylase Rtt109 is not essential for Mms1 function. We provide evidence that Mms1 function is particularly important when a single strand break is converted into a double strand break during replication. Genetic data connect Mms1 to a Mus81 and Rad22(Rad52) dependent, but Rhp51 independent, branch of homologous recombination. This is supported by results demonstrating that Mms1 is recruited to a site-specific replication fork barrier and that, in a Δmms1 strain, Rad22(Rad52) and RPA recruitment to blocked forks are reduced, whereas Rhp51 recruitment is unaffected. In addition, Mms1 appears to specifically promote chromosomal rearrangements in a recombination assay. These observations suggest that Mms1 acts to channel repair of perturbed replication into a particular sub-pathway of homologous recombination.","doi":"10.1016/j.dnarep.2010.11.013","authors":"Vejrup-Hansen R, Mizuno K, Miyabe I, Fleck O, Holmberg C, Murray JM, Carr AM, Nielsen O","authors_abbrev":"Vejrup-Hansen R et al.","pubmed_publication_date":"07 Mar 2011","pubmed_entrez_date":"2010-12-25","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.01","SPAC3A11.08","SPAC29B12.03","SPBC28F2.07","SPCC4G3.05c","SPAC20H4.07","SPBC3D6.10","SPAC11E3.04c","SPAC17H9.10c","SPBC3E7.08c","SPAC30D11.07","SPAC1783.04c","SPBC16D10.09","SPAPB24D3.04c","SPAC3G6.06c","SPAC30D11.10","SPAC644.14c","SPAC3H8.05c","SPBC216.06c"],"gene_count":19,"ltp_gene_count":19},{"uniquename":"PMID:10637604","title":"Cell-cycle regulatory proteins Hsl7p/Skb1p belong to the protein methyltransferase superfamily.","citation":"Trends Biochem Sci 2000 Jan;25(1):11-2","abstract":"","authors":"Ma XJ","authors_abbrev":"Ma XJ","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-01-19","publication_year":"2000","canto_session_key":"7fe269fad69a77bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-20 10:12:21","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-20 10:12:09","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16H5.11c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-20"},{"uniquename":"PMID:27165520","title":"Transcription of lncRNA prt, clustered prt RNA sites for Mmi1 binding, and RNA polymerase II CTD phospho-sites govern the repression of pho1 gene expression under phosphate-replete conditions in fission yeast.","citation":"RNA 2016 Jul;22(7):1011-25","abstract":"Expression of fission yeast Pho1 acid phosphatase is repressed during growth in phosphate-rich medium. Repression is mediated by transcription of the prt locus upstream of pho1 to produce a long noncoding (lnc) prt RNA. Repression is also governed by RNA polymerase II CTD phosphorylation status, whereby inability to place a Ser7-PO4 mark (as in S7A) derepresses Pho1 expression, and inability to place a Thr4-PO4 mark (as in T4A) hyper-represses Pho1 in phosphate replete cells. Here we find that basal pho1 expression from the prt-pho1 locus is inversely correlated with the activity of the prt promoter, which resides in a 110-nucleotide DNA segment preceding the prt transcription start site. CTD mutations S7A and T4A had no effect on the activity of the prt promoter or the pho1 promoter, suggesting that S7A and T4A affect post-initiation events in prt lncRNA synthesis that make it less and more repressive of pho1, respectively. prt lncRNA contains clusters of DSR (determinant of selective removal) sequences recognized by the YTH-domain-containing protein Mmi1. Altering the nucleobase sequence of two DSR clusters in the prt lncRNA caused hyper-repression of pho1 in phosphate replete cells, concomitant with increased levels of the prt transcript. The isolated Mmi1 YTH domain binds to RNAs with single or tandem DSR elements, to the latter in a noncooperative fashion. We report the 1.75 Å crystal structure of the Mmi1 YTH domain and provide evidence that Mmi1 recognizes DSR RNA via a binding mode distinct from that of structurally homologous YTH proteins that recognize m(6)A-modified RNA.","doi":"10.1261/rna.056515.116","authors":"Chatterjee D, Sanchez AM, Goldgur Y, Shuman S, Schwer B","authors_abbrev":"Chatterjee D et al.","pubmed_publication_date":"Jul 2016","pubmed_entrez_date":"2016-05-12","publication_year":"2016","canto_session_key":"3418ae66d9f08c88","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-05-13 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.12c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"5h8a","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A/B/C/D","position":"311-488"}],"title":"Mmi1 YTH domain","entry_authors":"Chatterjee D,Goldgur Y,Shuman S","entry_authors_abbrev":"Chatterjee D et al.","reference_uniquename":"PMID:27165520","experimental_method":"X-ray","resolution":"1.751"},{"pdb_id":"5hfz","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A/B/C/D","position":"319-488"}],"title":"Mmi1 YTH domain","entry_authors":"Chatterjee D,Goldgur Y,Shuman S","entry_authors_abbrev":"Chatterjee D et al.","reference_uniquename":"PMID:27165520","experimental_method":"X-ray","resolution":"1.96"}]},{"uniquename":"PMID:12753","title":"Mitochondrial adenosine triphosphatase of the fission yeast, Schizosaccharomyces pombe 972h-. Changes in activity and inhibitor-sensitivity in response to catabolite repression.","citation":"Biochem J 1976 Nov 15;160(2):335-42","abstract":"1. The specific activity of mitochondrial ATPase (adenosine triphosphatase) in extracts of Schizosaccharomyces pombe decreased 2.5-fold as the glucose concentration in the growth medium decreased from 50mM to 15mM. 2. During the late exponential phase of growth, ATPase activity doubled. 3. Sensitivity to oligomycin and Dio-9 as measured by values for I50(mug of inhibitor/mg of protein giving 50% inhibition) at pH 6.8 increased sixfold and ninefold respectively during the initial decrease in ATPase activity, and this degree of sensitivity was maintained for the remainder of the growth cycle. 4. Increased sensitivity to NN'-dicyclohexylcarbodi-imide, triethyltin and venturicidin was also observed during the early stage of glucose de-repression. 5. Smaller increases in sensitivity to efrapeptin, aurovertin, 7-chloro-4-nitrobenzo-2-oxa-1,3-diaz-le, quercetin and spegazzinine also occurred. 6. The ATPase of glycerol-grown cells was less sensitive to inhibitors than that of glucose-repressed cells; change in values for I50 were not so marked during the growth cycle of cells growing with glycerol. 7. When submitochondrial particles from glycerol-grown cells were tested by passage through Sephadex G-50, a fourfold increase in activity was accompanied by increased inhibitor resistance. 8. Gel filtration of submitochondrial particles from glucose-de-repressed cells gave similar results, whereas loss of ATPase occurred in submitochondrial particles from glucose-repressed cells. 9. It is proposed that alterations in sensitivity to inhibitors at different stages of glucose derepression may be partly controlled by a naturally occuring inhibitor of ATPase. 10. The inhibitors tested may be classififed into two groups on the basis of alterations of sensitivity of the ATPase during physiological modification: (a) oligomycin, Dio-9, NN'-dicyclohexylcarbodi-imide, venturicidin and triethyltin, and (b) efrapeptin, aurovertin, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, quercetin and spegazzinine.","authors":"Lloyd D, Edwards SW","authors_abbrev":"Lloyd D et al.","pubmed_publication_date":"15 Nov 1976","pubmed_entrez_date":"1976-11-15","publication_year":"1976","canto_session_key":"d062f134e07220a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2022-09-22 08:08:33","canto_approved_date":"2022-11-10 14:37:06","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-09-18 08:36:58","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2022-09-22"},{"uniquename":"PMID:19713940","title":"Fission yeast IQGAP arranges actin filaments into the cytokinetic contractile ring.","citation":"EMBO J 2009 Oct 21;28(20):3117-31","abstract":"The contractile ring (CR) consists of bundled actin filaments and myosin II; however, the actin-bundling factor remains elusive. We show that the fission yeast Schizosaccharomyces pombe IQGAP Rng2 is involved in the generation of CR F-actin and required for its arrangement into a ring. An N-terminal fragment of Rng2 is necessary for the function of Rng2 and is localized to CR F-actin. In vitro the fragment promotes actin polymerization and forms linear arrays of F-actin, which are resistant to the depolymerization induced by the actin-depolymerizing factor Adf1. Our findings indicate that Rng2 is involved in the generation of CR F-actin and simultaneously bundles the filaments and regulates its dynamics by counteracting the effects of Adf1, thus enabling the reconstruction of CR F-actin bundles, which provides an insight into the physical properties of the building blocks that comprise the CR.","doi":"10.1038/emboj.2009.252","authors":"Takaine M, Numata O, Nakano K","authors_abbrev":"Takaine M et al.","pubmed_publication_date":"21 Oct 2009","pubmed_entrez_date":"2009-08-29","publication_year":"2009","canto_session_key":"0b0990bc7e9460b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-12-20 15:32:53","canto_approved_date":"2025-09-04 11:47:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-20 15:32:44","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":70,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.03","SPAC24H6.05","SPAC20G4.06c","SPAC4F8.13c","SPBC1778.06c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-12-20"},{"uniquename":"PMID:10347220","title":"Characterization of human, Schizosaccharomyces pombe, and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes.","citation":"J Biol Chem 1999 Jun 04;274(23):16553-62","abstract":"Human and fission yeast cDNAs encoding mRNA (guanine-N7) methyltransferase were identified based on similarity of the human (Hcm1p; 476 amino acids) and Schizosaccharomyces pombe (Pcm1p; 389 amino acids) polypeptides to the cap methyltransferase of Saccharomyces cerevisiae (Abd1p). Expression of PCM1 or HCM1 in S. cerevisiae complemented the lethal phenotype resulting from deletion of the ABD1 gene, as did expression of the NH2-terminal deletion mutants PCM1(94-389) and HCM1(121-476). The CCM1 gene encoding Candida albicans cap methyltransferase (Ccm1p; 474 amino acids) was isolated from a C. albicans genomic library by selection for complementation of the conditional growth phenotype of S. cerevisiae abd1-ts mutants. Human cap methyltransferase was expressed in bacteria, purified, and characterized. Recombinant Hcm1p catalyzed quantitative S-adenosylmethionine-dependent conversion of GpppA-capped poly(A) to m7GpppA-capped poly(A). We identified by alanine-scanning mutagenesis eight amino acids (Asp-203, Gly-207, Asp-211, Asp-227, Arg-239, Tyr-289, Phe-291, and Phe-354) that are essential for human cap methyltransferase function in vivo. All eight residues are conserved in other cellular cap methyltransferases. Five of the mutant human proteins (D203A, R239A, Y289A, F291A, and F354A) were expressed in bacteria and found to be defective in cap methylation in vitro. Concordance of mutational effects on Hcm1p, Abd1p, and vaccinia capping enzyme underscores a conserved structural basis for cap methylation in DNA viruses, yeast, and metazoans. This is in contrast to the structural and mechanistic divergence of the RNA triphosphatase components of the yeast and metazoan capping systems. Nevertheless, we demonstrate that the entire three-component yeast capping apparatus, consisting of RNA 5'-triphosphatase (Cet1p), RNA guanylyltransferase (Ceg1p), and Abd1p could be replaced in vivo by the two-component mammalian apparatus consisting of a bifunctional triphosphatase-guanylyltransferase Mce1p and the methyltransferase Hcm1(121-476)p. Isogenic yeast strains with fungal versus mammalian capping systems should facilitate rational screens for antifungal drugs that target cap formation in vivo.","authors":"Saha N, Schwer B, Shuman S","authors_abbrev":"Saha N et al.","pubmed_publication_date":"04 Jun 1999","pubmed_entrez_date":"1999-05-29","publication_year":"1999","canto_session_key":"825a465bb2246064","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-08-04 12:57:07","canto_approved_date":"2023-12-10 10:05:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 12:16:53","canto_added_date":"2012-02-24 05:52:41","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC330.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:19474789","title":"A spatial gradient coordinates cell size and mitotic entry in fission yeast.","citation":"Nature 2009 Jun 11;459(7248):857-60","abstract":"Many eukaryotic cell types undergo size-dependent cell cycle transitions controlled by the ubiquitous cyclin-dependent kinase Cdk1 (refs 1-4). The proteins that control Cdk1 activity are well described but their links with mechanisms monitoring cell size remain elusive. In the fission yeast Schizosaccharomyces pombe, cells enter mitosis and divide at a defined and reproducible size owing to the regulated activity of Cdk1 (refs 2, 3). Here we show that the cell polarity protein kinase Pom1, which localizes to cell ends, regulates a signalling network that contributes to the control of mitotic entry. This network is located at cortical nodes in the middle of interphase cells, and these nodes contain the Cdk1 inhibitor Wee1, the Wee1-inhibitory kinases Cdr1 (also known as Nim1) and Cdr2, and the anillin-like protein Mid1. Cdr2 establishes the hierarchical localization of other proteins in the nodes, and receives negative regulatory signals from Pom1. Pom1 forms a polar gradient extending from the cell ends towards the cell middle and acts as a dose-dependent inhibitor of mitotic entry, working through the Cdr2 pathway. As cells elongate, Pom1 levels decrease at the cell middle, leading to mitotic entry. We propose that the Pom1 polar gradient and the medial cortical nodes generate information about cell size and coordinate this with mitotic entry by regulating Cdk1 through Pom1, Cdr2, Cdr1 and Wee1.","doi":"10.1038/nature08074","authors":"Moseley JB, Mayeux A, Paoletti A, Nurse P","authors_abbrev":"Moseley JB et al.","pubmed_publication_date":"11 Jun 2009","pubmed_entrez_date":"2009-05-29","publication_year":"2009","canto_session_key":"c599c5b1b32b1bc9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-10-04 15:24:41","canto_approved_date":"2026-06-08 07:42:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-26 17:01:20","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":54,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.06c","SPAC821.12","SPAC24H6.05","SPBC11B10.09","SPAC2F7.03c","SPAC57A10.02","SPBC1A4.05","SPBC1604.14c","SPCC4B3.15","SPCC1223.06","SPCC18B5.03","SPAC144.14","SPCC895.05","SPBC1706.01","SPBC530.04"],"gene_count":15,"ltp_gene_count":14,"approved_date":"2018-10-04"},{"uniquename":"PMID:25815904","title":"Contribution of dihydrouridine in folding of the D-arm in tRNA.","citation":"Org Biomol Chem 2015 May 07;13(17):4960-6","abstract":"Posttranscriptional modifications of transfer RNAs (tRNAs) are proven to be critical for all core aspects of tRNA function. While the majority of tRNA modifications were discovered in the 1970s, their contribution in tRNA folding, stability, and decoding often remains elusive. In this work an NMR study was performed to obtain more insight in the role of the dihydrouridine (D) modification in the D-arm of tRNAi(Met) from S. pombe. While the unmodified oligonucleotide adopted several undefined conformations that interconvert in solution, the presence of a D nucleoside triggered folding into a hairpin with a stable stem and flexible loop region. Apparently the D modification is required in the studied sequence to fold into a stable hairpin. Therefore we conclude that D contributes to the correct folding and stability of D-arm in tRNA. In contrast to what is generally assumed for nucleic acids, the sharp 'imino' signal for the D nucleobase at 10 ppm in 90% H2O is not indicative for the presence of a stable hydrogen bond. The strong increase in pKa upon loss of the aromatic character in the modified nucleobase slows down the exchange of its 'imino' proton significantly, allowing its observation even in an isolated D nucleoside in 90% H2O in acidic to neutral conditions.","doi":"10.1039/c5ob00164a","authors":"Dyubankova N, Sochacka E, Kraszewska K, Nawrot B, Herdewijn P, Lescrinier E","authors_abbrev":"Dyubankova N et al.","pubmed_publication_date":"07 May 2015","pubmed_entrez_date":"2015-03-28","publication_year":"2015","canto_session_key":"4ccdf40f0ac17b71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-03-01 20:19:45","canto_approved_date":"2023-03-01 20:21:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-01 20:19:07","canto_added_date":"2015-04-01 00:18:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPATRNAMET.01"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2023-03-01"},{"uniquename":"PMID:25520186","title":"ATPase-dependent auto-phosphorylation of the open condensin hinge diminishes DNA binding.","citation":"Open Biol 2014 Dec;4(12)","abstract":"Condensin, which contains two structural maintenance of chromosome (SMC) subunits and three regulatory non-SMC subunits, is essential for many chromosomal functions, including mitotic chromosome condensation and segregation. The ATPase domain of the SMC subunit comprises two termini connected by a long helical domain that is interrupted by a central hinge. The role of the ATPase domain has remained elusive. Here we report that the condensin SMC subunit of the fission yeast Schizosaccharomyces pombe is phosphorylated in a manner that requires the presence of the intact SMC ATPase Walker motif. Principal phosphorylation sites reside in the conserved, glycine-rich stretch at the hinge interface surrounded by the highly basic DNA-binding patch. Phosphorylation reduces affinity for DNA. Consistently, phosphomimetic mutants produce severe mitotic phenotypes. Structural evidence suggests that prior opening (though slight) of the hinge is necessary for phosphorylation, which is implicated in condensin's dissociation from and its progression along DNA.","doi":"10.1098/rsob.140193","authors":"Akai Y, Kanai R, Nakazawa N, Ebe M, Toyoshima C, Yanagida M","authors_abbrev":"Akai Y et al.","pubmed_publication_date":"Dec 2014","pubmed_entrez_date":"2014-12-19","publication_year":"2014","canto_session_key":"77f717dc87015fe5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Norihiko Nakazawa","canto_first_approved_date":"2016-07-02 17:45:21","canto_approved_date":"2024-12-03 08:16:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-27 09:21:30","canto_added_date":"2014-12-20 01:16:01","annotation_curators":[{"name":"Norihiko Nakazawa","community_curator":true,"annotation_count":13,"orcid":"0000-0001-8386-0812","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.03","SPCC306.03c","SPBC146.03c","SPBP4H10.06c","SPBC776.13"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-07-02"},{"uniquename":"PMID:12023299","title":"Cdc2-cyclin B kinase activity links Crb2 and Rqh1-topoisomerase III.","citation":"Genes Dev 2002 May 15;16(10):1195-208","abstract":"The availability of a sister chromatid, and thus the cell cycle phase in which DNA double-strand breaks (DSBs) occur, influences the choice between homologous recombination (HR) or nonhomologous end joining (NHEJ). The sequential activation and destruction of CDK-cyclin activities controls progression through the cell cycle. Here we provide evidence that the major Schizosaccharomyces pombe CDK, Cdc2-cyclin B, influences recombinational repair of radiation-induced DSBs during the G(2) phase at two distinct stages. At an early stage in HR, a defect in Cdc2 kinase activity, which is caused by a single amino acid change in cyclin B, affects the formation of Rhp51 (Rad51(sp)) foci in response to ionizing radiation in a process that is redundant with the function of Rad50. At a late stage in HR, low Cdc2-cyclin B activity prevents the proper regulation of topoisomerase III (Top3) function, disrupting a recombination step that occurs after the assembly of Rhp51 foci. This effect of Cdc2-cyclin B kinase on Top3 function is mediated by the BRCT-domain-containing checkpoint protein Crb2, thus linking checkpoint proteins directly with recombinational repair in G(2). Our data suggest a model in which CDK activity links processing of recombination intermediates to cell cycle progression via checkpoint proteins.","authors":"Caspari T, Murray JM, Carr AM","authors_abbrev":"Caspari T et al.","pubmed_publication_date":"15 May 2002","pubmed_entrez_date":"2002-05-23","publication_year":"2002","canto_session_key":"bb53d6c6ffb1be29","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-05-05 13:44:25","canto_approved_date":"2025-12-23 12:48:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-04 15:19:52","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":53,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC342.05","SPBC16G5.12c","SPBC11B10.09","SPAC2G11.12","SPBC3E7.08c","SPAC644.14c","SPAC3C7.03c","SPAC1556.01c","SPBC582.03"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-05-05"},{"uniquename":"PMID:16453725","title":"The cdc22 gene of Schizosaccharomyces pombe encodes a cell cycle-regulated transcript.","citation":"EMBO J 1986 Nov;5(11):2981-5","abstract":"Two independent DNA sequences, of 5.6 and 2.4 kb in size, were isolated from Schizosaccharomyces pombe gene libraries on the basis of their ability to rescue the temperature-conditional lethality conferred by a cdc22 mutation. Integration of these sequences into the S.pombe genome by homologous recombination, followed by genetic mapping, demonstrated that the site of integration of the 5.6 kb fragment is tightly linked to the cdc22 locus, while that of the 2.4 kb fragment is unlinked. This shows that the 5.6 kb fragment carries the authentic cdc22 gene while the 2.4 kb fragment carries and extragenic suppressor sequence. The cdc22 transcript was identified by Northern blot analysis and shown to be 3.3 kb in size. The level of the transcript during the cell cycle was investigated in synchronous cultures prepared by elutriation. The cdc22 transcript is cell cycle regulated, reaching a maximum level during late G1/S phase, at least 12-fold higher than the minimum level observed in mid G2.","authors":"Gordon CB, Fantes PA","authors_abbrev":"Gordon CB et al.","pubmed_publication_date":"Nov 1986","pubmed_entrez_date":"1986-11-01","publication_year":"1986","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24909749","title":"Endoplasmic reticulum stress response in yeast and humans.","citation":"Biosci Rep 2014 Jul 01;34(4)","abstract":"Stress pathways monitor intracellular systems and deploy a range of regulatory mechanisms in response to stress. One of the best-characterized pathways, the UPR (unfolded protein response), is an intracellular signal transduction pathway that monitors ER (endoplasmic reticulum) homoeostasis. Its activation is required to alleviate the effects of ER stress and is highly conserved from yeast to human. Although metazoans have three UPR outputs, yeast cells rely exclusively on the Ire1 (inositol-requiring enzyme-1) pathway, which is conserved in all Eukaryotes. In general, the UPR program activates hundreds of genes to alleviate ER stress but it can lead to apoptosis if the system fails to restore homoeostasis. In this review, we summarize the major advances in understanding the response to ER stress in Sc (Saccharomyces cerevisiae), Sp (Schizosaccharomyces pombe) and humans. The contribution of solved protein structures to a better understanding of the UPR pathway is discussed. Finally, we cover the interplay of ER stress in the development of diseases.","doi":"10.1042/BSR20140058","authors":"Wu H, Ng BS, Thibault G","authors_abbrev":"Wu H et al.","pubmed_publication_date":"01 Jul 2014","pubmed_entrez_date":"2014-06-10","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC12116","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2230715","title":"Effect of ethanol on the phospholipid and fatty acid content of Schizosaccharomyces pombe membranes.","citation":"J Gen Microbiol 1990 Jul;136(7):1271-7","abstract":"Ethanol at concentrations up to 5% (v/v) had no effect on the growth of Schizosaccharomyces pombe, whereas concentrations over 7.5% were inhibitory. The major membrane phospholipids in S. pombe cells growing aerobically in the absence of added ethanol were phosphatidylinositol, phosphatidylcholine and phosphatidylethanolamine. Oleic acid (18:1) was the main fatty acid. When ethanol (7.5%) was added to aerobically growing cultures, the phosphatidylinositol content increased, whereas the 18:1 content decreased. Similar changes were observed in the membrane phospholipids of cells grown anaerobically without ethanol. However, the presence of ethanol in anaerobically growing cultures had an opposite effect on fatty acids, as the 18:1 content increased. The results support the idea that ethanol tolerance in S. pombe may be connected with a high content of 18:1 fatty acids, and with the ability to maintain a high rate of phospholipid biosynthesis.","authors":"Koukou AI, Tsoukatos D, Drainas C","authors_abbrev":"Koukou AI et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15280226","title":"Functional dissection of the gamma-tubulin complex by suppressor analysis of gtb1 and alp4 mutations in Schizosaccharomyces pombe.","citation":"Genetics 2004 Jul;167(3):1095-107","abstract":"In fission yeast, gamma-tubulin (encoded by the gtb1+ gene), Alp4 (Spc97/GCP2), and Alp6 (Spc98/GCP3) are essential components of the gamma-tubulin complex. We isolated gtb1 mutants as allele-specific suppressors of temperature-sensitive alp4 mutations. Mutation sites in gtb1 mutants and in several alp4 alleles were determined. The majority of substituted amino acids were mapped to a small area on the predicted surface of the gamma-tubulin molecule that might directly interact with the Alp4 protein. The cold sensitivity of gamma-tubulin mutants was almost completely suppressed by an alpha-tubulin mutation and partially suppressed by a low concentration of thiabendazole, a microtubule assembly inhibitor. Other gtb1 mutants had increased resistance to this drug. Gel-filtration and immunoprecipitation analyses suggested that the mutant gamma-tubulin formed an altered gamma-tubulin complex with increased stability compared to wild-type gamma-tubulin. In most gtb1 mutants, sexual development was impaired, and aberrant asci that contained an irregular spore shape and number were produced. In contrast, spore formation was not appreciably damaged in some alp4 and alp6 mutants, even at temperatures where vegetative proliferation was substantially defective. These results suggested that the function of the gamma-tubulin complex or the requirement of each component of the complex is differentially regulated between the vegetative and sexual phases of the life cycle in fission yeast. In addition, genetic data indicated intimate functional connections of gamma-tubulin with several kinesin-like proteins.","authors":"Tange Y, Fujita A, Toda T, Niwa O","authors_abbrev":"Tange Y et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-07-29","publication_year":"2004","canto_session_key":"2f05d7fb9c25573f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-07-20 14:23:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-23 14:25:54","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPCC736.14","SPBC1685.15c","SPBC800.05c","SPBC2F12.13","SPBC428.20c","SPBC365.15"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2015-04-23"},{"uniquename":"PMID:14592707","title":"Mad1p, a component of the spindle assembly checkpoint in fission yeast, suppresses a novel septation-defective mutant, sun1, in a cell-division cycle.","citation":"FEMS Microbiol Lett 2003 Oct 24;227(2):183-8","abstract":"To enhance our understanding of the cytokinesis, we have carried out a genetic screen for temperature-sensitive Schizosaccharomyces pombe mutants that show defects in septum formation and cell division. Here we present the isolation and characterization of a new temperature-sensitive mutant, sun1 (septum uncontrolled), which undergoes uncontrolled septation during cell-division cycle at restrictive temperature (37 degrees C). In sun1 mutant, the actin ring and septum are positioned at random locations and angles, and the nuclear division cycle continues. These observations suggest that the sun1 gene product is required for the proper placement of the actin ring as well as precise septation. In a screen for the sun1(+) gene to complement the sun1 mutant, we have isolated a mad1(+) (mitotic arrest deficient) gene, which encodes a component of the spindle checkpoint in the cell-division cycle. Analysis of crossing the sun1 cell with the mad1(+) null mutant indicates that mad1(+) suppresses the sun1 mutant defective in controlled septation in a cell-division cycle.","authors":"Kim IG, Rhee DK, Jeong JW, Kim SC, Won M, Lee J, Song KW, Kim HB","authors_abbrev":"Kim IG et al.","pubmed_publication_date":"24 Oct 2003","pubmed_entrez_date":"2003-11-01","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17409062","title":"Suppression of the Schizosaccharomyces pombe cut12.1 cell-cycle defect by mutations in cdc25 and genes involved in transcriptional and translational control.","citation":"Genetics 2007 May;176(1):73-83","abstract":"Cdc25 phosphatase primes entry to mitosis by removing the inhibitory phosphate that is transferred to mitosis promoting factor (MPF) by Wee1 related kinases. A positive feedback loop then boosts Cdc25 and represses Wee1 activities to drive full-scale MPF activation and commitment to mitosis. Dominant mutations in the Schizosaccharomyces pombe spindle pole body (SPB) component Cut12 enable cdc25.22 mutants to overcome a G2 arrest at 36 degrees and enter mitosis. The recessive temperature-sensitive cut12.1 mutation results in the formation of monopolar spindles in which the spindle pole marker Sad1 is enriched on the nonfunctional SPB at 36 degrees . We identified mutations at five loci that suppressed the lethality of the recessive cut12.1 mutation at 36 degrees and conferred lethality at 20 degrees . Three of the five mutations led to the formation of monopolar spindles at restrictive temperatures, affected cell size at commitment to mitosis, and generated multiple Sad1 foci at nuclear periphery. The five loci, tfb2.rt1, tfb5.rt5, pla1.rt3, rpl4301.rt4, and rot2.1, and multicopy suppressors, including tfb1(+) and dbp10(+), are involved in transcription, translation, or RNA processing, prompting us to establish that elevating Cdc25 levels with the dominant cdc25.d1 allele, suppressed cut12.1. Thus, rot mutants provide a further link between protein production and cell-cycle progression.","authors":"Tallada VA, Bridge AJ, Emery PA, Hagan IM","authors_abbrev":"Tallada VA et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-04-06","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC32F12.15","SPBC649.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:12417737","title":"Two ubiquitin-conjugating enzymes, Rhp6 and UbcX, regulate heterochromatin silencing in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2002 Dec;22(23):8366-74","abstract":"Methylation of histone H3 has been linked to the assembly of higher-order chromatin structures. Very recently, several examples, including the Schizosaccharomyces pombe mating-type region, chicken beta-globin locus, and inactive X-chromosome, revealed that H3-Lys9-methyl (Me) is associated with silent chromatin while H3-Lys4-Me is prominent in active chromatin. Surprisingly, it was shown that homologs of Drosophila Su(var)3-9 specifically methylate the Lys9 residue of histone H3. Here, to identify putative enzymes responsible for destabilization of heterochromatin, we screened genes whose overexpressions disrupt silencing at the silent mat3 locus in fission yeast. Interestingly, we identified two genes, rhp6(+) and ubcX(+) (ubiquitin-conjugating enzyme participating in silencing), both of which encode ubiquitin-conjugating enzymes. Their overexpression disrupted silencing at centromeres and telomeres as well as at mat3. Additionally, the overexpression interfered with centromeric function, as confirmed by elevated minichromosome loss and antimicrotubule drug sensitivity. On the contrary, deletion of rhp6(+) or ubcX(+) enhanced silencing at all heterochromatic regions tested, indicating that they are negative regulators of silencing. More importantly, chromatin immunoprecipitation showed that their overexpression alleviated the level of H3-Lys9-Me while enhancing the level of H3-Lys4-Me at the silent regions. On the contrary, their deletions enhanced the level of H3-Lys9-Me while alleviating that of H3-Lys4-Me. Taken together, the data suggest that two ubiquitin-conjugating enzymes, Rhp6 and UbcX, affect methylation of histone H3 at silent chromatin, which then reconfigures silencing.","authors":"Choi ES, Kim HS, Jang YK, Hong SH, Park SD","authors_abbrev":"Choi ES et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2002-11-06","publication_year":"2002","canto_session_key":"791b07062cacb59e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-27 16:04:24","canto_approved_date":"2020-01-23 18:46:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-12 18:49:30","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.07c","SPBC1105.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-11-27"},{"uniquename":"PMID:12535076","title":"Modified yeast cells to investigate the coupling of G protein-coupled receptors to specific G proteins.","citation":"Mol Microbiol 2003 Feb;47(3):781-92","abstract":"G protein-coupled receptors (GPCRs) help to regulate the physiology of all the major organ systems. They respond to a multitude of ligands and activate a range of effector proteins to bring about the appropriate cellular response. The choice of effector is largely determined by the interaction of individual GPCRs with different G proteins. Several factors influence this interaction, and a better understanding of the process may enable a more rational approach to identifying compounds that affect particular signalling pathways. A number of systems have been developed for the analysis of GPCRs. All provide useful information, but the genetic amenability and relative simplicity of yeast makes them a particularly attractive option for ligand identification and pharmaceutical screening. Many, but not all, GPCRs are functional in the budding yeast Saccharomyces cerevisiae, and we have developed reporter strains of the fission yeast Schizosaccharomyces pombe as an alternative host. To provide a more generic system for investigating GPCRs, we created a series of yeast-human Galpha-transplants, in which the last five residues at the C-terminus of the yeast Galpha-subunit are replaced with the corresponding residues from different human G proteins. These enable GPCRs to be coupled to the Sz. pombe signalling machinery so that stimulation with an appropriate ligand induces the expression of a signal-dependent lacZ reporter gene. We demonstrate the specificity of the system using corticotropin releasing factor (CRF) and CRF-related peptides on two CRF receptors. We find that different combinations of ligand and receptor activate different Galpha-transplants, and the specificity of the coupling is similar to that in mammalian systems. Thus, CRF signalled through the Gs- and Gi-transplants, consistent with its regulation of adenylate cyclase, and was more active against the CRF-R1A receptor than against the CRF-R2B receptor. In contrast, urocortin II and urocortin III were selective for the CRF-R2B receptors. Furthermore, urocortin, but not CRF, induced signalling through the CRF-R1A receptor and the Gq-transplant. This is the first time that human GPCRs have been coupled to the signalling pathway in Sz. pombe, and the strains described in this study will complement the other systems available for studying this important family of receptors.","authors":"Ladds G, Davis K, Hillhouse EW, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-01-22","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25057016","title":"Csi1p recruits alp7p/TACC to the spindle pole bodies for bipolar spindle formation.","citation":"Mol Biol Cell 2014 Sep 15;25(18):2750-60","abstract":"Accurate chromosome segregation requires timely bipolar spindle formation during mitosis. The transforming acidic coiled-coil (TACC) family proteins and the ch-TOG family proteins are key players in bipolar spindle formation. They form a complex to stabilize spindle microtubules, mainly dependent on their localization to the centrosome (the spindle pole body [SPB] in yeast). The molecular mechanism underlying the targeting of the TACC-ch-TOG complex to the centrosome remains unclear. Here we show that the fission yeast Schizosaccharomyces pombe TACC orthologue alp7p is recruited to the SPB by csi1p. The csi1p-interacting region lies within the conserved TACC domain of alp7p, and the carboxyl-terminal domain of csi1p is responsible for interacting with alp7p. Compromised interaction between csi1p and alp7p impairs the localization of alp7p to the SPB during mitosis, thus delaying bipolar spindle formation and leading to anaphase B lagging chromosomes. Hence our study establishes that csi1p serves as a linking molecule tethering spindle-stabilizing factors to the SPB for promoting bipolar spindle assembly.","doi":"10.1091/mbc.E14-03-0786","authors":"Zheng F, Li T, Jin DY, Syrovatkina V, Scheffler K, Tran PT, Fu C","authors_abbrev":"Zheng F et al.","pubmed_publication_date":"15 Sep 2014","pubmed_entrez_date":"2014-07-25","publication_year":"2014","canto_session_key":"a475b51d06fe1b16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-07-31 08:07:42","canto_approved_date":"2025-09-04 11:33:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-21 09:34:09","canto_added_date":"2014-07-26 00:15:28","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":35,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC895.07","SPAC890.02c","SPBC2G2.14"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2023-07-31"},{"uniquename":"PMID:33992089","title":"Impact of uORFs in mediating regulation of translation in stress conditions.","citation":"BMC Mol Cell Biol 2021 May 16;22(1):29","abstract":"A large fraction of genes contains upstream ORFs (uORFs) in the 5' untranslated region (5'UTR). The translation of uORFs can inhibit the translation of the main coding sequence, for example by causing premature dissociation of the two ribosomal units or ribosome stalling. However, it is currently unknown if most uORFs are inhibitory or if this activity is restricted to specific cases. Here we interrogate ribosome profiling data from three different stress experiments in yeast to gain novel insights into this question.\nBy comparing ribosome occupancies in different conditions and experiments we obtain strong evidence that, in comparison to primary coding sequences (CDS), which undergo translational arrest during stress, the translation of uORFs is mostly unaffected by changes in the environment. As a result, the relative abundance of uORF-encoded peptides increases during stress. In general, the changes in the translational efficiency of regions containing uORFs do not seem to affect downstream translation. The exception are uORFs found in a subset of genes that are significantly up-regulated at the level of translation during stress; these uORFs tend to be translated at lower levels in stress conditions than in optimal growth conditions, facilitating the translation of the CDS during stress. We find new examples of uORF-mediated regulation of translation, including the Gcn4 functional homologue fil1 and ubi4 genes in S. pombe.\nWe find evidence that the relative amount of uORF-encoded peptides increases during stress. The increased translation of uORFs is however uncoupled from the general CDS translational repression observed during stress. In a subset of genes that encode proteins that need to be rapidly synthesized upon stress uORFs act as translational switches.","doi":"10.1186/s12860-021-00363-9","authors":"Moro SG, Hermans C, Ruiz-Orera J, Albà MM","authors_abbrev":"Moro SG et al.","pubmed_publication_date":"16 May 2021","pubmed_entrez_date":"2021-05-16","publication_year":"2021","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2021-05-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32313168","title":"Serine catabolism produces ROS, sensitizes cells to actin dysfunction, and suppresses cell growth in fission yeast.","citation":"J Antibiot (Tokyo) 2020 Aug;73(8):574-580","abstract":"Serine is an essential component in organisms as a building block of biomolecules, a precursor of metabolites, an allosteric regulator of an enzyme, etc. This amino acid is thought to be a key metabolite in human diseases including cancers and infectious diseases. To understand the consequence of serine catabolism, we screened natural products to identify a fungal metabolite chaetoglobosin D (ChD) as a specific inhibitor of fission yeast cell growth when cultivated with serine as a sole nitrogen source. ChD targets actin, and actin mutant cells showed severe growth defect on serine medium. ROS accumulated in cells when cultivated in serine medium, while actin mutant cells showed increased sensitivity to oxidative stress. ROS production is a new aspect of serine metabolism, which might be involved in disease progression, and actin could be the drug target for curing serine-dependent symptoms.","doi":"10.1038/s41429-020-0305-6","authors":"Kanou A, Nishimura S, Tabuchi T, Matsuyama A, Yoshida M, Kato T, Kakeya H","authors_abbrev":"Kanou A et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-04-22","publication_year":"2020","canto_session_key":"8d053bcab39833a9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"西村慎一","canto_first_approved_date":"2020-12-18 09:25:14","canto_approved_date":"2020-12-18 09:25:14","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-12-14 06:50:02","canto_added_date":"2020-04-23 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"西村慎一","community_curator":true,"annotation_count":2,"orcid":"0000-0002-5998-3780","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-12-18"},{"uniquename":"PMID:17005909","title":"Rho2 is a target of the farnesyltransferase Cpp1 and acts upstream of Pmk1 mitogen-activated protein kinase signaling in fission yeast.","citation":"Mol Biol Cell 2006 Dec;17(12):5028-37","abstract":"We have previously demonstrated that knockout of the calcineurin gene or inhibition of calcineurin activity by immunosuppressants resulted in hypersensitivity to Cl- in fission yeast. We also demonstrated that knockout of the components of the Pmk1 mitogen-activated protein kinase (MAPK) pathway, such as Pmk1 or Pek1 complemented the hypersensitivity to Cl-. Using this interaction between calcineurin and Pmk1 MAPK, here we developed a genetic screen that aims to identify new regulators of the Pmk1 signaling and isolated vic (viable in the presence of immunosuppressant and chloride ion) mutants. One of the mutants, vic1-1, carried a missense mutation in the cpp1+ gene encoding a beta subunit of the protein farnesyltransferase, which caused an amino acid substitution of aspartate 155 of Cpp1 to asparagine (Cpp1(D155N)). Analysis of the mutant strain revealed that Rho2 is a novel target of Cpp1. Moreover, Cpp1 and Rho2 act upstream of Pck2-Pmk1 MAPK signaling pathway, thereby resulting in the vic phenotype upon their mutations. Interestingly, compared with other substrates of Cpp1, defects of Rho2 function were more phenotypically manifested by the Cpp1(D155N) mutation. Together, our results demonstrate that Cpp1 is a key component of the Pck2-Pmk1 signaling through the spatial control of the small GTPase Rho2.","authors":"Ma Y, Kuno T, Kita A, Asayama Y, Sugiura R","authors_abbrev":"Ma Y et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-09-29","publication_year":"2006","canto_session_key":"d478de3cd9fda2d4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPAC17G6.04c","SPAC1F3.02c","SPAC17G8.14c","SPBC12D12.04c","SPAC16.01","SPBC119.08","SPBC543.07"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:5878307","title":"Screening of auxotrophic mutants of Schizosaccharomyces pombe with 2-deoxyglucose.","citation":"Mutat Res 1965 Aug;2(4):328-31","abstract":"","authors":"Megnet R","authors_abbrev":"Megnet R","pubmed_publication_date":"Aug 1965","pubmed_entrez_date":"1965-08-01","publication_year":"1965","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8392846","title":"The Schizosaccharomyces pombe pde1/cgs2 gene encodes a cyclic AMP phosphodiesterase.","citation":"Biochem Biophys Res Commun 1993 Jul 15;194(1):79-82","abstract":"We previously reported the identification of eight Sz. pombe cDNA clones that are capable of suppressing the heat-shock sensitive phenotype associated with deletion of IRA1 in S. cerevisiae. We report that one of these cDNA clones, pPSI5, encodes a protein, Pde1, that is 24% identical to the S. cerevisiae low-affinity cAMP phosphodiesterase. The pde1/cgs2 gene encoding this protein has been previously identified, and studies have shown that deletion of this gene results in elevated levels of intracellular cAMP and inhibition of meiosis. To demonstrate that Pde1 is a cAMP phosphodiesterase we expressed it in an S. cerevisiae strain which lacks the genomic cAMP phosphodiesterase genes. Extracts from such cells that express the Sz. pombe Pde1 exhibit high levels of cAMP phosphodiesterase activity.","authors":"Matviw H, Li J, Young D","authors_abbrev":"Matviw H et al.","pubmed_publication_date":"15 Jul 1993","pubmed_entrez_date":"1993-07-15","publication_year":"1993","canto_session_key":"4c0171c2779a200c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 14:07:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 14:07:06","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC285.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:33437930","title":"Pyrogallol induces oxidative stress defects in the fission yeast  S. pombe .","citation":"MicroPubl Biol 2021 Jan 07;2021","abstract":"Apart from the beneficial roles of pyrogallol in industries, it also tends to produce free radicals that trigger apoptosis in human cells. In this study, we checked the toxic effect of pyrogallol in fission yeast  S. pombe  cells. We observed that the wild type and  wat1/pop3  delete cells were unable to grow on plates containing pyrogallol in a dose-dependent manner. Furthermore, the  wat1/pop3  delete cells exhibit higher sensitivity against pyrogallol as compared to wild type cells suggesting that the pyrogallol induces oxidative stress. The exposure to pyrogallol also leads to the production of ROS and affects the sporulation in  S. pombe. ","doi":"10.17912/micropub.biology.000348","authors":"Ahamad N, Anjum S, Ahmed S","authors_abbrev":"Ahamad N et al.","pubmed_publication_date":"07 Jan 2021","pubmed_entrez_date":"2021-01-13","publication_year":"2021","canto_session_key":"ab9f58e60ef0a260","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shakil Ahmed","canto_first_approved_date":"2025-01-08 11:38:43","canto_approved_date":"2025-01-08 11:38:43","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-01-02 10:02:43","canto_added_date":"2021-01-15 01:15:05","annotation_curators":[{"name":"Shakil Ahmed","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21B10.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2025-01-08"},{"uniquename":"PMID:3011605","title":"Cloning and characterization of the Schizosaccharomyces pombe DNA ligase gene CDC17.","citation":"Gene 1986;41(2-3):321-5","abstract":"The Schizosaccharomyces pombe CDC17 gene has been cloned by complementation of the cdc17 mutant coding for temperature-sensitive DNA ligase. An allele-specific suppressor active only in the presence of a high osmotic pressure was also isolated. The cloned CDC17 gene failed to complement the analogous DNA ligase mutation, cdc9, in Saccharomyces cerevisiae, although the reverse complementation was successful [Barker and Johnston, Eur. J. Biochem. 134 (1983) 315-319]. The CDC17 gene specifies a 2.8-kb transcript.","authors":"Johnston LH, Barker DG, Nurse P","authors_abbrev":"Johnston LH et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_session_key":"4016ba9b210adaaa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-09-24 12:55:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 12:55:32","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-24"},{"uniquename":"PMID:3892556","title":"Ultraweak bioluminescence spectra of stationary phase Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Photochem Photobiol 1985 May;41(5):611-5","abstract":"","authors":"Quickenden TI, Comarmond MJ, Tilbury RN","authors_abbrev":"Quickenden TI et al.","pubmed_publication_date":"May 1985","pubmed_entrez_date":"1985-05-01","publication_year":"1985","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10521402","title":"Meiotic DNA replication checkpoint control in fission yeast.","citation":"Genes Dev 1999 Oct 01;13(19):2581-93","abstract":"In eukaryotes, the DNA replication checkpoint prevents entry into mitosis when DNA replication is incomplete and is crucial for maintaining genomic integrity. Much less is known about equivalent controls that operate during meiosis. Here, we show that a DNA replication checkpoint control operates during meiosis in fission yeast. The mitotic checkpoint Rad genes and the Cds1 protein kinase are required for the DNA replication checkpoint during meiosis, with Cds1 playing a more prominent role than it does during mitosis. When DNA replication is blocked, the checkpoint maintains Cdc2 tyrosine 15 phosphorylation keeping Cdc2 protein kinase activity low and preventing onset of meiosis I. Additionally, there is a second checkpoint acting during meiosis that is revealed if cells are prevented from maintaining Cdc2 tyrosine 15 phosphorylation when DNA replication is blocked. Such cells arrest with high Cdc2 protein kinase activity and separated spindle pole bodies, an arrest state similar to that observed in mitotic budding yeast cells when DNA replication is incomplete. This second checkpoint is meiosis specific and may reflect processes occurring only during meiosis such as increased recombination rates, an extended duration of nuclear division, or homolog chromosome pairing.","authors":"Murakami H, Nurse P","authors_abbrev":"Murakami H et al.","pubmed_publication_date":"01 Oct 1999","pubmed_entrez_date":"1999-10-16","publication_year":"1999","canto_session_key":"e6d26db4caf74ac5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-11-26 11:25:40","canto_approved_date":"2022-05-31 06:47:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-11-14 16:02:51","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":30,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC342.05","SPAC20G4.04c","SPBC11B10.09","SPAC1952.07","SPBC582.03","SPAC14C4.13","SPCC1259.13","SPCC18B5.11c","SPBC19C2.05","SPAC664.07c","SPCC18B5.03","SPBC216.05","SPBC660.14"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2018-11-26"},{"uniquename":"PMID:36012759","title":"The Catalytic Subunit of  Schizosaccharomyces pombe  CK2 (Cka1) Negatively Regulates RNA Polymerase II Transcription through Phosphorylation of Positive Cofactor 4 (PC4).","citation":"Int J Mol Sci 2022 Aug 22;23(16)","abstract":"Positive cofactor 4 (PC4) is a transcriptional coactivator that plays important roles in transcription and DNA replication. In mammals, PC4 is phosphorylated by CK2, and this event downregulates its RNA polymerase II (RNAPII) coactivator function. This work describes the effect of fission yeast PC4 phosphorylation on RNAPII transcription in a cell extract, which closely resembles the cellular context. We found that fission yeast PC4 is strongly phosphorylated by the catalytic subunit of CK2 (Cka1), while the regulatory subunit (Ckb1) downregulates the PC4 phosphorylation. The addition of Cka1 to an in vitro transcription assay can diminish the basal transcription from the Ad-MLP promoter; however, the addition of recombinant fission yeast PC4 or Ckb1 can stimulate the basal transcription in a cell extract. Fission yeast PC4 is phosphorylated in a domain which has consensus phosphorylation sites for CK2, and two serine residues were identified as critical for CK2 phosphorylation. Mutation of one of the serine residues in PC4 does not completely abolish the phosphorylation; however, when the two serine residues are mutated, CK2 is no longer able to phosphorylate PC4. The mutant which is not phosphorylated is able to stimulate transcription even though it is previously phosphorylated by Cka1, while the wild type and the point mutant are inactivated by Cka1 phosphorylation, and they cannot stimulate transcription by RNAPII in cell extracts. Those results demonstrate that CK2 can regulate the coactivator function of fission yeast PC4 and suggests that this event could be important in vivo as well.","doi":"10.3390/ijms23169499","authors":"Rojas DA, Urbina F, Solari A, Maldonado E","authors_abbrev":"Rojas DA et al.","pubmed_publication_date":"22 Aug 2022","pubmed_entrez_date":"2022-08-26","publication_year":"2022","canto_session_key":"3b44c4bd366e6d3c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-08-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:13597911","title":"Identification of the nucleus of a fission yeast with fluorescent dyes.","citation":"Exp Cell Res 1958 Oct;15(2):444-6","abstract":"","authors":"RUSTAD RC","authors_abbrev":"RUSTAD RC","pubmed_publication_date":"Oct 1958","pubmed_entrez_date":"1958-10-01","publication_year":"1958","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25602522","title":"The impact of the HIRA histone chaperone upon global nucleosome architecture.","citation":"Cell Cycle 2015;14(1):123-34","abstract":"HIRA is an evolutionarily conserved histone chaperone that mediates replication-independent nucleosome assembly and is important for a variety of processes such as cell cycle progression, development, and senescence. Here we have used a chromatin sequencing approach to determine the genome-wide contribution of HIRA to nucleosome organization in Schizosaccharomyces pombe. Cells lacking HIRA experience a global reduction in nucleosome occupancy at gene sequences, consistent with the proposed role for HIRA in chromatin reassembly behind elongating RNA polymerase II. In addition, we find that at its target promoters, HIRA commonly maintains the full occupancy of the -1 nucleosome. HIRA does not affect global chromatin structure at replication origins or in rDNA repeats but is required for nucleosome occupancy in silent regions of the genome. Nucleosome organization associated with the heterochromatic (dg-dh) repeats located at the centromere is perturbed by loss of HIRA function and furthermore HIRA is required for normal nucleosome occupancy at Tf2 LTR retrotransposons. Overall, our data indicate that HIRA plays an important role in maintaining nucleosome architecture at both euchromatic and heterochromatic loci.","doi":"10.4161/15384101.2014.967123","authors":"Gal C, Moore KM, Paszkiewicz K, Kent NA, Whitehall SK","authors_abbrev":"Gal C et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-01-21","publication_year":"2015","canto_session_key":"b9fa1072a11e2647","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-07 16:36:02","canto_approved_date":"2022-06-29 11:47:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-07 16:35:54","canto_added_date":"2015-01-22 01:15:29","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.05","SPBC31F10.13c","SPAC1783.07c","SPAC1783.06c","SPAC3G6.01"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2016-04-07"},{"uniquename":"PMID:27432898","title":"A single-headed fission yeast myosin V transports actin in a tropomyosin-dependent manner.","citation":"J Cell Biol 2016 Jul 18;214(2):167-79","abstract":"Myo51, a class V myosin in fission yeast, localizes to and assists in the assembly of the contractile ring, a conserved eukaryotic actomyosin structure that facilitates cytokinesis. Rng8 and Rng9 are binding partners that dictate the cellular localization and function of Myo51. Myo51 was expressed in insect cells in the presence or absence of Rng8/9. Surprisingly, electron microscopy of negatively stained images and hydrodynamic measurements showed that Myo51 is single headed, unlike most class V myosins. When Myo51-Rng8/9 was bound to actin-tropomyosin, two attachment sites were observed: the typical ATP-dependent motor domain attachment and a novel ATP-independent binding of the tail mediated by Rng8/9. A modified motility assay showed that this additional binding site anchors Myo51-Rng8/9 so that it can cross-link and slide actin-tropomyosin filaments relative to one another, functions that may explain the role of this motor in contractile ring assembly.","doi":"10.1083/jcb.201511102","authors":"Tang Q, Billington N, Krementsova EB, Bookwalter CS, Lord M, Trybus KM","authors_abbrev":"Tang Q et al.","pubmed_publication_date":"18 Jul 2016","pubmed_entrez_date":"2016-07-20","publication_year":"2016","canto_session_key":"0118151b17e0b012","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-21 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2D10.14c","SPAC3A12.14","SPAC4H3.14c","SPAP8A3.08","SPBP8B7.02"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:36477651","title":"S. pombe wtf drivers use dual transcriptional regulation and selective protein exclusion from spores to cause meiotic drive.","citation":"PLoS Genet 2022 Dec;18(12):e1009847","abstract":"Meiotic drivers bias gametogenesis to ensure their transmission into more than half the offspring of a heterozygote. In Schizosaccharomyces pombe, wtf meiotic drivers destroy the meiotic products (spores) that do not inherit the driver from a heterozygote, thereby reducing fertility. wtf drivers encode both a Wtfpoison protein and a Wtfantidote protein using alternative transcriptional start sites. Here, we analyze how the expression and localization of the Wtf proteins are regulated to achieve drive. We show that transcriptional timing and selective protein exclusion from developing spores ensure that all spores are exposed to Wtf4poison, but only the spores that inherit wtf4 receive a dose of Wtf4antidote sufficient for survival. In addition, we show that the Mei4 transcription factor, a master regulator of meiosis, controls the expression of the wtf4poison transcript. This transcriptional regulation, which includes the use of a critical meiotic transcription factor, likely complicates the universal suppression of wtf genes without concomitantly disrupting spore viability. We propose that these features contribute to the evolutionary success of the wtf drivers.","doi":"10.1371/journal.pgen.1009847","authors":"Nuckolls NL, Nidamangala Srinivasa A, Mok AC, Helston RM, Bravo Núñez MA, Lange JJ, Gallagher TJ, Seidel CW, Zanders SE","authors_abbrev":"Nuckolls NL et al.","pubmed_publication_date":"Dec 2022","pubmed_entrez_date":"2022-12-08","publication_year":"2022","canto_session_key":"e337f624ad51f24f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-12-09 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39527202","title":"Investigating Fission Yeast Mutagenesis Using Canavanine Sensitivity Assays.","citation":"Methods Mol Biol 2025;2862:195-208","abstract":"Fission yeast are genetically tractable and amenable to mutagenesis studies. Canavanine is a toxic antimetabolite that can be used to test mutation rate. Recent studies have shown that the molecular genetics of canavanine sensitivity are more complex than previously anticipated. However, genomics advances indicate that canavanine use to determine mutation remains an option. In this chapter, we provide methods to grow fission yeast and detect forward mutation in populations of canavanine-sensitive Schizosaccharomyces pombe. Wild-type S. pombe are functionally canavanine-sensitive and die in the presence of canavanine. These protocols use liquid cultures that are tested for density and viability through colony formation. The same cultures are plated onto canavanine-containing media. Cells are grown to find cells that can grow on the canavanine media. These resistant cells are compared to the number plated, and a mutation rate is calculated. While the protocol is straightforward, analysis and application of the data are evolving. These methods provide the ability to compare S. pombe mutant strains for the frequency and rate of mutation.","doi":"10.1007/978-1-0716-4168-2_14","authors":"Karam E, Sabatinos SA","authors_abbrev":"Karam E et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18758731","title":"The role and regulation of Trxl, a cytosolic thioredoxin in Schizosaccharomyces pombe.","citation":"J Microbiol 2008 Aug;46(4):408-14","abstract":"The genome of fission yeast Schizosaccharomyces pombe harbors two genes for thioredoxins, trx1(+) and trx2(+), which encode cytosolic and mitochondrial thioredoxins, respectively. The Deltatrx1 mutant was found sensitive to diverse external stressors such as various oxidants, heat, and salt, whereas Deltatrx2 mutant was not sensitive except to paraquat, a superoxide generator. Both Deltatrx1 and Deltatrx2 mutants were more resistant to diamide, a thiol-specific oxidant, than the wild type. The trx1(+) gene expression was induced by H(2)O(2) and menadione, being mediated through a stress-responsive transcription factor Papl. In Deltatrx1 cells, the basal expression of Pap1-regulated genes were elevated, suggesting a role for Trxl as a reducer for oxidized (activated) Papl. The Deltatrx1 mutant exhibited cysteine auxotrophy, which can be overcome by adding sulfite. This suggests that Trxl serves as a primary electron donor for 3'-phosphoadenosine-5'-phosphosulfate (PAPS) reductase and thus is an essential protein for sulfur assimilation in S. pombe. These results suggest that, in contrast to Trx2 whose role is more confined to mitochondrial functions, Trxl plays a major role in protecting S. pombe against various stressful conditions and enables proper sulfur metabolism.","doi":"10.1007/s12275-008-0076-4","authors":"Song JY, Roe JH","authors_abbrev":"Song JY et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-09-02","publication_year":"2008","canto_session_key":"87ac43cba4cb93a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-26 21:11:18","canto_approved_date":"2026-05-27 12:24:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 09:59:07","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC757.07c","SPAC7D4.07c","SPAC1783.07c","SPBC12D12.07c","SPBC29B5.01","SPBC3F6.03"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2015-01-26"},{"uniquename":"PMID:30670704","title":"lncRNA transcriptional initiation induces chromatin remodeling within a limited range in the fission yeast fbp1 promoter.","citation":"Sci Rep 2019 Jan 22;9(1):299","abstract":"Long noncoding RNAs (lncRNAs) transcribed across gene promoters have been detected. These regulate transcription by mechanisms that have not been fully elucidated. We herein show that the chromatin configuration is altered into an accessible state within 290 bp downstream from the initiation site of metabolic-stress-induced lncRNAs (mlonRNAs) in the promoter of the fission yeast fbp1 gene, whose transcription is massively induced upon glucose starvation. Chromatin upstream from fbp1 is progressively altered into an open configuration, as a cascade of transcription of three overlapping mlonRNA species (-a, -b and -c in order) occurs with transcriptional initiation sites progressing 5' to 3' upstream of the fbp1 promoter. Initiation of the shortest mlonRNA (mlonRNA-c) induces chromatin remodeling around a transcription factor-binding site and subsequent massive induction of fbp1. We identify the cis-element required for mlonRNA-c initiation, and by changing the distance between mlonRNA-initiation site and the transcription factor-binding site, we show that mlonRNA-initiation effectively induces chromatin remodeling in a limited distance within 290 bp. These results indicate that mlonRNAs are transcribed across the fbp1 promoter as a short-range inducer for local chromatin alterations, and suggest that strict chromatin modulation is archived via stepwise mlonRNA-initiations.","doi":"10.1038/s41598-018-36049-0","authors":"Senmatsu S, Asada R, Abe T, Hoffman CS, Ohta K, Hirota K","authors_abbrev":"Senmatsu S et al.","pubmed_publication_date":"22 Jan 2019","pubmed_entrez_date":"2019-01-24","publication_year":"2019","canto_session_key":"3ff8ede62899c8d2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-01-25 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41118763","title":"Delayed protein translocation protects mitochondria against toxic CAT-tailed proteins.","citation":"Mol Cell 2025 Nov 06;85(21):4082-4092.e7","abstract":"Ribosome-associated protein quality control (RQC) protects cells against the toxic effects of faulty polypeptides produced by stalled ribosomes. However, mitochondria are vulnerable to C-terminal alanyl and threonyl (CAT)-tailed proteins that are generated in this process, and faulty nuclear-encoded mitochondrial proteins are handled by the recently discovered mitoRQC. Here, we performed a genome-wide screen in yeast to identify additional proteins involved in mitoRQC. We found that peptidyl-tRNA hydrolase 2 (Pth2), present in the mitochondrial outer membrane, influences aggregation of CAT-tailed proteins without majorly affecting the CAT-tailing process itself. Peptidyl-tRNA hydrolase activity is essential during this process, yet the activity of Pth2 can be substituted by another peptidyl-tRNA hydrolase upon proper localization. Our data suggest that Pth2 acts by modulating protein translocation and that the mitochondrial proteostasis network is relieved through increased access of CAT-tailed proteins to cytosolic chaperones. Other hits obtained in the screen show that, in general, delayed protein translocation protects mitochondria against toxic CAT-tailed proteins.","doi":"10.1016/j.molcel.2025.09.030","authors":"Bertram N, Izawa T, Thoma F, Schwenkert S, Duvezin-Caubet S, Park SH, Wagener N, Devin A, Osman C, Neupert W, Mokranjac D","authors_abbrev":"Bertram N et al.","pubmed_publication_date":"06 Nov 2025","pubmed_entrez_date":"2025-10-21","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19A8.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21264388","title":"Comment on \"Deletion of btn1, an orthologue of CLN3, increases glycolysis and perturbs amino acid metabolism in the fission yeast model of Batten disease\".","citation":"Mol Biosyst 2011 Apr;7(4):1347-8; author reply 1349","abstract":"We provide a comment on the paper of Pears et al. (Mol. BioSyst., 2010, 6, 1093-1102).","doi":"10.1039/c0mb00299b","authors":"Pearce DA, Padilla-Lopez S","authors_abbrev":"Pearce DA et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2011-01-26","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12181359","title":"Role of the Rab GTP-binding protein Ypt3 in the fission yeast exocytic pathway and its connection to calcineurin function.","citation":"Mol Biol Cell 2002 Aug;13(8):2963-76","abstract":"A genetic screen for mutations synthetically lethal with fission yeast calcineurin deletion led to the identification of Ypt3, a homolog of mammalian Rab11 GTP-binding protein. A mutant with the temperature-sensitive ypt3-i5 allele showed pleiotropic phenotypes such as defects in cytokinesis, cell wall integrity, and vacuole fusion, and these were exacerbated by FK506-treatment, a specific inhibitor of calcineurin. Green fluorescent protein (GFP)-tagged Ypt3 showed cytoplasmic staining that was concentrated at growth sites, and this polarized localization required the actin cytoskeleton. It was also detected as a punctate staining in an actin-independent manner. Electron microscopy revealed that ypt3-i5 mutants accumulated aberrant Golgi-like structures and putative post-Golgi vesicles, which increased remarkably at the restrictive temperature. Consistently, the secretion of GFP fused with the pho1(+) leader peptide (SPL-GFP) was abolished at the restrictive temperature in ypt3-i5 mutants. FK506-treatment accentuated the accumulation of aberrant Golgi-like structures and caused a significant decrease of SPL-GFP secretion at a permissive temperature. These results suggest that Ypt3 is required at multiple steps of the exocytic pathway and its mutation affects diverse cellular processes and that calcineurin is functionally connected to these cellular processes.","authors":"Cheng H, Sugiura R, Wu W, Fujita M, Lu Y, Sio SO, Kawai R, Takegawa K, Shuntoh H, Kuno T","authors_abbrev":"Cheng H et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-08-16","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4H10.04","SPAC18G6.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:31817948","title":"Influence of  Saccharomyces  and non- Saccharomyces  Yeasts in the Formation of Pyranoanthocyanins and Polymeric Pigments during Red Wine Making.","citation":"Molecules 2019 Dec 08;24(24)","abstract":"Yeast are able to modulate many sensory parameters of wines during red must fermentation. The effect on color and on the formation of derived pigments during fermentation has been studied thoroughly since the 90s. Yeast can increase grape anthocyanin's color by acidification by hyperchromic effect (increase of flavylium molecules). Recent studies with non- Saccharomyces  species, as  Lachancea thermotolerans,  described the intense effect of some strains on anthocyanin's color, and subsequent, stability, by strongly reducing wine's pH during fermentation. Moreover, selected yeast strains of  Saccharomyces  have been shown to release metabolites such as pyruvic acid or acetaldehyde that promote the formation of vitisin A and B pyranoanthocyanins during must fermentation.  Schizosaccharomyces pombe,  because of its specific metabolism, can produce higher concentrations of pyruvate, which enhances the formation of vitisin A-type derivatives. The hydroxycinnamate decarboxylase activity that some  Saccharomyces  strains express during fermentation also promotes the formation of vinylphenolic derivatives. Some non- Saccharomyces  species, such as  S. pombe  or  P. guilliermondii  can also improve the production of these derivatives compared to selected strains of  Saccharomyces cerevisiae . Lastly, some yeasts are also able to modulate the formations of polymeric pigments between grape anthocyanins and flavonoids, such as catechins and procyanidins.","doi":"10.3390/molecules24244490","authors":"Morata A, Escott C, Loira I, Del Fresno JM, González C, Suárez-Lepe JA","authors_abbrev":"Morata A et al.","pubmed_publication_date":"08 Dec 2019","pubmed_entrez_date":"2019-12-11","publication_year":"2019","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9450053","title":"N-terminal processing of the M-factor mating pheromone in fission yeast.","citation":"Biochem Soc Trans 1997 Nov;25(4):S625","abstract":"","authors":"Hughes M, Davey J","authors_abbrev":"Hughes M et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-02-05","publication_year":"1997","canto_session_key":"30e28ee27fa724a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-08 09:11:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-08 09:11:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPACUNK4.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-08"},{"uniquename":"PMID:21865598","title":"The functionally distinct fission yeast formins have specific actin-assembly properties.","citation":"Mol Biol Cell 2011 Oct;22(20):3826-39","abstract":"Fission yeast expresses three formins required for distinct actin cytoskeletal processes: Cdc12 (cytokinesis), For3 (polarization), and Fus1 (mating). We propose that in addition to differential regulation, key actin-assembly properties tailor formins for a particular role. In direct comparison to the well-studied Cdc12, we report the first in vitro characterization of the actin-assembly properties of For3 and Fus1. All three share fundamental formin activities; however, particular reaction rates vary significantly. Cdc12 is an efficient nucleator (one filament per approximately 3 Cdc12 dimers) that processively elongates profilin-actin at a moderate rate of 10 subunits s(-1) μM(-1), but lacks filament-bundling activity. Fus1 is also an efficient nucleator, yet processively elongates profilin-actin at one-half the rate of and dissociates 10-fold more rapidly than Cdc12; it also bundles filaments. For3 nucleates filaments 100-fold less well than Fus1, but like Cdc12, processively elongates profilin-actin at a moderate rate and lacks filament-bundling activity. Additionally, both the formin homology FH1 and FH2 domains contribute to the overall rate of profilin-actin elongation. We also confirmed the physiological importance of the actin-assembly activity of the fission yeast formins. Point mutants that disrupt their ability to stimulate actin assembly in vitro do not function properly in vivo.","doi":"10.1091/mbc.E11-06-0492","authors":"Scott BJ, Neidt EM, Kovar DR","authors_abbrev":"Scott BJ et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-08-26","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17531816","title":"Functional separation of the requirements for establishment and maintenance of centromeric heterochromatin.","citation":"Mol Cell 2007 May 25;26(4):593-602","abstract":"The establishment and maintenance of centromeric heterochromatin in fission yeast require the RITS complex. Comprised of centromeric siRNAs, the chromodomain protein Chp1, Argonaute (Ago1), and Tas3, RITS couples the cellular RNAi pathway with assembly of constitutive heterochromatin. However, the mechanisms governing RITS-dependent establishment versus maintenance of centromeric heterochromatin remain unresolved. Here, we report that a mutant Tas3 protein that cannot bind Ago1 supports the maintenance of centromeric heterochromatin but cannot mediate efficient de novo establishment from cells transiently depleted for the histone H3 lysine 9 methyltransferase Clr4. In contrast, centromeric heterochromatin efficiently assembles in mutant cells transiently depleted for dicer. This mutant therefore allows ordering of the events leading to establishment of centromeric heterochromatin and places lysine 9 methylation of histone H3 upstream of dicer function.","authors":"Partridge JF, DeBeauchamp JL, Kosinski AM, Ulrich DL, Hadler MJ, Noffsinger VJ","authors_abbrev":"Partridge JF et al.","pubmed_publication_date":"25 May 2007","pubmed_entrez_date":"2007-05-29","publication_year":"2007","canto_session_key":"39df96dcfbe5d5ee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-05 13:51:42","canto_approved_date":"2026-03-11 16:17:49","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-03-05 13:51:28","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC83.03c","SPCC736.11","SPAC18G6.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-03-05"},{"uniquename":"PMID:10779336","title":"Fission yeast Eso1p is required for establishing sister chromatid cohesion during S phase.","citation":"Mol Cell Biol 2000 May;20(10):3459-69","abstract":"Sister chromatid cohesion is essential for cell viability. We have isolated a novel temperature-sensitive lethal mutant named eso1-H17 that displays spindle assembly checkpoint-dependent mitotic delay and abnormal chromosome segregation. At the permissive temperature, the eso1-H17 mutant shows mild sensitivity to UV irradiation and DNA-damaging chemicals. At the nonpermissive temperature, the mutant is arrested in M phase with a viability loss due to a failure to establish sister chromatid cohesion during S phase. The lethal M-phase arrest phenotype, however, is suppressed by inactivation of a spindle checkpoint. The eso1(+) gene is not essential for the onset and progression of DNA replication but has remarkable genetic interactions with those genes regulating the G(1)-S transition and DNA replication. The N-terminal two-thirds of Eso1p is highly homologous to DNA polymerase eta of budding yeast and humans, and the C-terminal one-third is homologous to budding yeast Eco1p (also called Ctf7p), which is required for the establishment of sister chromatid cohesion. Deletion analysis and determination of the mutation site reveal that the function of the Eco1p/Ctf7p-homologous domain is necessary and sufficient for sister chromatid cohesion. On the other hand, deletion of the DNA polymerase eta domain in Eso1p increases sensitivity to UV irradiation. These results indicate that Eso1p plays a dual role during DNA replication. The C-terminal region acts to establish sister chromatid cohesion, and the N-terminal region presumably catalyzes translesion DNA synthesis when template DNA contains lesions that block regular DNA replication.","authors":"Tanaka K, Yonekawa T, Kawasaki Y, Kai M, Furuya K, Iwasaki M, Murakami H, Yanagida M, Okayama H","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"May 2000","pubmed_entrez_date":"2000-04-25","publication_year":"2000","canto_session_key":"4fa485c82556641b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-02 14:41:15","canto_approved_date":"2022-09-21 11:14:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-02 14:40:47","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPBC25H2.13c","SPAPB2B4.03","SPBC16D10.09","SPBC16A3.11","SPAC22F3.09c","SPBC20F10.06","SPBC336.12c","SPBC2D10.06","SPAC31A2.05c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2018-03-02"},{"uniquename":"PMID:22139922","title":"Non-coding telomeric and subtelomeric transcripts are differentially regulated by telomeric and heterochromatin assembly factors in fission yeast.","citation":"Nucleic Acids Res 2012 Apr;40(7):2956-63","abstract":"While telomere repeat-containing non-coding RNA has been identified in a variety of eukaryotes, its biological role is not yet clear. We have identified telomeric transcripts in fission yeast, a model system that combines precise genetic manipulability with telomeres remarkably similar to those of human. Like human and budding yeast, fission yeast harbours a population of telomeric RNA molecules containing G-rich telomeric repeats transcribed from the subtelomere to the telomere. In addition, we detect substantial levels of C-rich telomeric RNA whose appearance is independent of the RNA-dependent RNA polymerase, suggesting that the telomere repeats themselves serve as promoter sites; multiple distinct subtelomeric RNAs are also present. The regulation of these transcripts depends on the telomere-associated proteins Taz1 and Rap1, as deletion of taz1(+) or rap1(+) leads to increased levels of both telomere repeat-containing and subtelomeric transcripts. In contrast, loss of the heterochromatin proteins Swi6 or Clr4 or the telomerase regulator Rif1 results in elevated subtelomeric RNA levels while telomere-repeat containing transcript levels remain repressed. Coupled with the large body of knowledge surrounding the functions of telomeric and heterochromatin factors in fission yeast, these in vivo analyses suggest testable models for the roles of TERRA in telomere function.","doi":"10.1093/nar/gkr1155","authors":"Greenwood J, Cooper JP","authors_abbrev":"Greenwood J et al.","pubmed_publication_date":"Apr 2012","pubmed_entrez_date":"2011-12-06","publication_year":"2012","canto_session_key":"f32a8924e1bed6cb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8505375","title":"Mycelial and syncytial growth in Schizosaccharomyces pombe induced by novel septation mutations.","citation":"J Cell Sci 1993 Feb;104 ( Pt 2):485-93","abstract":"Mutation in the gene sep1+ of the unicellular fission yeast Schizosaccharomyces pombe impairs cell separation after cytokinesis and confers a branching mycelial morphology. The mutant is not defective in cell wall beta-glucanase activity but shows increased sensitivity to Ca2+ and Mg2+, and increased resistance to the microtubule inhibitor benomyl. The mycelial growth of sep1-1 provides a convenient method for the examination of the polar growth pattern and for pedigree analysis as demonstrated by the segregation of mating types in the homothallic microhyphae. sep1 is closely linked to ade1 (0.94 cM) on the right arm of chromosome II. The ts mutation spl1-1 confers a bent cell shape and causes aberrant septum formation at the restrictive temperature. sep1+ and spl1+ perform closely related functions as their mutant alleles interact with each other and with another septation mutant cdc4-8. These functions may overlap with certain cytoskeletal processes and with the determination of cell polarity because the triple mutant forms huge multinucleate syncytia with promiscuous branching and rare septum formation.","authors":"Sipiczki M, Grallert B, Miklos I","authors_abbrev":"Sipiczki M et al.","pubmed_publication_date":"Feb 1993","pubmed_entrez_date":"1993-02-01","publication_year":"1993","canto_session_key":"c20bae5b2612d30c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-03-05 19:34:56","canto_approved_date":"2019-03-05 19:34:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-03-05 19:34:49","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPATRNAPRO.02","SPAP8A3.08","SPAC6F6.08c","SPBC4C3.12"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-03-05"},{"uniquename":"PMID:12569122","title":"Early-replicating heterochromatin.","citation":"Genes Dev 2003 Feb 01;17(3):330-5","abstract":"Euchromatin, which has an open structure and is frequently transcribed, tends to replicate in early S phase. Heterochromatin, which is more condensed and rarely transcribed, usually replicates in late S phase. Here, we report significant deviation from this correlation in the fission yeast, Schizosaccharomyces pombe. We found that heterochromatic centromeres and silent mating-type cassettes replicate in early S phase. Only heterochromatic telomeres replicate in late S phase. Research in other laboratories has shown that occasionally other organisms also replicate some of their heterochromatin in early S phase. Thus, late replication is not an obligatory feature of heterochromatin.","authors":"Kim SM, Dubey DD, Huberman JA","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"01 Feb 2003","pubmed_entrez_date":"2003-02-06","publication_year":"2003","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15449714","title":"[Molecular basis of kinetochore structure and kinetochore-spindle interaction].","citation":"Tanpakushitsu Kakusan Koso 2004 Sep;49(12):1982-9","abstract":"","authors":"Saitoh S, Takahashi K","authors_abbrev":"Saitoh S et al.","pubmed_publication_date":"Sep 2004","pubmed_entrez_date":"2004-09-29","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12374752","title":"Pre-spliceosome formation in S.pombe requires a stable complex of SF1-U2AF(59)-U2AF(23).","citation":"EMBO J 2002 Oct 15;21(20):5516-26","abstract":"We have initiated a biochemical analysis of splicing complexes in extracts from the fission yeast Schizosaccharomyces pombe. Extracts of S.pombe contain high levels of the spliceosome-like U2/5/6 tri-snRNP, which dissociates into mono-snRNPs in the presence of ATP, and supports binding of U2 snRNP to the 3' end of introns, yielding a weak ATP-independent E complex and the stable ATP-dependent complex A. The requirements for S.pombe complex A formation (pre-mRNA sequence elements, protein splicing factors, SF1/BBP and both subunits of U2AF) are analogous to those of mammalian complex A. The S.pombe SF1/BBP, U2AF(59) and U2AF(23) are tightly associated in a novel complex that is required for complex A formation. This pre-formed SF1- U2AF(59)-U2AF(23) complex may represent a streamlined mechanism for recognition of the branch site, pyrimidine tract and 3' splice site at the 3' end of introns.","authors":"Huang T, Vilardell J, Query CC","authors_abbrev":"Huang T et al.","pubmed_publication_date":"15 Oct 2002","pubmed_entrez_date":"2002-10-11","publication_year":"2002","canto_session_key":"cec0408e1de768d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-30 10:54:29","canto_approved_date":"2021-11-01 09:21:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-22 10:23:24","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.02","SPSNRNA.05","SPBC146.07","SPAP8A3.06","SPCC962.06c","SPSNRNA.06"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-09-30"},{"uniquename":"EMBL:AU011416","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6372869","title":"Dielectrophoretic properties of yeast cells dividing by budding and by transversal fission.","citation":"Biochim Biophys Acta 1984 Jun 19;804(2):221-9","abstract":"The dielectrophoretic behaviour of yeast cells dividing by budding or by transversal fission was analyzed. The results obtained show that the dielectrophoretic yield is a linear function of alternating voltage, cell concentration and the square root of the time of collection in all the species assayed. Dependence of the rate of collection on the frequency of the voltage applied (between 0.2 and 5 MHz) was also found. This behaviour is similar in the three microorganisms studied. The scale factor correlating the frequency spectrum for Saccharomyces cerevisiae and Saccharomycopsis lipolytica is proportional to cell size. However, these results can not be extended to Schizosaccharomyces pombe. A relationship between the dielectrophoretic yield and the age of the culture and the consumption of glucose has been established for the three yeast strains. Dielectrophoresis also permits the differentiation between viable and non-viable cells.","authors":"Iglesias FJ, Lopez MC, Santamaría C, Domínguez A","authors_abbrev":"Iglesias FJ et al.","pubmed_publication_date":"19 Jun 1984","pubmed_entrez_date":"1984-06-19","publication_year":"1984","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19875745","title":"Fission yeast and other yeasts as emergent models to unravel cellular aging in eukaryotes.","citation":"J Gerontol A Biol Sci Med Sci 2010 Jan;65(1):1-8","abstract":"In the past years, simple organisms such as yeasts and worms have contributed a great deal to aging research. Studies pioneered in Saccharomyces cerevisiae were useful to elucidate a significant number of molecular mechanisms underlying cellular aging and to discover novel longevity genes. Importantly, these genes proved many times to be conserved in multicellular eukaryotes. Consequently, such discovery approaches are being extended to other yeast models, such as Schizosaccharomyces pombe, Candida albicans, Kluyveromyces lactis, and Cryptococcus neoformans. In fission yeast, researchers have found links between asymmetrical cell division and nutrient signaling pathways with aging. In this review, we discuss the state of knowledge on the mechanisms controlling both replicative and chronological aging in S pombe and the other emergent yeast models.","doi":"10.1093/gerona/glp152","authors":"Roux AE, Chartrand P, Ferbeyre G, Rokeach LA","authors_abbrev":"Roux AE et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-10-31","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12869548","title":"Identification of dominant negative mutants of Rheb GTPase and their use to implicate the involvement of human Rheb in the activation of p70S6K.","citation":"J Biol Chem 2003 Oct 10;278(41):39921-30","abstract":"Rheb GTPases represent a unique family of the Ras superfamily of G-proteins. Studies on Rheb in Schizosaccharomyces pombe and Drosophila have shown that this small GTPase is essential and is involved in cell growth and cell cycle progression. The Drosophila studies also raised the possibility that Rheb is involved in the TOR/S6K signaling pathway. In this paper, we first report identification of dominant negative mutants of S. pombe Rheb (SpRheb). Screens of a randomly mutagenized SpRheb library yielded a mutant, SpRhebD60V, whose expression in S. pombe results in growth inhibition, G1 arrest, and induction of fnx1+, a gene whose expression is induced by the disruption of Rheb. Alteration of the Asp-60 residue to all possible amino acids by site-directed mutagenesis led to the identification of two particularly strong dominant negative mutants, D60I and D60K. Characterization of these dominant negative mutant proteins revealed that D60V and D60I exhibit preferential binding of GDP, while D60K lost the ability to bind both GTP and GDP. A possible use of the dominant negative mutants in the study of mammalian Rheb was explored by introducing dominant negative mutations into human Rheb. We show that transient expression of the wild type Rheb1 or Rheb2 causes activation of p70S6K, while expression of Rheb1D60K mutant results in inhibition of basal level activity of p70S6K. In addition, Rheb1D60K and Rheb1D60V mutants blocked nutrient- or serum-induced activation of p70S6K. This provides critical evidence that Rheb plays a role in the mTOR/S6K pathway in mammalian cells.","authors":"Tabancay AP, Gau CL, Machado IM, Uhlmann EJ, Gutmann DH, Guo L, Tamanoi F","authors_abbrev":"Tabancay AP et al.","pubmed_publication_date":"10 Oct 2003","pubmed_entrez_date":"2003-07-19","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.16c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:27871365","title":"Mechanism and Regulation of DNA-Protein Crosslink Repair by the DNA-Dependent Metalloprotease SPRTN.","citation":"Mol Cell 2016 Nov 17;64(4):688-703","abstract":"Covalent DNA-protein crosslinks (DPCs) are toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription. Little was known about DPC-specific repair mechanisms until the recent identification of a DPC-processing protease in yeast. The existence of a DPC protease in higher eukaryotes is inferred from data in Xenopus laevis egg extracts, but its identity remains elusive. Here we identify the metalloprotease SPRTN as the DPC protease acting in metazoans. Loss of SPRTN results in failure to repair DPCs and hypersensitivity to DPC-inducing agents. SPRTN accomplishes DPC processing through a unique DNA-induced protease activity, which is controlled by several sophisticated regulatory mechanisms. Cellular, biochemical, and structural studies define a DNA switch triggering its protease activity, a ubiquitin switch controlling SPRTN chromatin accessibility, and regulatory autocatalytic cleavage. Our data also provide a molecular explanation on how SPRTN deficiency causes the premature aging and cancer predisposition disorder Ruijs-Aalfs syndrome.","doi":"10.1016/j.molcel.2016.09.031","authors":"Stingele J, Bellelli R, Alte F, Hewitt G, Sarek G, Maslen SL, Tsutakawa SE, Borg A, Kjær S, Tainer JA, Skehel JM, Groll M, Boulton SJ","authors_abbrev":"Stingele J et al.","pubmed_publication_date":"17 Nov 2016","pubmed_entrez_date":"2016-11-23","publication_year":"2016","canto_session_key":"d43ed7beb6c57947","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-05-28 23:40:52","canto_approved_date":"2019-05-29 07:41:36","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-05-28 23:40:41","canto_added_date":"2017-09-03 00:15:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC521.02","SPCC1442.07c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-05-28","pdb_entries":[{"pdb_id":"5jig","gene_chains":[{"gene_uniquename":"SPCC1442.07c","chain":"A","position":"106-232"}],"title":"Crytsal structure of Wss1 from S. pombe","entry_authors":"Groll M,Stingele J,Boulton S","entry_authors_abbrev":"Groll M et al.","reference_uniquename":"PMID:27871365","experimental_method":"X-ray","resolution":"1.0"},{"pdb_id":"5ln5","gene_chains":[{"gene_uniquename":"SPCC1442.07c","chain":"A/B","position":"107-233"}],"title":"Crystal structure of the Wss1 E203Q mutant from S. pombe","entry_authors":"Groll M,Stingele J,Boulton SJ","entry_authors_abbrev":"Groll M et al.","reference_uniquename":"PMID:27871365","experimental_method":"X-ray","resolution":"1.75"}]},{"uniquename":"PMID:28522285","title":"Production of 3-hydroxypropionic acid via the malonyl-CoA pathway using recombinant fission yeast strains.","citation":"J Biosci Bioeng 2017 Oct;124(4):392-399","abstract":"3-Hydroxypropionic acid (3-HP) can be converted into derivatives such as acrylic acid, a source for producing super absorbent polymers. Although Escherichia coli has often been used for 3-HP production, it exhibits low tolerance to 3-HP. To circumvent this problem, we selected the fission yeast Schizosaccharomyces pombe as this microorganism has higher tolerance to 3-HP than E. coli. Therefore, we constructed S. pombe transformants overexpressing two genes, one encoding the S. pombe acetyl-CoA carboxylase (Cut6p) and the other encoding the malonyl-CoA reductase derived from Chloroflexus aurantiacus (CaMCR). To prevent the degradation of these expressed proteins, we employed an S. pombe protease-deficient strain. Moreover, to increase the cytosolic concentration of acetyl-CoA, we supplemented acetate to the medium, which improved 3-HP production. To further produce 3-HP by overexpressing Cut6p and CaMCR, we exploited the highly expressing S. pombe hsp9 promoter. Finally, culturing in high-density reached 3-HP production to 7.6 g/L at 31 h.","doi":"10.1016/j.jbiosc.2017.04.015","authors":"Suyama A, Higuchi Y, Urushihara M, Maeda Y, Takegawa K","authors_abbrev":"Suyama A et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-05-20","publication_year":"2017","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2017-05-21 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007862","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11129048","title":"The Prr1 response regulator is essential for transcription of ste11+ and for sexual development in fission yeast.","citation":"Mol Gen Genet 2000 Nov;264(4):441-51","abstract":"Schizosaccharomyces pombe expresses a putative transcription factor, named Prr1, which is intriguing in the sense that it contains a bacterial type of phospho-accepting receiver domain, preceded by a mammalian heat shock factor (HSF2)-like DNA-binding domain. The receiver domain is most probably involved in an as yet unidentified histidine-to-aspartate (His-to-Asp) phosphorelay pathway in S. pombe. In this study, the structure, function, and cellular localization of Prr1 were assessed in the context of oxidative stress and His-to-Asp phosphorelay. As the most intriguing result of this study, we found that Prr1 is essential not only for the expression of genes induced by oxidative stress (e.g., ctt1+ and trr1+), but also for the expression of ste11+, which in turn is responsible for the expression of a variety of genes required for sexual development. Accordingly, Prr1-deficient cells are not only hypersensitive to oxidative stress, but also severely defective in conjugation and/or spore formation. These results suggested that the transcription factor Prr1 plays a pivotal role in an as yet unknown signal transduction pathway that is implicated in sexual differentiation. These findings are discussed with special reference to the well-characterized transcription factors Pap1 and Atf1 of S. pombe.","authors":"Ohmiya R, Yamada H, Kato C, Aiba H, Mizuno T","authors_abbrev":"Ohmiya R et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-12-29","publication_year":"2000","canto_session_key":"8e27bf8723065210","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-14 13:34:16","canto_approved_date":"2026-04-08 11:04:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-15 01:21:31","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC8C9.14","SPBC29B5.01","SPBC32C12.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-09-14"},{"uniquename":"PMID:38938172","title":"Modeling the Evolution of S. pombe Populations with Multiple Killer Meiotic Drivers.","citation":"G3 (Bethesda) 2024 Jun 28;","abstract":"Meiotic drivers are selfish genetic loci that can be transmitted to more than half of the viable gametes produced by a heterozygote. This biased transmission gives meiotic drivers an evolutionary advantage that can allow them to spread over generations until all members of a population carry the driver. This evolutionary power can also be exploited to modify natural populations using synthetic drivers known as 'gene drives.' Recently, it has become clear that natural drivers can spread within genomes to birth multicopy gene families. To understand intragenomic spread of drivers, we model the evolution of two or more distinct meiotic drivers in a population. We employ the wtf killer meiotic drivers from Schizosaccharomyces pombe, which are multicopy in all sequenced isolates, as models. We find that a duplicate wtf driver identical to the parent gene can spread in a population unless, or until, the original driver is fixed. When the duplicate driver diverges to be distinct from the parent gene, we find that both drivers spread to fixation under most conditions, but both drivers can be lost under some conditions. Finally, we show that stronger drivers make weaker drivers go extinct in most, but not all, polymorphic populations with absolutely linked drivers. These results reveal the strong potential for natural meiotic drive loci to duplicate and diverge within genomes. Our findings also highlight duplication potential as a factor to consider in the design of synthetic gene drives.","doi":"10.1093/g3journal/jkae142","authors":"López Hernández JF, Rubinstein BY, Unckless RL, Zanders SE","authors_abbrev":"López Hernández JF et al.","pubmed_publication_date":"28 Jun 2024","pubmed_entrez_date":"2024-06-28","publication_year":"2024","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2024-06-28 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8167016","title":"The yeast actin cytoskeleton.","citation":"Curr Opin Cell Biol 1994 Feb;6(1):110-9","abstract":"Budding and fission yeast present significant advantages for studies of the actin cytoskeleton. The application of classical and molecular genetic techniques provides a facile route for the analysis of structure/function relationships, for the isolation of novel proteins involved in cytoskeletal function, and for deciphering the signals that regulate actin assembly in vivo. This review focuses on the budding yeast Saccharomyces cerevisiae and also identifies some recent advances from studies on the fission yeast Schizosaccharomyces pombe, for which studies on the actin cytoskeleton are still in their infancy.","authors":"Welch MD, Holtzman DA, Drubin DG","authors_abbrev":"Welch MD et al.","pubmed_publication_date":"Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11369865","title":"Overcoming the problems associated with poor spectra quality of the protein kinase Byr2 using residual dipolar couplings.","citation":"Protein Sci 2001 Jun;10(6):1260-3","abstract":"For the Ras-binding domain of the protein kinase Byr2, only a limited number of NOE contacts could be initially assigned unambiguously, as the quality of the NOESY spectra was too poor. However, the use of residual (1)H-(15)N dipolar couplings in the beginning of the structure determination process allows to overcome this problem. We used a three-step recipe for this procedure. A previously unknown structure could be calculated reasonably well with only a limited number of unambiguously assigned NOE contacts.","authors":"Gronwald W, Brunner E, Huber F, Wenzler M, Herrmann C, Kalbitzer HR","authors_abbrev":"Gronwald W et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-05-23","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35886027","title":"Impact of Chromosomal Context on Origin Selection and the Replication Program.","citation":"Genes (Basel) 2022 Jul 14;13(7)","abstract":"Eukaryotic DNA replication is regulated by conserved mechanisms that bring about a spatial and temporal organization in which distinct genomic domains are copied at characteristic times during S phase. Although this replication program has been closely linked with genome architecture, we still do not understand key aspects of how chromosomal context modulates the activity of replication origins. To address this question, we have exploited models that combine engineered genomic rearrangements with the unique replication programs of post-quiescence and pre-meiotic S phases. Our results demonstrate that large-scale inversions surprisingly do not affect cell proliferation and meiotic progression, despite inducing a restructuring of replication domains on each rearranged chromosome. Remarkably, these alterations in the organization of DNA replication are entirely due to changes in the positions of existing origins along the chromosome, as their efficiencies remain virtually unaffected genome wide. However, we identified striking alterations in origin firing proximal to the fusion points of each inversion, suggesting that the immediate chromosomal neighborhood of an origin is a crucial determinant of its activity. Interestingly, the impact of genome reorganization on replication initiation is highly comparable in the post-quiescent and pre-meiotic S phases, despite the differences in DNA metabolism in these two physiological states. Our findings therefore shed new light on how origin selection and the replication program are governed by chromosomal architecture.","doi":"10.3390/genes13071244","authors":"Lanteri L, Perrot A, Schausi-Tiffoche D, Wu PJ","authors_abbrev":"Lanteri L et al.","pubmed_publication_date":"14 Jul 2022","pubmed_entrez_date":"2022-07-27","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-07-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37746062","title":"Polarity kinases that phosphorylate F-BAR protein Cdc15 have unique localization patterns during cytokinesis and contributions to preventing tip septation in  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2023;2023","abstract":"The  Schizosaccharomyces pombe  F-BAR protein, Cdc15, facilitates the linkage between the cytokinetic ring and the plasma membrane. Cdc15 is phosphorylated on many sites by four polarity kinases and this antagonizes membrane interaction. Dephosphorylation of Cdc15 during mitosis induces its phase separation, allowing oligomerization, membrane association, and protein partner binding. Here, using live cell imaging we examined whether spatial separation of Cdc15 from its four identified kinases potentially explains their diverse effects on tip septation and the mitotic Cdc15 phosphorylation state. We identified a correlation between kinase localization and their ability to antagonize Cdc15 cytokinetic ring and membrane localization.","doi":"10.17912/micropub.biology.000965","authors":"Igarashi MG, Bhattacharjee R, Willet AH, Gould KL","authors_abbrev":"Igarashi MG et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-09-25","publication_year":"2023","canto_session_key":"8cb6518bf2bf38dc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2023-09-28 13:05:03","canto_approved_date":"2023-09-28 13:05:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-09-27 17:37:39","canto_added_date":"2023-09-25 23:25:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":10,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.14c","SPCC4B3.15","SPAC2F7.03c","SPAC20G8.05c","SPBC1604.14c","SPBC4F6.06"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2023-09-28"},{"uniquename":"PMID:3299000","title":"Characterisation of an autonomously replicating sequence from the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1987 Apr;207(1):161-4","abstract":"A DNA sequence has been isolated from Schizosaccharomyces pombe which promotes high frequency transformation of plasmids in the same organism. It is closely linked to the DNA ligase gene CDC17 and has therefore been named ARS17 although in structure it differs substantially from ARS elements in Saccharomyces cerevisiae. ARS17 spans some 1.8 kb of DNA and deletion of any part of this region affects activity. Moreover, there does not appear to be any short sequence which is, by itself, sufficient for high frequency transformation. ARS17 lies between and partly overlaps two divergently transcribed genes and it is extremely AT rich. It lacks the consensus sequence found in S. cerevisiae ARSs and it has no ARS activity in S. cerevisiae.","authors":"Johnston LH, Barker DG","authors_abbrev":"Johnston LH et al.","pubmed_publication_date":"Apr 1987","pubmed_entrez_date":"1987-04-01","publication_year":"1987","canto_session_key":"ff73963750a4b757","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-02-01 23:49:41","canto_approved_date":"2019-02-01 23:49:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-01 23:49:33","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-02-01"},{"uniquename":"PMID:15913924","title":"RNA maturation in mitochondria of S. cerevisiae and S. pombe.","citation":"Gene 2005 Jul 18;354:80-5","abstract":"Although the gene content is rather conserved, the genomes in mitochondria of yeasts vary dramatically in size [Clark-Walker, G.D., Evans, R.J., Hoeben, P., McArthur, C.R., 1985. Basis of diversity in yeast mitochondrial DNAs. In: Quagliariello, E.C., Palmieri, F., Saccone, C., Kroon, A.M. (Eds.). Achievements and Perspectives of Mitochondrial Research 2. Science Publishers, Amsterdam, pp. 71-78] and in the number of transcription units. Since the fidelity and processivity of the mitochondrial single-subunit phage-like RNA polymerase present in yeast mitochondria are certainly limited, one might speculate that the density of transcription initiation sites on the mitochondrial genomes is one of the factors influencing the genome size. In an effort to find common features among the apparent idiosyncrasies of Saccharomyces cerevisiae (with its extremely large mtDNA) and Schizosaccharomyces pombe (with its extremely small mitochondrial genome), the aim of this review is to compare recent data about transcription and generation of 5' and 3' ends of mature RNA transcripts in S. cerevisiae and in S. pombe. Both organisms are two attractive model systems enabling investigation of various aspects of mitochondrial genetics.","authors":"Schäfer B","authors_abbrev":"Schäfer B","pubmed_publication_date":"18 Jul 2005","pubmed_entrez_date":"2005-05-26","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1974520","title":"Human chorionic gonadotropin alpha and human cytomegalovirus promoters are extremely active in the fission yeast Schizosaccharomyces pombe.","citation":"FEBS Lett 1990 Jul 30;268(1):217-21","abstract":"We have investigated the transcriptional activity of human cytomegalovirus, herpes thymidine kinase, human chorionic gonadotropin alpha, somatostatin, immunoglobulin kappa chain, alpha crystallin, albumin and interferon-beta promoters in the fission yeast Schizosaccharomyces pombe. Among these, the human cytomegalovirus, human chorionic gonadotropin alpha, and somatostatin promoters were found to be very active, approximately 11-, 9-, and 0.9-fold as active as the SV40 early promoter, respectively. The remainder of the promoters studied were weak, having only 10-20% of the SV40 promoter activity. Primer extension analysis showed that the strong promoters initiated transcription in S. pombe at the same sites as in mammalian cells, indicating the high similarity between both transcriptional systems.","authors":"Toyama R, Okayama H","authors_abbrev":"Toyama R et al.","pubmed_publication_date":"30 Jul 1990","pubmed_entrez_date":"1990-07-30","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9090050","title":"Properties and heterologous expression of the glucose transporter GHT1 from Schizosaccharomyces pombe.","citation":"Yeast 1997 Mar 15;13(3):215-24","abstract":"Genomic DNA of the Schizosaccharomyces pombe glucose transporter, GHT1, was obtained by complementation of the glucose transport deficient Sz. pombe strain YGS-5. Here we describe the GHT1 gene that encodes a protein of 565 amino acids with a corresponding molecular mass of 62.5 kDa. This eukaryotic glucose transporter contains 12 putative transmembrane segments and is homologous to the HXT multigene family of S. cerevisiae with several amino acid motifs of this sugar transporter family. It is also homologous to other sugar carriers from human, mouse and Escherichia coli. The function of the Ght1 protein as a glucose transporter was proved both by homologous and heterologous expression in the Sz. pombe mutant YGS-5 and in the S. cerevisiae hxt mutant RE700A, respectively. Both transformed yeast strains transported D-glucose with substrate specificity similar to that in Sz. pombe wild-type cells. Moreover, the cells of the two transformed yeast strains accumulated 2-deoxy-D-glucose, a non-metabolizable D-glucose analogue, with an efficiency similar to Sz. pombe wild-type cells. The ability of the S. cerevisiae mutant RE700A to accumulate 2DG in an delta mu H+ dependent manner after transformation with GHT1 provides evidence that the Sz. pombe transporter catalyses an energy-dependent uptake of glucose.","authors":"Lichtenberg-Fraté H, Näschen T, Heiland S, Höfer M","authors_abbrev":"Lichtenberg-Fraté H et al.","pubmed_publication_date":"15 Mar 1997","pubmed_entrez_date":"1997-03-15","publication_year":"1997","canto_session_key":"39a5a6a1083e818a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-17 15:31:25","canto_approved_date":"2025-09-03 13:13:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-27 18:07:21","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1235.14","SPCC1235.13","SPCC548.07c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2014-11-17"},{"uniquename":"PMID:16622069","title":"Vacuolar protein sorting receptor in Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 2006 May;152(Pt 5):1523-1532","abstract":"The mechanism by which soluble proteins, such as carboxypeptidase Y, reach the vacuole in Saccharomyces cerevisiae is very similar to the mechanism of lysosomal protein sorting in mammalian cells. Vps10p is a receptor for transport of soluble vacuolar proteins in S. cerevisiae. vps10(+), a gene encoding a homologue of S. cerevisiae PEP1/VPS10, has been identified and deleted from the fission yeast Schizosaccharomyces pombe. Deletion of the vps10(+) gene resulted in missorting and secretion of Sch. pombe vacuolar carboxypeptidase Cpy1p, indicating that it is required for targeting Cpy1p to the vacuole. Sch. pombe Vps10p (SpVps10p) is a type I transmembrane protein and its C-terminal cytoplasmic tail domain is essential for Cpy1p transport to the vacuole. Cells expressing green fluorescent protein-tagged SpVps10p produced a punctate pattern of fluorescence, indicating that SpVps10p was largely localized in the Golgi compartment. In addition, Sch. pombe vps26(+), vps29(+) and vps35(+), encoding homologues of the S. cerevisiae retromer components VPS26, VPS29 and VPS35, were identified and deleted. Fluorescence microscopy demonstrated that SpVps10p mislocalized to the vacuolar membrane in these mutants. These results indicate that the vps26(+), vps29(+) and vps35(+) gene products are required for retrograde transport of SpVps10p from the prevacuolar compartment back to the Golgi in Sch. pombe cells.","doi":"10.1099/mic.0.28627-0","authors":"Iwaki T, Hosomi A, Tokudomi S, Kusunoki Y, Fujita Y, Giga-Hama Y, Tanaka N, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"May 2006","pubmed_entrez_date":"2006-04-20","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16C6.06","SPCC777.13","SPCPJ732.01","SPAC15E1.06","SPAC4G9.13c","SPAPJ696.01c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:15956211","title":"A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway.","citation":"Proc Natl Acad Sci U S A 2005 Jun 21;102(25):8875-80","abstract":"The Schizosaccharomyces pombe transcription factor Pap1 regulates antioxidant-gene transcription in response to H2O2. Pap1 activation occurs only at low, but not elevated, H2O2 concentrations that instead strongly trigger the mitogen-activated protein kinase Sty1 pathway. Here, we identify the peroxiredoxin Tpx1 as the upstream activator of Pap1. We show that, at low H2O2 concentrations, this oxidant scavenger can transfer a redox signal to Pap1, whereas higher concentrations of the oxidant inhibit the Tpx1-Pap1 redox relay through the temporal inactivation of Tpx1 by oxidation of its catalytic cysteine to a sulfinic acid. This cysteine modification can be reversed by the sulfiredoxin Srx1, its expression in response to high doses of H2O2 strictly depending on active Sty1. Thus, Tpx1 oxidation to the cysteine-sulfinic acid and its reversion by Srx1 constitutes a previously uncharacterized redox switch in H2O2 signaling, restricting Pap1 activation within a narrow range of H2O2 concentrations.","authors":"Vivancos AP, Castillo EA, Biteau B, Nicot C, Ayté J, Toledano MB, Hidalgo E","authors_abbrev":"Vivancos AP et al.","pubmed_publication_date":"21 Jun 2005","pubmed_entrez_date":"2005-06-16","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:238577","title":"Nonspecific acid phosphatase from Schizosaccharomyces pombe. Purification and physical chemical properties.","citation":"Biochemistry 1975 Jul;14(13):2847-52","abstract":"Repressible nonspecific acid phosphatase from Schizosaccharomyces pombe was purified to apparent homogeneity, as ascertained from ultracentrifugal, electrophoretic, and chromatographic data. The native protein has a molecular weight of 383,000 as determined by sucrose density gradient centrifugation and 381,000 as determined by gel filtration. The native protein can be dissociated in the presence of 8 M urea-1% sodium dodecyl sulfate into sub-units possessing an approximate molecular weight of 104,000. Neutral sugars account for about 66% of the total molecular weight and contribute to the high solubility and some of the other physical properties of this enzyme. Purified enzyme preparations have a Km for 4-nitrophenyl phosphate of 0.17 mM and a broad substrate specificity, but do not show diesterase activity. Phosphate and sulfate are competitive inhibitors. The enzyme is inactivated at neutral and alkaline pH and at relatively low temperatures. Mannose and galactose was found as the main components of the carbohydrate moiety; glucosamine was present in lower amounts. The amino acid analysis revealed a high content of aspartate, threonine, and serine; no sulfhydryl group could be detected. Pi is released in stoichiometric amount (1 mol per enzyme monomer) on protein digestion.","authors":"Dibenedetto G, Cozzani I","authors_abbrev":"Dibenedetto G et al.","pubmed_publication_date":"Jul 1975","pubmed_entrez_date":"1975-07-01","publication_year":"1975","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22279046","title":"Rif1 is a global regulator of timing of replication origin firing in fission yeast.","citation":"Genes Dev 2012 Jan 15;26(2):137-50","abstract":"One of the long-standing questions in eukaryotic DNA replication is the mechanisms that determine where and when a particular segment of the genome is replicated. Cdc7/Hsk1 is a conserved kinase required for initiation of DNA replication and may affect the site selection and timing of origin firing. We identified rif1Δ, a null mutant of rif1(+), a conserved telomere-binding factor, as an efficient bypass mutant of fission yeast hsk1. Extensive deregulation of dormant origins over a wide range of the chromosomes occurs in rif1Δ in the presence or absence of hydroxyurea (HU). At the same time, many early-firing, efficient origins are suppressed or delayed in firing timing in rif1Δ. Rif1 binds not only to telomeres, but also to many specific locations on the arm segments that only partially overlap with the prereplicative complex assembly sites, although Rif1 tends to bind in the vicinity of the late/dormant origins activated in rif1Δ. The binding to the arm segments occurs through M to G1 phase in a manner independent of Taz1 and appears to be essential for the replication timing program during the normal cell cycle. Our data demonstrate that Rif1 is a critical determinant of the origin activation program on the fission yeast chromosomes.","doi":"10.1101/gad.178491.111","authors":"Hayano M, Kanoh Y, Matsumoto S, Renard-Guillet C, Shirahige K, Masai H","authors_abbrev":"Hayano M et al.","pubmed_publication_date":"15 Jan 2012","pubmed_entrez_date":"2012-01-27","publication_year":"2012","canto_session_key":"1e2c67b565f85a95","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-01-22 15:32:24","canto_approved_date":"2022-09-29 15:25:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-01-22 15:32:15","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPAC6F6.17","SPAC17D4.02","SPAC16A10.07c","SPBC776.12c","SPAC694.06c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2020-01-22"},{"uniquename":"PMID:31597677","title":"Targeted Forward Genetics: Population-Scale Analyses of Allele Replacements Spanning Thousands of Base Pairs in Fission Yeast.","citation":"G3 (Bethesda) 2019 Dec 03;9(12):4097-4106","abstract":"Precise allele replacement (genome editing), without unwanted changes to the genome, provides a powerful tool to define the functions of DNA elements and encoded factors in their normal biological context. While CRISPR is now used extensively for gene targeting, its utility for precise allele replacement at population scale is limited because: (A) there is a strict requirement for a correctly positioned PAM motif to introduce recombinogenic dsDNA breaks (DSBs); (B) efficient replacements only occur very close to the DSBs; and (C) indels and off-target changes are frequently generated. Here we show, using a saturated mutation library with about 15,000 alleles of the  ade6  gene of  Schizosaccharomyces pombe , that pop-in, pop-out allele replacement circumvents these problems. Two rounds of selection ensure that clones arise by homologous recombination with the target locus. Moreover, the exceptionally high efficiency allows one to carry out the process in bulk, then screen individual clones for phenotypes and genotypes. Alleles were introduced successfully throughout the region targeted, up to 1,956 base pairs from the DSB. About 11% of mutant alleles were hypomorphic, demonstrating utility for analyses of essential genes and genetic elements. This process of \"targeted forward genetics\" can be used to analyze comprehensively, across thousands of base pairs within a specific target region, a variety of allelic changes, such as scanning amino acid substitutions, deletions, and epitope tags. The overall approach and optimized workflow are extensible to other organisms that support gene targeting.","doi":"10.1534/g3.119.400805","authors":"Storey AJ, Wang HP, Protacio RU, Davidson MK, Wahls WP","authors_abbrev":"Storey AJ et al.","pubmed_publication_date":"03 Dec 2019","pubmed_entrez_date":"2019-10-11","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-10-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11139608","title":"Characterization of Schizosaccharomyces pombe RNA triphosphatase.","citation":"Nucleic Acids Res 2001 Jan 15;29(2):387-96","abstract":"RNA triphosphatase catalyzes the first step in mRNA cap formation which entails the cleavage of the beta-gamma phosphoanhydride bond of triphosphate-terminated RNA to yield a diphosphate end that is then capped with GMP by RNA guanylyltransferase. Here we characterize a 303 amino acid RNA triphosphatase (Pct1p) encoded by the fission yeast SCHIZOSACCHAROMYCES: pombe. Pct1p hydrolyzes the gamma phosphate of triphosphate-terminated poly(A) in the presence of magnesium. Pct1p also hydrolyzes ATP to ADP and P(i) in the presence of manganese or cobalt (K(m) = 19 microM ATP; k(cat) = 67 s(-1)). Hydrolysis of 1 mM ATP is inhibited with increasing potency by inorganic phosphate (I(0.5) = 1 mM), pyrophosphate (I(0.5) = 0.4 mM) and tripolyphosphate (I(0.5) = 30 microM). Velocity sedimentation indicates that Pct1p is a homodimer. Pct1p is biochemically and structurally similar to the catalytic domain of Saccharomyces cerevisiae RNA triphosphatase Cet1p. Mechanistic conservation between Pct1p and Cet1p is underscored by a mutational analysis of the putative metal-binding site of Pct1p. Pct1p is functional in vivo in S.cerevisiae in lieu of Cet1p, provided that it is coexpressed with the S.pombe guanylyltransferase. Pct1p and other yeast RNA triphosphatases are completely unrelated, mechanistically and structurally, to the metazoan RNA triphosphatases, suggesting an abrupt evolutionary divergence of the capping apparatus during the transition from fungal to metazoan species.","authors":"Pei Y, Schwer B, Hausmann S, Shuman S","authors_abbrev":"Pei Y et al.","pubmed_publication_date":"15 Jan 2001","pubmed_entrez_date":"2001-01-05","publication_year":"2001","canto_session_key":"c3797f0e720a7e59","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-29 22:15:17","canto_approved_date":"2023-12-08 09:22:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-19 17:06:03","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.04","SPBC2F12.08c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-04-29"},{"uniquename":"PMID:31706948","title":"Decoupling of Rates of Protein Synthesis from Cell Expansion Leads to Supergrowth.","citation":"Cell Syst 2019 Nov 27;9(5):434-445.e6","abstract":"Cell growth is a complex process in which cells synthesize cellular components while they increase in size. It is generally assumed that the rate of biosynthesis must somehow be coordinated with the rate of growth in order to maintain intracellular concentrations. However, little is known about potential feedback mechanisms that could achieve proteome homeostasis or the consequences when this homeostasis is perturbed. Here, we identify conditions in which fission yeast cells are prevented from volume expansion but nevertheless continue to synthesize biomass, leading to general accumulation of proteins and increased cytoplasmic density. Upon removal of these perturbations, this biomass accumulation drove cells to undergo a multi-generational period of \"supergrowth\" wherein rapid volume growth outpaced biosynthesis, returning proteome concentrations back to normal within hours. These findings demonstrate a mechanism for global proteome homeostasis based on modulation of volume growth and dilution.","doi":"10.1016/j.cels.2019.10.001","authors":"Knapp BD, Odermatt P, Rojas ER, Cheng W, He X, Huang KC, Chang F","authors_abbrev":"Knapp BD et al.","pubmed_publication_date":"27 Nov 2019","pubmed_entrez_date":"2019-11-11","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-11-12 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20516199","title":"Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms.","citation":"Genes Dev 2010 Jun 01;24(11):1145-59","abstract":"The correct levels of deoxyribonucleotide triphosphates and their relative abundance are important to maintain genomic integrity. Ribonucleotide reductase (RNR) regulation is complex and multifaceted. RNR is regulated allosterically by two nucleotide-binding sites, by transcriptional control, and by small inhibitory proteins that associate with the R1 catalytic subunit. In addition, the subcellular localization of the R2 subunit is regulated through the cell cycle and in response to DNA damage. We show that the fission yeast small RNR inhibitor Spd1 is intrinsically disordered and regulates R2 nuclear import, as predicted by its relationship to Saccharomyces cerevisiae Dif1. We demonstrate that Spd1 can interact with both R1 and R2, and show that the major restraint of RNR in vivo by Spd1 is unrelated to R2 subcellular localization. Finally, we identify a new behavior for RNR complexes that potentially provides yet another mechanism to regulate dNTP synthesis via modulation of RNR complex architecture.","doi":"10.1101/gad.561910","authors":"Nestoras K, Mohammed AH, Schreurs AS, Fleck O, Watson AT, Poitelea M, O'Shea C, Chahwan C, Holmberg C, Kragelund BB, Nielsen O, Osborne M, Carr AM, Liu C","authors_abbrev":"Nestoras K et al.","pubmed_publication_date":"01 Jun 2010","pubmed_entrez_date":"2010-06-03","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16498704","title":"Basic methods for fission yeast.","citation":"Yeast 2006 Feb;23(3):173-83","abstract":"The fission yeast Schizosaccharomyces pombe is a popular model system, and has been particularly influential in studies of the cell cycle and chromosome dynamics. Despite its differences from Saccharomyces cerevisiae, the tools and methods for fission yeast are conceptually similar to those used in budding yeast. Here, we present basic methods sufficient for a beginner in this system to carry out most required manipulations for genetic analysis or molecular biology.","authors":"Forsburg SL, Rhind N","authors_abbrev":"Forsburg SL et al.","pubmed_publication_date":"Feb 2006","pubmed_entrez_date":"2006-02-25","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4669967","title":"Golgi apparatus in normal cells and protoplasts of Schizosaccharomyces pombe.","citation":"Microbios 1972;5(19):177-82","abstract":"","authors":"Smith DG, Svoboda A","authors_abbrev":"Smith DG et al.","pubmed_publication_date":"1972","pubmed_entrez_date":"1972-05-01","publication_year":"1972","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29727662","title":"Transcriptome-wide Interrogation of the Functional Intronome by Spliceosome Profiling.","citation":"Cell 2018 May 03;173(4):1031-1044.e13","abstract":"Full understanding of eukaryotic transcriptomes and how they respond to different conditions requires deep knowledge of all sites of intron excision. Although RNA sequencing (RNA-seq) provides much of this information, the low abundance of many spliced transcripts (often due to their rapid cytoplasmic decay) limits the ability of RNA-seq alone to reveal the full repertoire of spliced species. Here, we present \"spliceosome profiling,\" a strategy based on deep sequencing of RNAs co-purifying with late-stage spliceosomes. Spliceosome profiling allows for unambiguous mapping of intron ends to single-nucleotide resolution and branchpoint identification at unprecedented depths. Our data reveal hundreds of new introns in S. pombe and numerous others that were previously misannotated. By providing a means to directly interrogate sites of spliceosome assembly and catalysis genome-wide, spliceosome profiling promises to transform our understanding of RNA processing in the nucleus, much as ribosome profiling has transformed our understanding mRNA translation in the cytoplasm.","doi":"10.1016/j.cell.2018.03.062","authors":"Chen W, Moore J, Ozadam H, Shulha HP, Rhind N, Weng Z, Moore MJ","authors_abbrev":"Chen W et al.","pubmed_publication_date":"03 May 2018","pubmed_entrez_date":"2018-05-05","publication_year":"2018","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2018-05-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20139237","title":"Activated alleles of the Schizosaccharomyces pombe gpa2+ Galpha gene identify residues involved in GDP-GTP exchange.","citation":"Eukaryot Cell 2010 Apr;9(4):626-33","abstract":"The Schizosaccharomyces pombe glucose/cyclic AMP (cAMP) signaling pathway includes the Gpa2-Git5-Git11 heterotrimeric G protein, whose Gpa2 Galpha subunit directly binds to and activates adenylate cyclase in response to signaling from the Git3 G protein-coupled receptor. To study intrinsic and extrinsic regulation of Gpa2, we developed a plasmid-based screen to identify mutationally activated gpa2 alleles that bypass the loss of the Git5-Git11 Gbetagamma dimer to repress transcription of the glucose-regulated fbp1(+) gene. Fifteen independently isolated mutations alter 11 different Gpa2 residues, with all but one conferring a receptor-independent activated phenotype upon integration into the gpa2(+) chromosomal locus. Biochemical characterization of three activated Gpa2 proteins demonstrated an increased GDP-GTP exchange rate that would explain the mechanism of activation. Interestingly, the amino acid altered in the Gpa2(V90A) exchange rate mutant protein is in a region of Gpa2 with no obvious role in Galpha function, thus extending our understanding of Galpha protein structure-function relationships.","doi":"10.1128/EC.00010-10","authors":"Ivey FD, Taglia FX, Yang F, Lander MM, Kelly DA, Hoffman CS","authors_abbrev":"Ivey FD et al.","pubmed_publication_date":"Apr 2010","pubmed_entrez_date":"2010-02-09","publication_year":"2010","canto_session_key":"e806e3afc4cc7fc0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-28 10:10:02","canto_approved_date":"2022-03-21 17:33:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-12 10:37:50","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H3.13c","SPBC19C7.03","SPBC215.04","SPCC1753.02c","SPBC32H8.07"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-09-28"},{"uniquename":"PMID:16931912","title":"Spatial segregation of Ras signaling: new evidence from fission yeast.","citation":"Cell Cycle 2006 Sep;5(17):1936-9","abstract":"The Ras GTPases act as binary switches for signal transduction pathways that are important for growth regulation and tumorigenesis. Despite the biochemical simplicity of this switch, Ras proteins control multiple pathways, and the functions of the four mammalian Ras proteins are not overlapping. This raises an important question--how does a Ras protein selectively regulate a particular activity? One recently emerging model suggests that a single Ras protein can control different functions by acting in distinct cellular compartments. A critical test of this model is to identify pathways that are selectively controlled by Ras when it is localized to a particular compartment. A recent study has examined Ras signaling in the fission yeast Schizosaccharomyces pombe, which expresses only one Ras protein that controls two separate evolutionarily conserved pathways. This study demonstrates that whereas Ras localized to the plasma membrane selectively regulates a MAP kinase pathway to mediate mating pheromone signaling, Ras localized to the endomembrane activates a Cdc42 pathway to mediate cell polarity and protein trafficking. This study has provided unambiguous evidence for compartmentalized signaling of Ras.","authors":"Chang EC, Philips MR","authors_abbrev":"Chang EC et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-08-26","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7987414","title":"Phenotype of the fission yeast cell cycle regulatory mutant pim1-46 is suppressed by a tobacco cDNA encoding a small, Ran-like GTP-binding protein.","citation":"Plant J 1994 Oct;6(4):555-65","abstract":"Mutations in which the onset of mitosis is uncoupled from the completion of DNA replication has recently been described. Characterization of these mutants led to the identification of Pim1/Spi1 in fission yeast and RCC1/Ran proteins in mammalian cells. Their Saccharomyces cerevisae homologues, the MTR1/CNR1 proteins, appear to be involved in controlling RNA metabolism and transport. Here the isolation and partial characterization of plant cDNA clones which encode proteins homologous to the mammalian/fission yeast/budding yeast Ran/Spi/CNR proteins are reported. Higher plants appear to contain more than one gene per haploid genome which codes for Ran proteins. These genes are expressed in different plant tissues, including root tips and stems, known to contain mitotically active cells. The tobacco Ran-like proteins, like their mammalian and yeast homologues, are soluble proteins which are found in the cytoplasm and in the nucleus. In addition, it has been shown that overexpression of the tobacco Nt-Ran-A1 cDNA suppressed the phenotype of the temperature-sensitive fission yeast pim1-46 mutant. These results suggest that the plant Ran genes can be functionally equivalent to the mammalian/fission yeast/budding yeast Ran/Spi/CNR genes and that they may play a role: (i) in maintaining a coordinated cell cycle; (ii) in controlling RNA metabolism and transport in higher plants; and/or (iii) in protein import into the nucleus.","authors":"Merkle T, Haizel T, Matsumoto T, Harter K, Dallmann G, Nagy F","authors_abbrev":"Merkle T et al.","pubmed_publication_date":"Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_session_key":"ade4e74196f652e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-29 13:22:11","canto_approved_date":"2026-01-31 12:14:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-24 15:37:35","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC557.03c","SPBC1289.03c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-04-29"},{"uniquename":"PMID:38828770","title":"The fission yeast ortholog of Coilin, Mug174, forms Cajal body-like nuclear condensates and is essential for cellular quiescence.","citation":"Nucleic Acids Res 2024 Jun 03;","abstract":"The Cajal body, a nuclear condensate, is crucial for ribonucleoprotein assembly, including small nuclear RNPs (snRNPs). While Coilin has been identified as an integral component of Cajal bodies, its exact function remains unclear. Moreover, no Coilin ortholog has been found in unicellular organisms to date. This study unveils Mug174 (Meiosis-upregulated gene 174) as the Coilin ortholog in the fission yeast Schizosaccharomyces pombe. Mug174 forms phase-separated condensates in vitro and is often associated with the nucleolus and the cleavage body in vivo. The generation of Mug174 foci relies on the trimethylguanosine (TMG) synthase Tgs1. Moreover, Mug174 interacts with Tgs1 and U snRNAs. Deletion of the mug174+ gene in S. pombe causes diverse pleiotropic phenotypes, encompassing defects in vegetative growth, meiosis, pre-mRNA splicing, TMG capping of U snRNAs, and chromosome segregation. In addition, we identified weak homology between Mug174 and human Coilin. Notably, human Coilin expressed in fission yeast colocalizes with Mug174. Critically, Mug174 is indispensable for the maintenance of and transition from cellular quiescence. These findings highlight the Coilin ortholog in fission yeast and suggest that the Cajal body is implicated in cellular quiescence, thereby preventing human diseases.","doi":"10.1093/nar/gkae463","authors":"Deng X, Yao Q, Horvath A, Jiang Z, Zhao J, Fischer T, Sugiyama T","authors_abbrev":"Deng X et al.","pubmed_publication_date":"03 Jun 2024","pubmed_entrez_date":"2024-06-03","publication_year":"2024","canto_session_key":"3003c1548299203a","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-06-03 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1682.03c","SPAC2G11.15c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:31767786","title":"Interactions between SAM and the 5' UTR mRNA of the  sam1  gene regulate translation in  S. pombe .","citation":"RNA 2020 Feb;26(2):150-161","abstract":"The 5' untranslated region (5' UTR) of eukaryotic mRNA plays an important role in translation. Here we report the function of the 5' UTR mRNA of  S -adenosylmethionine synthetase ( sam1 ) in translational modulation in the presence of SAM in fission yeast  Schizosaccharomyces pombe  Reporter assays, binding and chemical probing experiments, and mutational analysis show that the 5' UTR mRNA of  sam1  binds to SAM to effect translation. Translational modulation is dependent on a tertiary structure transition in the RNA upon SAM binding. The characterization of such an RNA that is directly associated with an essential metabolic process in eukaryotes provides additional evidence that ligand binding by RNAs plays an important role in eukaryotic gene regulation.","doi":"10.1261/rna.072983.119","authors":"Zhang X, Sun W, Chen D, Murchie AIH","authors_abbrev":"Zhang X et al.","pubmed_publication_date":"Feb 2020","pubmed_entrez_date":"2019-11-27","publication_year":"2020","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-11-28 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14F5.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25373780","title":"A genomic Multiprocess survey of machineries that control and link cell shape, microtubule organization, and cell-cycle progression.","citation":"Dev Cell 2014 Oct 27;31(2):227-239","abstract":"Understanding cells as integrated systems requires that we systematically decipher how single genes affect multiple biological processes and how processes are functionally linked. Here, we used multiprocess phenotypic profiling, combining high-resolution 3D confocal microscopy and multiparametric image analysis, to simultaneously survey the fission yeast genome with respect to three key cellular processes: cell shape, microtubule organization, and cell-cycle progression. We identify, validate, and functionally annotate 262 genes controlling specific aspects of those processes. Of these, 62% had not been linked to these processes before and 35% are implicated in multiple processes. Importantly, we identify a conserved role for DNA-damage responses in controlling microtubule stability. In addition, we investigate how the processes are functionally linked. We show unexpectedly that disruption of cell-cycle progression does not necessarily affect cell size control and that distinct aspects of cell shape regulate microtubules and vice versa, identifying important systems-level links across these processes.","doi":"10.1016/j.devcel.2014.09.005","authors":"Graml V, Studera X, Lawson JLD, Chessel A, Geymonat M, Bortfeld-Miller M, Walter T, Wagstaff L, Piddini E, Carazo Salas RE","authors_abbrev":"Graml V et al.","pubmed_publication_date":"27 Oct 2014","pubmed_entrez_date":"2014-11-07","publication_year":"2014","canto_session_key":"b6cbfae4f8c5cbcb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-07-01 13:34:46","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-01 13:34:37","canto_added_date":"2014-11-08 01:15:26","annotation_curators":[],"file_curator_name":"Jonathan Lawson","file_curator_role":"community","annotation_file_curators":[{"name":"Jonathan Lawson","community_curator":true,"annotation_count":493,"orcid":"0000-0003-2331-2157","file_type":"PHAF","file_name":"PMID_25373780_phaf.tsv"}],"genes":["SPAC30.02c","SPCC1020.11c","SPAC3G9.08","SPAC1556.01c","SPBP22H7.08","SPAC14C4.10c","SPAC5H10.04","SPAC2C4.10c","SPAC6G10.02c","SPAC29B12.08","SPAC22A12.04c","SPCC790.02","SPCC1223.06","SPAC824.05","SPBC20F10.07","SPAC17A5.07c","SPAPB17E12.04c","SPBC21C3.02c","SPAC31A2.02","SPCC24B10.09","SPCC970.10c","SPBC1861.05","SPBC29A10.12","SPAC4C5.02c","SPAC3H8.05c","SPAC637.10c","SPBP8B7.18c","SPAC22H10.07","SPAC22F3.06c","SPBC19C2.13c","SPBC2D10.06","SPBC215.02","SPBC18H10.04c","SPBC713.11c","SPCC736.11","SPBC13G1.02","SPBC839.05c","SPAC343.20","SPBC21B10.13c","SPBC3H7.07c","SPAC4F10.04","SPAC20H4.07","SPAC664.03","SPAC30D11.05","SPCC63.02c","SPBC16C6.08c","SPAC1527.01","SPAC3A11.02","SPCC31H12.08c","SPAC21E11.03c","SPAC17A5.14","SPBC1734.07c","SPAC4H3.05","SPBC23G7.04c","SPAC323.05c","SPAC140.02","SPCC663.12","SPAC1F5.07c","SPCC594.05c","SPBC1105.04c","SPAC13C5.07","SPAC8C9.19","SPBC21H7.04","SPAC5D6.07c","SPAC8C9.03","SPCC895.06","SPBC3B9.09","SPAC11G7.02","SPAC3H8.09c","SPAC31F12.01","SPBC211.06","SPAC5D6.05","SPBC16G5.07c","SPAC23C11.10","SPBC3B8.02","SPCC24B10.08c","SPCC645.12c","SPAC6G9.04","SPCP1E11.05c","SPBP35G2.04c","SPBC23E6.08","SPAC26A3.09c","SPAC890.05","SPAC2F7.07c","SPBC543.08","SPAC6C3.08","SPAC3A12.13c","SPBC16G5.11c","SPAPB1E7.02c","SPAC3C7.03c","SPCC4G3.04c","SPAC227.17c","SPCC736.04c","SPBC3H7.10","SPCC1919.03c","SPAC4G8.07c","SPCC364.03","SPCC1322.03","SPCC23B6.03c","SPCC1450.03","SPCC11E10.06c","SPAC3A12.03c","SPAC16E8.08","SPAC3H1.13","SPAC1834.08","SPAC227.10","SPBP4H10.03","SPCC1840.03","SPAC644.14c","SPAC16E8.01","SPAC630.14c","SPAPYUG7.02c","SPBC4B4.06","SPBC1734.15","SPCC622.12c","SPCC965.06","SPAC1006.03c","SPAC29B12.04","SPBC1921.07c","SPCC1753.02c","SPAC27E2.03c","SPAC3F10.17","SPAC26H5.05","SPBC16E9.15","SPAC1952.05","SPCC24B10.12","SPBC336.14c","SPAPB1A10.08","SPAC31A2.13c","SPBPB7E8.01","SPAC4F8.01","SPAC22H10.11c","SPAC27D7.06","SPCC306.04c","SPAC16C9.05","SPBC17A3.05c","SPBC336.03","SPCC24B10.11c","SPAC17H9.19c","SPAC1F7.13c","SPAC1782.11","SPBC1706.01","SPCC584.11c","SPAC959.08","SPBC800.07c","SPBC13G1.08c","SPBC2G2.03c","SPCC1235.05c","SPAC2F7.03c","SPBC25B2.08","SPBP8B7.13","SPBC685.03","SPBC106.10","SPAC15E1.02c","SPBC146.09c","SPAC823.10c","SPAC29A4.20","SPBC11C11.09c","SPAC57A10.12c","SPBC19G7.16","SPCP1E11.06","SPCC338.08","SPBC29A10.01","SPAC1687.08","SPAC1F3.03","SPAC11E3.13c","SPAC11G7.04","SPBC1604.20c","SPAC31A2.11c","SPAC3H8.07c","SPBC2F12.11c","SPAC13G7.03","SPBC30B4.04c","SPAC17G8.05","SPAC1783.02c","SPBC2G2.01c","SPBC1718.07c","SPBC1604.12","SPAC17A2.09c","SPBC691.04","SPCC126.06","SPCC1672.04c","SPAC3A11.13","SPAC688.11","SPAC18G6.15","SPBC8D2.12c","SPAC1782.05","SPAC589.09","SPBC21.05c","SPCC1223.05c","SPCC1322.06","SPAC18B11.10","SPAC22F3.03c","SPAC823.05c","SPAC630.10","SPBC16A3.10","SPAC1F5.05c","SPAC328.04","SPBC36.04","SPAC227.01c","SPAC1142.07c","SPBC1D7.01","SPAC6G9.14","SPBC725.07","SPCC24B10.19c","SPAP14E8.02","SPAC23H3.13c","SPBC215.03c","SPAC17A5.08","SPAC23A1.16c","SPBC19F8.03c","SPBC27B12.10c","SPAC144.06","SPAC23D3.09","SPBC25H2.15","SPBC776.04","SPBC106.07c","SPAC3C7.08c","SPAC5H10.09c","SPAC12B10.10","SPBC800.03","SPCC1183.11","SPAC31G5.19","SPBC15D4.06","SPBC32F12.11","SPAC767.01c","SPBC13G1.10c","SPBC23E6.02","SPBC19C2.10","SPBC1539.08","SPAC9G1.03c","SPBC18H10.07","SPAC20G4.07c","SPBC16G5.15c","SPAC1610.02c","SPCC553.08c","SPBC32F12.05c","SPAC8F11.02c","SPBC29A10.16c","SPAC11G7.06c","SPBC19C2.02","SPAPB21F2.03","SPBC119.06","SPBC24C6.10c","SPCC188.07","SPBC409.07c","SPAC16C9.06c","SPBC146.13c","SPBC428.06c","SPBC21B10.05c","SPAC3C7.12","SPAC4G9.16c","SPCC338.16","SPAC3C7.06c","SPAC25H1.05","SPBC1289.16c","SPAC23H3.05c","SPBC2F12.03c","SPAC13G7.02c","SPAC25G10.03","SPBC1709.09","SPBC409.19c"],"gene_count":262,"ltp_gene_count":0,"approved_date":"2016-07-01"},{"uniquename":"PMID:12553909","title":"Schizosaccharomyces pombe Int6 and Ras homologs regulate cell division and mitotic fidelity via the proteasome.","citation":"Cell 2003 Jan 24;112(2):207-17","abstract":"Yin6 is a yeast homolog of Int6, which is implicated in tumorigenesis. We show that Yin6 binds to and regulates proteasome activity. Overexpression of Yin6 strengthens proteasome function while inactivation weakens and causes the accumulation of polyubiquitinated proteins including securin/Cut2 and cyclin/Cdc13. Yin6 regulates the proteasome by preferentially interacting with Rpn5, a conserved proteasome subunit, and affecting its localization/assembly. We showed previously that Yin6 cooperates with Ras1 to mediate chromosome segregation; here, we demonstrate that Ras1 similarly regulates the proteasome via Rpn5. In yeast, human Int6 binds Rpn5 and regulates its localization. We propose that human Int6, either alone or cooperatively with Ras, influences proteasome activities via Rpn5. Inactivating Int6 can lead to accumulation of mitotic regulators affecting cell division and mitotic fidelity.","authors":"Yen HC, Gordon C, Chang EC","authors_abbrev":"Yen HC et al.","pubmed_publication_date":"24 Jan 2003","pubmed_entrez_date":"2003-01-30","publication_year":"2003","canto_session_key":"20b51f83ef3dce69","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-29 11:28:53","canto_approved_date":"2026-01-31 13:26:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-23 15:47:38","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":52,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4.07c","SPAC17H9.09c","SPBC646.09c","SPAC637.07","SPAC31G5.13","SPBC14C8.01c","SPAC17C9.13c","SPBC16G5.01","SPAC637.10c","SPAC1420.03","SPBC582.03","SPAC16E8.09","SPAPB8E5.02c","SPBP19A11.03c"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2018-04-29"},{"uniquename":"PMID:29079705","title":"A novel de novo dominant mutation in  ISCU  associated with mitochondrial myopathy.","citation":"J Med Genet 2017 Dec;54(12):815-824","abstract":"A next-generation sequencing (NGS) approach was carried out on an Italian male who presented in childhood with ptosis, severe muscle weakness and exercise intolerance. His disease was slowly progressive, with partial recovery between episodes. Patient's specimens and yeast models were investigated.","doi":"10.1136/jmedgenet-2017-104822","authors":"Legati A, Reyes A, Ceccatelli Berti C, Stehling O, Marchet S, Lamperti C, Ferrari A, Robinson AJ, Mühlenhoff U, Lill R, Zeviani M, Goffrini P, Ghezzi D","authors_abbrev":"Legati A et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-10-29","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC227.13c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16222337","title":"Multistep and multimode cortical anchoring of tea1p at cell tips in fission yeast.","citation":"EMBO J 2005 Nov 02;24(21):3690-9","abstract":"The fission yeast cell-polarity regulator tea1p is targeted to cell tips by association with growing microtubule ends. Tea1p is subsequently anchored at the cell cortex at cell tips via an unknown mechanism that requires both the tea1p carboxy-terminus and the membrane protein mod5p. Here, we show that a tea1p-related protein, tea3p, binds independently to both mod5p and tea1p, and that tea1p and mod5p can also interact directly, independent of tea3p. Despite their related structures, different regions of tea1p and tea3p are required for their respective interactions with an essential central region of mod5p. We demonstrate that tea3p is required for proper cortical localization of tea1p, specifically at nongrowing cell tips, and that tea1p and mod5p are independently required for tea3p localization. Further, we find that tea3p fused to GFP or mCherry is cotransported with tea1p by microtubules to cell tips, but this occurs only in the absence of mod5p. These results suggest that independent protein-protein interactions among tea1p, tea3p and mod5p collectively contribute to tea1p anchoring at cell tips via a multistep and multimode mechanism.","authors":"Snaith HA, Samejima I, Sawin KE","authors_abbrev":"Snaith HA et al.","pubmed_publication_date":"02 Nov 2005","pubmed_entrez_date":"2005-10-14","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6G10.02c","SPCC1223.06","SPBC530.04"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AB084868","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.56"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPD171","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR11575","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:8021","SPAC1039.02","SPBPB2B2.06c","SPAC17G6.03"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:28892489","title":"Funneled potential and flux landscapes dictate the stabilities of both the states and the flow: Fission yeast cell cycle.","citation":"PLoS Comput Biol 2017 Sep;13(9):e1005710","abstract":"Using fission yeast cell cycle as an example, we uncovered that the non-equilibrium network dynamics and global properties are determined by two essential features: the potential landscape and the flux landscape. These two landscapes can be quantified through the decomposition of the dynamics into the detailed balance preserving part and detailed balance breaking non-equilibrium part. While the funneled potential landscape is often crucial for the stability of the single attractor networks, we have uncovered that the funneled flux landscape is crucial for the emergence and maintenance of the stable limit cycle oscillation flow. This provides a new interpretation of the origin for the limit cycle oscillations: There are many cycles and loops existed flowing through the state space and forming the flux landscapes, each cycle with a probability flux going through the loop. The limit cycle emerges when a loop stands out and carries significantly more probability flux than other loops. We explore how robustness ratio (RR) as the gap or steepness versus averaged variations or roughness of the landscape, quantifying the degrees of the funneling of the underlying potential and flux landscapes. We state that these two landscapes complement each other with one crucial for stabilities of states on the cycle and the other crucial for the stability of the flow along the cycle. The flux is directly related to the speed of the cell cycle. This allows us to identify the key factors and structure elements of the networks in determining the stability, speed and robustness of the fission yeast cell cycle oscillations. We see that the non-equilibriumness characterized by the degree of detailed balance breaking from the energy pump quantified by the flux is the cause of the energy dissipation for initiating and sustaining the replications essential for the origin and evolution of life. Regulating the cell cycle speed is crucial for designing the prevention and curing strategy of cancer.","doi":"10.1371/journal.pcbi.1005710","authors":"Luo X, Xu L, Han B, Wang J","authors_abbrev":"Luo X et al.","pubmed_publication_date":"Sep 2017","pubmed_entrez_date":"2017-09-12","publication_year":"2017","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2017-09-13 00:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16481403","title":"The fission yeast transforming acidic coiled coil-related protein Mia1p/Alp7p is required for formation and maintenance of persistent microtubule-organizing centers at the nuclear envelope.","citation":"Mol Biol Cell 2006 May;17(5):2212-22","abstract":"Microtubule-organizing centers (MTOCs) concentrate microtubule nucleation, attachment and bundling factors and thus restrict formation of microtubule arrays in spatial and temporal manner. How MTOCs occur remains an exciting question in cell biology. Here, we show that the transforming acidic coiled coil-related protein Mia1p/Alp7p functions in emergence of large MTOCs in interphase fission yeast cells. We found that Mia1p was a microtubule-binding protein that preferentially localized to the minus ends of microtubules and was associated with the sites of microtubule attachment to the nuclear envelope. Cells lacking Mia1p exhibited less microtubule bundles. Microtubules could be nucleated and bundled but were frequently released from the nucleation sites in mia1delta cells. Mia1p was required for stability of microtubule bundles and persistent use of nucleation sites both in interphase and postanaphase array dynamics. The gamma-tubulin-rich material was not organized in large perinuclear or microtubule-associated structures in mia1delta cells. Interestingly, absence of microtubules in dividing wild-type cells prevented appearance of large gamma-tubulin-rich MTOC structures in daughters. When microtubule polymerization was allowed, MTOCs were efficiently assembled de novo. We propose a model where MTOC emergence is a self-organizing process requiring the continuous association of microtubules with nucleation sites.","authors":"Zheng L, Schwartz C, Wee L, Oliferenko S","authors_abbrev":"Zheng L et al.","pubmed_publication_date":"May 2006","pubmed_entrez_date":"2006-02-17","publication_year":"2006","canto_session_key":"e7e1ea48e4e672fc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-02-19 22:10:18","canto_approved_date":"2018-02-19 22:10:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-12 17:56:59","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPBC20F10.06","SPAC890.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-02-19"},{"uniquename":"PMID:5868491","title":"Recombination among UV-induced andenine-l mutants of Schizosaccharomyces pombe.","citation":"Experientia 1965 Oct 15;21(10):582-3","abstract":"","authors":"Clarke CH","authors_abbrev":"Clarke CH","pubmed_publication_date":"15 Oct 1965","pubmed_entrez_date":"1965-10-15","publication_year":"1965","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12415007","title":"The small GTPase Rho3 and the diaphanous/formin For3 function in polarized cell growth in fission yeast.","citation":"J Cell Sci 2002 Dec 01;115(Pt 23):4629-39","abstract":"We identified a novel Rho gene rho3(+) and studied its interaction with diaphanous/formin for3(+) in the fission yeast Schizosaccharomyces pombe. Both rho3 null cells and for3 null cells showed defects in organization of not only actin cytoskeleton but also cytoplasmic microtubules (MTs). rho3 for3 double null cells had defects that were more severe than each single null cell: polarized growth was deficient in the double null cells. Function of For3 needed the highly conserved FH1 and FH2 domains, an N-terminal region containing a Rho-binding domain, and the C-terminal region. For3 bound to active forms of both Rho3 and Cdc42 but not to that of Rho1. For3 was localized as dots to the ends of interphase cells and to the mid-region in dividing cells. This localization was probably dependent on its interaction with Rho proteins. Overexpression of For3 produced huge swollen cells containing depolarized F-actin patches and thick cytoplasmic MT bundles. In addition, overexpression of a constitutively active Rho3Q71L induced a strong defect in cytokinesis. In conclusion, we propose that the Rho3-For3 signaling system functions in the polarized cell growth of fission yeast by controlling both actin cytoskeleton and MTs.","authors":"Nakano K, Imai J, Arai R, Toh-E A, Matsui Y, Mabuchi I","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"01 Dec 2002","pubmed_entrez_date":"2002-11-05","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.08","SPCC895.05","SPAC110.03"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:17174887","title":"Multiple mechanisms of meiotic recombination.","citation":"Cell 2006 Dec 15;127(6):1095-7","abstract":"In this issue, reveal that different meiotic recombination mechanisms predominate in fission yeast and budding yeast. Budding yeast usually form crossover recombinants through double Holliday junctions, whereas fission yeast unexpectedly appear to form crossover recombinants through single junctions.","authors":"Bishop DK","authors_abbrev":"Bishop DK","pubmed_publication_date":"15 Dec 2006","pubmed_entrez_date":"2006-12-19","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013709","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22121216","title":"OriDB, the DNA replication origin database updated and extended.","citation":"Nucleic Acids Res 2012 Jan;40(Database issue):D682-6","abstract":"OriDB (http://www.oridb.org/) is a database containing collated genome-wide mapping studies of confirmed and predicted replication origin sites. The original database collated and curated Saccharomyces cerevisiae origin mapping studies. Here, we report that the OriDB database and web site have been revamped to improve user accessibility to curated data sets, to greatly increase the number of curated origin mapping studies, and to include the collation of replication origin sites in the fission yeast Schizosaccharomyces pombe. The revised database structure underlies these improvements and will facilitate further expansion in the future. The updated OriDB for S. cerevisiae is available at http://cerevisiae.oridb.org/ and for S. pombe at http://pombe.oridb.org/.","doi":"10.1093/nar/gkr1091","authors":"Siow CC, Nieduszynska SR, Müller CA, Nieduszynski CA","authors_abbrev":"Siow CC et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2011-11-29","publication_year":"2012","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27003290","title":"A glucose-starvation response regulates the diffusion of macromolecules.","citation":"Elife 2016 Mar 22;5","abstract":"The organization and biophysical properties of the cytosol implicitly govern molecular interactions within cells. However, little is known about mechanisms by which cells regulate cytosolic properties and intracellular diffusion rates. Here, we demonstrate that the intracellular environment of budding yeast undertakes a startling transition upon glucose starvation in which macromolecular mobility is dramatically restricted, reducing the movement of both chromatin in the nucleus and mRNPs in the cytoplasm. This confinement cannot be explained by an ATP decrease or the physiological drop in intracellular pH. Rather, our results suggest that the regulation of diffusional mobility is induced by a reduction in cell volume and subsequent increase in molecular crowding which severely alters the biophysical properties of the intracellular environment. A similar response can be observed in fission yeast and bacteria. This reveals a novel mechanism by which cells globally alter their properties to establish a unique homeostasis during starvation.","doi":"10.7554/eLife.09376","authors":"Joyner RP, Tang JH, Helenius J, Dultz E, Brune C, Holt LJ, Huet S, Müller DJ, Weis K","authors_abbrev":"Joyner RP et al.","pubmed_publication_date":"22 Mar 2016","pubmed_entrez_date":"2016-03-23","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR021137","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC8D2.23","HGNC:14489"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16790931","title":"Detecting and overcoming hemihedral twinning during the MIR structure determination of Rna1p.","citation":"Acta Crystallogr D Biol Crystallogr 2006 Jul;62(Pt 7):750-65","abstract":"The structure of Rna1p was originally solved to 2.7 A resolution by MIRAS from crystals with partial hemihedral twinning in space group I4(1) [Hillig et al. (1999), Mol. Cell, 3, 781-791] by finding a low-twinned native crystal (twin fraction alpha=0.06) and after twin correction of all data sets. Rna1p crystals have now been used to examine how far twinning and twin correction affect MIR phasing with a higher resolution but highly twinned native data set. Even high hemihedral twinning [alphanative=0.39, alphaderivative=0.24] would not have hindered heavy-atom site identification of strong derivatives using difference Patterson maps. However, a weaker derivative could have been missed and refinement would have stalled at high R values had twinning not been identified and accounted for. Twin correction improved both site identification, experimental phasing statistics and MIR map quality. Different strategies were tested for refinement against twinned data. Using uncorrected twinned data and TWIN-CNS, Rna1p has now been refined to 2.2 A resolution (final twinned R and Rfree were 0.165 and 0.218, respectively). The increased resolution enabled release of the NCS restraints and allowed new conclusions to be drawn on the flexibility of the two molecules in the asymmetric unit. In the case of Rna1p, twinned crystal growth was possible owing to the presence of a twofold NCS axis almost parallel to the twin operator.","authors":"Hillig RC, Renault L","authors_abbrev":"Hillig RC et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-06-23","publication_year":"2006","canto_session_key":"50fa98ac03c3b6b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-03-08 18:23:46","canto_approved_date":"2023-03-08 18:23:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-08 18:23:31","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22E12.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-03-08","pdb_entries":[{"pdb_id":"2ca6","gene_chains":[{"gene_uniquename":"SPAC22E12.07","chain":"A/B","position":"1-386"}],"title":"MIRAS structure determination from hemihedrally twinned crystals","entry_authors":"Hillig RC,Renault L","entry_authors_abbrev":"Hillig RC et al.","reference_uniquename":"PMID:16790931","experimental_method":"X-ray","resolution":"2.2"}]},{"uniquename":"PMID:33375328","title":"Quick-Freeze, Deep-Etch Electron Microscopy Reveals the Characteristic Architecture of the Fission Yeast Spore.","citation":"J Fungi (Basel) 2020 Dec 26;7(1)","abstract":"The spore of the fission yeast  Schizosaccharomyces pombe  is a dormant cell that is resistant to a variety of environmental stresses. The  S. pombe  spore is coated by a proteinaceous surface layer, termed the Isp3 layer because it comprises mainly Isp3 protein. Although thin-section electron microscopy and scanning electron microscopy have revealed the fundamental structure of the spore, its architecture remains unclear. Here we visualized  S. pombe  spores by using a quick-freeze replica electron microscopy (QFDE-EM) at nanometer resolution, which revealed novel characteristic structures. QFDE-EM revealed that the Isp3 layer exists as an interwoven fibrillar layer. On the spore cell membrane, many deep invaginations, which are longer than those on the vegetative cell membrane, are aligned in parallel. We also observed that during spore germination, the cell surface changes from a smooth to a dendritic filamentous structure, the latter being characteristic of vegetative cells. These findings provide significant insight into not only the structural composition of the spore, but also the mechanism underlying the stress response of the cell.","doi":"10.3390/jof7010007","authors":"Tahara YO, Miyata M, Nakamura T","authors_abbrev":"Tahara YO et al.","pubmed_publication_date":"26 Dec 2020","pubmed_entrez_date":"2020-12-30","publication_year":"2020","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2021-01-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F8.05"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:29153394","title":"VCP/p97-Mediated Unfolding as a Principle in Protein Homeostasis and Signaling.","citation":"Mol Cell 2018 Jan 18;69(2):182-194","abstract":"The AAA+-type ATPase p97 governs an ever-expanding number of cellular processes reaching from degradation of damaged proteins and organelles to key signaling events and chromatin regulation with thousands of client proteins. With its relevance for cellular homeostasis and genome stability, it is linked to muscular and neuronal degeneration and, conversely, constitutes an attractive anti-cancer drug target. Its molecular function is ATP-driven protein unfolding, which is directed by ubiquitin and assisted by a host of cofactor proteins. This activity underlies p97's diverse ability to pull proteins out of membranes, unfold proteins for proteasomal degradation, or segregate proteins from partners for downstream activity. Recent advances in structural analysis and biochemical reconstitution have underscored this notion, resolved detailed molecular motions within the p97 hexamer, and suggested substrate threading through the central channel of the p97 hexamer as the driving mechanism. We will discuss the mechanisms and open questions in the context of the diverse cellular activities.","doi":"10.1016/j.molcel.2017.10.028","authors":"van den Boom J, Meyer H","authors_abbrev":"van den Boom J et al.","pubmed_publication_date":"18 Jan 2018","pubmed_entrez_date":"2017-11-21","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1565.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24484668","title":"Visualizing single rod-shaped fission yeast vertically in micro-sized holes on agarose pad made by soft lithography.","citation":"Methods Cell Biol 2014;120:227-34","abstract":"Fission yeast cells are rod-shaped unicellular organism that is normally imaged horizontally with its long axis parallel to image plane. This orientation, while practical, limits the imaging resolution of biological structures which are oriented perpendicular to the long axis of the cell. We present here a method to prepare agarose pads with micro-sized holes to load single fission yeast cell vertically and image cell with its long axis perpendicular to the image plane. As a demonstration, actomyosin ring contraction is shown with this new imaging device.","doi":"10.1016/B978-0-12-417136-7.00015-X","authors":"Wang L, Tran PT","authors_abbrev":"Wang L et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-04","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29914874","title":"Long noncoding RNA repertoire and targeting by nuclear exosome, cytoplasmic exonuclease, and RNAi in fission yeast.","citation":"RNA 2018 Sep;24(9):1195-1213","abstract":"Long noncoding RNAs (lncRNAs), which are longer than 200 nucleotides but often unstable, contribute a substantial and diverse portion to pervasive noncoding transcriptomes. Most lncRNAs are poorly annotated and understood, although several play important roles in gene regulation and diseases. Here we systematically uncover and analyze lncRNAs in  Schizosaccharomyces pombe.  Based on RNA-seq data from twelve RNA-processing mutants and nine physiological conditions, we identify 5775 novel lncRNAs, nearly 4× the previously annotated lncRNAs. The expression of most lncRNAs becomes strongly induced under the genetic and physiological perturbations, most notably during late meiosis. Most lncRNAs are cryptic and suppressed by three RNA-processing pathways: the nuclear exosome, cytoplasmic exonuclease, and RNAi. Double-mutant analyses reveal substantial coordination and redundancy among these pathways. We classify lncRNAs by their dominant pathway into cryptic unstable transcripts (CUTs), Xrn1-sensitive unstable transcripts (XUTs), and Dicer-sensitive unstable transcripts (DUTs). XUTs and DUTs are enriched for antisense lncRNAs, while CUTs are often bidirectional and actively translated. The cytoplasmic exonuclease, along with RNAi, dampens the expression of thousands of lncRNAs and mRNAs that become induced during meiosis. Antisense lncRNA expression mostly negatively correlates with sense mRNA expression in the physiological, but not the genetic conditions. Intergenic and bidirectional lncRNAs emerge from nucleosome-depleted regions, upstream of positioned nucleosomes. Our results highlight both similarities and differences to lncRNA regulation in budding yeast. This broad survey of the lncRNA repertoire and characteristics in  S. pombe,  and the interwoven regulatory pathways that target lncRNAs, provides a rich framework for their further functional analyses.","doi":"10.1261/rna.065524.118","authors":"Atkinson SR, Marguerat S, Bitton DA, Rodríguez-López M, Rallis C, Lemay JF, Cotobal C, Malecki M, Smialowski P, Mata J, Korber P, Bachand F, Bähler J","authors_abbrev":"Atkinson SR et al.","pubmed_publication_date":"Sep 2018","pubmed_entrez_date":"2018-06-20","publication_year":"2018","canto_session_key":"627a2efc48957a76","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jurg Bahler","canto_first_approved_date":"2019-01-11 17:29:27","canto_approved_date":"2026-01-26 11:35:03","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-01-02 13:47:55","canto_added_date":"2018-06-21 00:15:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jurg 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SpTRK gene encodes a potassium-specific transport protein TKHp in Schizosaccharomyces pombe.","citation":"J Membr Biol 1996 Jul;152(2):169-81","abstract":"Complementary DNAs involved in potassium transport in Schizosaccharomyces pombe were selected by complementation of defective K+ uptake in a trk1 trk2 mutant of Saccharomyces cerevisiae. Here we describe the SpTRK gene that encodes a protein of 833 amino acids. The predicted structure contains 12 putative membrane-spanning domains and resembles various high- and low-affinity systems for K+ transport in yeasts and plants. TKHp, the product of SpTRK exhibits high homology to TRK1 and TRK2 of Saccharomyces cerevisiae as well as to HKT1 of Triticum aestivum, but is not related to HAK1 of another ascomycete, Schwanniomyces occidentalis, suggesting that different routes for potassium uptake evolved independently. This protein is a potassium-specific transporter since functional analysis of the SpTRK complemented mutant strain of Sacch. cerevisiae revealed potassium transport affinities and uptake characteristics similar to those obtained in wild-type Sch. pombe. Patch-clamp analysis in the whole-cell mode confirmed the TKHp-mediated inward current in the complemented strain. The inward current increased by acidification of the extracellular medium thereby suggesting a mechanism of K+H+ cotransport. The inward current is not detectable when external K+ is substituted by Na+, documenting a distinct cation specificity of the protein.","authors":"Lichtenberg-Fraté H, Reid JD, Heyer M, Höfer M","authors_abbrev":"Lichtenberg-Fraté H et al.","pubmed_publication_date":"Jul 1996","pubmed_entrez_date":"1996-07-01","publication_year":"1996","canto_session_key":"16bfe6acf62c3846","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-11-07 16:20:32","canto_approved_date":"2017-11-07 16:20:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-11-14 14:09:46","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-11-07"},{"uniquename":"PMID:20948299","title":"Setting the F-BAR: functions and regulation of the F-BAR protein family.","citation":"Cell Cycle 2010 Oct 15;9(20):4091-7","abstract":"F-BAR domain proteins serve as transient linkers between the cell cortex and the cytoskeleton in multiple biological contexts. Recent studies have detailed roles for this protein family in endocytosis, cytokinesis, neurotransmission, motility and cellular morphogenesis. Here, we review emerging functional information regarding the recently recognized F-BAR domain family and the regulatory mechanisms whereby F-BAR proteins are deployed in diverse processes.","authors":"Roberts-Galbraith RH, Gould KL","authors_abbrev":"Roberts-Galbraith RH et al.","pubmed_publication_date":"15 Oct 2010","pubmed_entrez_date":"2010-10-16","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-02-28 14:19:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D89155","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8491190","title":"Two novel protein kinase C-related genes of fission yeast are essential for cell viability and implicated in cell shape control.","citation":"EMBO J 1993 May;12(5):1987-95","abstract":"Two novel protein kinase C (PKC)-like genes, pck1+ and pck2+ were isolated from fission yeast by PCR. Both contain common domains of PKC-related molecules, but lack a putative Ca(2+)-binding domain so that they may belong to the nPKC group. Gene disruption of pck1+ and pck2+ establishes that they share an overlapping essential function for cell viability. Cells of a single pck2 deletion display severe defects in cell shape; they are irregular and sometimes pear-like instead of cylindrical. In contrast, the induced overexpression of pck2+ is lethal, producing multiseptated and branched cells. These results suggest that fission yeast PKC-like genes are involved in the polarity of cell growth control. We show that pck2 is allelic to sts6, a locus we have previously identified by its supersensitivity to staurosporine, a potent protein kinase inhibitor [Toda et al. (1991) Genes Dev., 5, 60-73]. In addition, the lethal overexpression of pck2+ can be suppressed by staurosporine, indicating that fission yeast pck1 and pck2 are molecular targets of this inhibitor.","authors":"Toda T, Shimanuki M, Yanagida M","authors_abbrev":"Toda T et al.","pubmed_publication_date":"May 1993","pubmed_entrez_date":"1993-05-01","publication_year":"1993","canto_session_key":"d2202f49e28f4101","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-26 13:04:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-05-21 18:50:21","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.14c","SPBC12D12.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-05-21"},{"uniquename":"PMID:28715960","title":"Histone Methylation by SET Domain Proteins in Fungi.","citation":"Annu Rev Microbiol 2017 Sep 08;71:413-439","abstract":"Histone-modifying enzymes are responsible for regulating transcription, recombination, DNA repair, DNA replication, chromatid cohesion, and chromosome segregation. Fungi are ideally suited for comparative chromatin biology because sequencing of numerous genomes from many clades is coupled to existing rich methodology that allows truly holistic approaches, integrating evolutionary biology with mechanistic molecular biology and ecology, promising applications in medicine or plant pathology. While genome information is rich, mechanistic studies on histone modifications are largely restricted to two yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe, and one filamentous fungus, Neurospora crassa-three species that arguably are not representative of this diverse kingdom. Here, histone methylation serves as a paradigm to illustrate the roles chromatin modifications may play in more complex fungal life cycles. This review summarizes recent advances in our understanding of histone H3 methylation at two sites associated with active transcription, lysine 4 and lysine 36 (H3K4, H3K36); a site associated with the formation of constitutive heterochromatin, lysine 9 (H3K9); and a site associated with the formation of facultative heterochromatin, lysine 27 (H3K27). Special attention is paid to differences in how methylation marks interact in different taxa.","doi":"10.1146/annurev-micro-102215-095757","authors":"Freitag M","authors_abbrev":"Freitag M","pubmed_publication_date":"08 Sep 2017","pubmed_entrez_date":"2017-07-19","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-07-21 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11707284","title":"The protein phosphatase 2A B'-regulatory subunit par1p is implicated in regulation of the S. pombe septation initiation network.","citation":"FEBS Lett 2001 Nov 09;508(1):136-42","abstract":"In order to identify regulators of the Schizosaccharomyces pombe septation initiation network (SIN), which signals the onset of cell division, we have isolated extragenic suppressors of mutations in the GTPase spg1p, which is a central element in this pathway. One of these encodes the protein phosphatase 2A (PP2A) B'-regulatory subunit par1p. Loss of par1p function rescues mutants in cdc11, cdc7, and spg1, but no other SIN mutants. Our data suggest that PP2A-par1p acts as a negative regulator of SIN signalling.","authors":"Le Goff X, Buvelot S, Salimova E, Guerry F, Schmidt S, Cueille N, Cano E, Simanis V","authors_abbrev":"Le Goff X et al.","pubmed_publication_date":"09 Nov 2001","pubmed_entrez_date":"2001-11-15","publication_year":"2001","canto_session_key":"14946b41b544a62a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-04-28 06:20:01","canto_approved_date":"2020-01-22 22:17:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-15 11:51:59","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPCC4B3.15","SPAC24B11.11c","SPAC1565.06c","SPBC428.13c","SPBC244.01c","SPBC24C6.07","SPAC227.07c","SPCC188.02","SPBC21.06c","SPCC1739.11c"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2016-04-28"},{"uniquename":"PMID:4842083","title":"UV-induced replicating instability in Schizosaccharomyces pombe.","citation":"Mutat Res 1974 Jan;22(1):25-31","abstract":"","authors":"Nasim A","authors_abbrev":"Nasim A","pubmed_publication_date":"Jan 1974","pubmed_entrez_date":"1974-01-01","publication_year":"1974","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9737967","title":"Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1998 Sep 25;273(39):25098-105","abstract":"The mutY homolog (SpMYH) gene from a cDNA library of Schizosaccharomyces pombe encodes a protein of 461 amino acids that displays 28 and 31% identity to Escherichia coli MutY and human MutY homolog (MYH), respectively. Expressed SpMYH is able to complement an E. coli mutY mutant to reduce the mutation rate. Similar to E. coli MutY protein, purified recombinant SpMYH expressed in E. coli has adenine DNA glycosylase and apurinic/apyrimidinic lyase activities on A/G- and A/7,8-dihydro-8-oxoguanine (8-oxoG)-containing DNA. However, both enzymes have different salt requirements and slightly different substrate specificities. SpMYH has greater glycosylase activity on 2-aminopurine/G and A/2-aminopurine but weaker activity on A/C than E. coli MutY. Both enzymes also have different substrate binding affinity and catalytic parameters. Although SpMYH has great affinity to A/8-oxoG-containing DNA as MutY, the binding affinity to A/G-containing DNA is substantially lower for SpMYH than MutY. SpMYH has similar reactivity to both A/G- and A/8-oxoG-containing DNA; however, MutY cleaves A/G-containing DNA about 3-fold more efficiently than it does A/8-oxoG-containing DNA. Thus, SpMYH is the functional eukaryotic MutY homolog responsible for reduction of 8-oxoG mutational effect.","authors":"Lu AL, Fawcett WP","authors_abbrev":"Lu AL et al.","pubmed_publication_date":"25 Sep 1998","pubmed_entrez_date":"1998-09-17","publication_year":"1998","canto_session_key":"1d44ae6b2e750c85","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-03-26 22:35:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-05 16:37:32","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-05"},{"uniquename":"PMID:16842820","title":"A new model for Schizosaccharomyces pombe telomere recognition: the telomeric single-stranded DNA-binding activity of Pot11-389.","citation":"J Mol Biol 2006 Aug 04;361(1):80-93","abstract":"The protection of telomeres 1 (Pot1) proteins specifically recognize the single-stranded 3' end of the telomere, an activity essential for sustained cellular viability and proliferation. The current model for the telomeric single-stranded DNA (ssDNA) binding activity of Schizosaccharomyces pombe Pot1 is based on a 20 kDa fragment, Pot1pN. Recent biochemical studies suggest that SpPot1 contains a larger ssDNA-binding domain and we have identified a novel ssDNA-binding domain similar in size to the human Pot1 domain. This domain, Pot1(1-389), binds extremely tightly to an oligonucleotide consisting of two conserved hexameric S. pombe telomere repeats, d(GGTTACGGTTAC), with an affinity approximately 4000-fold tighter than Pot1pN binds its cognate ssDNA. The Pot1(1-389)/ssDNA complex exhibits a half-life of 53 min, consistent with that estimated for full-length SpPot1 and significantly longer than that of Pot1pN. Single nucleotide substitutions reveal that, in contrast to Pot1pN, tandem trinucleotide repeats (GTT) within d(GGTTACGGTTAC) are specifically recognized by Pot1(1-389). Interestingly, certain single nucleotide substitutions that impacted Pot1pN binding exhibited no effect on binding affinity by Pot1(1-389). However, these substitutions reduced binding affinity when simultaneously substituted in each hexameric repeat. The non-additive nature of these substitutions suggests that certain nucleotides are coupled through the ability of the flexible ssDNA oligonucleotide to adopt alternate, thermodynamically equivalent conformations. The biochemical behavior of Pot1(1-389) is more similar to that of the full-length SpPot1 protein than to that of Pot1pN, making Pot1(1-389) a valuable domain for the future study of how full-length SpPot1 interacts with telomeric ssDNA.","authors":"Croy JE, Podell ER, Wuttke DS","authors_abbrev":"Croy JE et al.","pubmed_publication_date":"04 Aug 2006","pubmed_entrez_date":"2006-07-18","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7479088","title":"A strategy for quickly identifying all unique two-hybrid or library plasmids within a pool of yeast transformants.","citation":"Nucleic Acids Res 1995 Oct 25;23(20):4222-3","abstract":"","authors":"Patterson TE, Stark GR, Sazer S","authors_abbrev":"Patterson TE et al.","pubmed_publication_date":"25 Oct 1995","pubmed_entrez_date":"1995-10-25","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11886858","title":"The serine/threonine kinase Cmk2 is required for oxidative stress response in fission yeast.","citation":"J Biol Chem 2002 May 17;277(20):17722-7","abstract":"Cmk2, a fission yeast Ser/Thr protein kinase homologous to mammalian calmodulin kinases, is essential for oxidative stress response. Cells lacking cmk2 gene were specifically sensitive to oxidative stress conditions. Upon stress, Cmk2 was phosphorylated in vivo, and this phosphorylation was dependent on the stress-activated MAPK Sty1/Spc1. Co-precipitation assays demonstrated that Cmk2 binds Sty1. Furthermore, in vivo or in vitro activated Sty1 was able to phosphorylate Cmk2, and the phosphorylation occurred at the C-terminal regulatory domain at Thr-411. Cell lethality caused by overexpression of Wis1 MAPK kinase was abolished by deletion of cmk2 or by mutation of Thr-411 of Cmk2. Taken together, our data suggest that Cmk2 acts downstream of Sty1 and is an essential kinase for oxidative stress responses.","authors":"Sánchez-Piris M, Posas F, Alemany V, Winge I, Hidalgo E, Bachs O, Aligue R","authors_abbrev":"Sánchez-Piris M et al.","pubmed_publication_date":"17 May 2002","pubmed_entrez_date":"2002-03-12","publication_year":"2002","canto_session_key":"f302ee9f01375c61","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-08 07:29:06","canto_approved_date":"2022-11-19 17:11:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-24 15:20:13","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23A1.06c","SPBC409.07c","SPAC24B11.06c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-08-08"},{"uniquename":"PMID:11689451","title":"Regulation of replication timing in fission yeast.","citation":"EMBO J 2001 Nov 01;20(21):6115-26","abstract":"Here we report the first characterization of replication timing and its regulation in the fission yeast Schizosaccharomyces pombe. We used three different synchronization methods: centrifugal elutriation, cdc10 temperature-shift and release, and starvation for deoxyribonucleoside triphosphates (dNTPs) by treatment with hydroxyurea (HU) followed by removal of HU, to study the times when specific autonomously replicating sequence elements (ARS elements; potential replication origins) replicate during S phase. We found that individual ARS elements replicate at characteristic times, some early and some late, independently of synchronization method. In wild-type cells treated with HU, early ARS elements replicated but late ones did not. However, in HU-treated mutant cells lacking the Rad3 (similar to human ATR and ATM) or Cds1 (similar to human CHK2) checkpoint kinase, both early and late ARS elements were able to replicate. Thus under conditions of dNTP starvation the Rad3 and Cds1 kinases are needed to suppress the replication of normally late-replicating regions.","authors":"Kim SM, Huberman JA","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"01 Nov 2001","pubmed_entrez_date":"2001-11-02","publication_year":"2001","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29799770","title":"The Rag GTPase-Ragulator complex attenuates TOR complex 1 signaling in fission yeast.","citation":"Autophagy 2018;14(6):1105-1106","abstract":"Target of rapamycin complex 1 (TORC1) is an evolutionarily conserved protein kinase complex, whose activation in response to nutrients suppresses autophagy. In mammalian cells, amino-acid stimuli induce lysosomal translocation and activation of MTORC1 through the RRAG GTPase heterodimer, which is tethered to the surface of lysosomes by the Ragulator complex. Our recent study demonstrated that the fission yeast Schizosaccharomyces pombe also has a Ragulator complex that anchors the Gtr1-Gtr2 Rag GTPase heterodimer to the vacuole, a lysosome-like organelle. Unexpectedly, however, neither vacuolar localization nor activation of TORC1 is dependent on the Rag-Ragulator complex, which instead plays a critical role in attenuating TORC1 signaling. Our findings suggest dual functionality of the Rag GTPase in both activation and inactivation of TORC1.","doi":"10.1080/15548627.2018.1444313","authors":"Fukuda T, Shiozaki K","authors_abbrev":"Fukuda T et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-05-26","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-05-30 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:13311482","title":"[Methodological Information on the Genetics of Schizosaccharomyces Pombe].","citation":"Schweiz Z Pathol Bakteriol 1955;18(5):1141-6","abstract":"","authors":"LEUPOLD U","authors_abbrev":"LEUPOLD U","pubmed_publication_date":"1955","pubmed_entrez_date":"1955-01-01","publication_year":"1955","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2020-09-25 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15300681","title":"Characterization of end4+, a gene required for endocytosis in Schizosaccharomyces pombe.","citation":"Yeast 2004 Jul 30;21(10):867-81","abstract":"To understand endocytic trafficking in Schizosaccharomyces pombe, we constructed an end4 disruption mutant. The end4+ gene encodes a protein homologous to Sla2p/End4p, which is essential for the assembly and function of the cytoskeleton and endocytosis in Saccharomyces cerevisiae. We characterized the fission yeast mutant end4 Delta as well as ypt7 Delta, which is deficient in vacuolar fusion and, hence, endocytosis. The delivery of FM4-64 to the vacuolar membrane, accumulation of Lucifer yellow CH and internalization of plasma membrane protein Map3-GFP were inhibited in the end4 mutant. Deletion of end4 resulted in pleiotropic phenotypes consistent with F-actin depolarization, including high temperature sensitivity, abnormal morphology and mating defects. Extensive missorting of carboxypeptidase Y was detected in the ypt7 mutant; however, little missorting was detected in the end4 mutant. These results indicate that End4p is essential for the internalization process and Ypt7p affects endocytosis at a post-internalization step after the intersection of the endocytic and the vacuolar protein-sorting pathways in fission yeast.","authors":"Iwaki T, Tanaka N, Takagi H, Giga-Hama Y, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"30 Jul 2004","pubmed_entrez_date":"2004-08-10","publication_year":"2004","canto_session_key":"fbdb631024e4e2dd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-20 12:00:15","canto_approved_date":"2026-04-15 16:21:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-20 12:00:09","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.11","SPAC3F10.10c","SPAC21E11.04","SPBC405.04c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-10-20"},{"uniquename":"PMID:32507070","title":"Puncta intended: connecting the dots between autophagy and cell stress networks.","citation":"Autophagy 2021 Apr;17(4):1028-1033","abstract":"Proteome profiling and global protein-interaction approaches have significantly improved our knowledge of the protein interactomes of autophagy and other cellular stress-response pathways. New discoveries regarding protein complexes, interaction partners, interaction domains, and biological roles of players that are part of these pathways are emerging. The fourth Vancouver Autophagy Symposium showcased research that expands our understanding of the protein interaction networks and molecular mechanisms underlying autophagy and other cellular stress responses in the context of distinct stressors. In the keynote presentation, Dr. Wade Harper described his team's recent discovery of a novel reticulophagy receptor for selective autophagic degradation of the endoplasmic reticulum, and discussed molecular mechanisms involved in ribophagy and non-autophagic ribosomal turnover. In other presentations, both omic and targeted approaches were used to reveal molecular players of other cellular stress responses including amyloid body and stress granule formation, anastasis, and extracellular vesicle biogenesis. Additional topics included the roles of autophagy in disease pathogenesis, autophagy regulatory mechanisms, and crosstalk between autophagy and cellular metabolism in anti-tumor immunity. The relationship between autophagy and other cell stress responses remains a relatively unexplored area in the field, with future investigations required to understand how the various processes are coordinated and connected in cells and tissues. Abbreviations:  A-bodies: amyloid bodies; ACM: amyloid-converting motif; AMFR/gp78: autocrine motility factor receptor; ATG: autophagy-related; ATG4B: autophagy related 4B cysteine peptidase; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; CAR T: chimeric antigen receptor T; CASP3: caspase 3; CCPG1: cell cycle progression 1; CAR: chimeric antigen receptor; CML: chronic myeloid leukemia; CCOCs: clear cell ovarian cancers; CVB3: coxsackievirus B3; CRISPR-Cas9: clustered regularly interspaced short palindromic repeats-CRISPR associated protein 9; DDXs: DEAD-box helicases; EIF2S1/EIF-2alpha: eukaryotic translation initiation factor 2 subunit alpha; EIF2AK3: eukaryotic translation initiation factor 2 alpha kinase 3; ER: endoplasmic reticulum; EV: extracellular vesicle; FAO: fatty acid oxidation; GABARAP: GABA type A receptor-associated protein; ILK: integrin linked kinase; ISR: integrated stress response; MTOR: mechanistic target of rapamycin kinase; MPECs: memory precursory effector T cells; MAVS: mitochondrial antiviral signaling protein; NBR1: NBR1 autophagy cargo receptor; PI4KB/PI4KIIIβ: phosphatidylinositol 4-kinase beta; PLEKHM1: pleckstrin homology and RUN domain containing M1; RB1CC1: RB1 inducible coiled-coil 1; RTN3: reticulon 3; rIGSRNAs: ribosomal intergenic noncoding RNAs; RPL29: ribosomal protein L29; RPS3: ribosomal protein S3;  S. cerevisiae: Saccharomyces cerevisiae ; sEV: small extracellular vesicles;  S. pombe: Schizosaccharomyces pombe ; SQSTM1: sequestosome 1; SF3B1: splicing factor 3b subunit 1; SILAC-MS: stable isotope labeling with amino acids in cell culture-mass spectrometry; SNAP29: synaptosome associated protein 29; TEX264: testis expressed 264, ER-phagy receptor; TNBC: triple-negative breast cancer; ULK1: unc-51 like autophagy activating kinase 1; VAS: Vancouver Autophagy Symposium.","doi":"10.1080/15548627.2020.1775394","authors":"Ho CJ, Samarasekera G, Rothe K, Xu J, Yang KC, Leung E, Chan M, Jiang X, Gorski SM","authors_abbrev":"Ho CJ et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2020-06-09","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-06-10 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11751918","title":"The fission yeast ES2 homologue, Bis1, interacts with the Ish1 stress-responsive nuclear envelope protein.","citation":"J Biol Chem 2002 Mar 22;277(12):10562-72","abstract":"In fission yeast, nutrient starvation induces physiological, biochemical, and morphological changes that enable survival. Collectively these changes are referred to as stationary phase. We have used a green fluorescent protein random insertional mutagenesis system to isolate two novel stress-response proteins required in stationary phase. Ish1 is a nuclear envelope protein that is present throughout the cell cycle and whose expression is increased in response to stresses such as glucose and nitrogen starvation, as well as osmotic stress. Expression of Ish1 is regulated by the Spc1 MAPK pathway through the Atf1 transcription factor. Although overexpression of Ish1 is lethal, cells lacking ish1 exhibit reduced viability in stationary phase. Bis1 is a novel interacting partner of Ish1. Bis1 is the Schizosaccharomyces pombe member of the ES2 nuclear protein family found in Mus musculus, Drosophila melanogaster, Homo sapiens, and Arabidopsis thaliana. Overexpression of Bis1 results in a cell elongation phenotype, whereas bis1(-) cells exhibit a reduced viability in stationary phase similar to that seen in ish1(-) cells.","authors":"Taricani L, Tejada ML, Young PG","authors_abbrev":"Taricani L et al.","pubmed_publication_date":"22 Mar 2002","pubmed_entrez_date":"2001-12-26","publication_year":"2002","canto_session_key":"db6309329cdcdb7b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-02 16:59:44","canto_approved_date":"2026-04-08 21:02:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-29 09:23:21","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.11c","SPAC26F1.10c","SPBC14F5.03c","SPBC1604.06c","SPAC19G12.10c","SPBC211.04c","SPAC3G9.10c","SPBC9B6.05c","SPAC644.04","SPAC6B12.15","SPCC364.02c","SPAC6F6.12","SPAC24B11.06c","SPAC27F1.04c","SPBC1105.04c","SPBC211.02c","SPCC162.08c","SPCC1672.10","SPAPB1E7.12","SPBC1604.08c","SPBC16H5.11c","SPBC839.10","SPAC23G3.11","SPAC22F3.13","SPBC29B5.01","SPBC365.12c","SPAC1687.05"],"gene_count":27,"ltp_gene_count":27,"approved_date":"2015-06-02"},{"uniquename":"PMID:27697865","title":"Inositol Pyrophosphate Kinase Asp1 Modulates Chromosome Segregation Fidelity and Spindle Function in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2016 Dec 15;36(24):3128-3140","abstract":"Chromosome transmission fidelity during mitosis is of critical importance for the fitness of an organism, as mistakes will lead to aneuploidy, which has a causative role in numerous severe diseases. Proper segregation of chromosomes depends on interdependent processes at the microtubule-kinetochore interface and the spindle assembly checkpoint. Here we report the discovery of a new element essential for chromosome transmission fidelity that implicates inositol pyrophosphates (IPPs) as playing a key role in this process. The protein is Asp1, the Schizosaccharomyces pombe member of the highly conserved Vip1 family. Vip1 enzymes are bifunctional: they consist of an IPP-generating kinase domain and a pyrophosphatase domain that uses such IPPs as substrates. We show that Asp1 kinase function is required for bipolar spindle formation. The absence of Asp1-generated IPPs resulted in errors in sister chromatid biorientation, a prolonged checkpoint-controlled delay of anaphase onset, and chromosome missegregation. Remarkably, expression of Asp1 variants that generated higher-than-wild-type levels of IPPs led to a faster-than-wild-type entry into anaphase A without an increase in chromosome missegregation. In fact, the chromosome transmission fidelity of a nonessential chromosome was enhanced with increased cellular IPPs. Thus, we identified an element that optimized the wild-type chromosome transmission process.","authors":"Topolski B, Jakopec V, Künzel NA, Fleig U","authors_abbrev":"Topolski B et al.","pubmed_publication_date":"15 Dec 2016","pubmed_entrez_date":"2016-10-05","publication_year":"2016","canto_session_key":"a2ee596ebb2b3e9a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ursula Fleig","canto_first_approved_date":"2018-04-17 11:53:45","canto_approved_date":"2025-02-27 09:19:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-03 11:29:31","canto_added_date":"2016-10-07 00:15:11","annotation_curators":[{"name":"Ursula Fleig","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPCC1672.06c","SPBC1685.15c","SPAC25G10.07c","SPAC3A11.14c","SPBC106.01"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-04-17"},{"uniquename":"PMID:931944","title":"Transport of glucose and glycine in Schizosaccharomyces pombe during the cell cycle.","citation":"J Bacteriol 1976 Jul;127(1):109-13","abstract":"Cell growth and uptake of glucose and glycine during the cell cycle were studied in synchronous cultures of Schizosaccharomyces pombe. Rates of accumulation of glucose and glycine were constant during most of the cell cycle, implying a constant rate of cell mass increase. Rates of uptake of glycine appeared to double at an average cell age of 0.9 generations.","authors":"Kubitschek HE, Claymen RV","authors_abbrev":"Kubitschek HE et al.","pubmed_publication_date":"Jul 1976","pubmed_entrez_date":"1976-07-01","publication_year":"1976","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11715017","title":"Mrc1 channels the DNA replication arrest signal to checkpoint kinase Cds1.","citation":"Nat Cell Biol 2001 Nov;3(11):966-72","abstract":"Checkpoint responses change as cells proceed through the cell cycle. Here we describe a novel checkpoint gene in fission yeast, mrc1 (mediator of replication checkpoint), that confers activation of the checkpoint kinase Cds1 to DNA synthesis (S) phase. Mrc1 associates with Cds1 and is required for regulation of Cds1 by the checkpoint kinase Rad3. Mrc1 is regulated by the cell cycle, with the appearance of Mrc1 mRNA and protein coinciding with S phase. We propose that coordinated expression of Mrc1 with replication control proteins helps to ensure activation of the appropriate checkpoint response during DNA replication.","authors":"Tanaka K, Russell P","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2001-11-21","publication_year":"2001","canto_session_key":"75089eca34e16a91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-03-21 14:23:13","canto_approved_date":"2021-10-27 23:23:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-21 14:23:08","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":30,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPCC18B5.11c","SPCC18B5.03","SPBC216.05","SPAC694.06c","SPBC660.14"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2018-03-21"},{"uniquename":"PMID:35234399","title":"[Construction and optimization of ergothioneine-producing  Escherichia coli ].","citation":"Sheng Wu Gong Cheng Xue Bao 2022 Feb 25;38(2):796-806","abstract":"Ergothioneine (ERG) is a natural antioxidant that has been widely used in the fields of food, medicine and cosmetics. Compared with traditional plant extraction and chemical synthesis approaches, microbial synthesis of ergothioneine has many advantages, such as the short production cycle and low cost, and thus has attracted intensive attention. In order to engineer an ergothioneine high-yielding  Escherichia coli  strain, the ergothioneine synthesis gene cluster  egtABCDE  from  Mycobacterium smegmatis  and  egt1  from  Schizosaccharomyces pombe  were introduced into  E. coli  BL21(DE3) to generate a strain E1-A1 harboring the ergothioneine biosynthesis pathway. As a result, (95.58±3.2) mg/L ergothioneine was produced in flask cultures. To further increase ergothioneine yield, the relevant enzymes for biosynthesis of histidine, methionine, and cysteine, the three precursor amino acids of ergothioneine, were overexpressed. Individual overexpression of  serA T410STOP   and  thrA  resulted in an ergothioneine titer of (134.83±4.22) mg/L and (130.26±3.34) mg/L, respectively, while co-overexpression of  serA T410STOP   and  thrA  increased the production of ergothioneine to (144.97±5.40) mg/L. Eventually, by adopting a fed-batch fermentation strategy in 3 L fermenter, the optimized strain E1-A1- thrA-serA  *  produced 548.75 mg/L and 710.53 mg/L ergothioneine in glucose inorganic salt medium and rich medium, respectively.","doi":"10.13345/j.cjb.210166","authors":"Wang L, Wang Y, Li J, DU G, Kang Z","authors_abbrev":"Wang L et al.","pubmed_publication_date":"25 Feb 2022","pubmed_entrez_date":"2022-03-02","publication_year":"2022","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2022-03-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18246107","title":"Once in a lifetime: strategies for preventing re-replication in prokaryotic and eukaryotic cells.","citation":"EMBO Rep 2008 Feb;9(2):151-6","abstract":"DNA replication is an extremely accurate process and cells have evolved intricate control mechanisms to ensure that each region of their genome is replicated only once during S phase. Here, we compare what is known about the processes that prevent re-replication in prokaryotic and eukaryotic cells by using the model organisms Escherichia coli and Schizosaccharomyces pombe as examples. Although the underlying molecular details are different, the logic behind the control mechanisms is similar. For example, after initiation, crucial molecules required for the loading of replicative helicases in both prokaryotes and eukaryotes are inactivated until the next cell cycle. Furthermore, in both systems the beta-clamp of the replicative polymerase associates with enzymatic activities that contribute to the inactivation of the helicase loaders. Finally, recent studies suggest that the control mechanism that prevents re-replication in both systems also increases the synthesis of DNA building blocks.","doi":"10.1038/sj.embor.2008.2","authors":"Nielsen O, Løbner-Olesen A","authors_abbrev":"Nielsen O et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2008-02-05","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20194963","title":"Transformation/transcription domain-associated protein (TRRAP)-mediated regulation of Wee1.","citation":"Genetics 2010 May;185(1):81-93","abstract":"The G2 DNA damage checkpoint inhibits Cdc2 and mitotic entry through the dual regulation of Wee1 and Cdc25 by the Chk1 effector kinase. Upregulation of Chk1 by mutation or overexpression bypasses the requirement for upstream regulators or DNA damage to promote a G2 cell cycle arrest. We screened in fission yeast for mutations that rendered cells resistant to overexpressed chk1(+). We identified a mutation in tra1, which encodes one of two homologs of transformation/transcription domain-associated protein (TRRAP), an ATM/R-related pseudokinase that scaffolds several histone acetyltransferase (HAT) complexes. Inhibition of histone deacetylases reverts the resistance to overexpressed chk1(+), suggesting this phenotype is due to a HAT activity, although expression of checkpoint and cell cycle genes is not greatly affected. Cells with mutant or deleted tra1 activate Chk1 normally and are checkpoint proficient. However, these cells are semi-wee even when overexpressing chk1(+) and accumulate inactive Wee1 protein. The changed division response (Cdr) kinases Cdr1 and Cdr2 are negative regulators of Wee1, and we show that they are required for the Tra1-dependent alterations to Wee1 function. This identifies Tra1 as another component controlling the timing of entry into mitosis via Cdc2 activation.","doi":"10.1534/genetics.110.114769","authors":"Calonge TM, Eshaghi M, Liu J, Ronai Z, O'Connell MJ","authors_abbrev":"Calonge TM et al.","pubmed_publication_date":"May 2010","pubmed_entrez_date":"2010-03-03","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPBP16F5.03c","SPAC57A10.02","SPBC36.05c","SPBC800.03","SPAC3G9.07c","SPAC1783.04c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:36830657","title":"Comparative Research: Regulatory Mechanisms of Ribosomal Gene Transcription in  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe .","citation":"Biomolecules 2023 Feb 03;13(2)","abstract":"Restricting ribosome biosynthesis and assembly in response to nutrient starvation is a universal phenomenon that enables cells to survive with limited intracellular resources. When cells experience starvation, nutrient signaling pathways, such as the target of rapamycin (TOR) and protein kinase A (PKA), become quiescent, leading to several transcription factors and histone modification enzymes cooperatively and rapidly repressing ribosomal genes. Fission yeast has factors for heterochromatin formation similar to mammalian cells, such as H3K9 methyltransferase and HP1 protein, which are absent in budding yeast. However, limited studies on heterochromatinization in ribosomal genes have been conducted on fission yeast. Herein, we shed light on and compare the regulatory mechanisms of ribosomal gene transcription in two species with the latest insights.","doi":"10.3390/biom13020288","authors":"Hirai H, Ohta K","authors_abbrev":"Hirai H et al.","pubmed_publication_date":"03 Feb 2023","pubmed_entrez_date":"2023-02-25","publication_year":"2023","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2023-02-26 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24508166","title":"Dueling kinases regulate cell size at division through the SAD kinase Cdr2.","citation":"Curr Biol 2014 Feb 17;24(4):428-33","abstract":"Cell size control requires mechanisms that integrate cell growth and division. Key to this integration in fission yeast is the SAD family kinase Cdr2, which organizes a set of cortical nodes in the cell middle to promote mitotic entry through Wee1 and Cdk1. Cdr2 is inhibited by a spatial gradient of the DYRK kinase Pom1 emanating from cell tips in a cell-size-dependent manner, but how the Pom1 gradient inhibits Cdr2 activity during cell growth is unknown. Here, we show that Pom1 acts to prevent activation of Cdr2 kinase activity by the CaMKK Ssp1. We found that Ssp1 activates Cdr2 through phosphorylation of a conserved threonine residue (Thr166) in the activation loop of the Cdr2 N-terminal kinase domain both in vitro and in cells. The levels of this activating phosphorylation increased with cell-cycle progression, and genetic epistasis demonstrated that Ssp1 promotes mitotic entry through Cdr2. Intriguingly, Pom1 phosophorylated the C-terminal domain of Cdr2, and this modification reduced Cdr2-T166 phosphorylation by Ssp1. These findings show how activation of the conserved mitotic inducer Cdr2 is integrated with an inhibitory spatial gradient to ensure proper cell size control at mitosis.","doi":"10.1016/j.cub.2014.01.009","authors":"Deng L, Baldissard S, Kettenbach AN, Gerber SA, Moseley JB","authors_abbrev":"Deng L et al.","pubmed_publication_date":"17 Feb 2014","pubmed_entrez_date":"2014-02-11","publication_year":"2014","canto_session_key":"c6be22ca31f0e630","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-04 15:28:34","canto_approved_date":"2026-01-27 16:21:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-23 17:59:11","canto_added_date":"2014-02-16 05:46:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":49,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC144.14","SPAC644.06c","SPBC1A4.05","SPAC57A10.02","SPCC297.03","SPAC2F7.03c","SPCC18B5.03","SPAC24H6.05"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2018-10-04"},{"uniquename":"PMID:16120966","title":"Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2005;33(15):4762-74","abstract":"As predicted by the amino acid sequence, the purified protein coded by Schizosaccharomyces pombe SPAC2F7.06c is a DNA polymerase (SpPol4) whose biochemical properties resemble those of other X family (PolX) members. Thus, this new PolX is template-dependent, polymerizes in a distributive manner, lacks a detectable 3'-->5' proofreading activity and its preferred substrates are small gaps with a 5'-phosphate group. Similarly to Polmu, SpPol4 can incorporate a ribonucleotide (rNTP) into a primer DNA. However, it is not responsible for the 1-2 rNTPs proposed to be present at the mating-type locus and those necessary for mating-type switching. Unlike Polmu, SpPol4 lacks terminal deoxynucleotidyltransferase activity and realigns the primer terminus to alternative template bases only under certain sequence contexts and, therefore, it is less error-prone than Polmu. Nonetheless, the biochemical properties of this gap-filling DNA polymerase are suitable for a possible role of SpPol4 in non-homologous end-joining. Unexpectedly based on sequence analysis, SpPol4 has deoxyribose phosphate lyase activity like Polbeta and Pollambda, and unlike Polmu, suggesting also a role of this enzyme in base excision repair. Therefore, SpPol4 is a unique enzyme whose enzymatic properties are hybrid of those described for mammalian Polbeta, Pollambda and Polmu.","authors":"González-Barrera S, Sánchez A, Ruiz JF, Juárez R, Picher AJ, Terrados G, Andrade P, Blanco L","authors_abbrev":"González-Barrera S et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-08-27","publication_year":"2005","canto_session_key":"cd90915e77803d7f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-01-10 17:04:00","canto_approved_date":"2019-01-10 17:04:01","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-01-10 16:35:04","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-01-10"},{"uniquename":"PMID:9191272","title":"Sxa2, a carboxypeptidase that degrades extracellular pheromone in fission yeast.","citation":"Biochem Soc Trans 1997 May;25(2):228S","abstract":"","authors":"Ladds G, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"d7ecd688fa54e0f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-01-07 11:14:25","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-02-16 22:47:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1296.03c","SPCC1795.06"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-02-16"},{"uniquename":"PMID:9388671","title":"Proteases involved in the maturation of the M-factor mating pheromone in fission yeast.","citation":"Biochem Soc Trans 1997 Aug;25(3):447S","abstract":"","authors":"Hughes M, Davey J","authors_abbrev":"Hughes M et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"7625c252ece8064a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-08 09:22:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-08 09:22:19","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBPJ4664.03","SPAC513.03","SPAPB8E5.05"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2014-08-08"},{"uniquename":"PMID:10899136","title":"Telomere-led bouquet formation facilitates homologous chromosome pairing and restricts ectopic interaction in fission yeast meiosis.","citation":"EMBO J 2000 Jul 17;19(14):3831-40","abstract":"A polarized chromosomal arrangement with clustered telomeres in a meiotic prophase nucleus is often called bouquet and is thought to be important for the pairing of homologous chromosomes. Fluorescence in situ hybridization in fission yeast indicated that chromosomal loci are positioned in an ordered manner as anticipated from the bouquet arrangement. Blocking the formation of the telomere cluster with the kms1 mutation created a disorganized chromosomal arrangement, not only for the regions proximal to the telomere but also for interstitial regions. The kms1 mutation also affected the positioning of a linear minichromosome. Consistent with this cytological observation, the frequency of ectopic homologous recombination between a linear minichromosome and a normal chromosome increased in the kms1 background. Intragenic recombination between allelic loci is reduced in the kms1 mutant, but those between non-allelic loci are unaffected or slightly increased. Thus, telomere-led chromosome organization facilitates homologous pairing and also restricts irregular chromosome pairing during meiosis.","authors":"Niwa O, Shimanuki M, Miki F","authors_abbrev":"Niwa O et al.","pubmed_publication_date":"17 Jul 2000","pubmed_entrez_date":"2000-07-19","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3A11.05c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:32075773","title":"Chaperone-Facilitated Aggregation of Thermo-Sensitive Proteins Shields Them from Degradation during Heat Stress.","citation":"Cell Rep 2020 Feb 18;30(7):2430-2443.e4","abstract":"Cells have developed protein quality-control strategies to manage the accumulation of misfolded substrates during heat stress. Using a soluble reporter of misfolding in fission yeast, Rho1.C17R-GFP, we demonstrate that upon mild heat shock, the reporter collapses in protein aggregate centers (PACs). They contain and/or require several chaperones, such as Hsp104, Hsp16, and the Hsp40/70 couple Mas5/Ssa2. Stress granules do not assemble at mild temperatures and, therefore, are not required for PAC formation; on the contrary, PACs may serve as nucleation centers for the assembly of stress granules. In contrast to the general belief, the dominant fate of these PACs is not degradation, and the aggregated reporter can be disassembled by chaperones and recovers native structure and activity. Using mass spectrometry, we show that thermo-unstable endogenous proteins form PACs as well. In conclusion, formation of PACs during heat shock is a chaperone-mediated adaptation strategy.","doi":"10.1016/j.celrep.2020.01.077","authors":"Cabrera M, Boronat S, Marte L, Vega M, Pérez P, Ayté J, Hidalgo E","authors_abbrev":"Cabrera M et al.","pubmed_publication_date":"18 Feb 2020","pubmed_entrez_date":"2020-02-21","publication_year":"2020","canto_session_key":"9b7a8fcbcc0f3510","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Margarita Cabrera","canto_first_approved_date":"2020-04-29 08:49:20","canto_approved_date":"2022-08-03 09:43:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-07-27 12:38:28","canto_added_date":"2020-02-22 01:15:05","annotation_curators":[{"name":"Margarita Cabrera","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.13","SPBC1347.05c","SPBC3E7.02c","SPAC926.04c","SPBC16D10.08c","SPAC25G10.08","SPBC2A9.04c","SPAC16E8.15","SPAC1F7.04","SPAC24B11.06c","SPAC57A7.12","SPAC57A7.04c","SPAC17C9.03","SPBC1734.11","SPAC13G7.02c","SPAC328.05","SPCC830.07c","SPCC330.05c","SPBC1709.05","SPAC167.07c","SPBC530.03c","SPBC1778.01c"],"gene_count":22,"ltp_gene_count":22,"approved_date":"2020-04-29"},{"uniquename":"PMID:2034223","title":"prp4 from Schizosaccharomyces pombe, a mutant deficient in pre-mRNA splicing isolated using genes containing artificial introns.","citation":"Mol Gen Genet 1991 Apr;226(1-2):305-9","abstract":"We have generated a bank of temperature-sensitive (ts) Schizosaccharomyces pombe mutant strains. About 150 of these mutants were transformed with a ura4 gene containing an artificial intron. We screened these ts mutants for mutants deficient in splicing of the ura4 intron. With this approach three mutants were isolated which have a general defect in the splicing process. Two of these mutants fall into the prp1 complementation group and one defines a new complementation group, prp4.","authors":"Rosenberg GH, Alahari SK, Käufer NF","authors_abbrev":"Rosenberg GH et al.","pubmed_publication_date":"Apr 1991","pubmed_entrez_date":"1991-04-01","publication_year":"1991","canto_session_key":"e9b4e33bc3a69417","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-11-21 16:23:18","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-01-30 15:51:06","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.07","SPCC777.14"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-01-30"},{"uniquename":"PMID:11839823","title":"Formation of a carboxy-terminal domain phosphatase (Fcp1)/TFIIF/RNA polymerase II (pol II) complex in Schizosaccharomyces pombe involves direct interaction between Fcp1 and the Rpb4 subunit of pol II.","citation":"Mol Cell Biol 2002 Mar;22(5):1577-88","abstract":"In transcriptional regulation, RNA polymerase II (pol II) interacts and forms complexes with a number of protein factors. To isolate and identify the pol II-associated proteins, we constructed a Schizosaccharomyces pombe strain carrying a FLAG tag sequence fused to the rpb3 gene encoding the pol II subunit Rpb3. By immunoaffinity purification with anti-FLAG antibody-resin, a pol II complex containing the Rpb1 subunit with a nonphosphorylated carboxyl-terminal domain (CTD) was isolated. In addition to the pol II subunits, the complex was found to contain three subunits of a transcription factor TFIIF (TFIIF alpha, TFIIF beta, and Tfg3) and TFIIF-interacting CTD-phosphatase Fcp1. The same type of pol II complex could also be purified from an Fcp1-tagged strain. The isolated Fcp1 showed CTD-phosphatase activity in vitro. The fcp1 gene is essential for cell viability. Fcp1 and pol II interacted directly in vitro. Furthermore, by chemical cross-linking, glutathione S-transferase pulldown, and affinity chromatography, the Fcp1-interacting subunit of pol II was identified as Rpb4, which plays regulatory roles in transcription. We also constructed an S. pombe thiamine-dependent rpb4 shut-off system. On repression of rpb4 expression, the cell produced more of the nonphosphorylated form of Rpb1, but the pol II complex isolated with the anti-FLAG antibody contained less Fcp1 and more of the phosphorylated form of Rpb1 with a concomitant reduction in Rpb4. This result indicates the importance of Fcp1-Rpb4 interaction for formation of the Fcp1/TFIIF/pol II complex in vivo.","authors":"Kimura M, Suzuki H, Ishihama A","authors_abbrev":"Kimura M et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-02-13","publication_year":"2002","canto_session_key":"ccf56c5e8829b9ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-07-03 07:52:37","canto_approved_date":"2024-04-04 10:52:59","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-01-15 10:42:36","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22H12.02","SPAPYUG7.04c","SPBC28F2.12","SPAC19B12.05c","SPBC19C2.03","SPCC1020.04c","SPAC3A12.07","SPCC1620.09c","SPAC1B3.12c","SPAC23C4.15","SPBC337.14","SPAC23G3.01","SPBC1198.13c","SPBC14C8.12","SPCC1442.10c","SPACUNK4.06c"],"gene_count":16,"ltp_gene_count":15,"approved_date":"2018-07-03"},{"uniquename":"PMID:12934016","title":"Comparing the continuous representation of time-series expression profiles to identify differentially expressed genes.","citation":"Proc Natl Acad Sci U S A 2003 Sep 02;100(18):10146-51","abstract":"We present a general algorithm to detect genes differentially expressed between two nonhomogeneous time-series data sets. As increasing amounts of high-throughput biological data become available, a major challenge in genomic and computational biology is to develop methods for comparing data from different experimental sources. Time-series whole-genome expression data are a particularly valuable source of information because they can describe an unfolding biological process such as the cell cycle or immune response. However, comparisons of time-series expression data sets are hindered by biological and experimental inconsistencies such as differences in sampling rate, variations in the timing of biological processes, and the lack of repeats. Our algorithm overcomes these difficulties by using a continuous representation for time-series data and combining a noise model for individual samples with a global difference measure. We introduce a corresponding statistical method for computing the significance of this differential expression measure. We used our algorithm to compare cell-cycle-dependent gene expression in wild-type and knockout yeast strains. Our algorithm identified a set of 56 differentially expressed genes, and these results were validated by using independent protein-DNA-binding data. Unlike previous methods, our algorithm was also able to identify 22 non-cell-cycle-regulated genes as differentially expressed. This set of genes is significantly correlated in a set of independent expression experiments, suggesting additional roles for the transcription factors Fkh1 and Fkh2 in controlling cellular activity in yeast.","authors":"Bar-Joseph Z, Gerber G, Simon I, Gifford DK, Jaakkola TS","authors_abbrev":"Bar-Joseph Z et al.","pubmed_publication_date":"02 Sep 2003","pubmed_entrez_date":"2003-08-23","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21989386","title":"Nucleosomal organization of replication origins and meiotic recombination hotspots in fission yeast.","citation":"EMBO J 2012 Jan 04;31(1):124-37","abstract":"In Schizosaccharomyces pombe, DNA replication origins (ORIs) and meiotic recombination hotspots lack consensus sequences and show a bias towards mapping to large intergenic regions (IGRs). To explore whether this preference depended on underlying chromatin features, we have generated genome-wide nucleosome profiles during mitosis and meiosis. We have found that meiotic double-strand break sites (DSBs) colocalize with nucleosome-depleted regions (NDRs) and that large IGRs include clusters of NDRs that overlap with almost half of all DSBs. By contrast, ORIs do not colocalize with NDRs and they are regulated independently of DSBs. Physical relocation of NDRs at ectopic loci or modification of their genomic distribution during meiosis was paralleled by the generation of new DSB sites. Over 80% of all meiotic DSBs colocalize with NDRs that are also present during mitosis, indicating that the recombination pattern is largely dependent on constitutive properties of the genome and, to a lesser extent, on the transcriptional profile during meiosis. The organization of ORIs and of DSBs regions in S. pombe reveals similarities and differences relative to Saccharomyces cerevisiae.","doi":"10.1038/emboj.2011.350","authors":"de Castro E, Soriano I, Marín L, Serrano R, Quintales L, Antequera F","authors_abbrev":"de Castro E et al.","pubmed_publication_date":"04 Jan 2012","pubmed_entrez_date":"2011-10-13","publication_year":"2012","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21767457","title":"DNA topoisomerase 2 mutant allele mildly delays the mitotic progression and activates the checkpoint protein kinase Chk1 in fission yeast Schizosaccharomyces pombe.","citation":"Genet Res (Camb) 2011 Aug;93(4):275-83","abstract":"DNA topoisomerases are specialized nuclear enzymes that perform topological modifications on double-stranded DNA (dsDNA) and hence are essential for DNA metabolism such as replication, transcription, recombination, condensation and segregation. In a genetic screen, we identified a temperature-sensitive mutant allele of topoisomerase 2 that exhibits conditional synthetic lethality with a chk1 knockout strain. The mutant allele of topoisomerase 2 is defective in chromosome segregation at a non-permissive temperature and there was increase in chromosome segregation defects in the double mutant of top2-10 and chk1 delete at a non-permissive temperature. More importantly, topoisomearse 2 mutant cells mildly delay the mitotic progression at non-permissive temperature that is mediated by checkpoint protein kinase Chk1. Additionally, top2-10 mutant cells also activate the Chk1 at a non-permissive temperature and this activation of Chk1 takes place at the time of mitosis. Interestingly, top2-10 mutant cells retain their viability at a non-permissive temperature if the cells are not allowed to enter into mitosis. Taking together our results, we speculate that in the top2-10 mutant, the segregation of entangled chromatids during mitosis could result in delaying the mitotic progression through the activation of Chk1 kinase.","doi":"10.1017/S0016672311000188","authors":"Yadav S, Verma SK, Ahmed S","authors_abbrev":"Yadav S et al.","pubmed_publication_date":"Aug 2011","pubmed_entrez_date":"2011-07-20","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1A4.03c","SPCC1259.13"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:21879336","title":"Multistep regulation of protein kinase A in its localization, phosphorylation and binding with a regulatory subunit in fission yeast.","citation":"Curr Genet 2011 Oct;57(5):353-65","abstract":"The cAMP-PKA is the major glucose-sensing pathway that controls sexual differentiation in Schizosaccharomyces pombe. Sequencing from the pka1 locus of recessive sam mutants, in which cells are highly inclined to sexual differentiation, led to the identification of mutations in the pka1 locus in sam5 (pka1-G441E) and sam7 (pka1-G441R). Rst2 and Ste11 proteins were induced and localized to the nucleus of sam5 and sam7 mutants even under rich glucose conditions, indicating that the function of Pka1 was completely abolished by mutations. Pka1-G441E and Pka1-G441R mutant proteins reside in the cytoplasm, even under glucose-rich conditions, while wild-type Pka1 resides in the nucleus, indicating that the functionality of Pka1 is important for its nuclear localization. This is supported by the observation that the Pka1-T356A mutant, which partially lacks Pka1 function, was localized to both the cytoplasm and the nucleus, but an active phosphomimetic Pka1-T356D mutant prtotein was localized to the nucleus under glucose-rich conditions. In addition to the basal phosphorylation of Pka1 at T356, hyperphosphorylation of Pka1 was observed under glucose-starved conditions, and such hyperphosphorylation was not observed in pka1-G441E, pka1-G441R, pka1-T356A or pka1-T356D mutants. As these mutant proteins failed to interact with a regulatory subunit Cgs1, hyperphosphorylation of Pka1 mutant proteins was considered to be dependent on Cgs1 interaction. Consistent with a role for Cgs1 in Pka1 phosphorylation, we detected the formation of a Cgs1-Pka1 complex prior to Pka1 hyperphosphorylation. Together, these results indicate that nuclear localization of Pka1 depends on its activity and hyperphosphorylation of Pka1 depends on Cgs1 interaction.","doi":"10.1007/s00294-011-0354-2","authors":"Gupta DR, Paul SK, Oowatari Y, Matsuo Y, Kawamukai M","authors_abbrev":"Gupta DR et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-09-01","publication_year":"2011","canto_session_key":"60d1480f79c0c05b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-06 12:13:29","canto_approved_date":"2026-05-13 12:05:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-22 14:13:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":42,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.02","SPBC106.10","SPAC8C9.03","SPBC32C12.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-02-06"},{"uniquename":"PMID:8586261","title":"Identification of 24-methylene-24,25-dihydrolanosterol as a precursor of ergosterol in the yeasts Schizosaccharomyces pombe and Schizosaccharomyces octosporus.","citation":"FEMS Microbiol Lett 1995 Dec 15;134(2-3):147-52","abstract":"Study of the plasma membrane sterol composition in the yeasts Schizosaccharomyces pombe and Schizosaccharomyces octosporus revealed the presence of ergosterol, lanosterol, dehydroergosterol, fecosterol, episterol and 24-methylene-24,25-dihydrolanosterol (eburicol), a C-31 derivative. The growth of both yeasts in the presence of ketoconazole led to a decrease by 85% of the ergosterol content while the levels of lanosterol and eburicol increased. This suggests that in the biosynthetic pathway of ergosterol in Schizosaccharomyces species, the transmethylation process on the C-24 may occur directly on lanosterol and not only on zymosterol. On the other hand, it cannot be excluded that in the genus Schizosaccharomyces two routes exist from lanosterol to ergosterol: the classical one via a direct C-14, C-4 demethylation of lanosterol and the second one via the formation of a C-31 derivative followed by demethylations.","authors":"Harmouch N, Coulon J, Bonaly R","authors_abbrev":"Harmouch N et al.","pubmed_publication_date":"15 Dec 1995","pubmed_entrez_date":"1995-12-15","publication_year":"1995","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10573846","title":"Dynamic confocal imaging of interphase and mitotic microtubules in the fission yeast, S. pombe.","citation":"Biol Bull 1999 Oct;197(2):262-3","abstract":"","authors":"Tran PT, Maddox P, Chang F, Inoué S","authors_abbrev":"Tran PT et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"1999-11-26","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21071413","title":"The BioGRID Interaction Database: 2011 update.","citation":"Nucleic Acids Res 2011 Jan;39(Database issue):D698-704","abstract":"The Biological General Repository for Interaction Datasets (BioGRID) is a public database that archives and disseminates genetic and protein interaction data from model organisms and humans (http://www.thebiogrid.org). BioGRID currently holds 347,966 interactions (170,162 genetic, 177,804 protein) curated from both high-throughput data sets and individual focused studies, as derived from over 23,000 publications in the primary literature. Complete coverage of the entire literature is maintained for budding yeast (Saccharomyces cerevisiae), fission yeast (Schizosaccharomyces pombe) and thale cress (Arabidopsis thaliana), and efforts to expand curation across multiple metazoan species are underway. The BioGRID houses 48,831 human protein interactions that have been curated from 10,247 publications. Current curation drives are focused on particular areas of biology to enable insights into conserved networks and pathways that are relevant to human health. The BioGRID 3.0 web interface contains new search and display features that enable rapid queries across multiple data types and sources. An automated Interaction Management System (IMS) is used to prioritize, coordinate and track curation across international sites and projects. BioGRID provides interaction data to several model organism databases, resources such as Entrez-Gene and other interaction meta-databases. The entire BioGRID 3.0 data collection may be downloaded in multiple file formats, including PSI MI XML. Source code for BioGRID 3.0 is freely available without any restrictions.","doi":"10.1093/nar/gkq1116","authors":"Stark C, Breitkreutz BJ, Chatr-Aryamontri A, Boucher L, Oughtred R, Livstone MS, Nixon J, Van Auken K, Wang X, Shi X, Reguly T, Rust JM, Winter A, Dolinski K, Tyers M","authors_abbrev":"Stark C et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-11-13","publication_year":"2011","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23121505","title":"Is oxidized thioredoxin a major trigger for cysteine oxidation? Clues from a redox proteomics approach.","citation":"Antioxid Redox Signal 2013 May 01;18(13):1549-56","abstract":"Cysteine oxidation mediates oxidative stress toxicity and signaling. It has been long proposed that the thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (Trr), is not only involved in recycling classical Trx substrates, such as ribonucleotide reductase, but it also regulates general cytoplasmic thiol homeostasis. To investigate such a role, we have performed a proteome-wide analysis of cells expressing or not the two components of the Trx system. We have compared the reversibly oxidized thiol proteomes of wild-type Schizosaccharomyces pombe cells with mutants lacking Trx or Trr. Specific Trx substrates are reversibly-oxidized in both strain backgrounds; however, in the absence of Trr, Trx can weakly recycle its substrates at the expense of an alternative electron donor. A massive thiol oxidation occurs only in cells lacking Trr, with 30% of all cysteine-containing peptides being reversibly oxidized; this oxidized cysteine proteome depends on the presence of Trxs. Our observations lead to the hypothesis that, in the absence of its reductase, the natural electron donor Trx becomes a powerful oxidant and triggers general thiol oxidation.","doi":"10.1089/ars.2012.5037","authors":"García-Santamarina S, Boronat S, Calvo IA, Rodríguez-Gabriel M, Ayté J, Molina H, Hidalgo E","authors_abbrev":"García-Santamarina S et al.","pubmed_publication_date":"01 May 2013","pubmed_entrez_date":"2012-11-06","publication_year":"2013","canto_session_key":"0fa7d4f9eab40c0b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3F6.03","SPAC7D4.07c","SPCC576.03c","SPBC577.08c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:10459013","title":"Sid2p, a spindle pole body kinase that regulates the onset of cytokinesis.","citation":"J Cell Biol 1999 Aug 23;146(4):777-90","abstract":"The fission yeast Schizosaccharomyces pombe divides by medial fission through the use of an actomyosin contractile ring. Precisely at the end of anaphase, the ring begins to constrict and the septum forms. Proper coordination of cell division with mitosis is crucial to ensure proper segregation of chromosomes to daughter cells. The Sid2p kinase is one of several proteins that function as part of a novel signaling pathway required for initiation of medial ring constriction and septation. Here, we show that Sid2p is a component of the spindle pole body at all stages of the cell cycle and localizes transiently to the cell division site during medial ring constriction and septation. A medial ring and an intact microtubule cytoskeleton are required for the localization of Sid2p to the division site. We have established an in vitro assay for measuring Sid2p kinase activity, and found that Sid2p kinase activity peaks during medial ring constriction and septation. Both Sid2p localization to the division site and activity depend on the function of all of the other septation initiation genes: cdc7, cdc11, cdc14, sid1, spg1, and sid4. Thus, Sid2p, a component of the spindle pole body, by virtue of its transient localization to the division site, appears to determine the timing of ring constriction and septum delivery in response to activating signals from other Sid gene products.","authors":"Sparks CA, Morphew M, McCollum D","authors_abbrev":"Sparks CA et al.","pubmed_publication_date":"23 Aug 1999","pubmed_entrez_date":"1999-08-25","publication_year":"1999","canto_session_key":"1a9429aa838169ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-09 17:08:21","canto_approved_date":"2024-09-25 13:51:06","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-04-20 15:31:22","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPAC24B11.11c","SPAC1565.06c","SPAC20G8.05c","SPBC244.01c","SPAC9G1.09","SPBC24C6.07","SPBC21.06c","SPAC4A8.15c","SPBC26H8.07c","SPCC1739.11c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2016-10-09"},{"uniquename":"PMID:21360734","title":"Quantitative analysis of yeast internal architecture using soft X-ray tomography.","citation":"Yeast 2011 Mar;28(3):227-36","abstract":"We used soft X-ray tomography (SXT)--a high-resolution, quantitative imaging technique--to measure cell size and organelle volumes in yeasts. Cell size is a key factor in initiating cell division in yeasts, whereas the number and volume of the organelles have a profound impact on the function and viability of a cell. Consequently, determining these cell parameters is fundamentally important in understanding yeast biology. SXT is well suited to this type of analysis. Specimens are imaged in a near-native state, and relatively large numbers of cells can be readily analysed. In this study, we characterized haploid and diploid strains of Saccharomyces cerevisiae at each of the key stages in the cell cycle and determined the relationships that exist cellular and organelle volumes. We then compared these results with SXT data obtained from Schizosaccharomyces pombe, the three main phenotypes displayed by the opportunistic yeast pathogen Candida albicans and from a coff1-22 mutant strain of S. cerevisiae. This comparison revealed that volumetric ratios were invariant, irrespective of yeast strain, ploidy or morphology, leading to the conclusion these volumetric ratios are common in all yeasts.","doi":"10.1002/yea.1834","authors":"Uchida M, Sun Y, McDermott G, Knoechel C, Le Gros MA, Parkinson D, Drubin DG, Larabell CA","authors_abbrev":"Uchida M et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-03-02","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41413653","title":"Phase separation drives cortical enrichment of the F-BAR proteins Rga7 and Rga8 to maintain cell integrity.","citation":"Cell Mol Life Sci 2025 Dec 19;82(1):442","abstract":"Polarized cell growth necessitates the dynamic remodeling of the plasma membrane, a process requiring BAR domain-containing proteins. While classical BAR proteins, with their crescent-shaped structure, are well characterized, the mechanisms underlying the localization and function of elongated F-BAR proteins remain unclear. Here, we demonstrate that the F-BAR domains of the fission yeast proteins Rga7 and Rga8 undergo liquid-liquid phase separation (LLPS). These domains form oligomers via hydrophobic interactions and assemble into condensates through electrostatic interactions mediated by the charged residues at their tips. Mutants deficient in phase separation fail to localize properly at cell poles, leading to defective polar distribution of key regulators, including the Rho GTPases, the exocyst complex, and glucan synthases, all crucial for maintaining cell integrity. We further show that Rga8 requires the actin transport system for tip localization, whereas Rga7 accumulates at cell tips via diffusion. The absence of both Rga7 and Rga8 causes cell lysis. Hence, our findings establish LLPS as a fundamental mechanism for the cortical accumulation and function of F-BAR proteins, providing new insights into their role in membrane dynamics.","doi":"10.1007/s00018-025-05977-2","authors":"Zheng B, Wei W, Zhang X, Wang L, Liu X, Song X, Xiang S, Xu C, Wang C, Lin Y, Zheng S, Fu C","authors_abbrev":"Zheng B et al.","pubmed_publication_date":"19 Dec 2025","pubmed_entrez_date":"2025-12-18","publication_year":"2025","canto_session_key":"fc12136458bdcc3c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-12-20 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7806241","title":"An algorithm to detect chimeric clones and random noise in genomic mapping.","citation":"Genomics 1994 Jul 15;22(2):482-6","abstract":"Experimental noise and noncontiguous clone inserts can pose serious problems in reconstructing genomic maps from hybridization data. We describe an algorithm that easily identifies false positive signals and clones containing chimeric inserts/internal deletions. The algorithm \"dechimerizes\" clones, splitting them into independent contiguous components and cleaning the initial library into a more consistent data set for further ordering. The effectiveness of the algorithm is demonstrated on both simulated data and the real YAC map of the whole genome of the fission yeast Schizosaccharomyces pombe.","authors":"Grigoriev A, Mott R, Lehrach H","authors_abbrev":"Grigoriev A et al.","pubmed_publication_date":"15 Jul 1994","pubmed_entrez_date":"1994-07-15","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20980623","title":"A novel role of Dma1 in regulating forespore membrane assembly and sporulation in fission yeast.","citation":"Mol Biol Cell 2010 Dec;21(24):4349-60","abstract":"In fission yeast Schizosaccharomyces pombe, a diploid mother cell differentiates into an ascus containing four haploid ascospores following meiotic nuclear divisions, through a process called sporulation. Several meiosis-specific proteins of fission yeast have been identified to play essential roles in meiotic progression and sporulation. We report here an unexpected function of mitotic spindle checkpoint protein Dma1 in proper spore formation. Consistent with its function in sporulation, expression of dma1(+) is up-regulated during meiosis I and II. We showed that Dma1 localizes to the SPB during meiosis and the maintenance of this localization at meiosis II depends on septation initiation network (SIN) scaffold proteins Sid4 and Cdc11. Cells lacking Dma1 display defects associated with sporulation but not nuclear division, leading frequently to formation of asci with fewer spores. Our genetic analyses support the notion that Dma1 functions in parallel with the meiosis-specific Sid2-related protein kinase Slk1/Mug27 and the SIN signaling during sporulation, possibly through regulating proper forespore membrane assembly. Our studies therefore revealed a novel function of Dma1 in regulating sporulation in fission yeast.","doi":"10.1091/mbc.E10-01-0079","authors":"Li WZ, Yu ZY, Ma PF, Wang Y, Jin QW","authors_abbrev":"Li WZ et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-10-29","publication_year":"2010","canto_session_key":"8c12b3f9cea0dcc2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Quan-wen Jin","canto_first_approved_date":"2020-02-18 12:20:35","canto_approved_date":"2024-06-26 10:10:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-07 09:06:19","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Quan-wen Jin","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPAC23C11.16","SPCC417.06c","SPBC21.06c","SPBC428.13c","SPAC607.10","SPAC9G1.09","SPAC1565.06c","SPAC17G8.10c","SPAC1F3.06c","SPCC1739.11c","SPBC244.01c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2020-02-18"},{"uniquename":"PMID:10915874","title":"DNA damage and cell cycle control in Schizosaccharomyces pombe.","citation":"Mutat Res 2000 Jun 30;451(1-2):211-26","abstract":"","authors":"Humphrey T","authors_abbrev":"Humphrey T","pubmed_publication_date":"30 Jun 2000","pubmed_entrez_date":"2000-08-01","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28476860","title":"An Evolutionary Perspective on Yeast Mating-Type Switching.","citation":"Genetics 2017 May;206(1):9-32","abstract":"Cell differentiation in yeast species is controlled by a reversible, programmed DNA-rearrangement process called mating-type switching. Switching is achieved by two functionally similar but structurally distinct processes in the budding yeast  Saccharomyces cerevisiae  and the fission yeast  Schizosaccharomyces pombe  In both species, haploid cells possess one active and two silent copies of the mating-type locus (a three-cassette structure), the active locus is cleaved, and synthesis-dependent strand annealing is used to replace it with a copy of a silent locus encoding the opposite mating-type information. Each species has its own set of components responsible for regulating these processes. In this review, we summarize knowledge about the function and evolution of mating-type switching components in these species, including mechanisms of heterochromatin formation,  MAT  locus cleavage, donor bias, lineage tracking, and environmental regulation of switching. We compare switching in these well-studied species to others such as  Kluyveromyces lactis  and the methylotrophic yeasts  Ogataea polymorpha  and  Komagataella phaffii  We focus on some key questions: Which cells switch mating type? What molecular apparatus is required for switching? Where did it come from? And what is the evolutionary purpose of switching?","doi":"10.1534/genetics.117.202036","authors":"Hanson SJ, Wolfe KH","authors_abbrev":"Hanson SJ et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2017-05-07","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-05-11 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22426216","title":"Interpolar microtubules are dispensable in fission yeast meiosis II.","citation":"Nat Commun 2012 Feb 28;3:695","abstract":"The mitotic spindle consists of two types of microtubules. Dynamic kinetochore microtubules capture kinetochores, whereas stable interpolar microtubules serve as the structural backbone that connects the two spindle poles. Both have been believed to be indispensable for cell division in eukaryotes. Here we demonstrate that interpolar microtubules are dispensable for the second division of meiosis in fission yeast. Even when interpolar microtubules are disrupted by a microtubule-depolymerizing drug, spindle poles separate and chromosomes segregate poleward in second division of meiosis in most zygotes, producing viable spores. The forespore membrane, which encapsulates the nucleus in second division of meiosis and is guided by septins and the leading-edge proteins, is responsible for carrying out meiotic events in the absence of interpolar microtubules. Furthermore, during physiological second division of meiosis without microtubule perturbation, the forespore membrane assembly contributes structurally to spindle pole separation and nuclear division, generating sufficient force for spindle pole separation and subsequent events independently of interpolar microtubules.","doi":"10.1038/ncomms1725","authors":"Akera T, Sato M, Yamamoto M","authors_abbrev":"Akera T et al.","pubmed_publication_date":"28 Feb 2012","pubmed_entrez_date":"2012-03-20","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084877","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19A8.16"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:31462441","title":"The PHD finger of Spp1 mediates histone modification cross-talk.","citation":"Biochem J 2019 Aug 28;476(16):2351-2354","abstract":"Binding of the Spp1 PHD finger to histone H3K4me3 is sensitive to adjacent post-translational modifications in the histone tail. This commentary discusses the findings of He and colleagues [ Biochem. J.  476 , 1957-1973] which show that the PHD finger binds to H3K4me3 in a selective manner which is conserved in the  Saccharomyces pombe  and mammalian orthologues of Spp1.","doi":"10.1042/BCJ20190492","authors":"Musselman CA, Kutateladze TG","authors_abbrev":"Musselman CA et al.","pubmed_publication_date":"28 Aug 2019","pubmed_entrez_date":"2019-08-30","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-08-31 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733417","title":"Analysis of  Schizosaccharomyces pombe  Meiosis.","citation":"Cold Spring Harb Protoc 2017 Sep 01;2017(9):pdb.top079855","abstract":"Meiosis is a specialized cell cycle that generates haploid gametes from diploid cells. The fission yeast  Schizosaccharomyces pombe  is one of the best model organisms for studying the regulatory mechanisms of meiosis.  S. pombe  cells, which normally grow in the haploid state, diploidize by conjugation and initiate meiosis when starved for nutrients, especially nitrogen. Following two rounds of chromosome segregation, spore formation takes place. The switch from mitosis to meiosis is controlled by a kinase, Pat1, and an RNA-binding protein, Mei2. Mei2 is also a key factor for meiosis-specific gene expression. Studies on  S. pombe  have offered insights into cell cycle regulation and chromosome segregation during meiosis. Here we outline the current understanding of the molecular mechanisms regulating the initiation and progression of meiosis, and introduce methods for the study of meiosis in fission yeast.","doi":"10.1101/pdb.top079855","authors":"Yamashita A, Sakuno T, Watanabe Y, Yamamoto M","authors_abbrev":"Yamashita A et al.","pubmed_publication_date":"01 Sep 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ632009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.43"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21103458","title":"Fast microfluidic temperature control for high resolution live cell imaging.","citation":"Lab Chip 2011 Feb 07;11(3):484-9","abstract":"One major advantage of using genetically tractable model organisms such as the fission yeast Schizosaccharomyces pombe is the ability to construct temperature-sensitive mutations in a gene. The resulting gene product or protein behaves as wildtype at permissive temperatures. At non-permissive or restrictive temperatures the protein becomes unstable and some or all of its functions are abrogated. The protein regains its function when returning to a permissive temperature. In principle, temperature-sensitive mutation enables precise temporal control of protein activity when coupled to a fast temperature controller. Current commercial temperature control devices do not have fast switching capability over a wide range of temperatures, making repeated temperature changes impossible or impractical at the cellular timescale of seconds or minutes. Microfabrication using soft-lithography is emerging as a powerful tool for cell biological research. We present here a simple disposable polydimethylsiloxane (PDMS) based microfluidic device capable of reversibly switching between 5 °C and 45 °C in less than 10 s. This device allows high-resolution live cell imaging with an oil immersion objective lens. We demonstrate the utility of this device for studying microtubule dynamics throughout the cell cycle.","doi":"10.1039/c0lc00222d","authors":"Velve Casquillas G, Fu C, Le Berre M, Cramer J, Meance S, Plecis A, Baigl D, Greffet JJ, Chen Y, Piel M, Tran PT","authors_abbrev":"Velve Casquillas G et al.","pubmed_publication_date":"07 Feb 2011","pubmed_entrez_date":"2010-11-25","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17312948","title":"Gene structure and biochemical characterization of mitochondrial single-stranded DNA binding protein from Schizosaccharomyces pombe.","citation":"DNA Seq 2006 Aug;17(4):287-91","abstract":"We studied the genomic structure and biochemical properties of Schizosaccharomyces pombe mitochondrial single-stranded DNA binding protein (mtSSB). We first determined the full-length cDNA sequence of mtSSB and clarified the exon/intron structure of the mtSSB gene (rim1), including the transcription initiation and polyadenylation sites. The cDNA of rim1 gene encoded 150 amino acids and the sequence showed homology to eukaryotic mtSSB and Escherichia coli SSB. We overexpressed mtSSB as a His-tag fusion protein in E. coli and obtained an anti-mtSSB antibody. Gel filtration analysis of S. pombe cell extracts clarified that mtSSB has a tetrameric structure. We also immunochemically detected mtSSB in S. pombe cell extract and showed that 15,000 molecules of mtSSB tetramer are present in a single S. pombe cell. Mature mtSSB lacking the presequence was overexpressed in E. coli in tetrameric soluble form. The recombinant mtSSB bound a single-stranded oligonucleotide and phiX174 virion DNA with almost identical binding activity as E. coli SSB.","authors":"Nishio M, Seki Y, Ikeda S","authors_abbrev":"Nishio M et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2007-02-23","publication_year":"2006","canto_session_key":"7902257bba065fc1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-06 08:09:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 09:33:23","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F3.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-05"},{"uniquename":"EMBL:AU011152","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34765162","title":"Competition dynamics in long-term propagations of  Schizosaccharomyces pombe  strain communities.","citation":"Ecol Evol 2021 Nov;11(21):15085-15097","abstract":"Experimental evolution studies with microorganisms such as bacteria and yeast have been an increasingly important and powerful tool to draw long-term inferences of how microbes interact. However, while several strains of the same species often exist in natural environments, many ecology and evolution studies in microbes are typically performed with isogenic populations of bacteria or yeast. In the present study, we firstly perform a genotypic and phenotypic characterization of two laboratory and eight natural strains of the yeast  Schizosaccharomyces pombe . We then propagated, in a rich resource environment, yeast communities of 2, 3, 4, and 5 strains for hundreds of generations and asked which fitness-related phenotypes-maximum growth rate or relative competitive fitness-would better predict the outcome of a focal strain during the propagations. While the strain's growth rates would wrongly predict long-term coexistence, pairwise competitive fitness with a focal strain qualitatively predicted the success or extinction of the focal strain by a simple multigenotype population genetics model, given the initial community composition. Interestingly, we have also measured the competitive fitness of the ancestral and evolved communities by the end of the experiment (≈370 generations) and observed frequent maladaptation to the abiotic environment in communities with more than three members. Overall, our results aid establishing pairwise competitive fitness as good qualitative measurement of long-term community composition but also reveal a complex adaptive scenario when trying to predict the evolutionary outcome of those communities.","doi":"10.1002/ece3.8191","authors":"Durão P, Amicone M, Perfeito L, Gordo I","authors_abbrev":"Durão P et al.","pubmed_publication_date":"Nov 2021","pubmed_entrez_date":"2021-11-12","publication_year":"2021","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-11-17 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19242681","title":"Gene transfer and protein release of fission yeast by application of a high voltage electric pulse.","citation":"Anal Bioanal Chem 2009 May;394(1):13-6","abstract":"A high voltage electric pulse can be applied to induce the uptake of DNA into cells and the release of protein from cells. In transformation procedures, electroporation is widely used since the technique is simple, rapid, reproducible, and highly efficient. In extraction of protein, on the other hand, electroextraction has many advantages over other conventional extractions. We have developed a highly efficient method for the electroporation of fission yeast. In particular, application of a high voltage electric pulse to fission yeast improves the cellular uptake and release of macromolecules controlled by both osmotic conditions and electric field strength.","doi":"10.1007/s00216-009-2678-z","authors":"Suga M, Hatakeyama T","authors_abbrev":"Suga M et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-02-27","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:L34882","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11971984","title":"The Schizosaccharomyces pombe rad60 gene is essential for repairing double-strand DNA breaks spontaneously occurring during replication and induced by DNA-damaging agents.","citation":"Mol Cell Biol 2002 May;22(10):3537-48","abstract":"To identify novel genes involved in DNA double-strand break (DSB) repair, we previously isolated Schizosaccharomyces pombe mutants which are hypersensitive to methyl methanesulfonate (MMS) and synthetic lethals with rad2. This study characterizes one of these mutants, rad60-1. The gene that complements the MMS sensitivity of this mutant was cloned and designated rad60. rad60 encodes a protein with 406 amino acids which has the conserved ubiquitin-2 motif found in ubiquitin family proteins. rad60-1 is hypersensitive to UV and gamma rays, epistatic to rhp51, and defective in the repair of DSBs caused by gamma-irradiation. The rad60-1 mutant is also temperature sensitive for growth. At the restrictive temperature (37 degrees C), rad60-1 cells grow for several divisions and then arrest with 2C DNA content; the arrested cells accumulate DSBs and have a diffuse and often aberrantly shaped nuclear chromosomal domain. The rad60-1 mutant is a synthetic lethal with rad18-X, and expression of wild-type rad60 from a multicopy plasmid partially suppresses the MMS sensitivity of rad18-X cells. rad18 encodes a conserved protein of the structural maintenance of chromosomes (SMC) family (A. R. Lehmann, M. Walicka, D. J. Griffiths, J. M. Murray, F. Z. Watts, S. McCready, and A. M. Carr, Mol. Cell. Biol. 15:7067-7080, 1995). These results suggest that S. pombe Rad60 is required to repair DSBs, which accumulate during replication, by recombination between sister chromatids. Rad60 may perform this function in concert with the SMC protein Rad18.","authors":"Morishita T, Tsutsui Y, Iwasaki H, Shinagawa H","authors_abbrev":"Morishita T et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-04-25","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1921.02","SPBC1734.06","SPAC3G6.06c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:30270044","title":"Protein AMPylation by an Evolutionarily Conserved Pseudokinase.","citation":"Cell 2018 Oct 18;175(3):809-821.e19","abstract":"Approximately 10% of human protein kinases are believed to be inactive and named pseudokinases because they lack residues required for catalysis. Here, we show that the highly conserved pseudokinase selenoprotein-O (SelO) transfers AMP from ATP to Ser, Thr, and Tyr residues on protein substrates (AMPylation), uncovering a previously unrecognized activity for a member of the protein kinase superfamily. The crystal structure of a SelO homolog reveals a protein kinase-like fold with ATP flipped in the active site, thus providing a structural basis for catalysis. SelO pseudokinases localize to the mitochondria and AMPylate proteins involved in redox homeostasis. Consequently, SelO activity is necessary for the proper cellular response to oxidative stress. Our results suggest that AMPylation may be a more widespread post-translational modification than previously appreciated and that pseudokinases should be analyzed for alternative transferase activities.","doi":"10.1016/j.cell.2018.08.046","authors":"Sreelatha A, Yee SS, Lopez VA, Park BC, Kinch LN, Pilch S, Servage KA, Zhang J, Jiou J, Karasiewicz-Urbańska M, Łobocka M, Grishin NV, Orth K, Kucharczyk R, Pawłowski K, Tomchick DR, Tagliabracci VS","authors_abbrev":"Sreelatha A et al.","pubmed_publication_date":"18 Oct 2018","pubmed_entrez_date":"2018-10-02","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G4.05c","SPAC4F10.20"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:20015079","title":"From meiosis to postmeiotic events: uncovering the molecular roles of the meiosis-specific recombinase Dmc1.","citation":"FEBS J 2010 Feb;277(3):590-8","abstract":"In meiosis, the accurate segregation of maternal and paternal chromosomes is accomplished by homologous recombination. A central player in meiotic recombination is the Dmc1 recombinase, a member of the RecA/Rad51 recombinase superfamily, which is widely conserved from viruses to humans. Dmc1 is a meiosis-specific protein that functions with the ubiquitously expressed homolog, the Rad51 recombinase, which is essential for both mitotic and meiotic recombination. Since its discovery, it has been speculated that Dmc1 is important for unique aspects of meiotic recombination. Understanding the distinctive properties of Dmc1, namely, the features that distinguish it from Rad51, will further clarify the mechanisms of meiotic recombination. Recent structural, biochemical, and genetic findings are now revealing the molecular mechanisms of Dmc1-mediated homologous recombination and its regulation by various recombination mediators.","doi":"10.1111/j.1742-4658.2009.07503.x","authors":"Kagawa W, Kurumizaka H","authors_abbrev":"Kagawa W et al.","pubmed_publication_date":"Feb 2010","pubmed_entrez_date":"2009-12-18","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37328480","title":"Chromatin remodeling by Pol II primes efficient Pol III transcription.","citation":"Nat Commun 2023 Jun 16;14(1):3587","abstract":"The packaging of the genetic material into chromatin imposes the remodeling of this barrier to allow efficient transcription. RNA polymerase II activity is coupled with several histone modification complexes that enforce remodeling. How RNA polymerase III (Pol III) counteracts the inhibitory effect of chromatin is unknown. We report here a mechanism where RNA Polymerase II (Pol II) transcription is required to prime and maintain nucleosome depletion at Pol III loci and contributes to efficient Pol III recruitment upon re-initiation of growth from stationary phase in Fission yeast. The Pcr1 transcription factor participates in the recruitment of Pol II, which affects local histone occupancy through the associated SAGA complex and a Pol II phospho-S2 CTD / Mst2 pathway. These data expand the central role of Pol II in gene expression beyond mRNA synthesis.","doi":"10.1038/s41467-023-39387-4","authors":"Yague-Sanz C, Migeot V, Larochelle M, Bachand F, Wéry M, Morillon A, Hermand D","authors_abbrev":"Yague-Sanz C et al.","pubmed_publication_date":"16 Jun 2023","pubmed_entrez_date":"2023-06-16","publication_year":"2023","canto_session_key":"6d39e63b44a9b7c2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-06-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6717440","title":"High-frequency cotransformation by copolymerization of plasmids in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1984 Apr;4(4):651-6","abstract":"We have developed a high-frequency cotransformation system which is useful in introducing nonreplicating circular DNA plasmids into the fission yeast Schizosaccharomyces pombe. This system depends on two factors: the ability of the ural-complementing helper plasmids pFYM2 and pFYM225 to propagate autonomously in S. pombe, and the intensive recombination activity intrinsic to this yeast. If cotransformed with a helper plasmid, plasmids such as YIp5 or YIp32, Escherichia coli-Saccharomyces cerevisiae shuttle vectors incapable of replication in S. pombe, can enter S. pombe and express the gene carried on them at a frequency comparable to that of autonomously replicating plasmids (10(3) to 10(4) transformants per microgram of DNA). Even if characters of the nonreplicating DNA are not selected directly, 50 to 70% of Ura+ cells transformed with the helper have also incorporated the nonreplicating plasmid. It is shown that these two plasmids have physically recombined at a site of common DNA sequence to form a heteropolymer in the fission yeast. Since any foreign DNA cloned in pBR322 or ColE1 derivatives can be incorporated into S. pombe by using pFYM2 or pFYM225 as a helper, this cotransformation system will serve as a convenient method to examine functional expression of such cloned DNA in S. pombe. This work also demonstrates that the kanamycin resistance gene carried by the bacterial transposon Tn903 can be expressed in S. pombe, as shown by its ability to inactivate the antibiotic G418.","authors":"Sakai K, Sakaguchi J, Yamamoto M","authors_abbrev":"Sakai K et al.","pubmed_publication_date":"Apr 1984","pubmed_entrez_date":"1984-04-01","publication_year":"1984","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9488484","title":"Isolation, characterization, and molecular cloning of a protein (Abp2) that binds to a Schizosaccharomyces pombe origin of replication (ars3002).","citation":"Mol Cell Biol 1998 Mar;18(3):1670-81","abstract":"The autonomously replicating sequence (ARS) element ars3002 is associated with the most active replication origin within a cluster of three closely spaced origins on chromosome III of Schizosaccharomyces pombe. A 361-bp portion of ars3002 containing detectable ARS activity includes multiple near matches to the S. pombe ARS consensus sequence previously reported by Maundrell et al. (K. Maundrell, A. Hutchison, and S. Shall, EMBO J. 7:2203-2209, 1988). Using a gel shift assay with a multimer of an oligonucleotide containing three overlapping matches to the Maundrell ARS consensus sequence, we have detected several proteins in S. pombe crude extracts that bind to the oligonucleotide and ars3002. One of these proteins, ARS binding protein 1, was previously described (Abpl [Y. Murakami, J. A. Huberman, and J. Hurwitz, Proc. Natl. Acad. Sci. USA 93:502-507, 1996]). In this report the isolation, characterization, and cloning of a second binding activity, designated ARS binding protein 2 (Abp2), are described. Purified Abp2 has an apparent molecular mass of 75 kDa. Footprinting analyses revealed that it binds preferentially to overlapping near matches to the Maundrell ARS consensus sequence. The gene abp2 was isolated, sequenced, and overexpressed in Escherichia coli. The DNA binding activity of overexpressed Abp2 was similar to that of native Abp2. The deduced amino acid sequence contains a region similar to a proline-rich motif (GRP) present in several proteins that bind A+T-rich DNA sequences. Replacement of amino acids within this motif with alanine either abolished or markedly reduced the DNA binding activity of the mutated Abp2 protein, indicating that this motif is essential for the DNA binding activity of Abp2. Disruption of the abp2 gene showed that the gene is not essential for cell viability. However, at elevated temperatures the null mutant was less viable than the wild type and exhibited changes in nuclear morphology. The null mutant entered mitosis with delayed kinetics when DNA replication was blocked with hydroxyurea, and advancement through mitosis led to the loss of cell viability and aberrant formation of septa. The null mutant was also sensitive to UV radiation, suggesting that Abp2 may play a role in regulating the cell cycle response to stress signals.","authors":"Sanchez JP, Murakami Y, Huberman JA, Hurwitz J","authors_abbrev":"Sanchez JP et al.","pubmed_publication_date":"Mar 1998","pubmed_entrez_date":"1998-03-06","publication_year":"1998","canto_session_key":"dcb5b815ca8cd5ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-29 08:15:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-29 08:15:43","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1861.02","SPAC23C4.18c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-29"},{"uniquename":"PMID:26673708","title":"A novel RNA-binding mode of the YTH domain reveals the mechanism for recognition of determinant of selective removal by Mmi1.","citation":"Nucleic Acids Res 2016 Jan 29;44(2):969-82","abstract":"The YTH domain-containing protein Mmi1, together with other factors, constitutes the machinery used to selectively remove meiosis-specific mRNA during the vegetative growth of fission yeast. Mmi1 directs meiotic mRNAs to the nuclear exosome for degradation by recognizing their DSR (determinant of selective removal) motif. Here, we present the crystal structure of the Mmi1 YTH domain in the apo state and in complex with a DSR motif, demonstrating that the Mmi1 YTH domain selectively recognizes the DSR motif. Intriguingly, Mmi1 also contains a potential m(6)A (N(6)-methyladenine)-binding pocket, but its binding of the DSR motif is dependent on a long groove opposite the m(6)A pocket. The DSR-binding mode is distinct from the m(6)A RNA-binding mode utilized by other YTH domains. Furthermore, the m(6)A pocket cannot bind m(6)A RNA. Our structural and biochemical experiments uncover the mechanism of the YTH domain in binding the DSR motif and help to elucidate the function of Mmi1.","doi":"10.1093/nar/gkv1382","authors":"Wang C, Zhu Y, Bao H, Jiang Y, Xu C, Wu J, Shi Y","authors_abbrev":"Wang C et al.","pubmed_publication_date":"29 Jan 2016","pubmed_entrez_date":"2015-12-18","publication_year":"2016","canto_session_key":"ba4d33259ff4db6d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-12-19 01:21:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.12c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"5dno","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A","position":"322-488"}],"title":"Crystal structure of Mmi1 YTH domain complex with RNA","entry_authors":"Wang CY,Zhu YW,Wu JH,Shi YY","entry_authors_abbrev":"Wang CY et al.","reference_uniquename":"PMID:26673708","experimental_method":"X-ray","resolution":"1.8"},{"pdb_id":"5dnp","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A/B","position":"322-488"}],"title":"Crystal structure of Mmi1 YTH domain","entry_authors":"Wang CY,Zhu YW,Shi YY,Wu JH","entry_authors_abbrev":"Wang CY et al.","reference_uniquename":"PMID:26673708","experimental_method":"X-ray","resolution":"2.3"}]},{"uniquename":"PMID:9309167","title":"An approach to identify functional homologues and suppressors of genes in fission yeast.","citation":"Curr Genet 1997 Jul;32(1):27-31","abstract":"We have developed a procedure using a bank of temperature-sensitive (ts) mutants of fission yeast to identify mutants which can be rescued by expression of a plasmid-borne gene of interest. The procedure has been used to identify new ts alleles of cdc2 and swi7/poll, a ts mutant rescued by actin, and to identify a ts allele of cdc11 which can be rescued by combined mammalian Myc and Max expression. The procedure should also be useful as an alternative approach to identify genes in fission yeast which are functionally homologous to genes of interest from other organisms.","authors":"Grallert B, Nurse P","authors_abbrev":"Grallert B et al.","pubmed_publication_date":"Jul 1997","pubmed_entrez_date":"1997-07-01","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8346915","title":"Two purine biosynthetic enzymes that are required for cadmium tolerance in Schizosaccharomyces pombe utilize cysteine sulfinate in vitro.","citation":"Arch Biochem Biophys 1993 Aug 01;304(2):392-401","abstract":"In plants and in certain fungi, exposure to heavy metals induces the synthesis of metal-binding peptides commonly known as phytochelatins. With cadmium, phytochelatins can sequester the metal into a sulfide-containing complex. From genetic analysis of fission yeast mutants, we previously reported that two genes in purine biosynthesis, encoding adenylosuccinate synthetase and succinoaminoimidazole carboxamide ribonucleotide (SAICAR) synthetase, are required for the biogenesis of the phytochelatin-cadmium-sulfide complex in vivo. We suggested that a sulfur analog of aspartate, cysteine sulfinate, might be utilized by these enzymes and that the cysteine sulfinate-derived products would then become intermediates or carriers in a sulfur transfer pathway leading to the sulfide found within the metal chelate. In this paper, we report that partially purified adenylosuccinate synthetase and SAICAR synthetase are capable of utilizing cysteine sulfinate in vitro to form sulfur analog products. Adenylosuccinate lyase, however, fails to catalyze further conversion of these sulfur derivatives. These observations support the genetic data implicating a link among purine biosynthetic enzymes, sulfur metabolism, and cadmium tolerance.","authors":"Juang RH, McCue KF, Ow DW","authors_abbrev":"Juang RH et al.","pubmed_publication_date":"01 Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_session_key":"8699a16a5d40e84b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-09 10:25:27","canto_approved_date":"2025-05-19 08:26:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-24 09:31:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC144.03","SPBC14F5.09c","SPBC409.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-02-09"},{"uniquename":"PMID:8262067","title":"The Schizosaccharomyces pombe cwg2+ gene codes for the beta subunit of a geranylgeranyltransferase type I required for beta-glucan synthesis.","citation":"EMBO J 1993 Dec 15;12(13):5245-54","abstract":"The product of the Schizosaccharomyces pombe cwg2+ gene is involved in the biosynthesis of beta-D-glucan. When grown at the non-permissive temperature, cwg2-1 mutant cells lyse in the absence of an osmotic stabilizer and display a reduced (1-3) beta-D-glucan content and (1-3) beta-D-glucan synthase activity. The cwg2+ gene was cloned by the rescue of the cwg2-1 mutant phenotype using an S. pombe genomic library and subsequently verified by integration of the appropriate insert into the S. pombe genome. Determination of the nucleotide sequence of this gene revealed a putative open reading frame of 1065 bp encoding a polypeptide of 355 amino acids with a calculated M(r) of 40,019. The cwg2+ DNA hybridizes to a main transcript, the 5' end of which maps to a position 469 bp upstream of the predicted start of translation. The sequence between the transcription and the translation start sites is unusually long and has several short open reading frames which suggest a translational control of the gene expression. Comparative analysis of the predicted amino acid sequence shows that it possesses significant similarity to three Saccharomyces cerevisiae proteins, encoded by the DPR1/RAM1, CDC43/CAL1 and ORF2/BET2 genes respectively, which are beta subunits of different prenyltransferases. When grown at 37 degrees C, cwg2-1 mutant extracts were specifically deficient in geranylgeranyltransferase type I activity, as measured in vitro. Multiple copies of the CDC43 gene can partially suppress the growth and (1-3) beta-D-glucan synthase defect of the cwg2-1 mutant at the restrictive temperature. In a similar manner, the cwg2+ gene can partially suppress the cdc43-2 growth defect. These results indicate that cwg2+ is the structural gene for the beta subunit of geranylgeranyltransferase type I in S. pombe and that this enzyme is required for (1-3) beta-D-glucan synthase activity. The functional homology of Cwg2 with Cdc43, which has been implicated in the control of cell polarity, suggests a link between two morphogenetic events such as establishment of cell polarity and cell wall biosynthesis.","authors":"Díaz M, Sanchez Y, Bennett T, Sun CR, Godoy C, Tamanoi F, Duran A, Perez P","authors_abbrev":"Díaz M et al.","pubmed_publication_date":"15 Dec 1993","pubmed_entrez_date":"1993-12-15","publication_year":"1993","canto_session_key":"18c568ac15d1468c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-13 07:27:49","canto_approved_date":"2022-06-11 08:35:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-13 07:27:43","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2E1P5.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-05-13"},{"uniquename":"PMID:16581849","title":"Analysis of a generic model of eukaryotic cell-cycle regulation.","citation":"Biophys J 2006 Jun 15;90(12):4361-79","abstract":"We propose a protein interaction network for the regulation of DNA synthesis and mitosis that emphasizes the universality of the regulatory system among eukaryotic cells. The idiosyncrasies of cell cycle regulation in particular organisms can be attributed, we claim, to specific settings of rate constants in the dynamic network of chemical reactions. The values of these rate constants are determined ultimately by the genetic makeup of an organism. To support these claims, we convert the reaction mechanism into a set of governing kinetic equations and provide parameter values (specific to budding yeast, fission yeast, frog eggs, and mammalian cells) that account for many curious features of cell cycle regulation in these organisms. Using one-parameter bifurcation diagrams, we show how overall cell growth drives progression through the cell cycle, how cell-size homeostasis can be achieved by two different strategies, and how mutations remodel bifurcation diagrams and create unusual cell-division phenotypes. The relation between gene dosage and phenotype can be summarized compactly in two-parameter bifurcation diagrams. Our approach provides a theoretical framework in which to understand both the universality and particularity of cell cycle regulation, and to construct, in modular fashion, increasingly complex models of the networks controlling cell growth and division.","authors":"Csikász-Nagy A, Battogtokh D, Chen KC, Novák B, Tyson JJ","authors_abbrev":"Csikász-Nagy A et al.","pubmed_publication_date":"15 Jun 2006","pubmed_entrez_date":"2006-04-04","publication_year":"2006","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF13934","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:24618","SPBC29A10.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20164182","title":"Rga4 modulates the activity of the fission yeast cell integrity MAPK pathway by acting as a Rho2 GTPase-activating protein.","citation":"J Biol Chem 2010 Apr 09;285(15):11516-25","abstract":"Rho GTPase-activating proteins (GAPs) are responsible for the inactivation of Rho GTPases, which are involved in the regulation of critical biological responses in eukaryotic cells, ranging from cell cycle control to cellular morphogenesis. The genome of fission yeast Schizosaccharomyces pombe contains six genes coding for putative Rho GTPases, whereas nine genes code for predicted Rho GAPs (Rga1 to Rga9). One of them, Rga4, has been recently described as a Cdc42 GAP, involved in the control of cell diameter and symmetry in fission yeast. In this work we show that Rga4 is also a Rho2 GAP that negatively modulates the activity of the cell integrity pathway and its main effector, MAPK Pmk1. The DYRK-type protein kinase Pom1, which regulates both the localization and phosphorylation state of Rga4, is also a negative regulator of the Pmk1 pathway, but this control is not dependent upon the Rga4 role as a Rho2-GAP. Hence, two subsets of Rga4 negatively regulate Cdc42 and Rho2 functions in a specific and unrelated way. Finally, we show that Rga7, another Rho2 GAP, down-regulates the Pmk1 pathway in addition to Rga4. These results reinforce the notion of the existence of complex mechanisms determining the selectivity of Rho GAPs toward Rho GTPases and their functions.","doi":"10.1074/jbc.M109.071027","authors":"Soto T, Villar-Tajadura MA, Madrid M, Vicente J, Gacto M, Pérez P, Cansado J","authors_abbrev":"Soto T et al.","pubmed_publication_date":"09 Apr 2010","pubmed_entrez_date":"2010-02-19","publication_year":"2010","canto_session_key":"9d4e23c125e5a359","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-07-09 14:52:18","canto_approved_date":"2020-07-09 14:52:18","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-07-09 14:52:11","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":66,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.09c","SPAC110.03","SPAC2F7.03c","SPAC16.01","SPAC24B11.06c","SPBC12D12.04c","SPBC119.08","SPBC354.13","SPBC28E12.03","SPBC23G7.08c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2020-07-09"},{"uniquename":"PMID:12633877","title":"The dihydroceramide desaturase is not essential for cell viability in Schizosaccharomyces pombe.","citation":"FEBS Lett 2003 Mar 13;538(1-3):192-6","abstract":"Recent studies have identified a new family of desaturase-like polypeptide sequences in many higher eukaryotes. Functional characterisation of one member of this family, from Schizosaccharomyces pombe, revealed the enzyme to be a sphingolipid desaturase. This S. pombe gene designated SDCB3b8.07c was identified as the dihydroceramide Delta(4)-desaturase, responsible for the synthesis of sphingosine. Homologous recombination was used to disrupt the endogenous S. pombe dihydroceramide Delta(4)-desaturase. Surprisingly, this had no effect on cell viability, indicating that sphingosine may not be crucial for normal S. pombe functions. This observation has implications for our understanding of the role of sphingosine and its phosphorylated metabolite sphingosine-1-phosphate in lower eukaryotes.","authors":"Garton S, Michaelson LV, Beaudoin F, Beale MH, Napier JA","authors_abbrev":"Garton S et al.","pubmed_publication_date":"13 Mar 2003","pubmed_entrez_date":"2003-03-14","publication_year":"2003","canto_session_key":"8fbb63ca25c84ad2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-04-30 08:33:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-30 08:29:27","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B8.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-30"},{"uniquename":"PMID:15704224","title":"Development of a genetic transformation system using new selectable markers for fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2005 Feb;22(3):193-202","abstract":"We describe the development of a new transformation system, using multiple auxotrophic marker genes, for the fission yeast Schizosaccharomyces pombe. We developed three new auxotrophic marker genes (arg12(+), tyr1(+) and ade7(+)) and generated a new host strain, YF043, by Cre-loxP-mediated gene disruption. YF043 possessed six mutated biosynthetic genes (leu1-32, ura4-M190T, arg12::loxP, tyr1::loxP, ade7::loxP and his2::loxP). The combination of this host strain and the new selectable markers can be used for gene disruption using the same preexisting transformation systems. In addition, Sz. pombe vectors were constructed, containing selectable marker genes that complement the auxotrophies of YF043. These new vectors are available for gene disruption and heterologous protein expression in strain YF043. The new Sz. pombe host strain will be a useful tool for molecular genetic studies of Sz. pombe where multiple recombinant modifications or multiple mutations are needed.","authors":"Fujita Y, Giga-Hama Y, Takegawa K","authors_abbrev":"Fujita Y et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2005-02-11","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.05c","SPCC1494.04c","SPBC409.10","SPBC1711.13"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:15705571","title":"Analysis of the role of phosphorylation in fission yeast Cdc13p/cyclinB function.","citation":"J Biol Chem 2005 Apr 15;280(15):14591-6","abstract":"The Cdk1p-cyclin B complex drives entry into mitosis in all eukaryotes. Cdc13p is the single essential cyclin in Schizosaccharomyces pombe and a member of the cyclin B family. Cdc13p abundance rises during G(2)-phase and falls as cells progress through mitosis and G(1). Cdc13p degradation, mediated by the anaphase-promoting complex, is an important mechanism of Cdk1p inhibition and mitotic exit. Cdk1p-cyclin B1 complexes shuttle between the nucleus and cytoplasm, and preventing nuclear accumulation of Cdk1p-cyclin B1 in mammalian cells appears to be one mechanism of preventing entry into mitosis during a DNA damage-induced checkpoint delay. In vertebrates, phosphorylation plays a key role in regulating the intracellular distribution of cyclins. Previous mass spectrometric analysis identified sites of Cdc13p phosphorylation. Here, we have confirmed that these sites are the sole in vivo Cdc13p phosphorylation sites and have studied the role that phosphorylation plays in Cdc13p localization and function. Our data indicate that Cdc13p accumulates in the nucleolus in response to G(2) checkpoint delays, rather than in the cytoplasm, and that phosphorylation plays no role in Cdc13p localization or function.","authors":"Ren L, Feoktistova A, McDonald WH, Haese GD, Morrell JL, Gould KL","authors_abbrev":"Ren L et al.","pubmed_publication_date":"15 Apr 2005","pubmed_entrez_date":"2005-02-12","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22504526","title":"Conditional inactivation of replication proteins in fission yeast using hormone-binding domains.","citation":"Methods 2012 Jun;57(2):227-33","abstract":"The fission yeast Schizosaccharomyces pombe is a useful model for analysing DNA replication as genetic methods to allow conditional inactivation of relevant proteins can provide important information about S-phase execution. A number of strategies are available to allow regulation of protein level or activity but there are disadvantages specific to each method and this may have limitations for particular proteins or experiments. We have investigated the utility of the inducible hormone-binding domain (HBD) system, which has been described in other organisms but little used in fission yeast, for the creation of conditional-lethal replication mutants. In this method, proteins are tagged with HBD and can be regulated with β-estradiol. In this article, we describe the application of this method in fission yeast, specifically with regard to analysis of the function of GINS, an essential component of the eukaryotic replicative helicase, the CMG complex.","doi":"10.1016/j.ymeth.2012.03.032","authors":"Pai CC, Schnick J, MacNeill SA, Kearsey SE","authors_abbrev":"Pai CC et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2012-04-17","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9218719","title":"General purpose tagging vectors for fission yeast.","citation":"Gene 1997 Jun 03;191(2):191-5","abstract":"We have designed a series of vectors for use in the fission yeast Schizosaccharomyces pombe that allow fusion of any protein of interest to a triple HA epitope or a GST domain. The HA epitope may be placed at the N terminus or the C terminus under three different versions of the nmt1 promoter, to allow varying levels of gene expression. The GST tag may be placed at the N terminus or C terminus under control of a fully active nmt1 promoter. This family of vectors has compatible restriction sites and modular design, so that the protein under study may be exchanged easily between different plasmids. Using the Cdc19p protein as a test case, we have demonstrated that these plasmids can express functional tagged proteins in the fission yeast cell.","authors":"Forsburg SL, Sherman DA","authors_abbrev":"Forsburg SL et al.","pubmed_publication_date":"03 Jun 1997","pubmed_entrez_date":"1997-06-03","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35856499","title":"Control of nuclear size by osmotic forces in  Schizosaccharomyces pombe .","citation":"Elife 2022 Jul 20;11","abstract":"The size of the nucleus scales robustly with cell size so that the nuclear-to-cell volume ratio (N/C ratio) is maintained during cell growth in many cell types. The mechanism responsible for this scaling remains mysterious. Previous studies have established that the N/C ratio is not determined by DNA amount but is instead influenced by factors such as nuclear envelope mechanics and nuclear transport. Here, we developed a quantitative model for nuclear size control based upon colloid osmotic pressure and tested key predictions in the fission yeast  Schizosaccharomyces pombe . This model posits that the N/C ratio is determined by the numbers of macromolecules in the nucleoplasm and cytoplasm. Osmotic shift experiments showed that the fission yeast nucleus behaves as an ideal osmometer whose volume is primarily dictated by osmotic forces. Inhibition of nuclear export caused accumulation of macromolecules in the nucleoplasm, leading to nuclear swelling. We further demonstrated that the N/C ratio is maintained by a homeostasis mechanism based upon synthesis of macromolecules during growth. These studies demonstrate the functions of colloid osmotic pressure in intracellular organization and size control.","doi":"10.7554/eLife.76075","authors":"Lemière J, Real-Calderon P, Holt LJ, Fai TG, Chang F","authors_abbrev":"Lemière J et al.","pubmed_publication_date":"20 Jul 2022","pubmed_entrez_date":"2022-07-20","publication_year":"2022","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2022-07-23 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10364209","title":"Phosphorylation of the myosin-II light chain does not regulate the timing of cytokinesis in fission yeast.","citation":"J Biol Chem 1999 Jun 18;274(25):17691-5","abstract":"Proper coordination of cytokinesis with chromosome separation during mitosis is crucial to ensure that each daughter cell inherits an equivalent set of chromosomes. It has been proposed that one mechanism by which this is achieved is through temporally regulated myosin regulatory light chain (RLC) phosphorylation (Satterwhite, L. L., and Pollard, T. D. (1992) Curr. Opin. Cell Biol. 4, 43-52). A variety of evidence is consistent with this model. A direct test of the importance of RLC phosphorylation in vivo has been done only in Dictyostelium and Drosophila; phosphorylation of the RLC is essential in Drosophila (Jordan, P., and Karess, R. (1997) J. Cell Biol. 139, 1805-1819) but not essential in Dictyostelium (Ostrow, B. D., Chen, P., and Chisholm, R. L. (1994) J. Cell Biol. 127, 1945-1955). The Schizosaccharomyces pombe myosin light chain Cdc4p is essential for cytokinesis, but it was unknown whether phosphorylation played a role in its regulation. Here we show that the S. pombe myosin light chain Cdc4p is phosphorylated in vivo on either serine 2 or 6 but not both. Mutation of either or both of these sites to alanine did not effect the ability of Cdc4p to bind the type II myosin Myo2p, and cells expressing only these mutated versions of Cdc4p grew and divided normally. Similarly, mutation of Ser-2, Ser-6, or both residues to aspartic acid did not affect growth or division of cells. Thus we conclude that phosphorylation of Cdc4p is not essential in vivo for the function of the protein.","authors":"McCollum D, Feoktistova A, Gould KL","authors_abbrev":"McCollum D et al.","pubmed_publication_date":"18 Jun 1999","pubmed_entrez_date":"1999-06-11","publication_year":"1999","canto_session_key":"fe6e8e353ea78411","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-30 10:13:00","canto_approved_date":"2020-12-30 10:13:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-30 10:12:53","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08","SPCC645.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-12-30"},{"uniquename":"PMID:19330768","title":"Tubulin heterodimers remain functional for one cell cycle after the inactivation of tubulin-folding cofactor D in fission yeast cells.","citation":"Yeast 2009 Apr;26(4):235-47","abstract":"Tubulin-folding cofactor D plays a major role in the formation of functional tubulin heterodimers, the subunits of microtubules (MTs) that are essential for cell division. Previous work has suggested that, in Schizosaccharomyces pombe, cofactor D function is required during G(1) or S phases of the cell cycle, and when it fails to function due to the temperature-sensitive mutation alp1-t1, cells are unable to segregate their chromosomes in the subsequent mitosis. Here we report that another mutation in the cofactor D gene, alp1-1315, causes failures in either the first or second mitosis in cells synchronized in G(1) or G(2) phases, respectively. Other results, however, suggest that the kinetics of viability loss in these mutants does not depend on progression through the cell cycle. When cofactor D function is perturbed in cells blocked in G(2), cytoplasmic MTs appear normal for 2-3 h but thereafter they disintegrate quickly, so that only a few short MTs remain. These residual MTs are, however, stably maintained, suggesting that they do not require active cofactor D function. The abrupt disassembly of MT cytoskeleton at restrictive temperature in non-cycling cofactor D mutant cells strongly suggests that the life-span of folded tubulin dimers might be downregulated. Indeed, this period is significantly shorter than the previously determined dissociation time of bovine tubulins in vitro. The death of mutant cells occurs inevitably after 2-3 h at restrictive temperature in the following mitosis, and is explained by the idea that MT structures formed in the absence of cofactor D cannot support normal cell division.","doi":"10.1002/yea.1663","authors":"Fedyanina OS, Book AJ, Grishchuk EL","authors_abbrev":"Fedyanina OS et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-03-31","publication_year":"2009","canto_session_key":"fd35ea91d23f5b2a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-03-30 16:40:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-09 13:27:26","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.04c","SPBC16A3.15c","SPAC24H6.05","SPBC800.05c","SPBC26H8.07c"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2016-03-09"},{"uniquename":"PMID:9862966","title":"A key role for replication factor C in DNA replication checkpoint function in fission yeast.","citation":"Nucleic Acids Res 1999 Jan 15;27(2):462-9","abstract":"Replication factor C (RF-C) is a five subunit DNA polymerase (Pol) delta/straightepsilon accessory factor required at the replication fork for loading the essential processivity factor PCNA onto the 3'-ends of nascent DNA strands. Here we describe the genetic analysis of the rfc2 +gene of the fission yeast Schizosaccharomyces pombe encoding a structural homologue of the budding yeast Rfc2p and human hRFC37 proteins. Deletion of the rfc2 + gene from the chromosome is lethal but does not result in the checkpoint-dependent cell cycle arrest seen in cells deleted for the gene encoding PCNA or for those genes encoding subunits of either Pol delta or Pol straightepsilon. Instead, rfc2 Delta cells proceed into mitosis with incompletely replicated DNA, indicating that the DNA replication checkpoint is inactive under these conditions. Taken together with recent results, these observations suggest a simple model in which assembly of the RF-C complex onto the 3'-end of the nascent RNA-DNA primer is the last step required for the establishment of a checkpoint-competent state.","authors":"Reynolds N, Fantes PA, MacNeill SA","authors_abbrev":"Reynolds N et al.","pubmed_publication_date":"15 Jan 1999","pubmed_entrez_date":"1998-12-24","publication_year":"1999","canto_session_key":"cf2a29ebf81ca19b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-11 15:08:08","canto_approved_date":"2021-03-25 15:16:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-09 16:25:56","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.02c","SPAC23D3.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-06-11"},{"uniquename":"PMID:18280238","title":"mRNA decapping is promoted by an RNA-binding channel in Dcp2.","citation":"Mol Cell 2008 Feb 15;29(3):324-36","abstract":"Cap hydrolysis by Dcp2 is a critical step in several eukaryotic mRNA decay pathways. Processing requires access to cap-proximal nucleotides and the coordinated assembly of a decapping mRNP, but the mechanism of substrate recognition and regulation by protein interactions have remained elusive. Using NMR spectroscopy and kinetic analyses, we show that yeast Dcp2 resolves interactions with the cap and RNA body using a bipartite surface that forms a channel intersecting the catalytic and regulatory Dcp1-binding domains. The interaction with cap is weak but specific and requires binding of the RNA body to a dynamic interface. The catalytic step is stimulated by Dcp1 and its interaction domain, likely through a substrate-induced conformational change. Thus, activation of the decapping mRNP is restricted by access to 5'-proximal nucleotides, a feature that could act as a checkpoint in mRNA metabolism.","doi":"10.1016/j.molcel.2007.11.027","authors":"Deshmukh MV, Jones BN, Quang-Dang DU, Flinders J, Floor SN, Kim C, Jemielity J, Kalek M, Darzynkiewicz E, Gross JD","authors_abbrev":"Deshmukh MV et al.","pubmed_publication_date":"15 Feb 2008","pubmed_entrez_date":"2008-02-19","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25712463","title":"Myosin motor isoforms direct specification of actomyosin function by tropomyosins.","citation":"Cytoskeleton (Hoboken) 2015 Mar;72(3):131-45","abstract":"Myosins and tropomyosins represent two cytoskeletal proteins that often work together with actin filaments in contractile and motile cellular processes. While the specialized role of tropomyosin in striated muscle myosin-II regulation is well characterized, its role in nonmuscle myosin regulation is poorly understood. We previously showed that fission yeast tropomyosin (Cdc8p) positively regulates myosin-II (Myo2p) and myosin-V (Myo52p) motors. To understand the broader implications of this regulation we examined the role of two mammalian tropomyosins (Tpm3.1cy/Tm5NM1 and Tpm4.2cy/Tm4) recently implicated in cancer cell proliferation and metastasis. Like Cdc8p, the Tpm3.1cy and Tpm4.2cy isoforms significantly enhance Myo2p and Myo52p motor activity, converting nonprocessive Myo52p molecules into processive motors that can walk along actin tracks as single molecules. In contrast to the positive regulation of Myo2p and Myo52p, Cdc8p and the mammalian tropomyosins potently inhibited skeletal muscle myosin-II, while having negligible effects on the highly processive mammalian myosin-Va. In support of a conserved role for certain tropomyosins in regulating nonmuscle actomyosin structures, Tpm3.1cy supported normal contractile ring function in fission yeast. Our work reveals that actomyosin regulation by tropomyosin is dependent on the myosin isoform, highlighting a general role for specific isoforms of tropomyosin in sorting myosin motor outputs.","doi":"10.1002/cm.21213","authors":"Clayton JE, Pollard LW, Murray GG, Lord M","authors_abbrev":"Clayton JE et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-02-26","publication_year":"2015","canto_session_key":"d4e3450499215924","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-02-27 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AF079307","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22554201","title":"Generation and analysis of a barcode-tagged insertion mutant library in the fission yeast Schizosaccharomyces pombe.","citation":"BMC Genomics 2012 May 03;13:161","abstract":"Barcodes are unique DNA sequence tags that can be used to specifically label individual mutants. The barcode-tagged open reading frame (ORF) haploid deletion mutant collections in the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe allow for high-throughput mutant phenotyping because the relative growth of mutants in a population can be determined by monitoring the proportions of their associated barcodes. While these mutant collections have greatly facilitated genome-wide studies, mutations in essential genes are not present, and the roles of these genes are not as easily studied. To further support genome-scale research in S. pombe, we generated a barcode-tagged fission yeast insertion mutant library that has the potential of generating viable mutations in both essential and non-essential genes and can be easily analyzed using standard molecular biological techniques.\nAn insertion vector containing a selectable ura4+ marker and a random barcode was used to generate a collection of 10,000 fission yeast insertion mutants stored individually in 384-well plates and as six pools of mixed mutants. Individual barcodes are flanked by Sfi I recognition sites and can be oligomerized in a unique orientation to facilitate barcode sequencing. Independent genetic screens on a subset of mutants suggest that this library contains a diverse collection of single insertion mutations. We present several approaches to determine insertion sites.\nThis collection of S. pombe barcode-tagged insertion mutants is well-suited for genome-wide studies. Because insertion mutations may eliminate, reduce or alter the function of essential and non-essential genes, this library will contain strains with a wide range of phenotypes that can be assayed by their associated barcodes. The design of the barcodes in this library allows for barcode sequencing using next generation or standard benchtop cloning approaches.","doi":"10.1186/1471-2164-13-161","authors":"Chen BR, Hale DC, Ciolek PJ, Runge KW","authors_abbrev":"Chen BR et al.","pubmed_publication_date":"03 May 2012","pubmed_entrez_date":"2012-05-05","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11884628","title":"Differential expression and requirements for Schizosaccharomyces pombe RAD52 homologs in DNA repair and recombination.","citation":"Nucleic Acids Res 2002 Mar 15;30(6):1316-24","abstract":"In fission yeast two RAD52 homologs have been identified, rad22A(+) and rad22B(+). Two-hybrid experiments and GST pull-down assays revealed physical interaction between Rad22A and Rad22B, which is dependent on the N-terminal regions. Interaction with Rhp51 is dependent on the C-terminal parts of either protein. Both Rad22A and Rad22B also interact with RPA. The expression of rad22B(+) in mitotically dividing cells is very low in comparison with rad22A(+) but is strongly enhanced after induction of meiosis, in contrast to rad22A(+). Rad22B mutant cells are not hypersensitive to DNA-damaging agents (X-rays, UV and cisplatin) and display normal levels of recombination. In these respects the Schizosaccharomyces pombe rad22B mutant resembles the weak phenotype of vertebrate cells deficient for RAD52. Mutation of rad22A(+) leads to severe sensitivity to DNA-damaging agents and to defects in recombination. In a rad22Arad22B double mutant a further increase in sensitivity to DNA-damaging agents and additional mitotic recombination defects were observed. The data presented here indicate that Rad22A and Rad22B have overlapping roles in repair and recombination, although specialized functions for each protein cannot be excluded.","authors":"van den Bosch M, Zonneveld JB, Vreeken K, de Vries FA, Lohman PH, Pastink A","authors_abbrev":"van den Bosch M et al.","pubmed_publication_date":"15 Mar 2002","pubmed_entrez_date":"2002-03-09","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC119.14","SPAC15A10.03c","SPAC30D11.10","SPAC644.14c"],"gene_count":4,"ltp_gene_count":3},{"uniquename":"PMID:19430462","title":"Decapping is preceded by 3' uridylation in a novel pathway of bulk mRNA turnover.","citation":"Nat Struct Mol Biol 2009 Jun;16(6):616-23","abstract":"Both end structures of eukaryotic mRNAs, namely the 5' cap and 3' poly(A) tail, are necessary for transcript stability, and loss of either is sufficient to stimulate decay. mRNA turnover is classically thought to be initiated by deadenylation, as has been particularly well described in Saccharomyces cerevisiae. Here we describe two additional, parallel decay pathways in the fission yeast Schizosaccharomyces pombe. First, in fission yeast mRNA decapping is frequently independent of deadenylation. Second, Cid1-dependent uridylation of polyadenylated mRNAs, such as act1, hcn1 and urg1, seems to stimulate decapping as part of a novel mRNA turnover pathway. Accordingly, urg1 mRNA is stabilized in cid1Delta cells. Uridylation and deadenylation act redundantly to stimulate decapping, and our data suggest that uridylation-dependent decapping is mediated by the Lsm1-7 complex. As human cells contain Cid1 orthologs, uridylation may form the basis of a widespread, conserved mechanism of mRNA decay.","doi":"10.1038/nsmb.1601","authors":"Rissland OS, Norbury CJ","authors_abbrev":"Rissland OS et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-05-12","publication_year":"2009","canto_session_key":"4f8815b38140d61d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chris Norbury","canto_first_approved_date":"2014-07-03 16:09:40","canto_approved_date":"2025-09-04 12:09:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-07 13:17:23","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Chris Norbury","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.21","SPBC3H7.06c","SPAC23C11.12","SPCC31H12.08c","SPAC19D5.03","SPBC32H8.12c","SPBC3D6.08c","SPBC29A10.09c","SPAC1002.19","SPAC140.02","SPCC13B11.01","SPAC22G7.04"],"gene_count":12,"ltp_gene_count":2,"approved_date":"2014-07-03"},{"uniquename":"PMID:17868468","title":"Adaptive expression responses in the Pol-gamma null strain of S. pombe depleted of mitochondrial genome.","citation":"BMC Genomics 2007 Sep 15;8:323","abstract":"DNA polymerase gamma(Pol-gamma) has been shown to be essential for maintenance of the mitochondrial genome (mtDNA) in the petite-positive budding yeast Saccharomyces cerevisiae. Budding yeast cells lacking mitochondria exhibit a slow-growing or petite-colony phenotype. Petite strains fail to grow on non-fermentable carbon sources. However, it is not clear whether the Pol-gamma is required for mtDNA maintenance in the petite-negative fission yeast Schizosaccharomyces pombe.\nWe show that disruption of the nuclear gene pog1+ that encodes Pol-gamma is sufficient to deplete mtDNA in S. pombe. Cells bearing pog1Delta allele require substantial growth periods to form petite colonies. Mitotracker assays indicate that pog1Delta cells are defective in mitochondrial function and EM analyses suggest that pog1Delta cells lack normal mitochondrial structures. Depletion of mtDNA in pog1Delta cells is evident from quantitative real-time PCR assays. Genome-wide expression profiles of pog1Delta and other mtDNA-less cells reveal that many genes involved in response to stimulus, energy derivation by oxidation of organic compounds, cellular carbohydrate metabolism, and energy reserve metabolism are induced. Conversely, many genes encoding proteins involved in amino acid metabolism and oxidative phosphorylation are repressed.\nBy showing that Pol-gamma is essential for mtDNA maintenance and disruption of pog1+ alters the genome-wide expression profiles, we demonstrated that cells lacking mtDNA exhibit adaptive nuclear gene expression responses in the petite-negative S. pombe.","authors":"Chu Z, Li J, Eshaghi M, Karuturi RK, Lin K, Liu J","authors_abbrev":"Chu Z et al.","pubmed_publication_date":"15 Sep 2007","pubmed_entrez_date":"2007-09-18","publication_year":"2007","canto_session_key":"bfb9017c2ff95ae7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-03-24 16:32:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-25 15:53:19","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC24B10.22"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-25"},{"uniquename":"PMID:12007437","title":"Cytokinesis: myosin spots the ring.","citation":"Curr Biol 2002 Apr 30;12(9):R334-6","abstract":"Faithful actomyosin ring assembly is pivotal for successful cell division. The mechanisms by which the actomyosin ring is assembled at the correct time and place remain unclear. Recent studies in fission yeast have shown that a myosin II-containing spot may be a novel progenitor structure essential for actomyosin ring assembly.","authors":"Hou MC, McCollum D","authors_abbrev":"Hou MC et al.","pubmed_publication_date":"30 Apr 2002","pubmed_entrez_date":"2002-05-15","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8422996","title":"Thiamine-repressible expression vectors pREP and pRIP for fission yeast.","citation":"Gene 1993 Jan 15;123(1):127-30","abstract":"The promoter and polyadenylation signal of the thiamine-repressible gene nmt1 of Schizosaccharomyces pombe have been used to construct the pREP extrachromosomally replicating plasmids and the pRIP integrative expression plasmids. These plasmids permit thiamine-mediated control of transcription to be applied to cloned genes.","authors":"Maundrell K","authors_abbrev":"Maundrell K","pubmed_publication_date":"15 Jan 1993","pubmed_entrez_date":"1993-01-15","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084862","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.50"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29196561","title":"Hierarchical Regulation of Centromeric Cohesion Protection by Meikin and Shugoshin during Meiosis I.","citation":"Cold Spring Harb Symp Quant Biol 2017;82:259-266","abstract":"The kinetochore is the key apparatus regulating chromosome segregation. Particularly in meiosis, unlike in mitosis, sister kinetochores are captured by microtubules emanating from the same spindle pole (mono-orientation), and sister chromatid cohesion mediated by cohesin is protected at centromeres in the following anaphase. Shugoshin, which localizes to centromeres depending on the phosphorylation of histone H2A by Bub1 kinase, plays a central role in protecting meiotic cohesin Rec8 from separase cleavage. Another key meiotic kinetochore factor, Moa1 (meikin), which was initially characterized as a mono-orientation factor in fission yeast, also regulates cohesion protection. Moa1, which associates stably with CENP-C during meiosis I, recruits Plo1 (polo-like kinase) to the kinetochores and phosphorylates Spc7 (KNL1), inducing the persistent accumulation of Bub1 at kinetochores. The meiotic Bub1 pool ensures robust Sgo1 (shugoshin) localization and cohesion protection at centromeres by cooperating with heterochromatin protein Swi6, which binds and stabilizes Sgo1. Further, molecular genetic analyses reveal a hierarchical regulation of centromeric cohesion protection by meikin and shugoshin during meiosis I.","doi":"10.1101/sqb.2017.82.033811","authors":"Miyazaki S, Kim J, Sakuno T, Watanabe Y","authors_abbrev":"Miyazaki S et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-12-03","publication_year":"2017","canto_session_key":"e2f3375e59d723f0","canto_annotation_status":"APPROVED","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_first_approved_date":"2024-04-24 16:30:40","canto_approved_date":"2024-04-24 16:30:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-24 15:04:32","canto_added_date":"2017-12-05 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP35G2.03c","SPAC23C11.16","SPCC1020.02","SPBC106.01","SPAC15E1.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2024-04-24"},{"uniquename":"GO_REF:0000044","title":"Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt. ","abstract":"Transitive assignment of GO terms based on the UniProtKB/Swiss-Prot Subcellular Location vocabulary. UniProtKB Subcellular Location is a controlled vocabulary used to supply subcellular location information to UniProtKB entries in the SUBCELLULAR LOCATION lines. Terms from this vocabulary are annotated manually to UniProtKB/Swiss-Prot entries but are automatically assigned to UniProtKB/TrEMBL entries from the underlying nucleic acid databases and/or by the UniProt automatic annotation program.","authors":"UniProt-GOA","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC823.16c","SPBC530.01","SPAC11H11.01","SPBC4B4.10c","SPBC119.12","SPAC30.01c","SPAC227.04","SPAC2F7.10","SPAC27D7.04","SPAC589.07c","SPAC23C4.16c","SPAC1783.02c","SPAC144.06","SPCC16A11.08","SPAC458.06","SPBP16F5.07","SPBC405.05","SPAC23H3.06","SPCC1682.11c","SPBC6B1.05c","SPAC4D7.01c","SPAC19G12.03","SPAC20G4.06c","SPAP11E10.02c","SPAC10F6.11c","SPBC31E1.01c","SPAC688.07c","SPAC1B3.07c","SPBC211.03c","SPAC1039.11c","SPBP22H7.04","SPCC613.03","SPBC776.06c","SPAC1D4.03c"],"gene_count":34,"ltp_gene_count":0},{"uniquename":"PMID:31945375","title":"Analysis of Active Site Architecture and Reaction Product Linkage Chemistry Reveals a Conserved Cleavage Substrate for an Endo-alpha-mannanase within Diverse Yeast Mannans.","citation":"J Mol Biol 2020 Feb 14;432(4):1083-1097","abstract":"Yeast α-mannan (YM) is a densely branched N-linked glycan that decorates the surface of yeast cell walls. Owing to the high degree of branching, cleavage of the backbone of YM appears to rely on the coupled action of side-chain-cleaving enzymes. Upon examining the genome sequences of bovine-adapted Bacteroides thetaiotaomicron strains, isolated for their ability to degrade YM, we have identified a tandem pair of genes inserted into an orphan pathway predicted to be involved in YM metabolism. Here, we investigated the activity of one of these enzymes, a predicted endo-mannanase from glycoside hydrolase (GH) family 76 (BtGH76-MD40). Purified recombinant BtGH76-MD40 displayed activity on structurally distinct YMs from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Linkage analysis of released oligosaccharide products from S. cerevisiae and S. pombe mannan determined BtGH76-MD40 targets a specific linkage that is conserved in structurally diverse YM substrates. In addition, using two differential derivatization methods, we have shown that there is an absolute requirement for undecorated d-mannopyranose in the -1 subsite. Determination of the BtGH76-MD40 X-ray crystal structure and structural superimposition and molecular docking of a branched alpha-mannopentatose substrate supported these findings. In contrast, BtGH76-MD40 can accommodate extended side chains in the +1 and -2 subsites, highlighting that a single alpha-1,6-mannosyl residue is a prerequisite for activity, and cleavage occurs at the reducing end of the undecorated monosaccharide. Collectively these results demonstrate how acquisition of new enzymes within extant pathways contributes to the functional abilities of saccharolytic bacteria persisting in complex digestive ecosystems.","doi":"10.1016/j.jmb.2019.12.048","authors":"Jones DR, Xing X, Tingley JP, Klassen L, King ML, Alexander TW, Abbott DW","authors_abbrev":"Jones DR et al.","pubmed_publication_date":"14 Feb 2020","pubmed_entrez_date":"2020-01-17","publication_year":"2020","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23145048","title":"A genetic and pharmacological analysis of isoprenoid pathway by LC-MS/MS in fission yeast.","citation":"PLoS One 2012;7(11):e49004","abstract":"Currently, statins are the only drugs acting on the mammalian isoprenoid pathway. The mammalian genes in this pathway are not easily amenable to genetic manipulation. Thus, it is difficult to study the effects of the inhibition of various enzymes on the intermediate and final products in the isoprenoid pathway. In fission yeast, antifungal compounds such as azoles and terbinafine are available as inhibitors of the pathway in addition to statins, and various isoprenoid pathway mutants are also available. Here in these mutants, treated with statins or antifungals, we quantified the final and intermediate products of the fission yeast isoprenoid pathway using liquid chromatography-mass spectrometry/mass spectrometry. In hmg1-1, a mutant of the gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGR), ergosterol (a final sterol product), and squalene (an intermediate pathway product), were decreased to approximately 80% and 10%, respectively, compared with that of wild-type cells. Consistently in wild-type cells, pravastatin, an HMGR inhibitor decreased ergosterol and squalene, and the effect was more pronounced on squalene. In hmg1-1 mutant and in wild-type cells treated with pravastatin, the decrease in the levels of farnesyl pyrophosphate and geranylgeranyl pyrophosphate respectively was larger than that of ergosterol but was smaller than that of squalene. In Δerg6 or Δsts1 cells, mutants of the genes involved in the last step of the pathway, ergosterol was not detected, and the changes of intermediate product levels were distinct from that of hmg1-1 mutant. Notably, in wild-type cells miconazole and terbinafine only slightly decreased ergosterol level. Altogether, these studies suggest that the pleiotropic phenotypes caused by the hmg1-1 mutation and pravastatin might be due to decreased levels of isoprenoid pyrophosphates or other isoprenoid pathway intermediate products rather than due to a decreased ergosterol level.","doi":"10.1371/journal.pone.0049004","authors":"Takami T, Fang Y, Zhou X, Jaiseng W, Ma Y, Kuno T","authors_abbrev":"Takami T et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-11-13","publication_year":"2012","canto_session_key":"9abb48d4dd839d0a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-07-24 08:04:12","canto_approved_date":"2024-05-01 08:52:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-18 23:59:29","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":45,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.16c","SPBC27B12.03c","SPAC19A8.04","SPAC20G4.07c","SPCC162.09c","SPBC16E9.05","SPBC36.06c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2013-07-24"},{"uniquename":"PMID:32142608","title":"Mutations in a Single Signaling Pathway Allow Cell Growth in Heavy Water.","citation":"ACS Synth Biol 2020 Apr 17;9(4):733-748","abstract":"Life is completely dependent on water. To analyze the role of water as a solvent in biology, we replaced water with heavy water (D 2 O) and investigated the biological effects by a wide range of techniques, using  Schizosaccharomyces pombe  as model organism. We show that high concentrations of D 2 O lead to altered glucose metabolism and growth retardation. After prolonged incubation in D 2 O, cells displayed gross morphological changes, thickened cell walls, and aberrant cytoskeletal organization. By transcriptomics and genetic screens, we show that the solvent replacement activates two signaling pathways: (1)  the heat-shock response pathway  and (2)  the cell integrity pathway . Although the heat-shock response system upregulates various chaperones and other stress-relieving enzymes, we find that the activation of this pathway does not offer any fitness advantage to the cells under the solvent-replaced conditions. However, limiting the D 2 O-triggered activation of the cell integrity pathway allows cell growth when H 2 O is completely replaced with D 2 O. The isolated D 2 O-tolerant strains may aid biological production of deuterated biomolecules.","doi":"10.1021/acssynbio.9b00376","authors":"Kampmeyer C, Johansen JV, Holmberg C, Karlson M, Gersing SK, Bordallo HN, Kragelund BB, Lerche MH, Jourdain I, Winther JR, Hartmann-Petersen R","authors_abbrev":"Kampmeyer C et al.","pubmed_publication_date":"17 Apr 2020","pubmed_entrez_date":"2020-03-07","publication_year":"2020","canto_session_key":"04fc263cb7454d53","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_first_approved_date":"2020-05-06 13:49:34","canto_approved_date":"2025-12-17 16:46:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-05-01 11:59:21","canto_added_date":"2020-03-08 01:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":48,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.15c","SPAC5D6.05","SPBP8B7.11","SPAC806.07","SPBC13G1.03c","SPAC328.01c","SPBP4H10.04","SPBC12D12.04c","SPAC343.13","SPAC4H3.13","SPAC12B10.12c","SPBC27B12.08","SPBC18H10.06c","SPCC970.10c","SPAC644.06c","SPAC13G7.03","SPCC1494.07","SPCC1281.01","SPAC6F6.01","SPAC2F7.07c","SPBC16E9.13","SPBC19C7.02","SPAPB2B4.02","SPAC1039.02","SPAC513.03","SPBC106.10","SPBC543.07","SPBC13G1.08c","SPBC119.08","SPAC10F6.13c","SPBC3B9.11c","SPAC17H9.10c","SPAC3H8.02","SPCC1739.14","SPCP1E11.06","SPBC23G7.08c","SPAC926.03","SPAC4D7.03","SPAC2F3.02","SPNCRNA.899","SPAC7D4.06c","SPAC26H5.05","SPAC26F1.04c","SPAC1F3.02c","SPBC21C3.20c","SPAC24C9.07c","SPCC970.06","SPBC1604.05","SPCC777.10c","SPBC1539.08","SPAC24B11.06c","SPBC16E9.08"],"gene_count":52,"ltp_gene_count":51,"approved_date":"2020-05-06"},{"uniquename":"PMID:21869531","title":"Complex formation, phosphorylation, and localization of protein kinase A of Schizosaccharomyces pombe upon glucose starvation.","citation":"Biosci Biotechnol Biochem 2011;75(8):1456-65","abstract":"Nine sam mutants that undergo sexual differentiation without requiring starvation in Schizosaccharomyces pombe were previously isolated. In this study, we identified a nonsense mutation on the pka1 locus in the sam6 mutant. pka1 encodes a catalytic subunit of protein kinase A (PKA). Replacement and overexpression of pka1 suppressed the KCl sensitivity and hyper-mating phenotype of sam6, confirming that sam6 is an allele of pka1. To characterize further the regulation of Pka1, we tested the physical interaction between Pka1 and Cgs1 (a regulatory subunit of PKA). Pka1 and Cgs1 physically interacted under glucose-limited conditions but not under glucose-rich conditions. In addition, the formation of a Pka1-Cgs1 complex was detected under glucose-limited conditions by Blue Native PAGE. Furthermore, the Pka1 protein was found to be phosphorylated under glucose-starved conditions, and at the same time its localization shifted from the nucleus towards the cytoplasm (mainly the vacuoles), suggesting a strong relationship among phosphorylation, complex formation, and the cytoplasmic distribution of Pka1.","authors":"Gupta DR, Paul SK, Oowatari Y, Matsuo Y, Kawamukai M","authors_abbrev":"Gupta DR et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-08-27","publication_year":"2011","canto_session_key":"a6a51043db00c124","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-13 13:54:50","canto_approved_date":"2022-06-06 07:03:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-10 08:11:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.13","SPAC24B11.06c","SPBC106.10","SPAC8C9.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-11-13"},{"uniquename":"PMID:22412019","title":"A stochastic model of kinetochore-microtubule attachment accurately describes fission yeast chromosome segregation.","citation":"J Cell Biol 2012 Mar 19;196(6):757-74","abstract":"In fission yeast, erroneous attachments of spindle microtubules to kinetochores are frequent in early mitosis. Most are corrected before anaphase onset by a mechanism involving the protein kinase Aurora B, which destabilizes kinetochore microtubules (ktMTs) in the absence of tension between sister chromatids. In this paper, we describe a minimal mathematical model of fission yeast chromosome segregation based on the stochastic attachment and detachment of ktMTs. The model accurately reproduces the timing of correct chromosome biorientation and segregation seen in fission yeast. Prevention of attachment defects requires both appropriate kinetochore orientation and an Aurora B-like activity. The model also reproduces abnormal chromosome segregation behavior (caused by, for example, inhibition of Aurora B). It predicts that, in metaphase, merotelic attachment is prevented by a kinetochore orientation effect and corrected by an Aurora B-like activity, whereas in anaphase, it is corrected through unbalanced forces applied to the kinetochore. These unbalanced forces are sufficient to prevent aneuploidy.","doi":"10.1083/jcb.201107124","authors":"Gay G, Courtheoux T, Reyes C, Tournier S, Gachet Y","authors_abbrev":"Gay G et al.","pubmed_publication_date":"19 Mar 2012","pubmed_entrez_date":"2012-03-14","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1186659","title":"Studies on the mechanism of electron trasport in the bc1-segment of the respiratory chain in yeast. III. Isolation and characterization of an antimycin resistant mutant ANT 8 in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1975;137(4):353-63","abstract":"1. A mutant (ANT 8) of Schizosaccharomyces pombe which shows resistance to antimycin both in vivo and in vitro is characterized biochemically and genetically. 2. In crosses of ANT 8 with auxotrophic strains, resistance to antimycin segregates 2:2 indicating that resistance is conferred by a single nuclear gene. Diploids heterozygous for the resistance gene, however, show segregation of the resistance and sensitivity during mitosis. Possible reasons for this segregation are discussed. 3. Compared with the wild type, the NADH oxidase of ANT 8 requires 13 times as much antimycin for 95% inhibition. After addition of ubiquinone-3, electron transport which is less sensitive to antimycin is found only in the mutant. 4. The resistance of the mutant ANT 8 si due to the much weaker binding of antimycin to mitochondria. As in the wild type, two antimycin binding sites can be separated by binding studies. From the inhibition curves it is evident that binding of antimycin to oxidized mitochondrial particles does not correspond with its inhibitory effect on the partly reduced enzyme in kinetic studies. 5. The peak of the b-cytochrome absorbing at 560.2 nm at 77 degrees K in the wild type is shifted to 561 nm in the mutant. 6. A special preparation method for mutant mitochondrial particles is described, yielding highly active enzymes and CO-insensitive cytochromes. 7. The results are discussed with reference to the components in our model of the respiratory chain, which may be responsible for this type of resistance.","authors":"Lang B, Burger G, Wolf K, Bandlow W, Kaudewitz F","authors_abbrev":"Lang B et al.","pubmed_publication_date":"1975","pubmed_entrez_date":"1975-01-01","publication_year":"1975","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14712642","title":"RNA polymerase III from the fission yeast, Schizosaccharomyces pombe.","citation":"Methods Enzymol 2003;370:165-73","abstract":"","authors":"Huang Y, Hamada M, Maraia RJ","authors_abbrev":"Huang Y et al.","pubmed_publication_date":"2003","pubmed_entrez_date":"2004-01-10","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24270859","title":"Timing of meiosis: microtubules on the move.","citation":"Cell Cycle 2014;13(1):13","abstract":"","doi":"10.4161/cc.27298","authors":"Nosek J, Tomaska L","authors_abbrev":"Nosek J et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2013-11-26","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29813055","title":"Parameter uncertainty quantification using surrogate models applied to a spatial model of yeast mating polarization.","citation":"PLoS Comput Biol 2018 May;14(5):e1006181","abstract":"A common challenge in systems biology is quantifying the effects of unknown parameters and estimating parameter values from data. For many systems, this task is computationally intractable due to expensive model evaluations and large numbers of parameters. In this work, we investigate a new method for performing sensitivity analysis and parameter estimation of complex biological models using techniques from uncertainty quantification. The primary advance is a significant improvement in computational efficiency from the replacement of model simulation by evaluation of a polynomial surrogate model. We demonstrate the method on two models of mating in budding yeast: a smaller ODE model of the heterotrimeric G-protein cycle, and a larger spatial model of pheromone-induced cell polarization. A small number of model simulations are used to fit the polynomial surrogates, which are then used to calculate global parameter sensitivities. The surrogate models also allow rapid Bayesian inference of the parameters via Markov chain Monte Carlo (MCMC) by eliminating model simulations at each step. Application to the ODE model shows results consistent with published single-point estimates for the model and data, with the added benefit of calculating the correlations between pairs of parameters. On the larger PDE model, the surrogate models allowed convergence for the distribution of 15 parameters, which otherwise would have been computationally prohibitive using simulations at each MCMC step. We inferred parameter distributions that in certain cases peaked at values different from published values, and showed that a wide range of parameters would permit polarization in the model. Strikingly our results suggested different diffusion constants for active versus inactive Cdc42 to achieve good polarization, which is consistent with experimental observations in another yeast species S. pombe.","doi":"10.1371/journal.pcbi.1006181","authors":"Renardy M, Yi TM, Xiu D, Chou CS","authors_abbrev":"Renardy M et al.","pubmed_publication_date":"May 2018","pubmed_entrez_date":"2018-05-30","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-06-01 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8493104","title":"Study of multiple fibrillarin mRNAs reveals that 3' end formation in Schizosaccharomyces pombe is sensitive to cold shock.","citation":"Nucleic Acids Res 1993 Apr 25;21(8):1881-7","abstract":"Fibrillarin is a nucleolar protein which is associated with small nucleolar RNAs, and is required for pre-rRNA processing. We have cloned and characterized the gene encoding fibrillarin in the fission yeast Schizosaccharomyces pombe and we have followed its expression under various conditions. Fission yeast fibrillarin is a 305 amino-acid protein which appears to be highly conserved throughout evolution. In Xenopus, human or Saccharomyces cerevisiae, a single fibrillarin mRNA is detected while, in S. pombe a single copy gene encodes different mRNAs which differ at the 3' ends. Under normal growth conditions, two mRNAs of 1.1 and 1.35 kb are detected with the 1.1 kb being the most abundant. Both the total amount and relative abundance of these two mRNAs are strongly affected by exposure to low temperature, namely the 1.1 kb mRNA almost disappears while the 1.35 kb is less markedly diminished. A new species of 3.2 kb accumulates in the cell, which contains an unusually long 3' untranslated region of 2 kb. We have found that exposure of the cells to a cold shock has a profound effect on 3' end formation in S.pombe since the transcription of several other mRNAs is also capable of skipping the normal 3' end site to terminate at a further downstream site.","authors":"Girard JP, Feliu J, Caizergues-Ferrer M, Lapeyre B","authors_abbrev":"Girard JP et al.","pubmed_publication_date":"25 Apr 1993","pubmed_entrez_date":"1993-04-25","publication_year":"1993","canto_session_key":"6f3905850a09f053","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-14 15:58:06","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-14 15:57:41","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC140.02","SPBC2D10.10c","SPBC20F10.01","SPCC330.05c","SPAC24H6.05"],"gene_count":5,"ltp_gene_count":0,"approved_date":"2014-08-14"},{"uniquename":"PMID:7823870","title":"Regulation of protein activities by fusion to steroid binding domains.","citation":"Methods Cell Biol 1994;43 Pt A:335-52","abstract":"","authors":"Mattioni T, Louvion JF, Picard D","authors_abbrev":"Mattioni T et al.","pubmed_publication_date":"1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35658118","title":"The acyl-CoA-binding protein Acb1 regulates mitochondria, lipid droplets, and cell proliferation.","citation":"FEBS Lett 2022 Jul;596(14):1795-1808","abstract":"Mitochondria are involved in many cellular activities, including energy metabolism and biosynthesis of nucleotides, fatty acids and amino acids. Mitochondrial morphology is a key factor in dictating mitochondrial functions. Here, we report that the acyl-CoA-binding protein (ACBP) Acb1 in the fission yeast Schizosaccharomyces pombe is required for the maintenance of tubular mitochondrial morphology and proper mitochondrial respiration. The absence of Acb1 causes severe mitochondrial fragmentation in a dynamin-related protein Dnm1-dependent manner and impairs mitochondrial respiration. Moreover, Acb1 regulates the remodelling of lipid droplets in nutrient-rich conditions. Importantly, Acb1 promotes cell survival when cells are cultured in nutrient-rich medium. Hence, our findings establish roles of ACBP in regulating mitochondria, lipid droplets and cell viability.","doi":"10.1002/1873-3468.14415","authors":"He J, Liu K, Zheng S, Wu Y, Zhao C, Yan S, Liu L, Ruan K, Ma X, Fu C","authors_abbrev":"He J et al.","pubmed_publication_date":"Jul 2022","pubmed_entrez_date":"2022-06-03","publication_year":"2022","canto_session_key":"e1f4d0eca71f1467","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-12-30 14:48:54","canto_approved_date":"2024-10-25 08:32:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-14 02:23:55","canto_added_date":"2022-06-08 00:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.08","SPBC1706.03","SPBC1539.06","SPAC1786.01c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2023-12-30"},{"uniquename":"PMID:12734797","title":"A 'marker switch' approach for targeted mutagenesis of genes in Schizosaccharomyces pombe.","citation":"Yeast 2003 May;20(7):587-94","abstract":"The completion of the Schizosaccharomyces pombe genome sequencing project has led to a dramatic acceleration of gene characterization in this system. Once a gene has been identified, the challenge then comes in using reverse genetics to generate a range of mutants in this gene of interest so that the powerful genetics and wealth of genetic backgrounds available in Sz. pombe can be exploited to study the function of the newly identified molecule. Beyond simple PCR-tagging approaches, the high frequency with which illegitimate recombination occurs in Sz. pombe has made the manipulation of some loci complex, time consuming and a process of trial and error. Here we describe a simple 'marker switch' approach that enables the rapid selection of integration events at the locus of interest from an excessive background of integration at heterologous sites. We use the generation of temperature-sensitive mutations in the plo1(+) gene to validate this approach.","authors":"MacIver FH, Glover DM, Hagan IM","authors_abbrev":"MacIver FH et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-05-08","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10508607","title":"The missing (L) UNC?","citation":"Curr Biol 1999 Sep 23;9(18):R708-10","abstract":"In many cells, centrosomes are required to position nuclei at specific locations in the cytoplasm. The nature of the link between centrosomes and nuclei is mysterious, but the recently characterised UNC84 protein appears to be involved.","authors":"Raff JW","authors_abbrev":"Raff JW","pubmed_publication_date":"23 Sep 1999","pubmed_entrez_date":"1999-10-06","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19880757","title":"Role of mitogen-activated protein kinase Sty1 in regulation of eukaryotic initiation factor 2alpha kinases in response to environmental stress in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2010 Jan;9(1):194-207","abstract":"The mitogen-activated protein kinase (MAPK) Sty1 is essential for the regulation of transcriptional responses that promote cell survival in response to different types of environmental stimuli in Schizosaccharomyces pombe. In fission yeast, three distinct eukaryotic initiation factor 2alpha (eIF2alpha) kinases, two mammalian HRI-related protein kinases (Hri1 and Hri2) and the Gcn2 ortholog, regulate protein synthesis in response to cellular stress conditions. In this study, we demonstrate that both Hri1 and Hri2 exhibited an autokinase activity, specifically phosphorylated eIF2alpha, and functionally replaced the endogenous Saccharomyces cerevisiae Gcn2. We further show that Gcn2, but not Hri1 or Hri2, is activated early after exposure to hydrogen peroxide and methyl methanesulfonate (MMS). Cells lacking Gcn2 exhibit a later activation of Hri2. The activated MAPK Sty1 negatively regulates Gcn2 and Hri2 activities under oxidative stress but not in response to MMS. In contrast, Hri2 is the primary activated eIF2alpha kinase in response to heat shock. In this case, the activation of Sty1 appears to be transitory and does not contribute to the modulation of the eIF2alpha kinase stress pathway. In strains lacking Hri2, a type 2A protein phosphatase is activated soon after heat shock to reduce eIF2alpha phosphorylation. Finally, the MAPK Sty1, but not the eIF2alpha kinases, is essential for survival upon oxidative stress or heat shock, but not upon MMS treatment. These findings point to a regulatory coordination between the Sty1 MAPK and eIF2alpha kinase pathways for a particular range of stress responses.","doi":"10.1128/EC.00185-09","authors":"Berlanga JJ, Rivero D, Martín R, Herrero S, Moreno S, de Haro C","authors_abbrev":"Berlanga JJ et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-11-03","publication_year":"2010","canto_session_key":"20eed3e16b16f5bc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G4.03c","SPAC3G9.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU008952","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8045419","title":"Identification of a Xenopus cDNA that prevents mitotic catastrophe in the fission yeast Schizosaccharomyces pombe.","citation":"Gene 1994 Jul 22;145(1):155-6","abstract":"A Xenopus total ovary cDNA library was constructed in a fission yeast expression vector. Using a genetic functional complementation method, we have identified a Xenopus cDNA clone that can rescue several different yeast mitotic catastrophe mutants defective in Wee1 kinase function at the restrictive temperature. The 3.0-kb cDNA clone contains an open reading frame (ORF) of 2226 nucleotides, encoding a predicted 82-kDa protein. The deduced amino acid (aa) sequence shows seven almost identical 30-aa tandem repeats, each of which contains a phosphorylation site meeting the consensus for both Cdc2 kinase and MAP kinase.","authors":"Su JY, Maller JL","authors_abbrev":"Su JY et al.","pubmed_publication_date":"22 Jul 1994","pubmed_entrez_date":"1994-07-22","publication_year":"1994","canto_session_key":"31e619f9512a4cb5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:17:35","canto_session_submitted_date":"2012-03-03 15:17:20","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:35055152","title":"Long RNA-Mediated Chromatin Regulation in Fission Yeast and Mammals.","citation":"Int J Mol Sci 2022 Jan 16;23(2)","abstract":"As part of a complex network of genome control, long regulatory RNAs exert significant influences on chromatin dynamics. Understanding how this occurs could illuminate new avenues for disease treatment and lead to new hypotheses that would advance gene regulatory research. Recent studies using the model fission yeast  Schizosaccharomyces pombe  ( S. pombe ) and powerful parallel sequencing technologies have provided many insights in this area. This review will give an overview of key findings in  S. pombe  that relate long RNAs to multiple levels of chromatin regulation: histone modifications, gene neighborhood regulation in  cis  and higher-order chromosomal ordering. Moreover, we discuss parallels recently found in mammals to help bridge the knowledge gap between the study systems.","doi":"10.3390/ijms23020968","authors":"Faber MW, Vo TV","authors_abbrev":"Faber MW et al.","pubmed_publication_date":"16 Jan 2022","pubmed_entrez_date":"2022-01-21","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-01-27 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29549126","title":"The major facilitator transporter Str3 is required for low-affinity heme acquisition in  Schizosaccharomyces pombe .","citation":"J Biol Chem 2018 Apr 27;293(17):6349-6362","abstract":"In the fission yeast  Schizosaccharomyces pombe , acquisition of exogenous heme is largely mediated by the cell membrane-associated Shu1. Here, we report that Str3, a member of the major facilitator superfamily of transporters, promotes cellular heme import. Using a strain that cannot synthesize heme  de novo  ( hem1 Δ) and lacks Shu1, we found that the heme-dependent growth deficit of this strain is rescued by hemin supplementation in the presence of Str3. Microscopic analyses of a  hem1 Δ  shu1 Δ  str3 Δ mutant strain in the presence of the heme analog zinc mesoporphyrin IX (ZnMP) revealed that ZnMP fails to accumulate within the mutant cells. In contrast, Str3-expressing  hem1 Δ  shu1 Δ cells could take up ZnMP at a 10-μm concentration. The yeast  Saccharomyces cerevisiae  cannot efficiently transport exogenously supplied hemin. However, heterologous expression of Str3 from  S. pombe  in  S. cerevisiae  resulted in ZnMP accumulation within  S. cerevisiae  cells. Moreover, hemin-agarose pulldown assays revealed that Str3 binds hemin. In contrast, an Str3 mutant in which Tyr and Ser residues of two putative heme-binding motifs ( 530 Y X  3 Y 534  and  552 S X  4 Y 557 ) had been replaced with alanines exhibited a loss of affinity for hemin. Furthermore, this Str3 mutant failed to rescue the heme-dependent growth deficit of a  hem1 Δ  shu1 Δ  str3 Δ strain. Further analysis by absorbance spectroscopy disclosed that a predicted extracellular loop region in Str3 containing the two putative heme-binding motifs interacts with hemin, with a  K D   of 6.6 μm Taken together, these results indicate that Str3 is a second cell-surface membrane protein for acquisition of exogenous heme in  S. pombe .","doi":"10.1074/jbc.RA118.002132","authors":"Normant V, Mourer T, Labbé S","authors_abbrev":"Normant V et al.","pubmed_publication_date":"27 Apr 2018","pubmed_entrez_date":"2018-03-18","publication_year":"2018","canto_session_key":"c6aa95e6f262f89b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-05 08:16:31","canto_approved_date":"2024-06-22 12:22:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-27 16:34:03","canto_added_date":"2018-03-21 01:15:15","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC359.05","SPAC2F3.09","SPAC1F8.03c","SPAC1F8.02c","SPAC23E2.01"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-06-05"},{"uniquename":"PMID:21288895","title":"Structure of a Ca2+-myristoyl switch protein that controls activation of a phosphatidylinositol 4-kinase in fission yeast.","citation":"J Biol Chem 2011 Apr 08;286(14):12565-77","abstract":"Neuronal calcium sensor (NCS) proteins transduce Ca2+ signals and are highly conserved from yeast to humans. We determined NMR structures of the NCS-1 homolog from fission yeast (Ncs1), which activates a phosphatidylinositol 4-kinase. Ncs1 contains an α-NH2-linked myristoyl group on a long N-terminal arm and four EF-hand motifs, three of which bind Ca2+, assembled into a compact structure. In Ca2+-free Ncs1, the N-terminal arm positions the fatty acyl chain inside a cavity near the C terminus. The C14 end of the myristate is surrounded by residues in the protein core, whereas its amide-linked (C1) end is flanked by residues at the protein surface. In Ca2+-bound Ncs1, the myristoyl group is extruded (Ca2+-myristoyl switch), exposing a prominent patch of hydrophobic residues that specifically contact phosphatidylinositol 4-kinase. The location of the buried myristate and structure of Ca2+-free Ncs1 are quite different from those in other NCS proteins. Thus, a unique remodeling of each NCS protein by its myristoyl group, and Ca2+-dependent unmasking of different residues, may explain how each family member recognizes distinct target proteins.","doi":"10.1074/jbc.M110.208868","authors":"Lim S, Strahl T, Thorner J, Ames JB","authors_abbrev":"Lim S et al.","pubmed_publication_date":"08 Apr 2011","pubmed_entrez_date":"2011-02-04","publication_year":"2011","canto_session_key":"2b4626e9f725d23e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-20 13:48:24","canto_approved_date":"2023-10-14 16:35:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-03 14:17:31","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.16c","SPAC18B11.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-11-20"},{"uniquename":"PMID:19230796","title":"The role of RAD6 in recombinational repair, checkpoints and meiosis via histone modification.","citation":"DNA Repair (Amst) 2009 Apr 05;8(4):470-82","abstract":"The Rad6 ubiquitin-conjugating enzyme in Saccharomyces cerevisiae is known to interact with three separate ubiquitin ligase proteins (Ubr1, Rad18, and Bre1) specific to different targets. The Rad6/Rad18 complex is central to translesion synthesis and the family of DNA transactions known as post-replication repair (PRR). A less well-known aspect of Rad6-mediated DNA repair, however, involves its function with Bre1 in mono-ubiquitinating the histone H2B residue lysine 123. Here, we review how this ubiquitination impacts histone H3 methylation, and how this in turn impacts the DNA damage response. In S. cerevisiae this pathway is required for checkpoint activation in G1, and contributes to DNA repair via the homologous recombination pathway (HRR) in G2 cells. Thus, RAD6 clearly plays a role in HRR in addition to its central role in PRR. We also summarize what is known about related repair pathways in other eukaryotes, including mammals. Recent literature emphasizes the role of methylated histones in S. cerevisiae, Schizosaccharomyces pombe and mammals in attracting the related DNA damage checkpoint proteins Rad9, Crb2 and 53BP1, respectively, to chromatin at the sites of DNA double-strand breaks. However, the specific histone modification pathways involved diverge in these different eukaryotes.","doi":"10.1016/j.dnarep.2009.01.007","authors":"Game JC, Chernikova SB","authors_abbrev":"Game JC et al.","pubmed_publication_date":"05 Apr 2009","pubmed_entrez_date":"2009-02-24","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30279276","title":"Differential GAP requirement for Cdc42-GTP polarization during proliferation and sexual reproduction.","citation":"J Cell Biol 2018 Dec 03;217(12):4215-4229","abstract":"The formation of a local zone of Cdc42 GTPase activity, which governs cell polarization in many cell types, requires not only local activation but also switch-off mechanisms. In this study, we identify Rga3, a paralog of Rga4, as a novel Cdc42 GTPase-activating protein (GAP) in the fission yeast  Schizosaccharomyces pombe  Contrary to Rga4, Rga3 localizes with Cdc42-GTP to sites of polarity. Rga3 is dispensable for cell polarization during mitotic growth, but it limits the lifetime of unstable Cdc42-GTP patches that underlie cell pairing during sexual reproduction, masking a partly compensatory patch-wandering motion. In consequence, cells lacking  rga3  hyperpolarize and lose out in mating competition. Rga3 synergizes with the Cdc42 GAPs Rga4 and Rga6 to restrict Cdc42-GTP zone sizes during mitotic growth. Surprisingly, triple-mutant cells, which are almost fully round, retain pheromone-dependent dynamic polarization of Cdc42-GTP, extend a polarized projection, and mate. Thus, the requirement for Cdc42-GTP hydrolysis by GAPs is distinct during polarization by intrinsic or extrinsic cues.","doi":"10.1083/jcb.201806016","authors":"Gallo Castro D, Martin SG","authors_abbrev":"Gallo Castro D et al.","pubmed_publication_date":"03 Dec 2018","pubmed_entrez_date":"2018-10-04","publication_year":"2018","canto_session_key":"4a2182374ad8d34e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2021-03-31 13:56:17","canto_approved_date":"2021-06-14 15:15:29","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-03-17 15:21:20","canto_added_date":"2018-10-05 00:15:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28E12.03","SPAC22H10.07","SPAC110.03","SPBC354.13","SPAC1296.03c","SPAC29A4.11"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2021-03-31"},{"uniquename":"PMID:8367291","title":"Subunits of the Schizosaccharomyces pombe RNA polymerase II: enzyme purification and structure of the subunit 3 gene.","citation":"Nucleic Acids Res 1993 Aug 11;21(16):3749-54","abstract":"To improve our understanding of the structure and function of eukaryotic RNA polymerase II, we purified the enzyme from the fission yeast Schizosaccharomyces pombe. The highly purified RNA polymerase II contained more than eleven polypeptides. The sizes of the largest the second-, and the third-largest polypeptides as measured by SDS-polyacrylamide gel electrophoresis were about 210, 150, and 40 kilodaltons (kDa), respectively, and are similar to those of RPB1, 2, and 3 subunits of Saccharomyces cerevisiae RNA polymerase II. Using the degenerated primers designed after amino acid micro-sequencing of the 40 kDa third-largest polypeptide (subunit 3), we cloned the subunit 3 gene (rpb3) and determined its DNA sequence. Taken together with the sequence of parts of PCR-amplified cDNA, the predicted coding sequence of rpb3, interrupted by two introns, was found to encode a polypeptide of 297 amino acid residues in length with a molecular weight of 34 kDa. The S. pombe subunit 3 contains four structural domains conserved for the alpha-subunit family of RNA polymerase from both eukaryotes and prokaryotes. A putative leucine zipper motif was found to exist in the C-terminal proximal conserved region (domain D). Possible functions of the conserved domains are discussed.","authors":"Azuma Y, Yamagishi M, Ishihama A","authors_abbrev":"Azuma Y et al.","pubmed_publication_date":"11 Aug 1993","pubmed_entrez_date":"1993-08-11","publication_year":"1993","canto_session_key":"bf0d5806b56b521d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-09-11 13:30:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-11 13:30:24","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1442.10c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-09-11"},{"uniquename":"PMID:22046364","title":"The fission yeast RNA binding protein Mmi1 regulates meiotic genes by controlling intron specific splicing and polyadenylation coupled RNA turnover.","citation":"PLoS One 2011;6(10):e26804","abstract":"The polyA tails of mRNAs are monitored by the exosome as a quality control mechanism. We find that fission yeast, Schizosaccharomyces pombe, adopts this RNA quality control mechanism to regulate a group of 30 or more meiotic genes at the level of both splicing and RNA turnover. In vegetative cells the RNA binding protein Mmi1 binds to the primary transcripts of these genes. We find the novel motif U(U/C/G)AAAC highly over-represented in targets of Mmi1. Mmi1 can specifically regulate the splicing of particular introns in a transcript: it inhibits the splicing of introns that are in the vicinity of putative Mmi1 binding sites, while allowing the splicing of other introns that are far from such sites. In addition, binding of Mmi1, particularly near the 3' end, alters 3' processing to promote extremely long polyA tails of up to a kilobase. The hyperadenylated transcripts are then targeted for degradation by the nuclear exonuclease Rrp6. The nuclear polyA binding protein Pab2 assists this hyperadenylation-mediated RNA decay. Rrp6 also targets other hyperadenylated transcripts, which become hyperadenylated in an unknown, but Mmi1-independent way. Thus, hyperadenylation may be a general signal for RNA degradation. In addition, binding of Mmi1 can affect the efficiency of 3' cleavage. Inactivation of Mmi1 in meiosis allows meiotic expression, through splicing and RNA stabilization, of at least 29 target genes, which are apparently constitutively transcribed.","doi":"10.1371/journal.pone.0026804","authors":"Chen HM, Futcher B, Leatherwood J","authors_abbrev":"Chen HM et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-11-03","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F3.01","SPCC736.12c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:30640914","title":"CDK contribution to DSB formation and recombination in fission yeast meiosis.","citation":"PLoS Genet 2019 Jan;15(1):e1007876","abstract":"CDKs (cyclin-dependent kinases) associate with different cyclins to form different CDK-complexes that are fundamental for an ordered cell cycle progression, and the coordination of this progression with different aspects of the cellular physiology. During meiosis programmed DNA double-strand breaks (DSBs) initiate recombination that in addition to generating genetic variability are essential for the reductional chromosome segregation during the first meiotic division, and therefore for genome stability and viability of the gametes. However, how meiotic progression and DSB formation are coordinated, and the role CDKs have in the process, is not well understood. We have used single and double cyclin deletion mutants, and chemical inhibition of global CDK activity using the cdc2-asM17 allele, to address the requirement of CDK activity for DSB formation and recombination in fission yeast. We report that several cyclins (Cig1, Cig2, and the meiosis-specific Crs1) control DSB formation and recombination, with a major contribution of Crs1. Moreover, complementation analysis indicates specificity at least for this cyclin, suggesting that different CDK complexes might act in different pathways to promote recombination. Down-regulation of CDK activity impinges on the formation of linear elements (LinEs, protein complexes required for break formation at most DSB hotspot sites). This defect correlates with a reduction in the capability of one structural component (Rec25) to bind chromatin, suggesting a molecular mechanism by which CDK controls break formation. However, reduction in DSB formation in cyclin deletion mutants does not always correspondingly correlate with a proportional reduction in meiotic recombination (crossovers), suggesting that specific CDK complexes might also control downstream events balancing repair pathways. Therefore, our work points to CDK regulation of DSB formation as a key conserved feature in the initiation of meiotic recombination, in addition to provide a view of possible roles CDK might have in other steps of the recombination process.","doi":"10.1371/journal.pgen.1007876","authors":"Bustamante-Jaramillo LF, Ramos C, Alonso L, Sesmero A, Segurado M, Martín-Castellanos C","authors_abbrev":"Bustamante-Jaramillo LF et al.","pubmed_publication_date":"Jan 2019","pubmed_entrez_date":"2019-01-15","publication_year":"2019","canto_session_key":"6e5ece46806fb848","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Cristina Martín-Castellanos","canto_first_approved_date":"2019-03-29 02:40:21","canto_approved_date":"2025-05-31 05:58:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-03-29 02:40:14","canto_added_date":"2019-01-16 01:15:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Cristina Martín-Castellanos","community_curator":true,"annotation_count":33,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC577.05c","SPBC19F5.01c","SPCC1322.13","SPCC4E9.02","SPBC1A4.02c","SPBC32F12.02","SPBC21H7.07c","SPCC1753.03c","SPBC11B10.09","SPAC17A5.18c","SPAPB2B4.03","SPAC25G10.04c","SPBC216.05","SPBC582.03","SPBC2G2.09c"],"gene_count":15,"ltp_gene_count":11,"approved_date":"2019-03-29"},{"uniquename":"EMBL:AU010226","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14765178","title":"Cell division: guardian spirit blesses meiosis.","citation":"Nature 2004 Feb 05;427(6974):495-7","abstract":"","authors":"Allshire R","authors_abbrev":"Allshire R","pubmed_publication_date":"05 Feb 2004","pubmed_entrez_date":"2004-02-07","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30108134","title":"Identification of an oncogenic network with prognostic and therapeutic value in prostate cancer.","citation":"Mol Syst Biol 2018 Aug 14;14(8):e8202","abstract":"Identifying critical pathways governing disease progression is essential for accurate prognosis and effective therapy. We developed a broadly applicable and novel systems-level gene discovery strategy. This approach focused on constitutively active androgen receptor (AR) splice variant-driven pathways as representative of an intractable mechanism of prostate cancer (PC) therapeutic resistance. We performed a meta-analysis of human prostate samples using weighted gene co-expression network analysis combined with experimental AR variant transcriptome analyses. An AR variant-driven gene module that is upregulated during human PC progression was identified. We filtered this module by identifying genes that functionally interacted with AR variants using a high-throughput synthetic genetic array screen in  Schizosaccharomyces pombe  This strategy identified seven AR variant-regulated genes that also enhance AR activity and drive cancer progression. Expression of the seven genes predicted poor disease-free survival in large independent PC patient cohorts. Pharmacologic inhibition of interacting members of the gene set potently and synergistically decreased PC cell proliferation. This unbiased and novel gene discovery strategy identified a clinically relevant, oncogenic, interacting gene hub with strong prognostic and therapeutic potential in PC.","doi":"10.15252/msb.20188202","authors":"Magani F, Bray ER, Martinez MJ, Zhao N, Copello VA, Heidman L, Peacock SO, Wiley DJ, D'Urso G, Burnstein KL","authors_abbrev":"Magani F et al.","pubmed_publication_date":"14 Aug 2018","pubmed_entrez_date":"2018-08-16","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-08-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013349","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8960127","title":"Analysis of spontaneous and double-strand break-induced recombination in rad mutants of S. pombe.","citation":"Mutat Res 1996 Dec 02;364(3):14-60","abstract":"Schizosaccharomyces pombe strains containing direct repeats of adeó heteroalleles separated by a functional uro4+ gene, and a DNA site for induction of a double-strand break (DSB), have been used to analyze pathways of spontaneous and DSB-induced intrachromosomal mitotic recombination. These substrates yield Ade+ Ura+ convertants or Ade+ Ura- deletions, by the DSB/gap repair and single-strand annealing (SSA) pathways of recombination, respectively. In S. cerevisiae, the DSB/gap repair pathway is RAD52 dependent, and the RAD1 and RAD10 genes are involved in the SSA pathway. We have sought to understand the genetic control of the pathways of mitotic recombination in S. pombe by determining the effects of mutations in six rad genes involved in DNA repair: rad1 and rad3 involved in checkpoint control in response to unreplicated or damaged DNA; rad5 (homologue of S. cerevisiae RAD3) and rad10 (homologue of S. cerevisiae RAD1) involved in nucleotide excision repair; rad21 and rad22 (homologue of S. cerevisiae RAD52) involved in the repair of ionizing radiation-induced DNA damage. The results suggest that the genetic control of the pathways of spontaneous and DSB-induced mitotic intrachromosomal recombination in S. pombe is different from that in S. cerevisiae.","authors":"Fortunato EA, Osman F, Subramani S","authors_abbrev":"Fortunato EA et al.","pubmed_publication_date":"02 Dec 1996","pubmed_entrez_date":"1996-12-02","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23108671","title":"Fission yeast TORC1 prevents eIF2α phosphorylation in response to nitrogen and amino acids via Gcn2 kinase.","citation":"J Cell Sci 2012 Dec 15;125(Pt 24):5955-9","abstract":"Serine 51 phosphorylation of the eukaryotic initiation factor-2α (eIF2α) is an important mechanism involved in blocking general protein synthesis in response to diverse types of stress. In fission yeast, three kinases (Hri1, Hri2 and Gcn2) can phosphorylate eIF2α at serine 51. In this study, we show that Tor2, as part of the TORC1 complex, prevents the phosphorylation of eIF2α in cells growing in the presence of nitrogen and amino acids. Inhibition of TORC1, either by rapamycin treatment, mutation of Tor2 or nitrogen deprivation, induces Gcn2-dependent phosphorylation of eIF2α.","doi":"10.1242/jcs.105395","authors":"Valbuena N, Rozalén AE, Moreno S","authors_abbrev":"Valbuena N et al.","pubmed_publication_date":"15 Dec 2012","pubmed_entrez_date":"2012-10-31","publication_year":"2012","canto_session_key":"09b918cc5a6b79f2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.07c","SPBC36B7.09"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:23727096","title":"Actin filament severing by cofilin dismantles actin patches and produces mother filaments for new patches.","citation":"Curr Biol 2013 Jul 08;23(13):1154-62","abstract":"Yeast cells depend on Arp2/3 complex to assemble actin filaments at sites of endocytosis, but the source of the initial filaments required to activate Arp2/3 complex is not known.\nWe tested the proposal that cofilin severs actin filaments during endocytosis in fission yeast cells using a mutant cofilin defective in severing. We used quantitative fluorescence microscopy to track mGFP-tagged proteins, including early endocytic adaptor proteins, activators of Arp2/3 complex, and actin filaments. Consistent with the hypothesis, actin patches disassembled far more slowly in cells depending on severing-deficient cofilin than in wild-type cells. Even more interesting, actin patches assembled slowly in these cofilin mutant cells. Adaptor proteins End4p and Pan1p accumulated and persisted at endocytic sites more than ten times longer than in wild-type cells, followed by slow but persistent recruitment of activators of Arp2/3 complex, including WASP and myosin-I. Mutations revealed that actin filament binding sites on adaptor proteins Pan1p and End4p contribute to initiating actin polymerization in actin patches.\nWe propose a \"sever, diffuse, and trigger\" model for the nucleation of actin filaments at sites of endocytosis, whereby cofilin generates actin filament fragments that diffuse through the cytoplasm, bind adaptor proteins at nascent sites of endocytosis, and serve as mother filaments to initiate the autocatalytic assembly of the branched actin filament network of each new patch. This hypothesis explains the source of the \"mother filaments\" that are absolutely required for Arp2/3 complex to nucleate actin polymerization.","doi":"10.1016/j.cub.2013.05.005","authors":"Chen Q, Pollard TD","authors_abbrev":"Chen Q et al.","pubmed_publication_date":"08 Jul 2013","pubmed_entrez_date":"2013-06-04","publication_year":"2013","canto_session_key":"39b02a678d369fc0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC162.07","SPAC25G10.09c","SPAC688.11","SPAC20G4.06c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:16278445","title":"Stress-activated protein kinase pathway functions to support protein synthesis and translational adaptation in response to environmental stress in fission yeast.","citation":"Eukaryot Cell 2005 Nov;4(11):1785-93","abstract":"The stress-activated protein kinase (SAPK) pathway plays a central role in coordinating gene expression in response to diverse environmental stress stimuli. We examined the role of this pathway in the translational response to stress in Schizosaccharomyces pombe. Exposing wild-type cells to osmotic stress (KCl) resulted in a rapid but transient reduction in protein synthesis. Protein synthesis was further reduced in mutants disrupting the SAPK pathway, including the mitogen-activated protein kinase Wis1 or the mitogen-activated protein kinase Spc1/Sty1, suggesting a role for these stress response factors in this translational control. Further polysome analyses revealed a role for Spc1 in supporting translation initiation during osmotic stress, and additionally in facilitating translational adaptation. Exposure to oxidative stress (H2O2) resulted in a striking reduction in translation initiation in wild-type cells, which was further reduced in spc1- cells. Reduced translation initiation correlated with phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (eIF2alpha) in wild-type cells. Disruption of Wis1 or Spc1 kinase or the downstream bZip transcription factors Atf1 and Pap1 resulted in a marked increase in eIF2alpha phosphorylation which was dependent on the eIF2alpha kinases Hri2 and Gcn2. These findings suggest a role for the SAPK pathway in supporting translation initiation and facilitating adaptation to environmental stress in part through reducing eIF2alpha phosphorylation in fission yeast.","authors":"Dunand-Sauthier I, Walker CA, Narasimhan J, Pearce AK, Wek RC, Humphrey TC","authors_abbrev":"Dunand-Sauthier I et al.","pubmed_publication_date":"Nov 2005","pubmed_entrez_date":"2005-11-10","publication_year":"2005","canto_session_key":"2896b103353173f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-11 16:29:19","canto_approved_date":"2017-10-11 16:29:19","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-10-11 16:29:11","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.03c","SPBC36B7.09","SPAC3G9.09c","SPAC222.07c","SPBC409.07c","SPBC29B5.01","SPAC24B11.06c","SPAC1783.07c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2017-10-11"},{"uniquename":"PMID:11795845","title":"The role of DSC1 components cdc10+, rep1+ and rep2+ in MCB gene transcription at the mitotic G1-S boundary in fission yeast.","citation":"Curr Genet 2001 Dec;40(4):251-9","abstract":"In this paper, we describe the transcription profile of a group of genes at the G1-S boundary of fission yeast in synchronously dividing mitotic cells, under a variety of different conditions. This transcription profile is unaffected in cells where either cdc10+ or cdc10-C4 are constitutively overexpressed. In contrast, overexpression of either rep1+ or rep2+ results in constitutive expression of MCB-regulated genes, suggesting that these polypeptides have important regulatory properties in controlling MCB transcription. Finally, we examine the pattern of MCB-regulated transcription in cells where the G1 period is extended. Surprisingly, we find that the wee1-50 mutation causes MCB transcription throughout the cell cycle, whereas cells re-fed after nitrogen starvation have normal expression patterns. The implications of these observations for understanding MCB-regulated transcription are discussed.","authors":"White S, Khaliq F, Sotiriou S, McInerny CJ","authors_abbrev":"White S et al.","pubmed_publication_date":"Dec 2001","pubmed_entrez_date":"2002-01-25","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2D10.06","SPBC336.12c"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:16550352","title":"A starvation-specific serine protease gene, isp6+, is involved in both autophagy and sexual development in Schizosaccharomyces pombe.","citation":"Curr Genet 2006 Jun;49(6):403-13","abstract":"Schizosaccharomyces pombe isp6(+) gene encodes a vacuolar serine protease, which is specifically induced during nitrogen starvation. An isp6-disruption mutant, isp6Delta, grew normally under normal conditions but was defective in large-scale protein degradation during nitrogen starvation, a hallmark of autophagy. Vacuoles are the organelles for such drastic protein degradation but those of isp6Delta were apparently aberrant. isp6Delta was infertile under nitrogen source-free conditions with poor expression of ste11(+), a gene critical for sexual development. A protein kinase A-disruption mutant, pka1Delta, is prone to sexual development because expression of ste11(+) is derepressed. However, isp6Deltapka1Delta still showed defects in ste11(+) expression and sexual development under nitrogen source-free conditions. isp6Delta and isp6Deltapka1Delta were able to initiate sexual development to produce spores when only a small amount of a nitrogen source was present. Pat1 protein kinase negatively controls meiosis, and a temperature-sensitive mutant of pat1, pat1-114, initiates meiosis irrespective of ploidy at the restrictive temperature. However, isp6Deltapat1-114 did not start meiosis under nitrogen source-free conditions even at the restrictive temperature. These observations suggest that isp6(+) contributes to sexual development by providing a nitrogen source through autophagy.","authors":"Nakashima A, Hasegawa T, Mori S, Ueno M, Tanaka S, Ushimaru T, Sato S, Uritani M","authors_abbrev":"Nakashima A et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-03-22","publication_year":"2006","canto_session_key":"b00d5cd157407943","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-01-15 20:14:08","canto_approved_date":"2024-12-12 13:37:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-10-21 09:23:49","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.03","SPBC30D10.10c","SPBC29B5.01","SPAC4A8.04","SPBC409.07c","SPBC32C12.02","SPBC106.10","SPBC19C2.05"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2018-01-15"},{"uniquename":"PMID:29165593","title":"FunCoup 4: new species, data, and visualization.","citation":"Nucleic Acids Res 2018 Jan 04;46(D1):D601-D607","abstract":"This release of the FunCoup database (http://funcoup.sbc.su.se) is the fourth generation of one of the most comprehensive databases for genome-wide functional association networks. These functional associations are inferred via integrating various data types using a naive Bayesian algorithm and orthology based information transfer across different species. This approach provides high coverage of the included genomes as well as high quality of inferred interactions. In this update of FunCoup we introduce four new eukaryotic species: Schizosaccharomyces pombe, Plasmodium falciparum, Bos taurus, Oryza sativa and open the database to the prokaryotic domain by including networks for Escherichia coli and Bacillus subtilis. The latter allows us to also introduce a new class of functional association between genes - co-occurrence in the same operon. We also supplemented the existing classes of functional association: metabolic, signaling, complex and physical protein interaction with up-to-date information. In this release we switched to InParanoid v8 as the source of orthology and base for calculation of phylogenetic profiles. While populating all other evidence types with new data we introduce a new evidence type based on quantitative mass spectrometry data. Finally, the new JavaScript based network viewer provides the user an intuitive and responsive platform to further evaluate the results.","doi":"10.1093/nar/gkx1138","authors":"Ogris C, Guala D, Sonnhammer ELL","authors_abbrev":"Ogris C et al.","pubmed_publication_date":"04 Jan 2018","pubmed_entrez_date":"2017-11-23","publication_year":"2018","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2017-11-24 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8887664","title":"Perturbations in the spi1p GTPase cycle of Schizosaccharomyces pombe through its GTPase-activating protein and guanine nucleotide exchange factor components result in similar phenotypic consequences.","citation":"Mol Cell Biol 1996 Nov;16(11):6352-62","abstract":"spi1p of Schizosaccharomyces pombe is a structural homolog of the mammalian GTPase Ran. The distribution between the GTP- and GDP-bound forms of the protein is regulated by evolutionarily conserved gene products, rna1p and pim1p, functioning as GTPase-activating protein (GAP) and guanine nucleotide exchange factor (GEF), respectively. Antibodies to spi1p, pim1p, and rna1p were generated and used to demonstrate that pim1p is exclusively nuclear, while rna1p is cytoplasmic. A loss of pim1p GEF activity or an increase in the rna1p GAP activity correlates with a change in the localization of the GTPase from predominantly nuclear to uniformly distributed, suggesting that the two forms are topologically segregated and that the nucleotide-bound state of spi1p may dictate its intracellular localization. We demonstrate that the phenotype of cells overproducing the GAP resembles the previously reported phenotype of mutants with alterations in the GEF: the cells are arrested in the cell cycle as septated, binucleated cells with highly condensed chromatin, fragmented nuclear envelopes, and abnormally wide septa. Consistent with the expectation that either an increased dosage of the GAP or a mutation in the GEF would lead to an increase of the spi1p-GDP/spi1p-GTP ratio relative to that of wild-type cells, overexpression of the GAP together with a mutation in the GEF is synthetically lethal. The similar phenotypic consequences of altering the functioning of the nuclear GEF or the cytoplasmic GAP suggest that there is a single pool of the spi1p GTPase that shuttles between the nucleus and the cytoplasm. Phenotypically, rna1 null mutants, in which spi1p-GTP would be expected to accumulate, resemble pim1(ts) and rna1p-overproducing cells, in which spi1p-GDP would be expected to accumulate. Taken together, these results support the hypothesis that the balance between the GDP- and GTP-bound forms of spi1p mediates the host of nuclear processes that are adversely affected when the functioning of different components of this system is perturbed in various organisms.","authors":"Matynia A, Dimitrov K, Mueller U, He X, Sazer S","authors_abbrev":"Matynia A et al.","pubmed_publication_date":"Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22E12.07","SPBC1289.03c","SPBC557.03c"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:16491466","title":"Construction of a protease-deficient strain set for the fission yeast Schizosaccharomyces pombe, useful for effective production of protease-sensitive heterologous proteins.","citation":"Yeast 2006 Jan 30;23(2):83-99","abstract":"One of the major problems hindering effective production and purification of heterologous proteins from the fission yeast Schizosaccharomyces pombe is proteolytic degradation of the recombinant gene products by host-specific proteases. As an initial solution to this problem, we constructed a protease-deficient disruptant set by respective disruption of 52 Sz. pombe protease genes. Functional screening of the resultant set was performed by observing secretory production of a proteolytically sensitive model protein, human growth hormone (hGH). The results indicated that some of the resultant disruptants were effective in reducing hGH degradation, as observed during the hGH expression procedure and mainly as a result of unknown serine- and/or cysteine-type proteases in the culture medium. These findings also demonstrated that construction of a protease-deficient strain set is not only useful for practical application in protein production, but also for functional screening, specification and modification of proteases in Sz. pombe, where further investigations of proteolytic processes and improvement through multiple gene manipulations are required.","authors":"Idiris A, Bi K, Tohda H, Kumagai H, Giga-Hama Y","authors_abbrev":"Idiris A et al.","pubmed_publication_date":"30 Jan 2006","pubmed_entrez_date":"2006-02-24","publication_year":"2006","canto_session_key":"443e3e7b8c5be9bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-09-28 20:20:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-02-15 14:55:41","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.12c","SPACUNK4.08","SPAC1F3.10c","SPAC3A11.10c","SPBC13E7.11","SPBC16G5.09","SPCC1259.02c","SPAC1006.01","SPBC543.09","SPAC4F10.02","SPBC1685.05","SPBC1921.05","SPCC1795.09","SPAC24C9.08","SPCC1840.04","SPBC119.17","SPAC13A11.05","SPBP23A10.15c","SPCC613.10","SPAC17A5.04c","SPBC18A7.01","SPBC1711.12","SPBC18E5.12c","SPBC336.13c","SPAC12B10.05","SPAC25B8.17","SPAC607.06c","SPAP14E8.04","SPCC965.12","SPAC19B12.08","SPBC1685.03","SPCC1259.10","SPAC22E12.09c","SPBC2D10.07c","SPAC14C4.15c","SPCC1322.05c","SPCC965.04c","SPBC23E6.05","SPAC19B12.06c","SPAC19G12.10c","SPAC3H1.05","SPBC16D10.03","SPBC3E7.10","SPAC22G7.01c","SPCC757.05c","SPAC3H1.02c","SPAC4A8.04","SPCC790.03","SPBC337.07c","SPACUNK4.12c","SPAC1296.03c","SPBP4H10.10","SPAC1687.02","SPAC26A3.01","SPBC14C8.03","SPAC22F3.06c","SPBC1198.08","SPBC354.09c","SPCC5E4.04","SPCC1919.12c","SPCC11E10.02c","SPAC23H4.09"],"gene_count":62,"ltp_gene_count":22,"approved_date":"2016-02-15"},{"uniquename":"PMID:23555033","title":"Fission yeast CSL proteins function as transcription factors.","citation":"PLoS One 2013;8(3):e59435","abstract":"Transcription factors of the CSL (CBF1/RBP-Jk/Suppressor of Hairless/LAG-1) family are key regulators of metazoan development and function as the effector components of the Notch receptor signalling pathway implicated in various cell fate decisions. CSL proteins recognize specifically the GTG[G/A]AA sequence motif and several mutants compromised in their ability to bind DNA have been reported. In our previous studies we have identified a number of novel putative CSL family members in fungi, organisms lacking the Notch pathway. It is not clear whether these represent genuine CSL family members.\nUsing a combination of in vitro and in vivo approaches we characterized the DNA binding properties of Cbf11 and Cbf12, the antagonistic CSL paralogs from the fission yeast, important for the proper coordination of cell cycle events and the regulation of cell adhesion. We have shown that a mutation of a conserved arginine residue abolishes DNA binding in both CSL paralogs, similar to the situation in mouse. We have also demonstrated the ability of Cbf11 and Cbf12 to activate gene expression in an autologous fission yeast reporter system.\nOur results indicate that the fission yeast CSL proteins are indeed genuine family members capable of functioning as transcription factors, and provide support for the ancient evolutionary origin of this important protein family.","doi":"10.1371/journal.pone.0059435","authors":"Oravcová M, Teska M, Půta F, Folk P, Převorovský M","authors_abbrev":"Oravcová M et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-04-05","publication_year":"2013","canto_session_key":"a78bfbf7b3a5462a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Martin Převorovský","canto_first_approved_date":"2019-01-29 10:58:24","canto_approved_date":"2025-09-04 10:04:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-29 10:58:15","canto_added_date":"2013-05-13 07:57:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Martin Převorovský","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.13","SPCC736.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-01-29"},{"uniquename":"PMID:18216783","title":"Cell cycle control of centromeric repeat transcription and heterochromatin assembly.","citation":"Nature 2008 Feb 07;451(7179):734-7","abstract":"Heterochromatin in eukaryotic genomes regulates diverse chromosomal processes including transcriptional silencing. However, in Schizosaccharomyces pombe RNA polymerase II (RNAPII) transcription of centromeric repeats is essential for RNA-interference-mediated heterochromatin assembly. Here we study heterochromatin dynamics during the cell cycle and its effect on RNAPII transcription. We describe a brief period during the S phase of the cell cycle in which RNAPII preferentially transcribes centromeric repeats. This period is enforced by heterochromatin, which restricts RNAPII accessibility at centromeric repeats for most of the cell cycle. RNAPII transcription during S phase is linked to loading of RNA interference and heterochromatin factors such as the Ago1 subunit of the RITS complex and the Clr4 methyltransferase complex subunit Rik1 (ref. 7). Moreover, Set2, an RNAPII-associated methyltransferase that methylates histone H3 lysine 36 at repeat loci during S phase, acts in a pathway parallel to Clr4 to promote heterochromatin assembly. We also show that phosphorylation of histone H3 serine 10 alters heterochromatin during mitosis, correlating with recruitment of condensin that affects silencing of centromeric repeats. Our analyses suggest at least two distinct modes of heterochromatin targeting to centromeric repeats, whereby RNAPII transcription of repeats and chromodomain proteins bound to methylated histone H3 lysine 9 mediate recruitment of silencing factors. Together, these processes probably facilitate heterochromatin maintenance through successive cell divisions.","doi":"10.1038/nature06561","authors":"Chen ES, Zhang K, Nicolas E, Cam HP, Zofall M, Grewal SI","authors_abbrev":"Chen ES et al.","pubmed_publication_date":"07 Feb 2008","pubmed_entrez_date":"2008-01-25","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.02c","SPBC428.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:38657142","title":"Parallel genetic screens identify nuclear envelope homeostasis as a key determinant of telomere entanglement resolution in fission yeast.","citation":"G3 (Bethesda) 2024 Apr 25;","abstract":"In fission yeast lacking the telomere binding protein, Taz1, replication forks stall at telomeres, triggering deleterious downstream events. Strand invasion from one taz1Δ telomeric stalled fork to another on a separate (non-sister) chromosome leads to telomere entanglements, which are resolved in mitosis at 32°C; however, entanglement resolution fails at ≤20°C, leading to cold-specific lethality. Previously, we found that loss of the mitotic function of Rif1, a conserved DNA replication and repair factor, suppresses cold sensitivity by promoting resolution of entanglements without affecting entanglement formation. To understand the underlying pathways of mitotic entanglement resolution, we performed a series of genomewide synthetic genetic array screens to generate a comprehensive list of genetic interactors of taz1Δ and rif1Δ. We modified a previously described screening method to ensure that the queried cells were kept in log phase growth. In addition to recapitulating previously identified genetic interactions, we find that loss of genes encoding components of the nuclear pore complex (NPC) promotes telomere disentanglement and suppresses taz1Δ cold sensitivity. We attribute this to more rapid anaphase midregion nuclear envelope (NE) breakdown in the absence of these NPC components. Loss of genes involved in lipid metabolism reverses the ability of rif1+ deletion to suppress taz1Δ cold sensitivity, again pinpointing NE modulation. A rif1+ separation-of-function mutant that specifically loses Rif1's mitotic functions yields similar genetic interactions. Genes promoting membrane fluidity were enriched in a parallel taz1+ synthetic lethal screen at permissive temperature, cementing the idea that the cold specificity of taz1Δ lethality stems from altered NE homeostasis.","doi":"10.1093/g3journal/jkae078","authors":"Nageshan RK, Krogan N, Cooper JP","authors_abbrev":"Nageshan RK et al.","pubmed_publication_date":"25 Apr 2024","pubmed_entrez_date":"2024-04-24","publication_year":"2024","canto_session_key":"f3487f0614f1515f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-04-24 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8832414","title":"The Schizosaccharomyces pombe pyp1 protein tyrosine phosphatase negatively regulates nutrient monitoring pathways.","citation":"J Cell Sci 1996 Jul;109 ( Pt 7)(0 7):1919-1925","abstract":"The Schizosaccharomyces pombe pyp1+ gene, encoding a protein tyrosine phosphatase (pyp1), was isolated as a high copy number suppressor of a mutation that results in reduced cAMP-dependent protein kinase (PKA) activity. Overexpression of pyp1+ inhibits both transcription of the fbp1 gene, which is negatively regulated by a glucose-induced activation of PKA, and sexual development, which is negatively regulated by PKA through a nitrogen- and glucose-monitoring mechanism. Overexpression of a catalytically inactive form of pyp1 has little effect on either process. Previous studies suggest that overexpression of pyp1+ results in a mitotic delay by positively regulating wee1 activity. We show that pyp1 repression of fbp1 transcription is independent of wee1. The direct role of the pyp1 protein is to dephosphorylate and inactivate the sty1/spc1 mitogen-activated protein kinase (MAPK) that is activated by the wis1 MAPK kinase. As overexpression of pyp1+ has no further effect upon the mitotic delay observed in a wis1 deletion strain, the role of pyp1 appears to be restricted to negative regulation of the sty1/spc1 MAPK. This study indicates that pyp1 negatively regulates fbp1 transcription, sexual development and mitosis by inactivation of the sty1/spc1 MAPK, but that bifurcations downstream of the MAPK separate these processes as seen by the differential role for the wee1 gene.","authors":"Santo PD, Blanchard B, Hoffman CS","authors_abbrev":"Santo PD et al.","pubmed_publication_date":"Jul 1996","pubmed_entrez_date":"1996-07-01","publication_year":"1996","canto_session_key":"2ada49dc0d73c586","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-13 16:04:16","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-13 16:03:46","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19D5.01","SPBC106.10","SPBC32H8.07","SPCC1753.02c","SPBC21C3.20c","SPCC18B5.03","SPBC19C7.03","SPBC36.12c","SPAC926.04c","SPAC23H3.13c","SPAC26F1.10c"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2014-08-13"},{"uniquename":"PMID:10923028","title":"The mating-type region of Schizosaccharomyces pombe h(-S) 972: sequencing and analysis of 69 kb including the expressed mat1 locus.","citation":"Yeast 2000 Aug;16(11):1061-7","abstract":"The sequence has been determined of 68 897 bp of genomic DNA including the expressed mat1 mating-type locus from Schizosaccharomyces pombe h(-S) strain 972. The DNA sequence, located on the long arm of fission yeast chromosome II and contained in two cosmid clones, was analysed to reveal one autonomously replicating sequence, two retrotransposon long terminal repeats (LTRs), one tRNA(Gly) gene and 33 open reading frames (ORFs), of which 15 contain introns. Nine of these ORFs code for previously described genes (trt1, rpl10, rps21, nif1, sui1 (psu1), matMi, matMc, let1 and rpa4), one of which (trt1) contains 15 introns, the highest number yet recorded in a gene of S. pombe. Of the remaining 24 ORFs, sequence similarity suggests that the function of 13 of the encoded proteins may be predicted and these include four mitochondrial proteins, two transport proteins, two signalling molecules, a component of serine palmitolytransferase, a homologue of 3-methyladenine DNA glycosylase, a multifunctional alcohol dehydrogenase, a killer toxin sensitivity factor and an acetyl transferase. Six deduced sequences appear to be related to proteins of unknown function in Saccharomyces cerevisiae or S. pombe and the remaining five are hypothetical proteins.","authors":"Xiang Z, Wood V, Rajandream MA, Barrell BG, Moore K, Hunt C, Aves SJ","authors_abbrev":"Xiang Z et al.","pubmed_publication_date":"Aug 2000","pubmed_entrez_date":"2000-08-03","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15635094","title":"Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I.","citation":"Mol Biol Cell 2005 Mar;16(3):1439-48","abstract":"Within the endoplasmic reticulum (ER), mannoses and glucoses, donated from dolichol-phosphate-mannose and -glucose, are transferred to N-glycan and GPI-anchor precursors, and serine/threonine residues in many proteins. Glycosyltransferases that mediate these reactions are ER-resident multitransmembrane proteins with common characteristics, forming a superfamily of >10 enzymes. Here, we report an essential component of glycosylphosphatidylinositol-mannosyltransferase I (GPI-MT-I), which transfers the first of the four mannoses in the GPI-anchor precursors. We isolated a Chinese hamster ovary (CHO) cell mutant defective in GPI-MT-I but not its catalytic component PIG-M. The mutant gene, termed phosphatidylinositolglycan-class X (PIG-X), encoded a 252-amino acid ER-resident type I transmembrane protein with a large lumenal domain. PIG-X and PIG-M formed a complex, and PIG-M expression was <10% in the absence of PIG-X, indicating that PIG-X stabilizes PIG-M. We found that Saccharomyces cerevisiae Pbn1p/YCL052Cp, which was previously reported to be involved in autoprocessing of proproteinase B, is the functional homologue of PIG-X; Pbn1p is critical for Gpi14p/YJR013Wp function, the yeast homologue of PIG-M. This is the first report of an essential subcomponent of glycosyltransferases using dolichol-phosphate-monosaccharide.","authors":"Ashida H, Hong Y, Murakami Y, Shishioh N, Sugimoto N, Kim YU, Maeda Y, Kinoshita T","authors_abbrev":"Ashida H et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2005-01-07","publication_year":"2005","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC13E7.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22971103","title":"Influence of peptide dipoles and hydrogen bonds on reactive cysteine pKa values in fission yeast DJ-1.","citation":"FEBS J 2012 Nov;279(22):4111-20","abstract":"Cysteine residues with depressed pK(a) values are critical for the functions of many proteins. Several types of interactions can stabilize cysteine thiolate anions, including hydrogen bonds between thiol(ate)s and nearby residues as well as electrostatic interactions involving charged residues or dipoles. Dipolar stabilization of thiolates by peptide groups has been suggested to play a particularly important role near the N-termini of α-helices. Using a combination of X-ray crystallography, site-directed mutagenesis and spectroscopic methods, we show that the reactive cysteine residue (Cys111) in Schizosaccharomyces pombe DJ-1 experiences a 0.6 unit depression of its thiol pK(a) as a consequence of a hydrogen bond donated by a threonine side chain (Thr114) to a nearby peptide carbonyl oxygen at the N-terminus of an α-helix. This extended hydrogen bonded interaction is consistent with a sum of dipoles model whereby the distal hydrogen bond polarizes and strengthens the direct hydrogen bond between the proximal amide hydrogen and the cysteine thiol(ate). Therefore, our results suggest that the local dipolar enhancement of hydrogen bonds can appreciably stabilize cysteine thiolate formation. However, the substitution of a valine residue with a proline at the i + 3 position has only a minor effect (0.3 units) on the pK(a) of Cys111. As proline has a reduced peptide dipole moment, this small effect suggests that a more extended helix macrodipolar effect does not play a major role in this system.","doi":"10.1111/febs.12004","authors":"Madzelan P, Labunska T, Wilson MA","authors_abbrev":"Madzelan P et al.","pubmed_publication_date":"Nov 2012","pubmed_entrez_date":"2012-09-14","publication_year":"2012","canto_session_key":"18d9978112bca10a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-02-17 11:20:34","canto_approved_date":"2023-02-17 11:20:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 11:20:25","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22E12.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-17","pdb_entries":[{"pdb_id":"4qyt","gene_chains":[{"gene_uniquename":"SPAC22E12.03c","chain":"A/B/C/D","position":"1-191"}],"title":"Schizosaccharomyces pombe DJ-1","entry_authors":"Wilson MA","entry_authors_abbrev":"Wilson MA","reference_uniquename":"PMID:22971103","experimental_method":"X-ray","resolution":"1.05"},{"pdb_id":"4ge3","gene_chains":[{"gene_uniquename":"SPAC22E12.03c","chain":"A/B/C/D","position":"1-191"}],"title":"Schizosaccharomyces pombe DJ-1 T114V mutant","entry_authors":"Madzelan P,Labunska T,Wilson MA","entry_authors_abbrev":"Madzelan P et al.","reference_uniquename":"PMID:22971103","experimental_method":"X-ray","resolution":"1.5"},{"pdb_id":"4ge0","gene_chains":[{"gene_uniquename":"SPAC22E12.03c","chain":"A/B/C/D","position":"1-191"}],"title":"Schizosaccharomyces pombe DJ-1 T114P mutant","entry_authors":"Madzelan P,Labunska T,Wilson MA","entry_authors_abbrev":"Madzelan P et al.","reference_uniquename":"PMID:22971103","experimental_method":"X-ray","resolution":"1.45"}]},{"uniquename":"PMID:9436303","title":"Polarity, spatial organisation of cytoskeleton, and nuclear division in morphologically altered cells of Schizosaccharomyces pombe.","citation":"Can J Microbiol 1997 Nov;43(11):991-8","abstract":"To gain more information about the determination of cell polarity and its relationship to the organisation of cytoskeleton, we have examined the mycelial mutant sep1-1 and the multinucleate multipolar syncytia of the triple mutant sep1-1 spl1-1 cdc4-8 by indirect immunofluorescence techniques. We have found that polarity is predetermined by the shape of the cell. During transition from mitosis to interphase the microtubules of the arising cytoplasmic cytoskeleton gradually form a basket-like pattern that reflects the curvatures of the cell envelope. The presumable growing poles, where actin accumulates, usually correlates with sites where the cell tapers and the microtubules converge. However, no growth can be launched at these sites if the cell surface has not been properly processed. Mitosis and meiosis are not affected significantly by changes in cell morphology and polarity, but larger cells are less effective during sporulation. The azygotic asci produced by multinucleate syncytia frequently contain over 20 ascospores.","authors":"Sipiczki M, Grallert A","authors_abbrev":"Sipiczki M et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-01-22","publication_year":"1997","canto_session_key":"70c279647d8b2d7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-31 12:01:40","canto_approved_date":"2019-01-31 12:01:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-01-31 12:01:32","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08","SPBC4C3.12","SPATRNAPRO.02"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-01-31"},{"uniquename":"PMID:18716626","title":"Heterochromatin links to centromeric protection by recruiting shugoshin.","citation":"Nature 2008 Sep 11;455(7210):251-5","abstract":"The centromere of a chromosome is composed mainly of two domains, a kinetochore assembling core centromere and peri-centromeric heterochromatin regions. The crucial role of centromeric heterochromatin is still unknown, because even in simpler unicellular organisms such as the fission yeast Schizosaccharomyces pombe, the heterochromatin protein Swi6 (HP1 homologue) has several functions at centromeres, including silencing gene expression and recombination, enriching cohesin, promoting kinetochore assembly, and, ultimately, preventing erroneous microtubule attachment to the kinetochores. Here we show that the requirement of heterochromatin for mitotic chromosome segregation is largely replaced by forcibly enriching cohesin at centromeres in fission yeast. However, this enrichment of cohesin is not sufficient to replace the meiotic requirement for heterochromatin. We find that the heterochromatin protein Swi6 associates directly with meiosis-specific shugoshin Sgo1, a protector of cohesin at centromeres. A point mutation of Sgo1 (V242E), which abolishes the interaction with Swi6, impairs the centromeric localization and function of Sgo1. The forced centromeric localization of Sgo1 restores proper meiotic chromosome segregation in swi6 cells. We also show that the direct link between HP1 and shugoshin is conserved in human cells. Taken together, our findings suggest that the recruitment of shugoshin is the important primary role for centromeric heterochromatin in ensuring eukaryotic chromosome segregation.","doi":"10.1038/nature07217","authors":"Yamagishi Y, Sakuno T, Shimura M, Watanabe Y","authors_abbrev":"Yamagishi Y et al.","pubmed_publication_date":"11 Sep 2008","pubmed_entrez_date":"2008-08-22","publication_year":"2008","canto_session_key":"ea1ec138d2671e21","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-04-25 11:08:54","canto_approved_date":"2024-04-02 11:51:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-04-15 10:44:12","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPBP35G2.03c","SPAC17H9.20","SPBC428.08c","SPAC664.01c","SPCC188.02"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2022-04-25"},{"uniquename":"PMID:29145618","title":"The histone variant H2A.Z promotes initiation of meiotic recombination in fission yeast.","citation":"Nucleic Acids Res 2018 Jan 25;46(2):609-620","abstract":"Meiotic recombination is initiated by programmed formation of DNA double strand breaks (DSBs), which are mainly formed at recombination hotspots. Meiotic DSBs require multiple proteins including the conserved protein Spo11 and its cofactors, and are influenced by chromatin structure. For example, local chromatin around hotspots directly impacts DSB formation. Moreover, DSB is proposed to occur in a higher-order chromatin architecture termed 'axis-loop', in which many loops protrude from cohesin-enriched axis. However, still much remains unknown about how meiotic DSBs are generated in chromatin. Here, we show that the conserved histone H2A variant H2A.Z promotes meiotic DSB formation in fission yeast. Detailed investigation revealed that H2A.Z is neither enriched around hotspots nor axis sites, and that transcript levels of DSB-promoting factors were maintained without H2A.Z. Moreover, H2A.Z appeared to be dispensable for chromatin binding of meiotic cohesin. Instead, in H2A.Z-lacking mutants, multiple proteins involved in DSB formation, such as the fission yeast Spo11 homolog and its regulators, were less associated with chromatin. Remarkably, nuclei were more compact in the absence of H2A.Z. Based on these, we propose that fission yeast H2A.Z promotes meiotic DSB formation partly through modulating chromosome architecture to enhance interaction between DSB-related proteins and cohesin-loaded chromatin.","doi":"10.1093/nar/gkx1110","authors":"Yamada S, Kugou K, Ding DQ, Fujita Y, Hiraoka Y, Murakami H, Ohta K, Yamada T","authors_abbrev":"Yamada S et al.","pubmed_publication_date":"25 Jan 2018","pubmed_entrez_date":"2017-11-18","publication_year":"2018","canto_session_key":"feefda5b01172064","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-11-19 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34005159","canto_session_key":"e79e3054a0b44e87","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29851556","title":"Mre11-Rad50-dependent activity of ATM/Tel1 at DNA breaks and telomeres in the absence of Nbs1.","citation":"Mol Biol Cell 2018 Jun 01;29(11):1389-1399","abstract":"The Mre11-Rad50-Nbs1 (MRN) protein complex and ATM/Tel1 kinase protect genome integrity through their functions in DNA double-strand break (DSB) repair, checkpoint signaling, and telomere maintenance. Nbs1 has a conserved C-terminal motif that binds ATM/Tel1, but the full extent and significance of ATM/Tel1 interactions with MRN are unknown. Here, we show that Tel1 overexpression bypasses the requirement for Nbs1 in DNA damage signaling and telomere maintenance. These activities require Mre11-Rad50, which localizes to DSBs and bind Tel1 in the absence of Nbs1. Fusion of the Tel1-binding motif of Nbs1 to Mre11 is sufficient to restore Tel1 signaling in nbs1Δ cells. Tel1 overexpression does not restore Tel1 signaling in cells carrying the rad50-I1192W mutation, which impairs the ability of Mre11-Rad50 to form the ATP-bound closed conformation. From these findings, we propose that Tel1 has a high-affinity interaction with the C-terminus of Nbs1 and a low-affinity association with Mre11-Rad50, which together accomplish efficient localization and activation of Tel1 at DSBs and telomeres.","doi":"10.1091/mbc.E17-07-0470","authors":"Limbo O, Yamada Y, Russell P","authors_abbrev":"Limbo O et al.","pubmed_publication_date":"01 Jun 2018","pubmed_entrez_date":"2018-06-01","publication_year":"2018","canto_session_key":"d68133bbe06d0602","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2019-05-10 14:50:42","canto_approved_date":"2024-07-04 06:38:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-03 21:03:16","canto_added_date":"2019-03-10 01:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Oliver Limbo","community_curator":true,"annotation_count":37,"orcid":null,"file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.09c","SPCC1259.13","SPAC3G6.06c","SPAC1556.01c","SPBC216.05","SPCC23B6.03c","SPAC13C5.07"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2019-05-10"},{"uniquename":"PMID:18466295","title":"The Schizosaccharomyces pombe endo-1,3-beta-glucanase Eng1 contains a novel carbohydrate binding module required for septum localization.","citation":"Mol Microbiol 2008 Jul;69(1):188-200","abstract":"Cell separation in Schizosaccharomyces pombe is achieved through the concerted action of the Eng1 endo-beta-1,3-glucanase and the Agn1 endo-alpha-1,3-glucanase, which are transported to the septum and localize to a ring-like structure that surrounds the septum. Correct localization of these hydrolases requires the presence of both the septins and the exocyst. In this work, we show that the glucanase Eng1 contains a region at the C-terminus that acts as a carbohydrate-binding module (CBM) and that it is not present in other members of glycoside hydrolases family 81 (GH81). In vitro, the purified CBM has affinity for beta-1,3-glucan chains with a minimum degree of polymerization of 30 glucose units. Deletion of the CBM results in a protein that is largely defective in complementing the separation defect of eng1Delta mutants. This defect is due to a reduction in the catalytic activity against insoluble substrates and to a defect in targeting of Eng1 to the septum, as the truncated protein localizes to the lateral cell wall of the cell. Thus, the targeting of Eng1 to the primary septum requires not only trans-factors (septins and the exocyst complex) but also a cis-element localized to the C-terminus of the protein.","doi":"10.1111/j.1365-2958.2008.06275.x","authors":"Martín-Cuadrado AB, Encinar del Dedo J, de Medina-Redondo M, Fontaine T, del Rey F, Latgé JP, Vázquez de Aldana CR","authors_abbrev":"Martín-Cuadrado AB et al.","pubmed_publication_date":"Jul 2008","pubmed_entrez_date":"2008-05-10","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.09"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:28471391","title":"The Combined Use of Schizosaccharomyces pombe and Lachancea thermotolerans-Effect on the Anthocyanin Wine Composition.","citation":"Molecules 2017 May 04;22(5)","abstract":"The most popular methodology to make red wine is through the combined use of  Saccharomyces cerevisiae  yeast and lactic acid bacteria, for alcoholic fermentation and malolactic fermentation respectively. This classic winemaking practice produces stable red wines from a microbiological point of view. This study aims to investigate a recent red winemaking biotechnology, which through the combined use of  Lachancea thermotolerans  and  Schizosaccharomyces pombe  is used as an alternative to the classic malolactic fermentation. In this new methodology,  Schizosaccharomyces  pombe  totally consumes malic acid, while  Lachancea thermotolerans  produces lactic acid, avoiding excessive deacidification of musts with low acidity in warm viticulture areas such as Spain. This new methodology has been reported to be a positive alternative to malolactic fermentation in low acidity wines, since it has the advantage to produce wines with a more fruity flavor, less acetic acid, less ethyl carbamate originators and less biogenic amines than the traditional wines produced via conventional fermentation techniques. The study focuses on unexplored facts related to this novel biotechnology such as color and anthocyanin profile.","doi":"10.3390/molecules22050739","authors":"Benito Á, Calderón F, Benito S","authors_abbrev":"Benito Á et al.","pubmed_publication_date":"04 May 2017","pubmed_entrez_date":"2017-05-05","publication_year":"2017","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2017-05-06 00:15:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10022880","title":"Control of growth and differentiation by Drosophila RasGAP, a homolog of p120 Ras-GTPase-activating protein.","citation":"Mol Cell Biol 1999 Mar;19(3):1928-37","abstract":"Mammalian Ras GTPase-activating protein (GAP), p120 Ras-GAP, has been implicated as both a downregulator and effector of Ras proteins, but its precise role in Ras-mediated signal transduction pathways is unclear. To begin a genetic analysis of the role of p120 Ras-GAP we identified a homolog from the fruit fly Drosophila melanogaster through its ability to complement the sterility of a Schizosaccharomyces pombe (fission yeast) gap1 mutant strain. Like its mammalian homolog, Drosophila RasGAP stimulated the intrinsic GTPase activity of normal mammalian H-Ras but not that of the oncogenic Val12 mutant. RasGAP was tyrosine phosphorylated in embryos and its Src homology 2 (SH2) domains could bind in vitro to a small number of tyrosine-phosphorylated proteins expressed at various developmental stages. Ectopic expression of RasGAP in the wing imaginal disc reduced the size of the adult wing by up to 45% and suppressed ectopic wing vein formation caused by expression of activated forms of Breathless and Heartless, two Drosophila receptor tyrosine kinases of the fibroblast growth factor receptor family. The in vivo effects of RasGAP overexpression required intact SH2 domains, indicating that intracellular localization of RasGAP through SH2-phosphotyrosine interactions is important for its activity. These results show that RasGAP can function as an inhibitor of signaling pathways mediated by Ras and receptor tyrosine kinases in vivo. Genetic interactions, however, suggested a Ras-independent role for RasGAP in the regulation of growth. The system described here should enable genetic screens to be performed to identify regulators and effectors of p120 Ras-GAP.","authors":"Feldmann P, Eicher EN, Leevers SJ, Hafen E, Hughes DA","authors_abbrev":"Feldmann P et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-02-18","publication_year":"1999","canto_session_key":"56b32ae70813bd30","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 17:20:15","canto_session_submitted_date":"2012-03-03 17:19:54","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC646.12c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:9799254","title":"Characterization of functional regions in the Schizosaccharomyces pombe mei3 developmental activator.","citation":"Genetics 1998 Nov;150(3):1007-18","abstract":"The Schizosaccharomyces pombe mei3(+) gene is expressed only in diploid cells undergoing meiosis. Ectopic expression of mei3(+) in haploid cells causes meiotic catastrophe. Mei3 is an inhibitor of Ran1/Pat1 kinase and contains a nine-amino-acid motif, Mei3-RKDIII, that resembles two regions in the Ste11 substrate for Ran1/Pat1. Substitution of serine for Arg-81 within Mei3-RKDIII transforms the inhibitor into a substrate for Ran1/Pat1. Thus, it is likely that Mei3-RKDIII defines a pseudosubstrate sequence. In this study, we constructed a series of mei3 deletion mutations and assayed each for activity. This analysis indicates that the carboxy-terminal domain of Mei3 is sufficient for function in vivo. Alanine-scanning mutagenesis identifies critical residues within the inhibitory domain. Two mutations, SM1 and SM8, fail to cause meiotic catastrophe. The SM1 mutation contains alterations of amino acid residues in Mei3-RKDIII. Recombinant SM1 protein exhibits reduced ability to inhibit Ran1/Pat1 kinase in vitro and interacts inefficiently with the kinase in a two-hybrid assay. The SM8 protein binds to Ran1/Pat1 in a two-hybrid assay but fails to inhibit Ran1/Pat1 substrate phosphorylation in vitro. These findings provide evidence that Mei3-RKDIII defines a Ran1/Pat1-binding site that is necessary but not sufficient for inhibition of the kinase. Using fusions to green fluorescent protein, the cellular localization of Ran1 and Mei3 was examined in living cells. Ran1 is concentrated in the nucleus. Mei3 is also enriched in the nucleus and, consistent with the genetic and biochemical results, the inhibitory domain of Mei3 is sufficient for nuclear localization.","authors":"Wang W, Li P, Schettino A, Peng Z, McLeod M","authors_abbrev":"Wang W et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1998-11-03","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPBC119.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7855597","title":"A role for exonuclease I from S. pombe in mutation avoidance and mismatch correction.","citation":"Science 1995 Feb 24;267(5201):1166-9","abstract":"Exonuclease I (Exo I) from Schizosaccharomyces pombe, a 5'-->3' double-stranded DNA exonuclease, is induced during meiotic prophase I. The exo1 gene is a member of a family of related DNA repair genes, including RAD2/rad13/xpgc and YKL510/rad2, conserved from yeast to humans. An exo1 mutant displays a mutator phenotype and alters activity of the ade6-M387 marker effect. These results suggest that Exo I acts in a pathway that corrects mismatched base pairs.","authors":"Szankasi P, Smith GR","authors_abbrev":"Szankasi P et al.","pubmed_publication_date":"24 Feb 1995","pubmed_entrez_date":"1995-02-24","publication_year":"1995","canto_session_key":"d059c2df7b2d6e91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-09-17 15:59:34","canto_approved_date":"2022-04-02 13:13:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-22 16:58:04","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.05","SPCC1322.13"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-09-17"},{"uniquename":"PMID:8515817","title":"Phosphorylation and inactivation of the mitotic inhibitor Wee1 by the nim1/cdr1 kinase.","citation":"Nature 1993 Jun 24;363(6431):736-8","abstract":"The G2-M phase transition in eukaryotes is regulated by the synergistic and opposing activities of a cascade of distinct protein kinases and phosphatases. This cascade converges on Cdc2, a serine/threonine protein kinase required for entry into mitosis (reviewed in ref. 1). In the fission yeast Schizosaccharomyces pombe, inactivation of the Cdc2/cyclin B complex is achieved by phosphorylation of tyrosine 15 by Wee1 (refs 2,3). The action of the Wee1 kinase is opposed by the action of the Cdc25 phosphatase, which dephosphorylates Cdc2 on tyrosine 15, thereby activating the Cdc2/cyclin B complex. Much less is known about the regulatory signals upstream of cdc25 and wee1. Genetics indicate that the mitotic inducer nim1/cdr1 acts upstream of wee1, possibly as a negative regulator of wee1 (refs 10, 11). To characterize the nim1/cdr1 protein (Nim1), we have overproduced it in both bacterial and baculoviral expression systems. We report that Nim1 possesses intrinsic serine-kinase, threonine-kinase and tyrosine-kinase activities. Co-expression of the Nim1 and Wee1 kinases in insect cells results in the phosphorylation of Wee1 and therefore a shift in its electrophoretic mobility on SDS-polyacrylamide gels. When Wee1 is phosphorylated, its ability to phosphorylate Cdc2 on tyrosine 15 is inhibited; treatment with phosphatase restores this kinase activity. Furthermore, purified bacterially produced Nim1 kinase directly phosphorylates and inactivates Wee1 in vitro. These results show that nim1/cdr1 functions as a positive regulator of mitosis by directly phosphorylating and inactivating the mitotic inhibitor Wee1.","authors":"Parker LL, Walter SA, Young PG, Piwnica-Worms H","authors_abbrev":"Parker LL et al.","pubmed_publication_date":"24 Jun 1993","pubmed_entrez_date":"1993-06-24","publication_year":"1993","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.06c","SPCC18B5.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:15219990","title":"The adrenodoxin-like ferredoxin of Schizosaccharomyces pombe mitochondria.","citation":"J Inorg Biochem 2004 Jul;98(7):1229-37","abstract":"The single mitochondrial type I [2Fe-2S] ferredoxin of the fission yeast Schizosaccharomyces pombe is produced as the carboxy terminal part of the electron-transfer-protein 1 (etp1) and cleaved off during mitochondrial import [Biochemistry 41 (2002) 2311-2321]. The UV/Vis (UV-visible) spectrum of the purified recombinant ferredoxin domain (etp1(fd)) expressed in Escherichia coli is similar to those of bovine Adx in the oxidized as well as in the reduced state. EPR (electronic paramagnetic resonance) studies revealed a correctly incorporated iron-sulfur cluster of the axial type. The redox potential of this protein was determined to be -353 mV, which is considerably lower than that of adrenodoxin (Adx, -273 mV). Several lines of evidence indicate that the protein forms dimers under physiological and denaturating conditions. Interestingly, the fission yeast ferredoxin could be shown to be active as an electron carrier in heterologous redox systems. It is able to transfer electrons to horse heart cytochrome c and to bovine cytochromes P450(scc) (CYP11A1) and P450(11 beta) (CYP11B1), thereby receiving electrons from bovine NADPH-dependent Adx reductase. The kinetics of substrate conversion in the etp1(fd)-supported CYP11A1 and CYP11B1-dependent systems mediated was studied.","authors":"Schiffler B, Bureik M, Reinle W, Müller EC, Hannemann F, Bernhardt R","authors_abbrev":"Schiffler B et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-06-29","publication_year":"2004","canto_session_key":"df1fa844a75ee0cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-04-09 14:21:12","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-30 14:34:18","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-03-30"},{"uniquename":"PMID:38916790","title":"Non-Mitochondrial Aconitase-2 Mediates the Transcription of Nuclear-Encoded Electron Transport Chain Genes in Fission Yeast.","citation":"J Microbiol 2024 Jun 25;","abstract":"Aconitase-2 (Aco2) is present in the mitochondria, cytosol, and nucleus of fission yeast. To explore its function beyond the well-known role in the mitochondrial tricarboxylic acid (TCA) cycle, we conducted genome-wide profiling using the aco2ΔNLS mutant, which lacks a nuclear localization signal (NLS). The RNA sequencing (RNA-seq) data showed a general downregulation of electron transport chain (ETC) genes in the aco2ΔNLS mutant, except for those in the complex II, leading to a growth defect in respiratory-prone media. Complementation analysis with non-catalytic Aco2 [aco2ΔNLS + aco2(3CS)], where three cysteines were substituted with serine, restored normal growth and typical ETC gene expression. This suggests that Aco2's catalytic activity is not essential for its role in ETC gene regulation. Our mRNA decay assay indicated that the decrease in ETC gene expression was due to transcriptional regulation rather than changes in mRNA stability. Additionally, we investigated the Php complex's role in ETC gene regulation and found that ETC genes, except those within complex II, were downregulated in php3Δ and php5Δ strains, similar to the aco2ΔNLS mutant. These findings highlight a novel role for nuclear aconitase in ETC gene regulation and suggest a potential connection between the Php complex and Aco2.","doi":"10.1007/s12275-024-00147-8","authors":"Kim HJ, Cho SY, Jung SJ, Cho YJ, Roe JH, Kim KD","authors_abbrev":"Kim HJ et al.","pubmed_publication_date":"25 Jun 2024","pubmed_entrez_date":"2024-06-25","publication_year":"2024","canto_session_key":"1ac93f8590d8bd66","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-06-25 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30280012","title":"Crystal structure and functional analysis of human C1ORF123.","citation":"PeerJ 2018;6:e5377","abstract":"Proteins of the DUF866 superfamily are exclusively found in eukaryotic cells. A member of the DUF866 superfamily, C1ORF123, is a human protein found in the open reading frame 123 of chromosome 1. The physiological role of C1ORF123 is yet to be determined. The only available protein structure of the DUF866 family shares just 26% sequence similarity and does not contain a zinc binding motif. Here, we present the crystal structure of the recombinant human C1ORF123 protein (rC1ORF123). The structure has a 2-fold internal symmetry dividing the monomeric protein into two mirrored halves that comprise of distinct electrostatic potential. The N-terminal half of rC1ORF123 includes a zinc-binding domain interacting with a zinc ion near to a potential ligand binding cavity. Functional studies of human C1ORF123 and its homologue in the fission yeast  Schizosaccharomyces pombe  (SpEss1) point to a role of DUF866 protein in mitochondrial oxidative phosphorylation.","doi":"10.7717/peerj.5377","authors":"A Rahaman SN, Mat Yusop J, Mohamed-Hussein ZA, Aizat WM, Ho KL, Teh AH, Waterman J, Tan BK, Tan HL, Li AY, Chen ES, Ng CL","authors_abbrev":"A Rahaman SN et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-10-04","publication_year":"2018","canto_session_key":"f7872927fe35893f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hwei-Ling Tan","canto_first_approved_date":"2018-10-11 09:36:06","canto_approved_date":"2018-10-11 09:36:06","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-10-11 03:40:27","canto_added_date":"2018-10-05 00:15:06","annotation_curators":[{"name":"Hwei-Ling Tan","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16A11.07","SPAC24B11.06c","SPAC222.03c","SPBC2D10.03c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-10-11"},{"uniquename":"GO_REF:0000086","title":"Representation of cell differentiation as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the differentiation process for a cell type as a biological process. The underlying equivalence axiom template is \"GO:0030154 and 'results in acquisition of features of' some C\", where C is a native cell (CL:0000003).","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9553071","title":"Selective inhibition of Ras interaction with its particular effector by synthetic peptides corresponding to the Ras effector region.","citation":"J Biol Chem 1998 Apr 24;273(17):10210-5","abstract":"Ras proteins possess multiple downstream effectors of distinct structures. We and others demonstrated that Ha-Ras carrying certain effector region mutations could interact differentially with its effectors, implying that significant differences exist in their Ras recognition mechanisms. Here, by employing the fluorescence polarization method, we measured the activity of effector region synthetic peptides bearing various amino acid substitutions to inhibit association of Ras with the effectors human Raf-1 and Schizosaccharomyces pombe Byr2. The effect of these peptides on association with another effector Saccharomyces cerevisiae adenylyl cyclase was also examined by measuring inhibition of the Ras-dependent adenylyl cyclase activity. The peptide corresponding to the residues 17-44 competitively inhibited Ras association with all the three effectors at the Ki values of 1 approximately 10 microM, and the inhibition was considerably attenuated by the D38A mutation. The peptide with the D38N mutation inhibited association of Ha-Ras with Byr2 but not with the others, whereas that with the P34G mutation inhibited association of Ha-Ras with Raf-1 and Byr2 but not with adenylyl cyclase. Thus, the specificity observed with the whole Ras protein was retained in the effector region peptide. These results suggest that the effector region residues constitute a major determinant for differential recognition of the effector molecules, raising a possibility for selective inhibition of a particular Ras function.","authors":"Ohnishi M, Yamawaki-Kataoka Y, Kariya K, Tamada M, Hu CD, Kataoka T","authors_abbrev":"Ohnishi M et al.","pubmed_publication_date":"24 Apr 1998","pubmed_entrez_date":"1998-05-30","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8374169","title":"Schizosaccharomyces pombe ypt5: a homologue of the rab5 endosome fusion regulator.","citation":"Mol Biol Cell 1993 Jun;4(6):583-92","abstract":"The ypt/rab proteins are a family of small GTP-binding proteins thought to be required for different stages of membrane traffic. From the fission yeast Schizosaccharomyces pombe we have isolated and characterized ypt5, a gene encoding a homologue of rab5, a mammalian protein apparently involved in regulating fusion of early endosomes. Recombinant ypt5 protein bound GTP. The ypt5 gene was found to be essential for viability on minimal media, but ypt5-disrupted cells grew slowly on some rich media and accumulated a population of small vesicles not observed in wild-type cells. Canine rab5 cDNA could replace the ypt5 gene in S. pombe and restore normal growth and viability. Ypt5 protein expressed in mammalian cells colocalized with the transferrin receptor to early endosomes. Thus, molecular aspects of the early endocytic pathway may be conserved between mammalian cells and S. pombe and hence may be amenable to genetic analysis.","authors":"Armstrong J, Craighead MW, Watson R, Ponnambalam S, Bowden S","authors_abbrev":"Armstrong J et al.","pubmed_publication_date":"Jun 1993","pubmed_entrez_date":"1993-06-01","publication_year":"1993","canto_session_key":"7ac1185c53b7efd4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-03-27 15:45:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-05 15:37:59","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.15"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-05"},{"uniquename":"PMID:33823663","title":"A TOR (target of rapamycin) and nutritional phosphoproteome of fission yeast reveals novel targets in networks conserved in humans.","citation":"Open Biol 2021 Apr;11(4):200405","abstract":"Fluctuations in TOR, AMPK and MAP-kinase signalling maintain cellular homeostasis and coordinate growth and division with environmental context. We have applied quantitative, SILAC mass spectrometry to map TOR and nutrient-controlled signalling in the fission yeast  Schizosaccharomyces pombe . Phosphorylation levels at more than 1000 sites were altered following nitrogen stress or Torin1 inhibition of the TORC1 and TORC2 networks that comprise TOR signalling. One hundred and thirty of these sites were regulated by both perturbations, and the majority of these (119) new targets have not previously been linked to either nutritional or TOR control in either yeasts or humans. Elimination of AMPK inhibition of TORC1, by removal of AMPK α  ( ssp2::ura4 +  ), identified phosphosites where nitrogen stress-induced changes were independent of TOR control. Using a yeast strain with an ATP analogue-sensitized Cdc2 kinase, we excluded sites that were changed as an indirect consequence of mitotic control modulation by nitrogen stress or TOR signalling. Nutritional control of gene expression was reflected in multiple targets in RNA metabolism, while significant modulation of actin cytoskeletal components points to adaptations in morphogenesis and cell integrity networks. Reduced phosphorylation of the MAPKK Byr1, at a site whose human equivalent controls docking between MEK and ERK, prevented sexual differentiation when resources were sparse but not eliminated.","doi":"10.1098/rsob.200405","authors":"Halova L, Cobley D, Franz-Wachtel M, Wang T, Morrison KR, Krug K, Nalpas N, Maček B, Hagan IM, Humphrey SJ, Petersen J","authors_abbrev":"Halova L et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2021-04-07","publication_year":"2021","canto_session_key":"260532ed016fea91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Janni Petersen","canto_first_approved_date":"2022-03-10 18:47:07","canto_approved_date":"2023-12-22 10:26:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-03-08 09:52:17","canto_added_date":"2021-04-10 00:15:06","annotation_curators":[{"name":"Janni 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of a semi-quantitative plate-based alpha-galactosidase gene reporter for Schizosaccharomyces pombe and its use to isolate a constitutively active Mam2.","citation":"Yeast 2005 Jan 15;22(1):31-41","abstract":"To extend the tools available for biochemical and genetical analysis in the fission yeast Schizosaccharomyces pombe we have investigated the development of gene reporter systems using the secreted alpha-galactosidase encoded by the Sz. pombe ORF SPAC869.07c (CAB60017), which we propose naming Mel1p to reflect its structural and functional similarity to MEL1p in Saccharomyces cerevisiae. The alpha-galactosidase activity can be monitored in liquid assays and converted the colourless substrate 5-bromo-4-chloro-3-indolyl-alpha-D-galactopyranoside (X-alpha-gal) into an insoluble blue product that was suitable for semi quantitative plate-based assays; colonies expressing the highest levels of alpha-galactosidase developed the most intense blue colour. Unlike assays based on beta-galactosidase, the Sz. pombe colonies develop the blue colouration under normal growth conditions, avoiding the need to replicate colonies to fresh plates for analysis. It is therefore suitable for screening large numbers of colonies. To illustrate the use of mel1 as a reporter we linked expression to the sxa2 gene promoter to provide a convenient readout for signalling through the pheromone response pathway. The sxa2 > mel1 strain identified constitutively active Mam2 pheromone receptors from a randomly mutagenised library. There was an approximate correlation between the intensity of the blue colour developed by each mutant colony and its level of constitutive activity and we identified a subset of mutants with low constitutive activity that could not have been isolated by a previous screen using nutritional selection. The mel1 alpha-galactosidase activity identified and characterised in this study can be easily adapted to provide a gene reporter for many biological processes and is a new addition to the research tools available in Sz. pombe.","authors":"Goddard A, Ladds G, Davey J","authors_abbrev":"Goddard A et al.","pubmed_publication_date":"15 Jan 2005","pubmed_entrez_date":"2004-12-08","publication_year":"2005","canto_session_key":"285a46669a679913","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-22 08:23:34","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-02-18 18:33:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11H11.04","SPAC869.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-02-18"},{"uniquename":"PMID:24710126","title":"The 19S proteasome subunit Rpt3 regulates distribution of CENP-A by associating with centromeric chromatin.","citation":"Nat Commun 2014 Apr 07;5:3597","abstract":"CENP-A, a variant of histone H3, is incorporated into centromeric chromatin and plays a role during kinetochore establishment. In fission yeast, the localization of CENP-A is limited to a region spanning 10-20 kb of the core domain of the centromere. Here, we report a mutant (rpt3-1) in which this region is expanded to 40-70 kb. Likely due to abnormal distribution of CENP-A, this mutant exhibits chromosome instability and enhanced gene silencing. Interestingly, the rpt3(+) gene encodes a subunit of the 19S proteasome, which localizes to the nuclear membrane. Although Rpt3 associates with centromeric chromatin, the mutant protein has lost this localization. A loss of the cut8(+) gene encoding an anchor of the proteasome to the nuclear membrane causes similar phenotypes as observed in the rpt3-1 mutant. Thus, we propose that the proteasome (or its subcomplex) associates with centromeric chromatin and regulates distribution of CENP-A.","doi":"10.1038/ncomms4597","authors":"Kitagawa T, Ishii K, Takeda K, Matsumoto T","authors_abbrev":"Kitagawa T et al.","pubmed_publication_date":"07 Apr 2014","pubmed_entrez_date":"2014-04-09","publication_year":"2014","canto_session_key":"8ad9bcb87e5ff032","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-05 17:11:52","canto_approved_date":"2022-10-03 10:08:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-23 15:49:46","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4.07c","SPAC17C9.13c","SPBC1105.11c","SPBC16G5.01","SPAC4A8.13c","SPBC1105.17","SPAC1834.04","SPBC8D2.04","SPAC664.01c","SPCC576.10c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2017-01-05"},{"uniquename":"PMID:39753782","title":"Dbi1 is an oxidoreductase and an assembly chaperone for mitochondrial inner membrane proteins.","citation":"EMBO Rep 2025 Feb;26(4):911-928","abstract":"Import and assembly of mitochondrial proteins into multimeric complexes are essential for cellular function. Yet, many steps of these processes and the proteins involved remain unknown. Here, we identify a novel pathway for disulfide bond formation and assembly of mitochondrial inner membrane (IM) proteins. Dbi1, a previously uncharacterized IM protein, interacts with an unassembled pool of Tim17, the central subunit of the presequence translocase of the IM, and is upregulated in cells with increased levels of unassembled Tim17. In the absence of Dbi1, the conformation of the presequence translocase is affected and stability of Tim17 is reduced. Furthermore, Dbi1, through its conserved CxxC motif, is involved in the formation of the disulfide bond in Tim17 in a manner independent of the disulfide relay system, the major oxidation-driven protein import pathway into mitochondria. The substrate spectrum of Dbi1 is not limited to Tim17 but includes at least two more IM proteins, Tim22 and Cox20. We conclude that Dbi1 is a novel oxidoreductase in mitochondria which introduces disulfide bonds into IM proteins and chaperones their assembly into multimeric protein complexes.","doi":"10.1038/s44319-024-00349-6","authors":"Badrie S, Hell K, Mokranjac D","authors_abbrev":"Badrie S et al.","pubmed_publication_date":"Feb 2025","pubmed_entrez_date":"2025-01-03","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC25H2.04c","SPBC25H2.18","SPAC3A12.16c","SPAC1F7.14c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:24190832","title":"Gene conversion in nonsense suppressors of Schizosaccharomyces pombe : II. Specific marker effects.","citation":"Curr Genet 1980 Feb;1(2):89-95","abstract":"Gene conversion and postmeiotic segregation patterns have been analysed at 14 mutant sites of sup3, sup8 and sup9 including 5 alleles with a strong marker effect on recombination frequencies in two-factor crosses. The total frequency of gene conversion and postmeiotic segregation tetrads is fairly constant within each gene, but may vary from one gene to another. About 97% of the conversion events are coconversions spanning the whole sup gene. Postmeiotic segregations are usually quite rare. None of the marker-effect alleles has an increased rate of hybrid DNA formation at the allele considered, as judged from the frequency of gene conversion and postmeiotic segregation in one-factor crosses. At least two of them, sup3-e and sup9-e, are associated with a high frequency of postmeiotic segregation indicating a poor repair of the corresponding base-pair mismatches. This is also observed in a two-factor cross and can account for the marker effect on recombination frequencies. The properties of a third marker effect allele, sup3-e,r10, are best explained by a higher probability of single site conversions as opposed to coconversions in two-factor crosses involving the mutant site r10.","doi":"10.1007/BF00446954","authors":"Thuriaux P, Minet M, Munz P, Ahmad A, Zbaeren D, Leupold U","authors_abbrev":"Thuriaux P et al.","pubmed_publication_date":"Feb 1980","pubmed_entrez_date":"2013-11-06","publication_year":"1980","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 06:09:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17317928","title":"A method for Pmo25-associated kinase assay in fission yeast: the activity is dependent on two gC kinases Nak1 and Sid1.","citation":"Biosci Biotechnol Biochem 2007 Feb;71(2):615-7","abstract":"In fission yeast, the conserved proteins, MO25/Pmo25, GC kinase/Nak1, Furry/Mor2, NDR kinase/Orb6, and Mob2, constitute the morphogenesis Orb6 network (MOR). Previously we showed that Pmo25 functions as an upstream component of MOR and that it plays a connecting role between the septation initiation network (SIN) and MOR. Here we establish a Pmo25-associated kinase assay and show that the activity is dependent on Nak1/MOR and Sid1/SIN.","authors":"Kume K, Goshima T, Miyahara K, Toda T, Hirata D","authors_abbrev":"Kume K et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-02-24","publication_year":"2007","canto_session_key":"7e66641cb8bf60c5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-06-11 12:00:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-08-16 15:48:58","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.12","SPAC24B11.11c","SPBP19A11.04c","SPAC1834.06c","SPBC21.06c","SPAC9G1.09","SPBC17F3.02"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2017-08-16"},{"uniquename":"PMID:15716375","title":"Temporal separation of replication and recombination requires the intra-S checkpoint.","citation":"J Cell Biol 2005 Feb 14;168(4):537-44","abstract":"In response to DNA damage and replication pausing, eukaryotes activate checkpoint pathways that prevent genomic instability by coordinating cell cycle progression with DNA repair. The intra-S-phase checkpoint has been proposed to protect stalled replication forks from pathological rearrangements that could result from unscheduled recombination. On the other hand, recombination may be needed to cope with either stalled forks or double-strand breaks resulting from hydroxyurea treatment. We have exploited fission yeast to elucidate the relationship between replication fork stalling, loading of replication and recombination proteins onto DNA, and the intra-S checkpoint. Here, we show that a functional recombination machinery is not essential for recovery from replication fork arrest and instead can lead to nonfunctional fork structures. We find that Rad22-containing foci are rare in S-phase cells, but peak in G2 phase cells after a perturbed S phase. Importantly, we find that the intra-S checkpoint is necessary to avoid aberrant strand-exchange events during a hydroxyurea block.","authors":"Meister P, Taddei A, Vernis L, Poidevin M, Gasser SM, Baldacci G","authors_abbrev":"Meister P et al.","pubmed_publication_date":"14 Feb 2005","pubmed_entrez_date":"2005-02-18","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29414789","title":"A long noncoding (lnc)RNA governs expression of the phosphate transporter Pho84 in fission yeast and has cascading effects on the flanking  prt  lncRNA and  pho1  genes.","citation":"J Biol Chem 2018 Mar 23;293(12):4456-4467","abstract":"The expression of the phosphate transporter Pho84 in fission yeast  Schizosaccharomyces pombe  is repressed in phosphate-rich medium and induced during phosphate starvation. Two other phosphate-responsive genes in  S. pombe  ( pho1  and  tgp1 ) had been shown to be repressed in  cis  by transcription of a long noncoding (lnc) RNA from the upstream flanking gene, but whether  pho84  expression is regulated in this manner is unclear. Here, we show that repression of  pho84  is enforced by transcription of the SPBC8E4.02c locus upstream of  pho84  to produce a lncRNA that we name  prt2  (   p ho - r epressive  t ranscript 2). We identify two essential elements of the  prt2  promoter, a HomolD box and a TATA box, mutations of which inactivate the  prt2  promoter and de-repress the downstream  pho84  promoter under phosphate-replete conditions. We find that  prt2  promoter inactivation also elicits a cascade effect on the adjacent downstream  prt  (lncRNA) and  pho1  (acid phosphatase) genes, whereby increased  pho84  transcription down-regulates  prt  lncRNA transcription and thereby de-represses  pho1  Our results establish a unified model for the repressive arm of fission yeast phosphate homeostasis, in which transcription of  prt2 ,  prt , and  nc-tgp1  lncRNAs interferes with the promoters of the flanking  pho84 ,  pho1 , and  tgp1  genes, respectively.","doi":"10.1074/jbc.RA117.001352","authors":"Garg A, Sanchez AM, Shuman S, Schwer B","authors_abbrev":"Garg A et al.","pubmed_publication_date":"23 Mar 2018","pubmed_entrez_date":"2018-02-08","publication_year":"2018","canto_session_key":"a93df4140a4b1e4c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Angad Garg","canto_first_approved_date":"2018-09-07 08:59:04","canto_approved_date":"2024-04-04 07:22:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-08-14 19:15:39","canto_added_date":"2018-02-09 01:15:19","annotation_curators":[{"name":"Angad Garg","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPBP4G3.02","SPBC27B12.11c","SPBC8E4.01c","SPNCRNA.1712","SPAC1F3.01","SPNCRNA.9001"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2018-09-07"},{"uniquename":"PMID:37528789","title":"[Inactivation of Ras1 in Fission Yeast Aggravates the Oxidative Stress Response Induced by Tert Butyl Hydroperoxide (tBHP)].","citation":"Mol Biol (Mosk) 2023;57(4):689-691","abstract":"Ras proteins are small GTPases and function as molecular switches to regulate cellular homeostasis. Ras-dependent signalling pathways regulate several essential processes such as cell cycle progression, growth, migration, apoptosis, and senescence. The dysregulation of Ras signaling pathway has been linked to several pathological outcomes. A potential role of RAS in regulating the redox signalling pathway has been established that includes the manipulation of ROS levels to provide a redox milieu that might be conducive to carcinogenesis. Reactive oxygen species (ROS) and mitochondrial impairment have been proposed as major factors affecting the physiology of cells and implicated in several pathologies. The present study was conducted to evaluate the role of Ras1, tert Butyl hydroperoxide (tBHP), and antimycin A in oxidative stress response in Schizosaccharomyces pombe cells. We observed decreased cell survival, higher levels of ROS, and mitochondrial dysfunctionality in ras1Δ cells and tBHP as well as respiratory inhibitor, antimycin A treated wild type cells. Furthermore, these defects were more profound in ras1Δ cells treated with tBHP or antimycin A. Additionally, Ras1 also has been shown to regulate the expression and activity of several antioxidant enzymes like glutathione peroxidase (GSH-Px), glutathione-S-transferase (GST), and catalase. Together, these results suggest the potential role of S. pombe Ras1 in mitigating oxidative stress response.","authors":"Masood N, Anjum S, Ahmed S","authors_abbrev":"Masood N et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-08-02","publication_year":"2023","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2023-08-03 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16682348","title":"A screen for cohesion mutants uncovers Ssl3, the fission yeast counterpart of the cohesin loading factor Scc4.","citation":"Curr Biol 2006 May 09;16(9):875-81","abstract":"Sister-chromatid cohesion is mediated by cohesin, a ring-shape complex made of four core subunits called Scc1, Scc3, Smc1, and Smc3 in Saccharomyces cerevisiae (Rad21, Psc3, Psm1, and Psm3 in Schizosaccharomyces pombe). How cohesin ensures cohesion is unknown, although its ring shape suggests that it may tether sister DNA strands by encircling them . Cohesion establishment is a two-step process. Cohesin is loaded on chromosomes before replication and cohesion is subsequently established during S phase. In S. cerevisiae, cohesin loading requires a separate complex containing the Scc2 and Scc4 proteins. Cohesin rings fail to associate with chromatin and cohesion can not establish when Scc2 is impaired . The mechanism of loading is unknown, although some data suggest that hydrolysis of ATP bound to Smc1/3 is required . Scc2 homologs exist in fission yeast (Mis4), Drosophila, Xenopus, and human . By contrast, no homolog of Scc4 has been identified so far. We report here on the identification of fission yeast Ssl3 as a Scc4-like factor. Ssl3 is in complex with Mis4 and, as a bona fide loading factor, Ssl3 is required in G1 for cohesin binding to chromosomes but dispensable in G2 when cohesion is established. The discovery of a functional homolog of Scc4 indicates that the machinery of cohesin loading is conserved among eukaryotes.","authors":"Bernard P, Drogat J, Maure JF, Dheur S, Vaur S, Genier S, Javerzat JP","authors_abbrev":"Bernard P et al.","pubmed_publication_date":"09 May 2006","pubmed_entrez_date":"2006-05-10","publication_year":"2006","canto_session_key":"3602d714a22a5fa7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-02 10:16:37","canto_approved_date":"2026-02-06 16:14:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-01 13:09:10","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.15c","SPAC1687.18c","SPAC664.01c","SPBC29A10.04","SPAC17H9.20","SPBC16A3.11","SPAC10F6.09c","SPCC338.17c","SPAC31A2.05c"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2016-09-02"},{"uniquename":"PMID:30541785","title":"Transposable element insertions in fission yeast drive adaptation to environmental stress.","citation":"Genome Res 2019 Jan;29(1):85-95","abstract":"Cells are regularly exposed to a range of naturally occurring stress that can restrict growth or cause lethality. In response, cells activate expression networks with hundreds of genes that together increase resistance to common environmental insults. However, stress response networks can be insufficient to ensure survival, which raises the question of whether cells possess genetic programs that can promote adaptation to novel forms of stress. We found transposable element (TE) mobility in  Schizosaccharomyces pombe  was greatly increased when cells were exposed to unusual forms of stress such as heavy metals, caffeine, and the plasticizer phthalate. By subjecting TE-tagged cells to CoCl 2 , we found the TE integration provided the major path to resistance. Groups of insertions that provided resistance were linked to TOR regulation and metal response genes. We extended our study of adaptation by analyzing TE positions in 57 genetically distinct wild strains. The genomic positions of 1048 polymorphic LTRs were strongly associated with a range of stress response genes, indicating TE integration promotes adaptation in natural conditions. These data provide strong support for the idea, first proposed by Barbara McClintock, that TEs provide a system to modify the genome in response to stress.","doi":"10.1101/gr.239699.118","authors":"Esnault C, Lee M, Ham C, Levin HL","authors_abbrev":"Esnault C et al.","pubmed_publication_date":"Jan 2019","pubmed_entrez_date":"2018-12-14","publication_year":"2019","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2018-12-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23791180","title":"Dynein motion switches from diffusive to directed upon cortical anchoring.","citation":"Cell 2013 Jun 20;153(7):1526-36","abstract":"Cytoplasmic dynein is a motor protein that exerts force on microtubules. To generate force for the movement of large organelles, dynein needs to be anchored, with the anchoring sites being typically located at the cell cortex. However, the mechanism by which dyneins target sites where they can generate large collective forces is unknown. Here, we directly observe single dyneins during meiotic nuclear oscillations in fission yeast and identify the steps of the dynein binding process: from the cytoplasm to the microtubule and from the microtubule to cortical anchors. We observed that dyneins on the microtubule move either in a diffusive or directed manner, with the switch from diffusion to directed movement occurring upon binding of dynein to cortical anchors. This dual behavior of dynein on the microtubule, together with the two steps of binding, enables dyneins to self-organize into a spatial pattern needed for them to generate large collective forces.","doi":"10.1016/j.cell.2013.05.020","authors":"Ananthanarayanan V, Schattat M, Vogel SK, Krull A, Pavin N, Tolić-Nørrelykke IM","authors_abbrev":"Ananthanarayanan V et al.","pubmed_publication_date":"20 Jun 2013","pubmed_entrez_date":"2013-06-25","publication_year":"2013","canto_session_key":"d1957b3954696746","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2251129","title":"Nucleotide sequence of the unassigned reading frame urf a in the mitochondrial genome of three Schizosaccharomyces pombe strains.","citation":"Nucleic Acids Res 1990 Nov 25;18(22):6686","abstract":"","authors":"Zimmer M, Schiebner T, Krabusch M, Wolf K","authors_abbrev":"Zimmer M et al.","pubmed_publication_date":"25 Nov 1990","pubmed_entrez_date":"1990-11-25","publication_year":"1990","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32389310","title":"Thoughts on the evolution of Core Environmental Responses in yeasts.","citation":"Fungal Biol 2020 May;124(5):475-481","abstract":"The model yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe, display Core Environmental Responses (CERs) that include the induction of a core set of stress genes in response to diverse environmental stresses. CERs underlie the phenomenon of stress cross-protection, whereby exposure to one type of stress can provide protection against subsequent exposure to a second type of stress. CERs have probably arisen through the accumulation, over evolutionary time, of protective anticipatory responses (\"adaptive prediction\"). CERs have been observed in other evolutionarily divergent fungi but, interestingly, not in the pathogenic yeast, Candida albicans. We argue that this is because we have not looked in the right place. In response to specific host inputs, C. albicans does activate anticipatory responses that protect it against impending attack from the immune system. Therefore, we suggest that C. albicans has evolved a CER that reflects the environmental challenges it faces in host niches.","doi":"10.1016/j.funbio.2020.01.003","authors":"Brown AJP, Larcombe DE, Pradhan A","authors_abbrev":"Brown AJP et al.","pubmed_publication_date":"May 2020","pubmed_entrez_date":"2020-05-12","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-05-13 00:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24636258","title":"Symmetry breaking in spore germination relies on an interplay between polar cap stability and spore wall mechanics.","citation":"Dev Cell 2014 Mar 10;28(5):534-46","abstract":"The morphogenesis of single cells depends on their ability to coordinate surface mechanics and polarity. During germination, spores of many species develop a polar tube that hatches out of a rigid outer spore wall (OSW) in a process termed outgrowth. However, how these awakening cells reorganize to stabilize this first growth axis remains unknown. Here, using quantitative experiments and modeling, we reveal the mechanisms underlying outgrowth in fission yeast. We find that, following an isotropic growth phase during which a single polarity cap wanders around the surface, outgrowth occurs when spores have doubled their volume, concomitantly with the stabilization of the cap and a singular rupture in the OSW. This rupture happens when OSW mechanical stress exceeds a threshold, releases the constraints of the OSW on growth, and stabilizes polarity. Thus, outgrowth exemplifies a self-organizing morphogenetic process in which reinforcements between growth and polarity coordinate mechanics and internal organization.","doi":"10.1016/j.devcel.2014.01.023","authors":"Bonazzi D, Julien JD, Romao M, Seddiki R, Piel M, Boudaoud A, Minc N","authors_abbrev":"Bonazzi D et al.","pubmed_publication_date":"10 Mar 2014","pubmed_entrez_date":"2014-03-19","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4394400","title":"Respiratory metabolism of a \"petite negative\"yeast Schizosaccharomyces pombe 972h-.","citation":"J Bacteriol 1970 Oct;104(1):473-81","abstract":"The respiratory metabolism of Schizosaccharomyces pombe 972h(-), a fission, haplontic, \"petite negative\" yeast, was studied. Glucose and glycerol are good growth substrates and are oxidized under appropriate conditions. l-Lactate, ethanol, malate, and succinate are oxidized but are poor substrates for growth. d-Lactate and pyruvate are neither oxidized nor used for growth. Limited growth was observed under anaerobic conditions. The addition of 0.3% KNO(3) to a rich medium relieves the oxygen requirement. A continuous increase of cell respiration during growth on repressive concentration of glucose was observed, suggesting the presence of glucose repression of respiration. Reduced nicotinamide adenine dinucleotide (NADH), succinate, alpha-glycerophosphate, and ascorbate plus tetramethyl-p-phenylenediamine are oxidized by a mitochondrial fraction. NADH and succinate oxidations are inhibited by antimycin A and NaCN but not by rotenone, suggesting the absence of the phosphorylation site I and the presence of sites II and III. The effects of several mitochondrial inhibitors on growth and respiration indicate that the requirement of an oxidant for growth is related neither to the functioning of the respiratory electron transport chain nor to the formation of respiratory energy. The previously suggested correlations between the nonviability of vegetative \"petites\" mutants, the absence of repression of respiration by glucose, and the incapacity to grow under anaerobic conditions are thus not strictly valid for S. pombe.","authors":"Heslot H, Goffeau A, Louis C","authors_abbrev":"Heslot H et al.","pubmed_publication_date":"Oct 1970","pubmed_entrez_date":"1970-10-01","publication_year":"1970","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23273506","title":"Non-productive DNA damage binding by DNA glycosylase-like protein Mag2 from Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2013 Mar 01;12(3):196-204","abstract":"Schizosaccharomyces pombe contains two paralogous proteins, Mag1 and Mag2, related to the helix-hairpin-helix (HhH) superfamily of alkylpurine DNA glycosylases from yeast and bacteria. Phylogenetic analysis of related proteins from four Schizosaccharomyces and other fungal species shows that the Mag1/Mag2 duplication is unique to the genus Schizosaccharomyces and most likely occurred in its ancestor. Mag1 excises N3- and N7-alkylguanines and 1,N(6)-ethenoadenine from DNA, whereas Mag2 has been reported to have no detectible alkylpurine base excision activity despite high sequence and active site similarity to Mag1. To understand this discrepancy we determined the crystal structure of Mag2 bound to abasic DNA and compared it to our previously determined Mag1-DNA structure. In contrast to Mag1, Mag2 does not flip the abasic moiety into the active site or stabilize the DNA strand 5' to the lesion, suggesting that it is incapable of forming a catalytically competent protein-DNA complex. Subtle differences in Mag1 and Mag2 interactions with the DNA duplex illustrate how Mag2 can stall at damage sites without fully engaging the lesion. We tested our structural predictions by mutational analysis of base excision and found a single amino acid responsible at least in part for Mag2's lack of activity. Substitution of Mag2 Asp56, which caps the helix at the base of the DNA intercalation loop, with the corresponding serine residue in Mag1 endows Mag2 with ɛA excision activity comparable to Mag1. This work provides novel insight into the chemical and physical determinants by which the HhH glycosylases engage DNA in a catalytically productive manner.","doi":"10.1016/j.dnarep.2012.12.001","authors":"Adhikary S, Cato MC, McGary KL, Rokas A, Eichman BF","authors_abbrev":"Adhikary S et al.","pubmed_publication_date":"01 Mar 2013","pubmed_entrez_date":"2013-01-01","publication_year":"2013","canto_session_key":"a7ac6f2d54760132","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-09 08:13:13","canto_approved_date":"2024-05-09 07:45:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-09 08:12:45","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-03-09","pdb_entries":[{"pdb_id":"4hsb","gene_chains":[{"gene_uniquename":"SPBC23G7.11","chain":"A","position":"1-213"}],"title":"S. pombe 3-methyladenine DNA glycosylase-like protein Mag2 bound to damaged DNA","entry_authors":"Adhikary S,Eichman BF","entry_authors_abbrev":"Adhikary S et al.","reference_uniquename":"PMID:23273506","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:21271286","title":"Ringing the changes: emerging roles for DASH at the kinetochore-microtubule Interface.","citation":"Chromosome Res 2011 Apr;19(3):393-407","abstract":"Regulated interaction between kinetochores and the mitotic spindle is essential for the fidelity of chromosome segregation. Potentially deleterious attachments are corrected during prometaphase and metaphase. Correct attachments must persist during anaphase, when spindle-generated forces separate chromosomes to opposite poles. In yeast, the heterodecameric DASH complex plays a vital pole in maintaining this link. In vitro DASH forms both oligomeric patches and rings that can form load-bearing attachments with the tips of polymerising and depolymerising microtubules. In vivo, DASH localises primarily at the kinetochore, and has a role maintaining correct attachment between spindles and chromosomes in both Saccharomyces cerevisiae and Schizosaccharomyces pombe. Recent work has begun to describe how DASH acts alongside other components of the outer kinetochore to create a dynamic, regulated kinetochore-microtubule interface. Here, we review some of the key experiments into DASH function and discuss their implications for the nature of kinetochore-microtubule attachments in yeast and other organisms.","doi":"10.1007/s10577-011-9185-8","authors":"Buttrick GJ, Millar JB","authors_abbrev":"Buttrick GJ et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2011-01-29","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37403782","title":"The fission yeast methyl phosphate capping enzyme Bmc1 guides 2'-O-methylation of the U6 snRNA.","citation":"Nucleic Acids Res 2023 Sep 08;51(16):8805-8819","abstract":"Splicing requires the tight coordination of dynamic spliceosomal RNAs and proteins. U6 is the only spliceosomal RNA transcribed by RNA Polymerase III and undergoes an extensive maturation process. In humans and fission yeast, this includes addition of a 5' γ-monomethyl phosphate cap by members of the Bin3/MePCE family as well as snoRNA guided 2'-O-methylation. Previously, we have shown that the Bin3/MePCE homolog Bmc1 is recruited to the S. pombe telomerase holoenzyme by the LARP7 family protein Pof8, where it acts in a catalytic-independent manner to protect the telomerase RNA and facilitate holoenzyme assembly. Here, we show that Bmc1 and Pof8 are required for the formation of a distinct U6 snRNP that promotes 2'-O-methylation of U6, and identify a non-canonical snoRNA that guides this methylation. We also show that the 5' γ-monomethyl phosphate capping activity of Bmc1 is not required for its role in promoting snoRNA guided 2'-O-methylation, and that this role relies on different regions of Pof8 from those required for Pof8 function in telomerase. Our results are consistent with a novel role for Bmc1/MePCE family members in stimulating 2'-O-methylation and a more general role for Bmc1 and Pof8 in guiding noncoding RNP assembly beyond the telomerase RNP.","doi":"10.1093/nar/gkad563","authors":"Porat J, Slat VA, Rader SD, Bayfield MA","authors_abbrev":"Porat J et al.","pubmed_publication_date":"08 Sep 2023","pubmed_entrez_date":"2023-07-05","publication_year":"2023","canto_session_key":"eec0954c4a56c293","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mark Bayfield","canto_first_approved_date":"2023-07-13 07:03:31","canto_approved_date":"2024-04-23 10:55:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-06 19:15:10","canto_added_date":"2023-07-06 00:15:12","annotation_curators":[{"name":"Mark Bayfield","community_curator":true,"annotation_count":7,"orcid":"0000-0002-8971-7598","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G6.17","SPSNRNA.06","SPBC1861.04c","SPAC22F3.05c","SPBC543.05c","SPBC2A9.10","SPSNORNA.25","SPNCRNA.530","SPCC18B5.09c","SPAC4C5.01"],"gene_count":10,"ltp_gene_count":5,"approved_date":"2023-07-13"},{"uniquename":"PMID:24432349","title":"Prp4 kinase is required for proper segregation of chromosomes during meiosis in Schizosaccharomyces pombe.","citation":"Acta Biochim Pol 2013;60(4):871-3","abstract":"Chromosome segregation during meiosis is a complex process, which leads to production of four haploid gametes from two precursor cells. Reversible phosphorylation of proteins plays a crucial role in this process. The Schizosaccharomyces pombe Prp4 is an essential serine/threonine protein kinase, which belongs to the Clk/Sty family. To study the role of Prp4 in meiosis, we analysed chromosome segregation in a strain carrying conditional analog-sensitive allele of Prp4 protein kinase (prp4-as2). Our data show, that Prp4 protein kinase plays important role in chromosome segregation during meiosis, as revealed by enhanced missegregation of chromosomes in prp4-as2 mutant cells.","authors":"Pozgajova M, Cipak L, Trakovicka A","authors_abbrev":"Pozgajova M et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2014-01-17","publication_year":"2013","canto_session_key":"441dfb6b37eb4a5d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30424766","title":"Enhancing 3-hydroxypropionic acid production in combination with sugar supply engineering by cell surface-display and metabolic engineering of Schizosaccharomyces pombe.","citation":"Microb Cell Fact 2018 Nov 13;17(1):176","abstract":"Economical production of value-added chemicals from renewable biomass is a promising path to sustainability. 3-Hydroxypropionic acid (3-HP) is an important chemical for building a bio-sustainable society. Establishment of 3-HP production from renewable resources such as glucose would provide a bio-sustainable alternative to the production of acrylic acid from fossil resources.\nHere, we describe metabolic engineering of the fission yeast Schizosaccharomyces pombe to enhance 3-HP production from glucose and cellobiose via the malonyl-CoA pathway. The mcr gene, encoding the malonyl-CoA reductase of Chloroflexus aurantiacus, was dissected into two functionally distinct fragments, and the activities of the encoded protein were balanced. To increase the cellular supply of malonyl-CoA and acetyl-CoA, we introduced genes encoding endogenous aldehyde dehydrogenase, acetyl-CoA synthase from Salmonella enterica, and endogenous pantothenate kinase. The resulting strain produced 3-HP at 1.0 g/L from a culture starting at a glucose concentration of 50 g/L. We also engineered the sugar supply by displaying beta-glucosidase (BGL) on the yeast cell surface. When grown on 50 g/L cellobiose, the beta-glucosidase-displaying strain consumed cellobiose efficiently and produced 3-HP at 3.5 g/L. Under fed-batch conditions starting from cellobiose, this strain produced 3-HP at up to 11.4 g/L, corresponding to a yield of 11.2% (g-3-HP/g-glucose; given that 1 g cellobiose corresponds to 1.1 g glucose upon digestion).\nIn this study, we constructed a series of S. pombe strains that produced 3-HP via the malonyl-CoA pathway. Our study also demonstrated that BGL display using cellobiose and/or cello-oligosaccharides as a carbon source has the potential to improve the titer and yield of malonyl-CoA- and acetyl-CoA-derived compounds.","doi":"10.1186/s12934-018-1025-5","authors":"Takayama S, Ozaki A, Konishi R, Otomo C, Kishida M, Hirata Y, Matsumoto T, Tanaka T, Kondo A","authors_abbrev":"Takayama S et al.","pubmed_publication_date":"13 Nov 2018","pubmed_entrez_date":"2018-11-15","publication_year":"2018","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2018-11-16 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23112169","title":"Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation-π interactions.","citation":"Proc Natl Acad Sci U S A 2012 Nov 13;109(46):18755-60","abstract":"Alkyltransferase-like (ATL) proteins in Schizosaccharomyces pombe (Atl1) and Thermus thermophilus (TTHA1564) protect against the adverse effects of DNA alkylation damage by flagging O(6)-alkylguanine lesions for nucleotide excision repair (NER). We show that both ATL proteins bind with high affinity to oligodeoxyribonucleotides containing O(6)-alkylguanines differing in size, polarity, and charge of the alkyl group. However, Atl1 shows a greater ability than TTHA1564 to distinguish between O(6)-alkylguanine and guanine and in an unprecedented mechanism uses Arg69 to probe the electrostatic potential surface of O(6)-alkylguanine, as determined using molecular mechanics calculations. An unexpected consequence of this feature is the recognition of 2,6-diaminopurine and 2-aminopurine, as confirmed in crystal structures of respective Atl1-DNA complexes. O(6)-Alkylguanine and guanine discrimination is diminished for Atl1 R69A and R69F mutants, and S. pombe R69A and R69F mutants are more sensitive toward alkylating agent toxicity, revealing the key role of Arg69 in identifying O(6)-alkylguanines critical for NER recognition.","doi":"10.1073/pnas.1209451109","authors":"Wilkinson OJ, Latypov V, Tubbs JL, Millington CL, Morita R, Blackburn H, Marriott A, McGown G, Thorncroft M, Watson AJ, Connolly BA, Grasby JA, Masui R, Hunter CA, Tainer JA, Margison GP, Williams DM","authors_abbrev":"Wilkinson OJ et al.","pubmed_publication_date":"13 Nov 2012","pubmed_entrez_date":"2012-11-01","publication_year":"2012","canto_session_key":"7ca7b767d537166d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"David Williams","canto_first_approved_date":"2016-07-18 13:19:29","canto_approved_date":"2019-08-22 17:03:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-05 15:14:38","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"David Williams","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1250.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-07-18","pdb_entries":[{"pdb_id":"4hdv","gene_chains":[{"gene_uniquename":"SPAC1250.04c","chain":"A","position":"1-108"}],"title":"Crystal structure of S. pombe ATL1 in complex with damaged DNA containing 2,6-diaminopurine","entry_authors":"Tubbs JL,Tainer JA","entry_authors_abbrev":"Tubbs JL et al.","reference_uniquename":"PMID:23112169","experimental_method":"X-ray","resolution":"2.702"},{"pdb_id":"4hdu","gene_chains":[{"gene_uniquename":"SPAC1250.04c","chain":"A","position":"1-108"}],"title":"Crystal structure of S. pombe ATL1 in complex with damaged DNA containing 2-aminopurine","entry_authors":"Tubbs JL,Tainer JA","entry_authors_abbrev":"Tubbs JL et al.","reference_uniquename":"PMID:23112169","experimental_method":"X-ray","resolution":"2.848"}]},{"uniquename":"PMID:11387325","title":"The length, phosphorylation state, and primary structure of the RNA polymerase II carboxyl-terminal domain dictate interactions with mRNA capping enzymes.","citation":"J Biol Chem 2001 Jul 27;276(30):28075-82","abstract":"The carboxyl-terminal domain (CTD) of elongating RNA polymerase II serves as a landing pad for macromolecular assemblies that regulate mRNA synthesis and processing. The capping apparatus is the first of the assemblies to act on the nascent pre-mRNA and the one for which binding of the catalytic components is most clearly dependent on CTD phosphorylation. The present study highlights a distinctive strategy of cap targeting in fission yeast whereby the triphosphatase (Pct1) and guanylyltransferase (Pce1) enzymes of the capping apparatus do not interact physically with each other (as they do in budding yeast and metazoans), but instead bind independently to the phosphorylated CTD. In vivo interactions of Pct1 and Pce1 with the CTD in a two-hybrid assay require 12 and 14 tandem repeats of the CTD heptapeptide, respectively. Pct1 and Pce1 bind in vitro to synthetic CTD peptides containing phosphoserine uniquely at position 5 or doubly at positions 2 and 5 of each of four tandem YSPTSPS repeats, but they bind weakly (Pce1) or not at all (Pct1) to a peptide containing phosphoserine at position 2. These results illustrate how remodeling of the CTD phosphorylation array might influence the recruitment and dissociation of the capping enzymes during elongation. But how does the CTD structure itself dictate interactions with the RNA processing enzymes independent of the phosphorylation state? Using CTD-Ser5 phosphopeptides containing alanine substitutions at other positions of the heptad, we define essential roles for Tyr-1 and Pro-3 (but not Thr-4 or Pro-6) in the binding of Schizosaccharomyces pombe guanylyltransferase. Tyr-1 is also essential for binding and allosteric activation of mammalian guanylyltransferase by CTD Ser5-PO4, whereas alanine mutations of Pro-3 and Pro-6 reduce the affinity for the allosteric CTD-binding site. These are the first structure-activity relationships deduced for an effector function of the phosphorylated CTD.","authors":"Pei Y, Hausmann S, Ho CK, Schwer B, Shuman S","authors_abbrev":"Pei Y et al.","pubmed_publication_date":"27 Jul 2001","pubmed_entrez_date":"2001-06-02","publication_year":"2001","canto_session_key":"bd11a19343ab24bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-29 12:12:56","canto_approved_date":"2024-03-03 10:29:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-29 12:12:48","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.04","SPBC2F12.08c","SPBC28F2.12"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2024-02-29"},{"uniquename":"EMBL:AU013667","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17572388","title":"Biotechnological synthesis of drug metabolites using human cytochrome P450 2D6 heterologously expressed in fission yeast exemplified for the designer drug metabolite 4'-hydroxymethyl-alpha-pyrrolidinobutyrophenone.","citation":"Biochem Pharmacol 2007 Aug 01;74(3):511-20","abstract":"The aim of this study was evaluating the principle feasibility of biotechnological synthesis of drug metabolites using heterologously expressed human cytochrome P450 (CYP) enzymes. Human CYP2D6 expressed in fission yeast (Schizosaccharomyces pombe) strain CAD58 was used as model enzyme and the designer drug 4'-methyl-alpha-pyrrolidinobutyrophenone (MPBP) as model drug. For synthesis of 4'-hydroxmethyl-alpha-pyrrolidinobutyrophenone (HO-MPBP), 250 micromol of MPBP.HNO(3) were incubated with one litre of CAD58 culture (10(8)cells/mL, pH 9, 48 h, 30 degrees C). HO-MPBP was isolated by liquid-liquid extraction and precipitated as its hydrochloride salt. Identity and purity of the product were tested by HPLC with ultraviolet (UV) detection, GC-MS, and (1)H-NMR. CAD58 was further characterized regarding the influence of incubation pH (5-10), cell density (10(7)-10(8)cells/mL), and incubation time (0-120 h) on metabolite formation using the substrates dextromethorphan and MPBP. The preparative experiment yielded 40 mg (141mumol) of HO-MPBP.HCl with a purity of >98%. In the characterization experiments, the metabolite formation rate peaked at pH 8. A linear relationship was observed between cell density and metabolite formation (R(2)>0.996). The rate of metabolite formation was slower in the earlier stages of incubation but then increased. For HO-MPBP, it became constant in the time interval of 2.5-34 h (R(2)>998).","authors":"Peters FT, Dragan CA, Wilde DR, Meyer MR, Zapp J, Bureik M, Maurer HH","authors_abbrev":"Peters FT et al.","pubmed_publication_date":"01 Aug 2007","pubmed_entrez_date":"2007-06-19","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23442800","title":"An E2 enzyme Ubc11 is required for ubiquitination of Slp1/Cdc20 and spindle checkpoint silencing in fission yeast.","citation":"Cell Cycle 2013 Mar 15;12(6):961-71","abstract":"For ordered mitotic progression, various proteins have to be regulated by an ubiquitin ligase, the anaphase-promoting complex or cyclosome (APC/C) with appropriate timing. Recent studies have implied that the activity of APC/C also contributes to release of mitotic checkpoint complexes (MCCs) from its target Cdc20 in the process of silencing the spindle assembly checkpoint (SAC). Here we describe a temperature-sensitive mutant (ubc11-P93L) in which cell cycle progression is arrested at mitosis. The mutant grows normally at the restrictive temperature when SAC is inactivated, suggesting that the arrest is not due to abnormal spindle assembly, but rather due to prolonged activation of SAC. Supporting this notion, MCCs remain bound to APC/C even when SAC is satisfied. The ubc11 (+) gene encodes one of the two E2 enzymes required for progression through mitosis in fission yeast. Remarkably, Slp1 (a fission yeast homolog of Cdc20), which is degraded in an APC/C-dependent manner, stays stable throughout the cell cycle in the ubc11-P93L mutant lacking the functional SAC. Other APC/C substrates, in contrast, were degraded on schedule. We have also found that a loss of Ubc4, the other E2 required for progression through mitosis, does not affect the stability of Slp1. We propose that each of the two E2 enzymes is responsible for collaborating with APC/C for a specific set of substrates, and that Ubc11 is responsible for regulating Slp1 with APC/C for silencing the SAC.","doi":"10.4161/cc.23946","authors":"Horikoshi Y, Habu T, Matsumoto T","authors_abbrev":"Horikoshi Y et al.","pubmed_publication_date":"15 Mar 2013","pubmed_entrez_date":"2013-02-28","publication_year":"2013","canto_session_key":"330f117d21a8480a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomohiro Matsumoto","canto_first_approved_date":"2017-12-08 20:44:43","canto_approved_date":"2024-04-23 11:51:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-23 03:05:22","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":35,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tomohiro Matsumoto","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.02","SPBC14C8.01c","SPAC6F12.14","SPAC821.08c","SPBC16G5.01","SPCC1259.15c","SPBC582.03","SPBC337.08c","SPBC20F10.06","SPBC1604.21c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2017-12-08"},{"uniquename":"PMID:17885803","title":"ROS production by adrenodoxin does not cause apoptosis in fission yeast.","citation":"Apoptosis 2007 Dec;12(12):2135-42","abstract":"We previously showed that production of reactive oxygen species (ROS) caused by overexpression of the mitochondrial electron transfer protein adrenodoxin (Adx) induces apoptosis in mammalian cells. In the fission yeast Schizosaccharomyces pombe, ROS are also produced in cells that undergo an apoptotic-like cell death, but it is not yet clear whether they are actually causative for this phenomenon or whether they are merely produced as a by-product. Therefore, the purpose of this study was to trigger mitochondrial ROS production in fission yeast by overexpression of either wildtype Adx (Adx-WT) or of several activated Adx mutants and to investigate its consequences. It was found that strong expression of either Adx-WT or Adx-S112W did not produce any ROS, while Adx-D113Y caused a twofold and Adx1-108 a threefold increase in ROS formation as compared to basal levels. However, no typical apoptotic markers or decreased viability could be observed in these strains. Since we previously observed that an increase in mitochondrial ROS formation of about 60% above basal levels is sufficient to strongly induce apoptosis in mammalian cells, we conclude that S. pombe is either very robust to mitochondrial ROS production or does not undergo apoptotic cell death in response to mitochondrial ROS at all.","authors":"Derouet-Hümbert E, Drăgan CA, Hakki T, Bureik M","authors_abbrev":"Derouet-Hümbert E et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-09-22","publication_year":"2007","canto_session_key":"400b571b0147ce78","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-10-06 14:14:47","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-06 14:14:40","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-10-06"},{"uniquename":"PMID:15161942","title":"The nucleolus is involved in mRNA export from the nucleus in fission yeast.","citation":"J Cell Sci 2004 Jun 15;117(Pt 14):2887-95","abstract":"To elucidate the mechanism of mRNA export from the nucleus, we isolated five novel temperature-sensitive mutants (ptr7 to ptr11) that accumulate poly(A)(+) RNA in the nuclei at the nonpermissive temperature in Schizosaccharomyces pombe. Of those, the ptr11 mutation was found in the top2(+) gene encoding DNA topoisomerase II. In addition to the nuclear accumulation of poly(A)(+) RNA, ptr11 exhibited the cut (cell untimely torn) phenotype at the nonpermissive temperature, like the previously isolated mutant, ptr4. In these two mutants, cytokinesis occurred without prior nuclear division, resulting in cleavage of the undivided nuclei by the septum. To investigate the relationship between mRNA export defects and the cut phenotype observed in ptr4 and ptr11, we analyzed 11 other mutants displaying the cut phenotype and found that all these tested mutants accumulate poly(A)(+) mRNA in the aberrantly cleaved nuclei. Interestingly, nuclear accumulation of poly(A)(+) mRNA was observed only in the anucleolate nuclei produced by aberrant cytokinesis. In addition, nuc1, the S. pombe mutant exhibiting a collapsed nucleolus, trapped poly(A)(+) mRNA in the nucleolar region at the nonpermissive temperature. In ptr11 and nuc1, mRNA transcribed from the intron-containing TBP gene showed nuclear accumulation, but not transcripts from the intron-less TBP cDNA, suggesting that the export pathway differs between the spliced and unspliced TBP mRNAs. These findings support the notion that a subset of mRNAs in yeast is exported from the nucleus through transient association with the nucleolus.","authors":"Ideue T, Azad AK, Yoshida J, Matsusaka T, Yanagida M, Ohshima Y, Tani T","authors_abbrev":"Ideue T et al.","pubmed_publication_date":"15 Jun 2004","pubmed_entrez_date":"2004-05-27","publication_year":"2004","canto_session_key":"89027fe6a1134146","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-05-10 15:43:47","canto_approved_date":"2025-09-10 10:19:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-28 17:07:28","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.03c","SPAC17C9.13c","SPBC1A4.03c","SPCC962.03c","SPAC17A5.06","SPBC14C8.01c","SPCC5E4.04","SPBC4C3.05c","SPAC56E4.04c","SPBP4H10.06c","SPAC17C9.01c","SPAC25G10.07c","SPAC23C4.18c","SPBC1A4.01","SPBC106.09","SPAC6F12.15c"],"gene_count":16,"ltp_gene_count":13,"approved_date":"2016-05-10"},{"uniquename":"PMID:10488332","title":"Cdc2 phosphorylation of Crb2 is required for reestablishing cell cycle progression after the damage checkpoint.","citation":"Mol Cell 1999 Aug;4(2):167-74","abstract":"DNA damage induces cell cycle arrest (called the damage checkpoint), during which cells carry out actions for repair. A fission yeast protein, Crb2/Rhp9, which resembles budding yeast Rad9p and human BRCA1, promotes checkpoint by activating Chk1 kinase, which restrains Cdc2 activation. We show here that phosphorylation of the T215 Cdc2 site of Crb2 is required for reentering the cell cycle after the damage-induced checkpoint arrest. If this site is nonphosphorylatable, irradiated cells remain arrested, though damage is repaired, and maintain the phosphorylated state of Chk1 kinase. The T215 site is in vitro phosphorylated by purified Cdc2 kinase. Phosphorylation of T215 occurs intensely in response to DNA damage at a late stage, suggesting an antagonistic role of Cdc2 phosphorylation toward checkpoint.","authors":"Esashi F, Yanagida M","authors_abbrev":"Esashi F et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-09-17","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC342.05","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:15377785","title":"Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces.","citation":"Proc Natl Acad Sci U S A 2004 Oct 12;101(41):14725-30","abstract":"Formins are large multidomain proteins required for assembly of actin cables that contribute to the polarity and division of animal and fungal cells. Formin homology-1 (FH1) domains bind profilin, and highly conserved FH2 domains nucleate actin filaments. We characterized the effects of two formins, budding yeast Bni1p and fission yeast Cdc12p, on actin assembly. We used evanescent wave fluorescence microscopy to observe assembly of actin filaments (i) nucleated by soluble formin FH1FH2 domains and (ii) associated with formin FH1FH2 domains immobilized on microscope slides. Bni1p(FH1FH2)p and Cdc12p(FH1FH2)p nucleated new actin filaments or captured the barbed ends of preformed actin filaments that grew by insertion of subunits between the immobilized formin and the barbed end of the filament. Both formins remained bound to growing actin filament barbed ends for >1,000 sec. Elongation of a filament between an immobilized formin and a second anchor point buckled filament segments as short as 0.7 microm, demonstrating that polymerization of single actin filaments produces forces of >1 piconewton, close to the theoretical maximum. After buckling, further growth produced long loops that did not supercoil, suggesting that formins do not stair step along the two subunits exposed on the growing barbed end. In agreement, Arp2/3 complex branched filaments did not rotate as they grew from formins attached to the slide surface. Formins are not mechanistically identical because barbed end elongation from Cdc12(FH1FH2)p, but not Bni1(FH1FH2)p, requires profilin. However, profilin increased the rate of Bni1(FH1FH2)p-mediated barbed end elongation from 75% to 100% of full-speed.","authors":"Kovar DR, Pollard TD","authors_abbrev":"Kovar DR et al.","pubmed_publication_date":"12 Oct 2004","pubmed_entrez_date":"2004-09-21","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15448184","title":"Comparative analysis of complete genomes reveals gene loss, acquisition and acceleration of evolutionary rates in Metazoa, suggests a prevalence of evolution via gene acquisition and indicates that the evolutionary rates in animals tend to be conserved.","citation":"Nucleic Acids Res 2004;32(17):5029-35","abstract":"In this study we systematically examined the differences between the proteomes of Metazoa and other eukaryotes. Metazoans (Homo sapiens, Ceanorhabditis elegans and Drosophila melanogaster) were compared with a plant (Arabidopsis thaliana), fungi (Saccharomyces cerevisiae and Schizosaccaromyces pombe) and Encephalitozoan cuniculi. We identified 159 gene families that were probably lost in the Metazoan branch and 1263 orthologous families that were specific to Metazoa and were likely to have originated in their last common ancestor (LCA). We analyzed the evolutionary rates of pan-eukaryotic protein families and identified those with higher rates in animals. The acceleration was shown to occur in: (i) the LCA of Metazoa or (ii) independently in the Metazoan phyla. A high proportion of the accelerated Metazoan protein families was found to participate in translation and ribosome biogenesis, particularly mitochondrial. By functional analysis we show that no metabolic pathway in animals evolved faster than in other organisms. We conclude that evolution in the LCA of Metazoa was extensive and proceeded largely by gene duplication and/or invention rather than by modification of extant proteins. Finally, we show that the rate of evolution of a gene family in animals has a clear, but not absolute, tendency to be conserved.","authors":"Babenko VN, Krylov DM","authors_abbrev":"Babenko VN et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-09-28","publication_year":"2004","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12511573","title":"Skp1 and the F-box protein Pof6 are essential for cell separation in fission yeast.","citation":"J Biol Chem 2003 Mar 14;278(11):9671-7","abstract":"Here we report functional characterization of the essential fission yeast Skp1 homologue. We have created a conditional allele of skp1 (skp1-3f) mimicking the mutation in the budding yeast skp1-3 allele. Although budding yeast skp1-3 arrests at the G(1)/S transition, skp1-3f cells progress through S phase and instead display two distinct phenotypes. A fraction of the skp1-3f cells arrest in mitosis with high Cdc2 activity. Other skp1-3f cells as well as the skp1-deleted cells accumulate abnormal thick septa leading to defects in cell separation. Subsequent identification of 16 fission yeast F-box proteins led to identification of the product of pof6 (for pombe F-box) as a Skp1-associated protein. Interestingly, cells deleted for the essential pof6 gene display a similar cell separation defect noted in skp1 mutants, and Pof6 localizes to septa and cell tips. Purification of Pof6 demonstrates association of Skp1, whereas the Pcu1 cullin was absent from the complex. These findings reveal an essential non-Skp1-Cdc53/Cullin-F-box protein function for the fission yeast Skp1 homologue and the F-box protein Pof6 in cell separation.","authors":"Hermand D, Bamps S, Tafforeau L, Vandenhaute J, Mäkelä TP","authors_abbrev":"Hermand D et al.","pubmed_publication_date":"14 Mar 2003","pubmed_entrez_date":"2003-01-04","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC409.05","SPCC18.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7555107","title":"Morphogenetic effects induced by spermine and ruthenium red in yeasts.","citation":"Cytobios 1995;81(327):201-11","abstract":"Spermine (Sp) produces growth inhibition and wall malformation in Saccharomyces cerevisiae in response to oversynthesis of beta-glucans and chitin. The effect is related to the polycation nature of the molecule. In the present work, to verify this hypothesis, the yeast was treated with the abiogenic polycation ruthenium red (RR). The strict analogy observed between the RR- and Sp-induced alterations reinforced our earlier assumption that Sp interacted with the anionic sites of the plasmalemma determining a spurious activation of the two inserted enzymes beta-glucan and chitin synthases. This view was further confirmed by the aberrant accumulation of beta-glucans in Schizosaccharomyces pombe and of chitin in Rhodotorula glutinis treated with Sp and RR. In these micro-organisms spermidine, which bears three amino groups instead of the four encountered in Sp, was ineffective. It is inferred that at least four cation sites must be present in a compound in order to affect wall morphogenesis in yeasts.","authors":"Poli F, Pancaldi S, Dall'Olio G, Fasulo MP","authors_abbrev":"Poli F et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29330317","title":"tRNA production links nutrient conditions to the onset of sexual differentiation through the TORC1 pathway.","citation":"EMBO Rep 2018 Mar;19(3)","abstract":"Target of rapamycin (TOR) kinase controls cell growth and metabolism in response to nutrient availability. In the fission yeast  Schizosaccharomyces pombe,  TOR complex 1 (TORC1) promotes vegetative growth and inhibits sexual differentiation in the presence of ample nutrients. Here, we report the isolation and characterization of mutants with similar phenotypes as TORC1 mutants, in that they initiate sexual differentiation even in nutrient-rich conditions. In most mutants identified, TORC1 activity is downregulated and the mutated genes are involved in tRNA expression or modification. Expression of tRNA precursors decreases when cells undergo sexual differentiation. Furthermore, overexpression of tRNA precursors prevents TORC1 downregulation upon nitrogen starvation and represses the initiation of sexual differentiation. Based on these observations, we propose that tRNA precursors operate in the  S. pombe  TORC1 pathway to switch growth mode from vegetative to reproductive.","doi":"10.15252/embr.201744867","authors":"Otsubo Y, Matsuo T, Nishimura A, Yamamoto M, Yamashita A","authors_abbrev":"Otsubo Y et al.","pubmed_publication_date":"Mar 2018","pubmed_entrez_date":"2018-01-14","publication_year":"2018","canto_session_key":"1161e0589c8a3c5a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Akira Yamashita","canto_first_approved_date":"2018-11-21 19:46:31","canto_approved_date":"2026-01-25 11:56:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-11-01 07:04:27","canto_added_date":"2018-01-16 01:15:25","annotation_curators":[{"name":"Akira Yamashita","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Antonia Lock","community_curator":false,"annotation_count":63,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP27G11.04c","SPAC31G5.12c","SPBC19C7.06","SPBC216.07c","SPAC10F6.03c","SPCC16C4.14c","SPAC4F10.07c","SPCC4G3.08","SPCC290.02","SPAC26F1.13c","SPAC57A10.10c","SPBC1773.10c","SPBC337.13c","SPCC330.10","SPBC19C2.05","SPBC25H2.02"],"gene_count":16,"ltp_gene_count":14,"approved_date":"2018-11-21"},{"uniquename":"PMID:39174851","title":"CDK phosphorylation of Sfr1 downregulates Rad51 function in late-meiotic homolog invasions.","citation":"EMBO J 2024 Aug 22;","abstract":"Meiosis is the developmental program that generates gametes. To produce healthy gametes, meiotic recombination creates reciprocal exchanges between each pair of homologous chromosomes that facilitate faithful chromosome segregation. Using fission yeast and biochemical, genetic, and cytological approaches, we have studied the role of CDK (cyclin-dependent kinase) in the control of Swi5-Sfr1, a Rad51-recombinase auxiliary factor involved in homolog invasion during recombination. We show that Sfr1 is a CDK target, and its phosphorylation downregulates Swi5-Sfr1 function in the meiotic prophase. Expression of a phospho-mimetic sfr1-7D mutant inhibits Rad51 binding, its robust chromosome loading, and subsequently decreases interhomolog recombination. On the other hand, the non-phosphorylatable sfr1-7A mutant alters Rad51 dynamics at late prophase, and exacerbates chromatin segregation defects and Rad51 retention observed in dbl2 deletion mutants when combined with them. We propose Sfr1 phospho-inhibition as a novel cell-cycle-dependent mechanism, which ensures timely resolution of recombination intermediates and successful chromosome distribution into the gametes. Furthermore, the N-terminal disordered part of Sfr1, an evolutionarily conserved feature, serves as a regulatory platform coordinating this phospho-regulation, protein localization and stability, with several CDK sites and regulatory sequences being conserved.","doi":"10.1038/s44318-024-00205-2","authors":"Palacios-Blanco I, Gómez L, Bort M, Mayerová N, Bágeľová Poláková S, Martín-Castellanos C","authors_abbrev":"Palacios-Blanco I et al.","pubmed_publication_date":"22 Aug 2024","pubmed_entrez_date":"2024-08-22","publication_year":"2024","canto_session_key":"8a93d8122afe38cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Cristina Martín-Castellanos","canto_first_approved_date":"2024-10-16 11:51:53","canto_approved_date":"2024-11-04 13:40:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-09-25 12:59:15","canto_added_date":"2024-08-23 23:25:05","annotation_curators":[{"name":"Cristina Martín-Castellanos","community_curator":true,"annotation_count":36,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":20,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC553.01c","SPBC11B10.09","SPBC582.03","SPAC644.14c","SPBC28F2.07","SPAC17A5.11"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2024-10-16"},{"uniquename":"PMID:22684255","title":"The S. pombe cytokinesis NDR kinase Sid2 activates Fin1 NIMA kinase to control mitotic commitment through Pom1/Wee1.","citation":"Nat Cell Biol 2012 Jun 10;14(7):738-45","abstract":"Mitotic exit integrates the reversal of the phosphorylation events initiated by mitotic kinases with a controlled cytokinesis event that cleaves the cell in two. The mitotic exit network (MEN) of budding yeast regulates both processes, whereas the fission yeast equivalent, the septum initiation network (SIN), controls only the execution of cytokinesis. The components and architecture of the SIN and MEN are highly conserved. At present, it is assumed that the functions of the core SIN-MEN components are restricted to their characterized roles at the end of mitosis. We now show that the NDR (nuclear Dbf2-related) kinase component of the fission yeast SIN, Sid2-Mob1, acts independently of the other known SIN components in G2 phase of the cell cycle to control the timing of mitotic commitment. Sid2-Mob1 promotes mitotic commitment by directly activating the NIMA (Never In Mitosis)-related kinase Fin1. Fin1's activation promotes its own destruction, thereby making Fin1 activation a transient feature of G2 phase. This spike of Fin1 activation modulates the activity of the Pom1/Cdr1/Cdr2 geometry network towards Wee1.","doi":"10.1038/ncb2514","authors":"Grallert A, Connolly Y, Smith DL, Simanis V, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"10 Jun 2012","pubmed_entrez_date":"2012-06-12","publication_year":"2012","canto_session_key":"4927cddae28a3185","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-24 16:53:52","canto_approved_date":"2024-07-02 17:48:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-24 16:53:34","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":29,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.06c","SPBC409.05","SPBC11B10.09","SPAC2F7.03c","SPAC19E9.02","SPAC24B11.11c","SPAC57A10.02","SPBC428.13c","SPBC23G7.04c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2020-12-24"},{"uniquename":"PMID:9450991","title":"Essential role of tubulin-folding cofactor D in microtubule assembly and its association with microtubules in fission yeast.","citation":"EMBO J 1998 Feb 02;17(3):658-66","abstract":"The main structural components of microtubules are alpha- and beta-tubulins. A group of proteins called cofactors are crucial in the formation of assembly-competent tubulin molecules in vitro. Whilst an in vitro role is emerging for these cofactors, their biological functions in vivo remain to be established. In order to understand the fundamental mechanisms that determine cell polarity, we have screened for fission yeast mutants with altered polarity. Here we show that alp1+ encodes a homologue of cofactor D and executes a function essential for cell viability. A temperature-sensitive alp1 mutant shows a variety of defects including abnormal mitoses, loss of microtubule structures, displacement of the nucleus, altered growth polarity and asymmetrical cell division. Overexpression of Alp1 is lethal in wild-type cells, resulting in altered cell shape, but is rescued by co-overexpression of beta-tubulin. Alp1 co-localizes with microtubules, both interphase arrays and mitotic spindles. Furthermore, Alp1 binds to and co-sediments with taxol (paclitaxel)-stabilized porcine microtubules. Our results suggest that, in addition to a function in the folding of beta-tubulin, cofactor D may play a vital role in microtubule-dependent processes as a microtubule-associated protein.","authors":"Hirata D, Masuda H, Eddison M, Toda T","authors_abbrev":"Hirata D et al.","pubmed_publication_date":"02 Feb 1998","pubmed_entrez_date":"1998-03-14","publication_year":"1998","canto_session_key":"37cb96e688f6a42c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-05-04 00:10:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-02 13:48:59","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPBC11C11.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-03-02"},{"uniquename":"PMID:2308866","title":"Transformation of Schizosaccharomyces pombe by electroporation.","citation":"Nucleic Acids Res 1990 Feb 11;18(3):688","abstract":"","authors":"Hood MT, Stachow C","authors_abbrev":"Hood MT et al.","pubmed_publication_date":"11 Feb 1990","pubmed_entrez_date":"1990-02-11","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21844224","title":"Spt6 is required for heterochromatic silencing in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2011 Oct;31(20):4193-204","abstract":"Spt6 is a conserved factor, critically required for several transcription- and chromatin-related processes. We now show that Spt6 and its binding partner, Iws1, are required for heterochromatic silencing in Schizosaccharomyces pombe. Our studies demonstrate that Spt6 is required for silencing of all heterochromatic loci and that an spt6 mutant has an unusual combination of heterochromatic phenotypes compared to previously studied silencing mutants. Unexpectedly, we find normal nucleosome positioning over heterochromatin and normal levels of histone H3K9 dimethylation at the endogenous pericentric repeats. However, we also find greatly reduced levels of H3K9 trimethylation, elevated levels of H3K14 acetylation, reduced recruitment of several silencing factors, and defects in heterochromatin spreading. Our evidence suggests that Spt6 plays a role at both the transcriptional and posttranscriptional levels; in an spt6 mutant, RNA polymerase II (RNAPII) occupancy at the pericentric regions is only modestly increased, while production of small interfering RNAs (siRNAs) is lost. Taken together, our results suggest that Spt6 is required for multiple steps in heterochromatic silencing by controlling chromatin, transcriptional, and posttranscriptional processes.","doi":"10.1128/MCB.05568-11","authors":"Kiely CM, Marguerat S, Garcia JF, Madhani HD, Bähler J, Winston F","authors_abbrev":"Kiely CM et al.","pubmed_publication_date":"Oct 2011","pubmed_entrez_date":"2011-08-17","publication_year":"2011","canto_session_key":"97535c919f7436fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-08-25 15:19:15","canto_approved_date":"2021-08-25 06:19:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-10-18 08:13:29","canto_added_date":"2012-02-17 11:02:58","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.08c","SPAC664.01c","SPBC19G7.16","SPAC17G8.13c","SPAC1952.05","SPAC1F7.01c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2018-08-25"},{"uniquename":"PMID:15196933","title":"Two different dihydroorotate dehydrogenases from yeast Saccharomyces kluyveri.","citation":"FEBS Lett 2004 Jun 18;568(1-3):129-34","abstract":"Genes for two structurally and functionally different dihydroorotate dehydrogenases (DHODHs, EC 1.3.99.11), catalyzing the fourth step of pyrimidine biosynthesis, have been previously found in yeast Saccharomyces kluyveri. One is closely related to the Schizosaccharomyces pombe mitochondrial family 2 enzymes, which use quinones as direct and oxygen as the final electron acceptor. The other one resembles the Saccharomyces cerevisiae cytosolic family 1A fumarate-utilizing DHODH. The DHODHs from S. kluyveri, Sch. pombe and S. cerevisiae, were expressed in Escherichia coli and compared for their biochemical properties and interaction with inhibitors. Benzoates as pyrimidine ring analogs were shown to be selective inhibitors of cytosolic DHODs. This unique property of Saccharomyces DHODHs could appoint DHODH as a species-specific target for novel anti-fungal therapeutics.","authors":"Zameitat E, Knecht W, Piskur J, Löffler M","authors_abbrev":"Zameitat E et al.","pubmed_publication_date":"18 Jun 2004","pubmed_entrez_date":"2004-06-16","publication_year":"2004","canto_session_key":"437e9f08bd800cd3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-04-29 14:39:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-04-30 07:13:46","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-30"},{"uniquename":"PMID:22901093","title":"Generalized adjacency and the conservation of gene clusters in genetic networks defined by synthetic lethals.","citation":"BMC Bioinformatics 2012 Jun 11;13 Suppl 9(Suppl 9):S8","abstract":"Given genetic networks derived from two genomes, it may be difficult to decide if their local structures are similar enough in both genomes to infer some ancestral configuration or some conserved functional relationships. Current methods all depend on searching for identical substructures.\nWe explore a generalized vertex proximity criterion, and present analytic and probability results for the comparison of random lattice networks.\nWe apply this criterion to the comparison of the genetic networks of two evolutionarily divergent yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe, derived using the Synthetic Genetic Array screen. We show that the overlapping parts of the networks of the two yeasts share a common structure beyond the shared edges. This may be due to their conservation of redundant pathways containing many synthetic lethal pairs of genes.\nDetecting the shared generalized adjacency clusters in the genetic networks of the two yeasts show that this analytical construct can be a useful tool in probing conserved network structure across divergent genomes.","doi":"10.1186/1471-2105-13-S9-S8","authors":"Yang Z, Sankoff D","authors_abbrev":"Yang Z et al.","pubmed_publication_date":"11 Jun 2012","pubmed_entrez_date":"2012-08-21","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14701809","title":"Ddb1 is required for the proteolysis of the Schizosaccharomyces pombe replication inhibitor Spd1 during S phase and after DNA damage.","citation":"J Biol Chem 2004 Mar 12;279(11):9937-43","abstract":"Recently we showed that the Schizosaccharomyces pombe ddb1 gene plays a role in S phase progression. A mutant S. pombe strain lacking expression of the ddb1 gene exhibited slow replication through both early and late regions causing a slow S phase phenotype. We attributed the phenotypes in the ddb1 strain to an increased activity of the replication checkpoint kinase Cds1. However, the basis for a high basal Cds1 activity in the ddb1 strain was not clear. It was shown that Ddb1 associates with the Cop9/signalosome. Moreover, the phenotypes of the Deltaddb1 strain are remarkably similar to the Deltacsn1 (or Deltacsn2) strain that lacks expression of the Csn1 (or Csn2) subunit of the Cop9/signalosome. Cop9/signalosome cooperates with Pcu4 to induce proteolysis of Spd1, which inhibits DNA replication by inhibiting ribonucleotide reductase. Therefore, we investigated whether Ddb1 is required for the proteolysis of Spd1. Here we show that a S. pombe strain lacking expression of Ddb1 fails to induce proteolysis of Spd1 in S phase and after DNA damage. Moreover, deletion of the spd1 gene attenuates the Cds1 kinase activity in cells lacking the expression of ddb1, suggesting that an accumulation of Spd1 results in the increase of Cds1 activity in the Deltaddb1 strain. In addition, the double mutant lacking spd1 and ddb1 no longer exhibits the growth defects and DNA damage sensitivity observed in the Deltaddb1 strain. Our results establish an essential role of Ddb1 in the proteolysis of Spd1. In addition, the observation provides evidence for a functional link between Ddb1 and the Cop9/signalosome.","authors":"Bondar T, Ponomarev A, Raychaudhuri P","authors_abbrev":"Bondar T et al.","pubmed_publication_date":"12 Mar 2004","pubmed_entrez_date":"2004-01-01","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.03","SPAC24H6.05","SPAC17H9.10c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:22146723","title":"Systematic localization study on novel proteins encoded by meiotically up-regulated ORFs in fission yeast.","citation":"Biosci Biotechnol Biochem 2011;75(12):2364-70","abstract":"We conducted a mitotic localization study on gene products encoded by 56 uncharacterized fission yeast ORFs that were transcriptionally up-regulated during meiotic division. Despite meiotic gene induction, these genes were expressed during mitosis as well. Seven gene products were localized in the nucleus and/or chromatin; another one was a mitosis-specific spindle pole body component and, intriguingly, its human homologue was also localized in the centrosome of cultured HeLa cells. Two products appeared to be localized in cytoplasmic microtubules, whereas four were mitochondrial proteins. Three other proteins were found in the medial ring upon cytokinesis and another was localized on the entire cell periphery. The remaining 38 proteins were detected in the cytoplasm and showed varied spatial patterns. This systematic study helps our integrated understanding of all the protein functions in the fission yeast as a eukaryotic model.","authors":"Ikebe C, Konishi M, Hirata D, Matsusaka T, Toda T","authors_abbrev":"Ikebe C et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-12-08","publication_year":"2011","canto_session_key":"3bfd50812796b793","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-12-15 14:58:33","canto_approved_date":"2026-02-15 08:22:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-05 01:26:33","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.17c","SPBC19C2.10","SPAC12B10.10","SPBC23G7.06c","SPCC1442.02","SPAP27G11.12","SPAC3H1.13","SPCC63.05","SPBC2G2.10c","SPBC1861.09","SPCC663.15c","SPBC27.04","SPBC21D10.08c","SPAC890.04c","SPAC144.07c","SPBC16E9.07","SPAC8C9.04","SPAC17G8.12","SPAC6G9.04","SPCC1682.03c","SPAC323.03c","SPBC211.03c","SPBC651.06","SPAC8C9.09c","SPAC890.03","SPBC1539.02","SPAC1687.10","SPCC4F11.03c","SPBC27B12.05","SPAC25H1.04","SPAC12G12.09","SPAC7D4.13c","SPAC328.08c","SPBC32H8.09","SPBP23A10.14c","SPBC28E12.04","SPBC713.09","SPBC651.12c","SPBC31F10.17c","SPAC3H8.04","SPAC17A2.08c","SPBC25H2.15","SPAC17A5.16","SPCC1322.02","SPCC1739.04c","SPAC15A10.13","SPAC25A8.02","SPCC553.01c","SPAC1A6.08c","SPBC25B2.07c","SPAC1610.04","SPAC5D6.02c","SPAPB21F2.02","SPAC16A10.08c","SPBC1773.09c","SPBC115.02c"],"gene_count":56,"ltp_gene_count":0,"approved_date":"2017-12-15"},{"uniquename":"PMID:2197558","title":"Striking conservation of TFIID in Schizosaccharomyces pombe and Saccharomyces cerevisiae.","citation":"Nature 1990 Jul 19;346(6281):291-4","abstract":"Eukaryotic promoters contain binding sites for basic transcription factors and gene-specific activator proteins. The transcription factors interact at the TATA box, which lies close to the position of transcription initiation. Activators typically bind to distant sites that can lie kilobases away from the initiation site. The factor TFIID binds specifically to the TATA box to initiate an ordered pathway of assembly of the basic transcription factors. Biochemical analyses have shown that human and Saccharomyces cerevisiae TFIID are functionally interchangeable in vitro. To study further the functional conservation of this critical factor, we are surveying proteins from divergent organisms that can substitute in vivo for the S. cerevisiae TFIID. We report here the isolation of a unique gene from Schizosaccharomyces pombe that fully complements a null mutation in SPT15, the gene that encodes TFIID in S. cerevisiae. The Schiz. pombe gene encodes a protein 93% identical (166/178) to S. cerevisiae TFIID in a region consisting of a direct repeat.","authors":"Fikes JD, Becker DM, Winston F, Guarente L","authors_abbrev":"Fikes JD et al.","pubmed_publication_date":"19 Jul 1990","pubmed_entrez_date":"1990-07-19","publication_year":"1990","canto_session_key":"e854e8f6cd924d1a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-09-01 11:20:35","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-09-01 11:20:28","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29E6.08"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2017-09-01"},{"uniquename":"PMID:17272281","title":"Rad4TopBP1 associates with Srr2, an Spc1 MAPK-regulated protein, in response to environmental stress.","citation":"J Biol Chem 2007 Mar 23;282(12):8793-800","abstract":"Rad4(TopBP1) is a scaffold in a protein complex containing both replication proteins and checkpoint proteins and plays essential roles in both replication and checkpoint responses. We have previously identified four novel fission yeast mutants of rad4+(TopBP1) to explore how Rad4(TopBP1), a single protein, can play multiple roles in genomic integrity maintenance. Among the four novel mutants, rad4-c17(TopBP1) is a thermosensitive mutant. Here, we characterized rad4-c17(TopBP1) and identified a rad4-c17(TopBP1) allele specific suppressor named srr2+ (suppressor of Rad4(TopBP1) R2 domain). srr2+ has previously been identified as an environmental stress-responsive gene (GenBank accession number AL049644.1, locus spcc191.01). srr2+ null cells are sensitive to hydroxyurea (HU) at elevated temperatures. Deletion of srr2+ in rad4-c17(TopBP1) exacerbates the HU sensitivity of the mutant. Overexpression of srr2+ suppresses the rad4-c17(TopBP1) mutant sensitivity to temperature and HU and restores the compromised ability of rad4-c17(TopBP1) to activating Cds1 kinase in response to HU treatment. Furthermore, stress-activated MAPK, Spc1 (also known as StyI or Phh1), induces the expression and phosphorylation of the Srr2 protein. Significantly, environmental stress induces co-precipitation of Srr2 protein with Rad4(TopBP1), and the co-precipitation is compromised in the rad4-c17(TopBP1) mutant. These results have led us to propose a model; Rad4(TopBP1) exists in a large protein complex to coordinate genomic perturbations with checkpoint responses to maintain genomic integrity. In addition, when cells experience environmental stress, Rad4(TopBP1) associates with Srr2, an Spc1 MAPK-responsive protein, to survive the stress, potentially by providing a link of the Spc1 MAPK response to checkpoint responses.","authors":"Taricani L, Wang TS","authors_abbrev":"Taricani L et al.","pubmed_publication_date":"23 Mar 2007","pubmed_entrez_date":"2007-02-03","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.18c","SPCC191.01"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:15657058","title":"The role of the regulatory subunit of fission yeast calcineurin for in vivo activity and its relevance to FK506 sensitivity.","citation":"J Biol Chem 2005 Apr 01;280(13):12231-8","abstract":"Calcineurin, a protein phosphatase required for Ca2+ signaling in many cell types, is a heterodimer composed of catalytic and regulatory subunits. The fission yeast genome encodes a single set of catalytic (Ppb1) and regulatory (Cnb1) subunits, providing an ideal model system to study the functions of these subunits in vivo. Here, we cloned the cnb1+ gene and showed that the cnb1 knock-out (Deltacnb1) exhibits identical phenotypes with Deltappb1 and that overexpression of Ppb1 failed to suppress the phenotypes of Deltacnb1. Interestingly, overexpression of the C-terminal-deleted Ppb1 (Ppb1DeltaC), the constitutively active form of Ppb1, also failed to suppress the phenotypes of Deltacnb1. FK506 caused MgCl2 sensitivity to the wild-type cells in an FKBP12-dependent manner. Co-overexpression of Ppb1 and Cnb1 suppressed the FK506-induced MgCl2 sensitivity, but the suppression was only partial, suggesting that an excess amount of the Ppb1-Cnb1 complex cannot compete out the FKBP12-FK506 complex. Although overexpression of Ppb1DeltaC alone had little effect on cell growth, co-overexpression of Ppb1DeltaC and Cnb1 caused a distinct growth defect. FK506 suppressed the growth defect when Cnb1 was co-expressed using the attenuated nmt1 promoter, but it failed to suppress the defect when Cnb1 was co-expressed using the wild-type nmt1 promoter. Knock-out of the prz1+ gene, encoding a downstream target transcription factor of calcineurin, suppressed the growth defect irrespective of the promoter potency. These results suggest that Cnb1 is essential for the activation of calcineurin and that the activated calcineurin is the pharmacological target of the FKBP12-FK506 complex in vivo.","authors":"Sio SO, Suehiro T, Sugiura R, Takeuchi M, Mukai H, Kuno T","authors_abbrev":"Sio SO et al.","pubmed_publication_date":"01 Apr 2005","pubmed_entrez_date":"2005-01-20","publication_year":"2005","canto_session_key":"3fbb994e3bfea4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-07-27 20:57:44","canto_approved_date":"2024-06-26 13:49:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-16 17:12:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC830.06","SPBC1685.01","SPAC4G8.13c","SPBP4H10.04"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-07-27"},{"uniquename":"PMID:16855021","title":"Fta2, an essential fission yeast kinetochore component, interacts closely with the conserved Mal2 protein.","citation":"Mol Biol Cell 2006 Oct;17(10):4167-78","abstract":"The fission yeast multiprotein-component Sim4 complex plays a fundamental role in the assembly of a functional kinetochore. It affects centromere association of the histone H3 variant CENP-A as well as kinetochore association of the DASH complex. Here, multicopy suppressor analysis of a mutant version of the Sim4 complex component Mal2 identified the essential Fta2 kinetochore protein, which is required for bipolar chromosome attachment. Kinetochore localization of Mal2 and Fta2 depends on each other, and overexpression of one protein can rescue the phenotype of the mutant version of the other protein. fta2 mal2 double mutants were inviable, implying that the two proteins have an overlapping function. This close interaction with Fta2 is not shared by other Sim4 complex components, indicating the existence of functional subgroups within this complex. The Sim4 complex seems to be assembled in a hierarchical way, because Fta2 is localized correctly in a sim4 mutant. However, Fta2 kinetochore localization is reduced in a spc7 mutant. Spc7, a suppressor of the EB1 family member Mal3, is part of the conserved Ndc80-MIND-Spc7 kinetochore complex.","authors":"Kerres A, Jakopec V, Beuter C, Karig I, Pöhlmann J, Pidoux A, Allshire R, Fleig U","authors_abbrev":"Kerres A et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-07-21","publication_year":"2006","canto_session_key":"61ef992598fe7287","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-12-17 18:19:23","canto_approved_date":"2026-06-21 06:53:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-17 17:59:56","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP22H7.09c","SPAC25B8.14","SPAC16A10.05c","SPCC1020.02","SPAC1783.03","SPBC18E5.03c","SPBC21.01","SPBC20F10.06","SPBC106.01","SPAC1687.20c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2014-12-17"},{"uniquename":"PMID:5574427","title":"On the effect of caffeine on mutation and recombination in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1971;110(4):348-54","abstract":"","authors":"Loprieno N, Schüpbach M","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"1971","pubmed_entrez_date":"1971-01-01","publication_year":"1971","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26960792","title":"Rga6 is a Fission Yeast Rho GAP Involved in Cdc42 Regulation of Polarized Growth.","citation":"Mol Biol Cell 2016 Mar 09;27(9):1524-35","abstract":"Active Cdc42 is essential for the establishment of polarized growth. This GTPase is negatively regulated by the GTPase-activating proteins (GAPs), which are important for the spatial specificity of Cdc42 function. Rga4 is the only GAP described as negative regulator of fission yeast Cdc42. We report here that Rga6 is another fission yeast Cdc42 GAP which shares some functions with Rga4. Cells lacking Rga6 are viable but slightly shorter and broader than wild type, and cells lacking Rga6 and Rga4 simultaneously are rounded. In these cells, active Cdc42 is observed all around the membrane. These additive effects indicate that both GAPs collaborate in the spatial regulation of active Cdc42. Rga6 localizes to the plasma membrane forming clusters different from those formed by Rga4. A polybasic region at the Rga6 C-terminus is responsible for its membrane localization. Rga6-GFP fluorescence decreases considerably at the growing tips, and this decrease is dependent on the actin cables. Notably, in the absence of Rga6 the amplitude of active Cdc42 oscillations at the tips decreases, and less GTP-Cdc42 accumulates at the new end of the cells. We propose here that Rga6 collaborates with Rga4 to spatially restrict active Cdc42 at the cell tips and maintain cell dimensions.","authors":"Revilla-Guarinos MT, Martín-García R, Villar-Tajadura MA, Estravís M, Coll PM, Pérez P","authors_abbrev":"Revilla-Guarinos MT et al.","pubmed_publication_date":"09 Mar 2016","pubmed_entrez_date":"2016-03-11","publication_year":"2016","canto_session_key":"e740e740b75c99d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pilar Perez","canto_first_approved_date":"2020-03-24 11:30:49","canto_approved_date":"2022-10-05 06:50:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-11 13:03:20","canto_added_date":"2016-03-12 01:15:29","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":36,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pilar Perez","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.11","SPAC110.03","SPCC895.05","SPBC28E12.03","SPAC16.01","SPAC4F10.15c","SPAC16E8.09","SPBC354.13"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2020-03-24"},{"uniquename":"PMID:15157889","title":"Imaging green fluorescent protein fusions in living fission yeast cells.","citation":"Methods 2004 Jul;33(3):220-5","abstract":"The use of green fluorescent protein (GFP) fusions as biosensors for examining protein localization and dynamics has revolutionized cell biology. Here, we describe the methods developed for imaging of GFP-fusions in the fission yeast Schizosaccharomyces pombe using fluorescence microscopy, with a focus on the use of time-lapse imaging to analyze the dynamics of microtubules. We discuss the considerations in fluorescence microscopy, cell preparation, data acquisition, and image analysis appropriate for analysis of living cells.","authors":"Tran PT, Paoletti A, Chang F","authors_abbrev":"Tran PT et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC06158","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1394510","title":"Regulation of pho1-encoded acid phosphatase of Schizosaccharomyces pombe by adenine and phosphate.","citation":"Curr Genet 1992 Oct;22(4):289-92","abstract":"Expression of pho1-encoded acid phosphatase of Schizosaccharomyces pombe has been reported to be regulated by phosphate. In this communication we show that it is also regulated by adenine. Starving adenine auxotrophic strains for adenine leads to a drastic increase of the enzymatic activity while adenine represses this activity. Full repression by adenine only occurs when phosphate is not growth limiting and vice versa. Regulation occurs at the level of mRNA. We isolated adenine non-repressible mutants. They define four genes (anr1, anr2, anr3, and anr5) which are involved in adenine-dependent pho1 expression. All anr mutants are also phosphate non-repressible. These results indicate that the generation and/or transduction of the intracellular signal responsible for pho1 repression is simultaneously dependent on both adenine and phosphate.","authors":"Schweingruber ME, Edenharter E, Zurlinden A, Stockmaier KM","authors_abbrev":"Schweingruber ME et al.","pubmed_publication_date":"Oct 1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_session_key":"33ea74c3360233bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-06-16 14:55:46","canto_approved_date":"2022-11-01 21:41:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-03 10:45:14","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.10","SPAC6F12.10c","SPBP4G3.02","SPBC14F5.09c","SPAC8E11.02c","SPBC405.01","SPBC428.03c","SPAC144.03","SPCC569.08c","SPCC1322.13","SPAC4D7.08c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2016-06-16"},{"uniquename":"EMBL:AU006799","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011236","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1779824","title":"Cadmium-binding peptide complexes from Schizosaccharomyces pombe.","citation":"Methods Enzymol 1991;205:603-10","abstract":"","authors":"Plocke DJ","authors_abbrev":"Plocke DJ","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1644273","title":"The clr1 locus regulates the expression of the cryptic mating-type loci of fission yeast.","citation":"Genetics 1992 Jun;131(2):287-96","abstract":"The mat2-P and mat3-M loci of fission yeast contain respectively the plus (P) and minus (M) mating-type information in a transcriptionally silent state. That information is transposed from the mat2 or mat3 donor locus via recombination into the expressed mating-type locus (mat1) resulting in switching of the cellular mating type. We have identified a gene, named clr1 (for cryptic loci regulator), whose mutations allow expression of the mat2 and mat3 loci. clr1 mutants undergo aberrant haploid meiosis, indicative of transcription of the silent genes. Production of mRNA from mat3 is detectable in clr1 mutants. Furthermore, the ura4 gene inserted near mat3, weakly expressed in wild-type cells, is derepressed in clr1 mutants. The clr1 mutations also permit meiotic recombination in the 15-kb mat2-mat3 interval, where recombination is normally inhibited. The clr1 locus is in the right arm of chromosome II. We suggest that clr1 regulates silencing of the mat2 and mat3 loci, and participates in establishing the \"cold spot\" for recombination by organizing the chromatin structure of the mating-type region.","authors":"Thon G, Klar AJ","authors_abbrev":"Thon G et al.","pubmed_publication_date":"Jun 1992","pubmed_entrez_date":"1992-06-01","publication_year":"1992","canto_session_key":"cd3459d6dadd81ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-02-13 11:13:23","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-11-01 12:15:59","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"vw253 cam.ac.uk","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.17"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-11-01"},{"uniquename":"PMID:11713305","title":"A second eIF4E protein in Schizosaccharomyces pombe has distinct eIF4G-binding properties.","citation":"Nucleic Acids Res 2001 Nov 15;29(22):4561-9","abstract":"The eukaryotic cap-binding proteins belonging to the eIF4E family are generally involved in mediating the recruitment of ribosomes to capped mRNA. We described previously a cap-binding protein (now called eIF4E1) in Schizosaccharomyces pombe that appears to have all of the usual structural and functional attributes of an eIF4E. We have now characterised a new type of cap-binding protein (eIF4E2) from this organism, which at the amino acid sequence level, is 52% identical and 59% similar to eIF4E1. eIF4E2 is not essential in S.pombe but has some novel properties that may be related to a special function in the cell. The ratio of eIF4E2:eIF4E1 in the cell shifts in favour of eIF4E2 at higher temperatures. Despite having all of the dorsal face amino acids that have so far been associated with eIF4G binding to eIF4E1, eIF4E2 binds the eIF4E-binding domain of S.pombe eIF4G >10(2)-times weaker than eIF4E1 in vitro. The eIF4E2 cap-binding affinity is in the typical micromolar range. The results suggest that eIF4E2 is not active on the main pathway of translation initiation in fission yeast but might play a role in the adaptation strategy of this organism under specific growth conditions. Moreover, they provide insight into the molecular characteristics required for tight binding to eIF4G.","authors":"Ptushkina M, Berthelot K, von der Haar T, Geffers L, Warwicker J, McCarthy JE","authors_abbrev":"Ptushkina M et al.","pubmed_publication_date":"15 Nov 2001","pubmed_entrez_date":"2001-11-20","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1629244","title":"Visualization of centromeric and nucleolar DNA in fission yeast by fluorescence in situ hybridization.","citation":"J Cell Sci 1992 Feb;101 ( Pt 2):267-75","abstract":"The nucleolar and centromeric DNAs of the fission yeast Schizosaccharomyces pombe were visualized in the nucleus by fluorescence in situ hybridization using repetitive ribosomal and centromeric DNAs as the probes. The rDNAs were seen in the nuclear domain previously assigned as nucleolar, that is, the region into which the rod-like chromatin protrudes from the hemispherical chromosomal domain. Using mitotically-arrested cells containing condensed chromosomes, it was demonstrated that the rDNAs were present on the smallest chromosome III, consistent with genetic data. Using a centromeric repetitive element as the hybridization probe, the centromere of chromosome III, cen3, which contains the largest number of the repetitive elements, was visualized. The centromere in interphase cells is located near the periphery of the nucleus as a single dot. Early in mitosis, however, it divides into two and is situated in the middle of the short mitotic spindle. After spindle extension in anaphase, the centromeric DNA is present at both ends of the spindle, that is, near the spindle pole bodies. The movement of cen3 during mitosis (anaphase A and B) is discussed in relation to spindle dynamics and chromosome separation.","authors":"Uzawa S, Yanagida M","authors_abbrev":"Uzawa S et al.","pubmed_publication_date":"Feb 1992","pubmed_entrez_date":"1992-02-01","publication_year":"1992","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12653962","title":"A brute force postgenome approach to identify temperature-sensitive mutations that negatively interact with separase and securin plasmids.","citation":"Genes Cells 2003 Apr;8(4):341-55","abstract":"The fission yeast Schizosaccharomyces pombe separase/Cut1 and securin/Cut2 are required for anaphase-specific activation of proteolysis that leads to proper sister chromatid separation. We intended to identify ts (temperature sensitive) strains whose growth was inhibited by multicopy plasmid pCUT1 or pCUT2 at the permissive temperature.\nAfter a one-by-one transformation of 1015 randomly isolated ts strains, 18 transformants that retarded in colony formation at the permissive or semipermissive temperature were isolated. Six of them, in the absence of pCUT1 or pCUT2, produced mitotic phenotypes with condensed chromosomes at the restrictive temperature. Gene cloning established that these mutants were defective in either the subunits (Cut9, Cut23, Cut20 or Apc10) of APC (anaphase promoting complex)/cyclosome or Cut8, a regulator for 26S proteasome localization. The inhibitory effect of separase against APC/cyclosome mutations was abolished when the catalytic site mutation C1730A was introduced and overproduced, indicating that inhibition needs an active separase. Securin/Cut2 overproduction also caused a negative effect on these mutants. Surprisingly, the phenotypes of cut9 and cut23 in the presence of pCUT1 or pCUT2 were not the mitotic arrest, and they were strikingly different depending on pCUT1 or pCUT2.\nThis study shows the functional link between separase/Cut1 and APC/cyclosome in a separase activity-dependent manner. The negative effect of active separase overproduction on APC/cyclosome mutations is possibly due to the direct inhibition of APC/cyclosome. In addition, the manner of the inhibition by high copy securin and separase plasmids were quite different each other and did not result in the mitotic block.","authors":"Matsumura T, Yuasa T, Hayashi T, Obara T, Kimata Y, Yanagida M","authors_abbrev":"Matsumura T et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-03-26","publication_year":"2003","canto_session_key":"809618c56c11583b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-08-22 21:13:25","canto_approved_date":"2022-08-17 12:28:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-14 14:15:56","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.13c","SPAC6F12.14","SPCC5E4.04","SPAC821.08c","SPAC8E11.02c","SPAC19G12.01c","SPAC17C9.01c","SPAC6F12.15c","SPBC1A4.01","SPBC14C8.01c","SPBC106.09","SPAC17A2.13c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2016-08-22"},{"uniquename":"PMID:26150232","title":"Pom1 gradient buffering through intermolecular auto-phosphorylation.","citation":"Mol Syst Biol 2015 Jul 06;11(7):818","abstract":"Concentration gradients provide spatial information for tissue patterning and cell organization, and their robustness under natural fluctuations is an evolutionary advantage. In rod-shaped Schizosaccharomyces pombe cells, the DYRK-family kinase Pom1 gradients control cell division timing and placement. Upon dephosphorylation by a Tea4-phosphatase complex, Pom1 associates with the plasma membrane at cell poles, where it diffuses and detaches upon auto-phosphorylation. Here, we demonstrate that Pom1 auto-phosphorylates intermolecularly, both in vitro and in vivo, which confers robustness to the gradient. Quantitative imaging reveals this robustness through two system's properties: The Pom1 gradient amplitude is inversely correlated with its decay length and is buffered against fluctuations in Tea4 levels. A theoretical model of Pom1 gradient formation through intermolecular auto-phosphorylation predicts both properties qualitatively and quantitatively. This provides a telling example where gradient robustness through super-linear decay, a principle hypothesized a decade ago, is achieved through autocatalysis. Concentration-dependent autocatalysis may be a widely used simple feedback to buffer biological activities.","doi":"10.15252/msb.20145996","authors":"Hersch M, Hachet O, Dalessi S, Ullal P, Bhatia P, Bergmann S, Martin SG","authors_abbrev":"Hersch M et al.","pubmed_publication_date":"06 Jul 2015","pubmed_entrez_date":"2015-07-08","publication_year":"2015","canto_session_key":"e223a3074a0b59fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_approved_date":"2017-05-01 18:08:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-29 15:29:13","canto_added_date":"2015-07-09 00:21:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2F7.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-29"},{"uniquename":"PMID:15728720","title":"Dissociation of the Nuf2-Ndc80 complex releases centromeres from the spindle-pole body during meiotic prophase in fission yeast.","citation":"Mol Biol Cell 2005 May;16(5):2325-38","abstract":"In the fission yeast Schizosaccharomyces pombe, centromeres remain clustered at the spindle-pole body (SPB) during mitotic interphase. In contrast, during meiotic prophase centromeres dissociate from the SPB. Here we examined the behavior of centromere proteins in living meiotic cells of S. pombe. We show that the Nuf2-Ndc80 complex proteins (Nuf2, Ndc80, Spc24, and Spc25) disappear from the centromere in meiotic prophase when the centromeres are separated from the SPB. The centromere protein Mis12 also dissociates during meiotic prophase; however, Mis6 remains throughout meiosis. When cells are induced to meiosis by inactivation of Pat1 kinase (a key negative regulator of meiosis), centromeres remain associated with the SPB during meiotic prophase. However, inactivation of Nuf2 by a mutation causes the release of centromeres from the SPB in pat1 mutant cells, suggesting that the Nuf2-Ndc80 complex connects centromeres to the SPB. We further found that removal of the Nuf2-Ndc80 complex from the centromere and centromere-SPB dissociation are caused by mating pheromone signaling. Because pat1 mutant cells also show aberrant chromosome segregation in the first meiotic division and this aberration is compensated by mating pheromone signaling, dissociation of the Nuf2-Ndc80 complex may be associated with remodeling of the kinetochore for meiotic chromosome segregation.","authors":"Asakawa H, Hayashi A, Haraguchi T, Hiraoka Y","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"May 2005","pubmed_entrez_date":"2005-02-25","publication_year":"2005","canto_session_key":"650057099746f1a6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-05-26 16:36:19","canto_approved_date":"2022-10-05 16:53:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-22 16:33:53","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.08","SPAC1687.20c","SPAC27F1.04c","SPBC11C11.03","SPBC409.04c","SPCC188.04c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-05-26"},{"uniquename":"PMID:36739946","title":"Aim18p and Aim46p are chalcone isomerase domain-containing mitochondrial hemoproteins in Saccharomyces cerevisiae.","citation":"J Biol Chem 2023 Mar;299(3):102981","abstract":"Chalcone isomerases (CHIs) have well-established roles in the biosynthesis of plant flavonoid metabolites. Saccharomyces cerevisiae possesses two predicted CHI-like proteins, Aim18p (encoded by YHR198C) and Aim46p (YHR199C), but it lacks other enzymes of the flavonoid pathway, suggesting that Aim18p and Aim46p employ the CHI fold for distinct purposes. Here, we demonstrate using proteinase K protection assays, sodium carbonate extractions, and crystallography that Aim18p and Aim46p reside on the mitochondrial inner membrane and adopt CHI folds, but they lack select active site residues and possess an extra fungal-specific loop. Consistent with these differences, Aim18p and Aim46p lack CHI activity and also the fatty acid-binding capabilities of other CHI-like proteins, but instead bind heme. We further show that diverse fungal homologs also bind heme and that Aim18p and Aim46p possess structural homology to a bacterial hemoprotein. Collectively, our work reveals a distinct function and cellular localization for two CHI-like proteins, introduces a new variation of a hemoprotein fold, and suggests that ancestral CHI-like proteins were hemoproteins.","doi":"10.1016/j.jbc.2023.102981","authors":"Schmitz JM, Wolters JF, Murray NH, Guerra RM, Bingman CA, Hittinger CT, Pagliarini DJ","authors_abbrev":"Schmitz JM et al.","pubmed_publication_date":"Mar 2023","pubmed_entrez_date":"2023-02-05","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18G6.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SP22371","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12065422","title":"Schizosaccharomyces pombe NIMA-related kinase, Fin1, regulates spindle formation and an affinity of Polo for the SPB.","citation":"EMBO J 2002 Jun 17;21(12):3096-107","abstract":"The Aspergillus nidulans protein kinase NIMA regulates mitotic commitment, while the human and Xenopus equivalents influence centrosome function. Two recessive, temperature-sensitive mutations in the Schizosaccharomyces pombe NIMA homologue, Fin1, blocked spindle formation at 37 degrees C. One of the two spindle pole bodies (SPBs) failed to nucleate microtubules. This phenotype was reduced by accelerating mitotic commitment through genetic inhibition of Wee1 or activation of either Cdc25 or Cdc2. Polo kinase (Plo1) normally associates with the SPB of mitotic, but not interphase cells. cut12.s11 is a dominant mutation in an SPB component that both suppresses cdc25 mutants and promotes Plo1 association with the interphase SPB. Both cut12.s11 phenotypes were abolished by removing Fin1 function. Elevating Fin1 levels promoted Plo1 recruitment to the interphase SPB of wild-type cells and reduced the severity of the cdc25.22 phenotype. These data are consistent with Fin1 regulating Plo1 function during mitotic commitment. The fin1 mitotic commitment and spindle phenotypes resemble distinct nimA phenotypes in different systems and suggest that the function of this family of kinases may be conserved across species.","authors":"Grallert A, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"17 Jun 2002","pubmed_entrez_date":"2002-06-18","publication_year":"2002","canto_session_key":"50345fb1226215ae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-26 21:15:44","canto_approved_date":"2022-03-23 18:20:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-26 21:14:28","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC19E9.02","SPBC106.01","SPAC23C11.16","SPBC649.05","SPCC1322.12c","SPCC18B5.03","SPAC24H6.05","SPBC20F10.06"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2020-12-26"},{"uniquename":"PMID:25319670","title":"Mutations in the proteolipid subunits of the vacuolar H+-ATPase provide resistance to indolotryptoline natural products.","citation":"Biochemistry 2014 Nov 18;53(45):7123-31","abstract":"Indolotryptoline natural products represent a small family of structurally unique chromopyrrolic acid-derived antiproliferative agents. Like many prospective anticancer agents before them, the exploration of their potential clinical utility has been hindered by the limited information known about their mechanism of action. To study the mode of action of two closely related indolotryptolines (BE-54017, cladoniamide A), we selected for drug resistant mutants using a multidrug resistance-suppressed (MDR-sup) Schizosaccharomyces pombe strain. As fission yeast maintains many of the basic cancer-relevant cellular processes present in human cells, it represents an appealing model to use in determining the potential molecular target of antiproliferative natural products through resistant mutant screening. Full genome sequencing of resistant mutants identified mutations in the c and c' subunits of the proteolipid substructure of the vacuolar H(+)-ATPase complex (V-ATPase). This collection of resistance-conferring mutations maps to a site that is distant from the nucleotide-binding sites of V-ATPase and distinct from sites found to confer resistance to known V-ATPase inhibitors. Acid vacuole staining, cross-resistance studies, and direct c/c' subunit mutagenesis all suggest that indolotryptolines are likely a structurally novel class of V-ATPase inhibitors. This work demonstrates the general utility of resistant mutant selection using MDR-sup S. pombe as a rapid and potentially systematic approach for studying the modes of action of cytotoxic natural products.","doi":"10.1021/bi501078j","authors":"Chang FY, Kawashima SA, Brady SF","authors_abbrev":"Chang FY et al.","pubmed_publication_date":"18 Nov 2014","pubmed_entrez_date":"2014-10-17","publication_year":"2014","canto_session_key":"1e068433e48dccc0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-10-18 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19066022","title":"In vivo labeling and analysis of mitochondrial translation products in budding and in fission yeasts.","citation":"Methods Mol Biol 2008;457:113-24","abstract":"Mitochondrial biogenesis requires the contribution of two genomes and of two compartmentalized protein synthesis systems (nuclear and mitochondrial). Mitochondrial protein synthesis is unique on many respects, including the use of a genetic code with deviations from the universal code, the use of a restricted number of transfer RNAs, and because of the large number of nuclear encoded factors involved in assembly of the mitochondrial biosynthetic apparatus. The mitochondrial biosynthetic apparatus is involved in the actual synthesis of a handful of proteins encoded in the mitochondrial DNA. The budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe are excellent models to identify and study factors required for mitochondrial translation. For that purpose, in vivo mitochondrial protein synthesis, following the incorporation of a radiolabeled precursor into the newly synthesized mitochondrial encoded products, is a relatively simple technique that has been extensively used. Although variations of this technique are well established for studies in S. cerevisiae, they have not been optimized yet for studies in S. pombe. In this chapter, we present an easy, fast and reliable method to in vivo radiolabel mitochondrial translation products from this fission yeast.","authors":"Gouget K, Verde F, Barrientos A","authors_abbrev":"Gouget K et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-12-11","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26257282","title":"Interaction between TBP and Condensin Drives the Organization and Faithful Segregation of Mitotic Chromosomes.","citation":"Mol Cell 2015 Sep 03;59(5):755-67","abstract":"Genome/chromosome organization is highly ordered and controls various nuclear events, although the molecular mechanisms underlying the functional organization remain largely unknown. Here, we show that the TATA box-binding protein (TBP) interacts with the Cnd2 kleisin subunit of condensin to mediate interphase and mitotic chromosomal organization in fission yeast. TBP recruits condensin onto RNA polymerase III-transcribed (Pol III) genes and highly transcribed Pol II genes; condensin in turn associates these genes with centromeres. Inhibition of the Cnd2-TBP interaction disrupts condensin localization across the genome and the proper assembly of mitotic chromosomes, leading to severe defects in chromosome segregation and eventually causing cellular lethality. We propose that the Cnd2-TBP interaction coordinates transcription with chromosomal architecture by linking dispersed gene loci with centromeres. This chromosome arrangement can contribute to the efficient transmission of physical force at the kinetochore to chromosomal arms, thereby supporting the fidelity of chromosome segregation.","doi":"10.1016/j.molcel.2015.07.007","authors":"Iwasaki O, Tanizawa H, Kim KD, Yokoyama Y, Corcoran CJ, Tanaka A, Skordalakes E, Showe LC, Noma K","authors_abbrev":"Iwasaki O et al.","pubmed_publication_date":"03 Sep 2015","pubmed_entrez_date":"2015-08-11","publication_year":"2015","canto_session_key":"6db3af07ba32218b","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-08-12 00:19:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.07","SPCC1919.14c","SPAC6F12.11c","SPBP4H10.06c","SPAC29E6.08","SPBC13E7.10c","SPCC16C4.14c","SPBC8D2.07c","SPBC21H7.05","SPCC188.03","SPAC1250.07","SPCC306.03c","SPBC146.03c","SPBC776.13"],"gene_count":14,"ltp_gene_count":14},{"uniquename":"PMID:15611161","title":"In vivo activation of protein kinase A in Schizosaccharomyces pombe requires threonine phosphorylation at its activation loop and is dependent on PDK1.","citation":"Genetics 2004 Dec;168(4):1843-53","abstract":"Phosphoinositide-dependent protein kinase 1 (PDK1) plays a central role in cellular signaling by phosphorylating members of the AGC family of kinases. This family includes protein kinase C (PKC), protein kinase B (PKB), p70/p90 ribosomal S6 kinases (RSK and S6K), and the catalytic subunit of cAMP-dependent protein kinase (PKA). Although PDK1 phosphorylates and activates PKC, PKB, and RSK in vivo, PDK1 regulation of PKA remains controversial. We isolated ksg1, the fission yeast ortholog of mammalian PDK1, as a suppressor of growth defects caused by loss of the stress-activated MAP kinase, Spc1. Here, we demonstrate that Ksg1 is required for activation of PKA. Cells containing the ksg1.12 thermolabile allele exhibit pleiotropic phenotypes, including the failure to arrest in G(1) and an inability to conjugate. The ksg1.12 allele strongly suppresses defects associated with unregulated PKA. Pka1, the catalytic subunit of cAMP-dependent protein kinase, is phosphorylated in vivo at Thr-356, which is located in the activation loop of the kinase and corresponds to Thr-197 in mammalian PKA. Phosphorylation of Thr-356 is required for in vivo activation of Pka1 and is dependent upon Ksg1. These data provide experimental evidence that PKA is a physiological substrate for PDK1.","authors":"Tang Y, McLeod M","authors_abbrev":"Tang Y et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-12-22","publication_year":"2004","canto_session_key":"1e46c55523f49c2a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-03-06 16:15:32","canto_approved_date":"2026-03-06 16:15:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-03-06 16:15:19","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.03","SPBC106.10","SPAC24B11.06c","SPCC576.15c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2026-03-06"},{"uniquename":"PMID:15576924","title":"Cell cycle molecules and mechanisms of the budding and fission yeasts.","citation":"Methods Mol Biol 2005;296:3-29","abstract":"The cell cycles of the budding yeast Saccharomyces cerevisiae and the fission yeast, Schizosaccharomyces pombe are currently the best understood of all eukaryotes. Studies in these two evolutionarily divergent organisms have identified common control mechanisms, which have provided paradigms for our understanding of the eukaryotic cell cycle. This chapter provides an overview of our current knowledge of the molecules and mechanisms that regulate the mitotic cell cycle in these two yeasts.","authors":"Humphrey T, Pearce A","authors_abbrev":"Humphrey T et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2004-12-04","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26404184","title":"High Confidence Fission Yeast SUMO Conjugates Identified by Tandem Denaturing Affinity Purification.","citation":"Sci Rep 2015 Sep 25;5:14389","abstract":"Covalent attachment of the small ubiquitin-like modifier (SUMO) to key targets in the proteome critically regulates the evolutionarily conserved processes of cell cycle control, transcription, DNA replication and maintenance of genome stability. The proteome-wide identification of SUMO conjugates in budding yeast has been invaluable in helping to define roles of SUMO in these processes. Like budding yeast, fission yeast is an important and popular model organism; however, the fission yeast Schizosaccharomyces pombe community currently lacks proteome-wide knowledge of SUMO pathway targets. To begin to address this deficiency, we adapted and used a highly stringent Tandem Denaturing Affinity Purification (TDAP) method, coupled with mass spectrometry, to identify fission yeast SUMO conjugates. Comparison of our data with that compiled in budding yeast reveals conservation of SUMO target enrichment in nuclear and chromatin-associated processes. Moreover, the SUMO \"cloud\" phenomenon, whereby multiple components of a single protein complex are SUMOylated, is also conserved. Overall, SUMO TDAP provides both a key resource of high confidence SUMO-modified target proteins in fission yeast, and a robust method for future analyses of SUMO function.","doi":"10.1038/srep14389","authors":"Nie M, Vashisht AA, Wohlschlegel JA, Boddy MN","authors_abbrev":"Nie M et al.","pubmed_publication_date":"25 Sep 2015","pubmed_entrez_date":"2015-09-26","publication_year":"2015","canto_session_key":"67c974d598eb5a92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Minghua Nie","canto_approved_date":"2015-12-07 16:37:04","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-18 00:08:11","canto_added_date":"2015-09-27 00:18:29","annotation_curators":[{"name":"Minghua Nie","community_curator":true,"annotation_count":166,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1815.01","SPAC22E12.19","SPAC521.05","SPBC32F12.11","SPCC1393.08","SPBC83.15","SPCP31B10.07","SPCC417.08","SPBC19C7.10","SPBC1604.05","SPAPB1E7.12","SPAC17H9.13c","SPAC3H5.08c","SPCC306.04c","SPBC1703.14c","SPBC21H7.02","SPBC2G5.05","SPAC1687.09","SPBC19F8.08","SPCC330.13","SPBC365.10","SPCC622.09","SPAC186.02c","SPAC25G10.08","SPAC30D11.13","SPAC631.02","SPAC959.03c","SPCC16C4.09","SPAC23A1.11","SPBPJ4664.04","SPAC6B12.05c","SPAC2E12.02","SPCC1919.14c","SPCC31H12.04c","SPBC29B5.01","SPAPB17E12.14c","SPAC1071.10c","SPAC15A10.02","SPBC1604.09c","SPBC2D10.10c","SPBC28F2.10c","SPBC1685.08","SPBC1734.01c","SPBC1347.02","SPAC23G3.09","SPCC594.05c","SPAC17G6.10","SPBC685.07c","SPAC19G12.10c","SPAC6F6.03c","SPAC1783.05","SPCC13B11.01","SPAC11E3.01c","SPBP4H10.15","SPAC926.04c","SPAC2F7.07c","SPAC26F1.06","SPCC1223.01","SPBC317.01","SPBP8B7.20c","SPAC23G3.06","SPCC320.10","SPBP8B7.16c","SPBP23A10.13","SPAC9E9.09c","SPBC1734.15","SPBC8D2.18c","SPBC1861.02","SPAC17A5.14","SPCC1183.08c","SPBC4B4.03","SPAC18B11.10","SPBC13E7.08c","SPBC36.05c","SPCC970.10c","SPBC31E1.06","SPCC1739.13","SPBC1A4.03c","SPBC119.10","SPBC13E7.10c","SPAC4C5.04","SPBC29A3.04","SPBC18H10.03","SPBC16H5.03c","SPAC23G3.01","SPBC651.01c","SPAC7D4.14c","SPBC839.05c","SPBC23E6.09","SPAC17C9.03","SPAC630.14c","SPBC1709.02c","SPAC6G9.09c","SPCC70.05c","SPCC1259.01c","SPBC1709.05","SPCC1620.09c","SPBC428.07","SPAC12G12.05c","SPAC8C9.14","SPAC9G1.13c","SPBC1711.06","SPBP22H7.02c","SPCC1494.06c","SPCC1672.02c","SPAC1250.01","SPCC18B5.01c","SPBC14F5.04c","SPBC106.18","SPBP8B7.19","SPAC13G7.02c","SPAC1486.04c","SPCC1183.07","SPBC12D12.05c","SPBC365.06","SPBC28F2.11","SPAC25G10.07c","SPAC890.08","SPCC1223.05c","SPAC4H3.10c","SPBC577.15c","SPAC17G6.16c","SPAC343.11c","SPBC32H8.12c","SPAC5H10.06c","SPBC1921.02","SPBC354.05c","SPBC1A4.02c","SPAC806.03c","SPBC1778.01c","SPCC191.07","SPBC8D2.06","SPAC1F8.07c","SPBP8B7.03c","SPCC613.01","SPAC1805.13","SPAC22G7.05","SPBC106.04","SPCC63.14","SPCC830.03","SPAC110.04c","SPBC1289.10c","SPAC31G5.03","SPAC2F7.03c","SPCC74.05","SPAC4D7.10c","SPAC589.10c","SPAC16E8.01","SPCC24B10.19c","SPAC26A3.07c","SPBC19C2.07","SPAC29B12.01","SPBC21B10.10","SPAC2E1P5.05","SPAC15A10.15","SPBC17D11.01","SPBP4H10.06c","SPBC577.08c","SPCC162.08c","SPAC25G10.01","SPAC56F8.03","SPBC19G7.16","SPAC2G11.14","SPBC28E12.05","SPAC17H9.04c","SPAC23C4.19"],"gene_count":166,"ltp_gene_count":166,"approved_date":"2015-11-18"},{"uniquename":"PMID:26310293","title":"Defects in tRNA Anticodon Loop 2'-O-Methylation Are Implicated in Nonsyndromic X-Linked Intellectual Disability due to Mutations in FTSJ1.","citation":"Hum Mutat 2015 Dec;36(12):1176-87","abstract":"tRNA modifications are crucial for efficient and accurate protein synthesis, and modification defects are frequently associated with disease. Yeast trm7Δ mutants grow poorly due to lack of 2'-O-methylated C32 (Cm32 ) and Gm34 on tRNA(Phe) , catalyzed by Trm7-Trm732 and Trm7-Trm734, respectively, which in turn results in loss of wybutosine at G37 . Mutations in human FTSJ1, the likely TRM7 homolog, cause nonsyndromic X-linked intellectual disability (NSXLID), but the role of FTSJ1 in tRNA modification is unknown. Here, we report that tRNA(Phe) from two genetically independent cell lines of NSXLID patients with loss-of-function FTSJ1 mutations nearly completely lacks Cm32 and Gm34 , and has reduced peroxywybutosine (o2yW37 ). Additionally, tRNA(Phe) from an NSXLID patient with a novel FTSJ1-p.A26P missense allele specifically lacks Gm34 , but has normal levels of Cm32 and o2yW37 . tRNA(Phe) from the corresponding Saccharomyces cerevisiae trm7-A26P mutant also specifically lacks Gm34 , and the reduced Gm34 is not due to weaker Trm734 binding. These results directly link defective 2'-O-methylation of the tRNA anticodon loop to FTSJ1 mutations, suggest that the modification defects cause NSXLID, and may implicate Gm34 of tRNA(Phe) as the critical modification. These results also underscore the widespread conservation of the circuitry for Trm7-dependent anticodon loop modification of eukaryotic tRNA(Phe) .","doi":"10.1002/humu.22897","authors":"Guy MP, Shaw M, Weiner CL, Hobson L, Stark Z, Rose K, Kalscheuer VM, Gecz J, Phizicky EM","authors_abbrev":"Guy MP et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2015-08-28","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU006769","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29784772","title":"A Heterochromatin Domain Forms Gradually at a New Telomere and Is Dynamic at Stable Telomeres.","citation":"Mol Cell Biol 2018 Aug 01;38(15)","abstract":"Heterochromatin domains play important roles in chromosome biology, organismal development, and aging, including centromere function, mammalian female X chromosome inactivation, and senescence-associated heterochromatin foci. In the fission yeast  Schizosaccharomyces pombe  and metazoans, heterochromatin contains histone H3 that is dimethylated at lysine 9. While factors required for heterochromatin have been identified, the dynamics of heterochromatin formation are poorly understood. Telomeres convert adjacent chromatin into heterochromatin. To form a new heterochromatic region in  S. pombe , an inducible DNA double-strand break (DSB) was engineered next to 48 bp of telomere repeats in euchromatin, which caused formation of a new telomere and the establishment and gradual spreading of a new heterochromatin domain. However, spreading was dynamic even after the telomere had reached its stable length, with reporter genes within the heterochromatin domain showing variegated expression. The system also revealed the presence of repeats located near the boundaries of euchromatin and heterochromatin that are oriented to allow the efficient healing of a euchromatic DSB to cap the chromosome end with a new telomere. Telomere formation in  S. pombe  therefore reveals novel aspects of heterochromatin dynamics and fail-safe mechanisms to repair subtelomeric breaks, with implications for similar processes in metazoan genomes.","doi":"10.1128/MCB.00393-17","authors":"Wang J, Eisenstatt JR, Audry J, Cornelius K, Shaughnessy M, Berkner KL, Runge KW","authors_abbrev":"Wang J et al.","pubmed_publication_date":"01 Aug 2018","pubmed_entrez_date":"2018-05-23","publication_year":"2018","canto_session_key":"d5cba0d1f38e5106","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-06-01 12:20:54","canto_approved_date":"2022-11-10 17:39:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-30 08:07:23","canto_added_date":"2018-05-24 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPCC330.05c","SPNCRNA.214","SPCC1322.13","SPBC428.08c"],"gene_count":5,"ltp_gene_count":0,"approved_date":"2018-06-01"},{"uniquename":"PMID:14655046","title":"Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fission yeast.","citation":"Mol Genet Genomics 2004 Jan;270(6):449-61","abstract":"In interphase cells of fission yeast, the spindle pole body (SPB) is thought to be connected with chromosomal centromeres by an as yet unknown mechanism that spans the nuclear membrane. To elucidate this mechanism, we performed two-hybrid screens for proteins that interact with Kms1 and Sad1, which are constitutive membrane-bound components of the SPB that interact with each other. Seven and 26 genes were identified whose products potentially interact with Kms1 and Sad1, respectively. With the exception of Dlc1 (a homolog of the 14-kDa dynein light chain), all of the Kms1 interactors also interacted with Sad1. Among the genes identified were the previously known genes rhp9+ / crb2+, cut6+, ags1+ / mok1+, gst3+, kms2+, and sid4+. The products of kms2+ and sid4+ localize to the SPB. The novel genes were characterized by constructing disruption mutations and by localization of the gene products. Two of them, putative homologues of budding yeast UFE1 (which encodes a t-SNARE) and SFH1 (an essential component of a chromatin-remodeling complex), were essential for viability. Two further genes, which were only conditionally essential, genetically interact with sad1+. One of these was named sif1+ (for Sad1-interacting factor) and is required for proper septum formation at high temperature. Cells in which this gene was overexpressed displayed a wee -like phenotype. The product of the other gene, apm1+, is very similar to the medium chain of an adaptor protein complex in clathrin-coated vesicles. Apm1 appears to be required for SPB separation and spindle formation, and tended to accumulate at the SPB when it was overproduced. It was functionally distinct from its homologues Apm2 and Apm4. Other novel genes identified in this study included one for a nucleoporin and genes encoding novel membrane-bound proteins that were genetically related to Sad1. We found that none of the newly identified genes tested were necessary for centromere/telomere clustering.","authors":"Miki F, Kurabayashi A, Tange Y, Okazaki K, Shimanuki M, Niwa O","authors_abbrev":"Miki F et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2003-12-05","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12D12.01","SPAC1805.08","SPBC342.05","SPBC3H7.13","SPAC12G12.15","SPAC17H9.05","SPAC19E9.01c","SPAC688.04c","SPBC1A4.05","SPBP16F5.07","SPBC244.01c","SPCC16C4.01","SPCC16A11.14","SPBC947.12","SPCP1E11.04c","SPAC3A11.05c","SPCC417.05c","SPAC17A2.14","SPBC16A3.08c","SPAC14C4.05c","SPCC895.04c","SPAC12G12.11c","SPBC29A3.16","SPAC222.14c","SPCC1235.06","SPAC3A12.13c","SPAC56E4.04c"],"gene_count":27,"ltp_gene_count":27},{"uniquename":"PMID:3910104","title":"Primary structures of ribosomal protein YS25 from Saccharomyces cerevisiae and its counterparts from Schizosaccharomyces pombe and rat liver.","citation":"Biochemistry 1985 Dec 03;24(25):7418-23","abstract":"Protein YS25 and its counterparts, SP-S28 and rat S21 [nomenclature according to Sherton, C. C., & Wool, I. G. (1972) J. Biol. Chem. 247, 4460-4467], from Saccharomyces cerevisiae, Schizosaccharomyces pombe, and rat liver cytoplasmic ribosomes, respectively, were sequenced by a combination of various enzymatic digestions and/or chemical cleavage. Proteins YS25 and SP-S28 consist of 87 amino acid residues, and rat S21 consists of 83. The amino termini are all N alpha-acetylated. The amino-terminal halves of the protein molecules are highly conserved (73-85% homologies) in contrast to the carboxy-terminal parts. Overall, rat S21 is 54% homologous to YS25 and 57% to SP-S28, despite a 76% homology between YS25 and SP-S28. Direct comparison with the available prokaryotic ribosomal protein sequences did not reveal any significant homology.","authors":"Itoh T, Otaka E, Matsui KA","authors_abbrev":"Itoh T et al.","pubmed_publication_date":"03 Dec 1985","pubmed_entrez_date":"1985-12-03","publication_year":"1985","canto_session_key":"069aad3a8520280d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-08-16 10:07:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-13 15:59:03","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC18E5.06","SPAC25G10.06","SPCC285.15c"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2013-08-13"},{"uniquename":"PMID:12244050","title":"Ctr6, a vacuolar membrane copper transporter in Schizosaccharomyces pombe.","citation":"J Biol Chem 2002 Nov 29;277(48):46676-86","abstract":"Aerobic organisms possess efficient systems for the transport of copper. This involves transporters that mediate the passage of copper across biological membranes to reach essential intracellular copper-requiring enzymes. In this report, we identify a new copper transporter in Schizosaccharomyces pombe, encoded by the ctr6(+) gene. The transcription of ctr6(+) is induced under copper-limiting conditions. This regulation is mediated by the cis-acting promoter element CuSE (copper-signaling element) through the copper-sensing transcription factor Cuf1. An S. pombe strain bearing a disrupted ctr6Delta allele displays a strong reduction of copper,zinc superoxide dismutase activity. When the ctr6+ gene is overexpressed from the thiamine-inducible nmt1(+) promoter, the cells are unable to grow on medium containing exogenous copper. Surprisingly, this copper-sensitive growth phenotype is not due to an increase of copper uptake at the cell surface. Instead, copper delivery across the plasma membrane is reduced. Consistently, this results in repressing ctr4(+) gene expression. By using a functional ctr6(+) epitope-tagged allele expressed under the control of its own promoter, we localize the Ctr6 protein on the membrane of vacuoles. Furthermore, we demonstrate that Ctr6 is an integral membrane protein that can trimerize. Moreover, we show that Ctr6 harbors a putative copper-binding Met-X-His-Cys-X-Met-X-Met motif in the amino terminus, which is essential for its function. Our findings suggest that under conditions in which copper is scarce, Ctr6 is required as a means to mobilize stored copper from the vacuole to the cytosol.","authors":"Bellemare DR, Shaner L, Morano KA, Beaudoin J, Langlois R, Labbe S","authors_abbrev":"Bellemare DR et al.","pubmed_publication_date":"29 Nov 2002","pubmed_entrez_date":"2002-09-24","publication_year":"2002","canto_session_key":"f33943b5f7a15c44","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-07-06 10:53:24","canto_approved_date":"2020-01-16 11:09:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-04-30 08:54:59","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1393.10","SPBC23G7.16","SPAC31A2.11c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-07-06"},{"uniquename":"GO_REF:0000003","title":"Gene Ontology annotation based on Enzyme Commission mapping","abstract":"Transitive assignment using Enzyme Commission identifiers. This method is used for any database entry, such as a protein record in UniProtKB or TrEMBL, that has had an Enzyme Commission number assigned. The corresponding GO term is determined using the EC cross-references in the GO molecular function ontology. Also see Hill et al., Genomics (2001) 74:121-128. The mapping file is available at http://www.geneontology.org/external2go/ec2go.","authors":"GOA curators, MGI curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9.04","SPCC1494.11c","SPAC19D5.09c","SPAC23A1.06c","SPAC16.04","SPAC13D1.01c","SPAC26A3.13c","SPAC2E1P3.03c","SPAC1486.02c","SPCC1020.14","SPBC646.03","SPBC19C2.01","SPAC167.08","SPBPB2B2.11","SPBC9B6.02c","SPAC922.03","SPBC1685.06","SPAC19A8.10","SPCC1183.03c","SPAC22G7.06c","SPBC1198.07c","SPBC1E8.04","SPBC1198.06c","SPAC4A8.11c","SPAC56E4.03","SPBC1289.17","SPBC18H10.08c","SPCC1494.05c","SPCC970.02","SPAC16C9.06c","SPAC22F3.06c","SPCC16A11.12c","SPAPB15E9.03c","SPAC27E2.08"],"gene_count":34,"ltp_gene_count":0},{"uniquename":"PMID:6079736","title":"A second linkage groups and the possibility of mitotic recombination in Schizosaccharomyces pombe.","citation":"Can J Genet Cytol 1967 Sep;9(3):473-81","abstract":"","authors":"Ali AM","authors_abbrev":"Ali AM","pubmed_publication_date":"Sep 1967","pubmed_entrez_date":"1967-09-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8782411","title":"Isolation and characterization of a glycosylation mutant from Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 1996 Jul;60(7):1156-9","abstract":"N-Linked oligosaccharides were elongated by glycosylation with mannose and galactose residues in the secretory pathway of Schizosaccharomyces pombe. The wild-type S. pombe cells were agglutinated by the additions of not only concanavalin A lectin, which is specific for mannose residues, but also PNA (from Arachis hypogaea) and RCA (Ricinus communis) lectins, which are specific for terminal galactose residues. By PNA-binding selection, we isolated an S. pombe mutant defective in protein glycosylation. The mutant cells, named gms1, were not agglutinated by PNA or RCA. In contrast, agglutination of the gms1 cells by the addition of concanavalin A was markedly increased. Structural studies on N-linked oligosaccharides from gms1 mutant cells showed that the number of alpha-1,2-linked galactose residues wes markedly reduced, and unsubstituted alpha-1,6-linked polymannose outer chains were attached to the core oligosaccharides.","authors":"Takegawa K, Tanaka N, Tabuchi M, Iwahara S","authors_abbrev":"Takegawa K et al.","pubmed_publication_date":"Jul 1996","pubmed_entrez_date":"1996-07-01","publication_year":"1996","canto_session_key":"cf93d3de33fd0ddf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-07 08:16:33","canto_approved_date":"2023-03-15 17:35:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-03-08 22:28:08","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-07"},{"uniquename":"PMID:9115430","title":"Chromatin proteins involved in the initiation of DNA replication.","citation":"Curr Opin Genet Dev 1997 Apr;7(2):152-7","abstract":"Eukaryotic DNA replication is regulated at least in part by the assembly of initiation proteins onto origins of replication. The origin recognition complex (ORC) is bound to origins throughout most of the cell cycle. Other initiation proteins, such as Cdc6 and the MCM/P1 proteins, are assembled onto ORC-containing chromatin during G1 to define a prereplicative complex. During S phase, these proteins are displaced from chromatin and their reassembly is inhibited by protein-dependent kinases.","authors":"Rowles A, Blow JJ","authors_abbrev":"Rowles A et al.","pubmed_publication_date":"Apr 1997","pubmed_entrez_date":"1997-04-01","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012795","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR014886","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G6.17","HGNC:24912"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19799180","title":"Gel electrophoresis assays for analyzing DNA double-strand breaks in Saccharomyces cerevisiae at various spatial resolutions.","citation":"Methods Mol Biol 2009;557:117-42","abstract":"Meiotic recombination is triggered by programmed DNA double-strand breaks (DSBs), which are catalyzed by Spo11 protein in a type II topoisomerase-like manner. Meiotic DSBs can be detected directly using physical assays (gel electrophoresis, Southern blotting, and indirect end-labeling) applied to samples of genomic DNA from sporulating cultures of budding and fission yeast. Such assays are extremely useful for quantifying and characterizing many aspects of the initiation of meiotic recombination, including the timing of DSB formation relative to other events, the distribution of DSBs across the genome, and the influence on DSB formation of mutations in recombination factors and other gene products. By varying the type of gel electrophoresis and other parameters, the spatial resolution of DSB analysis can range from single nucleotides up to whole yeast chromosomes.","doi":"10.1007/978-1-59745-527-5_9","authors":"Murakami H, Borde V, Nicolas A, Keeney S","authors_abbrev":"Murakami H et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-10-06","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1588907","title":"Molecular cloning and analysis of Schizosaccharomyces pombe rad9, a gene involved in DNA repair and mutagenesis.","citation":"Mol Gen Genet 1992 Apr;232(3):367-76","abstract":"The mutant allele rad9-192 renders Schizosaccharomyces pombe cells sensitive to ionizing radiation and UV light. We have isolated from a S. pombe genomic DNA library a unique recombinant plasmid that is capable of restoring wild-type levels of radioresistance to a rad9-192-containing cell population. Plasmid integration studies using the cloned DNA, coupled with mating and tetrad analyses, indicate that this isolated DNA contains the wild-type rad9 gene. We inactivated the repair function of the cloned fragment by a single insertion of the S. pombe ura4 gene. This nonfunctional fragment was used to create a viable disruption mutant, thus demonstrating that the rad9 gene does not encode an essential cellular function. In addition, the rad9-192 mutant population is as radiosensitive as the disruption mutant, indicating that rad9 gene function is severely if not totally inhibited by the molecular defect responsible for the rad9-192 phenotype. DNA sequence analysis of rad9 reveals an open reading frame of 1,278 bp, interrupted by three introns 53 bp, 57 bp, and 56 bp long, respectively, and ending in the termination codon TAG. This gene is capable of encoding a protein of 426 amino acids, with a corresponding calculated molecular weight of 47,464 daltons. No significant homology was detected between the rad9 gene or its deduced protein sequence and sequences previously entered into DNA and protein sequence data banks.","authors":"Lieberman HB, Hopkins KM, Laverty M, Chu HM","authors_abbrev":"Lieberman HB et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"671e6438a5ebc361","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-02-06 16:18:35","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-04-24 22:36:20","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-04-24"},{"uniquename":"PMID:21911358","title":"DNA-induced dimerization of the single-stranded DNA binding telomeric protein Pot1 from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2012 Jan;40(1):235-44","abstract":"Eukaryotic chromosome ends are protected from illicit DNA joining by protein-DNA complexes called telomeres. In most studied organisms, telomeric DNA is composed of multiple short G-rich repeats that end in a single-stranded tail that is protected by the protein POT1. Mammalian POT1 binds two telomeric repeats as a monomer in a sequence-specific manner, and discriminates against RNA of telomeric sequence. While addressing the RNA discrimination properties of SpPot1, the POT1 homolog in Schizosaccharomyces pombe, we found an unanticipated ssDNA-binding mode in which two SpPot1 molecules bind an oligonucleotide containing two telomeric repeats. DNA binding seems to be achieved via binding of the most N-terminal OB domain of each monomer to each telomeric repeat. The SpPot1 dimer may have evolved to accommodate the heterogeneous spacers that occur between S. pombe telomeric repeats, and it also has implications for telomere architecture. We further show that the S. pombe telomeric protein Tpz1, like its mammalian homolog TPP1, increases the affinity of Pot1 for telomeric single-stranded DNA and enhances the discrimination of Pot1 against RNA.","doi":"10.1093/nar/gkr721","authors":"Nandakumar J, Cech TR","authors_abbrev":"Nandakumar J et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2011-09-14","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26H5.06","SPAC6F6.16c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU008101","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8924996","title":"Genotoxicity testing in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 1996;53:343-53","abstract":"","authors":"McAthey P","authors_abbrev":"McAthey P","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26628015","title":"Characterization of Tamoxifen as an Antifungal Agent Using the Yeast Schizosaccharomyces Pombe Model Organism.","citation":"Kobe J Med Sci 2015 Oct 09;61(2):E54-63","abstract":"Tamoxifen, a selective estrogen receptor modulator used for managing breast cancer, is known to have antifungal activity. However, its molecular mechanism remains unknown. Using the fission yeast Schizosaccharomyces pombe as a model organism, we have explored the mechanism involved in antifungal action of tamoxifen. Since tamoxifen was shown to inhibit the binding of calmodulin to calcineurin in fungi, we first examined involvement of these molecules and found that overexpression of a catalytic subunit of calcineurin and its constitutively active mutant as well as calmodulin increases tamoxifen sensitivity. Since terbinafine and azoles inhibit enzymes for ergosterol biosynthesis, Erg1 and Erg11, for their antifungal actions, we also examined involvement of these molecules. Overexpression of Erg1 and Erg11 reduced the sensitivity to terbinafine and azoles, respectively, but increased tamoxifen sensitivity, suggesting that ergosterol biosynthesis is differently related to the action of tamoxifen and those of terbinafine and azoles. To elucidate molecules involved in tamoxifen action, we performed a genome-wide screen for altered sensitivity to tamoxifen using a fission yeast gene deletion library, and identified various hypersensitive and resistant mutants to this drug. Notably, these mutants are rarely overlapped with those identified in similar genetic screens with currently used antifungals, suggesting a novel mode of antifungal action. Furthermore, tamoxifen augmented antifungal actions of terbinafine and azoles, suggesting synergetic actions between these drugs. Therefore, our findings suggest that calmodulin-calcineurin pathway and ergosterol biosynthesis are related to antifungal action of tamoxifen, and propose novel targets for antifungal development as well as combined therapy with tamoxifen for fungal diseases.","authors":"Zhang X, Fang Y, Jaiseng W, Hu L, Lu Y, Ma Y, Furuyashiki T","authors_abbrev":"Zhang X et al.","pubmed_publication_date":"09 Oct 2015","pubmed_entrez_date":"2015-12-03","publication_year":"2015","canto_session_key":"eaab6d086b045989","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-02 16:12:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-02-02 16:12:30","canto_added_date":"2015-12-04 01:19:19","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":145,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_26628015_phaf.tsv"}],"genes":["SPCC1840.03","SPAC589.07c","SPAC29B12.11c","SPBC30D10.14","SPBC30B4.01c","SPAC4F8.01","SPAC3A12.10","SPAC328.10c","SPBP8B7.21","SPAC3A12.14","SPBP4H10.11c","SPBC6B1.06c","SPAC19G12.08","SPBC16C6.03c","SPAC1952.05","SPAC823.05c","SPBC2D10.06","SPAC227.01c","SPCC18B5.01c","SPAC19A8.05c","SPAC26A3.07c","SPACUNK4.12c","SPBC609.02","SPAC4G9.06c","SPBC11B10.07c","SPAC12G12.03","SPBC359.06","SPCC417.07c","SPBP4H10.04","SPAC30D11.07","SPAC144.11","SPBC409.20c","SPBC31F10.13c","SPBC365.14c","SPCC14G10.04","SPBC713.12","SPBC530.08","SPAC27E2.07","SPCC962.04","SPAC17G6.05c","SPBC19G7.04","SPAC343.18","SPBC16A3.16","SPAC17G6.06","SPAC17A2.06c","SPBC36.07","SPAC11D3.15","SPAC16A10.05c","SPBC609.04","SPAC13A11.02c","SPAC26A3.06","SPBC651.05c","SPBC19G7.03c","SPAC17C9.05c","SPBC609.03","SPAC19G12.02c","SPAC22F8.04","SPCC794.11c","SPAC57A7.08","SPBC16G5.02c","SPCC24B10.09","SPAC2H10.02c","SPBPB10D8.07c","SPAC1142.07c","SPBC530.05","SPAC4F10.04","SPCP1E11.04c","SPBC21B10.03c","SPCC1682.01","SPAC20G8.10c","SPBC29A10.16c","SPBC1709.09","SPAC9G1.12","SPBC31F10.02","SPAC3F10.17","SPCC31H12.05c","SPBC30B4.06c","SPAC25G10.06","SPBC1105.04c","SPAC824.09c","SPAC1D4.01","SPAC4G9.11c","SPBC23E6.08","SPBC1734.12c","SPBC3B8.03","SPBC660.11","SPAC6G9.15c","SPAC1B9.02c","SPAC9E9.14","SPCC162.10","SPAC3G9.05","SPBC25D12.05","SPCC4G3.04c","SPBC887.04c","SPCC830.06","SPAC1952.02","SPBC1604.08c","SPBC24C6.04","SPAC4A8.10","SPBC28F2.02","SPAP27G11.16","SPAPJ698.02c","SPAC23C11.02c","SPAC10F6.08c","SPBC14C8.17c","SPBC29A3.14c","SPCC162.11c","SPCC1235.13","SPAC57A10.14","SPAC823.16c","SPBC4F6.11c","SPBC106.07c","SPAP8A3.07c","SPBC29A3.02c","SPBC119.12","SPCC74.02c","SPAC664.04c","SPAC23C4.06c","SPBC18H10.11c","SPBC354.09c"],"gene_count":120,"ltp_gene_count":120,"approved_date":"2016-02-02"},{"uniquename":"PMID:25916707","title":"Incorporation of thymidine analogs for studying replication kinetics in fission yeast.","citation":"Methods Mol Biol 2015;1300:99-104","abstract":"Labeling DNA during in vivo replication by the incorporation of exogenous thymidine and thymidine analogs has been a mainstay of DNA replication and repair studies for decades. Unfortunately, thymidine labeling does not work in fungi, because they lack the thymidine salvage pathway required for uptake of exogenous thymidine. This obstacle to thymidine labeling has been overcome in yeast by engineering a minimal thymidine salvage pathway consisting of a nucleoside transporter to allow uptake of exogenous thymidine from the medium and a thymidine kinase to phosphorylate the thymidine into thymidine monophosphate, which can be used by the cell. This chapter describes the labeling of fission yeast, Schizosaccharomyces pombe, with the thymidine analog BrdU in order to identify sites and determine kinetics of DNA replication.","doi":"10.1007/978-1-4939-2596-4_6","authors":"Rhind N","authors_abbrev":"Rhind N","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-04-29","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-04-30 00:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2643117","title":"Construction of functional artificial minichromosomes in the fission yeast Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1989 Jan;86(2):577-81","abstract":"The centromere DNAs from chromosomes I and III of Schizosaccharomyces pombe have been cloned in an artificial chromosome vector in both budding and fission yeasts. In S. pombe, synthetic linear and circular minichromosomes containing an intact centromere are stable mitotically and behave as independent genetic linkage groups that segregate properly through meiosis. These experiments present a general strategy for the isolation of centromeres from other organisms.","authors":"Hahnenberger KM, Baum MP, Polizzi CM, Carbon J, Clarke L","authors_abbrev":"Hahnenberger KM et al.","pubmed_publication_date":"Jan 1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34446532","title":"Synthesis of modified nucleotide polymers by the poly(U) polymerase Cid1: application to direct RNA sequencing on nanopores.","citation":"RNA 2021 Dec;27(12):1497-1511","abstract":"Understanding transcriptomes requires documenting the structures, modifications, and abundances of RNAs as well as their proximity to other molecules. The methods that make this possible depend critically on enzymes (including mutant derivatives) that act on nucleic acids for capturing and sequencing RNA. We tested two 3' nucleotidyl transferases,  Saccharomyces cerevisiae  poly(A) polymerase and  Schizosaccharomyces pombe  Cid1, for the ability to add base and sugar modified rNTPs to free RNA 3' ends, eventually focusing on Cid1. Although unable to polymerize ΨTP or 1meΨTP, Cid1 can use 5meUTP and 4thioUTP. Surprisingly, Cid1 can use inosine triphosphate to add poly(I) to the 3' ends of a wide variety of RNA molecules. Most poly(A) mRNAs efficiently acquire a uniform tract of about 50 inosine residues from Cid1, whereas non-poly(A) RNAs acquire longer, more heterogeneous tails. Here we test these activities for use in direct RNA sequencing on nanopores, and find that Cid1-mediated poly(I)-tailing permits detection and quantification of both mRNAs and non-poly(A) RNAs simultaneously, as well as enabling the analysis of nascent RNAs associated with RNA polymerase II. Poly(I) produces a different current trace than poly(A), enabling recognition of native RNA 3' end sequence lost by in vitro poly(A) addition. Addition of poly(I) by Cid1 offers a broadly useful alternative to poly(A) capture for direct RNA sequencing on nanopores.","doi":"10.1261/rna.078898.121","authors":"Vo JM, Mulroney L, Quick-Cleveland J, Jain M, Akeson M, Ares M","authors_abbrev":"Vo JM et al.","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-08-27","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-08-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25736294","title":"Cell cycle control of spindle pole body duplication and splitting by Sfi1 and Cdc31 in fission yeast.","citation":"J Cell Sci 2015 Apr 15;128(8):1481-93","abstract":"Spindle pole biogenesis and segregation are tightly coordinated to produce a bipolar mitotic spindle. In yeasts, the spindle pole body (SPB) half-bridge composed of Sfi1 and Cdc31 duplicates to promote the biogenesis of a second SPB. Sfi1 accumulates at the half-bridge in two phases in Schizosaccharomyces pombe, from anaphase to early septation and throughout G2 phase. We found that the function of Sfi1-Cdc31 in SPB duplication is accomplished before septation ends and G2 accumulation starts. Thus, Sfi1 early accumulation at mitotic exit might correspond to half-bridge duplication. We further show that Cdc31 phosphorylation on serine 15 in a Cdk1 (encoded by cdc2) consensus site is required for the dissociation of a significant pool of Sfi1 from the bridge and timely segregation of SPBs at mitotic onset. This suggests that the Cdc31 N-terminus modulates the stability of Sfi1-Cdc31 arrays in fission yeast, and impacts on the timing of establishment of spindle bipolarity.","doi":"10.1242/jcs.159657","authors":"Bouhlel IB, Ohta M, Mayeux A, Bordes N, Dingli F, Boulanger J, Velve Casquillas G, Loew D, Tran PT, Sato M, Paoletti A","authors_abbrev":"Bouhlel IB et al.","pubmed_publication_date":"15 Apr 2015","pubmed_entrez_date":"2015-03-05","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-06 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17140794","title":"The cell-end factor pom1p inhibits mid1p in specification of the cell division plane in fission yeast.","citation":"Curr Biol 2006 Dec 19;16(24):2480-7","abstract":"Intrinsic spatial cues ensure the proper placement of the cell division plane. In the fission yeast Schizosaccharomyces pombe, the position of the nucleus helps to direct the medial positioning of contractile-ring assembly and subsequent cell division . An important factor in this process is mid1p (anillin-like protein), which is a peripheral-membrane protein that forms a broad cortical band of dots overlying the nucleus in interphase and recruits myosin in early mitosis . How mid1p localizes to this cortical band and tracks the nucleus is not clear, especially because its localization is independent of the cytoskeleton . Here, we used a combination of experimental and computational approaches to test mid1p localization mechanisms. We provide evidence that pom1p, a DYRK-family protein kinase that forms a concentration gradient emanating from the nongrowing cell end, inhibits mid1p. In pom1 mutants, mid1p is distributed over half of the cell, covering the nongrowing cell end. This abnormal distribution is established in a dynamic manner in interphase and leads to the formation of misplaced or multiple contractile rings. Our computational and experimental results support a model in which both positive cues from the medial nucleus and negative cues from the cell tips specify the position of the division plane.","authors":"Padte NN, Martin SG, Howard M, Chang F","authors_abbrev":"Padte NN et al.","pubmed_publication_date":"19 Dec 2006","pubmed_entrez_date":"2006-12-05","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27984725","title":"CDK Substrate Phosphorylation and Ordering the Cell Cycle.","citation":"Cell 2016 Dec 15;167(7):1750-1761.e16","abstract":"S phase and mitotic onset are brought about by the action of multiple different cyclin-CDK complexes. However, it has been suggested that changes in the total level of CDK kinase activity, rather than substrate specificity, drive the temporal ordering of S phase and mitosis. Here, we present a phosphoproteomics-based systems analysis of CDK substrates in fission yeast and demonstrate that the phosphorylation of different CDK substrates can be temporally ordered during the cell cycle by a single cyclin-CDK. This is achieved by rising CDK activity and the differential sensitivity of substrates to CDK activity over a wide dynamic range. This is combined with rapid phosphorylation turnover to generate clearly resolved substrate-specific activity thresholds, which in turn ensures the appropriate ordering of downstream cell-cycle events. Comparative analysis with wild-type cells expressing multiple cyclin-CDK complexes reveals how cyclin-substrate specificity works alongside activity thresholds to fine-tune the patterns of substrate phosphorylation.","doi":"10.1016/j.cell.2016.11.034","authors":"Swaffer MP, Jones AW, Flynn HR, Snijders AP, Nurse P","authors_abbrev":"Swaffer MP et al.","pubmed_publication_date":"15 Dec 2016","pubmed_entrez_date":"2016-12-17","publication_year":"2016","canto_session_key":"431ee93a3353689f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-07-11 16:50:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-11 16:50:10","canto_added_date":"2016-12-18 01:15:10","annotation_curators":[],"file_curator_name":"Matthew Swaffer","file_curator_role":"community","annotation_file_curators":[{"name":"Matthew Swaffer","community_curator":true,"annotation_count":335,"orcid":"0000-0002-8019-2887","file_type":"protein_modification","file_name":"PMID_27984725_modifications.tsv"}],"genes":["SPAC23G3.04","SPAC1F3.02c","SPAC22H10.11c","SPBC2G2.14","SPCP1E11.04c","SPBC4F6.06","SPBC1604.20c","SPBC19C7.10","SPAC23C4.18c","SPCC4G3.11","SPCC895.07","SPAC9G1.02","SPBC23G7.08c","SPAC24H6.09","SPAC1F5.04c","SPAC23D3.06c","SPAC12G12.03","SPCC645.06c","SPAC3G6.06c","SPBC609.01","SPAC23C11.16","SPAC29B12.07","SPAC1B2.03c","SPBC13E7.10c","SPBC216.01c","SPAC6F6.17","SPBC31F10.13c","SPBC1826.01c","SPAC7D4.14c","SPBC1706.01","SPCC1919.14c","SPAC5D6.07c","SPAC31A2.12","SPAC29A4.11","SPBPB7E8.02","SPCC1450.03","SPBC16A3.07c","SPAC16C9.05","SPBC6B1.02","SPAC15A10.16","SPCC23B6.04c","SPAC644.16","SPAC26A3.09c","SPBC16G5.15c","SPBC887.09c","SPBC17G9.08c","SPAC15A10.15","SPAC26A3.10","SPBC428.17c","SPBC1711.05","SPAC23A1.17","SPAC22F8.05","SPAC22E12.19","SPAC24H6.05","SPBC146.03c","SPBC14C8.19","SPAC20G8.05c","SPBC25D12.02c","SPBC428.10","SPBC4C3.12","SPCC1620.09c","SPBP8B7.26","SPBC336.15","SPBC27B12.04c","SPCC16C4.09","SPAC22F8.12c","SPBC2D10.04","SPAC23A1.06c","SPBC557.04","SPAC1782.09c","SPAC31A2.05c","SPCP1E11.11","SPBC13E7.03c","SPBC651.12c","SPCC1393.02c","SPAC57A10.05c","SPBC11B10.09","SPACUNK4.14","SPAC30D11.04c","SPAC3A11.06","SPBC947.12","SPBC29A10.15","SPBC365.07c","SPBC3H7.14","SPBC21B10.04c","SPAC18G6.10","SPBC6B1.04","SPBC12D12.01","SPAC6F12.02","SPAC24H6.08","SPBC1347.02","SPBC9B6.11c","SPBC9B6.03","SPBC2F12.03c","SPAC24B11.11c","SPAC8C9.04","SPCC962.02c","SPAC22E12.11c","SPAC29A4.16","SPAC4F10.13c","SPCC1322.08","SPAC16E8.01","SPAC222.10c","SPBC1347.10","SPBC13E7.07","SPBC1289.10c","SPBC18H10.04c","SPBC25B2.07c","SPBC530.04","SPCPJ732.01","SPCC1672.02c","SPAC26H5.02c","SPCC285.16c","SPAC11G7.01","SPAC16C9.07","SPAC31A2.07c","SPAC9G1.10c","SPBC15D4.01c","SPCC188.07","SPAC1B1.04c","SPBC106.16","SPAC29E6.02","SPBC4F6.12","SPAC1F3.06c","SPBC12C2.10c","SPBC32F12.06","SPAPJ760.02c","SPAPB1A10.09","SPCC417.07c","SPAC1952.16","SPCC584.04","SPAC15A10.02","SPCC16C4.07","SPCC16A11.17","SPAC2F7.03c","SPBC28F2.07","SPBC685.09","SPAC6B12.11","SPCC285.13c","SPBC336.12c","SPAC19E9.01c","SPAC30D11.10","SPAC9G1.06c","SPBC17D1.05","SPBC4F6.15c","SPCC777.08c","SPAC9.11","SPBC29B5.01","SPCC1620.14c","SPAC17A5.07c","SPBC28E12.03","SPAC9G1.07","SPAC24B11.07c","SPAC821.03c","SPAC26F1.10c","SPAC3F10.15c","SPAC6B12.05c","SPBC409.07c","SPCC550.13","SPCC736.12c","SPBC1D7.02c","SPCC736.14","SPBC17D11.05","SPAC24H6.06","SPAC4H3.11c","SPBC16A3.19","SPCC1739.01","SPCC622.16c","SPBC27.02c","SPAC31A2.14","SPAC3H1.11","SPCC1620.07c","SPBC1A4.03c","SPAC3G9.01","SPCC1795.01c","SPBC17A3.05c","SPBC14C8.14c","SPBC26H8.01","SPAC13G7.04c","SPBC28F2.11","SPAC19G12.07c","SPBC1289.04c","SPCC962.06c"],"gene_count":183,"ltp_gene_count":1,"approved_date":"2017-07-11"},{"uniquename":"PMID:6526810","title":"Formation of cadmium-binding peptide allomorphs in fission yeast.","citation":"J Biochem 1984 Nov;96(5):1375-9","abstract":"It has been reported that two kinds of Cd-binding peptide (Cd-BP1 and Cd-BP2) are induced in fission yeast upon exposure to Cd, and that they consist of the same unit peptide (cadystin), but Cd-BP1 binds 1.5 times more Cd atoms per cadystin than Cd-BP2 (Murasugi, A., Wada, C., & Hayashi, Y. (1981) J. Biochem. 90, 1561-1564). The relative amount of each allomorphic Cd-BP in the cell varied with time after induction and with the concentration of Cd in the induction medium. Further, the production of acid-labile sulfide in the cell increased greatly upon exposure to Cd and varied with time after Cd addition and with Cd concentration in the medium, as in the case of Cd-BP1. Since Cd-BP1 contains labile sulfide, the increase of labile sulfide production together with the increase of cellular Cd concentration may be the driving force to form Cd-BP1, resulting in the increase of the relative amount of Cd-BP1.","authors":"Murasugi A, Wada Nakagawa C, Hayashi Y","authors_abbrev":"Murasugi A et al.","pubmed_publication_date":"Nov 1984","pubmed_entrez_date":"1984-11-01","publication_year":"1984","canto_session_key":"b4082815f893bbf5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-26 13:24:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-09-26 13:24:21","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-09-26"},{"uniquename":"PMID:22604726","title":"Oscillatory dynamics of Cdc42 GTPase in the control of polarized growth.","citation":"Science 2012 Jul 13;337(6091):239-43","abstract":"Cells promote polarized growth by activation of Rho-family protein Cdc42 at the cell membrane. We combined experiments and modeling to study bipolar growth initiation in fission yeast. Concentrations of a fluorescent marker for active Cdc42, Cdc42 protein, Cdc42-activator Scd1, and scaffold protein Scd2 exhibited anticorrelated fluctuations and oscillations with a 5-minute average period at polarized cell tips. These dynamics indicate competition for active Cdc42 or its regulators and the presence of positive and delayed negative feedbacks. Cdc42 oscillations and spatial distribution were sensitive to the amounts of Cdc42-activator Gef1 and to the activity of Cdc42-dependent kinase Pak1, a negative regulator. Feedbacks regulating Cdc42 oscillations and spatial self-organization appear to provide a flexible mechanism for fission yeast cells to explore polarization states and to control their morphology.","doi":"10.1126/science.1218377","authors":"Das M, Drake T, Wiley DJ, Buchwald P, Vavylonis D, Verde F","authors_abbrev":"Das M et al.","pubmed_publication_date":"13 Jul 2012","pubmed_entrez_date":"2012-05-19","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22024167","title":"Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring.","citation":"J Cell Biol 2011 Oct 31;195(3):485-98","abstract":"We created two new mutants of fission yeast cofilin to investigate why cytokinesis in many organisms depends on this small actin-binding protein. These mutant cofilins bound actin monomers normally, but bound and severed ADP-actin filaments much slower than wild-type cofilin. Cells depending on mutant cofilins condensed nodes, precursors of the contractile ring, into clumps rather than rings. Starting from clumped nodes, mutant cells slowly assembled rings from diverse intermediate structures including spiral strands containing actin filaments and other contractile ring proteins. This process in mutant cells depended on α-actinin. These slowly assembled contractile rings constricted at a normal rate but with more variability, indicating ring constriction is not very sensitive to defects in severing by cofilin. Computer simulations of the search-capture-pull and release model of contractile ring formation predicted that nodes clump when the release step is slow, so cofilin severing of actin filament connections between nodes likely contributes to the release step.","doi":"10.1083/jcb.201103067","authors":"Chen Q, Pollard TD","authors_abbrev":"Chen Q et al.","pubmed_publication_date":"31 Oct 2011","pubmed_entrez_date":"2011-10-26","publication_year":"2011","canto_session_key":"389e7e262d4752a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-12-20 15:34:45","canto_approved_date":"2025-04-18 17:16:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-20 15:34:36","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":53,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC15A10.08","SPAC27F1.02c","SPAC926.03","SPAC20G4.06c","SPAC9G1.05"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-12-20"},{"uniquename":"PMID:27480720","title":"Synchronizing Progression of Schizosaccharomyces pombe Cells from G2 through Repeated Rounds of Mitosis and S Phase with cdc25-22 Arrest Release.","citation":"Cold Spring Harb Protoc 2016 Aug 01;2016(8)","abstract":"Transient inactivation of the cdc25(+) gene product by manipulation of the culture temperature for cdc25-22 cells is the most commonly exploited approach to mitotic synchronization in fission yeast. Because Cdc25 removes the inhibitory phosphate placed on Cdk1 by Wee1, inactivation of Cdc25 arrests cells at the G2/M boundary. Incubation at the restrictive temperature of 36°C for just over one generation time forces all cells in the culture to accumulate at the G2/M boundary. Restoration of Cdc25 function via a return to the permissive temperature or chemical inhibition of Wee1 activity at 36°C can then promote a highly synchronous wave of cell division throughout the culture. These approaches can be performed on any scale and thus support simultaneous assessment of numerous events within a single culture. After describing this simple and widely applicable procedure, we discuss frequently overlooked issues that can have a considerable impact on the interpretation of data from cdc25-22 induction-synchronized cultures.","doi":"10.1101/pdb.prot091264","authors":"Hagan IM, Grallert A, Simanis V","authors_abbrev":"Hagan IM et al.","pubmed_publication_date":"01 Aug 2016","pubmed_entrez_date":"2016-08-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-08-04 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40282392","title":"GC Content in Nuclear-Encoded Genes and Effective Number of Codons (ENC) Are Positively Correlated in AT-Rich Species and Negatively Correlated in GC-Rich Species.","citation":"Genes (Basel) 2025 Apr 05;16(4)","abstract":"Codon usage bias affects gene expression and translation efficiency across species. The effective number of codons (ENC) and GC content influence codon preference, often displaying unimodal or bimodal distributions. This study investigates the correlation between ENC and GC rankings across species and how their relationship affects codon usage distributions.\nThe correlation between ENC rank and GC rank differs among species, shaping codon usage distributions in opposite ways depending on whether a species' nuclear-encoded genes are AT-rich or GC-rich. Understanding these patterns might provide insights into translation efficiency, epigenetics mediated by CpG DNA methylation, epitranscriptomics of RNA modifications, RNA secondary structures, evolutionary pressures, and potential applications in genetic engineering and biotechnology.","doi":"10.3390/genes16040432","authors":"Ruden DM","authors_abbrev":"Ruden DM","pubmed_publication_date":"05 Apr 2025","pubmed_entrez_date":"2025-04-26","publication_year":"2025","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2025-04-26 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21528455","title":"Artificial tethering of Argonaute proteins for studying their role in translational repression of target mRNAs.","citation":"Methods Mol Biol 2011;725:191-206","abstract":"Small RNAs such as microRNAs (miRNAs) and small-interfering RNAs (siRNAs) associate with members of the RNA-binding Argonaute family proteins. Together they participate in transcriptional and posttranscriptional gene silencing mechanisms. The fate of the target mRNA is determined, in part, by the degree of complementarity with the small RNA. To examine the exact role of the Argonaute protein in the silencing complex, human Argonautes were artificially recruited to reporter mRNAs in a small RNA-independent manner by the BoxB-N-peptide tethering system. Tethering of Argonaute proteins to a reporter mRNA leads to the inhibition of translation, mimicking the repression seen with miRNAs. Similar tethering experiments were performed with fly and fission yeast Argonaute proteins and other components of the small RNP (ribonucleoprotein) complex, uncovering their specific roles in the silencing complexes containing them.","doi":"10.1007/978-1-61779-046-1_13","authors":"Eckhardt S, Szostak E, Yang Z, Pillai R","authors_abbrev":"Eckhardt S et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-04-30","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29321167","title":"Construction of Designer Selectable Marker Deletions with a CRISPR-Cas9 Toolbox in  Schizosaccharomyces pombe  and New Design of Common Entry Vectors.","citation":"G3 (Bethesda) 2018 Mar 02;8(3):789-796","abstract":"Vectors encoding selectable markers have been widely used in yeast to maintain or express exogenous DNA fragments. In the fission yeast  Schizosaccharomyces pombe , several engineered markers have been reported and widely used, such as  ura4  +  and  ScLEU2  from  Saccharomyces cerevisiae , which complement  ura4  and  leu1  mutations, respectively. These two auxotrophic markers share no homology with the  S. pombe  genome; however, most others can recombine with the genome due to sequence homology shared between the genomic and plasmid-borne copies of the markers. Here, we describe a CRISPR-Cas9 toolbox that can be used to quickly introduce \"designer\" auxotrophic marker deletions into host strains, including  leu1 -Δ 0 ,  his3 -Δ 0 , and  lys9 -Δ 0  Together with  ura4-D18 , this brings the total number of available designer deletion auxotrophic markers to four. The toolbox consists of a Cas9-gRNA expression vector and a donor DNA plasmid pair for each designer deletion. Using this toolbox, a set of auxotrophic  S. pombe  strains was constructed. Further, we reorganized essential components in the commonly used pREP series of plasmids and assembled the corresponding auxotrophic marker gene onto these plasmids. This toolbox for producing designer deletions, together with the newly developed strains and plasmids, will benefit the whole yeast community.","doi":"10.1534/g3.117.300363","authors":"Zhao Y, Boeke JD","authors_abbrev":"Zhao Y et al.","pubmed_publication_date":"02 Mar 2018","pubmed_entrez_date":"2018-01-12","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-01-14 01:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32007529","title":"Wdr70 regulates histone modification and genomic maintenance in fission yeast.","citation":"Biochim Biophys Acta Mol Cell Res 2020 May;1867(5):118665","abstract":"Eukaryotic genomes are packaged into highly condensed chromatin and this repressive chromatin barrier can be overcome by altering the chromatin structure via histone modification enzymes. Here, we report Wdr70 in Schizosaccharomyces pombe (spWdr70) plays important roles in multiple cellular processes including cell cycle progression, chromatin structure and DNA repair. Depletion of Wdr70 gene causes cell cycle delay, hypersensitivity to DNA damage reagents and quick phenotypic changes. Moreover, we observed strong genetic interaction between Wdr70 and genes regulating checkpoint and homologous recombination (HR), pinpointing the function of Wdr70 to DNA end resection. Finally, we show that the function of Wdr70 could be attributed to monoubiquitination of histone H2B (uH2B) in the vicinity of DNA double strand breaks (DSBs). Taken together, our data reveal that Wdr70 and H2B monoubiquitination-dependent chromatin modulation is required for chromatin homeostasis and genetic stability.","doi":"10.1016/j.bbamcr.2020.118665","authors":"Zeng M, Tang Z, Guo L, Wang X, Liu C","authors_abbrev":"Zeng M et al.","pubmed_publication_date":"May 2020","pubmed_entrez_date":"2020-02-03","publication_year":"2020","canto_session_key":"285545d18ef92b8a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38289024","title":"Heat stress-induced activation of MAPK pathway attenuates Atf1-dependent epigenetic inheritance of heterochromatin in fission yeast.","citation":"Elife 2024 Jan 30;13","abstract":"Eukaryotic cells are constantly exposed to various environmental stimuli. It remains largely unexplored how environmental cues bring about epigenetic fluctuations and affect heterochromatin stability. In the fission yeast  Schizosaccharomyces pombe , heterochromatic silencing is quite stable at pericentromeres but unstable at the mating-type ( mat ) locus under chronic heat stress, although both loci are within the major constitutive heterochromatin regions. Here, we found that the compromised gene silencing at the  mat  locus at elevated temperature is linked to the phosphorylation status of Atf1, a member of the ATF/CREB superfamily. Constitutive activation of MAPK signaling disrupts epigenetic maintenance of heterochromatin at the  mat  locus even under normal temperature. Mechanistically, phosphorylation of Atf1 impairs its interaction with heterochromatin protein Swi6 HP1 , resulting in lower site-specific Swi6 HP1  enrichment. Expression of non-phosphorylatable Atf1, tethering Swi6 HP1  to the  mat3M -flanking site or absence of the anti-silencing factor Epe1 can largely or partially rescue heat stress-induced defective heterochromatic maintenance at the  mat  locus.","doi":"10.7554/eLife.90525","authors":"Sun L, Liu L, Song C, Wang Y, Jin QW","authors_abbrev":"Sun L et al.","pubmed_publication_date":"30 Jan 2024","pubmed_entrez_date":"2024-01-30","publication_year":"2024","canto_session_key":"8eba150e69a624ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li Sun","canto_first_approved_date":"2024-04-05 14:27:55","canto_approved_date":"2026-06-26 07:58:03","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-04-02 12:50:14","canto_added_date":"2024-01-31 00:25:05","annotation_curators":[{"name":"Li Sun","community_curator":true,"annotation_count":11,"orcid":"0000-0003-0708-2881","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC36.05c","SPBC409.07c","SPBC428.08c","SPCC188.13c","SPBC29B5.01","SPCC622.16c","SPBC800.03","SPAC24B11.06c","SPAC664.01c"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2024-04-05"},{"uniquename":"PMID:11058086","title":"High dosage expression of a zinc finger protein, Grt1, suppresses a mutant of fission yeast slp1(+), a homolog of CDC20/p55CDC/Fizzy.","citation":"J Cell Sci 2000 Nov;113 ( Pt 22):3989-99","abstract":"Selective proteolysis at and after the onset of anaphase is a key cell cycle event required for sister chromatid separation as well as for exit from mitosis. It requires ubiquitination of substrates by Anaphase Promoting Complex(APC)/Cyclosome. Slp1, a WD-repeat protein, is a putative activator for APC in fission yeast. With another WD- repeat protein, Ste9/Srw1, it is thought to promote the proteolysis in a substrate-specific manner. We report here characterization of a temperature-sensitive (ts) slp1 mutant and its high-dosage suppressor, grt1(+). In cells arrested in metaphase, wild-type Slp1 was preferentially found in a complex with hyperphosphorylated Cut9 (subunit of APC), whereas the ts Slp1 protein, lacking the last 113 amino acids, failed to interact with Cut9. The temperature sensitivity was suppressed by high dosage expression of a zinc finger protein, Grt1. The ts slp1 mutant was unable to maintain the normal level of Grt1 protein. The reduction in the Grt1 level may be a primary defect since high dosage expression of grt1(+) rescues the slp1 mutant. The grt1-suppression had an additive effect to ste9 and wee1-50, both of which partially suppress the ts slp1 mutant. Therefore, grt1(+) would define an independent pathway that facilitates the function of Slp1.","authors":"Yamada HY, Matsumoto S, Matsumoto T","authors_abbrev":"Yamada HY et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-11-01","publication_year":"2000","canto_session_key":"8777f8b41d27a041","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-14 21:41:30","canto_approved_date":"2026-01-31 14:41:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-14 21:41:23","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPB8B6.04c","SPCC18B5.03","SPAC144.13c","SPAC25G10.07c","SPBC20F10.06","SPAC17C9.01c","SPAC6F12.15c","SPBC106.09","SPBC16G5.01","SPAC821.08c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-12-14"},{"uniquename":"PMID:26857223","title":"Lack of tRNA-i6A modification causes mitochondrial-like metabolic deficiency in S. pombe by limiting activity of cytosolic tRNATyr, not mito-tRNA.","citation":"RNA 2016 Apr;22(4):583-96","abstract":"tRNA-isopentenyl transferases (IPTases) are highly conserved enzymes that form isopentenyl-N(6)-A37 (i6A37) on subsets of tRNAs, enhancing their translation activity. Nuclear-encoded IPTases modify select cytosolic (cy-) and mitochondrial (mt-) tRNAs. Mutation in human IPTase, TRIT1, causes disease phenotypes characteristic of mitochondrial translation deficiency due to mt-tRNA dysfunction. Deletion of the Schizosaccharomyces pombe IPTase (tit1-Δ) causes slow growth in glycerol, as well as in rapamycin, an inhibitor of TOR kinase that maintains metabolic homeostasis. Schizosaccharomyces pombe IPTase modifies three different cy-tRNAs(Ser) as well as cy-tRNA(Tyr), cy-tRNA(Trp), and mt-tRNA(Trp). We show that lower ATP levels in tit1-Δ relative to tit1(+) cells are also more decreased by an inhibitor of oxidative phosphorylation, indicative of mitochondrial dysfunction. Here we asked if the tit1-Δ phenotypes are due to hypomodification of cy-tRNA or mt-tRNA. A cytosol-specific IPTase that modifies cy-tRNA, but not mt-tRNA, fully rescues the tit1-Δ phenotypes. Moreover, overexpression of cy-tRNAs also rescues the phenotypes, and cy-tRNA(Tyr) alone substantially does so. Bioinformatics indicate that cy-tRNA(Tyr) is most limiting for codon demand in tit1-Δ cells and that the cytosolic mRNAs most loaded with Tyr codons encode carbon metabolilizing enzymes, many of which are known to localize to mitochondria. Thus, S. pombe i6A37 hypomodification-associated metabolic deficiency results from hypoactivity of cy-tRNA, mostly tRNA(Tyr), and unlike human TRIT1-deficiency does not impair mitochondrial translation due to mt-tRNA hypomodification. We discuss species-specific aspects of i6A37. Specifically relevant to mitochondria, we show that its hypermodified version, ms2i6A37 (2-methylthiolated), which occurs on certain mammalian mt-tRNAs (but not cy-tRNAs), is not found in yeast.","doi":"10.1261/rna.054064.115","authors":"Lamichhane TN, Arimbasseri AG, Rijal K, Iben JR, Wei FY, Tomizawa K, Maraia RJ","authors_abbrev":"Lamichhane TN et al.","pubmed_publication_date":"Apr 2016","pubmed_entrez_date":"2016-02-10","publication_year":"2016","canto_session_key":"87f07c04ee2e8393","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-11 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23613586","title":"Structural analysis of Stc1 provides insights into the coupling of RNAi and chromatin modification.","citation":"Proc Natl Acad Sci U S A 2013 May 21;110(21):E1879-88","abstract":"Noncoding RNAs can modulate gene expression by directing modifications to histones that alter chromatin structure. In fission yeast, siRNAs produced via the RNAi pathway direct modifications associated with heterochromatin formation. siRNAs associate with the RNAi effector protein Argonaute 1 (Ago1), targeting the Ago1-containing RNA-induced transcriptional silencing (RITS) complex to homologous nascent transcripts. This promotes recruitment of the Clr4 complex (CLRC), which mediates methylation of histone H3 on lysine 9 (H3K9me) in cognate chromatin. A key question is how the RNAi and chromatin modification machineries are connected. Stc1 is a small protein recently shown to associate with both Ago1 and CLRC and to play a pivotal role in mediating the RNAi-dependent recruitment of CLRC to chromatin. To understand its mode of action, we have performed a detailed structural and functional analysis of the Stc1 protein. Our analyses reveal that the conserved N-terminal region of Stc1 represents an unusual tandem zinc finger domain, with similarities to common LIM domains but distinguished by a lack of preferred relative orientation of the two zinc fingers. We demonstrate that this tandem zinc finger domain is involved in binding Ago1, whereas the nonconserved C-terminal region mediates association with CLRC. These findings elucidate the molecular basis for the coupling of RNAi to chromatin modification in fission yeast.","doi":"10.1073/pnas.1212155110","authors":"He C, Pillai SS, Taglini F, Li F, Ruan K, Zhang J, Wu J, Shi Y, Bayne EH","authors_abbrev":"He C et al.","pubmed_publication_date":"21 May 2013","pubmed_entrez_date":"2013-04-25","publication_year":"2013","canto_session_key":"1e00c626a8ce874f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elizabeth Bayne","canto_first_approved_date":"2021-01-13 10:51:56","canto_approved_date":"2022-07-19 17:00:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-18 09:27:36","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Elizabeth Bayne","community_curator":true,"annotation_count":27,"orcid":"0000-0001-8775-999X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC11E10.08","SPCC613.12c","SPCC970.07c","SPBC428.08c","SPBP8B7.28c","SPCC736.11"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2021-01-13","pdb_entries":[{"pdb_id":"2luy","gene_chains":[{"gene_uniquename":"SPBP8B7.28c","chain":"A","position":"32-126"}],"title":"Solution structure of the tandem zinc finger domain of fission yeast Stc1","entry_authors":"He C,Shi Y,Bayne E,Wu J","entry_authors_abbrev":"He C et al.","reference_uniquename":"PMID:23613586","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:19686686","title":"Phospho-regulated interaction between kinesin-6 Klp9p and microtubule bundler Ase1p promotes spindle elongation.","citation":"Dev Cell 2009 Aug;17(2):257-67","abstract":"The spindle midzone-composed of antiparallel microtubules, microtubule-associated proteins (MAPs), and motors-is the structure responsible for microtubule organization and sliding during anaphase B. In general, MAPs and motors stabilize the midzone and motors produce sliding. We show that fission yeast kinesin-6 motor klp9p binds to the microtubule antiparallel bundler ase1p at the midzone at anaphase B onset. This interaction depends upon the phosphorylation states of klp9p and ase1p. The cyclin-dependent kinase cdc2p phosphorylates and its antagonist phosphatase clp1p dephosphorylates klp9p and ase1p to control the position and timing of klp9p-ase1p interaction. Failure of klp9p-ase1p binding leads to decreased spindle elongation velocity. The ase1p-mediated recruitment of klp9p to the midzone accelerates pole separation, as suggested by computer simulation. Our findings indicate that a phosphorylation switch controls the spatial-temporal interactions of motors and MAPs for proper anaphase B, and suggest a mechanism whereby a specific motor-MAP conformation enables efficient microtubule sliding.","doi":"10.1016/j.devcel.2009.06.012","authors":"Fu C, Ward JJ, Loiodice I, Velve-Casquillas G, Nedelec FJ, Tran PT","authors_abbrev":"Fu C et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-08-19","publication_year":"2009","canto_session_key":"fa51a7649e995191","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-07-26 15:41:13","canto_approved_date":"2023-07-26 11:12:43","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2018-07-26 13:51:40","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":55,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.10","SPAC3A11.14c","SPBC1604.20c","SPAC1834.07","SPBC582.03","SPBC11B10.09","SPBC15D4.01c","SPAPB1A10.09","SPAC1782.09c","SPAC25G10.07c","SPAC1093.06c","SPBC2F12.13","SPBC1685.15c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2018-07-26"},{"uniquename":"PMID:3830131","title":"Homology between the ran1+ gene of fission yeast and protein kinases.","citation":"EMBO J 1986 Dec 20;5(13):3665-71","abstract":"The ran1+ gene of the fission yeast Schizosaccharomyces pombe is a negative regulator of both sexual conjugation and meiosis. The nucleotide sequence of the gene has been determined and contains a region of open reading frame (ORF) capable of encoding a protein of 52,000 daltons. S1 nuclease analysis of ran1+-encoded RNA showed that the ORF was spanned by an uninterrupted transcript. A fragment of DNA containing the entire ran1+ gene was expressed in a bacterial expression vector and found to encode the expected product of 52,000 daltons. The putative ran1+ gene product shares significant sequence homology with known protein kinases. The level of the ran1+ transcript was similar in vegetative and meiotic cells suggesting that the ran1+ protein product rather than its transcript is regulated during sexual differentiation.","authors":"McLeod M, Beach D","authors_abbrev":"McLeod M et al.","pubmed_publication_date":"20 Dec 1986","pubmed_entrez_date":"1986-12-20","publication_year":"1986","canto_session_key":"24990138360fab50","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-31 16:06:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-31 16:05:52","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-31"},{"uniquename":"PMID:42015844","title":"Schizosaccharomyces Orthogroup (SOG) Resource: A Web Platform for Exploring Gene Conservation in Fission Yeasts.","citation":"Yeast 2026 Apr 22;","abstract":"The fission yeast Schizosaccharomyces pombe is a prominent model organism widely used to investigate fundamental cellular mechanisms. In addition to S. pombe, the genus Schizosaccharomyces includes six other species-S. octosporus, S. japonicus, S. cryophilus, S. osmophilus, S. lindneri, and S. versatilis. These fission yeast species share a common ancestor from which the genus diversified over more than 200 million years. This extensive evolutionary divergence provides opportunities for comparative genomics. Here, we present the Schizosaccharomyces orthogroup (SOG) resource, a web platform developed from our high-quality genome assemblies, gene annotations, and orthology assignments. Most fission yeast genes are assigned to one of over 5,000 orthogroups. The platform enables users to visualize orthogroup sequence alignments and phylogenetic trees, retrieve coding and flanking sequences, and explore the conservation of local synteny. This resource will benefit researchers focusing on individual genes as well as those investigating gene evolution at broader scales. It is freely accessible at https://www.sogweb.org.","doi":"10.1002/yea.70019","authors":"Jia GS, Suo F, Noly A, Fort P, Liang Y, Li W, Zhang WC, Li HL, Du XM, Zhang FY, Du TY, Hua Y, Bai FY, Wang QM, Brysch-Herzberg M, Helmlinger D, Du LL","authors_abbrev":"Jia GS et al.","pubmed_publication_date":"22 Apr 2026","pubmed_entrez_date":"2026-04-22","publication_year":"2026","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2026-04-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19704860","title":"Transcription of mRNA-type long non-coding RNAs (mlonRNAs) disrupts chromatin array.","citation":"Commun Integr Biol 2009;2(1):25-6","abstract":"Eukaryotic transcriptome analyses have revealed that many transcripts are non-coding RNAs (ncRNAs). In addition, most relatively large ( approximately several kb) polyadenylated mRNA type transcripts are transcribed from regions harboring little coding potential. However the role of such mRNA type long ncRNAs (mlonRNAs) is mostly unknown and has been a matter of debate. Recently, we showed that cascade of RNA polymerase II (RNAPII)-mediated transcriptional initiation of mlonRNA causes stepwise disruption of local chromatin array at the fission yeast Schizosaccharomyces pombe fbp1(+) promoter region. Here, we hypothesize that RNAPII transcription of mlonRNA disrupt chromatin array possibly collaborating with histone acetylation mechanism. In addition, conserved action of Atf1, a transcriptional activator and Tup11-Tup12 corepressors along mlonRNA transcription mediated chromatin regulation is suggested. This idea provides new insight into the biological meaning of mlonRNAs found in various eukaryotes.","authors":"Hirota K, Ohta K","authors_abbrev":"Hirota K et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-08-26","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25688133","title":"The F-BAR Cdc15 promotes contractile ring formation through the direct recruitment of the formin Cdc12.","citation":"J Cell Biol 2015 Feb 16;208(4):391-9","abstract":"In Schizosaccharomyces pombe, cytokinesis requires the assembly and constriction of an actomyosin-based contractile ring (CR). Nucleation of F-actin for the CR requires a single formin, Cdc12, that localizes to the cell middle at mitotic onset. Although genetic requirements for formin Cdc12 recruitment have been determined, the molecular mechanisms dictating its targeting to the medial cortex during cytokinesis are unknown. In this paper, we define a short motif within the N terminus of Cdc12 that binds directly to the F-BAR domain of the scaffolding protein Cdc15. Mutations preventing the Cdc12-Cdc15 interaction resulted in reduced Cdc12, F-actin, and actin-binding proteins at the CR, which in turn led to a delay in CR formation and sensitivity to other perturbations of CR assembly. We conclude that Cdc15 contributes to CR formation and cytokinesis via formin Cdc12 recruitment, defining a novel cytokinetic function for an F-BAR domain.","doi":"10.1083/jcb.201411097","authors":"Willet AH, McDonald NA, Bohnert KA, Baird MA, Allen JR, Davidson MW, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"16 Feb 2015","pubmed_entrez_date":"2015-02-18","publication_year":"2015","canto_session_key":"186e8e06649ff2d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2018-02-28 14:38:36","canto_approved_date":"2023-04-14 08:35:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-16 22:21:01","canto_added_date":"2015-02-19 01:15:27","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.03","SPAC20G8.05c","SPAC20G4.06c","SPAC15A10.08","SPCC4B3.15","SPAC1F5.04c","SPAC4F8.13c","SPCC645.05c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2018-02-28"},{"uniquename":"PMID:11895484","title":"Meu10 is required for spore wall maturation in Schizosaccharomyces pombe.","citation":"Genes Cells 2002 Feb;7(2):217-31","abstract":"Many genes are meiosis and/or sporulation-specifically transcribed during this process. Isolation and analysis of these genes might help us to understand how meiosis and sporulation are regulated. For this purpose, we have isolated a large number of cDNA clones from Schizosaccharomyces pombe whose expression is up-regulated during meiosis.\nWe have isolated meu10+ gene, which encodes 416 amino acids and bears homology to SPS2 of Saccharomyces cerevisiae. A strain whose meu10+ gene has been deleted forms no viable spores. Thin-section electron micrographs showed that the meu10Delta strain has abnormally formed spore walls, and then they disrupt, allowing cytoplasmic material to escape. The Meu10-GFP fusion protein is localized to the spore periphery, thereafter returned to the cytoplasm after sporulation. Meu10-GFP localization to the spore wall was almost normal in the bgs2Delta or chs1Delta mutants that lack 1,3-beta-glucan or chitin, respectively. In contrast, 1,3-beta-glucan is abnormally localized in meu10Delta cells. Meu10 has an N-terminal domain with homology to the mammalian insulin receptor and a C-terminal domain with a transmembrane motif. Mutants whose N-terminal or C-terminal domain was truncated were severely defective for sporulation.\nMeu10 is a spore wall component and plays a pivotal role in the formation of the mature spore wall structure.","authors":"Tougan T, Chiba Y, Kakihara Y, Hirata A, Nojima H","authors_abbrev":"Tougan T et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-03-16","publication_year":"2002","canto_session_key":"5097e18e203bd23d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-18 15:20:31","canto_approved_date":"2024-06-18 15:20:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-17 12:38:12","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G6.12c","SPAC24C9.07c","SPBC32H8.11","SPCC1223.12c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2024-06-18"},{"uniquename":"PMID:25392932","title":"RNA processing factors Swd2.2 and Sen1 antagonize RNA Pol III-dependent transcription and the localization of condensin at Pol III genes.","citation":"PLoS Genet 2014 Nov;10(11):e1004794","abstract":"Condensin-mediated chromosome condensation is essential for genome stability upon cell division. Genetic studies have indicated that the association of condensin with chromatin is intimately linked to gene transcription, but what transcription-associated feature(s) direct(s) the accumulation of condensin remains unclear. Here we show in fission yeast that condensin becomes strikingly enriched at RNA Pol III-transcribed genes when Swd2.2 and Sen1, two factors involved in the transcription process, are simultaneously deleted. Sen1 is an ATP-dependent helicase whose orthologue in Saccharomyces cerevisiae contributes both to terminate transcription of some RNA Pol II transcripts and to antagonize the formation of DNA:RNA hybrids in the genome. Using two independent mapping techniques, we show that DNA:RNA hybrids form in abundance at Pol III-transcribed genes in fission yeast but we demonstrate that they are unlikely to faciliate the recruitment of condensin. Instead, we show that Sen1 forms a stable and abundant complex with RNA Pol III and that Swd2.2 and Sen1 antagonize both the interaction of RNA Pol III with chromatin and RNA Pol III-dependent transcription. When Swd2.2 and Sen1 are lacking, the increased concentration of RNA Pol III and condensin at Pol III-transcribed genes is accompanied by the accumulation of topoisomerase I and II and by local nucleosome depletion, suggesting that Pol III-transcribed genes suffer topological stress. We provide evidence that this topological stress contributes to recruit and/or stabilize condensin at Pol III-transcribed genes in the absence of Swd2.2 and Sen1. Our data challenge the idea that a processive RNA polymerase hinders the binding of condensin and suggest that transcription-associated topological stress could in some circumstances facilitate the association of condensin.","doi":"10.1371/journal.pgen.1004794","authors":"Legros P, Malapert A, Niinuma S, Bernard P, Vanoosthuyse V","authors_abbrev":"Legros P et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-11-14","publication_year":"2014","canto_session_key":"b8319e8f5cb44f5a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Vincent Vanoosthuyse","canto_first_approved_date":"2014-11-26 08:33:29","canto_approved_date":"2021-04-14 11:48:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-17 13:24:59","canto_added_date":"2014-11-15 01:16:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Vanoosthuyse","community_curator":true,"annotation_count":14,"orcid":null,"file_type":null,"file_name":null},{"name":"Vincent Vanoosthuyse","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.12c","SPBC651.08c","SPBC1703.14c","SPBC146.03c","SPAPB1E7.10","SPCC330.13","SPAC6G9.10c","SPAC22A12.05","SPCC18.07","SPCC290.02","SPAC4G9.08c","SPAPB1E7.03","SPBC839.12","SPBC2G5.07c","SPAC824.04","SPBC336.06c","SPAC22A12.01c","SPBP4H10.06c","SPBC1289.07c","SPAC1687.01"],"gene_count":20,"ltp_gene_count":19,"approved_date":"2014-11-26"},{"uniquename":"PMID:27398807","title":"Functional Crosstalk between the PP2A and SUMO Pathways Revealed by Analysis of STUbL Suppressor, razor 1-1.","citation":"PLoS Genet 2016 Jul;12(7):e1006165","abstract":"Posttranslational modifications (PTMs) provide dynamic regulation of the cellular proteome, which is critical for both normal cell growth and for orchestrating rapid responses to environmental stresses, e.g. genotoxins. Key PTMs include ubiquitin, the Small Ubiquitin-like MOdifier SUMO, and phosphorylation. Recently, SUMO-targeted ubiquitin ligases (STUbLs) were found to integrate signaling through the SUMO and ubiquitin pathways. In general, STUbLs are recruited to target proteins decorated with poly-SUMO chains to ubiquitinate them and drive either their extraction from protein complexes, and/or their degradation at the proteasome. In fission yeast, reducing or preventing the formation of SUMO chains can circumvent the essential and DNA damage response functions of STUbL. This result indicates that whilst some STUbL \"targets\" have been identified, the crucial function of STUbL is to antagonize SUMO chain formation. Herein, by screening for additional STUbL suppressors, we reveal crosstalk between the serine/threonine phosphatase PP2A-Pab1B55 and the SUMO pathway. A hypomorphic Pab1B55 mutant not only suppresses STUbL dysfunction, but also mitigates the phenotypes associated with deletion of the SUMO protease Ulp2, or mutation of the STUbL cofactor Rad60. Together, our results reveal a novel role for PP2A-Pab1B55 in modulating SUMO pathway output, acting in parallel to known critical regulators of SUMOylation homeostasis. Given the broad evolutionary functional conservation of the PP2A and SUMO pathways, our results could be relevant to the ongoing attempts to therapeutically target these factors.","doi":"10.1371/journal.pgen.1006165","authors":"Nie M, Arner E, Prudden J, Schaffer L, Head S, Boddy MN","authors_abbrev":"Nie M et al.","pubmed_publication_date":"Jul 2016","pubmed_entrez_date":"2016-07-12","publication_year":"2016","canto_session_key":"d9011560b1887e36","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Minghua Nie","canto_first_approved_date":"2016-08-30 14:46:43","canto_approved_date":"2019-06-14 12:30:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-07-27 18:41:30","canto_added_date":"2016-07-13 00:15:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":102,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Minghua Nie","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC4G3.05c","SPAC1805.04","SPBC16A3.09c","SPCC1259.13","SPBC1921.02","SPAC1687.05","SPBC16H5.07c","SPAC644.14c","SPAC1782.05","SPAC17A5.07c","SPAC19A8.10","SPCC18B5.11c","SPBC3D6.11c","SPAC2G11.12","SPAC343.18","SPCC18B5.03","SPAC227.07c"],"gene_count":18,"ltp_gene_count":17,"approved_date":"2016-08-30"},{"uniquename":"PMID:8106391","title":"Structure/function relationship of the Chlorella glucose/H+ symporter.","citation":"J Biol Chem 1994 Feb 04;269(5):3498-502","abstract":"The Clorella kessleri HUP 1 gene coding for a hexose/H+ symporter has been expressed in a glucose uptake-deficient mutant of Schizosaccharomyces pombe. The transformants are able to grow on glucose and to accumulate 3-O-methylglucose 100-fold. This system has been used to test the activity of specifically mutated HUP 1 cDNAs. All three histidyl residues were exchanged with arginine (H73R, H170R, and H495R) without a major effect on transport activity. When Asp-44 within the first transmembrane helix was replaced by Asn, the transporter was inactive; replacement by Glu (D44E) resulted in a loss of activity by 90% and a 15-fold increased Km value. Glutamine residues conserved in all glucose transporters sequenced so far were exchanged: Q179N (in helix 5), Q298G and Q299N (both in helix 7). Whereas Q298G only resulted in a small Km change, both Q179N and Q299N showed an increase in Km by a factor of 10. Inserting 4 additional amino acids each into the two largest loops (1 and 6) reduced the activity dramatically; only in the latter case this was due to decreased protein synthesis or stability. Two COOH-terminal deletions (-27 and -43 amino acids) were also tested. The 27 COOH-terminal amino acids, but not the 43 COOH-terminal amino acids, could be removed without affecting transporter activity.","authors":"Caspari T, Stadler R, Sauer N, Tanner W","authors_abbrev":"Caspari T et al.","pubmed_publication_date":"04 Feb 1994","pubmed_entrez_date":"1994-02-04","publication_year":"1994","canto_session_key":"903b854e67cd0135","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:30:32","canto_session_submitted_date":"2012-03-03 15:30:17","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"EMBL:AU010291","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28410370","title":"A systematic screen for morphological abnormalities during fission yeast sexual reproduction identifies a mechanism of actin aster formation for cell fusion.","citation":"PLoS Genet 2017 Apr;13(4):e1006721","abstract":"In non-motile fungi, sexual reproduction relies on strong morphogenetic changes in response to pheromone signaling. We report here on a systematic screen for morphological abnormalities of the mating process in fission yeast Schizosaccharomyces pombe. We derived a homothallic (self-fertile) collection of viable deletions, which, upon visual screening, revealed a plethora of phenotypes affecting all stages of the mating process, including cell polarization, cell fusion and sporulation. Cell fusion relies on the formation of the fusion focus, an aster-like F-actin structure that is marked by strong local accumulation of the myosin V Myo52, which concentrates secretion at the fusion site. A secondary screen for fusion-defective mutants identified the myosin V Myo51-associated coiled-coil proteins Rng8 and Rng9 as critical for the coalescence of the fusion focus. Indeed, rng8Δ and rng9Δ mutant cells exhibit multiple stable dots at the cell-cell contact site, instead of the single focus observed in wildtype. Rng8 and Rng9 accumulate on the fusion focus, dependent on Myo51 and tropomyosin Cdc8. A tropomyosin mutant allele, which compromises Rng8/9 localization but not actin binding, similarly leads to multiple stable dots instead of a single focus. By contrast, myo51 deletion does not strongly affect fusion focus coalescence. We propose that focusing of the actin filaments in the fusion aster primarily relies on Rng8/9-dependent cross-linking of tropomyosin-actin filaments.","doi":"10.1371/journal.pgen.1006721","authors":"Dudin O, Merlini L, Bendezú FO, Groux R, Vincenzetti V, Martin SG","authors_abbrev":"Dudin O et al.","pubmed_publication_date":"Apr 2017","pubmed_entrez_date":"2017-04-15","publication_year":"2017","canto_session_key":"5724d1814ea9f342","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2021-03-17 16:18:07","canto_approved_date":"2026-03-28 12:49:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-03-09 21:15:05","canto_added_date":"2017-04-16 00:15:15","annotation_curators":[{"name":"Sophie Martin","community_curator":true,"annotation_count":35,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Sophie Martin","file_curator_role":"community","annotation_file_curators":[{"name":"Sophie 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usage is less optimized in eukaryotic gene segments encoding intrinsically disordered regions than in those encoding structural domains.","citation":"Nucleic Acids Res 2016 Dec 01;44(21):10051-10061","abstract":"Codon usage tends to be optimized in highly expressed genes. A plausible explanation for this phenomenon is that translational accuracy is increased in highly expressed genes with infrequent use of rare codons. Besides structural domains (SDs), eukaryotic proteins generally have intrinsically disordered regions (IDRs) that by themselves do not assume unique three-dimensional structures. As IDRs are free from structural constraint, they can probably accommodate more translational errors than SDs can. Thus, codon usage in IDRs is likely to be less optimized than that in SDs. Codon usage in all the genes of seven eukaryotes was examined in terms of both tRNA adaptation index and codon adaptation index. Different amino acid compositions in different protein regions were taken into account in calculating expected adaptation indices, to which observed indices were compared. Codon usage is less optimized in gene regions encoding IDRs than in those corresponding to SDs. The finding does not depend on whether IDRs are located at the N-terminus, in the middle, or at the C-terminus of proteins. Furthermore, the observation remains unchanged in two different algorithms used to predict IDRs in proteins. The result is consistent with the idea that IDRs tolerate more translational errors than SDs.","authors":"Homma K, Noguchi T, Fukuchi S","authors_abbrev":"Homma K et al.","pubmed_publication_date":"01 Dec 2016","pubmed_entrez_date":"2016-12-05","publication_year":"2016","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2017-06-15 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19584054","title":"The transcription factor Atf1 binds and activates the APC/C ubiquitin ligase in fission yeast.","citation":"J Biol Chem 2009 Sep 04;284(36):23989-94","abstract":"Fission yeast Atf1 is a member of the ATF/CREB basic leucine zipper (bZIP) family of transcription factors with strong homology to mammalian ATF2. Atf1 regulates transcription in response to stress stimuli and also plays a role in controlling heterochromatin formation and recombination. However, its DNA binding independent role is poorly studied. Here, we report that Atf1 has a distinct role in regulating the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. We have identified atf1(+) as a dose-dependent suppressor of apc5-1, a mutation causing mitotic arrest. Remarkably, the suppression is not dependent upon the bZIP domain and is therefore independent of the ability of Atf1 to bind DNA. Interestingly, Atf1 physically binds the APC/C in vivo. Furthermore, we show that addition of purified Atf1 proteins into a cell-free system stimulates ubiquitylation of cyclin B and securin by the APC/C. These results reveal a novel role for Atf1 in cell cycle control through protein-protein interaction.","doi":"10.1074/jbc.M109.018309","authors":"Ors A, Grimaldi M, Kimata Y, Wilkinson CR, Jones N, Yamano H","authors_abbrev":"Ors A et al.","pubmed_publication_date":"04 Sep 2009","pubmed_entrez_date":"2009-07-09","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12796476","title":"The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin.","citation":"J Cell Biol 2003 Jun 09;161(5):875-87","abstract":"Cytokinesis in most eukaryotes requires the assembly and contraction of a ring of actin filaments and myosin II. The fission yeast Schizosaccharomyces pombe requires the formin Cdc12p and profilin (Cdc3p) early in the assembly of the contractile ring. The proline-rich formin homology (FH) 1 domain binds profilin, and the FH2 domain binds actin. Expression of a construct consisting of the Cdc12 FH1 and FH2 domains complements a conditional mutant of Cdc12 at the restrictive temperature, but arrests cells at the permissive temperature. Cells overexpressing Cdc12(FH1FH2)p stop growing with excessive actin cables but no contractile rings. Like capping protein, purified Cdc12(FH1FH2)p caps the barbed end of actin filaments, preventing subunit addition and dissociation, inhibits end to end annealing of filaments, and nucleates filaments that grow exclusively from their pointed ends. The maximum yield is one filament pointed end per six formin polypeptides. Profilins that bind both actin and poly-l-proline inhibit nucleation by Cdc12(FH1FH2)p, but polymerization of monomeric actin is faster, because the filaments grow from their barbed ends at the same rate as uncapped filaments. On the other hand, Cdc12(FH1FH2)p blocks annealing even in the presence of profilin. Thus, formins are profilin-gated barbed end capping proteins with the ability to initiate actin filaments from actin monomers bound to profilin. These properties explain why contractile ring assembly requires both formin and profilin and why viability depends on the ability of profilin to bind both actin and poly-l-proline.","authors":"Kovar DR, Kuhn JR, Tichy AL, Pollard TD","authors_abbrev":"Kovar DR et al.","pubmed_publication_date":"09 Jun 2003","pubmed_entrez_date":"2003-06-11","publication_year":"2003","canto_session_key":"aa6c8a119000c53e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-15 15:08:06","canto_approved_date":"2022-10-01 00:09:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-17 18:49:01","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPAC1F5.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2020-12-15"},{"uniquename":"PMID:28017606","title":"Generation of a Spindle Checkpoint Arrest from Synthetic Signaling Assemblies.","citation":"Curr Biol 2017 Jan 09;27(1):137-143","abstract":"The spindle checkpoint acts as a mitotic surveillance system, monitoring interactions between kinetochores and spindle microtubules and ensuring high-fidelity chromosome segregation [1-3]. The checkpoint is activated by unattached kinetochores, and Mps1 kinase phosphorylates KNL1 on conserved MELT motifs to generate a binding site for the Bub3-Bub1 complex [4-7]. This leads to dynamic kinetochore recruitment of Mad proteins [8, 9], a conformational change in Mad2 [10-12], and formation of the mitotic checkpoint complex (MCC: Cdc20-Mad3-Mad2 [13-15]). MCC formation inhibits the anaphase-promoting complex/cyclosome (Cdc20-APC/C), thereby preventing the proteolytic destruction of securin and cyclin and delaying anaphase onset. What happens at kinetochores after Mps1-dependent Bub3-Bub1 recruitment remains mechanistically unclear, and it is not known whether kinetochore proteins other than KNL1 have significant roles to play in checkpoint signaling and MCC generation. Here, we take a reductionist approach, avoiding the complexities of kinetochores, and demonstrate that co-recruitment of KNL1 Spc7  and Mps1 Mph1  is sufficient to generate a robust checkpoint signal and prolonged mitotic arrest. We demonstrate that a Mad1-Bub1 complex is formed during synthetic checkpoint signaling. Analysis of bub3Δ mutants demonstrates that Bub3 acts to suppress premature checkpoint signaling. This synthetic system will enable detailed, mechanistic dissection of MCC generation and checkpoint silencing. After analyzing several mutants that affect localization of checkpoint complexes, we conclude that spindle checkpoint arrest can be independent of their kinetochore, spindle pole, and nuclear envelope localization.","doi":"10.1016/j.cub.2016.11.014","authors":"Yuan I, Leontiou I, Amin P, May KM, Soper Ní Chafraidh S, Zlámalová E, Hardwick KG","authors_abbrev":"Yuan I et al.","pubmed_publication_date":"09 Jan 2017","pubmed_entrez_date":"2016-12-27","publication_year":"2017","canto_session_key":"b015a7efb76f7cb7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-07-28 13:18:58","canto_approved_date":"2024-04-04 08:42:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-07-21 17:01:03","canto_added_date":"2018-07-18 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.01c","SPBC3D6.04c","SPBC106.01","SPBC365.15","SPCC1322.12c","SPCC1020.02","SPAC23H3.08c","SPBC20F10.06"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2020-07-28"},{"uniquename":"PMID:22646093","title":"A homeobox protein Phx1 regulates long-term survival and meiotic sporulation in Schizosaccharomyces pombe.","citation":"BMC Microbiol 2012 May 30;12:86","abstract":"In the fission yeast Schizosaccharomyces pombe, the phx1+ (pombe homeobox) gene was initially isolated as a multi-copy suppressor of lysine auxotrophy caused by depletion of copper/zinc-containing superoxide dismutase (CuZn-SOD). Overproduction of Phx1 increased the synthesis of homocitrate synthase, the first enzyme in lysine biosynthetic pathway, which is labile to oxidative stress. Phx1 has a well conserved DNA-binding domain called homeodomain at the N-terminal region and is predicted to be a transcription factor in S. pombe. However, its role has not been revealed in further detail. Here we examined its expression pattern and the phenotype of its null mutant to get clues on its function.\nFluorescence from the Phx1-GFP expressed from a chromosomal fusion gene demonstrated that it is localized primarily in the nucleus, and is distinctly visible during the stationary phase. When we replaced the N-terminal homeobox domain of Phx1 with the DNA binding domain of Pap1, a well-characterized transcription factor, the chimeric protein caused the elevation of transcripts from Pap1-dependent genes such as ctt1+ and trr1+, suggesting that Phx1 possesses transcriptional activating activity when bound to DNA. The amount of phx1+ transcripts sharply increased as cells entered the stationary phase and was maintained at high level throughout the stationary phase. Nutrient shift down to low nitrogen or carbon sources caused phx1+ induction during the exponential phase, suggesting that cells need Phx1 for maintenance function during nutrient starvation. The Δphx1 null mutant showed decreased viability in long-term culture, whereas overproduction of Phx1 increased viability. Decrease in long-term survival was also observed for Δphx1 under N- or C-starved conditions. In addition, Δphx1 mutant was more sensitive to various oxidants and heat shock. When we examined sporulation of the Δphx1/Δphx1 diploid strain, significant decrease in the formation of meiotic spores was observed.\nPhx1 is a transcriptional regulator whose synthesis is elevated during stationary phase and by nutrient starvation in S. pombe. It supports long-term survival and stress tolerance against oxidation and heat, and plays a key role in the formation of meiotic spores.","doi":"10.1186/1471-2180-12-86","authors":"Kim JY, Kwon ES, Roe JH","authors_abbrev":"Kim JY et al.","pubmed_publication_date":"30 May 2012","pubmed_entrez_date":"2012-06-01","publication_year":"2012","canto_session_key":"86972f489e91b2d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-10-05 17:30:01","canto_approved_date":"2024-09-03 15:14:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-14 12:57:02","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC32A11.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-05"},{"uniquename":"PMID:7876244","title":"Transport of metal-binding peptides by HMT1, a fission yeast ABC-type vacuolar membrane protein.","citation":"J Biol Chem 1995 Mar 03;270(9):4721-8","abstract":"The Schizosaccharomyces pombe hmt1 gene encodes an ABC (ATP-binding cassette)-type protein essential for Cd2+ tolerance. Immunoblot analysis of subcellular fractions indicates that the native HMT1 polypeptide is associated with the vacuolar membrane. Vacuolar membrane vesicles were purified from strains that hyperproduce, or are deficient in, the HMT1 protein. In vitro transport of radiolabeled substrates by these vesicles indicates that HMT1 is an ATP-dependent transporter of phytochelatins, the metal-chelating peptides involved in heavy metal tolerance of plants and certain fungi. Vacuolar vesicles containing HMT1 are capable of taking up both apo-phytochelatins and phytochelatin-Cd2+ complexes. HMT1 activity is sensitive to antibodies directed against this protein and to vanadate, but not to inhibitors affecting the vacuolar proton ATPase or ionophores that abolish the pH gradient across the vacuolar membrane. Vacuolar uptake of Cd2+ and of a glutathione conjugate were also observed, but are not attributable to HMT1. These studies highlight the importance of the yeast vacuole in detoxification of xenobiotics.","authors":"Ortiz DF, Ruscitti T, McCue KF, Ow DW","authors_abbrev":"Ortiz DF et al.","pubmed_publication_date":"03 Mar 1995","pubmed_entrez_date":"1995-03-03","publication_year":"1995","canto_session_key":"679b3d676f7d8b74","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-09 11:47:57","canto_approved_date":"2022-08-30 07:05:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-31 07:21:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-09"},{"uniquename":"PMID:9601606","title":"New nuclear functions for calmodulin.","citation":"Cell Calcium 1998;23(2-3):115-21","abstract":"The data reported here summarize a series of results which reveal new functions for nuclear calmodulin (CaM). The addition of CaM inhibitors to cultures of proliferating NRK cells blocked the activity of the cyclin-dependent protein kinases 4 (cdk4) and 2 (cdk2), which are enzymes implicated in the progression of G1 and in the onset of DNA replication, respectively. CaM modulates the activity of cdk4 by regulating the nuclear location of both cdk4 and cyclin D, its associated regulatory subunit. By using CaM-affinity chromatography, we have recently identified two new nuclear CaM-binding proteins: (i) the protein La/SSB, which is an autoantigen implicated in several autoimmune diseases such as lupus erythematosus and Sjögren's syndrome (since La/SSB participates in the process of transcription mediated by RNA polymerase III, CaM could be involved in the regulation of this process); and (ii) the protein SAP145, a member of the spliceosome-associated proteins (SAPs) which is a subunit of the splicing factor SF3(b). This finding suggests the involvement of CaM in pre-mRNA splicing. Finally, a screening for new CaM-binding proteins in the fission yeast performed by using the phage display analysis, revealed that several nucleolar-ribosomal proteins associate to CaM, suggesting that CaM modulates ribosomal assembly and/or function.","authors":"Agell N, Aligué R, Alemany V, Castro A, Jaime M, Pujol MJ, Rius E, Serratosa J, Taulés M, Bachs O","authors_abbrev":"Agell N et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-05-28","publication_year":"1998","canto_session_key":"7f0773b219ae4ce8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-12-09 21:43:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-09 21:43:00","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-12-09"},{"uniquename":"PMID:21289066","title":"Elimination of a specific histone H3K14 acetyltransferase complex bypasses the RNAi pathway to regulate pericentric heterochromatin functions.","citation":"Genes Dev 2011 Feb 01;25(3):214-9","abstract":"In Schizosaccharomyces pombe, the RNAi pathway is required for the formation of pericentric heterochromatin, proper chromosome segregation, and repression of pericentric meiotic recombination. Here we demonstrate that, when the activity of the histone H3 Lys 14 (H3K14) acetyltransferase Mst2 is eliminated, the RNAi machinery is no longer required for pericentric heterochromatin functions. We further reveal that reducing RNA polymerase II recruitment to pericentric regions is essential for maintaining heterochromatin in the absence of RNAi.","doi":"10.1101/gad.1993611","authors":"Reddy BD, Wang Y, Niu L, Higuchi EC, Marguerat SB, Bähler J, Smith GR, Jia S","authors_abbrev":"Reddy BD et al.","pubmed_publication_date":"01 Feb 2011","pubmed_entrez_date":"2011-02-04","publication_year":"2011","canto_session_key":"a6dda9b018758e69","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-04-04 06:29:33","canto_approved_date":"2020-06-29 06:46:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-26 21:43:02","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.09","SPAC18G6.02c","SPAC17G8.13c","SPAC140.03","SPCC188.13c","SPCC663.12","SPAC2F7.04","SPAC6F6.09","SPCC736.11","SPBC16G5.13","SPAC13G7.07","SPBP8B7.28c","SPBC17D11.04c","SPCC1393.05"],"gene_count":14,"ltp_gene_count":13,"approved_date":"2015-04-04"},{"uniquename":"PMID:9118252","title":"Regulation of meiosis in fission yeast.","citation":"Cell Struct Funct 1996 Oct;21(5):431-6","abstract":"The fission yeast Schizosaccharomyces pombe initiates sexual development under starved conditions. Nutritional starvation decreases the level of intracellular cAMP. This decrease induces expression of the ste11 gene, which encodes a key transcription factor for genes required for mating and meiosis. Mutational analyses of S. pombe genes encoding components of the cAMP cascade have shown that S. pombe cells stay in the mitotic cell cycle as long as the level of cAMP-dependent protein kinase activity is high, but are committed to mating and meiosis if this activity is lowered. To initiate meiosis in S. pombe, a protein kinase encoded by pat1 (also called ran1) should be inactivated. This inactivation results from deprivation of nutrients via a cascade of expression of genes including ste11. The mei2 gene encodes a factor indispensable for the initiation of meiosis, and its expression is regulated directly by Ste11. If Pat1 kinase is intact, it blocks Mei2 function. Mei2 is required at two distinct stages of meiosis, once prior to premeiotic DNA synthesis and then prior to the first meiotic division (meiosis I). Mei2 is an RNA-binding protein, and forms a complex with a specific RNA species to promote meiosis I. This RNA species, named meiRNA, is polyadenylated but is unlikely to encode a protein product. It is essential for meiosis I, but not for either cell growth or premeiotic DNA synthesis. These observations unequivocally demonstrate that RNA plays a critical role in the control of meiosis.","authors":"Yamamoto M","authors_abbrev":"Yamamoto M","pubmed_publication_date":"Oct 1996","pubmed_entrez_date":"1996-10-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013004","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7190865","title":"Microfilaments and cytoplasmic microtubules in cell division cycle mutants of Schizosaccharomyces pombe.","citation":"Can J Microbiol 1980 Feb;26(2):250-4","abstract":"The occurrence of axial cytoplasmic microtubules (25 nm in diameter) and of microfilaments (7 nm in diameter) associated in bundles just below the plasma membrane of the yeast Schizosaccharomyces pombe is described. Both types of cytoplasmic filamentous structures were present in the cell division cycle mutant cdc 12-112 of this fungus incubated for 6 h at the restrictive temperature of 35 degrees C. Microtubules and microfilaments probably function in septum formation and (or) in the volume-related control of the terminal phenotype of the mutant.","authors":"Streiblová E, Girbardt M","authors_abbrev":"Streiblová E et al.","pubmed_publication_date":"Feb 1980","pubmed_entrez_date":"1980-02-01","publication_year":"1980","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35670055","title":"Coupling of mitochondrial population evolution to microtubule dynamics in fission yeast cells: a kinetic Monte Carlo study.","citation":"Soft Matter 2022 Jun 15;18(23):4483-4492","abstract":"Mitochondrial populations in cells are maintained by cycles of fission and fusion events. Perturbation of this balance has been observed in several diseases such as cancer and neurodegeneration. In fission yeast cells, the association of mitochondria with microtubules inhibits mitochondrial fission [Mehta  et al. ,  J. Biol. Chem. , 2019,  294 , 3385], illustrating the intricate coupling between mitochondria and the dynamic population of microtubules within the cell. In order to understand this coupling, we carried out kinetic Monte Carlo (KMC) simulations to predict the evolution of mitochondrial size distributions for different cases; wild-type cells, cells with short and long microtubules, and cells without microtubules. Comparisons are made with mitochondrial distributions reported in experiments with fission yeast cells. Using experimentally determined mitochondrial fission and fusion frequencies, simulations implemented without the coupling of microtubule dynamics predicted an increase in the mean number of mitochondria, equilibrating within 50 s. The mitochondrial length distribution in these models also showed a higher occurrence of shorter mitochondria, implying a greater tendency for fission, similar to the scenario observed in the absence of microtubules and cells with short microtubules. Interestingly, this resulted in overestimating the mean number of mitochondria and underestimating mitochondrial lengths in cells with wild-type and long microtubules. However, coupling mitochondria's fission and fusion events to the microtubule dynamics effectively captured the mitochondrial number and size distributions in wild-type and cells with long microtubules. Thus, the model provides greater physical insight into the temporal evolution of mitochondrial populations in different microtubule environments, allowing one to study both the short-time evolution as observed in the experiments (<5 minutes) as well as their transition towards a steady-state (>15 minutes). Our study illustrates the critical role of microtubules in mitochondrial dynamics and coupling microtubule growth and shrinkage dynamics is critical to predicting the evolution of mitochondrial populations within the cell.","doi":"10.1039/d2sm00155a","authors":"Choudhury S, Ananthanarayanan V, Ayappa KG","authors_abbrev":"Choudhury S et al.","pubmed_publication_date":"15 Jun 2022","pubmed_entrez_date":"2022-06-07","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-06-09 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3936021","title":"Dimeric tRNA gene arrangement in Schizosaccharomyces pombe allows increased expression of the downstream gene.","citation":"Nucleic Acids Res 1985 Dec 20;13(24):8739-47","abstract":"Three Schizosaccharomyces pombe dimeric tRNA genes, consisting of a tRNASer gene encoding a minor species with an intervening sequence followed by a tRNAMeti gene, have been described [Mao et al. (1980) Cell 21, 509-516; Hottinger et al. (1982) Mol. Gen. Genet. 188, 219-224; Willis et al. (1984) EMBO J. 3, 1573-1580]. We have examined the reason for the dimeric structure by comparing the transcriptional efficiencies and competitive abilities of the genes subcloned from the dimeric arrangement. Both of the subcloned genes are active in vivo in Saccharomyces cerevisiae, but only the tRNASer gene is efficiently transcribed in vitro. The tRNASer gene competes efficiently for transcription factors, while the tRNAMeti gene does so only weakly. Thus, it appears that the dimeric arrangement is required to support expression of the tRNAMeti gene. S. pombe genes encoding major species of tRNASer are transcribed considerably less efficiently than are the minor genes from the dimers, so coupling of the tRNAMeti gene to the minor species genes should lead to efficient production of tRNAMeti.","authors":"Hottinger-Werlen A, Schaack J, Lapointe J, Mao J, Nichols M, Söll D","authors_abbrev":"Hottinger-Werlen A et al.","pubmed_publication_date":"20 Dec 1985","pubmed_entrez_date":"1985-12-20","publication_year":"1985","canto_session_key":"046482844d5d3cbc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-02-01 23:51:29","canto_approved_date":"2019-02-01 23:51:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-01 23:51:24","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-02-01"},{"uniquename":"PMID:10381393","title":"Functionally homologous DNA replication genes in fission and budding yeast.","citation":"J Cell Sci 1999 Jul;112 ( Pt 14):2381-90","abstract":"The cdc18(+) gene of the fission yeast Schizosaccharomyces pombe is involved in the initiation of DNA replication as well as in coupling the S phase to mitosis. In this work, we show that the Saccharomyces cerevisiae CDC6 gene complements cdc18-K46 ts and cdc18 deletion mutant S. pombe strains. The budding yeast gene suppresses both the initiation and the checkpoint defects associated with the lack of cdc18(+). The Cdc6 protein interacts in vivo with Cdc2 kinase complexes. Interestingly, Cdc6 is an in vitro substrate for Cdc13/Cdc2 and Cig1/Cdc2, but not for Cig2/Cdc2-associated kinases. Overexpression of Cdc6 in fission yeast induces multiple rounds of S-phase in the absence of mitosis and cell division. This CDC6-dependent continuous DNA synthesis phenotype is independent of the presence of a functional cdc18(+) gene product and, significantly, requires only Cig2/Cdc2-associated kinase activity. Finally, these S. pombe over-replicating cells do not require any protein synthesis other than that of Cdc6. Our data strongly suggest that CDC6 and cdc18(+) are functional homologues and also support the idea that controls restricting genome duplication diverge in fission and budding yeast.","authors":"Sánchez M, Calzada A, Bueno A","authors_abbrev":"Sánchez M et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-06-25","publication_year":"1999","canto_session_key":"bbbfbbfa3508968e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-04-08 13:35:04","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-04-08 13:34:47","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC14C8.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-04-08"},{"uniquename":"PMID:18562672","title":"The fission yeast BLM homolog Rqh1 promotes meiotic recombination.","citation":"Genetics 2008 Jul;179(3):1157-67","abstract":"RecQ helicases are found in organisms as diverse as bacteria, fungi, and mammals. These proteins promote genome stability, and mutations affecting human RecQ proteins underlie premature aging and cancer predisposition syndromes, including Bloom syndrome, caused by mutations affecting the BLM protein. In this study we show that mutants lacking the Rqh1 protein of the fission yeast Schizosaccharomyces pombe, a RecQ and BLM homolog, have substantially reduced meiotic recombination, both gene conversions and crossovers. The relative proportion of gene conversions having associated crossovers is unchanged from that in wild type. In rqh1 mutants, meiotic DNA double-strand breaks are formed and disappear with wild-type frequency and kinetics, and spore viability is only moderately reduced. Genetic analyses and the wild-type frequency of both intersister and interhomolog joint molecules argue against these phenotypes being explained by an increase in intersister recombination at the expense of interhomolog recombination. We suggest that Rqh1 extends hybrid DNA and biases the recombination outcome toward crossing over. Our results contrast dramatically with those from the budding yeast ortholog, Sgs1, which has a meiotic antirecombination function that suppresses recombination events involving more than two DNA duplexes. These observations underscore the multiple recombination functions of RecQ homologs and emphasize that even conserved proteins can be adapted to play different roles in different organisms.","doi":"10.1534/genetics.108.088955","authors":"Cromie GA, Hyppa RW, Smith GR","authors_abbrev":"Cromie GA et al.","pubmed_publication_date":"Jul 2008","pubmed_entrez_date":"2008-06-20","publication_year":"2008","canto_session_key":"d5671d546397969f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24403609","title":"Role of turgor pressure in endocytosis in fission yeast.","citation":"Mol Biol Cell 2014 Mar;25(5):679-87","abstract":"Yeast and other walled cells possess high internal turgor pressure that allows them to grow and survive in the environment. This turgor pressure, however, may oppose the invagination of the plasma membrane needed for endocytosis. Here we study the effects of turgor pressure on endocytosis in the fission yeast Schizosaccharomyces pombe by time-lapse imaging of individual endocytic sites. Decreasing effective turgor pressure by addition of sorbitol to the media significantly accelerates early steps in the endocytic process before actin assembly and membrane ingression but does not affect the velocity or depth of ingression of the endocytic pit in wild-type cells. Sorbitol also rescues endocytic ingression defects of certain endocytic mutants and of cells treated with a low dose of the actin inhibitor latrunculin A. Endocytosis proceeds after removal of the cell wall, suggesting that the cell wall does not contribute mechanically to this process. These studies suggest that endocytosis is governed by a mechanical balance between local actin-dependent inward forces and opposing forces from high internal turgor pressure on the plasma membrane.","doi":"10.1091/mbc.E13-10-0618","authors":"Basu R, Munteanu EL, Chang F","authors_abbrev":"Basu R et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-01-10","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU008065","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33445779","title":"Conserved and Divergent Mechanisms That Control TORC1 in Yeasts and Mammals.","citation":"Genes (Basel) 2021 Jan 12;12(1)","abstract":"Target of rapamycin complex 1 (TORC1), a serine/threonine-protein kinase complex highly conserved among eukaryotes, coordinates cellular growth and metabolism with environmental cues, including nutrients and growth factors. Aberrant TORC1 signaling is associated with cancers and various human diseases, and TORC1 also plays a key role in ageing and lifespan, urging current active research on the mechanisms of TORC1 regulation in a variety of model organisms. Identification and characterization of the RAG small GTPases as well as their regulators, many of which are highly conserved from yeast to humans, led to a series of breakthroughs in understanding the molecular bases of TORC1 regulation. Recruitment of mammalian TORC1 (mTORC1) by RAGs to lysosomal membranes is a key step for mTORC1 activation. Interestingly, the RAG GTPases in fission yeast are primarily responsible for attenuation of TORC1 activity on vacuoles, the yeast equivalent of lysosomes. In this review, we summarize our current knowledge about the functions of TORC1 regulators on yeast vacuoles, and illustrate the conserved and divergent mechanisms of TORC1 regulation between yeasts and mammals.","doi":"10.3390/genes12010088","authors":"Morozumi Y, Shiozaki K","authors_abbrev":"Morozumi Y et al.","pubmed_publication_date":"12 Jan 2021","pubmed_entrez_date":"2021-01-15","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-01-17 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1551569","title":"Isolation and characterization of regulatory mutants from Schizosaccharomyces pombe involved in thiamine-regulated gene expression.","citation":"Genetics 1992 Mar;130(3):445-9","abstract":"Mutants from Schizosaccharomyces pombe deficient in the regulation of thiamine-repressible acid phosphatase have been isolated. Mutants expressing derepressed levels of the enzyme in the presence and absence of thiamine map in three genes, tnr1, tnr2 and tnr3. mRNA levels of the pho4 gene (coding for thiamine repressible acid phosphatase) and another thiamine-regulatable gene, thi3 (coding for a thiamine biosynthetic enzyme and corresponding to nmt1) are constitutively synthesized in the mutants. The mutants also exhibit constitutive thiamine transport which is thiamine repressible in wild type. The tnr3 mutants reveal a 10-20-fold higher intracellular thiamine level than tnr1 and tnr2 mutants and wild type. Mutants expressing repressed levels of thiamine-repressible acid phosphatase map in gene thi1. No or little amounts of pho4- and nmt1-specific mRNA can be detected. These mutants are impaired in thiamine uptake and are thiamine auxotrophic due to the inability to synthesize the thiazole moiety of the thiamine molecule. All tested tnr and thi1 alleles are recessive, and thi1 mutations are epistatic over tnr mutations. We assume that the thi1 and tnr genes are involved in thiamine-mediated transcription control.","authors":"Schweingruber AM, Fankhauser H, Dlugonski J, Steinmann-Loss C, Schweingruber ME","authors_abbrev":"Schweingruber AM et al.","pubmed_publication_date":"Mar 1992","pubmed_entrez_date":"1992-03-01","publication_year":"1992","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F12.05c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"EMBL:AB017604","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12050156","title":"Surplus zinc is handled by Zym1 metallothionein and Zhf endoplasmic reticulum transporter in Schizosaccharomyces pombe.","citation":"J Biol Chem 2002 Aug 16;277(33):30394-400","abstract":"Homeostatic mechanisms prevent the accumulation of free zinc in the cytoplasm, raising questions regarding where surplus zinc is stored and how it is delivered to and from these stores. A genetic screen for zinc hypersensitivity in Schizosaccharomyces pombe identified a missense mutation truncating Zhf, an endoplasmic reticulum transporter. These cells were approximately 5-fold more zinc-sensitive than other independent mutants. The targeted disruption of zhf prevented growth on low zinc medium and caused hypersensitivity to elevated zinc/cobalt but resistance to cadmium. The exposure to elevated zinc but not copper also promotes the accumulation of transcripts encoding a metallothionein designated Zym1. The Sty1 pathway is required for maximal zym1 expression but is not obligatory for zinc perception. The targeted disruption of zym1 impaired cadmium tolerance but only slightly impaired zinc tolerance, whereas zym1 overexpression substantially rescued zinc hypersensitivity of zhf(-) cells. Four equivalents of zinc were displaced from Zym1 by up to 12 equivalents of p-(hydroxymercuri)phenylsulphonate. Zym1 thiols react rapidly with 5,5'-dithiobis-(2-nitrobenzoic acid) compared with bacterial zinc metallothionein (6.8 and 0.2 x 10(-4) s(-1), respectively). Zym1 is unlike known fungal metallothioneins that are induced by and sequester copper but not zinc. Less zinc but normal cadmium was accumulated by zym1Delta, consistent with zinc sequestration by Zym1 in vivo.","authors":"Borrelly GP, Harrison MD, Robinson AK, Cox SG, Robinson NJ, Whitehall SK","authors_abbrev":"Borrelly GP et al.","pubmed_publication_date":"16 Aug 2002","pubmed_entrez_date":"2002-06-07","publication_year":"2002","canto_session_key":"6e903e61b25296eb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-12-15 12:41:36","canto_approved_date":"2026-03-14 14:14:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-14 20:48:39","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.07c","SPAC23C11.14","SPAC21E11.03c","SPAC22H10.13"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2023-12-15"},{"uniquename":"PMID:37694715","title":"A ubiquitin-proteasome pathway degrades the inner nuclear membrane protein Bqt4 to maintain nuclear membrane homeostasis.","citation":"J Cell Sci 2023 Oct 01;136(19)","abstract":"Aberrant accumulation of inner nuclear membrane (INM) proteins is associated with deformed nuclear morphology and mammalian diseases. However, the mechanisms underlying the maintenance of INM homeostasis remain poorly understood. In this study, we explored the degradation mechanisms of the INM protein Bqt4 in the fission yeast Schizosaccharomyces pombe. We have previously shown that Bqt4 interacts with the transmembrane protein Bqt3 at the INM and is degraded in the absence of Bqt3. Here, we reveal that excess Bqt4, unassociated with Bqt3, is targeted for degradation by the ubiquitin-proteasome system localized in the nucleus and Bqt3 antagonizes this process. The degradation process involves the Doa10 E3 ligase complex at the INM. Bqt4 is a tail-anchored protein and the Cdc48 complex is required for its degradation. The C-terminal transmembrane domain of Bqt4 was necessary and sufficient for proteasome-dependent protein degradation. Accumulation of Bqt4 at the INM impaired cell viability with nuclear envelope deformation, suggesting that quantity control of Bqt4 plays an important role in nuclear membrane homeostasis.","doi":"10.1242/jcs.260930","authors":"Le TK, Hirano Y, Asakawa H, Okamoto K, Fukagawa T, Haraguchi T, Hiraoka Y","authors_abbrev":"Le TK et al.","pubmed_publication_date":"01 Oct 2023","pubmed_entrez_date":"2023-09-11","publication_year":"2023","canto_session_key":"886d6f892477dd42","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Hirano","canto_first_approved_date":"2023-11-19 15:04:10","canto_approved_date":"2024-03-28 17:56:41","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-11-25 08:04:02","canto_added_date":"2023-09-12 00:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yasuhiro Hirano","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14F5.07","SPBC16G5.01","SPBC19C7.02","SPBP16F5.04","SPAC17C9.13c","SPCC594.07c","SPAC15A10.11","SPAC10F6.05c","SPAC167.07c","SPBC947.10","SPAC1565.08","SPBC2A9.04c","SPBC4.07c","SPAC3A12.03c","SPAC19D5.04","SPBC19C7.10","SPAC6F12.15c"],"gene_count":17,"ltp_gene_count":16,"approved_date":"2023-11-19"},{"uniquename":"PMID:2388837","title":"Isolation of a Schizosaccharomyces pombe homologue to the rat ribosomal protein, L7.","citation":"Nucleic Acids Res 1990 Aug 11;18(15):4590","abstract":"","authors":"Murray JM, Watts FZ","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"11 Aug 1990","pubmed_entrez_date":"1990-08-11","publication_year":"1990","canto_session_key":"a07468731cc1f6b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:41:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 13:42:57","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-25"},{"uniquename":"PMID:23504563","title":"Schizosaccharomyces pombe disaggregation machinery chaperones support Saccharomyces cerevisiae growth and prion propagation.","citation":"Eukaryot Cell 2013 May;12(5):739-45","abstract":"Hsp100 chaperones protect microorganisms and plants from environmental stress by cooperating with Hsp70 and its nucleotide exchange factor (NEF) and Hsp40 cochaperones to resolubilize proteins from aggregates. The Saccharomyces cerevisiae Hsp104 (Sc-Hsp104)-based disaggregation machinery also is essential for replication of amyloid-based prions. Escherichia coli ClpB can substitute for Hsp104 to propagate [PSI(+)] prions in yeast, but only if E. coli DnaK and GrpE (Hsp70 and NEF) are coexpressed. Here, we tested if the reported inability of Schizosaccharomyces pombe Hsp104 (Sp-Hsp104) to support [PSI(+)] propagation was due to similar species-specific chaperone requirements and find that Sp-Hsp104 alone supported propagation of three different yeast prions. Sp-Hsp70 and Sp-Fes1p (NEF) likewise functioned in place of their Sa. cerevisiae counterparts. Thus, chaperones of these long-diverged species possess conserved activities that function in processes essential for both cell growth and prion propagation, suggesting Sc. pombe can propagate its own prions. We show that curing by Hsp104 overexpression and inactivation can be distinguished and confirm the observation that, unlike Sc-Hsp104, Sp-Hsp104 cannot cure yeast of [PSI(+)] when it is overexpressed. These results are consistent with a view that mechanisms underlying prion replication and elimination are distinct.","doi":"10.1128/EC.00301-12","authors":"Reidy M, Sharma R, Masison DC","authors_abbrev":"Reidy M et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-03-19","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12675805","title":"A new Schizosaccharomyces pombe base excision repair mutant, nth1, reveals overlapping pathways for repair of DNA base damage.","citation":"Mol Microbiol 2003 Apr;48(2):465-80","abstract":"Endonuclease III (Nth) enzyme from Escherichia coli is involved in base excision repair of oxidised pyrimidine residues in DNA. The Schizosaccharomyces pombe Nth1 protein is a sequence and functional homologue of E. coli Nth, possessing both DNA glycosylase and apurinic/apyrimidinic (AP) lyase activity. Here, we report the construction and characterization of the S. pombe nth1 mutant. The nth1 mutant exhibited no enhanced sensitivity to oxidising agents, UV or gamma-irradiation, but was hypersensitive to the alkylating agent methyl methanesulphonate (MMS). Analysis of base excision from DNA exposed to [3H]methyl-N-nitrosourea showed that the purified Nth1 enzyme did not remove alkylated bases such as 3-methyladenine and 7-methylguanine whereas methyl-formamidopyrimidine was excised efficiently. The repair of AP sites in S. pombe has previously been shown to be independent of Apn1-like AP endonuclease activity, and the main reason for the MMS sensitivity of nth1 cells appears to be their lack of AP lyase activity. The nth1 mutant also exhibited elevated frequencies of spontaneous mitotic intrachromosomal recombination, which is a phenotype shared by the MMS-hypersensitive DNA repair mutants rad2, rhp55 and NER repair mutants rad16, rhp14, rad13 and swi10. Epistasis analyses of nth1 and these DNA repair mutants suggest that several DNA damage repair/tolerance pathways participate in the processing of alkylation and spontaneous DNA damage in S. pombe.","authors":"Osman F, Bjørås M, Alseth I, Morland I, McCready S, Seeberg E, Tsaneva I","authors_abbrev":"Osman F et al.","pubmed_publication_date":"Apr 2003","pubmed_entrez_date":"2003-04-05","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC330.01c","SPAC3G6.06c","SPBC3E7.08c","SPBC4F6.15c","SPBC649.03","SPAC3C7.03c","SPAC30D11.07"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:9760444","title":"Regulation of DNA damage inducible rhp51+ gene, a rec A homolog from Schizosaccharomyces pombe.","citation":"J Toxicol Sci 1998 Jul;23 Suppl 2:110-6","abstract":"","authors":"Park SD, Jin YH, Jang YK","authors_abbrev":"Park SD et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-10-07","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14299875","title":"[ALCOHOL DEHYDROGENASE MUTANTS OF SCHIZOSACCHAROMYCES POMBE].","citation":"Pathol Microbiol (Basel) 1965;28:50-7","abstract":"","authors":"MEGNET R","authors_abbrev":"MEGNET R","pubmed_publication_date":"1965","pubmed_entrez_date":"1965-01-01","publication_year":"1965","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3553962","title":"Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2.","citation":"Nature 1987 May 7;327(6117):31-5","abstract":"A human homologue of the cdc2 gene has been cloned by expressing a human cDNA library in fission yeast and selecting for clones that can complement a mutant of cdc2. The predicted protein sequence of the human homologue is very similar to that of the yeast cdc2 gene. These data indicate that elements of the mechanism by which the cell cycle is controlled are likely to be conserved between yeast and humans.","authors":"Lee MG, Nurse P","authors_abbrev":"Lee MG et al.","pubmed_publication_date":"7 May 1987","pubmed_entrez_date":"1987-05-07","publication_year":"1987","canto_session_key":"7a84091768f3438d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-02-08 20:48:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 19:45:35","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-08"},{"uniquename":"PMID:10704362","title":"The ran decathlon: multiple roles of Ran.","citation":"J Cell Sci 2000 Apr;113 ( Pt 7):1111-8","abstract":"The Ran GTPase system affects many cellular processes, including the regulation of cell cycle progression, nuclear envelope structure and function, and nucleocytoplasmic transport. The biochemical basis for the involvement of Ran in nuclear import and export has been well documented, but the direct targets of Ran in other cellular processes have not yet been identified. There is, however, mounting evidence that Ran directly affects at least some of these other cellular processes by mechanisms independent of its role in transport. In this Commentary we discuss evidence linking Ran to different aspects of cell function, and how these multiple facets of Ran's activity may relate to each other.","authors":"Sazer S, Dasso M","authors_abbrev":"Sazer S et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-03-08","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:10:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24047646","title":"Pom1 and cell size homeostasis in fission yeast.","citation":"Cell Cycle 2013 Oct 01;12(19):3228-36","abstract":"Cells sense their size and use this information to coordinate cell division with cell growth to maintain a constant cell size within a given population. A model has been proposed for cell size control in the rod-shaped cells of the fission yeast, Schizosaccharomyces pombe. This involves a protein localized to the cell ends, which inhibits mitotic activators in the middle of the cell in a cell size-dependent manner. This protein, Pom1, along with another tip-localized protein, Nif1, have been implicated as direct sensors of cell size controlling the onset of mitosis. Here we have investigated cell size variability and size homeostasis at the G 2/M transition, focusing on the role of pom1 and nif1. Cells deleted for either of these 2 genes show wild-type size homeostasis both in size variability analyses and size homeostasis experiments. This indicates that these genes do not have a critical role as direct cell size sensors in the control mechanism. Cell size homeostasis also seems to be independent of Cdc2-Tyr15 phosphorylation, suggesting that the size sensing mechanism in fission yeast may act through an unidentified pathway regulating CDK activity by an unknown mechanism.","doi":"10.4161/cc.26462","authors":"Wood E, Nurse P","authors_abbrev":"Wood E et al.","pubmed_publication_date":"01 Oct 2013","pubmed_entrez_date":"2013-09-20","publication_year":"2013","canto_session_key":"c7de46ee1570b585","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-06-08 23:16:01","canto_approved_date":"2024-04-03 10:17:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-29 15:03:04","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Jacky Hayles","community_curator":true,"annotation_count":11,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19F5.01c","SPBC23G7.04c","SPAC2F7.03c","SPBC11B10.09","SPAC57A10.02","SPCC18B5.03"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2018-06-08"},{"uniquename":"PMID:36650056","title":"Protein S-palmitoylation regulates different stages of meiosis in  Schizosaccharomyces pombe .","citation":"Life Sci Alliance 2023 Apr;6(4)","abstract":"Posttranslational protein S-palmitoylation regulates the localization and function of its target proteins involved in diverse cellular processes including meiosis. In this study, we demonstrate that S-palmitoylation mediated by Erf2-Erf4 and Akr1 palmitoylacyltransferases is required at multiple meiotic stages in the fission yeast  Schizosaccharomyces pombe  We find that S-palmitoylation by Erf2-Erf4 is required for Ras1 localization at the cell periphery to enrich at the cell conjugation site for mating pheromone response. In the absence of Erf2 or Erf4, mutant cells are sterile. A role of Akr1 S-palmitoylating the nuclear fusion protein Tht1 to function in karyogamy is identified. We demonstrate that S-palmitoylation stabilizes and localizes Tht1 to ER, interacting with Sey1 ER fusion GTPase for proper meiotic nuclear fusion. In  akr1 ,  tht1 , or  sey1  mutant, meiotic cells, haploid nuclei are unfused with subsequent chromosome segregation defects. Erf2-Erf4 has an additional substrate of the spore coat protein Isp3. In the absence of Erf2, Isp3 is mislocalized from the spore coat. Together, these results highlight the versatility of the cellular processes in which protein S-palmitoylation participates.","doi":"10.26508/lsa.202201755","authors":"Pham TV, Hsiao WY, Wang YT, Yeh SD, Wang SW","authors_abbrev":"Pham TV et al.","pubmed_publication_date":"Apr 2023","pubmed_entrez_date":"2023-01-17","publication_year":"2023","canto_session_key":"089bad866432ef28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shao-Win Wang","canto_first_approved_date":"2023-02-08 09:54:23","canto_approved_date":"2026-01-01 20:20:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-06 18:13:26","canto_added_date":"2023-01-19 01:15:05","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":22,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Shao-Win Wang","community_curator":true,"annotation_count":27,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F8.05","SPBC3H7.09","SPAC222.14c","SPAC23C4.08","SPBC691.01","SPAC13C5.03","SPAC17H9.09c","SPBC2F12.15c","SPBC13G1.07","SPAC3F10.07c","SPAC2F7.10"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2023-02-08"},{"uniquename":"PMID:25183833","title":"Holliday junction resolvases.","citation":"Cold Spring Harb Perspect Biol 2014 Sep 02;6(9):a023192","abstract":"Four-way DNA intermediates, called Holliday junctions (HJs), can form during meiotic and mitotic recombination, and their removal is crucial for chromosome segregation. A group of ubiquitous and highly specialized structure-selective endonucleases catalyze the cleavage of HJs into two disconnected DNA duplexes in a reaction called HJ resolution. These enzymes, called HJ resolvases, have been identified in bacteria and their bacteriophages, archaea, and eukaryotes. In this review, we discuss fundamental aspects of the HJ structure and their interaction with junction-resolving enzymes. This is followed by a brief discussion of the eubacterial RuvABC enzymes, which provide the paradigm for HJ resolvases in other organisms. Finally, we review the biochemical and structural properties of some well-characterized resolvases from archaea, bacteriophage, and eukaryotes.","doi":"10.1101/cshperspect.a023192","authors":"Wyatt HD, West SC","authors_abbrev":"Wyatt HD et al.","pubmed_publication_date":"02 Sep 2014","pubmed_entrez_date":"2014-09-04","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-05-17 00:19:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15157887","title":"The N-degron approach to create temperature-sensitive mutants in Schizosaccharomyces pombe.","citation":"Methods 2004 Jul;33(3):206-12","abstract":"Conditional mutants are a vital tool for analysis of gene function. The use of temperature-sensitive mutants in Schizosaccharomyces pombe has significantly promoted understanding of many cellular processes. A portable heat-inducible amino-terminal degron (N-degron) for conditional degradation of a gene product has been previously described in Saccharomyces cerevisiae. This paper describes the adaptation of the N-degron method to create temperature-sensitive (ts) mutants in S. pombe. A ts derivative of the mouse dihydrofolate reductase with an amino-terminal arginine (Arg-DHFR(ts)) previously described in S. cerevisiae was fused to the N-terminus of Bir1p, a nuclear protein involved in mitotic chromosome segregation in S. pombe. This fusion allele, referred to as bir1-td, conferred a chromosome segregation defect at 36 degrees C, as with previously described alleles of bir1. Deletion of the S. pombe E3 ubiquitin ligase (N-recognin), Ubr11p, reversed the temperature-dependent lethality of bir1-td, providing evidence for N-end rule mediated destruction of Bir1p. The methods we describe should therefore facilitate analysis of essential genes in fission yeast for which conditionally lethal mutants are unavailable.","authors":"Rajagopalan S, Liling Z, Liu J, Balasubramanian M","authors_abbrev":"Rajagopalan S et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11426866","title":"Multifunctional cytokinesis genes in Schizosaccharomyces pombe.","citation":"Acta Biol Hung 2001;52(2-3):315-23","abstract":"The proper division of cells is essential for the production of viable daughter cells. In plants and fungi, the dividing cell produces a cross-wall or septum that bisects the cytoplasm. For separation of the daughter cells, the septum has to be cleaved. To study the regulation of this process, we isolated mutants defective in septum cleavage. The mutants showed highly pleiotropic phenotypes and defined 17 novel genes. The deduced amino acid sequences of the products of the cloned genes exhibited homologies to various transcription regulators of other organisms. The homologies and the pleiotropic effects of the mutations on sexual development, stress response, mitotic stability, septum initiation and septum placement indicated that these genes affect cell separation indirectly, through multifunctional regulatory modules.","authors":"Sipiczki M, Grallert A, Zilahi E, Miklós I, Sziljágyi Z","authors_abbrev":"Sipiczki M et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-06-28","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15242615","title":"Positioning and elongation of the fission yeast spindle by microtubule-based pushing.","citation":"Curr Biol 2004 Jul 13;14(13):1181-6","abstract":"In eukaryotic cells, proper position of the mitotic spindle is necessary for successful cell division and development. We explored the nature of forces governing the positioning and elongation of the mitotic spindle in Schizosaccharomyces pombe. We hypothesized that astral microtubules exert mechanical force on the S. pombe spindle and thus help align the spindle with the major axis of the cell. Microtubules were tagged with green fluorescent protein (GFP) and visualized by two-photon microscopy. Forces were inferred both from time-lapse imaging of mitotic cells and, more directly, from mechanical perturbations induced by laser dissection of the spindle and astral microtubules. We found that astral microtubules push on the spindle poles in S. pombe, in contrast to the pulling forces observed in a number of other cell types. Further, laser dissection of the spindle midzone induced spindle collapse inward. This offers direct evidence in support of the hypothesis that spindle elongation is driven by the sliding apart of antiparallel microtubules in the spindle midzone. Broken spindles recovered and mitosis completed as usual. We propose a model of spindle centering and elongation by microtubule-based pushing forces.","authors":"Tolić-Nørrelykke IM, Sacconi L, Thon G, Pavone FS","authors_abbrev":"Tolić-Nørrelykke IM et al.","pubmed_publication_date":"13 Jul 2004","pubmed_entrez_date":"2004-07-10","publication_year":"2004","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24442611","title":"Endogenous U2·U5·U6 snRNA complexes in S. pombe are intron lariat spliceosomes.","citation":"RNA 2014 Mar;20(3):308-20","abstract":"Excision of introns from pre-mRNAs is mediated by the spliceosome, a multi-megadalton complex consisting of U1, U2, U4/U6, and U5 snRNPs plus scores of associated proteins. Spliceosome assembly and disassembly are highly dynamic processes involving multiple stable intermediates. In this study, we utilized a split TAP-tag approach for large-scale purification of an abundant endogenous U2·U5·U6 complex from Schizosaccharomyces pombe. RNAseq revealed this complex to largely contain excised introns, indicating that it is primarily ILS (intron lariat spliceosome) complexes. These endogenous ILS complexes are remarkably resistant to both high-salt and nuclease digestion. Mass spectrometry analysis identified 68, 45, and 43 proteins in low-salt-, high-salt-, and micrococcal nuclease-treated preps, respectively. The protein content of a S. pombe ILS complex strongly resembles that previously reported for human spliced product (P) and Saccharomyces cerevisiae ILS complexes assembled on single pre-mRNAs in vitro. However, the ATP-dependent RNA helicase Brr2 was either substoichiometric in low-salt preps or completely absent from high-salt and MNase preps. Because Brr2 facilitates spliceosome disassembly, its relative absence may explain why the ILS complex accumulates logarithmically growing cultures and the inability of S. pombe extracts to support in vitro splicing.","doi":"10.1261/rna.040980.113","authors":"Chen W, Shulha HP, Ashar-Patel A, Yan J, Green KM, Query CC, Rhind N, Weng Z, Moore MJ","authors_abbrev":"Chen W et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-01-21","publication_year":"2014","canto_session_key":"b013aa2ff18fcfa7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Weijun Chen","canto_first_approved_date":"2017-01-26 22:17:05","canto_approved_date":"2023-04-13 08:08:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-26 22:15:01","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Weijun Chen","community_curator":true,"annotation_count":45,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.11c","SPBC211.02c","SPAC22F8.10c","SPBC3E7.13c","SPAC22H12.04c","SPBC6B1.10","SPCP1E11.07c","SPAC1F7.13c","SPBC11G11.06c","SPAC1486.03c","SPAC1F3.09","SPAC144.11","SPAC3A12.11c","SPAC12G12.03","SPAC664.05","SPCC794.09c","SPBC32H8.12c","SPBC32F12.11","SPBC19C2.14","SPAC26A3.04","SPBC1289.11","SPAC30D11.09","SPBC16H5.10c","SPCC1795.11","SPAC31G5.18c","SPBC337.06c","SPCC550.02c","SPBC354.12","SPAC1071.07c","SPBC646.02","SPBC31F10.11c","SPCC576.08c","SPCC364.02c","SPBC28F2.04c","SPBC215.12","SPBP22H7.07","SPBC3E7.14","SPCC16C4.13c","SPAC27F1.09c","SPCC1682.14","SPCC1739.13","SPBC18H10.10c","SPBC16A3.18","SPBC32F12.05c","SPAC57A10.03","SPAC27D7.07c","SPAC17A2.08c","SPAC2C4.03c","SPAC18G6.14c","SPAC9.03c","SPBP8B7.03c","SPAC12G12.04","SPBC106.18","SPBC16G5.14c","SPBC1861.08c","SPAC26A3.08","SPAC3G9.03","SPAC17A5.03","SPAPJ698.03c","SPBC24C6.11","SPAC521.05","SPCC188.11","SPAC57A7.04c","SPAC644.12","SPBC4B4.05","SPAC10F6.02c","SPAC4F8.12c","SPAC29A4.08c"],"gene_count":68,"ltp_gene_count":44,"approved_date":"2017-01-26"},{"uniquename":"PMID:26075619","title":"Deletion of Genes Encoding Arginase Improves Use of \"Heavy\" Isotope-Labeled Arginine for Mass Spectrometry in Fission Yeast.","citation":"PLoS One 2015;10(6):e0129548","abstract":"The use of \"heavy\" isotope-labeled arginine for stable isotope labeling by amino acids in cell culture (SILAC) mass spectrometry in the fission yeast Schizosaccharomyces pombe is hindered by the fact that under normal conditions, arginine is extensively catabolized in vivo, resulting in the appearance of \"heavy\"-isotope label in several other amino acids, most notably proline, but also glutamate, glutamine and lysine. This \"arginine conversion problem\" significantly impairs quantification of mass spectra. Previously, we developed a method to prevent arginine conversion in fission yeast SILAC, based on deletion of genes involved in arginine catabolism. Here we show that although this method is indeed successful when (13)C6-arginine (Arg-6) is used for labeling, it is less successful when (13)C6(15)N4-arginine (Arg-10), a theoretically preferable label, is used. In particular, we find that with this method, \"heavy\"-isotope label derived from Arg-10 is observed in amino acids other than arginine, indicating metabolic conversion of Arg-10. Arg-10 conversion, which severely complicates both MS and MS/MS analysis, is further confirmed by the presence of (13)C5(15)N2-arginine (Arg-7) in arginine-containing peptides from Arg-10-labeled cells. We describe how all of the problems associated with the use of Arg-10 can be overcome by a simple modification of our original method. We show that simultaneous deletion of the fission yeast arginase genes car1+ and aru1+ prevents virtually all of the arginine conversion that would otherwise result from the use of Arg-10. This solution should enable a wider use of heavy isotope-labeled amino acids in fission yeast SILAC.","doi":"10.1371/journal.pone.0129548","authors":"Borek WE, Zou J, Rappsilber J, Sawin KE","authors_abbrev":"Borek WE et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-06-16","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-06-17 00:20:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25375240","title":"The kinetochore protein Kis1/Eic1/Mis19 ensures the integrity of mitotic spindles through maintenance of kinetochore factors Mis6/CENP-I and CENP-A.","citation":"PLoS One 2014;9(11):e111905","abstract":"Microtubules play multiple roles in a wide range of cellular phenomena, including cell polarity establishment and chromosome segregation. A number of microtubule regulators have been identified, including microtubule-associated proteins and kinases, and knowledge of these factors has contributed to our molecular understanding of microtubule regulation of each relevant cellular process. The known regulators, however, are insufficient to explain how those processes are linked to one another, underscoring the need to identify additional regulators. To find such novel mechanisms and microtubule regulators, we performed a screen that combined genetics and microscopy for fission yeast mutants defective in microtubule organization. We isolated approximately 900 mutants showing defects in either microtubule organization or the nuclear envelope, and these mutants were classified into 12 categories. We particularly focused on one mutant, kis1, which displayed spindle defects in early mitosis. The kis1 mutant frequently failed to assemble a normal bipolar spindle. The responsible gene encoded a kinetochore protein, Mis19 (also known as Eic1), which localized to the interface of kinetochores and spindle poles. We also found that the inner kinetochore proteins Mis6/CENP-I and Cnp1/CENP-A were delocalized from kinetochores in the kis1 cells and that kinetochore-microtubule attachment was defective. Another mutant, mis6, also displayed similar spindle defects. We conclude that Kis1 is required for inner kinetochore organization, through which Kis1 ensures kinetochore-microtubule attachment and spindle integrity. Thus, we propose an unexpected relationship between inner kinetochore organization and spindle integrity.","doi":"10.1371/journal.pone.0111905","authors":"Hirai H, Arai K, Kariyazono R, Yamamoto M, Sato M","authors_abbrev":"Hirai H et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-11-07","publication_year":"2014","canto_session_key":"c061f382feb3bbd0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hayato Hirai","canto_first_approved_date":"2017-08-08 07:23:13","canto_approved_date":"2026-01-11 18:31:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-02 08:40:33","canto_added_date":"2014-11-08 01:15:26","annotation_curators":[{"name":"Hayato Hirai","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27B12.02","SPCC736.14","SPBC11B10.09","SPAC1687.20c","SPBC20F10.06","SPCC970.12","SPCC1672.10","SPBC1105.17"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2017-08-08"},{"uniquename":"PMID:28245054","title":"Fission yeast APC/C activators Slp1 and Fzr1 sequentially trigger two consecutive nuclear divisions during meiosis.","citation":"FEBS Lett 2017 Apr;591(7):1029-1040","abstract":"In meiosis, two rounds of nuclear division occur consecutively without DNA replication between the divisions. We isolated a fission yeast mutant in which the nucleus divides only once to generate two spores, as opposed to four, in meiosis. In this mutant, we found that the initiation codon of the slp1 +  gene is converted to ATA, producing a reduced amount of Slp1. As a member of the Fizzy family of anaphase-promoting complex/cyclosome (APC/C) activators, Slp1 is essential for vegetative growth; however, the mutant allele shows a phenotype only in meiosis. Slp1 insufficiency delays degradation of maturation-promoting factor at the first meiotic division, and another APC/C activator, Fzr1, which acts late in meiosis, terminates meiosis immediately after the delayed first division to produce two viable spores.","doi":"10.1002/1873-3468.12612","authors":"Chikashige Y, Yamane M, Okamasa K, Osakada H, Tsutsumi C, Nagahama Y, Fukuta N, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"Apr 2017","pubmed_entrez_date":"2017-03-01","publication_year":"2017","canto_session_key":"b377ec5799dccdc3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-03-02 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC5D6.08c","SPBC1198.12","SPAC821.08c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU009846","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9868582","title":"Ruptured fission yeast walls. Structural discontinuities related to the cell cycle.","citation":"Cell Biochem Biophys 1998;29(3):263-79","abstract":"Distributions of rupture sites of fission yeast cells ruptured by glass beads have been related to a new morphometric analysis. As shown previously (Johnson et al., Cell Biophysics, 1995), ruptures were not randomly distributed nor was their distribution dictated by geometry, rather, ruptures at the extensile end were related to cell length just as the rate of extension is related to cell length. The extension patterns of early log, mid-log, late log, and stationary phase cells from suspension cultures were found to approximate the linear growth patterns of Kubitschek and Clay (1986). The median length of cells was found to decline through the log phase in an unbalanced manner.","authors":"Piombo S, Calleja GB, Yoo BY, Johnson BF","authors_abbrev":"Piombo S et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-12-30","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4600142","title":"Chromosome-like particles during meiosis in fission yeast.","citation":"Arch Mikrobiol 1974 Feb 13;95(4):319-23","abstract":"","authors":"Egel R, Pentzos-Daponte A","authors_abbrev":"Egel R et al.","pubmed_publication_date":"13 Feb 1974","pubmed_entrez_date":"1974-02-13","publication_year":"1974","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30321377","title":"Proteomic profiling and functional characterization of post-translational modifications of the fission yeast RNA exosome.","citation":"Nucleic Acids Res 2018 Nov 30;46(21):11169-11183","abstract":"The RNA exosome is a conserved multi-subunit complex essential for processing and degradation of several types of RNAs. Although many of the functions of the RNA exosome are well established, whether the activity of this complex is regulated remains unclear. Here we performed a proteomic analysis of the RNA exosome complex purified from Schizosaccharomyces pombe and identified 39 post-translational modifications (PTMs), including phosphorylation, methylation, and acetylation sites. Interestingly, most of the modifications were identified in Dis3, a catalytic subunit of the RNA exosome, as well as in the exosome-associated RNA helicase, Mtr4. Functional analysis of selected PTM sites using modification-deficient and -mimetic versions of exosome subunits revealed substitutions that affected cell growth and exosome functions. Notably, our results suggest that site-specific phosphorylation in the catalytic center of Dis3 and in the helical bundle domain of Mtr4 control their activity. Our findings support a view in which post-translational modifications fine-tune exosome activity and add a layer of regulation to RNA degradation.","doi":"10.1093/nar/gky915","authors":"Telekawa C, Boisvert FM, Bachand F","authors_abbrev":"Telekawa C et al.","pubmed_publication_date":"30 Nov 2018","pubmed_entrez_date":"2018-10-16","publication_year":"2018","canto_session_key":"9c5610a31550884e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-10-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23D3.02","SPAC1805.11c","SPBC29A3.12","SPAC1782.09c","SPCC24B10.09","SPAC1B3.13","SPBC56F2.02","SPBC2G2.07c","SPAC343.02","SPBC1604.09c","SPAC1F7.13c","SPAC24C9.11","SPCP31B10.08c","SPCC1739.02c","SPBC577.02","SPAC22A12.12c","SPBC16E9.10c","SPAC12G12.06c","SPBC18H10.14","SPAC29A4.03c","SPBC106.19","SPBC8D2.05c","SPAC30D11.12","SPAC3G9.15c","SPBC2F12.03c","SPAC26A3.04","SPAC664.05","SPCC417.08","SPAC17C9.03","SPBC19F5.02c","SPAC26H5.05","SPCC4B3.15","SPAC1834.03c","SPAC2C4.11c","SPBC776.17","SPAC926.09c","SPAC22F3.04","SPBC2F12.02c","SPCP1E11.08","SPAC1610.02c","SPBC27B12.04c","SPBC887.14c","SPAC227.07c","SPAC3H1.09c","SPBC902.04","SPBC30D10.12c","SPBC32H8.13c","SPAC3G9.09c","SPAC1F7.02c","SPAC3H5.07","SPBC16G5.10","SPBC29B5.03c","SPBC776.08c","SPAC9.03c","SPAC22F8.09","SPBC23E6.07c","SPBC11C11.03","SPAC3H5.05c","SPAC2F7.14c","SPAC23C11.02c","SPBC4F6.06","SPAC1093.05","SPAC890.02c","SPCC736.12c","SPAC25G10.02","SPAPJ760.02c","SPBC800.04c","SPAC23C4.15","SPCC1739.07","SPAC23A1.11","SPAC521.05","SPBC2D10.10c","SPAC1071.07c","SPBP4H10.15","SPCP31B10.07","SPCC1223.07c","SPBC216.05","SPCC1183.07","SPAC15E1.03","SPBC1271.13","SPCC306.09c","SPBP8B7.20c","SPAC25G10.08","SPBC1604.06c","SPAC664.06","SPBC23E6.04c","SPAC18G6.06","SPBC28E12.04","SPBP8B7.16c","SPBP22H7.02c","SPAC926.08c","SPAC140.02","SPBC8D2.03c","SPCC1682.12c","SPCC126.05c","SPAC6F12.16c","SPBC13E7.04","SPCC1840.11","SPAC24H6.09","SPAC589.09","SPBC713.04c","SPBC25B2.05","SPCC16C4.07","SPBC839.04","SPAC17A5.14","SPCC1259.01c","SPCC895.07","SPBP35G2.07","SPAC22E12.13c","SPAC2F7.15","SPBC776.01","SPAC24B11.12c","SPCC16A11.17","SPAC23G3.02c","SPCC330.09","SPAC1687.03c","SPBC1921.01c","SPCC622.09","SPBC16G5.14c","SPAC22A12.07c","SPBC19C2.01","SPBC83.14c","SPCC16A11.05c","SPAC1486.11","SPBC13G1.09","SPBC14C8.14c","SPBC1709.05","SPBC16D10.11c","SPCC1393.03","SPCC757.08","SPBC1709.08","SPAC4C5.02c","SPAC24C9.10c","SPCC297.03","SPBC17D11.05","SPAC23C11.03","SPBC3F6.04c","SPBC646.10c","SPBC2F12.07c","SPAC20H4.01","SPBPB7E8.02","SPBC839.13c","SPAC26A3.07c","SPAC513.01c","SPBC1105.12","SPBC14F5.09c","SPBC20F10.05","SPCC5E4.07","SPCC16C4.09","SPBC365.04c","SPBP8B7.03c","SPBC17D1.03c","SPAC23A1.08c","SPAC664.04c","SPAC4F10.05c","SPAC806.03c","SPBC32F12.11","SPAC1F3.01","SPBC685.07c","SPAC19G12.06c","SPAC664.08c","SPBC1347.02","SPBC29A3.16","SPAC959.03c","SPAC1687.06c","SPBC115.01c","SPCC1235.02","SPBP35G2.04c","SPCC285.03","SPBC26H8.08c","SPCC1919.08c","SPCC31H12.04c","SPCC1795.11","SPACUNK4.11c","SPBC3H7.08c","SPCC613.05c","SPAC13G6.02c","SPBP22H7.07","SPAC1834.08","SPBC18H10.12c","SPAC23G3.06","SPBC17G9.07","SPAC4F8.04","SPAC6B12.15","SPBC1289.17","SPCC1620.14c","SPBC19G7.10c","SPCC364.03","SPBC839.05c","SPCC13B11.01","SPAC23A1.10","SPAC13A11.02c","SPCC576.08c","SPBC216.07c","SPAC644.17c","SPAC6G9.09c","SPAC18G6.07c","SPAC16E8.06c","SPAC20G8.09c","SPBC1105.19","SPBC28F2.12","SPCC74.05","SPBC19G7.03c","SPAC105.01c","SPBC16C6.02c","SPAC1142.04","SPCP1E11.11","SPCC306.07c","SPBC651.01c","SPBC4F6.04","SPAC2G11.02","SPBC211.08c","SPBC428.19c","SPAC31G5.15","SPBC887.07","SPCC14G10.02","SPCC18.12c","SPCC126.11c","SPAC3H8.03","SPBC4C3.05c","SPAC1B9.03c","SPAC16E8.15","SPAC4G9.17c","SPBC1815.01","SPCC1682.14","SPAC17H9.02","SPBP8B7.10c","SPAC4A8.11c","SPBC839.15c","SPAC1250.03","SPAC6F6.06c","SPBC21C3.20c","SPBC56F2.12","SPAC22F3.08c","SPAC12G12.02","SPBC11C11.07","SPBC12C2.12c","SPCC1494.06c","SPBC14F5.04c","SPBC1685.09","SPBC25B2.07c","SPAC589.10c","SPAC6F6.07c","SPAC56E4.04c","SPBC660.11","SPAC4F8.05c","SPAC9G1.03c","SPCC338.16","SPCC16C4.13c","SPCC1739.13","SPAC19D5.05c","SPBC1289.07c","SPAC607.02c","SPBC1539.10","SPBC26H8.10","SPAC6G9.02c","SPAC890.08","SPBC691.04","SPBP16F5.03c","SPAPB1A10.06c","SPAC17H9.05","SPAC1805.17","SPBC1539.03c","SPAC17A5.03","SPBC2F12.04","SPBC56F2.04","SPAC7D4.14c","SPCC736.14","SPBC31F10.14c","SPBC1711.05","SPAC18G6.14c","SPAC3G6.04","SPBC6B1.04","SPAC607.03c","SPAC1071.10c","SPBC11G11.03","SPAC3G9.10c","SPAC2F3.03c","SPAC3G9.03","SPAC31A2.07c","SPAC3A12.10","SPAC1006.03c","SPAC4F10.09c","SPAC1805.13","SPBC1711.06","SPBC29A3.06","SPCC16C4.15","SPCC1827.05c","SPAC2G11.11c","SPBC16G5.04","SPBC31E1.06","SPCC830.03","SPBC11C11.09c","SPAC222.06","SPBC3D6.15","SPAC110.01","SPBC776.11","SPAC57A7.06","SPBC21B10.03c","SPCC1183.08c","SPAC19B12.04","SPBC1A4.07c","SPAC3H5.10","SPBC11B10.04c","SPBC4F6.14","SPBC24C6.02","SPAC22G7.05","SPBPJ4664.02","SPAC1420.04c","SPBC19C2.07","SPAC11E3.15","SPCC1672.07","SPAC328.04","SPBC18H10.13","SPCC1322.11","SPBC3B9.14c","SPAC31G5.03","SPCC16A11.02","SPCC4G3.06c","SPAC1B3.10c","SPAC12G12.04","SPAC22A12.04c","SPAC29A4.04c","SPBC800.06","SPAC1565.05","SPAC4F10.06","SPAC4F8.02c","SPAC5D6.01","SPBC17G9.10","SPBC1D7.04","SPBC106.18","SPBC19F5.05c","SPBC29A3.14c","SPAC17H9.20","SPBC17D1.06","SPBP4H10.13","SPBC1921.03c","SPBC20F10.01","SPBC32H8.04c","SPBC543.06c","SPAPB17E12.13","SPBC4F6.07c","SPBC83.08","SPBC887.03c","SPAC144.11","SPBC16C6.11","SPCC18.14c","SPAC22H12.04c","SPCC1795.07","SPAC212.11","SPAC11E3.11c","SPAC31A2.08","SPBC1773.09c","SPCC895.09c","SPAC9G1.02","SPCC338.07c","SPAP27G11.13c","SPCC794.09c","SPCC1442.19","SPBP23A10.07","SPAC1F8.07c","SPAC19A8.07c","SPBC14C8.16c","SPCC417.07c","SPBC19C2.09","SPBC691.02c","SPAC227.02c","SPBC9B6.06","SPBP35G2.08c","SPAC27E2.10c","SPBC21H7.04","SPBC29A3.04","SPBC337.12","SPAC12G12.13c","SPAC16C9.06c","SPAC2E1P5.05","SPAC4F8.06","SPCC4G3.14","SPCC622.18"],"gene_count":379,"ltp_gene_count":0},{"uniquename":"PMID:7183688","title":"Patterns of protein synthesis during the cell cycle of the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1982 Dec;58:263-85","abstract":"The rate of protein synthesis through the cell cycle of Schizosaccharomyces pombe has been determined from the incorporation of pulses of [3H]tryptophan in synchronous cultures prepared by selection in an elutriating rotor. This selection procedure caused minimal perturbations as judged by asynchronous control cultures, which had also been put through the rotor. The rate of synthesis showed a periodic pattern rather than a smooth exponential increase. There was a sharp increase in the rate at an 'acceleration point' at about 0.9 of the cycle. Model-fitting by a novel procedure suggests that the average single cell has an increasing rate of protein synthesis for the first 60% of the cycle and a constant rate for the remaining 40%. The same pattern was shown in less extensive experiments with [3H]leucine and [3H]phenylalanine. It was also shown in a series of size mutants, which indicates that the pattern is not size-related, in contrast to earlier work on the rates of synthesis of messenger RNA. However, one large mutant (cdc 2.M35r20) had a significantly earlier acceleration point. Care was taken to justify the assumption that the rate of incorporation of tryptophan was a valid measure of the rate of protein synthesis. A tryptophan auxotroph was used to eliminate the problem of endogenous supply and the size of the metabolic pool was measured through the cycle. This pool did not show cell-cycle related fluctuations. An operational model of the pools is presented.","authors":"Creanor J, Mitchison JM","authors_abbrev":"Creanor J et al.","pubmed_publication_date":"Dec 1982","pubmed_entrez_date":"1982-12-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11511341","title":"The making and breaking of sister chromatid cohesion.","citation":"Cell 2001 Jul 27;106(2):137-40","abstract":"","authors":"Cohen-Fix O","authors_abbrev":"Cohen-Fix O","pubmed_publication_date":"27 Jul 2001","pubmed_entrez_date":"2001-08-21","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30426027","title":" Pap1    +   confers microtubule damage resistance to  mut2a , an extragenic suppressor of the  rad26:4A  allele in  S. pombe .","citation":"Mol Biol Res Commun 2018 Sep;7(3):97-106","abstract":"The DNA structure checkpoint protein Rad26 ATRIP  is also required for an interphase microtubule damage response. This checkpoint delays spindle pole body separation and entry into mitosis following treatment of cells with microtubule poisons. This checkpoint requires cytoplasmic Rad26 ATRIP , which is compromised by the  rad26:4A  allele that inhibits cytoplasmic accumulation of Rad26 ATRIP  following microtubule damage. The  rad26::4a  allele also disrupts minichromosome stability and cellular morphology, suggesting that the interphase microtubule damage checkpoint pathway operates in an effort to maintain chromosome stability and proper cell shape. To identify other proteins of the Rad26-dependent interphase microtubule damage response, we used ultra violet (UV) radiation to identify extragenic interaction suppressors of the  rad26::4A  growth defect on microtubule poisons. One suppressor mutation, which we named  mut2a , permitted growth of  rad26:4A  cells on MBC media and conferred sensitivity to a microtubulin poison upon genetic outcross. In an attempt to clone this interaction suppressor using a genomic library complementation strategy, we instead isolated  pap1   +  as an extracopy suppressor of the  mut2a  growth defect. We discuss the mechanism by which  pap1   +  overexpression may allow growth of  mut2a  cells in conditions that destabilize microtubules.","doi":"10.22099/mbrc.2018.29705.1324","authors":"Paliwal S, Wheeler R, D Wolkow T","authors_abbrev":"Paliwal S et al.","pubmed_publication_date":"Sep 2018","pubmed_entrez_date":"2018-11-15","publication_year":"2018","canto_session_key":"473a412b898cb1c3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-11-16 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1783.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23080121","title":"Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair.","citation":"Nucleic Acids Res 2012 Dec;40(22):11435-49","abstract":"The Mre11 complex (Mre11-Rad50-Nbs1 or MRN) binds double-strand breaks where it interacts with CtIP/Ctp1/Sae2 and ATM/Tel1 to preserve genome stability through its functions in homology-directed repair, checkpoint signaling and telomere maintenance. Here, we combine biochemical, structural and in vivo functional studies to uncover key properties of Mre11-W243R, a mutation identified in two pediatric cancer patients with enhanced ataxia telangiectasia-like disorder. Purified human Mre11-W243R retains nuclease and DNA binding activities in vitro. X-ray crystallography of Pyrococcus furiosus Mre11 indicates that an analogous mutation leaves the overall Mre11 three-dimensional structure and nuclease sites intact but disorders surface loops expected to regulate DNA and Rad50 interactions. The equivalent W248R allele in fission yeast allows Mre11 to form an MRN complex that efficiently binds double-strand breaks, activates Tel1/ATM and maintains telomeres; yet, it causes hypersensitivity to ionizing radiation and collapsed replication forks, increased Rad52 foci, defective Chk1 signaling and meiotic failure. W248R differs from other ataxia telangiectasia-like disorder analog alleles by the reduced stability of its interaction with Rad50 in cell lysates. Collective results suggest a separation-of-function mutation that disturbs interactions amongst the MRN subunits and Ctp1 required for DNA end processing in vivo but maintains interactions sufficient for Tel1/ATM checkpoint and telomere maintenance functions.","doi":"10.1093/nar/gks954","authors":"Limbo O, Moiani D, Kertokalio A, Wyman C, Tainer JA, Russell P","authors_abbrev":"Limbo O et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-10-20","publication_year":"2012","canto_session_key":"68ae1fabd9900b1b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2017-05-04 16:14:00","canto_approved_date":"2017-05-04 16:14:00","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2013-06-18 18:42:16","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":83,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.09c","SPBC216.05","SPBC29A10.05","SPCC1259.13","SPBC543.03c","SPAC13C5.07","SPCC622.08c","SPAC3G6.06c","SPAC19G12.06c","SPCC338.08","SPCC23B6.03c","SPAC1556.01c"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2017-05-04"},{"uniquename":"PMID:29899117","title":"Ccp1 modulates epigenetic stability at centromeres and affects heterochromatin distribution in  Schizosaccharomyces pombe .","citation":"J Biol Chem 2018 Aug 03;293(31):12068-12080","abstract":"Distinct chromatin organization features, such as centromeres and heterochromatin domains, are inherited epigenetically. However, the mechanisms that modulate the accuracy of epigenetic inheritance, especially at the individual nucleosome level, are not well-understood. Here, using ChIP and next-generation sequencing (ChIP-Seq), we characterized Ccp1, a homolog of the histone chaperone Vps75 in budding yeast that functions in centromere chromatin duplication and heterochromatin maintenance in fission yeast ( Schizosaccharomyces pombe ). We show that Ccp1 is enriched at the central core regions of the centromeres. Of note, among all histone chaperones characterized, deletion of the  ccp1  gene uniquely reduced the rate of epigenetic switching, manifested as position effect variegation within the centromeric core region (CEN-PEV). In contrast, gene deletion of other histone chaperones either elevated the PEV switching rates or did not affect centromeric PEV. Ccp1 and the kinetochore components Mis6 and Sim4 were mutually dependent for centromere or kinetochore association at the proper levels. Moreover, Ccp1 influenced heterochromatin distribution at multiple loci in the genome, including the subtelomeric and the pericentromeric regions. We also found that Gar2, a protein predominantly enriched in the nucleolus, functions similarly to Ccp1 in modulating the epigenetic stability of centromeric regions, although its mechanism remained unclear. Together, our results identify Ccp1 as an important player in modulating epigenetic stability and maintaining proper organization of multiple chromatin domains throughout the fission yeast genome.","doi":"10.1074/jbc.RA118.003873","authors":"Lu M, He X","authors_abbrev":"Lu M et al.","pubmed_publication_date":"03 Aug 2018","pubmed_entrez_date":"2018-06-15","publication_year":"2018","canto_session_key":"9f8b7fbbd3337ea2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-10-08 09:55:24","canto_approved_date":"2020-10-08 09:55:24","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-10-01 16:22:28","canto_added_date":"2018-06-16 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":55,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.11c","SPAC140.02","SPAC664.01c","SPBC16C6.10","SPAC4G9.06c","SPCC970.10c","SPBC36B7.08c","SPAC6G9.03c","SPBC409.04c","SPBC342.06c","SPCC548.05c","SPBP22H7.09c","SPAC26H5.03","SPAC11H11.05c","SPAC1687.20c","SPBC18E5.03c","SPAC1805.07c","SPCC364.06","SPBC27.02c","SPCC622.16c","SPBC29A10.03c","SPBC1105.17","SPAC25H1.06","SPBC31F10.13c","SPBC11C11.03","SPBC15D4.03","SPAC27F1.06c","SPCC1020.02","SPAC57A10.09c"],"gene_count":29,"ltp_gene_count":21,"approved_date":"2020-10-08"},{"uniquename":"PMID:22910366","title":"Organellar mechanosensitive channels in fission yeast regulate the hypo-osmotic shock response.","citation":"Nat Commun 2012;3:1020","abstract":"A key molecule of sensing machineries essential for survival upon hypo-osmotic shock is the mechanosensitive channel. The bacterial mechanosensitive channel MscS functions directly for this purpose by releasing cytoplasmic solutes out of the cell, whereas plant MscS homologues are found to function in chloroplast organization. Here we show that the fission yeast MscS homologues, designated Msy1 and Msy2, participate in the hypo-osmotic shock response by a mechanism different from that operated by the bacterial MscS. Upon hypo-osmotic shock, msy2(-) and msy1(-) msy2(-) cells display greater cell swelling than wild-type cells and undergo cell death. Cell swelling precedes an intracellular Ca(2+) increase, which was greater in msy1(-) and msy1(-) msy2(-) cells than in wild-type cells. Fluorescent microscopy showed that Msy1 and Msy2 localize mainly to the endoplasmic reticulum. These observations suggest that organellar Msy1 and Msy2 regulate intracellular Ca(2+) and cell volume for survival upon hypo-osmotic shock.","doi":"10.1038/ncomms2014","authors":"Nakayama Y, Yoshimura K, Iida H","authors_abbrev":"Nakayama Y et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-23","publication_year":"2012","canto_session_key":"8ffe6ded62ad4ebc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-05-23 16:08:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-04-29 12:23:33","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1183.11","SPAC2C4.17c","SPBC2F12.09c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2013-04-29"},{"uniquename":"PMID:30782298","title":"Thiamine leads to oxidative stress resistance via regulation of the glucose metabolism.","citation":"Cell Mol Biol (Noisy-le-grand) 2019 Jan 31;65(1):73-77","abstract":"Thiamine diphosphate (ThDP) is an essential cofactor for important enzymes in carbohydrate, amino acid and lipid metabolisms. It is also known that thiamine plays an important role in stress response of some organisms. In this study, we focused on the effect of thiamine on stress responses triggered by various stress agents. For this purpose, firstly, viability of Schizosaccharomyces pombe cell cultures was examined under oxidative, osmotic and heat stresses. The highest tolerance observed in cell viability due to the presence of extracellular thiamine (1.5 µM) was found only against oxidative stress. Then, enzyme activity of catalase and superoxide dismutase (SOD) involved in antioxidant defense mechanism and the expression analysis of genes encoding enzymes related to glucose metabolism and stress response pathways were investigated under oxidative stress. In this condition, it was not observed any difference in SOD and catalase activities, and their gene expressions due to the presence of thiamine, whereas the upregulation of pyruvate dehydrogenase (pdb1), transketolase (SPBC2G5.05), fructose-1,6-bis-phosphatase (fbp1) and the downregulation of pyruvate decarboxylase (pdc201) were observed. In conclusion, these findings suggest that extracellular thiamine leading to oxidative stress resistance have an impact on the regulation of glucose metabolism by shifting the energy generation from fermentation to respiration.","authors":"Kartal B, Palabiyik B","authors_abbrev":"Kartal B et al.","pubmed_publication_date":"31 Jan 2019","pubmed_entrez_date":"2019-02-21","publication_year":"2019","canto_session_key":"1037f652724b29bc","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_session_submitted_date":"2019-03-08 13:02:05","canto_added_date":"2019-02-22 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34897509","title":"Analysis of Eukaryotic lincRNA Sequences Indicates Signatures of Hindered Translation Linked to Selection Pressure.","citation":"Mol Biol Evol 2022 Feb 03;39(2)","abstract":"Long intergenic noncoding RNAs (lincRNAs) represent a large fraction of transcribed loci in eukaryotic genomes. Although classified as noncoding, most lincRNAs contain open reading frames (ORFs), and it remains unclear why cytoplasmic lincRNAs are not or very inefficiently translated. Here, we analyzed signatures of hindered translation in lincRNA sequences from five eukaryotes, covering a range of natural selection pressures. In fission yeast and Caenorhabditis elegans, that is, species under strong selection, we detected significantly shorter ORFs, a suboptimal sequence context around start codons for translation initiation, and trinucleotides (\"codons\") corresponding to less abundant tRNAs than for neutrally evolving control sequences, likely impeding translation elongation. For human, we detected signatures for cell-type-specific hindrance of lincRNA translation, in particular codons in abundant cytoplasmic lincRNAs corresponding to lower expressed tRNAs than control codons, in three out of five human cell lines. We verified that varying tRNA expression levels between cell lines are reflected in the amount of ribosomes bound to cytoplasmic lincRNAs in each cell line. We further propose that codons at ORF starts are particularly important for reducing ribosome-binding to cytoplasmic lincRNA ORFs. Altogether, our analyses indicate that in species under stronger selection lincRNAs evolved sequence features generally hindering translation and support cell-type-specific hindrance of translation efficiency in human lincRNAs. The sequence signatures we have identified may improve predicting peptide-coding and genuine noncoding lincRNAs in a cell type.","doi":"10.1093/molbev/msab356","authors":"Brümmer A, Dreos R, Marques AC, Bergmann S","authors_abbrev":"Brümmer A et al.","pubmed_publication_date":"03 Feb 2022","pubmed_entrez_date":"2021-12-13","publication_year":"2022","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2021-12-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16371129","title":"Distinct modes of DNA damage response in S. pombe G0 and vegetative cells.","citation":"Genes Cells 2006 Jan;11(1):13-27","abstract":"Upon nitrogen-starvation, mostly G2 vegetative (VE) fission yeast cells promote two rounds of division and enter the G0 state with 1C DNA via an uncommitted G1. Whilst G0 cells are permanently arrested, they keep viability through recycling the intracellular nitrogen. We here show that, whilst the DNA damages are efficiently repaired in G0 cells, neither Chk1 activation nor Cdc2 implication for Crb2 (53BP1 like) do not occur. ATR-like Rad3 and non-hyperphosphorylated Crb2 participate the repair processes in G0 cells that are more sensitive to UV and gamma-ray than in VE cells. The sensitivity like in VE cells is restored after replication in the nitrogen-replenished medium, suggesting that the damage hyper-sensitive nature of G0 cells is due to the error-prone repair for single DNA duplex chromosome. The double-strand break (DSB) repair in G0 cells required Pku80, one of non-homologous end joining (NHEJ) proteins. S. pombe G0 cells upon DNA damages thus respond distinctively from VE cells in regard with regulation of checkpoint proteins and the mode of repair that is dependent upon the use of NHEJ.","authors":"Mochida S, Yanagida M","authors_abbrev":"Mochida S et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2005-12-24","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36089751","title":"Schizosaccharomyces pombe Sls1 is primarily required for cox1 mRNA translation.","citation":"Yeast 2022 Oct;39(10):521-534","abstract":"Mitochondrial DNA (mtDNA) encodes essential subunits of the oxidative phosphorylation (OXPHOS) complexes; thus, the expression of mtDNA-encoded genes is essential for the synthesis of adenosine triphosphate. However, factors involved in mitochondrial translation have not been fully characterized. In this study, we characterized Schizosaccharomyces pombe Sls1, which has sequence similarity to Saccharomyces cerevisiae Sls1 that is required for the translation of all mtDNA-encoded messenger RNAs (mRNAs). Deletion of S. pombe sls1 severely impaired the growth of the cells on a rich medium containing the nonfermentable carbon source glycerol, which requires mitochondrial respiration. We found that the translation of mtDNA-encoded Cox1, the largest subunit of the cytochrome c oxidase complex, was severely impaired in Δsls1 cells. Deletion of S. pombe sls1 also resulted in a barely detectable steady-state level of mature cox1 mRNA. RNA immunoprecipitation showed that S. pombe Sls1 interacts with cox1 mRNA. Sucrose gradient sedimentation analysis revealed that S. pombe Sls1 is associated with the small subunit of mitochondrial ribosomes. Our results suggest that unlike S. cerevisiae Sls1, S. pombe Sls1 is primarily required for the accumulation and translation of cox1 mRNA.","doi":"10.1002/yea.3813","authors":"Wang Y, Luo Y, Huang Y","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"Oct 2022","pubmed_entrez_date":"2022-09-12","publication_year":"2022","canto_session_key":"9129b9f4cd235aec","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-15 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPMIT.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17046992","title":"Fission yeast Tor2 promotes cell growth and represses cell differentiation.","citation":"J Cell Sci 2006 Nov 01;119(Pt 21):4475-85","abstract":"The fission yeast Schizosaccharomyces pombe is an excellent model system in which to study the coordination of cell growth and cell differentiation. In the presence of nutrients, fission yeast cells grow and divide; in the absence of nutrients, they stop growing and undergo cell differentiation. The molecular mechanisms underlying this response are not fully understood. Here, we demonstrate that Tor2, a fission yeast member of the TOR protein kinase family, is central to controlling the switch between cell growth and cell differentiation in response to nutrient availability. Tor2 controls cell growth and ribosome biogenesis by regulating ribosomal protein gene expression. We have found that Tor2 has an additional function in repressing sexual differentiation. Tor2 overexpression strongly represses mating, meiosis and sporulation efficiency, whereas Tor2 inactivation has the opposite effect, leading to cell differentiation, regardless of the nutritional conditions. This newly revealed function of Tor2 appears to operate by interfering with the functions of the transcription factor Ste11 and the meiosis-promoting RNA-binding protein Mei2. Thus, our data reveal a unique regulatory function of the Tor pathway - ensuring that growth and cell differentiation become mutually exclusive and that the choice between them depends on environmental conditions.","authors":"Alvarez B, Moreno S","authors_abbrev":"Alvarez B et al.","pubmed_publication_date":"01 Nov 2006","pubmed_entrez_date":"2006-10-19","publication_year":"2006","canto_session_key":"5e362e900b991f0d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-07 16:12:20","canto_approved_date":"2026-01-31 15:31:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-07 16:11:25","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPBC32F12.09","SPBC32C12.02","SPBC2F12.04","SPAC144.11","SPAC57A7.11","SPBC216.07c","SPAC144.13c","SPBC119.04","SPBC21B10.05c","SPBC12C2.02c","SPBC19C2.05","SPBC30D10.10c"],"gene_count":13,"ltp_gene_count":10,"approved_date":"2017-02-07"},{"uniquename":"PMID:39012625","title":"Arp2/3-dependent endocytosis ensures Cdc42 oscillations by removing Pak1-mediated negative feedback.","citation":"J Cell Biol 2024 Sep 02;223(10)","abstract":"The GTPase Cdc42 regulates polarized growth in most eukaryotes. In the bipolar yeast Schizosaccharomyces pombe, Cdc42 activation cycles periodically at sites of polarized growth. These periodic cycles are caused by alternating positive feedback and time-delayed negative feedback loops. At each polarized end, negative feedback is established when active Cdc42 recruits the Pak1 kinase to prevent further Cdc42 activation. It is unclear how Cdc42 activation returns to each end after Pak1-dependent negative feedback. We find that disrupting branched actin-mediated endocytosis disables Cdc42 reactivation at the cell ends. Using experimental and mathematical approaches, we show that endocytosis-dependent Pak1 removal from the cell ends allows the Cdc42 activator Scd1 to return to that end to enable reactivation of Cdc42. Moreover, we show that Pak1 elicits its own removal via activation of endocytosis. These findings provide a deeper insight into the self-organization of Cdc42 regulation and reveal previously unknown feedback with endocytosis in the establishment of cell polarity.","doi":"10.1083/jcb.202311139","authors":"Harrell MA, Liu Z, Campbell BF, Chinsen O, Hong T, Das M","authors_abbrev":"Harrell MA et al.","pubmed_publication_date":"02 Sep 2024","pubmed_entrez_date":"2024-07-16","publication_year":"2024","canto_session_key":"86f9dd6401c5e32f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Maitreyi Das","canto_first_approved_date":"2024-08-01 09:19:33","canto_approved_date":"2024-08-01 09:19:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-27 19:07:07","canto_added_date":"2024-07-16 23:25:05","annotation_curators":[{"name":"Maitreyi Das","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":11,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.03","SPAC24H6.09","SPAC11H11.06","SPAC22H10.07","SPAC16E8.09","SPAC630.03","SPBC1604.14c","SPBC146.13c","SPBC354.13","SPCC895.05","SPBC28E12.03","SPBC1778.06c"],"gene_count":12,"ltp_gene_count":7,"approved_date":"2024-08-01"},{"uniquename":"PMID:7877997","title":"A mutation in the RCC1-related protein pim1 results in nuclear envelope fragmentation in fission yeast.","citation":"Proc Natl Acad Sci U S A 1995 Feb 28;92(5):1436-40","abstract":"Members of the RCC1 protein family are chromatin-associated guanine nucleotide exchange factors that have been implicated in diverse cellular processes in various organisms, yet no consensus has been reached as to their primary biological role. The fission yeast Schizosaccharomyces pombe, a single-celled eukaryote, provides an in vivo system in which to study the RCC1/Ran switch by using a temperature-sensitive mutant in the RCC1-related protein pim1. Mitotic entry in the pim1-d1ts mutant is normal, but mitotic exit leads to the accumulation of cells arrested with a medial septum and condensed chromosomes. Although the yeast nuclear envelope normally remains intact throughout the cell cycle, we found a striking fragmentation of the nuclear envelope in the pim1-d1ts mutant following mitosis. This resulted in chromatin that was no longer compartmentalized and an accumulation of pore-containing membranes in the cytoplasm. The development of this terminal phenotype was dependent on the passage of cells through mitosis and was coincident with the loss of viability. We propose that pim1 is required for the reestablishment of nuclear structure following mitosis in fission yeast.","authors":"Demeter J, Morphew M, Sazer S","authors_abbrev":"Demeter J et al.","pubmed_publication_date":"28 Feb 1995","pubmed_entrez_date":"1995-02-28","publication_year":"1995","canto_session_key":"e5f9d7f1e2a15ac3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-02-09 19:01:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-03 10:07:15","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC557.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-03"},{"uniquename":"PMID:14643429","title":"Checkpoint responses to replication stalling: inducing tolerance and preventing mutagenesis.","citation":"Mutat Res 2003 Nov 27;532(1-2):59-73","abstract":"Replication mutants often exhibit a mutator phenotype characterized by point mutations, single base frameshifts, and the deletion or duplication of sequences flanked by homologous repeats. Mutation in genes encoding checkpoint proteins can significantly affect the mutator phenotype. Here, we use fission yeast (Schizosaccharomyces pombe) as a model system to discuss the checkpoint responses to replication perturbations induced by replication mutants. Checkpoint activation induced by a DNA polymerase mutant, aside from delay of mitotic entry, up-regulates the translesion polymerase DinB (Polkappa). Checkpoint Rad9-Rad1-Hus1 (9-1-1) complex, which is loaded onto chromatin by the Rad17-Rfc2-5 checkpoint complex in response to replication perturbation, recruits DinB onto chromatin to generate the point mutations and single nucleotide frameshifts in the replication mutator. This chain of events reveals a novel checkpoint-induced tolerance mechanism that allows cells to cope with replication perturbation, presumably to make possible restarting stalled replication forks. Fission yeast Cds1 kinase plays an essential role in maintaining DNA replication fork stability in the face of DNA damage and replication fork stalling. Cds1 kinase is known to regulate three proteins that are implicated in maintaining replication fork stability: Mus81-Eme1, a hetero-dimeric structure-specific endonuclease complex; Rqh1, a RecQ-family helicase involved in suppressing inappropriate recombination during replication; and Rad60, a protein required for recombinational repair during replication. These Cds1-regulated proteins are thought to cooperatively prevent mutagenesis and maintain replication fork stability in cells under replication stress. These checkpoint-regulated processes allow cells to survive replication perturbation by preventing stalled replication forks from degenerating into deleterious DNA structures resulting in genomic instability and cancer development.","authors":"Kai M, Wang TS","authors_abbrev":"Kai M et al.","pubmed_publication_date":"27 Nov 2003","pubmed_entrez_date":"2003-12-04","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR019190","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC685.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26739115","title":"Label-free cell cycle analysis for high-throughput imaging flow cytometry.","citation":"Nat Commun 2016 Jan 07;7:10256","abstract":"Imaging flow cytometry combines the high-throughput capabilities of conventional flow cytometry with single-cell imaging. Here we demonstrate label-free prediction of DNA content and quantification of the mitotic cell cycle phases by applying supervised machine learning to morphological features extracted from brightfield and the typically ignored darkfield images of cells from an imaging flow cytometer. This method facilitates non-destructive monitoring of cells avoiding potentially confounding effects of fluorescent stains while maximizing available fluorescence channels. The method is effective in cell cycle analysis for mammalian cells, both fixed and live, and accurately assesses the impact of a cell cycle mitotic phase blocking agent. As the same method is effective in predicting the DNA content of fission yeast, it is likely to have a broad application to other cell types.","doi":"10.1038/ncomms10256","authors":"Blasi T, Hennig H, Summers HD, Theis FJ, Cerveira J, Patterson JO, Davies D, Filby A, Carpenter AE, Rees P","authors_abbrev":"Blasi T et al.","pubmed_publication_date":"07 Jan 2016","pubmed_entrez_date":"2016-01-08","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-01-21 01:15:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6059025","title":"Analysis of the mosaicism induced by hydroxylamine and nitrous acid in Schizosaccharomyces pombe.","citation":"Mutat Res 1967;4(4):441-7","abstract":"","authors":"Guglielminetti R, Bonatti S, Loprieno N, Abbondandolo A","authors_abbrev":"Guglielminetti R et al.","pubmed_publication_date":"1967","pubmed_entrez_date":"1967-07-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006804","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15506938","title":"Cell cycle-regulated transcription in fission yeast.","citation":"Biochem Soc Trans 2004 Dec;32(Pt 6):967-72","abstract":"A fundamental process in biology is the mechanism by which cells duplicate and divide to produce two identical daughter cells. The fission yeast, Schizosaccharomyces pombe, has proved to be an excellent model organism to study the role that gene expression plays in this process. The basic paradigm emerging is that a number of groups of genes are expressed in successive waves at different cell cycle times. Transcription of a particular group is controlled by a common DNA motif present in each gene's promoter, bound by a transcription factor complex. Each motif and transcription factor complex is specific to the time in the cell cycle when the group of genes is expressed. Examples of this are the MBF (MCB-binding factor)/MCB (MluI cell cycle box) system controlling gene expression at the start of S-phase, and PBF (PCB-binding factor)/PCB (Pombe cell cycle box) regulation of transcription at the end of mitosis. In some cases, these transcription control systems also operate during the alternative form of cell division, meiosis.","authors":"McInerny CJ","authors_abbrev":"McInerny CJ","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-10-28","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1448087","title":"The fission yeast genes pyp1+ and pyp2+ encode protein tyrosine phosphatases that negatively regulate mitosis.","citation":"Mol Cell Biol 1992 Dec;12(12):5571-80","abstract":"We have used degenerate oligonucleotide probes based on sequences conserved among known protein tyrosine phosphatases (PTPases) to identify two Schizosaccharomyces pombe genes encoding PTPases. We previously described the cloning of pyp1+ (S. Ottilie, J. Chernoff, G. Hannig, C. S. Hoffman, and R. L. Erikson, Proc. Natl. Acad. Sci. USA 88:3455-3459, 1991), and here we describe a second gene, called pyp2+. The C terminus of each protein contains sequences conserved in the apparent catalytic domains of all known PTPases. Disruption of pyp2+ results in viable cells, as was the case for pyp1+, whereas disruption of pyp2+ and pyp1+ results in synthetic lethality. Overexpression of either pyp1+ or pyp2+ in wild-type strains leads to a delay in mitosis but is suppressed by a wee1-50 mutation at 35 degrees C or a cdc2-1w mutation. A pyp1 disruption suppresses the temperature-sensitive lethality of a cdc25-22 mutation. Our data suggest that pyp1+ and pyp2+ act as negative regulators of mitosis upstream of the wee1+/mik1+ pathway.","authors":"Ottilie S, Chernoff J, Hannig G, Hoffman CS, Erikson RL","authors_abbrev":"Ottilie S et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"293cbd0b3d79a817","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-03-20 16:04:45","canto_approved_date":"2019-10-26 12:44:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-06-27 12:20:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.01","SPAC24H6.05","SPCC18B5.03","SPAC26F1.10c","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-03-20"},{"uniquename":"PMID:9685478","title":"Characterization of Schizosaccharomyces pombe Rad2 protein, a FEN-1 homolog.","citation":"Nucleic Acids Res 1998 Aug 15;26(16):3645-50","abstract":"FEN-1 proteins are a family of nucleases essential for lagging strand DNA synthesis. A gene with sequence similarity to FEN-1 protein-encoding genes, rad2 +, has been identified in Schizosaccharomyces pombe . We report the overexpression, purification, and character-ization of the putative S.pombe FEN-1 homolog, Rad2p. A GST-Rad2p fusion protein was over-expressed in Saccharomyces cerevisiae and purified to near homogeneity by GST affinity chromatography. Although Rad2p had been previously classified as a putative FEN-1 protein based on amino acid homology, there has been no biochemical evidence demonstrating flap endonuclease activity. DNA cleavage analysis of several different oligodeoxynucleotide structuresindicates that GST-Rad2p possesses both 5'-flap endonuclease and 5'-->3' double-stranded DNA exo-nuclease activities. GST-Rad2p incises a 5'-flap and a 5'-pseudo-Y structure one base 3' of the branch point in the duplex region and also degrades double-stranded DNA. This is the first report on the biochemical characterization of S.pombe Rad2p. The potential roles of Rad2p in DNA excision repair and other nucleic acid reactions are discussed.","authors":"Alleva JL, Doetsch PW","authors_abbrev":"Alleva JL et al.","pubmed_publication_date":"15 Aug 1998","pubmed_entrez_date":"1998-08-01","publication_year":"1998","canto_session_key":"2c94f8a9fd49f5ed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-14 13:49:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-04-14 13:49:10","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-14"},{"uniquename":"PMID:15509865","title":"The p150-Glued Ssm4p regulates microtubular dynamics and nuclear movement in fission yeast.","citation":"J Cell Sci 2004 Nov 01;117(Pt 23):5543-56","abstract":"During vegetative growth of the fission yeast Schizosaccharomyces pombe, microtubules nucleate from multiple microtubule organising centres (MTOCs) close to the nucleus, polymerising until they reach the end of the cell and then shrinking back to the cell centre. In response to mating pheromone, S. pombe undergoes a morphological switch from a vegetative to a shmooing growth pattern. The switch in growth mode is paralleled by a switch in microtubular dynamics. Microtubules nucleate mostly from a single MTOC and pull on the ends of the cell to move the nucleus back and forth. This movement continues after cellular and nuclear fusion in the zygote and is important to ensure correct chromosome pairing, recombination and segregation during meiosis. Here we show that Ssm4p, a p150-Glued protein, is induced specifically in response to pheromone and is required for this nuclear movement. Ssm4p is associated with the cytoplasmic dynein complex and together with the CLIP-170 homologue Tip1p regulates dynein heavy chain localisation. We also show that Ssm4p collaborates with Tip1p in establishing the shmooing microtubular array.","authors":"Niccoli T, Yamashita A, Nurse P, Yamamoto M","authors_abbrev":"Niccoli T et al.","pubmed_publication_date":"01 Nov 2004","pubmed_entrez_date":"2004-10-29","publication_year":"2004","canto_session_key":"348a4b2740f9819e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-09 16:40:37","canto_approved_date":"2022-05-12 10:07:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-11 14:47:37","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPAC1805.08","SPAC27D7.13c","SPBC646.17c","SPAC3C7.12"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-03-09"},{"uniquename":"PMID:11805113","title":"Functional interaction of MutY homolog with proliferating cell nuclear antigen in fission yeast, Schizosaccharomyces pombe.","citation":"J Biol Chem 2002 Apr 05;277(14):11853-8","abstract":"The MutY homolog (MYH) is responsible for removing adenines misincorporated on a template DNA strand containing G or 7,8-dihydro-8-oxoguanine (8-oxoG) and thus preventing G:C to T:A mutations. Human MYH has been shown to interact physically with human proliferating cell nuclear antigen (hPCNA). Here, we report that a similar interaction between SpMYH and SpPCNA occurs in the fission yeast Schizosaccharomyces pombe. Binding of SpMYH to SpPCNA was not observed when phenylalanine 444 in the PCNA binding motif of SpMYH was replaced with alanine. The F444A mutant of SpMYH expressed in yeast cells had normal adenine glycosylase and DNA binding activities. However, expression of this mutant form of SpMYH in a SpMYHDelta cell could not reduce the mutation frequency of the cell to the normal level. Moreover, SpMYH interacted with hPCNA, and SpPCNA interacted with hMYH but not with F518A/F519A mutant hMYH containing mutations in its PCNA binding motif. Although the SpMYHDelta cells expressing hMYH had partially reduced mutation frequency, the F518A/F519A mutant hMYH could not reduce the mutation frequency of SpMYHDelta cells. Thus, the interaction between SpMYH and SpPCNA is important for SpMYH biological function in mutation avoidance.","authors":"Chang DY, Lu AL","authors_abbrev":"Chang DY et al.","pubmed_publication_date":"05 Apr 2002","pubmed_entrez_date":"2002-01-24","publication_year":"2002","canto_session_key":"95939fd434aef229","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-02-29 14:39:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-02-29 14:39:33","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPAC26A3.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-02-29"},{"uniquename":"PMID:34806750","title":"Near-infrared imaging in fission yeast using a genetically encoded phycocyanobilin biosynthesis system.","citation":"J Cell Sci 2021 Dec 15;134(24)","abstract":"Near-infrared fluorescent protein (iRFP) is a bright and stable fluorescent protein with near-infrared excitation and emission maxima. Unlike the other conventional fluorescent proteins, iRFP requires biliverdin (BV) as a chromophore. Here, we report that phycocyanobilin (PCB) functions as a brighter chromophore for iRFP than BV, and that biosynthesis of PCB allows live-cell imaging with iRFP in the fission yeast Schizosaccharomyces pombe. We initially found that fission yeast cells did not produce BV and therefore did not show any iRFP fluorescence. The brightness of iRFP-PCB was higher than that of iRFP-BV both in vitro and in fission yeast. We introduced SynPCB2.1, a PCB biosynthesis system, into fission yeast, resulting in the brightest iRFP fluorescence. To make iRFP readily available in fission yeast, we developed an endogenous gene tagging system with iRFP and all-in-one integration plasmids carrying the iRFP-fused marker proteins together with SynPCB2.1. These tools not only enable the easy use of multiplexed live-cell imaging in fission yeast with a broader color palette, but also open the door to new opportunities for near-infrared fluorescence imaging in a wider range of living organisms. This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.259315","authors":"Sakai K, Kondo Y, Fujioka H, Kamiya M, Aoki K, Goto Y","authors_abbrev":"Sakai K et al.","pubmed_publication_date":"15 Dec 2021","pubmed_entrez_date":"2021-11-22","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-11-24 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38451028","title":"Telomere-to-telomere Schizosaccharomyces japonicus genome assembly reveals hitherto unknown genome features.","citation":"Yeast 2024 Mar;41(3):73-86","abstract":"Schizosaccharomyces japonicus belongs to the single-genus class Schizosaccharomycetes, otherwise known as \"fission yeasts.\" As part of a composite model system with its widely studied S. pombe sister species, S. japonicus has provided critical insights into the workings and the evolution of cell biological mechanisms. Furthermore, its divergent biology makes S. japonicus a valuable model organism in its own right. However, the currently available genome assembly contains gaps and has been unable to resolve centromeres and other repeat-rich chromosomal regions. Here we present a telomere-to-telomere long-read genome assembly of the S. japonicus genome. This includes the three megabase-length chromosomes, with centromeres hundreds of kilobases long, rich in 5S ribosomal RNA genes, transfer RNA genes, long terminal repeats, and short repeats. We identify a gene-sparse region on chromosome 2 that resembles a 331 kb centromeric duplication. We revise the genome size of S. japonicus to at least 16.6 Mb and possibly up to 18.12 Mb, at least 30% larger than previous estimates. Our whole genome assembly will support the growing S. japonicus research community and facilitate research in new directions, including centromere and DNA repeat evolution, and yeast comparative genomics.","doi":"10.1002/yea.3912","authors":"Etherington GJ, Wu PS, Oliferenko S, Uhlmann F, Nieduszynski CA","authors_abbrev":"Etherington GJ et al.","pubmed_publication_date":"Mar 2024","pubmed_entrez_date":"2024-03-07","publication_year":"2024","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2024-03-09 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8232284","title":"Intracellular pH in Schizosaccharomyces pombe--comparison with Saccharomyces cerevisiae.","citation":"Mol Cell Biochem 1993 Jul 21;124(2):131-40","abstract":"We examined cytoplasmic pH regulation in Schizosaccharomyces pombe and Saccharomyces cerevisiae using pH-sensitive fluorescent dyes. Of several different fluorescent compounds tested, carboxy-seminaphthorhodafluor-1 (C.SNARF-1) was the most effective. Leakage of C.SNARF-1 from S. pombe was much slower than leakage from C. cerevisiae. Using the pH-dependent fluorescence of C.SNARF-1 we showed that at an external pH of 7, mean resting internal pH was 7.0 for S. pombe and 6.6 for S. cerevisiae. We found that internal pH in S. pombe was maintained over a much narrower range in response to changes in external pH, especially at acidic pH. The addition of external glucose caused an intracellular alkalinization in both species, although the effect was much greater in S. cerevisiae than in S. pombe. The plasma membrane H(+)-ATPase inhibitor diethylstilbestrol reduced both the rate and extent of alkalinisation, with an IC50 of approximately 35 microM in both species. Amiloride also inhibited internal alkalinisation with IC50's of 745 microM for S. cerevisiae and 490 microM for S. pombe.","authors":"Haworth RS, Fliegel L","authors_abbrev":"Haworth RS et al.","pubmed_publication_date":"21 Jul 1993","pubmed_entrez_date":"1993-07-21","publication_year":"1993","canto_session_key":"01b7420c07bb5d03","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-12-01 10:39:00","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-01 10:38:23","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-12-01"},{"uniquename":"PMID:2798130","title":"Splicing of the U6 RNA precursor is impaired in fission yeast pre-mRNA splicing mutants.","citation":"Nucleic Acids Res 1989 Oct 11;17(19):7821-31","abstract":"U6 RNA is a member of a class of small abundant stable nuclear RNAs that are essential for splicing. In all species examined so far, the U6 RNA is a RNA polymerase III transcript. The U6 gene of the fission yeast Schizosaccharomyces pombe is unusual in that it is interrupted by an intron whose structure is similar to those found in pre-mRNAs. As part of our previous analysis of three S. pombe temperature sensitive pre-mRNA splicing mutants we examined their spliceosomal snRNA content. In contrast to the other snRNAs, the amount of U6 RNA is reduced at the restrictive temperature in all three of the mutants compared to the wild type. To investigate the cause of this reduction we have analyzed the efficiency of splicing of the U6 RNA precursor (U6 pre-RNA) in the pre-mRNA splicing mutants. At the restrictive temperature the ratio of unspliced U6 precursor to mature RNA is elevated in the mutants compared to the wild type grown under identical conditions, indicating a defect in U6 pre-RNA splicing. In this regard, the U6 RNA precursor behaves similarly to pre-mRNAs. Unspliced U6 pre-RNA was also detected in wild type cells under certain growth conditions.","authors":"Potashkin J, Frendewey D","authors_abbrev":"Potashkin J et al.","pubmed_publication_date":"11 Oct 1989","pubmed_entrez_date":"1989-10-11","publication_year":"1989","canto_session_key":"e8b7833f0d137e6b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-01-20 15:04:48","canto_approved_date":"2023-03-15 17:37:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-20 15:04:33","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.07","SPSNRNA.06","SPAC29E6.02","SPBC146.07"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2014-01-20"},{"uniquename":"EMBL:AU009010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10462526","title":"The S. pombe zfs1 gene is required to prevent septation if mitotic progression is inhibited.","citation":"J Cell Sci 1999 Sep;112 Pt 18:3103-14","abstract":"Schizosaccharomyces pombe cdc16p is required to limit the cell to forming a single division septum per cell cycle; the heat-sensitive loss-of-function mutant cdc16-116 completes mitosis, and then undergoes multiple rounds of septum formation without cell cleavage. cdc16p is a homologue of Saccharomyces cerevisiae BUB2p, and has also been implicated in the spindle assembly checkpoint function in S. pombe. To identify other proteins involved in regulating septum formation, we have screened for multicopy suppressors of the cdc16-116 mutation. In this paper, we describe one of these suppressors, zfs1. The null allele (zfs1-D1) is viable. However, at low temperatures it divides at a reduced size, while at higher temperatures, it partially suppresses heat sensitive mutants in genes signalling the onset of septum formation. Zfs1-D1 cells show an increased rate of chromosome loss during exponential growth. Moreover, if assembly of the spindle is prevented, zfs1-D1 cells do not arrest normally, but the activity of cdc2p kinase decays, and cells form a division septum without completing a normal mitosis. We conclude that zfs1 function is required to prevent septum formation and exit from mitosis if the mitotic spindle is not assembled. The suppression of cdc16-116 by zfs1 is independent of dma1 function and the spindle assembly checkpoint genes mad2 and mph1. The genetic interactions of zfs1 with genes regulating septum formation suggest that it may be a modulator of the signal transduction network controlling the onset of septum formation and exit from mitosis.","authors":"Beltraminelli N, Murone M, Simanis V","authors_abbrev":"Beltraminelli N et al.","pubmed_publication_date":"Sep 1999","pubmed_entrez_date":"1999-08-27","publication_year":"1999","canto_session_key":"e9505a55369a6ad9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-10-23 10:37:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-19 21:27:58","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1565.06c","SPAC9G1.09","SPBC1718.07c","SPCC1739.11c","SPCC18B5.03","SPBC21.06c","SPBC24C6.07","SPAC24B11.11c","SPBC244.01c","SPAC6F6.08c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2014-09-19"},{"uniquename":"PMID:10770926","title":"Isolation and characterization of various complexes of the minichromosome maintenance proteins of Schizosaccharomyces pombe.","citation":"J Biol Chem 2000 Jun 23;275(25):18871-8","abstract":"Minichromosome maintenance (Mcm) proteins 2-7 are highly conserved in eukaryotes and play an essential role in DNA replication. Here, we describe the reconstitution of the various complexes of the Mcm proteins of Schizosaccharomyces pombe using the baculovirus expression system. The simultaneous expression of all six of the Mcm proteins, as well as different combinations of these proteins, yielded several stable complexes that included the heterohexamer of Mcm2/3/4/5/6/7, the Mcm2/4/6/7 heterotetramer, the dimer of the Mcm4/6/7 heterotrimer, and the Mcm3/5 heterodimer. The purification and characterization of the biochemical properties of these complexes showed that only the dimeric complex of the Mcm4/6/7 heterotrimer possessed single stranded DNA-dependent ATPase, ATP-dependent single stranded DNA binding, and 3' to 5' DNA helicase activities. Consistent with these results, the interaction of either Mcm2 or Mcm3/5 with the Mcm4/6/7 complex resulted in the disassembly of the dimeric complex of Mcm4/6/7 and the loss of DNA helicase activity. These results suggest that the Mcm4/6/7 complex is a catalytic core of the Mcm complex and that Mcm2 and Mcm3/5 may be involved in the regulation of the activity of this complex.","authors":"Lee JK, Hurwitz J","authors_abbrev":"Lee JK et al.","pubmed_publication_date":"23 Jun 2000","pubmed_entrez_date":"2000-04-20","publication_year":"2000","canto_session_key":"e5f8e6c0322f4204","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-10-27 11:12:12","canto_approved_date":"2022-02-02 10:14:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-07 15:14:29","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B2.05","SPBC211.04c","SPCC16A11.17","SPBC4.04c","SPBC25D12.03c","SPCC1682.02c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-10-27"},{"uniquename":"PMID:12664932","title":"[New antifungal agents].","citation":"Jpn J Antibiot 2002 Dec;55(6):911-2","abstract":"","authors":"Miyazaki Y, Kawano S","authors_abbrev":"Miyazaki Y et al.","pubmed_publication_date":"Dec 2002","pubmed_entrez_date":"2003-04-01","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8305682","title":"Reversible tyrosine phosphorylation and cell cycle control.","citation":"Semin Cell Biol 1993 Dec;4(6):433-42","abstract":"In eukaryotic organisms, reversible tyrosine phosphorylation has been established as an important element in the regulation of cell growth and more recently as an essential element in the regulation of the cell division cycle. The activity of p34cdc2, a protein kinase whose activity is required for the entry of cells into mitosis, is tightly controlled by reversible phosphorylation at tyrosine 15. A complex network of interacting protein kinases and protein phosphatases regulate the state of p34cdc2 tyrosine phosphorylation and therefore the entry of cells into mitosis. In the fission yeast Schizosaccharomyces pombe, genes encoding several of these protein kinases and protein phosphatases have been obtained through genetic approaches. In this review, we will focus on the protein kinases encoded by wee1+, mik1+ and cdr1+/nim1+ and the protein phosphatases encoded by cdc25+ and pyp1+, pyp2+ and pyp3+. Homologs of many of these regulators have been identified and characterized in higher eukaryotes underscoring the importance of reversible tyrosine phosphorylation as a universal mechanism for the regulation of the cell division cycle.","authors":"Atherton-Fessler S, Hannig G, Piwnica-Worms H","authors_abbrev":"Atherton-Fessler S et al.","pubmed_publication_date":"Dec 1993","pubmed_entrez_date":"1993-12-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35996690","title":"Autophagy-related genes genetically interact with Pmk1 MAPK signaling in fission yeast.","citation":"MicroPubl Biol 2022;2022","abstract":"Apart from the highly conserved role in the cellular degradation process, autophagy also appears to play a key role in cellular proliferation. Here, we describe the genetic interaction of autophagy-related genes and Pmk1 MAPK signaling in fission yeast.  atg1  deletion cells (Δ  atg1  ) exhibit the  vic  (viable in the presence of immunosuppressant and Cl  -  ) phenotype, indicative of Pmk1 signaling inhibition. Moreover, the Δ  atg1  Δ  pmk1  double mutant resembles the single Δ  pmk1  mutant, suggesting that Atg1 functions in the Pmk1 pathway. In addition, the growth defect induced by overexpression of Pck2, an upstream activator of Pmk1 MAPK was alleviated by the deletion of  atg1  +   . Finally, the deletion of autophagy-related genes recapitulates Pmk1 MAPK signaling inhibition. Our data suggest a novel role for autophagy in MAPK signaling regulation.","doi":"10.17912/micropub.biology.000618","authors":"Takasaki T, Utsumi R, Shimada E, Tomimoto N, Satoh R, Sugiura R","authors_abbrev":"Takasaki T et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-08-23","publication_year":"2022","canto_session_key":"9c65aaa10de483cf","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-08-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17881496","title":"The Dam1/DASH complex is required for the retrieval of unclustered kinetochores in fission yeast.","citation":"J Cell Sci 2007 Oct 01;120(Pt 19):3345-51","abstract":"In fission yeast centromeres cluster at the nuclear envelope in a region underlying the spindle pole body during interphase, an arrangement known as a Rabl configuration. We have identified a strain in which one pair of sister kinetochores is unclustered from the others and binds the nuclear envelope at a point distal to the spindle pole body. We show that during mitosis unclustered kinetochores are captured by intranuclear spindle microtubules which then pull the kinetochores back to one of the two spindle poles before they are bi-oriented on the mitotic spindle. We find that kinetochore retrieval occurs at the depolymerising microtubule plus end and is dependent on the non-essential Dam1/DASH complex. In the absence of Dam1 unclustered kinetochores are captured on the lateral surface of spindle microtubule bundles but poleward kinetochore movement does not occur. These data provide the first direct evidence that the Dam1/DASH complex can couple the force generated by microtubule depolymerisation to direct chromosome movement in vivo.","authors":"Franco A, Meadows JC, Millar JB","authors_abbrev":"Franco A et al.","pubmed_publication_date":"01 Oct 2007","pubmed_entrez_date":"2007-09-21","publication_year":"2007","canto_session_key":"81e91219a1043368","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-11-07 20:07:54","canto_approved_date":"2020-12-28 15:10:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-05 14:57:58","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC417.07c","SPAC589.08c","SPBC2F12.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-11-07"},{"uniquename":"PMID:33737447","title":"Perfect Match Genomic Landscape strategy: Refinement and customization of reference genomes.","citation":"Proc Natl Acad Sci U S A 2021 Apr 06;118(14)","abstract":"When addressing a genomic question, having a reliable and adequate reference genome is of utmost importance. This drives the necessity to refine and customize reference genomes (RGs). Our laboratory has recently developed a strategy, the Perfect Match Genomic Landscape (PMGL), to detect variation between genomes [K. Palacios-Flores  et al.  Genetics  208, 1631-1641 (2018)]. The PMGL is precise and sensitive and, in contrast to most currently used algorithms, is nonstatistical in nature. Here we demonstrate the power of PMGL to refine and customize RGs. As a proof-of-concept, we refined different versions of the  Saccharomyces cerevisiae  RG. We applied the automatic PMGL pipeline to refine the genomes of microorganisms belonging to the three domains of life: the archaea  Methanococcus maripaludis  and  Pyrococcus furiosus ; the bacteria  Escherichia coli ,  Staphylococcus aureus , and  Bacillus subtilis ; and the eukarya  Schizosaccharomyces pombe ,  Aspergillus oryzae , and several strains of  Saccharomyces paradoxus.  We analyzed the reference genome of the virus SARS-CoV-2 and previously published viral genomes from patients' samples with COVID-19. We performed a mutation-accumulation experiment in  E. coli  and show that the PMGL strategy can detect specific mutations generated at any desired step of the whole procedure. We propose that PMGL can be used as a final step for the refinement and customization of any haploid genome, independently of the strategies and algorithms used in its assembly.","doi":"10.1073/pnas.2025192118","authors":"Palacios-Flores K, García-Sotelo J, Castillo A, Uribe C, Morales L, Boege M, Dávila G, Flores M, Palacios R","authors_abbrev":"Palacios-Flores K et al.","pubmed_publication_date":"06 Apr 2021","pubmed_entrez_date":"2021-03-19","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-03-21 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14629042","title":"Strand compositional asymmetries of nuclear DNA in eukaryotes.","citation":"J Mol Evol 2003 Sep;57(3):325-34","abstract":"Both DNA replication and transcription are structurally asymmetric processes. An asymmetric nucleotide substitution pattern has been observed between the leading and the lagging strand, and between the coding and the noncoding strand, in eubacterial, viral, and organelle genomes. Similar studies in eukaryotes have been rare, because the origins of replication in nuclear genomes are mostly unknown and the replicons are much shorter than those of prokaryotes. To circumvent these predicaments, all possible pairs of neighboring genes that are located on different strands of nuclear DNA were selected from the complete genomes of Saccharomyces cerevisiae, Schizosaccharomyces pombe, Plasmodium falciparum, Encephalitozoon cuniculi, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Anopheles gambiae, Mus musculus, and Homo sapiens. For such a pair of genes, one is likely coded from the leading strand and the other from the lagging strand. By examining the introns and the fourfold degenerate sites of codons in the genes of each pair, we found that the relative frequencies of T vs. A and of G vs. C are significantly skewed in most eukaryotes studied. In a gene pair, the potential effects of replication- and transcription-associated mutation bias on strand asymmetry are in the same direction for one gene where leading strand synthesis shares the same template with transcription, while they tend to be canceled out in the other gene. Our study demonstrates that DNA replication-associated and transcription-associated mutation bias and/or selective codon usage bias may affect the strand nucleotide composition asymmetrically in eukaryotic genomes.","authors":"Niu DK, Lin K, Zhang DY","authors_abbrev":"Niu DK et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-11-25","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22064468","title":"Dare to challenge the silence? Telomeric gene silencing revisited.","citation":"Nucleus 2011;2(6):513-6","abstract":"Gene silencing refers to position-dependent and promoter-independent repression of genes via the establishment and the maintenance of compacted heterochromatin. A very significant part of our knowledge on this phenomenon has been derived from studies in the yeasts S. cerevisiae and S. pombe. The gene silencing analyses in these species very often include the FOA-sensitivity assay, which detects the suppression of a reporter gene (URA3 in S. cerevisiae and URA4 in S. pombe) inserted at genomic locations of choice. Two recent studies have contested the validity of this assay and have set uneasy silence in the field. We are not certain how much of the previously acquired data truly deals with gene silencing. The current article comments on this challenge.","doi":"10.4161/nucl.2.6.17710","authors":"Yankulov K","authors_abbrev":"Yankulov K","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-11-09","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11991638","title":"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.","citation":"RNA 2002 Apr;8(4):426-39","abstract":"We describe characterization of spliceosomes affinity purified under native conditions. These spliceosomes consist largely of C complex containing splicing intermediates. After C complex assembly on an MS2 affinity-tagged pre-mRNA substrate containing a 3' splice site mutation, followed by RNase H digestion of earlier complexes, spliceosomes were purified by size exclusion and affinity selection. This protocol yielded 40S C complexes in sufficient quantities to visualize in negative stain by electron microscopy. Complexes purified in this way contain U2, U5, and U6 snRNAs, but very little U1 or U4 snRNA. Analysis by tandem mass spectrometry confirmed the presence of core snRNP proteins (SM and LSM), U2 and U5 snRNP-specific proteins, and the second step factors Prp16, Prp17, Slu7, and Prp22. In contrast, proteins specific to earlier splicing complexes, such as U2AF and U1 snRNP components, were not detected in C complex, but were present in similarly purified H complex. Images of these spliceosomes revealed single particles with dimensions of approximately 270 x 240 A that assort into well-defined classes. These images represent an important first step toward attaining a comprehensive three-dimensional understanding of pre-mRNA splicing.","authors":"Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ","authors_abbrev":"Jurica MS et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-05-07","publication_year":"2002","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37189462","title":"Transcriptional Regulation Technology for Gene Perturbation in Fission Yeast.","citation":"Biomolecules 2023 Apr 21;13(4)","abstract":"Isolation and introduction of genetic mutations is the primary approach to characterize gene functions in model yeasts. Although this approach has proven very powerful, it is not applicable to all genes in these organisms. For example, introducing defective mutations into essential genes causes lethality upon loss of function. To circumvent this difficulty, conditional and partial repression of target transcription is possible. While transcriptional regulation techniques, such as promoter replacement and 3' untranslated region (3'UTR) disruption, are available for yeast systems, CRISPR-Cas-based technologies have provided additional options. This review summarizes these gene perturbation technologies, including recent advances in methods based on CRISPR-Cas systems for  Schizosaccharomyces pombe . We discuss how biological resources afforded by CRISPRi can promote fission yeast genetics.","doi":"10.3390/biom13040716","authors":"Ishikawa K, Saitoh S","authors_abbrev":"Ishikawa K et al.","pubmed_publication_date":"21 Apr 2023","pubmed_entrez_date":"2023-05-16","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-05-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29183750","title":"Pheromone-inducible expression vectors for fission yeast Schizosaccharomyces pombe.","citation":"Plasmid 2018 Jan;95:1-6","abstract":"The fission yeast Schizosaccharomyces pombe is an attractive host for heterologous gene expression. However, expression systems for industrially viable large-scale fermentations are scarce. Several inducible expression vectors for S. pombe have been reported, with the strong thiamine-repressible nmt1 +  promoter or derivatives thereof most commonly employed. Previously, the promoter regions of the genes sxa2 +  and rep1 +  were utilized to couple pheromone signaling to the expression of reporter genes for quantitative assessment of the cellular response to mating pheromones. Here, we exploit these promoters to serve as highly effective, plasmid-based inducible expression systems for S. pombe. Simply by adding synthetic P-factor pheromone, both promoters conferred 50-60% higher peak expression levels than the nmt1 +  promoter. Full induction was significantly faster than observed for nmt1 + -based expression platforms. Furthermore, the sxa2 +  promoter showed very low basal activity and an overall 584-fold induction by synthetic P-factor pheromone. The dose-response curves of both promoters were assessed, providing the opportunity for facile tuning of the expression level by modulating P-factor concentration. Since the expression plasmids relying on the sxa2 +  and rep1 +  promoters require neither medium exchange nor glucose/thiamine starvation, they proved to be very convenient in handling. Hence, these expression vectors will improve the palette of valuable genetic tools for S. pombe, applicable to both basic research and biotechnology.","doi":"10.1016/j.plasmid.2017.11.002","authors":"Hennig S, Hornauer N, Rödel G, Ostermann K","authors_abbrev":"Hennig S et al.","pubmed_publication_date":"Jan 2018","pubmed_entrez_date":"2017-11-30","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-12-02 01:15:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24373411","title":"Fungal gene expression levels do not display a common mode of distribution.","citation":"BMC Res Notes 2013 Dec 28;6:559","abstract":"RNA-seq studies in metazoa have revealed a distinct, double-peaked (bimodal) distribution of gene expression independent of species and cell type. However, two studies in filamentous fungi yielded conflicting results, with a bimodal distribution in Pyronema confluens and varying distributions in Sordaria macrospora. To obtain a broader overview of global gene expression distributions in fungi, an additional 60 publicly available RNA-seq data sets from six ascomycetes and one basidiomycete were analyzed with respect to gene expression distributions.\nClustering of normalized, log2-transformed gene expression levels for each RNA-seq data set yielded distributions with one to five peaks. When only major peaks comprising at least 15% of all analyzed genes were considered, distributions ranged from one to three major peaks, suggesting that fungal gene expression is not generally bimodal. The number of peaks was not correlated with the phylogenetic position of a species; however, higher filamentous asco- and basidiomycetes showed up to three major peaks, whereas gene expression levels in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe had only one to two major peaks, with one predominant peak containing at least 70% of all expressed genes. In several species, the number of peaks varied even within a single species, e.g. depending on the growth conditions as evidenced in the one to three major peaks in different samples from Neurospora crassa. Earlier studies based on microarray and SAGE data revealed distributions of gene expression level that followed Zipf's law, i.e. log-transformed gene expression levels were inversely proportional to the log-transformed expression rank of a gene. However, analyses of the fungal RNA-seq data sets could not identify any that confirmed to Zipf's law.\nFungal gene expression patterns cannot generally be described by a single type of distribution (bimodal or Zipf's law). One hypothesis to explain this finding might be that gene expression in fungi is highly dynamic, and fine-tuned at the level of transcription not only for individual genes, but also at a global level.","doi":"10.1186/1756-0500-6-559","authors":"Nowrousian M","authors_abbrev":"Nowrousian M","pubmed_publication_date":"28 Dec 2013","pubmed_entrez_date":"2013-12-31","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010436","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29742018","title":"The kinase domain of CK1 enzymes contains the localization cue essential for compartmentalized signaling at the spindle pole.","citation":"Mol Biol Cell 2018 Jul 01;29(13):1664-1674","abstract":"CK1 protein kinases contribute to multiple biological processes, but how they are tailored to function in compartmentalized signaling events is largely unknown. Hhp1 and Hhp2 (Hhp1/2) are the soluble CK1 family members in Schizosaccharomyces pombe. One of their functions is to inhibit the septation initiation network (SIN) during a mitotic checkpoint arrest. The SIN is assembled by Sid4 at spindle pole bodies (SPBs), and though Hhp1/2 colocalize there, it is not known how they are targeted there or whether their SPB localization is required for SIN inhibition. Here, we establish that Hhp1/2 localize throughout the cell cycle to SPBs, as well as to the nucleus, cell tips, and division site. We find that their catalytic domains but not their enzymatic function are used for SPB targeting and that this targeting strategy is conserved in human CK1δ/ε localization to centrosomes. Further, we pinpoint amino acids in the Hhp1 catalytic domain required for SPB interaction; mutation of these residues disrupts Hhp1 association with the core SPB protein Ppc89, and the inhibition of cytokinesis in the setting of spindle stress. Taken together, these data have enabled us to define a molecular mechanism used by CK1 enzymes to target a specific cellular locale for compartmentalized signaling.","doi":"10.1091/mbc.E18-02-0129","authors":"Elmore ZC, Guillen RX, Gould KL","authors_abbrev":"Elmore ZC et al.","pubmed_publication_date":"01 Jul 2018","pubmed_entrez_date":"2018-05-10","publication_year":"2018","canto_session_key":"885eefd237119afe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Zachary Elmore","canto_first_approved_date":"2018-07-13 10:42:21","canto_approved_date":"2026-02-06 15:42:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-07-03 13:39:22","canto_added_date":"2018-05-11 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":99,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Zachary Elmore","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPBP35G2.05c","SPBC3H7.15","SPAC4H3.11c","SPAC17G8.10c","SPAC23C4.12","SPBC26H8.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-07-13"},{"uniquename":"PMID:15660136","title":"SCF(Pof1)-ubiquitin and its target Zip1 transcription factor mediate cadmium response in fission yeast.","citation":"EMBO J 2005 Feb 09;24(3):599-610","abstract":"Ubiquitin-dependent proteolysis regulates gene expression in many eukaryotic systems. Pof1 is an essential fission yeast F-box protein that is homologous to budding yeast Met30. Temperature-sensitive pof1 mutants display acute growth arrest with small cell size. Extragenic suppressor analysis identified Zip1, a bZIP (basic leucine zipper) transcription factor, as a target for Pof1. We show Zip1 is stabilized in pof1 mutants, Pof1 binds only phosphorylated forms of Zip1, and Zip1 is ubiquitylated in vivo, indicating that Zip1 is a substrate of SCF(Pof1). Genome-wide DNA microarray assay shows that many cadmium-induced genes are under the control of Zip1, suggesting Zip1 plays a role in cadmium response. Consistently, zip1 mutants are hypersensitive to cadmium and unlike wild type, lose cell viability under this stress. Intriguingly, cadmium exposure results in upregulation of Zip1 levels and leads wild-type cells to growth arrest with reduced cell size, reminiscent of pof1 phenotypes. Our results indicate that Zip1 mediates growth arrest in cadmium response, which is essential to maintain viability. Normally growing cells prevent this response through constitutive ubiquitylation and degradation of Zip1 via SCF(Pof1).","authors":"Harrison C, Katayama S, Dhut S, Chen D, Jones N, Bähler J, Toda T","authors_abbrev":"Harrison C et al.","pubmed_publication_date":"09 Feb 2005","pubmed_entrez_date":"2005-01-22","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC337.08c","SPAC25G10.03","SPAC57A10.05c","SPAC17G6.12","SPBC16G5.01"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:35100366","title":"Fission stories: using PomBase to understand Schizosaccharomyces pombe biology.","citation":"Genetics 2022 Apr 04;220(4)","abstract":"PomBase (www.pombase.org), the model organism database (MOD) for the fission yeast Schizosaccharomyces pombe, supports research within and beyond the S. pombe community by integrating and presenting genetic, molecular, and cell biological knowledge into intuitive displays and comprehensive data collections. With new content, novel query capabilities, and biologist-friendly data summaries and visualization, PomBase also drives innovation in the MOD community.","doi":"10.1093/genetics/iyab222","authors":"Harris MA, Rutherford KM, Hayles J, Lock A, Bähler J, Oliver SG, Mata J, Wood V","authors_abbrev":"Harris MA et al.","pubmed_publication_date":"04 Apr 2022","pubmed_entrez_date":"2022-01-31","publication_year":"2022","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2022-02-02 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11839292","title":"Checkpoints: how to flag up double-strand breaks.","citation":"Curr Biol 2002 Feb 05;12(3):R105-7","abstract":"How checkpoint pathways recognise double-strand breaks has long been a mystery. Recent studies have found that two distinct checkpoint protein complexes associate independently with chromatin at the sites of DNA damage. Why do two distinct mechanisms recognise strand lesions, and what does this tell us about the checkpoint pathways?","authors":"Caspari T, Carr AM","authors_abbrev":"Caspari T et al.","pubmed_publication_date":"05 Feb 2002","pubmed_entrez_date":"2002-02-13","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31053642","title":"The yeast protein Mam33 functions in the assembly of the mitochondrial ribosome.","citation":"J Biol Chem 2019 Jun 21;294(25):9813-9829","abstract":"Mitochondrial ribosomes are functionally specialized for the synthesis of several essential inner membrane proteins of the respiratory chain. Although remarkable progress has been made toward understanding the structure of mitoribosomes, the pathways and factors that facilitate their biogenesis remain largely unknown. The long unstructured domains of unassembled ribosomal proteins are highly prone to misfolding and often require dedicated chaperones to prevent aggregation. To date, chaperones that ensure safe delivery to the assembling ribosome have not been identified in the mitochondrion. In this study, a respiratory synthetic lethality screen revealed a role for an evolutionarily conserved mitochondrial matrix protein called Mam33 in  Saccharomyces cerevisiae  mitoribosome biogenesis. We found that the absence of Mam33 results in misassembled, aggregated ribosomes and a respiratory lethal phenotype in combination with other ribosome-assembly mutants. Using sucrose gradient sedimentation, native affinity purifications,  in vitro  binding assays, and SILAC-based quantitative proteomics, we found that Mam33 does not associate with the mature mitoribosome, but directly binds a subset of unassembled large subunit proteins. Based on these data, we propose that Mam33 binds specific mitoribosomal proteins to ensure proper assembly.","doi":"10.1074/jbc.RA119.008476","authors":"Hillman GA, Henry MF","authors_abbrev":"Hillman GA et al.","pubmed_publication_date":"21 Jun 2019","pubmed_entrez_date":"2019-05-05","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPMIT.01","SPBC776.07"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:15177031","title":"Tea2p kinesin is involved in spatial microtubule organization by transporting tip1p on microtubules.","citation":"Dev Cell 2004 Jun;6(6):831-43","abstract":"The positioning of growth sites in fission yeast cells is mediated by spatially controlled microtubule dynamics brought about by tip1p, a CLIP-170-like protein, which is localized at the microtubule tips and guides them to the cell ends. The kinesin tea2p is also located at microtubule tips and affects microtubule dynamics. Here we show that tea2p interacts with tip1p and that the two proteins move with high velocity along the microtubules toward their growing tips. There, tea2p and tip1p accumulate in larger particles. Particle formation requires the EB1 homolog, mal3p. Our results suggest a model in which kinesins regulate microtubule growth by transporting regulatory factors such as tip1p to the growing microtubule tips.","authors":"Busch KE, Hayles J, Nurse P, Brunner D","authors_abbrev":"Busch KE et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-06-05","publication_year":"2004","canto_session_key":"ce1fc9c90e999884","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-01-05 17:22:08","canto_approved_date":"2026-01-04 13:13:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-29 16:35:52","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":28,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.12","SPBC1604.20c","SPAC18G6.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-01-05"},{"uniquename":"PMID:31829937","title":"Direct comparison of clathrin-mediated endocytosis in budding and fission yeast reveals conserved and evolvable features.","citation":"Elife 2019 Dec 12;8","abstract":"Conserved proteins drive clathrin-mediated endocytosis (CME), which from yeast to humans involves a burst of actin assembly. To gain mechanistic insights into this process, we performed a side-by-side quantitative comparison of CME in two distantly related yeast species. Though endocytic protein abundance in  S. pombe  and  S. cerevisiae  is more similar than previously thought, membrane invagination speed and depth are two-fold greater in fission yeast. In both yeasts, accumulation of ~70 WASp molecules activates the Arp2/3 complex to drive membrane invagination. In contrast to budding yeast, WASp-mediated actin nucleation plays an essential role in fission yeast endocytosis. Genetics and live-cell imaging revealed core CME spatiodynamic similarities between the two yeasts, although the assembly of two zones of actin filaments is specific for fission yeast and not essential for CME. These studies identified conserved CME mechanisms and species-specific adaptations with broad implications that are expected to extend from yeast to humans.","doi":"10.7554/eLife.50749","authors":"Sun Y, Schöneberg J, Chen X, Jiang T, Kaplan C, Xu K, Pollard TD, Drubin DG","authors_abbrev":"Sun Y et al.","pubmed_publication_date":"12 Dec 2019","pubmed_entrez_date":"2019-12-13","publication_year":"2019","canto_session_key":"9f0164f6485af1c0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16541025","title":"Shugoshin collaborates with protein phosphatase 2A to protect cohesin.","citation":"Nature 2006 May 04;441(7089):46-52","abstract":"Sister chromatid cohesion, mediated by a complex called cohesin, is crucial--particularly at centromeres--for proper chromosome segregation in mitosis and meiosis. In animal mitotic cells, phosphorylation of cohesin promotes its dissociation from chromosomes, but centromeric cohesin is protected by shugoshin until kinetochores are properly captured by the spindle microtubules. However, the mechanism of shugoshin-dependent protection of cohesin is unknown. Here we find a specific subtype of serine/threonine protein phosphatase 2A (PP2A) associating with human shugoshin. PP2A colocalizes with shugoshin at centromeres and is required for centromeric protection. Purified shugoshin complex has an ability to reverse the phosphorylation of cohesin in vitro, suggesting that dephosphorylation of cohesin is the mechanism of protection at centromeres. Meiotic shugoshin of fission yeast also associates with PP2A, with both proteins collaboratively protecting Rec8-containing cohesin at centromeres. Thus, we have revealed a conserved mechanism of centromeric protection of eukaryotic chromosomes in mitosis and meiosis.","authors":"Kitajima TS, Sakuno T, Ishiguro K, Iemura S, Natsume T, Kawashima SA, Watanabe Y","authors_abbrev":"Kitajima TS et al.","pubmed_publication_date":"04 May 2006","pubmed_entrez_date":"2006-03-17","publication_year":"2006","canto_session_key":"a94ed2012c4ff5bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-03-16 11:26:00","canto_approved_date":"2024-04-02 14:49:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-20 11:52:53","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.03c","SPBC29A10.14","SPAP8A3.09c","SPAC823.15","SPCC188.02"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2021-03-16"},{"uniquename":"PMID:34208016","title":"Long Non-Coding RNAs in the Control of Gametogenesis: Lessons from Fission Yeast.","citation":"Noncoding RNA 2021 Jun 11;7(2)","abstract":"Long non-coding RNAs (lncRNAs) contribute to cell fate decisions by modulating genome expression and stability. In the fission yeast  Schizosaccharomyces pombe , the transition from mitosis to meiosis results in a marked remodeling of gene expression profiles, which ultimately ensures gamete production and inheritance of genetic information to the offspring. This key developmental process involves a set of dedicated lncRNAs that shape cell cycle-dependent transcriptomes through a variety of mechanisms, including epigenetic modifications and the modulation of transcription, post-transcriptional and post-translational regulations, and that contribute to meiosis-specific chromosomal events. In this review, we summarize the biology of these lncRNAs, from their identification to mechanism of action, and discuss their regulatory role in the control of gametogenesis.","doi":"10.3390/ncrna7020034","authors":"Andric V, Rougemaille M","authors_abbrev":"Andric V et al.","pubmed_publication_date":"11 Jun 2021","pubmed_entrez_date":"2021-07-02","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-07-04 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8562848","title":"A study of growth kinetics of the flocs from Schizosaccharomyces pombe.","citation":"Chin J Biotechnol 1995;11(2):125-30","abstract":"Inducing yeast cells to self-flocculate could be considered a cell immobilization method. The growth kinetics of the flocs from Schizosaccharomyces pombe was studied in an experimental suspended-bed bioreactor with starch hydrolysate obtained by two-stage enzymatic hydrolysis. It was discovered that a limited oxygen supply was necessary during continuous ethanol fermentation with yeast flocs. The oxygen supplied was a kind of limited substrate effecting on the floc growth. Further, a kinetic model describing this floc growth was proposed.","authors":"Bai F, Qin J, Xie J, Li N, Feng P","authors_abbrev":"Bai F et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1221303","title":"Repair in Schizosaccharomyces pombe as measured by recovery from caffeine enhancement of radiation-induced lethality.","citation":"Mol Gen Genet 1975 Dec 30;142(3):171-83","abstract":"Inhibition of DNA repair by caffeine is manifested in Schizosaccharomyces pombe wild-type cells as an enhancement of UV- or gamma-irradiation-induced lethality. The progress of DNA repair processes involving one or more caffeine-sensitive steps may be conveniently followed by measuring the concomitant decrease of this lethal enhancement effect. By measuring, during post-irradiation incubation, the ability of cells to overcome susceptibility to repair inhibition by caffeine, we have determined the time course and requirements for repair in S. pombe. Recovery began immediately and took 150-200 min after gamma-irradiation and more than 500 min after UV-irradiation, for exposures which gave about 10% survival in the absence of caffeine. An incubation medium capable of supporting growth was required for caffeine-sensitive repair; no recovery occurred under liquid holding conditions. Survival curves after various recovery times indicated that a logarithmic phase cell population was homogeneous with respect to caffeine-sensitive repair of both UV- and gamma-ray-induced damage. Recovery from caffeine inhibition was compared for cells of different physiological states (logarithmic and stationary phase); although the importance of the physiological state was not the same for the two types of radiation, recovery was found to occur more rapidly in the more radiation-resistant state, in each case.","authors":"Gentner NE, Werner MM","authors_abbrev":"Gentner NE et al.","pubmed_publication_date":"30 Dec 1975","pubmed_entrez_date":"1975-12-30","publication_year":"1975","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7865880","title":"Fission yeast minichromosome loss mutants mis cause lethal aneuploidy and replication abnormality.","citation":"Mol Biol Cell 1994 Oct;5(10):1145-58","abstract":"Precise chromosome transmission in cell division cycle is maintained by a number of genes. The attempt made in the present study was to isolate temperature-sensitive (ts) fission yeast mutants that display high loss rates of minichromosomes at permissive or semipermissive temperature (designated mis). By colony color assay of 539 ts strains that contain a minichromosome, we have identified 12 genetic loci (mis1-mis12) and determined their phenotypes at restrictive temperature. Seven of them are related to cell cycle block phenotype at restrictive temperature, three of them in mitosis. Unequal distribution of regular chromosomes in the daughters is extensive in mis6 and mis12. Cells become inviable after rounds of cell division due to missegregation. The phenotype of mis5 is DNA replication defect and hypersensitivity to UV ray and hydroxyurea. mis5+ encodes a novel member of the ubiquitous MCM family required for the onset of replication. The mis5+ gene is essential for viability and functionally distinct from other previously identified members in fission yeast, cdc21+, nda1+, and nda4+. The mis11 mutant phenotype was the cell division block with reduced cell size. Progression of the G1 and G2 phases is blocked in mis11. The cloned mis11+ gene is identical to prp2+, which is essential for RNA splicing and similar to a mammalian splicing factor U2AF65.","authors":"Takahashi K, Yamada H, Yanagida M","authors_abbrev":"Takahashi K et al.","pubmed_publication_date":"Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_session_key":"e8278d6fd6c40079","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-11-16 16:04:47","canto_approved_date":"2026-01-31 10:52:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-10-16 14:27:06","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":33,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPAC27E2.05","SPAC1687.20c","SPBC25B2.05","SPBC409.04c","SPBC146.07","SPBC336.04","SPCC16A11.17","SPBC211.04c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2015-11-16"},{"uniquename":"PMID:7804158","title":"Both glucose-type monosaccharides and one of their metabolites are required for activation of yeast plasma membrane H(+)-ATPase.","citation":"Cell Biol Int 1994 Aug;18(8):813-7","abstract":"Saccharomyces cerevisiae and Schizosaccharomyces pombe cells were grown on D-glucose, D-galactose, D-fructose, D-mannose, maltose, trehalose and ethanol. All these substrates were separately added to cells thus grown and the onset and rate of acidification mediated by the plasma membrane H(+)-ATPase were determined. Irrespective of the growth substrate, the best triggers of acidification in both species were fructose, mannose and glucose (with average rates of 5.2, 5.0 and 4.8 nmol H+ per min per mg dry weight, respectively, for S. cerevisiae, and 4.5, 6.8 and 5.8 for S. pombe). These were followed in S. cerevisiae by galactose in Gal-, Man- and Tre-grown cells (about 0.40 nmol H+) and by maltose in Mal- and Tre-grown cells (about 0.15 nmol H+). Trehalose elicited some response in only ethanol-grown cells while ethanol itself was completely ineffective in activating the H(+)-ATPase. In S. pombe, however, maltose caused an acidification rate of 3.6 nmol H+ per min per mg dry wt., followed by EtOH (().38), Gal (0.13) and Tre (0.05). 6-Deoxy-D-glucose and 2-deoxy-D-glucose, not metabolized or improperly metabolized analogues of glucose, had no effect whatsoever. It appears that the sensor triggering the ATPase-activating pathway is a complex responding both to a glucose-type sugar (Glc, Man, Fru) and possibly identical with one of the glucose carriers, and to one of its metabolites, most probably fructose-6-phosphate.","authors":"Kotyk A, Georghiou G","authors_abbrev":"Kotyk A et al.","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11348594","title":"Specificity determinants in phosphoinositide dephosphorylation: crystal structure of an archetypal inositol polyphosphate 5-phosphatase.","citation":"Cell 2001 May 04;105(3):379-89","abstract":"Inositol polyphosphate 5-phosphatases are central to intracellular processes ranging from membrane trafficking to Ca(2+) signaling, and defects in this activity result in the human disease Lowe syndrome. The 1.8 resolution structure of the inositol polyphosphate 5-phosphatase domain of SPsynaptojanin bound to Ca(2+) and inositol (1,4)-bisphosphate reveals a fold and an active site His and Asp pair resembling those of several Mg(2+)-dependent nucleases. Additional loops mediate specific inositol polyphosphate contacts. The 4-phosphate of inositol (1,4)-bisphosphate is misoriented by 4.6 compared to the reactive geometry observed in the apurinic/apyrimidinic endonuclease 1, explaining the dephosphorylation site selectivity of the 5-phosphatases. Based on the structure, a series of mutants are described that exhibit altered substrate specificity providing general determinants for substrate recognition.","authors":"Tsujishita Y, Guo S, Stolz LE, York JD, Hurley JH","authors_abbrev":"Tsujishita Y et al.","pubmed_publication_date":"04 May 2001","pubmed_entrez_date":"2001-05-12","publication_year":"2001","canto_session_key":"1600704abfba579c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-11 18:10:03","canto_approved_date":"2022-05-12 06:40:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-11 17:58:42","canto_added_date":"2015-02-11 15:28:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2G2.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-11","pdb_entries":[{"pdb_id":"1i9y","gene_chains":[{"gene_uniquename":"SPBC2G2.02","chain":"A","position":"534-880"}],"title":"CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 5-PHOSPHATASE DOMAIN (IPP5C) OF SPSYNAPTOJANIN","entry_authors":"Tsujishita Y,Guo S,Stolz L,York JD,Hurley JH","entry_authors_abbrev":"Tsujishita Y et al.","reference_uniquename":"PMID:11348594","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"1i9z","gene_chains":[{"gene_uniquename":"SPBC2G2.02","chain":"A","position":"534-880"}],"title":"CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 5-PHOSPHATASE DOMAIN (IPP5C) OF SPSYNAPTOJANIN IN COMPLEX WITH INOSITOL (1,4)-BISPHOSPHATE AND CALCIUM ION","entry_authors":"Tsujishita Y,Guo S,Stolz L,York JD,Hurley JH","entry_authors_abbrev":"Tsujishita Y et al.","reference_uniquename":"PMID:11348594","experimental_method":"X-ray","resolution":"1.8"}]},{"uniquename":"PMID:30206188","title":"Opposing kinesin complexes queue at plus tips to ensure microtubule catastrophe at cell ends.","citation":"EMBO Rep 2018 Nov;19(11)","abstract":"In fission yeast, the lengths of interphase microtubule (iMT) arrays are adapted to cell length to maintain cell polarity and to help centre the nucleus and cell division ring. Here, we show that length regulation of iMTs is dictated by spatially regulated competition between MT-stabilising Tea2/Tip1/Mal3 (Kinesin-7) and MT-destabilising Klp5/Klp6/Mcp1 (Kinesin-8) complexes at iMT plus ends. During MT growth, the Tea2/Tip1/Mal3 complex remains bound to the plus ends of iMT bundles, thereby restricting access to the plus ends by Klp5/Klp6/Mcp1, which accumulate behind it. At cell ends, Klp5/Klp6/Mcp1 invades the space occupied by the Tea2/Tip1/Tea1 kinesin complex triggering its displacement from iMT plus ends and MT catastrophe. These data show that  in vivo , whilst an iMT length-dependent model for catastrophe factor accumulation has validity, length control of iMTs is an emergent property reflecting spatially regulated competition between distinct kinesin complexes at the MT plus tip.","doi":"10.15252/embr.201846196","authors":"Meadows JC, Messin LJ, Kamnev A, Lancaster TC, Balasubramanian MK, Cross RA, Millar JB","authors_abbrev":"Meadows JC et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-09-13","publication_year":"2018","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-09-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012329","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU006854","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12723602","title":"Characterization of the Prr1 response regulator with special reference to sexual development in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2003 Mar;67(3):547-55","abstract":"The histidine (His)-to-Aspartate (Asp) phosphorelay is a paradigm of intracellular signaling systems through protein phosphorylation in both prokaryotes and eukaryotes. The fission yeast Schizosaccharomyces pombe has three histidine kinases (Phk1/Mak2, Phk2/Mak3, and Phk3/Mak1), together with two response regulators (Mcs4 and Prr1). The results of recent extensive studies suggested that these His-to-Asp phosphorelay components are involved in oxidative stress responses through the transcriptional regulation of several scavenger genes for toxic free radicals. It was also suggested that they were somehow implicated in control of both the mitotic and meiotic cell proliferations. Among these S. pombe His-to-Asp phosphorelay components, however, the function of Prr1 is less clear. We here characterized a mutant, named prr1-D418N, specifying an altered Prr1 protein that presumably acts as a gain-of-function (or constitutive-active) mutant, with special reference to sexual development. The mutant cells showed a striking phenotype in that they underwent mating even in a nitrogen-sufficient medium, under which conditions the wild-type cells hardly did so. Furthermore, the mutant cells underwent mating very rapidly in a nitrogen-deficient medium. Under anaerobic (or micro-aerobic) growth conditions, the wild-type cells were not capable of undergoing sexual development even in a nitrogen-deficient medium. The prr1-D418N cells underwent mating efficiently under such anaerobic growth conditions. Taken these together, it was suggested that the function of Prr1 is closely linked to the well-characterized signaling pathways for induction of the sexual development, in a way that this response regulator regulates a critical step of the initiation of meiosis through activating the transcription of ste11+, mam2+, and mei2+, in S. pombe.","authors":"Nakamichi N, Yanada H, Aiba H, Aoyama K, Ohmiya R, Mizuno T","authors_abbrev":"Nakamichi N et al.","pubmed_publication_date":"Mar 2003","pubmed_entrez_date":"2003-05-02","publication_year":"2003","canto_session_key":"9878a4d6e46a6189","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-04 09:48:21","canto_approved_date":"2026-04-08 11:04:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-25 15:11:19","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.08","SPAC24B11.06c","SPAC11H11.04","SPAC27D7.03c","SPCC74.06","SPAC8C9.14","SPAC27E2.09","SPBC32C12.02"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2017-08-04"},{"uniquename":"PMID:36963491","title":"The yeast Gdt1 protein mediates the exchange of H +  for Ca 2+  and Mn 2+  influencing the Golgi pH.","citation":"J Biol Chem 2023 May;299(5):104628","abstract":"The GDT1 family is broadly spread and highly conserved among living organisms. GDT1 members have functions in key processes like glycosylation in humans and yeasts and photosynthesis in plants. These functions are mediated by their ability to transport ions. While transport of Ca 2+  or Mn 2+  is well established for several GDT1 members, their transport mechanism is poorly understood. Here, we demonstrate that H +  ions are transported in exchange for Ca 2+  and Mn 2+  cations by the Golgi-localized yeast Gdt1 protein. We performed direct transport measurement across a biological membrane by expressing Gdt1p in Lactococcus lactis bacterial cells and by recording either the extracellular pH or the intracellular pH during the application of Ca 2+ , Mn 2+  or H +  gradients. Besides, in vivo cytosolic and Golgi pH measurements were performed in Saccharomyces cerevisiae with genetically encoded pH probes targeted to those subcellular compartments. These data point out that the flow of H +  ions carried by Gdt1p could be reversed according to the physiological conditions. Together, our experiments unravel the influence of the relative concentration gradients for Gdt1p-mediated H +  transport and pave the way to decipher the regulatory mechanisms driving the activity of GDT1 orthologs in various biological contexts.","doi":"10.1016/j.jbc.2023.104628","authors":"Deschamps A, Thines L, Colinet AS, Stribny J, Morsomme P","authors_abbrev":"Deschamps A et al.","pubmed_publication_date":"May 2023","pubmed_entrez_date":"2023-03-24","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC186.05c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33326250","title":"Time-varying mobility and turnover of actomyosin ring components during cytokinesis in  Schizosaccharomyces pombe .","citation":"Mol Biol Cell 2021 Feb 01;32(3):237-246","abstract":"Cytokinesis in many eukaryotes is dependent on a contractile actomyosin ring (AMR), composed of F-actin, myosin II, and other actin and myosin II regulators. Through fluorescence recovery after photobleaching experiments, many components of the AMR have been shown to be mobile and to undergo constant exchange with the cytosolic pools. However, how the mobility of its components changes at distinct stages of mitosis and cytokinesis has not been addressed. Here, we describe the mobility of eight  Schizosaccharomyces pombe  AMR proteins at different stages of mitosis and cytokinesis using an approach we have developed. We identified three classes of proteins, which showed 1) high (Ain1, Myo2, Myo51), 2) low (Rng2, Mid1, Myp2, Cdc12), and 3) cell cycle-dependent (Cdc15) mobile fractions. We observed that the F-BAR protein Cdc15 undergoes a 20-30% reduction in its mobile fraction after spindle breakdown and initiation of AMR contraction. Moreover, our data indicate that this change in Cdc15 mobility is dependent on the septation initiation network (SIN). Our work offers a novel strategy for estimating cell cycle-dependent mobile protein fractions in cellular structures and provides a valuable dataset, that is of interest to researchers working on cytokinesis.","doi":"10.1091/mbc.E20-09-0588","authors":"Kamnev A, Palani S, Zambon P, Cheffings T, Burroughs N, Balasubramanian MK","authors_abbrev":"Kamnev A et al.","pubmed_publication_date":"01 Feb 2021","pubmed_entrez_date":"2020-12-16","publication_year":"2021","canto_session_key":"582fad968b2c70f7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-12-18 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17637564","title":"The TSC/Rheb/TOR signaling pathway in fission yeast and mammalian cells: temperature sensitive and constitutive active mutants of TOR.","citation":"Cell Cycle 2007 Jul 15;6(14):1692-5","abstract":"The TSC/Rheb/TOR signaling pathway plays important roles in growth and cell cycle regulation. The main player TOR belongs to the PI3K-related protein kinase family. Recent studies utilizing fission yeast Tor2 have led to the identification of a number of amino acid changes that lead to inactivation as well as activation of TOR kinase. Also, constitutive active mutations in its upstream regulator, Rheb, have been identified. Isolation and characterization of temperature sensitive Tor2 mutants have established that this kinase functions as a key switch that determines cell fate between growth and sexual development. Introduction of Tor2 activating mutations into mTOR conferred nutrient independent activation of mTOR. Interestingly, these studies point to regions of TOR kinase important for its function.","authors":"Aspuria PJ, Sato T, Tamanoi F","authors_abbrev":"Aspuria PJ et al.","pubmed_publication_date":"15 Jul 2007","pubmed_entrez_date":"2007-07-20","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19185548","title":"The role of novel genes rrp1(+) and rrp2(+) in the repair of DNA damage in Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2009 May 01;8(5):627-36","abstract":"We identified two predicted proteins in Schizosaccharomyces pombe, Rrp1 (SPAC17A2.12) and Rrp2 (SPBC23E6.02) that share 34% and 36% similarity to Saccharomyces cerevisiae Ris1p, respectively. Ris1p is a DNA-dependent ATP-ase involved in gene silencing and DNA repair. Rrp1 and Rrp2 also share similarity with S. cerevisiae Rad5 and S. pombe Rad8, containing SNF2-N, RING finger and Helicase-C domains. To investigate the function of the Rrp proteins, we studied the DNA damage sensitivities and genetic interactions of null mutants with known DNA repair mutants. Single Deltarrp1 and Deltarrp2 mutants were not sensitive to CPT, 4NQO, CDPP, MMS, HU, UV or IR. The double mutants Deltarrp1 Deltarhp51 and Deltarrp2 Deltarhp51 plus the triple Deltarrp1 Deltarrp2 Deltarhp51 mutant did not display significant additional sensitivity. However, the double mutants Deltarrp1 Deltarhp57 and Deltarrp2 Deltarhp57 were significantly more sensitive to MMS, CPT, HU and IR than the Deltarhp57 single mutant. The checkpoint response in these strains was functional. In S. pombe, Rhp55/57 acts in parallel with a second mediator complex, Swi5/Sfr1, to facilitate Rhp51-dependent DNA repair. Deltarrp1 Deltasfr1 and Deltarrp2 Deltasfr1 double mutants did not show significant additional sensitivity, suggesting a function for Rrp proteins in the Swi5/Sfr1 pathway of DSB repair. Consistent with this, Deltarrp1 Deltarhp57 and Deltarrp2 Deltarhp57 mutants, but not Deltarrp1 Deltasfr1 or Deltarrp2 Deltasfr1 double mutants, exhibited slow growth and aberrations in cell and nuclear morphology that are typical of Deltarhp51.","doi":"10.1016/j.dnarep.2008.12.008","authors":"Dziadkowiec D, Petters E, Dyjankiewicz A, Karpiński P, Garcia V, Watson A, Carr AM","authors_abbrev":"Dziadkowiec D et al.","pubmed_publication_date":"01 May 2009","pubmed_entrez_date":"2009-02-03","publication_year":"2009","canto_session_key":"025da8633ca22521","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-25 12:25:25","canto_approved_date":"2024-01-10 22:53:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-19 16:27:22","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC20H4.07","SPCC1259.13","SPBC28F2.07","SPAC17A2.12","SPBC23E6.02"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-01-25"},{"uniquename":"PMID:38499152","title":"Sls1 and Mtf2 mediate the assembly of the Mrh5C complex required for activation of cox1 mRNA translation.","citation":"J Biol Chem 2024 Mar 16;:107176","abstract":"Mitochondrial translation depends on mRNA-specific activators. In Schizosaccharomyces pombe, DEAD-box protein Mrh5, pentatricopeptide repeat (PPR) protein Ppr4, Mtf2, and Sls1 form a stable complex (designated Mrh5C) required for translation of mitochondrial DNA (mtDNA)-encoded cox1 mRNA, the largest subunit of the cytochrome c oxidase complex. However, how Mrh5C is formed and what role Mrh5C plays in cox1 mRNA translation have not been reported. To address these questions, we investigated the role of individual Mrh5C subunits in the assembly and function of Mrh5C. Our results revealed that Mtf2 and Sls1 form a subcomplex that serves as a scaffold to bring Mrh5 and Ppr4 together. Mrh5C binds to the small subunit of the mitoribosome (mtSSU), but each subunit could not bind to the mtSSU independently. Importantly, Mrh5C is required for the association of cox1 mRNA with the mtSSU. Finally, we investigated the importance of the signature DEAD-box in Mrh5. We found that the DEAD-box of Mrh5 is required for the association of Mrh5C and cox1 mRNA with the mtSSU. Unexpectedly, this motif is also required for the interaction of Mrh5 with other Mrh5C subunits. Altogether, our results suggest that Mrh5 and Ppr4 cooperate in activating the translation of cox1 mRNA. Our results also suggest that Mrh5C activates the translation of cox1 mRNA by promoting the recruitment of cox1 mRNA to the mtSSU.","doi":"10.1016/j.jbc.2024.107176","authors":"Wang Y, Jin T, Huang Y","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"16 Mar 2024","pubmed_entrez_date":"2024-03-18","publication_year":"2024","canto_session_key":"81cc9cd6e028de43","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying  Luo","canto_first_approved_date":"2024-10-28 14:53:32","canto_approved_date":"2025-04-28 07:24:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-10-26 17:38:31","canto_added_date":"2024-03-20 00:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying  Luo","community_curator":true,"annotation_count":76,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F8.02c","SPMIT.09","SPMIT.04","SPMIT.01","SPRRNA.02","SPBC1105.03c","SPRRNA.01","SPAC5D6.12","SPMIT.08","SPAP8A3.14c","SPBC25D12.06","SPMIT.10","SPMIT.07","SPMIT.11","SPAC4G9.17c","SPMIT.05","SPAC2F7.15","SPAC23A1.18c","SPAC8C9.06c"],"gene_count":19,"ltp_gene_count":4,"approved_date":"2024-10-28"},{"uniquename":"PMID:24036117","title":"Mitochondrial ribosomal RNA (rRNA) methyltransferase family members are positioned to modify nascent rRNA in foci near the mitochondrial DNA nucleoid.","citation":"J Biol Chem 2013 Oct 25;288(43):31386-99","abstract":"We have identified RNMTL1, MRM1, and MRM2 (FtsJ2) as members of the RNA methyltransferase family that may be responsible for the three known 2'-O-ribose modifications of the 16 S rRNA core of the large mitochondrial ribosome subunit. These proteins are confined to foci located in the vicinity of mtDNA nucleoids. They show distinct patterns of association with mtDNA nucleoids and/or mitochondrial ribosomes in cell fractionation studies. We focused on the role of the least studied protein in this set, RNMTL1, to show that this protein interacts with the large ribosomal subunit as well as with a series of non-ribosomal proteins that may be involved in coupling of the rate of rRNA transcription and ribosome assembly in mitochondria. siRNA-directed silencing of RNMTL1 resulted in a significant inhibition of translation on mitochondrial ribosomes. Our results are consistent with a role for RNMTL1 in methylation of G(1370) of human 16 S rRNA.","doi":"10.1074/jbc.M113.515692","authors":"Lee KW, Okot-Kotber C, LaComb JF, Bogenhagen DF","authors_abbrev":"Lee KW et al.","pubmed_publication_date":"25 Oct 2013","pubmed_entrez_date":"2013-09-17","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1347.13c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:14731542","title":"Cyclin-dependent kinases: a new cell cycle motif?","citation":"Trends Cell Biol 1991 Nov;1(5):117-21","abstract":"Increasing evidence suggests that the eukaryotic cell cycle is controlled at several checkpoints by different members of a novel class of protein kinase, the cyclin-dependent kinases. To phosphorylate their substrates, these enzymes bind to proteins of the cyclin family--proteins that are synthesized and degraded at specific points in each cell cycle. The most well known of these kinases is the 34 kDa product of the cdc2 gene in fission yeast, p34cdc2; however, several putative cyclin-dependent kinases have now been cloned or identified. Some of these closely resemble p34cdc2. Here we review these new proteins, their potential roles in the cell cycle and the cyclins with which they may interact.","authors":"Pines J, Hunter T","authors_abbrev":"Pines J et al.","pubmed_publication_date":"Nov 1991","pubmed_entrez_date":"1991-11-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D89139","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14739927","title":"Regulation of checkpoint kinases through dynamic interaction with Crb2.","citation":"EMBO J 2004 Jan 28;23(2):418-28","abstract":"ATR/Rad3-like kinases promote the DNA damage checkpoint through regulating Chk1 that restrains the activation of cyclin-dependent kinases. In fission yeast, Crb2, a BRCT-domain protein that is similar to vertebrate 53BP1, plays a crucial role in establishing this checkpoint. We report here that Crb2 regulates DNA damage checkpoint through temporal and dynamic interactions with Rad3, Chk1 and replication factor Cut5. The active complex formation between Chk1 and Crb2 is regulated by Rad3 and became maximal during the checkpoint arrest. Chk1 activation seems to need two steps of interaction changes: the loss of Rad3-Chk1 and Rad3-Crb2 interactions, and the association between hyperphosphorylated forms of Chk1 and Crb2. Chk1 is the major checkpoint kinase for the arrest of DNA polymerase mutants. The in vitro assay of Chk1 showed that its activation requires the presence of Crb2 BRCT. Hyperphosphorylation of Crb2 is also dependent on its intact BRCT. Finally, we show direct interaction between Rad3 and Crb2, which is inhibitory to Rad3 activity. Hence, Crb2 is the first to interact with both Rad3 and Chk1 kinases.","authors":"Mochida S, Esashi F, Aono N, Tamai K, O'Connell MJ, Yanagida M","authors_abbrev":"Mochida S et al.","pubmed_publication_date":"28 Jan 2004","pubmed_entrez_date":"2004-01-24","publication_year":"2004","canto_session_key":"45b6d1dcc31ecbde","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-03-20 14:35:22","canto_approved_date":"2022-02-01 17:35:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-18 15:17:33","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":55,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.04","SPBC25H2.13c","SPAC23C4.18c","SPAC24H6.05","SPCC1259.13","SPAC3H5.06c","SPBC216.05","SPBC342.05","SPCC18B5.11c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-03-20"},{"uniquename":"PMID:34486060","title":"Reciprocal stabilization of transcription factor binding integrates two signaling pathways to regulate fission yeast fbp1 transcription.","citation":"Nucleic Acids Res 2021 Sep 27;49(17):9809-9820","abstract":"Transcriptional regulation, a pivotal biological process by which cells adapt to environmental fluctuations, is achieved by the binding of transcription factors to target sequences in a sequence-specific manner. However, how transcription factors recognize the correct target from amongst the numerous candidates in a genome has not been fully elucidated. We here show that, in the fission-yeast fbp1 gene, when transcription factors bind to target sequences in close proximity, their binding is reciprocally stabilized, thereby integrating distinct signal transduction pathways. The fbp1 gene is massively induced upon glucose starvation by the activation of two transcription factors, Atf1 and Rst2, mediated via distinct signal transduction pathways. Atf1 and Rst2 bind to the upstream-activating sequence 1 region, carrying two binding sites located 45 bp apart. Their binding is reciprocally stabilized due to the close proximity of the two target sites, which destabilizes the independent binding of Atf1 or Rst2. Tup11/12 (Tup-family co-repressors) suppress independent binding. These data demonstrate a previously unappreciated mechanism by which two transcription-factor binding sites, in close proximity, integrate two independent-signal pathways, thereby behaving as a hub for signal integration.","doi":"10.1093/nar/gkab758","authors":"Koda W, Senmatsu S, Abe T, Hoffman CS, Hirota K","authors_abbrev":"Koda W et al.","pubmed_publication_date":"27 Sep 2021","pubmed_entrez_date":"2021-09-06","publication_year":"2021","canto_session_key":"d538275f69772537","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-09-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28882432","title":"Analysis of ambient pH stress response mediated by iron and copper intake in Schizosaccharomyces pombe.","citation":"J Biosci Bioeng 2018 Jan;125(1):92-96","abstract":"The molecular mechanism of tolerance to alkaline pH is well studied in model fungi Aspergillus nidulans and Saccharomyces cerevisiae. However, how fission yeast Schizosaccharomyces pombe survives under alkaline stress remains largely unknown, as the genes involved in the alkaline stress response pathways of A. nidulans and S. cerevisiae were not found in the genome of this organism. Since uptake of iron and copper into cells is important for alkaline tolerance in S. cerevisiae, here we examined whether iron and copper uptake processes were involved in conferring tolerance to alkaline stress in S. pombe. We first revealed that S. pombe wild-type strain could not grow at a pH higher than 6.7. We further found that the growths of mutants harboring disruption in the iron uptake-related gene frp1 + , fio1 +  or fip1 +  were severely inhibited under ambient pH stress condition. In contrast, derepression of these genes, by deletion of their repressor gene fep1 + , caused cells to acquire resistance to pH stress. Together, these results suggested that uptake of iron is essential for ambient pH tolerance in S. pombe. We also found that copper is required for the pH stress response because disruptants of ctr4 + , ctr5 + , ccc2 +  and cuf1 +  genes, all of which are needed for regulating intracellular Cu + , displayed ambient pH sensitivity. Furthermore, supplementing Fe 2+  and Cu 2+  ions to the culture media improved growth under ambient pH stress. Taken together, our results suggested that uptake of iron and copper is the crucial factor needed for the adaptation of S. pombe to ambient pH stress.","doi":"10.1016/j.jbiosc.2017.08.008","authors":"Higuchi Y, Mori H, Kubota T, Takegawa K","authors_abbrev":"Higuchi Y et al.","pubmed_publication_date":"Jan 2018","pubmed_entrez_date":"2017-09-09","publication_year":"2018","canto_session_key":"78ac09df4c6c5d08","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2018-01-17 19:19:40","canto_approved_date":"2018-01-17 19:19:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-16 00:18:13","canto_added_date":"2017-09-12 00:15:14","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4F6.09","SPAC1142.05","SPBC1683.10c","SPCC1393.10","SPBC29A3.01","SPAC23E2.01","SPAC1F7.07c","SPBC1683.09c","SPAC1F7.08","SPAC31A2.11c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2018-01-17"},{"uniquename":"PMID:32957622","title":"Catalase T-Deficient Fission Yeast Meiocytes Show Resistance to Ionizing Radiation.","citation":"Antioxidants (Basel) 2020 Sep 17;9(9)","abstract":"Environmental stress, reactive oxygen species (ROS), or ionizing radiation (IR) can induce adverse effects in organisms and their cells, including mutations and premature aging. DNA damage and its faulty repair can lead to cell death or promote cancer through the accumulation of mutations. Misrepair in germ cells is particularly dangerous as it may lead to alterations in developmental programs and genetic disease in the offspring. DNA damage pathways and radical defense mechanisms mediate resistance to genotoxic stresses. Here, we investigated, in the fission yeast  Schizosaccharomyces pombe , the role of the H 2 O 2 -detoxifying enzyme cytosolic catalase T (Ctt1) and the Fe 2+ /Mn 2+  symporter Pcl1 in protecting meiotic chromosome dynamics and gamete formation from radicals generated by ROS and IR. We found that wild-type and  pcl1 -deficient cells respond similarly to X ray doses of up to 300 Gy, while  ctt1 ∆ meiocytes showed a moderate sensitivity to IR but a hypersensitivity to hydrogen peroxide with cells dying at >0.4 mM H 2 O 2 . Meiocytes deficient for  pcl1 , on the other hand, showed a resistance to hydrogen peroxide similar to that of the wild type, surviving doses >40 mM. In all, it appears that in the absence of the main H 2 O 2 -detoxifying pathway  S. pombe  meiocytes are able to survive significant doses of IR-induced radicals.","doi":"10.3390/antiox9090881","authors":"Muhtadi R, Lorenz A, Mpaulo SJ, Siebenwirth C, Scherthan H","authors_abbrev":"Muhtadi R et al.","pubmed_publication_date":"17 Sep 2020","pubmed_entrez_date":"2020-09-22","publication_year":"2020","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-09-24 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1683.10c","SPCC757.07c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"EMBL:SPC08605","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27371599","title":"Immunofluorescence Microscopy of Schizosaccharomyces pombe Using Chemical Fixation.","citation":"Cold Spring Harb Protoc 2016 Jul 01;2016(7)","abstract":"Establishing the subcellular distribution of molecules of interest and the dynamics of their spatial control underpins all areas of cell and developmental biology. Although the ability to monitor the distribution of fluorescent fusion proteins has revolutionized cell and developmental biology, indirect immunofluorescence microscopy of fixed samples remains an essential complement to this approach. Immunofluorescence is often a more appropriate approach for the study of subcellular architecture. It avoids potential artifacts caused by studying fusion proteins, which might show altered function under stressful imaging conditions. Furthermore, the quantitative analysis of multiple cells in an unperturbed population by immunofluorescence invariably provides a more accurate assessment of the spatial and temporal control of a particular process than does the analysis of individual cells that is the hallmark of live-cell imaging. Parallel studies of living and fixed cells often provide complementary data sets, both of which can be considered necessary for a comprehensive understanding of molecular function. This protocol provides a method for the visualization of the Schizosaccharomyces pombe microtubule cytoskeleton by indirect immunofluorescence microscopy following chemical fixation with formaldehyde and glutaraldehyde. It includes discussion of common modifications used to monitor the distribution of other fission yeast antigens and forms a basis from which to develop protocols to localize new molecules of interest.","doi":"10.1101/pdb.prot091017","authors":"Hagan IM","authors_abbrev":"Hagan IM","pubmed_publication_date":"01 Jul 2016","pubmed_entrez_date":"2016-07-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-07-04 00:15:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD140","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30195534","title":"Metabolism of Schizosaccharomyces pombe under reduced osmotic stress conditions afforded by fed-batch alcoholic fermentation of white grape must.","citation":"Food Res Int 2018 Nov;113:401-406","abstract":"Strains of Schizosaccharomyces pombe are being increasingly investigated with regards to their grape winemaking potential either in combination with the typical production yeast, Saccharomyces cerevisiae, or in monoseptic fermentations. Their ethanol tolerance and ability to degrade L-malic acid is oenologically convenient but contrasts with the comparatively high acetic acid and acetaldehyde formation potential which is considered undesirable, especially in white winemaking. The purpose of this work was to investigate the performance of a selected S. pombe strain in monoseptic femerntations of white grape must. Traditional batch fermentations were compared with an innovative and automated fed-batch fermentation technique were sugar concentrations are kept low during fermentations to decrease sugar induced osmotic stress. Because of its known effect on growth and ethanol tolerance, the effect of Mg was also tested. While Mg supplementation was not shown to significantly influence residual values of sugars, ethanol, glycerol, organic acids and acetaldehyde, the application of the fed-batch technique led to a fundamental change in yeast physiology. While glycerol values were only slightly reduced, the fed-batch approach allowed obtaining wines devoid of acetic acid whose levels were considerable in wines produced by the traditional batch technique (0.6 g/L). The work demonstrates that the acetic acid metabolism of S. pombe is associated to sugar induced osmotic stress such as for S. cerevisiae, too, and may be controlled by application of suitable fermentation techniques for winemaking.","doi":"10.1016/j.foodres.2018.07.003","authors":"Roca-Domènech G, Cordero-Otero R, Rozès N, Cléroux M, Pernet A, Mira de Orduña R","authors_abbrev":"Roca-Domènech G et al.","pubmed_publication_date":"Nov 2018","pubmed_entrez_date":"2018-09-10","publication_year":"2018","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2018-09-11 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16877568","title":"Ancient origin, functional conservation and fast evolution of DNA-dependent RNA polymerase III.","citation":"Nucleic Acids Res 2006;34(13):3615-24","abstract":"RNA polymerase III contains seventeen subunits in yeasts (Saccharomyces cerevisiae and Schizosaccharomyces pombe) and in human cells. Twelve of them are akin to the core RNA polymerase I or II. The five other are RNA polymerase III-specific and form the functionally distinct groups Rpc31-Rpc34-Rpc82 and Rpc37-Rpc53. Currently sequenced eukaryotic genomes revealed significant homology to these seventeen subunits in Fungi, Animals, Plants and Amoebozoans. Except for subunit Rpc31, this also extended to the much more distantly related genomes of Alveolates and Excavates, indicating that the complex subunit organization of RNA polymerase III emerged at a very early stage of eukaryotic evolution. The Sch.pombe subunits were expressed in S.cerevisiae null mutants and tested for growth. Ten core subunits showed heterospecific complementation, but the two largest catalytic subunits (Rpc1 and Rpc2) and all five RNA polymerase III-specific subunits (Rpc82, Rpc53, Rpc37, Rpc34 and Rpc31) were non-functional. Three highly conserved RNA polymerase III-specific domains were found in the twelve-subunit core structure. They correspond to the Rpc17-Rpc25 dimer, involved in transcription initiation, to an N-terminal domain of the largest subunit Rpc1 important to anchor Rpc31, Rpc34 and Rpc82, and to a C-terminal domain of Rpc1 that presumably holds Rpc37, Rpc53 and their Rpc11 partner.","authors":"Proshkina GM, Shematorova EK, Proshkin SA, Zaros C, Thuriaux P, Shpakovski GV","authors_abbrev":"Proshkina GM et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2006-08-01","publication_year":"2006","canto_session_key":"8de205fc14dca860","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-05-25 14:44:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-05-25 14:44:21","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1E7.10","SPCC290.02","SPCC330.13"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2017-05-25"},{"uniquename":"PMID:8036497","title":"14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast.","citation":"Science 1994 Jul 22;265(5171):533-5","abstract":"During the cell cycle, DNA is replicated and segregated equally into two daughter cells. The DNA damage checkpoint ensures that DNA damage is repaired before mitosis is attempted. Genetic studies of the fission yeast Schizosaccharomyces pombe have identified two genes, rad24 and rad25, that are required for this checkpoint. These genes encode 14-3-3 protein homologs that together provide a function that is essential for cell proliferation. In addition, S. pombe rad24 null mutants, and to a lesser extent rad25 null mutants, enter mitosis prematurely, which indicates that 14-3-3 proteins have a role in determining the timing of mitosis.","authors":"Ford JC, al-Khodairy F, Fotou E, Sheldrick KS, Griffiths DJ, Carr AM","authors_abbrev":"Ford JC et al.","pubmed_publication_date":"22 Jul 1994","pubmed_entrez_date":"1994-07-22","publication_year":"1994","canto_session_key":"5638fe150cf68f6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-12 20:58:20","canto_approved_date":"2021-12-13 18:05:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-23 13:15:12","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A2.13c","SPCC1259.13","SPAC8E11.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-09-12"},{"uniquename":"PMID:21858190","title":"N-termini of fungal CSL transcription factors are disordered, enriched in regulatory motifs and inhibit DNA binding in fission yeast.","citation":"PLoS One 2011;6(8):e23650","abstract":"CSL (CBF1/RBP-Jκ/Suppressor of Hairless/LAG-1) transcription factors are the effector components of the Notch receptor signalling pathway, which is critical for metazoan development. The metazoan CSL proteins (class M) can also function in a Notch-independent manner. Recently, two novel classes of CSL proteins, designated F1 and F2, have been identified in fungi. The role of the fungal CSL proteins is unclear, because the Notch pathway is not present in fungi. In fission yeast, the Cbf11 and Cbf12 CSL paralogs play antagonistic roles in cell adhesion and the coordination of cell and nuclear division. Unusually long N-terminal extensions are typical for fungal and invertebrate CSL family members. In this study, we investigate the functional significance of these extended N-termini of CSL proteins.\nWe identify 15 novel CSL family members from 7 fungal species and conduct bioinformatic analyses of a combined dataset containing 34 fungal and 11 metazoan CSL protein sequences. We show that the long, non-conserved N-terminal tails of fungal CSL proteins are likely disordered and enriched in phosphorylation sites and PEST motifs. In a case study of Cbf12 (class F2), we provide experimental evidence that the protein is proteolytically processed and that the N-terminus inhibits the Cbf12-dependent DNA binding activity in an electrophoretic mobility shift assay.\nThis study provides insight into the characteristics of the long N-terminal tails of fungal CSL proteins that may be crucial for controlling DNA-binding and CSL function. We propose that the regulation of DNA binding by Cbf12 via its N-terminal region represents an important means by which fission yeast strikes a balance between the class F1 and class F2 paralog activities. This mode of regulation might be shared with other CSL-positive fungi, some of which are relevant to human disease and biotechnology.","doi":"10.1371/journal.pone.0023650","authors":"Převorovský M, Atkinson SR, Ptáčková M, McLean JR, Gould K, Folk P, Půta F, Bähler J","authors_abbrev":"Převorovský M et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-08-23","publication_year":"2011","canto_session_key":"72dd3fcf9aae482b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-29 10:56:37","canto_approved_date":"2021-11-08 15:48:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-11 09:13:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.13","SPCC736.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-01-29"},{"uniquename":"PMID:24463365","title":"Systematic screen for mutants resistant to TORC1 inhibition in fission yeast reveals genes involved in cellular ageing and growth.","citation":"Biol Open 2014 Feb 15;3(2):161-71","abstract":"Target of rapamycin complex 1 (TORC1), which controls growth in response to nutrients, promotes ageing in multiple organisms. The fission yeast Schizosaccharomyces pombe emerges as a valuable genetic model system to study TORC1 function and cellular ageing. Here we exploited the combinatorial action of rapamycin and caffeine, which inhibit fission yeast growth in a TORC1-dependent manner. We screened a deletion library, comprising ∼84% of all non-essential fission yeast genes, for drug-resistant mutants. This screen identified 33 genes encoding functions such as transcription, kinases, mitochondrial respiration, biosynthesis, intra-cellular trafficking, and stress response. Among the corresponding mutants, 5 showed shortened and 21 showed increased maximal chronological lifespans; 15 of the latter mutants showed no further lifespan increase with rapamycin and might thus represent key targets downstream of TORC1. We pursued the long-lived sck2 mutant with additional functional analyses, revealing that the Sck2p kinase functions within the TORC1 network and is required for normal cell growth, global protein translation, and ribosomal S6 protein phosphorylation in a nutrient-dependent manner. Notably, slow cell growth was associated with all long-lived mutants while oxidative-stress resistance was not.","doi":"10.1242/bio.20147245","authors":"Rallis C, López-Maury L, Georgescu T, Pancaldi V, Bähler J","authors_abbrev":"Rallis C et al.","pubmed_publication_date":"15 Feb 2014","pubmed_entrez_date":"2014-01-28","publication_year":"2014","canto_session_key":"95bc2a3172175b7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-10-17 08:30:46","canto_approved_date":"2021-02-08 09:47:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-17 08:30:39","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":107,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_24463365_phaf.tsv"}],"genes":["SPBC16D10.07c","SPBC16E9.12c","SPAC688.10","SPBC428.06c","SPAC22F3.09c","SPCC16C4.09","SPAC3A11.13","SPAC19G12.02c","SPCC1223.15c","SPAC3H8.07c","SPCC622.16c","SPAC9.07c","SPAC27D7.11c","SPBC29A10.16c","SPBC12C2.02c","SPBC3H7.03c","SPAC22A12.11","SPAC17C9.02c","SPAC1556.02c","SPCC777.13","SPCC550.03c","SPBC15C4.06c","SPAC9E9.10c","SPAC3H1.08c","SPBPB7E8.01","SPAC4G8.05","SPCC1753.02c","SPAC1A6.04c","SPBC1539.08","SPAC25A8.01c","SPAC328.03","SPCPB16A4.02c","SPAC19G12.08","SPAC13G7.02c","SPAC2F3.15","SPAC17H9.19c","SPCC1450.05c","SPBC21C3.08c","SPBC27.08c","SPCC188.02","SPBC16E9.13","SPBC577.02","SPAC22F3.13","SPBC27B12.05","SPCP1E11.05c","SPCC1739.10","SPCC1450.11c","SPCC4G3.11","SPBC11B10.08","SPBC1198.11c","SPCC1259.03","SPBC1D7.03","SPBP4H10.16c","SPAC12B10.09","SPAC9E9.09c","SPBP8B7.21","SPAC13A11.04c","SPBP8B7.27","SPBPB10D8.06c","SPBP35G2.11c","SPAC227.05","SPAC750.04c","SPCC18B5.10c","SPBC32F12.08c","SPAC824.02","SPBP23A10.16","SPAC23H4.17c","SPBC25B2.04c","SPAC3G9.08","SPBC20F10.10","SPAC1687.15","SPBC354.09c","SPCC16C4.11","SPBC3H7.10","SPAC17H9.13c","SPAC22E12.14c","SPAC6G9.08","SPBC3H7.13","SPBC1778.03c","SPBC409.20c","SPCC794.01c","SPAC3A12.09c","SPAC2F7.03c","SPCC18B5.01c","SPBC32H8.07","SPBC23E6.08","SPBC1A4.10c","SPBC1921.07c","SPAC6B12.09","SPBC56F2.10c","SPAC1B9.02c","SPCC18B5.07c","SPAC17C9.14","SPAC11G7.02","SPBC2G5.03","SPAC1399.04c","SPBC2F12.03c","SPBP35G2.08c","SPAC16.05c","SPBC13E7.06","SPBC354.13","SPBC27.06c","SPBC119.08","SPAC1783.07c","SPCC4F11.02","SPBC4F6.06","SPBC31F10.03","SPBC1921.03c","SPAC23H3.13c","SPAC806.07","SPCC1322.08","SPAC2G11.07c","SPCC162.12","SPBC31F10.10c","SPAC17C9.10","SPAC3H1.12c","SPAC6F12.12","SPBC20F10.07","SPAC15A10.09c","SPCC613.12c","SPBC36.07","SPBC2F12.11c","SPBC215.02","SPAC10F6.11c","SPAC13G6.09","SPBC428.03c","SPBC428.02c","SPAC23D3.09","SPAC3H5.07","SPAC4A8.09c","SPAC14C4.06c","SPAC17G6.08","SPAC2F7.08c","SPBC1773.17c","SPBC4C3.12","SPBC365.14c","SPAC23A1.19c","SPCC417.06c","SPBC14F5.08","SPBC12D12.06","SPAC521.03","SPAC12B10.05","SPBC16E9.14c","SPAC2C4.16c","SPCC24B10.12","SPCC285.11","SPAC1F3.02c","SPCC417.07c","SPBC11C11.08","SPAC6B12.12","SPAC21E11.04","SPAC20H4.10","SPAC20H4.07","SPBC13G1.10c","SPAC19A8.04","SPAC139.01c","SPBC29A3.07c","SPAC20H4.02","SPAC30.02c","SPBC1A4.01","SPAC630.13c","SPBC106.01","SPAC1142.08","SPBC2G2.07c","SPCC895.06","SPBC947.08c","SPCC4B3.15","SPBC19C2.13c","SPAC644.14c","SPCC31H12.08c","SPAC10F6.14c","SPAC4G8.13c","SPAC4G8.11c","SPBC1D7.01","SPAC17H9.08","SPCC594.05c","SPAC17A5.02c","SPBC428.04","SPAC19E9.02","SPCC1902.01","SPCC338.16","SPAC2F3.11","SPCC16A11.08","SPAC664.02c","SPBC2G2.01c","SPAC22H10.03c","SPAC23H3.05c","SPAC9G1.07","SPBC354.05c","SPAC13G7.13c","SPCC23B6.05c","SPCC1739.03","SPBC1718.07c","SPBC215.03c","SPAC57A7.08","SPBC23E6.01c","SPAC17C9.09c","SPAC56F8.02","SPAC589.08c","SPCC584.02","SPAC637.13c","SPAC1039.02","SPBC660.14","SPAC821.07c","SPBC21C3.02c","SPCC1235.11","SPCC736.07c","SPAC16E8.01","SPBC16D10.08c","SPAC3F10.04","SPAC6B12.08","SPBC215.07c","SPBC3B8.10c","SPAC750.01","SPCC306.04c","SPAC1D4.03c","SPAC227.17c","SPAC3H1.06c","SPAC959.08","SPAC9.05","SPAC31G5.18c","SPBC800.08","SPAC323.03c","SPBC947.10","SPBC29A10.10c","SPAC13F5.03c"],"gene_count":226,"ltp_gene_count":9,"approved_date":"2014-10-17"},{"uniquename":"PMID:23466674","title":"Mate and fuse: how yeast cells do it.","citation":"Open Biol 2013 Mar 06;3(3):130008","abstract":"Many cells are able to orient themselves in a non-uniform environment by responding to localized cues. This leads to a polarized cellular response, where the cell can either grow or move towards the cue source. Fungal haploid cells secrete pheromones to signal mating, and respond by growing a mating projection towards a potential mate. Upon contact of the two partner cells, these fuse to form a diploid zygote. In this review, we present our current knowledge on the processes of mating signalling, pheromone-dependent polarized growth and cell fusion in Saccharomyces cerevisiae and Schizosaccharomyces pombe, two highly divergent ascomycete yeast models. While the global architecture of the mating response is very similar between these two species, they differ significantly both in their mating physiologies and in the molecular connections between pheromone perception and downstream responses. The use of both yeast models helps enlighten both conserved solutions and species-specific adaptations to a general biological problem.","doi":"10.1098/rsob.130008","authors":"Merlini L, Dudin O, Martin SG","authors_abbrev":"Merlini L et al.","pubmed_publication_date":"06 Mar 2013","pubmed_entrez_date":"2013-03-08","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7628434","title":"A novel protein kinase gene ssp1+ is required for alteration of growth polarity and actin localization in fission yeast.","citation":"EMBO J 1995 Jul 17;14(14):3325-38","abstract":"Temperature-sensitive suppressor mutants were isolated from two fission yeast mutants defective in cell shape control: ppe1, encoding a type 2A-like protein phosphatase, and sts5, one of 11 staurosporine-supersensitive mutants. Complementation tests showed that suppression was due to two chromosomal loci, ssp1 and ssp2. Cells of the ssp1 mutant grown at the restrictive temperature arrested uniformly with an elongated cell body and a 2C content of DNA. Interestingly, these mutant cells grew only in a monopolar manner. At a specific point in the G2 phase of the cell cycle, wild-type cells exhibit a drastic alteration in growth polarity, from mono- to bipolar. This change coincides with the distribution of cortical actin from one end of the cell to both ends. In the ssp1 mutant cells, cortical actin was localized only at one end, suggesting that the mutant fails to change growth polarity. Nucleotide sequence determination showed that ssp1+ encodes a novel protein kinase. Ectopic overexpression of ssp1+ resulted in an altered cell morphology and cortical actin was randomly dispersed within the cells. Immunocytological analysis revealed that the protein was primarily localized in the cytoplasm and that half of the protein existed in an insoluble fraction. These results show that the dynamics of actin-based growth polarity during the cell cycle are regulated, at least in part, by a novel set of protein kinases and phosphatases.","authors":"Matsusaka T, Hirata D, Yanagida M, Toda T","authors_abbrev":"Matsusaka T et al.","pubmed_publication_date":"17 Jul 1995","pubmed_entrez_date":"1995-07-17","publication_year":"1995","canto_session_key":"5f26e1abdd6bd258","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-07 14:55:38","canto_approved_date":"2026-01-29 13:34:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-20 10:57:20","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPCC297.03","SPCC16C4.09","SPCC74.03c","SPCC1739.12"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-10-07"},{"uniquename":"PMID:41214992","title":"Aldehyde metabolism in Maotai-flavor Baijiu: insights from integrated metagenomic and metaproteomic analyses.","citation":"Food Res Int 2025 Dec;221(Pt 3):117518","abstract":"Acetaldehyde and acetal are crucial to the flavor of Maotai-flavor Baijiu, affecting aroma release and sauce-aroma traits. Targeted control of acetaldehyde metabolic flux is critical for stabilizing base liquor quality. However, the diversity of acetaldehyde-metabolizing enzymes and their microbial drivers remain uncharacterized, critically impeding precision control. This study selected the third production round to systematically investigate acetaldehyde accumulation dynamics and metabolic mechanisms. Time-resolved profiling showed that acetaldehyde and acetal concentrations display an initial rise, followed by a decline and stabilization. By integrated metagenomic and metaproteomic analyses, we confirmed that the metabolic network comprised two biosynthetic and three conversion pathways. The dominant biosynthetic pathway featured pyruvate decarboxylase (PDC)-catalyzed decarboxylation, while ethanolamine ammonia-lyase contributed minimally. Among conversion pathways, NADH-dependent alcohol dehydrogenase (NADH-ADH) reduction to ethanol predominated, with lower-flux oxidation to acetate and acetyl-CoA. Dynamic enzyme profiling revealed that PDC activity preceded the activation of NADH-ADH during stacking fermentation, resulting in a temporal mismatch between aldehyde production and consumption, which led to metabolic retention. During pit fermentation, acetaldehyde was more efficiently converted to ethanol through upregulation of NADH-ADH and NADH/NAD +  ratio. As main contributors of PDC and NADH-ADH, Schizosaccharomyces pombe and Saccharomyces cerevisiae exhibited dual regulatory roles in acetaldehyde metabolism, with their metabolic mode shifts governed by dissolved oxygen and the NADH/NAD +  ratio. Microbial interaction analysis and simulated fermentation confirmed that Pichia kudriavzevii synergized with Saccharomyces cerevisiae and Schizosaccharomyces pombe, driving rapid acetaldehyde accumulation during the stacking fermentation. These findings establish a theoretical framework for optimizing brewing processes and enhancing base liquor quality.","doi":"10.1016/j.foodres.2025.117518","authors":"Li C, Yang F, Han Y, Yang C, Qin X, Zheng H, Chen L, Lu J, Zhang C, Lu F, Wang L","authors_abbrev":"Li C et al.","pubmed_publication_date":"Dec 2025","pubmed_entrez_date":"2025-11-11","publication_year":"2025","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2025-11-12 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17363897","title":"Mus81 cleavage of Holliday junctions: a failsafe for processing meiotic recombination intermediates?","citation":"EMBO J 2007 Apr 04;26(7):1891-901","abstract":"The Holliday junction (HJ) is a central intermediate of homologous recombination. Its cleavage is critical for the formation of crossover recombinants during meiosis, which in turn helps to establish chiasmata and promote genetic diversity. Enzymes that cleave HJs, called HJ resolvases, have been identified in all domains of life except eukaryotic nuclei. Controversially, the Mus81-Eme1 endonuclease has been proposed to be an example of a eukaryotic nuclear resolvase. However, hitherto little or no HJ cleavage has been detected in recombinant preparations of Mus81-Eme1. Here, we report the purification of active forms of recombinant Schizosaccharomyces pombe Mus81-Eme1 and Saccharomyces cerevisiae Mus81-Mms4, which display robust HJ cleavage in vitro, which, in the case of Mus81-Eme1, is as good as the archetypal HJ resolvase RuvC in single turnover kinetic analysis. We also present genetic evidence that suggests that this activity might be utilised as a back-up to Mus81-Eme1's main activity of cleaving nicked HJs during meiosis in S. pombe.","authors":"Gaskell LJ, Osman F, Gilbert RJ, Whitby MC","authors_abbrev":"Gaskell LJ et al.","pubmed_publication_date":"04 Apr 2007","pubmed_entrez_date":"2007-03-17","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18440981","title":"Involvement of fission yeast Clr6-HDAC in regulation of the checkpoint kinase Cds1.","citation":"Nucleic Acids Res 2008 Jun;36(10):3311-9","abstract":"Modification of the N-terminal tail of histones is required for various nuclear processes. Here, we show that fission yeast Clr6-HDAC (histone deacetylase) regulates the checkpoint kinase Cds1 when DNA replication encounters a stressful condition. We found that the global level of acetylation of histone H4 was constant throughout the normal cell cycle, but was reduced significantly when the cell recovered from the HU-induced cell cycle arrest (or slow DNA replication). We identified the Clr6-HDAC as a component responsible for the reduction in the level of the H4 acetylation. Although DNA replication was completed, the HU-induced cell cycle arrest could not be released even after removal of HU in the clr6-1 mutant. Under this experimental condition, Cds1 kinase was maintained active and remained bound tightly to chromatin. We also demonstrated that Cds1 was active even after treatment with caffeine, an inhibitor for ATM/ATR that is an activator of Cds1. These results indicate that inactivation of Cds1 requires functional Clr6-HDAC independently of the conventional DNA replication checkpoint. When DNA replication is impeded, Clr6-HDAC activity may monitor damage on chromatin structure/environment, which is required for inactivation of Cds1.","doi":"10.1093/nar/gkn203","authors":"Kunoh T, Habu T, Matsumoto T","authors_abbrev":"Kunoh T et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-04-29","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31768990","title":"Reconstitution of the Schizosaccharomyces pombe RNA Exosome.","citation":"Methods Mol Biol 2020;2062:449-465","abstract":"In this chapter, we describe methods to clone, express, purify, and reconstitute active S. pombe RNA exosomes. Reconstitution procedures are similar to methods that have been successful for the human and budding yeast exosome systems using protein subunits purified from the recombinant host E. coli. By applying these strategies, we can successfully reconstitute the S. pombe noncatalytic exosome core as well as complexes that contain the exoribonucleases Dis3 and Rrp6, cofactors Cti1 (equivalent to budding yeast Rrp47) and Mpp6 as well as the RNA helicase Mtr4.","doi":"10.1007/978-1-4939-9822-7_22","authors":"Januszyk K, Lima CD","authors_abbrev":"Januszyk K et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2019-11-27","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-11-28 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2000373","title":"Complementation of a yeast cell cycle mutant by an alfalfa cDNA encoding a protein kinase homologous to p34cdc2.","citation":"Proc Natl Acad Sci U S A 1991 Mar 01;88(5):1636-40","abstract":"The cdc2 protein kinase plays a central role in control of the eukaryotic cell cycle of animals and yeasts. We have isolated a cDNA clone (cdc2Ms) from alfalfa (Medicago sativa L.) that is homologous to the yeast cdc2/CDC28 genes. The encoded protein is 64% identical to the yeast and mammalian counterparts and shows all the prominent structural features known from these organisms. Antibody raised against a 16-amino acid synthetic peptide with crossreactivity against p34 proteins recognized a 34-kilodalton protein in extracts of alfalfa cells. When transferred into a fission yeast, the plant cdc2 homolog can complement a temperature-sensitive cdc2 mutant. Northern analysis revealed higher transcript levels in shoots and suspension cultures than in roots. In addition to the dominant transcript of 1.4 kilobases detected in the poly(A)+fraction, 2.5- and 1.2-kilobase transcripts were detected in total RNA preparations from shoots or somatic embryos. Suspension cultures that were induced to form somatic embryos by an auxin (2,4-dichlorophenoxyacetic acid) showed fluctuations in transcription pattern during the induction period and embryogenesis.","authors":"Hirt H, Páy A, Györgyey J, Bakó L, Németh K, Bögre L, Schweyen RJ, Heberle-Bors E, Dudits D","authors_abbrev":"Hirt H et al.","pubmed_publication_date":"01 Mar 1991","pubmed_entrez_date":"1991-03-01","publication_year":"1991","canto_session_key":"b9573a8f56efe3bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 12:52:14","canto_session_submitted_date":"2012-03-03 12:51:54","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:9201720","title":"Ran1 functions to control the Cdc10/Sct1 complex through Puc1.","citation":"Mol Biol Cell 1997 Jun;8(6):1117-28","abstract":"We have undertaken a biochemical analysis of the regulation of the G1/S-phase transition and commitment to the cell cycle in the fission yeast Schizosaccharomyces pombe. The execution of Start requires the activity of the Cdc2 protein kinase and the Sct1/Cdc10 transcription complex. Progression through G1 also requires the Ran1 protein kinase whose inactivation leads to activation of the meiotic pathway under conditions normally inhibitory to this process. We have found that in addition to Cdc2, Sct1/Cdc10 complex formation requires Ran1. We demonstrate that the Puc1 cyclin associates with Ran1 and Cdc10 in vivo and that the Ran1 protein kinase functions to control the association between Puc1 and Cdc10. In addition, we present evidence that the phosphorylation state of Cdc10 is altered upon inactivation of Ran1. These results provide biochemical evidence that demonstrate one mechanism by which the Ran1 protein kinase serves to control cell fate through Cdc10 and Puc1.","authors":"Caligiuri M, Connolly T, Beach D","authors_abbrev":"Caligiuri M et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"00d3dfd9f3b6d94e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-09 15:02:47","canto_approved_date":"2020-01-27 15:52:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-09 15:02:39","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19F5.01c","SPAC27D7.03c","SPBC336.12c","SPAC1F7.05","SPBC725.16","SPBC19C2.05","SPBC11B10.09","SPAPB2B4.03","SPCC4E9.02"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2018-06-09"},{"uniquename":"PMID:4698210","title":"Biosynthesis of branched-chain amino acids in Schizosaccharomyces pombe: properties of acetohydroxy acid synthetase.","citation":"J Bacteriol 1973 Apr;114(1):332-40","abstract":"The regulatory properties of acetohydroxy acid synthetase (AHAS), the first enzyme in the biosynthetic pathway to valine and the second in the isoleucine pathway, were investigated in the fission yeast Schizosaccharomyces pombe. The enzyme was partially purified from crude extracts by protamine sulfate treatment, ammonium sulfate fractionation, and gel filtration through Sephadex G-25. AHAS from S. pombe is unique in that its activity shows a single peak around pH 6.5; high sensitivity to feedback inhibition by valine at this pH (K(i) = 0.1 mM) indicates that the enzyme is involved in valine biosynthesis. Pyruvate saturation kinetics of AHAS extracted from cells grown on glycerol as sole carbon and energy source were normal and hyperbolic. In contrast, the enzyme from glucose-grown cells exhibited sigmoidal saturation kinetics, an effect which disappeared when the synthetase from such cells was partially purified. This phenomenon was shown to be due to competition for pyruvate between AHAS and pyruvate decarboxylase; the latter enzyme is present in large amounts in cells fermenting glucose. Valine inhibition is noncompetitive in nature, and this effector exhibits homotropic cooperative effects; isoleucine is a less-potent inhibitor of AHAS activity. Mercurial treatment reversibly desensitized the enzyme to valine inhibition. On the basis of these data, the S. pombe AHAS appears to be an allosteric regulatory enzyme with the properties of a negative V system.","authors":"McDonald RA, Satyanarayana T, Kaplan JG","authors_abbrev":"McDonald RA et al.","pubmed_publication_date":"Apr 1973","pubmed_entrez_date":"1973-04-01","publication_year":"1973","canto_session_key":"e83166112a9102b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-09-25 13:43:42","canto_approved_date":"2026-01-14 23:48:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-25 13:31:35","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-25"},{"uniquename":"PMID:26682798","title":"The spliceosome-associated protein Nrl1 suppresses homologous recombination-dependent R-loop formation in fission yeast.","citation":"Nucleic Acids Res 2016 Feb 29;44(4):1703-17","abstract":"The formation of RNA-DNA hybrids, referred to as R-loops, can promote genome instability and cancer development. Yet the mechanisms by which R-loops compromise genome instability are poorly understood. Here, we establish roles for the evolutionarily conserved Nrl1 protein in pre-mRNA splicing regulation, R-loop suppression and in maintaining genome stability. nrl1Δ mutants exhibit endogenous DNA damage, are sensitive to exogenous DNA damage, and have defects in homologous recombination (HR) repair. Concomitantly, nrl1Δ cells display significant changes in gene expression, similar to those induced by DNA damage in wild-type cells. Further, we find that nrl1Δ cells accumulate high levels of R-loops, which co-localize with HR repair factors and require Rad51 and Rad52 for their formation. Together, our findings support a model in which R-loop accumulation and subsequent DNA damage sequesters HR factors, thereby compromising HR repair at endogenously or exogenously induced DNA damage sites, leading to genome instability.","doi":"10.1093/nar/gkv1473","authors":"Aronica L, Kasparek T, Ruchman D, Marquez Y, Cipak L, Cipakova I, Anrather D, Mikolaskova B, Radtke M, Sarkar S, Pai CC, Blaikley E, Walker C, Shen KF, Schroeder R, Barta A, Forsburg SL, Humphrey TC","authors_abbrev":"Aronica L et al.","pubmed_publication_date":"29 Feb 2016","pubmed_entrez_date":"2015-12-20","publication_year":"2016","canto_session_key":"ccc014e047fc0f29","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-12-21 01:19:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC364.03","SPAC2C4.03c","SPBC1711.17","SPAC4F8.12c","SPBC215.12","SPBC19C2.14","SPCC550.02c","SPCC188.11","SPBC13E7.01","SPBC216.05","SPAC1783.08c","SPAC20H4.06c","SPAC29A4.08c","SPAC140.04","SPBC16H5.10c","SPBC6B1.10","SPAC17A2.08c","SPAC10F6.02c","SPAC4A8.09c","SPBC211.02c","SPAC644.12","SPAC17H9.02","SPBC1289.11","SPBC20F10.05","SPBC31F10.11c","SPCC576.11","SPAC30D11.10","SPAC9.03c","SPAC1486.03c"],"gene_count":29,"ltp_gene_count":29},{"uniquename":"PMID:38479839","title":"Coordination of histone chaperones for parental histone segregation and epigenetic inheritance.","citation":"Genes Dev 2024 Mar 13;","abstract":"Chromatin-based epigenetic memory relies on the accurate distribution of parental histone H3-H4 tetramers to newly replicated DNA strands. Mcm2, a subunit of the replicative helicase, and Dpb3/4, subunits of DNA polymerase ε, govern parental histone H3-H4 deposition to the lagging and leading strands, respectively. However, their contribution to epigenetic inheritance remains controversial. Here, using fission yeast heterochromatin inheritance systems that eliminate interference from initiation pathways, we show that a Mcm2 histone binding mutation severely disrupts heterochromatin inheritance, while mutations in Dpb3/4 cause only moderate defects. Surprisingly, simultaneous mutations of Mcm2 and Dpb3/4 stabilize heterochromatin inheritance. eSPAN (enrichment and sequencing of protein-associated nascent DNA) analyses confirmed the conservation of Mcm2 and Dpb3/4 functions in parental histone H3-H4 segregation, with their combined absence showing a more symmetric distribution of parental histone H3-H4 than either single mutation alone. Furthermore, the FACT histone chaperone regulates parental histone transfer to both strands and collaborates with Mcm2 and Dpb3/4 to maintain parental histone H3-H4 density and faithful heterochromatin inheritance. These results underscore the importance of both symmetric distribution of parental histones and their density at daughter strands for epigenetic inheritance and unveil distinctive properties of parental histone chaperones during DNA replication.","doi":"10.1101/gad.351278.123","authors":"Fang Y, Hua X, Shan CM, Toda T, Qiao F, Zhang Z, Jia S","authors_abbrev":"Fang Y et al.","pubmed_publication_date":"13 Mar 2024","pubmed_entrez_date":"2024-03-13","publication_year":"2024","canto_session_key":"8bd8f9428a9ef0ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Songtao Jia","canto_first_approved_date":"2024-04-18 09:44:51","canto_approved_date":"2024-05-17 13:03:03","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-21 18:22:13","canto_added_date":"2024-03-15 00:25:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":39,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Songtao Jia","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC609.05","SPBC1105.11c","SPBC3D6.09","SPCC1795.05c","SPBC4.04c","SPCC188.13c","SPCC16C4.22"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2024-04-18"},{"uniquename":"PMID:21247877","title":"A piggyBac transposon-based mutagenesis system for the fission yeast Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2011 Mar;39(6):e40","abstract":"The TTAA-specific transposon piggyBac (PB), originally isolated from the cabbage looper moth, Trichoplusia ni, has been utilized as an insertional mutagenesis tool in various eukaryotic organisms. Here, we show that PB transposes in the fission yeast Schizosaccharomyces pombe and leaves almost no footprints. We developed a PB-based mutagenesis system for S. pombe by constructing a strain with a selectable transposon excision marker and an integrated transposase gene. PB transposition in this strain has low chromosomal distribution bias as shown by deep sequencing-based insertion site mapping. Using this system, we obtained loss-of-function alleles of klp5 and klp6, and a gain-of-function allele of dam1 from a screen for mutants resistant to the microtubule-destabilizing drug thiabendazole. From another screen for cdc25-22 suppressors, we obtained multiple alleles of wee1 as expected. The success of these two screens demonstrated the usefulness of this PB-mediated mutagenesis tool for fission yeast.","doi":"10.1093/nar/gkq1358","authors":"Li J, Zhang JM, Li X, Suo F, Zhang MJ, Hou W, Han J, Du LL","authors_abbrev":"Li J et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-01-21","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19846658","title":"Bub3p facilitates spindle checkpoint silencing in fission yeast.","citation":"Mol Biol Cell 2009 Dec;20(24):5096-105","abstract":"Although critical for spindle checkpoint signaling, the role kinetochores play in anaphase promoting complex (APC) inhibition remains unclear. Here we show that spindle checkpoint proteins are severely depleted from unattached kinetochores in fission yeast cells lacking Bub3p. Surprisingly, a robust mitotic arrest is maintained in the majority of bub3 Delta cells, yet they die, suggesting that Bub3p is essential for successful checkpoint recovery. During recovery, two defects are observed: (1) cells mis-segregate chromosomes and (2) anaphase onset is significantly delayed. We show that Bub3p is required to activate the APC upon inhibition of Aurora kinase activity in checkpoint-arrested cells, suggesting that Bub3p is required for efficient checkpoint silencing downstream of Aurora kinase. Together, these results suggest that spindle checkpoint signals can be amplified in the nucleoplasm, yet kinetochore localization of spindle checkpoint components is required for proper recovery from a spindle checkpoint-dependent arrest.","authors":"Vanoosthuyse V, Meadows JC, van der Sar SJ, Millar JB, Hardwick KG","authors_abbrev":"Vanoosthuyse V et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-10-23","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27F1.04c","SPAC17H9.20","SPAC23H3.08c","SPBC26H8.07c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:39473973","title":"Limiting 20S proteasome assembly leads to unbalanced nucleo-cytoplasmic distribution of 26S/30S proteasomes and chronic proteotoxicity.","citation":"iScience 2024 Nov 15;27(11):111095","abstract":"In addition to the degradation of cell-cycle proteins, short-lived, damaged, or unfolded proteins are constantly cleared from cells by the proteasome. During proliferation, the proteasome localizes to the nucleus and cytoplasm; however, the functional relevance of this compartmentalization remains unclear. Here, we show that folding stress increases 26S/30S proteasome activity, which correlates with the upregulation of Ump1, a chaperone involved in 20S assembly. Conversely,  ump1  inactivation results in a drop of 20S and 26S/30S proteasomes. Limited 26S/30S proteasomes in  ump1 -deficient cells accumulate in the nucleus where they degrade mitotic substrates, allowing cells to proceed through mitosis; however, these cells present cytoplasmic aggregates and constitutive activation of the heat shock response. Thus, our data suggest that an increase in proteasome assembly induced by folding stress functions as an additional layer to proteasome regulation and highlight the importance of balanced proteasome compartmentalization to sustain cell proliferation while maintaining proper cytoplasmic proteostasis.","doi":"10.1016/j.isci.2024.111095","authors":"Ruiz-Romero G, Berdún MD, Hochstrasser M, Salas-Pino S, Daga RR","authors_abbrev":"Ruiz-Romero G et al.","pubmed_publication_date":"15 Nov 2024","pubmed_entrez_date":"2024-10-30","publication_year":"2024","canto_session_key":"8742732cbb42bffd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Gabriel Ruiz Romero","canto_first_approved_date":"2025-03-28 12:24:18","canto_approved_date":"2025-03-28 12:24:18","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-03-25 18:55:22","canto_added_date":"2025-03-01 10:32:39","annotation_curators":[{"name":"Gabriel Ruiz Romero","community_curator":true,"annotation_count":33,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":8,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1682.10","SPAPB8E5.02c","SPBC14C8.01c","SPBC16D10.08c","SPAC17C9.13c","SPAC31G5.13","SPBC17D11.07c","SPBC1604.08c","SPBP19A11.03c","SPCC1739.13","SPBC409.06","SPAC13G7.02c","SPAC607.05","SPAC2E12.02","SPBC106.16","SPBC582.03","SPCC14G10.03c"],"gene_count":17,"ltp_gene_count":6,"approved_date":"2025-03-28"},{"uniquename":"PMID:33860765","title":"Live-cell single-molecule tracking highlights requirements for stable Smc5/6 chromatin association in vivo.","citation":"Elife 2021 Apr 16;10","abstract":"The essential Smc5/6 complex is required in response to replication stress and is best known for ensuring the fidelity of homologous recombination. Using single-molecule tracking in live fission yeast to investigate Smc5/6 chromatin association, we show that Smc5/6 is chromatin associated in unchallenged cells and this depends on the non-SMC protein Nse6. We define a minimum of two Nse6-dependent sub-pathways, one of which requires the BRCT-domain protein Brc1. Using defined mutants in genes encoding the core Smc5/6 complex subunits, we show that the Nse3 double-stranded DNA binding activity and the arginine fingers of the two Smc5/6 ATPase binding sites are critical for chromatin association. Interestingly, disrupting the single-stranded DNA (ssDNA) binding activity at the hinge region does not prevent chromatin association but leads to elevated levels of gross chromosomal rearrangements during replication restart. This is consistent with a downstream function for ssDNA binding in regulating homologous recombination.","doi":"10.7554/eLife.68579","authors":"Etheridge TJ, Villahermosa D, Campillo-Funollet E, Herbert AD, Irmisch A, Watson AT, Dang HQ, Osborne MA, Oliver AW, Carr AM, Murray JM","authors_abbrev":"Etheridge TJ et al.","pubmed_publication_date":"16 Apr 2021","pubmed_entrez_date":"2021-04-16","publication_year":"2021","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-04-19 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31990439","title":"Organelle specific simultaneous Raman/green fluorescence protein microspectroscopy for living cell physicochemical studies.","citation":"J Biophotonics 2020 Apr;13(4):e201960163","abstract":"We demonstrate a novel bio-spectroscopic technique, \"simultaneous Raman/GFP microspectroscopy\". It enables organelle specific Raman microspectroscopy of living cells. Fission yeast, Schizosaccharomyces pombe, whose mitochondria are green fluorescence protein (GFP) labeled, is used as a test model system. Raman excitation laser and GFP excitation light irradiate the sample yeast cells simultaneously. GFP signal is monitored in the anti-Stokes region where interference from Raman scattering is negligibly small. Of note, 13 568 Raman spectra measured from different points of 19 living yeast cells are categorized according to their GFP fluorescence intensities, with the use of a two-component multivariate curve resolution with alternate least squares (MCR-ALS) analysis in the anti-Stokes region. This categorization allows us to know whether or not Raman spectra are taken from mitochondria. Raman spectra specific to mitochondria are obtained by an MCR-ALS analysis in the Stokes region of 1389 strongly GFP positive spectra. Two mitochondria specific Raman spectra have been obtained. The first one is dominated by protein Raman bands and the second by lipid Raman bands, being consistent with the known molecular composition of mitochondria. In addition, the second spectrum shows a strong band of ergosterol at 1602 cm -1  , previously reported as \"Raman spectroscopic signature of life of yeast.\"","doi":"10.1002/jbio.201960163","authors":"Wattanavichean N, Nishida I, Ando M, Kawamukai M, Yamamoto T, Hamaguchi HO","authors_abbrev":"Wattanavichean N et al.","pubmed_publication_date":"Apr 2020","pubmed_entrez_date":"2020-01-29","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21554766","title":"Deciphering transcription factor binding patterns from genome-wide high density ChIP-chip tiling array data.","citation":"BMC Proc 2011 May 28;5 Suppl 2(Suppl 2):S8","abstract":"The binding events of DNA-interacting proteins and their patterns can be extensively characterized by high density ChIP-chip tiling array data. The characteristics of the binding events could be different for different transcription factors. They may even vary for a given transcription factor among different interaction loci. The knowledge of binding sites and binding occupancy patterns are all very useful to understand the DNA-protein interaction and its role in the transcriptional regulation of genes.\nIn the view of the complexity of the DNA-protein interaction and the opportunity offered by high density tiled ChIP-chip data, we present a statistical procedure which focuses on identifying the interaction signal regions instead of signal peaks using moving window binomial testing method and deconvolving the patterns of interaction using peakedness and skewness scores. We analyzed ChIP-chip data of 4 different DNA interacting proteins including transcription factors and RNA polymerase in fission yeast using our procedure. Our analysis revealed the variation of binding patterns within and across different DNA interacting proteins. We present their utility in understanding transcriptional regulation from ChIP-chip data.\nOur method can successfully detect the signal regions and characterize the binding patterns in ChIP-chip data which help appropriate analysis of the ChIP-chip data.","doi":"10.1186/1753-6561-5-S2-S8","authors":"Li J, Zhu L, Eshaghi M, Liu J, Karuturi KM","authors_abbrev":"Li J et al.","pubmed_publication_date":"28 May 2011","pubmed_entrez_date":"2011-05-11","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30859719","title":"A new chromosomal rearrangement improves the adaptation of wine yeasts to sulfite.","citation":"Environ Microbiol 2019 May;21(5):1771-1781","abstract":"Sulfite-generating compounds are widely used during winemaking as preservatives because of its antimicrobial and antioxidant properties. Thus, wine yeast strains have developed different genetic strategies to increase its sulfite resistance. The most efficient sulfite detoxification mechanism in Saccharomyces cerevisiae uses a plasma membrane protein called Ssu1 to efflux sulfite. In wine yeast strains, two chromosomal translocations (VIIItXVI and XVtXVI) involving the SSU1 promoter region have been shown to upregulate SSU1 expression and, as a result, increase sulfite tolerance. In this study, we have identified a novel chromosomal rearrangement that triggers wine yeast sulfite adaptation. An inversion in chromosome XVI (inv-XVI) probably due to sequence microhomology, which involves SSU1 and GCR1 regulatory regions, increases the expression of SSU1 and the sulfite resistance of a commercial wine yeast strain. A detailed dissection of this chimeric SSU1 promoter indicates that both the removed SSU1 promoter sequence and the relocated GCR1 sequence contribute to SSU1 upregulation and sulfite tolerance. However, no relevant function has been attributed to the SSU1-promoter-binding transcription factor Fzf1. These results unveil a new genomic event that confers an evolutive advantage to wine yeast strains.","doi":"10.1111/1462-2920.14586","authors":"García-Ríos E, Nuévalos M, Barrio E, Puig S, Guillamón JM","authors_abbrev":"García-Ríos E et al.","pubmed_publication_date":"May 2019","pubmed_entrez_date":"2019-03-13","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBPB10D8.07c","SPBPB10D8.04c","SPBPB10D8.06c","SPBPB10D8.05c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"EMBL:SPD234","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31216223","title":"Anchoring of actin to the plasma membrane enables tension production in the fission yeast cytokinetic ring.","citation":"Mol Biol Cell 2019 Jul 22;30(16):2053-2064","abstract":"The cytokinetic ring generates tensile force that drives cell division, but how tension emerges from the relatively disordered ring organization remains unclear. Long ago, a musclelike sliding filament mechanism was proposed, but evidence for sarcomeric order is lacking. Here we present quantitative evidence that in fission yeast, ring tension originates from barbed-end anchoring of actin filaments to the plasma membrane, providing resistance to myosin forces that enables filaments to develop tension. The role of anchoring was highlighted by experiments on isolated fission yeast rings, where sections of ring became unanchored from the membrane and shortened ∼30-fold faster than normal. The dramatically elevated constriction rates are unexplained. Here we present a molecularly explicit simulation of constricting partially anchored rings as studied in these experiments. Simulations accurately reproduced the experimental constriction rates and showed that following anchor release, a segment becomes tensionless and shortens via a novel noncontractile reeling-in mechanism at about the velocity of load-free myosin II. The ends are reeled in by barbed end-anchored actin filaments in adjacent segments. Other actin anchoring schemes failed to constrict rings. Our results quantitatively support a specific organization and anchoring scheme that generate tension in the cytokinetic ring.","doi":"10.1091/mbc.E19-03-0173","authors":"Wang S, O'Shaughnessy B","authors_abbrev":"Wang S et al.","pubmed_publication_date":"22 Jul 2019","pubmed_entrez_date":"2019-06-20","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-06-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4054614","title":"[Specificity of replicating instability in Schizosaccharomyces pombe haploid yeasts].","citation":"Genetika 1985 Aug;21(8):1266-71","abstract":"UV-induced genetic instability in haploid Schizosaccharomyces pombe does not appear to be very locus-specific. This conclusion contradicts the data previously published by other authors. The possible causes for this discrepancy are discussed.","authors":"Kurennaia ON, Devin AB","authors_abbrev":"Kurennaia ON et al.","pubmed_publication_date":"Aug 1985","pubmed_entrez_date":"1985-08-01","publication_year":"1985","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16688222","title":"Histone H2B mutations in inner region affect ubiquitination, centromere function, silencing and chromosome segregation.","citation":"EMBO J 2006 Jun 07;25(11):2420-31","abstract":"The reiterated nature of histone genes has hampered genetic approach to dissect the role of histones in chromatin dynamics. We here report isolation of three temperature-sensitive (ts) Schizosaccharomyces pombe strains, containing amino-acid substitutions in the sole histone H2B gene (htb1+). The mutation sites reside in the highly conserved, non-helical residues of H2B, which are implicated in DNA-protein or protein-protein interactions in the nucleosome. In the allele of htb1-72, the substitution (G52D) occurs at the DNA binding loop L1, causing disruption of the gene silencing in heterochromatic regions and lagging chromosomes in anaphase. In another allele htb1-223 (P102L) locating in the junction between alpha3 and alphaC, the mutant residue is in contact with H2A and other histones, leading to structural aberrations in the central centromere chromatin and unequal chromosome segregation in anaphase. The third allele htb1-442 (E34K) near alpha1 displayed little defect. Evidence is provided that monoubiquitinated H2B is greatly unstable in P102L mutant, possibly owing to proteasome-independent destruction or enhanced deubiquitination. Histone H2B thus plays an important role in centromere/kinetochore formation.","authors":"Maruyama T, Nakamura T, Hayashi T, Yanagida M","authors_abbrev":"Maruyama T et al.","pubmed_publication_date":"07 Jun 2006","pubmed_entrez_date":"2006-05-12","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1687.20c","SPBC36.05c","SPBC409.04c","SPBC1105.17","SPCC622.09","SPBC776.02c","SPCC736.14","SPBC106.10"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:1323458","title":"An intracellular ATP-dependent calcium pump within the yeast Schizosaccharomyces pombe, encoded by the gene cta3.","citation":"Eur J Biochem 1992 Aug 01;207(3):1003-8","abstract":"We have permeabilized the plasma membranes of Schizosaccharomyces pombe cell with nystatin and measured ATP-dependent Ca2+ uptake in the presence of KNO3 and a protonophore in order to inhibit Ca2+ uptake into the vacuole. ATP-dependent Ca2+ accumulation into non-vacuolar Ca(2+)-storing organelles was detected. This Ca2+ uptake activity was maximal at pH 6 and inhibited by vanadate, the inhibitor of P-type ATPases. The null mutation of cta3, a putative Ca2+ gene, [Ghislain, M., Goffeau, A., Halachmi, D. and Eilam, Y. (1990) J. Biol. Chem. 265, 18400-18407] strongly reduced the level of ATP-dependent Ca2+ uptake into non-vacuolar intracellular storing organelles. This result suggests that cta3 encodes an intracellular ATP-dependent Ca2+ pump. The residual ATP-dependent Ca2+ uptake in the mutant strain indicated the presence of a second nonvacuolar, intracellular Ca(2+)-ATPase encoded by a different gene.","authors":"Halachmi D, Ghislain M, Eilam Y","authors_abbrev":"Halachmi D et al.","pubmed_publication_date":"01 Aug 1992","pubmed_entrez_date":"1992-08-01","publication_year":"1992","canto_session_key":"c933d84cfac5cc71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-19 09:59:23","canto_approved_date":"2023-01-26 10:59:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-12 15:15:56","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"vw253@cam.ac.uk","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC839.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-19"},{"uniquename":"PMID:17029695","title":"Electrophoresis of long DNA molecules in linear polyacrylamide solutions.","citation":"Biophys Chem 1998 Apr 20;71(2-3):113-23","abstract":"Electrophoresis of long DNA (T4 DNA; 166 kb, S. pombe chromosomal DNA; 3-6 Mb) in linear polyacrylamide solutions was investigated by fluorescence microscopy and capillary electrophoresis. In the past studies on electrophoresis of long DNA in a polymer solution, it was reported that DNA migrates in 'U-shape conformation'. We found that at higher polymer concentrations, the shape of the migrating DNA changes from U shape to linear shape ('I-shape conformation'). In the migration mode with the I-shape conformation, the DNA moves with almost constant velocity and constant shape. However, the migration velocity does depend on the DNA size, and it is possible to separate DNAs under this I-shape motion. Actually, Mb-sized DNAs are well separated within 5 min in the region for the I-shape motion by means of capillary electrophoresis with a DC field. Considering that it takes 20 h to separate Mb-sized DNAs by standard pulsed-field gel electrophoresis (PFGE), this results will be useful for the separation of giant DNAs.","authors":"Ueda M, Oana H, Baba Y, Doi M, Yoshikawa K","authors_abbrev":"Ueda M et al.","pubmed_publication_date":"20 Apr 1998","pubmed_entrez_date":"2006-10-13","publication_year":"1998","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16332887","title":"Cell adsorption and selective desorption for separation of microbial cells by using chitosan-immobilized silica.","citation":"Appl Environ Microbiol 2005 Dec;71(12):8895-902","abstract":"Cell adsorption and selective desorption for separation of microbial cells were conducted by using chitosan-immobilized silica (CIS). When chitosan was immobilized onto silica surfaces with glutaraldehyde, bacterial cells adsorbed well and retained viability. Testing of the adsorption and desorption ability of CIS using various microbes such as Escherichia coli, Aeromonas hydrophila, Pseudomonas aeruginosa, Bacillus subtilis, Micrococcus luteus, Staphylococcus aureus, Staphylococcus epidermidis, Lactobacillus casei, Streptococcus mutans, Streptococcus sobrinus, Streptococcus salivarius, Saccharomyces cerevisiae, Saccharomyces ludwigii, and Schizosaccharomyces pombe revealed that most microbes could be adsorbed and selectively desorbed under different conditions. In particular, recovery was improved when L-cysteine was added. A mixture of two bacterial strains adsorbed onto CIS could also be successfully separated by use of specific solutions for each strain. Most of the desorbed cells were alive. Thus, quantitative and selective fractionation of cells is readily achievable by employing chitosan, a known antibacterial material.","authors":"Kubota M, Matsui M, Chiku H, Kasashima N, Shimojoh M, Sakaguchi K","authors_abbrev":"Kubota M et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-12-08","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23779158","title":"The proteasome factor Bag101 binds to Rad22 and suppresses homologous recombination.","citation":"Sci Rep 2013;3:2022","abstract":"Although RAD52 plays a critical role in the initiation of homologous recombination (HR) by facilitating the replacement of RPA with RAD51, the mechanism controlling RAD52 remains elusive. Here, we show that Bag101, a factor implicated in proteasome functioning, regulates RAD52 protein levels and subsequent HR. LC-MS/MS analysis identified Bag101 which binds to Rad22, the fission yeast homologue of RAD52. Bag101 reduced HR frequency through its overexpression and conversely, HR frequencies were enhanced when it was deleted. Consistent with this observation, Rad22 protein levels was reduced in cells where bag101 was overexpressed even when Rad22 transcription was up-regulated, suggesting the operation of proteasome-mediated Rad22 degradation. Indeed, Rad22 protein levels were stabilized in proteasome mutants. Rad22 physically interacted with the BAG domain of Bag101, and a lack of this domain enhanced HR frequency. Similarly, radiation exposure triggered the dissociation of these proteins so that Rad22 was stabilized and able to enhance HR.","doi":"10.1038/srep02022","authors":"Saito Y, Takeda J, Okada M, Kobayashi J, Kato A, Hirota K, Taoka M, Matsumoto T, Komatsu K, Isobe T","authors_abbrev":"Saito Y et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-06-20","publication_year":"2013","canto_session_key":"bd4f401a22cd44b2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC660.13c","SPAC31G5.13","SPCC1672.02c","SPAC8F11.03","SPBC119.14","SPAC13G7.02c","SPCC1753.01c","SPBC16D10.04c","SPCC285.16c","SPBC83.08","SPAPB8E5.09","SPAC30D11.10","SPBC1861.02","SPAC2F3.04c","SPBC19G7.01c","SPCC1739.13","SPBC216.05","SPBC16G5.11c"],"gene_count":18,"ltp_gene_count":18},{"uniquename":"PMID:26072515","title":"Inferring orthologous gene regulatory networks using interspecies data fusion.","citation":"Bioinformatics 2015 Jun 15;31(12):i97-105","abstract":"The ability to jointly learn gene regulatory networks (GRNs) in, or leverage GRNs between related species would allow the vast amount of legacy data obtained in model organisms to inform the GRNs of more complex, or economically or medically relevant counterparts. Examples include transferring information from Arabidopsis thaliana into related crop species for food security purposes, or from mice into humans for medical applications. Here we develop two related Bayesian approaches to network inference that allow GRNs to be jointly inferred in, or leveraged between, several related species: in one framework, network information is directly propagated between species; in the second hierarchical approach, network information is propagated via an unobserved 'hypernetwork'. In both frameworks, information about network similarity is captured via graph kernels, with the networks additionally informed by species-specific time series gene expression data, when available, using Gaussian processes to model the dynamics of gene expression.\nResults on in silico benchmarks demonstrate that joint inference, and leveraging of known networks between species, offers better accuracy than standalone inference. The direct propagation of network information via the non-hierarchical framework is more appropriate when there are relatively few species, while the hierarchical approach is better suited when there are many species. Both methods are robust to small amounts of mislabelling of orthologues. Finally, the use of Saccharomyces cerevisiae data and networks to inform inference of networks in the budding yeast Schizosaccharomyces pombe predicts a novel role in cell cycle regulation for Gas1 (SPAC19B12.02c), a 1,3-beta-glucanosyltransferase.\nMATLAB code is available from http://go.warwick.ac.uk/systemsbiology/software/.","doi":"10.1093/bioinformatics/btv267","authors":"Penfold CA, Millar JB, Wild DL","authors_abbrev":"Penfold CA et al.","pubmed_publication_date":"15 Jun 2015","pubmed_entrez_date":"2015-06-15","publication_year":"2015","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2015-06-16 00:20:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9742201","title":"Dynamics of cell wall formation in fission yeast, Schizosaccharomyces pombe.","citation":"Fungal Genet Biol 1998;24(1-2):178-206","abstract":"Studies on the dynamics of surface and intracellular structures during cell wall formation from the reverting protoplast of Schizosaccharomyces pombe were reviewed, and the correlation between cell wall formation and actin cytoskeleton, which is the most important conductor of the mechanism, is described in this paper. A close spatial and temporal relationship between actin cytoskeleton and cell wall formation was found by using wild type and actin point-mutant cps8 of S. pombe. Concomitant with the cell wall formation, dynamic behavior of the intracellular secretion machinery, especially the Golgi apparatus and secretory vesicles, was analyzed by three-dimensional reconstruction of 40 to 80 serial sections at five reverting stages. Total reverting protoplast volume increased by 3.8 and 4.3 times at 3 and 5 h, respectively, and the volume of the Golgi apparatus in the corresponding stages increased 2.3- and 2. 5-fold over the same periods. The number of secretory vesicles also markedly increased by 3.4 and 5.8 times over that of the corresponding reverting protoplasts. Actin point-mutant cps8 cells have abnormal structure in the cell wall and septum, and the distribution pattern of the actin cytoskeleton during the reversion process was different from wild-type protoplasts. The profiles of actin showed one or two thick cables and patches in the cytoplasm which remained throughout reversion. The development of crosslinkage of the glucan fibrils which are beta-1,3-glucan in nature on the reverting protoplast surface was defective; the glucan networks consisted of thin, rope-shaped fibrils up to 30 nm in width which formed a ribbon-shape 200 nm wide in wild-type reverting protoplasts. The intrafibrillar space is not filled with amorphous particles of alpha-galactomannan in nature. The secretion machinery was seen to have a similar profile as the wild type. The above results suggest that actin cytoskeleton may control secretion of beta-1,6-glucan and other cell wall substances such as alpha-glucan and alpha-galactomannan rather than beta-1,3-glucan. Study of the role of actin cytoskeleton in the cell wall formation is contributing to the development of antifungal agents together with basic cell biology.","authors":"Osumi M, Sato M, Ishijima SA, Konomi M, Takagi T, Yaguchi H","authors_abbrev":"Osumi M et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-09-22","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24652292","title":"The human gene SLC25A29, of solute carrier family 25, encodes a mitochondrial transporter of basic amino acids.","citation":"J Biol Chem 2014 May 09;289(19):13374-84","abstract":"The human genome encodes 53 members of the solute carrier family 25 (SLC25), also called the mitochondrial carrier family, many of which have been shown to transport carboxylates, amino acids, nucleotides, and cofactors across the inner mitochondrial membrane, thereby connecting cytosolic and matrix functions. In this work, a member of this family, SLC25A29, previously reported to be a mitochondrial carnitine/acylcarnitine- or ornithine-like carrier, has been thoroughly characterized biochemically. The SLC25A29 gene was overexpressed in Escherichia coli, and the gene product was purified and reconstituted in phospholipid vesicles. Its transport properties and kinetic parameters demonstrate that SLC25A29 transports arginine, lysine, homoarginine, methylarginine and, to a much lesser extent, ornithine and histidine. Carnitine and acylcarnitines were not transported by SLC25A29. This carrier catalyzed substantial uniport besides a counter-exchange transport, exhibited a high transport affinity for arginine and lysine, and was saturable and inhibited by mercurial compounds and other inhibitors of mitochondrial carriers to various degrees. The main physiological role of SLC25A29 is to import basic amino acids into mitochondria for mitochondrial protein synthesis and amino acid degradation.","doi":"10.1074/jbc.M114.547448","authors":"Porcelli V, Fiermonte G, Longo A, Palmieri F","authors_abbrev":"Porcelli V et al.","pubmed_publication_date":"09 May 2014","pubmed_entrez_date":"2014-03-22","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9532803","title":"Multidrug resistance phenotype conferred by overexpressing bfr2+/pad1+/sks1+ or pap1+ genes and mediated by bfr1+ gene product, a structural and functional homologue of P-glycoprotein in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 1998 Feb;62(2):390-2","abstract":"We investigated the mechanism of multidrug resistance conferred by overexpression of bfr2+/pad1+/sks1+ or pap1+ genes of Schizosaccharomyces pombe. Overexpression of bfr2+ did not confer multidrug resistance on a pap1-disrupted strain. In a mutant with bfr1+ (a putative membrane transporter which belongs to the ATP-binding cassette superfamily) disrupted, overexpression of either bfr2+ or pap1+ did not confer multidrug resistance. These findings suggest that bfr1+ acts as the most downstream effector of the multidrug resistance conferred by bfr2+ and pap1+ genes.","authors":"Arioka M, Kouhashi M, Yoda K, Takatsuki A, Yamasaki M, Kitamoto K","authors_abbrev":"Arioka M et al.","pubmed_publication_date":"Feb 1998","pubmed_entrez_date":"1998-04-09","publication_year":"1998","canto_session_key":"a826f97af4e46f8f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-09-07 14:04:51","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-09-06 06:48:16","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.13","SPAC1783.07c","SPCC18B5.01c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2012-09-06"},{"uniquename":"EMBL:SPD166","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19250900","title":"CENP-A targeting moves a step back.","citation":"Mol Cell 2009 Feb 27;33(4):411-3","abstract":"In a recent issue of Molecular Cell, Pidoux et al. (2009) and Williams et al. (2009) identify S. pombe Scm3 as the proximate factor in the Cnp1/CENP-A deposition pathway, providing a direct connection to centromere-localized Mis16-Mis18.","doi":"10.1016/j.molcel.2009.02.006","authors":"Baker RE","authors_abbrev":"Baker RE","pubmed_publication_date":"27 Feb 2009","pubmed_entrez_date":"2009-03-03","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28991264","title":"Architectural alterations of the fission yeast genome during the cell cycle.","citation":"Nat Struct Mol Biol 2017 Nov;24(11):965-976","abstract":"Eukaryotic genomes are highly ordered through various mechanisms, including topologically associating domain (TAD) organization. We employed an in situ Hi-C approach to follow the 3D organization of the fission yeast genome during the cell cycle. We demonstrate that during mitosis, large domains of 300 kb-1 Mb are formed by condensin. This mitotic domain organization does not suddenly dissolve, but gradually diminishes until the next mitosis. By contrast, small domains of 30-40 kb that are formed by cohesin are relatively stable across the cell cycle. Condensin and cohesin mediate long- and short-range contacts, respectively, by bridging their binding sites, thereby forming the large and small domains. These domains are inversely regulated during the cell cycle but assemble independently. Our study describes the chromosomal oscillation between the formation and decay phases of the large and small domains, and we predict that the condensin-mediated domains serve as chromosomal compaction units.","doi":"10.1038/nsmb.3482","authors":"Tanizawa H, Kim KD, Iwasaki O, Noma KI","authors_abbrev":"Tanizawa H et al.","pubmed_publication_date":"Nov 2017","pubmed_entrez_date":"2017-10-10","publication_year":"2017","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2017-10-12 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22322963","title":"Expression of budding yeast IPT1 produces mannosyldiinositol phosphorylceramide in fission yeast and inhibits cell growth.","citation":"Microbiology (Reading) 2012 May;158(Pt 5):1219-1228","abstract":"In Saccharomyces (Sacc.) cerevisiae, the final step of the complex sphingolipid biosynthetic pathway requires Ipt1p for synthesis of mannosyldiinositol phosphorylceramide [M(IP)(2)C]. No fission yeast equivalent to Ipt1p has been found in the Schizosaccharomyces (Schiz.) pombe genome, and the most abundant complex sphingolipid is mannosylinositol phosphorylceramide. To examine the effect of expressing Sacc. cerevisiae IPT1 (ScIPT1) in Schiz. pombe, the ScIPT1 gene was cloned into an inducible fission yeast integrative vector and expressed in wild-type Schiz. pombe. In the Schiz. pombe ScIPT1-expressing cells, M(IP)(2)C was detected, indicating that ScIpt1p functions in M(IP)(2)C synthesis in Schiz. pombe. Expression of ScIPT1 caused pleiotropic phenotypes, including aberrant morphology and mislocalization of ergosterols in the plasma membrane. Furthermore, growth of Schiz. pombe was severely impaired. We analysed the sphingolipid composition of ScIPT1-expressing cells following a prolonged lag phase, and found that M(IP)(2)C was not synthesized, indicating that Ipt1p had been inactivated. GFP-tagged ScIpt1 localized primarily in the Golgi apparatus in wild-type Schiz. pombe. Over time, ScIpt1p was eventually transported to the vacuolar lumen through the multivesicular body pathway. These results indicate that M(IP)(2)C is toxic to Schiz. pombe and that fission yeast possesses an unknown mechanism to effectively extrude toxic sphingolipids from cells.","doi":"10.1099/mic.0.056184-0","authors":"Nakase M, Tani M, Takegawa K","authors_abbrev":"Nakase M et al.","pubmed_publication_date":"May 2012","pubmed_entrez_date":"2012-02-11","publication_year":"2012","canto_session_key":"60b8df9a8cafd815","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-07-06 07:11:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-06 07:10:18","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2016-07-06"},{"uniquename":"PMID:29684553","title":"Fission yeast cells overproducing HSET/KIFC1 provides a useful tool for identification and evaluation of human kinesin-14 inhibitors.","citation":"Fungal Genet Biol 2018 Jul;116:33-41","abstract":"Many human cancer cells contain more than two centrosomes, yet these cancer cells can form pseudo-bipolar spindles through the mechanism, called centrosome clustering, and survive, instead of committing lethal multipolar mitoses. Kinesin-14/HSET, a minus end-directed motor, plays a crucial role in centrosome clustering. Accordingly, HSET is deemed to be a promising chemotherapeutic target to selectively kill cancer cells. Recently, three HSET inhibitors (AZ82, CW069 and SR31527) have been reported, but their specificity and efficacy have not been evaluated rigorously. This downside partly stems from the lack of robust systems for the assessment of these drugs. Yeasts and filamentous fungi provide not only powerful models for basic and applied biology but also versatile tools for drug discovery and evaluation. Here we show that these three inhibitors on their own are cytotoxic to fission yeast, suggesting that they have off-targets in vivo except for kinesin-14. Nonetheless, intriguingly, AZ82 can neutralize otherwise toxic overproduced HSET; this includes a substantial reduction in the percentage of HSET-driven abnormal mitotic cells and partial suppression of its lethality. SR31527 also displays modest neutralizing activity, while we do not detect such activity in CW069. As an experimental proof-of-principle study, we have treated HSET-overproducing fission yeast cells with extracts prepared from various plant species and found activities that rescue HSET-driven lethality in those from Chamaecyparis pisifera and Toxicodendron trichocarpum. This methodology of protein overproduction in fission yeast, therefore, provides a convenient, functional assay system by which to screen for not only selective human kinesin-14 inhibitors but also those against other molecules of interest.","doi":"10.1016/j.fgb.2018.04.006","authors":"Yukawa M, Yamauchi T, Kurisawa N, Ahmed S, Kimura KI, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"Jul 2018","pubmed_entrez_date":"2018-04-24","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-04-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.10","SPAC3A11.14c","SPAC25G10.07c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:9613582","title":"Phosphoinositide-specific phospholipase C forms a complex with 14-3-3 proteins and is involved in expression of UV resistance in fission yeast.","citation":"Mol Gen Genet 1998 Apr;258(1-2):139-47","abstract":"The fission yeast plc1+ gene encodes phosphoinositide-specific phospholipase C. The two- hybrid interaction assay with plexA-plc1+ as a bait revealed that Plc1p interacted with the 14-3-3 proteins Rad24p and Rad25p. Formation of a complex containing Plc1p and Rad24p in vivo was confirmed by an immunological method. As predicted from the fact that rad24 null mutant cells are hypersensitive to UV irradiation, plc1 null mutant cells were almost as sensitive to UV irradiation as rad24 null mutant cells. In addition, deletion of rad24 in the plc1 null mutant cells did not enhance the UV sensitivity, indicating that plc1+ and rad24+ belong to the same epistasis group with respect to UV sensitivity. Whereas Rad24p has been reported to be involved in the DNA damage checkpoint pathway, the delay to mitosis after UV irradiation was not defective either in rad24 null mutant cells or in plcl null mutant cells in our analysis. Thus, Plc1p is responsible for resistance to UV irradiation, but not for the DNA damage checkpoint pathway, in cooperation with 14-3-3 proteins.","authors":"Andoh T, Kato T, Matsui Y, Toh-e A","authors_abbrev":"Andoh T et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-06-05","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F8.11","SPAC8E11.02c","SPAC17A2.13c","SPBC3E7.08c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:15485922","title":"Fission yeast Dna2 is required for generation of the telomeric single-strand overhang.","citation":"Mol Cell Biol 2004 Nov;24(21):9557-67","abstract":"It has been suggested that the Schizosaccharomyces pombe Rad50 (Rad50-Rad32-Nbs1) complex is required for the resection of the C-rich strand at telomere ends in taz1-d cells. However, the nuclease-deficient Rad32-D25A mutant can still resect the C-rich strand, suggesting the existence of a nuclease that resects the C-rich strand. Here, we demonstrate that a taz1-d dna2-2C double mutant lost the G-rich overhang at a semipermissive temperature. The amount of G-rich overhang in S phase in the dna2-C2 mutant was lower than that in wild-type cells at the semipermissive temperature. Dna2 bound to telomere DNA in a chromatin immunoprecipitation assay. Moreover, telomere length decreased with each generation after shift of the dna2-2C mutant to the semipermissive temperature. These results suggest that Dna2 is involved in the generation of G-rich overhangs in both wild-type cells and taz1-d cells. The dna2-C2 mutant was not gamma ray sensitive at the semipermissive temperature, suggesting that the ability to process double-strand break (DSB) ends was not affected in the dna2-C2 mutant. Our results reveal that DSB ends and telomere ends are processed by different mechanisms.","authors":"Tomita K, Kibe T, Kang HY, Seo YS, Uritani M, Ushimaru T, Ueno M","authors_abbrev":"Tomita K et al.","pubmed_publication_date":"Nov 2004","pubmed_entrez_date":"2004-10-16","publication_year":"2004","canto_session_key":"526628f82b16fbfd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-05-17 17:08:13","canto_approved_date":"2022-09-24 14:32:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-17 17:08:08","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":21,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.02c","SPBC29A10.05","SPAC3G6.06c","SPBC16D10.04c","SPAC16A10.07c","SPBC29A3.14c","SPAC1556.01c","SPBC216.05"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2016-05-17"},{"uniquename":"PMID:38598296","title":"The bistable mitotic switch in fission yeast.","citation":"Mol Biol Cell 2024 Apr 10;:mbcE24030142","abstract":"In favorable conditions, eukaryotic cells proceed irreversibly through the cell division cycle (G1-S-G2-M) in order to produce two daughter cells with the same number and identity of chromosomes of their progenitor. The integrity of this process is maintained by 'checkpoints' that hold a cell at particular transition points of the cycle until all requisite events are completed. The crucial functions of these checkpoints seem to depend on irreversible bistability of the underlying checkpoint control systems. Bistability of cell cycle transitions has been confirmed experimentally in frog egg extracts, budding yeast cells and mammalian cells. For fission yeast cells, a recent paper by Patterson et al. (2021) provides experimental evidence for an abrupt transition from G2 phase into mitosis, and we show that these data are consistent with a stochastic model of a bistable switch governing the G2/M checkpoint. Interestingly, our model suggests that their experimental data could also be explained by a reversible/sigmoidal switch, and stochastic simulations confirm this supposition. We propose a simple modification of their experimental protocol that could provide convincing evidence for (or against) bistability of the G2/M transition in fission yeast.","doi":"10.1091/mbc.E24-03-0142","authors":"Novák B, Tyson JJ","authors_abbrev":"Novák B et al.","pubmed_publication_date":"10 Apr 2024","pubmed_entrez_date":"2024-04-10","publication_year":"2024","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2024-04-10 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16808240","title":"[Analysis of mutations in the mat1 region of Schizosaccharomyces pombe strain with the deletion of gene rhp55+].","citation":"Genetika 2006 May;42(5):602-10","abstract":"DNA double-strand breaks may occur both under the action of various exogenous factors and in the course of cell metabolism processes, in particular, upon mating type switching in yeast. Genes belonging to the epistatic group RAD52 are known to repair such DNA damage. Molecular defects in mating type switching occurring after the deletion of gene rhp55+ encoding the paralog of recombinational protein Rhp51, which is a functional homolog of Escherichia coli RecA, were studied in fission yeast. Analysis of stable nonswitching segregants in h90 rhp55 mutants with unchanged configuration of the mating type switching locus but with a drastically decreased level of double-strand DNA break formation at the mat1 :1 locus demonstrated changes in DNA sequences within the region responsible for the generation of the breaks. These changes might have resulted from incorrect gene conversion upon repair of double-strand DNA breaks in Schizosaccharomyces pombe rhp55 mutants.","authors":"Vagin DA, Bashkirov VI, Khasanov FK","authors_abbrev":"Vagin DA et al.","pubmed_publication_date":"May 2006","pubmed_entrez_date":"2006-07-01","publication_year":"2006","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35008733","title":"The Ceramide Synthase Subunit Lac1 Regulates Cell Growth and Size in Fission Yeast.","citation":"Int J Mol Sci 2021 Dec 28;23(1)","abstract":"Cell division produces two viable cells of a defined size. Thus, all cells require mechanisms to measure growth and trigger cell division when sufficient growth has occurred. Previous data suggest a model in which growth rate and cell size are mechanistically linked by ceramide-dependent signals in budding yeast. However, the conservation of mechanisms that govern growth control is poorly understood. In fission yeast, ceramide synthase is encoded by two genes, Lac1 and Lag1. Here, we characterize them by using a combination of genetics, microscopy, and lipid analysis. We showed that Lac1 and Lag1 co-immunoprecipitate and co-localize at the endoplasmic reticulum. However, each protein generates different species of ceramides and complex sphingolipids. We further discovered that Lac1, but not Lag1, is specifically required for proper control of cell growth and size in  Schizosaccharomyces pombe . We propose that specific ceramide and sphingolipid species produced by Lac1 are required for normal control of cell growth and size in fission yeast.","doi":"10.3390/ijms23010303","authors":"Flor-Parra I, Sabido-Bozo S, Ikeda A, Hanaoka K, Aguilera-Romero A, Funato K, Muñiz M, Lucena R","authors_abbrev":"Flor-Parra I et al.","pubmed_publication_date":"28 Dec 2021","pubmed_entrez_date":"2022-01-11","publication_year":"2021","canto_session_key":"0fb2e4081135c7c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rafael Lucena","canto_first_approved_date":"2022-01-19 12:01:04","canto_approved_date":"2022-01-31 09:34:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-17 11:48:47","canto_added_date":"2022-01-13 01:15:04","annotation_curators":[{"name":"Rafael Lucena","community_curator":true,"annotation_count":12,"orcid":"0000-0003-2050-0611","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1A6.09c","SPBC3E7.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-01-19"},{"uniquename":"PMID:26063574","title":"Minishelterins separate telomere length regulation and end protection in fission yeast.","citation":"Genes Dev 2015 Jun 01;29(11):1164-74","abstract":"The conserved shelterin complex is critical for chromosome capping and maintaining telomere length homeostasis. In fission yeast, shelterin is comprised of five proteins. Taz1, Rap1, and Poz1 function as negative regulators of telomere elongation, whereas Pot1 and Tpz1 are critical for end capping and telomerase recruitment. How the five proteins work together to safeguard chromosome ends and promote telomere length homeostasis is a matter of great interest. Using a combination of deletions, fusions, and tethers, we define key elements of shelterin important for telomere length regulation. Surprisingly, deletion of the entire Rap1 and Poz1 proteins does not impair telomere length regulation as long as a static bridge is provided between Taz1 and Tpz1. Cells harboring minishelterin display wild-type telomere length and intact subtelomeric silencing. However, protection against end fusions in G1 is compromised in the absence of Rap1. Our data reveal a remarkable plasticity in shelterin architecture and separate functions in length regulation and end protection.","doi":"10.1101/gad.261123.115","authors":"Pan L, Hildebrand K, Stutz C, Thomä N, Baumann P","authors_abbrev":"Pan L et al.","pubmed_publication_date":"01 Jun 2015","pubmed_entrez_date":"2015-06-12","publication_year":"2015","canto_session_key":"3dab19b21ef25b2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lili Pan","canto_first_approved_date":"2017-11-08 15:15:02","canto_approved_date":"2024-04-04 10:26:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-11-02 15:29:22","canto_added_date":"2015-06-14 00:19:19","annotation_curators":[{"name":"Lili Pan","community_curator":true,"annotation_count":20,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1778.02","SPAC19G12.13c","SPAC6F6.16c","SPAC26H5.06","SPAC16A10.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-11-08"},{"uniquename":"PMID:11030744","title":"Dolichol phosphate mannose synthase from the filamentous fungus Trichoderma reesei belongs to the human and Schizosaccharomyces pombe class of the enzyme.","citation":"Glycobiology 2000 Oct;10(10):983-91","abstract":"Dolichol phosphate mannose (DPM) synthase activity, which is required in N:-glycosylation, O-mannosylation, and glycosylphosphatidylinositol membrane anchoring of protein, has been postulated to regulate the Trichoderma reesei secretory pathway. We have cloned a T.reesei cDNA that encodes a 243 amino acid protein whose amino acid sequence shows 67% and 65% identity, respectively, to the Schizosaccharomyces pombe and human DPM synthases, and which lacks the COOH-terminal hydrophobic domain characteristic of the Saccharomyces cerevisiae class of synthase. The Trichoderma dpm1 (Trdpm1) gene complements a lethal null mutation in the S.pombe dpm1(+) gene, but neither restores viability of a S.cerevisiae dpm1-disruptant nor complements the temperature-sensitivity of the S. cerevisiae dpm1-6 mutant. The T.reesei DPM synthase is therefore a member of the \"human\" class of enzyme. Overexpression of Trdpm1 in a dpm1(+)::his7/dpm1(+) S.pombe diploid resulted in a 4-fold increase in specific DPM synthase activity. However, neither the wild type T. reesei DPM synthase, nor a chimera consisting of this protein and the hydrophobic COOH terminus of the S.cerevisiae DPM synthase, complemented an S.cerevisiae dpm1 null mutant or gave active enzyme when expressed in E.coli. The level of the Trdpm1 mRNA in T.reesei QM9414 strain was dependent on the composition of the culture medium. Expression levels of Trdpm1 were directly correlated with the protein secretory capacity of the fungus.","authors":"Kruszewska JS, Saloheimo M, Migdalski A, Orlean P, Penttilä M, Palamarczyk G","authors_abbrev":"Kruszewska JS et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-10-13","publication_year":"2000","canto_session_key":"6f7567981a9b643d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-09-05 17:15:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-05 15:01:58","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.16c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-05"},{"uniquename":"PMID:24055157","title":"CK1 is required for a mitotic checkpoint that delays cytokinesis.","citation":"Curr Biol 2013 Oct 07;23(19):1920-6","abstract":"Failure to accurately partition genetic material during cell division causes aneuploidy and drives tumorigenesis. Cell-cycle checkpoints safeguard cells from such catastrophes by impeding cell-cycle progression when mistakes arise. FHA-RING E3 ligases, including human RNF8 and CHFR and fission yeast Dma1, relay checkpoint signals by binding phosphorylated proteins via their FHA domains and promoting ubiquitination of downstream targets. Upon mitotic checkpoint activation, S. pombe Dma1 concentrates at spindle pole bodies (SPBs) in an FHA-dependent manner and ubiquitinates Sid4, a scaffold of Polo kinase, to suspend cytokinesis. However, the kinase or kinases that phosphoprime Sid4 for Dma1-mediated ubiquitination are unknown. Here, we report that the highly conserved protein kinase CK1 transmits the signal necessary to stall cytokinesis by phosphopriming Sid4 for Dma1-mediated ubiquitination. Like Dma1, CK1 accumulates at SPBs during a mitotic arrest and associates stably with SPB components, including Sid4. Our results establish CK1 as an integral component of a mitotic, ubiquitin-mediated checkpoint pathway.","doi":"10.1016/j.cub.2013.07.077","authors":"Johnson AE, Chen JS, Gould KL","authors_abbrev":"Johnson AE et al.","pubmed_publication_date":"07 Oct 2013","pubmed_entrez_date":"2013-09-24","publication_year":"2013","canto_session_key":"5fec0b80ee107b83","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-28 21:06:25","canto_approved_date":"2026-04-11 03:55:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-28 21:02:14","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.12","SPAC222.10c","SPBC649.05","SPCC1739.11c","SPAC24B11.11c","SPBC32F12.04","SPBC21.06c","SPAC6G9.06c","SPCC417.07c","SPAC4H3.11c","SPCC1682.04","SPBC3H7.15","SPBC244.01c","SPBC1347.06c","SPAC17G8.10c"],"gene_count":15,"ltp_gene_count":5,"approved_date":"2022-09-28"},{"uniquename":"PMID:2011520","title":"Cloning and sequence determination of the Schizosaccharomyces pombe rpb1 gene encoding the largest subunit of RNA polymerase II.","citation":"Nucleic Acids Res 1991 Feb 11;19(3):461-8","abstract":"The gene, rpb1, encoding the largest subunit of RNA polymerase II has been cloned from Schizosaccharomyces pombe using the corresponding gene, RPB1, of Saccharomyces cerevisiae as a cross-hybridization probe. We have determined the complete sequence of this gene, and parts of PCR-amplified rpb1 cDNA. The predicted coding sequence, interrupted by six introns, encodes a polypeptide of 1,752 amino acid residues in length with a molecular weight of 194 kilodaltons. This polypeptide contains eight conserved structural domains characteristic of the largest subunit of RNA polymerases from other eukaryotes and, in addition, 29 repetitions of the C-terminal heptapeptide found in all the eukaryotic RNA polymerase II largest subunits so far examined.","authors":"Azuma Y, Yamagishi M, Ueshima R, Ishihama A","authors_abbrev":"Azuma Y et al.","pubmed_publication_date":"11 Feb 1991","pubmed_entrez_date":"1991-02-11","publication_year":"1991","canto_session_key":"5ab72266096af0f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:15:29","canto_approved_date":"2018-12-22 20:15:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 20:15:23","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:35403927","title":"Basis for using thioredoxin as an electron donor by Schizosaccharomyces pombe Gpx1 and Tpx1.","citation":"AMB Express 2022 Apr 11;12(1):41","abstract":"Glutathione (GSH) peroxidases (GPxs or GSHPx) and thioredoxin (Trx) peroxidases (TPxs) are two classes of peroxidases that catalyze the reduction of peroxides. GPxs and TPxs generally use GSH or Trx, respectively, to recycle the oxidized cysteine (Cys) residue in the protein. However, it is unclear why unlike human GPxs, the Schizosaccharomyces pombe Gpx1 (spGpx1) prefers Trx over GSH for recycling of the active-site peroxidatic Cys residue. Here, we compared spGpx1 and S. pombe Tpx1 (spTpx1) protein sequences with those of their respective homologs in Saccharomyces cerevisiae and humans. Our analysis revealed that like spTpx1, spGpx1 contains a pair of conserved Cys residues (Cys36 and Cys82). These two conserved Cys residues are named peroxidatic and resolving Cys residues, respectively, and are found only in GPxs and TPxs that prefer Trx as an electron donor. Our analysis suggested that Cys36 and Cys82 in spGpx1 are most likely to form a disulfide bond upon oxidation of Cys36. Molecular modelling predicted that a conformational change might be required for the formation of this disulfide bond. Evolutionary analysis suggested that fungal GPxs and TPxs are related by divergent evolution from a common ancestor. Our analyses support a prediction that while spGpx1 and spTpx1 are phylogenetically and functionally different, they evolved from a common ancestor and use a similar mechanism for recycling of the active-site peroxidatic Cys residue.","doi":"10.1186/s13568-022-01381-2","authors":"Ahmad F, Latif MF, Luo Y, Huang Y","authors_abbrev":"Ahmad F et al.","pubmed_publication_date":"11 Apr 2022","pubmed_entrez_date":"2022-04-11","publication_year":"2022","canto_session_key":"586754ee9292f573","canto_annotation_status":"APPROVED","canto_triage_status":"Bioinformatics","canto_curator_role":"PomBase","canto_first_approved_date":"2024-04-13 07:57:07","canto_approved_date":"2025-11-24 09:17:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-13 07:57:01","canto_added_date":"2022-04-13 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.03c","SPCC576.03c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2024-04-13"},{"uniquename":"PMID:19804756","title":"A supramodular FHA/BRCT-repeat architecture mediates Nbs1 adaptor function in response to DNA damage.","citation":"Cell 2009 Oct 02;139(1):100-11","abstract":"The Mre11/Rad50/Nbs1 protein complex plays central enzymatic and signaling roles in the DNA-damage response. Nuclease (Mre11) and scaffolding (Rad50) components of MRN have been extensively characterized, but the molecular basis of Nbs1 function has remained elusive. Here, we present a 2.3A crystal structure of the N-terminal region of fission yeast Nbs1, revealing an unusual but conserved architecture in which the FHA- and BRCT-repeat domains structurally coalesce. We demonstrate that diphosphorylated pSer-Asp-pThr-Asp motifs, recently identified as multicopy docking sites within Mdc1, are evolutionarily conserved Nbs1 binding targets. Furthermore, we show that similar phosphomotifs within Ctp1, the fission yeast ortholog of human CtIP, promote interactions with the Nbs1 FHA domain that are necessary for Ctp1-dependent resistance to DNA damage. Finally, we establish that human Nbs1 interactions with Mdc1 occur through both its FHA- and BRCT-repeat domains, suggesting how their structural and functional interdependence underpins Nbs1 adaptor functions in the DNA-damage response.","doi":"10.1016/j.cell.2009.07.043","authors":"Lloyd J, Chapman JR, Clapperton JA, Haire LF, Hartsuiker E, Li J, Carr AM, Jackson SP, Smerdon SJ","authors_abbrev":"Lloyd J et al.","pubmed_publication_date":"02 Oct 2009","pubmed_entrez_date":"2009-10-07","publication_year":"2009","canto_session_key":"e36b99ed5d28ee19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-03-22 16:12:25","canto_approved_date":"2023-12-07 17:47:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-22 16:12:14","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":80,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.08","SPBC6B1.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-03-22","pdb_entries":[{"pdb_id":"3i0m","gene_chains":[{"gene_uniquename":"SPBC6B1.09c","chain":"A","position":"1-324"}],"title":"Structure of the S. pombe Nbs1 FHA/BRCT-repeat domain","entry_authors":"Clapperton JA,Lloyd J,Chapman JR,Jackson SP,Smerdon SJ","entry_authors_abbrev":"Clapperton JA et al.","reference_uniquename":"PMID:19804756","experimental_method":"X-ray","resolution":"2.6"},{"pdb_id":"3i0n","gene_chains":[{"gene_uniquename":"SPBC6B1.09c","chain":"A/B","position":"1-324"}],"title":"Structure of the S. pombe Nbs1 FHA/BRCT-repeat domain","entry_authors":"Clapperton JA,Lloyd J,Chapman JR,Jackson SP,Smerdon SJ","entry_authors_abbrev":"Clapperton JA et al.","reference_uniquename":"PMID:19804756","experimental_method":"X-ray","resolution":"2.3"}]},{"uniquename":"PMID:24362567","title":"Aprataxin resolves adenylated RNA-DNA junctions to maintain genome integrity.","citation":"Nature 2014 Feb 06;506(7486):111-5","abstract":"Faithful maintenance and propagation of eukaryotic genomes is ensured by three-step DNA ligation reactions used by ATP-dependent DNA ligases. Paradoxically, when DNA ligases encounter nicked DNA structures with abnormal DNA termini, DNA ligase catalytic activity can generate and/or exacerbate DNA damage through abortive ligation that produces chemically adducted, toxic 5'-adenylated (5'-AMP) DNA lesions. Aprataxin (APTX) reverses DNA adenylation but the context for deadenylation repair is unclear. Here we examine the importance of APTX to RNase-H2-dependent excision repair (RER) of a lesion that is very frequently introduced into DNA, a ribonucleotide. We show that ligases generate adenylated 5' ends containing a ribose characteristic of RNase H2 incision. APTX efficiently repairs adenylated RNA-DNA, and acting in an RNA-DNA damage response (RDDR), promotes cellular survival and prevents S-phase checkpoint activation in budding yeast undergoing RER. Structure-function studies of human APTX-RNA-DNA-AMP-Zn complexes define a mechanism for detecting and reversing adenylation at RNA-DNA junctions. This involves A-form RNA binding, proper protein folding and conformational changes, all of which are affected by heritable APTX mutations in ataxia with oculomotor apraxia 1. Together, these results indicate that accumulation of adenylated RNA-DNA may contribute to neurological disease.","doi":"10.1038/nature12824","authors":"Tumbale P, Williams JS, Schellenberg MJ, Kunkel TA, Williams RS","authors_abbrev":"Tumbale P et al.","pubmed_publication_date":"06 Feb 2014","pubmed_entrez_date":"2013-12-24","publication_year":"2014","canto_session_key":"7192b795ff5a2cca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-12-15 21:45:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-12-15 21:45:22","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-12-15"},{"uniquename":"PMID:16756067","title":"[The role of recombinational repair proteins in mating type switching in fission yeast cells].","citation":"Genetika 2006 Apr;42(4):487-93","abstract":"DNA double-strand breaks (DSBs) occur after exposing cells to ionizing radiation or under the action of various antitumor antibiotics. They can be also generated in the course cell processes, such as meiosis and mating type switching in yeast. The most preferential mechanism for the correction of DNA DSB in yeasts is recombinational repair controlled by RAD52 group genes. The role of recombinational repair in mating type switching of fission yeast cells was examined on the example of genes of this group, rhp51+ and rhp51+. We constructed homothallic strains of genotypes h90 rhp51 and h90 rhp55, and found that mutant cells yielded colonies with the mottled phenotype. In addition, h90 cells with deletions in these genes were shown to segregate heterothallic iodine-negative colonies h- and h+. The genome region, responsible for the switching process in these segregants, was analyzed by DNA hybridization. As shown in this analysis, h+ segregants had the h+N or h90 configuration of the mat region, whereas h-, the h90 configuration. Segregants h+ contained DNA duplication in the mat region. DNA rearrangements were not detected at the mating type locus, but the level of DNA DSB formation was drastically decreased in these segregants. Thus, our results show that genes rhp51+ and rhp55+ are involved not only in the repair of induced DNA DSB, but also in the mechanism of mating type switching in fission yeast.","authors":"Vagin DA, Khasanov FK, Bashkirov VI","authors_abbrev":"Vagin DA et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-06-08","publication_year":"2006","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38629626","title":"A zinc-finger protein Moc3 functions as a transcription activator to promote RNAi-dependent constitutive heterochromatin establishment in fission yeast.","citation":"Genes Cells 2024 Apr 17;","abstract":"In fission yeast, Schizosaccharomyces pombe, constitutive heterochromatin defined by methylation of histone H3 lysine 9 (H3K9me) and its binding protein Swi6/HP1 localizes at the telomere, centromere, and mating-type loci. These loci contain DNA sequences called dg and dh, and the RNA interference (RNAi)-dependent system establishes and maintains heterochromatin at dg/dh. Bi-directional transcription at dg/dh induced by RNA polymerase II is critical in RNAi-dependent heterochromatin formation because the transcribed RNAs provide substrates for siRNA synthesis and a platform for assembling RNAi factors. However, a regulator of dg/dh transcription during the establishment of heterochromatin is not known. Here, we found that a zinc-finger protein Moc3 localizes dh and activates dh-forward transcription in its zinc-finger-dependent manner when heterochromatin structure or heterochromatin-dependent silencing is compromised. However, Moc3 does not localize at normal heterochromatin and does not activate the dh-forward transcription. Notably, the loss of Moc3 caused a retarded heterochromatin establishment, showing that Moc3-dependent dh-forward transcription is critical for RNAi-dependent heterochromatin establishment. Therefore, Moc3 is a transcriptional activator that induces RNAi to establish heterochromatin.","doi":"10.1111/gtc.13116","authors":"Mori M, Sato M, Takahata S, Kajitani T, Murakami Y","authors_abbrev":"Mori M et al.","pubmed_publication_date":"17 Apr 2024","pubmed_entrez_date":"2024-04-17","publication_year":"2024","canto_session_key":"1752e56114b1e7a7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-04-17 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24449889","title":"Kinetochore assembly and heterochromatin formation occur autonomously in Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 2014 Feb 04;111(5):1903-8","abstract":"Kinetochores in multicellular eukaryotes are usually associated with heterochromatin. Whether this heterochromatin simply promotes the cohesion necessary for accurate chromosome segregation at cell division or whether it also has a role in kinetochore assembly is unclear. Schizosaccharomyces pombe is an important experimental system for investigating centromere function, but all of the previous work with this species has exploited a single strain or its derivatives. The laboratory strain and most other S. pombe strains contain three chromosomes, but one recently discovered strain, CBS 2777, contains four. We show that the genome of CBS 2777 is related to that of the laboratory strain by a complex chromosome rearrangement. As a result, two of the kinetochores in CBS 2777 contain the central core sequences present in the laboratory strain centromeres, but lack adjacent heterochromatin. The closest block of heterochromatin to these rearranged kinetochores is ∼100 kb away at new telomeres. Despite lacking large amounts of adjacent heterochromatin, the rearranged kinetochores bind CENP-A(Cnp1) and CENP-C(Cnp3) in similar quantities and with similar specificities as those of the laboratory strain. The simplest interpretation of this result is that constitutive kinetochore assembly and heterochromatin formation occur autonomously.","doi":"10.1073/pnas.1216934111","authors":"Brown WR, Thomas G, Lee NC, Blythe M, Liti G, Warringer J, Loose MW","authors_abbrev":"Brown WR et al.","pubmed_publication_date":"04 Feb 2014","pubmed_entrez_date":"2014-01-23","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22512868","title":"Regulation of transcriptome, translation, and proteome in response to environmental stress in fission yeast.","citation":"Genome Biol 2012 Apr 18;13(4):R25","abstract":"Gene expression is controlled globally and at multiple levels in response to environmental stress, but the relationships among these dynamic regulatory changes are not clear. Here we analyzed global regulation during different stress conditions in fission yeast, Schizosaccharomyces pombe, combining dynamic genome-wide data on mRNA, translation, and protein profiles.\nWe observed a strong overall concordance between changes in mRNAs and co-directional changes in translation, for both induced and repressed genes, in response to three conditions: oxidative stress, heat shock, and DNA damage. However, approximately 200 genes each under oxidative and heat stress conditions showed discordant regulation with respect to mRNA and translation profiles, with genes and patterns of regulation being stress-specific. For oxidative stress, we also measured dynamic profiles for 2,147 proteins, comprising 43% of the proteome. The mRNAs induced during oxidative stress strongly correlated with increased protein expression, while repressed mRNAs did not relate to the corresponding protein profiles. Overall changes in relative protein expression correlated better with changes in mRNA expression than with changes in translational efficiency.\nThese data highlight a global coordination and fine-tuning of gene regulation during stress that mostly acts in the same direction at the levels of transcription and translation. In the oxidative stress condition analyzed, transcription dominates translation to control protein abundance. The concordant regulation of transcription and translation leads to the expected adjustment in protein expression only for up-regulated mRNAs. These patterns of control might reflect the need to balance protein production for stress survival given a limited translational capacity.","doi":"10.1186/gb-2012-13-4-r25","authors":"Lackner DH, Schmidt MW, Wu S, Wolf DA, Bähler J","authors_abbrev":"Lackner DH et al.","pubmed_publication_date":"18 Apr 2012","pubmed_entrez_date":"2012-04-20","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27999345","title":"Combined Use of S. pombe and L. thermotolerans in Winemaking. Beneficial Effects Determined Through the Study of Wines' Analytical Characteristics.","citation":"Molecules 2016 Dec 18;21(12)","abstract":"The most common way to produce red wine is through the use of  Saccharomyces cerevisiae  strains for alcoholic fermentation and lactic acid bacteria for malolactic fermentation. This traditional winemaking methodology produces microbiologically stable red wines. However, under specific conditions off-flavours can occur, wine quality can suffer and human health problems are possible, especially after the second fermentation by the lactic acid bacteria. In warm countries, problems during the malolactic fermentation arise because of the high pH of the must, which makes it very difficult to properly control the process. Under such conditions, wines with high acetic acid and histamine concentrations are commonly produced. This study investigates a recent red wine-making technology that uses a combination of  Lachancea thermotolerans  and  Schizosaccharomyces pombe  as an alternative to the conventional malolactic fermentation. This work studies new parameters such as aroma compounds, amino acids, ethanol index and sensory evaluation.  Schizosaccharomyces pombe  totally consumes malic acid while  Lachancea thermotolerans  produces lactic acid, avoiding excessive deacidification of musts with low acidity in warm viticulture areas. This methodology also reduces the malolactic fermentation hazards in wines with low acidity. The main products are wines that contain less acetic acid, less biogenic amines and precursors and less ethyl carbamate precursors than the traditional wines produced via conventional fermentation techniques.","doi":"10.3390/molecules21121744","authors":"Benito Á, Calderón F, Benito S","authors_abbrev":"Benito Á et al.","pubmed_publication_date":"18 Dec 2016","pubmed_entrez_date":"2016-12-22","publication_year":"2016","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2016-12-23 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPHSP70","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32970792","title":"The Pex3-Inp1 complex tethers yeast peroxisomes to the plasma membrane.","citation":"J Cell Biol 2020 Oct 05;219(10)","abstract":"A subset of peroxisomes is retained at the mother cell cortex by the Pex3-Inp1 complex. We identify Inp1 as the first known plasma membrane-peroxisome (PM-PER) tether by demonstrating that Inp1 meets the predefined criteria that a contact site tether protein must adhere to. We show that Inp1 is present in the correct subcellular location to interact with both the plasma membrane and peroxisomal membrane and has the structural and functional capacity to be a PM-PER tether. Additionally, expression of artificial PM-PER tethers is sufficient to restore retention in inp1Δ cells. We show that Inp1 mediates peroxisome retention via an N-terminal domain that binds PI(4,5)P2 and a C-terminal Pex3-binding domain, forming a bridge between the peroxisomal membrane and the plasma membrane. We provide the first molecular characterization of the PM-PER tether and show it anchors peroxisomes at the mother cell cortex, suggesting a new model for peroxisome retention.","doi":"10.1083/jcb.201906021","authors":"Hulmes GE, Hutchinson JD, Dahan N, Nuttall JM, Allwood EG, Ayscough KR, Hettema EH","authors_abbrev":"Hulmes GE et al.","pubmed_publication_date":"05 Oct 2020","pubmed_entrez_date":"2020-09-24","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29A4.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33374320","title":"FRCaMP, a Red Fluorescent Genetically Encoded Calcium Indicator Based on Calmodulin from Schizosaccharomyces Pombe Fungus.","citation":"Int J Mol Sci 2020 Dec 24;22(1)","abstract":"Red fluorescent genetically encoded calcium indicators (GECIs) have expanded the available pallet of colors used for the visualization of neuronal calcium activity in vivo. However, their calcium-binding domain is restricted by calmodulin from metazoans. In this study, we developed red GECI, called FRCaMP, using calmodulin (CaM) from  Schizosaccharomyces pombe  fungus as a calcium binding domain. Compared to the R-GECO1 indicator in vitro, the purified protein FRCaMP had similar spectral characteristics, brightness, and pH stability but a 1.3-fold lower ΔF/F calcium response and 2.6-fold tighter calcium affinity with K d  of 441 nM and 2.4-6.6-fold lower photostability. In the cytosol of cultured HeLa cells, FRCaMP visualized calcium transients with a ΔF/F dynamic range of 5.6, which was similar to that of R-GECO1. FRCaMP robustly visualized the spontaneous activity of neuronal cultures and had a similar ΔF/F dynamic range of 1.7 but 2.1-fold faster decay kinetics vs. NCaMP7. On electrically stimulated cultured neurons, FRCaMP demonstrated 1.8-fold faster decay kinetics and 1.7-fold lower ΔF/F values per one action potential of 0.23 compared to the NCaMP7 indicator. The fungus-originating CaM of the FRCaMP indicator version with a deleted M13-like peptide did not interact with the cytosolic environment of the HeLa cells in contrast to the metazoa-originating CaM of the similarly truncated version of the GCaMP6s indicator with a deleted M13-like peptide. Finally, we generated a split version of the FRCaMP indicator, which allowed the simultaneous detection of calcium transients and the heterodimerization of bJun/bFos interacting proteins in the nuclei of HeLa cells with a ΔF/F dynamic range of 9.4 and a contrast of 2.3-3.5, respectively.","doi":"10.3390/ijms22010111","authors":"Subach OM, Barykina NV, Chefanova ES, Vlaskina AV, Sotskov VP, Ivashkina OI, Anokhin KV, Subach FV","authors_abbrev":"Subach OM et al.","pubmed_publication_date":"24 Dec 2020","pubmed_entrez_date":"2020-12-30","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-01-02 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22978652","title":"A small molecule inhibitor of Pot1 binding to telomeric DNA.","citation":"Biochemistry 2012 Oct 09;51(40):7833-45","abstract":"Chromosome ends are complex structures, consisting of repetitive DNA sequence terminating in an ssDNA overhang with many associated proteins. Because alteration of the regulation of these ends is a hallmark of cancer, telomeres and telomere maintenance have been prime drug targets. The universally conserved ssDNA overhang is sequence-specifically bound and regulated by Pot1 (protection of telomeres 1), and perturbation of Pot1 function has deleterious effects for proliferating cells. The specificity of the Pot1/ssDNA interaction and the key involvement of this protein in telomere maintenance have suggested directed inhibition of Pot1/ssDNA binding as an efficient means of disrupting telomere function. To explore this idea, we developed a high-throughput time-resolved fluorescence resonance energy transfer (TR-FRET) screen for inhibitors of Pot1/ssDNA interaction. We conducted this screen with the DNA-binding subdomain of Schizosaccharomyces pombe Pot1 (Pot1pN), which confers the vast majority of Pot1 sequence-specificity and is highly similar to the first domain of human Pot1 (hPOT1). Screening a library of ∼20 000 compounds yielded a single inhibitor, which we found interacted tightly with sub-micromolar affinity. Furthermore, this compound, subsequently identified as the bis-azo dye Congo red (CR), was able to competitively inhibit hPOT1 binding to telomeric DNA. Isothermal titration calorimetry and NMR chemical shift analysis suggest that CR interacts specifically with the ssDNA-binding cleft of Pot1, and that alteration of this surface disrupts CR binding. The identification of a specific inhibitor of ssDNA interaction establishes a new pathway for targeted telomere disruption.","doi":"10.1021/bi300365k","authors":"Altschuler SE, Croy JE, Wuttke DS","authors_abbrev":"Altschuler SE et al.","pubmed_publication_date":"09 Oct 2012","pubmed_entrez_date":"2012-09-18","publication_year":"2012","canto_session_key":"6e9f54515f6080c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-11-04 12:26:11","canto_approved_date":"2020-01-17 19:17:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-25 08:00:51","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26H5.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-11-04"},{"uniquename":"PMID:39165565","title":"Extracellular calcium promotes internalization and degradation of the fission yeast TRP-like calcium ion channel Pkd2.","citation":"MicroPubl Biol 2024;2024","abstract":"The correct localization of proteins is linked to their cellular function. The  Schizosaccharomyces pombe  Pkd2 localizes to the endoplasmic reticulum and plasma membrane. Here we investigate the behavior of Pkd2 in response to calcium. Pkd2-GFP, normally enriched at the cell ends, is reduced from the plasma membrane by CaCl  2  addition, while cytoplasmic dots and free GFP are increased. This suggests that Pkd2 is internalized and degraded in response to extracellular CaCl  2  . This internalization is partially suppressed by treatment with an Arp2/3 inhibitor, CK-666. Our data provide new insights into the relationship between Pkd2 internalization and calcium response.","doi":"10.17912/micropub.biology.001265","authors":"Koyano T, Onishi K, Matsuyama M, Fukushima M, Kume K","authors_abbrev":"Koyano T et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-08-21","publication_year":"2024","canto_session_key":"c8860af873c0f200","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-09-30 16:25:19","canto_approved_date":"2024-09-30 16:25:20","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-09-30 09:52:59","canto_added_date":"2024-08-21 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2024-09-30"},{"uniquename":"PMID:27401558","title":"The Nrd1-like protein Seb1 coordinates cotranscriptional 3' end processing and polyadenylation site selection.","citation":"Genes Dev 2016 Jul 01;30(13):1558-72","abstract":"Termination of RNA polymerase II (RNAPII) transcription is associated with RNA 3' end formation. For coding genes, termination is initiated by the cleavage/polyadenylation machinery. In contrast, a majority of noncoding transcription events in Saccharomyces cerevisiae does not rely on RNA cleavage for termination but instead terminates via a pathway that requires the Nrd1-Nab3-Sen1 (NNS) complex. Here we show that the Schizosaccharomyces pombe ortholog of Nrd1, Seb1, does not function in NNS-like termination but promotes polyadenylation site selection of coding and noncoding genes. We found that Seb1 associates with 3' end processing factors, is enriched at the 3' end of genes, and binds RNA motifs downstream from cleavage sites. Importantly, a deficiency in Seb1 resulted in widespread changes in 3' untranslated region (UTR) length as a consequence of increased alternative polyadenylation. Given that Seb1 levels affected the recruitment of conserved 3' end processing factors, our findings indicate that the conserved RNA-binding protein Seb1 cotranscriptionally controls alternative polyadenylation.","doi":"10.1101/gad.280222.116","authors":"Lemay JF, Marguerat S, Larochelle M, Liu X, van Nues R, Hunyadkürti J, Hoque M, Tian B, Granneman S, Bähler J, Bachand F","authors_abbrev":"Lemay JF et al.","pubmed_publication_date":"01 Jul 2016","pubmed_entrez_date":"2016-07-13","publication_year":"2016","canto_session_key":"4fb0ad7bc2d593e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Marc Larochelle","canto_first_approved_date":"2018-03-27 14:01:53","canto_approved_date":"2024-04-03 13:21:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-23 20:30:15","canto_added_date":"2016-07-14 00:15:13","annotation_curators":[{"name":"Marc Larochelle","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1709.15c","SPAC6G9.10c","SPAC664.05","SPAC3H8.09c","SPAC140.02","SPCC1442.14c","SPBC29A10.10c","SPAC17H9.05","SPAC29A4.04c","SPBC18E5.06","SPBP23A10.07","SPBC28F2.12","SPBC29B5.03c","SPBC19C2.07","SPAC18G6.14c","SPBP8B7.16c","SPBC776.01","SPAC23G3.01","SPAC17G6.16c","SPBC4C3.05c","SPBC646.10c","SPAC1F7.02c","SPSNORNA.32","SPAC16E8.06c","SPAC222.09","SPAC23C4.15","SPBC17D1.06","SPBC2D10.10c","SPCC576.08c","SPSNORNA.35","SPAC26A3.12c","SPAC57A10.10c","SPBC19F5.05c","SPBC1709.08","SPBP8B7.20c","SPAC1071.01c","SPAC926.08c","SPBC1711.16","SPAC23G3.06","SPAC2F7.11","SPAC6F12.17","SPBC800.06","SPCC1183.07"],"gene_count":43,"ltp_gene_count":4,"approved_date":"2018-03-27"},{"uniquename":"EMBL:AU006519","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013340","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18679823","title":"Human carbamoyl-phosphate synthetase: insight into N-acetylglutamate interaction and the functional effects of a common single nucleotide polymorphism.","citation":"J Inherit Metab Dis 2008 Aug;31(4):481-91","abstract":"Human carbamoyl-phosphate synthetase (hCPS) has evolved three features that allow it to remove excess, potentially neurotoxic ammonia via the urea cycle: inability to use glutamine as an alternative nitrogen donor; a K(m) for ammonia 100-fold lower than for CPSs that also use glutamine; and required allosteric activation by N-acetylglutamate (AGA), a sensor of excess amino acids. To determine the structural features of hCPS that allow its unique functioning, we have developed the first recombinant expression system for hCPS, utilizing Schizosaccharomyces pombe. Of several common single-nucleotide polymorphisms identified in the gene encoding hCPS, only the one resulting in substitution of threonine at position 1406 with asparagine has been linked to phenotypic effects. We have expressed and characterized both variants of hCPS. The asparagine polymorph, hCPS_N, consistently displayed inferior catalytic properties, but the K(m) and k(cat) values for overall and partial reactions varied only by a factor of 1.7 or less. We have designed and characterized an hCPS construction from which the N-terminal domain A is deleted. hCPS_DeltaA was competent to bind AGA, demonstrating that domain A does not contain the AGA binding site. Thus, the site at the C/D boundary previously identified by AGA analogue labelling appears to be the functionally significant initial binding site for AGA. However, hCPS_DeltaA was not able to fully assume the catalytically competent conformation, with specific activity of CP formation decreased 700-fold.","doi":"10.1007/s10545-008-0913-y","authors":"Ahuja V, Powers-Lee SG","authors_abbrev":"Ahuja V et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-08-06","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB001021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.586"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU007699","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22580453","title":"Chemical inactivation of Pat1: a novel approach to synchronize meiosis.","citation":"Cell Cycle 2012 May 15;11(10):1875","abstract":"","doi":"10.4161/cc.20512","authors":"Pérez-Hidalgo L, Moreno S","authors_abbrev":"Pérez-Hidalgo L et al.","pubmed_publication_date":"15 May 2012","pubmed_entrez_date":"2012-05-15","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16199868","title":"Schizosaccharomyces pombe mst2+ encodes a MYST family histone acetyltransferase that negatively regulates telomere silencing.","citation":"Mol Cell Biol 2005 Oct;25(20):8887-903","abstract":"Histone acetylation and deacetylation are associated with transcriptional activity and the formation of constitutively silent heterochromatin. Increasingly, histone acetylation is also implicated in other chromosome transactions, including replication and segregation. We have cloned the only Schizosaccharomyces pombe MYST family histone acetyltransferase genes, mst1(+) and mst2(+). Mst1p, but not Mst2p, is essential for viability. Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle. Deltamst2 genetically interacts with mutants that affect heterochromatin, cohesion, and telomere structure. Mst2p is a negative regulator of silencing at the telomere but does not affect silencing in the centromere or mating type region. We generated a census of proteins and histone modifications at wild-type telomeres. A histone acetylation gradient at the telomeres is lost in Deltamst2 cells without affecting the distribution of Taz1p, Swi6p, Rad21p, or Sir2p. We propose that the increased telomeric silencing is caused by histone hypoacetylation and/or an increase in the ratio of methylated to acetylated histones. Although telomere length is normal, meiosis is aberrant in Deltamst2 diploid homozygote mutants, suggesting that telomeric histone acetylation contributes to normal meiotic progression.","authors":"Gómez EB, Espinosa JM, Forsburg SL","authors_abbrev":"Gómez EB et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-10-04","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.07c","SPBC776.12c","SPCC338.17c","SPAC17G8.13c","SPAC637.12c","SPAC664.01c","SPBC29A10.15"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:11250894","title":"Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA.","citation":"EMBO J 2001 Mar 15;20(6):1281-8","abstract":"Oxa1p is a member of the conserved Oxa1/YidC/Alb3 protein family involved in the membrane insertion of proteins. Oxa1p has been shown previously to directly facilitate the export of the N-terminal domains of membrane proteins across the inner membrane to the intermembrane space of mitochondria. Here we report on a general role of Oxa1p in the membrane insertion of proteins. (i) The function of Oxa1p is not limited to the insertion of membrane proteins that undergo N-terminal tail export; rather, it also extends to the insertion of other polytopic proteins such as the mitochondrially encoded Cox1p and Cox3p proteins. These are proteins whose N-termini are retained in the mitochondrial matrix. (ii) Oxa1p interacts directly with these substrates prior to completion of their synthesis. (iii) The interaction of Oxa1p with its substrates is particularly strong when nascent polypeptide chains are inserted into the inner membrane, suggesting a direct function of Oxa1p in co-translational insertion from the matrix. Taken together, we conclude that the Oxa1 complex represents a general membrane protein insertion machinery in the inner membrane of mitochondria.","authors":"Hell K, Neupert W, Stuart RA","authors_abbrev":"Hell K et al.","pubmed_publication_date":"15 Mar 2001","pubmed_entrez_date":"2001-03-17","publication_year":"2001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPMIT.01","SPAC9G1.04"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:39833200","title":"Centromere positioning orchestrates telomere bouquet formation and the initiation of meiotic differentiation.","citation":"Nat Commun 2025 Jan 20;16(1):837","abstract":"Accurate gametogenesis requires the establishment of the telomere bouquet, an evolutionarily conserved, 3D chromosomal arrangement. In this spatial configuration, telomeres temporarily aggregate at the nuclear envelope during meiotic prophase, which facilitates chromosome pairing and recombination. The mechanisms governing the assembly of the telomere bouquet remain largely unexplored, primarily due to the challenges in visualizing and manipulating the bouquet. Here, using Schizosaccharomyces pombe as a model system to elucidate telomere bouquet function, we reveal that centromeres, traditionally perceived as playing a passive role in the chromosomal reorganization necessary for bouquet assembly, play a key role in the initiation of telomere bouquet formation. We demonstrate that centromeres are capable to induce telomere mobilization, which is sufficient to trigger the first stages of bouquet assembly and the meiotic transcription program in mitotic cells. This discovery highlights the finely tuned control exerted over long-distance heterochromatic regions and underscores a pivotal step in the mechanism of eukaryotic telomere bouquet formation and meiotic transcriptional rewiring.","doi":"10.1038/s41467-025-56049-9","authors":"Jiménez-Martín A, Pineda-Santaella A, Martín-García R, Esteban-Villafañe R, Matarrese A, Pinto-Cruz J, Camacho-Cabañas S, León-Periñán D, Terrizzano A, Daga RR, Braun S, Fernández-Álvarez A","authors_abbrev":"Jiménez-Martín A et al.","pubmed_publication_date":"20 Jan 2025","pubmed_entrez_date":"2025-01-20","publication_year":"2025","canto_session_key":"c717e2d7ee7b8ded","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alfonso Fernández-Álvarez","canto_first_approved_date":"2026-06-05 06:58:33","canto_approved_date":"2026-06-05 06:58:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-05-29 07:13:37","canto_added_date":"2025-01-22 00:25:05","annotation_curators":[{"name":"Alfonso Fernández-Álvarez","community_curator":true,"annotation_count":19,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":83,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC622.16c","SPAC212.11","SPAC27F1.04c","SPBC1348.12","SPCC417.07c","SPAC869.04","SPBC365.15","SPCC594.05c","SPBC12D12.01","SPAC3A11.05c","SPBC428.08c","SPBPB2B2.13","SPBC1685.15c","SPAC1687.20c","SPAC18G6.10","SPBC2G2.14","SPBC19C7.10","SPCC1223.15c","SPAC29B12.02c","SPBCPT2R1.08c","SPBC1348.14c","SPBPB21E7.01c","SPAC16A10.07c","SPBC11C11.03","SPAC6G9.13c","SPBC1778.02","SPCC594.07c","SPAC15A10.15","SPAC186.01","SPAC25G10.04c","SPAC1F8.02c","SPCC306.04c","SPAC977.16c","SPBP4G3.03","SPBC32C12.02","SPAC1093.06c","SPAC1805.07c","SPAC1F8.01","SPAC27D7.03c","SPNCRNA.103","SPAC19E9.01c","SPBC32F12.05c","SPBC13G1.08c","SPAC1002.06c","SPCC895.07","SPAC977.18","SPAC750.01","SPAC17G8.13c","SPBC354.03","SPBC11B10.09","SPAC869.07c"],"gene_count":51,"ltp_gene_count":16,"approved_date":"2026-06-05"},{"uniquename":"PMID:12615979","title":"Polo boxes form a single functional domain that mediates interactions with multiple proteins in fission yeast polo kinase.","citation":"J Cell Sci 2003 Apr 01;116(Pt 7):1377-87","abstract":"Polo kinases play multiple roles in cell cycle regulation in eukaryotic cells. In addition to the kinase domain, conservation at the primary sequence level is also found in the non-catalytic region mainly in three blocks, namely the polo boxes. Although several studies have implicated the polo boxes in protein localisation, no systematic study to elucidate the roles of individual polo boxes has been carried out. Here we show, by using fission yeast, that the polo boxes form a single functional unit that is essential for both cellular function and cell-cycle-regulated localisation to the spindle pole bodies. Various polo box mutations abolish the mitotic arrest seen upon overexpression of plo1 but do not prevent the untimely septation seen under these conditions, showing that the functions of Plo1 may be separated. Plo1 interacts with multiple proteins including cell cycle regulators in a polo-box-dependent manner. Isolation of mutants that differentially disrupt these interactions revealed a role for the polo boxes in mediating protein-protein interactions.","authors":"Reynolds N, Ohkura H","authors_abbrev":"Reynolds N et al.","pubmed_publication_date":"01 Apr 2003","pubmed_entrez_date":"2003-03-05","publication_year":"2003","canto_session_key":"b74f9d9ca791af8a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-08-13 13:41:42","canto_approved_date":"2026-01-31 11:54:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-10 13:11:38","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":161,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_12615979_phaf.tsv"}],"genes":["SPCC4B3.15","SPBC800.09","SPAC26H5.05","SPAC6B12.08","SPAC6F12.14","SPAC1006.03c","SPBC20F10.06","SPAC23C11.16","SPAC1B9.02c","SPBC1861.02"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2015-08-13"},{"uniquename":"PMID:895713","title":"Slow UV-recovery and fast gamma-recovery in wild-type Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1977 Jul 20;154(2):123-8","abstract":"The time course of recovery in UV- or gamma-irradiated wild-type Schizosaccharomyces pombe has been determined by fractionated dose experiments and by measuring the rate at which the \"resistant shoulder\" of the survival curve was regained during post-irradiation incubation in growth medium. The kinetics of recovery after UV-irradiation were different from those after gamma-irradiation, and may be described as due to a fasy gamm-repair and a relatively slow UV-repair process. In fractionated dose experiments, for single exposures which gave about 10% survival, gamma-repair was rapid (t1/2 congruent to 2 h), began immediately, and was essentially complete within 3 h. UV-repair, in contrast, showed a lag of about 5h and was relatively show (t1/2 congruent to 10h). The nature of the recovery response was analyzed from the survival curves at intermediate times; recovery was evident as the reappearance of a shoulder. A heterogenous recovery was evident after UV-irradiation; after a 5 h lag, a progressively increasing fraction of the survivors regained UV-resistance, which suggested that some critical event or rate-limiting step was involved. A requirement for post-irradiation protein synthesis for activity of a recombinational repair pathway on UV-damage may be a factor in the UV-recovery lag. A homogeneous recovery response, however, was observed in gamma-irradiaged cells.","authors":"Gentner NE, Werner MM","authors_abbrev":"Gentner NE et al.","pubmed_publication_date":"20 Jul 1977","pubmed_entrez_date":"1977-07-20","publication_year":"1977","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41334522","title":"Application of a One-Step method for rapid detection of nucleic acids from fungi.","citation":"Mycology 2025;16(4):1824-1836","abstract":"PCR-based techniques play a crucial role in genotyping and genetic screening in fungal biology. Rapid access to nucleic acids for these reactions can significantly improve the efficiency of fungal analysis, especially when multiple samples need to be tested. In this study, we introduced a simple and rapid method for detecting small amounts of fungal DNA or RNA, named the One-Step method, and confirmed its applicability across various experimental scenarios for fungal detection. The method involves scraping a small quantity of spores or mycelium into sterile water, followed by heat shock, vortexing, and centrifugation to obtain a supernatant that serves as a template for the PCR reaction. Notably, nucleic acids were successfully extracted using the One-Step method from four different genera of fungi- Neurospora crassa ,  Aspergillus fumigatus ,  Fusarium oxysporum , and  Schizosaccharomyces pombe , as well as from two mycovirus-containing strains, yielding reliable results in PCR identification. However, the nucleic acids of  Cryptococcus neoformans  were not successfully extracted using the One-Step method, possibly due to the challenge of cleaving its polysaccharide capsule. Taken together, the One-Step method significantly reduces nucleic acids extraction time while enhancing strain screening efficiency in four different fungi, indicating a broad applicability in fungal biology.","doi":"10.1080/21501203.2025.2471979","authors":"Yuan J, Qiao F, Chang W, Yang Y, Song L, Liu XL, Tian WX, Ren J, Liu X","authors_abbrev":"Yuan J et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-12-03","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-12-04 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20867886","title":"Kinetics of myosin node aggregation into a contractile ring.","citation":"Phys Rev Lett 2010 Jul 23;105(4):048102","abstract":"We study a stochastic aggregation model for the assembly of the contractile ring from a broad band of nodes during cytokinesis in fission yeast. We found that bands of nodes condense into rings when the range of node interactions is larger than the width of the band. Wide bands are unstable to clump formation due to Poisson density fluctuations. We derive expressions for node kinetics and times for ring vs clump formation and test them using numerical simulations. These results suggest clump formation mechanisms in mutant cells.","authors":"Ojkic N, Vavylonis D","authors_abbrev":"Ojkic N et al.","pubmed_publication_date":"23 Jul 2010","pubmed_entrez_date":"2010-09-28","publication_year":"2010","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35501388","title":"POH1/Rpn11/PSMD14: a journey from basic research in fission yeast to a prognostic marker and a druggable target in cancer cells.","citation":"Br J Cancer 2022 Sep;127(5):788-799","abstract":"POH1/Rpn11/PSMD14 is a highly conserved protein in eukaryotes from unicellular organisms to human and has a crucial role in cellular homoeostasis. It is a subunit of the regulatory particle of the proteasome, where it acts as an intrinsic deubiquitinase removing polyubiquitin chains from substrate proteins. This function is not only coupled to the translocation of substrates into the core of the proteasome and their subsequent degradation but also, in some instances, to the stabilisation of ubiquitinated proteins through their deubiquitination. POH1 was initially discovered as a functional homologue of the fission yeast gene pad1 + , which confers drug resistance when overexpressed. In translational studies, expression of POH1 has been found to be increased in several tumour types relative to normal adjacent tissue and to correlate with tumour progression, higher tumour grade, decreased sensitivity to cytotoxic drugs and poor prognosis. Proteasome inhibitors targeting the core particle of the proteasome are highly active in the treatment of myeloma, and recently developed POH1 inhibitors, such as capzimin and thiolutin, have shown promising anticancer activity in cell lines of solid tumours and leukaemia. Here we give an overview of POH1 function in the cell, of its potential role in oncogenesis and of recent progress in developing POH1-targeting drugs.","doi":"10.1038/s41416-022-01829-z","authors":"Spataro V, Buetti-Dinh A","authors_abbrev":"Spataro V et al.","pubmed_publication_date":"Sep 2022","pubmed_entrez_date":"2022-05-02","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-05-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF09637","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC5D6.05","HGNC:25944"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26545917","title":"Iron-Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of Mutational Robustness of a Highly Specific Protein-Protein Interaction.","citation":"Mol Biol Evol 2016 Mar;33(3):643-56","abstract":"Biogenesis of iron-sulfur clusters (FeS) is a highly conserved process involving Hsp70 and J-protein chaperones. However, Hsp70 specialization differs among species. In most eukaryotes, including Schizosaccharomyces pombe, FeS biogenesis involves interaction between the J-protein Jac1 and the multifunctional Hsp70 Ssc1. But, in Saccharomyces cerevisiae and closely related species, Jac1 interacts with the specialized Hsp70 Ssq1, which emerged through duplication of SSC1. As little is known about how gene duplicates affect the robustness of their protein interaction partners, we analyzed the functional and evolutionary consequences of Ssq1 specialization on the ubiquitous J-protein cochaperone Jac1, by comparing S. cerevisiae and S. pombe. Although deletion of JAC1 is lethal in both species, alanine substitutions within the conserved His-Pro-Asp (HPD) motif, which is critical for Jac1:Hsp70 interaction, have species-specific effects. They are lethal in S. pombe, but not in S. cerevisiae. These in vivo differences correlated with in vitro biochemical measurements. Charged residues present in the J-domain of S. cerevisiae Jac1, but absent in S. pombe Jac1, are important for tolerance of S. cerevisiae Jac1 to HPD alterations. Moreover, Jac1 orthologs from species that encode Ssq1 have a higher sequence divergence. The simplest interpretation of our results is that Ssq1's coevolution with Jac1 resulted in expansion of their binding interface, thus increasing the efficiency of their interaction. Such an expansion could in turn compensate for negative effects of HPD substitutions. Thus, our results support the idea that the robustness of Jac1 emerged as consequence of its highly efficient and specific interaction with Ssq1.","doi":"10.1093/molbev/msv254","authors":"Delewski W, Paterkiewicz B, Manicki M, Schilke B, Tomiczek B, Ciesielski SJ, Nierzwicki L, Czub J, Dutkiewicz R, Craig EA, Marszalek J","authors_abbrev":"Delewski W et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2015-11-08","publication_year":"2016","canto_session_key":"8a6340471870ad39","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-09 18:39:30","canto_approved_date":"2026-01-12 18:54:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-19 08:28:59","canto_added_date":"2015-11-09 01:19:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.11","SPAC227.13c","SPAC144.08"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-03-09"},{"uniquename":"PMID:14765109","title":"Fission yeast Clp1p phosphatase affects G2/M transition and mitotic exit through Cdc25p inactivation.","citation":"EMBO J 2004 Feb 25;23(4):919-29","abstract":"The Cdc14 family of phosphatases specifically reverses proline-directed phosphorylation events. In Saccharomyces cerevisiae, Cdc14p promotes Cdk1p inactivation at mitotic exit by reversing Cdk1p-dependent phosphorylations. Cdk1p is a proline-directed kinase whose activity is required in all eukaryotes for the transit into mitosis. At mitotic commitment, Cdk1p participates in its own regulation by activating the mitotic inducing phosphatase, Cdc25p, and inhibiting the opposing kinase, Wee1p. We have investigated the ability of Schizosaccharomyces pombe Clp1p, a Cdc14p homolog, to disrupt this auto-amplification loop. We show here that Clp1p is required to dephosphorylate, destabilize, and inactivate Cdc25p at the end of mitosis. Clp1p promotes recognition of Cdc25p by the anaphase-promoting complex/cyclosome, an E3 ubiquitin ligase. Failure to inactivate and destabilize Cdc25p in late mitosis delays progression through anaphase, interferes with septation initiation network signaling, and additionally advances the commitment to mitotic entry in the next cycle. This may be a widely conserved mechanism whereby Cdc14 proteins contribute to Cdk1p inactivation.","authors":"Wolfe BA, Gould KL","authors_abbrev":"Wolfe BA et al.","pubmed_publication_date":"25 Feb 2004","pubmed_entrez_date":"2004-02-07","publication_year":"2004","canto_session_key":"dcc617998c81695a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC1782.09c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:23848460","title":"Cell length growth in fission yeast: an analysis of its bilinear character and the nature of its rate change transition.","citation":"FEMS Yeast Res 2013 Nov;13(7):635-49","abstract":"During their mitotic cycle, cylindrical fission yeast cells grow exclusively at their tips. Length growth starts at birth and halts at mitotic onset when the cells begin to prepare for division. While the growth pattern was initially considered to be exponential, during the last three decades an increasing amount of evidence indicated that it is rather a bilinear function [two linear segments separated by a rate change point (RCP)]. The main focus of this work was to clarify this and to elucidate the further question of whether the rate change occurs abruptly at the RCP or more smoothly during a transition period around it. We have analyzed the individual growth patterns obtained by time-lapse microscopy of 60 wild-type cells separately as well as that of the 'average' cell generated from their superposition. Linear, exponential, and bilinear functions were fitted to the data, and their suitability was compared using objective model selection criteria. This analysis found the overwhelming majority of the cells (70%) to have a bilinear growth pattern with close to half of them showing a smooth and not an abrupt transition. The growth pattern of the average cell was also found to be bilinear with a smooth transition.","doi":"10.1111/1567-1364.12064","authors":"Horváth A, Rácz-Mónus A, Buchwald P, Sveiczer Á","authors_abbrev":"Horváth A et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-07-16","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9501991","title":"Identification of open reading frames in Schizosaccharomyces pombe cDNAs.","citation":"DNA Res 1997 Dec 31;4(6):363-9","abstract":"A total of 214 non-overlapping cDNA clones from Schizosaccharomyces pombe were selected and completely sequenced. The clones not previously reported were divided into the following three groups: 1) homologous to Saccharomyces cerevisiae genes (139 clones); 2) homologous to genes from other organisms but not to those from Sac. cerevisiae (4 clones); and 3) no similar sequences (40 clones). Among the 31 sequences identical to those in the public databases, 4 genes have regions corresponding to introns. Protein sequences which had homologs both in budding yeast and mammals were compared with those from Sac. cerevisiae and mammals. The search revealed that the evolutionary distances among these species are similar at least with genes of this category.","authors":"Yoshioka S, Kato K, Nakai K, Okayama H, Nojima H","authors_abbrev":"Yoshioka S et al.","pubmed_publication_date":"31 Dec 1997","pubmed_entrez_date":"1998-03-21","publication_year":"1997","canto_session_key":"9a46e67b29b18794","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 15:13:29","canto_approved_date":"2019-01-07 15:13:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 15:13:15","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:10826891","title":"Sequential NMR assignment of the RAS-binding domain of Byr2.","citation":"J Biomol NMR 2000 Apr;16(4):355-6","abstract":"","authors":"Huber F, Gronwald W, Wohlgemuth S, Herrmann C, Geyer M, Wittinghofer A, Kalbitzer HR","authors_abbrev":"Huber F et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-05-29","publication_year":"2000","canto_session_key":"b753a5d2b7cb02b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-07 14:42:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-07 14:41:58","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1D7.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-08-07"},{"uniquename":"PMID:25653167","title":"Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine acetyltransferases that modify tRNAs assisted by the adaptor Tan1/THUMPD1.","citation":"Nucleic Acids Res 2015 Feb 27;43(4):2242-58","abstract":"The function of RNA is subtly modulated by post-transcriptional modifications. Here, we report an important crosstalk in the covalent modification of two classes of RNAs. We demonstrate that yeast Kre33 and human NAT10 are RNA cytosine acetyltransferases with, surprisingly, specificity toward both 18S rRNA and tRNAs. tRNA acetylation requires the intervention of a specific and conserved adaptor: yeast Tan1/human THUMPD1. In budding and fission yeasts, and in human cells, we found two acetylated cytosines on 18S rRNA, one in helix 34 important for translation accuracy and another in helix 45 near the decoding site. Efficient 18S rRNA acetylation in helix 45 involves, in human cells, the vertebrate-specific box C/D snoRNA U13, which, we suggest, exposes the substrate cytosine to modification through Watson-Crick base pairing with 18S rRNA precursors during small subunit biogenesis. Finally, while Kre33 and NAT10 are essential for pre-rRNA processing reactions leading to 18S rRNA synthesis, we demonstrate that rRNA acetylation is dispensable to yeast cells growth. The inactivation of NAT10 was suggested to suppress nuclear morphological defects observed in laminopathic patient cells through loss of microtubules modification and cytoskeleton reorganization. We rather propose the effects of NAT10 on laminopathic cells are due to reduced ribosome biogenesis or function.","doi":"10.1093/nar/gkv075","authors":"Sharma S, Langhendries JL, Watzinger P, Kötter P, Entian KD, Lafontaine DL","authors_abbrev":"Sharma S et al.","pubmed_publication_date":"27 Feb 2015","pubmed_entrez_date":"2015-02-06","publication_year":"2015","canto_session_key":"f52c0e93f74517d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2025-03-28 22:51:22","canto_approved_date":"2025-03-28 22:51:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-03-28 22:49:21","canto_added_date":"2015-10-28 17:37:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC25H2.10c","SPAC20G8.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2025-03-28"},{"uniquename":"PMID:8314772","title":"Comparative structural analysis of nuclear RNase P RNAs from yeast.","citation":"J Biol Chem 1993 Jul 05;268(19):14045-55","abstract":"Secondary structure models for yeast nuclear RNase P RNAs were derived by phylogenetic comparative analysis. RNase P RNA genes from six Saccharomyces species were characterized and compared with the published gene sequences of Saccharomyces cerevisiae (RPR1), Schizosaccharomyces pombe, and Schizosaccharomyces octosporus. The general organization of the Saccharomyces genes were similar: all were present in single copy and contained RNA polymerase III-specific regulatory elements, including tRNA gene-like A- and B-box promoters located within 5' leader regions and poly(T) terminators following the mature RNA domain. As observed previously, two RNase P RNAs were present in each of the species: a shorter RNA corresponding to the mature domain and a longer possible precursor RNA that includes the 5' leader sequences. The mature RNA domains of three of these genes were sufficiently divergent from the S. cerevisiae RNA such that compensatory base changes in paired elements were readily identified, yet homologous regions could be aligned. A striking common core of primary and secondary structure emerged for the Saccharomyces RNase P RNAs. Furthermore, the Schizosaccharomyces homologs conformed in large part to the Saccharomyces conserved core and shared with it a distinctive structural domain that has so far only been observed in the yeast nuclear RNase P RNAs. Comparison of the yeast core to a previously published eubacterial conserved core and to the RNA homologs from vertebrates revealed a number of similarities, suggesting that RNase P RNA from diverse sources may share a core of structurally conserved elements.","authors":"Tranguch AJ, Engelke DR","authors_abbrev":"Tranguch AJ et al.","pubmed_publication_date":"05 Jul 1993","pubmed_entrez_date":"1993-07-05","publication_year":"1993","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17101775","title":"Individual subunits of the Ssn6-Tup11/12 corepressor are selectively required for repression of different target genes.","citation":"Mol Cell Biol 2007 Feb;27(3):1069-82","abstract":"The Saccharomyces cerevisiae Ssn6 and Tup1 proteins form a corepressor complex that is recruited to target genes by DNA-bound repressor proteins. Repression occurs via several mechanisms, including interaction with hypoacetylated N termini of histones, recruitment of histone deacetylases (HDACs), and interactions with the RNA polymerase II holoenzyme. The distantly related fission yeast, Schizosaccharomyces pombe, has two partially redundant Tup1-like proteins that are dispensable during normal growth. In contrast, we show that Ssn6 is an essential protein in S. pombe, suggesting a function that is independent of Tup11 and Tup12. Consistently, the group of genes that requires Ssn6 for their regulation overlaps but is distinct from the group of genes that depend on Tup11 or Tup12. Global chip-on-chip analysis shows that Ssn6 is almost invariably found in the same genomic locations as Tup11 and/or Tup12. All three corepressor subunits are generally bound to genes that are selectively regulated by Ssn6 or Tup11/12, and thus, the subunit specificity is probably manifested in the context of a corepressor complex containing all three subunits. The corepressor binds to both the intergenic and coding regions of genes, but differential localization of the corepressor within genes does not appear to account for the selective dependence of target genes on the Ssn6 or Tup11/12 subunits. Ssn6, Tup11, and Tup12 are preferentially found at genomic locations at which histones are deacetylated, primarily by the Clr6 class I HDAC. Clr6 is also important for the repression of corepressor target genes. Interestingly, a subset of corepressor target genes, including direct target genes affected by Ssn6 overexpression, is associated with the function of class II (Clr3) and III (Hst4 and Sir2) HDACs.","authors":"Fagerström-Billai F, Durand-Dubief M, Ekwall K, Wright AP","authors_abbrev":"Fagerström-Billai F et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2006-11-15","publication_year":"2007","canto_session_key":"f21f12cb20a578a4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-12-03 17:26:44","canto_approved_date":"2022-10-04 08:43:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-24 15:38:49","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.10","SPBC23E6.09","SPAC630.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-12-03"},{"uniquename":"PMID:38971312","title":"TORC2 is required for accumulation of γH2A in response to DNA damage.","citation":"J Biol Chem 2024 Jul 04;:107531","abstract":"TOR protein kinases serve as the catalytic subunit of the TORC1 and TORC2 complexes, which regulate cellular growth, proliferation and survival. In the fission yeast, Schizosaccharomyces pombe, cells lacking TORC2 or its downstream kinase Gad8 (AKT or SGK1 in human cells) exhibit sensitivity to a wide range of stress conditions, including DNA damage stress. One of the first responses to DNA damage is the phosphorylation of C-terminal serine residues within histone H2AX in human cells (γH2AX), or histone H2A in yeast cells (γH2A). The kinases responsible for γH2A in S. pombe are the two DNA damage checkpoint kinases Rad3 and Tel1 (ATR and ATM, respectively, in human cells). Here we report that TORC2-Gad8 signaling is required for accumulation of γH2A in response to DNA damage and during quiescence. Using the TOR specific inhibitor, Torin1, we demonstrate that the effect of TORC2 on γH2A in response to DNA damage is immediate, rather than adaptive. The lack of γH2A is restored by deletion mutations of transcription and chromatin modification factors, including loss of components of Paf1C, SAGA, Mediator and the bromo-domain proteins Bdf1/Bdf2. Thus, we suggest that TORC2-Gad8 may affect the accumulation of γH2A by regulating chromatin structure and function.","doi":"10.1016/j.jbc.2024.107531","authors":"Cohen A, Lubenski L, Mouzon A, Kupiec M, Weisman R","authors_abbrev":"Cohen A et al.","pubmed_publication_date":"04 Jul 2024","pubmed_entrez_date":"2024-07-06","publication_year":"2024","canto_session_key":"6ffc63e387ccfe13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ronit Weisman","canto_first_approved_date":"2025-07-03 07:55:58","canto_approved_date":"2025-07-03 07:55:59","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-02-13 12:43:01","canto_added_date":"2024-07-07 23:25:04","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":47,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Ronit Weisman","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.02c","SPCC4G3.08","SPCC622.08c","SPAC19G12.06c","SPBC30D10.10c","SPAC2F7.04","SPBC216.07c","SPAPYUG7.02c","SPBC12C2.02c","SPBC216.05","SPAC631.02","SPAC1851.04c","SPCC23B6.03c","SPAC1952.05","SPBC16H5.07c","SPAC664.03","SPAC4C5.02c","SPAC589.02c","SPCC24B10.07","SPBC23E6.08","SPBC13E7.08c","SPAC13A11.04c","SPCC1450.02"],"gene_count":23,"ltp_gene_count":23,"approved_date":"2025-07-03"},{"uniquename":"EMBL:AJ632002","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.37"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17614284","title":"The chromatin-remodeling factor FACT contributes to centromeric heterochromatin independently of RNAi.","citation":"Curr Biol 2007 Jul 17;17(14):1219-24","abstract":"Centromeres exert vital cellular functions in mitosis and meiosis. A specialized histone and other chromatin-bound factors nucleate a dynamic protein assembly that is required for the proper segregation of sister chromatids. In several organisms, including the fission yeast, Schizosaccharomyces pombe, the RNAi pathway contributes to the formation of silent chromatin in pericentromeric regions. Little is known about how chromatin-remodeling factors contribute to heterochromatic integrity and centromere function. Here we show that the histone chaperone and remodeling complex FACT is required for centromeric-heterochromatin integrity and accurate chromosome segregation. We show that Spt16 and Pob3 are two subunits of the S. pombe FACT complex. Surprisingly, yeast strains deleted for pob3+ are viable and alleviate gene silencing at centromeric repeats and at the silent mating-type locus. Importantly, like heterochromatin and RNAi pathway mutants, Pob3 null strains exhibit lagging chromosomes on anaphase spindles. Whereas the processing of centromeric RNA transcripts into siRNAs is maintained in Pob3 mutants, Swi6-association with the centromere is reduced. Our studies provide the first experimental evidence for a role of the RNA polymerase II cofactor FACT in heterochromatin integrity and in centromere function.","authors":"Lejeune E, Bortfeld M, White SA, Pidoux AL, Ekwall K, Allshire RC, Ladurner AG","authors_abbrev":"Lejeune E et al.","pubmed_publication_date":"17 Jul 2007","pubmed_entrez_date":"2007-07-07","publication_year":"2007","canto_session_key":"8a3c8a8742417b66","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-05 09:10:40","canto_approved_date":"2024-07-05 09:10:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-06-28 12:32:08","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":78,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC965.07c","SPAC19G12.09","SPAC1B3.16c","SPAPB1A11.03","SPAC17C9.02c","SPAP8A3.04c","SPAC8E11.10","SPAC1F7.07c","SPCC965.14c","SPBC3B9.10","SPAC1002.19","SPBC365.20c","SPAC9E9.04","SPAC664.01c","SPAC19B12.09","SPAC212.11","SPBC146.08c","SPBC1683.09c","SPAC144.14","SPAC926.05c","SPAC29B12.04","SPBC1709.06","SPAC22F8.05","SPCC338.12","SPAC1F8.03c","SPBP22H7.08","SPAC9E9.03","SPAC5D6.05","SPAC11H11.05c","SPBC1921.06c","SPBC557.03c","SPAC750.07c","SPAC644.05c","SPAC12B10.10","SPAC1834.10c","SPBC609.05","SPCC622.19","SPAC212.08c","SPCC1739.08c","SPAC694.03","SPAC212.06c","SPBP23A10.03c","SPBP8B7.19","SPAC1002.17c","SPBC3E7.02c","SPMIT.01","SPBPJ4664.02","SPBPB2B2.01","SPAC22F8.08","SPAC1F7.08","SPAC20H4.03c","SPBC27B12.03c","SPAC6F6.08c","SPAC22F8.12c","SPAC29A4.06c","SPAC637.10c","SPAC1782.01"],"gene_count":57,"ltp_gene_count":3,"approved_date":"2024-07-05"},{"uniquename":"PMID:32084401","title":"The Hydrophobic Patch Directs Cyclin B to Centrosomes to Promote Global CDK Phosphorylation at Mitosis.","citation":"Curr Biol 2020 Mar 09;30(5):883-892.e4","abstract":"The cyclin-dependent kinases (CDKs) are the major cell-cycle regulators that phosphorylate hundreds of substrates, controlling the onset of S phase and M phase [1-3]. However, the patterns of substrate phosphorylation increase are not uniform, as different substrates become phosphorylated at different times as cells proceed through the cell cycle [4, 5]. In fission yeast, the correct ordering of CDK substrate phosphorylation can be established by the activity of a single mitotic cyclin-CDK complex [6, 7]. Here, we investigate the substrate-docking region, the hydrophobic patch, on the fission yeast mitotic cyclin Cdc13 as a potential mechanism to correctly order CDK substrate phosphorylation. We show that the hydrophobic patch targets Cdc13 to the yeast centrosome equivalent, the spindle pole body (SPB), and disruption of this motif prevents both centrosomal localization of Cdc13 and the onset of mitosis but does not prevent S phase. CDK phosphorylation in mitosis is compromised for approximately half of all mitotic CDK substrates, with substrates affected generally being those that require the highest levels of CDK activity to become phosphorylated and those that are located at the SPB. Our experiments suggest that the hydrophobic patch of mitotic cyclins contributes to CDK substrate selection by directing the localization of Cdc13-CDK to centrosomes and that this localization of CDK contributes to the CDK substrate phosphorylation necessary to ensure proper entry into mitosis. Finally, we show that mutation of the hydrophobic patch prevents cyclin B1 localization to centrosomes in human cells, suggesting that this mechanism of cyclin-CDK spatial regulation may be conserved across eukaryotes.","doi":"10.1016/j.cub.2019.12.053","authors":"Basu S, Roberts EL, Jones AW, Swaffer MP, Snijders AP, Nurse P","authors_abbrev":"Basu S et al.","pubmed_publication_date":"09 Mar 2020","pubmed_entrez_date":"2020-02-22","publication_year":"2020","canto_session_key":"e7cc68a1da978b38","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-02-24 16:59:16","canto_approved_date":"2025-09-03 11:39:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-17 12:20:47","canto_added_date":"2020-02-23 01:15:06","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":18,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC23C11.16","SPCC18B5.03","SPCC4E9.02","SPBC649.05","SPBC32F12.09","SPBC582.03","SPAPB2B4.03"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2021-02-24"},{"uniquename":"PMID:10371213","title":"Identification of cold-sensitive mutations in the Schizosaccharomyces pombe actin locus.","citation":"FEBS Lett 1999 May 28;451(3):321-6","abstract":"In recent years, the actin cytoskeleton in Schizosaccharomyces pombe has become the subject of intense scrutiny. However, to date, only a single actin mutation has been identified. Described here is the isolation and characterization of four new cold-sensitive actin mutations. Sequence analysis of the mutant actin genes indicated that each of these mutations caused alterations in single amino acids that are conserved in all actin sequences. These mutants differ in their phenotypes. One of these mutations (act1-48) was identified as an extragenic suppressor of a mutation in the cdc4 gene, which is required for actin ring formation and cytokinesis. Interestingly, when act1-48 mutant cells were shifted to the restrictive temperature, actin patches were not detected but the actin ring formation and stability was unaffected. The three other mutations, act1-16, act1-32 and act1-67, primarily affected the actin ring formation or stability while F-actin patches did not seem to be substantially different in appearance. Given that the ultrastructural architectures of F-actin patches and the F-actin ring are presently unclear, these mutations, which affect one structure or the other, should be useful for future studies on the role of actin itself in the function of these F-actin-containing structures in S. pombe.","authors":"McCollum D, Balasubramanian M, Gould K","authors_abbrev":"McCollum D et al.","pubmed_publication_date":"28 May 1999","pubmed_entrez_date":"1999-06-17","publication_year":"1999","canto_session_key":"5978a5dd32a32816","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Car,e","canto_first_approved_date":"2026-06-17 11:05:54","canto_approved_date":"2026-06-17 11:05:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-06-17 11:05:49","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Pascal Car,e","community_curator":false,"annotation_count":22,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPAP8A3.08","SPAC1F5.04c","SPBC32H8.12c","SPAC4A8.15c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2026-06-17"},{"uniquename":"PMID:21515633","title":"Gcn5 facilitates Pol II progression, rather than recruitment to nucleosome-depleted stress promoters, in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2011 Aug;39(15):6369-79","abstract":"In the fission yeast, the MAP kinase Sty1 and the transcription factor Atf1 regulate up to 400 genes in response to environmental signals, and both proteins have been shown to bind to their promoters in a stress-dependent manner. In a genetic search, we have isolated the histone H3 acetyltransferase Gcn5, a component of the SAGA complex, as being essential for oxidative stress survival and activation of those genes. Upon stress, Gcn5 is recruited to promoters and coding sequences of stress genes in a Sty1- and Atf1-dependent manner, causing both an enhanced acetylation of histone H3 and nucleosome eviction. Unexpectedly, recruitment of RNA polymerase II (Pol II) is not impaired in Δgcn5 cells. We show here that stress genes display a 400-bp long nucleosome depleted region upstream of the transcription start site even prior to activation. Stress treatment does not alter promoter nucleosome architecture, but induces eviction of the downstream nucleosomes at stress genes, which is not observed in Δgcn5 cells. We conclude that, while Pol II is recruited to nucleosome-free stress promoters in a transcription factor dependent manner, Gcn5 mediates eviction of nucleosomes positioned downstream of promoters, allowing efficient Pol II progression along the genes.","doi":"10.1093/nar/gkr255","authors":"Sansó M, Vargas-Pérez I, Quintales L, Antequera F, Ayté J, Hidalgo E","authors_abbrev":"Sansó M et al.","pubmed_publication_date":"Aug 2011","pubmed_entrez_date":"2011-04-26","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28525753","title":"The U6 snRNA m 6 A Methyltransferase METTL16 Regulates SAM Synthetase Intron Retention.","citation":"Cell 2017 May 18;169(5):824-835.e14","abstract":"Maintenance of proper levels of the methyl donor S-adenosylmethionine (SAM) is critical for a wide variety of biological processes. We demonstrate that the N 6 -adenosine methyltransferase METTL16 regulates expression of human MAT2A, which encodes the SAM synthetase expressed in most cells. Upon SAM depletion by methionine starvation, cells induce MAT2A expression by enhanced splicing of a retained intron. Induction requires METTL16 and its methylation substrate, a vertebrate conserved hairpin (hp1) in the MAT2A 3' UTR. Increasing METTL16 occupancy on the MAT2A 3' UTR is sufficient to induce efficient splicing. We propose that, under SAM-limiting conditions, METTL16 occupancy on hp1 increases due to inefficient enzymatic turnover, which promotes MAT2A splicing. We further show that METTL16 is the long-unknown methyltransferase for the U6 spliceosomal small nuclear RNA (snRNA). These observations suggest that the conserved U6 snRNA methyltransferase evolved an additional function in vertebrates to regulate SAM homeostasis.","doi":"10.1016/j.cell.2017.05.003","authors":"Pendleton KE, Chen B, Liu K, Hunter OV, Xie Y, Tu BP, Conrad NK","authors_abbrev":"Pendleton KE et al.","pubmed_publication_date":"18 May 2017","pubmed_entrez_date":"2017-05-20","publication_year":"2017","canto_session_key":"2210816ed12987ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-01-22 16:50:11","canto_approved_date":"2018-01-22 16:50:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-22 12:45:30","canto_added_date":"2017-06-07 07:30:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.06","SPAC27D7.08c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-01-22"},{"uniquename":"PMID:9233811","title":"Cell differentiation by interaction of two HMG-box proteins: Mat1-Mc activates M cell-specific genes in S.pombe by recruiting the ubiquitous transcription factor Ste11 to weak binding sites.","citation":"EMBO J 1997 Jul 01;16(13):4021-33","abstract":"The Schizosaccharomyces pombe mfm1 gene is expressed in an M cell-specific fashion. This regulation requires two HMG-box proteins: the ubiquitous Ste11 transcription factor and the M cell-controlling protein Mat1-Mc. Here we report that the mfm1 promoter contains a single, weak Stell-binding site (a so-called TR-box) that can confer M-specificity on a heterologous promoter when present in eight copies. In vitro, both Mat1-Mc and Ste11 can bind this box with approximately the same affinity. The Mat1-Mc protein caused a dramatic increase in the DNA-binding of Ste11 to this box, under conditions where we could not detect Mat1-Mc in the resulting protein-DNA complex. When we changed a single base in the mfm1 TR-box, such that it resembled those boxes found in ubiquitously expressed genes, Ste11 binding was enhanced, and in vivo the mfm1 gene also became expressed in P cells where Mat1-Mc is absent. These findings suggest that M-specificity results from Mat1-Mc-mediated Ste11 binding to weak TR-boxes. We have also defined a novel motif (termed M-box), adjacent to the mfm1 TR-box, to which Mat1-Mc binds strongly. A DNA fragment containing both the TR- and the M-box allowed the formation of a complex containing both Ste11 and Mat1-Mc. A single copy of this fragment was sufficient to activate a heterologous promoter in an M-specific fashion, suggesting that these two boxes act in a synergistic manner.","authors":"Kjaerulff S, Dooijes D, Clevers H, Nielsen O","authors_abbrev":"Kjaerulff S et al.","pubmed_publication_date":"01 Jul 1997","pubmed_entrez_date":"1997-07-01","publication_year":"1997","canto_session_key":"7f00e434e3b98736","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-09 14:39:24","canto_approved_date":"2026-04-11 20:09:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-09 14:39:17","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.09","SPBC32C12.02","SPBC23G7.17c","SPAPB8E5.05"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-12-09"},{"uniquename":"PMID:24741065","title":"S. pombe TORC1 activates the ubiquitin-proteasomal degradation of the meiotic regulator Mei2 in cooperation with Pat1 kinase.","citation":"J Cell Sci 2014 Jun 15;127(Pt 12):2639-46","abstract":"Target of rapamycin (TOR) kinase regulates cell metabolism and growth, acting as a subunit of two multi-protein complexes, TORC1 and TORC2. Known TORC substrates are either kinases or general factors involved in growth control. Here, we show that fission yeast TORC1, which promotes vegetative growth and suppresses sexual development, can phosphorylate Mei2 (a specific factor involved in switching the cell fate) in vitro. Alanine substitutions at the nine Mei2 phosphorylation sites stabilize the protein and promote mating and meiosis in vivo. We found that Mei2 is polyubiquitylated in vivo in a TORC1-dependent manner. Based on these data, we propose that TORC1 contributes to the suppression of sexual development by phosphorylating Mei2, in addition to controlling the cellular metabolic status.","doi":"10.1242/jcs.135517","authors":"Otsubo Y, Yamashita A, Ohno H, Yamamoto M","authors_abbrev":"Otsubo Y et al.","pubmed_publication_date":"15 Jun 2014","pubmed_entrez_date":"2014-04-18","publication_year":"2014","canto_session_key":"b732a3ac22de7b6e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-12 08:30:36","canto_approved_date":"2025-09-04 12:16:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-13 16:03:02","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.07c","SPAC27D7.03c","SPBC4.07c","SPAC57A7.11","SPBC337.08c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-06-12"},{"uniquename":"PMID:42067045","title":"Optimized protocol for high-efficiency mitochondrial RNA isolation from fission yeast in log phase and stationary phase.","citation":"J Microbiol Methods 2026 Apr 29;:107523","abstract":"The fission yeast Schizosaccharomyces pombe (S. pombe) serves as an important model organism for investigating mitochondrial function and gene regulation. However, obtaining sufficient quantity and high-quality mitochondrial RNA (mtRNA) for techniques like Northern blot analysis remains challenging, particularly from stationary-phase cells with rigid cell walls. We developed an improved extraction method by comparing conventional hot-phenol and commercial column-based approaches with modified Enzymatic-Phenol/Chloroform (EPC) protocol, which replaces harsh thermal/liquid nitrogen steps with gentle enzymatic lysis. Additionally, for hard-to-lyse stationary-phase cells, we introduced a specialized OM Buffer to enhance efficiency. The refined EPC protocol achieved substantially higher mtRNA yields without compromising RNA purity. Northern blot analysis confirmed successful isolation of mtRNAs, revealing strong, well-defined signals for mtRNA. This protocol provides a reliable tool for advanced mitochondrial research in S. pombe and other eukaryotes.","doi":"10.1016/j.mimet.2026.107523","authors":"Lu Y, Wang G, Shang J","authors_abbrev":"Lu Y et al.","pubmed_publication_date":"29 Apr 2026","pubmed_entrez_date":"2026-05-01","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-05-02 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35796993","title":"Thermofluor-Based Analysis of Protein Integrity and Ligand Interactions.","citation":"Methods Mol Biol 2022;2533:247-257","abstract":"Thermofluor is a fluorescence-based thermal shift assay, which measures temperature-induced protein unfolding and thereby yields valuable information about the integrity of a purified recombinant protein. Analysis of ligand binding to a protein is another popular application of this assay. Thermofluor requires neither protein labeling nor highly specialized equipment, and can be performed in a regular real-time PCR instrument. Thus, for a typical molecular biology laboratory, Thermofluor is a convenient method for the routine assessment of protein quality. Here, we provide Thermofluor protocols using the example of Cdc123. This ATP-grasp protein is an essential assembly chaperone of the eukaryotic translation initiation factor eIF2. We also report on a destabilized mutant protein version and on the ATP-mediated thermal stabilization of wild-type Cdc123 illustrating protein integrity assessment and ligand binding analysis as two major applications of the Thermofluor assay.","doi":"10.1007/978-1-0716-2501-9_15","authors":"Pinz S, Doskocil E, Seufert W","authors_abbrev":"Pinz S et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-07-07","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP27G11.03","SPBC17G9.09"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:26443059","title":"Sgf73, a subunit of SAGA complex, is required for the assembly of RITS complex in fission yeast.","citation":"Sci Rep 2015 Oct 07;5:14707","abstract":"RNA interference (RNAi) is a widespread gene-silencing mechanism and is required for heterochromatin assembly in a variety of organisms. The RNA-induced transcriptional silencing complex (RITS), composed of Ago1, Tas3 and Chp1, is a key component of RNAi machinery in fission yeast that connects short interference RNA (siRNA) and heterochromatin formation. However, the process by which RITS is assembled is not well understood. Here, we identified Sgf73, a subunit of the SAGA co-transcriptional complex, is required for pericentromeric heterochromatin silencing and the generation of siRNA. This novel role of Sgf73 is independent of enzymatic activities or structural integrity of SAGA. Instead, Sgf73 is physically associated with Ago1 and Chp1. The interactions among the subunits of the RITS, including those between Tas3 and Chp1, between Chp1 and Ago1, between Ago1 and Tas3, were all impaired by the deletion of sgf73(+). Consistently, the recruitment of Ago1 and Chp1 to the pericentromeric region was abolished in sgf73Δ cells. Our study unveils a moonlighting function of a SAGA subunit. It suggests Sgf73 is a novel factor that promotes assembly of RITS and RNAi-mediated heterochromatin formation.","doi":"10.1038/srep14707","authors":"Deng X, Zhou H, Zhang G, Wang W, Mao L, Zhou X, Yu Y, Lu H","authors_abbrev":"Deng X et al.","pubmed_publication_date":"07 Oct 2015","pubmed_entrez_date":"2015-10-08","publication_year":"2015","canto_session_key":"563bfc6f26ecd62e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-04-25 12:00:45","canto_approved_date":"2024-01-16 10:05:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-16 14:29:13","canto_added_date":"2015-10-09 00:18:52","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":57,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPAC140.03","SPBP8B7.28c","SPBC16C6.10","SPAC21E11.03c","SPAC1952.05","SPBC83.03c","SPAC18G6.02c","SPCC11E10.08","SPBC428.08c","SPCC663.12","SPAC13A11.04c","SPCC736.11","SPBC2D10.17","SPCC1739.03","SPAC6F12.09","SPBC28F2.12","SPCC188.13c","SPBC6B1.12c","SPBC582.04c","SPCC126.04c","SPBC800.03","SPAC13G7.07","SPCC613.12c","SPAC57A10.14","SPBC25H2.11c","SPBC1921.07c"],"gene_count":27,"ltp_gene_count":13,"approved_date":"2018-04-25"},{"uniquename":"PMID:2436053","title":"Need for DNA topoisomerase activity as a swivel for DNA replication for transcription of ribosomal RNA.","citation":"Nature 1987 Mar 26;326(6111):414-6","abstract":"Yeast strains with mutations in the genes for DNA topoisomerases I and II have been identified previously in both Saccharomyces cerevisiae and Schizosaccharomyces pombe. The topoisomerase II mutants (top2) are conditional-lethal temperature-sensitive (ts) mutants. They are defective in the termination of DNA replication and the segregation of daughter chromosomes, but otherwise appear to replicate and transcribe DNA normally. Topoisomerase I mutants (top1), including strains with null mutations are viable and exhibit no obvious growth defects, demonstrating that DNA topoisomerase I is not essential for viability in yeast. In contrast to the single mutants, top1 top2 ts double mutants from both Schizosaccharomyces pombe and Saccharomyces cerevisiae grow poorly at the permissive temperature and stop growth rapidly at the non-permissive temperature. Here we report that DNA and ribosomal RNA synthesis are drastically inhibited in an S. cerevisiae top1 top2 ts double mutant at the restrictive temperature, but that the rate of poly(A)+ RNA synthesis is reduced only about threefold and transfer DNA synthesis remains relatively normal. The results suggest that DNA replication and at least ribosomal RNA synthesis require an active topoisomerase, presumably to act as a swivel to relieve torsional stress, and that either topoisomerase can perform the required function (except in termination of DNA replication where topoisomerase II is required).","authors":"Brill SJ, DiNardo S, Voelkel-Meiman K, Sternglanz R","authors_abbrev":"Brill SJ et al.","pubmed_publication_date":"26 Mar 1987","pubmed_entrez_date":"1987-03-01","publication_year":"1987","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1A4.03c","SPBC1703.14c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:15277753","title":"Genetic analysis of chs1+ and chs2+ encoding chitin synthases from Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2004 Jul;68(7):1489-99","abstract":"To explore the function of chitin in Schizosaccharomyces pombe, we have cloned chs1+ and chs2+, encoding putative chitin synthases, based on sequences in the Sanger Centre database. The synthetic lethal phenotype of the S. cerevisiae chs1 chs2 chs3 mutant was complemented by expression of S. pombe chs1+ or chs1+, indicating that both chs1+ and chs2+ in fact encode chitin synthase. The homothallic Deltachs1 strain formed abnormal asci that contained 1, 2, or 3 spores, while the Deltachs2 strain had no noticeable phenotype. The chs1 chs2 double disruptant looked similar phenotypically to the Deltachs1 strain. The Chs2-GFP fusion protein predominantly localized at the septum after the septum was formed during vegetative growth. The level of chs2+ mRNA increased just before the septum was formed. Levels of Chs2-13Myc synthesis also changed during the cell cycle. Thus, chs1+ is required for proper spore formation, and chs2+ is perhaps involved in septum formation.","authors":"Matsuo Y, Tanaka K, Nakagawa T, Matsuda H, Kawamukai M","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-07-28","publication_year":"2004","canto_session_key":"bcadd142b293b43d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-20 20:48:23","canto_approved_date":"2025-10-03 16:56:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-20 20:48:15","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1709.01","SPAC13G6.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-10-20"},{"uniquename":"PMID:21949882","title":"Schizosaccharomyces pombe Ofd2 is a nuclear 2-oxoglutarate and iron dependent dioxygenase interacting with histones.","citation":"PLoS One 2011;6(9):e25188","abstract":"2-Oxoglutarate (2OG) dependent dioxygenases are ubiquitous iron containing enzymes that couple substrate oxidation to the conversion of 2OG to succinate and carbon dioxide. They participate in a wide range of biological processes including collagen biosynthesis, fatty acid metabolism, hypoxic sensing and demethylation of nucleic acids and histones. Although substantial progress has been made in elucidating their function, the role of many 2OG dioxygenases remains enigmatic. Here we have studied the 2OG and iron (Fe(II)) dependent dioxygenase Ofd2 in Schizosaccharomyces pombe, a member of the AlkB subfamily of dioxygenases. We show that decarboxylation of 2OG by recombinant Ofd2 is dependent on Fe(II) and a histidine residue predicted to be involved in Fe(II) coordination. The decarboxylase activity of Ofd2 is stimulated by histones, and H2A has the strongest effect. Ofd2 interacts with all four core histones, however, only very weakly with H4. Our results define a new subclass of AlkB proteins interacting with histones, which also might comprise some of the human AlkB homologs with unknown function.","doi":"10.1371/journal.pone.0025188","authors":"Korvald H, Mølstad Moe AM, Cederkvist FH, Thiede B, Laerdahl JK, Bjørås M, Alseth I","authors_abbrev":"Korvald H et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-09-28","publication_year":"2011","canto_session_key":"cb309c1fc155632b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-09-08 14:13:01","canto_approved_date":"2022-01-19 12:03:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-21 13:56:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-09-08"},{"uniquename":"PMID:36435910","title":"Fission yeast Dis1 is an unconventional TOG/XMAP215 that induces microtubule catastrophe to drive chromosome pulling.","citation":"Commun Biol 2022 Nov 26;5(1):1298","abstract":"The shortening of microtubules attached to kinetochores is the driving force of chromosome movement during cell division. Specific kinesins are believed to shorten microtubules but are dispensable for viability in yeast, implying the existence of additional factors responsible for microtubule shortening. Here, we demonstrate that Dis1, a TOG/XMAP215 ortholog in fission yeast, promotes microtubule shortening to carry chromosomes. Although TOG/XMAP215 orthologs are generally accepted as microtubule polymerases, Dis1 promoted microtubule catastrophe in vitro and in vivo. Notably, microtubule catastrophe was promoted when the tip was attached to kinetochores, as they steadily anchored Dis1 at the kinetochore-microtubule interface. Engineered Dis1 oligomers artificially tethered at a chromosome arm region induced the shortening of microtubules in contact, frequently pulling the chromosome arm towards spindle poles. This effect was not brought by oligomerised Alp14. Thus, unlike Alp14 and other TOG/XMAP215 orthologs, Dis1 plays an unconventional role in promoting microtubule catastrophe, thereby driving chromosome movement.","doi":"10.1038/s42003-022-04271-2","authors":"Murase Y, Yamagishi M, Okada N, Toya M, Yajima J, Hamada T, Sato M","authors_abbrev":"Murase Y et al.","pubmed_publication_date":"26 Nov 2022","pubmed_entrez_date":"2022-11-26","publication_year":"2022","canto_session_key":"dd3467c8fe93ae16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2023-05-23 15:32:40","canto_approved_date":"2025-09-04 12:18:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-10-23 19:50:08","canto_added_date":"2022-11-28 01:15:04","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":4,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Masamitsu Sato","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.03","SPCC736.14","SPAC27F1.04c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2023-05-23"},{"uniquename":"PMID:15302827","title":"The forkhead transcription factor Fkh2 regulates the cell division cycle of Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2004 Aug;3(4):944-54","abstract":"In eukaryotes the regulation of gene expression plays a key role in controlling cell cycle progression. Here, we demonstrate that a forkhead transcription factor, Fkh2, regulates the periodic expression of cdc15(+) and spo12(+) in the M and G(1) phases of the cell division cycle in the fission yeast Schizosaccharomyces pombe. We also show that Fkh2 is important for several cell cycle processes, including cell morphology and cell separation, nuclear structure and migration, and mitotic spindle function. We find that the expression of fkh2(+) is itself regulated in a cell cycle-dependent manner in G(1) coincident with the expression of cdc18(+), a Cdc10-regulated gene. However, fkh2(+) expression is independent of Cdc10 function. Fkh2 was found to be phosphorylated during the cell division cycle, with a timing that suggests that this posttranslational modification is important for cdc15(+) and spo12(+) expression. Related forkhead proteins regulate G(2) and M phase-specific gene expression in the evolutionarily distant Saccharomyces cerevisiae, suggesting that these proteins play conserved roles in regulating cell cycle processes in eukaryotes.","authors":"Bulmer R, Pic-Taylor A, Whitehall SK, Martin KA, Millar JB, Quinn J, Morgan BA","authors_abbrev":"Bulmer R et al.","pubmed_publication_date":"Aug 2004","pubmed_entrez_date":"2004-08-11","publication_year":"2004","canto_session_key":"11452248356b8b72","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-16 20:07:58","canto_approved_date":"2021-02-08 09:30:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-23 14:07:13","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4C3.12","SPAC20G8.05c","SPAC1142.08","SPAC24H6.05","SPBC14C8.07c","SPAC3F10.15c","SPBC336.12c","SPBC16G5.15c"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2016-02-16"},{"uniquename":"PMID:26092123","title":"Effects of FSGS-associated mutations on the stability and function of myosin-1 in fission yeast.","citation":"Dis Model Mech 2015 Aug 01;8(8):891-902","abstract":"Point mutations in the human MYO1E gene, encoding class I myosin Myo1e, are associated with focal segmental glomerulosclerosis (FSGS), a primary kidney disorder that leads to end-stage kidney disease. In this study, we used a simple model organism, fission yeast Schizosaccharomyces pombe, to test the effects of FSGS-associated mutations on myosin activity. Fission yeast has only one class I myosin, Myo1, which is involved in actin patch assembly at the sites of endocytosis. The amino acid residues mutated in individuals with FSGS are conserved between human Myo1e and yeast Myo1, which allowed us to introduce equivalent mutations into yeast myosin and use the resulting mutant strains for functional analysis. Yeast strains expressing mutant Myo1 exhibited defects in growth and endocytosis similar to those observed in the myo1 deletion strain. These mutations also disrupted Myo1 localization to endocytic actin patches and resulted in mis-localization of Myo1 to eisosomes, linear membrane microdomains found in yeast cells. Although both mutants examined in this study exhibited loss of function, one of these mutants was also characterized by the decreased protein stability. Thus, using the yeast model system, we were able to determine that the kidney-disease-associated mutations impair myosin functional activity and have differential effects on protein stability.","doi":"10.1242/dmm.020214","authors":"Bi J, Carroll RT, James ML, Ouderkirk JL, Krendel M, Sirotkin V","authors_abbrev":"Bi J et al.","pubmed_publication_date":"01 Aug 2015","pubmed_entrez_date":"2015-06-21","publication_year":"2015","canto_session_key":"705c77f569d699e8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-06-22 00:20:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21468206","title":"Transformation of Saccharomyces cerevisiae and other fungi: methods and possible underlying mechanism.","citation":"Bioeng Bugs 2010;1(6):395-403","abstract":"Transformation (i.e., genetic modification of a cell by the incorporation of exogenous DNA) is indispensable for manipulating fungi. Here, we review the transformation methods for Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida albicans, Pichia pastoris and Aspergillus species and discuss some common modifications to improve transformation efficiency. We also present a model of the mechanism underlying S. cerevisiae transformation, based on recent reports and the mechanism of transfection in mammalian systems. This model predicts that DNA attaches to the cell wall and enters the cell via endocytotic membrane invagination, although how DNA reaches the nucleus is unknown. Polyethylene glycol is indispensable for successful transformation of intact cells and the attachment of DNA and also possibly acts on the membrane to increase the transformation efficiency. Both lithium acetate and heat shock, which enhance the transformation efficiency of intact cells but not that of spheroplasts, probably help DNA to pass through the cell wall.","doi":"10.4161/bbug.1.6.13257","authors":"Kawai S, Hashimoto W, Murata K","authors_abbrev":"Kawai S et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2011-04-07","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38480568","title":"Effects of ScRgt1-Like DNA-binding transcription factor SpRgt1 (SPCC320.03) on Hexose transporters gene expression in Schizosaccharomyces pombe.","citation":"Arch Microbiol 2024 Mar 13;206(4):155","abstract":"Glucose, which plays an essential role in carbon and energy metabolism in eukaryotes, is vital in directing various energy-consuming cellular processes. In S. cerevisiae, transcription factors involved in regulating hexose transporters and their mechanisms of action under different carbon sources were revealed in detail. However, there is limited information on these processes in S. pombe. In this study, the effect of SPCC320.03 (named SpRgt1), the ortholog of ScRgt1 whose molecular mechanism is known in detail in S. cerevisiae, on the transcriptional regulation of hexose transporters (ght1-8) dependent on different carbon sources was investigated. We measured the transcript levels of ght1-8 using the qPCR technique and performed relative evaluation in S. pombe strains (parental, rgt1 deleted mutant, rgt1 overexpressed, and vectoral rgt1 carrying mutant). We aimed to investigate the transcriptional changes caused by the protein product of the rgt1 (SPCC320.03) gene in terms of ght1-8 genes in strains that are grown in different carbon sources (2% glucose, 2% glycerol + 0.1% glucose, and 2% gluconate). Here, we show that SpRgt1 is involved in the regulation of the ght3, ght4, ght6, and ght7 genes but that the ght1, ght2, ght5, and ght8 gene expression vary depending on carbon sources, independently of SpRgt1.","doi":"10.1007/s00203-024-03901-z","authors":"Ibisoglu MS, Tan M, Yilmazer M, Yilmaz S, Uzuner SK, Topal-Sarikaya A, Palabiyik B","authors_abbrev":"Ibisoglu MS et al.","pubmed_publication_date":"13 Mar 2024","pubmed_entrez_date":"2024-03-14","publication_year":"2024","canto_session_key":"94bb9444b545ee17","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-15 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC320.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32729986","title":"Newly identified genes contribute to vanillin tolerance in Saccharomyces cerevisiae.","citation":"Microb Biotechnol 2021 Mar;14(2):503-516","abstract":"Exploring the mechanisms of tolerance in microorganisms to vanillin, which is derived from lignin, will benefit the design of robust cell factories that produce biofuels and chemicals using lignocellulosic materials. Our objective was to identify the genes related to vanillin tolerance in Saccharomyces cerevisiae. We investigated the effects on vanillin tolerance of several genes that have site mutations in the highly vanillin-tolerant strain EMV-8 compared to its parental line NAN-27. The results showed that overexpression of GCY1, a gene that encodes an aldo-keto reductase that also has mRNA-binding activity, YPR1, a paralog of GCY1 that encodes an aldo-keto reductase, PEX5, a gene that encodes a peroxisomal membrane signal receptor and MBF1, a gene that encodes a multiprotein bridging factor increase the specific growth rates (μ) by 49%, 41%, 44% and 48 %, respectively, in medium containing 6 mmol l -1  vanillin. Among these gene products, Gcy1p and Ypr1p showed NADPH-dependent and NAD(P)H-dependent vanillin reductase activity, respectively. The reductase-inactive mutant Gcy1p Y56F  also increased vanillin tolerance in S. cerevisiae, suggesting that other mechanisms exist. Although TRS85 and PEX5, genes for which the mRNAs are binding targets of Gcy1p, were shown to be related to vanillin tolerance, both the mRNA and protein levels of these genes were not changed by overexpression of GCY1. The relationship between the mRNA-binding activity of Gcy1p and its positive effect on vanillin tolerance is still not clear. Finally, we found that the point mutation D112A in Mbf1p, which disrupts the binding of Mbf1p and the TATA element-binding protein (TBP), did not decrease the positive effect of Mbf1p on vanillin tolerance. This indicates that the binding of Mbf1p and TBP is not necessary for the positive effect on vanillin tolerance mediated by Mbf1p. We have successfully identified new genes related to vanillin tolerance and provided novel targets that can be used to improve the vanillin tolerance of S. cerevisiae. Moreover, we have extended our understanding of the proteins encoded by these genes.","doi":"10.1111/1751-7915.13643","authors":"Liang Z, Wang X, Bao X, Wei T, Hou J, Liu W, Shen Y","authors_abbrev":"Liang Z et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2020-07-31","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26F1.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20388511","title":"Avt5p is required for vacuolar uptake of amino acids in the fission yeast Schizosaccharomyces pombe.","citation":"FEBS Lett 2010 Jun 03;584(11):2339-45","abstract":"We identified SPBC1685.07c of Schizosaccharomyces pombe as a novel vacuolar protein, Avt5p, with similarity to vacuolar amino acid transporters Avt5p from Saccharomyces cerevisiae. Avt5p localizes to the vacuolar membrane and upon disruption of avt5, uptake of histidine, glutamate, tyrosine, arginine, lysine or serine was impaired. During nitrogen starvation, the transient increase of vacuolar lysine transport observed for wild-type cells still occurred in the mutant cells, however, uptake of glutamate did not significantly increase in response to nitrogen starvation. Our results show that under diverse growth conditions Avt5p is involved in vacuolar transport of a selective set of amino acids.","doi":"10.1016/j.febslet.2010.04.012","authors":"Chardwiriyapreecha S, Mukaiyama H, Sekito T, Iwaki T, Takegawa K, Kakinuma Y","authors_abbrev":"Chardwiriyapreecha S et al.","pubmed_publication_date":"03 Jun 2010","pubmed_entrez_date":"2010-04-15","publication_year":"2010","canto_session_key":"c49c381346278c08","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-08 15:01:03","canto_approved_date":"2025-03-25 06:30:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-08 16:07:26","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.07c","SPBC12C2.13c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-01-08"},{"uniquename":"PMID:31278118","title":"Cohesin Impedes Heterochromatin Assembly in Fission Yeast Cells Lacking Pds5.","citation":"Genetics 2019 Sep;213(1):127-141","abstract":"The fission yeast  Schizosaccharomyces pombe  is a powerful genetic model system for uncovering fundamental principles of heterochromatin assembly and epigenetic inheritance of chromatin states. Heterochromatin defined by histone H3 lysine 9 methylation and HP1 proteins coats large chromosomal domains at centromeres, telomeres, and the mating-type ( mat ) locus. Although genetic and biochemical studies have provided valuable insights into heterochromatin assembly, many key mechanistic details remain unclear. Here, we use a sensitized reporter system at the  mat  locus to screen for factors affecting heterochromatic silencing. In addition to known components of heterochromatin assembly pathways, our screen identified eight new factors including the cohesin-associated protein Pds5. We find that Pds5 enriched throughout heterochromatin domains is required for proper maintenance of heterochromatin. This function of Pds5 requires its associated Eso1 acetyltransferase, which is implicated in the acetylation of cohesin. Indeed, introducing an acetylation-mimicking mutation in a cohesin subunit suppresses defects in heterochromatin assembly in  pds5 ∆ and  eso1 ∆ cells. Our results show that in cells lacking Pds5, cohesin interferes with heterochromatin assembly. Supporting this, eliminating cohesin from the  mat  locus in the  pds5 ∆ mutant restores both heterochromatin assembly and gene silencing. These analyses highlight an unexpected requirement for Pds5 in ensuring proper coordination between cohesin and heterochromatin factors to effectively maintain gene silencing.","doi":"10.1534/genetics.119.302256","authors":"Folco HD, McCue A, Balachandran V, Grewal SIS","authors_abbrev":"Folco HD et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-07-07","publication_year":"2019","canto_session_key":"edfee9c20ff8ca78","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"H. Diego Folco","canto_first_approved_date":"2020-05-16 14:00:10","canto_approved_date":"2026-06-17 13:03:53","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-04-30 16:16:26","canto_added_date":"2019-07-08 00:15:04","annotation_curators":[{"name":"H. Diego Folco","community_curator":true,"annotation_count":43,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.07c","SPBC428.08c","SPBC16C6.10","SPBC428.17c","SPAC23C4.03","SPAC664.01c","SPAC17H9.20","SPBC31F10.13c","SPAC1B3.17","SPBC15D4.03","SPAC959.08","SPAC10F6.09c","SPBC2D10.17","SPCC663.04","SPCC11E10.08","SPBC800.03","SPBC609.05","SPBP35G2.10","SPAC694.06c","SPAC25A8.01c","SPBC29A10.14","SPBC11C11.09c","SPBC19F8.03c","SPBC428.07","SPCC4E9.01c","SPCC613.12c","SPCP1E11.10","SPCC338.17c","SPAC637.10c","SPBC1347.02","SPCC736.11","SPCC338.16","SPAC110.02","SPBC16A3.11","SPAC17C9.15c"],"gene_count":35,"ltp_gene_count":35,"approved_date":"2020-05-16"},{"uniquename":"PMID:12429929","title":"BRCA1 and Chk1 in G2/M checkpoint: a new order of regulation.","citation":"Cell Cycle 2002;1(3):178-80","abstract":"","authors":"Lee EY","authors_abbrev":"Lee EY","pubmed_publication_date":"2002","pubmed_entrez_date":"2002-11-14","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-11-26 01:19:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24806815","title":"Mdb1, a fission yeast homolog of human MDC1, modulates DNA damage response and mitotic spindle function.","citation":"PLoS One 2014;9(5):e97028","abstract":"During eukaryotic DNA damage response (DDR), one of the earliest events is the phosphorylation of the C-terminal SQ motif of histone H2AX (H2A in yeasts). In human cells, phosphorylated H2AX (γH2AX) is recognized by MDC1, which serves as a binding platform for the accumulation of a myriad of DDR factors on chromatin regions surrounding DNA lesions. Despite its important role in DDR, no homolog of MDC1 outside of metazoans has been described. Here, we report the characterization of Mdb1, a protein from the fission yeast Schizosaccharomyces pombe, which shares significant sequence homology with human MDC1 in their C-terminal tandem BRCT (tBRCT) domains. We show that in vitro, recombinant Mdb1 protein binds a phosphorylated H2A (γH2A) peptide, and the phospho-specific binding requires two conserved phospho-binding residues in the tBRCT domain of Mdb1. In vivo, Mdb1 forms nuclear foci at DNA double strand breaks (DSBs) induced by the HO endonuclease and ionizing radiation (IR). IR-induced Mdb1 focus formation depends on γH2A and the phospho-binding residues of Mdb1. Deleting the mdb1 gene does not overtly affect DNA damage sensitivity in a wild type background, but alters the DNA damage sensitivity of cells lacking another γH2A binder Crb2. Overexpression of Mdb1 causes severe DNA damage sensitivity in a manner that requires the interaction between Mdb1 and γH2A. During mitosis, Mdb1 localizes to spindles and concentrates at spindle midzones at late mitosis. The spindle midzone localization of Mdb1 requires its phospho-binding residues, but is independent of γH2A. Loss of Mdb1 or mutating its phospho-binding residues makes cells more resistant to the microtubule depolymerizing drug thiabendazole. We propose that Mdb1 performs dual roles in DDR and mitotic spindle regulation.","doi":"10.1371/journal.pone.0097028","authors":"Wei Y, Wang HT, Zhai Y, Russell P, Du LL","authors_abbrev":"Wei Y et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-05-09","publication_year":"2014","canto_session_key":"901cd8f6d579af4e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Li-Lin Du","canto_first_approved_date":"2015-06-10 08:03:21","canto_approved_date":"2025-09-04 10:31:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-21 05:02:56","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":40,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Li-Lin Du","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.12","SPCC622.08c","SPACUNK4.14","SPBC216.05","SPCC23B6.03c","SPBC342.05","SPAPB1A10.09","SPAC19G12.06c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-06-10"},{"uniquename":"PMID:32956753","title":"The N-terminus region of Drp1, a Rint1 family protein is essential for cell survival and its interaction with Rad50 protein in fission yeast S.pombe.","citation":"Biochim Biophys Acta Gen Subj 2021 Jan;1865(1):129739","abstract":"Defects in DNA repair pathway can lead to double-strand breaks leading to genomic instability. Earlier we have shown that S.pombe Drp1, a Rint1/Tip1 family protein is required for the recovery from DNA damage.\nVarious truncations of Drp1 protein were constructed and their role in DNA damage response and interaction with Rad50 protein has been studied by co-immunoprecipitation and pull-down assays.\nThe structural and functional analysis of Drp1 protein revealed that the N-terminus region of Drp1 is indispensable for the survival. The C-terminus truncation mutants, drp1C1Δ and drp1C2Δ exhibit temperature sensitive phenotype and are hypersensitive against DNA damaging agents with elevated level of Rad52-YFP foci at non-permissive temperature indicating the impairment for DNA damage repair pathway. The essential N-terminus region of Drp1 interacts with the C-terminus region of Rad50 and might be involved in influencing the MRN/X function. Small-angle X-ray (SAXS) analysis revealed three-domain like shapes in Drp1 protein while the C-terminus region of Rad50 exhibit unusual bulges. Computational docking studies revealed the amino acid residues at the C-terminus region of Rad50 that are involved in the interaction with the residues present at the N-terminal region of Drp1 indicating the importance of the N-terminal region of Drp1 protein.\nWe have identified the region of Drp1 and Rad50 proteins that are involved in the interaction and their role in the DNA damage response pathway has been analyzed.\nThe functional and structural aspects of fission yeast Drp1 protein and its interaction with Rad50 have been elucidated.","doi":"10.1016/j.bbagen.2020.129739","authors":"Gaurav S, Ranjan R, Kuldeep J, Dhiman K, Mahapatra PP, Ashish, Siddiqi MI, Ahmed S","authors_abbrev":"Gaurav S et al.","pubmed_publication_date":"Jan 2021","pubmed_entrez_date":"2020-09-21","publication_year":"2021","canto_session_key":"2a8601122076d17d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-09-23 00:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPBC691.02c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:22848669","title":"Studies on the roles of clathrin-mediated membrane trafficking and zinc transporter Cis4 in the transport of GPI-anchored proteins in fission yeast.","citation":"PLoS One 2012;7(7):e41946","abstract":"We previously identified Cis4, a zinc transporter belonging to the cation diffusion facilitator protein family, and we demonstrated that Cis4 is implicated in Golgi membrane trafficking in fission yeast. Here, we identified three glycosylphosphatidylinositol (GPI)-anchored proteins, namely Ecm33, Aah3, and Gaz2, as multicopy suppressors of the MgCl(2)-sensitive phenotype of cis4-1 mutant. The phenotypes of ecm33, aah3 and gaz2 deletion cells were distinct from each other, and Cis4 overexpression suppressed Δecm33 phenotypes but did not suppress Δaah3 defects. Notably, green fluorescent protein-tagged Ecm33, which was observed at the cell surface in wild-type cells, mostly localized as intracellular dots that are presumed to be the Golgi and endosomes in membrane-trafficking mutants, including Δapm1, ypt3-i5, and chc1-1 mutants. Interestingly, all these membrane-trafficking mutants showed hypersensitivity to BE49385A, an inhibitor of Its8 that is involved in GPI-anchored protein synthesis. Taken together, these results suggest that GPI-anchored proteins are transported through a clathrin-mediated post-Golgi membrane trafficking pathway and that zinc transporter Cis4 may play roles in membrane trafficking of GPI-anchored proteins in fission yeast.","doi":"10.1371/journal.pone.0041946","authors":"Jaiseng W, Fang Y, Ma Y, Sugiura R, Kuno T","authors_abbrev":"Jaiseng W et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-08-01","publication_year":"2012","canto_session_key":"13bf17b19bdebfdb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-27 12:21:41","canto_approved_date":"2025-05-27 14:12:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-27 12:19:29","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":53,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP16F5.07","SPAC26A3.05","SPCC63.02c","SPAC17D4.03c","SPBC839.08c","SPCC1322.03","SPAC1705.03c","SPBC1E8.05","SPAC18G6.03","SPBC1685.01"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2024-06-27"},{"uniquename":"PMID:28738844","title":"Analysis of SDHAF3 in familial and sporadic pheochromocytoma and paraganglioma.","citation":"BMC Cancer 2017 Jul 24;17(1):497","abstract":"Germline mutations in genes encoding subunits of succinate dehydrogenase (SDH) are associated with the development of pheochromocytoma (PC) and/or paraganglioma (PGL). As assembly factors have been identified as playing a role in maturation of individual SDH subunits and assembly of the functioning SDH complex, we hypothesized that SDHAF3 variants may be associated with PC/PGL and functionality of SDH.\nDNA was extracted from the blood of 37 individuals (from 23 families) with germline SDH mutations and 18 PC/PGL (15 sporadic, 3 familial) and screened for mutations using a custom gene panel, containing SDHAF3 (SDH assembly factor 3) as well as eight known PC/PGL susceptibility genes. Molecular and functional consequences of an identified sequence variant of SDHAF3 were assessed in yeast and mammalian cells (HEK293).\nUsing massively parallel sequencing, we identified a variant in SDHAF3, c.157 T > C (p.Phe53Leu), associated with increased prevalence in familial and sporadic PC/PGL (6.6%) when compared to normal populations (1.2% [1000 Genomes], p = 0.003; 2.1% [Exome Aggregation Consortium], p = 0.0063). In silico prediction tools suggest this variant is probably damaging to protein function, hence we assessed molecular and functional consequences of the resulting amino acid change (p.Phe53Leu) in yeast and human cells. We showed that introduction of SDHAF3 p.Phe53Leu into Sdh7 (ortholog of SDHAF3 in humans) null yeast resulted in impaired function, as observed by its failure to restore SDH activity when expressed in Sdh7 null yeast relative to WT SDHAF3. As SDHAF3 is involved in maturation of SDHB, we tested the functional impact of SDHAF3 c.157 T > C and various clinically relevant SDHB mutations on this interaction. Our in vitro studies in human cells show that SDHAF3 interacts with SDHB (residues 46 and 242), with impaired interaction observed in the presence of the SDHAF3 c.157 T > C variant.\nOur studies reveal novel insights into the biogenesis of SDH, uncovering a vital interaction between SDHAF3 and SDHB. We have shown that SDHAF3 interacts directly with SDHB (residue 242 being key to this interaction), and that a variant in SDHAF3 (c.157 T > C [p.Phe53Leu]) may be more prevalent in individuals with PC/PGL, and is hypomorphic via impaired interaction with SDHB.","doi":"10.1186/s12885-017-3486-z","authors":"Dwight T, Na U, Kim E, Zhu Y, Richardson AL, Robinson BG, Tucker KM, Gill AJ, Benn DE, Clifton-Bligh RJ, Winge DR","authors_abbrev":"Dwight T et al.","pubmed_publication_date":"24 Jul 2017","pubmed_entrez_date":"2017-07-26","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP23A10.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19629038","title":"Silent chromatin at the middle and ends: lessons from yeasts.","citation":"EMBO J 2009 Aug 05;28(15):2149-61","abstract":"Eukaryotic centromeres and telomeres are specialized chromosomal regions that share one common characteristic: their underlying DNA sequences are assembled into heritably repressed chromatin. Silent chromatin in budding and fission yeast is composed of fundamentally divergent proteins tat assemble very different chromatin structures. However, the ultimate behaviour of silent chromatin and the pathways that assemble it seem strikingly similar among Saccharomyces cerevisiae (S. cerevisiae), Schizosaccharomyces pombe (S. pombe) and other eukaryotes. Thus, studies in both yeasts have been instrumental in dissecting the mechanisms that establish and maintain silent chromatin in eukaryotes, contributing substantially to our understanding of epigenetic processes. In this review, we discuss current models for the generation of heterochromatic domains at centromeres and telomeres in the two yeast species.","doi":"10.1038/emboj.2009.185","authors":"Bühler M, Gasser SM","authors_abbrev":"Bühler M et al.","pubmed_publication_date":"05 Aug 2009","pubmed_entrez_date":"2009-07-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15274920","title":"Structure of the actin crosslinking core of fimbrin.","citation":"Structure 2004 Jun;12(6):999-1013","abstract":"Filamentous actin is organized into bundles and orthogonal networks by the fimbrin/alpha-actinin superfamily of F-actin crosslinking proteins. The crystal structure of the Arabidopsis thaliana and Schizosaccharomyces pombe fimbrin cores provides the first description of a functional F-actin crosslinking protein and highlights the compact and distinctly asymmetric organization of the fimbrin molecule, in which the two actin binding domains present distinct surfaces to solvent. The mapping of functionally important residues onto the structure affords new insights into the binding process and provides additional constraints which must be accommodated by models for F-actin binding and crosslinking. Most strikingly, this work provides unique insight into the mechanistic features of conditional-lethal mutants and their extragenic suppressors, which highlight conformational and dynamic properties required for fimbrin function. These results underscore the power of jointly considering structural and genetic suppressor data for obtaining unexpected and biologically relevant mechanistic information.","authors":"Klein MG, Shi W, Ramagopal U, Tseng Y, Wirtz D, Kovar DR, Staiger CJ, Almo SC","authors_abbrev":"Klein MG et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-07-28","publication_year":"2004","canto_session_key":"eb74b231a72506af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-06-30 13:50:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-06-30 13:50:21","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1778.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-06-30","pdb_entries":[{"pdb_id":"1rt8","gene_chains":[{"gene_uniquename":"SPBC1778.06c","chain":"A","position":"108-614"}],"title":"CRYSTAL STRUCTURE OF THE ACTIN-CROSSLINKING CORE OF SCHIZOSACCHAROMYCES POMBE FIMBRIN","entry_authors":"Klein MG,Shi W,Ramagopal U,Tseng Y,Wirtz D,Kovar DR,Staiger CJ,Almo SC","entry_authors_abbrev":"Klein MG et al.","reference_uniquename":"PMID:15274920","experimental_method":"X-ray","resolution":"2.0"}]},{"uniquename":"PMID:16054366","title":"Post-transcriptional control of gene expression: a genome-wide perspective.","citation":"Trends Biochem Sci 2005 Sep;30(9):506-14","abstract":"Gene expression is regulated at multiple levels, and cells need to integrate and coordinate different layers of control to implement the information in the genome. Post-transcriptional levels of regulation such as transcript turnover and translational control are an integral part of gene expression and might rival the sophistication and importance of transcriptional control. Microarray-based methods are increasingly used to study not only transcription but also global patterns of transcript decay and translation rates in addition to comprehensively identify targets of RNA-binding proteins. Such large-scale analyses have recently provided supplementary and unique insights into gene expression programs. Integration of several different datasets will ultimately lead to a system-wide understanding of the varied and complex mechanisms for gene expression control.","authors":"Mata J, Marguerat S, Bähler J","authors_abbrev":"Mata J et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-08-02","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29691402","title":"Repeated evolution of self-compatibility for reproductive assurance.","citation":"Nat Commun 2018 Apr 24;9(1):1639","abstract":"Sexual reproduction in eukaryotes requires the fusion of two compatible gametes of opposite sexes or mating types. To meet the challenge of finding a mating partner with compatible gametes, evolutionary mechanisms such as hermaphroditism and self-fertilization have repeatedly evolved. Here, by combining the insights from comparative genomics, computer simulations and experimental evolution in fission yeast, we shed light on the conditions promoting separate mating types or self-compatibility by mating-type switching. Analogous to multiple independent transitions between switchers and non-switchers in natural populations mediated by structural genomic changes, novel switching genotypes readily evolved under selection in the experimental populations. Detailed fitness measurements accompanied by computer simulations show the benefits and costs of switching during sexual and asexual reproduction, governing the occurrence of both strategies in nature. Our findings illuminate the trade-off between the benefits of reproductive assurance and its fitness costs under benign conditions facilitating the evolution of self-compatibility.","doi":"10.1038/s41467-018-04054-6","authors":"Nieuwenhuis BPS, Tusso S, Bjerling P, Stångberg J, Wolf JBW, Immler S","authors_abbrev":"Nieuwenhuis BPS et al.","pubmed_publication_date":"24 Apr 2018","pubmed_entrez_date":"2018-04-26","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-04-26 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24696293","title":"Ecl1 is activated by the transcription factor Atf1 in response to H2O2 stress in Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2014 Aug;289(4):685-93","abstract":"The Ecl1 family genes extend the lifespan of fission yeast when overexpressed. They also cause resistance against H(2)O(2) stress. In this study, we found that the bZip transcription factor Atf1 is a direct activator of the induction of extender of chronological lifespan (ecl1 (+)) by H(2)O(2) stress. Based on ChIP analysis, we identified that Atf1 binds to the upstream DNA region of ecl1(+). Previously, we reported that overexpression of ecl1(+) increased the expression of the catalase-encoding ctt1(+). This ecl1(+)-dependent increase of ctt1(+) expression occurred in ∆atf1 mutant. On the other hand, the activation of ctt1 (+) caused by the ∆pyp1 mutation, which enhances Sty1-Atf1 activity, could occur in ∆ecl1 mutant. Based on these results, we propose that Atf1 can regulate ctt1(+) in both an Ecl1-dependent and an Ecl1-independent manner.","doi":"10.1007/s00438-014-0845-1","authors":"Shimasaki T, Ohtsuka H, Naito C, Murakami H, Aiba H","authors_abbrev":"Shimasaki T et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-04-04","publication_year":"2014","canto_session_key":"62345443623a0faf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-07 16:46:11","canto_approved_date":"2025-09-03 18:11:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-22 08:31:09","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPBP35G2.16c","SPCC757.07c","SPAC26F1.10c","SPCC70.12c","SPBC8E4.12c","SPBC29B5.01","SPAC24B11.06c","SPCC576.03c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2017-12-07"},{"uniquename":"PMID:16024772","title":"A meiosis-specific cyclin regulated by splicing is required for proper progression through meiosis.","citation":"Mol Cell Biol 2005 Aug;25(15):6330-7","abstract":"The meiotic cell cycle is modified from the mitotic cell cycle by having a premeiotic S phase which leads to high levels of recombination, a reductional pattern of chromosome segregation at the first division, and a second division with no intervening DNA synthesis. Cyclin-dependent kinases are essential for progression through the meiotic cell cycle, as for the mitotic cycle. Here we show that a fission yeast cyclin, Rem1, is present only during meiosis. Cells lacking Rem1 have impaired meiotic recombination, and Rem1 is required for premeiotic DNA synthesis when Cig2 is not present. rem1 expression is regulated at the level of both transcription and splicing, with Mei4 as a positive and Cig2 a negative factor of rem1 splicing. This regulation ensures the timely appearance of the different cyclins during meiosis, which is required for the proper progression through the meiotic cell cycle. We propose that the meiosis-specific B-type cyclin Rem1 has a central role in bringing about progression through meiosis.","authors":"Malapeira J, Moldón A, Hidalgo E, Smith GR, Nurse P, Ayté J","authors_abbrev":"Malapeira J et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-07-19","publication_year":"2005","canto_session_key":"48d03bd19c1a86eb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16E9.17c","SPAPB2B4.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:41750377","title":"Transporter-Driven Glycerophosphocholine (GPC) Toxicity Is Conserved from Fission Yeast to Budding Yeast: Roles for Inositol Pyrophosphates and Gde1 Regulation in Fission Yeast.","citation":"Biomolecules 2026 Feb 16;16(2)","abstract":"Glycerophosphocholine (GPC) and glycerophosphoinositol (GPI) are phospholipid metabolites generated by phospholipase-mediated deacylation. In budding yeast, they enter cells via the Git1 permease; in fission yeast, the homolog is Tgp1. This study investigates why GPC is toxic to  asp1-STF  mutants, where Tgp1 is upregulated due to loss of Asp1 pyrophosphatase, resulting in elevated inositol pyrophosphate 1,5-IP 8 . We show that  S. pombe  Tgp1 specifically transports GPC, explaining why GPC, but not GPI, impairs growth. Increased GPC uptake slows doubling time but does not reduce viability. Toxicity is relieved by deletion of Gde1, a phosphodiesterase that hydrolyzes GPC to choline and glycerol-3-phosphate. Mutations in either the Gde1 active site or SPX domain also suppress toxicity, and radiolabeling confirms both domains are required for enzymatic activity. GPC is toxic in cells vastly overexpressing Tgp1 even without elevated IP 8 , but Gde1 loss does not suppress this effect. Similarly, in  S. cerevisiae  overexpressing the  Candida albicans  Git3 transporter, GPC provision causes toxicity independent of Gde1. Loss of Gpc1, the acyltransferase converting GPC to lysophosphatidylcholine, does not alter toxicity in either yeast. These findings highlight a conserved process by which GPC regulates growth and reveal a role for IP 8  in modulating this process.","doi":"10.3390/biom16020309","authors":"Hrach VL, Schwer B, Vitek L, Borowicz M, Innokentev A, Sanchez AM, Singer JR, Shuman S, Patton-Vogt J","authors_abbrev":"Hrach VL et al.","pubmed_publication_date":"16 Feb 2026","pubmed_entrez_date":"2026-02-27","publication_year":"2026","canto_session_key":"dfaf073c826d74b3","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-02-28 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1271.09","SPCC645.02","SPBC428.03c","SPAPB1E7.05","SPCC1672.06c","SPBP4G3.02"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:20929762","title":"Molecular biology. Surfing chromosomes (and Survivin).","citation":"Science 2010 Oct 08;330(6001):183-4","abstract":"","doi":"10.1126/science.1197261","authors":"Musacchio A","authors_abbrev":"Musacchio A","pubmed_publication_date":"08 Oct 2010","pubmed_entrez_date":"2010-10-09","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23222841","title":"Pivoting of microtubules around the spindle pole accelerates kinetochore capture.","citation":"Nat Cell Biol 2013 Jan;15(1):82-7","abstract":"During cell division, spindle microtubules attach to chromosomes through kinetochores, protein complexes on the chromosome. The central question is how microtubules find kinetochores. According to the pioneering idea termed search-and-capture, numerous microtubules grow from a centrosome in all directions and by chance capture kinetochores. The efficiency of search-and-capture can be improved by a bias in microtubule growth towards the kinetochores, by nucleation of microtubules at the kinetochores and at spindle microtubules, by kinetochore movement, or by a combination of these processes. Here we show in fission yeast that kinetochores are captured by microtubules pivoting around the spindle pole, instead of growing towards the kinetochores. This pivoting motion of microtubules is random and independent of ATP-driven motor activity. By introducing a theoretical model, we show that the measured random movement of microtubules and kinetochores is sufficient to explain the process of kinetochore capture. Our theory predicts that the speed of capture depends mainly on how fast microtubules pivot, which was confirmed experimentally by speeding up and slowing down microtubule pivoting. Thus, pivoting motion allows microtubules to explore space laterally, as they search for targets such as kinetochores.","doi":"10.1038/ncb2640","authors":"Kalinina I, Nandi A, Delivani P, Chacón MR, Klemm AH, Ramunno-Johnson D, Krull A, Lindner B, Pavin N, Tolić-Nørrelykke IM","authors_abbrev":"Kalinina I et al.","pubmed_publication_date":"Jan 2013","pubmed_entrez_date":"2012-12-11","publication_year":"2013","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8063718","title":"Dominance of metallothionein in metal ion buffering in yeast capable of synthesis of (gamma EC)nG isopeptides.","citation":"J Biol Chem 1994 Aug 19;269(33):21010-5","abstract":"The relationship of yeast metallothionein (MT) and (gamma EC)nG isopeptides (phytochelatins) in metal ion buffering was assessed. The effect of constitutive expression of yeast metallothionein (MT) genes on accumulation of metal-(gamma EC)nG isopeptide (phytochelatin) complexes was analyzed in Candida glabrata and Schizosaccharomyces pombe cultures incubated in the presence of cadmium salts. Constitutive expression of the Saccharomyces cerevisiae MT (CUP1) gene inhibited the accumulation of metal-phytochelatin complexes in both C. glabrata and S. pombe. Intracellular Cd(II) sequestration occurred by formation of CdMT complexes. Phytochelatin (gamma EC)nG complexes appear to function in metal buffering in cells when MT genes are not present or expressed. A third condition in which metal-(gamma EC)nG complexes are observed is when constitutively expressed MT does not accumulate. We observed that C. glabrata lacking the AMT1 gene necessary for copper induction of the MT genes expressed MTII constitutively, but this expression does not lead to CdMTII accumulation. Only Cd-(gamma EC)nG complexes accumulate. Likewise, metal exposed cultures of S. cerevisiae (cup1) transformed with C. glabrata MTII under the constitutive ADH1 promoter resulted in constitutive expression of MTII and accumulation of CuMTII complexes but no CdMTII complexes. The inability of constitutively expressed C. glabrata MTII to buffer Cd(II) ions may arise in part from an inherent kinetic lability of CdMTII complexes. Incubation of ZnMTII with a metallochromic chelator, 4-(2-pyridylazo)resorcinol resulted in greater Zn(II) loss than Zn(II) complexes with CUP1 MT and C. glabrata MTI. C. glabrata MTII appears to be the first MT described which forms an unstable Cd(II) complex.","authors":"Yu W, Santhanagopalan V, Sewell AK, Jensen LT, Winge DR","authors_abbrev":"Yu W et al.","pubmed_publication_date":"19 Aug 1994","pubmed_entrez_date":"1994-08-19","publication_year":"1994","canto_session_key":"0d9c7686b496bfb7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-09-30 13:59:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-09-30 13:54:33","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-09-30"},{"uniquename":"PMID:10766735","title":"Distinct protein interaction domains and protein spreading in a complex centromere.","citation":"Genes Dev 2000 Apr 01;14(7):783-91","abstract":"Fission yeast (Schizosaccharomyces pombe) centromeres are composed of large (40-100 kb) inverted repeats that display heterochromatic features, thus providing a good model for higher eukaryotic centromeres. The association of three proteins that mediate region-specific silencing across centromere 1 has been mapped by quantitative chromatin immunoprecipitation. Swi6 and Chp1 are confined to the flanking outer repeats and Swi6 can spread across at least 3 kb of extraneous chromatin in cen1. In contrast, Mis6 coats the inner repeats and central core. tRNA genes demarcate this transition zone. These analyses clearly define two distinct domains within this complex centromere which interact with different proteins.","authors":"Partridge JF, Borgstrøm B, Allshire RC","authors_abbrev":"Partridge JF et al.","pubmed_publication_date":"01 Apr 2000","pubmed_entrez_date":"2000-04-15","publication_year":"2000","canto_session_key":"47f385e95240624c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-02-02 10:03:08","canto_approved_date":"2024-02-20 18:23:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-22 13:58:12","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPAC18G6.02c","SPAC1687.20c","SPCC11E10.08","SPBC428.08c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-02-02"},{"uniquename":"PMID:16532353","title":"Meiotic recombination proteins localize to linear elements in Schizosaccharomyces pombe.","citation":"Chromosoma 2006 Aug;115(4):330-40","abstract":"In fission yeast, meiotic prophase nuclei develop structures known as linear elements (LinEs), instead of a canonical synaptonemal complex. LinEs contain Rec10 protein. While Rec10 is essential for meiotic recombination, the precise role of LinEs in this process is unknown. Using in situ immunostaining, we show that Rec7 (which is required for meiosis-specific DNA double-strand break (DSB) formation) aggregates in foci on LinEs. The strand exchange protein Rad51, which is known to mark the sites of DSBs, also localizes to LinEs, although to a lesser degree. The number of Rec7 foci corresponds well with the average number of genetic recombination events per meiosis suggesting that Rec7 marks the sites of recombination. Rec7 and Rad51 foci do not co-localize, presumably because they act sequentially on recombination sites. The localization of Rec7 is dependent on Rec10 but independent of the DSB-inducing protein Rec12/Spo11. Neither Rec7 nor Rad51 localization depends on the LinE-associated proteins Hop1 and Mek1, but the formation of Rad51 foci depends on Rec10, Rec7, and, as expected, Rec12/Spo11. We propose that LinEs form around designated recombination sites before the induction of DSBs and that most, if not all, meiotic recombination initiates within the setting provided by LinEs.","authors":"Lorenz A, Estreicher A, Kohli J, Loidl J","authors_abbrev":"Lorenz A et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-03-15","publication_year":"2006","canto_session_key":"b447b564f630559e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-07 14:30:50","canto_approved_date":"2020-07-09 15:44:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-08-07 14:30:44","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.04c","SPAC17A5.11","SPAC14C4.03","SPCC1753.03c","SPBC1718.02","SPBC29A10.14","SPAC644.14c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2017-08-07"},{"uniquename":"PMID:23349636","title":"Coordinated degradation of replisome components ensures genome stability upon replication stress in the absence of the replication fork protection complex.","citation":"PLoS Genet 2013;9(1):e1003213","abstract":"The stabilization of the replisome complex is essential in order to achieve highly processive DNA replication and preserve genomic integrity. Conversely, it would also be advantageous for the cell to abrogate replisome functions to prevent inappropriate replication when fork progression is adversely perturbed. However, such mechanisms remain elusive. Here we report that replicative DNA polymerases and helicases, the major components of the replisome, are degraded in concert in the absence of Swi1, a subunit of the replication fork protection complex. In sharp contrast, ORC and PCNA, which are also required for DNA replication, were stably maintained. We demonstrate that this degradation of DNA polymerases and helicases is dependent on the ubiquitin-proteasome system, in which the SCF(Pof3) ubiquitin ligase is involved. Consistently, we show that Pof3 interacts with DNA polymerase ε. Remarkably, forced accumulation of replisome components leads to abnormal DNA replication and mitotic catastrophes in the absence of Swi1. Swi1 is known to prevent fork collapse at natural replication block sites throughout the genome. Therefore, our results suggest that the cell elicits a program to degrade replisomes upon replication stress in the absence of Swi1. We also suggest that this program prevents inappropriate duplication of the genome, which in turn contributes to the preservation of genomic integrity.","doi":"10.1371/journal.pgen.1003213","authors":"Roseaulin LC, Noguchi C, Martinez E, Ziegler MA, Toda T, Noguchi E","authors_abbrev":"Roseaulin LC et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-01-26","publication_year":"2013","canto_session_key":"758c93b03dfe5c59","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Eishi Noguchi","canto_first_approved_date":"2017-12-11 17:20:22","canto_approved_date":"2026-01-29 11:56:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-30 13:36:40","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Eishi Noguchi","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4.04c","SPBC216.06c","SPBC25H2.13c","SPBC29A10.15","SPBC16G5.01","SPAC694.06c","SPBC211.04c","SPBC336.04","SPCC338.16","SPCC16A11.17","SPBC409.05"],"gene_count":11,"ltp_gene_count":5,"approved_date":"2017-12-11"},{"uniquename":"PMID:10607565","title":"A switch in microtubule dynamics at the onset of anaphase B in the mitotic spindle of Schizosaccharomyces pombe.","citation":"Curr Biol 1999 Dec 02;9(23):1423-6","abstract":"Microtubule dynamics have key roles in mitotic spindle assembly and chromosome movement [1]. Fast turnover of spindle microtubules at metaphase and polewards flux of microtubules (polewards movement of the microtubule lattice with depolymerization at the poles) at both metaphase and anaphase have been observed in mammalian cells [2]. Imaging spindle dynamics in genetically tractable yeasts is now possible using green fluorescent protein (GFP)-tagging of tubulin and sites on chromosomes [3] [4] [5] [6] [7] [8]. We used photobleaching of GFP-labeled tubulin to observe microtubule dynamics in the fission yeast Schizosaccharomyces pombe. Photobleaching did not perturb progress through mitosis. Bleached marks made on the spindle during metaphase recovered their fluorescence rapidly, indicating fast microtubule turnover. Recovery was spatially non-uniform, but we found no evidence for polewards flux. Marks made during anaphase B did not recover fluorescence, and were observed to slide away from each other at the same rate as spindle elongation. Fast microtubule turnover at metaphase and a switch to stable microtubules at anaphase suggest the existence of a cell-cycle-regulated molecular switch that controls microtubule dynamics and that may be conserved in evolution. Unlike the situation for vertebrate spindles, microtubule depolymerization at poles and polewards flux may not occur in S. pombe mitosis. We conclude that GFP-tubulin photobleaching in conjunction with mutant cells should aid research on molecular mechanisms causing and regulating dynamics.","authors":"Mallavarapu A, Sawin K, Mitchison T","authors_abbrev":"Mallavarapu A et al.","pubmed_publication_date":"02 Dec 1999","pubmed_entrez_date":"1999-12-23","publication_year":"1999","canto_session_key":"0d3f0457795bd6aa","canto_annotation_status":"APPROVED","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_first_approved_date":"2022-06-13 11:42:31","canto_approved_date":"2022-06-13 11:42:31","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-06-13 11:42:20","canto_added_date":"2012-02-24 05:52:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2022-06-13"},{"uniquename":"PMID:27613421","title":"Transcription-coupled changes to chromatin underpin gene silencing by transcriptional interference.","citation":"Nucleic Acids Res 2016 Dec 15;44(22):10619-10630","abstract":"Long non-coding RNA (lncRNA) transcription into a downstream promoter frequently results in transcriptional interference. However, the mechanism of this repression is not fully understood. We recently showed that drug tolerance in fission yeast Schizosaccharomyces pombe is controlled by lncRNA transcription upstream of the tgp1 +  permease gene. Here we demonstrate that transcriptional interference of tgp1 +  involves several transcription-coupled chromatin changes mediated by conserved elongation factors Set2, Clr6CII, Spt6 and FACT. These factors are known to travel with RNAPII and establish repressive chromatin in order to limit aberrant transcription initiation from cryptic promoters present in gene bodies. We therefore conclude that conserved RNAPII-associated mechanisms exist to both suppress intragenic cryptic promoters during genic transcription and to repress gene promoters by transcriptional interference. Our analyses also demonstrate that key mechanistic features of transcriptional interference are shared between S. pombe and the highly divergent budding yeast Saccharomyces cerevisiae Thus, transcriptional interference is an ancient, conserved mechanism for tightly controlling gene expression. Our mechanistic insights allowed us to predict and validate a second example of transcriptional interference involving the S. pombe pho1 +  gene. Given that eukaryotic genomes are pervasively transcribed, transcriptional interference likely represents a more general feature of gene regulation than is currently appreciated.","authors":"Ard R, Allshire RC","authors_abbrev":"Ard R et al.","pubmed_publication_date":"15 Dec 2016","pubmed_entrez_date":"2016-09-11","publication_year":"2016","canto_session_key":"797e255dbbd360de","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-09-12 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29B12.02c","SPBC1271.09"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:25009287","title":"Megadalton-node assembly by binding of Skb1 to the membrane anchor Slf1.","citation":"Mol Biol Cell 2014 Sep 01;25(17):2660-8","abstract":"The plasma membrane contains both dynamic and static microdomains. Given the growing appreciation of cortical microdomains in cell biology, it is important to determine the organizational principles that underlie assembly of compartmentalized structures at the plasma membrane. The fission yeast plasma membrane is highly compartmentalized by distinct sets of cortical nodes, which control signaling for cell cycle progression and cytokinesis. The mitotic inhibitor Skb1 localizes to a set of cortical nodes that provide spatial control over signaling for entry into mitosis. However, it has been unclear whether these nodes contain other proteins and how they might be organized and tethered to the plasma membrane. Here we show that Skb1 forms nodes by interacting with the novel protein Slf1, which is a limiting factor for node formation in cells. Using quantitative fluorescence microscopy and in vitro assays, we demonstrate that Skb1-Slf1 nodes are megadalton structures that are anchored to the membrane by a lipid-binding region in the Slf1 C-terminus. We propose a mechanism for higher-order node formation by Skb1 and Slf1, with implications for macromolecular assemblies in diverse cell types.","doi":"10.1091/mbc.E14-04-0896","authors":"Deng L, Kabeche R, Wang N, Wu JQ, Moseley JB","authors_abbrev":"Deng L et al.","pubmed_publication_date":"01 Sep 2014","pubmed_entrez_date":"2014-07-11","publication_year":"2014","canto_session_key":"5f0343986c82c553","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"James Moseley","canto_first_approved_date":"2016-10-26 14:16:14","canto_approved_date":"2025-11-27 23:05:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 13:35:22","canto_added_date":"2014-07-12 00:15:30","annotation_curators":[{"name":"James Moseley","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.03c","SPBC17D11.05","SPBC32F12.11","SPAC4A8.16c","SPBC16H5.11c","SPBP23A10.07","SPAC1565.08","SPAC17H9.04c","SPCC1620.11","SPBC1539.09c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2016-10-26"},{"uniquename":"PMID:12490702","title":"Characterization of the fission yeast ribosomal DNA binding factor: components share homology with Upstream Activating Factor and with SWI/SNF subunits.","citation":"Nucleic Acids Res 2002 Dec 15;30(24):5347-59","abstract":"A ribosomal DNA (rDNA) binding activity was previously characterized in fission yeast that recognized the upstream ribosomal RNA (rRNA) gene promoter in a sequence specific manner and which stimulated rRNA synthesis. It was found to share characteristics with Saccharomyces cerevisiae's Upstream Activating Factor (UAF), an RNA polymerase I (pol I) specific transcription stimulatory factor. Putative fission yeast homologs of the S.cerevisiae UAF subunits, Rrn5p and Rrn10p, were identified. The Schizosaccharomyces pombe rDNA binding activity/transcriptional stimulatory activity was found to co-fractionate with both SpRrn5h and SpRrn10h. Analysis of polypeptides interacting with SpRrn10h uncovered a 27 kDa polypeptide (Spp27) homologous to a SWI/SNF component (now known to be homologous to Uaf30p). The contributions of the S.pombe and S.cerevisiae upstream rDNA promoter domains were assessed in cross-species transcriptional assays. Furthermore, comparative genomic analysis revealed putative Rrn5p, Rrn10p, Rrn9p and p27 homologs in multiple non-vertebrates. The S.pombe rDNA binding activity is proposed to be an RNA pol I specific SWI/SNF type factor.","authors":"Liu M, Guo A, Boukhgalter B, Van Den Heuvel K, Tripp M, Pape L","authors_abbrev":"Liu M et al.","pubmed_publication_date":"15 Dec 2002","pubmed_entrez_date":"2002-12-20","publication_year":"2002","canto_session_key":"1c2be2da0ce4f585","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-05-30 15:54:51","canto_approved_date":"2018-06-21 09:01:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-30 15:54:43","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.08","SPBC3B8.11","SPCC285.17","SPAC29A4.10"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-05-30"},{"uniquename":"PMID:19571671","title":"Unrepaired oxidative DNA damage induces an ATR/ATM apoptotic-like response in quiescent fission yeast.","citation":"Cell Cycle 2009 Aug;8(15):2326-31","abstract":"Programmed cell death is a term which refers to a genetic decision of self-killing or suicide of a cell. Programmed cell death is not restricted to multicellular organisms and was described in a wide range of unicellular eukaryotes, indicating phylogenetically conserved functions, that participate in an adaptive response to cellular stress. Here we review and discuss our observations recently published in the EMBO Journal,(1) that non-dividing fission yeast, Schizosaccharomyces pombe, exhibits a DNA damage response leading to cell death. We found that Tdp1 protects quiescent S. pombe cells against oxidative DNA damage. Tdp1 is a well-conserved tyrosyl-DNA phosphodiesterase required for single-strand break DNA repair, the mutation of Tdp1 is responsible for the recessively inherited syndrome spinocerebellar ataxia with axonal neuropathy (SCAN1) in humans. We found that tdp1 mutant yeast cells grow, as well as the wild-type cells, during the vegetative state, but progressively die in the quiescent state. We showed that, in the absence of Tdp1, the accumulation of unrepaired oxidative DNA damage triggers a genetic response, leading to checkpoint-dependent (ATM/ATR) nuclear DNA degradation, reminiscent of apoptosis. Our results indicate that the reactive oxygen species (ROS) produced during mitochondrial respiration are the main DNA damaging agents in the physiological quiescent state.","authors":"Arcangioli B, Ben Hassine S","authors_abbrev":"Arcangioli B et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-07-03","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18377730","title":"A pheromone mutant of Schizosaccharomyces pombe displays nucleolar fragmentation.","citation":"BMB Rep 2008 Mar 31;41(3):248-53","abstract":"Stresses and nutritional starvation are two main external signals for the induction of sex pheromones in the fission yeast Schizosaccharomyces pombe. In an attempt to identify the components involved in transduction of starvation signals, we screened 135 temperature-sensitive (ts) mutants and isolated 6 mutants that induced the pheromone even in the presence of a nitrogen source. These mutants exhibited two distinct induction phenotypes: pheromone induction at restrictive but not at permissive temperatures; and pheromone induction at both permissive and restrictive temperatures. The times required for the maximum pheromone induction at the restrictive temperature differed slightly in each mutant. In addition to the pheromone induction phenotype, the ts243 and ts304 mutants exhibited cell-division-cycle defects. The ts304 mutant cells showed an abnormal cytoplasmic DAPI staining pattern. The nucleolus of this mutant seemed to be fragmented, a phenomenon which is typically observed in aged yeast cells. The result of our genetic analysis indicated that the pheromone induction mutants belonged to 6 separate complementation groups. We designated these mutants pws1 to pws6.","authors":"Jun J, Kim D","authors_abbrev":"Jun J et al.","pubmed_publication_date":"31 Mar 2008","pubmed_entrez_date":"2008-04-02","publication_year":"2008","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17135288","title":"Prohibitins interact genetically with Atp23, a novel processing peptidase and chaperone for the F1Fo-ATP synthase.","citation":"Mol Biol Cell 2007 Feb;18(2):627-35","abstract":"The generation of cellular energy depends on the coordinated assembly of nuclear and mitochondrial-encoded proteins into multisubunit respiratory chain complexes in the inner membrane of mitochondria. Here, we describe the identification of a conserved metallopeptidase present in the intermembrane space, termed Atp23, which exerts dual activities during the biogenesis of the F(1)F(O)-ATP synthase. On one hand, Atp23 serves as a processing peptidase and mediates the maturation of the mitochondrial-encoded F(O)-subunit Atp6 after its insertion into the inner membrane. On the other hand and independent of its proteolytic activity, Atp23 promotes the association of mature Atp6 with Atp9 oligomers. This assembly step is thus under the control of two substrate-specific chaperones, Atp10 and Atp23, which act on opposite sides of the inner membrane. Strikingly, both ATP10 and ATP23 were found to genetically interact with prohibitins, which build up large, ring-like assemblies with a proposed scaffolding function in the inner membrane. Our results therefore characterize not only a novel processing peptidase with chaperone activity in the mitochondrial intermembrane space but also link the function of prohibitins to the F(1)F(O)-ATP synthase complex.","authors":"Osman C, Wilmes C, Tatsuta T, Langer T","authors_abbrev":"Osman C et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2006-12-01","publication_year":"2007","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC320.12","SPMIT.10","SPAC4G8.11c","SPMIT.07"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:14766746","title":"Primer utilization by DNA polymerase alpha-primase is influenced by its interaction with Mcm10p.","citation":"J Biol Chem 2004 Apr 16;279(16):16144-53","abstract":"Models of DNA replication in yeast and Xenopus suggest that Mcm10p is required to generate the pre-initiation complex as well as progression of the replication fork during the elongation of DNA chains. In this report, we show that the Schizosaccharomyces pombe Mcm10p/Cdc23p binds to the S. pombe DNA polymerase (pol) alpha-primase complex in vitro by interacting specifically with the catalytic p180 subunit and stimulates DNA synthesis catalyzed by the pol alpha-primase complex with various primed DNA templates. We investigated the mechanism by which Mcm10p activates the polymerase activity of the pol alpha-primase complex by generating truncated derivatives of the full-length 593-amino acid Mcm10p. Their ability to stimulate pol alpha polymerase activity and bind to single-stranded DNA and to pol alpha were compared. Concomitant with increased deletion of the N-terminal region (from amino acids 95 to 415), Mcm10p derivatives lost their ability to stimulate pol alpha polymerase activity and bind to single-stranded DNA. Truncated derivatives of Mcm10p containing amino acids 1-416 retained the pol alpha binding activity, whereas the C terminus, amino acids 496-593, did not. These results demonstrate that both the single-stranded DNA binding and the pol alpha binding properties of Mcm10p play important roles in the activation. In accord with these findings, Mcm10p facilitated the binding of pol alpha-primase complex to primed DNA and formed a stable complex with pol alpha-primase on primed templates. A mutant that failed to activate or bind to DNA and pol alpha, was not observed in this complex. We suggest that the interaction of Mcm10p with the pol alpha-primase complex, its binding to single-stranded DNA, and its activation of the polymerase complex together contribute to its role in the elongation phase of DNA replication.","authors":"Fien K, Cho YS, Lee JK, Raychaudhuri S, Tappin I, Hurwitz J","authors_abbrev":"Fien K et al.","pubmed_publication_date":"16 Apr 2004","pubmed_entrez_date":"2004-02-10","publication_year":"2004","canto_session_key":"c60e704e5f4cb1e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-02-18 17:31:46","canto_approved_date":"2024-04-03 17:44:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-18 17:31:39","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c","SPBC1347.10"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-02-18"},{"uniquename":"PMID:16413587","title":"Bystander effects in unicellular organisms.","citation":"Mutat Res 2006 May 11;597(1-2):78-86","abstract":"Radiation-induced bystander effects have been seen in mammalian cells from diverse origins. These effects can be transmitted through the medium to cells not present at the time of irradiation. We have developed an assay for detecting bystander effects in the unicellular eukaryote, the fission yeast Schizosaccharomyces pombe. This assay allows maximal exposure of unirradiated cells to cells that have received electron beam irradiation. S. pombe cells were irradiated with 16-18 MeV electrons from a pulsed electron LINAC. When survival of the irradiated cells decreased to approximately 50%, forward-mutation to 2-deoxy-d-glucose resistance increased in the unirradiated bystander cells. Further increase in dose had no additional effect on this increase. In order to detect this response, it was necessary for the irradiated cell/unirradiated cell ratio to be high. Other cellular stresses, such as heat treatment, UV irradiation, and bleomycin exposure, also caused a detectable response in untreated cells grown with the treated cells. We discuss evolutionary implications of these results.","authors":"DeVeaux LC, Durtschi LS, Case JG, Wells DP","authors_abbrev":"DeVeaux LC et al.","pubmed_publication_date":"11 May 2006","pubmed_entrez_date":"2006-01-18","publication_year":"2006","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34157946","title":"TOR and MAP kinase pathways synergistically regulate autophagy in response to nutrient depletion in fission yeast.","citation":"Autophagy 2022 Feb;18(2):375-390","abstract":"General autophagy is an evolutionarily conserved process in eukaryotes, by which intracellular materials are transported into and degraded inside lysosomes or vacuoles, with the main goal of recycling those materials during periods of starvation. The molecular bases of autophagy have been widely described in  Saccharomyces cerevisiae , and the specific roles of Atg proteins in the process were first characterized in this model system. Important contributions have been made in  Schizosaccharomyces pombe  highlighting the evolutionary similarity and, at the same time, diversity of Atg components in autophagy. However, little is known regarding signals, pathways and role of autophagy in this distant yeast. Here, we undertake a global approach to investigate the signals, the pathways and the consequences of autophagy activation. We demonstrate that not only nitrogen but several nutritional deprivations including lack of carbon, sulfur, phosphorus or leucine sources, trigger autophagy, and that the TORC1, TORC2 and MAP kinase Sty1 pathways control the onset of autophagy. Furthermore, we identify an unexpected phenotype of autophagy-defective mutants, namely their inability to survive in the absence of leucine when biosynthesis of this amino acid is impaired. Abbreviations:  ATG: autophagy-related; cAMP: cyclic adenosine monophosphate; cDNA: complementary deoxyribonucleic acid; GFP: green fluorescence protein; Gluc: glucose; Leu: leucine; MAP: mitogen-activated protein; MM: minimal medium; PI: propidium iodine; PKA: protein kinase A; RNA: ribonucleic acid; RT-qPCR: real time quantitative polymerase chain reaction;  S. cerevisiae: Saccharomyces cerevisiae; S. pombe: Schizosaccharomyces pombe ; TCA: trichloroacetic acid; TOR: target of rapamycin; TORC1: target of rapamycin complex 1; TORC2: target of rapamycin complex 2; YE5S: yeast extract 5 amino acid supplemented.","doi":"10.1080/15548627.2021.1935522","authors":"Corral-Ramos C, Barrios R, Ayté J, Hidalgo E","authors_abbrev":"Corral-Ramos C et al.","pubmed_publication_date":"Feb 2022","pubmed_entrez_date":"2021-06-23","publication_year":"2022","canto_session_key":"238a7289cd7196b7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24B11.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28382430","title":"DNA Topoisomerase II modulates acetyl-regulation of cohesin-mediated chromosome dynamics.","citation":"Curr Genet 2017 Oct;63(5):923-930","abstract":"Cohesin is one of three multi-protein structural maintenance of chromosome (SMC) complexes that regulate eukaryotic chromosome dynamics. It forms a ring-shaped structure that embraces sister chromatids through interphase to promote their pairing. In preparation for mitosis, most cohesin is stripped from the chromosome arms in prophase by a poorly defined process that is associated with cohesin phosphorylation. In the fission yeast Schizosaccharomyces pombe this prophase pathway is dependent on the cohesin-related Smc5/6 complex, and this requirement is heightened in Smc5/6 hypomorphs by DNA damage, replication stress and Topoisomerase II (Top2) dysfunction. Cohesin interacts with chromosomes immediately upon mitotic exit and becomes cohesive coincident with DNA replication. Cohesiveness is promoted by acetylation of the Smc3 subunit by an acetyltransferase, known as Eso1 in the S. pombe, which counteracts the anti-cohesive function(s) of the cohesin regulators Pds5 and Wpl1. We recently showed that Eso1 and Smc5/6 antagonize each other, and concurrent inactivation restores sister chromatid separation following genotoxic stress. Here, we have investigated the relationship between Top2 and Eso1 in successful completion of mitosis. We observe that partial inactivation of both results in a synthetic lethal mitotic block, but this is not overcome by deleting pds5 or wpl1. However, analysis of both acetyl-blocking and mimetic mutations in Smc3 indicates that the cycling of cohesin acetyl-regulation is more important than acetyl-status per se, highlighting the non-linear nature of the cohesin cycle.","doi":"10.1007/s00294-017-0691-x","authors":"Lin SJ, O'Connell MJ","authors_abbrev":"Lin SJ et al.","pubmed_publication_date":"Oct 2017","pubmed_entrez_date":"2017-04-07","publication_year":"2017","canto_session_key":"7ea889fb240a2d21","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-04-08 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.02","SPCC5E4.06","SPBC428.17c","SPBC1A4.03c","SPBC16A3.11","SPAC10F6.09c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:26804377","title":"The architecture of the Schizosaccharomyces pombe CCR4-NOT complex.","citation":"Nat Commun 2016 Jan 25;7:10433","abstract":"CCR4-NOT is a large protein complex present both in cytoplasm and the nucleus of eukaryotic cells. Although it is involved in a variety of distinct processes related to expression of genetic information such as poly(A) tail shortening, transcription regulation, nuclear export and protein degradation, there is only fragmentary information available on some of its nine subunits. Here we show a comprehensive structural characterization of the native CCR4-NOT complex from Schizosaccharomyces pombe. Our cryo-EM 3D reconstruction of the complex, combined with techniques such as immunomicroscopy, RNA-nanogold labelling, docking of the available high-resolution structures and models of different subunits and domains, allow us to propose its full molecular architecture. We locate all functionally defined domains endowed with deadenylating and ubiquitinating activities, the nucleus-specific RNA-interacting subunit Mmi1, as well as surfaces responsible for protein-protein interactions. This information provides insight into cooperation of the different CCR4-NOT complex functions.","doi":"10.1038/ncomms10433","authors":"Ukleja M, Cuellar J, Siwaszek A, Kasprzak JM, Czarnocki-Cieciura M, Bujnicki JM, Dziembowski A, Valpuesta JM","authors_abbrev":"Ukleja M et al.","pubmed_publication_date":"25 Jan 2016","pubmed_entrez_date":"2016-01-26","publication_year":"2016","canto_session_key":"0c6c2b02f813ffc1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-12-12 19:10:08","canto_approved_date":"2026-06-19 15:39:34","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-12-12 19:09:24","canto_added_date":"2016-01-27 01:15:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Pascal Car,e","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29B12.06c","SPCC18.06c","SPAC20G8.06","SPAC16C9.04c","SPCC4G3.15c","SPCC736.12c","SPCC31H12.08c","SPAC1B3.05"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2016-12-12"},{"uniquename":"PMID:1704128","title":"Cloning by differential screening of a Xenopus cDNA coding for a protein highly homologous to cdc2.","citation":"Proc Natl Acad Sci U S A 1991 Feb 01;88(3):1039-43","abstract":"Fertilization of Xenopus laevis eggs triggers a period of rapid cell division comprising 12 nearly synchronous mitoses. Protein synthesis is required for these divisions, and new proteins appear after fertilization. Others proteins however, which are synthesized in the unfertilized egg, are no longer made in the early embryo. To identify such proteins, a differential screen of an egg cDNA library gave nine clones corresponding to mRNAs that are deadenylylated soon after fertilization. The sequence of one of these clones (Eg1) revealed a high homology to p34cdc2, the kinase subunit of maturation-promoting factor. Only 12 amino acids in the deduced amino acid sequence were unique to Eg1 when its sequence was compared to all other known examples of cdc2. Despite this strong similarity, however, Eg1 was unable to complement a yeast cdc2- mutant in Schizosaccharomyces pombe or a cdc28 mutant of Saccharomyces cerevisiae. Four Eg1 transcripts, two major and two minor, were found in Xenopus oocytes and early embryos. These RNAs appeared very early (stage I) in oogenesis and their level remained constant until the midblastula transition, at which time they declined. Eg1 RNA is found in the poly(A)+ fraction of oocytes only between the time of meiotic maturation and fertilization--that is to say, in the unfertilized egg. At fertilization the RNA loses its poly(A) tail and at the same time leaves the polyribosomes.","authors":"Paris J, Le Guellec R, Couturier A, Le Guellec K, Omilli F, Camonis J, MacNeill S, Philippe M","authors_abbrev":"Paris J et al.","pubmed_publication_date":"01 Feb 1991","pubmed_entrez_date":"1991-02-01","publication_year":"1991","canto_session_key":"374cc0e0716c87be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 12:18:27","canto_session_submitted_date":"2012-03-03 12:18:07","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:30736681","title":"eGFRD in all dimensions.","citation":"J Chem Phys 2019 Feb 07;150(5):054108","abstract":"Biochemical reactions often occur at low copy numbers but at once in crowded and diverse environments. Space and stochasticity therefore play an essential role in biochemical networks. Spatial-stochastic simulations have become a prominent tool for understanding how stochasticity at the microscopic level influences the macroscopic behavior of such systems. While particle-based models guarantee the level of detail necessary to accurately describe the microscopic dynamics at very low copy numbers, the algorithms used to simulate them typically imply trade-offs between computational efficiency and biochemical accuracy. eGFRD (enhanced Green's Function Reaction Dynamics) is an exact algorithm that evades such trade-offs by partitioning the N-particle system into M ≤ N analytically tractable one- and two-particle systems; the analytical solutions (Green's functions) then are used to implement an event-driven particle-based scheme that allows particles to make large jumps in time and space while retaining access to their state variables at arbitrary simulation times. Here we present \"eGFRD2,\" a new eGFRD version that implements the principle of eGFRD in all dimensions, thus enabling efficient particle-based simulation of biochemical reaction-diffusion processes in the 3D cytoplasm, on 2D planes representing membranes, and on 1D elongated cylinders representative of, e.g., cytoskeletal tracks or DNA; in 1D, it also incorporates convective motion used to model active transport. We find that, for low particle densities, eGFRD2 is up to 6 orders of magnitude faster than conventional Brownian dynamics. We exemplify the capabilities of eGFRD2 by simulating an idealized model of Pom1 gradient formation, which involves 3D diffusion, active transport on microtubules, and autophosphorylation on the membrane, confirming recent experimental and theoretical results on this system to hold under genuinely stochastic conditions.","doi":"10.1063/1.5064867","authors":"Sokolowski TR, Paijmans J, Bossen L, Miedema T, Wehrens M, Becker NB, Kaizu K, Takahashi K, Dogterom M, Ten Wolde PR","authors_abbrev":"Sokolowski TR et al.","pubmed_publication_date":"07 Feb 2019","pubmed_entrez_date":"2019-02-10","publication_year":"2019","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2019-03-09 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27012670","title":"Recognition of Poly-Ubiquitins by the Proteasome through Protein Refolding Guided by Electrostatic and Hydrophobic Interactions.","citation":"J Phys Chem B 2016 Aug 25;120(33):8137-46","abstract":"Specificity of protein degradation by cellular proteasomes comes from tetra-ubiquitin recognition. We carry out molecular dynamics simulations to characterize how the ubiquitin receptor Rpn10 recognizes in the 26S proteasome K48-linked tetra-ubiquitin. In the binding pose, ubiquitin and Rpn10 interact primarily through hydrophobic patches. However, K48-linked tetra-ubiquitin mostly assumes a closed form in solution prior to binding, in which its hydrophobic patches are not exposed to solvent. Likewise, the hydrophobic ubiquitin interacting motifs (UIMs) of Rpn10 are mostly protected prior to binding. As a result, ubiquitin recognition in the proteasome requires refolding of both K48-linked tetra-ubiquitin and Rpn10. Simulations suggest that conserved complementary electrostatic patterns of Rpn10 and ubiquitins guide protein association (stage 1 in the recognition process), which induces refolding (stage 2), and then facilitates formation of hydrophobic contacts (stage 3). The simulations also explain why Rpn10 has a higher affinity for K48-linked tetra-ubiquitin than for mono-ubiquitin and K48-linked di- and tri-ubiquitins. Simulation results expand on the current view that the flexible arm of Rpn10 acts as an extended fragment of α-helices and flexible coils in the recognition process.","doi":"10.1021/acs.jpcb.6b01327","authors":"Zhang Y, Vuković L, Rudack T, Han W, Schulten K","authors_abbrev":"Zhang Y et al.","pubmed_publication_date":"25 Aug 2016","pubmed_entrez_date":"2016-03-26","publication_year":"2016","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-04-22 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35512546","title":"Structural insights reveal the specific recognition of meiRNA by the Mei2 protein.","citation":"J Mol Cell Biol 2022 Sep 19;14(5)","abstract":"In the fission yeast Schizosaccharomyces pombe, Mei2, an RNA-binding protein essential for entry into meiosis, regulates meiosis initiation. Mei2 binds to a specific non-coding RNA species, meiRNA, and accumulates at the sme2 gene locus, which encodes meiRNA. Previous research has shown that the Mei2 C-terminal RNA recognition motif (RRM3) physically interacts with the meiRNA 5' region in vitro and stimulates meiosis in vivo. However, the underlying mechanisms still remain elusive. We first employed an in vitro crosslinking and immunoprecipitation sequencing (CLIP-seq) assay and demonstrated a preference for U-rich motifs of meiRNA by Mei2 RRM3. We then solved the crystal structures of Mei2 RRM3 in the apo form and complex with an 8mer RNA fragment, derived from meiRNA, as detected by in vitro CLIP-seq. These results provide structural insights into the Mei2 RRM3-meiRNA complex and reveal that Mei2 RRM3 binds specifically to the UUC(U) sequence. Furthermore, a structure-based Mei2 mutation, Mei2F644A causes defective karyogamy, suggesting an essential role of the RNA-binding ability of Mei2 in regulating meiosis.","doi":"10.1093/jmcb/mjac029","authors":"Shen S, Jian Y, Cai Z, Li F, Lv M, Liu Y, Wu J, Fu C, Shi Y","authors_abbrev":"Shen S et al.","pubmed_publication_date":"19 Sep 2022","pubmed_entrez_date":"2022-05-05","publication_year":"2022","canto_session_key":"5c8e5c615d0b3d1d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-17 16:53:31","canto_approved_date":"2025-05-28 15:13:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 16:53:25","canto_added_date":"2022-05-07 00:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.17","SPAC27D7.03c","SPNCRNA.103"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-02-17","pdb_entries":[{"pdb_id":"7eiu","gene_chains":[{"gene_uniquename":"SPAC27D7.03c","chain":"A/B","position":"580-733"}],"title":"Crystal structure of Mei2 RRM3 in complex with 8mer meiRNA","entry_authors":"Shen SY,Lv MQ","entry_authors_abbrev":"Shen SY et al.","reference_uniquename":"PMID:35512546","experimental_method":"X-ray","resolution":"2.349"},{"pdb_id":"7eio","gene_chains":[{"gene_uniquename":"SPAC27D7.03c","chain":"A/B","position":"580-733"}],"title":"Crystal Structure of Mei2 RRM3","entry_authors":"Shen SY,Li FD","entry_authors_abbrev":"Shen SY et al.","reference_uniquename":"PMID:35512546","experimental_method":"X-ray","resolution":"1.895"}]},{"uniquename":"PMID:21695638","title":"A fission yeast-based platform for phosphodiesterase inhibitor HTSs and analyses of phosphodiesterase activity.","citation":"Handb Exp Pharmacol 2011;(204):135-49","abstract":"Fission yeast strains have been engineered so that their growth behavior reflects the activity of heterologous cyclic nucleotide phosphodiesterases (PDEs). These strains can be used in High-Throughput Screens (HTSs) for PDE inhibitors that possess \"drug-like\" characteristics, displaying activity in a growth stimulation assay over a 48-h period. Through three generations of development, a collection of strains expressing 10 of the 11 mammalian PDE families that is appropriate for small molecule inhibitor screening has been generated in our laboratory. Strains unable to synthesize cyclic nucleotides allow characterization of PDE activity in that the enzyme's potency is reflected in the amount of either cAMP or cGMP that must be added to the growth medium to stimulate cell growth. In the future, this system could be used to screen cDNA libraries for biological regulators of target PDEs and for the construction of strains that co-express PDEs and associated regulatory proteins to facilitate molecular and genetic studies of their functions and, in particular, to identify whether different PDE-partner protein complexes show distinct patterns of inhibitor sensitivity.","doi":"10.1007/978-3-642-17969-3_5","authors":"Demirbas D, Ceyhan O, Wyman AR, Hoffman CS","authors_abbrev":"Demirbas D et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-06-23","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31904835","title":"Reduced Translational Efficiency of Eukaryotic Genes after Duplication Events.","citation":"Mol Biol Evol 2020 May 01;37(5):1452-1461","abstract":"Control of gene expression has been found to be predominantly determined at the level of protein translation. However, to date, reduced expression from duplicated genes in eukaryotes for dosage maintenance has only been linked to transcriptional control involving epigenetic mechanisms. Here, we hypothesize that dosage maintenance following gene duplication also involves regulation at the protein level. To test this hypothesis, we compared transcriptome and proteome data of yeast models, Saccharomyces cerevisiae and Schizosaccharomyces pombe, and worm models, Caenorhabditis elegans and Caenorhabditis briggsae, to investigate lineage-specifically duplicated genes. Duplicated genes in both eukaryotic models exhibited a reduced protein-to-mRNA abundance ratio. Moreover, dosage sensitive genes, represented by genes encoding protein complex subunits, reduced their protein-to-mRNA abundance ratios more significantly than the other genes after duplication events. An analysis of ribosome profiling (Ribo-Seq) data further showed that reduced translational efficiency was more prominent for dosage sensitive genes than for the other genes. Meanwhile, no difference in protein degradation rate was associated with duplication events. Translationally repressed duplicated genes were also more likely to be inhibited at the level of transcription. Taken together, these results suggest that translation-mediated dosage control is partially contributed by natural selection and it enhances transcriptional control in maintaining gene dosage after gene duplication events during eukaryotic genome evolution.","doi":"10.1093/molbev/msz309","authors":"Chang AY, Liao BY","authors_abbrev":"Chang AY et al.","pubmed_publication_date":"01 May 2020","pubmed_entrez_date":"2020-01-07","publication_year":"2020","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8462843","title":"Meiotic mismatch repair quantified on the basis of segregation patterns in Schizosaccharomyces pombe.","citation":"Genetics 1993 Apr;133(4):815-24","abstract":"Hybrid DNA with mismatched base pairs is a central intermediate of meiotic recombination. Mismatch repair leads either to restoration or conversion, while failure of repair results in postmeiotic segregation (PMS). The behavior of three G to C transversions in one-factor crosses with the wild-type alleles is studied in Schizosaccharomyces pombe. They lead to C/C and G/G mismatches and are compared with closely linked mutations yielding other mismatches. A method is presented for the detection of PMS in random spores. The procedure yields accurate PMS frequencies as shown by comparison with tetrad data. A scheme is presented for the calculation of the frequency of hybrid DNA formation and the efficiency of mismatch repair. The efficiency of C/C repair in S. pombe is calculated to be about 70%. Other mismatches are repaired with close to 100% efficiency. These results are compared with data published on mutations in Saccharomyces cerevisiae and Ascobolus immersus. This study forms the basis for the detailed analysis of the marker effects caused by G to C transversions in two-factor crosses.","authors":"Schär P, Munz P, Kohli J","authors_abbrev":"Schär P et al.","pubmed_publication_date":"Apr 1993","pubmed_entrez_date":"1993-04-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15353274","title":"DNA replication licensing.","citation":"Front Biosci 2004 Sep 01;9:2115-32","abstract":"The DNA replication licensing system ensures that chromosomal DNA is replicated precisely once before cell division occurs. A DNA helicase must be loaded on origin DNA for replication to initiate. Considerable evidence suggests that the MCM complex acts as a replicative helicase in eukaryotes. When the MCM complex is loaded on the chromatin, the replication origin is formally defined as being licensed for replication. Licensing takes place several hours before origins are activated to undergo replication in S-phase. Genetic and biochemical studies show that the licensing process is well conserved in eukaryotes. Cyclin Dependent Kinases (CDKs), the master regulators of the cell cycle, coordinate the initiation of the two key cell cycle events, replication of DNA and its segregation at mitosis. Eukaryotes have developed complex regulatory mechanisms to ensure that origin licensing is coordinated with these events so that genome integrity is preserved during successive cell divisions.","authors":"Nishitani H, Lygerou Z","authors_abbrev":"Nishitani H et al.","pubmed_publication_date":"01 Sep 2004","pubmed_entrez_date":"2004-09-09","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32319721","title":"Pyruvate kinase variant of fission yeast tunes carbon metabolism, cell regulation, growth and stress resistance.","citation":"Mol Syst Biol 2020 Apr;16(4):e9270","abstract":"Cells balance glycolysis with respiration to support their metabolic needs in different environmental or physiological contexts. With abundant glucose, many cells prefer to grow by aerobic glycolysis or fermentation. Using 161 natural isolates of fission yeast, we investigated the genetic basis and phenotypic effects of the fermentation-respiration balance. The laboratory and a few other strains depended more on respiration. This trait was associated with a single nucleotide polymorphism in a conserved region of Pyk1, the sole pyruvate kinase in fission yeast. This variant reduced Pyk1 activity and glycolytic flux. Replacing the \"low-activity\" pyk1 allele in the laboratory strain with the \"high-activity\" allele was sufficient to increase fermentation and decrease respiration. This metabolic rebalancing triggered systems-level adjustments in the transcriptome and proteome and in cellular traits, including increased growth and chronological lifespan but decreased resistance to oxidative stress. Thus, low Pyk1 activity does not lead to a growth advantage but to stress tolerance. The genetic tuning of glycolytic flux may reflect an adaptive trade-off in a species lacking pyruvate kinase isoforms.","doi":"10.15252/msb.20199270","authors":"Kamrad S, Grossbach J, Rodríguez-López M, Mülleder M, Townsend S, Cappelletti V, Stojanovski G, Correia-Melo C, Picotti P, Beyer A, Ralser M, Bähler J","authors_abbrev":"Kamrad S et al.","pubmed_publication_date":"Apr 2020","pubmed_entrez_date":"2020-04-23","publication_year":"2020","canto_session_key":"e630ab034081e15c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Stephan Kamrad","canto_first_approved_date":"2020-05-06 13:50:35","canto_approved_date":"2021-04-30 18:19:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-04-29 21:42:34","canto_added_date":"2020-04-24 00:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":12,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Stephan Kamrad","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4H3.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2020-05-06"},{"uniquename":"PMID:7646493","title":"Characterization of a novel Schizosaccharomyces pombe multidrug resistance transporter conferring brefeldin A resistance.","citation":"Biochem Biophys Res Commun 1995 Aug 15;213(2):410-8","abstract":"Brefeldin A disrupts protein secretion and causes the redistribution of the Golgi complex to endoplasmic reticulum in both mammalian cells and wild type Schizosaccharomyces pombe. We have previously isolated six different genes that, when present in multiple copies, confer brefeldin A resistance to wild type S. pombe. Here we present the characterization of one of these genes, hba2, which encodes a novel S. pombe protein that shares significant sequence similarity to members of the ATP-binding cassette superfamily of transport proteins. Examination of hba2 expression determined that this gene is overexpressed in mutant strains resistant to brefeldin A due to mutations in the negative regulator crm1 (bar1) gene or the bar2 gene. The increase of hba2 expression was independent of the pap1 transcription factor which is repressed by wild type crm1. These results suggest that crm1 negatively regulates multiple transcription factors including one that modulates hba2 transcription.","authors":"Turi TG, Rose JK","authors_abbrev":"Turi TG et al.","pubmed_publication_date":"15 Aug 1995","pubmed_entrez_date":"1995-08-15","publication_year":"1995","canto_session_key":"4b907e180fe3b4ab","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-06-06 15:24:56","canto_approved_date":"2022-02-07 14:55:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-04-24 15:27:37","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPCC18B5.01c","SPAC1805.17"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2013-06-06"},{"uniquename":"PMID:10874035","title":"One of two genes encoding glycyl-tRNA synthetase in Saccharomyces cerevisiae provides mitochondrial and cytoplasmic functions.","citation":"J Biol Chem 2000 Sep 08;275(36):27681-8","abstract":"In the yeast Saccharomyces cerevisiae, two genes (GRS1 and GRS2) encode glycyl-tRNA synthetase (GlyRS1 and GlyRS2, respectively). 59% of the sequence of GlyRS2 is identical to that of GlyRS1. Others have proposed that GRS1 and GRS2 encode the cytoplasmic and mitochondrial enzymes, respectively. In this work, we show that GRS1 encodes both functions, whereas GRS2 is dispensable. In addition, both cytoplasmic and mitochondrial phenotypes of the knockout allele of GRS1 in S. cerevisiae are complemented by the expression of the only known gene for glycyl-tRNA synthetase in Schizosaccharomyces pombe. Thus, a single gene for glycyl-tRNA synthetase likely encodes both cytoplasmic and mitochondrial activities in most or all yeast. Phylogenetic analysis shows that GlyRS2 is a predecessor of all yeast GlyRS homologues. Thus, GRS1 appears to be the result of a duplication of GRS2, which itself is pseudogene-like.","authors":"Turner RJ, Lovato M, Schimmel P","authors_abbrev":"Turner RJ et al.","pubmed_publication_date":"08 Sep 2000","pubmed_entrez_date":"2000-06-30","publication_year":"2000","canto_session_key":"5f4a2a8111128bed","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-04 15:10:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-04 15:09:52","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3F10.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-04"},{"uniquename":"PMID:23099646","title":"The DYRK1A gene is a cause of syndromic intellectual disability with severe microcephaly and epilepsy.","citation":"J Med Genet 2012 Dec;49(12):731-6","abstract":"DYRK1A plays different functions during development, with an important role in controlling brain growth through neuronal proliferation and neurogenesis. It is expressed in a gene dosage dependent manner since dyrk1a haploinsufficiency induces a reduced brain size in mice, and DYRK1A overexpression is the candidate gene for intellectual disability (ID) and microcephaly in Down syndrome. We have identified a 69 kb deletion including the 5' region of the DYRK1A gene in a patient with growth retardation, primary microcephaly, facial dysmorphism, seizures, ataxic gait, absent speech and ID. Because four patients previously reported with intragenic DYRK1A rearrangements or 21q22 microdeletions including only DYRK1A presented with overlapping phenotypes, we hypothesised that DYRK1A mutations could be responsible for syndromic ID with severe microcephaly and epilepsy.\nThe DYRK1A gene was studied by direct sequencing and quantitative PCR in a cohort of 105 patients with ID and at least two symptoms from the Angelman syndrome spectrum (microcephaly < -2.5 SD, ataxic gait, seizures and speech delay).\nWe identified a de novo frameshift mutation (c.290_291delCT; p.Ser97Cysfs*98) in a patient with growth retardation, primary severe microcephaly, delayed language, ID, and seizures.\nThe identification of a truncating mutation in a patient with ID, severe microcephaly, epilepsy, and growth retardation, combined with its dual function in regulating the neural proliferation/neuronal differentiation, adds DYRK1A to the list of genes responsible for such a phenotype. ID, microcephaly, epilepsy, and language delay are the more specific features associated with DYRK1A abnormalities. DYRK1A studies should be discussed in patients presenting such a phenotype.","doi":"10.1136/jmedgenet-2012-101251","authors":"Courcet JB, Faivre L, Malzac P, Masurel-Paulet A, Lopez E, Callier P, Lambert L, Lemesle M, Thevenon J, Gigot N, Duplomb L, Ragon C, Marle N, Mosca-Boidron AL, Huet F, Philippe C, Moncla A, Thauvin-Robinet C","authors_abbrev":"Courcet JB et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-10-27","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC823.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7908655","title":"Effects of the physiological state of five yeast species on H(+)-ATPase-related processes.","citation":"Folia Microbiol (Praha) 1993;38(6):467-72","abstract":"Effects of starvation and glucose preincubation on membrane potential, ATPase-mediated acidification and glutamic acid transport were studied in yeast species Saccharomyces cerevisiae, Schizosaccharomyces pombe, Dipodascus magnusii, Lodderomyces elongisporus and Rhodotorula gracilis. The membrane potential was highest after preincubation with glucose in all species but L. elongisporus and R. gracilis. In all cases the membranes were depolarized in the presence of 20 mmol/L KCl and hyperpolarized with 50 mumol/L diethylstilbestrol (DES). The extracellular acidification caused by addition of glucose was highest after preincubation with glucose in all cases except in R. gracilis where there was none. In all cases except in R. gracilis addition of KCl caused a marked increase in the acidification rate. Addition of DES with glucose caused a large decrease in rate in S. cerevisiae but had much less effect on the other species. Transport of glutamic acid was clearly increased after pretreatment with glucose in S. cerevisiae, S. pombe and D. magnusii (mainly due to enhanced synthesis of the carrier) but actually decreased in R. gracilis and L. elongisporus. Addition of DES had an inhibitory effect in all species but much more pronounced in S. cerevisiae and S. pombe than in others. In general, both the acidification and the transport of glutamate were enhanced after preincubation with glucose but much more so in the semianaerobic species, such as S. cerevisiae, than in the strict aerobes (R. gracilis) where the effect was occasionally negative. There was no relationship between the ATPase-mediated acidification and the membrane potential.","authors":"Kotyk A, Georghiou G","authors_abbrev":"Kotyk A et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:992030","title":"The genetic complexity of Schizosacćharomyces pombe mitochondrial DNA.","citation":"FEBS Lett 1976 Oct 15;69(1):211-5","abstract":"","authors":"Tabak HF, Weijers PJ","authors_abbrev":"Tabak HF et al.","pubmed_publication_date":"15 Oct 1976","pubmed_entrez_date":"1976-10-15","publication_year":"1976","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20002499","title":"High density of weak replication origins in a 75-kb region of chromosome 2 of fission yeast.","citation":"Genes Cells 2010 Jan;15(1):1-12","abstract":"Using a two-dimensional gel electrophoresis origin mapping technique and cell synchronization, we have studied replication timing and mapped origins in a 75-kb region of chromosome 2 of Schizosaccharomyces pombe. Three of the five mapped origins are moderately active and the other two are very weak. DNA fragments containing the three moderately active origins and one weak origin are ARS-positive whereas that containing the other weak origin is ARS-negative. Three ARS elements reported earlier from this region appear to be inactive as chromosomal origins. The centromere-proximal 45 kb of this region replicates earlier than the telomere-proximal 30 kb. A transition from early to late replication occurs within 10 kb of the chromosomally inactive ars727, suggesting a possible role of the previously reported late-replication-enforcing region in determining chromosomal replication timing of the region. These results in conjunction with those from some other studies suggest that, in S. pombe, the actual number of potential origins may be significantly higher than previously detected in many genome-wide studies, and the relationship between ARS activity and chromosomal origin activity is not as simple as in Saccharomyces cerevisiae.","doi":"10.1111/j.1365-2443.2009.01363.x","authors":"Dubey DD, Srivastava VK, Pratihar AS, Yadava MP","authors_abbrev":"Dubey DD et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-12-17","publication_year":"2010","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12036080","title":"Alpha-glucosidase mutant catalyzes \"alpha-glycosynthase\"-type reaction.","citation":"Biosci Biotechnol Biochem 2002 Apr;66(4):928-33","abstract":"Replacement of the catalytic nucleophile Asp481 by glycine in Schizosaccharomyces pombe alpha-glucosidase eliminated the hydrolytic activity. The mutant enzyme (D481G) was found to catalyze the formation of an alpha-glucosidic linkage from beta-glucosyl fluoride and 4-nitrophenyl (PNP) alpha-glucoside to produce two kinds of PNP alpha-diglucosides, alpha-isomaltoside and alpha-maltoside. The two products were not hydrolyzed by D481G, giving 41 and 29% yields of PNP alpha-isomaltoside and alpha-maltoside, respectively. PNP monoglycosides, such as alpha-xyloside, alpha-mannoside, or beta-glucoside, acted as the substrate, but PNP alpha-galactoside and maltose could not. No detectable product was observed in the combination of alpha-glucosyl fluoride and PNP alpha-glucoside. This study is the first report on an \"alpha-glycosynthase\"-type reaction to form an alpha-glycosidic linkage.","authors":"Okuyama M, Mori H, Watanabe K, Kimura A, Chiba S","authors_abbrev":"Okuyama M et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-05-31","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8536980","title":"Active and inactive transplacement of the M26 recombination hotspot in Schizosaccharomyces pombe.","citation":"Genetics 1995 Sep;141(1):33-48","abstract":"The ade6-M26 mutation of the fission yeast Schizosaccharomyces pombe creates a meiotic recombination hotspot that elevates ade6 intragenic recombination approximately 10-15-fold. A heptanucleotide sequence including the M26 point mutation is required but not sufficient for hotspot activity. We studied the effects of plasmid and chromosomal context on M26 hotspot activity. The M26 hotspot was inactive on a multicopy plasmid containing M26 embedded within 3.0 or 5.9 kb of ade6 DNA. Random S. pombe genomic fragments totaling approximately 7 Mb did not activate the M26 hotspot on a plasmid. M26 hotspot activity was maintained when 3.0-, 4.4-, and 5.9-kb ade6-M26 DNA fragments, with various amounts of non-S. pombe plasmid DNA, were integrated at the ura4 chromosomal locus, but only in certain configurations relative to the ura4 gene and the cointegrated plasmid DNA. Several integrations created new M26-independent recombination hotspots. In all cases the non-ade6 DNA was located > 1 kb from the M26 site, and in some cases > 2 kb. Because the chromosomal context effect was transmitted over large distances, and did not appear to be mediated by a single discrete DNA sequence element, we infer that the local chromatin structure has a pronounced effect on M26 hotspot activity.","authors":"Virgin JB, Metzger J, Smith GR","authors_abbrev":"Virgin JB et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10871341","title":"Isolation of an essential Schizosaccharomyces pombe gene, prp31(+), that links splicing and meiosis.","citation":"Nucleic Acids Res 2000 Jun 01;28(11):2214-20","abstract":"We carried out a screen for mutants that arrest prior to premeiotic S phase. One of the strains we isolated contains a temperature-sensitive allele mutation in the fission yeast prp31(+) gene. The prp31-E1 mutant is defective in vegetative cell growth and in meiotic progression. It is synthetically lethal with prp6 and displays a pre-mRNA splicing defect at the restrictive temperature. We cloned the wild-type gene by complementation of the temperature-sensitive mutant phenotype. Prp31p is closely related to human and budding yeast PRP31 homologs and is likely to function as a general splicing factor in both vegetative growth and sexual differentiation.","authors":"Bishop DT, McDonald WH, Gould KL, Forsburg SL","authors_abbrev":"Bishop DT et al.","pubmed_publication_date":"01 Jun 2000","pubmed_entrez_date":"2000-06-28","publication_year":"2000","canto_session_key":"a387442f1547e80a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-29 16:09:28","canto_approved_date":"2026-01-29 17:02:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-25 13:33:13","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.12","SPBC119.13c","SPAC2G11.14","SPBC11B10.02c"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2015-09-29"},{"uniquename":"PMID:35928155","title":"Sib1, Sib2, and Sib3 proteins are required for ferrichrome-mediated cross-feeding interaction between  Schizosaccharomyces pombe  and  Saccharomyces cerevisiae .","citation":"Front Microbiol 2022;13:962853","abstract":"Although  Saccharomyces cerevisiae  is unable to produce siderophores, this fungal organism can assimilate iron bound to the hydroxamate-type siderophore ferrichrome (Fc) produced and secreted by other microbes. Fc can enter  S. cerevisiae  cells  via  Arn1. Unlike  S. cerevisiae ,  Schizosaccharomyces pombe  synthesizes and secretes Fc. The  sib1   +  and  sib2   +  genes encode, respectively, a Fc synthetase and an ornithine-N 5 -oxygenase, which are required for Fc production. When both genes were expressed in  S. pombe , cross-feeding experiments revealed that  S. cerevisiae fet3 Δ  arn1-4 Δ cells expressing Arn1 could grow in the vicinity of  S. pombe  under low-iron conditions. In contrast, deletion of  sib1   +  and  sib2   +  produced a defect in the ability of  S. pombe  to keep  S. cerevisiae  cells alive when Fc is used as the sole source of iron. Further analysis identified a gene designated  sib3   +  that encodes an N 5 -transacetylase required for Fc production in  S. pombe . The  sib3 Δ mutant strain exhibited a severe growth defect in iron-poor media, and it was unable to promote Fc-dependent growth of  S. cerevisiae  cells. Microscopic analyses of  S. pombe  cells expressing a functional Sib3-GFP protein revealed that Sib3 was localized throughout the cells, with a proportion of Sib3 being colocalized with Sib1 and Sib2 within the cytosol. Collectively, these results describe the first example of a one-way cross-feeding interaction, with  S. pombe  providing Fc that enables  S. cerevisiae  to grow when Fc is used as the sole source of iron.","doi":"10.3389/fmicb.2022.962853","authors":"Brault A, Mbuya B, Labbé S","authors_abbrev":"Brault A et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-08-05","publication_year":"2022","canto_session_key":"2947d0ab43b84b32","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-08-07 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC17G9.06c","SPAC23G3.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:21779494","title":"Ras signaling in yeast.","citation":"Genes Cancer 2011 Mar;2(3):210-5","abstract":"Since the study of yeast RAS and adenylate cyclase in the early 1980s, yeasts including budding and fission yeasts contributed significantly to the study of Ras signaling. First, yeast studies provided insights into how Ras activates downstream signaling pathways. Second, yeast studies contributed to the identification and characterization of GAP and GEF proteins, key regulators of Ras. Finally, the study of yeast provided many important insights into the understanding of C-terminal processing and membrane association of Ras proteins.","doi":"10.1177/1947601911407322","authors":"Tamanoi F","authors_abbrev":"Tamanoi F","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2011-07-23","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:57:23","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25081204","title":"Negative feedback regulation of calcineurin-dependent Prz1 transcription factor by the CaMKK-CaMK1 axis in fission yeast.","citation":"Nucleic Acids Res 2014 Sep;42(15):9573-87","abstract":"Calcium signals trigger the translocation of the Prz1 transcription factor from the cytoplasm to the nucleus. The process is regulated by the calcium-activated phosphatase calcineurin, which activates Prz1 thereby maintaining active transcription during calcium signalling. When calcium signalling ceases, Prz1 is inactivated by phosphorylation and exported to the cytoplasm. In budding yeast and mammalian cells, different kinases have been reported to counter calcineurin activity and regulate nuclear export. Here, we show that the Ca(2+)/calmodulin-dependent kinase Cmk1 is first phosphorylated and activated by the newly identified kinase CaMKK2 homologue, Ckk2, in response to Ca(2+). Then, active Cmk1 binds, phosphorylates and inactivates Prz1 transcription activity whilst at the same time cmk1 expression is enhanced by Prz1 in response to Ca(2+). Furthermore, Cdc25 phosphatase is also phosphorylated by Cmk1, inducing cell cycle arrest in response to an increase in Ca(2+). Moreover, cmk1 deletion shows a high tolerance to chronic exposure to Ca(2+), due to the lack of cell cycle inhibition and elevated Prz1 activity. This work reveals that Cmk1 kinase activated by the newly identified Ckk2 counteracts calcineurin function by negatively regulating Prz1 activity which in turn is involved in activating cmk1 gene transcription. These results are the first insights into Cmk1 and Ckk2 function in Schizosaccharomyces pombe.","doi":"10.1093/nar/gku684","authors":"Cisneros-Barroso E, Yance-Chávez T, Kito A, Sugiura R, Gómez-Hierro A, Giménez-Zaragoza D, Aligue R","authors_abbrev":"Cisneros-Barroso E et al.","pubmed_publication_date":"Sep 2014","pubmed_entrez_date":"2014-08-02","publication_year":"2014","canto_session_key":"16267d2a11f0cdbf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rosa Aligue","canto_first_approved_date":"2017-09-22 16:03:52","canto_approved_date":"2025-06-08 16:23:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-27 08:30:25","canto_added_date":"2014-08-03 00:15:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Rosa Aligue","community_curator":true,"annotation_count":29,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC4G8.13c","SPCC1919.01","SPACUNK12.02c","SPBP4H10.04","SPCC830.06","SPCC297.03"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2017-09-22"},{"uniquename":"PMID:17158862","title":"Tetraplex structure of fission yeast telomeric DNA and unfolding of the tetraplex on the interaction with telomeric DNA binding protein Pot1.","citation":"J Biochem 2007 Jan;141(1):57-68","abstract":"To understand the regulation mechanism of fission yeast telomeric DNA, we analysed the structural properties of Gn: d(GnTTAC) (n=2-6) and 4Gn: d(GnTTAC)4 (n=3 and 4), and their interaction with the single-stranded telomeric DNA binding domain of telomere-binding protein Pot1 (Pot1DBD). G4, G5 and G6 formed a parallel tetraplex in contrast with no tetraplex formation by G2 and G3. Also, 4G4 adopted only an antiparallel tetraplex in spite of a mixture of parallel and antiparallel tetraplexes of 4G3. The variety of tetraplex structures was governed by the number of consecutive guanines in a single copy and the number of repeats. The antiparallel tetraplex of 4G4 became unfolded upon the interaction with Pot1DBD. The interaction with mutant Pot1DBD proteins revealed that the ability to unfold the antiparallel tetraplex was strongly correlated with the specific binding affinity for the single-stranded telomeric DNA. The result suggests that the decrease in the free single strand upon the complex formation with Pot1DBD may shift the equilibrium from the tetraplex to the single strand, which may cause the tetraplex unfolding. Considering that the antiparallel tetraplex inhibits telomerase-mediated telomere elongation, we conclude that the ability of Pot1 to unfold the antiparallel tetraplex is required for telomerase-mediated telomere regulation.","authors":"Torigoe H, Furukawa A","authors_abbrev":"Torigoe H et al.","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2006-12-13","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30805909","title":"Yeast Expression Systems: Overview and Recent Advances.","citation":"Mol Biotechnol 2019 May;61(5):365-384","abstract":"Yeasts are outstanding hosts for the production of functional recombinant proteins with industrial or medical applications. Great attention has been emerged on yeast due to the inherent advantages and new developments in this host cell. For the production of each specific product, the most appropriate expression system should be identified and optimized both on the genetic and fermentation levels, considering the features of the host, vector and expression strategies. Currently, several new systems are commercially available; some of them are private and need licensing. The potential for secretory expression of heterologous proteins in yeast proposed this system as a candidate for the production of complex eukaryotic proteins. The common yeast expression hosts used for recombinant proteins' expression include Saccharomyces cerevisiae, Pichia pastoris, Hansenula polymorpha, Yarrowia lipolytica, Arxula adeninivorans, Kluyveromyces lactis, and Schizosaccharomyces pombe. This review is dedicated to discuss on significant characteristics of the most common methylotrophic and non-methylotrophic yeast expression systems with an emphasis on their advantages and new developments.","doi":"10.1007/s12033-019-00164-8","authors":"Baghban R, Farajnia S, Rajabibazl M, Ghasemi Y, Mafi A, Hoseinpoor R, Rahbarnia L, Aria M","authors_abbrev":"Baghban R et al.","pubmed_publication_date":"May 2019","pubmed_entrez_date":"2019-02-27","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-02-27 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24330319","title":"Fission yeast IQGAP maintains F-actin-independent localization of myosin-II in the contractile ring.","citation":"Genes Cells 2014 Feb;19(2):161-76","abstract":"During cytokinesis in many eukaryotic cells, myosin-II concentrates at the equatorial cortex with actin filaments (F-actin) and is supposed to generate forces to divide the cell into two, which is called the contractile ring (CR) hypothesis. Several lines of evidence indicate that the myosin-II is recruited independently of F-actin and interacts specifically with the equatorial F-actin. Molecular details of these mechanisms are still unknown. We used the fission yeast Schizosaccharomyces pombe to investigate the regulation of myosin-II localization. We demonstrate that the CR myosin-II was composed of F-actin-dependent and -independent fractions by simultaneously observing F-actin and myosin. The F-actin-independent fraction was visualized as cortical dots in the absence of F-actin. IQGAP Rng2, an indispensable element of CR, was implicated in maintenance of the F-actin-independent fraction of myosin-II, whereas anillin Mid1 was required for assembly but not for maintenance of the fraction. In the CR of the rng2 mutant, myosin-II was less concentrated, unstable, and nonhomogeneous, which often resulted in cytokinesis failure. These results suggest that Rng2 tethers myosin-II to the cortex along the CR independently of F-actin to provide a sufficient concentration. The robust localization of myosin-II would ensure successful cytokinesis.","doi":"10.1111/gtc.12120","authors":"Takaine M, Numata O, Nakano K","authors_abbrev":"Takaine M et al.","pubmed_publication_date":"Feb 2014","pubmed_entrez_date":"2013-12-17","publication_year":"2014","canto_session_key":"a134ad477bd53983","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22907268","title":"A quantitative fitness analysis workflow.","citation":"J Vis Exp 2012 Aug 13;(66)","abstract":"Quantitative Fitness Analysis (QFA) is an experimental and computational workflow for comparing fitnesses of microbial cultures grown in parallel(1,2,3,4). QFA can be applied to focused observations of single cultures but is most useful for genome-wide genetic interaction or drug screens investigating up to thousands of independent cultures. The central experimental method is the inoculation of independent, dilute liquid microbial cultures onto solid agar plates which are incubated and regularly photographed. Photographs from each time-point are analyzed, producing quantitative cell density estimates, which are used to construct growth curves, allowing quantitative fitness measures to be derived. Culture fitnesses can be compared to quantify and rank genetic interaction strengths or drug sensitivities. The effect on culture fitness of any treatments added into substrate agar (e.g. small molecules, antibiotics or nutrients) or applied to plates externally (e.g. UV irradiation, temperature) can be quantified by QFA. The QFA workflow produces growth rate estimates analogous to those obtained by spectrophotometric measurement of parallel liquid cultures in 96-well or 200-well plate readers. Importantly, QFA has significantly higher throughput compared with such methods. QFA cultures grow on a solid agar surface and are therefore well aerated during growth without the need for stirring or shaking. QFA throughput is not as high as that of some Synthetic Genetic Array (SGA) screening methods(5,6). However, since QFA cultures are heavily diluted before being inoculated onto agar, QFA can capture more complete growth curves, including exponential and saturation phases(3). For example, growth curve observations allow culture doubling times to be estimated directly with high precision, as discussed previously(1). Here we present a specific QFA protocol applied to thousands of S. cerevisiae cultures which are automatically handled by robots during inoculation, incubation and imaging. Any of these automated steps can be replaced by an equivalent, manual procedure, with an associated reduction in throughput, and we also present a lower throughput manual protocol. The same QFA software tools can be applied to images captured in either workflow. We have extensive experience applying QFA to cultures of the budding yeast S. cerevisiae but we expect that QFA will prove equally useful for examining cultures of the fission yeast S. pombe and bacterial cultures.","doi":"10.3791/4018","authors":"Banks AP, Lawless C, Lydall DA","authors_abbrev":"Banks AP et al.","pubmed_publication_date":"13 Aug 2012","pubmed_entrez_date":"2012-08-22","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10585713","title":"cobA, a red fluorescent transcriptional reporter for Escherichia coli, yeast, and mammalian cells.","citation":"Nat Biotechnol 1999 Dec;17(12):1175-8","abstract":"We demonstrate the use of Propionibacterium freudenreichii uroporphyrinogen III methyltransferase (cobA) as a reporter of gene expression in Escherichia coli, fission yeast, and mammalian cells. Overexpression of cobA in cells resulted in bright red fluorescence that was visualized with standard fluorescence microscopy and fluorescence-activated cell sorting analysis at the single-cell level. As with green fluorescent protein (GFP), no addition of exogenous substrate was required. When expressed in Chinese hamster ovary cells from a bicistronic transcript, cobA and GFP gave rise to fluorescence signals of similar intensity. The bright red fluorescence generated by the cobA reporter promises a better signal-to-noise ratio than blue and green fluorescent reporter systems, as autofluorescence and light scattering of cells, media, and materials are reduced in the red wavelengths.","authors":"Wildt S, Deuschle U","authors_abbrev":"Wildt S et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-12-10","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010623","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2547147","title":"The ras oncogene--an important regulatory element in lower eucaryotic organisms.","citation":"Microbiol Rev 1989 Jun;53(2):171-85","abstract":"The ras proto-oncogene in mammalian cells encodes a 21-kilodalton guanosine triphosphate (GTP)-binding protein. This gene is frequently activated in human cancer. As one approach toward understanding the mechanisms of cellular transformation by ras, the function of this gene in lower eucaryotic organisms has been studied. In the yeast Saccharomyces cerevisiae, the RAS gene products serve as essential function by regulating cyclic adenosine monophosphate metabolism. Stimulation of adenylyl cyclase is dependent not only on RAS protein complexed to GTP, but also on the CDC25 and IRA gene products, which appear to control the RAS GTP-guanosine diphosphate cycle. Although analysis of RAS biochemistry in S. cerevisiae has identified mechanisms central to RAS action, RAS regulation of adenylyl cyclase appears to be strictly limited to this particular organism. In Schizosaccharomyces pombe, Dictyostelium discoideum, and Drosophila melanogaster, ras-encoded proteins are not involved with regulation of adenylyl cyclase, similar to what is observed in mammalian cells. However, the ras gene product in these other lower eucaryotes is clearly required for appropriate responses to extracellular signals such as mating factors and chemoattractants and for normal growth and development of the organism. The identification of other GTP-binding proteins in S. cerevisiae with distinct yet essential functions underscores the fundamental importance of G-protein regulatory processes in normal cell physiology.","authors":"Gibbs JB, Marshall MS","authors_abbrev":"Gibbs JB et al.","pubmed_publication_date":"Jun 1989","pubmed_entrez_date":"1989-06-01","publication_year":"1989","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11498594","title":"Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries.","citation":"Science 2001 Aug 10;293(5532):1150-5","abstract":"Eukaryotic genomes are organized into discrete structural and functional chromatin domains. Here, we show that distinct site-specific histone H3 methylation patterns define euchromatic and heterochromatic chromosomal domains within a 47-kilobase region of the mating-type locus in fission yeast. H3 methylated at lysine 9 (H3 Lys9), and its interacting Swi6 protein, are strictly localized to a 20-kilobase silent heterochromatic interval. In contrast, H3 methylated at lysine 4 (H3 Lys4) is specific to the surrounding euchromatic regions. Two inverted repeats flanking the silent interval serve as boundary elements to mark the borders between heterochromatin and euchromatin. Deletions of these boundary elements lead to spreading of H3 Lys9 methylation and Swi6 into neighboring sequences. Furthermore, the H3 Lys9 methylation and corresponding heterochromatin-associated complexes prevent H3 Lys4 methylation in the silent domain.","authors":"Noma K, Allis CD, Grewal SI","authors_abbrev":"Noma K et al.","pubmed_publication_date":"10 Aug 2001","pubmed_entrez_date":"2001-08-11","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15889146","title":"Replication fork blockage by RTS1 at an ectopic site promotes recombination in fission yeast.","citation":"EMBO J 2005 Jun 01;24(11):2011-23","abstract":"Homologous recombination is believed to play important roles in processing stalled/blocked replication forks in eukaryotes. In accordance with this, recombination is induced by replication fork barriers (RFBs) within the rDNA locus. However, the rDNA locus is a specialised region of the genome, and therefore the action of recombinases at its RFBs may be atypical. We show here for the first time that direct repeat recombination, dependent on Rad22 and Rhp51, is induced by replication fork blockage at a site-specific RFB (RTS1) within a 'typical' genomic locus in fission yeast. Importantly, when the RFB is positioned between the direct repeat, conservative gene conversion events predominate over deletion events. This is consistent with recombination occurring without breakage of the blocked fork. In the absence of the RecQ family DNA helicase Rqh1, deletion events increase dramatically, which correlates with the detection of one-sided DNA double-strand breaks at or near RTS1. These data indicate that Rqh1 acts to prevent blocked replication forks from collapsing and thereby inducing deletion events.","authors":"Ahn JS, Osman F, Whitby MC","authors_abbrev":"Ahn JS et al.","pubmed_publication_date":"01 Jun 2005","pubmed_entrez_date":"2005-05-13","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:3861929","title":"Characterization of meiosis-deficient mutants by electron microscopy and mapping of four essential genes in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1985;200(2):252-7","abstract":"Meiosis-deficient mutants of the fission yeast Schizosaccharomyces pombe carrying mei1, mei2, mei3, mei4 and mes1 mutant alleles were characterized by electron microscopy and staining of the nucleus with 4', 6-diamidino-2-phenylindole. Zygotes of either mei1, mei2 or mei3 mutants contained one round nucleus with a single spindle pole body (SPB). These mutants were arrested before premeiotic DNA synthesis. Zygotes of mei4 mutants had one elongated nucleus containing thick electron-dense filaments (linear elements). In the mes1 mutant, the first meiotic division was completed but the SBPs did not duplicate. Modification of the SPB (outer plaque formation) was also blocked and the forespore membrane was not assembled. By haploidization, random spore and tetrad analyses, four essential genes for meiosis (mei2, mei3, mei4 and mes1) were mapped. Gene mei2 was located on chromosome I 14.2 cM distant from ura2. Gene mei3 was linked to ade7 (45.4 cM) on chromosome II. Gene mei4 was linked to cdc2 (0.6 cM) on chromosome II. Gene mes1 was linked to ura3 (25.3 cM) on chromosome I.","authors":"Shimoda C, Hirata A, Kishida M, Hashida T, Tanaka K","authors_abbrev":"Shimoda C et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_session_key":"f47fd61f4184fd2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-04-17 14:22:40","canto_approved_date":"2023-01-09 09:39:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-04 14:39:28","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPMTR.02","SPAC5D6.08c","SPBC32H8.11","SPBC119.04"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-04-17"},{"uniquename":"PMID:10835346","title":"Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3.","citation":"EMBO J 2000 Jun 01;19(11):2475-82","abstract":"Dolichol-phosphate-mannose (DPM) synthase generates mannosyl donors for glycosylphosphatidylinositols, N-glycan and protein O- and C-mannosylation. In Saccharomyces cerevisiae, this enzyme is encoded by DPM1. We reported previously that mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2 subunits, and that DPM1 requires DPM2 for its stable expression in the endoplasmic reticulum. Here we report that human DPM synthase consists of three subunits. The third subunit, DPM3, comprises 92 amino acids associated with DPM1 via its C-terminal domain and with DPM2 via its N-terminal portion. The stability of DPM3 was dependent upon DPM2. However, overexpression of DPM3 in Lec15 cells, a null mutant of DPM2, restored the biosynthesis of DPM with an increase in DPM1, indicating that DPM3 directly stabilized DPM1. Therefore, DPM2 stabilizes DPM3 and DPM3 stabilizes DPM1. DPM synthase activity was 10 times higher in the presence of DPM2, indicating that DPM2 also plays a role in the enzymatic reaction. Schizosaccharomyces pombe has proteins that resemble three human subunits; S.pombe DPM3 restored biosynthesis of DPM in Lec15 cells, indicating its orthologous relationship to human DPM3.","authors":"Maeda Y, Tanaka S, Hino J, Kangawa K, Kinoshita T","authors_abbrev":"Maeda Y et al.","pubmed_publication_date":"01 Jun 2000","pubmed_entrez_date":"2000-06-03","publication_year":"2000","canto_session_key":"e0d36e697217de2a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-01-30 16:58:33","canto_approved_date":"2020-01-30 16:58:33","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-01-30 16:58:23","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1677.02","SPAC31G5.16c","SPBC21B10.11"],"gene_count":3,"ltp_gene_count":0,"approved_date":"2020-01-30"},{"uniquename":"PMID:30635653","title":"Using BEAN-counter to quantify genetic interactions from multiplexed barcode sequencing experiments.","citation":"Nat Protoc 2019 Feb;14(2):415-440","abstract":"The construction of genome-wide mutant collections has enabled high-throughput, high-dimensional quantitative characterization of gene and chemical function, particularly via genetic and chemical-genetic interaction experiments. As the throughput of such experiments increases with improvements in sequencing technology and sample multiplexing, appropriate tools must be developed to handle the large volume of data produced. Here, we describe how to apply our approach to high-throughput, fitness-based profiling of pooled mutant yeast collections using the BEAN-counter software pipeline (Barcoded Experiment Analysis for Next-generation sequencing) for analysis. The software has also successfully processed data from Schizosaccharomyces pombe, Escherichia coli, and Zymomonas mobilis mutant collections. We provide general recommendations for the design of large-scale, multiplexed barcode sequencing experiments. The procedure outlined here was used to score interactions for ~4 million chemical-by-mutant combinations in our recently published chemical-genetic interaction screen of nearly 14,000 chemical compounds across seven diverse compound collections. Here we selected a representative subset of these data on which to demonstrate our analysis pipeline. BEAN-counter is open source, written in Python, and freely available for academic use. Users should be proficient at the command line; advanced users who wish to analyze larger datasets with hundreds or more conditions should also be familiar with concepts in analysis of high-throughput biological data. BEAN-counter encapsulates the knowledge we have accumulated from, and successfully applied to, our multiplexed, pooled barcode sequencing experiments. This protocol will be useful to those interested in generating their own high-dimensional, quantitative characterizations of gene or chemical function in a high-throughput manner.","doi":"10.1038/s41596-018-0099-1","authors":"Simpkins SW, Deshpande R, Nelson J, Li SC, Piotrowski JS, Ward HN, Yashiroda Y, Osada H, Yoshida M, Boone C, Myers CL","authors_abbrev":"Simpkins SW et al.","pubmed_publication_date":"Feb 2019","pubmed_entrez_date":"2019-01-13","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-01-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22084306","title":"CENP-A exceeds microtubule attachment sites in centromere clusters of both budding and fission yeast.","citation":"J Cell Biol 2011 Nov 14;195(4):563-72","abstract":"The stoichiometries of kinetochores and their constituent proteins in yeast and vertebrate cells were determined using the histone H3 variant CENP-A, known as Cse4 in budding yeast, as a counting standard. One Cse4-containing nucleosome exists in the centromere (CEN) of each chromosome, so it has been assumed that each anaphase CEN/kinetochore cluster contains 32 Cse4 molecules. We report that anaphase CEN clusters instead contained approximately fourfold more Cse4 in Saccharomyces cerevisiae and ~40-fold more CENP-A (Cnp1) in Schizosaccharomyces pombe than predicted. These results suggest that the number of CENP-A molecules exceeds the number of kinetochore-microtubule (MT) attachment sites on each chromosome and that CENP-A is not the sole determinant of kinetochore assembly sites in either yeast. In addition, we show that fission yeast has enough Dam1-DASH complex for ring formation around attached MTs. The results of this study suggest the need for significant revision of existing CEN/kinetochore architectural models.","doi":"10.1083/jcb.201106078","authors":"Coffman VC, Wu P, Parthun MR, Wu JQ","authors_abbrev":"Coffman VC et al.","pubmed_publication_date":"14 Nov 2011","pubmed_entrez_date":"2011-11-16","publication_year":"2011","canto_session_key":"1ea5de9821b5eaf2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-28 11:22:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 14:59:16","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"quantitative_gene_expression","file_name":"PMID_22084306_Coffman_cnp1_protein_quantitative_expression.txt"}],"genes":["SPAC589.08c","SPBC27.02c","SPBC1105.17","SPBC11C11.03"],"gene_count":4,"ltp_gene_count":0,"approved_date":"2014-08-06"},{"uniquename":"PMID:8534915","title":"Schizosaccharomyces pombe zfs1+ encoding a zinc-finger protein functions in the mating pheromone recognition pathway.","citation":"Mol Biol Cell 1995 Sep;6(9):1185-95","abstract":"We isolated the Schizosaccharomyces pombe zfs1 gene as a multicopy suppressor of the sterility caused by overexpression of a double-stranded RNase. The deduced zfs1 gene product of 404 amino acids showed similarity to a mouse growth factor-inducible nuclear protein Nup475. Its C-terminal region carried two putative zinc-fingers, both of which should be intact for the protein to be functional as the suppressor. This protein appeared to localize in nuclei. Disruption of zfs1 was not lethal but conferred deficiency in mating and sporulation. Activation of transcription in response to the mating pheromone signaling was greatly reduced in the zfs1-disrupted cells. The mating deficiency of the zfs1-disruptant was suppressed partially by overexpression of either gpa1, ras1, byr1, or byr2, which are involved in the transmission of the pheromone signal. Disruption of zfs1 reduced both hypersensitivity of the ras1Val17 mutant to the mating pheromone and uncontrolled mating response caused by mutational activation of Gpa1, the G protein alpha subunit coupled to the mating pheromone receptors. However, overexpression of zfs1 could not bypass complete loss of function of either gpa1, ras1, byr1, or byr2. These observations indicate that the function of zfs1 is involved in the mating pheromone signaling pathway, and are consistent with its function being required to fully activate a factor in this pathway, either directly or indirectly.","authors":"Kanoh J, Sugimoto A, Yamamoto M","authors_abbrev":"Kanoh J et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_session_key":"67506e3e78c72666","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-08 12:25:13","canto_approved_date":"2019-06-14 09:08:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-31 15:55:57","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11H11.04","SPBC1D7.05","SPAC13D6.02c","SPAC1D4.13","SPBC32C12.02","SPMTR.02","SPBC24C6.06","SPBC119.11c","SPBC1718.07c","SPMTR.01","SPAC17H9.09c"],"gene_count":11,"ltp_gene_count":7,"approved_date":"2015-06-08"},{"uniquename":"PMID:33654945","title":"Quantification of Mitochondrial Dynamics in Fission Yeast.","citation":"Bio Protoc 2019 Dec 05;9(23):e3450","abstract":"Mitochondria are double-membraned organelles responsible for several functions in the cell including energy production, calcium signaling, and cellular metabolism. An equilibrium between fission and fusion events of mitochondria is required for their proper functioning. Mitochondrial morphologies have been quantified in yeast using image processing modules such as MitoGraph and MitoLoc. However, the dynamics of mitochondrial fission and fusion have not been analyzed in these methods. Here, we present a method for measuring mitochondrial morphologies, as well as estimation of fission and fusion frequencies of mitochondria in individual fission yeast cells whose mitochondria are fluorescently-tagged or stained. The latter relies on counting of individual mitochondria upon signal filtering in each frame of a time-lapse. Taken together, we present a simple protocol for analyzing mitochondrial dynamics, which can easily be adopted to other model systems.","doi":"10.21769/BioProtoc.3450","authors":"Chacko LA, Ananthanarayanan V","authors_abbrev":"Chacko LA et al.","pubmed_publication_date":"05 Dec 2019","pubmed_entrez_date":"2021-03-03","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-03-05 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"TreeFam:TF106367","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:9466","HGNC:9467","SPAC4A8.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20364342","title":"Functional interactions among members of the meiotic initiation complex in fission yeast.","citation":"Curr Genet 2010 Jun;56(3):237-49","abstract":"DNA double-strand breaks (DSBs) initiate meiotic recombination in Schizosaccharomyces pombe and in other organisms. The Rec12 protein catalyzes the formation of these DSBs in concert with a multitude of accessory proteins the role of which in this process remains to be discovered. In an all-to-all yeast two-hybrid matrix analysis, we discovered new interactions among putative members of the meiotic recombination initiation complex. We found that Rec7, an axial-element associated protein with homologies to Saccharomyces cerevisiae Rec114, is interacting with Rec24. Rec7 and Rec24 also co-immunoprecipitate in S. pombe during meiosis. An amino acid change in a conserved, C-terminal phenylalanine in Rec7, F325A interrupts the interaction with Rec24. Moreover, rec7F325A shows a recombination deficiency comparable to rec7Delta. Another interaction was detected between Rec12 and Rec14, the orthologs of which in S. cerevisiae Spo11 and Ski8 interact accordingly. Amino acid changes Rec12Q308A and Rec12R309A disrupt the interaction with Rec14, like the according amino acid changes Spo11Q376A and Spo11RE377AA loose the interaction with Ski8. Both amino acid changes in Rec12 reveal a recombination deficient rec12 (-) phenotype. We propose that both Rec7-Rec24 and Rec12-Rec14 form subcomplexes of the meiotic recombination initiation complex.","doi":"10.1007/s00294-010-0296-0","authors":"Steiner S, Kohli J, Ludin K","authors_abbrev":"Steiner S et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-04-06","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPAC1002.06c","SPAC1952.15c","SPBC32F12.02","SPAC6G9.13c","SPCC1753.03c","SPBC31F10.08"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:9552390","title":"Suc1: cdc2 affinity reagent or essential cdk adaptor protein?","citation":"Prog Cell Cycle Res 1996;2:129-35","abstract":"CKS proteins, for which the original member, p13suc1, was identified as a suppressor of cdc2 alleles in S. Pombe, have long served as a reagent for the purification of p34cdc2, whereas their biological function has remained elusive. Apparently conflicting data derived from different model systems may indicate a diversity of function for these proteins. Several new observations in yeast and Xenopus egg extracts together with new structural information tends to enhance the hypothesis that CKS proteins function to alter the activity of cdc2 at several important points in the cell cycle. Here we review previous observations and recent data that suggest CKS proteins serve as adaptor proteins that modify the functions of cdc2 throughout the cell cycle.","authors":"Vogel L, Baratte B","authors_abbrev":"Vogel L et al.","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20937798","title":"Tonoplast-localized Abc2 transporter mediates phytochelatin accumulation in vacuoles and confers cadmium tolerance.","citation":"J Biol Chem 2010 Dec 24;285(52):40416-26","abstract":"Phytochelatins mediate tolerance to heavy metals in plants and some fungi by sequestering phytochelatin-metal complexes into vacuoles. To date, only Schizosaccharomyces pombe Hmt1 has been described as a phytochelatin transporter and attempts to identify orthologous phytochelatin transporters in plants and other organisms have failed. Furthermore, recent data indicate that the hmt1 mutant accumulates significant phytochelatin levels in vacuoles, suggesting that unidentified phytochelatin transporters exist in fungi. Here, we show that deletion of all vacuolar ABC transporters abolishes phytochelatin accumulation in S. pombe vacuoles and abrogates (35)S-PC(2) uptake into S. pombe microsomal vesicles. Systematic analysis of the entire S. pombe ABC transporter family identified Abc2 as a full-size ABC transporter (ABCC-type) that mediates phytochelatin transport into vacuoles. The S. pombe abc1 abc2 abc3 abc4 hmt1 quintuple and abc2 hmt1 double mutant show no detectable phytochelatins in vacuoles. Abc2 expression restores phytochelatin accumulation into vacuoles and suppresses the cadmium sensitivity of the abc quintuple mutant. A novel, unexpected, function of Hmt1 in GS-conjugate transport is also shown. In contrast to Hmt1, Abc2 orthologs are widely distributed among kingdoms and are proposed as the long-sought vacuolar phytochelatin transporters in plants and other organisms.","doi":"10.1074/jbc.M110.155408","authors":"Mendoza-Cózatl DG, Zhai Z, Jobe TO, Akmakjian GZ, Song WY, Limbo O, Russell MR, Kozlovskyy VI, Martinoia E, Vatamaniuk OK, Russell P, Schroeder JI","authors_abbrev":"Mendoza-Cózatl DG et al.","pubmed_publication_date":"24 Dec 2010","pubmed_entrez_date":"2010-10-13","publication_year":"2010","canto_session_key":"e79441aacbe75066","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-13 22:10:42","canto_approved_date":"2025-09-04 09:45:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-08 15:57:55","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.01c","SPCC737.09c","SPAC30.04c","SPAC9E9.12c","SPAC11E3.03","SPAC3H1.10","SPAC3F10.11c","SPBC359.05","SPAPB24D3.09c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-09-13"},{"uniquename":"PMID:10837231","title":"Mob1p interacts with the Sid2p kinase and is required for cytokinesis in fission yeast.","citation":"Curr Biol 2000 May 18;10(10):619-22","abstract":"A great deal is now known about how cells regulate entry into mitosis, but only recently have the mechanisms controlling exit from mitosis and cytokinesis begun to be revealed. In the budding yeast Saccharomyces cerevisiae, Mob1p interacts with the Dbf2p kinase and cells containing mutations in these genes arrest in late anaphase [1] [2]. Proteins related to Mob1p are present in both plants and animals, but information about Mob1p function has been obtained only from budding yeast. Here, we describe the identification and characterization of Mob1p from Schizosaccharomyces pombe. Mob1p associates with the Sid2p kinase and like Sid2p, Mob1p is required for the initiation of cytokinesis, but not for mitotic exit. Mob1p localizes to the spindle pole body (SPB) and to the cell-division site during cell division, suggesting that it might be involved in transducing the signal to initiate cell division from the SPB to the division site. Mob1p is required for Sid2p localization, and Mob1p localization requires the function of the cdc7, cdc11, cdc14, spg1, sid1, sid2, and sid4 genes, suggesting that together with Sid2p, Mob1p functions at the end of the signaling cascade required to regulate the onset of cytokinesis at the end of mitosis.","authors":"Hou MC, Salek J, McCollum D","authors_abbrev":"Hou MC et al.","pubmed_publication_date":"18 May 2000","pubmed_entrez_date":"2000-06-06","publication_year":"2000","canto_session_key":"566579944fc22e68","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2025-01-28 18:11:47","canto_approved_date":"2025-01-28 18:11:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-01-28 18:11:40","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC244.01c","SPAC24B11.11c","SPCC1739.11c","SPBC24C6.07","SPBC428.13c","SPBC21.06c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2025-01-28"},{"uniquename":"PMID:10467002","title":"Gene ste20 controls amiloride sensitivity and fertility in Schizosaccharomyces pombe.","citation":"Curr Genet 1999 Jul;35(6):585-92","abstract":"It has been shown previously that amiloride, a widely used diuretic drug, inhibits growth in Schizosaccharomyces pombe. Here we show that the drug also alleviates repression by various nutrients of mating and sporulation in fission yeast. We selected spontaneous mutants that are amiloride-resistant and unable to mate and sporulate. One of them defines the gene ste20. This gene has been cloned and sequenced. It codes for a putative protein of 1309 amino acids. Its sequence does not provide any clues to its function. In contrast to the wild-type, mutants defective in this gene can grow in a medium containing 40 microm amiloride, do not arrest in G(1), and do not induce ste11 expression upon nitrogen starvation and thus are sterile. In addition the ste20 mutants are methylamine-sensitive, exhibit enhanced medium acidification and are defective in the utilization of gycerol as a carbon source.","authors":"Hilti N, Baumann D, Schweingruber AM, Bigler P, Schweingruber ME","authors_abbrev":"Hilti N et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-08-31","publication_year":"1999","canto_session_key":"9dfe93e3b0ec9286","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-04-10 16:25:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-10-26 05:22:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPBC12C2.02c","SPAC27D7.03c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2012-10-26"},{"uniquename":"PMID:14574615","title":"RNA polymerase II transcription apparatus in Schizosaccharomyces pombe.","citation":"Curr Genet 2004 Jan;44(6):287-94","abstract":"Eukaryotic RNA polymerase II (Pol II) transcription apparatus is a multi-protein complex consisting of the RNA polymerase II core enzyme (12 subunits), general transcription factors, the mediator, and some other specific accessory factors with regulatory functions. After genome sequencing was completed, the fission yeast Schizosaccharomyces pombe was recognized as a good model organism to study the Pol II transcription apparatus, because most genetic methods developed with the budding yeast Saccharomyces cerevisiae are applicable but the genetic systems of Sch. pombe, including transcription, are closer to those in higher eukaryotes. Recent studies on components of the Sch. pombe basal transcription machinery not only revealed a number of properties common in other eukaryotes but also illuminated some features unique to Sch. pombe. Convergence of information from both yeasts will provide us with a more general understanding of eukaryotic transcription.","authors":"Mitsuzawa H, Ishihama A","authors_abbrev":"Mitsuzawa H et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2003-10-24","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10766807","title":"Alternative excision repair pathway of UV-damaged DNA in Schizosaccharomyces pombe operates both in nucleus and in mitochondria.","citation":"J Biol Chem 2000 Apr 21;275(16):11824-8","abstract":"The fission yeast, Schizosaccharomyces pombe, possesses a UV-damaged DNA endonuclease-dependent excision repair (UVER) pathway in addition to nucleotide excision repair pathway for UV-induced DNA damage. We examined cyclobutane pyrimidine dimer removal from the myo2 locus on the nuclear genome and the coI locus on the mitochondrial genome by the two repair pathways. While nucleotide excision repair repairs damage only on the nuclear genome, UVER efficiently removes cyclobutane pyrimidine dimers on both nuclear and mitochondrial genomes. The ectopically expressed wild type UV-damaged DNA endonuclease was localized to both nucleus and mitochondria, while modifications of N-terminal methionine codons restricted its localization to either of two organelles, suggesting an alternative usage of multiple translation initiation sites for targeting the protein to different organelles. By introducing the same mutations into the chromosomal copy of the uvde(+) gene, we selectively inactivated UVER in either the nucleus or the mitochondria. The results of UV survival experiments indicate that although UVER efficiently removes damage on the mitochondrial genome, UVER in the mitochondria hardly contributes to UV resistance of S. pombe cells. We suggest a possible UVER function in mitochondria as a backup system for other UV damage tolerance mechanisms.","authors":"Yasuhira S, Yasui A","authors_abbrev":"Yasuhira S et al.","pubmed_publication_date":"21 Apr 2000","pubmed_entrez_date":"2000-04-15","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.09c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:14654689","title":"A novel allele of fission yeast rad11 that causes defects in DNA repair and telomere length regulation.","citation":"Nucleic Acids Res 2003 Dec 15;31(24):7141-9","abstract":"Replication protein A (RPA) is a heterotrimeric single-stranded DNA-binding protein involved in DNA replication, recombination and repair. In Saccharomyces cerevisiae, several mutants in the RFA1 gene encoding the large subunit of RPA have been isolated and one of the mutants with a missense allele, rfa1-D228Y, shows a synergistic reduction in telomere length when combined with a yku70 mutation. So far, only one mutant allele of the rad11(+) gene encoding the large subunit of RPA has been reported in Schizosaccharomyces pombe. To study the role of S.pombe RPA in DNA repair and possibly in telomere maintenance, we constructed a rad11-D223Y mutant, which corresponds to the S.cerevisiae rfa1-D228Y mutant. rad11-D223Y cells were methylmethane sulfonate, hydroxyurea, UV and gamma-ray sensitive, suggesting that rad11-D223Y cells have a defect in DNA repair activity. Unlike the S.cerevisiae rfa1-D228Y mutation, the rad11-D223Y mutation itself caused telomere shortening. Moreover, Rad11-Myc bound to telomere in a ChIP assay. These results strongly suggest that RPA is directly involved in telomere maintenance.","authors":"Ono Y, Tomita K, Matsuura A, Nakagawa T, Masukata H, Uritani M, Ushimaru T, Ueno M","authors_abbrev":"Ono Y et al.","pubmed_publication_date":"15 Dec 2003","pubmed_entrez_date":"2003-12-05","publication_year":"2003","canto_session_key":"4b35693cfa0373c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-05-17 13:58:53","canto_approved_date":"2024-06-26 10:37:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-17 13:58:47","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPBC660.13c","SPCC126.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-05-17"},{"uniquename":"PMID:27308584","title":"Aurora B kinase controls the separation of centromeric and telomeric heterochromatin.","citation":"Mol Cell Oncol 2016 Mar;3(2):e1043039","abstract":"The segregation of chromosomes is coordinated at multiple levels to prevent chromosome loss, a phenotype frequently observed in cancers. We recently described an essential role for telomeres in the physical separation of chromosomes and identified Aurora B kinase as a double agent involved in the separation of centromeric and telomeric heterochromatin.","doi":"10.1080/23723556.2015.1043039","authors":"Gachet Y, Reyes C, Tournier S","authors_abbrev":"Gachet Y et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2016-06-17","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-06-18 00:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20126540","title":"Timing robustness in the budding and fission yeast cell cycles.","citation":"PLoS One 2010 Feb 01;5(2):e8906","abstract":"Robustness of biological models has emerged as an important principle in systems biology. Many past analyses of Boolean models update all pending changes in signals simultaneously (i.e., synchronously), making it impossible to consider robustness to variations in timing that result from noise and different environmental conditions. We checked previously published mathematical models of the cell cycles of budding and fission yeast for robustness to timing variations by constructing Boolean models and analyzing them using model-checking software for the property of speed independence. Surprisingly, the models are nearly, but not totally, speed-independent. In some cases, examination of timing problems discovered in the analysis exposes apparent inaccuracies in the model. Biologically justified revisions to the model eliminate the timing problems. Furthermore, in silico random mutations in the regulatory interactions of a speed-independent Boolean model are shown to be unlikely to preserve speed independence, even in models that are otherwise functional, providing evidence for selection pressure to maintain timing robustness. Multiple cell cycle models exhibit strong robustness to timing variation, apparently due to evolutionary pressure. Thus, timing robustness can be a basis for generating testable hypotheses and can focus attention on aspects of a model that may need refinement.","doi":"10.1371/journal.pone.0008906","authors":"Mangla K, Dill DL, Horowitz MA","authors_abbrev":"Mangla K et al.","pubmed_publication_date":"01 Feb 2010","pubmed_entrez_date":"2010-02-04","publication_year":"2010","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12527774","title":"The phylogenetic diversity of eukaryotic transcription.","citation":"Nucleic Acids Res 2003 Jan 15;31(2):653-60","abstract":"Eukaryotic transcription is a highly regulated process involving interactions between large numbers of proteins. To analyse the phylogenetic distribution of the components of this process, six crown eukaryote group genomes were queried with a reference set of transcription-associated (TA) proteins. On average, one in 10 proteins encoded by these genomes were found to be homologous to sequences in the reference set. Analysis of families identified using an accurate sequence clustering algorithm and containing both TA proteins and eukaryotic sequences showed that in two-thirds of the families the homologues originate from a single kingdom. Furthermore, in only 15% of the fungal-specific clusters are the homologues present in both budding and fission yeast, as compared with the metazoan-specific clusters where 53% of the homologues originate from two or more species. Families whose members comprise general transcription factor or RNA polymerase subunits exhibit a low degree of taxon specificity, suggesting that the transcription initiation complex is highly conserved. This contrasts with transcriptional regulator families, that are primarily taxon-specific, indicating proteins controlling gene activation exhibit considerable sequence diversity across the eukaryotic domain.","authors":"Coulson RM, Ouzounis CA","authors_abbrev":"Coulson RM et al.","pubmed_publication_date":"15 Jan 2003","pubmed_entrez_date":"2003-01-16","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14963023","title":"A non-chromosomal factor allows viability of Schizosaccharomyces pombe lacking the essential chaperone calnexin.","citation":"J Cell Sci 2004 Feb 29;117(Pt 6):907-18","abstract":"Calnexin is a molecular chaperone playing key roles in protein folding and the quality control of this process in the endoplasmic reticulum. We, and others, have previously demonstrated that cnx1(+), the gene encoding the calnexin homologue in Schizosaccharomyces pombe, is essential for viability. We show that a particular cnx1 mutant induces a novel mechanism allowing the survival of S. pombe cells in the absence of calnexin/Cnx1p. Calnexin independence is dominant in diploid cells and is inherited in a non-Mendelian manner. Remarkably, this survival pathway, bypassing the necessity for calnexin, can be transmitted by transformation of cell extracts into a wild-type naive strain, thus implicating a non-chromosomal factor. Nuclease and UV treatments of cells extracts did not obliterate transmission of calnexin independence by transformation. However, protease digestion of extracts did reduce the appearance of calnexin-independent cells, indicating that a protein element is required for calnexin-less viability. We discuss a model in which this calnexin-less survival mechanism would be activated and perpetuated by a protein component acting as a genetic element.","authors":"Collin P, Beauregard PB, Elagöz A, Rokeach LA","authors_abbrev":"Collin P et al.","pubmed_publication_date":"29 Feb 2004","pubmed_entrez_date":"2004-02-14","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24469396","title":"Rad51-dependent aberrant chromosome structures at telomeres and ribosomal DNA activate the spindle assembly checkpoint.","citation":"Mol Cell Biol 2014 Apr;34(8):1389-97","abstract":"The spindle assembly checkpoint (SAC) monitors defects in kinetochore-microtubule attachment or lack of tension at kinetochores and arrests cells at prometaphase. In fission yeast, the double mutant between pot1Δ and the helicase-dead point mutant of the RecQ helicase Rqh1 gene (rqh1-hd) accumulates Rad51-dependent recombination intermediates at telomeres and enters mitosis with those intermediates. Here, we found that SAC-dependent prometaphase arrest occurred more frequently in pot1Δ rqh1-hd double mutants than in rqh1-hd single mutants. SAC-dependent prometaphase arrest also occurred more frequently in rqh1-hd single mutants after cells were released from DNA replication block compared to the rqh1-hd single mutant in the absence of exogenous insult to the DNA. In both cases, Mad2 foci persisted longer than usual at kinetochores, suggesting a defect in kinetochore-microtubule attachment. In pot1Δ rqh1-hd double mutants and rqh1-hd single mutants released from DNA replication block, SAC-dependent prometaphase arrest was suppressed by the removal of the recombination or replication intermediates. Our results indicate that the accumulation of recombination or replication intermediates induces SAC-dependent prometaphase arrest, possibly by affecting kinetochore-microtubule attachment.","doi":"10.1128/MCB.01704-13","authors":"Nakano A, Masuda K, Hiromoto T, Takahashi K, Matsumoto Y, Habib AG, Darwish AG, Yukawa M, Tsuchiya E, Ueno M","authors_abbrev":"Nakano A et al.","pubmed_publication_date":"Apr 2014","pubmed_entrez_date":"2014-01-29","publication_year":"2014","canto_session_key":"471c8e95402e4fe7","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPCC1322.12c","SPCC1259.13","SPAC2G11.12","SPAC26H5.06"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:30739171","title":"Immediate visualization of recombination events and chromosome segregation defects in fission yeast meiosis.","citation":"Chromosoma 2019 Sep;128(3):385-396","abstract":"Schizosaccharomyces pombe, also known as fission yeast, is an established model for studying chromosome biological processes. Over the years, research employing fission yeast has made important contributions to our knowledge about chromosome segregation during meiosis, as well as meiotic recombination and its regulation. Quantification of meiotic recombination frequency is not a straightforward undertaking, either requiring viable progeny for a genetic plating assay, or relying on laborious Southern blot analysis of recombination intermediates. Neither of these methods lends itself to high-throughput screens to identify novel meiotic factors. Here, we establish visual assays novel to Sz. pombe for characterizing chromosome segregation and meiotic recombination phenotypes. Genes expressing red, yellow, and/or cyan fluorophores from spore-autonomous promoters have been integrated into the fission yeast genomes, either close to the centromere of chromosome 1 to monitor chromosome segregation, or on the arm of chromosome 3 to form a genetic interval at which recombination frequency can be determined. The visual recombination assay allows straightforward and immediate assessment of the genetic outcome of a single meiosis by epi-fluorescence microscopy without requiring tetrad dissection. We also demonstrate that the recombination frequency analysis can be automatized by utilizing imaging flow cytometry to enable high-throughput screens. These assays have several advantages over traditional methods for analyzing meiotic phenotypes.","doi":"10.1007/s00412-019-00691-y","authors":"Li D, Roca M, Yuecel R, Lorenz A","authors_abbrev":"Li D et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-02-11","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-02-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8408281","title":"CO2 production in cell-free extracts of fission yeast detects cell cycle changes.","citation":"J Cell Sci 1993 Jun;105 ( Pt 2):529-31","abstract":"CO2 production was followed by manometry in starved cell-free extracts of fission yeast stimulated by unstarved cell-free extracts from a synchronous culture. The degree of stimulus, measured by the lag time in CO2 production, varied markedly during the cell cycle, with a maximum for cells at about mitosis and a minimum for septated cells. Similar differences in lag time were found with unstarved extracts of cdc13.117 grown at 37 degrees C and 35 degrees C.","authors":"Novak B, Sveiczer A, Mitchison JM","authors_abbrev":"Novak B et al.","pubmed_publication_date":"Jun 1993","pubmed_entrez_date":"1993-06-01","publication_year":"1993","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10471809","title":"Tpr1, a Schizosaccharomyces pombe protein involved in potassium transport.","citation":"FEBS Lett 1999 Sep 03;457(3):363-8","abstract":"The Schizosaccharomyces pombe Tpr1 was isolated as suppressor of the Saccharomyces cerevisiae Delta trk1,2 potassium uptake deficient phenotype. Tpr1, for tetratrico peptide repeat, encodes a 1039 amino acid residues protein with several reiterated TPR units displaying significant homology to p150(TSP), a recently identified phosphoprotein of mouse, to S. cerevisiae CTR9 and to related sequences of human, Caenorhabditis elegans, Methanoccocus jannaschii and Arabidopsis thaliana. Expression of Tpr1 restored growth on 0.2 mM K(+) media, induced K(+) transport with a K(T) of 4.6 mM and resumed inward currents of -90 pA at -250 mV (pH 7.2) conducting K(+) and other alkali-metal ions. The tetratrico peptide repeat is a degenerate motif of 34 amino acids that is repeated several times within TPR-containing proteins and has been suggested to mediate protein-protein interactions. The sequence and putative binding properties of Tpr1 suggest the protein unlikely as transporter but involved in the enhancement of K(+) uptake via conventional carriers.","authors":"Lichtenberg H, Heyer M, Höfer M","authors_abbrev":"Lichtenberg H et al.","pubmed_publication_date":"03 Sep 1999","pubmed_entrez_date":"1999-09-03","publication_year":"1999","canto_session_key":"c7d58f9bfb1fff3b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-06-05 09:11:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-23 18:12:11","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27D7.14c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-11-23"},{"uniquename":"PMID:27159499","title":"Avoiding artefacts when counting polymerized actin in live cells with LifeAct fused to fluorescent proteins.","citation":"Nat Cell Biol 2016 Jun;18(6):676-83","abstract":"When tagged with a fluorescent protein, actin is not fully functional, so the LifeAct peptide fused to a fluorescent protein is widely used to localize actin filaments in live cells. However, we find that these fusion proteins have many concentration-dependent effects on actin assembly in vitro and in fission yeast cells. mEGFP-LifeAct inhibits actin assembly during endocytosis as well as assembly and constriction of the cytokinetic contractile ring. Purified mEGFP-LifeAct and LifeAct-mCherry bind actin filaments with Kd values of ∼10 μM. LifeAct-mCherry can promote actin filament nucleation and either promote or inhibit filament elongation. Both separately and together, profilin and formins suppress these effects. LifeAct-mCherry can also promote or inhibit actin filament severing by cofilin. These concentration-dependent effects mean that caution is necessary when overexpressing LifeAct fusion proteins to label actin filaments in cells. Therefore, we used low micromolar concentrations of tagged LifeAct to follow assembly and disassembly of actin filaments in cells. Careful titrations also gave an estimate of a peak of ∼190,000 actin molecules (∼500 μm) in the fission yeast contractile ring. These filaments shorten from ∼500 to ∼100 subunits as the ring constricts.","doi":"10.1038/ncb3351","authors":"Courtemanche N, Pollard TD, Chen Q","authors_abbrev":"Courtemanche N et al.","pubmed_publication_date":"Jun 2016","pubmed_entrez_date":"2016-05-10","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-05-11 00:15:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23630156","title":"In vivo probing of the temperature responses of intracellular biomolecules in yeast cells by label-free Raman microspectroscopy.","citation":"Chembiochem 2013 May 27;14(8):1001-5","abstract":"Environmental temperature is an essential physical quantity that substantially influences cell physiology by changing the equilibria and kinetics of biochemical reactions occurring in cells. Although it has been extensively used as a readily controllable parameter in genetic and biochemical research, much remains to be explored about the temperature responses of intracellular biomolecules in vivo and at the molecular level. Here we report in vivo probing, achieved with label-free Raman microspectroscopy, of the temperature responses of major intracellular components such as lipids and proteins in living fission yeast cells. The characteristic Raman band at 1602 cm(-1), which has been attributed mainly to ergosterol, showed a significant decrease (≈47 %) in intensity at elevated temperatures above 35 °C. In contrast to this high temperature sensitivity of the ergosterol Raman band, the phospholipid and protein Raman bands did not vary much with increasing culture temperature in the 26-38 °C range. This finding agrees with a previous biochemical study that showed that the initial stages of ergosterol biosynthesis in yeast are hindered by temperature elevation. Moreover, our result demonstrates that Raman microspectroscopy holds promise for elucidation of temperature-dependent cellular activities in living cells, with a high molecular specificity that the commonly used fluorescence microscopy cannot offer.","doi":"10.1002/cbic.201300096","authors":"Chiu YF, Huang CK, Shigeto S","authors_abbrev":"Chiu YF et al.","pubmed_publication_date":"27 May 2013","pubmed_entrez_date":"2013-05-01","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17015032","title":"Reinterpreting pericentromeric heterochromatin.","citation":"Curr Opin Plant Biol 2006 Dec;9(6):647-53","abstract":"In fission yeast, pericentromeric heterochromatin is directly responsible for the sister chromatid cohesion that assures accurate chromosome segregation. In plants, however, heterochromatin and chromosome segregation appear to be largely unrelated: chromosome transmission is impaired by mutations in cohesion but not by mutations that affect heterochromatin formation. We argue that the formation of pericentromeric heterochromatin is primarily a response to constraints on chromosome mechanics that disfavor the transmission of recombination events in pericentromeric regions. This effect allows pericentromeres to expand to enormous sizes by the accumulation of transposons and through large-scale insertions and inversions. Although sister chromatid cohesion is spatially limited to pericentromeric regions at mitosis and meiosis II, the cohesive domains appear to be defined independently of heterochromatin. The available data from plants suggest that sister chromatid cohesion is marked by histone phosphorylation and mediated by Aurora kinases.","authors":"Topp CN, Dawe RK","authors_abbrev":"Topp CN et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-10-04","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD116","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11988741","title":"Maintenance of replication forks and the S-phase checkpoint by Cdc18p and Orp1p.","citation":"Nat Cell Biol 2002 May;4(5):384-8","abstract":"S-phase and DNA damage checkpoint controls block the onset of mitosis when DNA is damaged or DNA replication is incomplete. It has been proposed that damaged or incompletely replicated DNA generates structures that are sensed by the checkpoint control pathway, although little is known about the structures and mechanisms involved. Here, we show that the DNA replication initiation proteins Orp1p and Cdc18p are required to induce and maintain the S-phase checkpoint in Schizosaccharomyces pombe. The presence of DNA replication structures correlates with activation of the Cds1p checkpoint protein kinase and the S-phase checkpoint pathway. By contrast, induction of the DNA damage pathway is not dependent on Orp1p or Cdc18p. We propose that the presence of unresolved replication forks, together with Orp1p and Cdc18p, are necessary to activate the Cds1p-dependent S-phase checkpoint.","authors":"Murakami H, Yanow SK, Griffiths D, Nakanishi M, Nurse P","authors_abbrev":"Murakami H et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-05-04","publication_year":"2002","canto_session_key":"f655c12afd36086c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-16 13:50:19","canto_approved_date":"2026-02-06 20:42:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-16 13:49:46","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPCC18B5.11c","SPCC1259.13","SPBC29A10.15","SPBC14C8.07c","SPBC660.14"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-07-16"},{"uniquename":"PMID:27476112","title":"Role and organization of the actin cytoskeleton during cell-cell fusion.","citation":"Semin Cell Dev Biol 2016 Dec;60:121-126","abstract":"Cell-cell fusion is a ubiquitous process that underlies fertilization and development of eukaryotes. This process requires fusogenic machineries to promote plasma membrane merging, and also relies on the organization of dedicated sub-cortical cytoskeletal assemblies. This review describes the role of actin structures, so called actin fusion foci, essential for the fusion of two distinct cell types: Drosophila myoblast cells, which fuse to form myotubes, and sexually differentiated cells of the fission yeast Schizosaccharomyces pombe, which fuse to form a zygote. I describe the respective composition and organization of the two structures, discuss their proposed role in promoting plasma membrane apposition, and consider the universality of similar structures for cell-cell fusion.","doi":"10.1016/j.semcdb.2016.07.025","authors":"Martin SG","authors_abbrev":"Martin SG","pubmed_publication_date":"Dec 2016","pubmed_entrez_date":"2016-08-01","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-08-02 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16199877","title":"Suppressors of Bir1p (Survivin) identify roles for the chromosomal passenger protein Pic1p (INCENP) and the replication initiation factor Psf2p in chromosome segregation.","citation":"Mol Cell Biol 2005 Oct;25(20):9000-15","abstract":"Fission yeast Bir1p/Cut17p/Pbh1p, the homolog of human Survivin, is a conserved chromosomal passenger protein that is required for cell division and cytokinesis. To study how Bir1p promotes accurate segregation of chromosomes, we generated and analyzed a temperature-sensitive allele, bir1-46, and carried out genetic screens to find genes that interact with bir1(+). We identified Psf2p, a component of the GINS complex required for DNA replication initiation, as a high-copy-number suppressor of the bir1-46 growth defect. Loss of Psf2p function by depletion or deletion or by use of a temperature-sensitive allele, psf2-209, resulted in chromosome missegregation that was associated with mislocalization of Bir1p. We also found that the human homolog of Psf2p, PSF2, was required for proper chromosome segregation. In addition, we observed that high-copy-number expression of Pic1p, the fission yeast homolog of INCENP (inner centromere protein), suppressed bir1-46. Pic1p exhibited a localization pattern typical of chromosomal passenger proteins. Deletion of pic1(+) caused chromosome missegregation phenotypes similar to those of bir1-46. Our data suggest that Bir1p and Pic1p act as part of a conserved chromosomal passenger complex and that Psf2p/GINS indirectly affects the localization and function of this complex in chromosome segregation, perhaps through an S-phase role in centromere replication.","authors":"Huang HK, Bailis JM, Leverson JD, Gómez EB, Forsburg SL, Hunter T","authors_abbrev":"Huang HK et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-10-04","publication_year":"2005","canto_session_key":"888814a3416fe952","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-06-30 16:17:05","canto_approved_date":"2025-09-03 15:02:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-30 16:16:52","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":32,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.13c","SPCC962.02c","SPBP4H10.21c","SPBC336.15"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2020-06-30"},{"uniquename":"PMID:11683392","title":"Flp1, a fission yeast orthologue of the s. cerevisiae CDC14 gene, is not required for cyclin degradation or rum1p stabilisation at the end of mitosis.","citation":"J Cell Sci 2001 Jul;114(Pt 14):2649-64","abstract":"In Saccharomyces cerevisiae, the phosphoprotein phosphatase Cdc14p plays a central role in exit from mitosis, by promoting B-type cyclin degradation and allowing accumulation of the cyclin-dependent kinase inhibitor Sic1p. Cdc14p is sequestered in the nucleolus during interphase, from where it is released at the end of mitosis, dependent upon mitotic exit network function. The CDC14 gene is essential and loss-of-function mutants arrest at the end of mitosis. We have identified a fission yeast orthologue of CDC14 through database searches. A Schizosaccharomyces pombe flp1 (cdc fourteen-like-phosphatase) null mutant is viable, divides at a reduced size and shows defects in septation. flp1p is not the essential effector of the S. pombe septation initiation network, but may potentiate signalling of the onset of septation. In contrast to S. cerevisiae Cdc14p, flp1p is not required for the accumulation or destruction of the B-type cyclin cdc13p, the cyclin-dependent kinase inhibitor rum1p, or for dephosphorylation of the APC/C specificity factor ste9p in G1. Like its budding yeast counterpart, flp1p is restricted to the nucleolus until mitosis, when it is dispersed through the nucleus. In contrast to S. cerevisiae Cdc14p, flp1p is also present on the mitotic spindle and contractile ring. The potential roles of flp1p in cell cycle control are discussed.","authors":"Cueille N, Salimova E, Esteban V, Blanco M, Moreno S, Bueno A, Simanis V","authors_abbrev":"Cueille N et al.","pubmed_publication_date":"Jul 2001","pubmed_entrez_date":"2001-10-31","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC244.01c","SPAC1565.06c","SPBC24C6.07","SPAC6F6.08c","SPBC21.06c","SPBC428.13c","SPAC24B11.11c","SPBC11B10.09","SPCC18B5.03","SPCC1739.11c","SPAC1782.09c"],"gene_count":11,"ltp_gene_count":11},{"uniquename":"PMID:4187862","title":"The isolation of nuclei from the yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1969 Nov 19;195(1):230-3","abstract":"","authors":"Duffus JH","authors_abbrev":"Duffus JH","pubmed_publication_date":"19 Nov 1969","pubmed_entrez_date":"1969-11-19","publication_year":"1969","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17512396","title":"Inositol pyrophosphates get the vip1 treatment.","citation":"Cell 2007 May 18;129(4):647-9","abstract":"Inositol pyrophosphates are unique signaling molecules implicated in the regulation of diverse cellular processes. Two new studies by Mulugu et al. (2007) and Lee et al. (2007) extend the biological and metabolic diversity of this class of molecules. They identify yeast Vip1 as a new inositol pyrophosphate synthase and show that the products of Vip1 activity regulate a cyclin/cyclin-dependent kinase complex.","authors":"Onnebo SM, Saiardi A","authors_abbrev":"Onnebo SM et al.","pubmed_publication_date":"18 May 2007","pubmed_entrez_date":"2007-05-22","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14637153","title":"Role of guanine nucleotide exchange factors for Rho family GTPases in the regulation of cell morphology and actin cytoskeleton in fission yeast.","citation":"Biochem Biophys Res Commun 2003 Dec 12;312(2):414-20","abstract":"Rho GTPases regulate fundamental processes including cell morphology and migration in various organisms. Guanine nucleotide exchange factor (GEF) has a crucial role in activating small GTPase by exchange GDP for GTP. In fission yeast Schizosaccharomyces pombe, six members of the Rho small GTPase family were identified and reported to be involved in cell morphology and polarized cell growth. We identified seven genes encoding Rho GEF domain from genome sequence and analyzed. Overexpressions of identified genes in cell lead to change of morphology, suggesting that all of them are involved in the regulation of cell morphology. Although all of null mutants were viable, two of seven null cells had morphology defects and five of seven displayed altered actin cytoskeleton arrangements. Most of the double mutants were viable and biochemical analysis revealed that each of GEFs bound to several small G proteins. These data suggest that identified Rho GEFs are involved in the regulation of cell morphology and share signals via small GTPase Rho family.","authors":"Iwaki N, Karatsu K, Miyamoto M","authors_abbrev":"Iwaki N et al.","pubmed_publication_date":"12 Dec 2003","pubmed_entrez_date":"2003-11-26","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03","SPAC16.01","SPAC20H4.11c","SPAC16A10.04","SPAC1F7.04","SPAC16E8.09","SPCC645.07","SPAC23C4.08"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:18053736","title":"Plants, MEN and SIN.","citation":"Plant Physiol Biochem 2008 Jan;46(1):1-10","abstract":"In fission yeast, the onset of septation is signalled through the septum initiation network (SIN) signaling pathway. Similarly, in budding yeast the onset of budding is signalled through the mitotic exit network (MEN) pathway. We previously characterized in Arabidopsis signaling elements (GTPases, kinases) closely related to the core elements (spg1p/TEM1p, cdc7p/CDC15p) of the SIN and MEN pathways. Our first results suggested that a plant signaling pathway must be used to coordinate mitotic exit with cytokinesis. This review questioned the value of such an hypothesis in a multicellular organism. The core elements (G-protein, kinase) of the SIN and MEN pathways were only detected in fungi, plants and Mycetozoa. We also noticed that AtSGP GTPase and AtMAP3Kepsilon kinase revealed two paralogues in Arabidopsis. Although Arabidopsis genes complement fission yeast mutants, and Arabidopsis proteins interact with fission yeast proteins, plants do not use these core elements to coordinate the termination of cell division with cytokinesis. Transcriptional regulation and expression data suggest a function for the plant SIN-like elements in the control of cell type specification. Exploring the evolutionary conservation of an ancient signaling pathway provides evidence that evolution has recycled regulatory elements for elaborating a new signaling avenue.","authors":"Bedhomme M, Jouannic S, Champion A, Simanis V, Henry Y","authors_abbrev":"Bedhomme M et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-12-07","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15716132","title":"Vitamin B6 compounds prevent the death of yeast cells due to menadione, a reactive oxygen generator.","citation":"Biochim Biophys Acta 2005 Feb 11;1722(1):84-91","abstract":"The antioxidant effects of natural vitamin B(6) compounds on Schizosaccharomyces pombe cells treated with menadione sodium bisulfite (water-soluble menadione and a generator of superoxide, MSB) and the mechanism underlying the function were examined with the yeast cells treated with pyridoxal 5'-phosphate. Vitamin B(6) compounds showed no ex vivo reactivity toward MBS at pH 5.5 or 7.0. The yeast cells showed no growth in the medium containing 1.0 mM MSB. The coexistence of 1.0 mM of each vitamin B(6) compound supported the growth of the yeast cells. The efficacy order was pyridoxal 5'-phosphate>/=pyridoxamine 5'-phosphate>pyridoxamine>pyridoxal>/=pyridoxine. The first three compounds showed higher antioxidant activity than vitamin C did. Pyridoxal 5'-phosphate prevented the reduction of the glutathione content in the MSB-treated cells and, in turn, suppressed the increases in peroxide and thiobarbituric acid reactive substances in the yeast cells and increased the viability of the yeast cells under oxidative stress. The antioxidant function of pyridoxal 5'-phosphate was not dependent on the phosphorelay pathway, which finally triggers the expression of the catalase gene.","authors":"Chumnantana R, Yokochi N, Yagi T","authors_abbrev":"Chumnantana R et al.","pubmed_publication_date":"11 Feb 2005","pubmed_entrez_date":"2005-02-18","publication_year":"2005","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22442086","title":"Deficiency of ATP13A2 leads to lysosomal dysfunction, α-synuclein accumulation, and neurotoxicity.","citation":"J Neurosci 2012 Mar 21;32(12):4240-6","abstract":"The autophagy-lysosomal pathway plays an important role in the clearance of long-lived proteins and dysfunctional organelles. Lysosomal dysfunction has been implicated in several neurodegenerative disorders including Parkinson's disease and related synucleinopathies that are characterized by accumulations of α-synuclein in Lewy bodies. Recent identification of mutations in genes linked to lysosomal function and neurodegeneration has offered a unique opportunity to directly examine the role of lysosomes in disease pathogenesis. Mutations in lysosomal membrane protein ATP13A2 (PARK9) cause familial Kufor-Rakeb syndrome characterized by early-onset parkinsonism, pyramidal degeneration and dementia. While previous data suggested a role of ATP13A2 in α-synuclein misfolding and toxicity, the mechanistic link has not been established. Here we report that loss of ATP13A2 in human fibroblasts from patients with Kufor-Rakeb syndrome or in mouse primary neurons leads to impaired lysosomal degradation capacity. This lysosomal dysfunction results in accumulation of α-synuclein and toxicity in primary cortical neurons. Importantly, silencing of endogenous α-synuclein attenuated the toxicity in ATP13A2-depleted neurons, suggesting that loss of ATP13A2 mediates neurotoxicity at least in part via the accumulation of α-synuclein. Our findings implicate lysosomal dysfunction in the pathogenesis of Kufor-Rakeb syndrome and suggest that upregulation of lysosomal function and downregulation of α-synuclein represent important therapeutic strategies for this disorder.","doi":"10.1523/JNEUROSCI.5575-11.2012","authors":"Usenovic M, Tresse E, Mazzulli JR, Taylor JP, Krainc D","authors_abbrev":"Usenovic M et al.","pubmed_publication_date":"21 Mar 2012","pubmed_entrez_date":"2012-03-24","publication_year":"2012","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1672.11c","SPAC29A4.19c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:17538026","title":"The nucleolar Net1/Cfi1-related protein Dnt1 antagonizes the septation initiation network in fission yeast.","citation":"Mol Biol Cell 2007 Aug;18(8):2924-34","abstract":"The septation initiation network (SIN) and mitotic exit network (MEN) signaling pathways regulate cytokinesis and mitotic exit in the yeasts Schizosaccharomyces pombe, and Saccharomyces cerevisiae, respectively. One function of these pathways is to keep the Cdc14-family phosphatase, called Clp1 in S. pombe, from being sequestered and inhibited in the nucleolus. In S. pombe, the SIN and Clp1 act as part of a cytokinesis checkpoint that allows cells to cope with cytokinesis defects. The SIN promotes checkpoint function by 1) keeping Clp1 out of the nucleolus, 2) maintaining the cytokinetic apparatus, and 3) halting the cell cycle until cytokinesis is completed. In a screen for suppressors of the SIN mutant cytokinesis checkpoint defect, we identified a novel nucleolar protein called Dnt1 and other nucleolar proteins, including Rrn5 and Nuc1, which are known to be required for rDNA transcription. Dnt1 shows sequence homology to Net1/Cfi1, which encodes the nucleolar inhibitor of Cdc14 in budding yeast. Like Net1/Cfi1, Dnt1 is required for rDNA silencing and minichromosome maintenance, and both Dnt1 and Net1/Cfi1 negatively regulate the homologous SIN and MEN pathways. Unlike Net1/Cfi1, which regulates the MEN through the Cdc14 phosphatase, Dnt1 can inhibit SIN signaling independently of Clp1, suggesting a novel connection between the nucleolus and the SIN pathway.","authors":"Jin QW, Ray S, Choi SH, McCollum D","authors_abbrev":"Jin QW et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-06-01","publication_year":"2007","canto_session_key":"083a547f8abebb96","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-25 15:12:02","canto_approved_date":"2021-02-04 17:20:07","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-10-25 12:53:07","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC4C3.05c","SPAC9G1.09","YJL076W","YKR010C","SPBC24C6.07","SPAC1782.09c","SPCC645.05c","SPBC25D12.02c","SPAC29A4.10","SPAC24B11.11c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-01-25"},{"uniquename":"PMID:34589709","title":"Antiaging and Antioxidant Bioactivities of Asteraceae Plant Fractions on the Cellular Functions of the Yeast  Schizosaccharomyces pombe .","citation":"Adv Pharmacol Pharm Sci 2021;2021:2119634","abstract":"Research on antioxidants has been gaining worldwide attention because of their essential applications for medicinal purposes. In this study, we conducted bioprospecting of six Asteraceae plants as the source of antiaging and antioxidant agents. Water and chloroform fractions from  Ageratum conyzoides  L.,  Dichrocephala integrifolia  (L.f.) Kuntze,  Galinsoga parviflora  (Cav.),  Mikania micrantha  Kunth,  Sphagneticola trilobata  (L.) Pruski, and  Synedrella nodiflora  L. were collected and assayed for their in vitro antioxidant activities and potential antiaging properties using the yeast  Schizosaccharomyces pombe  as the model organism. Based on the in vitro assay, the water fractions of  S. trilobata  showed a strong antioxidant activity. Interestingly, all treatment solutions promoted the stress tolerance phenotype of  S. pombe  to strong H 2 O 2 -induced oxidative stress conditions. Moreover, compared with the treatments without plant extract/fraction, all extract and fraction treatments, except the chloroform fractions of  A. conyzoides , promoted yeast cell longevity. Strong induction of mitochondria activity was found following the treatments with the extracts and fractions of  S. nodiflora ,  D. integrifolia , and  M. micrantha  and likely mimicked the calorie restriction-induced lifespan. Interestingly,  S. nodiflora  water fractions significantly upregulated the mRNA transcripts of the Pap1-mediated core environmental stress response, namely, ctt1 gene in  S. pombe . These data indicated that the fractions of Asteraceae plants had potential antioxidant and antiaging activities through various cellular modulations.  S. nodiflora  water fraction has been shown to have antioxidant and antiaging activities in  S. pombe , by modulating stress tolerance response, inducing mitochondrial activity, and increasing the ctt1 gene expression. Compounds analysis identified that  S. nodiflora  water fraction contained some primarily compounds including oxyphyllacinol, valine, and sugiol.","doi":"10.1155/2021/2119634","authors":"Astuti RI, Prastya ME, Batubara I, Budiarti E, Ilmiyawati A","authors_abbrev":"Astuti RI et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-09-30","publication_year":"2021","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2021-10-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29423852","title":"Antibody Pull-Down Experiments in Fission Yeast.","citation":"Methods Mol Biol 2018;1721:117-123","abstract":"Proteins act as executors for almost all kinds of cellular processes. The majority of proteins achieve their proper functions through interacting with other proteins. Knowing the binding partners of a protein is instrumental for understanding its function. The antibody pull-down method is a powerful and common approach to detect protein-protein interactions. Here, an antibody pull-down protocol is described for detecting protein-protein interactions in fission yeast Schizosaccharomyces pombe.","doi":"10.1007/978-1-4939-7546-4_11","authors":"Dong Q, Li F","authors_abbrev":"Dong Q et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12565823","title":"The kic1 kinase of schizosaccharomyces pombe is a CLK/STY orthologue that regulates cell-cell separation.","citation":"Exp Cell Res 2003 Feb 01;283(1):101-15","abstract":"The CLK/STY kinases are a family of dual-specificity protein kinases implicated in the regulation of cellular growth and differentiation. Some of the kinases in the family are shown to phosphorylate serine-arginine-rich splicing factors and to regulate pre-mRNA splicing. However, the actual cellular mechanism that regulates cell growth, differentiation, and development by CLK/STY remains unclear. Here we show that a functionally conserved CLK/STY kinase exists in Schizosaccharomyces pombe, and this orthologue, called Kic1, regulates the cell surface and septum formation as well as a late step in cytokinesis. The Kic1 protein is modified in vivo, likely by phosphorylation, suggesting that it can be involved in a control cascade. In addition, kic1(+) together with dsk1(+), which encodes a related SR-specific protein kinase, constitutes a critical in vivo function for cell growth. The results provide the first in vivo evidence for the functional conservation of the CLK/STY family through evolution from fission yeast to mammals. Furthermore, since cell division and cell-cell interaction are fundamental for the differentiation and development of an organism, the novel cellular role of kic1(+) revealed from this study offers a clue to the understanding of its counterparts in higher eukaryotes.","authors":"Tang Z, Mandel LL, Yean SL, Lin CX, Chen T, Yanagida M, Lin RJ","authors_abbrev":"Tang Z et al.","pubmed_publication_date":"01 Feb 2003","pubmed_entrez_date":"2003-02-05","publication_year":"2003","canto_session_key":"af315062024a2cc5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-05-10 16:03:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-29 13:51:04","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC530.14c","SPAC29E6.08","SPAC1D4.11c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2016-04-29"},{"uniquename":"PMID:38446663","title":"RNAP II antagonizes mitotic chromatin folding and chromosome segregation by condensin.","citation":"Cell Rep 2024 Mar 05;43(3):113901","abstract":"Condensin shapes mitotic chromosomes by folding chromatin into loops, but whether it does so by DNA-loop extrusion remains speculative. Although loop-extruding cohesin is stalled by transcription, the impact of transcription on condensin, which is enriched at highly expressed genes in many species, remains unclear. Using degrons of Rpb1 or the torpedo nuclease Dhp1 XRN2  to either deplete or displace RNAPII on chromatin in fission yeast metaphase cells, we show that RNAPII does not load condensin on DNA. Instead, RNAPII retains condensin in cis and hinders its ability to fold mitotic chromatin and to support chromosome segregation, consistent with the stalling of a loop extruder. Transcription termination by Dhp1 limits such a hindrance. Our results shed light on the integrated functioning of condensin, and we argue that a tight control of transcription underlies mitotic chromosome assembly by loop-extruding condensin.","doi":"10.1016/j.celrep.2024.113901","authors":"Lebreton J, Colin L, Chatre E, Bernard P","authors_abbrev":"Lebreton J et al.","pubmed_publication_date":"05 Mar 2024","pubmed_entrez_date":"2024-03-06","publication_year":"2024","canto_session_key":"aa909da56dd1a008","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-07 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3453113","title":"The mitotic inducer nim1+ functions in a regulatory network of protein kinase homologs controlling the initiation of mitosis.","citation":"Cell 1987 May 22;49(4):569-76","abstract":"The newly discovered fission yeast mitotic control element nim1+ (new inducer of mitosis) is the first dose-dependent mitotic inducer identified as a protein kinase homolog. Increased nim1+ expression rescues mutants lacking the mitotic inducer cdc25+ and advances cells into mitosis at a reduced cell size; loss of nim1+ delays mitosis until cells have grown to a larger size. The nim1+ gene potentially encodes a 50 kd protein that contains the consensus sequences of protein kinases. Genetic evidence indicates that nim1+ is a negative regulator of the wee1+ mitotic inhibitor, another protein kinase homolog. The combined mitotic induction activities of nim1+ and cdc25+ counteract the wee1+ mitotic inhibitor in a regulatory network that appears also to involve the cdc2+ protein kinase, which is required for mitosis.","authors":"Russell P, Nurse P","authors_abbrev":"Russell P et al.","pubmed_publication_date":"22 May 1987","pubmed_entrez_date":"1987-05-22","publication_year":"1987","canto_session_key":"e44a40b1e329db2c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-05-12 12:30:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-05 18:01:54","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC644.06c","SPCC18B5.03"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2015-03-05"},{"uniquename":"PMID:3063695","title":"Chitosan-colloidal gold complexes as polycationic probes for the detection of anionic sites by transmission and scanning electron microscopy.","citation":"Histochemistry 1988;90(3):165-75","abstract":"A new cationic colloidal gold complex has been developed for ultrastructural localization of cell surface anionic sites by transmission and scanning electron microscopy. The marker is prepared by labelling gold particles of suitable sizes (6 to 70 nm in diameter) with chitosan, a polymer of beta (1----4)-linked D-glucosamine. Using human red blood cells as a model, chitosan-gold complexes were shown to be specific for anionic sites and at pH 2 for sialic acid residues. The binding capacity of complexes of different sizes with carboxymethyl and phosphorylated celluloses was examined as a function of pH and ionic strength. The results indicated that these complexes can be used under acidic conditions as well as in physiological buffers. The complexes were further tested by transmission and scanning electron microscopy in detecting anionic sites on cells of various origins such as Escherichia coli, Lactobacillus maltaromicus, Lactobacillus reuteri, Saccharomyces cerevisiae, Saccharomyces rouxii, Schizosaccharomyces pombe, Fusarium oxysporum, Catharantus roseus.","authors":"Horisberger M, Clerc MF","authors_abbrev":"Horisberger M et al.","pubmed_publication_date":"1988","pubmed_entrez_date":"1988-01-01","publication_year":"1988","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23319050","title":"Pdc1 functions in the assembly of P bodies in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2013 Mar;33(6):1244-53","abstract":"P bodies are cytoplasmic RNA granules containing the Dcp1-Dcp2 decapping enzymes where mRNA decay can occur. Here, we describe the characterization of P bodies in the fission yeast Schizosaccharomyces pombe. Most information on the property and function of P bodies stems from studies in the distantly related budding yeast Saccharomyces cerevisiae, and Edc3 was identified as a scaffold protein required for P-body assembly. However, we found that, unlike in S. cerevisiae, fission yeast Edc3 was dispensable for P-body formation. Pdc1, a novel partner of the fission yeast decapping enzyme, with a limited similarity to plant Edc4/Varicose that is required for the assembly of P bodies, was identified (tandem affinity purification-matrix-assisted laser desorption ionization tandem mass spectrometry [TAP-MALDI MS/MS]). Pdc1 interacts with Dcp2 through its C terminus and contains a coiled-coil region for self-interaction to mediate P-body formation. In line with the model that Pdc1 cross-bridges different proteins, additional interactions can be demonstrated with components such as Edc3 and Ste13. Although Pdc1 is not required for the interaction between Dcp1 and Dcp2, our data suggest that Pdc1 acts as a functional homologue of Edc4, a third component of the decapping enzymes that is thought to be absent from fungi. Together, these results highlight the diverse P-body protein compositions between different species and might help to provide insight into their evolutionary paths.","doi":"10.1128/MCB.01583-12","authors":"Wang CY, Chen WL, Wang SW","authors_abbrev":"Wang CY et al.","pubmed_publication_date":"Mar 2013","pubmed_entrez_date":"2013-01-16","publication_year":"2013","canto_session_key":"5d9eb85117dc739f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-09 17:43:08","canto_approved_date":"2023-09-02 14:22:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-03-20 21:49:24","canto_added_date":"2013-01-22 16:06:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":52,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.21","SPAC17A5.14","HGNC:17157","SPBC776.09","SPAC20G4.08","SPAC19A8.12","SPBC18E5.11c","SPAC926.04c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-02-09"},{"uniquename":"PMID:31362198","title":"1,8-Substituted anthraquinones, anthrones and bianthrones as potential non-azole leads against fungal infections.","citation":"Bioorg Chem 2019 Oct;91:103151","abstract":"The synthesis of a variety of 1,8-substituted anthraquinones, anthrones and bianthrones and their potential as antifungal agents is evaluated. Preliminary screening against Schizosaccharomyces pombe (S. pombe), a fission yeast, and Saccharomyces cerevisiae (S. cerevisiae), a budding yeast, is reported. Both these yeast species demonstrate close homologue to a number of pathogenic fungi.","doi":"10.1016/j.bioorg.2019.103151","authors":"Jalab M, Critchley ME, Taylor CM, Lawrence CL, Smith RB","authors_abbrev":"Jalab M et al.","pubmed_publication_date":"Oct 2019","pubmed_entrez_date":"2019-07-31","publication_year":"2019","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2019-08-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1844237","title":"Spi1 GTPase interacts with RCC1 to maintain interdependency of cell cycle events.","citation":"Princess Takamatsu Symp 1991;22:145-52","abstract":"A mutant which can enter mitosis at any cell cycle stage has been isolated and characterized in fission yeast. The pim1 (premature initiation of mitosis) mutant prearrested at G1/S can develop a mitotic spindle and has tightly condensed chromosomes upon shift to the restrictive temperature. pim1-induced mitosis requires maturation promoting factor (MPF) activity, but not the essential mitotic inducer, cdc25. The pim1+ gene encodes a homolog of regulator of chromosome condensation 1 (RCC1), a regulator of onset of mitosis in mammalian cells. A multicopy suppressor of pim1, spi1, was isolated, and found to encode a 25 kDa GTPase. The primary sequence of the spi1 GTPase shows extensive identity (80%) to human TC4, whose function is unknown. The spi1/TC4 GTPase defines a novel class in the \"ras-like\" GTPase family, which is distinct from ras, rho, or ypt. Disruption of the spi1+ gene causes genomic instability in a heterozygous diploid. These genetic data suggest that pim1+ and spi1+ interact to coordinate correct entry into mitosis. Immunological experiments demonstrate that the pim1+ and spi1+ products are physically associated. Mutation in the pim1 gene results in lowered affinity of the protein for the spi1 protein in vitro, which may explain why high dosages of the spi1 protein can rescue the pim1 mutant in vivo. The pim1/spi1 complex dissociates in the presence of Mg2+ and GTP. The current data suggests that pim1+ acts as a GTP exchanger for the spi1 GTPase.","authors":"Matsumoto T, Beach D","authors_abbrev":"Matsumoto T et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18641648","title":"Dynamic transcriptome of Schizosaccharomyces pombe shown by RNA-DNA hybrid mapping.","citation":"Nat Genet 2008 Aug;40(8):977-86","abstract":"We have determined the high-resolution strand-specific transcriptome of the fission yeast S. pombe under multiple growth conditions using a novel RNA-DNA hybridization mapping (HybMap) technique. HybMap uses an antibody against an RNA-DNA hybrid to detect RNA molecules hybridized to a high-density DNA oligonucleotide tiling microarray. HybMap showed exceptional dynamic range and reproducibility, and allowed us to identify strand-specific coding, noncoding and structural RNAs, as well as previously unknown RNAs conserved in distant yeast species. Notably, we found that virtually the entire euchromatic genome (including intergenics) is transcribed, with heterochromatin dampening intergenic transcription. We identified features including large numbers of condition-specific noncoding RNAs, extensive antisense transcription, new properties of antisense transcripts and induced divergent transcription. Furthermore, our HybMap data informed the efficiency and locations of RNA splicing genome-wide. Finally, we observed strand-specific transcription islands around tRNAs at heterochromatin boundaries inside centromeres. Here, we discuss these new features in terms of organism fitness and transcriptome evolution.","doi":"10.1038/ng.196","authors":"Dutrow N, Nix DA, Holt D, Milash B, Dalley B, Westbroek E, Parnell TJ, Cairns BR","authors_abbrev":"Dutrow N et al.","pubmed_publication_date":"Aug 2008","pubmed_entrez_date":"2008-07-22","publication_year":"2008","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.1293","SPNCRNA.808","SPNCRNA.499","SPNCRNA.497","SPNCRNA.498","SPNCRNA.530","SPNCRNA.1651","SPNCRNA.942","SPNCRNA.1490"],"gene_count":9,"ltp_gene_count":0},{"uniquename":"PMID:18719285","title":"Heterochromatin integrity affects chromosome reorganization after centromere dysfunction.","citation":"Science 2008 Aug 22;321(5892):1088-91","abstract":"The centromere is essential for the inheritance of genetic information on eukaryotic chromosomes. Epigenetic regulation of centromere identity has been implicated in genome stability, karyotype evolution, and speciation. However, little is known regarding the manner in which centromere dysfunction affects the chromosomal architectures. Here we show that in the fission yeast Schizosaccharomyces pombe, the conditional deletion of the centromere produces survivors that carry either a neocentromere-acquired chromosome at the subtelomeric region or an acentric chromosome rescued by intertelomere fusion with either of the remaining chromosomes. The ratio of neocentromere formation to telomere fusion is considerably decreased by the inactivation of genes involved in RNA interference-dependent heterochromatin formation. By affecting the modes of chromosomal reorganization, the genomic distribution of heterochromatin may influence the fate of karyotype evolution.","doi":"10.1126/science.1158699","authors":"Ishii K, Ogiyama Y, Chikashige Y, Soejima S, Masuda F, Kakuma T, Hiraoka Y, Takahashi K","authors_abbrev":"Ishii K et al.","pubmed_publication_date":"22 Aug 2008","pubmed_entrez_date":"2008-08-23","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27427983","title":"Destabilized SMC5/6 complex leads to chromosome breakage syndrome with severe lung disease.","citation":"J Clin Invest 2016 Aug 01;126(8):2881-92","abstract":"The structural maintenance of chromosomes (SMC) family of proteins supports mitotic proliferation, meiosis, and DNA repair to control genomic stability. Impairments in chromosome maintenance are linked to rare chromosome breakage disorders. Here, we have identified a chromosome breakage syndrome associated with severe lung disease in early childhood. Four children from two unrelated kindreds died of severe pulmonary disease during infancy following viral pneumonia with evidence of combined T and B cell immunodeficiency. Whole exome sequencing revealed biallelic missense mutations in the NSMCE3 (also known as NDNL2) gene, which encodes a subunit of the SMC5/6 complex that is essential for DNA damage response and chromosome segregation. The NSMCE3 mutations disrupted interactions within the SMC5/6 complex, leading to destabilization of the complex. Patient cells showed chromosome rearrangements, micronuclei, sensitivity to replication stress and DNA damage, and defective homologous recombination. This work associates missense mutations in NSMCE3 with an autosomal recessive chromosome breakage syndrome that leads to defective T and B cell function and acute respiratory distress syndrome in early childhood.","doi":"10.1172/JCI82890","authors":"van der Crabben SN, Hennus MP, McGregor GA, Ritter DI, Nagamani SC, Wells OS, Harakalova M, Chinn IK, Alt A, Vondrova L, Hochstenbach R, van Montfrans JM, Terheggen-Lagro SW, van Lieshout S, van Roosmalen MJ, Renkens I, Duran K, Nijman IJ, Kloosterman WP, Hennekam E, Orange JS, van Hasselt PM, Wheeler DA, Palecek JJ, Lehmann AR, Oliver AW, Pearl LH, Plon SE, Murray JM, van Haaften G","authors_abbrev":"van der Crabben SN et al.","pubmed_publication_date":"01 Aug 2016","pubmed_entrez_date":"2016-07-19","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC645.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20601686","title":"Pot1 inactivation leads to rampant telomere resection and loss in one cell cycle.","citation":"Nucleic Acids Res 2010 Nov;38(20):6968-75","abstract":"Removal of the conserved telomere protein, Pot1, confers the immediate loss of fission yeast telomeres. This drastic phenotype has established the centrality of Pot1 for telomere maintenance but prohibited elucidation of the intermediate steps leading to telomere loss. To circumvent this problem, we have generated a conditional allele, pot1-1. We show that loss of Pot1 function during G1 leads to rapid telomere erosion during the ensuing S/G2 period. Precipitous telomere loss depends upon S-phase progression and is preceded by 5' telomeric resection. Telomere loss is accompanied by ATR- and Chk1-mediated checkpoint activation, but is not caused by checkpoint arrest.","doi":"10.1093/nar/gkq580","authors":"Pitt CW, Cooper JP","authors_abbrev":"Pitt CW et al.","pubmed_publication_date":"Nov 2010","pubmed_entrez_date":"2010-07-06","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38985524","title":"The core spindle pole body scaffold Ppc89 links the pericentrin ortholog Pcp1 to the fission yeast spindle pole body via an evolutionarily conserved interface.","citation":"Mol Biol Cell 2024 Jul 10;:mbcE24050220","abstract":"Centrosomes and spindle pole bodies (SPBs) are important for mitotic spindle formation and serve as cellular signaling platforms. Although centrosomes and SPBs differ in morphology, many mechanistic insights into centrosome function have been gleaned from SPB studies. In the fission yeast  Schizosaccharomyces pombe , the ɑ-helical protein Ppc89, identified based on its interaction with the septation initiation network scaffold Sid4, comprises the SPB core. High-resolution imaging has suggested that SPB proteins assemble on the Ppc89 core during SPB duplication, but such interactions are undefined. Here, we define a connection between Ppc89 and the essential pericentrin Pcp1. Specifically, we found that a predicted third helix within Ppc89 binds the Pcp1 PACT domain complexed with calmodulin. Ppc89 helix 3 contains similarity to PINC motifs found in the centrosomal proteins fly SAS-6 and human Cep57 and also to the  S. cerevisiae  SPB protein Spc42. These motifs bind pericentrin-calmodulin complexes and AlphaFold2 models suggest a homologous complex assembles in all four organisms. Mutational analysis of the  S. pombe  complex supports the importance of Ppc89-Pcp1 binding interface in vivo. Our studies provide insight into the core architecture of the  S. pombe  SPB and suggest an evolutionarily conserved mechanism of scaffolding pericentrin-calmodulin complexes for mitotic spindle formation.","doi":"10.1091/mbc.E24-05-0220","authors":"Chen JS, Igarashi MG, Ren L, Hanna SM, Turner LA, McDonald NA, Beckley JR, Willet AH, Gould KL","authors_abbrev":"Chen JS et al.","pubmed_publication_date":"10 Jul 2024","pubmed_entrez_date":"2024-07-10","publication_year":"2024","canto_session_key":"397b85fc97c32b6a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2024-07-30 16:52:36","canto_approved_date":"2024-09-26 09:18:23","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-07-29 15:33:19","canto_added_date":"2024-07-10 23:25:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":21,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.14","SPBC244.01c","SPAC4H3.11c","SPAC6G9.06c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2024-07-30"},{"uniquename":"PMID:10203178","title":"The effects of ionizing radiation on DNA synthesis in eukaryotic cells.","citation":"Int J Radiat Biol 1999 Mar;75(3):267-83","abstract":"To review observations of the effects of ionizing radiation on DNA synthesis in eukaryotes.\nAvailable information broadly falls into two categories: descriptions of the phenomenon, including dose response data and analysis; and, more recently, investigations utilizing genetic approaches. The down-regulation of DNA replication in the presence of radiation-induced DNA damage appears to be an active cellular response, termed the S-phase damage-sensing (SDS) checkpoint control (Larner et al. 1997). Observations on a variety of eukaryotes, including man, suggest that the regulatory controls involved are highly conserved and may additionally function in G1 and G2 checkpoint controls. Budding yeast, fission yeast and human homologues are identified.\nThe SDS checkpoint control appears to be comprised of a complex of checkpoint proteins that respond to the stalled replication complex. The replication complex is thought to signal down-regulation of the mitotic kinase, ensuring that the cell does not enter mitosis while S phase is delayed. Concomitantly, the checkpoint complex is believed to transmit a signal via two key checkpoint proteins (Rad3 and Cds1 in the fission yeast), in order to arrest further DNA synthesis initiation.","authors":"Rowley R, Phillips EN, Schroeder AL","authors_abbrev":"Rowley R et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-04-15","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17696548","title":"Synthesis and enzyme inhibitory activity of the s-nucleoside analogue of the ribitylaminopyrimidine substrate of lumazine synthase and product of riboflavin synthase.","citation":"J Org Chem 2007 Sep 14;72(19):7167-75","abstract":"Lumazine synthase and riboflavin synthase catalyze the last two steps in the biosynthesis of riboflavin. To obtain structural and mechanistic probes of these two enzymes, as well as inhibitors of potential value as antibiotics, a sulfur analogue of the pyrimidine substrate of the lumazine synthase-catalyzed reaction and product of the riboflavin synthase-catalyzed reaction was designed. Facile syntheses of the S-nucleoside 5-amino-6-(D-ribitylthio)pyrimidine-2,4(1H,3H)-dione hydrochloride (15) and its nitro precursor 5-nitro-6-(D-ribitylthio)pyrimidine-2,4(1H,3H)-dione (14) are described. These compounds were tested against lumazine synthase and riboflavin synthase obtained from a variety of microorganisms. Compounds 14 and 15 were found to be inhibitors of both riboflavin synthase and lumazine synthase. Compound 14 is an inhibitor of Bacillus subtilis lumazine synthase (Ki 26 microM), Schizosaccharomyces pombe lumazine synthase (Ki 2.0 microM), Mycobacterium tuberculosis lumazine synthase (Ki 11 microM), Escherichia coli riboflavin synthase (Ki 2.7 microM), and Mycobacterium tuberculosis riboflavin synthase (Ki 0.56 muM), while compound 15 is an inhibitor of B. subtilis lumazine synthase (Ki 2.6 microM), S. pombe lumazine synthase (Ki 0.16 microM), M. tuberculosis lumazine synthase (Ki 31 microM), E. coli riboflavin synthase (Ki 47 microM), and M. tuberculosis riboflavin synthase (Ki 2.5 microM).","authors":"Talukdar A, Illarionov B, Bacher A, Fischer M, Cushman M","authors_abbrev":"Talukdar A et al.","pubmed_publication_date":"14 Sep 2007","pubmed_entrez_date":"2007-08-19","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1651177","title":"The mitochondrial genome of Schizosaccharomyces pombe. Stimulation of intra-chromosomal recombination in Escherichia coli by the gene product of the first cox1 intron.","citation":"Curr Genet 1991 Apr;19(4):295-9","abstract":"The open reading frame of the first intron of the mitochondrial cox1 gene (cox1I1) was expressed in Escherichia coli. The putative intron-encoded protein stimulated the formation of intra-chromosomal lac(+)-recombinants about threefold. No stimulation was found when the reading frame was inserted in the opposite direction, or when it was interrupted by a deletion. The intronic open reading frame did not complement recA- or recB- mutants of E. coli. In S. pombe, elimination of this intron did not abolish homologous recombination in mitochondria. A possible role of the recombinase activity in yeast mitochondria will be discussed.","authors":"Manna F, Massardo DR, Del Giudice L, Buonocore A, Nappo AG, Alifano P, Schäfer B, Wolf K","authors_abbrev":"Manna F et al.","pubmed_publication_date":"Apr 1991","pubmed_entrez_date":"1991-04-01","publication_year":"1991","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D89110","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3063400","title":"The primary structure of the leu1+ gene of Schizosaccharomyces pombe.","citation":"Curr Genet 1988 Oct;14(4):375-9","abstract":"A DNA fragment which carries the leu1 gene encoding beta-isopropylmalate dehydrogenase in Schizosaccharomyces pombe has been isolated by complementation of an E. coli leuB mutation. This 1.5 kb DNA fragment complements not only the S. pombe leu1 mutation, but also the S. cerevisiae leu2 mutation. The nucleotide sequence of the essential part of the leu1 gene and its flanking regions was determined. This sequence contains an open reading frame of 371 codons, from which a protein having a Mr = 39,732 can be predicted. The deduced amino acid sequence and its codon usage were compared with those of the S. cerevisiae LEU2 protein. The cloned DNA will be a useful marker when transforming S. pombe.","authors":"Kikuchi Y, Kitazawa Y, Shimatake H, Yamamoto M","authors_abbrev":"Kikuchi Y et al.","pubmed_publication_date":"Oct 1988","pubmed_entrez_date":"1988-10-01","publication_year":"1988","canto_session_key":"ad32f16e1b784a23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:45:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 18:56:04","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1A4.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-25"},{"uniquename":"PMID:11777938","title":"Polo boxes and Cut23 (Apc8) mediate an interaction between polo kinase and the anaphase-promoting complex for fission yeast mitosis.","citation":"J Cell Biol 2002 Jan 07;156(1):23-8","abstract":"The fission yeast plo1(+) gene encodes a polo-like kinase, a member of a conserved family of kinases which play multiple roles during the cell cycle. We show that Plo1 kinase physically interacts with the anaphase-promoting complex (APC)/cyclosome through the noncatalytic domain of Plo1 and the tetratricopeptide repeat domain of the subunit, Cut23. A new cut23 mutation, which specifically disrupts the interaction with Plo1, results in a metaphase arrest. This arrest can be rescued by high expression of Plo1 kinase. We suggest that this physical interaction is crucial for mitotic progression by targeting polo kinase activity toward the APC.","authors":"May KM, Reynolds N, Cullen CF, Yanagida M, Ohkura H","authors_abbrev":"May KM et al.","pubmed_publication_date":"07 Jan 2002","pubmed_entrez_date":"2002-01-05","publication_year":"2002","canto_session_key":"cbe3e38931547a9c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-02 20:48:27","canto_approved_date":"2022-02-24 11:45:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-09 15:45:27","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.01c","SPAC6F12.14","SPAC23C11.16","SPBC582.03"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2016-10-02"},{"uniquename":"PMID:19180640","title":"Plasmids with E2 epitope tags: tagging modules for N- and C-terminal PCR-based gene targeting in both budding and fission yeast, and inducible expression vectors for fission yeast.","citation":"Yeast 2009 Jan;26(1):55-66","abstract":"A single-step PCR-based epitope tagging enables fast and efficient gene targeting with various epitope tags. This report presents a series of plasmids for the E2 epitope tagging of proteins in Saccharomyces cerevisiae and Schizosaccharomyces pombe. E2Tags are 10-amino acids (epitope E2a: SSTSSDFRDR)- and 12 amino acids (epitope E2b: GVSSTSSDFRDR)-long peptides derived from the E2 protein of bovine papillomavirus type 1. The modules for C-terminal tagging with E2a and E2b epitopes were constructed by the modification of the pYM-series plasmid. The N-terminal E2a and E2b tagging modules were based on pOM-series plasmid. The pOM-series plasmids were selected for this study because of their use of the Cre-loxP recombination system. The latter enables a marker cassette to be removed after integration into the loci of interest and, thereafter, the tagged protein is expressed under its endogenous promoter. Specifically for fission yeast, high copy pREP plasmids containing the E2a epitope tag as an N-terminal or C-terminal tag were constructed. The properties of E2a and E2b epitopes and the sensitivity of two anti-E2 monoclonal antibodies (5E11 and 3F12) were tested using several S. cerevisiae and Sz. pombe E2-tagged strains.","doi":"10.1002/yea.1650","authors":"Tamm T","authors_abbrev":"Tamm T","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2009-01-31","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27611693","title":"A Taz1- and Microtubule-Dependent Regulatory Relationship between Telomere and Centromere Positions in Bouquet Formation Secures Proper Meiotic Divisions.","citation":"PLoS Genet 2016 Sep;12(9):e1006304","abstract":"During meiotic prophase, telomeres cluster, forming the bouquet chromosome arrangement, and facilitate homologous chromosome pairing. In fission yeast, bouquet formation requires switching of telomere and centromere positions. Centromeres are located at the spindle pole body (SPB) during mitotic interphase, and upon entering meiosis, telomeres cluster at the SPB, followed by centromere detachment from the SPB. Telomere clustering depends on the formation of the microtubule-organizing center at telomeres by the linker of nucleoskeleton and cytoskeleton complex (LINC), while centromere detachment depends on disassembly of kinetochores, which induces meiotic centromere formation. However, how the switching of telomere and centromere positions occurs during bouquet formation is not fully understood. Here, we show that, when impaired telomere interaction with the LINC or microtubule disruption inhibited telomere clustering, kinetochore disassembly-dependent centromere detachment and accompanying meiotic centromere formation were also inhibited. Efficient centromere detachment required telomere clustering-dependent SPB recruitment of a conserved telomere component, Taz1, and microtubules. Furthermore, when artificial SPB recruitment of Taz1 induced centromere detachment in telomere clustering-defective cells, spindle formation was impaired. Thus, detachment of centromeres from the SPB without telomere clustering causes spindle impairment. These findings establish novel regulatory mechanisms, which prevent concurrent detachment of telomeres and centromeres from the SPB during bouquet formation and secure proper meiotic divisions.","doi":"10.1371/journal.pgen.1006304","authors":"Katsumata K, Hirayasu A, Miyoshi J, Nishi E, Ichikawa K, Tateho K, Wakuda A, Matsuhara H, Yamamoto A","authors_abbrev":"Katsumata K et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-09-10","publication_year":"2016","canto_session_key":"a820d20db389b57f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ayumu Yamamoto","canto_first_approved_date":"2026-06-03 15:08:17","canto_approved_date":"2026-06-03 15:08:17","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-05-30 04:09:20","canto_added_date":"2016-09-11 00:15:13","annotation_curators":[{"name":"Ayumu Yamamoto","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":19,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.03c","SPCC417.07c","SPAC16A10.07c","SPAC19G12.13c","SPAC6G9.13c","SPAC17A5.11","SPBC12D12.01","SPBC1778.02"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2026-06-03"},{"uniquename":"PMID:25664722","title":"A global profile of replicative polymerase usage.","citation":"Nat Struct Mol Biol 2015 Mar;22(3):192-198","abstract":"Three eukaryotic DNA polymerases are essential for genome replication. Polymerase (Pol) α-primase initiates each synthesis event and is rapidly replaced by processive DNA polymerases: Polɛ replicates the leading strand, whereas Polδ performs lagging-strand synthesis. However, it is not known whether this division of labor is maintained across the whole genome or how uniform it is within single replicons. Using Schizosaccharomyces pombe, we have developed a polymerase usage sequencing (Pu-seq) strategy to map polymerase usage genome wide. Pu-seq provides direct replication-origin location and efficiency data and indirect estimates of replication timing. We confirm that the division of labor is broadly maintained across an entire genome. However, our data suggest a subtle variability in the usage of the two polymerases within individual replicons. We propose that this results from occasional leading-strand initiation by Polδ followed by exchange for Polɛ.","doi":"10.1038/nsmb.2962","authors":"Daigaku Y, Keszthelyi A, Müller CA, Miyabe I, Brooks T, Retkute R, Hubank M, Nieduszynski CA, Carr AM","authors_abbrev":"Daigaku Y et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-02-10","publication_year":"2015","canto_session_key":"a87bae2017e8cda0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasukazu Daigaku","canto_approved_date":"2015-11-11 09:40:09","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-11 09:39:57","canto_added_date":"2015-02-12 01:15:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Yasukazu Daigaku","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.04","SPBC25H2.13c","SPAC4G9.02","SPBC1734.06"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-11-11"},{"uniquename":"PMID:23370392","title":"A knockout screen for protein kinases required for the proper meiotic segregation of chromosomes in the fission yeast Schizosaccharomyces pombe.","citation":"Cell Cycle 2013 Feb 15;12(4):618-24","abstract":"The reduction of chromosome number during meiosis is achieved by two successive rounds of chromosome segregation after just single round of DNA replication. To identify novel proteins required for the proper segregation of chromosomes during meiosis, we analyzed the consequences of deleting Schizosaccharomyces pombe genes predicted to encode protein kinases that are not essential for cell viability. We show that Mph1, a member of the Mps1 family of spindle assembly checkpoint kinases, is required to prevent meiosis I homolog non-disjunction. We also provide evidence for a novel function of Spo4, the fission yeast ortholog of Dbf4-dependent Cdc7 kinase, in regulating the length of anaphase II spindles. In the absence of Spo4, abnormally elongated anaphase II spindles frequently overlap and thus destroy the linear order of nuclei in the ascus. Our observation that the spo4Δ mutant phenotype can be partially suppressed by inhibiting Cdc2-as suggests that dysregulation of the activity of this cyclin-dependent kinase may cause abnormal elongation of anaphase II spindles in spo4Δ mutant cells.","doi":"10.4161/cc.23513","authors":"Kovacikova I, Polakova S, Benko Z, Cipak L, Zhang L, Rumpf C, Miadokova E, Gregan J","authors_abbrev":"Kovacikova I et al.","pubmed_publication_date":"15 Feb 2013","pubmed_entrez_date":"2013-02-02","publication_year":"2013","canto_session_key":"05f3bece7874cdcf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-06-08 08:24:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-06 11:33:08","canto_added_date":"2013-05-15 10:15:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC24B10.07","SPCC63.08c","SPAC31G5.09c","SPBC29A10.02","SPBC1D7.05","SPAC23C4.12","SPCC74.03c","SPBC1778.04","SPBC106.01","SPAC1D4.13","SPAC24B11.06c","SPBC11B10.09","SPBC21.07c","SPCC297.03","SPCC417.06c","SPCC1322.12c","SPBC21C3.18"],"gene_count":17,"ltp_gene_count":14,"approved_date":"2013-06-06"},{"uniquename":"PMID:21899677","title":"Cdc42 regulates multiple membrane traffic events in fission yeast.","citation":"Traffic 2011 Dec;12(12):1744-58","abstract":"Fission yeast Cdc42 regulates polarized growth and is involved in For3 formin activation and actin cable assembly. We show here that a thermosensitive strain carrying the cdc42L160S allele has membrane traffic defects independent of the actin cable defects. This strain has decreased acid phosphatase (AP) secretion, intracellular accumulation of vesicles and fragmentation of vacuoles. In addition, the exocyst is not localized to the tips of these cells. Overproduction of the scaffold protein Pob1 suppressed cdc42L160S thermosensitive growth and restored exocyst localization and AP secretion. The GTPase Rho3 also suppressed cdc42L160S thermosensitivity, restored exocyst localization and AP secretion. However, Rho3 did not restore the actin cables in these cells as Pob1 does. Similarly, overexpression of psy1(+) , coding a syntaxin (t-SNARE) homolog, or of ypt2(+) , coding an SEC4 homolog in fission yeast, rescued growth at high temperature but did not restore actin cables, nor the exocyst-polarized localization. cdc42L160S cells also have defects in vacuole formation that were rescued by Pob1, Rho3 and Psy1. All together, we propose that Cdc42 and the scaffold Pob1 are required for membrane trafficking and fusion, contributing to polarized secretion, endosome recycling, vacuole formation and growth.","doi":"10.1111/j.1600-0854.2011.01275.x","authors":"Estravís M, Rincón SA, Santos B, Pérez P","authors_abbrev":"Estravís M et al.","pubmed_publication_date":"Dec 2011","pubmed_entrez_date":"2011-09-09","publication_year":"2011","canto_session_key":"0e0e9a4938b536b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-07-31 14:51:46","canto_approved_date":"2026-04-25 12:33:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-15 10:02:40","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.09","SPAC9E9.07c","SPBC106.20","SPAC6G9.11","SPAC110.03","SPBC1289.04c","SPAC19G12.10c","SPCC895.05","SPAC23C4.08","SPCC825.03c","SPBP4G3.02"],"gene_count":11,"ltp_gene_count":9,"approved_date":"2017-07-31"},{"uniquename":"PMID:10668632","title":"Identification of sds21 in fission yeast in an inhibitor-resistant high molecular mass protein phosphatase-1 complex.","citation":"Biochem Cell Biol 1999;77(6):551-8","abstract":"While characterizing the type-1 protein phosphatases sds21 and dis2 in fission yeast (Schizosaccharomyces pombe) a novel high molecular mass protein was identified with serine/threonine phosphatase activity (referred to as PP-R) that was resistant to a panel of characteristic inhibitors of protein phosphatases. Purification of the native sds21 catalytic isoform of protein phosphatase-1 (PP-1) from an S. pombe knockout strain lacking dis2 (deltadis2) resulted predominantly in identification of PP-R. To test the hypothesis that the catalytic activity of PP-R comprised sds21, a parallel purification was performed of PP-1 activity from an S. pombe knockout strain lacking sds21 (deltasds21). Both deltasds21 and deltadis2 strains exhibited similar protein phosphatase activity profiles as determined by DEAE-sepharose, Mono-Q and Superdex gel filtration chromatography. However, the peak of protein phosphatase activity from deltasds21 S. pombe that co-migrated with PP-R from deltadis2 S. pombe exhibited the sensitivity to a panel of inhibitors that was characteristic of a type-1 protein phosphatase. These data suggest that the catalytic subunit of PP-R comprises sds21 and that the resistance to inhibitors may originate from structural differences between dis2 and sds21 isoforms. A key structural feature present in sds21, but lacking in dis2, is a classical phosphorylation consensus sequence surrounding serine-145 of sds21. The previous hypothesis was that PP-1 activity among several lower eukaryotes may be regulated directly by cAMP-dependent protein kinase (PKA) phosphorylation. However, this study demonstrated that recombinant sds21 is not a target for PKA in vitro. The constrained configuration of the putative PKA site on the PP-1 holoenzyme may restrict its ability to be targeted by PKA.","authors":"Dawson JF, Holmes CF","authors_abbrev":"Dawson JF et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"2000-02-11","publication_year":"1999","canto_session_key":"840cd7ab39e62b22","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2017-09-14 03:12:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-14 03:12:45","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC31H12.05c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2017-09-14"},{"uniquename":"PMID:40402811","title":"Characterization of oncohistone H2B variants in Schizosaccharomyces pombe reveals a key role of H2B monoubiquitination deficiency in genomic instability by altering gene expression.","citation":"FEMS Yeast Res 2025 May 22;","abstract":"Various amino acid substitutions commonly occur at one residue of a histone in human cancers, but it remains unclear whether these histone variants have distinct oncogenic effects and mechanisms. Our previous modeling study in the fission yeast Schizosaccharomyces pombe (S. pombe) demonstrated that the oncohistone mutants H2BG52D, H2BD67N, and H2BP102L cause the homologous recombination defect and genomic instability by compromising H2B monoubiquitination (H2Bub). However, it is unknown whether other amino acid changes at the H2B-Gly52/Asp67/Pro102 residues influence H2Bub levels and whether they cause genomic instability by altering H2Bub-regulated gene expression. Here, we construct diverse onco-mutants at the sole H2B gene htb1-Gly52/Asp67/Pro102 sites in S. pombe and study their impacts on genotoxic response, H2Bub levels, and gene expression. Interestingly, the onco-mutants htb1-G52D, htb1-D67N, and htb1-P102L exclusively exhibit significant genotoxic sensitivity, reduced H2Bub levels, and altered gene expression. These defects can be rescued by restoring H2Bub levels with the deletion of the H2B deubiquitinase ubp8+. These strong genetic correlations suggest that H2Bub deficiency plays a determinant role in the genomic instability of htb1-Gly52/Asp67/Pro102 onco-mutants and that the alteration of gene expression due to reduced H2Bub levels is a novel mechanism underlying the genomic instability caused by htb1-G52D, htb1-D67N, and htb1-P102L onco-mutations.","doi":"10.1093/femsyr/foaf027","authors":"Lu G, Liu L, Opoku M, Zhu R, Wang H, Feng G","authors_abbrev":"Lu G et al.","pubmed_publication_date":"22 May 2025","pubmed_entrez_date":"2025-05-22","publication_year":"2025","canto_session_key":"17fa8e03c564e348","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Opoku Mitchell Agyei","canto_first_approved_date":"2025-12-17 09:19:09","canto_approved_date":"2025-12-17 09:19:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-11-10 08:01:52","canto_added_date":"2025-05-22 23:25:04","annotation_curators":[{"name":"Li Liu","community_curator":true,"annotation_count":1,"orcid":"0009-0000-6889-1426","file_type":null,"file_name":null},{"name":"Opoku Mitchell Agyei","community_curator":true,"annotation_count":152,"orcid":"0009-0007-5004-8781","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":105,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12","SPAC110.01","SPBC887.17","SPCC622.09","SPBC359.03c","SPAC13A11.04c","SPAC821.09"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2025-12-17"},{"uniquename":"PMID:28162898","title":"SIN-Dependent Dissociation of the SAD Kinase Cdr2 from the Cell Cortex Resets the Division Plane.","citation":"Curr Biol 2017 Feb 20;27(4):534-542","abstract":"Proper division plane positioning is crucial for faithful chromosome segregation but also influences cell size, position, or fate [1]. In fission yeast, medial division is controlled through negative signaling by the cell tips during interphase and positive signaling by the centrally placed nucleus at mitotic entry [2-4]: the cell geometry network (CGN), controlled by the inhibitory cortical gradient of the DYRK kinase Pom1 emanating from the cell tips, first promotes the medial localization of cytokinetic ring precursors organized by the SAD kinase Cdr2 to pre-define the division plane [5-8]; then, massive nuclear export of the anillin-like protein Mid1 at mitosis entry confirms or readjusts the division plane according to nuclear position and triggers the assembly of a medial contractile ring [5, 9-11]. Strikingly, the Hippo-like septation initiation network (SIN) induces Cdr2 dissociation from cytokinetic precursors at this stage [12-14]. We show here that SIN-dependent phosphorylation of Cdr2 promotes its interaction with the 14-3-3 protein Rad24 that sequesters it in the cytoplasm during cell division. If this interaction is compromised, cytokinetic precursors are asymmetrically distributed in the cortex of newborn cells, leading to asymmetrical division if nuclear signaling is abolished. We conclude that, through this new function, the SIN resets the division plane in newborn cells to ensure medial division.","doi":"10.1016/j.cub.2016.12.050","authors":"Rincon SA, Estravis M, Dingli F, Loew D, Tran PT, Paoletti A","authors_abbrev":"Rincon SA et al.","pubmed_publication_date":"20 Feb 2017","pubmed_entrez_date":"2017-02-07","publication_year":"2017","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-02-08 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC4B3.15","SPAC2F7.03c","SPAC24B11.11c","SPAC8E11.02c","SPAC57A10.02"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:41111108","title":"Bulk FRET Analysis of the Conformation of the Cohesin Ring.","citation":"Methods Mol Biol 2026;2991:137-145","abstract":"Cohesin is a member of the SMC protein family that exerts its chromosome functions by holding district DNA segments together using the ring structure. Topological cohesin loading involves complex, dynamic structural changes; these transitions are tightly linked to the initial cohesin association with DNA and subsequent DNA entrapment, which occurs through the transient opening of the ring at the interfaces between subunits. This chapter describes a method of monitoring the conformational changes of fission yeast cohesin that combines biochemical reconstitution and fluorescence resonance energy transfer (FRET). This method is useful for studying the structural dynamics and protein-protein interactions of not only cohesin but also other SMC proteins.","doi":"10.1007/978-1-0716-5005-9_9","authors":"Higashi TL","authors_abbrev":"Higashi TL","pubmed_publication_date":"2026","pubmed_entrez_date":"2025-10-19","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-10-20 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22505187","title":"Quantitative 3D imaging of yeast by hard X-ray tomography.","citation":"Microsc Res Tech 2012 May;75(5):662-6","abstract":"Full-field hard X-ray tomography could be used to obtain three-dimensional (3D) nanoscale structures of biological samples. The image of the fission yeast, Schizosaccharomyces pombe, was clearly visualized based on Zernike phase contrast imaging technique and heavy metal staining method at a spatial resolution better than 50 nm at the energy of 8 keV. The distributions and shapes of the organelles during the cell cycle were clearly visualized and two types of organelle were distinguished. The results for cells during various phases were compared and the ratios of organelle volume to cell volume can be analyzed quantitatively. It showed that the ratios remained constant between growth and division phase and increased strongly in stationary phase, following the shape and size of two types of organelles changes. Our results demonstrated that hard X-ray microscopy was a complementary method for imaging and revealing structural information for biological samples.","doi":"10.1002/jemt.21108","authors":"Zheng T, Li W, Guan Y, Song X, Xiong Y, Liu G, Tian Y","authors_abbrev":"Zheng T et al.","pubmed_publication_date":"May 2012","pubmed_entrez_date":"2012-04-17","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011603","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17381332","title":"Slicing and spreading of heterochromatic silencing by RNA interference.","citation":"Cold Spring Harb Symp Quant Biol 2006;71:497-503","abstract":"RNA interference (RNAi) can mediate gene silencing posttranscriptionally by target RNA cleavage, or transcriptionally by chromatin and DNA modification. Argonaute is an essential component of the RNAi machinery that displays endonucleolytic activity guided by bound small RNAs. This slicing activity has recently been shown to be required for gene silencing and spreading of histone modifications characteristic of heterochromatin in Schizosaccharomyces pombe. Argonaute proteins with catalytic and nucleic acid binding capacities are found to function in RNAi within both the plant and animal kingdoms. Here we review the requirement of slicing for silencing and spreading in S. pombe, plants, and humans.","authors":"Locke SM, Martienssen RA","authors_abbrev":"Locke SM et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-03-27","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31443136","title":"Sliding filament and fixed filament mechanisms contribute to ring tension in the cytokinetic contractile ring.","citation":"Cytoskeleton (Hoboken) 2019 Nov;76(11-12):611-625","abstract":"A fundamental challenge in cell biology is to understand how cells generate actomyosin-based contractile force. Here we study the actomyosin contractile ring that divides cells during cytokinesis and generates tension by a mechanism that remains poorly understood. Long ago a muscle-like sliding filament mechanism was proposed, but evidence for sarcomeric organization in contractile rings is lacking. We develop a coarse-grained model of the fission yeast cytokinetic ring, incorporating the two myosin-II isoforms Myo2 and Myp2 and severely constrained by experimental data. The model predicts that ring tension is indeed generated by a sliding filament mechanism, but a spatially and temporally homogeneous version of that in muscle. In this mechanism all pairs of oppositely oriented actin filaments are rendered tense as they are pulled toward one another and slide through clusters of myosin-II. The mechanism relies on anchoring of actin filament barbed ends to the plasma membrane, which resists lateral motion and enables filaments to become tense when pulled by myosin-II. A second fixed filament component is independent of lateral anchoring, generated by chains of like-oriented actin filaments. Myo2 contributes to both components, while Myp2 contributes to the sliding filament component only. In the face of instabilities inherent to actomyosin contractility, organizational homeostasis is maintained by rapid turnover of Myo2 and Myp2, and by drag forces that resist lateral motion of actin, Myo2 and Myp2. Thus, sliding and fixed filament mechanisms contribute to tension in the disordered contractile ring without the need for the sarcomeric architecture of muscle.","doi":"10.1002/cm.21558","authors":"Alonso-Matilla R, Thiyagarajan S, O'Shaughnessy B","authors_abbrev":"Alonso-Matilla R et al.","pubmed_publication_date":"Nov 2019","pubmed_entrez_date":"2019-08-24","publication_year":"2019","canto_session_key":"77e6945b859d6196","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-08-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1944337","title":"DNA repair in the fission yeast, Schizosaccharomyces pombe.","citation":"Mutat Res 1991;250(1-2):205-10","abstract":"Mutants of the fission yeast Schizosaccharomyces pombe which are sensitive to UV and/or gamma-irradiation have been assigned to 23 complementation groups, which can be assigned to three phenotypic groups. We have cloned genes which correct the deficiency in mutants corresponding to 12 of the complementation groups. Three genes in the excision-repair pathway have a high degree of sequence conservation with excision-repair genes from the evolutionarily distant budding yeast Saccharomyces cerevisiae. In contrast, those genes in the recombination repair pathway which have been characterised so far, show little homology with any previously characterised genes.","authors":"Lehmann AR, Carr AM, Watts FZ, Murray JM","authors_abbrev":"Lehmann AR et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-09-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36002457","title":"Structural analysis of Red1 as a conserved scaffold of the RNA-targeting MTREC/PAXT complex.","citation":"Nat Commun 2022 Aug 24;13(1):4969","abstract":"To eliminate specific or aberrant transcripts, eukaryotes use nuclear RNA-targeting complexes that deliver them to the exosome for degradation. S. pombe MTREC, and its human counterpart PAXT, are key players in this mechanism but inner workings of these complexes are not understood in sufficient detail. Here, we present an NMR structure of an MTREC scaffold protein Red1 helix-turn-helix domain bound to the Iss10 N-terminus and show this interaction is required for proper cellular growth and meiotic mRNA degradation. We also report a crystal structure of a Red1-Ars2 complex explaining mutually exclusive interactions of hARS2 with various ED/EGEI/L motif-possessing RNA regulators, including hZFC3H1 of PAXT, hFLASH or hNCBP3. Finally, we show that both Red1 and hZFC3H1 homo-dimerize via their coiled-coil regions indicating that MTREC and PAXT likely function as dimers. Our results, combining structures of three Red1 interfaces with in vivo studies, provide mechanistic insights into conserved features of MTREC/PAXT architecture.","doi":"10.1038/s41467-022-32542-3","authors":"Foucher AE, Touat-Todeschini L, Juarez-Martinez AB, Rakitch A, Laroussi H, Karczewski C, Acajjaoui S, Soler-López M, Cusack S, Mackereth CD, Verdel A, Kadlec J","authors_abbrev":"Foucher AE et al.","pubmed_publication_date":"24 Aug 2022","pubmed_entrez_date":"2022-08-24","publication_year":"2022","canto_session_key":"4843d60805e30d72","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-20 09:34:33","canto_approved_date":"2024-05-16 13:27:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-12 15:54:15","canto_added_date":"2022-08-27 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":39,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC70.09c","SPNCRNA.4748","SPAC1006.03c","SPBC216.02","SPAC17H9.02","SPBC725.08","SPAC7D4.14c","SPBP4G3.02","SPBC1D7.05","SPAC1952.15c"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2024-01-20","pdb_entries":[{"pdb_id":"7quu","gene_chains":[{"gene_uniquename":"SPAC7D4.14c","chain":"A","position":"2-44"},{"gene_uniquename":"SPAC1006.03c","chain":"B","position":"192-235"}],"title":"Red1-Iss10 complex","entry_authors":"Mackereth CD,Kadlec J,Laroussi H","entry_authors_abbrev":"Mackereth CD et al.","reference_uniquename":"PMID:36002457","experimental_method":"NMR","resolution":""},{"pdb_id":"7qy5","gene_chains":[{"gene_uniquename":"SPBC725.08","chain":"B/D/A/C","position":"68-183"},{"gene_uniquename":"SPAC1006.03c","chain":"F/G","position":"20-40"}],"title":"Crystal structure of the S.pombe Ars2-Red1 complex.","entry_authors":"Foucher AE,Kadlec J","entry_authors_abbrev":"Foucher AE et al.","reference_uniquename":"PMID:36002457","experimental_method":"X-ray","resolution":"2.77"}]},{"uniquename":"PMID:8636983","title":"Activation of a yeast pseudo DNA methyltransferase by deletion of a single amino acid.","citation":"J Mol Biol 1996 Apr 12;257(4):804-13","abstract":"The biological methylation cytosine bases in DNA is central to such diverse phenomena as restriction and modification in bacteria, repeat induced point-mutation (RIPing) in fungi and for programming gene expression patterns in vertebrates. Structural studies on HhaI DNA methyltransferase, together with the sequence comparisons of around 40 cytosine-specific DNA methyltransferases, have recently provided a molecular framework for understanding the mechanism of action of the related group of enzymes that catalyse this base modification. There are, however, a number of organisms, including Saccharomyces cerevisiae, Schizosaccharomyces pombe and Drosophila melanogaster, which have no detectable DNA methylation. Here we report that the product of the pmt1 gene recently identified in S. pombe, which contains most of the primary structure elements of a typical cytosine-specific DNA methyltransferase, is catalytically inert owing to the insertion of a Ser residue between the Pro-Cys motif found at the active site of all such DNA methyltransferases. Following deletion of this Ser residue, catalytic activity is restored and, using a range of DNA binding experiments, it is shown that the enzyme recognises and methylates the sequence CC(A/T)GG, the same sequence that is modified by the product of the Escherichia coli dcm gene. The pmt gene of S. pombe therefore encodes a pseudo DNA methyltranferase, which we have called psiM.SpoI.","authors":"Pinarbasi E, Elliott J, Hornby DP","authors_abbrev":"Pinarbasi E et al.","pubmed_publication_date":"12 Apr 1996","pubmed_entrez_date":"1996-04-12","publication_year":"1996","canto_session_key":"0073532f923b4a17","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-24 12:01:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-16 17:38:49","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C2.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-16"},{"uniquename":"PMID:35049972","title":"The Fission Yeast Cell Integrity Pathway: A Functional Hub for Cell Survival upon Stress and Beyond.","citation":"J Fungi (Basel) 2021 Dec 30;8(1)","abstract":"The survival of eukaryotic organisms during environmental changes is largely dependent on the adaptive responses elicited by signal transduction cascades, including those regulated by the Mitogen-Activated Protein Kinase (MAPK) pathways. The Cell Integrity Pathway (CIP), one of the three MAPK pathways found in the simple eukaryote fission of yeast  Schizosaccharomyces pombe , shows strong homology with mammalian Extracellular signal-Regulated Kinases (ERKs). Remarkably, studies over the last few decades have gradually positioned the CIP as a multi-faceted pathway that impacts multiple functional aspects of the fission yeast life cycle during unperturbed growth and in response to stress. They include the control of mRNA-stability through RNA binding proteins, regulation of calcium homeostasis, and modulation of cell wall integrity and cytokinesis. Moreover, distinct evidence has disclosed the existence of sophisticated interplay between the CIP and other environmentally regulated pathways, including Stress-Activated MAP Kinase signaling (SAPK) and the Target of Rapamycin (TOR). In this review we present a current overview of the organization and underlying regulatory mechanisms of the CIP in  S. pombe , describe its most prominent functions, and discuss possible targets of and roles for this pathway. The evolutionary conservation of CIP signaling in the dimorphic fission yeast  S. japonicus  will also be addressed.","doi":"10.3390/jof8010032","authors":"Cansado J, Soto T, Franco A, Vicente-Soler J, Madrid M","authors_abbrev":"Cansado J et al.","pubmed_publication_date":"30 Dec 2021","pubmed_entrez_date":"2022-01-20","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-01-22 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12130537","title":"Fission yeast CENP-B homologs nucleate centromeric heterochromatin by promoting heterochromatin-specific histone tail modifications.","citation":"Genes Dev 2002 Jul 15;16(14):1766-78","abstract":"Heterochromatin is a functionally important chromosomal component, especially at centromeres. In fission yeast, conserved heterochromatin-specific modifications of the histone H3 tail, involving deacetylation of Lys 9 and Lys 14 and subsequent methylation of Lys 9, promote the recruitment of a heterochromatin protein, Swi6, a homolog of the Drosophila heterochromatin protein 1. However, the primary determinants of the positioning of heterochromatin are still unclear. The fission yeast proteins Abp1, Cbh1, and Cbh2 are homologs of the human protein CENP-B that bind to centromeric alpha-satellite DNA and associate with centromeric heterochromatin. We show that the CENP-B homologs are functionally redundant at centromeres, and that Abp1 binds specifically to centromeric heterochromatin. In the absence of Abp1 or Cbh1, the centromeric association of Swi6 is diminished, resulting in a decrease in silencing of the region. CENP-B-homolog double disruptants show a synergistic reduction of Swi6 at centromeric heterochromatin, indicating that the three proteins are functionally redundant in the recruitment of Swi6. Furthermore, using chromatin immunoprecipitation assays, we show that disruption of CENP-B homologs causes a decrease in heterochromatin-specific modifications of histone H3. These results indicate that the CENP-B homologs act as site-specific nucleation factors for the formation of centromeric heterochromatin by heterochromatin-specific modifications of histone tails.","authors":"Nakagawa H, Lee JK, Hurwitz J, Allshire RC, Nakayama J, Grewal SI, Tanaka K, Murakami Y","authors_abbrev":"Nakagawa H et al.","pubmed_publication_date":"15 Jul 2002","pubmed_entrez_date":"2002-07-20","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18062930","title":"Functional characterisation of the Schizosaccharomyces pombe homologue of the leukaemia-associated translocation breakpoint binding protein translin and its binding partner, TRAX.","citation":"Biochim Biophys Acta 2008 Feb;1783(2):203-13","abstract":"Translin is a conserved protein which associates with the breakpoint junctions of chromosomal translocations linked with the development of some human cancers. It binds to both DNA and RNA and has been implicated in mRNA metabolism and regulation of genome stability. It has a binding partner, translin-associated protein X (TRAX), levels of which are regulated by the translin protein in higher eukaryotes. In this study we find that this regulatory function is conserved in the lower eukaryotes, suggesting that translin and TRAX have important functions which provide a selective advantage to both unicellular and multi-cellular eukaryotes, indicating that this function may not be tissue-specific in nature. However, to date, the biological importance of translin and TRAX remains unclear. Here we systematically investigate proposals that suggest translin and TRAX play roles in controlling mitotic cell proliferation, DNA damage responses, genome stability, meiotic/mitotic recombination and stability of GT-rich repeat sequences. We find no evidence for translin and/or TRAX primary function in these pathways, indicating that the conserved biochemical function of translin is not implicated in primary pathways for regulating genome stability and/or segregation.","authors":"Jaendling A, Ramayah S, Pryce DW, McFarlane RJ","authors_abbrev":"Jaendling A et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2007-12-08","publication_year":"2008","canto_session_key":"84d34826e72c8725","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-05-10 14:38:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-19 17:16:28","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":84,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16G5.01","SPCC1322.12c","SPAC24B11.06c","SPBC216.05","SPAC30.03c","SPCC736.09c","SPCC1183.05c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-01-19"},{"uniquename":"PMID:32889716","title":"Applications of Oxford Nanopore Sequencing in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2021;2196:97-116","abstract":"Recent years have seen great progresses in third-generation sequencing. New commercial platforms from Oxford Nanopore Technologies (ONT) can generate ultra-long reads from single-molecule nucleic acid fragments of kilobases up to megabases, exceeding the limitation of short reads and dependency on template amplification suffered by the previous generation of sequencing technologies. Moreover, it can detect epigenetic modifications directly, as well as providing all-around field usage, being pocket-sized and low cost. It has already been applied to yeast research in many aspects, such as complete de novo genome assemblies, the phylogeny of large-brewing yeasts, gene isoform identification, and base modification detection. These applications have delivered novel insights into yeast genomic and transcriptomic analysis.","doi":"10.1007/978-1-0716-0868-5_9","authors":"He M, Chi X, Ren J","authors_abbrev":"He M et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2020-09-05","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-09-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30020075","title":"Noncoding RNA-nucleated heterochromatin spreading is intrinsically labile and requires accessory elements for epigenetic stability.","citation":"Elife 2018 Jul 18;7","abstract":"The heterochromatin spreading reaction is a central contributor to the formation of gene-repressive structures, which are re-established with high positional precision, or fidelity, following replication. How the spreading reaction contributes to this fidelity is not clear. To resolve the origins of stable inheritance of repression, we probed the intrinsic character of spreading events in fission yeast using a system that quantitatively describes the spreading reaction in live single cells. We show that spreading triggered by noncoding RNA-nucleated elements is stochastic, multimodal, and fluctuates dynamically across time. This lack of stability correlates with high histone turnover. At the mating type locus, this unstable behavior is restrained by an accessory  cis- acting element  REIII , which represses histone turnover. Further,  REIII  safeguards epigenetic memory against environmental perturbations. Our results suggest that the most prevalent type of spreading, driven by noncoding RNA-nucleators, is epigenetically unstable and requires collaboration with accessory elements to achieve high fidelity.","doi":"10.7554/eLife.32948","authors":"Greenstein RA, Jones SK, Spivey EC, Rybarski JR, Finkelstein IJ, Al-Sady B","authors_abbrev":"Greenstein RA et al.","pubmed_publication_date":"18 Jul 2018","pubmed_entrez_date":"2018-07-19","publication_year":"2018","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2018-07-20 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11083870","title":"Bovine coupling factor 6, with just 14.5% shared identity, replaces subunit h in the yeast ATP synthase.","citation":"J Biol Chem 2001 Mar 16;276(11):8602-7","abstract":"The mammalian mitochondrial ATP synthase is composed of at least 16 polypeptides. With the exception of coupling factor F(6), there are likely yeast homologs for each of these polypeptides. There are no obvious yeast homologs of F(6), as predicted from primary sequence comparison of the putative peptides encoded by the open reading frames in the yeast genome. In this manuscript, we demonstrate that expression of bovine F(6) complements a null mutant in ATP14 gene in yeast Saccharomyces cerevisiae. Subunit h of the yeast ATP synthase is encoded by ATP14 and is just 14.5% identical to bovine F(6). Expression of bovine F(6) in an atp14 null mutant strain recovers oxidative phosphorylation, and the ATP synthase is active, although functioning with a lower efficiency than the wild type enzyme. Like subunit h, bovine F(6) is shown to interact mainly with subunit 4 (subunit b), a component of the second stalk of the enzyme. These data indicated the subunit h is the yeast homolog of mammalian coupling factor F(6).","authors":"Velours J, Vaillier J, Paumard P, Soubannier V, Lai-Zhang J, Mueller DM","authors_abbrev":"Velours J et al.","pubmed_publication_date":"16 Mar 2001","pubmed_entrez_date":"2000-11-18","publication_year":"2001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A3.10c","HGNC:847"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15923565","title":"Multiple reaction monitoring to identify sites of protein phosphorylation with high sensitivity.","citation":"Mol Cell Proteomics 2005 Aug;4(8):1134-44","abstract":"Phosphorylation governs the activity of many proteins. Insight into molecular mechanisms in biology would be immensely improved by robust, sensitive methods for identifying precisely sites of phosphate addition. An approach to selective mapping of protein phosphorylation sites on a specific target protein of interest using LC-MS is described here. In this approach multiple reaction monitoring is used as an extremely sensitive MS survey scan for potential phosphopeptides from a known protein. This is automatically followed by peptide sequencing and subsequent location of the phosphorylation site; both of these steps occur in a single LC-MS run, providing greater efficiency of sample use. The method is capable of detecting and sequencing phosphopeptides at low femtomole levels with high selectivity. As proof of the value of this approach in an experimental setting, a key Schizosaccharomyces pombe cell cycle regulatory protein, Cyclin B, was purified, and associated proteins were identified. Phosphorylation sites on these proteins were located. The technique, which we have called multiple reaction monitoring-initiated detection and sequencing (MIDAS), is shown to be a highly sensitive approach to the determination of protein phosphorylation.","authors":"Unwin RD, Griffiths JR, Leverentz MK, Grallert A, Hagan IM, Whetton AD","authors_abbrev":"Unwin RD et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-06-01","publication_year":"2005","canto_session_key":"41ad02354d88ab60","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-19 15:26:09","canto_approved_date":"2022-09-19 15:26:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-19 15:26:04","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC582.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-09-19"},{"uniquename":"PMID:30467716","title":"Co-evolution of spliceosomal disassembly interologs: crowning J-protein component with moonlighting RNA-binding activity.","citation":"Curr Genet 2019 Apr;65(2):561-573","abstract":"Spliceosome disassembly is catalyzed by the NineTeen-related (NTR) complex, which is constituted by several proteins, including Cwc23, Ntr1, and Ppr43. Cwc23 is an essential J-protein in Saccharomyces cerevisiae that recruits Ntr1, an NTC-related G-patch protein, to the spliceosome. Ntr1 interacts with Prp43, a DExD/H box RNA helicase protein, which facilitates the disassembly of spliceosomal intermediates. The interaction between Ntr1 and Prp43 is conserved and crucial for the disassembly process. However, the J-protein component of this complex is not studied in other eukaryotes. In silico analysis supported by results of yeast complementation and two-hybrid studies suggests that while Prp43 is highly conserved, both Ntr1 and Cwc23 are co-evolving components of the disassembly triad. The J-domain of Cwc23, which is otherwise dispensable for its function, is highly conserved, whereas the functionally critical C-terminus has significantly diverged in Cwc23 orthologs. Some eukaryotic orthologs of Cwc23 contain a distinct RNA recognition motif at their C-terminus and are able to bind RNA in vitro. Based on the results presented in this study, we propose that RNA-binding activity in some eukaryotic orthologs of Cwc23 might provide additional functional diversity or robustness to the J-protein/Hsp70 machine in spliceosomal remodelling processes.","doi":"10.1007/s00294-018-0906-9","authors":"Raut S, Yadav K, Verma AK, Tak Y, Waiker P, Sahi C","authors_abbrev":"Raut S et al.","pubmed_publication_date":"Apr 2019","pubmed_entrez_date":"2018-11-24","publication_year":"2019","canto_session_key":"eda8a5f3040cab08","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-19 15:33:46","canto_approved_date":"2019-01-19 15:33:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-19 15:25:28","canto_added_date":"2018-11-25 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC10H11.02","SPAC1486.03c","SPBC16H5.10c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-01-19"},{"uniquename":"PMID:10572171","title":"The top3(+) gene is essential in Schizosaccharomyces pombe and the lethality associated with its loss is caused by Rad12 helicase activity.","citation":"Nucleic Acids Res 1999 Dec 15;27(24):4715-24","abstract":"The topoisomerase III gene ( top3 (+)) from Schizosaccharomyces pombe was isolated and a targeted gene disruption ( top3 :: kan (R)) was used to make a diploid strain heterozygous for top3 (+). The diploid was sporulated and the top3 :: kan (R)spores went through four to eight cell divisions before arresting as elongated, predominantly binucleated cells with incompletely segregated chromosomes. This demonstrates that top3 (+)is essential for vegetative growth in fission yeast. The aberrant chromosomal segregation seen in top3 :: kan (R)cells is unlike the 'cut' phenotype seen in mitosis-defective mutants and so we refer to this phenotype as 'torn'. A deletion mutant, rad12-hd ( rad12 is a homolog of Saccharomyces cerevisiae SGS1), partially suppressed the lethality of top3 mutants. A point mutant, rad12-K547I, which presumably eliminates helicase activity, also suppresses the lethality of top3 mutants, demonstrating that the lethality seen in top3 (-)cells is most likely caused by the helicase activity of Rad12. This double mutant grows very slowly and has much lower viability compared to rad12-hd top3 :: kan (R)cells, implying that the helicase activity of Rad12 is not the only cause of top3 (-)lethality. The low viability of rad12 (-) top3 (-)mutants compared with rad12 single mutants suggests that Top3 also functions independently of Rad12.","authors":"Maftahi M, Han CS, Langston LD, Hope JC, Zigouras N, Freyer GA","authors_abbrev":"Maftahi M et al.","pubmed_publication_date":"15 Dec 1999","pubmed_entrez_date":"1999-11-26","publication_year":"1999","canto_session_key":"3415e752b6f0264a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-01 11:59:06","canto_approved_date":"2024-11-28 17:07:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-12 17:12:03","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPBC16G5.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-06-01"},{"uniquename":"PMID:24875629","title":"Essential domains of Schizosaccharomyces pombe Rad8 required for DNA damage response.","citation":"G3 (Bethesda) 2014 May 28;4(8):1373-84","abstract":"Schizosaccharomyces pombe Rad8 is a conserved protein homologous to S. cerevisiae Rad5 and human HLTF that is required for error-free postreplication repair by contributing to polyubiquitylation of PCNA. It has three conserved domains: an E3 ubiquitin ligase motif, a SNF2-family helicase domain, and a family-specific HIRAN domain. Data from humans and budding yeast suggest that helicase activity contributes to replication fork regression and template switching for fork restart. We constructed specific mutations in the three conserved domains and found that both the E3 ligase and HIRAN domains are required for proper response to DNA damage caused by a variety of agents. In contrast, mutations in the helicase domain show no phenotypes in a wild-type background. To determine whether Rad8 functionally overlaps with other helicases, we compared the phenotypes of single and double mutants with a panel of 23 nonessential helicase mutants, which we categorized into five phenotypic groups. Synthetic phenotypes with rad8∆ were observed for mutants affecting recombination, and a rad8 helicase mutation affected the HU response of a subset of recombination mutants. Our data suggest that the S. pombe Rad8 ubiquitin ligase activity is important for response to a variety of damaging agents, while the helicase domain plays only a minor role in modulating recombination-based fork restart during specific forms of replication stress.","doi":"10.1534/g3.114.011346","authors":"Ding L, Forsburg SL","authors_abbrev":"Ding L et al.","pubmed_publication_date":"28 May 2014","pubmed_entrez_date":"2014-05-31","publication_year":"2014","canto_session_key":"d2f50c8b6611d21c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20H4.04","SPAC13G6.01c","SPBC887.14c","SPAC9.05","SPBC29A10.05","SPBC30D10.04","SPBC660.13c","SPAC644.14c","SPAC3G6.11","SPAC2G11.12","SPAC694.06c","SPAC4H3.05","SPCP25A2.02c","SPAC15A10.03c","SPBC16D10.04c","SPBC336.01","SPCC18B5.11c","SPBC216.06c","SPAC13C5.07","SPBC16D10.09","SPAC3C7.03c","SPCC4G3.05c","SPAC20H4.07"],"gene_count":23,"ltp_gene_count":23},{"uniquename":"PMID:22970243","title":"Hpz1 modulates the G1-S transition in fission yeast.","citation":"PLoS One 2012;7(9):e44539","abstract":"Here we characterize a novel protein in S. pombe. It has a high degree of homology with the Zn-finger domain of the human Poly(ADP-ribose) polymerase (PARP). Surprisingly, the gene for this protein is, in many fungi, fused with and in the same reading frame as that encoding Rad3, the homologue of the human ATR checkpoint protein. We name the protein Hpz1 (Homologue of PARP-type Zn-finger). Hpz1 does not possess PARP activity, but is important for resistance to ultraviolet light in the G1 phase and to treatment with hydroxyurea, a drug that arrests DNA replication forks in the S phase. However, we find no evidence of a checkpoint function of Hpz1. Furthermore, absence of Hpz1 results in an advancement of S-phase entry after a G1 arrest as well as earlier recovery from a hydroxyurea block. The hpz1 gene is expressed mainly in the G1 phase and Hpz1 is localized to the nucleus. We conclude that Hpz1 regulates the initiation of the S phase and may cooperate with Rad3 in this function.","doi":"10.1371/journal.pone.0044539","authors":"Bøe CA, Knutsen JH, Boye E, Grallert B","authors_abbrev":"Bøe CA et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-09-13","publication_year":"2012","canto_session_key":"37af543e01be5659","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-08-01 12:41:04","canto_approved_date":"2023-05-03 15:20:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-06 16:44:22","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPBC2A9.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-01"},{"uniquename":"PMID:18007635","title":"Construction of conditional analog-sensitive kinase alleles in the fission yeast Schizosaccharomyces pombe.","citation":"Nat Protoc 2007;2(11):2996-3000","abstract":"Reversible protein phosphorylation is a major regulatory mechanism in a cell. A chemical-genetic strategy to conditionally inactivate protein kinases has been developed recently. Mutating a single residue in the ATP-binding pocket confers sensitivity to small-molecule inhibitors. The inhibitor can only bind to the mutant kinase and not to any other wild-type kinase, allowing specific inactivation of the modified kinase. Here, we describe a protocol to construct conditional analog-sensitive kinase alleles in the fission yeast Schizosaccharomyces pombe. This protocol can be completed in about 3 weeks and should be applicable to other organisms as well.","authors":"Gregan J, Zhang C, Rumpf C, Cipak L, Li Z, Uluocak P, Nasmyth K, Shokat KM","authors_abbrev":"Gregan J et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-11-17","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11226610","title":"Does S. pombe exploit the intrinsic asymmetry of DNA synthesis to imprint daughter cells for mating-type switching?","citation":"Trends Genet 2001 Mar;17(3):153-7","abstract":"Typically cell division is envisaged to be symmetrical, with both daughter cells being identical. However, during development and cellular differentiation, asymmetrical cell divisions have a crucial role. In this article, we describe a model of how Schizosaccharomyces pombe exploits the intrinsic asymmetry of DNA replication machinery--the difference between the replication of the leading strand and the lagging strand--to establish an asymmetrical mating-type switching pattern. This is the first system where the direction of DNA replication is involved in the formation of differentiated chromosomes. The discovery raises the possibility that DNA replication might be more generally involved in the establishment of asymmetric cellular differentiation.","authors":"Dalgaard JZ, Klar AJ","authors_abbrev":"Dalgaard JZ et al.","pubmed_publication_date":"Mar 2001","pubmed_entrez_date":"2001-02-28","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31855181","title":"The Fml1-MHF complex suppresses inter-fork strand annealing in fission yeast.","citation":"Elife 2019 Dec 19;8","abstract":"Previously we reported that a process called inter-fork strand annealing (IFSA) causes genomic deletions during the termination of DNA replication when an active replication fork converges on a collapsed fork (Morrow et al., 2017). We also identified the FANCM-related DNA helicase Fml1 as a potential suppressor of IFSA. Here, we confirm that Fml1 does indeed suppress IFSA, and show that this function depends on its catalytic activity and ability to interact with Mhf1-Mhf2 via its C-terminal domain. Finally, a plausible mechanism of IFSA suppression is demonstrated by the finding that Fml1 can catalyse regressed fork restoration in vitro.","doi":"10.7554/eLife.49784","authors":"Wong IN, Neo JP, Oehler J, Schafhauser S, Osman F, Carr SB, Whitby MC","authors_abbrev":"Wong IN et al.","pubmed_publication_date":"19 Dec 2019","pubmed_entrez_date":"2019-12-20","publication_year":"2019","canto_session_key":"bc38b80fe79ae1a4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11254133","title":"Isolation and characterization of the fission yeast gene Sprpa12+ reveals that the conserved C-terminal zinc-finger region is dispensable for the function of its product.","citation":"Mol Gen Genet 2001 Feb;264(6):852-9","abstract":"RNA polymerase I of Saccharomyces cerevisiae contains a small subunit, A12.2, encoded by RPA12, that was previously shown to be involved in the assembly and/or stabilization of the largest subunit, A190, of RNA polymerase I. To examine whether an equivalent subunit is present in another eukaryotic RNA polymerase I, we have cloned a Schizosaccahromyces pombe cDNA that is able to complement the rpa12 mutation in S. cerevisiae. The gene, named Sprpa12+, encodes a polypeptide of 119 amino acids that shows 55% identity to S. cerevisiae A12. 2 over its entire length, including two zinc-finger motifs. Disruption of the chromosomal Sprpa12+ gene shows that it is required for growth at higher temperatures but not at lower temperatures. Expression of Sprpa190+/nuc1+, which encodes the largest subunit of the S. pombe RNA polymerase I, from a multicopy plasmid can partially suppress the growth defect of the Sprpa12 disruptant at higher temperatures. These findings suggest that A12.2 subunit is functionally and structurally conserved between S. cerevisiae and S. pombe. Finally, the analysis of mutants suggests that SpRPA12 requires the zinc-finger domain in the N-terminal region but not the one in the C-terminal region for its function.","authors":"Imazawa Y, Imai K, Yao Y, Yamamoto K, Hisatake K, Muramatsu M, Nogi Y","authors_abbrev":"Imazawa Y et al.","pubmed_publication_date":"Feb 2001","pubmed_entrez_date":"2001-03-20","publication_year":"2001","canto_session_key":"efe981cbe3cf5ed3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-02 15:31:06","canto_approved_date":"2024-04-03 15:49:20","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2023-07-02 15:30:23","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.03","SPBC4C3.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-07-02"},{"uniquename":"PMID:15510221","title":"Genomic specification and epigenetic regulation of eukaryotic DNA replication origins.","citation":"EMBO J 2004 Nov 10;23(22):4365-70","abstract":"Identification of DNA replication origins (ORIs) at a genome-wide level in eukaryotes has proved to be difficult due to the high degree of degeneracy of their sequences. Recent structural and functional approaches, however, have circumvented this limitation and have provided reliable predictions of their genomic distribution in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, and they have also significantly increased the number of characterized ORIs in animals. This article reviews recent evidence on how ORIs are specified and maintained in these systems and on their regulation and sensitivity to epigenetic signals. It also discusses the possible additional involvement of ORIs in processes other than DNA replication.","authors":"Antequera F","authors_abbrev":"Antequera F","pubmed_publication_date":"10 Nov 2004","pubmed_entrez_date":"2004-10-29","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000015","title":"Use of the ND evidence code for Gene Ontology (GO) terms.","abstract":"Direct annotations to any of the three root terms 'molecular function; GO:0003674', 'biological process; GO:0008150' or 'cellular component; GO:0005575' indicate that curators have found no data supporting an annotation to a more specific term, either in the literature and/or by sequence similarity for this gene or protein as of the date of the annotation.","authors":"GO Curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD263","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9367158","title":"Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis.","citation":"Nature 1997 Nov 13;390(6656):187-92","abstract":"Inositol phospholipids play multiple roles in cell signalling systems. Two widespread eukaryotic phosphoinositide-based signal transduction mechanisms, phosphoinositidase C-catalysed phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) hydrolysis and 3-OH kinase-catalysed PtdIns(4,5)P2 phosphorylation, make the second messengers inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) sn-1,2-diacylglycerol and PtdIns(3,4,5)P3. In addition, PtdIns(4,5)P2 and PtdIns3P have been implicated in exocytosis and membrane trafficking. We now show that when the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe are hyperosmotically stressed, they rapidly synthesize phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) by a process that involves activation of a PtdIns3P 5-OH kinase. This PtdIns(3,5)P2 accumulation only occurs in yeasts that have an active vps34-encoded PtdIns 3-OH kinase, showing that this latter kinase makes the PtdIns3P needed for PtdIns(3,5)P2 synthesis and indicating that PtdIns(3,5)P2 may have a role in sorting vesicular proteins. PtdIns(3,5)P2 is also present in mammalian and plant cells: in monkey Cos-7 cells, its labelling is inversely related to the external osmotic pressure. The stimulation of a PtdIns3P 5-OH kinase-catalysed synthesis of PtdIns(3,5)P2, a molecule that might be a new type of phosphoinositide 'second messenger, thus appears to be central to a widespread and previously uncharacterized regulatory pathway.","authors":"Dove SK, Cooke FT, Douglas MR, Sayers LG, Parker PJ, Michell RH","authors_abbrev":"Dove SK et al.","pubmed_publication_date":"13 Nov 1997","pubmed_entrez_date":"1997-11-21","publication_year":"1997","canto_session_key":"b5ee773c3ae21390","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-02-27 10:44:00","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-02-27 10:43:54","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-02-27"},{"uniquename":"PMID:18474252","title":"Crosstalk between Nap1 protein and Cds1 checkpoint kinase to maintain chromatin integrity.","citation":"Biochim Biophys Acta 2008 Sep;1783(9):1595-604","abstract":"The nucleosome assembly protein Nap1 has been implicated in various cellular functions such as histone shuttling into the nucleus, nucleosome assembly, chromatin remodelling, transcriptional control and cell-cycle regulation in Saccharomyces cerevisiae. In Schizosaccharomyces pombe nap1 null mutant cells are viable but they showed a delay in the onset of mitosis which is rescued by the absence of the replication Cds1 checkpoint kinase. In contrast, the absence of the DNA-damage Chk1 checkpoint kinase is unable to rescue the delay. Moreover, the double nap1 cds1 mutant cells lose viability and cells show positive H2AX phosphorylation, suggesting that the viability of nap1-deleted cells is due to the Cds1 kinase. We also show that overexpression of Nap1 protein blocks the cell cycle in G1 phase.","doi":"10.1016/j.bbamcr.2008.03.019","authors":"Grande M, Lambea E, Fajardo A, López-Avilés S, Kellogg D, Aligue R","authors_abbrev":"Grande M et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-05-14","publication_year":"2008","canto_session_key":"bacb8daaa8ca06da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-01-08 14:49:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-14 14:48:46","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.11c","SPCC364.06","SPAPB2B4.03","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2014-07-14"},{"uniquename":"PMID:20230740","title":"Terminating histone synthesis to preserve centromere integrity.","citation":"Dev Cell 2010 Mar 16;18(3):335-6","abstract":"Histone protein synthesis is activated as cells enter S phase to allow packaging of the newly replicated DNA into chromatin. In this issue of Developmental Cell, Takayama and coworkers elucidate a mechanism for silencing histone expression at the end of S phase in S. pombe. Failure to shut off histone expression disrupts centromeric chromatin structure.","doi":"10.1016/j.devcel.2010.03.004","authors":"Marzluff WF","authors_abbrev":"Marzluff WF","pubmed_publication_date":"16 Mar 2010","pubmed_entrez_date":"2010-03-17","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30957637","title":"Fission yeast cells grow approximately exponentially.","citation":"Cell Cycle 2019 Apr;18(8):869-879","abstract":"How the rate of cell growth is influenced by cell size is a fundamental question of cell biology. The simple model that cell growth is proportional to cell size, based on the proposition that larger cells have proportionally greater synthetic capacity than smaller cells, leads to the prediction that the rate of cell growth increases exponentially with cell size. However, other modes of cell growth, including bilinear growth, have been reported. The distinction between exponential and bilinear growth has been explored in particular detail in the fission yeast Schizosaccharomyces pombe. We have revisited the mode of fission yeast cell growth using high-resolution time-lapse microscopy and find, as previously reported, that these two growth models are difficult to distinguish both because of the similarity in shapes between exponential and bilinear curves over the two-fold change in length of a normal cell cycle and because of the substantial biological and experimental noise inherent to these experiments. Therefore, we contrived to have cells grow more than twofold, by holding them in G2 for up to 8 h. Over this extended growth period, in which cells grow up to 5.5-fold, the two growth models diverge to the point that we can confidently exclude bilinear growth as a general model for fission yeast growth. Although the growth we observe is clearly more complicated than predicted by simple exponential growth, we find that exponential growth is a robust approximation of fission yeast growth, both during an unperturbed cell cycle and during extended periods of growth.","doi":"10.1080/15384101.2019.1595874","authors":"Pickering M, Hollis LN, D'Souza E, Rhind N","authors_abbrev":"Pickering M et al.","pubmed_publication_date":"Apr 2019","pubmed_entrez_date":"2019-04-09","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-04-09 09:26:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15904532","title":"PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes.","citation":"BMC Biol 2005 May 17;3:14","abstract":"PCI/MPN domain protein complexes comprise the 19S proteasome lid, the COP9 signalosome (CSN), and eukaryotic translation initiation factor 3 (eIF3). The eIF3 complex is thought to be composed of essential core subunits required for global protein synthesis and non-essential subunits that may modulate mRNA specificity. Interactions of unclear significance were reported between eIF3 subunits and PCI proteins contained in the CSN.\nHere, we report the unexpected finding that fission yeast has two distinct eIF3 complexes sharing common core subunits, but distinguished by the PCI proteins eIF3e and the novel eIF3m, which was previously annotated as a putative CSN subunit. Whereas neither eIF3e nor eIF3m contribute to the non-essential activities of CSN in cullin-RING ubiquitin ligase control, eif3m, unlike eif3e, is an essential gene required for global cellular protein synthesis and polysome formation. Using a ribonomic approach, this phenotypic distinction was correlated with a different set of mRNAs associated with the eIF3e and eIF3m complexes. Whereas the eIF3m complex appears to associate with the bulk of cellular mRNAs, the eIF3e complex associates with a far more restricted set. The microarray findings were independently corroborated for a random set of 14 mRNAs by RT-PCR analysis.\nWe propose that the PCI proteins eIF3e and eIF3m define distinct eIF3 complexes that may assist in the translation of different sets of mRNAs.","authors":"Zhou C, Arslan F, Wee S, Krishnan S, Ivanov AR, Oliva A, Leatherwood J, Wolf DA","authors_abbrev":"Zhou C et al.","pubmed_publication_date":"17 May 2005","pubmed_entrez_date":"2005-05-21","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC17D11.05","SPBC18H10.03","SPAC821.05","SPAC637.07","SPAC1751.03","SPAC4A8.16c","SPAC25G10.08","SPBC4C3.07","SPBC646.09c","SPAC4D7.05"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:34888655","title":"Molecular mechanisms for environmentally induced and evolutionarily rapid redistribution (plasticity) of meiotic recombination.","citation":"Genetics 2022 Feb 04;220(2)","abstract":"It has long been known (circa 1917) that environmental conditions, as well as speciation, can affect dramatically the frequency distribution of Spo11/Rec12-dependent meiotic recombination. Here, by analyzing DNA sequence-dependent meiotic recombination hotspots in the fission yeast Schizosaccharomyces pombe, we reveal a molecular basis for these phenomena. The impacts of changing environmental conditions (temperature, nutrients, and osmolarity) on local rates of recombination are mediated directly by DNA site-dependent hotspots (M26, CCAAT, and Oligo-C). This control is exerted through environmental condition-responsive signal transduction networks (involving Atf1, Pcr1, Php2, Php3, Php5, and Rst2). Strikingly, individual hotspots modulate rates of recombination over a very broad dynamic range in response to changing conditions. They can range from being quiescent to being highly proficient at promoting activity of the basal recombination machinery (Spo11/Rec12 complex). Moreover, each different class of hotspot functions as an independently controlled rheostat; a condition that increases the activity of one class can decrease the activity of another class. Together, the independent modulation of recombination rates by each different class of DNA site-dependent hotspots (of which there are many) provides a molecular mechanism for highly dynamic, large-scale changes in the global frequency distribution of meiotic recombination. Because hotspot-activating DNA sites discovered in fission yeast are conserved functionally in other species, this process can also explain the previously enigmatic, Prdm9-independent, evolutionarily rapid changes in hotspot usage between closely related species, subspecies, and isolated populations of the same species.","doi":"10.1093/genetics/iyab212","authors":"Protacio RU, Mukiza TO, Davidson MK, Wahls WP","authors_abbrev":"Protacio RU et al.","pubmed_publication_date":"04 Feb 2022","pubmed_entrez_date":"2021-12-10","publication_year":"2022","canto_session_key":"f82480dea3a879a4","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-12-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42085162","title":"Microhomology-mediated tandem duplication is a conserved mechanism of genomic variation with implications for human disease.","citation":"Proc Natl Acad Sci U S A 2026 May 12;123(19):e2606747123","abstract":"Tandem repeats are highly mutable genomic elements with significant functional consequences, yet the mechanisms underlying their evolutionary origin remain unclear. One proposed mechanism is microhomology-mediated tandem duplication (MTD), in which single-copy DNA segments flanked by microhomology undergo duplication and may subsequently expand. Although MTD was first described in   Schizosaccharomyces pombe  , its prevalence and evolutionary significance across life have not been systematically established. Using whole-genome deep sequencing and a unified analytical framework, we show that MTDs arise de novo across bacteria, archaea, fungi, and viruses. Analyses of 2,245 reference genomes, millions of genomes from 103 microbial species, and human datasets reveal that microhomology-mediated duplications constitute a major source of tandem duplication across domains of life. Genome-wide analyses show that most MTDs evolve under neutral or nearly neutral dynamics, while purifying selection preferentially depletes MTDs from coding regions. Mechanistically, deletion of the conserved flap endonuclease Rad27 specifically increases de novo MTD formation in budding yeast, implicating Okazaki fragment maturation in the generation of MTDs. In humans, microhomology signatures are pervasive among reference, polymorphic, and disease-associated tandem duplications and are enriched among pathogenic variants linked to genome stability and cancer. Together, these findings establish MTD as a conserved mechanism that shapes genomic variation, with implications for human disease.","doi":"10.1073/pnas.2606747123","authors":"Wei X, Gong W, Zheng Y, Zhang J, Wei X, Peng C, He X, Jiang C","authors_abbrev":"Wei X et al.","pubmed_publication_date":"12 May 2026","pubmed_entrez_date":"2026-05-05","publication_year":"2026","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2026-05-05 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29440398","title":"Assembly of the membrane domain of ATP synthase in human mitochondria.","citation":"Proc Natl Acad Sci U S A 2018 Mar 20;115(12):2988-2993","abstract":"The ATP synthase in human mitochondria is a membrane-bound assembly of 29 proteins of 18 kinds. All but two membrane components are encoded in nuclear genes, synthesized on cytoplasmic ribosomes, and imported into the matrix of the organelle, where they are assembled into the complex with ATP6 and ATP8, the products of overlapping genes in mitochondrial DNA. Disruption of individual human genes for the nuclear-encoded subunits in the membrane portion of the enzyme leads to the formation of intermediate vestigial ATPase complexes that provide a description of the pathway of assembly of the membrane domain. The key intermediate complex consists of the F 1 -c 8  complex inhibited by the ATPase inhibitor protein IF 1  and attached to the peripheral stalk, with subunits e, f, and g associated with the membrane domain of the peripheral stalk. This intermediate provides the template for insertion of ATP6 and ATP8, which are synthesized on mitochondrial ribosomes. Their association with the complex is stabilized by addition of the 6.8 proteolipid, and the complex is coupled to ATP synthesis at this point. A structure of the dimeric yeast F o  membrane domain is consistent with this model of assembly. The human 6.8 proteolipid (yeast j subunit) locks ATP6 and ATP8 into the membrane assembly, and the monomeric complexes then dimerize via interactions between ATP6 subunits and between 6.8 proteolipids (j subunits). The dimers are linked together back-to-face by DAPIT (diabetes-associated protein in insulin-sensitive tissue; yeast subunit k), forming long oligomers along the edges of the cristae.","doi":"10.1073/pnas.1722086115","authors":"He J, Ford HC, Carroll J, Douglas C, Gonzales E, Ding S, Fearnley IM, Walker JE","authors_abbrev":"He J et al.","pubmed_publication_date":"20 Mar 2018","pubmed_entrez_date":"2018-02-15","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:30889","SPAC25H1.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU011610","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21497579","title":"Redox chemistry of the Schizosaccharomyces pombe ferredoxin electron-transfer domain and influence of Cys to Ser substitutions.","citation":"J Inorg Biochem 2011 Jun;105(6):806-11","abstract":"Schizosaccharomyces pombe (Sp) ferredoxin contains a C-terminal electron transfer protein ferredoxin domain (etp(Fd)) that is homologous to adrenodoxin. The ferredoxin has been characterized by spectroelectrochemical methods, and Mössbauer, UV-Vis and circular dichroism spectroscopies. The Mössbauer spectrum is consistent with a standard diferric [2Fe-2S](2+) cluster. While showing sequence homology to vertebrate ferredoxins, the E°' and the reduction thermodynamics for etp(Fd) (-0.392 V) are similar to plant-type ferredoxins. Relatively stable Cys to Ser derivatives were made for each of the four bound Cys residues and variations in the visible spectrum in the 380-450 nm range were observed that are characteristic of oxygen ligated clusters, including members of the [2Fe-2S] cluster IscU/ISU scaffold proteins. Circular dichroism spectra were similar and consistent with no significant structural change accompanying these mutations. All derivatives were active in an NADPH-Fd reductase cytochrome c assay. The binding affinity of Fd to the reductase was similar, however, V(max) reflecting rate limiting electron transfer was found to decrease ~13-fold. The data are consistent with relatively minor perturbations of both the electronic properties of the cluster following substitution of the Fe-bond S atom with O, and the electronic coupling of the cluster to the protein.","doi":"10.1016/j.jinorgbio.2011.03.004","authors":"Wu SP, Bellei M, Mansy SS, Battistuzzi G, Sola M, Cowan JA","authors_abbrev":"Wu SP et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-04-19","publication_year":"2011","canto_session_key":"7c36a6929630977f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-04-09 14:24:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-05-24 11:53:37","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-05-24"},{"uniquename":"PMID:29860393","title":"Implementation of the CRISPR-Cas13a system in fission yeast and its repurposing for precise RNA editing.","citation":"Nucleic Acids Res 2018 Sep 06;46(15):e90","abstract":"In contrast to genome editing, which introduces genetic changes at the DNA level, disrupting or editing gene transcripts provides a distinct approach to perturbing a genetic system, offering benefits complementary to classic genetic approaches. To develop a new toolset for manipulating RNA, we first implemented a member of the type VI CRISPR systems, Cas13a from Leptotrichia shahii (LshCas13a), in Schizosaccharomyces pombe, an important model organism employed by biologists to study key cellular mechanisms conserved from yeast to humans. This approach was shown to knock down targeted endogenous gene transcripts with different efficiencies. Second, we engineered an RNA editing system by tethering an inactive form of LshCas13a (dCas13) to the catalytic domain of human adenosine deaminase acting on RNA type 2 (hADAR2d), which was shown to be programmable with crRNA to target messenger RNAs and precisely edit specific nucleotide residues. We optimized system parameters using a dual-fluorescence reporter and demonstrated the utility of the system in editing randomly selected endogenous gene transcripts. We further used it to restore the transposition of retrotransposon Tf1 mutants in fission yeast, providing a potential novel toolset for retrovirus manipulation and interference.","doi":"10.1093/nar/gky433","authors":"Jing X, Xie B, Chen L, Zhang N, Jiang Y, Qin H, Wang H, Hao P, Yang S, Li X","authors_abbrev":"Jing X et al.","pubmed_publication_date":"06 Sep 2018","pubmed_entrez_date":"2018-06-04","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-06-05 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17042740","title":"Fission yeast cytoskeletons and cell polarity factors: connecting at the cortex.","citation":"Biol Cell 2006 Nov;98(11):619-31","abstract":"Cell polarity is a fundamental property of cells from unicellular to multicellular organisms. Most of the time, it is essential so that the cells can achieve their function. The fission yeast Schizosaccharomyces pombe is a powerful genetic model organism for studying the molecular mechanisms of the cell polarity process. Indeed, S. pombe cells are rod-shaped and cell growth is restricted at the poles. The accurate localization of the cell growth machinery at the cell cortex, which involves the actin cytoskeleton, depends on cell polarity pathways that are temporally and spatially regulated. The importance of interphase microtubules and cell polarity factors acting at the cortex of cell ends in this process has been shown. Here, we review recent advances in knowledge of molecular pathways leading to the establishment of a cellular axis in fission yeast. We also describe the role of cortical proteins and mitotic cytoskeletal rearrangements that control the symmetry of cell division.","authors":"La Carbona S, Le Goff C, Le Goff X","authors_abbrev":"La Carbona S et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-10-18","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26083598","title":"Functional Expression and Characterization of Schizosaccharomyces pombe Avt3p as a Vacuolar Amino Acid Exporter in Saccharomyces cerevisiae.","citation":"PLoS One 2015;10(6):e0130542","abstract":"In Saccharomyces cerevisiae, Avt3p and Avt4p mediate the extrusion of several amino acids from the vacuolar lumen into the cytosol. SpAvt3p of Schizosaccharomyces pombe, a homologue of these vacuolar amino acid transporters, has been indicated to be involved in spore formation. In this study, we confirmed that GFP-SpAvt3p localized to the vacuolar membrane in S. pombe. The amounts of various amino acids increased significantly in the vacuolar pool of avt3Δ cells, but decreased in that of avt3+-overexpressing avt3Δ cells. These results suggest that SpAvt3p participates in the vacuolar compartmentalization of amino acids in S. pombe. To examine the export activity of SpAvt3p, we expressed the avt3+ gene in S. cerevisiae cells. We found that the heterologously overproduced GFP-SpAvt3p localized to the vacuolar membrane in S. cerevisiae. Using the vacuolar membrane vesicles isolated from avt3+-overexpressing S. cerevisiae cells, we detected the export activities of alanine and tyrosine in an ATP-dependent manner. These activities were inhibited by the addition of a V-ATPase inhibitor, concanamycin A, thereby suggesting that the activity of SpAvt3p is dependent on a proton electrochemical gradient generated by the action of V-ATPase. In addition, the amounts of various amino acids in the vacuolar pools of S. cerevisiae cells were decreased by the overproduction of SpAvt3p, which indicated that SpAvt3p was functional in S. cerevisiae cells. Thus, SpAvt3p is a vacuolar transporter that is involved in the export of amino acids from S. pombe vacuoles.","doi":"10.1371/journal.pone.0130542","authors":"Chardwiriyapreecha S, Manabe K, Iwaki T, Kawano-Kawada M, Sekito T, Lunprom S, Akiyama K, Takegawa K, Kakinuma Y","authors_abbrev":"Chardwiriyapreecha S et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-06-18","publication_year":"2015","canto_session_key":"5785790242ac75ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-09-16 14:12:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-08-06 15:08:07","canto_added_date":"2015-06-19 00:20:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H1.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-08-06"},{"uniquename":"PMID:17893680","title":"High-throughput genetic interaction mapping in the fission yeast Schizosaccharomyces pombe.","citation":"Nat Methods 2007 Oct;4(10):861-6","abstract":"Epistasis analysis, which reports on the extent to which the function of one gene depends on the presence of a second, is a powerful tool for studying the functional organization of the cell. Systematic genome-wide studies of epistasis, however, have been limited, with the majority of data being collected in the budding yeast, Saccharomyces cerevisiae. Here we present two 'pombe epistasis mapper' strategies, PEM-1 and PEM-2, which allow for high-throughput double mutant generation in the fission yeast, S. pombe. These approaches take advantage of a previously undescribed, recessive, cycloheximide-resistance mutation. Both systems can be used for genome-wide screens or for the generation of high-density, quantitative epistatic miniarray profiles (E-MAPs). Since S. cerevisiae and S. pombe are evolutionary distant, this methodology will provide insight into conserved biological pathways that are present in S. pombe, but not S. cerevisiae, and will enable a comprehensive analysis of the conservation of genetic interaction networks.","authors":"Roguev A, Wiren M, Weissman JS, Krogan NJ","authors_abbrev":"Roguev A et al.","pubmed_publication_date":"Oct 2007","pubmed_entrez_date":"2007-09-26","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4H3.05","SPAC2G11.12","SPBC216.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:8824587","title":"Conjugation, meiosis, and the osmotic stress response are regulated by Spc1 kinase through Atf1 transcription factor in fission yeast.","citation":"Genes Dev 1996 Sep 15;10(18):2276-88","abstract":"The stress-activated Wis1-Spc1 protein kinase cascade links mitotic control with environmental signals in Schizosaccharomyces pombe. Fission yeast spc1- mutants are delayed in G2 during normal growth and undergo G2 arrest when exposed to osmotic or oxidative stress. Here we report that Spc1 also has an important role in regulating sexual development in S. pombe. This discovery arose from the observation that Spc1 is activated in response to nitrogen limitation, a key signal that promotes conjugation in fission yeast. Mutant spc1- cells are defective at arresting in G2 during nitrogen starvation and exhibit a poor mating ability. These deficiencies correlate with a failure to induce transcription of ste11+, a gene that encodes a transcription factor responsible for expression of various meiotic genes. Two genes, atf1+ and atf21+, were cloned as multicopy suppressors of the spc1- mating defect. Atf1 and Atf21 are bZIP transcription factors that are most closely related to human ATF-2/CRE-BP1. Spc1 is required for stress-induced phosphorylation of Atf1. Atf1 is required for induction of meiotic genes and stress-response genes, such as gpd1+ and pyp2+, that are transcriptionally regulated by Spc1. atf1- and spc1- mutants are sensitive to osmotic stress and impaired for sexual development, showing that fission yeast uses a common pathway to respond to cytotoxic stress and nitrogen starvation. However, unlike spc1- mutants, atf1- cells have no mitotic cell-cycle defect, indicating that the stress response pathway bifurcates at Spc1 to regulate independently meiosis and mitosis.","authors":"Shiozaki K, Russell P","authors_abbrev":"Shiozaki K et al.","pubmed_publication_date":"15 Sep 1996","pubmed_entrez_date":"1996-09-15","publication_year":"1996","canto_session_key":"87780c68f55805a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-15 08:01:01","canto_approved_date":"2021-12-20 17:09:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-28 14:07:05","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.01","SPBC409.07c","SPBC29B5.01","SPAC24B11.06c","SPBC215.05","SPBC19C2.05","SPBC2F12.09c","SPBC32C12.02"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2017-09-15"},{"uniquename":"PMID:29593117","title":"Genetic defects in SAPK signalling, chromatin regulation, vesicle transport and CoA-related lipid metabolism are rescued by rapamycin in fission yeast.","citation":"Open Biol 2018 Mar;8(3)","abstract":"Rapamycin inhibits TOR (target of rapamycin) kinase, and is being used clinically to treat various diseases ranging from cancers to fibrodysplasia ossificans progressiva. To understand rapamycin mechanisms of action more comprehensively, 1014 temperature-sensitive (ts) fission yeast ( Schizosaccharomyces pombe ) mutants were screened in order to isolate strains in which the ts phenotype was rescued by rapamycin. Rapamycin-rescued 45 strains, among which 12 genes responsible for temperature sensitivity were identified. These genes are involved in stress-activated protein kinase (SAPK) signalling, chromatin regulation, vesicle transport, and CoA- and mevalonate-related lipid metabolism. Subsequent metabolome analyses revealed that rapamycin upregulated stress-responsive metabolites, while it downregulated purine biosynthesis intermediates and nucleotide derivatives. Rapamycin alleviated abnormalities in cell growth and cell division caused by  sty1  mutants (Δ sty1 ) of SAPK. Notably, in Δ sty1 , rapamycin reduced greater than 75% of overproduced metabolites (greater than 2× WT), like purine biosynthesis intermediates and nucleotide derivatives, to WT levels. This suggests that these compounds may be the points at which the SAPK/TOR balance regulates continuous cell proliferation. Rapamycin might be therapeutically useful for specific defects of these gene functions.","doi":"10.1098/rsob.170261","authors":"Sajiki K, Tahara Y, Villar-Briones A, Pluskal T, Teruya T, Mori A, Hatanaka M, Ebe M, Nakamura T, Aoki K, Nakaseko Y, Yanagida M","authors_abbrev":"Sajiki K et al.","pubmed_publication_date":"Mar 2018","pubmed_entrez_date":"2018-03-30","publication_year":"2018","canto_session_key":"7f897417cf4bd16b","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_session_submitted_date":"2019-02-08 18:55:28","canto_added_date":"2018-03-31 00:15:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17434129","title":"S. pombe LSD1 homologs regulate heterochromatin propagation and euchromatic gene transcription.","citation":"Mol Cell 2007 Apr 13;26(1):89-101","abstract":"LSD1 represses and activates transcription by demethylating histone H3K4me and H3K9me, respectively. Genetic ablation of the S. pombe homologs, splsd1 and splsd2, resulted in slow growth and lethality, respectively, underscoring their physiological importance. spLsd1 and spLsd2 form a stable protein complex, which exhibits demethylase activity toward methylated H3K9 in vitro. Both proteins were associated with the heterochromatin boundary regions and euchromatic gene promoters. Loss of spLsd1 resulted in increased H3K9 methylation accompanied by reduced euchromatic gene transcription and heterochromatin propagation. Removal of the H3K9 methylase Clr4 partially suppressed the slow growth phenotype of splsd1Delta. Conversely, catalytically inactivating point mutations in the splsd1 and splsd2 genes partially mimicked the growth and heterochromatin propagation phenotypes. Taken together, these findings suggest the importance of both enzymatic and nonenzymatic roles of spLsd1 in regulating heterochromatin propagation and euchromatic transcription and also suggest that misregulation of spLsd1/2 is likely to impact the epigenetic state of the cell.","authors":"Lan F, Zaratiegui M, Villén J, Vaughn MW, Verdel A, Huarte M, Shi Y, Gygi SP, Moazed D, Martienssen RA, Shi Y","authors_abbrev":"Lan F et al.","pubmed_publication_date":"13 Apr 2007","pubmed_entrez_date":"2007-04-17","publication_year":"2007","canto_session_key":"40b664513ff3dccd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-11-06 16:59:37","canto_approved_date":"2025-12-23 12:46:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-06 16:59:21","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":49,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPBC146.09c","SPBC28F2.12","SPAC29B12.02c","SPCC4B3.12","SPCC306.04c","SPBC428.08c","SPAC30D11.08c","SPAC23E2.02","SPCC4G3.07c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2020-11-06"},{"uniquename":"PMID:18481970","title":"An overview of the fission yeast septation initiation network (SIN).","citation":"Biochem Soc Trans 2008 Jun;36(Pt 3):411-5","abstract":"The fission yeast septation initiation network, or SIN, is a signal transduction network that is required for septum formation in Schizosaccharomyces pombe. Its activity is tightly regulated through the cell cycle, to ensure proper co-ordination of mitosis and cytokinesis. SIN signalling requires three protein kinases for its function and is mediated by a ras-superfamily GTPase. We discuss the elements of the SIN and how they are regulated.","doi":"10.1042/BST0360411","authors":"Krapp A, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-05-17","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32222534","title":"Maintenance of meiotic crossover against reduced double-strand break formation in fission yeast lacking histone H2A.Z.","citation":"Gene 2020 Jun 15;743:144615","abstract":"Meiotic crossover (CO) recombination initiates from programmed DNA double-strand breaks (DSBs) around hotspots, and results in reciprocal exchange of chromosome segments between homologous chromosomes (homologs). COs are crucial for most sexually-reproducing organisms because they promote accurate chromosome segregation and create genetic diversity. Therefore, faithful accomplishment of CO formation is ensured in many ways, but the bases of the regulation are not fully understood. Our previous study using fission yeast has revealed that mutants lacking the conserved histone H2A.Z are defective in DSB formation but maintain CO frequency at three loci tested. Here, we tested five additional sites to show that mutants lacking H2A.Z exhibit normal and increased CO frequency at two and three loci, respectively. Examining one of the CO-increased intervals in the mutant revealed that the CO upregulation is mediated at least partly at a recombination intermediate level. In addition, our genetic as well as genome-wide analyses implied a possibility that, even without H2A.Z, COs are maintained by weak and non-hotspot DSBs, which are processed preferentially as CO. These observations provide clues to further our understanding on CO control.","doi":"10.1016/j.gene.2020.144615","authors":"Yamada T, Yamada S, Ding DQ, Fujita Y, Takaya E, Hiraoka Y, Murakami H, Ohta K","authors_abbrev":"Yamada T et al.","pubmed_publication_date":"15 Jun 2020","pubmed_entrez_date":"2020-03-31","publication_year":"2020","canto_session_key":"570b1744ecf46e27","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-04-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11697911","title":"Evolution of the Rab family of small GTP-binding proteins.","citation":"J Mol Biol 2001 Nov 02;313(4):889-901","abstract":"Rab proteins are small GTP-binding proteins that form the largest family within the Ras superfamily. Rab proteins regulate vesicular trafficking pathways, behaving as membrane-associated molecular switches. Here, we have identified the complete Rab families in the Caenorhabditis elegans (29 members), Drosophila melanogaster (29), Homo sapiens (60) and Arabidopsis thaliana (57), and we defined criteria for annotation of this protein family in each organism. We studied sequence conservation patterns and observed that the RabF motifs and the RabSF regions previously described in mammalian Rabs are conserved across species. This is consistent with conserved recognition mechanisms by general regulators and specific effectors. We used phylogenetic analysis and other approaches to reconstruct the multiplication of the Rab family and observed that this family shows a strict phylogeny of function as opposed to a phylogeny of species. Furthermore, we observed that Rabs co-segregating in phylogenetic trees show a pattern of similar cellular localisation and/or function. Therefore, animal and fungi Rab proteins can be grouped in \"Rab functional groups\" according to their segregating patterns in phylogenetic trees. These functional groups reflect similarity of sequence, localisation and/or function, and may also represent shared ancestry. Rab functional groups can help the understanding of the functional evolution of the Rab family in particular and vesicular transport in general, and may be used to predict general functions for novel Rab sequences.","authors":"Pereira-Leal JB, Seabra MC","authors_abbrev":"Pereira-Leal JB et al.","pubmed_publication_date":"02 Nov 2001","pubmed_entrez_date":"2001-11-08","publication_year":"2001","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23874875","title":"Identification of a lifespan extending mutation in the Schizosaccharomyces pombe cyclin gene clg1+ by direct selection of long-lived mutants.","citation":"PLoS One 2013;8(7):e69084","abstract":"Model organisms such as budding yeast, worms and flies have proven instrumental in the discovery of genetic determinants of aging, and the fission yeast Schizosaccharomyces pombe is a promising new system for these studies. We devised an approach to directly select for long-lived S. pombe mutants from a random DNA insertion library. Each insertion mutation bears a unique sequence tag called a bar code that allows one to determine the proportion of an individual mutant in a culture containing thousands of different mutants. Aging these mutants in culture allowed identification of a long-lived mutant bearing an insertion mutation in the cyclin gene clg1(+). Clg1p, like Pas1p, physically associates with the cyclin-dependent kinase Pef1p. We identified a third Pef1p cyclin, Psl1p, and found that only loss of Clg1p or Pef1p extended lifespan. Genetic and co-immunoprecipitation results indicate that Pef1p controls lifespan through the downstream protein kinase Cek1p. While Pef1p is conserved as Pho85p in Saccharomyces cerevisiae, and as cdk5 in humans, genome-wide searches for lifespan regulators in S. cerevisiae have never identified Pho85p. Thus, the S. pombe system can be used to identify novel, evolutionarily conserved lifespan extending mutations, and our results suggest a potential role for mammalian cdk5 as a lifespan regulator.","doi":"10.1371/journal.pone.0069084","authors":"Chen BR, Li Y, Eisenstatt JR, Runge KW","authors_abbrev":"Chen BR et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-23","publication_year":"2013","canto_session_key":"4caff2b6e290929e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-06 07:10:18","canto_approved_date":"2022-02-07 20:01:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-17 09:13:53","canto_added_date":"2013-07-29 09:52:24","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC16C4.11","SPAPB18E9.02c","SPAC19E9.03","SPRRNA.47","SPBC20F10.10","SPCC1450.11c","SPBC1D7.03"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-09-06"},{"uniquename":"PMID:15128870","title":"A role for the Cdc14-family phosphatase Flp1p at the end of the cell cycle in controlling the rapid degradation of the mitotic inducer Cdc25p in fission yeast.","citation":"J Cell Sci 2004 May 15;117(Pt 12):2461-8","abstract":"The Schizosaccaromyces pombe protein Flp1p belongs to a conserved family of serine-threonine-phosphatases. The founding member of this family, Saccharomyces cerevisiae Cdc14p, is required for inactivation of mitotic CDKs and reversal of CDK mediated phosphorylation at the end of mitosis, thereby bringing about the M-G1 transition. Initial studies of Flp1p suggest that it may play a different role to Cdc14p. Here we show that Flp1p is required for rapid degradation of the mitotic inducer Cdc25p at the end of mitosis, and that Cdc25p is a substrate of Flp1p in vitro. Down-regulation of Cdc25p activity by Flp1p may ensure a prompt inactivation of mitotic CDK complexes to trigger cell division. Our results suggest a regulatory mechanism, and a universal role, for Cdc14p like proteins in coordination of cytokinesis with other cell cycle events.","authors":"Esteban V, Blanco M, Cueille N, Simanis V, Moreno S, Bueno A","authors_abbrev":"Esteban V et al.","pubmed_publication_date":"15 May 2004","pubmed_entrez_date":"2004-05-07","publication_year":"2004","canto_session_key":"2b63e5584fd23f3c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 13:12:21","canto_approved_date":"2021-06-24 15:54:48","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-05-10 14:42:09","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC336.12c","SPAC24H6.05","SPAC1782.09c","SPBC11B10.09","SPBC26H8.07c","SPCC18B5.03"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2019-01-30"},{"uniquename":"PMID:6580523","title":"Coordination of growth with cell division: regulation of synthesis of RNA during the cell cycle of the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1983;192(1-2):204-11","abstract":"In the fission yeast Schizosaccharomyces pombe the rate of RNA synthesis, as determined by pulse labeling, increases in a step-like manner in synchronous cultures prepared by centrifugal elutriation. Cultures prepared in this way show marked reductions in perturbations which can be caused by many synchrony techniques. Kinetic evidence indicates that alterations in pool metabolism are not responsible for the step pattern. The long period of increase in the rate doubling (relative to cell number increase) indicates that the period of increasing rate may be due to a growth period and not a sudden transition between a slow and a fast rate. An analysis of synchronous cultures of cells of different cell size and synchronous cultures of temperature sensitive mutants blocked in cell cycle progress indicated that neither size control, changes in DNA content nor septation are directly responsible for the steps in RNA synthesis. Instead the time of the rate change is associated with a specific point in the cell cycle, probably an event associated with nuclear division.","authors":"Elliott SG","authors_abbrev":"Elliott SG","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-01-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18042546","title":"Characterization of zfs1 as an mRNA-binding and -destabilizing protein in Schizosaccharomyces pombe.","citation":"J Biol Chem 2008 Feb 01;283(5):2586-94","abstract":"Tristetraprolin is a vertebrate CCCH tandem zinc finger protein that can bind to and destabilize certain mRNAs containing AU-rich element binding sites. zfs1 is the single gene in the fission yeast, Schizosaccharomyces pombe, that encodes a protein containing the critical features of the tristetraprolin zinc finger domain. zfs1 has been linked to pheromone signal transduction control and to the coordination of mitosis, but no biological function has been ascribed to the zfs1 protein. Through a functional genomics approach we compared transcript levels in wild-type and zfs1-deficient S. pombe strains; those elevated in the zfs1-deficient strain were examined for the presence of potential tristetraprolin-like binding sites. One such potential target transcript was encoded by arz1, a gene encoding a protein of unknown function that contains armadillo repeats. arz1 mRNA decay was inhibited in the zfs1-deficient strain when it was expressed under the control of a thiamine-repressible promoter. Mutations within one AU-rich element present in the arz1 3'-untranslated region protected this transcript from zfs1-promoted decay, whereas mutating another potential binding site had no effect. Binding assays confirmed a direct interaction between zfs1 and arz1 mRNA-based probes; this interaction was eliminated when key residues were mutated in either zfs1 zinc finger. zfs1 and its targets in S. pombe represent a useful model system for studies of zinc finger protein/AU-rich element interactions that result in mRNA decay.","authors":"Cuthbertson BJ, Liao Y, Birnbaumer L, Blackshear PJ","authors_abbrev":"Cuthbertson BJ et al.","pubmed_publication_date":"01 Feb 2008","pubmed_entrez_date":"2007-11-29","publication_year":"2008","canto_session_key":"a6db3010aab2735f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-07-12 09:47:57","canto_approved_date":"2025-09-02 17:09:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-10 15:02:20","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4D7.10c","SPAC8C9.16c","SPAC19G12.15c","SPAC343.06c","SPBC365.09c","SPAC7D4.12c","SPAC31A2.12","SPBC1718.07c","SPBC1289.13c","SPAC30D11.07","SPCC1494.03","SPBC17D11.01","SPBC20F10.03"],"gene_count":13,"ltp_gene_count":2,"approved_date":"2016-07-12"},{"uniquename":"PMID:28266914","title":"A central role for a region in the middle.","citation":"Elife 2017 Mar 07;6","abstract":"A domain called the 'Conserved region in the middle' is responsible for target recognition in the TORC2 complex in fission yeast and the mTORC2 complex in mammals.","doi":"10.7554/eLife.25700","authors":"Stuttfeld E, Imseng S, Maier T","authors_abbrev":"Stuttfeld E et al.","pubmed_publication_date":"07 Mar 2017","pubmed_entrez_date":"2017-03-08","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-03-09 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPYUG7.02c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11972773","title":"The p21-activated kinase, Shk1, is required for proper regulation of microtubule dynamics in the fission yeast, Schizosaccharomyces pombe.","citation":"Mol Microbiol 2002 Apr;44(2):325-34","abstract":"The p21-activated kinase, Shk1, is required for the proper establishment of cell polarity in the fission yeast, Schizosaccharomyces pombe. We showed recently that loss of the essential Shk1 inhibitor, Skb15, causes significant spindle defects in fission yeast, thus implicating Shk1 as a potential regulator of microtubule dynamics. Here, we show that cells deficient in Shk1 function have malformed interphase microtubules and mitotic microtubule spindles, are hypersensitive to the microtubule-destabilizing drug thiabendazole (TBZ) and cold sensitive for growth. TBZ treatment causes a downregulation of Shk1 kinase activity, which increases rapidly after release of cells from the drug, thus providing a correlation between Shk1 kinase function and active microtubule polymerization. Consistent with a role for Shk1 as a regulator of microtubule dynamics, green fluorescent protein (GFP)-Shk1 fusion proteins localize to interphase microtubules and mitotic microtubule spindles, as well as to cell ends and septum-forming regions of fission yeast cells. We show that loss of Tea1, a cell end- and microtubule-localized protein previously implicated as a regulator of microtubule dynamics in fission yeast, exacerbates the growth and microtubule defects resulting from partial loss of Shk1 and that Shk1 localizes to illicit growth tips produced by tea1 mutant cells. Our results demonstrate that Shk1 is required for the proper regulation of microtubule dynamics in fission yeast and implicate Tea1 as a potential Shk1 regulator.","authors":"Qyang Y, Yang P, Du H, Lai H, Kim H, Marcus S","authors_abbrev":"Qyang Y et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-26","publication_year":"2002","canto_session_key":"0335630039399ab3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-06-17 09:09:06","canto_approved_date":"2022-06-17 09:09:06","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-06-17 09:08:56","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":13,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.06","SPCC16C4.08c","SPBC1604.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2022-06-17"},{"uniquename":"PMID:15550239","title":"Making the right choice--long-range chromosomal interactions in development.","citation":"Cell 2004 Nov 24;119(5):583-6","abstract":"Schizosaccharomyces pombe has the remarkable potential to switch mating type as often as every generation, through selective interaction of an expressor locus with either of two transcriptionally silent donor loci. Recent results demonstrate that selection of the appropriate donor locus likely occurs through mating-type and heterochromatin-dependent spreading of a protein complex that marks the correct donor locus.","authors":"Broach JR","authors_abbrev":"Broach JR","pubmed_publication_date":"24 Nov 2004","pubmed_entrez_date":"2004-11-20","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41023123","title":"Rapalink-1 reveals TOR-dependent genes and an agmatinergic axis-based metabolic feedback regulating TOR activity and lifespan in fission yeast.","citation":"Commun Biol 2025 Sep 29;8(1):1364","abstract":"The Target of Rapamycin, TOR, is a conserved signalling pathway with characterised chemical inhibitors such as rapamycin and torin1. Bi-steric third-generation inhibitors, such as rapalink-1 have been developed, however, their effects on organismal gene expression and lifespan have not been characterised. Here, we demonstrate that rapalink-1 affects fission yeast spatial and temporal growth and prolongs chronological lifespan with a distinct TORC1 selectivity profile. Endosome and vesicle-mediated transport and homeostasis processes related to autophagy render cells resistant to rapalink-1. Our study reveals TOR-regulated genes with unknown roles in ageing, including all fission yeast agmatinases, the enzymes that convert agmatine to putrescine and urea. Through genome-wide screens, we identify sensitive and resistant mutants to agmatine and putrescine. Genetic interactome assays for the agmatinase agm1 and further cell and molecular analyses demonstrate that impairing the agmatinergic branch of arginine catabolism results in TOR activity levels that are beneficial for growth but detrimental for chronological ageing. Our study reveals the anti-ageing action of agmatinases within a metabolic circuit that regulates TOR activity, protein translation levels and lifespan.","doi":"10.1038/s42003-025-08731-3","authors":"Kumar J, Ng K, Rallis C","authors_abbrev":"Kumar J et al.","pubmed_publication_date":"29 Sep 2025","pubmed_entrez_date":"2025-09-29","publication_year":"2025","canto_session_key":"cec3af40ece4e1ec","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-09-30 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AJ632000","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.35"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19836238","title":"Stress-induced phosphorylation of S. pombe Atf1 abrogates its interaction with F box protein Fbh1.","citation":"Curr Biol 2009 Dec 01;19(22):1907-11","abstract":"The Atf1 transcription factor is critical for directing stress-induced gene expression in fission yeast [1]. Upon exposure to stress, Atf1 is hyperphosphorylated by the mitogen-activated protein kinase (MAPK) Sty1 [2, 3], which results in its stabilization [4]. The resulting increase in Atf1 is vital for a robust response to certain stresses [4]. Here we investigated the mechanism by which phosphorylation stabilizes Atf1. We show that Atf1 is a target for the ubiquitin-proteasome system and that its degradation is dependent upon an SCF E3 ligase containing the F box protein Fbh1. Turnover of Atf1 requires an intact F box, but not DNA helicase activity of Fbh1. Accordingly, disruption of Fbh1 F box function suppresses phenotypes associated with loss of Atf1 phosphorylation. Atf1 and Fbh1 interact under basal conditions, but this binding is lost upon stress. In contrast, a version of Atf1 lacking all intact MAPK sites still interacts with Fbh1 upon stress, indicating that the association between the F box protein and substrate is disrupted by stress-induced phosphorylation. Most F box protein-substrate interactions described to date are mediated positively by phosphorylation [5]. Thus, our findings represent a novel means of regulating the interaction between an F box protein and its substrate. Moreover, Atf1 is the first target described in any organism for the Fbh1 F box protein.","doi":"10.1016/j.cub.2009.09.044","authors":"Lawrence CL, Jones N, Wilkinson CR","authors_abbrev":"Lawrence CL et al.","pubmed_publication_date":"01 Dec 2009","pubmed_entrez_date":"2009-10-20","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC336.01","SPBC29B5.01","SPAC6G10.12c"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:7526164","title":"A new shuttle vector system for the identification of spontaneous and radiation-induced mutations in the fission yeast Schizosaccharomyces pombe.","citation":"Mutat Res 1994 Nov 01;311(1):111-23","abstract":"A shuttle vector, pCRR1, has been constructed for the detection of spontaneous and radiation-induced mutations in the fission yeast Schizosaccharomyces pombe. This vector contains an Escherichia coli supF suppressor tRNA gene as the target for mutagenesis and bacterial pMB1 and yeast ars1 replication origins, which can be used to propagate the plasmid in bacterial and fission yeast cells, respectively. supF mutations can be detected after plasmid transformation into S. pombe and recovery in a bacterial indicator system, KS40/pKY241, by selecting for nalidixic acid resistance and/or by screening for lacZ- cells. We found that UV light or gamma-rays induced mutations in a dose-dependent manner in this system. Treatment of ultraviolet light (UV)-irradiated DNA with E. coli photolyase, which monomerizes cyclobutane pyrimidine dimers, before introduction into S. pombe reduced mutation frequencies to nearly background levels, indicating that this type of lesion is the major source of mutations. Comparison of spontaneous and UV-induced mutation frequencies in rad+, rad8-190 and rad13-A cells revealed no significant difference in background levels or induced levels after exposure to 100 J/m2 of UV. However, when plasmid DNA was UV-irradiated with 500 J/m2, the rad8-190 cells generated only 38% as many induced supF mutations as the rad+ strain, whereas the rad13-A cells produced more than a 6-fold increase in mutability relative to the level observed for the wild-type strain. These mutability patterns are consistent with previous studies that characterized rad8-190 cells as hypomutable and rad13-A cells as hypermutable by UV light at chromosomal loci. Thus, this shuttle vector system provides a useful and sensitive tool to assess mutability in S. pombe.","authors":"Zhao Y, Goriparthi L, Lieberman HB","authors_abbrev":"Zhao Y et al.","pubmed_publication_date":"01 Nov 1994","pubmed_entrez_date":"1994-11-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20603077","title":"Dephosphorylation of F-BAR protein Cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site.","citation":"Mol Cell 2010 Jul 09;39(1):86-99","abstract":"Cytokinesis in Schizosaccharomyces pombe requires the function of Cdc15, the founding member of the pombe cdc15 homology (PCH) family of proteins. As an early, abundant contractile ring component with multiple binding partners, Cdc15 plays a key role in organizing the ring. We demonstrate that Cdc15 phosphorylation at many sites generates a closed conformation, inhibits Cdc15 assembly at the division site in interphase, and precludes interaction of Cdc15 with its binding partners. Cdc15 dephosphorylation induces an open conformation, oligomerization, and scaffolding activity during mitosis. Cdc15 mutants with reduced phosphorylation precociously appear at the division site in filament-like structures and display increased association with protein partners and the membrane. Our results indicate that Cdc15 phosphoregulation impels both assembly and disassembly of the contractile apparatus and suggest a regulatory strategy that PCH family and BAR superfamily members might broadly employ to achieve temporal specificity in their roles as linkers between membrane and cytoskeleton.","doi":"10.1016/j.molcel.2010.06.012","authors":"Roberts-Galbraith RH, Ohi MD, Ballif BA, Chen JS, McLeod I, McDonald WH, Gygi SP, Yates JR, Gould KL","authors_abbrev":"Roberts-Galbraith RH et al.","pubmed_publication_date":"09 Jul 2010","pubmed_entrez_date":"2010-07-07","publication_year":"2010","canto_session_key":"7da922bfc1ae22b3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2023-10-26 18:05:52","canto_approved_date":"2025-04-01 16:20:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-10-27 20:31:35","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":26,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23A1.17","SPCC31H12.08c","SPAC23C4.02","SPBC146.13c","SPAC57A7.10c","SPAC24C9.06c","SPBC31F10.06c","SPAC4F8.13c","SPCC1259.09c","SPAC4A8.15c","SPBC26H8.08c","SPAC25G10.09c","SPAC20G4.06c","SPAC8E11.02c","SPBC29A3.16","SPAC926.03","SPAC18G6.04c","SPAC24B11.11c","SPAC56F8.05c","SPBC691.04","SPBC1773.10c","SPAC6B12.12","SPBC1711.05","SPAC3F10.03","SPAC23C11.09","SPBC651.01c","SPAC3C7.08c","SPBC947.02","SPBC244.01c","SPBC16C6.07c","SPCC4B3.15","SPBC19G7.05c","SPAC1F5.04c","SPAC17A2.13c","SPAC9G1.06c","SPAC1782.09c","SPCC645.05c","SPAC1751.03","SPAP8A3.08","SPBC4F6.18c","SPCC1223.08c","SPBC215.05","SPAC6F6.03c","SPAC1805.11c","SPBC11C11.02","SPAC821.05","SPAC15A10.08","SPAC6F6.08c","SPAC18G6.05c","SPCC1840.02c","SPAC1F7.05","SPAC1834.03c","SPAC20G8.05c","SPBC839.10"],"gene_count":54,"ltp_gene_count":6,"approved_date":"2023-10-26"},{"uniquename":"PMID:28951543","title":"Mechanoregulated inhibition of formin facilitates contractile actomyosin ring assembly.","citation":"Nat Commun 2017 Sep 26;8(1):703","abstract":"Cytokinesis physically separates dividing cells by forming a contractile actomyosin ring. The fission yeast contractile ring has been proposed to assemble by Search-Capture-Pull-Release from cytokinesis precursor nodes that include the molecular motor type-II myosin Myo2 and the actin assembly factor formin Cdc12. By successfully reconstituting Search-Capture-Pull in vitro, we discovered that formin Cdc12 is a mechanosensor, whereby myosin pulling on formin-bound actin filaments inhibits Cdc12-mediated actin assembly. We mapped Cdc12 mechanoregulation to its formin homology 1 domain, which facilitates delivery of new actin subunits to the elongating actin filament. Quantitative modeling suggests that the pulling force of the myosin propagates through the actin filament, which behaves as an entropic spring, and thereby may stretch the disordered formin homology 1 domain and impede formin-mediated actin filament elongation. Finally, live cell imaging of mechano-insensitive formin mutant cells established that mechanoregulation of formin Cdc12 is required for efficient contractile ring assembly in vivo.The fission yeast cytokinetic ring assembles by Search-Capture-Pull-Release from precursor nodes that include formin Cdc12 and myosin Myo2. The authors reconstitute Search-Capture-Pull in vitro and find that Myo2 pulling on Cdc12-associated actin filaments mechano-inhibits Cdc12-mediated assembly, which enables proper ring assembly in vivo.","doi":"10.1038/s41467-017-00445-3","authors":"Zimmermann D, Homa KE, Hocky GM, Pollard LW, De La Cruz EM, Voth GA, Trybus KM, Kovar DR","authors_abbrev":"Zimmermann D et al.","pubmed_publication_date":"26 Sep 2017","pubmed_entrez_date":"2017-09-28","publication_year":"2017","canto_session_key":"1317fa7b05d89b57","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-09-29 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20075015","title":"Roles of Werner syndrome protein in protection of genome integrity.","citation":"DNA Repair (Amst) 2010 Mar 02;9(3):331-44","abstract":"Werner syndrome protein (WRN) is one of a family of five human RecQ helicases implicated in the maintenance of genome stability. The conserved RecQ family also includes RecQ1, Bloom syndrome protein (BLM), RecQ4, and RecQ5 in humans, as well as Sgs1 in Saccharomyces cerevisiae, Rqh1 in Schizosaccharomyces pombe, and homologs in Caenorhabditis elegans, Xenopus laevis, and Drosophila melanogaster. Defects in three of the RecQ helicases, RecQ4, BLM, and WRN, cause human pathologies linked with cancer predisposition and premature aging. Mutations in the WRN gene are the causative factor of Werner syndrome (WS). WRN is one of the best characterized of the RecQ helicases and is known to have roles in DNA replication and repair, transcription, and telomere maintenance. Studies both in vitro and in vivo indicate that the roles of WRN in a variety of DNA processes are mediated by post-translational modifications, as well as several important protein-protein interactions. In this work, we will summarize some of the early studies on the cellular roles of WRN and highlight the recent findings that shed some light on the link between the protein with its cellular functions and the disease pathology.","doi":"10.1016/j.dnarep.2009.12.011","authors":"Rossi ML, Ghosh AK, Bohr VA","authors_abbrev":"Rossi ML et al.","pubmed_publication_date":"02 Mar 2010","pubmed_entrez_date":"2010-01-16","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21385875","title":"Roles of fission yeast Grc3 protein in ribosomal RNA processing and heterochromatic gene silencing.","citation":"J Biol Chem 2011 Apr 29;286(17):15391-402","abstract":"Grc3 is an evolutionarily conserved protein. Genome-wide budding yeast studies suggest that Grc3 is involved in rRNA processing. In the fission yeast Schizosaccharomyces pombe, Grc3 was identified as a factor exhibiting distinct nuclear dot localization, yet its exact physiological function remains unknown. Here, we show that S. pombe Grc3 is required for both rRNA processing and heterochromatic gene silencing. Cytological analysis revealed that Grc3 nuclear dots correspond to heterochromatic regions and that some Grc3 is also present in the nucleolar peripheral region. Depleting the heterochromatic proteins Swi6 or Clr4 abolished heterochromatic localization of Grc3 and resulted in its preferential accumulation in the perinucleolar region, suggesting its dynamic association with these nuclear compartments. Cells expressing mutant grc3 showed defects in 25 S rRNA maturation and in heterochromatic gene silencing. Protein analysis of Grc3-containing complexes led to the identification of Las1 and components of the IPI complex (Rix1, Ipi1, and Crb3). All of these Grc3-interacting proteins showed a dynamic nuclear localization similar to that observed for Grc3, and those conditional mutants showed defects in both rRNA processing and silencing of centromeric transcripts. Our data suggest that Grc3 functions cooperatively with Las1 and the IPI complex in both ribosome biogenesis and heterochromatin assembly.","doi":"10.1074/jbc.M110.201343","authors":"Kitano E, Hayashi A, Kanai D, Shinmyozu K, Nakayama J","authors_abbrev":"Kitano E et al.","pubmed_publication_date":"29 Apr 2011","pubmed_entrez_date":"2011-03-10","publication_year":"2011","canto_session_key":"b2aa307bace87a2d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-22 20:06:56","canto_approved_date":"2026-01-30 07:09:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-26 18:37:04","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":46,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G7.08c","SPBC428.08c","SPAC1556.01c","SPCC1393.06c","SPBC16C6.12c","SPAC17A2.09c","SPCC830.03","SPAC664.01c","SPCC4G3.18"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-01-22"},{"uniquename":"PMID:40854669","title":"A novel signal peptide toolbox for optimized heterologous expression of yeast pheromones in Bacillus subtilis.","citation":"J Genet Eng Biotechnol 2025 Sep;23(3):100551","abstract":"Optimising downstream processes and achieving high product yields are essential for cost-effective and scalable bioproduction, with efficient protein secretion being a critical factor in industrial applications. To address this, we leveraged the widely utilised Sec secretion system of Bacillus subtilis to enhance heterologous protein secretion. Given the lack of reliable in silico tools for predicting optimal combinations of Sec system signal peptides (SPs) with a protein of interest (POI), we aimed to optimise the secretion efficiency of SP-POI pairings by a toolbox approach. We developed an integrative evaluation vector in which the promoter, SPs, and a coding sequence (CDS) of the POI are easily exchangeable. Further, we generated a toolbox containing 74 SPs naturally present in B. subtilis that can easily be integrated into the evaluation vector and thereby fused to the POI. As proof-of-concept, two short peptides from yeast: α-pheromone from Saccharomyces cerevisiae and P-pheromone from Schizosaccharomyces pombe were chosen as POI and secretion efficiency was measured. Successful expression and secretion of both peptides in B. subtilis were verified by an indirect ELISA assay. Eight out of 74 SPs facilitated P-pheromone secretion, while just three effectively enabled the expression of α-pheromone. The maximum observed peptide secretion levels were 43 nM for P-pheromone and 8 nM for α-pheromone. This work demonstrates the necessity of versatile screening approaches to find a matching pairing of the Sec secretion system SP and a POI. We close this gap by providing a robust toolbox with easily exchangeable elements.","doi":"10.1016/j.jgeb.2025.100551","authors":"Vološen T, Deda HM, Walther A, Popp PF, Mascher T, Wolf D","authors_abbrev":"Vološen T et al.","pubmed_publication_date":"Sep 2025","pubmed_entrez_date":"2025-08-25","publication_year":"2025","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2025-08-26 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012714","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR21324","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:34415","HGNC:37263","HGNC:24677","SPCC16A11.01","HGNC:28769","HGNC:25645"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16363811","title":"Parallels in rRNA processing: conserved features in the processing of the internal transcribed spacer 1 in the pre-rRNA from Schizosaccharomyces pombe.","citation":"Biochemistry 2005 Dec 27;44(51):16977-87","abstract":"Despite the large differences in their length and nucleotide composition, comparative analyses of the internal transcribed spacer 1 (ITS1) of widely divergent eukaryotes have suggested a simple core structure consisting of a central extended hairpin and lesser hairpin structures at the maturing junctions [Lalev, A. I., and Nazar, R. N. (1998) J. Mol. Biol. 284, 1341-1351]. In this study, the ITS1 in the pre-rRNA transcripts of Schizosaccharomyces pombe cells was examined with respect to structural features that underlie rRNA maturation. When plasmid-associated rRNA genes were expressed in vivo, a deletion of any major hairpin structure significantly reduced or eliminated both small and large subunit RNAs. Only changes in the central extended hairpin or junction regions, however, entirely eliminated plasmid-derived RNAs or resulted in elevated precursor levels. Structure-disrupting base substitutions within the RAC protein complex binding site in the extended hairpin indicated that the secondary structure was critical for rRNA maturation; composition or other changes with respect to the binding site had only modest effects. A similar disruption at the junction with the 18S rRNA also had striking effects on rRNA maturation, including a highly elevated level of unprocessed precursor and a surprisingly critical effect on 5.8S rRNA production. As previously observed with the 3' external transcribed spacer, the results are consistent with a maturation mechanism in which an initial cleavage in the 5' junction region may be directed by the RAC protein complex. Although not critical to rRNA processing, analyses of termini based on S1 nuclease protection as well as cleavage studies, in vitro, with Pac1 ribonuclease raise the possibility that in eukaryotes, as previously observed in bacteria, the RNase III homologues normally initiate the separation of the subunit RNAs.","authors":"Abeyrathne PD, Nazar RN","authors_abbrev":"Abeyrathne PD et al.","pubmed_publication_date":"27 Dec 2005","pubmed_entrez_date":"2005-12-21","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7011176","title":"Genetics of the fission yeast Schizosaccharomyces pombe.","citation":"Annu Rev Genet 1980;14:77-108","abstract":"","authors":"Egel R, Kohli J, Thuriaux P, Wolf K","authors_abbrev":"Egel R et al.","pubmed_publication_date":"1980","pubmed_entrez_date":"1980-01-01","publication_year":"1980","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2878925","title":"A single mutation confers vanadate resistance to the plasma membrane H+-ATPase from the yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1987 Jan 05;262(1):223-8","abstract":"A single-gene nuclear mutant has been selected from the yeast Schizosaccharomyces pombe for growth resistance to Dio-9, a plasma membrane H+-ATPase inhibitor. From this mutant, called pma1, an ATPase activity has been purified. It contains a Mr = 100,000 major polypeptide which is phosphorylated by [gamma-32P] ATP. Proton pumping is not impaired since the isolated mutant ATPase is able, in reconstituted proteoliposomes, to quench the fluorescence of the delta pH probe 9-amino-6-chloro-2-methoxy acridine. The isolated mutant ATPase is sensitive to Dio-9 as well as to seven other plasma membrane H+-ATPase inhibitors. The mutant H+-ATPase activity tested in vitro is, however, insensitive to vanadate. Its Km for MgATP is modified and its ATPase specific activity is decreased. The pma1 mutation decreases the rate of extracellular acidification induced by glucose when cells are incubated at pH 4.5 under nongrowing conditions. During growth, the intracellular mutant pH is more acid than the wild type one. The derepression by ammonia starvation of methionine transport is decreased in the mutant. The growth rate of pma1 mutants is reduced in minimal medium compared to rich medium, especially when combined to an auxotrophic mutation. It is concluded that the H+-ATPase activity from yeast plasma membranes controls the intracellular pH as well as the derepression of amino acid, purine, and pyrimidine uptakes. The pma1 mutation modifies several transport properties of the cells including those responsible for the uptake of Dio-9 and other inhibitors (Ulaszewski, S., Coddington, A., and Goffeau, A. (1986) Curr. Genet. 10, 359-364).","authors":"Ulaszewski S, Van Herck JC, Dufour JP, Kulpa J, Nieuwenhuis B, Goffeau A","authors_abbrev":"Ulaszewski S et al.","pubmed_publication_date":"05 Jan 1987","pubmed_entrez_date":"1987-01-05","publication_year":"1987","canto_session_key":"7f3bcf10bc2850ae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-08 08:52:46","canto_approved_date":"2023-01-27 16:55:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 16:16:21","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.10","SPAC1071.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-08"},{"uniquename":"PMID:9195756","title":"Schizosaccharomyces pombe fragile mutants as a host for heterologous protein production.","citation":"J Biotechnol 1997 Apr 25;54(2):121-9","abstract":"In order to gain information about the potential interest of the Schizosaccharomyces pombe srb 1 fragile mutants as a host for heterologous protein production, the extracellular secretion of homologous and heterologous invertases was investigated. Under catabolic derepression the fragile srb 1 mutants released into the extracellular medium 5-6-fold more invertase than the parental strain. When transformed with the SUC2 gene, which codes for Saccharomyces cerevisiae invertase, the srb 1-3 fragile mutant, grown under catabolic repression, released into the medium 3-fold more invertase than the wild-type transformant, even though the majority of the enzyme remained associated with the cell wall. Electrophoretic analysis revealed the presence in the fragile strains of some invertase forms with molecular weights smaller than their parallel wild-type strains, suggesting that the srb 1 mutants may underglycosylate not only their homologous but also the heterologous proteins.","authors":"Zárate V, Belda F","authors_abbrev":"Zárate V et al.","pubmed_publication_date":"25 Apr 1997","pubmed_entrez_date":"1997-04-25","publication_year":"1997","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3023839","title":"Replicating plasmids in Schizosaccharomyces pombe: improvement of symmetric segregation by a new genetic element.","citation":"Mol Cell Biol 1986 Jan;6(1):80-9","abstract":"We characterized a number of widely used yeast-Escherichia coli shuttle vectors in the fission yeast Schizosaccharomyces pombe. The 2 micron vectors pDB248 and YEp13 showed high frequency of transformation, intermediate mitotic and low meiotic stability, and a low copy number in S. pombe, analogous to their behavior in [cir0] strains of Saccharomyces cerevisiae. The S. cerevisiae integration vectors pLEU2 and pURA3 transformed S. pombe at very low frequencies but, surprisingly, in a nonintegrative fashion. Instead, they replicated autonomously, and they showed very high copy numbers (up to 150 copies per plasmid-containing cell). This could reflect a lack of sequence specificity for replication of plasmid DNA in S. pombe. pFL20, an S. pombe ars vector, and a series of plasmids derived from it were studied to analyze the unusually high stability of this plasmid. Mitotic stability and partitioning of the plasmids was measured by pedigree analysis of transformed S. pombe cells. An S. pombe DNA fragment (stb) was identified that stabilizes pFL20 by improvement of plasmid partitioning in mitosis and meiosis.","authors":"Heyer WD, Sipiczki M, Kohli J","authors_abbrev":"Heyer WD et al.","pubmed_publication_date":"Jan 1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8719881","title":"Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-specific PI 3-kinase essential for normal cell growth and vacuole morphology.","citation":"J Cell Sci 1995 Dec;108 ( Pt 12):3745-56","abstract":"We have cloned the gene, vps34+, from the fission yeast Schizosaccharomyces pombe which encodes an 801 amino acid protein with phosphatidylinositol 3-kinase activity. The S. pombe Vps34 protein shares 43% amino acid sequence identity with the Saccharomyces cerevisiae Vps34 protein and 28% identity with the p110 catalytic subunit of the mammalian phosphatidylinositol 3-kinase. When the vps34+ gene is disrupted, S.pombe strains are temperature-sensitive for growth and the mutant cells contain enlarged vacuoles. Furthermore, while wild-type strains exhibit substantial levels of phosphatidylinositol 3-kinase activity, this activity is not detected in the vps34 delta strain. S.pombe Vps34p-specific antiserum detects a single protein in cells of -90 kDa that fractionates almost exclusively with the crude membrane fraction. Phosphatidylinositol 3-kinase activity also is localized mainly in the membrane fraction of wild-type cells. Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring to yield phosphatidylinositol(3)phosphate. but does not utilize phosphatidylinositol(4)phosphate or phosphatidylinositol(4,5)bisphosphate as substrates. In addition, when compared to the mammalian p110 phosphatidylinositol 3-kinase, S. pombe Vps34p is relatively insensitive to the inhibitors wortmannin and LY294002. Together, these results indicate that S. pombe Vps34 is more similar to the phosphatidylinositol-specific 3-kinase, Vps34p from S. cerevisiae, and is distinct from the p110/p85 and G protein-coupled phosphatidylinositol 3-kinases from mammalian cells. These data are discussed in relation to the possible role of Vps34p in vesicle-mediated protein sorting to the S. pombe vacuole.","authors":"Takegawa K, DeWald DB, Emr SD","authors_abbrev":"Takegawa K et al.","pubmed_publication_date":"Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"6b8790f5b76d8e69","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-20 19:27:54","canto_approved_date":"2026-02-06 15:27:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-02-16 21:46:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC458.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-12-20"},{"uniquename":"PMID:37929004","title":"LAMMER Kinase Modulates Cell Cycle by Phosphorylating the MBF Repressor, Yox1, in  Schizosaccharomyces pombe .","citation":"Mycobiology 2023;51(5):372-378","abstract":"Lkh1, a LAMMER kinase homolog in the fission yeast  Schizosaccharomyces pombe , acts as a negative regulator of filamentous growth and flocculation. It is also involved in the response to oxidative stress. The  lkh1- deletion mutant displays slower cell growth, shorter cell size, and abnormal DNA content compared to the wild type. These phenotypes suggest that Lkh1 controls cell size and cell cycle progression. When we performed microarray analysis using the  lkh1- deletion mutant, we found that only four of the up-regulated genes in the  lkh1- deletion were associated with the cell cycle. Interestingly, all of these genes are regulated by the Mlu1 cell cycle box binding factor (MBF), which is a transcription complex responsible for regulating the expression of cell cycle genes during the G1/S phase. Transcription analyses of the MBF-dependent cell-cycle genes, including negative feedback regulators, confirmed the up-regulation of these genes by the deletion of  lkh1 . Pull-down assay confirmed the interaction between Lkh1 and Yox1, which is a negative feedback regulator of MBF. This result supports the involvement of LAMMER kinase in cell cycle regulation by modulating MBF activity.  In vitro  kinase assay and NetPhosK 2.0 analysis with the Yox1 T40,41A  mutant allele revealed that T40 and T41 residues are the phosphorylation sites mediated by Lkh1. These sites affect the G1/S cell cycle progression of fission yeast by modulating the activity of the MBF complex.","doi":"10.1080/12298093.2023.2262806","authors":"Park K, Lim JY, Kim JH, Lee J, Shin S, Park HM","authors_abbrev":"Park K et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-11-06","publication_year":"2023","canto_session_key":"8e2192720d3aaf9b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-11-07 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1D4.11c","SPBC21B10.13c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:19205745","title":"Redundant roles of Srs2 helicase and replication checkpoint in survival and rDNA maintenance in Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2009 May;281(5):497-509","abstract":"Srs2 helicase is believed to function as an anti-recombinase by resolving inappropriate Rad51-DNA filament. We found synthetic lethality or poor growth of srs2 with rad3 or mrc1 in Schizosaccharomyces pombe. Lethality may result from a defect in non-checkpoint function of Rad3 or Mrc1 in the absence of Srs2, because srs2 rad9, srs2 chk1 cds1 or srs2 mrc1-14A (non-phosphorylatable mrc1 allele) did not show significant growth impairment. Notably, the inactivation of rhp51/RAD51 or rad22/RAD52 failed to rescue the growth, suggesting that events that impose lethality are independent of homologous recombination. Incubation of the conditional srs2 rad3 ( ts ) cells at restrictive temperature led not only to a viability decrease but also to a remarkable shortening of rDNA clusters (approximately 100 copies). As opposed to the growth defect, shortening of rDNA clusters was also observed in srs2 rad9, srs2 chk1 cds1 or srs2 mrc1-14A, indicating that proper replication checkpoint signaling is critical for rDNA maintenance. Activation of Chk1 in the unchallenged mrc1-14A srs2 cells implies a certain level of spontaneous fork damage that might be the cause for rDNA instability. The data suggest that redundant functions of Srs2 and checkpoint proteins are essential for two independent aspects of genome maintenance.","doi":"10.1007/s00438-009-0426-x","authors":"Yasuhira S","authors_abbrev":"Yasuhira S","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-02-12","publication_year":"2009","canto_session_key":"1cf182adbddacf73","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-05-02 15:42:44","canto_approved_date":"2025-12-23 12:47:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-05-02 15:42:38","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":63,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.08","SPCC1259.13","SPAC664.07c","SPBC216.06c","SPAC3H5.06c","SPAC694.06c","SPCC18B5.11c","SPAC2G11.12","SPBC342.05","SPAC644.14c","SPBC336.04","SPAC30D11.10","SPAC3C7.03c","SPBC216.05","SPAC14C4.13","SPAC4H3.05","SPBC25H2.13c"],"gene_count":17,"ltp_gene_count":17,"approved_date":"2018-05-02"},{"uniquename":"PMID:16132818","title":"Telomere maintenance, function and evolution: the yeast paradigm.","citation":"Chromosome Res 2005;13(5):535-48","abstract":"Telomeres are multifunctional genetic elements that cap chromosome ends, playing essential roles in genome stability, chromosome higher-order organization and proliferation control. The telomere field has largely benefited from the study of unicellular eukaryotic organisms such as yeasts. Easy cultivation in laboratory conditions and powerful genetics have placed mainly Saccharomyces cerevisiae, Kluveromyces lactis and Schizosaccharomyces pombe as crucial model organisms for telomere biology research. Studies in these species have made it possible to elucidate the basic mechanisms of telomere maintenance, function and evolution. Moreover, comparative genomic analyses show that telomeres have evolved rapidly among yeast species and functional plasticity emerges as one of the driving forces of this evolution. This provides a precious opportunity to further our understanding of telomere biology.","authors":"Teixeira MT, Gilson E","authors_abbrev":"Teixeira MT et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-09-01","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2404993","title":"In vitro reactivation of spindle elongation in fission yeast nuc2 mutant cells.","citation":"J Cell Biol 1990 Feb;110(2):417-25","abstract":"To investigate the mechanisms of spindle elongation and chromosome separation in the fission yeast Schizosaccharomyces pombe, we have developed an in vitro assay using a temperature-sensitive mutant strain, nuc2. At the restrictive temperature, nuc2 cells are arrested at a metaphase-like stage with short spindles and condensed chromosomes. After permeabilization of spheroplasts of the arrested cells, spindle elongation was reactivated by addition of ATP and neurotubulin both at the restrictive and the permissive temperatures, but chromosome separation was not. This suggests that the nuc2 cells are impaired in function at a stage before sister chromatid disjunction. Spindle elongation required both ATP and exogenous tubulin and was inhibited by adenylyl imidodiphosphate (AMPPNP) or vanadate. The ends of yeast half-spindle microtubules pulse-labeled with biotinylated tubulin moved past each other during spindle elongation and a gap formed between the original half-spindles. These results suggest that the primary mechanochemical event responsible for spindle elongation is the sliding apart of antiparallel microtubules of the two half-spindles.","authors":"Masuda H, Hirano T, Yanagida M, Cande WZ","authors_abbrev":"Masuda H et al.","pubmed_publication_date":"Feb 1990","pubmed_entrez_date":"1990-02-01","publication_year":"1990","canto_session_key":"1fb20794cd6a0fac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-05-10 14:52:04","canto_approved_date":"2020-03-20 17:03:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-18 13:41:33","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-05-10"},{"uniquename":"PMID:24974934","title":"ChIPseek, a web-based analysis tool for ChIP data.","citation":"BMC Genomics 2014 Jun 30;15(1):539","abstract":"Chromatin is a dynamic but highly regulated structure. DNA-binding proteins such as transcription factors, epigenetic and chromatin modifiers are responsible for regulating specific gene expression pattern and may result in different phenotypes. To reveal the identity of the proteins associated with the specific region on DNA, chromatin immunoprecipitation (ChIP) is the most widely used technique. ChIP assay followed by next generation sequencing (ChIP-seq) or microarray (ChIP-chip) is often used to study patterns of protein-binding profiles in different cell types and in cancer samples on a genome-wide scale. However, only a limited number of bioinformatics tools are available for ChIP datasets analysis.\nWe present ChIPseek, a web-based tool for ChIP data analysis providing summary statistics in graphs and offering several commonly demanded analyses. ChIPseek can provide statistical summary of the dataset including histogram of peak length distribution, histogram of distances to the nearest transcription start site (TSS), and pie chart (or bar chart) of genomic locations for users to have a comprehensive view on the dataset for further analysis. For examining the potential functions of peaks, ChIPseek provides peak annotation, visualization of peak genomic location, motif identification, sequence extraction, and comparison between datasets. Beyond that, ChIPseek also offers users the flexibility to filter peaks and re-analyze the filtered subset of peaks. ChIPseek supports 20 different genome assemblies for 12 model organisms including human, mouse, rat, worm, fly, frog, zebrafish, chicken, yeast, fission yeast, Arabidopsis, and rice. We use demo datasets to demonstrate the usage and intuitive user interface of ChIPseek.\nChIPseek provides a user-friendly interface for biologists to analyze large-scale ChIP data without requiring any programing skills. All the results and figures produced by ChIPseek can be downloaded for further analysis. The analysis tools built into ChIPseek, especially the ones for selecting and examine a subset of peaks from ChIP data, provides invaluable helps for exploring the high through-put data from either ChIP-seq or ChIP-chip. ChIPseek is freely available at http://chipseek.cgu.edu.tw.","doi":"10.1186/1471-2164-15-539","authors":"Chen TW, Li HP, Lee CC, Gan RC, Huang PJ, Wu TH, Lee CY, Chang YF, Tang P","authors_abbrev":"Chen TW et al.","pubmed_publication_date":"30 Jun 2014","pubmed_entrez_date":"2014-07-01","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-07-02 00:15:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19244341","title":"Role of tropomyosin in formin-mediated contractile ring assembly in fission yeast.","citation":"Mol Biol Cell 2009 Apr;20(8):2160-73","abstract":"Like animal cells, fission yeast divides by assembling actin filaments into a contractile ring. In addition to formin Cdc12p and profilin, the single tropomyosin isoform SpTm is required for contractile ring assembly. Cdc12p nucleates actin filaments and remains processively associated with the elongating barbed end while driving the addition of profilin-actin. SpTm is thought to stabilize mature filaments, but it is not known how SpTm localizes to the contractile ring and whether SpTm plays a direct role in Cdc12p-mediated actin polymerization. Using \"bulk\" and single actin filament assays, we discovered that Cdc12p can recruit SpTm to actin filaments and that SpTm has diverse effects on Cdc12p-mediated actin assembly. On its own, SpTm inhibits actin filament elongation and depolymerization. However, Cdc12p completely overcomes the combined inhibition of actin nucleation and barbed end elongation by profilin and SpTm. Furthermore, SpTm increases the length of Cdc12p-nucleated actin filaments by enhancing the elongation rate twofold and by allowing them to anneal end to end. In contrast, SpTm ultimately turns off Cdc12p-mediated elongation by \"trapping\" Cdc12p within annealed filaments or by dissociating Cdc12p from the barbed end. Therefore, SpTm makes multiple contributions to contractile ring assembly during and after actin polymerization.","authors":"Skau CT, Neidt EM, Kovar DR","authors_abbrev":"Skau CT et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-02-27","publication_year":"2009","canto_session_key":"1425fec017208eec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-09-28 15:39:51","canto_approved_date":"2024-03-14 13:08:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-14 09:53:55","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27F1.02c","SPAC4A8.15c","SPAC1F5.04c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2017-09-28"},{"uniquename":"PMID:1483350","title":"Activation of MPF in fission yeast.","citation":"Ciba Found Symp 1992;170:50-8; discussion 58-71","abstract":"In fission yeast p34cdc2/cyclin is activated at the G2/M boundary by dephosphorylation of Tyr15 of the p34cdc2 subunit. Two protein phosphatases carry out this dephosphorylation event. The major activity is encoded by cdc25, which is a distantly related member of the protein tyrosine phosphatase family. A minor activity is provided by a newly identified fission yeast protein tyrosine phosphatase.","authors":"Millar JB, Lenaers G, McGowan C, Russell P","authors_abbrev":"Millar JB et al.","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23572041","title":"Spatiotemporal regulation of meiotic recombination by Liaisonin.","citation":"Bioarchitecture 2013;3(1):20-4","abstract":"Sexual reproduction involves diversification of genetic information in successive generations. Meiotic recombination, which substantially contributes to the increase in genetic diversity, is initiated by programmed DNA double-strand breaks (DSBs) catalyzed by the evolutionarily conserved Spo11 protein. Spo11 requires additional partner proteins for its DNA cleavage reaction. DSBs are preferentially introduced at defined chromosomal sites called \"recombination hotspots.\" Recent studies have revealed that meiotically established higher-order chromosome structures, such as chromosome axes and loops, are also crucial in the control of DSB formation. Most of the DSB sites are located within chromatin loop regions, while many of the proteins involved in DSB formation reside on chromosomal axes. Hence, DSB proteins and DSB sites seem to be distantly located. To resolve this paradox, we conducted comprehensive proteomics and ChIP-chip analyses on Spo11 partners in Schizosaccharomyces pombe, in combination with mutant studies. We identified two distinct DSB complexes, the \"DSBC (DSB Catalytic core)\" and \"SFT (Seven-Fifteen-Twenty four; Rec7-Rec15-Rec24)\" subcomplexes. The DSBC subcomplex contains Spo11 and functions as the catalytic core for the DNA cleavage reaction. The SFT subcomplex is assumed to execute regulatory functions. To activate the DSBC subcomplex, the SFT subcomplex tethers hotspots to axes via its interaction with Mde2, which can interact with proteins in both DSBC and SFT subcomplexes. Thus, Mde2 is likely to bridge these two subcomplexes, forming a \"tethered loop-axis complex.\" It should be noted that Mde2 expression is strictly regulated by S phase checkpoint monitoring of the completion of DNA replication. From these observations, we proposed that Mde2 is a central coupler for meiotic recombination initiation to establish a tethered loop-axis complex in liaison with the S phase checkpoint.","doi":"10.4161/bioa.23966","authors":"Miyoshi T, Ito M, Ohta K","authors_abbrev":"Miyoshi T et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-04-11","publication_year":"2013","canto_session_key":"4f9bfd94253c41f5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10380645","title":"The role of catalase in hydrogen peroxide resistance in fission yeast Schizosaccharomyces pombe.","citation":"Can J Microbiol 1999 Feb;45(2):125-9","abstract":"The role of catalase in hydrogen peroxide resistance in Schizosaccharomyces pombe was investigated. A catalase gene disruptant completely lacking catalase activity is more sensitive to hydrogen peroxide than the parent strain. The mutant does not acquire hydrogen peroxide resistance by osmotic stress, a treatment that induces catalase activity in the wild-type cells. The growth rate of the disruptant is not different from that of the parent strain. Additionally, transformed cells that overexpress the catalase activity are more resistant to hydrogen peroxide than wildtype cells with normal catalase activity. These results indicate that the catalase of S. pombe plays an important role in resistance to high concentrations of hydrogen peroxide but offers little in the way of protection from the hydrogen peroxide generated in small amounts under normal growth conditions.","authors":"Mutoh N, Nakagawa CW, Yamada K","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-06-25","publication_year":"1999","canto_session_key":"26776deaeb7536ef","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-03-20 12:44:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-12 11:15:59","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC757.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-06-12"},{"uniquename":"PMID:9601094","title":"Mph1, a member of the Mps1-like family of dual specificity protein kinases, is required for the spindle checkpoint in S. pombe.","citation":"J Cell Sci 1998 Jun;111 ( Pt 12):1635-47","abstract":"The spindle assembly checkpoint pathway is not essential for normal mitosis but ensures accurate nuclear division by blocking the metaphase to anaphase transition in response to a defective spindle. Here, we report the isolation of a new spindle checkpoint gene, mph1 (Mps1p-like pombe homolog), in the fission yeast Schizosaccharomyces pombe, that is required for checkpoint activation in response to spindle defects. mph1 functions upstream of mad2, a previously characterized component of the spindle checkpoint. Overexpression of mph1, like overexpression of mad2, mimics activation of the checkpoint and imposes a metaphase arrest. mph1 protein shares sequence similarity with Mps1p, a dual specificity kinase that functions in the spindle checkpoint of the budding yeast Saccharomyces cerevisiae. Complementation analysis demonstrates that mph1 and Mps1p are functionally related. They differ in that Mps1p, but not mph1, has an additional essential role in spindle pole body duplication. We propose that mph1 is the MPS1 equivalent in the spindle checkpoint pathway but not in the SPB duplication pathway. Overexpression of mad2 does not require mph1 to impose a metaphase arrest, which indicates a mechanism of spindle checkpoint activation other than mph1/Mps1p kinase-dependent phosphorylation. In the same screen which led to the isolation of mad2 and mph1, we also isolated dph1, a cDNA that encodes a protein 46% identical to an S. cerevisiae SPB duplication protein, Dsk2p. Our initial characterization indicates that S.p. dph1 and S.c. DSK2 are functionally similar. Together these results suggest that the budding and fission yeasts share common elements for SPB duplication, despite differences in SPB structure and the timing of SPB duplication relative to mitotic entry.","authors":"He X, Jones MH, Winey M, Sazer S","authors_abbrev":"He X et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-05-28","publication_year":"1998","canto_session_key":"4069663dbbd3273e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-30 15:50:50","canto_approved_date":"2022-08-29 15:23:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-30 15:50:44","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC106.01","SPAC26A3.16","SPBC20F10.06","SPBC26H8.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-10-30"},{"uniquename":"PMID:26098123","title":"Promoter nucleosome dynamics regulated by signalling through the CTD code.","citation":"Elife 2015 Jun 22;4:e09008","abstract":"The phosphorylation of the RNA polymerase II C-terminal domain (CTD) plays a key role in delineating transcribed regions within chromatin by recruiting histone methylases and deacetylases. Using genome-wide nucleosome mapping, we show that CTD S2 phosphorylation controls nucleosome dynamics in the promoter of a subset of 324 genes, including the regulators of cell differentiation ste11 and metabolic adaptation inv1. Mechanistic studies on these genes indicate that during gene activation a local increase of phospho-S2 CTD nearby the promoter impairs the phospho-S5 CTD-dependent recruitment of Set1 and the subsequent recruitment of specific HDACs, which leads to nucleosome depletion and efficient transcription. The early increase of phospho-S2 results from the phosphorylation of the CTD S2 kinase Lsk1 by MAP kinase in response to cellular signalling. The artificial tethering of the Lsk1 kinase at the ste11 promoter is sufficient to activate transcription. Therefore, signalling through the CTD code regulates promoter nucleosomes dynamics.","doi":"10.7554/eLife.09008","authors":"Materne P, Anandhakumar J, Migeot V, Soriano I, Yague-Sanz C, Hidalgo E, Mignion C, Quintales L, Antequera F, Hermand D","authors_abbrev":"Materne P et al.","pubmed_publication_date":"22 Jun 2015","pubmed_entrez_date":"2015-06-23","publication_year":"2015","canto_session_key":"bdc1158a29736e75","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-06-24 00:20:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC285.09c","SPAC22H10.09","SPBC1604.08c","SPAC1F7.01c","SPAC328.04","SPAC23H3.03c","SPAC4G9.13c","SPAC27D7.06","SPCC1795.06","SPBC21H7.04","SPBC2G2.10c","SPAC22F8.12c","SPAC631.02","SPAC23C4.06c","SPAC1851.03","SPAC11G7.02","SPCC1450.02","SPCC11E10.08","SPBC32H8.02c","SPAC31A2.11c","SPBC28F2.10c","SPAPJ698.02c","SPAC25B8.18","SPAC824.02","SPAC589.07c","SPAC3H8.05c","SPBC216.05","SPBC16D10.07c","SPAC4G8.10","SPCC594.04c","SPAC16E8.01","SPAC4F10.04","SPAC25H1.03","SPCC1450.08c","SPCC576.12c","SPAC10F6.16","SPAC7D4.12c","SPAC1556.05c","SPAC19B12.08","SPAC30.02c","SPCPJ732.01","SPAC26A3.07c","SPBC1861.07","SPAC7D4.04","SPCC895.07","SPAC15A10.03c","SPAC23C11.10","SPAC24B11.06c","SPAC3H1.12c","SPBC725.14","SPAC11E3.01c","SPBC947.02","SPBC16D10.08c","SPBC1778.01c","SPCC553.08c","SPBC1D7.03","SPAC1783.06c","SPBC337.11","SPAC23C11.15","SPBC14F5.03c","SPBC1271.12","SPCC306.04c","SPAC823.16c","SPAC13G6.10c","SPAC19D5.03","SPAC227.04","SPBC3B8.02","SPAC11G7.04","SPCC417.09c","SPBC3H7.10","SPBC32F12.05c","SPAC4F10.07c","SPAC9G1.07","SPAC1D4.06c","SPBC14C8.17c","SPBC1921.07c","SPAC3C7.03c","SPBC609.02","SPAC18G6.05c","SPBC1D7.05","SPAC17G8.13c","SPBC3H7.12","SPBC713.07c","SPBC29B5.02c","SPAC25H1.05","SPAC13G6.09","SPBC19C2.04c","SPCC31H12.03c","SPBC16A3.17c","SPAC20H4.07","SPAC31G5.09c","SPBC36B7.08c","SPBC800.03","SPAC1F8.03c","SPCC188.07","SPAC1071.07c","SPCC338.08","SPAC1782.09c","SPBC2F12.03c","SPBP4H10.03","SPCC794.11c","SPBC1773.12","SPBC4B4.10c","SPCC11E10.06c","SPAC3G9.07c","SPBC8D2.17","SPAC23D3.09","SPCC31H12.05c","SPBC1711.03","SPAC328.05","SPAC23E2.03c","SPCC338.16","SPAC25A8.02","SPBC25H2.15","SPAC16A10.03c","SPBC23G7.08c","SPBC119.12","SPAC139.03","SPBC21.05c","SPAC2C4.07c","SPAC20G4.02c","SPAC4C5.02c","SPAC31G5.19","SPBC15D4.07c","SPBC18H10.19","SPBC12C2.02c","SPAC110.02","SPBC30B4.04c","SPBC28F2.12","SPBC30D10.13c","SPAC2F3.15","SPBC29A3.13","SPCC1682.01","SPAC630.14c","SPAC4A8.09c","SPBC19G7.04","SPCC736.06","SPAC458.06","SPBC21B10.13c","SPBC31F10.13c","SPBC902.03","SPAC9G1.11c","SPAC31A2.02","SPAC688.11","SPBC27B12.11c","SPBC27B12.08","SPAC1782.05","SPBC4B4.03","SPBC4B4.04","SPAC824.04","SPAC4A8.10","SPAC3H8.02","SPBC18H10.06c","SPAC144.02","SPCC1235.09","SPBC1703.12","SPCC1442.01"],"gene_count":157,"ltp_gene_count":5},{"uniquename":"PMID:15229228","title":"Homo-oligomerization is the essential function of the tandem BRCT domains in the checkpoint protein Crb2.","citation":"J Biol Chem 2004 Sep 10;279(37):38409-14","abstract":"BRCT (BRCA1 C terminus) domains are frequently found as a tandem repeat in proteins involved in DNA damage responses, such as Saccharomyces cerevisiae Rad9, human 53BP1 and BRCA1. Tandem BRCT domains mediate protein-protein and protein-DNA interactions. However, the functional significance of these interactions is largely unknown. Here we report the oligomerization of Schizosaccharomyces pombe checkpoint protein Crb2 through its tandem BRCT domains. Truncated Crb2 without BRCT domains is defective in DNA damage checkpoint signaling. However, addition of either of two heterologous dimerization motifs largely restores the functions of truncated Crb2 without BRCT domains. Replacement of Crb2 BRCT domains with a dimerization motif also renders cells resistant to the dominant negative effect of overexpressing Crb2 BRCT domains. These results demonstrate that the crucial function of the tandem BRCT domains is to oligomerize Crb2.","authors":"Du LL, Moser BA, Russell P","authors_abbrev":"Du LL et al.","pubmed_publication_date":"10 Sep 2004","pubmed_entrez_date":"2004-07-02","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC342.05","SPBC216.05","SPCC1259.13","SPAC9E9.08","SPAC23C4.18c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:21478005","title":"Common ground: small RNA programming and chromatin modifications.","citation":"Curr Opin Cell Biol 2011 Jun;23(3):258-65","abstract":"Epigenetic mechanisms regulate genome structure and expression profiles in eukaryotes. RNA interference (RNAi) and other small RNA-based chromatin-modifying activities can act to reset the epigenetic landscape at defined chromatin domains. Centromeric heterochromatin assembly is a RNAi-dependent process in the fission yeast Schizosaccharomyces pombe, and provides a paradigm for detailed examination of such epigenetic processes. Here we review recent progress in understanding the mechanisms that underpin RNAi-mediated heterochromatin formation in S. pombe. We discuss recent analyses of the events that trigger RNAi and manipulations which uncouple RNAi and chromatin modification. Finally we provide an overview of similar molecular machineries across species where related small RNA pathways appear to drive the epigenetic reprogramming in germ cells and/or during early development in metazoans.","doi":"10.1016/j.ceb.2011.03.005","authors":"Lejeune E, Allshire RC","authors_abbrev":"Lejeune E et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-04-12","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR14445","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F10.13c","HGNC:11960","HGNC:9126"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9752720","title":"Genetic regulation of phospholipid metabolism: yeast as a model eukaryote.","citation":"Prog Nucleic Acid Res Mol Biol 1998;61:133-79","abstract":"Baker's yeast, Saccharomyces cerevisiae, is an excellent and an increasingly important model for the study of fundamental questions in eukaryotic cell biology and genetic regulation. The fission yeast, Schizosaccharomyces pombe, although not as intensively studied as S. cerevisiae, also has many advantages as a model system. In this review, we discuss progress over the past several decades in biochemical and molecular genetic studies of the regulation of phospholipid metabolism in these two organisms and higher eukaryotes. In S. cerevisiae, following the recent completion of the yeast genome project, a very high percentage of the gene-enzyme relationships in phospholipid metabolism have been assigned and the remaining assignments are expected to be completed rapidly. Complex transcriptional regulation, sensitive to the availability of phospholipid precusors, as well as growth phase, coordinates the expression of the structural genes encoding these enzymes in S. cerevisiae. In this article, this regulation is described, the mechanism by which the cell senses the ongoing metabolic activity in the pathways for phospholipid biosynthesis is discussed, and a model is presented. Recent information relating to the role of phosphatidylcholine turnover in S. cerevisiae and its relationship to the secretory pathway, as well as to the regulation of phospholipid metabolism, is also presented. Similarities in the role of phospholipase D-mediated phosphatidylcholine turnover in the secretory process in yeast and mammals lend further credence to yeast as a model system.","authors":"Henry SA, Patton-Vogt JL","authors_abbrev":"Henry SA et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-09-30","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16009511","title":"A DNA binding motif of meiotic recombinase Rec12 (Spo11) defined by essential glycine-202, and persistence of Rec12 protein after completion of recombination.","citation":"Gene 2005 Aug 15;356:77-84","abstract":"The Rec12 (Spo11) protein of the fission yeast Schizosaccharomyces pombe is a meiosis-specific ortholog of the catalytic subunit of type VI topoisomerases and is thought to catalyze double-strand DNA breaks that initiate recombination. We tested the hypothesis that the rec12-117 allele affects the choice of pathways by which recombination is resolved. DNA sequence analysis revealed a single missense mutation in the coding region (rec12-G202E). The corresponding glycine-202 residue of Rec12 protein is strictly conserved in proteins of the Rec12/Spo11/Top6A family. It maps to the base of the DNA binding pocket in the crystal structure of the archaeal ortholog, Top6A. The rec12-G202E mutants lacked crossover and non-crossover recombination, demonstrating that rec12-G202E does not affect choice of resolution pathway. Like rec12-D15 null mutants, the rec12-G202E mutants suffered chromosome segregation errors in meiosis I. The Rec12-G202E protein was as stable as wild-type Rec12, demonstrating that glycine-202 is essential for a biochemical activity of Rec12 protein, rather than for its stability. These findings suggest that Rec12 facilitates binding of the meiotic recombinase to its substrate, DNA. Interestingly, the bulk of Rec12 protein persisted until the time of anaphase I, and a portion of Rec12 protein persisted until the time of anaphase II, after which it was undetectable. This suggests that Rec12 protein has additional meiotic functions after completion of recombination in prophase, as inferred previously from genetic studies [Sharif, W.D., Glick, G.G., Davidson, M.K., Wahls, W.P., 2002. Distinct functions of S. pombe Rec12 (Spo11) protein and Rec12-dependent crossover recombination (chiasmata) in meiosis I; and a requirement for Rec12 in meiosis II. Cell Chromo. 1, 1].","authors":"DeWall KM, Davidson MK, Sharif WD, Wiley CA, Wahls WP","authors_abbrev":"DeWall KM et al.","pubmed_publication_date":"15 Aug 2005","pubmed_entrez_date":"2005-07-13","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17668038","title":"Cellular functions and transcriptional regulation of a third thioredoxin from Schizosaccharomyces pombe.","citation":"Can J Microbiol 2007 Jun;53(6):775-83","abstract":"The structural gene encoding a third thioredoxin (Trx) homologue, TRX3, of the fission yeast Schizosaccharomyces pombe was characterized and its regulation was studied. The determined DNA sequence encoded a putative 290 amino acid sequence of Trx with a molecular mass of 31,889 Da. The TRX3 mRNA level was increased in S. pombe cells harboring plasmid pTRX3, suggesting that the cloned TRX3 gene was functional. Yeast cultures harbouring plasmid pTRX3 exhibited shorter generation times and higher survival on solid minimal media plates incorporating mercury chloride (0.01 mmol/L) or hydrogen peroxide (1 mmol/L) compared with control cultures. Yeast cells containing extra copies of TRX3, but not TRX1 and TRX2, gave rise to lower reactive oxygen species levels than control cells. Oxidative stress owing to hydrogen peroxide and menadione enhanced the synthesis of beta-galactosidase from the TRX3-lacZ fusion gene in Pap1-positive cells but not in Pap1-negative cells. The TRX3 mRNA level was increased by oxidative stress only in Pap1-positive cells. Basal expression of the TRX3 gene also depended on Pap1. We concluded that S. pombe TRX3 is linked with yeast growth and oxidative stress response, with its expression being regulated by oxidative stress in a Pap1-dependent manner.","authors":"Kim SJ, Jung EM, Jung HJ, Song YS, Park EH, Lim CJ","authors_abbrev":"Kim SJ et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-08-02","publication_year":"2007","canto_session_key":"a6dfc0e19bdd277d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-04 15:38:17","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-04 15:38:07","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPBC577.08c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-12-04"},{"uniquename":"PMID:41498132","title":"Probing the proteome.","citation":"Elife 2026 Jan 07;15","abstract":"Raman spectroscopy can be used to predict cellular physiology and proteome composition in  E. coli .","doi":"10.7554/eLife.110102","authors":"Lin WH, Cheng CL","authors_abbrev":"Lin WH et al.","pubmed_publication_date":"07 Jan 2026","pubmed_entrez_date":"2026-01-07","publication_year":"2026","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2026-01-08 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18054176","title":"Gene tagging and gene replacement using recombinase-mediated cassette exchange in Schizosaccharomyces pombe.","citation":"Gene 2008 Jan 15;407(1-2):63-74","abstract":"Cre/lox site-specific recombination systems provide important tools for genetic manipulation. Here we present an efficient method for gene tagging and gene replacement using Cre recombinase-mediated cassette exchange (RMCE). The cassette consists of the S. pombe ura4(+) selectable marker flanked by a wild-type loxP site at one end and by a modified heterospecific lox site (loxM3) at the other. The cassette is stable because the flanking lox sites cannot recombine with each other. Following integration of the cassette at the chosen chromosomal locus, exchange is achieved by introducing a Cre-expression plasmid containing an equivalent cassette containing the required tag or gene sequence. Recombinants are selected by uracil prototrophy using the reagent 5-fluoroorotic acid (5-FOA). The cassette exchange system provides for repetitive integrations at the same locus, allowing different protein tags or gene sequences to be integrated quickly and efficiently. We have established a range of reagents and verified utility by C-terminally tagging the S. pombe rad4 and swi1 genes with yEGFP and the yEGFP derivatives yECFP and yECitrine and by transferring the coding sequence for both genes.","authors":"Watson AT, Garcia V, Bone N, Carr AM, Armstrong J","authors_abbrev":"Watson AT et al.","pubmed_publication_date":"15 Jan 2008","pubmed_entrez_date":"2007-12-07","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19593452","title":"Explaining lengths and shapes of yeast by scaling arguments.","citation":"PLoS One 2009 Jul 10;4(7):e6205","abstract":"Lengths and shapes are approached in different ways in different fields: they serve as a read-out for classifying genes or proteins in cell biology whereas they result from scaling arguments in condensed matter physics. Here, we propose a combined approach with examples illustrated for the fission yeast Schizosaccharomyces pombe.","doi":"10.1371/journal.pone.0006205","authors":"Riveline D","authors_abbrev":"Riveline D","pubmed_publication_date":"10 Jul 2009","pubmed_entrez_date":"2009-07-14","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF09814","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC119.16c","HGNC:29472"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23737303","title":"Coexpression of CPR from various origins enhances biotransformation activity of human CYPs in S. pombe.","citation":"Appl Biochem Biotechnol 2013 Aug;170(7):1751-66","abstract":"Cytochrome P450 enzymes (CYPs or P450s) are the most important enzymes involved in the phase I metabolism of drugs (and other xenobiotics) in humans, and the corresponding drug metabolites are needed as reference substances for their structural confirmation and for pharmacological or toxicological characterization. We have previously shown that biotechnological synthesis of such metabolites is feasible by whole-cell biotransformation with human CYPs recombinantly expressed in the fission yeast Schizosaccharomyces pombe. It was the aim of this study to compare the activity of seven human microsomal CYPs (CYP2C9, CYP2D6, CYP3A4, CYP3A5, CYP3A7, CYP17, and CYP21) upon coexpression with NADPH-cytochrome P450 oxidoreductases (CPRs) from various origins, namely, human CPR (hCPR) and its homologues from fission yeast (ccr1) and the bishop's weed Ammi majus (AmCPR), respectively. For this purpose, 28 recombinant strains were needed, with five of them having been constructed previously and 23 strains being newly constructed. Bioconversion experiments showed that coexpression of a CPR does not only influence the reaction rate but, in some cases, also exerts an influence on the metabolite pattern. For CYP3A enzymes, coexpression of hCPR yielded the best results, while for another two, hCPR was equally helpful as ccr1 (both CYP17 and CYP21) or AmCPR (CYP17 only), respectively. Interestingly, CYP2D6 displayed its highest activity when coexpressed with ccr1 and CYP2C9 with AmCPR. These results corroborate the view of CPR as a well-suited bio-brick in synthetic biology for the construction of artificial enzyme complexes.","doi":"10.1007/s12010-013-0303-2","authors":"Neunzig I, Widjaja M, Peters FT, Maurer HH, Hehn A, Bourgaud F, Bureik M","authors_abbrev":"Neunzig I et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-06-06","publication_year":"2013","canto_session_key":"8d9b09ddc7e7e061","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-08-29 09:06:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-08-20 19:53:06","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-08-20"},{"uniquename":"PMID:9740805","title":"A new large proteolytic complex distinct from the proteasome is present in the cytosol of fission yeast.","citation":"Curr Biol 1998 Sep 10;8(18):1023-6","abstract":"One eukaryotic proteolytic complex--the proteasome--is classed as the major nonlysosomal protease, by its known and suspected functions, its size and its complexity. It seems improbable that other enzymes may be capable of substituting, even partially, for the potent proteasome, as this complex has a vital role in many cellular processes. Nevertheless, it is possible to adapt cultured EL-4 mouse lymphoma cells to survive in the presence of a specific inhibitor of the proteasome. The inhibition of the proteasome in these adapted EL-4 cells is accompanied by a dramatic increase in the activity of a new, as yet uncharacterized, large proteolytic complex. Here, we have presented evidence that a similar proteolytic activity is constitutively present in fission yeast, Schizosaccharomyces pombe, and that the yeast and mouse enzymes share basic physicochemical properties. We have shown that the S. pombe protease is found in two stable oligomeric forms, both of which are peptidases, although only the larger form acts as a proteinase. The relative amounts of the large and the small forms of the protease in the complex depended on the growth phase of the yeast culture and affected enzyme activity, suggesting that the activity of the enzyme is regulated by its oligomerization status. We refer to the new proteolytic complex as the 'multicorn' to indicate its analogy to the archaebacterial tricorn protease.","authors":"Osmulski PA, Gaczynska M","authors_abbrev":"Osmulski PA et al.","pubmed_publication_date":"10 Sep 1998","pubmed_entrez_date":"1998-09-19","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP8A3.12c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:28242692","title":"LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells.","citation":"Proc Natl Acad Sci U S A 2017 Mar 14;114(11):E2166-E2175","abstract":"Endosomal sorting complexes required for transport III (ESCRT-III) proteins have been implicated in sealing the nuclear envelope in mammals, spindle pole body dynamics in fission yeast, and surveillance of defective nuclear pore complexes in budding yeast. Here, we report that Lem2p (LEM2), a member of the LEM (Lap2-Emerin-Man1) family of inner nuclear membrane proteins, and the ESCRT-II/ESCRT-III hybrid protein Cmp7p (CHMP7), work together to recruit additional ESCRT-III proteins to holes in the nuclear membrane. In  Schizosaccharomyces pombe , deletion of the ATPase  vps4  leads to severe defects in nuclear morphology and integrity. These phenotypes are suppressed by loss-of-function mutations that arise spontaneously in  lem2  or  cmp7 , implying that these proteins may function upstream in the same pathway. Building on these genetic interactions, we explored the role of LEM2 during nuclear envelope reformation in human cells. We found that CHMP7 and LEM2 enrich at the same region of the chromatin disk periphery during this window of cell division and that CHMP7 can bind directly to the C-terminal domain of LEM2 in vitro. We further found that, during nuclear envelope formation, recruitment of the ESCRT factors CHMP7, CHMP2A, and IST1/CHMP8 all depend on LEM2 in human cells. We conclude that Lem2p/LEM2 is a conserved nuclear site-specific adaptor that recruits Cmp7p/CHMP7 and downstream ESCRT factors to the nuclear envelope.","doi":"10.1073/pnas.1613916114","authors":"Gu M, LaJoie D, Chen OS, von Appen A, Ladinsky MS, Redd MJ, Nikolova L, Bjorkman PJ, Sundquist WI, Ullman KS, Frost A","authors_abbrev":"Gu M et al.","pubmed_publication_date":"14 Mar 2017","pubmed_entrez_date":"2017-03-01","publication_year":"2017","canto_session_key":"83bb6f203d9fe65a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Adam Frost","canto_first_approved_date":"2017-05-24 11:18:12","canto_approved_date":"2023-06-08 10:33:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-28 17:29:41","canto_added_date":"2017-03-02 01:15:13","annotation_curators":[{"name":"Adam Frost","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.18c","SPAC18G6.10","SPAC2G11.06"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-05-24"},{"uniquename":"PMID:21540880","title":"Evolutionary genomics: fission yeast compared and contrasted.","citation":"Nat Rev Genet 2011 Jun;12(6):381","abstract":"","doi":"10.1038/nrg3006","authors":"Muers M","authors_abbrev":"Muers M","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-05-05","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10021358","title":"Meiosis: MeiRNA hits the spot.","citation":"Curr Biol 1999 Jan 28;9(2):R66-9","abstract":"The protein Mei2 performs at least two functions required in fission yeast for the switch from mitotic to meiotic cell cycles. One of these functions also requires meiRNA. It appears that meiRNA targets Mei2 to the nucleus, where it can promote the first meiotic division.","authors":"Ohno M, Mattaj IW","authors_abbrev":"Ohno M et al.","pubmed_publication_date":"28 Jan 1999","pubmed_entrez_date":"1999-02-18","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29992245","title":"Fission yeast telosomes: non-canonical histone-containing chromatin structures dependent on shelterin and RNA.","citation":"Nucleic Acids Res 2018 Sep 28;46(17):8865-8875","abstract":"Despite the prime importance of telomeres in chromosome stability, significant mysteries surround the architecture of telomeric chromatin. Through micrococcal nuclease mapping, we show that fission yeast chromosome ends are assembled into distinct protected structures ('telosomes') encompassing the telomeric DNA repeats and over half a kilobase of subtelomeric DNA. Telosome formation depends on the conserved telomeric proteins Taz1 and Rap1, and surprisingly, RNA. Although yeast telomeres have long been thought to be free of histones, we show that this is not the case; telomere repeats contain histones. While telomeric histone H3 bears the heterochromatic lys9-methyl mark, we show that this mark is dispensable for telosome formation. Therefore, telomeric chromatin is organized at an architectural level, in which telomere-binding proteins and RNAs impose a unique nucleosome arrangement, and a second level, in which histone modifications are superimposed upon the higher order architecture.","doi":"10.1093/nar/gky605","authors":"Greenwood J, Patel H, Cech TR, Cooper JP","authors_abbrev":"Greenwood J et al.","pubmed_publication_date":"28 Sep 2018","pubmed_entrez_date":"2018-07-12","publication_year":"2018","canto_session_key":"9618709463d9799d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-07-13 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25533348","title":"Tolerance of deregulated G1/S transcription depends on critical G1/S regulon genes to prevent catastrophic genome instability.","citation":"Cell Rep 2014 Dec 24;9(6):2279-89","abstract":"Expression of a G1/S regulon of genes that are required for DNA replication is a ubiquitous mechanism for controlling cell proliferation; moreover, the pathological deregulated expression of E2F-regulated G1/S genes is found in every type of cancer. Cellular tolerance of deregulated G1/S transcription is surprising because this regulon includes many dosage-sensitive proteins. Here, we used the fission yeast Schizosaccharomyces pombe to investigate this issue. We report that deregulating the MBF G1/S regulon by eliminating the Nrm1 corepressor increases replication errors. Homology-directed repair proteins, including MBF-regulated Ctp1(CtIP), are essential to prevent catastrophic genome instability. Surprisingly, the normally inconsequential MBF-regulated S-phase cyclin Cig2 also becomes essential in the absence of Nrm1. This requirement was traced to cyclin-dependent kinase inhibition of the MBF-regulated Cdc18(Cdc6) replication origin-licensing factor. Collectively, these results establish that, although deregulation of G1/S transcription is well tolerated by cells, nonessential G1/S target genes become crucial for preventing catastrophic genome instability.","doi":"10.1016/j.celrep.2014.11.039","authors":"Caetano C, Limbo O, Farmer S, Klier S, Dovey C, Russell P, de Bruin RA","authors_abbrev":"Caetano C et al.","pubmed_publication_date":"24 Dec 2014","pubmed_entrez_date":"2014-12-24","publication_year":"2014","canto_session_key":"7e83e3410ced8531","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rob De Bruin","canto_first_approved_date":"2018-03-26 12:25:29","canto_approved_date":"2026-01-15 08:59:16","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-11-03 20:31:53","canto_added_date":"2014-12-25 01:15:27","annotation_curators":[{"name":"Rob De Bruin","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":56,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC30D11.10","SPAPB2B4.03","SPAC644.14c","SPBC21B10.13c","SPBC725.16","SPCC553.07c","SPAC1F7.05","SPBC16A3.07c","SPAC17H9.19c","SPAC22F3.09c","SPBC660.14","SPBC14C8.07c","SPBC428.18","SPAC13C5.07","SPAC644.05c","SPAP14E8.02","SPCC338.17c","SPCC4G3.05c","SPCC338.08"],"gene_count":20,"ltp_gene_count":12,"approved_date":"2018-03-26"},{"uniquename":"PMID:28749973","title":"Replication stress affects the fidelity of nucleosome-mediated epigenetic inheritance.","citation":"PLoS Genet 2017 Jul;13(7):e1006900","abstract":"The fidelity of epigenetic inheritance or, the precision by which epigenetic information is passed along, is an essential parameter for measuring the effectiveness of the process. How the precision of the process is achieved or modulated, however, remains largely elusive. We have performed quantitative measurement of epigenetic fidelity, using position effect variegation (PEV) in Schizosaccharomyces pombe as readout, to explore whether replication perturbation affects nucleosome-mediated epigenetic inheritance. We show that replication stresses, due to either hydroxyurea treatment or various forms of genetic lesions of the replication machinery, reduce the inheritance accuracy of CENP-A/Cnp1 nucleosome positioning within centromere. Mechanistically, we demonstrate that excessive formation of single-stranded DNA, a common molecular abnormality under these conditions, might have correlation with the reduction in fidelity of centromeric chromatin duplication. Furthermore, we show that replication stress broadly changes chromatin structure at various loci in the genome, such as telomere heterochromatin expanding and mating type locus heterochromatin spreading out of the boundaries. Interestingly, the levels of inheritable expanding at sub-telomeric heterochromatin regions are highly variable among independent cell populations. Finally, we show that HU treatment of the multi-cellular organisms C. elegans and D. melanogaster affects epigenetically programmed development and PEV, illustrating the evolutionary conservation of the phenomenon. Replication stress, in addition to its demonstrated role in genetic instability, promotes variable epigenetic instability throughout the epigenome.","doi":"10.1371/journal.pgen.1006900","authors":"Li W, Yi J, Agbu P, Zhou Z, Kelley RL, Kallgren S, Jia S, He X","authors_abbrev":"Li W et al.","pubmed_publication_date":"Jul 2017","pubmed_entrez_date":"2017-07-28","publication_year":"2017","canto_session_key":"5e36c5a5666b74e6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-07-29 00:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26182403","title":"The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the ABC protein Rli1 for iron-sulfur cluster insertion.","citation":"Elife 2015 Jul 16;4:e08231","abstract":"Cytosolic and nuclear iron-sulfur (Fe-S) proteins are involved in many essential pathways including translation and DNA maintenance. Their maturation requires the cytosolic Fe-S protein assembly (CIA) machinery. To identify new CIA proteins we employed systematic protein interaction approaches and discovered the essential proteins Yae1 and Lto1 as binding partners of the CIA targeting complex. Depletion of Yae1 or Lto1 results in defective Fe-S maturation of the ribosome-associated ABC protein Rli1, but surprisingly no other tested targets. Yae1 and Lto1 facilitate Fe-S cluster assembly on Rli1 in a chain of binding events. Lto1 uses its conserved C-terminal tryptophan for binding the CIA targeting complex, the deca-GX3 motifs in both Yae1 and Lto1 facilitate their complex formation, and Yae1 recruits Rli1. Human YAE1D1 and the cancer-related ORAOV1 can replace their yeast counterparts demonstrating evolutionary conservation. Collectively, the Yae1-Lto1 complex functions as a target-specific adaptor that recruits apo-Rli1 to the generic CIA machinery.","doi":"10.7554/eLife.08231","authors":"Paul VD, Mühlenhoff U, Stümpfig M, Seebacher J, Kugler KG, Renicke C, Taxis C, Gavin AC, Pierik AJ, Lill R","authors_abbrev":"Paul VD et al.","pubmed_publication_date":"16 Jul 2015","pubmed_entrez_date":"2015-07-17","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC191.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35954225","title":"Differential Paralog-Specific Expression of Multiple Small Subunit Proteins Cause Variations in Rpl42/eL42 Incorporation in Ribosome in Fission Yeast.","citation":"Cells 2022 Aug 02;11(15)","abstract":"Ribosomes within a cell are commonly viewed as biochemically homogenous RNA-protein super-complexes performing identical functions of protein synthesis. However, recent evidence suggests that ribosomes may be a more dynamic macromolecular complex with specialized roles. Here, we present extensive genetic and molecular evidence in the fission yeast  S. pombe  that the paralogous genes for many ribosomal proteins (RPs) are functionally different, despite that they encode the same ribosomal component, often with only subtle differences in the sequences. Focusing on the  rps8  paralog gene deletions  rps801d  and  rps802d , we showed that the mutant cells differ in the level of Rpl42p in actively translating ribosomes and that their phenotypic differences reside in the Rpl42p level variation instead of the subtle protein sequence difference between Rps801p and Rps802p. Additional 40S ribosomal protein paralog pairs also exhibit similar phenotypic differences via differential Rpl42p levels in actively translating ribosomes. Together, our work identifies variations in the Rpl42p level as a potential form of ribosome heterogeneity in biochemical compositions and suggests a possible connection between large and small subunits during ribosome biogenesis that may cause such heterogeneity. Additionally, it illustrates the complexity of the underlying mechanisms for the genetic specificity of ribosome paralogs.","doi":"10.3390/cells11152381","authors":"Li W, Zhang J, Cheng W, Li Y, Feng J, Qin J, He X","authors_abbrev":"Li W et al.","pubmed_publication_date":"02 Aug 2022","pubmed_entrez_date":"2022-08-12","publication_year":"2022","canto_session_key":"df506d60f86df0da","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-08-14 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7003311","title":"Genetic analysis of resistant mutants to antimitotic benzimidazole compounds in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1980;180(1):231-4","abstract":"Mutants resistant to the antimitotic compounds thiabendazole and methyl-2-benzimidazole-carbamate were isolated and analyzed genetically in the fission yeast. Schizosaccharomyces pombe. They comprised three groups in terms of genetic linkage. Mutants in one linkage group (ben1) differed phenotypically from those in the other two (ben2 and ben3). The former were resistant to the compounds at any physiological temperature tested, whereas the latter exhibited temperature dependent resistance. Through tetrad analysis, ben1 was mapped at the rightmost part of chromosome II, and ben2 was mapped near the centromere of the same chromosome. Haploidization experiments revealed the location of ben3 on chromosome II. By analogy with Aspergillus nidulans, it is suggested that one of these ben genes may code for tubulin.","authors":"Yamamoto M","authors_abbrev":"Yamamoto M","pubmed_publication_date":"1980","pubmed_entrez_date":"1980-01-01","publication_year":"1980","canto_session_key":"5c1c72c4c8850e21","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-30 13:04:39","canto_approved_date":"2023-10-05 20:25:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-30 13:04:31","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-30"},{"uniquename":"PMID:27010073","title":"dbPAF: an integrative database of protein phosphorylation in animals and fungi.","citation":"Sci Rep 2016 Mar 24;6:23534","abstract":"Protein phosphorylation is one of the most important post-translational modifications (PTMs) and regulates a broad spectrum of biological processes. Recent progresses in phosphoproteomic identifications have generated a flood of phosphorylation sites, while the integration of these sites is an urgent need. In this work, we developed a curated database of dbPAF, containing known phosphorylation sites in H. sapiens, M. musculus, R. norvegicus, D. melanogaster, C. elegans, S. pombe and S. cerevisiae. From the scientific literature and public databases, we totally collected and integrated 54,148 phosphoproteins with 483,001 phosphorylation sites. Multiple options were provided for accessing the data, while original references and other annotations were also present for each phosphoprotein. Based on the new data set, we computationally detected significantly over-represented sequence motifs around phosphorylation sites, predicted potential kinases that are responsible for the modification of collected phospho-sites, and evolutionarily analyzed phosphorylation conservation states across different species. Besides to be largely consistent with previous reports, our results also proposed new features of phospho-regulation. Taken together, our database can be useful for further analyses of protein phosphorylation in human and other model organisms. The dbPAF database was implemented in PHP + MySQL and freely available at http://dbpaf.biocuckoo.org.","doi":"10.1038/srep23534","authors":"Ullah S, Lin S, Xu Y, Deng W, Ma L, Zhang Y, Liu Z, Xue Y","authors_abbrev":"Ullah S et al.","pubmed_publication_date":"24 Mar 2016","pubmed_entrez_date":"2016-03-25","publication_year":"2016","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2016-03-29 00:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23401002","title":"Microtubule-organizing center formation at telomeres induces meiotic telomere clustering.","citation":"J Cell Biol 2013 Feb 18;200(4):385-95","abstract":"During meiosis, telomeres cluster and promote homologous chromosome pairing. Telomere clustering requires the interaction of telomeres with the nuclear membrane proteins SUN (Sad1/UNC-84) and KASH (Klarsicht/ANC-1/Syne homology). The mechanism by which telomeres gather remains elusive. In this paper, we show that telomere clustering in fission yeast depends on microtubules and the microtubule motors, cytoplasmic dynein, and kinesins. Furthermore, the γ-tubulin complex (γ-TuC) is recruited to SUN- and KASH-localized telomeres to form a novel microtubule-organizing center that we termed the \"telocentrosome.\" Telocentrosome formation depends on the γ-TuC regulator Mto1 and on the KASH protein Kms1, and depletion of either Mto1 or Kms1 caused severe telomere clustering defects. In addition, the dynein light chain (DLC) contributes to telocentrosome formation, and simultaneous depletion of DLC and dynein also caused severe clustering defects. Thus, the telocentrosome is essential for telomere clustering. We propose that telomere-localized SUN and KASH induce telocentrosome formation and that subsequent microtubule motor-dependent aggregation of telocentrosomes via the telocentrosome-nucleated microtubules causes telomere clustering.","doi":"10.1083/jcb.201207168","authors":"Yoshida M, Katsuyama S, Tateho K, Nakamura H, Miyoshi J, Ohba T, Matsuhara H, Miki F, Okazaki K, Haraguchi T, Niwa O, Hiraoka Y, Yamamoto A","authors_abbrev":"Yoshida M et al.","pubmed_publication_date":"18 Feb 2013","pubmed_entrez_date":"2013-02-13","publication_year":"2013","canto_session_key":"88a4bf2bfec84d82","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPAC1805.08"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:19194460","title":"Structure and function of the 5'-->3' exoribonuclease Rat1 and its activating partner Rai1.","citation":"Nature 2009 Apr 09;458(7239):784-8","abstract":"The 5'-->3' exoribonucleases (XRNs) comprise a large family of conserved enzymes in eukaryotes with crucial functions in RNA metabolism and RNA interference. XRN2, or Rat1 in yeast, functions primarily in the nucleus and also has an important role in transcription termination by RNA polymerase II (refs 7-14). Rat1 exoribonuclease activity is stimulated by the protein Rai1 (refs 15, 16). Here we report the crystal structure at 2.2 A resolution of Schizosaccharomyces pombe Rat1 in complex with Rai1, as well as the structures of Rai1 and its murine homologue Dom3Z alone at 2.0 A resolution. The structures reveal the molecular mechanism for the activation of Rat1 by Rai1 and for the exclusive exoribonuclease activity of Rat1. Biochemical studies confirm these observations, and show that Rai1 allows Rat1 to degrade RNAs with stable secondary structure more effectively. There are large differences in the active site landscape of Rat1 compared to related and PIN (PilT N terminus) domain-containing nucleases. Unexpectedly, we identified a large pocket in Rai1 and Dom3Z that contains highly conserved residues, including three acidic side chains that coordinate a divalent cation. Mutagenesis and biochemical studies demonstrate that Rai1 possesses pyrophosphohydrolase activity towards 5' triphosphorylated RNA. Such an activity is important for messenger RNA degradation in bacteria, but this is, to our knowledge, the first demonstration of this activity in eukaryotes and suggests that Rai1/Dom3Z may have additional important functions in RNA metabolism.","doi":"10.1038/nature07731","authors":"Xiang S, Cooper-Morgan A, Jiao X, Kiledjian M, Manley JL, Tong L","authors_abbrev":"Xiang S et al.","pubmed_publication_date":"09 Apr 2009","pubmed_entrez_date":"2009-02-06","publication_year":"2009","canto_session_key":"ccfd255382e7cb51","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-18 03:07:36","canto_approved_date":"2023-02-15 14:09:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-15 11:59:41","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.06c","SPAC26A3.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-01-18","pdb_entries":[{"pdb_id":"3fqd","gene_chains":[{"gene_uniquename":"SPAC19D5.06c","chain":"B","position":"1-352"},{"gene_uniquename":"SPAC26A3.12c","chain":"A","position":"1-885"}],"title":"Crystal Structure of the S. pombe Rat1-Rai1 Complex","entry_authors":"Xiang S,Tong L","entry_authors_abbrev":"Xiang S et al.","reference_uniquename":"PMID:19194460","experimental_method":"X-ray","resolution":"2.2"},{"pdb_id":"3fqg","gene_chains":[{"gene_uniquename":"SPAC19D5.06c","chain":"A","position":"1-352"}],"title":"Crystal Structure of the S. pombe Rai1","entry_authors":"Xiang S,Tong L","entry_authors_abbrev":"Xiang S et al.","reference_uniquename":"PMID:19194460","experimental_method":"X-ray","resolution":"2.0"}]},{"uniquename":"EMBL:X85040","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013449","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17409356","title":"Mitotic chromosome biorientation in fission yeast is enhanced by dynein and a minus-end-directed, kinesin-like protein.","citation":"Mol Biol Cell 2007 Jun;18(6):2216-25","abstract":"Chromosome biorientation, the attachment of sister kinetochores to sister spindle poles, is vitally important for accurate chromosome segregation. We have studied this process by following the congression of pole-proximal kinetochores and their subsequent anaphase segregation in fission yeast cells that carry deletions in any or all of this organism's minus end-directed, microtubule-dependent motors: two related kinesin 14s (Pkl1p and Klp2p) and dynein. None of these deletions abolished biorientation, but fewer chromosomes segregated normally without Pkl1p, and to a lesser degree without dynein, than in wild-type cells. In the absence of Pkl1p, which normally localizes to the spindle and its poles, the checkpoint that monitors chromosome biorientation was defective, leading to frequent precocious anaphase. Ultrastructural analysis of mutant mitotic spindles suggests that Pkl1p contributes to error-free biorientation by promoting normal spindle pole organization, whereas dynein helps to anchor a focused bundle of spindle microtubules at the pole.","authors":"Grishchuk EL, Spiridonov IS, McIntosh JR","authors_abbrev":"Grishchuk EL et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-04-06","publication_year":"2007","canto_session_key":"4e4f96374eeb7691","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.10","SPAC3A11.14c","SPAC1093.06c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10648145","title":"3D HCCH(3)-TOCSY for resonance assignment of methyl-containing side chains in (13)C-labeled proteins.","citation":"J Magn Reson 2000 Feb;142(2):288-93","abstract":"Two 3D experiments, (H)CCH(3)-TOCSY and H(C)CH(3)-TOCSY, are proposed for resonance assignment of methyl-containing amino acid side chains. After the initial proton-carbon INEPT step, during which either carbon or proton chemical shift labeling is achieved (t(1)), the magnetization is spread along the amino acid side chains by a carbon spin lock. The chemical shifts of methyl carbons are labeled (t(2)) during the following constant time interval. Finally the magnetization is transferred, in a reversed INEPT step, to methyl protons for detection (t(3)). The proposed experiments are characterized by high digital resolution in the methyl carbon dimension (t(2max) = 28.6 ms), optimum sensitivity due to the use of proton decoupling during the long constant time interval, and an optional removal of CH(2), or CH(2) and CH, resonances from the F(2)F(3) planes. The building blocks used in these experiments can be implemented in a range of heteronuclear experiments focusing on methyl resonances in proteins. The techniques are illustrated using a (15)N, (13)C-labeled E93D mutant of Schizosacharomyces pombe phosphoglycerate mutase (23.7 kDa).","authors":"Uhrín D, Uhrínová S, Leadbeater C, Nairn J, Price NC, Barlow PN","authors_abbrev":"Uhrín D et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-01-29","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33172987","title":"Fission yeast Opy1 is an endogenous PI(4,5)P 2  sensor that binds to the phosphatidylinositol 4-phosphate 5-kinase Its3.","citation":"J Cell Sci 2020 Dec 03;133(23)","abstract":"Phosphoinositides (PIPs) are a dynamic family of lipids that execute diverse roles in cell biology. PIP levels are regulated by numerous enzymes, but our understanding of how these enzymes are controlled in space and time is incomplete. One role of the PIP phosphatidylinositol (4,5)-bisphosphate [PI(4,5)P 2 ] is to anchor the cytokinetic ring (CR) to the plasma membrane (PM) in  Schizosaccharomyces pombe  While examining potential PI(4,5)P 2 -binding proteins for roles in CR anchoring, we identified the dual pleckstrin homology (PH) domain-containing protein Opy1. Although related proteins are implicated in PIP regulation, we found no role for  S. pombe  Opy1 in CR anchoring, which would be expected if it modulated PM PI(4,5)P 2  levels. Our data indicate that although Opy1 senses PM PI(4,5)P 2  levels and binds to the phosphatidylinositol 4-phosphate 5-kinase (PI5-kinase) Its3, Opy1 does not regulate Its3 kinase activity or PM PI(4,5)P 2  levels, a striking difference from its  Saccharomyces cerevisiae  homolog. However, overexpression of Opy1 resulted in cytokinesis defects, as might be expected if it sequestered PI(4,5)P 2  Our results highlight the evolutionary divergence of dual PH domain-containing proteins and the need for caution when interpreting results based on their overexpression.This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.247973","authors":"Snider CE, Willet AH, Brown HT, Chen JS, Evers JM, Gould KL","authors_abbrev":"Snider CE et al.","pubmed_publication_date":"03 Dec 2020","pubmed_entrez_date":"2020-11-11","publication_year":"2020","canto_session_key":"7574a76221b0ed26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chloe Snider","canto_first_approved_date":"2020-11-19 14:31:35","canto_approved_date":"2024-09-11 15:54:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-18 19:21:08","canto_added_date":"2020-11-13 01:15:05","annotation_curators":[{"name":"Chloe Snider","community_curator":true,"annotation_count":21,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.14","SPBC577.06c","SPBC2G2.02","SPBC577.13","SPCC794.08","SPCPB16A4.02c","SPAC9G1.10c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2020-11-19"},{"uniquename":"PMID:22542965","title":"Remarkably simple sequence requirement of the M-factor pheromone of Schizosaccharomyces pombe.","citation":"Genetics 2012 Jul;191(3):815-25","abstract":"The mating reaction is triggered by specific pheromones in a wide variety of organisms. Small peptides are used as mating pheromones in yeasts and fungi. In the fission yeast Schizosaccharomyces pombe, M-factor is a C terminally farnesylated nonapeptide secreted from M-cells, and its counterpart, P-factor, is a simple peptide composed of 23 amino acids. The primary structure requirements for the biological activity of pheromone peptides remain to be elucidated. Here, we conducted comprehensive substitution of each of the amino acids in M-factor peptide and inspected the mating ability of these missense mutants. Thirty-five sterile mutants were found among an array of 152 mutants with single amino acid substitutions. Mapping of the mutation sites clearly indicated that the sterile mutants were associated exclusively with four amino acid residues (VPYM) in the carboxyl-terminal half. In contrast, the substitution of four amino-terminal residues (YTPK) with any amino acid had no or only a slightly deleterious effect on mating. Furthermore, deletion of the three N-terminal residues caused no sterility, although truncation of a fourth residue had a marked effect. We conclude that a farnesylated hexapeptide (KVPYMC(Far)-OCH(3)) is the minimal M-factor that retains pheromone activity. At least 15 nonfunctional peptides were found to be secreted, suggesting that these mutant M-factor peptides are no longer recognized by the cognate receptor.","doi":"10.1534/genetics.112.140483","authors":"Seike T, Yamagishi Y, Iio H, Nakamura T, Shimoda C","authors_abbrev":"Seike T et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-05-01","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC02546","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39527200","title":"Proliferation Analyses of Conditional Knockdown Strains Using CRISPR Interference in Fission Yeast.","citation":"Methods Mol Biol 2025;2862:171-186","abstract":"CRISPR interference is a method to conditionally inhibit transcription of an arbitrary target gene. This is useful to study the functions of essential genes, which are required for cellular viability. Although many conditional gene perturbation techniques are available for Schizosaccharomyces pombe, CRISPRi facilitates construction of a large number of knockdown strains because of its systematic, simple procedure. Here, we describe a method to construct and characterize knockdown strains using dCas9-mediated CRISPRi in S. pombe, including a variation of CRISPRi induction technique in a 96-well format for high-throughput studies.","doi":"10.1007/978-1-0716-4168-2_12","authors":"Ishikawa K, Saitoh S","authors_abbrev":"Ishikawa K et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22363481","title":"S. pombe kinesins-8 promote both nucleation and catastrophe of microtubules.","citation":"PLoS One 2012;7(2):e30738","abstract":"The kinesins-8 were originally thought to be microtubule depolymerases, but are now emerging as more versatile catalysts of microtubule dynamics. We show here that S. pombe Klp5-436 and Klp6-440 are non-processive plus-end-directed motors whose in vitro velocities on S. pombe microtubules at 7 and 23 nm s(-1) are too slow to keep pace with the growing tips of dynamic interphase microtubules in living S. pombe. In vitro, Klp5 and 6 dimers exhibit a hitherto-undescribed combination of strong enhancement of microtubule nucleation with no effect on growth rate or catastrophe frequency. By contrast in vivo, both Klp5 and Klp6 promote microtubule catastrophe at cell ends whilst Klp6 also increases the number of interphase microtubule arrays (IMAs). Our data support a model in which Klp5/6 bind tightly to free tubulin heterodimers, strongly promoting the nucleation of new microtubules, and then continue to land as a tubulin-motor complex on the tips of growing microtubules, with the motors then dissociating after a few seconds residence on the lattice. In vivo, we predict that only at cell ends, when growing microtubule tips become lodged and their growth slows down, will Klp5/6 motor activity succeed in tracking growing microtubule tips. This mechanism would allow Klp5/6 to detect the arrival of microtubule tips at cells ends and to amplify the intrinsic tendency for microtubules to catastrophise in compression at cell ends. Our evidence identifies Klp5 and 6 as spatial regulators of microtubule dynamics that enhance both microtubule nucleation at the cell centre and microtubule catastrophe at the cell ends.","doi":"10.1371/journal.pone.0030738","authors":"Erent M, Drummond DR, Cross RA","authors_abbrev":"Erent M et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-02-25","publication_year":"2012","canto_session_key":"96db134a190f0043","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-08-25 09:58:51","canto_approved_date":"2022-08-25 09:58:51","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2022-08-25 09:58:40","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":2,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.15c","SPBC2F12.13"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2022-08-25"},{"uniquename":"PMID:26597962","title":"Site Specific Genetic Incorporation of Azidophenylalanine in Schizosaccharomyces pombe.","citation":"Sci Rep 2015 Nov 24;5:17196","abstract":"The diversity of protein functions is impacted in significant part by the chemical properties of the twenty amino acids, which are used as building blocks for nearly all proteins. The ability to incorporate unnatural amino acids (UAA) into proteins in a site specific manner can vastly expand the repertoire of protein functions and also allows detailed analysis of protein function. In recent years UAAs have been incorporated in a site-specific manner into proteins in a number of organisms. In nearly all cases, the amber codon is used as a sense codon, and an orthogonal tRNA/aminoacyl-tRNA synthetase (RS) pair is used to generate amber suppressing tRNAs charged with the UAA. In this work, we have developed tools to incorporate the cross-linking amino acid azido-phenylalanine (AzF) through the use of bacterial tRNA(Tyr) and a modified version of TyrRS, AzFRS, in Schizosaccharomyces pombe, which is an attractive model organism for the study of cell behavior and function. We have incorporated AzF into three different proteins. We show that the majority of AzF is modified to amino-phenyl alanine, but protein cross-linking was still observed. These studies set the stage for exploitation of this new technology for the analysis of S. pombe proteins.","doi":"10.1038/srep17196","authors":"Shao N, Singh NS, Slade SE, Jones AM, Balasubramanian MK","authors_abbrev":"Shao N et al.","pubmed_publication_date":"24 Nov 2015","pubmed_entrez_date":"2015-11-25","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-27 01:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11250892","title":"The role of Plo1 kinase in mitotic commitment and septation in Schizosaccharomyces pombe.","citation":"EMBO J 2001 Mar 15;20(6):1259-70","abstract":"Plo1-associated casein kinase activity peaked during mitosis before septation. Phosphatase treatment abolished this activity. Mitotic Plo1 activation had a requirement for prior activation of M-phase promoting factor (MPF), suggesting that Plo1 does not act as a mitotic trigger kinase to initiate MPF activation during mitotic commitment. A link between Plo1 and the septum initiating network (SIN) has been suggested by the inability of plo1 Delta cells to septate and the prolific septation following plo1(+) overexpression. Interphase activation of Spg1, the G protein that modulates SIN activity, induced septation but did not stimulate Plo1-associated kinase activity. Conversely, SIN inactivation did not affect the mitotic stimulation of Plo1-associated kinase activity. plo1.ts4 cells formed a misshapen actin ring, but rarely septated at 36 degrees C. Forced activation of Spg1 enabled plo1.ts4 mutant cells, but not cells with defects in the SIN component Sid2, to convert the actin ring to a septum. The ability of plo1(+) overexpression to induce septation was severely compromised by SIN inactivation. We propose that Plo1 acts before the SIN to control septation.","authors":"Tanaka K, Petersen J, MacIver F, Mulvihill DP, Glover DM, Hagan IM","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"15 Mar 2001","pubmed_entrez_date":"2001-03-17","publication_year":"2001","canto_session_key":"b687ff7ab68d1820","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-07-26 15:16:34","canto_approved_date":"2021-11-24 17:07:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-24 14:15:00","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1565.06c","SPAC23C11.16","SPAC6F6.08c","SPBC21.06c","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-07-26"},{"uniquename":"PMID:19209822","title":"Tropomyosin function in yeast.","citation":"Adv Exp Med Biol 2008;644:168-86","abstract":"Tropomyosins were discovered as regulators of actomyosin contractility in muscle cells, making yeasts and other fungi seem unlikely to harbor such proteins. Fungal cells are encased in a rigid cell wall and do not engage in the same sorts of contractile shape changes of animal cells. However, discovery of actin and myosin in yeast raised the possibility for a role for tropomyosin in regulating their interaction. Through a biochemical search, fungal tropomyosins were identified with strong similarities to their animal counterparts in terms ofprotein structure and physical properties. Two particular fungi, the buddingyeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe, have provided powerful genetic systems for studying tropomyosins in nonmetazoans. In these yeasts, tropomyosins associate with subsets ofactin filamentous structures. Mutational studies oftropomyosin genes and biochemical assays of purified proteins point to roles for these proteins as factors that stabilize actin filaments, promote actin-based structures of particular architecture and help maintain distinct biochemical identities among different filament populations. Tropomyosin-enriched filaments are the cytoskeletal structures that promote the major cell shape changes of these organisms: polarized growth and cell division.","authors":"Pruyne D","authors_abbrev":"Pruyne D","pubmed_publication_date":"2008","pubmed_entrez_date":"2009-02-13","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12867080","title":"Yeast RNA helicases of the DEAD-box family involved in translation initiation.","citation":"Biol Cell 2003;95(3-4):157-67","abstract":"RNA helicases of the DEAD-box and related families have been found to be required for all processes involving RNA molecules. Biochemical and genetic analyses have shown that at least two RNA helicases are required for translation initiation in yeast. Although it is generally believed that these enzymes are necessary to unwind secondary structures in the 5' untranslated region of mRNAs, their exact role has not been convincingly shown. We discuss here our present knowledge of the function of eIF4A and Ded1p, two DEAD-box proteins required for translation in eukaryotic cells.","authors":"Linder P","authors_abbrev":"Linder P","pubmed_publication_date":"2003","pubmed_entrez_date":"2003-07-18","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10452954","title":"Ras-mediated signaling pathway regulates the expression of a low-molecular-weight heat-shock protein in fission yeast.","citation":"Gene 1999 Aug 20;236(2):347-52","abstract":"In fission yeast, Schizosaccharomyces pombe, deficiency of ras1 gene causes an abnormal cell shape and abolishes mating ability. However, target genes of this signaling pathway are largely unknown because of the lack of an appropriate analysis system. To overcome this problem, we have started a novel project to categorize entire genes based on their expression levels under different growth conditions. Using this strategy, we screened genes whose expression levels were affected in the presence or absence of the ras1 gene product. For this purpose, we utilized high-density arrays of clones covering the entire genome of the fission yeast, and probed with labelled cDNA derived from various strains and growth conditions. Here, we demonstrate the detection of a low-molecular-weight heat-shock protein gene, hsp16, whose expression is very likely to be regulated by a ras-mediated signaling pathway, but not by the heat-shock response.","authors":"Danjoh I, Fujiyama A","authors_abbrev":"Danjoh I et al.","pubmed_publication_date":"20 Aug 1999","pubmed_entrez_date":"1999-08-24","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29931271","title":"Mitotic defects in fission yeast lipid metabolism 'cut' mutants are suppressed by ammonium chloride.","citation":"FEMS Yeast Res 2018 Sep 01;18(6)","abstract":"Fission yeast 'cut' mutants show defects in temporal coordination of nuclear division with cytokinesis, resulting in aberrant mitosis and lethality. Among other causes, the 'cut' phenotype can be triggered by genetic or chemical perturbation of lipid metabolism, supposedly resulting in shortage of membrane phospholipids and insufficient nuclear envelope expansion during anaphase. Interestingly, penetrance of the 'cut' phenotype in mutants of the transcription factor cbf11 and acetyl-coenzyme A carboxylase cut6, both related to lipid metabolism, is highly dependent on growth media, although the specific nutrient(s) affecting 'cut' occurrence is not known. In this study, we set out to identify the growth media component(s) responsible for 'cut' phenotype suppression in Δcbf11 and cut6-621 cells. We show that mitotic defects occur rapidly in Δcbf11 cells upon shift from the minimal EMM medium ('cut' suppressing) to the complex YES medium ('cut' promoting). By growing cells in YES medium supplemented with individual EMM components, we identified ammonium chloride, an efficiently utilized nitrogen source, as a specific and potent suppressor of the 'cut' phenotype in both Δcbf11 and cut6-621. Furthermore, we found that ammonium chloride boosts lipid droplet formation in wild-type cells. Our findings suggest a possible involvement of nutrient-responsive signaling in 'cut' suppression.","doi":"10.1093/femsyr/foy064","authors":"Zach R, Tvaružková J, Schätz M, Tupa O, Grallert B, Prevorovský M","authors_abbrev":"Zach R et al.","pubmed_publication_date":"01 Sep 2018","pubmed_entrez_date":"2018-06-23","publication_year":"2018","canto_session_key":"4b66c2494de872ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Martin Převorovský","canto_first_approved_date":"2018-06-27 12:51:34","canto_approved_date":"2018-06-27 12:51:34","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-06-25 11:24:28","canto_added_date":"2018-06-24 00:15:04","annotation_curators":[{"name":"Martin Převorovský","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.08","SPAC56E4.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-27"},{"uniquename":"PMID:8765156","title":"Molecular biology of DNA repair in the fission yeast Schizosaccharomyces pombe.","citation":"Mutat Res 1996 Aug 08;363(3):147-61","abstract":"","authors":"Lehmann AR","authors_abbrev":"Lehmann AR","pubmed_publication_date":"08 Aug 1996","pubmed_entrez_date":"1996-08-08","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18495844","title":"Interphase microtubule bundles use global cell shape to guide spindle alignment in fission yeast.","citation":"J Cell Sci 2008 Jun 15;121(Pt 12):1973-80","abstract":"Correct spindle alignment requires a cell to detect and interpret its global geometry and to communicate this information to the mitotic spindle. In the fission yeast, Schizosaccharomyces pombe, the mitotic spindle is aligned with the longitudinal axis of the rod-shaped cell. Here, using wild-type and cell-shape mutants we investigate the mechanism of initial spindle alignment and show that attachment of interphase microtubules to the spindle pole bodies (SPB), the yeast equivalent of the centrosome, is required to align duplicated SPBs, and thus the mitotic spindle, with the long axis of the cell. In the absence of interphase microtubules or attachment between the microtubules and the SPB, newly formed spindles are randomly oriented. We show that the axis of the mitotic spindle correlates with the axis along which the SPB, as a consequence of interphase microtubule dynamics, oscillates just before mitosis. We propose that cell geometry guides cytoplasmic microtubule alignment, which in turn, determines initial spindle alignment, and demonstrate that a failure of the spindle pre-alignment mechanism results in unequal chromosome segregation when spindle length is reduced.","doi":"10.1242/jcs.011825","authors":"Daga RR, Nurse P","authors_abbrev":"Daga RR et al.","pubmed_publication_date":"15 Jun 2008","pubmed_entrez_date":"2008-05-23","publication_year":"2008","canto_session_key":"a19f8cb91e1b57a2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2020-06-16 16:13:06","canto_approved_date":"2026-06-10 05:45:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-24 14:38:28","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":6,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC926.03","SPAC3C7.12","SPAC24B11.11c","SPAC821.12","SPCC417.07c","SPAC2F7.03c","SPBC649.05","SPBC800.05c","SPBC1706.01","SPCC1223.06"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2020-06-16"},{"uniquename":"PMID:8202597","title":"Randomly distributed DNA double-strand breaks as measured by pulsed field gel electrophoresis: a series of explanatory calculations.","citation":"Radiat Environ Biophys 1994;33(1):9-21","abstract":"The aim of this article is to characterize expressions of relevance to the interpretation of pulsed field gel electrophoresis (PFGE) experiments where randomly distributed double-strand breaks (DSBs) are detected as smears of DNA fragments. Specifically, equations for conversion of percentages of fragments in defined size ranges to DSBs were derived. Several models have been used, one of which is based on theoretically fragmented DNA from the fission yeast Schizosaccharomyces pombe, which has three PFGE separable chromosomes.","authors":"Cedervall B, Källman P","authors_abbrev":"Cedervall B et al.","pubmed_publication_date":"1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32318758","title":"Centromere targeting of Mis18 requires the interaction with DNA and H2A-H2B in fission yeast.","citation":"Cell Mol Life Sci 2021 Jan;78(1):373-384","abstract":"Faithful chromosome segregation during mitosis requires the correct assembly of kinetochore on the centromere. CENP-A is a variant of histone H3, which specializes the centromere region on chromatin and mediates the kinetochore assembly. The Mis18 complex plays a critical role in initiating the centromere loading of the newly-synthesized CENP-A. However, it remains unclear how Mis18 complex (spMis18, spMis16 and spMis19) is located to the centromere to license the recruitment of Cnp1 CENP-A  in Schizosaccharomyces pombe. We found that spMis18 directly binds to nucleosomal DNA through its extreme C-terminus and interacts with H2A-H2B dimer via the acidic region on the surface of its Yippee-like domain. Live-cell imaging confirmed that mutation of the acidic region and deletion of the extreme C-terminus significantly impairs the localization of spMis18 and Cnp1 to the centromere and delays chromosome segregation during mitosis. Our findings illustrate that the interaction of spMis18 with histone H2A-H2B and DNA plays important roles in the recruitment of spMis18 and Cnp1 to the centromere in fission yeast.","doi":"10.1007/s00018-020-03502-1","authors":"Zhang M, Zheng F, Xiong Y, Shao C, Wang C, Wu M, Niu X, Dong F, Zhang X, Fu C, Zang J","authors_abbrev":"Zhang M et al.","pubmed_publication_date":"Jan 2021","pubmed_entrez_date":"2020-04-23","publication_year":"2021","canto_session_key":"8dc06c38ba3b6500","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-04-24 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC970.12","SPBC1105.17"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:20705466","title":"Fimbrin and tropomyosin competition regulates endocytosis and cytokinesis kinetics in fission yeast.","citation":"Curr Biol 2010 Aug 24;20(16):1415-22","abstract":"Tropomyosin is an important actin filament-stabilizing protein that controls the access of other essential proteins to filaments, including myosin motors, Arp2/3 complex, formin, and cofilin. It is therefore critical to establish mechanisms for regulating the actin filament binding of tropomyosin. We examined how the actin filament crosslinking protein fimbrin Fim1p and tropomyosin Cdc8p affect each other's ability to bind filaments, localize to particular cellular structures, and regulate filament severing by cofilin Adf1p in fission yeast Schizosaccharomyces pombe.\nWe discovered a novel mechanism for regulating actin filament dynamics in fission yeast. Fim1p inhibits Cdc8p binding to actin filaments in vitro, which permits Adf1p-mediated severing in the presence of Cdc8p. In cells, the balance between Fim1p and Cdc8p is important for both endocytic actin patch kinetics and contractile ring assembly during cytokinesis. High Fim1p concentrations prevent Cdc8p from associating with actin patches, allowing rapid patch turnover and motility. In the absence of Fim1p, ectopic localization of Cdc8p to actin patches increases patch lifetime while decreasing patch motility. Fim1p and Cdc8p also play antagonistic roles during cytokinesis, in which the deletion of Fim1p rescues the contractile ring assembly defects caused by mutation of Cdc8p.\nFimbrin Fim1p dissociates tropomyosin Cdc8p from actin filaments, permitting cofilin Adf1p-mediated severing. Therefore, we propose that in addition to actin filament crosslinking, Fim1p has a novel role as a positive actin-binding \"selector\" protein that promotes the access of other proteins to actin filaments by inhibiting Cdc8p.","doi":"10.1016/j.cub.2010.06.020","authors":"Skau CT, Kovar DR","authors_abbrev":"Skau CT et al.","pubmed_publication_date":"24 Aug 2010","pubmed_entrez_date":"2010-08-14","publication_year":"2010","canto_session_key":"b5617d852b7dbffb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-06-30 14:29:55","canto_approved_date":"2026-04-21 18:16:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-30 14:29:48","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":30,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.06c","SPAC27F1.02c","SPBC32H8.12c","SPBC1778.06c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-06-30"},{"uniquename":"GO_REF:0000116","title":"Automatic Gene Ontology annotation based on Rhea mapping.","abstract":"Rhea (https://www.rhea-db.org/, PMID:30272209) is an expert-curated knowledgebase of chemical and transport reactions of biological interest - and the standard for enzyme and transporter annotation in UniProtKB (PMID:31688925). Rhea uses the chemical dictionary ChEBI (Chemical Entities of Biological Interest) to describe reaction participants and their chemical transformations in a computationally tractable manner. GO terms corresponding to Rhea reactions are assigned a Rhea database cross-reference. The corresponding GO term is automatically applied to all UniProt entries annotated with a Rhea reaction. The mapping file is available at: http://current.geneontology.org/ontology/external2go/rhea2go.","authors":"GO Central curators, GOA curators, Rhea curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC5H10.04","SPAC27E2.05","SPAC29A4.04c","SPAC23D3.04c","SPAC977.09c","SPCC1494.04c","SPAC57A10.12c","SPCC895.03c","SPBC887.01","SPBC26H8.01","SPAC21E11.05c","SPCC285.04","SPCC16C4.12","SPAC140.01","SPAC12B10.04","SPBC1683.11c","SPBC776.03","SPAC607.04","SPAC22A12.11","SPCC364.07","SPBC16H5.05c","SPCC63.04","SPAC227.14","SPCC162.05","SPBC13G1.02","SPCC1020.08","SPCC1183.02","SPCC553.04","SPAC22F8.05","SPAC926.09c","SPCC1450.09c","SPBC1347.13c","SPAC869.04","SPBC418.01c","SPBC15D4.06","SPAC22G7.06c","SPAC3A11.07","SPAC5H10.10","SPBC17G9.05","SPCC4G3.16","SPBC1348.10c","SPAC1527.01","SPCC18.15","SPBC17A3.09c","SPBC646.07c","SPACUNK4.16c","SPBC146.12","SPAC343.10","SPBC36.06c","SPBC947.15c","SPCC794.12c","SPCC162.11c","SPBC16A3.10","SPCC1281.07c","SPCC663.10","SPAC56F8.10","SPAC15E1.08","SPBC1A4.09","SPAC4D7.06c","SPAC1786.02","SPAC4G9.15","SPAC23C4.16c","SPBC23G7.10c","SPBC460.02c","SPAC977.16c","SPBC16D10.03","SPAC1834.05"],"gene_count":67,"ltp_gene_count":0},{"uniquename":"PMID:22496451","title":"Genetic screening for regulators of Prz1, a transcriptional factor acting downstream of calcineurin in fission yeast.","citation":"J Biol Chem 2012 Jun 01;287(23):19294-303","abstract":"Calcineurin phosphatase plays crucial roles in a wide variety of cell types and organisms. Dephosphorylation of the nuclear factor of activated T-cell (NFAT) family of transcriptional factors by calcineurin is essential for activating immune-responsive genes in mammals. NFAT activity is also regulated by diverse signaling pathways, which affect NFAT kinases and nuclear partner proteins. In fission yeast, calcineurin dephosphorylates and activates Prz1, a C2H2-type zinc finger transcriptional factor. Calcineurin-Prz1 signaling regulates the expression of the Pmc1 Ca(2+) pump. Prz1-overexpressing cells showed extremely slow growth and high transcriptional activity of Prz1 in the absence of stimulation. Here, we isolated seven genes as dosage-dependent suppressors of this slow growth phenotype. These seven genes encode Rad24, Rad25, Pka1, Msn5 (SPAC328.01c), Pac1, Ape2, and Tfs1. All of them decreased the high transcriptional activity caused by Prz1 overexpression. Overexpression of Pka1, Rad24, and Rad25 also repressed the Ca(2+)-induced transcriptional activity in cells with Prz1 expressed at wild-type levels. Knock-out of rad24 or rad25 significantly enhanced the transcriptional activity of Prz1, whereas knock-out or mutation of other genes did not enhance the activity. The 14-3-3 proteins, Rad24 and Rad25, bound Prz1 and the Rad24-binding site located at residues 421-426 of Prz1. In msn5 deletion mutants, GFP-Prz1 localized at nucleus in the absence of Ca(2+) stimulation, suggesting that Msn5 functions as an exportin for Prz1. In summary, our data suggest that Rad24 and Rad25 negatively regulate Prz1 and that Pka1, Msn5, Pac1, Tfs1, and Ape2 also regulate Prz1.","doi":"10.1074/jbc.M111.310615","authors":"Koike A, Kato T, Sugiura R, Ma Y, Tabata Y, Ohmoto K, Sio SO, Kuno T","authors_abbrev":"Koike A et al.","pubmed_publication_date":"01 Jun 2012","pubmed_entrez_date":"2012-04-13","publication_year":"2012","canto_session_key":"c1d9cf8c5062801d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-10 18:03:15","canto_approved_date":"2023-10-17 19:16:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-16 22:38:32","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":54,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC328.01c","SPBC119.11c","SPAC17A2.13c","SPBP4H10.04","SPBC1921.05","SPAC8E11.02c","SPAC4G8.13c","SPAC20H4.03c","SPAC6F12.02","SPBC106.10"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2017-01-10"},{"uniquename":"PMID:40520116","title":"Histone deacetylation as a landmark for Sgo2 relocation from centromeres to subtelomeres during interphase.","citation":"iScience 2025 Jun 20;28(6):112717","abstract":"Shugoshin family proteins localize to centromeres and play pivotal roles in chromosome segregation during mitosis and meiosis. In fission yeast, the Shugoshin paralog Sgo2 relocates from centromeres to subtelomeres during interphase, where it contributes to gene repression by establishing a subtelomere-specific condensed chromatin structure known as the knob. However, the mechanisms underlying subtelomere-specific Sgo2 localization and knob formation during interphase remain poorly understood. Here, we identified Nts1, a component of the histone deacetylase complex, as a key regulator of Sgo2 localization through a genetic screen. Deletion of both  nts1   +  and  set2   +  (which encodes a histone H3-K36 methyltransferase) resulted in an almost complete loss of Sgo2 localization and knob formation at subtelomeres, indicating that Nts1 and Set2 function redundantly to target Sgo2 to subtelomeres. Notably, Nts1 localizes to subtelomeres during interphase and promotes histone H4 deacetylation, suggesting that histone deacetylation serves as a landmark for subtelomere-specific Sgo2 localization and knob formation.","doi":"10.1016/j.isci.2025.112717","authors":"Osaki M, Otsubo Y, Nurani A, Asano N, Ono K, Kanoh J","authors_abbrev":"Osaki M et al.","pubmed_publication_date":"20 Jun 2025","pubmed_entrez_date":"2025-06-16","publication_year":"2025","canto_session_key":"d7647cb461f59424","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junko Kanoh","canto_first_approved_date":"2026-04-07 07:46:19","canto_approved_date":"2026-04-07 07:46:19","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-03-16 09:48:20","canto_added_date":"2025-06-16 23:25:04","annotation_curators":[{"name":"Junko Kanoh","community_curator":true,"annotation_count":60,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":6,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC5D6.02c","SPBC1685.08","SPBCPT2R1.08c","SPAC869.07c","SPAC16E8.12c","SPAC1F8.01","SPBPB2B2.13","SPAC29B12.02c","SPBC1348.14c","SPAC212.11","SPBC21C3.02c","SPAC15A10.15","SPBPB2B2.19c","SPBPB21E7.07","SPAC2F7.07c","SPBC1709.11c","SPCC24B10.19c","SPAC16C9.05","SPBP4G3.03","SPCC1322.12c","SPAC186.01"],"gene_count":21,"ltp_gene_count":11,"approved_date":"2026-04-07"},{"uniquename":"EMBL:SPC06887","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16473766","title":"Biosynthetic regulation of phytochelatins, heavy metal-binding peptides.","citation":"J Biosci Bioeng 2005 Dec;100(6):593-9","abstract":"Phytochelatins (PCs) are heavy metal-binding peptides that play important roles in the detoxification of toxic heavy metals and the regulation of intracellular concentrations of essential metals in eukaryotes, including higher plants, fungi, and microalgae. Recently, PC synthase genes in higher plants and fission yeast have been identified and characterized, enabling molecular biological studies to unravel the mechanisms underlying PC synthesis. Moreover, recent routine database searches have unexpectedly identified genes that are similar to plant PC synthase genes in the genomes of worms and some prokaryotes. In this review, we introduce these recent advances in our understanding of the molecular mechanisms for PC biosynthesis and functions in order to supply basic information about the unique and attractive peptides applicable to various fields.","authors":"Hirata K, Tsuji N, Miyamoto K","authors_abbrev":"Hirata K et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2006-02-14","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19915592","title":"An acetylated form of histone H2A.Z regulates chromosome architecture in Schizosaccharomyces pombe.","citation":"Nat Struct Mol Biol 2009 Dec;16(12):1286-93","abstract":"Histone variant H2A.Z has a conserved role in genome stability, although it remains unclear how this is mediated. Here we demonstrate that the fission yeast Swr1 ATPase inserts H2A.Z (Pht1) into chromatin and Kat5 acetyltransferase (Mst1) acetylates it. Deletion or an unacetylatable mutation of Pht1 leads to genome instability, primarily caused by chromosome entanglement and breakage at anaphase. This leads to the loss of telomere-proximal markers, though telomere protection and repeat length are unaffected by the absence of Pht1. Strikingly, the chromosome entanglement in pht1Delta anaphase cells can be rescued by forcing chromosome condensation before anaphase onset. We show that the condensin complex, required for the maintenance of anaphase chromosome condensation, prematurely dissociates from chromatin in the absence of Pht1. This and other findings suggest an important role for H2A.Z in the architecture of anaphase chromosomes.","doi":"10.1038/nsmb.1688","authors":"Kim HS, Vanoosthuyse V, Fillingham J, Roguev A, Watt S, Kislinger T, Treyer A, Carpenter LR, Bennett CS, Emili A, Greenblatt JF, Hardwick KG, Krogan NJ, Bähler J, Keogh MC","authors_abbrev":"Kim HS et al.","pubmed_publication_date":"Dec 2009","pubmed_entrez_date":"2009-11-17","publication_year":"2009","canto_session_key":"f90ddb2fa9bdc30c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-11-15 17:35:27","canto_approved_date":"2026-05-01 17:07:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-15 17:34:47","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":30,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC83.08","SPAC637.12c","SPBC32H8.12c","SPBC29A3.05","SPAPB8E5.09","SPCC338.17c","SPCC576.13","SPAC11E3.01c","SPAC9G1.13c","SPBP35G2.13c","SPAC343.11c","SPAC1F5.11c","SPAC4H3.02c","SPBP23A10.08","SPBC11B10.10c","SPAC17G8.07","SPCC550.12"],"gene_count":17,"ltp_gene_count":17,"approved_date":"2023-11-15"},{"uniquename":"PMID:18637840","title":"Loss of Zhf and the tightly regulated zinc-uptake system SpZrt1 in Schizosaccharomyces pombe reveals the delicacy of cellular zinc balance.","citation":"FEMS Yeast Res 2008 Sep;8(6):883-96","abstract":"Abstract Zinc is an essential micronutrient, and yet it can be toxic when present in excess. Zinc acquisition and distribution are dependent on tightly controlled transport of Zn(2+) ions. Schizosaccharomyces pombe represents a second eukaryotic model to study cellular metal homeostasis. In several ways its micronutrient metabolism is fundamentally different from Saccharomyces cerevisiae. We identified the first Zn(2+)-uptake system in S. pombe and named it SpZrt1. Knock-out strains for all three ZIP (Zrt, Irt-like protein) transporters in fission yeast were constructed. Only zrt1Delta cells were unable to grow at low Zn(2+) and showed reduced (65)Zn(2+) uptake. Elemental profiles revealed a strong decrease in zinc accumulation. Cd(2+) ions inhibited uptake but Fe(2+) or Mn(2+) did not. Both mRNA abundance and protein amount are tightly regulated. Zrt1 activity is rapidly shut down upon transfer of zinc-deficient cells to zinc-replete conditions. In cells lacking Zhf, a transporter mediating endoplasmic reticulum storage of zinc, this response is about 100-fold more sensitive. Thus, removal of excess of zinc from the cytosol is largely Zhf dependent. Moreover, cells deficient for both transporters are no longer able to adjust to changing external Zn(2+) concentrations. Optimal growth is restricted to a narrow range of Zn(2+) concentrations, illustrating the fine balance between micronutrient deficiency and toxicity.","doi":"10.1111/j.1567-1364.2008.00414.x","authors":"Boch A, Trampczynska A, Simm C, Taudte N, Krämer U, Clemens S","authors_abbrev":"Boch A et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-07-22","publication_year":"2008","canto_session_key":"b719dc2cd003f460","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-10-22 18:56:16","canto_approved_date":"2018-02-17 12:15:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-23 10:28:28","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":61,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.03","SPBC16D10.06","SPAC23C11.14","SPBC36.04","SPBC2G5.06c","SPCC126.09"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2017-10-22"},{"uniquename":"PMID:11878307","title":"Non-conventional yeasts.","citation":"Appl Microbiol Biotechnol 2002 Feb;58(2):147-56","abstract":"In the beginning there was yeast, and it raised bread, brewed beer, and made wine. After many not days but centuries and even millenia later, it was named Saccharomyces cerevisiae. After more years and centuries there was another yeast, and it was named Schizosaccharomyces pombe; now there were two stars in the yeast heaven. In only a few more years there were other yeasts, and then more, and more, and more. The era of the non-conventional yeasts had begun.","authors":"Spencer JF, Ragout de Spencer AL, Laluce C","authors_abbrev":"Spencer JF et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-03-07","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20345377","title":"Stress signalling to fungal stress-activated protein kinase pathways.","citation":"FEMS Microbiol Lett 2010 May;306(1):1-8","abstract":"The ability of microorganisms to survive and thrive within hostile environments depends on rapid and robust stress responses. Stress-activated protein kinase (SAPK) pathways are important stress-signalling modules found in all eukaryotes, including eukaryotic microorganisms such as fungi. These pathways consist of a SAPK that is activated by phosphorylation through a kinase cascade, and once activated, the SAPK phosphorylates a range of cytoplasmic and nuclear target substrates, which determine the appropriate response. However, despite their conservation in fungi, mechanisms that have evolved to relay stress signals to the SAPK module in different fungi have diverged significantly. Here, we present an overview of the diverse strategies used in the model yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, and the pathogenic fungus Candida albicans, to sense and transduce stress signals to their respective SAPKs.","doi":"10.1111/j.1574-6968.2010.01937.x","authors":"Smith DA, Morgan BA, Quinn J","authors_abbrev":"Smith DA et al.","pubmed_publication_date":"May 2010","pubmed_entrez_date":"2010-03-30","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3034608","title":"The product of the mei3+ gene, expressed under control of the mating-type locus, induces meiosis and sporulation in fission yeast.","citation":"EMBO J 1987 Mar;6(3):729-36","abstract":"In fission yeast the ability to undergo meiosis and sporulation is conferred by the matP+ and matM+ genes of the mating-type locus. Inactivation of ran1+, a negative regulator of meiosis, is thought to be an essential step in meiotic initiation. We have isolated a further meiotic control gene mei3+, and have shown the following: a null allele of mei3 totally inhibits meiosis; the mei3+ RNA transcript and its translational product are expressed only in matP+/matM+ diploids entering meiosis; forced expression of mei3+ in vegetative cells provokes haploid meiosis and sporulation. We suggest that the product of mei3+ gene, a protein of 21 kd, initiates meiosis by inactivating ran1+.","authors":"McLeod M, Stein M, Beach D","authors_abbrev":"McLeod M et al.","pubmed_publication_date":"Mar 1987","pubmed_entrez_date":"1987-03-01","publication_year":"1987","canto_session_key":"93c0ecbe5a58d0fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 10:00:18","canto_approved_date":"2024-04-04 11:50:15","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-02-26 09:48:03","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPBC119.04","SPBC19C2.05","SPMTR.02"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-06-10"},{"uniquename":"PMID:24532840","title":"Predicting the dynamics of protein abundance.","citation":"Mol Cell Proteomics 2014 May;13(5):1330-40","abstract":"Protein synthesis is finely regulated across all organisms, from bacteria to humans, and its integrity underpins many important processes. Emerging evidence suggests that the dynamic range of protein abundance is greater than that observed at the transcript level. Technological breakthroughs now mean that sequencing-based measurement of mRNA levels is routine, but protocols for measuring protein abundance remain both complex and expensive. This paper introduces a Bayesian network that integrates transcriptomic and proteomic data to predict protein abundance and to model the effects of its determinants. We aim to use this model to follow a molecular response over time, from condition-specific data, in order to understand adaptation during processes such as the cell cycle. With microarray data now available for many conditions, the general utility of a protein abundance predictor is broad. Whereas most quantitative proteomics studies have focused on higher organisms, we developed a predictive model of protein abundance for both Saccharomyces cerevisiae and Schizosaccharomyces pombe to explore the latitude at the protein level. Our predictor primarily relies on mRNA level, mRNA-protein interaction, mRNA folding energy and half-life, and tRNA adaptation. The combination of key features, allowing for the low certainty and uneven coverage of experimental observations, gives comparatively minor but robust prediction accuracy. The model substantially improved the analysis of protein regulation during the cell cycle: predicted protein abundance identified twice as many cell-cycle-associated proteins as experimental mRNA levels. Predicted protein abundance was more dynamic than observed mRNA expression, agreeing with experimental protein abundance from a human cell line. We illustrate how the same model can be used to predict the folding energy of mRNA when protein abundance is available, lending credence to the emerging view that mRNA folding affects translation efficiency. The software and data used in this research are available at http://bioinf.scmb.uq.edu.au/proteinabundance/.","doi":"10.1074/mcp.M113.033076","authors":"Mehdi AM, Patrick R, Bailey TL, Bodén M","authors_abbrev":"Mehdi AM et al.","pubmed_publication_date":"May 2014","pubmed_entrez_date":"2014-02-18","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38425362","title":"In vitro construction of the COQ metabolon unveils the molecular determinants of coenzyme Q biosynthesis.","citation":"Nat Catal 2024 Jan 03;7(2):148-160","abstract":"Metabolons are protein assemblies that perform a series of reactions in a metabolic pathway. However, the general importance and aptitude of metabolons for enzyme catalysis remain poorly understood. In animals, biosynthesis of coenzyme Q is currently attributed to ten different proteins, with COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9 forming the iconic COQ metabolon. Yet several reaction steps conducted by the metabolon remain enigmatic. To elucidate the prerequisites for animal coenzyme Q biosynthesis, we sought to construct the entire metabolon in vitro. Here we show that this approach, rooted in ancestral sequence reconstruction, reveals the enzymes responsible for the uncharacterized steps and captures the biosynthetic pathway in vitro. We demonstrate that COQ8, a kinase, increases and streamlines coenzyme Q production. Our findings provide crucial insight into how biocatalytic efficiency is regulated and enhanced by these biosynthetic engines in the context of the cell.","doi":"10.1038/s41929-023-01087-z","authors":"Nicoll CR, Alvigini L, Gottinger A, Cecchini D, Mannucci B, Corana F, Mascotti ML, Mattevi A","authors_abbrev":"Nicoll CR et al.","pubmed_publication_date":"03 Jan 2024","pubmed_entrez_date":"2024-03-01","publication_year":"2024","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2D10.18","SPAC19G12.11"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:9150257","title":"A novel fission yeast gene, kms1+, is required for the formation of meiotic prophase-specific nuclear architecture.","citation":"Mol Gen Genet 1997 Apr 16;254(3):238-49","abstract":"In the meiotic prophase nucleus of the fission yeast Schizosaccharomyces pombe, chromosomes are arranged in an oriented manner: telomeres cluster in close proximity to the spindle pole body (SPB), while centromeres form another cluster at some distance from the SPB. We have isolated a mutant, kms1, in which the structure of the meiotic prophase nucleus appears to be distorted. Using specific probes to localize the SPB and telomeres, multiple signals were observed in the mutant nuclei, in contrast to the case in wild-type. Genetic analysis showed that in the mutant, meiotic recombination frequency was reduced to about one-quarter of the wild-type level and meiotic segregation was impaired. This phenotype strongly suggests that the telomere-led rearrangement of chromosomal distribution that normally occurs in the fission yeast meiotic nucleus is an important prerequisite for the efficient pairing of homologous chromosomes. The kms1 mutant was also impaired in karyogamy, suggesting that the kms1+ gene is involved in SPB function. However, the kms1+ gene is dispensable for mitotic growth. The predicted amino acid sequence of the gene product shows no significant similarity to known proteins.","authors":"Shimanuki M, Miki F, Ding DQ, Chikashige Y, Hiraoka Y, Horio T, Niwa O","authors_abbrev":"Shimanuki M et al.","pubmed_publication_date":"16 Apr 1997","pubmed_entrez_date":"1997-04-16","publication_year":"1997","canto_session_key":"3b7eef1018efec35","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-09-25 13:43:26","canto_approved_date":"2024-03-28 15:53:33","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-09-25 13:42:42","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A11.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-25"},{"uniquename":"PMID:29422664","title":"Pof8 is a La-related protein and a constitutive component of telomerase in fission yeast.","citation":"Nat Commun 2018 Feb 08;9(1):587","abstract":"Telomerase reverse transcriptase (TERT) and the non-coding telomerase RNA subunit (TR) constitute the core of telomerase. Here we now report that the putative F-box protein Pof8 is also a constitutive component of active telomerase in fission yeast. Pof8 functions in a hierarchical assembly pathway by promoting the binding of the Lsm2-8 complex to telomerase RNA, which in turn promotes binding of the catalytic subunit. Loss of Pof8 reduces TER1 stability, causes a severe assembly defect, and results in critically short telomeres. Structure profile searches identified similarities between Pof8 and telomerase subunits from ciliated protozoa, making Pof8 next to TERT the most widely conserved telomerase subunits identified to date.","doi":"10.1038/s41467-017-02284-8","authors":"Páez-Moscoso DJ, Pan L, Sigauke RF, Schroeder MR, Tang W, Baumann P","authors_abbrev":"Páez-Moscoso DJ et al.","pubmed_publication_date":"08 Feb 2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_session_key":"92e920d99870dd0a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.214","SPBC30D10.06","SPAC26A3.08","SPBC20F10.09","SPBC11G11.06c","SPAC17G6.17"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:16899242","title":"Analysis of Mcm2-7 chromatin binding during anaphase and in the transition to quiescence in fission yeast.","citation":"Exp Cell Res 2006 Oct 15;312(17):3360-9","abstract":"Mcm2-7 proteins are generally considered to function as a heterohexameric complex, providing helicase activity for the elongation step of DNA replication. These proteins are loaded onto replication origins in M-G1 phase in a process termed licensing or pre-replicative complex formation. It is likely that Mcm2-7 proteins are loaded onto chromatin simultaneously as a pre-formed hexamer although some studies suggest that subcomplexes are recruited sequentially. To analyze this process in fission yeast, we have compared the levels and chromatin binding of Mcm2-7 proteins during the fission yeast cell cycle. Mcm subunits are present at approximately 1 x 10(4) molecules/cell and are bound with approximately equal stoichiometry on chromatin in G1/S phase cells. Using a single cell assay, we have correlated the timing of chromatin association of individual Mcm subunits with progression through mitosis. This showed that Mcm2, 4 and 7 associate with chromatin at about the same stage of anaphase, suggesting that licensing involves the simultaneous binding of these subunits. We also examined Mcm2-7 chromatin association when cells enter a G0-like quiescent state. Chromatin binding is lost in this transition in a process that does not require DNA replication or the selective degradation of specific subunits.","authors":"Namdar M, Kearsey SE","authors_abbrev":"Namdar M et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-08-11","publication_year":"2006","canto_session_key":"c87701f4494ce567","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-11-06 14:50:06","canto_approved_date":"2023-03-07 08:28:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-06 14:49:46","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPCC16A11.17","SPBC211.04c","SPBC4.04c","SPCC1682.02c","SPBC428.18","SPBC25D12.03c","SPAC1B2.05"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2014-11-06"},{"uniquename":"PMID:7859562","title":"Comparison of the two major ARS elements of the ura4 replication origin region with other ARS elements in the fission yeast, Schizosaccharomyces pombe.","citation":"Chromosoma 1994 Oct;103(6):414-22","abstract":"We have previously reported that the replication origin region located near the ura4 gene on chromosome III of the fission yeast, Schizosaccharomyces pombe, contains three closely spaced origins, each associated with an autonomously replicating sequence (ARS) element. Here we report the nucleotide sequences of two of these ARS elements, ars3002 and ars3003. The two ARS elements are located on either side of a transcribed 1.5 kb open reading frame. Like 11 other S. pombe ARS elements whose sequences have previously been determined in other laboratories, the 2 new ARS elements are unusually A+T-rich. All 13 ARS elements contain easily unwound stretches of DNA. Each of the ARS elements contains numerous copies, at a higher than expected frequency, of short stretches of A+T-rich DNA in which most of the Ts are on one strand and most of the As are on the complementary strand. We discuss the potential significance for ARS function of these multiple asymmetric A+T-rich sequences.","authors":"Zhu J, Carlson DL, Dubey DD, Sharma K, Huberman JA","authors_abbrev":"Zhu J et al.","pubmed_publication_date":"Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11106417","title":"Characterization of active-site mutants of Schizosaccharomyces pombe phosphoglycerate mutase. Elucidation of the roles of amino acids involved in substrate binding and catalysis.","citation":"Eur J Biochem 2000 Dec;267(24):7065-74","abstract":"The roles of a number of amino acids present at the active site of the monomeric phosphoglycerate mutase from the fission yeast Schizosaccharomyces pombe have been explored by site-directed mutagenesis. The amino acids examined could be divided broadly into those presumed from previous related structural studies to be important in the catalytic process (R14, S62 and E93) and those thought to be important in substrate binding (R94, R120 and R121). Most of these residues have not previously been studied by site-directed mutagenesis. All the mutants except R14 were expressed in an engineered null strain of Saccharomyces cerevisiae (S150-gpm:HIS) in good yield. The R14Q mutant was expressed in good yield in the transformed AH22 strain of S. cerevisiae. The S62A mutant was markedly unstable, preventing purification. The various mutants were purified to homogeneity and characterized in terms of kinetic parameters, CD and fluorescence spectra, stability towards denaturation by guanidinium chloride, and stability of phosphorylated enzyme intermediate. In addition, the binding of substrate (3-phosphoglycerate) to wild-type, E93D and R120,121Q enzymes was measured by isothermal titration calorimetry. The results provide evidence for the proposed roles of each of these amino acids in the catalytic cycle and in substrate binding, and will support the current investigation of the structure and dynamics of the enzyme using multidimensional NMR techniques.","authors":"Nairn J, Duncan D, Price NE, Kelly SM, Fothergill-Gilmore LA, Uhrinova S, Barlow PN, Rigden DJ, Price NC","authors_abbrev":"Nairn J et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-12-06","publication_year":"2000","canto_session_key":"236bdabf03aac7e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-13 07:11:33","canto_approved_date":"2023-07-13 07:11:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-03 17:49:44","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26F1.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-07-13"},{"uniquename":"EMBL:SPORF1","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8065904","title":"Identification of the DNA-binding domains of the switch-activating-protein Sap1 from S.pombe by random point mutations screening in E.coli.","citation":"Nucleic Acids Res 1994 Aug 11;22(15):2930-7","abstract":"Mating type switching in fission yeast, Schizosaccharomyces pombe, is initiated by a site-specific double-strand break (DSB) at the mat1 locus. The DSB is controlled from a distance by cis- and trans-acting elements. The switch-activating protein, Sap1 binds to the SAS1 cis-acting element which controls the frequency of the DSB at the mat1 locus and, consequently the efficiency of mating type switching. We developed a general method for screening randomly mutagenized expression libraries of DNA-binding protein in E.coli. Sap1 gene was mutagenized by PCR under conditions of reduced Taq polymerase fidelity. The mutated DNA was expressed in E.coli and screened for SAS1-recognition. This method was used to isolated 16 point mutations that abolished SAS1 interaction together with 18 mutations that did not affect binding. The position of these point mutations allowed the identification of three protein domains located in the N-terminal part of Sap1 that are essential for DNA-binding. Deletions and biochemical analysis showed that Sap1 is a dimer both in solution and when bound to SAS1 sequence. The dimerization domain was localized C-terminally to the three domains described above and when used in exess it inhibited DNA binding.","authors":"Arcangioli B, Ghazvini M, Ribes V","authors_abbrev":"Arcangioli B et al.","pubmed_publication_date":"11 Aug 1994","pubmed_entrez_date":"1994-08-11","publication_year":"1994","canto_session_key":"54d781648ef2d78e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-22 14:07:41","canto_approved_date":"2022-12-06 19:24:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-22 14:07:36","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_8065905_phaf.tsv"}],"genes":["SPCC1672.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-22"},{"uniquename":"TreeFam:TF324563","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC977.14c","YPL088W"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:40635464","title":"Fluorescent protein tags for human tropomyosin isoform comparison.","citation":"Biol Open 2025 Aug 15;14(8)","abstract":"Tropomyosin is an important actin cytoskeletal protein underpinning processes such as muscle contraction, cell shape and cell division. Defects in tropomyosin function can lead to diseases, including some myopathies and allergies. In cells, tropomyosin molecules form coiled-coil dimers, which then polymerise end-to-end with other dimers for actin association. Tropomyosin is challenging to tag for in vivo fluorescence microscopy without perturbing its polymerisation interfaces. We recently developed a fluorescent tag comprising a 40-amino acid flexible linker capable of detecting tropomyosin in S. pombe actin cables and the actomyosin ring, and in patch-like structures that were previously unappreciated. We also used this strategy successfully to tag human TPM2.2, a prominent human muscle isoform. Here, we expanded this tool to visualise eight other human tropomyosin isoforms, using mNeonGreen, mCherry, mStayGold(E138D) and mScarlet3-H tags. All showed typical tropomyosin fluorescence, no signs of cytotoxicity and are compatible with super-resolution microscopy. These tools singly or in combination should aid detailed mechanistic investigations of tropomyosin isoforms.","doi":"10.1242/bio.061992","authors":"Scott W, Polutranko V, Milczarek J, Hands-Portman I, Balasubramanian MK","authors_abbrev":"Scott W et al.","pubmed_publication_date":"15 Aug 2025","pubmed_entrez_date":"2025-07-10","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-07-10 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10799520","title":"Byr4 localizes to spindle-pole bodies in a cell cycle-regulated manner to control Cdc7 localization and septation in fission yeast.","citation":"J Biol Chem 2000 May 12;275(19):14381-7","abstract":"Cytokinesis and septation in the fission yeast Schizosaccharomyces pombe are studied as a model for mammalian cell division. In fission yeast, septation is positively regulated by Spg1, a Ras family GTPase that localizes to spindle-pole bodies (SPBs) throughout the cell cycle. As cells enter mitosis, Spg1 accumulates in an active, GTP-bound form and binds the Cdc7 protein kinase to cause Cdc7 translocation to SPBs. Cdc7 disappears from one SPB in mid-anaphase and from the second SPB in late mitosis. Byr4 plus Cdc16 negatively regulate septation by forming a two-component GTPase-activating protein for Spg1. These results led us to hypothesize that Byr4 localization to SPBs regulated the nucleotide state of Spg1, due to its ability to form Spg1GAP activity with Cdc16 and thus the binding of Cdc7 to Spg1 at SPBs. To test this hypothesis, Byr4 localization was determined using indirect immunofluorescence. This analysis revealed that Byr4 was localized to SPBs that did not contain Cdc7. In byr4(-) mutants, Cdc7 localized to interphase SPBs and only symmetrically localized to mitotic SPBs. In contrast, Byr4 overexpression prevented Spg1 and Cdc7 localization to SPBs. These results suggest that Byr4 localization to SPBs maintains Spg1 in an inactive form, presumably by stimulating Spg1 GTPase activity with Cdc16, and that loss of Byr4 from mitotic SPBs increases the active fraction of Spg1 and thereby increases Spg1-Cdc7 binding. Byr4 localization to SPBs was decreased in spg1, cdc16, sid4, and cdc11 mutants as well as in several mutants that affect medial F-actin structures, suggesting that multiple pathways regulate Byr4 localization to SPBs.","authors":"Li C, Furge KA, Cheng QC, Albright CF","authors_abbrev":"Li C et al.","pubmed_publication_date":"12 May 2000","pubmed_entrez_date":"2000-05-09","publication_year":"2000","canto_session_key":"50db88fdd925afa8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-10-17 08:25:55","canto_approved_date":"2024-09-25 14:04:08","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-10-17 08:25:47","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1565.06c","SPBC244.01c","SPCC1739.11c","SPAC222.10c","SPBC21.06c","SPAC6F6.08c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2021-10-17"},{"uniquename":"PMID:7732727","title":"Molecular cloning of the plc1+ gene of Schizosaccharomyces pombe, which encodes a putative phosphoinositide-specific phospholipase C.","citation":"Yeast 1995 Feb;11(2):179-85","abstract":"Exploiting the polymerase chain reaction, we have isolated a gene that encodes a putative phosphoinositide-specific phospholipase C (PLC) of the fission yeast Schizosaccharomyces pombe. Inspection of the nucleotide sequence of the gene revealed an open reading frame that can encode a polypeptide of 899 amino acid residues with a calculated molecular mass of 102 kDa. This putative polypeptide contains both the X and Y regions that are conserved among three classes of mammalian PLC, and also contains a presumptive Ca(2+)-binding site (an E-F hand motif). The structure of the putative protein is most similar to that of the delta class of PLC isozymes. To investigate the role of this gene, designated plc1+, gene disruption was carried out by interrupting the coding region with the ura4+ marker. Growth of plc1 cells was temperature-sensitive in rich medium, and cells could not grow in synthetic medium. Expression of the PLC1 gene of Saccharomyces cerevisiae suppressed the growth defect phenotype of plc1- cells, a strong suggestion that the plc1+ gene encodes PLC.","authors":"Andoh T, Yoko T, Matsui Y, Toh A","authors_abbrev":"Andoh T et al.","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_session_key":"756d37706d56fb90","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-16 14:21:34","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-10-21 11:23:09","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F8.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-21"},{"uniquename":"PMID:22347400","title":"A genomewide screen for suppressors of Alu-mediated rearrangements reveals a role for PIF1.","citation":"PLoS One 2012;7(2):e30748","abstract":"Alu-mediated rearrangement of tumor suppressor genes occurs frequently during carcinogenesis. In breast cancer, this mechanism contributes to loss of the wild-type BRCA1 allele in inherited disease and to loss of heterozygosity in sporadic cancer. To identify genes required for suppression of Alu-mediated recombination we performed a genomewide screen of a collection of 4672 yeast gene deletion mutants using a direct repeat recombination assay. The primary screen and subsequent analysis identified 12 candidate genes including TSA, ELG1, and RRM3, which are known to play a significant role in maintaining genomic stability. Genetic analysis of the corresponding human homologs was performed in sporadic breast tumors and in inherited BRCA1-associated carcinomas. Sequencing of these genes in high risk breast cancer families revealed a potential role for the helicase PIF1 in cancer predisposition. PIF1 variant L319P was identified in three breast cancer families; importantly, this variant, which is predicted to be functionally damaging, was not identified in a large series of controls nor has it been reported in either dbSNP or the 1000 Genomes Project. In Schizosaccharomyces pombe, Pfh1 is required to maintain both mitochondrial and nuclear genomic integrity. Functional studies in yeast of human PIF1 L319P revealed that this variant cannot complement the essential functions of Pfh1 in either the nucleus or mitochondria. Our results provide a global view of nonessential genes involved in suppressing Alu-mediated recombination and implicate variation in PIF1 in breast cancer predisposition.","doi":"10.1371/journal.pone.0030748","authors":"Chisholm KM, Aubert SD, Freese KP, Zakian VA, King MC, Welcsh PL","authors_abbrev":"Chisholm KM et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-02-21","publication_year":"2012","canto_session_key":"ac7f1c731acedeb3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-08-13 13:46:50","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-12 09:59:53","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC887.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-12"},{"uniquename":"PMID:7867936","title":"A cDNA from Schizosaccharomyces pombe encoding a putative enolase.","citation":"Gene 1995 Feb 27;154(1):109-13","abstract":"Here we report the isolation of an enolase (Eno)-encoding cDNA clone from Schizosaccharomyces pombe. The deduced amino acid (aa) sequence of the 1.4-kb cDNA shares identifies with a number of Eno from Escherichia coli to humans. The highest degree of similarity is to the known Eno from Saccharomyces cerevisiae and an Eno from Candida albicans. Northern blot analysis identified a single transcript of approx. 1.4 kb, which was most abundant when cells were grown in media with glucose as the carbon source, as opposed to glycerol/lactate or ethanol.","authors":"Jackson JC, Lopes JM","authors_abbrev":"Jackson JC et al.","pubmed_publication_date":"27 Feb 1995","pubmed_entrez_date":"1995-02-27","publication_year":"1995","canto_session_key":"f3af39e50b36ef4b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 14:58:37","canto_approved_date":"2019-01-07 14:58:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 14:58:31","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:38837137","title":"The micromammals.","citation":"G3 (Bethesda) 2024 Jun 05;14(6)","abstract":"In this editorial, Senior Editor Susan Forsburg examines the reasons to keep studying eukaryotic microbes like  S. pombe  and  S. cerevisiae —and other yeasts, algae, amoeba, and fungi—even as genetic and genomic technologies now allow manipulation and study of practically any organism. She explores the challenges and opportunities of working in these tiny organisms, pointing to the substantial biology their study has uncovered.","doi":"10.1093/g3journal/jkae073","authors":"Forsburg SL","authors_abbrev":"Forsburg SL","pubmed_publication_date":"05 Jun 2024","pubmed_entrez_date":"2024-06-05","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-06-06 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000047","title":"Gene Ontology annotation based on absence of key sequence residues.","abstract":"This describes a method for supplying a NOT-qualified, IKR-evidenced GO annotation to a gene product, when general sequence homology considerations would suggest a function or location, or a role in a biological process, but where a curator has determined that the absence of key sequence residues, known to be required for an expected activity or location, indicating the gene product is unlikely to be able to carry out the implied activity, involvement in a process or cellular component location. This reference should only be used used when an IKR-evidenced annotation is made based on curator judgement from manually reviewing the sequence of the gene product and where no publication can be found to support the curators conclusion. It is preferable to cite a peer-reviewed publication (such as a PubMed identifier) for IKR-evidenced annotations whenever possible. Curators will have carefully reviewed the sequence of the annotated protein, and established that the key residues known to be required for an expected activity or location are not present. Inclusion of an identifier in the 'with/from' field, that highlights to the user the lacking residues(e.g. an alignment, domain or rule identifier) is absolutely required when annotating to IKR with this GO_REF. Documentation on the GOC website provides more details on the <a href = \"http://www.geneontology.org/GO.evidence.shtml#ikr\">correct use of the IKR evidence code</a>.","authors":"GO curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1E7.04c","SPBC1709.01"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:9693378","title":"The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane.","citation":"Mol Biol Cell 1998 Aug;9(8):2231-47","abstract":"Eukaryotic proteins containing a C-terminal CAAX motif undergo a series of posttranslational CAAX-processing events that include isoprenylation, C-terminal proteolytic cleavage, and carboxyl methylation. We demonstrated previously that the STE14 gene product of Saccharomyces cerevisiae mediates the carboxyl methylation step of CAAX processing in yeast. In this study, we have investigated the subcellular localization of Ste14p, a predicted membrane-spanning protein, using a polyclonal antibody generated against the C terminus of Ste14p and an in vitro methyltransferase assay. We demonstrate by immunofluorescence and subcellular fractionation that Ste14p and its associated activity are localized to the endoplasmic reticulum (ER) membrane of yeast. In addition, other studies from our laboratory have shown that the CAAX proteases are also ER membrane proteins. Together these results indicate that the intracellular site of CAAX protein processing is the ER membrane, presumably on its cytosolic face. Interestingly, the insertion of a hemagglutinin epitope tag at the N terminus, at the C terminus, or at an internal site disrupts the ER localization of Ste14p and results in its mislocalization, apparently to the Golgi. We have also expressed the Ste14p homologue from Schizosaccharomyces pombe, mam4p, in S. cerevisiae and have shown that mam4p complements a Deltaste14 mutant. This finding, plus additional recent examples of cross-species complementation, indicates that the CAAX methyltransferase family consists of functional homologues.","authors":"Romano JD, Schmidt WK, Michaelis S","authors_abbrev":"Romano JD et al.","pubmed_publication_date":"Aug 1998","pubmed_entrez_date":"1998-08-07","publication_year":"1998","canto_session_key":"6959ca34d0bd6d1f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 16:45:12","canto_session_submitted_date":"2012-03-03 16:44:48","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC10F6.12c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:12207226","title":"Poly(A) site choice during mRNA 3'-end formation in the Schizosaccharomyces pombe wos2 gene.","citation":"Mol Genet Genomics 2002 Aug;267(6):792-6","abstract":"In the fission yeast Schizosaccharomyces pombe, the wos2 gene encodes p23, a highly conserved protein which functions as a co-chaperone for the heat shock protein Hsp90. This p23 protein binds to Hsp90, but its activities and regulatory mechanisms are still unclear. Northern analysis has shown that the wos2 gene produces three transcripts of about 1.1, 0.9 and 0.8 kb, which are expressed differentially depending on the growth temperature. The largest and the smallest transcripts were most abundant at 25 degrees C, whereas the 0.9-kb transcript predominated at 37 degrees C. A time-course analysis indicated that this 0.9-kb species rapidly increased in abundance after a shift from 25 degrees C to 37 degrees C, reaching a maximum after 15 min. A shift back to 25 degrees C resulted in a decline in the amount of this transcript, albeit at a slower rate. Expression analysis of wos2:ura4 and nmt1:wos2 constructs showed that the 3' untranslated region of wos2 alone directs the formation of these multiple, discrete wos2 mRNAs. Sequence analysis of cDNAs derived from these mRNAs showed that the use of different polyadenylation sites results in the production of the three differently sized wos2 transcripts. In the case of the 0.9- and 0.8-kb mRNA species, these sites lie in a predicted hairpin loop in the mRNA, suggesting that polyadenylation signals in wos2 transcripts may be mediated by RNA secondary structure. The possibility that differential thermal stability of these hairpin structures could influence polyadenylation site choice during formation of the 3'-ends of the mRNAs is discussed.","authors":"Muñoz MJ, Daga RR, Garzón A, Thode G, Jimenez J","authors_abbrev":"Muñoz MJ et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-09-11","publication_year":"2002","canto_session_key":"d21cf7d5b01ef3ae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-11-09 17:29:59","canto_approved_date":"2023-11-09 17:29:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-06 03:53:28","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9E9.13"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2023-11-09"},{"uniquename":"PMID:3916718","title":"Rapid alkaline preparation for yeast circular covalently closed DNA molecules.","citation":"Curr Genet 1985;9(2):123-6","abstract":"The alkaline preparation of prokaryotic plasmids (Birnboim and Doly, 1979) has been here adapted to yeast. By simple denaturation and renaturation steps we recovered, from Saccharomyces cerevisiae and Schizosaccharomyces pombe, a population of nucleic acid molecules highly enriched in circular forms. In S. cerevisiae killer strains it is possible to copurify double stranded RNA molecules. The overall recovery was estimated to be 10-30% of the total circular molecules.","authors":"Filetici P, Junakovic N, Ballario P","authors_abbrev":"Filetici P et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11918671","title":"Level of the RNA polymerase II in the fission yeast stays constant but phosphorylation of its carboxyl terminal domain varies depending on the phase and rate of cell growth.","citation":"Genes Cells 2002 Mar;7(3):273-84","abstract":"The RNA polymerase II of the fission yeast Schizosaccharomyces pombe consists of 12 Rpb subunits, of which four (Rpb1, Rpb2, Rpb3 and Rpb11) form the assembly and catalytic core and five (Rpb5, Rpb6, Rpb8, Rpb10 and Rpb12) are shared among RNA polymerases I, II and III. The intracellular levels of three RNA polymerase forms should be interrelated, but the control of RNA polymerase formation remains mostly unknown.\nTo reveal the physiological role and the synthesis control of each Rpb subunit, the intracellular levels of the Rpb proteins were examined in S. pombe growing at various phases under various conditions. Results indicate that the intracellular concentrations of the Rpb proteins stay constant at levels characteristic of the rate and phase of cell growth, and the relative level between the 12 subunits also remains constant, together implying that the intracellular concentration of RNA polymerase II stays constant, as in the case of prokaryotes. As an attempt to gain insights into the activity control of RNA polymerase II, we also analysed the phosphorylation level of the carboxyl-terminal domain (CTD) of the largest subunit Rpb1. Phosphorylated forms of Tyr1 and Thr4 within 29 repeats of the YSPTSPS heptapeptide were detected in both slow-migrating IIo and fast-migrating IIa forms of Rpb1 on SDS-PAGE (polyacrylamide gel electrophoresis). However, phosphorylated Ser2 and Ser5 were identified only in the IIo form, indicating that Ser phosphorylation contributes to the conformational change in CTD. The phosphorylation levels of Ser, Thr and Tyr all vary depending on the cell culture conditions.\nThe intracellular level of RNA polymerase II stays constant, but the amount engaged in transcription cycle varies depending on the culture conditions, as estimated from the sites and levels of phosphorylation of Rpb1 CTD.","authors":"Sakurai H, Ishihama A","authors_abbrev":"Sakurai H et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-29","publication_year":"2002","canto_session_key":"56e7806a8b535223","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-26 17:22:02","canto_approved_date":"2023-05-12 02:18:01","canto_approver_orcid":"0000-0001-6277-726X","canto_session_submitted_date":"2015-11-26 17:21:54","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3A12.07","SPBC337.14","SPBC14C8.12","SPAPYUG7.04c","SPCC1020.04c","SPCC1442.10c","SPAC23C4.15","SPAC23G3.01","SPACUNK4.06c","SPAC2F3.03c","SPBC28F2.12","SPBC1289.07c"],"gene_count":12,"ltp_gene_count":1,"approved_date":"2015-11-26"},{"uniquename":"PMID:24256270","title":"Understanding non-coding DNA regions in yeast.","citation":"Biochem Soc Trans 2013 Dec;41(6):1654-9","abstract":"Non-coding transcripts play an important role in gene expression regulation in all species, including budding and fission yeast. Such regulatory transcripts include intergenic ncRNA (non-coding RNA), 5' and 3' UTRs, introns and antisense transcripts. In the present review, we discuss advantages and limitations of recently developed sequencing techniques, such as ESTs, DNA microarrays, RNA-Seq (RNA sequencing), DRS (direct RNA sequencing) and TIF-Seq (transcript isoform sequencing). We provide an overview of methods applied in yeast and how each of them has contributed to our knowledge of gene expression regulation and transcription.","doi":"10.1042/BST20130144","authors":"Schlackow M, Gullerova M","authors_abbrev":"Schlackow M et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-22","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28366642","title":"Spt5 Plays Vital Roles in the Control of Sense and Antisense Transcription Elongation.","citation":"Mol Cell 2017 Apr 06;66(1):77-88.e5","abstract":"Spt5 is an essential and conserved factor that functions in transcription and co-transcriptional processes. However, many aspects of the requirement for Spt5 in transcription are poorly understood. We have analyzed the consequences of Spt5 depletion in Schizosaccharomyces pombe using four genome-wide approaches. Our results demonstrate that Spt5 is crucial for a normal rate of RNA synthesis and distribution of RNAPII over transcription units. In the absence of Spt5, RNAPII localization changes dramatically, with reduced levels and a relative accumulation over the first ∼500 bp, suggesting that Spt5 is required for transcription past a barrier. Spt5 depletion also results in widespread antisense transcription initiating within this barrier region. Deletions of this region alter the distribution of RNAPII on the sense strand, suggesting that the barrier observed after Spt5 depletion is normally a site at which Spt5 stimulates elongation. Our results reveal a global requirement for Spt5 in transcription elongation.","doi":"10.1016/j.molcel.2017.02.023","authors":"Shetty A, Kallgren SP, Demel C, Maier KC, Spatt D, Alver BH, Cramer P, Park PJ, Winston F","authors_abbrev":"Shetty A et al.","pubmed_publication_date":"06 Apr 2017","pubmed_entrez_date":"2017-04-04","publication_year":"2017","canto_session_key":"3cf736f8c8908f87","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Fred Winston","canto_first_approved_date":"2018-04-04 15:10:51","canto_approved_date":"2024-10-07 07:42:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-30 23:27:01","canto_added_date":"2017-04-05 00:15:12","annotation_curators":[{"name":"Fred Winston","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.03","SPAC1A6.04c","SPAC18B11.07c","SPBC651.09c","SPBC28F2.12","SPAC6F6.17","SPAC18G6.09c","SPAC19G12.08","SPAC1F3.01","SPAC29B12.02c","SPAPJ760.03c","SPBC119.10","SPAC23C4.19","SPCC1442.10c","SPAC1F7.01c","SPCC306.04c"],"gene_count":16,"ltp_gene_count":2,"approved_date":"2018-04-04"},{"uniquename":"PMID:15164362","title":"Transcriptional and post-translational regulation of neutral trehalase in Schizosaccharomyces pombe during thermal stress.","citation":"Yeast 2004 May;21(7):593-603","abstract":"In the fission yeast Schizosaccharomyces pombe, a heat shock enhances transcription of the ntp1(+) gene, encoding the hydrolytic enzyme neutral trehalase. As compared to wild-type cells, cells devoid of the MAP kinase Sty1p showed a strong decrease in ntp1(+) expression induced by the temperature upshift, indicating that the stress-activated protein kinase (SAPK) pathway regulates the expression of this gene during heat shock. The transcription factor Atf1p, which is the main downstream target for Sty1p in the SAPK pathway, appears to be involved in such control, since ntp1(+) expression under heat shock proved to be significantly blocked in atf1(+)-disrupted cells. Serial deletion and point mutation analyses of the ntp1(+) promoter, as well as electrophoretic mobility shift assays, revealed the existence of a CRE-like element as the target for Atf1p-mediated expression under thermal stress. The relevance of two putative HSE elements located in the ntp1(+) promoter was also investigated for their potential role in regulating ntp1(+) transcription during heat shock. The results support a model in which heat-induced Atf1p binding to the CRE-like element favours the subsequent interaction of the heat shock factor (HSF) with HSE elements in the ntp1(+) promoter. Unlike what happens under osmostress or oxidative treatments, Sty1p has no role in the post-translational activation of neutral trehalase induced by heat shock in the fission yeast.","authors":"Paredes V, Franco A, Madrid M, Soto T, Vicente-Soler J, Gacto M, Cansado J","authors_abbrev":"Paredes V et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-05-28","publication_year":"2004","canto_session_key":"54a26a25997d999a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-10-29 14:23:51","canto_approved_date":"2022-08-30 08:55:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-29 14:23:46","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPBC660.07","SPAC24B11.06c","SPAC21E11.03c","SPAC1783.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-10-29"},{"uniquename":"PMID:39520300","title":"Proteins and noncoding RNAs that promote homologous chromosome recognition and pairing in fission yeast meiosis undergo condensate formation in vitro.","citation":"FASEB J 2024 Nov 15;38(21):e70163","abstract":"Pairing of homologous chromosomes during meiosis is crucial for successful sexual reproduction. Previous studies have shown that the fission yeast sme2 RNA, a meiosis-specific long noncoding RNA (lncRNA), accumulates at the sme2 locus and plays a key role in mediating robust pairing during meiosis. Several RNA-binding proteins accumulate at the sme2 and other lncRNA gene loci in conjunction with the lncRNAs transcribed from these loci. These lncRNA-protein complexes form condensates that exhibit phase separation properties on chromosomes and are necessary for robust pairing of homologous chromosomes. To further understand the mechanisms by which phase separation affects homologous chromosome pairing, we conducted an in vitro phase separation assay with the sme2 RNA-associated proteins (Smps) and RNAs. Our findings reveal that one of the Smps, Seb1, forms condensates resembling phase separation; the observed number and size of these condensates increase upon the addition of another Smp, Rhn1, and purified RNAs. Additionally, we have found that RNAs protect Smp condensates from treatment with 1,6-hexanediol. The Smp condensates containing different types of RNA display distinct FRAP profiles, and the Smp condensates containing the same type of RNA tend to fuse together more readily than those containing different types of RNAs. Collectively, these results indicate that the specific RNA species within condensates modulate their physical properties, potentially enabling the formation of regional RNA-Smp condensates with distinct characteristics that facilitate homologous chromosome pairing.","doi":"10.1096/fj.202302563RR","authors":"Ding DQ, Okamasa K, Yoshimura Y, Matsuda A, Yamamoto TG, Hiraoka Y, Nakayama JI","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"15 Nov 2024","pubmed_entrez_date":"2024-11-09","publication_year":"2024","canto_session_key":"f592b2691e524e16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-ichi Nakayama","canto_first_approved_date":"2025-01-21 11:13:09","canto_approved_date":"2025-01-21 11:13:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-01-17 06:22:58","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[{"name":"Jun-ichi Nakayama","community_curator":true,"annotation_count":4,"orcid":"0000-0002-5597-8239","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.11c","SPAC644.16","SPBC16E9.12c","SPAC222.09","SPAC4G9.04c","SPBC337.03","SPNCRNA.130","SPNCRNA.103"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2025-01-21"},{"uniquename":"PMID:9973368","title":"Cell surface galactosylation is essential for nonsexual flocculation in Schizosaccharomyces pombe.","citation":"J Bacteriol 1999 Feb;181(4):1356-9","abstract":"We have isolated fission yeast mutants that constitutively flocculate upon growth in liquid media. One of these mutants, the gsf1 mutant, was found to cause dominant, nonsexual, and calcium-dependent aggregation of cells into flocs. Its flocculation was inhibited by the addition of galactose but was not affected by the addition of mannose or glucose, unlike Saccharomyces cerevisiae FLO mutants. The gsf1 mutant coflocculated with Schizosaccharomyces pombe wild-type cells, while no coflocculation was found with galactose-deficient (gms1Delta) cells. Moreover, flocculation of the gsf1 mutant was also inhibited by addition of cell wall galactomannan from wild-type cells but not from gms1Delta cells. These results suggested that galactose residues in the cell wall glycoproteins may be receptors of gsf1-mediated flocculation, and therefore cell surface galactosylation is required for nonsexual flocculation in S. pombe.","authors":"Tanaka N, Awai A, Bhuiyan MS, Fujita K, Fukui H, Takegawa K","authors_abbrev":"Tanaka N et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-02-11","publication_year":"1999","canto_session_key":"277a64012366b14f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-04 15:47:10","canto_approved_date":"2025-05-19 08:13:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-28 13:34:37","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC15D4.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-04"},{"uniquename":"PMID:31405990","title":"RNA-DNA Hybrids Support Recombination-Based Telomere Maintenance in Fission Yeast.","citation":"Genetics 2019 Oct;213(2):431-447","abstract":"A subset of cancers rely on telomerase-independent mechanisms to maintain their chromosome ends. The predominant \"alternative lengthening of telomeres\" pathway appears dependent on homology-directed repair (HDR) to maintain telomeric DNA. However, the molecular changes needed for cells to productively engage in telomeric HDR are poorly understood. To gain new insights into this transition, we monitored the state of telomeres during serial culture of fission yeast ( Schizosaccharomyces pombe ) lacking the telomerase recruitment factor Ccq1. Rad52 is loaded onto critically short telomeres shortly after germination despite continued telomere erosion, suggesting that recruitment of recombination factors is not sufficient to maintain telomeres in the absence of telomerase function. Instead, survivor formation coincides with the derepression of telomeric repeat-containing RNA (TERRA). In this context, degradation of TERRA associated with the telomere in the form of R-loops drives a severe growth crisis, ultimately leading to a novel type of survivor with linear chromosomes and altered cytological telomere characteristics, including the loss of the shelterin component Rap1 (but not the TRF1/TRF2 ortholog, Taz1) from the telomere. We demonstrate that deletion of Rap1 is protective in this context, preventing the growth crisis that is otherwise triggered by degradation of telomeric R-loops in survivors with linear chromosomes. These findings suggest that upregulation of telomere-engaged TERRA, or altered recruitment of shelterin components, can support telomerase-independent telomere maintenance.","doi":"10.1534/genetics.119.302606","authors":"Hu Y, Bennett HW, Liu N, Moravec M, Williams JF, Azzalin CM, King MC","authors_abbrev":"Hu Y et al.","pubmed_publication_date":"Oct 2019","pubmed_entrez_date":"2019-08-14","publication_year":"2019","canto_session_key":"4e543d94b99bb08c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-08-15 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22809830","title":"New multi-purpose high copy number vector with greater mitotic stability for diverse applications in fission yeast Schizosaccharomyces pombe.","citation":"Plasmid 2012 Nov;68(3):186-94","abstract":"We have constructed a pUC19-based multipurpose ATG vector in Schizosaccharomyces pombe with higher copy number and mitotic stability possible with commonly used vectors. The vector, having an NdeI site in its polylinker to provide ATG site for expression, carries a greatly truncated version of URA3 gene, URA3m, of Saccharomyces cerevisiae as a selection marker. In addition, it contains the mat2P-right flank region (mat2P-RF) of S. pombe as an autonomous replicating sequence (ARS) and a polylinker with wider choice of restriction sites. While URA3m confers an increase in plasmid copy number up to 200 copies/cell, mat2P-RF imparts greater mitotic stability than the standard ars1 element of S. pombe. Finally, the vector also includes the transcription termination signal of the nmt1 gene (Tnmt1). This basic vector should serve as a versatile tool for studies of gene function in S. pombe.","doi":"10.1016/j.plasmid.2012.07.001","authors":"Verma HK, Singh J","authors_abbrev":"Verma HK et al.","pubmed_publication_date":"Nov 2012","pubmed_entrez_date":"2012-07-20","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11073994","title":"Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes.","citation":"Mol Cell Biol 2000 Dec;20(23):8944-57","abstract":"Transcripts harboring premature signals for translation termination are recognized and rapidly degraded by eukaryotic cells through a pathway known as nonsense-mediated mRNA decay (NMD). In addition to protecting cells by preventing the translation of potentially deleterious truncated peptides, studies have suggested that NMD plays a broader role in the regulation of the steady-state levels of physiologic transcripts. In Saccharomyces cerevisiae, three trans-acting factors (Upf1p to Upf3p) are required for NMD. Orthologues of Upf1p have been identified in numerous species, showing that the NMD machinery, at least in part, is conserved through evolution. In this study, we demonstrate additional functional conservation of the NMD pathway through the identification of Upf2p homologues in Schizosaccharomyces pombe and humans (rent2). Disruption of S. pombe UPF2 established that this gene is required for NMD in fission yeast. rent2 was demonstrated to interact directly with rent1, a known trans-effector of NMD in mammalian cells. Additionally, fragments of rent2 were shown to possess nuclear targeting activity, although the native protein localizes to the cytoplasmic compartment. Finally, novel functional domains of Upf2p and rent2 with homology to eukaryotic initiation factor 4G (eIF4G) and other translational regulatory proteins were identified. Directed mutations within these so-called eIF4G homology (4GH) domains were sufficient to abolish the function of S. pombe Upf2p. Furthermore, using the two-hybrid system, we obtained evidence for direct interaction between rent2 and human eIF4AI and Sui1, both components of the translation initiation complex. Based on these findings, a novel model in which Upf2p and rent2 effects decreased translation and accelerated decay of nonsense transcripts through competitive interactions with eIF4G-binding partners is proposed.","authors":"Mendell JT, Medghalchi SM, Lake RG, Noensie EN, Dietz HC","authors_abbrev":"Mendell JT et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-14","publication_year":"2000","canto_session_key":"6ab8ed95449f4292","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-10-27 15:11:08","canto_approved_date":"2021-11-08 16:54:08","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-10-27 15:11:01","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19A8.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-10-27"},{"uniquename":"PMID:27028824","title":"[New Class of Sfr1 Protein Repeats Essential for Homologous Recombination in Schizosaccharomyces pombe Yeast in Mitosis].","citation":"Mol Biol (Mosk) 2016;50(1):179-83","abstract":"","doi":"10.7868/S0026898416010067","authors":"Khasanova OS, Khasanov FK","authors_abbrev":"Khasanova OS et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-03-31","publication_year":"2016","canto_triage_status":"Not English","canto_curator_role":"PomBase","canto_added_date":"2016-04-01 00:15:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23849629","title":"Division of labor between the chromodomains of HP1 and Suv39 methylase enables coordination of heterochromatin spread.","citation":"Mol Cell 2013 Jul 11;51(1):80-91","abstract":"In Schizosaccharomyces pombe, heterochromatin spread, which is marked by histone 3 lysine 9 methylation (H3K9me), requires the chromodomains (CDs) of the H3K9 methylase Suv39/Clr4 and the HP1/Swi6 protein. It is unclear how the actions of these two H3K9me-recognizing CDs are coordinated. We find that the intrinsic preference of Suv39/Clr4 is to generate dimethylated H3K9 product. The recognition of pre-existing H3K9me marks by the CD of Suv39/Clr4 stimulates overall catalysis, enabling the accumulation of small amounts of trimethylated product in vivo. Coincidentally, the Suv39/Clr4 CD, unlike the HP1/Swi6 CD, has been shown to prefer the trimethyl state over the dimethyl state. We show that this preference enables efficient heterochromatin spread in vivo by reducing competition with HP1 proteins for the more prevalent dimethyl state. Our results reveal a strategy by which \"writers\" and \"readers\" of a chromatin mark exploit different methylation states on the same residue in order to facilitate collaboration and avoid competition.","doi":"10.1016/j.molcel.2013.06.013","authors":"Al-Sady B, Madhani HD, Narlikar GJ","authors_abbrev":"Al-Sady B et al.","pubmed_publication_date":"11 Jul 2013","pubmed_entrez_date":"2013-07-16","publication_year":"2013","canto_session_key":"17e2a4dd60231bcc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c","SPAC1834.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:36178345","title":"Evolution of cell size control is canalized towards adders or sizers by cell cycle structure and selective pressures.","citation":"Elife 2022 Sep 30;11","abstract":"Cell size is controlled to be within a specific range to support physiological function. To control their size, cells use diverse mechanisms ranging from 'sizers', in which differences in cell size are compensated for in a single cell division cycle, to 'adders', in which a constant amount of cell growth occurs in each cell cycle. This diversity raises the question why a particular cell would implement one rather than another mechanism? To address this question, we performed a series of simulations evolving cell size control networks. The size control mechanism that evolved was influenced by both cell cycle structure and specific selection pressures. Moreover, evolved networks recapitulated known size control properties of naturally occurring networks. If the mechanism is based on a G1 size control and an S/G2/M timer, as found for budding yeast and some human cells, adders likely evolve. But, if the G1 phase is significantly longer than the S/G2/M phase, as is often the case in mammalian cells in vivo, sizers become more likely. Sizers also evolve when the cell cycle structure is inverted so that G1 is a timer, while S/G2/M performs size control, as is the case for the fission yeast  S. pombe . For some size control networks, cell size consistently decreases in each cycle until a burst of cell cycle inhibitor drives an extended G1 phase much like the cell division cycle of the green algae  Chlamydomonas . That these size control networks evolved such self-organized criticality shows how the evolution of complex systems can drive the emergence of critical processes.","doi":"10.7554/eLife.79919","authors":"Proulx-Giraldeau F, Skotheim JM, François P","authors_abbrev":"Proulx-Giraldeau F et al.","pubmed_publication_date":"30 Sep 2022","pubmed_entrez_date":"2022-09-30","publication_year":"2022","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2022-10-02 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38669080","title":"Short-homology-mediated PCR-based method for gene introduction in the fission yeast Schizosaccharomyces pombe.","citation":"Brief Funct Genomics 2024 Apr 26;","abstract":"Schizosaccharomyces pombe is a commonly utilized model organism for studying various aspects of eukaryotic cell physiology. One reason for its widespread use as an experimental system is the ease of genetic manipulations, leveraging the natural homology-targeted repair mechanism to accurately modify the genome. We conducted a study to assess the feasibility and efficiency of directly introducing exogenous genes into the fission yeast S. pombe using Polymerase Chain Reaction (PCR) with short-homology flanking sequences. Specifically, we amplified the NatMX6 gene (which provides resistance to nourseothricin) using PCR with oligonucleotides that had short flanking regions of 20 bp, 40 bp, 60 bp and 80 bp to the target gene. By using this purified PCR product, we successfully introduced the NatMX6 gene at position 171 385 on chromosome III in S. pombe. We have made a simple modification to the transformation procedure, resulting in a significant increase in transformation efficiency by at least 5-fold. The success rate of gene integration at the target position varied between 20% and 50% depending on the length of the flanking regions. Additionally, we discovered that the addition of dimethyl sulfoxide and boiled carrier DNA increased the number of transformants by ~60- and 3-fold, respectively. Furthermore, we found that the removal of the pku70+ gene improved the transformation efficiency to ~5% and reduced the formation of small background colonies. Overall, our results demonstrate that with this modified method, even very short stretches of homologous regions (as short as 20 bp) can be used to effectively target genes at a high frequency in S. pombe. This finding greatly facilitates the introduction of exogenous genes in this organism.","doi":"10.1093/bfgp/elae016","authors":"Zhang CX, Hou YC","authors_abbrev":"Zhang CX et al.","pubmed_publication_date":"26 Apr 2024","pubmed_entrez_date":"2024-04-26","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-04-26 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10982411","title":"A zinc-finger protein, Rst2p, regulates transcription of the fission yeast ste11(+) gene, which encodes a pivotal transcription factor for sexual development.","citation":"Mol Biol Cell 2000 Sep;11(9):3205-17","abstract":"Schizosaccharomyces pombe ste11 encodes a high-mobility group family transcriptional activator that is pivotal in sexual development. Transcription of ste11 is induced by starvation of nutrients via a decrease of the cAMP-dependent protein kinase (PKA) activity. Here we report the identification of a novel transcription factor, Rst2p, that directly regulates ste11 expression. Cells in which the rst2 gene was disrupted expressed ste11 poorly and were sterile, and this sterility could be suppressed by artificial expression of ste11. Disruption of rst2 suppressed hypermating and hypersporulation in the PKA-null mutant, whereas overexpression of rst2 induced sexual development in the PKA-activated mutant. Cloning analysis indicated that Rst2p was a Cys(2)His(2) zinc-finger protein carrying 567 amino acid residues. Rst2p could bind specifically to a stress response element-like cis element located in the ste11 promoter region, which was important for ste11 expression. Meanwhile, transcription of ste11 was reduced significantly by a defective mutation in itself. An artificial supply of functional Ste11p circumvented this reduction. A complete Ste11p-binding motif (TR box) found in the promoter region was necessary for the full expression of ste11, suggesting that Ste11p is involved in the activation of ste11. We conclude that transcription of ste11 is under autoregulation in addition to control through the PKA-Rst2p pathway.","authors":"Kunitomo H, Higuchi T, Iino Y, Yamamoto M","authors_abbrev":"Kunitomo H et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-09-12","publication_year":"2000","canto_session_key":"81b55b09766cafa9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-01 18:09:19","canto_approved_date":"2026-04-11 20:18:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-03 08:33:38","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":30,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10","SPBC32C12.02","SPAC6F12.02","SPAC8C9.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-11-01"},{"uniquename":"PMID:28918508","title":"Metabolic engineering of Schizosaccharomyces pombe to produce punicic acid, a conjugated fatty acid with nutraceutic properties.","citation":"Appl Microbiol Biotechnol 2017 Nov;101(21):7913-7922","abstract":"Punicic acid (PuA) is a conjugated linolenic acid (C18:3Δ 9c,11t,13c ) with a wide range of nutraceutic effects with the potential to reduce the incidence of a number of health disorders including diabetes, obesity, and cancer. It is the main component of seed oil from Punica granatum and Trichosanthes kirilowii. Previously, production of relatively high levels of this unusual fatty acid in the seed oil of transgenic Arabidopsis thaliana plant was accomplished by the use of A. thaliana fad3/fae1 mutant high in linoleic acid (18:2∆ 9c,12c ) and by co-expression of P. granatum FATTY ACID CONJUGASE (PgFADX) with Δ12-DESATURASE (FAD2). In the current study, P. granatum cDNAs governing PuA production were introduced into the yeast Schizosaccharomyces pombe. Expression of PgFADX alone resulted in production of PuA at the level of 19.6% of total fatty acids. Co-expression PgFADX with PgFAD2, however, further enhanced PuA content to 25.1% of total fatty acids, the highest level reported to date for heterologous expression. Therefore, microbial systems can be considered as a potential alternative to plant sources for a source of PuA for nutraceutic applications.","doi":"10.1007/s00253-017-8498-8","authors":"Garaiova M, Mietkiewska E, Weselake RJ, Holic R","authors_abbrev":"Garaiova M et al.","pubmed_publication_date":"Nov 2017","pubmed_entrez_date":"2017-09-18","publication_year":"2017","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2017-09-19 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26152728","title":"A Two-step Protein Quality Control Pathway for a Misfolded DJ-1 Variant in Fission Yeast.","citation":"J Biol Chem 2015 Aug 21;290(34):21141-21153","abstract":"A mutation, L166P, in the cytosolic protein, PARK7/DJ-1, causes protein misfolding and is linked to Parkinson disease. Here, we identify the fission yeast protein Sdj1 as the orthologue of DJ-1 and calculate by in silico saturation mutagenesis the effects of point mutants on its structural stability. We also map the degradation pathways for Sdj1-L169P, the fission yeast orthologue of the disease-causing DJ-1 L166P protein. Sdj1-L169P forms inclusions, which are enriched for the Hsp104 disaggregase. Hsp104 and Hsp70-type chaperones are required for efficient degradation of Sdj1-L169P. This also depends on the ribosome-associated E3 ligase Ltn1 and its co-factor Rqc1. Although Hsp104 is absolutely required for proteasomal degradation of Sdj1-L169P aggregates, the degradation of already aggregated Sdj1-L169P occurs independently of Ltn1 and Rqc1. Thus, our data point to soluble Sdj1-L169P being targeted early by Ltn1 and Rqc1. The fraction of Sdj1-L169P that escapes this first inspection then forms aggregates that are subsequently cleared via an Hsp104- and proteasome-dependent pathway.","doi":"10.1074/jbc.M115.662312","authors":"Mathiassen SG, Larsen IB, Poulsen EG, Madsen CT, Papaleo E, Lindorff-Larsen K, Kragelund BB, Nielsen ML, Kriegenburg F, Hartmann-Petersen R","authors_abbrev":"Mathiassen SG et al.","pubmed_publication_date":"21 Aug 2015","pubmed_entrez_date":"2015-07-09","publication_year":"2015","canto_session_key":"d800c02f9eed68d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rasmus Hartmann-Petersen","canto_first_approved_date":"2018-03-24 18:06:23","canto_approved_date":"2024-12-05 16:46:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-19 05:57:53","canto_added_date":"2015-07-11 00:21:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Rasmus Hartmann-Petersen","community_curator":true,"annotation_count":24,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.11","SPBC11C11.09c","SPBC1711.06","SPAC22A12.15c","SPBC776.01","SPCC132.04c","SPAC1142.01","SPAC694.05c","SPBC18H10.13","SPBC2G5.06c","SPAC1250.05","SPCC757.09c","SPAC3F10.03","SPCC584.04","SPBC1703.13c","SPCC1183.07","SPAC26H5.09c","SPAC144.11","SPBC16D10.08c","SPAC3H5.10","SPAC23G3.06","SPAC3H5.07","SPBC21D10.09c","SPAC521.05","SPCC584.01c","SPBC19F5.03","SPAC458.02c","SPBC11C11.07","SPAC24H6.04","SPAC23H4.10c","SPCC24B10.09","SPBC106.18","SPBC26H8.07c","SPAC5D6.01","SPAC4H3.01","SPBC646.10c","SPAP27G11.13c","SPCC622.18","SPBP8B7.03c","SPAC144.12","SPBC215.05","SPCC1322.13","SPAPB1E7.12","SPAC29A4.02c","SPAC3H5.05c","SPAC6F6.07c","SPAC17A2.13c","SPAC4G9.16c","SPBC83.08","SPCC736.15","SPAC890.08","SPAC6G10.08","SPBC16D10.11c","SPBC18H10.12c","SPBC354.12","SPAC26A3.04","SPBC23G7.12c","SPBC685.07c","SPBC365.03c","SPBC1734.11","SPAC19G12.05","SPBC17A3.04c","SPAC22G7.06c","SPAC1805.11c","SPAC1805.13","SPBC17G9.10","SPBC1A4.02c","SPBC1105.02c","SPBC2F12.04","SPAC22H12.04c","SPCC576.08c","SPAC3A11.12c","SPAC57A7.12","SPCC1739.13","SPBC29B5.03c","SPAC6B12.12","SPCC1322.11","SPACUNK4.15","SPBC428.05c","SPAC25B8.12c","SPAPB1E7.07","SPBC215.08c","SPBC947.15c","SPAC959.07","SPBC17G9.11c","SPAC17H9.05","SPAC3G9.11c","SPCC364.06","SPCC613.06","SPAPB8E5.06c","SPAC11E3.15","SPAC1F7.04","SPBC29A3.12","SPAC1071.07c","SPAC222.08c","SPBC3F6.03","SPBC2F12.07c","SPAC1834.04","SPCC1620.08","SPBC20F10.01","SPCC18B5.01c","SPBC1703.10","SPBC800.04c","SPCC74.05","SPAC110.04c","SPBC16H5.02","SPAC6C3.08","SPBC9B6.04c","SPAC23H3.09c","SPCC1906.01","SPAC14C4.14","SPAC18G6.14c","SPBC3E7.02c","SPAC328.10c","SPCC1620.06c","SPAC1834.02","SPCC13B11.01","SPAC4A8.11c","SPBC26H8.01","SPBC21C3.13","SPBC2D10.10c","SPAC13G7.02c","SPBC405.07","SPCC330.14c","SPBC29A3.04","SPCP31B10.08c","SPBC16G5.14c","SPAP8A3.07c","SPCC31H12.04c","SPBC21B10.10","SPAC13G6.02c","SPAC1565.08","SPAC1783.08c","SPBC18H10.02","SPAPB17E12.13","SPBC1289.03c","SPAC17G6.06","SPAC694.02","SPCC1393.03","SPCC1682.16","SPBC16H5.08c","SPCC330.06c","SPCC5E4.07","SPAC22E12.03c","SPCC1682.05c","SPAC1F8.07c","SPBC4F6.04","SPCC613.05c","SPAC17A5.15c","SPAC56E4.04c"],"gene_count":150,"ltp_gene_count":28,"approved_date":"2018-03-24"},{"uniquename":"PMID:28049809","title":"Electron Microscopy of Fission Yeast.","citation":"Cold Spring Harb Protoc 2017 Jan 03;2017(1)","abstract":"Electron microscopy (EM) can provide images of cells with a spatial resolution that significantly surpasses that available from light microscopy (LM), even with modern methods that give LM \"super resolution.\" However, EM resolution comes with costs in time spent with sample preparation, expense of instrumentation, and concerns regarding sample preparation artifacts. It is therefore important to know the limitations of EM as well as its strengths. Here we describe the most reliable methods for the preservation of fission yeast cells currently available. We describe the properties of images obtained by transmission EM (TEM) and contrast them with images from scanning EM (SEM). We also show how one can make three-dimensional TEM images and discuss several approaches to address the problem of localizing specific proteins within cells. We give references to work by others who have pursued similar goals with different methods, and we discuss briefly the complex subject of image interpretation.","doi":"10.1101/pdb.top079822","authors":"McIntosh JR, Morphew MK, Giddings TH","authors_abbrev":"McIntosh JR et al.","pubmed_publication_date":"03 Jan 2017","pubmed_entrez_date":"2017-01-05","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-01-06 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32915140","title":"Large domains of heterochromatin direct the formation of short mitotic chromosome loops.","citation":"Elife 2020 Sep 11;9","abstract":"During mitosis chromosomes reorganise into highly compact, rod-shaped forms, thought to consist of consecutive chromatin loops around a central protein scaffold. Condensin complexes are involved in chromatin compaction, but the contribution of other chromatin proteins, DNA sequence and histone modifications is less understood. A large region of fission yeast DNA inserted into a mouse chromosome was previously observed to adopt a mitotic organisation distinct from that of surrounding mouse DNA. Here, we show that a similar distinct structure is common to a large subset of insertion events in both mouse and human cells and is coincident with the presence of high levels of heterochromatic H3 lysine nine trimethylation (H3K9me3). Hi-C and microscopy indicate that the heterochromatinised fission yeast DNA is organised into smaller chromatin loops than flanking euchromatic mouse chromatin. We conclude that heterochromatin alters chromatin loop size, thus contributing to the distinct appearance of heterochromatin on mitotic chromosomes.","doi":"10.7554/eLife.57212","authors":"Fitz-James MH, Tong P, Pidoux AL, Ozadam H, Yang L, White SA, Dekker J, Allshire RC","authors_abbrev":"Fitz-James MH et al.","pubmed_publication_date":"11 Sep 2020","pubmed_entrez_date":"2020-09-11","publication_year":"2020","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2020-09-13 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15184402","title":"Regulation of a formin complex by the microtubule plus end protein tea1p.","citation":"J Cell Biol 2004 Jun 07;165(5):697-707","abstract":"The plus ends of microtubules have been speculated to regulate the actin cytoskeleton for the proper positioning of sites of cell polarization and cytokinesis. In the fission yeast Schizosaccharomyces pombe, interphase microtubules and the kelch repeat protein tea1p regulate polarized cell growth. Here, we show that tea1p is directly deposited at cell tips by microtubule plus ends. Tea1p associates in large \"polarisome\" complexes with bud6p and for3p, a formin that assembles actin cables. Tea1p also interacts in a separate complex with the CLIP-170 protein tip1p, a microtubule plus end-binding protein that anchors tea1p to the microtubule plus end. Localization experiments suggest that tea1p and bud6p regulate formin distribution and actin cable assembly. Although single mutants still polarize, for3Deltabud6Deltatea1Delta triple-mutant cells lack polarity, indicating that these proteins contribute overlapping functions in cell polarization. Thus, these experiments begin to elucidate how microtubules contribute to the proper spatial regulation of actin assembly and polarized cell growth.","authors":"Feierbach B, Verde F, Chang F","authors_abbrev":"Feierbach B et al.","pubmed_publication_date":"07 Jun 2004","pubmed_entrez_date":"2004-06-09","publication_year":"2004","canto_session_key":"ca29b665ec8b2f94","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-07-14 08:04:51","canto_approved_date":"2025-12-28 23:18:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-07-14 08:04:44","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":28,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15A10.16","SPCC1223.06","SPCC895.05","SPAC3C7.12"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2022-07-14"},{"uniquename":"PMID:16324155","title":"Rho1-GEFs Rgf1 and Rgf2 are involved in formation of cell wall and septum, while Rgf3 is involved in cytokinesis in fission yeast.","citation":"Genes Cells 2005 Dec;10(12):1189-202","abstract":"The Rho GTPase acts as a binary molecular switch by converting between a GDP-bound inactive and a GTP-bound active conformational state. The guanine nucleotide exchange factors (GEFs) are critical activators of Rho. Rho1 has been shown to regulate actin cytoskeleton and cell wall synthesis in the fission yeast Schizosaccharomyces pombe. Here we studied function of fission yeast RhoGEFs, Rgf1, Rgf2, and Rgf3. It was shown that these proteins have similar molecular structures, and function as GEFs for Rho1. Disruption of either rgf1 or rgf2 did not show a serious effect on the cell. On the other hand, disruption of rgf3 caused severe defects in contractile ring formation, F-actin patch localization, and septation during cytokinesis. Rgf1 and Rgf2 were localized to the cell ends during interphase and the septum. Rgf3 formed a ring at the division site, which was located outside the contractile ring and inside the septum where Rho1 was accumulated. In summary, Rgf1 and Rgf2 show functional redundancy, and roles of these RhoGEFs are likely to be different from that of Rgf3. Rho1 is likely to be activated by Rgf3 at the division site, and involved in contractile ring formation and/or maintenance and septation.","authors":"Mutoh T, Nakano K, Mabuchi I","authors_abbrev":"Mutoh T et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-12-06","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3F6.05","SPAC1006.06","SPBC19G7.05c","SPAC1F7.04","SPCC645.07","SPCC645.06c"],"gene_count":6,"ltp_gene_count":5},{"uniquename":"PMID:2249251","title":"The recombinational hot spot mutation ade6-M26 of Schizosaccharomyces pombe stimulates recombination at sites in a nearby interval.","citation":"Curr Genet 1990 Oct;18(3):193-7","abstract":"With the help of in vitro constructed intragenic double mutants, we investigated the influence of the recombinational hot spot mutation ade6-M26 on meiotic recombination between two additional ade6 mutations proximal to it. Recombination was stimulated four-fold when M26 was present in a heterozygous condition and ten-fold when homozygous. M26 itself remained unaffected in a substantial number of these events. This indicates that the stimulation can not only be due to a preferred conversion of M26 to wild-type with co-conversion of the second mutation in cis. A model is proposed in which M26 acts as an \"entry site\" for recombinational enzymes.","authors":"Grimm C, Munz P, Kohli J","authors_abbrev":"Grimm C et al.","pubmed_publication_date":"Oct 1990","pubmed_entrez_date":"1990-10-01","publication_year":"1990","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16624901","title":"A defect in protein farnesylation suppresses a loss of Schizosaccharomyces pombe tsc2+, a homolog of the human gene predisposing to tuberous sclerosis complex.","citation":"Genetics 2006 Jun;173(2):569-78","abstract":"Mutations in the human Tsc1 and Tsc2 genes predispose to tuberous sclerosis complex (TSC), a disorder characterized by the wide spread of benign tumors. Tsc1 and Tsc2 proteins form a complex and serve as a GTPase-activating protein (GAP) for Rheb, a GTPase regulating a downstream kinase, mTOR. The genome of Schizosaccharomyces pombe contains tsc1(+) and tsc2(+), homologs of human Tsc1 and Tsc2, respectively. In this study we analyzed the gene expression profile on a genomewide scale and found that deletion of either tsc1(+) or tsc2(+) affects gene induction upon nitrogen starvation. Three hours after nitrogen depletion genes encoding permeases and genes required for meiosis are less induced. Under the same condition, retrotransposons, G1-cyclin (pas1(+)), and inv1(+) are more induced. We also demonstrate that a mutation (cpp1-1) in a gene encoding a beta-subunit of a farnesyltransferase can suppress most of the phenotypes associated with deletion of tsc1(+) or tsc2(+). When a mutant of rhb1(+) (homolog of human Rheb), which bypasses the requirement of protein farnesylation, was expressed, the cpp1-1 mutation could no longer suppress, indicating that deficient farnesylation of Rhb1 contributes to the suppression. On the basis of these results, we discuss TSC pathology and possible improvement in chemotherapy for TSC.","authors":"Nakase Y, Fukuda K, Chikashige Y, Tsutsumi C, Morita D, Kawamoto S, Ohnuki M, Hiraoka Y, Matsumoto T","authors_abbrev":"Nakase Y et al.","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-04-21","publication_year":"2006","canto_session_key":"d0003ff073da52d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-03-06 15:30:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-03-06 15:30:17","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.07c","SPBC428.16c","SPCC191.11","SPAC22F3.13","SPAC27D7.03c","SPAPB1A10.04c","SPAC630.13c","SPAC17G6.04c","SPBC32C12.02","SPBC13G1.11","SPBC12C2.13c","SPBC36.06c"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2014-03-06"},{"uniquename":"PMID:11193425","title":"Identification and characterization of a novel gene, hos2+, the function of which is necessary for growth under high osmotic stress in fission yeast.","citation":"Biosci Biotechnol Biochem 2000 Nov;64(11):2493-6","abstract":"hos2 mutants of the fission yeast Schizosaccharomyces pombe showed the phenotype of high osmolarity sensitivity for growth. An S. pombe strain carrying the hos2-M10 allele cannot form colonies on agar plates containing 2 M glucose, but the parental strain can do so very well, as demonstrated previously. In this study, the hos2+ gene was identified as one that encodes a small protein of 94 amino acids, which shows no sequence similarity to any other proteins in the current databases. The hos2-M10 mutation resulted in Gln-62 to TAG-termination codon. A Hos2-defective (hos2delta) strain, which we then constructed, showed the phenotype of high osmolarity sensitivity, as in the case of the original hos2-M10 mutant. For this hos2delta mutant, three multicopy suppressor genes were isolated and one of which was identified as the pgk1+ gene, encoding a phosphoglycerate kinase.","authors":"Nakamichi N, Yamamoto E, Yamada H, Aiba H, Mizuno T","authors_abbrev":"Nakamichi N et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2001-02-24","publication_year":"2000","canto_session_key":"7f0df2e71ffbf638","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-26 15:30:02","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-26 15:29:55","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.07c","SPAC9.11","SPBC14F5.04c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-08-26"},{"uniquename":"PMID:30217891","title":"Physical basis for long-distance communication along meiotic chromosomes.","citation":"Proc Natl Acad Sci U S A 2018 Oct 02;115(40):E9333-E9342","abstract":"Viable gamete formation requires segregation of homologous chromosomes connected, in most species, by cross-overs. DNA double-strand break (DSB) formation and the resulting cross-overs are regulated at multiple levels to prevent overabundance along chromosomes. Meiotic cells coordinate these events between distant sites, but the physical basis of long-distance chromosomal communication has been unknown. We show that DSB hotspots up to ∼200 kb (∼35 cM) apart form clusters via hotspot-binding proteins Rec25 and Rec27 in fission yeast. Clustering coincides with hotspot competition and interference over similar distances. Without Tel1 (an ATM tumor-suppressor homolog), DSB and crossover interference become negative, reflecting coordinated action along a chromosome. These results indicate that DSB hotspots within a limited chromosomal region and bound by their protein determinants form a clustered structure that, via Tel1, allows only one DSB per region. Such a \"roulette\" process within clusters explains the observed pattern of crossover interference in fission yeast. Key structural and regulatory components of clusters are phylogenetically conserved, suggesting conservation of this vital regulation. Based on these observations, we propose a model and discuss variations in which clustering and competition between DSB sites leads to DSB interference and in turn produces crossover interference.","doi":"10.1073/pnas.1801920115","authors":"Fowler KR, Hyppa RW, Cromie GA, Smith GR","authors_abbrev":"Fowler KR et al.","pubmed_publication_date":"02 Oct 2018","pubmed_entrez_date":"2018-09-16","publication_year":"2018","canto_session_key":"1d2eeda40cb4401e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Gerald Smith","canto_first_approved_date":"2020-02-12 14:59:33","canto_approved_date":"2025-09-04 10:05:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-17 10:10:10","canto_added_date":"2018-09-17 00:15:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Gerald Smith","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17A5.18c","SPAC25G10.04c","SPBC29A10.14","SPBC19C2.05","SPBC577.05c","SPCC23B6.03c","SPAC17A5.11"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2020-02-12"},{"uniquename":"PMID:22500108","title":"Interaction between pheromone and its receptor of the fission yeast Schizosaccharomyces pombe examined by a force spectroscopy study.","citation":"J Biomed Biotechnol 2012;2012:804793","abstract":"Interaction between P-factor, a peptide pheromone composed of 23 amino acid residues, and its pheromone receptor, Mam2, on the cell surface of the fission yeast Schizosaccharomyces pombe was examined by an atomic force microscope (AFM). An AFM tip was modified with P-factor derivatives to perform force curve measurements. The specific interaction force between P-factor and Mam2 was calculated to be around 120 pN at a probe speed of 1.74 μm/s. When the AFM tip was modified with truncated P-factor derivative lacking C-terminal Leu, the specific interaction between the tip and the cell surface was not observed. These results were also confirmed with an assay system using a green fluorescent protein (GFP) reporter gene to monitor the activation level of signal transduction following the interaction of Mam2 with P-factor.","doi":"10.1155/2012/804793","authors":"Sasuga S, Abe R, Nikaido O, Kiyosaki S, Sekiguchi H, Ikai A, Osada T","authors_abbrev":"Sasuga S et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-04-14","publication_year":"2012","canto_session_key":"4acb2f022c79e2b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-11 21:08:34","canto_approved_date":"2025-12-29 06:38:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-04 15:06:41","canto_added_date":"2012-04-27 14:24:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.06","SPAC11H11.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-11"},{"uniquename":"PMID:2358444","title":"nmt1 of fission yeast. A highly transcribed gene completely repressed by thiamine.","citation":"J Biol Chem 1990 Jul 05;265(19):10857-64","abstract":"The first fully repressible gene in fission yeast is described. In minimal medium it is highly transcribed producing a mRNA which is 50-100 times more abundant than the cyc1 mRNA. By contrast, in minimal medium supplemented with thiamine at a concentration of 0.5 microM or greater the transcript is undetectable. The gene has been called nmt1 (for no message in thiamine). The 5' and 3' ends of the transcript have been mapped and indicate an unspliced mRNA of 1.3 kilobases with no evidence of heterogeneity at either end. The single major open reading frame encodes a protein of 39 kDa. The gene product is most likely involved in thiamine biosynthesis and consistent with this is the observation that the nmt1::ura4 disruption strain is a thiamine auxotroph. The kinetics of transcriptional repression and induction have been studied. Addition of thiamine to log phase cells growing minimal medium results in complete disappearance of the nmt1 message within 3 h. Removal of thiamine from the medium produces the first detectable message after 10 h and maximal steady-state levels after 16 h. Nuclear \"run on\" experiments demonstrate that control is exerted at the level of transcription initiation. The nmt1 promotor has been subcloned, and thiamine-mediated transcriptional control has been transferred to the bacterial reporter gene chloramphenicol acetyltransferase.","authors":"Maundrell K","authors_abbrev":"Maundrell K","pubmed_publication_date":"05 Jul 1990","pubmed_entrez_date":"1990-07-05","publication_year":"1990","canto_session_key":"1bd720a71d7eff96","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-09-17 13:49:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-05-26 08:58:39","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-26"},{"uniquename":"PMID:42247019","title":"Glucose metabolism and transcriptional responses to vitamin B6 in tau-expressing fission yeast cells.","citation":"Mol Biol Rep 2026 Jun 05;53(1)","abstract":"Tau pathology is increasingly recognized as a driver of metabolic dysfunction in neurodegenerative diseases, extending beyond protein aggregation to include impairments in glucose metabolism and redox homeostasis. However, how metabolic cofactors affect tau-associated metabolic stress remains incompletely understood.\nIn this study, we employed a fission yeast (Schizosaccharomyces pombe) model expressing human tau to investigate the effects of vitamin B6 on glucose metabolism and cellular redox balance under glucose-limited conditions in tau-expressing cells. Cells were treated with vitamin B6 and analyzed for tau expression and phosphorylation, glucose consumption, NAD⁺/NADH ratio, and the expression of selected glucose metabolism-related genes under glucose starvation conditions. Vitamin B6 treatment was associated with a reduction in tau protein expression and phosphorylation at specific residues (S262, S396, S404). In addition, vitamin B6 affected glucose metabolism-related gene expression and was accompanied by modest changes in glucose consumption and redox balance. These effects were observed in both control and tau-expressing cells, although the patterns of response differed between the two conditions. While vitamin B6 generally enhanced the expression of glucose utilization-related genes in control cells, its effects in tau-expressing cells were more variable, indicating altered metabolic regulation under tau-associated stress.\nThese findings suggest that vitamin B6 may contribute to cellular metabolic adaptation under tau-induced stress. This study demonstrates the usefulness of fission yeast as a tractable model for examining metabolic aspects of tau pathology and provides insight into how metabolic cofactors influence tau-associated cellular stress.","doi":"10.1007/s11033-026-12084-3","authors":"Yilmazer M, Karaer Uzuner S, Palabiyik B","authors_abbrev":"Yilmazer M et al.","pubmed_publication_date":"05 Jun 2026","pubmed_entrez_date":"2026-06-05","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-05 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC14SR","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16166653","title":"The mating type switch-activating protein Sap1 Is required for replication fork arrest at the rRNA genes of fission yeast.","citation":"Mol Cell Biol 2005 Oct;25(19):8755-61","abstract":"Schizosaccharomyces pombe rRNA genes contain three replication fork barriers (RFB1-3) located in the nontranscribed spacer. RFB2 and RFB3 require binding of the transcription terminator factor Reb1p to two identical recognition sequences that colocalize with these barriers. RFB1, which is the strongest of the three barriers, functions in a Reb1p-independent manner, and cognate DNA-binding proteins for this barrier have not been identified yet. Here we functionally define RFB1 within a 78-bp sequence located near the 3' end of the rRNA coding region. A protein that specifically binds to this sequence was purified by affinity chromatography and identified as Sap1p by mass spectrometry. Specific binding to RFB1 was confirmed by using Sap1p expressed in Escherichia coli. Sap1p is essential for viability and is required for efficient mating-type switching. Mutations in RFB1 that precluded formation of the Sap1p-RFB1 complex systematically abolished replication barrier function, indicating that Sap1p is required for replication fork blockage at RFB1.","authors":"Mejía-Ramírez E, Sánchez-Gorostiaga A, Krimer DB, Schvartzman JB, Hernández P","authors_abbrev":"Mejía-Ramírez E et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-09-17","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1672.02c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:22761595","title":"The Rad4(TopBP1) ATR-activation domain functions in G1/S phase in a chromatin-dependent manner.","citation":"PLoS Genet 2012 Jun;8(6):e1002801","abstract":"DNA damage checkpoint activation can be subdivided in two steps: initial activation and signal amplification. The events distinguishing these two phases and their genetic determinants remain obscure. TopBP1, a mediator protein containing multiple BRCT domains, binds to and activates the ATR/ATRIP complex through its ATR-Activation Domain (AAD). We show that Schizosaccharomyces pombe Rad4(TopBP1) AAD-defective strains are DNA damage sensitive during G1/S-phase, but not during G2. Using lacO-LacI tethering, we developed a DNA damage-independent assay for checkpoint activation that is Rad4(TopBP1) AAD-dependent. In this assay, checkpoint activation requires histone H2A phosphorylation, the interaction between TopBP1 and the 9-1-1 complex, and is mediated by the phospho-binding activity of Crb2(53BP1). Consistent with a model where Rad4(TopBP1) AAD-dependent checkpoint activation is ssDNA/RPA-independent and functions to amplify otherwise weak checkpoint signals, we demonstrate that the Rad4(TopBP1) AAD is important for Chk1 phosphorylation when resection is limited in G2 by ablation of the resecting nuclease, Exo1. We also show that the Rad4(TopBP1) AAD acts additively with a Rad9 AAD in G1/S phase but not G2. We propose that AAD-dependent Rad3(ATR) checkpoint amplification is particularly important when DNA resection is limiting. In S. pombe, this manifests in G1/S phase and relies on protein-chromatin interactions.","doi":"10.1371/journal.pgen.1002801","authors":"Lin SJ, Wardlaw CP, Morishita T, Miyabe I, Chahwan C, Caspari T, Schmidt U, Carr AM, Garcia V","authors_abbrev":"Lin SJ et al.","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2012-07-05","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC582.03","SPAC23C4.18c","SPCC23B6.03c","SPBC29A10.05","SPBC216.05","SPAC664.07c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:10652237","title":"Identification and characterization of the rhp23(+) DNA repair gene in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2000 Feb 05;268(1):210-5","abstract":"We have identified rhp23(+), the ortholog of the Saccharomyces cerevisiae RAD23 and human HHR23A and HHR23B genes, in Schizosaccharomyces pombe and examined its role in cell survival and DNA repair. In S. pombe two repair mechanisms are operative on UV-induced photoproducts, i.e., UV damage repair (UVDR) and nucleotide excision repair (NER). Here we show that Rhp23 is solely involved in NER and study its role in DNA repair in the absence of the UVDR pathway. S. pombe rhp23-deficient cells are sensitive toward UV irradiation, although not as sensitive as complete NER-deficient cells. Furthermore we demonstrate that the residual survival observed in rhp23-deficient cells is NER dependent. Despite this NER-dependent survival, uvde rhp23 double mutants are unable to repair cyclobutane pyrimidine dimers. The inability to remove these photolesions from both DNA strands clearly demonstrates that rhp23(+) is involved in transcription coupled repair as well as global genome repair.","authors":"Lombaerts M, Goeloe JI, den Dulk H, Brandsma JA, Brouwer J","authors_abbrev":"Lombaerts M et al.","pubmed_publication_date":"05 Feb 2000","pubmed_entrez_date":"2000-02-01","publication_year":"2000","canto_session_key":"b0cab57768ea770a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-10-31 15:49:13","canto_approved_date":"2019-10-31 15:49:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-10-31 15:49:04","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.12","SPBC3E7.08c","SPBC19C7.09c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-10-31"},{"uniquename":"PMID:33313420","title":" SpEDIT : A fast and efficient CRISPR/Cas9 method for fission yeast.","citation":"Wellcome Open Res 2020;5:274","abstract":"The CRISPR/Cas9 system allows scarless, marker-free genome editing. Current CRISPR/Cas9 systems for the fission yeast   Schizosaccharomyces pombe  rely on tedious and time-consuming cloning procedures to introduce a specific sgRNA target sequence into a Cas9-expressing plasmid. In addition, Cas9 endonuclease has been reported to be toxic to fission yeast when constitutively overexpressed from the strong   adh1  promoter. To overcome these problems we have developed an improved system,   SpEDIT , that uses a synthesised Cas9 sequence codon-optimised for   S. pombe  expressed from the medium strength   adh15  promoter. The   SpEDIT  system exhibits a flexible modular design where the sgRNA is fused to the 3' end of the self-cleaving hepatitis delta virus (HDV) ribozyme, allowing expression of the sgRNA cassette to be driven by RNA polymerase III from a tRNA gene sequence. Lastly, the inclusion of sites for the   Bsa I type IIS restriction enzyme flanking a GFP placeholder enables one-step Golden Gate mediated replacement of GFP with synthesized sgRNAs for expression. The   SpEDIT  system allowed a 100% mutagenesis efficiency to be achieved when generating targeted point mutants in the   ade6  +    or   ura4   +  genes by transformation of cells from asynchronous cultures.   SpEDIT  also permitted insertion, tagging and deletion events to be obtained with minimal effort. Simultaneous editing of two independent non-homologous loci was also readily achieved. Importantly the   SpEDIT  system displayed reduced toxicity compared to currently available   S. pombe  editing systems. Thus,   SpEDIT  provides an effective and user-friendly CRISPR/Cas9 procedure that significantly improves the genome editing toolbox for fission yeast.","doi":"10.12688/wellcomeopenres.16405.1","authors":"Torres-Garcia S, Di Pompeo L, Eivers L, Gaborieau B, White SA, Pidoux AL, Kanigowska P, Yaseen I, Cai Y, Allshire RC","authors_abbrev":"Torres-Garcia S et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-12-14","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-12-16 01:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SP40378","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33105893","title":"Cadmium-Induced Cell Homeostasis Impairment is Suppressed by the Tor1 Deficiency in Fission Yeast.","citation":"Int J Mol Sci 2020 Oct 22;21(21)","abstract":"Cadmium has no known physiological function in the body; however, its adverse effects are associated with cancer and many types of organ system damage. Although much has been shown about Cd toxicity, the underlying mechanisms of its responses to the organism remain unclear. In this study, the role of Tor1, a catalytic subunit of the target of rapamycin complex 2 (TORC2), in Cd-mediated effects on cell proliferation, the antioxidant system, morphology, and ionome balance was investigated in the eukaryotic model organism  Schizosaccharomyces pombe . Surprisingly, spectrophotometric and biochemical analyses revealed that the growth rate conditions and antioxidant defense mechanisms are considerably better in cells lacking the Tor1 signaling. The malondialdehyde (MDA) content of Tor1-deficient cells upon Cd treatment represents approximately half of the wild-type content. The microscopic determination of the cell morphological parameters indicates the role for Tor1 in cell shape maintenance. The ion content, determined by inductively coupled plasma optical emission spectroscopy (ICP-OES), showed that the Cd uptake potency was markedly lower in Tor1-depleted compared to wild-type cells. Conclusively, we show that the cadmium-mediated cell impairments in the fission yeast significantly depend on the Tor1 signaling. Additionally, the data presented here suggest the yet-undefined role of Tor1 in the transport of ions.","doi":"10.3390/ijms21217847","authors":"Požgajová M, Navrátilová A, Šebová E, Kovár M, Kačániová M","authors_abbrev":"Požgajová M et al.","pubmed_publication_date":"22 Oct 2020","pubmed_entrez_date":"2020-10-27","publication_year":"2020","canto_session_key":"e44f7edc570d3fc5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-10-29 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC30D10.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:23311928","title":"The zinc finger protein Gsf1 regulates Gsf2-dependent flocculation in fission yeast.","citation":"FEMS Yeast Res 2013 May;13(3):259-66","abstract":"Fission yeast flocculates nonsexually by induction of the flocculin encoded by gsf2(+) which is controlled by the positive regulator Mbx2. Here, we report a novel gene designated gsf1(+) found to be a negative regulator of nonsexual flocculation. We identified gsf1(+) as a multicopy suppressor of a sam2 mutation, which caused growth sensitivity to Ca(2+) and also found a nonsense mutation in gsf1(+) in a previously isolated gsf1 mutant. The gsf1(+) gene encodes a 547-aa protein containing a Zn(2)-Cys(6) binuclear cluster-type zinc finger motif. The Gsf1 protein localized in the nucleus, consistent with a role as a transcription factor. Deletion of gsf1(+) resulted in nonsexual flocculation inducible by CaCl2 , which was suppressed by the addition of EDTA or galactose. Both gsf2(+) and mbx2(+) were highly expressed in the gsf1 mutant. gsf1∆ gsf2∆ and gsf1∆ mbx2∆ double mutants did not flocculate, suggesting that gsf1(+) is an upstream regulator. In addition, the gsf1 mutant was sensitive to CaCl2 , KCl, HU, and TBZ, consistent with the possibility that gsf1(+) plays a role in functions unrelated to flocculation. Taken together, these results suggest that nonsexual flocculation in fission yeast is negatively controlled by Gsf1, which controls expression of mbx2(+) and gsf2(+) .","doi":"10.1111/1567-1364.12029","authors":"Matsuzawa T, Kageyama Y, Ooishi K, Kawamukai M, Takegawa K","authors_abbrev":"Matsuzawa T et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-01-15","publication_year":"2013","canto_session_key":"cc42fec3996fecfa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_approved_date":"2014-06-04 07:20:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-28 14:17:03","canto_added_date":"2013-06-16 07:56:20","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPCC1742.01","SPBC15D4.02","SPBC19G7.06","SPBC317.01"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2014-04-28"},{"uniquename":"EMBL:AB084824","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.12"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26901872","title":"Crystal structure of eukaryotic translation initiation factor 2B.","citation":"Nature 2016 Mar 03;531(7592):122-5","abstract":"Eukaryotic cells restrict protein synthesis under various stress conditions, by inhibiting the eukaryotic translation initiation factor 2B (eIF2B). eIF2B is the guanine nucleotide exchange factor for eIF2, a heterotrimeric G protein consisting of α-, β- and γ-subunits. eIF2B exchanges GDP for GTP on the γ-subunit of eIF2 (eIF2γ), and is inhibited by stress-induced phosphorylation of eIF2α. eIF2B is a heterodecameric complex of two copies each of the α-, β-, γ-, δ- and ε-subunits; its α-, β- and δ-subunits constitute the regulatory subcomplex, while the γ- and ε-subunits form the catalytic subcomplex. The three-dimensional structure of the entire eIF2B complex has not been determined. Here we present the crystal structure of Schizosaccharomyces pombe eIF2B with an unprecedented subunit arrangement, in which the α2β2δ2 hexameric regulatory subcomplex binds two γε dimeric catalytic subcomplexes on its opposite sides. A structure-based in vitro analysis by a surface-scanning site-directed photo-cross-linking method identified the eIF2α-binding and eIF2γ-binding interfaces, located far apart on the regulatory and catalytic subcomplexes, respectively. The eIF2γ-binding interface is located close to the conserved 'NF motif', which is important for nucleotide exchange. A structural model was constructed for the complex of eIF2B with phosphorylated eIF2α, which binds to eIF2B more strongly than the unphosphorylated form. These results indicate that the eIF2α phosphorylation generates the 'nonproductive' eIF2-eIF2B complex, which prevents nucleotide exchange on eIF2γ, and thus provide a structural framework for the eIF2B-mediated mechanism of stress-induced translational control.","doi":"10.1038/nature16991","authors":"Kashiwagi K, Takahashi M, Nishimoto M, Hiyama TB, Higo T, Umehara T, Sakamoto K, Ito T, Yokoyama S","authors_abbrev":"Kashiwagi K et al.","pubmed_publication_date":"03 Mar 2016","pubmed_entrez_date":"2016-02-23","publication_year":"2016","canto_session_key":"9cfe0e98ab60ebf4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-05-10 11:56:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-05-10 11:55:51","canto_added_date":"2016-02-25 01:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4D7.09","SPAC343.14c","SPAC21E11.06","SPAC8C9.15c","SPAC3G9.09c","SPCC11E10.07c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-05-10","pdb_entries":[{"pdb_id":"5b04","gene_chains":[{"gene_uniquename":"SPAC8C9.15c","chain":"I/J","position":"1-678"},{"gene_uniquename":"SPAC4D7.09","chain":"E/F","position":"1-458"},{"gene_uniquename":"SPAC21E11.06","chain":"G/H","position":"1-467"},{"gene_uniquename":"SPCC11E10.07c","chain":"A/B","position":"1-341"},{"gene_uniquename":"SPAC343.14c","chain":"C/D","position":"1-393"}],"title":"Crystal structure of the eukaryotic translation initiation factor 2B from Schizosaccharomyces pombe","entry_authors":"Kashiwagi K,Ito T,Yokoyama S","entry_authors_abbrev":"Kashiwagi K et al.","reference_uniquename":"PMID:26901872","experimental_method":"X-ray","resolution":"2.994"}]},{"uniquename":"PMID:141450","title":"Efflux of potassium induced by dio-9, a plasma membrane ATPase inhibitor in the yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1977 Jul 10;252(13):4577-83","abstract":"","authors":"Foury F, Boutry M, Goffeau A","authors_abbrev":"Foury F et al.","pubmed_publication_date":"10 Jul 1977","pubmed_entrez_date":"1977-07-10","publication_year":"1977","canto_session_key":"e56246e0cad18d3b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-23 17:56:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-23 17:56:00","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-23"},{"uniquename":"PMID:17690116","title":"Cdc18/CDC6 activates the Rad3-dependent checkpoint in the fission yeast.","citation":"Nucleic Acids Res 2007;35(16):5323-37","abstract":"A screen for genes that can ectopically activate a Rad3-dependent checkpoint block over mitosis in fission yeast has identified the DNA replication initiation factor cdc18 (known as CDC6 in other organisms). Either a stabilized form of Cdc18, the Cdc18-T6A phosphorylation mutant, or overexpression of wild type Cdc18, activate the Rad3-dependent S-M checkpoint in the apparent absence of detectable replication structures and gross DNA damage. This cell cycle block relies on the Rad checkpoint pathway and requires Chk1 phosphorylation and activation. Unexpectedly, Cdc18-T6A induces changes in the mobility of Chromosome III, affecting the size of a restriction fragment containing rDNA repeats and producing aberrant nucleolar structures. Recombination events within the rDNA appear to contribute at least in part to the cell cycle delay. We propose that an elevated level of Cdc18 activates the Rad3-dependent checkpoint either directly or indirectly, and additionally causes expansion of the rDNA repeats on Chromosome III.","authors":"Fersht N, Hermand D, Hayles J, Nurse P","authors_abbrev":"Fersht N et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-08-11","publication_year":"2007","canto_session_key":"8ca59104c61e0b02","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2020-11-11 14:20:01","canto_approved_date":"2025-07-02 06:24:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-10-30 09:05:55","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":36,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.13","SPAC694.06c","SPCC18B5.11c","SPCC1259.13","SPAC30D11.10","SPBC216.05","SPBC342.05","SPBC14C8.07c","SPBC1198.11c","SPAC664.07c","SPAC24H6.05","SPAC9E9.08","SPAC20G4.04c","SPAC140.02","SPAC1952.07"],"gene_count":15,"ltp_gene_count":13,"approved_date":"2020-11-11"},{"uniquename":"PMID:28343969","title":"Pds5 Regulates Sister-Chromatid Cohesion and Chromosome Bi-orientation through a Conserved Protein Interaction Module.","citation":"Curr Biol 2017 Apr 03;27(7):1005-1012","abstract":"Sister-chromatid cohesion is established by the cohesin complex in S phase and persists until metaphase, when sister chromatids are captured by microtubules emanating from opposite poles [1]. The Aurora-B-containing chromosome passenger complex (CPC) plays a crucial role in achieving chromosome bi-orientation by correcting erroneous microtubule attachment [2]. The centromeric localization of the CPC relies largely on histone H3-T3 phosphorylation (H3-pT3), which is mediated by the mitotic histone kinase Haspin/Hrk1 [3-5]. Hrk1 localization to centromeres depends largely on the cohesin subunit Pds5 in fission yeast [5]; however, it is unknown how Pds5 regulates Hrk1 localization. Here we identify a conserved Hrk1-interacting motif (HIM) in Pds5 and a Pds5-interacting motif (PIM) in Hrk1 in fission yeast. Mutations in either motif result in the displacement of Hrk1 from centromeres. We also show that the mechanism of Pds5-dependent Hrk1 recruitment is conserved in human cells. Notably, the PIM in Haspin/Hrk1 is reminiscent of the YSR motif found in the mammalian cohesin destabilizer Wapl and stabilizer Sororin, both of which bind PDS5 [6-12]. Similarly, and through the same motifs, fission yeast Pds5 binds to Wpl1/Wapl and acetyltransferase Eso1/Eco1, in addition to Hrk1. Thus, we have identified a protein-protein interaction module in Pds5 that serves as a chromatin platform for regulating sister-chromatid cohesion and chromosome bi-orientation.","doi":"10.1016/j.cub.2017.02.066","authors":"Goto Y, Yamagishi Y, Shintomi-Kawamura M, Abe M, Tanno Y, Watanabe Y","authors_abbrev":"Goto Y et al.","pubmed_publication_date":"03 Apr 2017","pubmed_entrez_date":"2017-03-28","publication_year":"2017","canto_session_key":"7803457eba12e494","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2018-06-28 15:53:19","canto_approved_date":"2024-11-17 12:19:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-24 18:38:21","canto_added_date":"2017-03-29 00:15:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":43,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC320.13c","SPAC23C4.03","SPAC10F6.09c","SPBC16A3.11","SPCC962.02c","SPBC428.17c","SPAC110.02","SPBC1A4.03c"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2018-06-28"},{"uniquename":"PMID:17301288","title":"Shugoshin 2 regulates localization of the chromosomal passenger proteins in fission yeast mitosis.","citation":"Mol Biol Cell 2007 May;18(5):1657-69","abstract":"Fission yeast has two members of the Shugoshin family, Sgo1 and Sgo2. Although Sgo1 has clearly been established as a protector of centromere cohesion in meiosis I, the roles of Sgo2 remain elusive. Here we show that Sgo2 is required to ensure proper chromosome biorientation upon recovery from a prolonged spindle checkpoint arrest. Consistent with this, Sgo2 is essential for maintaining the Passenger proteins on centromeres upon checkpoint activation. Interestingly, lack of Sgo2 has a more penetrant effect on the localization of Survivin than on the two other Passenger proteins INCENP and Aurora B, and the Survivin-INCENP complex but not the INCENP-Aurora B complex is destabilized in the absence of Sgo2. Finally we show that the conserved C-terminus of Sgo2 is crucial to maintain Sgo2 and Passenger proteins localization on centromeres upon prolonged checkpoint activation. Taken together, our results demonstrate that Sgo2 is important for chromosome biorientation and that it controls docking of the Passenger proteins on chromosomes in early mitotic cells.","authors":"Vanoosthuyse V, Prykhozhij S, Hardwick KG","authors_abbrev":"Vanoosthuyse V et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-02-16","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.15","SPCC962.02c","SPCC320.13c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:3912263","title":"Transcription of the triose-phosphate-isomerase gene of Schizosaccharomyces pombe initiates from a start point different from that in Saccharomyces cerevisiae.","citation":"Gene 1985;40(1):125-30","abstract":"Gene tpi, encoding the glycolytic enzyme triose phosphate isomerase (TPI) from the fission yeast Schizosaccharomyces pombe was cloned by complementation of a Saccharomyces cerevisiae tpil mutant. Nucleotide sequence analysis of the cloned gene revealed a single open reading frame (ORF) encoding a protein 59% homologous to S. cerevisiae TPI. The gene has a very high codon usage bias. Messenger RNA synthesis initiates at two points located 38 and 44 nucleotides downstream from a TATA box promoter sequence. In S. cerevisiae, transcription of this S. pombe gene initiates about 26 nucleotides downstream from the S. pombe start points. This observation indicates that the two yeasts have diverged in the mechanism which determines the 5' end of the messenger RNA relative to the TATA box. It appears that in some respects the transcription initiation mechanism of S. pombe more closely resembles that of higher eukaryotes than does the S. cerevisiae mechanism.","authors":"Russell PR","authors_abbrev":"Russell PR","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_session_key":"4e90eb1e64def030","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-02-26 15:46:36","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-02-26 15:46:23","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.21"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-02-26"},{"uniquename":"PMID:34967063","title":"The search for Schizosaccharomyces fission yeasts in environmental metatranscriptomes.","citation":"Yeast 2022 Jan;39(1-2):83-94","abstract":"Fission yeast is an important model organism in evolutionary genetics and cell biology research. Nevertheless, most research is limited to a single laboratory strain and knowledge of its natural occurrence is limited, which reduces our understanding of its life history and hinders isolation of new strains from nature. Understanding the natural diversity of fission yeast can provide insight into its genetic and phenotypic diversity and the evolutionary processes that shaped these. Here, we aimed to identify candidate natural habitats of fission yeasts by searching through a large collection of publicly available environmental metatranscriptomic datasets. Using a custom pipeline, we processed over 13,000 NCBI SRA accessions, from a wide range of 34 different environmental categories. Overall, we found a very low abundance of putative yeast transcripts, with most fission yeast signatures coming from the categories of 'food' and 'terrestrial arthropods'. Additionally, a signal could be found in a variety of marine and fresh aquatic habitats. Our results do not provide a conclusive answer on the natural habitat of fission yeasts, but our analysis further narrows the range of locations where fission yeasts naturally occur.","doi":"10.1002/yea.3689","authors":"Shraim R, Nieuwenhuis BPS","authors_abbrev":"Shraim R et al.","pubmed_publication_date":"Jan 2022","pubmed_entrez_date":"2021-12-30","publication_year":"2022","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2022-01-01 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11178109","title":"Multiple redundant sequence elements within the fission yeast ura4 replication origin enhancer.","citation":"BMC Mol Biol 2001;2:1","abstract":"Some origins in eukaryotic chromosomes fire more frequently than others. In the fission yeast, Schizosaccharomyces pombe, the relative firing frequencies of the three origins clustered 4-8 kbp upstream of the ura4 gene are controlled by a replication enhancer - an element that stimulates nearby origins in a relatively position-and orientation-independent fashion. The important sequence motifs within this enhancer were not previously localized.\nSystematic deletion of consecutive segments of approximately 50, approximately 100 or approximately 150 bp within the enhancer and its adjacent core origin (ars3002) revealed that several of the approximately 50-bp stretches within the enhancer contribute to its function in partially redundant fashion. Other stretches within the enhancer are inhibitory. Some of the stretches within the enhancer proved to be redundant with sequences within core ars3002. Consequently the collection of sequences important for core origin function was found to depend on whether the core origin is assayed in the presence or absence of the enhancer. Some of the important sequences in the core origin and enhancer co-localize with short runs of adenines or thymines, which may serve as binding sites for the fission yeast Origin Recognition Complex (ORC). Others co-localize with matches to consensus sequences commonly found in fission yeast replication origins.\nThe enhancer within the ura4 origin cluster in fission yeast contains multiple sequence motifs. Many of these stimulate origin function in partially redundant fashion. Some of them resemble motifs also found in core origins. The next step is to identify the proteins that bind to these stimulatory sequences.","authors":"Kim SM, Zhang DY, Huberman JA","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2001-02-15","publication_year":"2001","canto_session_key":"1de45d9ac9391475","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 21:24:18","canto_approved_date":"2019-01-31 21:24:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 21:24:11","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:7804140","title":"Univalent-cation-elicited acidification by yeasts.","citation":"Biochem Mol Biol Int 1994 Aug;33(6):1145-9","abstract":"Addition of univalent cations to sugar-metabolizing Saccharomyces cerevisiae, Schizosaccharomyces pombe and Lodderomyces elongisporus brought about a powerful acidification of the external medium with rates up to nearly 20 nmol H+ per min per mg dry wt. in S. cerevisiae, over 15 nmol in S. pombe, and 4.7 nmol in L. elongisporus. These rates were as much as 20 times, 5.5 times and 10.3 times, respectively. higher than in the absence of K+. Use of galactose-induced cells, of H(+)-ATPase-deficient mutants and observations over the entire growth curve indicated that the K+ effect on H+ extrusion is not connected with the H(+)-ATPase function as such but rather depends on metabolic reactions producing ATP. The effect has apparently nothing to do with the electrical potential across the plasma membrane.","authors":"Kotyk A, Georghiou G","authors_abbrev":"Kotyk A et al.","pubmed_publication_date":"Aug 1994","pubmed_entrez_date":"1994-08-01","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17276348","title":"A helping hand for cytochrome p450 enzymes.","citation":"Cell Metab 2007 Feb;5(2):81-3","abstract":"In this issue of Cell Metabolism, Espenshade and colleagues (Hughes et al., 2007) show that the hemoprotein Dap1/PGRMC1 forms a stable complex with several members of the cytochrome P450 superfamily of enzymes and positively regulates their activities. This action indicates an important role for Dap1/PGRMC1 in P450-catalyzed reactions, some of which are involved in the metabolism of sterols and pharmaceutical compounds.","authors":"Debose-Boyd RA","authors_abbrev":"Debose-Boyd RA","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-02-06","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12181336","title":"Cytoplasmic localization of Wis1 MAPKK by nuclear export signal is important for nuclear targeting of Spc1/Sty1 MAPK in fission yeast.","citation":"Mol Biol Cell 2002 Aug;13(8):2651-63","abstract":"Mitogen-activated protein kinase (MAPK) cascade is a ubiquitous signaling module that transmits extracellular stimuli through the cytoplasm to the nucleus; in response to activating stimuli, MAPKs translocate into the nucleus. Mammalian MEK MAPK kinases (MAPKKs) have in their N termini an MAPK-docking site and a nuclear export signal (NES) sequence, which are known to play critical roles in maintaining ERK MAPKs in the cytoplasm of unstimulated cells. Herein, we show that the Wis1 MAPKK of the stress-activated Spc1 MAPK cascade in fission yeast also has a MAPK-docking site and an NES sequence in its N-terminal domain. Unexpectedly, an inactivating mutation to the NES of chromosomal wis1(+) does not affect the subcellular localization of Spc1 MAPK, whereas this NES mutation disturbs the cytoplasmic localization of Wis1. However, when Wis1 is targeted to the nucleus by fusing to a nuclear localization signal sequence, stress-induced nuclear translocation of Spc1 is abrogated, indicating that cytoplasmic Wis1 is required for nuclear transport of Spc1 upon stress. Moreover, we have observed that a fraction of Wis1 translocates into the nucleus in response to stress. These results suggest that cytoplasmic localization of Wis1 MAPKK by its NES is important for stress signaling to the nucleus.","authors":"Nguyen AN, Ikner AD, Shiozaki M, Warren SM, Shiozaki K","authors_abbrev":"Nguyen AN et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-08-16","publication_year":"2002","canto_session_key":"1b4431af072117e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-18 18:36:42","canto_approved_date":"2026-01-27 14:14:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-18 18:36:36","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.17","SPAC24B11.06c","SPBC215.05","SPBC409.07c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2020-11-18"},{"uniquename":"PMID:20623139","title":"Isolation of a fission yeast mutant that is sensitive to valproic acid and defective in the gene encoding Ric1, a putative component of Ypt/Rab-specific GEF for Ryh1 GTPase.","citation":"Mol Genet Genomics 2010 Sep;284(3):161-71","abstract":"Valproic acid (VPA) causes various therapeutic and biological effects, but the exact mechanisms underlying these effects, however, remain elusive. To gain insights into the molecular mechanisms of VPA action, we performed in fission yeast a genetic screen for mutants that show VPA hypersensitivity and have identified several membrane-trafficking mutants including vas1-1/vps45 and vas2-1/aps1. Here, we describe the isolation and characterization of vas3-1/ric1-v3, a mutant allele of the ric1 (+) gene encoding a fission yeast homolog of the budding yeast Ric1p, a component of Ypt/Rab-specific guanyl-nucleotide exchange factor (GEF). The Rab GTPase Ryh1 knockout (Deltaryh1) cells and Deltaric1 cells exhibited similar phenotypes. The double knockout Deltaric1Deltaryh1 cells did not display synthetic growth defects. These results are consistent with the notion that Ric1 may be a component of the GEF complex for Ryh1. Overexpression of wild-type Ryh1 and the constitutively active Ryh1Q70L only partially suppressed the phenotypes of ric1-v3 and Deltaric1 cells, and they failed to localize to the Golgi/endosomes in ric1-v3 and Deltaric1 cells. Furthermore, we isolated vps15 (+) gene, encoding a serine/threonine protein kinase, as a dosage-dependent suppressor of the temperature-sensitive phenotype of ric1-v3 mutant, but not that of Deltaric1 cells. Our results showed that the ric1-v3 mutant allele has some residual functional activity and suggest that Vps15 plays a role in the regulation of Ric1 function. In conclusion, Ric1 is a putative component of GEF for Ryh1 and might be regulated by Vps15. Further studies are needed to reveal the mechanism underlying the regulation.","doi":"10.1007/s00438-010-0550-7","authors":"Ma Y, Sugiura R, Zhang L, Zhou X, Takeuchi M, He Y, Kuno T","authors_abbrev":"Ma Y et al.","pubmed_publication_date":"Sep 2010","pubmed_entrez_date":"2010-07-13","publication_year":"2010","canto_session_key":"e9611fbd9aa9473a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-06 17:02:01","canto_approved_date":"2020-07-31 15:47:18","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-02-24 20:59:27","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1851.04c","SPAC6G9.11","SPAC4C5.02c","SPBC119.07","SPBC13G1.11"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-01-06"},{"uniquename":"PMID:15194812","title":"A novel intermediate in initiation complex assembly for fission yeast DNA replication.","citation":"Mol Biol Cell 2004 Aug;15(8):3740-50","abstract":"Assembly of initiation factors on individual replication origins at onset of S phase is crucial for regulation of replication timing and repression of initiation by S-phase checkpoint control. We dissected the process of preinitiation complex formation using a point mutation in fission yeast nda4-108/mcm5 that shows tight genetic interactions with sna41(+)/cdc45(+). The mutation does not affect loading of MCM complex onto origins, but impairs Cdc45-loading, presumably because of a defect in interaction of MCM with Cdc45. In the mcm5 mutant, however, Sld3, which is required for Cdc45-loading, proficiently associates with origins. Origin-association of Sld3 without Cdc45 is also observed in the sna41/cdc45 mutant. These results suggest that Sld3-loading is independent of Cdc45-loading, which is different from those observed in budding yeast. Interestingly, returning the arrested mcm5 cells to the permissive temperature results in immediate loading of Cdc45 to the origin and resumption of DNA replication. These results suggest that the complex containing MCM and Sld3 is an intermediate for initiation of DNA replication in fission yeast.","authors":"Yamada Y, Nakagawa T, Masukata H","authors_abbrev":"Yamada Y et al.","pubmed_publication_date":"Aug 2004","pubmed_entrez_date":"2004-06-15","publication_year":"2004","canto_session_key":"6ba8570e85c749bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-12-22 11:48:33","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-09-19 12:30:23","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.06","SPAPB2B4.03","SPBC29A10.15","SPBC32F12.09","SPBC25D12.03c","SPBC211.04c","SPAC1B2.05","SPBC4.04c","SPAC17D4.02"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2014-09-19"},{"uniquename":"EMBL:AU008545","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28193844","title":"Heme Assimilation in  Schizosaccharomyces pombe  Requires Cell-surface-anchored Protein Shu1 and Vacuolar Transporter Abc3.","citation":"J Biol Chem 2017 Mar 24;292(12):4898-4912","abstract":"The  Schizosaccharomyces pombe shu1  +  gene encodes a cell-surface protein required for assimilation of exogenous heme. In this study, shaving experiments showed that Shu1 is released from membrane preparations when spheroplast lysates are incubated with phosphoinositide-specific phospholipase C (PI-PLC). Shu1 cleavability by PI-PLC and its predicted hydropathy profile strongly suggested that Shu1 is a glycosylphosphatidylinositol-anchored protein. When heme biosynthesis is selectively blocked in  hem1 Δ mutant cells, the heme analog zinc mesoporphyrin IX (ZnMP) first accumulates into vacuoles and then subsequently, within the cytoplasm in a rapid and Shu1-dependent manner. An HA 4 -tagged  shu1  +  allele that retained wild-type function localizes to the cell surface in response to low hemin concentrations, but under high hemin concentrations, Shu1-HA 4  re-localizes to the vacuolar membrane. Inactivation of  abc3  + , encoding a vacuolar membrane transporter, results in  hem1 Δ  abc3 Δ mutant cells being unable to grow in the presence of hemin as the sole iron source. In  hem1 Δ  abc3 Δ cells, ZnMP accumulates primarily in vacuoles and does not sequentially accumulate in the cytosol. Consistent with a role for Abc3 as vacuolar hemin exporter, results with hemin-agarose pulldown assays showed that Abc3 binds to hemin. In contrast, an Abc3 mutant in which an inverted Cys-Pro motif had been replaced with Ala residues fails to bind hemin with high affinity. Taken together, these results show that Shu1 undergoes rapid hemin-induced internalization from the cell surface to the vacuolar membrane and that the transporter Abc3 participates in the mobilization of stored heme from the vacuole to the cytosol.","doi":"10.1074/jbc.M117.776807","authors":"Mourer T, Normant V, Labbé S","authors_abbrev":"Mourer T et al.","pubmed_publication_date":"24 Mar 2017","pubmed_entrez_date":"2017-02-15","publication_year":"2017","canto_session_key":"104f1a2efcecbd00","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-13 07:12:36","canto_approved_date":"2022-08-30 07:03:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-13 07:12:30","canto_added_date":"2017-02-16 01:15:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC359.05","SPAC2F3.09","SPAC1F8.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-06-13"},{"uniquename":"PMID:20614012","title":"HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome.","citation":"PLoS One 2010 Jun 29;5(6):e11371","abstract":"HIV-1 Vpr is a virion-associated protein. Its activities link to viral pathogenesis and disease progression of HIV-infected patients. In vitro, Vpr moderately activates HIV-1 replication in proliferating T cells, but it is required for efficient viral infection and replication in vivo in non-dividing cells such as macrophages. How exactly Vpr contributes to viral replication remains elusive. We show here that Vpr stimulates HIV-1 replication at least in part through its interaction with hHR23A, a protein that binds to 19S subunit of the 26S proteasome and shuttles ubiquitinated proteins to the proteasome for degradation. The Vpr-proteasome interaction was initially discovered in fission yeast, where Vpr was shown to associate with Mts4 and Mts2, two 19S-associated proteins. The interaction of Vpr with the 19S subunit of the proteasome was further confirmed in mammalian cells where Vpr associates with the mammalian orthologues of fission yeast Mts4 and S5a. Consistently, depletion of hHR23A interrupts interaction of Vpr with proteasome in mammalian cells. Furthermore, Vpr promotes hHR23A-mediated protein-ubiquitination, and down-regulation of hHR23A using RNAi significantly reduced viral replication in non-proliferating MAGI-CCR5 cells and primary macrophages. These findings suggest that Vpr-proteasome interaction might counteract certain host restriction factor(s) to stimulate viral replication in non-dividing cells.","doi":"10.1371/journal.pone.0011371","authors":"Li G, Elder RT, Dubrovsky L, Liang D, Pushkarsky T, Chiu K, Fan T, Sire J, Bukrinsky M, Zhao RY","authors_abbrev":"Li G et al.","pubmed_publication_date":"29 Jun 2010","pubmed_entrez_date":"2010-07-09","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2D10.12","SPBP19A11.03c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:10954073","title":"The Holliday junction resolvase SpCCE1 prevents mitochondrial DNA aggregation in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 2000 Jul;263(6):889-97","abstract":"SpCCE1 (YDC2) from Schizosaccharomyces pombe is a DNA structure-specific endonuclease that resolves Holliday junctions in vitro. To investigate the in vivo function of SpCCE1 we made an Spcce1:ura4+ insertion mutant strain. This strain is viable and, despite being devoid of the Holliday junction resolvase activity that is readily detected in fractionated extracts from wild-type cells, exhibits normal levels of UV sensitivity and spontaneous or UV-induced mitotic recombination. In accordance with the absence of a nuclear phenotype, we show by fluorescence microscopy that a SpCCE1-GFP fusion localises exclusively to the mitochondria of S. pombe. In Saccharomyces cerevisiae the homologue of SpCCE1, CCE1, is known to function in the mitochondria where its role appears to be to remove recombination junctions and thus facilitate mitochondrial DNA segregation. A similar function can probably be attributed to SpCCE1 in S. pombe, since the majority of mitochondrial DNA from the Spcce1::ura4- strain is in an aggregated form apparently due to extensive interlinking of DNA molecules by recombination junctions. Surprisingly, this marked effect on the conformation of mitochondrial DNA results in little or no effect on proliferation or viability of the Spcce1::ura4+ strain. Possible explanations are discussed.","authors":"Doe CL, Osman F, Dixon J, Whitby MC","authors_abbrev":"Doe CL et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-08-23","publication_year":"2000","canto_session_key":"72f59f8e6feb16de","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-09-25 13:45:46","canto_approved_date":"2019-12-03 09:37:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-25 13:45:26","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-25"},{"uniquename":"PMID:20927605","title":"Convenient gram-scale metabolite synthesis by engineered fission yeast strains expressing functional human P450 systems.","citation":"Appl Biochem Biotechnol 2011 Apr;163(8):965-80","abstract":"The growing need for the characterization of cytochrome P450 (P450) metabolites often necessitates their synthesis up to Gram-scale. This task may in principle be achieved by using various techniques including chemical synthesis, the use of laboratory animals, in vitro P450 systems or microbial biotransformation. However, these approaches are in many instances unfavorable due to low yields, laborious purification, costs of cofactors, or the formation of non-physiologic metabolites. The fission yeast Schizosaccharomyces pombe has previously been shown by others and us to be very well suited for the heterologous expression of human P450s. In this study, we demonstrate whole-cell biotransformation reactions carried out with fission yeast strains that coexpress human cytochrome P450 reductase (CPR) and one of the following P450 isoforms: CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4, respectively. These strains could successfully convert their respective standard substrates but showed different responses with respect to incubation pH, the presence of glucose, and temperature, respectively. In addition, the preparative of synthesis of 2.8 g of 4'-hydroxydiclofenac was achieved by whole-cell biotransformation of diclofenac using a CPR-CYP2C9 coexpressing fission yeast strain.","doi":"10.1007/s12010-010-9100-3","authors":"Drăgan CA, Peters FT, Bour P, Schwaninger AE, Schaan SM, Neunzig I, Widjaja M, Zapp J, Kraemer T, Maurer HH, Bureik M","authors_abbrev":"Drăgan CA et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2010-10-08","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30217821","title":"Molecular architecture of G-quadruplex structures generated on duplex Rif1-binding sequences.","citation":"J Biol Chem 2018 Nov 02;293(44):17033-17049","abstract":"G-quadruplexes (G4s) are four-stranded DNA structures comprising stacks of four guanines, are prevalent in genomes, and have diverse biological functions in various chromosomal structures. A conserved protein, Rap1-interacting factor 1 (Rif1) from fission yeast ( Schizosaccharomyces pombe ), binds to Rif1-binding sequence (Rif1BS) and regulates DNA replication timing. Rif1BS is characterized by the presence of multiple G-tracts, often on both strands, and their unusual spacing. Although previous studies have suggested generation of G4-like structures on duplex Rif1BS, its precise molecular architecture remains unknown. Using gel-shift DNA binding assays and DNA footprinting with various nuclease probes, we show here that both of the Rif1BS strands adopt specific higher-order structures upon heat denaturation. We observed that the structure generated on the G-strand is consistent with a G4 having unusually long loop segments and that the structure on the complementary C-strand does not have an intercalated motif (i-motif). Instead, we found that the formation of the C-strand structure depends on the G4 formation on the G-strand. Thus, the higher-order structure generated at Rif1BS involved both DNA strands, and in some cases, G4s may form on both of these strands. The presence of multiple G-tracts permitted the formation of alternative structures when some G-tracts were mutated or disrupted by deazaguanine replacement, indicating the robust nature of DNA higher-order structures generated at Rif1BS. Our results provide general insights into DNA structures generated at G4-forming sequences on duplex DNA.","doi":"10.1074/jbc.RA118.005240","authors":"Masai H, Kakusho N, Fukatsu R, Ma Y, Iida K, Kanoh Y, Nagasawa K","authors_abbrev":"Masai H et al.","pubmed_publication_date":"02 Nov 2018","pubmed_entrez_date":"2018-09-16","publication_year":"2018","canto_session_key":"b20445317e600691","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-09-17 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.17"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18048158","title":"RNA string kernels for RNAi off-target evaluation.","citation":"Int J Bioinform Res Appl 2006;2(2):132-46","abstract":"RNA interference (RNAi) is a posttranscriptional gene silencing mechanism used to study gene functions, knock down viral genes, and treat diseases therapeutically. However, an 'off-target effect' deteriorates its specificity and applicability. Complete off-target effects can only be characterised by examining each gene in a genome, which is too expensive to conduct experimentally and motivates a computational study. To simulate the sequence matching between an siRNA and its target mRNA allowing for mismatches, G-U wobbles and bulges, we propose string kernels and develop their efficient implementations for off-target detection. We evaluate RNAi specificities in Schizosaccharomyces pombe, Caenorhabdithis elegans, and human genomes.","authors":"Qiu S, Lane T","authors_abbrev":"Qiu S et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-12-01","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30853434","title":"NDR Kinase Sid2 Drives Anillin-like Mid1 from the Membrane to Promote Cytokinesis and Medial Division Site Placement.","citation":"Curr Biol 2019 Mar 18;29(6):1055-1063.e2","abstract":"In animals and fungi, cytokinesis is facilitated by the constriction of an actomyosin contractile ring (CR) [1]. In Schizosaccharomyces pombe, the CR forms mid-cell during mitosis from clusters of proteins at the medial cell cortex called nodes [2]. The anillin-like protein Mid1 localizes to nodes and is required for CR assembly at mid-cell [3]. When CR constriction begins, Mid1 leaves the division site. How Mid1 disassociates and whether this step is important for cytokinetic progression has been unknown. The septation initiation network (SIN), analogous to the Hippo pathway of multicellular organisms, is a signaling cascade that triggers node dispersal, CR assembly and constriction, and septum formation [4, 5]. We report that the terminal SIN kinase, Sid2 [6], phosphorylates Mid1 to drive its removal from the cortex at CR constriction onset. A Mid1 mutant that cannot be phosphorylated by Sid2 remains cortical during cytokinesis, over-accumulates in interphase nodes following cell division in a manner dependent on the SAD kinase Cdr2, advances the G2/M transition, precociously recruits other CR components to nodes, pulls Cdr2 aberrantly into the CR, and reduces rates of CR maturation and constriction. When combined with cdr2 mutants that affect node assembly or disassembly, gross defects in division site positioning result. Our findings identify Mid1 as a key Sid2 substrate for SIN-mediated remodeling of the division site for efficient cytokinesis and provide evidence that nodes serve to integrate signals coordinating cell cycle progression and cytokinesis.","doi":"10.1016/j.cub.2019.01.075","authors":"Willet AH, DeWitt AK, Beckley JR, Clifford DM, Gould KL","authors_abbrev":"Willet AH et al.","pubmed_publication_date":"18 Mar 2019","pubmed_entrez_date":"2019-03-12","publication_year":"2019","canto_session_key":"de3fe5786898e2f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2019-04-18 14:48:55","canto_approved_date":"2025-07-22 15:51:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-04-01 17:58:24","canto_added_date":"2019-03-13 01:15:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":48,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.16","SPCC645.05c","SPCC4B3.15","SPAC2F7.03c","SPBC12D12.01","SPAC31A2.16","SPBC1A4.05","SPBC244.01c","SPAC57A10.02","SPAC24B11.11c","SPAC6F6.08c","SPAC926.03","SPAC644.06c","SPBC1604.08c","SPAC20G8.05c","SPAC4F8.13c","SPAC1F5.04c"],"gene_count":17,"ltp_gene_count":9,"approved_date":"2019-04-18"},{"uniquename":"EMBL:AU010458","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2107403","title":"Homologous activators of ras in fission and budding yeast.","citation":"Nature 1990 Mar 22;344(6264):355-7","abstract":"The ras proto-oncogene products are plasma membrane-bound, guanine nucleotide-binding proteins implicated in signal transduction across the plasma membrane. But the signal(s) that activates the ras pathway(s) is not known. In the budding yeast Saccharomyces cerevisiae, the CDC25 gene product acts upstream of Ras proteins, but it has not been clear whether CDC25 function is unique to the S. cerevisiae ras pathway. Here we report that the ste6 gene of fission yeast Schizosaccharomyces pombe is a homologue of CDC25: the ste6 gene product and the CDC25 gene product have significant amino-acid similarity in their C-terminal regions. Like the S. pombe ras1 gene, ste6 is essential for mating. Epistatic interactions indicate that the ste6 gene functions upstream of ras1. We propose that ste6 and CDC25 activate Ras protein through a common mechanism, perhaps by promoting GDP-GTP exchange, even though it seems that the function of Ras protein in budding yeast differs from that in fission yeast. Homologues of ste6 and CDC25 could regulate ras activity in other eukaryotic cells.","authors":"Hughes DA, Fukui Y, Yamamoto M","authors_abbrev":"Hughes DA et al.","pubmed_publication_date":"22 Mar 1990","pubmed_entrez_date":"1990-03-22","publication_year":"1990","canto_session_key":"e80c868d6c0d1ca5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-04-18 15:40:51","canto_approved_date":"2022-01-03 19:35:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-15 10:04:04","canto_added_date":"2012-02-24 05:55:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1442.01","SPAC17H9.09c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-04-18"},{"uniquename":"PMID:40114852","title":"Characterization and comparison of  Schizosaccharomyces pombe   cdc15  temperature-sensitive mutants.","citation":"MicroPubl Biol 2025;2025","abstract":"The F-BAR protein Cdc15 is essential for cytokinesis in the fission yeast  Schizosaccharomyces pombe  , playing a key scaffolding role and connecting the actomyosin-based cytokinetic ring to the plasma membrane. Here, we compared  cdc15  temperature-sensitive mutants isolated in multiple genetic screens. We determined the mutations within each  cdc15  mutant allele and analyzed their growth at different temperatures. Additionally, we report a new  cdc15  allele that highlights the requirement for Cdc15 in the recruitment of the early secretory pathway to the cellular division site. The new mutants described here expand the toolkit for studying cytokinesis in  S. pombe  .","doi":"10.17912/micropub.biology.001515","authors":"Turner LA, Vjestica A, Willet AH, Oliferenko S, Gould KL","authors_abbrev":"Turner LA et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-03-21","publication_year":"2025","canto_session_key":"f1b9bb385a8edc45","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2025-04-09 04:50:23","canto_approved_date":"2026-01-29 17:29:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-04-08 20:56:15","canto_added_date":"2025-03-22 00:25:04","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":15,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPAC22F8.08","SPAC20G8.05c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2025-04-09"},{"uniquename":"PMID:15629716","title":"Inactivation of the Cdc25 phosphatase by the stress-activated Srk1 kinase in fission yeast.","citation":"Mol Cell 2005 Jan 07;17(1):49-59","abstract":"The mechanisms by which environmental stress regulates cell cycle progression are poorly understood. In fission yeast, we show that Srk1 kinase, which associates with the stress-activated p38/Sty1 MAP kinase, regulates the onset of mitosis by inhibiting the Cdc25 phosphatase. Srk1 is periodically active in G2, and its overexpression causes cell cycle arrest in late G2 phase, whereas cells lacking srk1 enter mitosis prematurely. We find that Srk1 interacts with and phosphorylates Cdc25 at the same sites phosphorylated by the Chk1 and Cds1 (Chk2) kinases and that this phosphorylation is necessary for Srk1 to delay mitotic entry. Phosphorylation by Srk1 causes Cdc25 to bind to Rad24, a 14-3-3 protein family member, and accumulation of Cdc25 in the cytoplasm. However, Srk1 does not regulate Cdc25 in response to replication arrest or DNA damage but, rather, during a normal cell cycle and in response to nongenotoxic environmental stress.","authors":"López-Avilés S, Grande M, González M, Helgesen AL, Alemany V, Sanchez-Piris M, Bachs O, Millar JB, Aligue R","authors_abbrev":"López-Avilés S et al.","pubmed_publication_date":"07 Jan 2005","pubmed_entrez_date":"2005-01-05","publication_year":"2005","canto_session_key":"50a497b4c268664e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-23 16:21:46","canto_approved_date":"2023-10-13 08:30:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-21 13:55:38","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8E11.02c","SPAC24H6.05","SPCC1322.08","SPCC18B5.03","SPAC24B11.06c","SPBC11B10.09","SPAC11E3.09"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-03-23"},{"uniquename":"PMID:2541922","title":"Composite motifs and repeat symmetry in S. pombe centromeres: direct analysis by integration of NotI restriction sites.","citation":"Cell 1989 Jun 02;57(5):739-51","abstract":"S. pombe centromeres are large and complex. We introduced a method that enables us to characterize directly centromere DNAs. Genomic DNA fragments containing cen1, cen2, or cen3, respectively, are made by cleaving NotI sites integrated on target sites and are partially restricted for long-range mapping in PFG electrophoresis. The 40 kb long cen1 consists of two inverted approximately 10 kb motifs, each containing centromeric elements dg and dh, flanked by a central region. In cen2, three motifs are arranged in inverted and direct orientations with flanking domains, making up the approximately 70 kb long repetitious region. In cen3, approximately 15 copies of dg-dh constitute a region longer than 100 kb. A set of inverted motifs with an approximately 15 kb central region might be a prototype for the S. pombe centromeres. The motifs appear to play a role in chromosome stability and segregation. Their action may be additive, and the mutual directions of dg and dh inside a motif may not be essential for function.","authors":"Chikashige Y, Kinoshita N, Nakaseko Y, Matsumoto T, Murakami S, Niwa O, Yanagida M","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"02 Jun 1989","pubmed_entrez_date":"1989-06-02","publication_year":"1989","canto_session_key":"5536942e0e8c80b8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 22:16:19","canto_approved_date":"2018-12-22 22:16:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 22:16:15","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:16024659","title":"A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for heterochromatin formation.","citation":"Genes Dev 2005 Jul 15;19(14):1705-14","abstract":"Heterochromatin is critical for proper centromere and telomere function, and it plays a key role in the transcriptional silencing of specific genomic loci. In fission yeast, the Rik1 protein functions with the Clr4 histone methyltransferase at an early step in heterochromatin formation. Here, we use mass spectrometry and tandem affinity purification of a Rik1-TAP fusion protein to identify Rik1-associated proteins. These studies identify two novel proteins, Raf1 and Raf2, which we find are required for H3-K9 methylation and for transcriptional silencing within centromeric heterochromatin. We also find that subunits of a cullin-dependent E3 ubiquitin ligase are associated with Rik1 and Clr4, and Rik1-TAP preparations exhibit robust E3 ubiquitin ligase activity. Furthermore, expression of a dominant-negative allele of the Pcu4 cullin subunit disrupts regulation of K4 methylation within heterochromatin. These studies provide evidence for a novel Rik1-associated E3 ubiquitin ligase that is required for heterochromatin formation.","authors":"Horn PJ, Bastie JN, Peterson CL","authors_abbrev":"Horn PJ et al.","pubmed_publication_date":"15 Jul 2005","pubmed_entrez_date":"2005-07-19","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23H4.18c","SPBC428.08c","SPCC622.09","SPCC11E10.08","SPCC613.12c","SPAC3A11.08","SPCC970.07c"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:8978671","title":"The Schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin.","citation":"EMBO J 1996 Dec 02;15(23):6438-46","abstract":"The gene encoding the actin-related protein Arp3 was first identified in the fission yeast Schizosaccharomyces pombe and is a member of an evolutionarily conserved family of actin-related proteins. Here we present several key findings that define an essential role for Arp3p in the functioning of the cortical actin cytoskeleton. First, mutants in arp3 interact specifically with profilin and actin mutants. Second, Arp3 localizes to cortical actin patches which are required for polarized cell growth. Third, the arp3 gene is required for the reorganization of the actin cytoskeleton during the cell cycle. Finally, the Arp3 protein is present in a large protein complex. We believe that this complex may mediate the cortical functions of profilin at actin patches in S. pombe.","authors":"McCollum D, Feoktistova A, Morphew M, Balasubramanian M, Gould KL","authors_abbrev":"McCollum D et al.","pubmed_publication_date":"02 Dec 1996","pubmed_entrez_date":"1996-12-02","publication_year":"1996","canto_session_key":"c774be17d27e4ae9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-27 15:50:07","canto_approved_date":"2026-01-29 12:40:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-18 15:31:39","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":21,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.03","SPAC4A8.15c","SPBC32H8.12c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-04-27"},{"uniquename":"PMID:2900077","title":"Isolation of a DNA fragment which complements glutamine synthetase deficient strains of S. pombe.","citation":"Curr Genet 1988 Jun;13(6):487-94","abstract":"From a gene bank of S. pombe DNA, a 5.6 kb clone was isolated which complemented mutants defective in glutamine synthetase (GS) activity. Sub-cloning fragments of this 5.6 kb clone showed that the complementing activity was localised in a 1.6 kb HindIII-AvaI fragment and a partial DNA sequence revealed an open reading frame preceded by TATA sequences and a TGACTA sequence. Plasmid constructs carrying up to 3.4 kb of DNA used to transform gln- strains gave transformants which showed a wide range of GS activity, in some cases 100 times the wild-type level. These constructs identify DNA sequences lying downstream from the putative coding sequence which have effects on the total amount of enzyme activity, but do not affect the control imposed by the nitrogen source on which the cells are grown.","authors":"Barel I, Bignell G, Simpson A, MacDonald D","authors_abbrev":"Barel I et al.","pubmed_publication_date":"Jun 1988","pubmed_entrez_date":"1988-06-01","publication_year":"1988","canto_session_key":"11db51d15ea042b2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-07-01 11:05:26","canto_approved_date":"2026-01-25 05:49:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-07-01 10:43:49","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H4.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-07-01"},{"uniquename":"PMID:31627132","title":"Cross Talk between eIF2α and eEF2 Phosphorylation Pathways Optimizes Translational Arrest in Response to Oxidative Stress.","citation":"iScience 2019 Oct 25;20:466-480","abstract":"The cellular stress response triggers a cascade of events leading to transcriptional reprogramming and a transient inhibition of global protein synthesis, which is thought to be mediated by phosphorylation of eukaryotic initiation factor-2α (eIF2α). Using mouse embryonic fibroblasts (MEFs) and the fission yeast S. pombe, we report that rapid translational arrest and cell survival in response to hydrogen peroxide-induced oxidative stress do not rely on eIF2α kinases and eIF2α phosphorylation. Rather, H 2 O 2  induces a block in elongation through phosphorylation of eukaryotic elongation factor 2 (eEF2). Kinetic and dose-response analyses uncovered cross talk between the eIF2α and eEF2 phosphorylation pathways, indicating that, in MEFs, eEF2 phosphorylation initiates the acute shutdown in translation, which is maintained by eIF2α phosphorylation. Our results challenge the common conception that eIF2α phosphorylation is the primary trigger of translational arrest in response to oxidative stress and point to integrated control that may facilitate the survival of cancer cells.","doi":"10.1016/j.isci.2019.09.031","authors":"Sanchez M, Lin Y, Yang CC, McQuary P, Rosa Campos A, Aza Blanc P, Wolf DA","authors_abbrev":"Sanchez M et al.","pubmed_publication_date":"25 Oct 2019","pubmed_entrez_date":"2019-10-19","publication_year":"2019","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-10-20 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31969703","title":"Structure of the transcription coactivator SAGA.","citation":"Nature 2020 Jan;577(7792):717-720","abstract":"Gene transcription by RNA polymerase II is regulated by activator proteins that recruit the coactivator complexes SAGA (Spt-Ada-Gcn5-acetyltransferase) 1,2  and transcription factor IID (TFIID) 2-4 . SAGA is required for all regulated transcription 5  and is conserved among eukaryotes 6 . SAGA contains four modules 7-9 : the activator-binding Tra1 module, the core module, the histone acetyltransferase (HAT) module and the histone deubiquitination (DUB) module. Previous studies provided partial structures 10-14 , but the structure of the central core module is unknown. Here we present the cryo-electron microscopy structure of SAGA from the yeast Saccharomyces cerevisiae and resolve the core module at 3.3 Å resolution. The core module consists of subunits Taf5, Sgf73 and Spt20, and a histone octamer-like fold. The octamer-like fold comprises the heterodimers Taf6-Taf9, Taf10-Spt7 and Taf12-Ada1, and two histone-fold domains in Spt3. Spt3 and the adjacent subunit Spt8 interact with the TATA box-binding protein (TBP) 2,7,15-17 . The octamer-like fold and its TBP-interacting region are similar in TFIID, whereas Taf5 and the Taf6 HEAT domain adopt distinct conformations. Taf12 and Spt20 form flexible connections to the Tra1 module, whereas Sgf73 tethers the DUB module. Binding of a nucleosome to SAGA displaces the HAT and DUB modules from the core-module surface, allowing the DUB module to bind one face of an ubiquitinated nucleosome.","doi":"10.1038/s41586-020-1933-5","authors":"Wang H, Dienemann C, Stützer A, Urlaub H, Cheung ACM, Cramer P","authors_abbrev":"Wang H et al.","pubmed_publication_date":"Jan 2020","pubmed_entrez_date":"2020-01-24","publication_year":"2020","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC887.18c","SPCC5E4.03c","SPAC15A10.02","SPCC16C4.18c","SPBC25H2.11c","SPAC12G12.05c","SPBC21H7.02"],"gene_count":7,"ltp_gene_count":0},{"uniquename":"PMID:2937494","title":"Electron microscopic studies of condensed mitotic chromosomes in the fission yeast Schizosaccharomyces pombe.","citation":"Biol Cell 1985;55(1-2):27-34","abstract":"By blocking cells in mitosis with the anti-fungal drug thiabendazole, it has been possible to carry out ultrastructural studies on the condensed chromosomes of the fission yeast, Schizosaccharomyces pombe. It is estimated that the DNA in these chromosomes is compacted approximately 1000-fold, and that the nucleoprotein density is similar to that of higher eukaryotic metaphase chromosomes. A basic structural component of the condensed chromosomes appears to be a 50-60 nm fibre, which is often visible in a loop configuration on the periphery of the chromatids. This is reminiscent of the 50-60 nm fibre loops which are frequently seen in preparations of metaphase chromosomes, and suggests that mechanisms of nucleoprotein folding may be similar in both lower and higher eukaryotes.","authors":"Erard M, Barker DG","authors_abbrev":"Erard M et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013470","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9671035","title":"Global control of meiotic recombination genes by Schizosaccharomyces pombe rec16 (rep1).","citation":"Mol Gen Genet 1998 Jun;258(6):663-70","abstract":"The Schizosaccharomyces pombe rec16-125 mutation reduces meiotic recombination, delays premeiotic DNA synthesis, and reduces the accumulation of some but not other rec gene transcripts. To elucidate the function of the Rec16 global meiotic regulator, we cloned and sequenced rec16. The data revealed that rec16 is identical to rep1, which was previously shown to encode a protein with a zinc-finger motif required for pre-meiotic DNA synthesis. Transcripts of rec16 (rep1) were strongly induced and subsequently degraded during meiosis. In a rec16 (rep1) deletion mutant, meiotic induction of the seven rec genes tested, which appear to be directly involved in meiotic recombination, was significantly reduced or essentially abolished. Deletion of 80% of the gene essentially abolished meiotic recombination, whereas strains deleted for approximately one-quarter of the gene, from either end, retained partial activity. The rec16-125 mutation strongly reduced recombination in the intervals tested on chromosomes I and III, a phenotype characteristic of mutations in rec genes, such as rec7, whose expression requires Rec16 (Rep1). These results show that Rec16 (Rep1) does not have the regional specificity of Rec10. We infer that Rec16 (Rep1) is a transcriptional activator that is required for meiotic replication and recombination because it plays a role in the transcriptional induction of the rec and other meiosis-specific genes.","authors":"Ding R, Smith GR","authors_abbrev":"Ding R et al.","pubmed_publication_date":"Jun 1998","pubmed_entrez_date":"1998-07-22","publication_year":"1998","canto_session_key":"67a09675d9fe0893","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-07 09:44:52","canto_approved_date":"2019-11-07 09:44:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-07 09:44:47","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.02","SPBC1711.14","SPCC4E9.01c","SPCC1753.03c","SPCC1322.13","SPBC21B10.12","SPBC29A10.14","SPAC25G10.04c","SPBC2D10.06"],"gene_count":9,"ltp_gene_count":1,"approved_date":"2019-11-07"},{"uniquename":"PMID:40110920","title":"Improvement of Targeting Efficiency by Promoter Replacement of Markers in Integration Vectors.","citation":"Genes Cells 2025 Mar;30(2):e70013","abstract":"To establish a gene expression system that reflects physiological conditions, we developed a series of vectors that can be integrated into the chromosome. Compared with the integration vectors employing double-crossover recombination, single-crossover integration vectors have the advantage of high transformation efficiency. However, because single-crossover recombination generates repeat sequences upstream and downstream of the integrated fragment, this strategy is often associated with a risk that an integrated fragment may pop out from the chromosome during cultivation. Here, we assessed the frequency of pop-out using a fission yeast single-crossover integration vector, pDUAL. We also examined the effect of shortening the repeats on pop-out by employing a strategy involving heterologous replacement of the promoter for the leu1 marker in the vector. Due to the intrinsic low frequency of pop-out, the effect of promoter conversion on pop-out was negligible, if any. However, a clear ameliorative effect was observed in obtaining the desirable transformants in which a vector fragment was correctly inserted at the targeted locus, a result that may be driven by the limited potential for recombination in the promoter replacement construct.","doi":"10.1111/gtc.70013","authors":"Matsuyama A, Hashimoto A, Arioka M, Yoshida M","authors_abbrev":"Matsuyama A et al.","pubmed_publication_date":"Mar 2025","pubmed_entrez_date":"2025-03-20","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-03-21 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33728458","title":"Genome-wide screens in yeast models towards understanding chronological lifespan regulation.","citation":"Brief Funct Genomics 2022 Jan 25;21(1):4-12","abstract":"Cellular models such as yeasts are a driving force in biogerontology studies. Their simpler genome, short lifespans and vast genetic and genomics resources make them ideal to characterise pro-ageing and anti-ageing genes and signalling pathways. Over the last three decades, yeasts have contributed to the understanding of fundamental aspects of lifespan regulation including the roles of nutrient response, global protein translation rates and quality, DNA damage, oxidative stress, mitochondrial function and dysfunction as well as autophagy. In this short review, we focus on approaches used for competitive and non-competitive cell-based screens using the budding yeast Saccharomyces cerevisiae, and the fission yeast Schizosaccharomyces pombe, for deciphering the molecular mechanisms underlying chronological ageing. Automation accompanied with appropriate computational tools allowed manipulation of hundreds of thousands of colonies, generation, processing and analysis of genome-wide lifespan data. Together with barcoding and modern mutagenesis technologies, these approaches have allowed to take decisive steps towards a global, comprehensive view of cellular ageing.","doi":"10.1093/bfgp/elab011","authors":"Legon L, Rallis C","authors_abbrev":"Legon L et al.","pubmed_publication_date":"25 Jan 2022","pubmed_entrez_date":"2021-03-17","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-03-19 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34169552","title":"ZZ domains keep cytosol to vacuole delivery whiZZing along.","citation":"EMBO J 2021 Aug 02;40(15):e108777","abstract":"Selective autophagy relies on adaptor proteins to bind and transport cargos (or substrates) to the lysosome or vacuole, yet the mechanisms for cargo recognition are not well understood. In this issue, Wang et al (2021) showed that in the fission yeast, Nbr1, a homolog of a mammalian selective autophagy adaptor, recognizes vacuolar hydrolases Ams1 and Ape4 through both versatile and cargo-specific interactions with the Nbr1 ZZ1 domain.","doi":"10.15252/embj.2021108777","authors":"Hama Y, Zhang S, Mizushima N","authors_abbrev":"Hama Y et al.","pubmed_publication_date":"02 Aug 2021","pubmed_entrez_date":"2021-06-25","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-06-30 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2211869","title":"The transition of cells of the fission yeast beta-tubulin mutant nda3-311 as seen by freeze-substitution electron microscopy. Requirement of functional tubulin for spindle pole body duplication.","citation":"J Cell Sci 1990 Jun;96 ( Pt 2):275-82","abstract":"A previous fluorescence light-microscopic study showed that the fission yeast cold-sensitive beta-tubulin mutant nda3-311 was arrested with rod-like condensed chromosomes in a mitotic state at the restrictive temperature. Upon transfer to the permissive temperature, a spindle was formed and the nucleus was divided. In the present study, we employed freeze-substitution electron microscopy to examine the ultrastructure of arrested and released nda3-311 cells. In arrested cells, a single, displaced nucleus was seen with a single spindle pole body. Therefore, spindle pole body duplication seemed to require functional beta-tubulin. The nuclear membrane was highly deformed with a leaf-like profile in cross-section, possibly due to an interaction with the rod-like, condensed chromosomes. Upon transfer to the permissive temperature, the spindle pole duplicated and the daughter spindle pole bodies rapidly migrated to the opposite ends of the nucleus, accompanied by the formation of the mitotic spindle. Elongation of the nuclear envelope occurred with concomitant spindle extension, as in a wild-type mitosis. The deformed nuclear membrane became smooth and described a convex curve. The numerous vacuoles that are seen in the arrested cells decreased in number and increased in size. Septation was completed, leaving the two divided nuclei in one half of the cell. Hexagonally arranged microtubules, apparently forming the mitotic spindle, were observed in a cross-section of a cell after return to the permissive conditions.","authors":"Kanbe T, Hiraoka Y, Tanaka K, Yanagida M","authors_abbrev":"Kanbe T et al.","pubmed_publication_date":"Jun 1990","pubmed_entrez_date":"1990-06-01","publication_year":"1990","canto_session_key":"9ad17a9caa6fe2cf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-10-07 15:18:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-03-08 12:20:39","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-03-08"},{"uniquename":"PMID:11955632","title":"A potential membrane protein involved in pre-tRNA splicing of Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2002 Mar 19;1574(2):210-4","abstract":"We had previously isolated six pre-tRNA splicing mutants of Schizosaccharomyces pombe named ptp1 to ptp6. To investigate the molecular mechanism of tRNA splicing, we cloned the ptp4(+) gene by complementation of the temperature-sensitive growth defect. The ptp4(+) gene consists of three exons and encodes a putative protein of 218 amino acids with a molecular mass of 24.4 kDa. Analysis of the amino acid sequence reveals that the protein is a potential membrane protein with four membrane-spanning regions. The ptp4(+) shows significant similarity to the Saccharomyces cerevisiae putative protein YOR311C. Expression of the ptp4(+) gene in the ptp4(-) mutant restores the ability to splice tRNA. Northern blot analysis showed that the ptp4(+) gene is expressed in both mating-type cells of S. pombe. These results suggest that the Ptp4(+) could be a component involved in tRNA splicing.","authors":"Kim M, Hwang K, Lim CJ, Kim D","authors_abbrev":"Kim M et al.","pubmed_publication_date":"19 Mar 2002","pubmed_entrez_date":"2002-04-17","publication_year":"2002","canto_session_key":"6f2bb502b0b09c2b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-08-19 16:14:05","canto_approved_date":"2023-09-08 09:11:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 16:24:57","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-19"},{"uniquename":"PMID:25887563","title":"CodingQuarry: highly accurate hidden Markov model gene prediction in fungal genomes using RNA-seq transcripts.","citation":"BMC Genomics 2015 Mar 11;16(1):170","abstract":"The impact of gene annotation quality on functional and comparative genomics makes gene prediction an important process, particularly in non-model species, including many fungi. Sets of homologous protein sequences are rarely complete with respect to the fungal species of interest and are often small or unreliable, especially when closely related species have not been sequenced or annotated in detail. In these cases, protein homology-based evidence fails to correctly annotate many genes, or significantly improve ab initio predictions. Generalised hidden Markov models (GHMM) have proven to be invaluable tools in gene annotation and, recently, RNA-seq has emerged as a cost-effective means to significantly improve the quality of automated gene annotation. As these methods do not require sets of homologous proteins, improving gene prediction from these resources is of benefit to fungal researchers. While many pipelines now incorporate RNA-seq data in training GHMMs, there has been relatively little investigation into additionally combining RNA-seq data at the point of prediction, and room for improvement in this area motivates this study.\nCodingQuarry is a highly accurate, self-training GHMM fungal gene predictor designed to work with assembled, aligned RNA-seq transcripts. RNA-seq data informs annotations both during gene-model training and in prediction. Our approach capitalises on the high quality of fungal transcript assemblies by incorporating predictions made directly from transcript sequences. Correct predictions are made despite transcript assembly problems, including those caused by overlap between the transcripts of adjacent gene loci. Stringent benchmarking against high-confidence annotation subsets showed CodingQuarry predicted 91.3% of Schizosaccharomyces pombe genes and 90.4% of Saccharomyces cerevisiae genes perfectly. These results are 4-5% better than those of AUGUSTUS, the next best performing RNA-seq driven gene predictor tested. Comparisons against whole genome Sc. pombe and S. cerevisiae annotations further substantiate a 4-5% improvement in the number of correctly predicted genes.\nWe demonstrate the success of a novel method of incorporating RNA-seq data into GHMM fungal gene prediction. This shows that a high quality annotation can be achieved without relying on protein homology or a training set of genes. CodingQuarry is freely available ( https://sourceforge.net/projects/codingquarry/ ), and suitable for incorporation into genome annotation pipelines.","doi":"10.1186/s12864-015-1344-4","authors":"Testa AC, Hane JK, Ellwood SR, Oliver RP","authors_abbrev":"Testa AC et al.","pubmed_publication_date":"11 Mar 2015","pubmed_entrez_date":"2015-04-19","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-04-20 00:19:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20929775","title":"Two histone marks establish the inner centromere and chromosome bi-orientation.","citation":"Science 2010 Oct 08;330(6001):239-43","abstract":"For proper partitioning of chromosomes in mitosis, the chromosomal passenger complex (CPC) including Aurora B and survivin must be localized at the center of paired kinetochores, at the site called the inner centromere. It is largely unknown what defines the inner centromere and how the CPC is targeted to this site. Here, we show that the phosphorylation of histone H3-threonine 3 (H3-pT3) mediated by Haspin cooperates with Bub1-mediated histone 2A-serine 121 (H2A-S121) phosphorylation in targeting the CPC to the inner centromere in fission yeast and human cells. H3-pT3 promotes nucleosome binding of survivin, whereas phosphorylated H2A-S121 facilitates the binding of shugoshin, the centromeric CPC adaptor. Haspin colocalizes with cohesin by associating with Pds5, whereas Bub1 localizes at kinetochores. Thus, the inner centromere is defined by intersection of two histone kinases.","doi":"10.1126/science.1194498","authors":"Yamagishi Y, Honda T, Tanno Y, Watanabe Y","authors_abbrev":"Yamagishi Y et al.","pubmed_publication_date":"08 Oct 2010","pubmed_entrez_date":"2010-10-09","publication_year":"2010","canto_session_key":"d4e73d1a93ec5860","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-08-30 13:41:19","canto_approved_date":"2024-10-09 11:19:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-25 12:41:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":64,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.02","SPCC962.02c","SPCC1322.12c","SPAC664.01c","SPAC15A10.15","SPAC1834.04","SPCC622.08c","SPAC19G12.06c","SPBC8D2.04","SPAC17H9.20","SPAC23C4.03","SPBC1105.11c","SPCC320.13c"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2018-08-30"},{"uniquename":"PMID:28096519","title":"The nuclear poly(A) binding protein of mammals, but not of fission yeast, participates in mRNA polyadenylation.","citation":"RNA 2017 Apr;23(4):473-482","abstract":"The nuclear poly(A) binding protein (PABPN1) has been suggested, on the basis of biochemical evidence, to play a role in mRNA polyadenylation by strongly increasing the processivity of poly(A) polymerase. While experiments in metazoans have tended to support such a role, the results were not unequivocal, and genetic data show that the  S. pombe  ortholog of PABPN1, Pab2, is not involved in mRNA polyadenylation. The specific model in which PABPN1 increases the rate of poly(A) tail elongation has never been examined in vivo. Here, we have used 4-thiouridine pulse-labeling to examine the lengths of newly synthesized poly(A) tails in human cells. Knockdown of PABPN1 strongly reduced the synthesis of full-length tails of ∼250 nucleotides, as predicted from biochemical data. We have also purified  S. pombe  Pab2 and the  S. pombe  poly(A) polymerase, Pla1, and examined their in vitro activities. Whereas PABPN1 strongly increases the activity of its cognate poly(A) polymerase in vitro, Pab2 was unable to stimulate Pla1 to any significant extent. Thus, in vitro and in vivo data are consistent in supporting a role of PABPN1 but not  S. pombe  Pab2 in the polyadenylation of mRNA precursors.","doi":"10.1261/rna.057026.116","authors":"Kühn U, Buschmann J, Wahle E","authors_abbrev":"Kühn U et al.","pubmed_publication_date":"Apr 2017","pubmed_entrez_date":"2017-01-19","publication_year":"2017","canto_session_key":"b4434112f12609a3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-23 16:01:01","canto_approved_date":"2023-03-02 22:41:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-23 16:00:54","canto_added_date":"2017-01-19 01:15:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.04","SPBC16E9.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-11-23"},{"uniquename":"PMID:21945095","title":"Mcm10 interacts with Rad4/Cut5(TopBP1) and its association with origins of DNA replication is dependent on Rad4/Cut5(TopBP1).","citation":"DNA Repair (Amst) 2011 Nov 10;10(11):1154-63","abstract":"Initiation of DNA replication in eukaryotes is a highly conserved and ordered process involving the co-ordinated, stepwise association of distinct proteins at multiple origins of replication throughout the genome. Here, taking Schizosaccharomyces pombe as a model, the role of Rad4(TopBP1) in the assembly of the replication complex has been examined. Quantitative chromatin immunoprecipitation experiments confirm that Rad4(TopBP1) associates with origins of DNA replication and, in addition, demonstrate that the protein is not present within the active replisome. A direct interaction between Rad4(TopBP1) and Mcm10 is shown and this is reflected in the Rad4(TopBP1)-dependent origin association of Mcm10. Rad4(TopBP1) is also shown to interact with Sld2 and Sld3 and to be required for the stable origin association of these two proteins. Rad4(TopBP1) chromatin association at stalled replication forks was found to be dependent upon the checkpoint protein Rad9, which was not required for Rad4(TopBP1) origin association. Comparison of the levels of chromatin association at origins of replication and stalled replication forks and the differential requirement for Rad9 suggest functional differences for Rad4(TopBP1) at these distinct sites.","doi":"10.1016/j.dnarep.2011.09.001","authors":"Taylor M, Moore K, Murray J, Aves SJ, Price C","authors_abbrev":"Taylor M et al.","pubmed_publication_date":"10 Nov 2011","pubmed_entrez_date":"2011-09-28","publication_year":"2011","canto_session_key":"77007fae1e2ad4f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-02-03 13:49:39","canto_approved_date":"2023-11-27 08:37:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-03 13:49:33","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.07c","SPBC1347.10","SPAC24H6.06","SPAC6B12.11","SPAC23C4.18c","SPCC16A11.17","SPBC216.05","SPAC14C4.13"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-02-03"},{"uniquename":"PMID:23093598","title":"The common ancestral core of vertebrate and fungal telomerase RNAs.","citation":"Nucleic Acids Res 2013 Jan 07;41(1):450-62","abstract":"Telomerase is a ribonucleoprotein with an intrinsic telomerase RNA (TER) component. Within yeasts, TER is remarkably large and presents little similarity in secondary structure to vertebrate or ciliate TERs. To better understand the evolution of fungal telomerase, we identified 74 TERs from Pezizomycotina and Taphrinomycotina subphyla, sister clades to budding yeasts. We initially identified TER from Neurospora crassa using a novel deep-sequencing-based approach, and homologous TER sequences from available fungal genome databases by computational searches. Remarkably, TERs from these non-yeast fungi have many attributes in common with vertebrate TERs. Comparative phylogenetic analysis of highly conserved regions within Pezizomycotina TERs revealed two core domains nearly identical in secondary structure to the pseudoknot and CR4/5 within vertebrate TERs. We then analyzed N. crassa and Schizosaccharomyces pombe telomerase reconstituted in vitro, and showed that the two RNA core domains in both systems can reconstitute activity in trans as two separate RNA fragments. Furthermore, the primer-extension pulse-chase analysis affirmed that the reconstituted N. crassa telomerase synthesizes TTAGGG repeats with high processivity, a common attribute of vertebrate telomerase. Overall, this study reveals the common ancestral cores of vertebrate and fungal TERs, and provides insights into the molecular evolution of fungal TER structure and function.","doi":"10.1093/nar/gks980","authors":"Qi X, Li Y, Honda S, Hoffmann S, Marz M, Mosig A, Podlevsky JD, Stadler PF, Selker EU, Chen JJ","authors_abbrev":"Qi X et al.","pubmed_publication_date":"07 Jan 2013","pubmed_entrez_date":"2012-10-25","publication_year":"2013","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18628858","title":"Website review: how to get the best from fission yeast genome data.","citation":"Comp Funct Genomics 2002;3(3):282-8","abstract":"Researchers are increasingly depending on various centralized resources to access the vast amount of information reported in the literature and generated by systematic sequencing and functional genomics projects. Biological databases have become everyday working tools for many researchers. This dependency goes both ways in that the databases require continuous feedback from the research community to maintain accurate, reliable, and upto- date information. The fission yeast Schizosaccharomyces pombe has recently been sequenced, setting the stage for the post-genome era of this popular model organism. Here, we provide an overview of relevant databases available, or being developed, together with a compilation of Internet resources containing useful information and tools for fission yeast.","doi":"10.1002/cfg.175","authors":"Wood V, Bähler J","authors_abbrev":"Wood V et al.","pubmed_publication_date":"2002","pubmed_entrez_date":"2008-07-17","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17299416","title":"Comparative proteomic and transcriptomic profiling of the fission yeast Schizosaccharomyces pombe.","citation":"Mol Syst Biol 2007;3:79","abstract":"The fission yeast Schizosaccharomyces pombe is a widely used model organism to study basic mechanisms of eukaryotic biology, but unlike other model organisms, its proteome remains largely uncharacterized. Using a shotgun proteomics approach based on multidimensional prefractionation and tandem mass spectrometry, we have detected approximately 30% of the theoretical fission yeast proteome. Applying statistical modelling to normalize spectral counts to the number of predicted tryptic peptides, we have performed label-free quantification of 1465 proteins. The fission yeast protein data showed considerable correlations with mRNA levels and with the abundance of orthologous proteins in budding yeast. Functional pathway analysis indicated that the mRNA-protein correlation is strong for proteins involved in signalling and metabolic processes, but increasingly discordant for components of protein complexes, which clustered in groups with similar mRNA-protein ratios. Self-organizing map clustering of large-scale protein and mRNA data from fission and budding yeast revealed coordinate but not always concordant expression of components of functional pathways and protein complexes. This finding reaffirms at the protein level the considerable divergence in gene expression patterns of the two model organisms that was noticed in previous transcriptomic studies.","authors":"Schmidt MW, Houseman A, Ivanov AR, Wolf DA","authors_abbrev":"Schmidt MW et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-02-15","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40446033","title":"Mechanistic insights into the stimulation of the histone H3K9 methyltransferase Clr4 by proximal H3K14 ubiquitination.","citation":"Sci Adv 2025 May 30;11(22):eadu1864","abstract":"H3K9 methylation, a conserved heterochromatin marker, is crucial for chromosome segregation and gene regulation. Clr4 is the sole known methyltransferase catalyzing H3K9 methylation in  Schizosaccharomyces pombe . Clr4 K455/K472 automethylation and H3K14 ubiquitination (H3K14Ub) are vital activators of Clr4, ensuring appropriate heterochromatin deposition and preventing deleterious silencing. While automethylation's activation mechanism is uncovered, the mechanism of H3K14Ub's significantly stronger stimulation on Clr4 remains unclear. Here, we determined the crystal structures of Clr4 bound to ubiquitinated and unmodified H3 peptides at 2.60 and 2.39 angstrom, which revealed a synergistic mechanism underlying the pronounced stimulatory effect: H3K14Ub increases substrate affinity through multivalent interactions and facilitates the allosteric transition of Clr4 from an inactive apo conformation to a hyperactive \"catalyzing state,\" including conformational changes in the αC-SET-insertion region, autoregulatory loop, and the β9/10 loop. We finally propose a multilevel structural model for the Clr4 catalytic-regulatory cycle. This work provides structural insights into the interplay between histone modifications and their collective impact on epigenetic regulation.","doi":"10.1126/sciadv.adu1864","authors":"Du Y, Sun M, Li Z, Wu X, Qu Q, Ai H, Liu L","authors_abbrev":"Du Y et al.","pubmed_publication_date":"30 May 2025","pubmed_entrez_date":"2025-05-30","publication_year":"2025","canto_session_key":"ecbad24d71c19461","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-05-30 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC8D2.04","SPBC428.08c"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"9isz","gene_chains":[{"gene_uniquename":"SPBC428.08c","chain":"A/B","position":"191-490"},{"gene_uniquename":"SPBC8D2.04","chain":"E/F","position":"4-20"}],"title":"Structure of Clr4 catalyzing K14-ubiquitinated histone H3 K9 methylation","entry_authors":"Du YX,Liu L","entry_authors_abbrev":"Du YX et al.","reference_uniquename":"PMID:40446033","experimental_method":"X-ray","resolution":"2.6"},{"pdb_id":"9it4","gene_chains":[{"gene_uniquename":"SPBC428.08c","chain":"B","position":"191-490"},{"gene_uniquename":"SPBC8D2.04","chain":"F","position":"4-20"}],"title":"Structure of Clr4 catalyzing histone H3 K9 methylation","entry_authors":"Du YX,Liu L","entry_authors_abbrev":"Du YX et al.","reference_uniquename":"PMID:40446033","experimental_method":"X-ray","resolution":"2.39"}]},{"uniquename":"PMID:21541004","title":"Simon Labbé's work on iron and copper homeostasis.","citation":"World J Biol Chem 2010 May 26;1(5):196-200","abstract":"Iron and copper have a wealth of functions in biological systems, which makes them essential micronutrients for all living organisms. Defects in iron and copper homeostasis are directly responsible for diseases, and have been linked to impaired development, metabolic syndromes and fungal virulence. Consequently, it is crucial to gain a comprehensive understanding of the molecular bases of iron- and copper-dependent proteins in living systems. Simon Labbé maintains parallel programs on iron and copper homeostasis using the fission yeast Schizosaccharomyces pombe (Schiz. pombe) as a model system. The study of fission yeast transition-metal metabolism has been successful, not only in discerning the genes and pathways functioning in Schiz. pombe, but also the genes and pathways that are active in mammalian systems and for other fungi.","doi":"10.4331/wjbc.v1.i5.196","authors":"Labbé S","authors_abbrev":"Labbé S","pubmed_publication_date":"26 May 2010","pubmed_entrez_date":"2011-05-05","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8479429","title":"The cell cycle genes cdc22+ and suc22+ of the fission yeast Schizosaccharomyces pombe encode the large and small subunits of ribonucleotide reductase.","citation":"Mol Gen Genet 1993 Apr;238(1-2):241-51","abstract":"The cdc22+ gene of Schizosaccharomyces pombe is required early in the cell cycle, and its transcript varies in concentration in step with the cell cycle, with a peak level at the G1-S boundary. The sequences of the cdc22+ gene and of a multicopy suppressor of cdc22ts mutations, suc22+, have been determined. The cdc22+ open reading frame, which is interrupted in the genome by a single intron very close to its 5' end, encodes a protein of 811 amino acids, which has an amino acid sequence highly similar to that of the large subunit of ribonucleotide reductase from several species. The suc22+ gene contains an uninterrupted open reading frame of 391 amino acids, very similar to the sequence of the small subunit of ribonucleotide reductase. Disruption of either gene is lethal. Upstream of the cdc22+ coding region are seven short sequence elements similar to the recognition sequence for MluI, which are involved in regulating periodic transcription of the gene. Inhibition of DNA synthesis by hydroxyurea results in a several-fold increase in the level of the cdc22+ transcript. In contrast, hydroxyurea does not induce the 1.5 kb transcript of suc22+, but results in the induction of a 1.9 kb mRNA which hybridises to suc22+ DNA.","authors":"Fernandez Sarabia MJ, McInerny C, Harris P, Gordon C, Fantes P","authors_abbrev":"Fernandez Sarabia MJ et al.","pubmed_publication_date":"Apr 1993","pubmed_entrez_date":"1993-04-01","publication_year":"1993","canto_session_key":"d3ef79e3f89a4ef2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 16:01:28","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-31 17:22:09","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPBC25D12.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-31"},{"uniquename":"PMID:31087092","title":"Alp7-Mto1 and Alp14 synergize to promote interphase microtubule regrowth from the nuclear envelope.","citation":"J Mol Cell Biol 2019 Dec 23;11(11):944-955","abstract":"Microtubules grow not only from the centrosome but also from various noncentrosomal microtubule-organizing centers (MTOCs), including the nuclear envelope (NE) and pre-existing microtubules. The evolutionarily conserved proteins Mto1/CDK5RAP2 and Alp14/TOG/XMAP215 have been shown to be involved in promoting microtubule nucleation. However, it has remained elusive as to how the microtubule nucleation promoting factors are specified to various noncentrosomal MTOCs, particularly the NE, and how these proteins coordinate to organize microtubule assembly. Here, we demonstrate that in the fission yeast Schizosaccharomyces pombe, efficient interphase microtubule growth from the NE requires Alp7/TACC, Alp14/TOG/XMAP215, and Mto1/CDK5RAP2. The absence of Alp7, Alp14, or Mto1 compromises microtubule regrowth on the NE in cells undergoing microtubule repolymerization. We further demonstrate that Alp7 and Mto1 interdependently localize to the NE in cells without microtubules and that Alp14 localizes to the NE in an Alp7 and Mto1-dependent manner. Tethering Mto1 to the NE in cells lacking Alp7 partially restores microtubule number and the efficiency of microtubule generation from the NE. Hence, our study delineates that Alp7, Alp14, and Mto1 work in concert to regulate interphase microtubule regrowth on the NE.","doi":"10.1093/jmcb/mjz038","authors":"Liu W, Zheng F, Wang Y, Fu C","authors_abbrev":"Liu W et al.","pubmed_publication_date":"23 Dec 2019","pubmed_entrez_date":"2019-05-16","publication_year":"2019","canto_session_key":"de7fb03a2e70fba6","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-05-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19180638","title":"SpOPT1, a member of the oligopeptide family (OPT) of the fission yeast Schizosaccharomyces pombe, is involved in the transport of glutathione through the outer membrane of the cell.","citation":"Yeast 2009 Jan;26(1):67-73","abstract":"A protein involved in the transport of glutathione has been identified, cloned and characterized from the fission yeast Schizosaccharomyces pombe. Database searches revealed the Sz. pombe ORF SPAC29B12.10c as a close homologue to several members of the OPT family, including the Saccharomyces cerevisiae high-affinity glutathione transporter Hgt1p. The gene product of SPAC29B12.10c has been identified as a protein, named SpOPT1, localized within the plasma membrane, transporting the tripeptide glutathione. Disruption of SPAC29B12.10c led to strains inable to grow on media containing glutathione as a sole source of sulphur, due to the inability to internalize the tripeptide. Disruptants contained significantly less glutathione than wild-type cells. Furthermore, DeltaSpopt1 strains were non-viable in a glutathione biosynthesis-defective (Deltagsh2) background. However, it was possible to complement the disruption of Spopt1 by overexpressing the intact ORF in the disrupted strain.","doi":"10.1002/yea.1652","authors":"Dworeck T, Wolf K, Zimmermann M","authors_abbrev":"Dworeck T et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2009-01-31","publication_year":"2009","canto_session_key":"0148c364556794c5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-26 13:36:42","canto_approved_date":"2021-08-19 20:25:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-05 15:10:05","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3F10.04","SPAC29B12.10c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-10-26"},{"uniquename":"PMID:18256525","title":"What makes centromeric cohesion resistant to separase cleavage during meiosis I but not during meiosis II?","citation":"Cell Cycle 2008 Jan 15;7(2):151-3","abstract":"Segregation of chromosomes during meiosis I is triggered by separase cleavage of the cohesin's Rec8 subunit along chromosome arms. Centromeric cohesin is protected from separase cleavage during meiosis I by Sgo1/MEI-S332 proteins in complex with protein phosphatase 2A (PP2A). This retention of centromeric sister chromatid cohesion is essential for faithful segregation of chromatids during the second meiotic division. While Sgo1/PP2A complex is required for protecting centromeric sister chromatid cohesion during meiosis I, it is not known what renders the centromeric cohesion sensitive to separase cleavage during meiosis II. Our data suggest that the absence of Sgo1 and PP2A from meiosis II centromeres is not sufficient to render centromeric cohesion sensitive to cleavage by separase and additional factors are required to ensure the removal of centromeric cohesion during meiosis II.","authors":"Gregan J, Rumpf C, Li Z, Cipak L","authors_abbrev":"Gregan J et al.","pubmed_publication_date":"15 Jan 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11178233","title":"Where does fission yeast sit on the tree of life?","citation":"Genome Biol 2000;1(2):REVIEWS1011","abstract":"The budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe are as different from each other as either is from animals: their ancestors separated about 420 to 330 million years ago. Now that S. pombe is poised to join the post-genome era, its evolutionary position should become much clearer.","authors":"Sipiczki M","authors_abbrev":"Sipiczki M","pubmed_publication_date":"2000","pubmed_entrez_date":"2001-02-24","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10809753","title":"Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals that the polyubiquitin-binding site of this subunit is essential when Rpn12/Mts3 activity is compromised.","citation":"J Biol Chem 2000 May 19;275(20):15182-92","abstract":"Substrates are targeted for proteolysis by the ubiquitin pathway by the addition of a polyubiquitin chain before being degraded by the 26 S proteasome. Previously, a subunit of the proteasome, S5a, was identified that was able to bind to polyubiquitin in vitro and thus proposed to act as a substrate recognition component. Deletion of the corresponding Saccharomyces cerevisiae gene, MCB1/RPN10, rendered cells viable indicating that other proteasomal polyubiquitin receptors must exist. In this study, we describe pus1(+), the fission yeast homologue of RPN10. This gene is also not required for cell viability; however, the Deltapus1 mutant is synthetically lethal with mutations in other proteasomal component-encoding genes, namely mts3, pad1, and mts4 (RPN12, RPN11, and RPN1). Overexpression of pus1(+) is able to rescue mts3-1 at 32 degrees C but overexpression of a cDNA encoding a version of Pus1 that does not bind to polyubiquitin cannot and leads to greatly reduced viability when used to rescue the mts3-1Deltapus1 double mutant. The Mts3 protein was unable to bind to polyubiquitin in vitro, but the Pus1 and Mts3 proteins were found to bind to one another in vitro, which taken together with the genetic data suggests that they are also closely associated in vivo.","authors":"Wilkinson CR, Ferrell K, Penney M, Wallace M, Dubiel W, Gordon C","authors_abbrev":"Wilkinson CR et al.","pubmed_publication_date":"19 May 2000","pubmed_entrez_date":"2000-05-16","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31G5.13","SPBC16G5.01","SPAC637.10c","SPBP19A11.03c","SPBC29B5.01"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:6941065","title":"Nucleo-cytoplasmic interactions in the petite negative yeast Schizosaccharomyces pombe. Inhibition of nuclear and mitochondrial DNA syntheses in the absence of cytoplasmic protein synthesis.","citation":"Mol Gen Genet 1981;181(3):306-8","abstract":"In the petite positive yeast, Saccharomyces cerevisiae, cycloheximide selectively inhibits protein synthesis on cytoplasmic ribosomes, and, as a consequence, nuclear DNA synthesis. Mitochondrial DNA, however, is synthesized for 4-6 h after cessation of protein synthesis. In this paper we show that in contrast to Saccharomyces cerevisiae, synthesis of mitochondrial and nuclear DNA is tightly coordinated in the petite negative yeast Schizosaccharomyces pombe, since inhibition of cytoplasmic protein synthesis leads immediately to cessation of both nuclear and mitochondrial DNA synthesis.","authors":"Del Giudice L, Wolf K, Buono C, Manna F","authors_abbrev":"Del Giudice L et al.","pubmed_publication_date":"1981","pubmed_entrez_date":"1981-01-01","publication_year":"1981","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20106903","title":"Schizosaccharomyces pombe possesses two paralogous valyl-tRNA synthetase genes of mitochondrial origin.","citation":"Mol Biol Evol 2010 Jun;27(6):1415-24","abstract":"Previous studies showed that VAS1 of Saccharomyces cerevisiae encodes both cytosolic and mitochondrial forms of valyl-tRNA synthetase (ValRS) through alternative initiation of translation. We show herein that except for Schizosaccharomyces pombe, all yeast species studied contained a single ValRS gene encoding both forms, and all of the mature protein forms deduced from those genes possessed an N-terminal appended domain (Ad) that was absent from their bacterial relatives. In contrast, S. pombe contained two distinct nuclear ValRS genes, one encoding the mitochondrial form and the other its cytosolic counterpart. Although the cytosolic form closely resembles other yeast ValRS sequences (approximately 60% identity), the mitochondrial form exhibits significant divergence from others (approximately 35% identity). Both genes are active and essential for the survival of the yeast. Most conspicuously, the mitochondrial form lacks the characteristic Ad. A phylogenetic analysis further suggested that both forms of S. pombe ValRS are of mitochondrial origin, and the mitochondrial form is ancestral to the cytoplasmic form.","doi":"10.1093/molbev/msq025","authors":"Chiu WC, Chang CP, Wen WL, Wang SW, Wang CC","authors_abbrev":"Chiu WC et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-01-29","publication_year":"2010","canto_session_key":"472dca5794c2908f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-01-06 18:41:36","canto_approved_date":"2025-02-19 16:19:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-23 13:15:56","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.08c","SPBC1709.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-01-06"},{"uniquename":"PMID:38899894","title":"Membrane and organelle rearrangement during ascospore formation in budding yeast.","citation":"Microbiol Mol Biol Rev 2024 Jun 20;:e0001324","abstract":"SUMMARYIn ascomycete fungi, sexual spores, termed ascospores, are formed after meiosis. Ascospore formation is an unusual cell division in which daughter cells are created within the cytoplasm of the mother cell by  de novo  generation of membranes that encapsulate each of the haploid chromosome sets created by meiosis. This review describes the molecular events underlying the creation, expansion, and closure of these membranes in the budding yeast,  Saccharomyces cerevisiae . Recent advances in our understanding of the regulation of gene expression and the dynamic behavior of different membrane-bound organelles during this process are detailed. While less is known about ascospore formation in other systems, comparison to the distantly related fission yeast suggests that the molecular events will be broadly similar throughout the ascomycetes.","doi":"10.1128/mmbr.00013-24","authors":"Neiman AM","authors_abbrev":"Neiman AM","pubmed_publication_date":"20 Jun 2024","pubmed_entrez_date":"2024-06-20","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-06-20 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8319772","title":"In vivo phosphorylation, mitotic behavior, and nuclear binding of the catalytic subunit of DNA polymerase alpha in fission yeast.","citation":"Exp Cell Res 1993 Jul;207(1):41-7","abstract":"We studied the phosphorylation of fission yeast p170 (the catalytic subunit of DNA polymerase alpha) and its relationship to the cell cycle. In exponentially growing cells, p170 was phosphorylated at serine residues. Its phosphorylation level did not quantitatively change when cell strains carrying conditional cell division cycle (cdc) mutations arrested at different stages of the cell cycle, under restrictive growth conditions. Especially, phosphorylation did not significantly vary when cells carrying the temperature-sensitive cdc2-33 mutation were shifted to the restrictive temperature, which indicates a minor role, if any, of p34cdc2 in this process. Also, the extent of p170 phosphorylation did not remarkably change during mitosis, a situation which differs from that reported for human DNA polymerase alpha. We used immunofluorescence microscopy and cell fractionation to study the intracellular distribution of p170. We here provide evidence that the protein remains tenaciously associated with nuclear structures throughout the cell cycle and is not redistributed into the cytoplasm at mitosis, as it is in human cells. A possible correlation between phosphorylation, nuclear binding, and mitotic behavior of DNA polymerase alpha catalytic subunits in eukaryotes is therefore conceivable.","authors":"Bouvier D, De Recondo AM, Baldacci G","authors_abbrev":"Bouvier D et al.","pubmed_publication_date":"Jul 1993","pubmed_entrez_date":"1993-07-01","publication_year":"1993","canto_session_key":"33d5d91d38abcc47","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-07-22 13:16:35","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-07-22 13:16:29","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F7.05","SPAC3H5.06c","SPAC24H6.05","SPBC11B10.09"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-07-22"},{"uniquename":"PMID:15121850","title":"The Schizosaccharomyces pombe HIRA-like protein Hip1 is required for the periodic expression of histone genes and contributes to the function of complex centromeres.","citation":"Mol Cell Biol 2004 May;24(10):4309-20","abstract":"HIRA-like (Hir) proteins are evolutionarily conserved and are implicated in the assembly of repressive chromatin. In Saccharomyces cerevisiae, Hir proteins contribute to the function of centromeres. However, S. cerevisiae has point centromeres that are structurally different from the complex centromeres of metazoans. In contrast, Schizosaccharomyces pombe has complex centromeres whose domain structure is conserved with that of human centromeres. Therefore, we examined the functions of the fission yeast Hir proteins Slm9 and the previously uncharacterised protein Hip1. Deletion of hip1(+) resulted in phenotypes that were similar to those described previously for slm9 Delta cells: a cell cycle delay, synthetic lethality with cdc25-22, and poor recovery from nitrogen starvation. However, while it has previously been shown that Slm9 is not required for the periodic expression of histone H2A, we found that loss of Hip1 led to derepression of core histone genes expression outside of S phase. Importantly, we found that deletion of either hip1(+) or slm9(+) resulted in increased rates of chromosome loss, increased sensitivity to spindle damage, and reduced transcriptional silencing in the outer centromeric repeats. Thus, S. pombe Hir proteins contribute to pericentromeric heterochromatin, and our data thus suggest that Hir proteins may be required for the function of metazoan centromeres.","authors":"Blackwell C, Martin KA, Greenall A, Pidoux A, Allshire RC, Whitehall SK","authors_abbrev":"Blackwell C et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-05-04","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC15D4.03","SPBC31F10.13c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:17353272","title":"Mus81-Eme1-dependent and -independent crossovers form in mitotic cells during double-strand break repair in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2007 May;27(10):3828-38","abstract":"During meiosis, double-strand breaks (DSBs) lead to crossovers, thought to arise from the resolution of double Holliday junctions (HJs) by an HJ resolvase. In Schizosaccharomyces pombe, meiotic crossovers are produced primarily through a mechanism requiring the Mus81-Eme1 endonuclease complex. Less is known about the processes that produces crossovers during the repair of DSBs in mitotic cells. We employed an inducible DSB system to determine the role of Rqh1-Top3 and Mus81-Eme1 in mitotic DSB repair and crossover formation in S. pombe. In agreement with the meiotic data, crossovers are suppressed in cells lacking Mus81-Eme1. And relative to the wild type, rqh1Delta cells show a fourfold increase in crossover frequency. This suppression of crossover formation by Rqh1 is dependent on its helicase activity. We found that the synthetic lethality of cells lacking both Rqh1 and Eme1 is suppressed by loss of swi5(+), which allowed us to show that the excess crossovers formed in an rqh1Delta background are independent of Mus81-Eme1. This result suggests that a second process for crossover formation exists in S. pombe and is consistent with our finding that deletion of swi5(+) restored meiotic crossovers in eme1Delta cells. Evidence suggesting that Rqh1 also acts downstream of Swi5 in crossover formation was uncovered in these studies. Our results suggest that during Rhp51-dependent repair of DSBs, Rqh1-Top3 suppresses crossovers in the Rhp57-dependent pathway while Mus81-Eme1 and possibly Rqh1 promote crossovers in the Swi5-dependent pathway.","authors":"Hope JC, Cruzata LD, Duvshani A, Mitsumoto J, Maftahi M, Freyer GA","authors_abbrev":"Hope JC et al.","pubmed_publication_date":"May 2007","pubmed_entrez_date":"2007-03-14","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC409.03","SPAPB1E7.06c","SPAC3C7.03c"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:18606849","title":"CLASP regulates mitochondrial distribution in Schizosaccharomyces pombe.","citation":"J Cell Biol 2008 Jul 14;182(1):41-9","abstract":"Movement of mitochondria in Schizosaccharomyces pombe depends on their association with the dynamic, or plus ends, of microtubules, yet the molecular basis for this interaction is poorly understood. We identified mmd4 in a screen of temperature-sensitive S. pombe strains for aberrant mitochondrial morphology and distribution. Cells with the mmd4 mutation display mitochondrial aggregation near the cell ends at elevated temperatures, a phenotype similar to mitochondrial defects observed in wild-type cells after microtubule depolymerization. However, microtubule morphology and function appear normal in the mmd4 mutant. The mmd4 lesion maps to peg1(+), which encodes a microtubule-associated protein with homology to cytoplasmic linker protein-associated proteins (mammalian microtubule plus end-binding proteins). Peg1p localizes to the plus end of microtubules and to mitochondria and is recovered with mitochondria during subcellular fractionation. This mitochondrial-associated fraction of Peg1p displays properties of a peripherally associated protein. Peg1p is the first identified microtubule plus end-binding protein required for mitochondrial distribution and likely functions as a molecular link between mitochondria and microtubules.","doi":"10.1083/jcb.200712147","authors":"Chiron S, Bobkova A, Zhou H, Yaffe MP","authors_abbrev":"Chiron S et al.","pubmed_publication_date":"14 Jul 2008","pubmed_entrez_date":"2008-07-09","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20430061","title":"In vivo direct patulin-induced fluidization of the plasma membrane of fission yeast Schizosaccharomyces pombe.","citation":"Food Chem Toxicol 2010 Jul;48(7):1898-904","abstract":"Patulin is a toxic metabolite produced by various species of Penicillium, Aspergillus and Byssochlamys. In the present study, its effects on the plasma membrane of fission yeast Schizosaccharomyces pombe were investigated. The phase-transition temperature (G) of untreated cells, measured by electron paramagnetic resonance spectrometry proved to be 14.1 degrees C. Treatment of cells for 20 min with 50, 500, or 1000 microM patulin resulted in a decrease of the G value of the plasma membrane to 13.9, 10.1 or 8.7 degrees C, respectively. This change in the transition temperature was accompanied by the loss of compounds absorbing light at 260 nm. Treatment of cells with 50, 500 or 1000 microM patulin for 20 min induced the efflux of 25%, 30.5% or 34%, respectively, of these compounds. Besides its cytotoxic effects an adaptation process was observed. This is the first study to describe the direct interaction of patulin with the plasma membrane, a process which could definitely contribute to the adverse toxic effects induced by patulin.","doi":"10.1016/j.fct.2010.04.031","authors":"Horváth E, Papp G, Belágyi J, Gazdag Z, Vágvölgyi C, Pesti M","authors_abbrev":"Horváth E et al.","pubmed_publication_date":"Jul 2010","pubmed_entrez_date":"2010-05-01","publication_year":"2010","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20012578","title":"The initiation step of eukaryotic DNA replication.","citation":"Subcell Biochem 2010;50:79-104","abstract":"Eukaryotic initiation of DNA replication is a tightly regulated process. In the yeasts, S-phase-specific cyclin Cdk1 complex as well as Dfb4-Cdc7 kinase phosphorylate the initiation factors Sld2 and Sld3. These factors form a ternary complex with another initiation factor Dbp11 in their phosphorylated state, and associate with the origin of replication. This complex mediates the loading of Cdc45. A second complex called GINS and consisting of Sld5 and Psf1, 2 and 3 is also loaded onto the origin during the initiation process, in an interdependent manner with the Sld2/Sld3/Dpb11 complex. Both complexes cooperate in the recruitment of the replicative DNA polymerases, thus executing the initiation and subsequent establishment of the replication fork. Cdc45 and GINS are essential, well-conserved factors that are retained at the elongating replication fork. They form a stable helicase complex with MCM2-7 and mediate its contact to the replicative DNA polymerases. In contrast, the Sld2/Sld3/Dpb11 complex critical for the initiation is not retained by the elongating replication fork. Sld2 displays limited homology to the amino-terminal region of RecQL4 helicase, which may represent its metazoan orthologue, whereas Sld3 homologues have been identified only in fungi. Dbp11 and its fission yeast homologue Cut5 are members of a large family of BRCT-containing proteins including human TopBP1 and fruit fly Mus101. Similar principles of regulation apply also to human initiation of DNA replication, despite obvious differences in the detailed mechanisms. The regulatory initiation cascade is intimately intertwined with the cell cycle apparatus as well as the checkpoint control.","doi":"10.1007/978-90-481-3471-7_5","authors":"Pospiech H, Grosse F, Pisani FM","authors_abbrev":"Pospiech H et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2009-12-17","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR024661","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:28466","SPBC839.12","HGNC:30075"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32017882","title":"Membrane Biology: Transmembrane Helices Need to Fit the Surrounding Fat.","citation":"Curr Biol 2020 Feb 03;30(3):R122-R124","abstract":"A new study compares two sister species of fission yeast that use very different fatty acids to make membrane lipids and reveals an adaptation in transmembrane helix lengths that maintains membrane protein functions.","doi":"10.1016/j.cub.2019.12.010","authors":"Harayama T","authors_abbrev":"Harayama T","pubmed_publication_date":"03 Feb 2020","pubmed_entrez_date":"2020-02-05","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32435507","title":"Interfering with retrotransposition by two types of CRISPR effectors: Cas12a and Cas13a.","citation":"Cell Discov 2020;6:30","abstract":"CRISPRs are a promising tool being explored in combating exogenous retroviral pathogens and in disabling endogenous retroviruses for organ transplantation. The Cas12a and Cas13a systems offer novel mechanisms of CRISPR actions that have not been evaluated for retrovirus interference. Particularly, a latest study revealed that the activated Cas13a provided bacterial hosts with a \"passive protection\" mechanism to defend against DNA phage infection by inducing cell growth arrest in infected cells, which is especially significant as it endows Cas13a, a RNA-targeting CRISPR effector, with mount defense against both RNA and DNA invaders. Here, by refitting long terminal repeat retrotransposon Tf1 as a model system, which shares common features with retrovirus regarding their replication mechanism and life cycle, we repurposed CRISPR-Cas12a and -Cas13a to interfere with Tf1 retrotransposition, and evaluated their different mechanisms of action. Cas12a exhibited strong inhibition on retrotransposition, allowing marginal Tf1 transposition that was likely the result of a lasting pool of Tf1 RNA/cDNA intermediates protected within virus-like particles. The residual activities, however, were completely eliminated with new constructs for persistent crRNA targeting. On the other hand, targeting Cas13a to Tf1 RNA intermediates significantly inhibited Tf1 retrotransposition. However, unlike in bacterial hosts, the sustained activation of Cas13a by Tf1 transcripts did not cause cell growth arrest in  S. pombe , indicating that virus-activated Cas13a likely acted differently in eukaryotic cells. The study gained insight into the actions of novel CRISPR mechanisms in combating retroviral pathogens, and established system parameters for developing new strategies in treatment of retrovirus-related diseases.","doi":"10.1038/s41421-020-0164-0","authors":"Zhang N, Jing X, Liu Y, Chen M, Zhu X, Jiang J, Wang H, Li X, Hao P","authors_abbrev":"Zhang N et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-05-22","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-05-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26368543","title":"Critical Function of γH2A in S-Phase.","citation":"PLoS Genet 2015 Sep;11(9):e1005517","abstract":"Phosphorylation of histone H2AX by ATM and ATR establishes a chromatin recruitment platform for DNA damage response proteins. Phospho-H2AX (γH2AX) has been most intensively studied in the context of DNA double-strand breaks caused by exogenous clastogens, but recent studies suggest that DNA replication stress also triggers formation of γH2A (ortholog of γH2AX) in Schizosaccharomyces pombe. Here, a focused genetic screen in fission yeast reveals that γH2A is critical when there are defects in Replication Factor C (RFC), which loads proliferating cell nuclear antigen (PCNA) clamp onto duplex DNA. Surprisingly Chk1, Cds1/Chk2 and the Rad9-Hus1-Rad1 checkpoint clamp, which are crucial for surviving many genotoxins, are fully dispensable in RFC-defective cells. Immunoblot analysis confirms that Rad9-Hus1-Rad1 is not required for formation of γH2A by Rad3/ATR in S-phase. Defects in DNA polymerase epsilon, which binds PCNA in the replisome, also create an acute need for γH2A. These requirements for γH2A were traced to its role in docking with Brc1, which is a 6-BRCT-domain protein that is structurally related to budding yeast Rtt107 and mammalian PTIP. Brc1, which localizes at stalled replication forks by binding γH2A, prevents aberrant formation of Replication Protein A (RPA) foci in RFC-impaired cells, suggesting that Brc1-coated chromatin stabilizes replisomes when PCNA or DNA polymerase availability limits DNA synthesis.","doi":"10.1371/journal.pgen.1005517","authors":"Mejia-Ramirez E, Limbo O, Langerak P, Russell P","authors_abbrev":"Mejia-Ramirez E et al.","pubmed_publication_date":"Sep 2015","pubmed_entrez_date":"2015-09-15","publication_year":"2015","canto_session_key":"11dc4403d7d5569a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2017-01-12 16:23:05","canto_approved_date":"2026-01-29 15:51:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-22 21:44:17","canto_added_date":"2015-09-16 00:19:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.04c","SPAC27E2.10c","SPCC18B5.11c","SPBC947.11c","SPBC25H2.13c","SPCC4G3.05c","SPBC29A10.05","SPCC4B3.12","SPCC1259.13","SPAC14C4.13","SPBC216.05","SPCC23B6.03c","SPCC622.08c","SPBC342.05","SPBC4.04c","SPBC582.05c","SPAC13C5.07","SPAC19G12.06c","SPBC23E6.07c"],"gene_count":19,"ltp_gene_count":17,"approved_date":"2017-01-12"},{"uniquename":"PMID:27798845","title":"Spatial focalization of pheromone/MAPK signaling triggers commitment to cell-cell fusion.","citation":"Genes Dev 2016 Oct 01;30(19):2226-2239","abstract":"Cell fusion is universal in eukaryotes for fertilization and development, but what signals this process is unknown. Here, we show in Schizosaccharomyces pombe that fusion does not require a dedicated signal but is triggered by spatial focalization of the same pheromone-GPCR (G-protein-coupled receptor)-MAPK signaling cascade that drives earlier mating events. Autocrine cells expressing the receptor for their own pheromone trigger fusion attempts independently of cell-cell contact by concentrating pheromone release at the fusion focus, a dynamic actin aster underlying the secretion of cell wall hydrolases. Pheromone receptor and MAPK cascade are similarly enriched at the fusion focus, concomitant with fusion commitment in wild-type mating pairs. This focalization promotes cell fusion by immobilizing the fusion focus, thus driving local cell wall dissolution. We propose that fusion commitment is imposed by a local increase in MAPK concentration at the fusion focus, driven by a positive feedback between fusion focus formation and focalization of pheromone release and perception.","authors":"Dudin O, Merlini L, Martin SG","authors_abbrev":"Dudin O et al.","pubmed_publication_date":"01 Oct 2016","pubmed_entrez_date":"2016-11-01","publication_year":"2016","canto_session_key":"6585a50b0d18cc5e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2026-05-22 09:20:08","canto_approved_date":"2026-06-09 07:05:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-04-18 17:26:14","canto_added_date":"2016-11-02 01:15:10","annotation_curators":[{"name":"Sophie Martin","community_curator":true,"annotation_count":17,"orcid":"0000-0002-5317-2557","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC11H11.04","SPAC1D4.13","SPAC3F10.10c","SPCC1919.10c","SPBC24C6.06","SPBC1D7.05","SPAC22F3.12c","SPAC31G5.09c","SPAC20G4.02c","SPBC25B2.02c"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2026-05-22"},{"uniquename":"PMID:9736772","title":"Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human.","citation":"Hum Mol Genet 1998 Oct;7(11):1703-12","abstract":"X-linked myotubular myopathy (XLMTM) is a severe congenital muscle disorder due to mutations in the MTM1 gene. The corresponding protein, myotubularin, contains the consensus active site of tyrosine phosphatases (PTP) but otherwise shows no homology to other phosphatases. Myotubularin is able to hydrolyze a synthetic analogue of tyrosine phosphate, in a reaction inhibited by orthovanadate, and was recently shown to act on both phosphotyrosine and phosphoserine. This gene is conserved down to yeast and strong homologies were found with human ESTs, thus defining a new dual specificity phosphatase (DSP) family. We report the presence of novel members of the MTM gene family in Schizosaccharomyces pombe, Caenorhabditis elegans, zebrafish, Drosophila, mouse and man. This represents the largest family of DSPs described to date. Eight MTM-related genes were found in the human genome and we determined the chromosomal localization and expression pattern for most of them. A subclass of the myotubularin homologues lacks a functional PTP active site. Missense mutations found in XLMTM patients affect residues conserved in a Drosophila homologue. Comparison of the various genes allowed construction of a phylogenetic tree and reveals conserved residues which may be essential for function. These genes may be good candidates for other genetic diseases.","authors":"Laporte J, Blondeau F, Buj-Bello A, Tentler D, Kretz C, Dahl N, Mandel JL","authors_abbrev":"Laporte J et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-09-16","publication_year":"1998","canto_session_key":"b2ff4c933018c225","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-09 15:59:09","canto_approved_date":"2019-01-09 15:59:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-09 15:59:02","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19A8.03"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-01-09"},{"uniquename":"PMID:32735772","title":"A UPR-Induced Soluble ER-Phagy Receptor Acts with VAPs to Confer ER Stress Resistance.","citation":"Mol Cell 2020 Sep 17;79(6):963-977.e3","abstract":"Autophagic degradation of the endoplasmic reticulum (ER-phagy) is triggered by ER stress in diverse organisms. However, molecular mechanisms governing ER stress-induced ER-phagy remain insufficiently understood. Here we report that ER stress-induced ER-phagy in the fission yeast Schizosaccharomyces pombe requires Epr1, a soluble Atg8-interacting ER-phagy receptor. Epr1 localizes to the ER through interacting with integral ER membrane proteins VAPs. Bridging an Atg8-VAP association is the main ER-phagy role of Epr1, as it can be bypassed by an artificial Atg8-VAP tether. VAPs contribute to ER-phagy not only by tethering Atg8 to the ER membrane, but also by maintaining the ER-plasma membrane contact. Epr1 is upregulated during ER stress by the unfolded protein response (UPR) regulator Ire1. Loss of Epr1 reduces survival against ER stress. Conversely, increasing Epr1 expression suppresses the ER-phagy defect and ER stress sensitivity of cells lacking Ire1. Our findings expand and deepen the molecular understanding of ER-phagy.","doi":"10.1016/j.molcel.2020.07.019","authors":"Zhao D, Zou CX, Liu XM, Jiang ZD, Yu ZQ, Suo F, Du TY, Dong MQ, He W, Du LL","authors_abbrev":"Zhao D et al.","pubmed_publication_date":"17 Sep 2020","pubmed_entrez_date":"2020-08-01","publication_year":"2020","canto_session_key":"d335f8eb4efaf35d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Dan Zhao","canto_first_approved_date":"2020-08-13 14:52:12","canto_approved_date":"2025-03-04 13:45:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-08-06 04:28:15","canto_added_date":"2020-08-02 00:15:05","annotation_curators":[{"name":"Dan Zhao","community_curator":true,"annotation_count":53,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC167.01","SPBP8B7.24c","SPAC17C9.12","SPAC6B12.08","SPBC1778.01c","SPAC22H12.05c","SPBC16G5.05c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2020-08-13"},{"uniquename":"PMID:11201746","title":"Pre-meiotic S phase is linked to reductional chromosome segregation and recombination.","citation":"Nature 2001 Jan 18;409(6818):359-63","abstract":"Meiosis is initiated from G1 of the cell cycle and is characterized by a pre-meiotic S phase followed by two successive nuclear divisions. The first of these, meiosis I, differs from mitosis in having a reductional pattern of chromosome segregation. Here we show that meiosis can be initiated from G2 in fission yeast cells by ectopically activating the meiosis-inducing network. The subsequent meiosis I occurs without a pre-meiotic S phase and with decreased recombination, and exhibits a mitotic pattern of equational chromosome segregation. The subsequent meiosis II results in random chromosome segregation. This behaviour is similar to that observed in cells lacking the meiotic cohesin Rec8 (refs 3, 4), which becomes associated with chromosomes at G1/S phase, including the inner centromere, a region that is probably critical for sister-centromere orientation. If the expression of Rec8 is delayed to S phase/G2, then the centromeres behave equationally. We propose that the presence of Rec8 in chromatin is required at the pre-meiotic S phase to construct centromeres that behave reductionally and chromosome arms capable of a high level of recombination, and that this explains why meiosis is initiated from G1 of the cell cycle.","authors":"Watanabe Y, Yokobayashi S, Yamamoto M, Nurse P","authors_abbrev":"Watanabe Y et al.","pubmed_publication_date":"18 Jan 2001","pubmed_entrez_date":"2001-02-24","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9736616","title":"Apc10 and Ste9/Srw1, two regulators of the APC-cyclosome, as well as the CDK inhibitor Rum1 are required for G1 cell-cycle arrest in fission yeast.","citation":"EMBO J 1998 Sep 15;17(18):5388-99","abstract":"Many eukaryotic cells arrest the cell cycle at G1 phase upon nutrient deprivation. In fission yeast, during nitrogen starvation, cells divide twice and arrest at G1. We have isolated a novel type of sterile mutant, which undergoes one additional S phase upon starvation and, as a result, arrests at G2. Three loci (apc10, ste9/srw1 and rum1) were identified. The apc10 mutants, previously unidentified, show, in addition to sterility, temperature-sensitive growth with defects in chromosome segregation. apc10(+) is essential for viability, encodes a conserved protein (a homologue of budding yeast Apc10/Doc1) and is required for ubiquitination and degradation of mitotic B-type cyclins. Apc10 does not co-sediment with the 20S APC-cyclosome, a ubiquitin ligase for B-type cyclins, and in the apc10 mutant the 20S complex is intact, suggesting that it is a novel regulator for this complex. A subpopulation of Apc10 does co-immunoprecipitate with the anaphase-promoting complex (APC). A second gene, ste9(+)/srw1(+), encodes a member of the fizzy-related family, also regulators of the APC. Finally, Rum1 is a cyclin-dependent kinase (CDK) inhibitor which exists only in G1. The results suggest that dual downregulation of CDK, one via the APC and the other via the CDK inhibitor, is a universal mechanism that is used to arrest cell cycle progression at G1.","authors":"Kominami K, Seth-Smith H, Toda T","authors_abbrev":"Kominami K et al.","pubmed_publication_date":"15 Sep 1998","pubmed_entrez_date":"1998-09-16","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1A4.01","SPAPB2B4.03","SPBC32F12.09","SPAC17C9.01c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:4210284","title":"Rough membranes in Schizosaccharomyces pombe protoplasts.","citation":"Exp Cell Res 1974 Jul;87(1):213-8","abstract":"","authors":"Hereward FV","authors_abbrev":"Hereward FV","pubmed_publication_date":"Jul 1974","pubmed_entrez_date":"1974-07-01","publication_year":"1974","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17596184","title":"Splitting of the fission yeast septum.","citation":"FEMS Yeast Res 2007 Sep;7(6):761-70","abstract":"In cell-walled organisms, a cross wall (septum) is produced during cytokinesis, which then splits in certain organisms to allow the daughter cells to separate. The formation and the subsequent cleavage of the septum require wall synthesis and wall degradation, which need to be strictly coordinated in order to prevent cell lysis. The dividing fission yeast (Schizosaccharomyces) cell produces a three-layered septum in which the middle layer and a narrow band of the adjacent cell wall can be degraded without threatening the integrity of the separating daughter cells. This spatially very precise process requires the activity of the Agn1p 1,3-alpha-glucanase and the Eng1p 1,3-beta-glucanase, which are localized to the septum by a complex mechanism involving the formation of a septin ring and the directed activity of the exocyst system. The Sep1p-Ace2p transcription-factor cascade regulates the expression of many genes producing proteins for this complex process. Recent advances in research into the molecular mechanisms of separation and its regulation are discussed in this review.","authors":"Sipiczki M","authors_abbrev":"Sipiczki M","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-06-29","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20657649","title":"Two origins for the gene encoding alpha-isopropylmalate synthase in fungi.","citation":"PLoS One 2010 Jul 15;5(7):e11605","abstract":"The biosynthesis of leucine is a biochemical pathway common to prokaryotes, plants and fungi, but absent from humans and animals. The pathway is a proposed target for antimicrobial therapy.\nHere we identified the leuA gene encoding alpha-isopropylmalate synthase in the zygomycete fungus Phycomyces blakesleeanus using a genetic mapping approach with crosses between wild type and leucine auxotrophic strains. To confirm the function of the gene, Phycomyces leuA was used to complement the auxotrophic phenotype exhibited by mutation of the leu3+ gene of the ascomycete fungus Schizosaccharomyces pombe. Phylogenetic analysis revealed that the leuA gene in Phycomyces, other zygomycetes, and the chytrids is more closely related to homologs in plants and photosynthetic bacteria than ascomycetes or basidiomycetes, and suggests that the Dikarya have acquired the gene more recently.\nThe identification of leuA in Phycomyces adds to the growing body of evidence that some primary metabolic pathways or parts of them have arisen multiple times during the evolution of fungi, probably through horizontal gene transfer events.","doi":"10.1371/journal.pone.0011605","authors":"Larson EM, Idnurm A","authors_abbrev":"Larson EM et al.","pubmed_publication_date":"15 Jul 2010","pubmed_entrez_date":"2010-07-27","publication_year":"2010","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC3E7.16c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:1756737","title":"p80cdc25 mitotic inducer is the tyrosine phosphatase that activates p34cdc2 kinase in fission yeast.","citation":"EMBO J 1991 Dec;10(13):4301-9","abstract":"We have investigated the mechanism by which fission yeast p80cdc25 induces mitosis. The in vivo active domain was localized to the C-terminal 23 kDa of p80cdc25. This domain produced as a bacterial fusion protein (GST-cdc25) caused tyrosyl dephosphorylation and activation of immunoprecipitated p34cdc2. Furthermore, GST-cdc25 dephosphorylated both para-nitrophenyl-phosphate (pNPP) and casein phosphorylated on serine in vitro. Reaction requirements and inhibitor sensitivities were the same as those of phosphotyrosine phosphatases (PTPases). Analysis of cdc25 C-terminal domains from a variety of species revealed a conserved motif having critical residues present at the active site of PTPases. Mutation of the cdc25 Cys480 codon, corresponding to an essential cysteine in the active site of PTPases, abolished the phosphatase activity of GST-cdc25. These data indicate that cdc25 proteins define a novel subclass of eukaryotic PTPases, and strongly argue that cdc25 proteins directly dephosphorylate and activate p34cdc2 kinase to induce M-phase.","authors":"Millar JB, McGowan CH, Lenaers G, Jones R, Russell P","authors_abbrev":"Millar JB et al.","pubmed_publication_date":"Dec 1991","pubmed_entrez_date":"1991-12-01","publication_year":"1991","canto_session_key":"218f353c1d014d1b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-19 11:08:07","canto_approved_date":"2026-01-26 21:49:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-18 11:14:22","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPBC11B10.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-09-19"},{"uniquename":"PMID:18665268","title":"Mitochondrial dysfunction increases oxidative stress and decreases chronological life span in fission yeast.","citation":"PLoS One 2008 Jul 30;3(7):e2842","abstract":"Oxidative stress is a probable cause of aging and associated diseases. Reactive oxygen species (ROS) originate mainly from endogenous sources, namely the mitochondria.\nWe analyzed the effect of aerobic metabolism on oxidative damage in Schizosaccharomyces pombe by global mapping of those genes that are required for growth on both respiratory-proficient media and hydrogen-peroxide-containing fermentable media. Out of a collection of approximately 2700 haploid yeast deletion mutants, 51 were sensitive to both conditions and 19 of these were related to mitochondrial function. Twelve deletion mutants lacked components of the electron transport chain. The growth defects of these mutants can be alleviated by the addition of antioxidants, which points to intrinsic oxidative stress as the origin of the phenotypes observed. These respiration-deficient mutants display elevated steady-state levels of ROS, probably due to enhanced electron leakage from their defective transport chains, which compromises the viability of chronologically-aged cells.\nIndividual mitochondrial dysfunctions have often been described as the cause of diseases or aging, and our global characterization emphasizes the primacy of oxidative stress in the etiology of such processes.","doi":"10.1371/journal.pone.0002842","authors":"Zuin A, Gabrielli N, Calvo IA, García-Santamarina S, Hoe KL, Kim DU, Park HO, Hayles J, Ayté J, Hidalgo E","authors_abbrev":"Zuin A et al.","pubmed_publication_date":"30 Jul 2008","pubmed_entrez_date":"2008-07-31","publication_year":"2008","canto_session_key":"64f7161c76795058","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2013-12-16 17:13:57","canto_approved_date":"2021-08-18 18:44:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-12-16 17:13:25","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":180,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_18665268_phaf.tsv"}],"genes":["SPAC8C9.06c","SPAC13G7.06","SPAC1635.01","SPAC22F3.10c","SPBC27.08c","SPAC1782.11","SPCC1322.01","SPBC660.10","SPAC343.10","SPBC16H5.06","SPAC222.05c","SPAC1610.02c","SPAC13G7.07","SPAC9G1.12","SPBC25H2.08c","SPCC1672.06c","SPBC28F2.10c","SPAC6B12.12","SPAC4G9.09c","SPBC25B2.04c","SPAC31A2.11c","SPBPJ4664.01","SPCC162.05","SPAC56F8.04c","SPCC4G3.04c","SPBC119.06","SPCC188.13c","SPAC3H8.09c","SPAC14C4.03","SPBC4F6.06","SPBC106.02c","SPBC2G2.07c","SPBC26H8.12","SPAC1071.11","SPAC1687.12c","SPAC1B2.04","SPCC1672.04c","SPAC24B11.06c","SPBC336.13c","SPAC23E2.01","SPAC4D7.06c","SPBC18H10.11c","SPBC1539.03c","SPBC36.07","SPBC36.04","SPAC10F6.08c","SPBC3H7.10","SPAC10F6.01c","SPCC16A11.07","SPCC338.14","SPAC1783.07c","SPAC1071.02","SPBC25D12.06"],"gene_count":53,"ltp_gene_count":0,"approved_date":"2013-12-16"},{"uniquename":"PMID:12944482","title":"The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint.","citation":"Mol Cell Biol 2003 Sep;23(18):6564-73","abstract":"Mre11, Rad50, and Nbs1 form a conserved heterotrimeric complex that is involved in recombination and DNA damage checkpoints. Mutations in this complex disrupt the S-phase DNA damage checkpoint, the checkpoint which slows replication in response to DNA damage, and cause chromosome instability and cancer in humans. However, how these proteins function and specifically where they act in the checkpoint signaling pathway remain crucial questions. We identified fission yeast Nbs1 by using a comparative genomic approach and showed that the genes for human Nbs1 and fission yeast Nbs1 and that for their budding yeast counterpart, Xrs2, are members of an evolutionarily related but rapidly diverging gene family. Fission yeast Nbs1, Rad32 (the homolog of Mre11), and Rad50 are involved in DNA damage repair, telomere regulation, and the S-phase DNA damage checkpoint. However, they are not required for G(2) DNA damage checkpoint. Our results suggest that a complex of Rad32, Rad50, and Nbs1 acts specifically in the S-phase branch of the DNA damage checkpoint and is not involved in general DNA damage recognition or signaling.","authors":"Chahwan C, Nakamura TM, Sivakumar S, Russell P, Rhind N","authors_abbrev":"Chahwan C et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-08-29","publication_year":"2003","canto_session_key":"5a399588f4944392","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-05-11 15:33:40","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-05-11 15:33:35","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":45,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPBC6B1.09c","SPCC23B6.03c","SPBC216.05","SPAC13C5.07"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-05-11"},{"uniquename":"PMID:29149597","title":"Structural Basis for Shelterin Bridge Assembly.","citation":"Mol Cell 2017 Nov 16;68(4):698-714.e5","abstract":"Telomere elongation through telomerase enables chromosome survival during cellular proliferation. The conserved multifunctional shelterin complex associates with telomeres to coordinate multiple telomere activities, including telomere elongation by telomerase. Similar to the human shelterin, fission yeast shelterin is composed of telomeric sequence-specific double- and single-stranded DNA-binding proteins, Taz1 and Pot1, respectively, bridged by Rap1, Poz1, and Tpz1. Here, we report the crystal structure of the fission yeast Tpz1 475-508 -Poz1-Rap1 467-496  complex that provides the structural basis for shelterin bridge assembly. Biochemical analyses reveal that shelterin bridge assembly is a hierarchical process in which Tpz1 binding to Poz1 elicits structural changes in Poz1, allosterically promoting Rap1 binding to Poz1. Perturbation of the cooperative Tpz1-Poz1-Rap1 assembly through mutation of the \"conformational trigger\" in Poz1 leads to unregulated telomere lengthening. Furthermore, we find that the human shelterin counterparts TPP1-TIN2-TRF2 also assemble hierarchically, indicating cooperativity as a conserved driving force for shelterin assembly.","doi":"10.1016/j.molcel.2017.10.032","authors":"Kim JK, Liu J, Hu X, Yu C, Roskamp K, Sankaran B, Huang L, Komives EA, Qiao F","authors_abbrev":"Kim JK et al.","pubmed_publication_date":"16 Nov 2017","pubmed_entrez_date":"2017-11-18","publication_year":"2017","canto_session_key":"c2300e5c031f17ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Feng Qiao","canto_first_approved_date":"2017-12-29 22:44:00","canto_approved_date":"2025-09-02 18:47:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-26 22:04:06","canto_added_date":"2017-11-19 01:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Feng Qiao","community_curator":true,"annotation_count":129,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.13c","SPAC6F6.16c","SPBC1778.02","SPAC16A10.07c","SPCC188.07"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2017-12-29","pdb_entries":[{"pdb_id":"5we0","gene_chains":[{"gene_uniquename":"SPAC19G12.13c","chain":"A/D/G/J","position":"2-249"},{"gene_uniquename":"SPAC6F6.16c","chain":"B/E/H/K","position":"476-508"},{"gene_uniquename":"SPBC1778.02","chain":"C/F/I/L","position":"467-496"}],"title":"Structural Basis for Shelterin Bridge Assembly","entry_authors":"Kim J-K,Liu J,Hu X,Yu C,Roskamp K,Sankaran B,Huang L,Komives E-A,Qiao F","entry_authors_abbrev":"Kim J-K et al.","reference_uniquename":"PMID:29149597","experimental_method":"X-ray","resolution":"2.3"},{"pdb_id":"5we1","gene_chains":[{"gene_uniquename":"SPAC19G12.13c","chain":"A/C","position":"30-249"},{"gene_uniquename":"SPAC6F6.16c","chain":"B/D","position":"476-508"}],"title":"Structural Basis for Shelterin Bridge Assembly","entry_authors":"Kim J-K,Liu J,Hu X,Yu C,Roskamp K,Sankaran B,Huang L,Komives E-A,Qiao F","entry_authors_abbrev":"Kim J-K et al.","reference_uniquename":"PMID:29149597","experimental_method":"X-ray","resolution":"3.202"},{"pdb_id":"5we2","gene_chains":[{"gene_uniquename":"SPAC19G12.13c","chain":"A/C","position":"2-249"},{"gene_uniquename":"SPAC6F6.16c","chain":"B/D","position":"476-508"},{"gene_uniquename":"SPBC1778.02","chain":"F","position":"467-496"}],"title":"Structural Basis for Telomere Length Regulation by the Shelterin Bridge","entry_authors":"Kim J-K,Liu J,Hu X,Sankaran B,Qiao F","entry_authors_abbrev":"Kim J-K et al.","reference_uniquename":"PMID:29149597","experimental_method":"X-ray","resolution":"2.5"}]},{"uniquename":"PMID:6132459","title":"In vivo and in vitro mutagenicity studies of a possible carcinogen, trichloroethylene, and its two stabilizers, epichlorohydrin and 1,2-epoxybutane.","citation":"Teratog Carcinog Mutagen 1983;3(1):75-87","abstract":"In vivo and in vitro methodologies that have employed the yeast Schizosaccharomyces pombe as genetic indicator have been utilized to investigate the mutagenicity of two trichloroethylene (TCE) samples of pure and technical grade. Mutagenicity assays were also performed on two stabilizers contained in the technical grade sample: epichlorohydrin and 1,2-epoxybutane. In the in vitro studies a metabolic conversion system was supplied by liver homogenate (S-9) from mice and rats untreated and pretreated with phenobarbital and/or beta-naphthoflavone. Up to highly toxic doses of TCE were applied to growing and stationary-phase yeast cells. In the in vivo studies two different host-mediated assays, intrasanguineous and intraperitoneal methodologies, were performed on different mice breeds treated by oral administration. Epichlorohydrin and epoxybutane were tested singly or combined in a mixture of the same ratio as in the technical grade TCE sample. Both TCE samples gave negative results for in vivo and in vitro assays, whereas the two contaminants were found mutagenic only in vitro. The high toxicity of the technical TCE sample did not allow us to reach concentrations containing effective levels of its two additives.","authors":"Rossi AM, Migliore L, Barale R, Loprieno N","authors_abbrev":"Rossi AM et al.","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-01-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SP37354","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2714252","title":"Mapping the double-strand breaks at the mating-type locus in fission yeast by genomic sequencing.","citation":"EMBO J 1989 Jan;8(1):269-76","abstract":"In fission yeast mating-type switching is initiated by the formation of a double-strand DNA break at the mating-type locus. A prerequisite for generation of the break is some 'imprinting' of the DNA in the previous cell cycle. We have used the technique of genomic sequencing to map the position of the break directly on chromosomal DNA cleaved in vivo. On one strand the break is situated very close to the right-hand border of the expressed mat1 cassette. Cells of opposite mating type, P and M, have their breaks at slightly different positions on this strand. On the other DNA strand of both alleles the ends are probably masked by tightly bound proteins and therefore the precise nature of the break could not be determined. Since the break is stable throughout the cell cycle, these proteins may function in vivo to confer structural stability on the chromosomes having the break. The implications of these findings for models of mating-type switching are discussed.","authors":"Nielsen O, Egel R","authors_abbrev":"Nielsen O et al.","pubmed_publication_date":"Jan 1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011953","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16866873","title":"Actin-capping protein is involved in controlling organization of actin cytoskeleton together with ADF/cofilin, profilin and F-actin crosslinking proteins in fission yeast.","citation":"Genes Cells 2006 Aug;11(8):893-905","abstract":"Actin-capping protein (CP) is a heterodimeric protein which is expressed in various eukaryotic cells. CP binds to the barbed end of the actin filaments in vitro and inhibits both the association and dissociation of actin monomers at this end. However, the cellular role of CP has not been uncovered. Here we investigated the function of CP in fission yeast cells. The fission yeast CP is composed of Acp1 and Acp2. It was found that Acp2 accumulated as cortical dots at the cell ends during interphase and the mid-region of mitotic cells, which disappeared in the absence of Acp1 or F-actin. Acp1 and Acp2, when co-over-expressed, decreased F-actin structures in cells, and cytokinesis was often interrupted in these cells. On the other hand, disruption of one of the CP genes affected the distribution of F-actin patches at cell ends and decreased the rate of actin depolymerization in vivo. Moreover, genetic analysis showed that CP controls actin dynamics together with ADF/cofilin and profilin. In addition, CP is likely involved in assembling the F-actin contractile ring and F-actin patch with F-actin-crosslinking proteins.","authors":"Nakano K, Mabuchi I","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-07-27","publication_year":"2006","canto_session_key":"b85e9f77ce708b04","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-09-14 16:49:05","canto_approved_date":"2026-01-22 12:14:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-14 16:48:54","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":80,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.08","SPAC4F8.13c","SPAC4A8.05c","SPBC1778.06c","SPBC21.06c","SPAC27F1.02c","SPCC895.05","SPAC631.01c","SPAC20G8.05c","SPCC645.05c","SPBC146.13c","SPAC20G4.06c","SPAC12B10.07","SPAC4A8.15c","SPAC1F5.04c","SPAC15A10.08","SPAC630.03"],"gene_count":17,"ltp_gene_count":8,"approved_date":"2017-09-14"},{"uniquename":"PMID:1496556","title":"Developmental choices in mating-type interconversion in fission yeast.","citation":"Trends Genet 1992 Jun;8(6):208-13","abstract":"Fission yeast cells follow a specific pattern of mating (cell) type switching in single cell pedigrees. Asymmetric cell divisions producing sisters of different developmental fates result from inheritance of specific parental DNA strands according to the classical model of semiconservative replication and segregation.","authors":"Klar AJ","authors_abbrev":"Klar AJ","pubmed_publication_date":"Jun 1992","pubmed_entrez_date":"1992-06-01","publication_year":"1992","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12512257","title":"From yeast genetics to biotechnology.","citation":"Acta Microbiol Immunol Hung 2002;49(4):483-91","abstract":"Roots of classical yeast genetics go back to the early work of Lindegreen in the 1930s, who studied thallism, sporulation and inheritance of wine yeast strains belonging to S. cerevisiae. Consequent mutation and hybridization of heterothallic S. cerevisae strains resulted in the discovery of life cycle and mating type system, as well as construction of the genetic map. Elaboration of induced mutation and controlled hybridization of yeast strains opened up new possibilities for the genetic analysis of technologically important properties and for the production of improved industrial strains, but a big drawback was the widely different genetic properties of laboratory and industrial yeast strains. Genetic analysis and mapping of industrial strains were generally hindered because of homothallism, poor sporulation and/or low spore viability of brewing and wine yeast strains [1, 2]. In spite of this, there are a few examples of the application of sexual hybridization in the study of genetic control of important technological properties, e.g. sugar utilization, flocculation and flavor production in brewing yeast strains [3] or in the improvement of ethanol producing S. cerevisiae strains [4]. Rare mating and application of karyogamy deficient (kar-) mutants also proved useful in strain improvement [5]. Importance of yeasts in biotechnology is enormous. This includes food and beverage fermentation processes where a wide range of yeast species are playing role, but S. cerevisiae is undoubtedly the most important species among them. New biotechnology is aiming to improve these technologies, but besides this, a completely new area of yeast utilization has been emerged, especially in the pharmaceutical and medical areas. Without decreasing the importance of S. cerevisiae, numerous other yeast species, e.g. Kluyveromyces lactis, Hansenula polymorpha, Pichia pastoris, Schizosaccharomyces pombe and Yarrowia lipolytica have gained increasing potentialities in the modern fermentation biotechnology [6]. Developments in yeast genetics, biochemistry, physiology and process engineering provided bases of rapid development in modern biotechnology, but elaboration of the recombinant DNA technique is far the most important milestone in this field. Other molecular genetic techniques, as molecular genotyping of yeast strains proved also very beneficial in yeast fermentation technologies, because dynamics of both the natural and inoculated yeast biota could be followed by these versatile DNA-based techniques.","authors":"Maráz A","authors_abbrev":"Maráz A","pubmed_publication_date":"2002","pubmed_entrez_date":"2003-01-07","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8590465","title":"As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe.","citation":"Curr Genet 1995 Jul;28(2):138-49","abstract":"The organisation of the URA1 gene of Schizosaccharomyces pombe was determined from the entire cDNA cloned by the transformation of an ATCase-deficient strain of Saccharomyces cerevisiae. The URA1 gene encodes the bifunctional protein GLNase/CPSase-ATCase which catalyses the first two steps of the pyrimidine biosynthesis pathway. The complete nucleotide sequence of the URA1 cDNA was elucidated and the deduced amino-acid sequence was used to define four domains in the protein; three functional domains, corresponding to GLNase (glutamine amidotransferase), CPSase (carbamoylphosphate synthetase) and ATCase (aspartate transcarbamoylase) activities, and one cryptic DHOase (dihydroorotase) domain. Genetic investigations confirmed that both GLNase/CPSase and ATCase activities are carried out by the same polypeptide. They are also both feedback-inhibited by UTP (uridine triphosphate). Its organization and regulation indicate that the S. pombe URA1 gene product appears very similar to the S. cerevisiae URA2 gene product.","authors":"Lollier M, Jaquet L, Nedeva T, Lacroute F, Potier S, Souciet JL","authors_abbrev":"Lollier M et al.","pubmed_publication_date":"Jul 1995","pubmed_entrez_date":"1995-07-01","publication_year":"1995","canto_session_key":"85e6122e0094ad3d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-06-29 08:39:22","canto_approved_date":"2025-12-05 19:13:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-29 08:38:38","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22G7.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-06-29"},{"uniquename":"PMID:2780299","title":"Nucleotide sequence of the gene encoding the small ribosomal RNA in the mitochondrial genome of the fission yeast Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1989 Aug 25;17(16):6730","abstract":"","authors":"Trinkl H, Lang BF, Wolf K","authors_abbrev":"Trinkl H et al.","pubmed_publication_date":"25 Aug 1989","pubmed_entrez_date":"1989-08-25","publication_year":"1989","canto_session_key":"5aa7eb236ab48899","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 14:53:13","canto_approved_date":"2019-01-07 14:53:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 14:53:06","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"PMID:21984210","title":"Structure of an aprataxin-DNA complex with insights into AOA1 neurodegenerative disease.","citation":"Nat Struct Mol Biol 2011 Oct 09;18(11):1189-95","abstract":"DNA ligases finalize DNA replication and repair through DNA nick-sealing reactions that can abort to generate cytotoxic 5'-adenylation DNA damage. Aprataxin (Aptx) catalyzes direct reversal of 5'-adenylate adducts to protect genome integrity. Here the structure of a Schizosaccharomyces pombe Aptx-DNA-AMP-Zn(2+) complex reveals active site and DNA interaction clefts formed by fusing a histidine triad (HIT) nucleotide hydrolase with a DNA minor groove-binding C(2)HE zinc finger (Znf). An Aptx helical 'wedge' interrogates the base stack for sensing DNA ends or DNA nicks. The HIT-Znf, the wedge and an '[F/Y]PK' pivot motif cooperate to distort terminal DNA base-pairing and direct 5'-adenylate into the active site pocket. Structural and mutational data support a wedge-pivot-cut HIT-Znf catalytic mechanism for 5'-adenylate adduct recognition and removal and suggest that mutations affecting protein folding, the active site pocket and the pivot motif underlie Aptx dysfunction in the neurodegenerative disorder ataxia with oculomotor apraxia 1 (AOA1).","doi":"10.1038/nsmb.2146","authors":"Tumbale P, Appel CD, Kraehenbuehl R, Robertson PD, Williams JS, Krahn J, Ahel I, Williams RS","authors_abbrev":"Tumbale P et al.","pubmed_publication_date":"09 Oct 2011","pubmed_entrez_date":"2011-10-11","publication_year":"2011","canto_session_key":"af26dae3243e8f93","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-08-12 09:45:51","canto_approved_date":"2020-01-23 13:19:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-12 09:45:44","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-08-12","pdb_entries":[{"pdb_id":"3szq","gene_chains":[{"gene_uniquename":"SPCC18.09c","chain":"A","position":"31-232"}],"title":"Structure of an S. pombe APTX/DNA/AMP/Zn complex","entry_authors":"Tumbale P,Krahn J,Williams RS","entry_authors_abbrev":"Tumbale P et al.","reference_uniquename":"PMID:21984210","experimental_method":"X-ray","resolution":"2.353"}]},{"uniquename":"PMID:27934694","title":"Metabolomic Analysis of Schizosaccharomyces pombe: Sample Preparation, Detection, and Data Interpretation.","citation":"Cold Spring Harb Protoc 2016 Dec 01;2016(12)","abstract":"Metabolomics is a modern field of chemical biology that strives to simultaneously quantify hundreds of cellular metabolites. Techniques for metabolomic analysis in Schizosaccharomyces pombe have only recently been developed. Here we introduce methods that provide a complete workflow for metabolomic analysis in S. pombe Based on available literature, we estimate the yeast metabolome to comprise on the order of several thousand different metabolites. We discuss the feasibility of extraction and detection of such a large number of metabolites, and the influences of various parameters on the results. Among the parameters addressed are cell cultivation conditions, metabolite extraction techniques, and detection and quantification methods. Further, we provide recommendations on data management and data processing for metabolomic experiments, and describe possible pitfalls regarding the interpretation of metabolomic data. Finally, we briefly discuss potential future developments of this technique.","doi":"10.1101/pdb.top079921","authors":"Pluskal T, Yanagida M","authors_abbrev":"Pluskal T et al.","pubmed_publication_date":"01 Dec 2016","pubmed_entrez_date":"2016-12-10","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-12-11 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17870620","title":"Molecular phylogenetics of ascomycotal adhesins--a novel family of putative cell-surface adhesive proteins in fission yeasts.","citation":"Fungal Genet Biol 2008 Apr;45(4):485-97","abstract":"In this work, we identify a family of putative adhesins in the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. The members of this family share a conserved tandem repeat related to those found in the Candida albicans Als family of adhesins. Unlike previously characterised adhesins that possess conserved ligand-binding domains at the N-terminus, this group of proteins carry ligand-binding domains at their C-termini. We demonstrate that one such domain--the uncharacterised GLEYA domain, is related to the lectin-like ligand-binding domain found in the Saccharomyces cerevisiae Flo proteins. Unlike the Flo and Als proteins, the fission yeast adhesins do not contain detectable glycosyl phosphatidyl inositol (GPI) membrane anchor signals to mediate their attachment to the cell wall, which may suggest a novel cell wall attachment mechanism. Further sequence analysis identified several putative adhesins in the sub-phylum of Pezizomycotina, where only a few adhesins have been described to date.","authors":"Linder T, Gustafsson CM","authors_abbrev":"Linder T et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2007-09-18","publication_year":"2008","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC359.04c","SPBC21D10.06c","SPAC1F8.06","SPBC1348.08c","SPAC977.07c","SPCC188.09c","SPBC947.04","SPAC186.01","SPAPB2C8.01"],"gene_count":9,"ltp_gene_count":0},{"uniquename":"PMID:4717522","title":"Cell division in yeasts: movement of organelles associated with cell plate growth of Schizosaccharomyces pombe.","citation":"J Bacteriol 1973 Jul;115(1):358-66","abstract":"Electron microscopy of dividing fission yeast cells shows establishment of an annular rudiment (AR) of electron-transparent material under the old cell wall as the first sign of elaboration of the cell plate. The AR grows centripetally, finally closing at the mid-point of the cell. During the inward growth of the AR it is thickened by addition of denser material which becomes the scar plug after fission; the electron-transparent material is lost at fission. Lying always between the cytoplasmic membrane and the cell wall is a dark layer of variable thickness. This layer becomes markedly thickened into a fillet at the base of the centripetally growing cell plate. The fission process begins after the cell plate is completely elaborated. One striking feature of fission is the migration of dense material from the fillet at the base of the cell plate outwardly through the matrix of the cell wall to its final resting place as a dark ring, a \"fuscannel,\" adjacent to the fission scar. The inclusion of Golgi bodies in many sections suggests their involvement in cell plate elaboration, presumably through production of the dense bodies which are seen to fuse with the dark layer proximal to the growing cell plate.","authors":"Johnson BF, Yoo BY, Calleja GB","authors_abbrev":"Johnson BF et al.","pubmed_publication_date":"Jul 1973","pubmed_entrez_date":"1973-07-01","publication_year":"1973","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38405799","title":"A systematic quantitative approach comprehensively defines domain-specific functional pathways linked to  Schizosaccharomyces pombe  heterochromatin regulation.","citation":"bioRxiv 2024 Feb 15;","abstract":"Heterochromatin plays a critical role in regulating gene expression and maintaining genome integrity. While structural and enzymatic components have been linked to heterochromatin establishment, a comprehensive view of the underlying pathways at diverse heterochromatin domains remains elusive. Here, we developed a systematic approach to identify factors involved in heterochromatin silencing at pericentromeres, subtelomeres, and the silent mating type locus in  Schizosaccharomyces pombe  . Using quantitative measures, iterative genetic screening, and domain-specific heterochromatin reporters, we identified 369 mutants with different degrees of reduced or enhanced silencing. As expected, mutations in the core heterochromatin machinery globally decreased silencing. However, most other mutants exhibited distinct qualitative and quantitative profiles that indicate domain-specific functions. For example, decreased mating type silencing was linked to mutations in heterochromatin maintenance genes, while compromised subtelomere silencing was associated with metabolic pathways. Furthermore, similar phenotypic profiles revealed shared functions for subunits within complexes. We also discovered that the uncharacterized protein Dhm2 plays a crucial role in maintaining constitutive and facultative heterochromatin, while its absence caused phenotypes akin to DNA replication-deficient mutants. Collectively, our systematic approach unveiled a landscape of domain-specific heterochromatin regulators controlling distinct states and identified Dhm2 as a previously unknown factor linked to heterochromatin inheritance and replication fidelity.","doi":"10.1101/2024.02.13.579970","authors":"Muhammad A, Sarkadi Z, van Emden T, Mazumder A, Capella M, Fekete G, Sreechakram VNS, Al-Sady B, Papp B, Barrales RR, Braun S","authors_abbrev":"Muhammad A et al.","pubmed_publication_date":"15 Feb 2024","pubmed_entrez_date":"2024-02-26","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-02-27 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15157891","title":"Tandem affinity purification and identification of protein complex components.","citation":"Methods 2004 Jul;33(3):239-44","abstract":"As with the budding yeast Saccharomyces cerevisiae, the completion of the Schizosaccharomyces pombe genome sequence has opened new opportunities to investigate the functional organization of a eukaryotic cell. These include analysis of gene expression patterns, comprehensive gene knockout and synthetic lethal screens, global protein localization analysis, and direct protein interaction mapping. We describe here the tandem affinity purification or TAP approach combined with DALPC mass spectrometry to identify components of protein complexes as we have applied it to S. pombe. This approach can theoretically be applied to the entire proteome as has been done in S. cerevisiae to gain insight into functional protein assemblies and to elucidate functions of uncharacterized proteins.","authors":"Gould KL, Ren L, Feoktistova AS, Jennings JL, Link AJ","authors_abbrev":"Gould KL et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-05-26","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18031226","title":"The role of Schizosaccharomyces pombe SUMO ligases in genome stability.","citation":"Biochem Soc Trans 2007 Dec;35(Pt 6):1379-84","abstract":"SUMOylation is a post-translational modification that affects a large number of proteins, many of which are nuclear. While the role of SUMOylation is beginning to be elucidated, it is clear that understanding the mechanisms that regulate the process is likely to be important. Control of the levels of SUMOylation is brought about through a balance of conjugating and deconjugating activities, i.e. of SUMO (small ubiquitin-related modifier) conjugators and ligases versus SUMO proteases. Although conjugation of SUMO to proteins can occur in the absence of a SUMO ligase, it is apparent that SUMO ligases facilitate the SUMOylation of specific subsets of proteins. Two SUMO ligases in Schizosaccharomyces pombe, Pli1 and Nse2, have been identified, both of which have roles in genome stability. We report here on a comparison between the properties of the two proteins and discuss potential roles for the proteins.","authors":"Watts FZ, Skilton A, Ho JC, Boyd LK, Trickey MA, Gardner L, Ogi FX, Outwin EA","authors_abbrev":"Watts FZ et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-11-23","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC126.02c","SPBC16G5.12c","SPAC2G11.12","SPBC1703.14c","SPAC30D11.10","SPCC5E4.06","SPAC16A10.06c","SPAC1687.05"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:8861202","title":"The sxa2-dependent inactivation of the P-factor mating pheromone in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Microbiol 1996 Apr;20(1):35-42","abstract":"Haploid cells of the fission yeast Schizosaccharomyces pombe exist in one of two mating types, referred to as M and P. Conjugation occurs between cells of opposite mating type and is controlled by the reciprocal action of diffusible pheromones. Loss of function of the sxa2 gene in M cells causes hypersensitivity to the P-factor mating pheromone and a reduction in mating efficiency. Here we demonstrate the secretion of an sxa2-dependent carboxypeptidase that inactivates P-factor by removal of the C-terminal leucine residue.","authors":"Ladds G, Rasmussen EM, Young T, Nielsen O, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_session_key":"ce4cb6da2a1e760","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-03-29 13:30:25","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-07-10 08:06:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.06","SPAC1296.03c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-07-10"},{"uniquename":"PMID:33386485","title":"Spatial sequestration of misfolded proteins as an active chaperone-mediated process during heat stress.","citation":"Curr Genet 2021 Apr;67(2):237-243","abstract":"Under thermal stress, different protein quality control (PQC) strategies are activated to maintain an intact proteome, which may vary from one model system to another. Hence thermo-sensitive proteins that lose their active conformation might be refolded with the aid of chaperones or removed by the ubiquitin-proteasome system or the process of autophagy. We have recently developed thermo-sensitive reporters to study PQC in fission yeast and shown the relevance of a third adaptation strategy: the sequestration of misfolded proteins into inclusions which will prevent a rapid degradation and allow the refolding once stress ends. These protein inclusions, protein aggregate centers (PACs), contain a broad spectrum of misfolding/aggregation-prone proteins and chaperones involved in their assembly or dissolution. The chaperone couple Mas5/Ssa2 plays a crucial role in PAC formation, whereas the Hsp104 chaperone promotes their disassembly. The absence of aggregates observed in cells lacking Mas5 could be also explained by the activation of the transcription factor Hsf1 and the induction of chaperone genes, we have excluded this possibility here demonstrating that increased Hsf1 activity and the subsequent overexpression of chaperones do not prevent the assembly of protein aggregates. Protein deposition at certain locations also constitutes a tactic to inactivate proteins temporally. This is the case of Pyp1, the main phosphatase of the stress response kinase Sty1. Upon stress imposition, misfolded Pyp1 is sequestered into cytosolic protein foci while active Sty1 at the nucleus switches on the transcriptional response. In conclusion, we propose that the assembly of aggregation-like foci, PACs in fission yeast, is a crucial PQC strategy during heat stress, and that the Hsp40 chaperone Mas5 is required for PAC assembly and connects physiological and heat-shock triggered PQC.","doi":"10.1007/s00294-020-01135-2","authors":"Boronat S, Cabrera M, Hidalgo E","authors_abbrev":"Boronat S et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2021-01-02","publication_year":"2021","canto_session_key":"50f15c1a29c5c86a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Susanna Boronat","canto_first_approved_date":"2021-07-07 12:30:35","canto_approved_date":"2024-06-28 09:24:11","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-06-27 16:53:12","canto_added_date":"2021-01-04 01:15:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Susanna Boronat","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.02c","SPBC1734.11","SPAC26F1.10c","SPBC16D10.08c","SPAC2E12.02","SPAC24B11.06c","SPAC1F7.04"],"gene_count":7,"ltp_gene_count":2,"approved_date":"2021-07-07"},{"uniquename":"PMID:16920610","title":"Molecular biology: silencing unlimited.","citation":"Curr Biol 2006 Aug 22;16(16):R635-8","abstract":"Heterochromatin domains are essential for normal chromosome functions. The Eri1 ribonuclease is a negative regulator of the RNA interference machinery; recent studies have shown that, in fission yeast lacking Eri1, heterochromatin formation is more promiscuous.","authors":"Almeida R, Buscaino A, Allshire RC","authors_abbrev":"Almeida R et al.","pubmed_publication_date":"22 Aug 2006","pubmed_entrez_date":"2006-08-22","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35024575","title":"Isolated THATCH domain of End4 is unable to bind F-actin independently in the fission yeast  Schizosaccharomyces pombe .","citation":"MicroPubl Biol 2022;2022","abstract":"Clathrin mediated endocytosis (CME) in the fission yeast  Schizosaccharomyces pombe  critically depends on the connection between the lipid membrane and F-actin. The fission yeast endocytic protein End4 (homologous to Sla2 in budding yeast and HIP1R in human) contains a N-terminal domain that binds to PIP2 on the membrane, and a C-terminal THATCH domain that is postulated to be a binding partner of F-actin  in vivo . Purified THATCH domain of the budding yeast Sla2, however, shows low affinity to F-actin  in vitro . We tested if isolated THATCH domain still has low affinity to F-actin  in vivo , using TEV protease (TEVp)-mediated protein cleaving to separate the THATCH domain from the rest of End4. Our results indicate that the isolated THATCH domain of End4 is unable to bind F-actin independently  in vivo , consistent with the low affinity of the THATCH domain to F-actin measured from  in vitro  binding assays.","doi":"10.17912/micropub.biology.000508","authors":"Ren Y, Berro J","authors_abbrev":"Ren Y et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-01-13","publication_year":"2022","canto_session_key":"93cc304cf9878a34","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Julien Berro","canto_first_approved_date":"2022-07-01 07:26:27","canto_approved_date":"2022-07-01 07:26:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-06-30 16:22:33","canto_added_date":"2022-01-15 01:15:04","annotation_curators":[{"name":"Julien Berro","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-07-01"},{"uniquename":"EMBL:AU007395","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10805785","title":"Sid4p is required to localize components of the septation initiation pathway to the spindle pole body in fission yeast.","citation":"Proc Natl Acad Sci U S A 2000 May 09;97(10):5249-54","abstract":"A mutation in the Schizosaccharomyces pombe sid4(+) (septation initiation defective) gene was isolated in a screen for mutants defective in cytokinesis. We have cloned sid4(+) and have found that sid4(+) encodes a previously unknown 76.4-kDa protein that localizes to the spindle pole body (SPB) throughout the cell cycle. Sid4p is required for SPB localization of key regulators of septation initiation, including the GTPase Spg1p, the protein kinase Cdc7p, and the GTPase-activating protein Byr4p. An N-terminally truncated Sid4p mutant does not localize to SPBs and when overproduced acts as a dominant-negative mutant by titrating endogenous Sid4p and Spg1p from the SPB. Conversely, the Sid4p N-terminal 153 amino acids are sufficient for SPB localization. Biochemical studies demonstrate that Sid4p interacts with itself, and yeast two-hybrid analysis shows that its self-interaction domain lies within the C-terminal half of the protein. Our data indicate that Sid4p SPB localization is a prerequisite for the execution of the Spg1p signaling cascade.","authors":"Chang L, Gould KL","authors_abbrev":"Chang L et al.","pubmed_publication_date":"09 May 2000","pubmed_entrez_date":"2000-05-11","publication_year":"2000","canto_session_key":"e45f4e0f49c95352","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-12-29 16:53:54","canto_approved_date":"2021-11-03 19:40:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-29 16:53:44","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.11c","SPAC24B11.11c","SPAC6F6.08c","SPAC222.10c","SPBC21.06c","SPBC24C6.07","SPBC244.01c","SPAC20G8.05c","SPAC1565.06c","SPAC9G1.09"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2020-12-29"},{"uniquename":"EMBL:AU009960","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9366254","title":"Fission yeast dihydrolipoamide dehydrogenase gene is involved in G1/S cell cycle progression.","citation":"Biochim Biophys Acta 1997 Oct 11;1358(3):229-39","abstract":"Using functional complementation with a Schizosaccharomyces pombe genomic library, we have isolated a clone complementing a G1/S phase progression defective mutant. The newly isolated temperature-sensitive mutant, cyj150, showed elongated morphology at a restrictive temperature of 36 degrees C and DNA content analysis of the mutant indicated a defect in cell cycle progression at the G1/S phase. Sequence analysis of the genomic and cDNA clones complementing this elongated phenotype at 36 degrees C show that it encodes a protein that has 50% amino acid identity with dihydrolipoamide dehydrogenase from Saccharomyces cerevisiae and garden pea. Alignment of the deduced amino acid sequence of S. pombe dihydrolipoamide dehydrogenase (dld1+) with glutathione reductase and mercuric reductase revealed extensive homologies throughout the primary sequence and protein structure, and contained amino acid sequences of the active site region conserved from prokaryote to higher eukaryote. Gene disruption and tetrad analysis showed that dld1+ is an essential gene for cell viability. Northern analysis indicates that transcriptional expression of this gene is not fluctuated according to the cell cycle. However, it is certain that malfunction of this Dld1 protein blocks the progression of cell cycle from G1 to S phase. The sequence of the dld1+ gene is available in EMBL/GenBank under Accession Number L40360.","authors":"Jang YJ, Chung KS, Park C, Yoo HS","authors_abbrev":"Jang YJ et al.","pubmed_publication_date":"11 Oct 1997","pubmed_entrez_date":"1997-11-20","publication_year":"1997","canto_session_key":"12bdf99ec7ed84ce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-04-13 11:40:29","canto_approved_date":"2024-03-19 07:31:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-14 15:34:23","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1002.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-04-13"},{"uniquename":"PMID:27466272","title":"A Genetic Screen for Fission Yeast Gene Deletion Mutants Exhibiting Hypersensitivity to Latrunculin A.","citation":"G3 (Bethesda) 2016 Oct 13;6(10):3399-3408","abstract":"Fission yeast cells treated with low doses of the actin depolymerizing drug, latrunculin A (LatA), delay entry into mitosis via a mechanism that is dependent on both the Clp1p and Rad24p proteins. During this delay, cells remain in a cytokinesis-competent state that is characterized by continuous repair and/or reestablishment of the actomyosin ring. In this manner, cells ensure the faithful completion of the preceding cytokinesis in response to perturbation of the cell division machinery. To uncover other genes with a role in this response, or simply genes with roles in adapting to LatA-induced stress, we carried out a genome-wide screen and identified a group of 38 gene deletion mutants that are hyper-sensitive to the drug. As expected, we found genes affecting cytokinesis and/or the actin cytoskeleton within this set (ain1, acp2, imp2). We also identified genes with roles in histone modification (tra1, ngg1), intracellular transport (apl5, aps3), and glucose-mediated signaling (git3, git5, git11, pka1, cgs2). Importantly, while the identified gene deletion mutants are prone to cytokinesis failure in the presence of LatA, they are nevertheless fully capable of cell division in the absence of the drug. These results indicate that fission yeast cells make use of a diverse set of regulatory modules to counter abnormal cytoskeletal perturbations, and furthermore, that these modules act redundantly to ensure cell survival and proliferation.","doi":"10.1534/g3.116.032664","authors":"Asadi F, Michalski D, Karagiannis J","authors_abbrev":"Asadi F et al.","pubmed_publication_date":"13 Oct 2016","pubmed_entrez_date":"2016-07-29","publication_year":"2016","canto_session_key":"f69c11e3ebdf6a8f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-30 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21948086","title":"DNA replication induces compositional biases in yeast.","citation":"Mol Biol Evol 2012 Mar;29(3):893-904","abstract":"Asymmetries intrinsic to the process of DNA replication are expected to cause differences in the substitution patterns of the leading and the lagging strands and to induce compositional biases. These biases have been detected in the majority of eubacterial genomes but rarely in eukaryotes. Only in the human genome, the activity of a minority of replication origins seems to generate compositional biases. In this work, we provide evidence for replication-associated GC and TA skews in the genomes of two yeast species, Saccharomyces cerevisiae and Kluyveromyces lactis, whereas the data for the Schizosaccharomyces pombe genome are less conclusive. In contrast with the genomes of Homo sapiens and of the majority of eubacteria, the leading strand is enriched in cytosine and adenine in both S. cerevisiae and K. lactis. We observed significant variations across the interorigin intervals of several substitution rates in the S. cerevisiae lineage since its divergence from S. paradoxus. We also found that the S. cerevisiae genome is far from compositional equilibrium and that its present compositional biases are due to substitution rates operating before its divergence from S. paradoxus. Finally, we observed that replication and transcription tend to be cooriented in the S. cerevisiae genome, especially for genes encoding subunits of protein complexes. Taken together, our results suggest that replication-related compositional biases may be a feature of many eukaryotic genomes despite the stochastic nature of the firing of replication origins in these genomes.","doi":"10.1093/molbev/msr240","authors":"Marsolier-Kergoat MC, Goldar A","authors_abbrev":"Marsolier-Kergoat MC et al.","pubmed_publication_date":"Mar 2012","pubmed_entrez_date":"2011-09-28","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40011088","title":"Pericentromeric sequences, where a conservation paradox occurs.","citation":"Trends Cell Biol 2025 Feb 25;","abstract":"Pericentromeric sequences are characterized by their tandem repeat structure, heterochromatinization, and rapid evolution. The rapid evolvement creates highly diversified pericentromeric sequences, which facilitate reproductive isolation, as best exemplified in Drosophila studies. Despite their high variability, pericentromeric sequences ranging from fission yeast to humans are heterochromatinized with the same histone modification, H3K9 methylation. These features present a paradox, how highly variable sequences get recognized by conserved machineries. This Opinion discusses how this paradox is resolved and how diversification and conservation get unified at pericentromeric sequences.","doi":"10.1016/j.tcb.2025.01.011","authors":"Ma R, Zhu B","authors_abbrev":"Ma R et al.","pubmed_publication_date":"25 Feb 2025","pubmed_entrez_date":"2025-02-26","publication_year":"2025","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2025-02-28 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2325655","title":"A gene family for acidic ribosomal proteins in Schizosaccharomyces pombe: two essential and two nonessential genes.","citation":"Mol Cell Biol 1990 May;10(5):2341-8","abstract":"We have cloned the genes for small acidic ribosomal proteins (A-proteins) of the fission yeast Schizosaccharomyces pombe. S. pombe contains four transcribed genes for small A-proteins per haploid genome, as is the case for Saccharomyces cerevisiae. In contrast, multicellular eucaryotes contain two transcribed genes per haploid genome. The four proteins of S. pombe, besides sharing a high overall similarity, form two couples of nearly identical sequences. Their corresponding genes have a very conserved structure and are transcribed to a similar level. Surprisingly, of each couple of genes coding for nearly identical proteins, one is essential for cell growth, whereas the other is not. We suggest that the unequal importance of the four small A-proteins for cell survival is related to their physical organization in 60S ribosomal subunits.","authors":"Beltrame M, Bianchi ME","authors_abbrev":"Beltrame M et al.","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_session_key":"70a8731b7ac05bcd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-09-25 13:38:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 11:05:08","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP8B7.06","SPBC3B9.13c","SPBC23G7.15c","SPAC644.15"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2013-09-24"},{"uniquename":"PMID:1588914","title":"Five novel elements involved in the regulation of mitosis in fission yeast.","citation":"Mol Gen Genet 1992 Apr;232(3):440-6","abstract":"Five new elements of the mitotic control in the fission yeast Schizosaccharomyces pombe were isolated from gene libraries as multicopy suppressors of the conditional lethal phenotype of win1-1 wee1ts cdc25ts triple mutant strains. These genes were designated wis1(+)-wis5+ for win suppressing, and do not correspond to win1+ or any of the previously characterised mitotic control genes. None of the wis genes is capable of suppressing the cdc phenotype of cdc25ts strains, suggesting that their effect is not simply to reverse the effect of loss of cdc25 function. wis1+ has been previously reported to encode a putative serine/threonine protein kinase that acts as a dosage-dependent inducer of mitosis. wis4+ appears to be a specific suppressor of the win1-1 mutation. wis2+ and wis3+ are capable of suppressing a wide range of cdc phenotypes arising from the combination of various mutations with wee1ts and cdc25ts, suggesting that the wis2+ and wis3+ products may interact with elements central to the mitotic control.","authors":"Warbrick E, Fantes PA","authors_abbrev":"Warbrick E et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"f8fd03e7d6da971d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2017-06-15 15:25:31","canto_approved_date":"2026-02-06 17:00:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-05 09:46:53","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":71,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.09","SPBC19F8.07","SPAC9G1.02","SPAC644.06c","SPAC57A10.02","SPBC11B10.09","SPAC24H6.05","SPBC409.07c","SPAC3F10.15c","SPBC887.10","SPCC18B5.03","SPBC582.03","SPAC1B3.03c"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2017-06-15"},{"uniquename":"PMID:32234663","title":"Iron-sulfur cluster signaling: The common thread in fungal iron regulation.","citation":"Curr Opin Chem Biol 2020 Apr;55:189-201","abstract":"Iron homeostasis in fungi involves balancing iron uptake and storage with iron utilization to achieve adequate, nontoxic levels of this essential nutrient. Extensive work in the nonpathogenic yeast Saccharomyces cerevisiae and Schizosaccharomyces pombe has uncovered unique iron regulation networks for each organism that control iron metabolism via distinct molecular mechanisms. However, common themes have emerged from these studies. The activities of all fungal iron-sensing transcription factors characterized to date are regulated via iron-sulfur cluster signaling. Furthermore, glutaredoxins often play a key role in relaying the intracellular iron status to these DNA-binding proteins. Recent work with fungal pathogens, including Candida and Aspergillus species and Cryptococcus neoformans, has revealed novel iron regulation mechanisms, yet similar roles for iron-sulfur clusters and glutaredoxins in iron signaling have been confirmed. This review will focus on these recent discoveries regarding iron regulation pathways in both pathogenic and nonpathogenic fungi.","doi":"10.1016/j.cbpa.2020.02.008","authors":"Gupta M, Outten CE","authors_abbrev":"Gupta M et al.","pubmed_publication_date":"Apr 2020","pubmed_entrez_date":"2020-04-03","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-04-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30806623","title":"Kinesin-6 regulates cell-size-dependent spindle elongation velocity to keep mitosis duration constant in fission yeast.","citation":"Elife 2019 Feb 26;8","abstract":"The length of the mitotic spindle scales with cell size in a wide range of organisms during embryonic development. Interestingly, in  C. elegans  embryos, this goes along with temporal regulation: larger cells speed up spindle assembly and elongation. We demonstrate that, similarly in fission yeast, spindle length and spindle dynamics adjust to cell size, which allows to keep mitosis duration constant. Since prolongation of mitosis was shown to affect cell viability, this may resemble a mechanism to regulate mitosis duration. We further reveal how the velocity of spindle elongation is regulated: coupled to cell size, the amount of kinesin-6 Klp9 molecules increases, resulting in an acceleration of spindle elongation in anaphase B. In addition, the number of Klp9 binding sites to microtubules increases overproportionally to Klp9 molecules, suggesting that molecular crowding inversely correlates to cell size and might have an impact on spindle elongation velocity control.","doi":"10.7554/eLife.42182","authors":"Krüger LK, Sanchez JL, Paoletti A, Tran PT","authors_abbrev":"Krüger LK et al.","pubmed_publication_date":"26 Feb 2019","pubmed_entrez_date":"2019-02-27","publication_year":"2019","canto_session_key":"bd553a3d6f928456","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramirez","canto_first_approved_date":"2023-07-21 14:24:39","canto_approved_date":"2023-07-21 14:25:26","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-07-21 14:24:31","canto_added_date":"2019-02-28 01:15:04","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":18,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.10","SPAC24H6.05","SPAPB1A10.09","SPCC18B5.03","SPBC15D4.01c","SPAC3A11.14c","SPAC25G10.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2023-07-21"},{"uniquename":"PMID:29123917","title":"The telomere bouquet facilitates meiotic prophase progression and exit in fission yeast.","citation":"Cell Discov 2017;3:17041","abstract":"During meiotic prophase, chromosome arrangement and oscillation promote the pairing of homologous chromosomes for meiotic recombination. This dramatic movement involves clustering of telomeres at the nuclear membrane to form the so-called telomere bouquet. In fission yeast, the telomere bouquet is formed near the spindle pole body (SPB), which is the microtubule organising centre, functionally equivalent to the metazoan centrosome. Disruption of bouquet configuration impedes homologous chromosome pairing, meiotic recombination and spindle formation. Here, we demonstrate that the bouquet is maintained throughout meiotic prophase and promotes timely prophase exit in fission yeast. Persistent DNA damages, induced during meiotic recombination, activate the Rad3 and Chk1 DNA damage checkpoint kinases and extend the bouquet stage beyond the chromosome oscillation period. The auxin-inducible degron system demonstrated that premature termination of the bouquet stage leads to severe extension of prophase and consequently spindle formation defects. However, this delayed exit from meiotic prophase was not caused by residual DNA damage. Rather, loss of chromosome contact with the SPB caused delayed accumulation of CDK1-cyclin B at the SPB, which correlated with impaired SPB separation. In the absence of the bouquet, CDK1-cyclin B localised near the telomeres but not at the SPB at the later stage of meiotic prophase. Thus, bouquet configuration is maintained throughout meiotic prophase, by which this spatial organisation may facilitate local and timely activation of CDK1 near the SPB. Our findings illustrate that chromosome contact with the nuclear membrane synchronises meiotic progression of the nucleoplasmic chromosomes with that of the cytoplasmic SPB.","doi":"10.1038/celldisc.2017.41","authors":"Moiseeva V, Amelina H, Collopy LC, Armstrong CA, Pearson SR, Tomita K","authors_abbrev":"Moiseeva V et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-11-11","publication_year":"2017","canto_session_key":"05cfc921ac6e7ee8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kazunori Tomita","canto_first_approved_date":"2018-01-17 18:32:51","canto_approved_date":"2025-09-03 14:57:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-11 14:04:37","canto_added_date":"2017-11-12 01:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":28,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kazunori Tomita","community_curator":true,"annotation_count":9,"orcid":"0000-0003-1096-6725","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC222.15","SPBC11B10.09","SPBC32H8.11","SPAC30D11.10","SPCC1259.13","SPAC17A5.11","SPAC22F3.03c","SPBC582.03","SPCC18B5.11c","SPAC6G9.13c","SPBC216.05"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2018-01-17"},{"uniquename":"PMID:20559026","title":"Move over: DLIC-like protein in pole position in meiosis.","citation":"Cell Cycle 2010 Jun 01;9(11):2059","abstract":"","authors":"Clyne RK","authors_abbrev":"Clyne RK","pubmed_publication_date":"01 Jun 2010","pubmed_entrez_date":"2010-06-19","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23892058","title":"Interactions between peptidyl tRNA hydrolase homologs and the ribosomal release factor Mrf1 in S. pombe mitochondria.","citation":"Mitochondrion 2013 Nov;13(6):871-80","abstract":"Mitochondrial translation synthesizes key subunits of the respiratory complexes. In Schizosaccharomyces pombe, strains lacking Mrf1, the mitochondrial stop codon recognition factor, are viable, suggesting that other factors can play a role in translation termination. S. pombe contains four predicted peptidyl tRNA hydrolases, two of which (Pth3 and Pth4), have a GGQ motif that is conserved in class I release factors. We show that high dosage of Pth4 can compensate for the absence of Mrf1 and loss of Pth4 exacerbates the lack of Mrf1. Also Pth4 is a component of the mitochondrial ribosome, suggesting that it could help recycling stalled ribosomes.","doi":"10.1016/j.mito.2013.07.115","authors":"Dujeancourt L, Richter R, Chrzanowska-Lightowlers ZM, Bonnefoy N, Herbert CJ","authors_abbrev":"Dujeancourt L et al.","pubmed_publication_date":"Nov 2013","pubmed_entrez_date":"2013-07-30","publication_year":"2013","canto_session_key":"7a2dc662e622f42a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-10 17:07:07","canto_approved_date":"2021-02-26 14:29:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-23 13:05:54","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.18c","SPAC589.11","SPAC24C9.10c","SPMIT.11","SPAC2F7.17"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2015-06-10"},{"uniquename":"PMID:2127797","title":"Glycoprotein molecules in the walls of Schizosaccharomyces pombe wild-type cells and a morphologically altered mutant resistant to papulacandin B.","citation":"J Gen Microbiol 1990 Nov;136(11):2251-9","abstract":"Schizosaccharomyces pombe cell walls contain two major glycoprotein species, I and II, with molecular masses of 2 x 10(6) and 5 x 10(5) Da respectively, as determined by gel filtration chromatography and PAGE. The ratio of sugar to protein is higher in species I than in species II. Much of the sugar in both glycoproteins (about 85% in wild-type cells) is O-linked to the peptide moiety. The morphological sph1 mutant is resistant to papulacandin B, and its cell wall contains less glycoprotein II (but not less glycoprotein I) than the parental wild-type strain, although glycoprotein II is still synthesized and released into the growth medium. Papulacandin B largely reverses the morphological alteration of the mutant, and returns the ratio between species I and II to about that found in the parental strain, although the absolute amount of species II is still lower in the mutant. The results point to the importance of the relative amounts of the different wall polymers in determining cell morphology.","authors":"Font de Mora J, Valentín E, Herrero E, Sentandreu R","authors_abbrev":"Font de Mora J et al.","pubmed_publication_date":"Nov 1990","pubmed_entrez_date":"1990-11-01","publication_year":"1990","canto_session_key":"c5d95cfad80ef2e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-07-01 10:40:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-13 13:05:16","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-06-13"},{"uniquename":"PMID:10660074","title":"Characterization of a Saccharomyces cerevisiae homologue of Schizosaccharomyces pombe Chk1 involved in DNA-damage-induced M-phase arrest.","citation":"Mol Gen Genet 2000 Jan;262(6):1132-46","abstract":"Chk1 is an evolutionarily conserved protein kinase that plays an essential role in mediating G2 arrest in response to DNA damage in Schizosaccharomyces pombe and human cells. It functions by maintaining the inhibition (by phosphorylation of a specific tyrosine residue) of the cyclin-dependent kinase Cdc2 that initiates the G2/M transition. Here, we characterize a structural homologue of Chk1 in the budding yeast Saccharomyces cerevisiae. In this organism, G2/M arrest following DNA damage is considered to be independent of tyrosine phosphorylation of the Cdc2 homologue Cdc28. Nevertheless, a partial defect in G2/M-phase arrest following treatment with ionizing radiation, but not UV radiation, is associated with deletion of CHK1. The fact that such an effect remains detectable in cells synchronized with the microtubule inhibitor nocodazole prior to gamma irradiation implies the existence of a CHK1-dependent checkpoint in M phase. We conclude from epistasis analysis that Chk1 participates in the Pds1-dependent subpathway of M-phase arrest. In spite of the partial checkpoint defect of the chk1 mutant, the survival of colony-forming cells is not notably decreased following UV and gamma irradiation. In two-hybrid screens, we identified a heme-binding stress protein (encoded by the yeast ORF YNL234W), a protein involved in genomic silencing (Sas3) and Chk1 itself as interacting partners of Chk1.","authors":"Liu Y, Vidanes G, Lin YC, Mori S, Siede W","authors_abbrev":"Liu Y et al.","pubmed_publication_date":"Jan 2000","pubmed_entrez_date":"2000-02-05","publication_year":"2000","canto_session_key":"a291ec51cc4320e1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-11-08 20:12:00","canto_approved_date":"2019-11-08 20:12:00","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-08 20:11:54","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-11-08"},{"uniquename":"PMID:3241624","title":"Genetic engineering of Schizosaccharomyces pombe: a system for gene disruption and replacement using the ura4 gene as a selectable marker.","citation":"Mol Gen Genet 1988 Dec;215(1):81-6","abstract":"A system is described for gene disruption and replacement in Schizosaccharomyces pombe based on the homologous selectable marker, ura4, the structural gene for orotidine-5'-phosphate decarboxylase. The presence of a single copy of the wild-type gene can rescue a ura4 auxotrophic mutant. Furthermore, ura4- cells can be selected for in the presence of 5-fluoroorotic acid (5-FOA). This allows a convenient means of selecting for both forward and backward mutations. The sequence of a 1.8 kb HindIII fragment which contains the functional gene is reported. It encodes a single open reading frame of 264 amino acids which shows considerable conservation with the orotidine-5'-phosphate (OMP) decarboxylases from other organisms. The ura4 transcript is approximately 850 nucleotides long. It begins 51 bp upstream of the protein coding sequence and is unusual in that transcription termination occurs at or very close to the translational stop codon. To facilitate the use of ura4 in gene disruption experiments we have also constructed a novel strain of S. pombe called ura4-D18, in which the 1.8 kb HindIII fragment has been deleted from the chromosome. Using a combination of this strain and vectors containing ura4 as a selectable marker, we present a general method for targeting recombination events to the chromosomal locus under investigation.","authors":"Grimm C, Kohli J, Murray J, Maundrell K","authors_abbrev":"Grimm C et al.","pubmed_publication_date":"Dec 1988","pubmed_entrez_date":"1988-12-01","publication_year":"1988","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34100774","title":"Crystal structure of the Thr316Ala mutant of a yeast JAMM deubiquitinase: implication of active-site loop dynamics in catalysis.","citation":"Acta Crystallogr F Struct Biol Commun 2021 Jun 01;77(Pt 6):163-170","abstract":"AMSH, an endosome-associated deubiquitinase (DUB) with a high specificity for Lys63-linked polyubiquitin chains, plays an important role in endosomal-lysosomal sorting and down-regulation of cell-surface receptors. AMSH belongs to the JAMM family of DUBs that contain two insertion segments, Ins-1 and Ins-2, in the catalytic domain relative to the JAMM core found in the archaebacterial AfJAMM. Structural analyses of the AMSH homologs human AMSH-LP and fission yeast Sst2 reveal a flap-like structure formed by Ins-2 near the active site that appears to open and close during its catalytic cycle. A conserved phenylalanine residue of the flap interacts with a conserved aspartate residue of the Ins-1 β-turn to form a closed `lid' over the active site in the substrate-bound state. Analyses of these two residues (Phe403 and Asp315) in Sst2 showed that their interaction plays an important role in controlling the flexibility of Ins-2. The Lys63-linked diubiquitin substrate-bound form of Sst2 showed that the conserved phenylalanine also interacts with Thr316 of Ins-1, which is substituted by tyrosine in other AMSH orthologs. Although Thr316 makes no direct interaction with the substrate, its mutation to alanine resulted in a significant loss of activity. In order to understand the contribution of Thr316 to catalysis, the crystal structure of this mutant was determined. In spite of the effect of the mutation on catalytic activity, the structure of the Sst2 Thr316Ala mutant did not reveal significant changes in either the overall structure or the active-site arrangement relative to the wild type. The Phe403-Thr316 van der Waals interaction is impaired by the Thr316Ala mutation, abrogating the adoption of the closed active-site conformation required for catalysis. Since van der Waals interactions with phenylalanine are conserved across substrate-bound forms of AMSH-LP and Sst2, these interactions may be critical for loop immobilization and the positioning of the isopeptide bond of Lys63-linked polyubiquitin-chain substrates.","doi":"10.1107/S2053230X21005124","authors":"Shrestha R, Das C","authors_abbrev":"Shrestha R et al.","pubmed_publication_date":"01 Jun 2021","pubmed_entrez_date":"2021-06-08","publication_year":"2021","canto_session_key":"0cc6e2982ac94ff8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-10 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC337.08c","SPAC19B12.10"],"gene_count":2,"ltp_gene_count":2,"pdb_entries":[{"pdb_id":"7lm3","gene_chains":[{"gene_uniquename":"SPAC19B12.10","chain":"A/B","position":"245-435"}],"title":"Crystal Structure of Thr316Ala mutant of JAMM domain of S. pombe","entry_authors":"Shrestha R,Das C","entry_authors_abbrev":"Shrestha R et al.","reference_uniquename":"PMID:34100774","experimental_method":"X-ray","resolution":"2.7"}]},{"uniquename":"PMID:22674789","title":"A new method to efficiently induce a site-specific double-strand break in the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2012 Jul;29(7):275-91","abstract":"Double-strand DNA breaks are a serious threat to cellular viability and yeast systems have proved invaluable in helping to understand how these potentially toxic lesions are sensed and repaired. An important method to study the processing of DNA breaks in the budding yeast Saccharomyces cerevisiae is to introduce a unique double-strand break into the genome by regulating the expression of the site-specific HO endonuclease with a galactose inducible promoter. Variations of the HO site-specific DSB assay have been adapted to many organisms, but the methodology has seen only limited use in the fission yeast Schizosaccharomyces pombe because of the lack of a promoter capable of inducing endonuclease expression on a relatively short time scale (~1 h). We have overcome this limitation by developing a new assay in which expression of the homing endonuclease I-PpoI is tightly regulated with a tetracycline-inducible promoter. We show that induction of the I-PpoI endonuclease produces rapid cutting of a defined cleavage site (> 80% after 1 h), efficient cell cycle arrest and significant accumulation of the checkpoint protein Crb2 at break-adjacent regions in a manner that is analogous to published findings with DSBs produced by an acute exposure to ionizing irradiation. This assay provides an important new tool for the fission yeast community and, because many aspects of mammalian chromatin organization have been well-conserved in Sz. pombe but not in S. cerevisiae, also offers an attractive system to decipher the role of chromatin structure in modulating the repair of double-stranded DNA breaks.","doi":"10.1002/yea.2908","authors":"Sunder S, Greeson-Lott NT, Runge KW, Sanders SL","authors_abbrev":"Sunder S et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-06-08","publication_year":"2012","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1319571","title":"Cloning and characterisation of the S. pombe rad15 gene, a homologue to the S. cerevisiae RAD3 and human ERCC2 genes.","citation":"Nucleic Acids Res 1992 Jun 11;20(11):2673-8","abstract":"The RAD3 gene of Saccharomyces cerevisiae encodes an ATP-dependent 5'-3' DNA helicase, which is involved in excision repair of ultraviolet radiation damage. By hybridisation of a Schizosaccharomyces pombe genomic library with a RAD3 gene probe we have isolated the S. pombe homologue of RAD3. We have also cloned the rad15 gene of S. pombe by complementation of radiation-sensitive phenotype of the rad15 mutant. Comparison of the restriction map and DNA sequence, shows that the S. pombe rad15 gene is identical to the gene homologous to S. cerevisiae RAD3, identified by hybridisation. The S. pombe rad15.P mutant is highly sensitive to UV radiation, but only slightly sensitive to ionising radiation, as expected for a mutant defective in excision repair. DNA sequence analysis of the rad15 gene indicates an open reading frame of 772 amino acids, and this is consistent with a transcript size of 2.6 kb as detected by Northern analysis. The predicted rad15 protein has 65% identity to RAD3 and 55% identity to the human homologue ERCC2. This homology is particularly striking in the regions identified as being conserved in a group of DNA helicases. Gene deletion experiments indicate that, like the S. cerevisiae RAD3 gene, the S. pombe rad15 gene is essential for viability, suggesting that the protein product has a role in cell proliferation and not solely in DNA repair.","authors":"Murray JM, Doe CL, Schenk P, Carr AM, Lehmann AR, Watts FZ","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"11 Jun 1992","pubmed_entrez_date":"1992-06-11","publication_year":"1992","canto_session_key":"0633f4467e41f64b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-01-09 17:03:20","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-04-24 22:22:09","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-04-24"},{"uniquename":"PMID:1448080","title":"Fission yeast pap1-dependent transcription is negatively regulated by an essential nuclear protein, crm1.","citation":"Mol Cell Biol 1992 Dec;12(12):5474-84","abstract":"The fission yeast pap1+ gene encodes an AP-1-like transcription factor that contains a leucine zipper motif. We identified a target gene of pap1, the p25 gene. The 5' upstream region of the p25 gene contains an AP-1 site, and by DNase I footprint analysis, we showed that the pap1 protein binds to the AP-1 site as well as to a 14-bp palindrome sequence. p25 is overproduced when the pap1+ gene is overexpressed, whereas p25 is not produced at all in the pap1 deletion mutant. p25 was previously found to be overproduced in strains carrying cold-sensitive crm1 mutations whose gene product is essential for viability and is thought to play an important role in maintenance of a proper chromosomal architecture. Deletion and site-directed mutagenesis of sequences upstream of the p25 gene demonstrated that the AP-1 site as well as the palindrome sequence are crucial for transcriptional activation either by pap1 overproduction or by the cold-sensitive crm1 mutation; pap1+ is apparently negatively regulated by crm1+. Moreover, we found that cold-sensitive crm1 mutations are suppressed by the deletion of pap1+, further indicating a close relationship between crm1+ and pap1+. The crm1 protein is highly conserved; the budding yeast homolog, CRM1, which complements the fission yeast cold-sensitive crm1 mutation, was isolated and found to also be essential for viability. These results suggest the functional importance of chromosome structure on the regulation of gene expression through the pap1 transcription factor.","authors":"Toda T, Shimanuki M, Saka Y, Yamano H, Adachi Y, Shirakawa M, Kyogoku Y, Yanagida M","authors_abbrev":"Toda T et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"0370b9834de2dfe6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-12 15:46:07","canto_approved_date":"2023-09-11 07:24:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-25 15:27:59","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.14c","SPAC1805.17","SPAC1783.07c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-05-12"},{"uniquename":"PMID:9870697","title":"Differential effects of caffeine on DNA damage and replication cell cycle checkpoints in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1998 Nov;260(4):319-34","abstract":"Caffeine potentiates the lethal effects of ultraviolet and ionising radiation on wild-type Schizosaccharomyces pombe cells. In previous studies this was attributed to the inhibition by caffeine of a novel DNA repair pathway in S. pombe that was absent in the budding yeast Saccharomyces cerevisiae. Studies with radiation-sensitive S. pombe mutants suggested that this caffeine-sensitive pathway could repair ultraviolet radiation damage in the absence of nucleotide excision repair. The alternative pathway was thought to be recombinational and to operate in the G2 phase of the cell cycle. However, in this study we show that cells held in G1 of the cell cycle can remove ultraviolet-induced lesions in the absence of nucleotide excision repair. We also show that recombination-defective mutants, and those now known to define the alternative repair pathway, still exhibit the caffeine effect. Our observations suggest that the basis of the caffeine effect is not due to direct inhibition of recombinational repair. The mutants originally thought to be involved in a caffeine-sensitive recombinational repair process are now known to be defective in arresting the cell cycle in S and/or G2 following DNA damage or incomplete replication. The gene products may also have an additional role in a DNA repair or damage tolerance pathway. The effect of caffeine could, therefore, be due to interference with DNA damage checkpoints, or inhibition of the DNA damage repair/tolerance pathway. Using a combination of flow cytometric analysis, mitotic index analysis and fluorescence microscopy we show that caffeine interferes with intra-S phase and G2 DNA damage checkpoints, overcoming cell cycle delays associated with damaged DNA. In contrast, caffeine has no effect on the DNA replication S phase checkpoint in response to inhibition of DNA synthesis by hydroxyurea.","authors":"Osman F, McCready S","authors_abbrev":"Osman F et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1998-12-31","publication_year":"1998","canto_session_key":"dcf8c388387a8b08","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-26 08:39:43","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-26 08:39:36","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC30D11.10","SPAC1952.07","SPAC15A10.03c","SPAC644.14c","SPBC336.12c","SPBC3E7.08c","SPAC3G6.06c","SPBC19C7.09c","SPCC338.17c","SPCC5E4.06","SPCC18B5.11c"],"gene_count":12,"ltp_gene_count":7,"approved_date":"2014-11-26"},{"uniquename":"PMID:23695302","title":"Functional characterization of fission yeast transcription factors by overexpression analysis.","citation":"Genetics 2013 Aug;194(4):873-84","abstract":"In Schizosaccharomyces pombe, over 90% of transcription factor genes are nonessential. Moreover, the majority do not exhibit significant growth defects under optimal conditions when deleted, complicating their functional characterization and target gene identification. Here, we systematically overexpressed 99 transcription factor genes with the nmt1 promoter and found that 64 transcription factor genes exhibited reduced fitness when ectopically expressed. Cell cycle defects were also often observed. We further investigated three uncharacterized transcription factor genes (toe1(+)-toe3(+)) that displayed cell elongation when overexpressed. Ectopic expression of toe1(+) resulted in a G1 delay while toe2(+) and toe3(+) overexpression produced an accumulation of septated cells with abnormalities in septum formation and nuclear segregation, respectively. Transcriptome profiling and ChIP-chip analysis of the transcription factor overexpression strains indicated that Toe1 activates target genes of the pyrimidine-salvage pathway, while Toe3 regulates target genes involved in polyamine synthesis. We also found that ectopic expression of the putative target genes SPBC3H7.05c, and dad5(+) and SPAC11D3.06 could recapitulate the cell cycle phenotypes of toe2(+) and toe3(+) overexpression, respectively. Furthermore, single deletions of the putative target genes urg2(+) and SPAC1399.04c, and SPBC3H7.05c, SPACUNK4.15, and rds1(+), could suppress the phenotypes of toe1(+) and toe2(+) overexpression, respectively. This study implicates new transcription factors and metabolism genes in cell cycle regulation and demonstrates the potential of systematic overexpression analysis to elucidate the function and target genes of transcription factors in S. pombe.","doi":"10.1534/genetics.113.150870","authors":"Vachon L, Wood J, Kwon EJ, Laderoute A, Chatfield-Reed K, Karagiannis J, Chua G","authors_abbrev":"Vachon L et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-05-23","publication_year":"2013","canto_session_key":"94e20d207ffa7a12","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-08 09:35:23","canto_approved_date":"2026-01-12 17:12:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 17:14:24","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Antonia Lock","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":151,"orcid":"0000-0003-1179-5999","file_type":"PHAF","file_name":"PMID_23695302_phaf.tsv"}],"genes":["SPBC3H7.05c","SPBC530.05","SPAC8C9.14","SPCC417.09c","SPBC1683.06c","SPAC4G8.13c","SPAC31A2.11c","SPCC417.02","SPAC144.09c","SPBC1D7.02c","SPAC21E11.03c","SPAC3G9.14","SPAC11E3.06","SPBC21B10.13c","SPBC17D1.01","SPAC25G10.03","SPAC6F12.02","SPBC1198.04c","SPBC19C7.10","SPBC336.12c","SPAC11D3.07c","SPAC821.07c","SPAC56F8.16","SPBC1683.13c","SPCC1393.08","SPBC56F2.05c","SPAC23E2.01","SPAC1002.17c","SPAC3H1.11","SPAC1039.05c","SPBC1105.14","SPCC1902.01","SPBC27B12.11c","SPAC1142.08","SPBC1773.16c","SPAC139.03","SPBC32C12.02","SPBC354.05c","SPAC11D3.06","SPAC3H8.08c","SPCC757.04","SPACUNK4.15","SPAC343.12","SPAC10F6.08c","SPBP8B7.30c","SPBC2F12.09c","SPCC1919.14c","SPBC317.01","SPAC22F3.02","SPAC6G10.12c","SPAPB24D3.01","SPBC16G5.15c","SPBC725.16","SPAC19B12.07c","SPBP4H10.09","SPCC320.03","SPAC23H4.01c","SPAC1B1.01","SPCC290.04","SPBC16G5.17","SPAC25B8.19c","SPCC965.10","SPCC736.08","SPAP14E8.02","SPAC1002.19","SPAC25B8.11","SPBC725.11c","SPAC1002.18","SPAC32A11.03c","SPAC1399.05c","SPAC2H10.01","SPCC1223.13","SPAC22F3.09c","SPAC16.05c","SPAC1399.04c","SPBC4C3.12","SPAC1783.07c","SPCC1795.05c","SPAC2E12.02","SPBC2D10.06","SPBC3B8.02","SPBC23G7.09"],"gene_count":82,"ltp_gene_count":78,"approved_date":"2017-03-08"},{"uniquename":"PMID:11335722","title":"Rapamycin blocks sexual development in fission yeast through inhibition of the cellular function of an FKBP12 homolog.","citation":"J Biol Chem 2001 Jul 06;276(27):24736-42","abstract":"FKBP12 is a ubiquitous and a highly conserved prolyl isomerase that binds the immunosuppressive drugs FK506 and rapamycin. Members of the FKBP12 family have been implicated in many processes that include intracellular protein folding, transport, and assembly. In the budding yeast Saccharomyces cerevisiae and in human T cells, rapamycin forms a complex with FKBP12 that inhibits cell cycle progression by inhibition of the TOR kinases. We reported previously that rapamycin does not inhibit the vegetative growth of the fission yeast Schizosaccharomyces pombe; however, it specifically inhibits its sexual development. Here we show that disruption of the S. pombe FKBP12 homolog, fkh1(+), at its chromosomal locus results in a mating-deficient phenotype that is highly similar to that obtained by treatment of wild type cells with rapamycin. A screen for fkh1 mutants that can confer rapamycin resistance identified five amino acids in Fkh1 that are critical for the effect of rapamycin in S. pombe. All five amino acids are located in the putative rapamycin binding pocket. Together, our findings indicate that Fkh1 has an important role in sexual development and serves as the target for rapamycin action in S. pombe.","authors":"Weisman R, Finkelstein S, Choder M","authors_abbrev":"Weisman R et al.","pubmed_publication_date":"06 Jul 2001","pubmed_entrez_date":"2001-05-04","publication_year":"2001","canto_session_key":"ae029b5da42522e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-03-30 14:11:06","canto_approved_date":"2019-06-14 12:18:37","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-30 14:11:00","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["HGNC:3712","SPBC839.17c","HGNC:21376","HGNC:3711"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-03-30"},{"uniquename":"EMBL:SPC07942","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2729583","title":"Isolation of DNA from yeasts.","citation":"Anal Biochem 1989 Apr;178(1):82-7","abstract":"Methods are described that allow DNA to be prepared from widely different yeasts (Candida utilis, Saccharomyces cerevisiae, and Schizosaccharomyces pombe). The methods are reliably reproducible, and the DNA obtained is of appropriate quality for the construction of gene libraries (upper limit of size range consistently 50-150 kbp). In method A, yeast cells are converted into spheroplasts by treatment with a highly purified mixture of enzymes from Trichoderma harzianum, the spheroplasts are lysed in a lauroylsarcosinate/EDTA buffer, and the lysate is incubated with proteinase K and then directly centrifuged through a cesium trifluoroacetate gradient. DNA is recovered from the appropriate fractions by ethanol precipitation, and the redissolved precipitate is incubated with ribonuclease. For the rest of the isolation, two protocols are given, one avoiding and one including phenol/chloroform extraction. In this way, DNA up to about 150 kbp in size can be obtained. In method B, spheroplasts are not made. Yeast cells are broken by grinding under liquid nitrogen and are then worked up in a manner similar to method A, protocol 2. Subsequent steps depend on the purpose for which the DNA is required. Traditional methods of sucrose or salt density gradient centrifugation or agarose gel electrophoresis are applicable for size selection. A sodium iodide/silica matrix technique allows fast and effective DNA recovery from agarose gels.","authors":"Mann W, Jeffery J","authors_abbrev":"Mann W et al.","pubmed_publication_date":"Apr 1989","pubmed_entrez_date":"1989-04-01","publication_year":"1989","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD223","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25008109","title":"A mutation in the human CBP4 ortholog UQCC3 impairs complex III assembly, activity and cytochrome b stability.","citation":"Hum Mol Genet 2014 Dec 01;23(23):6356-65","abstract":"Complex III (cytochrome bc1) is a protein complex of the mitochondrial inner membrane that transfers electrons from ubiquinol to cytochrome c. Its assembly requires the coordinated expression of mitochondrial-encoded cytochrome b and nuclear-encoded subunits and assembly factors. Complex III deficiency is a severe multisystem disorder caused by mutations in subunit genes or assembly factors. Sequence-profile-based orthology predicts C11orf83, hereafter named UQCC3, to be the ortholog of the fungal complex III assembly factor CBP4. We describe a homozygous c.59T>A missense mutation in UQCC3 from a consanguineous patient diagnosed with isolated complex III deficiency, displaying lactic acidosis, hypoglycemia, hypotonia and delayed development without dysmorphic features. Patient fibroblasts have reduced complex III activity and lower levels of the holocomplex and its subunits than controls. They have no detectable UQCC3 protein and have lower levels of cytochrome b protein. Furthermore, in patient cells, cytochrome b is absent from a high-molecular-weight complex III. UQCC3 is reduced in cells depleted for the complex III assembly factors UQCC1 and UQCC2. Conversely, absence of UQCC3 in patient cells does not affect UQCC1 and UQCC2. This suggests that UQCC3 functions in the complex III assembly pathway downstream of UQCC1 and UQCC2 and is consistent with what is known about the function of Cbp4 and of the fungal orthologs of UQCC1 and UQCC2, Cbp3 and Cbp6. We conclude that UQCC3 functions in complex III assembly and that the c.59T>A mutation has a causal role in complex III deficiency.","doi":"10.1093/hmg/ddu357","authors":"Wanschers BF, Szklarczyk R, van den Brand MA, Jonckheere A, Suijskens J, Smeets R, Rodenburg RJ, Stephan K, Helland IB, Elkamil A, Rootwelt T, Ott M, van den Heuvel L, Nijtmans LG, Huynen MA","authors_abbrev":"Wanschers BF et al.","pubmed_publication_date":"01 Dec 2014","pubmed_entrez_date":"2014-07-11","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:34399","SPBC27B12.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29187422","title":"Dependency of Heterochromatin Domains on Replication Factors.","citation":"G3 (Bethesda) 2018 Feb 02;8(2):477-489","abstract":"Chromatin structure regulates both genome expression and dynamics in eukaryotes, where large heterochromatic regions are epigenetically silenced through the methylation of histone H3K9, histone deacetylation, and the assembly of repressive complexes. Previous genetic screens with the fission yeast  Schizosaccharomyces pombe  have led to the identification of key enzymatic activities and structural constituents of heterochromatin. We report here on additional factors discovered by screening a library of deletion mutants for silencing defects at the edge of a heterochromatic domain bound by its natural boundary-the  IR-R  +  element-or by ectopic boundaries. We found that several components of the DNA replication progression complex (RPC), including Mrc1/Claspin, Mcl1/Ctf4, Swi1/Timeless, Swi3/Tipin, and the FACT subunit Pob3, are essential for robust heterochromatic silencing, as are the ubiquitin ligase components Pof3 and Def1, which have been implicated in the removal of stalled DNA and RNA polymerases from chromatin. Moreover, the search identified the cohesin release factor Wpl1 and the forkhead protein Fkh2, both likely to function through genome organization, the Ssz1 chaperone, the Fkbp39 proline  cis-trans  isomerase, which acts on histone H3P30 and P38 in  Saccharomyces cerevisiae , and the chromatin remodeler Fft3. In addition to their effects in the mating-type region, to varying extents, these factors take part in heterochromatic silencing in pericentromeric regions and telomeres, revealing for many a general effect in heterochromatin. This list of factors provides precious new clues with which to study the spatiotemporal organization and dynamics of heterochromatic regions in connection with DNA replication.","doi":"10.1534/g3.117.300341","authors":"Jahn LJ, Mason B, Brøgger P, Toteva T, Nielsen DK, Thon G","authors_abbrev":"Jahn LJ et al.","pubmed_publication_date":"02 Feb 2018","pubmed_entrez_date":"2017-12-01","publication_year":"2018","canto_session_key":"7d964e97a3ae5e57","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-12-02 01:15:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9404894","title":"The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation.","citation":"RNA 1997 Dec;3(12):1434-43","abstract":"Most RNA polymerase III transcripts are bound immediately after synthesis by an abundant nuclear phosphoprotein known as the La autoantigen. Experiments performed in the budding yeast Saccharomyces cerevisiae have revealed that binding of the La protein to tRNA precursors is required for the endonucleolytic maturation of the 3' terminus of many tRNAs. In the absence of this protein, the 3' ends of these tRNAs are trimmed by exonucleases (Yoo CJ, Wolin SL, 1997, Cell 89:393-402). Here we report the characterization of the La protein in the fission yeast Schizosaccharomyces pombe. As was described for budding yeast, S. pombe cells lacking the La protein are viable and exhibit alterations in the pathway of pre-tRNA maturation. Introduction of either the human, S. cerevisiae, or S. pombe La protein into these cells restores the detected pattern of tRNA processing intermediates to that of wild-type cells. By performing immunoprecipitations from cells that were metabolically labeled with 32P-orthophosphate, we demonstrate that the S. pombe and S. cerevisiae La proteins, like the human La protein, are phosphorylated in vivo. Thus, although the La protein is dispensable for growth in these yeasts, both the structure of the protein and its function in pre-tRNA maturation have been highly conserved throughout evolution.","authors":"Van Horn DJ, Yoo CJ, Xue D, Shi H, Wolin SL","authors_abbrev":"Van Horn DJ et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1997-12-24","publication_year":"1997","canto_session_key":"6192a64da93c9f81","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-10-01 15:25:32","canto_approved_date":"2021-11-01 18:20:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-24 16:09:30","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPAC57A10.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-10-01"},{"uniquename":"PMID:36724944","title":"Fission Yeast PUF Proteins Puf3 and Puf4 Are Novel Regulators of PI4P5K Signaling.","citation":"Biol Pharm Bull 2023;46(2):163-169","abstract":"Phosphatidylinositol-4-phosphate 5-kinase (PI4P5K) is a highly conserved enzyme that generates phosphatidylinositol-4,5-bisphosphate (PI(4,5)P 2 ) by phosphorylating phosphatidylinositol 4-phosphate (PI(4)P). Schizosaccharomyces pombe (S. pombe) its3-1 is a loss-of-function mutation in the essential its3 +  gene that encodes a PI4P5K. Its3 regulates cell proliferation, cytokinesis, cell integrity, and membrane trafficking, but little is known about the regulatory mechanisms of Its3. To identify regulators of Its3, we performed a genetic screening utilizing the high-temperature sensitivity (TS) of its3-1 and identified puf3 +  and puf4 + , encoding Pumilio/PUF family RNA-binding proteins as multicopy suppressors of its3-1 cells. The deletions of the PUF domains in the puf3 +  and puf4 +  genes resulted in the reduced ability to suppress its3-1, suggesting that the suppression by Puf3 and Puf4 may involve their RNA-binding activities. The gene knockout of Puf4, but not that of Puf3, exacerbated the TS of its3-1. Interestingly, mutant Its3 expression levels both at mRNA and protein levels were lower than those of the wild-type (WT) Its3. Consistently, the overexpression of the mutant its3-1 gene suppressed the its3-1 phenotypes. Notably, Puf3 and Puf4 overexpression increased the mRNA and protein expression levels of both Its3 and Its3-1. Collectively, our genetic screening revealed a functional relationship between the Pumilio/PUF family RNA-binding proteins and PI4P5K.","doi":"10.1248/bpb.b22-00569","authors":"Satoh R, Tanaka T, Yoshida N, Tanaka C, Takasaki T, Sugiura R","authors_abbrev":"Satoh R et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-02-01","publication_year":"2023","canto_session_key":"51391264be9c55f2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-02-03 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9617223","title":"[Foreign gene expression in fission yeast S. pombe].","citation":"Seikagaku 1998 Apr;70(4):300-4","abstract":"","authors":"Giga-Hama Y, Kumagai H","authors_abbrev":"Giga-Hama Y et al.","pubmed_publication_date":"Apr 1998","pubmed_entrez_date":"1998-06-09","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11754480","title":"Sulphur amino acid synthesis in Schizosaccharomyces pombe represents a specific variant of sulphur metabolism in fungi.","citation":"Yeast 2002 Jan 15;19(1):29-35","abstract":"Schizosaccharomyces pombe, in contrast to Saccharomyces cerevisiae and Aspergillus nidulans, lacks cystathionine beta-synthase and cystathionine gamma-lyase, two enzymes in the pathway from methionine to cysteine. As a consequence, methionine cannot serve as an efficient sulphur source for the fungus and does not bring about repression of sulphur assimilation, which is under control of the cysteine-mediated sulphur metabolite repression system. This system operates at the transcriptional level, as was shown for the homocysteine synthase encoding gene. Our results corroborate the growing evidence that cysteine is the major low-molecular-weight effector in the regulation of sulphur metabolism in bacteria, fungi and plants.","authors":"Brzywczy J, Sieńko M, Kucharska A, Paszewski A","authors_abbrev":"Brzywczy J et al.","pubmed_publication_date":"15 Jan 2002","pubmed_entrez_date":"2002-01-05","publication_year":"2002","canto_session_key":"ed153e3b45363fc1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-09-20 13:52:04","canto_approved_date":"2025-03-24 08:24:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-19 10:25:39","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC428.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-20"},{"uniquename":"EMBL:AB028068","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11069761","title":"The S. pombe rlc1 gene encodes a putative myosin regulatory light chain that binds the type II myosins myo3p and myo2p.","citation":"J Cell Sci 2000 Dec;113 Pt 23:4157-63","abstract":"In order to identify additional components important for cell division in the fission yeast Schizosaccharomyces pombe we have screened a bank of conditional cold-sensitive mutants for cytokinesis defects. One of these mutants showed a delay in cell cleavage, and strong genetic interactions with other genes implicated in medial ring formation. Cloning of the corresponding gene indicates that it encodes a protein with significant homology to the regulatory light chain of non-muscle myosins. We have named the gene rlc1 (regulatory light chain 1). The gene is not essential for division, but null mutants display a cell cleavage defect and form an aberrant F-actin ring. Two myosin-II heavy chains have been identified in fission yeast: Co-immunoprecipitation experiments indicate that rlc1p associates more strongly with myo3p than myo2p.","authors":"Le Goff X, Motegi F, Salimova E, Mabuchi I, Simanis V","authors_abbrev":"Le Goff X et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2000-11-09","publication_year":"2000","canto_session_key":"e10c528c467ca938","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-26 14:28:07","canto_approved_date":"2026-01-30 15:32:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-25 16:50:00","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPAC926.03","SPAC4A8.05c","SPAP8A3.08","SPAC4F8.13c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-01-26"},{"uniquename":"PMID:25128706","title":"Regulation of oxidative stress-induced cytotoxic processes of citrinin in the fission yeast Schizosaccharomyces pombe.","citation":"Toxicon 2014 Nov;90:155-66","abstract":"In this study, the citrinin (CTN)-induced accumulation of reactive oxygen species (ROS) and the regulation of the activities of antioxidant enzymes were investigated in acute toxicity tests in Schizosaccharomyces pombe. 30% of the CTN was accumulated by the cells in 1000 μM CTN solution. In comparison with the control, exposure of 10(7) cells ml(-1) to 1000 μM CTN for 60 min at pH = 4.5 induced significantly (p < 1%) elevated levels of peroxides and total ROS, but not of superoxide or hydroxyl radicals, while there was a 3-fold increase in the concentration of glutathione. ROS-induced adaptation processes at cell and molecular levels via activation of the redox-sensitive transcription factors Pap1 and (in part) Atf1 resulted in significantly increased specific activities of glutathione peroxidases, glucose-6-phosphate dehydrogenase and glutathione S-transferase and in decreased levels of catalase and glutathione reductase, but no changes were detected in the activities of superoxide dismutases. This treatment caused a G2/M cell cycle arrest and elevated the number of fragmented nuclei, which is one of the markers of apoptosis. Comparison of these results with those for the positive control, 200 μM H2O2, suggested that CTN induced a medium level of oxidative stress.","doi":"10.1016/j.toxicon.2014.08.005","authors":"Máté G, Gazdag Z, Mike N, Papp G, Pócsi I, Pesti M","authors_abbrev":"Máté G et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-08-17","publication_year":"2014","canto_session_key":"4feb4d8f4e75337a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-08-18 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6036166","title":"Gene-controlled UV-sensitivity in Schizosaccharomyces pombe.","citation":"Mutat Res 1967;4(2):219-21","abstract":"","authors":"Haefnar K, Howery L","authors_abbrev":"Haefnar K et al.","pubmed_publication_date":"1967","pubmed_entrez_date":"1967-03-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8552194","title":"Interaction of Cdc2 and Cdc18 with a fission yeast ORC2-like protein.","citation":"Nature 1996 Jan 25;379(6563):360-3","abstract":"In fission yeast, Cdc2 kinase has both positive and negative roles in regulating DNA replication, being first necessary for the transition from G1 to S phase and later required to prevent the re-initiation of DNA replication during G2. We report here that Cdc2 interacts with Orp2, a protein similar to the Orc2 replication factor subunit of Saccharomyces cerevisiae origin recognition complex (ORC). ORC binds chromosomal origins and is essential for chromosomal replication initiation. Fission yeast Orp2 is required for DNA replication and interacts with the rate-limiting replication activator Cdc18. Cells lacking Orp2 undergo aberrant mitosis, indicating that Orp2 is involved in generating a checkpoint signal. These findings suggest that ORC functions are conserved among eukaryotes and provide evidence that Cdc2 controls DNA replication initiation by acting directly at chromosomal origins.","authors":"Leatherwood J, Lopez-Girona A, Russell P","authors_abbrev":"Leatherwood J et al.","pubmed_publication_date":"25 Jan 1996","pubmed_entrez_date":"1996-01-25","publication_year":"1996","canto_session_key":"7b4cc66d70a89e8d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-06-29 10:42:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-22 17:30:12","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPBC11B10.09","SPBC582.03","SPAC1952.07","SPBC685.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2012-11-22"},{"uniquename":"PMID:17932456","title":"Studies on fungal Pumilio gene family through mining multiple genome-scale data sets.","citation":"Kobe J Med Sci 2007;53(4):163-9","abstract":"The genes belonging to Pumilio gene family of the fission yeast Schizosaccharomyces pombe (S. pombe) were compared with genome information of the several fungi and their functions have been inferred using public-access databases disclosed on the internet websites. The Pumilio-family genes are conserved from yeast to man and have been considered to suppress the expression of other genes by binding their specific target messenger RNAs. In S. pombe genome, nine genes belonging to Pumilio gene family were found and were clustered into four groups by homology of their amino acid sequences. Each gene has been analyzed to search 'close orthologue' in the genomes of Saccharomyces cerevisiae, Candida parapsilosis, Aspergillus fumigatus, Phytophthora infestans, Pneumocystis carinii and Neurospora crassa, using protein-protein blast P search. Consequently, we found several genes belonging to Pumilio gene family in the genomes of Saccharomyces cerevisiae, Candida parapsilosis, and Neurospora crassa. Evolution and function of these genes can be expected from the analysis based on the molecular phylogenies.","authors":"Matsushima Y, Sugiura R, Kuno T","authors_abbrev":"Matsushima Y et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-10-13","publication_year":"2007","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26416026","title":"Mutation in WDR4 impairs tRNA m(7)G46 methylation and causes a distinct form of microcephalic primordial dwarfism.","citation":"Genome Biol 2015 Sep 28;16:210","abstract":"Primordial dwarfism is a state of extreme prenatal and postnatal growth deficiency, and is characterized by marked clinical and genetic heterogeneity.\nTwo presumably unrelated consanguineous families presented with an apparently novel form of primordial dwarfism in which severe growth deficiency is accompanied by distinct facial dysmorphism, brain malformation (microcephaly, agenesis of corpus callosum, and simplified gyration), and severe encephalopathy with seizures. Combined autozygome/exome analysis revealed a novel missense mutation in WDR4 as the likely causal variant. WDR4 is the human ortholog of the yeast Trm82, an essential component of the Trm8/Trm82 holoenzyme that effects a highly conserved and specific (m(7)G46) methylation of tRNA. The human mutation and the corresponding yeast mutation result in a significant reduction of m(7)G46 methylation of specific tRNA species, which provides a potential mechanism for primordial dwarfism associated with this lesion, since reduced m(7)G46 modification causes a growth deficiency phenotype in yeast.\nOur study expands the number of biological pathways underlying primordial dwarfism and adds to a growing list of human diseases linked to abnormal tRNA modification.","doi":"10.1186/s13059-015-0779-x","authors":"Shaheen R, Abdel-Salam GM, Guy MP, Alomar R, Abdel-Hamid MS, Afifi HH, Ismail SI, Emam BA, Phizicky EM, Alkuraya FS","authors_abbrev":"Shaheen R et al.","pubmed_publication_date":"28 Sep 2015","pubmed_entrez_date":"2015-09-30","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16358314","title":"Construction and characterization of a series of vectors for Schizosaccharomyces pombe.","citation":"Yeast 2005 Dec;22(16):1307-14","abstract":"A set of vectors was created to allow cloning and expression studies in Schizosaccharomyces pombe. These vectors had a uniform backbone with an efficient Sz. pombe ARS, ARS3002, but different selectable markers--his3+, leu1+, ade6+ and ura4+. The vectors functioned efficiently as autonomously replicating plasmids that could also be converted into integrating vectors. The ura4+-containing vector was used to construct a Sz. pombe genomic library.","authors":"Adams C, Haldar D, Kamakaka RT","authors_abbrev":"Adams C et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-12-17","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18922765","title":"Phylogenomic analyses support the monophyly of Taphrinomycotina, including Schizosaccharomyces fission yeasts.","citation":"Mol Biol Evol 2009 Jan;26(1):27-34","abstract":"Several morphologically dissimilar ascomycete fungi including Schizosaccharomyces, Taphrina, Saitoella, Pneumocystis, and Neolecta have been grouped into the taxon Taphrinomycotina (Archiascomycota or Archiascomycotina), originally based on rRNA phylogeny. These analyses lack statistically significant support for the monophyly of this grouping, and although confirmed by more recent multigene analyses, this topology is contradicted by mitochondrial phylogenies. To resolve this inconsistency, we have assembled phylogenomic mitochondrial and nuclear data sets from four distantly related taphrinomycotina taxa: Schizosaccharomyces pombe, Pneumocystis carinii, Saitoella complicata, and Taphrina deformans. Our phylogenomic analyses based on nuclear data (113 proteins) conclusively support the monophyly of Taphrinomycotina, diverging as a sister group to Saccharomycotina + Pezizomycotina. However, despite the improved taxon sampling, Taphrinomycotina continue to be paraphyletic with the mitochondrial data set (13 proteins): Schizosaccharomyces species associate with budding yeasts (Saccharomycotina) and the other Taphrinomycotina group as a sister group to Saccharomycotina + Pezizomycotina. Yet, as Schizosaccharomyces and Saccharomycotina species are fast evolving, the mitochondrial phylogeny may be influenced by a long-branch attraction (LBA) artifact. After removal of fast-evolving sequence positions from the mitochondrial data set, we recover the monophyly of Taphrinomycotina. Our combined results suggest that Taphrinomycotina is a legitimate taxon, that this group of species diverges as a sister group to Saccharomycotina + Pezizomycotina, and that phylogenetic positioning of yeasts and fission yeasts with mitochondrial data is plagued by a strong LBA artifact.","doi":"10.1093/molbev/msn221","authors":"Liu Y, Leigh JW, Brinkmann H, Cushion MT, Rodriguez-Ezpeleta N, Philippe H, Lang BF","authors_abbrev":"Liu Y et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2008-10-17","publication_year":"2009","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21700","title":"Purification of the tyrosine inhibitable 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 1977 Dec 08;485(2):446-51","abstract":"A method is described for the purification of the tyrosine inhibitable isoenzyme 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase (7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate-lyase(pyruvate phosphorylating), EC 4.1.2.15) to homogeneity as judged by polyacrylamide gel electrophoresis.","authors":"Bracher M, Schweingruber E","authors_abbrev":"Bracher M et al.","pubmed_publication_date":"08 Dec 1977","pubmed_entrez_date":"1977-12-08","publication_year":"1977","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36107819","title":"cAMP-Protein kinase A and stress-activated MAP kinase signaling mediate transcriptional control of autophagy in fission yeast during glucose limitation or starvation.","citation":"Autophagy 2023 Apr;19(4):1311-1331","abstract":"Macroautophagy/autophagy is an essential adaptive physiological response in eukaryotes induced during nutrient starvation, including glucose, the primary immediate carbon and energy source for most cells. Although the molecular mechanisms that induce autophagy during glucose starvation have been extensively explored in the budding yeast  Saccharomyces cerevisiae , little is known about how this coping response is regulated in the evolutionary distant fission yeast  Schizosaccharomyces pombe . Here, we show that  S. pombe  autophagy in response to glucose limitation relies on mitochondrial respiration and the electron transport chain (ETC), but, in contrast to  S. cerevisiae , the AMP-activated protein kinase (AMPK) and DNA damage response pathway components do not modulate fission yeast autophagic flux under these conditions. In the presence of glucose, the cAMP-protein kinase A (PKA) signaling pathway constitutively represses  S. pombe  autophagy by downregulating the transcription factor Rst2, which promotes the expression of respiratory genes required for autophagy induction under limited glucose availability. Furthermore, the stress-activated protein kinase (SAPK) signaling pathway, and its central mitogen-activated protein kinase (MAPK) Sty1, positively modulate autophagy upon glucose limitation at the transcriptional level through its downstream effector Atf1 and by direct  in vivo  phosphorylation of Rst2 at S292. Thus, our data indicate that the signaling pathways that govern autophagy during glucose shortage or starvation have evolved differently in  S. pombe  and uncover the existence of sophisticated and multifaceted mechanisms that control this self-preservation and survival response.","doi":"10.1080/15548627.2022.2125204","authors":"Pérez-Díaz AJ, Vázquez-Marín B, Vicente-Soler J, Prieto-Ruiz F, Soto T, Franco A, Cansado J, Madrid M","authors_abbrev":"Pérez-Díaz AJ et al.","pubmed_publication_date":"Apr 2023","pubmed_entrez_date":"2022-09-15","publication_year":"2023","canto_session_key":"80b89071063fc4bc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-09-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC6F12.02","SPAC24B11.06c","SPBC106.10"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:2174117","title":"Two related families of retrotransposons from Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1990 Dec;10(12):6791-8","abstract":"Two related families of transposons were isolated from schizosaccharomyces pombe, an organism which has been the object of extensive genetic studies which had previously produced no evidence for the existence of such elements. These two classes of repeated DNAs, dubbed Tf1 (transposon of fission yeast 1) and Tf2 have many properties of retrotransposons. Tf1 and Tf2 both possess long terminal repeats and predicted protein sequences that resemble the protease, reverse transcriptase, and integrase domains of retroviruses. The chromosomal locations and total numbers of Tf1 and Tf2 differ greatly in various isolates of S. pombe. The Tf elements are expressed in the form of 4.5-kb mRNAs. The complete sequence of Tf1 was determined and suggests that a novel mechanism for regulating its gene expression may be used.","authors":"Levin HL, Weaver DC, Boeke JD","authors_abbrev":"Levin HL et al.","pubmed_publication_date":"Dec 1990","pubmed_entrez_date":"1990-12-01","publication_year":"1990","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33956138","title":"Genome-wide screening of genes associated with momilactone B sensitivity in the fission yeast Schizosaccharomyces pombe.","citation":"G3 (Bethesda) 2021 Aug 07;11(8)","abstract":"Momilactone B is a natural product with dual biological activities, including antimicrobial and allelopathic properties, and plays a major role in plant chemical defense against competitive plants and pathogens. The pharmacological effects of momilactone B on mammalian cells have also been reported. However, little is known about the molecular and cellular mechanisms underlying its broad bioactivity. In this study, the genetic determinants of momilactone B sensitivity in yeast were explored to gain insight into its mode of action. We screened fission yeast mutants resistant to momilactone B from a pooled culture containing genome-wide gene-overexpressing strains in a drug-hypersensitive genetic background. Overexpression of pmd1, bfr1, pap1, arp9, or SPAC9E9.06c conferred resistance to momilactone B. In addition, a drug-hypersensitive, barcoded deletion library was newly constructed and the genes that imparted altered sensitivity to momilactone B upon deletion were identified. Gene Ontology and fission yeast phenotype ontology enrichment analyses predicted the biological pathways related to the mode of action of momilactone B. The validation of predictions revealed that momilactone B induced abnormal phenotypes such as multiseptated cells and disrupted organization of the microtubule structure. This is the first investigation of the mechanism underlying the antifungal activity of momilactone B against yeast. The results and datasets obtained in this study narrow the possible targets of momilactone B and facilitate further studies regarding its mode of action.","doi":"10.1093/g3journal/jkab156","authors":"Tomita K, Yashiroda Y, Matsuo Y, Piotrowski JS, Li SC, Okamoto R, Yoshimura M, Kimura H, Kawamura Y, Kawamukai M, Boone C, Yoshida M, Nojiri H, Okada K","authors_abbrev":"Tomita K et al.","pubmed_publication_date":"07 Aug 2021","pubmed_entrez_date":"2021-05-06","publication_year":"2021","canto_session_key":"8825323d2460dd0f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11709167","title":"Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe.","citation":"Structure 2001 Nov;9(11):1029-41","abstract":"After activation, small GTPases such as Ras transfer the incoming signal to effectors by specifically interacting with the binding domain of these proteins. Structural details of the binding domain of different effectors determine which pathway is predominantly activated. Byr2 from fission yeast is a functional homolog of Raf, which is the direct downstream target of Ras in mammalians that initiates a protein kinase cascade. The amino acid sequence of Byr2's Ras binding domain is only weakly related to that of Raf, and Byr2's three-dimensional structure is unknown.\nWe have solved the 3D structure of the Ras binding domain of Byr2 (Byr2RBD) from Schizosaccharomyces pombe in solution. The structure consists of three alpha helices and a mixed five-stranded beta pleated sheet arranged in the topology betabetaalphabetabetaalphabetaalpha with the first seven canonic secondary structure elements forming a ubiquitin superfold. 15N-(1)H-TROSY-HSQC spectroscopy of the complex of Byr2RBD with Ras*Mg(2+)*GppNHp reveals that the first and second beta strands and the first alpha helix of Byr2 are mainly involved in the protein-protein interaction as observed in other Ras binding domains. Although the putative interaction site of H-Ras from human and Ras1 from S. pombe are identical in sequence, binding to Byr2 leads to small but significant differences in the NMR spectra, indicating a slightly different binding mode.\nThe ubiquitin superfold appears to be the general structural motif for Ras binding domains even in cases with vanishing sequence identity. However, details of the 3D structure and the interacting interface are different, thereby determining the specifity of the recognition of Ras and Ras-related proteins.","authors":"Gronwald W, Huber F, Grünewald P, Spörner M, Wohlgemuth S, Herrmann C, Kalbitzer HR","authors_abbrev":"Gronwald W et al.","pubmed_publication_date":"Nov 2001","pubmed_entrez_date":"2001-11-16","publication_year":"2001","canto_session_key":"394ee4139d392a24","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-05-20 14:25:59","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-05-20 14:25:53","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC1D7.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-05-20","pdb_entries":[{"pdb_id":"1i35","gene_chains":[{"gene_uniquename":"SPBC1D7.05","chain":"A","position":"71-165"}],"title":"SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF THE PROTEIN KINASE BYR2 FROM SCHIZOSACCHAROMYCES POMBE","entry_authors":"Gronwald W,Huber F,Grunewald P,Sporner M,Wohlgemuth S,Herrmann C,Kalbitzer HR","entry_authors_abbrev":"Gronwald W et al.","reference_uniquename":"PMID:11709167","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:21199192","title":"Fission yeast ATF/CREB family protein Atf21 plays important roles in production of normal spores.","citation":"Genes Cells 2011 Feb;16(2):217-30","abstract":"Activating transcription factor/cAMP response element binding protein (ATF/CREB) family transcription factors play central roles in maintaining cellular homeostasis. They are activated in response to environmental stimuli, bind to CRE sequences in the promoters of stress-response genes and regulate transcription. Although ATF/CREB proteins are widely conserved among most eukaryotes, their characteristics are highly diverse. Here, we investigated the functions of a fission yeast ATF/CREB protein Atf21 to find out its unique properties. We show that Atf21 is dispensable for the adaptive response to several stresses such as nitrogen starvation and for meiotic events including nuclear divisions. However, spores derived from atf21Δ mutants are not as mature as wild-type ones and are unable to form colonies under nutrition-rich conditions. Furthermore, we demonstrate that the Atf21 protein, which is scarce in early meiosis, gradually accumulates as meiosis proceeds; it reaches maximum levels approximately 8 h after nitrogen starvation and is present during germination. These results suggest that Atf21 is expressed and functions long after nitrogen starvation. Given that other well-characterized fission yeast ATF/CREB proteins Atf1 and Pcr1 accumulate and function promptly upon exposure to environmental stresses, we propose that Atf21 is a distinct member of the ATF/CREB family in fission yeast.","doi":"10.1111/j.1365-2443.2010.01480.x","authors":"Morita T, Yamada T, Yamada S, Matsumoto K, Ohta K","authors_abbrev":"Morita T et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2011-01-05","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23974178","title":"Genome architecture is a selectable trait that can be maintained by antagonistic pleiotropy.","citation":"Nat Commun 2013;4:2235","abstract":"Chromosomal rearrangements are mutations contributing to both within and between species variation; however their contribution to fitness is yet to be measured. Here we show that chromosomal rearrangements are pervasive in natural isolates of Schizosaccharomyces pombe and contribute to reproductive isolation. To determine the fitness effects of chromosome structure, we constructed two inversions and eight translocations without changing the coding sequence. We show that chromosomal rearrangements contribute to both reproductive success in meiosis and growth rate in mitosis with a strong genotype by environment interaction. These changes are accompanied by alterations in gene expression. Strikingly, we find several examples leading to antagonistic pleiotropy. Even though chromosomal rearrangements may have a deleterious effect during sexual reproduction, some compensate with a strong growth advantage in mitosis. Our results constitute the first quantification of fitness effects caused by de novo mutations that result in chromosomal rearrangement variation and suggest a mechanism for their maintenance in natural populations.","doi":"10.1038/ncomms3235","authors":"Avelar AT, Perfeito L, Gordo I, Ferreira MG","authors_abbrev":"Avelar AT et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-08-27","publication_year":"2013","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2013-10-09 03:17:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3409871","title":"Cold-sensitive and caffeine-supersensitive mutants of the Schizosaccharomyces pombe dis genes implicated in sister chromatid separation during mitosis.","citation":"EMBO J 1988 May;7(5):1465-73","abstract":"We isolated novel classes of Schizosaccharomyces pombe cold-sensitive dis mutants that block mitotic chromosome separation (nine mapped in the dis1 gene and one each in the dis2 and dis3 genes). Defective phenotype at restrictive temperature is similar among the mutants; the chromosomes condense and anomalously move to the cell ends in the absence of their disjoining so that they are unequally distributed at the two cell ends. Synchronous culture analyses indicate that the cells can enter into mitosis at normal timing but become lethal during mitosis. In comparison with the wild-type mitosis, defects are found in the early spindle structure, the mitotic chromosome structure, the poleward chromosome movement by the spindle elongation and the telophase spindle degradation. The dis mutants lose at permissive temperature an artificial minichromosome at higher rates than occur in the wild type. We found that all the dis mutants isolated are supersensitive to caffeine at permissive temperature. Furthermore, the mutant cells in the presence of caffeine produce a phenotype similar to that obtained at restrictive temperature. We suggest that the dis genes are required for the sister chromatid separation at the time of mitosis and that caffeine might affect the dis gene expression. We cloned, in addition to the dis2+ and dis3+ genes, multicopy extragenic suppressor sequences which complement dis1 and dis2 mutations. A complex regulatory system may exist for the execution of the dis+ gene functions.","authors":"Ohkura H, Adachi Y, Kinoshita N, Niwa O, Toda T, Yanagida M","authors_abbrev":"Ohkura H et al.","pubmed_publication_date":"May 1988","pubmed_entrez_date":"1988-05-01","publication_year":"1988","canto_session_key":"3e76f432dc79dfae","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-02-08 15:40:41","canto_approved_date":"2026-01-31 13:07:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-10 15:04:37","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.10","SPBC26H8.07c","SPCC736.14","SPAC17C9.01c","SPBC16A3.15c","SPBC776.02c"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2016-02-08"},{"uniquename":"PMID:12697825","title":"Ste11p, a high-mobility-group box DNA-binding protein, undergoes pheromone- and nutrient-regulated nuclear-cytoplasmic shuttling.","citation":"Mol Cell Biol 2003 May;23(9):3253-64","abstract":"The high-mobility-group (HMG) box is a conserved DNA-binding domain found in a family of transcription factors that regulate growth and development. One family member, Ste11p, directs sexual differentiation of Schizosaccharomyces pombe by binding specific DNA sequences upstream of genes required for mating and meiosis. Here, we show that Ste11p is a shuttling protein. In growing cells, Ste11p is present in low levels and is pancellular. Mating pheromones and nutrient limitation trigger nuclear accumulation and increased expression of the transcription factor. Several mechanisms likely control Ste11p localization. First, the 14-3-3 protein, Rad24p, binds phosphorylated Ste11p and inhibits its nuclear accumulation. Second, the HMG domain of Ste11p contains a basic cluster nuclear localization signal. Finally, treatment of cells with leptomycin B, an exportin inhibitor, results in the nuclear accumulation of Ste11p. A Ste11p deletion mutation, DeltaC54, mimics the effects of leptomycin B. The C54 region contains no identifiable nuclear export signal but instead is required for biological activity and to stimulate Ste11p target gene expression. These results provide evidence that both nuclear import and export mechanisms operate to regulate cellular localization of an HMG box protein. In addition, they establish a paradigm for the potential role of pheromone/hormone-like polypeptides in cellular localization of this important class of developmental regulators.","authors":"Qin J, Kang W, Leung B, McLeod M","authors_abbrev":"Qin J et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-04-17","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32C12.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26392826","title":"Visualizing the entire DNA from a chromosome in a single frame.","citation":"Biomicrofluidics 2015 Jul;9(4):044114","abstract":"The contiguity and phase of sequence information are intrinsic to obtain complete understanding of the genome and its relationship to phenotype. We report the fabrication and application of a novel nanochannel design that folds megabase lengths of genomic DNA into a systematic back-and-forth meandering path. Such meandering nanochannels enabled us to visualize the complete 5.7 Mbp (1 mm) stained DNA length of a Schizosaccharomyces pombe chromosome in a single frame of a CCD. We were able to hold the DNA in situ while implementing partial denaturation to obtain a barcode pattern that we could match to a reference map using the Poland-Scheraga model for DNA melting. The facility to compose such long linear lengths of genomic DNA in one field of view enabled us to directly visualize a repeat motif, count the repeat unit number, and chart its location in the genome by reference to unique barcode motifs found at measurable distances from the repeat. Meandering nanochannel dimensions can easily be tailored to human chromosome scales, which would enable the whole genome to be visualized in seconds.","doi":"10.1063/1.4923262","authors":"Freitag C, Noble C, Fritzsche J, Persson F, Reiter-Schad M, Nilsson AN, Granéli A, Ambjörnsson T, Mir KU, Tegenfeldt JO","authors_abbrev":"Freitag C et al.","pubmed_publication_date":"Jul 2015","pubmed_entrez_date":"2015-09-23","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-09-25 00:19:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36782025","title":"Phase separation in fungi.","citation":"Nat Microbiol 2023 Mar;8(3):375-386","abstract":"Phase separation, in which macromolecules partition into a concentrated phase that is immiscible with a dilute phase, is involved with fundamental cellular processes across the tree of life. We review the principles of phase separation and highlight how it impacts diverse processes in the fungal kingdom. These include the regulation of autophagy, cell signalling pathways, transcriptional circuits and the establishment of asymmetry in fungal cells. We describe examples of stable, phase-separated assemblies including membraneless organelles such as the nucleolus as well as transient condensates that also arise through phase separation and enable cells to rapidly and reversibly respond to important environmental cues. We showcase how research into phase separation in model yeasts, such as Saccharomyces cerevisiae and Schizosaccharomyces pombe, in conjunction with that in plant and human fungal pathogens, such as Ashbya gossypii and Candida albicans, is continuing to enrich our understanding of fundamental molecular processes.","doi":"10.1038/s41564-022-01314-6","authors":"Staples MI, Frazer C, Fawzi NL, Bennett RJ","authors_abbrev":"Staples MI et al.","pubmed_publication_date":"Mar 2023","pubmed_entrez_date":"2023-02-13","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-02-15 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17030601","title":"Smc5/6 is required for repair at collapsed replication forks.","citation":"Mol Cell Biol 2006 Dec;26(24):9387-401","abstract":"In eukaryotes, three pairs of structural-maintenance-of-chromosome (SMC) proteins are found in conserved multisubunit protein complexes required for chromosomal organization. Cohesin, the Smc1/3 complex, mediates sister chromatid cohesion while two condensin complexes containing Smc2/4 facilitate chromosome condensation. Smc5/6 scaffolds an essential complex required for homologous recombination repair. We have examined the response of smc6 mutants to the inhibition of DNA replication. We define homologous recombination-dependent and -independent functions for Smc6 during replication inhibition and provide evidence for a Rad60-independent function within S phase, in addition to a Rad60-dependent function following S phase. Both genetic and physical data show that when forks collapse (i.e., are not stabilized by the Cds1Chk2 checkpoint), Smc6 is required for the effective repair of resulting lesions but not for the recruitment of recombination proteins. We further demonstrate that when the Rad60-dependent, post-S-phase Smc6 function is compromised, the resulting recombination-dependent DNA intermediates that accumulate following release from replication arrest are not recognized by the G2/M checkpoint.","authors":"Ampatzidou E, Irmisch A, O'Connell MJ, Murray JM","authors_abbrev":"Ampatzidou E et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-10-13","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22039153","title":"PomBase: a comprehensive online resource for fission yeast.","citation":"Nucleic Acids Res 2012 Jan;40(Database issue):D695-9","abstract":"PomBase (www.pombase.org) is a new model organism database established to provide access to comprehensive, accurate, and up-to-date molecular data and biological information for the fission yeast Schizosaccharomyces pombe to effectively support both exploratory and hypothesis-driven research. PomBase encompasses annotation of genomic sequence and features, comprehensive manual literature curation and genome-wide data sets, and supports sophisticated user-defined queries. The implementation of PomBase integrates a Chado relational database that houses manually curated data with Ensembl software that supports sequence-based annotation and web access. PomBase will provide user-friendly tools to promote curation by experts within the fission yeast community. This will make a key contribution to shaping its content and ensuring its comprehensiveness and long-term relevance.","doi":"10.1093/nar/gkr853","authors":"Wood V, Harris MA, McDowall MD, Rutherford K, Vaughan BW, Staines DM, Aslett M, Lock A, Bähler J, Kersey PJ, Oliver SG","authors_abbrev":"Wood V et al.","pubmed_publication_date":"Jan 2012","pubmed_entrez_date":"2011-11-01","publication_year":"2012","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4472733","title":"Premeiotic DNA synthesis in fission yeast.","citation":"Exp Cell Res 1974 Sep;88(1):127-34","abstract":"","authors":"Egel R, Egel-Mitani M","authors_abbrev":"Egel R et al.","pubmed_publication_date":"Sep 1974","pubmed_entrez_date":"1974-09-01","publication_year":"1974","canto_session_key":"0e2fe7100270115d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-09 14:18:02","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-09 14:17:54","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.02c","SPMTR.02","SPBC119.04"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-10-09"},{"uniquename":"PMID:31688924","title":"Intraspecies cell-cell communication in yeast.","citation":"FEMS Yeast Res 2019 Nov 01;19(7)","abstract":"Although yeasts are unicellular microorganisms that can live independently, they can also communicate with other cells, in order to adapt to the environment. Two yeast species, the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe, engage in various kinds of intraspecies cell-cell communication using peptides and chemical molecules that they produce, constituting a sort of 'language'. Cell-cell communication is a fundamental biological process, and its ultimate purpose is to promote survival by sexual reproduction and acquisition of nutrients from the environment. This review summarizes what is known about intraspecies cell-cell communication mediated by molecules including mating pheromones, volatile gases, aromatic alcohols and oxylipins in laboratory strains of S. cerevisiae and S. pombe.","doi":"10.1093/femsyr/foz071","authors":"Yashiroda Y, Yoshida M","authors_abbrev":"Yashiroda Y et al.","pubmed_publication_date":"01 Nov 2019","pubmed_entrez_date":"2019-11-06","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-11-08 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10747048","title":"Autoregulated expression of Schizosaccharomyces pombe meiosis-specific transcription factor Mei4 and a genome-wide search for its target genes.","citation":"Genetics 2000 Apr;154(4):1497-508","abstract":"The Schizosaccharomyces pombe mei4(+) gene encoding a forkhead transcription factor is necessary for the progression of meiosis and sporulation. We searched for novel meiotic genes, the expression of which is dependent on Mei4p, since only the spo6(+) gene has been assigned to its targets. Six known genes responsible for meiotic recombination were examined by Northern blotting, but none were Mei4 dependent for transcription. We determined the important cis-acting element, designated FLEX, to which Mei4p can bind. The S. pombe genome sequence database (The Sanger Centre, UK) was scanned for the central core heptamer and its flanking 3' sequence of FLEX composed of 17 nucleotides, and 10 candidate targets of Mei4 were selected. These contained a FLEX-like sequence in the 5' upstream nontranslatable region within 1 kb of the initiation codon. Northern blotting confirmed that 9 of them, named mde1(+) to mde9(+), were transcriptionally induced during meiosis and were dependent on mei4(+). Most mde genes have not been genetically defined yet, except for mde9(+), which is identical to spn5(+), which encodes one of the septin family of proteins. mde3(+) and a related gene pit1(+) encode proteins related to Saccharomyces cerevisiae Ime2. The double disruptant frequently produced asci having an abnormal number and size of spores, although it completed meiosis. We also found that the forkhead DNA-binding domain of Mei4p binds to the FLEX-like element in the putative promoter region of mei4 and that the maximum induction level of mei4 mRNA required functional mei4 activity. Furthermore, expression of a reporter gene driven by the authentic mei4 promoter was induced in vegetative cells by ectopic overproduction of Mei4p. These results suggest that mei4 transcription is positively autoregulated.","authors":"Abe H, Shimoda C","authors_abbrev":"Abe H et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-04-04","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19F8.01c","SPBC31F10.08","SPAC3C7.06c","SPBC32H8.11","SPAC16E8.05c","SPCC320.07c","SPBC8D2.19","SPBC6B1.04","SPAC25H1.09","SPBC8D2.18c","SPAC24C9.15c"],"gene_count":11,"ltp_gene_count":3},{"uniquename":"PMID:19217403","title":"Fission yeast Scm3 mediates stable assembly of Cnp1/CENP-A into centromeric chromatin.","citation":"Mol Cell 2009 Feb 13;33(3):287-98","abstract":"Mis16 and Mis18 are subunits of a protein complex required for incorporation of the histone H3 variant CenH3 (Cnp1/CENP-A) into centromeric chromatin in Schizosaccharomyces pombe and mammals. How the Mis16-Mis18 complex performs this function is unknown. Here, we report that the Mis16-Mis18 complex is required for centromere localization of Scm3(Sp), a Cnp1-binding protein related to Saccharomyces cerevisiae Scm3. Scm3(Sp) is required for centromeric localization of Cnp1, while Scm3(Sp) localizes at centromeres independently of Cnp1. Like the Mis16-Mis18 complex but unlike Cnp1, Scm3(Sp) dissociates from centromeres during mitosis. Inactivation of Scm3(Sp) or Mis18 increases centromere localization of histones H3 and H2A/H2B, which are largely absent from centromeres in wild-type cells. Whereas S. cerevisiae Scm3 is proposed to replace histone H2A/H2B in centromeric nucleosomes, the dynamic behavior of S. pombe Scm3 suggests that it acts as a Cnp1 assembly/maintenance factor that directly mediates the stable deposition of Cnp1 into centromeric chromatin.","doi":"10.1016/j.molcel.2009.01.017","authors":"Williams JS, Hayashi T, Yanagida M, Russell P","authors_abbrev":"Williams JS et al.","pubmed_publication_date":"13 Feb 2009","pubmed_entrez_date":"2009-02-17","publication_year":"2009","canto_session_key":"dc80ed40f3a61b23","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-05 14:24:46","canto_approved_date":"2022-11-03 14:01:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-01-04 21:25:38","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":101,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPCC622.09","SPBC8D2.04","SPBC21.01","SPBP22H7.09c","SPAC1687.20c","SPCC1672.10","SPBC1105.17","SPAC688.02c","SPBC409.04c","SPAC1834.04","SPAPB1A10.02","SPCC970.12","SPBC1105.11c"],"gene_count":14,"ltp_gene_count":10,"approved_date":"2017-01-05"},{"uniquename":"PMID:12049653","title":"Role of ATP-binding motifs on DNA-binding activity and biological function of Rhp51, a Rad51 homologue in fission yeast.","citation":"Biochem J 2002 Jun 15;364(Pt 3):869-74","abstract":"Rhp51, a RecA and Rad51 homologue of Schizosaccharomyces pombe, plays a pivotal role in homologous recombination and recombinational repair. It has a set of the well-conserved type A and type B ATP-binding motifs, which are highly conserved in all RecA homologues. In a previous study [Kim, Lee, Park, Park and Park (2001) Nucleic Acids Res. 29, 1724-1732], we reported that a single mutation of the conserved lysine in A motif [Lys(155)-->Ala (K155A)] destroyed the DNA repair ability of Rhp51 and that overexpression of this mutant protein conferred dominant negativity. In the present paper, we investigated DNA-binding properties of recombinant Rhp51 and its mutant proteins. Purified Rhp51 protein showed ATP-dependent double- and single-strand DNA-binding activities. To characterize the role of ATP-binding motifs, we generated Rhp51 K155A and Rhp51 Asp(244)-->Gln (D244Q), which have a single amino acid substitution in A and B motifs respectively. Interestingly, K155A and D244Q mutations impaired ATP-dependent DNA binding in a different manner. K155A lost the DNA binding itself, whereas D244Q maintained the binding ability but lost the ATP dependency. However, despite the difference in DNA-binding ability, both mutations failed to rescue the methylmethane sulphonate and UV sensitivity of the rhp51Delta mutant. Together, these results suggested that not only the DNA binding but also the ATP dependence in DNA binding is required for proper in vivo functioning of Rhp51.","authors":"Kim WJ, Lee H, Park EJ, Hong SH, Park SD","authors_abbrev":"Kim WJ et al.","pubmed_publication_date":"15 Jun 2002","pubmed_entrez_date":"2002-06-07","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9455919","title":"Aspartic acid 252 and asparagine 185 are essential for activity of lipid N-acetylglucosaminylphosphate transferase.","citation":"Glycobiology 1997 Dec;7(8):1181-91","abstract":"A key step in the assembly of oligosaccharide-lipid intermediates in N-linked glycosylation is the transfer of N-acetylglucosamine 1-phosphate to dolichyl phosphate, catalyzed by the enzyme UDP-N-acetylglucosaminyl:dolichyl phosphate N-acetylglucosaminyl phosphoryl transferase (L-G1PT). Comparison of the amino acid sequences of L-G1PT from five diverse species showed 75 amino acids identical in all five proteins. Using site-directed mutagenesis, we analyzed the importance of a number of these conserved residues to the enzymatic activity of L-G1PT using a plasmid shuffling procedure in Schizosaccharomyces pombe. S. pombe cells containing a chromosomal deletion of the essential gpt+ gene are rescued by a plasmid containing the S. pombe gpt open reading frame. Replacement of that plasmid by a plasmid encoding a mutated hamster L-G1PT cDNA sequence indicated that the mutated protein provided sufficient enzyme activity to permit cell growth. Mutations of aspartic acid 252 and asparagine 185 did not allow plasmid shuffling, indicating these residues were essential for activity. A combination of mutations at asparagine 182 and tryptophan 122 did not allow plasmid shuffling, although the single mutations did. Overexpression of the mutant proteins in S. pombe conferred tunicamycin (TM) resistance, indicating that the mutant proteins had a conformation necessary for binding TM, a substrate analog. The mutant proteins were also detected in Western blots and were correctly localized to the membrane fractions. However, the overexpressed proteins did not increase the endogenous level of enzymatic activity in these cells, indicating they were enzymatically inactive.","authors":"Scocca JR, Krag SS","authors_abbrev":"Scocca JR et al.","pubmed_publication_date":"Dec 1997","pubmed_entrez_date":"1998-02-10","publication_year":"1997","canto_session_key":"795b4de655831d91","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-02-28 14:03:38","canto_approved_date":"2024-06-30 20:04:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-28 14:03:30","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC15D4.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-02-28"},{"uniquename":"PMID:18378776","title":"The Clp1/Cdc14 phosphatase contributes to the robustness of cytokinesis by association with anillin-related Mid1.","citation":"J Cell Biol 2008 Apr 07;181(1):79-88","abstract":"Cdc14 phosphatases antagonize cyclin-dependent kinase-directed phosphorylation events and are involved in several facets of cell cycle control. We investigate the role of the fission yeast Cdc14 homologue Clp1/Flp1 in cytokinesis. We find that Clp1/Flp1 is tethered at the contractile ring (CR) through its association with anillin-related Mid1. Fluorescent recovery after photobleaching analyses indicate that Mid1, unlike other tested CR components, is anchored at the cell midzone, and this physical property is likely to account for its scaffolding role. By generating a mutation in mid1 that selectively disrupts Clp1/Flp1 tethering, we reveal the specific functional consequences of Clp1/Flp1 activity at the CR, including dephosphorylation of the essential CR component Cdc15, reductions in CR protein mobility, and CR resistance to mild perturbation. Our evidence indicates that Clp1/Flp1 must interact with the Mid1 scaffold to ensure the fidelity of Schizosaccharomyces pombe cytokinesis.","doi":"10.1083/jcb.200709060","authors":"Clifford DM, Wolfe BA, Roberts-Galbraith RH, McDonald WH, Yates JR, Gould KL","authors_abbrev":"Clifford DM et al.","pubmed_publication_date":"07 Apr 2008","pubmed_entrez_date":"2008-04-02","publication_year":"2008","canto_session_key":"3c126315549fc38f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-11-20 19:53:01","canto_approved_date":"2026-02-14 08:40:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-27 15:21:14","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":51,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.05c","SPBC19G7.05c","SPAC1782.09c","SPAC926.03","SPAC1F5.04c","SPAC20G8.05c","SPAC23C11.16","SPAC4A8.15c","SPCC4B3.15"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2018-11-20"},{"uniquename":"PMID:28667014","title":"The gluconate shunt is an alternative route for directing glucose into the pentose phosphate pathway in fission yeast.","citation":"J Biol Chem 2017 Aug 18;292(33):13823-13832","abstract":"Glycolysis and the pentose phosphate pathway both play a central role in the degradation of glucose in all domains of life. Another metabolic route that can facilitate glucose breakdown is the gluconate shunt. In this shunt glucose dehydrogenase and gluconate kinase catalyze the two-step conversion of glucose into the pentose phosphate pathway intermediate 6-phosphogluconate. Despite the presence of these enzymes in many organisms, their only established role is in the production of 6-phosphogluconate for the Entner-Doudoroff pathway. In this report we performed metabolic profiling on a strain of  Schizosaccharomyces pombe  lacking the zinc-responsive transcriptional repressor Loz1 with the goal of identifying metabolic pathways that were altered by cellular zinc status. This profiling revealed that  loz1 Δ cells accumulate higher levels of gluconate. We show that the altered gluconate levels in  loz1 Δ cells result from increased expression of  gcd1  By analyzing the activity of recombinant Gcd1  in vitro  and by measuring gluconate levels in strains lacking enzymes of the gluconate shunt we demonstrate that Gcd1 encodes a novel NADP + -dependent glucose dehydrogenase that acts in a pathway with the Idn1 gluconate kinase. We also find that cells lacking  gcd1  and  zwf1 , which encode the first enzyme in the pentose phosphate pathway, have a more severe growth phenotype than cells lacking  zwf1  We propose that in  S. pombe  Gcd1 and Idn1 act together to shunt glucose into the pentose phosphate pathway, creating an alternative route for directing glucose into the pentose phosphate pathway that bypasses hexokinase and the rate-limiting enzyme glucose-6-phosphate dehydrogenase.","doi":"10.1074/jbc.M117.798488","authors":"Corkins ME, Wilson S, Cocuron JC, Alonso AP, Bird AJ","authors_abbrev":"Corkins ME et al.","pubmed_publication_date":"18 Aug 2017","pubmed_entrez_date":"2017-07-02","publication_year":"2017","canto_session_key":"2041b5cb2443f86c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Stevin Wilson","canto_approved_date":"2017-08-02 15:51:10","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-07-27 10:39:10","canto_added_date":"2017-07-03 00:15:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Stevin Wilson","community_curator":true,"annotation_count":24,"orcid":"0000-0002-9662-5501","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25B8.19c","SPAC3A12.18","SPAC4G9.12","SPCC794.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-07-27"},{"uniquename":"EMBL:SPD139","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29596413","title":"Lack of 2'-O-methylation in the tRNA anticodon loop of two phylogenetically distant yeast species activates the general amino acid control pathway.","citation":"PLoS Genet 2018 Mar;14(3):e1007288","abstract":"Modification defects in the tRNA anticodon loop often impair yeast growth and cause human disease. In the budding yeast Saccharomyces cerevisiae and the phylogenetically distant fission yeast Schizosaccharomyces pombe, trm7Δ mutants grow poorly due to lack of 2'-O-methylation of C32 and G34 in the tRNAPhe anticodon loop, and lesions in the human TRM7 homolog FTSJ1 cause non-syndromic X-linked intellectual disability (NSXLID). However, it is unclear why trm7Δ mutants grow poorly. We show here that despite the fact that S. cerevisiae trm7Δ mutants had no detectable tRNAPhe charging defect in rich media, the cells constitutively activated a robust general amino acid control (GAAC) response, acting through Gcn2, which senses uncharged tRNA. Consistent with reduced available charged tRNAPhe, the trm7Δ growth defect was suppressed by spontaneous mutations in phenylalanyl-tRNA synthetase (PheRS) or in the pol III negative regulator MAF1, and by overexpression of tRNAPhe, PheRS, or EF-1A; all of these also reduced GAAC activation. Genetic analysis also demonstrated that the trm7Δ growth defect was due to the constitutive robust GAAC activation as well as to the reduced available charged tRNAPhe. Robust GAAC activation was not observed with several other anticodon loop modification mutants. Analysis of S. pombe trm7 mutants led to similar observations. S. pombe Trm7 depletion also resulted in no observable tRNAPhe charging defect and a robust GAAC response, and suppressors mapped to PheRS and reduced GAAC activation. We speculate that GAAC activation is widely conserved in trm7 mutants in eukaryotes, including metazoans, and might play a role in FTSJ1-mediated NSXLID.","doi":"10.1371/journal.pgen.1007288","authors":"Han L, Guy MP, Kon Y, Phizicky EM","authors_abbrev":"Han L et al.","pubmed_publication_date":"Mar 2018","pubmed_entrez_date":"2018-03-30","publication_year":"2018","canto_session_key":"d84353df94449c44","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-07-29 16:36:23","canto_approved_date":"2024-12-11 22:42:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-03 11:34:42","canto_added_date":"2018-03-31 00:15:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC56E4.03","SPAC3G9.06","SPATRNAPHE.01","SPBC1773.13","SPBC1105.02c","SPBC1306.02","SPAC4F10.03c","SPCC1494.07","SPAC23A1.12c","SPBC25D12.05"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2019-07-29"},{"uniquename":"PMID:16857197","title":"The fission yeast Map4 protein is a novel adhesin required for mating.","citation":"FEBS Lett 2006 Aug 07;580(18):4457-62","abstract":"Cell adhesion is required for many cellular processes. In fungi, cell-cell contact during mating, flocculation or virulence is mediated by adhesins, which typically are glycosyl phosphatidyl inositol (GPI)-modified cell wall glycoproteins. Proteins with internal repeats (PIR) are surface proteins involved in the response to stress. In Schizosaccharomyces pombe no adhesins or PIR proteins have been described. Here we study the S. pombe Map4p, which defines a new class of surface protein that is not GPI-modified and has a serine/threonine rich domain and internal repeats that differ from those present in PIR proteins. Map4p is a mating type-specific adhesin required for mating in h(+) cells and enhances cell adhesion when overexpressed.","authors":"Sharifmoghadam MR, Bustos-Sanmamed P, Valdivieso MH","authors_abbrev":"Sharifmoghadam MR et al.","pubmed_publication_date":"07 Aug 2006","pubmed_entrez_date":"2006-07-22","publication_year":"2006","canto_session_key":"be24c30941f300dc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-21 12:14:18","canto_approved_date":"2026-01-01 19:02:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-20 09:10:34","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21D10.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-11-21"},{"uniquename":"PMID:9649518","title":"A screen for genes involved in the anaphase proteolytic pathway identifies tsm1(+), a novel Schizosaccharomyces pombe gene important for microtubule integrity.","citation":"Genetics 1998 Jul;149(3):1251-64","abstract":"The growth of several mitotic mutants of Schizosaccharomyces pombe, including nuc2-663, is inhibited by the protease inhibitor N-Tosyl-L-Phenylalanine Chloromethyl Ketone (TPCK). Because nuc2(+) encodes a presumptive component of the Anaphase Promoting Complex, which is required for the ubiquitin-dependent proteolysis of certain proteins during exit from mitosis, we have used sensitivity to TPCK as a criterion by which to search for novel S. pombe mutants defective in the anaphase-promoting pathway. In a genetic screen for temperature-sensitive mitotic mutants that were also sensitive to TPCK at a permissive temperature, we isolated three tsm (TPCK-sensitive mitotic) strains. Two of these are alleles of cut1(+), but tsm1-512 maps to a novel genetic location. The tsm1-512 mutation leads to delayed nuclear division at restrictive temperatures, apparently as a result of an impaired ability to form a metaphase spindle. After shift of early G2 cells to 36 degrees, tsm1-512 arrests transiently in the second mitotic division and then exits mitosis, as judged by spindle elongation and septation. The chromosomes, however, often fail to segregate properly. Genetic interactions between tsm1-512 and components of the anaphase proteolytic pathway suggest a functional involvement of the Tsm1 protein in this pathway.","authors":"Grishchuk EL, Howe JL, McIntosh JR","authors_abbrev":"Grishchuk EL et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-07-03","publication_year":"1998","canto_session_key":"608b9b753b7c64f3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-04-19 17:50:58","canto_approved_date":"2026-01-29 19:11:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-19 17:50:34","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC962.03c","SPBC11C11.04c","SPCC5E4.04","SPBC16A3.15c","SPAC56E4.04c","SPAC20G8.05c","SPAC17C9.01c","SPBC11B10.09"],"gene_count":8,"ltp_gene_count":6,"approved_date":"2016-04-19"},{"uniquename":"PMID:15710398","title":"Msp1p is an intermembrane space dynamin-related protein that mediates mitochondrial fusion in a Dnm1p-dependent manner in S. pombe.","citation":"FEBS Lett 2005 Feb 14;579(5):1109-16","abstract":"Mitochondrial morphology is controlled by large GTPases, such as Msp1p, whose action on mitochondrial membranes is not yet understood. The sub-mitochondrial localization of Msp1p, the subject of ongoing controversies, was found to be within the intermembrane space. Overexpression of Msp1p led to aggregation of the mitochondrial network, while its downregulation resulted in fragmentation of this network. Mutations affecting the integrity of the Msp1p GTPase function had a dominant phenotype and induced mitochondrial fragmentation followed by mitochondrial DNA loss and cell death. These effects were not observed in cells deleted for Dnm1p, an actor in mitochondrial fission, suggesting that Msp1p is involved in the fusion of mitochondria.","authors":"Guillou E, Bousquet C, Daloyau M, Emorine LJ, Belenguer P","authors_abbrev":"Guillou E et al.","pubmed_publication_date":"14 Feb 2005","pubmed_entrez_date":"2005-02-16","publication_year":"2005","canto_session_key":"f15fd8abedae83c7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-09-01 17:59:45","canto_approved_date":"2025-09-03 14:13:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-08-17 21:27:12","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.06","SPBC12C2.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-09-01"},{"uniquename":"PMID:34910589","title":"A model of actin-driven endocytosis explains differences of endocytic motility in budding and fission yeast.","citation":"Mol Biol Cell 2022 Mar 01;33(3):ar16","abstract":"A comparative study (Sun  et al. , 2019) showed that the abundance of proteins at sites of endocytosis in fission and budding yeast is more similar in the two species than previously thought, yet membrane invaginations in fission yeast elongate twofold faster and are nearly twice as long as in budding yeast. Here we use a three-dimensional model of a motile endocytic invagination (Nickaeen  et al. , 2019) to investigate factors affecting elongation of the invaginations. We found that differences in turgor pressure in the two yeast species can largely explain the paradoxical differences observed experimentally in endocytic motility.","doi":"10.1091/mbc.E21-07-0362","authors":"Nickaeen M, Berro J, Pollard TD, Slepchenko BM","authors_abbrev":"Nickaeen M et al.","pubmed_publication_date":"01 Mar 2022","pubmed_entrez_date":"2021-12-15","publication_year":"2022","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2021-12-17 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38833506","title":"A systematic screen identifies Saf5 as a link between splicing and transcription in fission yeast.","citation":"PLoS Genet 2024 Jun 04;20(6):e1011316","abstract":"Splicing is an important step of gene expression regulation in eukaryotes, as there are many mRNA precursors that can be alternatively spliced in different tissues, at different cell cycle phases or under different external stimuli. We have developed several integrated fluorescence-based in vivo splicing reporter constructs that allow the quantification of fission yeast splicing in vivo on intact cells, and we have compared their splicing efficiency in a wild type strain and in a prp2-1 (U2AF65) genetic background, showing a clear dependency between Prp2 and a consensus signal at 5' splicing site (5'SS). To isolate novel genes involved in regulated splicing, we have crossed the reporter showing more intron retention with the Schizosaccharomyces pombe knock out collection. Among the candidate genes involved in the regulation of splicing, we have detected strong splicing defects in two of the mutants -Δcwf12, a member of the NineTeen Complex (NTC) and Δsaf5, a methylosome subunit that acts together with the survival motor neuron (SMN) complex in small nuclear ribonucleoproteins (snRNP) biogenesis. We have identified that strains with mutations in cwf12 have inefficient splicing, mainly when the 5'SS differs from the consensus. However, although Δsaf5 cells also have some dependency on 5'SS sequence, we noticed that when one intron of a given pre-mRNA was affected, the rest of the introns of the same pre-mRNA had high probabilities of being also affected. This observation points Saf5 as a link between transcription rate and splicing.","doi":"10.1371/journal.pgen.1011316","authors":"Borao S, Vega M, Boronat S, Hidalgo E, Hümmer S, Ayté J","authors_abbrev":"Borao S et al.","pubmed_publication_date":"04 Jun 2024","pubmed_entrez_date":"2024-06-04","publication_year":"2024","canto_session_key":"da18465232a360d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Montserrat Vega","canto_first_approved_date":"2024-12-30 17:14:32","canto_approved_date":"2026-02-19 10:10:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-29 19:22:32","canto_added_date":"2024-06-04 23:25:05","annotation_curators":[{"name":"Montserrat Vega","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC663.11","SPBC32F12.05c","SPBC32H8.10","SPAC30D11.09","SPAC1610.01","SPCC736.12c","SPAC1705.02","SPAC23C11.10","SPBC146.07"],"gene_count":9,"ltp_gene_count":7,"approved_date":"2024-12-30"},{"uniquename":"PMID:19646873","title":"The conserved NDR kinase Orb6 controls polarized cell growth by spatial regulation of the small GTPase Cdc42.","citation":"Curr Biol 2009 Aug 11;19(15):1314-9","abstract":"The conserved NDR kinase regulates cell morphogenesis and polarized cell growth in different eukaryotic cells ranging from yeast to neurons. Although studies have unraveled the mechanism of regulation of NDR kinase activity, the mechanism of morphology control by NDR and the effectors that mediate NDR function are unknown. Via a chemical genetic approach, we show that the fission yeast NDR homolog, Orb6 kinase, maintains polarized cell growth at the cell tips by spatially regulating the localization of Cdc42 GTPase, a key morphology regulator. Loss of Orb6 kinase activity leads to the recruitment of Cdc42 GTPase and the Cdc42-dependent formin For3, normally found only at the cell tips, to the cell sides. Furthermore, we show that loss of Orb6 kinase activity leads to ectopic lateral localization of the Cdc42 guanine nucleotide exchange factor (GEF) Gef1, but not of the other Cdc42 GEF, Scd1. Consistent with these observations, gef1 deletion suppresses the increased cell diameter phenotype of orb6 mutants. In contrast, the microtubule cytoskeleton and the localization of the microtubule-dependent polarity markers Tea1 and Tea4 are not altered by loss of Orb6 kinase activity. Our findings indicate that the conserved NDR kinase Orb6 regulates cell polarity by spatially restricting the localization and activity of Cdc42 GTPase.","doi":"10.1016/j.cub.2009.06.057","authors":"Das M, Wiley DJ, Chen X, Shah K, Verde F","authors_abbrev":"Das M et al.","pubmed_publication_date":"11 Aug 2009","pubmed_entrez_date":"2009-08-04","publication_year":"2009","canto_session_key":"d9659faec55f853e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 16:35:13","canto_approved_date":"2023-12-27 20:42:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-07 17:13:51","canto_added_date":"2012-02-19 21:32:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":41,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC895.05","SPBC28E12.03","SPBC1706.01","SPAC821.12","SPAC16E8.09","SPAC23C11.11","SPBC1604.14c","SPBC17F3.02","SPAC24H6.09","SPCC1919.10c","SPCC1223.06","SPAC110.03"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2019-01-30"},{"uniquename":"PMID:19776021","title":"Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis.","citation":"J Biol Chem 2009 Dec 18;284(51):35769-80","abstract":"Homocitrate synthase (HCS) catalyzes the first and committed step in lysine biosynthesis in many fungi and certain Archaea and is a potential target for antifungal drugs. Here we report the crystal structure of the HCS apoenzyme from Schizosaccharomyces pombe and two distinct structures of the enzyme in complex with the substrate 2-oxoglutarate (2-OG). The structures reveal that HCS forms an intertwined homodimer stabilized by domain-swapping between the N- and C-terminal domains of each monomer. The N-terminal catalytic domain is composed of a TIM barrel fold in which 2-OG binds via hydrogen bonds and coordination to the active site divalent metal ion, whereas the C-terminal domain is composed of mixed alpha/beta topology. In the structures of the HCS apoenzyme and one of the 2-OG binary complexes, a lid motif from the C-terminal domain occludes the entrance to the active site of the neighboring monomer, whereas in the second 2-OG complex the lid is disordered, suggesting that it regulates substrate access to the active site through its apparent flexibility. Mutations of the active site residues involved in 2-OG binding or implicated in acid-base catalysis impair or abolish activity in vitro and in vivo. Together, these results yield new insights into the structure and catalytic mechanism of HCSs and furnish a platform for developing HCS-selective inhibitors.","doi":"10.1074/jbc.M109.046821","authors":"Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC","authors_abbrev":"Bulfer SL et al.","pubmed_publication_date":"18 Dec 2009","pubmed_entrez_date":"2009-09-25","publication_year":"2009","canto_session_key":"7a4af6960244c85a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-11-07 17:18:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-31 21:49:56","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":20,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-31","pdb_entries":[{"pdb_id":"3ivu","gene_chains":[{"gene_uniquename":"SPBC1105.02c","chain":"A/B","position":"1-418"}],"title":"Homocitrate Synthase Lys4 bound to 2-OG","entry_authors":"Bulfer SL,Scott EM,Couture J-F,Pillus L,Trievel RC","entry_authors_abbrev":"Bulfer SL et al.","reference_uniquename":"PMID:19776021","experimental_method":"X-ray","resolution":"2.72"},{"pdb_id":"3ivs","gene_chains":[{"gene_uniquename":"SPBC1105.02c","chain":"A/B","position":"1-418"}],"title":"Homocitrate Synthase Lys4","entry_authors":"Bulfer SL,Scott EM,Couture J-F,Pillus L,Trievel RC","entry_authors_abbrev":"Bulfer SL et al.","reference_uniquename":"PMID:19776021","experimental_method":"X-ray","resolution":"2.24"},{"pdb_id":"3ivt","gene_chains":[{"gene_uniquename":"SPBC1105.02c","chain":"A/B","position":"1-418"}],"title":"Homocitrate Synthase Lys4 bound to 2-OG","entry_authors":"Bulfer SL,Scott EM,Couture J-F,Pillus L,Trievel RC","entry_authors_abbrev":"Bulfer SL et al.","reference_uniquename":"PMID:19776021","experimental_method":"X-ray","resolution":"2.67"}]},{"uniquename":"PMID:16118428","title":"Intracellular expression of recombinant antibody fluorescent protein fusions for localization of target antigens in Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2006;313:97-105","abstract":"Intracellular localization is important for the characterization of a gene product. Microscopy of fluorescent protein fusions has become the method of choice to define the spatial and temporal behavior of a protein. We show here that recombinant antibody fluorescent protein fusions can be used to monitor the localization of intracellular antigens in fixed or living cells. A most successful application of phage-display technology has been the isolation of recombinant antibodies from large combinatorial repertoires. The most versatile antibody format is the single-chain Fv fragment (scFv) in which a flexible polypeptide linker joins the heavy- and light-chain antibody variable domains. Commercial systems are now available to produce scFv phage-display libraries encoding a large pool of binding specificities from which antibodies can be isolated and used as immunochemical or intracellular reagents. We designed a plasmid for ectopic expression of a recombinant antibody fused to a green fluorescent protein (GFP) under the control of an attenuated nmt1 promoter in Schizosaccharomyces pombe.","authors":"Alting-Mees MA, Risseeuw EP, Liu E, Desautels M, Crosby WA, Hemmingsen SM","authors_abbrev":"Alting-Mees MA et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2005-08-25","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:D31852","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.103"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:28412269","title":"Towards an understanding of the isotype-specific functions of tubulin in neurons: Technical advances in tubulin expression and purification.","citation":"Neurosci Res 2017 Sep;122:1-8","abstract":"Microtubules are cytoskeletal filaments critical for determining the complex morphology of neurons, as well as the basic architecture and organization of mitosis in all eukaryotic cells. Microtubules in humans are composed of 8 α- and 9 β-tubulin isotypes, each of which is encoded by different members of a multi-gene family. The expression pattern of tubulin isotypes, in addition to isotype-specific post-translational modifications, is thought to be critical for the morphogenesis of axons and dendrites. Recent studies revealed that several neurodevelopmental disorders are caused by mutations of specific tubulin isotypes, suggesting that each tubulin isotype has distinct functions. Therefore, in vitro and in vivo functional analyses of tubulin isotypes are important to understand the pathogenesis of developmental disorders. Likewise, analysis of developmental disorders may clarify the function of different tubulin isotypes. In this respect, both the preparation of specific tubulin isotypes and of specific mutant tubulin proteins is critical to understanding the function of tubulin. In the last 20 years, various methods have been developed to study functional differences between tubulin isotypes and the functional defects caused by tubulin mutations. These technical achievements have been discussed in this review. The function of tubulin/microtubules in neuronal morphogenesis as revealed through these techniques has also been described.","doi":"10.1016/j.neures.2017.04.002","authors":"Minoura I","authors_abbrev":"Minoura I","pubmed_publication_date":"Sep 2017","pubmed_entrez_date":"2017-04-17","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-04-18 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12018855","title":"Pap1-mediated regulation of thioredoxin gene from Schizosaccharomyces pombe.","citation":"Mol Cells 2002 Apr 30;13(2):315-21","abstract":"The genomic DNA encoding thioredoxin (TRX) was previously isolated from the fission yeast Schizosaccharomyces pombe. In this investigation, regulation of the S. pombe TRX gene was studied in lacZ translational fusions. The synthesis of beta-galactosidase from the fusion plasmid pYKT24 was significantly enhanced by treatments with cadmium chloride, zinc chloride, and high temperatures. Synthesis of beta-galactosidase from the fusion plasmid was significantly decreased by higher concentrations (5 microM, 10 microM) of mercuric chloride, whereas it was enhanced by its lower concentration (1 microM). Diamide affected the synthesis of beta-galactosidase in the same manner with mercuric chloride. However, high osmolarity had no effect on the beta-galactosidase synthesis from the fusion plasmid pYKT24. Various fusion plasmids were constructed to carry serially deleted upstream regions of the TRX gene. Pap1 mediates the regulation of the S. pombe TRX gene. The upstream region, between 987 and 1,270 bp from the translational initiation point, is responsible for the regulation.","authors":"Cho YW, Kim D, Park EH, Lim CJ","authors_abbrev":"Cho YW et al.","pubmed_publication_date":"30 Apr 2002","pubmed_entrez_date":"2002-05-23","publication_year":"2002","canto_session_key":"ca6a225fe804208f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-19 10:09:18","canto_approved_date":"2023-07-10 16:33:19","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2014-11-06 11:14:06","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPAC7D4.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-19"},{"uniquename":"PMID:6347688","title":"Saccharomyces cerevisiae cdc9, a structural gene for yeast DNA ligase which complements Schizosaccharomyces pombe cdc17.","citation":"Eur J Biochem 1983 Aug 01;134(2):315-9","abstract":"The Saccharomyces cerevisiae cdc9 gene has been cloned in the vector YRp12 by complementation of the temperature-sensitive lesion in vivo. The gene is contained within a 3300-base-pair fragment of DNA, which maps to the chromosomal locus of cdc9 and which is able to complement a DNA-ligase-deficient mutant of the fission yeast Schizosaccharomyces pombe.","authors":"Barker DG, Johnston LH","authors_abbrev":"Barker DG et al.","pubmed_publication_date":"01 Aug 1983","pubmed_entrez_date":"1983-08-01","publication_year":"1983","canto_session_key":"625a46ecb87fa108","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 13:58:13","canto_session_submitted_date":"2012-03-03 13:57:28","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G8.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-03-03"},{"uniquename":"EMBL:AJ544685","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.20"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22790398","title":"Genomics of alternative sulfur utilization in ascomycetous yeasts.","citation":"Microbiology (Reading) 2012 Oct;158(Pt 10):2585-2597","abstract":"Thirteen ascomycetous yeast strains with sequenced genomes were assayed for their ability to grow on chemically defined medium with 16 different sulfur compounds as the only significant source of sulfur. These compounds included sulfoxides, sulfones, sulfonates, sulfamates and sulfate esters. Broad utilization of alternative sulfur sources was observed in Komagataella pastoris (syn. Pichia pastoris), Lodderomyces elongisporus, Millerozyma farinosa (syn. Pichia sorbitophila), Pachysolen tannophilus, Scheffersomyces stipitis (syn. Pichia stipitis), Spathaspora passalidarum, Yamadazyma tenuis (syn. Candida tenuis) and Yarrowia lipolytica. Kluyveromyces lactis, Saccharomyces cerevisiae and Zygosaccharomyces rouxii were mainly able to utilize sulfonates and sulfate esters, while Lachancea thermotolerans and Schizosaccharomyces pombe were limited to aromatic sulfate esters. Genome analysis identified several candidate genes with bacterial homologues that had been previously shown to be involved in the utilization of alternative sulfur sources. Analysis of candidate gene promoter sequences revealed a significant overrepresentation of DNA motifs that have been shown to regulate sulfur metabolism in Sacc. cerevisiae.","doi":"10.1099/mic.0.060285-0","authors":"Linder T","authors_abbrev":"Linder T","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-07-14","publication_year":"2012","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16134115","title":"The cyclophilin repertoire of the fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2005 Sep;22(12):927-45","abstract":"The cyclophilin repertoire of the fission yeast Schizosaccharomyces pombe is comprised of nine members that are distributed over all three of its chromosomes and range from small single-domain to large multi-domain proteins. Each cyclophilin possesses only a single prolyl-isomerase domain, and these vary in their degree of consensus, including at positions that are likely to affect their drug-binding ability and catalytic activity. The additional identified motifs are involved in putative protein or RNA interactions, while a novel domain that is specific to SpCyp7 and its orthologues may have functions that include an interaction with hnRNPs. The Sz. pombe cyclophilins are found throughout the cell but appear to be absent from the mitochondria, which is unique among the characterized eukaryotic repertoires. SpCyp5, SpCyp6 and SpCyp8 have exhibited significant upregulation of their expression during the meiotic cycle and SpCyp5 has exhibited significant upregulation of its expression during heat stress. All nine have identified members in the repertoires of H. sapiens, D. melanogaster and A. thaliana. However, only three identified members in the cyclophilin repertoire of S. cerevisiae with SpCyp7 identifying a fourth protein that is not a member of the recognized repertoire due to its possession of a degenerate prolyl-isomerase domain. The cyclophilin repertoire of Sz. pombe therefore represents a better model group for the study of cyclophilin function in the higher eukaryotes.","authors":"Pemberton TJ, Kay JE","authors_abbrev":"Pemberton TJ et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-09-01","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15665379","title":"The EB1 homolog Mal3 stimulates the ATPase of the kinesin Tea2 by recruiting it to the microtubule.","citation":"J Biol Chem 2005 Apr 01;280(13):12299-304","abstract":"Tea2 is a kinesin family member from Schizosaccharomyces pombe that is targeted to microtubule tips and cell ends in a process that depends on Mal3. Constructs of Tea2 containing the motor domain only or the motor domain plus the N-terminal extension are monomeric, whereas a construct including the first predicted coiled coil region is dimeric. These constructs have a low basal rate of ATP hydrolysis of <0.1 s(-1), but microtubules stimulate the rate of ATP hydrolysis to a maximum of approximately 15 s(-1). Hydrodynamic analysis of Mal3 indicates that it is dimeric. Mal3 is known to associate with Tea2, and analysis with the above Tea2 constructs indicates that the principal site of interaction of Mal3 with Tea2 is the N-terminal extension, although a weaker interaction is also observed with the motor domain alone. In parallel to the binding studies, Mal3 strongly stimulates the ATPase of constructs containing the N-terminal extension by decreasing the K0.5(MT) for stimulation by microtubules but only weakly stimulates motor domains without the N-terminal extension. Mal3 reduces the K0.5(MT) values without affecting the k(cat) value at saturating microtubule level. Binding of Mal3 to microtubules induces an increase in the binding of Tea2 and a reciprocal stimulation of Mal3 binding by Tea2 is also observed. Tea2 is a plus end directed motor that drives sliding of axonemes when adsorbed to a glass surface. The sliding rate is initially unaffected by Mal3, but axonemes stop moving on continued exposure to Mal3.","authors":"Browning H, Hackney DD","authors_abbrev":"Browning H et al.","pubmed_publication_date":"01 Apr 2005","pubmed_entrez_date":"2005-01-25","publication_year":"2005","canto_session_key":"564d70e29944c82f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-09-27 15:41:00","canto_approved_date":"2024-03-28 16:56:18","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-09-27 15:40:53","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPBC1604.20c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-09-27"},{"uniquename":"PMID:10629038","title":"Biochemical and genetic conservation of fission yeast Dsk1 and human SR protein-specific kinase 1.","citation":"Mol Cell Biol 2000 Feb;20(3):816-24","abstract":"Arginine/serine-rich (RS) domain-containing proteins and their phosphorylation by specific protein kinases constitute control circuits to regulate pre-mRNA splicing and coordinate splicing with transcription in mammalian cells. We present here the finding that similar SR networks exist in Schizosaccharomyces pombe. We previously showed that Dsk1 protein, originally described as a mitotic regulator, displays high activity in phosphorylating S. pombe Prp2 protein (spU2AF59), a homologue of human U2AF65. We now demonstrate that Dsk1 also phosphorylates two recently identified fission yeast proteins with RS repeats, Srp1 and Srp2, in vitro. The phosphorylated proteins bear the same phosphoepitope found in mammalian SR proteins. Consistent with its substrate specificity, Dsk1 forms kinase-competent complexes with those proteins. Furthermore, dsk1(+) gene determines the phenotype of prp2(+) overexpression, providing in vivo evidence that Prp2 is a target for Dsk1. The dsk1-null mutant strain became severely sick with the additional deletion of a related kinase gene. Significantly, human SR protein-specific kinase 1 (SRPK1) complements the growth defect of the double-deletion mutant. In conjunction with the resemblance of dsk1(+) and SRPK1 in sequence homology, biochemical properties, and overexpression phenotypes, the complementation result indicates that SRPK1 is a functional homologue of Dsk1. Collectively, our studies illustrate the conserved SR networks in S. pombe consisting of RS domain-containing proteins and SR protein-specific kinases and thus establish the importance of the networks in eucaryotic organisms.","authors":"Tang Z, Kuo T, Shen J, Lin RJ","authors_abbrev":"Tang Z et al.","pubmed_publication_date":"Feb 2000","pubmed_entrez_date":"2000-01-11","publication_year":"2000","canto_session_key":"661d2fef98eb1626","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-07-13 12:01:47","canto_approved_date":"2023-12-24 11:08:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-13 12:01:41","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16.02c","SPBC146.07","SPBC11C11.08","SPAC1D4.11c","SPBC530.14c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-07-13"},{"uniquename":"PMID:4347685","title":"Role of mitochondria in the sex-directed flocculation of a fission yeast.","citation":"Arch Biochem Biophys 1973 Jan;154(1):382-6","abstract":"","authors":"Calleja GB","authors_abbrev":"Calleja GB","pubmed_publication_date":"Jan 1973","pubmed_entrez_date":"1973-01-01","publication_year":"1973","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36169220","title":"Functional integration of a semi-synthetic azido-queuosine derivative into translation and a tRNA modification circuit.","citation":"Nucleic Acids Res 2022 Oct 14;50(18):10785-10800","abstract":"Substitution of the queuine nucleobase precursor preQ1 by an azide-containing derivative (azido-propyl-preQ1) led to incorporation of this clickable chemical entity into tRNA via transglycosylation in vitro as well as in vivo in Escherichia coli, Schizosaccharomyces pombe and human cells. The resulting semi-synthetic RNA modification, here termed Q-L1, was present in tRNAs on actively translating ribosomes, indicating functional integration into aminoacylation and recruitment to the ribosome. The azide moiety of Q-L1 facilitates analytics via click conjugation of a fluorescent dye, or of biotin for affinity purification. Combining the latter with RNAseq showed that TGT maintained its native tRNA substrate specificity in S. pombe cells. The semi-synthetic tRNA modification Q-L1 was also functional in tRNA maturation, in effectively replacing the natural queuosine in its stimulation of further modification of tRNAAsp with 5-methylcytosine at position 38 by the tRNA methyltransferase Dnmt2 in S. pombe. This is the first demonstrated in vivo integration of a synthetic moiety into an RNA modification circuit, where one RNA modification stimulates another. In summary, the scarcity of queuosinylation sites in cellular RNA, makes our synthetic q/Q system a 'minimally invasive' system for placement of a non-natural, clickable nucleobase within the total cellular RNA.","doi":"10.1093/nar/gkac822","authors":"Bessler L, Kaur N, Vogt LM, Flemmich L, Siebenaller C, Winz ML, Tuorto F, Micura R, Ehrenhofer-Murray AE, Helm M","authors_abbrev":"Bessler L et al.","pubmed_publication_date":"14 Oct 2022","pubmed_entrez_date":"2022-09-28","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-09-29 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17151234","title":"Xlf1 is required for DNA repair by nonhomologous end joining in Schizosaccharomyces pombe.","citation":"Genetics 2007 Feb;175(2):963-7","abstract":"The accurate repair of DNA double-strand breaks is essential for cell survival and maintenance of genome integrity. Here we describe xlf1+, a gene in the fission yeast Schizosaccharomyces pombe that is required for repair of double-strand breaks by nonhomologous end joining during G1 phase of the cell cycle. Xlf1 is the ortholog of budding yeast Nej1 and human XLF/Cernunnos proteins.","authors":"Cavero S, Chahwan C, Russell P","authors_abbrev":"Cavero S et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2006-12-08","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.14c","SPBC543.03c"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"PMID:35314193","title":"Fission yeast Duf89 and Duf8901 are cobalt/nickel-dependent phosphatase-pyrophosphatases that act via a covalent aspartyl-phosphate intermediate.","citation":"J Biol Chem 2022 May;298(5):101851","abstract":"Domain of Unknown Function 89 (DUF89) proteins are metal-dependent phosphohydrolases. Exemplary DUF89 enzymes differ in their metal and phosphosubstrate preferences. Here, we interrogated the activities and structures of two DUF89 paralogs from fission yeast-Duf89 and Duf8901. We find that Duf89 and Duf8901 are cobalt/nickel-dependent phosphohydrolases adept at hydrolyzing p-nitrophenylphosphate and PP i . Crystal structures of metal-free Duf89 and Co 2+ -bound Duf8901 disclosed two enzyme conformations that differed with respect to the position of a three-helix module, which is either oriented away from the active site in Duf89 or forms a lid over the active site in Duf8901. Lid closure results in a 16 Å movement of Duf8901 Asp195, vis-à-vis Asp199 in Duf89, that brings Asp195 into contact with an octahedrally coordinated cobalt. Reaction of Duf8901 with BeCl 2  and NaF in the presence of divalent cations Co 2+ , Ni 2+ , or Zn 2+  generated covalent Duf8901-(Asp248)-beryllium trifluoride (BeF 3 )•Co 2+ , Duf8901-(Asp248)-BeF 3 •Ni 2+ , or Duf8901-(Asp248)-BeF 3 •Zn 2+  adducts, the structures of which suggest a two-step catalytic mechanism via formation and hydrolysis of an enzyme-(aspartyl)-phosphate intermediate. Alanine mutations of Duf8901 Asp248, Asn249, Lys401, Asp286, and Asp195 that interact with BeF 3 •Co 2+  squelched p-nitrophenylphosphatase activity. A 1.8 Å structure of a Duf8901-(Asp248)-AlF 4 -OH 2 •Co 2+  transition-state mimetic suggests an associative mechanism in which Asp195 and Asp363 orient and activate the water nucleophile. Whereas deletion of the duf89 gene elicited a phenotype in which expression of phosphate homeostasis gene pho1 was derepressed, deleting duf8901 did not, thereby hinting that the DUF89 paralogs have distinct functional repertoires in vivo.","doi":"10.1016/j.jbc.2022.101851","authors":"Sanchez AM, Jacewicz A, Shuman S","authors_abbrev":"Sanchez AM et al.","pubmed_publication_date":"May 2022","pubmed_entrez_date":"2022-03-22","publication_year":"2022","canto_session_key":"2571bb5c8f7d465c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2022-10-25 21:01:28","canto_approved_date":"2023-12-31 14:07:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-10-21 04:27:30","canto_added_date":"2022-03-24 01:15:06","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":20,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC806.04c","SPBP4G3.02","SPCC1393.13"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2022-10-25","pdb_entries":[{"pdb_id":"7u1v","gene_chains":[{"gene_uniquename":"SPAC806.04c","chain":"A/B","position":"1-438"}],"title":"Structure of SPAC806.04c protein from fission yeast covalently bound to BeF3","entry_authors":"Jacewicz A,Sanchez AM,Shuman S","entry_authors_abbrev":"Jacewicz A et al.","reference_uniquename":"PMID:35314193","experimental_method":"X-ray","resolution":"2.1"},{"pdb_id":"7t7o","gene_chains":[{"gene_uniquename":"SPAC806.04c","chain":"A/B","position":"1-438"}],"title":"Structure of SPAC806.04c protein from fission yeast covalently bound to BeF3","entry_authors":"Jacewicz A,Sanchez AM,Shuman S","entry_authors_abbrev":"Jacewicz A et al.","reference_uniquename":"PMID:35314193","experimental_method":"X-ray","resolution":"2.16"},{"pdb_id":"7t7n","gene_chains":[{"gene_uniquename":"SPCC1393.13","chain":"B","position":"1-442"}],"title":"Structure of SPCC1393.13 protein from fission yeast","entry_authors":"Jacewicz A,Sanchez AM,Shuman S","entry_authors_abbrev":"Jacewicz A et al.","reference_uniquename":"PMID:35314193","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"7t7k","gene_chains":[{"gene_uniquename":"SPAC806.04c","chain":"A/B","position":"1-438"}],"title":"Structure of SPAC806.04c protein from fission yeast bound to Co2+","entry_authors":"Jacewicz A,Sanchez AM,Shuman S","entry_authors_abbrev":"Jacewicz A et al.","reference_uniquename":"PMID:35314193","experimental_method":"X-ray","resolution":"1.9"},{"pdb_id":"7u1x","gene_chains":[{"gene_uniquename":"SPAC806.04c","chain":"A/B","position":"1-438"}],"title":"Structure of SPAC806.04c protein from fission yeast covalently bound to BeF3","entry_authors":"Jacewicz A,Sanchez AM,Shuman S","entry_authors_abbrev":"Jacewicz A et al.","reference_uniquename":"PMID:35314193","experimental_method":"X-ray","resolution":"2.12"},{"pdb_id":"7u1y","gene_chains":[{"gene_uniquename":"SPAC806.04c","chain":"A","position":"1-438"}],"title":"Structure of SPAC806.04c protein from fission yeast bound to AlF4 and Co2+","entry_authors":"Jacewicz A,Sanchez AM,Shuman S","entry_authors_abbrev":"Jacewicz A et al.","reference_uniquename":"PMID:35314193","experimental_method":"X-ray","resolution":"1.81"}]},{"uniquename":"EMBL:AU012784","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6207634","title":"The use of primuline to identify the septum polysaccharide of the fission yeast Schizosaccharomyces pombe.","citation":"Stain Technol 1984 Mar;59(2):79-82","abstract":"Treatment of cells and purified cell walls of the fission yeast Schizosaccharomyces pombe with primuline reveals the septum as a bright fluorescent band. When polysaccharides containing (1----3)-beta-, (1----6)-beta- or (1----3)-alpha-glucosidic linkages are treated with primuline, only those molecules containing chains of (1----3)-beta-glucosyl residues are stained. This implies that (1----3)-beta-glucan is present in the septum of Schiz. pombe as the main constituent.","authors":"Duffus JH, McDowell W, Manners DJ","authors_abbrev":"Duffus JH et al.","pubmed_publication_date":"Mar 1984","pubmed_entrez_date":"1984-03-01","publication_year":"1984","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34153074","title":"The leucine-NH4+ uptake regulator Any1 limits growth as part of a general amino acid control response to loss of La protein by fission yeast.","citation":"PLoS One 2021;16(6):e0253494","abstract":"The sla1+ gene of Schizosachharoymces pombe encodes La protein which promotes proper processing of precursor-tRNAs. Deletion of sla1 (sla1Δ) leads to disrupted tRNA processing and sensitivity to target of rapamycin (TOR) inhibition. Consistent with this, media containing NH4+ inhibits leucine uptake and growth of sla1Δ cells. Here, transcriptome analysis reveals that genes upregulated in sla1Δ cells exhibit highly significant overalp with general amino acid control (GAAC) genes in relevant transcriptomes from other studies. Growth in NH4+ media leads to additional induced genes that are part of a core environmental stress response (CESR). The sla1Δ GAAC response adds to evidence linking tRNA homeostasis and broad signaling in S. pombe. We provide evidence that deletion of the Rrp6 subunit of the nuclear exosome selectively dampens a subset of GAAC genes in sla1Δ cells suggesting that nuclear surveillance-mediated signaling occurs in S. pombe. To study the NH4+-effects, we isolated sla1Δ spontaneous revertants (SSR) of the slow growth phenotype and found that GAAC gene expression and rapamycin hypersensitivity were also reversed. Genome sequencing identified a F32V substitution in Any1, a known negative regulator of NH4+-sensitive leucine uptake linked to TOR. We show that 3H-leucine uptake by SSR-any1-F32V cells in NH4+-media is more robust than by sla1Δ cells. Moreover, F32V may alter any1+ function in sla1Δ vs. sla1+ cells in a distinctive way. Thus deletion of La, a tRNA processing factor leads to a GAAC response involving reprogramming of amino acid metabolism, and isolation of the any1-F32V rescuing mutant provides an additional specific link.","doi":"10.1371/journal.pone.0253494","authors":"Cherkasova V, Iben JR, Pridham KJ, Kessler AC, Maraia RJ","authors_abbrev":"Cherkasova V et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-06-21","publication_year":"2021","canto_session_key":"cc11842daf0c3b3a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-06-23 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14528010","title":"Slx1-Slx4 are subunits of a structure-specific endonuclease that maintains ribosomal DNA in fission yeast.","citation":"Mol Biol Cell 2004 Jan;15(1):71-80","abstract":"In most eukaryotes, genes encoding ribosomal RNAs (rDNA) are clustered in long tandem head-to-tail repeats. Studies of Saccharomyces cerevisiae have indicated that rDNA copy number is maintained through recombination events associated with site-specific blockage of replication forks (RFs). Here, we describe two Schizosaccharomyces pombe proteins, homologs of S. cerevisiae Slx1 and Slx4, as subunits of a novel type of endonuclease that maintains rDNA copy number. The Slx1-Slx4-dependent endonuclease introduces single-strand cuts in duplex DNA on the 3' side of junctions with single-strand DNA. Deletion of Slx1 or Rqh1 RecQ-like DNA helicase provokes rDNA contraction, whereas simultaneous elimination of Slx1-Slx4 endonuclease and Rqh1 is lethal. Slx1 associates with chromatin at two foci characteristic of the two rDNA repeat loci in S. pombe. We propose a model in which the Slx1-Slx4 complex is involved in the control of the expansion and contraction of the rDNA loci by initiating recombination events at stalled RFs.","authors":"Coulon S, Gaillard PHL, Chahwan C, McDonald WH, Yates JR, Russell P","authors_abbrev":"Coulon S et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2003-10-07","publication_year":"2004","canto_session_key":"796a4851ed930759","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-11-12 10:50:08","canto_approved_date":"2025-09-04 11:24:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-12 10:49:59","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.06c","SPAC2G11.12","SPAP27G11.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-11-12"},{"uniquename":"PMID:21593208","title":"CDK promotes interactions of Sld3 and Drc1 with Cut5 for initiation of DNA replication in fission yeast.","citation":"Mol Biol Cell 2011 Jul 15;22(14):2620-33","abstract":"Cyclin-dependent kinase (CDK) plays essential roles in the initiation of DNA replication in eukaryotes. Although interactions of CDK-phosphorylated Sld2/Drc1 and Sld3 with Dpb11 have been shown to be essential in budding yeast, it is not known whether the mechanism is conserved. In this study, we investigated how CDK promotes the assembly of replication proteins onto replication origins in fission yeast. Phosphorylation of Sld3 was found to be dependent on CDK in S phase. Alanine substitutions at CDK sites decreased the interaction with Cut5/Dpb11 at the N-terminal BRCT motifs and decreased the loading of Cut5 onto replication origins. This defect was suppressed by overexpression of drc1(+). Phosphorylation of a conserved CDK site, Thr-111, in Drc1 was critical for interaction with Cut5 at the C-terminal BRCT motifs and was required for loading of Cut5. In a yeast three-hybrid assay, Sld3, Cut5, and Drc1 were found to form a ternary complex dependent on the CDK sites of Sld3 and Drc1, and Drc1-Cut5 binding enhanced the Sld3-Cut5 interaction. These results show that the mechanism of CDK-dependent loading of Cut5 is conserved in fission yeast in a manner similar to that elucidated in budding yeast.","doi":"10.1091/mbc.E10-12-0995","authors":"Fukuura M, Nagao K, Obuse C, Takahashi TS, Nakagawa T, Masukata H","authors_abbrev":"Fukuura M et al.","pubmed_publication_date":"15 Jul 2011","pubmed_entrez_date":"2011-05-20","publication_year":"2011","canto_session_key":"462b1f18876a3bee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-01-15 17:03:07","canto_approved_date":"2022-09-21 15:44:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-01-15 17:02:29","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":87,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4.04c","SPBP4H10.21c","SPBC725.13c","SPCC16A11.17","SPAC6B12.11","SPAC227.16c","SPAC23C4.18c","SPAC24H6.06","SPBC11B10.09","SPBC211.04c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2020-01-15"},{"uniquename":"PMID:16291725","title":"btn1, the Schizosaccharomyces pombe homologue of the human Batten disease gene CLN3, regulates vacuole homeostasis.","citation":"J Cell Sci 2005 Dec 01;118(Pt 23):5525-36","abstract":"We have cloned the Schizosaccharomyces pombe homologue of the human Batten disease gene, CLN3. This gene, btn1, encodes a predicted transmembrane protein that is 30% identical and 48% similar to its human counterpart. Cells deleted for btn1 were viable but had enlarged and more alkaline vacuoles. Conversely overexpression of Btn1p reduced both vacuole diameter and pH. Thus Btn1p regulates vacuole homeostasis. The vacuolar defects of btn1Delta cells were rescued by heterologous expression of CLN3, proving that Btn1p and CLN3 are functional homologues. The disease severity of Batten disease-causing mutations (G187A, E295K and V330F), when expressed in btn1 appeared to correlate with their effect on vacuolar pH, suggesting that elevated lysosomal pH contributes to the disease process. In fission yeast, both Btn1p and CLN3 trafficked to the vacuole membrane via early endocytic and pre-vacuolar compartments, and localisation of Btn1p to the vacuole membrane was dependent on the Ras GTPase Ypt7p. Importantly, vacuoles in cells deleted for both ypt7 and btn1 were larger and more alkaline than those of cells deleted for ypt7 alone, indicating that Btn1p has a functional role prior to reaching the vacuole. Consistently, btn1 and vma1, the gene encoding subunit A of the V1 portion of vATPase, showed conditional synthetic lethality, and in cells deleted for vma1 (a subunit of the vacuolar ATPase) Btn1p was essential for septum deposition during cytokinesis.","authors":"Gachet Y, Codlin S, Hyams JS, Mole SE","authors_abbrev":"Gachet Y et al.","pubmed_publication_date":"01 Dec 2005","pubmed_entrez_date":"2005-11-18","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2C4.13","SPAPB2B4.05","SPAC343.05","SPAC607.09c","SPBC405.04c"],"gene_count":5,"ltp_gene_count":3},{"uniquename":"PMID:35676478","title":"Core control principles of the eukaryotic cell cycle.","citation":"Nature 2022 Jul;607(7918):381-386","abstract":"Cyclin-dependent kinases (CDKs) lie at the heart of eukaryotic cell cycle control, with different cyclin-CDK complexes initiating DNA replication (S-CDKs) and mitosis (M-CDKs) 1,2 . However, the principles on which cyclin-CDK complexes organize the temporal order of cell cycle events are contentious 3 . One model proposes that S-CDKs and M-CDKs are functionally specialized, with substantially different substrate specificities to execute different cell cycle events 4-6 . A second model proposes that S-CDKs and M-CDKs are redundant with each other, with both acting as sources of overall CDK activity 7,8 . In this model, increasing CDK activity, rather than CDK substrate specificity, orders cell cycle events 9,10 . Here we reconcile these two views of core cell cycle control. Using phosphoproteomic assays of in vivo CDK activity in fission yeast, we find that S-CDK and M-CDK substrate specificities are remarkably similar, showing that S-CDKs and M-CDKs are not completely specialized for S phase and mitosis alone. Normally, S-CDK cannot drive mitosis but can do so when protein phosphatase 1 is removed from the centrosome. Thus, increasing S-CDK activity in vivo is sufficient to overcome substrate specificity differences between S-CDK and M-CDK, and allows S-CDK to carry out M-CDK function. Therefore, we unite the two opposing views of cell cycle control, showing that the core cell cycle engine is largely based on a quantitative increase in CDK activity through the cell cycle, combined with minor and surmountable qualitative differences in catalytic specialization of S-CDKs and M-CDKs.","doi":"10.1038/s41586-022-04798-8","authors":"Basu S, Greenwood J, Jones AW, Nurse P","authors_abbrev":"Basu S et al.","pubmed_publication_date":"Jul 2022","pubmed_entrez_date":"2022-06-08","publication_year":"2022","canto_session_key":"277396acb0ad5aef","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-06-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7575489","title":"G1 regulation and checkpoints operating around START in fission yeast.","citation":"Bioessays 1995 Jun;17(6):481-90","abstract":"Three major aspects of G1 regulation acting at START in fission yeast are discussed in this review. Firstly, progression towards S phase in the mitotic cycle. This is controlled by the activation of transcription complexes at START which cause cell cycle-dependent activation of genes required for DNA synthesis. The second aspect is the regulation of developmental fate occurring during G1. Passage through START appears to inhibit sexual differentiation because the meiotic and mitotic pathways are mutually exclusive. This is brought about because the meiotic pathway is inhibited by the same gene functions that are required for S phase onset. Thirdly, distinct checkpoint, or dependency, controls operate both pre- and post-START in the mitotic cycle to inhibit mitosis in the absence of replicated DNA, and also to limit rounds of DNA replication to one per cell cycle.","authors":"Woollard A, Nurse P","authors_abbrev":"Woollard A et al.","pubmed_publication_date":"Jun 1995","pubmed_entrez_date":"1995-06-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23028742","title":"The natural anticancer agent plumbagin induces potent cytotoxicity in MCF-7 human breast cancer cells by inhibiting a PI-5 kinase for ROS generation.","citation":"PLoS One 2012;7(9):e45023","abstract":"Drug-induced haploinsufficiency (DIH) in yeast has been considered a valuable tool for drug target identification. A plant metabolite, plumbagin, has potent anticancer activity via reactive oxygen species (ROS) generation. However, the detailed molecular targets of plumbagin for ROS generation are not understood. Here, using DIH and heterozygous deletion mutants of the fission yeast Schizosaccharomyces pombe, we identified 1, 4-phopshatidylinositol 5-kinase (PI5K) its3 as a new molecular target of plumbagin for ROS generation. Plumbagin showed potent anti-proliferative activity (GI(50); 10 µM) and induced cell elongation and septum formation in wild-type S. pombe. Furthermore, plumbagin dramatically increased the intracellular ROS level, and pretreatment with the ROS scavenger, N-acetyl cysteine (NAC), protected against growth inhibition by plumbagin, suggesting that ROS play a crucial role in the anti-proliferative activity in S. pombe. Interestingly, significant DIH was observed in an its3-deleted heterozygous mutant, in which ROS generation by plumbagin was higher than that in wild-type cells, implying that its3 contributes to ROS generation by plumbagin in this yeast. In MCF7 human breast cancer cells, plumbagin significantly decreased the level of a human ortholog, 1, 4-phopshatidylinositol 5-kinase (PI5K)-1B, of yeast its3, and knockdown of PI5K-1B using siPI5K-1B increased the ROS level and decreased cell viability. Taken together, these results clearly show that PI5K-1B plays a crucial role in ROS generation as a new molecular target of plumbagin. Moreover, drug target screening using DIH in S. pombe deletion mutants is a valuable tool for identifying molecular targets of anticancer agents.","doi":"10.1371/journal.pone.0045023","authors":"Lee JH, Yeon JH, Kim H, Roh W, Chae J, Park HO, Kim DM","authors_abbrev":"Lee JH et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-10-03","publication_year":"2012","canto_session_key":"ed12ab2f3f0456f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-02-20 10:52:59","canto_approved_date":"2024-07-22 11:31:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-20 10:52:52","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.14","SPBC32H8.12c","SPBC18H10.03","SPAC4D7.05","SPBC216.07c","SPBC649.05","SPAC458.05","SPAC16E8.15","SPBC1734.14c","SPBC9B6.04c","SPBC11B10.09"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2014-02-20"},{"uniquename":"EMBL:AU012339","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41797432","title":"The Hemoprotein Hhy1 Promotes Heme-Dependent Catalase Activity of Ctt1.","citation":"Mol Microbiol 2026 Mar 08;","abstract":"In this study, we generated a Schizosaccharomyces pombe strain deficient in heme and siderophore biosynthesis, as well as in reductive iron uptake. Using this hem1Δ sib1Δ sib2Δ fio1Δ fip1Δ mutant strain, we identified Hhy1, a novel protein required for optimal growth when cells rely on exogenous hemin as their sole source of heme. The expression of Hhy1 is upregulated under low-iron conditions and downregulated when iron levels increase. Fluorescence microscopy analysis shows that the Hhy1-GFP fluorescent signal mirrors hhy1 +  mRNA expression, being primarily detected in the cytoplasm of iron-starved hem1Δ sib1Δ sib2Δ fio1Δ fip1Δ cells. Further monitoring of intracellular heme or its analog zinc mesoporphyrin IX revealed that hem1Δ sib1Δ sib2Δ fio1Δ fip1Δ cells lacking Hhy1 accumulate these molecules more persistently than cells expressing Hhy1. Consistent with a role for Hhy1 in heme homeostasis, hhy1Δ cells exhibit reduced heme-dependent activity of the catalase Ctt1. Coimmunoprecipitation and bimolecular fluorescence complementation experiments show that Hhy1 interacts with Ctt1. Absorbance spectroscopy and hemin-agarose pull-down assays demonstrate that Hhy1 binds hemin, with an equilibrium dissociation constant of 1.09 μM. Taken together, these findings indicate that the iron-regulated cytoplasmic hemoprotein Hhy1 interacts with Ctt1, promoting its full activation against oxidative stress under hemin-dependent growth conditions.","doi":"10.1111/mmi.70062","authors":"Vahsen T, Plante S, Mbuya B, Labbé S","authors_abbrev":"Vahsen T et al.","pubmed_publication_date":"08 Mar 2026","pubmed_entrez_date":"2026-03-09","publication_year":"2026","canto_session_key":"aacaf845a4f9aa96","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-03-10 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11195093","title":"The use of morphomutants to investigate septum formation and cell separation in Schizosaccharomyces pombe.","citation":"Arch Microbiol 2000 Dec;174(6):386-92","abstract":"Cytokinesis in the fission yeast Schizosaccharomyces begins by formation of a medially placed actomyosin ring, continues by progressive development of a septum, and is completed by cleavage of the mature septum to bring about cell separation. The cytological analysis of the Schizosaccharomyces pombe morphomutants sph2-3 and sep1-1 presented here demonstrates that the medial actomyosin ring colocalizes to the leading edge of the centripetally growing septum, and cleavage of the septum is triggered by rupture of the mother cell wall at the septal basis.","authors":"Sipiczki M, Bozsik A","authors_abbrev":"Sipiczki M et al.","pubmed_publication_date":"Dec 2000","pubmed_entrez_date":"2001-02-24","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3347503","title":"Strain-dependent variation of intron-exon pairings in a group II intron of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1988 Feb 25;16(4):1629","abstract":"","authors":"Welser F, Wolf K","authors_abbrev":"Welser F et al.","pubmed_publication_date":"25 Feb 1988","pubmed_entrez_date":"1988-02-25","publication_year":"1988","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8515818","title":"Nim1 kinase promotes mitosis by inactivating Wee1 tyrosine kinase.","citation":"Nature 1993 Jun 24;363(6431):738-41","abstract":"In most species, including the fission yeast Schizosaccharomyces pombe, the Cdc2/cyclin B mitosis-inducing kinase is maintained in an inhibited state during interphase as a result of phosphorylation of a tyrosine residue in the ATP-binding region of Cdc2 (refs 1-3). This site is phosphorylated by Wee1 kinase and dephosphorylated by Cdc25 phosphatase. In fission yeast an additional element of the G2/M control Nim1/Cdr1 kinase, has been identified which functions as a potent mitotic inducer. These studies suggested that Nim1 acts by inhibiting Wee1, perhaps by direct phosphorylation. Consistent with this model, we report here that Wee1 is hyperphosphorylated in cells that overproduce Nim1. Likewise, Wee1 phosphorylation is reduced in nim1- cells. Highly purified Nim1 kinase phosphorylates Wee1 in vitro, resulting in strong inhibition of Wee1 kinase. These observations show that Nim1 promotes the onset of mitosis by inhibiting Wee1.","authors":"Wu L, Russell P","authors_abbrev":"Wu L et al.","pubmed_publication_date":"24 Jun 1993","pubmed_entrez_date":"1993-06-24","publication_year":"1993","canto_session_key":"041a348f5a9e0ac6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-02-24 14:28:41","canto_approved_date":"2025-07-02 05:46:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-17 10:08:36","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":22,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC24H6.05","SPAC644.06c","SPCC18B5.03","SPBC660.14"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2021-02-24"},{"uniquename":"PMID:32085395","title":"Maintenance of Yeast Genome Integrity by RecQ Family DNA Helicases.","citation":"Genes (Basel) 2020 Feb 18;11(2)","abstract":"With roles in DNA repair, recombination, replication and transcription, members of the RecQ DNA helicase family maintain genome integrity from bacteria to mammals. Mutations in human RecQ helicases BLM, WRN and RecQL4 cause incurable disorders characterized by genome instability, increased cancer predisposition and premature adult-onset aging. Yeast cells lacking the RecQ helicase Sgs1 share many of the cellular defects of human cells lacking BLM, including hypersensitivity to DNA damaging agents and replication stress, shortened lifespan, genome instability and mitotic hyper-recombination, making them invaluable model systems for elucidating eukaryotic RecQ helicase function. Yeast and human RecQ helicases have common DNA substrates and domain structures and share similar physical interaction partners. Here, we review the major cellular functions of the yeast RecQ helicases Sgs1 of  Saccharomyces cerevisiae  and Rqh1 of  Schizosaccharomyces pombe  and provide an outlook on some of the outstanding questions in the field.","doi":"10.3390/genes11020205","authors":"Gupta SV, Schmidt KH","authors_abbrev":"Gupta SV et al.","pubmed_publication_date":"18 Feb 2020","pubmed_entrez_date":"2020-02-23","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-02-24 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:93456","title":"Reconstitution by lipids of the activity of a plasma membrane ATPase purified from the yeast Schizosaccharomyces pombe [proceedings].","citation":"Arch Int Physiol Biochim 1979 Aug;87(3):622-3","abstract":"","authors":"Dufour JP, Goffeau A","authors_abbrev":"Dufour JP et al.","pubmed_publication_date":"Aug 1979","pubmed_entrez_date":"1979-08-01","publication_year":"1979","canto_session_key":"adfe74518f7b3d79","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-23 17:59:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-23 17:59:41","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-23"},{"uniquename":"PMID:39527212","title":"An \"In Schizo\" Evaluation System to Screen for Human Kinesin-5 Inhibitors.","citation":"Methods Mol Biol 2025;2862:333-351","abstract":"Kinesin-5 motor proteins are essential for mitotic spindle formation and maintenance, ensuring accurate chromosome segregation. Human kinesin-5 is highly expressed in various cancer cells but not in nonproliferative tissues; therefore, it is expected to be an attractive target for cancer chemotherapy, with fewer adverse side effects. Many inhibitors have been developed and subjected to clinical trials; however, they have not yet been commercially distributed because of their poor efficacy and frequent drug resistance. Establishing in vivo assay systems to easily monitor inhibitory activity is necessary and valuable to develop more effective inhibitors. Here, we report a procedure to evaluate the inhibitory activity against human kinesin-5 using a fission yeast-based system called \"in schizo\". Our approach could further be used to screen for inhibitors against kinesin-5 and other human cancer-related targets.","doi":"10.1007/978-1-0716-4168-2_24","authors":"Afdilla FD, Hwang W, Yukawa M","authors_abbrev":"Afdilla FD et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9721610","title":"K(+)-fluxes through plasma membrane of Schizosaccharomyces pombe as measured by whole-cell patch clamp.","citation":"Folia Microbiol (Praha) 1998;43(2):195-7","abstract":"","authors":"Höfer M, Lenz J, Heyer M, Vacata V, Lichtenberg-Fraté H","authors_abbrev":"Höfer M et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-08-29","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8559063","title":"An intron-containing meiosis-induced recombination gene, rec15, of Schizosaccharomyces pombe.","citation":"Mol Microbiol 1995 Aug;17(3):439-48","abstract":"Mutations in the rec15 gene of Schizosaccharomyces pombe reduce meiotic recombinant frequencies, in the three intervals tested, as much as 1000-fold but have no detectable mitotic phenotype. The rec15 gene was mapped to within 1 cM of mat1. The gene was cloned by genetic complementation and its nucleotide sequence determined. Deletion analysis and gene replacement confirmed that the clones contained the rec15 gene on DNA fragments as short as 1.3 kb. The nucleotide sequence of the 1.3 kb fragment predicted that rec15 had a 49 bp intron separating two exons encoding a 180-amino-acid polypeptide product. This predicted intron was confirmed by reverse transcriptase-polymerase chain reaction (RT-PCR) analysis. During thermally induced meiosis in a pat1-114 (Ts) mutant, the rec15 transcripts were induced to maximal levels at 2-3h but were present at much lower levels before and after this time. The transient induction of the transcripts and the phenotype of a rec15 null (deletion) mutation suggest that the rec15 gene product is required during the early stages of meiosis for meiotic recombination.","authors":"Lin Y, Smith GR","authors_abbrev":"Lin Y et al.","pubmed_publication_date":"Aug 1995","pubmed_entrez_date":"1995-08-01","publication_year":"1995","canto_session_key":"98701a51b49ebbb5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-09-25 08:23:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-09-24 16:18:31","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1711.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-09-24"},{"uniquename":"PMID:19052544","title":"Spliceosomal cleavage generates the 3' end of telomerase RNA.","citation":"Nature 2008 Dec 18;456(7224):910-4","abstract":"Telomeres cap the ends of chromosomes and provide a means to complete replication. The DNA portion of telomeres is synthesized by the enzyme telomerase using part of an RNA subunit as a template for reverse transcription. How the mature 3' end of telomerase RNA is generated has so far remained elusive. Here we show that in Schizosaccharomyces pombe telomerase RNA transcripts must be processed to generate functional telomerase. Characterization of the maturation pathway uncovered an unexpected role for the spliceosome, which normally catalyses splicing of pre-messenger RNA. The first spliceosomal cleavage reaction generates the mature 3' end of telomerase RNA (TER1, the functional RNA encoded by the ter1(+) gene), releasing the active form of the RNA without exon ligation. Blocking the first step or permitting completion of splicing generates inactive forms of TER1 and causes progressive telomere shortening. We establish that 3' end processing of TER1 is critical for telomerase function and describe a previously unknown mechanism for RNA maturation that uses the ability of the spliceosome to mediate site-specific cleavage.","doi":"10.1038/nature07584","authors":"Box JA, Bunch JT, Tang W, Baumann P","authors_abbrev":"Box JA et al.","pubmed_publication_date":"18 Dec 2008","pubmed_entrez_date":"2008-12-05","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.214"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:18789404","title":"Repair of deaminated base damage by Schizosaccharomyces pombe thymine DNA glycosylase.","citation":"DNA Repair (Amst) 2008 Dec 01;7(12):1962-72","abstract":"Thymine DNA glycosylases (TDG) in eukaryotic organisms are known for their double-stranded glycosylase activity on guanine/uracil (G/U) base pairs. Schizosaccharomyces pombe (Spo) TDG is a member of the MUG/TDG family that belongs to a uracil DNA glycosylase superfamily. This work investigates the DNA repair activity of Spo TDG on all four deaminated bases: xanthine (X) and oxanine (O) from guanine, hypoxanthine (I) from adenine, and uracil from cytosine. Unexpectedly, Spo TDG exhibits glycosylase activity on all deaminated bases in both double-stranded and single-stranded DNA in the descending order of X>I>U>>O. In comparison, human TDG only excises deaminated bases from G/U and, to a much lower extent, A/U and G/I base pairs. Amino acid substitutions in motifs 1 and 2 of Spo TDG show a significant impact on deaminated base repair activity. The overall mutational effects are characterized by a loss of glycosylase activity on oxanine in all five mutants. L157I in motif 1 and G288M in motif 2 retain xanthine DNA glycosylase (XDG) activity but reduce excision of hypoxanthine and uracil, in particular in C/I, single-stranded hypoxanthine (ss-I), A/U, and single-stranded uracil (ss-U). A proline substitution at I289 in motif 2 causes a significant reduction in XDG activity and a loss of activity on C/I, ss-I, A/U, C/U, G/U, and ss-U. S291G only retains reduced activity on T/I and G/I base pairs. S163A can still excise hypoxanthine and uracil in mismatched base pairs but loses XDG activity, making it the closest mutant, functionally, to human TDG. The relationship among amino acid substitutions, binding affinity and base recognition is discussed.","doi":"10.1016/j.dnarep.2008.08.006","authors":"Dong L, Mi R, Glass RA, Barry JN, Cao W","authors_abbrev":"Dong L et al.","pubmed_publication_date":"01 Dec 2008","pubmed_entrez_date":"2008-09-16","publication_year":"2008","canto_session_key":"1d6c5bf0855bd48b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-01-30 16:05:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-30 16:05:42","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC965.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-30"},{"uniquename":"PMID:27664222","title":"A Pap1-Oxs1 signaling pathway for disulfide stress in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2017 Jan 09;45(1):106-114","abstract":"We describe a Pap1-Oxs1 pathway for diamide-induced disulfide stress in Schizosaccharomyces pombe, where the nucleocytoplasmic HMG protein Oxs1 acts cooperatively with Pap1 to regulate transcription. Oxs1 and Pap1 form a complex when cells are exposed to diamide or Cd that causes disulfide stress. When examined for promoters up-regulated by diamide, effective Pap1 binding to these targets requires Oxs1, and vice versa. With some genes, each protein alone enhances transcription, but the presence of both exerts an additive positive effect. In other genes, although transcription is induced by diamide, Oxs1 or Pap1 plays a negative role with full de-repression requiring loss of both proteins. In a third class of genes, Oxs1 positively regulates expression, but in its absence, Pap1 plays a negative role. The Oxs1-Pap1 regulatory interaction appears evolutionarily conserved, as heterologous (human, mouse and Arabidopsis) Oxs1 and Pap1-homologues can bind interchangeably with each other in vitro, and at least in the fission yeast, heterologous Oxs1 and Pap1-homologues can substitute for S. pombe Oxs1 and Pap1 to enhance stress tolerance.","doi":"10.1093/nar/gkw818","authors":"He Y, Chen Y, Song W, Zhu L, Dong Z, Ow DW","authors_abbrev":"He Y et al.","pubmed_publication_date":"09 Jan 2017","pubmed_entrez_date":"2016-09-25","publication_year":"2017","canto_session_key":"d00aadd46396cb11","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-29 16:31:43","canto_approved_date":"2025-12-23 19:24:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-29 16:31:35","canto_added_date":"2016-09-26 00:15:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.06c","SPBC36.02c","SPAC1B3.03c","SPBC29A10.12","SPBC1347.14c","SPBC29B5.01","SPCC1739.13","SPAC926.04c","SPAC1783.07c","SPAC21E11.03c","SPAC23D3.12","SPBC1347.11"],"gene_count":12,"ltp_gene_count":5,"approved_date":"2018-01-29"},{"uniquename":"PMID:23874188","title":"Dynamics of SIN asymmetry establishment.","citation":"PLoS Comput Biol 2013;9(7):e1003147","abstract":"Timing of cell division is coordinated by the Septation Initiation Network (SIN) in fission yeast. SIN activation is initiated at the two spindle pole bodies (SPB) of the cell in metaphase, but only one of these SPBs contains an active SIN in anaphase, while SIN is inactivated in the other by the Cdc16-Byr4 GAP complex. Most of the factors that are needed for such asymmetry establishment have been already characterized, but we lack the molecular details that drive such quick asymmetric distribution of molecules at the two SPBs. Here we investigate the problem by computational modeling and, after establishing a minimal system with two antagonists that can drive reliable asymmetry establishment, we incorporate the current knowledge on the basic SIN regulators into an extended model with molecular details of the key regulators. The model can capture several peculiar earlier experimental findings and also predicts the behavior of double and triple SIN mutants. We experimentally tested one prediction, that phosphorylation of the scaffold protein Cdc11 by a SIN kinase and the core cell cycle regulatory Cyclin dependent kinase (Cdk) can compensate for mutations in the SIN inhibitor Cdc16 with different efficiencies. One aspect of the prediction failed, highlighting a potential hole in our current knowledge. Further experimental tests revealed that SIN induced Cdc11 phosphorylation might have two separate effects. We conclude that SIN asymmetry is established by the antagonistic interactions between SIN and its inhibitor Cdc16-Byr4, partially through the regulation of Cdc11 phosphorylation states.","doi":"10.1371/journal.pcbi.1003147","authors":"Bajpai A, Feoktistova A, Chen JS, McCollum D, Sato M, Carazo-Salas RE, Gould KL, Csikász-Nagy A","authors_abbrev":"Bajpai A et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-23","publication_year":"2013","canto_session_key":"addd2b43e02fbb5c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jun-Song Chen","canto_first_approved_date":"2015-08-25 14:06:44","canto_approved_date":"2023-08-10 08:34:56","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2015-08-25 14:02:34","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[{"name":"Jun-Song Chen","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.11c","SPAC6F6.08c","SPBC3H7.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-08-25"},{"uniquename":"PMID:1464317","title":"A new cdc gene required for S phase entry of Schizosaccharomyces pombe encodes a protein similar to the cdc 10+ and SWI4 gene products.","citation":"EMBO J 1992 Dec;11(13):4923-32","abstract":"We have isolated a new cell division cycle gene (res1+) required for entry into S phase, as a multicopy dual suppressor of the pat1 and cdc10 mutants of the fission yeast Schizosaccharomyces pombe. The res1+ gene specifies a 72 kDa protein with two copies of the cdc10/SWI6 motif. A disruptant of res1+ grows poorly at 30 degrees C with severe heat- and cold-sensitivities, and completely arrests in G1 at 36 degrees C and 23 degrees C. The arrested disruptant retains a full conjugation ability. In addition to the cdc10/SWI6 motif, Res1 and SWI4 proteins share a remarkable homology in their amino-terminal region, whereas Cdc10 and SWI6 do so in their carboxy-terminal region. Moreover, the amino-terminal region is essential for the function of Res1 as it is for the function of SWI4. Furthermore, analogous to the relationship of SWI4 to SWI6, the res1+ gene effectively rescues cdc10 mutants, but the cdc10+ gene cannot rescue the res1- phenotype. Thus, striking similarities exist in both structural and functional relationships between Res1 and SWI4, and between Cdc10 and SWI6. In view of the fact that SWI4 and SWI6 form a transcription factor complex and activate promoters containing the SWI4/SWI6 dependent cell-cycle box, Res1 might be a putative association partner of Cdc10 which appears to be involved at least in the activation of promoters containing a MluI cell-cycle box.","authors":"Tanaka K, Okazaki K, Okazaki N, Ueda T, Sugiyama A, Nojima H, Okayama H","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"2177442f77f4a649","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-04-21 11:41:07","canto_approved_date":"2023-09-11 10:23:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-20 16:04:29","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPBC725.16","SPAC31G5.11","SPBC336.12c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-04-21"},{"uniquename":"PMID:18212052","title":"Chp1-Tas3 interaction is required to recruit RITS to fission yeast centromeres and for maintenance of centromeric heterochromatin.","citation":"Mol Cell Biol 2008 Apr;28(7):2154-66","abstract":"The maintenance of centromeric heterochromatin in fission yeast relies on the RNA interference-dependent complexes RITS (RNA-induced transcriptional silencing complex) and RDRC (RNA-directed RNA polymerase complex), which cooperate in a positive feedback loop to recruit high levels of histone H3 K9 methyltransferase activity to centromeres and to promote the assembly and maintenance of centromeric heterochromatin. However, it is unclear how these complexes are targeted to chromatin. RITS comprises Chp1, which binds K9-methylated histone H3; Ago1, which binds short interfering (siRNAs); the adaptor protein Tas3, which links Ago1 to Chp1; and centromeric siRNAs. We have generated mutants in RITS to determine the contribution of the two potential chromatin-targeting proteins Chp1 and Ago1 to the centromeric recruitment of RITS. Mutations in Tas3 that disrupt Ago1 binding are permissive for RITS recruitment and maintain centromeric heterochromatin, but the role of Tas3's interaction with Chp1 is unknown. Here, we define the Chp1 interaction domain of Tas3. A strain expressing a tas3 mutant that cannot bind Chp1 (Tas3(Delta)(10-24)) failed to maintain centromeric heterochromatin, with a loss of centromeric siRNAs, a failure to recruit RITS and RDRC to centromeres, and high levels of chromosome loss. These findings suggest a pivotal role for Chp1 and its association with Tas3 for the recruitment of RITS, RDRC, and histone H3 K9 methyltransferase activity to centromeres.","doi":"10.1128/MCB.01637-07","authors":"Debeauchamp JL, Moses A, Noffsinger VJ, Ulrich DL, Job G, Kosinski AM, Partridge JF","authors_abbrev":"Debeauchamp JL et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-01-24","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21620704","title":"Characterization of dip1p reveals a switch in Arp2/3-dependent actin assembly for fission yeast endocytosis.","citation":"Curr Biol 2011 Jun 07;21(11):905-16","abstract":"During endocytosis in yeast, a choreographed series of discrete local events at the plasma membrane lead to a rapid burst of actin polymerization and the subsequent internalization of an endocytic vesicle. What initiates Arp2/3-dependent actin polymerization in this process is not well understood.\nThe Schizosaccharomyces pombe WISH/DIP/SPIN90 ortholog dip1p is an actin-patch protein that regulates the temporal sequence of endocytic events. dip1Δ mutants exhibit a novel phenotype in which early events such as WASp localization occur normally but arrival of Arp2/3, actin polymerization, and subsequent steps are delayed and occur with apparently random timing. In studying this mutant, we demonstrate that positive feedback loops of WASp, rapid actin assembly, and Arp2/3 contribute to switch-like behavior that initiates actin polymerization. In the absence of dip1p, a subset of patches is activated concurrently with the \"touch\" of a neighboring endocytic vesicle.\nThese studies reveal a switch-like mechanism responsible for the initiation of actin assembly during endocytosis. This switch may be activated in at least two ways, through a dip1p-dependent mechanism and through contact with another endocytic vesicle.","doi":"10.1016/j.cub.2011.04.047","authors":"Basu R, Chang F","authors_abbrev":"Basu R et al.","pubmed_publication_date":"07 Jun 2011","pubmed_entrez_date":"2011-05-31","publication_year":"2011","canto_session_key":"d9c2950e923ec818","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-12-24 17:20:17","canto_approved_date":"2025-12-11 12:41:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-12-23 19:55:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":18,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C4.02","SPBC146.13c","SPAC16E8.01","SPAC17G8.04c","SPBC24C6.10c","SPAC4F10.15c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2016-12-24"},{"uniquename":"PMID:24173337","title":"The mitochondrial genome of the fission yeast schizosaccharomyces pombe : I. isolation and physical mapping of mitochondrial DNA.","citation":"Curr Genet 1983 Jul;7(4):273-84","abstract":"1) We have identified by electron microscopy and isolated a circular DNA species of approximately 6 µm contour length from DNase treated mitochondrial fractions of the petite negative yeast Schizosaccharomyces pombe (S. pombe). 2) Another molecular species of about 3 µm length is also present in mitochondrial fractions. These molecules, however, disappear after DNase treatment or extensive washing, indicating their extramitochondrial location. There is evidence (Fournier et al. 1981) that these molecules represent a multicopy plasmid coding for the genes of cytoplasmic ribosomal RNAs. 3) A restriction enzyme cleavage map of the 6 µm species was constructed using twelve enzymes. Physical mapping revealed a genome length of approximately 18.9 kilobase pairs, thus confirming the electron microscopic data. 4) Northern hybridization of mitochondrial RNA with restriction fragments of mitochondrial DNA revealed two major signals which are attributed to the small and large ribosomal RNA. Apparently both rRNA genes map close together. 5) Spontaneous mit(-) deletion mutants were characterized phenotypically and the location of their deletions was determined. 6) In strains carrying a cytoplasmic mutator (Seitz-Mayr and Wolf 1982) or derived from mutator strains four restriction sites have been mapped, which are not present in the mitochondrial DNA of the parental strain. These extra sites are very likely consequences of the action of the mutator. 7) In conclusion we have presented evidence that the 6 µm circular DNA species is the mitochondrial genome of fission yeast. Special features of this genome are discussed in comparison with other mitochondrial genomes.","doi":"10.1007/BF00376072","authors":"Anziano PQ, Perlman PS, Lang BF, Wolf K","authors_abbrev":"Anziano PQ et al.","pubmed_publication_date":"Jul 1983","pubmed_entrez_date":"2013-11-01","publication_year":"1983","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11385632","title":"How do meiotic chromosomes meet their homologous partners?: lessons from fission yeast.","citation":"Bioessays 2001 Jun;23(6):526-33","abstract":"Homologous chromosome pairing is required for proper chromosome segregation and recombination during meiosis. The mechanism by which a pair of homologous chromosomes contact each other to establish pairing is not fully understood. When pairing occurs during meiotic prophase in the fission yeast, Schizosaccharomyces pombe, the nucleus oscillates between the cell poles and telomeres remain clustered at the leading edge of the moving nucleus. These meiosis-specific activities produce movements of telomere-bundled chromosomes. Several lines of evidence suggest that these movements facilitate homologous chromosome pairing by aligning homologous chromosomes and promoting contact between homologous regions. Since telomere clustering and nuclear or chromosome movements in meiotic prophase have been observed in a wide range of eukaryotic organisms, it is suggested that telomere-mediated chromosome movements are general activities that facilitate homologous chromosome pairing.","authors":"Yamamoto A, Hiraoka Y","authors_abbrev":"Yamamoto A et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-06-01","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10801440","title":"Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis.","citation":"Curr Biol 2000 May 04;10(9):517-25","abstract":"Proteins such as HP1, found in fruit flies and mammals, and Swi6, its fission yeast homologue, carry a chromodomain (CD) and a chromo shadow domain (CSD). These proteins are required to form functional transcriptionally silent centromeric chromatin, and their mutation leads to chromosome segregation defects. CSDs have only been found in tandem in proteins containing the related CD. Most HP1-interacting proteins have been found to associate through the CSD and many of these ligands contain a conserved pentapeptide motif.\nThe 1.9 A crystal structure of the Swi6 CSD is presented here. This reveals a novel dimeric structure that is distinct from the previously reported monomeric nuclear magnetic resonance (NMR) structure of the CD from the mouse modifier 1 protein (MoMOD1, also known as HP1beta or M31). A prominent pit with a non-polar base is generated at the dimer interface, and is commensurate with binding an extended pentapeptide motif. Sequence alignments based on this structure highlight differences between CDs and CSDs that are superimposed on a common structural core. The analyses also revealed a previously unrecognised circumferential hydrophobic sash around the surface of the CD structure.\nDimerisation through the CSD of HP1-like proteins results in the simultaneous formation of a putative protein-protein interaction pit, providing a potential means of targeting CSD-containing proteins to particular chromatin sites.","authors":"Cowieson NP, Partridge JF, Allshire RC, McLaughlin PJ","authors_abbrev":"Cowieson NP et al.","pubmed_publication_date":"04 May 2000","pubmed_entrez_date":"2000-05-10","publication_year":"2000","canto_session_key":"223577fe64743894","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-17 16:14:01","canto_approved_date":"2023-02-17 16:14:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 16:13:54","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-17","pdb_entries":[{"pdb_id":"1e0b","gene_chains":[{"gene_uniquename":"SPAC664.01c","chain":"A/B","position":"261-328"}],"title":"Chromo shadow domain from fission yeast swi6 protein.","entry_authors":"Cowieson NP,Partridge JF,Allshire RC,Mclaughlin PJ","entry_authors_abbrev":"Cowieson NP et al.","reference_uniquename":"PMID:10801440","experimental_method":"X-ray","resolution":"1.9"}]},{"uniquename":"PMID:6948995","title":"Induction of trehalase activity on a nitrogen-free medium: a sporulation-specific event in the fission yeast, Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1981;183(1):32-6","abstract":"Kinetic experiments with synchronously sporulating cultures of a homothallic h90 strain of Schizosaccharomyces pombe showed that trehalase activity abruptly increased in the late sporulation process, coinciding with the appearance of visible spores. Trehalase activity was absent in vegetative cells. A set of strains different in genetic constitution at the mating type loci was tested for induction of trehalase on nitrogen-free sporulation medium. The appearance of trehalase activity on the sporulation medium was observed only in sporulating cultures; cultures of homothallic strains (h 90) and diploid strains heterozygous for mating type (h +/h-), and mixed cultures of heterothallic h+ and h- strains. Trehalase activity was not induced in nonsporogenic strains: heterothallic haploid strains (h+ and h-), diploid strains homozygous for mating type (h+/h+ and h-/h-) and the homothallic strain harboring the mutation in the mat2 gene, which was unable to undergo the first meiotic division. Trehalose accumulation on the sporulation medium was observed solely in the sporulating cultures. These results led us to conclude that the induction of trehalase activity as well as the accumulation of trehalose in the medium lacking nitrogen sources was a sporulation-specific event under the control of the mating type genes.","authors":"Inoue H, Shimoda C","authors_abbrev":"Inoue H et al.","pubmed_publication_date":"1981","pubmed_entrez_date":"1981-01-01","publication_year":"1981","canto_session_key":"ce34ef6bbf1bf95d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-28 10:31:11","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-09-28 12:44:45","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMTR.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-09-28"},{"uniquename":"PMID:21148484","title":"Purification of actin from fission yeast Schizosaccharomyces pombe and characterization of functional differences from muscle actin.","citation":"J Biol Chem 2011 Feb 18;286(7):5784-92","abstract":"Fission yeast Schizosaccharomyces pombe is an important genetic model organism for studying the mechanisms of endocytosis and cytokinesis. However, most work on the biochemical properties of fission yeast actin-binding proteins has been done with skeletal muscle actin for matters of convenience. When simulations of mathematical models of the mechanism of endocytosis were compared with events in live cells, some of the reactions appeared to be much faster than observed in biochemical experiments with muscle actin. Here, we used gelsolin affinity chromatography to purify actin from fission yeast. S. pombe actin shares many properties with skeletal muscle actin but has higher intrinsic nucleotide exchange rate, faster trimer nucleus formation, faster phosphate dissociation rate from polymerized actin, and faster nucleation of actin filaments with Arp2/3 complex. These properties close the gap between the biochemistry and predictions made by mathematical models of endocytosis in S. pombe cells.","doi":"10.1074/jbc.M110.199794","authors":"Ti SC, Pollard TD","authors_abbrev":"Ti SC et al.","pubmed_publication_date":"18 Feb 2011","pubmed_entrez_date":"2010-12-15","publication_year":"2011","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC20G4.06c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU010570","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.93"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10071222","title":"Mutations in the Schizosaccharomyces pombe heat shock factor that differentially affect responses to heat and cadmium stress.","citation":"Mol Gen Genet 1999 Feb;261(1):161-9","abstract":"Heat shock factor (hsf) is the transcriptional activator that governs the transcriptional response of eukaryotic cells to stressful conditions. The structure and regulation of hsf is highly conserved. We describe deletion mutations in hsf+ that alter the ability of Schizosaccharomyces pombe to respond to different stressful conditions. One mutation causes increased sensitivity to cadmium while maintaining near normal sensitivity to heat stress, while another mutation confers increased sensitivity to heat stress but retains normal sensitivity to cadmium. Despite the differential sensitivity of these two strains to cadmium and heat stress, the mutant hsf proteins in each strain were activated by both cadmium and heat. However, we found that these mutations differentially affected the ability of hsf to activate different promoters: one mutated hsf activated the ssp1+ gene better than the wis2+ gene following either stress, while the other mutated hsf activated wis2+ better than ssp1+. We propose that the differential ability of strains that contain these mutant hsfs to survive cadmium and heat stress is not caused by differences in activation of hsf, but is caused instead by differential abilities of the mutant hsfs to activate the appropriate sets of genes needed for survival.","authors":"Saltsman KA, Prentice HL, Kingston RE","authors_abbrev":"Saltsman KA et al.","pubmed_publication_date":"Feb 1999","pubmed_entrez_date":"1999-03-10","publication_year":"1999","canto_session_key":"ede6ebd38992d401","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-02-19 17:48:49","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-02-19 17:48:34","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B3.03c","SPAC2E12.02"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-02-19"},{"uniquename":"PMID:19202278","title":"The och1 mutant of Schizosaccharomyces pombe produces galactosylated core structures of N-linked oligosaccharides.","citation":"Biosci Biotechnol Biochem 2009 Feb;73(2):407-14","abstract":"Unlike the budding yeast Saccharomyces cerevisiae, the fission yeast Schizosaccharomyces pombe synthesizes large outer chains on the N-linked oligosaccharides that consist mainly of D-Gal and D-Man residues. The fission yeast och1(+) gene product has alpha1,6-mannosyltransferase activity, and Och1p is the key enzyme in the initiation of outer chain elongation. Although the in vitro substrate specificity of S. pombe Och1p has been reported (Yoko-o et al., FEBS Lett., 489, 75-80 (2001)), the structure of the N-linked oligosaccharides of och1Delta cells has not been investigated. In this study, we report a structural analysis of S. pombe N-linked oligosaccharides. Lectin blot analysis indicated that galactose residues were attached to the cell surface glycoproteins of the och1Delta cells. We conducted a structural analysis of pyridylaminated N-linked oligosaccharides prepared from galactomannoproteins by HPLC and (1)H NMR. These analyses revealed that the N-linked oligosaccharides of the och1Delta cells displayed heterogeneity in the glycan consisting of Hex(11-15)GlcNAc(2). The structural heterogeneity arose mainly from the addition of alpha1,2- and alpha1,3-Gal residues to the Man(9)GlcNAc(2) core structure.","authors":"Ohashi T, Ikeda Y, Tanaka N, Nakakita S, Natsuka S, Giga-Hama Y, Takegawa K","authors_abbrev":"Ohashi T et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2009-02-10","publication_year":"2009","canto_session_key":"009ec61b646df625","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-11-07 17:42:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-31 17:54:18","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.03","SPAC1006.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-10-31"},{"uniquename":"PMID:965428","title":"Rates of synthesis of polyadenylated messenger RNA and ribosomal RNA during the cell cycle of Schizosaccharomyces pombe. With an appendix: calculation of the pattern of protein accumulation from observed changes in the rate of messenger RNA synthesis.","citation":"J Cell Sci 1976 Aug;21(3):497-521","abstract":"The rates of polyadenylated messenger RNA and ribosomal RNA synthesis were measured in synchronously dividing cultures of fission yeast (Schizosaccharomyces pombe). Control asynchronous cultures, which had been exposed to the conditions used for preparing synchronous cultures, were investigated to check for effects of the synchronization procedure itself on RNA synthesis. After each period of DNA synthesis in synchronous culture, the rates of messenger and ribosomal RNA synthesis doubled, suggesting that gene number controls the rate of messenger and ribosomal RNA synthesis. This was confirmed by experiments with asynchronous, exponential-phase cultures in which DNA synthesis was inhibited by hydroxyurea. Both synchronous culture and hydroxyurea experiments suggested that there is a delay of 15 min (0-1 of the cell generation time) between replication of the DNA and transcription of both gene copies. A pattern of protein accumulation was calculated from changes in the rate of polyadenylated messenger RNA synthesis during synchronous culture. The simulated pattern indicates that protein is accumulated linearly, with a doubling in the rate of accumulation once per cell cycle. The simulated pattern of protein accumulation is very similar to measurements previously reported by other workers of changes in activities of 3 enzymes in synchronous cultures. It is suggested that the doubling of the rate of messenger RNA synthesis, as a consequence of the replication of the DNA once per cycle, provides the basis of a mechanism for control of the doubling of other cellular constituents during the cell cycle.","authors":"Fraser RS, Moreno F","authors_abbrev":"Fraser RS et al.","pubmed_publication_date":"Aug 1976","pubmed_entrez_date":"1976-08-01","publication_year":"1976","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9638658","title":"Byr4, a dosage-dependent regulator of cytokinesis in S. pombe, interacts with a possible small GTPase pathway including Spg1 and Cdc16.","citation":"Mol Cells 1998 Apr 30;8(2):240-5","abstract":"Coordination between karyokinesis and cytokinesis in the cell division cycle is fundamental to a precise transmission of duplicated genome into dividing daughter cells. byr4, a previously isolated essential gene, affects the mitotic cell cycle and cytokinesis in S. pombe. Phenotypic analyses of the null alleles and the overexpression of byr4 suggest that byr4 is a dosage-dependent coordinator of karyokinesis and cytokinesis (Song et al., 1996). In this study, the functional mechanisms of byr4 were investigated using a byr4 mutant that exhibits byr4 overexpression phenotypes in thiamine deficient media. Genetic suppression analyses of this byr4 mutant with other cytokinesis regulatory genes in S. pombe, cdc16, cdc7, cdc15, cdc14, and plo1, show that byr4 overexpression phenotypes are suppressed by the overexpression of cdc16 and cdc7, but not by plo1, cdc14, and cdc15. Also, the basal expression of byr4 and cdc7 suppresses the temperature-sensitive cdc16 mutation. However, the basal expression of either byr4 or cdc16 does not suppress the temperature-sensitive cdc7 mutation. The results of these suppression tests suggest that byr4 genetically interacts with cdc16 and cdc7: byr4 functions at the same level with or downstream of cdc16 and upstream of cdc7. In the present study, we also show that Byr4 interacts with Cdc16 and Spg1 in the yeast two-hybrid assays. Recent reports suggest a possible small GTPase pathway to regulate the timing of cytokinesis where Cdc16 functions as a GAP (GTPase activating protein), Spg1 as a GTPase, and Cdc7 as a downstream effector. Combined genetic and two-hybrid analyses of this study strongly suggest that Byr4 directly interacts with this possible small GTPase pathway including Cdc16, Spg1, and Cdc7 to regulate cytokinesis in S. pombe.","authors":"Jwa M, Song K","authors_abbrev":"Jwa M et al.","pubmed_publication_date":"30 Apr 1998","pubmed_entrez_date":"1998-06-25","publication_year":"1998","canto_session_key":"fb4cc27075ec3038","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-12-30 09:45:43","canto_approved_date":"2020-12-30 09:45:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-12-30 09:45:25","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPAC1565.06c","SPBC21.06c","SPAC222.10c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2020-12-30"},{"uniquename":"PMID:29458562","title":"The fission yeast Schizosaccharomyces pombe Mtf2 is required for mitochondrial cox1 gene expression.","citation":"Microbiology (Reading) 2018 Mar;164(3):400-409","abstract":"Mitochondrial gene expression is essential for adenosine triphosphate synthesis via oxidative phosphorylation, which is the universal energy currency of cells. Here, we report the identification and characterization of a homologue of Saccharomyces cerevisiae Mtf2 (also called Nam1) in Schizosaccharomyces pombe. The Δmtf2 mutant with the intron-containing mitochondrial DNA (mtDNA) exhibited impaired growth on a rich medium containing the non-fermentable carbon source glycerol, suggesting that mtf2 is involved in mitochondrial function. mtf2 deletion in a mitochondrial intron-containing background resulted in a barely detectable level of the cox1 mRNA and a reduction in the level of the cob1 mRNA, and severely impaired cox1 translation. In contrast, mtf2 deletion in a mitochondrial intron-less background did not affect the levels of cox1 and cob1 mRNAs. However, Cox1 synthesis could not be restored to the control level in the Δmtf2 mutant with intron-less mtDNA. Our results suggest that unlike its counterpart in S. cerevisiae which plays a general role in synthesis of mtDNA-encoded proteins, S. pombe Mtf2 primarily functions in cox1 translation and the effect of mtf2 deletion on splicing of introns in mtDNA is likely due to a deficiency in the synthesis of intron-encoded maturases.","doi":"10.1099/mic.0.000602","authors":"Liu J, Li Y, Chen J, Wang Y, Zou M, Su R, Huang Y","authors_abbrev":"Liu J et al.","pubmed_publication_date":"Mar 2018","pubmed_entrez_date":"2018-02-21","publication_year":"2018","canto_session_key":"509fee002381b763","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2018-03-24 19:21:36","canto_approved_date":"2025-12-13 20:48:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-07 13:47:41","canto_added_date":"2018-02-28 22:13:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1296.02","SPMIT.04","SPMIT.01","SPMIT.11","SPMIT.05","SPAC5D6.12"],"gene_count":6,"ltp_gene_count":1,"approved_date":"2018-03-24"},{"uniquename":"PMID:11893740","title":"Interactions between fission yeast mRNA capping enzymes and elongation factor Spt5.","citation":"J Biol Chem 2002 May 31;277(22):19639-48","abstract":"Elongating RNA polymerase II is targeted by macromolecular assemblies that regulate mRNA synthesis and processing. The capping apparatus is the first of the assemblies to act on the nascent pre-mRNA. Although recruitment of the capping enzymes to the transcription complex is dependent on phosphorylation of the C-terminal domain of the Rpb1 subunit of polymerase II (Pol-II), there may be additional levels of control that coordinate capping with elongation. Here we show that the triphosphatase (Pct1) and guanylyltransferase (Pce1) enzymes of the fission yeast capping apparatus bind independently to the elongation factor Spt5. The C-terminal domain of the 990-amino acid Schizosaccharomyces pombe Spt5 protein, composed of repeats of a nonapeptide motif (consensus sequence TPAWNSGSK), is necessary and sufficient for binding to the capping enzymes in vivo (in a two-hybrid assay) and in vitro. As few as four nonamer repeats suffice for Spt5 binding to Pct1 in vitro, whereas six repeats are required for Spt5 binding to Pce1. A 116-amino acid fragment of the guanylyltransferase Pce1 suffices for binding to the Spt5 C-terminal domain (CTD) but not for binding to the Pol-II CTD. Pct1 and Pce1 can bind simultaneously to the Spt5 CTD in vitro. We find that Spt5 is essential for viability of S. pombe and that it interacts in vivo with S. pombe Spt4 via a central domain distinct from the Spt5 CTD. We suggest that Spt5-induced arrest of elongation at promoter proximal positions ensures a temporal window for recruitment of the capping enzymes.","authors":"Pei Y, Shuman S","authors_abbrev":"Pei Y et al.","pubmed_publication_date":"31 May 2002","pubmed_entrez_date":"2002-03-15","publication_year":"2002","canto_session_key":"a7783e0178e299cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-05-05 16:09:43","canto_approved_date":"2021-09-27 17:16:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-05-05 16:09:38","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":51,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_11893740_phaf.tsv"}],"genes":["SPAC644.04","SPBC2F12.08c","SPBC21C3.16c","SPBC28F2.12","SPAC23C4.19"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-05-05"},{"uniquename":"PMID:36551189","title":"Regulation Mechanisms of Meiotic Recombination Revealed from the Analysis of a Fission Yeast Recombination Hotspot  ade6-M26 .","citation":"Biomolecules 2022 Nov 26;12(12)","abstract":"Meiotic recombination is a pivotal event that ensures faithful chromosome segregation and creates genetic diversity in gametes. Meiotic recombination is initiated by programmed double-strand breaks (DSBs), which are catalyzed by the conserved Spo11 protein. Spo11 is an enzyme with structural similarity to topoisomerase II and induces DSBs through the nucleophilic attack of the phosphodiester bond by the hydroxy group of its tyrosine (Tyr) catalytic residue. DSBs caused by Spo11 are repaired by homologous recombination using homologous chromosomes as donors, resulting in crossovers/chiasmata, which ensure physical contact between homologous chromosomes. Thus, the site of meiotic recombination is determined by the site of the induced DSB on the chromosome. Meiotic recombination is not uniformly induced, and sites showing high recombination rates are referred to as recombination hotspots. In fission yeast,  ade6-M26 , a nonsense point mutation of  ade6  is a well-characterized meiotic recombination hotspot caused by the heptanucleotide sequence 5'-ATGACGT-3' at the  M26  mutation point. In this review, we summarize the meiotic recombination mechanisms revealed by the analysis of the fission  ade6-M26  gene as a model system.","doi":"10.3390/biom12121761","authors":"Hirota K","authors_abbrev":"Hirota K","pubmed_publication_date":"26 Nov 2022","pubmed_entrez_date":"2022-12-23","publication_year":"2022","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2022-12-24 01:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1367623","title":"Yeast systems for the commercial production of heterologous proteins.","citation":"Biotechnology (N Y) 1991 Nov;9(11):1067-72","abstract":"Yeasts are attractive hosts for the production of heterologous proteins. Unlike prokaryotic systems, their eukaryotic subcellular organization enables them to carry out many of the post-translational folding, processing and modification events required to produce \"authentic\" and bioactive mammalian proteins. In addition, they retain the advantages of a unicellular microorganism, with respect to rapid growth and ease of genetic manipulation. The vast majority of yeast expression work has focused on the well-characterized baker's yeast Saccharomyces cerevisiae. However, with the development of DNA transformation technologies, a growing number of non-Saccharomyces yeasts are becoming available as hosts for recombinant polypeptide production. These include Hansenula polymorpha, Kluyveromyces lactis, Pichia pastoris, Schizosaccharomyces pombe, Schwanniomyces occidentalis and Yarrowia lipolytica. The performance of these alternative yeast expression systems is reviewed here relative to S. cerevisiae, and the advantages and limitations of these systems are discussed.","authors":"Buckholz RG, Gleeson MA","authors_abbrev":"Buckholz RG et al.","pubmed_publication_date":"Nov 1991","pubmed_entrez_date":"1991-11-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24115911","title":"Structure of UreG/UreF/UreH complex reveals how urease accessory proteins facilitate maturation of Helicobacter pylori urease.","citation":"PLoS Biol 2013 Oct;11(10):e1001678","abstract":"Urease is a metalloenzyme essential for the survival of Helicobacter pylori in acidic gastric environment. Maturation of urease involves carbamylation of Lys219 and insertion of two nickel ions at its active site. This process requires GTP hydrolysis and the formation of a preactivation complex consisting of apo-urease and urease accessory proteins UreF, UreH, and UreG. UreF and UreH form a complex to recruit UreG, which is a SIMIBI class GTPase, to the preactivation complex. We report here the crystal structure of the UreG/UreF/UreH complex, which illustrates how UreF and UreH facilitate dimerization of UreG, and assembles its metal binding site by juxtaposing two invariant Cys66-Pro67-His68 metal binding motif at the interface to form the (UreG/UreF/UreH)2 complex. Interaction studies revealed that addition of nickel and GTP to the UreG/UreF/UreH complex releases a UreG dimer that binds a nickel ion at the dimeric interface. Substitution of Cys66 and His68 with alanine abolishes the formation of the nickel-charged UreG dimer. This nickel-charged UreG dimer can activate urease in vitro in the presence of the UreF/UreH complex. Static light scattering and atomic absorption spectroscopy measurements demonstrated that the nickel-charged UreG dimer, upon GTP hydrolysis, reverts to its monomeric form and releases nickel to urease. Based on our results, we propose a mechanism on how urease accessory proteins facilitate maturation of urease.","doi":"10.1371/journal.pbio.1001678","authors":"Fong YH, Wong HC, Yuen MH, Lau PH, Chen YW, Wong KB","authors_abbrev":"Fong YH et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-10-12","publication_year":"2013","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC29A4.13","SPAC3A12.09c","SPCPB16A4.05c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:26918805","title":"Consequences of abnormal CDK activity in S phase.","citation":"Cell Cycle 2016;15(7):963-73","abstract":"Cyclin Dependent Kinases (CDKs) are important regulators of DNA replication. In this work we have investigated the consequences of increasing or decreasing the CDK activity in S phase. To this end we identified S-phase regulators of the fission yeast CDK, Cdc2, and used appropriate mutants to modulate Cdc2 activity. In fission yeast Mik1 has been thought to be the main regulator of Cdc2 activity in S phase. However, we find that Wee1 has a major function in S phase and thus we used wee1 mutants to investigate the consequences of increased Cdc2 activity. These wee1 mutants display increased replication stress and, particularly in the absence of the S-phase checkpoint, accumulate DNA damage. Notably, more cells incorporate EdU in a wee1(-) strain as compared to wildtype, suggesting altered regulation of DNA replication. In addition, a higher number of cells contain chromatin-bound Cdc45, an indicator of active replication forks. In addition, we found that Cdc25 is required to activate Cdc2 in S phase and used a cdc25 mutant to explore a situation where Cdc2 activity is reduced. Interestingly, a cdc25 mutant has a higher tolerance for replication stress than wild-type cells, suggesting that reduced CDK activity in S phase confers resistance to at least some forms of replication stress.","doi":"10.1080/15384101.2016.1152423","authors":"Anda S, Rothe C, Boye E, Grallert B","authors_abbrev":"Anda S et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-02-27","publication_year":"2016","canto_session_key":"667fe5fdf54cf125","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-28 01:15:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPAC29B12.03","SPCC18B5.03","SPBC216.05","SPCC18B5.11c","SPAC24H6.05","SPBC660.14"],"gene_count":7,"ltp_gene_count":6},{"uniquename":"PMID:24173579","title":"RNAi function, diversity, and loss in the fungal kingdom.","citation":"Chromosome Res 2013 Dec;21(6-7):561-72","abstract":"RNAi is conserved and has been studied in a broad cross-section of the fungal kingdom, including Neurospora crassa, Schizosaccharomyces pombe, Cryptococcus neoformans, and Mucor circinelloides. And yet well known species, including the model yeast Saccharomyces cerevisiae and the plant pathogen Ustilago maydis, have lost RNAi, providing insights and opportunities to illuminate benefits conferred both by the presence of RNAi and its loss. Some of the earliest studies of RNAi were conducted in Neurospora, contemporaneously with the elucidation of RNAi in Caenorhabditis elegans. RNAi is a key epigenetic mechanism for maintaining genomic stability and integrity, as well as to defend against viruses, and given its ubiquity was likely present in the last eukaryotic common ancestor. In this review, we describe the diversity of RNAi mechanisms found in the fungi, highlighting recent work in Neurospora, S. pombe, and Cryptococcus. Finally, we consider frequent, independent losses of RNAi in diverse fungal lineages and both review and speculate on evolutionary forces that may drive the losses or result therefrom.","doi":"10.1007/s10577-013-9388-2","authors":"Billmyre RB, Calo S, Feretzaki M, Wang X, Heitman J","authors_abbrev":"Billmyre RB et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-01","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-11-03 08:45:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28494091","title":"Fermentation Characteristics and Aromatic Profile of Plum Wines Produced with Indigenous Microbiota and Pure Cultures of Selected Yeast.","citation":"J Food Sci 2017 Jun;82(6):1443-1450","abstract":"The aim of this study was to assess and compare fermentation characteristics and aromatic profile of plum wines produced with indigenous microbiota and pure cultures of different selected yeast. Experiments were carried out with plum (Prunus domestica L.) varieties of different fruit ripening times (Čačanska rana, Čačanska lepotica, and Požegača). Wine fermentations were conducted by the activity of indigenous microbiota, commercially available Saccharomyces cerevisiae and Saccharomyces bayanus yeast strains and joint activity of Schizosaccharomyces pombe and S. cerevisiae (sequential inoculation). Statistically significant differences in fermentative characteristics and the content of certain volatile compounds were observed as a result of metabolic activity of various indigenous and/or selected yeasts during fermentation of plum pomace. Minimal duration of fermentation (4 to 5 d) and fastest ethanol production rate (from 12.3 to 15.5 g/L/d) were the characteristics of the studied S. cerevisiae strains. Isobutanol, 3-methyl-1-butanol, 1-heptanol, and 1-octanol were the most prevalent higher alcohols in the tested plum wine samples. The predominant ester in plum wines was ethyl acetate, ethyl lactate, amyl acetate, isoamyl acetate, and ethyl palmitate, esters responsible for the floral and fruity olfactory tones, were also present in large amounts. Also, the use of S. cerevisiae strains resulted in the production of plum wines with better sensory characteristics than ones produced with other investigated yeasts. Obtained results are significant since there is limited data on the compounds responsible for the unique flavor of plum wine, as well as on the impact of different yeast starter cultures application on the overall quality of fruit wines.","doi":"10.1111/1750-3841.13736","authors":"Miljić U, Puškaš V, Vučurović V, Muzalevski A","authors_abbrev":"Miljić U et al.","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2017-05-12","publication_year":"2017","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2017-05-13 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25635048","title":"Evolutionarily conserved binding of translationally controlled tumor protein to eukaryotic elongation factor 1B.","citation":"J Biol Chem 2015 Apr 03;290(14):8694-710","abstract":"Translationally controlled tumor protein (TCTP) is an abundant protein that is highly conserved in eukaryotes. However, its primary function is still not clear. Human TCTP interacts with the metazoan-specific eukaryotic elongation factor 1Bδ (eEF1Bδ) and inhibits its guanine nucleotide exchange factor (GEF) activity, but the structural mechanism remains unknown. The interaction between TCTP and eEF1Bδ was investigated by NMR titration, structure determination, paramagnetic relaxation enhancement, site-directed mutagenesis, isothermal titration calorimetry, and HADDOCK docking. We first demonstrated that the catalytic GEF domain of eEF1Bδ is not responsible for binding to TCTP but rather a previously unnoticed central acidic region (CAR) domain in eEF1Bδ. The mutagenesis data and the structural model of the TCTP-eEF1Bδ CAR domain complex revealed the key binding residues. These residues are highly conserved in eukaryotic TCTPs and in eEF1B GEFs, including the eukaryotically conserved eEF1Bα, implying the interaction may be conserved in all eukaryotes. Interactions were confirmed between TCTP and the eEF1Bα CAR domain for human, fission yeast, and unicellular photosynthetic microalgal proteins, suggesting that involvement in protein translation through the conserved interaction with eEF1B represents a primary function of TCTP.","doi":"10.1074/jbc.M114.628594","authors":"Wu H, Gong W, Yao X, Wang J, Perrett S, Feng Y","authors_abbrev":"Wu H et al.","pubmed_publication_date":"03 Apr 2015","pubmed_entrez_date":"2015-01-31","publication_year":"2015","canto_session_key":"3bd7b8426557a053","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-01-31 15:27:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-31 15:27:26","canto_added_date":"2015-01-31 14:29:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F12.02c","SPCC1450.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-01-31"},{"uniquename":"PMID:14676319","title":"Phylogenomic analysis of type I polyketide synthase genes in pathogenic and saprobic ascomycetes.","citation":"Proc Natl Acad Sci U S A 2003 Dec 23;100(26):15670-5","abstract":"Fungal type I polyketides (PKs) are synthesized by PK synthases (PKSs) and include well known secondary metabolites such as the anticholesterol drug lovastatin and the potent natural carcinogen aflatoxin. Other type I PKs are known to be virulence factors for some plant pathogens and pigments such as melanin. In this study, a phylogenomic approach was used to investigate the origin and diversity of fungal genes encoding putative PKSs that are predicted to synthesize type I PKs. The resulting genealogy, constructed by using the highly conserved PKS ketosynthase (KS) domain, indicated that: (i). Species within subphylum Pezizomycotina (phylum Ascomycota) but not early diverging ascomycetes, like Saccharomyces cerevisiae (Saccharomycotina) or Schizosaccharomyces pombe (Taphrinomycotina), had large numbers (7-25) of PKS genes. (ii). Bacteria and fungi had separate groups of PKS genes; the few exceptions are the likely result of horizontal gene transfer from bacteria to various sublineages of fungi. (iii). The bulk of genes encoding fungal PKSs fell into eight groups. Four groups were predicted to synthesize variously reduced PKs, and four groups were predicted to make unreduced PKs. (iv). Species within different classes of Pezizomycotina shared the same groups of PKS genes. (v). Different fungal genomes shared few putative orthologous PKS genes, even between closely related genomes in the same class or genus. (vi) The discontinuous distributions of orthologous PKSs among fungal species can be explained by gene duplication, divergence, and gene loss; horizontal gene transfer among fungi does not need to be invoked.","authors":"Kroken S, Glass NL, Taylor JW, Yoder OC, Turgeon BG","authors_abbrev":"Kroken S et al.","pubmed_publication_date":"23 Dec 2003","pubmed_entrez_date":"2003-12-17","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32964921","title":"Smc5/6, an atypical SMC complex with two RING-type subunits.","citation":"Biochem Soc Trans 2020 Oct 30;48(5):2159-2171","abstract":"The Smc5/6 complex plays essential roles in chromosome segregation and repair, by promoting disjunction of sister chromatids. The core of the complex is constituted by an heterodimer of Structural Maintenance of Chromosomes (SMC) proteins that use ATP hydrolysis to dynamically associate with and organize chromosomes. In addition, the Smc5/6 complex contains six non-SMC subunits. Remarkably, and differently to other SMC complexes, the Nse1 and Nse2 subunits contain RING-type domains typically found in E3 ligases, pointing to the capacity to regulate other proteins and complexes through ubiquitin-like modifiers. Nse2 codes for a C-terminal SP-RING domain with SUMO ligase activity, assisting Smc5/6 functions in chromosome segregation through sumoylation of several chromosome-associated proteins. Nse1 codes for a C-terminal NH-RING domain and, although it has been proposed to have ubiquitin ligase activity, no Smc5/6-dependent ubiquitylation target has been described to date. Here, we review the function of the two RING domains of the Smc5/6 complex in the broader context of SMC complexes as global chromosome organizers of the genome.","doi":"10.1042/BST20200389","authors":"Solé-Soler R, Torres-Rosell J","authors_abbrev":"Solé-Soler R et al.","pubmed_publication_date":"30 Oct 2020","pubmed_entrez_date":"2020-09-23","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-08-11 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29423843","title":"Analysis of Fission Yeast Single DNA Molecules on the Megabase Scale Using DNA Combing.","citation":"Methods Mol Biol 2018;1721:9-24","abstract":"DNA combing enables the quantitative analysis of DNA replication, DNA recombination, DNA-protein interaction, and DNA methylation along genomic single DNA molecules at 1 kb resolution. However, DNA combing has been restricted to short 200-500 kb long DNA fragments, which introduces significant bias in data analysis. An improved DNA combing methodology that allows to routinely image Mb-scale single DNA molecules and occasionally up to full-length fission yeast chromosomes is presented in this chapter. DNA combing of Mb-scale single DNA molecules can be applied to accurately measure the dynamic properties of DNA replication such as the rate of origin firing, replication fork velocity, fork directionality and the frequency of fork blockage. In addition, Mb-scale single DNA molecules enable the quantitative analysis of complex genomic rearrangements including gross chromosomal translocations, repetitive DNA sequences, large deletions, and duplications, which are difficult to investigate with deep sequencing strategies.","doi":"10.1007/978-1-4939-7546-4_2","authors":"Kaykov A, Nurse P","authors_abbrev":"Kaykov A et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31180322","title":"Cooperation between tropomyosin and α-actinin inhibits fimbrin association with actin filament networks in fission yeast.","citation":"Elife 2019 Jun 10;8","abstract":"We previously discovered that competition between fission yeast actin binding proteins (ABPs) for binding F-actin facilitates their sorting to different cellular networks. Specifically, competition between endocytic actin patch ABPs fimbrin Fim1 and cofilin Adf1 enhances their activities, and prevents tropomyosin Cdc8's association with actin patches. However, these interactions do not explain how Fim1 is prevented from associating strongly with other F-actin networks such as the contractile ring. Here, we identified α-actinin Ain1, a contractile ring ABP, as another Fim1 competitor. Fim1 competes with Ain1 for association with F-actin, which is dependent upon their F-actin residence time. While Fim1 outcompetes both Ain1 and Cdc8 individually, Cdc8 enhances the F-actin bundling activity of Ain1, allowing Ain1 to generate F-actin bundles that Cdc8 can bind in the presence of Fim1. Therefore, the combination of contractile ring ABPs Ain1 and Cdc8 is capable of inhibiting Fim1's association with F-actin networks.","doi":"10.7554/eLife.47279","authors":"Christensen JR, Homa KE, Morganthaler AN, Brown RR, Suarez C, Harker AJ, O'Connell ME, Kovar DR","authors_abbrev":"Christensen JR et al.","pubmed_publication_date":"10 Jun 2019","pubmed_entrez_date":"2019-06-11","publication_year":"2019","canto_session_key":"7ffa6ef54106be21","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-06-12 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15A10.08","SPAC27F1.02c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:36287046","title":"Quantitative Assessment of Histone H2B Monoubiquitination in Yeast Using Immunoblotting.","citation":"Methods Protoc 2022 Sep 24;5(5)","abstract":"Studies in  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe  have enhanced our understanding of the regulation and functions of histone H2B monoubiquitination (H2Bub1), a key epigenetic marker with important roles in transcription and other processes. The detection of H2Bub1 in yeasts using immunoblotting has been greatly facilitated by the commercial availability of antibodies against yeast histone H2B and the cross-reactivity of an antibody raised against monoubiquitinated human H2BK120. These antibodies have obviated the need to express epitope-tagged histone H2B to detect H2Bub1 in yeasts. Here, we provide a step-by-step protocol and best practices for the quantification of H2Bub1 in yeast systems, from cell extract preparation to immunoblotting using the commercially available antibodies. We demonstrate that the commercial antibodies can effectively and accurately detect H2Bub1 in  S. cerevisiae  and  S. pombe . Further, we show that the C-terminal epitope-tagging of histone H2B alters the steady-state levels of H2Bub1 in yeast systems. We report a sectioned blot probing approach combined with the serial dilution of protein lysates and the use of reversibly stained proteins as loading controls that together provide a cost-effective and sensitive method for the quantitative evaluation of H2Bub1 in yeast.","doi":"10.3390/mps5050074","authors":"Leng AM, Radmall KS, Shukla PK, Chandrasekharan MB","authors_abbrev":"Leng AM et al.","pubmed_publication_date":"24 Sep 2022","pubmed_entrez_date":"2022-10-26","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-10-28 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7809130","title":"Comparisons of eukaryotic genomic sequences.","citation":"Proc Natl Acad Sci U S A 1994 Dec 20;91(26):12832-6","abstract":"A method for assessing genomic similarity based on relative abundances of short oligonucleotides in large DNA samples is introduced. The method requires neither homologous sequences nor prior sequence alignments. The analysis centers on (i) dinucleotide (and tri- and tetra-) relative abundance extremes in genomic sequences, (ii) distances between sequences based on all dinucleotide relative abundance values, and (iii) a multidimensional partial ordering protocol. The emphasis in this paper is on assessments of general relatedness of genomes as distinguished from phylogenetic reconstructions. Our methods demonstrate that the relative abundance distances almost always differ more for genomic interspecific sequence comparisons than for genomic intraspecific sequence comparisons, indicating congruence over different genome sequence samples. The genomic comparisons are generally concordant with accepted phylogenies among vertebrate and among fungal species sequences. Several unexpected relationships between the major groups of metazoa, fungal, and protist DNA emerge, including the following. (i) Schizosaccharomyces pombe and Saccharomyces cerevisiae in dinucleotide relative abundance distances are as similar to each other as human is to bovine. (ii) S. cerevisiae, although substantially far from, is significantly closer to the vertebrates than are the invertebrates (Drosophila melanogaster, Bombyx mori, and Caenorhabditis elegans). This phenomenon may suggest variable evolutionary rates during the metazoan radiations and slower changes in the fungal divergences, and/or a polyphyletic origin of metazoa. (iii) The genomic sequences of D. melanogaster and Trypanosoma brucei are strikingly similar. This DNA similarity might be explained by some molecular adaptation of the parasite to its dipteran (tsetse fly) host, a host-parasite gene transfer hypothesis. Robustness of the methods may be due to a genomic signature of dinucleotide relative abundance values reflecting DNA structures related to dinucleotide stacking energies, constraints of DNA curvature, and mechanisms attendant to replication, repair, and recombination.","authors":"Karlin S, Ladunga I","authors_abbrev":"Karlin S et al.","pubmed_publication_date":"20 Dec 1994","pubmed_entrez_date":"1994-12-20","publication_year":"1994","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35147499","title":"The MIDAS domain of AAA mechanoenzyme Mdn1 forms catch bonds with two different substrates.","citation":"Elife 2022 Feb 11;11","abstract":"Catch bonds are a form of mechanoregulation wherein protein-ligand interactions are strengthened by the application of dissociative tension. Currently, the best-characterized examples of catch bonds are between single protein-ligand pairs. The essential AAA (ATPase associated with diverse cellular activities) mechanoenzyme Mdn1 drives at least two separate steps in ribosome biogenesis, using its MIDAS domain to extract the ubiquitin-like (UBL) domain-containing proteins Rsa4 and Ytm1 from ribosomal precursors. However, it must subsequently release these assembly factors to reinitiate the enzymatic cycle. The mechanism underlying the switching of the MIDAS-UBL interaction between strongly and weakly bound states is unknown. Here, we use optical tweezers to investigate the force dependence of MIDAS-UBL binding. Parallel experiments with Rsa4 and Ytm1 show that forces up to ~4 pN, matching the magnitude of force produced by AAA proteins similar to Mdn1, enhance the MIDAS domain binding lifetime up to 10-fold, and higher forces accelerate dissociation. Together, our studies indicate that Mdn1's MIDAS domain can form catch bonds with more than one UBL substrate, and provide insights into how mechanoregulation may contribute to the Mdn1 enzymatic cycle during ribosome biogenesis.","doi":"10.7554/eLife.73534","authors":"Mickolajczyk KJ, Olinares PDB, Chait BT, Liu S, Kapoor TM","authors_abbrev":"Mickolajczyk KJ et al.","pubmed_publication_date":"11 Feb 2022","pubmed_entrez_date":"2022-02-11","publication_year":"2022","canto_session_key":"8c23265e650c312e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-03-04 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22615807","title":"Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe.","citation":"PLoS One 2012;7(5):e36768","abstract":"Sm-like (Lsm) proteins are ubiquitous and function in many aspects of RNA metabolism, including pre-mRNA splicing, nuclear RNA processing, mRNA decay and miRNA biogenesis. Here three crystal structures including Lsm3, Lsm4 and Lsm5/6/7 sub-complex from S. pombe are reported. These structures show that all the five individual Lsm subunits share a conserved Sm fold, and Lsm3, Lsm4, and Lsm5/6/7 form a heptamer, a trimer and a hexamer within the crystal lattice, respectively. Analytical ultracentrifugation indicates that Lsm3 and Lsm5/6/7 sub-complex exist in solution as a heptamer and a hexamer, respectively while Lsm4 undergoes a dynamic equilibrium between monomer and trimer in solution. RNA binding assays show that Lsm2/3 and Lsm5/6/7 bind to oligo(U) whereas no RNA binding is observed for Lsm3 and Lsm4. Analysis of the inter-subunit interactions in Lsm5/6/7 reveals the organization order among Lsm5, Lsm6 and Lsm7.","doi":"10.1371/journal.pone.0036768","authors":"Wu D, Jiang S, Bowler MW, Song H","authors_abbrev":"Wu D et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-05-23","publication_year":"2012","canto_session_key":"c9f33602640ff7ad","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-02-15 17:57:12","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-02-15 17:57:00","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":15,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC1620.01c","SPBC30D10.06","SPAC2F3.17c","SPBC20F10.09","SPCC285.12","SPBC9B6.05c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2017-02-15","pdb_entries":[{"pdb_id":"4emg","gene_chains":[{"gene_uniquename":"SPBC9B6.05c","chain":"A/B/C/D/E/F/G/H/I/J/K/L/M/N","position":"1-93"}],"title":"Crystal structure of SpLsm3","entry_authors":"Jiang SM,Wu DH,Song HW","entry_authors_abbrev":"Jiang SM et al.","reference_uniquename":"PMID:22615807","experimental_method":"X-ray","resolution":"2.7"},{"pdb_id":"4emh","gene_chains":[{"gene_uniquename":"SPBC30D10.06","chain":"A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/T/U/V/W/X/Y","position":"1-91"}],"title":"Crystal structure of SpLsm4","entry_authors":"Jiang SM,Wu DH,Song HW","entry_authors_abbrev":"Jiang SM et al.","reference_uniquename":"PMID:22615807","experimental_method":"X-ray","resolution":"2.2"},{"pdb_id":"4emk","gene_chains":[{"gene_uniquename":"SPBC20F10.09","chain":"A","position":"1-80"},{"gene_uniquename":"SPCC285.12","chain":"C","position":"1-113"},{"gene_uniquename":"SPAC2F3.17c","chain":"B","position":"1-75"}],"title":"Crystal structure of SpLsm5/6/7","entry_authors":"Jiang SM,Wu DH,Song HW","entry_authors_abbrev":"Jiang SM et al.","reference_uniquename":"PMID:22615807","experimental_method":"X-ray","resolution":"2.3"}]},{"uniquename":"PMID:40543417","title":"The Obg-like ATPase Ola1 prevents excessive mitochondrial reactive oxygen species by inhibiting MAPK/Pmk1 signaling in fission yeast.","citation":"Microbiol Res 2025 Jun 16;299:128259","abstract":"Ola1 plays critical roles in maintaining cellular homeostasis by regulating the cell cycle, translation, and heat shock responses. Additionally, it modulates antioxidant responses and redox homeostasis, processes in which mitochondria are key contributors. However, the precise mechanism by which Ola1 modules mitochondrial reactive oxygen species (mtROS) levels and the functional consequences of this regulation remain poorly understood. In this study, we demonstrate that the absence of Ola1 leads to increased mtROS levels through the modulation of the MAPK/Pmk1 signaling pathway in the fission yeast Schizosaccharomyces pombe. We further establish that Ola1 physically interacts with both MAPK/Pmk1 and its upstream kinase Pek1 (MAPKK), thereby inhibiting MAPK/Pmk1 signaling. Moreover, we show that increased mtROS levels in cells lacking Ola1 promote nuclear localization of the stress-responsive transcription factor Hsf1 and upregulate Ssa1, the fission yeast homolog of mammalian Hsp70. Therefore, our findings uncover a previously uncharacterized role of Ola1 in modulating mtROS through the MAPK/Pmk1 signaling pathway and underscore the crucial function of Ola1 in stress response and the maintenance of cellular homeostasis.","doi":"10.1016/j.micres.2025.128259","authors":"Luo S, Zhu M, Fu C","authors_abbrev":"Luo S et al.","pubmed_publication_date":"16 Jun 2025","pubmed_entrez_date":"2025-06-21","publication_year":"2025","canto_session_key":"02ab4de8de36d301","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-06-22 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC27E2.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25411334","title":"The Rho-GEF Gef3 interacts with the septin complex and activates the GTPase Rho4 during fission yeast cytokinesis.","citation":"Mol Biol Cell 2015 Jan 15;26(2):238-55","abstract":"Rho GTPases, activated by Rho guanine nucleotide exchange factors (GEFs), are conserved molecular switches for signal transductions that regulate diverse cellular processes, including cell polarization and cytokinesis. The fission yeast Schizosaccharomyces pombe has six Rho GTPases (Cdc42 and Rho1-Rho5) and seven Rho GEFs (Scd1, Rgf1-Rgf3, and Gef1-Gef3). The GEFs for Rho2-Rho5 have not been unequivocally assigned. In particular, Gef3, the smallest Rho GEF, was barely studied. Here we show that Gef3 colocalizes with septins at the cell equator. Gef3 physically interacts with septins and anillin Mid2 and depends on them to localize. Gef3 coprecipitates with GDP-bound Rho4 in vitro and accelerates nucleotide exchange of Rho4, suggesting that Gef3 is a GEF for Rho4. Consistently, Gef3 and Rho4 are in the same genetic pathways to regulate septum formation and/or cell separation. In gef3∆ cells, the localizations of two potential Rho4 effectors--glucanases Eng1 and Agn1--are abnormal, and active Rho4 level is reduced, indicating that Gef3 is involved in Rho4 activation in vivo. Moreover, overexpression of active Rho4 or Eng1 rescues the septation defects of mutants containing gef3∆. Together our data support that Gef3 interacts with the septin complex and activates Rho4 GTPase as a Rho GEF for septation in fission yeast.","doi":"10.1091/mbc.E14-07-1196","authors":"Wang N, Wang M, Zhu YH, Grosel TW, Sun D, Kudryashov DS, Wu JQ","authors_abbrev":"Wang N et al.","pubmed_publication_date":"15 Jan 2015","pubmed_entrez_date":"2014-11-21","publication_year":"2015","canto_session_key":"e7582f1802a42934","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jian-Qiu Wu","canto_first_approved_date":"2016-09-03 16:31:57","canto_approved_date":"2024-06-26 10:30:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-17 20:52:52","canto_added_date":"2014-11-22 01:16:49","annotation_curators":[{"name":"Jian-Qiu Wu","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC970.09","SPAC16A10.04","SPCC895.05","SPAC821.09","SPCC1919.10c","SPCC16C4.07","SPAC24H6.09","SPAC14C4.09","SPAPYUG7.03c","SPAC23C4.08","SPBC29A3.17","SPBC106.20","SPBC16A3.01","SPAC4F10.11","SPAC110.03"],"gene_count":15,"ltp_gene_count":12,"approved_date":"2016-09-03"},{"uniquename":"PMID:27657680","title":"A dominant variant in DMXL2 is linked to nonsyndromic hearing loss.","citation":"Genet Med 2017 May;19(5):553-558","abstract":"To explore the genetic etiology of deafness in a dominant family with late-onset, progressive, nonsyndromic hearing loss.\nGenome-wide linkage analysis was performed for 21 family members. Candidate pathogenic variants were identified by whole-exome sequencing of selected family members and confirmed by Sanger sequencing of all family members. Cochlear expression of Dmxl2 was investigated by reverse-transcription polymerase chain reaction (RT-PCR) and immunostaining of the organ of Corti from mice.\nThe causative gene was mapped to a 9.68-Mb candidate region on chromosome 15q21.2 (maximum logarithm of the odds score = 4.03) that contained no previously described deafness genes. Whole-exome sequencing identified heterozygous c.7250G>A (p.Arg2417His) in DMXL2 as the only candidate pathogenic variant segregating the hearing loss. In mouse cochlea, expression of DMXL2 was restricted to the hair cells and the spiral ganglion neurons.\nOur data indicated that the p.Arg2417His variant in DMXL2 is associated with dominant, nonsyndromic hearing loss and suggested an important role of DMXL2 in inner ear function.Genet Med advance online publication 22 September 2016.","doi":"10.1038/gim.2016.142","authors":"Chen DY, Liu XF, Lin XJ, Zhang D, Chai YC, Yu DH, Sun CL, Wang XL, Zhu WD, Chen Y, Sun LH, Wang XW, Shi FX, Huang ZW, Yang T, Wu H","authors_abbrev":"Chen DY et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2016-09-23","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1105.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15908586","title":"The CHD remodeling factor Hrp1 stimulates CENP-A loading to centromeres.","citation":"Nucleic Acids Res 2005;33(9):2868-79","abstract":"Centromeres of fission yeast are arranged with a central core DNA sequence flanked by repeated sequences. The centromere-associated histone H3 variant Cnp1 (SpCENP-A) binds exclusively to central core DNA, while the heterochromatin proteins and cohesins bind the surrounding outer repeats. CHD (chromo-helicase/ATPase DNA binding) chromatin remodeling factors were recently shown to affect chromatin assembly in vitro. Here, we report that the CHD protein Hrp1 plays a key role at fission yeast centromeres. The hrp1Delta mutant disrupts silencing of the outer repeats and central core regions of the centromere and displays chromosome segregation defects characteristic for dysfunction of both regions. Importantly, Hrp1 is required to maintain high levels of Cnp1 and low levels of histone H3 and H4 acetylation at the central core region. Hrp1 interacts directly with the centromere in early S-phase when centromeres are replicated, suggesting that Hrp1 plays a direct role in chromatin assembly during DNA replication.","authors":"Walfridsson J, Bjerling P, Thalen M, Yoo EJ, Park SD, Ekwall K","authors_abbrev":"Walfridsson J et al.","pubmed_publication_date":"2005","pubmed_entrez_date":"2005-05-24","publication_year":"2005","canto_session_key":"e64d08d70519aefd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-28 13:04:33","canto_approved_date":"2024-01-18 12:01:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-26 09:42:25","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1105.17","SPAC1687.20c","SPAC1834.04","SPAC688.02c","SPAC1783.05","SPAC3G6.01","SPCC188.13c","SPBC1105.11c","SPBC8D2.04","SPCC290.04"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2023-02-28"},{"uniquename":"PMID:16291757","title":"Stress-induced response, localization, and regulation of the Pmk1 cell integrity pathway in Schizosaccharomyces pombe.","citation":"J Biol Chem 2006 Jan 27;281(4):2033-43","abstract":"Mitogen-activated protein kinase (MAPK) signaling pathways are critical for the sensing and response of eukaryotic cells to extracellular changes. In Schizosaccharomyces pombe, MAPK Pmk1/Spm1 has been involved in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis, as part of the so-called cell integrity pathway together with MAPK kinase kinase Mkh1 and MAPK kinase Pek1. We show that Pmk1 is activated in multiple stress situations, including hyper- or hypotonic stress, glucose deprivation, presence of cell wall-damaging compounds, and oxidative stress induced by hydrogen peroxide or pro-oxidants. The stress-induced activation of Pmk1 was completely dependent on Mkh1 and Pek1 function, supporting a nonbranched pathway in the regulation of MAPK activation. Fluorescence microscopy revealed that Mkh1, Pek1, and Pmp1 (a protein phosphatase that inactivates Pmk1) are cytoplasmic proteins. Mkh1 and Pek1 were also found at the septum, whereas Pmk1 localized in both cytoplasm and nucleus as well as in the mitotic spindle and septum during cytokinesis. Interestingly, Pmk1 subcellular localization was unaffected by stress or the absence of Mkh1 and Pek1, suggesting that its activation by the Mkh1-Pek1 cascade takes place at the cytoplasm and/or septum and that the active and inactive forms of this kinase cross the nuclear membrane. Cdc42 GTPase and its effectors, p21-activated kinases Pak2 and Pak1, are not upstream elements controlling the basal level or the stress-induced activation of Pmk1. However, Sty1 MAPK was essential for proper Pmk1 deactivation after hypertonic stress in a process regulated by Atf1 transcription factor. These results provide the first evidence for the existence of cross-talk between two MAPK cascades during the stress response in fission yeast.","authors":"Madrid M, Soto T, Khong HK, Franco A, Vicente J, Pérez P, Gacto M, Cansado J","authors_abbrev":"Madrid M et al.","pubmed_publication_date":"27 Jan 2006","pubmed_entrez_date":"2005-11-18","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC119.08","SPBC543.07","SPBC1685.01","SPAC1F3.02c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:8029017","title":"Nonhomologous DNA end joining in Schizosaccharomyces pombe efficiently eliminates DNA double-strand-breaks from haploid sequences.","citation":"Nucleic Acids Res 1994 Jun 11;22(11):2094-101","abstract":"Cells of higher eucaryotes are known to possess mechanisms of illegitimate recombination which promote the joining between nonhomologous ends of broken DNA and thus may serve as basic tools of double-strand-break (DSB) repair. Here we show that cells of the fission yeast Schizosaccharomyces pombe also contain activities of nonhomologous DNA end joining resembling the ones found in higher eucaryotes. Nonhomologous end joining activities were detected by transformation of linearized self-replicating plasmids in yeast cells employing a selection procedure which only propagates transformants carrying recircularized plasmid molecules. Linear plasmid substrates were generated by duplicate restriction cuts carrying either blunt ends or 3' or 5' protruding single strands (PSS) of 4 nt which were efficiently joined in any tested combination. Sequence analysis of joined products revealed that junctional sequences were shortened by 1 to 14 nt. Two mechanisms may account for junction formation (i) loss of terminal nucleotides from PSS tails to produce blunt ends which can be joined to abutting ends and (ii) interactions of DNA termini at patches of sequence homologies (1-4 bp) by formation of overlap intermediates which are subsequently processed. A general feature of the yeast joining system is that end joining can only be detected in the absence of sequence homology between the linear substrate and host genome. In the presence of homology, nonhomologous DNA end joining is efficiently competed by activities of homologous recombination.","authors":"Goedecke W, Pfeiffer P, Vielmetter W","authors_abbrev":"Goedecke W et al.","pubmed_publication_date":"11 Jun 1994","pubmed_entrez_date":"1994-06-11","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23394829","title":"Identification of SIN pathway targets reveals mechanisms of crosstalk between NDR kinase pathways.","citation":"Curr Biol 2013 Feb 18;23(4):333-8","abstract":"The septum initiation network (SIN) regulates multiple functions during late mitosis to ensure successful completion of cytokinesis in Schizosaccharomyces pombe. One mechanism by which the SIN promotes cytokinesis is by inhibiting a competing polarity pathway called the MOR, which is required for initiation of polarized growth following completion of cytokinesis. Mutual antagonism between the two NDR kinase pathways, SIN and MOR, is required to coordinate cytoskeletal rearrangements during the mitosis-interphase transition. To determine how the SIN regulates the MOR pathway, we developed a proteomics approach that allowed us to identify multiple substrates of the SIN effector kinase Sid2, including the MOR pathway components Nak1 kinase and an associated protein, Sog2. We show that Sid2 phosphorylation of Nak1 causes removal of Nak1 from the spindle pole bodies, which may both relieve Nak1 inhibition of the SIN and block MOR signaling by preventing interaction of Nak1 with the scaffold protein Mor2. Because the SIN and MOR are conserved in mammalian cells (Hippo and Ndr1/2 pathways, respectively), this work may provide important insight into how the activities of these essential pathways are coordinated.","doi":"10.1016/j.cub.2013.01.014","authors":"Gupta S, Mana-Capelli S, McLean JR, Chen CT, Ray S, Gould KL, McCollum D","authors_abbrev":"Gupta S et al.","pubmed_publication_date":"18 Feb 2013","pubmed_entrez_date":"2013-02-12","publication_year":"2013","canto_session_key":"72fbfb14c00e0ddd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-08-29 15:51:49","canto_approved_date":"2019-10-30 14:56:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-03-21 14:29:25","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":31,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.05","SPCC645.07","SPCC16C4.07","SPBC887.09c","SPBC20F10.06","SPAC3G9.05","SPAC6F6.08c","SPAC1782.09c","SPBP19A11.04c","SPBC106.01","SPBC32C12.03c","SPAC9G1.09","SPAC17A2.13c","SPBC17F3.02","SPAC24B11.11c","SPAC16E8.08","SPCC1739.11c","SPAC8E11.02c","SPCC1902.02","SPAC4A8.15c","SPAPB1A10.09"],"gene_count":21,"ltp_gene_count":19,"approved_date":"2018-08-29"},{"uniquename":"PMID:30968190","title":"The evolution of peptide mating pheromones in fission yeast.","citation":"Curr Genet 2019 Oct;65(5):1107-1111","abstract":"In fungi, sexual reproduction primarily depends on the interaction between peptide pheromones and their receptors. Most ascomycete fungi produce two classes of peptide mating pheromones, a simple peptide and a modified peptide. These peptides are recognized by their corresponding receptors on the surface of cells of the opposite mating type to induce the mating reaction. Pheromone diversification may be associated with reproductive isolation, which restricts gene flow among populations; thus, it remains unclear how pheromones diversify without loss of successful mating. Here, I provide a brief review of recent findings on the 'asymmetric' diversification of peptide pheromones in the fission yeast Schizosaccharomyces pombe, and discuss evolution of the mating pheromones in fission yeast.","doi":"10.1007/s00294-019-00968-w","authors":"Seike T","authors_abbrev":"Seike T","pubmed_publication_date":"Oct 2019","pubmed_entrez_date":"2019-04-11","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-04-12 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39143218","title":"Structural basis for transthiolation intermediates in the ubiquitin pathway.","citation":"Nature 2024 Sep;633(8028):216-223","abstract":"Transthiolation (also known as transthioesterification) reactions are used in the biosynthesis of acetyl coenzyme A, fatty acids and polyketides, and for post-translational modification by ubiquitin (Ub) and ubiquitin-like (Ubl) proteins 1-3 . For the Ub pathway, E1 enzymes catalyse transthiolation from an E1~Ub thioester to an E2~Ub thioester. Transthiolation is also required for transfer of Ub from an E2~Ub thioester to HECT (homologous to E6AP C terminus) and RBR (ring-between-ring) E3 ligases to form E3~Ub thioesters 4-6 . How isoenergetic transfer of thioester bonds is driven forward by enzymes in the Ub pathway remains unclear. Here we isolate mimics of transient transthiolation intermediates for E1-Ub(T)-E2 and E2-Ub(T)-E3 HECT  complexes (where T denotes Ub in a thioester or Ub undergoing transthiolation) using a chemical strategy with native enzymes and near-native Ub to capture and visualize a continuum of structures determined by single-particle cryo-electron microscopy. These structures and accompanying biochemical experiments illuminate conformational changes in Ub, E1, E2 and E3 that are coordinated with the chemical reactions to facilitate directional transfer of Ub from each enzyme to the next.","doi":"10.1038/s41586-024-07828-9","authors":"Kochańczyk T, Hann ZS, Lux MC, Delos Reyes AMV, Ji C, Tan DS, Lima CD","authors_abbrev":"Kochańczyk T et al.","pubmed_publication_date":"Sep 2024","pubmed_entrez_date":"2024-08-14","publication_year":"2024","canto_triage_status":"Structure","canto_curator_role":"PomBase","canto_added_date":"2024-09-26 23:25:07","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC337.08c","SPBC119.02","SPAC1805.12c","SPAC1805.15c","SPBC1604.21c"],"gene_count":5,"ltp_gene_count":5,"pdb_entries":[{"pdb_id":"9b5t","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - cluster 5 map and model (ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.16"},{"pdb_id":"9b5x","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - Ub(T) class 10 map and model from cluster 5 (ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"4.16"},{"pdb_id":"9b5w","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - Ub(T) class 1 map and model from cluster 5 (ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.96"},{"pdb_id":"9b5c","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - consensus map and model","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.5"},{"pdb_id":"9b5m","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - consensus map and model","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.79"},{"pdb_id":"9b55","gene_chains":[{"gene_uniquename":"SPAC1805.12c","chain":"B","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"A","position":"1-147"},{"gene_uniquename":"SPAC1805.15c","chain":"C","position":"295-671"}],"title":"Ubiquitin E2-Ub-E3 HECT tetrahedral transthiolation intermediate mimic - state 1","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.23"},{"pdb_id":"9b5a","gene_chains":[{"gene_uniquename":"SPAC1805.12c","chain":"B","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"A","position":"1-147"},{"gene_uniquename":"SPAC1805.15c","chain":"C","position":"295-671"}],"title":"Ubiquitin E2-Ub-E3 HECT tetrahedral transthiolation intermediate mimic - state 6","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.65"},{"pdb_id":"9b5i","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPBC337.08c","chain":"B","position":"305-380"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - cluster 4 map and model (Ub(A)-AMP/PPi/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.7"},{"pdb_id":"9b57","gene_chains":[{"gene_uniquename":"SPAC1805.12c","chain":"B","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"A","position":"1-147"},{"gene_uniquename":"SPAC1805.15c","chain":"C","position":"295-671"}],"title":"Ubiquitin E2-Ub-E3 HECT tetrahedral transthiolation intermediate mimic - state 3","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.37"},{"pdb_id":"9b5g","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - cluster 2 map and model (Ub(A)/ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.67"},{"pdb_id":"9b5e","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - Ub(T) class 10 map and model from consensus","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.81"},{"pdb_id":"9b59","gene_chains":[{"gene_uniquename":"SPAC1805.12c","chain":"B","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"A","position":"1-147"},{"gene_uniquename":"SPAC1805.15c","chain":"C","position":"295-671"}],"title":"Ubiquitin E2-Ub-E3 HECT tetrahedral transthiolation intermediate mimic - state 5","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.49"},{"pdb_id":"9b5v","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - Ub(T) class 10 map and model from cluster 1 (ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.94"},{"pdb_id":"9b5d","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - Ub(T) class 1 map and model from consensus","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.8"},{"pdb_id":"9b5r","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - cluster 3 map and model (ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.95"},{"pdb_id":"9b5j","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - cluster 5 map and model (Ub(A)-AMP)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.86"},{"pdb_id":"9b5f","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPBC337.08c","chain":"B","position":"305-380"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - cluster 1 map and model (Ub(A)/ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.78"},{"pdb_id":"9b5p","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - cluster 1 map and model (ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.08"},{"pdb_id":"9b5n","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - Ub(T) class 1 map and model from consensus","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.12"},{"pdb_id":"9b5l","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPBC337.08c","chain":"B","position":"305-380"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - Ub(T) class 10 map and model from cluster 5 (Ub(A)-AMP)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.3"},{"pdb_id":"9b58","gene_chains":[{"gene_uniquename":"SPAC1805.12c","chain":"B","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"A","position":"1-147"},{"gene_uniquename":"SPAC1805.15c","chain":"C","position":"295-671"}],"title":"Ubiquitin E2-Ub-E3 HECT tetrahedral transthiolation intermediate mimic - state 4","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.39"},{"pdb_id":"9b5o","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - Ub(T) class 10 map and model from consensus","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.19"},{"pdb_id":"9b56","gene_chains":[{"gene_uniquename":"SPAC1805.12c","chain":"B","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"A","position":"1-147"},{"gene_uniquename":"SPAC1805.15c","chain":"C","position":"295-671"}],"title":"Ubiquitin E2-Ub-E3 HECT tetrahedral transthiolation intermediate mimic - state 2","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.35"},{"pdb_id":"9b5h","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - cluster 3 map and model (Ub(A)-AMP/PPi/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.69"},{"pdb_id":"9b5s","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - cluster 4 map and model (ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.96"},{"pdb_id":"9b5b","gene_chains":[{"gene_uniquename":"SPAC1805.12c","chain":"B","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"A","position":"1-147"},{"gene_uniquename":"SPAC1805.15c","chain":"C","position":"295-671"}],"title":"Ubiquitin E2-Ub-E3 HECT tetrahedral transthiolation intermediate mimic - state 7","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.31"},{"pdb_id":"9b5q","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - cluster 2 map and model (ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"2.95"},{"pdb_id":"9b5u","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (singly Ub-loaded) - Ub(T) class 1 map and model from cluster 1 (ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.67"},{"pdb_id":"9b5k","gene_chains":[{"gene_uniquename":"SPBC1604.21c","chain":"A","position":"13-1012"},{"gene_uniquename":"SPAC1805.12c","chain":"B/D","position":"1-75"},{"gene_uniquename":"SPBC119.02","chain":"C","position":"1-147"}],"title":"Ubiquitin E1-Ub-E2 tetrahedral transthiolation intermediate mimic (doubly Ub-loaded) - Ub(T) class 1 map and model from cluster 1 (Ub(A)/ATP/Mg)","entry_authors":"Kochanczyk T,Lima CD","entry_authors_abbrev":"Kochanczyk T et al.","reference_uniquename":"PMID:39143218","experimental_method":"EM","resolution":"3.16"}]},{"uniquename":"PMID:36820394","title":"Inorganic polyphosphate abets silencing of a sub-telomeric gene cluster in fission yeast.","citation":"MicroPubl Biol 2023;2023","abstract":"Inorganic polyphosphate is a ubiquitous polymer with myriad roles in cell and organismal physiology. Whereas there is evidence for nuclear polyphosphate, its impact on transcriptional regulation in eukaryotes is unkown. Transcriptional profiling of fission yeast cells lacking polyphosphate (via deletion of the catalytic subunit Vtc4 of the Vtc4/Vtc2 polyphosphate polymerase complex) elicited de-repression of four protein-coding genes located within the right sub-telomeric arm of chromosome I that is known to be transcriptionally silenced by the TORC2 complex. These genes were equally de-repressed in  vtc2  ∆ cells and in cells expressing polymerase-dead Vtc4, signifying that polyphosphate synthesis is required for repression of these sub-telomeric genes.","doi":"10.17912/micropub.biology.000744","authors":"Sanchez AM, Garg A, Schwer B, Shuman S","authors_abbrev":"Sanchez AM et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-02-23","publication_year":"2023","canto_session_key":"7e7d155c2e0f6d6b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2023-04-17 13:34:44","canto_approved_date":"2023-04-17 13:34:44","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-04-11 17:30:03","canto_added_date":"2023-02-24 01:15:04","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":51,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.04","SPAC13G7.02c","SPCC794.01c","SPBC16E9.16c","SPCC338.12","SPBC29B5.02c","SPBC24C6.09c","SPAC14C4.11","SPAP8A3.04c","SPBC660.06","SPCC1223.13","SPBC1711.15c","SPBC1289.14","SPCC794.04c","SPCC1322.14c","SPAC27D7.03c","SPAC23A1.10","SPBC1815.01","SPCC1235.14","SPBC336.08","SPCC1020.06c","SPBC354.12","SPCC794.09c","SPAC22A12.17c","SPAC186.01","SPBC725.10","SPAC186.04c","SPBC839.15c","SPBC21C3.19","SPAC26F1.14c","SPBC16A3.08c","SPAC23H3.15c","SPAC750.01","SPACUNK4.17","SPAC637.03","SPAC26H5.09c","SPAC1039.09","SPAC1805.10","SPAC15E1.02c","SPBC23G7.13c","SPAC186.06","SPBPB21E7.01c","SPBPB8B6.04c","SPAC186.05c"],"gene_count":44,"ltp_gene_count":2,"approved_date":"2023-04-17"},{"uniquename":"PMID:8524294","title":"Schizosaccharomyces pombe skp1+ encodes a protein kinase related to mammalian glycogen synthase kinase 3 and complements a cdc14 cytokinesis mutant.","citation":"Mol Cell Biol 1996 Jan;16(1):179-91","abstract":"We report the cloning of the skp1+ gene, a Schizosaccharomyces pombe homolog of the glycogen synthase kinase 3 (GSK-3) family whose members in higher eukaryotes are involved in cell fate determination, nuclear signalling, and hormonal regulation. skp1 is 67% identical to mammalian GSK-3 beta and displays similar biochemical properties in vitro. Like GSK-3 beta, skp1 is phosphorylated on a conserved tyrosine residue, and this phosphorylation is required for efficient activity. skp1 is also phosphorylated at a serine which has been identified as S-335. Phosphorylation at this site is likely to inhibit its function. Unlike the mammalian enzyme, skp1 both tyrosine autophosphorylates in yeast cells and can phosphorylate other proteins on tyrosine in bacteria. The skp1+ gene is not essential. However, cells with deletions in skp1+ are sensitive to heat shock and exhibit defects in sporulation. Overexpression of wild-type skp1+ specifically complements cdc14-118, one of several mutations causing a defect in cytokinesis. In addition, certain phosphorylation site mutants induce a delay or block in cytokinesis when overexpressed. Together, these data identify novel interactions of a fission yeast GSK-3 homolog with elements of the cytokinesis machinery.","authors":"Plyte SE, Feoktistova A, Burke JD, Woodgett JR, Gould KL","authors_abbrev":"Plyte SE et al.","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_session_key":"d37836a2104d53bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-04 15:35:13","canto_approved_date":"2024-03-28 12:56:22","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-08-08 08:52:16","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.15","SPBC24C6.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-10-04"},{"uniquename":"PMID:10518997","title":"Life cycles of yeast spindle pole bodies: getting microtubules into a closed nucleus.","citation":"Biol Cell 1999;91(4-5):305-12","abstract":"The spindle pole body (SPB) is the principal microtubule organizing center of budding and fission yeast. We have examined SPBs and their associated microtubules from both organisms, using electron microscopy and three-dimensional reconstruction techniques, to identify the structural changes that accompany progression through the cell cycle. In this report, we compare these changes in the two kinds of yeasts and present a model for how microtubules get into a closed nucleus.","authors":"McIntosh JR, O'Toole ET","authors_abbrev":"McIntosh JR et al.","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-10-16","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37699057","title":"pomBseen: An automated pipeline for analysis of fission yeast images.","citation":"PLoS One 2023;18(9):e0291391","abstract":"Fission yeast is a model organism widely used for studies of eukaryotic cell biology. As such, it is subject to bright-field and fluorescent microscopy. Manual analysis of such data can be laborious and subjective. Therefore, we have developed pomBseen, an image analysis pipeline for the quantitation of fission yeast micrographs containing a bright-field channel and up to two fluorescent channels. It accepts a wide range of image formats and produces a table with the size and total and nuclear fluorescent intensities of the cells in the image. Benchmarking of the pipeline against manually annotated datasets demonstrates that it reliably segments cells and acquires their image parameters. Written in MATLAB, pomBseen is also available as a standalone application.","doi":"10.1371/journal.pone.0291391","authors":"Ohira M, Rhind N","authors_abbrev":"Ohira M et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-09-12","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-09-13 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39126071","title":"Utilizing Deep Neural Networks to Fill Gaps in Small Genomes.","citation":"Int J Mol Sci 2024 Aug 04;25(15)","abstract":"With the widespread adoption of next-generation sequencing technologies, the speed and convenience of genome sequencing have significantly improved, and many biological genomes have been sequenced. However, during the assembly of small genomes, we still face a series of challenges, including repetitive fragments, inverted repeats, low sequencing coverage, and the limitations of sequencing technologies. These challenges lead to unknown gaps in small genomes, hindering complete genome assembly. Although there are many existing assembly software options, they do not fully utilize the potential of artificial intelligence technologies, resulting in limited improvement in gap filling. Here, we propose a novel method, DLGapCloser, based on deep learning, aimed at assisting traditional tools in further filling gaps in small genomes. Firstly, we created four datasets based on the original genomes of  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe ,  Neurospora crassa , and  Micromonas pusilla . To further extract effective information from the gene sequences, we also added homologous genomes to enrich the datasets. Secondly, we proposed the DGCNet model, which effectively extracts features and learns context from sequences flanking gaps. Addressing issues with early pruning and high memory usage in the Beam Search algorithm, we developed a new prediction algorithm, Wave-Beam Search. This algorithm alternates between expansion and contraction phases, enhancing efficiency and accuracy. Experimental results showed that the Wave-Beam Search algorithm improved the gap-filling performance of assembly tools by 7.35%, 28.57%, 42.85%, and 8.33% on the original results. Finally, we established new gap-filling standards and created and implemented a novel evaluation method. Validation on the genomes of  Saccharomyces cerevisiae ,  Schizosaccharomyces pombe ,  Neurospora crassa , and  Micromonas pusilla  showed that DLGapCloser increased the number of filled gaps by 8.05%, 15.3%, 1.4%, and 7% compared to traditional assembly tools.","doi":"10.3390/ijms25158502","authors":"Chen Y, Wang G, Zhang T","authors_abbrev":"Chen Y et al.","pubmed_publication_date":"04 Aug 2024","pubmed_entrez_date":"2024-08-10","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-08-10 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8537450","title":"DNA polymerase alpha, a component of the replication initiation complex, is essential for the checkpoint coupling S phase to mitosis in fission yeast.","citation":"J Cell Sci 1995 Sep;108 ( Pt 9):3109-18","abstract":"Genetic analysis in the yeast Schizosaccharomyces pombe has shown that three genes cdc18, cut5, and cdt1, are essential for DNA synthesis and also for the checkpoint control that couples completion of DNA replication to the onset of mitosis. To test whether assembly of the replication initiation complex is an important element in the checkpoint control pathway we have investigated if DNA polymerase alpha (pol1), a component of the initiation complex, is essential for the S-phase checkpoint control. We show that germinating S. pombe spores disrupted for the pol1 gene enter mitosis despite defects in DNA synthesis. This is shown by monitoring septation index, DNA content, and by direct immunofluorescence of mitotic spindles using antibodies to alpha-tubulin. In addition we have isolated six temperature sensitive mutants in the pol1 gene that cause cell cycle arrest when grown at the nonpermissive temperature. Our experiments support a model in which DNA polymerase alpha, in addition to being part of the initiation complex, is required for a checkpoint signal that is activated as cells traverse START, and is essential to prevent mitosis until S phase has been completed. In contrast, proteins responsible for the elongation of DNA may not be necessary for this checkpoint signal.","authors":"D'Urso G, Grallert B, Nurse P","authors_abbrev":"D'Urso G et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_session_key":"8d38eba2ecda335a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-02-10 09:32:15","canto_approved_date":"2026-01-29 15:27:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-18 16:13:29","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3H5.06c","SPBC16D10.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-02-10"},{"uniquename":"PMID:28871121","title":"Effects of cycloheximide on the interpretation of ribosome profiling experiments in Schizosaccharomyces pombe.","citation":"Sci Rep 2017 Sep 04;7(1):10331","abstract":"Stress conditions lead to global and gene-specific changes in RNA translation. Ribosome profiling experiments have identified genome-wide alterations in the distribution of ribosomes along mRNAs. However, it is contentious whether these changes reflect real responses, or whether they are artefacts caused by the use of inhibitors of translation (notably cycloheximide). To address this issue we performed ribosome profiling with the fission yeast Schizosaccharomyces pombe under conditions of exponential growth (unstressed) and nitrogen starvation (nutritional stress), and both in the presence and absence of cycloheximide. We examined several aspects of the translational response, including density of ribosomal footprints on coding sequences, 5' leader ribosomal densities, distribution of ribosomes along coding sequences, and ribosome codon occupancies. Cycloheximide had minor effects on overall ribosome density, which affected mostly mRNAs encoding ribosomal proteins. Nitrogen starvation caused an accumulation of ribosomes on 5' leaders in both cycloheximide-treated and untreated cells. By contrast, stress-induced ribosome accumulation on the 5' side of coding sequences was cycloheximide-dependent. Finally, codon occupancy showed strong positive correlations in cycloheximide-treated and untreated cells. Our results demonstrate that cycloheximide does influence some of the results of ribosome profiling experiments, although it is not clear if this effect is always artefactual.","doi":"10.1038/s41598-017-10650-1","authors":"Duncan CDS, Mata J","authors_abbrev":"Duncan CDS et al.","pubmed_publication_date":"04 Sep 2017","pubmed_entrez_date":"2017-09-06","publication_year":"2017","canto_session_key":"0fc3eb7ca076ede2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-09-07 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11058076","title":"Chk1 and Cds1: linchpins of the DNA damage and replication checkpoint pathways.","citation":"J Cell Sci 2000 Nov;113 ( Pt 22)(Pt 22):3889-96","abstract":"Recent work on the mechanisms of DNA damage and replication cell cycle checkpoints has revealed great similarity between the checkpoint pathways of organisms as diverse as yeasts, flies and humans. However, there are differences in the ways these organisms regulate their cell cycles. To connect the conserved checkpoint pathways with various cell cycle targets requires an adaptable link that can target different cell cycle components in different organisms. The Chk1 and Cds1 protein kinases, downstream effectors in the checkpoint pathways, seem to play just such roles. Perhaps more surprisingly, the two kinases not only have different targets in different organisms but also seem to respond to different signals in different organisms. So, whereas in fission yeast Chk1 is required for the DNA damage checkpoint and Cds1 is specifically involved in the replication checkpoint, their roles seem to be shuffled in metazoans.","authors":"Rhind N, Russell P","authors_abbrev":"Rhind N et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-11-01","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18653539","title":"Caspase-dependent and -independent lipotoxic cell-death pathways in fission yeast.","citation":"J Cell Sci 2008 Aug 15;121(Pt 16):2671-84","abstract":"Understanding the mechanisms underlying lipid-induced cell death has significant implications in both cell biology and human diseases. Previously, we showed that fission-yeast Schizosaccharomyces pombe cells deficient in triacylglycerol synthesis display apoptotic markers upon entry into stationary phase. Here, we characterize the sequential molecular events that take place at the onset of cell death in S. pombe, including a surge of diacylglycerol, post-mitotic arrest, alterations in mitochondrial activities and in intracellular redox balance, chromatin condensation, nuclear-envelope fragmentation, and eventually plasma-membrane permeabilization. Our results demonstrated active roles of mitochondria and reactive oxygen species in cell death, and identified novel cell-death regulators--including metacaspase Pca1, BH3-domain protein Rad9, and diacylglycerol-binding proteins Pck1 and Bzz1. Most importantly, we show that, under different conditions and stimuli, failure to maintain intracellular-lipid homeostasis can lead to cell death with different phenotypic manifestations, genetic criteria and cellular mechanisms, pointing to the existence of multiple lipotoxic pathways in this organism. Our study represents the first in-depth analysis of cell-death pathways in S. pombe.","doi":"10.1242/jcs.028977","authors":"Low CP, Shui G, Liew LP, Buttner S, Madeo F, Dawes IW, Wenk MR, Yang H","authors_abbrev":"Low CP et al.","pubmed_publication_date":"15 Aug 2008","pubmed_entrez_date":"2008-07-26","publication_year":"2008","canto_session_key":"a60531b182edb2d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-11-19 09:42:18","canto_approved_date":"2021-06-22 14:16:59","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-11-02 12:35:40","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":15,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1235.15","SPCC1840.04","SPBC12C2.05c","SPAC664.07c","SPAC17G8.14c","SPBC776.14"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-11-19"},{"uniquename":"PMID:17355287","title":"A gene duplication led to specialized gamma-aminobutyrate and beta-alanine aminotransferase in yeast.","citation":"FEBS J 2007 Apr;274(7):1804-17","abstract":"In humans, beta-alanine (BAL) and the neurotransmitter gamma-aminobutyrate (GABA) are transaminated by a single aminotransferase enzyme. Apparently, yeast originally also had a single enzyme, but the corresponding gene was duplicated in the Saccharomyces kluyveri lineage. SkUGA1 encodes a homologue of Saccharomyces cerevisiae GABA aminotransferase, and SkPYD4 encodes an enzyme involved in both BAL and GABA transamination. SkPYD4 and SkUGA1 as well as S. cerevisiae UGA1 and Schizosaccharomyces pombe UGA1 were subcloned, over-expressed and purified. One discontinuous and two continuous coupled assays were used to characterize the substrate specificity and kinetic parameters of the four enzymes. It was found that the cofactor pyridoxal 5'-phosphate is needed for enzymatic activity and alpha-ketoglutarate, and not pyruvate, as the amino group acceptor. SkPyd4p preferentially uses BAL as the amino group donor (V(max)/K(m)=0.78 U x mg(-1) x mm(-1)), but can also use GABA (V(max)/K(m)=0.42 U x mg(-1) x mm(-1)), while SkUga1p only uses GABA (V(max)/K(m)=4.01 U x mg(-1) x mm(-1)). SpUga1p and ScUga1p transaminate only GABA and not BAL. While mammals degrade BAL and GABA with only one enzyme, but in different tissues, S. kluyveri and related yeasts have two different genes/enzymes to apparently 'distinguish' between the two reactions in a single cell. It is likely that upon duplication approximately 200 million years ago, a specialized Uga1p evolved into a 'novel' transaminase enzyme with broader substrate specificity.","authors":"Andersen G, Andersen B, Dobritzsch D, Schnackerz KD, Piskur J","authors_abbrev":"Andersen G et al.","pubmed_publication_date":"Apr 2007","pubmed_entrez_date":"2007-03-16","publication_year":"2007","canto_session_key":"e04357e1270cbd51","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-09-18 19:14:14","canto_approved_date":"2026-01-17 10:46:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-09-18 19:14:01","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2022-09-18"},{"uniquename":"PMID:26359299","title":"Fission yeast kinesin-8 controls chromosome congression independently of oscillations.","citation":"J Cell Sci 2015 Oct 15;128(20):3720-30","abstract":"In higher eukaryotes, efficient chromosome congression relies, among other players, on the activity of chromokinesins. Here, we provide a quantitative analysis of kinetochore oscillations and positioning in Schizosaccharomyces pombe, a model organism lacking chromokinesins. In wild-type cells, chromosomes align during prophase and, while oscillating, maintain this alignment throughout metaphase. Chromosome oscillations are dispensable both for kinetochore congression and stable kinetochore alignment during metaphase. In higher eukaryotes, kinesin-8 family members control chromosome congression by regulating their oscillations. By contrast, here, we demonstrate that fission yeast kinesin-8 controls chromosome congression by an alternative mechanism. We propose that kinesin-8 aligns chromosomes by controlling pulling forces in a length-dependent manner. A coarse-grained model of chromosome segregation implemented with a length-dependent process that controls the force at kinetochores is necessary and sufficient to mimic kinetochore alignment, and prevents the appearance of lagging chromosomes. Taken together, these data illustrate how the local action of a motor protein at kinetochores provides spatial cues within the spindle to align chromosomes and to prevent aneuploidy.","doi":"10.1242/jcs.160465","authors":"Mary H, Fouchard J, Gay G, Reyes C, Gauthier T, Gruget C, Pécréaux J, Tournier S, Gachet Y","authors_abbrev":"Mary H et al.","pubmed_publication_date":"15 Oct 2015","pubmed_entrez_date":"2015-09-12","publication_year":"2015","canto_session_key":"5ade41ae7e0543d6","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-09-13 00:18:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24385151","title":"Synchronized fission yeast meiosis using an ATP analog-sensitive Pat1 protein kinase.","citation":"Nat Protoc 2014 Jan;9(1):223-31","abstract":"Synchronous cultures are often indispensable for studying meiosis. Here we present an optimized protocol for induction of synchronous meiosis in the fission yeast Schizosaccharomyces pombe. Chemical inactivation of an ATP analog-sensitive form of the Pat1 kinase (pat1-as2) by adding the ATP analog 1-NM-PP1 in G1-arrested cells allows the induction of synchronous meiosis at optimal temperature (25°C). Importantly, this protocol eliminates detrimental effects of elevated temperature (34°C), which is required to inactivate the commonly used temperature-sensitive Pat1 kinase mutant (pat1-114). The addition of the mat-Pc gene to a mat1-M strain further improves chromosome segregation and spore viability. Thus, our protocol offers highly synchronous meiosis at optimal temperature, with most characteristics similar to those of wild-type meiosis. The synchronization protocol can be completed in 5 d (not including strain production, which may take as long as 2 or 3 months).","doi":"10.1038/nprot.2014.013","authors":"Cipak L, Polakova S, Hyppa RW, Smith GR, Gregan J","authors_abbrev":"Cipak L et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2014-01-04","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11959501","title":"Transcription factor complexes.","citation":"Curr Opin Struct Biol 2002 Apr;12(2):225-30","abstract":"Considerable progress has been made during the past year on structural studies of the eukaryotic and bacterial transcription factors that control RNA polymerase function via the formation of multiprotein complexes on promoter DNA. Recently determined structures include negative cofactor 2 recognizing a preformed TATA-box-binding protein-DNA binary complex, a dimer of BmrR bound to both DNA and tetra-phenylphosphonium, DNA-bound complexes of SarA and FadR, leukemia-associated AML1-CBFbeta-DNA ternary complexes and a SAP1-SRF-DNA ternary complex.","authors":"Burley SK, Kamada K","authors_abbrev":"Burley SK et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-18","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23245849","title":"Sculpting of DNA at abasic sites by DNA glycosylase homolog mag2.","citation":"Structure 2013 Jan 08;21(1):154-166","abstract":"Modifications and loss of bases are frequent types of DNA lesions, often handled by the base excision repair (BER) pathway. BER is initiated by DNA glycosylases, generating abasic (AP) sites that are subsequently cleaved by AP endonucleases, which further pass on nicked DNA to downstream DNA polymerases and ligases. The coordinated handover of cytotoxic intermediates between different BER enzymes is most likely facilitated by the DNA conformation. Here, we present the atomic structure of Schizosaccharomyces pombe Mag2 in complex with DNA to reveal an unexpected structural basis for nonenzymatic AP site recognition with an unflipped AP site. Two surface-exposed loops intercalate and widen the DNA minor groove to generate a DNA conformation previously only found in the mismatch repair MutS-DNA complex. Consequently, the molecular role of Mag2 appears to be AP site recognition and protection, while possibly facilitating damage signaling by structurally sculpting the DNA substrate.","doi":"10.1016/j.str.2012.11.004","authors":"Dalhus B, Nilsen L, Korvald H, Huffman J, Forstrøm RJ, McMurray CT, Alseth I, Tainer JA, Bjørås M","authors_abbrev":"Dalhus B et al.","pubmed_publication_date":"08 Jan 2013","pubmed_entrez_date":"2012-12-19","publication_year":"2013","canto_session_key":"416865874f3e468b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-02-24 14:53:54","canto_approved_date":"2025-09-04 06:49:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-14 20:25:22","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.11","SPAC30D11.07","SPBC3D6.10","SPAPB24D3.04c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2020-02-24","pdb_entries":[{"pdb_id":"4b22","gene_chains":[{"gene_uniquename":"SPBC23G7.11","chain":"A","position":"1-213"}],"title":"Unprecedented sculpting of DNA at abasic sites by DNA glycosylase homolog Mag2","entry_authors":"Dalhus B,Nilsen L,Korvald H,Huffman J,Forstrom RJ,McMurray CT,Alseth I,Tainer JA,Bjoras M","entry_authors_abbrev":"Dalhus B et al.","reference_uniquename":"PMID:23245849","experimental_method":"X-ray","resolution":"1.9"},{"pdb_id":"4b23","gene_chains":[{"gene_uniquename":"SPBC23G7.11","chain":"A","position":"1-213"}],"title":"Unprecedented sculpting of DNA at abasic sites by DNA glycosylase homolog Mag2","entry_authors":"Dalhus B,Nilsen L,Korvald H,Huffman J,Forstrom RJ,McMurray CT,Alseth I,Tainer JA,Bjoras M","entry_authors_abbrev":"Dalhus B et al.","reference_uniquename":"PMID:23245849","experimental_method":"X-ray","resolution":"2.0"},{"pdb_id":"4b21","gene_chains":[{"gene_uniquename":"SPBC23G7.11","chain":"A","position":"1-213"}],"title":"Unprecedented sculpting of DNA at abasic sites by DNA glycosylase homolog Mag2","entry_authors":"Dalhus B,Nilsen L,Korvald H,Huffman J,Forstrom RJ,McMurray CT,Alseth I,Tainer JA,Bjoras M","entry_authors_abbrev":"Dalhus B et al.","reference_uniquename":"PMID:23245849","experimental_method":"X-ray","resolution":"1.45"},{"pdb_id":"4b24","gene_chains":[{"gene_uniquename":"SPBC23G7.11","chain":"A","position":"1-213"}],"title":"Unprecedented sculpting of DNA at abasic sites by DNA glycosylase homolog Mag2","entry_authors":"Dalhus B,Nilsen L,Korvald H,Huffman J,Forstrom RJ,McMurray CT,Alseth I,Tainer JA,Bjoras M","entry_authors_abbrev":"Dalhus B et al.","reference_uniquename":"PMID:23245849","experimental_method":"X-ray","resolution":"2.3"}]},{"uniquename":"PMID:19050035","title":"Gene expression trends and protein features effectively complement each other in gene function prediction.","citation":"Bioinformatics 2009 Feb 01;25(3):322-30","abstract":"Genome-scale 'omics' data constitute a potentially rich source of information about biological systems and their function. There is a plethora of tools and methods available to mine omics data. However, the diversity and complexity of different omics data types is a stumbling block for multi-data integration, hence there is a dire need for additional methods to exploit potential synergy from integrated orthogonal data. Rough Sets provide an efficient means to use complex information in classification approaches. Here, we set out to explore the possibilities of Rough Sets to incorporate diverse information sources in a functional classification of unknown genes.\nWe explored the use of Rough Sets for a novel data integration strategy where gene expression data, protein features and Gene Ontology (GO) annotations were combined to describe general and biologically relevant patterns represented by If-Then rules. The descriptive rules were used to predict the function of unknown genes in Arabidopsis thaliana and Schizosaccharomyces pombe. The If-Then rule models showed success rates of up to 0.89 (discriminative and predictive power for both modeled organisms); whereas, models built solely of one data type (protein features or gene expression data) yielded success rates varying from 0.68 to 0.78. Our models were applied to generate classifications for many unknown genes, of which a sizeable number were confirmed either by PubMed literature reports or electronically interfered annotations. Finally, we studied cell cycle protein-protein interactions derived from both tandem affinity purification experiments and in silico experiments in the BioGRID interactome database and found strong experimental evidence for the predictions generated by our models. The results show that our approach can be used to build very robust models that create synergy from integrating gene expression data and protein features.\nThe Rough Set-based method is implemented in the Rosetta toolkit kernel version 1.0.1 available at: http://rosetta.lcb.uu.se/","doi":"10.1093/bioinformatics/btn625","authors":"Wabnik K, Hvidsten TR, Kedzierska A, Van Leene J, De Jaeger G, Beemster GT, Komorowski J, Kuiper MT","authors_abbrev":"Wabnik K et al.","pubmed_publication_date":"01 Feb 2009","pubmed_entrez_date":"2008-12-04","publication_year":"2009","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32610611","title":"CDK Regulation of Meiosis: Lessons from  S. cerevisiae  and  S. pombe .","citation":"Genes (Basel) 2020 Jun 29;11(7)","abstract":"Meiotic progression requires precise orchestration, such that one round of DNA replication is followed by two meiotic divisions. The order and timing of meiotic events is controlled through the modulation of the phosphorylation state of proteins. Key components of this phospho-regulatory system include cyclin-dependent kinase (CDK) and its cyclin regulatory subunits. Over the past two decades, studies in budding and fission yeast have greatly informed our understanding of the role of CDK in meiotic regulation. In this review, we provide an overview of how CDK controls meiotic events in both budding and fission yeast. We discuss mechanisms of CDK regulation through post-translational modifications and changes in the levels of cyclins. Finally, we highlight the similarities and differences in CDK regulation between the two yeast species. Since CDK and many meiotic regulators are highly conserved, the findings in budding and fission yeasts have revealed conserved mechanisms of meiotic regulation among eukaryotes.","doi":"10.3390/genes11070723","authors":"MacKenzie AM, Lacefield S","authors_abbrev":"MacKenzie AM et al.","pubmed_publication_date":"29 Jun 2020","pubmed_entrez_date":"2020-07-03","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-07-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14625676","title":"Composition and conservation of the telomeric complex.","citation":"Cell Mol Life Sci 2003 Nov;60(11):2295-302","abstract":"The telomere is composed of telomeric DNA and telomere-associated proteins. Recently, many telomere-associated proteins have been identified, and various telomere functions have been uncovered. In budding yeast, scRap1 binds directly to telomeric DNA, and other telomere regulators (Sir proteins and Rif proteins) are recruited to the telomeres by interacting with scRap1. Cdc13 binds to the most distal end of the chromosome and recruits telomerase to the telomeres. In fission yeast and humans, TTAGGG repeat binding factor (TRF) family proteins bind directly to telomeric DNA, and Rap1 proteins and other telomere regulators are recruited to the telomeres by interacting with the TRF family proteins. Both organisms have Pot1 proteins at the most distal end of the telomere instead of a budding-yeast Cdc13-like protein. Therefore, fission yeast and humans have in part common telomeric compositions that differ from that of budding yeast, a result that suggests budding yeast has lost some telomere components during the course of evolution.","authors":"Kanoh J, Ishikawa F","authors_abbrev":"Kanoh J et al.","pubmed_publication_date":"Nov 2003","pubmed_entrez_date":"2003-11-20","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33544225","title":"The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S] 2+  cluster in vivo.","citation":"J Biol Inorg Chem 2021 Feb;26(1):93-108","abstract":"The Schizosaccharomyces pombe Asp1 protein is a bifunctional kinase/pyrophosphatase that belongs to the highly conserved eukaryotic diphosphoinositol pentakisphosphate kinase PPIP5K/Vip1 family. The N-terminal Asp1 kinase domain generates specific high-energy inositol pyrophosphate (IPP) molecules, which are hydrolyzed by the C-terminal Asp1 pyrophosphatase domain (Asp1 365-920 ). Thus, Asp1 activities regulate the intracellular level of a specific class of IPP molecules, which control a wide number of biological processes ranging from cell morphogenesis to chromosome transmission. Recently, it was shown that chemical reconstitution of Asp1 371-920  leads to the formation of a [2Fe-2S] cluster; however, the biological relevance of the cofactor remained under debate. In this study, we provide evidence for the presence of the Fe-S cluster in Asp1 365-920  inside the cell. However, we show that the Fe-S cluster does not influence Asp1 pyrophosphatase activity in vitro or in vivo. Characterization of the as-isolated protein by electronic absorption spectroscopy, mass spectrometry, and X-ray absorption spectroscopy is consistent with the presence of a [2Fe-2S] 2+  cluster in the enzyme. Furthermore, we have identified the cysteine ligands of the cluster. Overall, our work reveals that Asp1 contains an Fe-S cluster in vivo that is not involved in its pyrophosphatase activity.","doi":"10.1007/s00775-020-01840-w","authors":"Rosenbach H, Walla E, Cutsail GE, Birrell JA, Pascual-Ortiz M, DeBeer S, Fleig U, Span I","authors_abbrev":"Rosenbach H et al.","pubmed_publication_date":"Feb 2021","pubmed_entrez_date":"2021-02-05","publication_year":"2021","canto_session_key":"44fe6006b86661fb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-02-07 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7760826","title":"A novel mechanism of self-primed reverse transcription defines a new family of retroelements.","citation":"Mol Cell Biol 1995 Jun;15(6):3310-7","abstract":"Retroviruses and long terminal repeat (LTR)-containing retrotransposons initiate reverse transcription by using a specific tRNA primer than anneals to the primer-binding site of the retroelement transcript. Sequences from a large number of retroviruses and LTR-containing retrotransposons had indicated that the role of tRNAs in priming reverse transcription is universal among these LTR-containing retroelements. Data presented here strongly support the surprising conclusion that Tf1, a highly active LTR-containing retrotransposon isolated from Schizosaccharomyces pombe, undergoes a novel self-priming process that requires hybridization between the primer-binding site and the first 11 bases of the Tf1 transcript. Single-base mutations in these regions block transposition and reverse transcription, while compensatory mutations that reestablish complementarily rescue both defects. In addition, the sequence of the minus-strand RNA primer of reverse transcription was consistent with its being derived from the 5' end of the Tf1 transcript. Evidence that this mechanism defines a new family of retroelements is presented.","authors":"Levin HL","authors_abbrev":"Levin HL","pubmed_publication_date":"Jun 1995","pubmed_entrez_date":"1995-06-01","publication_year":"1995","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10712506","title":"Mechanisms of sod2 gene amplification in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2000 Mar;11(3):873-86","abstract":"Gene amplification in eukaryotes plays an important role in drug resistance, tumorigenesis, and evolution. The Schizosaccharomyces pombe sod2 gene provides a useful model system to analyze this process. sod2 is near the telomere of chromosome I and encodes a plasma membrane Na(+)(Li(+))/H(+) antiporter. When sod2 is amplified, S. pombe survives otherwise lethal concentrations of LiCl, and >90% of the amplified sod2 genes are found in 180- and 225-kilobase (kb) linear amplicons. The sequence of the novel joint of the 180-kb amplicon indicates that it is formed by recombination between homologous regions near the telomeres of the long arm of chromosome I and the short arm of chromosome II. The 225-kb amplicon, isolated three times more frequently than the 180-kb amplicon, is a palindrome derived from a region near the telomere of chromosome I. The center of symmetry of this palindrome contains an inverted repeat consisting of two identical 134-base pair sequences separated by a 290-base pair spacer. LiCl-resistant mutants arise 200-600 times more frequently in strains deficient for topoisomerases or DNA ligase activity than in wild-type strains, but the mutant cells contain the same amplicons. These data suggest that amplicon formation may begin with DNA lesions such as breaks. In the case of the 225-kb amplicon, the breaks may lead to a hairpin structure, which is then replicated to form a double-stranded linear amplicon, or to a cruciform structure, which is then resolved to yield the same amplicon.","authors":"Albrecht EB, Hunyady AB, Stark GR, Patterson TE","authors_abbrev":"Albrecht EB et al.","pubmed_publication_date":"Mar 2000","pubmed_entrez_date":"2000-03-11","publication_year":"2000","canto_session_key":"f7a5828208a1fb1f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-08 10:53:00","canto_approved_date":"2019-11-08 10:53:00","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-08 10:52:55","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1703.14c","SPAC20G8.01","SPAC977.10","SPBC1A4.03c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2019-11-08"},{"uniquename":"PMID:9923668","title":"Cell cycle. Checkpoint on the nuclear frontier.","citation":"Nature 1999 Jan 14;397(6715):104-5","abstract":"","authors":"Pines J","authors_abbrev":"Pines J","pubmed_publication_date":"14 Jan 1999","pubmed_entrez_date":"1999-01-29","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31147914","title":"Analysis of the Chromosomal Localization of Yeast SMC Complexes by Chromatin Immunoprecipitation.","citation":"Methods Mol Biol 2019;2004:119-138","abstract":"A plethora of biological processes like gene transcription, DNA replication, DNA recombination, and chromosome segregation are mediated through protein-DNA interactions. A powerful method for investigating proteins within a native chromatin environment in the cell is chromatin immunoprecipitation (ChIP). Combined with the recent technological advancement in next generation sequencing, the ChIP assay can map the exact binding sites of a protein of interest across the entire genome. Here we describe a-step-by step protocol for ChIP followed by library preparation for ChIP-seq from yeast cells.","doi":"10.1007/978-1-4939-9520-2_10","authors":"Makrantoni V, Robertson D, Marston AL","authors_abbrev":"Makrantoni V et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-06-01","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-06-01 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC29A10.14"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPGNRP","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11029045","title":"A role for the START gene-specific transcription factor complex in the inactivation of cyclin B and Cut2 destruction.","citation":"Mol Biol Cell 2000 Oct;11(10):3411-24","abstract":"Hyperactivation of Cdc2 in fission yeast causes cells to undergo a lethal premature mitosis called mitotic catastrophe. This phenotype is observed in cdc2-3w wee1-50 cells at high temperature. Eleven of 17 mutants that suppress this phenotype define a single complementation group, mcs1. The mcs1-77 mutant also suppresses lethal inactivation of the Wee1 and Mik1 tyrosine kinases and thus delays mitosis independently of Cdc2 tyrosine phosphorylation. We have cloned mcs1 by isolating suppressors of the cell cycle arrest phenotype of mcs1-77 cdc25-22 cells and found that it encodes Res2, a component of the START gene-specific transcription factor complex MBF (also known as DSC-1). The mcs1-77 mutant bears a single point mutation in the DNA-binding domain of Res2 that causes glycine 68 to be replaced by a serine residue. Importantly, two substrates of the anaphase-promoting complex (APC), the major B-type cyclin, Cdc13, and the anaphase inhibitor, Cut2, are unstable in G2-phase mcs1-77 cells. Consistent with this, we observe abnormal sister chromatid separation in mcs1-77 cdc25-22 cells at the restrictive temperature. Mutation of either Cdc10 or Res1 also deregulates MBF-dependent transcription and causes a G2 delay. We find that this cell cycle delay is abolished in the absence of the APC regulator Ste9/Srw1 and that the periodic expression of Ste9/Srw1 is controlled by the MBF complex. These data suggest that in fission yeast the MBF complex plays a key role in the inactivation of cyclin B and Cut2 destruction by controlling the periodic production of APC regulators.","authors":"Tournier S, Millar JB","authors_abbrev":"Tournier S et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-10-12","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2F12.11c","SPBC336.12c","SPBC660.14","SPCC18B5.03","SPAC22F3.09c","SPBC11B10.09","SPBC725.16","SPAC24H6.05"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:2292520","title":"Growth inhibitory and biocidal activity of some isothiazolone biocides.","citation":"J Appl Bacteriol 1990 Oct;69(4):569-77","abstract":"Similar patterns of growth inhibition were observed for the three biocides, benzisothiazol-3-one (BIT), 5-chloro-N-methylisothiazol-3-one (CMIT) and N-methylisothiazol-3-one (MIT) against Escherichia coli ATCC 8739 and Schizosaccharomyces pombe NCYC 1354. After periods of induced stasis, proportional to biocide concentration, growth proceeded at an inhibited rate. Extrapolation of the static periods and inhibited growth rates against biocide concentration gave minimum growth inhibitory concentration estimates of 0.1-0.5 micrograms/ml for CMIT, 15-20 micrograms/ml for BIT and 40-250 micrograms/ml for MIT. Patterns of growth inhibition by CMIT and induced morphological changes in inhibited cultures suggested this compound to also inhibit initiation of DNA replication. Growth inhibitory activity was rapidly quenched by the addition of thiol-containing materials such as glutathione and cysteine. The activity of CMIT was additionally quenched by the presence of the non-thiol amino acids valine and/or histidine. These results suggest that the chlorinated isothiazolones can react with amines as well as with essential thiol groups.","authors":"Collier PJ, Ramsey AJ, Austin P, Gilbert P","authors_abbrev":"Collier PJ et al.","pubmed_publication_date":"Oct 1990","pubmed_entrez_date":"1990-10-01","publication_year":"1990","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10749922","title":"Multistep phosphorelay proteins transmit oxidative stress signals to the fission yeast stress-activated protein kinase.","citation":"Mol Biol Cell 2000 Apr;11(4):1169-81","abstract":"In response to oxidative stress, eukaryotic cells induce transcription of genes required for detoxification of oxidants. Here we present evidence that oxidative stress stimuli are transmitted by a multistep phosphorelay system to the Spc1/Sty1 stress-activated protein kinase in the fission yeast Schizosaccharomyces pombe. The fission yeast mpr1(+) gene encodes a novel protein with a histidine-containing phosphotransfer domain homologous to the budding yeast Ypd1. Spc1 activation upon oxidative stress is severely impaired in the Deltampr1 mutant as well as in the mpr1HQ strain, in which the putative phosphorylation site Mpr1-His221 is substituted with glutamine. In response to oxidative stress, Mpr1 binds to the Mcs4 response regulator that functions upstream of the Spc1 cascade, suggesting that Mcs4 is a cognate response regulator for Mpr1. Unexpectedly, when exposed to hydrogen peroxide, Deltampr1 cells can induce the catalase gene ctt1(+), one of the transcriptional targets of the Spc1 pathway, and survive oxidative stress in the absence of significant Spc1 activation. We have found that Pap1, a bZIP transcription factor homologous to human c-Jun, can mediate induction of ctt1(+) expression upon oxidative stress independently of the Spc1 stress-activated protein kinase. These studies show that oxidative stress stimuli are transmitted by multiple pathways to induce specific gene expression.","authors":"Nguyen AN, Lee A, Place W, Shiozaki K","authors_abbrev":"Nguyen AN et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-04-06","publication_year":"2000","canto_session_key":"ed04f04bf6b4ebbc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-27 15:50:28","canto_approved_date":"2023-05-16 07:56:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-03 16:54:06","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC725.02","SPAC8C9.14","SPBC409.07c","SPBC29B5.01","SPBC887.10","SPCC757.07c","SPAC24B11.06c","SPAC1783.07c"],"gene_count":8,"ltp_gene_count":7,"approved_date":"2017-09-27"},{"uniquename":"PMID:4148397","title":"Presence of glutamate synthase in fission yeasts and its possible role in ammonia assimilation.","citation":"Nat New Biol 1973 Nov 28;246(152):115-6","abstract":"","authors":"Brown CM, Burn VJ, Johnson B","authors_abbrev":"Brown CM et al.","pubmed_publication_date":"28 Nov 1973","pubmed_entrez_date":"1973-11-28","publication_year":"1973","canto_session_key":"e7c9063b1d75df32","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-08-16 15:00:53","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2017-08-16 15:00:39","canto_added_date":"2016-09-04 13:34:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1E7.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-08-16"},{"uniquename":"PMID:36699351","title":"MUNDO: protein function prediction embedded in a multispecies world.","citation":"Bioinform Adv 2022;2(1):vbab025","abstract":"Leveraging cross-species information in protein function prediction can add significant power to network-based protein function prediction methods, because so much functional information is conserved across at least close scales of evolution. We introduce MUNDO, a new cross-species co-embedding method that combines a single-network embedding method with a co-embedding method to predict functional annotations in a target species, leveraging also functional annotations in a model species network.\nAcross a wide range of parameter choices, MUNDO performs best at predicting annotations in the mouse network, when trained on mouse and human protein-protein interaction (PPI) networks, in the human network, when trained on human and mouse PPIs, and in Baker's yeast, when trained on Fission and Baker's yeast, as compared to competitor methods. MUNDO also outperforms all the cross-species methods when predicting in Fission yeast when trained on Fission and Baker's yeast; however, in this single case, discarding the information from the other species and using annotations from the Fission yeast network alone usually performs best.\nAll code is available and can be accessed here: github.com/v0rtex20k/MUNDO.","doi":"10.1093/bioadv/vbab025","authors":"Arsenescu V, Devkota K, Erden M, Shpilker P, Werenski M, Cowen LJ","authors_abbrev":"Arsenescu V et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2023-01-26","publication_year":"2022","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2023-01-27 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29473861","title":"Nutrient Limitation Inactivates Mrc1-to-Cds1 Checkpoint Signalling in Schizosaccharomyces pombe.","citation":"Cells 2018 Feb 23;7(2)","abstract":"The  S. pombe  checkpoint kinase, Cds1, protects the integrity of stalled DNA replication forks after its phosphorylation at threonine-11 by Rad3 (ATR). Modified Cds1 associates through its N-terminal forkhead-associated domain (FHA)-domain with Mrc1 (Claspin) at stalled forks. We report here that nutrient starvation results in post-translational changes to Cds1 and the loss of Mrc1. A drop in glucose after a down-shift from 3% to 0.1-0.3%, or when cells enter the stationary phase, triggers a sharp decline in Mrc1 and the accumulation of insoluble Cds1. Before this transition, Cds1 is transiently activated and phosphorylated by Rad3 when glucose levels fall. Because this coincides with the phosphorylation of histone 2AX at S129 by Rad3, an event that occurs towards the end of every unperturbed S phase, we suggest that a glucose limitation promotes the exit from the S phase. Since nitrogen starvation also depletes Mrc1 while Cds1 is post-translationally modified, we suggest that nutrient limitation is the general signal that promotes exit from S phase before it inactivates the Mrc1-Cds1 signalling component. Why Cds1 accumulates in resting cells while its activator Mrc1 declines is, as yet, unclear but suggests a novel function of Cds1 in non-replicating cells.","doi":"10.3390/cells7020015","authors":"Fletcher J, Griffiths L, Caspari T","authors_abbrev":"Fletcher J et al.","pubmed_publication_date":"23 Feb 2018","pubmed_entrez_date":"2018-02-24","publication_year":"2018","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-02-28 22:13:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25165823","title":"Multiple regulation of Rad51-mediated homologous recombination by fission yeast Fbh1.","citation":"PLoS Genet 2014 Aug;10(8):e1004542","abstract":"Fbh1, an F-box helicase related to bacterial UvrD, has been proposed to modulate homologous recombination in fission yeast. We provide several lines of evidence for such modulation. Fbh1, but not the related helicases Srs2 and Rqh1, suppressed the formation of crossover recombinants from single HO-induced DNA double-strand breaks. Purified Fbh1 in complex with Skp1 (Fbh1-Skp1 complex) inhibited Rad51-driven DNA strand exchange by disrupting Rad51 nucleoprotein filaments in an ATP-dependent manner; this disruption was alleviated by the Swi5-Sfr1 complex, an auxiliary activator of Rad51. In addition, the reconstituted SCFFbh1 complex, composed of purified Fbh1-Skp1 and Pcu1-Rbx1, displayed ubiquitin-ligase E3 activity toward Rad51. Furthermore, Fbh1 reduced the protein level of Rad51 in stationary phase in an F-box-dependent, but not in a helicase domain-independent manner. These results suggest that Fbh1 negatively regulates Rad51-mediated homologous recombination via its two putative, unrelated activities, namely DNA unwinding/translocation and ubiquitin ligation. In addition to its anti-recombinase activity, we tentatively suggest that Fbh1 might also have a pro-recombination role in vivo, because the Fbh1-Skp1 complex stimulated Rad51-mediated strand exchange in vitro after strand exchange had been initiated.","doi":"10.1371/journal.pgen.1004542","authors":"Tsutsui Y, Kurokawa Y, Ito K, Siddique MS, Kawano Y, Yamao F, Iwasaki H","authors_abbrev":"Tsutsui Y et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-08-29","publication_year":"2014","canto_session_key":"8c596f264411204a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Tsutsui","canto_first_approved_date":"2016-09-03 12:05:22","canto_approved_date":"2024-04-23 11:59:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-12 10:20:05","canto_added_date":"2014-08-30 00:15:24","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":37,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Yasuhiro Tsutsui","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.21c","SPBC1105.09","SPAC2G11.12","SPBC409.05","SPBC409.03","SPAC23H4.18c","SPAC644.14c","SPBC28F2.07","SPBC119.02","SPAC4H3.05","SPBC336.01","SPAC17G6.12","SPAC20H4.07"],"gene_count":13,"ltp_gene_count":13,"approved_date":"2016-09-03"},{"uniquename":"PMID:26354422","title":"Ccq1-Tpz1TPP1 interaction facilitates telomerase and SHREC association with telomeres in fission yeast.","citation":"Mol Biol Cell 2015 Nov 01;26(21):3857-66","abstract":"Evolutionarily conserved shelterin complex is essential for telomere maintenance in the fission yeast Schizosaccharomyces pombe. Elimination of the fission yeast shelterin subunit Ccq1 causes progressive loss of telomeres due to the inability to recruit telomerase, activates the DNA damage checkpoint, and loses heterochromatin at telomere/subtelomere regions due to reduced recruitment of the heterochromatin regulator complex Snf2/histone deacetylase-containing repressor complex (SHREC). The shelterin subunit Tpz1(TPP1) directly interacts with Ccq1 through conserved C-terminal residues in Tpz1(TPP1), and tpz1 mutants that fail to interact with Ccq1 show telomere shortening, checkpoint activation, and loss of heterochromatin. While we have previously concluded that Ccq1-Tpz1(TPP1) interaction contributes to Ccq1 accumulation and telomerase recruitment based on analysis of tpz1 mutants that fail to interact with Ccq1, another study reported that loss of Ccq1-Tpz1(TPP1) interaction does not affect accumulation of Ccq1 or telomerase. Furthermore, it remained unclear whether loss of Ccq1-Tpz1(TPP1) interaction affects SHREC accumulation at telomeres. To resolve these issues, we identified and characterized a series of ccq1 mutations that disrupt Ccq1-Tpz1(TPP1) interaction. Characterization of these ccq1 mutants established that Ccq1-Tpz1(TPP1) interaction contributes to optimal binding of the Ccq1-SHREC complex, and is critical for Rad3(ATR)/Tel1(ATM)-dependent Ccq1 Thr93 phosphorylation and telomerase recruitment.","doi":"10.1091/mbc.E15-07-0481","authors":"Moser BA, Raguimova ON, Nakamura TM","authors_abbrev":"Moser BA et al.","pubmed_publication_date":"01 Nov 2015","pubmed_entrez_date":"2015-09-11","publication_year":"2015","canto_session_key":"256d20aa6cc284d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-09-13 00:18:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC188.07","SPAC6F6.16c","SPAC19G12.13c","SPBC800.03"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:9774332","title":"A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase.","citation":"EMBO J 1998 Oct 15;17(20):5877-86","abstract":"A key element in the quality control of glycoprotein folding is the UDP-Glc:glycoprotein glucosyltransferase (GT), which in cell-free assays exclusively glucosylates misfolded glycoproteins. In order to test if such a protein conformation is a sufficient condition for in vivo glucosylation of all N-linked oligosaccharides by GT, a Schizosaccharomyces pombe double mutant (gls2/alg6) was constructed. With this mutant, Man9GlcNAc2 is transferred to proteins and no removal of glucose units added by GT occurs as it lacks glucosidase II. The same proportion of glucosylated (Glc1Man9GlcNAc2) and unglucosylated (Man9GlcNAc2 and Man8GlcNAc2) endoplasmic reticulum (ER)-specific compounds was produced when cells were pre-incubated for 10, 20 or 30 min and further incubated with [14C]glucose for 10 min at 28 degrees C with or without 5 mM dithiothreitol (DTT), thus indicating not only that DTT did not affect protein glucosylation but also that no increased glucosylation of glycoproteins occurred in the presence of the drug. Monitoring Golgi-specific modifications of oligosaccharides after pulse-chase experiments performed in the presence or absence of 5 mM DTT showed that exit of the bulk of glycoproteins synthesized from the ER and thence their proper folding had been prevented by the drug. Cells pulse-chase labeled at 37 degrees C in the absence of DTT also yielded glucosylated and unglucosylated protein-linked oligosaccharides without Golgi-specific modifications. It was concluded that a misfolded protein conformation is not a sufficient condition for in vivo glucosylation of all N-linked oligosaccharides by GT.","authors":"Fernández F, D'Alessio C, Fanchiotti S, Parodi AJ","authors_abbrev":"Fernández F et al.","pubmed_publication_date":"15 Oct 1998","pubmed_entrez_date":"1998-10-17","publication_year":"1998","canto_session_key":"c053a2d58993a5bb","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2087776","title":"Sexual differentiation in fission yeast.","citation":"Trends Genet 1990 Nov;6(11):369-73","abstract":"The regulation of sexual reproduction in yeast constitutes the highest level of differentiation observed in these unicellular organisms. The various ramifications of this system involve DNA rearrangement, transcriptional control, post-translational modification (such as protein phosphorylation) and receptor/signal processing. A few basic similarities are common to both fission and budding yeasts. The wiring of the regulatory circuitry, however, varies considerably between these divergent yeast groups.","authors":"Egel R, Nielsen O, Weilguny D","authors_abbrev":"Egel R et al.","pubmed_publication_date":"Nov 1990","pubmed_entrez_date":"1990-11-01","publication_year":"1990","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007542","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35586315","title":"Quantitative analysis of protein-RNA interactions in fission yeast.","citation":"STAR Protoc 2022 Jun 17;3(2):101373","abstract":"Characterizing the interactions between RNAs and proteins  in vivo  is key to better understand how organisms regulate gene expression. Here, we describe a robust and quantitative protocol to measure specific RNA-protein interactions in a native context using RNA immunoprecipitation (RIP). We provide a comprehensive experimental framework to detect cotranslational interactions and detail the quantitative analysis of purified RNAs by PCR and high-throughput sequencing. Although we developed the protocol in fission yeast, it can be readily implemented in other yeast species. For complete details on the use and execution of this protocol, please refer to Toullec et al. (2021).","doi":"10.1016/j.xpro.2022.101373","authors":"Elías-Villalobos A, Duncan C, Mata J, Helmlinger D","authors_abbrev":"Elías-Villalobos A et al.","pubmed_publication_date":"17 Jun 2022","pubmed_entrez_date":"2022-05-19","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-05-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24591591","title":"Individual letters of the RNA polymerase II CTD code govern distinct gene expression programs in fission yeast.","citation":"Proc Natl Acad Sci U S A 2014 Mar 18;111(11):4185-90","abstract":"The primary structure and phosphorylation pattern of the tandem Y(1)S(2)P(3)T(4)S(5)P(6)S(7) repeats of the RNA polymerase II carboxyl-terminal domain (CTD) comprise an informational code that coordinates transcription, chromatin modification, and RNA processing. To gauge the contributions of individual CTD coding \"letters\" to gene expression, we analyzed the poly(A)(+) transcriptomes of fission yeast mutants that lack each of the four inessential CTD phosphoacceptors: Tyr1, Ser2, Thr4, and Ser7. There was a hierarchy of CTD mutational effects with respect to the number of dysregulated protein-coding RNAs, with S2A (n = 227) >> Y1F (n = 71) > S7A (n = 58) >> T4A (n = 7). The majority of the protein-coding RNAs affected in Y1F cells were coordinately affected by S2A, suggesting that Tyr1-Ser2 constitutes a two-letter code \"word.\" Y1F and S2A elicited increased expression of genes encoding proteins involved in iron uptake (Frp1, Fip1, Fio1, Str3, Str1, Sib1), without affecting the expression of the genes that repress the iron regulon, implying that Tyr1-Ser2 transduces a repressive signal. Y1F and S2A cells had increased levels of ferric reductase activity and were hypersensitive to phleomycin, indicative of elevated intracellular iron. The T4A and S7A mutations had opposing effects on the phosphate response pathway. T4A reduced the expression of two genes encoding proteins involved in phosphate acquisition (the Pho1 acid phosphatase and the phosphate transporter SPBC8E4.01c), without affecting the expression of known genes that regulate the phosphate response pathway, whereas S7A increased pho1(+) expression. These results highlight specific cellular gene expression programs that are responsive to distinct CTD cues.","doi":"10.1073/pnas.1321842111","authors":"Schwer B, Bitton DA, Sanchez AM, Bähler J, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"18 Mar 2014","pubmed_entrez_date":"2014-03-05","publication_year":"2014","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-03-05 12:03:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11095681","title":"Fission yeast retrotransposon Tf1 integration is targeted to 5' ends of open reading frames.","citation":"Nucleic Acids Res 2000 Dec 01;28(23):4709-16","abstract":"Target site selection of transposable elements is usually not random but involves some specificity for a DNA sequence or a DNA binding host factor. We have investigated the target site selection of the long terminal repeat-containing retrotransposon Tf1 from the fission yeast Schizosaccharomyces pombe. By monitoring induced transposition events we found that Tf1 integration sites were distributed throughout the genome. Mapping these insertions revealed that Tf1 did not integrate into open reading frames, but occurred preferentially in longer intergenic regions with integration biased towards a region 100-420 bp upstream of the translation start site. Northern blot analysis showed that transcription of genes adjacent to Tf1 insertions was not significantly changed.","authors":"Behrens R, Hayles J, Nurse P","authors_abbrev":"Behrens R et al.","pubmed_publication_date":"01 Dec 2000","pubmed_entrez_date":"2000-11-30","publication_year":"2000","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16303848","title":"A role for the fission yeast Rqh1 helicase in chromosome segregation.","citation":"J Cell Sci 2005 Dec 15;118(Pt 24):5777-84","abstract":"Schizosaccharomyces pombe Rqh1 protein is a member of the RecQ DNA helicase family. Members of this protein family are mutated in several human genome instability syndromes, including Bloom, Werner and Rothmund-Thomson syndromes. RecQ helicases participate in recombination repair of stalled replication forks or DNA breaks, but the precise mechanisms that lead to the development of cancer in these diseases have remained obscure. Here, we reveal a function for Rqh1 in chromosome segregation even in the absence of exogenous insult to the DNA. We show that cells lacking Rqh1 are delayed in anaphase progression, and show lagging chromosomal DNA, which is particularly apparent in the rDNA locus. This mitotic delay is dependent on the spindle checkpoint, as deletion of mad2 abolishes the delay as well as the accumulation of Cut2 in rqh1delta cells. Furthermore, relieving replication fork arrest in the rDNA repeat by deletion of reb1+ partially suppresses rqh1delta phenotypes. These data are consistent with the function of the Top3-RecQ complex in maintenance of the rDNA structure by processing aberrant chromosome structures arising from DNA replication. The chromosome segregation defects seen in the absence of functional RecQ helicases may contribute to the pathogenesis of human RecQ helicase disorders.","authors":"Win TZ, Mankouri HW, Hickson ID, Wang SW","authors_abbrev":"Win TZ et al.","pubmed_publication_date":"15 Dec 2005","pubmed_entrez_date":"2005-11-24","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC20F10.06","SPBC1198.11c","SPAC2G11.12"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:19627505","title":"The tetraspan protein Dni1p is required for correct membrane organization and cell wall remodelling during mating in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2009 Aug;73(4):695-709","abstract":"In fungi, success of mating requires that both cells agglutinate, modify their extracellular envelopes, and fuse their plasma membranes and nuclei to produce a zygote. Here we studied the role of the Schizosaccharomyces pombe Dni1 protein in the cell fusion step of mating. Dni1p is a tetraspan protein bearing a conserved cystein motif similar to that present in fungal claudin-related proteins. Dni1p expression is induced during mating and Dni1p concentrates as discrete patches at the cell-cell contact area and along the mating bridge. Proper Dni1p localization depends on Fus1p, actin and integrity of lipid rafts. In dni1Delta mutants, cell differentiation and agglutination are as efficient as in the wild-type strain, but cell fusion is significantly reduced at temperatures above 25 degrees C. We found that the defect in cell fusion was not associated with an altered cytoskeleton, with an abnormal distribution of Fus1p, or with a defect in calcium accumulation, but with a severe disorganization of the plasma membrane and cell wall at the area of cell-cell contact. These results show that Dni1p plays a relevant role in co-ordinating membrane organization and cell wall remodelling during mating, a function that has not been described for other proteins in the fission yeast.","doi":"10.1111/j.1365-2958.2009.06800.x","authors":"Clemente-Ramos JA, Martín-García R, Sharifmoghadam MR, Konomi M, Osumi M, Valdivieso MH","authors_abbrev":"Clemente-Ramos JA et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-07-25","publication_year":"2009","canto_session_key":"19cb5710ede28157","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-02-13 11:36:33","canto_approved_date":"2026-02-26 14:25:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-19 20:47:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.12","SPAC20G4.02c","SPAC31G5.07","SPAC27F1.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-02-13"},{"uniquename":"PMID:32441227","title":"Glucose limitation and  pka1  deletion rescue aberrant mitotic spindle formation induced by Mal3 overexpression in  Schizosaccharomyces pombe .","citation":"Biosci Biotechnol Biochem 2020 Aug;84(8):1667-1680","abstract":"The cAMP-dependent protein kinase Pka1 is known as a regulator of glycogenesis, transition into meiosis, proper chromosome segregation, and stress responses in  Schizosaccharomyces pombe . We demonstrated that both the cAMP/PKA pathway and glucose limitation play roles in appropriate spindle formation. Overexpression of Mal3 (1-308), an EB1 family protein, caused growth defects, increased 4C DNA content, and induced monopolar spindle formation. Overproduction of a high-affinity microtubule binding mutant (Q89R) and a recombinant protein possessing the CH and EB1 domains (1-241) both resulted in more severe phenotypes than Mal3 (1-308). Loss of functional Pka1 and glucose limitation rescued the phenotypes of Mal3-overexpressing cells, whereas deletion of Tor1 or Ssp2 did not. Growth defects and monopolar spindle formation in a kinesin-5 mutant,  cut7-446 , was partially rescued by  pka1  deletion or glucose limitation. These findings suggest that Pka1 and glucose limitation regulate proper spindle formation in Mal3-overexpressing cells and the  cut7-446  mutant.","doi":"10.1080/09168451.2020.1763157","authors":"Tanabe T, Kawamukai M, Matsuo Y","authors_abbrev":"Tanabe T et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-05-23","publication_year":"2020","canto_session_key":"8bbf0b2fcfdbcf46","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Matsuo","canto_first_approved_date":"2020-06-12 12:27:02","canto_approved_date":"2026-05-13 14:42:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-05 04:50:02","canto_added_date":"2020-05-24 00:15:05","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Yasuhiro Matsuo","community_curator":true,"annotation_count":51,"orcid":"0000-0002-2858-7179","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.10c","SPBC106.10","SPAC18G6.15","SPAC8C9.03","SPCC74.03c","SPBC19C7.03","SPAC25G10.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2020-06-12"},{"uniquename":"PMID:18328827","title":"Programmed cell death in fission yeast Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2008 Jul;1783(7):1335-49","abstract":"Yeasts have proven to be invaluable, genetically tractable systems to study various fundamental biological processes including programmed cell death. Recent advances in the elucidation of the molecular pathways underlying apoptotic cell death in yeasts have revealed remarkable similarities to mammalian apoptosis at cellular, organelle and macromolecular levels, thus making a strong case for the relevance of yeast models of regulated cell death. Programmed cell death has been reported in fission yeast Schizosaccharomyces pombe, primarily in the contexts of perturbed intracellular lipid metabolism, defective DNA replication, improper mitotic entry, chronological and replicative aging. Here we review the current understanding of the programmed cell death in fission yeast, paying particular attention to lipid-induced cell death. We discuss our recent findings that fission yeast exhibits plasticity of apoptotic and non-apoptotic modes of cell death in response to different lipid stimuli and growth conditions, and that mitochondria, reactive oxygen species and novel cell death mediators including metacaspase Pca1, SpRad9 and Pck1 are involved in the lipotoxic cell death. We also present perspectives on how various aspects of the cell and molecular biology of this organism can be explored to shed light on the governing principles underlying lipid-mediated signaling and cell demise.","doi":"10.1016/j.bbamcr.2008.02.002","authors":"Low CP, Yang H","authors_abbrev":"Low CP et al.","pubmed_publication_date":"Jul 2008","pubmed_entrez_date":"2008-03-11","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32612670","title":"Caffeine as a tool for investigating the integration of Cdc25 phosphorylation, activity and ubiquitin-dependent degradation in  Schizosaccharomyces pombe .","citation":"Cell Div 2020;15:10","abstract":"The evolutionarily conserved Cdc25 phosphatase is an essential protein that removes inhibitory phosphorylation moieties on the mitotic regulator Cdc2. Together with the Wee1 kinase, a negative regulator of Cdc2 activity, Cdc25 is thus a central regulator of cell cycle progression in  Schizosaccharomyces pombe . The expression and activity of Cdc25 is dependent on the activity of the Target of Rapamycin Complex 1 (TORC1). TORC1 inhibition leads to the activation of Cdc25 and repression of Wee1, leading to advanced entry into mitosis. Withdrawal of nitrogen leads to rapid Cdc25 degradation via the ubiquitin- dependent degradation pathway by the Pub1 E3- ligase. Caffeine is believed to mediate the override of DNA damage checkpoint signalling, by inhibiting the activity of the ataxia telangiectasia mutated (ATM)/Rad3 homologues. This model remains controversial, as TORC1 appears to be the preferred target of caffeine in vivo. Recent studies suggest that caffeine induces DNA damage checkpoint override by inducing the nuclear accumulation of Cdc25 in  S. pombe . Caffeine may thus modulate Cdc25 activity and stability via inhibition of TORC1. A clearer understanding of the mechanisms by which caffeine stabilises Cdc25, may provide novel insights into how TORC1 and DNA damage signalling is integrated.","doi":"10.1186/s13008-020-00066-1","authors":"Alao JP, Sunnerhagen P","authors_abbrev":"Alao JP et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-07-03","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-07-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPD267","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2858389","title":"Essential arginyl residues in the H+-translocating ATPase of plasma membrane from the yeast Schizosaccharomyces pombe.","citation":"Eur J Biochem 1985 Apr 01;148(1):35-9","abstract":"The H+-translocating adenosine-5'-triphosphatase (ATPase) purified from the yeast Schizosaccharomyces pombe is inactivated upon incubation with the arginine modifier 2,3-butanedione. The inactivation of the enzyme is maximal at pH values above 8.5. The modified enzyme is reactivated when incubated in the absence of borate after removal of 2,3-butanedione. The extent of inactivation is half maximal at 10 mM 2,3-butanedione for an incubation of 30 min at 30 degrees C at pH 7.0. Under the same conditions, the time-dependence of inactivation is biphasic in a semi-logarithmic plot with half-lives of 10.9 min and 65.9 min. Incubation with 2,3-butanedione lowering markedly the maximal rate of ATPase activity does not modify the Km for MgATP. These data suggest that two classes of arginyl residues play essential role in the plasma membrane ATPase activity. Magnesium adenosine 5'-triphosphate (MgATP) and magnesium adenosine 5'-diphosphate (MgADP), the specific substrate and product, protect partially against enzyme inactivation by 2,3-butanedione. Free ATP or MgGTP which are not enzyme substrates do not protect. Free magnesium, another effector of enzyme activity, exhibits partial protection at magnesium concentrations up to 0.5 mM, while increased inactivation is observed at higher Mg2+ concentrations. These protections indicate either the existence of at least one reactive arginyl in the substrate binding site or a general change of enzyme conformation induced by MgATP, MgADP or free magnesium.","authors":"Di Pietro A, Goffeau A","authors_abbrev":"Di Pietro A et al.","pubmed_publication_date":"01 Apr 1985","pubmed_entrez_date":"1985-04-01","publication_year":"1985","canto_session_key":"3d42172a07d9c16d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-03-21 13:00:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 20:11:35","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-02-08"},{"uniquename":"PMID:15347659","title":"DNA replication checkpoint control mediated by the spindle checkpoint protein Mad2p in fission yeast.","citation":"J Biol Chem 2004 Nov 05;279(45):47372-8","abstract":"The relationship between the DNA replication and spindle checkpoints of the cell cycle is unclear, given that in most eukaryotes, spindle formation occurs only after DNA replication is complete. Fission yeast rad3 mutant cells, which are deficient in DNA replication checkpoint function, enter, progress through, and exit mitosis even when DNA replication is blocked. In contrast, the entry of cds1 mutant cells into mitosis is delayed by several hours when DNA replication is inhibited. We show here that this delay in mitotic entry in cds1 cells is due in part to activation of the spindle checkpoint protein Mad2p. In the presence of the DNA replication inhibitor hydroxyurea (HU), cds1 mad2 cells entered and progressed through mitosis earlier than did cds1 cells. Overexpression of Mad2p or inactivation of Slp1p, a regulator of the anaphase-promoting complex, also rescued the checkpoint defect of HU-treated rad3 cells. Rad3p was shown to be involved in the physical interaction between Mad2p and Slp1p in the presence of HU. These results suggested that Mad2p and Slp1p act downstream of Rad3p in the DNA replication checkpoint and that Mad2p is required for the DNA replication checkpoint when Cds1p is compromised.","authors":"Sugimoto I, Murakami H, Tonami Y, Moriyama A, Nakanishi M","authors_abbrev":"Sugimoto I et al.","pubmed_publication_date":"05 Nov 2004","pubmed_entrez_date":"2004-09-07","publication_year":"2004","canto_session_key":"93ca4cadd1ff6a75","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-09-14 15:53:38","canto_approved_date":"2021-01-05 17:01:20","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-01-08 15:07:28","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":19,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPCC1322.12c","SPBC3D6.04c","SPBC20F10.06","SPCC1795.01c","SPAC821.08c","SPBC582.03","SPBC11B10.09","SPBC216.05"],"gene_count":9,"ltp_gene_count":4,"approved_date":"2018-09-14"},{"uniquename":"PMID:4371850","title":"Regulation of purine metabolism in Schizosaccharomyces pombe. IV. Variations in the stability and kinetic parameters of amidophosphoribosyltransferase depending on growth phase and growth conditions.","citation":"Biochim Biophys Acta 1974 Nov 25;370(1):85-95","abstract":"","authors":"Nagy M, Reichert U, Ribet AM","authors_abbrev":"Nagy M et al.","pubmed_publication_date":"25 Nov 1974","pubmed_entrez_date":"1974-11-25","publication_year":"1974","canto_session_key":"609d8d388d2619ff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-10-10 19:27:46","canto_approved_date":"2018-10-10 19:27:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-10 19:11:15","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4D7.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-10"},{"uniquename":"PMID:12522768","title":"Identification of PEX7 as the second gene involved in Refsum disease.","citation":"Am J Hum Genet 2003 Feb;72(2):471-7","abstract":"Patients affected with Refsum disease (RD) have elevated levels of phytanic acid due to a deficiency of the peroxisomal enzyme phytanoyl-CoA hydroxylase (PhyH). In most patients with RD, disease-causing mutations in the PHYH gene have been identified, but, in a subset, no mutations could be found, indicating that the condition is genetically heterogeneous. Linkage analysis of a few patients diagnosed with RD, but without mutations in PHYH, suggested a second locus on chromosome 6q22-24. This region includes the PEX7 gene, which codes for the peroxin 7 receptor protein required for peroxisomal import of proteins containing a peroxisomal targeting signal type 2. Mutations in PEX7 normally cause rhizomelic chondrodysplasia punctata type 1, a severe peroxisomal disorder. Biochemical analyses of the patients with RD revealed defects not only in phytanic acid alpha-oxidation but also in plasmalogen synthesis and peroxisomal thiolase. Furthermore, we identified mutations in the PEX7 gene. Our data show that mutations in the PEX7 gene may result in a broad clinical spectrum ranging from severe rhizomelic chondrodysplasia punctata to relatively mild RD and that clinical diagnosis of conditions involving retinitis pigmentosa, ataxia, and polyneuropathy may require a full screen of peroxisomal functions.","authors":"van den Brink DM, Brites P, Haasjes J, Wierzbicki AS, Mitchell J, Lambert-Hamill M, de Belleroche J, Jansen GA, Waterham HR, Wanders RJ","authors_abbrev":"van den Brink DM et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-01-11","publication_year":"2003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17D4.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:26944332","title":"DSS1/Sem1, a Multifunctional and Intrinsically Disordered Protein.","citation":"Trends Biochem Sci 2016 May;41(5):446-459","abstract":"DSS1/Sem1 is a versatile intrinsically disordered protein. Besides being a bona fide subunit of the 26S proteasome, DSS1 associates with other protein complexes, including BRCA2-RPA, involved in homologous recombination; the Csn12-Thp3 complex, involved in RNA splicing; the integrator, involved in transcription; and the TREX-2 complex, involved in nuclear export of mRNA and transcription elongation. As a subunit of the proteasome, DSS1 functions both in complex assembly and possibly as a ubiquitin receptor. Here, we summarise structural and functional aspects of DSS1/Sem1 with particular emphasis on its multifunctional and disordered properties. We suggest that DSS1/Sem1 can act as a polyanionic adhesive to prevent nonproductive interactions during construction of protein assemblies, uniquely employing different structures when associating with the diverse multisubunit complexes.","doi":"10.1016/j.tibs.2016.02.004","authors":"Kragelund BB, Schenstrøm SM, Rebula CA, Panse VG, Hartmann-Petersen R","authors_abbrev":"Kragelund BB et al.","pubmed_publication_date":"May 2016","pubmed_entrez_date":"2016-03-06","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:16687577","title":"Cell cycle-dependent roles for the FCH-domain protein Cdc15p in formation of the actomyosin ring in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2006 Jul;17(7):3254-66","abstract":"Cell division in the fission yeast Schizosaccharomyces pombe requires the formation and constriction of an actomyosin ring at the division site. The actomyosin ring is assembled in metaphase and anaphase A, is maintained throughout mitosis, and constricts after completion of anaphase. Maintenance of the actomyosin ring during late stages of mitosis depends on the septation initiation network (SIN), a signaling cascade that also regulates the deposition of the division septum. However, SIN is not active in metaphase and is not required for the initial assembly of the actomyosin ring early in mitosis. The FER/CIP4-homology (FCH) domain protein Cdc15p is a component of the actomyosin ring. Mutations in cdc15 lead to failure in cytokinesis and result in the formation of elongated, multinucleate cells without a division septum. Here we present evidence that the requirement of Cdc15p for actomyosin ring formation is dependent on the stage of mitosis. Although cdc15 mutants are competent to assemble actomyosin rings in metaphase, they are unable to maintain actomyosin rings late in mitosis when SIN is active. In the absence of functional Cdc15p, ring formation upon metaphase arrest depends on the anillin-like Mid1p. Interestingly, when cytokinesis is delayed due to perturbations to the division machinery, Cdc15p is maintained in a hypophosphorylated form. The dephosphorylation of Cdc15p, which occurs transiently in unperturbed cytokinesis, is partially dependent on the phosphatase Clp1p/Flp1p. This suggests a mechanism where both SIN and Clp1p/Flp1p contribute to maintenance of the actomyosin ring in late mitosis through Cdc15p, possibly by regulating its phosphorylation status.","authors":"Wachtler V, Huang Y, Karagiannis J, Balasubramanian MK","authors_abbrev":"Wachtler V et al.","pubmed_publication_date":"Jul 2006","pubmed_entrez_date":"2006-05-12","publication_year":"2006","canto_session_key":"1eaa4ef71c675ac0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-06 11:47:14","canto_approved_date":"2023-06-23 15:25:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-02-28 14:06:19","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F6.08c","SPBC21.06c","SPAP8A3.08","SPAC20G8.05c","SPAC926.03","SPBC19G7.05c","SPAC1782.09c","SPBC11C11.04c","SPAC1F5.04c","SPCC4B3.15"],"gene_count":10,"ltp_gene_count":5,"approved_date":"2018-03-06"},{"uniquename":"PMID:10747864","title":"Atomic force microscopy reveals two conformations of the 20 S proteasome from fission yeast.","citation":"J Biol Chem 2000 May 05;275(18):13171-4","abstract":"The proteasome is a major cytosolic proteolytic complex, indispensable in eukaryotic cells. The barrel-shaped core of this enzyme, the 20 S proteasome, is built from 28 subunits forming four stacked rings. The two inner beta-rings harbor active centers, whereas the two outer alpha-rings play a structural role. Crystal structure of the yeast 20 S particle showed that the entrance to the central channel was sealed. Because of this result, the path of substrates into the catalytic chamber has remained enigmatic. We have used tapping mode atomic force microscopy (AFM) in liquid to address the dynamic aspects of the 20 S proteasomes from fission yeast. We present here evidence that, when observed with AFM, the proteasome particles in top view position have either open or closed entrance to the central channel. The preferred conformation depends on the ligands present. Apparently, the addition of a substrate to the uninhibited proteasome shifts the equilibrium toward the open conformation. These results shed new light on the possible path of the substrate into the proteolytic chamber.","authors":"Osmulski PA, Gaczynska M","authors_abbrev":"Osmulski PA et al.","pubmed_publication_date":"05 May 2000","pubmed_entrez_date":"2000-04-05","publication_year":"2000","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19619485","title":"Cell size control: governed by a spatial gradient.","citation":"Dev Cell 2009 Jul;17(1):3-4","abstract":"The phenomenon of cell size homeostasis, whereby cells coordinate growth and division to maintain a uniform cell size, has been an outstanding issue in cell biology for many decades. Two recent studies in Nature in fission yeast demonstrate that a gradient of the polarity factor Pom1 is a sensor of cell length that determines the onset of Cdc2 activation and mitosis.","doi":"10.1016/j.devcel.2009.07.006","authors":"Almeida R, Tyers M","authors_abbrev":"Almeida R et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-07-22","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15659877","title":"Fission yeast epsin, Ent1p is required for endocytosis and involved in actin organization.","citation":"Kobe J Med Sci 2004 Jan;50(1-2):47-57","abstract":"In this study, we have characterized an essential gene ent1+ encoding fission yeast epsin, which is similar to mammalian and budding yeast endocytic protein epsins. The S. pombe Ent1p contains ENTH (epsin amino-terminal homology) domain at its amino terminus, two copies of a ubiquitin-interacting motif (UIM) immediately carboxyl-terminal to the ENTH domain, three NPF motifs in the carboxyl-terminal half, and the clathrin-binding motif at the carboxyl terminal. When repressed the expression of ent1+ gene, the conditional ent1 gene knockout cells showed a marked defect in internalization of fluorescent dyes, suggesting that Ent1p is essential for endocytosis. Changes in conserved amino acid residues within ENTH domain in ent1 mutant cells revealed temperature-sensitive defect in actin organization and cell morphology. The Ent1p bound PI(4,5)P2 and PI(3,5)P2 immobilized onto nitrocellulose in vitro and also weakly bound PI(3,4)P2, PI(3,4,5)P3, PI4P and PI5P. Surprisingly, the localization of Ent1p-GFP was not affected even in the its3-1 cells, in which the level of PI(4,5)P2 was severely reduced, suggesting that PI(4,5)P2 may not be essential for proper localization of Ent1p at endocytic sites. Our findings indicate that S. pombe Ent1p is an essential component in endocytic process, and involved in actin organization and cell morphogenesis.","authors":"Sakamoto C, Kawamoto C, Takeuchi K, Miyamoto I, Shuntoh H","authors_abbrev":"Sakamoto C et al.","pubmed_publication_date":"Jan 2004","pubmed_entrez_date":"2005-01-22","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC162.07"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:7768995","title":"The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis.","citation":"J Cell Sci 1995 Feb;108 ( Pt 2):475-86","abstract":"Normal eukaryotic cells do not enter mitosis unless DNA is fully replicated and repaired. Controls called 'checkpoints', mediate cell cycle arrest in response to unreplicated or damaged DNA. Two independent Schizosaccharomyces pombe mutant screens, both of which aimed to isolate new elements involved in checkpoint controls, have identified alleles of the hus5+ gene that are abnormally sensitive to both inhibitors of DNA synthesis and to ionizing radiation. We have cloned and sequenced the hus5+ gene. It is a novel member of the E2 family of ubiquitin conjugating enzymes (UBCs). To understand the role of hus5+ in cell cycle control we have characterized the phenotypes of the hus5 mutants and the hus5 gene disruption. We find that, whilst the mutants are sensitive to inhibitors of DNA synthesis and to irradiation, this is not due to an inability to undergo mitotic arrest. Thus, the hus5+ gene product is not directly involved in checkpoint control. However, in common with a large class of previously characterized checkpoint genes, it is required for efficient recovery from DNA damage or S-phase arrest and manifests a rapid death phenotype in combination with a temperature sensitive S phase and late S/G2 phase cdc mutants. In addition, hus5 deletion mutants are severely impaired in growth and exhibit high levels of abortive mitoses, suggesting a role for hus5+ in chromosome segregation. We conclude that this novel UBC enzyme plays multiple roles and is virtually essential for cell proliferation.","authors":"al-Khodairy F, Enoch T, Hagan IM, Carr AM","authors_abbrev":"al-Khodairy F et al.","pubmed_publication_date":"Feb 1995","pubmed_entrez_date":"1995-02-01","publication_year":"1995","canto_session_key":"238d4f23ca2cdcd5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-07-21 23:32:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-19 14:40:59","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":13,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC9E9.08","SPAC1F7.05","SPAC30D11.13","SPCC1259.13"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2014-05-19"},{"uniquename":"PMID:27074839","title":"Meiotic chromosome mobility in fission yeast is resistant to environmental stress.","citation":"Sci Rep 2016 Apr 14;6:24222","abstract":"The formation of healthy gametes requires pairing of homologous chromosomes (homologs) as a prerequisite for their correct segregation during meiosis. Initially, homolog alignment is promoted by meiotic chromosome movements feeding into intimate homolog pairing by homologous recombination and/or synaptonemal complex formation. Meiotic chromosome movements in the fission yeast, Schizosaccharomyces pombe, depend on astral microtubule dynamics that drag the nucleus through the zygote; known as horsetail movement. The response of microtubule-led meiotic chromosome movements to environmental stresses such as ionizing irradiation (IR) and associated reactive oxygen species (ROS) is not known. Here, we show that, in contrast to budding yeast, the horsetail movement is largely radiation-resistant, which is likely mediated by a potent antioxidant defense. IR exposure of sporulating S. pombe cells induced misrepair and irreparable DNA double strand breaks causing chromosome fragmentation, missegregation and gamete death. Comparing radiation outcome in fission and budding yeast, and studying meiosis with poisoned microtubules indicates that the increased gamete death after IR is innate to fission yeast. Inhibition of meiotic chromosome mobility in the face of IR failed to influence the course of DSB repair, indicating that paralysis of meiotic chromosome mobility in a genotoxic environment is not a universal response among species.","doi":"10.1038/srep24222","authors":"Illner D, Lorenz A, Scherthan H","authors_abbrev":"Illner D et al.","pubmed_publication_date":"14 Apr 2016","pubmed_entrez_date":"2016-04-15","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-04-17 00:15:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:EF192607","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1223.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15035822","title":"Grasping the message: regulated mRNA stability in free radical stress responses. Rodríguez-Gabriel MA, Burns G, McDonald WH et al. RNA-binding protein Csx1 mediates global control of gene expression in response to oxidative stress. EMBO J 2003; 22: 6256-6266.","citation":"Redox Rep 2004;9(1):3-5","abstract":"","authors":"Demple B","authors_abbrev":"Demple B","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-03-24","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8163491","title":"ntf1+ encodes a 6-cysteine zinc finger-containing transcription factor that regulates the nmt1 promoter in fission yeast.","citation":"J Biol Chem 1994 Apr 22;269(16):11921-6","abstract":"The nmt1+ gene of the fission yeast Schizosaccharomyces pombe is subject to transcriptional repression mediated by thiamine. The promoter of nmt1+ has been used to construct a series of vectors that are now commonly used for the regulated expression of genes in S. pombe. In this report, we described ntf1+, a gene involved in regulating nmt1+ expression. The ntf1+ gene was cloned in a high copy suppressor screen that utilized a construct, nmt1:wee1+, in which expression of the mitotic inhibitor Wee1 tyrosine kinase was placed under the control of the nmt1 promoter. ntf1+ encodes a 706-amino acid protein that shares substantial homology with a family of Cys6 zinc finger-containing transcription factors typified by GAL4 from Saccharomyces cerevisiae. Increased gene dosage of ntf1+ greatly increases both the repressed and derepressed activity of the nmt1 promoter. Cells having a disrupted version of ntf1+ are viable thiamine prototrophs, but basal expression from the nmt1 promoter is greatly reduced. These data demonstrate that Ntf1 plays an important role in regulating nmt1 expression.","authors":"Tang CS, Bueno A, Russell P","authors_abbrev":"Tang CS et al.","pubmed_publication_date":"22 Apr 1994","pubmed_entrez_date":"1994-04-22","publication_year":"1994","canto_session_key":"cac62efc496fffc5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-02-09 18:01:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-04 11:34:13","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05","SPCC1223.02","SPAC1486.10","SPAC19D5.01"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2013-06-04"},{"uniquename":"PMID:31206516","title":"Regulation of ectopic heterochromatin-mediated epigenetic diversification by the JmjC family protein Epe1.","citation":"PLoS Genet 2019 Jun;15(6):e1008129","abstract":"H3K9 methylation (H3K9me) is a conserved marker of heterochromatin, a transcriptionally silent chromatin structure. Knowledge of the mechanisms for regulating heterochromatin distribution is limited. The fission yeast JmjC domain-containing protein Epe1 localizes to heterochromatin mainly through its interaction with Swi6, a homologue of heterochromatin protein 1 (HP1), and directs JmjC-mediated H3K9me demethylation in vivo. Here, we found that loss of epe1 (epe1Δ) induced a red-white variegated phenotype in a red-pigment accumulation background that generated uniform red colonies. Analysis of isolated red and white colonies revealed that silencing of genes involved in pigment accumulation by stochastic ectopic heterochromatin formation led to white colony formation. In addition, genome-wide analysis of red- and white-isolated clones revealed that epe1Δ resulted in a heterogeneous heterochromatin distribution among clones. We found that Epe1 had an N-terminal domain distinct from its JmjC domain, which activated transcription in both fission and budding yeasts. The N-terminal transcriptional activation (NTA) domain was involved in suppression of ectopic heterochromatin-mediated red-white variegation. We introduced a single copy of Epe1 into epe1Δ clones harboring ectopic heterochromatin, and found that Epe1 could reduce H3K9me from ectopic heterochromatin but some of the heterochromatin persisted. This persistence was due to a latent H3K9me source embedded in ectopic heterochromatin. Epe1H297A, a canonical JmjC mutant, suppressed red-white variegation, but entirely failed to remove already-established ectopic heterochromatin, suggesting that Epe1 prevented stochastic de novo deposition of ectopic H3K9me in an NTA-dependent but JmjC-independent manner, while its JmjC domain mediated removal of H3K9me from established ectopic heterochromatin. Our results suggest that Epe1 not only limits the distribution of heterochromatin but also controls the balance between suppression and retention of heterochromatin-mediated epigenetic diversification.","doi":"10.1371/journal.pgen.1008129","authors":"Sorida M, Hirauchi T, Ishizaki H, Kaito W, Shimada A, Mori C, Chikashige Y, Hiraoka Y, Suzuki Y, Ohkawa Y, Kato H, Takahata S, Murakami Y","authors_abbrev":"Sorida M et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-06-18","publication_year":"2019","canto_session_key":"35e6ffe290c8f5c3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masato Sorida","canto_first_approved_date":"2024-01-01 15:44:03","canto_approved_date":"2024-04-23 16:07:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-31 22:32:01","canto_added_date":"2019-06-19 00:15:04","annotation_curators":[{"name":"Masato Sorida","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC631.02","SPBC18H10.16","SPAC664.01c","SPBC16D10.07c","SPBC428.08c","SPAC16A10.07c","SPCC622.16c","SPBC405.01","SPCC569.08c","SPCC736.11","SPAC959.05c","SPBC800.03"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2024-01-01"},{"uniquename":"PMID:22508988","title":"Separate domains of fission yeast Cdk9 (P-TEFb) are required for capping enzyme recruitment and primed (Ser7-phosphorylated) Rpb1 carboxyl-terminal domain substrate recognition.","citation":"Mol Cell Biol 2012 Jul;32(13):2372-83","abstract":"In fission yeast, discrete steps in mRNA maturation and synthesis depend on a complex containing the 5'-cap methyltransferase Pcm1 and Cdk9, which phosphorylates the RNA polymerase II (Pol II) carboxyl-terminal domain (CTD) and the processivity factor Spt5 to promote transcript elongation. Here we show that a Cdk9 carboxyl-terminal extension, distinct from the catalytic domain, mediates binding to both Pcm1 and the Pol II CTD. Removal of this segment diminishes Cdk9/Pcm1 chromatin recruitment and Spt5 phosphorylation in vivo and leads to slow growth and hypersensitivity to cold temperature, nutrient limitation, and the IMP dehydrogenase inhibitor mycophenolic acid (MPA). These phenotypes, and the Spt5 phosphorylation defect, are suppressed by Pcm1 overproduction, suggesting that normal transcript elongation and gene expression depend on physical linkage between Cdk9 and Pcm1. The extension is dispensable, however, for recognition of CTD substrates \"primed\" by Mcs6 (Cdk7). On defined peptide substrates in vitro, Cdk9 prefers CTD repeats phosphorylated at Ser7 over unmodified repeats. In vivo, Ser7 phosphorylation depends on Mcs6 activity, suggesting a conserved mechanism, independent of chromatin recruitment, to order transcriptional CDK functions. Therefore, fission yeast Cdk9 comprises a catalytic domain sufficient for primed substrate recognition and a multivalent recruitment module that couples transcription with capping.","doi":"10.1128/MCB.06657-11","authors":"St Amour CV, Sansó M, Bösken CA, Lee KM, Larochelle S, Zhang C, Shokat KM, Geyer M, Fisher RP","authors_abbrev":"St Amour CV et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-04-18","publication_year":"2012","canto_session_key":"ab801a175ed0c533","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Robert Fisher","canto_first_approved_date":"2019-10-31 11:53:39","canto_approved_date":"2024-03-20 07:34:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-14 19:25:03","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Robert Fisher","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16C9.06c","SPAC821.09","SPCC330.10","SPBC32H8.10","SPAC1687.11","SPBC28F2.12","SPBC19F8.07","SPBC32F12.06","SPAC644.04","SPAC1D4.06c","SPAC23C4.19"],"gene_count":11,"ltp_gene_count":8,"approved_date":"2019-10-31"},{"uniquename":"PMID:17360628","title":"Structural characterization of the fission yeast U5.U2/U6 spliceosome complex.","citation":"Proc Natl Acad Sci U S A 2007 Feb 27;104(9):3195-200","abstract":"The spliceosome is a dynamic macromolecular machine that catalyzes the excision of introns from pre-mRNA. The megadalton-sized spliceosome is composed of four small nuclear RNPs and additional pre-mRNA splicing factors. The formation of an active spliceosome involves a series of regulated steps that requires the assembly and disassembly of large multiprotein/RNA complexes. The dynamic nature of the pre-mRNA splicing reaction has hampered progress in analyzing the structure of spliceosomal complexes. We have used cryo-electron microscopy to produce a 29-A density map of a stable 37S spliceosomal complex from the genetically tractable fission yeast, Schizosaccharomyces pombe. Containing the U2, U5, and U6 snRNAs, pre-mRNA splicing intermediates, U2 and U5 snRNP proteins, the Nineteen Complex (NTC), and second-step splicing factors, this complex closely resembles in vitro purified mammalian C complex. The density map reveals an asymmetric particle, approximately 30 x 20 x 18 nm in size, which is composed of distinct domains that contact each other at the center of the complex.","authors":"Ohi MD, Ren L, Wall JS, Gould KL, Walz T","authors_abbrev":"Ohi MD et al.","pubmed_publication_date":"27 Feb 2007","pubmed_entrez_date":"2007-03-16","publication_year":"2007","canto_session_key":"37f8e8f14defdf7e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-11 13:31:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-11 13:30:46","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-08-11"},{"uniquename":"PMID:52399","title":"Role of cell wall topography in conjugation of Schizosaccharomyces pombe.","citation":"Can J Microbiol 1975 Sep;21(9):1399-405","abstract":"The surface of the zygotes of Schizosaccharomyces pombe was studied by observing fluorescence following primulin treatment. Conjugation occurred only at the poles. Competence to fuse was independent of actual pole growth and pole ontogeny (old or new pole). The cells were competent to fuse throughout the first three-quarters of the cell cycle. Morphological criteria indicate that cell pairs are not synchronized at the moment of fusion. The length of the G1 phases of individual conjugating cells apparently ranges from 0.1 to 0.7 of the cell cycle duration.","authors":"Streiblová E, Wolf A","authors_abbrev":"Streiblová E et al.","pubmed_publication_date":"Sep 1975","pubmed_entrez_date":"1975-09-01","publication_year":"1975","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26244885","title":"An Extended, Boolean Model of the Septation Initiation Network in S.Pombe Provides Insights into Its Regulation.","citation":"PLoS One 2015;10(8):e0134214","abstract":"Cytokinesis in fission yeast is controlled by the Septation Initiation Network (SIN), a protein kinase signaling network using the spindle pole body as scaffold. In order to describe the qualitative behavior of the system and predict unknown mutant behaviors we decided to adopt a Boolean modeling approach. In this paper, we report the construction of an extended, Boolean model of the SIN, comprising most SIN components and regulators as individual, experimentally testable nodes. The model uses CDK activity levels as control nodes for the simulation of SIN related events in different stages of the cell cycle. The model was optimized using single knock-out experiments of known phenotypic effect as a training set, and was able to correctly predict a double knock-out test set. Moreover, the model has made in silico predictions that have been validated in vivo, providing new insights into the regulation and hierarchical organization of the SIN.","doi":"10.1371/journal.pone.0134214","authors":"Chasapi A, Wachowicz P, Niknejad A, Collin P, Krapp A, Cano E, Simanis V, Xenarios I","authors_abbrev":"Chasapi A et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-08-06","publication_year":"2015","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2015-08-07 00:20:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34853311","title":"Structural basis for the E3 ligase activity enhancement of yeast Nse2 by SUMO-interacting motifs.","citation":"Nat Commun 2021 Dec 01;12(1):7013","abstract":"Post-translational modification of proteins by ubiquitin and ubiquitin-like modifiers, such as SUMO, are key events in protein homeostasis or DNA damage response. Smc5/6 is a nuclear multi-subunit complex that participates in the recombinational DNA repair processes and is required in the maintenance of chromosome integrity. Nse2 is a subunit of the Smc5/6 complex that possesses SUMO E3 ligase activity by the presence of a SP-RING domain that activates the E2~SUMO thioester for discharge on the substrate. Here we present the crystal structure of the SUMO E3 ligase Nse2 in complex with an E2-SUMO thioester mimetic. In addition to the interface between the SP-RING domain and the E2, the complex reveals how two SIM (SUMO-Interacting Motif) -like motifs in Nse2 are restructured upon binding the donor and E2-backside SUMO during the E3-dependent discharge reaction. Both SIM interfaces are essential in the activity of Nse2 and are required to cope with DNA damage.","doi":"10.1038/s41467-021-27301-9","authors":"Varejão N, Lascorz J, Codina-Fabra J, Bellí G, Borràs-Gas H, Torres-Rosell J, Reverter D","authors_abbrev":"Varejão N et al.","pubmed_publication_date":"01 Dec 2021","pubmed_entrez_date":"2021-12-02","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.13","SPAC16A10.06c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:22711988","title":"Sos7, an essential component of the conserved Schizosaccharomyces pombe Ndc80-MIND-Spc7 complex, identifies a new family of fungal kinetochore proteins.","citation":"Mol Cell Biol 2012 Aug;32(16):3308-20","abstract":"Chromosome segregation is powered by the kinetochore, a large macromolecular structure assembled on centromeric chromatin. Attachment of sister chromatids to microtubules is mediated by the highly conserved tripartite KMN (acronym for KNL-1-Mis12-Ndc80) kinetochore network. In the fission yeast Schizosaccharomyces pombe, the equivalent complex is called NMS (Ndc80-MIND-Spc7). Here, we show that not all components of the NMS complex had been identified previously. A 10th NMS component exists, the essential Sos7 protein, which is a genetic and physical interaction partner of Spc7. The analysis of sos7 kinetochore-null mutant yeast strains demonstrated that Sos7 is central to NMS function. In particular, Sos7 is required for kinetochore targeting of Spc7 as well as components of the MIND complex. sos7 mutant strains show severe chromosome missegregation phenotypes and have compromised microtubule-kinetochore interactions. Sos7 is the founding member of a functionally conserved fungal kinetochore family not present in the point centromere carrying Saccharomycotina clusters, suggesting that the new Sos7 family might be a signature motif of fungi with regional centromeres.","doi":"10.1128/MCB.00212-12","authors":"Jakopec V, Topolski B, Fleig U","authors_abbrev":"Jakopec V et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-06-20","publication_year":"2012","canto_session_key":"8acb880886aa8d18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"ursula fleig","canto_first_approved_date":"2016-10-10 22:21:00","canto_approved_date":"2025-09-04 06:28:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-24 14:47:13","canto_added_date":"2012-06-22 19:06:44","annotation_curators":[{"name":"ursula fleig","community_curator":true,"annotation_count":25,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC409.09c","SPBC409.04c","SPCC1020.02","SPAPB17E12.06"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-10-10"},{"uniquename":"PMID:35011726","title":"Role of Nse1 Subunit of SMC5/6 Complex as a Ubiquitin Ligase.","citation":"Cells 2022 Jan 04;11(1)","abstract":"Structural Maintenance of Chromosomes (SMC) complexes are important for many aspects of the chromosomal organization. Unlike cohesin and condensin, the SMC5/6 complex contains a variant RING domain carried by its Nse1 subunit. RING domains are characteristic for ubiquitin ligases, and human NSE1 has been shown to possess ubiquitin-ligase activity in vitro. However, other studies were unable to show such activity. Here, we confirm Nse1 ubiquitin-ligase activity using purified  Schizosaccharomyces pombe  proteins. We demonstrate that the Nse1 ligase activity is stimulated by Nse3 and Nse4. We show that Nse1 specifically utilizes Ubc13/Mms2 E2 enzyme and interacts directly with ubiquitin. We identify the Nse1 mutation (R188E) that specifically disrupts its E3 activity and demonstrate that the Nse1-dependent ubiquitination is particularly important under replication stress. Moreover, we determine Nse4 (lysine K181) as the first known SMC5/6-associated Nse1 substrate. Interestingly, abolition of Nse4 modification at K181 leads to suppression of DNA-damage sensitivity of other SMC5/6 mutants. Altogether, this study brings new evidence for Nse1 ubiquitin ligase activity, significantly advancing our understanding of this enigmatic SMC5/6 function.","doi":"10.3390/cells11010165","authors":"Kolesar P, Stejskal K, Potesil D, Murray JM, Palecek JJ","authors_abbrev":"Kolesar P et al.","pubmed_publication_date":"04 Jan 2022","pubmed_entrez_date":"2022-01-11","publication_year":"2022","canto_session_key":"96964a18b157de92","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Kolesar","canto_first_approved_date":"2022-10-17 14:21:39","canto_approved_date":"2022-10-31 14:35:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-10-14 13:37:33","canto_added_date":"2022-01-13 01:15:04","annotation_curators":[{"name":"Peter Kolesar","community_curator":true,"annotation_count":7,"orcid":"0000-0002-3315-3586","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.06","SPCC645.04","SPBC1604.21c","SPCC338.05c","SPBC20F10.04c","SPAC11E3.08c","SPCC550.05","SPAC11E3.04c","SPBC337.08c","SPAC16A10.06c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2022-10-17"},{"uniquename":"PMID:39932033","title":"Saccharomyces cerevisiae Dmo2p is required for the stability and maturation of newly translated Cox2p.","citation":"FEBS J 2025 Feb 11;","abstract":"Based on available platforms detailing the Saccharomyces cerevisiae mitochondrial proteome and other high-throughput studies, we identified the yeast gene DMO2 as having a profile of genetic and physical interactions that indicate a putative role in mitochondrial respiration. Dmo2p is a homologue to human distal membrane-arm assembly complex protein 1 (DMAC1); both proteins have two conserved cysteines in a Cx 2 C motif. Here, we localised Dmo2p in the mitochondrial inner membrane with the conserved cysteines facing the intermembrane space. The respiratory deficiency of dmo2 mutants at 37°C led to a reduction in cytochrome c oxidase (COX) activity (COX) and in the formation of cytochrome bc 1  complex-COX supercomplexes; dmo2 also has a rapid turnover of Cox2p, the second subunit of the COX complex that harbours the binuclear Cu A  centre. Moreover, Dmo2p co-immunoprecipitates with Cox2p and components required for maturation of the Cu A  centre, such as Sco1p and Sco2p. Finally, DMO2 overexpression can suppress cox23 respiratory deficiency, a mutant that has impaired mitochondrial copper homeostasis. Mass spectrometry data unveiled the interaction of Dmo2p with different large molecular complexes, including bc 1 -COX supercomplexes, the TIM23 machinery and the ADP/ATP nucleotide translocator. Overall, our data suggest that Dmo2p is required for Cox2p maturation, potentially by aiding proteins involved in copper transport and incorporation into Cox2p.","doi":"10.1111/febs.70009","authors":"Soares MAKM, Franco LVR, Chagas JAC, Gomes F, Barros MH","authors_abbrev":"Soares MAKM et al.","pubmed_publication_date":"11 Feb 2025","pubmed_entrez_date":"2025-02-11","publication_year":"2025","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.14c","SPMIT.11"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:28476936","title":"Genome-wide screen for cell growth regulators in fission yeast.","citation":"J Cell Sci 2017 Jun 15;130(12):2049-2055","abstract":"Cellular growth control is important for all living organisms, but experimental investigation into this problem is difficult because of the complex range of growth regulatory mechanisms. Here, we have used the fission yeast  Schizosaccharomyces pombe  to identify potential master regulators of growth. At the restrictive temperature, the  S. pombe pat1 ts  mei4Δ  strain enters the meiotic developmental program, but arrests in meiotic G2 phase as  mei4 +   is essential for meiotic progression. These cells do not grow, even in an abundance of nutrients. To identify regulators of growth that can reverse this growth arrest, we introduced an ORFeome plasmid library into the  pat1 ts mei4Δ  strain. Overexpression of eight genes promoted cell growth; two of these were core RNA polymerase subunits, and one was  sck2 +   , an S6 kinase thought to contribute to TORC1 signalling. Sck2 had the greatest effect on cell growth, and we also show that it significantly increases the cellular transcription rate. These findings indicate, for the first time, that global transcriptional control mediated through S6 kinase signalling is central to cellular growth control.","doi":"10.1242/jcs.200865","authors":"Weston L, Greenwood J, Nurse P","authors_abbrev":"Weston L et al.","pubmed_publication_date":"15 Jun 2017","pubmed_entrez_date":"2017-05-07","publication_year":"2017","canto_session_key":"5b68d89f4f39e301","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2021-06-08 09:34:04","canto_approved_date":"2024-03-29 09:33:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-04 12:06:36","canto_added_date":"2017-05-11 00:15:13","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":29,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B9.02c","SPAC23C4.15","SPAC1B3.12c","SPCC1620.12c","SPBC19C2.05","SPBC146.14c","SPCC4G3.08","SPAC3H5.11","SPAC3A12.07","SPBC337.14","SPACUNK4.06c","SPAC23H4.08","SPBC28F2.12","SPAC23G3.01","SPCC24B10.07","SPAC56F8.07","SPAC22E12.14c","SPCC320.07c","SPCC1442.10c","SPBC14C8.12","SPBC19C2.03","SPCC1020.04c","SPBC32H8.11","SPAC27D7.03c","SPAPYUG7.04c"],"gene_count":25,"ltp_gene_count":24,"approved_date":"2021-06-08"},{"uniquename":"PMID:24454826","title":"E3 ubiquitin ligase Pub1 is implicated in endocytosis of a GPI-anchored protein Ecm33 in fission yeast.","citation":"PLoS One 2014;9(1):e85238","abstract":"We previously identified three glycosylphosphatidylinositol (GPI)-anchored proteins including Ecm33, as multicopy suppressors of the phenotypes of a mutant allele of cis4(+) that encodes a zinc transporter in fission yeast. Here, we further identified two multicopy suppressor genes, ubi1 (+) and ubc4 (+), encoding ubiquitin-ribosomal fusion protein and ubiquitin conjugating enzyme E2, respectively. In addition, Ubi1 or Ubc4 overexpression failed to suppress the phenotypes of the double deletion of cis4 (+) and pub1 (+) gene, which encodes a HECT-type ubiquitin ligase E3. During exponential phase GFP-Ecm33 localized at the growing cell tips of the cell surface and the medial region in wild-type cells. Notably, during the post-exponential and stationary phase, GFP-Ecm33 in wild-type cells was internalized and mostly localized to the Golgi/endosomes, but it was still stably localized at the cell surface in Δpub1 cells. The Δpub1 cells showed osomoremedial phenotypes to various drugs indicating their defects in cell wall integrity. Altogether, our findings reveal a novel role for Pub1 in endocytosis of Ecm33 and regulation of cell wall integrity in fission yeast.","doi":"10.1371/journal.pone.0085238","authors":"Fang Y, Jaiseng W, Ma Y, Hu L, Yamazaki S, Zhang X, Hayafuji T, Shi L, Kuno T","authors_abbrev":"Fang Y et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-01-24","publication_year":"2014","canto_session_key":"c76735ba97e3453b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-06-08 21:14:26","canto_approved_date":"2026-06-08 21:14:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-05-31 16:44:08","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":35,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16E9.11c","SPAC6G10.11c","SPBP16F5.07","SPAC11G7.04","SPBC119.02","SPAC11G7.02","SPBC337.08c","SPAC17D4.03c","SPAC1805.15c","SPAC1705.03c","SPBC359.03c"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2026-06-08"},{"uniquename":"PMID:2274023","title":"Molecular basis for determining the sensitivity of eucaryotes to the antimitotic drug rhizoxin.","citation":"Mol Gen Genet 1990 Jul;222(2-3):169-75","abstract":"Rhizoxin, an antibiotic, exhibits potent anti-mitotic activity against most eucaryotic cells including those of higher vertebrates, plants and fungi by binding to beta-tubulin. The benA gene of three independently isolated rhizoxin-resistant (Rhir) mutants of Aspergillus nidulans was cloned, sequenced and compared with that of the wild-type, rhizoxin-sensitive (Rhis) strain. In all three Rhir mutants, the AAC codon for Asn-100 of the benA beta-tubulin gene was altered to ATC, coding for Ile. Sequence displacement experiments confirmed that the substitution of Ile for Asn-100 confers resistance to rhizoxin in this organism. The amino acid sequences of beta-tubulin surrounding the 100th amino acid residue from the N-terminus including Asn-100 are highly conserved with a few exceptions. The fission yeast Schizosaccharomyces pombe and the budding yeast Saccharomyces cerevisiae are naturally occurring Rhir organisms whose beta-tubulin genes encode Ile and Val respectively at the 100th amino acid residue. The Ile-100 of S. pombe and the Val-100 of S. cerevisiae were altered to Asn using site-directed mutagenesis and gene displacement techniques. The resultant haploid strains of these two yeasts uniquely expressing beta-tubulin (Asn-100) instead of beta-tubulin (Ile-100 or Val-100) were found to be Rhis. Haploid yeast expressing beta-tubulin (Asn-100) is normal except for its sensitivity to rhizoxin. These results suggest that rhizoxin resistance has a common basis in both naturally occurring species and experimentally selected mutants in the substitution of Ile or Val for Asn-100 in beta-tubulin.","authors":"Takahashi M, Matsumoto S, Iwasaki S, Yahara I","authors_abbrev":"Takahashi M et al.","pubmed_publication_date":"Jul 1990","pubmed_entrez_date":"1990-07-01","publication_year":"1990","canto_session_key":"b7e3c44b6b780f5b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-04-24 11:56:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-08 16:39:31","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-08"},{"uniquename":"PMID:7889931","title":"The crystal structure of p13suc1, a p34cdc2-interacting cell cycle control protein.","citation":"EMBO J 1995 Mar 01;14(5):1004-14","abstract":"p13suc1 binds to p34cdc2 kinase and is essential for cell cycle progression in eukaryotic cells. The crystal structure of S.pombe p13suc1 has been solved to 2.7 A resolution using data collected at the ESRF source, Grenoble, from both native crystals and crystals of a seleno-methionine derivative. The starting point for structure solution was the determination of the six selenium sites by direct methods. The structure is dominated by a four-stranded beta-sheet, with four further alpha-helical regions. p13suc1 crystallizes as a dimer in the asymmetric unit stabilized by the binding of two zinc ions. A third zinc site stabilizes the higher-order crystal packing. The sites are consistent with a requirement for zinc during crystal growth. A likely site for p13suc1-protein interaction is immediately evident on one face of the p13suc1 surface. This region comprises a group of conserved, exposed aromatic and hydrophobic residues below a flexible negatively charged loop. A conserved positively charged area would also present a notable surface feature in the monomer, but is buried at the dimer interface. p13suc1 is larger than its recently solved human homologue p9CKS2, with the extra polypeptide forming a helical N-terminal extension and a surface loop between alpha-helices 3 and 4. Notably, p13suc1 does not show the unusual beta-strand exchange that creates an intimate p9CKS2 dimer. p13suc1 cannot oligomerize to form a stable hexamer as has been proposed for p9CKS2.","authors":"Endicott JA, Noble ME, Garman EF, Brown N, Rasmussen B, Nurse P, Johnson LN","authors_abbrev":"Endicott JA et al.","pubmed_publication_date":"01 Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_session_key":"d9347ce7c1c04a41","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-04-25 10:18:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-24 11:44:39","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1734.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-24"},{"uniquename":"PMID:19704894","title":"Exploring the conservation of synthetic lethal genetic interaction networks.","citation":"Commun Integr Biol 2009;2(2):78-81","abstract":"High-throughput studies have enabled the large-scale mapping of synthetic lethal genetic interaction networks in the budding yeast Saccharomyces cerevisiae (S. cerevisiae). Recently, complementary high-throughput methods have been developed to map genetic interactions in the fission yeast Schizosaccharomyces pombe (S. pombe), enabling comparative analyses of genetic interaction networks between S. pombe and S. cerevisiae, two species separated by hundreds of millions of years of evolution. The resultant data has providing our first view of a possible core genetic interaction network shared between two distantly related eukaryotes, and identified numerous species-specific interactions that may contribute to the unique biology of these two different organisms. These and other results suggest that comparative interactomic studies will provide novel insights into the structure of genetic interaction networks.","authors":"Dixon SJ, Andrews BJ, Boone C","authors_abbrev":"Dixon SJ et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-08-26","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36630955","title":"Zinc-finger protein Zpr1 is a bespoke chaperone essential for eEF1A biogenesis.","citation":"Mol Cell 2023 Jan 19;83(2):252-265.e13","abstract":"The conserved regulon of heat shock factor 1 in budding yeast contains chaperones for general protein folding as well as zinc-finger protein Zpr1, whose essential role in archaea and eukaryotes remains unknown. Here, we show that Zpr1 depletion causes acute proteotoxicity driven by biosynthesis of misfolded eukaryotic translation elongation factor 1A (eEF1A). Prolonged Zpr1 depletion leads to eEF1A insufficiency, thereby inducing the integrated stress response and inhibiting protein synthesis. Strikingly, we show by using two distinct biochemical reconstitution approaches that Zpr1 enables eEF1A to achieve a conformational state resistant to protease digestion. Lastly, we use a ColabFold model of the Zpr1-eEF1A complex to reveal a folding mechanism mediated by the Zpr1's zinc-finger and alpha-helical hairpin structures. Our work uncovers the long-sought-after function of Zpr1 as a bespoke chaperone tailored to the biogenesis of one of the most abundant proteins in the cell.","doi":"10.1016/j.molcel.2022.12.012","authors":"Sabbarini IM, Reif D, McQuown AJ, Nelliat AR, Prince J, Membreno BS, Wu CC, Murray AW, Denic V","authors_abbrev":"Sabbarini IM et al.","pubmed_publication_date":"19 Jan 2023","pubmed_entrez_date":"2023-01-11","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC794.09c","SPAC15A10.04c","SPBC839.15c","SPAC23A1.10"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:17194026","title":"A fission yeast-based test system for the determination of IC50 values of anti-prostate tumor drugs acting on CYP21.","citation":"J Enzyme Inhib Med Chem 2006 Oct;21(5):547-56","abstract":"Human steroid 21-hydroxylase (CYP21) and steroid 17alpha-hydroxylase/17,20-lyase (CYP17) are two closely related cytochrome P450 enzymes involved in the steroidogenesis of glucocorticoids, mineralocorticoids, and sex hormones, respectively. Compounds that inhibit CYP17 activity are of pharmacological interest as they could be used for the treatment of prostate cancer. However, in many cases little is known about a possible co-inhibition of CYP21 activity by CYP17 inhibitors, which would greatly reduce their pharmacological value. We have previously shown that fission yeast strains expressing mammalian cytochrome P450 steroid hydroxylases are suitable systems for whole-cell conversion of steroids and may be used for biotechnological applications or for screening of inhibitors. In this study, we developed a very simple and fast method for the determination of enzyme inhibition using Schizosaccharomyces pombe strains that functionally express either human CYP17 or CYP21. Using this system we tested several compounds of different structural classes with known CYP17 inhibitory potency (i.e. Sa 40, YZ5ay, BW33, and ketoconazole) and determined IC50 values that were about one order of magnitude higher in comparison to data previously reported using human testes microsomes. One compound, YZ5ay, was found to be a moderate CYP21 inhibitor with an IC50 value of 15 microM, which is about eight-fold higher than the value determined for CYP17 inhibition (1.8 microM) in fission yeast. We conclude that, in principle, co-inhibition of CYP21 by CYP17 inhibitors cannot be ruled out.","authors":"Drăgan CA, Hartmann RW, Bureik M","authors_abbrev":"Drăgan CA et al.","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-12-30","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17660439","title":"Essential roles of class E Vps proteins for sorting into multivesicular bodies in Schizosaccharomyces pombe.","citation":"Microbiology (Reading) 2007 Aug;153(Pt 8):2753-2764","abstract":"The multivesicular body (MVB) sorting pathway is required for a number of biological processes, including downregulation of cell-surface proteins and protein sorting into the vacuolar lumen. The function of this pathway requires endosomal sorting complexes required for transport (ESCRT) composed of class E vacuolar protein sorting (Vps) proteins in Saccharomyces cerevisiae, many of which are conserved in Schizosaccharomyces pombe. Of these, sst4/vps27 (homologous to VPS27) and sst6 (similar to VPS23) have been identified as suppressors of sterility in ste12Delta (sst), although their functions have not been uncovered to date. In this report, these two sst genes are shown to be required for vacuolar sorting of carboxypeptidase Y (CPY) and an MVB marker, the ubiquitin-GFP-carboxypeptidase S (Ub-GFP-CPS) fusion protein, despite the lack of the ubiquitin E2 variant domain in Sst6p. Disruption mutants of a variety of other class E vps homologues also had defects in sorting of CPY and Ub-GFP-CPS. Sch. pombe has a mammalian AMSH homologue, sst2. Phenotypic analyses suggested that Sst2p is a class E Vps protein. Taken together, these results suggest that sorting into multivesicular bodies is dependent on class E Vps proteins, including Sst2p, in Sch. pombe.","doi":"10.1099/mic.0.2007/006072-0","authors":"Iwaki T, Onishi M, Ikeuchi M, Kita A, Sugiura R, Giga-Hama Y, Fukui Y, Takegawa K","authors_abbrev":"Iwaki T et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-07-31","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC11H11.01","SPAC9E9.14","SPBC1734.08","SPAC19A8.05c","SPAC1B3.07c","SPAC19B12.10","SPAC4F8.01","SPBC4B4.06","SPAC2G11.06","SPBC651.05c","SPAC1142.07c","SPBC3B9.09","SPBC215.14c"],"gene_count":13,"ltp_gene_count":13},{"uniquename":"PMID:23716598","title":"Lack of tRNA modification isopentenyl-A37 alters mRNA decoding and causes metabolic deficiencies in fission yeast.","citation":"Mol Cell Biol 2013 Aug;33(15):2918-29","abstract":"tRNA isopentenyltransferases (Tit1) modify tRNA position 37, adjacent to the anticodon, to N6-isopentenyladenosine (i6A37) in all cells, yet the tRNA subsets selected for modification vary among species, and their relevance to phenotypes is unknown. We examined the function of i6A37 in Schizosaccharomyces pombe tit1+ and tit1-Δ cells by using a β-galactosidase codon-swap reporter whose catalytic activity is sensitive to accurate decoding of codon 503. i6A37 increased the activity of tRNACys at a cognate codon and that of tRNATyr at a near-cognate codon, suggesting that i6A37 promotes decoding activity generally and increases fidelity at cognate codons while decreasing fidelity at noncognate codons. S. pombe cells lacking tit1+ exhibit slow growth in glycerol or rapamycin. While existing data link wobble base U34 modifications to translation of functionally related mRNAs, whether this might extend to the anticodon-adjacent position 37 was unknown. Indeed, we found a biased presence of i6A37-cognate codons in high-abundance mRNAs for ribosome subunits and energy metabolism, congruent with the observed phenotypes and the idea that i6A37 promotes translational efficiency. Polysome profiles confirmed the decreased translational efficiency of mRNAs in tit1-Δ cells. Because subsets of i6A37-tRNAs differ among species, as do their cognate codon-sensitive mRNAs, these genomic variables may underlie associated phenotypic differences.","doi":"10.1128/MCB.00278-13","authors":"Lamichhane TN, Blewett NH, Crawford AK, Cherkasova VA, Iben JR, Begley TJ, Farabaugh PJ, Maraia RJ","authors_abbrev":"Lamichhane TN et al.","pubmed_publication_date":"Aug 2013","pubmed_entrez_date":"2013-05-30","publication_year":"2013","canto_session_key":"7a4c7e82dec01c2b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19154515","title":"On the molecular etiology of Cornelia de Lange syndrome.","citation":"Ann N Y Acad Sci 2009 Jan;1151:22-37","abstract":"Cornelia de Lange syndrome (CdLS) is genetically heterogeneous and is usually sporadic, occurring approximately once per 10,000 births. CdLS individuals display diverse and variable deficits in growth, mental development, limbs, and organs. In the past few years it has been shown that CdLS is caused by gene mutations affecting proteins involved in sister chromatid cohesion. Studies in model organisms, and more recently in human cells, have revealed, somewhat unexpectedly, that the developmental deficits in CdLS likely arise from changes in gene expression. The mechanisms by which cohesion factors regulate gene expression remain to be elucidated, but current data suggest that they likely regulate transcription in multiple ways.","doi":"10.1111/j.1749-6632.2008.03450.x","authors":"Dorsett D, Krantz ID","authors_abbrev":"Dorsett D et al.","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2009-01-22","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34575767","title":"The Role of the Cell Integrity Pathway in Septum Assembly in Yeast.","citation":"J Fungi (Basel) 2021 Sep 06;7(9)","abstract":"Cytokinesis divides a mother cell into two daughter cells at the end of each cell cycle and proceeds via the assembly and constriction of a contractile actomyosin ring (CAR). Ring constriction promotes division furrow ingression, after sister chromatids are segregated to opposing sides of the cleavage plane. Cytokinesis contributes to genome integrity because the cells that fail to complete cytokinesis often reduplicate their chromosomes. While in animal cells, the last steps of cytokinesis involve extracellular matrix remodelling and mid-body abscission, in yeast, CAR constriction is coupled to the synthesis of a polysaccharide septum. To preserve cell integrity during cytokinesis, fungal cells remodel their cell wall through signalling pathways that connect receptors to downstream effectors, initiating a cascade of biological signals. One of the best-studied signalling pathways is the cell wall integrity pathway (CWI) of the budding yeast  Saccharomyces cerevisiae  and its counterpart in the fission yeast  Schizosaccharomyces pombe , the cell integrity pathway (CIP). Both are signal transduction pathways relying upon a cascade of MAP kinases. However, despite strong similarities in the assembly of the septa in both yeasts, there are significant mechanistic differences, including the relationship of this process with the cell integrity signalling pathways.","doi":"10.3390/jof7090729","authors":"Roncero C, Celador R, Sánchez N, García P, Sánchez Y","authors_abbrev":"Roncero C et al.","pubmed_publication_date":"06 Sep 2021","pubmed_entrez_date":"2021-09-28","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-09-30 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6048122","title":"\"Twin meiosis\" and other ambivalences in the life cycle of Schizosaccharomyces pombe.","citation":"Science 1967 Nov 10;158(3802):796-8","abstract":"Diploid cells of the yeast Schizosaccharomyces pombe carrying the mating-type allele h(90) are capable of sporulation and copulation. After copulation karyogamy does not always occur. In this case both nuclei will undergo meioses separately (twin meiosis). Asci with eight haploid spores derive from this event. Diploid cells homozygous for the mating-type alleles h(+) or h(-) do not sporulate. However, their nuclei can perform meiosis when they are in a common cytoplasm with a diploid nucleus of compatible mating type.","authors":"Gutz H","authors_abbrev":"Gutz H","pubmed_publication_date":"10 Nov 1967","pubmed_entrez_date":"1967-11-10","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10683446","title":"A conserved small GTP-binding protein Alp41 is essential for the cofactor-dependent biogenesis of microtubules in fission yeast.","citation":"FEBS Lett 2000 Feb 18;468(1):84-8","abstract":"The proper folding of tubulins and their incorporation into microtubules consist of a series of reactions, in which evolutionarily conserved proteins, cofactors A to E, play a vital role. We have cloned a fission yeast gene (alp41(+)) which encodes a highly conserved small GTP-binding protein homologous to budding yeast CIN4 and human ARF-like Arl2. alp41(+) is essential, disruption of which results in microtubule dysfunction and growth polarity defects. Genetic analysis indicates that Alp41 plays a crucial role in the cofactor-dependent pathway, in which it functions upstream of the cofactor D homologue Alp1(D) and possibly in concert with Alp21(E).","authors":"Radcliffe PA, Vardy L, Toda T","authors_abbrev":"Radcliffe PA et al.","pubmed_publication_date":"18 Feb 2000","pubmed_entrez_date":"2000-02-23","publication_year":"2000","canto_session_key":"f66edfaf0b084408","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-09-07 18:56:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-25 14:46:43","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.05c","SPAC13D6.05","SPBC11C11.04c","SPAC22H10.10"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-03-25"},{"uniquename":"PMID:38715219","title":"Rcn1, the fission yeast homolog of human DSCR1, regulates arsenite tolerance independently from calcineurin.","citation":"Genes Cells 2024 May 07;","abstract":"Calcineurin (CN) is a conserved Ca 2+ /calmodulin-dependent phosphoprotein phosphatase that plays a key role in Ca 2+  signaling. Regulator of calcineurin 1 (RCAN1), also known as Down syndrome critical region gene 1 (DSCR1), interacts with calcineurin and inhibits calcineurin-dependent signaling in various organisms. Ppb1, the fission yeast calcineurin regulates Cl - -homeostasis, and Ppb1 deletion induces MgCl 2  hypersensitivity. Here, we characterize the conserved and novel roles of the fission yeast RCAN1 homolog rcn1 + . Consistent with its role as an endogenous calcineurin inhibitor, Rcn1 overproduction reproduced the calcineurin-null phenotypes, including MgCl 2  hypersensitivity and inhibition of calcineurin signaling upon extracellular Ca 2+  stimuli as evaluated by the nuclear translocation and transcriptional activation of the calcineurin substrate Prz1. Notably, overexpression of rcn1 +  causes hypersensitivity to arsenite, whereas calcineurin deletion induces arsenite tolerance, showing a phenotypic discrepancy between Rcn1 overexpression and calcineurin deletion. Importantly, although Rcn1 deletion induces modest sensitivities to arsenite and MgCl 2  in wild-type cells, the arsenite tolerance, but not MgCl 2  sensitivity, associated with Ppb1 deletion was markedly suppressed by Rcn1 deletion. Collectively, our findings reveal a previously unrecognized functional collaboration between Rcn1 and calcineurin, wherein Rcn1 not only negatively regulates calcineurin in the Cl -  homeostasis, but also Rcn1 mediates calcineurin signaling to modulate arsenite cytotoxicity.","doi":"10.1111/gtc.13122","authors":"Takasaki T, Bamba A, Kukita Y, Nishida A, Kanbayashi D, Hagihara K, Satoh R, Ishihara K, Sugiura R","authors_abbrev":"Takasaki T et al.","pubmed_publication_date":"07 May 2024","pubmed_entrez_date":"2024-05-08","publication_year":"2024","canto_session_key":"9badee1f1771fa51","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-05-08 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC13G6.15c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34791222","title":"Segregating Complete Tf2 Elements Are Largely Neutral in Fission Yeast.","citation":"Genome Biol Evol 2021 Nov 05;13(11)","abstract":"Transposable elements (TEs) comprise a large proportion of the eukaryote genomes. Yet it remains poorly understood how TEs influence the fitness of the hosts carrying them. Here, we empirically test the impact of TEs on the host fitness in the fission yeast Schizosaccharomyces pombe. We find that two families of TEs (Tf1 and Tf2 elements), both of which belong to long terminal repeat retrotransposons, are highly polymorphic among individual S. pombe strains. Only 13 complete Tf2 elements are identified in S. pombe laboratory strain 972. These 13 Tf2 elements integrated into host genomes in very recent time and are segregating within the S. pombe population. Through knocking out each of the 13 Tf2 elements in S. pombe strain 972, we find Tf2 knockout does not affect the host fitness, and Tf2 elements do not alter the expression of nearby genes. Challenged by diverse forms of stress, the Tf2 knockout strains do not exhibit different growth rates from wild-type strain. Together, we conclude that segregating complete Tf2 elements insertions are largely neutral to host fitness in the fission yeast. Our study provides genome-wide empirical support for the selfish nature of TEs in fission yeast.","doi":"10.1093/gbe/evab254","authors":"Wang Y, Wang Q, Wu Z, Han GZ","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"05 Nov 2021","pubmed_entrez_date":"2021-11-18","publication_year":"2021","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2021-11-20 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11741288","title":"Pleckstrin homology domain interacts with Rkp1/Cpc2, a RACK1 homolog, to modulate Pck2-mediated signaling process in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2001 Dec 21;289(5):987-92","abstract":"Rkp1/Cpc2, a fission yeast RACK1 homolog, interacts with Pck2, a PKC homolog, and is involved in the regulation of pck2-mediated signaling process. The N-terminal region of split pleckstrin homology domain (nPH) in human PLC-gamma1 bound to Rkp1/Cpc2 concomitantly with Pck2. nPH inhibited kinase activity of GST-Pck2 purified from Schizosaccharomyces pombe in vitro. The lethality induced by pck2(+) overexpression was suppressed by coexpression of either rkp1(+) or nPH domain. This result suggests that Rkp1/Cpc2 interacts with PH domain-containing protein and regulates the Pck2-mediated signaling process in S. pombe.","authors":"Won M, Jang YJ, Chung KS, Kim DU, Hoe KL, Han MY, Kim HB, Lee SH, Oh HW, Yoo HS","authors_abbrev":"Won M et al.","pubmed_publication_date":"21 Dec 2001","pubmed_entrez_date":"2001-12-14","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31777937","title":"A novel 5'-hydroxyl dinucleotide hydrolase activity for the DXO/Rai1 family of enzymes.","citation":"Nucleic Acids Res 2020 Jan 10;48(1):349-358","abstract":"Modifications at the 5'-end of RNAs play a pivotal role in determining their fate. In eukaryotes, the DXO/Rai1 family of enzymes removes numerous 5'-end RNA modifications, thereby regulating RNA turnover. Mouse DXO catalyzes the elimination of incomplete 5'-end caps (including pyrophosphate) and the non-canonical NAD+ cap on mRNAs, and possesses distributive 5'-3' exoribonuclease activity toward 5'-monophosphate (5'-PO4) RNA. Here, we demonstrate that DXO also catalyzes the hydrolysis of RNAs bearing a 5'-hydroxyl group (5'-OH RNA). The crystal structure of DXO in complex with a 5'-OH RNA substrate mimic at 2.0 Å resolution provides elegant insight into the molecular mechanism of this activity. More importantly, the structure predicts that DXO first removes a dinucleotide from 5'-OH RNA. Our nuclease assays confirm this prediction and demonstrate that this 5'-hydroxyl dinucleotide hydrolase (HDH) activity for DXO is higher than the subsequent 5'-3' exoribonuclease activity for selected substrates. Fission yeast Rai1 also has HDH activity although it does not have 5'-3' exonuclease activity, and the Rat1-Rai1 complex can completely degrade 5'-OH RNA. An Arabidopsis DXO1 variant is active toward 5'-OH RNA but prefers 5'-PO4 RNA. Collectively, these studies demonstrate the diverse activities of DXO/Rai1 and expands the collection of RNA substrates that can undergo 5'-3' mediated decay.","doi":"10.1093/nar/gkz1107","authors":"Doamekpor SK, Gozdek A, Kwasnik A, Kufel J, Tong L","authors_abbrev":"Doamekpor SK et al.","pubmed_publication_date":"10 Jan 2020","pubmed_entrez_date":"2019-11-29","publication_year":"2020","canto_session_key":"5029f97c642fcc70","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-06-25 10:10:53","canto_approved_date":"2025-09-03 20:52:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-06-25 10:10:47","canto_added_date":"2019-11-30 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-06-25"},{"uniquename":"PMID:11752617","title":"Application of the chromatin immunoprecipitation method to identify in vivo protein-DNA associations in fission yeast.","citation":"Sci STKE 2000 Oct 31;2000(56):pl1","abstract":"The chromatin immunoprecipitation (ChIP) method provides an ideal tool for detecting direct or indirect interactions between proteins of interest and DNAs with known sequences. Here, we introduce the ChIP protocol used in our laboratory to identify in vivo protein-DNA association in the fission yeast Schizosaccharomyces pombe. The cytological and genetic merits of the fission yeast for studying control of the eukaryotic cell cycle and chromosome dynamics are reinforced by application of this ChIP method.","authors":"Takahashi K, Saitoh S, Yanagida M","authors_abbrev":"Takahashi K et al.","pubmed_publication_date":"31 Oct 2000","pubmed_entrez_date":"2001-12-26","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12724426","title":"Role for the fission yeast RecQ helicase in DNA repair in G2.","citation":"Mol Cell Biol 2003 May;23(10):3692-705","abstract":"Members of the RecQ helicase subfamily are mutated in several human genomic instability syndromes, such as Bloom, Werner, and Rothmund-Thomson syndromes. We show that Rqh1, the single Schizosaccharomyces pombe homologue, is a 3'-to-5' helicase and exists with Top3 in a high-molecular-weight complex. top3 deletion is inviable, and this is suppressed by concomitant loss of rqh1 helicase activity or loss of recombination functions. This is consistent with RecQ helicases in other systems. By using epistasis analysis of the UV radiation sensitivity and by analyzing the kinetics of Rhp51 (Rad51 homologue), Rqh1, and Top3 focus formation in response to UV in synchronized cells, we identify the first evidence of a function for Rqh1 and Top3 in the repair of UV-induced DNA damage in G(2). Our data provide evidence that Rqh1 functions after Rad51 focus formation during DNA repair. We also identify a function for Rqh1 upstream of recombination in an Rhp18-dependent (Rad18 homologue) pathway. The model that these data allow us to propose helps to reconcile different interpretations of RecQ family helicase function that have arisen between work based on the S. pombe system and models based on studies of Saccharomyces cerevisiae SGS1 suggesting that RecQ helicases act before Rad51.","authors":"Laursen LV, Ampatzidou E, Andersen AH, Murray JM","authors_abbrev":"Laursen LV et al.","pubmed_publication_date":"May 2003","pubmed_entrez_date":"2003-05-02","publication_year":"2003","canto_session_key":"55c12e425ccc4499","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-12-01 11:34:14","canto_approved_date":"2021-02-28 10:56:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-13 10:24:52","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":52,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.03c","SPAC1952.07","SPAC2G11.12","SPAC15A10.03c","SPBC16G5.12c","SPAC30D11.10","SPAC9E9.08","SPBC1734.06","SPCC18B5.11c","SPBC19C7.09c","SPBC216.05","SPAC644.14c"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2016-12-01"},{"uniquename":"PMID:7834739","title":"MAP kinase pathways in yeast: for mating and more.","citation":"Cell 1995 Jan 27;80(2):187-97","abstract":"","authors":"Herskowitz I","authors_abbrev":"Herskowitz I","pubmed_publication_date":"27 Jan 1995","pubmed_entrez_date":"1995-01-27","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12521307","title":"Regulation of septation and cytokinesis during resumption of cell division requires uvi31+, a UV-inducible gene of fission yeast.","citation":"Mol Cells 2002 Dec 31;14(3):425-30","abstract":"uvi31+ is a sequence homolog of Escherichia coli bolA gene in Schizosaccharomyces pombe, identified as a UV-inducible gene. Here, the cellular function of uvi31+ was investigated by null mutant analysis. Deletion of uvi31+ led to a delayed germination of spore and defects in subsequent cell division. However, the uvi31 mutant cell proliferated faster with smaller cell size than the wild-type cell during vegetative growth. In addition, the uvi31 mutant was sensitive to UV-light. It showed a normal cell cycle delay after UV-irradiation but displayed aberrant septum formation and defective cytokinesis when released from the UV damage checkpoint. These results suggest that uvi31+ may be involved in control of cell division, especially during the resumption from cell cycle arrest.","authors":"Kim MJ, Kim HS, Lee JK, Lee CB, Park SD","authors_abbrev":"Kim MJ et al.","pubmed_publication_date":"31 Dec 2002","pubmed_entrez_date":"2003-01-11","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16E9.06c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:24313451","title":"Deubiquitinating activity of Sdu1, a putative member of the PPPDE peptidase family, in Schizosaccharomyces pombe.","citation":"Can J Microbiol 2013 Dec;59(12):789-96","abstract":"The Schizosaccharomyces pombe sdu⁺ gene encoding a putative member of the PPPDE (Permuted Papain fold Peptidases of DsRNA viruses and Eukaryotes) superfamily was cloned into an Escherichia coli - yeast shuttle vector pRS316, resulting in the recombinant plasmid pYSTP. The determined nucleotide sequence carries 1207 bp, which would encode a protein of 201 amino acid residues. The S. pombe cells harboring pYSTP contained higher sdu1⁺ mRNA and deubiquitinating activity levels than the vector control cells, indicating that the sdu1⁺ gene is functioning. They exhibited a better growth in normal rich medium than the vector control cells. When shifted into the fresh medium containing hydrogen peroxide, menadione, or sodium nitroprusside, the S. pombe cells harboring pYSTP were able to grow reasonably well, while the growth of the vector control cells was arrested. The reactive oxygen species and total glutathione levels of the S. pombe cells harboring pYSTP were lower and higher than those of the vector control cells under the same stressful conditions, respectively. They exhibited a lower nitric oxide level than the vector control cells when subjected to sodium nitroprusside. Taken together, the sdu1⁺ gene encodes an actual protein having deubiquitinating activity and is involved in the response against oxidative and nitrosative stresses in S. pombe.","doi":"10.1139/cjm-2013-0453","authors":"Kim Y, Jo H, Lim CJ","authors_abbrev":"Kim Y et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-12-10","publication_year":"2013","canto_session_key":"fe724bae9eef58f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-29 15:48:40","canto_approved_date":"2024-02-20 15:11:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-24 14:35:39","canto_added_date":"2014-02-13 16:20:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPYUG7.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-06-29"},{"uniquename":"PMID:22846459","title":"HINT: High-quality protein interactomes and their applications in understanding human disease.","citation":"BMC Syst Biol 2012 Jul 30;6:92","abstract":"A global map of protein-protein interactions in cellular systems provides key insights into the workings of an organism. A repository of well-validated high-quality protein-protein interactions can be used in both large- and small-scale studies to generate and validate a wide range of functional hypotheses.\nWe develop HINT (http://hint.yulab.org) - a database of high-quality protein-protein interactomes for human, Saccharomyces cerevisiae, Schizosaccharomyces pombe, and Oryza sativa. These were collected from several databases and filtered both systematically and manually to remove low-quality/erroneous interactions. The resulting datasets are classified by type (binary physical interactions vs. co-complex associations) and data source (high-throughput systematic setups vs. literature-curated small-scale experiments). We find strong sociological sampling biases in literature-curated datasets of small-scale interactions. An interactome without such sampling biases was used to understand network properties of human disease-genes - hubs are unlikely to cause disease, but if they do, they usually cause multiple disorders.\nHINT is of significant interest to researchers in all fields of biology as it addresses the ubiquitous need of having a repository of high-quality protein-protein interactions. These datasets can be utilized to generate specific hypotheses about specific proteins and/or pathways, as well as analyzing global properties of cellular networks. HINT will be regularly updated and all versions will be tracked.","doi":"10.1186/1752-0509-6-92","authors":"Das J, Yu H","authors_abbrev":"Das J et al.","pubmed_publication_date":"30 Jul 2012","pubmed_entrez_date":"2012-08-01","publication_year":"2012","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21093791","title":"Gene regulation: global transcription rates scale with size.","citation":"Curr Biol 2010 Nov 23;20(22):R979-81","abstract":"Is bigger better? Scientists have long puzzled over the potential relationship between cell size and the rate of mRNA production. A recent report builds a strong case that global transcription rates scale with size.","doi":"10.1016/j.cub.2010.09.064","authors":"Dungrawala H, Manukyan A, Schneider BL","authors_abbrev":"Dungrawala H et al.","pubmed_publication_date":"23 Nov 2010","pubmed_entrez_date":"2010-11-25","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8665904","title":"Enzymic characterization of fission yeast farnesyl transferase: recognition of the -CAAL motif at the C-terminus.","citation":"Eur J Biochem 1996 Mar 15;236(3):847-51","abstract":"The enzyme farnesyl transferase (FTase) catalyzes the posttranslational modification of Ras and other Ras family proteins with a C15 farnesyl group. The target proteins have a consensus -CAAX motif (X, any amino acid except leucine) at the C-terminus. Since proteins that have leucine as the C-terminal amino acid X are modified with a C20 geranylgeranyl group, it is thought that the C-terminal leucine is the signal (-CAAL motif) for selection of isoprenoid molecules. Here, we report the presence of multiple FTase activities in the fission yeast Schizosaccharomyces pombe, each seeming to correspond to a particular protein known to be modified by the farnesyl group in vivo. Using enzymic activities specific to S. pombe Ras1, we found similar affinities for FTases in the wild-type (EVSTKCCVIC) and mutant Ras1 peptide, in which the C-terminal amino acid is replaced by leucine (EVSTKCCVIL). These results suggest that recognition and selection of the correct isoprenoid group by the FTases require other amino acid sequences of the target protein in addition to the C-terminal -CAAX motif.","authors":"Danjoh I, Fujiyama A","authors_abbrev":"Danjoh I et al.","pubmed_publication_date":"15 Mar 1996","pubmed_entrez_date":"1996-03-15","publication_year":"1996","canto_session_key":"beb039c2f820770d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-06-28 23:08:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-28 23:07:54","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1A10.04c","SPAC17G6.04c"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2016-06-28"},{"uniquename":"EMBL:SPO6032","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21576223","title":"Ultrafine anaphase bridges, broken DNA and illegitimate recombination induced by a replication fork barrier.","citation":"Nucleic Acids Res 2011 Aug;39(15):6568-84","abstract":"Most DNA double-strand breaks (DSBs) in S- and G2-phase cells are repaired accurately by Rad51-dependent sister chromatid recombination. However, a minority give rise to gross chromosome rearrangements (GCRs), which can result in disease/death. What determines whether a DSB is repaired accurately or inaccurately is currently unclear. We provide evidence that suggests that perturbing replication by a non-programmed protein-DNA replication fork barrier results in the persistence of replication intermediates (most likely regions of unreplicated DNA) into mitosis, which results in anaphase bridge formation and ultimately to DNA breakage. However, unlike previously characterised replication-associated DSBs, these breaks are repaired mainly by Rad51-independent processes such as single-strand annealing, and are therefore prone to generate GCRs. These data highlight how a replication-associated DSB can be predisposed to give rise to genome rearrangements in eukaryotes.","doi":"10.1093/nar/gkr340","authors":"Sofueva S, Osman F, Lorenz A, Steinacher R, Castagnetti S, Ledesma J, Whitby MC","authors_abbrev":"Sofueva S et al.","pubmed_publication_date":"Aug 2011","pubmed_entrez_date":"2011-05-18","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40750456","title":"Construction of a heterologous protein secretion system using the protein disulfide isomerase Pdi1p in Schizosaccharomycespombe.","citation":"J Biosci Bioeng 2025 Jul 31;","abstract":"The fission yeast Schizosaccharomyces pombe has been often used as a host for heterologous protein production; however, a method for extracellular secretion of heterologous protein would be advantageous for ease of purification and for native protein structure. In a previous study, overexpression of endogenous protein disulfide isomerase (PDI) genes improved the secretion of recombinant human transferrin in S. pombe. In the present study, we have explored whether Pdi1 can be used for the secretion of heterologous proteins in S. pombe. Overexpression of a fusion protein of Pdi1p and the heterologous protein EGFP (Pdi1p-EGFP), in the host S. pombe A8 strain, which lacks eight intracellular and extracellular proteases, resulted in efficient extracellular secretion of the fusion protein. To identify the optimal region of Pdi1p for use as an extracellular carrier, we compared the secretion of EGFP fused to the N-terminal Pdi1p signal domain and deletion mutants of Pdi1p. The signal sequence alone did not improve secretion, but deletion of two domains at the C-terminus did improve secretion. Notably, the x domain was important for secretion of the fusion protein. As a result of these findings, we have established a system for efficient secretion of target heterologous proteins by using optimally designed Pdi1p as a carrier for extracellular secretion.","doi":"10.1016/j.jbiosc.2025.07.003","authors":"Tominaga A, Kotani T, Watanabe M, Takegawa K","authors_abbrev":"Tominaga A et al.","pubmed_publication_date":"31 Jul 2025","pubmed_entrez_date":"2025-08-01","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-08-02 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9608944","title":"[Exon-intron organization rpb10+ and rpc10+ genes of Schizosaccharomyces pombe, coding for mini-subunits of nuclear RNA-polymerase I-III].","citation":"Mol Biol (Mosk) 1998;32(2):285-90","abstract":"","authors":"Shpakovskiĭ GV, Proshkin SA, Lebedenko EN","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-06-03","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8988253","title":"Mitochondrial distribution and inheritance.","citation":"Experientia 1996 Dec 15;52(12):1111-6","abstract":"Mechanisms mediating the inheritance of mitochondria are poorly understood, but recent studies with the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe have begun to identify components that facilitate this essential process. These components have been identified through the analysis of conditional yeast mutants that display aberrant mitochondrial distribution at restrictive conditions. The analysis of these mutants has uncovered several novel proteins that are localized either to cytoskeletal structures or to the mitochondria themselves. Many mitochondrial inheritance mutants also show altered mitochondrial morphology and defects in maintenance of the mitochondrial genome. Although some inheritance components and mechanisms appear to function specifically in certain types of cells, other conserved proteins are likely to mediate mitochondrial behavior in all eukaryotic cells.","authors":"Berger KH, Yaffe MP","authors_abbrev":"Berger KH et al.","pubmed_publication_date":"15 Dec 1996","pubmed_entrez_date":"1996-12-15","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"InterPro:IPR019558","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:12566","HGNC:23149","HGNC:23150","HGNC:948","SPAC11E3.02c","HGNC:23147"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25822347","title":"Role of swi7H4 mutant allele of DNA polymerase α in the DNA damage checkpoint response.","citation":"PLoS One 2015;10(3):e0124063","abstract":"Besides being a mediator of initiation of DNA replication, DNA polymerase α plays a key role in chromosome maintenance. Swi7H4, a novel temperature sensitive mutant of DNA polymerase α was shown to be defective in transcriptional silencing at the mating type centromere and telomere loci. It is also required for the establishment of chromatin state that can recruit the components of the heterochromatin machinery at these regions. Recently the role of DNA polymerase α in the S-phase alkylation damage response in S. pombe has also been studied. Here we investigate whether defects generated by swi7H4, a mutant allele of DNA polymerase α can activate a checkpoint response. We show that swi7H4 exhibit conditional synthetic lethality with chk1 null mutant and the double mutant of swi7H4 with chk1 deletion aggravate the chromosome segregation defects. More importantly swi7H4 mutant cells delay the mitotic progression at non permissive temperature that is mediated by checkpoint protein kinase Chk1. In addition we show that, in the swi7H4 mutant background, cells accumulate DNA damage at non permissive temperature activating the checkpoint kinase protein Chk1. Further, we observed synthetic lethality between swi7H4 and a number of genes involved in DNA repair pathway at semi permissive temperature. We summarize that defects in swi7H4 mutant results in DNA damage that delay mitosis in a Chk1 dependent manner that also require the damage repair pathway for proper recovery.","doi":"10.1371/journal.pone.0124063","authors":"Khan S, Ahmed S","authors_abbrev":"Khan S et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-03-31","publication_year":"2015","canto_session_key":"09f664bfd80469a8","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-04-01 00:18:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPCC1259.13","SPAC3H5.06c","SPAC644.14c","SPAC2G11.12"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:15550243","title":"Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage.","citation":"Cell 2004 Nov 24;119(5):603-14","abstract":"Histone lysine methylation is a key regulator of gene expression and heterochromatin function, but little is known as to how this modification impinges on other chromatin activities. Here we demonstrate that a previously uncharacterized SET domain protein, Set9, is responsible for H4-K20 methylation in the fission yeast Schizosaccharomyces pombe. Surprisingly, H4-K20 methylation does not have any apparent role in the regulation of gene expression or heterochromatin function. Rather, we find the modification has a role in DNA damage response. Loss of Set9 activity or mutation of H4-K20 markedly impairs cell survival after genotoxic challenge and compromises the ability of cells to maintain checkpoint mediated cell cycle arrest. Genetic experiments link Set9 to Crb2, a homolog of the mammalian checkpoint protein 53BP1, and the enzyme is required for Crb2 localization to sites of DNA damage. These results argue that H4-K20 methylation functions as a \"histone mark\" required for the recruitment of the checkpoint protein Crb2.","authors":"Sanders SL, Portoso M, Mata J, Bähler J, Allshire RC, Kouzarides T","authors_abbrev":"Sanders SL et al.","pubmed_publication_date":"24 Nov 2004","pubmed_entrez_date":"2004-11-20","publication_year":"2004","canto_session_key":"2b924b1ab23dde19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-03-31 08:05:19","canto_approved_date":"2026-02-09 10:12:02","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-21 17:33:46","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":44,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.05","SPCC18B5.11c","SPBC428.08c","SPBP8B7.07c","SPAC1834.03c","SPBC342.05","SPBC8D2.04","SPBC1105.12","SPCC1739.05","SPBC8D2.03c","SPCC1259.13","SPCC4B3.12","SPCC297.04c","SPCC306.04c","SPAC1834.04","SPAC29B12.02c","SPAC694.06c","SPBC1105.11c"],"gene_count":18,"ltp_gene_count":13,"approved_date":"2024-03-31"},{"uniquename":"PMID:38909706","title":"Structure-activity relationship study of nitrogen signaling factors.","citation":"Bioorg Med Chem Lett 2024 Jun 21;:129857","abstract":"We have synthesized 10 analogs of oxylipins, which are nitrogen signaling factors (NSFs) that mediate cell-to-cell communication in the fission yeast Schizosaccharomyces pombe, and evaluated their structure-activity relationships with the aim of developing molecular probes for NSFs. We found that the OH or OAc group at C10 could be replaced with a compact amide (17) or carbamate (19). Introducing an alkyne as a detection tag at C10 led to decreased, though still sufficient, activity. Introducing an alkyne at the C18 position showed a similar trend, suggesting tolerance is relatively low even for compact functional groups such as alkynes. Although introduction of a diazirine moiety as a photoreactive group at the C5 position decreased the activity, we found that introducing diazirine at the C13 position was acceptable, and compound 38 exhibited potent NSF activity. These findings will be helpful in the development of molecular probes for NSFs.","doi":"10.1016/j.bmcl.2024.129857","authors":"Matoba H, Oba K, Li H, Mizuno Y, Wang Q, Yoritate M, Aso M, Sodeoka M, Yoshida M, Yashiroda Y, Hirai G","authors_abbrev":"Matoba H et al.","pubmed_publication_date":"21 Jun 2024","pubmed_entrez_date":"2024-06-23","publication_year":"2024","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2024-06-24 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15976807","title":"Comprehensive analysis of heterochromatin- and RNAi-mediated epigenetic control of the fission yeast genome.","citation":"Nat Genet 2005 Aug;37(8):809-19","abstract":"The organization of eukaryotic genomes into distinct structural and functional domains is important for the regulation and transduction of genetic information. Here, we investigated heterochromatin and euchromatin profiles of the entire fission yeast genome and explored the role of RNA interference (RNAi) in genome organization. Histone H3 methylated at Lys4, which defines euchromatin, was not only distributed across most of the chromosomal landscape but was also present at the centromere core, the site of kinetochore assembly. In contrast, histone H3 methylated at Lys9 and its interacting protein Swi6/HP1, which define heterochromatin, coated extended domains associated with a variety of repeat elements and small islands corresponding to meiotic genes. Notably, RNAi components were distributed throughout all these heterochromatin domains, and their localization depended on Clr4/Suv39h histone methyltransferase. Sequencing of small interfering RNAs (siRNAs) associated with the RITS RNAi effector complex identified hot spots of siRNAs, which mapped to a diverse array of elements in these RNAi-heterochromatin domains. We found that Clr4/Suv39h predominantly silenced repeat elements whose derived transcripts, transcribed mainly by RNA polymerase II, serve as a source for siRNAs. Our analyses also uncover an important role for the RNAi machinery in maintaining genomic integrity.","authors":"Cam HP, Sugiyama T, Chen ES, Chen X, FitzGerald PC, Grewal SI","authors_abbrev":"Cam HP et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-06-25","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.84","SPNCRNA.95"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"EMBL:AU007706","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPPTC1X","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7565591","title":"Gene regulation by antisense RNA in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1995 Aug 21;248(3):293-300","abstract":"This report describes experiments designed to demonstrate the suitability of the fission yeast Schizosaccharomyces pombe as a host for antisense RNA regulation. A lacZ gene-expressing yeast strain was constructed and used as a host for the expression of a series of antisense RNAs complementary to various regions of the target lacZ mRNA. All lacZ antisense genes were placed under control of the thiamine-repressible nmt1 promoter of S. pombe and expressed from episomal plasmids. For each antisense plasmid a corresponding sense control plasmid was constructed. All lacZ antisense genes were shown to express antisense RNAs of the expected size at equivalent steady-state levels. beta-Galactosidase activity in transformed cells expressing the long, short 5' or short 3' lacZ antisense RNAs was shown to be reduced by 45%, 20%, and 10%, respectively, relative to control transformants. Further experiments indicated that antisense RNA regulation in this system was conditional and reversible, with the observed reduction of beta-galactosidase activity being dependent on the transcription of lacZ antisense RNA. Our results represent the first successful example of antisense RNA regulation of gene expression in yeast and establish S. pombe as an experimental model for the biochemical analysis of antisense RNA regulation.","authors":"Arndt GM, Atkins D, Patrikakis M, Izant JG","authors_abbrev":"Arndt GM et al.","pubmed_publication_date":"21 Aug 1995","pubmed_entrez_date":"1995-08-21","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8668131","title":"Cloning by functional complementation, and inactivation, of the Schizosaccharomyces pombe homologue of the Saccharomyces cerevisiae gene ABC1.","citation":"Mol Gen Genet 1996 May 23;251(2):204-10","abstract":"The Saccharomyces cerevisiae gene ABC1 is required for the correct functioning of the bc1 complex of the mitochondrial respiratory chain. By functional complementation of a S. cerevisiae abc1(-) mutant, we have cloned a Schizosaccharomyces pombe cDNA, whose predicted product is 50% identical to the Abc1 protein. Significant homology is also observed with bacterial, nematode, and even human amino acid sequences of unknown function, suggesting that the Abc1 protein is conserved through evolution. The cloned cDNA corresponds to a single S. pombe gene abc1Sp, located on chromosome II, expression of which is not regulated by the carbon source. Inactivation of the abc1Sp gene by homologous gene replacement causes a respiratory deficiency which is efficiently rescued by the expression of the S. cerevisiae ABC1 gene. The inactivated strain shows a drastic decrease in the bc1 complex activity. a decrease in cytochrome aa3 and a slow growth phenotype. To our knowledge, this is the first example of the inactivation of a respiratory gene in S. pombe. Our results highlight the fact that S. pombe growth is highly dependent upon respiration, and that S. pombe could represent a valuable model for studying nucleo-mitochondrial interactions in higher eukaryotes.","authors":"Bonnefoy N, Kermorgant M, Brivet-Chevillotte P, Dujardin G","authors_abbrev":"Bonnefoy N et al.","pubmed_publication_date":"23 May 1996","pubmed_entrez_date":"1996-05-23","publication_year":"1996","canto_session_key":"b74b5e273e9ba8f0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-05-02 16:22:00","canto_approved_date":"2025-05-19 08:34:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-24 08:53:46","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.18"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-02"},{"uniquename":"PMID:11707530","title":"Isolation and characterization of the Pin1/Ess1p homologue in Schizosaccharomyces pombe.","citation":"J Cell Sci 2001 Oct;114(Pt 20):3779-88","abstract":"Pin1/Ess1p is a highly conserved WW domain-containing peptidyl-prolyl isomerase (PPIase); its WW domain binds specifically to phospho-Ser/Thr-Pro sequences and its catalytic domain isomerizes phospho-Ser/Thr-Pro bonds. Pin1 PPIase activity can alter protein conformation in a phosphorylation-dependent manner and/or promote protein dephosphorylation. Human Pin1 interacts with mitotic phosphoproteins, such as NIMA, Cdc25 and Wee1, and inhibits G(2)/M progression in Xenopus extracts. Depletion of Pin1 in HeLa cells and deletion of ESS1 in S. cerevisiae result in mitotic arrest. In addition, Pin1/Ess1p play roles in transcription in S. cerevisiae and in mammalian somatic cells. The S. pombe genome sequence has an open reading frame (ORF) that has 47% identity with Pin1. Expression of this ORF rescued the growth defect caused by ess1 deletion in S. cerevisiae, indicating that S. pombe Pin1p is a functional Pin1 homologue. Overexpression of pin1(+) in S. pombe caused slow growth and a G(1) delay. Deletion of pin1(+) (pin1 Delta) did not affect cell cycle progression or cell growth, but increased sensitivity to the cyclophilin inhibitor, cyclosporin A, suggesting that cyclophilin family PPIases have overlapping functions with the Pin1p PPIase. Deletion of pin1(+) did not affect the DNA replication checkpoint, but conferred a modest increase in UV sensitivity. Furthermore, the pin1 Delta allele caused a synthetic growth defect when combined with either cdc25-22 or wee1-50 but not the cdc24-1 temperature-sensitive mutant. The pin1 Delta strain showed increased sensitivity to the PP1/PP2A family phosphatase inhibitor, okadaic acid, suggesting that Pin1p plays a role in protein dephosphorylation as a result of its ability to increase the population of phospho-Ser/Thr-Pro peptide bonds in the trans conformation that is required for PP2A-mediated dephosphorylation. Our genetic data also suggest that Pin1p might function as a positive regulator of Cdc25p and Wee1p.","authors":"Huang HK, Forsburg SL, John UP, O'Connell MJ, Hunter T","authors_abbrev":"Huang HK et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-11-15","publication_year":"2001","canto_session_key":"5b00ac57e2eaf984","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-02 16:44:10","canto_approved_date":"2019-06-14 12:44:46","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-23 13:11:55","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19E9.02","SPCC18B5.03","SPBC216.05","SPBC336.12c","SPAC24H6.05","SPCC16C4.03"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-06-02"},{"uniquename":"PMID:17077120","title":"Pom1 kinase links division plane position to cell polarity by regulating Mid1p cortical distribution.","citation":"J Cell Sci 2006 Nov 15;119(Pt 22):4710-8","abstract":"In fission yeast, Mid1p, a major determinant for division plane position, defines a medial cortical compartment where it recruits myosin II at the onset of mitosis to initiate contractile ring assembly. How Mid1p is restricted to the medial cortex is unknown. We report here that in a pom1 polarity mutant, which displays a monopolar growth pattern, Mid1p distribution expands towards the non-growing cell tip, uncoupling Mid1p localization from nuclear position. This accounts for the displacement of the contractile ring during mitosis. By contrast, Mid1p localization is normal in a bud6Delta strain, indicating that Mid1p misdistribution is not a general consequence of monopolar growth. We conclude that Pom1 kinase acts as a negative regulator of Mid1p distribution, excluding Mid1p from non-growing ends, whereas a Pom1-independent mechanism prevents Mid1p association with growing ends. Our work therefore provides evidence that cell polarity regulators influence the distribution of Mid1p, linking division plane position to cell polarity.","authors":"Celton-Morizur S, Racine V, Sibarita JB, Paoletti A","authors_abbrev":"Celton-Morizur S et al.","pubmed_publication_date":"15 Nov 2006","pubmed_entrez_date":"2006-11-02","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3023070","title":"The nucleotide sequence of the fission yeast DNA topoisomerase II gene: structural and functional relationships to other DNA topoisomerases.","citation":"EMBO J 1986 Sep;5(9):2355-61","abstract":"We have determined the complete nucleotide sequence of a 5.3-kb long genomic DNA fragment of the fission yeast Schizosaccharomyces pombe that encodes DNA topoisomerase II. It contains a 4293 bp long single open reading frame. The predicted polypeptide has 1431 residues (mol. wt 162,000) and shows three characteristic domains; the large C-terminal region, which consists of alternating acidic-basic stretches and might be a chromatin-binding domain, the NH2 half domain homologous to the ATP-binding gyrB subunit of bacterial gyrase and the central-to-latter part which is homologous to the NH2 domain of the catalytic gyrA subunit, suggesting a possible evolutionary consequence of the gene fusion of the bacterial gyrase subunits into the eucaryotic DNA topoisomerase II gene. We have found that the cloned fission yeast TOP2 gene can complement the budding yeast top2 mutation, although the fission yeast TOP2 protein sequence is only 50% homologous to the recently determined sequence of budding yeast (J.C. Wang, personal communication). Conversely, the budding yeast TOP2 gene can complement the fission yeast top2 mutations, indicating that their DNA topoisomerase II genes are functionally exchangeable.","authors":"Uemura T, Morikawa K, Yanagida M","authors_abbrev":"Uemura T et al.","pubmed_publication_date":"Sep 1986","pubmed_entrez_date":"1986-09-01","publication_year":"1986","canto_session_key":"68526ba93fd36e45","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-09-25 13:40:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-24 13:26:17","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1A4.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-09-24"},{"uniquename":"PMID:12907709","title":"Rpb7 subunit of RNA polymerase II interacts with an RNA-binding protein involved in processing of transcripts.","citation":"Nucleic Acids Res 2003 Aug 15;31(16):4696-701","abstract":"Rpb4-Rpb7, a dissociable subcomplex of RNA polymerase II (pol II), is required for transcription initiation. To understand the role of Rpb7 in transcription initiation or other processes in transcription, we carried out a two-hybrid screen for proteins that interact with Rpb7 of the fission yeast Schizosaccharomyces pombe. The screen identified the S.pombe homolog of the Saccharomyces cerevisiae Nrd1, an RNA-binding protein implicated in 3' end formation of small nucleolar and small nuclear RNAs transcribed by pol II. The S.pombe protein, named Seb1 for seven binding, was essential for cell viability, and bound directly to Rpb7 in vitro. Saccharomyces cerevisiae Rpb7 also interacted with Nrd1, indicating that the interaction is conserved in evolution. Glu166 and/or Asp167 of S.pombe Rpb7, residues near the C-terminus of the 172 amino acid protein, were found to be important for its interaction with Seb1. Our results suggest that Rpb7 may function to anchor a processing factor to the pol II apparatus, thereby coupling RNA processing to transcription. The role for Rpb7 is consistent with its location in the pol II complex determined by recent structural studies.","authors":"Mitsuzawa H, Kanda E, Ishihama A","authors_abbrev":"Mitsuzawa H et al.","pubmed_publication_date":"15 Aug 2003","pubmed_entrez_date":"2003-08-09","publication_year":"2003","canto_session_key":"65e9ada10beab310","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-08-01 15:47:14","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-01 15:47:07","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPACUNK4.06c","SPAC222.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-08-01"},{"uniquename":"PMID:18948703","title":"The meiotic recombination hotspots of Schizosaccharomyces pombe.","citation":"Genome Dyn 2009;5:1-13","abstract":"Meiotic recombination predominantly occurs at genomic loci referred to as recombination hotspots. The fission yeast, Schizosaccharomyces pombe, has proved to be an excellent model organism in which to study details of the molecular basis of meiotic recombination hotspot activation. S. pombe has a number of different classes of meiotic hotspots, indicating that a single pathway does not confer hotspot activity throughout the genome. The M26-related hotspots are a particularly well characterised group of hotspots and details of the molecular activation of M26-related hotspots are now coming to light. Moreover, genome-wide DNA array analysis has been applied to the question of meiotic recombination in this organism and we are now starting to get a picture of recombination hotspot distribution on a genome-wide scale.","doi":"10.1159/000166614","authors":"Pryce DW, McFarlane RJ","authors_abbrev":"Pryce DW et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2008-10-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10102365","title":"Isolation of multicopy suppressors of the calcium sensitivity of a mutant lacking the bZIP transcription factor Atf1 in fission yeast.","citation":"Mol Gen Genet 1999 Mar;261(2):297-306","abstract":"In Schizosaccharomyces pombe, recent studies have uncovered a set of putative transcription factors of the basic leucine zipper (bZIP) type (e.g., Atf1, Pcr1, Pap1), which function downstream of the Sty1 mitogen-activated protein kinase (MAPK) cascade which is involved in stress-activated signal transduction. Accordingly, a delta atf1 mutant is known to exhibit osmosensitivity for growth, since one of the targets of Atf1 is the gpd1+ gene, which is responsible for the osmoadaptive glycerol production mediated by the Sty1 MAPK cascade. During the course of our studies on the osmotic response in S. pombe, we found that growth of a delta atf1 mutant is highly sensitive to the level of Ca2+ ions in the medium (but less sensitive to Mg2+ and Na+ ions). This phenotype seemed to be relevant to the osmosensitivity, because an delta gpd1 mutant showed a similar phenotype. An attempt was therefore made to isolate multicopy suppressors of the calcium sensitivity exhibited by the delta atf1 cells. Among such suppressors were several bZIP factors, including two known proteins (Atf21 and Pcr1), and two new ones (named Atf31 and Zip1). These factors were characterized further, in comparison to Atf1, with special reference to the Sty1 MAPK signaling pathway.","authors":"Ohmiya R, Kato C, Yamada H, Aiba H, Mizuno T","authors_abbrev":"Ohmiya R et al.","pubmed_publication_date":"Mar 1999","pubmed_entrez_date":"1999-04-02","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25G10.03","SPAC22F3.02","SPBC29B5.01","SPBC2F12.09c","SPAC21E11.03c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:17074490","title":"Pombe Cdc15 homology proteins: regulators of membrane dynamics and the actin cytoskeleton.","citation":"Trends Biochem Sci 2006 Dec;31(12):670-9","abstract":"Pombe Cdc15 homology (PCH) proteins have emerged in many species as important coordinators of signalling pathways that regulate actomyosin assembly and membrane dynamics. For example, the prototype PCH protein, Cdc15p of Schizosaccharomyces pombe, has a role in assembly of the contractile ring, which is needed to separate dividing cells. Recently, mammalian PCH proteins have been found to bind phospholipids and to participate in membrane deformation. These findings suggest that PCH proteins are crucial linkers of membrane dynamics and actin polymerization, for example, during the internalization of transmembrane receptors. Intriguingly, some members of the PCH protein family are mutated in neurodegenerative and inflammatory diseases, which has implications for the identification of cures for such disorders.","authors":"Aspenström P, Fransson A, Richnau N","authors_abbrev":"Aspenström P et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-11-01","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26613727","title":"Regulation of mitochondrial inner membrane fusion: divergent evolution with similar solutions?","citation":"Curr Genet 2016 May;62(2):291-4","abstract":"Continuous mitochondrial fusion and fission define the dynamic shape of mitochondria. One essential player of mitochondrial fusion is the conserved inner membrane dynamin-like GTPase Mgm1/OPA1. Limited proteolysis of this protein has been proposed as a mechanism to separate and subsequently eliminate dysfunctional parts from the mitochondrial network. Here, I briefly summarize our current knowledge about the underlying proteolytic processing steps in mammals, baker's yeast, Schizosaccharomyces pombe, Drosophila melanogaster and Aspergillus fumigatus. The apparent great diversity in Mgm1/OPA1 processing among the analyzed species indicates a surprising mechanistic heterogeneity in the regulation of mitochondrial inner membrane fusion.","doi":"10.1007/s00294-015-0542-6","authors":"Wagener J","authors_abbrev":"Wagener J","pubmed_publication_date":"May 2016","pubmed_entrez_date":"2015-11-29","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-11-30 01:19:33","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1718.06","SPAP14E8.04","SPAC6G9.06c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:2657742","title":"Genetic analysis of Schizosaccharomyces pombe 7SL RNA: a structural motif that includes a conserved tetranucleotide loop is important for function.","citation":"Proc Natl Acad Sci U S A 1989 Jun;86(11):4137-41","abstract":"We have studied the effects of mutations in a 6-base segment of Schizosaccharomyces pombe 7SL RNA, which lies within a 35-nucleotide domain whose sequence and secondary structure are conserved in RNAs from many divergent organisms, including the 7SL component of human signal recognition particle (SRP). Surprisingly, many changes in this region can be tolerated under normal growth conditions. An exception is the lethality of several mutations at positions 159 and 160, 2 nucleotides previously shown to be protected from RNase digestion by the 19-kDa canine SRP protein. Nucleotide 160 is, in addition, the most highly conserved base in a consensus sequence for the most common tetranucleotide loop in ribosomal RNAs. Mutations that are likely to affect the stability and/or conformation of the RNA give rise to a conditional phenotype: when osmolarity of the medium is raised, the RNAs become partially or completely defective in function at high temperature.","authors":"Liao XB, Brennwald P, Wise JA","authors_abbrev":"Liao XB et al.","pubmed_publication_date":"Jun 1989","pubmed_entrez_date":"1989-06-01","publication_year":"1989","canto_session_key":"09d41e1b20ab357c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-09 14:57:26","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-09 14:57:11","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":54,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_2657742_phaf.tsv"}],"genes":["SPNCRNA.98"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-09"},{"uniquename":"PMID:19028606","title":"Functional interactions of meiotic recombination factors Rdh54 and Dmc1.","citation":"DNA Repair (Amst) 2009 Feb 01;8(2):279-84","abstract":"Genetic studies in budding and fission yeasts have provided evidence that Rdh54, a Swi2/Snf2-like factor, synergizes with the Dmc1 recombinase to mediate inter-homologue recombination during meiosis. Rdh54 associates with Dmc1 in the yeast two-hybrid assay, but whether the Rdh54-Dmc1 interaction is direct and the manner in which these two recombination factors may functionally co-operate to accomplish their biological task have not yet been defined. Here, using purified Schizosaccharomyces pombe proteins, we demonstrate complex formation between Rdh54 and Dmc1 and enhancement of the recombinase activity of Dmc1 by Rdh54. Consistent with published cytological and chromatin immunoprecipitation data that implicate Rdh54 in preventing the non-specific association of Dmc1 with chromatin, we show here that Rdh54 mediates the efficient removal of Dmc1 from dsDNA. These functional attributes of Rdh54 are reliant on its ATPase function. The results presented herein provide valuable information concerning the Rdh54-Dmc1 protein pair that is germane for understanding their role in meiotic recombination. The biochemical systems established in this study should be useful for the continuing dissection of the action mechanism of Rdh54 and Dmc1.","doi":"10.1016/j.dnarep.2008.10.012","authors":"Chi P, Kwon Y, Moses DN, Seong C, Sehorn MG, Singh AK, Tsubouchi H, Greene EC, Klein HL, Sung P","authors_abbrev":"Chi P et al.","pubmed_publication_date":"01 Feb 2009","pubmed_entrez_date":"2008-11-26","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC8E11.03c","SPAC22F3.03c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:2347311","title":"Substrate recognition by RNase P and by the catalytic M1 RNA: identification of possible contact points in pre-tRNAs.","citation":"EMBO J 1990 Jun;9(6):1929-37","abstract":"Modified bases were introduced into pre-tRNAs during in vitro RNA synthesis or by chemical modification. These RNAs were used as substrates for the catalytic M1 RNA and the RNase P holoenzyme from Schizosaccharomyces pombe. The synthetic approach permitted the insertion of 100% m7GTP into pre-tRNAs and this resulted in complete inhibition of the specific 5' processing reactions. Partially modified RNAs were obtained by chemical modifications of purines and uridines in the pre-tRNAs. This allowed detailed analyses of specific bases excluded in the products. With pre-tRNA(Ser) and initiator pre-tRNA(Met), strong effects were observed in the T arm and weaker effects in the anticodon stem. Only minor base exclusions were detected in the acceptor stem of pre-tRNA(Ser) and in the D arm of pre-tRNA(Met).","authors":"Kahle D, Wehmeyer U, Krupp G","authors_abbrev":"Kahle D et al.","pubmed_publication_date":"Jun 1990","pubmed_entrez_date":"1990-06-01","publication_year":"1990","canto_session_key":"6356759908a71ded","canto_annotation_status":"SESSION_ACCEPTED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.128"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:35286199","title":"Mitotic spindle formation in the absence of Polo kinase.","citation":"Proc Natl Acad Sci U S A 2022 Mar 22;119(12):e2114429119","abstract":"SignificanceMitosis is an essential process in all eukaryotes, but paradoxically, genes required for mitosis vary among species. The essentiality of many mitotic genes was bypassed by activating alternative mechanisms during evolution. However, bypass events have rarely been recapitulated experimentally. Here, using the fission yeast  Schizosaccharomyces pombe , the essentiality of a kinase (Plo1) required for bipolar spindle formation was bypassed by other mutations, many of which are associated with glucose metabolism. The Plo1 bypass by the reduction in glucose uptake was dependent on another kinase (casein kinase I), which potentiated spindle microtubule formation. This study illustrates a rare experimental bypass of essentiality for mitotic genes and provides insights into the molecular diversity of mitosis.","doi":"10.1073/pnas.2114429119","authors":"Kim J, Goshima G","authors_abbrev":"Kim J et al.","pubmed_publication_date":"22 Mar 2022","pubmed_entrez_date":"2022-03-14","publication_year":"2022","canto_session_key":"7db555db2a36a8e7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Gohta Goshima","canto_first_approved_date":"2022-05-31 09:13:09","canto_approved_date":"2022-06-06 16:50:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-04-13 12:25:45","canto_added_date":"2022-03-16 01:15:05","annotation_curators":[{"name":"Gohta Goshima","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null},{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":36,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.10c","SPCC548.06c","SPBC19C7.03","SPAC23C11.16","SPCC1322.12c","SPCC126.04c","SPBC25H2.11c","SPAC57A7.11","SPCC4B3.15","SPAC4D7.10c","SPBC32H8.07","SPBC428.20c","SPBC365.15","SPCC1672.06c","SPBC21.06c","SPCC1235.14","SPBC21C3.20c","SPBC106.10","SPBC3H7.15","SPAC13G6.14","SPAC7D4.03c","SPAC23C4.12"],"gene_count":22,"ltp_gene_count":20,"approved_date":"2022-05-31"},{"uniquename":"PMID:7217015","title":"Isolation of cell size mutants of a fission yeast by a new selective method: characterization of mutants and implications for division control mechanisms.","citation":"J Bacteriol 1981 May;146(2):746-54","abstract":"Previously known cell size (wee) mutations of fission yeast suppress the mitotic block caused by a defective cdc25 allele. Some 700 revertants of cdc25-22 were obtained after ultraviolet mutagenesis and selection at the restrictive temperature. Most revertants carried the original cdc25 lesion plus a mutation in or very close to the wee1 gene. Two partial wee1 mutations of a new type were found among the revertants. Two new wee mutations mapping at the cdc2 gene (cdc2-w mutants) were also obtained. The various mutations were examined for their effects on cell division size, their efficiency as cdc25 suppressors, and their dominance relations. Full wee1 mutations were found to suppress cdc25 lesions very efficiently, whereas partial wee1 mutations were poor suppressors. The cdc25 suppression ability of cdc2-w mutations was allele specific for cdc2, suggesting bifunctionality of the gene product. The wee1 mutations were recessive for cdc25 suppression; cdc2-w mutations were dominant. A model is proposed for the genetic control of mitotic timing and cell division size, in which the cdc2+ product is needed and is rate limiting for mitosis. The cdc2+ activity is inhibited by the wee1+ product, whereas the cdc25+ product relieves this inhibition.","authors":"Fantes PA","authors_abbrev":"Fantes PA","pubmed_publication_date":"May 1981","pubmed_entrez_date":"1981-05-01","publication_year":"1981","canto_session_key":"30796594bcb61414","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-06-25 13:45:56","canto_approved_date":"2024-07-04 06:38:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-25 13:45:43","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":31,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-06-25"},{"uniquename":"PMID:1525861","title":"Trans-acting factors and properly positioned DNA elements repress mating-type genes in fission yeast.","citation":"Curr Genet 1992 Apr;21(4-5):331-8","abstract":"Repression of the mating-type P genes at the silent mat2-P locus in fission yeast is dependent on four cis-acting DNA elements, two on each side of the coding sequences. The mechanism by which these elements exert their influence on the mating-type promoter is studied here by insertion of a bacterial antibiotic resistance gene at several positions in the silent region. The behavior of the resistance gene itself, and the changes its insertion causes in mating-type expression, reveal that the repressive elements have a limited range of action and that the four elements have unequal effects on gene expression. Repression of the antibiotic resistance gene inside the silent region leads to an antibiotic-sensitive phenotype and facilitates the selection of resistant mutants. These mutants can de-repress the resistance gene at other positions than the one used for their selection. Strong antibiotic resistance correlates with derepression of the plasmid-borne mating-type cassette. These data argue that mat2-P repression is dependent on trans-acting factors and the positioning of the repressive DNA elements, but less dependent on the nature of the affected promoter.","authors":"Ekwall K, Olsson T, Ruusala T","authors_abbrev":"Ekwall K et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9810469","title":"Functional analysis of domains in the Byr2 kinase.","citation":"Biochimie 1998 Jul;80(7):621-5","abstract":"The activation of mitogen-activated protein (MAP) kinase cascades by the Ras GTPase is an evolutionarily conserved signal transduction mechanism. To better understand the interaction between Ras and its target kinase, we study the yeast Schizosaccharomyces pombe where the Ras1 GTPase activates the Byr2 kinase. The Byr2 kinase contains an N-terminal regulatory region and a C-terminal kinase region. The regulatory region can be divided into a sterile-alpha motif (SAM) that binds Ste4, a Ras1-binding domain (RBD) that binds activated Ras1, and a catalytic binding domain (CBD) that interacts with the Byr2 kinase domain. To analyze the importance of functional domains of the Byr2 kinase, a biological assay was used that exploited the ability of Byr2 to partially bypass the need for Ras1 in sporulation. Analysis of mutants using this assay showed that SAM and RBD were very important for Ras1-stimulated sporulation. Three activating mutations were identified within the N-terminal lobe of the Byr2 kinase domain that partially bypassed the need for Ras1 for sporulation. These activating mutations may identify a region of the Byr2 kinase domain that interacts with the CBD since mutations in the CBD which disrupt binding to the kinase domain also increase Byr2 function.","authors":"Bauman P, Albright CF","authors_abbrev":"Bauman P et al.","pubmed_publication_date":"Jul 1998","pubmed_entrez_date":"1998-11-12","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22144463","title":"RNA elimination machinery targeting meiotic mRNAs promotes facultative heterochromatin formation.","citation":"Science 2012 Jan 06;335(6064):96-100","abstract":"Facultative heterochromatin that changes during cellular differentiation coordinates regulated gene expression, but its assembly is poorly understood. Here, we describe facultative heterochromatin islands in fission yeast and show that their formation at meiotic genes requires factors that eliminate meiotic messenger RNAs (mRNAs) during vegetative growth. Blocking production of meiotic mRNA or loss of RNA elimination factors, including Mmi1 and Red1 proteins, abolishes heterochromatin islands. RNA elimination machinery is enriched at meiotic loci and interacts with Clr4/SUV39h, a methyltransferase involved in heterochromatin assembly. Heterochromatin islands disassemble in response to nutritional signals that induce sexual differentiation. This process involves the antisilencing factor Epe1, the loss of which causes dramatic increase in heterochromatic loci. Our analyses uncover unexpected regulatory roles for mRNA-processing factors that assemble dynamic heterochromatin to modulate gene expression.","doi":"10.1126/science.1211651","authors":"Zofall M, Yamanaka S, Reyes-Turcu FE, Zhang K, Rubin C, Grewal SI","authors_abbrev":"Zofall M et al.","pubmed_publication_date":"06 Jan 2012","pubmed_entrez_date":"2011-12-07","publication_year":"2012","canto_session_key":"68637de9f01b5872","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-11-26 17:03:19","canto_approved_date":"2024-05-07 13:50:28","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-03 10:51:52","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":44,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.14c","SPCC736.12c","SPBC32H8.10","SPCC970.07c","SPCC338.17c","SPAC1006.03c","SPAC27D7.13c","SPBP35G2.10","SPAC18G6.02c","SPBC428.08c","SPCC736.11","SPCC613.12c","SPBC2D10.17","SPBC16E9.12c","SPAC1F3.01","SPBC800.03","SPCC188.13c","SPAC31A2.05c","SPAC1B3.17","SPCC622.16c","SPBC16D10.07c","SPBC32H8.11","SPAC664.01c"],"gene_count":23,"ltp_gene_count":20,"approved_date":"2020-11-26"},{"uniquename":"PMID:2512297","title":"A galactosyltransferase from the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Biol 1989 Dec;109(6 Pt 1):2693-702","abstract":"A membrane-associated galactosyltransferase has been purified to homogeneity from the fission yeast, Schizosaccharomyces pombe. The enzyme has a molecular weight of 61,000 and is capable of transfering galactose from UDP-galactose (UDP-Gal) to a variety of mannose-based acceptors to form an alpha-1,2 galactosyl mannoside linkage. Immunofluorescence localization of the protein is consistent with the presence of the enzyme in the Golgi apparatus of S. pombe. This, together with the presence of terminal, alpha-linked galactose on the N-linked oligosaccharides of S. pombe secretory proteins, suggests that the galactosyltransferase is an enzyme involved in the processing of glycoproteins transported through the Golgi apparatus in fission yeast.","authors":"Chappell TG, Warren G","authors_abbrev":"Chappell TG et al.","pubmed_publication_date":"Dec 1989","pubmed_entrez_date":"1989-12-01","publication_year":"1989","canto_session_key":"7ae8160e9a367b95","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-12-07 18:14:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-12-07 18:14:00","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-12-07"},{"uniquename":"PMID:20226011","title":"Large-scale transcriptome data reveals transcriptional activity of fission yeast LTR retrotransposons.","citation":"BMC Genomics 2010 Mar 12;11:167","abstract":"Retrotransposons are transposable elements that proliferate within eukaryotic genomes through a process involving reverse transcription. The numbers of retrotransposons within genomes and differences between closely related species may yield insight into the evolutionary history of the elements. Less is known about the ongoing dynamics of retrotransposons, as analysis of genome sequences will only reveal insertions of retrotransposons that are fixed--or near fixation--in the population or strain from which genetic material has been extracted for sequencing. One pre-requisite for retrotransposition is transcription of the elements. Given their intrinsic sequence redundancy, transcriptome-level analyses of transposable elements are scarce. We have used recently published transcriptome data from the fission yeast Schizosaccharomyces pombe to assess the ability to detect and describe transcriptional activity from Long Terminal Repeat (LTR) retrotransposons. LTR retrotransposons are normally flanked by two LTR sequences. However, the majority of LTR sequences in S. pombe exist as solitary LTRs, i.e. as single terminal repeat sequences not flanking a retrotransposon. Transcriptional activity was analysed for both full-length LTR retrotransposons and solitary LTRs.\nTwo independent sets of transcriptome data reveal the presence of full-length, polyadenylated transcripts from LTR retrotransposons in S. pombe during growth phase in rich medium. The redundancy of retrotransposon sequences makes it difficult to assess which elements are transcriptionally active, but data strongly indicates that only a subset of the LTR retrotransposons contribute significantly to the detected transcription. A considerable level of reverse strand transcription is also detected. Equal levels of transcriptional activity are observed from both strands of solitary LTR sequences. Transcriptome data collected during meiosis suggests that transcription of solitary LTRs is correlated with the transcription of nearby protein-coding genes.\nPresumably, the host organism negatively regulates proliferation of LTR retrotransposons. The finding of considerable transcriptional activity of retrotransposons suggests that part of this regulation is likely to take place at a post-transcriptional level. Alternatively, the transcriptional activity may signify a hitherto unrecognized activity level of retrotransposon proliferation. Our findings underline the usefulness of transcriptome data in elucidating dynamics in retrotransposon transcription.","doi":"10.1186/1471-2164-11-167","authors":"Mourier T, Willerslev E","authors_abbrev":"Mourier T et al.","pubmed_publication_date":"12 Mar 2010","pubmed_entrez_date":"2010-03-16","publication_year":"2010","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37182105","title":"Reliable and robust control of nucleus centering is contingent on nonequilibrium force patterns.","citation":"iScience 2023 May 19;26(5):106665","abstract":"Cell centers their division apparatus to ensure symmetric cell division, a challenging task when the governing dynamics is stochastic. Using fission yeast, we show that the patterning of nonequilibrium polymerization forces of microtubule (MT) bundles  controls  the precise localization of spindle pole body (SPB), and hence the division septum, at the onset of mitosis. We define two cellular objectives,  reliability , the mean SPB position relative to the geometric center, and  robustness , the variance of the SPB position, which are sensitive to genetic perturbations that change cell length, MT bundle number/orientation, and MT dynamics. We show that simultaneous control of reliability and robustness is required to minimize septum positioning error achieved by the wild type (WT). A stochastic model for the MT-based nucleus centering, with parameters measured directly or estimated using Bayesian inference, recapitulates the maximum fidelity of WT. Using this, we perform a sensitivity analysis of the parameters that control nuclear centering.","doi":"10.1016/j.isci.2023.106665","authors":"Jain I, Rao M, Tran PT","authors_abbrev":"Jain I et al.","pubmed_publication_date":"19 May 2023","pubmed_entrez_date":"2023-05-14","publication_year":"2023","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2023-05-15 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15372743","title":"The central role of a CDK in controlling the fission yeast cell cycle.","citation":"Harvey Lect 1996;92:55-64","abstract":"","authors":"Nurse P","authors_abbrev":"Nurse P","pubmed_publication_date":"1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12889791","title":"Screening of yeasts for cell-free production of (R)-phenylacetylcarbinol.","citation":"Biotechnol Lett 2003 Jun;25(11):841-5","abstract":"105 yeast strains from 10 genera and 40 species were evaluated for cell-free production of (R)-phenylacetylcarbinol (PAC), the chiral precursor in the manufacture of the pharmaceuticals ephedrine and pseudoephedrine. Carboligase activity of pyruvate decarboxylase (PDC), forming PAC from benzaldehyde and pyruvate, was found in extracts of 98 strains. PAC was not formed from benzaldehyde and acetaldehyde, an activity of bacterial PDCs from Zymomonas mobilis and Zymobacter palmae. Two interesting groups of candidates were identified in the yeast screening: carboligase activities of Schizosaccharomyces pombe PDCs were very low but showed best resistance to pre-incubation with acetaldehyde and benzaldehyde; and highest carboligase activities combined with medium resistance were found in strains of Candida utilis, C. tropicalis and C. albicans.","authors":"Rosche B, Breuer M, Hauer B, Rogers PL","authors_abbrev":"Rosche B et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-08-02","publication_year":"2003","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36798368","title":"Quantifying yeast microtubules and spindles using the Toolkit for Automated Microtubule Tracking (TAMiT).","citation":"bioRxiv 2023 Feb 08;","abstract":"Fluorescently labeled proteins absorb and emit light, appearing as Gaussian spots in fluorescence imaging. When fluorescent tags are added to cytoskeletal polymers such as microtubules, a line of fluorescence and even non-linear structures results. While much progress has been made in techniques for imaging and microscopy, image analysis is less well developed. Current analysis of fluorescent microtubules uses either manual tools, such as kymographs, or automated software. As a result, our ability to quantify microtubule dynamics and organization from light microscopy remains limited. Despite development of automated microtubule analysis tools for  in vitro  studies, analysis of images from cells often depends heavily on manual analysis. One of the main reasons for this disparity is the low signal-to-noise ratio in cells, where background fluorescence is typically higher than in reconstituted systems. Here, we present the Toolkit for Automated Microtubule Tracking (TAMiT), which automatically detects, optimizes and tracks fluorescent microtubules in living yeast cells with sub-pixel accuracy. Using basic information about microtubule organization, TAMiT detects linear and curved polymers using a geometrical scanning technique. Images are fit via an optimization problem for the microtubule image parameters that is solved using non-linear least squares in Matlab. We benchmark our software using simulated images and show that it reliably detects microtubules, even at low signal-to-noise ratios. Then, we use TAMiT to measure monopolar spindle microtubule bundle number, length, and lifetime in a large dataset that includes several  S. pombe  mutants that affect microtubule dynamics and bundling. The results from the automated analysis are consistent with previous work, and suggest a direct role for CLASP/Cls1 in bundling spindle microtubules. We also illustrate automated tracking of single curved astral microtubules in  S. cerevisiae  , with measurement of dynamic instability parameters. The results obtained with our fully-automated software are similar to results using hand-tracked measurements. Therefore, TAMiT can facilitate automated analysis of spindle and microtubule dynamics in yeast cells.","doi":"10.1101/2023.02.07.527544","authors":"Ansari S, Gergely ZR, Flynn P, Li G, Moore JK, Betterton MD","authors_abbrev":"Ansari S et al.","pubmed_publication_date":"08 Feb 2023","pubmed_entrez_date":"2023-02-17","publication_year":"2023","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2023-02-18 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19039128","title":"Biochemistry. Controlled chaos.","citation":"Science 2008 Nov 28;322(5906):1340-1","abstract":"","doi":"10.1126/science.1167453","authors":"Uversky VN, Dunker AK","authors_abbrev":"Uversky VN et al.","pubmed_publication_date":"28 Nov 2008","pubmed_entrez_date":"2008-11-29","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8548290","title":"The chk1 pathway is required to prevent mitosis following cell-cycle arrest at 'start'.","citation":"Curr Biol 1995 Oct 01;5(10):1179-90","abstract":"The G2-M-phase transition is controlled by cell-cycle checkpoint pathways which inhibit mitosis if previous events are incomplete or if the DNA is damaged. Genetic analyses in yeast have defined two related, but distinct, pathways which prevent mitosis--one which acts when S phase is inhibited, and one which acts when the DNA is damaged. In the fission yeast Schizosaccharomyces pombe, many of the gene products involved have been identified. Six 'radiation checkpoint' (rad) gene products are required for both the S-M and DNA-damage checkpoints, whereas Chk1, a putative protein kinase, is required only for the DNA-damage checkpoint and not for the S-M checkpoint following the inhibition of DNA synthesis.\nWe have genetically defined a third mitotic control checkpoint pathway in fission yeast which prevents mitosis when passage through 'start' (the commitment point in G1) is compromized. In cycling cells arrested at start, mitosis is prevented by a Chk1-dependent pathway. In the absence of Chk1, G1 cells attempt an abortive mitosis with a 1C DNA content without entering S phase. Similar results are seen in the absence of Rad17, a typical example of a rad gene product.\nGenetic dissection of checkpoints in logarithmically growing fission yeast has identified a pathway that couples mitosis to correct passage through start. This pathway is related to the DNA-structure check-points which ensure that mitosis is dependent on the completion of replication and the integrity of the DNA. We propose that all three mitotic control checkpoints monitor distinct DNA or protein structures at different stages in the cell cycle.","authors":"Carr AM, Moudjou M, Bentley NJ, Hagan IM","authors_abbrev":"Carr AM et al.","pubmed_publication_date":"01 Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15876866","title":"Evidence that DNA damage detection machinery participates in DNA repair.","citation":"Cell Cycle 2005 Apr;4(4):529-32","abstract":"The toroidal Rad9-Rad1-Hus1 checkpoint complex (9-1-1) is structurally similar to the proliferating cell nuclear antigen (PCNA), which serves as a sliding clamp platform for DNA replication and repair. 9-1-1 has been characterized as a sensor of DNA damage that functions in concert with the checkpoint control proteins ATM and ATR. However, recent data suggest that the 9-1-1 complex and its individual Rad9 component serve different and multiple functions in cells by sensing DNA damage, stimulating apoptosis, and regulating gene transcription. Recently it was reported that 9-1-1 interacts with and/or stimulates components of the base excision repair (BER) pathway including the S. pombe MutY homolog (MYH), human polymerase beta (Polbeta), and flap endonuclease 1 (FEN1). Furthermore, preliminary results indicate a stimulation of DNA ligase I. In this review, the likely direct participation of 9-1-1 in DNA repair is discussed.","authors":"Helt CE, Wang W, Keng PC, Bambara RA","authors_abbrev":"Helt CE et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-05-07","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12626410","title":"In vitro oligosaccharide synthesis using intact yeast cells that display glycosyltransferases at the cell surface through cell wall-anchored protein Pir.","citation":"Glycobiology 2003 Feb;13(2):87-95","abstract":"A glycosyltransferase was fused to the yeast cell wall protein Pir, which forms the Pir1-4 protein family and is incorporated into the cell wall by an unknown linkage to be displayed at the yeast cell surface. We first expressed the PIR1-HA-gma12+ fusion, in which gma12+ encodes alpha-1,2-galactosyltransferase from the fission yeast Schizosaccharomyces pombe under the Saccharomyces cerevisiae GAPDH promoter. The alpha-1,2-galactosyltransferase activity was detected at the surface of the intact cells that produce Pir1-HA-Gma12 fusion. To further demonstrate sequential oligosaccharide synthesis, two plasmids containing PIR1-HA-KRE2 and PIR2-FLAG-MNN1 fusion genes were constructed in which KRE2 and MNN1 encode alpha-1,2-mannosyltransferase and alpha-1,3-mannosyltransferase from S. cerevisiae, respectively. The intact yeast cells transformed with these two plasmids added mannoses initially with an alpha-1,2 linkage and subsequently with an alpha-1,3 linkage to the alpha-1,2-mannobiose acceptor in the presence of a GDP-mannose donor, demonstrating that Pir1 and Pir2 can be used as anchors to simultaneously immobilize several glycosyltransferases at the yeast cell surface. Based on the high acceptor specificity of glycosyltransferases, we propose a simple in vitro method for oligosaccharide synthesis using the yeast intact cell as a biocatalyst.","authors":"Abe H, Shimma Y, Jigami Y","authors_abbrev":"Abe H et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-03-11","publication_year":"2003","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27451356","title":"Skb5, an SH3 adaptor protein, regulates Pmk1 MAPK signaling by controlling the intracellular localization of the MAPKKK Mkh1.","citation":"J Cell Sci 2016 Aug 15;129(16):3189-202","abstract":"The mitogen-activated protein kinase (MAPK) cascade is a highly conserved signaling module composed of MAPK kinase kinases (MAPKKKs), MAPK kinases (MAPKK) and MAPKs. The MAPKKK Mkh1 is an initiating kinase in Pmk1 MAPK signaling, which regulates cell integrity in fission yeast (Schizosaccharomyces pombe). Our genetic screen for regulators of Pmk1 signaling identified Shk1 kinase binding protein 5 (Skb5), an SH3-domain-containing adaptor protein. Here, we show that Skb5 serves as an inhibitor of Pmk1 MAPK signaling activation by downregulating Mkh1 localization to cell tips through its interaction with the SH3 domain. Consistent with this, the Mkh1(3PA) mutant protein, with impaired Skb5 binding, remained in the cell tips, even when Skb5 was overproduced. Intriguingly, Skb5 needs Mkh1 to localize to the growing ends as Mkh1 deletion and disruption of Mkh1 binding impairs Skb5 localization. Deletion of Pck2, an upstream activator of Mkh1, impaired the cell tip localization of Mkh1 and Skb5 as well as the Mkh1-Skb5 interaction. Interestingly, both Pck2 and Mkh1 localized to the cell tips at the G1/S phase, which coincided with Pmk1 MAPK activation. Taken together, Mkh1 localization to cell tips is important for transmitting upstream signaling to Pmk1, and Skb5 spatially regulates this process.","doi":"10.1242/jcs.188854","authors":"Kanda Y, Satoh R, Matsumoto S, Ikeda C, Inutsuka N, Hagihara K, Matzno S, Tsujimoto S, Kita A, Sugiura R","authors_abbrev":"Kanda Y et al.","pubmed_publication_date":"15 Aug 2016","pubmed_entrez_date":"2016-07-25","publication_year":"2016","canto_session_key":"7efbf9c6242aa883","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-29 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1685.01","SPAC1F3.02c","SPCC24B10.13","SPBC12D12.04c","SPCC4F11.02","SPBC543.07","SPAC16.01"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:33536434","title":"A scaffold lncRNA shapes the mitosis to meiosis switch.","citation":"Nat Commun 2021 Feb 03;12(1):770","abstract":"Long non-coding RNAs (lncRNAs) contribute to the regulation of gene expression in response to intra- or extracellular signals but the underlying molecular mechanisms remain largely unexplored. Here, we identify an uncharacterized lncRNA as a central player in shaping the meiotic gene expression program in fission yeast. We report that this regulatory RNA, termed mamRNA, scaffolds the antagonistic RNA-binding proteins Mmi1 and Mei2 to ensure their reciprocal inhibition and fine tune meiotic mRNA degradation during mitotic growth. Mechanistically, mamRNA allows Mmi1 to target Mei2 for ubiquitin-mediated downregulation, and conversely enables accumulating Mei2 to impede Mmi1 activity, thereby reinforcing the mitosis to meiosis switch. These regulations also occur within a unique Mmi1-containing nuclear body, positioning mamRNA as a spatially-confined sensor of Mei2 levels. Our results thus provide a mechanistic basis for the mutual control of gametogenesis effectors and further expand our vision of the regulatory potential of lncRNAs.","doi":"10.1038/s41467-021-21032-7","authors":"Andric V, Nevers A, Hazra D, Auxilien S, Menant A, Graille M, Palancade B, Rougemaille M","authors_abbrev":"Andric V et al.","pubmed_publication_date":"03 Feb 2021","pubmed_entrez_date":"2021-02-04","publication_year":"2021","canto_session_key":"a5289f010104594b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mathieu Rougemaille","canto_first_approved_date":"2023-03-27 15:17:41","canto_approved_date":"2023-05-05 15:04:07","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-03-19 11:02:37","canto_added_date":"2021-02-06 01:15:04","annotation_curators":[{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":24,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Mathieu Rougemaille","community_curator":true,"annotation_count":43,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.13c","SPAC27D7.03c","SPCC736.12c","SPBC2D10.06","SPNCRNA.1715","SPBC216.02","SPAC16C9.04c","SPBC32H8.11","SPNCRNA.130","SPNCRNA.103"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2023-03-27","pdb_entries":[{"pdb_id":"6yyl","gene_chains":[{"gene_uniquename":"SPAC27D7.03c","chain":"A/C","position":"579-750"}],"title":"Crystal structure of S. pombe Mei2 RRM3 domain","entry_authors":"Graille M,Hazra D","entry_authors_abbrev":"Graille M et al.","reference_uniquename":"PMID:33536434","experimental_method":"X-ray","resolution":"1.89"},{"pdb_id":"6yym","gene_chains":[{"gene_uniquename":"SPAC27D7.03c","chain":"A","position":"579-750"}],"title":"Structure of S. pombe Mei2 RRM3 domain bound to RNA","entry_authors":"Hazra D,Graille M","entry_authors_abbrev":"Hazra D et al.","reference_uniquename":"PMID:33536434","experimental_method":"X-ray","resolution":"2.63"}]},{"uniquename":"PMID:22300943","title":"Conserved regulators of the cell separation process in Schizosaccharomyces.","citation":"Fungal Genet Biol 2012 Mar;49(3):235-49","abstract":"The fission yeasts (Schizosaccharomyces) representing a highly divergent phylogenetic branch of Fungi evolved from filamentous ancestors by gradual transition from mycelial growth to yeast morphology. For the transition, a mechanism had been developed that separates the sister cells after the completion of cytokinesis. Numerous components of the separation mechanism have been characterised in Schizosaccharomycespombe, including the zinc-finger transcription factor Ace2p and the fork-head transcription factor Sep1p. Here we show that both regulators have regions conserved within the genus. The most conserved parts contain the DNA-binding domains whose amino-acid sequences perfectly reflect the phylogenetic positions of the species. The less conserved parts of the proteins contain sequence blocks specific for the whole genus or only for the species propagating predominantly or exclusively as yeasts. Inactivation of either gene in the dimorphic species Schizosaccharomycesjaponicus abolished cell separation in the yeast phase conferring hypha-like morphology but did not change the growth pattern to unipolar and did not cause extensive polar vacuolation characteristic of the true mycelium. Neither mutation affected the mycelial phase, but both mutations hampered the hyphal fragmentation at the mycelium-to-yeast transition. Ace2p(Sj) acts downstream of Sep1p(Sj) and regulates the orthologues of the Ace2p-dependent S.pombe genes agn1(+) (1,3-alpha-glucanase) and eng1(+) (1,3-beta-glucanase) but does not regulate the orthologue of cfh4(+) (chitin synthase regulatory factor). These results and the complementation of the cell separation defects of the ace2(-) and sep1(-) mutations of S.pombe by heterologously expressed ace2(Sj) and sep1(Sj) indicate that the cell separation mechanism is conserved in the Schizosaccharomyces genus.","doi":"10.1016/j.fgb.2012.01.003","authors":"Balazs A, Batta G, Miklos I, Acs-Szabo L, Vazquez de Aldana CR, Sipiczki M","authors_abbrev":"Balazs A et al.","pubmed_publication_date":"Mar 2012","pubmed_entrez_date":"2012-02-04","publication_year":"2012","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24186293","title":"Two Extramitochondrial Circular DNA Species in the Petite Negative Yeast Schizosaccharomyces pombe: Relative abundance and size determination by electron microscopy.","citation":"Curr Genet 1982 Aug;5(3):187-9","abstract":"In this paper we present the electron microscopic analysis of two distinct extramitochondrial circular DNA species in the fission yeast Schizosaccharomyces pombe (S. pombe). Both DNA species can be isolated from mitochondrial fractions, but disappear after DNase treatment of mitochondria, demonstrating their extramitochondrial location. The size of these molecular species is 3.08 ± 0.18 μm and 2.00 ± 0.09 μm (standard deviation). They are present in a ratio of approximately 9:1 in the DNA preparations analyzed.","doi":"10.1007/BF00391804","authors":"Manna F, Del Giudice L, Schreil WH, Wolf K","authors_abbrev":"Manna F et al.","pubmed_publication_date":"Aug 1982","pubmed_entrez_date":"2013-11-05","publication_year":"1982","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 06:09:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34100129","title":"Stress granules safeguard against MAPK signaling hyperactivation by sequestering PKC/Pck2: new findings and perspectives.","citation":"Curr Genet 2021 Dec;67(6):857-863","abstract":"Stress granule (SG) assembly is a conserved cellular strategy that copes with stress-related damage and promotes cell survival. SGs form through a process of liquid-liquid phase separation. Cellular signaling also appears to employ SG assembly as a mechanism for controlling cell survival and cell death by spatial compartmentalization of signal-transducing factors. While several lines of evidence highlight the importance of SGs as signaling hubs, where protein components of signaling pathways can be temporarily sequestered, shielded from the cytoplasm, the regulation and physiological significance of SGs in this aspect remain largely obscure. A recent study of the heat-shock response in the fission yeast Schizosaaccharomyces pombe provides an unexpected answer to this question. Recently, we demonstrated that the PKC orthologue Pck2 in fission yeast translocates into SGs through phase separation in a PKC kinase activity-dependent manner upon high-heat stress (HHS). Importantly, the downstream MAPK Pmk1 promotes Pck2 recruitment into SGs, which intercepts MAPK hyperactivation and cell death, thus posing SGs as a negative feedback circuit in controlling MAPK signaling. Intriguingly, HHS, but not modest-heat stress targets Pck2 to SGs, independent of canonical SG machinery. Finally, cells fail to activate MAPK signaling when Pck2 is sequestrated into SGs. In this review, we will discuss how SGs have a role as signaling hubs beyond serving as a repository for non-translated mRNAs during acute stress.","doi":"10.1007/s00294-021-01192-1","authors":"Sugiura R","authors_abbrev":"Sugiura R","pubmed_publication_date":"Dec 2021","pubmed_entrez_date":"2021-06-08","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-06-10 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11642635","title":"Update on antifungal agents.","citation":"Pediatr Infect Dis J 2001 Oct;20(10):993-5","abstract":"","authors":"Wellington M, Gigliotti F","authors_abbrev":"Wellington M et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-10-20","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPU59385","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38245838","title":"Transposon removal Reveals Their Adaptive Fitness Contribution.","citation":"Genome Biol Evol 2024 Jan 20;","abstract":"Transposable Elements (TE) are molecular parasites that persist in their host genome by generating new copies to outpace natural selection. TE exert a large influence on host genome evolution, in some cases providing adaptive changes. Here we measure the fitness effect of the TE insertions in the fission yeast Schizosaccharomyces pombe type strain by removing all insertions of its only native TE family, the LTR retrotransposon Tf2. We show that Tf2 elements provide a positive fitness contribution to its host. Tf2 ablation results in changes to the regulation of a mitochondrial gene and, consistently, the fitness effect is sensitive to growth conditions. We propose that Tf2 influence host fitness in a directed manner by dynamically rewiring the transcriptional response to metabolic stress.","doi":"10.1093/gbe/evae010","authors":"Cranz-Mileva S, Reilly E, Chalhoub N, Patel R, Atanassova T, Cao W, Ellison C, Zaratiegui M","authors_abbrev":"Cranz-Mileva S et al.","pubmed_publication_date":"20 Jan 2024","pubmed_entrez_date":"2024-01-21","publication_year":"2024","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2024-01-22 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26567340","title":"Genome-wide Screening of Regulators of Catalase Expression: ROLE OF A TRANSCRIPTION COMPLEX AND HISTONE AND tRNA MODIFICATION COMPLEXES ON ADAPTATION TO STRESS.","citation":"J Biol Chem 2016 Jan 08;291(2):790-9","abstract":"In response to environmental cues, the mitogen-activated protein kinase Sty1-driven signaling cascade activates hundreds of genes to induce a robust anti-stress cellular response in fission yeast. Thus, upon stress imposition Sty1 transiently accumulates in the nucleus where it up-regulates transcription through the Atf1 transcription factor. Several regulators of transcription and translation have been identified as important to mount an integral response to oxidative stress, such as the Spt-Ada-Gcn5-acetyl transferase or Elongator complexes, respectively. With the aim of identifying new regulators of this massive gene expression program, we have used a GFP-based protein reporter and screened a fission yeast deletion collection using flow cytometry. We find that the levels of catalase fused to GFP, both before and after a threat of peroxides, are altered in hundreds of strains lacking components of chromatin modifiers, transcription complexes, and modulators of translation. Thus, the transcription elongation complex Paf1, the histone methylase Set1-COMPASS, and the translation-related Trm112 dimers are all involved in full expression of Ctt1-GFP and in wild-type tolerance to peroxides.","doi":"10.1074/jbc.M115.696658","authors":"García P, Encinar Del Dedo J, Ayté J, Hidalgo E","authors_abbrev":"García P et al.","pubmed_publication_date":"08 Jan 2016","pubmed_entrez_date":"2015-11-15","publication_year":"2016","canto_session_key":"3eb3ce0ee3010824","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Patricia Garcia","canto_first_approved_date":"2016-01-13 11:25:09","canto_approved_date":"2023-05-03 15:37:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-16 17:50:10","canto_added_date":"2015-11-16 01:19:15","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Patricia Garcia","community_curator":true,"annotation_count":46,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H3.05c","SPBC13G1.08c","SPBC651.09c","SPCC306.04c","SPCC594.05c","SPBC354.03","SPAC1952.05","SPAC1783.07c","SPAC13D6.03c","SPAC21E11.03c","SPAC31A2.02","SPAC664.03","SPBC887.10","SPBC13E7.08c","SPCC24B10.08c","SPBC28F2.10c","SPAC29A4.20","SPAC17A2.09c","SPAC323.05c","SPBC29B5.01","SPAC24B11.06c","SPAC1006.09","SPCC757.07c","SPAC9G1.02","SPAC17G8.09","SPBC3H7.10"],"gene_count":26,"ltp_gene_count":26,"approved_date":"2016-01-13"},{"uniquename":"PMID:23249883","title":"Mapping genomic hotspots of DNA damage by a single-strand-DNA-compatible and strand-specific ChIP-seq method.","citation":"Genome Res 2013 Apr;23(4):705-15","abstract":"Spontaneous DNA damage may occur nonrandomly in the genome, especially when genome maintenance mechanisms are undermined. We developed single-strand DNA (ssDNA)-associated protein immunoprecipitation followed by sequencing (SPI-seq) to map genomic hotspots of DNA damage. We demonstrated this method with Rad52, a homologous recombination repair protein, which binds to ssDNA formed at DNA lesions. SPI-seq faithfully detected, in fission yeast, Rad52 enrichment at artificially induced double-strand breaks (DSBs) as well as endogenously programmed DSBs for mating-type switching. Applying Rad52 SPI-seq to fission yeast mutants defective in DNA helicase Pfh1 or histone H3K56 deacetylase Hst4, led to global views of DNA lesion hotspots emerging in these mutants. We also found serendipitously that histone dosage aberration can activate retrotransposon Tf2 and cause the accumulation of a Tf2 cDNA species bound by Rad52. SPI-seq should be widely applicable for mapping sites of DNA damage and uncovering the causes of genome instability.","doi":"10.1101/gr.146357.112","authors":"Zhou ZX, Zhang MJ, Peng X, Takayama Y, Xu XY, Huang LZ, Du LL","authors_abbrev":"Zhou ZX et al.","pubmed_publication_date":"Apr 2013","pubmed_entrez_date":"2012-12-20","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1309808","title":"Identification of heme and copper ligands in subunit I of the cytochrome bo complex in Escherichia coli.","citation":"J Biol Chem 1992 Jan 25;267(3):2096-104","abstract":"The cytochrome bo complex is a terminal ubiquinol oxidase in the aerobic respiratory chain of Escherichia coli (Kita, K., Konishi, K., and Anraku, Y. (1984) J. Biol. Chem. 259, 3368-3374) and functions as a proton pump. It belongs to the heme-copper oxidase superfamily with the aa3-type cytochrome c oxidases in mitochondria and aerobic bacteria. In order to identify ligands of hemes and copper, we have substituted eight conserved histidines in subunit I by alanine and, in addition, His-106, -284, and -421 by glutamine and methionine. Western immunoblotting analysis showed that all the mutations do not affect the expression level of subunit I in the cytoplasmic membrane, indicating that these histidines are not crucial for its stability. A single copy expression vector carrying a single mutation at the invariant histidines, His-106, His-284, His-333, His-334, His-419, and His-421, of subunit I was unable to support the aerobic growth of a strain in which the chromosomal terminal oxidase genes (the cyo and cyd operons) have been deleted. The same mutations caused a complete loss of ubiquinol oxidase activity of the partially purified enzymes. Spectroscopic analysis of mutant oxidases in the cytoplasmic membrane revealed that substitutions of His-106 and -421 specifically eliminated a 563.5 nm peak of the low spin heme and that replacements of His-106, -284, and -419 reduced the extent of the CO-binding high spin heme. These spectroscopic properties of mutant oxidases were further confirmed with partially purified preparations. Atomic absorption analysis showed that substitutions of His-106, -333, -334, and -419 eliminated CuB almost completely. Based on these findings, we conclude that His-106 and -421 function as the axial ligands of the low spin heme and His-284 is a possible ligand of the high spin heme. His-333, -334, and -419 residues are attributed to the ligands of CuB. We present a helical wheel model of the redox center in subunit I, which consists of the membrane-spanning regions II, VI, VII, and X, and discuss the implications of the model.","authors":"Minagawa J, Mogi T, Gennis RB, Anraku Y","authors_abbrev":"Minagawa J et al.","pubmed_publication_date":"25 Jan 1992","pubmed_entrez_date":"1992-01-25","publication_year":"1992","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPMIT.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9370325","title":"The phospholipid methyltransferases in yeast.","citation":"Biochim Biophys Acta 1997 Sep 04;1348(1-2):134-41","abstract":"In fungal microorganisms including fission yeast, Schizosaccharomyces pombe and baker's yeast, Saccharomyces cerevisiae, two enzymes are required to catalyze the synthesis of phosphatidylcholine (PC) from phosphatidylethanolamine (PE). The genes encoding the class I and class II phospholipid N-methyltransferases (PLMTs) have been cloned from both yeasts. The class II PLMTs catalyze the first methylation step from PE to phosphatidyl-monomethylethanolamine (PMME). Representatives of the class II type enzymes have been isolated only from yeast and the amino acid sequence of these enzymes contain regions of internal duplication. The class I PLMTs catalyze the last two methylation steps from PMME to PC. The class I PLMTs from both yeasts are homologous to the products of the phosphatidylethanolamine methyltransferase (PEMT) genes isolated from mouse and rat (described in the article by Vance et al. in this volume). Like the mammalian PEMT gene products, the S. cerevisiae class I enzyme can catalyze all three methylation steps to PC biosynthesis. S. cerevisiae strains, in which either the class II or class I enzyme is deleted, grow slowly in the absence of choline and exhibit low levels of PC. However, in S. pombe, mutants lacking either one of the two PLMTs are choline auxotrophs. Thus, both enzymes are required in S. pombe for maximal growth in the absence of exogenous choline. The S. cerevisiae methyltransferase genes are regulated at the level of transcription in response to the soluble precursors, inositol and choline as well as to growth phase. The mechanism of regulation of the S. pombe methyltransferases is not yet understood but appears to occur post-transcriptionally in response to choline availability. In addition, the S. pombe PLMT genes are regulated transcriptionally in response to growth phase.","authors":"Kanipes MI, Henry SA","authors_abbrev":"Kanipes MI et al.","pubmed_publication_date":"04 Sep 1997","pubmed_entrez_date":"1997-11-25","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23588069","title":"Making chromosomes hot for breakage.","citation":"Cell Cycle 2013 May 01;12(9):1327-8","abstract":"","doi":"10.4161/cc.24576","authors":"Martín-Castellanos C, Fowler KR, Smith GR","authors_abbrev":"Martín-Castellanos C et al.","pubmed_publication_date":"01 May 2013","pubmed_entrez_date":"2013-04-17","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24458466","title":"Cytoplasmic microtubules in a yeast.","citation":"Planta 1974 Dec;117(4):355-60","abstract":"Electron micrographs showing cytoplasmic microtubules in the fission yeast Schizosaccharomyces pombe are described. The microtubules are found closely apposed to the microtubule organizing centre on the nuclear membrane and to mitochondria.","doi":"10.1007/BF00388030","authors":"Hereward FV","authors_abbrev":"Hereward FV","pubmed_publication_date":"Dec 1974","pubmed_entrez_date":"2014-01-25","publication_year":"1974","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 06:09:41","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20372962","title":"Optic atrophy 3 as a protein of the mitochondrial outer membrane induces mitochondrial fragmentation.","citation":"Cell Mol Life Sci 2010 Aug;67(16):2839-50","abstract":"The optic atrophy 3 (OPA3) gene, which has no known homolog or biological function, is mutated in patients with hereditary optic neuropathies. Here, we identified OPA3 as an integral protein of the mitochondrial outer membrane (MOM), with a C-terminus exposed to the cytosol and an N-terminal mitochondrial targeting domain. By quantitative analysis, we demonstrated that overexpression of OPA3 significantly induced mitochondrial fragmentation, whereas OPA3 knockdown resulted in highly elongated mitochondria. Cells with mitochondria fragmented by OPA3 did not undergo spontaneous apoptotic cell death, but were significantly sensitized to staurosporine- and TRAIL-induced apoptosis. In contrast, overexpression of a familial OPA3 mutant (G93S) induced mitochondrial fragmentation and spontaneous apoptosis, suggesting that OPA3 mutations may cause optic atrophy via a gain-of-function mechanism. Together, these results indicate that OPA3, as an integral MOM protein, has a crucial role in mitochondrial fission, and provides a direct link between mitochondrial morphology and optic atrophy.","doi":"10.1007/s00018-010-0365-z","authors":"Ryu SW, Jeong HJ, Choi M, Karbowski M, Choi C","authors_abbrev":"Ryu SW et al.","pubmed_publication_date":"Aug 2010","pubmed_entrez_date":"2010-04-08","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1703.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:32569690","title":"The differences between fungal α-glucan synthase determining pullulan synthesis and that controlling cell wall α-1,3 glucan synthesis.","citation":"Int J Biol Macromol 2020 Nov 01;162:436-444","abstract":"The fungal α-glucan synthases (Agss) are multi-domain proteins catalyzing biosynthesis of cell wall α-1,3-glucan which determines cell wall integrity or fungal pathogenicity and pullulan which is a maltotriosyl polymer made of α-1,4 and α-1,6 bound glucose units. The Agss family can be divided into 11 groups, some of which lost the original functions due to accumulation of harmful mutations or gene loss. Schizosaccharomyces pombe kept five kinds of Agss in the genome while Aspergillus spp. and Penicillium spp. lost one or two or three kinds of Agss. All the human, animal and plant pathogens kept only one single kind of Ags or only one active Ags for synthesis of cell wall α-1,3-glucan, a virulence factor. While the genus Aureobasidium spp. contained three kinds of Agss, of which only some of the Ags2 was involved in pullulan biosynthesis. Although many Agss contained Big_5 domain, only the Big_5 domain with conserved amino acids LQS from some strains of A. melanogenum could catalyze pullulan biosynthesis. This whole amino acid sequence and phylogenetic differences may cause non-α-1,3-glucan synthesizing activity of some fungal Agss.","doi":"10.1016/j.ijbiomac.2020.06.147","authors":"Qi CY, Jia SL, Wei X, Yang G, Chi Z, Liu GL, Hu Z, Chi ZM","authors_abbrev":"Qi CY et al.","pubmed_publication_date":"01 Nov 2020","pubmed_entrez_date":"2020-06-23","publication_year":"2020","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2020-06-24 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22325349","title":"Peroxiredoxins as molecular triage agents, sacrificing themselves to enhance cell survival during a peroxide attack.","citation":"Mol Cell 2012 Feb 10;45(3):275-8","abstract":"In this issue of Molecular Cell, Day et al. (2012) reveal a surprising benefit of peroxiredoxin inactivation at high H(2)O(2), showing that in Schizosaccharomyces pombe turning off peroxide defenses preserves the pool of reduced thioredoxin for repairing proteins vital to survival.","doi":"10.1016/j.molcel.2012.01.012","authors":"Karplus PA, Poole LB","authors_abbrev":"Karplus PA et al.","pubmed_publication_date":"10 Feb 2012","pubmed_entrez_date":"2012-02-14","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2184030","title":"The rhp6+ gene of Schizosaccharomyces pombe: a structural and functional homolog of the RAD6 gene from the distantly related yeast Saccharomyces cerevisiae.","citation":"EMBO J 1990 May;9(5):1423-30","abstract":"The RAD6 gene of Saccharomyces cerevisiae encodes a ubiquitin conjugating enzyme and is required for DNA repair, DNA-damage-induced mutagenesis and sporulation. Here, we show that RAD6 and the rhp6+ gene from the distantly related yeast Schizosaccharomyces pombe share a high degree of structural and functional homology. The predominantly acidic carboxyl-terminal 21 amino acids present in the RAD6 protein are absent in the rhp6(+)-encoded protein; otherwise, the two proteins are very similar, with 77% identical residues. Like rad6, null mutations of the rhp6+ gene confer a defect in DNA repair, UV mutagenesis and sporulation, and the RAD6 and rhp6+ genes can functionally substitute for one another. These observations suggest that functional interactions between RAD6 (rhp6+) protein and other components of the DNA repair complex have been conserved among eukaryotes.","authors":"Reynolds P, Koken MH, Hoeijmakers JH, Prakash S, Prakash L","authors_abbrev":"Reynolds P et al.","pubmed_publication_date":"May 1990","pubmed_entrez_date":"1990-05-01","publication_year":"1990","canto_session_key":"47797c5ac471b4da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-01-07 16:13:40","canto_approved_date":"2019-06-14 08:54:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-11-25 00:49:49","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-01-07"},{"uniquename":"PMID:38991050","title":"Role of diffusion and reaction of the constituents in spreading of histone modification marks.","citation":"PLoS Comput Biol 2024 Jul 11;20(7):e1012235","abstract":"Cells switch genes ON or OFF by altering the state of chromatin via histone modifications at specific regulatory locations along the chromatin polymer. These gene regulation processes are carried out by a network of reactions in which the histone marks spread to neighboring regions with the help of enzymes. In the literature, this spreading has been studied as a purely kinetic, non-diffusive process considering the interactions between neighboring nucleosomes. In this work, we go beyond this framework and study the spreading of modifications using a reaction-diffusion (RD) model accounting for the diffusion of the constituents. We quantitatively segregate the modification profiles generated from kinetic and RD models. The diffusion and degradation of enzymes set a natural length scale for limiting the domain size of modification spreading, and the resulting enzyme limitation is inherent in our model. We also demonstrate the emergence of confined modification domains without the explicit requirement of a nucleation site. We explore polymer compaction effects on spreading and show that single-cell domains may differ from averaged profiles. We find that the modification profiles from our model are comparable with existing H3K9me3 data of S. pombe.","doi":"10.1371/journal.pcbi.1012235","authors":"Manivannan V, Inamdar MM, Padinhateeri R","authors_abbrev":"Manivannan V et al.","pubmed_publication_date":"11 Jul 2024","pubmed_entrez_date":"2024-07-11","publication_year":"2024","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2024-07-11 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39739812","title":"Predicting gene sequences with AI to study codon usage patterns.","citation":"Proc Natl Acad Sci U S A 2025 Jan 07;122(1):e2410003121","abstract":"Selective pressure acts on the codon use, optimizing multiple, overlapping signals that are only partially understood. We trained AI models to predict codons given their amino acid sequence in the eukaryotes  Saccharomyces cerevisiae  and  Schizosaccharomyces pombe  and the bacteria  Escherichia coli  and  Bacillus subtilis  to study the extent to which we can learn patterns in naturally occurring codons to improve predictions. We trained our models on a subset of the proteins and evaluated their predictions on large, separate sets of proteins of varying lengths and expression levels. Our models significantly outperformed naïve frequency-based approaches, demonstrating that there are learnable dependencies in evolutionary-selected codon usage. The prediction accuracy advantage of our models is greater for highly expressed genes and is greater in bacteria than eukaryotes, supporting the hypothesis that there is a monotonic relationship between selective pressure for complex codon patterns and effective population size. In  S .  cerevisiae  and bacteria, our models were more accurate for longer proteins, suggesting that the learned patterns may be related to cotranslational folding. Gene functionality and conservation were also important determinants that affect the performance of our models. Finally, we showed that using information encoded in homologous proteins has only a minor effect on prediction accuracy, perhaps due to complex codon-usage codes in genes undergoing rapid evolution. Our study employing contemporary AI methods offers a unique perspective and a deep-learning-based prediction tool for evolutionary-selected codons. We hope that these can be useful to optimize codon usage in endogenous and heterologous proteins.","doi":"10.1073/pnas.2410003121","authors":"Sidi T, Bahiri-Elitzur S, Tuller T, Kolodny R","authors_abbrev":"Sidi T et al.","pubmed_publication_date":"07 Jan 2025","pubmed_entrez_date":"2024-12-31","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-01-02 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:00000111","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16014916","title":"The long terminal repeat-containing retrotransposon Tf1 possesses amino acids in gag that regulate nuclear localization and particle formation.","citation":"J Virol 2005 Aug;79(15):9540-55","abstract":"Tf1 is a long terminal repeat-containing retrotransposon of Schizosaccharomyces pombe that is studied to further our understanding of retrovirus propagation. One important application is to examine Tf1 as a model for how human immunodeficiency virus type 1 proteins enter the nucleus. The accumulation of Tf1 Gag in the nucleus requires an N-terminal nuclear localization signal (NLS) and the nuclear pore factor Nup124p. Here, we report that NLS activity is regulated by adjacent residues. Five mutant transposons were made, each with sequential tracts of four amino acids in Gag replaced by alanines. All five versions of Tf1 transposed with frequencies that were significantly lower than that of the wild type. Although all five made normal amounts of Gag, two of the mutations did not make cDNA, indicating that Gag contributed to reverse transcription. The localization of the Gag in the nucleus was significantly reduced by mutations A1, A2, and A3. These results identified residues in Gag that contribute to the function of the NLS. The Gags of A4 and A5 localized within the nucleus but exhibited severe defects in the formation of virus-like particles. Of particular interest was that the mutations in Gag-A4 and Gag-A5 caused their nuclear localization to become independent of Nup124p. These results suggested that Nup124p was only required for import of Tf1 Gag because of its extensive multimerization.","authors":"Kim MK, Claiborn KC, Levin HL","authors_abbrev":"Kim MK et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-07-15","publication_year":"2005","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9017391","title":"apd1+, a gene required for red pigment formation in ade6 mutants of Schizosaccharomyces pombe, encodes an enzyme required for glutathione biosynthesis: a role for glutathione and a glutathione-conjugate pump.","citation":"Genetics 1997 Jan;145(1):75-83","abstract":"Mutants in the adenine biosynthetic pathway of yeasts (ade1 and ade2 of Saccharomyces cerevisiae, ade6 and ade7 of Schizosaccharomyces pombe) accumulate an intense red pigment in their vacuoles when grown under adenine-limiting conditions. The precise events that determine the formation of the pigment are however, still unknown. We have begun a genetic investigation into the nature and cause of pigmentation of ade6 mutants of S. pombe and have discovered that one of these pigmentation defective mutants, apd1 (adenine pigmentation defective), is a strict glutathione auxotroph. The gene apd1+ was found to encode the first enzyme in glutathione biosynthesis, gamma-glutamylcysteine synthetase, gcs1+. This gene when expressed in the mutant could confer both glutathione prototrophy and the characteristic red pigmentation, and disruption of the gene led to a loss in both phenotypes. Supplementation of glutathione in the medium, however, could only restore growth but not the pigmentation because the cells were unable to achieve sufficient intracellular levels of glutathione. Disruption of the second enzyme in glutathione biosynthesis, glutathione synthetase gsh2+, also led to glutathione auxotrophy, but only a partial defect in pigment formation. A reevaluation of the major amino acids previously reported to be present in the pigment indicated that the pigment is probably a glutathione conjugate. The ability of vanadate to inhibit pigment formation indicated that the conjugate was transported into the vacuole through a glutathione-conjugate pump. This was further confirmed using strains of S. cerevisiae bearing disruptions in the recently identified glutathione-conjugate pump, YCF1, where a significant reduction in pigment formation was observed. The pump of S. pombe is distinct from the previously identified vacuolar pump, hmt1p, for transporting cadystin peptides into vacuoles of S. pombe.","authors":"Chaudhuri B, Ingavale S, Bachhawat AK","authors_abbrev":"Chaudhuri B et al.","pubmed_publication_date":"Jan 1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_session_key":"40aa30b33b608f68","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-05-25 17:08:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-06-20 13:42:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13","SPAC3F10.04","SPCC737.09c","SPAC22F3.10c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2012-06-20"},{"uniquename":"PMID:11270572","title":"Schizosaccharomyces pombe taf1+ is required for nitrogen starvation-induced sexual development and for entering the dormant GO state.","citation":"Curr Genet 2001 Jan;38(6):307-13","abstract":"Environmental change, such as nutritional starvation, induces physiological and morphological alterations that enable fission yeast cells to survive. We isolated a novel gene, taf1+, required for the response to nitrogen starvation in the fission yeast Schizosaccharomyces pombe. taf1 disruptants could not mate upon nitrogen starvation, but could upon carbon starvation. taf1 disruptants had a defect in inducing stell+ expression under nitrogen starvation conditions. Furthermore, they lost viability quickly in nitrogen-depleted medium. Unlike wild-type cells, starved taf1-cells had nuclear chromatin that were flat and adhered to the cell periphery. These results indicate that tqf1+ is required for nitrogen starvation-induced sexual development and entering the dormant G0 state.","authors":"Ueno M, Kurokawa R, Renauld H, Watanabe K, Ushimaru T, Uritani M, Yoshinaga K, Hiraoka Y","authors_abbrev":"Ueno M et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2001-03-29","publication_year":"2001","canto_session_key":"4a6747e22f344bb1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-05-02 12:24:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-05-02 12:24:10","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC7D4.04","SPAC16A10.07c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2014-05-02"},{"uniquename":"PMID:40741734","title":"Quantification of Cyclin-CDK dissociation constants using FCCS with green and near-infrared fluorescent proteins.","citation":"J Cell Sci 2025 Jul 31;","abstract":"The cell cycle is a highly coordinated process governed by cyclin-bound cyclin-dependent kinases (CDKs). While the interaction between cyclin and CDK are well-documented, the dissociation constants (Kd) between specific cyclin-CDK pairs within living cells remain poorly understood. Fluorescence cross-correlation spectroscopy (FCCS) enables the quantification of the Kd, but challenges remain in selecting an optimal pair of fluorescent molecules for FCCS in a living cell. In this study, we demonstrate that mNeonGreen and phycocyanobilin-bound miRFP670 represent a suitable pair for FCCS in living cells from the viewpoint of high photostability and low bleed-through. This fluorescent protein pair enables us to measure the Kd values of the cyclin-dependent kinase Cdc2 and B-type cyclin Cdc13 in fission yeast cells. Moreover, we roughly estimated the Kd values for 36 cyclin-CDK complexes, formed by 9 distinct cyclins and 4 CDKs, in mammalian cells, including unconventional cyclin-CDK pairs. These measurements suggest potential versatility of cyclin-CDK binding in cell cycle progression, with implications for understanding cell cycle regulation in both fission yeast and higher eukaryotes.","doi":"10.1242/jcs.263921","authors":"Toyama A, Goto Y, Yamauchi Y, Sugiyama H, Kondo Y, Mochizuki A, Aoki K","authors_abbrev":"Toyama A et al.","pubmed_publication_date":"31 Jul 2025","pubmed_entrez_date":"2025-07-31","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-31 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:318606","title":"Induction of gene mutations and gene conversions by vinyl chloride metabolites in yeast.","citation":"Cancer Res 1977 Jan;37(1):253-7","abstract":"Chloroethylene oxide and 2-chloroacetaldehyde, two metabolites of vinyl chloride, and 2-chloroethanol, a putative metabolic intermediate, were assayed for their genetic activity in the yeasts Schizosaccharomyces pombe and Saccharomyces cerevisiae. Chloroethylene oxide was found to be the most effective in inducing forward mutations in Sch. pombe and gene conversions in S. cerevisiae, increasing the mutation and conversion frequencies 340 and 50 times, respectively, over those of the controls. In either the presence or the absence of mouse liver microsomes, 2-chloroacetaldehyde showed only feeble genetic activity, and 2-chloroethanol was completely inactive in both yeast strains. In contrast to vinyl chloride, 2-chloroacetaldehyde did not induce forward mutations in Sch. pombe inthe host-mediated assay in mice. The results strongly support the hypothesis that chloroethylene oxide is one of the principal mutagenic agents formed from vinyl chloride in the presence of mouse liver enzymes.","authors":"Loprieno N, Barale R, Baroncelli S, Bartsch H, Bronzetti G, Cammelini A, Corsi C, Frezza D, Nieri R, Leporini C, Rosellini D, Rossi AM","authors_abbrev":"Loprieno N et al.","pubmed_publication_date":"Jan 1977","pubmed_entrez_date":"1977-01-01","publication_year":"1977","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17922236","title":"Genomic expression patterns in cell separation mutants of Schizosaccharomyces pombe defective in the genes sep10 ( + ) and sep15 ( + ) coding for the Mediator subunits Med31 and Med8.","citation":"Mol Genet Genomics 2008 Mar;279(3):225-38","abstract":"Cell division is controlled by a complex network involving regulated transcription of genes and postranslational modification of proteins. The aim of this study is to demonstrate that the Mediator complex, a general regulator of transcription, is involved in the regulation of the second phase (cell separation) of cell division of the fission yeast Schizosaccharomyces pombe. In previous studies we have found that the fission yeast cell separation genes sep10 ( + ) and sep15 ( + ) code for proteins (Med31 and Med8) associated with the Mediator complex. Here, we show by genome-wide gene expression profiling of mutants defective in these genes that both Med8 and Med31 control large, partially overlapping sets of genes scattered over the entire genome and involved in diverse biological functions. Six cell separation genes controlled by the transcription factors Sep1 and Ace2 are among the target genes. Since neither sep1 ( + ) nor ace2 ( + ) is affected in the mutant cells, we propose that the Med8 and Med31 proteins act as coactivators of the Sep1-Ace2-dependent cell separation genes. The results also indicate that the subunits of Mediator may contribute to the coordination of cellular processes by fine-tuning of the expression of larger sets of genes.","authors":"Miklos I, Szilagyi Z, Watt S, Zilahi E, Batta G, Antunovics Z, Enczi K, Bähler J, Sipiczki M","authors_abbrev":"Miklos I et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2007-10-09","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCP31B10.03c","SPBC21.04"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AU013353","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10915873","title":"Repair of UV damage in the fission yeast Schizosaccharomyces pombe.","citation":"Mutat Res 2000 Jun 30;451(1-2):197-210","abstract":"This review is concerned with repair and tolerance of UV damage in the fission yeast, Schizosaccharomyces pombe and with the differences between Sch. pombe and budding yeast, Saccharomyces cerevisiae in their response to UV irradiation. Sch. pombe is not as sensitive to ultra-violet radiation as Sac. cerevisiae nor are any of its mutants as sensitive as the most sensitive Sac. cerevisiae mutants. This can be explained in part by the fact that Sch. pombe, unlike budding yeast or mammalian cells, has an extra pathway (UVER) for excision of UV photoproducts in addition to nucleotide excision repair (NER). However, even in mutants lacking this additional pathway, there are significant differences between the two yeasts. Sch. pombe mutants that lack the alternative pathway are still more UV-resistant than wild-type Sac. cerevisiae; recombination mutants are significantly UV sensitive (unlike their Sac. cerevisiae equivalents); mutants lacking the second pathway are sensitized to UV by caffeine; and checkpoint mutants are relatively more sensitive than the budding yeast equivalents. In addition, Sch. pombe has no photolyase. Thus, the response to UV in the two yeasts has a number of significant differences, which are not accounted for entirely by the existence of two alternative excision repair pathways. The long G2 in Sch. pombe, its well-developed recombination pathways and efficient cell cycle checkpoints are all significant components in survival of UV damage.","authors":"McCready SJ, Osman1 F, Yasui A","authors_abbrev":"McCready SJ et al.","pubmed_publication_date":"30 Jun 2000","pubmed_entrez_date":"2000-08-01","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33506191","title":"Escape from mitotic catastrophe by actin-dependent nuclear displacement in fission yeast.","citation":"iScience 2021 Jan 22;24(1):102031","abstract":"Eukaryotic cells position the nucleus within the proper intracellular space, thereby safeguarding a variety of cellular processes. In fission yeast, the interphase nucleus is placed in the cell middle in a microtubule-dependent manner. By contrast, how the mitotic nucleus is positioned remains elusive. Here we show that several cell-cycle mutants that arrest in mitosis all displace the nucleus toward one end of the cell. Intriguingly, the actin cytoskeleton is responsible for nuclear movement. Time-lapse live imaging indicates that mitosis-specific F-actin cables possibly push the nucleus through direct interaction with the nuclear envelope, and subsequently actomyosin ring constriction further shifts the nucleus away from the center. This nuclear movement is beneficial, because if the nuclei were retained in the center, unseparated chromosomes would be intersected by the contractile actin ring and the septum, imposing the lethal cut phenotype. Thus, fission yeast escapes from mitotic catastrophe by means of actin-dependent nuclear movement.","doi":"10.1016/j.isci.2020.102031","authors":"Yukawa M, Teratani Y, Toda T","authors_abbrev":"Yukawa M et al.","pubmed_publication_date":"22 Jan 2021","pubmed_entrez_date":"2021-01-28","publication_year":"2021","canto_session_key":"dc8fa114b5d1cd1f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masashi Yukawa","canto_first_approved_date":"2021-02-10 19:41:56","canto_approved_date":"2022-07-20 13:24:08","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2021-02-03 23:38:11","canto_added_date":"2021-01-30 01:15:06","annotation_curators":[{"name":"Masashi Yukawa","community_curator":true,"annotation_count":13,"orcid":"0000-0002-1723-890X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c","SPAC6F12.15c","SPBC2D10.14c","SPBC21.06c","SPAC1F5.04c","SPCC613.04c","SPCC645.05c","SPBC20F10.06","SPBC26H8.07c","SPAC17C9.01c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2021-02-10"},{"uniquename":"PMID:34035174","title":"Spreading and epigenetic inheritance of heterochromatin require a critical density of histone H3 lysine 9 tri-methylation.","citation":"Proc Natl Acad Sci U S A 2021 Jun 01;118(22)","abstract":"Heterochromatin assembly requires methylation of histone H3 lysine 9 (H3K9me) and serves as a paradigm for understanding the importance of histone modifications in epigenetic genome control. Heterochromatin is nucleated at specific genomic sites and spreads across extended chromosomal domains to promote gene silencing. Moreover, heterochromatic structures can be epigenetically inherited in a self-templating manner, which is critical for stable gene repression. The spreading and inheritance of heterochromatin are believed to be dependent on preexisting H3K9 tri-methylation (H3K9me3), which is recognized by the histone methyltransferase Clr4/Suv39h via its chromodomain, to promote further deposition of H3K9me. However, the process involving the coupling of the \"read\" and \"write\" capabilities of histone methyltransferases is poorly understood. From an unbiased genetic screen, we characterize a dominant-negative mutation in histone H3 (H3 G13D ) that impairs the propagation of endogenous and ectopic heterochromatin domains in the fission yeast genome. H3 G13D  blocks methylation of H3K9 by the Clr4/Suv39h methyltransferase and acts in a dosage-dependent manner to interfere with the spreading and maintenance of heterochromatin. Our analyses show that the incorporation of unmethylatable histone H3 G13D  into chromatin decreases H3K9me3 density and thereby compromises the read-write capability of Clr4/Suv39h. Consistently, enhancing the affinity of Clr4/Suv39h for methylated H3K9 is sufficient to overcome the defects in heterochromatin assembly caused by H3 G13D  Our work directly implicates methylated histones in the transmission of epigenetic memory and shows that a critical density threshold of H3K9me3 is required to promote epigenetic inheritance of heterochromatin through the read-write mechanism.","doi":"10.1073/pnas.2100699118","authors":"Cutter DiPiazza AR, Taneja N, Dhakshnamoorthy J, Wheeler D, Holla S, Grewal SIS","authors_abbrev":"Cutter DiPiazza AR et al.","pubmed_publication_date":"01 Jun 2021","pubmed_entrez_date":"2021-05-26","publication_year":"2021","canto_session_key":"e1de8240b1f80add","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-05-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33823662","title":"Multiple nutritional phenotypes of fission yeast mutants defective in genes encoding essential mitochondrial proteins.","citation":"Open Biol 2021 Apr;11(4):200369","abstract":"Mitochondria are essential for regulation of cellular respiration, energy production, small molecule metabolism, anti-oxidation and cell ageing, among other things. While the mitochondrial genome contains a small number of protein-coding genes, the great majority of mitochondrial proteins are encoded by chromosomal genes. In the fission yeast  Schizosaccharomyces pombe , 770 proteins encoded by chromosomal genes are located in mitochondria. Of these, 195 proteins, many of which are implicated in translation and transport, are absolutely essential for viability. We isolated and characterized eight temperature-sensitive ( ts ) strains with mutations in essential mitochondrial proteins. Interestingly, they are also sensitive to limited nutrition (glucose and/or nitrogen), producing low-glucose-sensitive and 'super-housekeeping' phenotypes. They fail to produce colonies under low-glucose conditions at the permissive temperature or lose cell viability under nitrogen starvation at the restrictive temperature. The majority of these  ts  mitochondrial mutations may cause defects of gene expression in the mitochondrial genome.  mrp4  and  mrp17  are defective in mitochondrial ribosomal proteins.  ppr3  is defective in rRNA expression, and  trz2  and  vrs2  are defective in tRNA maturation. This study promises potentially large dividends because mitochondrial quiescent functions are vital for human brain and muscle, and also for longevity.","doi":"10.1098/rsob.200369","authors":"Uehara L, Saitoh S, Mori A, Sajiki K, Toyoda Y, Masuda F, Soejima S, Tahara Y, Yanagida M","authors_abbrev":"Uehara L et al.","pubmed_publication_date":"Apr 2021","pubmed_entrez_date":"2021-04-07","publication_year":"2021","canto_session_key":"2c9236cd451a19c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shigeaki Saitoh","canto_first_approved_date":"2021-04-27 13:06:21","canto_approved_date":"2023-11-19 09:18:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-04-16 03:52:29","canto_added_date":"2021-04-10 00:15:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":20,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Shigeaki Saitoh","community_curator":true,"annotation_count":26,"orcid":"0000-0001-5408-296X","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC343.08c","SPBC19G7.07c","SPAC24C9.10c","SPBC887.13c","SPAC4A8.08c","SPBC3D6.03c","SPAC6F12.17"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2021-04-27"},{"uniquename":"PMID:11872168","title":"Genes for a nuclease and a protease are involved in the drastic decrease in cellular RNA amount in fission yeast cells during nitrogen starvation.","citation":"J Biochem 2002 Mar;131(3):391-8","abstract":"Cellular RNA in Schizosaccharomyces pombe cells drastically decreases in amount during nitrogen starvation. Previously, we found and purified a soluble RNA-degrading enzyme whose activity drastically increased in the cells of S. pombe undergoing nitrogen starvation. The enzyme was a nuclease encoded by pnu1(+). In this study, the increase in the RNA-degrading activity and the decrease in cellular RNA level are examined in a null-mutant of pnu1(+) (pnu1Delta). During nitrogen starvation, wild-type cells show an apparent increase in RNA-degrading activity, whereas the pnu1Delta cells do not. The wild-type cells show a drastic decrease in cellular RNA amount, whereas the pnu1Delta cells show only a slight decrease. These results suggest that Pnu1 nuclease is implicated in the decrease in cellular RNA amount during nitrogen starvation, probably via the RNA-degrading activity. The increase in the RNA-degrading activity is independent of both the Wis1 stress-activated MAP kinase cascade and Tor1 signaling pathway, but it is strongly dependent on isp6(+), a gene for a possible protease, whose expression is induced during nitrogen starvation. A disruption mutant for isp6(+) (isp6Delta) is deficient in both the increase in the RNA-degrading activity and the drastic decrease in the cellular RNA amount during nitrogen starvation, which suggests that isp6(+) is involved in the RNA degradation via regulating the RNA-degrading activity of Pnu1.","authors":"Nakashima A, Yoshida M, Nakayama K, Kato-Furuno A, Ueno M, Ushimaru T, Uritani M","authors_abbrev":"Nakashima A et al.","pubmed_publication_date":"Mar 2002","pubmed_entrez_date":"2002-03-02","publication_year":"2002","canto_session_key":"b2f89f832b64979e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-01-17 18:12:37","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-01-17 18:12:29","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC4A8.04","SPBC30D10.10c","SPAC17C9.08","SPAC8C9.03","SPAC29B12.06c","SPBC409.07c","SPBC106.10"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2017-01-17"},{"uniquename":"PMID:16087749","title":"Histone H3 K36 methylation is associated with transcription elongation in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2005 Aug;4(8):1446-54","abstract":"Set2 methylation of histone H3 at lysine 36 (K36) has recently been shown to be associated with RNA polymerase II (Pol II) elongation in Saccharomyces cerevisiae. However, whether this modification is conserved and associated with transcription elongation in other organisms is not known. Here we report the identification and characterization of the Set2 ortholog responsible for K36 methylation in the fission yeast Schizosaccharomyces pombe. We find that similar to the budding yeast enzyme, S. pombe Set2 is also a robust nucleosome-selective H3 methyltransferase that is specific for K36. Deletion of the S. pombe set2+ gene results in complete abolishment of K36 methylation as well as a slow-growth phenotype on plates containing synthetic medium. These results indicate that Set2 is the sole enzyme responsible for this modification in fission yeast and is important for cell growth under stressed conditions. Using the chromatin immunoprecipitation assay, we demonstrate that K36 methylation in S. pombe is associated with the transcribed regions of Pol II-regulated genes and is devoid in regions that are not transcribed by Pol II. Consistent with a role for Set2 in transcription elongation, we find that S. pombe Set2 associates with the hyperphosphorylated form of Pol II and can fully rescue K36 methylation and Pol II interaction in budding yeast cells deleted for Set2. These results, along with our finding that K36 methylation is highly conserved among eukaryotes, imply a conserved role for this modification in the transcription elongation process.","authors":"Morris SA, Shibata Y, Noma K, Tsukamoto Y, Warren E, Temple B, Grewal SI, Strahl BD","authors_abbrev":"Morris SA et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-08-10","publication_year":"2005","canto_session_key":"df0514b2d11d29a7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-02-15 18:23:54","canto_approved_date":"2026-02-09 10:05:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-05-14 16:25:33","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":6,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.04","SPBC28F2.12","SPAC1834.04","SPBC1105.11c","SPCC306.04c","SPAC29B12.02c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2024-02-15"},{"uniquename":"PMID:32435206","title":"Posttranslational Arginylation Enzyme Arginyltransferase1 Shows Genetic Interactions With Specific Cellular Pathways  in vivo .","citation":"Front Physiol 2020;11:427","abstract":"Arginyltransferase1 (ATE1) is a conserved enzyme in eukaryotes mediating posttranslational arginylation, the addition of an extra arginine to an existing protein. In mammals, the dysregulations of the ATE1 gene ( ate1 ) is shown to be involved in cardiovascular abnormalities, cancer, and aging-related diseases. Although biochemical evidence suggested that arginylation may be involved in stress response and/or protein degradation, the physiological role of ATE1  in vivo  has never been systematically determined. This gap of knowledge leads to difficulties for interpreting the involvements of ATE1 in diseases pathogenesis. Since  ate1  is highly conserved between human and the unicellular organism  Schizosaccharomyces pombe  ( S. pombe ), we take advantage of the gene-knockout library of  S. pombe , to investigate the genetic interactions between  ate1  and other genes in a systematic and unbiased manner. By this approach, we found that  ate1  has a surprisingly small and focused impact size. Among the 3659 tested genes, which covers nearly 75% of the genome of  S. pombe , less than 5% of them displayed significant genetic interactions with  ate1 . Furthermore, these  ate1 -interacting partners can be grouped into a few discrete clustered categories based on their functions or their physical interactions. These categories include translation/transcription regulation, biosynthesis/metabolism of biomolecules (including histidine), cell morphology and cellular dynamics, response to oxidative or metabolic stress, ribosomal structure and function, and mitochondrial function. Unexpectedly, inconsistent to popular belief, very few genes in the global ubiquitination or degradation pathways showed interactions with  ate1 . Our results suggested that ATE1 specifically regulates a handful of cellular processes  in vivo , which will provide critical mechanistic leads for studying the involvements of ATE1 in normal physiologies as well as in diseased conditions.","doi":"10.3389/fphys.2020.00427","authors":"Wiley DJ, D'Urso G, Zhang F","authors_abbrev":"Wiley DJ et al.","pubmed_publication_date":"2020","pubmed_entrez_date":"2020-05-22","publication_year":"2020","canto_session_key":"192edce4d528c05c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-09-09 14:17:31","canto_approved_date":"2020-09-09 14:17:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-09-09 14:17:23","canto_added_date":"2020-05-23 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":154,"orcid":"0000-0003-4148-4606","file_type":"interaction","file_name":"PMID_32435206_scored_interactions.tab2.txt"}],"genes":["SPBC354.08c","SPCC1393.08","SPAC4F10.11","SPAC16.01","SPAC18G6.05c","SPACUNK4.13c","SPAC23H3.06","SPAC25G10.05c","SPBC6B1.10","SPAC22H10.11c","SPBC405.07","SPAC23C11.04c","SPCC1183.11","SPAC3C7.04","SPCC962.04","SPAC22F8.09","SPBC839.15c","SPAC3C7.08c","SPBC365.10","SPAC26H5.10c","SPCC4F11.04c","SPAC22F8.11","SPCP1E11.10","SPBC776.01","SPAC2F3.08","SPAC6G9.03c","SPBC2F12.11c","SPAC6F12.03c","SPCC285.15c","SPAC589.10c","SPAC732.02c","SPAC144.14","SPBC1921.01c","SPAC13G7.13c","SPAC1486.01","SPCPB16A4.03c","SPAC3H8.05c","SPAC17G8.06c","SPCC1259.01c","SPAC1071.07c","SPBC3B8.03","SPAC23H4.12","SPBC2D10.13","SPAC12B10.10","SPAC10F6.16","SPAC19G12.15c","SPAC1783.07c","SPAPB1E7.02c","SPBC20F10.05","SPAC3G6.09c","SPAC9G1.03c","SPAC1556.05c","SPCC338.08","SPBC14F5.03c","SPBC83.02c","SPAC17C9.11c","SPBC1734.13","SPAC1071.02","SPAC13D6.02c","SPBC29B5.03c","SPBC215.05","SPBC56F2.08c","SPAC22G7.03","SPBC21H7.07c","SPCC584.01c","SPBC56F2.05c","SPAC22F8.04","SPBC1921.03c","SPAC19G12.08","SPCC1223.05c","SPBC1734.11","SPAC14C4.14","SPAC31A2.02","SPCC1919.15","SPBC337.15c","SPAC3F10.09","SPAC6G10.12c","SPCC5E4.07","SPAC144.01","SPAC1851.04c","SPAC1782.11","SPAC25A8.02","SPAC9E9.09c","SPAC3G9.07c","SPAC22F3.12c","SPBC1271.14","SPAC17A5.16","SPBC4C3.06","SPCC553.12c","SPBC17G9.10","SPCC794.01c","SPAC30C2.06c","SPBC19F5.01c","SPAC31A2.13c","SPBC1703.13c","SPCC576.11","SPAC1782.07","SPBC354.07c","SPBC16E9.16c","SPBC31A8.01c","SPCC1259.03","SPBC11C11.07","SPBC19G7.06","SPAC25H1.02","SPAC4G9.16c","SPAP14E8.04","SPAP27G11.06c","SPAC26H5.04","SPAC227.07c","SPBC1D7.03","SPBC1A4.04","SPBC16H5.07c","SPCC61.05","SPBC3H7.07c","SPAC21E11.03c","SPAC4F10.05c","SPCC613.06","SPBC16A3.19","SPBC800.03","SPAC29A4.09","SPBC2G5.06c","SPAC186.08c","SPBC646.02","SPBC29A3.02c","SPAC144.11","SPBCPT2R1.01c","SPAC4G9.15","SPBC106.17c","SPAC15A10.09c","SPAC23C11.10","SPAC6G9.14","SPBC3D6.04c","SPAC29B12.05c","SPBC1773.17c","SPAP11E10.02c","SPBC1711.13","SPAC17C9.02c","SPAC2F3.16","SPAC14C4.01c","SPBC1711.15c","SPAC1093.01","SPCC548.06c","SPAC14C4.12c","SPAC13G6.02c","SPAC2F7.04","SPCC1672.04c","SPAC25G10.06","SPAC3C7.07c","SPBC21C3.20c","SPAC9G1.11c","SPBC1718.07c","SPBC19G7.04","SPAC13C5.07","SPAC31A2.11c","SPBC119.12"],"gene_count":155,"ltp_gene_count":1,"approved_date":"2020-09-09"},{"uniquename":"PMID:15068784","title":"Reconstruction of microtubules; entry into interphase.","citation":"Dev Cell 2004 Apr;6(4):456-8","abstract":"Microtubules display dramatic morphological alterations from mitotic spindles to fibrous interphase structures upon exit from mitosis. In this issue of Developmental Cell, Zimmerman et al. shed a novel light on the molecular mechanism of microtubule structure reorganization during cytokinesis.","authors":"Sato M, Toda T","authors_abbrev":"Sato M et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-04-08","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16434698","title":"A simple and effective chromosome modification method for large-scale deletion of genome sequences and identification of essential genes in fission yeast.","citation":"Nucleic Acids Res 2006 Jan 24;34(2):e11","abstract":"The technologies for chromosome modification developed to date are not satisfactorily universal, owing to the typical requirements for special enzymes and sequences. In the present report, we propose a new approach for chromosome modification in Schizosaccharomyces pombe that does not involve any special enzymes or sequences. This method, designated the 'Latour system', has wide applicability with extremely high efficiency, although both the basic principle and the operation are very simple. We demonstrate the ability of the Latour system to discriminate essential genes, with a long chromosomal area of 100 kb containing 33 genes deleted simultaneously and efficiently. Since no foreign sequences are retained after deletion using the Latour system, this system can be repeatedly applied at other sites. Provided that a negative selectable marker is available, the Latour system relies solely upon homologous recombination, which is highly conserved in living organisms. For this reason, it is expected that the system will be applicable to various yeasts.","authors":"Hirashima K, Iwaki T, Takegawa K, Giga-Hama Y, Tohda H","authors_abbrev":"Hirashima K et al.","pubmed_publication_date":"24 Jan 2006","pubmed_entrez_date":"2006-01-26","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000081","title":"Representation of plant formation as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the formation of a plant structure as a biological process. The underlying equivalence axiom template is \"'anatomical structure formation involved in morphogenesis' and 'results in formation of' some P\", where P is a plant anatomical entity (PO:0025131).","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1318497","title":"Reduction in the intracellular cAMP level triggers initiation of sexual development in fission yeast.","citation":"Mol Gen Genet 1992 May;233(1-2):17-24","abstract":"Schizosaccharomyces pombe initiates sexual development in response to nutritional starvation. The level of cAMP in S. pombe cells changed during the transition from exponential growth to stationary phase. It also changed in response to a shift from nitrogen-rich medium to nitrogen-free medium. A decrease of approximately 50% was observed in either case, suggesting that S. pombe cells contain less cAMP when they initiate sexual development. S. pombe cells that expressed the catalytic domain of Saccharomyces cerevisiae adenylyl cyclase from the S. pombe adh1 promoter contained 5 times as much cAMP as the wild type and could not initiate mating and meiosis. These observations, together with previous findings that exogenously added cAMP inhibits mating and meiosis and that cells with little cAMP are highly derepressed for sexual development, strongly suggest that cAMP functions as a key regulator of sexual development in S. pombe. The pde1 gene, which encodes a protein homologous to S. cerevisiae cAMP phosphodiesterase I, was isolated as a multicopy suppressor of the sterility caused by a high cAMP level. Disruption of pde1 made S. pombe cells partially sterile and meiosis-deficient, indicating that this cAMP phosphodiesterase plays an important role in balancing the cAMP level in vivo.","authors":"Mochizuki N, Yamamoto M","authors_abbrev":"Mochizuki N et al.","pubmed_publication_date":"May 1992","pubmed_entrez_date":"1992-05-01","publication_year":"1992","canto_session_key":"e27e03453e7612c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 19:43:43","canto_approved_date":"2021-01-19 09:09:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-06 09:07:24","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC285.09c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-10"},{"uniquename":"PMID:14643439","title":"Apoptosis-like yeast cell death in response to DNA damage and replication defects.","citation":"Mutat Res 2003 Nov 27;532(1-2):227-43","abstract":"In budding (Saccharomyces cerevisiae) and fission (Schizosaccharomyces pombe) yeast and other unicellular organisms, DNA damage and other stimuli can induce cell death resembling apoptosis in metazoans, including the activation of a recently discovered caspase-like molecule in budding yeast. Induction of apoptotic-like cell death in yeasts requires homologues of cell cycle checkpoint proteins that are often required for apoptosis in metazoan cells. Here, we summarize these findings and our unpublished results which show that an important component of metazoan apoptosis recently detected in budding yeast-reactive oxygen species (ROS)-can also be detected in fission yeast undergoing an apoptotic-like cell death. ROS were detected in fission and budding yeast cells bearing conditional mutations in genes encoding DNA replication initiation proteins and in fission yeast cells with mutations that deregulate cyclin-dependent kinases (CDKs). These mutations may cause DNA damage by permitting entry of cells into S phase with a reduced number of replication forks and/or passage through mitosis with incompletely replicated chromosomes. This may be relevant to the frequent requirement for elevated CDK activity in mammalian apoptosis, and to the recent discovery that the initiation protein Cdc6 is destroyed during apoptosis in mammals and in budding yeast cells exposed to lethal levels of DNA damage. Our data indicate that connections between apoptosis-like cell death and DNA replication or CDK activity are complex. Some apoptosis-like pathways require checkpoint proteins, others are inhibited by them, and others are independent of them. This complexity resembles that of apoptotic pathways in mammalian cells, which are frequently deregulated in cancer. The greater genetic tractability of yeasts should help to delineate these complex pathways and their relationships to cancer and to the effects of apoptosis-inducing drugs that inhibit DNA replication.","authors":"Burhans WC, Weinberger M, Marchetti MA, Ramachandran L, D'Urso G, Huberman JA","authors_abbrev":"Burhans WC et al.","pubmed_publication_date":"27 Nov 2003","pubmed_entrez_date":"2003-12-04","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11414703","title":"The fission yeast ortholog of the coregulator SKIP interacts with the small subunit of U2AF.","citation":"Biochem Biophys Res Commun 2001 Jun 29;284(5):1148-54","abstract":"The mode of action of transcriptional coregulators may involve the recruitment of spliceosome components. Using the two-hybrid screen, we examined the interaction partners of spSNW1, the S. pombe ortholog of the human coregulator SNW1/SKIP/NCoA-62, and found it to interact with the small subunit of the splicing factor U2AF (spU2AF23). The interaction involves the C-terminal parts of spU2AF23 and spSNW1. Tagged variants of both proteins were expressed in S. pombe and the interaction was proved by coprecipitation in nuclear extracts. This interaction would explain the finding of SKIP in nuclear speckles (Mintz, P. J., et al., EMBO J. 18, 4308-4320, 1999) and in reconstituted spliceosomes (Neubauer, G., et al., Nat. Genet. 20, 46-50, 1998). We deleted the spSNW1 gene in the diploid strain and demonstrated that spSNW1 is an essential gene in S. pombe.","authors":"Ambrozková M, Půta F, Fuková I, Skruzný M, Brábek J, Folk P","authors_abbrev":"Ambrozková M et al.","pubmed_publication_date":"29 Jun 2001","pubmed_entrez_date":"2001-06-21","publication_year":"2001","canto_session_key":"d712ca99b02b1957","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-16 12:42:03","canto_approved_date":"2024-02-16 12:42:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-16 12:41:55","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.06","SPCC188.11"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-02-16"},{"uniquename":"EMBL:AB084852","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.40"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24560273","title":"Replication origin selection regulates the distribution of meiotic recombination.","citation":"Mol Cell 2014 Feb 20;53(4):655-62","abstract":"The program of DNA replication, defined by the temporal and spatial pattern of origin activation, is altered during development and in cancers. However, whether changes in origin usage play a role in regulating specific biological processes remains unknown. We investigated the consequences of modifying origin selection on meiosis in fission yeast. Genome-wide changes in the replication program of premeiotic S phase do not affect meiotic progression, indicating that meiosis neither activates nor requires a particular origin pattern. In contrast, local changes in origin efficiencies between different replication programs lead to changes in Rad51 recombination factor binding and recombination frequencies in these domains. We observed similar results for Rad51 when changes in efficiencies were generated by directly targeting expression of the Cdc45 replication factor. We conclude that origin selection is a key determinant for organizing meiotic recombination, providing evidence that genome-wide modifications in replication program can modulate cellular physiology.","doi":"10.1016/j.molcel.2014.01.022","authors":"Wu PY, Nurse P","authors_abbrev":"Wu PY et al.","pubmed_publication_date":"20 Feb 2014","pubmed_entrez_date":"2014-02-25","publication_year":"2014","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2014-04-04 03:36:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24602883","title":"Actin cytoskeleton: a nucleator face-off.","citation":"Curr Biol 2014 Mar 03;24(5):R194-6","abstract":"Actin assembly proteins initiate the formation of diverse cytoskeletal structures in a single cell. A new study shows that assembly factors compete for actin monomers, leading to homeostasis between different actin networks.","doi":"10.1016/j.cub.2014.01.043","authors":"Moseley JB","authors_abbrev":"Moseley JB","pubmed_publication_date":"03 Mar 2014","pubmed_entrez_date":"2014-03-08","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-04-07 00:16:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21673110","title":"Rrn7 protein, an RNA polymerase I transcription factor, is required for RNA polymerase II-dependent transcription directed by core promoters with a HomolD box sequence.","citation":"J Biol Chem 2011 Jul 29;286(30):26480-6","abstract":"The region in promoters that specifies the transcription machinery is called the core promoter, displaying core promoter elements (CPE) necessary for establishment of a preinitiation complex and the initiation of transcription. A classical CPE is the TATA box. In fission yeast, Schizosaccharomyces pombe, a new CPE, called HomolD box, was discovered. Collectively, 141 ribosomal protein genes encoding the full set of 79 different ribosomal proteins and more than 60 other housekeeping genes display a HomolD box in the core promoter. Here, we show that transcription directed by the HomolD box requires the RNA polymerase II machinery, including the general transcription factors. Most intriguingly, however, we identify, by DNA affinity purification, Rrn7 as the protein binding to the HomolD box. Rrn7 is an evolutionary conserved member of the RNA polymerase I machinery involved in transcription initiation of core ribosomal DNA promoters. ChIP shows that Rrn7 cross-links to a ribosomal protein gene promoter containing the HomolD box but not to a promoter containing a TATA box. Taken together, our results suggest that Rrn7 is an excellent candidate to be involved in the coordination of ribosomal DNA and ribosomal gene transcription during ribosome synthesis and, therefore, offer a new perspective to study conservation and evolvability of regulatory networks in eukaryotes.","doi":"10.1074/jbc.M111.224337","authors":"Rojas DA, Moreira-Ramos S, Zock-Emmenthal S, Urbina F, Contreras-Levicoy J, Käufer NF, Maldonado E","authors_abbrev":"Rojas DA et al.","pubmed_publication_date":"29 Jul 2011","pubmed_entrez_date":"2011-06-16","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12193640","title":"Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi.","citation":"Science 2002 Sep 13;297(5588):1833-7","abstract":"Eukaryotic heterochromatin is characterized by a high density of repeats and transposons, as well as by modified histones, and influences both gene expression and chromosome segregation. In the fission yeast Schizosaccharomyces pombe, we deleted the argonaute, dicer, and RNA-dependent RNA polymerase gene homologs, which encode part of the machinery responsible for RNA interference (RNAi). Deletion results in the aberrant accumulation of complementary transcripts from centromeric heterochromatic repeats. This is accompanied by transcriptional de-repression of transgenes integrated at the centromere, loss of histone H3 lysine-9 methylation, and impairment of centromere function. We propose that double-stranded RNA arising from centromeric repeats targets formation and maintenance of heterochromatin through RNAi.","authors":"Volpe TA, Kidner C, Hall IM, Teng G, Grewal SI, Martienssen RA","authors_abbrev":"Volpe TA et al.","pubmed_publication_date":"13 Sep 2002","pubmed_entrez_date":"2002-08-24","publication_year":"2002","canto_session_key":"1e28c66329150744","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-01-25 10:04:55","canto_approved_date":"2024-01-25 10:04:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-19 17:09:39","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":23,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c","SPCC736.11","SPAC6F12.09","SPAC664.01c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2024-01-25"},{"uniquename":"PMID:16980386","title":"Linear element-independent meiotic recombination in Schizosaccharomyces pombe.","citation":"Genetics 2006 Nov;174(3):1105-14","abstract":"Most organisms form protein-rich, linear, ladder-like structures associated with chromosomes during early meiosis, the synaptonemal complex. In Schizosaccharomyces pombe, linear elements (LinEs) are thread-like, proteinacious chromosome-associated structures that form during early meiosis. LinEs are related to axial elements, the synaptonemal complex precursors of other organisms. Previous studies have led to the suggestion that axial structures are essential to mediate meiotic recombination. Rec10 protein is a major component of S. pombe LinEs and is required for their development. In this report we study recombination in a number of rec10 mutants, one of which (rec10-155) does not form LinEs, but is predicted to encode a truncated Rec10 protein. This mutant has levels of crossing over and gene conversion substantially higher than a rec10 null mutant (rec10-175) and forms cytologically detectable Rad51 foci indicative of meiotic recombination intermediates. These data demonstrate that while Rec10 is required for meiotic recombination, substantial meiotic recombination can occur in rec10 mutants that do not form LinEs, indicating that LinEs per se are not essential for all meiotic recombination.","authors":"Wells JL, Pryce DW, Estreicher A, Loidl J, McFarlane RJ","authors_abbrev":"Wells JL et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2006-09-19","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38583078","title":"Live-cell fluorescence imaging and optogenetic control of PKA kinase activity in fission yeast Schizosaccharomyces pombe.","citation":"Yeast 2024 Apr 07;","abstract":"The cAMP-PKA signaling pathway plays a crucial role in sensing and responding to nutrient availability in the fission yeast Schizosaccharomyces pombe. This pathway monitors external glucose levels to control cell growth and sexual differentiation. However, the temporal dynamics of the cAMP-PKA pathway in response to external stimuli remains unclear mainly due to the lack of tools to quantitatively visualize the activity of the pathway. Here, we report the development of the kinase translocation reporter (KTR)-based biosensor spPKA-KTR1.0, which allows us to measure the dynamics of PKA activity in fission yeast cells. The spPKA-KTR1.0 is derived from the transcription factor Rst2, which translocates from the nucleus to the cytoplasm upon PKA activation. We found that spPKA-KTR1.0 translocates between the nucleus and cytoplasm in a cAMP-PKA pathway-dependent manner, indicating that the spPKA-KTR1.0 is a reliable indicator of the PKA activity in fission yeast cells. In addition, we implemented a system that simultaneously visualizes and manipulates the cAMP-PKA signaling dynamics by introducing bPAC, a photoactivatable adenylate cyclase, in combination with spPKA-KTR1.0. This system offers an opportunity for investigating the role of the signaling dynamics of the cAMP-PKA pathway in fission yeast cells with higher temporal resolution.","doi":"10.1002/yea.3937","authors":"Sakai K, Aoki K, Goto Y","authors_abbrev":"Sakai K et al.","pubmed_publication_date":"07 Apr 2024","pubmed_entrez_date":"2024-04-07","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-04-07 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6765174","title":"Expression of the cloned uracil permease gene of Saccharomyces cerevisiae in a heterologous membrane.","citation":"EMBO J 1982;1(3):375-7","abstract":"A piece of DNA of the yeast Saccharomyces cerevisiae complementing the uracil permease gene was introduced into a plasmid able to replicate autonomously in Schizosaccharomyces pombe. A strain of S. pombe lacking uracil transport activity was transformed with this new plasmid carrying the gene of S. cerevisiae. The behaviour of the transformant shows not only an expression of the uracil permease gene in the heterologous membrane but also that the transport of uracil is active and coupled to the energy furnishing system of the heterologous host.","authors":"Chevallier MR, Lacroute F","authors_abbrev":"Chevallier MR et al.","pubmed_publication_date":"1982","pubmed_entrez_date":"1982-01-01","publication_year":"1982","canto_session_key":"241f95f5abd9008e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-09-17 20:49:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-25 12:17:55","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1399.03","SPCC330.05c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2013-09-25"},{"uniquename":"PMID:33035200","title":"Non-random distribution of vacuoles in Schizosaccharomyces pombe.","citation":"Phys Biol 2020 Oct 09;17(6):065004","abstract":"A central question in eukaryotic cell biology asks, during cell division, how is the growth and distribution of organelles regulated to ensure each daughter cell receives an appropriate amount. For vacuoles in budding yeast, there are well described organelle-to-cell size scaling trends as well as inheritance mechanisms involving highly coordinated movements. It is unclear whether such mechanisms are necessary in the symmetrically dividing fission yeast, Schizosaccharomyces pombe, in which random partitioning may be utilized to distribute vacuoles to daughter cells. To address the increasing need for high-throughput analysis, we are augmenting existing semi-automated image processing by developing fully automated machine learning methods for locating vacuoles and segmenting fission yeast cells from brightfield and fluorescence micrographs. All strains studied show qualitative correlations in vacuole-to-cell size scaling trends, i.e. vacuole volume, surface area, and number all increase with cell size. Furthermore, increasing vacuole number was found to be a consistent mechanism for the increase in total vacuole size in the cell. Vacuoles are not distributed evenly throughout the cell with respect to available cytoplasm. Rather, vacuoles show distinct peaks in distribution close to the nucleus, and this preferential localization was confirmed in mutants in which nucleus position is perturbed. Disruption of microtubules leads to quantitative changes in both vacuole size scaling trends and distribution patterns, indicating the microtubule cytoskeleton is a key mechanism for maintaining vacuole structure.","doi":"10.1088/1478-3975/aba510","authors":"Chadwick WL, Biswas SK, Bianco S, Chan YM","authors_abbrev":"Chadwick WL et al.","pubmed_publication_date":"09 Oct 2020","pubmed_entrez_date":"2020-10-09","publication_year":"2020","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2020-10-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30395243","title":"Genome-wide transcriptional response to altered levels of the Rpb7 subunit of RNA polymerase II identifies its role in DNA damage response in Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2019 Jan 01;19(1)","abstract":"Transcription of protein-coding genes is a highly regulated process. In eukaryotes, it involves cross-talk between the RNA polymerase II enzyme and different proteins of the transcriptional machinery. Twelve different subunits, Rpb1 to Rpb12, constitute RNA polymerase II. The sequence of the Rpb7 subunit is highly conserved across organisms. However, our knowledge and understanding of the role of Rpb7 in Schizosaccharomyces pombe is still limited. Therefore, in the present study we have studied the transcriptional response of S. pombe cells expressing reduced levels of rpb7+. Our global transcriptional analysis revealed that expression of genes belonging to different DNA repair pathways was downregulated by reduced rpb7+ expression. It was observed that survival of S. pombe cells expressing low rpb7+ levels was compromised under genotoxic stress conditions. Rpb7 also exhibited genetic interaction with genes of various DNA repair pathways. Furthermore, the growth sensitivity of S. pombe cells with low rpb7+ levels under DNA-damaging conditions was completely rescued by human Rpb7, indicating a functional conservation between these proteins. In summary, results from our whole-genome level gene expression analysis, as well as phenotypic and genetic experiments suggest a role for Rpb7 in DNA damage response in S. pombe.","doi":"10.1093/femsyr/foy118","authors":"Kumar D, Sharma N","authors_abbrev":"Kumar D et al.","pubmed_publication_date":"01 Jan 2019","pubmed_entrez_date":"2018-11-06","publication_year":"2019","canto_session_key":"43b227a2fd5ba314","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-11-07 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007268","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11566197","title":"Ca(2+) and H+ homeostasis in fission yeast: a role of Ca(2+)/H+ exchange and distinct V-H+-ATPases of the secretory pathway organelles.","citation":"FEBS Lett 2001 Sep 14;505(2):321-4","abstract":"We determined the H+ and Ca(2+) uptake by fission yeast membranes separated on sucrose gradient and found that (i) Ca(2+) sequestering is due to Ca(2+)/H+ antiporter(s) localized to secretory pathway organelles while Ca(2+)-ATPase activity is not detectable in their membranes; (ii) immunochemically distinct V-H+-ATPases acidify the lumen of the secretory pathway organelles. The data indicate that the endoplasmic reticulum, Golgi and vacuole form a network of Ca(2+) and H+ stores in the single cell, providing favorable conditions for such key processes as protein folding/sorting, membrane fusion, ion homeostasis and Ca(2+) signaling in a differential and local manner.","authors":"Okorokov LA, Silva FE, Okorokova Façanha AL","authors_abbrev":"Okorokov LA et al.","pubmed_publication_date":"14 Sep 2001","pubmed_entrez_date":"2001-09-22","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9675818","title":"The C-terminal hydrophobic repeat of Schizosaccharomyces pombe heat shock factor is not required for heat-induced DNA-binding.","citation":"Yeast 1998 Jun 15;14(8):733-46","abstract":"The C-terminal hydrophobic repeat (CTR) of heat shock transcription factor (HSF) has been proposed to regulate DNA binding by intramolecular interactions with the leucine zipper motifs present in the HSF trimerization domain. Schizosaccharomyces pombe provides a useful model organism for the study of the regulation of HSF DNA binding because, unlike Saccharomyces cerevisiae, S. pombe hsf is highly heat shock inducible for DNA binding and contains a clear homology to the CTR. We examined the role that the CTR plays in the regulation of S. pombe hsf by constructing isogenic strains bearing deletion and point mutations in the chromosomal copy of hsf. Surprisingly, we found that point mutation of key hydrophobic amino acids within the CTR, as well as full deletion of it, yielded factors that show normal binding at normal growth temperatures and full levels of heat-induced binding. Deletion of the CTR did, however, slightly lower the temperature required for maximal activation. In contrast, a large deletion of the C-terminus, which removes close to a third of the coding sequence, was deregulated and bound DNA at control temperature. Several of the deletion mutants were significantly reduced in their level of expression, yet they showed wild-type levels of DNA binding activity following heat shock. These experiments demonstrate that appropriate regulation of the DNA binding activity of S. pombe hsf is not solely dependent upon the CTR, and imply that a feedback mechanism exists that establishes proper levels of DNA binding following heat shock despite mutations that significantly alter levels of total hsf.","authors":"Saltsman KA, Prentice HL, Kingston RE","authors_abbrev":"Saltsman KA et al.","pubmed_publication_date":"15 Jun 1998","pubmed_entrez_date":"1998-07-24","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12100563","title":"Diethylmaleate activates the transcription factor Pap1 by covalent modification of critical cysteine residues.","citation":"Mol Microbiol 2002 Jul;45(1):243-54","abstract":"During the last decade, much has been learnt about the mechanisms by which oxidative stress is perceived by aerobic organisms. The Schizosaccharomyces pombe Pap1 protein is a transcription factor localized at the cytoplasm, which accumulates in the nucleus in response to different inducers, such as the pro-oxidant hydrogen peroxide (H2O2) or the glutathione-depleting agent diethylmaleate (DEM). As described for other H2O2 sensors, our genetic data indicates that H2O2 reversibly oxidizes two cysteine residues in Pap1 (Cys278 and Cys501). Surprisingly, our studies demonstrate that DEM generates a non-reversible modification of at least two cysteine residues located in or close to the nuclear export signal of Pap1 (Cys523 and Cys532). This modification impedes the interaction of the nuclear exporter Crm1 with the nuclear export signal located at the carboxy-terminal domain of Pap1. Mass spectrometry data suggest that DEM binds to the thiol groups of the target cysteine residues through the formation of a thioether. Here we show that DEM triggers Pap1 nuclear accumulation by a novel molecular mechanism.","authors":"Castillo EA, Ayté J, Chiva C, Moldón A, Carrascal M, Abián J, Jones N, Hidalgo E","authors_abbrev":"Castillo EA et al.","pubmed_publication_date":"Jul 2002","pubmed_entrez_date":"2002-07-09","publication_year":"2002","canto_session_key":"bd17578dd6875e29","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-06-06 15:25:46","canto_approved_date":"2022-05-27 06:43:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-17 11:13:21","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":26,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1805.17","SPBC3F6.03","SPAC1783.07c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2013-06-06"},{"uniquename":"PMID:26743946","title":"The (elusive) role of the SMC5/6 complex.","citation":"Cell Cycle 2016;15(6):775-6","abstract":"","doi":"10.1080/15384101.2015.1137713","authors":"Fernandez-Capetillo O","authors_abbrev":"Fernandez-Capetillo O","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-01-09","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-12-17 01:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41744897","title":"Ifn1 is an intracellular GMP 5'-nucleotidase induced during the fission yeast response to phosphate starvation.","citation":"mBio 2026 Feb 26;:e0394225","abstract":" Schizosaccharomyces pombe  adapts to phosphate starvation by upregulating the expression of (i) a cell-surface acid phosphatase, Pho1, that mobilizes inorganic phosphate from the extracellular milieu; (ii) transmembrane transporters that take up inorganic phosphate (Pho84, Pho841, and Pho842) and glycerophosphocholine (Tgp1); and (iii) secreted extracellular 5'-nucleotidase enzymes (Efn1 and Efn2) that release inorganic phosphate from rNMPs, with a preference for CMP. The expression of SPAC24B11.05, a fission yeast homolog of the budding yeast 5'-nucleotidase Sdt1, is upregulated during phosphate starvation, and the protein accumulates without being secreted. Here, we characterized recombinant SPAC24B11.05 (herein Ifn1, for intracellular 5'-nucleotidase) as a Mg 2+ -dependent phosphohydrolase of the aspartyl-phosphatase (HAD) superfamily. Unlike Sdt1, which is specific for pyrimidine mononucleotides and nicotinamide mononucleotide (NMN), Ifn1 displays a preference for hydrolysis of GMP > IMP > CMP > AMP > UMP and is unable to hydrolyze NMN. Ifn1 activity is abolished by alanine mutations of the Asp11 nucleophile of the signature  11  D LDNC 15  motif and by alanines in lieu of Asp80 and Asp174 that are predicted to coordinate the ribose hydroxyls and the metal cofactor, respectively. Changing Ifn1 Arg50, which is predicted to engage the guanine nucleobase, to Asn, the corresponding residue in Sdt1, enhances hydrolysis of CMP and AMP and suppresses hydrolysis of GMP, IMP, and UMP, with no gain of activity with NMN. We find that overexpression of catalytically active Ifn1 is toxic to fission yeast.IMPORTANCEPhosphate starvation in fission yeast triggers increased expression of enzymes with imputed roles in phosphate dynamics. Many starvation-induced phosphohydrolases are annotated as acting on nucleotides, though their substrate specificities have not been interrogated. Here, we characterize fission yeast Ifn1 as a starvation-induced 5'-nucleotidase of the aspartyl-phosphatase (HAD) superfamily with a preference for hydrolysis of GMP and IMP that distinguishes it from the homologous budding yeast pyrimidine-specific 5'-nucleotidase Sdt1. A single swap of Ifn1 Arg50 to Asn (the equivalent position in Sdt1) elicits a substrate switch, manifested as a gain of activity with CMP and suppression of activity with GMP and IMP. An emergent theme is that 5'-nucleotidase substrate specificity is a tunable property.","doi":"10.1128/mbio.03942-25","authors":"Innokentev A, Schwer B, Shuman S","authors_abbrev":"Innokentev A et al.","pubmed_publication_date":"26 Feb 2026","pubmed_entrez_date":"2026-02-26","publication_year":"2026","canto_session_key":"0d1398eaa9b48533","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Innokentev Aleksei","canto_first_approved_date":"2026-05-22 06:01:14","canto_approved_date":"2026-05-22 06:01:14","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-03-26 19:51:05","canto_added_date":"2026-02-27 00:25:07","annotation_curators":[{"name":"Innokentev Aleksei","community_curator":true,"annotation_count":4,"orcid":"0009-0007-0407-476X","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":10,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.05"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2026-05-22"},{"uniquename":"PMID:12696147","title":"[RNA binding protein Mei2, a master regulator of meiosis].","citation":"Tanpakushitsu Kakusan Koso 2003 Mar;48(4 Suppl):398-403","abstract":"","authors":"Watanabe Y","authors_abbrev":"Watanabe Y","pubmed_publication_date":"Mar 2003","pubmed_entrez_date":"2003-04-17","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32372157","title":"Characterisation of unessential genes required for survival under conditions of DNA stress.","citation":"J Genet Eng Biotechnol 2020 May 06;18(1):14","abstract":"Genomic instability is a hallmark of cancer. Cancer progression depends on the development and amplification of mutations that alter the cellular response to threats to the genome. This can lead to DNA replication stress and the potential loss of genetic integrity of the newly formed cells. This study utilised fission yeast to map the interactions occurring in some of the most crucial pathways in both DNA replication and checkpoint monitoring involving Rad4, the Schizosaccharomyces pombe (S. pombe) TopBP1 homologue. We have modelled conditions of replication stress in the genetically tractable fission yeast, S. pombe using the hypomorphic rad4-116 allele. Synthetic genetic analysis was used to identify processes required for cell survival under conditions of DNA replication stress. With the aim of mapping the genetic interactions of rad4 and its mutant allele, rad4-116, several genes that could have an interaction with rad4 during replication stress have emerged as attractive.\nInteractions with genes involved in chromatin remodelling, such as hip1, and replication fork stalling resolution, such as mrc1, swi1 and swi3 were explored and confirmed. The interactions of Rad4 with each of the genes provided separate and distinct tumour formation pathways, as evident in the synthetically lethal interactions. Even within the same complex, rad4-116 double mutants behaved differently proving that Rad4 interacts at different levels and functions with the same proteins.\nResults from this study provide a novel view of the rad4 interactions, the association of Rad4 with the replisome. The study also provides the groundwork on a theoretical and practical level for the exploration and separation of interactions of TopBP1 with the histone chaperone family and the replisome.","doi":"10.1186/s43141-020-00025-x","authors":"Ahmed Ezzat H, Price C","authors_abbrev":"Ahmed Ezzat H et al.","pubmed_publication_date":"06 May 2020","pubmed_entrez_date":"2020-05-07","publication_year":"2020","canto_session_key":"03b83a8274fb915a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-05-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.06c","SPAC23C4.18c","SPBC30D10.04","SPAC694.06c","SPBC31F10.13c"],"gene_count":5,"ltp_gene_count":0},{"uniquename":"PMID:356943","title":"Germination and outgrowth of Schizosaccharomyces pombe ascospores isolated by Urografin density gradient centrifugation.","citation":"Can J Microbiol 1978 Aug;24(8):893-7","abstract":"A simple method for the isolation of single ascospores of the fission yeast Schizosaccharomyces pombe was examined. Single spores in the 7-day-old sporulating culture of a homothallic strain were separated from remaining vegetative cells by isopycnic centrifugation in the linear gradient from 10 to 60% of Urografin solution at 700 X g for 20 min. Protein content of isolated spores was very low as compared with that of vegetative cells. The isolated spores germinated through the following steps when cultured in a liquid medium at 25--35 degrees C; loss of refractility (darkening) under a phase-contrast microscope, spherical growth (swelling), emergence of germ tubes, elongation of germ tubes, cell plate formation, and cell separation. The absorbance at 650 nm of the spore suspension initially decreased, accompanied by darkening of spores, and then increased with spherical growth. The germination rate of isolated spores reached almost 100%.","authors":"Nishi K, Shimoda C, Hayashibe M","authors_abbrev":"Nishi K et al.","pubmed_publication_date":"Aug 1978","pubmed_entrez_date":"1978-08-01","publication_year":"1978","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36574843","title":"Regulation of cell size and Wee1 kinase by elevated levels of the cell cycle regulatory protein kinase Cdr2.","citation":"J Biol Chem 2023 Feb;299(2):102831","abstract":"Many cell cycle regulatory proteins catalyze cell cycle progression in a concentration-dependent manner. In the fission yeast Schizosaccharomyces pombe, the protein kinase Cdr2 promotes mitotic entry by organizing cortical oligomeric nodes that lead to inhibition of Wee1, which itself inhibits the cyclin-dependent kinase Cdk1. cdr2Δ cells lack nodes and divide at increased size due to overactive Wee1, but it has not been known how increased Cdr2 levels might impact Wee1 and cell size. It also has not been clear if and how Cdr2 might regulate Wee1 in the absence of the related kinase Cdr1/Nim1. Using a tetracycline-inducible expression system, we found that a 6× increase in Cdr2 expression caused hyperphosphorylation of Wee1 and reduction in cell size even in the absence of Cdr1/Nim1. This overexpressed Cdr2 formed clusters that sequestered Wee1 adjacent to the nuclear envelope. Cdr2 mutants that disrupt either kinase activity or clustering ability failed to sequester Wee1 and to reduce cell size. We propose that Cdr2 acts as a dosage-dependent regulator of cell size by sequestering its substrate Wee1 in cytoplasmic clusters, away from Cdk1 in the nucleus. This mechanism has implications for other clustered kinases, which may act similarly by sequestering substrates.","doi":"10.1016/j.jbc.2022.102831","authors":"Berg RA, Moseley JB","authors_abbrev":"Berg RA et al.","pubmed_publication_date":"Feb 2023","pubmed_entrez_date":"2022-12-27","publication_year":"2023","canto_session_key":"b85e8d183eac4d18","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Rachel Berg","canto_first_approved_date":"2023-12-31 22:10:21","canto_approved_date":"2023-12-31 22:10:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-18 18:08:28","canto_added_date":"2022-12-29 01:15:05","annotation_curators":[{"name":"Rachel Berg","community_curator":true,"annotation_count":17,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPCC4B3.15","SPAC644.06c","SPBC1539.08","SPCC18B5.03"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2023-12-31"},{"uniquename":"PMID:26720005","title":"RNA Polymerase III Output Is Functionally Linked to tRNA Dimethyl-G26 Modification.","citation":"PLoS Genet 2015 Dec;11(12):e1005671","abstract":"Control of the differential abundance or activity of tRNAs can be important determinants of gene regulation. RNA polymerase (RNAP) III synthesizes all tRNAs in eukaryotes and it derepression is associated with cancer. Maf1 is a conserved general repressor of RNAP III under the control of the target of rapamycin (TOR) that acts to integrate transcriptional output and protein synthetic demand toward metabolic economy. Studies in budding yeast have indicated that the global tRNA gene activation that occurs with derepression of RNAP III via maf1-deletion is accompanied by a paradoxical loss of tRNA-mediated nonsense suppressor activity, manifested as an antisuppression phenotype, by an unknown mechanism. We show that maf1-antisuppression also occurs in the fission yeast S. pombe amidst general activation of RNAP III. We used tRNA-HydroSeq to document that little changes occurred in the relative levels of different tRNAs in maf1Δ cells. By contrast, the efficiency of N2,N2-dimethyl G26 (m(2)2G26) modification on certain tRNAs was decreased in response to maf1-deletion and associated with antisuppression, and was validated by other methods. Over-expression of Trm1, which produces m(2)2G26, reversed maf1-antisuppression. A model that emerges is that competition by increased tRNA levels in maf1Δ cells leads to m(2)2G26 hypomodification due to limiting Trm1, reducing the activity of suppressor-tRNASerUCA and accounting for antisuppression. Consistent with this, we show that RNAP III mutations associated with hypomyelinating leukodystrophy decrease tRNA transcription, increase m(2)2G26 efficiency and reverse antisuppression. Extending this more broadly, we show that a decrease in tRNA synthesis by treatment with rapamycin leads to increased m(2)2G26 modification and that this response is conserved among highly divergent yeasts and human cells.","doi":"10.1371/journal.pgen.1005671","authors":"Arimbasseri AG, Blewett NH, Iben JR, Lamichhane TN, Cherkasova V, Hafner M, Maraia RJ","authors_abbrev":"Arimbasseri AG et al.","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2016-01-01","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-01-02 01:20:18","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31G5.12c","SPBC25D12.05"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:1986225","title":"Regulation of heat shock factor in Schizosaccharomyces pombe more closely resembles regulation in mammals than in Saccharomyces cerevisiae.","citation":"Mol Cell Biol 1991 Jan;11(1):281-8","abstract":"The heat shock response appears to be universal. All eucaryotes studied encode a protein, heat shock factor (HSF), that is believed to regulate transcription of heat shock genes. This protein binds to a regulatory sequence, the heat shock element, that is absolutely conserved among eucaryotes. We report here the identification of HSF in the fission yeast Schizosaccharomyces pombe. HSF binding was not observed in extracts from normally growing S. pombe (28 degrees C) but was detected in increasing amounts as the temperature of heat shock increased between 39 and 45 degrees C. This regulation is in contrast to that observed in Saccharomyces cerevisiae, in which HSF binding is detectable at both normal and heat shock temperatures. The S. pombe factor bound specifically to the heat shock element, as judged by methylation interference and DNase I protection analysis. The induction of S. pombe HSF was not inhibited by cycloheximide, suggesting that induction occurs posttranslationally, and the induced factor was shown to be phosphorylated. S. pombe HSF was purified to near homogeneity and was shown to have an apparent mobility of approximately 108 kDa. Since heat-induced DNA binding by HSF had previously been demonstrated only in metazoans, the conservation of heat-induced DNA binding by HSF among S. pombe and metazoans suggests that this mode of regulation is evolutionarily ancient.","authors":"Gallo GJ, Schuetz TJ, Kingston RE","authors_abbrev":"Gallo GJ et al.","pubmed_publication_date":"Jan 1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_session_key":"ef9d86a4bd905168","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-12 15:51:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 15:50:46","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2E12.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-03-12"},{"uniquename":"PMID:30513113","title":"Adding phosphorylation events to the core oscillator driving the cell cycle of fission yeast.","citation":"PLoS One 2018;13(12):e0208515","abstract":"Much is known about the regulatory elements controlling the cell cycle in fission yeast (Schizosaccharomyces pombe). This regulation is mainly done by the (cyclin-dependent kinase/cyclin) complex (Cdc2/Cdc13) that activates specific target genes and proteins via phosphorylation events during the cell cycle in a time-dependent manner. However, more work is still needed to complement the existing gaps in the current fission yeast gene regulatory network to be able to overcome abnormalities in its growth, repair and development, i.e. explain many phenomena including mitotic catastrophe. In this work we complement the previously presented core oscillator of the cell cycle of fission yeast by selected phosphorylation events and study their effects on the temporal evolution of the core oscillator based Boolean network. Thereby, we attempt to establish a regulatory link between the autonomous cell cycle oscillator and the remainder of the cell. We suggest the unclear yet regulatory effect of phosphorylation on the added components, and discuss many unreported points regarding the temporal evolution of the cell cycle and its components. To better visualize the results regardless of the programming background we developed an Android application that can be used to run the core and extended model of the fission yeast cell cycle step by step.","doi":"10.1371/journal.pone.0208515","authors":"Humaidan D, Breinig F, Helms V","authors_abbrev":"Humaidan D et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-12-05","publication_year":"2018","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-12-06 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21847092","title":"An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer.","citation":"EMBO J 2011 Aug 16;30(20):4223-35","abstract":"Dicer proteins function in RNA interference (RNAi) pathways by generating small RNAs (sRNAs). Here, we report the solution structure of the C-terminal domain of Schizosaccharomyces pombe Dicer (Dcr1). The structure reveals an unusual double-stranded RNA binding domain (dsRBD) fold embedding a novel zinc-binding motif that is conserved among dicers in yeast. Although the C-terminal domain of Dcr1 still binds nucleic acids, this property is dispensable for proper functioning of Dcr1. In contrast, disruption of zinc coordination renders Dcr1 mainly cytoplasmic and leads to remarkable changes in gene expression and loss of heterochromatin assembly. In summary, our results reveal novel insights into the mechanism of nuclear retention of Dcr1 and raise the possibility that this new class of dsRBDs might generally function in nucleocytoplasmic trafficking and not substrate binding. The C-terminal domain of Dcr1 constitutes a novel regulatory module that might represent a potential target for therapeutic intervention with fungal diseases.","doi":"10.1038/emboj.2011.300","authors":"Barraud P, Emmerth S, Shimada Y, Hotz HR, Allain FH, Bühler M","authors_abbrev":"Barraud P et al.","pubmed_publication_date":"16 Aug 2011","pubmed_entrez_date":"2011-08-18","publication_year":"2011","canto_session_key":"797e7567a449409b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Marc Buehler","canto_first_approved_date":"2016-06-16 14:53:09","canto_approved_date":"2022-02-23 12:17:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-08 09:49:56","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":29,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Marc Buehler","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-06-16","pdb_entries":[{"pdb_id":"2l6m","gene_chains":[{"gene_uniquename":"SPCC188.13c","chain":"A","position":"1259-1358"}],"title":"Structure of C-terminal dsRBD of the Fission Yeast DICER (Dcr1)","entry_authors":"Barraud P,Allain FH-T","entry_authors_abbrev":"Barraud P et al.","reference_uniquename":"PMID:21847092","experimental_method":"NMR","resolution":""}]},{"uniquename":"PMID:7687541","title":"Regulation of RNA processing and transport by a nuclear guanine nucleotide release protein and members of the Ras superfamily.","citation":"EMBO J 1993 Jul;12(7):2929-37","abstract":"The RCC1 gene of mammals encodes a guanine nucleotide release protein (GNRP). RCC1 and a homolog in Saccharomyces cerevisiae (MTR1/PRP20/SRM1) have previously been implicated in control of mRNA metabolism and export from the nucleus. We here demonstrate that a temperature-sensitive fission yeast mutant which has a mutation in a homologous gene, and two of three additional (mtr1/prp20/srm1) mutants accumulate nuclear poly(A)+ RNA at 37 degrees C. In S.cerevisiae, maturation of rRNA and tRNA is also inhibited at 37 degrees C. Nevertheless, studies with the corresponding BHK-21 cell mutant indicate that protein import into the nucleus continues. MTR1 homologs regulate RNA processing at a point which is distinct from their regulation of chromosome condensation since: (i) poly(A)+ RNA accumulation in the fission yeast mutant precedes chromosome condensation, and (ii) unlike chromosome condensation, accumulation of nuclear poly(A)+ RNA does not require p34cdc28 kinase activation or protein synthesis. Moreover, experiments involving inhibition of DNA synthesis indicate that the S.cerevisiae homolog does not govern cell cycle checkpoint control. Since RCC1p acts as GNRP for Ran, a small nuclear GTPase of the ras superfamily, we have identified two homologs of Ran in S.cerevisiae (CNR1 and CNR2). Only CNR1 is essential, but both code for proteins extremely similar to Ran and can suppress mtr1 mutations in allele-specific fashion. Thus, MTR1 and its homologs appear to act as GNRPs for a family of conserved GTPases in controlling RNA metabolism and transport. Their role in governing checkpoint control appears to be restricted to higher eukaryotes.","authors":"Kadowaki T, Goldfarb D, Spitz LM, Tartakoff AM, Ohno M","authors_abbrev":"Kadowaki T et al.","pubmed_publication_date":"Jul 1993","pubmed_entrez_date":"1993-07-01","publication_year":"1993","canto_session_key":"fe11aad740874c4e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-10-10 19:27:29","canto_approved_date":"2018-10-10 19:27:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-10 19:26:50","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC557.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-10"},{"uniquename":"PMID:24733494","title":"Rapid regulation of nuclear proteins by rapamycin-induced translocation in fission yeast.","citation":"Yeast 2014 Jul;31(7):253-64","abstract":"Genetic analysis of protein function requires a rapid means of inactivating the gene under study. Typically, this exploits temperature-sensitive mutations or promoter shut-off techniques. We report the adaptation to Schizosaccharomyces pombe of the anchor-away technique, originally designed in budding yeast by Laemmli lab. This method relies on a rapamycin-mediated interaction between the FRB- and FKBP12-binding domains to relocalize nuclear proteins of interest to the cytoplasm. We demonstrate a rapid nuclear depletion of abundant proteins as proof of principle.","doi":"10.1002/yea.3014","authors":"Ding L, Laor D, Weisman R, Forsburg SL","authors_abbrev":"Ding L et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-04-16","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15215412","title":"Proteome Analyst: custom predictions with explanations in a web-based tool for high-throughput proteome annotations.","citation":"Nucleic Acids Res 2004 Jul 01;32(Web Server issue):W365-71","abstract":"Proteome Analyst (PA) (http://www.cs.ualberta.ca/~bioinfo/PA/) is a publicly available, high-throughput, web-based system for predicting various properties of each protein in an entire proteome. Using machine-learned classifiers, PA can predict, for example, the GeneQuiz general function and Gene Ontology (GO) molecular function of a protein. In addition, PA is currently the most accurate and most comprehensive system for predicting subcellular localization, the location within a cell where a protein performs its main function. Two other capabilities of PA are notable. First, PA can create a custom classifier to predict a new property, without requiring any programming, based on labeled training data (i.e. a set of examples, each with the correct classification label) provided by a user. PA has been used to create custom classifiers for potassium-ion channel proteins and other general function ontologies. Second, PA provides a sophisticated explanation feature that shows why one prediction is chosen over another. The PA system produces a Naïve Bayes classifier, which is amenable to a graphical and interactive approach to explanations for its predictions; transparent predictions increase the user's confidence in, and understanding of, PA.","authors":"Szafron D, Lu P, Greiner R, Wishart DS, Poulin B, Eisner R, Lu Z, Anvik J, Macdonell C, Fyshe A, Meeuwis D","authors_abbrev":"Szafron D et al.","pubmed_publication_date":"01 Jul 2004","pubmed_entrez_date":"2004-06-25","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-09-21 00:12:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000043","title":"Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping","abstract":"Transitive assignments using UniProtKB/Swiss-Prot keywords. The UniProtKB keyword controlled vocabulary contains 10 different categories of information to UniProtKB entries. Further information on the UniProtKB keyword resource can be found at https://www.uniprot.org/keywords/.","authors":"UniProt-GOA","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3F10.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30715423","title":"Queuine links translational control in eukaryotes to a micronutrient from bacteria.","citation":"Nucleic Acids Res 2019 Apr 23;47(7):3711-3727","abstract":"In eukaryotes, the wobble position of tRNA with a GUN anticodon is modified to the 7-deaza-guanosine derivative queuosine (Q34), but the original source of Q is bacterial, since Q is synthesized by eubacteria and salvaged by eukaryotes for incorporation into tRNA. Q34 modification stimulates Dnmt2/Pmt1-dependent C38 methylation (m5C38) in the tRNAAsp anticodon loop in Schizosaccharomyces pombe. Here, we show by ribosome profiling in S. pombe that Q modification enhances the translational speed of the C-ending codons for aspartate (GAC) and histidine (CAC) and reduces that of U-ending codons for asparagine (AAU) and tyrosine (UAU), thus equilibrating the genome-wide translation of synonymous Q codons. Furthermore, Q prevents translation errors by suppressing second-position misreading of the glycine codon GGC, but not of wobble misreading. The absence of Q causes reduced translation of mRNAs involved in mitochondrial functions, and accordingly, lack of Q modification causes a mitochondrial defect in S. pombe. We also show that Q-dependent stimulation of Dnmt2 is conserved in mice. Our findings reveal a direct mechanism for the regulation of translational speed and fidelity in eukaryotes by a nutrient originating from bacteria.","doi":"10.1093/nar/gkz063","authors":"Müller M, Legrand C, Tuorto F, Kelly VP, Atlasi Y, Lyko F, Ehrenhofer-Murray AE","authors_abbrev":"Müller M et al.","pubmed_publication_date":"23 Apr 2019","pubmed_entrez_date":"2019-02-05","publication_year":"2019","canto_session_key":"14e1a7106407e8d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ann Ehrenhofer-Murray","canto_first_approved_date":"2022-08-17 16:39:29","canto_approved_date":"2024-04-12 15:42:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-08-17 09:52:39","canto_added_date":"2019-02-06 01:15:06","annotation_curators":[{"name":"Ann Ehrenhofer-Murray","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMIT.11","SPAC2F3.13c","SPBC29A10.13","SPMIT.01","SPAC24C9.16c","SPBC19C2.02","SPMIT.05","SPBC16C6.08c"],"gene_count":8,"ltp_gene_count":2,"approved_date":"2022-08-17"},{"uniquename":"PMID:26613610","title":"Dominance from the perspective of gene-gene and gene-chemical interactions.","citation":"Genetica 2016 Feb;144(1):23-36","abstract":"In this study, we used genetic interaction (GI) and gene-chemical interaction (GCI) data to compare mutations with different dominance phenotypes. Our analysis focused primarily on Saccharomyces cerevisiae, where haploinsufficient genes (HI; genes with dominant loss-of-function mutations) were found to be participating in gene expression processes, namely, the translation and regulation of gene transcription. Non-ribosomal HI genes (mainly regulators of gene transcription) were found to have more GIs and GCIs than haplosufficient (HS) genes. Several properties seem to lead to the enrichment of interactions, most notably, the following: importance, pleiotropy, gene expression level and gene expression variation. Importantly, after these properties were appropriately considered in the analysis, the correlation between dominance and GI/GCI degrees was still observed. Strikingly, for the GCIs of heterozygous strains, haploinsufficiency was the only property significantly correlated with the number of GCIs. We found ribosomal HI genes to be depleted in GIs/GCIs. This finding can be explained by their high variation in gene expression under different genetic backgrounds and environmental conditions. We observed the same distributions of GIs among non-ribosomal HI, ribosomal HI and HS genes in three other species: Schizosaccharomyces pombe, Drosophila melanogaster and Homo sapiens. One potentially interesting exception was the lack of significant differences in the degree of GIs between non-ribosomal HI and HS genes in Schizosaccharomyces pombe.","doi":"10.1007/s10709-015-9875-9","authors":"Gladki A, Zielenkiewicz P, Kaczanowski S","authors_abbrev":"Gladki A et al.","pubmed_publication_date":"Feb 2016","pubmed_entrez_date":"2015-11-29","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2015-11-30 01:19:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19460865","title":"Characterization of the Schizosaccharomyces pombe Spt5-Spt4 complex.","citation":"RNA 2009 Jul;15(7):1241-50","abstract":"The Spt5-Spt4 complex regulates early transcription elongation by RNA polymerase II and has an imputed role in pre-mRNA processing via its physical association with mRNA capping enzymes. Here we characterize the Schizosaccharomyces pombe core Spt5-Spt4 complex as a heterodimer and map a trypsin-resistant Spt4-binding domain within the Spt5 subunit. A genetic analysis of Spt4 in S. pombe revealed it to be inessential for growth at 25 degrees C-30 degrees C but critical at 37 degrees C. These results echo the conditional spt4Delta growth phenotype in budding yeast, where we find that Saccharomyces cerevisiae and S. pombe Spt4 are functionally interchangeable. Complementation of S. cerevisiae spt4Delta and a two-hybrid assay for Spt4-Spt5 interaction provided a readout of the effects of 33 missense and truncation mutations on S. pombe Spt4 function in vivo, which were interpreted in light of the recent crystal structure of S. cerevisiae Spt4 fused to a fragment of Spt5. Our results highlight the importance of the Spt4 Zn2+-binding residues--Cys12, Cys15, Cys29, and Asp32--and of Ser57, a conserved constituent of the Spt4-Spt5 interface. The 990-amino acid S. pombe Spt5 protein has an exceptionally regular carboxyl-terminal domain (CTD) composed of 18 nonapeptide repeats. We find that as few as three nonamer repeats sufficed for S. pombe growth, but only when Spt4 was present. Synthetic lethality of the spt5(1-835) spt4Delta double mutant at 34 degrees C suggests that interaction of Spt4 with the central domain of Spt5 overlaps functionally with the Spt5 CTD.","doi":"10.1261/rna.1572709","authors":"Schwer B, Schneider S, Pei Y, Aronova A, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-05-23","publication_year":"2009","canto_session_key":"19675180d80ed5f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-12-05 17:36:48","canto_approved_date":"2022-05-19 15:38:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-26 16:14:31","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21C3.16c","SPAC23C4.19"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-12-05"},{"uniquename":"PMID:21317872","title":"Red1 promotes the elimination of meiosis-specific mRNAs in vegetatively growing fission yeast.","citation":"EMBO J 2011 Mar 16;30(6):1027-39","abstract":"Meiosis-specific mRNAs are transcribed in vegetative fission yeast, and these meiotic mRNAs are selectively removed from mitotic cells to suppress meiosis. This RNA elimination system requires degradation signal sequences called determinant of selective removal (DSR), an RNA-binding protein Mmi1, polyadenylation factors, and the nuclear exosome. However, the detailed mechanism by which meiotic mRNAs are selectively degraded in mitosis but not meiosis is not understood fully. Here we report that Red1, a novel protein, is essential for elimination of meiotic mRNAs from mitotic cells. A red1 deletion results in the accumulation of a large number of meiotic mRNAs in mitotic cells. Red1 interacts with Mmi1, Pla1, the canonical poly(A) polymerase, and Rrp6, a subunit of the nuclear exosome, and promotes the destabilization of DSR-containing mRNAs. Moreover, Red1 forms nuclear bodies in mitotic cells, and these foci are disassembled during meiosis. These results demonstrate that Red1 is involved in DSR-directed RNA decay to prevent ectopic expression of meiotic mRNAs in vegetative cells.","doi":"10.1038/emboj.2011.32","authors":"Sugiyama T, Sugioka-Sugiyama R","authors_abbrev":"Sugiyama T et al.","pubmed_publication_date":"16 Mar 2011","pubmed_entrez_date":"2011-02-15","publication_year":"2011","canto_session_key":"f17c3d43d258f9f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tomo Sugiyama","canto_first_approved_date":"2017-06-30 11:03:31","canto_approved_date":"2025-02-11 16:12:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-21 15:48:11","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":42,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Tomo Sugiyama","community_curator":true,"annotation_count":12,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC70.09c","SPBC16E9.12c","SPAC1565.04c","SPBC216.02","SPBC2G2.09c","SPBPB2B2.19c","SPBCPT2R1.01c","SPAC750.07c","SPAC4G9.04c","SPAC5D6.05","SPCC736.12c","SPBC1271.06c","SPAC212.08c","SPNCRNA.103","SPBC32H8.11","SPBC29A10.02","SPAC1006.03c","SPBC359.02","SPAC57A10.04","SPAC27D7.13c","SPCC1223.12c","SPBPB10D8.03","SPBC29A10.14","SPAC1F3.01","SPAC27D7.03c","SPBC2D10.06","SPBC646.04"],"gene_count":27,"ltp_gene_count":12,"approved_date":"2017-06-30"},{"uniquename":"PMID:32513655","title":"Pdc2/Pat1 increases the range of decay factors and RNA bound by the Lsm1-7 complex.","citation":"RNA 2020 Oct;26(10):1380-1388","abstract":"Pat1, known as Pdc2 in fission yeast, promotes the activation and assembly of multiple proteins during mRNA decay. After deadenylation, the Pat1/Lsm1-7 complex binds to transcripts containing oligo(A) tails, which can be modified by the addition of several terminal uridine residues. Pat1 enhances Lsm1-7 binding to the 3' end, but it is unknown how this interaction is influenced by nucleotide composition. Here we examine Pat1/Lsm1-7 binding to a series of oligoribonucleotides containing different A/U contents using recombinant purified proteins from fission yeast. We observe a positive correlation between fractional uridine content and Lsm1-7 binding affinity. Addition of Pat1 broadens RNA specificity of Lsm1-7 by enhancing binding to A-rich RNAs and increases cooperativity on all oligonucleotides tested. Consistent with increased cooperativity, Pat1 promotes multimerization of the Lsm1-7 complex, which is potentiated by RNA binding. Furthermore, the inherent ability of Pat1 to multimerize drives liquid-liquid phase separation with multivalent decapping enzyme complexes of Dcp1/Dcp2. Our results uncover how Pat1 regulates RNA binding and higher order assembly by mRNA decay factors.","doi":"10.1261/rna.075812.120","authors":"Lobel JH, Gross JD","authors_abbrev":"Lobel JH et al.","pubmed_publication_date":"Oct 2020","pubmed_entrez_date":"2020-06-10","publication_year":"2020","canto_session_key":"ec0e3adeb7cd52d9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-06-11 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19G7.10c","SPAC19A8.12","SPBC3D6.08c","SPBC19C2.05"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:10645483","title":"[Characteristics of the cDNA of the Schizosaccharomyces pombe rpa43+ gene: structural similarity of the Rpa43 subunit of RNA-polymerase I with the Rpc25 subunit of RNA-polymerase III].","citation":"Bioorg Khim 1999 Oct;25(10):791-6","abstract":"We isolated and characterized full-length cDNA of the rpa43+ gene encoding one of subunits of the nuclear RNA polymerase I of Schizosaccharomyces pombe. The gene contains two introns and is located on chromosome II. Comparison of the primary structure of the subunit Rpa43 of Sz. pombe (173 aa; M 19,385 Da; pl 5.36), deduced from the cDNA obtained, with the amino acid sequences of subunits A43 from Saccharomyces cerevisiae and Drosophila melanogaster demonstrates a high divergence of this protein in evolution. A comparison of the Rpa43 with other proteins from the SwissProt database revealed a similarity of this subunit to subunit Rpc25 of RNA polymerase III, which, as was shown previously, is structurally similar to subunit Rpb7 of RNA polymerase II. Thus, including the Rpa43<-->Rpc25<-->Rpb7 family, nuclear RNA polymerases I-III contain at least 11 identical and/or similar subunits. This fact illustrates a pronounced resemblance of the organization of all three enzymes of the eukaryotic transcription apparatus. Moreover, at least ten out of these eleven families of eukaryotic RNA polymerase subunits have homologues in the 13-subunit archaeal RNA polymerase.","authors":"Shpakovskiĭ GV, Shematorova EK","authors_abbrev":"Shpakovskiĭ GV et al.","pubmed_publication_date":"Oct 1999","pubmed_entrez_date":"2000-01-25","publication_year":"1999","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38663097","title":"Bqt4 affects relative movement between SPB and nucleolus in fission yeast.","citation":"Biochem Biophys Res Commun 2024 Apr 23;714:149970","abstract":"Movement dynamics in the nucleus involve various biological processes, including DNA repair, which is crucial for cancer prevention. Changes in the movement of the components of the nucleus indicate the changes in movement dynamics in the nucleus. In Schizosaccharomyces pombe, the inner nuclear membrane protein Bqt4 plays an essential role in attaching telomeres to the nuclear envelope. We observed that the deletion of bqt4 +  caused a significant decrease in the mean square displacement (MSD) calculated from the distance between the nucleolar center and spindle pole body (SPB), hereafter referred to as MSD (SPB-Nucleolus) . The MSD (SPB-Nucleolus)  decrease in bqt4Δ was microtubule-dependent. The Rap1-binding ability loss mutant, bqt4 F46A , and nonspecific DNA-binding ability mutants, bqt4 3E-A , did not exhibit an MSD (SPB-Nucleolus)  decrease compared to the WT. Moreover, the bqt4 3E-A rap1Δ double mutant and 1-262 amino acids truncated mutant bqt4ΔN (263-432), which does not have either Rap1-binding or nonspecific DNA-binding abilities, did not exhibit the MSD(SPB-Nucleolus) decrease to the same extent as bqt4Δ. These results suggest that the unknown function of Bqt4 in the C-terminal domain is essential for the maintenance of the pattern of relative movement between SPB and the nucleolus.","doi":"10.1016/j.bbrc.2024.149970","authors":"Wang K, Ito H, Kanoh J, Ueno M","authors_abbrev":"Wang K et al.","pubmed_publication_date":"23 Apr 2024","pubmed_entrez_date":"2024-04-25","publication_year":"2024","canto_session_key":"2a1f9a9d870187d5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-04-26 23:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19C7.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9821289","title":"Inactivation of the plasma membrane ATPase of Schizosaccharomyces pombe by hydrogen peroxide and by the Fenton reagent (Fe2+/H2O2): nonradical vs. radical-induced oxidation.","citation":"Folia Microbiol (Praha) 1998;43(4):361-7","abstract":"In the absence of added Fe2+, the ATPase activity of isolated Schizosaccharomyces pombe plasma membranes (5-7 mumol P(i) per mg protein per min) is moderately inhibited by H2O2 in a concentration-dependent manner. Sizable inactivation occurs only at 50-80 mmol/L H2O2. The process, probably a direct oxidative action of H2O2 on the enzyme, is not induced by the indigenous membrane-bound iron (19.3 nmol/mg membrane protein), is not affected by the radical scavengers mannitol and Tris, and involves a decrease of both the K(m) of the enzyme for ATP and the V of ATP splitting. On exposing the membranes to the Fenton reagent (50 mumol/L Fe2+ + 20 mmol/L H2O2), which causes a fast production of HO. radicals, the ATPase is 50-60% inactivated and 90% of added Fe2+ is oxidized to Fe3+ within 1 min. The inactivation occurs only when Fe2+ is added before H2O2 and can thus bind to the membranes. The lack of effect of radical scavengers (mannitol, Tris) indicates that HO. radicals produced in the bulk phase play no role in inactivation. Blockage of the inactivation by the iron chelator deferrioxamine implies that the process requires the presence of Fe2+ ions bound to binding sites on the enzyme molecules. Added catalase, which competes with Fe2+ for H2O2, slows down the inactivation but in some cases increases its total extent, probably due to the formation of the superoxide radical that gives rise to delayed HO. production.","authors":"Sigler K, Gille G, Vacata V, Stadler N, Höfer M","authors_abbrev":"Sigler K et al.","pubmed_publication_date":"1998","pubmed_entrez_date":"1998-11-20","publication_year":"1998","canto_session_key":"2aea6e031e3c6302","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-11-24 12:52:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-24 12:52:12","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-11-24"},{"uniquename":"PMID:26258632","title":"Mad1 promotes chromosome congression by anchoring a kinesin motor to the kinetochore.","citation":"Nat Cell Biol 2015 Sep;17(9):1124-33","abstract":"For proper partitioning of genomes in mitosis, all chromosomes must be aligned at the spindle equator before the onset of anaphase. The spindle assembly checkpoint (SAC) monitors this process, generating a 'wait anaphase' signal at unattached kinetochores of misaligned chromosomes. However, the link between SAC activation and chromosome alignment is poorly understood. Here we show that Mad1, a core SAC component, plays a hitherto concealed role in chromosome alignment. Protein-protein interaction screening revealed that fission yeast Mad1 binds the plus-end-directed kinesin-5 motor protein Cut7 (Eg5 homologue), which is generally thought to promote spindle bipolarity. We demonstrate that Mad1 recruits Cut7 to kinetochores of misaligned chromosomes and promotes chromosome gliding towards the spindle equator. Similarly, human Mad1 recruits another kinetochore motor CENP-E, revealing that Mad1 is the conserved dual-function protein acting in SAC activation and chromosome gliding. Our results suggest that the mitotic checkpoint has co-evolved with a mechanism to drive chromosome congression.","doi":"10.1038/ncb3219","authors":"Akera T, Goto Y, Sato M, Yamamoto M, Watanabe Y","authors_abbrev":"Akera T et al.","pubmed_publication_date":"Sep 2015","pubmed_entrez_date":"2015-08-11","publication_year":"2015","canto_session_key":"558b22ef42aa6ec2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2016-10-02 21:11:29","canto_approved_date":"2024-03-27 14:46:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-19 21:33:06","canto_added_date":"2015-08-12 00:19:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":30,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.04c","SPAC25G10.07c","SPAC23H3.08c","SPCC1795.01c","SPCC1322.12c","SPBC106.01","SPBC20F10.06"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-10-02"},{"uniquename":"PMID:31477575","title":"Modulation of TOR complex 2 signaling by the stress-activated MAPK pathway in fission yeast.","citation":"J Cell Sci 2019 Oct 10;132(19)","abstract":"Sin1 is a substrate-binding subunit of target of rapamycin complex 2 (TORC2), an evolutionarily conserved protein kinase complex. In fission yeast, Sin1 has also been identified as a protein that interacts with Spc1 (also known as Sty1) in the stress-activated protein kinase (SAPK) pathway. Therefore, this study examined the relationship between TORC2 and Spc1 signaling. We found that the common docking (CD) domain of Spc1 interacts with a cluster of basic amino acid residues in Sin1. Although diminished TORC2 activity in the absence of the functional Spc1 cascade suggests positive regulation of TORC2 by Spc1, such regulation appears to be independent of the Sin1-Spc1 interaction. Hyperosmotic stress transiently inhibits TORC2, and its swift recovery is dependent on Spc1, the transcription factor Atf1, and the glycelrol-3-phosphate dehydrogenase Gpd1, whose expression is induced upon osmostress by the Spc1-Atf1 pathway. Thus, cellular adaptation to osmostress seems important for TORC2 reactivation, though Spc1 and Atf1 contribute to TORC2 activation also in the absence of osmostress. These results indicate coordinated actions of the SAPK and TORC2 pathways, both of which are essential for fission yeast cells to survive environmental stress.","doi":"10.1242/jcs.236133","authors":"Morigasaki S, Chin LC, Hatano T, Emori M, Iwamoto M, Tatebe H, Shiozaki K","authors_abbrev":"Morigasaki S et al.","pubmed_publication_date":"10 Oct 2019","pubmed_entrez_date":"2019-09-04","publication_year":"2019","canto_session_key":"c6d1b50aea743116","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaz Shiozaki","canto_first_approved_date":"2019-11-01 17:29:54","canto_approved_date":"2022-09-21 14:57:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-11 08:13:22","canto_added_date":"2019-09-05 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":24,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Kaz Shiozaki","community_curator":true,"annotation_count":28,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.02c","SPAC23D3.04c","SPAPYUG7.02c","SPBC409.07c","SPBC215.05","SPCC24B10.07","SPAC24B11.06c","SPBC29B5.01","SPBC21B10.05c","SPBC119.08","SPAC637.13c","SPBC30D10.10c","SPCC777.08c"],"gene_count":13,"ltp_gene_count":8,"approved_date":"2019-11-01"},{"uniquename":"PMID:20097624","title":"Unwinding the functions of the Pif1 family helicases.","citation":"DNA Repair (Amst) 2010 Mar 02;9(3):237-49","abstract":"Helicases are ubiquitous enzymes found in all organisms that are necessary for all (or virtually all) aspects of nucleic acid metabolism. The Pif1 helicase family is a group of 5'-->3' directed, ATP-dependent, super family IB helicases found in nearly all eukaryotes. Here, we review the discovery, evolution, and what is currently known about these enzymes in Saccharomyces cerevisiae (ScPif1 and ScRrm3), Schizosaccharomyces pombe (SpPfh1), Trypanosoma brucei (TbPIF1, 2, 5, and 8), mice (mPif1), and humans (hPif1). Pif1 helicases variously affect telomeric, ribosomal, and mitochondrial DNA replication, as well as Okazaki fragment maturation, and in at least some cases affect these processes by using their helicase activity to disrupt stable nucleoprotein complexes. While the functions of these enzymes vary within and between organisms, it is evident that Pif1 family helicases are crucial for both nuclear and mitochondrial genome maintenance.","doi":"10.1016/j.dnarep.2010.01.008","authors":"Bochman ML, Sabouri N, Zakian VA","authors_abbrev":"Bochman ML et al.","pubmed_publication_date":"02 Mar 2010","pubmed_entrez_date":"2010-01-26","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4644410","title":"Experimental inhibition of cell wall formation and of reversion in Nadsonia elongata and Schizosaccharomyces pombe protoplasts.","citation":"Protoplasma 1972;75(4):405-19","abstract":"","authors":"Havelková M","authors_abbrev":"Havelková M","pubmed_publication_date":"1972","pubmed_entrez_date":"1972-01-01","publication_year":"1972","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3743551","title":"Two RNA species co-purify with RNase P from the fission yeast Schizosaccharomyces pombe.","citation":"EMBO J 1986 Jul;5(7):1697-703","abstract":"RNase P activity from Schizosaccharomyces pombe co-purifies with two RNA species. These RNAs are associated with enzyme activity as judged by titrated micrococcal nuclease inactivation experiments. The two RNAs, K1- and K2-RNA, are 285 and 270 nucleotides long, respectively. Both RNAs are transcribed from one gene, present in a single copy in the haploid genome. The primary and a secondary structure of K RNAs have been determined and compared with M1 RNA, their counterpart from Escherichia coli. Very limited sequence homology was observed, and this agrees with the finding that no cross-hybridization with M1 RNA can be detected in a Southern analysis with yeast genomic DNA. However, the secondary structures of K RNA and M1 RNA show the same basic organization and one conserved local motif, the sequence GUG--AGGPu in an exposed hairpin loop.","authors":"Krupp G, Cherayil B, Frendewey D, Nishikawa S, Söll D","authors_abbrev":"Krupp G et al.","pubmed_publication_date":"Jul 1986","pubmed_entrez_date":"1986-07-01","publication_year":"1986","canto_session_key":"94d2a0c92c10b65b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-08 09:52:19","canto_approved_date":"2022-06-05 16:39:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-16 16:45:47","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.128"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-08"},{"uniquename":"PMID:32839613","title":"Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state.","citation":"Nat Struct Mol Biol 2020 Nov;27(11):1009-1016","abstract":"Arp2/3 complex, a crucial actin filament nucleator, undergoes structural rearrangements during activation by nucleation-promoting factors (NPFs). However, the conformational pathway leading to the nucleation-competent state is unclear due to lack of high-resolution structures of the activated state. Here we report a ~3.9 Å resolution cryo-EM structure of activated Schizosaccharomyces pombe Arp2/3 complex bound to the S. pombe NPF Dip1 and attached to the end of the nucleated actin filament. The structure reveals global and local conformational changes that allow the two actin-related proteins in Arp2/3 complex to mimic a filamentous actin dimer and template nucleation. Activation occurs through a clamp-twisting mechanism, in which Dip1 forces two core subunits in Arp2/3 complex to pivot around one another, shifting half of the complex into a new activated position. By showing how Dip1 stimulates activation, the structure reveals how NPFs can activate Arp2/3 complex in diverse cellular processes.","doi":"10.1038/s41594-020-0481-x","authors":"Shaaban M, Chowdhury S, Nolen BJ","authors_abbrev":"Shaaban M et al.","pubmed_publication_date":"Nov 2020","pubmed_entrez_date":"2020-08-26","publication_year":"2020","canto_session_key":"afd6b31bd08a71c2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-08-27 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.03","SPBC1778.08c","SPAC17G8.04c","SPAC6F6.10c","SPAC11H11.06","SPBC14C8.06","SPBC24C6.10c","SPAC6G9.07c"],"gene_count":8,"ltp_gene_count":8,"pdb_entries":[{"pdb_id":"6w17","gene_chains":[{"gene_uniquename":"SPAC6F6.10c","chain":"D","position":"1-317"},{"gene_uniquename":"SPBC24C6.10c","chain":"H","position":"1-374"},{"gene_uniquename":"SPAC630.03","chain":"A","position":"1-427"},{"gene_uniquename":"SPBC14C8.06","chain":"C","position":"1-377"},{"gene_uniquename":"SPAC17G8.04c","chain":"G","position":"1-152"},{"gene_uniquename":"SPAC6G9.07c","chain":"F","position":"1-168"},{"gene_uniquename":"SPAC11H11.06","chain":"B","position":"1-390"},{"gene_uniquename":"SPBC1778.08c","chain":"E","position":"1-174"}],"title":"Structure of Dip1-activated Arp2/3 complex with nucleated actin filament","entry_authors":"Shaaban M,Nolen BJ,Chowdhury S","entry_authors_abbrev":"Shaaban M et al.","reference_uniquename":"PMID:32839613","experimental_method":"EM","resolution":"3.9"},{"pdb_id":"6w18","gene_chains":[{"gene_uniquename":"SPAC6F6.10c","chain":"D","position":"1-317"},{"gene_uniquename":"SPAC630.03","chain":"A","position":"1-427"},{"gene_uniquename":"SPBC14C8.06","chain":"C","position":"1-377"},{"gene_uniquename":"SPAC17G8.04c","chain":"G","position":"1-152"},{"gene_uniquename":"SPAC6G9.07c","chain":"F","position":"1-168"},{"gene_uniquename":"SPAC11H11.06","chain":"B","position":"1-390"},{"gene_uniquename":"SPBC1778.08c","chain":"E","position":"1-174"}],"title":"Structure of S. pombe Arp2/3 complex in inactive state","entry_authors":"Shaaban M,Nolen BJ,Chowdhury S","entry_authors_abbrev":"Shaaban M et al.","reference_uniquename":"PMID:32839613","experimental_method":"EM","resolution":"4.2"}]},{"uniquename":"PMID:8536990","title":"The rec8 gene of Schizosaccharomyces pombe is involved in linear element formation, chromosome pairing and sister-chromatid cohesion during meiosis.","citation":"Genetics 1995 Sep;141(1):61-73","abstract":"The fission yeast Schizosaccharomyces pombe does not form tripartite synaptonemal complexes during meiotic prophase, but axial core-like structures (linear elements). To probe the relationship between meiotic recombination and the structure, pairing, and segregation of meiotic chromosomes, we genetically and cytologically characterized the rec8-110 mutant, which is partially deficient in meiotic recombination. The pattern of spore viability indicates that chromosome segregation is affected in the mutant. A detailed segregational analysis in the rec8-110 mutant revealed more spores disomic for chromosome III than in a wild-type strain. Aberrant segregations are caused by precocious segregation of sister chromatids at meiosis I, rather than by nondisjunction as a consequence of lack of crossovers. In situ hybridization further showed that the sister chromatids are separated prematurely during meiotic prophase. Moreover, the mutant forms aberrant linear elements and shows a shortened meiotic prophase. Meiotic chromosome pairing in interstitial and centromeric regions is strongly impaired in rec8-110, whereas the chromosome ends are less deficient in pairing. We propose that the rec8 gene encodes a protein required for linear element formation and that the different phenotypes of rec8-110 reflect direct and indirect consequences of the absence of regular linear elements.","authors":"Molnar M, Bähler J, Sipiczki M, Kohli J","authors_abbrev":"Molnar M et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_session_key":"2e628911863cd67c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-30 13:06:33","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-30 13:06:17","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A10.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-30"},{"uniquename":"PMID:27582274","title":"Polyadenylation site selection: linking transcription and RNA processing via a conserved carboxy-terminal domain (CTD)-interacting protein.","citation":"Curr Genet 2017 May;63(2):195-199","abstract":"Despite the fact that the process of mRNA polyadenylation has been known for more than 40 years, a detailed understating of the mechanism underlying polyadenylation site selection is still far from complete. As 3' end processing is intimately associated with RNA polymerase II (RNAPII) transcription, factors that can successively interact with the transcription machinery and recognize cis-acting sequences on the nascent pre-mRNA would be well suited to contribute to poly(A) site selection. Studies using the fission yeast Schizosaccharomyces pombe have recently identified Seb1, a protein that shares homology with Saccharomyces cerevisiae Nrd1 and human SCAF4/8, and that is critical for poly(A) site selection. Seb1 binds to the C-terminal domain (CTD) of RNAPII via a conserved CTD-interaction domain and recognizes specific sequence motifs clustered downstream of the polyadenylation site on the uncleaved pre-mRNA. In this short review, we summarize insights into Seb1-dependent poly(A) site selection and discuss some unanswered questions regarding its molecular mechanism and conservation.","doi":"10.1007/s00294-016-0645-8","authors":"Larochelle M, Hunyadkürti J, Bachand F","authors_abbrev":"Larochelle M et al.","pubmed_publication_date":"May 2017","pubmed_entrez_date":"2016-09-02","publication_year":"2017","canto_session_key":"216b45645076768d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Marc Larochelle","canto_first_approved_date":"2018-03-21 13:55:10","canto_approved_date":"2024-04-03 16:36:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-03-19 19:45:28","canto_added_date":"2016-09-03 00:15:11","annotation_curators":[{"name":"Marc Larochelle","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC222.09","SPAC4G9.04c","SPBC19C2.07","SPCC576.08c","SPAC2F7.11"],"gene_count":5,"ltp_gene_count":2,"approved_date":"2018-03-21"},{"uniquename":"PMID:8631306","title":"A single fission yeast mitotic cyclin B p34cdc2 kinase promotes both S-phase and mitosis in the absence of G1 cyclins.","citation":"EMBO J 1996 Feb 15;15(4):850-60","abstract":"Deletion of the fission yeast mitotic B-type cyclin gene cdc13 causes cells to undergo successive rounds of DNA replication. We have used a strain which expresses cdc13 conditionally to investigate re-replication. Activity of Start genes cdc2 and cdc10 is necessary and p34cdc2 kinase is active in re-replicating cells. We tested to see whether other cyclins were required for re-replication using cdc13delta. Further deletion of cig1 and puc1 had no effect, but deletion of cig2/cyc17 caused a severe delay in re-replication. Deletion of cig1 and cig2/cyc17 together abolished re-replication completely and cells arrested in G1. This, and analysis of the temperature sensitive cdc13-117 mutant, suggests that cdc13 can effectively substitute for the G1 cyclin activity of cig2/cyc17. We have characterized p56cdc13 activity and find evidence that in the absence of G1 cyclins, S-phase is delayed until the mitotic p34cdc2-p56cdc13 kinase is sufficiently active. These data suggest that a single oscillation of p34cdc2 kinase activity provided by a single B-type cyclin can promote ordered progression into both DNA replication and mitosis, and that the level of cyclin-dependent kinase activity may act as a master regulator dictating whether cells undergo S-phase or mitosis.","authors":"Fisher DL, Nurse P","authors_abbrev":"Fisher DL et al.","pubmed_publication_date":"15 Feb 1996","pubmed_entrez_date":"1996-02-15","publication_year":"1996","canto_session_key":"a78d5a33655067b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-05-03 20:36:36","canto_approved_date":"2024-08-13 15:59:57","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-06-11 21:29:50","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC11B10.09","SPCC4E9.02","SPAPB2B4.03","SPBC336.12c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2016-05-03"},{"uniquename":"PMID:31575705","title":"Chromatin remodeler Fft3 plays a dual role at blocked DNA replication forks.","citation":"Life Sci Alliance 2019 Oct;2(5)","abstract":"Here, we investigate the function of fission yeast Fun30/Smarcad1 family of SNF2 ATPase-dependent chromatin remodeling enzymes in DNA damage repair. There are three Fun30 homologues in fission yeast, Fft1, Fft2, and Fft3. We find that only Fft3 has a function in DNA repair and it is needed for single-strand annealing of an induced double-strand break. Furthermore, we use an inducible replication fork barrier system to show that Fft3 has two distinct roles at blocked DNA replication forks. First, Fft3 is needed for the resection of nascent strands, and second, it is required to restart the blocked forks. The latter function is independent of its ATPase activity.","doi":"10.26508/lsa.201900433","authors":"Ait-Saada A, Khorosjutina O, Chen J, Kramarz K, Maksimov V, Svensson JP, Lambert S, Ekwall K","authors_abbrev":"Ait-Saada A et al.","pubmed_publication_date":"Oct 2019","pubmed_entrez_date":"2019-10-03","publication_year":"2019","canto_session_key":"6d4a9d65ed297cda","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Karl Ekwall","canto_first_approved_date":"2020-03-03 13:22:29","canto_approved_date":"2024-03-04 11:11:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-02-20 09:47:52","canto_added_date":"2019-10-04 00:15:03","annotation_curators":[{"name":"Karl Ekwall","community_curator":true,"annotation_count":6,"orcid":"0000-0002-3029-4041","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25A8.01c","SPCC1235.05c","SPAC20G8.08c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2020-03-03"},{"uniquename":"PMID:28623092","title":"CtIP/Ctp1/Sae2, molecular form fit for function.","citation":"DNA Repair (Amst) 2017 Aug;56:109-117","abstract":"Vertebrate CtIP, and its fission yeast (Ctp1), budding yeast (Sae2) and plant (Com1) orthologs have emerged as key regulatory molecules in cellular responses to DNA double strand breaks (DSBs). By modulating the nucleolytic 5'-3' resection activity of the Mre11/Rad50/Nbs1 (MRN) DSB repair processing and signaling complex, CtIP/Ctp1/Sae2/Com1 is integral to the channeling of DNA double strand breaks through DSB repair by homologous recombination (HR). Nearly two decades since its discovery, emerging new data are defining the molecular underpinnings for CtIP DSB repair regulatory activities. CtIP homologs are largely intrinsically unstructured proteins comprised of expanded regions of low complexity sequence, rather than defined folded domains typical of DNA damage metabolizing enzymes and nucleases. A compact structurally conserved N-terminus forms a functionally critical tetrameric helical dimer of dimers (THDD) region that bridges CtIP oligomers, and is flexibly appended to a conserved C-terminal Sae2-homology DNA binding and DSB repair pathway choice regulatory hub which influences nucleolytic activities of the MRN core nuclease complex. The emerging evidence from structural, biophysical, and biological studies converges on CtIP having functional roles in DSB repair that include: 1) dynamic DNA strand coordination through direct DNA binding and DNA bridging activities, 2) MRN nuclease complex cofactor functions that direct MRN endonucleolytic cleavage of protein-blocked DSB ends and 3) acting as a protein binding hub targeted by the cell cycle regulatory apparatus, which influences CtIP expression and activity via layers of post-translational modifications, protein-protein interactions and DNA binding.","doi":"10.1016/j.dnarep.2017.06.013","authors":"Andres SN, Williams RS","authors_abbrev":"Andres SN et al.","pubmed_publication_date":"Aug 2017","pubmed_entrez_date":"2017-06-18","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-06-19 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26945040","title":"Local potentiation of stress-responsive genes by upstream noncoding transcription.","citation":"Nucleic Acids Res 2016 Jun 20;44(11):5174-89","abstract":"It has been postulated that a myriad of long noncoding RNAs (lncRNAs) contribute to gene regulation. In fission yeast, glucose starvation triggers lncRNA transcription across promoter regions of stress-responsive genes including fbp1 (fructose-1,6-bisphosphatase1). At the fbp1 promoter, this transcription promotes chromatin remodeling and fbp1 mRNA expression. Here, we demonstrate that such upstream noncoding transcription facilitates promoter association of the stress-responsive transcriptional activator Atf1 at the sites of transcription, leading to activation of the downstream stress genes. Genome-wide analyses revealed that ∼50 Atf1-binding sites show marked decrease in Atf1 occupancy when cells are treated with a transcription inhibitor. Most of these transcription-enhanced Atf1-binding sites are associated with stress-dependent induction of the adjacent mRNAs or lncRNAs, as observed in fbp1 These Atf1-binding sites exhibit low Atf1 occupancy and high histone density in glucose-rich conditions, and undergo dramatic changes in chromatin status after glucose depletion: enhanced Atf1 binding, histone eviction, and histone H3 acetylation. We also found that upstream transcripts bind to the Groucho-Tup1 type transcriptional corepressors Tup11 and Tup12, and locally antagonize their repressive functions on Atf1 binding. These results reveal a new mechanism in which upstream noncoding transcription locally magnifies the specific activation of stress-inducible genes via counteraction of corepressors.","doi":"10.1093/nar/gkw142","authors":"Takemata N, Oda A, Yamada T, Galipon J, Miyoshi T, Suzuki Y, Sugano S, Hoffman CS, Hirota K, Ohta K","authors_abbrev":"Takemata N et al.","pubmed_publication_date":"20 Jun 2016","pubmed_entrez_date":"2016-03-06","publication_year":"2016","canto_session_key":"c6d5c6f113d49ea5","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-03-07 01:15:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28467824","title":"Core Mediator structure at 3.4 Å extends model of transcription initiation complex.","citation":"Nature 2017 May 11;545(7653):248-251","abstract":"Mediator is a multiprotein co-activator that binds the transcription pre-initiation complex (PIC) and regulates RNA polymerase (Pol) II. The Mediator head and middle modules form the essential core Mediator (cMed), whereas the tail and kinase modules play regulatory roles. The architecture of Mediator and its position on the PIC are known, but atomic details are limited to Mediator subcomplexes. Here we report the crystal structure of the 15-subunit cMed from Schizosaccharomyces pombe at 3.4 Å resolution. The structure shows an unaltered head module, and reveals the intricate middle module, which we show is globally required for transcription. Sites of known Mediator mutations cluster at the interface between the head and middle modules, and in terminal regions of the head subunits Med6 (ref. 16) and Med17 (ref. 17) that tether the middle module. The structure led to a model for Saccharomyces cerevisiae cMed that could be combined with the 3.6 Å cryo-electron microscopy structure of the core PIC (cPIC). The resulting atomic model of the cPIC-cMed complex informs on interactions of the submodules forming the middle module, called beam, knob, plank, connector, and hook. The hook is flexibly linked to Mediator by a conserved hinge and contacts the transcription initiation factor IIH (TFIIH) kinase that phosphorylates the carboxy (C)-terminal domain (CTD) of Pol II and was recently positioned on the PIC. The hook also contains residues that crosslink to the CTD and reside in a previously described cradle. These results provide a framework for understanding Mediator function, including its role in stimulating CTD phosphorylation by TFIIH.","doi":"10.1038/nature22328","authors":"Nozawa K, Schneider TR, Cramer P","authors_abbrev":"Nozawa K et al.","pubmed_publication_date":"11 May 2017","pubmed_entrez_date":"2017-05-04","publication_year":"2017","canto_session_key":"3e0a5d273c70b058","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-18 17:00:02","canto_approved_date":"2023-07-05 15:52:57","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-02-18 16:59:54","canto_added_date":"2017-05-05 00:15:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":32,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.10c","SPBC1604.10","SPAC24C9.04","SPBC1105.06","SPAC1002.15c","SPBC14F5.08","SPAC17G8.05","SPAC29A4.07","SPCP31B10.03c","SPBC31F10.09c","SPAC644.10","SPCC1450.05c","SPBC31F10.04c","SPAC5D6.05","SPBC21.04"],"gene_count":15,"ltp_gene_count":15,"approved_date":"2023-02-18","pdb_entries":[{"pdb_id":"5n9j","gene_chains":[{"gene_uniquename":"SPAC24C9.04","chain":"F","position":"1-121"},{"gene_uniquename":"SPAC29A4.07","chain":"Z","position":"1-136"},{"gene_uniquename":"SPAC5D6.05","chain":"X","position":"1-207"},{"gene_uniquename":"SPBC14F5.08","chain":"E","position":"1-376"},{"gene_uniquename":"SPBC1604.10","chain":"D","position":"1-138"},{"gene_uniquename":"SPBC21.04","chain":"U","position":"1-200"},{"gene_uniquename":"SPBC31F10.04c","chain":"W","position":"1-545"},{"gene_uniquename":"SPBC31F10.09c","chain":"B","position":"1-144"},{"gene_uniquename":"SPAC17G8.05","chain":"Y","position":"1-193"},{"gene_uniquename":"SPAC644.10","chain":"V","position":"1-112"},{"gene_uniquename":"SPBC1A4.10c","chain":"A","position":"2-580"},{"gene_uniquename":"SPAC1002.15c","chain":"S","position":"1-216"},{"gene_uniquename":"SPCP31B10.03c","chain":"R","position":"1-139"},{"gene_uniquename":"SPCC1450.05c","chain":"C","position":"1-138"},{"gene_uniquename":"SPBC1105.06","chain":"G","position":"1-239"}],"title":"Core Mediator of transcriptional regulation","entry_authors":"Nozawa K,Schneider TR,Cramer P","entry_authors_abbrev":"Nozawa K et al.","reference_uniquename":"PMID:28467824","experimental_method":"X-ray","resolution":"3.4"}]},{"uniquename":"PMID:7851760","title":"The mutator gene swi8 effects specific mutations in the mating-type region of Schizosaccharomyces pombe.","citation":"Genetics 1994 Nov;138(3):621-32","abstract":"The swi8+ gene of Schizosaccharomyces pombe appears to be involved in the termination step of copy synthesis during mating-type (MT) switching. Mutations in swi8 confer a general mutator phenotype and, in particular, generate specific mutations in the MT region. Sequencing of the MT cassettes of the h90 swi8-137 mutant revealed three altered sites. One is situated at the switching (smt) signal adjacent to the H1 homology box of the expression locus mat1:1. It reduces the rate of MT switching. The alteration at the smt signal arose frequently in other h90 swi8 strains and is probably caused by gene conversion in which the sequence adjacent to the H1 box of mat2:2 is used as template. This change might be generated during the process of MT switching when hybrid DNA formation is anomalously extended into the more heterologous region flanking the H1 homology box. In addition to the gene conversion at mat1:1, two mutations were found in the H3 homology boxes of the silent cassettes mat2:2 and mat3:3.","authors":"Fleck O, Rudolph C, Albrecht A, Lorentz A, Schär P, Schmidt H","authors_abbrev":"Fleck O et al.","pubmed_publication_date":"Nov 1994","pubmed_entrez_date":"1994-11-01","publication_year":"1994","canto_session_key":"0deeb7d3d09fc191","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-27 10:55:29","canto_approved_date":"2022-12-12 17:25:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-27 10:55:22","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-02-27"},{"uniquename":"PMID:15797383","title":"SREBP pathway responds to sterols and functions as an oxygen sensor in fission yeast.","citation":"Cell 2005 Mar 25;120(6):831-42","abstract":"Cholesterol and fatty acid synthesis in mammals are controlled by SREBPs, a family of membrane bound transcription factors. Our studies identified homologs of SREBP, its binding partner SCAP, and the ER retention protein Insig in Schizosaccharomyces pombe, named sre1+, scp1+, and ins1+. Like SREBP, Sre1 is cleaved and activated in response to sterol depletion in a Scp1-dependent manner. Microarray analysis revealed that Sre1 activates sterol biosynthetic enzymes as in mammals, and, surprisingly, Sre1 also stimulates transcription of genes required for adaptation to hypoxia. Furthermore, Sre1 rapidly activates these target genes in response to low oxygen and is itself required for anaerobic growth. Based on these findings, we propose and test a model in which Sre1 and Scp1 monitor oxygen-dependent sterol synthesis as an indirect measure of oxygen supply and mediate a hypoxic response in fission yeast.","authors":"Hughes AL, Todd BL, Espenshade PJ","authors_abbrev":"Hughes AL et al.","pubmed_publication_date":"25 Mar 2005","pubmed_entrez_date":"2005-03-31","publication_year":"2005","canto_session_key":"889b897cf264bfe3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-01-07 11:29:57","canto_approved_date":"2021-12-21 15:01:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-01-07 11:29:50","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.09","SPBC354.05c","SPCC306.05c","SPAC19G12.08","SPAC1687.16c","SPAC30C2.02","SPAC926.09c","SPCC162.09c","SPAC4F8.14c","SPAC222.11","SPBC3B9.15c","SPAC17A2.05","SPAC630.08c","SPAC2F3.09"],"gene_count":14,"ltp_gene_count":4,"approved_date":"2020-01-07"},{"uniquename":"PMID:7883794","title":"Regulation of the cell cycle timing of Start in fission yeast by the rum1+ gene.","citation":"J Cell Sci Suppl 1994;18:63-8","abstract":"We have identified the rum1+ gene as a new regulator of the G1-phase of the fission yeast cell cycle. rum1+ determines the cell cycle timing of Start, by maintaining cells in a pre-Start state until they have attained a minimal critical mass. Cells lacking rum1+ are unable to arrest in pre-Start G1 in response to nitrogen starvation and are subsequently sterile. In addition, rum1+ prevents entry into mitosis from pre-Start G1, as shown by the fact that cdc10 mutants in the absence of rum1+ undergo lethal mitosis without entering S-phase.","authors":"Moreno S, Labib K, Correa J, Nurse P","authors_abbrev":"Moreno S et al.","pubmed_publication_date":"1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_session_key":"69269d206e6ff52a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2019-03-08 16:20:51","canto_approved_date":"2024-04-04 10:06:26","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-02-27 16:31:47","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":9,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPBC32F12.09","SPBC336.12c","SPAC24H6.05","SPBC11B10.09"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2019-03-08"},{"uniquename":"PMID:12897162","title":"Replication checkpoint kinase Cds1 regulates recombinational repair protein Rad60.","citation":"Mol Cell Biol 2003 Aug;23(16):5939-46","abstract":"Genome integrity is protected by Cds1 (Chk2), a checkpoint kinase that stabilizes arrested replication forks. How Cds1 accomplishes this task is unknown. We report that Cds1 interacts with Rad60, a protein required for recombinational repair in fission yeast. Cds1 activation triggers Rad60 phosphorylation and nuclear delocalization. A Rad60 mutant that inhibits regulation by Cds1 renders cells specifically sensitive to replication fork arrest. Genetic and biochemical studies indicate that Rad60 functions codependently with Smc5 and Smc6, subunits of an SMC (structural maintenance of chromosomes) complex required for recombinational repair. These studies indicate that regulation of Rad60 is an important part of the replication checkpoint response controlled by Cds1. We propose that control of Rad60 regulates recombination events at stalled forks.","authors":"Boddy MN, Shanahan P, McDonald WH, Lopez-Girona A, Noguchi E, Yates III JR, Russell P","authors_abbrev":"Boddy MN et al.","pubmed_publication_date":"Aug 2003","pubmed_entrez_date":"2003-08-05","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["YDR363W","SPBC1921.02","SPAC14C4.02c","SPCC18B5.11c","SPCC4G3.05c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"EMBL:SPCAP","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12011934","title":"Centromere domain organization and histone modifications.","citation":"Braz J Med Biol Res 2002 May;35(5):499-507","abstract":"Centromere function requires the proper coordination of several subfunctions, such as kinetochore assembly, sister chromatid cohesion, binding of kinetochore microtubules, orientation of sister kinetochores to opposite spindle poles, and their movement towards the spindle poles. Centromere structure appears to be organized in different, separable domains in order to accomplish these functions. Despite the conserved nature of centromere functions, the molecular genetic definition of the DNA sequences that form a centromere in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe, in the fruit fly Drosophila melanogaster, and in humans has revealed little conservation at the level of centromere DNA sequences. Also at the protein level few centromere proteins are conserved in all of these four organisms and many are unique to the different organisms. The recent analysis of the centromere structure in the yeast S. pombe by electron microscopy and detailed immunofluorescence microscopy of Drosophila centromeres have brought to light striking similarities at the overall structural level between these centromeres and the human centromere. The structural organization of the centromere is generally multilayered with a heterochromatin domain and a central core/inner plate region, which harbors the outer plate structures of the kinetochore. It is becoming increasingly clear that the key factors for assembly and function of the centromere structure are the specialized histones and modified histones which are present in the centromeric heterochromatin and in the chromatin of the central core. Thus, despite the differences in the DNA sequences and the proteins that define a centromere, there is an overall structural similarity between centromeres in evolutionarily diverse eukaryotes.","authors":"Bjerling P, Ekwall K","authors_abbrev":"Bjerling P et al.","pubmed_publication_date":"May 2002","pubmed_entrez_date":"2002-05-16","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8312388","title":"Purification and characterization of the endogenous inhibitor for proteinase B from Schizosaccharomyces pombe.","citation":"Biochimie 1993;75(10):855-9","abstract":"A rapid purification procedure for the endogenous inhibitor of proteinase yspB from Schizosaccharomyces pombe is described. Starting from a boiled extract, the purification procedure included an ionic exchange chromatography and two reverse phase chromatographies using a HPLC system. The molecular mass of the purified polypeptide was estimated to be 8,100 Da by gel filtration. The isoelectric point of the inhibitor was found to be 5.3 after electrofocusing of a purified preparation. The amino acid composition of the proteinase yspB inhibitor was analyzed after acid hydrolysis. The calculated number of residues was 67 and the corresponding molecular mass 7370 Da. There are several differences in the molecular characteristics between the inhibitor from Schizosaccharomyces pombe and the corresponding inhibitor previously purified from Saccharomyces cerevisiae which might reflect the evolutionary divergence between the two yeast genera.","authors":"Escudero B, Parra F, Suárez-Rendueles P","authors_abbrev":"Escudero B et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_session_key":"afb36655fc9930c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-06-06 07:18:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-24 12:50:27","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.12","SPAC4A8.04"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-04-24"},{"uniquename":"PMID:19029336","title":"Schizosaccharomyces pombe Pak-related protein, Pak1p/Orb2p, phosphorylates myosin regulatory light chain to inhibit cytokinesis.","citation":"J Cell Biol 2008 Dec 01;183(5):785-93","abstract":"p21-activated kinases (Paks) have been identified in a variety of eukaryotic cells as key effectors of the Cdc42 family of guanosine triphosphatases. Pak kinases play important roles in regulating the filamentous actin cytoskeleton. In this study, we describe a function for the Schizosaccharomyces pombe Pak-related protein Pak1p/Orb2p in cytokinesis. Pak1p localizes to the actomyosin ring during mitosis and cytokinesis. Loss of Pak1p function leads to accelerated cytokinesis. Pak1p mediates phosphorylation of myosin II regulatory light chain Rlc1p at serine residues 35 and 36 in vivo. Interestingly, loss of Pak1p function or substitution of serine 35 and serine 36 of Rlc1p with alanines, thereby mimicking a dephosphorylated state of Rlc1p, leads to defective coordination of mitosis and cytokinesis. This study reveals a new mechanism involving Pak1p kinase that helps ensure the fidelity of cytokinesis.","doi":"10.1083/jcb.200806127","authors":"Loo TH, Balasubramanian M","authors_abbrev":"Loo TH et al.","pubmed_publication_date":"01 Dec 2008","pubmed_entrez_date":"2008-11-26","publication_year":"2008","canto_session_key":"5a0d6b947eb9ce6d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-05-29 12:57:08","canto_approved_date":"2025-12-20 11:35:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-18 12:53:26","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1604.14c","SPAC926.03","SPAPB1A10.09","SPBC19G7.05c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2018-05-29"},{"uniquename":"PMID:26213367","title":"Human Mpn1 promotes post-transcriptional processing and stability of U6atac.","citation":"FEBS Lett 2015 Aug 19;589(18):2417-23","abstract":"Mpn1 is an exoribonuclease that modifies the spliceosomal small nuclear RNA (snRNA) U6 by trimming its oligouridine tail and introducing a cyclic phosphate group (>p). Mpn1 deficiency induces U6 3' end misprocessing, accelerated U6 decay and pre-mRNA splicing defects. Mutations in the human MPN1 gene are associated with the genodermatosis Clericuzio-type poikiloderma with neutropenia (PN). Here we present the deep sequencing of the >p-containing transcriptomes of mpn1Δ fission yeast and PN cells. While in yeast U6 seems to be the only substrate of Mpn1, human Mpn1 also processes U6atac snRNA. PN cells bear unstable U6atac species with aberrantly long and oligoadenylated 3' ends. Our data corroborate the link between Mpn1 and snRNA stability suggesting that PN could derive from pre-mRNA splicing aberrations.","doi":"10.1016/j.febslet.2015.06.046","authors":"Shchepachev V, Wischnewski H, Soneson C, Arnold AW, Azzalin CM","authors_abbrev":"Shchepachev V et al.","pubmed_publication_date":"19 Aug 2015","pubmed_entrez_date":"2015-07-28","publication_year":"2015","canto_session_key":"30fb4194283d2ce2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-08-25 12:48:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-08-25 12:48:20","canto_added_date":"2015-07-29 00:21:25","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.10","SPAC12G12.13c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-08-25"},{"uniquename":"PMID:15289661","title":"The roles of histone modifications and small RNA in centromere function.","citation":"Chromosome Res 2004;12(6):535-42","abstract":"Here, epigenetic regulation of centromeric chromatin in fission yeast (Schizosaccharomyces pombe) is reviewed, focussing on the role of histone modifications and the link to RNA interference (RNAi). Fission yeast centromeres are organized into two structurally and functionally distinct domains, both of which are required for centromere function. The central core domain anchors the kinetochore structure while the flanking heterochromatin domain is important for sister centromere cohesion. The chromatin structure of both domains is regulated epigenetically. In the central core domain, the histone H3 variant Cnp1(CENP-A) plays a key role. In the flanking heterochromatin domain, histones are kept underacetylated by the histone deacetylases (HDACs) Clr3, Clr6 and Sir2, and methylated by Clr4 methyltransferase (HMTase) to create a specific binding site for the Swi6 protein. Swi6 then directly mediates cohesin binding to the centromeric heterochromatin. Recently, a surprising link was made between heterochromatin formation and RNAi.","authors":"Ekwall K","authors_abbrev":"Ekwall K","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-08-04","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2854522","title":"Cloning and sequence determination of the gene encoding the largest subunit of the fission yeast Schizosaccharomyces pombe RNA polymerase I.","citation":"Gene 1988 Dec 30;74(2):503-15","abstract":"The gene encoding the largest subunit of RNA polymerase I (SPRPA190) was cloned from the fission yeast Schizosaccharomyces pombe by cross-hybridization with a probe containing part of the corresponding Saccharomyces cerevisiae gene RPA190. The SPRPA190 gene is present in a single copy per haploid genome and is essential for cell growth. The polypeptide encoded by this gene, as deduced from the nucleotide sequence of the uninterrupted coding frame, consists of 1689 amino acids and its calculated Mr is 189,300. The amino acid identity between the subunits of the two yeast species is 50%. Amino acid sequence conservation covers the regions previously suggested to be functionally important for the S. cerevisiae enzyme. In addition, two markedly hydrophilic regions recognized in the S. cerevisiae polypeptide can also be recognized in the S. pombe polypeptide in approximately the same positions, even though the amino acid sequences in these regions are diverged from each other. In the 5'-flanking region of the gene, several nucleotide sequence elements are detected which are also found in the two S. pombe ribosomal protein genes so far sequenced.","authors":"Yamagishi M, Nomura M","authors_abbrev":"Yamagishi M et al.","pubmed_publication_date":"30 Dec 1988","pubmed_entrez_date":"1988-12-30","publication_year":"1988","canto_session_key":"d8ee2338d00d8234","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-01-30 15:46:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 15:35:34","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC4C3.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-25"},{"uniquename":"PMID:2894829","title":"Isolation of mutants of Schizosaccharomyces pombe unable to synthesize cadystin, small cadmium-binding peptides.","citation":"Biochem Biophys Res Commun 1988 Feb 29;151(1):32-9","abstract":"Schizosaccharomyces pombe synthesize small cadmium-binding peptides cadystin, structure of which is (gamma-Glu-Cys)n-Gly, in response to cadmium. Mutants unable to synthesize cadystin were found in the mutants hypersensitive to cadmium. Some of them lack activity of either gamma-glutamylcysteine synthetase (EC 6.3.2.2) or glutathione synthetase (EC 6.3.2.3), enzyme involved in glutathione biosynthesis. Some mutants have the same activity levels of these enzymes as wild type has. These results indicate that some steps of cadystin biosynthesis are catalyzed by the enzymes catalyzing glutathione biosynthesis.","authors":"Mutoh N, Hayashi Y","authors_abbrev":"Mutoh N et al.","pubmed_publication_date":"29 Feb 1988","pubmed_entrez_date":"1988-02-29","publication_year":"1988","canto_session_key":"1cc5c597f8a24352","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2013-11-14 08:38:09","canto_approved_date":"2026-01-23 13:40:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-10 19:40:23","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22F3.10c","SPAC3F10.04"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2013-11-14"},{"uniquename":"PMID:19251905","title":"AtVPS45 is a positive regulator of the SYP41/SYP61/VTI12 SNARE complex involved in trafficking of vacuolar cargo.","citation":"Plant Physiol 2009 Apr;149(4):1668-78","abstract":"We report a functional characterization of AtVPS45 (for vacuolar protein sorting 45), a protein from the Sec1/Munc18 family in Arabidopsis (Arabidopsis thaliana) that interacts at the trans-Golgi network (TGN) with the SYP41/SYP61/VTI12 SNARE complex. A null allele of AtVPS45 was male gametophytic lethal, whereas stable RNA interference lines with reduced AtVPS45 protein levels had stunted growth but were viable and fertile. In the silenced lines, we observed defects in vacuole formation that correlated with a reduction in cell expansion and with autophagy-related defects in nutrient turnover. Moreover, transport of vacuolar cargo with carboxy-terminal vacuolar sorting determinants was blocked in the silenced lines, suggesting that AtVPS45 functions in vesicle trafficking to the vacuole. These trafficking defects are similar to those observed in vti12 mutants, supporting a functional relationship between AtVPS45 and VTI12. Consistent with this, we found a decrease in SYP41 protein levels coupled to the silencing of AtVPS45, pointing to instability and malfunction of the SYP41/SYP61/VTI12 SNARE complex in the absence of its cognate Sec1/Munc18 regulator. Based on its localization on the TGN, we hypothesized that AtVPS45 could be involved in membrane fusion of retrograde vesicles recycling vacuolar trafficking machinery. Indeed, in the AtVPS45-silenced plants, we found a striking alteration in the subcellular fractionation pattern of vacuolar sorting receptors, which are required for sorting of carboxy-terminal vacuolar sorting determinant-containing cargo. We propose that AtVPS45 is essential for recycling of the vacuolar sorting receptors back to the TGN and that blocking this step underlies the defects in vacuolar cargo trafficking observed in the silenced lines.","doi":"10.1104/pp.108.134361","authors":"Zouhar J, Rojo E, Bassham DC","authors_abbrev":"Zouhar J et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-03-03","publication_year":"2009","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10884416","title":"Modeling the fission yeast cell cycle: quantized cycle times in wee1- cdc25Delta mutant cells.","citation":"Proc Natl Acad Sci U S A 2000 Jul 05;97(14):7865-70","abstract":"A detailed mathematical model for the fission yeast mitotic cycle is developed based on positive and negative feedback loops by which Cdc13/Cdc2 kinase activates and inactivates itself. Positive feedbacks are created by Cdc13/Cdc2-dependent phosphorylation of specific substrates: inactivating its negative regulators (Rum1, Ste9 and Wee1/Mik1) and activating its positive regulator (Cdc25). A slow negative feedback loop is turned on during mitosis by activation of Slp1/anaphase-promoting complex (APC), which indirectly re-activates the negative regulators, leading to a drop in Cdc13/Cdc2 activity and exit from mitosis. The model explains how fission yeast cells can exit mitosis in the absence of Ste9 (Cdc13 degradation) and Rum1 (an inhibitor of Cdc13/Cdc2). We also show that, if the positive feedback loops accelerating the G(2)/M transition (through Wee1 and Cdc25) are weak, then cells can reset back to G(2) from early stages of mitosis by premature activation of the negative feedback loop. This resetting can happen more than once, resulting in a quantized distribution of cycle times, as observed experimentally in wee1(-) cdc25Delta mutant cells. Our quantitative description of these quantized cycles demonstrates the utility of mathematical modeling, because these cycles cannot be understood by intuitive arguments alone.","authors":"Sveiczer A, Csikasz-Nagy A, Gyorffy B, Tyson JJ, Novak B","authors_abbrev":"Sveiczer A et al.","pubmed_publication_date":"05 Jul 2000","pubmed_entrez_date":"2000-07-08","publication_year":"2000","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7370111","title":"The problem of negative results for styrene in the in vitro mutagenesis test with metabolic activation (microsomal assay):explanation by gas chromatographic analysis.","citation":"Boll Soc Ital Biol Sper 1980 Feb 15;56(3):203-7","abstract":"Mutagenic experiments in vitro were performed on yeast (S. pombe) with styrene with metabolic activation by adding at fixed times fresh mouse microsomes to the incubation mixture. Preceding studies with a single initial addition of microsomes were negative up to the maximal dose of 100 mM styrene for 60 min (5). The addition of fresh microsomes at the times 12, 24, 36 and 48 min in the presence of EDTA 40 mM resulted in an increased toxicity of styrene in vitro, but not in increased mutagenicity. Gas chromatographic determination of styrene oxide in the incubation mixture with 50 mM styrene revealed a concentration of active metabolite not capable of acting mutagenically.","authors":"Bauer C, Leporini C, Bronzetti G, Corsi C, Nieri R, Del Carratore R, Tonarelli S","authors_abbrev":"Bauer C et al.","pubmed_publication_date":"15 Feb 1980","pubmed_entrez_date":"1980-02-15","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12137808","title":"Development of a test system for inhibitors of human aldosterone synthase (CYP11B2): screening in fission yeast and evaluation of selectivity in V79 cells.","citation":"J Steroid Biochem Mol Biol 2002 Jun;81(2):173-9","abstract":"Aldosterone synthase (CYP11B2) is a mitochondrial cytochrome P450 enzyme catalyzing the last steps of aldosterone production in the adrenal cortex. A new pharmacological approach for the treatment of the aldosterone induced effects in congestive heart failure and all forms of hyperaldosteronism could be the use of CYP11B2 inhibitors. In search for such compounds, it was our goal to develop a cellular enzyme assay suitable for screening high numbers of compounds. An assay procedure for the evaluation of inhibitors using the human CYP11B2 expressed in fission yeast Schizosaccharomyces pombe was established and a series of 10 compounds was tested in this whole cellular system. Human 11beta-hydroxylase (CYP11B1), which catalyzes the production of glucocorticoids, shows more than 90% homology compared to human CYP11B2. As this enzyme should not be affected, strong inhibitors of CYP11B2 have to be tested for selectivity. For that purpose, an assay procedure with V79MZ cells that express human CYP11B1 and CYP11B2, respectively, was integrated into the evaluation process. Using these screening procedures a potent and rather selective non-steroidal inhibitor of human CYP11B2 was detected with an IC(50) value of 59nM. We also identified a very potent inhibitor of both enzymes showing a stronger inhibitory activity against the cortisol producing CYP11B1.","authors":"Ehmer PB, Bureik M, Bernhardt R, Müller U, Hartmann RW","authors_abbrev":"Ehmer PB et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-07-26","publication_year":"2002","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29196559","title":"Remarkable Evolutionary Plasticity of Centromeric Chromatin.","citation":"Cold Spring Harb Symp Quant Biol 2017;82:71-82","abstract":"Centromeres were familiar to cell biologists in the late 19th century, but for most eukaryotes the basis for centromere specification has remained enigmatic. Much attention has been focused on the cenH3 (CENP-A) histone variant, which forms the foundation of the centromere. To investigate the DNA sequence requirements for centromere specification, we applied a variety of epigenomic approaches, which have revealed surprising diversity in centromeric chromatin properties. Whereas each point centromere of budding yeast is occupied by a single precisely positioned tetrameric nucleosome with one cenH3 molecule, the \"regional\" centromeres of fission yeast contain unphased presumably octameric nucleosomes with two cenH3s. In  Caenorhabditis elegans , kinetochores assemble all along the chromosome at sites of cenH3 nucleosomes that resemble budding yeast point centromeres, whereas holocentric insects lack cenH3 entirely. The \"satellite\" centromeres of most animals and plants consist of cenH3-containing particles that are precisely positioned over homogeneous tandem repeats, but in humans, different α-satellite subfamilies are occupied by CENP-A nucleosomes with very different conformations. We suggest that this extraordinary evolutionary diversity of centromeric chromatin architectures can be understood in terms of the simplicity of the task of equal chromosome segregation that is continually subverted by selfish DNA sequences.","doi":"10.1101/sqb.2017.82.033605","authors":"Henikoff S, Thakur J, Kasinathan S, Talbert PB","authors_abbrev":"Henikoff S et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2017-12-03","publication_year":"2017","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2017-12-05 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084838","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.26"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:3477553","title":"Growth polarity and cytokinesis in fission yeast: the role of the cytoskeleton.","citation":"J Cell Sci Suppl 1986;5:229-41","abstract":"The distribution of F-actin in the fission yeast Schizosaccharomyces pombe was investigated by fluorescence microscopy using rhodamine-conjugated phalloidin. Fluorescence was seen either at the ends of the cell or at the cell equator. End staining was predominantly in the form of dots whilst equatorial actin was resolved as a filamentous band. The different staining patterns showed a close correlation with the known pattern of cell wall deposition through the cell cycle. In small, newly divided cells actin was localized at the single growing cell end whilst initiation of bipolar cell growth was coincident with the appearance of actin at both ends of the cell. As cells ceased to grow and entered cell division, a ring of actin was seen to anticipate the deposition of the septum at cytokinesis. The relationship between actin and cell wall deposition was further confirmed in three temperature-sensitive cell division cycle (cdc) mutants; cdc10, cdc11 and cdc13. Immunofluorescence microscopy of S. pombe with an anti-tubulin antibody revealed a system of cytoplasmic microtubules extending between the cell ends. The function of these was investigated in the cold-sensitive, benomyl-resistant mutant ben4. In cold-grown cells actin was seen to form conspicuous filamentous rings around the nucleus. The origin of these and the possible role of microtubules in the cell-cycle-dependent rearrangements of F-actin are discussed.","authors":"Marks J, Hagan IM, Hyams JS","authors_abbrev":"Marks J et al.","pubmed_publication_date":"1986","pubmed_entrez_date":"1986-01-01","publication_year":"1986","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10974558","title":"Corrigendum to: \"A new inducible protein expression system in fission yeast based on the glucose-repressed inv1 promoter\".","citation":"Gene 2000 Aug 22;254(1-2):265-6","abstract":"","authors":"Iacovoni JS, Russell P, Gaits F","authors_abbrev":"Iacovoni JS et al.","pubmed_publication_date":"22 Aug 2000","pubmed_entrez_date":"2000-09-07","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25368411","title":"Nic1 inactivation enables stable isotope labeling with 13C615N4-arginine in Schizosaccharomyces pombe.","citation":"Mol Cell Proteomics 2015 Jan;14(1):243-50","abstract":"Stable Isotope Labeling by Amino Acids (SILAC) is a commonly used method in quantitative proteomics. Because of compatibility with trypsin digestion, arginine and lysine are the most widely used amino acids for SILAC labeling. We observed that Schizosaccharomyces pombe (fission yeast) cannot be labeled with a specific form of arginine, (13)C(6) (15)N(4)-arginine (Arg-10), which limits the exploitation of SILAC technology in this model organism. We hypothesized that in the fission yeast the guanidinium group of (13)C(6) (15)N(4)-arginine is catabolized by arginase and urease activity to (15)N1-labeled ammonia that is used as a precursor for general amino acid biosynthesis. We show that disruption of Ni(2+)-dependent urease activity, through deletion of the sole Ni(2+) transporter Nic1, blocks this recycling in ammonium-supplemented EMMG medium to enable (13)C(6) (15)N(4)-arginine labeling for SILAC strategies in S. pombe. Finally, we employed Arg-10 in a triple-SILAC experiment to perform quantitative comparison of G1 + S, M, and G2 cell cycle phases in S. pombe.","doi":"10.1074/mcp.O114.045302","authors":"Carpy A, Patel A, Tay YD, Hagan IM, Macek B","authors_abbrev":"Carpy A et al.","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-11-05","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-11-06 01:16:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23669133","title":"Csi1 illuminates the mechanism and function of Rabl configuration.","citation":"Nucleus 2013;4(3):176-81","abstract":"The nuclear envelope not only compartmentalizes the genome but is also home to the SUN-KASH domain proteins, which play essential roles both in genome organization and in linking the nucleus to the cytoskeleton. In interphase fission yeast cells, centromeres are clustered near the nuclear periphery. A recent report demonstrates that the inner nuclear membrane SUN domain protein Sad1 and a novel protein Csi1 connect centromeres to the nuclear envelope and that centromere clustering during interphase is critical for the efficient capture of kinetochores by microtubules during mitosis.","doi":"10.4161/nucl.24876","authors":"Hou H, Kallgren SP, Jia S","authors_abbrev":"Hou H et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-05-15","publication_year":"2013","canto_session_key":"daa8cb6e58fafa6c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Haitong Hou","canto_approved_date":"2013-07-12 14:39:30","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-07-11 16:41:08","canto_added_date":"2013-06-16 07:56:18","annotation_curators":[{"name":"Haitong Hou","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.03c","SPBC12D12.01","SPBC2G2.14"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2013-07-11"},{"uniquename":"EMBL:SPPYP","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1272244","title":"Genetic analysis of antisuppressor mutants in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1976 Dec 31;142(4):251-61","abstract":"Fourteen unlinked sin genes could be mutated to recessive antisuppressor alleles preventing the expression of suppressors in the fission yeast Schizosaccharomyces pombe. cyh1 alleles, resistant to the ribosomal inhibitor cycloheximide, also have some antisuppressor effect. The genetical and physiological characterization of these mutants is consistent with the hypothesis that they affect components of the messenger RNA translation machinery such as tRNA modifying enzymes or ribosomal proteins.","authors":"Thuriaux P, Minet M, Hofer F, Leupold U","authors_abbrev":"Thuriaux P et al.","pubmed_publication_date":"31 Dec 1976","pubmed_entrez_date":"1976-12-31","publication_year":"1976","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25466257","title":"Global proteome turnover analyses of the Yeasts S. cerevisiae and S. pombe.","citation":"Cell Rep 2014 Dec 11;9(5):1959-1965","abstract":"How cells maintain specific levels of each protein and whether that control is evolutionarily conserved are key questions. Here, we report proteome-wide steady-state protein turnover rate measurements for the evolutionarily distant but ecologically similar yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe. We find that the half-life of most proteins is much longer than currently thought and determined to a large degree by protein synthesis and dilution due to cell division. However, we detect a significant subset of proteins (∼15%) in both yeasts that are turned over rapidly. In addition, the relative abundances of orthologous proteins between the two yeasts are highly conserved across the 400 million years of evolution. In contrast, their respective turnover rates differ considerably. Our data provide a high-confidence resource for studying protein degradation in common yeast model systems.","doi":"10.1016/j.celrep.2014.10.065","authors":"Christiano R, Nagaraj N, Fröhlich F, Walther TC","authors_abbrev":"Christiano R et al.","pubmed_publication_date":"11 Dec 2014","pubmed_entrez_date":"2014-12-04","publication_year":"2014","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2014-12-05 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17027039","title":"A general bilinear model to describe growth or decline time profiles.","citation":"Math Biosci 2007 Jan;205(1):108-36","abstract":"Linear models are widely used because of their unrivaled simplicity, but they cannot be applied for data that have a turning-or rate-change-point, even if the data show good linearity sufficiently far from this point. To describe such bilinear-type data, a completely generalized version of a linearized biexponential model (LinBiExp) is proposed here to make possible smooth and fully parametrizable transitions between two linear segments while still maintaining a clear connection with the linear models. Applications and brief conclusions are presented for various time profiles of biological and medical interest including growth profiles, such as those of human stature, agricultural crops and fruits, multicellular tumor spheroids, single fission yeast cells, or even labor productivity, and decline profiles, such as age-effects on cognition in patients who develop dementia and lactation yields in dairy cattle. In all these cases, quantitative model selection criteria such as the Akaike and the Schwartz Bayesian information criteria indicated the superiority of the bilinear model compared to adequate less parametrized alternatives such as linear, parabolic, exponential, or classical growth (e.g., logistic, Gompertz, Weibull, and Richards) models. LinBiExp provides a versatile and useful five-parameter bilinear functional form that is convenient to implement, is suitable for full optimization, and uses intuitive and easily interpretable parameters.","authors":"Buchwald P","authors_abbrev":"Buchwald P","pubmed_publication_date":"Jan 2007","pubmed_entrez_date":"2006-10-10","publication_year":"2007","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9755190","title":"Histone deacetylase homologs regulate epigenetic inheritance of transcriptional silencing and chromosome segregation in fission yeast.","citation":"Genetics 1998 Oct;150(2):563-76","abstract":"Position-effect control at the silent mat2-mat3 interval and at centromeres and telomeres in fission yeast is suggested to be mediated through the assembly of heterochromatin-like structures. Therefore, trans-acting genes that affect silencing may encode either chromatin proteins, factors that modify them, or factors that affect chromatin assembly. Here, we report the identification of an essential gene, clr6 (cryptic loci regulator), which encodes a putative histone deacetylase that when mutated affects epigenetically maintained repression at the mat2-mat3 region and at centromeres and reduces the fidelity of chromosome segregation. Furthermore, we show that the Clr3 protein, when mutated, alleviates recombination block at mat region as well as silencing at donor loci and at centromeres and telomeres, also shares strong homology to known histone deacetylases. Genetic analyses indicate that silencing might be regulated by at least two overlapping histone deacetylase activities. We also found that transient inhibition of histone deacetylase activity by trichostatin A results in the increased missegregation of chromosomes in subsequent generations and, remarkably, alters the imprint at the mat locus, causing the heritable conversion of the repressed epigenetic state to the expressed state. This work supports the model that the level of histone deacetylation has a role in the assembly of repressive heterochromatin and provides insight into the mechanism of epigenetic inheritance.","authors":"Grewal SI, Bonaduce MJ, Klar AJ","authors_abbrev":"Grewal SI et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-10-02","publication_year":"1998","canto_session_key":"733ed151713320db","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-05-18 09:18:54","canto_approved_date":"2024-01-08 20:45:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-11 15:00:26","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":31,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.07c","SPBC36.05c","SPBC800.03","SPBC2D10.17"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-05-18"},{"uniquename":"PMID:12725728","title":"The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function.","citation":"Curr Biol 2003 Apr 29;13(9):715-24","abstract":"Myosins are motor proteins involved in processes like cell motility, vesicle transport, or cytokinesis. In a variety of organisms, a novel group of proteins forming the UCS (UNC-45/CRO1/SHE4) domain-containing family are essential for proper myosin function. The Saccharomyces cerevisae UCS domain protein She4p is involved in two myosin-requiring events, endocytosis and mRNA localization.\nIn contrast to UCS domain proteins from other organisms that interact with class II myosins, we demonstrate that She4p associates with yeast class I and class V myosins. She4p binds to motor domains of class V myosin Myo4p and class I myosin Myo5p, and this binding depends on She4p's UCS domain. In vivo, She4p is essential for the function and localization of Myo3p, Myo4p, and Myo5p (but not of Myo2p) and for colocalization of class I myosins with cortical actin patches. In vitro, She4p stimulates binding of Myo5p to filamentous actin. Wild-type She4p, but not a mutant lacking the UCS domain, accumulates in a cap-like structure at the bud tip. This localization requires Myo2p and actin, suggesting a Myo2-dependent mechanism by which She4p is targeted to the bud cap. Localization of She4p is essential for proper positioning and myosin-actin association of cortical Myo5p.\nOur results suggest that She4p is a novel myosin motor domain binding protein and operates as a localized regulator of myosin function of class I and likely class V myosins.","authors":"Wesche S, Arnold M, Jansen RP","authors_abbrev":"Wesche S et al.","pubmed_publication_date":"29 Apr 2003","pubmed_entrez_date":"2003-05-03","publication_year":"2003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC613.04c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1312461","title":"Demonstration of retrotransposition of the Tf1 element in fission yeast.","citation":"EMBO J 1992 Mar;11(3):1145-53","abstract":"Tf1, a retrotransposon from fission yeast, has LTRs and coding sequences resembling the protease, reverse transcriptase and integrase domains of retroviral pol genes. A unique aspect of Tf1 is that it contains a single open reading frame whereas other retroviruses and retrotransposons usually possess two or more open reading frames. To determine whether Tf1 can transpose, we overproduced Tf1 transcripts encoded by a plasmid copy of the element marked with a neo gene. Approximately 0.1-4.0% of the cell population acquired chromosomally inherited resistance to G418. DNA blot analysis demonstrated that such strains had acquired both Tf1 and neo specific sequences within a restriction fragment of the same size; the size of this restriction fragment varied between different isolates. Structural analysis of the cloned DNA flanking the Tf1-neo element of two transposition candidates with the same regions in the parent strain showed that the ability to grow on G418 was due to transposition of Tf1-neo and not other types of recombination events.","authors":"Levin HL, Boeke JD","authors_abbrev":"Levin HL et al.","pubmed_publication_date":"Mar 1992","pubmed_entrez_date":"1992-03-01","publication_year":"1992","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10497270","title":"Topoisomerase III is essential for accurate nuclear division in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1999 Oct 15;27(20):4050-8","abstract":"Topoisomerases catalyse changes in the topological state of DNA and are required for many aspects of DNA metabolism. While the functions of topoisomerases I and II in eukaryotes are well established, the role of topoisomerase III remains poorly defined. We have identified a gene in the fission yeast Schizosaccharomyces pombe, designated top3 (+), which shows significant sequence similarity to genes encoding topoisomerase III enzymes in other eukaryotic species. In common with murine TOP3 alpha, but in contrast to Saccharomyces cerevisiae TOP3, the S.pombe top3 (+)gene is essential for long-term cell viability. Fission yeast haploid spores containing a disrupted top3 (+)gene germinate successfully, but then undergo only a limited number of cell divisions. Analysis of these top3 mutants revealed evidence of aberrant mitotic chromosome segregation, including the 'cut' phenotype, where septation is completed prior to nuclear division. Consistent with the existence of an intimate association (originally identified in S.cerevisiae ) between topoisomerase III and DNA helicases of the RecQ family, deletion of the rqh1 (+)gene encoding the only known RecQ helicase in S.pombe suppresses lethality in top3 mutants. This conservation of genetic interaction between two widely diverged yeasts suggests that the RecQ family helicases encoded by the Bloom's and Werner's syndrome genes are likely to act in concert with topoisomerase III isozymes in human cells. Our data are consistent with a model in which the association of a RecQ helicase and topoisomerase III is important for facilitating decatenation of late stage replicons to permit faithful chromosome segregation during anaphase.","authors":"Goodwin A, Wang SW, Toda T, Norbury C, Hickson ID","authors_abbrev":"Goodwin A et al.","pubmed_publication_date":"15 Oct 1999","pubmed_entrez_date":"1999-09-25","publication_year":"1999","canto_session_key":"2267c01b48c1c47c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-02-22 18:50:52","canto_approved_date":"2020-06-19 12:22:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-22 18:50:45","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16G5.12c","SPAC2G11.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-02-22"},{"uniquename":"PMID:32071154","title":"Fission Yeast Puf2, a Pumilio and FBF Family RNA-Binding Protein, Links Stress Granules to Processing Bodies.","citation":"Mol Cell Biol 2020 Apr 13;40(9)","abstract":"Stress granules (SGs) are cytoplasmic aggregates formed upon stress when untranslated messenger ribonucleoproteins accumulate in the cells. In a green fluorescent protein library screening of the fission yeast SG proteins, Puf2 of the PUF family of RNA-binding proteins was identified that is required for SG formation after deprivation of glucose. Accordingly, the  puf2  mutant is defective in recovery from glucose starvation with a much longer lag to reenter the cell cycle. In keeping with these results, Puf2 contains several low-complexity and intrinsically disordered protein regions with a tendency to form aggregates and, when overexpressed, it represses translation to induce aggregation of poly(A) binding protein Pabp, the signature constituent of SGs. Intriguingly, overexpression of Puf2 also enhances the structure of processing bodies (PBs), another type of cytoplasmic RNA granule, a complex of factors involved in mRNA degradation. In this study, we demonstrate a function of the fission yeast PB in SG formation and show Puf2 may provide a link between these two structures.","doi":"10.1128/MCB.00589-19","authors":"Hsiao WY, Wang YT, Wang SW","authors_abbrev":"Hsiao WY et al.","pubmed_publication_date":"13 Apr 2020","pubmed_entrez_date":"2020-02-20","publication_year":"2020","canto_session_key":"779cb119eb8301e0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Shao-Win Wang","canto_first_approved_date":"2020-04-10 14:42:51","canto_approved_date":"2021-04-07 15:27:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-31 07:15:57","canto_added_date":"2020-02-21 01:15:04","annotation_curators":[{"name":"Shao-Win Wang","community_curator":true,"annotation_count":32,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":42,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G6.02c","SPAC17C9.03","SPBC3D6.08c","SPAC664.04c","SPBC409.07c","SPBC17A3.04c","SPCC550.14","SPAC4G8.03c","SPAC1751.03","SPAC6G10.11c","SPCC1682.08c","SPBC23E6.01c","SPAC24H6.07","SPAC30C2.04","SPCP1E11.11","SPAC25G10.08","SPAC821.05","SPBC18E5.11c","SPBC3B9.21","SPAC20G4.08","SPAC22A12.04c","SPBC18H10.04c","SPBC21B10.03c","SPCC31H12.08c","SPAC6G9.14","SPAC17A2.09c","SPBC17D11.05","SPAC4D7.05","SPAC1687.22c","SPAC24B11.06c","SPBC56F2.08c","SPAC23C11.02c","SPAC637.07","SPBP35G2.14","SPAC17A5.15c","SPAC19A8.12","SPBC18H10.13","SPBC1709.02c","SPAC17A5.14","SPBP8B7.21","SPBC3D6.15","SPBC776.09","SPAC4G9.05","SPAC57A7.04c","SPBC19G7.10c","SPBP8B7.11"],"gene_count":46,"ltp_gene_count":28,"approved_date":"2020-04-10"},{"uniquename":"PMID:34188069","title":"Cell wall integrity is compromised under temperature stress in Schizosaccharomyces pombe expressing a valproic acid-sensitive vas4 mutant.","citation":"Sci Rep 2021 Jun 29;11(1):13483","abstract":"Valproic acid (VPA) is widely used as a eutherapeutic and safe anticonvulsant drug, but the mechanism is not well elucidated. Histone deacetylases (HDACs) were first identified as direct targets of VPA. Many loss-of function mutants in S. pombe have been shown to be VPA sensitive but not sensitive to other HDAC inhibitors, such as sodium butyrate or trichostatin A (TSA). This difference suggests that there are multiple VPA target genes. In the current study, we isolated a VPA-sensitive (vas) mutant, vas4-1, and cloned the VPA target gene vas4 + /vrg4 +  by performing complementation experiments. The vas4 + /vrg4 +  gene encodes a putative Golgi GDP-mannose transporter, Vrg4, which is highly homologous with ScVrg4p. Physiological experiments indicated that SpVrg4p is involved in maintaining cell wall integrity (CWI) under high- or low-temperature stress. The results of a coimmunoprecipitation assay suggested that SpVrg4p may be transferred from the ER to the Golgi through SpGot1p loaded COPII vesicles, and both single and double mutations (S263C and A271V) in SpVrg4p compromised this transfer. Our results suggested that CWI in S. pombe is compromised under temperature stress by the VPA-sensitive vas4 mutant.","doi":"10.1038/s41598-021-92466-8","authors":"Qiao S, Luo X, Wang H, Fang Y, Zhang L","authors_abbrev":"Qiao S et al.","pubmed_publication_date":"29 Jun 2021","pubmed_entrez_date":"2021-06-30","publication_year":"2021","canto_session_key":"108d7be560f7a78f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-07-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7596817","title":"gar2 is a nucleolar protein from Schizosaccharomyces pombe required for 18S rRNA and 40S ribosomal subunit accumulation.","citation":"Nucleic Acids Res 1995 Jun 11;23(11):1912-8","abstract":"Several nucleolar proteins, such as nucleolin, NOP1/fibrillarin, SSB1, NSR1 and GAR1 share a common glycine and arginine rich structural motif called the GAR domain. To identify novel nucleolar proteins from fission yeast we screened Schizosaccharomyces pombe genomic DNA libraries with a probe encompassing the GAR structural motif. Here we report the identification and characterization of a S.pombe gene coding for a novel nucleolar protein, designated gar2. The structure of the fission yeast gar2 is reminiscent of that of nucleolin from vertebrates and NSR1 from Saccharomyces cerevisiae. In addition, like these proteins, gar2 has a nucleolar localisation. The disruption of the gar2+ gene affects normal cell growth, leads to an accumulation of 35S pre-rRNA and a decrease of mature 18S rRNA steady state levels. Moreover, ribosomal profiles of the mutant show an increase of free 60S ribosomal subunits and an absence of free 40S ribosomal subunits. gar2 is able to rescue a S.cerevisiae mutant lacking NSR1, thus establishing gar2 as a functional homolog of NSR1. We propose that gar2 helps the assembly of pre-ribosomal particles containing 18S rRNA.","authors":"Gulli MP, Girard JP, Zabetakis D, Lapeyre B, Melese T, Caizergues-Ferrer M","authors_abbrev":"Gulli MP et al.","pubmed_publication_date":"11 Jun 1995","pubmed_entrez_date":"1995-06-11","publication_year":"1995","canto_session_key":"ab7d71d62a2030e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-04-21 12:53:15","canto_approved_date":"2026-02-20 13:33:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-19 12:03:32","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC140.02"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-04-21"},{"uniquename":"PMID:10843998","title":"Transcription termination by RNA polymerase III in fission yeast. A genetic and biochemically tractable model system.","citation":"J Biol Chem 2000 Sep 15;275(37):29076-81","abstract":"In order for RNA polymerase (pol) III to produce a sufficient quantity of RNAs of appropriate structure, initiation, termination, and reinitiation must be accurate and efficient. Termination-associated factors have been shown to facilitate reinitiation and regulate transcription in some species. Suppressor tRNA genes that differ in the dT(n) termination signal were examined for function in Schizosaccharomyces pombe. We also developed an S. pombe extract that is active for tRNA transcription that is described here for the first time. The ability of this tRNA gene to be transcribed in extracts from different species allowed us to compare termination in three model systems. Although human pol III terminates efficiently at 4 dTs and S. pombe at 5 dTs, Saccharomyces cerevisiae pol III requires 6 dTs to direct comparable but lower termination efficiency and also appears qualitatively distinct. Interestingly, this pattern of sensitivity to a minimal dT(n) termination signal was found to correlate with the sensitivity to alpha-amanitin, as S. pombe was intermediate between human and S. cerevisiae pols III. The results establish that the pols III of S. cerevisiae, S. pombe, and human exhibit distinctive properties and that termination occurs in S. pombe in a manner that is functionally more similar to human than is S. cerevisiae.","authors":"Hamada M, Sakulich AL, Koduru SB, Maraia RJ","authors_abbrev":"Hamada M et al.","pubmed_publication_date":"15 Sep 2000","pubmed_entrez_date":"2000-06-14","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15616197","title":"Identification of cell cycle-regulated genes in fission yeast.","citation":"Mol Biol Cell 2005 Mar;16(3):1026-42","abstract":"Cell cycle progression is both regulated and accompanied by periodic changes in the expression levels of a large number of genes. To investigate cell cycle-regulated transcriptional programs in the fission yeast Schizosaccharomyces pombe, we developed a whole-genome oligonucleotide-based DNA microarray. Microarray analysis of both wild-type and cdc25 mutant cell cultures was performed to identify transcripts whose levels oscillated during the cell cycle. Using an unsupervised algorithm, we identified 747 genes that met the criteria for cell cycle-regulated expression. Peaks of gene expression were found to be distributed throughout the entire cell cycle. Furthermore, we found that four promoter motifs exhibited strong association with cell cycle phase-specific expression. Examination of the regulation of MCB motif-containing genes through the perturbation of DNA synthesis control/MCB-binding factor (DSC/MBF)-mediated transcription in arrested synchronous cdc10 mutant cell cultures revealed a subset of functional targets of the DSC/MBF transcription factor complex, as well as certain gene promoter requirements. Finally, we compared our data with those for the budding yeast Saccharomyces cerevisiae and found approximately 140 genes that are cell cycle regulated in both yeasts, suggesting that these genes may play an evolutionarily conserved role in regulation of cell cycle-specific processes. Our complete data sets are available at http://giscompute.gis.a-star.edu.sg/~gisljh/CDC.","authors":"Peng X, Karuturi RK, Miller LD, Lin K, Jia Y, Kondu P, Wang L, Wong LS, Liu ET, Balasubramanian MK, Liu J","authors_abbrev":"Peng X et al.","pubmed_publication_date":"Mar 2005","pubmed_entrez_date":"2004-12-24","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25273478","title":"Constriction model of actomyosin ring for cytokinesis by fission yeast using a two-state sliding filament mechanism.","citation":"J Chem Phys 2014 Sep 28;141(12):125101","abstract":"We developed a model describing the structure and contractile mechanism of the actomyosin ring in fission yeast, Schizosaccharomyces pombe. The proposed ring includes actin, myosin, and α-actinin, and is organized into a structure similar to that of muscle sarcomeres. This structure justifies the use of the sliding-filament mechanism developed by Huxley and Hill, but it is probably less organized relative to that of muscle sarcomeres. Ring contraction tension was generated via the same fundamental mechanism used to generate muscle tension, but some physicochemical parameters were adjusted to be consistent with the proposed ring structure. Simulations allowed an estimate of ring constriction tension that reproduced the observed ring constriction velocity using a physiologically possible, self-consistent set of parameters. Proposed molecular-level properties responsible for the thousand-fold slower constriction velocity of the ring relative to that of muscle sarcomeres include fewer myosin molecules involved, a less organized contractile configuration, a low α-actinin concentration, and a high resistance membrane tension. Ring constriction velocity is demonstrated as an exponential function of time despite a near linear appearance. We proposed a hypothesis to explain why excess myosin heads inhibit constriction velocity rather than enhance it. The model revealed how myosin concentration and elastic resistance tension are balanced during cytokinesis in S. pombe.","doi":"10.1063/1.4896164","authors":"Jung YW, Mascagni M","authors_abbrev":"Jung YW et al.","pubmed_publication_date":"28 Sep 2014","pubmed_entrez_date":"2014-10-03","publication_year":"2014","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2014-10-04 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16085489","title":"The 14-3-3 protein rad24p modulates function of the cdc14p family phosphatase clp1p/flp1p in fission yeast.","citation":"Curr Biol 2005 Aug 09;15(15):1376-83","abstract":"Schizosaccharomyces pombe cells divide through the use of an actomyosin-based contractile ring. In response to perturbation of the actomyosin ring, S. pombe cells delay in a \"cytokinesis-competent\" state characterized by continuous repair and maintenance of the actomyosin ring and a G2 delay. This checkpoint mechanism requires the function of the Cdc14p-family phosphatase Clp1p/Flp1p and the septation initiation network (SIN). In response to cytokinetic defects, Clp1p, normally nucleolar in interphase, is retained in the cytoplasm until completion of cell division in a SIN-dependent manner. Here, we show that a phosphorylated form of Clp1p binds the 14-3-3 protein Rad24p and is retained in the cytoplasm in a Rad24p-dependent manner in response to cytokinesis defects. This physical interaction depends on the function of the SIN component, Sid2p. In the absence of Rad24p, cells are unable to maintain SIN signaling and lose viability upon mild cytokinetic stress. The requirement of Rad24p in this checkpoint is bypassed by ectopic activation of the SIN. Furthermore, SIN-dependent nuclear exclusion of Clp1p is dependent on Rad24p function. We conclude that Rad24p-mediated cytoplasmic retention of Clp1p/Flp1p is important for cell viability upon stress to the division apparatus.","authors":"Mishra M, Karagiannis J, Sevugan M, Singh P, Balasubramanian MK","authors_abbrev":"Mishra M et al.","pubmed_publication_date":"09 Aug 2005","pubmed_entrez_date":"2005-08-09","publication_year":"2005","canto_session_key":"33e1584505554874","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-21 11:20:20","canto_approved_date":"2024-09-25 14:06:19","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2020-01-22 22:42:24","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPBC21.06c","SPAC4A8.15c","SPAC8E11.02c","SPAP8A3.08","SPAC1782.09c","SPCC1739.11c","SPBC244.01c","SPBC19G7.05c","SPAC17A2.13c","SPAC6F6.08c","SPAC1F5.04c"],"gene_count":12,"ltp_gene_count":11,"approved_date":"2016-09-21"},{"uniquename":"GO_REF:0000024","title":"Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.","abstract":"Method for transferring manual annotations to an entry based on a curator's judgment of its similarity to a putative ortholog that has annotations that are supported with experimental evidence. Annotations are created when a curator judges that the sequence of a protein shows high similarity to another protein that has annotation(s) supported by experimental evidence (and therefore display one of the evidence codes EXP, IDA, IGI, IMP, IPI or IEP). Annotations resulting from the transfer of GO terms display the 'ISS' evidence code and include an accession for the protein from which the annotation was projected in the 'with' field (column 8). This field can contain either a UniProtKB accession or an IPI (International Protein Index) identifier. Only annotations with an experimental evidence code and which do not have the 'NOT' qualifier are transferred. Putative orthologs are chosen using information combined from a variety of complementary sources. Potential orthologs are initially identified using sequence similarity search programs such as BLAST. Orthology relationships are then verified manually using a combination of resources including sequence analysis tools, phylogenetic and comparative genomics databases such as Ensembl Compara, INPARANOID and OrthoMCL, as well as other specialised databases such as species-specific collections (e.g. HGNC's HCOP). In all cases curators check each alignment and use their experience to assess whether similarity is considered to be strong enough to infer that the two proteins have a common function so that they can confidently project an annotation. While there is no fixed cut-off point in percentage sequence similarity, generally proteins which have greater than 30% identity that covers greater than 80% of the length of both proteins are examined further. For mammalian proteins this cut-off tends to be higher, with an average of 80% identity over 90% of the length of both proteins. Strict orthologs are desirable but not essential. In general, when there is evidence of multiple paralogs for a single species, annotations using less specific GO terms are transferred to the paralogs, however, annotations using more specific GO terms may be transferred to the most similar paralog in each species, this decision is taken on a case by case basis and may be influenced by statements by researchers in the field. Further detailed information on this procedure, including how ISS annotations are made to protein isoforms, can be found at: http://www.ebi.ac.uk/GOA/ISS_method.html.","authors":"AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators.","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.11","SPAC3H1.08c","SPAC3A12.11c","SPAC1486.05","SPBC365.20c","SPCC16A11.08","SPAC30D11.07","SPBP35G2.16c","SPAC11G7.01","SPAC1556.08c","SPAC57A10.08c","SPCC965.03","SPBC14C8.09c","SPAC3A11.03","SPAC27D7.14c","SPBC3F6.03","SPCC737.08","SPCC1840.09","SPBC1778.03c","SPAC4G9.02","SPBC29A3.06","SPAC1F7.14c","SPBC16E9.18","SPBC27B12.10c","SPBC20F10.01","SPCC330.13","SPAC328.05","SPCC1322.13","SPAC20G8.09c","SPAC16E8.17c","SPAC9G1.05","SPAC17G6.02c","SPBC1539.09c","SPAC977.09c","SPBC1198.08","SPCC1840.11","SPAC688.09","SPBC4B4.07c","SPCC1620.07c","SPAPB1E7.03","SPBC1539.06","SPCC1620.10","SPAC3G6.03c","SPAC25B8.09","SPAC1834.05","SPAC3G9.15c","SPBC25B2.01","SPAC27F1.06c","SPAP11E10.01","SPBC3H7.03c","SPAC4G9.17c","SPBC1271.05c","SPCC1739.02c","SPCC736.10c","SPCC737.02c","SPAC977.01","SPBC2F12.15c","SPCC285.16c","SPBC4B4.04","SPAC2C4.03c","SPAC1610.02c","SPAC1527.02","SPAC1039.07c","SPAC18G6.06","SPAC4F10.07c","SPAC1A6.10","SPAPB17E12.10c","SPAC19G12.08","SPCC16C4.13c","SPAC23A1.15c","SPAC30D11.05","SPCC825.05c","SPAC25B8.17","SPAPJ691.03","SPCC594.06c","SPAC977.02","SPCC24B10.22","SPAC1805.09c","SPAC3A12.13c","SPCC1682.14","SPBC646.14c","SPBC800.09","SPAC644.10","SPBC16D10.01c","SPAC56E4.05","SPBC14C8.02","SPAC227.19c","SPBC336.13c","SPCC162.06c","SPCC4G3.17","SPBC18H10.13","SPAC22H12.03","SPBC3B9.11c","SPAC222.05c","SPCC777.10c","SPAC6F12.06","SPAC16A10.05c","SPBC12C2.05c","SPAC1002.05c","SPAC13G6.02c","SPAC23G3.06","SPBC16C6.06","SPBC17D1.03c","SPAC4D7.10c","SPAC9G1.08c","SPAC22F8.09","SPAC3F10.12c","SPAC25H1.02","SPAC750.04c","SPAC644.18c","SPAPB1A11.02","SPCC16C4.01","SPAC1B3.18c","SPAC15A10.05c","SPAC3F10.06c","SPBC9B6.07","SPBC29A3.11c","SPBC106.15","SPAC19B12.11c","SPCPB1C11.02","SPAC17A2.02c","SPBC15D4.11c","SPCC24B10.04","SPAC25A8.03c","SPBC119.06","SPBC1604.07","SPBC27B12.07","SPAC9E9.04","SPBC21C3.13","SPAC12G12.12","SPBC29A3.10c","SPBC12D12.05c","SPBC19C2.15c","SPAPB8E5.05","SPAC227.10","SPAP32A8.02","SPAC8C9.16c","SPAC1687.21","SPBC13G1.11","SPAC8F11.03","SPBC776.06c","SPAC29A4.03c","SPBC428.01c","SPCC285.12","SPBC16E9.06c","SPAC16.04","SPAC25H1.05","SPCC622.16c","SPBC4F6.04","SPCC4G3.02","SPAP27G11.03","SPAC23C4.14","SPAC10F6.10","SPAC56F8.08","SPBC19F8.05","SPAC589.05c","SPBC211.01","SPAC6F6.13c","SPBC428.19c","SPBC685.04c","SPBC354.10","SPAC16E8.03","SPAC11D3.10","SPAC29A4.09","SPBC16A3.16","SPCC548.03c","SPBC146.04","SPCC191.08","SPBC1711.11","SPAC6C3.09","SPAPB8E5.02c","SPCC63.05","SPAPB1A10.11c","SPAC31A2.11c","SPBC887.12","SPBC18H10.19","SPBC3B9.13c","SPAPB24D3.09c","SPAC1039.08","SPBC28E12.06c","SPCC965.09","SPCP31B10.07","SPAC227.18","SPCPJ732.02c","SPBC16A3.18","SPBC32F12.08c","SPAC2E1P5.05","SPBP35G2.07","SPAC16E8.10c","SPAC19A8.06","SPAC17H9.16","SPCC306.04c","SPBC3D6.08c","SPAC1565.08","SPSNRNA.02","SPBC1A4.09","SPBC29A10.10c","SPBC17A3.10","SPAC22H12.04c","SPCC306.06c","SPAC3G9.09c","SPBC359.01","SPBC36B7.02","SPBC31F10.11c","SPAC30D11.04c","SPCC1322.09","SPCC31H12.07","SPBC3B8.07c","SPBC1604.25","SPAC31A2.15c","SPAC1F12.05","SPCC63.11","SPBC19C7.11","SPCC162.07","SPCC74.05","SPCC330.09","SPBC27.01c","SPAC11G7.04","SPBC21B10.07","SPCC126.06","SPBC56F2.09c","SPBC4F6.14","SPBC13E7.05","SPBC1683.05","SPBC428.02c","SPBC543.03c","SPAC8F11.02c","SPBC2D10.13","SPAC12G12.15","SPBC1773.17c","SPBC19C7.01","SPCC970.06","SPAC31G5.19","SPAC24C9.10c","SPAC17A2.03c","SPBC1289.14","SPAC1486.07c","SPAC2F3.01","SPBC3B8.05","SPBC3B9.14c","SPCC1840.04","SPAC1002.14","SPBC365.07c","SPBC11G11.05","SPAP7G5.06","SPBC1271.13","SPBC1718.06","SPAC4F10.09c","SPAC1006.01","SPAC644.08","SPCC645.02","SPCC4G3.10c","SPAC664.05","SPBP4H10.15","SPCC18.17c","SPBC16G5.04","SPBC16D10.02","SPBP35G2.05c","SPBPB8B6.02c","SPAC1A6.03c","SPCC16A11.04","SPMIT.06","SPCC1322.12c","SPBC577.13","SPBC800.06","SPBPB8B6.03","SPCC584.11c","SPBC409.14c","SPAC22A12.12c","SPBC336.05c","SPBC23G7.05","SPAC9.05","SPCC1442.03","SPBC19G7.01c","SPAC4D7.03","SPCC1322.01","SPBC660.05","SPAC3A12.08","SPAC30C2.05","SPBC8D2.13","SPCC576.05","SPBC36.09","SPBP8B7.15c","SPBC1685.02c","SPBC146.09c","SPAC30D11.11","SPAC15E1.10","SPAC821.05","SPCC576.09","SPAC22E12.10c","SPAC57A7.15c","SPAC3H8.06","SPBC8E4.04","SPAC1687.06c","SPAC823.11","SPAC1834.01","SPBC1198.14c","SPAC23C11.05","SPAP4C9.02","SPAPB2B4.01c","SPBC16G5.10","SPBC428.16c","SPBC776.08c","SPBC17A3.03c","SPAC17G6.04c","SPAC343.04c","SPAC26H5.08c","SPBC119.14","SPBC25D12.02c","SPBP4H10.12","SPBC418.01c","SPAC23A1.16c","SPAC6F12.08c","SPBC19G7.04","SPCC1281.05","SPBC29A3.04","SPBC902.03","SPAC3H5.12c","SPCC18.16c","SPCC663.09c","SPBC30D10.12c","SPAC1805.10","SPAP27G11.15","SPAC2F7.17","SPAC328.01c","SPCC970.08","SPCC320.07c","SPCPB1C11.03","SPAC4G8.09","SPACUNK4.07c","SPAC3H1.14","SPAC3G9.16c","SPAC25H1.07","SPBC16H5.10c","SPCC191.02c","SPAPB1A10.10c","SPCC1450.07c","SPCC132.01c","SPAC17G6.06","SPCC777.05","SPBC1604.06c","SPCC1223.03c","SPBC12D12.09","SPBC27B12.14","SPBC13G1.13","SPAC12G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BC3E7.01","SPAC3C7.06c","SPAC1687.09","SPAC11E3.07","SPBC887.07","SPAC1B1.04c","SPBC1826.01c","SPCC1919.12c","SPAC4G8.10","SPCC794.02","SPAC2F3.16","SPBC543.09","SPAC11D3.13","SPAC25B8.05","SPAC24B11.12c","SPBC8D2.12c","SPAC513.06c","SPCC16A11.07","SPCC1223.05c","SPAC1565.05","SPCC965.04c","SPCC23B6.02c","SPCC830.10","SPBC19C7.04c","SPAC630.06c","SPAC17G8.15","SPBC2F12.10","SPAC4H3.01","SPBC21.07c","SPAC513.03","SPAP27G11.02","SPAC19G12.10c","SPBC1652.01","SPAC4D7.13","SPAC22F8.05","SPBC1703.14c","SPCC1840.06","SPCC645.14c","SPCC364.02c","SPAC29E6.10c","SPBC1271.09","SPAC521.02","SPAC19A8.08","SPBC36B7.05c","SPCC1919.11","SPBC13A2.04c","SPBC354.05c","SPAC3A12.02","SPAC750.08c","SPAC1A6.04c","SPAC6F12.17","SPBC29A10.16c","SPCC24B10.05","SPAC1782.08c","SPBC29A3.08","SPBC16H5.14c","SPCC569.05c","SPBC244.02c","SPAC23A1.02c","SPBP35G2.09","SPAPB8E5.10","SPAC18G6.05c","SPBP23A10.15c","SPBC14F5.07","SPAC694.04c","SPAC8C9.08","SPBC800.04c","SPCC794.09c","SPBC839.13c","SPAC4D7.14","SPAC6G9.11","SPBC83.18c","SPBC12C2.13c","SPCC16A11.09c","SPAC328.09","SPBC1198.05","SPBC460.01c","SPAC25B8.13c","SPAC3G9.17","SPAC13A11.05","SPAC4H3.07c","SPAC644.05c","SPAC3A12.17c","SPAC23H4.01c","SPBP23A10.03c","SPBC19C2.10","SPAC144.11","SPBC839.12","SPAC23H4.15","SPAC6C3.02c","SPCC16C4.22","SPBC1685.16","SPAP8A3.10","SPBC577.04","SPAC1F5.10","SPAC1296.06","SPBC23E6.04c","SPAC57A10.09c","SPAC4F8.12c","SPCC553.08c","SPBC354.07c","SPBC56F2.04","SPCC1827.06c","SPAC323.02c","SPBC16H5.05c","SPSNRNA.05","SPBC29A3.13","SPBC3E7.09","SPAC1556.05c","SPBC3E7.08c","SPBPB2B2.01","SPAC767.01c","SPAPB8E5.04c","SPAC824.06","SPCC1281.02c","SPAP32A8.03c","SPAC637.05c","SPCC330.20","SPBC16E9.19","SPBC13E7.01","SPAC140.01","SPAC890.05","SPBC947.10","SPAC20G8.03","SPAC19G12.05","SPBC4F6.17c","SPBC16H5.08c","SPAC1805.12c","SPAC1F5.06","SPAC10F6.13c","SPAC23C11.17","SPCC338.12","SPAC589.06c","SPBC1348.09","SPAC6B12.11","SPBC17G9.07","SPBC1105.09","SPBC19C2.01","SPCC1494.06c","SPBC26H8.16","SPAC1D4.08","SPAC23D3.11","SPBC36.02c","SPAC13G6.04","SPBC115.01c","SPBC1604.05","SPBC30D10.11","SPBC29A10.15","SPBC543.08","SPCC777.04","SPAC17A5.03","SPBC8D2.01","SPBC1289.09","SPBC2D10.20","SPAC1527.03","SPBC83.09c","SPBC19C2.04c","SPAC26F1.09","SPAC9G1.10c","SPAC15A10.06","SPAC30D11.03","SPCC1672.09","SPBC215.06c","SPAC22F3.06c","SPAC10F6.08c","SPAC144.03","SPBC713.10","SPBC106.13","SPAC17C9.09c","SPBC31F10.07","SPAC23H3.12c","SPBC16A3.02c","SPAC3F10.08c","SPAC328.10c","SPBC23E6.01c","SPAC17A2.06c","SPBC1604.11","SPBC409.16c","SPAC222.03c","SPCC70.03c","SPBC9B6.03","SPAC1952.02","SPCC1322.14c","SPCC553.03","SPBC1604.09c","SPAC22G7.02","SPCC1906.04","SPBC428.04","SPBC19C2.09","SPBC13G1.04c","SPCC1020.02","SPCC18.04","SPBC1539.07c","SPAPB21F2.03","SPCC965.11c","SPBC29A10.13","SPAC22H10.05c","SPCC70.02c","SPBC31E1.06","SPAC823.17","SPBC651.01c","SPBC800.02","SPAC26A3.12c","SPAC9E9.11","SPBC1683.03c","SPAC1F7.02c","SPAC139.06","SPBC11G11.01","SPAC22E12.11c","SPCC4G3.13c","SPAC57A10.11c","SPAC1751.02c","SPAC29B12.07","SPAC22E12.17c","SPBC4.04c","SPCC1494.01","SPCC1183.08c","SPAC4F10.16c","SPBC23E6.02","SPCC1235.08c","SPAC30D11.01c","SPAC12G12.16c","SPBC17D11.08","SPAC3H8.05c","SPCC830.03","SPBC8E4.12c","SPCC757.05c","SPBP26C9.03c","SPBC19F5.02c","SPBC660.06","SPCC737.05","SPAC13G6.05c","SPBC27B12.09c","SPAC6F6.19","SPBC8D2.05c","SPAC23C11.03","SPBC13E7.11","SPAP8A3.11c","SPBC23E6.05","SPMIT.05","SPAP27G11.06c","SPAPB1E7.12","SPCC895.06","SPAC19B12.08","SPAC16C9.03","SPBC11G11.06c","SPAPB1A10.12c","SPBC3H7.09","SPBC25H2.09","SPBC14C8.03","SPAC17C9.14","SPAC1B1.02c","SPAC3H1.02c","SPAC19B12.09","SPBC1921.01c","SPAC1039.02","SPBC16G5.02c","SPBC28E12.04","SPAC15A10.09c","SPAC2C4.12c","SPAC1F3.04c","SPBP22H7.06","SPAC23A1.10","SPBC211.07c","SPAC1687.03c","SPACUNK4.16c","SPCC61.03","SPBC1289.05c","SPAC29A4.20","SPBC32H8.03","SPBC365.03c","SPAC20G4.01","SPBC3E7.14","SPAC13A11.06","SPAC823.16c","SPAC26H5.09c","SPAC664.11","SPAP14E8.02","SPBC1347.08c","SPBC4F6.10","SPAC8C9.05","SPAC1486.09","SPAC806.07","SPCC11E10.01","SPCC63.14","SPBC16A3.13","SPAC328.08c","SPAC821.13c","SPAC2G11.15c","SPAC1093.03","SPAC3H5.07","SPAC26A3.07c","SPAC14C4.16","SPCC14G10.04","SPAC30C2.02","SPAPB8E5.07c","SPAC12G12.02","SPAC27D7.07c","SPBP23A10.16","SPCC18.12c","SPBC31E1.01c","SPBC11B10.01","SPAC6B12.18","SPAC31A2.13c","SPAPB17E12.12c","SPBC1703.10","SPAC16C9.06c","SPAPB24D3.10c","SPAC10F6.12c","SPCC1020.09","SPAC8C9.07","SPBC17A3.06","SPBC354.14c","SPCC1183.02","SPAC6F12.16c","SPBC8D2.14c","SPAC17H9.03c","SPCC338.11c","SPBC26H8.05c","SPAC20H4.01","SPAC2C4.11c","SPBC16A3.17c","SPBC365.05c","SPAC5H10.08c","SPAC26A3.10","SPBC365.11","SPBC17G9.09","SPAC22E12.05c","SPAC10F6.17c","SPBC4B4.05","SPCC1682.08c","SPCC1620.12c","SPAC4A8.10","SPBC3B9.03","SPBC19G7.03c","SPAC3H8.03","SPBC1683.06c","SPAC1071.03c","SPBC1604.13c","SPAC977.08","SPCC1393.03","SPAC8C9.17c","SPBC115.03","SPCC970.11c"],"gene_count":2102,"ltp_gene_count":0},{"uniquename":"PMID:15060149","title":"Initiation of cytokinesis is controlled through multiple modes of regulation of the Sid2p-Mob1p kinase complex.","citation":"Mol Cell Biol 2004 Apr;24(8):3262-76","abstract":"The Sid2p-Mob1p kinase complex is an important component of the septation initiation network (SIN) in the fission yeast Schizosaccharomyces pombe. However, regulation of this complex is still elusive. Here we show that Mob1p is required not only for the subcellular localization of Sid2p but also for its kinase activity. We identified a region at the amino terminus of Sid2p that is required for Mob1p binding and spindle pole body (SPB) localization. Deletion of this region abolishes Mob1p binding and diminishes SPB localization, whereas this region alone is sufficient to associate with Mob1p and SPBs. We further show that a similar region of the N terminus of the Sid2p-related protein kinase Orb6p binds to the Mob1p-related protein Mob2p, suggesting that this may be a conserved mode of interaction for this family of kinases. Phosphorylation of Ser402 and especially Thr578 is important for Sid2p function. Sid2p with a mutation of Thr578 to Ala (T578A) can no longer rescue sid2-250 mutant cells, and this results in reduction of Mob1p binding. Sid2p mutants mimicking phosphorylation at this site (T578D and T578E) can rescue sid2-250 cells, enhance Sid2p kinase activity, and partially rescue growth defects of upstream sin mutants. Interestingly, Sid2p, but not Mob1p, is self-associated. Our experiments suggest that self-associated Sid2p is inactive. This self-association is mediated by a region that overlaps with Mob1p and SPB binding sites. Overexpression of Mob1p is able to disrupt the self-association of Sid2p. Taken together, our results suggest that Sid2p kinase may utilize multiple modes of regulation including self-association, Mob1p binding, and phosphorylation to achieve its full activity at an appropriate time and place in the cell.","authors":"Hou MC, Guertin DA, McCollum D","authors_abbrev":"Hou MC et al.","pubmed_publication_date":"Apr 2004","pubmed_entrez_date":"2004-04-03","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC428.13c","SPAC24B11.11c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:5328721","title":"Ribosome numbers in a fission yeast.","citation":"Nature 1965 Jul 17;207(994):322-3","abstract":"","authors":"Maclean N","authors_abbrev":"Maclean N","pubmed_publication_date":"17 Jul 1965","pubmed_entrez_date":"1965-07-17","publication_year":"1965","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9705504","title":"Schizosaccharomyces pombe Mcm3p, an essential nuclear protein, associates tightly with Nda4p (Mcm5p).","citation":"Nucleic Acids Res 1998 Sep 01;26(17):3955-60","abstract":"MCM proteins are required for the proper regulation of DNA replication. There are six MCM proteins in all eukaryotes which interact to form a large complex. We report the cloning of fission yeast mcm3 +. mcm3 + is essential and spores carrying a Delta mcm3 disruption arrest with an apparently replicated DNA content. The protein is found constitutively in the nucleus and levels remain constant throughout the cell cycle. Mcm3p binds particularly tightly to Nda4p (Mcm5p), but is loosely associated with the other Schizosaccharomyces pombe MCM proteins. Thus, Mcm3p is a peripheral MCM subunit.","authors":"Sherman DA, Forsburg SL","authors_abbrev":"Sherman DA et al.","pubmed_publication_date":"01 Sep 1998","pubmed_entrez_date":"1998-08-15","publication_year":"1998","canto_session_key":"9dca83e6946db798","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-06-10 11:30:16","canto_approved_date":"2021-04-16 13:29:30","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-08-17 10:46:23","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":3,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1682.02c","SPAC1B2.05"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-06-10"},{"uniquename":"PMID:19453973","title":"Two fission yeast rab7 homologs, ypt7 and ypt71, play antagonistic roles in the regulation of vacuolar morphology.","citation":"Traffic 2009 Jul;10(7):912-24","abstract":"Small guanine triphosphatases (GTPases) of the Rab family are key regulators of membrane trafficking events between the various subcellular compartments in eukaryotic cells. Rab7 is a conserved protein required in the late endocytic pathway and in lysosome biogenesis. A Schizosaccharomyces pombe (S. pombe) homolog of Rab7, Ypt7, is necessary for trafficking from the endosome to the vacuole and for homotypic vacuole fusion. Here, we identified and characterized a second fission yeast Rab7 homolog, Ypt71. Ypt71 is localized to the vacuolar membrane. Cells deleted for ypt71(+) exhibit normal growth rates and morphology. Interestingly, a ypt71 null mutant contains large vacuoles in contrast with the small fragmented vacuoles found in the ypt7 null mutant. Furthermore, the ypt71 mutation does not enhance or alleviate the temperature sensitivity or vacuole fusion defect of ypt7Delta cells. Like ypt7Delta cells, overexpression of ypt71(+) caused fragmentation of vacuoles and inhibits vacuole fusion under hypotonic conditions. Thus, the two S. pombe Rab7 homologs act antagonistically in regulating vacuolar morphology. Analysis of a chimeric Ypt7/Ypt71 protein showed that Rab7-directed vacuole dynamics, fusion versus fission, largely depends on the medial region of the protein, including a part of RabSF3/alpha3-L7.","doi":"10.1111/j.1600-0854.2009.00907.x","authors":"Kashiwazaki J, Iwaki T, Takegawa K, Shimoda C, Nakamura T","authors_abbrev":"Kashiwazaki J et al.","pubmed_publication_date":"Jul 2009","pubmed_entrez_date":"2009-05-21","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB1A10.10c","SPBC405.04c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11298744","title":"Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of alpha-glucosidase from Schizosaccharomyces pombe.","citation":"Eur J Biochem 2001 Apr;268(8):2270-80","abstract":"cDNA encoding Schizosaccharomyces pombe alpha-glucosidase was cloned from a library constructed from mRNA of the fission yeast, and expressed in Saccharomyces cerevisiae. The cDNA, 4176 bp in length, included a single ORF composed of 2910 bp encoding a polypeptide of 969 amino-acid residues with M(r) 106 138. The deduced amino-acid sequence showed a high homology to those of alpha-glucosidases from molds, plants and mammals. Therefore, the enzyme was categorized into the alpha-glucosidase family II. By site-directed mutagenesis, Asp481, Glu484 and Asp647 residues were confirmed to be essential in the catalytic reaction. The carboxyl group (-COOH) of the Asp647 residue was for the first time shown to be the most likely proton donor acting as the acid catalyst in the alpha-glucosidase of family II. Studies with the chemical modifier conduritol B epoxide suggested that the carboxylate group (-COO-) of the Asp481 residue was the catalytic nucleophile, although the role of the Glu484 residue remains obscure.","authors":"Okuyama M, Okuno A, Shimizu N, Mori H, Kimura A, Chiba S","authors_abbrev":"Okuyama M et al.","pubmed_publication_date":"Apr 2001","pubmed_entrez_date":"2001-04-12","publication_year":"2001","canto_session_key":"9829ae1d7c3785b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-11 19:03:04","canto_approved_date":"2024-06-13 19:19:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-11 19:02:55","canto_added_date":"2012-02-24 05:51:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB24D3.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-11"},{"uniquename":"PMID:9370332","title":"Phosphatidylglycerophosphate synthase from yeast.","citation":"Biochim Biophys Acta 1997 Sep 04;1348(1-2):187-91","abstract":"The phospholipid cardiolipin, or diphosphatidylglycerol, is ubiquitous in eucaryotes. It is unique in structure, subcellular localization, and potential function. Because it is found predominantly in the mitochondrial inner membrane, it is an excellent marker for mitochondrial biogenesis. Cardiolipin is required for activity of several mitochondrial enzymes and possibly also for import of proteins into the mitochondrion. To understand the role of cardiolipin in these cellular events, it is necessary to characterize the enzymes of the cardiolipin pathway, as well as the genes that control the expression of these enzymes. To date, the structural genes encoding the cardiolipin biosynthetic enzymes have not been identified in any eucaryotic organism. However, considerable information is available regarding the regulation of this pathway in yeast. The activity and regulation of the first enzyme of the pathway, CDP-diacylglycerol:sn-glycerol-3-phosphate 3-phosphatidyltransferase (phosphatidylglycerophosphate (PGP) synthase, EC 2.7.8.5), has been characterized in two evolutionarily divergent yeasts, Saccharomyces cerevisiae and Schizosaccharomyces pombe. In contrast to the second and third enzymes of the pathway, this enzyme is highly regulated, both by cross-pathway control and by factors affecting mitochondrial development. PGP synthase from S. pombe (and cardiolipin synthase from S. cerevisiae) have been purified to homogeneity. The amino acid sequences of these enzymes, combined with the availability of the complete genome sequence from S. cerevisiae will simplify the cloning of these genes in the near future.","authors":"Minskoff SA, Greenberg ML","authors_abbrev":"Minskoff SA et al.","pubmed_publication_date":"04 Sep 1997","pubmed_entrez_date":"1997-11-25","publication_year":"1997","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22174761","title":"Roles of the DYRK kinase Pom2 in cytokinesis, mitochondrial morphology, and sporulation in fission yeast.","citation":"PLoS One 2011;6(12):e28000","abstract":"Pom2 is predicted to be a dual-specificity tyrosine-phosphorylation regulated kinase (DYRK) related to Pom1 in Schizosaccharomyces pombe. DYRKs share a kinase domain capable of catalyzing autophosphorylation on tyrosine and exogenous phosphorylation on serine/threonine residues. Here we show that Pom2 is functionally different from the well-characterized Pom1, although they share 55% identity in the kinase domain and the Pom2 kinase domain functionally complements that of Pom1. Pom2 localizes to mitochondria throughout the cell cycle and to the contractile ring during late stages of cytokinesis. Overexpression but not deletion of pom2 results in severe defects in cytokinesis, indicating that Pom2 might share an overlapping function with other proteins in regulating cytokinesis. Gain and loss of function analyses reveal that Pom2 is required for maintaining mitochondrial morphology independently of microtubules. Intriguingly, most meiotic pom2Δ cells form aberrant asci with meiotic and/or forespore membrane formation defects. Taken together, Pom2 is a novel DYRK kinase involved in regulating cytokinesis, mitochondrial morphology, meiosis, and sporulation in fission yeast.","doi":"10.1371/journal.pone.0028000","authors":"Wu P, Zhao R, Ye Y, Wu JQ","authors_abbrev":"Wu P et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-12-17","publication_year":"2011","canto_session_key":"f122857006f86cc9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-09 11:55:06","canto_approved_date":"2020-01-22 22:22:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-01 09:51:19","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC825.03c","SPAC16C9.07","SPAC2F7.03c","SPBC800.05c","SPAC1786.03","SPAC926.03","SPAC24H6.05","SPBC12D12.01"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2017-11-09"},{"uniquename":"PMID:31147907","title":"Efficient Depletion of Fission Yeast Condensin by Combined Transcriptional Repression and Auxin-Induced Degradation.","citation":"Methods Mol Biol 2019;2004:25-33","abstract":"Structural maintenance of chromosomes (SMC) complexes play pivotal roles in controlling chromatin organization. Condensin is an essential SMC complex that compacts chromatin to form condensed chromosomes in mitosis. Complete condensin inactivation is necessary to reveal how condensin converts interphase chromatin into mitotic chromosomes. Here, we have developed a condensin depletion system in fission yeast that combines transcriptional repression with auxin-inducible protein degradation. This achieves efficient condensin depletion without need for a temperature shift. Our system is useful when studying how condensin contributes to chromosome architecture and is applicable to the study of other SMC complexes.","doi":"10.1007/978-1-4939-9520-2_3","authors":"Kakui Y, Uhlmann F","authors_abbrev":"Kakui Y et al.","pubmed_publication_date":"2019","pubmed_entrez_date":"2019-06-01","publication_year":"2019","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2019-06-01 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33877578","title":"Potential roles of condensin in genome organization and beyond in fission yeast.","citation":"J Microbiol 2021 May;59(5):449-459","abstract":"The genome is highly organized hierarchically by the function of structural maintenance of chromosomes (SMC) complex proteins such as condensin and cohesin from bacteria to humans. Although the roles of SMC complex proteins have been well characterized, their specialized roles in nuclear processes remain unclear. Condensin and cohesin have distinct binding sites and mediate long-range and short-range genomic associations, respectively, to form cell cycle-specific genome organization. Condensin can be recruited to highly expressed genes as well as dispersed repeat genetic elements, such as Pol III-transcribed genes, LTR retrotransposon, and rDNA repeat. In particular, mitotic transcription factors Ace2 and Ams2 recruit condensin to their target genes, forming centromeric clustering during mitosis. Condensin is potentially involved in various chromosomal processes such as the mobility of chromosomes, chromosome territories, DNA reannealing, and transcription factories. The current knowledge of condensin in fission yeast summarized in this review can help us understand how condensin mediates genome organization and participates in chromosomal processes in other organisms.","doi":"10.1007/s12275-021-1039-2","authors":"Kim KD","authors_abbrev":"Kim KD","pubmed_publication_date":"May 2021","pubmed_entrez_date":"2021-04-20","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-04-22 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"GO_REF:0000076","title":"Representation of transport or vesicle-mediated transport from cell component to cell component as biological process in the Gene Ontology","abstract":"We have created a standard template for classes describing the transport or vesicle-mediated transport from cellular component to cellular component as a biological process. The underlying equivalence axiom templates are \"GO:0006810 and 'has_target_start_location' some F and 'has_target_end_location' some T\" (transport) and \"GO:0016192 and 'has_target_start_location' some F and 'has_target_end_location' some T\" (vesicle-mediated transport), where F and T are a cellular components.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34829158","title":"An Integrative View of the Role of  Lachancea thermotolerans  in Wine Technology.","citation":"Foods 2021 Nov 21;10(11)","abstract":"The interest in  Lachancea thermotolerans , a yeast species with unusual characteristics, has notably increased in all ecological, evolutionary, and industrial aspects. One of the key characteristics of  L. thermotolerans  is the production of high quantities of lactic acid compared to other yeast species. Its evolution has mainly been driven by the influence of the environment and domestication, allowing several metabolic traits to arise. The molecular regulation of the fermentative process in  L. thermotolerans  shows interesting routes that play a complementary or protective role against fermentative stresses. One route that is activated under this condition is involved in the production of lactic acid, presenting a complete system for its production, showing the involvement of several enzymes and transporters. In winemaking, the use of  L. thermotolerans  is nowadays mostly focused in early-medium-maturity grape varieties, in which over-ripening can produce wines lacking acidity and with high concentrations of ethanol. Recent studies have reported new positive influences on quality apart from lactic acid acidification, such as improvements in color, glutathione production, aroma, malic acid, polysaccharides, or specific enzymatic activities that constitute interesting new criteria for selecting better strains. This positive influence on winemaking has increased the availability of commercial strains during recent years, allowing comparisons among some of those products. Initially, the management of  L. thermotolerans  was thought to be combined with  Saccaharomyces cerevisiae  to properly end alcoholic fermentation, but new studies are innovating and reporting combinations with other key enological microorganisms such as  Schizosaccharomyces pombe ,  Oenocous oeni ,  Lactiplantibacillus plantarum , or other non- Saccharomyces .","doi":"10.3390/foods10112878","authors":"Vicente J, Navascués E, Calderón F, Santos A, Marquina D, Benito S","authors_abbrev":"Vicente J et al.","pubmed_publication_date":"21 Nov 2021","pubmed_entrez_date":"2021-11-27","publication_year":"2021","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2021-11-29 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10954585","title":"Antizyme expression: a subversion of triplet decoding, which is remarkably conserved by evolution, is a sensor for an autoregulatory circuit.","citation":"Nucleic Acids Res 2000 Sep 01;28(17):3185-96","abstract":"The efficiency of programmed ribosomal frameshifting in decoding antizyme mRNA is the sensor for an autoregulatory circuit that controls cellular polyamine levels in organisms ranging from the yeast Schizosaccharomyces pombe to Drosophila to mammals. Comparison of the frameshift sites and flanking stimulatory signals in many organisms now permits a reconstruction of the likely evolutionary path of the remarkably conserved mRNA sequences involved in the frameshifting.","authors":"Ivanov IP, Gesteland RF, Atkins JF","authors_abbrev":"Ivanov IP et al.","pubmed_publication_date":"01 Sep 2000","pubmed_entrez_date":"2000-08-23","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11679064","title":"Accumulation of metal-binding peptides in fission yeast requires hmt2+.","citation":"Mol Microbiol 2001 Oct;42(1):29-36","abstract":"The fission yeast Schizosaccharomyces pombe detoxifies cadmium by synthesizing phytochelatins, peptides of the structure (gamma-GluCys)nGly, which bind cadmium and mediate its sequestration into the vacuole. The fission yeast protein HMT2, a mitochondrial enzyme that can oxidize sulphide, appears to be essential for tolerance to multiple forms of stress, including exposure to cadmium. We found that the hmt2- mutant is unable to accumulate normal levels of phytochelatins in response to cadmium, although the cells possess a phytochelatin synthase that is active in vitro. Radioactive pulse-chase experiments demonstrated that the defect lies in two steps: the synthesis of phytochelations and the upregulation of glutathione production. Phytochelatins, once formed, are stable. hmt2- cells accumulate high levels of sulphide and, when exposed to cadmium, display bright fluorescent bodies consistent with cadmium sulphide. We propose that the precipitation of free cadmium blocks phytochelatin synthesis in vivo, by preventing upregulation of glutathione production and formation of the cadmium-glutathione thiolate required as a substrate by phytochelatin synthase. Thus, although sulphide is required for phytochelatin-mediated metal tolerance, aberrantly high sulphide levels can inhibit this pathway. Precise regulation of sulphur metabolism, mediated in part by HMT2, is essential for metal tolerance in fission yeast.","authors":"Vande Weghe JG, Ow DW","authors_abbrev":"Vande Weghe JG et al.","pubmed_publication_date":"Oct 2001","pubmed_entrez_date":"2001-10-27","publication_year":"2001","canto_session_key":"9783fa1f671d65ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-21 13:14:54","canto_approved_date":"2026-01-12 16:06:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-20 08:50:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":11,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2G5.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-10-21"},{"uniquename":"PMID:40519184","title":"N-Terminus of Cid14 Activates RNA Unwinding by Mtr4 in the  Schizosaccharomyces pombe  TRAMP Complex.","citation":"Biochemistry 2025 Jun 16;","abstract":"The TRAMP ( Tr f4- A ir2- M tr4  p olyadenylation) complex is a multiprotein assembly that targets RNA substrates for processing or degradation by the nuclear exosome. In  Saccharomyces cerevisiae , the helicase activity of Mtr4 is enhanced by TRAMP assembly. Here we identify unexpected species-specific differences in the ability of Mtr4 to unwind a model RNA substrate. Unlike  S. cerevisiae  Mtr4,  Schizosaccharomyces pombe  Mtr4 retains RNA-stimulated ATPase activity, but is unable to unwind a model RNA substrate. This decoupling of ATPase and helicase activity is overcome by TRAMP formation. We further demonstrate that activation of helicase activity is accomplished by unique interactions with multiple regions of the intrinsically disordered N-terminus of the poly(A) polymerase, Cid14 (the  S. pombe  homologue of  S. cerevisiae  Trf4). Finally, we propose a model where Mtr4 adaptor complexes regulate unwinding activity by coordinating interdomain interactions within the helicase core.","doi":"10.1021/acs.biochem.5c00159","authors":"Gold MD, Staten MD, Morgan KE, Armah ENA, Johnson SJ","authors_abbrev":"Gold MD et al.","pubmed_publication_date":"16 Jun 2025","pubmed_entrez_date":"2025-06-16","publication_year":"2025","canto_session_key":"89deab7ebc7e7ed9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-06-16 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD100","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1996332","title":"Clustered tRNA genes in Schizosaccharomyces pombe centromeric DNA sequence repeats.","citation":"Proc Natl Acad Sci U S A 1991 Feb 15;88(4):1306-10","abstract":"The centromere-associated B' and B DNA sequence repeats of Schizosaccharomyces pombe chromosomes I and II have been found to contain clusters of tRNA genes. The centromere II region (cen2) includes at least 22 tRNA genes distributed among five copies of the B sequence repeat containing genes specifying tRNA(Ile), tRNA(Ala), and tRNA(Val). Individual B repeats are variously associated with other tRNA genes, including those specifying tRNA(Lys), tRNA(Arg), and tRNA(Glu2). The centromere I region (cen1) contains at least six tRNA genes in two copies of the B' repeated element, including genes specifying tRNA(Ile), tRNA(Ala), and tRNA(Glu3). Multiple tandemly arranged clusters of tRNA genes are presumably conserved due to restricted recombination frequencies in the centromere regions.","authors":"Kuhn RM, Clarke L, Carbon J","authors_abbrev":"Kuhn RM et al.","pubmed_publication_date":"15 Feb 1991","pubmed_entrez_date":"1991-02-15","publication_year":"1991","canto_session_key":"2840fcfd9050bf89","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-07 22:10:55","canto_approved_date":"2019-01-07 22:10:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-07 22:10:48","canto_added_date":"2012-02-24 05:55:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2019-01-07"},{"uniquename":"GO_REF:0000058","title":"Representation of regulation in the Gene Ontology (biological process) ","abstract":"We have created a standard template for the definition of classes for the regulation of a biological process. This includes the definitions for positive and negative regulation. The equivalence axiom templates are \"GO:0065007 and 'regulates' some X\" (regulation), \"GO:0065007 and 'negatively_regulates' some X\" (negative regulation), and \"GO:0065007 and 'positively_regulates' some X\" (positive regulation), where X is a biological process.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010390","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30733442","title":"The Elongator subunit Elp3 is a non-canonical tRNA acetyltransferase.","citation":"Nat Commun 2019 Feb 07;10(1):625","abstract":"The Elongator complex catalyzes posttranscriptional tRNA modifications by attaching carboxy-methyl (cm 5 ) moieties to uridine bases located in the wobble position. The catalytic subunit Elp3 is highly conserved and harbors two individual subdomains, a radical S-adenosyl methionine (rSAM) and a lysine acetyltransferase (KAT) domain. The details of its modification reaction cycle and particularly the substrate specificity of its KAT domain remain elusive. Here, we present the co-crystal structure of bacterial Elp3 (DmcElp3) bound to an acetyl-CoA analog and compare it to the structure of a monomeric archaeal Elp3 from Methanocaldococcus infernus (MinElp3). Furthermore, we identify crucial active site residues, confirm the importance of the extended N-terminus for substrate recognition and uncover the specific induction of acetyl-CoA hydrolysis by different tRNA species. In summary, our results establish the clinically relevant Elongator subunit as a non-canonical acetyltransferase and genuine tRNA modification enzyme.","doi":"10.1038/s41467-019-08579-2","authors":"Lin TY, Abbassi NEH, Zakrzewski K, Chramiec-Głąbik A, Jemioła-Rzemińska M, Różycki J, Glatt S","authors_abbrev":"Lin TY et al.","pubmed_publication_date":"07 Feb 2019","pubmed_entrez_date":"2019-02-09","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24866464","title":"Mitochondrial protein translocases for survival and wellbeing.","citation":"FEBS Lett 2014 Aug 01;588(15):2484-95","abstract":"Mitochondria are involved in many essential cellular activities. These broad functions explicate the need for the well-orchestrated biogenesis of mitochondrial proteins to avoid death and pathological consequences, both in unicellular and more complex organisms. Yeast as a model organism has been pivotal in identifying components and mechanisms that drive the transport and sorting of nuclear-encoded mitochondrial proteins. The machinery components that are involved in the import of mitochondrial proteins are generally evolutionarily conserved within the eukaryotic kingdom. However, topological and functional differences have been observed. We review the similarities and differences in mitochondrial translocases from yeast to human. Additionally, we provide a systematic overview of the contribution of mitochondrial import machineries to human pathologies, including cancer, mitochondrial diseases, and neurodegeneration.","doi":"10.1016/j.febslet.2014.05.028","authors":"Sokol AM, Sztolsztener ME, Wasilewski M, Heinz E, Chacinska A","authors_abbrev":"Sokol AM et al.","pubmed_publication_date":"01 Aug 2014","pubmed_entrez_date":"2014-05-29","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22484924","title":"CUE domain-containing protein Vps901 is required for vacuolar protein transport in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2012;76(4):652-9","abstract":"The functions of two Schizosaccharomyces pombe Vps9-like genes, SPBC4F6.10/vps901(+) and SPBC29A10.11c/vps902(+), were characterized. Genomic sequence analysis predicted that Vps901p contains a VPS9 domain, whereas cDNA analyses revealed that Vps901p contains a CUE domain (coupling of ubiquitin to ER degradation) in its C-terminal region. Deletion of vps901(+) resulted in mis-sorting and secretion of S. pombe vacuolar carboxypeptidase Cpy1p, whereas deletion of vps902(+) had no effect, suggesting that only Vps901p functions in vacuolar protein transport in S. pombe. Deletion of vps901(+) further produced pleiotropic phenotypes, including vacuolar homotypic fusion and endocytosis defects. Heterologous expression of the budding yeast VPS9 gene corrected the CPY mis-sorting defect in vps901Δ cells. These findings suggest that the VPS9 domain of Vps901p is required for vacuolar protein trafficking in S. pombe.","authors":"Nakase M, Tsukamoto Y, Hosomi A, Matsuda T, Miyamoto M, Takegawa K","authors_abbrev":"Nakase M et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-04-10","publication_year":"2012","canto_session_key":"92800aaf61c226d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kaoru Takegawa","canto_first_approved_date":"2017-11-21 16:17:30","canto_approved_date":"2026-05-27 03:13:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-05 06:05:50","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Kaoru Takegawa","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16C6.06","SPCPJ732.01","SPAC10F6.13c","SPBC29A10.11c","SPBC4F6.10","SPAC6G9.11","SPBC359.03c","SPAC24C9.08"],"gene_count":8,"ltp_gene_count":3,"approved_date":"2017-11-21"},{"uniquename":"PMID:19329575","title":"Epigenetic inheritance and reprogramming in plants and fission yeast.","citation":"Cold Spring Harb Symp Quant Biol 2008;73:265-71","abstract":"Plants and fission yeast exhibit a wealth of epigenetic phenomena, including transposon regulation, heterochromatic silencing, and gene imprinting. They provide excellent model organisms to address the question of how epigenetic information is propagated to daughter cells. We have addressed the questions of establishment, maintenance, and inheritance of heterochromatic silencing using the fission yeast Schizosaccharomyces pombe and the plant Arabidopsis thaliana by using a variety of genetic and genomic approaches. We present here results showing the cell cycle dependence of RNA in fission yeast RNA interference (RNAi), which is required for proper transcriptional silencing of the centromeric heterochromatin, and that this process occurs during S phase, allowing for precise copying and reestablishment of heterochromatic histone modifications following DNA replication and cell division. We also show that in plants, cells in culture and male germ-line cells undergo massive epigenomic changes correlated with the appearance of a novel class of 21-nucleotide small interfering RNA (siRNA) from transcriptionally reactivated transposable elements (TEs) following loss of heterochromatic DNA and histone methylation. We propose a model for the role of deliberate TE reactivation in germ-line companion cells as part of a developmental mechanism for first revealing and then silencing TEs via small RNA, which may contribute to reprogramming during early development in plants and animals.","doi":"10.1101/sqb.2008.73.062","authors":"Martienssen RA, Kloc A, Slotkin RK, Tanurdzić M","authors_abbrev":"Martienssen RA et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2009-03-31","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23857276","title":"Crystal structure of the yeast TSC1 core domain and implications for tuberous sclerosis pathological mutations.","citation":"Nat Commun 2013;4:2135","abstract":"Tuberous sclerosis complex is a disease caused by mutations in two tumor-suppressor genes, TSC1 and TSC2. The TSC1 protein, also known as hamartin, has a critical role in controlling mTOR signalling. TSC1 does not bear apparent sequence homology with other proteins. Here we show that the N-terminal half of yeast TSC1 forms a protease-resistant domain, which is evolutionarily conserved. The crystal structure of this yeast TSC1 core domain shows that it contains a pseudo-HEAT repeat fold with its C-terminal end capped by a helical subdomain. This allows us to model the three-dimensional structure of the human TSC1 N-terminal domain (TSC1-NTD), which anchors essentially all pathogenic TSC1 missense mutations found in tuberous sclerosis patients. Interestingly, most pathogenic mutations map inside of the folded TSC1-NTD structure, whereas most non-pathogenic variants are on the structural surface. This indicates that the disruption of the TSC1-NTD globular structure is a major cause of tuberous sclerosis.","doi":"10.1038/ncomms3135","authors":"Sun W, Zhu YJ, Wang Z, Zhong Q, Gao F, Lou J, Gong W, Xu W","authors_abbrev":"Sun W et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-17","publication_year":"2013","canto_session_key":"3d058f907631e762","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-02-17 18:27:45","canto_approved_date":"2023-02-17 18:27:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-17 18:27:37","canto_added_date":"2014-02-16 05:46:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F3.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-17","pdb_entries":[{"pdb_id":"4kk0","gene_chains":[{"gene_uniquename":"SPAC22F3.13","chain":"A/B/C/D/E/F/G/H/I/J","position":"1-431"}],"title":"Crystal Structure of TSC1 core domain from S. pombe","entry_authors":"Sun W,Zhu Y,Wang ZZ,Zhong Q,Gao F,Lou JZ,Gong WM,Xu WQ","entry_authors_abbrev":"Sun W et al.","reference_uniquename":"PMID:23857276","experimental_method":"X-ray","resolution":"2.9"},{"pdb_id":"4kk1","gene_chains":[{"gene_uniquename":"SPAC22F3.13","chain":"A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T","position":"1-431"}],"title":"Crystal Structure of TSC1 core domain from S. pombe","entry_authors":"Sun W,Zhu Y,Wang ZZ,Zhong Q,Gao F,Lou JZ,Gong WM,Xu WQ","entry_authors_abbrev":"Sun W et al.","reference_uniquename":"PMID:23857276","experimental_method":"X-ray","resolution":"3.3"}]},{"uniquename":"PMID:28335716","title":"Human MFAP1 is a cryptic ortholog of the Saccharomyces cerevisiae Spp381 splicing factor.","citation":"BMC Evol Biol 2017 Mar 24;17(1):91","abstract":"Pre-mRNA splicing involves the stepwise assembly of a pre-catalytic spliceosome, followed by its catalytic activation, splicing catalysis and disassembly. Formation of the pre-catalytic spliceosomal B complex involves the incorporation of the U4/U6.U5 tri-snRNP and of a group of non-snRNP B-specific proteins. While in Saccharomyces cerevisiae the Prp38 and Snu23 proteins are recruited as components of the tri-snRNP, metazoan orthologs of Prp38 and Snu23 associate independently of the tri-snRNP as members of the B-specific proteins. The human spliceosome contains about 80 proteins that lack obvious orthologs in yeast, including most of the B-specific proteins apart from Prp38 and Snu23. Conversely, the tri-snRNP protein Spp381 is one of only five S. cerevisiae splicing factors without a known human ortholog.\nUsing InParanoid, a state-of-the-art method for ortholog inference between pairs of species, and systematic BLAST searches we identified the human B-specific protein MFAP1 as a putative ortholog of the S. cerevisiae tri-snRNP protein Spp381. Bioinformatics revealed that MFAP1 and Spp381 share characteristic structural features, including intrinsic disorder, an elongated shape, solvent exposure of most residues and a trend to adopt α-helical structures. In vitro binding studies showed that human MFAP1 and yeast Spp381 bind their respective Prp38 proteins via equivalent interfaces and that they cross-interact with the Prp38 proteins of the respective other species. Furthermore, MFAP1 and Spp381 both form higher-order complexes that additionally include Snu23, suggesting that they are parts of equivalent spliceosomal sub-complexes. Finally, similar to yeast Spp381, human MFAP1 partially rescued a growth defect of the temperature-sensitive mutant yeast strain prp38-1.\nHuman B-specific protein MFAP1 structurally and functionally resembles the yeast tri-snRNP-specific protein Spp381 and thus qualifies as its so far missing ortholog. Our study indicates that the yeast Snu23-Prp38-Spp381 triple complex was evolutionarily reprogrammed from a tri-snRNP-specific module in yeast to the B-specific Snu23-Prp38-MFAP1 module in metazoa, affording higher flexibility in spliceosome assembly and thus, presumably, in splicing regulation.","doi":"10.1186/s12862-017-0923-1","authors":"Ulrich AK, Wahl MC","authors_abbrev":"Ulrich AK et al.","pubmed_publication_date":"24 Mar 2017","pubmed_entrez_date":"2017-03-25","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["YBR152W","SPAC1782.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10631515","title":"A small-molecule catalyst of protein folding in vitro and in vivo.","citation":"Chem Biol 1999 Dec;6(12):871-9","abstract":"The formation of native disulfide bonds between cysteine residues often limits the rate and yield of protein folding. The enzyme protein disulfide isomerase (PDI) catalyzes the interchange of disulfide bonds in substrate proteins. The two -Cys-Gly-His-Cys- active sites of PDI provide a thiol that has a low pKa value and a disulfide bond of high reduction potential (Eo').\nA synthetic small-molecule dithiol, (+/-)-trans-1,2-bis(2-mercaptoacetamido)cyclohexane (BMC), has a pKa value of 8.3 and an Eo' value of -0.24 V. These values are similar to those of the PDI active sites. BMC catalyzes the activation of scrambled ribonuclease A, an inactive enzyme with non-native disulfide bonds, and doubles the yield of active enzyme. A monothiol analog of BMC, N-methylmercaptoacetamide, is a less efficient catalyst than BMC. BMC in the growth medium of Saccharomyces cerevisiae cells increases by > threefold the heterologous secretion of Schizosaccharomyces pombe acid phosphatase, which has eight disulfide bonds. This effect is similar to that from the overproduction of PDI in the S. cerevisiae cells, indicating that BMC, like PDI, can catalyze protein folding in vivo.\nA small-molecule dithiol with a low thiol pKa value and high disulfide Eo' value can mimic PDI by catalyzing the formation of native disulfide bonds in proteins, both in vitro and in vivo.","authors":"Woycechowsky KJ, Wittrup KD, Raines RT","authors_abbrev":"Woycechowsky KJ et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"2000-01-13","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17072887","title":"Growth arrest and chromosome instability in aneuploid yeast.","citation":"Yeast 2006 Oct 15;23(13):937-50","abstract":"Aneuploid generation and stability are biologically important. In the present study, we investigated fission yeast aneuploids, focusing on the process through which aneuploidy is resolved into stable euploidy. The viability and growth patterns of aneuploid spores were greatly influenced by culture conditions, including nutrition and temperature. Germ tube formation and DNA synthesis in a major portion of aneuploids were greatly delayed or arrested. Observation of individual spores and their growth profiles revealed that a certain type(s) of aneuploid resolved its aneuploidy into normal euploids through anomalous cell divisions, which in many cases produced dead cells. Another type of aneuploid, disomy of chromosome 3, the only maintainable aneuploid between n and 2n, showed a peculiar cell division arrest phenotype under a certain growth condition. Microcolonies that formed from this type of aneuploid often contained a population of cells that became incompetent for cell division. This cell division arrest was not due to a nutritional limitation. During this peculiar process of colony formation, stable haploids or diploids were frequently produced. All other types of aneuploids are usually inviable, at least under our experimental conditions. To examine the aneuploid issue more systematically, we constructed a system to select for disomy of chromosome 1 or 2 using intragenic complementation of ade6-M210 and -M216 alleles. This genetic selection system revealed that fission yeast aneuploids can be stabilized through structural chromosome changes, including partial duplication and circular mini-chromosomes.","authors":"Niwa O, Tange Y, Kurabayashi A","authors_abbrev":"Niwa O et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24838944","title":"Dma1-dependent degradation of SIN proteins during meiosis in Schizosaccharomyces pombe.","citation":"J Cell Sci 2014 Jul 15;127(Pt 14):3149-61","abstract":"The Schizosaccharomyces pombe septation initiation network (SIN) is required for cytokinesis during vegetative growth and for spore formation during meiosis. Regulation of the SIN during mitosis has been studied extensively, but less is known about its meiotic regulation. Here, we show that several aspects of SIN regulation differ between mitosis and meiosis. First, the presence of GTP-bound Spg1p is not the main determinant of the timing of Cdc7p and Sid1p association with the spindle pole body (SPB) during meiosis. Second, the localisation dependencies of SIN proteins differ from those in mitotic cells, suggesting a modified functional organisation of the SIN during meiosis. Third, there is stage-specific degradation of SIN components in meiosis; Byr4p is degraded after meiosis I, whereas the degradation of Cdc7p, Cdc11p and Sid4p occurs after the second meiotic division and depends upon the ubiquitin ligase Dma1p. Finally, Dma1p-dependent degradation is not restricted to the SIN, as we show that Dma1p is needed for the degradation of Mcp6p (also known as Hrs1p) during meiosis I. Taken together, these data suggest that stage-specific targeted proteolysis plays an important role in regulating meiotic progression.","doi":"10.1242/jcs.148585","authors":"Krapp A, Simanis V","authors_abbrev":"Krapp A et al.","pubmed_publication_date":"15 Jul 2014","pubmed_entrez_date":"2014-05-20","publication_year":"2014","canto_session_key":"f1cc03a9de929ac1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-04-22 11:05:51","canto_approved_date":"2025-04-22 11:05:51","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2025-04-22 11:03:02","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":32,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPAC9G1.09","SPBC582.06c","SPAC1F3.06c","SPBC244.01c","SPAC222.10c","SPAC1565.06c","SPAC6F6.08c","SPCC1739.11c","SPAC17G8.10c","SPBC1347.03"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2025-04-22"},{"uniquename":"PMID:35173235","title":"Prediction of serine phosphorylation sites mapping on Schizosaccharomyces Pombe by fusing three encoding schemes with the random forest classifier.","citation":"Sci Rep 2022 Feb 16;12(1):2632","abstract":"Serine phosphorylation is one type of protein post-translational modifications (PTMs), which plays an essential role in various cellular processes and disease pathogenesis. Numerous methods are used for the prediction of phosphorylation sites. However, the traditional wet-lab based experimental approaches are time-consuming, laborious, and expensive. In this work, a computational predictor was proposed to predict serine phosphorylation sites mapping on Schizosaccharomyces pombe (SP) by the fusion of three encoding schemes namely k-spaced amino acid pair composition (CKSAAP), binary and amino acid composition (AAC) with the random forest (RF) classifier. So far, the proposed method is firstly developed to predict serine phosphorylation sites for SP. Both the training and independent test performance scores were used to investigate the success of the proposed RF based fusion prediction model compared to others. We also investigated their performances by 5-fold cross-validation (CV). In all cases, it was observed that the recommended predictor achieves the largest scores of true positive rate (TPR), true negative rate (TNR), accuracy (ACC), Mathew coefficient of correlation (MCC), Area under the ROC curve (AUC) and pAUC (partial AUC) at false positive rate (FPR) = 0.20. Thus, the prediction performance as discussed in this paper indicates that the proposed approach may be a beneficial and motivating computational resource for predicting serine phosphorylation sites in the case of Fungi. The online interface of the software for the proposed prediction model is publicly available at http://mollah-bioinformaticslab-stat.ru.ac.bd/PredSPS/ .","doi":"10.1038/s41598-022-06529-5","authors":"Tasmia SA, Kibria MK, Tuly KF, Islam MA, Khatun MS, Hasan MM, Mollah MNH","authors_abbrev":"Tasmia SA et al.","pubmed_publication_date":"16 Feb 2022","pubmed_entrez_date":"2022-02-17","publication_year":"2022","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2022-02-20 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35733025","title":"Investigating Mitotic Inheritance of Histone Modifications Using Tethering Strategies.","citation":"Methods Mol Biol 2022;2529:419-440","abstract":"The covalent and reversible modification of histones enables cells to establish heritable gene expression patterns without altering their genetic blueprint. Epigenetic mechanisms regulate gene expression in two separate ways: (1) establishment, which depends on sequence-specific DNA- or RNA-binding proteins that recruit histone-modifying enzymes to unique genomic loci, and (2) maintenance, which is sequence-independent and depends on the autonomous propagation of preexisting chromatin states during DNA replication. Only a subset of the vast repertoire of histone modifications in the genome is heritable. Here, we describe a synthetic biology approach to tether histone-modifying enzymes to engineer chromatin states in living cells and evaluate their potential for mitotic inheritance. In S. pombe, fusing the H3K9 methyltransferase, Clr4, to the tetracycline-inducible TetR DNA-binding domain facilitates rapid and reversible control of heterochromatin assembly. We describe a framework to successfully implement an inducible heterochromatin establishment system and evaluate its molecular properties. We anticipate that our innovative genetic strategy will be broadly applicable to the discovery of protein complexes and separation-of-function alleles of heterochromatin-associated factors with unique roles in epigenetic inheritance.","doi":"10.1007/978-1-0716-2481-4_18","authors":"Larkin A, Ames A, Seman M, Ragunathan K","authors_abbrev":"Larkin A et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-06-22","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-06-25 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31345994","title":"Histone H2B Ubiquitylation Regulates Histone Gene Expression by Suppressing Antisense Transcription in Fission Yeast.","citation":"Genetics 2019 Sep;213(1):161-172","abstract":"Histone H2B monoubiquitylation (H2Bub1) is tightly linked to RNA polymerase II transcription elongation, and is also directly implicated in DNA replication and repair. Loss of H2Bub1 is associated with defects in cell cycle progression, but how these are related to its various functions, and the underlying mechanisms involved, is not understood. Here we describe a role for H2Bub1 in the regulation of replication-dependent histone genes in the fission yeast  Schizosaccharomyces pombe  H2Bub1 activates histone genes indirectly by suppressing antisense transcription of  ams2 +   -a gene encoding a GATA-type transcription factor that activates histone genes and is required for assembly of centromeric chromatin. Mutants lacking the ubiquitylation site in H2B or the H2B-specific E3 ubiquitin ligase Brl2 had elevated levels of  ams2 +   antisense transcripts and reduced Ams2 protein levels. These defects were reversed upon inhibition of Cdk9-an ortholog of the kinase component of positive transcription elongation factor b (P-TEFb)-indicating that they likely resulted from aberrant transcription elongation. Reduced Cdk9 activity also partially rescued chromosome segregation phenotypes of H2Bub1 mutants. In a genome-wide analysis, loss of H2Bub1 led to increased antisense transcripts at over 500 protein-coding genes in H2Bub1 mutants; for a subset of these, including several genes involved in chromosome segregation and chromatin assembly, antisense derepression was Cdk9-dependent. Our results highlight antisense suppression as a key feature of cell cycle-dependent gene regulation by H2Bub1, and suggest that aberrant transcription elongation may underlie the effects of H2Bub1 loss on cell cycle progression.","doi":"10.1534/genetics.119.302499","authors":"Pagé V, Chen JJ, Durand-Dubief M, Grabowski D, Oya E, Sansô M, Martin RD, Hébert TE, Fisher RP, Ekwall K, Tanny JC","authors_abbrev":"Pagé V et al.","pubmed_publication_date":"Sep 2019","pubmed_entrez_date":"2019-07-27","publication_year":"2019","canto_session_key":"80bab75459a4ce45","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-07-29 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32H8.10"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:41518600","title":"PomBase in 2026: Expanding Knowledge, Modelling Connections.","citation":"Genetics 2026 Jan 10;","abstract":"PomBase is the model organism database dedicated to the fission yeast Schizosaccharomyces pombe. In this update, we outline recent progress in literature curation, the introduction of new tools, and enhancements designed to better support the research community. We highlight our recent effort to curate biological pathways and modules as causal networks using Gene Ontology - Causal Activity Modelling (GO-CAM) and describe new features that utilize these models to guide and inform hypothesis-driven research.","doi":"10.1093/genetics/iyag001","authors":"Carme P, Rutherford K, Bähler J, Mata J, Wood V","authors_abbrev":"Carme P et al.","pubmed_publication_date":"10 Jan 2026","pubmed_entrez_date":"2026-01-10","publication_year":"2026","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2026-01-12 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25847133","title":"RNA pol II transcript abundance controls condensin accumulation at mitotically up-regulated and heat-shock-inducible genes in fission yeast.","citation":"Genes Cells 2015 Jun;20(6):481-99","abstract":"Condensin plays fundamental roles in chromosome dynamics. In this study, we determined the binding sites of condensin on fission yeast (Schizosaccharomyces pombe) chromosomes at the level of nucleotide sequences using chromatin immunoprecipitation (ChIP) and ChIP sequencing (ChIP-seq). We found that condensin binds to RNA polymerase I-, II- and III-transcribed genes during both mitosis and interphase, and we focused on pol II constitutive and inducible genes. Accumulation sites for condensin are distinct from those of cohesin and DNA topoisomerase II. Using cell cycle stage and heat-shock-inducible genes, we show that pol II-mediated transcripts cause condensin accumulation. First, condensin's enrichment on mitotically activated genes was abolished by deleting the sep1(+) gene that encodes an M-phase-specific forkhead transcription factor. Second, by raising the temperature, condensin accumulation was rapidly induced at heat-shock protein genes in interphase and even during mid-mitosis. In interphase, condensin accumulates preferentially during the postreplicative phase. Pol II-mediated transcription was neither repressed nor activated by condensin, as levels of transcripts per se did not change when mutant condensin failed to associate with chromosomal DNA. However, massive chromosome missegregation occurred, suggesting that abundant pol II transcription may require active condensin before proper chromosome segregation.","doi":"10.1111/gtc.12239","authors":"Nakazawa N, Sajiki K, Xu X, Villar-Briones A, Arakawa O, Yanagida M","authors_abbrev":"Nakazawa N et al.","pubmed_publication_date":"Jun 2015","pubmed_entrez_date":"2015-04-08","publication_year":"2015","canto_session_key":"0e65902eb994aa19","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Norihiko Nakazawa","canto_approved_date":"2015-10-20 02:19:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-08-28 10:34:18","canto_added_date":"2015-04-09 00:18:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Norihiko Nakazawa","community_curator":true,"annotation_count":5,"orcid":"0000-0001-8386-0812","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC776.13","SPBC1105.05","SPAC19B12.02c","SPCC338.17c","SPAC821.08c","SPAC926.04c","SPBC1A4.03c","SPAC13G7.02c","SPBC4C3.12","SPBP4H10.06c","SPAC1705.03c"],"gene_count":11,"ltp_gene_count":5,"approved_date":"2015-08-28"},{"uniquename":"PMID:28733414","title":"Live Cell Imaging in Fission Yeast.","citation":"Cold Spring Harb Protoc 2017 Oct 03;2017(10):pdb.top090621","abstract":"Live cell imaging complements the array of biochemical and molecular genetic approaches to provide a comprehensive insight into functional dependencies and molecular interactions in fission yeast. Fluorescent proteins and vital dyes reveal dynamic changes in the spatial distribution of organelles and the proteome and how each alters in response to changes in environmental and genetic composition. This introduction discusses key issues and basic image analysis for live cell imaging of fission yeast.","doi":"10.1101/pdb.top090621","authors":"Mulvihill DP","authors_abbrev":"Mulvihill DP","pubmed_publication_date":"03 Oct 2017","pubmed_entrez_date":"2017-07-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17072894","title":"The fission yeast spindle orientation checkpoint: a model that generates tension?","citation":"Yeast 2006 Oct 15;23(13):1015-29","abstract":"In all eukaryotes, the alignment of the mitotic spindle with the axis of cell polarity is essential for accurate chromosome segregation as well as for the establishment of cell fate, and thus morphogenesis, during development. Studies in invertebrates, higher eukaryotes and yeast suggest that astral microtubules interact with the cell cortex to position the spindle. These microtubules are thought to impose pushing or pulling forces on the spindle poles to affect the rotation or movement of the spindle. In the fission yeast model, where cell division is symmetrical, spindle rotation is dependent on the interaction of astral microtubules with the cortical actin cytoskeleton. In these cells, a bub1-dependent mitotic checkpoint, the spindle orientation checkpoint (SOC), is activated when the spindles fail to align with the cell polarity axis. In this paper we review the mechanism that orientates the spindle during mitosis in fission yeast, and discuss the consequences of misorientation on metaphase progression.","authors":"Gachet Y, Reyes C, Goldstone S, Tournier S","authors_abbrev":"Gachet Y et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26729303","title":"A diffusion model for the coordination of DNA replication in Schizosaccharomyces pombe.","citation":"Sci Rep 2016 Jan 05;6:18757","abstract":"The locations of proteins and epigenetic marks on the chromosomal DNA sequence are believed to demarcate the eukaryotic genome into distinct structural and functional domains that contribute to gene regulation and genome organization. However, how these proteins and epigenetic marks are organized in three dimensions remains unknown. Recent advances in proximity-ligation methodologies and high resolution microscopy have begun to expand our understanding of these spatial relationships. Here we use polymer models to examine the spatial organization of epigenetic marks, euchromatin and heterochromatin, and origins of replication within the Schizosaccharomyces pombe genome. These models incorporate data from microscopy and proximity-ligation experiments that inform on the positions of certain elements and contacts within and between chromosomes. Our results show a striking degree of compartmentalization of epigenetic and genomic features and lead to the proposal of a diffusion based mechanism, centred on the spindle pole body, for the coordination of DNA replication in S. pombe.","doi":"10.1038/srep18757","authors":"Pichugina T, Sugawara T, Kaykov A, Schierding W, Masuda K, Uewaki J, Grand RS, Allison JR, Martienssen RA, Nurse P, Ueno M, O'Sullivan JM","authors_abbrev":"Pichugina T et al.","pubmed_publication_date":"05 Jan 2016","pubmed_entrez_date":"2016-01-06","publication_year":"2016","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2016-01-07 01:19:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6628191","title":"[Replicating instability and ploidy of Schizosaccharomyces pombe].","citation":"Dokl Akad Nauk SSSR 1983;271(4):980-4","abstract":"","authors":"Kurennaia ON, Devin AB","authors_abbrev":"Kurennaia ON et al.","pubmed_publication_date":"1983","pubmed_entrez_date":"1983-01-01","publication_year":"1983","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27466282","title":"The Cell Biology of Fission Yeast Septation.","citation":"Microbiol Mol Biol Rev 2016 Sep;80(3):779-91","abstract":"In animal cells, cytokinesis requires the formation of a cleavage furrow that divides the cell into two daughter cells. Furrow formation is achieved by constriction of an actomyosin ring that invaginates the plasma membrane. However, fungal cells contain a rigid extracellular cell wall surrounding the plasma membrane; thus, fungal cytokinesis also requires the formation of a special septum wall structure between the dividing cells. The septum biosynthesis must be strictly coordinated with the deposition of new plasma membrane material and actomyosin ring closure and must occur in such a way that no breach in the cell wall occurs at any time. Because of the high turgor pressure in the fungal cell, even a minor local defect might lead to cell lysis and death. Here we review our knowledge of the septum structure in the fission yeast Schizosaccharomyces pombe and of the recent advances in our understanding of the relationship between septum biosynthesis and actomyosin ring constriction and how the two collaborate to build a cross-walled septum able to support the high turgor pressure of the cell. In addition, we discuss the importance of the septum biosynthesis for the steady ingression of the cleavage furrow.","doi":"10.1128/MMBR.00013-16","authors":"García Cortés JC, Ramos M, Osumi M, Pérez P, Ribas JC","authors_abbrev":"García Cortés JC et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-07-29","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-07-30 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19911044","title":"Ctp1 and the MRN-complex are required for endonucleolytic Rec12 removal with release of a single class of oligonucleotides in fission yeast.","citation":"PLoS Genet 2009 Nov;5(11):e1000722","abstract":"DNA double-strand breaks (DSBs) are formed during meiosis by the action of the topoisomerase-like Spo11/Rec12 protein, which remains covalently bound to the 5' ends of the broken DNA. Spo11/Rec12 removal is required for resection and initiation of strand invasion for DSB repair. It was previously shown that budding yeast Spo11, the homolog of fission yeast Rec12, is removed from DNA by endonucleolytic cleavage. The release of two Spo11 bound oligonucleotide classes, heterogeneous in length, led to the conjecture of asymmetric cleavage. In fission yeast, we found only one class of oligonucleotides bound to Rec12 ranging in length from 17 to 27 nucleotides. Ctp1, Rad50, and the nuclease activity of Rad32, the fission yeast homolog of Mre11, are required for endonucleolytic Rec12 removal. Further, we detected no Rec12 removal in a rad50S mutant. However, strains with additional loss of components localizing to the linear elements, Hop1 or Mek1, showed some Rec12 removal, a restoration depending on Ctp1 and Rad32 nuclease activity. But, deletion of hop1 or mek1 did not suppress the phenotypes of ctp1Delta and the nuclease dead mutant (rad32-D65N). We discuss what consequences for subsequent repair a single class of Rec12-oligonucleotides may have during meiotic recombination in fission yeast in comparison to two classes of Spo11-oligonucleotides in budding yeast. Furthermore, we hypothesize on the participation of Hop1 and Mek1 in Rec12 removal.","doi":"10.1371/journal.pgen.1000722","authors":"Rothenberg M, Kohli J, Ludin K","authors_abbrev":"Rothenberg M et al.","pubmed_publication_date":"Nov 2009","pubmed_entrez_date":"2009-11-14","publication_year":"2009","canto_session_key":"6a9c8e26d513116c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-03-26 12:32:35","canto_approved_date":"2023-01-06 16:01:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-03-23 16:00:19","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":31,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1556.01c","SPCC338.08","SPAC13C5.07","SPAC17A5.11","SPAC14C4.03","SPBC1718.02"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-03-26"},{"uniquename":"PMID:22156748","title":"The inner nuclear membrane proteins Man1 and Ima1 link to two different types of chromatin at the nuclear periphery in S. pombe.","citation":"Nucleus 2012;3(1):77-87","abstract":"Metazoan chromatin at the nuclear periphery is generally characterized by lowly expressed genes and repressive chromatin marks and presents a sub-compartment with properties distinct from the nuclear interior. To test whether the S. pombe nuclear periphery behaves similarly, we used DNA adenine methyltransferase identification (DamID) to map the target loci of two inner nuclear membrane proteins, Ima1 and Man1. We found that peripheral chromatin shows low levels of RNA-Polymerase II and nucleosome occupancy, both characteristic of repressed chromatin regions. Consistently, lowly expressed genes preferentially associate with the periphery and highly expressed genes are depleted from it. When looking at peripheral intergenic regions (IGRs), we found that divergent IGRs are enriched compared with convergent IGRs, indicating that transcription preferentially points away from the periphery rather than toward it. Interestingly, we found that Ima1 and Man1 have common, but also separate target regions in the genome. Ima1-interacting loci were enriched for the RNAi components Dcr1 and Rdp1. This agrees with previous findings that Dcr1 is localized at the nuclear periphery. In contrast, Man1 target loci were bound by the heterochromatin protein Swi6, especially at subtelomeric regions. Subtelomeric chromatin was shown to form a unique chromatin type lacking both repressive and active chromatin features and containing low levels of the histone variant H2A.Z. Thus, we find that the fission yeast nuclear periphery shows similar properties to those of metazoan cells, despite the absence of a nuclear lamina. Our results point to a role of nuclear membrane proteins in organizing chromatin domains and loops.","authors":"Steglich B, Filion GJ, van Steensel B, Ekwall K","authors_abbrev":"Steglich B et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2011-12-14","publication_year":"2012","canto_session_key":"c9bb9214228ec27e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-09 11:46:22","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-21 17:40:42","canto_added_date":"2012-02-17 16:51:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.03c","SPAC14C4.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-21"},{"uniquename":"PMID:10526233","title":"Fission yeast APC/cyclosome subunits, Cut20/Apc4 and Cut23/Apc8, in regulating metaphase-anaphase progression and cellular stress responses.","citation":"Genes Cells 1999 Aug;4(8):445-63","abstract":"The 20S cyclosome/APC complex promotes metaphase-anaphase transition by ubiquitinating its specific substrates such as mitotic cyclins and anaphase inhibitor Cut2/Pds1/securin. The complex has been shown to contain more than 10 proteins in budding yeast and frog. In fission yeast, however, only five (Cut4, Cut9, Nuc2, Apc10, Hcn1) have been identified.\nMore than five hundred temperature-sensitive mutants were screened for identifying those defective in mitotic anaphase. Fifty-five showed the cut (cell untimely torn) phenotype or metaphase-arrest phenotypes, 27 of them locating at new loci. Their extracts were run in sucrose gradient centrifugation, and four showed alterations in the sedimentation profiles. The gene products of cut20+ and cut23+ were thus identified. Phenotypes of cut20-100 mutant highly resemble cut4-533 in many ways: they are hypersensitive to canavanine and CdCl2, and suppressed by PKA-inactivating regulators, cAMP-dependent phosphodiesterase and PKA regulatory subunits. Cut20 interacts closely with Cut4 in the assembly process of cyclosome. But cut20 mutant differs from cut4, as a novel gene stw1+ suppresses cut20 mutant but not cut4. cut23-194 mutant cells are sterile and blocked at metaphase, but does not show sensitivity to the stress and cAMP. TPR repeat-containing Cut23 may not be the stable component of APC/cyclosome, and its level significantly fluctuates during cell cycle. Cut23 may be ubiquitinated and degraded in a cell cycle dependent fashion.\nWe identified two new subunits of fission yeast cyclosome/APC complex. Our observations indicate that cyclosome components are divided into several subgroups with distinctly different roles.","authors":"Yamashita YM, Nakaseko Y, Kumada K, Nakagawa T, Yanagida M","authors_abbrev":"Yamashita YM et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-10-20","publication_year":"1999","canto_session_key":"8f53c0c80571a308","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-03-02 08:13:19","canto_approved_date":"2026-01-29 12:21:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-26 18:03:08","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.09","SPAC19G12.01c","SPAC6F12.15c","SPAC8C9.03","SPCC285.09c","SPAC6F12.14","SPAC17C9.01c","SPAC13G6.14"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-03-02"},{"uniquename":"PMID:24316080","title":"Dissection of a redox relay: H2O2-dependent activation of the transcription factor Pap1 through the peroxidatic Tpx1-thioredoxin cycle.","citation":"Cell Rep 2013 Dec 12;5(5):1413-24","abstract":"In fission yeast, the transcription factor Pap1 undergoes H2O2-dependent oxidation that promotes its nuclear accumulation and the activation of an antioxidant gene program. However, the mechanisms that regulate the sensitivity and selectivity of Pap1 activation by peroxides are not fully understood. Here, we demonstrate that the peroxiredoxin Tpx1, the sensor of this signaling cascade, activates the otherwise unresponsive Pap1 protein once the main cytosolic reduced thioredoxin, Trx1, becomes transiently depleted. In other words, Pap1 works as an alternative electron donor for oxidized Tpx1. We have trapped the very transient Tpx1-Pap1 intermediate in cells depleted in Trx1, as we show here using mass spectrometry. Recycling of Tpx1 by Trx1 is required for the efficient signaling to Pap1, suggesting that the complete cycle of H2O2 scavenging by Tpx1 and further recycling of oxidized Tpx1 by Trx1 is required for full downstream activation of the redox cascade.","doi":"10.1016/j.celrep.2013.11.027","authors":"Calvo IA, Boronat S, Domènech A, García-Santamarina S, Ayté J, Hidalgo E","authors_abbrev":"Calvo IA et al.","pubmed_publication_date":"12 Dec 2013","pubmed_entrez_date":"2013-12-10","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1783.07c","SPCC576.03c","SPAC7D4.07c","SPBC32F12.03c","SPBC577.08c"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:27918601","title":"Identifying genes required for respiratory growth of fission yeast.","citation":"Wellcome Open Res 2016;1:12","abstract":"We have used both auxotroph and prototroph versions of the latest deletion-mutant library to identify genes required for respiratory growth on solid glycerol medium in fission yeast. This data set complements and enhances our recent study on functional and regulatory aspects of energy metabolism by providing additional proteins that are involved in respiration. Most proteins identified in this mutant screen have not been implicated in respiration in budding yeast. We also provide a protocol to generate a prototrophic mutant library, and data on technical and biological reproducibility of colony-based high-throughput screens.","doi":"10.12688/wellcomeopenres.9992.1","authors":"Malecki M, Bähler J","authors_abbrev":"Malecki M et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-12-06","publication_year":"2016","canto_session_key":"5dd86c90f530fd65","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-10-19 16:36:51","canto_approved_date":"2023-04-03 16:05:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-19 16:36:24","canto_added_date":"2016-12-07 01:15:11","annotation_curators":[],"file_curator_name":"Michal Malecki","file_curator_role":"community","annotation_file_curators":[{"name":"Michal Malecki","community_curator":true,"annotation_count":221,"orcid":"0000-0002-1525-5036","file_type":"PHAF","file_name":"PMID_27918601_phaf.tsv"}],"genes":["SPBC543.09","SPAC14C4.14","SPBC409.19c","SPCC663.01c","SPAC1635.01","SPAC8C9.06c","SPAC1565.01","SPBC365.14c","SPAC11E3.05","SPBC25H2.09","SPBP35G2.05c","SPCC1020.06c","SPAC3H8.09c","SPCC584.01c","SPCC1442.15c","SPAC5H10.04","SPAC22A12.11","SPAC31A2.11c","SPAC4D7.10c","SPBC56F2.09c","SPAP27G11.02","SPAC637.11","SPAC823.17","SPBC27B12.03c","SPBC354.08c","SPBC530.11c","SPBC3D6.06c","SPAC6F12.02","SPBC25H2.08c","SPBC27.06c","SPBC17A3.05c","SPBC23G7.06c","SPBC3H7.10","SPCC895.06","SPCC548.07c","SPCC550.14","SPAC22A12.01c","SPAC13G6.10c","SPBC146.13c","SPAC56F8.02","SPAC977.10","SPBC725.12","SPAC11G7.02","SPBC1A4.02c","SPAC3A12.12","SPCC330.12c","SPBC691.04","SPCC74.03c","SPAC2F7.03c","SPCC285.09c","SPAC6B12.08","SPBP4H10.10","SPBC16H5.07c","SPBC1604.07","SPCC970.06","SPBC646.09c","SPCC794.08","SPAC1610.03c","SPBC21B10.05c","SPCC794.10","SPAC1556.08c","SPCC1393.08","SPAC110.02","SPAC1F5.08c","SPAC4G9.20c","SPCC1322.01","SPCC736.07c","SPAC1039.06","SPAC222.12c","SPBC660.10","SPCC4G3.04c","SPBC31F10.09c","SPBC18E5.05c","SPCC1919.10c","SPAC1071.11","SPAC1399.02","SPAC13F5.03c","SPAC3A12.13c","SPAC227.17c","SPCC645.07","SPAC17G8.14c","SPBP8B7.08c","SPBC3E7.16c","SPAC19G12.15c","SPBC1306.02","SPBC17G9.07","SPCC1919.03c","SPCC191.07","SPBC3H7.03c","SPAC2F7.17","SPBC30B4.06c","SPAC821.05","SPAC4G8.13c","SPAC19A8.08","SPAC22H10.09","SPAC57A7.08","SPAC31A2.06","SPAC2C4.17c","SPAC4A8.04","SPBC19G7.10c","SPCC297.03","SPBC106.05c","SPBP4H10.03","SPAC1071.07c","SPBC29A3.17","SPAC19A8.04","SPAC4G8.05","SPAC144.04c","SPCC737.09c","SPAC25B8.05","SPCC895.05","SPAC3F10.17","SPAC1B3.01c","SPAC30C2.08","SPAC8C9.09c","SPBC25B2.04c","SPAC27D7.08c","SPAC22F3.07c","SPBC16A3.16","SPBC2G5.06c","SPBC1709.09","SPBC32H8.02c","SPBC776.15c","SPBC4F6.08c","SPCP1E11.02","SPAC29B12.04","SPAC1F5.10","SPBC27B12.10c","SPAC1296.02","SPAC4C5.04","SPBC1198.14c","SPAC17H9.04c","SPAC222.08c","SPAC17H9.10c","SPBC12D12.07c","SPAC23D3.09","SPBC1778.06c","SPAC1142.07c","SPAC30D11.11","SPAC9E9.09c","SPBC18H10.11c","SPAC1486.08","SPCC16A11.08","SPAC458.05","SPBC336.13c","SPAC140.01","SPBC1D7.04","SPBC1778.01c","SPAC926.03","SPBC21C3.03","SPAC823.11","SPBP23A10.10","SPAC732.02c","SPBC26H8.03","SPCC4B3.15","SPBC106.19","SPBC947.15c","SPAC17H9.12c","SPAC2F7.02c","SPCC1442.03","SPAC2F7.09c","SPBC2A9.11c","SPAC1556.05c","SPBC1A4.09","SPCC569.04","SPAC13G7.03","SPBC23G7.13c","SPBC16E9.03c","SPBC29A3.01","SPAC12B10.03","SPAC22A12.10","SPCC1442.05c","SPAC6B12.12","SPBC4C3.12","SPBC1215.01","SPBC16A3.03c","SPAC31A2.14","SPAC19G12.13c","SPBC1778.03c","SPBC776.09","SPBP8B7.25","SPAC27E2.11c","SPCC4B3.17","SPAC637.07","SPCC736.06","SPAC4F8.03","SPAC1782.08c","SPAC1D4.01","SPAC9.12c","SPAC13C5.05c","SPCC1840.09","SPCC16A11.07","SPAC4H3.07c","SPAP8A3.07c","SPBC1289.06c","SPBC1198.11c","SPAC1610.02c","SPBC19F8.06c","SPAC12B10.09","SPBC428.06c","SPBC119.06","SPBC21B10.03c","SPAC144.03","SPAC22F3.06c","SPBC29A10.13","SPCC825.01","SPAC3H8.03","SPAC9E9.10c","SPBC1105.04c","SPAC16C9.06c","SPAC26A3.01","SPBC14C8.16c","SPBC32F12.03c","SPAC25G10.09c","SPBC1711.13","SPBC30D10.10c","SPAC4G8.11c","SPAC222.05c","SPAPJ691.03","SPAC26H5.04","SPBC3B8.02"],"gene_count":221,"ltp_gene_count":0,"approved_date":"2017-10-19"},{"uniquename":"PMID:15448137","title":"Atf1-Pcr1-M26 complex links stress-activated MAPK and cAMP-dependent protein kinase pathways via chromatin remodeling of cgs2+.","citation":"J Biol Chem 2004 Dec 03;279(49):50857-63","abstract":"Although co-ordinate interaction between different signal transduction pathways is essential for developmental decisions, interpathway connections are often obscured and difficult to identify due to cross-talk. Here signals from the fission yeast stress-activated MAPK Spc1 are shown to regulate Cgs2, a negative regulator of the cAMP-dependent protein kinase (protein kinase A) pathway. Pathway integration is achieved via Spc1-dependent binding of Atf1-Pcr1 heterodimer to an M26 DNA site in the cgs2+ promoter, which remodels chromatin to regulate expression of cgs2+ and targets downstream of protein kinase A. This direct interpathway connection co-ordinates signals of nitrogen and carbon source depletion to affect a G0 cell-cycle checkpoint and sexual differentiation. The Atf1-Pcr1-M26 complex-dependent chromatin remodeling provides a molecular mechanism whereby Atf1-Pcr1 heterodimer can function differentially as either a transcriptional activator, or as a transcriptional repressor, or as an inducer of meiotic recombination. We also show that the Atf1-Pcr1-M26 complex functions as both an inducer and repressor of chromatin remodeling, which provides a way for various chromatin remodeling-dependent effector functions to be regulated.","authors":"Davidson MK, Shandilya HK, Hirota K, Ohta K, Wahls WP","authors_abbrev":"Davidson MK et al.","pubmed_publication_date":"03 Dec 2004","pubmed_entrez_date":"2004-09-28","publication_year":"2004","canto_session_key":"65ee22c229c3e125","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 19:46:40","canto_approved_date":"2024-04-03 10:08:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-20 17:10:48","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPBC29B5.01","SPCC285.09c","SPAC24B11.06c","SPAC21E11.03c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-06-10"},{"uniquename":"PMID:20347428","title":"A histone-fold complex and FANCM form a conserved DNA-remodeling complex to maintain genome stability.","citation":"Mol Cell 2010 Mar 26;37(6):865-78","abstract":"FANCM remodels branched DNA structures and plays essential roles in the cellular response to DNA replication stress. Here, we show that FANCM forms a conserved DNA-remodeling complex with a histone-fold heterodimer, MHF. We find that MHF stimulates DNA binding and replication fork remodeling by FANCM. In the cell, FANCM and MHF are rapidly recruited to forks stalled by DNA interstrand crosslinks, and both are required for cellular resistance to such lesions. In vertebrates, FANCM-MHF associates with the Fanconi anemia (FA) core complex, promotes FANCD2 monoubiquitination in response to DNA damage, and suppresses sister-chromatid exchanges. Yeast orthologs of these proteins function together to resist MMS-induced DNA damage and promote gene conversion at blocked replication forks. Thus, FANCM-MHF is an essential DNA-remodeling complex that protects replication forks from yeast to human.","doi":"10.1016/j.molcel.2010.01.039","authors":"Yan Z, Delannoy M, Ling C, Daee D, Osman F, Muniandy PA, Shen X, Oostra AB, Du H, Steltenpool J, Lin T, Schuster B, Décaillet C, Stasiak A, Stasiak AZ, Stone S, Hoatlin ME, Schindler D, Woodcock CL, Joenje H, Sen R, de Winter JP, Li L, Seidman MM, Whitby MC, Myung K, Constantinou A, Wang W","authors_abbrev":"Yan Z et al.","pubmed_publication_date":"26 Mar 2010","pubmed_entrez_date":"2010-03-30","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:11422","SPCC576.12c","HGNC:23163","SPBC2D10.16","SPAC9.05","HGNC:23168"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:17434133","title":"A network of multiple regulatory layers shapes gene expression in fission yeast.","citation":"Mol Cell 2007 Apr 13;26(1):145-55","abstract":"Gene expression is controlled at multiple layers, and cells may integrate different regulatory steps for coherent production of proper protein levels. We applied various microarray-based approaches to determine key gene-expression intermediates in exponentially growing fission yeast, providing genome-wide data for translational profiles, mRNA steady-state levels, polyadenylation profiles, start-codon sequence context, mRNA half-lives, and RNA polymerase II occupancy. We uncovered widespread and unexpected relationships between distinct aspects of gene expression. Translation and polyadenylation are aligned on a global scale with both the lengths and levels of mRNAs: efficiently translated mRNAs have longer poly(A) tails and are shorter, more stable, and more efficiently transcribed on average. Transcription and translation may be independently but congruently optimized to streamline protein production. These rich data sets, all acquired under a standardized condition, reveal a substantial coordination between regulatory layers and provide a basis for a systems-level understanding of multilayered gene-expression programs.","authors":"Lackner DH, Beilharz TH, Marguerat S, Mata J, Watt S, Schubert F, Preiss T, Bähler J","authors_abbrev":"Lackner DH et al.","pubmed_publication_date":"13 Apr 2007","pubmed_entrez_date":"2007-04-17","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26631139","title":"Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe.","citation":"Cell Stress Chaperones 2016 Mar;21(2):327-38","abstract":"Changes in the levels of three structurally and functionally different important thermoprotectant molecules, namely small heat shock proteins (sHsps), trehalose, and lipids, have been investigated upon heat shock in Schizosaccharomyces pombe. Both α-crystallin-type sHsps (Hsp15.8 and Hsp16) were induced after prolonged high-temperature treatment but with different kinetic profiles. The shsp null mutants display a weak, but significant, heat sensitivity indicating their importance in the thermal stress management. The heat induction of sHsps is different in wild type and in highly heat-sensitive trehalose-deficient (tps1Δ) cells; however, trehalose level did not show significant alteration in shsp mutants. The altered timing of trehalose accumulation and induction of sHsps suggest that the disaccharide might provide protection at the early stage of the heat stress while elevated amount of sHsps are required at the later phase. The cellular lipid compositions of two different temperature-adapted wild-type S. pombe cells are also altered according to the rule of homeoviscous adaptation, indicating their crucial role in adapting to the environmental temperature changes. Both Hsp15.8 and Hsp16 are able to bind to different lipids isolated from S. pombe, whose interaction might provide a powerful protection against heat-induced damages of the membranes. Our data suggest that all the three investigated thermoprotectant macromolecules play a pivotal role during the thermal stress management in the fission yeast.","doi":"10.1007/s12192-015-0662-4","authors":"Glatz A, Pilbat AM, Németh GL, Vince-Kontár K, Jósvay K, Hunya Á, Udvardy A, Gombos I, Péter M, Balogh G, Horváth I, Vígh L, Török Z","authors_abbrev":"Glatz A et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2015-12-04","publication_year":"2016","canto_session_key":"741e37a44e48bc4a","canto_annotation_status":"CURATION_PAUSED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-12-05 01:19:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15107426","title":"The Schizosaccharomyces pombe Pccs protein functions in both copper trafficking and metal detoxification pathways.","citation":"J Biol Chem 2004 Jul 02;279(27):28744-55","abstract":"Because copper is both an essential cofactor and a toxic metal, different strategies have evolved to appropriately regulate its homeostasis as a function of changing environmental copper levels. In this report, we describe a metallochaperone-like protein from Schizosaccharomyces pombe that maintains the delicate balance between essentiality and toxicity. This protein, designated Pccs, has four distinct domains. SOD activity assays reveal that the first three domains of Pccs are necessary and sufficient to deliver copper to its target, copper-zinc superoxide dismutase (SOD1). Pccs domain IV, which is absent in Saccharomyces cerevisiae CCS1, contains seventeen cysteine residues, eight pairs of which are in a potential metal coordination arrangement, Cys-Cys. We show that S. cerevisiae ace1Delta mutant cells expressing the full-length Pccs molecule are resistant to copper toxicity. Furthermore, we demonstrate that the Pccs domain IV enhances copper resistance of the ace1Delta cells by an order of magnitude compared with that observed in the same strain expressing a pccs+ I-II-III allele encoding Pccs domains I-III. We consistently found that S. pombe cells disrupted in the pccs+ gene exhibit an increased sensitivity to copper and cadmium. Furthermore, we demonstrate that overexpression of pccs+ is associated with increased copper resistance in fission yeast cells. Taken together, our findings suggest that Pccs activates apo-SOD1 under copper-limiting conditions through the use of its first three domains and protects cells against metal ion toxicity via its fourth domain.","authors":"Laliberté J, Whitson LJ, Beaudoin J, Holloway SP, Hart PJ, Labbé S","authors_abbrev":"Laliberté J et al.","pubmed_publication_date":"02 Jul 2004","pubmed_entrez_date":"2004-04-27","publication_year":"2004","canto_session_key":"9a6963fe53b113ea","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2026-03-13 13:38:12","canto_approved_date":"2026-03-13 15:16:53","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-03-13 13:38:06","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22H10.13","SPBC29A3.01","SPAC821.10c","SPBC1709.10c","SPAC22E12.04","SPBC23G7.16"],"gene_count":6,"ltp_gene_count":3,"approved_date":"2026-03-13"},{"uniquename":"EMBL:AU009268","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22323607","title":"Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan.","citation":"Proc Natl Acad Sci U S A 2012 Feb 21;109(8):2872-7","abstract":"Conformational dynamics in bilobed enzymes can be used to regulate their activity. One such enzyme, the eukaryotic decapping enzyme Dcp2, controls the half-life of mRNA by cleaving the 5' cap structure, which exposes a monophosphate that is efficiently degraded by exonucleases. Decapping by Dcp2 is thought to be controlled by an open-to-closed transition involving formation of a composite active site with two domains sandwiching substrate, but many details of this process are not understood. Here, using NMR spectroscopy and enzyme kinetics, we show that Trp43 of Schizosaccharomyces pombe Dcp2 is a conserved gatekeeper of this open-to-closed transition. We find that Dcp2 samples multiple conformations in solution on the millisecond-microsecond timescale. Mutation of the gatekeeper tryptophan abolishes the dynamic behavior of Dcp2 and attenuates coactivation by a yeast enhancer of decapping (Edc1). Our results determine the dynamics of the open-to-closed transition in Dcp2, suggest a structural pathway for coactivation, predict that Dcp1 directly contacts the catalytic domain of Dcp2, and show that coactivation of decapping by Dcp2 is linked to formation of the composite active site.","doi":"10.1073/pnas.1113620109","authors":"Floor SN, Borja MS, Gross JD","authors_abbrev":"Floor SN et al.","pubmed_publication_date":"21 Feb 2012","pubmed_entrez_date":"2012-02-11","publication_year":"2012","canto_session_key":"9288ccb2385d9465","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-10-21 16:34:37","canto_approved_date":"2023-04-18 18:40:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-21 12:33:30","canto_added_date":"2012-02-24 05:46:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3B9.21","SPAC19A8.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-10-21"},{"uniquename":"PMID:25916706","title":"Measuring DNA content by flow cytometry in fission yeast.","citation":"Methods Mol Biol 2015;1300:79-97","abstract":"Flow cytometry is an essential tool to monitor DNA content and determine cell cycle distribution. Its utility in fission yeast reflects the ease of sample preparation, the stochiometric binding of the most popular DNA dyes (propidium iodide and Sytox Green), and ability to monitor cell size. However, the study of DNA replication with multicolour flow analysis has lagged behind its use in mammalian cells. We present basic and advanced protocols for analysis of DNA replication in fission yeast by flow cytometry including whole cell, nuclear \"ghosts,\" two-color imaging with BrdU, and estimates of DNA synthesis using EdU.","doi":"10.1007/978-1-4939-2596-4_5","authors":"Sabatinos SA, Forsburg SL","authors_abbrev":"Sabatinos SA et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-04-29","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-04-30 00:19:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18256242","title":"Chromodomains direct integration of retrotransposons to heterochromatin.","citation":"Genome Res 2008 Mar;18(3):359-69","abstract":"The enrichment of mobile genetic elements in heterochromatin may be due, in part, to targeted integration. The chromoviruses are Ty3/gypsy retrotransposons with chromodomains at their integrase C termini. Chromodomains are logical determinants for targeting to heterochromatin, because the chromodomain of heterochromatin protein 1 (HP1) typically recognizes histone H3 K9 methylation, an epigenetic mark characteristic of heterochromatin. We describe three groups of chromoviruses based on amino acid sequence relationships of their integrase C termini. Genome sequence analysis indicates that representative chromoviruses from each group are enriched in gene-poor regions of the genome relative to other retrotransposons, and when fused to fluorescent marker proteins, the chromodomains target proteins to specific subnuclear foci coincident with heterochromatin. The chromodomain of the fungal element, MAGGY, interacts with histone H3 dimethyl- and trimethyl-K9, and when the MAGGY chromodomain is fused to integrase of the Schizosaccharomyces pombe Tf1 retrotransposon, new Tf1 insertions are directed to sites of H3 K9 methylation. Repetitive sequences such as transposable elements trigger the RNAi pathway resulting in their epigenetic modification. Our results suggest a dynamic interplay between retrotransposons and heterochromatin, wherein mobile elements recognize heterochromatin at the time of integration and then perpetuate the heterochromatic mark by triggering epigenetic modification.","doi":"10.1101/gr.7146408","authors":"Gao X, Hou Y, Ebina H, Levin HL, Voytas DF","authors_abbrev":"Gao X et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38344063","title":"Quality Control Method and Device for Producing Agarose Micropads.","citation":"MicroPubl Biol 2024;2024","abstract":"In brightfield and fluorescence microscopy, capturing images that show well-focused and immobile microorganisms can be challenging. An agarose-based gel pad reduces the variability of results, especially in conditions like uneven specimen staging, variable fluid dynamics, and Brownian motion that plague conventional wet mount setups. To correct these discrepancies during image acquisition, we analyzed three micropad preparation setups. We tested the quality and consistency of pads and images resulting from each setup. Our examination reveals that improved gel pad flatness is associated with better image quality. Moreover, we observe increased consistency in gel pad construction connected to the use of a 3D-printed setup. These findings highlight the technical benefits arising from incorporating micropad-generating platforms that increase the consistency of results in imaging pipelines. Additionally, our use of a quantitative approach to examine pad flatness suggests its inclusion in quality control pipelines to reduce variation in gel pad construction and image quality over time and between investigators. Finally, our use of a 3D-printed setup coupled with a quantitative downstream routine suggests their application in microscopy experiments that involve model organisms relevant to human health and disease.","doi":"10.17912/micropub.biology.001081","authors":"Vo M, Kuo-Esser L, Dominguez M, Driggers J, Kuchinski K, Perez S, Luck T, Tran T, Tran T, Gerberry D, Wetzel H, Escorcia W","authors_abbrev":"Vo M et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-02-12","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-10-01 17:43:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20829796","title":"HAATI survivors replace canonical telomeres with blocks of generic heterochromatin.","citation":"Nature 2010 Sep 09;467(7312):223-7","abstract":"The notion that telomeres are essential for chromosome linearity stems from the existence of two chief dangers: inappropriate DNA damage response (DDR) reactions that mistake natural chromosome ends for double-strand DNA breaks (DSBs), and the progressive loss of DNA from chromosomal termini due to the end replication problem. Telomeres avert the former peril by binding sequence-specific end-protection factors that control the access of DDR activities. The latter threat is tackled by recruiting telomerase, a reverse transcriptase that uses an integral RNA subunit to template the addition of telomere repeats to chromosome ends. Here we describe an alternative mode of linear chromosome maintenance in which canonical telomeres are superseded by blocks of heterochromatin. We show that in the absence of telomerase, Schizosaccharomyces pombe cells can survive telomere sequence loss by continually amplifying and rearranging heterochromatic sequences. Because the heterochromatin assembly machinery is required for this survival mode, we have termed it 'HAATI' (heterochromatin amplification-mediated and telomerase-independent). HAATI uses the canonical end-protection protein Pot1 (ref. 4) and its interacting partner Ccq1 (ref. 5) to preserve chromosome linearity. The data suggest a model in which Ccq1 is recruited by the amplified heterochromatin and provides an anchor for Pot1, which accomplishes its end-protection function in the absence of its cognate DNA-binding sequence. HAATI resembles the chromosome end-maintenance strategy found in Drosophila melanogaster, which lacks specific telomere sequences but nonetheless assembles terminal heterochromatin structures that recruit end-protection factors. These findings reveal a previously unrecognized mode by which cancer cells might escape the requirement for telomerase activation, and offer a tool for studying genomes that sustain unusually high levels of heterochromatinization.","doi":"10.1038/nature09374","authors":"Jain D, Hebden AK, Nakamura TM, Miller KM, Cooper JP","authors_abbrev":"Jain D et al.","pubmed_publication_date":"09 Sep 2010","pubmed_entrez_date":"2010-09-11","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31010807","title":"Structure of Fission Yeast Transcription Factor Pho7 Bound to  pho1  Promoter DNA and Effect of Pho7 Mutations on DNA Binding and Phosphate Homeostasis.","citation":"Mol Cell Biol 2019 Jul 01;39(13)","abstract":"Pho7 is the  Schizosaccharomyces pombe  fission yeast Zn 2 Cys 6  transcriptional factor that drives a response to phosphate starvation in which phosphate acquisition genes are upregulated. Here we report a crystal structure at 1.6-Å resolution of the Pho7 DNA-binding domain (DBD) bound at its target site 2 in the  pho1  promoter (5'-TCGGAAATTAAAAA). Comparison to the previously reported structure of Pho7 DBD in complex with its binding site in the  tgp1  promoter (5'-TCGGACATTCAAAT) reveals shared determinants of target site specificity as well as variations in the protein-DNA interface that accommodate different promoter DNA sequences. Mutagenesis of Pho7 amino acids at the DNA interface identified nucleobase contacts at the periphery of the footprint that are essential for the induction of  pho1  expression in response to phosphate starvation and for Pho7 binding to site 1 in the  pho1  promoter.","doi":"10.1128/MCB.00132-19","authors":"Garg A, Goldgur Y, Sanchez AM, Schwer B, Shuman S","authors_abbrev":"Garg A et al.","pubmed_publication_date":"01 Jul 2019","pubmed_entrez_date":"2019-04-24","publication_year":"2019","canto_session_key":"f61c7346be6b7a50","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Angad Garg","canto_first_approved_date":"2022-01-17 13:44:08","canto_approved_date":"2022-01-17 18:52:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-13 18:13:21","canto_added_date":"2019-04-25 00:15:05","annotation_curators":[{"name":"Angad Garg","community_curator":true,"annotation_count":32,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPBC27B12.11c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2022-01-17","pdb_entries":[{"pdb_id":"6o19","gene_chains":[{"gene_uniquename":"SPBC27B12.11c","chain":"A","position":"279-336"}],"title":"Crystal Structure of Pho7 complex with pho1 promoter site 2","entry_authors":"Garg A,Goldgur Y,Shuman S","entry_authors_abbrev":"Garg A et al.","reference_uniquename":"PMID:31010807","experimental_method":"X-ray","resolution":"1.596"}]},{"uniquename":"PMID:24039245","title":"The human kinesin-14 HSET tracks the tips of growing microtubules in vitro.","citation":"Cytoskeleton (Hoboken) 2013 Sep;70(9):515-21","abstract":"Tip-tracking of kinesin-14 motor proteins is believed to be crucial for the assembly and maintenance of dynamic microtubule arrays. However, in contrast to other members of the kinesin-14 family, H. sapiens kinesin-14 HSET has so far never been observed to be prominently located at microtubule plus ends. Here, using an in vitro microtubule dynamics reconstitution assay we observe tip-tracking of GFP-HSET in the presence of H. sapiens EB1 (hsEB1). Tip-tracking depended on the SxIP-like motif in HSET as well as on the EB homology domain in hsEB1. D. melanogaster Ncd and S. pombe Klp2 tip-tracking reconstitution assays accompanied by kinesin-14 amino acid sequence comparisons suggest that SxIP-like motif mediated tip-tracking dependent on EB family proteins is conserved in the kinesin-14 family of molecular motors.","doi":"10.1002/cm.21133","authors":"Braun M, Lansky Z, Bajer S, Fink G, Kasprzak AA, Diez S","authors_abbrev":"Braun M et al.","pubmed_publication_date":"Sep 2013","pubmed_entrez_date":"2013-09-17","publication_year":"2013","canto_session_key":"cea510a27fb48927","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-06-30 14:25:39","canto_approved_date":"2022-02-02 17:14:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-11 10:48:58","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.10","SPAC18G6.15"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-06-30"},{"uniquename":"EMBL:SPMOP1MCS","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11553715","title":"The domain structure of centromeres is conserved from fission yeast to humans.","citation":"Mol Biol Cell 2001 Sep;12(9):2767-75","abstract":"The centromeric DNA of fission yeast is arranged with a central core flanked by repeated sequences. The centromere-associated proteins, Mis6p and Cnp1p (SpCENP-A), associate exclusively with central core DNA, whereas the Swi6 protein binds the surrounding repeats. Here, electron microscopy and immunofluorescence light microscopy reveal that the central core and flanking regions occupy distinct positions within a heterochromatic domain. An \"anchor\" structure containing the Ndc80 protein resides between this heterochromatic domain and the spindle pole body. The organization of centromere-associated proteins in fission yeast is reminiscent of the multilayered structures of human kinetochores, indicating that such domain structure is conserved in eukaryotes.","authors":"Kniola B, O'Toole E, McIntosh JR, Mellone B, Allshire R, Mengarelli S, Hultenby K, Ekwall K","authors_abbrev":"Kniola B et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-09-13","publication_year":"2001","canto_session_key":"4e4a74761fe0e5cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-02-24 18:37:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-22 14:38:34","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1687.20c","SPBC11C11.03","SPAC664.01c","SPBC1105.17"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-01-22"},{"uniquename":"PMID:34209806","title":"Identification of Nrl1 Domains Responsible for Interactions with RNA-Processing Factors and Regulation of Nrl1 Function by Phosphorylation.","citation":"Int J Mol Sci 2021 Jun 29;22(13)","abstract":"Pre-mRNA splicing is a key process in the regulation of gene expression. In the fission yeast  Schizosaccharomyces pombe , Nrl1 regulates splicing and expression of several genes and non-coding RNAs, and also suppresses the accumulation of R-loops. Here, we report analysis of interactions between Nrl1 and selected RNA-processing proteins and regulation of Nrl1 function by phosphorylation. Bacterial two-hybrid system (BACTH) assays revealed that the N-terminal region of Nrl1 is important for the interaction with ATP-dependent RNA helicase Mtl1 while the C-terminal region of Nrl1 is important for interactions with spliceosome components Ctr1, Ntr2, and Syf3. Consistent with this result, tandem affinity purification showed that Mtl1, but not Ctr1, Ntr2, or Syf3, co-purifies with the N-terminal region of Nrl1. Interestingly, mass-spectrometry analysis revealed that in addition to previously identified phosphorylation sites, Nrl1 is also phosphorylated on serines 86 and 112, and that Nrl1-TAP co-purifies with Cka1, the catalytic subunit of casein kinase 2. In vitro assay showed that Cka1 can phosphorylate bacterially expressed Nrl1 fragments. An analysis of non-phosphorylatable  nrl1  mutants revealed defects in gene expression and splicing consistent with the notion that phosphorylation is an important regulator of Nrl1 function. Taken together, our results provide insights into two mechanisms that are involved in the regulation of the spliceosome-associated factor Nrl1, namely domain-specific interactions between Nrl1 and RNA-processing proteins and post-translational modification of Nrl1 by phosphorylation.","doi":"10.3390/ijms22137011","authors":"Mikolaskova B, Jurcik M, Cipakova I, Selicky T, Jurcik J, Polakova SB, Stupenova E, Dudas A, Sivakova B, Bellova J, Barath P, Aronica L, Gregan J, Cipak L","authors_abbrev":"Mikolaskova B et al.","pubmed_publication_date":"29 Jun 2021","pubmed_entrez_date":"2021-07-02","publication_year":"2021","canto_session_key":"24d8dd57a8133df4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Lubos Cipak","canto_first_approved_date":"2021-07-30 14:57:45","canto_approved_date":"2023-12-24 11:01:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-07-29 04:48:52","canto_added_date":"2021-07-04 00:15:05","annotation_curators":[{"name":"Lubos Cipak","community_curator":true,"annotation_count":13,"orcid":"0000-0001-7897-6001","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB24D3.10c","SPAC23C11.11","SPAC29A4.08c","SPAC140.04","SPBC23G7.10c","SPCC794.01c","SPBPB2B2.01","SPCC548.07c","SPAC17A2.08c","SPBC20F10.05","SPBC31F10.11c","SPAC1F3.09","SPAC17H9.02","SPAC4G8.03c"],"gene_count":14,"ltp_gene_count":7,"approved_date":"2021-07-30"},{"uniquename":"PMID:38188419","title":"A missense mutation in the  suc22  gene encoding the small subunit of ribonucleotide reductase significantly sensitizes fission yeast to chronic treatment with hydroxyurea.","citation":"MicroPubl Biol 2023;2023","abstract":"Ribonucleotide reductase (RNR) is essential for the biosynthesis of dNTPs and a therapeutic target. We have identified a missense mutation in  suc22  , which encodes the small subunit of RNR in fission yeast. The  suc22-S239F  mutation significantly sensitizes the cells to chronic but not acute treatment with the RNR inhibitor hydroxyurea. Preliminary data indicate that the drug sensitivity is likely due to decreased RNR activity. Since  S239F  is the first missense mutation reported for  suc22  and the mutated residue is highly conserved, the results will be useful for future yeast genetic studies and potentially, the development of new therapeutics targeting RNR.","doi":"10.17912/micropub.biology.001041","authors":"Davi K, Yurtsever I, Xu YJ","authors_abbrev":"Davi K et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2024-01-08","publication_year":"2023","canto_session_key":"f29d798df96c977e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yongjie Xu","canto_first_approved_date":"2024-10-01 07:56:28","canto_approved_date":"2024-10-01 07:56:29","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-04 07:05:48","canto_added_date":"2024-01-09 00:25:06","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":9,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Yongjie Xu","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13A11.02c","SPAC222.11","SPBC25D12.04","SPCC18B5.11c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2024-10-01"},{"uniquename":"PMID:5705827","title":"Repair-mechanisms and radiation-induced mutations in fission yeast.","citation":"Genetics 1968 Jul;59(3):327-33","abstract":"","authors":"Nasim A","authors_abbrev":"Nasim A","pubmed_publication_date":"Jul 1968","pubmed_entrez_date":"1968-07-01","publication_year":"1968","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9013721","title":"Structural and functional analysis of the nucleolus of the fission yeast Schizosaccharomyces pombe.","citation":"Eur J Cell Biol 1997 Jan;72(1):13-23","abstract":"Yeasts are an attractive model for the study of ribosome synthesis. However, our understanding of the relationship between the structure and function of the yeast nucleolus, in which preribosomal particles are synthesized, requires further investigations using microscopic approaches and in situ molecular biology. Combining cryofixation and cryosubstitution of Schizosaccharomyces pombe, we could identify morphologically distinct substructures in the nucleolus similar to the components of nucleoli of higher eukaryotes such as the fibrillar centers (FCs), the dense fibrillar component (DFC) and the granular component (GC). We complemented this morphological study by performing in situ hybridization and immunocytochemistry at the electron microscopy level. Using a probe complementary to the entire rRNA transcription unit of S. pombe, we detected rDNA at the periphery of the FCs, while immunocytochemistry with antibodies specific for the RNA polymerase I and the gar1 protein provided evidence that transcription and early steps of maturation take place in the DFC that extends throughout the nucleolus. We also present evidence that preribosomal subunits may be exported along tracks to the cytoplasm through all of the pores of the nuclear envelope and not just those in the portion of the envelope close to the nucleolus.","authors":"Léger-Silvestre I, Noaillac-Depeyre J, Faubladier M, Gas N","authors_abbrev":"Léger-Silvestre I et al.","pubmed_publication_date":"Jan 1997","pubmed_entrez_date":"1997-01-01","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21664261","title":"Regulation of gene expression at the fission yeast Schizosaccharomyces pombe urg1 locus.","citation":"Gene 2011 Sep 15;484(1-2):75-85","abstract":"The lack of a rapid and efficient system to regulate transcriptional induction in the fission yeast Schizosaccharomyces pombe is currently a limitation of this model eukaryote. The commonly used nmt1 promoter has excellent dynamic range and a low \"off-state\" transcription, but takes 14-16 hours to induce upon thiamine withdrawal. Conversely, other induction systems have rapid response times, but suffer from a limited dynamic range and/or relatively high levels of off-state transcription. Recently, the urg1 gene was identified as a rapidly induced transcript, responding to uracil addition in ~30 min and exhibiting low off-state transcription and high dynamic range. However, attempts to reproduce this ectopically result in a significant increase in off-state transcription, severely limiting utility. To overcome this, we have adapted the Cre/lox recombination-mediated cassette exchange (RCME) system to facilitate easy insertion of sequences at the urg1 locus. We show that the P(urg1) induction kinetics are maintained when ectopic open reading frames (ORFs) replace the native urg1 ORF. As proof of principle, we characterise HO-endonuclease expression in cells harbouring a novel S. pombe single-strand annealing (SSA) assay. After 60 min induction we observe clear double-strand breaks, demonstrate >90% of cells are committed to SSA and show that the Rad22(Rad52) repair protein associates robustly with sequences adjacent to the DSB. This inducible system will be a valuable tool for future studies in S. pombe.","doi":"10.1016/j.gene.2011.05.028","authors":"Watson AT, Werler P, Carr AM","authors_abbrev":"Watson AT et al.","pubmed_publication_date":"15 Sep 2011","pubmed_entrez_date":"2011-06-14","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:4046021","title":"The mitochondrial genome of the fission yeast Schizosaccharomyces pombe. The cytochrome b gene has an intron closely related to the first two introns in the Saccharomyces cerevisiae cox1 gene.","citation":"J Mol Biol 1985 Aug 05;184(3):353-66","abstract":"The DNA sequence of the cob region of the Schizosaccharomyces pombe mitochondrial DNA has been determined. The cytochrome b structural gene is interrupted by an intron of 2526 base-pairs, which has an open reading frame of 2421 base-pairs in phase with the upstream exon. The position of the intron differs from those found in the cob genes of Saccharomyces cerevisiae, Aspergillus nidulans or Neurospora crassa. The Sch. pombe cob intron has the potential of assuming an RNA secondary structure almost identical to that proposed for the first two cox1 introns (group II) in S. cerevisiae and the p1-cox1 intron in Podospora anserina. It has most of the consensus nucleotides in the central core structure described for this group of introns and its comparison with other group II introns allows the identification of an additional conserved nucleotide stretch. A comparison of the predicted protein sequences of group II intronic coding regions reveals three highly conserved blocks showing pairwise amino acid identities of 34 to 53%. These regions comprise over 50% of the coding length of the intron but do not include the 5' region, which has strong secondary structural features. In addition to the potential intron folding, long helical structures involving repetitive sequences can be formed in the flanking cob exon regions. A comparison of the Sch. pombe cytochrome b sequence with those available from other organisms indicates that Sch. pombe is evolutionarily distant from both budding yeasts and filamentous fungi. As was seen for the Sch. pombe cox1 gene (Lang, 1984), the cob exons are translated using the universal genetic code and this distinguishes Sch. pombe mitochondria from all other fungal and animal mitochondrial systems.","authors":"Lang BF, Ahne F, Bonen L","authors_abbrev":"Lang BF et al.","pubmed_publication_date":"05 Aug 1985","pubmed_entrez_date":"1985-08-05","publication_year":"1985","canto_triage_status":"Mitochondrial sequence related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1464318","title":"Pyp3 PTPase acts as a mitotic inducer in fission yeast.","citation":"EMBO J 1992 Dec;11(13):4933-41","abstract":"The p34cdc2 M-phase kinase is regulated by inhibitory phosphorylation of Tyr15, largely through the actions of the p107wee1 tyrosine kinase and p80cdc25 protein tyrosine phosphatase (PTPase). In this study we demonstrate that a second PTPase, encoded by pyp3, also contributes to tyrosyl dephosphorylation of p34cdc2. Pyp3 was identified as a high copy suppressor of a cdc25- mutation. The pyp3 gene encodes a 33 kDa PTPase that is more closely related to human PTP1B and fission yeast pyp1 and pyp2 PTPases than to cdc25. Pyp3 does not share an essential overlapping function with pyp1 or pyp2. We demonstrate that disruption of pyp3 causes a mitotic delay that is greatly exacerbated in cells that are partially defective for cdc25 function and that pyp3 function is essential in cdc25-disruption wee1- strains. Pyp3 PTPase effectively dephosphorylates and activates the p34cdc2 kinase in vitro. We conclude that the pyp3 PTPase acts cooperatively with p80cdc25 to dephosphorylate Tyr15 of p34cdc2.","authors":"Millar JB, Lenaers G, Russell P","authors_abbrev":"Millar JB et al.","pubmed_publication_date":"Dec 1992","pubmed_entrez_date":"1992-12-01","publication_year":"1992","canto_session_key":"abf32a065b08bcd5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-05-25 12:18:11","canto_approved_date":"2021-02-25 17:03:16","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2013-01-30 11:15:01","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPCC18B5.03","SPAC26F1.10c","SPBC11B10.09","SPAC644.06c","SPAC19D5.01","SPAC11E3.09"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2018-05-25"},{"uniquename":"PMID:7010087","title":"[Variability of a distant hybrid produced as a result of crossing Saccharomyces cerevisiae with Schizosaccharomyces pombe].","citation":"Mikrobiologiia 1980;49(6):1003-5","abstract":"","authors":"Kosikov KV","authors_abbrev":"Kosikov KV","pubmed_publication_date":"1980","pubmed_entrez_date":"1980-11-01","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32432970","title":"Roles of Mso1 and the SM protein Sec1 in efficient vesicle fusion during fission yeast cytokinesis.","citation":"Mol Biol Cell 2020 Jul 15;31(15):1570-1583","abstract":"Membrane trafficking during cytokinesis is essential for the delivery of membrane lipids and cargoes to the division site. However, the molecular mechanisms are still incompletely understood. In this study, we demonstrate the importance of uncharacterized fission yeast proteins Mso1 and Sec1 in membrane trafficking during cytokinesis. Fission yeast Mso1 shares homology with budding yeast Mso1 and human Mint1, proteins that interact with Sec1/Munc18 family proteins during vesicle fusion. Sec1/Munc18 proteins and their interactors are important regulators of SNARE complex formation during vesicle fusion. The roles of these proteins in vesicle trafficking during cytokinesis have been barely studied. Here, we show that fission yeast Mso1 is also a Sec1-binding protein and Mso1 and Sec1 localize to the division site interdependently during cytokinesis. The loss of Sec1 localization in  mso1Δ  cells results in a decrease in vesicle fusion and cytokinesis defects such as slow ring constriction, defective ring disassembly, and delayed plasma membrane closure. We also find that Mso1 and Sec1 may have functions independent of the exocyst tethering complex on the plasma membrane at the division site. Together, Mso1 and Sec1 play essential roles in regulating vesicle fusion and cargo delivery at the division site during cytokinesis.","doi":"10.1091/mbc.E20-01-0067","authors":"Gerien KS, Zhang S, Russell AC, Zhu YH, Purde V, Wu JQ","authors_abbrev":"Gerien KS et al.","pubmed_publication_date":"15 Jul 2020","pubmed_entrez_date":"2020-05-21","publication_year":"2020","canto_session_key":"866dd74b90f43e98","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-05-22 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14970648","title":"Analysis of the fission yeast Schizosaccharomyces pombe cell cycle.","citation":"Methods Mol Biol 2004;241:93-111","abstract":"","authors":"Gómez EB, Forsburg SL","authors_abbrev":"Gómez EB et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-02-19","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30388401","title":"Causative Mutations and Mechanism of Androgenetic Hydatidiform Moles.","citation":"Am J Hum Genet 2018 Nov 01;103(5):740-751","abstract":"Androgenetic complete hydatidiform moles are human pregnancies with no embryos and affect 1 in every 1,400 pregnancies. They have mostly androgenetic monospermic genomes with all the chromosomes originating from a haploid sperm and no maternal chromosomes. Androgenetic complete hydatidiform moles were described in 1977, but how they occur has remained an open question. We identified bi-allelic deleterious mutations in MEI1, TOP6BL/C11orf80, and REC114, with roles in meiotic double-strand breaks formation in women with recurrent androgenetic complete hydatidiform moles. We investigated the occurrence of androgenesis in Mei1-deficient female mice and discovered that 8% of their oocytes lose all their chromosomes by extruding them with the spindles into the first polar body. We demonstrate that Mei1 -/-  oocytes are capable of fertilization and 5% produce androgenetic zygotes. Thus, we uncover a meiotic abnormality in mammals and a mechanism for the genesis of androgenetic zygotes that is the extrusion of all maternal chromosomes and their spindles into the first polar body.","doi":"10.1016/j.ajhg.2018.10.007","authors":"Nguyen NMP, Ge ZJ, Reddy R, Fahiminiya S, Sauthier P, Bagga R, Sahin FI, Mahadevan S, Osmond M, Breguet M, Rahimi K, Lapensee L, Hovanes K, Srinivasan R, Van den Veyver IB, Sahoo T, Ao A, Majewski J, Taketo T, Slim R","authors_abbrev":"Nguyen NMP et al.","pubmed_publication_date":"01 Nov 2018","pubmed_entrez_date":"2018-11-03","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC21B10.12"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22841486","title":"A central coupler for recombination initiation linking chromosome architecture to S phase checkpoint.","citation":"Mol Cell 2012 Sep 14;47(5):722-33","abstract":"Higher-order chromosome structure is assumed to control various DNA-templated reactions in eukaryotes. Meiotic chromosomes implement developed structures called \"axes\" and \"loops\"; both are suggested to tether each other, activating Spo11 to catalyze meiotic DNA double-strand breaks (DSBs) at recombination hotspots. We found that the Schizosaccharomyces pombe Spo11 homolog Rec12 and its partners form two distinct subcomplexes, DSBC (Rec6-Rec12-Rec14) and SFT (Rec7-Rec15-Rec24). Mde2, whose expression is strictly regulated by the replication checkpoint, interacts with Rec15 to stabilize the SFT subcomplex and further binds Rec14 in DSBC. Rec10 provides a docking platform for SFT binding to axes and can partially interact with DSB sites located in loops depending upon Mde2, which is indicative of the formation of multiprotein-based tethered axis-loop complex. These data lead us to propose a mechanism by which Mde2 functions as a recombination initiation mediator to tether axes and loops, in liaison with the meiotic replication checkpoint.","doi":"10.1016/j.molcel.2012.06.023","authors":"Miyoshi T, Ito M, Kugou K, Yamada S, Furuichi M, Oda A, Yamada T, Hirota K, Masai H, Ohta K","authors_abbrev":"Miyoshi T et al.","pubmed_publication_date":"14 Sep 2012","pubmed_entrez_date":"2012-07-31","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC32F12.02","SPAC17A5.11","SPBC1711.14","SPCC1753.03c","SPBC21B10.12","SPAC1952.15c","SPBC31F10.08","SPAC25G10.04c"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:15020842","title":"Resisting arrest: recovery from checkpoint arrest through dephosphorylation of Chk1 by PP1.","citation":"Cell Cycle 2004 May;3(5):529-33","abstract":"The G2 DNA damage checkpoint prevents mitotic entry in the presence of damaged DNA, and thus is essential for cells to replicate with stable genetic inheritance. Whilst significant progress has been made in the past 10 years on the mechanism of checkpoint activation, little attention has been paid to how the DNA damage checkpoint is switched off to allow cell cycle re-entry. Insight into the mechanism of cell cycle re-entry was recently provided by our finding that the Schizosaccharomyces pombe type 1 phosphatase (PP1) Dis2 dephosphorylates the checkpoint effector kinase Chk1. This occurs on a site phosphorylated by the ATR homologue Rad3 in response to DNA damage, and results in Chk1 inactivation and checkpoint release. Here we discuss the implications of this finding on DNA damage checkpoint signaling, and speculate on models for checkpoint maintenance and release.","authors":"den Elzen N, Kosoy A, Christopoulos H, O'Connell MJ","authors_abbrev":"den Elzen N et al.","pubmed_publication_date":"May 2004","pubmed_entrez_date":"2004-03-17","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17895368","title":"Schizosaccharomyces pombe protein phosphatase 1 in mitosis, endocytosis and a partnership with Wsh3/Tea4 to control polarised growth.","citation":"J Cell Sci 2007 Oct 15;120(Pt 20):3589-601","abstract":"PP1 holoenzymes are composed of a small number of catalytic subunits and an array of regulatory, targeting, subunits. The Schizosaccharomyces pombe genome encodes two highly related catalytic subunits, Dis2 and Sds21. The gene for either protein can be individually deleted, however, simultaneous deletion of both is lethal. We fused enhanced green fluorescent protein (EGFP) coding sequences to the 5' end of the endogenous sds21(+) and dis2(+) genes. Dis2.NEGFP accumulated in nuclei, associated with centromeres, foci at cell tips and endocytic vesicles. This actin-dependent endocytosis occurred between nuclei and growing tips and was polarised towards growing tips. When dis2(+) was present, Sds21.NEGFP was predominantly a nuclear protein, greatly enriched in the nucleolus. When dis2(+) was deleted, Sds21.NEGFP levels increased and Sds21.NEGFP was then clearly detected at centromeres, endocytic vesicles and cell tips. Dis2.NEGFP was recruited to cell tips by the formin binding, stress pathway scaffold Wsh3 (also known as Tea4). Wsh3/Tea4 modulates polarised tip growth in unperturbed cell cycles and governs polarised growth following osmotic stress. Mutating the PP1 recruiting RVXF motif in Wsh3/Tea4 blocked PP1 binding, altered cell cycle regulated growth to induce branching, induced branching from existing tips in response to stress, and blocked the induction of actin filaments that would otherwise arise from Wsh3/Tea4 overproduction.","authors":"Alvarez-Tabarés I, Grallert A, Ortiz JM, Hagan IM","authors_abbrev":"Alvarez-Tabarés I et al.","pubmed_publication_date":"15 Oct 2007","pubmed_entrez_date":"2007-09-27","publication_year":"2007","canto_session_key":"7e515ab57f64e77b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-03 09:39:14","canto_approved_date":"2020-06-22 15:07:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-03 09:38:57","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC15A10.16","SPAC6G10.02c","SPAC688.11","SPAC18G6.15","SPBC776.02c","SPAC3C7.12","SPAC6G9.06c","SPCC31H12.05c","SPBC336.12c","SPBC1706.01","SPCC1223.06","SPAC2F7.03c","SPAC1687.20c","SPAC3G9.12","SPBC1604.20c"],"gene_count":16,"ltp_gene_count":10,"approved_date":"2015-02-03"},{"uniquename":"PMID:8104396","title":"Mating of the fission yeast occurs independently of pmd1+ gene product, a structural homologue of budding yeast STE6 and mammalian P-glycoproteins.","citation":"Arch Microbiol 1993;160(2):162-5","abstract":"The pmd1+, a multidrug resistance gene of the fission yeast Schizosaccharomyces pombe, encodes a protein similar to the budding yeast Saccharomyces cerevisiae STE6 gene product and mammalian P-glycoproteins. The STE6 protein is a membrane transporter of a-factor, a mating pheromone of a-type S. cerevisiae, which is structurally related to M-factor of the fission yeast. However, heterothallic or homothallic pmd1 null mutant cells of S. pombe, which were constructed by means of gene disruption, showed no significant decrease in the mating abilities. On the other hand, the multidrug resistance conferred by the pmd1+ was overcome by the treatment with verapamil, a typical inhibitor of mammalian P-glycoproteins. These results indicate that the pmd1+ gene product is functionally similar to mammalian P-glycoproteins, rather than to the budding yeast STE6.","authors":"Nishi K, Yoshida M, Horinouchi S, Beppu T","authors_abbrev":"Nishi K et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_session_key":"8647733c62a91a35","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-07-31 16:08:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-07-31 16:08:09","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC663.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-07-31"},{"uniquename":"PMID:10373564","title":"Defects in components of the proteasome enhance transcriptional silencing at fission yeast centromeres and impair chromosome segregation.","citation":"Mol Cell Biol 1999 Jul;19(7):5155-65","abstract":"Fission yeast centromeres are transcriptionally silent and form a heterochromatin-like structure essential for normal centromere function; this appears analogous to heterochromatin and position effect variegation in other eukaryotes. Conditional mutations in three genes designated cep (centromere enhancer of position effect) were found to enhance transcriptional silencing within centromeres. Cloning of the cep1(+) and cep2(+) genes by functional complementation revealed that they are identical to the previously described genes pad1(+) and mts2(+), respectively, which both encode subunits of the proteasome 19S cap. Like Mts2 and Mts4, epitope-tagged Cep1/Pad1 localizes to or near the nuclear envelope throughout the cell cycle. The cep mutants display a range of phenotypes depending on the temperature. Silencing within the central domain of centromeres is increased at 36 degrees C. This suggests that the proteasome is involved in regulating silencing and thus centromeric chromatin architecture, possibly by lowering the level of some chromatin-associated protein by ubiquitin-dependent degradation. This is the first report of defective proteasome function affecting heterochromatin-mediated transcriptional silencing. At 36 and 32 degrees C, the cep mutants lose chromosomes at an elevated rate, and at 18 degrees C, the mutants are cryosensitive for growth. Cytological analysis at 18 degrees C revealed a defect in sister chromatid separation while other mitotic events occurred normally, indicating that cep mutations might interfere specifically with the degradation of inhibitor(s) of sister chromatid separation. These observations suggest that 19S subunits confer a level of substrate specificity on the proteasome and raise the possibility of a link between components involved in centromere architecture and sister chromatid cohesion.","authors":"Javerzat JP, McGurk G, Cranston G, Barreau C, Bernard P, Gordon C, Allshire R","authors_abbrev":"Javerzat JP et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-06-22","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19171118","title":"Proline 146 is critical to the structure, function and targeting of sod2, the Na+/H+ exchanger of Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2009 May;1788(5):983-92","abstract":"Sod2 is the Na(+)/H(+) exchanger of the fission yeast Schizosaccharomyces pombe that is principally responsible for salt tolerance. We examined the role of nine polar, membrane associated amino acids in the ability of the protein to confer salt tolerance in S. pombe. Wild type sod2 protein with a C-terminal GFP tag effectively rescued salt tolerance in S. pombe with deleted endogenous sod2. Sod2 protein with the mutations P163A, P183A, D298N, D389N, E390Q, E392Q and E397Q also conveyed salt tolerance as effectively as the wild type sod2 protein. In contrast, the mutation P146A resulted in a protein that did not convey salt tolerance nearly as effectively as the wild type and did not extrude Na(+) as well as the wild type. Mutation of Pro(146) to Ser, Asp or Lys had an intermediate effect. Mutation of Thr(142) to Ser resulted in a slightly defective protein. Western blot analysis showed that all mutant proteins were expressed at similar levels as wild type sod2 protein. Examination of the localization of the proteins showed that wild type and most sod2 mutants were present in the plasma membrane while the P146A mutant had an intracellular localization. Limited tryptic digestion suggested that the P146A sod2 protein had a change in conformation in comparison to the wild type protein. The results suggest that Pro(146) is an amino acid critical to sod2 structure, function and localization.","doi":"10.1016/j.bbamem.2009.01.001","authors":"Ndayizeye M, Touret N, Fliegel L","authors_abbrev":"Ndayizeye M et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-01-28","publication_year":"2009","canto_session_key":"881f48fa75b1371a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 13:52:18","canto_approved_date":"2022-06-14 15:28:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-12-01 14:37:31","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":63,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC977.10"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-31"},{"uniquename":"PMID:11554922","title":"Bir1/Cut17 moving from chromosome to spindle upon the loss of cohesion is required for condensation, spindle elongation and repair.","citation":"Genes Cells 2001 Sep;6(9):743-63","abstract":"In mammals, proteins containing BIR domains (IAPs and survivin) are implicated in inhibiting apoptosis and sister chromatid separation. In the nematode, Bir1 is required for a proper localization of aurora kinase, which moves from the mitotic chromosome in metaphase to the spindle midzone in anaphase as a passenger. Fission yeast Bir1/Pbh1 is essential for normal mitosis.\nA temperature sensitive mutant cut17-275 exhibits the defect in condensation and spindle elongation at 36 degrees C, while securin is degraded. Gene cloning shows that the cut17+ gene is identical to bir1+/pbh1+. At 26 degrees C, cut17-275 is UV sensitive as the repair of DNA damage is severely compromised. Bir1/Cut17 is a nuclear protein in interphase, which is then required for recruiting condensin to the mitotic nucleus, and concentrates to form a discrete number of dots from prometaphase to metaphase. Once the chromatids are separated, Bir1/Cut17 no longer binds to kinetochores and instead moves to the middle of spindle. Chromatin immunoprecipitation suggested that Bir1/Cut17 associates with the outer repetitious centromere region in metaphase. Following the initiation of anaphase the protein switches from being a chromosomal protein to a spindle protein. This transit is stringently regulated by the state of sister chromatid cohesion proteins Mis4 and Rad21. Ark1, is an aurora kinase homologue whose mitotic distribution is identical to, and under the control of Bir1/Cut17.\nBir1/Cut17 and Ark1 act as \"passengers\" but they may play a main role as a recruitment factor, essential for condensation, spindle elongation and DNA repair. Bir1/Cut17 should have roles both in mitotic and in interphase chromosome. The proper location of Ark1 requires Bir1/Cut17, and the mitotic localization of Bir1/Cut17 requires sister cohesion.","authors":"Morishita J, Matsusaka T, Goshima G, Nakamura T, Tatebe H, Yanagida M","authors_abbrev":"Morishita J et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-09-14","publication_year":"2001","canto_session_key":"f79afeafbdf2d0ec","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-08-18 11:18:14","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-08-18 11:18:02","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":59,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPCC306.03c","SPCC962.02c","SPBC14C8.01c","SPBC146.03c","SPCC320.13c","SPCC338.17c"],"gene_count":7,"ltp_gene_count":4,"approved_date":"2015-08-18"},{"uniquename":"PMID:19563121","title":"Cell-cycle synchrony for analysis of S. pombe DNA replication.","citation":"Methods Mol Biol 2009;521:437-48","abstract":"Analysis of S phase events requires the ability to synchronize the cell cycle for subsequent physiological or molecular analysis. The cell cycle can be arrested at different stages, using drugs or temperature-sensitive mutations, and then released (block and release). These methods offer high levels of synchrony. Synchrony is lower in methods that fractionate the cells (lactose gradient synchrony), which avoids any cell-cycle perturbation. The degree of synchronization is assessed by monitoring cell morphology or DNA content. The choice of method is influenced by the needs of the experiment and the requirements of any mutations already in the strain of interest.","doi":"10.1007/978-1-60327-815-7_24","authors":"Luche DD, Forsburg SL","authors_abbrev":"Luche DD et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-07-01","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18387623","title":"Fabrication of highly insulating tethered bilayer lipid membrane using yeast cell membrane fractions for measuring ion channel activity.","citation":"J Colloid Interface Sci 2008 Jun 15;322(2):465-72","abstract":"A tethered bilayer lipid membrane (tBLM) was fabricated on a gold electrode using 1,2-dipalmitoyl-sn-glycero-phosphothioethanol as a tethering lipid and the membrane fractions of Saccharomyces pombe yeast cells to deposit the upper leaflet. The membrane fractions were characterized using transmission electron microscopy and dynamic light scattering and found to be similar in size to small unilamellar vesicles of synthetic lipids. The dynamics of membrane-fraction deposition and rupture on the tethering-lipid layer were measured using quartz crystal microgravimetry. The electrochemical properties of the resulting tBLM were characterized using electrical impedance spectroscopy and cyclic voltammetry. The tBLM's electrical resistance was greater than 1 MOmegacm(2), suggesting a defect-free membrane. The suitability of tBLM produced using membrane fractions for measuring ion-channel activities was shown by a decrease in membrane resistance from 1.6 to 0.43 MOmegacm(2) following addition of gramicidin. The use of membrane fractions to form high-quality tBLM on gold electrodes suggests a new approach to characterize membrane proteins, in which the upper leaflet of the tBLM is deposited, and overexpressed membrane proteins are incorporated, in a single step. This approach would be especially useful for proteins whose activity is lost or altered during extraction, purification, and reconstitution, or whose activities are strongly influenced by the lipid composition of the bilayer.","doi":"10.1016/j.jcis.2008.02.064","authors":"Jadhav SR, Sui D, Garavito RM, Worden RM","authors_abbrev":"Jadhav SR et al.","pubmed_publication_date":"15 Jun 2008","pubmed_entrez_date":"2008-04-05","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12578838","title":"The Schizosaccharomyces pombe Cuf1 is composed of functional modules from two distinct classes of copper metalloregulatory transcription factors.","citation":"J Biol Chem 2003 Apr 18;278(16):14565-77","abstract":"In fission yeast, the genes encoding proteins that are components of the copper transporter family are controlled at the transcriptional level by the Cuf1 transcription factor. Under low copper availability, Cuf1 induces expression of the copper transporter genes. In contrast, sufficient levels of copper inactivate Cuf1 and expression of its target genes. Our study reveals that Cuf1 harbors a putative copper-binding motif, Cys-X-Cys-X(3)-Cys-X-Cys-X(2)-Cys-X(2)-His, within its carboxyl-terminal region to sense changing environmental copper levels. Binding studies reveal that the amino-terminal 174-residue segment of Cuf1 expressed as a fusion protein in Escherichia coli specifically interacts with the cis-acting copper transporter promoter element CuSE (copper-signaling element). Within this region, the first 61 amino acids of Cuf1 exhibit more overall homology to the Saccharomyces cerevisiae Ace1 copper-detoxifying factor (from residues 1 to 63) than to Mac1, its functional ortholog. Consistently, we demonstrate that a chimeric Cuf1 protein bearing the amino-terminal 63-residue segment of Ace1 complements cuf1 Delta null phenotypes. Furthermore, we show that Schizosaccharomyces pombe cuf1Delta mutant cells expressing the full-length S. cerevisiae Ace1 protein are hypersensitive to copper ions, with a concomitant up-regulation of CuSE-mediated gene expression in fission yeast. Taken together, these studies reveal that S. cerevisiae Ace1 1-63 is functionally exchangeable with S. pombe Cuf1 1-61, and the nature of the amino acids located downstream of this amino-terminal conserved region may be crucial in dictating the type of regulatory response required to establish and maintain copper homeostasis.","authors":"Beaudoin J, Mercier A, Langlois R, Labbé S","authors_abbrev":"Beaudoin J et al.","pubmed_publication_date":"18 Apr 2003","pubmed_entrez_date":"2003-02-13","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1393.10","SPAC31A2.11c"],"gene_count":2,"ltp_gene_count":1},{"uniquename":"EMBL:AJ632001","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.36"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7613861","title":"The cell cycle and suc1: from structure to function?","citation":"Structure 1995 Apr 15;3(4):321-5","abstract":"Structures have recently been determined for the yeast Schizosaccharomyces pombe cell cycle regulatory protein, CKS/suc1, and its human equivalent. The structures provide some long-awaited clues about the role of CKS/suc1 in cell cycle control.","authors":"Endicott JA, Nurse P","authors_abbrev":"Endicott JA et al.","pubmed_publication_date":"15 Apr 1995","pubmed_entrez_date":"1995-04-15","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17072880","title":"Tools and resources for Sz. pombe: a report from the 2006 European Fission Yeast Meeting.","citation":"Yeast 2006 Oct 15;23(13):901-3","abstract":"Schizosaccharomyces pombe has always suffered from a relative paucity of tools and resources, particularly when compared to Saccharomyces cerevisiae. The European Fission Yeast Meeting, held in March 2006, brought together a significant proportion of the Sz. pombe research community, so it was an ideal opportunity to hold a discussion session on the future needs of those working on this model organism. While the session generated a consensus on the most essential requirements, it also demonstrated the frustrations and concerns of those working with Sz. pombe. The community was also briefed regarding the future transition of the current database (Sz. pombe GeneDB) to a fully-fledged Model Organism Database (MOD) to support the needs of both fission yeast and the broader scientific community.","authors":"Wixon J, Wood V","authors_abbrev":"Wixon J et al.","pubmed_publication_date":"15 Oct 2006","pubmed_entrez_date":"2006-10-31","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24196444","title":"Mal3, the Schizosaccharomyces pombe homolog of EB1, is required for karyogamy and for promoting oscillatory nuclear movement during meiosis.","citation":"Cell Cycle 2014;13(1):72-7","abstract":"Two successive rounds of chromosome segregation following a single round of DNA replication enable the production of haploid gametes during meiosis. In the fission yeast Schizosaccharomyces pombe, karyogamy is the process where the nuclei from 2 haploid cells fuse to create a diploid nucleus, which then undergoes meiosis to produce 4 haploid spores. By screening a collection of S. pombe deletion strains, we found that the deletion of 2 genes, mal3 and mto1, leads to the production of asci containing up to 8 spores. Here, we show that Mal3, the fission yeast member of the EB1 family of conserved microtubule plus-end tracking proteins, is required for karyogamy, oscillatory nuclear movement, and proper segregation of chromosomes during meiosis. In the absence of Mal3, meiosis frequently initiates before the completion of karyogamy, thus producing up to 8 nuclei in a single ascus. Our results provide new evidence that fission yeast can initiate meiosis prior to completing karyogamy.","doi":"10.4161/cc.26815","authors":"Polakova S, Benko Z, Zhang L, Gregan J","authors_abbrev":"Polakova S et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2013-11-08","publication_year":"2014","canto_session_key":"5407743d150ff7e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silvia Polakova","canto_first_approved_date":"2015-04-29 08:33:04","canto_approved_date":"2026-04-05 07:44:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-01 12:09:42","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Silvia Polakova","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC417.07c","SPAC18G6.15"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-04-29"},{"uniquename":"PMID:22747640","title":"Conserved rules govern genetic interaction degree across species.","citation":"Genome Biol 2012 Jul 02;13(7):R57","abstract":"Synthetic genetic interactions have recently been mapped on a genome scale in the budding yeast Saccharomyces cerevisiae, providing a functional view of the central processes of eukaryotic life. Currently, comprehensive genetic interaction networks have not been determined for other species, and we therefore sought to model conserved aspects of genetic interaction networks in order to enable the transfer of knowledge between species.\nUsing a combination of physiological and evolutionary properties of genes, we built models that successfully predicted the genetic interaction degree of S. cerevisiae genes. Importantly, a model trained on S. cerevisiae gene features and degree also accurately predicted interaction degree in the fission yeast Schizosaccharomyces pombe, suggesting that many of the predictive relationships discovered in S. cerevisiae also hold in this evolutionarily distant yeast. In both species, high single mutant fitness defect, protein disorder, pleiotropy, protein-protein interaction network degree, and low expression variation were significantly predictive of genetic interaction degree. A comparison of the predicted genetic interaction degrees of S. pombe genes to the degrees of S. cerevisiae orthologs revealed functional rewiring of specific biological processes that distinguish these two species. Finally, predicted differences in genetic interaction degree were independently supported by differences in co-expression relationships of the two species.\nOur findings show that there are common relationships between gene properties and genetic interaction network topology in two evolutionarily distant species. This conservation allows use of the extensively mapped S. cerevisiae genetic interaction network as an orthology-independent reference to guide the study of more complex species.","doi":"10.1186/gb-2012-13-7-r57","authors":"Koch EN, Costanzo M, Bellay J, Deshpande R, Chatfield-Reed K, Chua G, D'Urso G, Andrews BJ, Boone C, Myers CL","authors_abbrev":"Koch EN et al.","pubmed_publication_date":"02 Jul 2012","pubmed_entrez_date":"2012-07-04","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18000002","title":"The BioGRID Interaction Database: 2008 update.","citation":"Nucleic Acids Res 2008 Jan;36(Database issue):D637-40","abstract":"The Biological General Repository for Interaction Datasets (BioGRID) database (http://www.thebiogrid.org) was developed to house and distribute collections of protein and genetic interactions from major model organism species. BioGRID currently contains over 198 000 interactions from six different species, as derived from both high-throughput studies and conventional focused studies. Through comprehensive curation efforts, BioGRID now includes a virtually complete set of interactions reported to date in the primary literature for both the budding yeast Saccharomyces cerevisiae and the fission yeast Schizosaccharomyces pombe. A number of new features have been added to the BioGRID including an improved user interface to display interactions based on different attributes, a mirror site and a dedicated interaction management system to coordinate curation across different locations. The BioGRID provides interaction data with monthly updates to Saccharomyces Genome Database, Flybase and Entrez Gene. Source code for the BioGRID and the linked Osprey network visualization system is now freely available without restriction.","authors":"Breitkreutz BJ, Stark C, Reguly T, Boucher L, Breitkreutz A, Livstone M, Oughtred R, Lackner DH, Bähler J, Wood V, Dolinski K, Tyers M","authors_abbrev":"Breitkreutz BJ et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-11-15","publication_year":"2008","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9562621","title":"Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3.","citation":"J Biochem 1998 May;123(5):883-90","abstract":"Saccharomyces cerevisiae Dis3p, which interacts with Ran/Gsp1p, complements Schizosaccharomyces pombe dis3-54. Consistent with the functional conservation of Dis3p in S. cerevisiae and S. pombe, the human ORF (accession number: R27667) was found to be highly homologous to yeast Dis3p. Based on its nucleotide sequence, we cloned a full-sized human DIS3 cDNA. The cloned human cDNA partly but significantly restored the temperature-sensitivity of S. cerevisiae dis3. Thus, Dis3p was found to be structurally and functionally conserved from yeast to mammals. Consistent with the report that S. cerevisiae Dis3p is identical to Rrp44p, which comprises the exosome involved in ribosomal RNA processing, S. cerevisiae Dis3p was found to be localized in the nucleolus. Similar to S. cerevisiae Dis3p, human Dis3p enhanced RCC1-stimulated nucleotide release from Ran, in a dose-dependent manner, and bound to GTP- or GDP-Ran.","authors":"Shiomi T, Fukushima K, Suzuki N, Nakashima N, Noguchi E, Nishimoto T","authors_abbrev":"Shiomi T et al.","pubmed_publication_date":"May 1998","pubmed_entrez_date":"1998-06-19","publication_year":"1998","canto_session_key":"a8028fb1543db88d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 16:37:09","canto_session_submitted_date":"2012-03-03 16:36:54","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC26H8.10"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:7502067","title":"The centromere: hub of chromosomal activities.","citation":"Science 1995 Dec 08;270(5242):1591-4","abstract":"Centromeres are the structures that direct eukaryotic chromosome segregation in mitosis and meiosis. There are two major classes of centromeres. Point centromeres, found in the budding yeasts, are compact loci whose constituent proteins are now beginning to yield to biochemical analysis. Regional centromeres, best described in the fission yeast Schizosaccharomyces pombe, encompass many kilobases of DNA and are packaged into heterochromatin. Their associated proteins are as yet poorly understood. In addition to providing the site for microtubule attachment, centromeres also have an important role in checkpoint regulation during mitosis.","authors":"Pluta AF, Mackay AM, Ainsztein AM, Goldberg IG, Earnshaw WC","authors_abbrev":"Pluta AF et al.","pubmed_publication_date":"08 Dec 1995","pubmed_entrez_date":"1995-12-08","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16175211","title":"Stress-dependent regulation of a monothiol glutaredoxin gene from Schizosaccharomyces pombe.","citation":"Can J Microbiol 2005 Jul;51(7):613-20","abstract":"Glutaredoxin (Grx) is a small, heat-stable protein acting as a multi-functional glutathione-dependent disulfide oxidoreductase. In this work, a gene encoding the monothiol glutaredoxin Grx4 was cloned from the genomic DNA of the fission yeast Schizosaccharomyces pombe. The determined DNA sequence carries 1706 bp, which is able to encode the putative 244 amino acid sequence of Grx with 27 099 Da. It does not contain an intron, and the sequence CGFS is found in the active site. Grx activity was increased 1.46-fold in S. pombe cells harboring the cloned Grx4 gene, indicating that the Grx4 gene is in vivo functioning. Although aluminum, cadmium, and hydrogen peroxide marginally enhanced the synthesis of beta-galactosidase from the Grx4-lacZ fusion gene, NO-generating sodium nitroprusside (0.5 mmol/L and 1.0 mmol/L) and potassium chloride (0.2 mol/L and 0.5 mol/L) significantly enhanced it. The Grx4 mRNA level was also enhanced after the treatment with sodium nitroprusside and potassium chloride. The synthesis of beta-galactosidase from the Grx4-lacZ gene was increased by fermentable carbon sources, such as glucose (lower than 2%) and sucrose, but not by nonfermentable carbon sources such as acetate and ethanol. The basal expression of the S. pombe Grx4 gene did not depend on the presence of Pap1. These results imply that the S. pombe monothiol Grx4 gene is genuinely functional and regulated by a variety of stresses.","authors":"Kim HG, Kim BC, Park EH, Lim CJ","authors_abbrev":"Kim HG et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-09-22","publication_year":"2005","canto_session_key":"b6a5d15f66e77ab4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-11-07 11:31:03","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-11-06 10:50:16","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.06","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-11-06"},{"uniquename":"PMID:3782042","title":"Malate transport in Schizosaccharomyces pombe.","citation":"J Bacteriol 1986 Dec;168(3):1439-43","abstract":"The transport of malate was studied in a Schizosaccharomyces pombe wild-type strain and in mutant strains unable to utilize malic acid. Two groups of such mutants, i.e., malic enzyme-deficient and malate transport-defective mutants, were differentiated by a 14C-labeled L-malate transport assay and by starch gel electrophoresis followed by activity staining for malic enzyme (malate dehydrogenase [oxaloacetate decarboxylating] [NAD+]; 1.1.1.38) and malate dehydrogenase (1.1.1.37). Transport of malate in S. pombe was constitutive and strongly inhibited by inhibitors of oxidative phosphorylation and of the formulation of proton gradients. Transport was a saturable function of the malate concentration. The apparent Km and Vmax values for transport by the parent were 3.7 mM and 40 nmol/min per mg of protein, respectively, while those of the malic enzyme-deficient mutant were 5.7 mM and 33 nmol/min per mg of protein, respectively. Malate transport was pH and temperature dependent. The specificity of transport was studied with various substrates, including mono- and dicarboxylic acids, and the possibility of a common transport system for dicarboxylic acids is discussed.","authors":"Osothsilp C, Subden RE","authors_abbrev":"Osothsilp C et al.","pubmed_publication_date":"Dec 1986","pubmed_entrez_date":"1986-12-01","publication_year":"1986","canto_session_key":"d64a3c20bbe7fd3c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-12-08 22:53:30","canto_approved_date":"2022-02-07 17:10:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-08 22:53:21","canto_added_date":"2012-02-24 05:55:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB8E5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-12-08"},{"uniquename":"PMID:26890608","title":"A functional genome-wide genetic screening identifies new pathways controlling the G1/S transcriptional wave.","citation":"Cell Cycle 2016;15(5):720-9","abstract":"The Schizosaccharomyces pombe MBF complex activates the transcription of genes required for DNA synthesis and S phase. The MBF complex contains several proteins, including the core components Cdc10, Res1 and Res2, the co-repressor proteins Yox1 and Nrm1 and the co-activator Rep2. It has recently been shown how MBF is regulated when either the DNA damage or the DNA synthesis checkpoints are activated. However, how MBF is regulated in a normal unperturbed cell cycle is still not well understood. We have set up a genome-wide genomic screen searching for global regulators of MBF. We have crossed our knock-out collection library with a reporter strain that allows the measurement of MBF activity in live cells by flow cytometry. We confirm previously known regulators of MBF and show that COP9/signalosome and tRNA methyltransferases also regulate MBF activity.","doi":"10.1080/15384101.2016.1148839","authors":"Gaspa L, González-Medina A, Hidalgo E, Ayté J","authors_abbrev":"Gaspa L et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-02-19","publication_year":"2016","canto_session_key":"4e4a8605a4b1fccb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-03-15 09:47:51","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-03-03 10:03:59","canto_added_date":"2016-02-20 01:15:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":66,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC10F6.13c","SPBC365.14c","SPAC17H9.10c","SPAC16E8.01","SPAPB17E12.04c","SPAC23C4.11","SPAC6G10.06","SPAC22F3.09c","SPAC4F10.13c","SPBC3H7.10","SPAC1071.02","SPBC19G7.06","SPAC14C4.09","SPAC12G12.13c","SPAC29B12.03","SPBC216.05","SPBC36.07","SPAC13D6.03c","SPCC162.11c","SPBC30B4.04c","SPBC3B8.03","SPBC2F12.11c","SPBC24C6.10c","SPAC26A3.06","SPBC19G7.10c","SPCC126.04c","SPBC21B10.13c","SPBC16D10.02","SPBC725.16","SPAC1250.03","SPBC215.03c","SPAC1783.04c","SPBC337.03","SPAPB17E12.05","SPAC17H9.19c","SPAC17A5.14","SPCC18B5.11c","SPBC16G5.15c","SPAC30.02c","SPBC3E7.15c","SPCC74.05","SPAPB1E7.06c","SPAC30D11.10","SPAC31A2.02","SPAC25G10.06","SPBC106.20","SPCC18.01c","SPAPB1A10.15","SPBC354.12","SPAC323.05c","SPBC31E1.02c","SPCC11E10.06c","SPCC338.16","SPBC16A3.07c","SPBC3H7.07c","SPAC694.06c","SPAC26A3.07c","SPBC19C7.12c"],"gene_count":58,"ltp_gene_count":51,"approved_date":"2016-03-03"},{"uniquename":"PMID:38899862","title":"Suppression of inositol pyrophosphate toxicosis and hyper-repression of the fission yeast  PHO  regulon by loss-of-function mutations in chromatin remodelers Snf22 and Sol1.","citation":"mBio 2024 Jun 20;:e0125224","abstract":"Inositol pyrophosphates are signaling molecules that regulate cellular phosphate homeostasis in eukaryal taxa. In fission yeast, where the phosphate regulon (comprising phosphate acquisition genes  pho1 ,  pho84 , and  tgp1 ) is repressed under phosphate-replete conditions by lncRNA-mediated transcriptional interference, mutations of inositol pyrophosphatases that increase IP 8  levels derepress the  PHO  regulon by eliciting precocious termination of lncRNA transcription. Asp1 pyrophosphatase mutations resulting in too much IP 8  are cytotoxic in YES medium owing to overexpression of glycerophosphodiester transporter Tgp1. IP 8  toxicosis is ameliorated by mutations in cleavage/polyadenylation and termination factors, perturbations of the Pol2 CTD code, and mutations in SPX domain proteins that act as inositol pyrophosphate sensors. Here, we show that IP 8  toxicity is alleviated by deletion of  snf22  + , the gene encoding the ATPase subunit of the SWI/SNF chromatin remodeling complex, by an ATPase-inactivating  snf22- ( D996A-E997A ) allele, and by deletion of the gene encoding SWI/SNF subunit Sol1. Deletion of  snf22 +   hyper-repressed  pho1  expression in phosphate-replete cells; suppressed the  pho1  derepression elicited by mutations in Pol2 CTD, termination factor Seb1, Asp1 pyrophosphatase, and 14-3-3 protein Rad24 (that favor precocious  prt  lncRNA termination); and delayed  pho1  induction during phosphate starvation. RNA analysis and lack of mutational synergies suggest that Snf22 is not impacting 3'-processing/termination. Using reporter assays, we find that Snf22 is important for the activity of the  tgp1  and  pho1  promoters, but not for the promoters that drive the synthesis of the  PHO -repressive lncRNAs. Transcription profiling of  snf22 ∆ and  snf22- ( D996A-E997A ) cells identified an additional set of 66 protein-coding genes that were downregulated in both mutants.IMPORTANCERepression of the fission yeast  PHO  genes  tgp1 ,  pho1 , and  pho84  by lncRNA-mediated interference is sensitive to inositol pyrophosphate dynamics. Cytotoxic  asp1-STF  alleles derepress the  PHO  genes via the action of IP 8  as an agonist of precocious lncRNA 3'-processing/termination. IP 8  toxicosis is alleviated by mutations of the Pol2 CTD and the 3'-processing/termination machinery that dampen the impact of toxic IP 8  levels on termination. In this study, a forward genetic screen revealed that IP 8  toxicity is suppressed by mutations of the Snf22 and Sol1 subunits of the SWI/SNF chromatin remodeling complex. Genetic and biochemical evidence indicates that the SWI/SNF is not affecting 3'-processing/termination or lncRNA promoter activity. Rather, SWI/SNF is critical for firing the  PHO  mRNA promoters. Our results implicate the ATP-dependent nucleosome remodeling activity of SWI/SNF as necessary to ensure full access of  PHO -activating transcription factor Pho7 to its binding sites in the  PHO  mRNA promoters.","doi":"10.1128/mbio.01252-24","authors":"Schwer B, Innokentev A, Sanchez AM, Garg A, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"20 Jun 2024","pubmed_entrez_date":"2024-06-20","publication_year":"2024","canto_session_key":"6339283c028dd2d6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ana M. Sanchez","canto_first_approved_date":"2024-07-23 14:48:58","canto_approved_date":"2024-07-23 14:48:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-23 14:19:08","canto_added_date":"2024-06-20 23:25:05","annotation_curators":[{"name":"Ana M. Sanchez","community_curator":true,"annotation_count":209,"orcid":"0000-0002-9119-7624","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBPB2B2.01","SPBPB21E7.11","SPCC1223.03c","SPCC757.07c","SPBC1271.07c","SPBP4G3.02","SPBC36.03c","SPCC584.16c","SPBC1683.08","SPCC1235.17","SPAC3G9.04","SPCC794.04c","SPBC337.03","SPBC29B5.02c","SPCC74.02c","SPAC2E1P3.05c","SPAC8E11.02c","SPBC1271.09","SPAC5H10.03","SPAC11D3.19","SPBC26H8.11c","SPBC1289.14","SPBPB8B6.04c","SPAC11H11.04","SPBC359.02","SPCC1235.18","SPAC110.01","SPBC359.05","SPCC1739.08c","SPBPB2B2.05","SPCC1235.14","SPBC56F2.06","SPAC1F7.08","SPBC359.06","SPCC794.12c","SPAC1F8.03c","SPBC1348.14c","SPAC19G12.17","SPAC17D4.01","SPCC548.07c","SPBC1683.09c","SPAC13G6.14","SPCC1393.13","SPBPB2B2.10c","SPBC30B4.04c","SPCC1620.14c","SPAC1A6.04c","SPAC6B12.07c","SPCC70.08c","SPCC794.01c","SPBC23G7.13c","SPBC1685.17","SPBC28F2.12","SPAC17A2.11","SPAC1039.02","SPBPB2B2.12c","SPAPB8E5.05","SPAC3C7.14c","SPCC1672.06c","SPBPB10D8.01","SPAC513.07","SPAC1F8.01","SPBC1861.02","SPAC4H3.03c","SPAC27D7.11c","SPBC4F6.09","SPAC186.05c","SPBC8E4.01c","SPBPB21E7.04c","SPCPB1C11.03","SPBP4H10.10","SPAC11E3.01c","SPBC1271.08c","SPBPB2B2.06c","SPAC222.09","SPAPB24D3.07c","SPBC8E4.12c","SPBP4H10.09","SPAC824.04","SPBPB21E7.07","SPAC15E1.02c"],"gene_count":81,"ltp_gene_count":16,"approved_date":"2024-07-23"},{"uniquename":"PMID:12473680","title":"Cleavage of model replication forks by fission yeast Mus81-Eme1 and budding yeast Mus81-Mms4.","citation":"J Biol Chem 2003 Feb 28;278(9):6928-35","abstract":"The blockage of replication forks can result in the disassembly of the replicative apparatus and reversal of the fork to form a DNA junction that must be processed in order for replication to restart and sister chromatids to segregate at mitosis. Fission yeast Mus81-Eme1 and budding yeast Mus81-Mms4 are endonucleases that have been implicated in the processing of aberrant DNA junctions formed at stalled replication forks. Here we have investigated the activity of purified Mus81-Eme1 and Mus81-Mms4 on substrates that resemble DNA junctions that are expected to form when a replication fork reverses. Both enzymes cleave Holliday junctions and substrates that resemble normal replication forks poorly or not at all. However, forks where the equivalents of either both the leading and lagging strands or just the lagging strand are juxtaposed at the junction point, or where either the leading or lagging strand has been unwound to produce a fork with a single-stranded tail, are cleaved well. Cleavage sites map predominantly between 3 and 6 bp 5' of the junction point. For most substrates the leading strand template is cleaved. The sole exception is a fork with a 5' single-stranded tail, which is cleaved in the lagging strand template.","authors":"Whitby MC, Osman F, Dixon J","authors_abbrev":"Whitby MC et al.","pubmed_publication_date":"28 Feb 2003","pubmed_entrez_date":"2002-12-11","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30297419","title":"Swi5-Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation.","citation":"Proc Natl Acad Sci U S A 2018 Oct 23;115(43):E10059-E10068","abstract":"Eukaryotic Rad51 protein is essential for homologous-recombination repair of DNA double-strand breaks. Rad51 recombinases first assemble onto single-stranded DNA to form a nucleoprotein filament, required for function in homology pairing and strand exchange. This filament assembly is the first regulation step in homologous recombination. Rad51 nucleation is kinetically slow, and several accessory factors have been identified to regulate this step. Swi5-Sfr1 (S5S1) stimulates Rad51-mediated homologous recombination by stabilizing Rad51 nucleoprotein filaments, but the mechanism of stabilization is unclear. We used single-molecule tethered particle motion experiments to show that mouse S5S1 (mS5S1) efficiently stimulates mouse RAD51 (mRAD51) nucleus formation and inhibits mRAD51 dissociation from filaments. We also used single-molecule fluorescence resonance energy transfer experiments to show that mS5S1 promotes stable nucleus formation by specifically preventing mRAD51 dissociation. This leads to a reduction of nucleation size from three mRAD51 to two mRAD51 molecules in the presence of mS5S1. Compared with mRAD51, fission yeast Rad51 (SpRad51) exhibits fast nucleation but quickly dissociates from the filament. SpS5S1 specifically reduces SpRad51 disassembly to maintain a stable filament. These results clearly demonstrate the conserved function of S5S1 by primarily stabilizing Rad51 on DNA, allowing both the formation of the stable nucleus and the maintenance of filament length.","doi":"10.1073/pnas.1812753115","authors":"Lu CH, Yeh HY, Su GC, Ito K, Kurokawa Y, Iwasaki H, Chi P, Li HW","authors_abbrev":"Lu CH et al.","pubmed_publication_date":"23 Oct 2018","pubmed_entrez_date":"2018-10-10","publication_year":"2018","canto_session_key":"9390d5b48f1d21af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hiroshi Iwasaki","canto_first_approved_date":"2019-02-05 16:16:02","canto_approved_date":"2022-09-08 08:29:02","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-02-03 09:48:57","canto_added_date":"2018-10-11 00:15:05","annotation_curators":[{"name":"Hiroshi Iwasaki","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c","SPBC28F2.07","SPBC409.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-02-05"},{"uniquename":"PMID:9325316","title":"RNA polymerase II subunits 2, 3, and 11 form a core subassembly with DNA binding activity.","citation":"J Biol Chem 1997 Oct 10;272(41):25851-5","abstract":"RNA polymerase II purified from the fission yeast Schizosaccharomyces pombe consists of 10 species of subunit polypeptide. We introduced a histidine cluster tag sequence into the chromosomal rpb1 and rpb3 genes, which encode subunit 1 (Rpb1) and subunit 3 (Rpb3), respectively, and purified the RNA polymerase by Ni2+ affinity chromatography. After stepwise dissociation of the Rpb1- and Rpb3-tagged RNA polymerases fixed on Ni2+-resin by increasing concentrations of urea or guanidium hydrochloride, Rpb2-Rpb3-Rpb11 or Rpb2-Rpb3-Rpb11-Rpb10 complexes were obtained. Since the complex consisting of Rpb2, Rpb3, and Rpb11 cannot be dissociated even after treatment with 6 M urea buffer, we propose that this complex represents a core subassembly of the RNA polymerase II, analogous to the alpha2beta complex in the assembly of Escherichia coli RNA polymerase. Both the Rpb2-Rpb3-Rpb11 complex and the free Rpb1 protein showed DNA binding activity, although the affinity was weaker compared with the intact RNA polymerase.","authors":"Kimura M, Ishiguro A, Ishihama A","authors_abbrev":"Kimura M et al.","pubmed_publication_date":"10 Oct 1997","pubmed_entrez_date":"1997-11-05","publication_year":"1997","canto_session_key":"dfb57891720b2902","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-12 06:23:31","canto_approved_date":"2025-09-02 21:21:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 06:23:22","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.03","SPBC14C8.12","SPCC1020.04c","SPBC28F2.12","SPACUNK4.06c","SPAC23G3.01","SPCC1442.10c","SPAC1B3.12c","SPAC3A12.07","SPAC23C4.15"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2018-06-12"},{"uniquename":"PMID:15369671","title":"Mis16 and Mis18 are required for CENP-A loading and histone deacetylation at centromeres.","citation":"Cell 2004 Sep 17;118(6):715-29","abstract":"Centromeres contain specialized chromatin that includes the centromere-specific histone H3 variant, spCENP-A/Cnp1. Here we report identification of five fission yeast centromere proteins, Mis14-18. Mis14 is recruited to kinetochores independently of CENP-A, and, conversely, CENP-A does not require Mis14 to associate with centromeres. In contrast, Mis15, Mis16 (strong similarity with human RbAp48 and RbAp46), Mis17, and Mis18 are all part of the CENP-A recruitment pathway. Mis15 and Mis17 form an evolutionarily conserved complex that also includes Mis6. Mis16 and Mis18 form a complex and maintain the deacetylated state of histones specifically in the central core of centromeres. Mis16 and Mis18 are the most upstream factors in kinetochore assembly as they can associate with kinetochores in all kinetochore mutants except for mis18 and mis16, respectively. RNAi knockdown in human cells shows that Mis16 function is conserved as RbAp48 and RbAp46 are both required for localization of human CENP-A.","authors":"Hayashi T, Fujita Y, Iwasaki O, Adachi Y, Takahashi K, Yanagida M","authors_abbrev":"Hayashi T et al.","pubmed_publication_date":"17 Sep 2004","pubmed_entrez_date":"2004-09-17","publication_year":"2004","canto_session_key":"6bede5008acef48c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2019-01-29 16:33:15","canto_approved_date":"2026-01-30 13:28:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-31 13:16:06","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":59,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC688.02c","SPCC970.12","SPCC1672.10","SPBC27B12.02","SPBC21.01","SPBP22H7.09c","SPBC409.04c","SPBC1105.17","SPAC1687.20c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2019-01-29"},{"uniquename":"PMID:35262697","title":"Replication stress induced by the ribonucleotide reductase inhibitor guanazole, triapine and gemcitabine in fission yeast.","citation":"FEMS Yeast Res 2022 Mar 24;22(1)","abstract":"Schizosaccharomyces pombe is an established yeast model for studying the cellular mechanisms conserved in humans, such as the DNA replication checkpoint. The replication checkpoint deals with replication stress caused by numerous endogenous and exogenous factors that perturb fork movement. If undealt with, perturbed forks collapse, causing chromosomal DNA damage or cell death. Hydroxyurea (HU) is an inhibitor of ribonucleotide reductase (RNR) commonly used in checkpoint studies. It produces replication stress by depleting dNTPs, which slows the movement of ongoing forks and thus activates the replication checkpoint. However, HU also causes side effects such as oxidative stress, particularly under chronic exposure conditions, which complicates the studies. To find a drug that generates replication stress more specifically, we tested three other RNR inhibitors gemcitabine, guanazole and triapine in S. pombe under various experimental conditions. Our results show that guanazole and triapine can produce replication stress more specifically than HU under chronic, not acute drug treatment conditions. Therefore, using the two drugs in spot assay, the method commonly used for testing drug sensitivity in yeasts, should benefit the checkpoint studies in S. pombe and likely the research in other model systems.","doi":"10.1093/femsyr/foac014","authors":"Alyahya MY, Khan S, Bhadra S, Samuel RE, Xu YJ","authors_abbrev":"Alyahya MY et al.","pubmed_publication_date":"24 Mar 2022","pubmed_entrez_date":"2022-03-09","publication_year":"2022","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-03-12 01:15:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC216.05","SPCC1259.13"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:9560221","title":"A distinct cyclin-dependent kinase-activating kinase of Arabidopsis thaliana.","citation":"Proc Natl Acad Sci U S A 1998 Apr 28;95(9):5021-6","abstract":"The activation of cyclin-dependent kinases (CDKs) requires phosphorylation of a threonine residue within the T-loop catalyzed by CDK-activating kinases (CAKs). Thus far no functional CAK homologue has been reported in plants. We screened an Arabidopsis cDNA expression library for complementation of a budding yeast CAK mutant. A cDNA, cak1At, was isolated that suppressed the CAK mutation in budding yeast, and it also complemented a fission yeast CAK mutant. cak1At encodes a protein related to animal CAKs. The CAK similarity was restricted to the conserved kinase domains, leading to classification of Cak1At as a distinct CDK in the phylogenetic tree. Immunoprecipitates with the anti-Cak1At antibody phosphorylated human CDK2 at the threonine residue (T160) within the T-loop and activated its activity to phosphorylate histone H1. Whereas CAKs in animals and fission yeast are involved in regulation of the cell cycle and basal transcription by phosphorylating the carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II, Cak1At did not phosphorylate the CTD. An Arabidopsis CTD-kinase isolated separately from Cak1At was shown to interact with the yeast protein p13(suc1), but it had no CDK2-kinase activity. Therefore, the CTD of RNA polymerase II is probably phosphorylated by a Cdc2-related kinase distinct from Cak1At. cak1At is a single-copy gene in Arabidopsis and is highly expressed in proliferating cells of suspension cultures.","authors":"Umeda M, Bhalerao RP, Schell J, Uchimiya H, Koncz C","authors_abbrev":"Umeda M et al.","pubmed_publication_date":"28 Apr 1998","pubmed_entrez_date":"1998-06-06","publication_year":"1998","canto_session_key":"3bf1632ffd681a25","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-01-07 01:57:08","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-01-07 01:56:58","canto_added_date":"2012-02-24 05:53:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19F8.07"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2016-01-07"},{"uniquename":"PMID:20682311","title":"Fission yeast telomeres forecast the end of the crisis.","citation":"FEBS Lett 2010 Sep 10;584(17):3725-33","abstract":"Recent years have placed fission yeast at the forefront of telomere research, as this organism combines a high level of conservation with human telomeres and precise genetic manipulability. Here we highlight some of the latest knowledge of fission yeast telomere maintenance and dysfunction, and illustrate how principles arising from fission yeast research are raising novel questions about telomere plasticity and function in all eukaryotes.","doi":"10.1016/j.febslet.2010.07.045","authors":"Dehé PM, Cooper JP","authors_abbrev":"Dehé PM et al.","pubmed_publication_date":"10 Sep 2010","pubmed_entrez_date":"2010-08-05","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10398680","title":"Proper metaphase spindle length is determined by centromere proteins Mis12 and Mis6 required for faithful chromosome segregation.","citation":"Genes Dev 1999 Jul 01;13(13):1664-77","abstract":"High-fidelity chromosome transmission is fundamental in controlling the quality of the cell division cycle. The spindle pole-to-pole distance remains constant from metaphase to anaphase A. We show that fission yeast sister centromere-connecting proteins, Mis6 and Mis12, are required for correct spindle morphogenesis, determining metaphase spindle length. Thirty-five to sixty percent extension of metaphase spindle length takes place in mis6 and mis12 mutants. This may be due to incorrect spindle morphogenesis containing impaired sister centromeres or force unbalance between pulling by the linked sister kinetochores and kinetochore-independent pushing. The mutant spindle fully extends in anaphase, although it is accompanied by drastic missegregation by aberrant sister centromere separation. Hence, metaphase spindle length may be crucial for segregation fidelity. Suppressors of mis12 partly restore normal metaphase spindle length. In mis4 that is defective in sister chromatid cohesion, metaphase spindle length is also long, but anaphase spindle extension is blocked, probably due to the activated spindle checkpoint. Extensive missegregation is caused in mis12 only when Mis12 is inactivated from the previous M through to the following M, an effective way to avoid missegregation in the cell cycle. Mis12 has conserved homologs in budding yeast and filamentous fungi.","authors":"Goshima G, Saitoh S, Yanagida M","authors_abbrev":"Goshima G et al.","pubmed_publication_date":"01 Jul 1999","pubmed_entrez_date":"1999-07-10","publication_year":"1999","canto_session_key":"6e84b9c4c93de258","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-02-01 21:05:10","canto_approved_date":"2025-12-09 09:41:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-21 08:57:34","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":27,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPAC1687.20c","SPBC409.04c","SPCC736.14","SPBC106.09"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2019-02-01"},{"uniquename":"PMID:17021256","title":"Noncore components of the fission yeast gamma-tubulin complex.","citation":"Mol Biol Cell 2006 Dec;17(12):5075-93","abstract":"Relatively little is known about the in vivo function of individual components of the eukaryotic gamma-tubulin complex (gamma-TuC). We identified three genes, gfh1+, mod21+, and mod22+, in a screen for fission yeast mutants affecting microtubule organization. gfh1+ is a previously characterized gamma-TuC protein weakly similar to human gamma-TuC subunit GCP4, whereas mod21+ is novel and shows weak similarity to human gamma-TuC subunit GCP5. We show that mod21p is a bona fide gamma-TuC protein and that, like gfh1Delta mutants, mod21Delta mutants are viable. We find that gfh1Delta and mod21Delta mutants have qualitatively normal microtubule nucleation from all types of microtubule-organizing centers (MTOCs) in vivo but quantitatively reduced nucleation from interphase MTOCs, and this is exacerbated by mutations in mod22+. Simultaneous deletion of gfh1p, mod21p, and alp16p, a third nonessential gamma-TuC protein, does not lead to additive defects, suggesting that all three proteins contribute to a single function. Coimmunoprecipitation experiments suggest that gfh1p and alp16p are codependent for association with a small \"core\" gamma-TuC, whereas mod21p is more peripherally associated, and that gfh1p and mod21p may form a subcomplex independently of the small gamma-TuC. Interestingly, sucrose gradient analysis suggests that the major form of the gamma-TuC in fission yeast may be a small complex. We propose that gfh1p, mod21p, and alp16 act as facultative \"noncore\" components of the fission yeast gamma-TuC and enhance its microtubule-nucleating ability.","authors":"Anders A, Lourenço PC, Sawin KE","authors_abbrev":"Anders A et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-10-06","publication_year":"2006","canto_session_key":"68aba795ee98fdcb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-09-15 12:47:39","canto_approved_date":"2022-07-21 08:17:13","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2015-09-15 12:47:31","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4G3.19","SPBC211.06","SPBC428.20c","SPBC365.15","SPCP1E11.06","SPAC806.08c","SPBC32F12.04"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2015-09-15"},{"uniquename":"PMID:15695360","title":"Mitochondrial translation: elongation factor tu is essential in fission yeast and depends on an exchange factor conserved in humans but not in budding yeast.","citation":"Genetics 2005 Apr;169(4):1891-901","abstract":"The translation elongation factor EF-Tu is a GTPase that delivers amino-acylated tRNAs to the ribosome during the elongation step of translation. EF-Tu/GDP is recycled by the guanine nucleotide exchange factor EF-Ts. Whereas EF-Ts is lacking in S. cerevisiae, both translation factors are found in S. pombe and H. sapiens mitochondria, consistent with the known similarity between fission yeast and human cell mitochondrial physiology. We constructed yeast mutants lacking these elongation factors. We show that mitochondrial translation is vital for S. pombe, as it is for human cells. In a genetic background allowing the loss of mitochondrial functions, a block in mitochondrial translation in S. pombe leads to a major depletion of mtDNA. The relationships between EF-Ts and EF-Tu from both yeasts and humans were investigated through functional complementation and coexpression experiments and by a search for suppressors of the absence of the S. pombe EF-Ts. We find that S. cerevisiae EF-Tu is functionally equivalent to the S. pombe EF-Tu/EF-Ts couple. Point mutations in the S. pombe EF-Tu can render it independent of its exchange factor, thereby mimicking the situation in S. cerevisiae.","authors":"Chiron S, Suleau A, Bonnefoy N","authors_abbrev":"Chiron S et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-02-08","publication_year":"2005","canto_session_key":"f0cb65a7aa96a0d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-04 13:03:34","canto_approved_date":"2025-04-01 08:19:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-04 09:09:37","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.07c","SPBC9B6.04c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-07-04"},{"uniquename":"PMID:36536175","title":"Multivalent interactions facilitate motor-dependent protein accumulation at growing microtubule plus-ends.","citation":"Nat Cell Biol 2023 Jan;25(1):68-78","abstract":"Growing microtubule ends organize end-tracking proteins into comets of mixed composition. Here using a reconstituted fission yeast system consisting of end-binding protein Mal3, kinesin Tea2 and cargo Tip1, we found that these proteins can be driven into liquid-phase droplets both in solution and at microtubule ends under crowding conditions. In the absence of crowding agents, cryo-electron tomography revealed that motor-dependent comets consist of disordered networks where multivalent interactions may facilitate non-stoichiometric accumulation of cargo Tip1. We found that two disordered protein regions in Mal3 are required for the formation of droplets and motor-dependent accumulation of Tip1, while autonomous Mal3 comet formation requires only one of them. Using theoretical modelling, we explore possible mechanisms by which motor activity and multivalent interactions may lead to the observed enrichment of Tip1 at microtubule ends. We conclude that microtubule ends may act as platforms where multivalent interactions condense microtubule-associated proteins into large multi-protein complexes.","doi":"10.1038/s41556-022-01037-0","authors":"Maan R, Reese L, Volkov VA, King MR, van der Sluis EO, Andrea N, Evers WH, Jakobi AJ, Dogterom M","authors_abbrev":"Maan R et al.","pubmed_publication_date":"Jan 2023","pubmed_entrez_date":"2022-12-19","publication_year":"2023","canto_session_key":"13fb833c2ab8cd13","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-03-10 19:39:41","canto_approved_date":"2023-03-10 19:41:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-10 19:39:34","canto_added_date":"2022-12-21 01:15:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.12","SPBC1604.20c","SPAC18G6.15"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2023-03-10"},{"uniquename":"PMID:8939596","title":"Cell cycle: reaching for a role for the Cks proteins.","citation":"Curr Biol 1996 Nov 01;6(11):1399-402","abstract":"The Cks proteins are essential components of the cyclin-dependent protein kinases that regulate mitosis in all eukaryotes, but their precise function remains obscure. The crystal structures of several Cks proteins offer insights into their roles during the cell cycle.","authors":"Pines J","authors_abbrev":"Pines J","pubmed_publication_date":"01 Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15030757","title":"Dynamics of homologous chromosome pairing during meiotic prophase in fission yeast.","citation":"Dev Cell 2004 Mar;6(3):329-41","abstract":"Pairing of homologous chromosomes is important for homologous recombination and correct chromosome segregation during meiosis. It has been proposed that telomere clustering, nuclear oscillation, and recombination during meiotic prophase facilitate homologous chromosome pairing in fission yeast. Here we examined the contributions of these chromosomal events to homologous chromosome pairing, by directly observing the dynamics of chromosomal loci in living cells of fission yeast. Homologous loci exhibited a dynamic process of association and dissociation during the time course of meiotic prophase. Lack of nuclear oscillation reduced association frequency for both centromeric and arm regions of the chromosome. Lack of telomere clustering or recombination reduced association frequency at arm regions, but not significantly at centromeric regions. Our results indicate that homologous chromosomes are spatially aligned by oscillation of telomere-bundled chromosomes and physically linked by recombination at chromosome arm regions; this recombination is not required for association of homologous centromeres.","authors":"Ding DQ, Yamamoto A, Haraguchi T, Hiraoka Y","authors_abbrev":"Ding DQ et al.","pubmed_publication_date":"Mar 2004","pubmed_entrez_date":"2004-03-20","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27872152","title":"An unconventional interaction between Dis1/TOG and Mal3/EB1 in fission yeast promotes the fidelity of chromosome segregation.","citation":"J Cell Sci 2016 Dec 15;129(24):4592-4606","abstract":"Dynamic microtubule plus-ends interact with various intracellular target regions such as the cell cortex and the kinetochore. Two conserved families of microtubule plus-end-tracking proteins, the XMAP215, ch-TOG or CKAP5 family and the end-binding 1 (EB1, also known as MAPRE1) family, play pivotal roles in regulating microtubule dynamics. Here, we study the functional interplay between fission yeast Dis1, a member of the XMAP215/TOG family, and Mal3, an EB1 protein. Using an in vitro microscopy assay, we find that purified Dis1 autonomously tracks growing microtubule ends and is a bona fide microtubule polymerase. Mal3 recruits additional Dis1 to microtubule ends, explaining the synergistic enhancement of microtubule dynamicity by these proteins. A non-canonical binding motif in Dis1 mediates the interaction with Mal3. X-ray crystallography shows that this new motif interacts in an unconventional configuration with the conserved hydrophobic cavity formed within the Mal3 C-terminal region that typically interacts with the canonical SXIP motif. Selectively perturbing the Mal3-Dis1 interaction in living cells demonstrates that it is important for accurate chromosome segregation. Whereas, in some metazoans, the interaction between EB1 and the XMAP215/TOG family members requires an additional binding partner, fission yeast relies on a direct interaction, indicating evolutionary plasticity of this critical interaction module.","authors":"Matsuo Y, Maurer SP, Yukawa M, Zakian S, Singleton MR, Surrey T, Toda T","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"15 Dec 2016","pubmed_entrez_date":"2016-11-23","publication_year":"2016","canto_session_key":"297bcc54c0cd9972","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2017-04-17 19:45:02","canto_approved_date":"2024-06-26 09:43:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-03 03:35:23","canto_added_date":"2016-11-24 01:15:11","annotation_curators":[{"name":"Takashi Toda","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPBC16A3.15c","SPCC736.14","SPCC895.07"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-04-17","pdb_entries":[{"pdb_id":"5m97","gene_chains":[{"gene_uniquename":"SPAC18G6.15","chain":"A/B","position":"174-247"}],"title":"Structure of the Mal3 EB1-like domain","entry_authors":"Zakian S,Singleton MR","entry_authors_abbrev":"Zakian S et al.","reference_uniquename":"PMID:27872152","experimental_method":"X-ray","resolution":"1.33"},{"pdb_id":"5m9e","gene_chains":[{"gene_uniquename":"SPCC736.14","chain":"E/F/G/H","position":"833-852"},{"gene_uniquename":"SPAC18G6.15","chain":"A/B/C/D","position":"174-247"}],"title":"Interactions between the Mal3 EB1-like domain and Dis1","entry_authors":"Zakian S,Singleton MR","entry_authors_abbrev":"Zakian S et al.","reference_uniquename":"PMID:27872152","experimental_method":"X-ray","resolution":"2.83"}]},{"uniquename":"EMBL:AU013145","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22508721","title":"RNAi in fission yeast finds new targets and new ways of targeting at the nuclear periphery.","citation":"Genes Dev 2012 Apr 15;26(8):741-5","abstract":"RNAi in Schizosaccharomyces pombe is critical for centromeric heterochromatin formation. It has remained unclear, however, whether RNAi also regulates the expression of protein-coding loci. In the April 1, 2012, issue of Genes & Development, Woolcock and colleagues (pp. 683-667) reported an elegant mechanism for the conditional RNAi-mediated repression of stress response genes involving association with Dcr1 at the nuclear pore. Unexpectedly, the initial targeting of RNAi components to these genes does not require small RNA guides.","doi":"10.1101/gad.191155.112","authors":"Holoch D, Moazed D","authors_abbrev":"Holoch D et al.","pubmed_publication_date":"15 Apr 2012","pubmed_entrez_date":"2012-04-18","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35673994","title":"Actin assembly requirements of the formin Fus1 to build the fusion focus.","citation":"J Cell Sci 2022 Jul 01;135(13)","abstract":"In formin-family proteins, actin filament nucleation and elongation activities reside in the formin homology 1 (FH1) and FH2 domains, with reaction rates that vary by at least 20-fold between formins. Each cell expresses distinct formins that assemble one or several actin structures, raising the question of what confers each formin its specificity. Here, using the formin Fus1 in Schizosaccharomyces pombe, we systematically probed the importance of formin nucleation and elongation rates in vivo. Fus1 assembles the actin fusion focus, necessary for gamete fusion to form the zygote during sexual reproduction. By constructing chimeric formins with combinations of FH1 and FH2 domains previously characterized in vitro, we establish that changes in formin nucleation and elongation rates have direct consequences on fusion focus architecture, and that Fus1 native high nucleation and low elongation rates are optimal for fusion focus assembly. We further describe a point mutant in Fus1 FH2 that preserves native nucleation and elongation rates in vitro but alters function in vivo, indicating an additional FH2 domain property. Thus, rates of actin assembly are tailored for assembly of specific actin structures.","doi":"10.1242/jcs.260289","authors":"Billault-Chaumartin I, Michon L, Anderson CA, Yde SE, Suarez C, Iwaszkiewicz J, Zoete V, Kovar DR, Martin SG","authors_abbrev":"Billault-Chaumartin I et al.","pubmed_publication_date":"01 Jul 2022","pubmed_entrez_date":"2022-06-08","publication_year":"2022","canto_session_key":"345d6b0c8bf7e493","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2022-07-19 07:37:03","canto_approved_date":"2024-06-15 20:57:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-03 08:01:44","canto_added_date":"2022-06-10 00:15:03","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":1,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":36,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.02c","SPAC20G4.02c","SPCC895.05","SPAC27F1.02c","SPAC1F5.04c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2022-07-19"},{"uniquename":"PMID:16879101","title":"Physical and functional interactions between MutY glycosylase homologue (MYH) and checkpoint proteins Rad9-Rad1-Hus1.","citation":"Biochem J 2006 Nov 15;400(1):53-62","abstract":"The MYH (MutY glycosylase homologue) increases replication fidelity by removing adenines or 2-hydroxyadenine misincorporated opposite GO (7,8-dihydro-8-oxo-guanine). The 9-1-1 complex (Rad9, Rad1 and Hus1 heterotrimer complex) has been suggested as a DNA damage sensor. Here, we report that hMYH (human MYH) interacts with hHus1 (human Hus1) and hRad1 (human Rad1), but not with hRad9. In addition, interactions between MYH and the 9-1-1 complex, from both the fission yeast Schizosaccharomyces pombe and human cells, are partially interchangeable. The major Hus1-binding site is localized to residues 295-350 of hMYH and to residues 245-293 of SpMYH (S. pombe MYH). Val315 of hMYH and Ile261 of SpMYH play important roles for their interactions with Hus1. hHus1 protein and the 9-1-1 complex of S. pombe can enhance the glycosylase activity of SpMYH. Moreover, the interaction of hMYH-hHus1 is enhanced following ionizing radiation. A significant fraction of the hMYH nuclear foci co-localizes with hRad9 foci in H2O2-treated cells. These results reveal that the 9-1-1 complex plays a direct role in base excision repair.","authors":"Shi G, Chang DY, Cheng CC, Guan X, Venclovas C, Lu AL","authors_abbrev":"Shi G et al.","pubmed_publication_date":"15 Nov 2006","pubmed_entrez_date":"2006-08-02","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17550896","title":"The fission yeast Jmj2 reverses histone H3 Lysine 4 trimethylation.","citation":"J Biol Chem 2007 Jul 27;282(30):21662-70","abstract":"Histone methylation regulates transcription, chromatin structure, and the epigenetic state of the cell. Recent studies identified the JmjC domain as a catalytic module for histone demethylation. Schizosaccharomyces pombe contains seven JmjC proteins, but it was unclear whether any of them functioned as histone demethylases. In this report, we show that the JmjC protein Jmj2, which is evolutionarily conserved from yeast to human, reversed trimethylated H3-Lys-4 to di- and mono-but not unmethylated products. Overexpression of Jmj2 but not a catalytically inactive mutant reduced H3-Lys-4 trimethylation levels in vivo and suppressed the toxicity caused by overexpression of the H3-Lys-4-me3-binding protein Yng1 in budding yeast. Genome-wide analysis showed that the loss of jmj2 was associated with an increase in the H3-Lys-4-me3 signal, which was enriched near the transcriptional start sites and the coding regions. At the mating-type locus, the loss of jmj2 or substitution of jmj2 with a catalytically inactive form is correlated with increased reporter gene transcription and H3-Lys-4-me3/2 levels, suggesting that Jmj2 and its demethylase activity may play a role in heterochromatin biology. Our findings identified a novel S. pombe histone demethylase with specificity toward di- and trimethylated histone H3-Lys-4 and a possible role in heterochromatin regulation.","authors":"Huarte M, Lan F, Kim T, Vaughn MW, Zaratiegui M, Martienssen RA, Buratowski S, Shi Y","authors_abbrev":"Huarte M et al.","pubmed_publication_date":"27 Jul 2007","pubmed_entrez_date":"2007-06-07","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1002.05c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:11453249","title":"The Schizosaccharomyces pombe Cdc42p GTPase signals through Pak2p and the Mkh1p-Pek1p-Spm1p MAP kinase pathway.","citation":"Curr Genet 2001 Jun;39(4):205-9","abstract":"The Cdc42p GTPase is involved in many aspects of growth and cell-cycle regulation, including actin cytoskeletal rearrangements and activation of signal transduction pathways. To further investigate these functions, genetic interactions were examined between Schizosaccharomyces pombe Cdc42p, its effectors Pak1p and Pak2p, and the Mkh1p-Pek1p-Spm1p signal transduction pathway, which functions in cytokinesis and cell division. Expression of a truncated version of Pak2p lacking its N-terminal autoinhibitory domain led to a growth defect that was suppressed by deltamkh1 and deltaspm1 null mutations and an elongated cell phenotype indicative of a cell division defect that was suppressed by the deltamkh1 mutation. In addition, expression of the constitutively activated cdc42G12V mutant allele led to a growth defect that was rescued by the deltapak2 and deltamkh1 mutations. The deltapak2 mutation did not suppress the growth defect conferred by plasmid expression of Mkh1p, suggesting that Pak2p functions upstream of Mkh1p in this pathway. A two-hybrid protein interaction was observed between Pak2p and Mkh1p, but not between Pak1p and Mkh1p. These results are consistent with Cdc42p interacting with Pak2p to signal through the Mkh1p-Pek1p-Spm1p pathway.","authors":"Merla A, Johnson DI","authors_abbrev":"Merla A et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-07-17","publication_year":"2001","canto_session_key":"b8d42702f18c7b0d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2025-11-19 09:51:58","canto_approved_date":"2025-12-14 19:16:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-10-23 11:03:29","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":16,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.08","SPAC1F5.09c","SPAC110.03","SPAC1F3.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2025-11-19"},{"uniquename":"PMID:18793338","title":"Rga2 is a Rho2 GAP that regulates morphogenesis and cell integrity in S. pombe.","citation":"Mol Microbiol 2008 Nov;70(4):867-81","abstract":"Schizosaccharomyces pombe Rho2 GTPase regulates alpha-D-glucan synthesis and acts upstream of Pck2 to activate the MAP kinase pathway for cell integrity. However, little is known about its regulation. Here we describe Rga2 as a Rho2 GTPase-activating protein (GAP) that regulates cell morphology. rga2+ gene is not essential for growth but its deletion causes longer and thinner cells whereas rga2+ overexpression causes shorter and broader cells. rga2+ overexpression also causes abnormal accumulation of Calcofluor-stained material and cell lysis, suggesting that it also participates in cell wall integrity. Rga2 localizes to growth tips and septum region. The N-terminal region of the protein is required for its correct localization whereas the PH domain is necessary exclusively for Rga2 localization to the division area. Also, Rga2 localization depends on polarity markers and on actin polymerization. Rga2 interacts with Rho2 and possesses in vitro and in vivo GAP activity for this GTPase. Accordingly, rga2Delta cells contain more alpha-D-glucan and therefore partially suppress the thermosensitivity of mok1-664 cells, which have a defective alpha-D-glucan synthase. Additionally, genetic interactions and biochemical analysis suggest that Rga2 regulates Rho2-Pck2 interaction and might participate in the regulation of the MAPK cell integrity pathway.","doi":"10.1111/j.1365-2958.2008.06447.x","authors":"Villar-Tajadura MA, Coll PM, Madrid M, Cansado J, Santos B, Pérez P","authors_abbrev":"Villar-Tajadura MA et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-09-17","publication_year":"2008","canto_session_key":"74503deb11e399af","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-05-19 18:05:52","canto_approved_date":"2026-01-29 13:46:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-08 14:15:38","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":85,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.08c","SPAC110.03","SPBC119.08","SPAC29A4.11","SPAC26A3.09c","SPBC354.13","SPAC16.01","SPBC12D12.04c","SPAC4A8.15c","SPAC1F7.04","SPCC1281.01","SPAC1F3.02c","SPAC23C4.08","SPAC20H4.11c","SPAC16A10.04"],"gene_count":15,"ltp_gene_count":11,"approved_date":"2017-05-19"},{"uniquename":"PMID:11027257","title":"Analysis of fission yeast primase defines the checkpoint responses to aberrant S phase initiation.","citation":"Mol Cell Biol 2000 Nov;20(21):7853-66","abstract":"To investigate the checkpoint response to aberrant initiation, we analyzed the cell cycle checkpoint response induced by mutations of Schizosaccharomyces pombe DNA primase. DNA primase has two subunits, Spp1 and Spp2 (S. pombe primases 1 and 2). Spp1 is the catalytic subunit that synthesizes the RNA primer, which is then extended by DNA polymerase alpha (Polalpha) to synthesize an initiation DNA structure, and this catalytic function of Polalpha is a prerequisite for generating the S-M phase checkpoint. Here we show that Spp2 is required for coupling the function of Spp1 to Polalpha. Thermosensitive mutations of spp2(+) destabilize the Polalpha-primase complex, resulting in an allele-specific S phase checkpoint defect. The mutant exhibiting a more severe checkpoint defect also has a higher extent of Polalpha-primase complex instability and deficiency in the hydroxyurea-induced Cds1-mediated intra-S phase checkpoint response. However, this mutant is able to activate the Cds1 response to S phase arrest induced by temperature. These findings suggest that the Cds1 response to the S-phase arrest signal(s) induced by a initiation mutant is different from that induced by hydroxyurea. Interestingly, a polalphats mutant with a defective S-M phase checkpoint and an spp2 mutant with an intact checkpoint have a similar Polalpha-primase complex stability, and the Cds1 response induced by hydroxyurea or by the mutant arrests at the restrictive temperature. Thus, the Cds1-mediated intra-S phase checkpoint response induced by hydroxyurea can also be distinguished from the S-M phase checkpoint response that requires the initiation DNA synthesis by Polalpha.","authors":"Tan S, Wang TS","authors_abbrev":"Tan S et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-10-12","publication_year":"2000","canto_session_key":"bf9273ed8cb720b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-06-01 15:25:39","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-13 11:54:15","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":78,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17D11.06","SPAC3H5.06c","SPAC6B12.10c","SPBC216.05","SPCC18B5.11c","SPCC1259.13","SPAC1952.07","SPAC664.07c","SPAC14C4.13","SPAC9E9.08","SPAC20G4.04c"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2015-02-13"},{"uniquename":"PMID:18367542","title":"Meiotic spindle pole bodies acquire the ability to assemble the spore plasma membrane by sequential recruitment of sporulation-specific components in fission yeast.","citation":"Mol Biol Cell 2008 Jun;19(6):2476-87","abstract":"The spindle pole body (SPB) of Schizosaccharomyces pombe is required for assembly of the forespore membrane (FSM) during meiosis. Before de novo biogenesis of the FSM, the meiotic SPB forms outer plaques, an event referred to as SPB modification. A constitutive SPB component, Spo15, plays an indispensable role in SPB modification and sporulation. Here, we analyzed two sporulation-specific genes, spo13(+) and spo2(+), which are not required for progression of meiotic nuclear divisions, but are essential for sporulation. Spo13 is a 16-kDa coiled-coil protein, and Spo2 is a 15-kDa nonconserved protein. Both Spo13 and Spo2 specifically associated with the meiotic SPB. The respective deletion mutants are viable, but defective in SPB modification and in the onset of FSM formation. Spo13 and Spo2 localized on the cytoplasmic side of the SPB in close contact with the nascent FSM. Localization of Spo13 to the SPB was dependent on Spo15 and Spo2; that of Spo2 depended only on Spo15, suggesting that their recruitment to the SPB is strictly controlled. Spo2 physically associated with both Spo15 and Spo13, but Spo13 and Spo15 did not interact directly. Taken together, these observations indicate that Spo2 is recruited to the SPB during meiosis and then assists in the localization of Spo13 to the outer surface of the SPB.","authors":"Nakase Y, Nakamura-Kubo M, Ye Y, Hirata A, Shimoda C, Nakamura T","authors_abbrev":"Nakase Y et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-03-28","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1183.12","SPBC16C6.14","SPAC1F3.06c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:10082519","title":"The schizosaccharomyces pombe dim1(+) gene interacts with the anaphase-promoting complex or cyclosome (APC/C) component lid1(+) and is required for APC/C function.","citation":"Mol Cell Biol 1999 Apr;19(4):2535-46","abstract":"The Schizosaccharomyces pombe dim1(+) gene is required for entry into mitosis and for chromosome segregation during mitosis. To further understand dim1p function, we undertook a synthetic lethal screen with the temperature-sensitive dim1-35 mutant and isolated lid (for lethal in dim1-35) mutants. Here, we describe the temperature-sensitive lid1-6 mutant. At the restrictive temperature of 36 degrees C, lid1-6 mutant cells arrest with a \"cut\" phenotype similar to that of cut4 and cut9 mutants. An epitope-tagged version of lid1p is a component of a multiprotein approximately 20S complex; the presence of lid1p in this complex depends upon functional cut9(+). lid1p-myc coimmunoprecipitates with several other proteins, including cut9p and nuc2p, and the presence of cut9p in a 20S complex depends upon the activity of lid1(+). Further, lid1(+) function is required for the multiubiquitination of cut2p, an anaphase-promoting complex or cyclosome (APC/C) target. Thus, lid1p is a component of the S. pombe APC/C. In dim1 mutants, the abundances of lid1p and the APC/C complex decline significantly, and the ubiquitination of an APC/C target is abolished. These data suggest that at least one role of dim1p is to maintain or establish the steady-state level of the APC/C.","authors":"Berry LD, Feoktistova A, Wright MD, Gould KL","authors_abbrev":"Berry LD et al.","pubmed_publication_date":"Apr 1999","pubmed_entrez_date":"1999-03-19","publication_year":"1999","canto_session_key":"fa117091c52b1032","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-28 15:08:48","canto_approved_date":"2022-02-07 17:35:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-23 18:01:58","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.15c","SPBC16G5.01","SPCC16A11.05c","SPAC19G12.01c","SPBC14C8.01c","SPAC17C9.01c"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-01-28"},{"uniquename":"PMID:17998401","title":"Nuclear size control in fission yeast.","citation":"J Cell Biol 2007 Nov 19;179(4):593-600","abstract":"A long-standing biological question is how a eukaryotic cell controls the size of its nucleus. We report here that in fission yeast, nuclear size is proportional to cell size over a 35-fold range, and use mutants to show that a 16-fold change in nuclear DNA content does not influence the relative size of the nucleus. Multi-nucleated cells with unevenly distributed nuclei reveal that nuclei surrounded by a greater volume of cytoplasm grow more rapidly. During interphase of the cell cycle nuclear growth is proportional to cell growth, and during mitosis there is a rapid expansion of the nuclear envelope. When the nuclear/cell (N/C) volume ratio is increased by centrifugation or genetic manipulation, nuclear growth is arrested while the cell continues to grow; in contrast, low N/C ratios are rapidly corrected by nuclear growth. We propose that there is a general cellular control linking nuclear growth to cell size.","authors":"Neumann FR, Nurse P","authors_abbrev":"Neumann FR et al.","pubmed_publication_date":"19 Nov 2007","pubmed_entrez_date":"2007-11-14","publication_year":"2007","canto_session_key":"c7ebad4e7cc6e618","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ryoko Mandeville","canto_first_approved_date":"2012-07-16 12:40:52","canto_approved_date":"2024-08-13 16:04:38","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-07-10 14:04:00","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Ryoko Mandeville","community_curator":true,"annotation_count":6,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.12","SPAC24H6.05","SPBC336.12c","SPBC1604.14c","SPCC18B5.03","SPBC582.03"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2012-07-16"},{"uniquename":"PMID:8557039","title":"Schizosaccharomyces pombe atf1+ encodes a transcription factor required for sexual development and entry into stationary phase.","citation":"EMBO J 1995 Dec 15;14(24):6193-208","abstract":"We describe the identification and characterization of a transcription factor encoded by the atf1+ gene of the fission yeast Schizosaccharomyces pombe. The factor Atf1, contains a bZIP domain at its C-terminus with strong homology to members of the ATF/CREB family of mammalian factors and in vitro binds specifically to ATF/CRE recognition sites. Furthermore the ATF-like binding activity detected in extracts from fission yeast cells is entirely lost upon deletion of the atf1+ gene. Upon growth to saturation, fission yeast cells exit the mitotic cycle and enter a G0-like stationary phase. However, on rich medium, entry of atf1- cells into stationary phase is restricted and they rapidly lose viability; this does not occur on minimal medium unless cAMP levels are raised. Thus stationary phase entry appears to be regulated negatively by cAMP and positively by Atf1. atf1- cells are also sterile and this sterility appears to be due to a combination of two defects: first, upon nitrogen starvation the majority of atf1- cells fail to arrest in the G1 phase of the cell cycle and second, the induction of ste11+ expression is lost. Thus expression of ste11+ represents a second example of an event that is negatively regulated by the cAMP pathway and positively regulated by Atf1. Despite their close association however, these two regulatory pathways function independently and Atf1 activity is not directly modulated by cAMP levels or mutations that alter the activity of components of the cAMP signalling pathway. Thus Atf1 is a transcription factor that plays an important role in the response of cells to adverse environmental conditions, which is to exit the mitotic cell cycle and either sexually differentiate or enter a resting state.","authors":"Takeda T, Toda T, Kominami K, Kohnosu A, Yanagida M, Jones N","authors_abbrev":"Takeda T et al.","pubmed_publication_date":"15 Dec 1995","pubmed_entrez_date":"1995-12-15","publication_year":"1995","canto_session_key":"597903fea2d2816c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-06-03 08:14:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-08 13:48:58","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPBC19C2.05","SPBC32C12.02","SPBC1198.14c","SPBC29B5.01","SPAC27D7.03c","SPCC285.09c","SPAC8C9.03"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2015-01-08"},{"uniquename":"PMID:9211981","title":"Mitosis-specific phosphorylation of gar2, a fission yeast nucleolar protein structurally related to nucleolin.","citation":"Chromosoma 1997 Jun;105(7-8):532-41","abstract":"The nucleolar protein gar2 of fission yeast is structurally related to the multifunctional nucleolar protein nucleolin from vertebrates and has been shown to be implicated in production of 18S rRNA. gar2 contains several potential casein kinase 2 (CK2) phosphorylation sites and a single putative p34(cdc2 )phosphorylation site in the consensus S50PKK. Here, we show that, like nucleolin, gar2 is phosphorylated in vitro by both highly purified CK2 from CHO cells and p34(cdc2 )from starfish oocytes. Moreover, the substitution of alanine for the N-terminal serine 50 abolishes phosphorylation by p34(cdc2 )in vitro. We also provide evidence that gar2 is phosphorylated in vitro by a p13(suc1)-Sepharose-bound kinase from Schizosaccharomyces pombe extracts that displays cell cycle-regulated activity similar to that of the p34(cdc2(kinase. In vivo 32P labeling of cells indicates that gar2 is a phosphoprotein and that incorporation of phosphate on residue 50 occurs specifically at mitosis. Taken together, these results lead us to propose that gar2 is likely to be an in vivo substrate for the mitotic p34(cdc2 )kinase. However, this posttranslational modification of the gar2 protein does not appear to be essential for normal production of 18S rRNA.","authors":"Gulli MP, Faubladier M, Sicard H, Caizergues-Ferrer M","authors_abbrev":"Gulli MP et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"884f96c5ddfddf7d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-02-19 18:57:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-16 13:09:26","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPBC20F10.01","SPAC140.02","SPBC1734.14c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-02-16"},{"uniquename":"PMID:11686304","title":"XMog1, a nuclear ran-binding protein in Xenopus, is a functional homologue of Schizosaccharomyces pombe mog1p that co-operates with RanBP1 to control generation of Ran-GTP.","citation":"J Cell Sci 2001 Aug;114(Pt 16):3013-23","abstract":"Ran is a multifunctional small GTPase of the Ras superfamily that plays roles in nucleocytoplasmic transport, mitotic spindle assembly and nuclear envelope formation. By screening a Xenopus oocyte cDNA library for Ran-GTP-binding proteins using the two-hybrid system of co-expression in yeast, we identified XMog1, a 20.4 kDa polypeptide related to Mog1p in Saccharomyces cerevisiae and similar gene products in Schizosaccharomyces pombe, Arabidopsis and mammals. We show that cDNAs encoding XMog1 and S. cerevisiae Mog1p rescue the growth defect of S. pombe cells lacking mog1, demonstrating conservation of their functions. In Xenopus somatic cells and transfected mammalian cells, XMogl is localised to the nucleus. XMog1 alone does not stimulate Ran GTPase activity or nucleotide exchange, but causes nucleotide release from Ran-GTP and forms a complex with nucleotide-free Ran. However, in combination with Ran-binding protein 1 (RanBP1), XMog1 promotes the release of GDP and the selective binding of GTP to Ran. XMog1 and RanBP1 also promote selective GTP loading onto Ran catalysed by the nuclear guanine nucleotide exchange factor, RCC1. We propose that Mog1-related proteins, together with RanBP1, facilitate the generation of Ran-GTP from Ran-GDP in the nucleus.","authors":"Nicolás FJ, Moore WJ, Zhang C, Clarke PR","authors_abbrev":"Nicolás FJ et al.","pubmed_publication_date":"Aug 2001","pubmed_entrez_date":"2001-11-01","publication_year":"2001","canto_session_key":"ca5db7cd89404661","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-09-28 11:25:15","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-09-28 11:25:08","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1840.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-09-28"},{"uniquename":"PMID:32185489","title":"Machinery for fungal heme acquisition.","citation":"Curr Genet 2020 Aug;66(4):703-711","abstract":"Iron is essential for nearly all aerobic organisms. One source of iron in nature is in the form of heme. Due to its critical physiological importance as a cofactor for several enzymes, organisms have evolved various means to secure heme for their needs. In the case of heme prototrophs, these organisms possess a highly conserved eight-step biosynthetic pathway. Another means used by many organisms is to acquire heme from external sources. As opposed to the knowledge of enzymes responsible for heme biosynthesis, the nature of the players and mechanisms involved in the acquisition of exogenous heme is limited. This review focuses on a description of newly discovered proteins that have novel functions in heme assimilation in the model organism Schizosaccharomyces pombe. This tractable model allows the use of the power of genetics to selectively block heme biosynthesis, setting conditions to investigate the mechanisms by which external heme is taken up by the cells. Studies have revealed that S. pombe possesses two independent heme uptake systems that require Shu1 and Str3, respectively. Heme-bound iron is captured by Shu1 at the cell surface, triggering its internalization to the vacuole with the aid of ubiquitinated proteins and the ESCRT machinery. In the case of the plasma membrane transporter Str3, it promotes cellular heme import in cells lacking Shu1. The discovery of these two pathways may contribute to gain novel insights into the mechanisms whereby fungi assimilate heme, which is an essentially biological process for their ability to invade and colonize new niches.","doi":"10.1007/s00294-020-01067-x","authors":"Labbé S, Mourer T, Brault A, Vahsen T","authors_abbrev":"Labbé S et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-03-19","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-03-20 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PANTHER:PTHR10632","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC2G5.06c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:9356477","title":"Schizosaccharomyces pombe cdc20+ encodes DNA polymerase epsilon and is required for chromosomal replication but not for the S phase checkpoint.","citation":"Proc Natl Acad Sci U S A 1997 Nov 11;94(23):12491-6","abstract":"In fission yeast both DNA polymerase alpha (pol alpha) and delta (pol delta) are required for DNA chromosomal replication. Here we demonstrate that Schizosaccharomyces pombe cdc20+ encodes the catalytic subunit of DNA polymerase epsilon (pol epsilon) and that this enzyme is also required for DNA replication. Following a shift to the restrictive temperature, cdc20 temperature-sensitive mutant cells block at the onset of DNA replication, suggesting that cdc20+ is required early in S phase very near to the initiation step. In the budding yeast Saccharomyces cerevisiae, it has been reported that in addition to its proposed role in chromosomal replication, DNA pol epsilon (encoded by POL2) also functions directly as an S phase checkpoint sensor [Navas, T. A., Zhou, Z. & Elledge, S. J. (1995) Cell 80, 29-39]. We have investigated whether cdc20+ is required for the checkpoint control operating in fission yeast, and our data indicate that pol epsilon does not have a role as a checkpoint sensor coordinating S phase with mitosis. In contrast, germinating spores disrupted for the gene encoding pol alpha rapidly enter mitosis in the absence of DNA synthesis, suggesting that in the absence of pol alpha, normal coordination between S phase and mitosis is lost. We propose that the checkpoint signal operating in S phase depends on assembly of the replication initiation complex, and that this signal is generated prior to the elongation stage of DNA synthesis.","authors":"D'Urso G, Nurse P","authors_abbrev":"D'Urso G et al.","pubmed_publication_date":"11 Nov 1997","pubmed_entrez_date":"1997-11-14","publication_year":"1997","canto_session_key":"e8951bae6a6840f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-03-17 16:51:36","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-03-17 16:51:29","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":11,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.09","SPAC3H5.06c","SPBC25H2.13c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-03-17"},{"uniquename":"PMID:29215009","title":"The end-joining factor Ku acts in the end-resection of double strand break-free arrested replication forks.","citation":"Nat Commun 2017 Dec 07;8(1):1982","abstract":"Replication requires homologous recombination (HR) to stabilize and restart terminally arrested forks. HR-mediated fork processing requires single stranded DNA (ssDNA) gaps and not necessarily double strand breaks. We used genetic and molecular assays to investigate fork-resection and restart at dysfunctional, unbroken forks in Schizosaccharomyces pombe. Here, we report that fork-resection is a two-step process regulated by the non-homologous end joining factor Ku. An initial resection mediated by MRN-Ctp1 removes Ku from terminally arrested forks, generating ~110 bp sized gaps obligatory for subsequent Exo1-mediated long-range resection and replication restart. The mere lack of Ku impacts the processing of arrested forks, leading to an extensive resection, a reduced recruitment of RPA and Rad51 and a slower fork-restart process. We propose that terminally arrested forks undergo fork reversal, providing a single DNA end for Ku binding. We uncover a role for Ku in regulating end-resection of unbroken forks and in fine-tuning HR-mediated replication restart.","doi":"10.1038/s41467-017-02144-5","authors":"Teixeira-Silva A, Ait Saada A, Hardy J, Iraqui I, Nocente MC, Fréon K, Lambert SAE","authors_abbrev":"Teixeira-Silva A et al.","pubmed_publication_date":"07 Dec 2017","pubmed_entrez_date":"2017-12-08","publication_year":"2017","canto_session_key":"e8bfc899ec0c73d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sarah Lambert","canto_first_approved_date":"2018-01-10 11:30:42","canto_approved_date":"2022-02-25 05:00:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-12-14 17:20:23","canto_added_date":"2017-12-09 01:15:56","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sarah Lambert","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPCC338.08","SPAC13C5.07","SPAC1556.01c","SPCC126.02c","SPAC644.14c","SPBC29A10.05","SPBC660.13c","SPCC23B6.05c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2018-01-10"},{"uniquename":"PMID:15975911","title":"The novel fission yeast protein Pal1p interacts with Hip1-related Sla2p/End4p and is involved in cellular morphogenesis.","citation":"Mol Biol Cell 2005 Sep;16(9):4124-38","abstract":"The establishment and maintenance of characteristic cellular morphologies is a fundamental property of all cells. Here we describe Schizosaccharomyces pombe Pal1p, a protein important for maintenance of cylindrical cellular morphology. Pal1p is a novel membrane-associated protein that localizes to the growing tips of interphase cells and to the division site in cells undergoing cytokinesis in an F-actin- and microtubule-independent manner. Cells deleted for pal1 display morphological defects, characterized by the occurrence of spherical and pear-shaped cells with an abnormal cell wall. Pal1p physically interacts and displays overlapping localization with the Huntingtin-interacting-protein (Hip1)-related protein Sla2p/End4p, which is also required for establishment of cylindrical cellular morphology. Sla2p is important for efficient localization of Pal1p to the sites of polarized growth and appears to function upstream of Pal1p. Interestingly, spherical pal1Delta mutants polarize to establish a pearlike morphology before mitosis in a manner dependent on the kelch-repeat protein Tea1p and the cell cycle inhibitory kinase Wee1p. Thus, overlapping mechanisms involving Pal1p, Tea1p, and Sla2p contribute to the establishment of cylindrical cellular morphology, which is important for proper spatial regulation of cytokinesis.","authors":"Ge W, Chew TG, Wachtler V, Naqvi SN, Balasubramanian MK","authors_abbrev":"Ge W et al.","pubmed_publication_date":"Sep 2005","pubmed_entrez_date":"2005-06-25","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPCP1E11.04c","SPAC688.11","SPCC1223.06"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"EMBL:SPP68DBP","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18818364","title":"Conservation and rewiring of functional modules revealed by an epistasis map in fission yeast.","citation":"Science 2008 Oct 17;322(5900):405-10","abstract":"An epistasis map (E-MAP) was constructed in the fission yeast, Schizosaccharomyces pombe, by systematically measuring the phenotypes associated with pairs of mutations. This high-density, quantitative genetic interaction map focused on various aspects of chromosome function, including transcription regulation and DNA repair/replication. The E-MAP uncovered a previously unidentified component of the RNA interference (RNAi) machinery (rsh1) and linked the RNAi pathway to several other biological processes. Comparison of the S. pombe E-MAP to an analogous genetic map from the budding yeast revealed that, whereas negative interactions were conserved between genes involved in similar biological processes, positive interactions and overall genetic profiles between pairs of genes coding for physically associated proteins were even more conserved. Hence, conservation occurs at the level of the functional module (protein complex), but the genetic cross talk between modules can differ substantially.","doi":"10.1126/science.1162609","authors":"Roguev A, Bandyopadhyay S, Zofall M, Zhang K, Fischer T, Collins SR, Qu H, Shales M, Park HO, Hayles J, Hoe KL, Kim DU, Ideker T, Grewal SI, Weissman JS, Krogan NJ","authors_abbrev":"Roguev A et al.","pubmed_publication_date":"17 Oct 2008","pubmed_entrez_date":"2008-09-27","publication_year":"2008","canto_session_key":"280115e26e3b662f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-02-23 17:41:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-23 17:19:09","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC823.14","SPCC613.12c","SPBC660.11","SPBC15D4.10c","SPBC36.07","SPBC428.17c","SPAC23G3.08c","SPAC1783.05","SPAC1B3.02c","SPBC83.03c","SPAC1805.03c","SPAPB24D3.04c","SPBC17D11.02c","SPBC8D2.04","SPCC285.16c","SPBC215.07c","SPAC11D3.07c","SPBC2F12.12c","SPCC1259.03","SPAC3G6.06c","SPAC9.05","SPBC36.05c","SPCC364.06","SPAC4C5.02c","SPAC20G4.04c","SPAP14E8.02","SPBC19F5.02c","SPCC1020.10","SPAC1834.08","SPAC4H3.07c","SPAC105.03c","SPBC30D10.04","SPCC4G3.19","SPAC27F1.03c","SPBC16E9.11c","SPAC227.05","SPAC56F8.08","SPBC800.05c","SPAC25H1.06","SPAC139.01c","SPBC29A3.09c","SPAC20H4.07","SPBC1778.02","SPBC336.05c","SPCC663.12","SPAC17C9.09c","SPAC26F1.02","SPBC16G5.11c","SPAC644.14c","SPBC13E7.08c","SPBC16G5.03","SPBC8D2.16c","SPCC622.17","SPBC83.05","SPAC1952.07","SPCC1183.06","SPAPB1A10.09","SPBC1198.14c","SPAC29B12.06c","SPAPYUG7.06","SPAC589.07c","SPBC16E9.17c","SPAC12B10.13","SPBC1105.11c","SPCC188.02","SPAC806.08c","SPAC2G11.07c","SPAC6G9.03c","SPBC16H5.05c","SPBC20F10.06","SPCC18B5.10c","SPBC3H7.06c","SPCC31H12.08c","SPBC14F5.08","SPBC609.05","SPCC737.07c","SPBC27.02c","SPCC18B5.11c","SPBC725.06c","SPAC23A1.02c","SPBC3H7.10","SPAC22F3.03c","SPBP4H10.16c","SPBC21B10.12","SPAC664.07c","SPAC23H4.10c","SPCC126.07c","SPBC1718.02","SPAC2F7.08c","SPBC31F10.10c","SPAC23A1.07","SPAC1834.07","SPAC57A10.09c","SPCC1672.08c","SPAC144.05","SPAC1687.22c","SPBC1773.11c","SPBC342.06c","SPCC11E10.06c","SPAC1952.06c","SPBC12D12.02c","SPBC1105.04c","SPCP25A2.02c","SPCC188.13c","SPCC306.04c","SPBC800.03","SPAC22E12.14c","SPCC584.02","SPBC1347.12","SPAC343.04c","SPAC17A5.16","SPAC1834.04","SPAC824.04","SPCC4B3.12","SPBP4H10.17c","SPCC1739.05","SPAC25A8.01c","SPBC28F2.11","SPAC17G8.05","SPAC110.02","SPAC227.10","SPBC119.14","SPBC336.01","SPBC1685.04","SPAC1687.13c","SPAC1782.05","SPAC3C7.09","SPAC4G8.06c","SPAC9G1.10c","SPAC3A11.13","SPCC1393.02c","SPBP8B7.21","SPBC16E9.12c","SPAC25B8.07c","SPAC12G12.01c","SPBC1703.14c","SPAC3G9.12","SPAC8E11.03c","SPBC24C6.05","SPCC1739.03","SPCC550.03c","SPBC36B7.08c","SPAC2F7.03c","SPAC11E3.01c","SPAC13F5.01c","SPBC428.08c","SPAP27G11.15","SPCC1223.01","SPBC14F5.13c","SPAC20G4.01","SPBPB10D8.02c","SPCC18B5.07c","SPAC1805.07c","SPBC1604.20c","SPAC167.07c","SPBC12D12.06","SPBC1604.19c","SPBC354.03","SPBC30B4.02c","SPAC25G10.02","SPAC16A10.02","SPAC227.14","SPBC1734.07c","SPBC23E6.08","SPBC106.13","SPAC3G6.01","SPBC1734.15","SPAC4H3.02c","SPAC589.02c","SPAC13A11.04c","SPAC12B10.01c","SPAC17C9.05c","SPAC11G7.02","SPBC1703.11","SPCC126.13c","SPCC622.19","SPAC3G6.11","SPCC1020.09","SPBC1198.11c","SPBC29A10.10c","SPAC3C7.01c","SPAPB24D3.02c","SPAC3C7.14c","SPCC895.06","SPBC2D10.14c","SPBC577.03c","SPBC609.03","SPAC31A2.15c","SPBC543.10","SPAC806.07","SPBC32H8.11","SPBC2A9.04c","SPBC2A9.03","SPBC1703.04","SPAC25B8.05","SPCC18B5.05c","SPAC328.01c","SPBC1289.11","SPAC17G6.03","SPAC29A4.02c","SPAC1071.02","SPCC18.13","SPAC23D3.09","SPCC550.12","SPBC13G1.10c","SPAC1002.15c","SPCC757.10","SPBC29A10.05","SPCC594.05c","SPCC1020.12c","SPAC3A12.03c","SPBC17A3.03c","SPAC630.10","SPBC3E7.08c","SPBC1604.10","SPAC1002.05c","SPBC21D10.10","SPACUNK4.16c","SPAC1782.01","SPBC3D6.04c","SPCC162.11c","SPCC1223.10c","SPBC342.05","SPBP35G2.08c","SPAC20H4.10","SPAC26H5.05","SPCC1919.05","SPAPB21F2.03","SPAC15E1.10","SPAC19D5.02c","SPAC1142.03c","SPBC582.10c","SPCC18.10","SPCC622.15c","SPBP8B7.18c","SPBC800.09","SPAC17G8.07","SPCC23B6.03c","SPCC18.06c","SPAC14C4.13","SPAC694.06c","SPAC6F12.06","SPAC9E9.08","SPAC1093.03","SPAC1F3.09","SPBP8B7.10c","SPAC18G6.15","SPAC23G3.07c","SPBC19F5.01c","SPAC22F3.08c","SPAC16A10.05c","SPBC1539.10","SPBP8B7.27","SPBC1347.02","SPBC18E5.05c","SPBC1685.15c","SPBP8B7.23","SPBC13G1.08c","SPAC688.14","SPCC663.05c","SPCC1223.11","SPBC12C2.05c","SPBC543.03c","SPBC3H7.07c","SPBC1773.16c","SPCC126.03","SPBC11B10.10c","SPCC1322.06","SPAC3C7.12","SPBC4B4.03","SPAC13C5.07","SPBP23A10.16","SPBC16H5.13","SPAC1565.07c","SPBC3D6.10","SPBC12D12.09","SPAC14C4.12c","SPBC119.08","SPBC1D7.05","SPAC2F3.16","SPCC132.02","SPAC3H1.12c","SPBC2G2.02","SPAC664.02c","SPAC343.11c","SPCC622.08c","SPAC4H3.05","SPAC4F10.11","SPBC16D10.07c","SPBC337.03","SPAC20H4.04","SPAC821.06","SPBC649.03","SPCC550.15c","SPCC1450.11c","SPBC577.13","SPAC3A11.03","SPAC637.06","SPAC1F5.09c","SPBC2F12.03c","SPCC306.07c","SPAC823.03","SPCC18.11c","SPBC56F2.08c","SPAC19A8.04","SPBC13E7.09","SPAC17H9.10c","SPAC4A8.05c","SPBC609.02","SPAC20H4.08","SPAC1B3.03c","SPAC23C4.02","SPCC1393.05","SPBC557.04","SPAC328.06","SPAC1952.12c","SPCC548.05c","SPAC22H10.03c","SPAC31F12.01","SPBC530.06c","SPAC9G1.12","SPAC890.03","SPAC10F6.05c","SPAC458.06","SPAC11E3.04c","SPAC22F3.09c","SPCC1450.05c","SPBC18H10.06c","SPAC18G6.02c","SPBC839.13c","SPBC3F6.01c","SPBC211.06","SPCC24B10.18","SPBC27.04","SPAC631.02","SPAC23H4.08","SPBC530.14c","SPAC15A10.11","SPCC1020.05","SPAC1687.14c","SPAC222.15","SPBC11C11.11c","SPAC27F1.06c","SPBC947.10","SPBPB2B2.13","SPBP35G2.06c","SPBC839.03c","SPBC170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source-dependent regulation of the Schizosaccharomyces pombe pbh1 gene.","citation":"J Microbiol 2006 Dec;44(6):689-93","abstract":"Pbh1, from the fission yeast Schizosaccharomyces pombe, is a baculoviral inhibitor of apoptosis (IAP) repeat (BIR) domain-containing protein. Its unique encoding gene was previously found to be regulated by nitric oxide and nitrogen starvation. In the current work, the Pbh1-lacZ fusion gene was used to elucidate the transcriptional regulation of the pbh1 gene under various carbon sources. When fermentable carbon sources, such as glucose (at a low concentration of 0.2%), sucrose (2.0%) and lactose (2.0%), were the sole carbon source, the synthesis of beta-galactosidase from the Pbh1-lacZ fusion gene was reasonably enhanced. However, the induction by these fermentable carbon sources was abolished in the Pap1-negative S. pombe cells, implying that this type of induction of the pbh1 gene is mediated by Pap1. Ethanol (2.0%), a nonfermentable carbon source, was also able to enhance the synthesis of beta-galactosidase from the fusion gene in wild-type cells but not in Pap1-negative cells. The results indicate that the S. pombe pbh1 gene is up-regulated under metabolic oxidative stress in a Pap1-dependent manner.","authors":"Kim SJ, Cho NC, Ryu IW, Kim K, Park EH, Lim CJ","authors_abbrev":"Kim SJ et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2007-01-06","publication_year":"2006","canto_session_key":"d03fa64f02ae05bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-12-04 00:04:26","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-12-04 00:04:16","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC962.02c","SPAC1783.07c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-12-04"},{"uniquename":"PMID:21084840","title":"The Mek1 phosphorylation cascade plays a role in meiotic recombination of Schizosaccharomyces pombe.","citation":"Cell Cycle 2010 Dec 01;9(23):4688-702","abstract":"Mek1 is a Chk2/Rad53/Cds1-related protein kinase that is required for proper meiotic progression of Schizosaccharomyces pombe. However, the molecular mechanisms of Mek1 regulation and Mek1 phosphorylation targets are unclear. Here, we report that Mek1 is phosphorylated at serine-12 (S12), S14 and threonine-15 (T15) by Rad3 (ATR) and/or Tel1 (ATM) kinases that are activated by meiotic programmed double-strand breaks (DSBs). Mutations of these sites by alanine replacement caused abnormal meiotic progression and recombination rates. Phosphorylation of these sites triggers autophosphorylation of Mek1; indeed, alanine replacement mutations of Mek1-T318 and -T322 residues in the activation loop of Mek1 reduced Mek1 kinase activity and meiotic recombination rates. Substrates of Mek1 include Mus81-T275, Rdh54-T6 and Rdh54-T673. Mus81-T275 is known to regulate the Mus81 function in DNA cleavage, whereas Rdh54-T6A/T673A mutant cells showed abnormal meiotic recombination. Taken together, we conclude that the phosphorylation of Mek1 by Rad3 or Tel1, Mek1 autophosphorylation and Mus81 or Rdh54 phosphorylation by Mek1 regulate meiotic progression in S. pombe.","authors":"Tougan T, Kasama T, Ohtaka A, Okuzaki D, Saito TT, Russell P, Nojima H","authors_abbrev":"Tougan T et al.","pubmed_publication_date":"01 Dec 2010","pubmed_entrez_date":"2010-11-19","publication_year":"2010","canto_session_key":"ccbd850b80722817","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takahiro Tougan","canto_first_approved_date":"2016-09-08 13:58:33","canto_approved_date":"2024-04-15 16:08:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-09-03 17:45:34","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":68,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Takahiro Tougan","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPAC15A10.03c","SPAC14C4.03","SPBC216.05","SPCC4G3.05c","SPCC23B6.03c","SPAC22F3.03c","SPAC17A5.11","SPAC22F3.02","SPBC29B5.01"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2016-09-08"},{"uniquename":"PMID:11410325","title":"Role of cAMP-dependent protein kinase in the regulation of DNA repair.","citation":"Cancer Lett 2001 Aug 10;169(1):51-8","abstract":"Enhanced DNA repair is an important factor in drug resistance in cancer. Using cell-free extracts derived from the fission yeast, Schizosaccharomyces pombe, we demonstrate in an in vitro system DNA repair system that increased cAMP levels, which activates cAMP-dependent protein kinase (PKA), inhibits repair of ultraviolet (UV)-damaged DNA. Supplementing the cell-free system with the catalytic kinase subunit of PKA also inhibits DNA repair. In contrast, addition of the PKA inhibitor H-89 enhances repair activity. These results show that PKA regulates DNA repair synthesis, thus implicating the cAMP signaling pathway in DNA damage response and repair of UV-damaged DNA lesions.","authors":"Lee CH, Sidik K, Chin KV","authors_abbrev":"Lee CH et al.","pubmed_publication_date":"10 Aug 2001","pubmed_entrez_date":"2001-06-19","publication_year":"2001","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41542823","title":"Analysis of Treacher Collins syndrome 4-associated mutations in Schizosaccharomyces pombe.","citation":"FEBS Open Bio 2026 Jan 16;","abstract":"Treacher Collins syndrome (TCS) is a rare congenital disorder characterized by craniofacial deformities. Although mutations in several genes involved in ribosome biogenesis have been identified in patients with TCS, the molecular mechanisms underlying their effects remain poorly understood. In this study, we analyzed the effects of TCS type 4 (TCS4)-associated mutations in Schizosaccharomyces pombe by introducing R1022C or R1022S mutations into Rpa2, the second-largest subunit of RNA polymerase I (Pol I). The rpa2 R1022C  and rpa2 R1022S  mutants exhibited impaired cell growth under nutrient-rich conditions without affecting the Rpa2 protein levels. Furthermore, Pol I abnormally accumulated at the 5' region of rDNA in these mutants, resulting in defective 35S pre-rRNA biogenesis and increased sensitivity to the Pol I inhibitor BMH-21. These findings highlight the essential role of the Rpa2 residues associated with TCS4 in rRNA transcription and cell growth.","doi":"10.1002/2211-5463.70152","authors":"Kawakami K, Kato H","authors_abbrev":"Kawakami K et al.","pubmed_publication_date":"16 Jan 2026","pubmed_entrez_date":"2026-01-16","publication_year":"2026","canto_session_key":"86cf66ecead88bdb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-01-17 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP23A10.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:849098","title":"Localization of alpha-Galactomannan on the surface of Schizosaccharomyces pombe cells by scanning electron microscopy.","citation":"Arch Microbiol 1977 Mar 01;112(2):123-6","abstract":"Galactomannan was localized by scanning and transmission electron microscopy on the cells and cell walls of Schizosaccharomyces pombe. The markers were prepared from colloidal gold granules labelled with an alpha-galactopyranosyl-binding lectin isolated from the seeds of Bandeiraea simplicifolia. Part or all of this alpha-galactomannan was present in the outer layer of the cell wall and was uniformly distributed even on the fission scars.","authors":"Horiseberger M, Rosset J","authors_abbrev":"Horiseberger M et al.","pubmed_publication_date":"01 Mar 1977","pubmed_entrez_date":"1977-03-01","publication_year":"1977","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39527211","title":"Identifying Drug Sensitivities in Fission Yeast by Assessing Growth Kinetics.","citation":"Methods Mol Biol 2025;2862:321-331","abstract":"Kinetic assays can detect growth response to changing conditions in fission yeast. This may allow the use of fission yeast in drug library screens. Building upon our other work to examine half-maximal inhibitory concentrations, kinetic curves show direct response of cell populations to varying drug concentrations and conditions. The slope is useful to assess growth rate. Absolute growth height can be used to understand overall culture response and compare between doses or strains. This can be paired with a metabolic screening reagent, CCK8, which detects dehydrogenase activity as a proxy for proliferation. These methods assess time-based changes in fission yeast health and provide inexpensive and high-content alternatives to colony-forming assays.","doi":"10.1007/978-1-0716-4168-2_23","authors":"Sanayhie SA, Sabatinos SA","authors_abbrev":"Sanayhie SA et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7862141","title":"The sak1+ gene of Schizosaccharomyces pombe encodes an RFX family DNA-binding protein that positively regulates cyclic AMP-dependent protein kinase-mediated exit from the mitotic cell cycle.","citation":"Mol Cell Biol 1995 Mar;15(3):1479-88","abstract":"In Schizosaccharomyces pombe, meiosis is initiated by conditions of nutrient deprivation. Mutations in genes encoding elements of the cyclic AMP-dependent protein kinase (cAPK) pathway interfere with meiosis. Loss-of-function alleles of genes that stimulate the activity of cAPK allow cells to bypass the normal requirement of starvation for conjugation and meiosis. Alternatively, loss-of-function alleles of genes that inhibit cAPK lead to the inability to undergo sexual differentiation. The cgs1+ gene encodes the regulatory subunit of cAPK, and the cgs2+ gene encodes a cyclic AMP phosphodiesterase. Thus, both genes encode proteins which negatively regulate the activity of cAPK. Loss of either cgs1 or cgs2 prevents haploid cells from conjugating and diploid cells from undergoing meiosis. In addition to these defects, cells are unable to enter stationary phase. We describe a novel gene, sak1+, which when present on a plasmid overcomes the aberrant phenotypes associated with unregulated cAPK activity. Genetic analysis of sak1+ (suppressor of A-kinase) reveals that it functions downstream of cyclic AMP-dependent protein kinase to allow cells to exist the mitotic cycle and enter either stationary phase or the pathway leading to sexual differentiation. The sak1+ gene is essential for cell viability, and a null allele causes multiple defects in cell morphology and nuclear division. Thus, sak1+ is an important regulatory element in the life cycle of S. pombe. Sequence analysis shows that the predicted product of the sak1+ gene is an 87-kDa protein which shares homology to the RFX family of DNA-binding proteins identified in humans and mice. One member of this family, RFX1, is a transcription factor for a variety of viral and cellular genes.","authors":"Wu SY, McLeod M","authors_abbrev":"Wu SY et al.","pubmed_publication_date":"Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_session_key":"a816cad3073d0712","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-08-26 14:31:01","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-08-26 14:30:13","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.03c","SPAC3G9.14","SPAC8C9.03","SPCC285.09c","SPBC1198.14c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2015-08-26"},{"uniquename":"PMID:21327090","title":"Nuclear envelope attachment is not necessary for telomere function in fission yeast.","citation":"Nucleus 2010;1(6):481-6","abstract":"Inner nuclear membrane (INM) proteins can be important for positioning chromosomes within the nucleus. Little is known about INM proteins in the fission yeast Schizossacharomayces pombe. Telomeres are the most obvious chromosomal sites that are anchored to the nuclear envelope in this organism. A group of proteins that tether telomeres to the spindle-pole body (SPB) during meiotic prophase, such as Bqt1, Bqt2 and Sad1, has been identified previously, but proteins for anchoring telomeres to the nuclear envelope in vegetative cells have not been identified until recently. A recent report demonstrates that Bqt3 and Bqt4 are INM proteins that affect nuclear positioning of telomeres in vegetative cells, and consequently affect the telomere clustering in meiotic prophase. Interestingly, in the absence of Bqt4, telomeres are separated from the nuclear envelope but telomere silencing and telomere length are properly regulated. An important implication of these results is that the functional integrity of telomeres is maintained independently of their connection to the nuclear envelope.","doi":"10.4161/nucl.1.6.13113","authors":"Chikashige Y, Haraguchi T, Hiraoka Y","authors_abbrev":"Chikashige Y et al.","pubmed_publication_date":"2010","pubmed_entrez_date":"2011-02-18","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12796297","title":"Novel Rho GTPase involved in cytokinesis and cell wall integrity in the fission yeast Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2003 Jun;2(3):521-33","abstract":"The Rho family of GTPases is present in all eukaryotic cells from yeast to mammals; they are regulators in signaling pathways that control actin organization and morphogenetic processes. In yeast, Rho GTPases are implicated in cell polarity processes and cell wall biosynthesis. It is known that Rho1 and Rho2 are key proteins in the construction of the cell wall, an essential structure that in Schizosaccharomyces pombe is composed of beta-glucan, alpha-glucan, and mannoproteins. Rho1 regulates the synthesis of 1,3-beta-D-glucan by activation of the 1,3-beta-D-glucan synthase, and Rho2 regulates the synthesis of alpha-glucan by the 1,3-alpha-D-glucan synthase Mok1. Here we describe the characterization of another Rho GTPase in fission yeast, Rho4. rho4Delta cells are viable but display cell separation defects at high temperature. In agreement with this observation, Rho4 localizes to the septum. Overexpression of rho4(+) causes lysis and morphological defects. Several lines of evidence indicate that both rho4(+) deletion or rho4(+) overexpression result in a defective cell wall, suggesting an additional role for Rho4 in cell wall integrity. Rho4Delta cells also accumulate secretory vesicles around the septum and are defective in actin polarization. We propose that Rho4 could be involved in the regulation of the septum degradation during cytokinesis.","authors":"Santos B, Gutiérrez J, Calonge TM, Pérez P","authors_abbrev":"Santos B et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-06-11","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25469537","title":"The interdependence of the Rho GTPases and apicobasal cell polarity.","citation":"Small GTPases 2014;5(2):10","abstract":"Signaling via the Rho GTPases provides crucial regulation of numerous cell polarization events, including apicobasal (AB) polarity, polarized cell migration, polarized cell division and neuronal polarity. Here we review the relationships between the Rho family GTPases and epithelial AB polarization events, focusing on the 3 best-characterized members: Rho, Rac and Cdc42. We discuss a multitude of processes that are important for AB polarization, including lumen formation, apical membrane specification, cell-cell junction assembly and maintenance, as well as tissue polarity. Our discussions aim to highlight the immensely complex regulatory mechanisms that encompass Rho GTPase signaling during AB polarization. More specifically, in this review we discuss several emerging common themes, that include: 1) the need for Rho GTPase activities to be carefully balanced in both a spatial and temporal manner through a multitude of mechanisms; 2) the existence of signaling feedback loops and crosstalk to create robust cellular responses; and 3) the frequent multifunctionality that exists among AB polarity regulators. Regarding this latter theme, we provide further discussion of the potential plasticity of the cell polarity machinery and as a result the possible implications for human disease.","doi":"10.4161/21541248.2014.973768","authors":"Mack NA, Georgiou M","authors_abbrev":"Mack NA et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-12-04","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-12-05 01:15:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25487150","title":"A PP1-PP2A phosphatase relay controls mitotic progression.","citation":"Nature 2015 Jan 01;517(7532):94-98","abstract":"The widespread reorganization of cellular architecture in mitosis is achieved through extensive protein phosphorylation, driven by the coordinated activation of a mitotic kinase network and repression of counteracting phosphatases. Phosphatase activity must subsequently be restored to promote mitotic exit. Although Cdc14 phosphatase drives this reversal in budding yeast, protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) activities have each been independently linked to mitotic exit control in other eukaryotes. Here we describe a mitotic phosphatase relay in which PP1 reactivation is required for the reactivation of both PP2A-B55 and PP2A-B56 to coordinate mitotic progression and exit in fission yeast. The staged recruitment of PP1 (the Dis2 isoform) to the regulatory subunits of the PP2A-B55 and PP2A-B56 (B55 also known as Pab1; B56 also known as Par1) holoenzymes sequentially activates each phosphatase. The pathway is blocked in early mitosis because the Cdk1-cyclin B kinase (Cdk1 also known as Cdc2) inhibits PP1 activity, but declining cyclin B levels later in mitosis permit PP1 to auto-reactivate. PP1 first reactivates PP2A-B55; this enables PP2A-B55 in turn to promote the reactivation of PP2A-B56 by dephosphorylating a PP1-docking site in PP2A-B56, thereby promoting the recruitment of PP1. PP1 recruitment to human, mitotic PP2A-B56 holoenzymes and the sequences of these conserved PP1-docking motifs suggest that PP1 regulates PP2A-B55 and PP2A-B56 activities in a variety of signalling contexts throughout eukaryotes.","doi":"10.1038/nature14019","authors":"Grallert A, Boke E, Hagting A, Hodgson B, Connolly Y, Griffiths JR, Smith DL, Pines J, Hagan IM","authors_abbrev":"Grallert A et al.","pubmed_publication_date":"01 Jan 2015","pubmed_entrez_date":"2014-12-10","publication_year":"2015","canto_session_key":"3c76dc8ec0d97857","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-04-29 13:24:16","canto_approved_date":"2024-07-10 20:43:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-04 14:51:58","canto_added_date":"2014-12-11 01:15:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":31,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.02","SPBC776.02c","SPBC649.05","SPAC227.07c","SPAC23C11.16","SPCC736.14","SPBC16G5.01","SPBC11B10.09","SPAC6F12.12"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2017-04-29"},{"uniquename":"PMID:23861937","title":"Genome-wide screening for genes associated with valproic acid sensitivity in fission yeast.","citation":"PLoS One 2013;8(7):e68738","abstract":"We have been studying the action mechanisms of valproic acid (VPA) in fission yeast Schizosaccharomyces pombe by developing a genetic screen for mutants that show hypersensitivity to VPA. In the present study, we performed a genome-wide screen of 3004 haploid deletion strains and confirmed 148 deletion strains to be VPA sensitive. Of the 148 strains, 93 strains also showed sensitivity to another aliphatic acids HDAC inhibitor, sodium butyrate (SB), and 55 strains showed sensitivity to VPA but not to SB. Interestingly, we found that both VPA and SB treatment induced a marked increase in the transcription activity of Atf1 in wild-type cells. However, in clr6-1, a mutant allele the clr6(+) gene encoding class I HDAC, neither VPA- nor SB induced the activation of Atf1 transcription activity. We also found that VPA, but not SB, caused an increase in cytoplasmic Ca(2+) level. We further found that the cytoplasmic Ca(2+) increase was caused by Ca(2+) influx from extracellular medium via Cch1-Yam8 channel complex. Altogether, our present study indicates that VPA and SB play similar but distinct roles in multiple physiological processes in fission yeast.","doi":"10.1371/journal.pone.0068738","authors":"Zhang L, Ma N, Liu Q, Ma Y","authors_abbrev":"Zhang L et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-18","publication_year":"2013","canto_session_key":"ef5df4274493a38a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-24 14:01:47","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-24 14:01:41","canto_added_date":"2013-07-31 05:32:42","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":448,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_23861937_phaf.tsv"}],"genes":["SPAC8E11.05c","SPAC1071.02","SPAC1F5.05c","SPAC17H9.09c","SPAC19G12.08","SPCC736.07c","SPBC16E9.12c","SPAC630.13c","SPCC126.13c","SPBP4H10.17c","SPBC1778.05c","SPCC74.02c","SPCC364.06","SPCC74.09","SPAC227.01c","SPAC23H4.17c","SPAC19G12.02c","SPBC4F6.10","SPAC140.02","SPBC56F2.08c","SPBC30B4.04c","SPAC23C11.14","SPBC609.04","SPAC29B12.06c","SPBC30B4.06c","SPBC4F6.06","SPAC31G5.18c","SPBC11B10.10c","SPCC31H12.08c","SPBC1105.08","SPBC337.03","SPBC12C2.02c","SPBC1D7.03","SPBC1289.09","SPBC29A3.05","SPBC4F6.11c","SPBC11B10.07c","SPBC215.03c","SPAC1527.02","SPAC18B11.10","SPCC11E10.04","SPAC5D6.09c","SPBC6B1.06c","SPAC6C3.07","SPBC354.07c","SPBC1778.02","SPAC25G10.06","SPBC3H7.03c","SPBC2D10.16","SPBC23E6.08","SPAPB17E12.04c","SPBC530.01","SPAC1071.11","SPCC11E10.06c","SPCPJ732.01","SPBC15D4.02","SPBC16D10.08c","SPAC6G9.15c","SPBC119.08","SPAC9E9.14","SPAC1783.07c","SPBC21D10.10","SPAC1952.02","SPAC1610.02c","SPBC3E7.09","SPBC29A3.10c","SPCC794.03","SPAC23H3.06","SPAC23C11.10","SPBC3B8.03","SPAC22E12.11c","SPCC1393.08","SPBC21C3.02c","SPBC16H5.06","SPAC3H5.08c","SPAPYUG7.04c","SPAC1705.02","SPBC1683.03c","SPBC4F6.12","SPAC10F6.08c","SPBC2F12.12c","SPAC30D11.13","SPCC126.08c","SPBC660.05","SPAC30D11.05","SPAC30C2.02","SPBC1773.12","SPCC895.05","SPCC777.08c","SPBC13E7.08c","SPAC18G6.13","SPAC20H4.03c","SPBC725.09c","SPBC13G1.08c","SPBC359.06","SPCC622.12c","SPAPB1E7.02c","SPAC630.14c","SPAC22F3.13","SPAC25B8.19c","SPBPB2B2.14c","SPAC15A10.11","SPBC1271.10c","SPBC543.07","SPAC12B10.03","SPBC1604.08c","SPAC15E1.06","SPAC6F12.06","SPAC56F8.12","SPBC354.10","SPCC594.05c","SPBC119.12","SPBC106.17c","SPCC757.09c","SPAC1782.01","SPAC144.02","SPBC29A10.16c","SPAC4G8.08","SPAC29B12.11c","SPAC2G11.03c","SPBC30D10.14","SPAC9.02c","SPAC23C4.08","SPAC4G9.13c","SPBC25B2.02c","SPBC2G5.06c","SPCC24B10.11c","SPBP16F5.07","SPBC16D10.07c","SPAC19A8.11c","SPAC1006.03c","SPBC16G5.02c","SPBC1198.03c","SPAC6G9.14","SPCC297.05","SPCC1739.01","SPCC16C4.20c","SPCP1E11.06","SPBC4C3.08","SPBC31F10.02","SPAC6B12.07c","SPAC25B8.05","SPAC8E11.02c","SPAC1687.12c","SPBC3H7.12","SPAC1805.16c","SPAC959.08","SPAC2C4.07c"],"gene_count":148,"ltp_gene_count":0,"approved_date":"2014-07-24"},{"uniquename":"PMID:9760264","title":"Kinetics of dimerization and interactions of p13suc1 with cyclin-dependent kinases.","citation":"Biochemistry 1998 Oct 06;37(40):14257-66","abstract":"The impact of p13suc1 on the conformation and regulation of cyclin-dependent kinases (cdks) and cyclins was investigated by spectroscopic and rapid kinetic approaches. In the absence of phosphorylation on cdks, p13suc1 formed stable complexes, mainly stabilized by hydrophobic interactions, specifically with cdk2 and cdc2. The presence of cyclin A, associated with cdk2 or cdc2, increased the stability of the interaction between cdk2 and p13suc1 by a factor of 2. However, cyclin A did not modify the association rate of p13suc1 to cdk2, but the dissociation rate, which was decreased 3-fold. Moreover, binding of p13suc1 to cdk2 resulted in a 2-fold decrease in the release of nucleotide from cdk2, indicating that p13suc1 induces a marked change in the structure of the nucleotide binding site of cdks. On the basis of the structure of cdk2/CksHs1 complex and on our kinetic results, we propose that the binding of Cks proteins to C-lobe of cdk2 is stabilized by the presence of cyclin A and that it may modify the orientation of the loop carrying residues 14 and 15 and their consequent access for dephosphorylation by cdc25 phosphatases. Finally, we have shown that dimerization of p13suc1 in the presence of zinc abolishes its interaction with cdks, which suggests that the binding of p13suc1 to cdk2 or cdk2/cyclin A may be regulated by dimerization of p13suc1 in vivo.","authors":"Morris MC, Heitz F, Divita G","authors_abbrev":"Morris MC et al.","pubmed_publication_date":"06 Oct 1998","pubmed_entrez_date":"1998-10-07","publication_year":"1998","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24131582","title":"Autosomal recessive axonal neuropathy with neuromyotonia: a rare entity.","citation":"Pediatr Neurol 2014 Jan;50(1):104-7","abstract":"Autosomal recessive axonal neuropathy with neuromyotonia is a recently described entity associated to the HINT1 gene, encoding histidine triad nucleotide-binding protein 1.\nThe authors report a Portuguese 16-year-old girl of Roma ethnicity, descendant of consanguineous parents, with progressive distal muscular atrophy and weakness, beginning at age 6. After several years of extensive investigation with inconclusive results, clinical myotonia was identified. Electrophysiologic studies revealed neuromyotonia associated with a severe chronic predominantly motor axonal neuropathy and homozygous mutation (c.334 C > A, p.H112 N) in HINT1 was detected.\nThis report emphasizes the late onset of clinical myotonia essential to the diagnosis.","doi":"10.1016/j.pediatrneurol.2013.08.028","authors":"Caetano JS, Costa C, Baets J, Zimon Phd M, Venâncio Phd M, Saraiva Phd J, Negrão L, Fineza I","authors_abbrev":"Caetano JS et al.","pubmed_publication_date":"Jan 2014","pubmed_entrez_date":"2013-10-18","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1442.14c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:33049028","title":"Schizosaccharomyces pombe Ppr10 is required for mitochondrial translation.","citation":"FEMS Microbiol Lett 2020 Oct 21;367(19)","abstract":"The mitochondrial genome encodes key components of the oxidative phosphorylation (OXPHOS) system, whose expression is essential for mitochondrial functions. We have previously shown that deletion of the Schizosaccharomyces pombe ppr10 encoding a pentatricopeptide repeat protein severely reduces the mature levels of intron-containing mitochondrial transcripts cox1 and cob1, and severely impairs mitochondrial translation. In this study, we examined the possibility that the reduced levels of Cox1 and Cob1 proteins in cells were due to lowered levels of cox1 and cob1 mRNAs. We found that deletion of ppr10 did not affect the levels of mature cox1 and cob1 mRNAs in a mitochondrial intronless background. However, synthesis of Cox1 and Cob1 proteins were still severely affected by deletion of ppr10 in a mitochondrial intronless background. Consistent with this, we found that deletion of mitochondrial introns could not rescue the respiratory growth defect of Δppr10 cells. Our results reveal that Ppr10 is not required for the stability of cox1 and cob1 mRNAs, and provide further support for the idea that Ppr10 plays a critical role in mitochondrial translation.","doi":"10.1093/femsle/fnaa170","authors":"Liu Z, Li Y, Xie W, Huang Y","authors_abbrev":"Liu Z et al.","pubmed_publication_date":"21 Oct 2020","pubmed_entrez_date":"2020-10-13","publication_year":"2020","canto_session_key":"0985d9c7ca7f7a05","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2021-02-08 16:31:25","canto_approved_date":"2021-02-08 16:31:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-05 11:44:27","canto_added_date":"2020-10-15 00:15:07","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPMIT.07","SPMIT.08","SPMIT.09","SPMIT.01","SPBC106.19","SPMIT.10","SPMIT.11","SPMIT.05","SPMIT.04"],"gene_count":9,"ltp_gene_count":1,"approved_date":"2021-02-08"},{"uniquename":"PMID:2795654","title":"Schizosaccharomyces pombe U4 small nuclear RNA closely resembles vertebrate U4 and is required for growth.","citation":"J Mol Biol 1989 Aug 05;208(3):371-9","abstract":"The single-copy gene snu4, which encodes the small nuclear RNA (snRNA) U4, has been cloned and sequenced. Schizosaccharomyces pombe U4 is 128 nucleotides in length, similar in size to vertebrate U4 and shows substantial primary and secondary structure homology. The gene lacks sequences closely resembling vertebrate snRNA transcription signals, but has a TATA box at -33 to -30; TATA sequences flanked by several additional conserved nucleotides are found in the same position in the 5' regions of other snRNA genes from Schiz. pombe. The cloned snu4 gene was disrupted by transposon mutagenesis and used to replace one chromosomal copy of snu4 in a diploid strain. On sporulation snu4- haploid strains could not be recovered, demonstrating that U4 is required, at least for spore germination. Haploid snu4- strains are viable if they also carry snu4+ on a replicating plasmid but are unable to loose the plasmid under non-selective growth, demonstrating a continuous requirement for U4 for viability.","authors":"Dandekar T, Ribes V, Tollervey D","authors_abbrev":"Dandekar T et al.","pubmed_publication_date":"05 Aug 1989","pubmed_entrez_date":"1989-08-05","publication_year":"1989","canto_session_key":"9ef19b84bfc2287a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 15:48:40","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-19 13:56:40","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.06","SPSNRNA.04"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2014-06-19"},{"uniquename":"PMID:19117951","title":"Interaction of APC/C-E3 ligase with Swi6/HP1 and Clr4/Suv39 in heterochromatin assembly in fission yeast.","citation":"J Biol Chem 2009 Mar 13;284(11):7165-76","abstract":"Heterochromatin assembly in fission yeast is initiated by binding of Swi6/HP1 to the Lys-9-dimethylated H3 followed by spreading via cooperative recruitment of Swi6/HP1. Recruitment of Cohesin by Swi6/HP1 further stabilizes the heterochromatin structure and integrity. Subsequently, polyubiquitylation of Cut2 by anaphase-promoting complex-cyclosome (APC/C)-ubiquitin-protein isopeptide ligase (E3 ligase) followed by degradation of Cut2 releases Cut1, which cleaves the Rad21 subunit of Cohesin, facilitating sister chromatid separation during mitosis. Here, we demonstrate a surprising role of APC/C in assembly of heterochromatin and silencing at mating type, centromere, and ribosomal DNA loci. Coincidentally with the loss of silencing, recruitment of Swi6, H3-Lys-9-Me2, and Clr4 at dg-dh repeats at cen1 and the K region of mat locus is abrogated in mutants cut4, cut9, and nuc2. Surprisingly, both Cut4 and Cut9 are also highly enriched at these regions in wild type and depleted in swi6Delta mutant. Cut4 and Cut9 interact directly with Swi6/HP1 and Clr4, whereas the mutant Cut4 does not, suggesting that a direct physical interaction of APC subunits Cut4 and Cut9 with Swi6 and Clr4 is instrumental in heterochromatin assembly. The silencing defect in APC mutants is causally related to ubiquitylation activity of APC-E3 ligase. Like swi6 mutant, APC mutants are also defective in Cohesin recruitment and exhibit defects like lagging chromosomes, chromosome loss, and aberrant recombination in the mat region. In addition, APC mutants exhibit a bidirectional expression of dh repeats, suggesting a role in the RNA interference pathway. Thus, APC and heterochromatin proteins Swi6 and Clr4 play a mutually cooperative role in heterochromatin assembly, thereby ensuring chromosomal integrity, inheritance, and segregation during mitosis and meiosis.","doi":"10.1074/jbc.M806461200","authors":"Dubey RN, Nakwal N, Bisht KK, Saini A, Haldar S, Singh J","authors_abbrev":"Dubey RN et al.","pubmed_publication_date":"13 Mar 2009","pubmed_entrez_date":"2009-01-02","publication_year":"2009","canto_session_key":"00d5ca171998803c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-04-29 13:10:06","canto_approved_date":"2026-01-29 12:30:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-29 13:09:22","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":39,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC664.01c","SPCC338.17c","SPAC17C9.01c","SPBC106.09","SPBC14C8.01c","SPAC6F12.15c"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2017-04-29"},{"uniquename":"PMID:3221399","title":"DNA sequence analysis of the ade6 gene of Schizosaccharomyces pombe. Wild-type and mutant alleles including the recombination host spot allele ade6-M26.","citation":"J Mol Biol 1988 Dec 20;204(4):917-25","abstract":"The gene ade6 is located on chromosome III of the fission yeast Schizosaccharomyces pombe. It codes for the enzyme phosphoribosylaminoimidazole carboxylase involved in purine biosynthesis. A DNA fragment of 3043 nucleotides has been sequenced. It complements ade6 mutations when present on plasmids. An uninterrupted open reading frame of 552 amino acid residues was identified. A method for the cloning of chromosomal mutations by repair of gapped replication vectors in vivo has been developed. Twelve ade6 mutant alleles have been isolated. The sequence alterations of four mutant alleles have been determined. Among them are the ade6-M26 recombination hot spot mutation and the nearby ade6-M375 control mutation. Both are G to T base substitutions, converting adjacent glycine codons to TGA termination codons. They are suppressed by defined tRNA nonsense suppressors of the UGA type. The ade6-M26 mutation leads to a tenfold increase of the occurrence of conversion tetrads in comparison with other ade6 mutations. Possible explanations for the M26-induced increase of recombination frequency are discussed in relation to specific features of the nucleotide sequence identified in the region of the M26 mutation.","authors":"Szankasi P, Heyer WD, Schuchert P, Kohli J","authors_abbrev":"Szankasi P et al.","pubmed_publication_date":"20 Dec 1988","pubmed_entrez_date":"1988-12-20","publication_year":"1988","canto_session_key":"b7cd44c1f2b3e5bd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-22 17:36:12","canto_approved_date":"2019-06-11 11:47:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-30 10:52:58","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1322.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-03-22"},{"uniquename":"PMID:12951601","title":"Deletion of Mia1/Alp7 activates Mad2-dependent spindle assembly checkpoint in fission yeast.","citation":"Nat Cell Biol 2003 Sep;5(9):764-6; author reply 766","abstract":"","authors":"Sato M, Koonrugsa N, Toda T, Vardy L, Tournier S, Millar JB","authors_abbrev":"Sato M et al.","pubmed_publication_date":"Sep 2003","pubmed_entrez_date":"2003-09-03","publication_year":"2003","canto_session_key":"f4d5b599093ab44e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-26 11:47:33","canto_approved_date":"2021-06-18 15:49:31","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-01-30 18:24:39","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.01c","SPAC890.02c","SPBC3D6.04c","SPBC20F10.06","SPCC1322.12c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-01-26"},{"uniquename":"PMID:27756188","title":"cAMP-dependent protein kinase involves calcium tolerance through the regulation of Prz1 in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2017 Feb;81(2):231-241","abstract":"The cAMP-dependent protein kinase Pka1 is known as a regulator of glycogenesis, meiosis, and stress responses in Schizosaccharomyces pombe. We demonstrated that Pka1 is responsible for calcium tolerance. Loss of functional components of the PKA pathway such as Git3, Gpa2, Cyr1, and Pka1 yields a CaCl 2 -sensitive phenotype, while loss of Cgs1, a regulatory subunit of PKA, results in CaCl 2  tolerance. Cytoplasmic distribution of Cgs1 and Pka1 is increased by the addition of CaCl 2 , suggesting that CaCl 2  induces dissociation of Cgs1 and Pka1. The expression of Prz1, a transcriptional regulator in calcium homeostasis, is elevated in a pka1∆ strain and in a wild type strain under glucose-limited conditions. Accordingly, higher expression of Prz1 in the wild type strain results in a CaCl 2 -sensitive phenotype. These findings suggest that Pka1 is essential for tolerance to exogenous CaCl 2 , probably because the expression level of Prz1 needs to be properly regulated by Pka1.","doi":"10.1080/09168451.2016.1246171","authors":"Matsuo Y, Kawamukai M","authors_abbrev":"Matsuo Y et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-10-21","publication_year":"2017","canto_session_key":"d3c8f98508a05f51","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_approved_date":"2017-01-17 10:34:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-12-28 06:36:06","canto_added_date":"2016-10-22 00:15:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10","SPAC8C9.03","SPAC24B11.06c","SPAC23H3.13c","SPBC19C7.03","SPCC1753.02c","SPAC4G8.13c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-12-28"},{"uniquename":"PMID:15607976","title":"Two RNAi complexes, RITS and RDRC, physically interact and localize to noncoding centromeric RNAs.","citation":"Cell 2004 Dec 17;119(6):789-802","abstract":"RNAi-mediated heterochromatin assembly in fission yeast requires the RNA-induced transcriptional silencing (RITS) complex and a putative RNA-directed RNA polymerase (Rdp1). Here we show that Rdp1 is associated with two conserved proteins, Hrr1, an RNA helicase, and Cid12, a member of the polyA polymerase family, in a complex that has RNA-directed RNA polymerase activity (RDRC, RNA-directed RNA polymerase complex). RDRC physically interacts with RITS in a manner that requires the Dicer ribonuclease (Dcr1) and the Clr4 histone methyltransferase. Moreover, both complexes are localized to the nucleus and associate with noncoding centromeric RNAs in a Dcr1-dependent manner. In cells lacking Rdp1, Hrr1, or Cid12, RITS complexes are devoid of siRNAs and fail to localize to centromeric DNA repeats to initiate heterochromatin assembly. These findings reveal a physical and functional link between Rdp1 and RITS and suggest that noncoding RNAs provide a platform for siRNA-dependent localization of RNAi complexes to specific chromosome regions.","authors":"Motamedi MR, Verdel A, Colmenares SU, Gerber SA, Gygi SP, Moazed D","authors_abbrev":"Motamedi MR et al.","pubmed_publication_date":"17 Dec 2004","pubmed_entrez_date":"2004-12-21","publication_year":"2004","canto_session_key":"29d94bfa44bcdf74","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-06-18 15:16:30","canto_approved_date":"2025-04-24 10:53:47","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-06-15 21:01:35","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":31,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1B1.01","SPCC188.13c","SPBC83.03c","SPCC1739.03","SPAC6F12.09","SPBC428.08c","SPCC663.12","SPAC18G6.02c","SPCC736.11"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2024-06-18"},{"uniquename":"PMID:28935259","title":"Module-based systematic construction of plasmids for episomal gene expression in fission yeast.","citation":"Gene 2017 Dec 30;637:14-24","abstract":"The fission yeast Schizosaccharomyces pombe is a powerful model organism for cell biology and molecular biology, as genetic manipulation is easily achieved. Introduction of exogenous genes cloned in episomal plasmids into yeast cells can be done through well-established transformation methods. For expression of genes in S. pombe cells, the multi-copy plasmid pREP1 and its derivatives, including pREP41 and pREP81, have been widely used as vectors. Although recent advancement of technology brought a number of useful genetic elements such as new promoters, selection marker genes and fluorescent protein tags, introduction of those elements into conventional pREP1 requires a large commitment of both time and effort because cloning procedures need to be repeated until the final products are constructed. Here, we introduce materials and methods to construct many pREP1-type plasmids easily and systematically using the Golden Gate shuffling method, which enables one-step ligation of many DNA fragments into a plasmid. These materials and methods support creation of expression plasmids employing a variety of novel genetic elements, which will further facilitate genetic studies using S. pombe.","doi":"10.1016/j.gene.2017.09.030","authors":"Kiriya K, Tsuyuzaki H, Sato M","authors_abbrev":"Kiriya K et al.","pubmed_publication_date":"30 Dec 2017","pubmed_entrez_date":"2017-09-23","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-09-24 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17996697","title":"Ctp1/CtIP and the MRN complex collaborate in the initial steps of homologous recombination.","citation":"Mol Cell 2007 Nov 09;28(3):351-2","abstract":"In a recent issue of Molecular Cell, Limbo et al. (2007) identify a new homologous recombination factor, Ctp1 in S. pombe, a homolog of Sae2/Com1 in S. cerevisiae and CtIP in mammals, that operates cooperatively with the MRN complex.","authors":"Takeda S, Nakamura K, Taniguchi Y, Paull TT","authors_abbrev":"Takeda S et al.","pubmed_publication_date":"09 Nov 2007","pubmed_entrez_date":"2007-11-13","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17363901","title":"Hob3p, the fission yeast ortholog of human BIN3, localizes Cdc42p to the division site and regulates cytokinesis.","citation":"EMBO J 2007 Apr 04;26(7):1865-77","abstract":"Cdc42 GTPase is required for polarization in eukaryotic cells, but its spatial regulation is poorly understood. In Schizosaccharomyces pombe, Cdc42p is activated by Scd1p and Gef1p, two guanine-nucleotide exchange factors. Two-hybrid screening identified Hob3p as a Gef1p binding partner. Hob3p is a BAR domain-containing protein ortholog of human Bin3. Hob3p also interacts directly with Cdc42p independently of Gef1p. Hob3p, Cdc42p and Gef1p form a complex, and Hob3p facilitates Gef1p-Cdc42p interaction and activation. Hob3p forms a ring in the division area, similar to that of Gef1p. This localization requires actin polymerization and Cdc15p but is independent of the septation initiation network. Hob3p is required for the concentration of Cdc42p to the division area. The actomyosin ring contraction is slower in hob3Delta than in wild-type cells, and this contributes to its cytokinesis defect. Moreover, this report extends previous evidence that human Bin3 suppresses the cytokinesis phenotype of hob3Delta cells, showing that Bin3 can partially recover the GTP-Cdc42p level and its localization. These results suggest that Hob3p is required to recruit and activate Cdc42p at the cell division site and that this function might be conserved in other eukaryotes.","authors":"Coll PM, Rincon SA, Izquierdo RA, Perez P","authors_abbrev":"Coll PM et al.","pubmed_publication_date":"04 Apr 2007","pubmed_entrez_date":"2007-03-17","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC110.03","SPBC725.09c","SPAC24H6.09"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:2263480","title":"Glycerol-3-phosphate dehydrogenase homologue from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1990 Dec 11;18(23):7145","abstract":"","authors":"Pidoux AL, Fawell EH, Armstrong J","authors_abbrev":"Pidoux AL et al.","pubmed_publication_date":"11 Dec 1990","pubmed_entrez_date":"1990-12-11","publication_year":"1990","canto_session_key":"3d2efe633eaaf7b9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:40:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-24 18:54:05","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2013-01-24"},{"uniquename":"PMID:2900761","title":"Four mating-type genes control sexual differentiation in the fission yeast.","citation":"EMBO J 1988 May;7(5):1537-47","abstract":"The mating-type region of fission yeast consists of three components, mat1, mat2-P and mat3-M, each separated by 15 kb. Cell-type is determined by the alternate allele present at mat1, either P in an h+ or M in an h- cell. mat2-P and mat3-M serve as donors of information that is transposed to mat1 during a switch of mating type. We have determined the nucleotide sequence of each component of mat. The P and M specific regions are 1104 and 1128 bp, respectively, and bounded by sequences common to each mating-type cassette (H1; 59 bp and H2; 135 bp). A third sequence is present at mat2-P and mat3-M but absent at mat1 (H3; 57 bp), and may be involved in transcriptional repression of these cassettes. mat1-P and mat1-M each encode two genes (Pc; 118 amino acids, Pi; 159 amino acids, Mc; 181 amino acids and Mi; 42 amino acids). Introduction of opal or frame-shift mutations into the open-reading-frame of each gene revealed that Pc and Mc are necessary and sufficient for mating and confer an h+ or h- mating type respectively. All four genes are required for meiotic competence in an h+/h- diploid. The transcription of each mat gene is strongly influenced by nutritional conditions and full induction was observed only in nitrogen-free medium. The predicted product of the Pi gene contains a region of homology with the homeobox sequence, suggesting that this gene encodes a DNA binding protein that directly regulates the expression of other genes.","authors":"Kelly M, Burke J, Smith M, Klar A, Beach D","authors_abbrev":"Kelly M et al.","pubmed_publication_date":"May 1988","pubmed_entrez_date":"1988-05-01","publication_year":"1988","canto_session_key":"5289777e56b6c6be","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 13:15:30","canto_approved_date":"2026-04-08 07:37:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-18 10:22:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC23G7.17c","SPBC23G7.09","SPMTR.02","SPMTR.01"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-06-10"},{"uniquename":"EMBL:AU011189","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:42132940","title":"Chromosome segregation synchrony in S. pombe is noise limited and arises without positive feedback.","citation":"J Cell Biol 2026 Jul 06;225(7)","abstract":"Anaphase is a key cell cycle transition that ensures faithful genome inheritance. At anaphase onset, sister chromatids separate abruptly and synchronously upon activation of the protease separase. Major cell cycle transitions often involve positive feedback, which contributes to their abruptness and irreversibility; however, whether such feedback is required for anaphase remains unclear. Here, we analyze sister chromatid separation dynamics in fission yeast using high-resolution live-cell imaging and computational modeling. We find that anaphase synchrony relies on fast degradation of the separase inhibitor securin but does not require separase-mediated positive feedback. Hence, sister chromatid separation, being inherently irreversible, may be one of the few major cell cycle transitions that can proceed without positive feedback. A stochastic model fitted to the data revealed that separation synchrony is limited by stochasticity resulting from small-number effects. Together, these results support a feedback-independent mechanism for anaphase onset and identify molecular noise as a fundamental constraint on its temporal precision.","doi":"10.1083/jcb.202602088","authors":"Williams W, Phan K, Chen J, Legewie S, Kamenz J, Hauf S","authors_abbrev":"Williams W et al.","pubmed_publication_date":"06 Jul 2026","pubmed_entrez_date":"2026-05-14","publication_year":"2026","canto_session_key":"96b8cf58649f1852","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-05-14 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7614549","title":"Construction of a marker gene cassette which is repeatedly usable for gene disruption in yeast.","citation":"Curr Genet 1995 Mar;27(4):293-7","abstract":"A disruption cassette has been constructed containing the LEU2 gene flanked by directly repeated site-specific recombination sites of the yeast plasmid, pSB3, which resembles the 2 microns DNA of Saccharomyces cerevisiae. A disruption constructed by inserting this DNA fragment acquires a Leu+ phenotype, which can be easily removed by expressing the FLP-PSB3 gene encoding the site-specific recombinase of pSB3. A test was made using a Schizosaccharomyces pombe host. The ura4+ gene of S. pombe was replaced with the ura4::LEU2 gene constructed by inserting the disruption cassette into the ura4+ gene. Then, the FLP-pSB3 gene driven by the nmt1+ promoter was introduced into this disruptant. Upon de-repression of the nmt1 promoter by removing thiamine from the medium, the rate of appearance of Leu- was increased. As expected the ura4+ locus underwent a structural change. Thus, the FLP-pSB3 protein and its target site can function adequately in S. pombe.","authors":"Toh-e A","authors_abbrev":"Toh-e A","pubmed_publication_date":"Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU010941","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9857180","title":"Fission yeast Csk1 is a CAK-activating kinase (CAKAK).","citation":"EMBO J 1998 Dec 15;17(24):7230-8","abstract":"Cell cycle progression is dependent on the sequential activity of cyclin-dependent kinases (CDKs). For full activity, CDKs require an activating phosphorylation of a conserved residue (corresponding to Thr160 in human CDK2) carried out by the CDK-activating kinase (CAK). Two distinct CAK kinases have been described: in budding yeast Saccharomyces cerevisiae, the Cak1/Civ1 kinase is responsible for CAK activity. In several other species including human, Xenopus, Drosophila and fission yeast Schizosaccharomyces pombe, CAK has been identified as a complex homologous to CDK7-cyclin H (Mcs6-Mcs2 in fission yeast). Here we identify the fission yeast Csk1 kinase as an in vivo activating kinase of the Mcs6-Mcs2 CAK defining Csk1 as a CAK-activating kinase (CAKAK).","authors":"Hermand D, Pihlak A, Westerling T, Damagnez V, Vandenhaute J, Cottarel G, Mäkelä TP","authors_abbrev":"Hermand D et al.","pubmed_publication_date":"15 Dec 1998","pubmed_entrez_date":"1998-12-19","publication_year":"1998","canto_session_key":"086398e75ff8af16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-03-29 13:40:57","canto_approved_date":"2021-07-16 08:16:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-17 08:35:45","canto_added_date":"2012-02-24 05:53:01","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.06c","SPBC19F8.07","SPBP16F5.02"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-03-29"},{"uniquename":"PMID:24240238","title":"Elimination of shelterin components bypasses RNAi for pericentric heterochromatin assembly.","citation":"Genes Dev 2013 Nov 15;27(22):2489-99","abstract":"The RNAi pathway is required for heterochromatin assembly at repetitive DNA elements in diverse organisms. In fission yeast, loss of RNAi causes pericentric heterochromatin defects, compromising gene silencing and chromosome segregation. Here we show that deletion of telomere shelterin components restores pericentric heterochromatin and its functions in RNAi mutants. We further isolated a separation-of-function mutant of Poz1 and revealed that defective telomere silencing, but not telomere length control, is critical for bypassing RNAi. Further analyses demonstrated that compromising shelterin-mediated heterochromatin assembly in RNAi mutants releases heterochromatin protein Swi6, which is redistributed to pericentric regions through RNAi-independent heterochromatin assembly pathways. Given the high mobility of Swi6 protein and that increased levels of Swi6 facilitates heterochromatin spreading as well as ectopic heterochromatin assembly, our results suggest that constitutive heterochromatin domains use multiple pathways to form high-affinity platforms to restrain Swi6, thus limiting its availability and avoiding promiscuous heterochromatin formation.","doi":"10.1101/gad.226118.113","authors":"Tadeo X, Wang J, Kallgren SP, Liu J, Reddy BD, Qiao F, Jia S","authors_abbrev":"Tadeo X et al.","pubmed_publication_date":"15 Nov 2013","pubmed_entrez_date":"2013-11-19","publication_year":"2013","canto_session_key":"f5f173fa6df509a1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Songtao Jia","canto_first_approved_date":"2018-04-17 11:00:30","canto_approved_date":"2024-06-07 16:37:38","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-07-13 21:15:50","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":168,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Songtao Jia","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC188.13c","SPAC18G6.02c","SPAC13G7.07","SPAC26H5.06","SPAC19G12.13c","SPBC16D10.07c","SPAC6F12.09","SPCC188.07","SPBC800.03","SPBC28F2.12","SPAC31G5.18c","SPBC428.08c","SPAC664.01c","SPCC338.17c","SPCC736.11","SPAC16A10.07c","SPBC29A3.14c","SPBC1778.02","SPAC6F6.16c"],"gene_count":19,"ltp_gene_count":17,"approved_date":"2018-04-17"},{"uniquename":"PMID:23115244","title":"Cells lacking pfh1, a fission yeast homolog of mammalian frataxin protein, display constitutive activation of the iron starvation response.","citation":"J Biol Chem 2012 Dec 14;287(51):43042-51","abstract":"Friedreich ataxia is a genetic disease caused by deficiencies in frataxin. This protein has homologs not only in higher eukaryotes but also in bacteria, fungi, and plants. The function of this protein is still controversial. We have identified a frataxin homolog in fission yeast, and we have analyzed whether its depletion leads to any of the phenotypes observed in other organisms. Cells deleted in pfh1 are sensitive to growth under aerobic conditions, display increased levels of total iron, hallmarks of oxidative stress such as protein carbonylation, decreased aconitase activity, and lower levels of oxygen consumption compared with wild-type cells. This mitochondrial protein seems to be important for iron and/or reactive oxygen species homeostasis. We have analyzed the proteome of cells devoid of Pfh1, and we determined that gene products up- and down-regulated upon iron depletion in wild-type cells are constitutively misregulated in this mutant. Because of the particular signaling pathway components governing the iron starvation response in fission yeast, our experiments suggest that cells lacking Pfh1 display a decrease of cytosolic available iron that triggers activation of Grx4, the common regulator of the iron starvation gene expression program. Our Schizosaccharomyces pombe Δpfh1 strain constitutes a new and useful model system to study Friedreich ataxia.","doi":"10.1074/jbc.M112.421735","authors":"Gabrielli N, Ayté J, Hidalgo E","authors_abbrev":"Gabrielli N et al.","pubmed_publication_date":"14 Dec 2012","pubmed_entrez_date":"2012-11-02","publication_year":"2012","canto_session_key":"1f78fe7de80af20c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-09-06 14:14:58","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-03-15 16:30:00","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":55,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3F6.03","SPBC1683.10c","SPBC16E9.01c","SPAC24B11.06c","SPCC1183.03c","SPBC26H8.06","SPAC3C7.14c","SPBC609.04","SPAC1F8.03c","SPAC7D4.07c","SPAC23E2.01","SPCC645.03c","SPCC663.08c","SPAC1F7.08","SPAC1783.07c","SPCC576.03c"],"gene_count":16,"ltp_gene_count":5,"approved_date":"2013-03-15"},{"uniquename":"PMID:16079915","title":"The DASH complex and Klp5/Klp6 kinesin coordinate bipolar chromosome attachment in fission yeast.","citation":"EMBO J 2005 Aug 17;24(16):2931-43","abstract":"We identified a truncated allele of dam1 as a multicopy suppressor of the sensitivity of cdc13-117 (cyclin B) and mal3-1 (EB-1) cells to thiabendazole, a microtubule poison. We find that Dam1 binds to the plus end of spindle microtubules and kinetochores as cells enter mitosis and this is dependent on other components of the fission yeast DASH complex, including Ask1, Duo1, Spc34 and Dad1. By contrast, Dad1 remains bound to kinetochores throughout the cell cycle and its association is dependent on the Mis6 and Mal2, but not Mis12, Nuf2 or Cnp1, kinetochore proteins. In cells lacking Dam1, or other components of the DASH complex, anaphase is delayed due to activation of the spindle assembly checkpoint and lagging sister chromatids are frequently observed and occasionally sister chromatid pairs segregate to the same spindle pole. We find that the mitotic centromere-associated Klp5/Klp6 kinesin complex is essential in cells lacking components of the DASH complex. Cells lacking both Dam1 and Klp5 undergo a first cell cycle arrest in mitosis due to a failure to establish bipolar chromosome attachment.","authors":"Sanchez-Perez I, Renwick SJ, Crawley K, Karig I, Buck V, Meadows JC, Franco-Sanchez A, Fleig U, Toda T, Millar JB","authors_abbrev":"Sanchez-Perez I et al.","pubmed_publication_date":"17 Aug 2005","pubmed_entrez_date":"2005-08-05","publication_year":"2005","canto_session_key":"9106d45ba943a620","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-04-06 13:27:39","canto_approved_date":"2023-06-10 07:23:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-16 10:57:19","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":47,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.15c","SPAC16A10.05c","SPAC17A5.09c","SPCC1322.12c","SPBC1105.17","SPAC589.08c","SPBC20F10.06","SPBC776.02c","SPAC27F1.04c","SPBC27.02c","SPBC32F12.08c","SPBC409.04c","SPAC18G6.15","SPBC2F12.13","SPBC582.03","SPAC25B8.14","SPAC1687.20c","SPAC8C9.17c"],"gene_count":18,"ltp_gene_count":14,"approved_date":"2016-04-06"},{"uniquename":"PMID:29017047","title":"Cell Biology: Capturing Formin's Mechano-Inhibition.","citation":"Curr Biol 2017 Oct 09;27(19):R1078-R1080","abstract":"Formins polymerize actin filaments for the cytokinetic contractile ring. Using in vitro reconstitution of fission yeast contractile ring precursor nodes containing formins and myosin, a new study shows that formin-mediated polymerization is strongly inhibited upon the capture and pulling of actin filaments by myosin, a result that has broad implications for cellular mechanosensing.","doi":"10.1016/j.cub.2017.08.020","authors":"Vavylonis D, Horan BG","authors_abbrev":"Vavylonis D et al.","pubmed_publication_date":"09 Oct 2017","pubmed_entrez_date":"2017-10-11","publication_year":"2017","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2017-10-12 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38778900","title":"CRISPR-Cas9 editing efficiency in fission yeast is not limited by homology search and is improved by combining gap-repair with fluoride selection.","citation":"MicroPubl Biol 2024;2024","abstract":"Protocols for CRISPR-Cas9 editing have been implemented in most model organisms, including fission yeast, for which some improvements have also been later described. Here, we report an improvement to the CRISPR-Cas9 protocol in fission yeast, as we combine a cloning free gap-repair method with our previously described fluoride selection marker, which speeds up genome editing. We also report a wide variability of editing efficiencies at different loci along the genome, and we demonstrate that this variability cannot be explained by the location of the edited sequences in the genome. Lastly, our attempt at improving editing efficiency by targeting the donor DNA to the cut site using a HaloTag strategy to link the donor DNA to two proteins of the homologous recombination repair machinery ( Rad51 or Rad52 ) fell short, which shows that editing efficiency in fission yeast is likely not limited by homology search.","doi":"10.17912/micropub.biology.001191","authors":"Fernandez R, Berro J","authors_abbrev":"Fernandez R et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-05-23","publication_year":"2024","canto_session_key":"d46d1ba4e8ebd921","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-05-23 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1193372","title":"A new type of mutation in Schizosaccharomyces pombe: vegetative iodine reaction.","citation":"Genetics 1975 Aug;80(4):711-4","abstract":"Colonies of Schizosaccharomyces pombe that contain ascospores (e.g., colonies of homothallic strains) turn black after treatment with iodine vapors. Heterothallic strains of S. pombe normally do not show this reaction. In experiments with the latter strains we found mutants which exhibit a positive iodine reaction though they do not contain ascospores. This phenotype is due to mutations in a new gene, vir1 (vegatative iodine reaction). The vir1 locus is not linked with the mating-type genes.--Strains of mating-type h-S are known not to give any spontaneous mating-type mutations. Mating-type mutations were also not found after treatment with nitrous acid.","authors":"Meade JH, Gutz H","authors_abbrev":"Meade JH et al.","pubmed_publication_date":"Aug 1975","pubmed_entrez_date":"1975-08-01","publication_year":"1975","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10704373","title":"A checkpoint that monitors cytokinesis in Schizosaccharomyces pombe.","citation":"J Cell Sci 2000 Apr;113 ( Pt 7):1223-30","abstract":"Cell division in Schizosaccharomyces pombe is achieved through the use of a medially positioned actomyosin ring. A division septum is formed centripetally, concomitant with actomyosin ring constriction. Genetic screens have identified mutations in a number of genes that affect actomyosin ring or septum assembly. These cytokinesis-defective mutants, however, undergo multiple S and M phases and die as elongated cells with multiple nuclei. Recently, we have shown that a mutant allele of the S. pombe drc1(+)/cps1(+) gene, which encodes a 1,3-(beta)-glucan synthase subunit, is defective in cytokinesis but displays a novel phenotype. drc1-191/cps1-191 cells are capable of assembling actomyosin rings and completing mitosis, but are incapable of assembling the division septum, causing them to arrest as binucleate cells with a stable actomyosin ring. Each nucleus in arrested cps1-191 cells is able to undergo S phase but these G(2) nuclei are significantly delayed for entry into the M phase. In this study we have investigated the mechanism that causes cps1-191 to block with two G(2) nuclei. We show that the inability of cps1-191 mutants to proceed through multiple mitotic cycles is not related to a defect in cell growth. Rather, the failure to complete some aspect of cytokinesis may prevent the G(2)/M transition of the two interphase-G(2) nuclei. The G(2)/M transition defect of cps1-191 mutants is suppressed by a mutation in the wee1 gene and also by the dominant cdc2 allele cdc2-1w, but not the cdc2-3w allele. Transient depolymerization of all F-actin structures also allowed a significant proportion of the cps1-191 cells to undergo a second round of mitosis. We conclude that an F-actin and Wee1p dependent checkpoint blocks G(2)/M transition until previous cytokinesis is completed.","authors":"Liu J, Wang H, Balasubramanian MK","authors_abbrev":"Liu J et al.","pubmed_publication_date":"Apr 2000","pubmed_entrez_date":"2000-03-08","publication_year":"2000","canto_session_key":"0e6617414b5607b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-12-21 10:42:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-21 12:31:40","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19G7.05c","SPCC18B5.03","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-10-21"},{"uniquename":"PMID:1286615","title":"The Drosophila cdc25 homolog twine is required for meiosis.","citation":"Development 1992 Oct;116(2):405-16","abstract":"We have identified a second cdc25 homolog in Drosophila. In contrast to string (the first homolog identified in Drosophila) this second homolog, twine, does not function in the mitotic cell cycle, but is specialized for meiosis. Expression of twine was observed exclusively in male and female gonads. twine transcripts are present in germ cells during meiosis, and appear only late during gametogenesis, well after the end of the mitotic germ cell divisions. The sterile Drosophila mutant, mat(2)synHB5, which had previously been isolated and mapped to the same genomic region as twine (35F), was found to carry a missense mutation in the twine gene. This missense mutation in twine abolished its ability to complement a mutation in Schizosaccharomyces pombe cdc25. Phenotypic analysis of mat(2)synHB5 mutant flies revealed a complete block of meiosis in males and severe meiotic defects in females.","authors":"Courtot C, Fankhauser C, Simanis V, Lehner CF","authors_abbrev":"Courtot C et al.","pubmed_publication_date":"Oct 1992","pubmed_entrez_date":"1992-10-01","publication_year":"1992","canto_session_key":"9f289c06ca518581","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-03-20 01:16:31","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-03-20 01:16:23","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC24H6.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-03-20"},{"uniquename":"PMID:12449370","title":"Gap repair transformation in fission yeast to exchange plasmid-selectable markers.","citation":"Biotechniques 2002 Nov;33(5):978, 980, 982","abstract":"","authors":"Kelly DA, Hoffman CS","authors_abbrev":"Kelly DA et al.","pubmed_publication_date":"Nov 2002","pubmed_entrez_date":"2002-11-27","publication_year":"2002","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17284461","title":"Biochemical and genetic analysis of RNA cap guanine-N2 methyltransferases from Giardia lamblia and Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2007;35(5):1411-20","abstract":"RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine. Here we performed a mutational analysis of Giardia Tgs2, entailing an alanine scan of 17 residues within the minimal active domain. Alanine substitutions at Phe18, Thr40, Asp76, Asn103 and Asp140 reduced methyltransferase specific activity to <3% of wild-type Tgs2, thereby defining these residues as essential. Alanines at Pro142, Tyr148 and Pro185 reduced activity to 7-12% of wild-type. Structure-activity relationships at Phe18, Thr40, Asp76, Asn103, Asp140 and Tyr148, and at three other essential residues defined previously (Asp68, Glu91 and Trp143) were gleaned by testing the effects of 18 conservative substitutions. Our results engender a provisional map of the Tgs2 active site, which we discuss in light of crystal structures of related methyltransferases. A genetic analysis of S. pombe Tgs1 showed that it is nonessential. An S. pombe tgs1Delta strain grows normally, notwithstanding the absence of 2,2,7-trimethylguanosine caps on its U1, U2, U4 and U5 snRNAs. However, we find that S. pombe requires cap guanine-N7 methylation catalyzed by the enzyme Pcm1. Deletion of the pcm1(+) gene was lethal, as were missense mutations in the Pcm1 active site. Thus, whereas m(7)G caps are essential in both S. pombe and S. cerevisiae, m(2,2,7)G caps are not.","authors":"Hausmann S, Ramirez A, Schneider S, Schwer B, Shuman S","authors_abbrev":"Hausmann S et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-02-08","publication_year":"2007","canto_session_key":"56c05885cd46f22e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-14 11:50:14","canto_approved_date":"2023-11-19 16:14:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-06-20 15:57:21","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.04","SPSNRNA.02","SPSNRNA.01","SPCC330.10","SPAC2G11.15c","SPSNRNA.05"],"gene_count":6,"ltp_gene_count":2,"approved_date":"2015-07-14"},{"uniquename":"PMID:22748672","title":"Polynucleotide kinase/phosphatase, Pnk1, is involved in base excision repair in Schizosaccharomyces pombe.","citation":"DNA Repair (Amst) 2012 Aug 01;11(8):676-83","abstract":"We previously reported that Schizosaccharomyces pombe pnk1 cells are more sensitive than wild-type cells to γ-radiation and camptothecin, indicating that Pnk1 is required for DNA repair. Here, we report that pnk1pku70 and pnk1rhp51 double mutants are more sensitive to γ-radiation than single mutants, from which we infer that Pnk1's primary role is independent of either homologous recombination or non-homologous end joining mechanisms. We also report that pnk1 cells are more sensitive than wild-type cells to oxidizing and alkylating agents, suggesting that Pnk1 is involved in base excision repair. Mutational analysis of Pnk1 revealed that the DNA 3'-phosphatase activity is necessary for repair of DNA damage, whereas the 5'-kinase activity is dispensable. A role for Pnk1 in base excision repair is supported by genetic analyses which revealed that pnk1apn2 is synthetically lethal, suggesting that Pnk1 and Apn2 may function in parallel pathways essential for the repair of endogenous DNA damage. Furthermore, the nth1pnk1apn2 and tdp1pnk1apn2 triple mutants are viable, implying that single-strand breaks with 3'-blocked termini produced by Nth1 and Tdp1 contribute to synthetic lethality. We also examined the sensitivity to methyl methanesulfonate of all single and double mutant combinations of nth1, apn2, tdp1 and pnk1. Together, our results support a model where Tdp1 and Pnk1 act in concert in an Apn2-independent base excision repair pathway to repair 3'-blocked termini produced by Nth1; and they also provide evidence that Pnk1 has additional roles in base excision repair.","doi":"10.1016/j.dnarep.2012.06.001","authors":"Kashkina E, Qi T, Weinfeld M, Young D","authors_abbrev":"Kashkina E et al.","pubmed_publication_date":"01 Aug 2012","pubmed_entrez_date":"2012-07-04","publication_year":"2012","canto_session_key":"6eecc9d84084dc5c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-05-23 16:11:50","canto_approved_date":"2024-03-28 17:36:06","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2013-05-17 10:48:50","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":41,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3D6.10","SPAC23C11.04c","SPAC19G12.15c","SPCC126.02c","SPCP31B10.05","SPAC30D11.07","SPAC644.14c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2013-05-23"},{"uniquename":"PMID:38393482","title":"MAARS Software for Automatic and Quantitative Analysis of Mitotic Progression.","citation":"Methods Mol Biol 2024;2740:275-293","abstract":"In this chapter, we describe a software called MAARS (Mitotic Analysis And Recording System) that enables automatic and quantitative analysis of mitotic progression on an open-source platform. This computer-assisted analysis of cell division allows the unbiased acquisition of multiple parameters such as cell shape or size, metaphase or anaphase delays, as well as various mitotic abnormalities. This chapter describes the power of such an expert system to highlight the complexity of the mechanisms required to prevent mitotic chromosome segregation errors, leading to aneuploidy.","doi":"10.1007/978-1-0716-3557-5_17","authors":"Li T, Gachet Y, Tournier S","authors_abbrev":"Li T et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-02-23","publication_year":"2024","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-02-24 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26858975","title":"Gene expression profiling data of Schizosaccharomyces pombe under nitrosative stress using differential display.","citation":"Data Brief 2016 Mar;6:101-11","abstract":"Excess production of nitric oxide (NO) and reactive nitrogen intermediates (RNIs) causes nitrosative stress on cells. Schizosaccharomyces pombe was used as a model to study nitrosative stress response. In the present data article, we have used differential display to identify the differentially expressed genes in the fission yeast under nitrosative stress conditions. We have used pure NO donor compound detaNONOate at final concentrations of 0.1 mM and 1 mM to treat the cells for 15 min alongside control before studying their gene expression profiles. At both the treated conditions, we identified genes which were commonly repressed while several genes were induced upon both 0.1 mM and 1 mM treatments. The differentially expressed genes were further analyzed in DAVID and categorized into several different pathways.","doi":"10.1016/j.dib.2015.11.047","authors":"Biswas P, Majumdar U, Ghosh S","authors_abbrev":"Biswas P et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2016-02-10","publication_year":"2016","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-11 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27402158","title":"Phospho-site mutants of the RNA Polymerase II C-terminal domain alter subtelomeric gene expression and chromatin modification state in fission yeast.","citation":"Nucleic Acids Res 2016 Nov 02;44(19):9180-9189","abstract":"Eukaryotic gene expression requires that RNA Polymerase II (RNAP II) gain access to DNA in the context of chromatin. The C-terminal domain (CTD) of RNAP II recruits chromatin modifying enzymes to promoters, allowing for transcription initiation or repression. Specific CTD phosphorylation marks facilitate recruitment of chromatin modifiers, transcriptional regulators, and RNA processing factors during the transcription cycle. However, the readable code for recruiting such factors is still not fully defined and how CTD modifications affect related families of genes or regional gene expression is not well understood. Here, we examine the effects of manipulating the Y 1 S 2 P 3 T 4 S 5 P 6 S 7  heptapeptide repeat of the CTD of RNAP II in Schizosaccharomyces pombe by substituting non-phosphorylatable alanines for Ser2 and/or Ser7 and the phosphomimetic glutamic acid for Ser7. Global gene expression analyses were conducted using splicing-sensitive microarrays and validated via RT-qPCR. The CTD mutations did not affect pre-mRNA splicing or snRNA levels. Rather, the data revealed upregulation of subtelomeric genes and alteration of the repressive histone H3 lysine 9 methylation (H3K9me) landscape. The data further indicate that H3K9me and expression status are not fully correlated, suggestive of CTD-dependent subtelomeric repression mechansims that act independently of H3K9me levels.","authors":"Inada M, Nichols RJ, Parsa JY, Homer CM, Benn RA, Hoxie RS, Madhani HD, Shuman S, Schwer B, Pleiss JA","authors_abbrev":"Inada M et al.","pubmed_publication_date":"02 Nov 2016","pubmed_entrez_date":"2016-07-13","publication_year":"2016","canto_session_key":"ee7f5d7f07285799","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-07-14 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18256284","title":"Sister kinetochore recapture in fission yeast occurs by two distinct mechanisms, both requiring Dam1 and Klp2.","citation":"Mol Biol Cell 2008 Apr;19(4):1646-62","abstract":"In eukaryotic cells, proper formation of the spindle is necessary for successful cell division. We have studied chromosome recapture in the fission yeast Schizosaccharomyces pombe. We show by live cell analysis that lost kinetochores interact laterally with intranuclear microtubules (INMs) and that both microtubule depolymerization (end-on pulling) and minus-end-directed movement (microtubule sliding) contribute to chromosome retrieval to the spindle pole body (SPB). We find that the minus-end-directed motor Klp2 colocalizes with the kinetochore during its transport to the SPB and contributes to the effectiveness of retrieval by affecting both end-on pulling and lateral sliding. Furthermore, we provide in vivo evidence that Dam1, a component of the DASH complex, also colocalizes with the kinetochore during its transport and is essential for its retrieval by either of these mechanisms. Finally, we find that the position of the unattached kinetochore correlates with the size and orientation of the INMs, suggesting that chromosome recapture may not be a random process.","authors":"Gachet Y, Reyes C, Courthéoux T, Goldstone S, Gay G, Serrurier C, Tournier S","authors_abbrev":"Gachet Y et al.","pubmed_publication_date":"Apr 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_session_key":"f78a781e3e01fdf4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-11 21:22:44","canto_approved_date":"2020-09-21 11:14:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-06 15:37:52","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC27.02c","SPAC589.08c","SPAC18G6.15","SPAC664.10","SPAC1093.06c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-10-11"},{"uniquename":"PMID:11129054","title":"A novel member of the Swi6p family of fission yeast chromo domain-containing proteins associates with the centromere in vivo and affects chromosome segregation.","citation":"Mol Gen Genet 2000 Nov;264(4):492-505","abstract":"We previously used a genetic approach to identify a new class of Schizosaccharomyces pombe genes (chromosome loss when overexpressed; clo genes) that, when present in elevated dosage, cause the loss of an otherwise stable cen1 linear minichromosome at high rates. Here we report the identities of two clo genes; one encodes histone H3.3 and the other, designated clo2, encodes a novel protein with significant homology to fission yeast Swi6p, human and Drosophila HP1 heterochromatin proteins, and other chromo domain-containing proteins. Members of this group have been shown to localize to heterochromatic DNA, including centromeres, and to play roles in chromatin formation and organization. The S. pombe Clo2 protein localizes to centromere DNA in vivo, and overexpression of clo2 leads to a dramatic increase in the rate of mitotic loss of an artificial chromosome. Clo2p is not essential for mitotic growth, however, even in cells that also lack Swi6p. Thus, fission yeast appears to utilize multiple, functionally redundant, HP1-related proteins for heterochromatin-associated activities at centromeres and perhaps elsewhere in the genome.","authors":"Halverson D, Gutkin G, Clarke L","authors_abbrev":"Halverson D et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-12-29","publication_year":"2000","canto_session_key":"e203075a594c47c9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-07-02 15:02:39","canto_approved_date":"2023-07-02 15:02:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-02 15:02:33","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16C6.10","SPAC644.06c","SPBC1105.11c","SPAC664.01c","SPBC1105.04c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2023-07-02"},{"uniquename":"PMID:15470237","title":"Introns and splicing elements of five diverse fungi.","citation":"Eukaryot Cell 2004 Oct;3(5):1088-100","abstract":"Genomic sequences and expressed sequence tag data for a diverse group of fungi (Saccharomyces cerevisiae, Schizosaccharomyces pombe, Aspergillus nidulans, Neurospora crassa, and Cryptococcus neoformans) provided the opportunity to accurately characterize conserved intronic elements. An examination of large intron data sets revealed that fungal introns in general are short, that 98% or more of them belong to the canonical splice site (ss) class (5'GU...AG3'), and that they have polypyrimidine tracts predominantly in the region between the 5' ss and the branch point. Information content is high in the 5' ss, branch site, and 3' ss regions of the introns but low in the exon regions adjacent to the introns in the fungi examined. The two yeasts have broader intron length ranges and correspondingly higher intron information content than the other fungi. Generally, as intron length increases in the fungi, so does intron information content. Homologs of U2AF spliceosomal proteins were found in all species except for S. cerevisiae, suggesting a nonconventional role for U2AF in the absence of canonical polypyrimidine tracts in the majority of introns. Our observations imply that splicing in fungi may be different from that in vertebrates and may require additional proteins that interact with polypyrimidine tracts upstream of the branch point. Theoretical protein homologs for Nam8p and TIA-1, two proteins that require U-rich regions upstream of the branch point to function, were found. There appear to be sufficient differences between S. cerevisiae and S. pombe introns and the introns of two filamentous members of the Ascomycota and one member of the Basidiomycota to warrant the development of new model organisms for studying the splicing mechanisms of fungi.","authors":"Kupfer DM, Drabenstot SD, Buchanan KL, Lai H, Zhu H, Dyer DW, Roe BA, Murphy JW","authors_abbrev":"Kupfer DM et al.","pubmed_publication_date":"Oct 2004","pubmed_entrez_date":"2004-10-08","publication_year":"2004","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20655879","title":"The MAP kinase Pmk1 and protein kinase A are required for rotenone resistance in the fission yeast, Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2010 Aug 20;399(2):123-8","abstract":"Rotenone is a widely used pesticide that induces Parkinson's disease-like symptoms in rats and death of dopaminergic neurons in culture. Although rotenone is a potent inhibitor of complex I of the mitochondrial electron transport chain, it can induce death of dopaminergic neurons independently of complex I inhibition. Here we describe effects of rotenone in the fission yeast, Schizosaccharomyces pombe, which lacks complex I and carries out rotenone-insensitive cellular respiration. We show that rotenone induces generation of reactive oxygen species (ROS) as well as fragmentation of mitochondrial networks in treated S. pombe cells. While rotenone is only modestly inhibitory to growth of wild type S. pombe cells, it is strongly inhibitory to growth of mutants lacking the ERK-type MAP kinase, Pmk1, or protein kinase A (PKA). In contrast, cells lacking the p38 MAP kinase, Spc1, exhibit modest resistance to rotenone. Consistent with these findings, we provide evidence that Pmk1 and PKA, but not Spc1, are required for clearance of ROS in rotenone treated S. pombe cells. Our results demonstrate the usefulness of S. pombe for elucidating complex I-independent molecular targets of rotenone as well as mechanisms conferring resistance to the toxin.","doi":"10.1016/j.bbrc.2010.07.014","authors":"Wang Y, Gulis G, Buckner S, Johnson PC, Sullivan D, Busenlehner L, Marcus S","authors_abbrev":"Wang Y et al.","pubmed_publication_date":"20 Aug 2010","pubmed_entrez_date":"2010-07-27","publication_year":"2010","canto_session_key":"1fea86053265e7bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-10-22 15:36:59","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-10-22 15:36:52","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10","SPAC24B11.06c","SPBC119.08"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2014-10-22"},{"uniquename":"PMID:16079182","title":"Role of septins and the exocyst complex in the function of hydrolytic enzymes responsible for fission yeast cell separation.","citation":"Mol Biol Cell 2005 Oct;16(10):4867-81","abstract":"Cell separation in Schizosaccharomyces pombe is achieved by the concerted action of the Eng1 endo-beta-1,3-glucanase and the Agn1 endo-alpha-1,3-glucanase, which are transported to the septum and localize to a ringlike structure that surrounds the septum. The requirements for the correct localization of both hydrolases as a ring were analyzed using green fluorescent protein fusion proteins. Targeting to the septum required a functional exocyst, because both proteins failed to localize correctly in sec8-1 or exo70delta mutants, suggesting that Agn1 and Eng1 might be two of the cargo proteins present in the vesicles that accumulate in exocyst mutants. Septins and Mid2 were also required for correct formation of a ring. In their absence, Eng1 and Agn1 were found in a disk-like structure that spanned the septum, rather than in a ring. Even though septin and mid2delta mutants have a cell separation defect, the septum and the distribution of linear beta-1,3-glucans were normal in these cells, suggesting that mislocalization of Eng1 and Agn1 might be the reason underlying the failure to separate efficiently. Thus, one of the functions of the septin ring would be to act as a positional marker for the localization of hydrolytic proteins to the medial region.","authors":"Martín-Cuadrado AB, Morrell JL, Konomi M, An H, Petit C, Osumi M, Balasubramanian M, Gould KL, Del Rey F, de Aldana CR","authors_abbrev":"Martín-Cuadrado AB et al.","pubmed_publication_date":"Oct 2005","pubmed_entrez_date":"2005-08-05","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15964266","title":"Cyclin degradation: don't mes(s) with meiosis.","citation":"Curr Biol 2005 Jun 21;15(12):R461-3","abstract":"Cyclin degradation is required for exit from mitosis and enables a new round of DNA replication in the subsequent S phase. A recent study in fission yeast shows that, during exit from meiosis I, the Mes1 protein partially inhibits cyclin degradation and thereby allows entry into meiosis II without an intervening S phase.","authors":"Peters JM","authors_abbrev":"Peters JM","pubmed_publication_date":"21 Jun 2005","pubmed_entrez_date":"2005-06-21","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9645434","title":"Alteration of the largest subunit of RNA polymerase II and its effect on chromosome stability in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1998 May;258(3):279-87","abstract":"A mutation in the RNA polymerase II largest subunit (RpII LS) that is related to abnormal induction of sister chromatid exchange has previously been described the CHO-K1 cell mutant tsTM4. To elucidate the molecular basis of this effect we introduced the mutation into the homologous site in the Schizosaccharomyces pombe rpbl gene, which encodes RpII LS. Since the tsTM4 mutant exhibited a decrease in the rate of DNA synthesis in cells arrested in S phase at the nonpermissive temperature, we focussed on the study of growth, the cell cycle, and chromosome stability at various temperatures. First, we examined the effects of the mutation on haploid yeast cells. The mutant showed slower growth than the wild type, but cell growth was not arrested at the nonpermissive temperature. When growing cells were shifted to the nonpermissive temperature, an accumulation of cells in G1 and/or G0 was observed. Tetrad analysis suggested that these phenotypes were associated with the mutation. In diploid cells, chromosome instability was detected by loss of intragenic complementation between two alleles of the ade6 gene. An abnormal fraction of cells containing an intermediate DNA content was also observed by FACS analysis. The accumulation of this fraction may reflect the fact that a large number of cells are in S phase or have an abnormal DNA content as a result of chromosome instability. These observations demonstrate that the S. pombe rpb1 mutant exhibits a phenotype very similar to that of the CHO-K1 cell mutant tsTM4.","authors":"Sugaya K, Ajimura M, Tsuji H, Morimyo M, Mita K","authors_abbrev":"Sugaya K et al.","pubmed_publication_date":"May 1998","pubmed_entrez_date":"1998-06-30","publication_year":"1998","canto_session_key":"fc98ac3577f19f5d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-12 14:59:14","canto_approved_date":"2018-06-12 14:59:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-12 14:58:17","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28F2.12"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-12"},{"uniquename":"EMBL:X54301","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37207657","title":"The molecular basis of heterochromatin assembly and epigenetic inheritance.","citation":"Mol Cell 2023 Jun 01;83(11):1767-1785","abstract":"Heterochromatin plays a fundamental role in gene regulation, genome integrity, and silencing of repetitive DNA elements. Histone modifications are essential for the establishment of heterochromatin domains, which is initiated by the recruitment of histone-modifying enzymes to nucleation sites. This leads to the deposition of histone H3 lysine-9 methylation (H3K9me), which provides the foundation for building high-concentration territories of heterochromatin proteins and the spread of heterochromatin across extended domains. Moreover, heterochromatin can be epigenetically inherited during cell division in a self-templating manner. This involves a \"read-write\" mechanism where pre-existing modified histones, such as tri-methylated H3K9 (H3K9me3), support chromatin association of the histone methyltransferase to promote further deposition of H3K9me. Recent studies suggest that a critical density of H3K9me3 and its associated factors is necessary for the propagation of heterochromatin domains across multiple generations. In this review, I discuss the key experiments that have highlighted the importance of modified histones for epigenetic inheritance.","doi":"10.1016/j.molcel.2023.04.020","authors":"Grewal SIS","authors_abbrev":"Grewal SIS","pubmed_publication_date":"01 Jun 2023","pubmed_entrez_date":"2023-05-19","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-06-06 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21856157","title":"mmb1p binds mitochondria to dynamic microtubules.","citation":"Curr Biol 2011 Sep 13;21(17):1431-9","abstract":"Mitochondria form a dynamic tubular network within the cell. Proper mitochondria movement and distribution are critical for their localized function in cell metabolism, growth, and survival. In mammalian cells, mechanisms of mitochondria positioning appear dependent on the microtubule cytoskeleton, with kinesin or dynein motors carrying mitochondria as cargos and distributing them throughout the microtubule network. Interestingly, the timescale of microtubule dynamics occurs in seconds, and the timescale of mitochondria distribution occurs in minutes. How does the cell couple these two time constants?\nFission yeast also relies on microtubules for mitochondria distribution. We report here a new microtubule-dependent but motor-independent mechanism for proper mitochondria positioning in fission yeast. We identify the protein mmb1p, which binds to mitochondria and microtubules. mmb1p attaches the tubular mitochondria to the microtubule lattice at multiple discrete interaction sites. mmb1 deletion causes mitochondria to aggregate, with the long-term consequence of defective mitochondria distribution and cell death. mmb1p decreases microtubule dynamicity.\nmmb1p is a new microtubule-mitochondria binding protein. We propose that mmb1p acts to couple long-term mitochondria distribution to short-term microtubule dynamics by attenuating microtubule dynamics, thus enhancing the mitochondria-microtubule interaction time.","doi":"10.1016/j.cub.2011.07.013","authors":"Fu C, Jain D, Costa J, Velve-Casquillas G, Tran PT","authors_abbrev":"Fu C et al.","pubmed_publication_date":"13 Sep 2011","pubmed_entrez_date":"2011-08-23","publication_year":"2011","canto_session_key":"425f7241a2674896","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-12-19 21:52:12","canto_approved_date":"2022-07-23 08:38:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-11-22 08:18:19","canto_added_date":"2012-02-17 19:06:06","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPBC25B2.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-12-19"},{"uniquename":"PMID:37477900","title":"ER-localized Shr3 is a selective co-translational folding chaperone necessary for amino acid permease biogenesis.","citation":"J Cell Biol 2023 Sep 04;222(9)","abstract":"Proteins with multiple membrane-spanning segments (MS) co-translationally insert into the endoplasmic reticulum (ER) membrane of eukaryotic cells. Shr3, an ER membrane-localized chaperone in Saccharomyces cerevisiae, is required for the functional expression of a family of 18 amino acid permeases (AAP) comprised of 12 MS. We have used comprehensive scanning mutagenesis and deletion analysis of Shr3 combined with a modified split-ubiquitin approach to probe chaperone-substrate interactions in vivo. Shr3 selectively interacts with nested C-terminal AAP truncations in marked contrast to similar truncations of non-Shr3 substrate sugar transporters. Shr3-AAP interactions initiate with the first four MS of AAP and successively strengthen but weaken abruptly when all 12 MS are present. Shr3-AAP interactions are based on structural rather than sequence-specific interactions involving membrane and luminal domains of Shr3. The data align with Shr3 engaging nascent N-terminal chains of AAP, functioning as a scaffold to facilitate folding as translation completes.","doi":"10.1083/jcb.202208060","authors":"Myronidi I, Ring A, Wu F, Ljungdahl PO","authors_abbrev":"Myronidi I et al.","pubmed_publication_date":"04 Sep 2023","pubmed_entrez_date":"2023-07-21","publication_year":"2023","canto_session_key":"cd1281e3fd065290","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-01-04 11:24:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC409.20c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15504913","title":"UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II.","citation":"J Cell Biol 2004 Oct 25;167(2):315-25","abstract":"We purified native Myo2p/Cdc4p/Rlc1p (Myo2), the myosin-II motor required for cytokinesis by Schizosaccharomyces pombe. The Myo2p heavy chain associates with two light chains, Cdc4p and Rlc1p. Although crude Myo2 supported gliding motility of actin filaments in vitro, purified Myo2 lacked this activity in spite of retaining full Ca-ATPase activity and partial actin-activated Mg-ATPase activity. Unc45-/Cro1p-/She4p-related (UCS) protein Rng3p restored the full motility and actin-activated Mg-ATPase activity of purified Myo2. The COOH-terminal UCS domain of Rng3p alone restored motility to pure Myo2. Thus, Rng3p contributes directly to the motility activity of native Myo2. Consistent with a role in Myo2 activation, Rng3p colocalizes with Myo2p in the cytokinetic contractile ring. The absence of Rlc1p or mutations in the Myo2p head or Rng3p compromise the in vitro motility of Myo2 and explain the defects in cytokinesis associated with some of these mutations. In contrast, Myo2 with certain temperature-sensitive forms of Cdc4p has normal motility, so these mutations compromise other functions of Cdc4p required for cytokinesis.","authors":"Lord M, Pollard TD","authors_abbrev":"Lord M et al.","pubmed_publication_date":"25 Oct 2004","pubmed_entrez_date":"2004-10-27","publication_year":"2004","canto_session_key":"fe0f450d0b971f5a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-07 16:19:50","canto_approved_date":"2025-03-03 21:10:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-02 08:59:04","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":44,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.13c","SPAC29A4.05","SPAC3A12.14","SPCC645.05c","SPAP8A3.08","SPCC613.04c","SPAC926.03"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2024-05-07"},{"uniquename":"PMID:8127718","title":"Inhibition of protein synthesis by an efficiently expressed mutation in the yeast 5.8S ribosomal RNA.","citation":"Nucleic Acids Res 1994 Feb 25;22(4):686-93","abstract":"Recent studies on the inhibition of protein synthesis by specific anti 5.8S rRNA oligonucleotides strongly suggested that this RNA plays an important role in eukaryotic ribosome function. To evaluate this possibility further, a ribosomal DNA transcription unit from Schizosaccharomyces pombe was cloned into yeast shuttle vectors with copy numbers ranging from 2 to approximately 90 per cell; to allow direct detection of expressed RNA and to disrupt the function of the 5.8S rRNA molecule, a five base insertion was made in a universally conserved GAAC sequence. The altered mobility of the mutant RNA was readily detected by gel electrophoresis and analyses indicated that mutant RNA transcription reflected the ratio of plasmid to endogenous rDNA. The highest copy number plasmid resulted in about 40-50% mutant RNA. This mutant RNA was readily integrated into the ribosome structure resulting in an in vivo ribosome population which was also about 40-50% mutant; the rates of growth and protein synthesis were equally reduced by approximately 40%. A comparable level of inhibition in protein synthesis was demonstrated in vitro and polyribosomal profiles revealed a consistent increase in size. Subsequent RNA analyses indicated a normal distribution of mutant RNA in both monoribosomes and polyribosomes, but elevated tRNA levels in mutant polyribosomes. Additional mutations in alternate GAAC sequences revealed similar but cumulative effects on both protein synthesis and polyribosome profiles. Taken together, these results suggest little or no effect on initiation but provide in vivo evidence of a functional role for the 5.8S rRNA in protein elongation.","authors":"Abou Elela S, Good L, Melekhovets YF, Nazar RN","authors_abbrev":"Abou Elela S et al.","pubmed_publication_date":"25 Feb 1994","pubmed_entrez_date":"1994-02-25","publication_year":"1994","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27797084","title":"A Protocol for Measuring Mitotic Chromosome Condensation Quantitatively in Fission Yeast Cells.","citation":"Methods Mol Biol 2017;1515:245-255","abstract":"Even though the formation of compact cylindrical chromosomes early during mitosis or meiosis is a prerequisite for the successful segregation of eukaryotic genomes, little is known about the molecular basis of this chromosome condensation process. Here, we describe in detail the protocol for a quantitative chromosome condensation assay in fission yeast cells, which is based on precise time-resolved measurements of the distances between two fluorescently labeled positions on the same chromosome. In combination with an automated computational analysis pipeline, this assay enables the study of various candidate proteins for their roles in regulating genome topology during cell divisions.","authors":"Schiklenk C, Petrova B, Haering CH","authors_abbrev":"Schiklenk C et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2016-11-01","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-02 01:15:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8973306","title":"Cloning and characterization of hsc1+, a heat shock cognate gene of the fission yeast Schizosaccharomyces pombe.","citation":"Gene 1996 Nov 28;181(1-2):45-9","abstract":"A heat shock cognate gene from the fission yeast Schizosaccharomyces pombe (Sp), designated hsc1+, was cloned. The putative translation product of hsc1+ contains 613 aa, with an estimated molecular mass of 67,205 Da, and is more similar to the Saccharomyces cerevisiae (Sc) heat shock cognate protein SSB1 (69% identity) than the Sp heat-inducible ssp1+ gene product (41% identity). The hsc1+ mRNA was abundant during steady-state growth at 23 degrees C and decreased upon heat shock. Immunoblot analysis showed that the hsc1 protein is also abundant and constitutively expressed, however, we could not observe significant change in the protein level upon heat shock. DNA blot analyses indicated that hsc1+ is localized in Sp chromosome II, and suggested that the Sp genome contains a relatively smaller number of HSP70 genes compared with the Sc genome.","authors":"Oishi K, Sugiura R, Shuntoh H, Kuno T","authors_abbrev":"Oishi K et al.","pubmed_publication_date":"28 Nov 1996","pubmed_entrez_date":"1996-11-28","publication_year":"1996","canto_session_key":"e2682fdbd9836e34","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-10-29 11:14:24","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-29 11:14:14","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1709.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-10-29"},{"uniquename":"PMID:8421694","title":"Genome mapping by nonrandom anchoring: a discrete theoretical analysis.","citation":"Proc Natl Acad Sci U S A 1993 Jan 15;90(2):600-4","abstract":"As part of our effort to construct a physical map of the genome of the fission yeast Schizosaccharomyces pombe, we have made theoretical predictions for the progress expected, as measured by the expected length fraction of island coverage and by the expected properties of the anchored islands such as the number and the size of islands. Our experimental strategy is to construct a random clone library and screen the library for clones having unique sequence at both ends. This scheme is essentially the same as the clone-limited double sequence-tagged-site selection scheme which was used in a computer simulation by Palazzolo et al. [Palazzolo, M. J., Sawyer, S. A., Martin, C. H., Smoller, D. A. & Hartl, D. L. (1991) Proc. Natl. Acad. Sci. USA 88, 8034-8038]. Both simulation and ongoing experiments in our laboratory have shown that the nonrandom anchoring method is far superior to random anchoring. In this paper, we propose a theoretical model to explain the simulated data and the experimental data.","authors":"Zhang MQ, Marr TG","authors_abbrev":"Zhang MQ et al.","pubmed_publication_date":"15 Jan 1993","pubmed_entrez_date":"1993-01-15","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24728197","title":"The basic leucine zipper domain transcription factor Atf1 directly controls Cdc13 expression and regulates mitotic entry independently of Wee1 and Cdc25 in Schizosaccharomyces pombe.","citation":"Eukaryot Cell 2014 Jun;13(6):813-21","abstract":"Progression into mitosis is a major point of regulation in the Schizosaccharomyces pombe cell cycle, and its proper control is essential for maintenance of genomic stability. Investigation of the G(2)/M progression event in S. pombe has revealed the existence of a complex regulatory process that is responsible for making the decision to enter mitosis. Newer aspects of this regulation are still being revealed. In this paper, we report the discovery of a novel mode of regulation of G(2)/M progression in S. pombe. We show that the mitogen-activated protein kinase (MAPK)-regulated transcription factor Atf1 is a regulator of Cdc13 (mitotic cyclin) transcription and is therefore a prominent player in the regulation of mitosis in S. pombe. We have used genetic approaches to study the effect of overexpression or deletion of Atf1 on the cell length and G(2)/M progression of S. pombe cells. Our results clearly show that Atf1 overexpression accelerates mitosis, leading to an accumulation of cells with shorter lengths. The previously known major regulators of entry into mitosis are the Cdc25 phosphatase and the Wee1 kinase, which modulate cyclin-dependent kinase (CDK) activity. The significantly striking aspect of our discovery is that Atf1-mediated G(2)/M progression is independent of both Cdc25 and Wee1. We have shown that Atf1 binds to the Cdc13 promoter, leading to activation of Cdc13 expression. This leads to enhanced nuclear localization of CDK Cdc2, thereby promoting the G(2)/M transition.","doi":"10.1128/EC.00059-14","authors":"Bandyopadhyay S, Dey I, Suresh M, Sundaram G","authors_abbrev":"Bandyopadhyay S et al.","pubmed_publication_date":"Jun 2014","pubmed_entrez_date":"2014-04-15","publication_year":"2014","canto_session_key":"7b0762e353cab896","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Geetanjali Sundaram","canto_first_approved_date":"2018-04-11 16:45:11","canto_approved_date":"2019-06-14 12:54:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-02-29 10:11:30","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Geetanjali Sundaram","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC24H6.05","SPBC11B10.09","SPBC29B5.01","SPBC582.03"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-04-11"},{"uniquename":"PMID:26812546","title":"Mutation in ATG5 reduces autophagy and leads to ataxia with developmental delay.","citation":"Elife 2016 Jan 26;5","abstract":"Autophagy is required for the homeostasis of cellular material and is proposed to be involved in many aspects of health. Defects in the autophagy pathway have been observed in neurodegenerative disorders; however, no genetically-inherited pathogenic mutations in any of the core autophagy-related (ATG) genes have been reported in human patients to date. We identified a homozygous missense mutation, changing a conserved amino acid, in ATG5 in two siblings with congenital ataxia, mental retardation, and developmental delay. The subjects' cells display a decrease in autophagy flux and defects in conjugation of ATG12 to ATG5. The homologous mutation in yeast demonstrates a 30-50% reduction of induced autophagy. Flies in which Atg5 is substituted with the mutant human ATG5 exhibit severe movement disorder, in contrast to flies expressing the wild-type human protein. Our results demonstrate the critical role of autophagy in preventing neurological diseases and maintaining neuronal health.","doi":"10.7554/eLife.12245","authors":"Kim M, Sandford E, Gatica D, Qiu Y, Liu X, Zheng Y, Schulman BA, Xu J, Semple I, Ro SH, Kim B, Mavioglu RN, Tolun A, Jipa A, Takats S, Karpati M, Li JZ, Yapici Z, Juhasz G, Lee JH, Klionsky DJ, Burmeister M","authors_abbrev":"Kim M et al.","pubmed_publication_date":"26 Jan 2016","pubmed_entrez_date":"2016-01-27","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4B4.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15452279","title":"A general role of the DNA glycosylase Nth1 in the abasic sites cleavage step of base excision repair in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 2004;32(17):5119-25","abstract":"One of the most frequent lesions formed in cellular DNA are abasic (apurinic/apyrimidinic, AP) sites that are both cytotoxic and mutagenic, and must be removed efficiently to maintain genetic stability. It is generally believed that the repair of AP sites is initiated by the AP endonucleases; however, an alternative pathway seems to prevail in Schizosaccharomyces pombe. A mutant lacking the DNA glycosylase/AP lyase Nth1 is very sensitive to the alkylating agent methyl methanesulfonate (MMS), suggesting a role for Nth1 in base excision repair (BER) of alkylation damage. Here, we have further evaluated the role of Nth1 and the second putative S.pombe AP endonuclease Apn2, in abasic site repair. The deletion of the apn2 open reading frame dramatically increased the sensitivity of the yeast cells to MMS, also demonstrating that the Apn2 has an important function in the BER pathway. The deletion of nth1 in the apn2 mutant strain partially relieves the MMS sensitivity of the apn2 single mutant, indicating that the Apn2 and Nth1 act in the same pathway for the repair of abasic sites. Analysis of the AP site cleavage in whole cell extracts of wild-type and mutant strains showed that the AP lyase activity of Nth1 represents the major AP site incision activity in vitro. Assays with DNA substrates containing base lesions removed by monofunctional DNA glycosylases Udg and MutY showed that Nth1 will also cleave the abasic sites formed by these enzymes and thus act downstream of these enzymes in the BER pathway. We suggest that the main function of Apn2 in BER is to remove the resulting 3'-blocking termini following AP lyase cleavage by Nth1.","authors":"Alseth I, Korvald H, Osman F, Seeberg E, Bjørås M","authors_abbrev":"Alseth I et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-09-29","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8396547","title":"Sequence analysis of closely related retrotransposon families from fission yeast.","citation":"Gene 1993 Sep 06;131(1):135-9","abstract":"Two families of retrotransposons, Tf1 and Tf2, have been isolated from the fission yeast, Schizosaccharomyces pombe. We report here the nucleotide (nt) sequence of a Tf2 element, the only retrotransposon family known from the commonly used laboratory strains, 972 and 975, and their derivatives. The total nt sequence of Tf2 was derived from the complete sequence of the coding region and 3' long terminal repeat (LTR) of randomly cloned element Tf2-1, and from a full 5' LTR and approximately one-third of the open reading frame (ORF) of Tf2-43, a Tf2 element found in the head-to-head orientation adjacent to the Sz. pombe rpb6 gene. The two Tf2 sequences are nearly identical and both of them contain a single ORF encoding a protein with regions of sequence similar to protease, reverse transcriptase, RNase H (RH) and integrase from other retrotransposons and retroviruses. Sequence comparisons between Tf1 and Tf2 indicate an extreme divergence of the putative capsid protein-encoding regions of these two elements, as well as divergence of a segment of the LTR, but otherwise virtually identical sequence.","authors":"Weaver DC, Shpakovski GV, Caputo E, Levin HL, Boeke JD","authors_abbrev":"Weaver DC et al.","pubmed_publication_date":"06 Sep 1993","pubmed_entrez_date":"1993-09-06","publication_year":"1993","canto_triage_status":"Transposon related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21870281","title":"Studying S-phase DNA damage checkpoints using the fission yeast Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2011;782:13-21","abstract":"Slowing of replication in response to DNA damage is a universal response to DNA damage during S-phase. Originally discovered to be defective in checkpoint mutant cells in metazoans, this S-phase DNA damage checkpoint response has been extensively studied in yeast. Unlike other checkpoints that completely arrest cell cycle, the S-phase DNA damage checkpoint slows but does not completely halt replication in response to DNA damage. An analysis of mutants defective in the slowing response requires a sensitive assay to measure this quantitative effect. The use of centrifugal elutriation to synchronize cells and improved techniques in preparing cells for flow cytometry allow for more sensitive and accurate measurement of cells' ability to slow replication in the presence of DNA damage. This chapter describes the use of transient cdc10-M17 temperature sensitive allele arrest and release combined with centrifugal elutriation to synchronize cells in G1. The S-phase progression of these cells is then assayed by flow cytometry of isolated nuclei, which allows sensitive determination of replication kinetics.","doi":"10.1007/978-1-61779-273-1_2","authors":"Willis N, Rhind N","authors_abbrev":"Willis N et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-08-27","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36626373","title":"Using canavanine resistance to measure mutation rates in Schizosaccharomyces pombe.","citation":"PLoS One 2023;18(1):e0271016","abstract":"We constructed a panel of S. pombe strains expressing DNA polymerase ε variants associated with cancer, specifically POLES297F, POLEV411L, POLEL424V, POLES459F, and used these to compare mutation rates determined by canavanine resistance with other selective methods. Canavanine-resistance mutation rates are broadly similar to those seen with reversion of the ade-485 mutation to adenine prototrophy, but lower than 5-fluoroorotic acid (FOA)-resistance rates (inactivation of ura4+ or ura5+ genes). Inactivation of several genes has been associated with canavanine resistance in S. pombe but surprisingly whole genome sequencing showed that 8/8 spontaneous canavanine-resistant mutants have an R175C mutation in the any1/arn1 gene. This gene encodes an α-arrestin-like protein involved in mediating Pub1 ubiquitylation of target proteins, and the phenotypic resistance to canavanine by this single mutation is similar to that shown by the original \"can1-1\" strain, which also has the any1R175C mutation. Some of the spontaneous mutants have additional mutations in arginine transporters, suggesting that this may marginally increase resistance to canavanine. The any1R175C strain showed internalisation of the Cat1 arginine transporter as previously reported, explaining the canavanine-resistance phenotype.","doi":"10.1371/journal.pone.0271016","authors":"Pai CC, Heitzer E, Bertrand S, Toumazou S, Humphrey TC, Kearsey SE","authors_abbrev":"Pai CC et al.","pubmed_publication_date":"2023","pubmed_entrez_date":"2023-01-10","publication_year":"2023","canto_session_key":"83887018316db0aa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Stephen Kearsey","canto_first_approved_date":"2023-02-26 10:05:27","canto_approved_date":"2023-03-03 14:03:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-22 15:11:02","canto_added_date":"2023-01-11 01:15:06","annotation_curators":[{"name":"Stephen Kearsey","community_curator":true,"annotation_count":1,"orcid":"0000-0002-3339-2667","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25H2.13c","SPBC18H10.20c","SPAC869.11","SPBC18H10.16","SPBC359.03c","SPAC19E9.03","SPBPB2B2.01"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2023-02-26"},{"uniquename":"PMID:19856119","title":"Spatial regulation and organization of DNA replication within the nucleus.","citation":"Chromosome Res 2010 Jan;18(1):7-17","abstract":"Duplication of chromosomal DNA is a temporally and spatially regulated process. The timing of DNA replication initiation at various origins is highly coordinated; some origins fire early and others late during S phase. Moreover, inside the nuclei, the bulk of DNA replication is physically organized in replication factories, consisting of DNA polymerases and other replication proteins. In this review article, we discuss how DNA replication is organized and regulated spatially within the nucleus and how this spatial organization is linked to temporal regulation. We focus on DNA replication in budding yeast and fission yeast and, where applicable, compare yeast DNA replication with that in bacteria and metazoans.","doi":"10.1007/s10577-009-9088-0","authors":"Natsume T, Tanaka TU","authors_abbrev":"Natsume T et al.","pubmed_publication_date":"Jan 2010","pubmed_entrez_date":"2009-10-27","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22840777","title":"Analyzing fission yeast multidrug resistance mechanisms to develop a genetically tractable model system for chemical biology.","citation":"Chem Biol 2012 Jul 27;19(7):893-901","abstract":"Chemical inhibitors can help analyze dynamic cellular processes, particularly when probes are active in genetically tractable model systems. Although fission yeast has served as an important model system, which shares more cellular processes (e.g., RNAi) with humans than budding yeast, its use for chemical biology has been limited by its multidrug resistance (MDR) response. Using genomics and genetics approaches, we identified the key transcription factors and drug-efflux transporters responsible for fission yeast MDR and designed strains sensitive to a wide-range of chemical inhibitors, including commonly used probes. We used this strain, along with acute chemical inhibition and high-resolution imaging, to examine metaphase spindle organization in a \"closed\" mitosis. Together, our findings suggest that our fission yeast strains will allow the use of several inhibitors as probes, discovery of new inhibitors, and analysis of drug action.","doi":"10.1016/j.chembiol.2012.06.008","authors":"Kawashima SA, Takemoto A, Nurse P, Kapoor TM","authors_abbrev":"Kawashima SA et al.","pubmed_publication_date":"27 Jul 2012","pubmed_entrez_date":"2012-07-31","publication_year":"2012","canto_session_key":"f94801dfb551d839","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-04-16 09:35:20","canto_approved_date":"2022-06-01 15:21:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-11-26 10:37:17","canto_added_date":"2012-08-14 08:00:41","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":59,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC4B3.06c","SPAC19A8.05c","SPAC30.04c","SPAC23G3.03","SPAPB1A10.08","SPAC23H3.15c","SPAC26H5.08c","SPCC737.04","SPBC530.05","SPBPB21E7.04c","SPAC630.05","SPAC1002.16c","SPAC15A10.01","SPBC1683.07","SPCC330.03c","SPBC3H7.13","SPCC576.17c","SPCC70.08c","SPCPB1C11.02","SPCC737.09c","SPBC9B6.09c","SPAC23C11.06c","SPBC359.05","SPBC16G5.16","SPAC9E9.12c","SPAC25B8.09","SPBPB2B2.12c","SPAPB24D3.09c","SPBC887.15c","SPAC1002.17c","SPBC1271.08c","SPBC2G2.01c","SPBC1773.16c","SPAC1687.07","SPAPB2B4.04c","SPAC2F3.05c","SPBC365.12c","SPBC25B2.08","SPBC1773.12","SPBC1198.14c","SPBC530.08","SPAC23H4.01c","SPAC869.02c","SPACUNK4.17","SPAC17C9.16c","SPAC1783.07c","SPAC144.10c","SPAC212.02","SPCC18B5.01c","SPAC16A10.01","SPAC688.04c","SPAPB24D3.01","SPAC3H8.02","SPAC19E9.03","SPBC1683.09c","SPBC36B7.02","SPBC26H8.11c","SPCC584.16c","SPBC1271.03c","SPBPB2B2.18","SPBC1198.01","SPAC630.04c","SPAC1039.08","SPBC119.05c","SPCC663.03","SPAC824.02","SPBC19C7.04c","SPBC1105.14","SPAC20G4.03c","SPAC186.03","SPBP35G2.13c","SPCC191.01","SPAC17G6.02c","SPBC12C2.09c","SPAC8C9.16c","SPBC3H7.05c","SPBC56F2.06","SPBPB21E7.07","SPCC338.18","SPAC13C5.05c","SPBP4G3.03","SPAC3F10.11c","SPCC417.05c","SPAC19G12.09","SPAC1952.04c","SPAC2F3.08","SPBC15C4.06c","SPCC736.13","SPCC1020.10","SPAC3A11.10c","SPAC977.09c","SPAC637.03","SPCC1020.05","SPBC1271.07c","SPBPB2B2.01","SPBC25B2.02c","SPAPB24D3.07c","SPAC823.03","SPBC660.05","SPBC660.06","SPBC119.03","SPAC27D7.09c","SPAC2E1P3.01","SPBC609.04","SPBC16E9.16c","SPBC36.03c","SPAC11E3.14","SPAC15A10.10","SPAC18B11.03c","SPAC27D7.11c","SPACUNK12.02c","SPBC725.03","SPAC24B11.12c","SPAC513.07","SPAC4G8.13c","SPBC29B5.02c"],"gene_count":116,"ltp_gene_count":12,"approved_date":"2013-04-16"},{"uniquename":"PMID:18794373","title":"Mechanistic insights into replication termination as revealed by investigations of the Reb1-Ter3 complex of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 2008 Nov;28(22):6844-57","abstract":"Relatively little is known about the interaction of eukaryotic replication terminator proteins with the cognate termini and the replication termination mechanism. Here, we report a biochemical analysis of the interaction of the Reb1 terminator protein of Schizosaccharomyces pombe, which binds to the Ter3 site present in the nontranscribed spacers of ribosomal DNA, located in chromosome III. We show that Reb1 is a dimeric protein and that the N-terminal dimerization domain of the protein is dispensable for replication termination. Unlike its mammalian counterpart Ttf1, Reb1 did not need an accessory protein to bind to Ter3. The two myb/SANT domains and an adjacent, N-terminal 154-amino-acid-long segment (called the myb-associated domain) were both necessary and sufficient for optimal DNA binding in vitro and fork arrest in vivo. The protein and its binding site Ter3 were unable to arrest forks initiated in vivo from ars of Saccharomyces cerevisiae in the cell milieu of the latter despite the facts that the protein retained the proper affinity of binding, was located in vivo at the Ter site, and apparently was not displaced by the \"sweepase\" Rrm3. These observations suggest that replication fork arrest is not an intrinsic property of the Reb1-Ter3 complex.","doi":"10.1128/MCB.01235-08","authors":"Biswas S, Bastia D","authors_abbrev":"Biswas S et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-09-17","publication_year":"2008","canto_session_key":"324cb9a522d25d63","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-12-18 11:19:07","canto_approved_date":"2026-02-16 16:41:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-18 11:14:47","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-12-18"},{"uniquename":"EMBL:SPAJ2494","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9191270","title":"Identification of a putative G protein-coupled receptor kinase in Schizosaccharomyces pombe.","citation":"Biochem Soc Trans 1997 May;25(2):226S","abstract":"","authors":"Watson P, Davey J","authors_abbrev":"Watson P et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"b9471202da214e59","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:48:24","canto_session_submitted_date":"2012-02-27 11:09:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:33406066","title":"Cell cycle-dependent and independent mating blocks ensure fungal zygote survival and ploidy maintenance.","citation":"PLoS Biol 2021 Jan;19(1):e3001067","abstract":"To ensure genome stability, sexually reproducing organisms require that mating brings together exactly 2 haploid gametes and that meiosis occurs only in diploid zygotes. In the fission yeast Schizosaccharomyces pombe, fertilization triggers the Mei3-Pat1-Mei2 signaling cascade, which represses subsequent mating and initiates meiosis. Here, we establish a degron system to specifically degrade proteins postfusion and demonstrate that mating blocks not only safeguard zygote ploidy but also prevent lysis caused by aberrant fusion attempts. Using long-term imaging and flow-cytometry approaches, we identify previously unrecognized and independent roles for Mei3 and Mei2 in zygotes. We show that Mei3 promotes premeiotic S-phase independently of Mei2 and that cell cycle progression is both necessary and sufficient to reduce zygotic mating behaviors. Mei2 not only imposes the meiotic program and promotes the meiotic cycle, but also blocks mating behaviors independently of Mei3 and cell cycle progression. Thus, we find that fungi preserve zygote ploidy and survival by at least 2 mechanisms where the zygotic fate imposed by Mei2 and the cell cycle reentry triggered by Mei3 synergize to prevent zygotic mating.","doi":"10.1371/journal.pbio.3001067","authors":"Vještica A, Bérard M, Liu G, Merlini L, Nkosi PJ, Martin SG","authors_abbrev":"Vještica A et al.","pubmed_publication_date":"Jan 2021","pubmed_entrez_date":"2021-01-06","publication_year":"2021","canto_session_key":"e4dec70d9b01ce1f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-01-08 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22786806","title":"Polar opposites: Fine-tuning cytokinesis through SIN asymmetry.","citation":"Cytoskeleton (Hoboken) 2012 Oct;69(10):686-99","abstract":"Mitotic exit and cell division must be spatially and temporally integrated to facilitate equal division of genetic material between daughter cells. In the fission yeast, Schizosaccharomyces pombe, a spindle pole body (SPB) localized signaling cascade termed the septation initiation network (SIN) couples mitotic exit with cytokinesis. The SIN is controlled at many levels to ensure that cytokinesis is executed once per cell cycle and only after cells segregate their DNA. An interesting facet of the SIN is that its activity is asymmetric on the two SPBs during anaphase; however, how and why the SIN is asymmetric has remained elusive. Many key factors controlling SIN asymmetry have now been identified, shedding light on the significance of SIN asymmetry in regulating cytokinesis. In this review, we highlight recent advances in our understanding of SIN regulation, with an emphasis on how SIN asymmetry is achieved and how this aspect of SIN regulation fine-tunes cytokinesis.","doi":"10.1002/cm.21044","authors":"Johnson AE, McCollum D, Gould KL","authors_abbrev":"Johnson AE et al.","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-07-13","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:X78871","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27886462","title":"Loss of ppr3, ppr4, ppr6, or ppr10 perturbs iron homeostasis and leads to apoptotic cell death in Schizosaccharomyces pombe.","citation":"FEBS J 2017 Jan;284(2):324-337","abstract":"Pentatricopeptide repeat (PPR) proteins characterized by tandem arrays of a degenerate 35-amino-acid repeat belong to a large family of RNA-binding proteins that are involved in post-transcriptional control of organelle gene expression. PPR proteins are ubiquitous in eukaryotes, and particularly prevalent in higher plants. Schizosaccharomyces pombe has 10 PPR proteins. Among them, ppr3, ppr4, ppr6, and ppr10 participate in mitochondrial post-transcriptional processes and are required for mitochondrial electron transport chain (ETC) function. In the present work, we showed that deletion of ppr3, ppr4, ppr6, or ppr10 led to apoptotic cell death, as revealed by DAPI and Annexin V-FITC staining. These mutants also exhibited elevated levels of reactive oxygen species (ROS). RNA sequencing (RNA-seq) and quantitative RT-PCR analyses revealed that deletion of ppr10 affected critical biological processes. In particular, a core set of genes involved in iron uptake and/or iron homeostasis was elevated in the Δppr10 mutant, suggesting an elevated level of intracellular iron in the mutant. Consistent with this notion, Δppr3, Δppr4, Δppr6, and Δppr10 mutants exhibited increased sensitivity to iron. Furthermore, the iron chelator, bathophenanthroline disulfonic acid, but not the calcium chelator EGTA, nearly restored the viabilities of Δppr3, Δppr4, Δppr6, and Δppr10 mutants, and reduced ROS levels in the mutants. These results show for the first time that deletion of a ppr gene leads to perturbation of iron homeostasis. Our results also suggest that disrupted iron homeostasis in Δppr3, Δppr4, Δppr6, and Δppr10 mutants may lead to an increase in the level of ROS and induction of apoptotic cell death in S. pombe.\nThe RNA-seq data have been deposited in the National Center for Biotechnology Information (NCBI) BioProject database (accession number SRP091623) and Gene Expression Omnibus (GEO) database (accession number GSE90144).","doi":"10.1111/febs.13978","authors":"Su Y, Yang Y, Huang Y","authors_abbrev":"Su Y et al.","pubmed_publication_date":"Jan 2017","pubmed_entrez_date":"2016-11-26","publication_year":"2017","canto_session_key":"934af5b83ca408f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2017-04-19 08:16:55","canto_approved_date":"2021-06-11 15:25:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-12-01 12:05:27","canto_added_date":"2016-11-27 01:15:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"val","community_curator":false,"annotation_count":63,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1683.09c","SPBC19G7.07c","SPAC1F7.07c","SPBC1604.02c","SPAC8C9.06c","SPBC29A3.18","SPBC4F6.09","SPBC660.07","SPBC16H5.06","SPBC16C6.08c","SPCC737.02c","SPAC1F8.03c","SPAC1F7.08","SPCC1739.09c","SPAPB15E9.01c","SPAC977.07c","SPACUNK4.16c","SPAPB24D3.10c","SPCC11E10.04","SPAC186.01","SPBC18H10.11c","SPCC1020.03","SPAC328.03","SPBC1289.06c","SPBP4H10.08","SPBC1683.10c","SPCC338.10c","SPCC1742.01","SPBC359.04c","SPAC1F8.06","SPAC23G3.03","SPAC1B2.04","SPBC106.19","SPBC947.04","SPAC1093.01","SPAC869.07c","SPAC1F8.02c","SPBC16A3.03c","SPBC947.05c"],"gene_count":39,"ltp_gene_count":9,"approved_date":"2017-04-19"},{"uniquename":"PMID:16741708","title":"Telomere length homeostasis.","citation":"Chromosoma 2006 Dec;115(6):413-25","abstract":"The physical ends of chromosomes, known as telomeres, protect chromosome ends from nucleolytic degradation and DNA repair activities. Conventional DNA replication enzymes lack the ability to fully replicate telomere ends. In addition, nucleolytic activities contribute to telomere erosion. Short telomeres trigger DNA damage checkpoints, which mediate cellular senescence. Telomere length homeostasis requires telomerase, a cellular reverse transcriptase, which uses an internal RNA moiety as a template for the synthesis of telomere repeats. Telomerase elongates the 3' ends of chromosomes, whereas the complementary strand is filled in by conventional DNA polymerases. In humans, telomerase is ubiquitously expressed only during the first weeks of embryogenesis, and is subsequently downregulated in most cell types. Correct telomere length setting is crucial for long-term survival. The telomere length reserve must be sufficient to avoid premature cellular senescence and the acceleration of age-related disease. On the other side, telomere shortening suppresses tumor formation through limiting the replicative potential of cells. In recent years, novel insight into the regulation of telomerase at chromosome ends has increased our understanding on how telomere length homeostasis in telomerase-positive cells is achieved. Factors that recruit telomerase to telomeres in a cell cycle-dependent manner have been identified in Saccharomyces cerevisiae. In humans, telomerase assembles with telomeres during S phase of the cell cycle. Presumably through mediating formation of alternative telomere structures, telomere-binding proteins regulate telomerase activity in cis to favor preferential elongation of the shortest telomeres. Phosphoinositide 3-kinase related kinases are also required for telomerase activation at chromosome ends, at least in budding and fission yeast. In vivo analysis of telomere elongation kinetics shows that telomerase does not act on every telomere in each cell cycle but that it exhibits an increasing preference for telomeres as their lengths decline. This suggests a model in which telomeres switch between extendible and nonextendible states in a length-dependent manner. In this review we expand this model to incorporate the finding that telomerase levels also limit telomere length and we propose a second switch between a non-telomerase-associated \"extendible\" and a telomerase-associated \"extending\" state.","authors":"Hug N, Lingner J","authors_abbrev":"Hug N et al.","pubmed_publication_date":"Dec 2006","pubmed_entrez_date":"2006-06-03","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23103765","title":"CHD1 remodelers regulate nucleosome spacing in vitro and align nucleosomal arrays over gene coding regions in S. pombe.","citation":"EMBO J 2012 Nov 28;31(23):4388-403","abstract":"Nucleosome positioning governs access to eukaryotic genomes. Many genes show a stereotypic organisation at their 5'end: a nucleosome free region just upstream of the transcription start site (TSS) followed by a regular nucleosomal array over the coding region. The determinants for this pattern are unclear, but nucleosome remodelers are likely critical. Here we study the role of remodelers in global nucleosome positioning in S. pombe and the corresponding changes in expression. We find a striking evolutionary shift in remodeler usage between budding and fission yeast. The S. pombe RSC complex does not seem to be involved in nucleosome positioning, despite its prominent role in S. cerevisiae. While S. pombe lacks ISWI-type remodelers, it has two CHD1-type ATPases, Hrp1 and Hrp3. We demonstrate nucleosome spacing activity for Hrp1 and Hrp3 in vitro, and that together they are essential for linking regular genic arrays to most TSSs in vivo. Impaired arrays in the absence of either or both remodelers may lead to increased cryptic antisense transcription, but overall gene expression levels are only mildly affected.","doi":"10.1038/emboj.2012.289","authors":"Pointner J, Persson J, Prasad P, Norman-Axelsson U, Strålfors A, Khorosjutina O, Krietenstein N, Svensson JP, Ekwall K, Korber P","authors_abbrev":"Pointner J et al.","pubmed_publication_date":"28 Nov 2012","pubmed_entrez_date":"2012-10-30","publication_year":"2012","canto_session_key":"89ee84cdc4db21b4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.01","SPAC1783.05","SPBP35G2.10"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:12185840","title":"Schizosaccharomyces pombe Pmf1p is structurally and functionally related to Mmf1p of Saccharomyces cerevisiae.","citation":"Yeast 2002 Jun 15;19(8):703-11","abstract":"A novel family of small proteins, termed p14.5 or YERO57c/YJGFc, has been identified. Independent studies indicate that p14.5 family members are multifunctional proteins involved in several pathways, e.g. regulation of translation or activation of the protease mu-calpain. We have previously shown that Mmf1p, a p14.5 of the budding yeast Saccharomyces cerevisiae, is localized in the mitochondria and influences mitochondrial DNA stability. In addition, we have demonstrated that Mmf1p is functionally related to p14.5 of mammalian cells. To explore further the evolutionary conservation of the mitochondrial function(s) of the p14.5s we have extended our study to the fission yeast, Schizosaccharomyces pombe. In this organism two p14.5 homologous proteins are present: Pmf1p (pombe mitochondrial factor 1) and Hpm1p (homologous Pmf1p factor 1). We have generated a specific Pmf1p antibody, which recognizes a single band of approximately 15 kDa in total cellular extracts. Cellular fractionation experiments indicate that Pmf1p localizes in the mitochondria as well as in the cytoplasm. We also show that Pmf1p shares several properties of S. cerevisiae Mmf1p. Indeed, Pmf1p restores the wild-type phenotype when expressed in delta mmf1 S. cerevisiae cells. Deletion of the leader sequence of Pmf1p abrogates its ability to localize in mitochondria and to functionally replace Mmf1p. Thus, these data together with our previous study show that the mitochondrial function(s) of the p14.5 family members are highly conserved in eukaryotic cells.","authors":"Marchini A, Accardi R, Malanchi I, Schyr E, Oxelmark E, De Pinto V, Jauniaux JC, Maundrell K, Tommasino M","authors_abbrev":"Marchini A et al.","pubmed_publication_date":"15 Jun 2002","pubmed_entrez_date":"2002-08-21","publication_year":"2002","canto_session_key":"6f44322282953a7c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-10-31 22:00:24","canto_approved_date":"2022-02-07 16:41:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-10-31 20:11:29","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2G2.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-10-31"},{"uniquename":"PMID:17696611","title":"SREBP controls oxygen-dependent mobilization of retrotransposons in fission yeast.","citation":"PLoS Genet 2007 Aug;3(8):e131","abstract":"Retrotransposons are mobile genetic elements that proliferate through an RNA intermediate. Transposons do not encode transcription factors and thus rely on host factors for mRNA expression and survival. Despite information regarding conditions under which elements are upregulated, much remains to be learned about the regulatory mechanisms or factors controlling retrotransposon expression. Here, we report that low oxygen activates the fission yeast Tf2 family of retrotransposons. Sre1, the yeast ortholog of the mammalian membrane-bound transcription factor sterol regulatory element binding protein (SREBP), directly induces the expression and mobilization of Tf2 retrotransposons under low oxygen. Sre1 binds to DNA sequences in the Tf2 long terminal repeat that functions as an oxygen-dependent promoter. We find that Tf2 solo long terminal repeats throughout the genome direct oxygen-dependent expression of adjacent coding and noncoding sequences, providing a potential mechanism for the generation of oxygen-dependent gene expression.","authors":"Sehgal A, Lee CY, Espenshade PJ","authors_abbrev":"Sehgal A et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-08-19","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10447591","title":"Reconstitution of caspase-mediated cell-death signalling in Schizosaccharomyces pombe.","citation":"Curr Genet 1999 Aug;36(1-2):21-8","abstract":"Two pro-apoptotic proteases, caspase-1 and caspase-3, have been expressed as full-length proteins in the fission yeast Schizosaccharomyces pombe. Both proteins autoprocess to generate the corresponding active enzyme and both are lethal to the yeast cell. Lethality is due to catalytic activity since the expression of the inactive mutant forms of both caspases does not result in an obvious phenotype. Caspase-expressing yeast can be rescued by co-expression of the baculovirus protein p35, a known inhibitor of the caspase family. Co-expression of Bcl-2, another anti-apoptotic protein, does not prevent the cell death induced by either caspase. However, Bcl-2 is itself cleaved by both caspase-1 and caspase-3 at two adjacent recognition sites, YEWD(31')A and DAGD(34')V respectively, immediately downstream from the N-terminal BH4 domain, a region of Bcl-2 which is essential for its anti-apoptotic activity; similar cleavage of Bcl-2 by caspases has been demonstrated in mammalian cells. Hence, key elements of the apoptotic pathway can be reliably reconstituted in fission yeast, opening the way to exploit yeast in order to study the control of apoptosis. Furthermore, the activity of caspase-3, although not caspase-1, can be demonstrated in vitro using chromogenic substrates. This offers the possibility of using caspase-producing strains of yeast to screen for chemical inhibitors either in vivo or in vitro.","authors":"Ryser S, Vial E, Magnenat E, Schlegel W, Maundrell K","authors_abbrev":"Ryser S et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-08-14","publication_year":"1999","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16483313","title":"Securin can have a separase cleavage site by substitution mutations in the domain required for stabilization and inhibition of separase.","citation":"Genes Cells 2006 Mar;11(3):247-60","abstract":"Securin-separase complex is required for sister chromatid separation. Securin degrades in an APC/cyclosome dependent manner. Separase is activated on the destruction of securin and cleaves cohesin. Fission yeast securin/Cut2 required for proper separase localization has the motifs for destruction and separase-binding at the N- and C-termini, respectively. We report here the third essential domain, which becomes toxic when the 76-amino acid fragment (81-156) in the middle is overproduced. The fragment inhibits separase, while separase is recruited normally and securin is destroyed. It may interfere with separase activation after destruction of securin. If the 127DIE129 stretch is substituted for AIA, the fragment toxicity and the full-length function are abolished. Interestingly, Cut2 is cleaved in a separase dependent manner if the cleavage consensus is introduced following the DIE sequence. This finding is consistent with the proposed model that the DIE region may mimic the cleavage site of separase and inhibit the activation of separase. Evidence for physical interaction between the fragment and separase is provided. A temperature sensitive mutation cut1-K73 isolated by its specific resistance to the fragment toxicity resides in the superhelical region of separase, suggesting that the catalytic site and the helical region in separase may cooperate for activation.","authors":"Nagao K, Yanagida M","authors_abbrev":"Nagao K et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-02-18","publication_year":"2006","canto_session_key":"0ed011499aba521b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-03-01 18:17:43","canto_approved_date":"2026-01-31 14:54:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-19 14:26:13","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.17c","SPCC5E4.04","SPBC14C8.01c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2018-03-01"},{"uniquename":"PMID:19823717","title":"Towards real time analysis of protein secretion from single cells.","citation":"Lab Chip 2009 Nov 07;9(21):3047-9","abstract":"","doi":"10.1039/b908679j","authors":"Kortmann H, Kurth F, Blank LM, Dittrich PS, Schmid A","authors_abbrev":"Kortmann H et al.","pubmed_publication_date":"07 Nov 2009","pubmed_entrez_date":"2009-10-14","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27171419","title":"Histone H2B ubiquitylation represses gametogenesis by opposing RSC-dependent chromatin remodeling at the ste11 master regulator locus.","citation":"Elife 2016 May 12;5","abstract":"In fission yeast, the ste11 gene encodes the master regulator initiating the switch from vegetative growth to gametogenesis. In a previous paper, we showed that the methylation of H3K4 and consequent promoter nucleosome deacetylation repress ste11 induction and cell differentiation (Materne et al., 2015) but the regulatory steps remain poorly understood. Here we report a genetic screen that highlighted H2B deubiquitylation and the RSC remodeling complex as activators of ste11 expression. Mechanistic analyses revealed more complex, opposite roles of H2Bubi at the promoter where it represses expression, and over the transcribed region where it sustains it. By promoting H3K4 methylation at the promoter, H2Bubi initiates the deacetylation process, which decreases chromatin remodeling by RSC. Upon induction, this process is reversed and efficient NDR (nucleosome depleted region) formation leads to high expression. Therefore, H2Bubi represses gametogenesis by opposing the recruitment of RSC at the promoter of the master regulator ste11 gene.","doi":"10.7554/eLife.13500","authors":"Materne P, Vázquez E, Sánchez M, Yague-Sanz C, Anandhakumar J, Migeot V, Antequera F, Hermand D","authors_abbrev":"Materne P et al.","pubmed_publication_date":"12 May 2016","pubmed_entrez_date":"2016-05-13","publication_year":"2016","canto_session_key":"74f4cbe8e05fa5c6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-05-15 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2F3.15","SPCC622.09"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:7883711","title":"bfr1+, a novel gene of Schizosaccharomyces pombe which confers brefeldin A resistance, is structurally related to the ATP-binding cassette superfamily.","citation":"J Bacteriol 1995 Mar;177(6):1536-43","abstract":"We have isolated a Schizosaccharomyces pombe gene, bfr1+, which on a multicopy plasmid vector, pDB248', confers resistance to brefeldin A (BFA), an inhibitor of intracellular protein transport. This gene encodes a novel protein of 1,531 amino acids with an intramolecular duplicated structure, each half containing a single ATP-binding consensus sequence and a set of six transmembrane sequences. This structural characteristic of bfr1+ protein resembles that of mammalian P-glycoprotein, which, by exporting a variety of anticancer drugs, has been shown to be responsible for multidrug resistance in tumor cells. Consistent with this is that S. pombe cells harboring bfr1+ on pDB248' are resistant to actinomycin D, cerulenin, and cytochalasin B, as well as to BFA. The relative positions of the ATP-binding sequences and the clusters of transmembrane sequences within the bfr1+ protein are, however, transposed in comparison with those in P-glycoprotein; the bfr1+ protein has N-terminal ATP-binding sequence followed by transmembrane segments in each half of the molecule. The bfr1+ protein exhibited significant homology in primary and secondary structures with two recently identified multidrug resistance gene products of Saccharomyces cerevisiae, Snq2 and Sts1/Pdr5/Ydr1. The bfr1+ gene is not essential for cell growth or mating, but a delta bfr1 mutant exhibited hypersensitivity to BFA. We propose that the bfr1+ protein is another member of the ATP-binding cassette superfamily and serves as an efflux pump of various antibiotics.","authors":"Nagao K, Taguchi Y, Arioka M, Kadokura H, Takatsuki A, Yoda K, Yamasaki M","authors_abbrev":"Nagao K et al.","pubmed_publication_date":"Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_session_key":"55963af43fa3c0bf","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-12-09 15:49:35","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-01-30 16:20:29","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-30"},{"uniquename":"PMID:22084379","title":"Regulation of entry into gametogenesis.","citation":"Philos Trans R Soc Lond B Biol Sci 2011 Dec 27;366(1584):3521-31","abstract":"Gametogenesis is a fundamental aspect of sexual reproduction in eukaryotes. In the unicellular fungi Saccharomyces cerevisiae (budding yeast) and Schizosaccharomyces pombe (fission yeast), where this developmental programme has been extensively studied, entry into gametogenesis requires the convergence of multiple signals on the promoter of a master regulator. Starvation signals and cellular mating-type information promote the transcription of cell fate inducers, which in turn initiate a transcriptional cascade that propels a unique type of cell division, meiosis, and gamete morphogenesis. Here, we will provide an overview of how entry into gametogenesis is initiated in budding and fission yeast and discuss potential conserved features in the germ cell development of higher eukaryotes.","doi":"10.1098/rstb.2011.0081","authors":"van Werven FJ, Amon A","authors_abbrev":"van Werven FJ et al.","pubmed_publication_date":"27 Dec 2011","pubmed_entrez_date":"2011-11-16","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8175662","title":"Glycoprotein synthesis in yeast. Early events in N-linked oligosaccharide processing in Schizosaccharomyces pombe.","citation":"J Biol Chem 1994 Apr 29;269(17):12527-35","abstract":"Oligosaccharide-lipid precursors and glycoprotein N-linked oligosaccharides isolated from the fission yeast, Schizosaccharomyces pombe, were compared with those from the budding yeast, Saccharomyces cerevisiae. Bio-Gel P-4 chromatography of oligosaccharide intermediates showed that Glc3Man9GlcNAc2-PP-dol synthesis, transfer of glycan to protein, and glucose removal to yield Man9GlcNAc2 proceeded in S. pombe as in S. cerevisiae. Two series of oligosaccharides were released from S. pombe glycoproteins by endo-beta-N-acetylglucosaminidase H; large \"mannan-like\" structures and smaller precursor or \"core-filling\" species. Unexpectedly, the smallest S. pombe N-linked glycan was Man9GlcNAc, confirmed by 500 MHz 1H NMR spectroscopy to be the lipid-linked isomer. No endoplasmic reticulum Man9-alpha 1,2-mannosidase activity was detected in S. pombe, thus identifying Man9GlcNAc as the minimum precursor for oligosaccharide elongation in contrast to the Man8GlcNAc2 intermediate identified in S. cerevisiae (Byrd, J. C., Tarentino, A. L., Maley, F., Atkinson, P. H., and Trimble, R. B. (1982) J. Biol. Chem. 257, 14657-14666). S. pombe Hex10GlcNAc was at least four isomers by high pH anion-exchange chromatography with pulsed amperometric detection. Compositional analyses identified two of the major species as GalMan9GlcNAc and GlcMan9GlcNAc, the latter of which suggests that glycan trimming may be attenuated in the S. pombe endoplasmic reticulum. Hex13GlcNAc from S. pombe was homogeneous by mass spectrometry but yielded 12 species by high pH anion-exchange chromatography. Compositional analyses, alpha-galactosidase digestion, and lectin affinity chromatography on Griffonia simplicifolia lectin I-agarose indicated these to be a family of GalxMan13-xGlcNAc isomers (X = 1-4 residues). The absence of Man9GlcNAc2 to Man8GlcNAc2 trimming in S. pombe and elongation of the lipid precursor of Man9GlcNAc with both Man and Gal to form \"galactomannans\" provides a novel system for N-linked glycoprotein processing studies.","authors":"Ziegler FD, Gemmill TR, Trimble RB","authors_abbrev":"Ziegler FD et al.","pubmed_publication_date":"29 Apr 1994","pubmed_entrez_date":"1994-04-29","publication_year":"1994","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34458935","title":"Nickel induced cell impairments are negatively regulated by the Tor1 kinase in Schizosaccharomyces pombe.","citation":"World J Microbiol Biotechnol 2021 Aug 30;37(10):165","abstract":"In our study we investigated the effect of different nickel (NiSO 4 ·6H 2 O) (Ni) concentrations on cell division, cellular morphology and ionome homeostasis of the eukaryotic model organism Schizosaccharomyces pombe. Target of rapamycin (TOR) protein kinase is one of the key regulators of cell growth under different environmental stresses. We analyzed the effect of Ni on cell strains lacking the Tor1 signaling pathway utilizing light-absorbance spectroscopy, visualization, microscopy and inductively coupled plasma optical emission spectroscopy. Interestingly, our findings revealed that Ni mediated cell growth alterations are noticeably lower in Tor1 deficient cells. Greater size of Tor1 depleted cells reached similar quantitative parameters to wild type cells upon incubation with 400 μM Ni. Differences of ion levels among the two tested yeast strains were detected even before Ni addition. Addition of high concentration (1 mM) of the heavy metal, representing acute contamination, caused considerable changes in the ionome of both strains. Strikingly, Tor1 deficient cells displayed largely reduced Ni content after treatment compared to wild type controls (644.1 ± 49 vs. 2096.8 ± 75 μg/g), suggesting its significant role in Ni trafficking. Together our results predict yet undefined role for the Tor1 signaling in metal uptake and/or metabolism.","doi":"10.1007/s11274-021-03130-2","authors":"Navratilova A, Kovar M, Trakovicka A, Pozgajova M","authors_abbrev":"Navratilova A et al.","pubmed_publication_date":"30 Aug 2021","pubmed_entrez_date":"2021-08-30","publication_year":"2021","canto_session_key":"e2ec517a7b0628af","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-09-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC30D10.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU012619","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24244528","title":"UCS protein Rng3p is essential for myosin-II motor activity during cytokinesis in fission yeast.","citation":"PLoS One 2013;8(11):e79593","abstract":"UCS proteins have been proposed to operate as co-chaperones that work with Hsp90 in the de novo folding of myosin motors. The fission yeast UCS protein Rng3p is essential for actomyosin ring assembly and cytokinesis. Here we investigated the role of Rng3p in fission yeast myosin-II (Myo2p) motor activity. Myo2p isolated from an arrested rng3-65 mutant was capable of binding actin, yet lacked stability and activity based on its expression levels and inactivity in ATPase and actin filament gliding assays. Myo2p isolated from a myo2-E1 mutant (a mutant hyper-sensitive to perturbation of Rng3p function) showed similar behavior in the same assays and exhibited an altered motor conformation based on limited proteolysis experiments. We propose that Rng3p is not required for the folding of motors per se, but instead works to ensure the activity of intrinsically unstable myosin-II motors. Rng3p is specific to conventional myosin-II and the actomyosin ring, and is not required for unconventional myosin motor function at other actin structures. However, artificial destabilization of myosin-I motors at endocytic actin patches (using a myo1-E1 mutant) led to recruitment of Rng3p to patches. Thus, while Rng3p is specific to myosin-II, UCS proteins are adaptable and can respond to changes in the stability of other myosin motors.","doi":"10.1371/journal.pone.0079593","authors":"Stark BC, James ML, Pollard LW, Sirotkin V, Lord M","authors_abbrev":"Stark BC et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-11-19","publication_year":"2013","canto_session_key":"3a995b73ca205826","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2021-01-13 15:51:40","canto_approved_date":"2025-05-28 10:51:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-09 10:31:13","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC613.04c","SPCC645.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2021-01-13"},{"uniquename":"PMID:35567482","title":"Determinants of RPA megafoci localization to the nuclear periphery in response to replication stress.","citation":"G3 (Bethesda) 2022 Jul 06;12(7)","abstract":"Upon replication stress, ssDNA, coated by the ssDNA-binding protein RPA, accumulates and generates a signal to activate the replication stress response. Severe replication stress induced by the loss of minichromosome maintenance helicase subunit Mcm4 in the temperature-sensitive Schizosaccharomyces pombe degron mutant (mcm4-dg) results in the formation of a large RPA focus that is translocated to the nuclear periphery. We show that resection and repair processes and chromatin remodeler Swr1/Ino80 are involved in the large RPA foci formation and its relocalization to nuclear periphery. This concentrated accumulation of RPA increases the recruitment of Cds1 to chromatin and results in an aberrant cell cycle that lacks MBF-mediated G1/S accumulation of Tos4. These findings reveal a distinct replication stress response mediated by localized accumulation of RPA that allows the evasion of cell cycle arrest.","doi":"10.1093/g3journal/jkac116","authors":"Kim SM, Forsburg SL","authors_abbrev":"Kim SM et al.","pubmed_publication_date":"06 Jul 2022","pubmed_entrez_date":"2022-05-14","publication_year":"2022","canto_session_key":"4eb4b28a282d51e5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-05-16 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16A11.17"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:41786187","title":"Shugoshin holds the potential to inhibit APC/C and thereby prevents separase activation.","citation":"Int J Biol Macromol 2026 Mar 03;:151175","abstract":"Accurate chromosome segregation during mitosis and meiosis depends on shugoshin protein which localizes at the centromere of chromosomes. Sgo1, a meiosis-specific shugoshin in fission yeast, collaborates with the PP2A phosphatase enzyme to remove phosphate groups from Rec8 cohesin, thereby preventing its cleavage by separase during meiosis. Here we demonstrate that ectopic expression of Sgo1 causes chromosome segregation errors during mitosis, especially in cut1-206 separase mutant cells. However, Sgo1D-box mutant does not exhibit this effect in cut1-206 cells. Our molecular genetic analyses suggest that the Sgo1 D-box directly binds Slp1/CDC20, inhibiting APC/C-dependent separase activation and consequently preventing Rad21 cohesin cleavage. In contrast, during meiosis, the Sgo1 D-box mutant makes the cut1-206 mutant more difficult to cleave Rec8 cohesin. This is because the D-box mutation increases the amount of Sgo1 protein during meiosis, thereby enhancing its canonical protective ability against Rec8 cohesin. Thus, our studies using a separase mutant have revealed that Sgo1 has multiple faces to protect coheisn.","doi":"10.1016/j.ijbiomac.2026.151175","authors":"Zhang K, Guo S, Sun L, Hou H, Watanabe Y","authors_abbrev":"Zhang K et al.","pubmed_publication_date":"03 Mar 2026","pubmed_entrez_date":"2026-03-05","publication_year":"2026","canto_session_key":"9debc7862e07fda7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yoshinori Watanabe","canto_first_approved_date":"2026-04-20 15:56:39","canto_approved_date":"2026-04-20 15:56:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-04-13 05:23:08","canto_added_date":"2026-03-08 00:25:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":11,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yoshinori Watanabe","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC15E1.07c","SPAC821.08c","SPBC29A10.14","SPBP35G2.03c","SPCC188.02","SPCC5E4.04"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2026-04-20"},{"uniquename":"PMID:12930956","title":"Fission yeast Rhp51 is required for the maintenance of telomere structure in the absence of the Ku heterodimer.","citation":"Nucleic Acids Res 2003 Sep 01;31(17):5054-63","abstract":"The Schizosaccharomyces pombe Ku70-Ku80 heterodimer is required for telomere length regulation. Lack of pku70+ results in telomere shortening and striking rearrangements of telomere-associated sequences. We found that the rearrangements of telomere-associated sequences in pku80+ mutants are Rhp51 dependent, but not Rad50 dependent. Rhp51 bound to telomere ends when the Ku heterodimer was not present at telomere ends. We also found that the single-stranded G-rich tails increased in S phase in wild-type strains, while deletion of pku70+ increased the single-stranded overhang in both G2 and S phase. Based on these observations, we propose that Rhp51 binds to the G-rich overhang and promotes homologous pairing between two different telomere ends in the absence of Ku heterodimer. Moreover, pku80 rhp51 double mutants showed a significantly reduced telomere hybridization signal. Our results suggest that, although Ku heterodimer sequesters Rhp51 from telomere ends to inhibit homologous recombination activity, Rhp51 plays important roles for the maintenance of telomere ends in the absence of the Ku heterodimer.","authors":"Kibe T, Tomita K, Matsuura A, Izawa D, Kodaira T, Ushimaru T, Uritani M, Ueno M","authors_abbrev":"Kibe T et al.","pubmed_publication_date":"01 Sep 2003","pubmed_entrez_date":"2003-08-22","publication_year":"2003","canto_session_key":"2c44c3c8075d143b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-05-06 15:18:59","canto_approved_date":"2024-06-28 10:17:07","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-05-06 15:18:53","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":14,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC543.03c","SPAC30D11.10","SPAC1556.01c","SPAC644.14c","SPCC126.02c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2016-05-06"},{"uniquename":"PMID:10698951","title":"Essential interaction between the fission yeast DNA polymerase delta subunit Cdc27 and Pcn1 (PCNA) mediated through a C-terminal p21(Cip1)-like PCNA binding motif.","citation":"EMBO J 2000 Mar 01;19(5):1108-18","abstract":"Direct interaction between DNA polymerase delta and its processivity factor proliferating cell nuclear antigen (PCNA) is essential for effective replication of the eukaryotic genome, yet the precise manner by which this occurs is unclear. We show that the 54 kDa subunit of DNA polymerase delta from Schizosaccharomyces pombe interacts directly with Pcn1 (PCNA) both in vivo and in vitro. Binding is effected via a short sequence at the C-terminus of Cdc27 with significant similarity to the canonical PCNA binding motif first identified in the mammalian p21(Cip1) protein. This motif is both necessary and sufficient for binding of Pcn1 by Cdc27 in vitro and is essential for Cdc27 function in vivo. We also show that the Pcn1 binding motif in Cdc27 is distinct from its binding site for Cdc1, the 55 kDa B-subunit of polymerase delta, and present evidence that Cdc27 can bind to Pcn1 and Cdc1 simultaneously. Finally, we show that Cdc27 performs at least two distinct essential functions, one of which is independent of Pcn1 binding.","authors":"Reynolds N, Warbrick E, Fantes PA, MacNeill SA","authors_abbrev":"Reynolds N et al.","pubmed_publication_date":"01 Mar 2000","pubmed_entrez_date":"2000-03-04","publication_year":"2000","canto_session_key":"cf72468ea0fb98d3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-30 15:57:48","canto_approved_date":"2022-01-01 19:04:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-30 15:57:41","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":37,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27E2.05","SPBC16D10.09","SPBC1734.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-04-30"},{"uniquename":"PMID:15471884","title":"DNA binding domain in the replication checkpoint protein Mrc1 of Schizosaccharomyces pombe.","citation":"J Biol Chem 2004 Dec 17;279(51):53023-7","abstract":"The replication checkpoint is activated when replication forks are obstructed by DNA lesions or protein complexes bound to DNA or when DNA synthesis is restrained by the limited availability of deoxyribonucleotides. This checkpoint preserves genome integrity by stabilizing stalled forks and delaying the onset of mitosis. In the fission yeast Schizosaccharomyces pombe, Mrc1 is a replication checkpoint adaptor protein that allows the sensor kinase Rad3-Rad26 to activate the effector kinase Cds1. In Saccharomyces cerevisiae, Mrc1 associates with replication forks and co-precipitates with the DNA replication protein Cdc45. Whether or not Mrc1 interacts directly with DNA is unknown. Here we define a approximately 150 amino acid DNA binding domain (DBD) in the N-terminal region of S. pombe Mrc1. The DBD interacts preferentially with branched DNA structures in vitro. Deletion of the DBD or point mutations that diminish its DNA binding activity render cells sensitive to the replication inhibitor hydroxyurea. These mutations also impair the replication checkpoint arrest. The DBD has a helix-loop-helix motif that is predicted to bind DNA. This motif is conserved in the recently identified N-terminal DBD of human Claspin, a presumptive homolog of yeast Mrc1 proteins.","authors":"Zhao H, Russell P","authors_abbrev":"Zhao H et al.","pubmed_publication_date":"17 Dec 2004","pubmed_entrez_date":"2004-10-09","publication_year":"2004","canto_session_key":"5e1ab5b7f5ffc7d5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-04-06 09:19:26","canto_approved_date":"2026-06-09 08:15:44","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-04-06 09:19:17","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":10,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC694.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-04-06"},{"uniquename":"PMID:23826334","title":"Deletion of the fission yeast homologue of human insulinase reveals a TORC1-dependent pathway mediating resistance to proteotoxic stress.","citation":"PLoS One 2013;8(6):e67705","abstract":"Insulin Degrading Enzyme (IDE) is a protease conserved through evolution with a role in diabetes and Alzheimer's disease. The reason underlying its ubiquitous expression including cells lacking identified IDE substrates remains unknown. Here we show that the fission yeast IDE homologue (Iph1) modulates cellular sensitivity to endoplasmic reticulum (ER) stress in a manner dependent on TORC1 (Target of Rapamycin Complex 1). Reduced sensitivity to tunicamycin was associated with a smaller number of cells undergoing apoptosis. Wild type levels of tunicamycin sensitivity were restored in iph1 null cells when the TORC1 complex was inhibited by rapamycin or by heat inactivation of the Tor2 kinase. Although Iph1 cleaved hallmark IDE substrates including insulin efficiently, its role in the ER stress response was independent of its catalytic activity since expression of inactive Iph1 restored normal sensitivity. Importantly, wild type as well as inactive human IDE complemented gene-invalidated yeast cells when expressed at the genomic locus under the control of iph1(+) promoter. These results suggest that IDE has a previously unknown function unrelated to substrate cleavage, which links sensitivity to ER stress to a pro-survival role of the TORC1 pathway.","doi":"10.1371/journal.pone.0067705","authors":"Beuzelin C, Evnouchidou I, Rigolet P, Cauvet-Burgevin A, Girard PM, Dardalhon D, Culina S, Gdoura A, van Endert P, Francesconi S","authors_abbrev":"Beuzelin C et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-07-05","publication_year":"2013","canto_session_key":"c6faf2cb64062885","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-07-16 14:10:23","annotation_curators":[],"annotation_file_curators":[],"genes":["SPACUNK4.12c","SPBC30D10.10c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:10494821","title":"Felix Hoppe-Seyler Lecture 1999. Cyclin dependent kinases and regulation of the fission yeast cell cycle.","citation":"Biol Chem 1999;380(7-8):729-33","abstract":"The cyclin dependent kinases (CDKs), formed by complexes between Cdc2p and the B-cyclins Cig2p and Cdc13p, have a central role in regulating the fission yeast cell cycle and maintaining genomic stability. The CDK Cig2p/Cdc2p controls the onset of S-phase and the CDK Cdc13p/Cdc2p controls the onset of mitosis and ensures that there is only one S-phase in each cell. Cdc13p/Cdc2p can replace Cig2p/Cdc2p forthe onset of S-phase, suggesting that the increasing activity of a single CDK during the cell cycle is sufficient to drive a cell in an orderly fashion into S-phase and into mitosis. If S-phase is incomplete, then inhibition of Cdc13p/ Cdc2p prevents cells with unreplicated DNA from undergoing a catastrophic entry into mitosis. Control of CDK activity is also important to allow cells to exit the cell cycle and accumulate in G1 in response to nutritional deprivation and the presence of pheromone.","authors":"Nurse P","authors_abbrev":"Nurse P","pubmed_publication_date":"1999","pubmed_entrez_date":"1999-09-24","publication_year":"1999","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU013563","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19521533","title":"Universal temporal profile of replication origin activation in eukaryotes.","citation":"PLoS One 2009 Jun 12;4(6):e5899","abstract":"Although replication proteins are conserved among eukaryotes, the sequence requirements for replication initiation differ between species. In all species, however, replication origins fire asynchronously throughout S phase. The temporal program of origin firing is reproducible in cell populations but largely probabilistic at the single-cell level. The mechanisms and the significance of this program are unclear. Replication timing has been correlated with gene activity in metazoans but not in yeast. One potential role for a temporal regulation of origin firing is to minimize fluctuations in replication end time and avoid persistence of unreplicated DNA in mitosis. Here, we have extracted the population-averaged temporal profiles of replication initiation rates for S. cerevisiae, S. pombe, D. melanogaster, X. laevis and H. sapiens from genome-wide replication timing and DNA combing data. All the profiles have a strikingly similar shape, increasing during the first half of S phase then decreasing before its end. A previously proposed minimal model of stochastic initiation modulated by accumulation of a recyclable, limiting replication-fork factor and fork-promoted initiation of new origins, quantitatively described the observed profiles without requiring new implementations.The selective pressure for timely completion of genome replication and optimal usage of replication proteins that must be imported into the cell nucleus can explain the generic shape of the profiles. We have identified a universal behavior of eukaryotic replication initiation that transcends the mechanisms of origin specification. The population-averaged efficiency of replication origin usage changes during S phase in a strikingly similar manner in a highly diverse set of eukaryotes. The quantitative model previously proposed for origin activation in X. laevis can be generalized to explain this evolutionary conservation.","doi":"10.1371/journal.pone.0005899","authors":"Goldar A, Marsolier-Kergoat MC, Hyrien O","authors_abbrev":"Goldar A et al.","pubmed_publication_date":"12 Jun 2009","pubmed_entrez_date":"2009-06-13","publication_year":"2009","canto_triage_status":"DNA replication related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26900659","title":"Novel morpholinoquinoline nucleus clubbed with pyrazoline scaffolds: Synthesis, antibacterial, antitubercular and antimalarial activities.","citation":"Eur J Med Chem 2016 Apr 13;112:270-279","abstract":"A series of novel morpholinoquinoline based conjugates with pyrazoline moiety were synthesized under microwave irradiation. The newly synthesized compounds were screened for their preliminary in vitro antibacterial activity against a panel of pathogenic strains of bacteria and fungi, antituberculosis activity against Mycobacterium tuberculosis H37Rv and antimalarial activity against Plasmodium falciparum. Most of them exhibited significant antibacterial activity as compared to the first line drugs. Compounds 6a and 9d were found to possess excellent antibacterial activity potency as compared to ampicillin (286 μM), chloramphenicol (154 μM) and ciprofloxacin (150 μM). In antifungal screening, against Candida albicans, compounds 6c, 7c, 8a, 8b, 8c and 9b showed significant activity as compared to griseofulvin (1147 μM). Compounds 8b, 6b, 9d, 6a, 9b, 7b and 8a displayed brilliant activity against P. falciparum strain as compared to chloroquine (IC50 0.062 μM) as well as quinine (IC50 0.826 μM). Compounds 6d, 7b, 8b, 9c and 9d exhibited superior antitubercular activity. Among them 8b was found to be equipotent to rifampicin with 95% inhibition. The cytotoxicity of the synthesized compounds was tested using bioassay of Schizosaccharomyces pombe cells at cellular level.","doi":"10.1016/j.ejmech.2016.02.016","authors":"Karad SC, Purohit VB, Thakor P, Thakkar VR, Raval DK","authors_abbrev":"Karad SC et al.","pubmed_publication_date":"13 Apr 2016","pubmed_entrez_date":"2016-02-23","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-02-25 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU007763","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34944077","title":"Mitophagy in Yeast: Molecular Mechanism and Regulation.","citation":"Cells 2021 Dec 17;10(12)","abstract":"Mitophagy is a type of autophagy that selectively degrades mitochondria. Mitochondria, known as the \"powerhouse of the cell\", supply the majority of the energy required by cells. During energy production, mitochondria produce reactive oxygen species (ROS) as byproducts. The ROS damage mitochondria, and the damaged mitochondria further produce mitochondrial ROS. The increased mitochondrial ROS damage cellular components, including mitochondria themselves, and leads to diverse pathologies. Accordingly, it is crucial to eliminate excessive or damaged mitochondria to maintain mitochondrial homeostasis, in which mitophagy is believed to play a major role. Recently, the molecular mechanism and physiological role of mitophagy have been vigorously studied in yeast and mammalian cells. In yeast, Atg32 and Atg43, mitochondrial outer membrane proteins, were identified as mitophagy receptors in budding yeast and fission yeast, respectively. Here we summarize the molecular mechanisms of mitophagy in yeast, as revealed by the analysis of Atg32 and Atg43, and review recent progress in our understanding of mitophagy induction and regulation in yeast.","doi":"10.3390/cells10123569","authors":"Innokentev A, Kanki T","authors_abbrev":"Innokentev A et al.","pubmed_publication_date":"17 Dec 2021","pubmed_entrez_date":"2021-12-24","publication_year":"2021","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-12-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.01c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:7657164","title":"Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell size at division in fission yeast.","citation":"Genes Dev 1995 Sep 01;9(17):2117-30","abstract":"Simultaneous inactivation of pyp1 and pyp2 PTPases in fission yeast leads to aberrant cell morphology and growth arrest. Spontaneous recessive mutations that bypass the requirement for pyp1 and pyp2 and reside in two complementation groups were isolated, sty1 and sty2. sty1- and sty2- mutant cells are substantially delayed in the timing of mitotic initiation. We have isolated the sty1 gene, which encodes a MAP kinase that is closely related to a subfamily of MAP kinases regulated by osmotic stress including Saccharomyces cervisiae HOG1 and human CSBP1. We find that sty2 is allelic to the wis1 MAP kinase kinase and that delta sty1 and delta wis1 cells are unable to grow in high osmolarity medium. Osmotic stress induces both tyrosine phosphorylation of Sty1 and a reduction in cell size at division. Pyp2 associates with and tyrosine dephosphorylates Sty1 in vitro. We find that wis1-dependent induction of pyp2 mRNA is responsible for tyrosine dephosphorylation of Sty1 in vivo on prolonged exposure to osmotic stress. We conclude that Pyp1 and Pyp2 are tyrosine-specific MAP kinase phosphatases that inactivate an osmoregulated MAP kinase, Sty1, which acts downstream of the Wis1 MAP kinase kinase to control cell size at division in fission yeast.","authors":"Millar JB, Buck V, Wilkinson MG","authors_abbrev":"Millar JB et al.","pubmed_publication_date":"01 Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_session_key":"beeee61f81d10c76","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-02 14:14:33","canto_approved_date":"2025-06-12 05:50:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-05-28 10:46:21","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":46,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24H6.05","SPAC26F1.10c","SPAC24B11.06c","SPAC19D5.01","SPBC409.07c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2018-10-02"},{"uniquename":"PANTHER:PTHR13420","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:26239","SPBC839.19"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:AU012722","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22504286","title":"The telomeric transcriptome: from fission yeast to mammals.","citation":"Int J Biochem Cell Biol 2012 Jul;44(7):1055-9","abstract":"The ends of linear eukaryotic chromosomes are transcribed into different species of non-coding transcripts (the telomeric transcriptome), including TERRA (telomeric repeat-containing RNA) molecules; however, the functions associated with the telomeric transcriptome remain elusive. Experimental evidence accumulated during the past few years indicates that the transcriptional activity of telomeres is changed in cells in which the integrity of the telomeres or the heterochromatic state of chromosome ends is altered. On the contrary transcription of a telomere appears not to be influenced by its length. In this paper we briefly review the current state of knowledge on the composition, biogenesis, and regulation of the telomeric transcriptome from yeasts to humans. We also suggest a model in which TERRA is part of the DNA damage response triggered by dysfunctional telomeres and discuss the potential involvement of telomere transcription in the development of human pathologies.","doi":"10.1016/j.biocel.2012.03.021","authors":"Bah A, Azzalin CM","authors_abbrev":"Bah A et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-04-17","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11524018","title":"Quaternary and domain structure of glycoprotein processing glucosidase II.","citation":"Biochemistry 2001 Sep 04;40(35):10717-22","abstract":"Glucose trimming from newly synthesized glycoproteins regulates their interaction with the calnexin/calreticulin chaperone system. We have recently proposed that glucosidase II consisted of two different subunits, alpha and beta. The alpha subunit is the catalytic component, and deletion of its homologue in yeast obliterates glucosidase II activity. Deletion of the homologue of the noncatalytic beta subunit in Schizosaccharomices pombe drastically reduces glucosidase II activity, but the role of the beta subunit in glucosidase II activity has not been established. Furthermore, a direct interaction between alpha and beta subunits has not been demonstrated. Using chemical cross-linking and hydrodynamic analysis by analytical ultracentrifugation, we found that the two subunits form a defined complex, composed of one catalytic subunit and one accessory subunit (alpha(1)beta(1)) with a molecular mass of 161 kDa. The complex had an s value of 6.3 S, indicative of a highly nonglobular shape. The asymmetric shape of the alpha(1)beta(1) complex was confirmed by its high susceptibility to proteases. The beta subunit could be proteolytically removed from the alpha(1)beta(1) complex without affecting catalysis, demonstrating that it is not required for glucosidase II activity in vitro. Furthermore, we isolated a monomeric C-terminal fragment of the alpha subunit, which retained full glucosidase activity. We conclude that the catalytic core of glucosidase II resides in a globular domain of the alpha subunit, which can function independently of the beta subunit, while the complete alpha and beta subunits assemble in a defined heterodimeric complex with a highly extended conformation, which may favor interaction with other proteins in the endoplasmic reticulum (ER). Through its C-terminal HDEL signal, the beta subunit may retain the complete alpha(1)beta(1) complex in the ER.","authors":"Trombetta ES, Fleming KG, Helenius A","authors_abbrev":"Trombetta ES et al.","pubmed_publication_date":"04 Sep 2001","pubmed_entrez_date":"2001-08-29","publication_year":"2001","canto_session_key":"e7042597535762b5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-07-16 12:16:32","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-16 12:16:25","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-07-16"},{"uniquename":"PMID:42270435","title":"Interaction Between Rec8 and Mis4 Is Required for Axis-Loop Chromatin Formation and Homologous Chromosome Recombination During Meiosis.","citation":"Genes Cells 2026 Jul;31(4):e70128","abstract":"The Rec8 cohesin complex is required for the pairing and recombination of homologous chromosomes during meiosis, as well as for the cohesion of sister chromatids. In the fission yeast Schizosaccharomyces pombe, we previously identified a rec8-F204S mutant that lost the ability to assemble the axis-loop chromatin structure without losing sister chromatid cohesion. This mutant showed reduced meiotic recombination, indicating that pairing and recombination of homologous chromosomes require the formation of the axis-loop chromatin structure mediated by the Rec8 cohesin complex. Loading of the Rec8 cohesin complex onto chromatin is mediated by Mis4 (NIPBL in humans; Scc2 in yeast). In this study, to elucidate the functions of Mis4, we identified a mis4-LR mutant (L1150S and R1159G) that reproduced the phenotypes of the rec8-F204S mutant, which is defective in chromatin axis formation and homologous recombination while retaining sister chromatid cohesion. These mutation sites (Mis4-L1150, Mis4-R1159, and Rec8-F204) are all localized at the interaction surface between Mis4 and Rec8. Biochemical analysis revealed that the Mis4-LR mutant protein exhibited reduced Rec8-binding activity. Considering that the mis4-LR mutant phenocopied the rec8-F204S mutant, our results demonstrate that the Mis4-Rec8 interaction is required for proper formation of Rec8-dependent meiotic chromosome axis.","doi":"10.1111/gtc.70128","authors":"Sakuno T, Murayama Y, Haraguchi T, Hiraoka Y","authors_abbrev":"Sakuno T et al.","pubmed_publication_date":"Jul 2026","pubmed_entrez_date":"2026-06-10","publication_year":"2026","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2026-06-11 23:25:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33260998","title":"High-Throughput Flow Cytometry Combined with Genetic Analysis Brings New Insights into the Understanding of Chromatin Regulation of Cellular Quiescence.","citation":"Int J Mol Sci 2020 Nov 27;21(23)","abstract":"Cellular quiescence is a reversible differentiation state when cells are changing the gene expression program to reduce metabolic functions and adapt to a new cellular environment. When fission yeast cells are deprived of nitrogen in the absence of any mating partner, cells can reversibly arrest in a differentiated G 0 -like cellular state, called quiescence. This change is accompanied by a marked alteration of nuclear organization and a global reduction of transcription. Using high-throughput flow cytometry combined with genetic analysis, we describe the results of a comprehensive screen for genes encoding chromatin components and regulators that are required for the entry and the maintenance of cellular quiescence. We show that the histone acetylase and deacetylase complexes, SAGA and Rpd3, have key roles both for G 0  entry and survival during quiescence. We reveal a novel function for the Ino80 nucleosome remodeling complex in cellular quiescence. Finally, we demonstrate that components of the MRN complex, Rad3, the nonhomologous end-joining, and nucleotide excision DNA repair pathways are essential for viability in G 0. ","doi":"10.3390/ijms21239022","authors":"Zahedi Y, Durand-Dubief M, Ekwall K","authors_abbrev":"Zahedi Y et al.","pubmed_publication_date":"27 Nov 2020","pubmed_entrez_date":"2020-12-02","publication_year":"2020","canto_session_key":"989d12e87f7e108e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2020-12-14 13:08:21","canto_approved_date":"2020-12-14 13:08:21","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2020-12-14 13:08:11","canto_added_date":"2020-12-04 01:15:05","annotation_curators":[],"file_curator_name":"Karl Ekwall","file_curator_role":"community","annotation_file_curators":[{"name":"Karl Ekwall","community_curator":true,"annotation_count":978,"orcid":"0000-0002-3029-4041","file_type":"PHAF","file_name":"PMID_33260998_phaf.tsv"}],"genes":["SPBC16A3.19","SPBC3B8.02","SPBC839.17c","SPBC649.03","SPAC3G6.06c","SPBC1773.01","SPBC31F10.14c","SPAC1420.03","SPCC622.16c","SPAC25H1.06","SPBC16G5.03","SPCC338.05c","SPAC4F10.14c","SPAC25G10.02","SPBC4B4.03","SPAC16E8.13","SPAC664.15","SPAC8C9.14","SPBC15C4.06c","SPBC19G7.01c","SPBC11B10.10c","SPAC19G12.13c","SPAC23H4.09","SPAC1687.14c","SPBC16E9.11c","SPAC20G4.04c","SPBC29A10.03c","SPBC30D10.04","SPBC1347.01c","SPCC1494.03","SPBC3E7.02c","SPBP8B7.07c","SPAC16.05c","SPCC1322.12c","SPBC3D6.04c","SPAC1002.14","SPBC15D4.01c","SPBC16D10.08c","SPBP8B7.25","SPCC1223.01","SPBC16C6.10","SPCC1682.13","SPBC1105.14","SPAC1556.01c","SPCC1223.13","SPCP25A2.02c","SPAC13G7.07","SPBP16F5.07","SPCC550.14","SPCC4G3.15c","SPAC1F7.11c","SPBC12D12.02c","SPCC11E10.08","SPAC821.07c","SPAC20H4.04","SPBC106.01","SPAC25B8.11","SPAC10F6.16","SPBC17G9.02c","SPAC806.08c","SPBC14F5.12c","SPBP35G2.03c","SPBP16F5.03c","SPCC1393.02c","SPAC3H1.12c","SPCC553.07c","SPBC215.03c","SPCC364.02c","SPCC1795.01c","SPBC36B7.03","SPCC4E9.01c","SPAC20G8.08c","SPBC1271.01c","SPAC23D3.01","SPAC22A12.01c","SPBC947.11c","SPBC27.02c","SPBC28E12.02","SPBC2F12.13","SPAC644.14c","SPAC3G9.01","SPBC83.03c","SPAC2H10.01","SPCC1739.12","SPBC13E7.08c","SPAC3G6.11","SPCC16C4.03","SPAC29B12.01","SPBC887.04c","SPAC23C4.12","SPAC29B12.02c","SPAC16E8.12c","SPAC589.08c","SPAC14C4.12c","SPBC36B7.05c","SPBC725.11c","SPBP16F5.04","SPAPB1A11.04c","SPAP27G11.15","SPBC1604.16c","SPAC31G5.11","SPCC777.02","SPBP22H7.05c","SPBC902.04","SPAC22F3.02","SPCC417.02","SPAC57A7.09","SPAC17H9.03c","SPBC19F8.02","SPAC3G6.01","SPAC17A5.11","SPCC1902.01","SPAC1327.01c","SPAC23C4.03","SPCC1322.14c","SPAC20H4.10","SPAC30.03c","SPBPB8B6.04c","SPCP31B10.05","SPAC11H11.05c","SPBC19G7.16","SPBC20F10.06","SPBC119.06","SPBC354.05c","SPAC26H5.03","SPAC1486.02c","SPAC4H3.01","SPBC16G5.16","SPCC1739.05","SPAC20H4.02","SPBC1773.12","SPCC364.06","SPBC1105.12","SPCC1919.15","SPCC594.07c","SPBC29A3.03c","SPAC694.06c","SPBC1347.02","SPAC1834.04","SPAPB17E12.03","SPCC18.03","SPCC18.06c","SPAC23C11.08","SPBC800.02","SPAC6G9.10c","SPAC17G8.10c","SPCC126.07c","SPAC17G8.09","SPAC17H9.14c","SPBC1105.09","SPBC16H5.05c","SPBC776.02c","SPAC4D7.07c","SPAC824.04","SPAC3A11.13","SPAC23A1.07","SPBC405.06","SPBC11G11.05","SPAC57A10.09c","SPAC31G5.18c","SPAC13G6.01c","SPAC1002.05c","SPAC29A4.18","SPBP8B7.23","SPAC13F5.05","SPCC16A11.16c","SPBC31F10.13c","SPAC4H3.05","SPAC823.03","SPAC6B12.05c","SPCC4G3.19","SPCC757.04","SPCC1393.08","SPAC12G12.10","SPAC4G9.11c","SPCC24B10.16c","SPBC16A3.07c","SPCC23B6.03c","SPAC222.04c","SPBC15D4.03","SPBC1685.08","SPAC17H9.10c","SPAC11D3.16c","SPBC19C2.14","SPBC20F10.10","SPBC2D10.12","SPAC24H6.03","SPCC285.16c","SPBC3D6.10","SPBC317.01","SPBC609.05","SPAC13C5.07","SPBC530.05","SPAC23D3.09","SPAC1565.07c","SPBC25D12.02c","SPBC902.02c","SPAC4F10.02","SPAC26H5.02c","SPCC188.13c","SPCC548.05c","SPBC1A4.03c","SPAC664.01c","SPBC1D7.01","SPAC22F8.12c","SPBC32F12.07c","SPAC23H3.05c","SPBC29B5.01","SPCC24B10.07","SPAC2E1P5.03","SPBC17D11.04c","SPAC1399.05c","SPBC1778.02","SPBC725.12","SPBC3H7.15","SPAC13D6.01","SPAC1486.10","SPBC56F2.05c","SPAC1952.05","SPAC11E3.05","SPAC17H9.19c","SPBC8D2.04","SPAC12B10.12c","SPAC12G12.01c","SPBC16G5.11c","SPBC13E7.06","SPBP8B7.30c","SPAC32A11.03c","SPAC22F3.06c","SPAC11E3.04c","SPBC1773.09c","SPAC17A2.12","SPCC1442.13c","SPAC9E9.13","SPCC306.04c","SPAC23C4.09c","SPCC1393.05","SPBC4F6.15c","SPAC5D6.08c","SPAC13D6.02c","SPCC320.03","SPCC553.04","SPAC6G9.13c","SPAC18B11.07c","SPCC663.12","SPCC830.07c","SPAC19G12.02c","SPAC1F3.06c","SPAC11G7.04","SPBC15C4.01c","SPBC582.04c","SPAC16C9.04c","SPAC31A2.11c","SPAC31A2.15c","SPAC13A11.04c","SPBC2D10.20","SPAC15A10.11","SPAC4G9.06c","SPAC22E12.19","SPAC6G9.03c","SPAC2F3.15","SPAC2C4.10c","SPAC222.15","SPBC530.11c","SPBC19G7.04","SPCC188.07","SPAC1B3.17","SPAC13A11.03","SPAC30D11.14c","SPBC4F6.16c","SPAC140.03","SPAC6F6.03c","SPAC7D4.14c","SPAC5D6.02c","SPCC4G3.05c","SPAC6B12.08","SPCC970.07c","SPAC1687.05","SPAC17G8.07","SPCC1020.12c","SPCC285.17","SPBC2G2.14","SPAC10F6.08c","SPBP35G2.10","SPAC23E2.01","SPBC29A3.13","SPBC1105.11c","SPBC947.01","SPAPYUG7.04c","SPAC1142.03c","SPAC1687.09","SPBC6B1.04","SPAC10F6.11c","SPAC19E9.02","SPCC736.11","SPBC28F2.10c","SPBC3D6.13c","SPCC645.13","SPBC17A3.10","SPAC19A8.10","SPCC1322.02","SPBC16D10.07c","SPBC29A10.05","SPAC21E11.05c","SPBC21D10.10","SPAC1B3.05","SPBC215.02","SPCC736.08","SPCC74.03c","SPAC14C4.13","SPCC18.09c","SPAC18G6.15","SPBC365.06","SPBC651.11c","SPBC15D4.02","SPBC582.05c","SPBC1861.01c","SPAC1039.05c","SPAC637.10c","SPAC2F7.08c","SPBC12D12.09","SPBC713.06","SPBC1198.11c","SPAC664.07c","SPBC21D10.12","SPAC1071.06","SPAC16C9.05","SPBC2D10.06","SPCC24B10.08c","SPAC11D3.07c","SPAC3H8.08c","SPAPB8E5.02c","SPCC1223.15c","SPCC594.05c","SPBC428.06c","SPBC1734.06","SPAC25A8.01c","SPAC23H4.02","SPBC19C7.10","SPAC22F3.03c","SPBC2F12.09c","SPAC20G4.01","SPBC21C3.20c","SPBC32F12.08c","SPAC19D5.11c","SPBC1778.10c","SPAC139.03","SPCC1494.10","SPCC126.02c","SPBC1683.13c","SPBC543.03c","SPAC3A11.14c","SPBC1734.15","SPBCPT2R1.08c","SPAC1F12.06c","SPBC3D6.09","SPCC622.19","SPBC1921.07c","SPAC323.03c","SPCC576.12c","SPBC17D11.02c","SPCC417.09c","SPAC227.10","SPAPB24D3.01","SPBC1347.07","SPCC417.07c","SPAC1805.07c","SPBP8B7.28c","SPBC21B10.05c","SPAC1250.03","SPAC3A11.05c","SPCC1739.13","SPBC1685.11","SPBC28F2.03","SPCC737.07c","SPAC144.14","SPAC22H12.02","SPAC19G12.03","SPAC664.03","SPAC15A10.03c","SPBC2D10.13","SPAC56F8.16","SPBC216.05","SPBC685.02","SPAC227.05","SPCC1259.13","SPAC25H1.02","SPCP31B10.06","SPAP8A3.02c","SPBC2D10.11c","SPCC1183.06","SPCC24B10.22","SPBP8B7.27","SPAC12G12.16c","SPCC613.12c","SPAP14E8.02","SPBC1734.05c","SPAC8C9.17c","SPBC354.03","SPCC1442.02","SPAC1071.02","SPBC2D10.16","SPAC1093.06c","SPAC1B3.03c","SPBC11B10.06","SPAC14C4.16","SPAC27D7.13c","SPAC6B12.07c","SPAC12B10.01c","SPCC1322.16","SPBC19C7.09c","SPAC589.10c","SPBC1703.04","SPBC660.11","SPAC29B12.08","SPAC1783.07c","SPBC1861.02","SPCC663.11","SPAC105.03c","SPAC1782.01","SPAC144.05","SPBC1711.03","SPBC19F8.04c","SPBC902.06","SPCC1259.04","SPAC13F5.01c","SPAPB1A10.09","SPAC20H4.07","SPAC26A3.02","SPAC23A1.19c","SPBP4H10.07","SPBC2A9.07c","SPBC577.15c","SPCC338.06c","SPAC890.02c","SPAC1142.08","SPAC22F3.04","SPBP4H10.19c","SPCC1020.11c","SPAC1783.04c","SPBP18G5.03","SPBC16A3.08c","SPBC1652.01","SPAC1805.08","SPAC16C9.06c","SPAC3G9.08","SPAC22F3.09c","SPBC11B10.05c","SPBC336.05c","SPBC2D10.17","SPCC645.08c","SPAC1071.09c","SPBC2F12.12c","SPBC337.08c","SPAC1805.15c","SPAC57A10.14","SPAC139.01c","SPBC21B10.13c","SPAC24B11.10c","SPAC3A12.12","SPBC29A3.14c","SPAC57A10.02","SPAC3C7.14c","SPBC19C2.09","SPAC16A10.05c","SPBC20F10.05","SPCC548.04","SPBC530.14c","SPBC1685.15c","SPAC2F7.06c","SPBC17D11.08","SPAPB17E12.04c","SPBC1718.02","SPAC664.02c","SPCC965.05c","SPAC926.05c","SPAC18G6.10","SPBC530.08","SPAC513.05","SPCC970.01","SPAC16A10.02","SPCC24B10.19c","SPAPB1E7.06c","SPAC688.06c","SPAC10F6.05c","SPAC22F3.11c","SPAC15A10.15","SPBC3E7.09","SPAC4D7.11","SPAC6G9.16c"],"gene_count":490,"ltp_gene_count":0,"approved_date":"2020-12-14"},{"uniquename":"PMID:32997199","title":"Cooperativity of membrane-protein and protein-protein interactions control membrane remodeling by epsin 1 and affects clathrin-mediated endocytosis.","citation":"Cell Mol Life Sci 2021 Mar;78(5):2355-2370","abstract":"Membrane remodeling is a critical process for many membrane trafficking events, including clathrin-mediated endocytosis. Several molecular mechanisms for protein-induced membrane curvature have been described in some detail. Contrary, the effect that the physico-chemical properties of the membrane have on these processes is far less well understood. Here, we show that the membrane binding and curvature-inducing ENTH domain of epsin1 is regulated by phosphatidylserine (PS). ENTH binds to membranes in a PI(4,5)P 2 -dependent manner but only induces curvature in the presence of PS. On PS-containing membranes, the ENTH domain forms rigid homo-oligomers and assembles into clusters. Membrane binding and membrane remodeling can be separated by structure-to-function mutants. Such oligomerization mutants bind to membranes but do not show membrane remodeling activity. In vivo, they are not able to rescue defects in epidermal growth factor receptor (EGFR) endocytosis in epsin knock-down cells. Together, these data show that the membrane lipid composition is important for the regulation of protein-dependent membrane deformation during clathrin-mediated endocytosis.","doi":"10.1007/s00018-020-03647-z","authors":"Kroppen B, Teske N, Yambire KF, Denkert N, Mukherjee I, Tarasenko D, Jaipuria G, Zweckstetter M, Milosevic I, Steinem C, Meinecke M","authors_abbrev":"Kroppen B et al.","pubmed_publication_date":"Mar 2021","pubmed_entrez_date":"2020-09-30","publication_year":"2021","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC162.07"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22139357","title":"H₂O₂ stress-specific regulation of S. pombe MAPK Sty1 by mitochondrial protein phosphatase Ptc4.","citation":"EMBO J 2012 Feb 01;31(3):563-75","abstract":"In fission yeast, the stress-activated MAP kinase, Sty1, is activated via phosphorylation upon exposure to stress and orchestrates an appropriate response. Its activity is attenuated by either serine/threonine PP2C or tyrosine phosphatases. Here, we found that the PP2C phosphatase, Ptc4, plays an important role in inactivating Sty1 specifically upon oxidative stress. Sty1 activity remains high in a ptc4 deletion mutant upon H(2)O(2) but not under other types of stress. Surprisingly, Ptc4 localizes to the mitochondria and is targeted there by an N-terminal mitochondrial targeting sequence (MTS), which is cleaved upon import. A fraction of Sty1 also localizes to the mitochondria suggesting that Ptc4 attenuates the activity of a mitochondrial pool of this MAPK. Cleavage of the Ptc4 MTS is greatly reduced specifically upon H(2)O(2), resulting in the full-length form of the phosphatase; this displays a stronger interaction with Sty1, thus suggesting a novel mechanism by which the negative regulation of MAPK signalling is controlled and providing an explanation for the oxidative stress-specific nature of the regulation of Sty1 by Ptc4.","doi":"10.1038/emboj.2011.438","authors":"Di Y, Holmes EJ, Butt A, Dawson K, Mironov A, Kotiadis VN, Gourlay CW, Jones N, Wilkinson CR","authors_abbrev":"Di Y et al.","pubmed_publication_date":"01 Feb 2012","pubmed_entrez_date":"2011-12-06","publication_year":"2012","canto_session_key":"65d2b7e51ba7ff2f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-27 14:59:03","canto_approved_date":"2026-04-18 22:04:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-30 15:25:38","canto_added_date":"2012-02-24 05:46:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":51,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC12G12.04","SPAC24B11.06c","SPCC4F11.02","SPCC1223.11","SPAC4A8.03c","SPAC26F1.10c","SPAC2G11.07c","SPAC19D5.01","SPMIT.11","SPBC409.07c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2017-09-27"},{"uniquename":"EMBL:AU007631","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30230473","title":"Condensin controls cellular RNA levels through the accurate segregation of chromosomes instead of directly regulating transcription.","citation":"Elife 2018 Sep 19;7","abstract":"Condensins are genome organisers that shape chromosomes and promote their accurate transmission. Several studies have also implicated condensins in gene expression, although any mechanisms have remained enigmatic. Here, we report on the role of condensin in gene expression in fission and budding yeasts. In contrast to previous studies, we provide compelling evidence that condensin plays no direct role in the maintenance of the transcriptome, neither during interphase nor during mitosis. We further show that the changes in gene expression in post-mitotic fission yeast cells that result from condensin inactivation are largely a consequence of chromosome missegregation during anaphase, which notably depletes the RNA-exosome from daughter cells. Crucially, preventing karyotype abnormalities in daughter cells restores a normal transcriptome despite condensin inactivation. Thus, chromosome instability, rather than a direct role of condensin in the transcription process, changes gene expression. This knowledge challenges the concept of gene regulation by canonical condensin complexes.","doi":"10.7554/eLife.38517","authors":"Hocquet C, Robellet X, Modolo L, Sun XM, Burny C, Cuylen-Haering S, Toselli E, Clauder-Münster S, Steinmetz L, Haering CH, Marguerat S, Bernard P","authors_abbrev":"Hocquet C et al.","pubmed_publication_date":"19 Sep 2018","pubmed_entrez_date":"2018-09-20","publication_year":"2018","canto_session_key":"e51b0284bc2e8dc8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-09-21 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36287824","title":"Imp2p forms actin-dependent clusters and imparts stiffness to the contractile ring.","citation":"Mol Biol Cell 2022 Dec 01;33(14):ar145","abstract":"The contractile ring must anchor to the plasma membrane and cell wall to transmit its tension. F-BAR domain containing proteins including Imp2p and Cdc15p in fission yeast are likely candidate anchoring proteins based on their mutant phenotypes. Cdc15p is a node component, links the actin bundle to the plasma membrane, recruits Bgs1p to the division plane, prevents contractile ring sliding, and contributes to the stiffness of the contractile ring. Less is known about Imp2p. We found that similarly to Cdc15p, Imp2p contributes to the stiffness of the contractile ring and assembles into protein clusters. Imp2p clusters contain approximately eight Imp2p dimers and depend on the actin network for their stability at the division plane. Importantly, Imp2p and Cdc15p reciprocally affect the amount of each other in the contractile ring, indicating that the two proteins influence each other during cytokinesis, which may partially explain their similar phenotypes.","doi":"10.1091/mbc.E22-06-0221","authors":"Bellingham-Johnstun K, Commer B, Levesque B, Tyree ZL, Laplante C","authors_abbrev":"Bellingham-Johnstun K et al.","pubmed_publication_date":"01 Dec 2022","pubmed_entrez_date":"2022-10-26","publication_year":"2022","canto_session_key":"a6b360390b9f2e33","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Caroline Laplante","canto_first_approved_date":"2024-11-08 18:07:22","canto_approved_date":"2024-11-08 18:07:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-04 22:36:37","canto_added_date":"2022-10-28 00:15:03","annotation_curators":[{"name":"Caroline Laplante","community_curator":true,"annotation_count":5,"orcid":"0000-0001-8980-0271","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.02","SPAC20G8.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-11-08"},{"uniquename":"PMID:36633091","title":"Microtubule-mitochondrial attachment facilitates cell division symmetry and mitochondrial partitioning in fission yeast.","citation":"J Cell Sci 2023 Jan 01;136(1)","abstract":"Association with microtubules inhibits the fission of mitochondria in Schizosaccharomyces pombe. Here, we show that this attachment of mitochondria to microtubules is an important cell-intrinsic factor in determining cell division symmetry. By comparing mutant cells that exhibited enhanced attachment and no attachment of mitochondria to microtubules (Dnm1Δ and Mmb1Δ, respectively), we show that microtubules in these mutants displayed aberrant dynamics compared to wild-type cells, which resulted in errors in nuclear positioning. This translated to cell division asymmetry in a significant proportion of both Dnm1Δ and Mmb1Δ cells. Asymmetric division in Dnm1Δ and Mmb1Δ cells resulted in unequal distribution of mitochondria, with the daughter cell that received more mitochondria growing faster than the other daughter cell. Taken together, we show the existence of homeostatic feedback controls between mitochondria and microtubules in fission yeast, which directly influence mitochondrial partitioning and, thereby, cell growth. This article has an associated First Person interview with the first author of the paper.","doi":"10.1242/jcs.260705","authors":"Chacko LA, Mikus F, Ariotti N, Dey G, Ananthanarayanan V","authors_abbrev":"Chacko LA et al.","pubmed_publication_date":"01 Jan 2023","pubmed_entrez_date":"2023-01-12","publication_year":"2023","canto_session_key":"6b5237fc76de962d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Leeba Ann Chacko","canto_first_approved_date":"2023-02-06 10:50:37","canto_approved_date":"2023-02-07 08:53:07","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2023-02-02 03:03:47","canto_added_date":"2023-01-13 01:15:05","annotation_curators":[{"name":"Leeba Ann Chacko","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Manuel Lera Ramirez","community_curator":false,"annotation_count":5,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.08","SPAC2F7.03c","SPBC1604.20c","SPBC2F12.13","SPBC25B2.07c","SPBC1685.15c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2023-02-06"},{"uniquename":"PMID:34726351","title":"Leaving histone unturned for epigenetic inheritance.","citation":"FEBS J 2023 Jan;290(2):310-320","abstract":"Post-translational modifications in histones play important roles in regulating chromatin structure and gene expression programs, and the modified histones can be passed on to subsequent generations as an epigenetic memory. The fission yeast has been a great model organism for studying histone modifications in heterochromatin assembly and epigenetic inheritance. Here, we review findings in this organism that cemented the idea of chromatin-based inheritance and highlight recent studies that reveal the role of histone turnover in regulating this process.","doi":"10.1111/febs.16260","authors":"Shan CM, Fang Y, Jia S","authors_abbrev":"Shan CM et al.","pubmed_publication_date":"Jan 2023","pubmed_entrez_date":"2021-11-02","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-11-04 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:30861598","title":"Magnesium enhances dehydration tolerance in Schizosaccharomyces pombe by promoting intracellular 5'-methylthioadenosine accumulation.","citation":"Yeast 2019 Jul;36(7):449-461","abstract":"","doi":"10.1002/yea.3386","authors":"Roca-Domènech G, Poblet M, Rozès N, Cordero-Otero R","authors_abbrev":"Roca-Domènech G et al.","pubmed_publication_date":"Jul 2019","pubmed_entrez_date":"2019-03-13","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-03-14 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2602122","title":"Sequence of the ribosomal protein gene KD4 from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1989 Dec 11;17(23):10118","abstract":"","authors":"Teletski C, Käufer NF","authors_abbrev":"Teletski C et al.","pubmed_publication_date":"11 Dec 1989","pubmed_entrez_date":"1989-12-11","publication_year":"1989","canto_session_key":"9ab33e2720bba395","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2019-01-31 18:05:21","canto_approved_date":"2019-01-31 18:05:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-31 17:37:02","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.13c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2019-01-31"},{"uniquename":"PMID:21127171","title":"The evolution of aerobic fermentation in Schizosaccharomyces pombe was associated with regulatory reprogramming but not nucleosome reorganization.","citation":"Mol Biol Evol 2011 Apr;28(4):1407-13","abstract":"Aerobic fermentation has evolved independently in two yeast lineages, the Saccharomyces cerevisiae and the Schizosaccharomyces pombe lineages. In the S. cerevisiae lineage, the evolution of aerobic fermentation was shown to be associated with transcriptional reprogramming of the genes involved in respiration and was recently suggested to be linked to changes in nucleosome occupancy pattern in the promoter regions of respiration-related genes. In contrast, little is known about the genetic basis for the evolution of aerobic fermentation in the Sch. pombe lineage. In particular, it is not known whether respiration-related genes in Sch. pombe have undergone a transcriptional reprogramming or changes in nucleosome occupancy pattern in their promoter regions. In this study, we compared genome-wide gene expression profiles of Sch. pombe with those of S. cerevisiae and the aerobic respiration yeast Candida albicans. We found that the expression profile of respiration-related genes in Sch. pombe is similar to that of S. cerevisiae, but different from that of C. albicans, suggesting that their transcriptional regulation has been reprogrammed during the evolution of aerobic fermentation. However, we found no significant nucleosome organization change in the promoter of respiration-related gene in Sch. pombe.","doi":"10.1093/molbev/msq324","authors":"Lin Z, Li WH","authors_abbrev":"Lin Z et al.","pubmed_publication_date":"Apr 2011","pubmed_entrez_date":"2010-12-04","publication_year":"2011","canto_session_key":"a1b3ae4254dc7eb7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-10-15 22:03:25","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-10-15 22:03:14","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2015-10-15"},{"uniquename":"PMID:35393344","title":"Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex.","citation":"Genes Dev 2022 Apr 01;36(7-8):408-413","abstract":"Chaperones influence histone conformation and intermolecular interaction in multiprotein complexes, and the structures obtained with full-length histones often provide more accurate and comprehensive views. Here, our structure of the Hat1-Hat2 acetyltransferase complex bound to Asf1-H3-H4 shows that the core domains of H3 and H4 are involved in binding Hat1 and Hat2, and the N-terminal tail of H3 makes extensive interaction with Hat2. These findings expand the knowledge about histone-protein interaction and implicate a function of Hat2/RbAp46/48, which is a versatile histone chaperone found in many chromatin-associated complexes, in the passing of histones between chaperones.","doi":"10.1101/gad.349099.121","authors":"Yue Y, Yang WS, Zhang L, Liu CP, Xu RM","authors_abbrev":"Yue Y et al.","pubmed_publication_date":"01 Apr 2022","pubmed_entrez_date":"2022-04-08","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1482118","title":"Genetics of the fission yeast Schizosaccharomyces pombe.","citation":"Annu Rev Genet 1992;26:373-402","abstract":"","authors":"Hayles J, Nurse P","authors_abbrev":"Hayles J et al.","pubmed_publication_date":"1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27191590","title":"Fission Yeast SCYL1/2 Homologue Ppk32: A Novel Regulator of TOR Signalling That Governs Survival during Brefeldin A Induced Stress to Protein Trafficking.","citation":"PLoS Genet 2016 May;12(5):e1006041","abstract":"Target of Rapamycin (TOR) signalling allows eukaryotic cells to adjust cell growth in response to changes in their nutritional and environmental context. The two distinct TOR complexes (TORC1/2) localise to the cell's internal membrane compartments; the endoplasmic reticulum (ER), Golgi apparatus and lysosomes/vacuoles. Here, we show that Ppk32, a SCYL family pseudo-kinase, is a novel regulator of TOR signalling. The absence of ppk32 expression confers resistance to TOR inhibition. Ppk32 inhibition of TORC1 is critical for cell survival following Brefeldin A (BFA) induced stress. Treatment of wild type cells with either the TORC1 specific inhibitor rapamycin or the general TOR inhibitor Torin1 confirmed that a reduction in TORC1 activity promoted recovery from BFA induced stress. Phosphorylation of Ppk32 on two residues that are conserved within the SCYL pseudo-kinase family are required for this TOR inhibition. Phosphorylation on these sites controls Ppk32 protein levels and sensitivity to BFA. BFA induced ER stress does not account for the response to BFA that we report here, however BFA is also known to induce Golgi stress and impair traffic to lysosomes. In summary, Ppk32 reduce TOR signalling in response to BFA induced stress to support cell survival.","doi":"10.1371/journal.pgen.1006041","authors":"Kowalczyk KM, Petersen J","authors_abbrev":"Kowalczyk KM et al.","pubmed_publication_date":"May 2016","pubmed_entrez_date":"2016-05-19","publication_year":"2016","canto_session_key":"9d9a265db15a87cd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Katarzyna Kowalczyk","canto_first_approved_date":"2018-03-26 13:42:17","canto_approved_date":"2023-04-19 07:21:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-10 17:40:10","canto_added_date":"2016-05-20 00:15:12","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":32,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Katarzyna Kowalczyk","community_curator":true,"annotation_count":18,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.10c","SPAC31G5.12c","SPCC24B10.07","SPBC216.07c","SPBP23A10.10","SPBC839.17c","SPBC1A4.02c","SPAC15A10.13","SPBC12C2.02c","SPAC167.01"],"gene_count":10,"ltp_gene_count":8,"approved_date":"2018-03-26"},{"uniquename":"PMID:7887248","title":"Ferric iron reduction and iron uptake in eucaryotes: studies with the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Adv Exp Med Biol 1994;356:81-9","abstract":"","authors":"Anderson GJ, Dancis A, Roman DG, Klausner RD","authors_abbrev":"Anderson GJ et al.","pubmed_publication_date":"1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17900713","title":"Increase in Fru-2,6-P(2) levels results in altered cell division in Schizosaccharomyces pombe.","citation":"Biochim Biophys Acta 2008 Jan;1783(1):144-52","abstract":"Mitogenic response to growth factors is concomitant with the modulation they exert on the levels of Fructose 2,6-bisphosphate (Fru-2,6-P2), an essential activator of the glycolytic flux. In mammalian cells, decreased Fru-2,6-P2 concentration causes cell cycle delay, whereas high levels of Fru-2,6-P2 sensitize cells to apoptosis. In order to analyze the cell cycle consequences due to changes in Fru-2,6-P2 levels, the bisphosphatase-dead mutant (H258A) of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase enzyme was over-expressed in Schizosaccharomyces pombe cells and the variation in cell phenotype was studied. The results obtained demonstrate that the increase in Fru-2,6-P2 levels results in a defective division of S. pombe, as revealed by an altered multisepted phenotype. The H258A-expressing cells showed impairment of cytokinesis, but normal nuclear division. In order to identify cellular mediators responsible for this effect, we transformed different S. pombe strains and observed that the cytokinetic defect was absent in cells defective for Wee1 kinase function. Therefore, in S. pombe, Wee1 integrates the metabolic signal emerging from changes in Fru-2,6-P2 content, thus coupling metabolism with cell proliferation. As the key regulators of the cell cycle checkpoints are conserved throughout evolution, these results may help to understand the experimental evidences obtained by manipulation of Fru-2,6-P2 levels in mammalian cells.","authors":"Fernández de Mattos S, Alemany V, Aligué R, Tauler A","authors_abbrev":"Fernández de Mattos S et al.","pubmed_publication_date":"Jan 2008","pubmed_entrez_date":"2007-09-29","publication_year":"2008","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPAC144.17c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"EMBL:AF053410","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21712547","title":"Mitotic substrates of the kinase aurora with roles in chromatin regulation identified through quantitative phosphoproteomics of fission yeast.","citation":"Sci Signal 2011 Jun 28;4(179):rs6","abstract":"Kinases of the Aurora family are essential for the proper execution of mitosis in eukaryotes, and Aurora inhibitors are in clinical trials as anticancer drugs. We applied site-specific quantitative phosphoproteomics in conjunction with chemical inhibition of Aurora to identify mitotic Aurora substrates in fission yeast on a proteome-wide scale. We detected 8000 phosphorylation events, of which we assigned almost 6000 to a specific residue; 220 were reduced in cells exposed to the Aurora inhibitor. After controlling for unspecific effects of the inhibitor, we classified 70 sites (on 42 proteins) as probable targets of Aurora, which enabled refinement of the consensus sequence for phosphorylation by Aurora. Several of the substrate candidates were known targets of Aurora, validating the approach, but most represented newly detected Aurora substrates. The involvement of these Aurora substrates in diverse aspects of chromatin dynamics suggests that in addition to its established role in controlling chromosome compaction and attachment to the mitotic spindle, Aurora influences other aspects of chromatin architecture and function during mitosis.","doi":"10.1126/scisignal.2001588","authors":"Koch A, Krug K, Pengelley S, Macek B, Hauf S","authors_abbrev":"Koch A et al.","pubmed_publication_date":"28 Jun 2011","pubmed_entrez_date":"2011-06-30","publication_year":"2011","canto_session_key":"a7ecbdb97e27015e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-04-04 07:58:23","canto_approved_date":"2026-01-29 13:35:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-01 15:09:55","canto_added_date":"2012-02-24 05:46:56","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":93,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Alejandro Carpy","file_curator_role":"community","annotation_file_curators":[{"name":"Alejandro 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and Rad32Mre11 nuclease activity are required for Rec12Spo11 removal, but Rec12Spo11 removal is dispensable for other MRN-dependent meiotic functions.","citation":"Mol Cell Biol 2009 Apr;29(7):1671-81","abstract":"The evolutionarily conserved Mre11/Rad50/Nbs1 (MRN) complex is involved in various aspects of meiosis. Whereas available evidence suggests that the Mre11 nuclease activity might be responsible for Spo11 removal in Saccharomyces cerevisiae, this has not been confirmed experimentally. This study demonstrates for the first time that Mre11 (Schizosaccharomyces pombe Rad32(Mre11)) nuclease activity is required for the removal of Rec12(Spo11). Furthermore, we show that the CtIP homologue Ctp1 is required for Rec12(Spo11) removal, confirming functional conservation between Ctp1(CtIP) and the more distantly related Sae2 protein from Saccharomyces cerevisiae. Finally, we show that the MRN complex is required for meiotic recombination, chromatin remodeling at the ade6-M26 recombination hot spot, and formation of linear elements (which are the equivalent of the synaptonemal complex found in other eukaryotes) but that all of these functions are proficient in a rad50S mutant, which is deficient for Rec12(Spo11) removal. These observations suggest that the conserved role of the MRN complex in these meiotic functions is independent of Rec12(Spo11) removal.","doi":"10.1128/MCB.01182-08","authors":"Hartsuiker E, Mizuno K, Molnar M, Kohli J, Ohta K, Carr AM","authors_abbrev":"Hartsuiker E et al.","pubmed_publication_date":"Apr 2009","pubmed_entrez_date":"2009-01-14","publication_year":"2009","canto_session_key":"6378670e7a31c356","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-02-02 14:32:35","canto_approved_date":"2023-01-06 16:02:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-02 14:32:20","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":43,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13C5.07","SPCC338.08","SPAC1556.01c","SPAC17A5.11"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-02-02"},{"uniquename":"PMID:41919593","title":"Two binding sites are better than one.","citation":"Elife 2026 Apr 01;15","abstract":"The reasons why two multiprotein complexes - VPS34 complex I and VPS34 complex II - are activated by different Rab proteins are becoming clearer.","doi":"10.7554/eLife.110917","authors":"Scott MK, Burke JE","authors_abbrev":"Scott MK et al.","pubmed_publication_date":"01 Apr 2026","pubmed_entrez_date":"2026-04-01","publication_year":"2026","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2026-04-01 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:711673","title":"Relationship between extracellular enzymes and cell growth during the cell cycle of the fission yeast Schizosaccharomyces pombe: acid phosphatase.","citation":"J Bacteriol 1978 Nov;136(2):558-64","abstract":"By using the intact cells of the fission yeast Schizosaccharomyces pombe, the activity of acid phosphatase (EC 3.1.3.2) was compared through the cell cycle with the growth in cell length as a measure of cell growth. The cells of a growing asynchronous culture increased exponentially in number and in total enzyme activity, but remained constant in average length and in specific activity, In a synchronous culture prepared by selection or by induction, the specific activity was periodic in parallel with the increase in average cell length. When hydroxyurea was added to an asynchronous or a synchronous culture by selection, both specific and total activity followed the same continuous pattern as the growth in cell length after the stoppage of cell division. When oversized cells produced by a hydroxyurea pulse treatment to the culture previously syndronized by selection were transferred to a poor medium, they divided synchronously but could hardly grow in the total cell length. In this experimental situation, the total enzyme activity also scarcely increased through three division cycles. These results suggested that the increase in acid phosphatase in dependent on cell elongation.","authors":"Miyata M, Miyata H","authors_abbrev":"Miyata M et al.","pubmed_publication_date":"Nov 1978","pubmed_entrez_date":"1978-11-01","publication_year":"1978","canto_session_key":"ae4836b75fe11b97","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-23 14:16:20","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-23 14:16:03","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-23"},{"uniquename":"PMID:17426123","title":"Stimulation of fission yeast and mouse Hop2-Mnd1 of the Dmc1 and Rad51 recombinases.","citation":"Nucleic Acids Res 2007;35(8):2719-33","abstract":"Genetic analysis of fission yeast suggests a role for the spHop2-Mnd1 proteins in the Rad51 and Dmc1-dependent meiotic recombination pathways. In order to gain biochemical insights into this process, we purified Schizosaccharomyces pombe Hop2-Mnd1 to homogeneity. spHop2 and spMnd1 interact by co-immunoprecipitation and two-hybrid analysis. Electron microscopy reveals that S. pombe Hop2-Mnd1 binds single-strand DNA ends of 3'-tailed DNA. Interestingly, spHop2-Mnd1 promotes the renaturation of complementary single-strand DNA and catalyses strand exchange reactions with short oligonucleotides. Importantly, we show that spHop2-Mnd1 stimulates spDmc1-dependent strand exchange and strand invasion. Ca(2+) alleviate the requirement for the order of addition of the proteins on DNA. We also demonstrate that while spHop2-Mnd1 affects spDmc1 specifically, mHop2 or mHop2-Mnd1 stimulates both the hRad51 and hDmc1 recombinases in strand exchange assays. Thus, our results suggest a crucial role for S. pombe and mouse Hop2-Mnd1 in homologous pairing and strand exchange and reveal evolutionary divergence in their specificity for the Dmc1 and Rad51 recombinases.","authors":"Ploquin M, Petukhova GV, Morneau D, Déry U, Bransi A, Stasiak A, Camerini-Otero RD, Masson JY","authors_abbrev":"Ploquin M et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-04-12","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC222.15","SPAC13A11.03"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:12589433","title":"Mkp1 and Mkp2, two MAPKAP-kinase homologues in Schizosaccharomyces pombe, interact with the MAP kinase Sty1.","citation":"Mol Genet Genomics 2003 Feb;268(5):585-97","abstract":"Mkp1 ( MAPKAP kinase Schizosaccharomyces pombe 1) and Mkp2 are two members from fission yeast of the sub-class of putative MAPK-activated protein kinases in yeasts, the other known members being Rck1 and Rck2 from Saccharomyces cerevisiae. The Mkp1 protein is readily co-immunoprecipitated with Sty1 from S. pombe extracts; Mkp2 shows a weaker interaction with Sty1. In mkp1 mutants, conjugation and meiosis proceed more readily and rapidly than in wild-type cells, in analogy to what was previously found for S. cerevisiae rck1 mutants. Conversely, overexpression of mkp1(+) delays meiosis. Mkp1 is phosphorylated in vivo in a sty1(+)-dependent manner; this modification is removed when cells are starved for nitrogen, a condition that is conducive to entry into stationary phase and meiosis. Overexpression of mkp1(+), like a sty1 mutation, also causes vegetative cells to elongate. The level of Mkp1 phosphorylation drops as cells enter mitosis. We have localised Mkp1 to the cytoplasm, excluded from the nucleus, in vegetative cells. The Mkp1 protein accumulates in zygotic asci and is concentrated within spores. The mkp2(+) gene has no noticeable impact on meiosis. Mkp2 is excluded from the nucleus in vegetative cells, and is concentrated at the septa of dividing cells. Mkp2 does not accumulate in meiotic cells.","authors":"Asp E, Sunnerhagen P","authors_abbrev":"Asp E et al.","pubmed_publication_date":"Feb 2003","pubmed_entrez_date":"2003-02-18","publication_year":"2003","canto_session_key":"c308fd5e60491c28","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-11-28 10:43:14","canto_approved_date":"2020-11-30 16:53:30","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2019-11-26 18:33:17","canto_added_date":"2012-02-24 05:50:57","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23A1.06c","SPAC24B11.06c","SPBC32C12.02","SPCC1322.08"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2019-11-28"},{"uniquename":"PMID:19574738","title":"The G(2) DNA damage checkpoint: could this ancient regulator be the Achilles heel of cancer?","citation":"Cancer Biol Ther 2009 Aug;8(15):1433-9","abstract":"The maintenance of genomic integrity is important in normal cell growth and organism development, as well as in the prevention of cancer. Cell cycle checkpoints allow the cell time to complete replication and repair DNA damage before it can pass to the next cell cycle stage. These checkpoints ensure faithful segregation of one undamaged copy of the genome to each daughter cell. In humans, a DNA damage-based checkpoint signal in G(1) is propagated through activation of the tumor suppressor p53, which is mutated in many cancers. Chk1, a serine/threonine kinase, controls checkpoint responses in G(2). Chk1 is activated by the concerted action of many upstream proteins and prevents a cell from entering mitosis with damaged or incompletely replicated DNA. This checkpoint is conserved from the fission yeast, Schizosaccharomyces pombe through to humans. However, unlike p53, G(2) checkpoint genes are rarely if ever mutated in cancer cells. This suggests that these genes are essential for tumor cell viability and may represent valid anti-cancer drug targets. This review will describe the current understanding of the G(2) checkpoint including how the human biology has been informed by studies in fission yeast. It will also discuss the present status and future of potential cancer therapies aimed at inactivating this signaling pathway in tumor cells.","authors":"Kuntz K, O'Connell MJ","authors_abbrev":"Kuntz K et al.","pubmed_publication_date":"Aug 2009","pubmed_entrez_date":"2009-07-04","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22419817","title":"The fission yeast septation initiation network (SIN) kinase, Sid2, is required for SIN asymmetry and regulates the SIN scaffold, Cdc11.","citation":"Mol Biol Cell 2012 May;23(9):1636-45","abstract":"The Schizosaccharomyces pombe septation initiation network (SIN) is an Spg1-GTPase-mediated protein kinase cascade that triggers actomyosin ring constriction, septation, and cell division. The SIN is assembled at the spindle pole body (SPB) on the scaffold proteins Cdc11 and Sid4, with Cdc11 binding directly to SIN signaling components. Proficient SIN activity requires the asymmetric distribution of its signaling components to one of the two SPBs during anaphase, and Cdc11 hyperphosphorylation correlates with proficient SIN activity. In this paper, we show that the last protein kinase in the signaling cascade, Sid2, feeds back to phosphorylate Cdc11 during mitosis. The characterization of Cdc11 phosphomutants provides evidence that Sid2-mediated Cdc11 phosphorylation promotes the association of the SIN kinase, Cdc7, with the SPB and maximum SIN signaling during anaphase. We also show that Sid2 is crucial for the establishment of SIN asymmetry, indicating a positive-feedback loop is an important element of the SIN.","doi":"10.1091/mbc.E11-09-0792","authors":"Feoktistova A, Morrell-Falvey J, Chen JS, Singh NS, Balasubramanian MK, Gould KL","authors_abbrev":"Feoktistova A et al.","pubmed_publication_date":"May 2012","pubmed_entrez_date":"2012-03-16","publication_year":"2012","canto_session_key":"65edebcc485f98a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kathy Gould","canto_first_approved_date":"2017-10-23 14:13:35","canto_approved_date":"2021-08-02 10:26:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-22 17:37:11","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[{"name":"Kathy Gould","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":9,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPBC21.06c","SPBC428.13c","SPBC244.01c","SPAC8E11.02c","SPAC6F6.08c","SPCC1739.11c","SPAC9G1.09"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2017-10-23"},{"uniquename":"Pfam:PF06657","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:30794","HGNC:21561","SPAC4H3.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPD195","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24763107","title":"Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (Fission Yeast).","citation":"Mol Cell Proteomics 2014 Aug;13(8):1925-36","abstract":"To quantify cell cycle-dependent fluctuations on a proteome-wide scale, we performed integrative analysis of the proteome and phosphoproteome during the four major phases of the cell cycle in Schizosaccharomyces pombe. In highly synchronized cells, we identified 3753 proteins and 3682 phosphorylation events and relatively quantified 65% of the data across all phases. Quantitative changes during the cell cycle were infrequent and weak in the proteome but prominent in the phosphoproteome. Protein phosphorylation peaked in mitosis, where the median phosphorylation site occupancy was 44%, about 2-fold higher than in other phases. We measured copy numbers of 3178 proteins, which together with phosphorylation site stoichiometry enabled us to estimate the absolute amount of protein-bound phosphate, as well as its change across the cell cycle. Our results indicate that 23% of the average intracellular ATP is utilized by protein kinases to phosphorylate their substrates to drive regulatory processes during cell division. Accordingly, we observe that phosphate transporters and phosphate-metabolizing enzymes are phosphorylated and therefore likely to be regulated in mitosis.","doi":"10.1074/mcp.M113.035824","authors":"Carpy A, Krug K, Graf S, Koch A, Popic S, Hauf S, Macek B","authors_abbrev":"Carpy A et al.","pubmed_publication_date":"Aug 2014","pubmed_entrez_date":"2014-04-26","publication_year":"2014","canto_session_key":"f248129e68667867","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-03-30 16:41:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-02-23 19:09:43","canto_added_date":"2014-04-27 21:33:14","annotation_curators":[],"file_curator_name":"Alejandro Carpy","file_curator_role":"community","annotation_file_curators":[{"name":"Alejandro 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competition between capping protein and formin Cdc12p during cytokinesis in fission yeast.","citation":"Mol Biol Cell 2005 May;16(5):2313-24","abstract":"Fission yeast capping protein SpCP is a heterodimer of two subunits (Acp1p and Acp2p) that binds actin filament barbed ends. Neither acp1 nor acp2 is required for viability, but cells lacking either or both subunits have cytokinesis defects under stressful conditions, including elevated temperature, osmotic stress, or in combination with numerous mild mutations in genes important for cytokinesis. Defects arise as the contractile ring constricts and disassembles, resulting in delays in cell separation. Genetic and biochemical interactions show that the cytokinesis formin Cdc12p competes with capping protein for actin filament barbed ends in cells. Deletion of acp2 partly suppresses cytokinesis defects in temperature-sensitive cdc12-112 cells and mild overexpression of capping protein kills cdc12-112 cells. Biochemically, profilin has opposite effects on filaments capped with Cdc12p and capping protein. Profilin depolymerizes actin filaments capped by capping protein but allows filaments capped by Cdc12p to grow at their barbed ends. Once associated with a barbed end, either Cdc12p or capping protein prevents the other from influencing polymerization at that end. Given that capping protein arrives at the division site 20 min later than Cdc12p, capping protein may slowly replace Cdc12p on filament barbed ends in preparation for filament disassembly during ring constriction.","authors":"Kovar DR, Wu JQ, Pollard TD","authors_abbrev":"Kovar DR et al.","pubmed_publication_date":"May 2005","pubmed_entrez_date":"2005-03-04","publication_year":"2005","canto_session_key":"de3fe3d88f14e4a8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-09-28 15:39:00","canto_approved_date":"2026-06-17 12:53:05","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-09-14 16:11:23","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":174,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.06","SPAC27F1.02c","SPAC1F5.04c","SPBC32H8.12c","SPCC4B3.15","SPBC21.06c","SPCC645.05c","SPAC630.03","SPCC895.05","SPAP8A3.08","SPAC4A8.05c","SPAC12B10.07","SPAC4A8.15c","SPAC15A10.08","SPAC4F8.13c","SPAC20G8.05c","SPAC631.01c","SPAC926.03","SPBC26H8.07c","SPBC1778.06c"],"gene_count":20,"ltp_gene_count":20,"approved_date":"2017-09-28"},{"uniquename":"PMID:8387358","title":"Interaction of the pim1/spi1 mitotic checkpoint with a protein phosphatase.","citation":"Mol Biol Cell 1993 Mar;4(3):337-45","abstract":"Loss of p58pim1, a homolog of human RCC1, results in uncoupling of mitosis from the completion of DNA replication in fission yeast. An extragenic suppressor of a mutant allele of pim1, esp1, has been isolated and characterized. esp1 encodes a predicted product of 305 amino acid residues, which shares 71% identity with budding yeast SIT4, a type2A related protein phosphatase. p58pim1 binds p25spi1, a 25-kd ras-related GTPase previously isolated as a high dosage suppressor of pim1. The complex dissociates in the presence of guanine nucleotides and Mg2+. The mutant p58pim1 is defective in its ability to bind p25spi1, suggesting that the physical interaction is essential for the maintenance of the interdependency of cell cycle event. In the esp1 pim1 double mutant, the mutant p58pim1 protein is still defective in its ability to bind to p25spi1. However, pmi1 induced premature mitosis is completely suppressed, suggesting that esp1 may act downstream of the p58pim1/p25spi1 physical interaction but upstream of the activation of the M-phase specific histone H1 kinase.","authors":"Matsumoto T, Beach D","authors_abbrev":"Matsumoto T et al.","pubmed_publication_date":"Mar 1993","pubmed_entrez_date":"1993-03-01","publication_year":"1993","canto_session_key":"403333495bb6ddb2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-07-28 16:40:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-28 16:40:48","canto_added_date":"2012-02-24 05:55:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":8,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1739.12","SPBC557.03c","SPBC1289.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-07-28"},{"uniquename":"PMID:20829365","title":"Pma1, a P-type proton ATPase, is a determinant of chronological life span in fission yeast.","citation":"J Biol Chem 2010 Nov 05;285(45):34616-20","abstract":"Chronological life span is defined by how long a cell can survive in a non-dividing state. In yeast, it is measured by viability after entry into stationary phase. To date, some factors affecting chronological life span have been identified; however, the molecular details of how these factors regulate chronological life span have not yet been elucidated clearly. Because life span is a complicated phenomenon and is supposedly regulated by many factors, it is necessary to identify new factors affecting chronological life span to understand life span regulation. To this end, we have screened for long-lived mutants and identified Pma1, an essential P-type proton ATPase, as one of the determinants of chronological life span. We show that partial loss of Pma1 activity not only by mutations but also by treatment with the Pma1 inhibitory chemical vanadate resulted in the long-lived phenotype in Schizosaccharomyces pombe. These findings suggest a novel way to manipulate chronological life span by modulating Pma1 as a molecular target.","doi":"10.1074/jbc.M110.175562","authors":"Ito H, Oshiro T, Fujita Y, Kubota S, Naito C, Ohtsuka H, Murakami H, Aiba H","authors_abbrev":"Ito H et al.","pubmed_publication_date":"05 Nov 2010","pubmed_entrez_date":"2010-09-11","publication_year":"2010","canto_session_key":"0fd8899c3eff64d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_first_approved_date":"2019-10-15 23:58:16","canto_approved_date":"2020-03-15 15:11:11","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-09-29 06:38:12","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":2,"orcid":"0000-0002-7775-0446","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.10c","SPCC757.07c"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2019-10-15"},{"uniquename":"PMID:38524400","title":"Evaluation of the probiotic potential of yeast isolated from kombucha in New Zealand.","citation":"Curr Res Food Sci 2024;8:100711","abstract":"The current study investigated the  in vitro  probiotic potential of yeast isolated from kombucha, a tea beverage fermented with a symbiotic culture of acetic acid bacteria and yeast. A total of 62 yeast strains were previously isolated from four different commercial kombucha samples sold in New Zealand. Fifteen representative isolates belonging to eight different species were evaluated for their growth under different conditions (temperature, low pH, concentrations of bile salts, and NaCl). Cell surface characteristics, functional and enzymatic activities of the selected strains were also studied in triplicate experiments. Results showed that six strains ( Dekkera bruxellensis  LBY1,  Sachizosaccharomyces pombe  LBY5,  Hanseniaspora valbyensis  DOY1,  Brettanomyces anomalus  DOY8,  Pichia kudraivzevii  GBY1, and  Saccharomyces cerevisiae  GBY2) were able to grow under low-acid conditions (at pH 2 and pH 3) and in the presence of bile salts. This suggests their potential to survive passage through the human gut. All 15 strains exhibited negative enzymatic activity reactions (haemolytic, gelatinase, phospholipase, and protease activities), and thus, they can be considered safe to consume. Notably, two of the fifteen strains ( Pichia kudraivzevii  GBY1 and  Saccharomyces cerevisiae  GBY2) exhibited desirable cell surface hydrophobicity (64.60-83.87%), auto-aggregation (>98%), co-aggregation, resistance to eight tested antibiotics (ampicillin, chloramphenicol, colistin sulphate, kanamycin, nalidixic acid, nitrofurantoin, streptomycin, and tetracycline), and high levels of antioxidant activities (>90%). Together, our data reveal the probiotic activities of two yeast strains GBY1 and GBY2 and their potential application in functional food production.","doi":"10.1016/j.crfs.2024.100711","authors":"Wang B, Rutherfurd-Markwick K, Liu N, Zhang XX, Mutukumira AN","authors_abbrev":"Wang B et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-03-25","publication_year":"2024","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2024-03-26 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3058333","title":"Multiple phosphorylated forms of the product of the fission yeast cell division cycle gene cdc2+.","citation":"Curr Genet 1988 Sep;14(3):235-40","abstract":"The 34 kilodalton protein product (p34) of the cdc2+ cell cycle control gene of Schizosaccharomyces pombe was expressed in bacteria. Monoclonal antibodies raised against this protein are capable of immunoprecipitating p34cdc2 from yeast lysates. Immunoprecipitates of [35S]methionine- and [32P]orthophosphate-labeled p34cdc2 were analyzed by two-dimensional gel electrophoresis. The cdc2+ gene product is homogeneous in size but resolves into seven species of differing charge. At least four of these species are phosphorylated. Phosphoamino acid analysis reveals that phosphorylation occurs mainly on threonine residues. The pattern of p34 phosphorylation is unaltered at the nonpermissive temperature in strains carrying temperature sensitive alleles of weel-50 and ran1-114 or in a strain overproducing the ran1+ gene product.","authors":"Potashkin JA, Beach DH","authors_abbrev":"Potashkin JA et al.","pubmed_publication_date":"Sep 1988","pubmed_entrez_date":"1988-09-01","publication_year":"1988","canto_session_key":"1249fce88c3284d4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-17 14:47:01","canto_approved_date":"2023-12-07 17:45:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-25 18:24:41","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C2.05","SPCC18B5.03","SPBC11B10.09"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-11-17"},{"uniquename":"PMID:15727839","title":"Effects of exogenous ubiquitin on cell division cycle mutants of Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 2005 Mar 01;244(1):187-91","abstract":"Many important cellular processes like cell cycle are regulated by selective degradation of short-lived cellular proteins via the ubiquitin-proteasome pathway. Deregulation in degradation of any of these controlling molecules can lead to abnormalities like malignancies, neurodegenerative disorders, etc. Research on effects of exogenously added Ubiquitin (Ub) on cell cycle has been lacking. This report describes the effects of exogenously added Ub on the growth of Schizosaccharomyces pombe cells. Addition of Ub was found to cause inhibition in growth of cells. In temperature sensitive cell division cycle mutant, which exhibits arrest at the G2 phase, the exogenously added Ub affected the cell-cycle arrest. Addition of Lactacystin, an inhibitor of the proteasome degradation pathway, abolished the effects of externally added Ub. A proposal has been made on the mechanism through which externally added Ub may exert its effects on cells.","authors":"Kutty BC, Pasupathy K, Mishra KP","authors_abbrev":"Kutty BC et al.","pubmed_publication_date":"01 Mar 2005","pubmed_entrez_date":"2005-02-25","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22608966","title":"Functional implications from the Cid1 poly(U) polymerase crystal structure.","citation":"Structure 2012 Jun 06;20(6):977-86","abstract":"In eukaryotes, mRNA degradation begins with poly(A) tail removal, followed by decapping, and the mRNA body is degraded by exonucleases. In recent years, the major influence of 3'-end uridylation as a regulatory step within several RNA degradation pathways has generated significant attention toward the responsible enzymes, which are called poly(U) polymerases (PUPs). We determined the atomic structure of the Cid1 protein, the founding member of the PUP family, in its UTP-bound form, allowing unambiguous positioning of the UTP molecule. Our data also suggest that the RNA substrate accommodation and product translocation by the Cid1 protein rely on local and global movements of the enzyme. Supplemented by point mutations, the atomic model is used to propose a catalytic cycle. Our study underlines the Cid1 RNA binding properties, a feature with critical implications for miRNAs, histone mRNAs, and, more generally, cellular RNA degradation.","doi":"10.1016/j.str.2012.04.006","authors":"Munoz-Tello P, Gabus C, Thore S","authors_abbrev":"Munoz-Tello P et al.","pubmed_publication_date":"06 Jun 2012","pubmed_entrez_date":"2012-05-22","publication_year":"2012","canto_session_key":"824e349310ec0ddd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-02-16 07:21:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-15 07:57:06","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-02-15","pdb_entries":[{"pdb_id":"4ep7","gene_chains":[{"gene_uniquename":"SPAC19D5.03","chain":"A/B","position":"40-377"}],"title":"Functional implications from the Cid1 poly(U) polymerase crystal structure","entry_authors":"Munoz-Tello P,Gabus C,Thore S","entry_authors_abbrev":"Munoz-Tello P et al.","reference_uniquename":"PMID:22608966","experimental_method":"X-ray","resolution":"2.2805"}]},{"uniquename":"PMID:22696680","title":"Fission yeast Alp14 is a dose-dependent plus end-tracking microtubule polymerase.","citation":"Mol Biol Cell 2012 Aug;23(15):2878-90","abstract":"XMAP215/Dis1 proteins are conserved tubulin-binding TOG-domain proteins that regulate microtubule (MT) plus-end dynamics. Here we show that Alp14, a XMAP215 orthologue in fission yeast, Schizosaccharomyces pombe, has properties of a MT polymerase. In vivo, Alp14 localizes to growing MT plus ends in a manner independent of Mal3 (EB1). alp14-null mutants display short interphase MTs with twofold slower assembly rate and frequent pauses. Alp14 is a homodimer that binds a single tubulin dimer. In vitro, purified Alp14 molecules track growing MT plus ends and accelerate MT assembly threefold. TOG-domain mutants demonstrate that tubulin binding is critical for function and plus end localization. Overexpression of Alp14 or only its TOG domains causes complete MT loss in vivo, and high Alp14 concentration inhibits MT assembly in vitro. These inhibitory effects may arise from Alp14 sequestration of tubulin and effects on the MT. Our studies suggest that Alp14 regulates the polymerization state of tubulin by cycling between a tubulin dimer-bound cytoplasmic state and a MT polymerase state that promotes rapid MT assembly.","doi":"10.1091/mbc.E12-03-0205","authors":"Al-Bassam J, Kim H, Flor-Parra I, Lal N, Velji H, Chang F","authors_abbrev":"Al-Bassam J et al.","pubmed_publication_date":"Aug 2012","pubmed_entrez_date":"2012-06-15","publication_year":"2012","canto_session_key":"69d5c50d65bdb7fe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-06-15 08:26:31","canto_approved_date":"2025-09-04 06:31:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-05 16:35:07","canto_added_date":"2012-11-19 00:16:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPCC1223.06","SPAC3C7.12","SPAC18G6.15","SPBC1604.20c","SPCC895.07","SPBC16A3.15c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2017-06-15"},{"uniquename":"EMBL:AU007206","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU009291","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9070271","title":"PCNA and DNA polymerase delta catalytic subunit from Schizosaccharomyces pombe do not interact directly.","citation":"Biochem Biophys Res Commun 1997 Feb 13;231(2):321-8","abstract":"DNA polymerase delta (pol delta) is constituted of at least two subunits: the catalytic subunit of about 125 kDa (p125), and a subunit of approximately 50 kDa (p50) of unknown function. Processivity of pol delta is dependent on its auxiliary protein PCNA (proliferating cell nuclear antigen). Contradictory data were reported regarding a direct interaction between p125 and PCNA. We investigated this matter further using the baculovirus system to overexpress p125 and PCNA from S. pombe. We show that the recombinant p125 is active for basal DNA polymerase activity and for 3'-->5' exonuclease activity but is not stimulated by PCNA. Interaction between p125 and PCNA was tested by: (i) co-immunoprecipitation assay using antibodies specific for one or other polypeptides after co-expression in insect cells, and (ii) a two-hybrid assay. In both cases, no direct interaction between the two proteins was detected. Taken together, our data show that p125 and PCNA do not interact directly.","authors":"Tratner I, Piard K, Grenon M, Perderiset M, Baldacci G","authors_abbrev":"Tratner I et al.","pubmed_publication_date":"13 Feb 1997","pubmed_entrez_date":"1997-02-13","publication_year":"1997","canto_session_key":"38ba4d994780e497","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-17 16:54:36","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-03-17 16:54:03","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.04","SPBC16D10.09"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2015-03-17"},{"uniquename":"PMID:12789340","title":"Fission yeast mod5p regulates polarized growth through anchoring of tea1p at cell tips.","citation":"Nature 2003 Jun 05;423(6940):647-51","abstract":"Microtubules have a central role in eukaryotic cell polarity, in part through interactions between microtubule end-binding proteins and the cell cortex. In the fission yeast Schizosaccharomyces pombe, microtubules and the polarity modulator tea1p maintain cylindrical cell shape and strictly antipodal cell growth. The tea1p protein is transported to cell tips by association with growing microtubule plus ends; once at cell tips, tea1p releases from microtubule ends and associates with the cell cortex, where it coordinates polarized growth. Here we describe a cortical protein, mod5p, that regulates the dynamic behaviour of tea1p. In mod5Delta cells, tea1p is efficiently transported on microtubules to cell tips but fails to anchor properly at the cortex and thus fails to accumulate to normal levels. mod5p contains a signal for carboxy-terminal prenylation and in wild-type cells is associated with the plasma membrane at cell tips. However, in tea1Delta cells, although mod5p remains localized to the plasma membrane, mod5p is no longer restricted to the cell tips. We propose that tea1p and mod5p act in a positive-feedback loop in the microtubule-mediated regulation of cell polarity.","authors":"Snaith HA, Sawin KE","authors_abbrev":"Snaith HA et al.","pubmed_publication_date":"05 Jun 2003","pubmed_entrez_date":"2003-06-06","publication_year":"2003","canto_session_key":"f7e3367c6996a6f9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2020-08-20 17:14:41","canto_approved_date":"2025-11-27 22:55:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-08-20 17:14:32","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":19,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"legacy_modifications_from_contigs.tsv"}],"genes":["SPCC1223.06","SPAC3C7.12","SPAC6G10.02c","SPBC1604.20c","SPAC15A10.16","SPAC2F7.03c","SPBC530.04"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2020-08-20"},{"uniquename":"PMID:32144435","title":"ERH proteins: connecting RNA processing to tumorigenesis?","citation":"Curr Genet 2020 Aug;66(4):689-692","abstract":"With the development of -omics approaches, the scientific community is now submerged by a wealth of information that can be used to analyze various parameters: the degree of protein sequence conservation, protein 3D structures as well as RNA and protein expression levels in various benign and tumor tissues, during organism development or upon exposure to chemicals such as endocrine disrupters. However, if such information can be used to identify genes with potentially important biological function, additional studies are needed to deeply characterize their cellular function in model organisms. Here, we discuss the case of such a gene: ERH, encoding a highly conserved homodimeric protein found in unicellular eukaryotes, plants and metazoan, of yet unknown biological function, which might be linked to mRNA metabolism and that is emerging as important for cell migration and metastasis.","doi":"10.1007/s00294-020-01065-z","authors":"Graille M, Rougemaille M","authors_abbrev":"Graille M et al.","pubmed_publication_date":"Aug 2020","pubmed_entrez_date":"2020-03-08","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-03-13 01:15:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32415081","title":"Ribonucleotide incorporation in yeast genomic DNA shows preference for cytosine and guanosine preceded by deoxyadenosine.","citation":"Nat Commun 2020 May 15;11(1):2447","abstract":"Despite the abundance of ribonucleoside monophosphates (rNMPs) in DNA, sites of rNMP incorporation remain poorly characterized. Here, by using ribose-seq and Ribose-Map techniques, we built and analyzed high-throughput sequencing libraries of rNMPs derived from mitochondrial and nuclear DNA of budding and fission yeast. We reveal both common and unique features of rNMP sites among yeast species and strains, and between wild type and different ribonuclease H-mutant genotypes. We demonstrate that the rNMPs are not randomly incorporated in DNA. We highlight signatures and patterns of rNMPs, including sites within trinucleotide-repeat tracts. Our results uncover that the deoxyribonucleotide immediately upstream of the rNMPs has a strong influence on rNMP distribution, suggesting a mechanism of rNMP accommodation by DNA polymerases as a driving force of rNMP incorporation. Consistently, we find deoxyadenosine upstream from the most abundant genomic rCMPs and rGMPs. This study establishes a framework to better understand mechanisms of rNMP incorporation in DNA.","doi":"10.1038/s41467-020-16152-5","authors":"Balachander S, Gombolay AL, Yang T, Xu P, Newnam G, Keskin H, El-Sayed WMM, Bryksin AV, Tao S, Bowen NE, Schinazi RF, Kim B, Koh KD, Vannberg FO, Storici F","authors_abbrev":"Balachander S et al.","pubmed_publication_date":"15 May 2020","pubmed_entrez_date":"2020-05-17","publication_year":"2020","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2020-05-18 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23171760","title":"Mediator regulates non-coding RNA transcription at fission yeast centromeres.","citation":"Epigenetics Chromatin 2012 Nov 21;5(1):19","abstract":"In fission yeast, centromeric heterochromatin is necessary for the fidelity of chromosome segregation. Propagation of heterochromatin in dividing cells requires RNA interference (RNAi) and transcription of centromeric repeats by RNA polymerase II during the S phase of the cell cycle.\nWe found that the Med8-Med18-Med20 submodule of the Mediator complex is required for the transcriptional regulation of native centromeric dh and dg repeats and for the silencing of reporter genes inserted in centromeric heterochromatin. Mutations in the Med8-Med18-Med20 submodule did not alter Mediator occupancy at centromeres; however, they led to an increased recruitment of RNA polymerase II to centromeres and reduced levels of centromeric H3K9 methylation accounting for the centromeric desilencing. Further, we observed that Med18 and Med20 were required for efficient processing of dh transcripts into siRNA. Consistent with defects in centromeric heterochromatin, cells lacking Med18 or Med20 displayed elevated rates of mitotic chromosome loss.\nOur data demonstrate a role for the Med8-Med18-Med20 Mediator submodule in the regulation of non-coding RNA transcription at Schizosaccharomyces pombe centromeres. In wild-type cells this submodule limits RNA polymerase II access to the heterochromatic DNA of the centromeres. Additionally, the submodule may act as an assembly platform for the RNAi machinery or regulate the activity of the RNAi pathway. Consequently, Med8-Med18-Med20 is required for silencing of centromeres and proper mitotic chromosome segregation.","doi":"10.1186/1756-8935-5-19","authors":"Thorsen M, Hansen H, Venturi M, Holmberg S, Thon G","authors_abbrev":"Thorsen M et al.","pubmed_publication_date":"21 Nov 2012","pubmed_entrez_date":"2012-11-23","publication_year":"2012","canto_session_key":"c42bc80dfc05303f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41154583","title":"Mitochondrial Translation Inhibition Triggers an Rst2-Controlled Transcriptional Reprogramming of Carbon Metabolism in Stationary-Phase Cells of Fission Yeast.","citation":"Biomolecules 2025 Sep 24;15(10)","abstract":"Mitochondria possess their own genome, which encodes subunits of the electron transport chain, rendering mitochondrial protein translation essential for cellular energy metabolism. Mitochondrial dysfunction affects nuclear transcription through the retrograde response. We applied RNA-seq to investigate whether and how the inhibition of mitochondrial translation by chloramphenicol (CAP) affects transcriptome regulation in proliferating or stationary-phase cells of  Schizosaccharomyces pombe  growing in fermentative or respiratory media. Stationary-phase cells in glucose medium exhibited the strongest transcriptome response to CAP, characterized by expression signatures similar to those observed under other stresses, including the retrograde response. The induced genes were also significantly enriched in cytoplasmic carbon metabolism pathways, reflecting a transcriptional reprogramming from respiration to fermentation. The transcription factors Scr1 and Rst2, regulators of carbon catabolite repression (CCR), controlled a common set of carbon metabolism genes in CAP-treated stationary-phase cells, and they showed opposing effects on the lifespan of these cells. Rst2 was required for the induction of carbon metabolism genes and maintained nuclear localization in CAP-treated stationary-phase cells. A systematic genetic interaction screen revealed functional relationships of Rst2 with processes related to stress and starvation responses. These findings uncover a complex transcriptional program in stationary-phase cells that adapt to inhibited mitochondrial translation, including stress- and retrograde-like responses, contributions of the CCR factors Scr1 and Rst2, and adjustment of carbon metabolism to deal with mitochondrial dysfunction.","doi":"10.3390/biom15101354","authors":"Luo Y, Hassan S, Raut S, Bähler J","authors_abbrev":"Luo Y et al.","pubmed_publication_date":"24 Sep 2025","pubmed_entrez_date":"2025-10-29","publication_year":"2025","canto_session_key":"5a55f0cdf55a92f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying  Luo","canto_first_approved_date":"2026-03-17 07:58:14","canto_approved_date":"2026-04-13 17:32:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2026-03-11 10:08:07","canto_added_date":"2025-10-30 00:25:06","annotation_curators":[{"name":"Ying  Luo","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1D7.02c","SPAC6F12.02"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2026-03-17"},{"uniquename":"PMID:22610605","title":"Cadmium-induced proteome remodeling regulated by Spc1/Sty1 and Zip1 in fission yeast.","citation":"Toxicol Sci 2012 Sep;129(1):200-12","abstract":"Stress-activated protein kinases and transcription factors are crucial for surviving exposure to cadmium and other environmental toxicants, but their effects on the proteome remain largely unexplored. In this study, isobaric tag for relative and absolute quantitation reveals that cadmium stress triggers rapid proteome remodeling in the fission yeast Schizosaccharomyces pombe. Spc1/Sty1, a mitogen/stress-activated protein kinase homologous to human p38 and Saccharomyces cerevisiae Hog1, controls many of these changes, including enzymes of the oxidative phase of the pentose phosphate pathway and trehalose metabolism. Genetic studies indicate that control of carbohydrate metabolism by Spc1 is required for cadmium tolerance. The bZIP transcription factor Zip1, which is functionally related to human Nrf2 and S. cerevisiae Met4, has a smaller effect on cadmium-induced proteome remodeling, but it is required for production of key proteins involved in sulfur metabolism, which are essential for cadmium resistance. These studies reveal how Spc1 and Zip1 independently reshape the proteome to modulate cellular defense mechanisms against the toxic effects of cadmium.","doi":"10.1093/toxsci/kfs179","authors":"Guo L, Ghassemian M, Komives EA, Russell P","authors_abbrev":"Guo L et al.","pubmed_publication_date":"Sep 2012","pubmed_entrez_date":"2012-05-22","publication_year":"2012","canto_session_key":"c7bc12d254d2c07e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9298283","title":"The ultradian clocks of eukaryotic microbes: timekeeping devices displaying a homeostasis of the period.","citation":"Chronobiol Int 1997 Sep;14(5):469-79","abstract":"Temperature compensation of their period is one of the canonical characteristics of circadian rhythms, yet it is not restricted to circadian rhythms. This short review summarizes the evidence for ultradian rhythms, with periods from 1 minute to several hours, that likewise display a strict temperature compensation. They have been observed mostly in unicellular organisms in which their constancy of period at different temperatures, as well as under different growth conditions (e.g., medium type, carbon source), indicates a general homeostasis of the period. Up to eight different parameters, including cell division, cell motility, and energy metabolism, were observed to oscillate with the same periodicity and therefore appear to be under the control of the same central pacemaker. This suggests that these ultradian clocks should be considered as cellular timekeeping devices that in fast-growing cells take over temporal control of cellular functions controlled by the circadian clock in slow-growing or nongrowing cells. Being potential relatives of circadian clocks, these ultradian rhythms may serve as model systems in chronobiological research. Indeed, mutations have been found that affect both circadian and ultradian periods, indicating that the respective oscillators share some mechanistic features. In the haploid yeast Schizosaccharomyces pombe, a number of genes have been identified where mutation, deletion, or overexpression affect the ultradian clock. Since most of these genes play roles in cellular metabolism and signaling, and mutations have pleiotropic effects, it has to be assumed that the clock is deeply embedded in cellular physiology. It is therefore suggested that mechanisms ensuring temperature compensation and general homeostasis of period are to be sought in a wider context.","authors":"Kippert F","authors_abbrev":"Kippert F","pubmed_publication_date":"Sep 1997","pubmed_entrez_date":"1997-09-23","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20870879","title":"Reorganization of the growth pattern of Schizosaccharomyces pombe in invasive filament formation.","citation":"Eukaryot Cell 2010 Nov;9(11):1788-97","abstract":"The organization and control of polarized growth through the cell cycle of Schizosaccharomyces pombe, a single-celled eukaryote, have been studied extensively. We have investigated the changes in these processes when S. pombe differentiates to form multicellular invasive mycelia and have found striking alterations to the behavior of some of the key regulatory proteins. Cells at the tips of invading filaments are considerably more elongated than cells growing singly and grow at one pole only. The filament tip follows a strict direction of growth through multiple cell cycles. A group of proteins involved in the growth process and actin regulation, comprising Spo20, Bgs4, activated Cdc42, and Crn1, are all concentrated at the growing tip, unlike their distribution at both ends of single cells. In contrast, several proteins implicated in microtubule-dependent organization of growth, including Tea1, Tea4, Mod5, and Pom1, all show the opposite effect and are relatively depleted at the growing end and enriched at the nongrowing end, although Tea1 appears to continue to be delivered to both ends. A third group acting at different stages of the cell cycle, including Bud6, Rga4, and Mid1, localize similarly in filaments and single cells, while Nif1 shows a reciprocal localization to Pom1.","doi":"10.1128/EC.00084-10","authors":"Dodgson J, Brown W, Rosa CA, Armstrong J","authors_abbrev":"Dodgson J et al.","pubmed_publication_date":"Nov 2010","pubmed_entrez_date":"2010-09-28","publication_year":"2010","canto_session_key":"184eec9f7bdbd8f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2012-05-03 13:22:46","canto_approved_date":"2020-01-21 18:40:15","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-05-03 12:29:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1223.06","SPAC2F7.03c","SPCC4B3.15","SPBC1706.01","SPAC3H8.10","SPAC15A10.16","SPBC23G7.04c","SPAC110.03","SPAC23C4.02","SPBC28E12.03","SPCC1840.02c","SPBC530.04"],"gene_count":12,"ltp_gene_count":12,"approved_date":"2012-05-03"},{"uniquename":"PMID:21980566","title":"Nuclear translocation of RanGAP1 coincides with virtual nuclear envelope breakdown in fission yeast meiosis.","citation":"Commun Integr Biol 2011 May;4(3):312-4","abstract":"In higher eukaryotes, mitosis proceeds with nuclear envelope breakdown (NEBD) and disassembly of the nuclear pore complex (NPC); this is designated \"open\" mitosis. On the other hand, in many fungi, mitosis and chromosome segregation takes place without NEBD; this is designated \"closed\" mitosis. In a recent study on Schizosaccharomyces pombe, a closed mitosis organism, we reported a novel phenomenon that is equivalent to NEBD: a mixing of nuclear proteins and cytoplasmic proteins occurred transiently for a few minutes in meiosis without physical breakdown of the nuclear envelope. We designated this event virtual nuclear envelope breakdown (V-NEBD). In S. pombe, nuclear translocation of Rna1, a RanGAP1 homolog in S. pombe, occurs during meiosis, and this translocation of Rna1 leads to collapse of the Ran-GTP gradient across the nuclear envelope and occurs coincidently with V-NEBD. Here, we describe possible roles of RanGAP1 in V-NEBD in S. pombe and provide insights into the roles V-NEBD may play in meiosis.","doi":"10.4161/cib.4.3.14808","authors":"Asakawa H, Hiraoka Y, Haraguchi T","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"May 2011","pubmed_entrez_date":"2011-10-08","publication_year":"2011","canto_session_key":"00231b1f99c9ea49","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-08-02 15:14:16","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-08-02 01:28:31","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2016-08-02"},{"uniquename":"PMID:9763447","title":"cut11(+): A gene required for cell cycle-dependent spindle pole body anchoring in the nuclear envelope and bipolar spindle formation in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1998 Oct;9(10):2839-55","abstract":"The \"cut\" mutants of Schizosaccharomyces pombe are defective in spindle formation and/or chromosome segregation, but they proceed through the cell cycle, resulting in lethality. Analysis of temperature-sensitive alleles of cut11(+) suggests that this gene is required for the formation of a functional bipolar spindle. Defective spindle structure was revealed with fluorescent probes for tubulin and DNA. Three-dimensional reconstruction of mutant spindles by serial sectioning and electron microscopy showed that the spindle pole bodies (SPBs) either failed to complete normal duplication or were free floating in the nucleoplasm. Localization of Cut11p tagged with the green fluorescent protein showed punctate nuclear envelope staining throughout the cell cycle and SPBs staining from early prophase to mid anaphase. This SPB localization correlates with the time in the cell cycle when SPBs are inserted into the nuclear envelope. Immunoelectron microscopy confirmed the localization of Cut11p to mitotic SPBs and nuclear pore complexes. Cloning and sequencing showed that cut11(+) encodes a novel protein with seven putative membrane-spanning domains and homology to the Saccharomyces cerevisiae gene NDC1. These data suggest that Cut11p associates with nuclear pore complexes and mitotic SPBs as an anchor in the nuclear envelope; this role is essential for mitosis.","authors":"West RR, Vaisberg EV, Ding R, Nurse P, McIntosh JR","authors_abbrev":"West RR et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-10-08","publication_year":"1998","canto_session_key":"36f40baed62fc60c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-01-06 20:52:15","canto_approved_date":"2026-06-01 06:51:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-01-03 09:43:16","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPBC649.05","SPAC1786.03"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-01-06"},{"uniquename":"PMID:28497540","title":"Meikin-associated polo-like kinase specifies Bub1 distribution in meiosis I.","citation":"Genes Cells 2017 Jun;22(6):552-567","abstract":"In meiosis I, sister chromatids are captured by microtubules emanating from the same pole (mono-orientation), and centromeric cohesion is protected throughout anaphase. Shugoshin, which is localized to centromeres depending on the phosphorylation of histone H2A by Bub1 kinase, plays a central role in protecting meiotic cohesin Rec8 from separase cleavage. Another key meiotic kinetochore factor, meikin, may regulate cohesion protection, although the underlying molecular mechanisms remain elusive. Here, we show that fission yeast Moa1 (meikin), which associates stably with CENP-C during meiosis I, recruits Plo1 (polo-like kinase) to the kinetochores and phosphorylates Spc7 (KNL1) to accumulate Bub1. Consequently, in contrast to the transient kinetochore localization of mitotic Bub1, meiotic Bub1 persists at kinetochores until anaphase I. The meiotic Bub1 pool ensures robust Sgo1 (shugoshin) localization and cohesion protection at centromeres by cooperating with heterochromatin protein Swi6, which binds and stabilizes Sgo1. Furthermore, molecular genetic analyses show a hierarchical regulation of centromeric cohesion protection by meikin and shugoshin that is important for establishing meiosis-specific chromosome segregation. We provide evidence that the meiosis-specific Bub1 regulation is conserved in mouse.","doi":"10.1111/gtc.12496","authors":"Miyazaki S, Kim J, Yamagishi Y, Ishiguro T, Okada Y, Tanno Y, Sakuno T, Watanabe Y","authors_abbrev":"Miyazaki S et al.","pubmed_publication_date":"Jun 2017","pubmed_entrez_date":"2017-05-13","publication_year":"2017","canto_session_key":"2a8be2bb0239204b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-11-27 20:01:56","canto_approved_date":"2025-09-03 14:45:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-11-27 14:20:42","canto_added_date":"2017-05-14 00:15:14","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":44,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBP35G2.03c","SPBC20F10.06","SPBC106.01","SPCC1020.02","SPCC1322.12c","SPBC1861.01c","SPAC23H3.08c","SPAC23C11.16","SPAC15E1.07c","SPAC664.01c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2019-11-27"},{"uniquename":"PMID:15591066","title":"Expression of a RecQ helicase homolog affects progression through crisis in fission yeast lacking telomerase.","citation":"J Biol Chem 2005 Feb 18;280(7):5249-57","abstract":"RecQ helicases play roles in telomere maintenance in cancerous human cells using the alternative lengthening of telomeres mechanism and in budding yeast lacking telomerase. Fission yeast lacking the catalytic subunit of telomerase (trt1(+)) up-regulate the expression of a previously uncharacterized sub-telomeric open reading frame as survivors emerge from crisis. Here we show that this open reading frame encodes a protein with homology to RecQ helicases such as the human Bloom's and Werner's syndrome proteins and that copies of the helicase gene are present on multiple chromosome ends. Characterization of the helicase transcript revealed a 7.6-kilobase RNA that was associated with polyribosomes, suggesting it is translated. A 3.6-kilobase domain of the helicase gene predicted to encode the region with catalytic activity was cloned, and both native and mutant forms of this domain were overexpressed in trt1(-) cells as they progressed through crisis. Overexpression of the native form caused cells to recover from crisis earlier than cells with a vector-only control, whereas overexpression of the mutant form caused delayed recovery from crisis. Taken together, the sequence homology, functional analysis, and site-directed mutagenesis indicate that the protein is likely a second fission yeast RecQ helicase (in addition to Rqh1) that participates in telomere metabolism during crisis. These results strengthen the notion that in multiple organisms RecQ helicases contribute to survival after telomere damage.","authors":"Mandell JG, Goodrich KJ, Bähler J, Cech TR","authors_abbrev":"Mandell JG et al.","pubmed_publication_date":"18 Feb 2005","pubmed_entrez_date":"2004-12-14","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC212.11","SPBCPT2R1.08c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:24818994","title":"The S. pombe translation initiation factor eIF4G is Sumoylated and associates with the SUMO protease Ulp2.","citation":"PLoS One 2014;9(5):e94182","abstract":"SUMO is a small post-translational modifier, that is attached to lysine residues in target proteins. It acts by altering protein-protein interactions, protein localisation and protein activity. SUMO chains can also act as substrates for ubiquitination, resulting in proteasome-mediated degradation of the target protein. SUMO is removed from target proteins by one of a number of specific proteases. The processes of sumoylation and desumoylation have well documented roles in DNA metabolism and in the maintenance of chromatin structure. To further analyse the role of this modification, we have purified protein complexes containing the S. pombe SUMO protease, Ulp2. These complexes contain proteins required for ribosome biogenesis, RNA stability and protein synthesis. Here we have focussed on two translation initiation factors that we identified as co-purifying with Ulp2, eIF4G and eIF3h. We demonstrate that eIF4G, but not eIF3h, is sumoylated. This modification is increased under conditions that produce cytoplasmic stress granules. Consistent with this we observe partial co-localisation of eIF4G and SUMO in stressed cells. Using HeLa cells, we demonstrate that human eIF4GI is also sumoylated; in vitro studies indicate that human eIF4GI is modified on K1368 and K1588, that are located in the C-terminal eIF4A- and Mnk-binding sites respectively.","doi":"10.1371/journal.pone.0094182","authors":"Jongjitwimol J, Feng M, Zhou L, Wilkinson O, Small L, Baldock R, Taylor DL, Smith D, Bowler LD, Morley SJ, Watts FZ","authors_abbrev":"Jongjitwimol J et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-05-14","publication_year":"2014","canto_session_key":"1116101d850ce3e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-11-01 21:32:31","canto_approved_date":"2017-11-01 21:32:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-19 16:17:34","canto_added_date":"2014-06-09 10:36:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":19,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.05","SPAC23A1.10","SPCC1183.07","SPBC1709.05","SPAC57A7.04c","SPBC17D11.05","SPAC17A5.07c","SPAC694.02","SPAC17A5.14","SPBC19G7.09","SPAC17A5.03","SPBC83.14c","SPAC29A4.08c","SPAC57A10.10c","SPBC839.15c","SPAC17H9.13c","SPAC32A11.04c","SPAC3G9.09c","SPBP8B7.20c","SPCC417.08","SPBC19G7.10c","SPBC800.08","SPAPB8E5.06c","SPCP31B10.07","SPBC4C3.05c","SPBC354.12","SPAC25G10.08","SPAC4A8.16c","SPBC660.11","SPBP23A10.07","SPBC16H5.02","SPAC16C9.06c","SPAC22G7.05","SPAC17C9.03","SPBC16H5.12c","SPAC513.01c","SPAC26A3.12c","SPBC32F12.11","SPBP4H10.15","SPBC365.06","SPAC1142.04","SPBP8B7.16c","SPCC794.09c","SPCC16C4.15"],"gene_count":44,"ltp_gene_count":44,"approved_date":"2017-11-01"},{"uniquename":"PMID:12067650","title":"The many faces of histone lysine methylation.","citation":"Curr Opin Cell Biol 2002 Jun;14(3):286-98","abstract":"Diverse post-translational modifications of histone amino termini represent an important epigenetic mechanism for the organisation of chromatin structure and the regulation of gene activity. Within the past two years, great progress has been made in understanding the functional implications of histone methylation; in particular through the characterisation of histone methyltransferases that direct the site-specific methylation of, for example, lysine 9 and lysine 4 positions in the histone H3 amino terminus. All known histone methyltransferases of this type contain the evolutionarily conserved SET domain and appear to be able to stimulate either gene repression or gene activation. Methylation of H3 Lys9 and Lys4 has been visualised in native chromatin, indicating opposite roles in structuring repressive or accessible chromatin domains. For example, at the mating-type loci in Schizosaccharomyces pombe, at pericentric heterochromatin and at the inactive X chromosome in mammals, striking differences between these distinct marks have been observed. H3 Lys9 methylation is also important to direct additional epigenetic signals such as DNA methylation--for example, in Neurospora crassa and in Arabidopsis thaliana. Together, the available data strongly establish histone lysine methylation as a central modification for the epigenetic organisation of eukaryotic genomes.","authors":"Lachner M, Jenuwein T","authors_abbrev":"Lachner M et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-06-18","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11943358","title":"Electro-orientation of Schizosaccharomyces pombe in high conductivity media.","citation":"J Microbiol Methods 2002 Jun;50(1):55-62","abstract":"The orientation of microbial cells may be important in cell-cell interactions within microbial consortia. As part of our research programme aimed at the construction of Artificial Structured Microbial Consortia (ASMC), we have investigated the electro-orientation of Schizosaccharomyces pombe in AC electric fields, and studied the effects of the applied frequency, voltage, and distance between the electrodes, at different medium conductivities. It is shown that the electro-orientation of S. pombe in media with conductivities similar to that of growth media is feasible using microelectrodes. Oriented growth of S. pombe can be obtained when continuously exposed to AC electric fields in growth medium over extended periods.","authors":"Markx GH, Alp B, McGilchrist A","authors_abbrev":"Markx GH et al.","pubmed_publication_date":"Jun 2002","pubmed_entrez_date":"2002-04-12","publication_year":"2002","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8774852","title":"An actin point-mutation neighboring the 'hydrophobic plug' causes defects in the maintenance of cell polarity and septum organization in the fission yeast Schizosaccharomyces pombe.","citation":"FEBS Lett 1996 Sep 02;392(3):237-41","abstract":"The fission yeast cps8 mutation gives rise to abnormally enlarged and dispolarized cells, each of which contains several nuclei with aberrant multisepta. Molecular cloning and sequence analysis of the cps8 gene indicated that it encodes an actin with an amino acid substitution of aspartic acid for glycine at residue 273 in the hydrophobic loop that is located between actin subdomains 3 and 4. Fluorescence microscopy using phalloidin and anti-actin antibody revealed changes in the F-actin structure and distribution in the mutant cells. These results indicate that the hydrophobic loop plays an essential role for creating normal F-actin structure, only by which cell polarity and the late mitotic events can be maintained properly.","authors":"Ishiguro J, Kobayashi W","authors_abbrev":"Ishiguro J et al.","pubmed_publication_date":"02 Sep 1996","pubmed_entrez_date":"1996-09-02","publication_year":"1996","canto_session_key":"16b1348c23ad9e5d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-12-17 14:17:00","canto_approved_date":"2019-12-17 14:17:01","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-12-17 14:16:48","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-12-17"},{"uniquename":"PMID:29916047","title":"An agent-based model of the fission yeast cell cycle.","citation":"Curr Genet 2019 Feb;65(1):193-200","abstract":"The objective of this paper is to develop a computational model of the fission yeast (Schizosaccharomyces pombe) cell cycle using agent-based modeling (ABM), to study the sequence of states of the proteins and time of the cell cycle phases, under the action of proteins that regulate its cell cycle. The model relies only on the conceptual model of the yeast cell cycle regulatory network, where each protein has been represented as an agent with a property called activity that represents its biological function and a stochastic Brownian movement. The results indicate that the simulated phase time did have similar results in comparison with other models using mathematical approaches. Similarly, the correct sequence of states was achieved, and the model was run under different initial states to understand its emergent behaviors. The cell reached the G1 stationary state 94% of the times when running the model under biological initial conditions and 87% of the times when running the model through all the different combinations of initial states. Such results imply that the cell was capable to fix toward the biological expected phenomena. These results show that ABM is a suitable technique to study protein-protein interactions without using, often unavailable, kinetic parameters, or differential equations. This model sets as a base for further studies that involve the cell cycle of the fission yeast, with a special attention to studies and development of drug treatments for specific types of cancer.","doi":"10.1007/s00294-018-0859-z","authors":"Castro C, Flores DL, Cervantes-Vásquez D, Vargas-Viveros E, Gutiérrez-López E, Muñoz-Muñoz F","authors_abbrev":"Castro C et al.","pubmed_publication_date":"Feb 2019","pubmed_entrez_date":"2018-06-20","publication_year":"2019","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2018-06-21 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21256022","title":"Ndc80 internal loop interacts with Dis1/TOG to ensure proper kinetochore-spindle attachment in fission yeast.","citation":"Curr Biol 2011 Feb 08;21(3):214-20","abstract":"The Ndc80 complex, a conserved outer kinetochore complex, comprising four components (Ndc80/Hec1, Nuf2, Spc24, and Spc25), constitutes one of the core microtubule-binding sites within the kinetochore. Despite this knowledge, molecular mechanisms by which this complex contributes to establishment of correct bipolar attachment of the kinetochore to the spindle microtubule remain largely elusive. Here we show that the conserved internal loop of fission yeast Ndc80 directly binds the Dis1/TOG microtubule-associated protein, thereby coupling spindle microtubule dynamics with kinetochore capture. Ndc80 loop mutant proteins fail to recruit Dis1 to kinetochores, imposing unstable attachment and frequent spindle collapse. In these mutants, mitotic progression is halted attributable to spindle assembly checkpoint activation, and chromosomes remain in the vicinity of the spindle poles without congression. dis1 deletion precisely phenocopies the loop mutants. Intriguingly, forced targeting of Dis1 to the Ndc80 complex rescues loop mutant's defects. We propose that Ndc80 comprises two microtubule-interacting interfaces: the N-terminal region directly binds the microtubule lattice, while the internal loop interacts with the plus end of microtubules via Dis1/TOG. Therefore, our results provide a crucial insight into how the Ndc80 complex establishes stable bipolar attachment to the spindle microtubule.","doi":"10.1016/j.cub.2010.12.048","authors":"Hsu KS, Toda T","authors_abbrev":"Hsu KS et al.","pubmed_publication_date":"08 Feb 2011","pubmed_entrez_date":"2011-01-25","publication_year":"2011","canto_session_key":"53b4f5e5547d3733","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2017-10-26 15:33:15","canto_approved_date":"2025-12-31 11:39:40","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-09 11:20:48","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[{"name":"Takashi Toda","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.03","SPCC736.14","SPAC589.08c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-10-26"},{"uniquename":"PMID:15925945","title":"Direct activation of fission yeast adenylyl cyclase by heterotrimeric G protein gpa2.","citation":"Kobe J Med Sci 2004;50(3-4):111-21","abstract":"Genetic studies on Schizosaccharomyces pombe adenylyl cyclase (cyr1) have shown that its activity is positively regulated by a heterotrimetric G protein a subunit gpa2 and that the resulting increase in intracellular cAMP concentration causes inhibition of sexual development including mating and meiosis. However, molecular mechanism underlying this gpa2-dependent regulation of cyr1 remains to be clarified. Here, we show that gpa2 exhibits a direct and GTP-dependent binding to the Ras-associating domain (RAD) of cyr1, which is identified by a computer algorithm-based search of the cyr1 amino acid sequence. Overexpression of this RAD results in acceleration of the sexual development of fission yeast cells presumably by competitive sequestration of gpa2. Furthermore, cyr1 is activated in vitro by the addition of purified gpa2, which is converted to the active state by treatment with AlF4-. These results indicate a crucial role of the RAD as a direct binding site of gpa2 in activation of cyr1. Thus, RADs, which have been defined as a conserved motif shared among the Ras-family small G protein-associating domains, are for the first time shown to exhibit a functional association with a member of the heterotrimeric G proteins.","authors":"Ogihara H, Shima F, Naito K, Asato T, Kariya K, Kataoka T","authors_abbrev":"Ogihara H et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2005-06-01","publication_year":"2004","canto_session_key":"1f9e5de7abad88fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-11-14 17:37:01","canto_approved_date":"2020-12-13 11:13:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-09-21 15:35:13","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H3.13c","SPBC19C7.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-11-14"},{"uniquename":"PMID:38360270","title":"A KDELR-mediated ER-retrieval system modulates mitochondrial functions via the unfolded protein response in fission yeast.","citation":"J Biol Chem 2024 Feb 13;:105754","abstract":"KDELR (Erd2 in yeasts) is a receptor protein that retrieves ER-resident proteins from the Golgi apparatus. However, the role of the KDELR-mediated ER-retrieval system in regulating cellular homeostasis remains elusive. Here we show that the absence of Erd2 triggers the unfolded protein response (UPR) and enhances mitochondrial respiration and reactive oxygen species (ROS) in an UPR-dependent manner in the fission yeast Schizosaccharomyces Pombe. Moreover, we perform transcriptomic analysis and find that the expression of genes related to mitochondrial respiration and the tricarboxylic acid cycle is upregulated in a UPR-dependent manner in cells lacking Erd2. The increased mitochondrial respiration and ROS production is required for cell survival in the absence of Erd2. Therefore, our findings reveal a novel role of the KDELR/Erd2-mediated ER-retrieval system in modulating mitochondrial functions and highlight its importance for cellular homeostasis in the fission yeast.","doi":"10.1016/j.jbc.2024.105754","authors":"Zhu M, Fang Z, Wu Y, Dong F, Wang Y, Zheng F, Ma X, Ma S, He J, Liu X, Yao X, Fu C","authors_abbrev":"Zhu M et al.","pubmed_publication_date":"13 Feb 2024","pubmed_entrez_date":"2024-02-15","publication_year":"2024","canto_session_key":"2c52a27e773dd541","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Mengdan Zhu","canto_first_approved_date":"2024-03-31 08:09:55","canto_approved_date":"2024-04-10 09:09:20","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-03-15 18:32:55","canto_added_date":"2024-02-17 00:25:04","annotation_curators":[{"name":"Mengdan Zhu","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":40,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.14","SPAC167.01","SPCC830.08c","SPBC16H5.06","SPBC16E9.01c","SPBC3B8.02","SPAC23C11.08","SPBC29A10.08","SPAC222.12c","SPBP8B7.22","SPBC725.11c","SPCC1739.09c"],"gene_count":12,"ltp_gene_count":8,"approved_date":"2024-03-31"},{"uniquename":"PMID:21179023","title":"Cross-species chemogenomic profiling reveals evolutionarily conserved drug mode of action.","citation":"Mol Syst Biol 2010 Dec 21;6:451","abstract":"We present a cross-species chemogenomic screening platform using libraries of haploid deletion mutants from two yeast species, Saccharomyces cerevisiae and Schizosaccharomyces pombe. We screened a set of compounds of known and unknown mode of action (MoA) and derived quantitative drug scores (or D-scores), identifying mutants that are either sensitive or resistant to particular compounds. We found that compound-functional module relationships are more conserved than individual compound-gene interactions between these two species. Furthermore, we observed that combining data from both species allows for more accurate prediction of MoA. Finally, using this platform, we identified a novel small molecule that acts as a DNA damaging agent and demonstrate that its MoA is conserved in human cells.","doi":"10.1038/msb.2010.107","authors":"Kapitzky L, Beltrao P, Berens TJ, Gassner N, Zhou C, Wüster A, Wu J, Babu MM, Elledge SJ, Toczyski D, Lokey RS, Krogan NJ","authors_abbrev":"Kapitzky L et al.","pubmed_publication_date":"21 Dec 2010","pubmed_entrez_date":"2010-12-24","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18579787","title":"The FACT Spt16 \"peptidase\" domain is a histone H3-H4 binding module.","citation":"Proc Natl Acad Sci U S A 2008 Jul 01;105(26):8884-9","abstract":"The FACT complex is a conserved cofactor for RNA polymerase II elongation through nucleosomes. FACT bears histone chaperone activity and contributes to chromatin integrity. However, the molecular mechanisms behind FACT function remain elusive. Here we report biochemical, structural, and mutational analyses that identify the peptidase homology domain of the Schizosaccharomyces pombe FACT large subunit Spt16 (Spt16-N) as a binding module for histones H3 and H4. The 2.1-A crystal structure of Spt16-N reveals an aminopeptidase P fold whose enzymatic activity has been lost. Instead, the highly conserved fold directly binds histones H3-H4 through a tight interaction with their globular core domains, as well as with their N-terminal tails. Mutations within a conserved surface pocket in Spt16-N or posttranslational modification of the histone H4 tail reduce interaction in vitro, whereas the globular domains of H3-H4 and the H3 tail bind distinct Spt16-N surfaces. Our analysis suggests that the N-terminal domain of Spt16 may add to the known H2A-H2B chaperone activity of FACT by including a H3-H4 tail and H3-H4 core binding function mediated by the N terminus of Spt16. We suggest that these interactions may aid FACT-mediated nucleosome reorganization events.","doi":"10.1073/pnas.0712293105","authors":"Stuwe T, Hothorn M, Lejeune E, Rybin V, Bortfeld M, Scheffzek K, Ladurner AG","authors_abbrev":"Stuwe T et al.","pubmed_publication_date":"01 Jul 2008","pubmed_entrez_date":"2008-06-27","publication_year":"2008","canto_session_key":"929e3ae344538c03","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-02-09 15:33:07","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-12-13 14:26:56","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.03c","SPBC1105.12","SPAC1834.04","SPBC8D2.03c","SPBC8D2.04","SPBP8B7.19","SPBC1105.11c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2012-12-13","pdb_entries":[{"pdb_id":"3cb5","gene_chains":[{"gene_uniquename":"SPBP8B7.19","chain":"A/B","position":"1-442"}],"title":"Crystal Structure of the S. pombe Peptidase Homology Domain of FACT complex subunit Spt16 (form A)","entry_authors":"Stuwe T,Hothorn M,Lejeune E,Bortfeld-Miller M,Scheffzek K,Ladurner AG","entry_authors_abbrev":"Stuwe T et al.","reference_uniquename":"PMID:18579787","experimental_method":"X-ray","resolution":"2.05"},{"pdb_id":"3cb6","gene_chains":[{"gene_uniquename":"SPBP8B7.19","chain":"A","position":"1-442"}],"title":"Crystal Structure of the S. pombe Peptidase Homology Domain of FACT complex subunit Spt16 (form B)","entry_authors":"Stuwe T,Hothorn M,Lejeune E,Bortfeld-Miller M,Scheffzek K,Ladurner AG","entry_authors_abbrev":"Stuwe T et al.","reference_uniquename":"PMID:18579787","experimental_method":"X-ray","resolution":"1.84"}]},{"uniquename":"PMID:21149581","title":"Genomic mRNA profiling reveals compensatory mechanisms for the requirement of the essential splicing factor U2AF.","citation":"Mol Cell Biol 2011 Feb;31(4):652-61","abstract":"The large subunit of the U2 auxiliary factor (U2AF) recognizes the polypyrimidine tract (Py-tract) located adjacent to the 3' splice site to facilitate U2 snRNP recruitment. While U2AF is considered essential for pre-mRNA splicing, its requirement for splicing on a genome-wide level has not been analyzed. Using Solexa sequencing, we performed mRNA profiling for splicing in the Schizosaccharomyces pombe U2AF(59) (prp2.1) temperature-sensitive mutant. Surprisingly, our analysis revealed that introns show a range of splicing defects in the mutant strain. While U2AF(59) inactivation (nonpermissive) conditions inhibit splicing of some introns, others are spliced apparently normally. Bioinformatics analysis indicated that U2AF(59)-insensitive introns have stronger 5' splice sites and higher A/U content. Most importantly, features that contribute to U2AF(59) insensitivity of an intron unexpectedly reside in its 5'-most 30 nucleotides. These include the 5' splice site, a guanosine at position 7, and the 5' splice site-to-branch point sequence context. A differential requirement (similar to U2AF(59)) for introns may also apply to other general splicing factors (e.g., prp10). Our combined results indicate that U2AF insensitivity is a common phenomenon and that varied intron features support the existence of unrecognized aspects of spliceosome assembly.","doi":"10.1128/MCB.01000-10","authors":"Sridharan V, Heimiller J, Singh R","authors_abbrev":"Sridharan V et al.","pubmed_publication_date":"Feb 2011","pubmed_entrez_date":"2010-12-15","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11842100","title":"The Schizosaccharomyces pombe mgU6-47 gene is required for 2'-O-methylation of U6 snRNA at A41.","citation":"Nucleic Acids Res 2002 Feb 15;30(4):894-902","abstract":"Through a computer search of DNA databases, we have identified the homologs of the mgU6-47 snoRNA gene from the yeast Schizosaccharomyces pombe, the fly Drosophila melanogaster and human. The three box C/D-containing snoRNA genes showed no significant similarity in their sequences except for an 11 nt long complementarity to U6 snRNA, suggesting that the mechanism of snoRNA guided snRNA methylation is conserved from mammals to yeast. The corresponding snoRNAs have been positively detected by reverse transcription and northern blotting. Taking advantage of the fission yeast system, we have disrupted the yeast mgU6-47 gene and demonstrated that it is absolutely required for site-specific 2'-O-methylation of U6 at position A41. No growth differences between mgU6-47 gene-disrupted and wild-type cells were observed, suggesting that the mgU6-47 gene, as for most rRNA methylation guides, is dispensable in yeast. Nevertheless, it was revealed by temperature shift assay that abolition of A41 methylation in yeast U6 snRNA might cause a small decrease in mRNA splicing efficiency. The timing of S.pombe U6 pre-RNA transport in the nucleus for splicing and methylation was also analyzed and is described.","authors":"Zhou H, Chen YQ, Du YP, Qu LH","authors_abbrev":"Zhou H et al.","pubmed_publication_date":"15 Feb 2002","pubmed_entrez_date":"2002-02-14","publication_year":"2002","canto_session_key":"f823839cd52d54e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-07 22:44:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-09-07 21:29:38","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNORNA.25","SPSNRNA.06"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-09-07"},{"uniquename":"PMID:26093291","title":"Long G2 accumulates recombination intermediates and disturbs chromosome segregation at dysfunction telomere in Schizosaccharomyces pombe.","citation":"Biochem Biophys Res Commun 2015 Aug 14;464(1):140-6","abstract":"Protection of telomere (Pot1) is a single-stranded telomere binding protein which is essential for chromosome ends protection. Fission yeast Rqh1 is a member of RecQ helicases family which has essential roles in the maintenance of genomic stability and regulation of homologous recombination. Double mutant between fission yeast pot1Δ and rqh1 helicase dead (rqh1-hd) maintains telomere by homologous recombination. In pot1Δ rqh1-hd double mutant, recombination intermediates accumulate near telomere which disturb chromosome segregation and make cells sensitive to microtubule inhibitors thiabendazole (TBZ). Deletion of chk1(+) or mutation of its kinase domain shortens the G2 of pot1Δ rqh1-hd double mutant and suppresses both the accumulation of recombination intermediates and the TBZ sensitivity of that double mutant. In this study, we asked whether the long G2 is the reason for the TBZ sensitivity of pot1Δ rqh1-hd double mutant. We found that shortening the G2 of pot1Δ rqh1-hd double mutant by additional mutations of wee1 and mik1 or gain of function mutation of Cdc2 suppresses both the accumulation of recombination intermediates and the TBZ sensitivity of pot1Δ rqh1-hd double mutant. Our results suggest that long G2 of pot1Δ rqh1-hd double mutant may allow time for the accumulation of recombination intermediates which disturb chromosome segregation and make cells sensitive to TBZ.","doi":"10.1016/j.bbrc.2015.06.098","authors":"Habib AG, Masuda K, Yukawa M, Tsuchiya E, Ueno M","authors_abbrev":"Habib AG et al.","pubmed_publication_date":"14 Aug 2015","pubmed_entrez_date":"2015-06-21","publication_year":"2015","canto_session_key":"5c3399b38391e7b0","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-06-22 00:20:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC18B5.03","SPCC1259.13","SPAC2G11.12","SPAC26H5.06","SPBC11B10.09","SPBC660.14"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:18761674","title":"Fission yeast chromatin assembly factor 1 assists in the replication-coupled maintenance of heterochromatin.","citation":"Genes Cells 2008 Oct;13(10):1027-43","abstract":"Chromatin assembly factor-1 (CAF1) is a well-conserved histone chaperone that loads the histone H3-H4 complex onto newly synthesized DNA in vitro through interaction with the replication factor PCNA. CAF1 is considered to be involved in heterochromatin maintenance in several organisms, but the evidence is circumstantial and functional details have not been established. We identified fission yeast CAF-1 (spCAF1), which interacts with PCNA in S phase. Depletion of spCAF1 caused defects in silencing at centromeric and mating locus heterochromatin, accompanied with a decrease in Swi6, the fission yeast HP1 homologue. Loss of spCAF1 destabilized both the silent and active states of chromatin at the meta-stable heterochromatic region, with a more pronounced effect on the silent state, indicating that spCAF1 is involved in the maintenance of heterochromatin. Swi6 dissociated from heterochromatin during G1/S phase appears to associate with spCAF1. In early S phase, spCAF1 localized to replicating heterochromatin as well as euchromatin and remained associated with Swi6, and Swi6 then bound to heterochromatin. Taken together, we propose that spCAF1 functions in heterochromatin maintenance by recruiting dislocated Swi6 during replication to replicated heterochromatin at the replication fork.","doi":"10.1111/j.1365-2443.2008.01225.x","authors":"Dohke K, Miyazaki S, Tanaka K, Urano T, Grewal SI, Murakami Y","authors_abbrev":"Dohke K et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-09-03","publication_year":"2008","canto_session_key":"7959dfb6db2b260d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-06-04 13:47:46","canto_approved_date":"2022-02-11 14:50:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-28 15:36:09","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":60,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25H1.06","HGNC:1910","SPAC664.01c","HGNC:1911","YBR195C","SPBC16D10.09","SPAC26H5.03","SPBC29A10.03c","SPBC428.08c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2015-06-04"},{"uniquename":"PMID:29424342","title":"YTH-RNA-binding protein prevents deleterious expression of meiotic proteins by tethering their mRNAs to nuclear foci.","citation":"Elife 2018 Feb 09;7","abstract":"Accurate and extensive regulation of meiotic gene expression is crucial to distinguish germ cells from somatic cells. In the fission yeast  Schizosaccharomyces pombe,  a YTH family RNA-binding protein, Mmi1, directs the nuclear exosome-mediated elimination of meiotic transcripts during vegetative proliferation. Mmi1 also induces the formation of facultative heterochromatin at a subset of its target genes. Here, we show that Mmi1 prevents the mistimed expression of meiotic proteins by tethering their mRNAs to the nuclear foci. Mmi1 interacts with itself with the assistance of a homolog of Enhancer of Rudimentary, Erh1. Mmi1 self-interaction is required for foci formation, target transcript elimination, their nuclear retention, and protein expression inhibition. We propose that nuclear foci formed by Mmi1 are not only the site of RNA degradation, but also of sequestration of meiotic transcripts from the translation machinery.","doi":"10.7554/eLife.32155","authors":"Shichino Y, Otsubo Y, Kimori Y, Yamamoto M, Yamashita A","authors_abbrev":"Shichino Y et al.","pubmed_publication_date":"09 Feb 2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_session_key":"89222eafc99f3372","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Akira Yamashita","canto_first_approved_date":"2019-04-30 10:29:53","canto_approved_date":"2024-06-27 16:54:35","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2019-02-21 02:59:24","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[{"name":"Akira Yamashita","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Antonia Lock","community_curator":false,"annotation_count":69,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.11","SPAC19G12.17","SPBC16E9.12c","SPAC1006.03c","SPAC1F3.01","SPBC16A3.05c","SPBC2A9.11c","SPBC337.03","SPAC27D7.13c","SPCC736.12c"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2019-04-30"},{"uniquename":"PMID:28925811","title":"It's fun to transcribe with Fun30: A model for nucleosome dynamics during RNA polymerase II-mediated elongation.","citation":"Transcription 2018;9(2):108-116","abstract":"The ability of elongating RNA polymerase II (RNAPII) to regulate the nucleosome barrier is poorly understood because we do not know enough about the involved factors and we lack a conceptual framework to model this process. Our group recently identified the conserved Fun30/SMARCAD1 family chromatin-remodeling factor, Fun30 Fft3 , as being critical for relieving the nucleosome barrier during RNAPII-mediated elongation, and proposed a model illustrating how Fun30 Fft3  may contribute to nucleosome disassembly during RNAPII-mediated elongation. Here, we present a model that describes nucleosome dynamics during RNAPII-mediated elongation in mathematical terms and addresses the involvement of Fun30 Fft3  in this process.","doi":"10.1080/21541264.2017.1356434","authors":"Lee J, Choi ES, Lee D","authors_abbrev":"Lee J et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2017-09-20","publication_year":"2018","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2018-11-11 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9339378","title":"Genomic organization and functional analysis of the murine protein phosphatase 1c gamma (Ppp1cc) gene.","citation":"Genomics 1997 Oct 01;45(1):211-5","abstract":"Protein phosphatase 1 holoenzymes are composed of catalytic subunits in combination with various regulatory subunits. In rodents, four different catalytic isoforms are known, PP1c alpha, -delta, -gamma 1, and -gamma 2. Here we describe the genomic organization of the murine Ppp1cc gene that encodes the PP1c gamma 1 and PP1c gamma 2 isoforms. We determined that Ppp1cc maps to F1.2-G1.2 on chromosome 5 by FISH mapping. Southern hybridization and analysis of cross-hybridizing genomic clones revealed four Ppp1cc-related pseudogenes in the mouse genome. The authentic Ppp1cc gene encodes two isoforms, PP1c gamma 1 and PP1c gamma 2, that arise from alternative splicing and differ by retention of the last intron. The introns of Ppp1cc are flanked by short direct repeats, the significance of which is not clear. Both isoforms retain phosphatase function since they are able to complement the cold-sensitive PP1 defect caused by the dis2-11 mutation in the fission yeast Schizosaccharomyces pombe.","authors":"Okano K, Heng H, Trevisanato S, Tyers M, Varmuza S","authors_abbrev":"Okano K et al.","pubmed_publication_date":"01 Oct 1997","pubmed_entrez_date":"1997-10-27","publication_year":"1997","canto_session_key":"e64f8f392c63b081","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 16:20:39","canto_session_submitted_date":"2012-03-03 16:20:19","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC776.02c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"EMBL:AU009580","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27540631","title":"The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis.","citation":"Elife 2016 Aug 19;5","abstract":"Mitochondrial fatty acid synthesis (FASII) and iron sulfur cluster (FeS) biogenesis are both vital biosynthetic processes within mitochondria. In this study, we demonstrate that the mitochondrial acyl carrier protein (ACP), which has a well-known role in FASII, plays an unexpected and evolutionarily conserved role in FeS biogenesis. ACP is a stable and essential subunit of the eukaryotic FeS biogenesis complex. In the absence of ACP, the complex is destabilized resulting in a profound depletion of FeS throughout the cell. This role of ACP depends upon its covalently bound 4'-phosphopantetheine (4-PP)-conjugated acyl chain to support maximal cysteine desulfurase activity. Thus, it is likely that ACP is not simply an obligate subunit but also exploits the 4-PP-conjugated acyl chain to coordinate mitochondrial fatty acid and FeS biogenesis.","doi":"10.7554/eLife.17828","authors":"Van Vranken JG, Jeong MY, Wei P, Chen YC, Gygi SP, Winge DR, Rutter J","authors_abbrev":"Van Vranken JG et al.","pubmed_publication_date":"19 Aug 2016","pubmed_entrez_date":"2016-08-20","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4H3.09"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:17329975","title":"A probabilistic model for cell cycle distributions in synchrony experiments.","citation":"Cell Cycle 2007 Feb 15;6(4):478-88","abstract":"Synchronized populations of cells are often used to study dynamic processes during the cell division cycle. However, the analysis of time series measurements made on synchronized populations is confounded by the fact that populations lose synchrony over time. Time series measurements are thus averages over a population distribution that is broadening over time. Moreover, direct comparison of measurements taken from multiple synchrony experiments is difficult, as the kinetics of progression during the time series are rarely comparable. Here, we present a flexible mathematical model that describes the dynamics of population distributions resulting from synchrony loss over time. The model was developed using S. cerevisiae, but we show that it can be easily adapted to predict distributions in other organisms. We demonstrate that the model reliably fits data collected from populations synchronized by multiple techniques, and can accurately predict cell cycle distributions as measured by other experimental assays. To indicate its broad applicability, we show that the model can be used to compare global periodic transcription data sets from different organisms: S. cerevisiae and S. pombe.","authors":"Orlando DA, Lin CY, Bernard A, Iversen ES, Hartemink AJ, Haase SB","authors_abbrev":"Orlando DA et al.","pubmed_publication_date":"15 Feb 2007","pubmed_entrez_date":"2007-03-03","publication_year":"2007","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35217638","title":"A putative cap binding protein and the methyl phosphate capping enzyme Bin3/MePCE function in telomerase biogenesis.","citation":"Nat Commun 2022 Feb 25;13(1):1067","abstract":"Telomerase reverse transcriptase (TERT) and the noncoding telomerase RNA (TR) subunit constitute the core of telomerase. Additional subunits are required for ribonucleoprotein complex assembly and in some cases remain stably associated with the active holoenzyme. Pof8, a member of the LARP7 protein family is such a constitutive component of telomerase in fission yeast. Using affinity purification of Pof8, we have identified two previously uncharacterized proteins that form a complex with Pof8 and participate in telomerase biogenesis. Both proteins participate in ribonucleoprotein complex assembly and are required for wildtype telomerase activity and telomere length maintenance. One factor we named Thc1 (Telomerase Holoenzyme Component 1) shares structural similarity with the nuclear cap binding complex and the poly-adenosine ribonuclease (PARN), the other is the ortholog of the methyl phosphate capping enzyme (Bin3/MePCE) in metazoans and was named Bmc1 (Bin3/MePCE 1) to reflect its evolutionary roots. Thc1 and Bmc1 function together with Pof8 in recognizing correctly folded telomerase RNA and promoting the recruitment of the Lsm2-8 complex and the catalytic subunit to assemble functional telomerase.","doi":"10.1038/s41467-022-28545-9","authors":"Páez-Moscoso DJ, Ho DV, Pan L, Hildebrand K, Jensen KL, Levy MJ, Florens L, Baumann P","authors_abbrev":"Páez-Moscoso DJ et al.","pubmed_publication_date":"25 Feb 2022","pubmed_entrez_date":"2022-02-26","publication_year":"2022","canto_session_key":"67eda549b501124e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-02-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15821139","title":"Systematic deletion analysis of fission yeast protein kinases.","citation":"Eukaryot Cell 2005 Apr;4(4):799-813","abstract":"Eukaryotic protein kinases are key molecules mediating signal transduction that play a pivotal role in the regulation of various biological processes, including cell cycle progression, cellular morphogenesis, development, and cellular response to environmental changes. A total of 106 eukaryotic protein kinase catalytic-domain-containing proteins have been found in the entire fission yeast genome, 44% (or 64%) of which possess orthologues (or nearest homologues) in humans, based on sequence similarity within catalytic domains. Systematic deletion analysis of all putative protein kinase-encoding genes have revealed that 17 out of 106 were essential for viability, including three previously uncharacterized putative protein kinases. Although the remaining 89 protein kinase mutants were able to form colonies under optimal growth conditions, 46% of the mutants exhibited hypersensitivity to at least 1 of the 17 different stress factors tested. Phenotypic assessment of these mutants allowed us to arrange kinases into functional groups. Based on the results of this assay, we propose also the existence of four major signaling pathways that are involved in the response to 17 stresses tested. Microarray analysis demonstrated a significant correlation between the expression signature and growth phenotype of kinase mutants tested. Our complete microarray data sets are available at http://giscompute.gis.a-star.edu.sg/~gisljh/kinome.","authors":"Bimbó A, Jia Y, Poh SL, Karuturi RK, den Elzen N, Peng X, Zheng L, O'Connell M, Liu ET, Balasubramanian MK, Liu J","authors_abbrev":"Bimbó A et al.","pubmed_publication_date":"Apr 2005","pubmed_entrez_date":"2005-04-12","publication_year":"2005","canto_session_key":"6d7eb81578954307","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-12 17:42:54","canto_approved_date":"2023-09-25 14:57:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-03-05 09:56:52","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"file_curator_name":"Manuel Lera-Ramirez","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Manuel Lera-Ramirez","community_curator":false,"annotation_count":608,"orcid":"0000-0002-8666-9746","file_type":"PHAF","file_name":"PMID_15821139_phaf.tsv"}],"genes":["SPAC890.03","SPAC31G5.09c","SPCC1259.13","SPCC63.08c","SPAC57A10.02","SPBC36B7.09","SPBC119.07","SPCC1322.12c","SPBP35G2.05c","SPBC530.14c","SPAC2F7.03c","SPAC823.03","SPBC1D7.05","SPAC1F3.02c","SPCC74.03c","SPAC16C9.07","SPCC417.06c","SPBP23A10.10","SPAC22E12.14c","SPBC1861.09","SPAC1F5.09c","SPAC15A10.13","SPCC297.03","SPBC32C12.03c","SPCC70.05c","SPCC1322.08","SPBC3H7.15","SPBC409.07c","SPBC18H10.15","SPAC1006.09","SPAC1D4.11c","SPBC6B1.02","SPAC23H4.02","SPBC1778.10c","SPBC557.04","SPBC543.07","SPAC167.01","SPAC29A4.16","SPBC12D12.04c","SPCP1E11.02","SPCC24B10.07","SPAC3C7.06c","SPBC8D2.19","SPCC1020.10","SPAC23H4.17c","SPBC337.04","SPAC23A1.06c","SPAC17G8.14c","SPAC24B11.06c","SPAC20G4.03c","SPBC119.08","SPAC644.06c","SPAC1687.15","SPCC162.10","SPBC725.06c","SPBC106.10","SPCC1919.01","SPAC22G7.08","SPACUNK12.02c","SPAC4G8.05","SPAPB18E9.02c","SPAC12B10.14c","SPAC19E9.02","SPAC110.01","SPCC4G3.08","SPBC16E9.13","SPCC1450.11c","SPAC1805.01c","SPCC18B5.03","SPAC1D4.13","SPAC9G1.02","SPAC222.07c","SPAC14C4.03","SPBC21C3.18","SPAC23C4.12","SPCC16C4.11","SPBC660.14","SPCC18B5.11c","SPBC4F6.06","SPBC106.01","SPBC336.14c","SPBC21.07c","SPBC8D2.01","SPAC2C4.14c","SPAC1D4.06c","SPAC1805.05","SPAC2F3.15","SPBC17F3.02","SPBC32H8.10"],"gene_count":89,"ltp_gene_count":4,"approved_date":"2015-11-12"},{"uniquename":"EMBL:AB084847","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.35"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25186232","title":"The Role of PICALM in Alzheimer's Disease.","citation":"Mol Neurobiol 2015 Aug;52(1):399-413","abstract":"Alzheimer's disease (AD) is a highly heritable disease (with heritability up to 76%) with a complex genetic profile of susceptibility, among which large genome-wide association studies (GWASs) pointed to the phosphatidylinositol-binding clathrin assembly protein (PICALM) gene as a susceptibility locus for late-onset Alzheimer's disease (LOAD) incidence. Here, we summarize the known functions of PICALM and discuss its genetic polymorphisms and their potential physiological effects associated with LOAD. Compelling data indicated that PICALM affects AD risk primarily by modulating production, transportation, and clearance of β-amyloid (Aβ) peptide, but other Aβ-independent pathways are discussed, including tauopathy, synaptic dysfunction, disorganized lipid metabolism, immune disorder, and disrupted iron homeostasis. Finally, given the potential involvement of PICALM in facilitating AD occurrence in multiple ways, it might be possible that targeting PICALM might provide promising and novel avenues for AD therapy.","doi":"10.1007/s12035-014-8878-3","authors":"Xu W, Tan L, Yu JT","authors_abbrev":"Xu W et al.","pubmed_publication_date":"Aug 2015","pubmed_entrez_date":"2014-09-05","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC19F8.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38598031","title":"Pps1, phosphatidylserine synthase, regulates the salt stress response in Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2024 Apr 10;299(1):43","abstract":"Phosphatidylserine (PS) is important for maintaining growth, cytoskeleton, and various functions in yeast; however, its role in stress responses is poorly understood. In Schizosaccharomyces pombe, the PS synthase deletion (pps1∆) mutant shows defects in growth, morphology, cytokinesis, actin cytoskeleton, and cell wall integrity, and these phenotypes are rescued by ethanolamine supplementation. Here, we evaluated the role of Pps1 in the salt stress response in S. pombe. We found that pps1∆ cells are sensitive to salt stresses such as KCl and CaCl 2  even in the presence of ethanolamine. Loss of the functional cAMP-dependent protein kinase (git3∆ or pka1∆) or phospholipase B Plb1 (plb1∆) enhanced the salt stress-sensitive phenotype in pps1∆ cells. Green fluorescent protein (GFP)-Pps1 was localized at the plasma membrane and endoplasmic reticulum regardless of the stress conditions. In pka1∆ cells, GFP-Pps1 was accumulated around the nucleus under the KCl stress. Pka1 was localized in the nucleus and the cytoplasm under normal conditions and transferred from the nucleus to the cytoplasm under salt-stress conditions. Pka1 translocated from the nucleus to the cytoplasm during CaCl 2  stress in the wild-type cells, while it remained localized in the nucleus in pps1∆ cells. Expression and phosphorylation of Pka1-GFP were not changed in pps1∆ cells. Our results demonstrate that Pps1 plays an important role in the salt stress response in S. pombe.","doi":"10.1007/s00438-024-02135-4","authors":"Naozuka G, Kawamukai M, Matsuo Y","authors_abbrev":"Naozuka G et al.","pubmed_publication_date":"10 Apr 2024","pubmed_entrez_date":"2024-04-10","publication_year":"2024","canto_session_key":"7e8ed360ac228b68","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Matsuo","canto_first_approved_date":"2024-04-30 14:33:22","canto_approved_date":"2024-04-30 14:33:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-25 17:26:03","canto_added_date":"2024-04-10 23:25:06","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":16,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Yasuhiro Matsuo","community_curator":true,"annotation_count":43,"orcid":"0000-0002-2858-7179","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.10","SPBC19C7.03","SPCC1753.02c","SPAC8C9.03","SPCC1442.12","SPAC1A6.04c","SPAC6F12.02"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2024-04-30"},{"uniquename":"PMID:11279037","title":"Two WD repeat-containing TATA-binding protein-associated factors in fission yeast that suppress defects in the anaphase-promoting complex.","citation":"J Biol Chem 2001 May 18;276(20):17117-24","abstract":"The general transcription factor IID consists of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). Here we report the isolation of two related TAF genes from the fission yeast Schizosaccharomyces pombe as multicopy suppressors of a temperature-sensitive mutation in the ubiquitin-conjugating enzyme gene ubcP4(+). The ubcP4(ts) mutation causes cell cycle arrest in mitosis, probably due to defects in ubiquitination mediated by the anaphase-promoting complex/cyclosome. One multicopy suppressor is the previously reported gene taf72(+), whereas the other is a previously unidentified gene named taf73(+). We show that the taf73(+) gene, like taf72(+), is essential for cell viability. The taf72(+) and taf73(+) genes encode proteins homologous to WD repeat-containing TAFs such as human TAF100, Drosophila TAF80/85, and Saccharomyces cerevisiae TAF90. We demonstrate that TAF72 and TAF73 proteins are present in the same complex with TBP and other TAFs and that TAF72, but not TAF73, is associated with the putative histone acetylase Gcn5. We also show that overexpression of TAF72 or TAF73 suppresses the cell cycle arrest in mitosis caused by a mutation in the anaphase-promoting complex/cyclosome subunit gene cut9(+). These results suggest that TAF72 and TAF73 may regulate the expression of genes involved in ubiquitin-dependent proteolysis during mitosis. Our study thus provides evidence for a possible role of WD repeat-containing TAFs in the expression of genes involved in progression through the M phase of the cell cycle.","authors":"Mitsuzawa H, Seino H, Yamao F, Ishihama A","authors_abbrev":"Mitsuzawa H et al.","pubmed_publication_date":"18 May 2001","pubmed_entrez_date":"2001-03-30","publication_year":"2001","canto_session_key":"9075dee80f064d3a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-11-27 16:08:31","canto_approved_date":"2024-04-04 09:54:13","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-11-18 13:23:55","canto_added_date":"2012-02-24 05:51:58","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC5E4.03c","SPAC29E6.08","SPCC1259.15c","SPAC13F5.02c","SPBC15D4.14","SPAC1952.05","SPAC6F12.15c","SPAC2G11.14"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2015-11-27"},{"uniquename":"PMID:11741326","title":"Negative regulation of filamentous growth and flocculation by Lkh1, a fission yeast LAMMER kinase homolog.","citation":"Biochem Biophys Res Commun 2001 Dec 21;289(5):1237-42","abstract":"We have isolated a full-length cDNA clone that encodes for a Schizosaccharomyces pombe homolog of the dual-specificity protein kinase of the LAMMER family, lkh1 (lammer kinase homolog). The proposed Lkh1 protein contains 575 amino acids. The lkh1(+) null mutant is viable, but exhibits flocculation upon reaching stationary phase in liquid media and filamentous adhesion growth on solid media. Analysis of the flocculation activity of the lkh1(+) null mutant indicates that asexual aggregation of S. pombe cells into floccules is divalent cation-dependent and galactose-specific. We also demonstrate that the Saccharomyces cerevisiae LAMMER kinase homolog, Kns1, can substitute for the Lkh1 function in S. pombe.","authors":"Kim KH, Cho YM, Kang WH, Kim JH, Byun KH, Park YD, Bae KS, Park HM","authors_abbrev":"Kim KH et al.","pubmed_publication_date":"21 Dec 2001","pubmed_entrez_date":"2001-12-14","publication_year":"2001","canto_session_key":"7d664a208ad17b7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-19 15:04:54","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-19 15:04:48","canto_added_date":"2012-02-24 05:51:19","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":5,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-19"},{"uniquename":"PMID:37525511","title":"ecl family genes: Factors linking starvation and lifespan extension in Schizosaccharomyces pombe.","citation":"Mol Microbiol 2023 Nov;120(5):645-657","abstract":"In the fission yeast Schizosaccharomyces pombe, the duration of survival in the stationary phase, termed the chronological lifespan (CLS), is affected by various environmental factors and the corresponding gene activities. The ecl family genes were identified in the genomic region encoding non-coding RNA as positive regulators of CLS in S. pombe, and subsequently shown to encode relatively short proteins. Several studies revealed that ecl family genes respond to various nutritional starvation conditions via different mechanisms, and they are additionally involved in stress resistance, autophagy, sexual differentiation, and cell cycle control. Recent studies reported that Ecl family proteins strongly suppress target of rapamycin complex 1, which is a conserved eukaryotic nutrient-sensing kinase complex that also regulates longevity in a variety of organisms. In this review, we introduce the regulatory mechanisms of Ecl family proteins and discuss their emerging findings.","doi":"10.1111/mmi.15134","authors":"Ohtsuka H, Otsubo Y, Shimasaki T, Yamashita A, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Nov 2023","pubmed_entrez_date":"2023-08-01","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-08-02 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40216096","title":"The glutathione system maintains the thiol redox balance in the mitochondria of fission yeast.","citation":"Free Radic Biol Med 2025 Apr 09;","abstract":"The thioredoxin and glutathione (GSH)-glutaredoxin electron donor pathways provide a reducing environment to the cell and maintain homeostasis of numerous redox reactions. The abundant tripeptide GSH has multiple roles, including redox buffering, detoxification, peroxide scavenging and iron-sulfur cluster assembly. Glutathione reductase, Pgr1 in fission yeast, maintains glutathione reduced, and it is essential in most organisms. Cells lacking Pgr1 exhibit severe pleiotropic defects. We used multiple approaches to unravel the compartment-specific roles of Pgr1. Our findings confirmed that Pgr1 had dual cytosolic and mitochondrial localization. Mitochondrial homeostasis was severely impaired in Δpgr1 cells and most of these defects were restored by expression of an exclusively mitochondrial Pgr1 isoform. As expected, the cytosol of Δpgr1 cells showed low ratio of reduced-to-oxidized glutathione. However, this did not significantly affect peroxiredoxin-dependent hydrogen peroxide scavenging, suggesting a minimal role, if any, of GSH in cytosolic thiol reduction. The transcriptome of Δpgr1 cells revealed signatures of oxidative stress and iron deprivation, suggesting that the GSH-containing sensor of iron starvation, the glutaredoxin Grx4, is also a sensor of GSH oxidation. In the mitochondria, Pgr1 not only provided the GSH electron donor for the glutaredoxin-based pathway but also recycled mitochondrial Trx2, thereby contributing to thiol redox homeostasis in the matrix. In conclusion, glutathione reductase is essential for maintaining a balanced redox environment in the mitochondria by recycling Trx2, Grx2 and the GSH-containing Grx5, and therefore contributes to the processes of iron-sulfur cluster assembly and respiration, while controlling Grx4 dynamics in the cytosol.","doi":"10.1016/j.freeradbiomed.2025.04.012","authors":"de Cubas L, Boronat S, Vega M, Domènech A, Gómez-Armengol F, Artemov A, Lyublinskaya O, Ayté J, Hidalgo E","authors_abbrev":"de Cubas L et al.","pubmed_publication_date":"09 Apr 2025","pubmed_entrez_date":"2025-04-11","publication_year":"2025","canto_session_key":"e00ef45ba9992bb8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-04-12 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10867006","title":"Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs.","citation":"J Biol Chem 2000 Sep 01;275(35):27266-73","abstract":"Sequence-specific high mobility group (HMG) box factors bind and bend DNA via interactions in the minor groove. Three-dimensional NMR analyses have provided the structural basis for this interaction. The cognate HMG domain DNA motif is generally believed to span 6-8 bases. However, alignment of promoter elements controlled by the yeast genes ste11 and Rox1 has indicated strict conservation of a larger DNA motif. By site selection, we identify a highly specific 12-base pair motif for Ste11, AGAACAAAGAAA. Similarly, we show that Tcf1, MatMc, and Sox4 bind unique, highly specific DNA motifs of 12, 12, and 10 base pairs, respectively. Footprinting with a deletion mutant of Ste11 reveals a novel interaction between the 3' base pairs of the extended DNA motif and amino acids C-terminal to the HMG domain. The sequence-specific interaction of Ste11 with these 3' base pairs contributes significantly to binding and bending of the DNA motif.","authors":"van Beest M, Dooijes D, van De Wetering M, Kjaerulff S, Bonvin A, Nielsen O, Clevers H","authors_abbrev":"van Beest M et al.","pubmed_publication_date":"01 Sep 2000","pubmed_entrez_date":"2000-06-27","publication_year":"2000","canto_session_key":"465139f68bfd6a53","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 14:26:43","canto_approved_date":"2022-02-07 14:38:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-10 10:17:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPBC23G7.09"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-06-10"},{"uniquename":"PMID:5955982","title":"Osmotic remedial and osmotic sensitive mutants of Schizosaccharomyces pombe.","citation":"Experientia 1966 Apr 15;22(4):216-8","abstract":"","authors":"Megnet R","authors_abbrev":"Megnet R","pubmed_publication_date":"15 Apr 1966","pubmed_entrez_date":"1966-04-15","publication_year":"1966","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2297790","title":"Snap helix with knob and hole: essential repeats in S. pombe nuclear protein nuc2+.","citation":"Cell 1990 Jan 26;60(2):319-28","abstract":"The S. pombe nuc2+ gene is required for mitotic chromosome disjunction. Its mutation arrests mitosis at the metaphase. The gene product is present in the nuclear scaffold-like fraction. The nuc2+ protein contains a domain, separated from ten 34 amino acid repeat segments, that is capable of binding AT-rich DNA in vitro. The ts mutation resides in one of the 34 amino acid repeats. Circular dichroism, limited proteolysis of the repeats, and model fitting indicate the presence of helical segments connected by protease-sensitive hinges. We propose that these repeats form a novel secondary structure (snap helix) having \"knob and hole\" helix-associating motifs. The packing of the snap helices would be stabilized by the bonding between the hydrophobic amino acids surrounding the knobs and holes. The nuc2+ protein may in one way bind to DNA and in another way mutually associate to form a part of the chromosome scaffold.","authors":"Hirano T, Kinoshita N, Morikawa K, Yanagida M","authors_abbrev":"Hirano T et al.","pubmed_publication_date":"26 Jan 1990","pubmed_entrez_date":"1990-01-26","publication_year":"1990","canto_session_key":"86aee7c359360302","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-05-13 13:00:45","canto_approved_date":"2022-02-02 16:16:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-13 13:00:39","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.01c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-13"},{"uniquename":"PMID:10805744","title":"Cpc2, a fission yeast homologue of mammalian RACK1 protein, interacts with Ran1 (Pat1) kinase To regulate cell cycle progression and meiotic development.","citation":"Mol Cell Biol 2000 Jun;20(11):4016-27","abstract":"The Schizosaccharomyces pombe ran1/pat1 gene regulates the transition between mitosis and meiosis. Inactivation of Ran1 (Pat1) kinase is necessary and sufficient for cells to exit the cell cycle and undergo meiosis. The yeast two-hybrid interaction trap was used to identify protein partners for Ran1/Pat1. Here we report the identification of one of these, Cpc2. Cpc2 encodes a homologue of RACK1, a WD protein with homology to the beta subunit of heterotrimeric G proteins. RACK1 is a highly conserved protein, although its function remains undefined. In mammalian cells, RACK1 physically associates with some signal transduction proteins, including Src and protein kinase C. Fission yeast cells containing a cpc2 null allele are viable but cell cycle delayed. cpc2Delta cells fail to accumulate in G(1) when starved of nitrogen. This leads to defects in conjugation and meiosis. Copurification studies show that although Cpc2 and Ran1 (Pat1) physically associate, Cpc2 does not alter Ran1 (Pat1) kinase activity in vitro. Using a Ran1 (Pat1) fusion to green fluorescent protein, we show that localization of the kinase is impaired in cpc2Delta cells. Thus, in parallel with the proposed role of RACK1 in mammalian cells, fission yeast cpc2 may function as an anchoring protein for Ran1 (Pat1) kinase. All defects associated with loss of cpc2 are reversed in cells expressing mammalian RACK1, demonstrating that the fission yeast and mammalian gene products are indeed functional homologues.","authors":"McLeod M, Shor B, Caporaso A, Wang W, Chen H, Hu L","authors_abbrev":"McLeod M et al.","pubmed_publication_date":"Jun 2000","pubmed_entrez_date":"2000-05-11","publication_year":"2000","canto_session_key":"2448c15f14dc6041","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-10 22:21:44","canto_approved_date":"2022-01-31 12:04:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-09 11:17:26","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":3,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC8C9.03","SPBC19C2.05","SPAC6B12.15","SPBC19C7.03"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-06-10"},{"uniquename":"PMID:27388936","title":"Disruption of snRNP biogenesis factors Tgs1 and pICln induces phenotypes that mirror aspects of SMN-Gemins complex perturbation in Drosophila, providing new insights into spinal muscular atrophy.","citation":"Neurobiol Dis 2016 Oct;94:245-58","abstract":"The neuromuscular disorder, spinal muscular atrophy (SMA), results from insufficient levels of the survival motor neuron (SMN) protein. Together with Gemins 2-8 and Unrip, SMN forms the large macromolecular SMN-Gemins complex, which is known to be indispensable for chaperoning the assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs). It remains unclear whether disruption of this function is responsible for the selective neuromuscular degeneration in SMA. In the present study, we first show that loss of wmd, the Drosophila Unrip orthologue, has a negative impact on the motor system. However, due to lack of a functional relationship between wmd/Unrip and Gemin3, it is likely that Unrip joined the SMN-Gemins complex only recently in evolution. Second, we uncover that disruption of either Tgs1 or pICln, two cardinal players in snRNP biogenesis, results in viability and motor phenotypes that closely resemble those previously uncovered on loss of the constituent members of the SMN-Gemins complex. Interestingly, overexpression of both factors leads to motor dysfunction in Drosophila, a situation analogous to that of Gemin2. Toxicity is conserved in the yeast S. pombe where pICln overexpression induces a surplus of Sm proteins in the cytoplasm, indicating that a block in snRNP biogenesis is partly responsible for this phenotype. Importantly, we show a strong functional relationship and a physical interaction between Gemin3 and either Tgs1 or pICln. We propose that snRNP biogenesis is the pathway connecting the SMN-Gemins complex to a functional neuromuscular system, and its disturbance most likely leads to the motor dysfunction that is typical in SMA.","doi":"10.1016/j.nbd.2016.06.015","authors":"Borg RM, Fenech Salerno B, Vassallo N, Bordonne R, Cauchi RJ","authors_abbrev":"Borg RM et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-07-09","publication_year":"2016","canto_session_key":"635d1ba383ac123c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-08-02 19:48:17","canto_approved_date":"2023-09-06 03:57:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-07-30 05:40:47","canto_added_date":"2016-07-10 00:15:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26A3.08","SPAC2G11.08c","SPAC2G11.15c","SPAC1610.01"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2016-08-02"},{"uniquename":"PMID:38103546","title":"Anillin-related Mid1 as an adaptive and multimodal contractile ring anchoring protein: A simulation study.","citation":"Structure 2023 Dec 12;","abstract":"Cytokinesis of animal and fungi cells depends crucially on the anillin scaffold proteins. Fission yeast anillin-related Mid1 anchors cytokinetic ring precursor nodes to the membrane. However, it is unclear if both of its Pleckstrin Homology (PH) and C2 C-terminal domains bind to the membrane as monomers or dimers, and if one domain plays a dominant role. We studied Mid1 membrane binding with all-atom molecular dynamics near a membrane with yeast-like lipid composition. In simulations with the full C terminal region started away from the membrane, Mid1 binds through the disordered L3 loop of C2 in a vertical orientation, with the PH away from the membrane. However, a configuration with both C2 and PH initially bound to the membrane remains associated with the membrane. Simulations of C2-PH dimers show extensive asymmetric membrane contacts. These multiple modes of binding may reflect Mid1's multiple interactions with membranes, node proteins, and ability to sustain mechanical forces.","doi":"10.1016/j.str.2023.11.010","authors":"Hall AR, Choi YK, Im W, Vavylonis D","authors_abbrev":"Hall AR et al.","pubmed_publication_date":"12 Dec 2023","pubmed_entrez_date":"2023-12-16","publication_year":"2023","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2023-12-18 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26151635","title":"Determination of Temporal Order among the Components of an Oscillatory System.","citation":"PLoS One 2015;10(7):e0124842","abstract":"Oscillatory systems in biology are tightly regulated process where the individual components (e.g. genes) express in an orderly manner by virtue of their functions. The temporal order among the components of an oscillatory system may potentially be disrupted for various reasons (e.g. environmental factors). As a result some components of the system may go out of order or even cease to participate in the oscillatory process. In this article, we develop a novel framework to evaluate whether the temporal order is unchanged in different populations (or experimental conditions). We also develop methodology to estimate the order among the components with a suitable notion of \"confidence.\" Using publicly available data on S. pombe, S. cerevisiae and Homo sapiens we discover that the temporal order among the genes cdc18; mik1; hhf1; hta2; fkh2 and klp5 is evolutionarily conserved from yeast to humans.","doi":"10.1371/journal.pone.0124842","authors":"Barragán S, Rueda C, Fernández MA, Peddada SD","authors_abbrev":"Barragán S et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-07-08","publication_year":"2015","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2015-07-09 00:21:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPD249","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8462094","title":"High resolution cosmid and P1 maps spanning the 14 Mb genome of the fission yeast S. pombe.","citation":"Cell 1993 Apr 09;73(1):109-20","abstract":"Gridded on high density filters, a P1 genomic library of 17-fold coverage and a cosmid library of 8 genome equivalents, both made from S. pombe strain 972h-, were ordered by hybridizing genetic markers and individual clones from the two libraries. Yeast artificial chromosome (YAC) clones covering the entire genome were used to subdivide the libraries, and hybridization of short oligonucleotides and DNA pools made from randomly selected cosmids provided further mapping information. Restriction digests were generated as an independent confirmation of the clone order. The high resolution clone map was aligned to the genetic map and the physical Notl and YAC maps. The usefulness of the various mapping techniques and cloning procedures could be assessed upon the different data sets.","authors":"Hoheisel JD, Maier E, Mott R, McCarthy L, Grigoriev AV, Schalkwyk LC, Nizetic D, Francis F, Lehrach H","authors_abbrev":"Hoheisel JD et al.","pubmed_publication_date":"09 Apr 1993","pubmed_entrez_date":"1993-04-09","publication_year":"1993","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11884512","title":"Cell-cycle-dependent localisation of Ulp1, a Schizosaccharomyces pombe Pmt3 (SUMO)-specific protease.","citation":"J Cell Sci 2002 Mar 15;115(Pt 6):1113-22","abstract":"We report here on the characterisation of Ulp1, a component of the SUMO modification process in S. pombe. Recombinant S. pombe Ulp1 has de-sumoylating activity; it is involved in the processing of Pmt3 (S. pombe SUMO) and can, to a limited extent, remove Pmt3 from modified targets in S. pombe cell extracts. ulp1 is not essential for cell viability, but cells lacking the gene display severe cell and nuclear abnormalities. ulp1-null (ulp1.d) cells are sensitive to ultraviolet radiation in a manner similar to rad31.d and hus5.62, which have mutations in one subunit of the activator and the conjugator for the ubiquitin-like protein SUMO respectively. However ulp1.d cells are less sensitive to ionising radiation and hydroxyurea (HU) than are rad31.d and hus5.62. ulp1-null cells are defective in processing precursor Pmt3 and display reduced levels of Pmt3 conjugates compared with wild-type cells. The slow growth phenotype of ulp1 null cells is not substantially rescued by over-expression of the mature form of Pmt3 (Pmt3-GG), suggesting that the de-conjugating activity of Ulp1 is required for normal cell cycle progression. During the S and G2 phases of the cell cycle the Ulp1 protein is localised to the nuclear periphery. However, during mitosis the pattern of staining alters, and during anaphase, Ulp1 is observed within the nucleus. Ulp1 localisation at the nuclear periphery is generally re-established by the time of septation (S phase).","authors":"Taylor DL, Ho JC, Oliver A, Watts FZ","authors_abbrev":"Taylor DL et al.","pubmed_publication_date":"15 Mar 2002","pubmed_entrez_date":"2002-03-09","publication_year":"2002","canto_session_key":"2b478b09a3eb713b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-11-01 21:31:31","canto_approved_date":"2023-03-11 09:27:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-07-19 20:00:56","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.13","SPBC365.06","SPBC19G7.09"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2017-11-01"},{"uniquename":"PMID:7937842","title":"Negative regulation of mitosis in fission yeast by catalytically inactive pyp1 and pyp2 mutants.","citation":"Proc Natl Acad Sci U S A 1994 Oct 11;91(21):10084-8","abstract":"The Schizosaccharomyces pombe genes pyp1+ and pyp2+ encode protein tyrosine phosphatases (PTPases) that act as negative regulators of mitosis upstream of the wee1+/mik1+ pathway. Here we provide evidence that pyp1+ and pyp2+ function independently of cdr1+(nim1+) in the inhibition of mitosis and that the wee1 kinase is not a direct substrate of either PTPase. In a pyp1::ura4 cdc25-22 genetic background, overexpression of either the N-terminal domain of pyp1+ or a catalytically inactive mutant, pyp1C470S, causes cell cycle arrest. This phenotype reverses the suppression of a cdc25 temperature-sensitive mutation at 35 degrees C caused by a pyp1 disruption. Furthermore, pyp1C470S and a catalytically inactive mutant of pyp2, pyp2C630S, induce mitotic delay as do their wild-type counterparts. Analysis of pyp1+ and pyp2+ further reveals that in vitro PTPase activity of pyp1 and pyp2, as well as their biological activity, is dependent on the presence of N-terminal sequences that are not normally considered part of PTPase catalytic domains.","authors":"Hannig G, Ottilie S, Erikson RL","authors_abbrev":"Hannig G et al.","pubmed_publication_date":"11 Oct 1994","pubmed_entrez_date":"1994-10-11","publication_year":"1994","canto_session_key":"63e0144a077da09e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-10-31 16:41:32","canto_approved_date":"2024-04-04 11:16:06","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2014-08-07 09:41:11","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":35,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19D5.01","SPAC644.06c","SPAC26F1.10c","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-10-31"},{"uniquename":"EMBL:AU011777","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9237993","title":"Purification and characterization of a CENP-B homologue protein that binds to the centromeric K-type repeat DNA of Schizosaccharomyces pombe.","citation":"Proc Natl Acad Sci U S A 1997 Aug 05;94(16):8427-32","abstract":"We have purified and characterized a novel 60-kDa protein that binds to centromeric K-type repeat DNA from Schizosaccharomyces pombe. This protein was initially purified by its ability to bind to the autonomously replicating sequence 3002 DNA. Cloning of the gene encoding this protein revealed that it possesses significant homology to the mammalian centromere DNA-binding protein CENP-B and S. pombe Abp1, and this gene was designated as cbh+ (CENP-B homologue). Cbh protein specifically interacts in vitro with the K-type repeat DNA, which is essential for centromere function. The Cbh-binding consensus sequence was determined by DNase I footprinting assays as PyPuATATPyPuTA, featuring an inverted repeat of the first four nucleotides. Based on its binding activity to centromeric DNA and homology to centromere proteins, we suggest that this protein may be a functional homologue of the mammalian CENP-B in S. pombe.","authors":"Lee JK, Huberman JA, Hurwitz J","authors_abbrev":"Lee JK et al.","pubmed_publication_date":"05 Aug 1997","pubmed_entrez_date":"1997-08-05","publication_year":"1997","canto_session_key":"eda2f671f89a9196","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-04-29 21:31:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-29 19:09:26","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9E9.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-29"},{"uniquename":"EMBL:SPD261","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17559414","title":"Functional characterization of the phosphorelay protein Mpr1p from Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2007 Sep;7(6):912-21","abstract":"Histidine-containing phosphotransfer (HPt) proteins play an essential role in multistep histidine-aspartate phosphorelay signal transduction systems in prokaryotes and eukaryotes. The putative HPt protein in Schizosaccharomyces pombe, Mpr1p (also known as Spy1p), is a 295 amino acid protein that appears to be composed of more than one functional domain. The amino acid sequence of the N-terminal region of Mpr1p lacks homology to other known proteins, whereas the C-terminal domain is predicted to have structural similarity to the Ypd1p HPt protein from Saccharomyces cerevisiae. This study provides both in vitro and in vivo evidence that the C-terminal domain of Mpr1p indeed functions as an HPt protein in shuttling phosphoryl groups from one response regulator domain to another. Furthermore, we find that various deletions of the N-terminal region diminish both the phosphotransfer activity of Mpr1p and its affinity for response regulator domains, suggesting a possible role for the N-terminal domain in HPt-response regulator domain interactions.","authors":"Tan H, Janiak-Spens F, West AH","authors_abbrev":"Tan H et al.","pubmed_publication_date":"Sep 2007","pubmed_entrez_date":"2007-06-15","publication_year":"2007","canto_session_key":"e6d7e22d7df32487","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-08-04 11:06:47","canto_approved_date":"2022-03-15 12:21:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-22 13:21:19","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC74.06","SPAC27E2.09","SPAC8C9.14","SPBC725.02","SPBC887.10","SPAC1834.08"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2017-08-04"},{"uniquename":"PMID:9450030","title":"Lithium affects the ultradian clock of Schizosaccharomyces pombe by inhibition of inositol monophosphatase.","citation":"Biochem Soc Trans 1997 Nov;25(4):S602","abstract":"","authors":"Kippert F","authors_abbrev":"Kippert F","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-02-05","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12637515","title":"Physical and functional interaction of the yeast corepressor Tup1 with mRNA 5'-triphosphatase.","citation":"J Biol Chem 2003 May 23;278(21):18895-901","abstract":"The Tup1-Ssn6 complex is an important corepressor in Saccharomyces cerevisiae that inhibits transcription through interactions with the basal transcription machinery and by remodeling chromatin. In a two-hybrid screen for factors that interact with the Schizosaccharomyces pombe Tup1 ortholog, Tup11, we isolated the pct1+ cDNA. The pct1+ gene encodes an mRNA 5'-triphosphatase, which catalyzes the first step of mRNA capping reactions. Pct1 did not interact with the S. pombe Ssn6 ortholog. In vitro glutathione S-transferase pull-down experiments revealed that Pct1 binds to the WD repeat regions of Tup11 and the functionally redundant Tup12 protein. Similarly, the S. cerevisiae Tup1 protein associates with the mRNA 5'-triphosphatase encoded by the CET1 gene. The highly conserved C-terminal domain of Cet1 interacts with Tup1 in vitro, and Tup1-Ssn6 complexes co-purify with the Cet1 protein, indicating that in vivo interactions also occur between these proteins. Over-expression of CET1 compromised repression of an MFA2-lacZ reporter gene that is subject to Tup1-Ssn6 repression. These genetic and biochemical interactions between Tup1-Ssn6 and Cet1 indicate that the capping enzyme associated with RNA polymerase II is a target of the corepressor complex.","authors":"Mukai Y, Davie JK, Dent SY","authors_abbrev":"Mukai Y et al.","pubmed_publication_date":"23 May 2003","pubmed_entrez_date":"2003-03-15","publication_year":"2003","canto_session_key":"f599ba15f58402d0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-14 15:24:53","canto_approved_date":"2022-02-07 14:31:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-14 15:24:46","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.04","SPAC630.14c","SPAC18B11.10"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-01-14"},{"uniquename":"PMID:27518095","title":"Active Center Control of Termination by RNA Polymerase III and tRNA Gene Transcription Levels In Vivo.","citation":"PLoS Genet 2016 Aug;12(8):e1006253","abstract":"The ability of RNA polymerase (RNAP) III to efficiently recycle from termination to reinitiation is critical for abundant tRNA production during cellular proliferation, development and cancer. Yet understanding of the unique termination mechanisms used by RNAP III is incomplete, as is its link to high transcription output. We used two tRNA-mediated suppression systems to screen for Rpc1 mutants with gain- and loss- of termination phenotypes in S. pombe. 122 point mutation mutants were mapped to a recently solved 3.9 Å structure of yeast RNAP III elongation complex (EC); they cluster in the active center bridge helix and trigger loop, as well as the pore and funnel, the latter of which indicate involvement of the RNA cleavage domain of the C11 subunit in termination. Purified RNAP III from a readthrough (RT) mutant exhibits increased elongation rate. The data strongly support a kinetic coupling model in which elongation rate is inversely related to termination efficiency. The mutants exhibit good correlations of terminator RT in vitro and in vivo, and surprisingly, amounts of transcription in vivo. Because assessing in vivo transcription can be confounded by various parameters, we used a tRNA reporter with a processing defect and a strong terminator. By ruling out differences in RNA decay rates, the data indicate that mutants with the RT phenotype synthesize more RNA than wild type cells, and than can be accounted for by their increased elongation rate. Finally, increased activity by the mutants appears unrelated to the RNAP III repressor, Maf1. The results show that the mobile elements of the RNAP III active center, including C11, are key determinants of termination, and that some of the mutations activate RNAP III for overall transcription. Similar mutations in spontaneous cancer suggest this as an unforeseen mechanism of RNAP III activation in disease.","doi":"10.1371/journal.pgen.1006253","authors":"Rijal K, Maraia RJ","authors_abbrev":"Rijal K et al.","pubmed_publication_date":"Aug 2016","pubmed_entrez_date":"2016-08-13","publication_year":"2016","canto_session_key":"8e39d3b94517bf64","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-08-17 00:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8709952","title":"The genetics of the repair of 5-azacytidine-mediated DNA damage in the fission yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1996 Jun 24;251(4):483-92","abstract":"We have recently demonstrated that Schizosaccharomyces pombe cells treated with the nucleoside analogue 5-azacytidine (5-azaC) require previously characterised G2 checkpoint mechanisms for survival. Here we present a survey of known DNA repair mutations which defines those genes required for survival in the presence of 5-azaC. Using a combination of single-mutant and epistasis analyses we find that the excision, mismatch and recombinational repair pathways are all required in some degree for the repair of 5-azaC-mediated DNA damage. There are distinct differences in the epistatic interactions of several of the repair mutations with respect to 5-azaC-mediated DNA damage relative to UV-mediated DNA damage.","authors":"Hegde V, McFarlane RJ, Taylor EM, Price C","authors_abbrev":"Hegde V et al.","pubmed_publication_date":"24 Jun 1996","pubmed_entrez_date":"1996-06-24","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPAC2G11.12","SPCC970.01","SPBC3E7.08c","SPAC13G6.01c"],"gene_count":5,"ltp_gene_count":4},{"uniquename":"PMID:31936296","title":"Protein Phosphatases in G1 Regulation.","citation":"Int J Mol Sci 2020 Jan 08;21(2)","abstract":"Eukaryotic cells make the decision to proliferate, to differentiate or to cease dividing during G1, before passage through the restriction point or Start. Keeping cyclin-dependent kinase (CDK) activity low during this period restricts commitment to a new cell cycle and is essential to provide the adequate timeframe for the sensing of environmental signals. Here, we review the role of protein phosphatases in the modulation of CDK activity and as the counteracting force for CDK-dependent substrate phosphorylation, in budding and fission yeast. Moreover, we discuss recent findings that place protein phosphatases in the interface between nutritional signalling pathways and the cell cycle machinery.","doi":"10.3390/ijms21020395","authors":"Martín R, Stonyte V, Lopez-Aviles S","authors_abbrev":"Martín R et al.","pubmed_publication_date":"08 Jan 2020","pubmed_entrez_date":"2020-01-16","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9092661","title":"Characterization of the alternative excision repair pathway of UV-damaged DNA in Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1997 Apr 15;25(8):1553-8","abstract":"Schizosaccharomyces pombe cells deficient in nucleotide excision repair (NER) are still able to remove photoproducts from cellular DNA, showing that there is a second pathway for repair of UV damage in this organism. We have characterized this repair pathway by cloning and disruption of the genomic gene encoding UV damage endonuclease (UVDE). Although uvde gene disruptant cells are only mildly UV sensitive, a double disruptant of uvde and rad13 (a S. pombe mutant defective in NER) was synergistically more sensitive than either single disruptant and was unable to remove any photoproducts from cellular DNA. Analysis of the kinetics of photoproduct removal in different mutants showed that the UVDE-mediated pathway operates much more rapidly than NER. In contrast to a previous report, our genetic analysis showed that rad12 and uvde are not the same gene. Disruption of the rad2 gene encoding a structure- specific flap endonuclease makes cells UV sensitive, but much of this sensitivity is not observed if the uvde gene is also disrupted. Further genetic and immunochemical analyses suggest that DNA incised by UVDE is processed by two separate mechanisms, one dependent and one independent of flap endonuclease.","authors":"Yonemasu R, McCready SJ, Murray JM, Osman F, Takao M, Yamamoto K, Lehmann AR, Yasui A","authors_abbrev":"Yonemasu R et al.","pubmed_publication_date":"15 Apr 1997","pubmed_entrez_date":"1997-04-15","publication_year":"1997","canto_session_key":"ef012afa9234a01e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sumir Pandit","canto_first_approved_date":"2023-11-26 19:43:16","canto_approved_date":"2023-12-21 11:23:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-24 15:41:57","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Sumir Pandit","community_curator":true,"annotation_count":5,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G6.06c","SPBC3E7.08c","SPBC19C7.09c","SPAC2G11.12"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2023-11-26"},{"uniquename":"PMID:20637317","title":"Whole-cell biotransformation assay for investigation of the human drug metabolizing enzyme CYP3A7.","citation":"Biochim Biophys Acta 2011 Jan;1814(1):161-7","abstract":"The cytochrome P450 isoform CYP3A7 (wildtype) is the major form of CYP in human fetal liver. Since it is not exclusively expressed in the fetus but also in a significant number of adults, CYP3A7 has been moving into the focus of investigation on adverse drug reactions and interindividual differences in drug metabolism in the last few years. In addition, CYP3A7 is overexpressed in hepatocellular carcinoma (HCC), where it contributes to the elimination of drugs. We here report the development of a convenient and reliable whole-cell system for testing CYP3A7 activity using recombinant fission yeast. As expected, catalytic properties of wild type CYP3A7.1 and its polymorphic form CYP3A7.2 towards DHEA and testosterone resembled those reported previously. Interestingly, both isoforms of CYP3A7 did not metabolize the anti-cancer drug sorafenib (which is approved for the treatment of HCC), while CYP3A4 produced the N-oxide in our system, as expected. This finding suggests that CYP3A7 activity does not influence the effectiveness of this anti-cancer drug against HCC. Furthermore, CYP3A7-expressing fission yeast cells specifically converted a luciferin-derivate (luciferin-PFBE) to a luminescent product and this activity can conveniently be monitored by spectrometry, which allowed the determination of IC₅₀-values for the broad-range P450 inhibitors econazole and miconazole, respectively. We believe that these new tools for a fast and easy investigation of substrates and inhibitors of human CYP3A7 will contribute to the gain of important insights for drug metabolism, efficacy and safety.","doi":"10.1016/j.bbapap.2010.07.011","authors":"Neunzig I, Drăgan CA, Widjaja M, Schwaninger AE, Peters FT, Maurer HH, Bureik M","authors_abbrev":"Neunzig I et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-07-20","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15802518","title":"Dynein promotes achiasmate segregation in Schizosaccharomyces pombe.","citation":"Genetics 2005 Jun;170(2):581-90","abstract":"Most organisms use crossovers (chiasmata) to maintain physical connections between homologous chromosomes that ensure their proper segregation at the first meiotic division. The fission yeast Schizosaccharomyces pombe has a residual ability to segregate homologous chromosomes in the absence of meiotic recombination (achiasmate segregation). Using cytologically tagged chromosomes, we established a role for the microtubule motor dynein in meiotic chromosome segregation. Dhc1, the motor subunit of dynein, is required for chromosome segregation in both the presence and the absence of recombination. Dlc1, a member of the Tctex-1 dynein light-chain family, preferentially affects the segregation of achiasmate chromosomes. Dlc1 is the first identified protein, outside of Drosophila, that preferentially affects achiasmate chromosome segregation. We discuss possible roles of the dynein motor in this process.","authors":"Davis L, Smith GR","authors_abbrev":"Davis L et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-04-02","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:49","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1805.08","SPAC1093.06c","SPAC17A5.11"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:3601654","title":"A novel sequence common to the centromere regions of Schizosaccharomyces pombe chromosomes.","citation":"Nucleic Acids Res 1987 Jun 25;15(12):4705-15","abstract":"An approximately 4 kb long sequence (designated dh) is located in the centromere regions of all three chromosomes of S. pombe. There is one copy each of dh per centromere in chromosomes I and II and multiples in the centromere of chromosome III. Nucleotide sequence determination shows that dhI and dhII are highly homologous. A part of the sequence (ca. 300-400 bp) contains short direct repeats, otherwise dh is in general internally non-repetitious. Although there are three segmental deletions (total 821 bp) and two insertions (27 bp) in dhII (an 80% overall homology to dhI), there are only nine substitutions between dhI and dhII in the remaining 3980 bp, giving a 99.77% homology. The substitutions are restricted to the non-repetitious domains and are only of the pyrimidine-pyrimidine or purine-purine types. A possible conformational role of dh is discussed.","authors":"Nakaseko Y, Kinoshita N, Yanagida M","authors_abbrev":"Nakaseko Y et al.","pubmed_publication_date":"25 Jun 1987","pubmed_entrez_date":"1987-06-25","publication_year":"1987","canto_session_key":"9a2813671be3bfd1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:23:00","canto_approved_date":"2018-12-22 20:23:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 20:22:13","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:23516381","title":"DNA topoisomerase III localizes to centromeres and affects centromeric CENP-A levels in fission yeast.","citation":"PLoS Genet 2013;9(3):e1003371","abstract":"Centromeres are specialized chromatin regions marked by the presence of nucleosomes containing the centromere-specific histone H3 variant CENP-A, which is essential for chromosome segregation. Assembly and disassembly of nucleosomes is intimately linked to DNA topology, and DNA topoisomerases have previously been implicated in the dynamics of canonical H3 nucleosomes. Here we show that Schizosaccharomyces pombe Top3 and its partner Rqh1 are involved in controlling the levels of CENP-A(Cnp1) at centromeres. Both top3 and rqh1 mutants display defects in chromosome segregation. Using chromatin immunoprecipitation and tiling microarrays, we show that Top3, unlike Top1 and Top2, is highly enriched at centromeric central domains, demonstrating that Top3 is the major topoisomerase in this region. Moreover, centromeric Top3 occupancy positively correlates with CENP-A(Cnp1) occupancy. Intriguingly, both top3 and rqh1 mutants display increased relative enrichment of CENP-A(Cnp1) at centromeric central domains. Thus, Top3 and Rqh1 normally limit the levels of CENP-A(Cnp1) in this region. This new role is independent of the established function of Top3 and Rqh1 in homologous recombination downstream of Rad51. Therefore, we hypothesize that the Top3-Rqh1 complex has an important role in controlling centromere DNA topology, which in turn affects the dynamics of CENP-A(Cnp1) nucleosomes.","doi":"10.1371/journal.pgen.1003371","authors":"Norman-Axelsson U, Durand-Dubief M, Prasad P, Ekwall K","authors_abbrev":"Norman-Axelsson U et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-03-22","publication_year":"2013","canto_session_key":"0ff8fcd8e6096af8","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.12","SPAC644.14c","SPBC16G5.12c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:15385632","title":"Requirements of fission yeast septins for complex formation, localization, and function.","citation":"Mol Biol Cell 2004 Dec;15(12):5551-64","abstract":"Septins are GTP binding proteins important for cytokinesis in many eukaryotes. The Schizosaccaromyces pombe genome sequence predicts orthologues of four of five Saccharomyces cerevisiae septins involved in cytokinesis and these are named Spns1-4p. That spns1-4 are not essential genes permitted the application of a combined genetic and proteomics approach to determine their functional relationships. Our findings indicate that Spns1-4p are present throughout interphase as a diffusely localized approximately 8.5S complex containing two copies of each septin linked together as a chain in the order Spn3p-Spn4p-Spn1p-Spn2p. Septin recruitment to the medial region of the cell is genetically separable from ring formation, and whereas it is normally restricted to mitosis, it can be promoted without activation of the mitotic cell cycle machinery. Coalescence into ring structures requires Spn1p and Spn4p associate with at least one other septin subunit and the expression of Mid2p that is normally restricted to mitosis. This study establishes the functional requirements for septin complex organization in vivo.","authors":"An H, Morrell JL, Jennings JL, Link AJ, Gould KL","authors_abbrev":"An H et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-09-24","publication_year":"2004","canto_session_key":"94d96dad24c762d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-06-15 09:01:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-06-15 08:59:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":49,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9G1.11c","SPBC16A3.01","SPAC821.06","SPAC4F10.11","SPCC4B3.15"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-06-15"},{"uniquename":"PMID:23365689","title":"Cellular robustness conferred by genetic crosstalk underlies resistance against chemotherapeutic drug doxorubicin in fission yeast.","citation":"PLoS One 2013;8(1):e55041","abstract":"Doxorubicin is an anthracycline antibiotic that is among one of the most commonly used chemotherapeutic agents in the clinical setting. The usage of doxorubicin is faced with many problems including severe side effects and chemoresistance. To overcome these challenges, it is important to gain an understanding of the underlying molecular mechanisms with regards to the mode of action of doxorubicin. To facilitate this aim, we identified the genes that are required for doxorubicin resistance in the fission yeast Schizosaccharomyces pombe. We further demonstrated interplay between factors controlling various aspects of chromosome metabolism, mitochondrial respiration and membrane transport. In the nucleus we observed that the subunits of the Ino80, RSC, and SAGA complexes function in the similar epistatic group that shares significant overlap with the homologous recombination genes. However, these factors generally act in synergistic manner with the chromosome segregation regulator DASH complex proteins, possibly forming two major arms for regulating doxorubicin resistance in the nucleus. Simultaneous disruption of genes function in membrane efflux transport or the mitochondrial respiratory chain integrity in the mutants defective in either Ino80 or HR function resulted in cumulative upregulation of drug-specific growth defects, suggesting a rewiring of pathways that synergize only when the cells is exposed to the cytotoxic stress. Taken together, our work not only identified factors that are required for survival of the cells in the presence of doxorubicin but has further demonstrated that an extensive molecular crosstalk exists between these factors to robustly confer doxorubicin resistance.","doi":"10.1371/journal.pone.0055041","authors":"Tay Z, Eng RJ, Sajiki K, Lim KK, Tang MY, Yanagida M, Chen ES","authors_abbrev":"Tay Z et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-02-01","publication_year":"2013","canto_session_key":"b8a380167acb4791","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-07-16 15:50:26","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-07-16 16:02:25","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":91,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_23365689_phaf.tsv"}],"genes":["SPAC8E11.02c","SPBC4B4.03","SPAC144.02","SPCC16C4.20c","SPCC162.05","SPBC106.05c","SPBC4F6.10","SPBC27B12.10c","SPCC18.06c","SPAC16A10.05c","SPCC1259.03","SPCC757.10","SPCC1739.14","SPAC644.14c","SPBC28F2.10c","SPBC21B10.13c","SPAPB1A10.09","SPCC31H12.08c","SPBC146.12","SPBC32F12.08c","SPAC17H9.19c","SPAC3H8.05c","SPBC19G7.10c","SPCC23B6.05c","SPAC4F10.04","SPAC23H3.06","SPAC664.02c","SPBC18H10.02","SPCC576.12c","SPAC17G8.07","SPAC9E9.09c","SPBC16A3.07c","SPBC337.15c","SPBC2D10.13","SPCC18.02","SPBC215.03c","SPAC23G3.04","SPAC14C4.16","SPBC651.07","SPBC365.10","SPBC1105.10","SPBP8B7.22","SPAC23D3.09","SPBC106.04","SPAC13C5.07","SPCC777.13","SPAC23C11.08","SPCC1840.09","SPAC1687.12c","SPBC1604.02c","SPBC17A3.05c","SPAPB17E12.04c","SPBC947.14c","SPAC1805.07c","SPBC21C3.20c","SPAC6G9.14","SPAC144.06","SPAC10F6.08c","SPBC2F12.12c","SPAC2F7.07c","SPCC24B10.08c","SPAC2F3.11","SPCC16A11.07","SPCC338.08","SPCC1223.15c","SPCC663.03","SPCC1672.04c","SPBC32H8.07","SPBC2D10.16","SPBC18H10.04c","SPAPB1E7.02c","SPAC2C4.05","SPAC56F8.04c","SPAC29B12.08","SPAC823.10c","SPBC17D1.02","SPCC1259.04","SPAC1952.05","SPAC1B2.04","SPBC16H5.13","SPAC31G5.19","SPAC17H9.08","SPAC222.04c","SPBPJ4664.01","SPAC513.03","SPAC3C7.03c","SPCC417.02","SPBC1734.15","SPAC6B12.05c","SPAC15A10.03c","SPAC630.14c"],"gene_count":91,"ltp_gene_count":10,"approved_date":"2014-07-16"},{"uniquename":"PMID:5410810","title":"The production, by nitrous acid, of complete and mosaic mutations during defined nuclear stages in cells of Schizosaccharomyces pombe.","citation":"Mutat Res 1970 Jan;9(1):59-69","abstract":"","authors":"Abbondandolo A, Bonatti S","authors_abbrev":"Abbondandolo A et al.","pubmed_publication_date":"Jan 1970","pubmed_entrez_date":"1970-01-01","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20694152","title":"Dynamics of Kv1 channel transport in axons.","citation":"PLoS One 2010 Aug 04;5(8):e11931","abstract":"Concerted actions of various ion channels that are precisely targeted along axons are crucial for action potential initiation and propagation, and neurotransmitter release. However, the dynamics of channel protein transport in axons remain unknown. Here, using time-lapse imaging, we found fluorescently tagged Kv1.2 voltage-gated K(+) channels (YFP-Kv1.2) moved bi-directionally in discrete puncta along hippocampal axons. Expressing Kvbeta2, a Kv1 accessory subunit, markedly increased the velocity, the travel distance, and the percentage of moving time of these puncta in both anterograde and retrograde directions. Suppressing the Kvbeta2-associated protein, plus-end binding protein EB1 or kinesin II/KIF3A, by siRNA, significantly decreased the velocity of YFP-Kv1.2 moving puncta in both directions. Kvbeta2 mutants with disrupted either Kv1.2-Kvbeta2 binding or Kvbeta2-EB1 binding failed to increase the velocity of YFP-Kv1.2 puncta, confirming a central role of Kvbeta2. Furthermore, fluorescently tagged Kv1.2 and Kvbeta2 co-moved along axons. Surprisingly, when co-moving with Kv1.2 and Kvbeta2, EB1 appeared to travel markedly faster than its plus-end tracking. Finally, using fission yeast S. pombe expressing YFP-fusion proteins as reference standards to calibrate our microscope, we estimated the numbers of YFP-Kv1.2 tetramers in axonal puncta. Taken together, our results suggest that proper amounts of Kv1 channels and their associated proteins are required for efficient transport of Kv1 channel proteins along axons.","doi":"10.1371/journal.pone.0011931","authors":"Gu Y, Gu C","authors_abbrev":"Gu Y et al.","pubmed_publication_date":"04 Aug 2010","pubmed_entrez_date":"2010-08-10","publication_year":"2010","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10066548","title":"On growth and form: control of cell morphogenesis in fission yeast.","citation":"Curr Opin Microbiol 1998 Dec;1(6):712-8","abstract":"In the past year, we have gained considerable insight into the process of cell morphogenesis and the establishment of positional information in fission yeast. The highlights include a better understanding of the role of the microtubule cytoskeleton in the control of cell shape, as well as the identification of novel genes essential for the establishment of cell polarity and for the positioning of the site of cell division.","authors":"Verde F","authors_abbrev":"Verde F","pubmed_publication_date":"Dec 1998","pubmed_entrez_date":"1999-03-06","publication_year":"1998","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11015731","title":"Construction of fission yeast vectors with a novel selection strategy that allows their use in wild-type fission yeasts.","citation":"Yeast 2000 Oct;16(14):1345-50","abstract":"Novel vectors that use the Pichia pastoris INO1 gene as a selectable marker and exploit the natural inositol auxotrophy of the fission yeast are described. These plasmids also contained other features desirable in a plasmid cloning vector. These plasmids were evaluated in other species of Schizosaccharomyces and found to replicate autonomously in another variety of S. pombe, S. pombe var. malidevorans. These plasmids can be used for transformation of any wild-type S. pombe strain without the need for selection by induced auxotrophic mutations, or by selection by drug resistance markers, and should greatly assist genetic and molecular manipulations in these yeasts.","authors":"Ingavale SS, Sharma KG, Bachhawat AK","authors_abbrev":"Ingavale SS et al.","pubmed_publication_date":"Oct 2000","pubmed_entrez_date":"2000-10-04","publication_year":"2000","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11952833","title":"The gamma-tubulin complex protein Alp4 provides a link between the metaphase checkpoint and cytokinesis in fission yeast.","citation":"Genes Cells 2002 Apr;7(4):365-73","abstract":"The progression of cytokinesis requires cyclin B destruction by the anaphase promoting complex (APC/C) and, in fission yeast, activation of the septation initiation network (SIN) is also essential. The gamma-tubulin complex (gamma-TuC) localizes to the centrosome throughout the cell cycle and is directly involved in the organization of the mitotic spindle.\nWe have previously shown that the mutant defective in alp4+ (Spc97/GCP2) displays bipolar spindle defects due to a failure in the recruitment of the gamma-TuC on to the spindle pole body (SPB, the centrosome equivalent). Here we show that in these mutants the Mad2 checkpoint is activated, yet septation proceeds due to the untimely activation of the SIN. The Sid1 kinase, the downstream effector of the SIN, is recruited prematurely to both, instead of only one, of the SPBs, which triggers septation despite the presence of monopolar spindles. Remarkably, cyclin B levels, which would normally have declined, remain high at the SPB in septated mutant cells.\nWe propose a novel role of the gamma-TuC in inhibiting activation of the SIN until cyclin B is destroyed. Given the ubiquitous existence of the gamma-TuC, this mechanism may be conserved throughout evolution and function to couple cytokinesis to mitotic exit.","authors":"Vardy L, Fujita A, Toda T","authors_abbrev":"Vardy L et al.","pubmed_publication_date":"Apr 2002","pubmed_entrez_date":"2002-04-16","publication_year":"2002","canto_session_key":"dae563ad8708026c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-07-20 13:15:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-24 10:44:54","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC21.06c","SPBC582.03","SPAC9G1.09","SPBC365.15"],"gene_count":4,"ltp_gene_count":1,"approved_date":"2015-03-24"},{"uniquename":"PMID:29292846","title":"Lem2 is retained at the nuclear envelope through its interaction with Bqt4 in fission yeast.","citation":"Genes Cells 2018 Mar;23(3):122-135","abstract":"Inner nuclear membrane (INM) proteins are thought to play important roles in modulating nuclear organization and function through their interactions with chromatin. However, these INM proteins share redundant functions in metazoans that pose difficulties for functional studies. The fission yeast Schizosaccharomyces pombe exhibits a relatively small number of INM proteins, and molecular genetic tools are available to separate their redundant functions. In S. pombe, it has been reported that among potentially redundant INM proteins, Lem2 displays a unique genetic interaction with another INM protein, Bqt4, which is involved in anchoring telomeres to the nuclear envelope. Double mutations in the lem2 and bqt4 genes confer synthetic lethality during vegetative growth. Here, we show that Lem2 is retained at the nuclear envelope through its interaction with Bqt4, as the loss of Bqt4 results in the exclusive accumulation of Lem2 to the spindle pole body (SPB). An N-terminal nucleoplasmic region of Lem2 bears affinity to both Bqt4 and the SPB in a competitive manner. In contrast, the synthetic lethality of the lem2 bqt4 double mutant is suppressed by the C-terminal region of Lem2. These results indicate that the N-terminal and C-terminal domains of Lem2 show independent functions with respect to Bqt4.","doi":"10.1111/gtc.12557","authors":"Hirano Y, Kinugasa Y, Asakawa H, Chikashige Y, Obuse C, Haraguchi T, Hiraoka Y","authors_abbrev":"Hirano Y et al.","pubmed_publication_date":"Mar 2018","pubmed_entrez_date":"2018-01-03","publication_year":"2018","canto_session_key":"6ed5c1503e2a7ae8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yasuhiro Hirano","canto_first_approved_date":"2019-10-02 14:32:34","canto_approved_date":"2025-09-04 12:19:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-09-04 07:50:38","canto_added_date":"2018-01-04 01:15:17","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":22,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yasuhiro Hirano","community_curator":true,"annotation_count":4,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.10","SPAC18G6.10","SPAC14C4.05c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-10-02"},{"uniquename":"PMID:9552364","title":"The fission yeast Nim1/Cdr1 kinase: a link between nutritional state and cell cycle control.","citation":"Prog Cell Cycle Res 1995;1:207-14","abstract":"Close connections appear to exist between extra-cellular signals that regulate cell proliferation and the protein kinases that control the cell cycle machinery. The fission yeast nim1 kinase is an inducer of cdc2 kinase activity acting through the inhibition of wee1 kinase. Nim1 function is required for a correct cellular response to nutritional starvation. In the absence of nim1, starved cells are unable to decrease their size at mitosis, to arrest their cycle in G1 and to enter G0. Here, we review our current knowledge on the role and the regulation of nim1 in connecting cell cycle and nutritional pathways.","authors":"Belenguer P, Pelloquin L, Baldin V, Oustrin ML, Ducommun B","authors_abbrev":"Belenguer P et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19750511","title":"An improved strategy for tandem affinity purification-tagging of Schizosaccharomyces pombe genes.","citation":"Proteomics 2009 Oct;9(20):4825-8","abstract":"Tandem affinity purification (TAP) is a method that allows rapid purification of native protein complexes. We developed an improved technique to fuse the fission yeast genes with a TAP tag. Our technique is based on tagging constructs that contain regions homologous to the target gene cloned into vectors carrying a TAP tag. We used this technique to design strategies for TAP-tagging of predicted Schizosaccharomyces pombe genes (http://mendel.imp.ac.at/Pombe_tagging/). To validate the approach, we purified the proteins, which associated with two evolutionarily conserved proteins Swi5 and Sfr1 as well as three protein kinases Ksg1, Orb6 and Sid1.","doi":"10.1002/pmic.200800948","authors":"Cipak L, Spirek M, Novatchkova M, Chen Z, Rumpf C, Lugmayr W, Mechtler K, Ammerer G, Csaszar E, Gregan J","authors_abbrev":"Cipak L et al.","pubmed_publication_date":"Oct 2009","pubmed_entrez_date":"2009-09-15","publication_year":"2009","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:49","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25109267","title":"Suppression of ricinoleic acid toxicity by ptl2 overexpression in fission yeast Schizosaccharomyces pombe.","citation":"Appl Microbiol Biotechnol 2014 Nov;98(22):9325-37","abstract":"We previously succeeded to obtain a high content of ricinoleic acid (RA), a hydroxylated fatty acid with great values as a petrochemical replacement, in fission yeast Schizosaccharomyces pombe by introducing Claviceps purpurea oleate Δ12-hydroxylase gene (CpFAH12). Although the production was toxic to S. pombe cells, we identified plg7, encoding phospholipase A2, as a multicopy suppressor that restored the growth defect by removing RA from phospholipids and induced secretion of a part of the released free RA into culture media. In this study, we extended our analysis and examined the effect of triglyceride (TG) lipase overexpression on the tolerance to RA toxicity and RA productivity. S. pombe has three TG lipase genes, ptl1, ptl2, and ptl3, which have high protein sequence similarities to each other and to Saccharomyces cerevisiae counterparts TGL3, TGL4, and TGL5, but only ptl2 overexpression suppressed the growth defect induced by RA production, and the culture grown at 20 °C secreted free RA into media like plg7 overexpression. Suppression by ptl2 was independent of plg7, and a large amount of free RA was accumulated in the cells concomitant with the decrease in RA moieties in phospholipids. Furthermore, the suppression by ptl2 was attenuated by bromoenol lactone (BEL), a phospholipase A2 specific inhibitor, suggesting that Ptl2p may have phospholipase activity. Simultaneous overexpression of ptl2 and plg7 in the FAH12 integrant increased secretion and intracellular accumulation of RA 1.2- and 1.3-fold, respectively, compared to those with single overexpression of plg7 on day 10 at 20 °C.","doi":"10.1007/s00253-014-6006-y","authors":"Yazawa H, Ogiso M, Kumagai H, Uemura H","authors_abbrev":"Yazawa H et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-08-12","publication_year":"2014","canto_session_key":"f3e92e0c38be784b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-26 18:08:34","canto_approved_date":"2018-01-26 18:08:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-26 12:00:02","canto_added_date":"2014-08-13 00:15:26","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1786.01c","SPBC106.11c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-01-26"},{"uniquename":"PMID:15279790","title":"Claspin, a regulator of Chk1 in DNA replication stress pathway.","citation":"DNA Repair (Amst) 2004;3(8-9):1033-7","abstract":"Regulation of the vertebrate checkpoint kinase Chk1 involves several protein complexes including the recently identified protein Claspin. Claspin associates with Chk1 upon replication stress and DNA damage and is required for Chk1 activation in both Xenopus and human systems. More importantly, Claspin is involved in regulation of cell cycle checkpoints. Here, we discuss the emerging roles of Claspin in the Chk1 pathway and its functions in checkpoint control.","authors":"Chini CC, Chen J","authors_abbrev":"Chini CC et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-07-29","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-11-26 01:19:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18788459","title":"[Molecular basis of the formation and branch migration of Holliday recombination intermediates mediated by eukaryotic recombinases].","citation":"Tanpakushitsu Kakusan Koso 2008 Sep;53(11):1351-9","abstract":"","authors":"Murayama Y, Iwasaki H","authors_abbrev":"Murayama Y et al.","pubmed_publication_date":"Sep 2008","pubmed_entrez_date":"2008-09-16","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32755476","title":"Inhibition of cell membrane ingression at the division site by cell walls in fission yeast.","citation":"Mol Biol Cell 2020 Oct 01;31(21):2306-2314","abstract":"Eukaryotic cells assemble actomyosin rings during cytokinesis to function as force-generating machines to drive membrane invagination and to counteract the intracellular pressure and the cell surface tension. How the extracellular matrix affects actomyosin ring contraction has not been fully explored. While studying the  Schizosaccharomyces pombe  1,3-β-glucan-synthase mutant  cps1 -191, which is defective in division septum synthesis and arrests with a stable actomyosin ring, we found that weakening of the extracellular glycan matrix caused the generated spheroplasts to divide under the nonpermissive condition. This nonmedial slow division was dependent on a functional actomyosin ring and vesicular trafficking, but independent of normal septum synthesis. Interestingly, the high intracellular turgor pressure appears to play a minimal role in inhibiting ring contraction in the absence of cell wall remodeling in  cps1 -191 mutants, as decreasing the turgor pressure alone did not enable spheroplast division. We propose that during cytokinesis, the extracellular glycan matrix restricts actomyosin ring contraction and membrane ingression, and remodeling of the extracellular components through division septum synthesis relieves the inhibition and facilitates actomyosin ring contraction.","doi":"10.1091/mbc.E20-04-0245","authors":"Chew TG, Lim TC, Osaki Y, Huang J, Kamnev A, Hatano T, Osumi M, Balasubramanian MK","authors_abbrev":"Chew TG et al.","pubmed_publication_date":"01 Oct 2020","pubmed_entrez_date":"2020-08-07","publication_year":"2020","canto_session_key":"79254a1ac862de88","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-08-08 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24484667","title":"Microfabricated chambers as force sensors for probing forces of fungal growth.","citation":"Methods Cell Biol 2014;120:215-26","abstract":"The mechanical properties of fungal cells influence their growth, division, morphogenesis, and invasiveness. These cells are characterized by high internal turgor pressure contained by a stiff but elastic cell wall. In here, we describe simple and versatile methods to measure forces of fungal growth, turgor pressure, and elastic moduli of fungi cell wall, using microfabricated polydimethylsiloxane wells of varying stiffness as single cell force sensors. We demonstrate the strength of this method with the rod-shape fission yeast Schizosaccaromyces pombe and highlight how it may be implemented for studying mechanical properties of other walled cells.","doi":"10.1016/B978-0-12-417136-7.00014-8","authors":"Minc N","authors_abbrev":"Minc N","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-02-04","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37298423","title":"The Product of the Fission Yeast  fhl1  Gene Binds to the HomolE Box and Activates In Vitro Transcription of Ribosomal Protein Genes.","citation":"Int J Mol Sci 2023 May 30;24(11)","abstract":"Fission yeast ribosomal protein genes (RPGs) contain a HomolD box as a core promoter element required for transcription. Some of the RPGs also contain a consensus sequence named HomolE, located upstream of the HomolD box. The HomolE box acts as an upstream activating sequence (UAS), and it is able to activate transcription in RPG promoters containing a HomolD box. In this work, we identified a HomolE-binding protein (HEBP) as a polypeptide of 100 kDa, which was able to bind to the HomolE box in a Southwestern blot assay. The features of this polypeptide were similar to the product of the  fhl1  gene of fission yeast. The Fhl1 protein is the homolog of the FHL1 protein of budding yeast and possesses fork-head-associated (FHA) and fork-head (FH) domains. The product of the  fhl1  gene was expressed and purified from bacteria, and it was demonstrated that is able to bind the HomolE box in an electrophoretic mobility assay (EMSA), as well as being able to activate in vitro transcription from an RPG gene promoter containing HomolE boxes upstream of the HomolD box. These results indicate that the product of the  fhl1  gene of fission yeast can bind to the HomolE box, and it activates the transcription of RPGs.","doi":"10.3390/ijms24119472","authors":"Maldonado E, Morales-Pison S, Urbina F, Arias C, Castillo C, Jara L, Solari A","authors_abbrev":"Maldonado E et al.","pubmed_publication_date":"30 May 2023","pubmed_entrez_date":"2023-06-10","publication_year":"2023","canto_session_key":"d4c7f89946ff3a37","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-06-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26013808","title":"A mass spectrometry-based method for comprehensive quantitative determination of post-transcriptional RNA modifications: the complete chemical structure of Schizosaccharomyces pombe ribosomal RNAs.","citation":"Nucleic Acids Res 2015 Oct 15;43(18):e115","abstract":"We present a liquid chromatography-mass spectrometry (LC-MS)-based method for comprehensive quantitative identification of post-transcriptional modifications (PTMs) of RNA. We incorporated an in vitro-transcribed, heavy isotope-labeled reference RNA into a sample RNA solution, digested the mixture with a number of RNases and detected the post-transcriptionally modified oligonucleotides quantitatively based on shifts in retention time and the MS signal in subsequent LC-MS. This allowed the determination and quantitation of all PTMs in Schizosaccharomyces pombe ribosomal (r)RNAs and generated the first complete PTM maps of eukaryotic rRNAs at single-nucleotide resolution. There were 122 modified sites, most of which appear to locate at the interface of ribosomal subunits where translation takes place. We also identified PTMs at specific locations in rRNAs that were altered in response to growth conditions of yeast cells, suggesting that the cells coordinately regulate the modification levels of RNA.","doi":"10.1093/nar/gkv560","authors":"Taoka M, Nobe Y, Hori M, Takeuchi A, Masaki S, Yamauchi Y, Nakayama H, Takahashi N, Isobe T","authors_abbrev":"Taoka M et al.","pubmed_publication_date":"15 Oct 2015","pubmed_entrez_date":"2015-05-28","publication_year":"2015","canto_session_key":"07e36abbe47a5cfe","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-05-29 00:19:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17248776","title":"The Number of Chromosomes in SCHIZOSACCHAROMYCES POMBE: Light Microscopy of Stained Preparations.","citation":"Genetics 1977 Nov;87(3):491-7","abstract":"Chromosomes have been counted with the light microscope in fixed and stained preparations of Schizosaccharomyces pombe. The least ambiguous images were seen in zygotes fixed at meta-, ana- and telophase of meiosis II. They suggest that the haploid number of chromosomes in S. pombe is three.","authors":"Robinow CF","authors_abbrev":"Robinow CF","pubmed_publication_date":"Nov 1977","pubmed_entrez_date":"1977-11-01","publication_year":"1977","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28903054","title":"Mechanical Forces of Fission Yeast Growth.","citation":"Curr Biol 2014 Jun 16;24(12):1436","abstract":"","doi":"10.1016/j.cub.2014.05.054","authors":"Minc N, Boudaoud A, Chang F","authors_abbrev":"Minc N et al.","pubmed_publication_date":"16 Jun 2014","pubmed_entrez_date":"2017-09-14","publication_year":"2014","canto_session_key":"e8a8cd6d3cc9f389","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-09-16 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18036269","title":"Shaken not stirred: a global research cocktail served in Hinxton.","citation":"Genome Biol 2007;8(11):320","abstract":"A report of the 2007 Cold Spring Harbor Laboratory/Wellcome Trust Conference on Functional Genomics and Systems Biology, Hinxton, UK, 10-13 October 2007.","authors":"Marguerat S, Wilhelm BT, Bähler J","authors_abbrev":"Marguerat S et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-11-27","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15659644","title":"Fission yeast mto2p regulates microtubule nucleation by the centrosomin-related protein mto1p.","citation":"Mol Biol Cell 2005 Jun;16(6):3040-51","abstract":"From an insertional mutagenesis screen, we isolated a novel gene, mto2+, involved in microtubule organization in fission yeast. mto2Delta strains are viable but exhibit defects in interphase microtubule nucleation and in formation of the postanaphase microtubule array at the end of mitosis. The mto2Delta defects represent a subset of the defects displayed by cells deleted for mto1+ (also known as mod20+ and mbo1+), a centrosomin-related protein required to recruit the gamma-tubulin complex to cytoplasmic microtubule-organizing centers (MTOCs). We show that mto2p colocalizes with mto1p at MTOCs throughout the cell cycle and that mto1p and mto2p coimmunoprecipitate from cytoplasmic extracts. In vitro studies suggest that mto2p binds directly to mto1p. In mto2Delta mutants, although some aspects of mto1p localization are perturbed, mto1p can still localize to spindle pole bodies and the cell division site and to \"satellite\" particles on interphase microtubules. In mto1Delta mutants, localization of mto2p to all of these MTOCs is strongly reduced or absent. We also find that in mto2Delta mutants, cytoplasmic forms of the gamma-tubulin complex are mislocalized, and the gamma-tubulin complex no longer coimmunoprecipitates with mto1p from cell extracts. These experiments establish mto2p as a major regulator of mto1p-mediated microtubule nucleation by the gamma-tubulin complex.","authors":"Samejima I, Lourenço PC, Snaith HA, Sawin KE","authors_abbrev":"Samejima I et al.","pubmed_publication_date":"Jun 2005","pubmed_entrez_date":"2005-01-22","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC902.06","SPCC417.07c","SPBC365.15"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:8873452","title":"Characterization of cwl1+, a gene from Schizosaccharomyces pombe whose overexpression causes cell lysis.","citation":"Yeast 1996 Aug;12(10):983-90","abstract":"From a Schizosaccharomyces pombe genomic library we have isolated the gene cwl1+ that causes cell lysis when it is overexpressed in the absence of an osmotic stabilizer. Southern hybridization showed that cwl1+ exists as a single copy in the S. pombe genome. The cwl1+ gene nucleotide sequence revealed a putative open reading frame of 924 bp encoding a polypeptide of 308 amino acids with a calculated Mt of 27000. The cwl1+ DNA hybridizes to a major RNA transcript of 1.5 kb whose 5' end maps at a position 452 bp upstream from the predicted translation start. Comparison of the amino acid sequence with those included in the current databases, showed no significant similarity to any known sequences. Cells overexpressing the cwl1+ gene under the control of the S. pombe nmt inducible promoter displayed a reduced cell wall content, were unable to separate after division and lysed drastically in the absence of osmotic stabilizer. Disruption of the cwl1+ gene caused no noticeable phenotype.","authors":"Godoy C, Arellano M, Diaz M, Duran A, Perez P","authors_abbrev":"Godoy C et al.","pubmed_publication_date":"Aug 1996","pubmed_entrez_date":"1996-08-01","publication_year":"1996","canto_session_key":"a7f436801fb9dd71","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-02-07 18:24:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-01 12:05:14","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC31A8.01c","SPCC830.08c","SPBC1539.04"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2013-02-01"},{"uniquename":"PMID:6252475","title":"In vitro suppression of UGA codons in a mitochondrial mRNA.","citation":"Nature 1980 Sep 25;287(5780):361-3","abstract":"Although both prokaryotic and eukaryotic messenger RNAs can be easily translated in heterologous protein-synthesizing systems, attempts to achieve correct synthesis of mitochondrial proteins by translation of mitochondrial mRNAs in such systems have failed. In general, the products of synthesis are of low molecular weight and presumably represent fragments of mitochondrial proteins. These fragments display a strong tendency to aggregate. Explanations have included the use by mitochondria of codons requiring a specialized tRNA population and the fortuitous occurrence within genes of purine-rich sequences resembling bacterial ribosome binding sites. In addition, the long 5'-leader sequences present in many mitochondrial (mt) RNAs may also contribute to difficulties in mRNA recognition by heterologous ribosomes. Recent sequence analysis of human mtDNA suggests that the genetic code used by mammalian mitochondria deviates in a number of respects from the 'universal' code, the most striking of these being the use of the UGA termination codon to specify tryptophan. That this may also apply in yeast mitochondria has been shown by Fox and Macino et al., thus providing an obvious and easily testable explanation for the inability of heterologous systems to synthesize full-length mitochondrial proteins. We confirm this explanation and describe here the in vitro synthesis of a full-length subunit II of yeast cytochrome c oxidase in a wheat-germ extract supplemented with a partially purified mitochondrial mRNA for this protein and a UGA-suppressor tRNA from Schizosaccharomyces pombe.","authors":"De Ronde A, Van Loon AP, Grivell LA, Kohli J","authors_abbrev":"De Ronde A et al.","pubmed_publication_date":"25 Sep 1980","pubmed_entrez_date":"1980-09-25","publication_year":"1980","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19202289","title":"The Schizosaccharomyces pombe syntaxin 1 homolog, Psy1, is essential in the development of the forespore membrane.","citation":"Biosci Biotechnol Biochem 2009 Feb;73(2):339-45","abstract":"Syntaxin is a component of t-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE), which is responsible for docking membrane vesicles at the target membrane and is highly conserved among eukaryotes. In the fission yeast Schizosaccharomyces pombe, the psy1(+) gene encoding a syntaxin 1 homolog was originally isolated as a multicopy suppressor of the sporulation-deficient mutant, spo3, but little is known about the way Psy1 is involved in sporulation. Here we report the isolation of a sporulation-defective mutant, psy1-S1, generated by random PCR mutagenesis. psy1-S1 also exhibited temperature sensitivity in growth. In psy1-S1 cells, assembly of the forespore membrane (FSM) initiated near the spindle pole bodies during meiosis II, but subsequent expansion of the membrane was severely impaired. Overproduction of the cognate SNARE proteins, Syb1 and Sec9, suppressed both the temperature sensitivity and sporulation defects of psy1-S1. These results indicate that Psy1 plays an essential role in FSM formation coordinated by Syb1 and Sec9.","authors":"Maeda Y, Kashiwazaki J, Shimoda C, Nakamura T","authors_abbrev":"Maeda Y et al.","pubmed_publication_date":"Feb 2009","pubmed_entrez_date":"2009-02-10","publication_year":"2009","canto_session_key":"0a18d3058ad0058a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-11-23 19:23:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-11-12 10:10:56","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.11","SPBC26H8.02c","SPCC825.03c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-11-12"},{"uniquename":"PMID:18076573","title":"Rapamycin sensitivity of the Schizosaccharomyces pombe tor2 mutant and organization of two highly phosphorylated TOR complexes by specific and common subunits.","citation":"Genes Cells 2007 Dec;12(12):1357-70","abstract":"Nutrients are essential for cell growth and division. Screening of Schizosaccharomyces pombe temperature-sensitive strains led to the isolation of a nutrient-insensitive mutant, tor2-287. This mutant produces a nitrogen starvation-induced arrest phenotype in rich media, fails to recover from the arrest, and is hypersensitive to rapamycin. The L2048S substitution mutation in the catalytic domain in close proximity to the adenine base of ATP is unique as it is the sole known genetic cause of rapamycin hypersensitivity. Localization of Tor2 was speckled in the vegetative cytoplasm, and both speckled and membranous in the arrested cell cytoplasm. Using mass spectroscopic analysis, we identified six subunits (Tco89, Bit61, Toc1, Tel2, Tti1 and Cka1) that, in addition to the six previously identified subunits (Tor1, Tor2, Mip1/Raptor, Ste20/Rictor, Sin1/Avo1 and Wat1/Lst8), comprise the TOR complexes (TORCs). All of the subunits so far examined are multiply phosphorylated. Tel2 bound to Tti1 interacts with various phosphatidyl inositol kinase (PIK)-related kinases including Tra1, Tra2 and Rad3, as well as Tor1 and Tor2. Schizosaccharomyces pombe TORCs should thus be functionally redundant and might be broadly regulated through different subunits that are either common or specific to the two TORCs, or even common to various PIK-related kinases. Functional redundancy of the TORCs may explain the rapamycin hypersensitivity of tor2-287.","authors":"Hayashi T, Hatanaka M, Nagao K, Nakaseko Y, Kanoh J, Kokubu A, Ebe M, Yanagida M","authors_abbrev":"Hayashi T et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-12-14","publication_year":"2007","canto_session_key":"703aa934daf915d2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-05 14:49:19","canto_approved_date":"2022-02-07 15:50:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-11-20 17:52:32","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"antonia lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.10c","SPAC458.03","SPBP18G5.03","SPCC777.08c","SPCC162.12","SPAC57A7.11","SPAC1F5.11c","SPCC23B6.03c","SPAPYUG7.02c","SPAC23C11.11","SPBP16F5.03c","YPL180W","SPBC21B10.05c","SPBC216.07c","SPBC216.05","SPBC12C2.02c","SPBC1604.17c","SPCC622.13c"],"gene_count":17,"ltp_gene_count":17,"approved_date":"2017-07-05"},{"uniquename":"PMID:16088874","title":"A rapid and simple procedure for high-efficiency lithium acetate transformation of cryopreserved Schizosaccharomyces pombe cells.","citation":"Yeast 2005 Jul 30;22(10):799-804","abstract":"A rapid, simple, convenient, and highly efficient transformation of the fission yeast Schizosaccharomyces pombe has been developed. Freezing fission yeast cells in glycerol, a permeating cryoprotectant, with lithium acetate improved remarkably the transformation efficiency by one to two orders of magnitude. The optimum concentration of glycerol was found to be 30%, which is higher than that (10-15%) in the conventional cryopreservation of yeast cells. Glycerol not only played a role in cryopreserving the competent cells but also improved the transformation efficiency of the process. The thawed cell suspension with glycerol and lithium acetate was immediately mixed with carrier DNA, plasmid DNA and polyethylene glycol. Next, the mixture was heat shocked and directly spread on a selection plate. This simple procedure yielded more than 10(6) transformants/microg plasmid DNA, reducing the time required to only 20 min in total, including the thawing time. Furthermore, the frozen competent cells were stored long-term for more than 3 months without any significant loss of efficiency.","authors":"Suga M, Hatakeyama T","authors_abbrev":"Suga M et al.","pubmed_publication_date":"30 Jul 2005","pubmed_entrez_date":"2005-08-10","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26312418","title":"Disaggregases, molecular chaperones that resolubilize protein aggregates.","citation":"An Acad Bras Cienc 2015 Aug;87(2 Suppl):1273-92","abstract":"The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of protein aggregates, an insoluble association of polypeptides that harm cell physiology, either by themselves or in the process of formation. Several biological processes have evolved to prevent and eliminate the existence of non-functional and amyloidogenic aggregates, as they are associated with several human pathologies. Molecular chaperones and heat shock proteins are specialized in controlling the quality of the proteins in the cell, specifically by aiding proper folding, and dissolution and clearance of already formed protein aggregates. The latter is a function of disaggregases, mainly represented by the ClpB/Hsp104 subfamily of molecular chaperones, that are ubiquitous in all organisms but, surprisingly, have no orthologs in the cytosol of metazoan cells. This review aims to describe the characteristics of disaggregases and to discuss the function of yeast Hsp104, a disaggregase that is also involved in prion propagation and inheritance.","doi":"10.1590/0001-3765201520140671","authors":"Mokry DZ, Abrahão J, Ramos CH","authors_abbrev":"Mokry DZ et al.","pubmed_publication_date":"Aug 2015","pubmed_entrez_date":"2015-08-28","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2021-01-22 12:19:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24774534","title":"Schizosaccharomyces pombe centromere protein Mis19 links Mis16 and Mis18 to recruit CENP-A through interacting with NMD factors and the SWI/SNF complex.","citation":"Genes Cells 2014 Jul;19(7):541-54","abstract":"CENP-A is a centromere-specific variant of histone H3 that is required for accurate chromosome segregation. The fission yeast Schizosaccharomyces pombe and mammalian Mis16 and Mis18 form a complex essential for CENP-A recruitment to centromeres. It is unclear, however, how the Mis16-Mis18 complex achieves this function. Here, we identified, by mass spectrometry, novel fission yeast centromere proteins Mis19 and Mis20 that directly interact with Mis16 and Mis18. Like Mis18, Mis19 and Mis20 are localized at the centromeres during interphase, but not in mitosis. Inactivation of Mis19 in a newly isolated temperature-sensitive mutant resulted in CENP-A delocalization and massive chromosome missegregation, whereas Mis20 was dispensable for proper chromosome segregation. Mis19 might be a bridge component for Mis16 and Mis18. We isolated extragenic suppressor mutants for temperature-sensitive mis18 and mis19 mutants and used whole-genome sequencing to determine the mutated sites. We identified two groups of loss-of-function suppressor mutations in non-sense-mediated mRNA decay factors (upf2 and ebs1), and in SWI/SNF chromatin-remodeling components (snf5, snf22 and sol1). Our results suggest that the Mis16-Mis18-Mis19-Mis20 CENP-A-recruiting complex, which is functional in the G1-S phase, may be counteracted by the SWI/SNF chromatin-remodeling complex and non-sense-mediated mRNA decay, which may prevent CENP-A deposition at the centromere.","doi":"10.1111/gtc.12152","authors":"Hayashi T, Ebe M, Nagao K, Kokubu A, Sajiki K, Yanagida M","authors_abbrev":"Hayashi T et al.","pubmed_publication_date":"Jul 2014","pubmed_entrez_date":"2014-04-30","publication_year":"2014","canto_session_key":"17f50a0cd9b7972b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takeshi Hayashi","canto_first_approved_date":"2019-01-29 16:52:24","canto_approved_date":"2026-01-29 17:52:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-26 07:45:56","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Takeshi Hayashi","community_curator":true,"annotation_count":33,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":37,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC16C9.06c","SPBC27B12.02","SPBC409.04c","SPAC13G7.03","SPCC1620.14c","SPAC139.06","SPCC970.12","SPBC2F12.03c","SPBC30B4.04c","SPBC1105.17","SPAC19A8.08","SPAC2F7.08c","SPBC776.16","SPCC1672.10","SPAC1687.20c"],"gene_count":15,"ltp_gene_count":13,"approved_date":"2019-01-29"},{"uniquename":"PMID:18094683","title":"Host genome surveillance for retrotransposons by transposon-derived proteins.","citation":"Nature 2008 Jan 24;451(7177):431-6","abstract":"Transposable elements and their remnants constitute a substantial fraction of eukaryotic genomes. Host genomes have evolved defence mechanisms, including chromatin modifications and RNA interference, to regulate transposable elements. Here we describe a genome surveillance mechanism for retrotransposons by transposase-derived centromeric protein CENP-B homologues of the fission yeast Schizosaccharomyces pombe. CENP-B homologues of S. pombe localize at and recruit histone deacetylases to silence Tf2 retrotransposons. CENP-Bs also repress solo long terminal repeats (LTRs) and LTR-associated genes. Tf2 elements are clustered into 'Tf' bodies, the organization of which depends on CENP-Bs that display discrete nuclear structures. Furthermore, CENP-Bs prevent an 'extinct' Tf1 retrotransposon from re-entering the host genome by blocking its recombination with extant Tf2, and silence and immobilize a Tf1 integrant that becomes sequestered into Tf bodies. Our results reveal a probable ancient retrotransposon surveillance pathway important for host genome integrity, and highlight potential conflicts between DNA transposons and retrotransposons, major transposable elements believed to have greatly moulded the evolution of genomes.","authors":"Cam HP, Noma K, Ebina H, Levin HL, Grewal SI","authors_abbrev":"Cam HP et al.","pubmed_publication_date":"24 Jan 2008","pubmed_entrez_date":"2007-12-21","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1105.04c","SPBC800.03","SPBC31F10.13c","SPBC14F5.12c","SPAC9E9.10c","SPBC36.05c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:21401840","title":"Pob1 ensures cylindrical cell shape by coupling two distinct rho signaling events during secretory vesicle targeting.","citation":"Traffic 2011 Jun;12(6):726-39","abstract":"Proper cell morphogenesis requires the co-ordination of cell polarity, cytoskeletal organization and vesicle trafficking. The Schizosaccharomyces pombe mutant pob1-664 has a curious lemon-like shape, the basis of which is not understood. Here, we found abundant vesicle accumulation in these cells, suggesting that Pob1 plays a role in vesicle trafficking. We identified Rho3 as a multicopy suppressor of this phenotype. Because Rho3 function is related to For3, an actin-polymerizing protein, and Sec8, a component of the exocyst complex, we analyzed their functional relationship with Pob1. Pob1 was essential for the formation of actin cables (by interacting with For3) and for the polarized localization of Sec8. Although neither For3 nor Sec8 is essential for polarized growth, their simultaneous disruption prevented tip growth and yielded a lemon-like cell morphology similar to pob1-664. Thus, Pob1 may ensure cylindrical cell shape of S. pombe by coupling actin-mediated vesicle transport and exocyst-mediated vesicle tethering during secretory vesicle targeting.","doi":"10.1111/j.1600-0854.2011.01190.x","authors":"Nakano K, Toya M, Yoneda A, Asami Y, Yamashita A, Kamasawa N, Osumi M, Yamamoto M","authors_abbrev":"Nakano K et al.","pubmed_publication_date":"Jun 2011","pubmed_entrez_date":"2011-03-16","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC1289.04c","SPAC110.03","SPAC23C4.08","SPCC970.09","SPCC895.05","SPBC106.20"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:8227198","title":"Six git genes encode a glucose-induced adenylate cyclase activation pathway in the fission yeast Schizosaccharomyces pombe.","citation":"J Cell Sci 1993 Aug;105 ( Pt 4)(0 4):1095-100","abstract":"An important eukaryotic signal transduction pathway involves the regulation of the effector enzyme adenylate cyclase, which produces the second messenger, cAMP. Previous genetic analyses demonstrated that glucose repression of transcription of the Schizosaccharomyces pombe fbp1 gene requires the function of adenylate cyclase, encoded by the git2 gene. As mutations in git2 and in six additional git genes are suppressed by exogenous cAMP, these 'upstream' git genes were proposed to act to produce a glucose-induced cAMP signal. We report here that assays of cAMP levels in wild-type and various mutant S. pombe cells, before and after exposure to glucose, show that this is the case. The data suggest that the cAMP signal results from the activation of adenylate cyclase. Therefore these 'upstream' git genes appear to encode a glucose-induced adenylate cyclase activation pathway. Assays of cAMP on a strain carrying a mutation in the git6 gene, which acts downstream of adenylate cyclase, indicate that git6 may function to feedback regulate adenylate cyclase activity. Thus git6 may encode a cAMP-dependent protein kinase.","authors":"Byrne SM, Hoffman CS","authors_abbrev":"Byrne SM et al.","pubmed_publication_date":"Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_session_key":"219e86a87274fe5f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-04-08 17:02:31","canto_approved_date":"2023-09-19 12:25:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-10-22 14:56:53","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC19C7.03","SPCC285.09c","SPAC23H3.13c","SPCC1753.02c","SPAC926.04c","SPBC36.12c","SPBC106.10","SPBC32H8.07","SPBC21C3.20c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2020-04-08"},{"uniquename":"EMBL:FY124947","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20094029","title":"gammaH2A binds Brc1 to maintain genome integrity during S-phase.","citation":"EMBO J 2010 Mar 17;29(6):1136-48","abstract":"ATM(Tel1) and ATR(Rad3) checkpoint kinases phosphorylate the C-terminus of histone H2AX (H2A in yeasts) in chromatin flanking DNA damage, establishing a recruitment platform for checkpoint and repair proteins. Phospho-H2A/X (gammaH2A/X)-binding proteins at double-strand breaks (DSBs) have been characterized, but those required for replication stress responses are unknown. Here, we present genetic, biochemical, small angle X-ray scattering (SAXS), and X-ray structural studies of the Schizosaccharomyces pombe Brc1, a 6-BRCT-domain protein that is structurally related to Saccharomyces cerevisiae Rtt107 and mammalian PTIP. Brc1 binds gammaH2A to form spontaneous and DNA damage-induced nuclear foci. Spontaneous Brc1 foci colocalize with ribosomal DNA repeats, a region prone to fork pausing and genomic instability, whereas DNA damage-induced Brc1 foci colocalize with DSB response factors. gammaH2A binding is critical for Brc1 function. The 1.45 A resolution crystal structure of Brc1-gammaH2A complex shows how variable BRCT insertion loops sculpt tandem-BRCT phosphoprotein-binding pockets to facilitate unique phosphoprotein-interaction specificities, and unveils an acidic DNA-mimicking Brc1 surface. From these results, Brc1 docking to gammaH2A emerges as a critical chromatin-specific response to replication-associated DNA damage.","doi":"10.1038/emboj.2009.413","authors":"Williams JS, Williams RS, Dovey CL, Guenther G, Tainer JA, Russell P","authors_abbrev":"Williams JS et al.","pubmed_publication_date":"17 Mar 2010","pubmed_entrez_date":"2010-01-23","publication_year":"2010","canto_session_key":"31248641de1cbfdc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2015-04-22 11:40:46","canto_approved_date":"2019-06-14 13:44:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-24 21:22:51","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[{"name":"Paul Russell","community_curator":true,"annotation_count":15,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.05c","SPBC342.05","SPAC30D11.10","SPAC19G12.06c","SPCC622.08c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2015-04-22","pdb_entries":[{"pdb_id":"3l40","gene_chains":[{"gene_uniquename":"SPBC582.05c","chain":"A/B","position":"630-849"}],"title":"Crystal Structure of S. pombe Brc1 BRCT5-BRCT6 domains","entry_authors":"Williams RS,Williams JS,Guenther G,Tainer JA","entry_authors_abbrev":"Williams RS et al.","reference_uniquename":"PMID:20094029","experimental_method":"X-ray","resolution":"1.55"},{"pdb_id":"3l41","gene_chains":[{"gene_uniquename":"SPBC582.05c","chain":"A","position":"630-849"}],"title":"Crystal Structure of S. pombe Brc1 BRCT5-BRCT6 domains in complex with phosphorylated H2A","entry_authors":"Williams RS,Williams JS,Guenther G,Tainer JA","entry_authors_abbrev":"Williams RS et al.","reference_uniquename":"PMID:20094029","experimental_method":"X-ray","resolution":"1.45"}]},{"uniquename":"PMID:1844245","title":"Mammalian G2 regulatory genes and their possible involvement in genetic instability in cancer cells.","citation":"Princess Takamatsu Symp 1991;22:231-8","abstract":"In the fission yeast Schizosaccharomyces pombe, mitosis is initiated following the activation of the cdc2+/cyclin B kinase. The cdc2+/cyclin B kinase is positively regulated by cdc25+ tyrosine phosphatase and negatively regulated by wee1+/mik1+ tyrosine kinases. This regulatory system is evolutionarily conserved throughout higher eukaryotes. Drosophila and humans contain a cdc25+ gene homolog called String and CDC25Hs (hereafter referred to as CDC25Hul), respectively. We recently cloned a wee1+ homolog (WEE1Hu) and two additional cdc25+ homologs (CDC25Hu2 and CDC25Hu3) from human cells. Consequently, human cells contain at least one wee1+ and three cdc25+ homologs. Both CDC25Hu1 and CDC25Hu2 resemble the cdc25+ gene not only in structure and function but also in the mode of expression. They are expressed mostly in G2. On the other hand, CDC25Hu3 is expressed mostly in early S, indicating that it has some novel function in the early phase of the cell cycle. In all the cell lines examined, CDC25Hu2 is expressed to a greater extent than CDC25Hu1 or CDC25Hu3. The expression of CDC25Hu2 is particularly high in various cancer cells including those transformed by SV40 or human papilloma virus type 16 E6, E7, both of which are well known for their ability to induce genomic instability. In addition, there is a noticeable correlation between the extent of aneuploidy and the level of CDC25Hu2 expression in the cancer cells examined. In view of the fact that overexpression of cdc25+ under certain conditions induces genomic instability in the fission yeast, overexpression of CDC25Hu2 associated with many cancer cells might play at least a role in the induction of their chromosomal abnormalities.","authors":"Okayama H, Nagata A, Igarashi M, Suto K, Jinno S","authors_abbrev":"Okayama H et al.","pubmed_publication_date":"1991","pubmed_entrez_date":"1991-01-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:21","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8496185","title":"Molecular analysis of the essential gene for adenylate kinase from the fission yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 1993 May 25;268(15):11326-34","abstract":"The enzyme-catalyzed transfer of the terminal phosphoryl group from ATP to an acceptor molecule is an important reaction in a wide variety of biological processes. I demonstrate here the essential function of an ATP:AMP phosphotransferase (adenylate kinase) in the fission yeast Schizosaccharomyces pombe. A cDNA clone encoding immunoreactive adenylate kinase from S. pombe was isolated from a lambda gt11 expression library by cross-reaction with antibodies raised against the recently characterized ADK1 enzyme from the budding yeast Saccharomyces cerevisiae. Subsequent cloning and nucleotide sequence analysis of the S. pombe adenylate kinase gene, adk1, revealed a coding region of 660 nucleotides. The alignment of the two amino acid sequences from S. cerevisiae and S. pombe shows 67% identity. By gene disruption and tetrad analysis it is demonstrated that adk1 is absolutely essential for cell viability. This is in contrast to the ADK1 gene of S. cerevisiae, the deletion of which was shown to lead to a slower cell growth rate rather than to a lethal phenotype. Expression of adk1 in the S. cerevisiae ADK1 deletion strain restored normal cell growth, demonstrating that ADK1 and adk1 are functionally interchangeable. However, despite lack of absolute substrate specificity of adenylate kinases, adk1 could not complement the loss of function of the guanylate kinase encoding gene in a S. cerevisiae null mutant strain, thus highlighting the functional uniqueness of each nucleoside monophosphate kinase. Using suitable expression vectors, large amounts of active adk1 enzyme were produced in either yeast species and in E. coli. The purified enzyme exhibits a high preference for adenine nucleotides, with ATP being a 10 times more efficient phosphoryl donor than GTP.","authors":"Konrad M","authors_abbrev":"Konrad M","pubmed_publication_date":"25 May 1993","pubmed_entrez_date":"1993-05-25","publication_year":"1993","canto_session_key":"31f078678cafa180","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-08 08:50:45","canto_approved_date":"2020-01-17 19:39:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-08 08:50:36","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4G9.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-08"},{"uniquename":"PMID:7956085","title":"Structure and function of Schizosaccharomyces pombe centromeres.","citation":"Cold Spring Harb Symp Quant Biol 1993;58:687-95","abstract":"","authors":"Clarke L, Baum M, Marschall LG, Ngan VK, Steiner NC","authors_abbrev":"Clarke L et al.","pubmed_publication_date":"1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41676957","title":"Trafficking of the human Na + /H +  antiporter NHA2 to the plasma membrane requires cornichon COPII cargo receptors.","citation":"Protein Sci 2026 Mar;35(3):e70492","abstract":"A key prerequisite of transporter proteins' function is their trafficking to the target cellular membranes where they fulfill distinct physiological roles. Cornichon proteins (CNIH/Erv14) represent a highly conserved family of coat protein complex II (COPII)-coated vesicle cargo receptors that facilitate the exit of numerous transporters from the endoplasmic reticulum (ER) to proceed via the secretory pathway. Despite their biomedical significance, the cargo specificities of the four human cornichons (CNIH1-4) remain largely unexplored. Here, we conducted a bioinformatics analysis of the CNIH/Erv14 family, revealing evolutionary conservation profiles of the family based on an alignment of 1879 sequences. AlphaFold3 modeling predicts that residues identified as the most evolutionarily conserved in cornichon family interact with Sec24 proteins of COPII vesicles. We also demonstrate the suitability of the model yeast Saccharomyces cerevisiae for studying the properties and putative interactors of human cornichons. We engineered S. cerevisiae strains in which the endogenous cornichon gene (ERV14) was replaced with human CNIH1, CNIH2, or CNIH4 coding sequences or CNIH coding sequences were expressed from multi-copy plasmids. The studied human cornichons were functional in S. cerevisiae cells and, to varying extents, complemented the differing phenotypes related to yeast ScErv14 roles in monovalent-cation homeostasis. The presence of human CNIHs supported the functioning of the yeast plasma-membrane Na + , K + /H +  antiporter Nha1, a known cargo of ScErv14. Both yeast ScErv14 and human CNIH cornichons improved the plasma-membrane targeting and functioning of the human Na + /H +  antiporter NHA2 in yeast cells, identifying NHA2 as a novel cargo of cornichon COPII cargo receptors.","doi":"10.1002/pro.70492","authors":"Kacovská K, Papoušková K, Masrati G, Rosas-Santiago P, Przeczková T, Žárská V, Ben-Tal N, Zimmermannová O","authors_abbrev":"Kacovská K et al.","pubmed_publication_date":"Mar 2026","pubmed_entrez_date":"2026-02-12","publication_year":"2026","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F8.08","SPAC2C4.05","SPAC30C2.05"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:26896847","title":"Ensembl comparative genomics resources.","citation":"Database (Oxford) 2016;2016","abstract":"Evolution provides the unifying framework with which to understand biology. The coherent investigation of genic and genomic data often requires comparative genomics analyses based on whole-genome alignments, sets of homologous genes and other relevant datasets in order to evaluate and answer evolutionary-related questions. However, the complexity and computational requirements of producing such data are substantial: this has led to only a small number of reference resources that are used for most comparative analyses. The Ensembl comparative genomics resources are one such reference set that facilitates comprehensive and reproducible analysis of chordate genome data. Ensembl computes pairwise and multiple whole-genome alignments from which large-scale synteny, per-base conservation scores and constrained elements are obtained. Gene alignments are used to define Ensembl Protein Families, GeneTrees and homologies for both protein-coding and non-coding RNA genes. These resources are updated frequently and have a consistent informatics infrastructure and data presentation across all supported species. Specialized web-based visualizations are also available including synteny displays, collapsible gene tree plots, a gene family locator and different alignment views. The Ensembl comparative genomics infrastructure is extensively reused for the analysis of non-vertebrate species by other projects including Ensembl Genomes and Gramene and much of the information here is relevant to these projects. The consistency of the annotation across species and the focus on vertebrates makes Ensembl an ideal system to perform and support vertebrate comparative genomic analyses. We use robust software and pipelines to produce reference comparative data and make it freely available. Database URL: http://www.ensembl.org.","doi":"10.1093/database/bav096","authors":"Herrero J, Muffato M, Beal K, Fitzgerald S, Gordon L, Pignatelli M, Vilella AJ, Searle SM, Amode R, Brent S, Spooner W, Kulesha E, Yates A, Flicek P","authors_abbrev":"Herrero J et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2016-02-21","publication_year":"2016","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SJAG_02611","SPBC215.11c","SJAG_02580","SJAG_05248","SJAG_02191","SJAG_05001","SPBC460.01c","SPBC4C3.09","SPBC20F10.10","SPCC364.03","SPCC613.06","SJAG_05398","SPAC3A12.10","SJAG_02243","SJAG_16455","SJAG_02073","SPAC3G9.17","SJAG_03762","SPAC644.15","SPAC29B12.14c","SJAG_00335","SJAG_04897","SJAG_04478","SJAG_02283","SJAG_03568","SPAC521.03","SJAG_04672","SPCC1183.08c","SPAC2F3.13c","SJAG_01078","SJAG_02079","SJAG_03644","SJAG_04910","SPBC530.07c","SJAG_00544","SPAC17G6.06","SPBC3E7.04c","SJAG_04534","SJAG_02113","SJAG_01551","SJAG_03425","SPBC839.19","SJAG_01939","SPCC1259.14c","SPBC649.02","SJAG_02335","SJAG_04135","SPCC1235.13","SJAG_04714","SPAC30D11.12","SPAC23A1.11","SPAC23C11.02c","SJAG_03922","SPBC29A3.14c","SPAC3H5.12c","SJAG_05153","SJAG_02280","SJAG_03373","SPAC13G6.07c","SPAC6B12.19","SJAG_06622","SJAG_06022","SPBC4F6.04","SJAG_04188","SJAG_01656","SPCC13B11.01","SJAG_02548","SPBC21B10.10","SJAG_MIT09","SPCP1E11.09c","SPAC6G9.09c","SPAC1039.05c","SJAG_03863","SJAG_MIT13","SPBC530.16","SJAG_02794","SPBC11C11.07","SPCC1739.08c","SPAC13G7.02c","SPBC13E7.01","SPBC21H7.03c","SJAG_01506","SPAC26H5.10c","SJAG_02698","SPAC23A1.10","SPAC688.16","SPBC119.18","SPAC19B12.04","SPAC1805.18","SJAG_06612","SJAG_02957","SPBC14C8.19","SJAG_02081","SJAG_05326","SPMIT.04","SPBC1105.12","SJAG_01492","SPAC22E12.06c","SPBC16C6.02c","SPMIT.07","SJAG_00589","SPAC1F7.13c","SJAG_06576","SPBC14C8.03","SJAG_03099","SJAG_05694","SJAG_02154","SJAG_02361","SPBC8D2.03c","SJAG_02682","SJAG_01366","SJAG_05033","SPCC24B10.09","SPBC1271.09","SJAG_06603","SJAG_05573","SPAC3H5.13","SJAG_06586","SJAG_02707","SPAC5H10.13c","SJAG_03611","SJAG_04055","SPCC663.18","SPBC8E4.01c","SJAG_00600","SJAG_MIT15","SJAG_04720","SPAC1071.07c","SJAG_05325","SJAG_01296","SPAC11D3.15","SPBC23E6.08","SJAG_00109","SPAC22H12.04c","SJAG_01129","SPAC26A3.01","SPAC30D11.10","SPAC6G9.04","SPAC26H5.09c","SPBC1652.02","SJAG_01411","SPBC947.03c","SJAG_04633","SPCC1620.03","SPBC776.11","SPBC530.02","SJAG_00733","SJAG_03323","SPAC23H3.04","SJAG_04095","SJAG_01087","SPBC685.06","SJAG_04715","SJAG_04176","SJAG_02139","SJAG_04458","SPAC869.11","SJAG_02803","SJAG_05413","SJAG_02155","SJAG_00468","SJAG_02476","SPAC977.09c","SPBC800.04c","SPAC8C9.09c","SPBC3E7.02c","SJAG_02010","SJAG_01853","SJAG_00629","SJAG_03365","SPAC1B3.21","SPACUNK4.17","SJAG_06514","SPCC757.11c","SJAG_00587","SJAG_MIT03","SJAG_01548","SJAG_01032","SJAG_MIT37","SJAG_01348","SPAC13G6.02c","SPAC13C5.07","SPBC1921.01c","SJAG_03824","SPAC12B10.14c","SJAG_02861","SPBC577.02","SPBC16A3.17c","SJAG_06449","SPBC32F12.16","SJAG_00688","SJAG_00254","SJAG_00107","SJAG_00940","SJAG_01721","SJAG_04168","SJAG_06597","SJAG_03122","SPAC664.04c","SPAC167.09","SPAPB2C8.01","SPBC21D10.07","SJAG_03197","SPAC26A3.04","SJAG_03133","SJAG_01970","SPAC19B12.13","SPAC1250.05","SJAG_03180","SPCC24B10.03","SPAC3G9.11c","SJAG_03608","SPBC21C3.13","SPCC794.09c","SJAG_04695","SJAG_06613","SJAG_00019","SPAC3H5.05c","SPAPB17E12.13","SJAG_03999","SPBC17G9.07","SJAG_03423","SPCC126.13c","SJAG_01885","SPAC56F8.04c","SPCC1393.03","SJAG_03790","SPCC1919.08c","SJAG_MIT07","SJAG_05979","SJAG_04277","SPCC330.07c","SJAG_03326","SPAC144.11","SJAG_00018","SJAG_06425","SJAG_00096","SPAC806.04c","SPAC18B11.08c","SJAG_06440","SPAC17A5.03","SJAG_01676","SJAG_02138","SPAC212.06c","SPAP11E10.02c","SPAPB1E7.12","SPBC115.03","SPBC23G7.15c","SJAG_06621","SPBC18H10.14","SPAC3H1.06c","SPBC1289.13c","SJAG_02735","SPAC22A12.04c","SJAG_03828","SJAG_02904","SJAG_05372","SJAG_03321","SPAC17A2.01","SPAC869.05c","SJAG_01632","SPBC1348.08c","SPBC8E4.04","SPCC613.02","SJAG_05414","SJAG_00034","SJAG_01202","SJAG_16453","SJAG_04010","SJAG_01923","SJAG_03871","SJAG_02369","SJAG_04663","SPBC56F2.02","SJAG_01095","SPBP8B7.05c","SJAG_06534","SPBC19F8.08","SJAG_01287","SJAG_05321","SPCC4B3.20","SPAC521.05","SJAG_00310","SPBC36.03c","SPAC1783.08c","SPBC3D6.15","SJAG_00166","SPCC1322.11","SPAC3G9.03","SJAG_01512","SJAG_04029","SPBC359.01","SJAG_06383","SJAG_01580","SPBC14C8.09c","SPCC1739.13","SJAG_04256","SJAG_02960","SPMIT.09","SPAC227.19c","SJAG_05558","SPBPB2B2.06c","SPCP31B10.07","SPAC823.15","SPAPJ698.02c","SJAG_02546","SPCC188.09c","SPAPB8E5.06c","SJAG_01850","SJAG_05896","SJAG_00465","SJAG_03971","SPBC30B4.09","SPBC3F6.03","SPBC2G2.05","SJAG_04020","SJAG_03606","SPCC330.14c","SPBC29A3.12","SPAC19G12.17","SPBC19G7.03c","SJAG_05342","SJAG_02093","SJAG_02871","SPBC106.18","SJAG_02229","SJAG_05978","SJAG_03652","SJAG_01096","SPAC19A8.16","SPBC4F6.09","SPBC839.04","SJAG_00960","SPAC23C11.14","SPAC4G9.16c","SJAG_03422","SPBC1105.11c","SJAG_05926","SJAG_03859","SJAG_01113","SPAPB17E12.05","SJAG_MIT06","SJAG_01995","SJAG_01322","SJAG_02840","SPBC16C6.03c","SJAG_03903","SJAG_06598","SPAC212.11","SPAC222.19","SPAC4D7.14","SJAG_01975","SJAG_05693","SPBC460.05","SJAG_02956","SJAG_051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ount":357,"ltp_gene_count":0},{"uniquename":"PMID:8380233","title":"Schizosaccharomyces pombe map3+ encodes the putative M-factor receptor.","citation":"Mol Cell Biol 1993 Jan;13(1):80-8","abstract":"A defect in the map3 gene of the fission yeast Schizosaccharomyces pombe causes h+ mating-type-specific sterility. This gene was cloned by complementation. Nucleotide sequence analysis showed that it has a coding capacity of 365 amino acids. The deduced map3 gene product is a putative seven-transmembrane protein and has 20.0% amino acid identity with the a-factor receptor of Saccharomyces cerevisiae, encoded by STE3. It is also homologous with the Ustilago maydis mating pheromone receptors. The map3 gene is expressed in h+ cells but not in h- cells, and the transcripts are induced in response to nitrogen starvation. h+ cells defective in map3 do not respond to purified M-factor. When map3 is expressed ectopically in h- cells, they apparently acquire the ability to respond to the M-factor produced by themselves. The gpa1 gene, which encodes the alpha-subunit of a G-protein presumed to couple with the mating pheromone receptors, is essential for this function of map3. These observations strongly suggest that map3 encodes the M-factor receptor. Furthermore, this study provides strong support for the notion that pheromone signaling is essential for initiation of meiosis in S. pombe and that either M-factor signaling or P-factor signaling alone is sufficient.","authors":"Tanaka K, Davey J, Imai Y, Yamamoto M","authors_abbrev":"Tanaka K et al.","pubmed_publication_date":"Jan 1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_session_key":"5586aa35c0a6802f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-11 21:09:57","canto_approved_date":"2026-02-09 12:36:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-10 08:02:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC513.03","SPBC25B2.02c","SPAC3F10.10c","SPAPB8E5.05","SPBPJ4664.03"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2018-06-11"},{"uniquename":"PMID:8088538","title":"The isolation and characterization of the gene (dfr1) encoding dihydrofolate reductase (DHFR) in Schizosaccharomyces pombe.","citation":"Gene 1994 Sep 15;147(1):131-5","abstract":"A sequence encoding dihydrofolate reductase (DHFR) was isolated from a Schizosaccharomyces pombe cDNA library by selecting for trimethoprim resistance in Escherichia coli. The sequence was found to be functional in both Saccharomyces cerevisiae and Sz. pombe. When present on a multicopy plasmid, it confers increased resistance to concentrations of the drug methotrexate that are otherwise inhibitory for the standard yeast strains. The sequence was mapped by DNA hybridizations between genes adh1 and ade5 on chromosome III of Sz. pombe. The 1.6-kb insert contains a 1.5-kb open reading frame (ORF) with strong sequence similarity to other described DHFR-encoding genes. The similarity, however, is limited to a 678-bp sequence, occupying the 3'-half of the ORF. No similarity to other described DNA sequences or proteins could be found for the 5'-half. Southern and Northern blots indicate that the entire insert is present intact in the Sz. pombe genome and produces a 1.7-kb RNA transcript.","authors":"Bertani LE, Campbell JL","authors_abbrev":"Bertani LE et al.","pubmed_publication_date":"15 Sep 1994","pubmed_entrez_date":"1994-09-15","publication_year":"1994","canto_session_key":"6baab3278ca7c013","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-05-05 14:26:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-05 14:26:31","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1223.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-05-05"},{"uniquename":"PMID:8007985","title":"Structural and functional conservation of the human homolog of the Schizosaccharomyces pombe rad2 gene, which is required for chromosome segregation and recovery from DNA damage.","citation":"Mol Cell Biol 1994 Jul;14(7):4878-88","abstract":"The rad2 mutant of Schizosaccharomyces pombe is sensitive to UV irradiation and deficient in the repair of UV damage. In addition, it has a very high degree of chromosome loss and/or nondisjunction. We have cloned the rad2 gene and have shown it to be a member of the Saccharomyces cerevisiae RAD2/S. pombe rad13/human XPG family. Using degenerate PCR, we have cloned the human homolog of the rad2 gene. Human cDNA has 55% amino acid sequence identity to the rad2 gene and is able to complement the UV sensitivity of the rad2 null mutant. We have thus isolated a novel human gene which is likely to be involved both in controlling the fidelity of chromosome segregation and in the repair of UV-induced DNA damage. Its involvement in two fundamental processes for maintaining chromosomal integrity suggests that it is likely to be an important component of cancer avoidance mechanisms.","authors":"Murray JM, Tavassoli M, al-Harithy R, Sheldrick KS, Lehmann AR, Carr AM, Watts FZ","authors_abbrev":"Murray JM et al.","pubmed_publication_date":"Jul 1994","pubmed_entrez_date":"1994-07-01","publication_year":"1994","canto_session_key":"e0786e69efaa5521","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 15:03:18","canto_session_submitted_date":"2012-03-03 15:02:30","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.06c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:20299455","title":"The fission yeast inhibitor of growth (ING) protein Png1p functions in response to DNA damage.","citation":"J Biol Chem 2010 May 21;285(21):15786-93","abstract":"In budding yeast and human cells, ING (inhibitor of growth) tumor suppressor proteins play important roles in response to DNA damage by modulating chromatin structure through collaborating with histone acetyltransferase or histone deacetylase complexes. However, the biological functions of ING family proteins in fission yeast are poorly defined. Here, we report that Png1p, a fission yeast ING homolog protein, is required for cell growth under normal and DNA-damaged conditions. Png1p was further confirmed to regulate histone H4 acetylation through collaboration with the MYST family histone acetyltransferase 1 (Mst1). Additionally, both fission yeast PNG1 and MST1 can functionally complement their budding yeast correspondence homologs YNG2 and ESA1, respectively. These results suggest that ING proteins in fission yeast might also conserve function, similar to ING proteins in budding yeast and human cells. We also showed that decreased acetylation in Deltapng1 cells resulted in genome-wide down-regulation of 756 open reading frames, including the central DNA repair gene RAD22. Overexpression of RAD22 partially rescued the png1 mutant phenotype under both normal and DNA-damaged conditions. Furthermore, decreased expression of RAD22 in Deltapng1 cells was confirmed to be caused by decreased H4 acetylation at its promoter. Altogether, these results indicate that Png1p is required for histone H4 acetylation and functions upstream of RAD22 in the DNA damage response pathway.","doi":"10.1074/jbc.M110.101832","authors":"Chen JQ, Li Y, Pan X, Lei BK, Chang C, Liu ZX, Lu H","authors_abbrev":"Chen JQ et al.","pubmed_publication_date":"21 May 2010","pubmed_entrez_date":"2010-03-20","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC30D11.10","SPAC3G9.08","SPAC637.12c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU008665","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9326594","title":"DNA polymerase delta isolated from Schizosaccharomyces pombe contains five subunits.","citation":"Proc Natl Acad Sci U S A 1997 Oct 14;94(21):11244-9","abstract":"DNA polymerase delta (pol delta) plays an essential role in DNA replication, repair, and recombination. We have purified pol delta from Schizosaccharomyces pombe more than 10(3)-fold and demonstrated that the polymerase activity of purified S. pombe pol delta is completely dependent on proliferating cell nuclear antigen and replication factor C. SDS/PAGE analysis of the purified fraction indicated that the pol delta complex consists of five subunits that migrate with apparent molecular masses of 125, 55, 54, 42, and 22 kDa. Western blot analysis indicated that the 125, 55, and 54 kDa proteins are the large catalytic subunit (Pol3), Cdc1, and Cdc27, respectively. The identity of the other two subunits, p42 and p22, was determined following proteolytic digestion and sequence analysis of the resulting peptides. The peptide sequences derived from the p22 subunit indicated that this subunit is identical to Cdm1, previously identified as a multicopy suppressor of the temperature-sensitive cdc1-P13 mutant, whereas peptide sequences derived from the p42 subunit were identical to a previously uncharacterized ORF located on S. pombe chromosome 1.","authors":"Zuo S, Gibbs E, Kelman Z, Wang TS, O'Donnell M, MacNeill SA, Hurwitz J","authors_abbrev":"Zuo S et al.","pubmed_publication_date":"14 Oct 1997","pubmed_entrez_date":"1997-10-23","publication_year":"1997","canto_session_key":"c5b603a0b93314e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-05-12 14:40:41","canto_approved_date":"2022-02-24 20:55:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-04-07 14:38:21","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":7,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27E2.05","SPBC12D12.02c","SPBC336.04","SPBC16D10.09","SPBC1734.02c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2015-05-12"},{"uniquename":"PMID:26582015","title":"Selective oxidation of UDP-glucose to UDP-glucuronic acid using permeabilized Schizosaccharomyces pombe expressing human UDP-glucose 6-dehydrogenase.","citation":"Biotechnol Lett 2016 Mar;38(3):477-81","abstract":"To use permeabilized cells of the fission yeast, Schizosaccharomyces pombe, that expresses human UDP-glucose 6-dehydrogenase (UGDH, EC 1.1.1.22), for the production of UDP-glucuronic acid from UDP-glucose.\nIn cell extracts no activity was detected. Therefore, cells were permeabilized with 0.3 % (v/v) Triton X-100. After washing away all low molecular weight metabolites, the permeabilized cells were directly used as whole cell biocatalyst. Substrates were 5 mM UDP-glucose and 10 mM NAD(+). Divalent cations were not added to the reaction medium as they promoted UDP-glucose hydrolysis. With this reaction system 5 mM UDP-glucose were converted into 5 mM UDP-glucuronic acid within 3 h.\nRecombinant permeabilized cells of S. pombe can be used to synthesize UDP-glucuronic acid with 100 % yield and selectivity.","doi":"10.1007/s10529-015-1995-x","authors":"Weyler C, Bureik M, Heinzle E","authors_abbrev":"Weyler C et al.","pubmed_publication_date":"Mar 2016","pubmed_entrez_date":"2015-11-20","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-21 01:19:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB084815","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:25331280","title":"A yeast pheromone-based inter-species communication system.","citation":"Appl Microbiol Biotechnol 2015 Feb;99(3):1299-308","abstract":"We report on a pheromone-based inter-species communication system, allowing for a controlled cell-cell communication between the two species Saccharomyces cerevisiae and Schizosaccharomyces pombe as a proof of principle. It exploits the mating response pathways of the two yeast species employing the pheromones, α- or P-factor, as signaling molecules. The authentic and chimeric pheromone-encoding genes were engineered to code for the P-factor in S. cerevisiae and the α-factor in S. pombe. Upon transformation of the respective constructs, cells were enabled to express the mating pheromone of the opposite species. The supernatant of cultures of S. pombe cells expressing α-factor were able to induce a G1 arrest in the cell cycle, a change in morphology to the typical shmoo effect and expression driven by the pheromone-responsive FIG1 promoter in S. cerevisiae. The supernatant of cultures of S. cerevisiae cells expressing P-factor similarly induced cell cycle arrest in G1, an alteration in morphology typical for mating as well as the activation of the pheromone-responsive promoters of the rep1 and sxa2 genes in a pheromone-hypersensitive reporter strain of S. pombe. Apparently, both heterologous pheromones were correctly processed and secreted in an active form by the cells of the other species. Our data clearly show that the species-specific pheromone systems of yeast species can be exploited for a controlled inter-species communication.","doi":"10.1007/s00253-014-6133-5","authors":"Hennig S, Clemens A, Rödel G, Ostermann K","authors_abbrev":"Hennig S et al.","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2014-10-22","publication_year":"2015","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2014-10-23 00:15:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35353987","title":"Kinase domain autophosphorylation rewires the activity and substrate specificity of CK1 enzymes.","citation":"Mol Cell 2022 Jun 02;82(11):2006-2020.e8","abstract":"CK1s are acidophilic serine/threonine kinases with multiple critical cellular functions; their misregulation contributes to cancer, neurodegenerative diseases, and sleep phase disorders. Here, we describe an evolutionarily conserved mechanism of CK1 activity: autophosphorylation of a threonine (T220 in human CK1δ) located at the N terminus of helix αG, proximal to the substrate binding cleft. Crystal structures and molecular dynamics simulations uncovered inherent plasticity in αG that increased upon T220 autophosphorylation. The phosphorylation-induced structural changes significantly altered the conformation of the substrate binding cleft, affecting substrate specificity. In T220 phosphorylated yeast and human CK1s, activity toward many substrates was decreased, but we also identified a high-affinity substrate that was phosphorylated more rapidly, and quantitative phosphoproteomics revealed that disrupting T220 autophosphorylation rewired CK1 signaling in Schizosaccharomyces pombe. T220 is present exclusively in the CK1 family, thus its autophosphorylation may have evolved as a unique regulatory mechanism for this important family.","doi":"10.1016/j.molcel.2022.03.005","authors":"Cullati SN, Chaikuad A, Chen JS, Gebel J, Tesmer L, Zhubi R, Navarrete-Perea J, Guillen RX, Gygi SP, Hummer G, Dötsch V, Knapp S, Gould KL","authors_abbrev":"Cullati SN et al.","pubmed_publication_date":"02 Jun 2022","pubmed_entrez_date":"2022-03-30","publication_year":"2022","canto_session_key":"25e40241a9fb9067","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-04-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14722091","title":"Fission yeast homolog of neuronal calcium sensor-1 (Ncs1p) regulates sporulation and confers calcium tolerance.","citation":"J Biol Chem 2004 Mar 26;279(13):12744-54","abstract":"The neuronal calcium sensor (NCS) proteins (e.g. recoverin, neurocalcins, and frequenin) are expressed at highest levels in excitable cells, and some of them regulate desensitization of G protein-coupled receptors. Here we present NMR analysis and genetic functional studies of an NCS homolog in fission yeast (Ncs1p). Ncs1p binds three Ca2+ ions at saturation with an apparent affinity of 2 microm and Hill coefficient of 1.9. Analysis of NMR and fluorescence spectra of Ncs1p revealed significant Ca2+-induced protein conformational changes indicative of a Ca2+-myristoyl switch. The amino-terminal myristoyl group is sequestered inside a hydrophobic cavity of the Ca2+-free protein and becomes solvent-exposed in the Ca2+-bound protein. Subcellular fractionation experiments showed that myristoylation and Ca2+ binding by Ncs1p are essential for its translocation from cytoplasm to membranes. The ncs1 deletion mutant (ncs1Delta) showed two distinct phenotypes: nutrition-insensitive sexual development and a growth defect at high levels of extracellular Ca2+ (0.1 m CaCl(2)). Analysis of Ncs1p mutants lacking myristoylation (Ncs1p(G2A)) or deficient in Ca2+ binding (Ncs1p(E84Q/E120Q/E168Q)) revealed that Ca2+ binding was essential for both phenotypes, while myristoylation was less critical. Exogenous cAMP, a key regulator for sexual development, suppressed conjugation and sporulation of ncs1Delta, suggesting involvement of Ncs1p in the adenylate cyclase pathway turned on by the glucose-sensing G protein-coupled receptor Git3p. Starvation-independent sexual development of ncs1Delta was also complemented by retinal recoverin, which controls Ca2+-regulated desensitization of rhodopsin. In contrast, the Ca2+-intolerance of ncs1Delta was not affected by cAMP or recoverin, suggesting that the two ncs1Delta phenotypes are mechanistically independent. We propose that Schizosaccharomyces pombe Ncs1p negatively regulates sporulation perhaps by controlling Ca2+-dependent desensitization of Git3p.","authors":"Hamasaki-Katagiri N, Molchanova T, Takeda K, Ames JB","authors_abbrev":"Hamasaki-Katagiri N et al.","pubmed_publication_date":"26 Mar 2004","pubmed_entrez_date":"2004-01-15","publication_year":"2004","canto_session_key":"3b98520c5f6ca92f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-11-23 14:44:39","canto_approved_date":"2024-03-25 15:31:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-07 14:49:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18B11.04"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-11-23"},{"uniquename":"EMBL:AU011775","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31558680","title":"Reversible solidification of fission yeast cytoplasm after prolonged nutrient starvation.","citation":"J Cell Sci 2019 Nov 08;132(21)","abstract":"Cells depend on a highly ordered organisation of their content and must develop strategies to maintain the anisotropic distribution of organelles during periods of nutrient shortage. One of these strategies is to solidify the cytoplasm, which was observed in bacteria and yeast cells with acutely interrupted energy production. Here, we describe a different type of cytoplasm solidification fission yeast cells switch to, after having run out of nutrients during multiple days in culture. It provides the most profound reversible cytoplasmic solidification of yeast cells described to date. Our data exclude the previously proposed mechanisms for cytoplasm solidification in yeasts and suggest a mechanism that immobilises cellular components in a size-dependent manner. We provide experimental evidence that, in addition to time, cells use intrinsic nutrients and energy sources to reach this state. Such cytoplasmic solidification may provide a robust means to protect cellular architecture in dormant cells.","doi":"10.1242/jcs.231688","authors":"Heimlicher MB, Bächler M, Liu M, Ibeneche-Nnewihe C, Florin EL, Hoenger A, Brunner D","authors_abbrev":"Heimlicher MB et al.","pubmed_publication_date":"08 Nov 2019","pubmed_entrez_date":"2019-09-28","publication_year":"2019","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2019-09-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34440706","title":"ZC3HC1 Is a Novel Inherent Component of the Nuclear Basket, Resident in a State of Reciprocal Dependence with TPR.","citation":"Cells 2021 Jul 30;10(8)","abstract":"The nuclear basket (NB) scaffold, a fibrillar structure anchored to the nuclear pore complex (NPC), is regarded as constructed of polypeptides of the coiled-coil dominated protein TPR to which other proteins can bind without contributing to the NB's structural integrity. Here we report vertebrate protein ZC3HC1 as a novel inherent constituent of the NB, common at the nuclear envelopes (NE) of proliferating and non-dividing, terminally differentiated cells of different morphogenetic origin. Formerly described as a protein of other functions, we instead present the NB component ZC3HC1 as a protein required for enabling distinct amounts of TPR to occur NB-appended, with such ZC3HC1-dependency applying to about half the total amount of TPR at the NEs of different somatic cell types. Furthermore, pointing to an NB structure more complex than previously anticipated, we discuss how ZC3HC1 and the ZC3HC1-dependent TPR polypeptides could enlarge the NB's functional repertoire.","doi":"10.3390/cells10081937","authors":"Gunkel P, Iino H, Krull S, Cordes VC","authors_abbrev":"Gunkel P et al.","pubmed_publication_date":"30 Jul 2021","pubmed_entrez_date":"2021-08-27","publication_year":"2021","canto_session_key":"5cd85ab54733f0d7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-03-13 15:41:08","canto_approved_date":"2024-05-02 05:55:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-03-13 12:41:59","canto_added_date":"2024-02-22 13:18:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1753.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2024-03-13"},{"uniquename":"PMID:4612335","title":"Action of ethidium bromide on mitochondrial DNA in the petite-negative yeast Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1974;131(4):333-8","abstract":"","authors":"Bandlow W, Kaudewitz F","authors_abbrev":"Bandlow W et al.","pubmed_publication_date":"1974","pubmed_entrez_date":"1974-01-01","publication_year":"1974","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9371883","title":"Molecular characterization of a novel fission yeast gene spUAP2 that interacts with the splicing factor spU2AF59.","citation":"Curr Genet 1997 Nov;32(5):323-30","abstract":"A protein essential for pre-mRNA splicing, the U2 auxiliary factor (U2AF), is composed of a large and small subunit. Previously we cloned and characterized both subunits, spU2AF59 and spU2AF23, from fission yeast. We now report a novel U2AF-associated-protein, spUAP2, which interacts with both subunits. SpUAP2 contains a classical and a degenerate RNA recognition motif (RRM), both of which are required for interaction with spU2AF59. Interaction also requires the arginine/serine-rich region and the first RRM of spU2AF59. A null allele of the gene for spUAP2 is lethal.","authors":"McKinney R, Wentz-Hunter K, Schmidt H, Potashkin J","authors_abbrev":"McKinney R et al.","pubmed_publication_date":"Nov 1997","pubmed_entrez_date":"1998-02-07","publication_year":"1997","canto_session_key":"9bde74c8ee3e19f5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-09-17 15:45:50","canto_approved_date":"2025-05-16 06:43:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-30 16:15:32","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":8,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.06","SPBC146.07","SPBC1289.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-09-17"},{"uniquename":"PMID:11683390","title":"In vivo localisation of fission yeast cyclin-dependent kinase cdc2p and cyclin B cdc13p during mitosis and meiosis.","citation":"J Cell Sci 2001 Jul;114(Pt 14):2627-40","abstract":"We investigated the in vivo localisation of fission yeast cyclin-dependent kinase cdc2p during mitosis and meiosis. Fusion to yellow fluorescent protein (YFP) revealed that cdc2-YFP is present in the cytoplasm at all stages of the cell cycle. Nuclear cdc2-YFP fluorescence oscillates with that of cdc13-YFP cyclin. At G1/S, at least one of cdc13p, cig1p or cig2p B-type cyclins is required for the accumulation of cdc2-YFP into the nucleus. Cdc2-YFP and cdc13-YFP are highly enriched on the spindle pole body of cells in late G2 or arrested at S phase. Both accumulate on the spindle pole bodies and the spindle in prophase and metaphase independently of the microtubule-associated protein dis1p. In anaphase, the cdc2p/cdc13p complex leaves the spindle prior to sister chromatid separation, and cdc13-YFP is enriched at the nuclear periphery before fluorescence disappears. If cdc13p cannot be recognized by the anaphase-promoting complex, cdc2-YFP and cdc13-YFP remain associated with the spindle. In mating cells, cdc2-YFP enters the nucleus as soon as the cells undergo fusion. During karyogamy and meiotic prophase, cdc2-YFP is highly enriched on the centromeres. In meiosis I, association of cdc2-YFP with the spindle and the spindle pole bodies shows differences to mitotic cells, suggesting different mechanisms of spindle formation. This study suggests that changes in cdc2p localisation are important for both mitosis and meiosis regulation.","authors":"Decottignies A, Zarzov P, Nurse P","authors_abbrev":"Decottignies A et al.","pubmed_publication_date":"Jul 2001","pubmed_entrez_date":"2001-10-31","publication_year":"2001","canto_session_key":"f96ee693f519ef9d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2016-12-21 13:43:22","canto_approved_date":"2024-08-13 15:55:54","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-10-25 13:22:24","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":47,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.09","SPBC582.03","SPBC11B10.09","SPBC4.07c","SPCC736.14","SPCC4E9.02","SPBC336.12c","SPAPB2B4.03","SPBC649.05"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2016-12-21"},{"uniquename":"PMID:35662333","title":"Fluorescence exclusion - a rapid, accurate and powerful method for measuring yeast cell volume.","citation":"J Cell Sci 2022 Jul 01;135(13)","abstract":"Cells exist in an astonishing range of volumes across and within species. However, our understanding of cell size control remains limited, owing in large part to the challenges associated with accurate determination of cell volume. Much of our comprehension of size regulation derives from yeast models, but even for these morphologically stereotypical cells, assessment of cell volume has mostly relied on proxies and extrapolations from two-dimensional measurements. Recently, the fluorescence exclusion method (FXm) was developed to evaluate the size of mammalian cells, but whether it could be applied to smaller cells remained unknown. Using specifically designed microfluidic chips and an improved data analysis pipeline, we show here that FXm reliably detects subtle differences in the volume of fission yeast cells, even for those with altered shapes. Moreover, it allows for the monitoring of dynamic volume changes at the single-cell level with high time resolution. Collectively, our work highlights how the coupling of FXm with yeast genetics will bring new insights into the complex biology of cell growth.","doi":"10.1242/jcs.259392","authors":"García-Ruano D, Venkova L, Jain A, Ryan JC, Radhakrishnan Balasubramaniam V, Piel M, Coudreuse D","authors_abbrev":"García-Ruano D et al.","pubmed_publication_date":"01 Jul 2022","pubmed_entrez_date":"2022-06-06","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-06-08 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28423198","title":"An estradiol-inducible promoter enables fast, graduated control of gene expression in fission yeast.","citation":"Yeast 2017 Aug;34(8):323-334","abstract":"The fission yeast Schizosaccharomyces pombe lacks a diverse toolkit of inducible promoters for experimental manipulation. Available inducible promoters suffer from slow induction kinetics, limited control of expression levels and/or a requirement for defined growth medium. In particular, no S. pombe inducible promoter systems exhibit a linear dose-response, which would allow expression to be tuned to specific levels. We have adapted a fast, orthogonal promoter system with a large dynamic range and a linear dose response, based on β-estradiol-regulated function of the human oestrogen receptor, for use in S. pombe. We show that this promoter system, termed Z 3  EV, turns on quickly, can reach a maximal induction of 20-fold, and exhibits a linear dose response over its entire induction range, with few off-target effects. We demonstrate the utility of this system by regulating the mitotic inhibitor Wee1 to create a strain in which cell size is regulated by β-estradiol concentration. This promoter system will be of great utility for experimentally regulating gene expression in fission yeast. Copyright © 2017 John Wiley & Sons, Ltd.","doi":"10.1002/yea.3235","authors":"Ohira MJ, Hendrickson DG, Scott McIsaac R, Rhind N","authors_abbrev":"Ohira MJ et al.","pubmed_publication_date":"Aug 2017","pubmed_entrez_date":"2017-04-20","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-04-21 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12918382","title":"The phenomenon of spore killing in Schizosaccharomyces pombe hybrids.","citation":"Dokl Biol Sci 2001;379:385-8","abstract":"","authors":"Kondrat'eva VI, Naumov GI","authors_abbrev":"Kondrat'eva VI et al.","pubmed_publication_date":"2001","pubmed_entrez_date":"2003-08-16","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31703473","title":"Shaping the Nascent Ribosome: AAA-ATPases in Eukaryotic Ribosome Biogenesis.","citation":"Biomolecules 2019 Nov 07;9(11)","abstract":"AAA-ATPases are molecular engines evolutionarily optimized for the remodeling of proteins and macromolecular assemblies. Three AAA-ATPases are currently known to be involved in the remodeling of the eukaryotic ribosome, a megadalton range ribonucleoprotein complex responsible for the translation of mRNAs into proteins. The correct assembly of the ribosome is performed by a plethora of additional and transiently acting pre-ribosome maturation factors that act in a timely and spatially orchestrated manner. Minimal disorder of the assembly cascade prohibits the formation of functional ribosomes and results in defects in proliferation and growth. Rix7, Rea1, and Drg1, which are well conserved across eukaryotes, are involved in different maturation steps of pre-60S ribosomal particles. These AAA-ATPases provide energy for the efficient removal of specific assembly factors from pre-60S particles after they have fulfilled their function in the maturation cascade. Recent structural and functional insights have provided the first glimpse into the molecular mechanism of target recognition and remodeling by Rix7, Rea1, and Drg1. Here we summarize current knowledge on the AAA-ATPases involved in eukaryotic ribosome biogenesis. We highlight the latest insights into their mechanism of mechano-chemical complex remodeling driven by advanced cryo-EM structures and the use of highly specific AAA inhibitors.","doi":"10.3390/biom9110715","authors":"Prattes M, Lo YH, Bergler H, Stanley RE","authors_abbrev":"Prattes M et al.","pubmed_publication_date":"07 Nov 2019","pubmed_entrez_date":"2019-11-10","publication_year":"2019","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16E9.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:24937146","title":"Targeting Alp7/TACC to the spindle pole body is essential for mitotic spindle assembly in fission yeast.","citation":"FEBS Lett 2014 Aug 25;588(17):2814-21","abstract":"The conserved TACC protein family localises to the centrosome (the spindle pole body, SPB in fungi) and mitotic spindles, thereby playing a crucial role in bipolar spindle assembly. However, it remains elusive how TACC proteins are recruited to the centrosome/SPB. Here, using fission yeast Alp7/TACC, we have determined clustered five amino acid residues within the TACC domain required for SPB localisation. Critically, these sequences are essential for the functions of Alp7, including proper spindle formation and mitotic progression. Moreover, we have identified pericentrin-like Pcp1 as a loading factor to the mitotic SPB, although Pcp1 is not a sole platform.","doi":"10.1016/j.febslet.2014.06.027","authors":"Tang NH, Okada N, Fong CS, Arai K, Sato M, Toda T","authors_abbrev":"Tang NH et al.","pubmed_publication_date":"25 Aug 2014","pubmed_entrez_date":"2014-06-18","publication_year":"2014","canto_session_key":"13f535eec84725d1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2017-11-02 13:10:14","canto_approved_date":"2025-05-27 14:18:08","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-07-31 15:45:01","canto_added_date":"2014-06-24 00:15:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Takashi Toda","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC736.14","SPBC20F10.06","SPBC365.15","SPAC6G9.06c","SPAC890.02c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-11-02"},{"uniquename":"PMID:29878109","title":"Disruption of ppr3, ppr4, ppr6 or ppr10 induces flocculation and filamentous growth in Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 2018 Aug 01;365(16)","abstract":"Pentatricopeptide repeat (PPR) proteins are major players in mitochondrial and chloroplast RNA metabolism, which is essential for normal organellar function. The fission yeast Schizosaccharomyces pombe has 10 PPR proteins. We have previously reported that loss of ppr3, ppr4, ppr6 or ppr10 perturbs iron homeostasis leading to accumulation of reactive oxygen species and apoptotic cell death. In the present study, we show that loss of ppr3, ppr4, ppr6 or ppr10 can cause non-sexual flocculation and filamentous growth of cells. Furthermore, expression of a number of genes encoding cell-surface flocculins and cell wall-remodeling enzymes are induced in these ppr-deletion mutants. We also show that Δppr10 cells, and, to a lesser extent, Δppr4 and Δppr6 cells, exhibited increased tolerance to H2O2 toxicity compared with the wild-type strain. Finally, we found that overexpression of genes involved in iron uptake and/or iron homeostasis could cause the flocculation of wild-type cells. Our findings suggest that an elevated level of intracellular iron in the mutant caused by loss of ppr3, ppr4, ppr6 or ppr10 may result in flocculation and filamentous growth in S. pombe.","doi":"10.1093/femsle/fny141","authors":"Su Y, Chen J, Huang Y","authors_abbrev":"Su Y et al.","pubmed_publication_date":"01 Aug 2018","pubmed_entrez_date":"2018-06-08","publication_year":"2018","canto_session_key":"48cf4f96208f7406","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ying Huang","canto_first_approved_date":"2018-06-26 14:07:26","canto_approved_date":"2020-09-29 18:29:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-19 08:19:37","canto_added_date":"2018-06-09 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Ying Huang","community_curator":true,"annotation_count":8,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC106.19","SPBC19G7.07c","SPAC8C9.06c","SPAC24B11.11c","SPAC1F8.02c","SPAC1F7.07c","SPCC11E10.04","SPAC1F7.08","SPBC4F6.09","SPBC947.05c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2018-06-26"},{"uniquename":"PMID:38803357","title":"The NDR family of kinases: essential regulators of aging.","citation":"Front Mol Neurosci 2024;17:1371086","abstract":"Aging is defined as a progressive decline of cognitive and physiological functions over lifetime. Since the definition of the nine hallmarks of aging in 2013 by López-Otin, numerous studies have attempted to identify the main regulators and contributors in the aging process. One interesting group of proteins whose participation has been implicated in several aging hallmarks are the nuclear DBF2-related (NDR) family of serine-threonine AGC kinases. They are one of the core components of the Hippo signaling pathway and include NDR1, NDR2, LATS1 and LATS2 in mammals, along with its highly conserved metazoan orthologs; Trc in  Drosophila melanogaster , SAX-1 in  Caenorhabditis elegans , CBK1, DBF20 in  Saccharomyces cerevisiae  and orb6 in  Saccharomyces pombe . These kinases have been independently linked to the regulation of widely diverse cellular processes disrupted during aging such as the cell cycle progression, transcription, intercellular communication, nutrient homeostasis, autophagy, apoptosis, and stem cell differentiation. However, a comprehensive overview of the state-of-the-art knowledge regarding the post-translational modifications of and by NDR kinases in aging has not been conducted. In this review, we summarize the current understanding of the NDR family of kinases, focusing on their relevance to various aging hallmarks, and emphasize the growing body of evidence that suggests NDR kinases are essential regulators of aging across species.","doi":"10.3389/fnmol.2024.1371086","authors":"Jonischkies K, Del Angel M, Demiray YE, Loaiza Zambrano A, Stork O","authors_abbrev":"Jonischkies K et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-05-28","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-05-28 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26115316","title":"Saccharomyces cerevisiae Eukaryotic Elongation Factor 1A (eEF1A) Is Methylated at Lys-390 by a METTL21-Like Methyltransferase.","citation":"PLoS One 2015;10(6):e0131426","abstract":"The human methyltransferases (MTases) METTL21A and VCP-KMT (METTL21D) were recently shown to methylate single lysine residues in Hsp70 proteins and in VCP, respectively. The yet uncharacterized MTase encoded by the YNL024C gene in Saccharomyces cerevisiae shows high sequence similarity to METTL21A and VCP-KMT, as well as to their uncharacterized paralogues METTL21B and METTL21C. Despite being most similar to METTL21A, the Ynl024c protein does not methylate yeast Hsp70 proteins, which were found to be unmethylated on the relevant lysine residue. Eukaryotic translation elongation factor eEF1A in yeast has been reported to contain four methylated lysine residues (Lys30, Lys79, Lys318 and Lys390), and we here show that the YNL024C gene is required for methylation of eEF1A at Lys390, the only of these methylations for which the responsible MTase has not yet been identified. Lys390 was found in a partially monomethylated state in wild-type yeast cells but was exclusively unmethylated in a ynl024cΔ strain, and over-expression of Ynl024c caused a dramatic increase in Lys390 methylation, with trimethylation becoming the predominant state. Our results demonstrate that Ynl024c is the enzyme responsible for methylation of eEF1A at Lys390, and in accordance with prior naming of similar enzymes, we suggest that Ynl024c is renamed to Efm6 (Elongation factor MTase 6).","doi":"10.1371/journal.pone.0131426","authors":"Jakobsson ME, Davydova E, Małecki J, Moen A, Falnes PØ","authors_abbrev":"Jakobsson ME et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-06-27","publication_year":"2015","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC794.09c","SPBC839.15c","SPAC23A1.10","SPAC23C4.06c"],"gene_count":4,"ltp_gene_count":0},{"uniquename":"PMID:9211790","title":"Caffeine-resistance in S. pombe: mutations in three novel caf genes increase caffeine tolerance and affect radiation sensitivity, fertility, and cell cycle.","citation":"Curr Genet 1997 Jun;31(6):481-7","abstract":"Caffeine is a well known base analogue and is cytotoxic to both animal and yeast cells. There are two possible mechanisms by which yeast cells tolerate caffeine concentrations higher than normal, by mutation or by physiological adaptation. We have isolated novel caffeine-resistant mutants of S. pombe which define three distinct genes caf2, caf3 and caf4. These mutants achieved a level of caffeine resistance which is presumed to represent the upper limit attainable by mutation. The caf2-caf4 mutations, as well as the previously identified caf1 mutation, confer UV-sensitivity, caffeine-resistant UV repair, impaired fertility and sporulation, as well as a lengthened cell cycle. They are partially dominant for caffeine resistance and recessive for UV sensitivity. Some auxotrophic caf3-89 double mutants show drastically decreased caffeine resistance. The caf4 mutant is more resistant to gamma-radiation than wild-type cells and shows pH-sensitive growth. As each caf mutation can, individually, confer maximum caffeine resistance to the cells, all four genes are expected to operate in the same pathway. This pathway might also be responsible for the physiological adaptation since adaptation is lost in caf1-caf4 mutants.","authors":"Benko Z, Miklos I, Carr AM, Sipiczki M","authors_abbrev":"Benko Z et al.","pubmed_publication_date":"Jun 1997","pubmed_entrez_date":"1997-06-01","publication_year":"1997","canto_session_key":"9076c0731474baf4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-01-07 16:10:07","canto_approved_date":"2021-09-26 04:47:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-06-12 11:36:41","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":37,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCPB16A4.03c","SPCC330.05c","SPBC418.01c","SPBC1539.09c","SPAC22G7.06c","SPBC14F5.09c","SPAC1783.07c","SPBC365.13c","SPBC3F6.03","SPBC215.08c","SPAC1805.17"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2014-01-07"},{"uniquename":"PMID:30639107","title":"Reprogramming Cdr2-Dependent Geometry-Based Cell Size Control in Fission Yeast.","citation":"Curr Biol 2019 Jan 21;29(2):350-358.e4","abstract":"How cell size is determined and maintained remains unclear, even in simple model organisms. In proliferating cells, cell size is regulated by coordinating growth and division through sizer, adder, or timer mechanisms or through some combination [1, 2]. Currently, the best-characterized example of sizer behavior is in fission yeast, Schizosaccharomyces pombe, which enters mitosis at a minimal cell size threshold. The peripheral membrane kinase Cdr2 localizes in clusters (nodes) on the medial plasma membrane and promotes mitotic entry [3]. Here, we show that the Cdr2 nodal density, which scales with cell size, is used by the cell to sense and control its size. By analyzing cells of different widths, we first show that cdr2 +  cells divide at a fixed cell surface area. However, division in the cdr2Δ mutant is more closely specified by cell volume, suggesting that Cdr2 is essential for area sensing and supporting the existence of a Cdr2-independent secondary sizer mechanism more closely based on volume. To investigate how Cdr2 nodes may sense area, we derive a minimal mathematical model that incorporates the cytoplasmic kinase Ssp1 as a Cdr2 activator. The model predicts that a cdr2 mutant in an Ssp1 phosphorylation site (cdr2-T166A) [4] should form nodes whose density registers cell length. We confirm this prediction experimentally and find that thin cells now follow this new scaling by dividing at constant length instead of area. This work supports the role of Cdr2 as a sizer factor and highlights the importance of studying geometrical aspects of size control.","doi":"10.1016/j.cub.2018.12.017","authors":"Facchetti G, Knapp B, Flor-Parra I, Chang F, Howard M","authors_abbrev":"Facchetti G et al.","pubmed_publication_date":"21 Jan 2019","pubmed_entrez_date":"2019-01-15","publication_year":"2019","canto_session_key":"d61fe0b11445626b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Giuseppe Facchetti","canto_first_approved_date":"2024-10-16 09:37:21","canto_approved_date":"2024-10-16 09:37:21","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-09-10 20:11:43","canto_added_date":"2019-01-16 01:15:05","annotation_curators":[{"name":"Giuseppe Facchetti","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":17,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC28E12.03","SPAC57A10.02","SPAC26A3.09c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2024-10-16"},{"uniquename":"PMID:17656356","title":"Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins.","citation":"J Biol Chem 2007 Sep 21;282(38):28014-24","abstract":"We investigated how heterodimeric capping proteins bind to and dissociate from the barbed ends of actin filaments by observing single muscle actin filaments by total internal reflection fluorescence microscopy. The barbed end rate constants for mouse capping protein (CP) association of 2.6 x 10(6) M(-1) s(-1) and dissociation of 0.0003 s(-1) agree with published values measured in bulk assays. The polyphosphoinositides (PPIs), phosphatidylinositol 3,4-bisphosphate (PI(3,4)P(2)), PI(4,5)P(2), and PI(3,4,5)P(3), prevent CP from binding to barbed ends, but three different assays showed that none of these lipids dissociate CP from filaments at concentrations that block CP binding to barbed ends. The affinity of fission yeast CP for barbed ends is a thousandfold less than mouse CP, because of a slower association rate constant (1.1 x 10(5) M(-1) s(-1)) and a faster dissociation rate constant (0.004 s(-1)). PPIs do not inhibit binding of fission yeast CP to filament ends. Comparison of homology models revealed that fission yeast CP lacks a large patch of basic residues along the actin-binding surface on mouse CP. PPIs binding to this site might interfere sterically with capping, but this site would be inaccessible when CP is bound to the end of a filament.","authors":"Kuhn JR, Pollard TD","authors_abbrev":"Kuhn JR et al.","pubmed_publication_date":"21 Sep 2007","pubmed_entrez_date":"2007-07-28","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11606752","title":"Redundant control of rereplication in fission yeast.","citation":"Proc Natl Acad Sci U S A 2001 Nov 06;98(23):13114-9","abstract":"The initiation of DNA replication at replication origins in eukaryotic cells is tightly controlled to ensure that the genome is duplicated only once each cell cycle. We present evidence that in fission yeast, independent regulation of two essential components of the initiation complex, Cdc18 and Cdt1, contributes to the prevention of reinitiation of DNA replication. Cdc18 is negatively controlled by cyclin-dependent kinase (CDK) phosphorylation, but low level expression of a mutant form of Cdc18 lacking CDK phosphorylation sites (Cdc18(CDK)) is not sufficient to induce rereplication. Similar to Cdc18, Cdt1 is expressed periodically in the cell cycle, accumulating in the nucleus in G(1) and declining in G(2). When Cdt1 is expressed constitutively from an ectopic promoter, it accumulates in the nucleus throughout the cell cycle but does not promote reinitiation. However, constitutive expression of Cdt1, together with Cdc18(CDK), is sufficient to induce extra rounds of DNA replication in the absence of mitosis. Significantly greater levels of rereplication can be induced by coexpression of Cdc18(CDK) and a Cdt1 mutant lacking a conserved C-terminal motif. In contrast, uncontrolled DNA replication does not occur when either mutant protein is expressed in the absence of the other. Constitutive expression of wild-type or mutant Cdt1 also leads to an increase in the levels of Cdc18(CDK), possibly as a result of increased protein stability. Our data are consistent with the hypothesis that control of rereplication depends on a redundant mechanism in which negative regulation of Cdt1 functions in parallel with the negative regulation of Cdc18.","authors":"Gopalakrishnan V, Simancek P, Houchens C, Snaith HA, Frattini MG, Sazer S, Kelly TJ","authors_abbrev":"Gopalakrishnan V et al.","pubmed_publication_date":"06 Nov 2001","pubmed_entrez_date":"2001-10-19","publication_year":"2001","canto_session_key":"755324957441e428","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-08-07 14:59:08","canto_approved_date":"2022-09-08 10:42:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-07 14:59:00","canto_added_date":"2012-02-24 05:51:41","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c","SPBC428.18","SPBC211.04c","SPBC25D12.03c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-08-07"},{"uniquename":"PMID:11084332","title":"Cut8, essential for anaphase, controls localization of 26S proteasome, facilitating destruction of cyclin and Cut2.","citation":"Curr Biol 2000 Nov 02;10(21):1329-38","abstract":"Anaphase-promoting complex (APC)/cyclosome and 26S proteasome are respectively required for polyubiquitination and degradation of mitotic cyclin and anaphase inhibitor Cut2 (Pds1/securin). In fission yeast, mutant cells defective in cyclosome and proteasome fail to complete mitosis and have hypercondensed chromosomes and a short spindle. A similar phenotype is seen in a temperature-sensitive strain cut8-563 at 36 degrees C, but the molecular basis for Cut8 function is little understood.\nAt high temperature, the level of Cut8 greatly increases and it becomes essential to the progression of anaphase. In cut8 mutants, chromosome mis-segregation and aberrant spindle dynamics occur, but cytokinesis takes place with normal timing, leading to the cut phenotype. This is due to the fact that destruction of mitotic cyclin and Cut2 in the nucleus is dramatically delayed, though polyubiquitination of Cdc13 occurs in cut8 mutant. Cut8 is localized chiefly to the nucleus and nuclear periphery, a distribution highly similar to that of 26S proteasome. In cut8 mutant, however, 26S proteasome becomes mostly cytoplasmic, showing that Cut8 is needed for its proper localization.\nCut8 is a novel evolutionarily conserved heat-inducible regulator. It facilitates anaphase-promoting proteolysis by recruiting 26S proteasome to a functionally efficient nuclear location.","authors":"Tatebe H, Yanagida M","authors_abbrev":"Tatebe H et al.","pubmed_publication_date":"02 Nov 2000","pubmed_entrez_date":"2000-11-21","publication_year":"2000","canto_session_key":"dd0dc92db12b47e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-05 15:53:43","canto_approved_date":"2023-01-26 10:31:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-25 09:38:21","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17C9.13c","SPAC6F12.15c","SPBC776.02c","SPBC4.07c","SPBC11B10.09","SPAC31G5.13","SPBP19A11.03c","SPBC336.12c","SPAC821.08c","SPBC16G5.01","SPBC14C8.01c","SPBC106.09","SPBC582.03"],"gene_count":13,"ltp_gene_count":12,"approved_date":"2017-01-05"},{"uniquename":"PMID:10794172","title":"The Schizosaccharomyces pombe rfc3+ gene encodes a homologue of the human hRFC36 and Saccharomyces cerevisiae Rfc3 subunits of replication factor C.","citation":"Curr Genet 2000 Mar;37(3):159-67","abstract":"In the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe replication factor C (RF-C) plays key roles both in chromosomal DNA replication and in DNA replication checkpoint function. At the replication fork, the five-subunit RF-C complex functions to load the trimeric polymerase accessory factor PCNA onto DNA. PCNA then acts as a sliding clamp, tethering Pol delta to the DNA to maximise its processivity. Here we describe the cloning of the S. pombe rfc3+ gene, encoding a homologue of the S. cerevisiae Rfc3 and human hRFC36 proteins. The 1026 bp rfc3+ ORF is interrupted by five introns, ranging in size from 49 to 165 bp. The spliced ORF is predicted to encode a 342 amino-acid protein that is approximately 50% identical at the amino acid sequence level to the S. cerevisiae Rfc3 and human hRFC36 proteins. As expected, S. pombe rfc3+ is an essential gene, with rfc3delta cells being defective for DNA replication. Loss of rfc3+ function can be rescued by heterologous expression of either the S. cerevisiae Rfc3 or human hRFC36 proteins in S. pombe.","authors":"Gray FC, MacNeill SA","authors_abbrev":"Gray FC et al.","pubmed_publication_date":"Mar 2000","pubmed_entrez_date":"2000-05-04","publication_year":"2000","canto_session_key":"821b2d16547fc51d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2016-02-05 15:39:38","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2016-02-04 17:22:30","canto_added_date":"2012-02-24 05:52:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":5,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27E2.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-02-04"},{"uniquename":"EMBL:AU013226","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19007748","title":"Glycolipid transfer proteins and membrane interaction.","citation":"Biochim Biophys Acta 2009 Jan;1788(1):267-72","abstract":"The glycolipid transfer protein is found from animals and fungi to plants and red micro-alga. Some eukaryotes that do not encode the glucosylceramide synthase like the yeast Schizosaccharomyces pombe and Saccharomyces cerevisiae do neither produce glycolipid transfer like proteins. On the other hand yeast like Eremothecium gossypii that do synthesize glucosylceramide also express glycolipid transfer protein. Based on this novel genetic relationship it is not far fetched to assume that there must be a strong correlation between the synthesis of the glycolipid precursor and the glycolipid transfer protein. Because the glycolipid transfer protein is localized in the cytosol it is unlikely that it would participate in events associated with lipid rafts or caveolar structures, since they are found on the outer leaflet of the plasma membrane. Rather, GLTP is likely to be involved in events at the cytosolic side of the plasma membrane or the endoplasmic reticulum, maybe function as a reporter or sensor of glycolipid levels. A similar function has been proposed for other proteins with affinity for lipids like the oxysterol binding proteins and phosphatidylinositol transfer proteins that are thought to be able act as lipid sensors. Recent discoveries in the glycolipid transfer protein field are discussed.","doi":"10.1016/j.bbamem.2008.10.003","authors":"Mattjus P","authors_abbrev":"Mattjus P","pubmed_publication_date":"Jan 2009","pubmed_entrez_date":"2008-11-15","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3896246","title":"Mutagenicity studies on denzimol, a new anticonvulsant drug.","citation":"Arzneimittelforschung 1985;35(5):793-6","abstract":"N-[beta-[4-(beta-Phenylethyl)phenyl]-beta-hydroxyethyl] imidazole hydrochloride (denzimol, Rec 15-1533), a new anticonvulsant drug, was tested using the Ames procedures with and without metabolic activation, on five strains of Salmonella tythimurium and using the host mediated assay with Schizosaccharomyces pombe as microorganism test. In both tests the drug did not show any mutagenic activity when compared with mutagenic standards.","authors":"Veronese M, Barzaghi D, Bertoncini A, Zadro M","authors_abbrev":"Veronese M et al.","pubmed_publication_date":"1985","pubmed_entrez_date":"1985-01-01","publication_year":"1985","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15840944","title":"Hsp16p is required for thermotolerance in nuclear mRNA export in fission yeast Schizosaccharomyces pombe.","citation":"Cell Struct Funct 2005 Feb;29(5-6):125-38","abstract":"Export of mRNA from the nucleus to the cytoplasm is one of the essential steps for eukaryotic gene expression. In the fission yeast Schizosaccharomyces pombe, heat shock stress at 42 degrees C causes block of mRNA export from the nucleus. We now report that saline and ethanol stresses also inhibit nuclear mRNA export, resulting in accumulation of bulk poly (A)+ RNA, as well as a specific mRNA, in the nucleus. Under stressed conditions, an mRNA export receptor Mex67p relocates to the nucleolus from the nuclear periphery and this relocation is closely correlated with inhibition of mRNA export by the stresses. Pretreatment of cells with a mild saline stress induced thermotolerance in mRNA export in a similar manner seen with mild heat pretreatment and protected mRNA export machinery from the subsequent severe heat shock. In contrast, mild ethanol stress could not induce the thermotolerance in mRNA export, suggesting that the stress response induced by ethanol differs from that induced by saline and heat shock stresses. In addition, we found that the Spc1p MAPK pathway is involved in induction of thermotolerance in mRNA export. Of the downstream targets for Spc1p, the Atf1p transcription factor was essential for induction of thermotolerance in mRNA export. We also found that Hsp16p, the expression of which is controlled by Atf1p, is involved in acquisition of thermotolerance in mRNA export in S. pombe.","authors":"Yoshida J, Tani T","authors_abbrev":"Yoshida J et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2005-04-21","publication_year":"2005","canto_session_key":"02a74a589bd79b26","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-28 15:55:18","canto_approved_date":"2017-09-28 15:55:18","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-09-28 15:55:12","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3E7.02c","SPBC29B5.01","SPAC1783.07c","SPAC24B11.06c","SPBC1921.03c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-09-28"},{"uniquename":"PMID:29188185","title":"Metabolic engineering of  Schizosaccharomyces pombe  via CRISPR-Cas9 genome editing for lactic acid production from glucose and cellobiose.","citation":"Metab Eng Commun 2017 Dec;5:60-67","abstract":"Modification of the Schizosaccharomyces pombe genome is often laborious, time consuming due to the lower efficiency of homologous recombination. Here, we constructed metabolically engineered S. pombe strains using a CRISPR-Cas9 system and also demonstrated D-lactic acid (D-LA) production from glucose and cellobiose. Genes encoding two separate pyruvate decarboxylases (PDCs), an L-lactic acid dehydrogenase (L-LDH), and a minor alcohol dehydrogenase (SPBC337.11) were disrupted, thereby attenuating ethanol production. To increase the cellular supply of acetyl-CoA, an important metabolite for growth, we introduced genes encoding bacterial acetylating acetaldehyde dehydrogenase enzymes (Escherichia coli MhpF and EutE). D-LA production by the resulting strain was achieved by expressing a Lactobacillus plantarum gene encoding D-lactate dehydrogenase. The engineered strain efficiently consumed glucose and produced D-LA at 25.2 g/L from 35.5 g/L of consumed glucose with a yield of 0.71 g D-LA / g glucose. We further modified this strain by expressing beta-glucosidase by cell surface display; the resulting strain produced D-LA at 24.4 g/L from 30 g/L of cellobiose in minimal medium, with a yield of 0.68 g D-LA / g glucose. To our knowledge, this study represents the first report of a S. pombe strain that was metabolically engineered using a CRISPR-Cas9 system, and demonstrates the possibility of engineering S. pombe for the production of value-added chemicals.","doi":"10.1016/j.meteno.2017.08.002","authors":"Ozaki A, Konishi R, Otomo C, Kishida M, Takayama S, Matsumoto T, Tanaka T, Kondo A","authors_abbrev":"Ozaki A et al.","pubmed_publication_date":"Dec 2017","pubmed_entrez_date":"2017-12-01","publication_year":"2017","canto_session_key":"5c28c36edd6c3e15","canto_annotation_status":"APPROVED","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_first_approved_date":"2024-11-18 13:24:30","canto_approved_date":"2024-11-18 13:24:30","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-11-18 13:24:21","canto_added_date":"2017-12-02 01:15:45","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC186.08c","SPBC337.11"],"gene_count":2,"ltp_gene_count":0,"approved_date":"2024-11-18"},{"uniquename":"PMID:18262494","title":"Fission yeast dam1-A8 mutant is resistant to and rescued by an anti-microtubule agent.","citation":"Biochem Biophys Res Commun 2008 Apr 11;368(3):670-6","abstract":"The Dam1/DASH outer kinetochore complex is required for high-fidelity chromosome segregation in budding and fission yeast. Unlike budding yeast, the fission yeast complex is non-essential, however it promotes bipolar microtubule attachment in conjunction with microtubule-depolymerising kinesin-8 Klp5 and Klp6. Here, we screened for dam1 temperature sensitive mutants in a klp5 null background and identified dam1-A8 that contains two amino acid substitutions in the C-terminus (H126R and E149G). dam1-A8klp5 mutant cells display massive chromosome missegregation with lagging chromosomes and monopolar attachment of sister chromatids to one SPB (spindle pole body). Unexpectedly contrary to a deletion mutant that is hypersensitive to microtubule-destabilising drugs, dam1-A8 is resistant and furthermore the temperature sensitivity of dam1-A8klp5 is rescued by addition of these drugs. This indicates that the hyper-stabilised rigidity of kinetochore-spindle mal-attachments is the primary cause of lethality. Our result shows that fine-tuning of Dam1 activity is essential for chromosome bi-orientation.","doi":"10.1016/j.bbrc.2008.01.156","authors":"Griffiths K, Masuda H, Dhut S, Toda T","authors_abbrev":"Griffiths K et al.","pubmed_publication_date":"11 Apr 2008","pubmed_entrez_date":"2008-02-12","publication_year":"2008","canto_session_key":"495506fbf084566b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2016-04-19 10:32:00","canto_approved_date":"2020-06-19 12:39:29","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-04-05 16:44:51","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC589.08c","SPBC1685.15c","SPBC2F12.13"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2016-04-19"},{"uniquename":"PMID:15964794","title":"ATM activation and its recruitment to damaged DNA require binding to the C terminus of Nbs1.","citation":"Mol Cell Biol 2005 Jul;25(13):5363-79","abstract":"ATM has a central role in controlling the cellular responses to DNA damage. It and other phosphoinositide 3-kinase-related kinases (PIKKs) have giant helical HEAT repeat domains in their amino-terminal regions. The functions of these domains in PIKKs are not well understood. ATM activation in response to DNA damage appears to be regulated by the Mre11-Rad50-Nbs1 (MRN) complex, although the exact functional relationship between the MRN complex and ATM is uncertain. Here we show that two pairs of HEAT repeats in fission yeast ATM (Tel1) interact with an FXF/Y motif at the C terminus of Nbs1. This interaction resembles nucleoporin FXFG motif binding to HEAT repeats in importin-beta. Budding yeast Nbs1 (Xrs2) appears to have two FXF/Y motifs that interact with Tel1 (ATM). In Xenopus egg extracts, the C terminus of Nbs1 recruits ATM to damaged DNA, where it is subsequently autophosphorylated. This interaction is essential for ATM activation. A C-terminal 147-amino-acid fragment of Nbs1 that has the Mre11- and ATM-binding domains can restore ATM activation in an Nbs1-depleted extract. We conclude that an interaction between specific HEAT repeats in ATM and the C-terminal FXF/Y domain of Nbs1 is essential for ATM activation. We propose that conformational changes in the MRN complex that occur upon binding to damaged DNA are transmitted through the FXF/Y-HEAT interface to activate ATM. This interaction also retains active ATM at sites of DNA damage.","authors":"You Z, Chahwan C, Bailis J, Hunter T, Russell P","authors_abbrev":"You Z et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-06-21","publication_year":"2005","canto_session_key":"50f9b65c9dfeebee","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-06-17 14:58:53","canto_approved_date":"2022-02-24 11:54:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-17 14:58:46","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":40,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13C5.07","SPBC216.05","SPBC6B1.09c","SPCC23B6.03c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2016-06-17"},{"uniquename":"PMID:23231582","title":"Genome-wide characterization of the phosphate starvation response in Schizosaccharomyces pombe.","citation":"BMC Genomics 2012 Dec 12;13:697","abstract":"Inorganic phosphate is an essential nutrient required by organisms for growth. During phosphate starvation, Saccharomyces cerevisiae activates the phosphate signal transduction (PHO) pathway, leading to expression of the secreted acid phosphatase, PHO5. The fission yeast, Schizosaccharomyces pombe, regulates expression of the ScPHO5 homolog (pho1+) via a non-orthologous PHO pathway involving genetically identified positive (pho7+) and negative (csk1+) regulators. The genes induced by phosphate limitation and the molecular mechanism by which pho7+ and csk1+ function are unknown. Here we use a combination of molecular biology, expression microarrays, and chromatin immunoprecipitation coupled with high-throughput sequencing (ChIP-Seq) to characterize the role of pho7+ and csk1+ in the PHO response.\nWe define the set of genes that comprise the initial response to phosphate starvation in S. pombe. We identify a conserved PHO response that contains the ScPHO5 (pho1+), ScPHO84 (SPBC8E4.01c), and ScGIT1 (SPBC1271.09) orthologs. We identify members of the Pho7 regulon and characterize Pho7 binding in response to phosphate-limitation and Csk1 activity. We demonstrate that activation of pho1+ requires Pho7 binding to a UAS in the pho1+ promoter and that Csk1 repression does not regulate Pho7 enrichment. Further, we find that Pho7-dependent activation is not limited to phosphate-starvation, as additional environmental stress response pathways require pho7+ for maximal induction.\nWe provide a global analysis of the transcriptional response to phosphate limitation in S. pombe. Our results elucidate the conserved core regulon induced in response to phosphate starvation in this ascomycete distantly related to S. cerevisiae and provide a better understanding of flexibility in environmental stress response networks.","doi":"10.1186/1471-2164-13-697","authors":"Carter-O'Connell I, Peel MT, Wykoff DD, O'Shea EK","authors_abbrev":"Carter-O'Connell I et al.","pubmed_publication_date":"12 Dec 2012","pubmed_entrez_date":"2012-12-13","publication_year":"2012","canto_session_key":"efb40309f7d22a73","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-02-03 16:01:06","canto_approved_date":"2025-09-04 12:13:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-02-03 16:00:55","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":48,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":148,"orcid":"0000-0003-4148-4606","file_type":"qualitative_gene_expression","file_name":"PMID_23231582_Carter-OConnell_qualitative_expression.txt"}],"genes":["SPAC23H3.15c","SPCC1393.10","SPAC1F7.07c","SPAC6F12.03c","SPAC4D7.02c","SPBC11C11.06c","SPCC330.06c","SPAC212.10","SPBP23A10.16","SPCC18.01c","SPAC31G5.12c","SPAC806.11","SPAC1142.05","SPACUNK4.15","SPBC660.05","SPAC19G12.09","SPAC19G12.06c","SPBC1271.09","SPBC800.11","SPAC11H11.06","SPBC1604.05","SPBC23G7.11","SPAC6B12.03c","SPAC1F8.03c","SPAC1486.01","SPBC8E4.01c","SPCC736.15","SPBC16D10.06","SPAC15A10.05c","SPAC24B11.05","SPAC637.03","SPBC32F12.12c","SPAP32A8.02","SPBC215.05","SPBPB7E8.01","SPBC1105.05","SPAPB8E5.04c","SPCC1322.04","SPCC757.07c","SPBC16H5.02","SPCC622.08c","SPCP31B10.06","SPBPB21E7.08","SPAC167.06c","SPAC10F6.06","SPAC30D11.01c","SPBC2A9.02","SPAC22H12.01c","SPCC11E10.01","SPAC212.09c","SPAC458.04c","SPAC750.08c","SPBC1815.01","SPBC16A3.02c","SPBC725.10","SPAC29A4.17c","SPBC16D10.08c","SPAC22A12.11","SPAPB15E9.01c","SPBC660.06","SPAC23C4.05c","SPAC14C4.01c","SPAC1635.01","SPCC1322.10","SPAC27D7.09c","SPAC977.13c","SPCC965.07c","SPAC328.03","SPBC32H8.12c","SPCC1840.06","SPAC1002.17c","SPBC14F5.04c","SPCC794.12c","SPBC119.03","SPACUNK4.16c","SPCC965.06","SPAC1F7.08","SPAC3C7.05c","SPAC23D3.11","SPAC57A10.09c","SPBC16H5.06","SPBC21H7.06c","SPAC513.07","SPBC8E4.04","SPAC23G3.03","SPAC17A2.13c","SPAC26F1.07","SPCC63.14","SPAC3G6.07","SPAC1D4.06c","SPAC4A8.04","SPBC1685.14c","SPBC3E7.02c","SPBC725.09c","SPAC3C7.14c","SPBPB2B2.05","SPBPB2B2.06c","SPCC1235.01","SPAP8A3.04c","SPBC660.07","SPAC513.02","SPAC1705.03c","SPAC29B12.03","SPBC215.11c","SPAPJ691.02","SPAC140.01","SPBC21B10.04c","SPCC576.03c","SPAC13C5.04","SPAC25G10.01","SPAC15E1.02c","SPBCPT2R1.07c","SPBC21C3.19","SPBC30D10.14","SPAC17G6.13","SPBP8B7.24c","SPBC27B12.11c","SPCC1322.14c","SPAC9E9.11","SPAC9E9.02","SPAC4F8.07c","SPCC338.12","SPAC2E1P3.05c","SPBC1685.13","SPBC32F12.03c","SPAC23C11.05","SPAC25B8.12c","SPAC4H3.08","SPBC56F2.06","SPBC36.03c","SPCC1393.12","SPAC26F1.04c","SPBC1652.01","SPBCPT2R1.10","SPBC2D10.05","SPAC19B12.08","SPAC22H10.13","SPAPB1E7.05","SPAC22F8.05","SPBC216.03","SPCC1020.06c","SPCC338.18","SPAC13G7.02c","SPCC830.08c","SPCC13B11.01","SPBC3D6.02","SPBC725.03","SPBC1773.02c","SPAC14C4.11","SPAC3C7.13c","SPBC12C2.12c","SPBC19C7.04c","SPBC16E9.16c","SPAC9E9.09c","SPCC24B10.21","SPCC622.09","SPCC191.01","SPBP4G3.02","SPAC8C9.03","SPBC9B6.08"],"gene_count":160,"ltp_gene_count":2,"approved_date":"2021-02-03"},{"uniquename":"PMID:6094012","title":"The NDA3 gene of fission yeast encodes beta-tubulin: a cold-sensitive nda3 mutation reversibly blocks spindle formation and chromosome movement in mitosis.","citation":"Cell 1984 Dec;39(2 Pt 1):349-58","abstract":"The cells of a cold-sensitive mutant nda3-KM311 of the fission yeast Schizosaccharomyces pombe were arrested highly synchronously at a step similar to mitotic prophase when incubated at a restrictive temperature. DAPI staining and indirect immunofluorescence microscopy showed three condensed chromosomes but no spindle. Six minutes after the temperature shifted to a permissive one, the spindle appeared and elongated. The chromosomes were separated at a constant speed (relative velocity 1 micron/min), and the spindle disappeared after the chromosomes reached opposite ends of the cell. The NDA3 gene of S. pombe was cloned by transformation. The 2.6 kb Hind III genomic DNA that complemented the nda3 mutations had only one coding frame split with five short introns. The predicted amino acid sequence contained 448 residues, and was 75% homologous to that of chicken beta-tubulin.","authors":"Hiraoka Y, Toda T, Yanagida M","authors_abbrev":"Hiraoka Y et al.","pubmed_publication_date":"Dec 1984","pubmed_entrez_date":"1984-12-01","publication_year":"1984","canto_session_key":"d6f2102e260ba45e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-03-07 17:13:32","canto_approved_date":"2023-12-24 11:45:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-12-24 11:45:03","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":6,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC26H8.07c","SPBC800.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-03-07"},{"uniquename":"PMID:34731607","title":"Stress-dependent inhibition of polarized cell growth through unbalancing the GEF/GAP regulation of Cdc42.","citation":"Cell Rep 2021 Nov 02;37(5):109951","abstract":"Cdc42 GTPase rules cell polarity and growth in fission yeast. It is negatively and positively regulated by GTPase-activating proteins (GAPs) and guanine nucleotide exchange factors (GEFs), respectively. Active Cdc42-GTP localizes to the poles, where it associates with numerous proteins constituting the polarity module. However, little is known about its downregulation. We describe here that oxidative stress causes Sty1-kinase-dependent Cdc42 inactivation at cell poles. Both the amount of active Cdc42 at tips and cell length inversely correlate with Sty1 activity, explaining the elongated morphology of Δsty1 cells. We have created stress-blinded cell poles either by eliminating two Cdc42 GAPs or through the constitutive tethering of Gef1 to cell tips, and we biochemically demonstrate that the GAPs Rga3/6 and the GEF Gef1 are direct substrates of Sty1. We propose that phosphorylation of Rga3/6 and Gef1 mediates the Sty1-dependent inhibition of Cdc42 at cell tips, halting polarized growth during stress adaptation.","doi":"10.1016/j.celrep.2021.109951","authors":"Salat-Canela C, Carmona M, Martín-García R, Pérez P, Ayté J, Hidalgo E","authors_abbrev":"Salat-Canela C et al.","pubmed_publication_date":"02 Nov 2021","pubmed_entrez_date":"2021-11-03","publication_year":"2021","canto_session_key":"c079bea431744930","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2021-11-05 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16E8.09","SPAC24B11.06c","SPAC110.03","SPAC29A4.11","SPBC354.13"],"gene_count":5,"ltp_gene_count":0},{"uniquename":"PMID:22682253","title":"Functional repurposing revealed by comparing S. pombe and S. cerevisiae genetic interactions.","citation":"Cell 2012 Jun 08;149(6):1339-52","abstract":"We present a genetic interaction map of pairwise measures including ∼40% of nonessential S. pombe genes. By comparing interaction maps for fission and budding yeast, we confirmed widespread conservation of genetic relationships within and between complexes and pathways. However, we identified an important subset of orthologous complexes that have undergone functional \"repurposing\": the evolution of divergent functions and partnerships. We validated three functional repurposing events in S. pombe and mammalian cells and discovered that (1) two lumenal sensors of misfolded ER proteins, the kinase/nuclease Ire1 and the glucosyltransferase Gpt1, act together to mount an ER stress response; (2) ESCRT factors regulate spindle-pole-body duplication; and (3) a membrane-protein phosphatase and kinase complex, the STRIPAK complex, bridges the cis-Golgi, the centrosome, and the outer nuclear membrane to direct mitotic progression. Each discovery opens new areas of inquiry and-together-have implications for model organism-based research and the evolution of genetic systems.","doi":"10.1016/j.cell.2012.04.028","authors":"Frost A, Elgort MG, Brandman O, Ives C, Collins SR, Miller-Vedam L, Weibezahn J, Hein MY, Poser I, Mann M, Hyman AA, Weissman JS","authors_abbrev":"Frost A et al.","pubmed_publication_date":"08 Jun 2012","pubmed_entrez_date":"2012-06-12","publication_year":"2012","canto_session_key":"12eed81e6d3ba9da","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"vw253@cam.ac.uk","canto_approved_date":"2017-01-18 14:43:45","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-08-30 11:14:15","canto_added_date":"2012-08-23 14:55:14","annotation_curators":[{"name":"vw253@cam.ac.uk","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.06","SPAC1142.07c","SPBC27B12.04c","SPAC167.01","SPBC1773.01","SPBC3H7.13","SPBPJ4664.06","SPAC3C7.11c","SPAC22A12.15c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2012-08-30"},{"uniquename":"PMID:20885790","title":"Critical functions of Rpa3/Ssb3 in S-phase DNA damage responses in fission yeast.","citation":"PLoS Genet 2010 Sep 23;6(9):e1001138","abstract":"Replication Protein A (RPA) is a heterotrimeric, single-stranded DNA (ssDNA)-binding complex required for DNA replication and repair, homologous recombination, DNA damage checkpoint signaling, and telomere maintenance. Whilst the larger RPA subunits, Rpa1 and Rpa2, have essential interactions with ssDNA, the molecular functions of the smallest subunit Rpa3 are unknown. Here, we investigate the Rpa3 ortholog Ssb3 in Schizosaccharomyces pombe and find that it is dispensable for cell viability, checkpoint signaling, RPA foci formation, and meiosis. However, increased spontaneous Rad11Rpa1 and Rad22Rad52 nuclear foci in ssb3Δ cells indicate genome maintenance defects. Moreover, Ssb3 is required for resistance to genotoxins that disrupt DNA replication. Genetic interaction studies indicate that Ssb3 has a close functional relationship with the Mms1-Mms22 protein complex, which is required for survival after DNA damage in S-phase, and with the mitotic functions of Mus81-Eme1 Holliday junction resolvase that is required for recovery from replication fork collapse. From these studies we propose that Ssb3 plays a critical role in mediating RPA functions that are required for repair or tolerance of DNA lesions in S-phase. Rpa3 orthologs in humans and other species may have a similar function.","doi":"10.1371/journal.pgen.1001138","authors":"Cavero S, Limbo O, Russell P","authors_abbrev":"Cavero S et al.","pubmed_publication_date":"23 Sep 2010","pubmed_entrez_date":"2010-10-02","publication_year":"2010","canto_session_key":"4dfa9e1e417a7efe","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2018-10-02 10:26:44","canto_approved_date":"2024-04-03 08:58:01","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2018-09-25 22:52:21","canto_added_date":"2012-02-24 05:47:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":75,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC216.06c","SPBC902.02c","SPAC3H8.05c","SPBC216.05","SPCC4G3.05c","SPAC644.14c","SPAC27E2.10c","SPBC660.13c","SPCC23B6.05c","SPBC3E7.08c","SPBC409.03","SPAC6B12.02c","SPBC30D10.04","SPAC3G6.06c","SPBC28F2.07","SPBC582.05c","SPBC4F6.15c","SPAC3C7.03c","SPAC30D11.10","SPCC18B5.11c","SPCC1259.13"],"gene_count":21,"ltp_gene_count":20,"approved_date":"2018-10-02"},{"uniquename":"PMID:36045206","title":"Cell Cycle Synchrony Methods for Fission Yeast, Schizosaccharomyces pombe.","citation":"Methods Mol Biol 2022;2579:169-179","abstract":"The fission yeast, Schizosaccharomyces pombe, is a genetically tractable model organism for cell cycle and molecular genetics research. We describe methods to synchronize S. pombe cultures, and the benefits and limitations of each. Drug-induced synchrony is a convenient method to arrest the cell cycle. An example of the drug hydroxyurea is shown, which arrests cells in S-phase. Environmental modulation through media composition or growth conditions may also be used to synchronize cultures, most commonly with nitrogen depletion to arrest in G1-phase. Finally, examples of temperature-sensitive conditional alleles are shown which arrest the cell cycle at key transition points. Each of these methods must be assessed relative to the desired effect and the process being studied, providing the best synchrony with the fewest off-target effects.","doi":"10.1007/978-1-0716-2736-5_13","authors":"Kianfard Z, Cheung K, Sabatinos SA","authors_abbrev":"Kianfard Z et al.","pubmed_publication_date":"2022","pubmed_entrez_date":"2022-08-31","publication_year":"2022","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2022-09-03 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC336.12c","SPAC24H6.05","SPAC1F7.05"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:30318141","title":"Structural Insights into Mdn1, an Essential AAA Protein Required for Ribosome Biogenesis.","citation":"Cell 2018 Oct 18;175(3):822-834.e18","abstract":"Mdn1 is an essential AAA (ATPase associated with various activities) protein that removes assembly factors from distinct precursors of the ribosomal 60S subunit. However, Mdn1's large size (∼5,000 amino acid [aa]) and its limited homology to other well-studied proteins have restricted our understanding of its remodeling function. Here, we present structures for S. pombe Mdn1 in the presence of AMPPNP at up to ∼4 Å or ATP plus Rbin-1, a chemical inhibitor, at ∼8 Å resolution. These data reveal that Mdn1's MIDAS domain is tethered to its ring-shaped AAA domain through an ∼20 nm long structured linker and a flexible ∼500 aa Asp/Glu-rich motif. We find that the MIDAS domain, which also binds other ribosome-assembly factors, docks onto the AAA ring in a nucleotide state-specific manner. Together, our findings reveal how conformational changes in the AAA ring can be directly transmitted to the MIDAS domain and thereby drive the targeted release of assembly factors from ribosomal 60S-subunit precursors.","doi":"10.1016/j.cell.2018.09.015","authors":"Chen Z, Suzuki H, Kobayashi Y, Wang AC, DiMaio F, Kawashima SA, Walz T, Kapoor TM","authors_abbrev":"Chen Z et al.","pubmed_publication_date":"18 Oct 2018","pubmed_entrez_date":"2018-10-16","publication_year":"2018","canto_session_key":"8937e38b7cfec64c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2018-10-23 13:17:47","canto_approved_date":"2021-09-29 10:23:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-10-21 18:17:52","canto_added_date":"2018-10-17 00:15:04","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":4,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC737.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-10-23","pdb_entries":[{"pdb_id":"6or5","gene_chains":[{"gene_uniquename":"SPCC737.08","chain":"A","position":"1-4717"}],"title":"Full-length S. pombe Mdn1 in the presence of AMPPNP (ring region)","entry_authors":"Chen Z,Suzuki H,Wang AC,DiMaio F,Walz T,Kapoor TM","entry_authors_abbrev":"Chen Z et al.","reference_uniquename":"PMID:30318141","experimental_method":"EM","resolution":"4.0"},{"pdb_id":"6or6","gene_chains":[{"gene_uniquename":"SPCC737.08","chain":"A","position":"1-4717"}],"title":"Full-length S. pombe Mdn1 in the presence of AMPPNP (tail region)","entry_authors":"Chen Z,Suzuki H,Wang AC,DiMaio F,Walz T,Kapoor TM","entry_authors_abbrev":"Chen Z et al.","reference_uniquename":"PMID:30318141","experimental_method":"EM","resolution":"5.3"},{"pdb_id":"6orb","gene_chains":[{"gene_uniquename":"SPCC737.08","chain":"A","position":"1-4717"}],"title":"Full-length S. pombe Mdn1 in the presence of ATP and Rbin-1","entry_authors":"Chen Z,Suzuki H,Wang AC,DiMaio F,Walz T,Kapoor TM","entry_authors_abbrev":"Chen Z et al.","reference_uniquename":"PMID:30318141","experimental_method":"EM","resolution":"7.7"}]},{"uniquename":"PMID:11956316","title":"The novel HECT-type ubiquitin-protein ligase Pub2p shares partially overlapping function with Pub1p in Schizosaccharomyces pombe.","citation":"J Cell Sci 2002 May 01;115(Pt 9):1847-57","abstract":"The fission yeast Schizosaccharomyces pombe has three putative ubiquitin-protein ligases of the Nedd4/Rsp5 family, named Pub1p, Pub2p and Pub3p. Pub1p has been reported to be involved in cell cycle regulation and proliferation under acidic pH conditions. Here we characterize Pub2p, which contains a conserved HECT domain and a WW domain but lacks a C2 domain. Transcription of the pub2(+) gene was constitutive and further enhanced by nitrogen starvation. A pub2-null mutation gave no remarkable phenotypes, but intensified temperature sensitivity in a pub1Delta background. Moderately overexpressed pub2(+) suppressed the temperature sensitivity of pub1Delta cells, which suggests that the function of Pub2p overlaps with that of Pub1p. Overexpression of pub2(+) by a strong nmt1 promoter in wild-type strains caused growth arrest and cell elongation, probably owing to defects in G2 progression or the G2/M transition. Unlike Pub1p, however, overexpression of Pub2p did not reduce the levels of Cdc25p. Pub2-GFP was found throughout the cell, especially at the cell surface in the polar regions. Pub2p contains a conserved cysteine residue (Cys639) in its putative catalytic HECT domain that can be thiol-ubiquitinated. Substitution of Cys639 by alanine (Pub2CA) caused a functional defect, because growth arrest and cell elongation were not induced by overexpression of Pub2CA. A chimeric Pub1 protein, in which the HECT domain was replaced by the Pub2 HECT domain, completely suppressed the temperature sensitivity of pub1Delta cells, suggesting that the HECT domain of Pub2p has the catalytic activity of a ubiquitin ligase. We conclude that Pub2p is a HECT-type ubiquitin-protein ligase that shares partially overlapping function with Pub1p.","authors":"Tamai KK, Shimoda C","authors_abbrev":"Tamai KK et al.","pubmed_publication_date":"01 May 2002","pubmed_entrez_date":"2002-04-17","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:17","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1805.15c","SPBC16E9.11c","SPAC11G7.02"],"gene_count":3,"ltp_gene_count":2},{"uniquename":"PMID:8227200","title":"The BiP protein and the endoplasmic reticulum of Schizosaccharomyces pombe: fate of the nuclear envelope during cell division.","citation":"J Cell Sci 1993 Aug;105 ( Pt 4):1115-20","abstract":"A polyclonal antibody was raised to the C-terminal region of fission yeast BiP. The use of this antibody for immunoprecipitation, western blotting and immunofluorescence has confirmed and extended the observations made previously with an epitope-tagged BiP molecule. A fraction of BiP protein is glycosylated in Schizosaccharomyces pombe cells. Pulse-chase experiments showed that this modification occurs rapidly upon synthesis and that the extent of glycosylation does not then change with time. BiP protein is induced by elevated temperatures and by treatment with tunicamycin. The antibody cross-reacts with proteins of similar molecular weight in the yeasts Kluyveromyces lactis and Schizosaccharomyces japonicus. Immunofluorescence of BiP has been used to follow the behaviour of the ER and in particular the nuclear envelope through the cell cycle.","authors":"Pidoux AL, Armstrong J","authors_abbrev":"Pidoux AL et al.","pubmed_publication_date":"Aug 1993","pubmed_entrez_date":"1993-08-01","publication_year":"1993","canto_session_key":"3aac4505bb3ec2e8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2016-09-02 18:05:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-28 23:51:22","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22A12.15c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-06-28"},{"uniquename":"PMID:17435009","title":"Mcp4, a meiotic coiled-coil protein, plays a role in F-actin positioning during Schizosaccharomyces pombe meiosis.","citation":"Eukaryot Cell 2007 Jun;6(6):971-83","abstract":"Some meiosis-specific proteins of Schizosaccharomyces pombe harbor coiled-coil motifs and play essential roles in meiotic progression. Here we describe Mcp4, a novel meiosis-specific protein whose expression is abruptly induced at the horsetail phase and which remains expressed until sporulation is finished. Fluorescence microscopic analysis revealed that Mcp4 alters its subcellular localization during meiosis in a manner that partially resembles the movement of F-actin during meiosis. Mcp4 and F-actin never colocalize; rather, they are located in a side-by-side manner. When forespore membrane formation begins at metaphase II, the Mcp4 signals assemble at the lagging face of the dividing nuclei. At this stage, they are sandwiched between F-actin and the nucleus. Mcp4, in turn, appears to sandwich F-actin with Meu14. In mcp4Delta cells at anaphase II, the F-actin, which is normally dumbbell-shaped, adopts an abnormal balloon shape. Spores of mcp4Delta cells were sensitive to NaCl, although their shape and viability were normal. Taken together, we conclude that Mcp4 plays a role in the accurate positioning of F-actin during S. pombe meiosis.","authors":"Ohtaka A, Okuzaki D, Saito TT, Nojima H","authors_abbrev":"Ohtaka A et al.","pubmed_publication_date":"Jun 2007","pubmed_entrez_date":"2007-04-17","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16E9.08"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:23921640","title":"RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74.","citation":"Nucleic Acids Res 2013 Oct;41(19):9183-96","abstract":"Transcription of tRNA-encoding genes by RNA polymerase (Pol) III requires the six-subunit general transcription factor IIIC that uses subcomplexes τA and τB to recognize two gene-internal promoter elements named A- and B-box. The Schizosaccharomyces pombe τA subcomplex comprises subunits Sfc1, Sfc4 and Sfc7. The crystal structure of the Sfc1/Sfc7 heterodimer reveals similar domains and overall domain architecture to the Pol II-specific general transcription factor TFIIF Rap30/Rap74. The N-terminal Sfc1/Sfc7 dimerization module consists of a triple β-barrel similar to the N-terminal TFIIF Rap30/Rap74 dimerization module, whereas the C-terminal Sfc1 DNA-binding domain contains a winged-helix domain most similar to the TFIIF Rap30 C-terminal winged-helix domain. Sfc1 DNA-binding domain recognizes single and double-stranded DNA by an unknown mechanism. Several features observed for A-box recognition by τA resemble the recognition of promoters by bacterial RNA polymerase, where σ factor unfolds double-stranded DNA and stabilizes the non-coding DNA strand in an open conformation. Such a function has also been proposed for TFIIF, suggesting that the observed structural similarity between Sfc1/Sfc7 and TFIIF Rap30/Rap74 might also reflect similar functions.","doi":"10.1093/nar/gkt664","authors":"Taylor NM, Baudin F, von Scheven G, Müller CW","authors_abbrev":"Taylor NM et al.","pubmed_publication_date":"Oct 2013","pubmed_entrez_date":"2013-08-08","publication_year":"2013","canto_session_key":"78e568bb1e219f50","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2014-05-06 12:14:07","canto_approved_date":"2023-02-23 19:50:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-05-06 10:24:54","canto_added_date":"2013-08-22 05:19:07","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6F12.11c","SPAC1250.07"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2014-05-06","pdb_entries":[{"pdb_id":"4bji","gene_chains":[{"gene_uniquename":"SPAC6F12.11c","chain":"A","position":"186-396"}],"title":"Sfc1-DBD","entry_authors":"Taylor NMI,Baudin F,von Scheven G,Muller CW","entry_authors_abbrev":"Taylor NMI et al.","reference_uniquename":"PMID:23921640","experimental_method":"X-ray","resolution":"1.45"},{"pdb_id":"4bjj","gene_chains":[{"gene_uniquename":"SPAC1250.07","chain":"B","position":"2-101"},{"gene_uniquename":"SPAC6F12.11c","chain":"A","position":"1-110"}],"title":"Sfc1-Sfc7 dimerization module","entry_authors":"Taylor NMI,Baudin F,von Scheven G,Muller CW","entry_authors_abbrev":"Taylor NMI et al.","reference_uniquename":"PMID:23921640","experimental_method":"X-ray","resolution":"2.4"}]},{"uniquename":"PMID:29958883","title":"Role of nucleocytoplasmic transport in interphase microtubule organization in fission yeast.","citation":"Biochem Biophys Res Commun 2018 Sep 05;503(2):1160-1167","abstract":"The proper organization of microtubules is essential for many cellular functions. Microtubule organization and reorganization are highly regulated during the cell cycle, but the underlying mechanisms remain elusive. Here we characterized unusual interphase microtubule organization in fission yeast nuclear export mutant crm1-124. The mutant cells have an intranuclear microtubule bundle during interphase that pushes the nuclear envelope to assume a protruding morphology. We showed that the formation of this protruding microtubule bundle requires the nuclear accumulation of two microtubule-associated proteins (MAPs), Alp14/TOG and Mal3/EB1. Interestingly, the forced accumulation of Alp14 in the nucleus of wild type cells is sufficient to form the intranuclear microtubule bundle. Furthermore, the frequency of the intranuclear microtubule formation by Alp14 accumulated in the nucleus is prominently increased by a reduction in the nucleation activity of interphase cytoplasmic microtubules. We propose that properly regulated nucleocytoplasmic transport and maintained activity of cytoplasmic microtubule nucleation during interphase are important for the proper organization of interphase cytoplasmic microtubules.","doi":"10.1016/j.bbrc.2018.06.135","authors":"Kume K, Kaneko S, Nishikawa K, Mizunuma M, Hirata D","authors_abbrev":"Kume K et al.","pubmed_publication_date":"05 Sep 2018","pubmed_entrez_date":"2018-07-01","publication_year":"2018","canto_session_key":"897c5fbea8a285d1","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-07-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP19A11.04c","SPBC902.06","SPCC895.07","SPCC417.07c","SPBC1604.08c","SPAC18G6.15","SPAC1805.17"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:26519302","title":"Real-Time Visualization and Quantification of Contractile Ring Proteins in Single Living Cells.","citation":"Methods Mol Biol 2016;1369:9-23","abstract":"Single-cell microscopy provides a powerful tool to visualize cellular and subcellular processes in wild-type and mutant cells by observing fluorescently tagged proteins. Here, we describe three simple methods to visualize fission yeast cells: gelatin slides, coverslip-bottom dishes, and tetrad fluorescence microscopy. These imaging methods and data analysis using free software make it possible to quantify protein localization, dynamics, and concentration with high spatial and temporal resolution. In fission yeast, the actomyosin contractile ring is essential for cytokinesis. We use the visualization and quantification of contractile ring proteins as an example to demonstrate how to use these methods.","doi":"10.1007/978-1-4939-3145-3_2","authors":"Davidson R, Liu Y, Gerien KS, Wu JQ","authors_abbrev":"Davidson R et al.","pubmed_publication_date":"2016","pubmed_entrez_date":"2015-11-01","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-11-02 01:19:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU014451","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12676091","title":"S. pombe aurora kinase/survivin is required for chromosome condensation and the spindle checkpoint attachment response.","citation":"Curr Biol 2003 Apr 01;13(7):590-7","abstract":"The spindle checkpoint inhibits anaphase until all chromosomes have established bipolar attachment. Two kinetochore states trigger this checkpoint. The absence of microtubules activates the attachment response, while the inability of attached microtubules to generate tension triggers the tension/orientation response. The single aurora kinase of budding yeast, Ipl1, is required for the tension/orientation, but not attachment, response. In contrast, we find that the single aurora kinase of fission yeast, Ark1, is required for the attachment response. Having established that the initiator codon assigned to ark1(+) was incorrect and that Ark1-associated kinase activity depended upon survivin function and phosphorylation, we found that the loss of Ark1 from kinetochores by either depletion or use of a survivin mutant overides the checkpoint response to microtubule depolymerization. Ark1/survivin function was not required for the association of Bub1 or Mad3 with the kinetochores. However, it was required for two aspects of Mad2 function that accompany checkpoint activation: full-scale association with kinetochores and formation of a complex with Mad3. Neither the phosphorylation of histone H3 that accompanies chromosome condensation nor condensin recruitment to mitotic chromatin were seen when Ark1 function was compromised. Cytokinesis was not affected by Ark1 depletion or expression of the \"kinase dead\" ark1.K118R mutant.","authors":"Petersen J, Hagan IM","authors_abbrev":"Petersen J et al.","pubmed_publication_date":"01 Apr 2003","pubmed_entrez_date":"2003-04-05","publication_year":"2003","canto_session_key":"467e6f07be778615","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC320.13c","SPCC1795.01c","SPBC20F10.06"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:23066509","title":"New twists in the unfolded protein response.","citation":"Elife 2012 Oct 15;1:e00243","abstract":"The response of S. pombe, also known as fission yeast, to misfolded proteins involves mechanisms that have not been observed in other species.","doi":"10.7554/eLife.00243","authors":"Cross BC, Ron D","authors_abbrev":"Cross BC et al.","pubmed_publication_date":"15 Oct 2012","pubmed_entrez_date":"2012-10-16","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC167.01"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2911265","title":"Existence and expression of photoreactivation repair genes in various yeast species.","citation":"Mutat Res 1989 Jan;217(1):3-10","abstract":"Photoreactivation repair (Phr) activities in cell extracts of 13 different yeast species were measured by the Haemophilus influenzae transformation assay. Five species including Schizosaccharomyces pombe showed no or low enzymatic activity. In contrast to the other species, chromosomal DNAs of these 5 species did not show detectable hybridization using a DNA fragment of the photolyase PHR1 gene of Saccharomyces cervisiae as a probe even at a low stringency condition. When the PHR1 gene was attached to the 5'-flanking sequence of the iso-1-cytochrome c (CYC-1) gene of S. cerevisiae and introduced into S. pombe cells, the transformants acquired a high Phr activity, indicating that the PHR1 gene alone can provide a Phr-negative species with this repair activity and the light-absorbing cofactor(s) must be present in S. pombe. Our results also demonstrated that the 5'-flanking sequence of the S. cerevisiae CYC-1 gene works in S. pombe as a regulatory element.","authors":"Yasui A, Eker AP, Koken M","authors_abbrev":"Yasui A et al.","pubmed_publication_date":"Jan 1989","pubmed_entrez_date":"1989-01-01","publication_year":"1989","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35080989","title":"Homology-directed repair involves multiple strand invasion cycles in fission yeast.","citation":"Mol Biol Cell 2022 Apr 01;33(4):ar30","abstract":"Homology-directed repair of DNA double-strand breaks (DSBs) represents a highly faithful pathway. Non-crossover repair dominates in mitotically growing cells, likely through a preference for synthesis-dependent strand annealing (SDSA). How homology-directed repair mechanism choice is orchestrated in time and space is not well understood. Here, we develop a microscopy-based assay in living fission yeast to determine the dynamics and kinetics of an engineered, site-specific interhomologue repair event. We observe highly efficient homology search and homology-directed repair in this system. Surprisingly, the initial distance between the DSB and the donor sequence does not correlate with the duration of repair. Instead, we observe that repair often involves multiple site-specific and Rad51-dependent colocalization events between the DSB and donor sequence. Upon loss of the RecQ helicase Rqh1 (BLM in humans) we observe rapid repair possibly involving a single strand invasion event, suggesting that multiple strand invasion cycles antagonized by Rqh1 could reflect ongoing SDSA. However, failure to colocalize with the donor sequence and execute repair is also more likely in  rqh1Δ  cells, possibly reflecting erroneous strand invasion. This work has implications for the molecular etiology of Bloom syndrome, caused by mutations in BLM and characterized by aberrant sister chromatid crossovers and inefficient repair.","doi":"10.1091/mbc.E20-07-0433","authors":"Vines AJ, Cox K, Leland BA, King MC","authors_abbrev":"Vines AJ et al.","pubmed_publication_date":"01 Apr 2022","pubmed_entrez_date":"2022-01-26","publication_year":"2022","canto_session_key":"8a9d05000ee132ba","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-01-28 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17425674","title":"Why do some yeast species require niacin for growth? Different modes of NAD synthesis.","citation":"FEMS Yeast Res 2007 Aug;7(5):657-64","abstract":"NAD holds a key position in metabolism and cellular regulatory events as a major redox carrier and a signalling molecule. NAD biosynthesis pathways have been reconstructed and compared in seven yeast species with completely sequenced genomes, including Saccharomyces cerevisiae, Kluyveromyces lactis, Candida glabrata, Debaryomyces hansenii, Candida albicans, Yarrowia lipolytica and Schizosaccharomyces pombe. Both amino acid and nucleotide sequence similarity analysis in silico indicated that de novo NAD biosynthesis might not exist in K. lactis, C. glabrata and Schiz. pombe, while other species have the kynurenine pathway. It also showed that the NAD salvage pathway via nicotinic acid and nicotinic acid mononucleotide is conserved in all of these yeasts. Deletion of KlNPT1 (the gene for nicotinate phosphoribosyl-transferase) is lethal, which demonstrates that this salvage pathway, utilizing exogenous nicotinic acid, is the unique route to synthesize NAD in K. lactis. The results suggested that the basis of the variation of niacin requirements in yeasts lies in their different combinations of NAD biosynthesis pathways. The de novo pathway is absent but the salvage pathway is conserved in niacin-negative yeasts, while both pathways coexist in niacin-positive yeasts.","authors":"Li YF, Bao WG","authors_abbrev":"Li YF et al.","pubmed_publication_date":"Aug 2007","pubmed_entrez_date":"2007-04-12","publication_year":"2007","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011829","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19282671","title":"How does a millimeter-sized cell find its center?","citation":"Cell Cycle 2009 Apr 15;8(8):1115-21","abstract":"Microtubules play a central role in centering the nucleus or mitotic spindle in eukaryotic cells. However, despite common use of microtubules for centering, physical mechanisms can vary greatly, and depend on cell size and cell type. In the small fission yeast cells, the nucleus can be centered by pushing forces that are generated when growing microtubules hit the cell boundary. This mechanism may not be possible in larger cells, because the compressive force that microtubules can sustain are limited by buckling, so maximal force decreases with microtubule length. In a well-studied intermediate sized cell, the C. elegans fertilized egg, centrosomes are centered by cortex-attached motors that pull on microtubules. This mechanism is widely assumed to be general for larger cells. However, re-evaluation of classic experiments in a very large cell, the fertilized amphibian egg, argues against such generality. In these large eggs, movement of asters away from a part of the cell boundary that they are touching cannot be mediated by cortical pulling, because the astral microtubules are too short to reach the opposite cell boundary. Additionally, Herlant and Brachet discovered a century ago that multiple asters within a single egg center relative to the cell boundary, but also relative to each other. Here, we summarize current understanding of microtubule organization during the first cell cycle in a fertilized Xenopus egg, discuss how microtubule asters move towards the center of this very large cell, and how multiple asters shape and position themselves relative to each other.","authors":"Wühr M, Dumont S, Groen AC, Needleman DJ, Mitchison TJ","authors_abbrev":"Wühr M et al.","pubmed_publication_date":"15 Apr 2009","pubmed_entrez_date":"2009-03-14","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1606618","title":"twine, a cdc25 homolog that functions in the male and female germline of Drosophila.","citation":"Cell 1992 Jun 12;69(6):977-88","abstract":"twine is the second homolog of the fission yeast gene cdc25 to be found in Drosophila. Both string and twine cDNAs can rescue a temperature-sensitive cdc25 mutation in fission yeast, but not a deletion. We detect the expression of string but not twine transcripts in the proliferating cells of newly cellularized embryos, in third instar larval brains, and in imaginal discs. Both genes are abundantly expressed in nurse cells during oogenesis, the maternal transcripts persisting throughout the syncytial stage of embryonic development. In the testis, twine transcripts are seen in the growing stage of premeiotic cysts. Analysis of a twine mutant suggests a requirement for the gene during oogenesis, during syncytial embryonic development, and for male meiosis. Meiosis does not occur in homozygous twine males, which produce cysts containing 16 rather than 64 spermatids.","authors":"Alphey L, Jimenez J, White-Cooper H, Dawson I, Nurse P, Glover DM","authors_abbrev":"Alphey L et al.","pubmed_publication_date":"12 Jun 1992","pubmed_entrez_date":"1992-06-12","publication_year":"1992","canto_session_key":"7ac96c656f5dbde9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 12:06:40","canto_session_submitted_date":"2012-03-03 12:06:15","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:9358179","title":"Both the polypyrimidine tract and the 3' splice site function prior to the first step of splicing in fission yeast.","citation":"Nucleic Acids Res 1997 Nov 15;25(22):4658-65","abstract":"While it is known that several trans -acting splicing factors are highly conserved between Schizosaccharomyces pombe and mammals, the roles of cis -acting signals have received comparatively little attention. In Saccharomyces cerevisiae, sequences downstream from the branch point are not required prior to the first transesterification reaction, whereas in mammals the polypyrimidine tract and, in some introns, the 3' AG dinucleotide are critical for initial recognition of an intron. We have investigated the contribution of these two sequence elements to splicing in S.pombe. To determine the stage at which the polypyrimidine tract functions, we analyzed the second intron of the cdc2 gene (cdc 2-Int2), in which pyrimidines span the entire interval between the branch point and 3' splice site. Our data indicate that substitution of a polypurine tract results in accumulation of linear pre-mRNA, while expanding the polypyrimidine tract enhances splicing efficiency, as in mammals. To examine the role of the AG dinucleotide in cdc 2-Int2 splicing, we mutated the 3' splice junction in both the wild-type and pyrimidine tract variant RNAs. These changes block the first transesterification reaction, as in a subset of mammalian introns. However, in contrast to the situation in mammals, we were unable to rescue the first step of splicing in a 3' splice site mutant by expanding the polypyrimidine tract. Mutating the terminal G in the third intron of the nda 3 gene (nda 3-Int3) also blocks the first transesterification reaction, suggesting that early recognition of the 3' splice site is a general property of fission yeast introns. Counter to earlier work with an artificial intron, it is not possible to restore the first step of splicing in cdc 2-Int2 and nda 3-Int3 3' splice site mutants by introducing compensatory changes in U1 snRNA. These results highlight the diversity and probable redundancy of mechanisms for identifying the 3' ends of introns.","authors":"Romfo CM, Wise JA","authors_abbrev":"Romfo CM et al.","pubmed_publication_date":"15 Nov 1997","pubmed_entrez_date":"1998-02-12","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:20","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34328525","title":"Spectrum of Protein Location in Proteomes Captures Evolutionary Relationship Between Species.","citation":"J Mol Evol 2021 Oct;89(8):544-553","abstract":"The native subcellular location (also referred to as localization or cellular compartment) of a protein is the one in which it acts most frequently; it is one aspect of protein function. Do ten eukaryotic model organisms differ in their location spectrum, i.e., the fraction of its proteome in each of seven major cellular compartments? As experimental annotations of locations remain biased and incomplete, we need prediction methods to answer this question. After systematic bias corrections, the complete but faulty prediction methods appeared to be more appropriate to compare location spectra between species than the incomplete more accurate experimental data. This work compared the location spectra for ten eukaryotes: Homo sapiens (human), Gorilla gorilla (gorilla), Pan troglodytes (chimpanzee), Mus musculus (mouse), Rattus norvegicus (rat), Drosophila melanogaster (fruit/vinegar fly), Anopheles gambiae (African malaria mosquito), Caenorhabitis elegans (nematode), Saccharomyces cerevisiae (baker's yeast), and Schizosaccharomyces pombe (fission yeast). The two largest classes were predicted to be the nucleus and the cytoplasm together accounting for 47-62% of all proteins, while 7-21% of the proteins were predicted in the plasma membrane and 4-15% to be secreted. Overall, the predicted location spectra were largely similar. However, in detail, the differences sufficed to plot trees (UPGMA) and 2D (PCA) maps relating the ten organisms using a simple Euclidean distance in seven states (location classes). The relations based on the simple predicted location spectra captured aspects of cross-species comparisons usually revealed only by much more detailed evolutionary comparisons. Most interestingly, known phylogenetic relations were reproduced better by paralog-only than by ortholog-only trees.","doi":"10.1007/s00239-021-10022-4","authors":"Marot-Lassauzaie V, Goldberg T, Armenteros JJA, Nielsen H, Rost B","authors_abbrev":"Marot-Lassauzaie V et al.","pubmed_publication_date":"Oct 2021","pubmed_entrez_date":"2021-07-30","publication_year":"2021","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2021-08-01 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2587274","title":"Sequence and structure of U5 snRNA from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1989 Nov 25;17(22):9483","abstract":"","authors":"Small K, Brennwald P, Skinner H, Schaefer K, Wise JA","authors_abbrev":"Small K et al.","pubmed_publication_date":"25 Nov 1989","pubmed_entrez_date":"1989-11-25","publication_year":"1989","canto_session_key":"832ea43d4b3fb6f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-19 15:43:57","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-19 15:43:40","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.05"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-19"},{"uniquename":"PMID:15226425","title":"Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast.","citation":"Mol Cell Biol 2004 Jul;24(14):6215-30","abstract":"Mammalian ATR and ATM checkpoint kinases modulate chromatin structures near DNA breaks by phosphorylating a serine residue in the carboxy-terminal tail SQE motif of histone H2AX. Histone H2A is similarly regulated in Saccharomyces cerevisiae. The phosphorylated forms of H2AX and H2A, known as gamma-H2AX and gamma-H2A, are thought to be important for DNA repair, although their evolutionarily conserved roles are unknown. Here, we investigate gamma-H2A in the fission yeast Schizosaccharomyces pombe. We show that formation of gamma-H2A redundantly requires the ATR/ATM-related kinases Rad3 and Tel1. Mutation of the SQE motif to AQE (H2A-AQE) in the two histone H2A genes caused sensitivity to a wide range of genotoxic agents, increased spontaneous DNA damage, and impaired checkpoint maintenance. The H2A-AQE mutations displayed a striking synergistic interaction with rad22Delta (Rad52 homolog) in ionizing radiation (IR) survival. These phenotypes correlated with defective phosphorylation of the checkpoint proteins Crb2 and Chk1 and a failure to recruit large amounts of Crb2 to damaged DNA. Surprisingly, the H2A-AQE mutations substantially suppressed the IR hypersensitivity of crb2Delta cells by a mechanism that required the RecQ-like DNA helicase Rqh1. We propose that gamma-H2A modulates checkpoint and DNA repair through large-scale recruitment of Crb2 to damaged DNA. This function correlates with evidence that gamma-H2AX regulates recruitment of several BRCA1 carboxyl terminus domain-containing proteins (NBS1, 53BP1, MDC1/NFBD1, and BRCA1) in mammals.","authors":"Nakamura TM, Du LL, Redon C, Russell P","authors_abbrev":"Nakamura TM et al.","pubmed_publication_date":"Jul 2004","pubmed_entrez_date":"2004-07-01","publication_year":"2004","canto_session_key":"d2288b20e67eb62d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-23 18:16:14","canto_approved_date":"2025-01-01 16:29:35","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-08 14:37:22","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":63,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC342.05","SPAC19G12.06c","SPCC1183.05c","SPAC13C5.07","SPCC1259.13","SPCC126.02c","SPAC694.06c","SPCC18B5.11c","SPAC2G11.12","SPBC216.05","SPCC23B6.03c","SPAC644.14c","SPAC30D11.10","SPCC622.08c"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2017-01-23"},{"uniquename":"PMID:8557037","title":"Identification of a cdk-activating kinase in fission yeast.","citation":"EMBO J 1995 Dec 15;14(24):6173-83","abstract":"We have identified a second cyclin-dependent kinase (cdk) in fission yeast, crk1, which encodes a 335 amino acid protein that is most closely related to the KIN28 gene product from Saccharomyces cerevisiae and to a cdk activating kinase (CAK) encoded by the MO15 gene from Xenopus laevis, crk1 is essential for viability and delta crk1 cells arrest with septa and condensed chromatin. We show that Crk1 associates with the Mcs2 mitotic catastrophe suppressor, a cyclin H-like molecule, and overexpression of crk1 rescues the cell-cycle arrest defect of a mcs2-75 cdc2-3w cdc25-22 triple mutant at high temperature. The Crk1-Mcs2 complex possesses CAK activity in vitro in that it phosphorylates human Cdk2 on Thr160 which results in its activation in the presence of cyclin A. In addition Crk1-Mcs2 effectively phosphorylates a peptide corresponding to the C-terminal repeat domain (CTD) of RNA polymerase II. We demonstrate that crk1 is allelic to the mcs6 mitotic catastrophe suppressor and that the X.laevis MO15 gene rescues the cell-cycle arrest of an mcs6-13 cdc2-3w cdc25-22 at high temperature. Together these data suggest that the Crk1-Mcs2 complex is a CAK that interacts genetically with Cdc2 in fission yeast.","authors":"Buck V, Russell P, Millar JB","authors_abbrev":"Buck V et al.","pubmed_publication_date":"15 Dec 1995","pubmed_entrez_date":"1995-12-15","publication_year":"1995","canto_session_key":"f7d320e81fb9bd5f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-04-25 07:40:04","canto_approved_date":"2024-01-09 11:48:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-01-21 00:02:33","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":10,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPAC24H6.05","SPBC19F8.07","SPBP16F5.02","SPBC28F2.12"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2017-04-25"},{"uniquename":"PMID:41236477","title":"Actin arginylation alters myosin engagement and F-actin patterning despite structural conservation.","citation":"J Cell Biol 2026 Jan 05;225(1)","abstract":"Actin is a conserved protein with crucial roles in cell polarity, division, and muscle contraction. Its function is regulated in part by posttranslational modifications, one of which is N-terminal arginylation. What is the structure of arginylated-β-actin (R-β-actin), and how does it regulate F-actin function? Here we report the 3.6 Å structures of ADP-R-β-actin filaments, which are nearly identical to that of non-arginylated F-actin. In vitro assays reveal that the interaction between myosin-II and actin is altered upon actin arginylation, characterized by frequent detachment of R-actin filaments from myosin-II. In vivo, replacement of the only actin gene in Schizosaccharomyces pombe with a synthetic gene encoding R-Sp-actin reduces Arp2/3-based actin patches while thickening formin-induced actin cables. Consistent with defective interactions between myosin-II and R-actin filaments, assembly and constriction of the cytokinetic actomyosin ring are perturbed in R-Sp-actin cells. Thus, despite structural similarity of arginylated and non-arginylated actin filaments, actin arginylation affects F-actin assortment into distinct subcellular structures and its interaction with myosin-II.","doi":"10.1083/jcb.202409067","authors":"Pinto CS, Bakker SE, Suchenko A, Kolodny IM, Hussain H, Hatano T, Sampath K, Chinthalapudi K, Heissler SM, Mishima M, Balasubramanian M","authors_abbrev":"Pinto CS et al.","pubmed_publication_date":"05 Jan 2026","pubmed_entrez_date":"2025-11-14","publication_year":"2026","canto_session_key":"4a386604130652e6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Clyde Savio Pinto","canto_first_approved_date":"2025-12-16 12:24:26","canto_approved_date":"2026-02-26 16:39:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2025-12-11 17:10:49","canto_added_date":"2025-11-15 00:25:04","annotation_curators":[{"name":"Clyde Savio Pinto","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":3,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPCC645.05c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2025-12-16"},{"uniquename":"PMID:34346684","title":"Identifying G-Quadruplex-DNA-Disrupting Small Molecules.","citation":"J Am Chem Soc 2021 Aug 18;143(32):12567-12577","abstract":"The quest for small molecules that strongly bind to G-quadruplex-DNA (G4), so-called G4 ligands, has invigorated the G4 research field from its very inception. Massive efforts have been invested to discover or rationally design G4 ligands, evaluate their G4-interacting properties in vitro through a series of now widely accepted and routinely implemented assays, and use them as innovative chemical biology tools to interrogate cellular networks that might involve G4s. In sharp contrast, only uncoordinated efforts aimed at developing small molecules that destabilize G4s have been invested to date, even though it is now recognized that such molecular tools would have tremendous application in neurobiology as many genetic and age-related diseases are caused by an overrepresentation of G4s. Herein, we report on our efforts to develop in vitro assays to reliably identify molecules able to destabilize G4s. This workflow comprises the newly designed G4-unfold assay, adapted from the G4-helicase assay implemented with Pif1, as well as a series of biophysical and biochemical techniques classically used to study G4/ligand interactions (CD, UV-vis, PAGE, and FRET-melting), and a qPCR stop assay, adapted from a  Taq -based protocol recently used to identify G4s in the genomic DNA of  Schizosaccharomyces pombe . This unique, multipronged approach leads to the characterization of a phenylpyrrolocytosine (PhpC)-based G-clamp analog as a prototype of G4-disrupting small molecule whose properties are validated through many different and complementary in vitro evaluations.","doi":"10.1021/jacs.1c04426","authors":"Mitteaux J, Lejault P, Wojciechowski F, Joubert A, Boudon J, Desbois N, Gros CP, Hudson RHE, Boulé JB, Granzhan A, Monchaud D","authors_abbrev":"Mitteaux J et al.","pubmed_publication_date":"18 Aug 2021","pubmed_entrez_date":"2021-08-04","publication_year":"2021","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2021-08-06 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18368917","title":"Mcml0 and DNA replication in fission yeast.","citation":"SEB Exp Biol Ser 2008;59:45-69","abstract":"","authors":"Moore K, Aves SJ","authors_abbrev":"Moore K et al.","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-03-29","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6077525","title":"Concerning the mechanism of ultraviolet mutagenesis. A micromanipulatory pedigree analysis in Schizosaccharomyces pombe.","citation":"Genetics 1967 Sep;57(1):169-78","abstract":"","authors":"Haefner K","authors_abbrev":"Haefner K","pubmed_publication_date":"Sep 1967","pubmed_entrez_date":"1967-09-01","publication_year":"1967","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012395","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25356590","title":"Multifaceted genome control by Set1 Dependent and Independent of H3K4 methylation and the Set1C/COMPASS complex.","citation":"PLoS Genet 2014 Oct;10(10):e1004740","abstract":"Histone modifiers are critical regulators of chromatin-based processes in eukaryotes. The histone methyltransferase Set1, a component of the Set1C/COMPASS complex, catalyzes the methylation at lysine 4 of histone H3 (H3K4me), a hallmark of euchromatin. Here, we show that the fission yeast Schizosaccharomyces pombe Set1 utilizes distinct domain modules to regulate disparate classes of repetitive elements associated with euchromatin and heterochromatin via H3K4me-dependent and -independent pathways. Set1 employs its RNA-binding RRM2 and catalytic SET domains to repress Tf2 retrotransposons and pericentromeric repeats while relying on its H3K4me function to maintain transcriptional repression at the silent mating type (mat) locus and subtelomeric regions. These repressive functions of Set1 correlate with the requirement of Set1C components to maintain repression at the mat locus and subtelomeres while dispensing Set1C in repressing Tf2s and pericentromeric repeats. We show that the contributions of several Set1C subunits to the states of H3K4me diverge considerably from those of Saccharomyces cerevisiae orthologs. Moreover, unlike S. cerevisiae, the regulation of Set1 protein level is not coupled to the status of H3K4me or histone H2B ubiquitination by the HULC complex. Intriguingly, we uncover a genome organization role for Set1C and H3K4me in mediating the clustering of Tf2s into Tf bodies by antagonizing the acetyltransferase Mst1-mediated H3K4 acetylation. Our study provides unexpected insights into the regulatory intricacies of a highly conserved chromatin-modifying complex with diverse roles in genome control.","doi":"10.1371/journal.pgen.1004740","authors":"Mikheyeva IV, Grady PJ, Tamburini FB, Lorenz DR, Cam HP","authors_abbrev":"Mikheyeva IV et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-10-31","publication_year":"2014","canto_session_key":"12c405f9c577461c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-07-05 09:46:53","canto_approved_date":"2025-09-03 17:20:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-28 17:35:38","canto_added_date":"2014-11-01 01:15:25","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":111,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1834.04","SPAC22F8.12c","SPBC8D2.04","SPCC18.11c","SPCC306.04c","SPAC23H3.05c","SPCC594.05c","SPNCRNA.07","SPCC1919.15","SPBC32H8.12c","SPBC354.03","SPAC637.12c","SPBC13G1.08c","SPAC17G8.09","SPBC1105.11c","SPBC18H10.06c","SPCC622.09","SPAC18B11.07c","SPCC970.10c"],"gene_count":19,"ltp_gene_count":17,"approved_date":"2024-07-05"},{"uniquename":"PMID:15004206","title":"Proteomic study for the cellular responses to Cd2+ in Schizosaccharomyces pombe through amino acid-coded mass tagging and liquid chromatography tandem mass spectrometry.","citation":"Mol Cell Proteomics 2004 Jun;3(6):596-607","abstract":"Cadmium (Cd(2+)) is one of well-known toxic heavy metal ions. To gain a global understanding how Cd(2+) affects cells at the molecular level, we systematically studied the cellular response of the fission yeast Schizosaccharomyces pombe to Cd(2+) using our integrated proteomic strategy of amino acid-coded mass tagging (AACT) and liquid chromatography-tandem mass spectrometry. Our proteome-wide investigation unequivocally identified 1133 S. pombe proteins. Of which, the AACT-based quantitative analysis revealed 106 up-regulated and 55 down-regulated proteins on the Cd(2+) exposure. The most prevalent functional class in the up-regulated proteins, approximately 28% of our profile, was the proteins involved in protein biosynthesis, showing a time-dependent biphasic expression pattern characteristic with rapid initial induction and later repression. Most significantly, 27 proteins functionally classified as cell rescue and defense were up-regulated for oxygen and radical detoxification, heat shock response, and other stress response. Furthermore, the large precursor sequence coverage of our AACT approach allowed us to unequivocally identify and quantitate different isozymes for glutathione S-transferase, which have close similarity in their amino acid sequence. Our quantitative dataset also showed that 80% of the up-regulated proteins found in the S. pombe response were different from those in the Saccharomyces cerevisiae response. The function of some of the key identifications was validated through biochemical assays. It is very interesting that the induction of cysteine synthase expression was not observed in our study, although it has been proven as a critical enzyme to supply free cysteines for the enhancing synthesis of Cd(2+)-sequestering molecules such as glutathione and phytochelatins in plants and some yeasts. Our quantitative proteomic result instead suggested that, as an alternative mechanism for the detoxification of Cd(2+), S. pombe produced significantly higher level of inorganic sulfide to immobilize cellular Cd(2+) as a form of CdS nanocrystallites capped with glutathione and/or phytochelatins.","authors":"Bae W, Chen X","authors_abbrev":"Bae W et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-03-09","publication_year":"2004","canto_session_key":"f048a6e4660e1695","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-22 15:50:56","canto_session_submitted_date":"2012-02-27 11:08:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-02-27"},{"uniquename":"PMID:22641371","title":"PABPN1 shuts down alternative poly(A) sites.","citation":"Cell Res 2012 Oct;22(10):1419-21","abstract":"Although overlooked for many years, alternative cleavage and polyadenylation (APA) is now emerging as a major mechanism of gene regulation. A recent study identifies poly(A)-binding protein nuclear 1 (PABPN1), a general factor of polyadenylation, as a suppressor of alternative poly(A) sites.","doi":"10.1038/cr.2012.86","authors":"Simonelig M","authors_abbrev":"Simonelig M","pubmed_publication_date":"Oct 2012","pubmed_entrez_date":"2012-05-30","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8088540","title":"Thiamine-repressible genes in Schizosaccharomyces pombe are regulated by a Cys6 zinc-finger motif-containing protein.","citation":"Gene 1994 Sep 15;147(1):141-4","abstract":"Our previous genetic data indicate that the product of the Schizosaccharomyces pombe thi1 gene acts as an activator of several thiamine-repressible genes which are involved in the control of thiamine metabolism [Schweingruber et al., Genetics 130 (1992) 445-449; Zurlinden and Schweingruber, Gene 117 (1992) 141-143]. In this communication, we report the cloning and sequencing of thi1 and show that it carries an open reading frame which translates into a 775-amino-acid protein with the characteristics of a Cys6 zinc-finger-motif-containing transcription factor, as typified by Saccharomyces cerevisae GAL4. We, therefore, suggest that the thi1-encoded protein binds to upstream activator sequences of thiamine-repressible genes.","authors":"Fankhauser H, Schweingruber ME","authors_abbrev":"Fankhauser H et al.","pubmed_publication_date":"15 Sep 1994","pubmed_entrez_date":"1994-09-15","publication_year":"1994","canto_session_key":"97c5db6384b6d757","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-31 13:11:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 13:10:59","canto_added_date":"2012-02-24 05:54:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1486.10"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-07-31"},{"uniquename":"PMID:21749953","title":"Cell polarity: which way to grow in an electric field?","citation":"Curr Biol 2010 Apr 27;20(8):R355-6","abstract":"Cell polarity can be influenced by an electric field, but the mechanisms behind this response are poorly understood. A new paper shows that fission yeast cells change their direction of growth in an external electric field and suggests mechanisms based on the cortical pH gradient and on electrophoresis of membrane proteins.","doi":"10.1016/j.cub.2010.03.022","authors":"Kalinina IM, Krstić V, Tolić-Nørrelykke IM","authors_abbrev":"Kalinina IM et al.","pubmed_publication_date":"27 Apr 2010","pubmed_entrez_date":"2011-07-14","publication_year":"2010","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU011864","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27664031","title":"C-terminal region of Mad2 plays an important role during mitotic spindle checkpoint in fission yeast Schizosaccharomyces pombe.","citation":"Mol Biol Rep 2017 Feb;44(1):89-96","abstract":"The mitotic arrest deficiency 2 (Mad2) protein is an essential component of the spindle assembly checkpoint that interacts with Cdc20/Slp1 and inhibit its ability to activate anaphase promoting complex/cyclosome (APC/C). In bladder cancer cell line the C-terminal residue of the mad2 gene has been found to be deleted. In this study we tried to understand the role of the C-terminal region of mad2 on the spindle checkpoint function. To envisage the role of C-terminal region of Mad2, we truncated 25 residues of Mad2 C-terminal region in fission yeast S.pombe and characterized its effect on spindle assembly checkpoint function. The cells containing C-terminal truncation of Mad2 exhibit sensitivity towards microtubule destabilizing agent suggesting perturbation of spindle assembly checkpoint. Further, the C-terminal truncation of Mad2 exhibit reduced viability in the nda3-KM311 mutant background at non-permissive temperature. Truncation in mad2 gene also affects its foci forming ability at unattached kinetochore suggesting that the mad2-∆CT mutant is unable to maintain spindle checkpoint activation. However, in response to the defective microtubule, only brief delay of mitotic progression was observed in Mad2 C-terminal truncation mutant. In addition we have shown that the deletion of two β strands of Mad2 protein abolishes its ability to interact with APC activator protein Slp1/Cdc20. We purpose that the truncation of two β strands (β7 and β8) of Mad2 destabilize the safety belt and affect the Cdc20-Mad2 interaction leading to defects in the spindle checkpoint activation.","doi":"10.1007/s11033-016-4083-y","authors":"Singh GK, Karade SS, Ranjan R, Ahamad N, Ahmed S","authors_abbrev":"Singh GK et al.","pubmed_publication_date":"Feb 2017","pubmed_entrez_date":"2016-09-25","publication_year":"2017","canto_session_key":"55568a998c1ac78b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-09-26 00:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.08c","SPBC20F10.06","SPBC26H8.07c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:26575035","title":"Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe.","citation":"PLoS One 2015;10(11):e0143037","abstract":"Calcium/calmodulin-dependent protein kinase kinase (CaMKK) is required for diverse cellular functions. Mammalian CaMKK activates CaMKs and also the evolutionarily-conserved AMP-activated protein kinase (AMPK). The fission yeast Schizosaccharomyces pombe CaMKK, Ssp1, is required for tolerance to limited glucose through the AMPK, Ssp2, and for the integration of cell growth and division through the SAD kinase Cdr2.\nHere we report that Ssp1 controls the G2/M transition by regulating the activity of the CaMK Srk1. We show that inhibition of Cdc25 by Srk1 is regulated by Ssp1; and also that restoring growth polarity and actin localization of ssp1-deleted cells by removing the actin-monomer-binding protein, twinfilin, is sufficient to suppress the ssp1 phenotype.\nThese findings demonstrate that entry into mitosis is mediated by a network of proteins, including the Ssp1 and Srk1 kinases. Ssp1 connects the network of components that ensures proper polarity and cell size with the network of proteins that regulates Cdk1-cyclin B activity, in which Srk1 plays an inhibitory role.","doi":"10.1371/journal.pone.0143037","authors":"Gómez-Hierro A, Lambea E, Giménez-Zaragoza D, López-Avilés S, Yance-Chávez T, Montserrat M, Pujol MJ, Bachs O, Aligue R","authors_abbrev":"Gómez-Hierro A et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-11-18","publication_year":"2015","canto_session_key":"3352c7c843c04aca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-09-13 17:01:21","canto_approved_date":"2019-06-14 12:20:29","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-09-13 17:01:15","canto_added_date":"2015-11-19 01:19:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23A1.06c","SPAC57A10.02","SPCC126.06","SPCC297.03","SPAC24H6.05","SPCC18B5.03","SPCC1322.08"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2017-09-13"},{"uniquename":"PMID:37949217","title":"Phosphate uptake restriction, phosphate export, and polyphosphate synthesis contribute synergistically to cellular proliferation and survival.","citation":"J Biol Chem 2023 Nov 08;299(12):105454","abstract":"Phosphate (Pi) is a macronutrient, and Pi homeostasis is essential for life. Pi homeostasis has been intensively studied; however, many questions remain, even at the cellular level. Using Schizosaccharomyces pombe, we sought to better understand cellular Pi homeostasis and showed that three Pi regulators with SPX domains, Xpr1/Spx2, Pqr1, and the VTC complex synergistically contribute to Pi homeostasis to support cell proliferation and survival. SPX domains bind to inositol pyrophosphate and modulate activities of Pi-related proteins. Xpr1 is a plasma membrane protein and its Pi-exporting activity has been demonstrated in metazoan orthologs, but not in fungi. We first found that S. pombe Xpr1 is a Pi exporter, activity of which is regulated and accelerated in the mutants of Pqr1 and the VTC complex. Pqr1 is the ubiquitin ligase downregulating the Pi importers, Pho84 and Pho842. The VTC complex synthesizes polyphosphate in vacuoles. Triple deletion of Xpr1, Pqr1, and Vtc4, the catalytic core of the VTC complex, was nearly lethal in normal medium but survivable at lower [Pi]. All double-deletion mutants of the three genes were viable at normal Pi, but Δpqr1Δxpr1 showed severe viability loss at high [Pi], accompanied by hyper-elevation of cellular total Pi and free Pi. This study suggests that the three cellular processes, restriction of Pi uptake, Pi export, and polyP synthesis, contribute synergistically to cell proliferation through maintenance of Pi homeostasis, leading to the hypothesis that cooperation between Pqr1, Xpr1, and the VTC complex protects the cytoplasm and/or the nucleus from lethal elevation of free Pi.","doi":"10.1016/j.jbc.2023.105454","authors":"Takado M, Komamura T, Nishimura T, Ohkubo I, Ohuchi K, Matsumoto T, Takeda K","authors_abbrev":"Takado M et al.","pubmed_publication_date":"08 Nov 2023","pubmed_entrez_date":"2023-11-10","publication_year":"2023","canto_session_key":"2b2266764f759556","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Kojiro Takeda","canto_first_approved_date":"2024-05-23 10:24:11","canto_approved_date":"2024-10-01 06:44:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-02 11:02:04","canto_added_date":"2023-11-12 00:25:05","annotation_curators":[{"name":"Kojiro Takeda","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23D3.12","SPAC6B12.07c","SPCC1827.07c","SPCC1322.14c","SPBC8E4.01c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2024-05-23"},{"uniquename":"PMID:22624651","title":"A systematic screen reveals new elements acting at the G2/M cell cycle control.","citation":"Genome Biol 2012 May 24;13(5):R36","abstract":"The major cell cycle control acting at the G2 to mitosis transition is triggered in all eukaryotes by cyclin-dependent kinases (CDKs). In the fission yeast Schizosaccharomyces pombe the activation of the G2/M CDK is regulated primarily by dephosphorylation of the conserved residue Tyr15 in response to the stress-nutritional response and cell geometry sensing pathways. To obtain a more complete view of the G2/M control we have screened systematically for gene deletions that advance cells prematurely into mitosis.\nA screen of 82% of fission yeast non-essential genes, comprising approximately 3,000 gene deletion mutants, identified 18 genes that act negatively at mitotic entry, 7 of which have not been previously described as cell cycle regulators. Eleven of the 18 genes function through the stress response and cell geometry sensing pathways, both of which act through CDK Tyr15 phosphorylation, and 4 of the remaining genes regulate the G2/M transition by inputs from hitherto unknown pathways. Three genes act independently of CDK Tyr15 phosphorylation and define additional uncharacterized molecular control mechanisms.\nDespite extensive investigation of the G2/M control, our work has revealed new components of characterized pathways that regulate CDK Tyr15 phosphorylation and new components of novel mechanisms controlling mitotic entry.","doi":"10.1186/gb-2012-13-5-r36","authors":"Navarro FJ, Nurse P","authors_abbrev":"Navarro FJ et al.","pubmed_publication_date":"24 May 2012","pubmed_entrez_date":"2012-05-26","publication_year":"2012","canto_session_key":"2614826033a82ee6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Francisco Navarro","canto_first_approved_date":"2015-05-19 13:05:32","canto_approved_date":"2023-06-21 11:24:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-26 11:03:48","canto_added_date":"2012-05-29 06:53:57","annotation_curators":[{"name":"Francisco Navarro","community_curator":true,"annotation_count":31,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC26F1.10c","SPBC30B4.04c","SPBC19F8.02","SPAC31A2.13c","SPBC106.10","SPBC1718.07c","SPAC1782.09c","SPAC2F7.03c","SPCC126.04c","SPAC2F7.08c","SPAC17G6.04c","SPAC27E2.03c","SPAC24B11.06c","SPBC3E7.15c","SPAC1782.05","SPAC227.01c","SPAC23H3.13c","SPCC1620.14c","SPBC23G7.04c","SPCC1753.02c","SPBC32H8.07","SPBC16E9.12c","SPBC16H5.07c","SPCC1919.05","SPCC18B5.03","SPAC644.06c"],"gene_count":26,"ltp_gene_count":21,"approved_date":"2015-05-19"},{"uniquename":"PMID:15850449","title":"The alpha-glucanase Agn1p is required for cell separation in Schizosaccharomyces pombe.","citation":"Biol Cell 2005 Jul;97(7):569-76","abstract":"In animal cells, cytokinesis occurs by constriction of an actomyosin ring. In fission yeast, ring constriction is followed by deposition of a multilayered division septum that must be cleaved to release the two daughter cells. Although many studies have focused on the actomyosin ring and septum assembly, little is known about the later steps involving the cleavage of the cell wall.\nWe identified a novel gene in Schizosaccharomyces pombe, namely the agn1(+) gene that has homology to fungal 1,3-alpha-glucanases (mutanases). Disruption of the agn1(+) gene is not lethal to the cells, but does interfere with their separation, whereas overexpression of Agn1p is toxic and causes cell lysis. Agn1p levels reach a peak during septation and the protein localizes to the septum region before cell separation. Moreover, agn1(+) is responsible for the 1,3-alpha-glucanase activity, which shows a maximum at the end of septation.\nOur results clearly suggest the existence of a relationship between agn1(+), 1,3-alpha-glucanase activity and the completion of septation in S. pombe. Agn1p could be involved in the cleavage of the cylinder of the old wall that surrounds the primary septum, a region rich in alpha-glucans.","authors":"García I, Jiménez D, Martín V, Durán A, Sánchez Y","authors_abbrev":"García I et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-04-27","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012641","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26883383","title":"Determinants of RNA metabolism in the Schizosaccharomyces pombe genome.","citation":"Mol Syst Biol 2016 Feb 16;12(2):857","abstract":"To decrypt the regulatory code of the genome, sequence elements must be defined that determine the kinetics of RNA metabolism and thus gene expression. Here, we attempt such decryption in an eukaryotic model organism, the fission yeast S. pombe. We first derive an improved genome annotation that redefines borders of 36% of expressed mRNAs and adds 487 non-coding RNAs (ncRNAs). We then combine RNA labeling in vivo with mathematical modeling to obtain rates of RNA synthesis and degradation for 5,484 expressed RNAs and splicing rates for 4,958 introns. We identify functional sequence elements in DNA and RNA that control RNA metabolic rates and quantify the contributions of individual nucleotides to RNA synthesis, splicing, and degradation. Our approach reveals distinct kinetics of mRNA and ncRNA metabolism, separates antisense regulation by transcription interference from RNA interference, and provides a general tool for studying the regulatory code of genomes.","doi":"10.15252/msb.20156526","authors":"Eser P, Wachutka L, Maier KC, Demel C, Boroni M, Iyer S, Cramer P, Gagneur J","authors_abbrev":"Eser P et al.","pubmed_publication_date":"16 Feb 2016","pubmed_entrez_date":"2016-02-18","publication_year":"2016","canto_session_key":"971e28a7669ea228","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-01-05 12:29:02","canto_approved_date":"2021-01-05 12:29:02","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2021-01-05 12:28:55","canto_added_date":"2016-02-19 01:15:23","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2021-01-05"},{"uniquename":"PMID:38287927","title":"Fission yeast spindle dynamics and chromosome segregation fidelity show distinct thermosensitivity.","citation":"MicroPubl Biol 2024;2024","abstract":"Cellular processes rely on proteins with temperature-dependent stability and activity. While thermosensitivity in biological networks is well-explored, the effect of temperature on complex mechanochemical assemblies, like the spindle, is rarely studied. We examined fission yeast spindle dynamics and chromosome segregation from 15⁰C to 40⁰C. Our findings reveal that these parameters follow U-shaped temperature-dependent curves but reach their minima at different temperatures. Specifically, spindle dynamics peak around 35⁰C, whereas chromosome segregation defects are minimized at 25⁰C. This suggests a scenario in which mitotic errors are tolerated to expedite rapid cell cycle progression.","doi":"10.17912/micropub.biology.001048","authors":"Chaba Z, Jain I, Tran PT","authors_abbrev":"Chaba Z et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-01-30","publication_year":"2024","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2024-01-31 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40317199","title":"Diploidy confers genomic instability in Schizosaccharomyces pombe.","citation":"Genetics 2025 May 03;","abstract":"Whole genome duplication, or polyploidy, has been implicated in driving genome instability and tumorigenesis. Recent studies suggest that polyploidy in tumors promotes cancer genome evolution, progression, and chemoresistance resulting in worse prognosis of survival. The mechanisms by which whole genome duplications confer genome instability are not yet fully understood. In this study, we use Schizosaccharomyces pombe (fission yeast) diploids to investigate how whole genome duplication affects genome maintenance and response to stress. We find that S. pombe diploids are sensitive to replication stress and DNA damage, exhibit high levels of loss of heterozygosity, and become dependent on a group of ploidy-specific lethal genes for viability. These findings are observed in other eukaryotic models suggesting conserved consequences of polyploidy. We further investigate ploidy-specific lethal genes by depleting them using an auxin-inducible degron system to elucidate the mechanisms of genome maintenance in diploids. Overall, this work provides new insights on how whole genome duplications lead to genome instability.","doi":"10.1093/genetics/iyaf078","authors":"Park JM, Pinski DF, Forsburg SL","authors_abbrev":"Park JM et al.","pubmed_publication_date":"03 May 2025","pubmed_entrez_date":"2025-05-03","publication_year":"2025","canto_session_key":"6d2a1c0e01aec2fb","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-05-04 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8848833","title":"The molecular control mechanisms of meiosis in fission yeast.","citation":"Trends Biochem Sci 1996 Jan;21(1):18-22","abstract":"Recent experiments have shown that the inactivation of a protein kinase, pat1, and the activation of an RNA-binding protein, mei2, commit fission yeast cells to enter meiosis. Both the cyclic AMP cascade and the mitogen-activated protein kinase cascade seem to be involved in this activation/inactivation. An RNA molecule that cooperates with mei2 to play a critical role in the promotion of meiosis I has also been identified.","authors":"Yamamoto M","authors_abbrev":"Yamamoto M","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17471929","title":"[Chromosome dynamics during meiosis].","citation":"Tanpakushitsu Kakusan Koso 2006 Nov;51(14 Suppl):2159-64","abstract":"","authors":"Asakawa H, Hiraoka Y","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"Nov 2006","pubmed_entrez_date":"2007-05-03","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19464963","title":"DNA damage checkpoint inactivation: adaptation and recovery.","citation":"DNA Repair (Amst) 2009 Sep 02;8(9):1101-9","abstract":"The DNA damage checkpoint is a stress response pathway detecting pathological structures of nuclear DNA and inducing appropriate responses. These responses include cell cycle arrests, histone modifications, changes in the transcription programme and post-translational modifications of proteins involved in DNA repair. Inactivation of the DNA damage checkpoint responses can occur under two circumstances: either DNA damage has disappeared and the whole pathway is inactivated in a process termed recovery, or DNA damage persists but all or part of the pathway is nevertheless inactivated, which is called adaptation. We present here a review of these inactivating processes of the DNA damage checkpoint primarily in the budding yeast Saccharomyces cerevisiae but also with reference to studies in Schizosaccharomyces pombe and in animal cells.","doi":"10.1016/j.dnarep.2009.04.008","authors":"Clémenson C, Marsolier-Kergoat MC","authors_abbrev":"Clémenson C et al.","pubmed_publication_date":"02 Sep 2009","pubmed_entrez_date":"2009-05-26","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33730068","title":"High-throughput transcriptome sequencing and comparative analysis of Escherichia coli and Schizosaccharomyces pombe in respiratory and fermentative growth.","citation":"PLoS One 2021;16(3):e0248513","abstract":"In spite of increased complexity in eukaryotes compared to prokaryotes, several basic metabolic and regulatory processes are conserved. Here we explored analogies in the eubacteria Escherichia coli and the unicellular fission yeast Schizosaccharomyces pombe transcriptomes under two carbon sources: 2% glucose; or a mix of 2% glycerol and 0.2% sodium acetate using the same growth media and growth phase. Overall, twelve RNA-seq libraries were constructed. A total of 593 and 860 genes were detected as differentially expressed for E. coli and S. pombe, respectively, with a log2 of the Fold Change ≥ 1 and False Discovery Rate ≤ 0.05. In aerobic glycolysis, most of the expressed genes were associated with cell proliferation in both organisms, including amino acid metabolism and glycolysis. In contrast in glycerol/acetate condition, genes related to flagellar assembly and membrane proteins were differentially expressed such as the general transcription factors fliA, flhD, flhC, and flagellum assembly genes were detected in E. coli, whereas in S. pombe genes for hexose transporters, integral membrane proteins, galactose metabolism, and ncRNAs related to cellular stress were overexpressed. In general, our study shows that a conserved \"foraging behavior\" response is observed in these eukaryotic and eubacterial organisms in gluconeogenic carbon sources.","doi":"10.1371/journal.pone.0248513","authors":"Vichi J, Salazar E, Jacinto VJ, Rodriguez LO, Grande R, Dantán-González E, Morett E, Hernández-Mendoza A","authors_abbrev":"Vichi J et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-03-17","publication_year":"2021","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2021-03-19 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15627960","title":"Liquid ultraviolet matrix-assisted laser desorption/ionization -- mass spectrometry for automated proteomic analysis.","citation":"Proteomics 2005 Feb;5(2):360-70","abstract":"We have combined several key sample preparation steps for the use of a liquid matrix system to provide high analytical sensitivity in automated ultraviolet -- matrix-assisted laser desorption/ionisation -- mass spectrometry (UV-MALDI-MS). This new sample preparation protocol employs a matrix-mixture which is based on the glycerol matrix-mixture described by Sze et al. The low-femtomole sensitivity that is achievable with this new preparation protocol enables proteomic analysis of protein digests comparable to solid-state matrix systems. For automated data acquisition and analysis, the MALDI performance of this liquid matrix surpasses the conventional solid-state MALDI matrices. Besides the inherent general advantages of liquid samples for automated sample preparation and data acquisition the use of the presented liquid matrix significantly reduces the extent of unspecific ion signals in peptide mass fingerprints compared to typically used solid matrices, such as 2,5-dihydroxybenzoic acid (DHB) or alpha-cyano-hydroxycinnamic acid (CHCA). In particular, matrix and low-mass ion signals and ion signals resulting from cation adduct formation are dramatically reduced. Consequently, the confidence level of protein identification by peptide mass mapping of in-solution and in-gel digests is generally higher.","authors":"Cramer R, Corless S","authors_abbrev":"Cramer R et al.","pubmed_publication_date":"Feb 2005","pubmed_entrez_date":"2005-01-04","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20456449","title":"ERCC6 founder mutation identified in Finnish patients with COFS syndrome.","citation":"Clin Genet 2010 Dec;78(6):541-7","abstract":"Cerebro-oculo-facio-skeletal (COFS) syndrome is an autosomal recessive disorder characterized by microcephaly, congenital cataracts, facial dysmorphism, neurogenic arthrogryposis, growth failure and severe psychomotor retardation. We report a large consanguineous pedigree from northern Finland with six individuals belonging into four different sibships and affected with typical COFS syndrome phenotype. Two deceased patients have been published previously in 1982 as the first cases exhibiting cerebral calcifications typical for this disorder. Two living and one of the deceased patients were all shown to possess a novel homozygous mutation in the ERCC6 [Cockayne syndrome B (CSB)] gene, thereby confirming the diagnosis on molecular genetic level even for the earlier published cases. Genealogical investigation showed a common ancestor living in a northeastern village in Finland in the 18th century for all six patients implying a founder effect.","doi":"10.1111/j.1399-0004.2010.01424.x","authors":"Jaakkola E, Mustonen A, Olsen P, Miettinen S, Savuoja T, Raams A, Jaspers NG, Shao H, Wu BL, Ignatius J","authors_abbrev":"Jaakkola E et al.","pubmed_publication_date":"Dec 2010","pubmed_entrez_date":"2010-05-12","publication_year":"2010","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC577.09","SPCP25A2.02c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:21189291","title":"Role for cohesin in the formation of a heterochromatic domain at fission yeast subtelomeres.","citation":"Mol Cell Biol 2011 Mar;31(5):1088-97","abstract":"Increasing evidence implicates cohesin in the control of gene expression. Here we report the first analysis of cohesin-dependent gene regulation in fission yeast. Global expression profiling of the mis4-367 cohesin loader mutant identified a small number of upregulated and downregulated genes within subtelomeric domains (SD). These 20- to 40-kb regions between chromosome arm euchromatin and telomere-proximal heterochromatin are characterized by a combination of euchromatin (methylated lysine 4 on histone H3/methylated Tysine 9 on histone H3 [H3K4me]) and heterochromatin (H3K9me) marks. We focused our analysis on the chromosome 1 right SD, which contains several upregulated genes and is bordered on the telomere-distal side by a pair of downregulated genes. We find that the expression changes in the SD also occur in a mutant of the cohesin core component Rad21. Remarkably, mutation of Rad21 results in the depletion of Swi6 binding in the SD. In fact, the Rad21 mutation phenocopied Swi6 loss of function: both mutations led to reduced cohesin binding, reduced H3K9me, and similar gene expression changes in the SD. In particular, expression of the gene pair bordering the SD was dependent both on cohesin and on Swi6. Our data indicate that cohesin participates in the setup of a subtelomeric heterochromatin domain and controls the expression of the genes residing in that domain.","doi":"10.1128/MCB.01290-10","authors":"Dheur S, Saupe SJ, Genier S, Vazquez S, Javerzat JP","authors_abbrev":"Dheur S et al.","pubmed_publication_date":"Mar 2011","pubmed_entrez_date":"2010-12-30","publication_year":"2011","canto_session_key":"e7a39a5199b41598","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC31A2.05c","SPCC338.17c","SPAC664.01c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:38728403","title":"Substrate displacement of CK1 C-termini regulates kinase specificity.","citation":"Sci Adv 2024 May 10;10(19):eadj5185","abstract":"CK1 kinases participate in many signaling pathways, and their regulation is of meaningful biological consequence. CK1s autophosphorylate their C-terminal noncatalytic tails, and eliminating these tails increases substrate phosphorylation in vitro, suggesting that the autophosphorylated C-termini act as inhibitory pseudosubstrates. To test this prediction, we comprehensively identified the autophosphorylation sites on  Schizosaccharomyces pombe  Hhp1 and human CK1ε. Phosphoablating mutations increased Hhp1 and CK1ε activity toward substrates. Peptides corresponding to the C-termini interacted with the kinase domains only when phosphorylated, and substrates competitively inhibited binding of the autophosphorylated tails to the substrate binding grooves. Tail autophosphorylation influenced the catalytic efficiency with which CK1s targeted different substrates, and truncating the tail of CK1δ broadened its linear peptide substrate motif, indicating that tails contribute to substrate specificity as well. Considering autophosphorylation of both T220 in the catalytic domain and C-terminal sites, we propose a displacement specificity model to describe how autophosphorylation modulates substrate specificity for the CK1 family.","doi":"10.1126/sciadv.adj5185","authors":"Cullati SN, Akizuki K, Chen JS, Johnson JL, Yaron-Barir TM, Cantley LC, Gould KL","authors_abbrev":"Cullati SN et al.","pubmed_publication_date":"10 May 2024","pubmed_entrez_date":"2024-05-10","publication_year":"2024","canto_session_key":"1bf2214f97661127","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-05-10 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7889932","title":"Crystal structure of casein kinase-1, a phosphate-directed protein kinase.","citation":"EMBO J 1995 Mar 01;14(5):1015-23","abstract":"The structure of a truncated variant of casein kinase-1 from Schizosaccharomyces pombe, has been determined in complex with MgATP at 2.0 A resolution. The model resembles the 'closed', ATP-bound conformations of the cyclin-dependent kinase 2 and the cAMP-dependent protein kinase, with clear differences in the structure of surface loops that impart unique features to casein kinase-1. The structure is of unphosphorylated, active conformation of casein kinase-1 and the peptide-binding site is fully accessible to substrate.","authors":"Xu RM, Carmel G, Sweet RM, Kuret J, Cheng X","authors_abbrev":"Xu RM et al.","pubmed_publication_date":"01 Mar 1995","pubmed_entrez_date":"1995-03-01","publication_year":"1995","canto_session_key":"ec4424d3ed6a4dc1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-01-30 15:53:30","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-28 15:20:17","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1347.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-28","pdb_entries":[{"pdb_id":"1csn","gene_chains":[{"gene_uniquename":"SPBC1347.06c","chain":"A","position":"1-298"}],"title":"BINARY COMPLEX OF CASEIN KINASE-1 WITH MGATP","entry_authors":"Xu R-M,Cheng X","entry_authors_abbrev":"Xu R-M et al.","reference_uniquename":"PMID:7889932","experimental_method":"X-ray","resolution":"2.0"}]},{"uniquename":"PMID:11514535","title":"Autophosphorylation of archaeal Cdc6 homologues is regulated by DNA.","citation":"J Bacteriol 2001 Sep;183(18):5459-64","abstract":"The initiator protein Cdc6 (Cdc18 in fission yeast) plays an essential role in the initiation of eukaryotic DNA replication. In yeast the protein is expressed before initiation of DNA replication and is thought to be essential for loading of the helicase onto origin DNA. The biochemical properties of the protein, however, are largely unknown. Using three archaeal homologues of Cdc6, it was found that the proteins are autophosphorylated on Ser residues. The winged-helix domain at the C terminus of Cdc6 interacts with DNA, which apparently regulates the autophosphorylation reaction. Yeast Cdc18 was also found to autophosphorylate, suggesting that this function of Cdc6 may play a widely conserved and essential role in replication initiation.","authors":"Grabowski B, Kelman Z","authors_abbrev":"Grabowski B et al.","pubmed_publication_date":"Sep 2001","pubmed_entrez_date":"2001-08-22","publication_year":"2001","canto_session_key":"12569b80abe268ca","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-29 14:09:44","canto_approved_date":"2022-08-04 12:13:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-12 15:21:46","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC14C8.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-01-29"},{"uniquename":"PMID:16524899","title":"Fission yeast Rho5p GTPase is a functional paralogue of Rho1p that plays a role in survival of spores and stationary-phase cells.","citation":"Eukaryot Cell 2006 Mar;5(3):435-46","abstract":"The Rho GTPase family and their effectors are key regulators involved in many eukaryotic cell functions related to actin organization and polarity establishment. Schizosaccharomyces pombe Rho1p is essential, directly activates the (1,3)-beta-d-glucan synthase, and participates in regulation of cell wall growth and morphogenesis. Here we describe the characterization of the fission yeast Rho5p GTPase, highly homologous to Rho1p, sharing 86% identity and 95% similarity. Overexpression of the hyperactive allele rho5-G15V causes a morphological effect similar to that of rho1-G15V, but the penetrance is significantly lower, and overexpression of the dominant-negative allele rho5-T20N causes lysis like that of rho1-T20N. Importantly, overexpression of rho5(+) but no other rho genes is able to rescue the lethality of rho1Delta cells. Shutoff experiments indicated that Rho5p can replace Rho1p, but it is not as effective in maintaining cell wall integrity or actin organization. rho5(+) expression is hardly detected during log-phase growth but is induced under nutritional starvation conditions. rho5Delta cells are viable and do not display any defects during logarithmic growth. However, when rho1(+) expression is repressed during stationary phase, rho5Delta cells display reduced viability. Ascospores lacking Rho5p are less resistant to heat or lytic enzymes than wild-type spores. Moreover, h(90) mutant strains carrying the hyperactive rho5-G15V or the dominant-negative rho5-T20N alleles display severe ascospore formation defects. These results suggest that Rho5p functions in a way similar to, but less efficient than, Rho1p, plays a nonessential role during stationary phase, and participates in the spore wall formation.","authors":"Rincón SA, Santos B, Pérez P","authors_abbrev":"Rincón SA et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-03-10","publication_year":"2006","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F7.04","SPAC20H4.11c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:15992541","title":"The fission yeast homolog of the human transcription factor EAP30 blocks meiotic spindle pole body amplification.","citation":"Dev Cell 2005 Jul;9(1):63-73","abstract":"Centrosome aberrations caused by misregulated centrosome maturation result in defective spindle and genomic instability. Here we report that the fission yeast homolog of the human transcription factor EAP30, Dot2, negatively regulates meiotic spindle pole body (SPB, the yeast equivalent of centrosome) maturation. dot2 mutants show excess electron-dense material accumulating near SPBs, which we refer to as aberrant microtubule organization centers (AMtOCs). These AMtOCs assemble multipolar spindles, leading to chromosome missegregation. SPB aberrations were associated with elevated levels of Pcp1, the fission yeast ortholog of pericentrin/kentrin, and reducing pcp1(+) expression significantly suppressed AMtOCs in dot2-439 cells. Our findings, therefore, uncover meiosis-specific regulation of SPB maturation and provide evidence that a member of the conserved EAP30 family is required for maintenance of genome stability through regulation of SPB maturation. EAP30 is part of a transcription factor complex associated with acute myeloid leukemia, so these results may have relevance to human cancer.","authors":"Jin Y, Mancuso JJ, Uzawa S, Cronembold D, Cande WZ","authors_abbrev":"Jin Y et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-07-05","publication_year":"2005","canto_session_key":"1ebe4a1548de4aff","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-05-09 16:38:17","canto_approved_date":"2024-04-03 15:35:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-05-09 16:38:09","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC651.05c","SPBC19C2.05","SPAC6G9.06c"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2017-05-09"},{"uniquename":"PMID:14504268","title":"Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication.","citation":"J Cell Biol 2003 Sep 29;162(7):1211-21","abstract":"Centrins are calmodulin-like proteins present in microtubule-organizing centers. The Saccharomyces cerevisiae centrin, Cdc31p, was functionally tagged with a single Z domain of protein A, and used in pull-down experiments to isolate Cdc31p-binding proteins. One of these, Sfi1p, localizes to the half-bridge of the spindle pole body (SPB), where Cdc31p is also localized. Temperature-sensitive mutants in SFI1 show a defect in SPB duplication and genetic interactions with cdc31-1. Sfi1p contains multiple internal repeats that are also present in a Schizosaccharomyces pombe protein, which also localizes to the SPB, and in several human proteins, one of which localizes close to the centriole region. Cdc31p binds directly to individual Sfi1 repeats in a 1:1 ratio, so a single molecule of Sfi1p binds multiple molecules of Cdc31p. The centrosomal human protein containing Sfi1 repeats also binds centrin in the repeat region, showing that this centrin-binding motif is conserved.","authors":"Kilmartin JV","authors_abbrev":"Kilmartin JV","pubmed_publication_date":"29 Sep 2003","pubmed_entrez_date":"2003-09-25","publication_year":"2003","canto_session_key":"2a6bdba9e752cc0c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-11-22 12:41:33","canto_approved_date":"2017-11-22 12:41:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-22 12:41:26","canto_added_date":"2012-02-24 05:50:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC8D2.05c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-11-22"},{"uniquename":"EMBL:AU013273","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37189341","title":"Regulation of the SUV39H Family Methyltransferases: Insights from Fission Yeast.","citation":"Biomolecules 2023 Mar 25;13(4)","abstract":"Histones, which make up nucleosomes, undergo various post-translational modifications, such as acetylation, methylation, phosphorylation, and ubiquitylation. In particular, histone methylation serves different cellular functions depending on the location of the amino acid residue undergoing modification, and is tightly regulated by the antagonistic action of histone methyltransferases and demethylases. The SUV39H family of histone methyltransferases (HMTases) are evolutionarily conserved from fission yeast to humans and play an important role in the formation of higher-order chromatin structures called heterochromatin. The SUV39H family HMTases catalyzes the methylation of histone H3 lysine 9 (H3K9), and this modification serves as a binding site for heterochromatin protein 1 (HP1) to form a higher-order chromatin structure. While the regulatory mechanism of this family of enzymes has been extensively studied in various model organisms, Clr4, a fission yeast homologue, has made an important contribution. In this review, we focus on the regulatory mechanisms of the SUV39H family of proteins, in particular, the molecular mechanisms revealed by the studies of the fission yeast Clr4, and discuss their generality in comparison to other HMTases.","doi":"10.3390/biom13040593","authors":"Nakamura R, Nakayama JI","authors_abbrev":"Nakamura R et al.","pubmed_publication_date":"25 Mar 2023","pubmed_entrez_date":"2023-05-16","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-05-17 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11278267","title":"The highly conserved protein methyltransferase, Skb1, is a mediator of hyperosmotic stress response in the fission yeast Schizosaccharomyces pombe.","citation":"J Biol Chem 2001 May 04;276(18):14549-52","abstract":"The p21-activated kinase, Shk1, is required for cell viability, establishment and maintenance of cell polarity, and proper mating response in the fission yeast, Schizosaccharomyces pombe. Previous genetic studies suggested that a presumptive protein methyltransferase, Skb1, functions as a positive modulator of Shk1. However, unlike Shk1, Skb1 is not required for viability or mating of S. pombe cells and contributes only modestly to the regulation of cell morphology under normal growth conditions. Here we demonstrate that Skb1 plays a more significant role in regulating cell growth and polarity under conditions of hyperosmotic stress. We provide evidence that the inability of skb1Delta cells to properly maintain cell polarity in hyperosmotic conditions results from inefficient subcellular targeting of F-actin. We show that Skb1 localizes to cell ends, sites of septation, and nuclei of S. pombe cells. Hyperosmotic shock results in substantial delocalization of Skb1 from cell ends and nuclei, as well as stimulation of Skb1 protein methyltransferase activity. Taken together, our results demonstrate a new role for Skb1 as a mediator of hyperosmotic stress response in fission yeast. We show that the protein methyltransferase activity of the human Skb1 homolog, Skb1Hs, is also stimulated by hyperosmotic stress in fission yeast, providing evidence for evolutionary conservation of a role for Skb1-related proteins as mediators of hyperosmotic stress response, as well as mechanisms involved in regulating this novel class of protein methyltransferases.","authors":"Bao S, Qyang Y, Yang P, Kim H, Du H, Bartholomeusz G, Henkel J, Pimental R, Verde F, Marcus S","authors_abbrev":"Bao S et al.","pubmed_publication_date":"04 May 2001","pubmed_entrez_date":"2001-03-30","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC16H5.11c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:38254628","title":"Gross Chromosomal Rearrangement at Centromeres.","citation":"Biomolecules 2023 Dec 24;14(1)","abstract":"Centromeres play essential roles in the faithful segregation of chromosomes. CENP-A, the centromere-specific histone H3 variant, and heterochromatin characterized by di- or tri-methylation of histone H3 9th lysine (H3K9) are the hallmarks of centromere chromatin. Contrary to the epigenetic marks, DNA sequences underlying the centromere region of chromosomes are not well conserved through evolution. However, centromeres consist of repetitive sequences in many eukaryotes, including animals, plants, and a subset of fungi, including fission yeast. Advances in long-read sequencing techniques have uncovered the complete sequence of human centromeres containing more than thousands of alpha satellite repeats and other types of repetitive sequences. Not only tandem but also inverted repeats are present at a centromere. DNA recombination between centromere repeats can result in gross chromosomal rearrangement (GCR), such as translocation and isochromosome formation. CENP-A chromatin and heterochromatin suppress the centromeric GCR. The key player of homologous recombination, Rad51, safeguards centromere integrity through conservative noncrossover recombination between centromere repeats. In contrast to Rad51-dependent recombination, Rad52-mediated single-strand annealing (SSA) and microhomology-mediated end-joining (MMEJ) lead to centromeric GCR. This review summarizes recent findings on the role of centromere and recombination proteins in maintaining centromere integrity and discusses how GCR occurs at centromeres.","doi":"10.3390/biom14010028","authors":"Xu R, Pan Z, Nakagawa T","authors_abbrev":"Xu R et al.","pubmed_publication_date":"24 Dec 2023","pubmed_entrez_date":"2024-01-23","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-01-24 00:25:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30530495","title":"The 40S ribosomal protein uS5 (RPS2) assembles into an extraribosomal complex with human ZNF277 that competes with the PRMT3-uS5 interaction.","citation":"J Biol Chem 2019 Feb 08;294(6):1944-1955","abstract":"Ribosomal (r)-proteins are generally viewed as ubiquitous, constitutive proteins that simply function to maintain ribosome integrity. However, findings in the past decade have led to the idea that r-proteins have evolved specialized functions beyond the ribosome. For example, the 40S ribosomal protein uS5 (RPS2) is known to form an extraribosomal complex with the protein arginine methyltransferase PRMT3 that is conserved from fission yeast to humans. However, the full scope of uS5's extraribosomal functions, including whether uS5 interacts with any other proteins, is not known. In this study, we identify the conserved zinc finger protein 277 (ZNF277) as a new uS5-associated protein by using quantitative proteomics approaches in human cells. As previously shown for PRMT3, we found that ZNF277 uses a C2H2-type zinc finger domain to recognize uS5. Analysis of protein-protein interactions in living cells indicated that the ZNF277-uS5 complex is found in the cytoplasm and the nucleolus. Furthermore, we show that ZNF277 and PRMT3 compete for uS5 binding, because overexpression of PRMT3 inhibited the formation of the ZNF277-uS5 complex, whereas depletion of cellular ZNF277 resulted in increased levels of uS5-PRMT3. Notably, our results reveal that ZNF277 recognizes nascent uS5 in the course of mRNA translation, suggesting cotranslational assembly of the ZNF277-uS5 complex. Our findings thus unveil an intricate network of evolutionarily conserved protein-protein interactions involving extraribosomal uS5, suggesting a key role for uS5 beyond the ribosome.","doi":"10.1074/jbc.RA118.004928","authors":"Dionne KL, Bergeron D, Landry-Voyer AM, Bachand F","authors_abbrev":"Dionne KL et al.","pubmed_publication_date":"08 Feb 2019","pubmed_entrez_date":"2018-12-12","publication_year":"2019","canto_session_key":"a5925fdc3fbbcb27","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2018-12-13 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC576.08c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:1324908","title":"Regulation of CDP-diacylglycerol synthesis and utilization by inositol and choline in Schizosaccharomyces pombe.","citation":"J Bacteriol 1992 Sep;174(17):5711-8","abstract":"CDP-diacylglycerol (CDP-DG) is an important branchpoint intermediate in eucaryotic phospholipid biosynthesis and could be a key regulatory site in phospholipid metabolism. Therefore, we examined the effects of growth phase, phospholipid precursors, and the disruption of phosphatidylcholine (PC) synthesis on the membrane-associated phospholipid biosynthetic enzymes CDP-DG synthase, phosphatidylglycerolphosphate (PGP) synthase, phosphatidylinositol (PI) synthase, and phosphatidylserine (PS) synthase in cell extracts of the fission yeast Schizosaccharomyces pombe. In complete synthetic medium containing inositol, maximal expression of CDP-DG synthase, PGP synthase, PI synthase, and PS synthase in wild-type cells occurred in the exponential phase of growth and decreased two- to fourfold in the stationary phase of growth. In cells starved for inositol, this decrease in PGP synthase, PI synthase, and PS synthase expression was not observed. Starvation for inositol resulted in a twofold derepression of PGP synthase and PS synthase expression, while PI synthase expression decreased initially and then remained constant. Upon the addition of inositol to inositol-starved cells, there was a rapid and continued increase in PI synthase expression. We examined expression of these enzymes in cho2 and cho1 mutants, which are blocked in the methylation pathway for synthesis of PC. Choline starvation resulted in a decrease in PS synthase and CDP-DG synthase expression in cho1 but not cho2 cells. Expression of PGP synthase and PI synthase was not affected by choline starvation. Inositol starvation resulted in a 1.7-fold derepression of PGP synthase expression in cho2 but not cho1 cells when PC was synthesized. PS synthase expression was not depressed, while CDP-DG synthase and PI synthase expression decreased in cho2 and cho1 cells in the absence of inositol. These results demonstrate that (i) CDP-DG synthase, PGP synthase, PI synthase, and PS synthase are similarly regulated by growth phase; (ii) inositol affects the expression of PGP synthase, PI synthase, and PS synthase; (iii) disruption of the methylation pathway results in aberrant patterns of regulation of growth phase and phospholipid precursors. Important differences between S. pombe and Saccharomyces cerevisiae with regard to regulation of these enzymes are discussed.","authors":"Gaynor PM, Greenberg ML","authors_abbrev":"Gaynor PM et al.","pubmed_publication_date":"Sep 1992","pubmed_entrez_date":"1992-09-01","publication_year":"1992","canto_session_key":"ee55ca52710667a5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-02-12 15:08:05","canto_approved_date":"2023-12-30 16:40:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-28 16:10:38","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1442.12","SPBC26H8.03","SPAC1D4.08","SPBP18G5.02","SPBC13A2.03","SPBC337.16"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2017-02-12"},{"uniquename":"PMID:26696398","title":"Autophagy is required for efficient meiosis progression and proper meiotic chromosome segregation in fission yeast.","citation":"Genes Cells 2016 Jan;21(1):65-87","abstract":"Autophagy is a conserved intracellular degradation system, which contributes to development and differentiation of various organisms. Yeast cells undergo meiosis under nitrogen-starved conditions and require autophagy for meiosis initiation. However, the precise roles of autophagy in meiosis remain unclear. Here, we show that autophagy is required for efficient meiosis progression and proper meiotic chromosome segregation in fission yeast. Autophagy-defective strains bearing a mutation in the autophagy core factor gene atg1, atg7, or atg14 exhibit deformed nuclear structures during meiosis. These mutant cells require an extracellular nitrogen supply for meiosis progression following their entry into meiosis and show delayed meiosis progression even with a nitrogen supply. In addition, they show frequent chromosome dissociation from the spindle together with spindle overextension, forming extra nuclei. Furthermore, Aurora kinase, which regulates chromosome segregation and spindle elongation, is significantly increased at the centromere and spindle in the mutant cells. Aurora kinase down-regulation eliminated delayed initiation of meiosis I and II, chromosome dissociation, and spindle overextension, indicating that increased Aurora kinase activity may cause these aberrances in the mutant cells. Our findings show a hitherto unrecognized relationship of autophagy with the nuclear structure, regulation of cell cycle progression, and chromosome segregation in meiosis.","doi":"10.1111/gtc.12320","authors":"Matsuhara H, Yamamoto A","authors_abbrev":"Matsuhara H et al.","pubmed_publication_date":"Jan 2016","pubmed_entrez_date":"2015-12-24","publication_year":"2016","canto_session_key":"393d0a5aae35d3ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Ayumu Yamamoto","canto_first_approved_date":"2017-05-05 06:34:23","canto_approved_date":"2022-12-29 19:10:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-05-20 11:46:18","canto_added_date":"2015-12-25 01:19:07","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":44,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Ayumu Yamamoto","community_curator":true,"annotation_count":9,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.05c","SPCC63.08c","SPBC29A3.02c","SPBC1711.13","SPAC25A8.02","SPCC320.13c","SPBC1A4.02c","SPBC11B10.02c","SPBC20F10.06"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-05-05"},{"uniquename":"PMID:21195141","title":"Global genome organization mediated by RNA polymerase III-transcribed genes in fission yeast.","citation":"Gene 2012 Feb 10;493(2):195-200","abstract":"Eukaryotic genomes exist as an elaborate three-dimensional structure in the nucleus. Recent studies have shown that this higher-order organization of the chromatin fiber is coupled to various nuclear processes including transcription. In fission yeast, we demonstrated that RNA polymerase III (Pol III)-transcribed genes such as tRNA and 5S rRNA genes, dispersed throughout chromosomal arm regions, localize to centromeres in interphase. This centromeric association of Pol III genes, mediated by the condensin complex, becomes prominent during mitosis. Here, we discuss potential roles of the Pol III gene-mediated genome organization during interphase and mitosis, and hypothesize that the interphase genome structure serves as a scaffold for the efficient assembly of condensed mitotic chromosomes and that tethering of chromosomal arm regions to centromeres allows chromosomes to properly segregate along the spindle microtubules during anaphase.","doi":"10.1016/j.gene.2010.12.011","authors":"Iwasaki O, Noma K","authors_abbrev":"Iwasaki O et al.","pubmed_publication_date":"10 Feb 2012","pubmed_entrez_date":"2011-01-04","publication_year":"2012","canto_triage_status":"3D genome organization","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30462301","title":"Structural insights into chromosome attachment to the nuclear envelope by an inner nuclear membrane protein Bqt4 in fission yeast.","citation":"Nucleic Acids Res 2019 Feb 20;47(3):1573-1584","abstract":"The dynamic association of chromosomes with the nuclear envelope (NE) is essential for chromosome maintenance. Schizosaccharomyces pombe inner nuclear membrane protein Bqt4 plays a critical role in connecting telomeres to the NE, mainly through a direct interaction with the telomeric protein Rap1. Bqt4 also interacts with Lem2 for pericentric heterochromatin maintenance. How Bqt4 coordinates the interactions with different proteins to exert their functions is unclear. Here, we report the crystal structures of the N-terminal domain of Bqt4 in complexes with Bqt4-binding motifs from Rap1, Lem2, and Sad1. The structural, biochemical and cellular analyses reveal that the N-terminal domain of Bqt4 is a protein-interaction module that recognizes a consensus motif and plays essential roles in telomere-NE association and meiosis progression. Phosphorylation of Bqt4-interacting proteins may act as a switch to regulate these interactions during cell cycles. Our studies provide structural insights into the identification and regulation of Bqt4-mediated interactions.","doi":"10.1093/nar/gky1186","authors":"Hu C, Inoue H, Sun W, Takeshita Y, Huang Y, Xu Y, Kanoh J, Chen Y","authors_abbrev":"Hu C et al.","pubmed_publication_date":"20 Feb 2019","pubmed_entrez_date":"2018-11-22","publication_year":"2019","canto_session_key":"f965fe048f417771","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-07 23:26:47","canto_approved_date":"2023-06-08 10:50:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-03 12:21:07","canto_added_date":"2018-11-23 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":53,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.10","SPBC12D12.01","SPBC19C7.10","SPBC1778.02"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2019-10-07","pdb_entries":[{"pdb_id":"6a6w","gene_chains":[{"gene_uniquename":"SPBC19C7.10","chain":"A","position":"2-140"},{"gene_uniquename":"SPBC12D12.01","chain":"B","position":"88-101"}],"title":"Crystal structure of fission yeast inner membrane protein Bqt4 in complex with Sad1","entry_authors":"Chen Y,Hu C","entry_authors_abbrev":"Chen Y et al.","reference_uniquename":"PMID:30462301","experimental_method":"X-ray","resolution":"2.601"},{"pdb_id":"5yc2","gene_chains":[{"gene_uniquename":"SPBC19C7.10","chain":"A/A/C/C","position":"9-140"},{"gene_uniquename":"SPBC1778.02","chain":"B/D","position":"498-512"}],"title":"Crystal structure of inner membrane protein Bqt4 in complex with telomeric protein Rap1","entry_authors":"Chen Y,Hu C","entry_authors_abbrev":"Chen Y et al.","reference_uniquename":"PMID:30462301","experimental_method":"X-ray","resolution":"2.704"},{"pdb_id":"5yca","gene_chains":[{"gene_uniquename":"SPBC19C7.10","chain":"A/A","position":"9-140"},{"gene_uniquename":"SPAC18G6.10","chain":"C","position":"261-279"}],"title":"Crystal structure of inner membrane protein Bqt4 in complex with LEM2","entry_authors":"Chen Y,Hu C","entry_authors_abbrev":"Chen Y et al.","reference_uniquename":"PMID:30462301","experimental_method":"X-ray","resolution":"1.57"}]},{"uniquename":"PMID:10567571","title":"Conservation of histone binding and transcriptional repressor functions in a Schizosaccharomyces pombe Tup1p homolog.","citation":"Mol Cell Biol 1999 Dec;19(12):8461-8","abstract":"The Ssn6p-Tup1p corepressor complex is important to the regulation of several diverse genes in Saccharomyces cerevisiae and serves as a model for corepressor functions. To investigate the evolutionary conservation of these functions, sequences homologous to the S. cerevisiae TUP1 gene were cloned from Kluyveromyces lactis (TUP1) and Schizosaccharomyces pombe (tup11(+)). Interestingly, while the K. lactis TUP1 gene complemented an S. cerevisiae tup1 null mutation, the S. pombe tup11(+) gene did not, even when expressed under the control of the S. cerevisiae TUP1 promoter. However, an S. pombe Tup11p-LexA fusion protein repressed transcription of a corresponding reporter gene, indicating that this Tup1p homolog has intrinsic repressor activity. Moreover, a chimeric protein containing the amino-terminal Ssn6p-binding domain of S. cerevisiae Tup1p and 544 amino acids from the C-terminal region of S. pombe Tup11p complemented the S. cerevisiae tup1 mutation. The failure of native S. pombe Tup11p to complement loss of Tup1p functions in S. cerevisiae corresponds to an inability to bind to S. cerevisiae Ssn6p in vitro. Disruption of tup11(+) in combination with a disruption of tup12(+), another TUP1 homolog gene in S. pombe, causes a defect in glucose repression of fbp1(+), suggesting that S. pombe Tup1p homologs function as repressors in S. pombe. Furthermore, Tup11p binds specifically to histones H3 and H4 in vitro, indicating that both the repression and histone binding functions of Tup1p-related proteins are conserved across species.","authors":"Mukai Y, Matsuo E, Roth SY, Harashima S","authors_abbrev":"Mukai Y et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-11-24","publication_year":"1999","canto_session_key":"ee1bdbedc81ae324","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-06-07 10:19:21","canto_approved_date":"2026-01-06 13:07:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-06-07 10:19:15","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC630.14c","SPBC1198.14c","SPAC18B11.10"],"gene_count":3,"ltp_gene_count":2,"approved_date":"2019-06-07"},{"uniquename":"PMID:32034465","title":"Genetic investigation of formaldehyde-induced DNA damage response in Schizosaccharomyces pombe.","citation":"Curr Genet 2020 Jun;66(3):593-605","abstract":"Formaldehyde is a common environmental pollutant and is associated with adverse health effects. Formaldehyde is also considered to be a carcinogen because it can form DNA adducts, leading to genomic instability. How these adducts are prevented and removed is not fully understood. In this study, we used the fission yeast Schizosaccharomyces pombe as a model organism to investigate cellular tolerance pathways against formaldehyde exposure. We show that Fmd1 is a major formaldehyde dehydrogenase that functions to detoxify formaldehyde and that Fmd1 is critical to minimize formaldehyde-mediated DNA lesions. Our investigation revealed that nucleotide excision repair and homologous recombination have major roles in cellular tolerance to formaldehyde, while mutations in the Fanconi anemia, translesion synthesis, and base excision repair pathways also render cells sensitive to formaldehyde. We also demonstrate that loss of Wss1 or Wss2, proteases involved in the removal of DNA-protein crosslinks, sensitizes cells to formaldehyde and leads to replication defects. These results suggest that formaldehyde generates a variety of DNA lesions, including interstrand crosslinks, DNA-protein crosslinks, and base adducts. Thus, our genetic studies provide a framework for future investigation regarding health effects resulting from formaldehyde exposure.","doi":"10.1007/s00294-020-01057-z","authors":"Anandarajan V, Noguchi C, Oleksak J, Grothusen G, Terlecky D, Noguchi E","authors_abbrev":"Anandarajan V et al.","pubmed_publication_date":"Jun 2020","pubmed_entrez_date":"2020-02-09","publication_year":"2020","canto_session_key":"296774c7adb28ef3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Eishi Noguchi","canto_first_approved_date":"2020-04-20 14:04:50","canto_approved_date":"2026-01-14 22:28:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-31 15:16:34","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[{"name":"Eishi Noguchi","community_curator":true,"annotation_count":46,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":53,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1442.07c","SPBC4F6.15c","SPCC550.10","SPBC3D6.10","SPAC22A12.01c","SPAC30D11.07","SPAC30D11.10","SPAC9E9.09c","SPCC13B11.04c","SPAC9.05","SPCC13B11.01","SPBC146.06c","SPAC521.02","SPAC688.10","SPAC922.07c","SPCC553.07c","SPBC16A3.11","SPBC1198.01","SPBC216.06c","SPCC970.01","SPAC3G6.11","SPAC9E9.08","SPBC216.05","SPAC644.14c","SPBC1539.07c"],"gene_count":25,"ltp_gene_count":25,"approved_date":"2020-04-20"},{"uniquename":"PMID:8537298","title":"Transcriptional regulation of catalase gene in the fission yeast Schizosaccharomyces pombe: molecular cloning of the catalase gene and northern blot analyses of the transcript.","citation":"J Biochem 1995 Jul;118(1):109-16","abstract":"Exposure of Schizosaccharomyces pombe cells to various stresses including 0.2 mM hydrogen peroxide, 50 microM menadione, 10 J/m2 of UV irradiation at 255 nm, and high osmolarity (0.5 M sorbitol or 0.3 M NaCl) induces catalase [EC 1.11.1.6] activity. A part of the catalase gene of S. pombe was amplified by PCR with oligonucleotide primers designed from amino acid sequences conserved in several species of catalases. The catalase gene including its flanking sequence of S. pombe was cloned from a genomic DNA library of S. pombe, which was constructed on the EMBL3 vector, using the PCR-amplified DNA as a radioactive probe. A 3.5 kb HindIII fragment, which hybridized with the PCR-amplified probe, was subcloned into pUC19 and sequenced. The fragment contains one long open reading frame without any intron. The polypeptide deduced from the nucleotide sequence consists of 512 amino acid residues and is homologous to several other catalases. Amino acid sequences of the proteolytic peptides obtained from the purified catalase of S. pombe coincided with the amino acid sequence predicted from the DNA sequence. Transcription of this gene starts at 370 bases upstream of the initiation methionine codon. Northern blot analyses of the catalase mRNA revealed that the stresses which induce the catalase activity also induce the transcription of the catalase gene. The induction of the catalase mRNA by hydrogen peroxide is not inhibited by cycloheximide or staurosporine.","authors":"Nakagawa CW, Mutoh N, Hayashi Y","authors_abbrev":"Nakagawa CW et al.","pubmed_publication_date":"Jul 1995","pubmed_entrez_date":"1995-07-01","publication_year":"1995","canto_session_key":"efa39b714ee98362","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-01-18 18:43:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-01-14 11:33:52","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC757.07c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-01-14"},{"uniquename":"PMID:37485750","title":"Genetic effects on molecular network states explain complex traits.","citation":"Mol Syst Biol 2023 Aug 08;19(8):e11493","abstract":"The complexity of many cellular and organismal traits results from the integration of genetic and environmental factors via molecular networks. Network structure and effect propagation are best understood at the level of functional modules, but so far, no concept has been established to include the global network state. Here, we show when and how genetic perturbations lead to molecular changes that are confined to small parts of a network versus when they lead to modulation of network states. Integrating multi-omics profiling of genetically heterogeneous budding and fission yeast strains with an array of cellular traits identified a central state transition of the yeast molecular network that is related to PKA and TOR (PT) signaling. Genetic variants affecting this PT state globally shifted the molecular network along a single-dimensional axis, thereby modulating processes including energy and amino acid metabolism, transcription, translation, cell cycle control, and cellular stress response. We propose that genetic effects can propagate through large parts of molecular networks because of the functional requirement to centrally coordinate the activity of fundamental cellular processes.","doi":"10.15252/msb.202211493","authors":"Weith M, Großbach J, Clement-Ziza M, Gillet L, Rodríguez-López M, Marguerat S, Workman CT, Picotti P, Bähler J, Aebersold R, Beyer A","authors_abbrev":"Weith M et al.","pubmed_publication_date":"08 Aug 2023","pubmed_entrez_date":"2023-07-24","publication_year":"2023","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2023-07-25 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23028933","title":"Sip1, a conserved AP-1 accessory protein, is important for Golgi/endosome trafficking in fission yeast.","citation":"PLoS One 2012;7(9):e45324","abstract":"We had previously identified the mutant allele of apm1(+) that encodes a homolog of the mammalian μ 1A subunit of the clathrin-associated adaptor protein-1 (AP-1) complex and demonstrated that the AP-1 complex plays a role in Golgi/endosome trafficking, secretion, and vacuole fusion in fission yeast. Here, we isolated a mutant allele of its4(+)/sip1(+), which encodes a conserved AP-1 accessory protein. The its4-1/sip1-i4 mutants and apm1-deletion cells exhibited similar phenotypes, including sensitivity to the calcineurin inhibitor FK506, Cl(-) and valproic acid as well as various defects in Golgi/endosomal trafficking and cytokinesis. Electron micrographs of sip1-i4 mutants revealed vacuole fragmentation and accumulation of abnormal Golgi-like structures and secretory vesicles. Overexpression of Apm1 suppressed defective membrane trafficking in sip1-i4 mutants. The Sip1-green fluorescent protein (GFP) co-localized with Apm1-mCherry at Golgi/endosomes, and Sip1 physically interacted with each subunit of the AP-1 complex. We found that Sip1 was a Golgi/endosomal protein and the sip1-i4 mutation affected AP-1 localization at Golgi/endosomes, thus indicating that Sip1 recruited the AP-1 complex to endosomal membranes by physically interacting with each subunit of this complex. Furthermore, Sip1 is required for the correct localization of Bgs1/Cps1, 1,3-β-D-glucan synthase to polarized growth sites. Consistently, the sip1-i4 mutants displayed a severe sensitivity to micafungin, a potent inhibitor of 1,3-β-D-glucan synthase. Taken together, our findings reveal a role for Sip1 in the regulation of Golgi/endosome trafficking in coordination with the AP-1 complex, and identified Bgs1, required for cell wall synthesis, as the new cargo of AP-1-dependent trafficking.","doi":"10.1371/journal.pone.0045324","authors":"Yu Y, Kita A, Udo M, Katayama Y, Shintani M, Park K, Hagihara K, Umeda N, Sugiura R","authors_abbrev":"Yu Y et al.","pubmed_publication_date":"2012","pubmed_entrez_date":"2012-10-03","publication_year":"2012","canto_session_key":"81d8a22cd0b8ab13","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP16F5.07","SPCP1E11.06","SPAP27G11.06c","SPBC947.02","SPBC27B12.08"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:19913479","title":"Cryo-EM reveals promoter DNA binding and conformational flexibility of the general transcription factor TFIID.","citation":"Structure 2009 Nov 11;17(11):1442-52","abstract":"The general transcription factor IID (TFIID) is required for initiation of RNA polymerase II-dependent transcription at many eukaryotic promoters. TFIID comprises the TATA-binding protein (TBP) and several conserved TBP-associated factors (TAFs). Recognition of the core promoter by TFIID assists assembly of the preinitiation complex. Using cryo-electron microscopy in combination with methods for ab initio single-particle reconstruction and heterogeneity analysis, we have produced density maps of two conformational states of Schizosaccharomyces pombe TFIID, containing and lacking TBP. We report that TBP-binding is coupled to a massive histone-fold domain rearrangement. Moreover, docking of the TBP-TAF1(N-terminus) atomic structure to the TFIID map and reconstruction of a TAF-promoter DNA complex helps to account for TAF-dependent regulation of promoter-TBP and promoter-TAF interactions.","doi":"10.1016/j.str.2009.09.007","authors":"Elmlund H, Baraznenok V, Linder T, Szilagyi Z, Rofougaran R, Hofer A, Hebert H, Lindahl M, Gustafsson CM","authors_abbrev":"Elmlund H et al.","pubmed_publication_date":"11 Nov 2009","pubmed_entrez_date":"2009-11-17","publication_year":"2009","canto_session_key":"7ecdc999a92abc03","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-06-13 04:05:52","canto_approved_date":"2024-06-13 04:05:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-13 04:05:46","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1002.04c","SPCC1259.06","SPAC15A10.02","SPAC823.06","SPBC15D4.14","SPAC12G12.05c","SPCC1494.02c","SPBC21H7.02","SPAC23G3.09","SPCC16C4.18c","SPCC5E4.03c","SPAC13F5.02c","SPAC3A12.05c","SPAC2G11.14"],"gene_count":14,"ltp_gene_count":14,"approved_date":"2024-06-13"},{"uniquename":"PMID:23223895","title":"Phosphorylation network dynamics in the control of cell cycle transitions.","citation":"J Cell Sci 2012 Oct 15;125(Pt 20):4703-11","abstract":"Fifteen years ago, it was proposed that the cell cycle in fission yeast can be driven by quantitative changes in the activity of a single protein kinase complex comprising a cyclin - namely cyclin B - and cyclin dependent kinase 1 (Cdk1). When its activity is low, Cdk1 triggers the onset of S phase; when its activity level exceeds a specific threshold, it promotes entry into mitosis. This model has redefined our understanding of the essential functional inputs that organize cell cycle progression, and its main principles now appear to be applicable to all eukaryotic cells. But how does a change in the activity of one kinase generate ordered progression through the cell cycle in order to separate DNA replication from mitosis? To answer this question, we must consider the biochemical processes that underlie the phosphorylation of Cdk1 substrates. In this Commentary, we discuss recent findings that have shed light on how the threshold levels of Cdk1 activity that are required for progression through each phase are determined, how an increase in Cdk activity generates directionality in the cell cycle, and why cell cycle transitions are abrupt rather than gradual. These considerations lead to a general quantitative model of cell cycle control, in which opposing kinase and phosphatase activities have an essential role in ensuring dynamic transitions.","doi":"10.1242/jcs.106351","authors":"Fisher D, Krasinska L, Coudreuse D, Novák B","authors_abbrev":"Fisher D et al.","pubmed_publication_date":"15 Oct 2012","pubmed_entrez_date":"2012-12-11","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17707223","title":"Dicer finds a new partner in transcriptional gene silencing.","citation":"Mol Cell 2007 Aug 17;27(4):519-20","abstract":"In a recent study in Molecular Cell, Colmenares et al. (2007) showed that fission yeast Dicer is physically and functionally associated with RNA-dependent RNA polymerase complex (RDRC), revealing a concerted mechanism in transcriptional gene silencing.","authors":"Shiekhattar R","authors_abbrev":"Shiekhattar R","pubmed_publication_date":"17 Aug 2007","pubmed_entrez_date":"2007-08-21","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37126401","title":"Loops and the activity of loop extrusion factors constrain chromatin dynamics.","citation":"Mol Biol Cell 2023 Jul 01;34(8):ar78","abstract":"The chromosomes-DNA polymers and their binding proteins-are compacted into a spatially organized, yet dynamic, three-dimensional structure. Recent genome-wide chromatin conformation capture experiments reveal a hierarchical organization of the DNA structure that is imposed, at least in part, by looping interactions arising from the activity of loop extrusion factors. The dynamics of chromatin reflects the response of the polymer to a combination of thermal fluctuations and active processes. However, how chromosome structure and enzymes acting on chromatin together define its dynamics remains poorly understood. To gain insight into the structure-dynamics relationship of chromatin, we combine high-precision microscopy in living  Schizosaccharomyces pombe  cells with systematic genetic perturbations and Rouse model polymer simulations. We first investigated how the activity of two loop extrusion factors, the cohesin and condensin complexes, influences chromatin dynamics. We observed that deactivating cohesin, or to a lesser extent condensin, increased chromatin mobility, suggesting that loop extrusion constrains rather than agitates chromatin motion. Our corresponding simulations reveal that the introduction of loops is sufficient to explain the constraining activity of loop extrusion factors, highlighting that the conformation adopted by the polymer plays a key role in defining its dynamics. Moreover, we find that the number of loops or residence times of loop extrusion factors influence the dynamic behavior of the chromatin polymer. Last, we observe that the activity of the INO80 chromatin remodeler, but not the SWI/SNF or RSC complexes, is critical for ATP-dependent chromatin mobility in fission yeast. Taking the data together, we suggest that thermal and INO80-dependent activities exert forces that drive chromatin fluctuations, which are constrained by the organization of the chromosome into loops.","doi":"10.1091/mbc.E23-04-0119","authors":"Bailey MLP, Surovtsev I, Williams JF, Yan H, Yuan T, Li K, Duseau K, Mochrie SGJ, King MC","authors_abbrev":"Bailey MLP et al.","pubmed_publication_date":"01 Jul 2023","pubmed_entrez_date":"2023-05-01","publication_year":"2023","canto_session_key":"b4e7159963874dbc","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-05-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32614646","title":"Genetic suppression of defective profilin by attenuated Myosin II reveals a potential role for Myosin II in actin dynamics in vivo in fission yeast.","citation":"Mol Biol Cell 2020 Sep 01;31(19):2107-2114","abstract":"The actin cytoskeleton plays a variety of roles in eukaryotic cell physiology, ranging from cell polarity and migration to cytokinesis. Key to the function of the actin cytoskeleton is the mechanisms that control its assembly, stability, and turnover. Through genetic analyses in  Schizosaccharomyces pombe , we found that  myo2 -S1 ( myo2 -G515D), a Myosin II mutant allele, was capable of rescuing lethality caused by partial defects in actin nucleation/stability caused, for example, through compromised function of the actin-binding protein Cdc3-profilin. The mutation in  myo2 -S1 affects the activation loop of Myosin II, which is involved in physical interaction with subdomain 1 of actin and in stimulating the ATPase activity of Myosin. Consistently, actomyosin rings in  myo2 -S1 cell ghosts were unstable and severely compromised in contraction on ATP addition. These studies strongly suggest a role for Myo2 in actin cytoskeletal disassembly and turnover in vivo, and that compromise of this activity leads to genetic suppression of mutants defective in actin filament assembly/stability at the division site.","doi":"10.1091/mbc.E20-04-0224","authors":"Zambon P, Palani S, Jadhav SS, Gayathri P, Balasubramanian MK","authors_abbrev":"Zambon P et al.","pubmed_publication_date":"01 Sep 2020","pubmed_entrez_date":"2020-07-03","publication_year":"2020","canto_session_key":"bd33532b60f3d4b2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-07-04 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26720418","title":"Why Are tRNAs Overproduced in the Absence of Maf1, a Negative Regulator of RNAP III, Not Fully Functional?","citation":"PLoS Genet 2015 Dec;11(12):e1005743","abstract":"","doi":"10.1371/journal.pgen.1005743","authors":"Boguta M","authors_abbrev":"Boguta M","pubmed_publication_date":"Dec 2015","pubmed_entrez_date":"2016-01-01","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-05-13 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31030285","title":"CoQ 10  production in Schizosaccharomyces pombe is increased by reduction of glucose levels or deletion of pka1.","citation":"Appl Microbiol Biotechnol 2019 Jun;103(12):4899-4915","abstract":"Coenzyme Q (CoQ) is an essential component of the electron transport system that produces ATP in nearly all living cells. CoQ 10  is a popular commercial food supplement around the world, and demand for efficient production of this molecule has increased in recent years. In this study, we explored CoQ 10  production in the fission yeast Schizosaccharomyces pombe. We found that CoQ 10  level was higher in stationary phase than in log phase, and that it increased when the cells were grown in a low concentration of glucose, in maltose, or in glycerol/ethanol medium. Because glucose signaling is mediated by cAMP, we evaluated the involvement of this pathway in CoQ biosynthesis. Loss of Pka1, the catalytic subunit of cAMP-dependent protein kinase, increased production of CoQ 10 , whereas loss of the regulatory subunit Cgs1 decreased production. Manipulation of other components of the cAMP-signaling pathway affected CoQ 10  production in a consistent manner. We also found that glycerol metabolism was controlled by the cAMP/PKA pathway. CoQ 10  production by the S. pombe ∆pka1 reached 0.98 mg/g dry cell weight in medium containing a non-fermentable carbon source [2% glycerol (w/v) and 1% ethanol (w/v) supplemented with 0.5% casamino acids (w/v)], twofold higher than the production in wild-type cells under normal growth conditions. These findings demonstrate that carbon source, growth phase, and the cAMP-signaling pathway are important factors in CoQ 10  production in S. pombe.","doi":"10.1007/s00253-019-09843-7","authors":"Nishida I, Yokomi K, Hosono K, Hayashi K, Matsuo Y, Kaino T, Kawamukai M","authors_abbrev":"Nishida I et al.","pubmed_publication_date":"Jun 2019","pubmed_entrez_date":"2019-04-29","publication_year":"2019","canto_session_key":"e69ef00f0c3516d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_first_approved_date":"2019-07-13 07:56:51","canto_approved_date":"2025-09-03 12:26:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-07-11 10:23:49","canto_added_date":"2019-04-30 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":49,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":10,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC8C9.03","SPCC162.10","SPAC23A1.06c","SPAC1D4.13","SPAC110.01","SPBC3H7.15","SPAC890.03","SPBC1D7.05","SPBC18H10.15","SPCC1753.02c","SPAC23H3.13c","SPAC1006.09","SPAC17G8.14c","SPAC644.06c","SPCC74.03c","SPBC106.10","SPBC336.14c","SPAC1834.08","SPAC22E12.14c","SPBP23A10.10","SPBC216.05","SPAC1687.12c","SPCC4G3.04c","SPCC1450.11c","SPAC16C9.07","SPAC13F5.03c","SPAC19G12.12","SPBC1861.09","SPBC6B1.02","SPAC1805.05","SPBP35G2.05c","SPAC1D4.06c","SPAC24B11.06c","SPBC8D2.19","SPBC19C7.03","SPAC6F12.02","SPBC12D12.04c","SPAC3C7.06c","SPAC9G1.02","SPBC2D10.18","SPAC2F3.15","SPBC16E9.13","SPBC106.01","SPCC162.05","SPBC119.07","SPBC725.06c"],"gene_count":46,"ltp_gene_count":40,"approved_date":"2019-07-13"},{"uniquename":"PMID:20823543","title":"Expression, purification and crystallization of Swi5 and the Swi5-Sfr1 complex from fission yeast.","citation":"Acta Crystallogr Sect F Struct Biol Cryst Commun 2010 Sep 01;66(Pt 9):1124-6","abstract":"The assembly of the presynaptic filament of recombinases represents the most important step in homologous recombination. The formation of the filament requires assistance from mediator proteins. Swi5 and Sfr1 have been identified as mediators in fission yeast and these proteins form a complex that stimulates strand exchange. Here, the expression, purification and crystallization of Swi5 and its complex with an N-terminally truncated form of Sfr1 (DeltaN180Sfr1) are presented. Analytical ultracentrifugation of the purified samples showed that Swi5 and the protein complex exist as tetramers and heterodimers in solution, respectively. Swi5 was crystallized in two forms belonging to space groups C2 and R3 and the crystals diffracted to 2.7 A resolution. Swi5-DeltaN180Sfr1 was crystallized in space group P2(1)2(1)2 and the crystals diffracted to 2.3 A resolution. The crystals of Swi5 and Swi5-DeltaN180Sfr1 are likely to contain one tetramer and two heterodimers in the asymmetric unit, respectively.","doi":"10.1107/S1744309110032239","authors":"Kuwabara N, Hashimoto H, Yamada N, Unzai S, Ikeguchi M, Sato M, Murayama Y, Iwasaki H, Shimizu T","authors_abbrev":"Kuwabara N et al.","pubmed_publication_date":"01 Sep 2010","pubmed_entrez_date":"2010-09-09","publication_year":"2010","canto_session_key":"7eab4b570ebddbdc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2024-06-26 19:37:32","canto_approved_date":"2024-06-26 19:37:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-06-26 19:37:13","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC28F2.07","SPBC409.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-06-26"},{"uniquename":"PMID:9118941","title":"Functional characterization of the fission yeast Start-specific transcription factor Res2.","citation":"EMBO J 1997 Mar 03;16(5):1023-34","abstract":"In the fission yeast Schizosaccharomyces pombe, transcriptional activation at Start is mediated by complexes that bind the MCB. Two such complexes have been identified; both contain the Cdc10 protein in partnership with either the Res1 or Res2 protein. Characterization of null mutants suggests that the Res1-Cdc10 complex predominantly functions in mitotic cells whereas the Res2-Cdc10 complex is required for meiosis and spore formation. Here we have characterized the functional domains of the Res2 protein. The N-terminus is both necessary and sufficient for DNA binding, whereas the C-terminus is the region involved in the interaction with the Cdc10 protein. The centrally located ankyrin repeats are dispensable for both functions. Res2 binds to DNA as a dimer. In addition, complexes containing both Res1 and Res2 can form and bind to DNA in vitro. Furthermore, the major MCB-specific complex detected in extracts from wild-type cells contains Res1 and Res2; the complex is lost when either gene is deleted and can be recognized by antibodies specific to both proteins. In order to understand the basis for the specific function of Res2 in meiosis, hybrids between Res1 and Res2 were constructed and their functions analysed. The results indicate an absolute requirement for the Res2 C-terminus for normal meiosis to occur whereas the origin of the DNA-binding region is irrelevant. The implications of these results for the regulation of the MCB-binding complexes will be discussed.","authors":"Zhu Y, Takeda T, Whitehall S, Peat N, Jones N","authors_abbrev":"Zhu Y et al.","pubmed_publication_date":"03 Mar 1997","pubmed_entrez_date":"1997-03-03","publication_year":"1997","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22F3.09c","SPBC725.16","SPBC336.12c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:27365210","title":"The fission yeast MTREC and EJC orthologs ensure the maturation of meiotic transcripts during meiosis.","citation":"RNA 2016 Sep;22(9):1349-59","abstract":"Meiosis is a highly regulated process by which genetic information is transmitted through sexual reproduction. It encompasses unique mechanisms that do not occur in vegetative cells, producing a distinct, well-regulated meiotic transcriptome. During vegetative growth, many meiotic genes are constitutively transcribed, but most of the resulting mRNAs are rapidly eliminated by the Mmi1-MTREC (Mtl1-Red1 core) complex. While Mmi1-MTREC targets premature meiotic RNAs for degradation by the nuclear 3'-5' exoribonuclease exosome during mitotic growth, its role in meiotic gene expression during meiosis is not known. Here, we report that Red5, an essential MTREC component, interacts with pFal1, an ortholog of eukaryotic translation initiation factor eIF4aIII in the fission yeast Schizosaccharomyces pombe In mammals, together with MAGO (Mnh1), Rnps1, and Y14, elF4AIII (pFal1) forms the core of the exon junction complex (EJC), which is essential for transcriptional surveillance and localization of mature mRNAs. In fission yeast, two EJC orthologs, pFal1 and Mnh1, are functionally connected with MTREC, specifically in the process of meiotic gene expression during meiosis. Although pFal1 interacts with Mnh1, Y14, and Rnps1, its association with Mnh1 is not disrupted upon loss of Y14 or Rnps1. Mutations of Red1, Red5, pFal1, or Mnh1 produce severe meiotic defects; the abundance of meiotic transcripts during meiosis decreases; and mRNA maturation processes such as splicing are impaired. Since studying meiosis in mammalian germline cells is difficult, our findings in fission yeast may help to define the general mechanisms involved in accurate meiotic gene expression in higher eukaryotes.","doi":"10.1261/rna.055608.115","authors":"Marayati BF, Hoskins V, Boger RW, Tucker JF, Fishman ES, Bray AS, Zhang K","authors_abbrev":"Marayati BF et al.","pubmed_publication_date":"Sep 2016","pubmed_entrez_date":"2016-07-02","publication_year":"2016","canto_session_key":"48ad18999497e29d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Bahjat Fadi Marayati","canto_first_approved_date":"2024-01-20 09:27:17","canto_approved_date":"2024-01-20 09:27:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-16 18:13:21","canto_added_date":"2016-07-03 00:16:07","annotation_curators":[{"name":"Bahjat Fadi Marayati","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":26,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27D7.13c","SPBC337.12","SPBC13G1.14c","SPAC1F5.10","SPBC32H8.11","SPBC29A10.14","SPBC16D10.07c","SPBC3B9.08c","SPBC902.05c","SPAC23A1.09","SPAC1006.03c"],"gene_count":11,"ltp_gene_count":6,"approved_date":"2024-01-20"},{"uniquename":"PMID:17550626","title":"Reconstruction of the kinetochore: a prelude to meiosis.","citation":"Cell Div 2007 Jun 06;2:17","abstract":"In eukaryotic organisms, chromosomes are spatially organized within the nucleus. Such nuclear architecture provides a physical framework for the genetic activities of chromosomes, and changes its functional organization as the cell moves through the phases of the cell cycle. The fission yeast Schizosaccharomyces pombe provides a striking example of nuclear reorganization during the transition from mitosis to meiosis. In this organism, centromeres remain clustered at the spindle-pole body (SPB; a centrosome-equivalent structure in fungi) during mitotic interphase. In contrast, during meiotic prophase, centromeres dissociate from the SPB and telomeres cluster to the SPB. Recent studies revealed that this repositioning of chromosomes is regulated by mating pheromone signaling. Some centromere proteins disappear from the centromere in response to mating pheromone, leading to dissociation of centromeres from the SPB. Interestingly, mating pheromone signaling is also required for monopolar orientation of the kinetochore which is crucial for proper segregation of sister chromatids during meiosis. When meiosis is induced in the absence of mating pheromone signaling, aberrant chromosome behaviors are observed: the centromere proteins remain at the centromere; the centromere remains associated with the SPB; and sister chromatids segregate precociously in the first meiotic division. These aberrant chromosome behaviors are all normalized by activating the mating pheromone signaling pathway. Thus, action of mating pheromone on the centromere is important for coherent behavior of chromosomes in meiosis. Here we discuss repositioning and reconstruction of the centromere during the transition from mitosis to meiosis, and highlight its significance for proper progression of meiosis.","authors":"Asakawa H, Haraguchi T, Hiraoka Y","authors_abbrev":"Asakawa H et al.","pubmed_publication_date":"06 Jun 2007","pubmed_entrez_date":"2007-06-07","publication_year":"2007","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15053869","title":"Homolog pairing in S. pombe: the ends are the means.","citation":"Mol Cell 2004 Mar 26;13(6):766-8","abstract":"The pairing of homologous chromosomes is a universal feature of meiosis and is important for the accurate segregation of chromosomes in the first of two meiotic divisions. In the March issue of Developmental Cell, report findings in fission yeast which point to telomere clustering and movement as being important determinants of homolog pairing.","authors":"Burgess SM","authors_abbrev":"Burgess SM","pubmed_publication_date":"26 Mar 2004","pubmed_entrez_date":"2004-04-01","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:25","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10523639","title":"The Rpb4 subunit of fission yeast Schizosaccharomyces pombe RNA polymerase II is essential for cell viability and similar in structure to the corresponding subunits of higher eukaryotes.","citation":"Mol Cell Biol 1999 Nov;19(11):7511-8","abstract":"Both the gene and the cDNA encoding the Rpb4 subunit of RNA polymerase II were cloned from the fission yeast Schizosaccharomyces pombe. The cDNA sequence indicates that Rpb4 consists of 135 amino acid residues with a molecular weight of 15,362. As in the case of the corresponding subunits from higher eukaryotes such as humans and the plant Arabidopsis thaliana, Rpb4 is smaller than RPB4 from the budding yeast Saccharomyces cerevisiae and lacks several segments, which are present in the S. cerevisiae RPB4 subunit, including the highly charged sequence in the central portion. The RPB4 subunit of S. cerevisiae is not essential for normal cell growth but is required for cell viability under stress conditions. In contrast, S. pombe Rpb4 was found to be essential even under normal growth conditions. The fraction of RNA polymerase II containing RPB4 in exponentially growing cells of S. cerevisiae is about 20%, but S. pombe RNA polymerase II contains the stoichiometric amount of Rpb4 even at the exponential growth phase. In contrast to the RPB4 homologues from higher eukaryotes, however, S. pombe Rpb4 formed stable hybrid heterodimers with S. cerevisiae RPB7, suggesting that S. pombe Rpb4 is similar, in its structure and essential role in cell viability, to the corresponding subunits from higher eukaryotes. However, S. pombe Rpb4 is closer in certain molecular functions to S. cerevisiae RPB4 than the eukaryotic RPB4 homologues.","authors":"Sakurai H, Mitsuzawa H, Kimura M, Ishihama A","authors_abbrev":"Sakurai H et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-10-19","publication_year":"1999","canto_session_key":"64b9b811ffb4d361","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2018-07-04 07:21:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-30 11:44:50","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC337.14","SPAPYUG7.04c","SPBC14C8.12","SPCC1442.10c","SPACUNK4.06c","SPAC3A12.07"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2014-06-30"},{"uniquename":"Pfam:PF06991","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:7032","SPAC1782.03"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37939109","title":"Spt5 C-terminal repeat domain phosphorylation and length negatively regulate heterochromatin through distinct mechanisms.","citation":"PLoS Genet 2023 Nov;19(11):e1010492","abstract":"Heterochromatin is a condensed chromatin structure that represses transcription of repetitive DNA elements and developmental genes, and is required for genome stability. Paradoxically, transcription of heterochromatic sequences is required for establishment of heterochromatin in diverse eukaryotic species. As such, components of the transcriptional machinery can play important roles in establishing heterochromatin. How these factors coordinate with heterochromatin proteins at nascent heterochromatic transcripts remains poorly understood. In the model eukaryote Schizosaccharomyces pombe (S. pombe), heterochromatin nucleation can be coupled to processing of nascent transcripts by the RNA interference (RNAi) pathway, or to other post-transcriptional mechanisms that are RNAi-independent. Here we show that the RNA polymerase II processivity factor Spt5 negatively regulates heterochromatin in S. pombe through its C-terminal domain (CTD). The Spt5 CTD is analogous to the CTD of the RNA polymerase II large subunit, and is comprised of multiple repeats of an amino acid motif that is phosphorylated by Cdk9. We provide evidence that genetic ablation of Spt5 CTD phosphorylation results in aberrant RNAi-dependent nucleation of heterochromatin at an ectopic location, as well as inappropriate spread of heterochromatin proximal to centromeres. In contrast, truncation of Spt5 CTD repeat number enhanced RNAi-independent heterochromatin formation and bypassed the requirement for RNAi. We relate these phenotypes to the known Spt5 CTD-binding factor Prf1/Rtf1. This separation of function argues that Spt5 CTD phosphorylation and CTD length restrict heterochromatin through unique mechanisms. More broadly, our findings argue that length and phosphorylation of the Spt5 CTD repeat array have distinct regulatory effects on transcription.","doi":"10.1371/journal.pgen.1010492","authors":"MacKinnon S, Pagé V, Chen JJ, Shariat-Panahi A, Martin RD, Hébert TE, Tanny JC","authors_abbrev":"MacKinnon S et al.","pubmed_publication_date":"Nov 2023","pubmed_entrez_date":"2023-11-08","publication_year":"2023","canto_session_key":"fedfea479083201f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-11-09 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8785278","title":"Calcium and cell cycle progression: possible effects of external perturbations on cell proliferation.","citation":"Biophys J 1996 Mar;70(3):1198-213","abstract":"Exit from the phase of cellular division appears to be driven by a calcium signal that triggers a cascade of events leading to the completion of mitosis. Here we propose a model that relates the dynamics of cytosolic calcium to progression through mitosis, G1 and G2 phases of the cell cycle. To this end, the assumption has been made that the transient rise ir cytosolic calcium concentration during mitosis is induced by inositol(1,4,5)triphosphate (IP3), which in turn is released at high levels of mitosis-promoting factor (MPF). On this basis, a system of ordinary differential equations is proposed to simulate the evolution of ten cell-cycle-specific molecular species, including cyclins A and B, MPF, IP3, Ca2+, the CaMKII holoenzyme, and the ubiquitination complex. The influence on the cell proliferation capacity exerted by external perturbations, like calcium microinjections, depletion of intracellular calcium stores, electromagnetic fields, or stimulation/inhibition of different calcium currents through the plasma membrane, can be studied by appropriate modulation of the parameters involved in the signal transduction pathway.","authors":"Baran I","authors_abbrev":"Baran I","pubmed_publication_date":"Mar 1996","pubmed_entrez_date":"1996-03-01","publication_year":"1996","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25728061","title":"Dynamic transition of transcription and chromatin landscape during fission yeast adaptation to glucose starvation.","citation":"Genes Cells 2015 May;20(5):392-407","abstract":"Shortage of glucose, the primary energy source for all organisms, is one of the most critical stresses influencing cell viability. Glucose starvation promptly induces changes in mRNA and noncoding RNA (ncRNA) transcription. We previously reported that glucose starvation induces long ncRNA (lncRNA) transcription in the 5' segment of a fission yeast gluconeogenesis gene (fbp1+), which leads to stepwise chromatin alteration around the fbp1+ promoter and to subsequent robust gene activation. Here, we analyzed genomewide transcription by strand-specific RNA sequencing, together with chromatin landscape by immunoprecipitation sequencing (ChIP-seq). Clustering analysis showed that distinct mRNAs and ncRNAs are induced at the early, middle and later stages of cellular response to glucose starvation. The starvation-induced transcription depends substantially on the stress-responsive transcription factor Atf1. Using a new computer program that examines dynamic changes in expression patterns, we identified ncRNAs with similar behavior to the fbp1+ lncRNA. We confirmed that there are continuous lncRNAs associated with local reduction of histone density. Overlapping with the regions for transcription of these lncRNAs, antisense RNAs are antagonistically transcribed under glucose-rich conditions. These results suggest that Atf1-dependent integrated networks of mRNA and lncRNA govern drastic changes in cell physiology in response to glucose starvation.","doi":"10.1111/gtc.12229","authors":"Oda A, Takemata N, Hirata Y, Miyoshi T, Suzuki Y, Sugano S, Ohta K","authors_abbrev":"Oda A et al.","pubmed_publication_date":"May 2015","pubmed_entrez_date":"2015-03-03","publication_year":"2015","canto_session_key":"e415e099b05ffa29","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-04 01:15:39","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31473486","title":"Identification of putative G-quadruplex DNA structures in S. pombe genome by quantitative PCR stop assay.","citation":"DNA Repair (Amst) 2019 Oct;82:102678","abstract":"In order to understand in which biological processes the four-stranded G-quadruplex (G4) DNA structures play a role, it is important to determine which predicted regions can actually adopt a G4 structure. Here, to identify DNA regions in Schizosaccharomyces pombe that fold into G4 structures, we first optimized a quantitative PCR (qPCR) assay using the G4 stabilizer, PhenDC3. We call this method the qPCR stop assay, and used it to screen for G4 structures in genomic DNA. The presence of G4 stabilizers inhibited DNA amplification in 14/15 unexplored genomic regions in S. pombe that encompassed predicted G4 structures, suggesting that at these sites the stabilized G4 structure formed an obstacle for the DNA polymerase. Furthermore, the formation of G4 structures was confirmed by complementary in vitro assays. In vivo, the S. pombe G4 unwinder Pif1 helicase, Pfh1, was associated with tested G4 sites, suggesting that the G4 structures also formed in vivo. Thus, we propose that the confirmed G4 structures in S. pombe form an obstacle for replication in vivo, and that the qPCR stop assay is a method that can be used to identify G4 structures. Finally, we suggest that the qPCR stop assay can also be used for identifying G4 structures in other organisms, as well as being adapted to screen for novel G4 stabilizers.","doi":"10.1016/j.dnarep.2019.102678","authors":"Jamroskovic J, Obi I, Movahedi A, Chand K, Chorell E, Sabouri N","authors_abbrev":"Jamroskovic J et al.","pubmed_publication_date":"Oct 2019","pubmed_entrez_date":"2019-09-02","publication_year":"2019","canto_triage_status":"Browser datasets, to host","canto_curator_role":"PomBase","canto_added_date":"2019-09-03 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8553696","title":"Schizosaccharomyces pombe RNase MRP RNA is homologous to metazoan RNase MRP RNAs and may provide clues to interrelationships between RNase MRP and RNase P.","citation":"Yeast 1995 Oct;11(13):1249-64","abstract":"RNase MRP and RNase P ribonucleoproteins are structurally and functionally similar across a large evolutionary distance. To better characterize possible complex interrelationships between these two enzymes, we have employed the fission yeast Schizosaccharomyces pombe. Unlike Saccharomyces cerevisiae, S. pombe is believed to harbour only one genetic locus for the RNA component of RNase P and does not contain a known mitochondrially encoded RNase P RNA. We have identified the single nuclear gene for the RNA component of RNase MRP in S. pombe, mrp-1, by homology to vertebrate RNase MRP RNAs. The mrp-1 gene encodes an RNA of maximum mature length 400 nucleotides that shares a high degree of identity, in evolutionarily conserved regions, to both vertebrate RNase MRP RNAs and S. pombe RNase P RNA. Disruption of mrp-1 in the diploid strain SP826 and sporulation of tetrads resulted in a 2 dead:2 viable segregation, consistent with the gene being essential. Lethality is rescued by a plasmid-borne copy of mrp-1. Partially purified ribonucleoprotein RNase MRP activity correctly and efficiently processed all previously characterized heterologous mitochondrial RNA substrates. The compact mitochondrial genome of S. pombe contains sequence elements with > 50% identity to mammalian D-loop CSBI and CSBII elements. The identification of mrp-1 in S. pombe should facilitate not only comparisons between the related ribonucleoproteins RNase MRP and RNase P, but should also provide an opportunity for genetic elucidation of RNase MRP function in a situation reflective of the animal kingdom.","authors":"Paluh JL, Clayton DA","authors_abbrev":"Paluh JL et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_session_key":"0cb3f8833f205812","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-11 11:04:56","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-11 11:04:50","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPNCRNA.82","YNCN0013W"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-11"},{"uniquename":"PMID:7430074","title":"Induction of arginase and ornithine transaminase in the fission yeast Schizosaccharomyces pombe.","citation":"J Bacteriol 1980 Nov;144(2):836-9","abstract":"The induction of arginase and ornithine transaminase in the fission yeast Schizosaccharomyces pombe requires the absence of ammonia and the presence of the inducer arginine. It seems that immediate arginase degradation is initiated by starved cells or ones from which arginine has been removed.","authors":"Benítez T, Farrar L","authors_abbrev":"Benítez T et al.","pubmed_publication_date":"Nov 1980","pubmed_entrez_date":"1980-11-01","publication_year":"1980","canto_session_key":"efa5b22593f09d4a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-08-04 10:10:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-04 10:10:22","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2014-08-04"},{"uniquename":"PMID:7929575","title":"Dynamics of chromosome organization and pairing during meiotic prophase in fission yeast.","citation":"J Cell Biol 1994 Oct;127(2):273-85","abstract":"Interactions between homologous chromosomes (pairing, recombination) are of central importance for meiosis. We studied entire chromosomes and defined chromosomal subregions in synchronous meiotic cultures of Schizosaccharomyces pombe by fluorescence in situ hybridization. Probes of different complexity were applied to spread nuclei, to delineate whole chromosomes, to visualize repeated sequences of centromeres, telomeres, and ribosomal DNA, and to study unique sequences of different chromosomal regions. In diploid nuclei, homologous chromosomes share a joint territory even before entry into meiosis. The centromeres of all chromosomes are clustered in vegetative and meiotic prophase cells, whereas the telomeres cluster near the nucleolus early in meiosis and maintain this configuration throughout meiotic prophase. Telomeres and centromeres appear to play crucial roles for chromosome organization and pairing, both in vegetative cells and during meiosis. Homologous pairing of unique sequences shows regional differences and is most frequent near centromeres and telomeres. Multiple homologous interactions are formed independently of each other. Pairing increases during meiosis, but not all chromosomal regions become closely paired in every meiosis. There is no detectable axial compaction of chromosomes in meiotic prophase. S. pombe does not form mature synaptonemal complexes, but axial element-like structures (linear elements), which were analyzed in parallel. Their appearance coincides with pairing of interstitial chromosomal regions. Axial elements may define minimal structures required for efficient pairing and recombination of meiotic chromosomes.","authors":"Scherthan H, Bähler J, Kohli J","authors_abbrev":"Scherthan H et al.","pubmed_publication_date":"Oct 1994","pubmed_entrez_date":"1994-10-01","publication_year":"1994","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38913087","title":"Mutational analyses of the interacting domains of Schizosaccharomyces pombe Byr2 with 14-3-3s.","citation":"Curr Genet 2024 Jun 24;70(1):8","abstract":"The Byr2 kinase of fission yeast Schizosaccharomyces pombe is recruited to the membrane with the assistance of Ras1. Byr2 is also negatively regulated by 14-3-3 proteins encoded by rad24 and rad25. We conducted domain and mutational analysis of Byr2 to determine which region is critical for its binding to 14-3-3 proteins. Rad24 and Rad25 bound to both the Ras interaction domain in the N-terminus and to the C-terminal catalytic domain of Byr2. When amino acid residues S87 and T94 of the Ras-interacting domain of Byr2 were mutated to alanine, Rad24 could no longer bind to Byr2. S402, S566, S650, and S654 mutations in the C-terminal domain of Byr2 also abolished its interaction with Rad24 and Rad25. More than three mutations in the C-terminal domain were required to abolish completely its interaction with 14-3-3 protein, suggesting that multiple residues are involved in this interaction. Expression of the N-terminal domain of Byr2 in wild-type cells lowered the mating ratio, because it likely blocked the interaction of Byr2 with Ste4 and Ras1, whereas expression of the catalytic domain of Byr2 increased the mating ratio as a result of freeing from intramolecular regulation by the N-terminal domain of Byr2. The S87A and T94A mutations of Byr2 increased the mating ratio and attenuated inhibition of Byr2 by Rad24; therefore, these two amino acids are critical for its regulation by Rad24. S566 of Byr2 is critical for activity of Byr2 but not for its interaction with 14-3-3 proteins. In this study, we show that 14-3-3 proteins interact with two separate domains in Byr2 as negative regulators.","doi":"10.1007/s00294-024-01293-7","authors":"Kobayashi-Ooka Y, Ozoe F, Kawamukai M","authors_abbrev":"Kobayashi-Ooka Y et al.","pubmed_publication_date":"24 Jun 2024","pubmed_entrez_date":"2024-06-24","publication_year":"2024","canto_session_key":"2b8cb5911bb6a83f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Makoto Kawamukai","canto_first_approved_date":"2024-08-23 12:53:12","canto_approved_date":"2024-09-24 09:46:19","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2024-08-23 08:16:19","canto_added_date":"2024-06-24 23:25:05","annotation_curators":[{"name":"Makoto Kawamukai","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":70,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1D7.05","SPAC17A2.13c","SPAC8E11.02c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2024-08-23"},{"uniquename":"PMID:11459187","title":"The 5' terminal region of the Schizosaccharomyces pombe mes1 mRNA is crucial for its meiosis-specific splicing.","citation":"Mol Genet Genomics 2001 Jun;265(4):673-82","abstract":"The mes1+ gene of Schizosaccharomyces pombe is required for the second meiotic division. The single 75-nt intron in mes1 is spliced out only in meiotic cells. Here we report a cis-acting element which is responsible for meiosis-specific splicing. Both 5' and 3' splice sites of the mes1 intron deviate from the consensus sequence. Point mutations which altered these sites so that they conformed to the consensus, however, did not affect the splicing pattern of mes1. Neither replacement of the mes1 intron with the constitutively spliced intron of the nda3 gene, nor replacement of the 3' exon with E. coli lacZ changed the splicing pattern. In contrast, deletion of the 5' terminal 125 nt from the 5' exon derepressed splicing in vegetative cells, implying that this 5' terminal sequence, named SRE (mes1 splicing repression element), inhibits splicing of the downstream intron. A potential stem-loop structure in the SRE is predicted. Disruption of this stem structure by mutation abolished the repression of mes1 splicing in vegetative cells. Overexpression of the SRE sequence on a multicopy plasmid also relieved the repression of splicing of the authentic mes1 transcripts. These results suggest that as yet unknown trans-acting factors inhibit splicing of the mes1 transcript in vegetative cells by interacting with the cis-element SRE.","authors":"Shimoseki M, Shimoda C","authors_abbrev":"Shimoseki M et al.","pubmed_publication_date":"Jun 2001","pubmed_entrez_date":"2001-07-19","publication_year":"2001","canto_session_key":"fcc880c3678cd8c4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC5D6.08c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:10438489","title":"Purification, molecular cloning, and catalytic activity of Schizosaccharomyces pombe pyridoxal reductase. A possible additional family in the aldo-keto reductase superfamily.","citation":"J Biol Chem 1999 Aug 13;274(33):23185-90","abstract":"Pyridoxal reductase (PL reductase), which catalyzes reduction of PL by NADPH to form pyridoxine and NADP(+), was purified from Schizosaccharomyces pombe. The purified enzyme was very unstable but was stabilized by low concentrations of various detergents such as Tween 40. The enzyme was a monomeric protein with the native molecular weight of 41,000 +/- 1,600. The enzyme showed a single absorption peak at 280 nm (E(1%) = 10.0). PL and 2-nitrobenzaldehyde were excellent substrates, and no measurable activity was observed with short chain aliphatic aldehydes; substrate specificity of PL reductase was obviously different from those of yeast aldo-keto reductases (AKRs) so far purified. The peptide sequences of PL reductase were identical with those in a hypothetical 333-amino acid protein from S. pombe (the DDBJ/EMBL/GenBank(TM) accession number D89205). The gene corresponding to this protein was expressed in Escherichia coli, and the purified protein was found to have PL reductase activity. The recombinant PL reductase showed the same properties as those of native PL reductase. PL reductase showed only low sequence identities with members of AKR superfamily established to date; it shows the highest identity (18.5%) with human Shaker-related voltage-gated K(+) channel beta2 subunit. The elements of secondary structure of PL reductase, however, distributed similarly to those demonstrated in the three-dimensional structure of human aldose reductase except that loop A region is lost, and loop B region is extended. Amino acid residues involved in substrate binding or catalysis are also conserved. Conservation of these features, together with the major modifications, establish PL reductase as the first member of a new AKR family, AKR8.","authors":"Nakano M, Morita T, Yamamoto T, Sano H, Ashiuchi M, Masui R, Kuramitsu S, Yagi T","authors_abbrev":"Nakano M et al.","pubmed_publication_date":"13 Aug 1999","pubmed_entrez_date":"1999-08-07","publication_year":"1999","canto_session_key":"e5eec519ae02eee2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-06-30 10:11:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-06-30 10:11:04","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC9E9.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-30"},{"uniquename":"PMID:15958184","title":"A coupled fluorescent assay for histone methyltransferases.","citation":"Anal Biochem 2005 Jul 01;342(1):86-92","abstract":"Histone methyltransferases (HMTs) catalyze the S-adenosylmethionine (AdoMet)-dependent methylation of lysines and arginines in the nucleosomal core histones H3 and H4 and the linker histone H1b. Methylation of these residues regulates either transcriptional activation or silencing, depending on the residue modified and its degree of methylation. Despite an intense interest in elucidating the functions of HMTs in transcriptional regulation, these enzymes have remained challenging to quantitatively assay. To characterize the substrate specificity of HMTs, we have developed a coupled-fluorescence-based assay for AdoMet-dependent methyltransferases. This assay utilizes S-adenosylhomocysteine hydrolase (SAHH) to hydrolyze the methyltransfer product S-adenosylhomocysteine (AdoHcy) to homocysteine (Hcy) and adenosine (Ado). The Hcy concentration is then determined through conjugation of its free sulfhydryl moiety to a thiol-sensitive fluorophore. Using this assay, we have determined the kinetic parameters for the methylation of a synthetic histone H3 peptide (corresponding to residues 1-15 of the native protein) by Schizosaccharomyces pombe CLR4, an H3 Lys-9-specific methyltransferase. The fluorescent SAHH-coupled assay allows rapid and facile determination of HMT kinetics and can be adapted to measure the enzymatic activity of a wide variety of AdoMet-dependent methyltransferases.","authors":"Collazo E, Couture JF, Bulfer S, Trievel RC","authors_abbrev":"Collazo E et al.","pubmed_publication_date":"01 Jul 2005","pubmed_entrez_date":"2005-06-17","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26030876","title":"Structure of the Atg101-Atg13 complex reveals essential roles of Atg101 in autophagy initiation.","citation":"Nat Struct Mol Biol 2015 Jul;22(7):572-80","abstract":"Atg101 is an essential component of the autophagy-initiating ULK complex in higher eukaryotes, but it is absent from the functionally equivalent Atg1 complex in budding yeast. Here, we report the crystal structure of the fission yeast Atg101-Atg13 complex. Atg101 has a Hop1, Rev7 and Mad2 (HORMA) architecture similar to that of Atg13. Mad2 HORMA has two distinct conformations (O-Mad2 and C-Mad2), and, intriguingly, Atg101 resembles O-Mad2 rather than the C-Mad2-like Atg13. Atg13 HORMA from higher eukaryotes possesses an inherently unstable fold, which is stabilized by Atg101 via interactions analogous to those between O-Mad2 and C-Mad2. Mutational studies revealed that Atg101 is responsible for recruiting downstream factors to the autophagosome-formation site in mammals via a newly identified WF finger. These data define the molecular functions of Atg101, providing a basis for elucidating the molecular mechanisms of mammalian autophagy initiation by the ULK complex.","doi":"10.1038/nsmb.3036","authors":"Suzuki H, Kaizuka T, Mizushima N, Noda NN","authors_abbrev":"Suzuki H et al.","pubmed_publication_date":"Jul 2015","pubmed_entrez_date":"2015-06-02","publication_year":"2015","canto_session_key":"a3f71315809a4d83","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-08-23 08:24:03","canto_approved_date":"2023-07-05 11:31:16","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2019-08-13 12:26:48","canto_added_date":"2015-06-03 00:19:13","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4F10.07c","SPAC25H1.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2019-08-23","pdb_entries":[{"pdb_id":"4yk8","gene_chains":[{"gene_uniquename":"SPAC25H1.03","chain":"A","position":"1-184"},{"gene_uniquename":"SPAC4F10.07c","chain":"B","position":"32-269"}],"title":"Crystal structure of the Atg101-Atg13 complex from fission yeast","entry_authors":"Suzuki H,Noda NN","entry_authors_abbrev":"Suzuki H et al.","reference_uniquename":"PMID:26030876","experimental_method":"X-ray","resolution":"3.0"}]},{"uniquename":"PMID:9748434","title":"Isolation and characterization of high-osmolarity-sensitive mutants of fission yeast.","citation":"J Bacteriol 1998 Oct;180(19):5038-43","abstract":"For the fission yeast Schizosaccharomyces pombe, adaptation to high-osmolarity medium is mediated by a mitogen-activated protein (MAP) kinase cascade, involving the Wis1 MAP kinase kinase and the Sty1 MAP kinase. The MAP kinase pathway transduces an osmotic signal and accordingly regulates the expression of the downstream target gene (gpd1(+)) that encodes NADH-dependent glycerol-3-phosphate dehydrogenase, in order to adaptively accumulate glycerol inside the cells as an osmoprotectant. We previously characterized a set of high-osmolarity-sensitive S. pombe mutants, including wis1, sty1, and gpd1. In this study, we attempted to further isolate novel osmolarity-sensitive mutants. For some of the mutants isolated, profiles of glycerol production in response to the osmolarity of the growth medium were indistinguishable from that of the wild-type cells, suggesting that they are novel types. They were classified into three distinct types genetically and, thus, were designated hos1, hos2, and hos3 (high osmolarity sensitive) mutants. One of them, the hos1 mutant, was characterized in detail. The hos1 mutant was demonstrated to have a mutational lesion in the known ryh1(+) gene, which encodes a small GTP-binding protein. Disruption of the ryh1(+) gene results not only in osmosensitivity but also in temperature sensitivity for growth. It was also found that the delta ryh1 mutant is severely sterile. These results are discussed with special reference to the osmoadaptation of S. pombe.","authors":"Aiba H, Kawaura R, Yamamoto E, Yamada H, Takegawa K, Mizuno T","authors_abbrev":"Aiba H et al.","pubmed_publication_date":"Oct 1998","pubmed_entrez_date":"1998-09-28","publication_year":"1998","canto_session_key":"8113a880cb66e90a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-09-10 16:30:50","canto_approved_date":"2026-01-31 15:30:58","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-10 16:30:44","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4C5.02c","SPAC1805.07c","SPCC417.02","SPBC215.05"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2014-09-10"},{"uniquename":"PMID:41891373","title":"Curcumin delays cytokinesis in fission yeast by targeting the septin ring.","citation":"J Cell Sci 2026 Apr 15;139(8)","abstract":"Curcumin is the active compound of one of the most widely used spices (turmeric) in the world and it is thought to also possess anti-fungal and other biological activities. However, the molecular and cellular targets of curcumin remain unknown. Here, we undertook a novel imaging-based approach to determine the intracellular distribution of curcumin using the model organism fission yeast Schizosaccharomyces pombe by taking advantage of the intrinsic fluorescence of curcumin. Live fluorescence microscopy revealed for the first time that curcumin, at a concentration of just 1 μM, formed a narrow circumferential ring around the equatorial plane of dividing cells within minutes after being added to the yeast culture. The intensity of this ring increased proportionally to the concentration of curcumin and gradually over time. The curcumin ring colocalized both spatially and temporally with septin ring and the exocyst complex at the equatorial plane during cytokinesis. Deletion of one of the septin genes (spn4) reduced the frequency of curcumin ring formation by 74%. Micromolar concentrations of curcumin slowed down the contractile ring constriction by up to 49% in a dosage-dependent manner. Besides fission yeast, curcumin similarly targets the division plane of two other yeasts, Saccharomyces cerevisiae and Candida albicans. Thus, curcumin, originating from plants, targets the septin cytoskeleton to delay yeast cytokinesis, suggesting its potential anti-fungal activity and use as a fluorescence probe for yeast septins.","doi":"10.1242/jcs.264321","authors":"Kulasegaram V, Dias DA, Okorokova-Façanha A, Chen Q","authors_abbrev":"Kulasegaram V et al.","pubmed_publication_date":"15 Apr 2026","pubmed_entrez_date":"2026-03-27","publication_year":"2026","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2026-03-28 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8750242","title":"Molecular cloning and sequencing of the hcs gene, which encodes 3-hydroxy-3-methylglutaryl coenzyme A synthase of Schizosaccharomyces pombe.","citation":"Yeast 1995 Dec;11(15):1533-7","abstract":"We have cloned and sequenced the hcs gene, which is thought to encode a 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase consisting of 447 amino acids, from the fission yeast Schizosaccharomyces pombe. The predicted amino acid sequence of the hcs product of S. pombe has homology with the HMG-CoA synthase of rat (47.8%), chicken (49.2%), hamster (47.1%) and human cells (46.9%). One of the hcs genes was replaced with a marker gene in the diploid cell. No viable hcs-disrupted haploid was isolated after tetrad dissection, suggesting that the hcs gene is essential for growth. However the hcs-defective mutant could be grown on a medium containing 5 mg/ml mevalonate. These results strongly support that the hcs gene encodes HMG-CoA synthase and S. pombe contains a single copy of the hcs gene.","authors":"Katayama S, Adachi N, Takao K, Nakagawa T, Matsuda H, Kawamukai M","authors_abbrev":"Katayama S et al.","pubmed_publication_date":"Dec 1995","pubmed_entrez_date":"1995-12-01","publication_year":"1995","canto_session_key":"40f6fe5d97c8f8f5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2014-08-01 06:30:24","canto_approved_date":"2026-06-13 13:42:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-31 16:27:04","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC4F8.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-01"},{"uniquename":"PMID:16561035","title":"A Remarkable Fission Yeast, Schizosaccharomyces versatilis NOV. SP.","citation":"J Bacteriol 1945 Nov;50(5):597-607","abstract":"","authors":"Wickerham LJ, Duprat E","authors_abbrev":"Wickerham LJ et al.","pubmed_publication_date":"Nov 1945","pubmed_entrez_date":"1945-11-01","publication_year":"1945","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8264618","title":"Concerted action of RAS and G proteins in the sexual response pathways of Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1994 Jan;14(1):50-8","abstract":"We have shown that the expression of mam2, the gene encoding the Schizosaccharomyces pombe P-factor pheromone receptor, is dependent upon components of the pheromone signal transduction pathway, including Ras1, Gpa1, Byr1 and Byr2, each of which is required for both conjugation and sporulation. Studies of the expression of mam2 in mutant S. pombe cells confirm previous conclusions, based on the ability of cells to sporulate, that the Byr1 protein kinase acts downstream of the Byr2 protein kinase and that both act downstream of Ras1, the S. pombe RAS homolog, and Gpa1, the G alpha component that mediates the occupancy of the mam2 receptor. In addition, our present studies show that Ras1 and Gpa1 each act downstream from the other and hence act in concert. The Spk1 kinase, which is required for conjugation and sporulation and which is a structural and functional homolog of the vertebrate MAP kinases, is not required for mam2 expression.","authors":"Xu HP, White M, Marcus S, Wigler M","authors_abbrev":"Xu HP et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_session_key":"68eabeff9a77bf16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2020-01-21 17:19:06","canto_approved_date":"2020-01-21 17:19:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2020-01-21 17:18:59","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":34,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32C12.02","SPAC13D6.02c","SPAC1D4.13","SPCC1442.01","SPBC1D7.05","SPBC24C6.06","SPAC11H11.04","SPAC17H9.09c","SPAC31G5.09c"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2020-01-21"},{"uniquename":"PMID:12218190","title":"Cytoplasmic poly(A) polymerases mediate cellular responses to S phase arrest.","citation":"Proc Natl Acad Sci U S A 2002 Sep 17;99(19):12079-84","abstract":"The S-M checkpoint delays mitosis until DNA replication is complete; cells defective in this checkpoint lose viability when DNA replication is inhibited. This inviability can be suppressed in fission yeast by overexpression of Cid1 or the related protein Cid13. Fission yeast contain six cid1/cid13-like genes, whereas budding yeast has just two, TRF4 and TRF5. Trf4 and Trf5 were recently reported to comprise an essential DNA polymerase activity required for the establishment of sister chromatid cohesion. In contrast, we find that Cid1 is not a DNA polymerase but instead uses RNA substrates and has poly(A) polymerase activity. Unlike the previously characterized yeast poly(A) polymerase, which is a nuclear enzyme, Cid1 and Cid13 are constitutively cytoplasmic. Cid1 has a degree of substrate specificity in vitro, consistent with the notion that it targets a subset of cytoplasmic mRNAs for polyadenylation in vivo, hence increasing their stability and/or efficiency of translation. Preferred Cid1 targets presumably include mRNAs encoding components of the S-M checkpoint, whereas Cid13 targets are likely to be involved in dNTP metabolism. Cytoplasmic polyadenylation is known to be an important regulatory mechanism during early development in animals. Our findings in yeast suggest that this level of gene regulation is of more general significance in eukaryotic cells.","authors":"Read RL, Martinho RG, Wang SW, Carr AM, Norbury CJ","authors_abbrev":"Read RL et al.","pubmed_publication_date":"17 Sep 2002","pubmed_entrez_date":"2002-09-10","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC821.04c","SPAC19D5.03","SPBC216.05"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PB_REF:0000008","title":"Distant orthologs supported by Pfam-N","abstract":"Ortholog predicted using Pfam-N (PMID: 35190689), and manually reviewed and manually reviewed for context (length, functional attributes and other features). See DOI: 10.1007/4735_97 for a description of our manual review process.","authors":"PomBase curators","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.07c","YAL055W","YOR350C","SPAC15A10.17","SPAC57A7.15c","YOL044W","SPCC16C4.04","HGNC:7686","SPAP27G11.08c","YBR230C","SPAC607.02c","SPAC2C4.10c","HGNC:33451","SPAC1805.10","SPCC1393.11","SPBC19G7.18c","HGNC:21691","HGNC:28569","SPBC16A3.03c","SPBC11C11.06c","HGNC:26119","HGNC:23098","YBR131W"],"gene_count":12,"ltp_gene_count":0},{"uniquename":"PMID:11248251","title":"Involvement of mitochondrial ferredoxin and Cox15p in hydroxylation of heme O.","citation":"FEBS Lett 2001 Mar 09;492(1-2):133-8","abstract":"Cox15p is essential for the biogenesis of cytochrome oxidase [Glerum et al., J. Biol. Chem. 272 (1997) 19088-19094]. We show here that cox15 mutants are blocked in heme A but not heme O biosynthesis. In Schizosaccharomyces pombe COX15 is fused to YAH1, the yeast gene for mitochondrial ferredoxin (adrenodoxin). A fusion of Cox15p and Yah1p in Saccharomyces cerevisiae rescued both cox15 and yah1 null mutants. This suggests that Yah1p functions in concert with Cox15p. We propose that Cox15p functions together with Yah1p and its putative reductase (Arh1p) in the hydroxylation of heme O.","authors":"Barros MH, Carlson CG, Glerum DM, Tzagoloff A","authors_abbrev":"Barros MH et al.","pubmed_publication_date":"09 Mar 2001","pubmed_entrez_date":"2001-03-15","publication_year":"2001","canto_session_key":"44e84d2e1bfe62fa","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-12-30 14:34:07","canto_approved_date":"2025-02-17 15:46:24","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-11-29 17:08:12","canto_added_date":"2012-02-24 05:51:59","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":9,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22E12.10c","SPBC365.02c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2023-12-30"},{"uniquename":"EMBL:AY091590","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12606555","title":"Functional characterization and localization of acetyl-CoA hydrolase, Ach1p, in Saccharomyces cerevisiae.","citation":"J Biol Chem 2003 May 09;278(19):17203-9","abstract":"Acetyl-CoA hydrolase (Ach1p), catalyzing the hydrolysis of acetyl-CoA, is presumably involved in regulating intracellular acetyl-CoA or CoASH pools; however, its intracellular functions and distribution remain to be established. Using site-directed mutagenesis analysis, we demonstrated that the enzymatic activity of Ach1p is dependent upon its putative acetyl-CoA binding sites. The ach1 mutant causes a growth defect in acetate but not in other non-fermentable carbon sources, suggesting that Ach1p is not involved in mitochondrial biogenesis. Overexpression of Ach1p, but not constructs containing acetyl-CoA binding site mutations, in ach1-1 complemented the defect of acetate utilization. By subcellular fractionation, most of the Ach1p in yeast was distributed with mitochondria and little Ach1p in the cytoplasm. By immunofluorescence microscopy, we show that Ach1p and acetyl-CoA binding site-mutated constructs, but not its N-terminal deleted construct, are localized in mitochondria. Moreover, the onset of pseudohyphal development in homozygote ach1-1 diploids was abolished. We infer that Ach1p may be involved in a novel acetyl-CoA biogenesis and/or acetate utilization in mitochondria and thereby indirectly affect pseudohyphal development in yeast.","authors":"Buu LM, Chen YC, Lee FJ","authors_abbrev":"Buu LM et al.","pubmed_publication_date":"09 May 2003","pubmed_entrez_date":"2003-02-28","publication_year":"2003","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.09c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:19815179","title":"Role of spindle asymmetry in cellular dynamics.","citation":"Int Rev Cell Mol Biol 2009;278:149-213","abstract":"The mitotic spindle is mostly perceived as a symmetric structure. However, in many cell divisions, the two poles of the spindle organize asters with different dynamics, associate with different biomolecules or subcellular domains, and perform different functions. In this chapter, we describe some of the most prominent examples of spindle asymmetry. These are encountered during cell-cycle progression in budding and fission yeast and during asymmetric cell divisions of stem cells and embryos. We analyze the molecular mechanisms that lead to generation of spindle asymmetry and discuss the importance of spindle-pole differentiation for the correct outcome of cell division.","doi":"10.1016/S1937-6448(09)78004-9","authors":"Barral Y, Liakopoulos D","authors_abbrev":"Barral Y et al.","pubmed_publication_date":"2009","pubmed_entrez_date":"2009-10-10","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20634885","title":"TOR and PKA pathways synergize at the level of the Ste11 transcription factor to prevent mating and meiosis in fission yeast.","citation":"PLoS One 2010 Jul 09;5(7):e11514","abstract":"In the fission yeast Schizosaccharomyces pombe, the TOR (target of rapamycin) and PKA (protein kinase A) signaling transduction pathways regulate the expression of genes required for cell growth and sexual differentiation in response to the nutritional environment. Inhibition of Tor2 signaling results in the induction of genes involved in sexual differentiation, and the cells undergo mating and meiosis, even under good nutritional conditions. The same phenotype is observed in mutants in which the PKA pathway is inactive. By contrast, Tor2 overexpression or mutations that hyperactivate PKA signaling impair sexual differentiation, even under poor nutritional conditions. Accordingly, a very important question is to understand the molecular mechanism by which these two pathways coordinately regulate gene expression in response to nutrients.\nHere we demonstrate that TOR and PKA pathways operate coordinately to negatively regulate sexual differentiation by inhibiting the nuclear accumulation of the Ste11 transcription factor. However, the Tor2 pathway is unable to block the nuclear localization of Ste11 under good nutritional conditions when the PKA pathway is inactive. Using microarray analyses, we found that both pathways inhibit sexual differentiation by blocking ste11-dependent gene expression.\nWe conclude that both the PKA and the TOR pathways inhibit Ste11 nuclear accumulation to repress Ste11-dependent gene expression. However, the PKA pathway plays a quantitatively more important role than the TOR pathway in this process.","doi":"10.1371/journal.pone.0011514","authors":"Valbuena N, Moreno S","authors_abbrev":"Valbuena N et al.","pubmed_publication_date":"09 Jul 2010","pubmed_entrez_date":"2010-07-17","publication_year":"2010","canto_session_key":"c22fae2b021bf85d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-14 20:21:20","canto_approved_date":"2026-04-08 11:09:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-03 15:54:31","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.09","SPBC106.10","SPBC32C12.02","SPBC216.07c","SPAC8C9.03","SPAC6F12.02","SPBC19C7.03"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2016-01-14"},{"uniquename":"EMBL:D85902","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12699646","title":"Protein homeostasis: a degrading role for Int6/eIF3e.","citation":"Curr Biol 2003 Apr 15;13(8):R323-5","abstract":"Similarities between the three related \"PCI\" complexes--eIF3, the COP9 signalosome and the proteasome lid--have hinted at novel pathways controlling protein homeostasis. Recent experiments with fission yeast have begun to weigh in with genetic evidence.","authors":"von Arnim AG, Chamovitz DA","authors_abbrev":"von Arnim AG et al.","pubmed_publication_date":"15 Apr 2003","pubmed_entrez_date":"2003-04-18","publication_year":"2003","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:33925026","title":"Dual Impact of a Benzimidazole Resistant β-Tubulin on Microtubule Behavior in Fission Yeast.","citation":"Cells 2021 Apr 28;10(5)","abstract":"The cytoskeleton microtubule consists of polymerized αβ-tubulin dimers and plays essential roles in many cellular events. Reagents that inhibit microtubule behaviors have been developed as antifungal, antiparasitic, and anticancer drugs. Benzimidazole compounds, including thiabendazole (TBZ), carbendazim (MBC), and nocodazole, are prevailing microtubule poisons that target β-tubulin and inhibit microtubule polymerization. The molecular basis, however, as to how the drug acts on β-tubulin remains controversial. Here, we characterize the  S. pombe  β-tubulin mutant  nda3-TB101 , which was previously isolated as a mutant resistance to benzimidazole. The mutation site tyrosine at position 50 is located in the interface of two lateral β-tubulin proteins and at the gate of a putative binging pocket for benzimidazole. Our observation revealed two properties of the mutant tubulin. First, the dynamics of cellular microtubules comprising the mutant β-tubulin were stabilized in the absence of benzimidazole. Second, the mutant protein reduced the affinity to benzimidazole in vitro. We therefore conclude that the mutant β-tubulin Nda3-TB101 exerts a dual effect on microtubule behaviors: the mutant β-tubulin stabilizes microtubules and is insensitive to benzimidazole drugs. This notion fine-tunes the current elusive molecular model regarding binding of benzimidazole to β-tubulin.","doi":"10.3390/cells10051042","authors":"Minagawa M, Shirato M, Toya M, Sato M","authors_abbrev":"Minagawa M et al.","pubmed_publication_date":"28 Apr 2021","pubmed_entrez_date":"2021-04-30","publication_year":"2021","canto_session_key":"d8d0ae0fabd341f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Masamitsu Sato","canto_first_approved_date":"2021-05-21 10:54:09","canto_approved_date":"2024-03-29 10:18:16","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-05-12 13:52:29","canto_added_date":"2021-05-02 00:15:05","annotation_curators":[{"name":"Masamitsu Sato","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC18G6.15","SPCC895.07","SPAC890.02c","SPBC26H8.07c","SPBC1685.15c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2021-05-21"},{"uniquename":"PMID:16110343","title":"Comparative genomics and disorder prediction identify biologically relevant SH3 protein interactions.","citation":"PLoS Comput Biol 2005 Aug;1(3):e26","abstract":"Protein interaction networks are an important part of the post-genomic effort to integrate a part-list view of the cell into system-level understanding. Using a set of 11 yeast genomes we show that combining comparative genomics and secondary structure information greatly increases consensus-based prediction of SH3 targets. Benchmarking of our method against positive and negative standards gave 83% accuracy with 26% coverage. The concept of an optimal divergence time for effective comparative genomics studies was analyzed, demonstrating that genomes of species that diverged very recently from Saccharomyces cerevisiae(S. mikatae, S. bayanus, and S. paradoxus), or a long time ago (Neurospora crassa and Schizosaccharomyces pombe), contain less information for accurate prediction of SH3 targets than species within the optimal divergence time proposed. We also show here that intrinsically disordered SH3 domain targets are more probable sites of interaction than equivalent sites within ordered regions. Our findings highlight several novel S. cerevisiae SH3 protein interactions, the value of selection of optimal divergence times in comparative genomics studies, and the importance of intrinsic disorder for protein interactions. Based on our results we propose novel roles for the S. cerevisiae proteins Abp1p in endocytosis and Hse1p in endosome protein sorting.","authors":"Beltrao P, Serrano L","authors_abbrev":"Beltrao P et al.","pubmed_publication_date":"Aug 2005","pubmed_entrez_date":"2005-08-20","publication_year":"2005","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8026462","title":"Characterization of two protein kinases from Schizosaccharomyces pombe involved in the regulation of DNA repair.","citation":"EMBO J 1994 Jun 15;13(12):2777-88","abstract":"We have identified two novel genes designated hhp1+ and hhp2+ in the fission yeast Schizosaccharomyces pombe. The hhp1+ and hhp2+ genes encode two closely related protein kinases that share significant sequence identities with Hrr25p from Saccharomyces cerevisiae. Characterization of strains harboring single and double mutations in the hhp+ genes reveals DNA repair defects in these cells. Schizosaccharomyces pombe strains lacking either or both Hhp activities reveal differences in their ability to withstand DNA lesions caused by either methyl methanesulfonate (MMS) or gamma-rays which correlate with their ability to repair DNA strand breaks caused by these agents. We suggest that Hhp1 and Hhp2 are involved in the regulation of distinct and overlapping DNA repair pathways in S. pombe.","authors":"Dhillon N, Hoekstra MF","authors_abbrev":"Dhillon N et al.","pubmed_publication_date":"15 Jun 1994","pubmed_entrez_date":"1994-06-15","publication_year":"1994","canto_session_key":"99136d907cd60958","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-04 13:46:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-09-04 13:46:29","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC3H7.15","SPAC23C4.12"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-09-04"},{"uniquename":"PMID:34499159","title":"Fission yeast TOR complex 1 phosphorylates Psk1 through an evolutionarily conserved interaction mediated by the TOS motif.","citation":"J Cell Sci 2021 Oct 01;134(19)","abstract":"TOR complex 1 (TORC1) is a multi-subunit protein kinase complex that controls cellular growth in response to environmental cues. The regulatory subunits of mammalian TORC1 (mTORC1) include RAPTOR (also known as RPTOR), which recruits mTORC1 substrates, such as S6K1 (also known as RPS6KB1) and 4EBP1 (EIF4EBP1), by interacting with their TOR signaling (TOS) motif. Despite the evolutionary conservation of TORC1, no TOS motif has been described in lower eukaryotes. In the present study, we show that the fission yeast S6 kinase Psk1 contains a TOS motif that interacts with Mip1, a RAPTOR ortholog. The TOS motif in Psk1 resembles those in mammals, including the conserved phenylalanine and aspartic acid residues essential for the Mip1 interaction and TORC1-dependent phosphorylation of Psk1. The binding of the TOS motif to Mip1 is dependent on Mip1 Tyr-533, whose equivalent in RAPTOR is known to interact with the TOS motif in their co-crystals. Furthermore, we utilized the mip1-Y533A mutation to screen the known TORC1 substrates in fission yeast and successfully identified Atg13 as a novel TOS-motif-containing substrate. These results strongly suggest that the TOS motif represents an evolutionarily conserved mechanism of the substrate recognition by TORC1.","doi":"10.1242/jcs.258865","authors":"Morozumi Y, Hishinuma A, Furusawa S, Sofyantoro F, Tatebe H, Shiozaki K","authors_abbrev":"Morozumi Y et al.","pubmed_publication_date":"01 Oct 2021","pubmed_entrez_date":"2021-09-09","publication_year":"2021","canto_session_key":"a21807569990efc2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Yuichi Morozumi","canto_first_approved_date":"2021-09-23 17:10:41","canto_approved_date":"2021-09-23 17:18:54","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-23 17:10:56","canto_added_date":"2021-09-11 00:15:03","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null},{"name":"Yuichi Morozumi","community_curator":true,"annotation_count":52,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC13G6.07c","SPCC4G3.08","SPAC31G5.12c","SPAC4F10.07c","SPAC22E12.14c","SPAC57A7.11","SPAPB1E7.12","SPBC216.07c","SPAC1B9.02c"],"gene_count":9,"ltp_gene_count":3,"approved_date":"2021-09-23"},{"uniquename":"PMID:17295836","title":"Fission yeast autophagy induced by nitrogen starvation generates a nitrogen source that drives adaptation processes.","citation":"Genes Cells 2007 Feb;12(2):155-70","abstract":"Autophagy is a conserved bulk protein degradation process that is proposed to play a role in events that arise when organisms are forced to radically change their fate, including nutritional starvation, differentiation and development. In our present study, we have identified fission yeast autophagy as a bulk protein degradation process induced by the deprivation of environmental nitrogen, the effects of which are known to trigger sexual differentiation as an adaptive response. Autophagy-defective mutants were found to be sterile in the absence of environmental nitrogen, but could complete sexual differentiation when nitrogen was supplied, suggesting that the major function of autophagy is to provide a nitrogen source. In addition, the environmental nitrogen levels act as an autophagy \"on/off\" switch, whereas components essential for sexual differentiation were dispensable for this regulation. We propose that fission yeast autophagy functions to supply nitrogen and is activated when cells cannot access exogenous nitrogen, thus ensuring that they can adapt and subsequently propagate.","authors":"Kohda TA, Tanaka K, Konomi M, Sato M, Osumi M, Yamamoto M","authors_abbrev":"Kohda TA et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-02-14","publication_year":"2007","canto_session_key":"b25a6bc32f67d4fb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-20 23:59:40","canto_approved_date":"2019-10-16 14:55:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-01-20 23:59:29","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":68,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC330.05c","SPBC32C12.02","SPAC4F10.07c","SPCC63.08c","SPCC777.09c","SPBP8B7.24c","SPBC30D10.10c","SPAC227.18","SPAC4A8.04","SPBC1A4.02c"],"gene_count":10,"ltp_gene_count":10,"approved_date":"2016-01-20"},{"uniquename":"EMBL:AJ251854","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNORNA.04"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:8939063","title":"Cdc6 and DNA replication: limited to humble origins.","citation":"Bioessays 1996 Nov;18(11):859-62","abstract":"The budding yeast Cdc6 protein is important for regulating DNA replication initiation. Cdc6p acts at replication origins, and cdc6-1 mutants arrest with unreplicated DNA and show elevated minichromosome loss rates. Overexpression of the related Cdc18 protein in fission yeast results in DNA rereplication; however, Cdc6p overexpression does not cause this result. A recent paper further defines the role of Cdc6p in DNA replication. Cdc6p only promotes DNA replication between the end of mitosis and late G1, and although the Cdc6 protein is highly unstable, neither degradation nor nuclear localization is critical for limiting DNA replication to this interval.","authors":"Heichman KA","authors_abbrev":"Heichman KA","pubmed_publication_date":"Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18505873","title":"Schizosaccharomyces pombe histone acetyltransferase Mst1 (KAT5) is an essential protein required for damage response and chromosome segregation.","citation":"Genetics 2008 Jun;179(2):757-71","abstract":"Schizosaccharomyces pombe Mst1 is a member of the MYST family of histone acetyltransferases and is the likely ortholog of Saccharomyces cerevisiae Esa1 and human Tip60 (KAT5). We have isolated a temperature-sensitive allele of this essential gene. mst1 cells show a pleiotropic phenotype at the restrictive temperature. They are sensitive to a variety of DNA-damaging agents and to the spindle poison thiabendazole. mst1 has an increased frequency of Rad22 repair foci, suggesting endogenous damage. Two-hybrid results show that Mst1 interacts with a number of proteins involved in chromosome integrity and centromere function, including the methyltransferase Skb1, the recombination mediator Rad22 (Sc Rad52), the chromatin assembly factor Hip1 (Sc Hir1), and the Msc1 protein related to a family of histone demethylases. mst1 mutant sensitivity to hydroxyurea suggests a defect in recovery following HU arrest. We conclude that Mst1 plays essential roles in maintenance of genome stability and recovery from DNA damage.","doi":"10.1534/genetics.107.085779","authors":"Gómez EB, Nugent RL, Laria S, Forsburg SL","authors_abbrev":"Gómez EB et al.","pubmed_publication_date":"Jun 2008","pubmed_entrez_date":"2008-05-29","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC428.08c","SPBC776.12c","SPAC637.12c","SPAC9E9.10c","SPAC343.11c","SPBC25D12.03c","SPCC16A11.17","SPBC800.03","SPBC16H5.11c","SPBC31F10.13c","SPBC4.04c","SPAC2G11.14","SPAC22F3.09c","SPAC30D11.10","SPAC15A10.16","SPAC664.01c","SPAC1834.11c","SPAC644.14c","SPBC29A10.15","SPAC3H5.06c","SPAC1556.01c"],"gene_count":21,"ltp_gene_count":21},{"uniquename":"PMID:23619768","title":"Functional characterization of Upf1 targets in Schizosaccharomyces pombe.","citation":"RNA Biol 2013 Jun;10(6):1057-65","abstract":"Nonsense-mediated mRNA decay (NMD) is a highly conserved mechanism of mRNA degradation. NMD eliminates mRNAs containing premature termination codons (PTCs), preventing the production of truncated proteins with possible deleterious effects. However, there is mounting evidence that NMD factors, like Upf1, Upf2 and Upf3, participate in general regulation of gene expression, affecting the expression of genes lacking PTCs. We have used the fission yeast Schizosaccharomyces pombe to identify mRNAs directly regulated by NMD. Using a combination of genetic and biochemical approaches, we have defined a population of fission yeast mRNAs specifically regulated by Upf1. We show that other components of the Upf complex, Upf2 and Upf3, are required for binding of Upf1 to its RNA targets and for the proper response of fission yeast to oxidative stress. Finally, we investigated the physiological importance of this phenomenon, and demonstrate that the Upf1-dependent downregulation of some of its direct targets is necessary for normal resistance to oxidative stress.","doi":"10.4161/rna.24569","authors":"Matia-González AM, Hasan A, Moe GH, Mata J, Rodríguez-Gabriel MA","authors_abbrev":"Matia-González AM et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-04-27","publication_year":"2013","canto_session_key":"4e18f61e8bc4c5e9","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC63.13","SPAC11D3.09","SPAC16C9.06c","SPBC1347.07"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:8574899","title":"Endogenous endonuclease hypersensitive sites in Schizosaccharomyces pombe chromosomes.","citation":"Genet Anal 1995 Oct;12(2):85-93","abstract":"A novel method was used to characterize the long range susceptibility of Schizosaccharomyces pombe chromosomal DNA to endogenous endonuclease cleavage. Analyses of pulsed field gel experiments revealed two periodicities in the distribution of endogenous endonuclease hypersensitive sites. Endonuclease cleavage sites occurred, roughly at 30-509 kilobase pairs (kb) intervals under physiological conditions (25 mM KCl). At higher salt concentrations (250 mM KCl or 0.2 M and 0.9 M NaCl), endonuclease hypersensitive sites occurred at 200-300 kb intervals. Endonuclease hypersensitive sites in different chromosomal regions were monitored during different stages of the cell cycle. DNA sequencing around the endonuclease hypersensitive sites revealed the presence of clusters of A+T-rich motifs, autonomously replicating sequences (ARSs) in sequences (a characteristic of the scaffold-associated regions (SARs) and the presence of a CTG trinucleotide at most sites.","authors":"Fan JB, Smith CL","authors_abbrev":"Fan JB et al.","pubmed_publication_date":"Oct 1995","pubmed_entrez_date":"1995-10-01","publication_year":"1995","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25262651","title":"De novo mutations in synaptic transmission genes including DNM1 cause epileptic encephalopathies.","citation":"Am J Hum Genet 2014 Oct 02;95(4):360-70","abstract":"Emerging evidence indicates that epileptic encephalopathies are genetically highly heterogeneous, underscoring the need for large cohorts of well-characterized individuals to further define the genetic landscape. Through a collaboration between two consortia (EuroEPINOMICS and Epi4K/EPGP), we analyzed exome-sequencing data of 356 trios with the \"classical\" epileptic encephalopathies, infantile spasms and Lennox Gastaut syndrome, including 264 trios previously analyzed by the Epi4K/EPGP consortium. In this expanded cohort, we find 429 de novo mutations, including de novo mutations in DNM1 in five individuals and de novo mutations in GABBR2, FASN, and RYR3 in two individuals each. Unlike previous studies, this cohort is sufficiently large to show a significant excess of de novo mutations in epileptic encephalopathy probands compared to the general population using a likelihood analysis (p = 8.2 × 10(-4)), supporting a prominent role for de novo mutations in epileptic encephalopathies. We bring statistical evidence that mutations in DNM1 cause epileptic encephalopathy, find suggestive evidence for a role of three additional genes, and show that at least 12% of analyzed individuals have an identifiable causal de novo mutation. Strikingly, 75% of mutations in these probands are predicted to disrupt a protein involved in regulating synaptic transmission, and there is a significant enrichment of de novo mutations in genes in this pathway in the entire cohort as well. These findings emphasize an important role for synaptic dysregulation in epileptic encephalopathies, above and beyond that caused by ion channel dysfunction.","doi":"10.1016/j.ajhg.2014.08.013","authors":"EuroEPINOMICS-RES Consortium, Epilepsy Phenome/Genome Project, Epi4K Consortium","authors_abbrev":"EuroEPINOMICS-RES Consortium et al.","pubmed_publication_date":"02 Oct 2014","pubmed_entrez_date":"2014-09-30","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12C2.08"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34864879","title":"Complementation of fission yeast kinesin-5/Cut7 with human Eg5 provides a versatile platform for screening of anticancer compounds.","citation":"Biosci Biotechnol Biochem 2022 Jan 24;86(2):254-259","abstract":"Kinesin-5 family proteins are essential for bipolar spindle assembly to ensure mitotic fidelity. Here, we demonstrate evolutionary functional conservation of kinesin-5 between human and fission yeast. Human Eg5 expressed in the nucleus replaces fission yeast counterpart Cut7. Intriguingly, Eg5 overproduction results in cytotoxicity. This phenotype provides a useful platform for the development of novel kinesin-5 inhibitors as anticancer drugs.","doi":"10.1093/bbb/zbab212","authors":"Hwang W, Toda T, Yukawa M","authors_abbrev":"Hwang W et al.","pubmed_publication_date":"24 Jan 2022","pubmed_entrez_date":"2021-12-05","publication_year":"2022","canto_session_key":"b04f65f05c1bf815","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-12-30 10:04:59","canto_approved_date":"2024-12-30 10:05:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-11-28 17:58:01","canto_added_date":"2021-12-08 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC25G10.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2024-12-30"},{"uniquename":"PMID:28572184","title":"Construction, Growth, and Harvesting of Fission Yeast Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) Strains.","citation":"Cold Spring Harb Protoc 2017 Jun 01;2017(6):pdb.prot091678","abstract":"Stable isotope labeling by amino acids in cell culture (SILAC) enables the relative quantification of protein amounts and posttranslational modifications in complex biological samples through the use of stable heavy isotope-labeled amino acids. Here we describe methods for the application of SILAC to fission yeast  Schizosaccharomyces pombe  using either labeled lysine or a combination of labeled lysine and labeled arginine. The latter approach is more complicated than the use of labeled lysine alone but may yield a more comprehensive (phospho)proteomic analysis. The protocol includes methods for construction of SILAC-compatible strains, growth of cultures in labeled medium, cell harvesting, and protein extraction.","doi":"10.1101/pdb.prot091678","authors":"Koch A, Bicho CC, Borek WE, Carpy A, Maček B, Hauf S, Sawin KE","authors_abbrev":"Koch A et al.","pubmed_publication_date":"01 Jun 2017","pubmed_entrez_date":"2017-06-03","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-06-04 00:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11409178","title":"Fission yeast tor1 functions in response to various stresses including nitrogen starvation, high osmolarity, and high temperature.","citation":"Curr Genet 2001 May;39(3):166-74","abstract":"A target of rapamycin (TOR) protein is a protein kinase that exerts cellular signal transduction to regulate cell growth in response to extracellular nutrient conditions. In the Schizosaccharomyces pombe genome database, there are two genes encoding TOR-related proteins, but their functions have not been analyzed. Here we report that one of the genes, referred to as tor1+, is required for sexual development induced by nitrogen starvation. Ste11 is a key transcription factor for the initiation of sexual development. The expression of ste11+ is normally regulated in tor1- cells; and overexpression of ste11+ hardly rescues the defect in fertility in tor1-. Upon nitrogen starvation, tor1+ cells promote two rounds of the cell cycle to become arrested at the G1 phase before initiation of sexual development. The tor1- cells do not promote such a cell cycle, suggesting that Tor1 is necessary for the response to nitrogen starvation. The tor1- cells show no growth or very slow growth under various stress conditions, including external high pH, high concentrations of salts or sorbitol, and high temperature. These results suggest that Tor1 is necessary for any response to a wide range of stresses. The vegetative growth of tor1- cells is inhibited by rapamycin, although tor1+ cells are resistant to the drug. The tor1- cells are hypersensitive to fluphenazine and cyclosporin A, which specifically inhibit calmodulin and calcineurin, respectively.","authors":"Kawai M, Nakashima A, Ueno M, Ushimaru T, Aiba K, Doi H, Uritani M","authors_abbrev":"Kawai M et al.","pubmed_publication_date":"May 2001","pubmed_entrez_date":"2001-06-21","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18729046","title":"A vector system for genomic FLAG epitope-tagging in Schizosaccharomyces pombe.","citation":"Biotechnol J 2008 Oct;3(9-10):1280-5","abstract":"The fission yeast Schizosaccharomyces pombe is a popular model organism to study various cellular processes, although research tools available for S. pombe are relatively inadequate. To facilitate genetic and biochemical investigation in S. pombe, we report here a system of vectors for genomic FLAG epitope-tagging. These vectors enable us to amplify gene-targeting fragments for integration into specific loci of the S. pombe genome. All vectors in this report were designed to express FLAG epitope-tagged proteins from their endogenous genomic loci. Vectors for N-terminal FLAG epitope-tagging allow us to control protein expression levels using the wild-type nmt1 promoter, its weaker derivatives, and the urg1 promoter. These vectors are available with various antibiotic markers including kanMX6, hphMX6, natMX6 and bleMX6, and the his3(+) marker. Vectors for C-terminal FLAG epitope-tagging were designed to express FLAG-fusion proteins under the control of their native promoters at their own genomic loci, allowing us to characterize protein functions under physiological conditions. These vectors are available with kanMX6, hphMX6, nat-MX6 and bleMX6 markers. The series of vectors described in this report should prove useful for protein studies in fission yeast.","doi":"10.1002/biot.200800140","authors":"Noguchi C, Garabedian MV, Malik M, Noguchi E","authors_abbrev":"Noguchi C et al.","pubmed_publication_date":"Oct 2008","pubmed_entrez_date":"2008-08-30","publication_year":"2008","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28283058","title":"5' End Nicotinamide Adenine Dinucleotide Cap in Human Cells Promotes RNA Decay through DXO-Mediated deNADding.","citation":"Cell 2017 Mar 09;168(6):1015-1027.e10","abstract":"Eukaryotic mRNAs generally possess a 5' end N7 methyl guanosine (m 7 G) cap that promotes their translation and stability. However, mammalian mRNAs can also carry a 5' end nicotinamide adenine dinucleotide (NAD + ) cap that, in contrast to the m 7 G cap, does not support translation but instead promotes mRNA decay. The mammalian and fungal noncanonical DXO/Rai1 decapping enzymes efficiently remove NAD +  caps, and cocrystal structures of DXO/Rai1 with 3'-NADP +  illuminate the molecular mechanism for how the \"deNADding\" reaction produces NAD +  and 5' phosphate RNA. Removal of DXO from cells increases NAD + -capped mRNA levels and enables detection of NAD + -capped intronic small nucleolar RNAs (snoRNAs), suggesting NAD +  caps can be added to 5'-processed termini. Our findings establish NAD +  as an alternative mammalian RNA cap and DXO as a deNADding enzyme modulating cellular levels of NAD + -capped RNAs. Collectively, these data reveal that mammalian RNAs can harbor a 5' end modification distinct from the classical m 7 G cap that promotes rather than inhibits RNA decay.","doi":"10.1016/j.cell.2017.02.019","authors":"Jiao X, Doamekpor SK, Bird JG, Nickels BE, Tong L, Hart RP, Kiledjian M","authors_abbrev":"Jiao X et al.","pubmed_publication_date":"09 Mar 2017","pubmed_entrez_date":"2017-03-12","publication_year":"2017","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC19D5.06c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:14984369","title":"Cell viability and secretion of active proteins in Schizosaccharomyces pombe do not require the chaperone function of calnexin.","citation":"Biochem J 2004 Jun 01;380(Pt 2):441-8","abstract":"Folding of newly synthesized proteins within the ER (endoplasmic reticulum) is a rate-limiting step in protein secretion. Thus ER molecular chaperones and foldases have a major impact in determining the rate and yield of these crucial cellular processes. Calnexin is a key ER chaperone implicated in the folding, retention and targeting for degradation of proteins that go through the secretory pathway. Calnexin molecules contain a highly conserved central domain (hcd) that has been proposed to be involved in the interaction with folding substrates and other chaperones. To gain a better understanding of the roles played by calnexin in the secretory pathway, we examined the efficiency of fission yeast (Schizosaccharomyces pombe) strains expressing calnexin mutants to secrete different model proteins. Remarkably, calnexin hcd-deletion mutants, although devoid of detectable chaperone activity in vitro, confer viability and cause a considerable increase in the secretion of heterologous cellulase. Surprisingly the quality-control efficiency, measured as the activity/amount ratio of secreted model protein, was not severely reduced in these calnexin hcd-deletion mutant strains. Our results indicate that the essential function of calnexin does not reside in its role in the folding or in the retention of misfolded proteins. These observations suggest the existence of a highly stringent quality control mechanism in the ER of S. pombe that might reduce the secretion efficiency of endogenous proteins.","authors":"Maréchal A, Tanguay PL, Callejo M, Guérin R, Boileau G, Rokeach LA","authors_abbrev":"Maréchal A et al.","pubmed_publication_date":"01 Jun 2004","pubmed_entrez_date":"2004-02-27","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3C7.11c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:21540296","title":"Condensin phosphorylated by the Aurora-B-like kinase Ark1 is continuously required until telophase in a mode distinct from Top2.","citation":"J Cell Sci 2011 Jun 01;124(Pt 11):1795-807","abstract":"Condensin is a conserved protein complex that functions in chromosome condensation and segregation. It has not been previously unequivocally determined whether condensin is required throughout mitosis. Here, we examined whether Schizosaccharomyces pombe condensin continuously acts on chromosomes during mitosis and compared its role with that of DNA topoisomerase II (Top2). Using double mutants containing a temperature-sensitive allele of the condensin SMC2 subunit cut14 (cut14-208) or of top2, together with the cold-sensitive nda3-KM311 mutation (in β-tubulin), temperature-shift experiments were performed. These experiments allowed inactivation of condensin or Top2 at various stages throughout mitosis, even after late anaphase. The results established that mitotic chromosomes require condensin and Top2 throughout mitosis, even in telophase. We then showed that the Cnd2 subunit of condensin (also known as Barren) is the target subunit of Aurora-B-like kinase Ark1 and that Ark1-mediated phosphorylation of Cnd2 occurred throughout mitosis. The phosphorylation sites in Cnd2 were determined by mass spectrometry, and alanine and glutamate residue replacement mutant constructs for these sites were constructed. Alanine substitution mutants of Cnd2, which mimic the unphosphorylated protein, exhibited broad mitotic defects, including at telophase, and overexpression of these constructs caused a severe dominant-negative effect. By contrast, glutamate substitution mutants, which mimic the phosphorylated protein, alleviated the segregation defect in Ark1-inhibited cells. In telophase, the condensin subunits in cut14-208 mutant accumulated in lumps that contained telomeric DNA and proteins that failed to segregate. Condensin might thus serve to keep the segregated chromosomes apart during telophase.","doi":"10.1242/jcs.078733","authors":"Nakazawa N, Mehrotra R, Ebe M, Yanagida M","authors_abbrev":"Nakazawa N et al.","pubmed_publication_date":"01 Jun 2011","pubmed_entrez_date":"2011-05-05","publication_year":"2011","canto_session_key":"200ad9dc9f52e2f1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-10-30 20:07:03","canto_approved_date":"2017-10-30 20:07:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-01 07:44:55","canto_added_date":"2012-02-24 05:47:11","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":59,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.03c","SPBC582.03","SPCC306.03c","SPBC26H8.07c","SPBC776.13","SPCC320.13c","SPBC146.03c","SPBP4H10.06c","SPCC188.03"],"gene_count":9,"ltp_gene_count":8,"approved_date":"2017-10-30"},{"uniquename":"PMID:2987220","title":"Isolation of the fructose-1,6-bisphosphatase gene of the yeast Schizosaccharomyces pombe. Evidence for transcriptional regulation.","citation":"J Biol Chem 1985 May 25;260(10):6348-53","abstract":"The fructose-1,6-bisphosphatase structural gene (FBP+) of Schizosaccharomyces pombe has been isolated by genetic complementation of a deficient mutant, which is characterized by the inability to grow on a nonfermentable carbon source such as glycerol. Growth on glycerol-containing medium was restored in a S. pombe fructose-1,6-bisphosphatase-deficient mutant (fbp-16) when it was transformed with a plasmid (pAVO4) carrying FBP+. The transformant displayed a 5-fold increase in enzymatic activity when compared to the parental S. pombe strain. Subcloning of DNA fragments from the 8.5-kilobase (kb) insert of pAVO4 defined a 4-kb DNA fragment which contained the functional FBP+ gene and its regulatory region. When this gene was placed under the control of the lac promoter-operator, functional expression in Escherichia coli was obtained, as deduced by complementation of bacterial fructose-1,6-bisphosphatase mutants. The FBP+ gene encodes a 1.9-kb glucose-repressible transcript whose appearance in S. pombe is correlated with fructose-1,6-bisphosphatase derepression in glycerol-containing medium. We suggest that the regulation of the S. pombe FBP+ gene is exerted at the transcriptional level. The S. pombe FBP+ gene gave rise to a 1.9-kb transcript in Saccharomyces cerevisiae, but not to measurable enzymatic activity.","authors":"Vassarotti A, Friesen JD","authors_abbrev":"Vassarotti A et al.","pubmed_publication_date":"25 May 1985","pubmed_entrez_date":"1985-05-25","publication_year":"1985","canto_session_key":"1ec0f3118bd2afb6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-06 20:00:16","canto_approved_date":"2022-02-07 15:05:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-01-06 19:59:59","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1198.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-06"},{"uniquename":"EMBL:AB084845","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.33"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:22017871","title":"Regulation of the Sre1 hypoxic transcription factor by oxygen-dependent control of DNA binding.","citation":"Mol Cell 2011 Oct 21;44(2):225-34","abstract":"Regulation of gene expression plays an integral role in adaptation of cells to hypoxic stress. In mammals, prolyl hydroxylases control levels of the central transcription factor hypoxia inducible factor (HIF) through regulation of HIFα subunit stability. Here, we report that the hydroxylase Ofd1 regulates the Sre1 hypoxic transcription factor in fission yeast by controlling DNA binding. Prolyl hydroxylases require oxygen as a substrate, and the activity of Ofd1 regulates Sre1-dependent transcription. In the presence of oxygen, Ofd1 binds the Sre1 N-terminal transcription factor domain (Sre1N) and inhibits Sre1-dependent transcription by blocking DNA binding. In the absence of oxygen, the inhibitor Nro1 binds Ofd1, thereby releasing Sre1N and leading to activation of genes required for hypoxic growth. In contrast to the HIF system, where proline hydroxylation is essential for regulation, Ofd1 inhibition of Sre1N does not require hydroxylation and, thus, defines a new mechanism for hypoxic gene regulation.","doi":"10.1016/j.molcel.2011.08.031","authors":"Lee CY, Yeh TL, Hughes BT, Espenshade PJ","authors_abbrev":"Lee CY et al.","pubmed_publication_date":"21 Oct 2011","pubmed_entrez_date":"2011-10-25","publication_year":"2011","canto_session_key":"4d5512a5dc8ea4bc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Peter Espenshade","canto_first_approved_date":"2017-11-10 00:48:52","canto_approved_date":"2024-03-12 07:27:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-11-30 14:48:10","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":20,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Peter Espenshade","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC6B1.08c","SPAC15A10.11","SPBC19C2.09","SPBC19C7.02","SPCC4B3.07","SPAC18B11.07c","SPAC1687.16c","SPAC222.11","SPAC17A2.05"],"gene_count":9,"ltp_gene_count":6,"approved_date":"2017-11-10"},{"uniquename":"PMID:39412391","title":"Negative regulation of APC/C activation by MAPK-mediated attenuation of Cdc20 Slp1  under stress.","citation":"Elife 2024 Oct 16;13","abstract":"Mitotic anaphase onset is a key cellular process tightly regulated by multiple kinases. The involvement of mitogen-activated protein kinases (MAPKs) in this process has been established in  Xenopus  egg extracts. However, the detailed regulatory cascade remains elusive, and it is also unknown whether the MAPK-dependent mitotic regulation is evolutionarily conserved in the single-cell eukaryotic organisms such as fission yeast ( Schizosaccharomyces pombe ). Here, we show that two MAPKs in  S. pombe  indeed act in concert to restrain anaphase-promoting complex/cyclosome (APC/C) activity upon activation of the spindle assembly checkpoint (SAC). One MAPK, Pmk1, binds to and phosphorylates Slp1 Cdc20 , the co-activator of APC/C. Phosphorylation of Slp1 Cdc20  by Pmk1, but not by Cdk1, promotes its subsequent ubiquitylation and degradation. Intriguingly, Pmk1-mediated phosphorylation event is also required to sustain SAC under environmental stress. Thus, our study establishes a new underlying molecular mechanism of negative regulation of APC/C by MAPK upon stress stimuli, and provides a previously unappreciated framework for regulation of anaphase entry in eukaryotic cells.","doi":"10.7554/eLife.97896","authors":"Sun L, Chen X, Song C, Shi W, Liu L, Bai S, Wang X, Chen J, Jiang C, Wang SM, Luo ZQ, Wang R, Wang Y, Jin QW","authors_abbrev":"Sun L et al.","pubmed_publication_date":"16 Oct 2024","pubmed_entrez_date":"2024-10-16","publication_year":"2024","canto_session_key":"b1575578703a0584","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-10-16 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34967417","title":"Redirecting meiotic DNA break hotspot determinant proteins alters localized spatial control of DNA break formation and repair.","citation":"Nucleic Acids Res 2022 Jan 25;50(2):899-914","abstract":"During meiosis, DNA double-strand breaks (DSBs) are formed at high frequency at special chromosomal sites, called DSB hotspots, to generate crossovers that aid proper chromosome segregation. Multiple chromosomal features affect hotspot formation. In the fission yeast S. pombe the linear element proteins Rec25, Rec27 and Mug20 are hotspot determinants - they bind hotspots with high specificity and are necessary for nearly all DSBs at hotspots. To assess whether they are also sufficient for hotspot determination, we localized each linear element protein to a novel chromosomal site (ade6 with lacO substitutions) by fusion to the Escherichia coli LacI repressor. The Mug20-LacI plus lacO combination, but not the two separate lac elements, produced a strong ade6 DSB hotspot, comparable to strong endogenous DSB hotspots. This hotspot had unexpectedly low ade6 recombinant frequency and negligible DSB hotspot competition, although like endogenous hotspots it manifested DSB interference. We infer that linear element proteins must be properly placed by endogenous functions to impose hotspot competition and proper partner choice for DSB repair. Our results support and expand our previously proposed DSB hotspot-clustering model for local control of meiotic recombination.","doi":"10.1093/nar/gkab1253","authors":"Hyppa RW, Cho JD, Nambiar M, Smith GR","authors_abbrev":"Hyppa RW et al.","pubmed_publication_date":"25 Jan 2022","pubmed_entrez_date":"2021-12-30","publication_year":"2022","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-01-01 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28733411","title":"DNA Preparation from  Schizosaccharomyces pombe .","citation":"Cold Spring Harb Protoc 2018 Jan 02;2018(1)","abstract":"This protocol includes two methods for genomic DNA preparation from  Schizosaccharomyces pombe  The first is a quick method for preparation of DNA suitable for polymerase chain reaction (PCR) genotyping. The second, longer method yields high-quality DNA that can be used for amplification of targeting cassettes.","doi":"10.1101/pdb.prot091959","authors":"Roguev A, Xu J, Krogan NJ","authors_abbrev":"Roguev A et al.","pubmed_publication_date":"02 Jan 2018","pubmed_entrez_date":"2017-07-23","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2017-07-25 00:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9990507","title":"Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo-complexes together with cullin-1 in the fission yeast SCF (Skp1-Cullin-1-F-box) ubiquitin ligase.","citation":"Genes Cells 1998 Nov;3(11):721-35","abstract":"In the ubiquitin-dependent proteolysis pathway, a ubiquitin ligase (E3) is responsible for substrate selectivity and timing of degradation. A novel E3, SCF (Skp1-Cullin-1/Cdc53-F-box) plays a pivotal role in cell cycle progression. In fission yeast, F-box/WD-repeat protein Pop1 regulates the level of the CDK (cyclin-dependent kinase) inhibitor Rum1 and the S phase regulator Cdc18.\nWe have cloned and characterized the pop2+ gene which encodes the Pop1-related F-box/WD-repeat protein. Pop2 plays a role which overlaps with Pop1 in the degradation of Rum1 and Cdc18. However, these two proteins are not functional homologues. Pop1 and Pop2 form hetero-as well as homo-dimers in the cell. We have analysed two fission yeast cullin members and found that cullin-1 functions as a component of SCFPop1,2, whilst cullin-3 is involved in the distinct stress-response pathway.\nFission yeast SCF is composed of Pop1 and Pop2, two structurally related but functionally independent F-box/WD-repeat proteins. By forming three distinct complexes, SCFPop1/Pop1, SCFPop1/Pop2 and SCFPop2/Pop2, SCF has evolved a sophisticated mechanism to control the level of Rum1 and Cdc18. Fission yeast SCF also contains cullin-1 as a universal scaffold and each cullin member plays a distinct biological role.","authors":"Kominami K, Ochotorena I, Toda T","authors_abbrev":"Kominami K et al.","pubmed_publication_date":"Nov 1998","pubmed_entrez_date":"1999-02-17","publication_year":"1998","canto_session_key":"41fb94c2ebeaee82","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-05-09 14:40:24","canto_approved_date":"2019-05-09 15:10:34","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2019-05-09 15:10:27","canto_added_date":"2012-02-24 05:53:00","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":26,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G6.12","SPBC14C8.07c","SPBC1718.01","SPBC32F12.09","SPAC4D7.03","SPAC24H6.03"],"gene_count":6,"ltp_gene_count":4,"approved_date":"2019-05-09"},{"uniquename":"PMID:17230581","title":"The 160 N-terminal residues of calnexin define a novel region supporting viability in Schizosaccharomyces pombe.","citation":"Yeast 2007 Feb;24(2):89-103","abstract":"Protein secretion is a complex process that can be modulated by folding factors in the endoplasmic reticulum (ER), such as calnexin, a highly-conserved molecular chaperone involved in quality control. In Schizosaccharomyces pombe, calnexin (Cnx1p) is essential for cell viability. The calnexin/Cnx1p determinants required for viability have been mapped within the last 123 residues of its C-terminus. To better understand the role(s) of calnexin/Cnx1p in secretion, we screened for cnx1 mutants 'super-secreting' cellulase. We identified ss14_cnx1, a mutant secreting 10-fold higher levels of the glycoprotein cellulase than the wild-type strain. While cellulase did not interact with ss14_Cnx1p, the ratio of secreted activity/quantity for this enzyme was not affected, suggesting that the quality control of folding in the ER was adequate in the mutant strain. Surprisingly, the ss14_Cnx1p mutant is composed of the 160 N-terminal amino acids of the mature molecule, thus this mutant defines a novel calnexin/Cnx1p region supporting Sz. pombe viability. Interestingly, like viable mutants spanning the last 52 aa of calnexin/Cnx1p, the 160 N-terminal residues encoded by ss14_cnx1 also forms a complex with the essential BiP chaperone. These results reveal the so far unidentified importance of the N-terminal region of calnexin/Cnx1p.","authors":"Hajjar F, Beauregard PB, Rokeach LA","authors_abbrev":"Hajjar F et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2007-01-19","publication_year":"2007","canto_session_key":"e5fd3c0c269a8bf9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-06 19:33:32","canto_approved_date":"2019-05-13 00:25:06","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-01-06 19:33:23","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.11c","SPAC22A12.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-01-06"},{"uniquename":"PMID:6252189","title":"Synchronization of cell division in microorganisms by percoll gradients.","citation":"J Bacteriol 1980 Oct;144(1):17-21","abstract":"We describe a method for obtaining synchronously dividing cells of bacteria (Escherichia coli B and K-12 and Bacillus subtilis 168) and fission yeasts (Schizosaccharomyces pombe) by the use of Percoll density gradients.","authors":"Dwek RD, Kobrin LH, Grossman N, Ron EZ","authors_abbrev":"Dwek RD et al.","pubmed_publication_date":"Oct 1980","pubmed_entrez_date":"1980-10-01","publication_year":"1980","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29641590","title":"Structural and functional analysis of Utp24, an endonuclease for processing 18S ribosomal RNA.","citation":"PLoS One 2018;13(4):e0195723","abstract":"The precursor ribosomal RNA is processed by multiple steps of nucleolytic cleavage to generate mature rRNAs. Utp24 is a PIN domain endonuclease in the early 90S precursor of small ribosomal subunit and is proposed to cleave at sites A1 and A2 of pre-rRNA. Here we determine the crystal structure of Utp24 from Schizosaccharomyces pombe at 2.1 angstrom resolution. Utp24 structurally resembles the ribosome assembly factor Utp23 and both contain a Zn-finger motif. Functional analysis in Saccharomyces cerevisiae shows that depletion of Utp24 disturbs the assembly of 90S and abolishes cleavage at sites A0, A1 and A2. The 90S assembled with inactivated Utp24 is arrested at a post-A0-cleavage state and contains enriched nuclear exosome for degradation of 5' ETS. Despite of high sequence conservation, Utp24 from other organisms is unable to form an active 90S in S. cerevisiae, suggesting that Utp24 needs to be precisely positioned in 90S. Our study provides biochemical and structural insight into the role of Utp24 in 90S assembly and activity.","doi":"10.1371/journal.pone.0195723","authors":"An W, Du Y, Ye K","authors_abbrev":"An W et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-04-12","publication_year":"2018","canto_session_key":"ec4393738ec076b0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-08-29 19:06:32","canto_approved_date":"2019-08-29 19:06:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-08-13 10:46:07","canto_added_date":"2018-04-13 00:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":10,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-08-29","pdb_entries":[{"pdb_id":"5yz4","gene_chains":[{"gene_uniquename":"SPBC32H8.04c","chain":"A","position":"60-192"}],"title":"Structure of the PIN domain endonuclease Utp24","entry_authors":"Du Y,An W,Ye K","entry_authors_abbrev":"Du Y et al.","reference_uniquename":"PMID:29641590","experimental_method":"X-ray","resolution":"2.135"}]},{"uniquename":"EMBL:AU008959","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19039133","title":"Tight regulation of unstructured proteins: from transcript synthesis to protein degradation.","citation":"Science 2008 Nov 28;322(5906):1365-8","abstract":"Altered abundance of several intrinsically unstructured proteins (IUPs) has been associated with perturbed cellular signaling that may lead to pathological conditions such as cancer. Therefore, it is important to understand how cells precisely regulate the availability of IUPs. We observed that regulation of transcript clearance, proteolytic degradation, and translational rate contribute to controlling the abundance of IUPs, some of which are present in low amounts and for short periods of time. Abundant phosphorylation and low stochasticity in transcription and translation indicate that the availability of IUPs can be finely tuned. Fidelity in signaling may require that most IUPs be available in appropriate amounts and not present longer than needed.","doi":"10.1126/science.1163581","authors":"Gsponer J, Futschik ME, Teichmann SA, Babu MM","authors_abbrev":"Gsponer J et al.","pubmed_publication_date":"28 Nov 2008","pubmed_entrez_date":"2008-11-29","publication_year":"2008","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9135149","title":"Nif1, a novel mitotic inhibitor in Schizosaccharomyces pombe.","citation":"EMBO J 1997 Mar 17;16(6):1342-50","abstract":"In Schizosaccharomyces pombe, the activity of the M-phase-inducing Cdc2/Cdc13 cyclin-dependent kinase is inhibited by Wee1 and Mik1 tyrosine kinases, and activated by Cdc25 and Pyp3 tyrosine phosphatases. Cdc2/Cdc13 activity is also indirectly regulated by the approximately 70 kDa Nim1 (Cdrl) serine/threonine kinase, which promotes mitosis by inhibiting Wee1 via direct phosphorylation. To understand better the function and regulation of Nim1, the yeast two-hybrid system was used to isolate S.pombe cDNA clones encoding proteins that interact with Nim1. Sixteen of the 17 cDNA clones were derived from the same gene, named nif1 + (nim1 interacting factor-1). Nif1 is a novel approximately 75 kDa protein containing a leucine zipper motif. The Nif1-Nim1 interaction requires a small region of Nim1 that immediately follows the N-terminal catalytic domain. This region is required for Nim1 activity both in vivo and in vitro. delta nif1 mutants are approximately 10% smaller than wild type, indicating that Nif1 is involved in inhibiting the onset of mitosis. Consistent with this proposal, overproduction of Nif1 was found to cause a cell elongation phenotype that is very similar to delta nim1 mutants. Nif1 overproduction causes cell cycle arrest in cells that are partly defective for Cdc25 activity, but has no effect in delta nim1 or delta wee1 mutants. Nif1 also inhibits Nim1-mediated phosphorylation of Wee1 in an insect cell expression system. These observations strongly suggest that Nif1 negatively regulates the onset of mitosis by a novel mechanism, namely inhibiting Nim1 kinase.","authors":"Wu L, Russell P","authors_abbrev":"Wu L et al.","pubmed_publication_date":"17 Mar 1997","pubmed_entrez_date":"1997-03-17","publication_year":"1997","canto_session_key":"98c68aa0197ec5dc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2017-01-09 20:14:19","canto_approved_date":"2022-06-07 08:43:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-12-30 16:50:25","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.06c","SPCC18B5.03","SPBC23G7.04c","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":2,"approved_date":"2017-01-09"},{"uniquename":"PMID:26889830","title":"A Novel Epigenetic Silencing Pathway Involving the Highly Conserved 5'-3' Exoribonuclease Dhp1/Rat1/Xrn2 in Schizosaccharomyces pombe.","citation":"PLoS Genet 2016 Feb;12(2):e1005873","abstract":"Epigenetic gene silencing plays a critical role in regulating gene expression and contributes to organismal development and cell fate acquisition in eukaryotes. In fission yeast, Schizosaccharomyces pombe, heterochromatin-associated gene silencing is known to be mediated by RNA processing pathways including RNA interference (RNAi) and a 3'-5' exoribonuclease complex, the exosome. Here, we report a new RNA-processing pathway that contributes to epigenetic gene silencing and assembly of heterochromatin mediated by 5'-3' exoribonuclease Dhp1/Rat1/Xrn2. Dhp1 mutation causes defective gene silencing both at peri-centromeric regions and at the silent mating type locus. Intriguingly, mutation in either of the two well-characterized Dhp1-interacting proteins, the Din1 pyrophosphohydrolase or the Rhn1 transcription termination factor, does not result in silencing defects at the main heterochromatic regions. We demonstrate that Dhp1 interacts with heterochromatic factors and is essential in the sequential steps of establishing silencing in a manner independent of both RNAi and the exosome. Genomic and genetic analyses suggest that Dhp1 is involved in post-transcriptional silencing of repetitive regions through its RNA processing activity. The results describe the unexpected role of Dhp1/Rat1/Xrn2 in chromatin-based silencing and elucidate how various RNA-processing pathways, acting together or independently, contribute to epigenetic regulation of the eukaryotic genome.","doi":"10.1371/journal.pgen.1005873","authors":"Tucker JF, Ohle C, Schermann G, Bendrin K, Zhang W, Fischer T, Zhang K","authors_abbrev":"Tucker JF et al.","pubmed_publication_date":"Feb 2016","pubmed_entrez_date":"2016-02-19","publication_year":"2016","canto_session_key":"a0f78e9e9c3c9c40","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-20 01:15:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1F3.01","SPCC736.11","SPACUNK4.06c","SPBC800.03","SPAC26A3.12c","SPAC23G3.01","SPCC188.13c","SPBC16D10.07c"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:15385623","title":"Spindle pole body duplication in fission yeast occurs at the G1/S boundary but maturation is blocked until exit from S by an event downstream of cdc10+.","citation":"Mol Biol Cell 2004 Dec;15(12):5219-30","abstract":"The regulation and timing of spindle pole body (SPB) duplication and maturation in fission yeast was examined by transmission electron microscopy. When cells are arrested at G1 by nitrogen starvation, the SPB is unduplicated. On release from G1, the SPBs were duplicated after 1-2 h. In cells arrested at S by hydroxyurea, SPBs are duplicated but not mature. In G1 arrest/release experiments with cdc2.33 cells at the restrictive temperature, SPBs remained single, whereas in cells at the permissive temperature, SPBs were duplicated. In cdc10 mutant cells, the SPBs seem not only to be duplicated but also to undergo partial maturation, including invagination of the nuclear envelope underneath the SPB. There may be an S-phase-specific inhibitor of SPB maturation whose expression is under control of cdc10(+). This model was examined by induction of overreplication of the genome by overexpression of rum1p or cdc18p. In cdc18p-overexpressing cells, the SPBs are duplicated but not mature, suggesting that cdc18p is one component of this feedback mechanism. In contrast, cells overexpressing rum1p have large, deformed SPBs accompanied by other features of maturation and duplication. We propose a feedback mechanism for maturation of the SPB that is coupled with exit from S to trigger morphological changes.","authors":"Uzawa S, Li F, Jin Y, McDonald KL, Braunfeld MB, Agard DA, Cande WZ","authors_abbrev":"Uzawa S et al.","pubmed_publication_date":"Dec 2004","pubmed_entrez_date":"2004-09-24","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29797299","title":"Schizosaccharomyces pombe as an Efficient Yeast to Convert Sugarcane Bagasse Pretreated with Ionic Liquids in Ethanol.","citation":"Appl Biochem Biotechnol 2018 Dec;186(4):960-971","abstract":"Pretreatment of lignocellulosic biomass with ionic liquids (ILs) has been extensively studied, being regarded as one of the most promising methods for obtaining fermentable sugars. In this research, it was investigated the production of ethanol from sugars released from sugarcane bagasse pretreated with the ionic liquids [C 4 mim][OAc] and [C 2 mim][OAc], hydrolysed with Penicillium echinulatum enzymes and using Saccharomyces cerevisiae and Schizosaccharomyces pombe. Yields of about 43 and 56% of ethanol were observed for S. cerevisiae and biomass pretreated with [C 2 mim][OAc] and [C 4 mim][OAc], respectively. S. pombe yielded 52 and 78% ethanol for [C 2 mim][OAc] and [C 4 mim][OAc], respectively. These results indicate that S. pombe showed best performance for alcoholic fermentation from sugars released from pretreated biomass by ILs.","doi":"10.1007/s12010-018-2788-1","authors":"Tura A, Fontana RC, Camassola M","authors_abbrev":"Tura A et al.","pubmed_publication_date":"Dec 2018","pubmed_entrez_date":"2018-05-26","publication_year":"2018","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2018-05-30 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20074552","title":"Formation of C-terminally truncated version of the Taz1 protein employs cleavage-box structure in mRNA.","citation":"Biochem Biophys Res Commun 2010 Feb 12;392(3):391-6","abstract":"When expressed in various hosts the taz1(+) gene encoding the fission yeast telomere-binding protein produces two forms of polypeptides: full-length (Taz1p) and truncated (Taz1pDeltaC) version lacking almost entire Myb-domain. Whereas Taz1p binds telomeric DNA in vitro, Taz1pDeltaC forms long filaments unable of DNA binding. The formation of Taz1pDeltaC is a result of neither site-specific proteolysis, nor premature termination of transcription. In silico analysis of the taz1(+) RNA transcript revealed a stem-loop structure at the site of cleavage (cleavage box; CB). In order to explore whether it possesses inherent destabilizing effects, we cloned CB sequence into the open reading frame (ORF) of glutathione-S-transferase (GST) and observed that when expressed in Escherichia coli the engineered gene produced two forms of the reporter protein. The formation of the truncated version of GST was abolished, when CB was replaced with recoded sequence containing synonymous codons thus indicating that the truncation is based on structural properties of taz1(+) mRNA.","doi":"10.1016/j.bbrc.2010.01.033","authors":"Gunisova S, Bartosova Z, Kramara J, Nosek J, Tomaska L","authors_abbrev":"Gunisova S et al.","pubmed_publication_date":"12 Feb 2010","pubmed_entrez_date":"2010-01-16","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.07c"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:10671561","title":"Structure and activity associated with multiple forms of Schizosaccharomyces pombe DNA polymerase delta.","citation":"J Biol Chem 2000 Feb 18;275(7):5153-62","abstract":"DNA polymerase delta (Pol delta) isolated from Schizosaccharomyces pombe (sp) consists of at least four subunits, Pol3, Cdc1, Cdc27, and Cdm1. We have reconstituted the four-subunit complex by simultaneously expressing these polypeptides in baculovirus-infected insect cells. The properties of the purified cloned spPol delta were identical to the native spPol delta isolated from S. pombe cells. In addition, we also isolated a three-subunit complex containing Pol3, Cdc1, and Cdm1. Both three- and four-subunit complexes required replication factor C and proliferating cell nuclear antigen for DNA replication. However, in the presence of low levels of polymerase complexes, the three-subunit complex was less efficient than the four-subunit complex in supporting DNA replication. The inefficient synthesis of DNA by the three-subunit complex can be remedied by the addition of Cdc27, the subunit missing in the three-subunit complex. Gel filtration analysis demonstrated that the three-subunit complex is a monomer of the heterotrimer (Pol3, Cdc1, and Cdm1) and that the four-subunit complex is a dimer of the heterotetramer (Pol3, Cdc1, Cdc27, and Cdm1), similar to the structure of native spPol delta. We have further shown that Cdc1 and Cdc27 interact to form a heterodimeric complex. Gel filtration studies indicate that the structure of this complex is dimeric. These observations suggest that the Cdc27 subunit may play an important role contributing to the dimerization of Pol delta.","authors":"Zuo S, Bermudez V, Zhang G, Kelman Z, Hurwitz J","authors_abbrev":"Zuo S et al.","pubmed_publication_date":"18 Feb 2000","pubmed_entrez_date":"2000-02-15","publication_year":"2000","canto_session_key":"8906e563e3e59f46","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-04-22 15:28:24","canto_approved_date":"2019-10-17 10:05:32","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-04-22 15:28:13","canto_added_date":"2012-02-24 05:52:20","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC27E2.05","SPBC336.04","SPBC12D12.02c","SPBC1734.02c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-04-22"},{"uniquename":"PMID:8207058","title":"The Schizosaccharomyces pombe cdc3+ gene encodes a profilin essential for cytokinesis.","citation":"J Cell Biol 1994 Jun;125(6):1289-301","abstract":"The fission yeast Schizosaccharomyces pombe divides by medial fission and, like many higher eukaryotic cells, requires the function of an F-actin contractile ring for cytokinesis. In S. pombe, a class of cdc- mutants defective for cytokinesis, but not for DNA replication, mitosis, or septum synthesis, have been identified. In this paper, we present the characterization of one of these mutants, cdc3-124. Temperature shift experiments reveal that mutants in cdc3 are incapable of forming an F-actin contractile ring. We have molecularly cloned cdc3 and used the cdc3+ genomic DNA to create a strain carrying a cdc3 null mutation by homologous recombination in vivo. Cells bearing a cdc3-null allele are inviable. They arrest the cell cycle at cytokinesis without forming a contractile ring. DNA sequence analysis of the cdc3+ gene reveals that it encodes profilin, an actin-monomer-binding protein. In light of recent studies with profilins, we propose that Cdc3-profilin plays an essential role in cytokinesis by catalyzing the formation of the F-actin contractile ring. Consistent with this proposal are our observations that Cdc3-profilin localizes to the medial region of the cell where the F-actin contractile ring forms, and that it is essential for F-actin ring formation. Cells overproducing Cdc3-profilin become elongated, dumbbell shaped, and arrest at cytokinesis without any detectable F-actin staining. This effect of Cdc3-profilin overproduction is relieved by introduction of a multicopy plasmid carrying the actin encoding gene, act1+. We attribute these effects to potential sequestration of actin monomers by profilin, when present in excess.","authors":"Balasubramanian MK, Hirani BR, Burke JD, Gould KL","authors_abbrev":"Balasubramanian MK et al.","pubmed_publication_date":"Jun 1994","pubmed_entrez_date":"1994-06-01","publication_year":"1994","canto_session_key":"141ca8ee8d8465c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2015-01-09 17:30:07","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-07-30 12:26:01","canto_added_date":"2012-02-24 05:54:30","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":16,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32H8.12c","SPAC4A8.15c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-07-30"},{"uniquename":"PMID:2227411","title":"Human cDNAs encoding homologs of the small p34Cdc28/Cdc2-associated protein of Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Genes Dev 1990 Aug;4(8):1332-44","abstract":"The Cks1 protein is a component of the Cdc28 protein kinase in the budding yeast Saccharomyces cerevisiae. This paper reports the cloning of two homologs of the S. cerevisiae CKS1 gene from human cells. These homologs, CKShs1 and CKShs2, both encode proteins of 79 amino acids that share considerable homology at the amino acid level with the products of CKS1 from S. cerevisiae and suc1+ from the fission yeast Schizosaccharomyces pombe. Both human homologs are capable of rescuing a null mutation of the S. cerevisiae CKS1 gene when expressed from the S. cerevisiae GAL1 promoter. S. pombe suc1+ expressed from the GAL1 promoter is also capable of rescuing a S. cerevisiae cks1 null mutation. Ckshs1 or Ckshs2 protein linked to Sepharose beads can bind the Cdc28/Cdc2 protein kinase from both S. cerevisiae and human cells. The CKShs1 and CKShs2 mRNAs are expressed in different patterns through the cell cycle in HeLa cells, which may reflect specialized roles for the encoded proteins.","authors":"Richardson HE, Stueland CS, Thomas J, Russell P, Reed SI","authors_abbrev":"Richardson HE et al.","pubmed_publication_date":"Aug 1990","pubmed_entrez_date":"1990-08-01","publication_year":"1990","canto_session_key":"1411e304c9b04d6a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-03-03 13:27:30","canto_session_submitted_date":"2012-03-03 13:27:07","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-03-03"},{"uniquename":"PMID:34347309","title":"TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins.","citation":"Proteins 2022 Jan;90(1):164-175","abstract":"TMEM106B is an integral membrane protein of late endosomes and lysosomes involved in neuronal function, its overexpression being associated with familial frontotemporal lobar degeneration, and point mutation linked to hypomyelination. It has also been identified in multiple screens for host proteins required for productive SARS-CoV-2 infection. Because standard approaches to understand TMEM106B at the sequence level find no homology to other proteins, it has remained a protein of unknown function. Here, the standard tool PSI-BLAST was used in a nonstandard way to show that the lumenal portion of TMEM106B is a member of the late embryogenesis abundant-2 (LEA-2) domain superfamily. More sensitive tools (HMMER, HHpred, and trRosetta) extended this to predict LEA-2 domains in two yeast proteins. One is Vac7, a regulator of PI(3,5)P 2  production in the degradative vacuole, equivalent to the lysosome, which has a LEA-2 domain in its lumenal domain. The other is Tag1, another vacuolar protein, which signals to terminate autophagy and has three LEA-2 domains in its lumenal domain. Further analysis of LEA-2 structures indicated that LEA-2 domains have a long, conserved lipid-binding groove. This implies that TMEM106B, Vac7, and Tag1 may all be lipid transfer proteins in the lumen of late endocytic organelles.","doi":"10.1002/prot.26201","authors":"Levine TP","authors_abbrev":"Levine TP","pubmed_publication_date":"Jan 2022","pubmed_entrez_date":"2021-08-04","publication_year":"2022","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:22407","SPBP8B7.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:2311128","title":"Construction of an h+S strain of Schizosaccharomyces pombe.","citation":"Curr Genet 1990 Jan;17(1):13-9","abstract":"By spontaneous in vivo integration of a mat2:1 degrees plasmid, containing a Plus (P) cassette, into an h-L MT region of Schizosaccharomyces pombe an h+ strain was obtained which neither mutates to h- nor to h90. Southern blotting showed that it possesses the same mating-type (MT) configuration as h-S except that P information resides in both cassettes. Therefore the strain was called h+S. By crossing h+S with the h- strain LK42 of Engelke et al. (1987) it was possible to obtain h- recombinants with the MT configuration mat1:1(M)smt-o-L-mat2:3(P). Because of the totally defective smt signal (smt-o) in these recombinants no MT switching occurs, so that M information is conserved in mat1:1; furthermore the cassette mat2:3(P) is not expressed like in strains with a K region. This proves that the K region does not cause the silencing of mat2:3(P).","authors":"Heim L","authors_abbrev":"Heim L","pubmed_publication_date":"Jan 1990","pubmed_entrez_date":"1990-01-01","publication_year":"1990","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26062005","title":"Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition.","citation":"Biochemistry 2015 Jul 07;54(26):4097-111","abstract":"N-Glycans are modified as part of a quality control mechanism during glycoprotein folding in the endoplasmic reticulum (ER). Glucosidase II (GII) plays a critical role by generating monoglucosylated glycans that are recognized by lectin chaperones, calnexin and calreticulin. To understand how the hydrolytic activity of GIIα is enhanced by the mannose 6-phosphate receptor (MPR) homology domain (MRH domain) of its β subunit, we now report a 1.6 Å resolution crystal structure of the MRH domain of GIIβ bound to mannose. A comparison of ligand-bound and unbound structures reveals no major difference in their overall fold, but rather a repositioning of side chains throughout the binding pocket, including Y372. Mutation of Y372 inhibits GII activity, demonstrating an important role for Y372 in regulating GII activity. Comparison of the MRH domains of GIIβ, MPRs, and the ER lectin OS-9 identified conserved residues that are critical for the structural integrity and architecture of the carbohydrate binding pocket. As shown by nuclear magnetic resonance spectroscopy, mutations of the primary binding pocket residues and adjacent W409, all of which inhibit the activity of GII both in vitro and in vivo, do not cause a significant change in the overall fold of the GIIβ MRH domain but impact locally the stability of the binding pocket. W409 does not directly contact mannose; rather, its indole ring is stabilized by binding into a hydrophobic pocket of an adjacent crystallographic neighbor. This suggests that W409 interacts with a hydrophobic region of the GIIβ or GIIα subunit to modulate its effect on GII activity.","doi":"10.1021/acs.biochem.5b00256","authors":"Olson LJ, Orsi R, Peterson FC, Parodi AJ, Kim JJ, D'Alessio C, Dahms NM","authors_abbrev":"Olson LJ et al.","pubmed_publication_date":"07 Jul 2015","pubmed_entrez_date":"2015-06-11","publication_year":"2015","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-02-14 04:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC825.02"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"4xqm","gene_chains":[{"gene_uniquename":"SPCC825.02","chain":"A","position":"380-473"}],"title":"Crystal structure of the MRH domain of Glucosidase II beta bound to mannose","entry_authors":"Olson LJ,Dahms NM,Kim J-JP","entry_authors_abbrev":"Olson LJ et al.","reference_uniquename":"PMID:26062005","experimental_method":"X-ray","resolution":"1.625"}]},{"uniquename":"PMID:12153582","title":"Molecular interaction of neutral trehalase with other enzymes of trehalose metabolism in the fission yeast Schizosaccharomyces pombe.","citation":"Eur J Biochem 2002 Aug;269(15):3847-55","abstract":"Trehalose metabolism is an essential component of the stress response in yeast cells. In this work we show that the products of the principal genes involved in trehalose metabolism in Schizosaccharomyces pombe, tps1+ (coding for trehalose-6-P synthase, Tps1p), ntp1+ (encoding neutral trehalase, Ntp1p) and tpp1+ (that codes for trehalose-6-P phosphatase, Tpp1p), interact in vitro with each other and with themselves to form protein complexes. Disruption of the gene tps1+ blocks the activation of the neutral trehalase induced by heat shock but not by osmotic stress. We propose that this association may reflect the Tps1p-dependent requirement for thermal activation of trehalase. Data reported here indicate that following a heat shock the enzyme activity of trehalase is associated with Ntp1p dimers or trimers but not with either Ntp1p monomers or with complexes involving Tps1p. These results raise the possibility that heat shock and osmotic stress activate trehalase differentially by acting in the first case through an specific mechanism involving Tps1p-Ntp1p complexes. This study provides the first evidence for the participation of the catabolic enzyme trehalase in the structural framework of a regulatory macromolecular complex containing trehalose-6-P synthase in the fission yeast.","authors":"Soto T, Franco A, Padmanabhan S, Vicente-Soler J, Cansado J, Gacto M","authors_abbrev":"Soto T et al.","pubmed_publication_date":"Aug 2002","pubmed_entrez_date":"2002-08-03","publication_year":"2002","canto_session_key":"3f5975a0627e25e2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-09-12 06:33:31","canto_approved_date":"2024-02-16 18:27:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-09-10 13:07:03","canto_added_date":"2012-02-24 05:51:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.15c","SPAC328.03","SPBC660.07","SPBC1A4.05"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2013-09-12"},{"uniquename":"PMID:42173869","title":"Recognition and silencing of a new transposable element.","citation":"Nat Commun 2026 May 22;","abstract":"Genomes constantly face threats from transposable elements (TEs) and other genomic parasites. While the silencing of existing TE has been well studied, little is known about how cells recognize new invading TEs that they have not previously encountered. Here we explore this question by inserting foreign sequences into S. pombe. Our data revealed that the newly invading TE tj1 is recognized and targeted for silencing by RNAi and heterochromatin. The efficiency of recognition, as well as the degree and stability of silencing, depends on the copy number and insertion location of the TE. We demonstrated that RNA, rather than DNA, is sensed, and that the efficiency of TE recognition correlates with levels of RNA antisense to the TE, generated from upstream transcripts. We also show that various genes of non-transposable nature can initiate silencing. Our data show that silencing may not require recognition of specific elements in the transposon by the host defense systems, and suggest that disruption of host transcription patterns triggers recognition of TE.","doi":"10.1038/s41467-026-72981-w","authors":"Salvi L, Yan Y, Halic M","authors_abbrev":"Salvi L et al.","pubmed_publication_date":"22 May 2026","pubmed_entrez_date":"2026-05-22","publication_year":"2026","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2026-05-23 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23640107","title":"Screening for long-lived genes identifies Oga1, a guanine-quadruplex associated protein that affects the chronological lifespan of the fission yeast Schizosaccharomyces pombe.","citation":"Mol Genet Genomics 2013 Jun;288(5-6):285-95","abstract":"Schizosaccharomyces pombe and Saccharomyces cerevisiae are excellent model organisms to study lifespan. We conducted screening to identify novel genes that, when overexpressed, extended the chronological lifespan of fission yeast. We identified seven genes, among which we focused on SPBC16A3.08c. The gene product showed similarity to Ylr150w of S. cerevisiae, which has affinity for guanine-quadruplex nucleic acids (G4). The SPBC16A3.08c product associated with G4 in vitro and complemented the phenotype of an S. cerevisiae Ylr150w deletion mutant. From these results, we proposed that SPBC16A3.08c encoded for a functional homolog of Ylr150w, which we designated ortholog of G4-associated protein (oga1 (+)). oga1 (+) overexpression extended the chronological lifespan and also decreased mating efficiency and caused both high and low temperature-sensitive growth. Deleting oga1 (+) resulted in caffeine-sensitive and canavanine-resistant phenotypes. Based on these results, we discuss the function of Oga1 on the chronological lifespan of fission yeast.","doi":"10.1007/s00438-013-0748-6","authors":"Ohtsuka H, Ogawa S, Kawamura H, Sakai E, Ichinose K, Murakami H, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Jun 2013","pubmed_entrez_date":"2013-05-04","publication_year":"2013","canto_session_key":"6c14340df9876d6b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-05-23 15:35:00","canto_approved_date":"2026-03-30 09:21:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-09 08:42:48","canto_added_date":"2013-05-07 15:34:21","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC30D10.10c","SPBC30D10.13c","SPBC337.09","SPBC725.10","SPBC28F2.03","SPBC16A3.08c","SPAC1556.02c","SPCC18.02"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2013-05-23"},{"uniquename":"PMID:37572670","title":"A peroxiredoxin-P38 MAPK scaffold increases MAPK activity by MAP3K-independent mechanisms.","citation":"Mol Cell 2023 Sep 07;83(17):3140-3154.e7","abstract":"Peroxiredoxins (Prdxs) utilize reversibly oxidized cysteine residues to reduce peroxides and promote H 2 O 2  signal transduction, including H 2 O 2 -induced activation of P38 MAPK. Prdxs form H 2 O 2 -induced disulfide complexes with many proteins, including multiple kinases involved in P38 MAPK signaling. Here, we show that a genetically encoded fusion between a Prdx and P38 MAPK is sufficient to hyperactivate the kinase in yeast and human cells by a mechanism that does not require the H 2 O 2 -sensing cysteine of the Prdx. We demonstrate that a P38-Prdx fusion protein compensates for loss of the yeast scaffold protein Mcs4 and MAP3K activity, driving yeast into mitosis. Based on our findings, we propose that the H 2 O 2 -induced formation of Prdx-MAPK disulfide complexes provides an alternative scaffold and signaling platform for MAPKK-MAPK signaling. The demonstration that formation of a complex with a Prdx is sufficient to modify the activity of a kinase has broad implications for peroxide-based signal transduction in eukaryotes.","doi":"10.1016/j.molcel.2023.07.018","authors":"Cao M, Day AM, Galler M, Latimer HR, Byrne DP, Foy TW, Dwyer E, Bennett E, Palmer J, Morgan BA, Eyers PA, Veal EA","authors_abbrev":"Cao M et al.","pubmed_publication_date":"07 Sep 2023","pubmed_entrez_date":"2023-08-12","publication_year":"2023","canto_session_key":"83cfcf15c86bcfbb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elizabeth Veal","canto_first_approved_date":"2024-01-26 14:23:52","canto_approved_date":"2025-10-12 21:04:00","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-01-22 15:21:40","canto_added_date":"2023-08-14 00:15:05","annotation_curators":[{"name":"Elizabeth Veal","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC7D4.07c","SPBC887.10","SPAC26F1.10c","SPAC24B11.06c","SPCC576.03c","SPBC409.07c","SPAC19D5.01","HGNC:9353","HGNC:9352"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2024-01-26"},{"uniquename":"PMID:24146635","title":"Hsp70-Hsp40 chaperone complex functions in controlling polarized growth by repressing Hsf1-driven heat stress-associated transcription.","citation":"PLoS Genet 2013;9(10):e1003886","abstract":"How the molecular mechanisms of stress response are integrated at the cellular level remains obscure. Here we show that the cellular polarity machinery in the fission yeast Schizosaccharomyces pombe undergoes dynamic adaptation to thermal stress resulting in a period of decreased Cdc42 activity and altered, monopolar growth. Cells where the heat stress-associated transcription was genetically upregulated exhibit similar growth patterning in the absence of temperature insults. We identify the Ssa2-Mas5/Hsp70-Hsp40 chaperone complex as repressor of the heat shock transcription factor Hsf1. Cells lacking this chaperone activity constitutively activate the heat-stress-associated transcriptional program. Interestingly, they also exhibit intermittent monopolar growth within a physiological temperature range and are unable to adapt to heat stress. We propose that by negatively regulating the heat stress-associated transcription, the Ssa2-Mas5 chaperone system could optimize cellular growth under different temperature regiments.","doi":"10.1371/journal.pgen.1003886","authors":"Vjestica A, Zhang D, Liu J, Oliferenko S","authors_abbrev":"Vjestica A et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-10-23","publication_year":"2013","canto_session_key":"c29f51c4cc86096d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Aleksandar Vjestica","canto_first_approved_date":"2018-10-15 12:39:04","canto_approved_date":"2025-09-03 18:09:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-30 15:15:27","canto_added_date":"2013-11-01 02:19:01","annotation_curators":[{"name":"Aleksandar Vjestica","community_curator":true,"annotation_count":7,"orcid":null,"file_type":null,"file_name":null},{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":71,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.03","SPBC28E12.03","SPAC2F7.03c","SPCC1919.10c","SPCC1223.06","SPAC926.04c","SPAC2E12.02","SPAC13G7.02c","SPCC895.05","SPBC19G7.05c","SPBC1706.01","SPAC16E8.09","SPCC830.07c","SPBC1734.11","SPBC16D10.08c","SPAC24H6.09","SPCC1739.13","SPCC1235.10c"],"gene_count":18,"ltp_gene_count":11,"approved_date":"2018-10-15"},{"uniquename":"PMID:23255127","title":"An Atg10-like E2 enzyme is essential for cell cycle progression but not autophagy in Schizosaccharomyces pombe.","citation":"Cell Cycle 2013 Jan 15;12(2):271-7","abstract":"Many proteins involved in autophagy have been identified in the yeast Saccharomyces cerevisiae. For example, Atg3 and Atg10 are two E2 enzymes that facilitate the conjugation of the ubiquitin-like proteins (Ubls) Atg8 and Atg12, respectively. Here, we describe the identification and characterization of the predicted Atg10 homolog (SpAtg10) of the evolutionarily distant Schizosaccharomyces pombe. Unexpectedly, SpAtg10 is not essential for autophagy. Instead, we find that SpAtg10 is essential for normal cell cycle progression, and for responses to various stress conditions that perturb the cell cycle, independently of Atg12 conjugation. Taken together, our data indicate that autophagic Ubl conjugation pathways differ between eukaryotes and, furthermore, that enzymes such as Atg10 may have additional functions in controlling key cellular processes such as cell cycle progression. Atg10-related proteins are found from yeast to humans, and, thus, this study has implications for understanding the functions of this protein family in Ubl conjugation in eukaryotes.","doi":"10.4161/cc.23055","authors":"Flanagan MD, Whitehall SK, Morgan BA","authors_abbrev":"Flanagan MD et al.","pubmed_publication_date":"15 Jan 2013","pubmed_entrez_date":"2012-12-21","publication_year":"2013","canto_session_key":"c9924d01b60c447e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11864615","title":"RAC protein directs the complete removal of the 3' external transcribed spacer by the Pac1 nuclease.","citation":"Mol Cell 2002 Feb;9(2):433-7","abstract":"In Schizosaccharomyces pombe, interdependency in rRNA processing is mediated by a large protein complex (RAC) which contains independent binding sites for each of the transcribed spacers. The RAC complex exhibits no nuclease activity but dramatically alters the efficiency and specificity of the Pac1 nuclease, leading to the complete removal of the 3' ETS. Furthermore, the affinity of RAC protein for mutant 3' ETS correlates closely with in vivo effects on rRNA processing, and changes which disrupt RAC protein binding also inhibit Pac1 nuclease cleavage at the 3' end of the 25S rRNA sequence. The observations indicate that, in the presence of the RAC protein/3' ETS complex, cleavage by the RNase III-like homolog is not restricted to the known intermediate sites but also is directed at the 3' end of the 25S rRNA.","authors":"Spasov K, Perdomo LI, Evakine E, Nazar RN","authors_abbrev":"Spasov K et al.","pubmed_publication_date":"Feb 2002","pubmed_entrez_date":"2002-02-28","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPC05887","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24120641","title":"Dip1 defines a class of Arp2/3 complex activators that function without preformed actin filaments.","citation":"Curr Biol 2013 Oct 21;23(20):1990-8","abstract":"Arp2/3 complex is a key actin cytoskeletal regulator that creates branched actin filament networks in response to cellular signals. WASP-activated Arp2/3 complex assembles branched actin networks by nucleating new filaments from the sides of pre-existing ones. WASP-mediated activation requires seed filaments, to which the WASP-bound Arp2/3 complex can bind to form branches, but the source of the first substrate filaments for branching is unknown.\nHere we show that Dip1, a member of the WISH/DIP/SPIN90 family of actin regulators, potently activates Arp2/3 complex without preformed filaments. Unlike other Arp2/3 complex activators, Dip1 does not bind actin monomers or filaments, and it interacts with the complex using a non-WASP-like binding mode. In addition, Dip1-activated Arp2/3 complex creates linear instead of branched actin filament networks.\nOur data show the mechanism by which Dip1 and other WISH/DIP/SPIN90 proteins can provide seed filaments to Arp2/3 complex to serve as master switches in initiating branched actin assembly. This mechanism is distinct from other known activators of Arp2/3 complex.","doi":"10.1016/j.cub.2013.08.029","authors":"Wagner AR, Luan Q, Liu SL, Nolen BJ","authors_abbrev":"Wagner AR et al.","pubmed_publication_date":"21 Oct 2013","pubmed_entrez_date":"2013-10-15","publication_year":"2013","canto_session_key":"c74c34c1101ef487","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-10-02 00:32:50","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC630.03","SPBC32H8.12c","SPBC24C6.10c","SPAC4F10.15c"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:5516425","title":"Mitotic mapping of Schizosaccharomyces pombe.","citation":"Genet Res 1970 Oct 02;16(2):127-44","abstract":"","authors":"Flores da Cunha M","authors_abbrev":"Flores da Cunha M","pubmed_publication_date":"02 Oct 1970","pubmed_entrez_date":"1970-10-02","publication_year":"1970","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26832665","title":"The effect of the cwf14 gene of fission yeast on cell wall integrity is associated with rho1.","citation":"J Microbiol 2016 Feb;54(2):98-105","abstract":"In all eukaryotic organisms, a wide range of morphologies are responsible for critical cellular function and development. In particular, the Rho GTPases, which are highly conserved from yeast to mammals, are key molecules in signaling pathways that control cell polarity processes and cell wall biosynthesis, which are fundamental aspects of morphogenesis. Therefore, using haploinsufficiency deletion mutants of the fission yeast Schizosaccharomyces pombe, we screened the slow-growing mutants and their morphogenesis, specifically focusing on regulation of their Rho GTPases. Based on this screening, we found that the cwf14 mutant of S. pombe exhibited the slow growth and abnormal phenotypes with an elongated cell shape and thicker cell wall when compared with wild-type cells. In particular, cells with the cwf14 deletion showed excessive Rho1 expression. However, the wildtype strain with ectopically expressed Rho1 did not exhibited any significant change in the level of cwf14, suggesting that cwf14 may act on the upstream of Rho1. Furthermore, the cells with a cwf14 deletion also have increased sensitivity to β-glucanase, a cell wall-digesting enzyme, which is also seen in Rho1-overexpressing cells. Overall, our results suggest that the cwf14 plays a key role in fission yeast morphogenesis and cell wall biosynthesis and/or degradation possibly via the regulation of Rho1 expression.","doi":"10.1007/s12275-016-5569-y","authors":"Kim DU, Maeng S, Lee H, Nam M, Lee SJ, Hoe KL","authors_abbrev":"Kim DU et al.","pubmed_publication_date":"Feb 2016","pubmed_entrez_date":"2016-02-03","publication_year":"2016","canto_session_key":"a85d49b0fd79feb2","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-02-04 01:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC24C6.11"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38180730","title":"LAMMER Kinase Governs the Expression and Cellular Localization of Gas2, a Key Regulator of Flocculation in Schizosaccharomyces pombe.","citation":"J Microbiol 2024 Jan 05;","abstract":"It was reported that LAMMER kinase in Schizosaccharomyces pombe plays an important role in cation-dependent and galactose-specific flocculation. Analogous to other flocculating yeasts, when cell wall extracts of the Δlkh1 strain were treated to the wild-type strain, it displayed flocculation. Gas2, a 1,3-β-glucanosyl transferase, was isolated from the EDTA-extracted cell-surface proteins in the Δlkh1 strain. While disruption of the gas2 +  gene was not lethal and reduced the flocculation activity of the ∆lkh1 strain, the expression of a secreted form of Gas2, in which the GPI anchor addition sequences had been removed, conferred the ability to flocculate upon the WT strain. The Gas2-mediated flocculation was strongly inhibited by galactose but not by glucose. Immunostaining analysis showed that the cell surface localization of Gas2 was crucial for the flocculation of fission yeast. In addition, we identified the regulation of mbx2 +  expression by Lkh1 using RT-qPCR. Taken together, we found that Lkh1 induces asexual flocculation by regulating not only the localization of Gas2 but also the transcription of gas2 +  through Mbx2.","doi":"10.1007/s12275-023-00097-7","authors":"Kang WH, Park YD, Lim JY, Park HM","authors_abbrev":"Kang WH et al.","pubmed_publication_date":"05 Jan 2024","pubmed_entrez_date":"2024-01-05","publication_year":"2024","canto_session_key":"8214ab1ca2d0574c","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-01-06 00:25:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1D4.11c","SPBC29A10.08"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:38392827","title":"Processes Controlling the Contractile Ring during Cytokinesis in Fission Yeast, Including the Role of ESCRT Proteins.","citation":"J Fungi (Basel) 2024 Feb 15;10(2)","abstract":"Cytokinesis, as the last stage of the cell division cycle, is a tightly controlled process amongst all eukaryotes, with defective division leading to severe cellular consequences and implicated in serious human diseases and conditions such as cancer. Both mammalian cells and the fission yeast  Schizosaccharomyces pombe  use binary fission to divide into two equally sized daughter cells. Similar to mammalian cells, in  S. pombe , cytokinetic division is driven by the assembly of an actomyosin contractile ring (ACR) at the cell equator between the two cell tips. The ACR is composed of a complex network of membrane scaffold proteins, actin filaments, myosin motors and other cytokinesis regulators. The contraction of the ACR leads to the formation of a cleavage furrow which is severed by the endosomal sorting complex required for transport (ESCRT) proteins, leading to the final cell separation during the last stage of cytokinesis, the abscission. This review describes recent findings defining the two phases of cytokinesis in  S. pombe : ACR assembly and constriction, and their coordination with septation. In summary, we provide an overview of the current understanding of the mechanisms regulating ACR-mediated cytokinesis in  S. pombe  and emphasize a potential role of ESCRT proteins in this process.","doi":"10.3390/jof10020154","authors":"Rezig IM, Yaduma WG, McInerny CJ","authors_abbrev":"Rezig IM et al.","pubmed_publication_date":"15 Feb 2024","pubmed_entrez_date":"2024-02-23","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-02-24 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16079916","title":"Genomewide analysis of nucleosome density histone acetylation and HDAC function in fission yeast.","citation":"EMBO J 2005 Aug 17;24(16):2906-18","abstract":"We have conducted a genomewide investigation into the enzymatic specificity, expression profiles, and binding locations of four histone deacetylases (HDACs), representing the three different phylogenetic classes in fission yeast (Schizosaccharomyces pombe). By directly comparing nucleosome density, histone acetylation patterns and HDAC binding in both intergenic and coding regions with gene expression profiles, we found that Sir2 (class III) and Hos2 (class I) have a role in preventing histone loss; Clr6 (class I) is the principal enzyme in promoter-localized repression. Hos2 has an unexpected role in promoting high expression of growth-related genes by deacetylating H4K16Ac in their open reading frames. Clr3 (class II) acts cooperatively with Sir2 throughout the genome, including the silent regions: rDNA, centromeres, mat2/3 and telomeres. The most significant acetylation sites are H3K14Ac for Clr3 and H3K9Ac for Sir2 at their genomic targets. Clr3 also affects subtelomeric regions which contain clustered stress- and meiosis-induced genes. Thus, this combined genomic approach has uncovered different roles for fission yeast HDACs at the silent regions in repression and activation of gene expression.","authors":"Wirén M, Silverstein RA, Sinha I, Walfridsson J, Lee HM, Laurenson P, Pillus L, Robyr D, Grunstein M, Ekwall K","authors_abbrev":"Wirén M et al.","pubmed_publication_date":"17 Aug 2005","pubmed_entrez_date":"2005-08-05","publication_year":"2005","canto_session_key":"d30dca7bfe4b2d3d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-02-12 16:15:16","canto_approved_date":"2024-09-26 09:02:29","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2021-02-12 16:14:54","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":24,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Pascal Carme","community_curator":false,"annotation_count":1,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC800.03","SPAC3G9.07c","SPBC36.05c","SPBC16D10.07c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2021-02-12"},{"uniquename":"PMID:20544037","title":"WD40 domain divergence is important for functional differences between the fission yeast Tup11 and Tup12 co-repressor proteins.","citation":"PLoS One 2010 Jun 08;5(6):e11009","abstract":"We have previously demonstrated that subsets of Ssn6/Tup target genes have distinct requirements for the Schizosaccharomyces pombe homologs of the Tup1/Groucho/TLE co-repressor proteins, Tup11 and Tup12. The very high level of divergence in the histone interacting repression domains of the two proteins suggested that determinants distinguishing Tup11 and Tup12 might be located in this domain. Here we have combined phylogenetic and structural analysis as well as phenotypic characterization, under stress conditions that specifically require Tup12, to identify and characterize the domains involved in Tup12-specific action. The results indicate that divergence in the repression domain is not generally relevant for Tup12-specific function. Instead, we show that the more highly conserved C-terminal WD40 repeat domain of Tup12 is important for Tup12-specific function. Surface amino acid residues specific for the WD40 repeat domain of Tup12 proteins in different fission yeasts are clustered in blade 3 of the propeller-like structure that is characteristic of WD40 repeat domains. The Tup11 and Tup12 proteins in fission yeasts thus provide an excellent model system for studying the functional divergence of WD40 repeat domains.","doi":"10.1371/journal.pone.0011009","authors":"Ferreira ME, Berndt KD, Nilsson J, Wright AP","authors_abbrev":"Ferreira ME et al.","pubmed_publication_date":"08 Jun 2010","pubmed_entrez_date":"2010-06-15","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC18B11.10","SPAC630.14c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:25117315","title":"A potential protective role for thiamine in glucose-driven oxidative stress.","citation":"Genet Mol Res 2014 Jul 25;13(3):5582-93","abstract":"The relationship between glucose repression and the oxidative stress response was investigated in Schizosaccharomyces pombe wild type cells (972h(-)) and glucose repression resistant mutant type cells (ird11). We aimed to reveal the mechanism of simultaneous resistance to glucose repression and oxidative stress in ird11 mutants. Compared to the wild type, the expression of the sty1 gene was not altered in the ird11 mutant under normal growth conditions, but decreased after exposure to H2O2. This effect was clearly explained by the immunoblotting results, which showed elevated levels of a much more stable phosphorylated form of Sty1 mitogen-activated protein kinase in the ird11 mutant. Increased ght3 gene expression levels were also found, which may play a role in protecting the ird11 mutant from the deleterious effects of oxidative stress. In addition, decreased expression levels of glycolytic enzyme enolase- and thiamine synthesis/transport-related genes were detected. This might have resulted from the flux redirection toward mitochondrial respiration, which would enhance NADPH generation to prevent the high reactive oxygen species accumulation that is generated by respiration. Some evidence supported a flux shift toward fermentation as well as respiration. We conclude that a defect in the glucose-sensing signaling pathway in ird11 mutants likely causes erroneous low glucose-sensing signaling and high ATP production. This most likely occurs because high glucose availability in the medium induces an impairment in the respiratory chain and fermentation balance in these cells, which might explain the glucose repression and oxidative stress resistance in ird11 compared to the wild type.","doi":"10.4238/2014.July.25.13","authors":"Palabiyik B, Jafari Ghods F, Onay Ucar E","authors_abbrev":"Palabiyik B et al.","pubmed_publication_date":"25 Jul 2014","pubmed_entrez_date":"2014-08-14","publication_year":"2014","canto_session_key":"8c4a5ea8b73d4404","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2016-07-14 14:17:42","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-07-12 08:18:56","canto_added_date":"2014-08-16 00:15:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBP4G3.02","SPAC1006.09","SPAC23H4.10c","SPBP8B7.18c","SPBC17A3.06","SPBC19C2.03","SPBC354.12","SPCC1259.09c","SPBPB21E7.01c","SPAC17A2.01","SPAPYUG7.04c","SPAC513.02","SPBC3E7.12c","SPAC22A12.05","SPAC513.05","SPAC22F8.05","SPBPB2B2.12c","SPCC1223.02","SPAC1F8.01","SPCC548.06c","SPAC4G8.13c","SPAC19G12.04","SPBC26H8.01","SPAC23A1.03","SPCC18B5.05c","SPBC25B2.02c","SPAC5H10.06c","SPBP16F5.03c","SPCC1672.03c","SPAC13F5.03c","SPAC186.09","SPAC1039.11c","SPBC8E4.04"],"gene_count":33,"ltp_gene_count":0,"approved_date":"2016-07-12"},{"uniquename":"PMID:11403492","title":"Bioskin as an affinity matrix for the separation of glycoproteins.","citation":"J Chromatogr A 2001 May 11;917(1-2):55-61","abstract":"Bioskin is a natural product produced by a mixed culture of Acetobacter xylinum, Saccharomyces cerevisiae and S. pombe cultured on media containing sucrose. It is of fibrillar nature able to retain some proteins, such as cytochrome c, by adsorption, and mainly composed of glucosamine and N-acetyl-D-glucosamine. This makes it possible that, at an adequate pH value, proteins charged as polyanionic molecules, such as catalase, can be retained by ionic adsorption using the positively charged amino groups of the matrix. In addition, bioskin can also be used as an affinity matrix to retain glycoproteins able to perform specific affinity reactions with the amino sugars of the matrix, such as invertase, fetuin or ovalbumin. Its possible use as a chromatographic support is discussed.","authors":"Vicente C, Sebastián B, Fontaniella B, Márquez A, Xavier Filho L, Legaz ME","authors_abbrev":"Vicente C et al.","pubmed_publication_date":"11 May 2001","pubmed_entrez_date":"2001-06-14","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34674264","title":"Localization of the ubiquitin ligase Dma1 to the fission yeast contractile ring is modulated by phosphorylation.","citation":"FEBS Lett 2021 Nov;595(22):2781-2792","abstract":"The timing of cytokinesis relative to other mitotic events in the fission yeast Schizosaccharomyces pombe is controlled by the septation initiation network (SIN). During a mitotic checkpoint, the SIN is inhibited by the E3 ubiquitin ligase Dma1 to prevent chromosome mis-segregation. Dma1 dynamically localizes to spindle pole bodies (SPBs) and the contractile ring (CR) during mitosis, though its role at the CR is unknown. Here, we examined whether Dma1 phosphorylation affects its localization or function. We found that preventing Dma1 phosphorylation by substituting the six phosphosites with alanines diminished its CR localization but did not affect its mitotic checkpoint function. These studies reinforce the conclusion that Dma1 localization to the SPB is key to its role in the mitotic checkpoint.","doi":"10.1002/1873-3468.14211","authors":"Chen JS, Jones CM, Igarashi MG, Ren L, Johnson AE, Gould KL","authors_abbrev":"Chen JS et al.","pubmed_publication_date":"Nov 2021","pubmed_entrez_date":"2021-10-21","publication_year":"2021","canto_session_key":"e68d23abf86a3c7c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Junsong Chen","canto_first_approved_date":"2022-04-25 11:11:33","canto_approved_date":"2023-10-20 12:39:31","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-04-08 15:30:13","canto_added_date":"2021-10-25 00:15:04","annotation_curators":[{"name":"Junsong Chen","community_curator":true,"annotation_count":33,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":3,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPBC244.01c","SPAC23C11.16","SPAC23C11.11","SPAC17G8.10c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2022-04-25"},{"uniquename":"PMID:19336419","title":"Cotranscriptional recruitment of the nuclear poly(A)-binding protein Pab2 to nascent transcripts and association with translating mRNPs.","citation":"Nucleic Acids Res 2009 Jun;37(10):3418-30","abstract":"Synthesis of the pre-mRNA poly(A) tail in the nucleus has important consequences on the translational activity of the mature mRNA in the cytoplasm. In most eukaryotes, nuclear polyadenylation of pre-mRNAs is thought to require the nuclear poly(A)-binding protein (PABP2/PABPN1) for poly(A) tail synthesis and ultimate length control. As yet, however, the extent of the association between PABP2 and the exported mRNA remains poorly understood. Here, we used chromatin immunoprecipitation (ChIP) assays to show that the fission yeast ortholog of mammalian PABP2 (Pab2) is cotranscriptionally recruited to active genes. Notably, the association of Pab2 to genes precedes that of a typical 3'-processing/polyadenylation factor, suggesting that Pab2 recruitment during the transcription cycle precedes polyadenylation. The inclusion of an RNase step in our ChIP and immunoprecipitation assays suggests that Pab2 is cotranscriptionally recruited via nascent mRNA ribonucleoprotein (mRNPs). Tandem affinity purification coupled with mass spectrometry also revealed that Pab2 associates with several ribosomal proteins as well as general translation factors. Importantly, whereas previous results suggest that the nuclear poly(A)-binding protein is not present on cytoplasmic mRNAs, we show that fission yeast Pab2 is associated with polysomes. Our findings suggest that Pab2 is recruited to nascent mRNPs during transcription and remains associated with translated mRNPs after nuclear export.","doi":"10.1093/nar/gkp207","authors":"Lemieux C, Bachand F","authors_abbrev":"Lemieux C et al.","pubmed_publication_date":"Jun 2009","pubmed_entrez_date":"2009-04-02","publication_year":"2009","canto_session_key":"e6b059781e6820b1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-05-22 07:47:18","canto_approved_date":"2024-02-12 19:20:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-05-21 10:26:58","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":60,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16E9.12c","SPAC57A7.04c","SPBC25H2.07","SPCC584.04","SPCC622.18","SPAPB8E5.06c","SPBC18H10.12c","SPBC28F2.12","SPBC660.11","SPBC14F5.08","SPBC1105.07c","SPAC959.08","SPCC1393.03","SPAC18G6.14c","SPAC664.05","SPBC776.01","SPAC19A8.12","SPBC11G11.07","SPBC405.07","SPAC5D6.01","SPBC19G7.03c","SPBC776.09","SPCC1795.11","SPAC24C9.11","SPBC530.14c","SPAC2C4.16c","SPAC3A12.10","SPAC637.07","SPAC4G9.08c","SPBC29A3.04","SPBC1A4.07c","SPAC6G10.07","SPBC29A3.12","SPBP8B7.03c","SPAC17A5.14","SPAC6F12.16c","SPAC31G5.03","SPAC521.05","SPAC9G1.03c","SPBC16E9.13","SPBC365.03c","SPCC794.09c","SPCC970.05","SPAC6F6.07c","SPCC1682.08c","SPAPB1A10.03","SPAC890.08","SPBC1711.06","SPCC1739.01","SPBC19F8.07","SPAC24H6.07","SPCC16C4.13c","SPBC106.18","SPBC11C11.07","SPAC26A3.07c","SPBC646.04","SPCC5E4.07","SPCC576.08c","SPAC17A5.03"],"gene_count":59,"ltp_gene_count":59,"approved_date":"2013-05-22"},{"uniquename":"EMBL:SPD210","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9710608","title":"The role of fnx1, a fission yeast multidrug resistance protein, in the transition of cells to a quiescent G0 state.","citation":"Mol Cell Biol 1998 Sep;18(9):5239-46","abstract":"Most microorganisms live in conditions of nutrient limitation in their natural habitats. When exposed to these conditions they respond with physiological and morphological changes that enable them to survive. To obtain insights into the molecular mechanisms of this response a systematic genetic screen was performed to identify genes that when overexpressed can induce a starvation-like response in the yeast species Schizosaccharomyces pombe. One gene that meets these criteria, fnx1(+), induces, transcriptionally correlates with, and is required for the entry into the quiescent G0 state that is normally induced by nitrogen starvation. fnx1(+) encodes a protein with sequence similarity to the proton-driven plasma membrane transporters from the multidrug resistance group of the major facilitator superfamily of proteins. We propose that fnx1(+) plays a role in the entry into G0, possibly by facilitating the release of a signaling substance into the environment as a means of cell-to-cell communication.","authors":"Dimitrov K, Sazer S","authors_abbrev":"Dimitrov K et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-08-26","publication_year":"1998","canto_session_key":"e0dfd1b0fc3b5cce","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2017-04-12 07:07:20","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2017-04-12 07:07:11","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC285.09c","SPBC12C2.13c"],"gene_count":3,"ltp_gene_count":1,"approved_date":"2017-04-12"},{"uniquename":"PMID:2891694","title":"Mutation of a conserved glycine residue modifies the vanadate sensitivity of the plasma membrane H+-ATPase from Schizosaccharomyces pombe.","citation":"J Biol Chem 1987 Dec 25;262(36):17549-55","abstract":"The structural gene pma+1 for the H+-ATPase from the fission yeast Schizosaccharomyces pombe has been isolated and sequenced. The intron-less gene encodes for a protein of Mr = 99,769 which is 75% homologous to those of Saccharomyces cerevisiae and Neurospora crassa. The S. pombe pma+1 gene complements not only S. pombe pma-1-1 but also S. cerevisiae pma-1-4 mutants selected for in vitro vanadate-resistant ATPase activity. The sequence of the S. pombe mutant pma-1-1 allele reveals that the glycine residue 268, which is perfectly conserved in the transduction domain of all animal and fungal transport ATPases sequenced so far, is modified into an aspartate residue by the mutation. Replacement of glycine 268 by aspartate has been monitored by the appearance of a new PvuI restriction site in the mutant DNA. Mitotic cosegregation has been observed between the PvuI site and vanadate-resistant ATPase activity in a growing population of S. pombe transformants.","authors":"Ghislain M, Schlesser A, Goffeau A","authors_abbrev":"Ghislain M et al.","pubmed_publication_date":"25 Dec 1987","pubmed_entrez_date":"1987-12-25","publication_year":"1987","canto_session_key":"85e0cb1804d80d90","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2012-12-01 13:43:22","canto_approved_date":"2021-06-16 14:33:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-30 10:50:15","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1071.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-12-01"},{"uniquename":"PMID:40737086","title":"SnoBIRD: a tool to identify C/D box snoRNAs and refine their annotation across all eukaryotes.","citation":"Nucleic Acids Res 2025 Jul 19;53(14)","abstract":"Small nucleolar RNAs (snoRNAs), a group of noncoding RNAs present amongst all eukaryotes, are most extensively characterized for their regulation of ribosome biogenesis and splicing. Despite their central roles, current snoRNA annotations remain incomplete. Several eukaryote genome annotations contain few or no snoRNAs, and none distinguish expressed snoRNAs from their pseudogenes-a recently characterized snoRNA subclass with distinct features and expression levels. To address this, we developed SnoBIRD, a BERT-based C/D box snoRNA predictor trained on snoRNAs spanning all eukaryote kingdoms. We show that SnoBIRD outperforms existing tools and is the only predictor capable of identifying snoRNA pseudogenes using biologically relevant signal. Applied on the fission yeast and human genomes, we demonstrate that only SnoBIRD scales well with genome size in terms of runtime, and we identify and experimentally validate several new SnoBIRD-predicted C/D box snoRNAs. By running SnoBIRD on multiple eukaryote genomes, we identify hundreds of novel snoRNA candidates and highlight SnoBIRD's usefulness to determine the evolutionary paths of snoRNAs distributed across different species. Overall, SnoBIRD represents a user-friendly and efficient tool for reliably predicting C/D box snoRNAs and their pseudogenes across any eukaryote genome.","doi":"10.1093/nar/gkaf708","authors":"Fafard-Couture É, Boulanger C, Faucher-Giguère L, Sinagoga V, Berthoumieux M, Hedjam J, Marcel V, Durand S, Bayfield MA, Bachand F, Abou Elela S, Jacques PÉ, Scott MS","authors_abbrev":"Fafard-Couture É et al.","pubmed_publication_date":"19 Jul 2025","pubmed_entrez_date":"2025-07-30","publication_year":"2025","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-07-30 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19942852","title":"Fission yeast Pcp1 links polo kinase-mediated mitotic entry to gamma-tubulin-dependent spindle formation.","citation":"EMBO J 2010 Jan 06;29(1):120-30","abstract":"The centrosomal pericentrin-related proteins play pivotal roles in various aspects of cell division; however their underlying mechanisms remain largely elusive. Here we show that fission-yeast pericentrin-like Pcp1 regulates multiple functions of the spindle pole body (SPB) through recruiting two critical factors, the gamma-tubulin complex (gamma-TuC) and polo kinase (Plo1). We isolated two pcp1 mutants (pcp1-15 and pcp1-18) that display similar abnormal spindles, but with remarkably different molecular defects. Both mutants exhibit defective monopolar spindle microtubules that emanate from the mother SPB. However, while pcp1-15 fails to localise the gamma-TuC to the mitotic SPB, pcp1-18 is specifically defective in recruiting Plo1. Consistently Pcp1 forms a complex with both gamma-TuC and Plo1 in the cell. pcp1-18 is further defective in the mitotic-specific reorganisation of the nuclear envelope (NE), leading to impairment of SPB insertion into the NE. Moreover pcp1-18, but not pcp1-15, is rescued by overproducing nuclear pore components or advancing mitotic onset. The central role for Pcp1 in orchestrating these processes provides mechanistic insight into how the centrosome regulates multiple cellular pathways.","doi":"10.1038/emboj.2009.331","authors":"Fong CS, Sato M, Toda T","authors_abbrev":"Fong CS et al.","pubmed_publication_date":"06 Jan 2010","pubmed_entrez_date":"2009-11-28","publication_year":"2010","canto_session_key":"97c70bbdfd19df1d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-06-26 06:44:30","canto_approved_date":"2026-06-07 19:53:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-06-21 14:28:05","canto_added_date":"2012-02-24 05:47:48","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.04","SPBC649.05","SPBC428.20c","SPBC21.06c","SPCC18B5.03","SPBC365.15","SPAC1786.03","SPAC6G9.06c","SPAC23C11.16","SPBC29A10.07"],"gene_count":10,"ltp_gene_count":7,"approved_date":"2018-06-26"},{"uniquename":"PMID:26940262","title":"Zinc sensing and regulation in yeast model systems.","citation":"Arch Biochem Biophys 2016 Dec 01;611:30-36","abstract":"The Zap1 transcription factor of Saccharomyces cerevisiae and the Loz1 transcription factor of Schizosaccharomyces pombe both play a central role in zinc homeostasis by controlling the expression of genes necessary for zinc metabolism. Zap1 activates gene expression when cells are limited for zinc, while Loz1 is required for gene repression when zinc is in excess. In this review we highlight what is known about the underlying mechanisms by which these factors are regulated by zinc, and how transcriptional activation and repression in eukaryotic cells can be finely tuned according to intracellular zinc availability.","doi":"10.1016/j.abb.2016.02.031","authors":"Wilson S, Bird AJ","authors_abbrev":"Wilson S et al.","pubmed_publication_date":"01 Dec 2016","pubmed_entrez_date":"2016-03-05","publication_year":"2016","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2016-03-06 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC25B8.19c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:31427431","title":"Kinesin-8 and Dis1/TOG collaborate to limit spindle elongation from prophase to anaphase A for proper chromosome segregation in fission yeast.","citation":"J Cell Sci 2019 Sep 23;132(18)","abstract":"High-fidelity chromosome segregation relies on proper microtubule regulation. Kinesin-8 has been shown to destabilise microtubules to reduce metaphase spindle length and chromosome movements in multiple species. XMAP215/chTOG polymerases catalyse microtubule growth for spindle assembly, elongation and kinetochore-microtubule attachment. Understanding of their biochemical activity has advanced, but little work directly addresses the functionality and interplay of these conserved factors. We utilised the synthetic lethality of fission yeast kinesin-8 (Klp5-Klp6) and XMAP215/chTOG (Dis1) to study their individual and overlapping roles. We found that the non-motor kinesin-8 tailbox is essential for mitotic function; mutation compromises plus-end-directed processivity. Klp5-Klp6 induces catastrophes to control microtubule length and, surprisingly, Dis1 collaborates with kinesin-8 to slow spindle elongation. Together, they enforce a maximum spindle length for a viable metaphase-anaphase transition and limit elongation during anaphase A to prevent lagging chromatids. Our work provides mechanistic insight into how kinesin-8 negatively regulates microtubules and how this functionally overlaps with Dis1 and highlights the importance of spindle length control in mitosis.","doi":"10.1242/jcs.232306","authors":"Pinder C, Matsuo Y, Maurer SP, Toda T","authors_abbrev":"Pinder C et al.","pubmed_publication_date":"23 Sep 2019","pubmed_entrez_date":"2019-08-21","publication_year":"2019","canto_session_key":"75f4f061893fee16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2019-09-09 22:34:56","canto_approved_date":"2022-11-01 17:38:00","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2019-08-26 00:37:35","canto_added_date":"2019-08-22 00:15:04","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":68,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Takashi Toda","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2F12.13","SPCC736.14","SPBC1685.15c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-09-09"},{"uniquename":"PMID:38989013","title":"Characterization of temperature-sensitive alleles of  Schizosaccharomyces pombe  septation initiation network components.","citation":"MicroPubl Biol 2024;2024","abstract":"The  Schizosaccharomyces pombe  septation initiation network (SIN) promotes cytokinesis and septation. Comprised of a protein kinase cascade triggered by activation of a small GTPase and inhibited by a two-component GAP that localize to the spindle pole bodies in a cell cycle specific manner. Here, we characterized temperature-sensitive mutants isolated in the 1990s in four SIN components. We determined the mutations within each  cdc14  ,  cdc16  ,  sid1 ,  and  sid2  mutant allele and analyzed their growth at different temperatures compared with known mutant alleles. The new mutants described here expand the toolkit for studying SIN signaling.","doi":"10.17912/micropub.biology.001249","authors":"Turner LA, Willet AH, Gould KL","authors_abbrev":"Turner LA et al.","pubmed_publication_date":"2024","pubmed_entrez_date":"2024-07-11","publication_year":"2024","canto_session_key":"0917f87a0b7a8795","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alaina Willet","canto_first_approved_date":"2024-07-30 14:55:49","canto_approved_date":"2026-01-31 12:37:51","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-07-29 15:04:37","canto_added_date":"2024-07-11 23:25:06","annotation_curators":[{"name":"Alaina Willet","community_curator":true,"annotation_count":14,"orcid":"0000-0002-0163-4772","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC24B11.11c","SPAC9G1.09","SPAC6F6.08c","SPBC24C6.07"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2024-07-30"},{"uniquename":"PMID:19371376","title":"Schizosaccharomyces pombe cell division cycle under limited glucose requires Ssp1 kinase, the putative CaMKK, and Sds23, a PP2A-related phosphatase inhibitor.","citation":"Genes Cells 2009 May;14(5):539-54","abstract":"Calcium/calmodulin-dependent protein kinase (CaMK) is required for diverse cellular functions, and similar kinases exist in fungi. Although mammalian CaMK kinase (CaMKK) activates CaMK and also evolutionarily-conserved AMP-activated protein kinase (AMPK), CaMKK is yet to be established in yeast. We here report that the fission yeast Schizosaccharomyces pombe Ssp1 kinase, which controls G2/M transition and response to stress, is the putative CaMKK. Ssp1 has a CaM binding domain (CBD) and associates with 14-3-3 proteins as mammalian CaMKK does. Temperature-sensitive ssp1 mutants isolated are defective in the tolerance to limited glucose, and this tolerance requires the conserved stretch present between the kinase domain and CBD. Sds23, multi-copy suppressor for mutants defective in type 1 phosphatase and APC/cyclosome, also suppresses the ssp1 phenotype, and is required for the tolerance to limited glucose. We demonstrate that Sds23 binds to type 2A protein phosphatases (PP2A) and PP2A-related phosphatase Ppe1, and that Sds23 inhibits Ppe1 phosphatase activity. Ssp1 and Ppe1 thus seem to antagonize in utilizing limited glucose. We also show that Ppk9 and Ssp2 are the catalytic subunits of AMPK and AMPK-related kinases, respectively, which bind to common beta-(Amk2) and gamma-(Cbs2) subunits.","doi":"10.1111/j.1365-2443.2009.01290.x","authors":"Hanyu Y, Imai KK, Kawasaki Y, Nakamura T, Nakaseko Y, Nagao K, Kokubu A, Ebe M, Fujisawa A, Hayashi T, Obuse C, Yanagida M","authors_abbrev":"Hanyu Y et al.","pubmed_publication_date":"May 2009","pubmed_entrez_date":"2009-04-18","publication_year":"2009","canto_session_key":"7a0e423521cbb7b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-10-02 21:05:39","canto_approved_date":"2026-01-29 13:32:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-07-10 19:21:51","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":73,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAP8A3.09c","SPBC30B4.05","SPAC23H4.02","SPBC16H5.07c","SPCC1919.10c","SPBC18E5.05c","SPCC11E10.06c","SPBC8E4.01c","SPCC4B3.16","SPCC1450.11c","SPAC1556.08c","SPAC1751.03","SPCC1739.12","SPAC17A2.13c","SPAC17A5.12","SPBC36.07","SPCC297.03","SPBC3H7.10","SPCC663.01c","SPBC646.13","SPAC8E11.02c","SPCC1919.15","SPCC74.03c","SPAC227.07c","SPBC215.12","SPAC823.15","SPAC4D7.08c","SPBC4F6.17c","SPAC29A4.20","SPAC18G6.05c","SPAC23G3.06","SPCC895.06","SPCC1919.03c"],"gene_count":33,"ltp_gene_count":33,"approved_date":"2016-10-02"},{"uniquename":"PMID:20395362","title":"Histone acetylation in heterochromatin assembly.","citation":"Genes Dev 2010 Apr 15;24(8):738-40","abstract":"Histone acetylation is generally considered a mark involved in activating gene expression by making chromatin structures less compact. In the April 1, 2010, issue of Genes & Development, Xhemalce and Kouzarides (pp. 647-652) demonstrate that the acetylation of histone H3 at Lys 4 (H3K4) plays a role in the formation of repressive heterochromatin in Schizosaccharomyces pombe. H3K4 acetylation mediates a switch of chromodomain proteins associated with methylated H3K9 during heterochromatin assembly.","doi":"10.1101/gad.1922110","authors":"Kim JH, Workman JL","authors_abbrev":"Kim JH et al.","pubmed_publication_date":"15 Apr 2010","pubmed_entrez_date":"2010-04-17","publication_year":"2010","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10408447","title":"Orientation of DNA replication establishes mating-type switching pattern in S. pombe.","citation":"Nature 1999 Jul 08;400(6740):181-4","abstract":"The fission yeast Schizosaccharomyces pombe normally has haploid cells of two mating types, which differ at the chromosomal locus mat1. After two consecutive asymmetric cell divisions, only one in four 'grand-daughter' cells undergoes a 'mating-type switch', in which genetic information is transferred to mat1 from the mat2-P or mat3-M donor loci. This switching pattern probably results from an imprinting event at mat1 that marks one sister chromatid in a strand-specific manner, and is related to a site-specific, double-stranded DNA break at mat1. Here we show that the genetic imprint is a strand-specific, alkali-labile DNA modification at mat1. The DNA break is an artefact, created from the imprint during DNA purification. We also propose and test the model that mat1 is preferentially replicated by a centromere-distal origin(s), so that the strand-specific imprint occurs only during lagging-strand synthesis. Altering the origin of replication, by inverting mat1 or introducing an origin of replication, affects the imprinting and switching efficiencies in predicted ways. Two-dimensional gel analysis confirmed that mat1 is preferentially replicated by a centromere-distal origin(s). Thus, the DNA replication machinery may confer different developmental potential to sister cells.","authors":"Dalgaard JZ, Klar AJ","authors_abbrev":"Dalgaard JZ et al.","pubmed_publication_date":"08 Jul 1999","pubmed_entrez_date":"1999-07-17","publication_year":"1999","canto_triage_status":"Mating-type related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9745019","title":"ras1 and pat1 alleles interact to quantitatively and qualitatively alter conjugation in fission yeast.","citation":"Curr Genet 1998 Sep;34(3):172-82","abstract":"To identify novel components of ras1+ signalling in Schizosaccharomyces pombe, extragenic suppressors of the mating defect of ras1 effector mutants were isolated. A novel allele of pat1, pat1-e1, was isolated that increases the mating of ras1-D43E mutants to near wild-type levels but does not suppress the mating defect of ras1-I41M, ras1-Y37F, or ras1-Y45I mutants. This allele-specific suppression is not a characteristic of all pat1 alleles since pat1-3 and pat1-114 partially and equally suppress ras1-D43E and ras1-I41M mutants. Analysis of mating cultures showed that ras1-D43E and pat1-e1 interact to qualitatively alter the mating response. While pat1-e1 ras1-D43E cells were delayed in agglutination, cell-cycle delay, and mat1-Pm transcription, they induce mat1-Mc at the same time and mate more rapidly than other mating cultures. These results suggest that pheromone signalling, but not nutritional signalling, is delayed in pat1-e1 ras1-D43E cells. We hypothesize that this delay causes an elevated pheromone response and thus suppression of the mating defect of the ras1-D43E mutant by pat1-e1.","authors":"Mach KE, Cheng Q, Albright CF","authors_abbrev":"Mach KE et al.","pubmed_publication_date":"Sep 1998","pubmed_entrez_date":"1998-09-24","publication_year":"1998","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17H9.09c","SPBC19C2.05","SPBC354.05c","SPBC19C2.09","SPBC1D7.05"],"gene_count":5,"ltp_gene_count":5},{"uniquename":"PMID:9153756","title":"Isolation of a Schizosaccharomyces pombe gene which in high copy confers resistance to the nucleoside analogue 5-azacytidine.","citation":"Yeast 1997 Apr;13(5):463-74","abstract":"Treatment of Schizosaccharomyces pombe with the C5 DNA methyltransferase (C5Mtase) inhibitor 5-azacytidine (5-azaC) has previously been shown to induce G2 checkpoint-dependent cell cycle arrest. S. pombe strains defective in both the checkpoint control pathways and in DNA repair processes are sensitive to 5-azaC. Here we describe the isolation of azr1+, as a multi-copy suppressor of the 5-azaC sensitivity of G2 checkpoint and DNA repair-deficient strains. azr1+ encodes a putative 25 kDa protein with limited homology to a Saccharomyces cerevisiae open reading frame of unknown function. The azr1+ gene is not essential and the null mutant shows no alteration in either DNA repair or checkpoint properties. We also report the sequence of the putative fission yeast cytidine deaminase gene, designated pcd1+, which lies immediately adjacent to azr1+ but which plays only a moderate role in suppression of 5-azaC sensitivity.","authors":"Platt GM, Price C","authors_abbrev":"Platt GM et al.","pubmed_publication_date":"Apr 1997","pubmed_entrez_date":"1997-04-01","publication_year":"1997","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1556.03"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:27803257","title":"Chromatin Immunoprecipitation (ChIP) in Schizosaccharomyces pombe.","citation":"Cold Spring Harb Protoc 2016 Nov 01;2016(11)","abstract":"Chromatin immunoprecipitation (ChIP), the cross-linking of chromatin followed by immunoprecipitation with antibodies against a chromatin target, is a key method for measuring association of proteins with a specific genomic region(s). As a negative control, a mock ChIP experiment in which no antibody is added to the immunoprecipitation reaction is included. Enriched DNA fragments from a ChIP experiment can be analyzed in a variety of ways. For semiquantitative analysis, a region of interest can be amplified using standard polymerase chain reaction (PCR) techniques. PCR products are analyzed on agarose (or polyacrylamide) gels and band intensity calculated with a standard imaging software. ChIP enrichment is usually calculated as the ratio of ChIP to input compared with a similar ratio for a reference region not expected to be enriched for that factor. For heterochromatin analysis, housekeeping genes such as act1 +  are good references. Real-time quantitative PCR (qPCR) can be used for a fully quantitative approach. If a factor is to be mapped across the genome, ChIP DNA can be amplified and labeled for microarray analysis or scrutinized on a next-generation DNA sequencing platform.","doi":"10.1101/pdb.prot091546","authors":"Cam HP, Whitehall S","authors_abbrev":"Cam HP et al.","pubmed_publication_date":"01 Nov 2016","pubmed_entrez_date":"2016-11-03","publication_year":"2016","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-04 01:15:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23045396","title":"Continued DNA synthesis in replication checkpoint mutants leads to fork collapse.","citation":"Mol Cell Biol 2012 Dec;32(24):4986-97","abstract":"Hydroxyurea (HU) treatment activates the intra-S phase checkpoint proteins Cds1 and Mrc1 to prevent replication fork collapse. We found that prolonged DNA synthesis occurs in cds1Δ and mrc1Δ checkpoint mutants in the presence of HU and continues after release. This is coincident with increased DNA damage measured by phosphorylated histone H2A in whole cells during release. High-resolution live-cell imaging shows that mutants first accumulate extensive replication protein A (RPA) foci, followed by increased Rad52. Both DNA synthesis and RPA accumulation require the MCM helicase. We propose that a replication fork \"collapse point\" in HU-treated cells describes the point at which accumulated DNA damage and instability at individual forks prevent further replication. After this point, cds1Δ and mrc1Δ forks cannot complete genome replication. These observations establish replication fork collapse as a dynamic process that continues after release from HU block.","doi":"10.1128/MCB.01060-12","authors":"Sabatinos SA, Green MD, Forsburg SL","authors_abbrev":"Sabatinos SA et al.","pubmed_publication_date":"Dec 2012","pubmed_entrez_date":"2012-10-10","publication_year":"2012","canto_session_key":"6c9b9a730ab2b68f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:21","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC16A11.17","SPCC18B5.11c","SPBC776.12c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"EMBL:AU006782","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7851795","title":"Mutations derepressing silent centromeric domains in fission yeast disrupt chromosome segregation.","citation":"Genes Dev 1995 Jan 15;9(2):218-33","abstract":"The ura4+ gene displays phenotypes consistent with variegated expression when inserted at 11 sites throughout fission yeast centromere 1. An abrupt transition occurs between the zone of centromeric repression and two adjacent expressed sites. Mutations in six genes alleviate repression of the silent-mating type loci and of ura4+ expressed from a site adjacent to the silent locus, mat3-M. Defects at all six loci affect repression of the ura4+ gene adjacent to telomeres and at the three centromeric sites tested. The clr4-S5 and rik1-304 mutations cause the most dramatic derepression at two out of three sites within cen1. All six mutations had only slight or intermediate effects on a third site in the center of cen1 or on telomeric repression. Strains with lesions at the clr4, rik1, and swi6 loci have highly elevated rates of chromosome loss. We propose that the products of these genes are integral in the assembly of a heterochromatin-like structure, with distinct domains, enclosing the entire centromeric region that reduces or excludes access to transcription factors. The formation of this heterochromatic structure may be an absolute requirement for the formation of a fully functional centromere.","authors":"Allshire RC, Nimmo ER, Ekwall K, Javerzat JP, Cranston G","authors_abbrev":"Allshire RC et al.","pubmed_publication_date":"15 Jan 1995","pubmed_entrez_date":"1995-01-15","publication_year":"1995","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7651412","title":"The essential DNA-binding protein sap1 of Schizosaccharomyces pombe contains two independent oligomerization interfaces that dictate the relative orientation of the DNA-binding domain.","citation":"Mol Cell Biol 1995 Sep;15(9):4939-46","abstract":"The sap1 gene from Schizosaccharomyces pombe, which is essential for mating-type switching and for growth, encodes a sequence-specific DNA-binding protein with no homology to other known proteins. We have used a reiterative selection procedure to isolate binding sites for sap1, using a bacterially expressed protein and randomized double-strand oligonucleotides. The sap1 homodimer preferentially selects a pentameric motif, TA(A/G)CG, organized as a direct repeat and spaced by 5 nucleotides. Removal of a C-terminal dimerization domain abolishes recognition of the direct repeat and creates a new specificity for a DNA sequence containing the same pentameric motif but organized as an inverted repeat. We present evidence that the orientation of the DNA-binding domain is controlled by two independent oligomerization interfaces. The C-terminal dimerization domain allows a head-to-tail organization of the DNA-binding domains in solution, while an N-terminal domain is involved in a cooperative interaction on the DNA target between pairs of dimers.","authors":"Ghazvini M, Ribes V, Arcangioli B","authors_abbrev":"Ghazvini M et al.","pubmed_publication_date":"Sep 1995","pubmed_entrez_date":"1995-09-01","publication_year":"1995","canto_session_key":"60eab3fe44de3034","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2014-08-28 14:57:37","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-08-28 14:57:30","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-28"},{"uniquename":"PMID:15353355","title":"A report on single exon genes (SEG) in eukaryotes.","citation":"Front Biosci 2004 Sep 01;9:3262-7","abstract":"Single exon genes (SEG) are archetypical of prokaryotes. Hence, their presence in intron-rich, multi-cellular eukaryotic genomes is perplexing. Consequently, a study on SEG origin and evolution is important. Towards this goal, we took the first initiative of identifying and counting SEG in nine completely sequenced eukaryotic organisms--four of which are unicellular (E. cuniculi, S. cerevisiae, S. pombe, P. falciparum) and five of which are multi-cellular (C. elegans, A. thaliana, D. melanogaster, M. musculus, H. sapiens). This exercise enabled us to compare their proportion in unicellular and multi-cellular genomes. The comparison suggests that the SEG fraction decreases with gene count (r = -0.80) and increases with gene density (r = 0.88) in these genomes. We also examined the distribution patterns of their protein lengths in different genomes.","authors":"Sakharkar MK, Chow VT, Chaturvedi I, Mathura VS, Shapshak P, Kangueane P","authors_abbrev":"Sakharkar MK et al.","pubmed_publication_date":"01 Sep 2004","pubmed_entrez_date":"2004-09-09","publication_year":"2004","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16431364","title":"A heterochromatin barrier partitions the fission yeast centromere into discrete chromatin domains.","citation":"Curr Biol 2006 Jan 24;16(2):119-29","abstract":"Centromeres are cis-acting chromosomal domains that direct kinetochore formation, enabling faithful chromosome segregation. Centromeric regions of higher eukaryotes are structurally complex, consisting of various epigenetically modified chromatin types including specialized chromatin at the kinetochore itself, pericentromeric heterochromatin, and flanking euchromatin. Although the features necessary for the establishment and maintenance of discrete chromatin domains remain poorly understood, two models have been proposed based either on the passive convergence of competing activities involved in individual domain formation or, alternatively, on the action of specific genomic sequences and associated proteins to actively block the propagation of one chromatin type into another.\nFunctional analysis of centromeric sequences located at the intersection of Schizosaccharomyces pombe central core chromatin and outer repeat heterochromatin identified a chromatin barrier that contains a transfer RNA (tRNA) gene. Deletion or modification of the barrier sequences result in the propagation of pericentromeric heterochromatin beyond its normal boundary. The tRNA gene is transcriptionally active, and barrier activity requires sequences necessary for RNA polymerase III transcription. Moreover, absence of the barrier results in abnormal meiotic chromosome segregation.\nThe identification of DNA sequences with chromatin barrier activity at the fission yeast centromere provides a model for establishment of centromeric chromatin domains in higher eukaryotes.","authors":"Scott KC, Merrett SL, Willard HF","authors_abbrev":"Scott KC et al.","pubmed_publication_date":"24 Jan 2006","pubmed_entrez_date":"2006-01-25","publication_year":"2006","canto_triage_status":"Sequence feature or region","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17310250","title":"Two different Argonaute complexes are required for siRNA generation and heterochromatin assembly in fission yeast.","citation":"Nat Struct Mol Biol 2007 Mar;14(3):200-7","abstract":"The RNA-induced transcriptional silencing (RITS) complex, containing Ago1, Chp1, Tas3 and centromeric small interfering RNAs (siRNAs), is required for heterochromatic gene silencing at centromeres. Here, we identify a second fission yeast Argonaute complex (Argonaute siRNA chaperone, ARC), which contains, in addition to Ago1, two previously uncharacterized proteins, Arb1 and Arb2, both of which are required for histone H3 Lys9 (H3-K9) methylation, heterochromatin assembly and siRNA generation. Furthermore, whereas siRNAs in the RITS complex are mostly single-stranded, siRNAs associated with ARC are mostly double-stranded, indicating that Arb1 and Arb2 inhibit the release of the siRNA passenger strand from Ago1. Consistent with this observation, purified Arb1 inhibits the slicer activity of Ago1 in vitro, and purified catalytically inactive Ago1 contains only double-stranded siRNA. Finally, we show that slicer activity is required for the siRNA-dependent association of Ago1 with chromatin and for the spreading of histone H3-K9 methylation.","authors":"Buker SM, Iida T, Bühler M, Villén J, Gygi SP, Nakayama J, Moazed D","authors_abbrev":"Buker SM et al.","pubmed_publication_date":"Mar 2007","pubmed_entrez_date":"2007-02-21","publication_year":"2007","canto_session_key":"d47ecc7ad5ebfe9e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-25 09:17:39","canto_approved_date":"2024-05-25 09:17:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-24 15:35:38","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":38,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC140.03","SPAC13G7.07","SPAC664.01c","SPCC736.11","SPAC18G6.02c"],"gene_count":5,"ltp_gene_count":3,"approved_date":"2024-05-25"},{"uniquename":"EMBL:AU014090","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6754292","title":"Cell cycle operation during batch growth of fission yeast populations.","citation":"Cytometry 1982 Sep;3(2):123-8","abstract":"Batch cultivation provides a continuous sequence of different environments useful for studying responses of cell cycle controls. Flow cytometry measurements have been made of the frequency functions for protein, RNA, and DNA at different times during batch growth of the fission yeast Schizosaccharomyces pombe. The mean cellular protein and RNA contents and their variances tend to increase with increasing population specific growth rates. Analysis of the mid-exponential phase DNA frequency function data indicates that DNA synthesis occupies 12% of the total cell cycle time and is completed at the same time as cell separation. Coordination of DNA synthesis and cell separation is less precise when population growth rate is low in late lag and early stationary phases.","authors":"Agar DW, Bailey JE","authors_abbrev":"Agar DW et al.","pubmed_publication_date":"Sep 1982","pubmed_entrez_date":"1982-09-01","publication_year":"1982","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17716957","title":"Fission yeast Swi5 protein, a novel DNA recombination mediator.","citation":"DNA Repair (Amst) 2008 Jan 01;7(1):1-9","abstract":"The Schizosaccharomyces pombe Swi5 protein forms two distinct protein complexes, Swi5-Sfr1 and Swi5-Swi2, each of which plays an important role in the related but functionally distinct processes of homologous recombination and mating-type switching, respectively. The Swi5-Sfr1 mediator complex has been shown to associate with the two RecA-like recombinases, Rhp51 (spRad51) and Dmc1, and to stimulate in vitro DNA strand exchange reactions mediated by these proteins. Genetic analysis indicates that Swi5-Sfr1 works independently of another mediator complex, Rhp55-Rhp57, during Rhp51-dependent recombinational repair. In addition, mutations affecting the two mediators generate distinct repair spectra of HO endonuclease-induced DNA double strand breaks, suggesting that these recombination mediators differently regulate recombination outcomes in an independent manner.","authors":"Haruta N, Akamatsu Y, Tsutsui Y, Kurokawa Y, Murayama Y, Arcangioli B, Iwasaki H","authors_abbrev":"Haruta N et al.","pubmed_publication_date":"01 Jan 2008","pubmed_entrez_date":"2007-08-25","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:14652737","title":"Fission yeast Cdc37 is required for multiple cell cycle functions.","citation":"Mol Genet Genomics 2004 Feb;271(1):82-90","abstract":"The identification of a Schizosaccharomyces pombe homologue of the cdc37 gene is described. The gene product is most similar to the budding yeast homologue, but shows similarity to metazoan Cdc37 proteins, with a region of high similarity at the extreme N-terminus. Gene transplacement experiments in diploid cells followed by tetrad dissection show that the gene is essential. Depletion of the gene product after switching off expression of cdc37 from the regulatable nmt81 promoter results in cessation of growth and division. The cells arrest heterogeneously, with a significant proportion showing mitotic defects; paradoxically, a proportion of the cells show a short-cell phenotype consistent with an advanced cell cycle.","authors":"Westwood PK, Martin IV, Fantes PA","authors_abbrev":"Westwood PK et al.","pubmed_publication_date":"Feb 2004","pubmed_entrez_date":"2003-12-04","publication_year":"2004","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15279787","title":"Dial 9-1-1 for DNA damage: the Rad9-Hus1-Rad1 (9-1-1) clamp complex.","citation":"DNA Repair (Amst) 2004;3(8-9):1009-14","abstract":"Genotoxic stress activates checkpoint signaling pathways that block cell cycle progression, trigger apoptosis, and regulate DNA repair. Studies in yeast and humans have shown that Rad9, Hus1, Rad1, and Rad17 play key roles in checkpoint activation. Three of these proteins-Rad9, Hus1, and Rad1-interact in a heterotrimeric complex (dubbed the 9-1-1 complex), which resembles a PCNA-like sliding clamp, whereas Rad17 is part of a clamp-loading complex that is related to the PCNA clamp loader, replication factor-C (RFC). In response to genotoxic damage, the 9-1-1 complex is loaded around DNA by the Rad17-containing clamp loader. The DNA-bound 9-1-1 complex then facilitates ATR-mediated phosphorylation and activation of Chk1, a protein kinase that regulates S-phase progression, G2/M arrest, and replication fork stabilization. In addition to its role in checkpoint activation, accumulating evidence suggests that the 9-1-1 complex also participates in DNA repair. Taken together, these findings suggest that the 9-1-1 clamp is a multifunctional complex that is loaded onto DNA at sites of damage, where it coordinates checkpoint activation and DNA repair.","authors":"Parrilla-Castellar ER, Arlander SJ, Karnitz L","authors_abbrev":"Parrilla-Castellar ER et al.","pubmed_publication_date":"2004","pubmed_entrez_date":"2004-07-29","publication_year":"2004","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:07","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30959830","title":"Mitogen-Activated Protein Kinase Phosphatases (MKPs) in Fungal Signaling: Conservation, Function, and Regulation.","citation":"Int J Mol Sci 2019 Apr 05;20(7)","abstract":"Mitogen-activated protein kinases (MAPKs) are key mediators of signaling in fungi, participating in the response to diverse stresses and in developmental processes. Since the precise regulation of MAPKs is fundamental for cell physiology, fungi bear dual specificity phosphatases (DUSPs) that act as MAP kinase phosphatases (MKPs). Whereas fungal MKPs share characteristic domains of this phosphatase subfamily, they also have specific interaction motifs and particular activation mechanisms, which, for example, allow some yeast MKPs, such as  Saccharomyces cerevisiae  Sdp1, to couple oxidative stress with substrate recognition. Model yeasts show that MKPs play a key role in the modulation of MAPK signaling flow. Mutants affected in  S. cerevisiae  Msg5 or in  Schizosaccharomyces pombe  Pmp1 display MAPK hyperactivation and specific phenotypes. MKPs from virulent fungi, such as  Candida albicans  Cpp1,  Fusarium graminearum  Msg5, and  Pyricularia oryzae  Pmp1, are relevant for pathogenicity. Apart from transcriptional regulation, MKPs can be post-transcriptionally regulated by RNA-binding proteins such as Rnc1, which stabilizes the  S. pombe   PMP1  mRNA.  P. oryzae  Pmp1 activity and  S. cerevisiae  Msg5 stability are regulated by phosphorylation and ubiquitination, respectively. Therefore, fungi offer a platform to gain insight into the regulatory mechanisms that control MKPs.","doi":"10.3390/ijms20071709","authors":"González-Rubio G, Fernández-Acero T, Martín H, Molina M","authors_abbrev":"González-Rubio G et al.","pubmed_publication_date":"05 Apr 2019","pubmed_entrez_date":"2019-04-10","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-04-11 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17G6.04c","SPBC1685.01"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:1620594","title":"Activity of chimeric RNAs of U6 snRNA and (-)sTRSV in the cleavage of a substrate RNA.","citation":"Nucleic Acids Res 1992 Jun 25;20(12):2991-6","abstract":"U6 small nuclear RNA is one of the spliceosomal RNAs essential for pre-mRNA splicing. Discovery of mRNA-type introns in the highly conserved region of the U6 snRNA genes led to the hypothesis that U6 snRNA functions as a catalytic element during pre-mRNA splicing. The highly conserved region of U6 snRNA has a structural similarity with the catalytic domain of the negative strand of the satellite RNA of tobacco ring spot virus [(-)sTRSV], suggesting that the highly conserved region of U6 snRNA forms the catalytic center. We examined whether synthetic RNAs consisting of the sequence of the highly conserved region of U6 snRNA or various chimeric RNAs between the U6 region and the catalytic RNA of (-)sTRSV could cleave a substrate RNA that can partially base-pair with them and have a GU sequence. Chimeric RNAs with 70 to 83% sequence identity with the conserved region of S. pombe U6 snRNA cleaved the substrate RNA at the 5' side of the GU sequence, which is shared by the 5' end of an intron in a pre-mRNA. We found that the highly conserved region of U6 snRNA and the catalytic domain of (-)sTRSV are strikingly similar in structure to the catalytic core region of the group I self-splicing intron in cyanobacteria. These results suggest that U6 snRNA, (-)sTRSV and the group I self-splicing intron originated from a common ancestral RNA, and support the hypothesis that U6 snRNA catalyzes pre-mRNA splicing reaction.","authors":"Tani T, Takahashi Y, Ohshima Y","authors_abbrev":"Tani T et al.","pubmed_publication_date":"25 Jun 1992","pubmed_entrez_date":"1992-06-25","publication_year":"1992","canto_session_key":"32b20f35508dc1c9","canto_annotation_status":"APPROVED","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_approved_date":"2014-06-20 13:42:27","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-20 13:42:05","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPSNRNA.06"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2014-06-20"},{"uniquename":"PMID:38493594","title":"Arp2/3 complex- and formin-mediated actin cytoskeleton networks facilitate actin binding protein sorting in fission yeast.","citation":"Eur J Cell Biol 2024 Mar 16;103(2):151404","abstract":"While it is well-established that F-actin networks with specific organizations and dynamics are tightly regulated by distinct sets of associated actin-binding proteins (ABPs), how ABPs self-sort to particular F-actin networks remains largely unclear. We report that actin assembly factors Arp2/3 complex and formin Cdc12 tune the association of ABPs fimbrin Fim1 and tropomyosin Cdc8 to different F-actin networks in fission yeast. Genetic and pharmacological disruption of F-actin networks revealed that Fim1 is preferentially directed to Arp2/3-complex mediated actin patches, whereas Cdc8 is preferentially targeted to formin Cdc12-mediated filaments in the contractile ring. To investigate the role of Arp2/3 complex- and formin Cdc12-mediated actin assembly, we used four-color TIRF microscopy to observe the in vitro reconstitution of ABP sorting with purified proteins. Fim1 or Cdc8 alone bind similarly well to filaments assembled by either assembly factor. However, in 'competition' reactions containing both actin assembly factors and both ABPs, ∼2.0-fold more Fim1 and ∼3.5-fold more Cdc8 accumulates on Arp2/3 complex branch points and formin Cdc12-assembled actin filaments, respectively. These findings indicate that F-actin assembly factors Arp2/3 complex and formin Cdc12 help facilitate the recruitment of specific ABPs, thereby tuning ABP sorting and subsequently establishing the identity of F-actin networks in fission yeast.","doi":"10.1016/j.ejcb.2024.151404","authors":"Homa KE, Hocky GM, Suarez C, Kovar DR","authors_abbrev":"Homa KE et al.","pubmed_publication_date":"16 Mar 2024","pubmed_entrez_date":"2024-03-17","publication_year":"2024","canto_session_key":"154e065de1c7603b","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-03-19 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3233558","title":"Pseudo-exponential growth in length of the fission yeast, Schizosaccharomyces pombe.","citation":"Can J Microbiol 1988 Dec;34(12):1338-43","abstract":"The growth patterns of individual cells of the fission yeast (Schizosaccharomyces pombe wild-type cells, strain 972 h-; cells exposed to hydroxyurea; and cdc mutants, 11-123, 2-33) were investigated by time-lapse photomicrography. Wild-type cells showed one, two, or three linear-growth segments followed by a constant-length stage. Cells with two segments were most frequent. Hydroxyurea cells that divided as oversized cells (about three times the birth length) had three linear-growth segments in a cycle. Mutant cdc11-123 cells did not divide but had a constant-length stage separating the cycles; both the first and second cycles consisted of two linear-growth segments, and cells were oversized at the second constant-length stage (about 3.5 times the birth length). Elongating cdc2-33 cells that did not divide and were oversized (about five times the birth length) while under observation, showed four linear-growth segments. Cells of all strains showed 30 to 40% increase in growth rate at the rate-change point and maintained approximate exponential (pseudo-exponential) growth. We conclude that the normal growth pattern of individual fission-yeast cells is the pseudo-exponential pattern.","authors":"Miyata H, Miyata M, Johnson BF","authors_abbrev":"Miyata H et al.","pubmed_publication_date":"Dec 1988","pubmed_entrez_date":"1988-12-01","publication_year":"1988","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41091578","title":"Localization and function of septins are susceptible to epitope tagging.","citation":"Mol Biol Cell 2025 Oct 15;:mbcE25050217","abstract":"Septins are hetero-oligomeric cytoskeletal proteins that assemble into filaments and scaffolds on the plasma membrane to aid cytokinesis, morphogenesis, and other cellular processes. Epitope tagging is widely used to study septin localization and function. However, functionality testing of tagged septins is often insufficient because of technical challenges. Fission yeast provides an ideal genetic system to test functionalities and localizations of tagged septins. mEGFP/mYFP tagged septins Spn1 and Spn4 localize exclusively to the division site as double rings during cytokinesis, but tdTomato tagged septins also localize to puncta or short linear structures across the plasma membrane. It was proposed that these additional septin structures serve as diffusion barriers and are important for the localizations and functions of several proteins, including the NDR-kinase Sid2 and active Cdc42 GTPase. By analyzing cell morphology, cytokinesis defects, and genetic interactions between tagged septins and three mutations, we find that septins are less functional with tdTomato or 3HA than other tags. Additionally, Sid2 appearance at the division site is after septins and delayed in septin deletions, contrary to previous reports. Our data re-emphasize the need for rigorous functional tests of tagged septins and for caution in interpreting function and localization data when using epitope tagged septins. [Media: see text].","doi":"10.1091/mbc.E25-05-0217","authors":"Gregory JR, Llaneza IMA, Osmani AH, Gosselin HE, Sabzian SA, Wu JQ","authors_abbrev":"Gregory JR et al.","pubmed_publication_date":"15 Oct 2025","pubmed_entrez_date":"2025-10-15","publication_year":"2025","canto_session_key":"422b5d9e0bdcaf0a","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2025-10-15 23:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10747036","title":"A novel SMC protein complex in Schizosaccharomyces pombe contains the Rad18 DNA repair protein.","citation":"EMBO J 2000 Apr 03;19(7):1691-702","abstract":"In Schizosaccharomyces pombe, rad18 is an essential gene involved in the repair of DNA damage produced by ionizing radiation and in tolerance of UV-induced DNA damage. The Rad18 protein is a member of the SMC (structural maintenance of chromosomes) superfamily, and we show that, like the other SMC proteins in condensin and cohesin, Rad18 is a component of a high-molecular-weight complex. This complex contains at least six other proteins, the largest of which is Spr18, a novel SMC family member closely related to Rad18, and likely to be its heterodimeric partner. SMC proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. We show that the N-terminal ATP-binding domain of Rad18 is essential for all functions, and overexpression of an N-terminal mutant has a dominant-negative effect. We have identified an important mutation (S1045A) near the C-terminus of Rad18 that separates its repair and essential roles. Potential models for the role of the Rad18-Spr18 complex during DNA repair are discussed.","authors":"Fousteri MI, Lehmann AR","authors_abbrev":"Fousteri MI et al.","pubmed_publication_date":"03 Apr 2000","pubmed_entrez_date":"2000-04-04","publication_year":"2000","canto_session_key":"6844e4fe3a13f7c1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-02-13 16:10:53","canto_approved_date":"2021-05-07 13:32:34","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-05-07 13:32:23","canto_added_date":"2012-02-24 05:52:19","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC14C4.02c","SPCC5E4.06"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-02-13"},{"uniquename":"PMID:15509866","title":"Fkh2p and Sep1p regulate mitotic gene transcription in fission yeast.","citation":"J Cell Sci 2004 Nov 01;117(Pt 23):5623-32","abstract":"In the fission yeast Schizosaccharomyces pombe, several genes including cdc15+, spo12+, fin1+, slp1+, ace2+ and plo1+ are periodically expressed during M phase. The products of these genes control various aspects of cell cycle progression including sister chromatid separation, septation and cytokinesis. We demonstrate that periodic expression of these genes is regulated by a common promoter sequence element, named a PCB. In a genetic screen for cell cycle regulators we have identified a novel forkhead transcription factor, Fkh2p, which is periodically phosphorylated in M phase. We show that Fhk2p and another forkhead transcription factor, Sep1p, are necessary for PCB-driven M-phase-specific transcription. In a previous report we identified a complex by electrophoretic mobility shift assay, which we termed PBF, that binds to a 150 bp region of the cdc15+ promoter that contains the PCB element. We have identified Mbx1p, a novel MADS box protein, as a component of PBF. However, although Mbx1p is periodically phosphorylated in M phase, Mbx1p is not required for periodic gene transcription in M phase. Moreover, although PBF is absent in strains bearing a C-terminal epitope tag on Fkh2p, simultaneous deletion of fkh2+ and sep1+ does not abolish PBF binding activity. This suggests that Mbx1p binds to gene promoters, but is not required for transcriptional activation. Together these results suggest that the activation of the Fkh2p and Sep1p forkhead transcription factors triggers mitotic gene transcription in fission yeast.","authors":"Buck V, Ng SS, Ruiz-Garcia AB, Papadopoulou K, Bhatti S, Samuel JM, Anderson M, Millar JB, McInerny CJ","authors_abbrev":"Buck V et al.","pubmed_publication_date":"01 Nov 2004","pubmed_entrez_date":"2004-10-29","publication_year":"2004","canto_session_key":"386eb2f16aa6dee7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-11-26 17:32:24","canto_approved_date":"2024-04-03 08:02:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-11-26 17:32:16","canto_added_date":"2012-02-24 05:50:06","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":61,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC821.08c","SPAC6G10.12c","SPAC3F10.15c","SPBC317.01","SPAC11E3.06","SPAC1F3.06c","SPAC20G8.05c","SPAC19E9.02","SPAC1142.08","SPBC16G5.15c","SPBC4C3.12","SPBC19G7.06"],"gene_count":12,"ltp_gene_count":6,"approved_date":"2015-11-26"},{"uniquename":"PMID:20473289","title":"Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.","citation":"Nat Biotechnol 2010 Jun;28(6):617-623","abstract":"We report the construction and analysis of 4,836 heterozygous diploid deletion mutants covering 98.4% of the fission yeast genome providing a tool for studying eukaryotic biology. Comprehensive gene dispensability comparisons with budding yeast--the only other eukaryote for which a comprehensive knockout library exists--revealed that 83% of single-copy orthologs in the two yeasts had conserved dispensability. Gene dispensability differed for certain pathways between the two yeasts, including mitochondrial translation and cell cycle checkpoint control. We show that fission yeast has more essential genes than budding yeast and that essential genes are more likely than nonessential genes to be present in a single copy, to be broadly conserved and to contain introns. Growth fitness analyses determined sets of haploinsufficient and haploproficient genes for fission yeast, and comparisons with budding yeast identified specific ribosomal proteins and RNA polymerase subunits, which may act more generally to regulate eukaryotic cell growth.","doi":"10.1038/nbt.1628","authors":"Kim DU, Hayles J, Kim D, Wood V, Park HO, Won M, Yoo HS, Duhig T, Nam M, Palmer G, Han S, Jeffery L, Baek ST, Lee H, Shim YS, Lee M, Kim L, Heo KS, Noh EJ, Lee AR, Jang YJ, Chung KS, Choi SJ, Park JY, Park Y, Kim HM, Park SK, Park HJ, Kang EJ, Kim HB, Kang HS, Park HM, Kim K, Song K, Song KB, Nurse P, Hoe KL","authors_abbrev":"Kim DU et al.","pubmed_publication_date":"Jun 2010","pubmed_entrez_date":"2010-05-18","publication_year":"2010","canto_session_key":"ad1aab863f8d55c4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-08-21 17:40:41","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-08-21 16:20:51","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val 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repair in Schizosaccharomyces pombe requires the mutL homologous gene pms1: molecular cloning and functional analysis.","citation":"Genetics 1997 Aug;146(4):1275-86","abstract":"Homologues of the bacterial mutS and mutL genes involved in DNA mismatch repair have been found in organisms from bacteria to humans. Here, we describe the structure and function of a newly identified Schizosaccharomyces pombe that encodes a predicted amino acid sequence of 794 residues with a high degree of homology to MutL related proteins. On the basis of its closer relationship to the eukaryotic \"PMS\" genes than to the \"MLH\" genes, we have designated the S. pombe homologue pms1. Disruption of the pms1 gene causes a significant increase of spontaneous mutagenesis as documented by reversion rate measurements. Tetrad analyses of crosses homozygous for the pms1 mutation reveal a reduction of spore viability from > 92% to 80% associated with a low proportion (approximately 50%) of meioses producing four viable spores and a significant, allele-dependent increase of the level of post-meiotic segregation of genetic marker allele pairs. The mutant phenotypes are consistent with a general function of pms1 in correction of mismatched base pairs arising as a consequence of DNA polymerase errors during DNA synthesis, or of hybrid DNA formation between homologous but not perfectly complementary DNA strands during meiotic recombination.","authors":"Schär P, Baur M, Schneider C, Kohli J","authors_abbrev":"Schär P et al.","pubmed_publication_date":"Aug 1997","pubmed_entrez_date":"1997-08-01","publication_year":"1997","canto_session_key":"9791248f9ea31d50","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-06-09 11:39:52","canto_approved_date":"2018-06-09 11:39:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-06-09 11:39:45","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":6,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC19G12.02c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-06-09"},{"uniquename":"PMID:21572561","title":"3' processing of eukaryotic precursor tRNAs.","citation":"Wiley Interdiscip Rev RNA 2011;2(3):362-75","abstract":"Biogenesis of eukaryotic tRNAs requires transcription by RNA polymerase III and subsequent processing. 5' processing of precursor tRNA occurs by a single mechanism, cleavage by RNase P, and usually occurs before 3' processing although some conditions allow observation of the 3'-first pathway. 3' processing is relatively complex and is the focus of this review. Precursor RNA 3'-end formation begins with pol III termination generating a variable length 3'-oligo(U) tract that represents an underappreciated and previously unreviewed determinant of processing. Evidence that the pol III-intrinsic 3'exonuclease activity mediated by Rpc11p affects 3'oligo(U) length is reviewed. In addition to multiple 3' nucleases, precursor tRNA(pre-tRNA) processing involves La and Lsm, distinct oligo(U)-binding proteins with proposed chaperone activities. 3' processing is performed by the endonuclease RNase Z or the exonuclease Rex1p (possibly others) along alternate pathways conditional on La. We review a Schizosaccharomyces pombe tRNA reporter system that has been used to distinguish two chaperone activities of La protein to its two conserved RNA binding motifs. Pre-tRNAs with structural impairments are degraded by a nuclear surveillance system that mediates polyadenylation by the TRAMP complex followed by 3'-digestion by the nuclear exosome which appears to compete with 3' processing. We also try to reconcile limited data on pre-tRNA processing and Lsm proteins which largely affect precursors but not mature tRNAs.A pathway is proposed in which 3' oligo(U) length is a primary determinant of La binding with subsequent steps distinguished by 3'-endo versus exo nucleases,chaperone activities, and nuclear surveillance.","doi":"10.1002/wrna.64","authors":"Maraia RJ, Lamichhane TN","authors_abbrev":"Maraia RJ et al.","pubmed_publication_date":"2011","pubmed_entrez_date":"2011-05-17","publication_year":"2011","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:46:57","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC637.09","SPAC22A12.05","SPAC1F3.01","SPAC57A10.10c","SPCC1840.10"],"gene_count":5,"ltp_gene_count":0},{"uniquename":"PMID:16723501","title":"Rad4TopBP1, a scaffold protein, plays separate roles in DNA damage and replication checkpoints and DNA replication.","citation":"Mol Biol Cell 2006 Aug;17(8):3456-68","abstract":"Rad4TopBP1, a BRCT domain protein, is required for both DNA replication and checkpoint responses. Little is known about how the multiple roles of Rad4TopBP1 are coordinated in maintaining genome integrity. We show here that Rad4TopBP1 of fission yeast physically interacts with the checkpoint sensor proteins, the replicative DNA polymerases, and a WD-repeat protein, Crb3. We identified four novel mutants to investigate how Rad4TopBP1 could have multiple roles in maintaining genomic integrity. A novel mutation in the third BRCT domain of rad4+TopBP1 abolishes DNA damage checkpoint response, but not DNA replication, replication checkpoint, and cell cycle progression. This mutant protein is able to associate with all three replicative polymerases and checkpoint proteins Rad3ATR-Rad26ATRIP, Hus1, Rad9, and Rad17 but has a compromised association with Crb3. Furthermore, the damaged-induced Rad9 phosphorylation is significantly reduced in this rad4TopBP1 mutant. Genetic and biochemical analyses suggest that Crb3 has a role in the maintenance of DNA damage checkpoint and influences the Rad4TopBP1 damage checkpoint function. Taken together, our data suggest that Rad4TopBP1 provides a scaffold to a large complex containing checkpoint and replication proteins thereby separately enforcing checkpoint responses to DNA damage and replication perturbations during the cell cycle.","authors":"Taricani L, Wang TS","authors_abbrev":"Taricani L et al.","pubmed_publication_date":"Aug 2006","pubmed_entrez_date":"2006-05-26","publication_year":"2006","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:25","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1259.13","SPBC216.05","SPBP8B7.14c","SPAC664.07c","SPCC18B5.11c","SPAC9E9.08","SPAC20G4.04c","SPAC23C4.18c","SPAC14C4.13","SPAC13G7.08c"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:31050341","title":"Stable Pom1 clusters form a glucose-modulated concentration gradient that regulates mitotic entry.","citation":"Elife 2019 May 03;8","abstract":"Control of cell size requires molecular size sensors that are coupled to the cell cycle. Rod-shaped fission yeast cells divide at a threshold size partly due to Cdr2 kinase, which forms nodes at the medial cell cortex where it inhibits the Cdk1-inhibitor Wee1. Pom1 kinase phosphorylates and inhibits Cdr2, and forms cortical concentration gradients from cell poles. Pom1 inhibits Cdr2 signaling to Wee1 specifically in small cells, but the time and place of their regulatory interactions were unclear. We show that Pom1 forms stable oligomeric clusters that dynamically sample the cell cortex. Binding frequency is patterned into a concentration gradient by the polarity landmarks Tea1 and Tea4. Pom1 clusters colocalize with Cdr2 nodes, forming a glucose-modulated inhibitory threshold against node activation. Our work reveals how Pom1-Cdr2-Wee1 operates in multiprotein clusters at the cortex to promote mitotic entry at a cell size that can be modified by nutrient availability.","doi":"10.7554/eLife.46003","authors":"Allard CAH, Opalko HE, Moseley JB","authors_abbrev":"Allard CAH et al.","pubmed_publication_date":"03 May 2019","pubmed_entrez_date":"2019-05-04","publication_year":"2019","canto_session_key":"c3254b8f177a2c0d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-05-04 00:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC57A10.02"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:11808194","title":"[The role of pre-meiotic S phase].","citation":"Tanpakushitsu Kakusan Koso 2002 Jan;47(1):45-50","abstract":"","authors":"Watanabe Y","authors_abbrev":"Watanabe Y","pubmed_publication_date":"Jan 2002","pubmed_entrez_date":"2002-01-26","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:18","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24312601","title":"Fingolimod (FTY720) stimulates Ca(2+)/calcineurin signaling in fission yeast.","citation":"PLoS One 2013;8(12):e81907","abstract":"Fingolimod hydrochloride (FTY720) is the first in class of sphingosine 1-phosphate (S1P) receptor modulator approved to treat multiple sclerosis via down-regulation of G protein-coupled S1P receptor 1 by its phosphorylated form (FTY720-P). Many studies have revealed that FTY720 exerts various biological effects, including antitumor activities, angiogenesis inhibition, Ca(2+) mobilization and apoptosis, independently of S1P receptors. However, the exact mechanisms underlying their effects or signaling pathways mediated by FTY720 have not been completely established. To gain further insights into molecular mechanisms of FTY720 action, the effect of FTY720 on Ca(2+) signaling in fission yeast was analyzed. The addition of Ca(2+) enhanced the sensitivity induced by FTY720, and mutants lacking genes required for calcium homeostasis, including calcineurin and its downstream transcription factor, Ppb1-responsive zinc finger protein (Prz1), were hypersensitive to FTY720 and CaCl2. The effect of FTY720 on calcineurin signaling was monitored by utilizing a luciferase reporter construct fused to three tandem repeats of the calcineurin-dependent response element (CDRE), which gives an accurate measure of calcineurin activity. The addition of FTY720 increased calcineurin activity as well as Ca(2+) influx in a concentration-dependent manner. Notably, the FTY720-mediated Ca(2+) influx and calcineurin activation were reduced markedly by the deletion of yam8 (+) or cch1 (+) encoding putative subunits of a Ca(2+) channel. Consistently, the deletion of Pmk1 mitogen-activated protein kinase (MAPK), which plays an important role in the activation of the Yam8/Cch1 channel, markedly decreased the intracellular Ca(2+) levels upon FTY720 treatment. These results suggest that the FTY720-stimulated Ca(2+)/calcineurin signaling activation partly involves the Yam8/Cch1 channel in fission yeast.","doi":"10.1371/journal.pone.0081907","authors":"Hagihara K, Kita A, Mizukura A, Yao M, Kitai Y, Kunoh T, Masuko T, Matzno S, Chiba K, Sugiura R","authors_abbrev":"Hagihara K et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-12-07","publication_year":"2013","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1791747","title":"Radiation resistance in Schizosaccharomyces pombe.","citation":"Mol Microbiol 1991 Oct;5(10):2311-4","abstract":"The fission yeast Schizosaccharomyces pombe serves as an excellent alternative and complementary model system for the analysis of genes and gene products involved in DNA repair. This brief review outlines the advantages of S. pombe and describes the radiation-sensitive mutants available for the analysis of DNA repair and recombination mechanisms in this organism. The progress in the cloning and characterization of representative genes is also described.","authors":"Subramani S","authors_abbrev":"Subramani S","pubmed_publication_date":"Oct 1991","pubmed_entrez_date":"1991-10-01","publication_year":"1991","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:5111492","title":"The isolation and genetic classification of UV-sensitive mutants of Schizosaccharomyces pombe.","citation":"Mutat Res 1971 Apr;11(4):361-71","abstract":"","authors":"Schüpbach M","authors_abbrev":"Schüpbach M","pubmed_publication_date":"Apr 1971","pubmed_entrez_date":"1971-04-01","publication_year":"1971","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10958692","title":"Conservation of heterochromatin protein 1 function.","citation":"Mol Cell Biol 2000 Sep;20(18):6970-83","abstract":"Heterochromatin represents a cytologically visible state of heritable gene repression. In the yeast, Schizosaccharomyces pombe, the swi6 gene encodes a heterochromatin protein 1 (HP1)-like chromodomain protein that localizes to heterochromatin domains, including the centromeres, telomeres, and the donor mating-type loci, and is involved in silencing at these loci. We identify here the functional domains of swi6p and demonstrate that the chromodomain from a mammalian HP1-like protein, M31, can functionally replace that of swi6p, showing that chromodomain function is conserved from yeasts to humans. Site-directed mutagenesis, based on a modeled three-dimensional structure of the swi6p chromodomain, shows that the hydrophobic amino acids which lie in the core of the structure are critical for biological function. Gel filtration, gel overlay experiments, and mass spectroscopy show that HP1 proteins can self-associate, and we suggest that it is as oligomers that HP1 proteins are incorporated into heterochromatin complexes that silence gene activity.","authors":"Wang G, Ma A, Chow CM, Horsley D, Brown NR, Cowell IG, Singh PB","authors_abbrev":"Wang G et al.","pubmed_publication_date":"Sep 2000","pubmed_entrez_date":"2000-08-25","publication_year":"2000","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:01","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:28041796","title":"A PP2A-B55-Mediated Crosstalk between TORC1 and TORC2 Regulates the Differentiation Response in Fission Yeast.","citation":"Curr Biol 2017 Jan 23;27(2):175-188","abstract":"Extracellular cues regulate cell fate, and this is mainly achieved through the engagement of specific transcriptional programs. The TORC1 and TORC2 complexes mediate the integration of nutritional cues to cellular behavior, but their interplay is poorly understood. Here, we use fission yeast to investigate how phosphatase activity participates in this interplay during the switch from proliferation to sexual differentiation. We find that loss of PP2A-B55 Pab1  enhances the expression of differentiation-specific genes and leads to premature conjugation. pab1 deletion brings about a transcriptional profile similar to TORC1 inactivation, and deletion of pab1 overcomes the repression of differentiation genes in cells overexpressing TORC1. Importantly, we show that this effect is mediated by an increased TORC2-AKT (Gad8) signaling. Under nutrient-rich conditions, PP2A-B55 Pab1  dephosphorylates Gad8 Ser546, repressing its activity. Conversely, TORC1 inactivation upon starvation leads to the inactivation of PP2A-B55 Pab1  through the Greatwall-Endosulfin pathway. This results in the activation of Gad8 and the commitment to differentiation. Thus, PP2A-B55 Pab1  enables a crosstalk between the two TOR complexes that controls cell-fate decisions in response to nutrient availability.","doi":"10.1016/j.cub.2016.11.037","authors":"Martín R, Portantier M, Chica N, Nyquist-Andersen M, Mata J, Lopez-Aviles S","authors_abbrev":"Martín R et al.","pubmed_publication_date":"23 Jan 2017","pubmed_entrez_date":"2017-01-03","publication_year":"2017","canto_session_key":"2ff9544218a3c825","canto_annotation_status":"APPROVAL_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2026-05-27 09:21:06","canto_added_date":"2017-01-05 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC24B10.07","SPBC16H5.07c","SPBC216.07c","SPAPYUG7.02c","SPAC10F6.16","SPAC4C5.02c","SPAC227.07c","SPAC630.13c","SPBC30D10.10c","SPBC16G5.15c"],"gene_count":10,"ltp_gene_count":10},{"uniquename":"PMID:12901373","title":"Parallel evolution by gene duplication in the genomes of two unicellular fungi.","citation":"Genome Res 2003 Jun;13(6A):1259-64","abstract":"Phylogenetic analysis of conserved gene families in fission yeast Schizosaccharomyces pombe and brewer's yeast Saccharomyces cerevisiae showed that gene duplications have occurred independently in the same families in each of these two lineages to a far greater extent than expected by chance. These species represent distinct lineages of the phylum Ascomycota that independently evolved a \"yeast\" life cycle with a unicellular thallus that reproduces by budding, and many of the genes that have duplicated independently in the two lineages are known to be involved in crucial aspects of this life cycle. Parallel gene duplication thus appears to have played a role in the independent origin of similar adaptations in the two species. The results indicate that using phylogenetic analysis to test for parallel gene duplication in different species may help in identifying genes responsible for similar but independently evolved adaptations","authors":"Hughes AL, Friedman R","authors_abbrev":"Hughes AL et al.","pubmed_publication_date":"Jun 2003","pubmed_entrez_date":"2003-08-07","publication_year":"2003","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:39957727","title":"Experimental evolution of multicellularity via cuboidal cell packing in fission yeast.","citation":"Evol Lett 2024 Oct;8(5):695-704","abstract":"The evolution of multicellularity represents a major transition in life's history, enabling the rise of complex organisms. Multicellular groups can evolve through multiple developmental modes, but a common step is the formation of permanent cell-cell attachments after division. The characteristics of the multicellular morphology that emerges have profound consequences for the subsequent evolution of a nascent multicellular lineage, but little prior work has investigated these dynamics directly. Here, we examine a widespread yet understudied emergent multicellular morphology: cuboidal packing. Extinct and extant multicellular organisms across the tree of life have evolved to form groups in which spherical cells divide but remain attached, forming approximately cubic subunits. To experimentally investigate the evolution of cuboidal cell packing, we used settling selection to favor the evolution of simple multicellularity in unicellular, spherical  Schizosaccharomyces pombe  yeast. Multicellular clusters with cuboidal organization rapidly evolved, displacing the unicellular ancestor. These clusters displayed key hallmarks of an evolutionary transition in individuality: groups possess an emergent life cycle driven by physical fracture, group size is heritable, and they respond to group-level selection via multicellular adaptation. In 2 out of 5 lineages, group formation was driven by mutations in the  ace2  gene, preventing daughter cell separation after division. Remarkably,  ace2  mutations also underlie the transition to multicellularity in  Saccharomyces cerevisiae  and  Candida glabrata , lineages that last shared a common ancestor   >   300 million years ago. Our results provide insight into the evolution of cuboidal cell packing, an understudied multicellular morphology, and highlight the deeply convergent potential for a transition to multicellular individuality within fungi.","doi":"10.1093/evlett/qrae024","authors":"Pineau RM, Kahn PC, Lac DT, Belpaire TER, Denning MG, Wong W, Ratcliff WC, Bozdag GO","authors_abbrev":"Pineau RM et al.","pubmed_publication_date":"Oct 2024","pubmed_entrez_date":"2025-02-17","publication_year":"2024","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2025-02-18 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7269657","title":"Multiple septation in multinuclear protoplasts of Schizosaccharomyces pombe.","citation":"Z Allg Mikrobiol 1981;21(3):261-6","abstract":"The dependence of septation on karyokinesis was studied in protoplasts of the fission yeast Schizosaccharomyces pombe. The mononuclear protoplast produces a single centrally located septum. In multinuclear reverting protoplasts, on the other hand, the formation of a single septum was a rare event. In each protoplast instead of one, two to six septa were formed. These findings suggest some closer relations between the formation of septa and the number of nuclei present in the protoplast. Our results obtained with protoplasts also imply that the initiation of septum formation is possible only in the presence of a complete cell wall. In reverting multinuclear protoplasts undergoing more than one mitosis, no septation is initiated until the cell wall has been completed. Only the complete cell wall can induce the formation of one or several septa in mono- and multinuclear protoplasts, respectively.","authors":"Havelková M","authors_abbrev":"Havelková M","pubmed_publication_date":"1981","pubmed_entrez_date":"1981-01-01","publication_year":"1981","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22503534","title":"How to build a robust intracellular concentration gradient.","citation":"Trends Cell Biol 2012 Jun;22(6):311-7","abstract":"Concentration gradients of morphogens are critical regulators of patterning in developmental biology. Increasingly, intracellular concentration gradients have also been found to orchestrate spatial organization, but inside single cells, where they regulate processes such as cell division, polarity and mitotic spindle dynamics. Here, we discuss recent progress in understanding how such intracellular gradients can be built robustly. We focus particularly on the Pom1p gradient in fission yeast, elucidating how various buffering mechanisms operate to ensure precise gradient formation. In this case, a systems-level understanding of the entire mechanism of precise gradient construction is now within reach, with important implications for gradients in both intracellular and developmental contexts.","doi":"10.1016/j.tcb.2012.03.002","authors":"Howard M","authors_abbrev":"Howard M","pubmed_publication_date":"Jun 2012","pubmed_entrez_date":"2012-04-17","publication_year":"2012","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29934597","title":"Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species.","citation":"Sci Rep 2018 Jun 22;8(1):9554","abstract":"Huntington's disease is caused by the pathological expansion of a polyglutamine (polyQ) stretch in Huntingtin (Htt), but the molecular mechanisms by which polyQ expansion in Htt causes toxicity in selective neuronal populations remain poorly understood. Interestingly, heterologous expression of expanded polyQ Htt is toxic in Saccharomyces cerevisiae cells, but has no effect in Schizosaccharomyces pombe, a related yeast species possessing very few endogenous polyQ or Q/N-rich proteins. Here, we used a comprehensive and unbiased mass spectrometric approach to identify proteins that bind Htt in a length-dependent manner in both species. Analysis of the expanded polyQ-associated proteins reveals marked enrichment of proteins that are localized to and play functional roles in nucleoli and mitochondria in S. cerevisiae, but not in S. pombe. Moreover, expanded polyQ Htt appears to interact preferentially with endogenous polyQ and Q/N-rich proteins, which are rare in S. pombe, as well as proteins containing coiled-coil motifs in S. cerevisiae. Taken together, these results suggest that polyQ expansion of Htt may cause cellular toxicity in S. cerevisiae by sequestering endogenous polyQ and Q/N-rich proteins, particularly within nucleoli and mitochondria.","doi":"10.1038/s41598-018-27900-5","authors":"Zhao Y, Zurawel AA, Jenkins NP, Duennwald ML, Cheng C, Kettenbach AN, Supattapone S","authors_abbrev":"Zhao Y et al.","pubmed_publication_date":"22 Jun 2018","pubmed_entrez_date":"2018-06-24","publication_year":"2018","canto_triage_status":"Mutagenicity or toxicity study","canto_curator_role":"PomBase","canto_added_date":"2018-06-25 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16157682","title":"The Clr7 and Clr8 directionality factors and the Pcu4 cullin mediate heterochromatin formation in the fission yeast Schizosaccharomyces pombe.","citation":"Genetics 2005 Dec;171(4):1583-95","abstract":"Fission yeast heterochromatin is formed at centromeres, telomeres, and in the mating-type region where it mediates the transcriptional silencing of the mat2-P and mat3-M donor loci and the directionality of mating-type switching. We conducted a genetic screen for directionality mutants. This screen revealed the essential role of two previously uncharacterized factors, Clr7 and Clr8, in heterochromatin formation. Clr7 and Clr8 are required for localization of the Swi6 chromodomain protein and for histone H3 lysine 9 methylation, thereby influencing not only mating-type switching but also transcriptional silencing in all previously characterized heterochromatic regions, chromosome segregation, and meiotic recombination in the mating-type region. We present evidence for physical interactions between Clr7 and the mating-type region and between Clr7 and the S. pombe cullin Pcu4, indicating that a complex containing these proteins mediates an early step in heterochromatin formation and implying a role for ubiquitination at this early stage prior to the action of the Clr4 histone methyl-transferase. Like Clr7 and Clr8, Pcu4 is required for histone H3 lysine 9 methylation, and bidirectional centromeric transcripts that are normally processed into siRNA by the RNAi machinery in wild-type cells are easily detected in cells lacking Clr7, Clr8, or Pcu4. Another physical interaction, between the nucleoporin Nup189 and Clr8, suggests that Clr8 might be involved in tethering heterochromatic regions to the nuclear envelope by association with the nuclear-pore complex.","authors":"Thon G, Hansen KR, Altes SP, Sidhu D, Singh G, Verhein-Hansen J, Bonaduce MJ, Klar AJ","authors_abbrev":"Thon G et al.","pubmed_publication_date":"Dec 2005","pubmed_entrez_date":"2005-09-15","publication_year":"2005","canto_session_key":"35a8810c7dfc8c9d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Pascal Carme","canto_first_approved_date":"2024-05-03 14:29:19","canto_approved_date":"2024-05-03 14:29:19","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-05-02 09:04:03","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Pascal Carme","community_curator":false,"annotation_count":27,"orcid":"0009-0003-9059-1333","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC613.12c","SPAC3A11.08","SPAC1486.05","SPAC664.01c","SPCC970.07c"],"gene_count":5,"ltp_gene_count":4,"approved_date":"2024-05-03"},{"uniquename":"PANTHER:PTHR15892","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1919.08c","HGNC:14036"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:29423844","title":"Chromatin Immunoprecipitation-Polymerase Chain Reaction (ChIP-PCR) Detects Methylation, Acetylation, and Ubiquitylation in S. pombe.","citation":"Methods Mol Biol 2018;1721:25-34","abstract":"The distribution of modified histones within the fission yeast Schizosaccharomyces pombe genome is ultimately dependent upon the transcriptional activity and in turn influences the ability of the polymerases to bind and progress through the chromatin template. The Chromatin Immunoprecipitation-Polymerase Chain Reaction (ChIP-PCR) method currently provides the highest resolution, accuracy, and reproducibility to characterize histones modifications within a defined region of the genome. The following protocol details the method applied to S. pombe.","doi":"10.1007/978-1-4939-7546-4_3","authors":"Migeot V, Hermand D","authors_abbrev":"Migeot V et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"Pfam:PF12749","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC22H10.13"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37655454","title":"Long non-coding RNA and ribosomal protein genes in a yeast ageing model: an investigation for undergraduate research-based learning.","citation":"Essays Biochem 2023 Sep 13;67(5):893-901","abstract":"The unicellular yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe are widely used eukaryotic model organisms. Research exploiting the tractability of these model systems has contributed significantly to our understanding of a wide range of fundamental processes. In this article, we outline the features of yeast that have similarly been exploited for undergraduate research training. We selected examples from published literature that demonstrate the utility of the yeast system for research-based learning embedded in the curriculum. We further describe a project which we designed for the team-based final-year dissertation projects module on our transnational joint programme, which investigates whether the expression and functions of the budding yeast RPL36 ribosomal protein paralogs are influenced by the overlapping long non-coding RNA genes. Students carry out the experimental procedures in a 2-week timetabled teaching block and exercise widely applicable biochemical techniques, including aseptic yeast cell culture and sample collection, RNA isolation, qRT-PCR quantitation, protein extraction and Western blot analysis, and cell cycle progression patterns using light microscopy and flow cytometry. It is challenging to design training programmes for undergraduates that are meaningful as well as practical and economical, but it is possible to transform active research projects into authentic research experiences. We consider yeast to be an ideal model organism for such projects. These can be adapted to the constraints of course schedules and explore fundamental biochemical topics which are evolutionarily conserved from yeast to mammals.","doi":"10.1042/EBC20230010","authors":"Hwang GH, Clyne RK","authors_abbrev":"Hwang GH et al.","pubmed_publication_date":"13 Sep 2023","pubmed_entrez_date":"2023-09-01","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-09-02 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3380699","title":"Resolution of Schizosaccharomyces pombe chromosomes by field inversion gel electrophoresis.","citation":"Nucleic Acids Res 1988 May 25;16(10):4727","abstract":"","authors":"Turmel C, Lalande M","authors_abbrev":"Turmel C et al.","pubmed_publication_date":"25 May 1988","pubmed_entrez_date":"1988-05-25","publication_year":"1988","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:37","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9125114","title":"The Schizosaccharomyces pombe gms1+ gene encodes an UDP-galactose transporter homologue required for protein galactosylation.","citation":"Biochem Biophys Res Commun 1997 Mar 06;232(1):121-5","abstract":"In a previous study, we isolated a Schizosaccharomyces pombe mutant defective in protein galactosylation (Takegawa, K., Tanaka, N., Tabuchi, M. and Iwahara, S. (1996) Biosci. Biochem. Biotech. 60, 1156-1159). From an S. pombe genomic library, we cloned the gms1+ gene which restored the galactosylation of cell wall glycoproteins. Gms1 protein shares significant sequence similarity with human UDP-galactose and murine CMP-sialic acid transporters. The fission yeast strains deleted for the gms1+ gene lacked galactose residues in sell surface glycoproteins and were significantly decreased in UDP-galactose transport activity. These results showed that the gms1+ encodes an UDP-galactose transporter, and this protein appears to be an essential role for the incorporation of UDP-galactose into the lumen of Golgi in s. pombe.","authors":"Tabuchi M, Tanaka N, Iwahara S, Takegawa K","authors_abbrev":"Tabuchi M et al.","pubmed_publication_date":"06 Mar 1997","pubmed_entrez_date":"1997-03-06","publication_year":"1997","canto_session_key":"60a204a00657319d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-06-04 07:08:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-14 15:50:24","canto_added_date":"2012-02-24 05:53:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1795.03"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-14"},{"uniquename":"PMID:24477934","title":"Mad1 contribution to spindle assembly checkpoint signalling goes beyond presenting Mad2 at kinetochores.","citation":"EMBO Rep 2014 Mar;15(3):291-8","abstract":"The spindle assembly checkpoint inhibits anaphase until all chromosomes have become attached to the mitotic spindle. A complex between the checkpoint proteins Mad1 and Mad2 provides a platform for Mad2:Mad2 dimerization at unattached kinetochores, which enables Mad2 to delay anaphase. Here, we show that mutations in Bub1 and within the Mad1 C-terminal domain impair the kinetochore localization of Mad1:Mad2 and abrogate checkpoint activity. Artificial kinetochore recruitment of Mad1 in these mutants co-recruits Mad2; however, the checkpoint remains non-functional. We identify specific mutations within the C-terminal head of Mad1 that impair checkpoint activity without affecting the kinetochore localization of Bub1, Mad1 or Mad2. Hence, Mad1 potentially in conjunction with Bub1 has a crucial role in checkpoint signalling in addition to presenting Mad2.","doi":"10.1002/embr.201338114","authors":"Heinrich S, Sewart K, Windecker H, Langegger M, Schmidt N, Hustedt N, Hauf S","authors_abbrev":"Heinrich S et al.","pubmed_publication_date":"Mar 2014","pubmed_entrez_date":"2014-01-31","publication_year":"2014","canto_session_key":"3154c42f677dce94","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Silke Hauf","canto_first_approved_date":"2020-06-04 17:30:18","canto_approved_date":"2024-11-28 18:09:47","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-06-15 13:44:58","canto_added_date":"2014-11-09 01:15:25","annotation_curators":[{"name":"Silke Hauf","community_curator":true,"annotation_count":55,"orcid":"0000-0001-5938-721X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11C11.03","SPAC29E6.04","SPCC1795.01c","SPCC1020.02","SPCC188.04c","SPCC1322.12c","SPBC409.09c","SPAC688.02c","SPBC3D6.04c","SPBC20F10.06","SPBC336.08","SPAC27F1.04c","SPBC409.04c","SPCC162.08c","SPAC23H3.08c"],"gene_count":15,"ltp_gene_count":12,"approved_date":"2020-06-04"},{"uniquename":"PMID:8019001","title":"Identification and characterization of new elements involved in checkpoint and feedback controls in fission yeast.","citation":"Mol Biol Cell 1994 Feb;5(2):147-60","abstract":"To investigate the mechanisms that ensure the dependency relationships between cell cycle events and to investigate the checkpoints that prevent progression through the cell cycle after DNA damage, we have isolated mutants defective in the checkpoint and feedback control pathways. We report the isolation and characterization of 11 new loci that define distinct classes of mutants defective in one or more of the checkpoint and feedback control pathways. Two mutants, rad26.T12 and rad27.T15, were selected for molecular analysis. The null allele of the rad26 gene (rad26.d) shares the phenotype reported for the \"checkpoint rad\" mutants rad1, rad3, rad9, rad17, and hus1, which are defective in the radiation checkpoint and in the feedback controls that ensure the order of cell cycle events. The null allele of the rad27 gene (rad27.d) defines a new class of Schizosaccharomyces pombe mutant. The rad27 complementing gene codes for a putative protein kinase that is required for cell cycle arrest after DNA damage but not for the feedback control that links mitosis to the completion of prior DNA synthesis (the same gene has recently been described by Walworth et al. (1993) as chk1). These properties are similar to those of the rad9 gene of Saccharomyces cerevisiae. A comparative analysis of the radiation responses in rad26.d, rad26.T12, and rad27.d cells has revealed the existence of two separable responses to DNA damage controlled by the \"checkpoint rad\" genes. The first, G2 arrest, is defective in rad27.d and rad26.d but is unaffected in rad26.T12 cells. The second response is not associated with G2 arrest after DNA damage and is defective in rad26.d and rad26.T12 but not rad27.d cells. A study of the radiation sensitivity of these mutants through the cell cycle suggests that this second response is associated with S phase and that the checkpoint rad mutants, in addition to an inability to arrest mitosis after radiation, are defective in an S phase radiation checkpoint.","authors":"al-Khodairy F, Fotou E, Sheldrick KS, Griffiths DJ, Lehmann AR, Carr AM","authors_abbrev":"al-Khodairy F et al.","pubmed_publication_date":"Feb 1994","pubmed_entrez_date":"1994-02-01","publication_year":"1994","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC14C4.13"],"gene_count":1,"ltp_gene_count":1},{"uniquename":"PMID:3549293","title":"Molecular characterisation of the DNA ligase gene, CDC17, from the fission yeast Schizosaccharomyces pombe.","citation":"Eur J Biochem 1987 Feb 02;162(3):659-67","abstract":"We have sequenced a 4200-base-pair fragment of Schizosaccharomyces pombe DNA which encompasses the entire DNA ligase gene, CDC17. S1 mapping has enabled us to identify two small introns (40 and 62 nucleotides) at the 5' end of the coding region of the gene and their 3' internal conserved sequences match the CTRAY consensus found in other S. pombe introns. The major transcription initiation and 3' polyadenylation sites have been mapped and are preceded by higher eukaryotic-like TATA and AATAAA sequences respectively. Furthermore, the CDC17 mRNA carries a poly(A) tail whose length (approximately 250 nucleotides) is typical of that found in higher eukaryotic mRNAs, and is in contrast to the much shorter polyadenylated sequences found for the mRNAs of the budding yeast, Saccharomyces cerevisiae. The deduced amino acid sequence of the S. pombe DNA ligase predicts a protein of 86182 daltons, and an overall 53% homology with the same enzyme from S. cerevisiae. In particular, a stretch of 24 amino acids with 100% sequence homology spans the putative ATP-binding region which is also conserved in T4 and T7 bacteriophage DNA ligases.","authors":"Barker DG, White JH, Johnston LH","authors_abbrev":"Barker DG et al.","pubmed_publication_date":"02 Feb 1987","pubmed_entrez_date":"1987-02-02","publication_year":"1987","canto_session_key":"e955446047c6c4c0","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-30 15:52:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-28 14:35:24","canto_added_date":"2012-02-24 05:55:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC20G8.01"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2013-01-28"},{"uniquename":"PMID:16421249","title":"Rgf1p is a specific Rho1-GEF that coordinates cell polarization with cell wall biogenesis in fission yeast.","citation":"Mol Biol Cell 2006 Apr;17(4):1620-31","abstract":"Rho1p regulates cell integrity by controlling the actin cytoskeleton and cell wall synthesis. We have identified a new GEF, designated Rgf1p, which specifically regulates Rho1p during polarized growth. The phenotype of rgf1 null cells was very similar to that seen after depletion of Rho1p, 30% of cells being lysed. In addition, rgf1(+) deletion caused hypersensitivity to the antifungal drug Caspofungin and defects in the establishment of bipolar growth. rho1(+), but none of the other GTPases of the Rho-family, suppressed the rgf1Delta phenotypes. Moreover, deletion of rgf1(+) suppressed the severe growth defect in rga1(+) null mutants (a Rho1-GAP, negative regulator). Rgf1p and Rho1p coimmunoprecipitated and overexpression of rgf1(+) specifically increased the GTP-bound Rho1p; it caused changes in cell morphology, and a large increase in beta(1,3)-glucan synthase activity. These effects were similar to those elicited when the hyperactive rho1-G15V allele was expressed. A genetic relationship was observed between Rgf1p, Bgs4p (beta[1,3]-glucan synthase), and Pck1p (protein kinase C [PKC] homologue); Bgs4p and Pck1p suppressed the hypersensitivity to Caspofungin in rgf1Delta mutants. Rgf1p localized to the growing ends and the septum, where Rho1, Pck1p, and Bgs4p are known to function. Our results suggest that Rgf1p probably activates the Rho functions necessary for coordinating actin deposition with cell wall biosynthesis during bipolar growth, allowing the cells to remodel their wall without risk of rupture.","authors":"García P, Tajadura V, García I, Sánchez Y","authors_abbrev":"García P et al.","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-01-20","publication_year":"2006","canto_session_key":"0fd9142a80a1f4c8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2022-06-14 14:15:43","canto_approved_date":"2025-09-04 11:38:18","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-01-08 16:25:58","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":40,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC17G8.14c","SPAC1F7.04","SPCC645.07","SPAC23C4.08","SPAC20H4.11c","SPAC19B12.03","SPAC110.03","SPBC3F6.05","SPCC645.06c","SPBC12D12.04c","SPCC1840.02c","SPBC19G7.05c","SPAC24C9.07c","SPAC16.01","SPAC16A10.04"],"gene_count":15,"ltp_gene_count":13,"approved_date":"2022-06-14"},{"uniquename":"PMID:33257499","title":"An image analysis method to survey the dynamics of polar protein abundance in the regulation of tip growth.","citation":"J Cell Sci 2020 Nov 30;133(22)","abstract":"Tip growth is critical for the lifestyle of many walled cells. In yeast and fungi, this process is typically associated with the polarized deposition of conserved tip factors, including landmarks, Rho GTPases, cytoskeleton regulators, and membrane and cell wall remodelers. Because tip growth speeds may vary extensively between life cycles or species, we asked whether the local amount of specific polar elements could determine or limit tip growth speeds. Using the model fission yeast, we developed a quantitative image analysis pipeline to dynamically correlate single tip elongation speeds and polar protein abundance in large data sets. We found that polarity landmarks are typically diluted by growth. In contrast, tip growth speed is positively correlated with the local amount of factors related to actin, secretion or cell wall remodeling, but, surprisingly, exhibits long saturation plateaus above certain concentrations of those factors. Similar saturation observed for Spitzenkörper components in much faster growing fungal hyphae suggests that elements independent of canonical surface remodelers may limit single tip growth. This work provides standardized methods and resources to decipher the complex mechanisms that control cell growth.This article has an associated First Person interview with Sarah Taheraly, joint first author of the paper.","doi":"10.1242/jcs.252064","authors":"Taheraly S, Ershov D, Dmitrieff S, Minc N","authors_abbrev":"Taheraly S et al.","pubmed_publication_date":"30 Nov 2020","pubmed_entrez_date":"2020-12-01","publication_year":"2020","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-12-04 01:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012964","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31053168","title":"Transcriptomics data of 11 species of yeast identically grown in rich media and oxidative stress conditions.","citation":"BMC Res Notes 2019 May 03;12(1):250","abstract":"The objective of this experiment was to identify transcripts in baker's yeast (Saccharomyces cerevisiae) that could have originated from previously non-coding genomic regions, or de novo. We generated this data to be able to compare the transcriptomes of different species of Ascomycota.\nWe generated high-depth RNA sequencing data for 11 species of yeast: Saccharomyces cerevisiae, Saccharomyces paradoxus, Saccharomyces mikatae, Saccharomyces kudriavzevii, Saccharomyces bayanus, Naumovia castelii, Kluyveromyces lactis, Lachancea waltii, Lachancea thermotolerans, Lachancea kluyveri, and Schizosaccharomyces pombe. Using RNA-Seq from yeast grown in rich and oxidative conditions we created genome-guided de novo assemblies of the transcriptomes for each species. We included synthetic spike-in transcripts in each sample to determine the lower limit of detection of the sequencing platform as well as the reliability of our de novo transcriptome assembly pipeline. We subsequently compared the de novo transcripts assemblies to the reference gene annotations and generated assemblies that comprised both annotated and novel transcripts.","doi":"10.1186/s13104-019-4286-0","authors":"Blevins WR, Carey LB, Albà MM","authors_abbrev":"Blevins WR et al.","pubmed_publication_date":"03 May 2019","pubmed_entrez_date":"2019-05-05","publication_year":"2019","canto_session_key":"ccfaee077dcaf2d9","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2021-11-24 19:50:48","canto_approved_date":"2021-11-24 19:50:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-11-24 09:33:31","canto_added_date":"2019-05-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2021-11-24"},{"uniquename":"PMID:9092673","title":"An immunoaffinity purified Schizosaccharomyces pombe TBP-containing complex directs correct initiation of the S.pombe rRNA gene promoter.","citation":"Nucleic Acids Res 1997 Apr 15;25(8):1633-40","abstract":"The multi-protein complex SL1, containing TBP, which is essential for RNA polymerase I catalyzed transcription, has been analyzed in fission yeast. It was immunopurified based on association of component subunits with epitope-tagged TBP. To enable this analysis, a strain of Schizosaccharomyces pombe was created where the only functional TBP coding sequences were those of FLAG-TBP. RNA polymerase I transcription components were fractionated from this strain and the TBP-associated polypeptides were subsequently immunopurified together with the epitope- tagged TBP. An assessment of the activity of this candidate SL1 complex was undertaken cross-species. This fission yeast TBP-containing complex displays two activities in redirecting transcriptional initiation of an S. pombe rDNA gene promoter cross-species in Saccharomyces cerevisiae transcription reactions: it both blocks an incorrect transcriptional start site at +7 and directs initiation at the correct site for S. pombe rRNA synthesis. This complex is essential for accurate initiation of the S.pombe rRNA gene: rRNA synthesis is reconstituted when this S.pombe TBP-containing complex is combined with a S.pombe fraction immunodepleted of TBP.","authors":"Chen L, Guo A, Pape L","authors_abbrev":"Chen L et al.","pubmed_publication_date":"15 Apr 1997","pubmed_entrez_date":"1997-04-15","publication_year":"1997","canto_session_key":"b94f4ce3363d1f68","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-04-25 03:01:16","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-28 14:59:57","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29E6.08"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-28"},{"uniquename":"PMID:5982833","title":"[The role of protein sulfhydryl groups in the process of cell mitotic division].","citation":"Dokl Akad Nauk SSSR 1966 Feb 01;166(4):965-7","abstract":"","authors":"Alov IA, Aspiz ME","authors_abbrev":"Alov IA et al.","pubmed_publication_date":"01 Feb 1966","pubmed_entrez_date":"1966-02-01","publication_year":"1966","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-10-09 09:08:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34296454","title":"The TOR-dependent phosphoproteome and regulation of cellular protein synthesis.","citation":"EMBO J 2021 Aug 16;40(16):e107911","abstract":"Cell growth is orchestrated by a number of interlinking cellular processes. Components of the TOR pathway have been proposed as potential regulators of cell growth, but little is known about their immediate effects on protein synthesis in response to TOR-dependent growth inhibition. Here, we present a resource providing an in-depth characterisation of Schizosaccharomyces pombe phosphoproteome in relation to changes observed in global cellular protein synthesis upon TOR inhibition. We find that after TOR inhibition, the rate of protein synthesis is rapidly reduced and that notable phosphorylation changes are observed in proteins involved in a range of cellular processes. We show that this reduction in protein synthesis rates upon TOR inhibition is not dependent on S6K activity, but is partially dependent on the S. pombe homologue of eIF4G, Tif471. Our study demonstrates the impact of TOR-dependent phospho-regulation on the rate of protein synthesis and establishes a foundational resource for further investigation of additional TOR-regulated targets both in fission yeast and other eukaryotes.","doi":"10.15252/embj.2021107911","authors":"Mak T, Jones AW, Nurse P","authors_abbrev":"Mak T et al.","pubmed_publication_date":"16 Aug 2021","pubmed_entrez_date":"2021-07-23","publication_year":"2021","canto_session_key":"fb4d3db1b9346bf1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Tiffany Mak","canto_first_approved_date":"2021-11-04 14:45:32","canto_approved_date":"2022-02-24 14:00:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-10-27 14:49:17","canto_added_date":"2021-07-24 11:41:46","annotation_curators":[{"name":"Tiffany Mak","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":8,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"file_curator_name":"Val Wood","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Val Wood","community_curator":false,"annotation_count":908,"orcid":"0000-0001-6330-7526","file_type":"protein_modification","file_name":"PMID_34296454_modifications.tsv"}],"genes":["SPAC24H6.05","SPCC330.07c","SPAC15A10.02","SPBC18H10.04c","SPAC23E2.01","SPCC1672.11c","SPBC2D10.11c","SPAC30C2.06c","SPCC1183.06","SPCC1739.01","SPAC1B3.16c","SPBC16A3.01","SPAC8C9.15c","SPBC16A3.19","SPAC19A8.01c","SPAC19A8.05c","SPAC31G5.12c","SPCC4G3.11","SPCC188.02","SPAC9G1.10c","SPAC17G6.09","SPCC297.05","SPAC3H1.09c","SPAPB2B4.04c","SPAC13A11.01c","SPAC3A11.06","SPBP19A11.04c","SPAC11E3.11c","SPBC8D2.20c","SPAC1327.01c","SPBC15C4.05","SPAC1B9.02c","SPBC119.07","SPAP7G5.06","SPBC1289.10c","SPAC19E9.01c","SPBC14F5.03c","SPCC1259.08","SPCC70.05c","SPBC800.09","SPAC3G9.05","SPAC7D4.04","SPAC1006.09","SPAC821.12","SPAC2F7.02c","SPAC227.06","SPBC947.01","SPAC23G3.04","SPBC1709.18","SPAC3F10.11c","SPAC29B12.10c","SPBC26H8.01","SPBC1706.01","SPAC17A2.14","SPAC4H3.13","SPAC9G1.02","SPCC4G3.16","SPBC8D2.02c","SPAC22F8.09","SPCC584.04","SPBC1734.16c","SPAC32A11.03c","SPAC688.07c","SPAC890.05","SPBC13G1.09","SPAC22F8.08","SPAC926.06c","SPBC27B12.04c","SPAC521.04c","SPCC1795.02c","SPAC1952.13","SPCC1281.01","SPAC9.03c","SPAC1952.16","SPBC13G1.10c","SPAC2E1P3.04","SPBC1861.09","SPAC19G12.02c","SPBC19F8.03c","SPAC23G3.12c","SPCC757.09c","SPAC167.05","SPCC14G10.04","SPAC22E12.14c","SPAC458.02c","SPAC5D6.07c","SPCC18.04","SPAC12G12.03","SPAC22H10.11c","SPAC13G7.13c","SPAC821.03c","SPCC1393.08","SPCC1902.02","SPAC29A4.16","SPAC4A8.05c","SPAC57A7.08","SPCC645.06c","SPCC550.15c","SPCC1322.09","SPAC6G9.11","SPAC4A8.16c","SPCC338.17c","SPAPJ696.01c","SPBC2A9.04c","SPAC25G10.03","SPAC17A2.13c","SPCC2H8.02","SPCC285.14","SPBC30D10.10c","SPAC4D7.01c","SPCC1450.11c","SPAC32A11.04c","SPAC140.02","SPAPB1E7.12","SPCC31H12.08c","SPAC14C4.12c","SPCC4B3.15","SPCC1919.09","SPBC365.07c","SPCC18B5.07c","SPCC1223.06","SPAC2G11.04","SPAC328.06","SPAC24B11.10c","SPAC2F3.08","SPBC2F12.03c","SPBC16A3.07c","SPAC30.01c","SPAC27D7.03c","SPAC4F10.13c","SPAC1B3.05","SPAC18B11.06","SPAC25G10.09c","SPAC4G8.03c","SPAC13F5.02c","SPCC4G3.15c","SPBC19G7.05c","SPAC17C9.03","SPBP8B7.05c","SPAC458.07","SPCC1620.09c","SPAC10F6.16","SPBC530.05","SPCC970.08","SPCC584.13","SPAC56F8.03","SPAC23C4.10","SPBC31E1.04","SPCC1322.08","SPBC26H8.04c","SPCC5E4.06","SPAC29B12.02c","SPBC530.01","SPAC20G8.06","SPBC25B2.03","SPBC3B9.06c","SPAC30D11.11","SPBC4.02c","SPAC23G3.08c","SPAC23H3.15c","SPBC800.10c","SPBC1289.04c","SPAPB1A10.13","SPBC354.10","SPAC11E3.05","SPAC1F3.05","SPAC3H8.02","SPAC16C9.07","SPBP8B7.26","SPCC622.14","SPBC887.09c","SPCC364.06","SPBC106.04","SPCC1902.01","SPAPB1E7.05","SPBC530.04","SPCC777.05","SPCC594.02c","SPBC2F12.05c","SPBC23G7.06c","SPAC1F3.06c","SPBC216.07c","SPAC15A10.16","SPAC26H5.05","SPBC106.01","SPCC330.13","SPAC25B8.13c","SPAC2E12.02","SPBC29A3.04","SPAC3G6.04","SPBC119.09c","SPBC18H10.16","SPAC7D4.12c","SPAC1A6.07","SPAC24B11.07c","SPAC17G8.12","SPCC1020.10","SPAC29E6.06c","SPAC4F8.13c","SPAC57A10.10c","SPAC2C4.07c","SPAC22E12.16c","SPBC4F6.12","SPAC1782.09c","SPBC3E7.06c","SPCC4B3.07","SPAC4G8.05","SPAC23A1.09","SPAC16A10.01","SPCC1259.04","SPCC1919.03c","SPBC21.06c","SPBC32C12.03c","SPAC343.09","SPAC22A12.14c","SPBC428.10","SPBC2G2.12","SPAC23D3.06c","SPCC285.13c","SPAC22F3.13","SPAC29A4.11","SPCC584.15c","SPAC1F7.03","SPAC631.02","SPBC18E5.07","SPBC1604.12","SPCC4G3.08","SPAC1834.01","SPBC30D10.05c","SPBC409.07c","SPAC110.01","SPBC146.03c","SPAC9G1.06c","SPAC6G10.02c","SPBC29A10.17","SPBC6B1.02","SPCC16C4.09","SPBC16A3.08c","SPBC354.05c","SPAC20H4.03c","SPAC6F6.09","SPAC1687.04","SPCP1E11.04c","SPAC22F8.12c","SPBC13E7.03c","SPBPB7E8.02","SPCC191.01","SPAC3H5.08c","SPAC824.09c","SPCC1795.11","SPBC902.06","SPCC645.07","SPBC2G2.11","SPAC29B12.04","SPBC16H5.08c","SPAC16E8.09","SPBC354.13","SPAC24B11.11c","SPAC30D11.04c","SPBC16A3.18","SPBC16G5.15c","SPCC970.04c","SPAC589.03c","SPAC17H9.04c","SPBC4C3.06","SPCC162.12","SPAC607.07c","SPACUNK4.16c","SPAC29B12.07","SPCC1322.14c","SPBP8B7.11","SPCP31B10.06","SPCC1672.08c","SPAC2F7.03c","SPAC4G9.22","SPBC18H10.20c","SPBC28E12.06c","SPAC1B1.02c","SPAC22E12.17c","SPCC1393.02c","SPAC29E6.02","SPBC16C6.13c","SPBC17G9.08c","SPAC20G4.08","SPCC23B6.04c","SPBC17D1.05","SPAC144.14","SPBC1921.07c","SPBC11C11.02","SPCC622.10c","SPBC12C2.10c","SPAC16E8.01","SPBC16E9.02c","SPAC24H6.11c","SPAC14C4.11","SPAC4F10.07c","SPCC63.08c","SPBC16E9.13","SPBC2G2.03c","SPAC24H6.09","SPBC1D7.03","SPBC646.13","SPAC17A5.12","SPCC417.07c","SPBP18G5.03","SPCP1E11.02","SPBC660.07","SPCC895.07","SPBC15D4.07c","SPAC1687.09","SPAC227.07c","SPAC6F12.02","SPBC23E6.08","SPAC23A1.17","SPAC6G9.15c","SPCC1827.02c","SPCC16C4.16c","SPBP35G2.14","SPBC3F6.05","SPAC19G12.06c","SPAC16.05c","SPAC22F8.05","SPAC17C9.10","SPAC26F1.01","SPCC330.11","SPCC1739.14","SPAC4F8.11","SPAC1006.08","SPAC13G6.02c","SPBC405.02c","SPBC211.03c","SPCC594.01","SPBC3B9.10","SPAC10F6.06","SPCC16C4.07","SPAC20G8.05c","SPAC13C5.02","SPBC12C2.05c","SPAC6G10.12c","SPAC17H9.09c","SPBC557.04","SPBC215.05","SPBC26H8.02c","SPAC227.15","SPAC13G6.07c","SPCC622.08c"],"gene_count":346,"ltp_gene_count":5,"approved_date":"2021-11-04"},{"uniquename":"PMID:34382996","title":"Ultrastructural plasma membrane asymmetries in tension and curvature promote yeast cell fusion.","citation":"J Cell Biol 2021 Oct 04;220(10)","abstract":"Cell-cell fusion is central for sexual reproduction, and generally involves gametes of different shapes and sizes. In walled fission yeast Schizosaccharomyces pombe, the fusion of h+ and h- isogametes requires the fusion focus, an actin structure that concentrates glucanase-containing vesicles for cell wall digestion. Here, we present a quantitative correlative light and electron microscopy (CLEM) tomographic dataset of the fusion site, which reveals the fusion focus ultrastructure. Unexpectedly, gametes show marked asymmetries: a taut, convex plasma membrane of h- cells progressively protrudes into a more slack, wavy plasma membrane of h+ cells. Asymmetries are relaxed upon fusion, with observations of ramified fusion pores. h+ cells have a higher exo-/endocytosis ratio than h- cells, and local reduction in exocytosis strongly diminishes membrane waviness. Reciprocally, turgor pressure reduction specifically in h- cells impedes their protrusions into h+ cells and delays cell fusion. We hypothesize that asymmetric membrane conformations, due to differential turgor pressure and exocytosis/endocytosis ratios between mating types, favor cell-cell fusion.","doi":"10.1083/jcb.202103142","authors":"Muriel O, Michon L, Kukulski W, Martin SG","authors_abbrev":"Muriel O et al.","pubmed_publication_date":"04 Oct 2021","pubmed_entrez_date":"2021-08-12","publication_year":"2021","canto_session_key":"465d15e06c53416f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2021-10-07 11:32:14","canto_approved_date":"2023-06-09 11:39:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-10-01 15:25:51","canto_added_date":"2021-08-14 00:15:04","annotation_curators":[{"name":"Sophie Martin","community_curator":true,"annotation_count":11,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":4,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1919.10c","SPAC29A4.11","SPAC20G4.02c","SPAC18G6.03","SPBC17F3.01c","SPBC354.13","SPBC28E12.03","SPBC1778.06c","SPBC215.05","SPAC6F12.08c"],"gene_count":10,"ltp_gene_count":4,"approved_date":"2021-10-07"},{"uniquename":"PANTHER:PTHR15492","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:1587","SPAC22E12.18"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:38058121","title":"Diversity and functional specialization of H3K9-specific histone methyltransferases.","citation":"Bioessays 2023 Dec 06;:e2300163","abstract":"Histone modifications play a critical role in the control over activities of the eukaryotic genome; among these chemical alterations, the methylation of lysine K9 in histone H3 (H3K9) is one of the most extensively studied. The number of enzymes capable of methylating H3K9 varies greatly across different organisms: in fission yeast, only one such methyltransferase is present, whereas in mammals, 10 are known. If there are several such enzymes, each of them must have some specific function, and they can interact with one another. Thus arises a complex system of interchangeability, \"division of labor,\" and contacts with each other and with diverse proteins. Histone methyltransferases specialize in the number of methyl groups that they attach and have different intracellular localizations as well as different distributions on chromosomes. Each also shows distinct binding to different types of sequences and has a specific set of nonhistone substrates.","doi":"10.1002/bies.202300163","authors":"Koryakov DE","authors_abbrev":"Koryakov DE","pubmed_publication_date":"06 Dec 2023","pubmed_entrez_date":"2023-12-07","publication_year":"2023","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2023-12-08 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:54096","title":"[Proceedings: Combined effect of an inhibitor of mitochondrial nucleotide translocation and a respiratory inhibitor on growth of the yeast Schizosaccharomyces pombe].","citation":"Arch Int Physiol Biochim 1975 May;83(2):379-80","abstract":"","authors":"Labaille MF, Goffeau A","authors_abbrev":"Labaille MF et al.","pubmed_publication_date":"May 1975","pubmed_entrez_date":"1975-05-01","publication_year":"1975","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19028693","title":"Incompatibility with formin Cdc12p prevents human profilin from substituting for fission yeast profilin: insights from crystal structures of fission yeast profilin.","citation":"J Biol Chem 2009 Jan 23;284(4):2088-97","abstract":"Expression of human profilin-I does not complement the temperature-sensitive cdc3-124 mutation of the single profilin gene in fission yeast Schizosaccharomyces pombe, resulting in death from cytokinesis defects. Human profilin-I and S. pombe profilin have similar affinities for actin monomers, the FH1 domain of fission yeast formin Cdc12p and poly-L-proline (Lu, J., and Pollard, T. D. (2001) Mol. Biol. Cell 12, 1161-1175), but human profilin-I does not stimulate actin filament elongation by formin Cdc12p like S. pombe profilin. Two crystal structures of S. pombe profilin and homology models of S. pombe profilin bound to actin show how the two profilins bind to identical surfaces on animal and yeast actins even though 75% of the residues on the profilin side of the interaction differ in the two profilins. Overexpression of human profilin-I in fission yeast expressing native profilin also causes cytokinesis defects incompatible with viability. Human profilin-I with the R88E mutation has no detectable affinity for actin and does not have this dominant overexpression phenotype. The Y6D mutation reduces the affinity of human profilin-I for poly-l-proline by 1000-fold, but overexpression of Y6D profilin in fission yeast is lethal. The most likely hypotheses to explain the incompatibility of human profilin-I with Cdc12p are differences in interactions with the proline-rich sequences in the FH1 domain of Cdc12p and wider \"wings\" that interact with actin.","doi":"10.1074/jbc.M807073200","authors":"Ezezika OC, Younger NS, Lu J, Kaiser DA, Corbin ZA, Nolen BJ, Kovar DR, Pollard TD","authors_abbrev":"Ezezika OC et al.","pubmed_publication_date":"23 Jan 2009","pubmed_entrez_date":"2008-11-26","publication_year":"2009","canto_session_key":"b70bd196896e5558","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2023-02-20 16:03:11","canto_approved_date":"2023-02-20 16:03:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-02-20 16:02:54","canto_added_date":"2012-02-24 05:48:12","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.15c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2023-02-20","pdb_entries":[{"pdb_id":"3d9y","gene_chains":[{"gene_uniquename":"SPAC4A8.15c","chain":"A/B","position":"1-127"}],"title":"Crystal Structure of Profilin from Schizosaccharomyces pombe","entry_authors":"Ezezika OC,Nolen BJ,Pollard TD","entry_authors_abbrev":"Ezezika OC et al.","reference_uniquename":"PMID:19028693","experimental_method":"X-ray","resolution":"1.65"},{"pdb_id":"3dav","gene_chains":[{"gene_uniquename":"SPAC4A8.15c","chain":"A/B","position":"1-127"}],"title":"Schizosaccharomyces Pombe Profilin crystallized from Sodium formate","entry_authors":"Ezezika OC,Nolen BJ,Pollard TD","entry_authors_abbrev":"Ezezika OC et al.","reference_uniquename":"PMID:19028693","experimental_method":"X-ray","resolution":"2.2"}]},{"uniquename":"PMID:14745780","title":"A DNA microarray for fission yeast: minimal changes in global gene expression after temperature shift.","citation":"Yeast 2004 Jan 15;21(1):25-39","abstract":"Completion of the fission yeast genome sequence has opened up possibilities for post-genomic approaches. We have constructed a DNA microarray for genome-wide gene expression analysis in fission yeast. The microarray contains DNA fragments, PCR-amplified from a genomic DNA template, that represent > 99% of the 5000 or so annotated fission yeast genes, as well as a number of control sequences. The GenomePRIDE software used attempts to design similarly sized DNA fragments corresponding to gene regions within single exons, near the 3'-end of genes that lack homology to other fission yeast genes. To validate the design and utility of the array, we studied expression changes after a 2 h temperature shift from 25 degrees C to 36 degrees C, conditions widely used when studying temperature-sensitive mutants. Obligingly, the vast majority of genes do not change more than two-fold, supporting the widely held view that temperature-shift experiments specifically reveal phenotypes associated with temperature-sensitive mutants. However, we did identify a small group of genes that showed a reproducible change in expression. Importantly, most of these corresponded to previously characterized heat-shock genes, whose expression has been reported to change after more extreme temperature shifts than those used here. We conclude that the DNA microarray represents a useful resource for fission yeast researchers as well as the broader yeast community, since it will facilitate comparison with the distantly related budding yeast, Saccharomyces cerevisiae. To maximize the utility of this resource, the array and its component parts are fully described in On-line Supplementary Information and are also available commercially.","authors":"Xue Y, Haas SA, Brino L, Gusnanto A, Reimers M, Talibi D, Vingron M, Ekwall K, Wright AP","authors_abbrev":"Xue Y et al.","pubmed_publication_date":"15 Jan 2004","pubmed_entrez_date":"2004-01-28","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1729693","title":"Chromosomal context dependence of a eukaryotic recombinational hot spot.","citation":"Proc Natl Acad Sci U S A 1992 Jan 01;89(1):227-31","abstract":"The single base-pair mutation M26 in the ade6 gene of the fission yeast Schizosaccharomyces pombe creates a hot spot for meiotic homologous recombination. When DNA fragments containing M26 and up to 3.0 kilobases of surrounding DNA were moved to the ura4 gene or to a multicopy plasmid, M26 had no detectable hot spot activity. Our results indicate that nucleotide sequences at least 1 kilobase away from M26 are required for M26 hot spot activity and suggest that, as for transcriptional promoters, a second site or proper chromatin structure is required for activation of this eukaryotic recombinational hot spot. We discuss the implications of these results for studies of other meiotic recombinational hot spots and for gene targeting.","authors":"Ponticelli AS, Smith GR","authors_abbrev":"Ponticelli AS et al.","pubmed_publication_date":"01 Jan 1992","pubmed_entrez_date":"1992-01-01","publication_year":"1992","canto_triage_status":"DNA recombination related","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18628853","title":"Upstream - news in genomics.","citation":"Comp Funct Genomics 2002;3(3):221-5","abstract":"In recent months a bumper crop of genomes has been completed, including the fission yeast (Schizosaccharomyces pombe) and rice (Oryza sativa). Two large-scale studies of Saccharomyces cerevisiae protein complexes provided a picture of the eukaryotic proteome as a network of complexes. Amongst the other stories of interest was a demonstration that proteomic analysis of blood samples can be used to detect ovarian cancer, perhaps even as early as stage I.","doi":"10.1002/cfg.172","authors":"","authors_abbrev":"","pubmed_publication_date":"2002","pubmed_entrez_date":"2008-07-17","publication_year":"2002","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:1563349","title":"Checkpoint controls in Schizosaccharomyces pombe: rad1.","citation":"EMBO J 1992 Apr;11(4):1335-42","abstract":"'Checkpoint' controls ensure that the events of the cell cycle are completed in an orderly fashion. For example, such controls delay mitosis until DNA synthesis and repair of radiation-induced DNA damage are complete. The rad series of radiosensitive fission yeast mutants was examined to identify strains deficient for the DNA damage-responsive checkpoint control. Five were identified. A characterization of one (rad1-1) and the wild-type is presented. The rad1-1 mutant does not arrest after irradiation, is sensitive to killing by radiation and is not arrested by hydroxyurea, and thus is also deficient for the DNA synthesis-responsive checkpoint control. The radiosensitivity of the rad1-1 mutant was greatly reduced when irradiated and maintained for 6 h in a non-dividing (density inhibited) state, demonstrating that rad1-1 is repair proficient and radiosensitive only through failure to delay. The checkpoint controls for which rad1 is required appear to regulate G2-M progression through the activity of cdc2, here implicated in this role by the coincidence of the radiation transition point and the cdc2 execution point.","authors":"Rowley R, Subramani S, Young PG","authors_abbrev":"Rowley R et al.","pubmed_publication_date":"Apr 1992","pubmed_entrez_date":"1992-04-01","publication_year":"1992","canto_session_key":"69403b8ceb819841","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2013-02-17 13:35:00","canto_approved_date":"2019-06-06 09:44:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-17 13:34:44","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":18,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G8.01","SPAC1952.07","SPAC14C4.13","SPAC23C4.18c","SPBC11B10.09","SPBC216.05","SPAC664.07c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2013-02-17"},{"uniquename":"PMID:12084729","title":"Comparison of Cak1p-like cyclin-dependent kinase-activating kinases.","citation":"J Biol Chem 2002 Sep 06;277(36):33482-9","abstract":"Cyclin-dependent kinases (cdks) coordinate progression through the eukaryotic cell cycle and require phosphorylation by a cdk-activating kinase (CAK) for full activity. In most eukaryotes Cdk7 is the catalytic subunit of a heterotrimeric CAK (Cdk7-cyclin H-Mat1) that is also involved in transcription as part of the transcription factor IIH complex. The Saccharomyces cerevisiae CAK, Cak1p, is a monomeric protein kinase with an atypical sequence and unusual biochemical properties compared with trimeric CAKs and other protein kinases. We sought to determine whether these properties were shared by a small group of monomeric CAKs that can function in place of CAK1 in S. cerevisiae. We found that Schizosaccharomyces pombe Csk1, Candida albicans Cak1, and Arabidopsis thaliana Cak1At, like Cak1p, all displayed a preference for cyclin-free cdk substrates, were insensitive to the protein kinase inhibitor 5'-fluorosulfonylbenzoyladenosine (FSBA), and were insensitive to mutation of a highly conserved lysine residue found in the nucleotide binding pocket of all protein kinases. The S. pombe and C. albicans kinases also resembled Cak1p in their kinetics of nucleotide and protein substrate utilization. Conservation of these unusual properties in fungi and plants points to shared evolutionary requirements not met by Cdk7 and raises the possibility of developing antifungal agents targeting CAKs.","authors":"Tsakraklides V, Solomon MJ","authors_abbrev":"Tsakraklides V et al.","pubmed_publication_date":"06 Sep 2002","pubmed_entrez_date":"2002-06-27","publication_year":"2002","canto_session_key":"0cb771b42fc56c00","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2014-08-07 14:06:23","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2014-08-07 14:04:43","canto_added_date":"2012-02-24 05:51:16","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1D4.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-07"},{"uniquename":"PMID:5158751","title":"[Replicating instability in a series of cell generations using Schizosaccharomyces pombe yeasts as an example].","citation":"Dokl Akad Nauk SSSR 1971;201(6):1469-72","abstract":"","authors":"Kurennaia ON, Dubinin NP, Kurlapova LD, Tarasov VA","authors_abbrev":"Kurennaia ON et al.","pubmed_publication_date":"1971","pubmed_entrez_date":"1971-01-01","publication_year":"1971","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:13407436","title":"[Remote hybridization of yeasts. III. Production of hybrids Saccharomyces cerevisiae (race XII) and Schizosaccharomyces pombe by copulation of growing spore].","citation":"Mikrobiologiia 1956;25(5):533-6","abstract":"","authors":"KOSIKOV KV","authors_abbrev":"KOSIKOV KV","pubmed_publication_date":"1956","pubmed_entrez_date":"1956-09-01","publication_year":"1956","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8955892","title":"Identification and characterization of a mitochondrial endonuclease from yeast, Schizosaccharomyces pombe.","citation":"Biochem Mol Biol Int 1996 Nov;40(5):1017-24","abstract":"Schizosaccharomyces pombe mitochondria were isolated from the cells treated with Novozyme 234, and purified in a Percoll gradient. A zymographic assay in a SDS-polyacrylamide gel containing single-stranded DNA revealed that an endonuclease of 32 kDa is associated with the mitochondria. The endonuclease was extracted from the mitochondria with 0.5 M KCl and was partially purified. The 32-kDa enzyme degraded both DNA and RNA at a weak alkaline pH, but preferred single-stranded DNA. The enzyme required Mg2+ or Mn2+, but not Ca2+ or Zn2+ for activity, and was inhibited by 50% with a 150 mM salt solution. Nicks generated by the enzyme could be resealed with T4 DNA ligase, indicating that the enzyme produces 5'-P and 3'-OH ends.","authors":"Ikeda S, Maeda N, Ohshima T, Takata N","authors_abbrev":"Ikeda S et al.","pubmed_publication_date":"Nov 1996","pubmed_entrez_date":"1996-11-01","publication_year":"1996","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7883793","title":"Coupling of DNA replication and mitosis by fission yeast rad4/cut5.","citation":"J Cell Sci Suppl 1994;18:57-61","abstract":"The fission yeast cut5+ (identical to rad4+) gene is essential for S phase. Its temperature-sensitive (ts) mutation causes mitosis while S phase is inhibited: dependence of mitosis upon the completion of S phase is abolished. If DNA is damaged in mutant cells, however, cell division is arrested. Thus the checkpoint control system for DNA damage is functional, while that for DNA synthesis inhibition is not in the cut5 mutants. Transcription of the cut5+ gene is not under the direct control of cdc10+, which encodes a transcription factor for the START of cell cycle. The transcript level does not change during the cell cycle. The protein product has four distinct domains and is enriched in the nucleus. Its level does not alter during the cell cycle. The N-domain is important for cut5 protein function: it is essential for complementation of ts cut5 mutations and its overexpression blocks cell division. Furthermore, it resembles the N-terminal repeat domain of proto-oncoprotein Ect2, which, in the C-domain, contains a regulator-like sequence for small G proteins. We discuss a hypothesis that the cut5 protein is an essential component of the checkpoint control system for the completion of DNA synthesis. The restraint of mitosis until the completion of S phase is mediated by the cut5 protein, which can sense the state of chromosome duplication and negatively interacts with M phase regulators such as cdc25 and cdc2.","authors":"Saka Y, Fantes P, Yanagida M","authors_abbrev":"Saka Y et al.","pubmed_publication_date":"1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8890634","title":"[The fission yeast cdc18+ gene links S phase to START and plays a major role in the initiation of DNA replication].","citation":"Tanpakushitsu Kakusan Koso 1996 Sep;41(12 Suppl):1761-8","abstract":"","authors":"Nishitani H","authors_abbrev":"Nishitani H","pubmed_publication_date":"Sep 1996","pubmed_entrez_date":"1996-09-01","publication_year":"1996","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:53:54","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23200991","title":"Cdc42 explores the cell periphery for mate selection in fission yeast.","citation":"Curr Biol 2013 Jan 07;23(1):42-7","abstract":"How cells polarize in response to external cues is a fundamental biological problem. For mating, yeast cells orient growth toward the source of a pheromone gradient produced by cells of the opposite mating type. Polarized growth depends on the small GTPase Cdc42, a central eukaryotic polarity regulator that controls signaling, cytoskeleton polarization, and vesicle trafficking. However, the mechanisms of polarity establishment and mate selection in complex cellular environments are poorly understood. Here we show that, in fission yeast, low-level pheromone signaling promotes a novel polarization state, where active Cdc42, its GEF Scd1, and scaffold Scd2 form colocalizing dynamic zones that sample the periphery of the cell. Two direct Cdc42 effectors--actin cables marked by myosin V Myo52 and the exocyst complex labeled by Sec6 and Sec8--also dynamically colocalize with active Cdc42. However, these cells do not grow due to a block in the exocytosis of cell wall synthases Bgs1 and Bgs4. High-level pheromone stabilizes active Cdc42 zones and promotes cell wall synthase exocytosis and polarized growth. However, in the absence of prior low-level pheromone signaling, exploration fails, and cells polarize growth at cell poles by default. Consequently, these cells show altered partner choice, mating preferentially with sister rather than nonsister cells. Thus, Cdc42 exploration serves to orient growth for partner selection. This process may also promote genetic diversification.","doi":"10.1016/j.cub.2012.10.042","authors":"Bendezú FO, Martin SG","authors_abbrev":"Bendezú FO et al.","pubmed_publication_date":"07 Jan 2013","pubmed_entrez_date":"2012-12-04","publication_year":"2013","canto_session_key":"71e50efc69bcd7d5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Sophie Martin","canto_first_approved_date":"2016-12-01 15:02:22","canto_approved_date":"2022-08-03 10:20:58","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2016-11-15 15:47:24","canto_added_date":"2013-01-03 02:47:33","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Sophie Martin","community_curator":true,"annotation_count":13,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.03","SPAC3F10.10c","SPBC19G7.05c","SPCC1235.10c","SPAC22H10.07","SPCC1919.10c","SPAC16E8.09","SPAC22F3.12c"],"gene_count":8,"ltp_gene_count":8,"approved_date":"2016-12-01"},{"uniquename":"PMID:22733402","title":"Centromeric heterochromatin assembly in fission yeast--balancing transcription, RNA interference and chromatin modification.","citation":"Chromosome Res 2012 Jul;20(5):521-34","abstract":"Distinct regions of the eukaryotic genome are packaged into different types of chromatin, with euchromatin representing gene rich, transcriptionally active regions and heterochromatin more condensed and gene poor. The assembly and maintenance of heterochromatin is important for many aspects of genome control, including silencing of gene transcription, suppression of recombination, and to ensure proper chromosome segregation. The precise mechanisms underlying heterochromatin establishment and maintenance are still unclear, but much progress has been made towards understanding this process during the last few years, particularly from studies performed in fission yeast. In this review, we hope to provide a conceptual model of centromeric heterochromatin in fission yeast that integrates our current understanding of the competing forces of transcription, replication, and RNA decay that influence its assembly and propagation.","doi":"10.1007/s10577-012-9288-x","authors":"Alper BJ, Lowe BR, Partridge JF","authors_abbrev":"Alper BJ et al.","pubmed_publication_date":"Jul 2012","pubmed_entrez_date":"2012-06-27","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18023413","title":"Dss1 associating with the proteasome functions in selective nuclear mRNA export in yeast.","citation":"Biochem Biophys Res Commun 2008 Jan 25;365(4):664-71","abstract":"Dss1p is an evolutionarily conserved small protein that interacts with BRCA2, a tumor suppressor protein, in humans. The Schizosaccharomyces pombe strain lacking the dss1(+) gene (Deltadss1) shows a temperature-sensitive growth defect and accumulation of bulk poly(A)(+) RNA in the nucleus at a nonpermissive temperature. In situ hybridization using probes for several specific mRNAs, however, revealed that the analyzed mRNAs were exported normally to the cytoplasm in Deltadss1, suggesting that Dss1p is required for export of some subsets of mRNAs. We identified the pad1(+) gene, which encodes a component of the 26S proteasome, as a suppressor for the ts(-) phenotype of Deltadss1. Unexpectedly, overexpression of Pad1p could suppress neither the defect in nuclear mRNA export nor a defect in proteasome function. In addition, loss of proteasome functions does not cause defective nuclear mRNA export. Dss1p seems to be a multifunctional protein involved in nuclear export of specific sets of mRNAs and the ubiquitin-proteasome pathway in fission yeast.","authors":"Mannen T, Andoh T, Tani T","authors_abbrev":"Mannen T et al.","pubmed_publication_date":"25 Jan 2008","pubmed_entrez_date":"2007-11-21","publication_year":"2008","canto_session_key":"a2af386d7f306918","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-11-20 13:34:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-20 13:34:00","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC29E6.08","SPBC16G5.01","SPBC215.05","SPAC3G6.02","SPBC4.07c","SPAC31G5.13","SPBC16A3.05c"],"gene_count":7,"ltp_gene_count":5,"approved_date":"2014-11-20"},{"uniquename":"PMID:8388878","title":"Cell cycle-dependent specific positioning and clustering of centromeres and telomeres in fission yeast.","citation":"J Cell Biol 1993 Jun;121(5):961-76","abstract":"Fluorescence in situ hybridization (FISH) shows that fission yeast centromeres and telomeres make up specific spatial arrangements in the nucleus. Their positioning and clustering are cell cycle regulated. In G2, centromeres cluster adjacent to the spindle pole body (SPB), while in mitosis, their association with each other and with the SPB is disrupted. Similarly, telomeres cluster at the nuclear periphery in G2 and their associations are disrupted in mitosis. Mitotic centromeres interact with the spindle. They remain undivided until the spindle reaches a critical length, then separate and move towards the poles. This demonstrated, for the first time, that anaphase A occurs in fission yeast. The mode of anaphase A and B is similar to that of higher eukaryotes. In nda3 and cut7 mutants defective in tubulin of a kinesin-related motor, cells are blocked in early stages of mitosis due to the absence of the spindle, and centromeres dissociate but remain close to the SPB, whereas in a metaphase-arrested nuc2 mutant, they reside at the middle of the spindle. FISH is therefore a powerful tool for analyzing mitotic chromosome movement and disjunction using various mutants. Surprisingly, in top2 defective in DNA topoisomerase II, while most chromatid DNAs remain undivided, sister centromeres are separated. Significance of this finding is discussed. In contrast, most chromatid DNAs are separated but telomeric DNAs are not in cut1 mutant. In cut1, the dependence of SPB duplication on the completion of mitosis is abolished. In crm1 mutant cells defective in higher-order chromosome organization, the interphase arrangements of centromeres and telomeres are disrupted.","authors":"Funabiki H, Hagan I, Uzawa S, Yanagida M","authors_abbrev":"Funabiki H et al.","pubmed_publication_date":"Jun 1993","pubmed_entrez_date":"1993-06-01","publication_year":"1993","canto_session_key":"7757853a6136d59d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2013-02-09 21:28:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-28 17:15:48","canto_added_date":"2012-02-24 05:54:46","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1A4.03c","SPAC17C9.01c","SPAC1805.17","SPCC5E4.04","SPAC25G10.07c","SPBC26H8.07c"],"gene_count":6,"ltp_gene_count":1,"approved_date":"2013-01-28"},{"uniquename":"PMID:7199315","title":"Mutagenicity studies on fenticonazole, a new antifungal imidazole derivative.","citation":"Arzneimittelforschung 1981;31(12):2142-4","abstract":"The forward mutational assay on Schizosaccharomyces pombe and the mitotic gene conversion assay on Saccharomyces cerevisiae were performed in order to verify whether alpha-(2,4-dichlorophenyl)-beta,N-imidazolylethyl 4-phenylthiobenzyl ether nitrate (fenticonazole, Rec 15/1476) shows a potential mutagenicity. In both tests the drug does not seem to possess any mutagenic activity when compared with mutagenic standards.","authors":"Veronese M, Barzaghi D, Bertoncini A, Zadro M","authors_abbrev":"Veronese M et al.","pubmed_publication_date":"1981","pubmed_entrez_date":"1981-01-01","publication_year":"1981","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31010665","title":"Theory of Cytoskeletal Reorganization during Cross-Linker-Mediated Mitotic Spindle Assembly.","citation":"Biophys J 2019 May 07;116(9):1719-1731","abstract":"Cells grow, move, and respond to outside stimuli by large-scale cytoskeletal reorganization. A prototypical example of cytoskeletal remodeling is mitotic spindle assembly, during which microtubules nucleate, undergo dynamic instability, bundle, and organize into a bipolar spindle. Key mechanisms of this process include regulated filament polymerization, cross-linking, and motor-protein activity. Remarkably, using passive cross-linkers, fission yeast can assemble a bipolar spindle in the absence of motor proteins. We develop a torque-balance model that describes this reorganization because of dynamic microtubule bundles, spindle-pole bodies, the nuclear envelope, and passive cross-linkers to predict spindle-assembly dynamics. We compare these results to those obtained with kinetic Monte Carlo-Brownian dynamics simulations, which include cross-linker-binding kinetics and other stochastic effects. Our results show that rapid cross-linker reorganization to microtubule overlaps facilitates cross-linker-driven spindle assembly, a testable prediction for future experiments. Combining these two modeling techniques, we illustrate a general method for studying cytoskeletal network reorganization.","doi":"10.1016/j.bpj.2019.03.013","authors":"Lamson AR, Edelmaier CJ, Glaser MA, Betterton MD","authors_abbrev":"Lamson AR et al.","pubmed_publication_date":"07 May 2019","pubmed_entrez_date":"2019-04-24","publication_year":"2019","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2019-04-25 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8043756","title":"Theoretical dynamics of the cyclin B-MPF system: a possible role for p13suc1.","citation":"Biosystems 1994;32(2):97-109","abstract":"In dividing cells, entry into mitosis is caused by maturation promoting factor (MPF), which is formed autocatalytically by activation of a complex of p34cdc2 and cyclin B. This biochemical system may oscillate, causing repeated mitosis. It is shown mathematically that the oscillatory tendency would be enhanced by a cofactor which binds to MPF and inhibits its autocatalytic action. A candidate for such a cofactor is the suc1 gene product p13, which binds to p34cdc2/cyclin B complex and inhibits MPF-induced MPF activation. At a steady rate of cyclin biosynthesis, with small amounts converted to MPF, p13suc1 would have to be titrated by MPF before autocatalysis could begin. This would have three possibly important effects: (1) it would determine the 'threshold' cyclin accumulation (and hence the corresponding time-delay) for MPF activation; (2) it would cause the accumulation of a backlog of MPF precursor (tyrosine-phosphorylated p34cdc2/cyclin B) sufficient to produce a substantial MPF pulse when MPF autocatalysis begins; (3) it would give the autocatalysis a high reaction order, which tends to destabilize the steady state, promote autonomous oscillations, and enhance the triggering property (excitability) of the system. The MPF pulse generated by this system may be essential for the proper triggering of the events of M phase, including the cyclin degradation which inactivates MPF at the end of M phase. This model offers explanations for several puzzling effects of p13suc1, including the fact that p13suc1, though an inhibitor of MPF activation, is nevertheless necessary for mitosis.","authors":"Thron CD","authors_abbrev":"Thron CD","pubmed_publication_date":"1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:35584675","title":"Zng1 is a GTP-dependent zinc transferase needed for activation of methionine aminopeptidase.","citation":"Cell Rep 2022 May 17;39(7):110834","abstract":"The evolution of zinc (Zn) as a protein cofactor altered the functional landscape of biology, but dependency on Zn also created an Achilles' heel, necessitating adaptive mechanisms to ensure Zn availability to proteins. A debated strategy is whether metallochaperones exist to prioritize essential Zn-dependent proteins. Here, we present evidence for a conserved family of putative metal transferases in human and fungi, which interact with Zn-dependent methionine aminopeptidase type I (MetAP1/Map1p/Fma1). Deletion of the putative metal transferase in Saccharomyces cerevisiae (ZNG1; formerly YNR029c) leads to defective Map1p function and a Zn-deficiency growth defect. In vitro, Zng1p can transfer Zn 2+  or Co 2+  to apo-Map1p, but unlike characterized copper chaperones, transfer is dependent on GTP hydrolysis. Proteomics reveal mis-regulation of the Zap1p transcription factor regulon because of loss of ZNG1 and Map1p activity, suggesting that Zng1p is required to avoid a compounding effect of Map1p dysfunction on survival during Zn limitation.","doi":"10.1016/j.celrep.2022.110834","authors":"Pasquini M, Grosjean N, Hixson KK, Nicora CD, Yee EF, Lipton M, Blaby IK, Haley JD, Blaby-Haas CE","authors_abbrev":"Pasquini M et al.","pubmed_publication_date":"17 May 2022","pubmed_entrez_date":"2022-05-18","publication_year":"2022","canto_session_key":"d2876b218a4ffe9d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-10-19 15:21:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC15D4.05"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:37243596","title":"Stn1-Ten1 and Taz1 independently promote replication of subtelomeric fragile sequences in fission yeast.","citation":"Cell Rep 2023 Jun 27;42(6):112537","abstract":"Efficient replication of terminal DNA is crucial to maintain telomere stability. In fission yeast, Taz1 and the Stn1-Ten1 (ST) complex play prominent roles in DNA-ends replication. However, their function remains elusive. Here, we have analyzed genome-wide replication and show that ST does not affect genome-wide replication but is crucial for the efficient replication of a subtelomeric region called STE3-2. We further show that, when ST function is compromised, a homologous recombination (HR)-based fork restart mechanism becomes necessary for STE3-2 stability. While both Taz1 and Stn1 bind to STE3-2, we find that the STE3-2 replication function of ST is independent of Taz1 but relies on its association with the shelterin proteins Pot1-Tpz1-Poz1. Finally, we demonstrate that the firing of an origin normally inhibited by Rif1 can circumvent the replication defect of subtelomeres when ST function is compromised. Our results help illuminate why fission yeast telomeres are terminal fragile sites.","doi":"10.1016/j.celrep.2023.112537","authors":"Vaurs M, Naiman K, Bouabboune C, Rai S, Ptasińska K, Rives M, Matmati S, Carr AM, Géli V, Coulon S","authors_abbrev":"Vaurs M et al.","pubmed_publication_date":"27 Jun 2023","pubmed_entrez_date":"2023-05-27","publication_year":"2023","canto_session_key":"320471d563a0eb2e","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2023-05-28 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC16A10.07c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:20231270","title":"Schizosaccharomyces pombe Dss1p is a DNA damage checkpoint protein that recruits Rad24p, Cdc25p, and Rae1p to DNA double-strand breaks.","citation":"J Biol Chem 2010 May 07;285(19):14122-33","abstract":"Schizosaccharomyces pombe Dss1p and its homologs function in multiple cellular processes including recombinational repair of DNA and nuclear export of messenger RNA. We found that Tap-tagged Rad24p, a member of the 14-3-3 class of proteins, co-purified Dss1p along with mitotic activator Cdc25p, messenger RNA export/cell cycle factor Rae1p, 19 S proteasomal factors, and recombination protein Rhp51p (a Rad51p homolog). Using chromatin immunoprecipitation, we found that Dss1p recruited Rad24p and Rae1p to the double-strand break (DSB) sites. Furthermore, Cdc25p also recruited to the DSB site, and its recruitment was dependent on Dss1p, Rad24p, and the protein kinase Chk1p. Following DSB, all nuclear Cdc25p was found to be chromatin-associated. We found that Dss1p and Rae1p have a DNA damage checkpoint function, and upon treatment with UV light Deltadss1 cells entered mitosis prematurely with indistinguishable timing from Deltarad24 cells. Taken together, these results suggest that Dss1p plays a critical role in linking repair and checkpoint factors to damaged DNA sites by specifically recruiting Rad24p and Cdc25p to the DSBs. We suggest that the sequestration of Cdc25p to DNA damage sites could provide a mechanism for S. pombe cells to arrest at G(2)/M boundary in response to DNA damage.","doi":"10.1074/jbc.M109.083485","authors":"Selvanathan SP, Thakurta AG, Dhakshnamoorthy J, Zhou M, Veenstra TD, Dhar R","authors_abbrev":"Selvanathan SP et al.","pubmed_publication_date":"07 May 2010","pubmed_entrez_date":"2010-03-17","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC644.14c","SPAC3G6.02","SPAPB8E5.02c","SPAC23G3.11","SPAC17C9.03","SPBC17D11.05","SPAC8E11.02c","SPCC1739.13","SPBC16A3.05c","SPBP19A11.03c","SPAC13G7.02c","SPAC25G10.08","SPAC1F7.05","SPBC4.07c","SPAC1420.03","SPAC24H6.05","SPAC20G8.05c","SPAC17A2.13c"],"gene_count":18,"ltp_gene_count":18},{"uniquename":"EMBL:AU008061","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12409469","title":"The severe slow growth of Deltasrs2 Deltarqh1 in Schizosaccharomyces pombe is suppressed by loss of recombination and checkpoint genes.","citation":"Nucleic Acids Res 2002 Nov 01;30(21):4781-92","abstract":"Our interest in the Schizosaccharomyces pombe RecQ helicase, rqh1+, led us to investigate the function of a related putative DNA helicase, srs2+. We identified the srs2+ homolog in S.pombe, and found that srs2+ is not essential for cell viability. A Deltasrs2 Deltarqh1 double mutant grows extremely slowly with aberrant shaped cells and low viability. This slow growth does not appear to be related to stalled replication, as Deltasrs2 Deltarqh1 cells showed higher survival rates, compared with Deltarqh1, when stalled forks were increased by UV irradiation or hydroxy urea treatment. Consistent with this result, we found that Deltasrs2 Deltarqh1 cells progress through S-phase with a slight delay, but undergo a checkpoint-dependent arrest presumably at G2/M. Further, we found that Deltasrs2 Deltarqh1 slow growth is related to recombination, as loss of either the rhp51+ or rhp57+ recombination genes improves cell growth in the double mutant. Deltasrs2 is also synthetic lethal with Deltarhp54, another homologous recombination gene. This lethality is suppressed in a Deltarhp51 background. Together, these results demonstrate a clear genetic interaction between rqh1+, srs2+ and the genes of the homologous recombination pathway.","authors":"Maftahi M, Hope JC, Delgado-Cruzata L, Han CS, Freyer GA","authors_abbrev":"Maftahi M et al.","pubmed_publication_date":"01 Nov 2002","pubmed_entrez_date":"2002-11-01","publication_year":"2002","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:59","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC15A10.03c","SPAC2G11.12","SPBC16G5.12c","SPAC4H3.05"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:17650318","title":"Combined analysis reveals a core set of cycling genes.","citation":"Genome Biol 2007;8(7):R146","abstract":"Global transcript levels throughout the cell cycle have been characterized using microarrays in several species. Early analysis of these experiments focused on individual species. More recently, a number of studies have concluded that a surprisingly small number of genes conserved in two or more species are periodically transcribed in these species. Combining and comparing data from multiple species is challenging because of noise in expression data, the different synchronization and scoring methods used, and the need to determine an accurate set of homologs.\nTo solve these problems, we developed and applied a new algorithm to analyze expression data from multiple species simultaneously. Unlike previous studies, we find that more than 20% of cycling genes in budding yeast have cycling homologs in fission yeast and 5% to 7% of cycling genes in each of four species have cycling homologs in all other species. These conserved cycling genes display much stronger cell cycle characteristics in several complementary high throughput datasets. Essentiality analysis for yeast and human genes confirms these findings. Motif analysis indicates conservation in the corresponding regulatory mechanisms. Gene Ontology analysis and analysis of the genes in the conserved sets sheds light on the evolution of specific subfunctions within the cell cycle.\nOur results indicate that the conservation in cyclic expression patterns is much greater than was previously thought. These genes are highly enriched for most cell cycle categories, and a large percentage of them are essential, supporting our claim that cross-species analysis can identify the core set of cycling genes.","authors":"Lu Y, Mahony S, Benos PV, Rosenfeld R, Simon I, Breeden LL, Bar-Joseph Z","authors_abbrev":"Lu Y et al.","pubmed_publication_date":"2007","pubmed_entrez_date":"2007-07-26","publication_year":"2007","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12705888","title":"Patterns of context-dependent codon biases.","citation":"Biochem Biophys Res Commun 2003 Apr 25;304(1):86-90","abstract":"The association of codon context and codon usage was studied in seven bacteria as well as Schizosaccharomyces pombe and Encephalitozoon cuniculi. The association is strongest in magnitude closest to the codons of interest but there is apparently no rule about which of the two contexts is generally strongest associated to codon usage. In all bacterial species and in the intron-rich Sch. pombe it was furthermore observed from plots of chi2 versus N that the wobble positions of codons in the proximity cause regular peaks both upstream and downstream. This observation is discussed in relation to a possible effect of mutational pressure on the association of codon usage and codon context. Absence of peaks corresponding to the wobble positions in the intron-poor En. cuniculi, and presence in Sch. pombe, may indicate that the role of introns in the context-dependent codon bias is negligible.","authors":"Fuglsang A","authors_abbrev":"Fuglsang A","pubmed_publication_date":"25 Apr 2003","pubmed_entrez_date":"2003-04-23","publication_year":"2003","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:11551952","title":"Fidelity and damage bypass ability of Schizosaccharomyces pombe Eso1 protein, comprised of DNA polymerase eta and sister chromatid cohesion protein Ctf7.","citation":"J Biol Chem 2001 Nov 16;276(46):42857-62","abstract":"DNA polymerase eta (Poleta) functions in error-free bypass of ultraviolet light-induced DNA lesions, and mutational inactivation of Poleta in humans causes the cancer prone syndrome, the variant form of xeroderma pigmentosum (XPV). Both Saccharomyces cerevisiae and human Poleta efficiently insert two adenines opposite the two thymines of a cyclobutane pyrimidine dimer. Interestingly, in the fission yeast Schizosaccharomyces pombe, the eso1(+) encoded protein is comprised of two domains, wherein the NH(2) terminus is highly homologous to Poleta, and the COOH terminus is highly homologous to the S. cerevisiae Ctf7 protein which is essential for the establishment of sister chromatid cohesion during S phase. Here we characterize the DNA polymerase activity of S. pombe GST-Eso1 fusion protein and a truncated version containing only the Poleta domain. Both proteins exhibit a similar DNA polymerase activity with a low processivity, and steady-state kinetic analyses show that on undamaged DNA, both proteins misincorporate nucleotides with frequencies of approximately 10(-2) to 10(-3). We also examine the two proteins for their ability to replicate a cyclobutane pyrimidine dimer-containing DNA template and find that both proteins replicate through the lesion equally well. Thus, fusion with Ctf7 has no significant effect on the DNA replication or damage bypass properties of Poleta. The possible role of Ctf7 fusion with Poleta in the replication of Cohesin-bound DNA sequences is discussed.","authors":"Madril AC, Johnson RE, Washington MT, Prakash L, Prakash S","authors_abbrev":"Madril AC et al.","pubmed_publication_date":"16 Nov 2001","pubmed_entrez_date":"2001-09-12","publication_year":"2001","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:51:42","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21410566","title":"Fission yeast Ubr1 ubiquitin ligase influences the oxidative stress response via degradation of active Pap1 bZIP transcription factor in the nucleus.","citation":"Mol Microbiol 2011 May;80(3):739-55","abstract":"Cells adapt to oxidative stress by transcriptional activation of genes encoding antioxidants and proteins of other protective roles. A bZIP transcription factor, Pap1, plays a critical role in this process and overexpression of Pap1 confers resistance to various oxidants and drugs in fission yeast. Pap1 temporarily enters the nucleus upon oxidative stress but returns to the cytoplasm once cells adapt to the stress, suggesting that cellular localization regulates Pap1 function. We report here an additional regulatory mechanism that Ubr1 ubiquitin ligase-dependent degradation lowered the Pap1 protein levels. ubr1 cells were causally resistant to hydrogen peroxide because of the increment of Pap1 levels. Pap1 was preferentially degraded in the nucleus where Ubr1 was consistently enriched. Proteolysis was critical to downregulate Pap1 especially when its activation persisted, as constitutively nuclear Pap1 severely inhibited growth in ubr1 mutants. Inactive mutations in the bZIP DNA binding domain stabilized Pap1 but rescued the lethality caused by constitutively active Pap1 in ubr1 mutants. These findings indicate that either nuclear export or Ubr1-mediated proteolysis must be operative to prevent uncontrolled Pap1 function. Coincidental dysfunction in both inhibitory pathways causes lethality because of prolonged activation of Pap1. Ubr1 is a critical regulator for the homeostasis of oxidative stress response.","doi":"10.1111/j.1365-2958.2011.07605.x","authors":"Kitamura K, Taki M, Tanaka N, Yamashita I","authors_abbrev":"Kitamura K et al.","pubmed_publication_date":"May 2011","pubmed_entrez_date":"2011-03-18","publication_year":"2011","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC365.13c","SPAC1783.07c","SPBC19C7.02"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:28806726","title":"Replication fork slowing and stalling are distinct, checkpoint-independent consequences of replicating damaged DNA.","citation":"PLoS Genet 2017 Aug;13(8):e1006958","abstract":"In response to DNA damage during S phase, cells slow DNA replication. This slowing is orchestrated by the intra-S checkpoint and involves inhibition of origin firing and reduction of replication fork speed. Slowing of replication allows for tolerance of DNA damage and suppresses genomic instability. Although the mechanisms of origin inhibition by the intra-S checkpoint are understood, major questions remain about how the checkpoint regulates replication forks: Does the checkpoint regulate the rate of fork progression? Does the checkpoint affect all forks, or only those encountering damage? Does the checkpoint facilitate the replication of polymerase-blocking lesions? To address these questions, we have analyzed the checkpoint in the fission yeast Schizosaccharomyces pombe using a single-molecule DNA combing assay, which allows us to unambiguously separate the contribution of origin and fork regulation towards replication slowing, and allows us to investigate the behavior of individual forks. Moreover, we have interrogated the role of forks interacting with individual sites of damage by using three damaging agents-MMS, 4NQO and bleomycin-that cause similar levels of replication slowing with very different frequency of DNA lesions. We find that the checkpoint slows replication by inhibiting origin firing, but not by decreasing fork rates. However, the checkpoint appears to facilitate replication of damaged templates, allowing forks to more quickly pass lesions. Finally, using a novel analytic approach, we rigorously identify fork stalling events in our combing data and show that they play a previously unappreciated role in shaping replication kinetics in response to DNA damage.","doi":"10.1371/journal.pgen.1006958","authors":"Iyer DR, Rhind N","authors_abbrev":"Iyer DR et al.","pubmed_publication_date":"Aug 2017","pubmed_entrez_date":"2017-08-15","publication_year":"2017","canto_session_key":"781f89391335e10b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Divya Iyer","canto_first_approved_date":"2017-10-17 15:47:49","canto_approved_date":"2025-09-03 13:29:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-02 19:02:10","canto_added_date":"2017-08-16 00:15:25","annotation_curators":[{"name":"Divya Iyer","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":13,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.13c","SPCC18B5.11c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-10-17"},{"uniquename":"PMID:10588653","title":"A mutant of Arp2p causes partial disassembly of the Arp2/3 complex and loss of cortical actin function in fission yeast.","citation":"Mol Biol Cell 1999 Dec;10(12):4201-15","abstract":"The Arp2/3 complex is an essential component of the yeast actin cytoskeleton that localizes to cortical actin patches. We have isolated and characterized a temperature-sensitive mutant of Schizosaccharomyces pombe arp2 that displays a defect in cortical actin patch distribution. The arp2(+) gene encodes an essential actin-related protein that colocalizes with actin at the cortical actin patch. Sucrose gradient analysis of the Arp2/3 complex in the arp2-1 mutant indicated that the Arp2p and Arc18p subunits are specifically lost from the complex at restrictive temperature. These results are consistent with immunolocalization studies of the mutant that show that Arp2-1p is diffusely localized in the cytoplasm at restrictive temperature. Interestingly, Arp3p remains localized to the cortical actin patch under the same restrictive conditions, leading to the hypothesis that loss of Arp2p from the actin patch affects patch motility but does not severely compromise its architecture. Analysis of the mutant Arp2 protein demonstrated defects in ATP and Arp3p binding, suggesting a possible model for disruption of the complex.","authors":"Morrell JL, Morphew M, Gould KL","authors_abbrev":"Morrell JL et al.","pubmed_publication_date":"Dec 1999","pubmed_entrez_date":"1999-12-10","publication_year":"1999","canto_session_key":"708918cfe8faf590","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-09-03 17:09:23","canto_approved_date":"2026-01-31 17:41:32","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-01 10:39:42","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":28,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC4A8.15c","SPBC14C8.06","SPAC6G9.07c","SPBC1778.08c","SPAC630.03","SPAC11H11.06"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2020-09-03"},{"uniquename":"PMID:26104357","title":"A Unique DNA Recombination Mechanism of the Mating/Cell-type Switching of Fission Yeasts: a Review.","citation":"Microbiol Spectr 2014 Oct;2(5)","abstract":"Cells of the highly diverged Schizosaccharomyces (S.) pombe and S. japonicus fission yeasts exist in one of two sex/mating types, called P (for plus) or M (for minus), specified by which allele, M or P, resides at mat1. The fission yeasts have evolved an elegant mechanism for switching P or M information at mat1 by a programmed DNA recombination event with a copy of one of the two silent mating-type genes residing nearby in the genome. The switching process is highly cell-cycle and generation dependent such that only one of four grandchildren of a cell switches mating type. Extensive studies of fission yeast established the natural DNA strand chirality at the mat1 locus as the primary basis of asymmetric cell division. The asymmetry results from a unique site- and strand-specific epigenetic \"imprint\" at mat1 installed in one of the two chromatids during DNA replication. The imprint is inherited by one daughter cell, maintained for one cell cycle, and is then used for initiating recombination during mat1 replication in the following cell cycle. This mechanism of cell-type switching is considered to be unique to these two organisms, but determining the operation of such a mechanism in other organisms has not been possible for technical reasons. This review summarizes recent exciting developments in the understanding of mating-type switching in fission yeasts and extends these observations to suggest how such a DNA strand-based epigenetic mechanism of cellular differentiation could also operate in diploid organisms.","doi":"10.1128/microbiolspec.MDNA3-0003-2014","authors":"Klar AJS, Ishikawa K, Moore S","authors_abbrev":"Klar AJS et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2015-06-25","publication_year":"2014","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-06-26 00:20:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:FY093953","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.95","SPNCRNA.84"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:8264625","title":"The Schizosaccharomyces pombe casein kinase II alpha and beta subunits: evolutionary conservation and positive role of the beta subunit.","citation":"Mol Cell Biol 1994 Jan;14(1):576-86","abstract":"Casein kinase II is a key regulatory enzyme involved in many cellular processes, including the control of growth and cell division. We report the molecular cloning and sequencing of cDNAs encoding the alpha and the beta subunits of casein kinase II of Schizosaccharomyces pombe. The deduced amino acid sequence of Cka1, the alpha catalytic subunit, shows high sequence similarity to alpha subunits identified in other species. The amino acid sequence of Ckb1, the S. pombe beta subunit, is 57% identical to that of the human beta subunit. Cka1 overexpression results in no detectable phenotype. In contrast, Ckb1 overexpression inhibits cell growth and cytokinesis, with formation of multiseptated cells. Disruption of the ckb1+ gene causes a cold-sensitive phenotype and abnormalities in cell shape. In these cells, the casein kinase II activity is reduced to undetectable levels, demonstrating that Ckb1 is required for enzyme activity in vivo. In agreement with this, the activity measured in a strain expressing high levels of Cka1 is enhanced only when the Ckb1 protein is coexpressed. Altogether, our data suggest that Ckb1 is a positive regulator of the enzyme activity, and that it plays a role in mediating the interaction of casein kinase II with downstream targets and/or with additional regulators.","authors":"Roussou I, Draetta G","authors_abbrev":"Roussou I et al.","pubmed_publication_date":"Jan 1994","pubmed_entrez_date":"1994-01-01","publication_year":"1994","canto_session_key":"dc5b0f7869ec439e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2017-02-12 19:32:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-03-04 17:02:41","canto_added_date":"2012-02-24 05:54:44","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":16,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.11","SPAC1851.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2016-03-04"},{"uniquename":"PMID:8657126","title":"Cig2, a B-type cyclin, promotes the onset of S in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1996 Apr;16(4):1527-33","abstract":"Cdc2, a catalytic subunit of cyclin-dependent kinases, is required for both the G1-to-S and G2-to-M transitions in the fission yeast Schizosaccharomyces pombe. Cdc13, a B-type cyclin, is required for the M-phase induction function of Cd2. Two additional B-type cyclins, Cig1 and Cig2, have been identified in S. pombe, but none of the B-type cyclins are individually required for the onset of S. We report that Cdc13 is important for DNA replication in a strain lacking Cig2. Unlike deltacdc13 cells, double-mutant deltacdc13 deltacig2 cells are defective in undergoing multiple rounds of DNA replication. The conclusion that Cig2 promotes S is further supported by the finding that Cig2 protein and Cig2-associated kinase activity appear soon after the completion of M and peak during S, as well as the observation that S is delayed in deltacig2 cells as they recover from a G1 arrest induced by nitrogen starvation. These studies indicate that Cig2 is the primary S-phase-promoting cyclin in S. pombe but that Cdc13 can effectively substitute for Cig2 in deltacig2 cells. These observations also suggest that the gradual increase in the activity of Cdc2-Cdc13 kinase can be sufficient for the correct temporal ordering of S and M phases in deltacig2 cells.","authors":"Mondesert O, McGowan CH, Russell P","authors_abbrev":"Mondesert O et al.","pubmed_publication_date":"Apr 1996","pubmed_entrez_date":"1996-04-01","publication_year":"1996","canto_session_key":"6d5e3bbf11d54761","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2017-04-02 18:27:52","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-11 22:57:19","canto_added_date":"2012-02-24 05:54:09","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPAC1F7.05","SPAPB2B4.03","SPBC336.12c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2014-06-11"},{"uniquename":"GO_REF:0000062","title":"Representation of processes occurring in parts of the cell in the Gene Ontology","abstract":"We have created a standard template for classes describing processes occurring in parts of the cell. The underlying equivalence axiom template is \"P and 'occurs in' some C\", where P is a biological process and C is a cellular component.","authors":"GO ontology editors","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25640442","title":"Measurement and manipulation of cell size parameters in fission yeast.","citation":"Methods Cell Biol 2015;125:423-36","abstract":"Cells usually grow to a certain size before they divide. The fission yeast Schizosaccharomyces pombe is an established model to dissect the molecular control of cell size homeostasis and cell cycle. In this chapter, we describe two simple methods to: (1) precisely compute geometrical parameters (cell length, diameter, surface, and volume) of single growing and dividing fission yeast cells with image analysis scripts and (2) manipulate cell diameter with microfabricated chambers and assess for cell size at division. We demonstrate the strength of these approaches in the context of growing spores, which constantly change size and shape and in deriving allometric relationships between cell geometrical parameters associated with G2/M transition. We emphasize these methods to be useful to investigate problems of growth, size, and division in fungal or bacterial cells.","doi":"10.1016/bs.mcb.2014.10.011","authors":"Zegman Y, Bonazzi D, Minc N","authors_abbrev":"Zegman Y et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-02-03","publication_year":"2015","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-02-04 01:15:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8437586","title":"Mutational analysis of the fission yeast p34cdc2 protein kinase gene.","citation":"Mol Gen Genet 1993 Jan;236(2-3):415-26","abstract":"The p34cdc2 protein serine-threonine kinase plays an essential role in the life cycle of fission yeast, being required for both the G1-S and G2-M transitions during mitotic growth, and also for the second meiotic nuclear division. Functional homologues of p34cdc2 (each ca. 60% identical to the fission yeast prototype) have been isolated from organisms as diverse as humans, insects and plants, and there is now considerable evidence supporting the view that fundamental aspects of the cell cycle controls uncovered in fission yeast will prove to be conserved in all eukaryotes. By comparing the amino acid sequences of fission yeast p34cdc2 with its higher eukaryotic counterparts it is possible to identify conserved residues that are likely to be centrally important for p34cdc2 function. Here the effects are described of mutating a number of these conserved residues. Twenty-three new mutant alleles have been constructed and tested. We show that replacing cysteine 67 with tryptophan renders the resulting mutant protein p80cdc25-independent (while neither leucine, isoleucine nor valine has this effect) and that several of the amino acids within the highly conserved PSTAIRE region are not absolutely required for p34cdc2 function. Five acidic amino acids have also been mutated within p34cdc2, which are invariant across the eukaryotic protein kinase family. Acid-to-base mutations at three of these residues resulted in a dominant-negative, cell cycle arrest phenotype while similar mutations at the other two simply abolished p34cdc2 protein function. The results are discussed with reference to the predicted tertiary structure of the p34cdc2 enzyme.","authors":"MacNeill SA, Nurse P","authors_abbrev":"MacNeill SA et al.","pubmed_publication_date":"Jan 1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_session_key":"b94d5bebcfaa526b","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Jacky Hayles","canto_first_approved_date":"2018-04-06 13:32:28","canto_approved_date":"2025-09-02 16:24:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-04-05 15:45:52","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[{"name":"Jacky Hayles","community_curator":true,"annotation_count":219,"orcid":"0000-0002-8599-8206","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC582.03","SPBC11B10.09","SPAC24H6.05","SPCC18B5.03"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2018-04-06"},{"uniquename":"PMID:38673778","title":"Dysfunction of Gpl1-Gih35-Wdr83 Complex in  S. pombe  Affects the Splicing of DNA Damage Repair Factors Resulting in Increased Sensitivity to DNA Damage.","citation":"Int J Mol Sci 2024 Apr 10;25(8)","abstract":"Pre-mRNA splicing plays a key role in the regulation of gene expression. Recent discoveries suggest that defects in pre-mRNA splicing, resulting from the dysfunction of certain splicing factors, can impact the expression of genes crucial for genome surveillance mechanisms, including those involved in cellular response to DNA damage. In this study, we analyzed how cells with a non-functional spliceosome-associated Gpl1-Gih35-Wdr83 complex respond to DNA damage. Additionally, we investigated the role of this complex in regulating the splicing of factors involved in DNA damage repair. Our findings reveal that the deletion of any component within the Gpl1-Gih35-Wdr83 complex leads to a significant accumulation of unspliced pre-mRNAs of DNA repair factors. Consequently, mutant cells lacking this complex exhibit increased sensitivity to DNA-damaging agents. These results highlight the importance of the Gpl1-Gih35-Wdr83 complex in regulating the expression of DNA repair factors, thereby protecting the stability of the genome following DNA damage.","doi":"10.3390/ijms25084192","authors":"Cipakova I, Jurcik M, Selicky T, Lalakova LO, Jakubikova J, Cipak L","authors_abbrev":"Cipakova I et al.","pubmed_publication_date":"10 Apr 2024","pubmed_entrez_date":"2024-04-27","publication_year":"2024","canto_session_key":"1b1c2d338aee1868","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2024-04-27 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC713.05","SPAC20H4.06c","SPAC20H4.09"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:10880469","title":"Genetic analyses of Schizosaccharomyces pombe dna2(+) reveal that dna2 plays an essential role in Okazaki fragment metabolism.","citation":"Genetics 2000 Jul;155(3):1055-67","abstract":"In this report, we investigated the phenotypes caused by temperature-sensitive (ts) mutant alleles of dna2(+) of Schizosaccharomyces pombe, a homologue of DNA2 of budding yeast, in an attempt to further define its function in vivo with respect to lagging-strand synthesis during the S-phase of the cell cycle. At the restrictive temperature, dna2 (ts) cells arrested at late S-phase but were unaffected in bulk DNA synthesis. Moreover, they exhibited aberrant mitosis when combined with checkpoint mutations, in keeping with a role for Dna2 in Okazaki fragment maturation. Similarly, spores in which dna2(+) was disrupted duplicated their DNA content during germination and also arrested at late S-phase. Inactivation of dna2(+) led to chromosome fragmentation strikingly similar to that seen when cdc17(+), the DNA ligase I gene, is inactivated. The temperature-dependent lethality of dna2 (ts) mutants was suppressed by overexpression of genes encoding subunits of polymerase delta (cdc1(+) and cdc27(+)), DNA ligase I (cdc17(+)), and Fen-1 (rad2(+)). Each of these gene products plays a role in the elongation or maturation of Okazaki fragments. Moreover, they all interacted with S. pombe Dna2 in a yeast two-hybrid assay, albeit to different extents. On the basis of these results, we conclude that dna2(+) plays a direct role in the Okazaki fragment elongation and maturation. We propose that dna2(+) acts as a central protein to form a complex with other proteins required to coordinate the multienzyme process for Okazaki fragment elongation and maturation.","authors":"Kang HY, Choi E, Bae SH, Lee KH, Gim BS, Kim HD, Park C, MacNeill SA, Seo YS","authors_abbrev":"Kang HY et al.","pubmed_publication_date":"Jul 2000","pubmed_entrez_date":"2000-07-06","publication_year":"2000","canto_session_key":"32e5984a7be84674","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2018-05-14 15:22:13","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2015-02-09 16:16:30","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC20G4.04c","SPAC3G6.06c","SPBC16D10.04c","SPAC27E2.05","SPAC8F11.07c","SPAC20G8.01","SPBC1734.02c"],"gene_count":7,"ltp_gene_count":7,"approved_date":"2015-02-09"},{"uniquename":"PMID:18503766","title":"Identification of the fnx1+ and fnx2+ genes for vacuolar amino acid transporters in Schizosaccharomyces pombe.","citation":"FEBS Lett 2008 Jun 25;582(15):2225-30","abstract":"We have identified the Schizosaccharomyces pombe SPBC3E7.06c gene (fnx2(+)) from a homology search with the fnx1(+) gene involving in G(0) arrest upon nitrogen starvation. Green fluorescent protein-fused Fnx1p and Fnx2p localized exclusively to the vacuolar membrane. Uptake of histidine or isoleucine by S. pombe cells was inhibited by concanamycin A, a specific inhibitor of the vacuolar H(+)-ATPase. Amino acid uptake was also defective in the vacuolar ATPase mutant, suggesting that vacuolar compartmentalization is critical for amino acid uptake by whole cells. In both Deltafnx1 and Deltafnx2 mutant cells, uptake of lysine, isoleucine or asparagine was impaired. These results suggest that fnx1(+) and fnx2(+) are involved in vacuolar amino acid uptake in S. pombe.","doi":"10.1016/j.febslet.2008.05.017","authors":"Chardwiriyapreecha S, Shimazu M, Morita T, Sekito T, Akiyama K, Takegawa K, Kakinuma Y","authors_abbrev":"Chardwiriyapreecha S et al.","pubmed_publication_date":"25 Jun 2008","pubmed_entrez_date":"2008-05-28","publication_year":"2008","canto_session_key":"7a232376d5ceda7a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2015-03-31 14:12:10","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-03-31 14:12:05","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":9,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC12C2.13c","YBR293W","SPBC3E7.06c","SPAC343.05","YMR088C"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2015-03-31"},{"uniquename":"PMID:7642144","title":"A K-252a-resistance gene, sks1+, encodes a protein similar to the Caenorhabditis elegans F37 A4.5 gene product and confers multidrug resistance in Schizosaccharomyces pombe.","citation":"Gene 1995 Aug 08;161(1):93-6","abstract":"A gene named sks1+ was cloned as a suppressor of the K-252a-sensitivity phenotype of Schizosaccharomyces pombe (Sp) from a gene library of the parental Sp chromosomal DNA constructed with a multicopy vector pDB248'. The gene encoded a 308-amino-acid (aa) protein similar to the Caenorhabditis elegans F37 A4.5 gene product and to the mouse and Drosophila Mov34 gene products. The sks1+ null mutants obtained by gene disruption were non-viable, indicating that sks1+ is essential for vegetative growth. The parental Sp strain carrying multiple copies of sks1+ showed distinct cross-resistance to staurosporine, thiabendazole and vanadate in addition to K-252a, although Sks1 has no similarity in aa sequence to those of ATP-binding cassette (ABC)-type transporters. The multicopy plasmid containing sks1+ conferred multidrug resistance (MDR), even in a mutant cell defective in pmd1+ encoding an ABC-type transporter. It is therefore unlikely that the function of pmd1+ is involved in MDR conferred by sks1+. These results suggest that sks1+ is a functionally novel MDR gene.","authors":"Usui T, Yoshida M, Honda A, Beppu T, Horinouchi S","authors_abbrev":"Usui T et al.","pubmed_publication_date":"08 Aug 1995","pubmed_entrez_date":"1995-08-08","publication_year":"1995","canto_session_key":"26d744db2d025a87","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-01-18 11:08:50","canto_approved_date":"2022-02-02 14:16:06","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-02-28 19:37:49","canto_added_date":"2012-02-24 05:54:11","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":7,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC31G5.13"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-18"},{"uniquename":"PMID:1550959","title":"Genetic and biochemical analysis of the adenylyl cyclase-associated protein, cap, in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 1992 Feb;3(2):167-80","abstract":"We have identified, cloned, and studied a gene, cap, encoding a protein that is associated with adenylyl cyclase in the fission yeast Schizosaccharomyces pombe. This protein shares significant sequence homology with the adenylyl cyclase-associated CAP protein in the yeast Saccharomyces cerevisiae. CAP is a bifunctional protein; the N-terminal domain appears to be involved in cellular responsiveness to RAS, whereas loss of the C-terminal portion is associated with morphological and nutritional defects. S. pombe cap can suppress phenotypes associated with deletion of the C-terminal CAP domain in S. cerevisiae but does not suppress phenotypes associated with deletion of the N-terminal domain. Analysis of cap disruptants also mapped the function of cap to two domains. The functional loss of the C-terminal region of S. pombe cap results in abnormal cellular morphology, slow growth, and failure to grow at 37 degrees C. Increases in mating and sporulation were observed when the entire gene was disrupted. Overproduction of both cap and adenylyl cyclase results in highly elongated large cells that are sterile and have measurably higher levels of adenylyl cyclase activity. Our results indicate that cap is required for the proper function of S. pombe adenylyl cyclase but that the C-terminal domain of cap has other functions that are shared with the C-terminal domain of S. cerevisiae CAP.","authors":"Kawamukai M, Gerst J, Field J, Riggs M, Rodgers L, Wigler M, Young D","authors_abbrev":"Kawamukai M et al.","pubmed_publication_date":"Feb 1992","pubmed_entrez_date":"1992-02-01","publication_year":"1992","canto_session_key":"3bce65ea848fff57","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-04-28 16:03:03","canto_approved_date":"2026-03-20 08:53:56","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2012-12-27 16:54:13","canto_added_date":"2012-02-24 05:55:05","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":1,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC306.09c","SPBC19C7.03"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2015-04-28"},{"uniquename":"PMID:9037770","title":"Abc1: a new ABC transporter from the fission yeast Schizosaccharomyces pombe.","citation":"FEMS Microbiol Lett 1997 Feb 01;147(1):97-102","abstract":"We have isolated the abc1 gene from the fission yeast Schizosaccharomyces pombe. Sequence analysis suggests that the Abc1 protein is a member of the ABC superfamily of transporters and is composed of two structurally homologous halves, each consisting of a hydrophobic region of six transmembrane domains and a hydrophilic region containing one ATP-binding site. The abc1 gene appears to be expressed under all growth conditions but gene disruption experiments indicate that it is not essential for growth. The sequence of the abc1 gene has been deposited in the EMBL data library under the Accession Number Y09354.","authors":"Christensen PU, Davis K, Nielsen O, Davey J","authors_abbrev":"Christensen PU et al.","pubmed_publication_date":"01 Feb 1997","pubmed_entrez_date":"1997-02-01","publication_year":"1997","canto_session_key":"b00a5065fbeb471","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2012-04-30 17:23:32","canto_session_submitted_date":"2012-04-27 16:04:08","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC9E9.12c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-04-27"},{"uniquename":"PMID:31026495","title":"A fission yeast platform for heterologous expression of mammalian adenylyl cyclases and high throughput screening.","citation":"Cell Signal 2019 Aug;60:114-121","abstract":"The fission yeast Schizosaccharomyces pombe uses a cAMP signaling pathway to link glucose-sensing to Protein Kinase A activity in order to regulate cell growth, sexual development, gluconeogenesis, and exit from stationary phase. We previously used a PKA-repressed fbp1-ura4 reporter to conduct high throughput screens (HTSs) for inhibitors of heterologously-expressed mammalian cyclic nucleotide phosphodiesterases (PDEs). Here, we describe the successful expression of all ten mammalian adenylyl cyclase (AC) genes, along with the human GNAS Gα s  gene. By measuring expression of an fbp1-GFP reporter together with direct measurements of intracellular cAMP levels, we can detect both basal AC activity from all ten AC genes as well as GNAS-stimulated activity from eight of the nine transmembrane ACs (tmACs; AC2-AC9). The ability to use this platform to conduct HTS for novel chemical probes that reduce PKA activity was demonstrated by a pilot screen of the LOPAC® 1280  library, leading to the identification of diphenyleneiodonium chloride (DPI) as an inhibitor of basal AC activity. This screening technology could open the door to the development of therapeutic compounds that target GNAS or the ACs, an area in which there is significant unmet need.","doi":"10.1016/j.cellsig.2019.04.010","authors":"Getz RA, Kwak G, Cornell S, Mbugua S, Eberhard J, Huang SX, Abbasi Z, de Medeiros AS, Thomas R, Bukowski B, Dranchak PK, Inglese J, Hoffman CS","authors_abbrev":"Getz RA et al.","pubmed_publication_date":"Aug 2019","pubmed_entrez_date":"2019-04-27","publication_year":"2019","canto_triage_status":"Biotech","canto_curator_role":"PomBase","canto_added_date":"2019-04-28 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7214237","title":"Hybridization studies within the genus Schizosaccharomyces Lindner.","citation":"Can J Microbiol 1981 Feb;27(2):184-91","abstract":"Hybridization studies based on the prototrophic selection technique, involving the use of auxotrophic mutants of strains of five accepted species of the genus Schizosaccharomyces, are reported. Intrastrain recombinants were recovered in five out of six tested parental pairs. Interstrain recombinants were recovered from crosses involving strains of S. japonicus and strains of S. pombe. No recombinants were recovered in 62 interspecific crosses involving all possible combinations of the six representatives of the genus.","authors":"Johannsen E","authors_abbrev":"Johannsen E","pubmed_publication_date":"Feb 1981","pubmed_entrez_date":"1981-02-01","publication_year":"1981","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:53","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16216079","title":"Catalytic mechanism of fungal homoserine transacetylase.","citation":"Biochemistry 2005 Oct 18;44(41):13560-6","abstract":"Homoserine transacetylase is a required catalyst in the biochemical pathway that metabolizes Asp to Met in fungi. The enzyme from the yeast Schizosaccharomyces pombe activates the hydroxyl group of L-homoserine by acetylation from acetyl coenzyme A. This enzyme is unique to fungi and some bacteria and presents an important new target for drug discovery. Steady-state kinetic parameters provide evidence that this enzyme follows a ping-pong mechanism. Proton inventory was consistent with a single-proton transfer, and pH studies suggested the participation of at least one residue with a pKa value of 6.4-6.6, possibly a His or Asp/Glu in catalysis. Protein sequence alignments indicate that this enzyme belongs to the alpha/beta-hydrolase fold superfamily of enzymes, indicating the involvement of an active-site nucleophile and possibly a canonical catalytic triad. We constructed site-specific mutants and identified Ser163, Asp403, and His432 as the likely active-site residues of a catalytic triad based on steady-state kinetics and genetic complementation of a yeast null mutant. Moreover, unlike the wild-type enzyme, inactive site mutants were not capable of producing an acetyl-enzyme intermediate. Homoserine transacetylase therefore catalyzes the acetylation of L-homoserine via a covalent acyl-enzyme intermediate through an active-site Ser. These results form the basis of future exploitation of this enzyme as an antimicrobial target.","authors":"Nazi I, Wright GD","authors_abbrev":"Nazi I et al.","pubmed_publication_date":"18 Oct 2005","pubmed_entrez_date":"2005-10-12","publication_year":"2005","canto_session_key":"9349842f00f1494f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-10-31 11:40:45","canto_approved_date":"2019-11-05 08:30:39","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-30 19:16:37","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":5,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC56F2.11"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-10-31"},{"uniquename":"PMID:30997531","title":"Transcriptional silencing of centromere repeats by heterochromatin safeguards chromosome integrity.","citation":"Curr Genet 2019 Oct;65(5):1089-1098","abstract":"The centromere region of chromosomes consists of repetitive DNA sequences, and is, therefore, one of the fragile sites of chromosomes in many eukaryotes. In the core region, the histone H3 variant CENP-A forms centromere-specific nucleosomes that are required for kinetochore formation. In the pericentromeric region, histone H3 is methylated at lysine 9 (H3K9) and heterochromatin is formed. The transcription of pericentromeric repeats by RNA polymerase II is strictly repressed by heterochromatin. However, the role of the transcriptional silencing of the pericentromeric repeats remains largely unclear. Here, we focus on the chromosomal rearrangements that occur at the repetitive centromeres, and highlight our recent studies showing that transcriptional silencing by heterochromatin suppresses gross chromosomal rearrangements (GCRs) at centromeres in fission yeast. Inactivation of the Clr4 methyltransferase, which is essential for the H3K9 methylation, increased GCRs with breakpoints located in centromeric repeats. However, mutations in RNA polymerase II or the transcription factor Tfs1/TFIIS, which promotes restart of RNA polymerase II following its backtracking, reduced the GCRs that occur in the absence of Clr4, demonstrating that heterochromatin suppresses GCRs by repressing the Tfs1-dependent transcription. We also discuss how the transcriptional restart gives rise to chromosomal rearrangements at centromeres.","doi":"10.1007/s00294-019-00975-x","authors":"Nakagawa T, Okita AK","authors_abbrev":"Nakagawa T et al.","pubmed_publication_date":"Oct 2019","pubmed_entrez_date":"2019-04-19","publication_year":"2019","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2019-04-20 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27815906","title":"Synchronization of Yeast.","citation":"Methods Mol Biol 2017;1524:215-242","abstract":"The budding yeast Saccharomyces cerevisiae and fission yeast Schizosaccharomyces pombe are amongst the simplest and most powerful model systems for studying the genetics of cell cycle control. Because yeast grows very rapidly in a simple and economical media, large numbers of cells can easily be obtained for genetic, molecular, and biochemical studies of the cell cycle. The use of synchronized cultures greatly aids in the ease and interpretation of cell cycle studies. In principle, there are two general methods for obtaining synchronized yeast populations. Block-and-release methods can be used to induce cell cycle synchrony. Alternatively, centrifugal elutriation can be used to select synchronous populations. Because each method has innate advantages and disadvantages, the use of multiple approaches helps in generalizing results. An overview of the most commonly used methods to generate synchronized yeast cultures is presented along with working Notes: a section that includes practical comments, experimental considerations and observations, and hints regarding the pros and cons innate to each approach.","authors":"Smith J, Manukyan A, Hua H, Dungrawala H, Schneider BL","authors_abbrev":"Smith J et al.","pubmed_publication_date":"2017","pubmed_entrez_date":"2016-11-06","publication_year":"2017","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2016-11-08 01:15:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21089469","title":"[Regulation of initiation of DNA replication in through G1 to S phases: overview].","citation":"Tanpakushitsu Kakusan Koso 2009 Mar;54(4 Suppl):317-9","abstract":"","authors":"Masukata H","authors_abbrev":"Masukata H","pubmed_publication_date":"Mar 2009","pubmed_entrez_date":"2010-11-25","publication_year":"2009","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8524332","title":"Stockpiling of Cdc25 during a DNA replication checkpoint arrest in Schizosaccharomyces pombe.","citation":"Mol Cell Biol 1996 Jan;16(1):86-93","abstract":"The DNA replication checkpoint couples the onset of mitosis with the completion of S phase. It is clear that in the fission yeast Schizosaccharomyces pombe, operation of this checkpoint requires maintenance of the inhibitory tyrosyl phosphorylation of Cdc2. Cdc25 phosphatase induces mitosis by dephosphorylating tyrosine 15 of Cdc2. In this report, Cdc25 is shown to accumulate to a very high level in cells arrested in S. This shows that mechanisms which modulate the abundance of Cdc25 are unconnected to the DNA replication checkpoint. Using a Cdc2/cyclin B activation assay, we found that Cdc25 activity increased approximately 10-fold during transit through M phase. Cdc25 was activated by phosphorylations that were dependent on Cdc2 activity in vivo. Cdc25 activation was suppressed in cells arrested in G1 and S. However, Cdc25 was more highly modified and appeared to be somewhat more active in S than in G1. This finding might be connected to the fact that progression from G1 to S increases the likelihood that constitutive Cdc25 overproduction will cause inappropriate mitosis.","authors":"Kovelman R, Russell P","authors_abbrev":"Kovelman R et al.","pubmed_publication_date":"Jan 1996","pubmed_entrez_date":"1996-01-01","publication_year":"1996","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:19359250","title":"A methyltransferase-independent function for Rmt3 in ribosomal subunit homeostasis.","citation":"J Biol Chem 2009 May 29;284(22):15026-37","abstract":"Schizosaccharomyces pombe Rmt3 is a member of the protein-arginine methyltransferase (PRMT) family and is the homolog of human PRMT3. We previously characterized Rmt3 as a ribosomal protein methyltransferase based on the identification of the 40 S Rps2 (ribosomal protein S2) as a substrate of Rmt3. RMT3-null cells produce nonmethylated Rps2 and show mis-regulation of the 40 S/60 S ribosomal subunit ratio due to a small subunit deficit. For this study, we have generated a series of RMT3 alleles that express various amino acid substitutions to characterize the functional domains of Rmt3 in Rps2 binding, Rps2 arginine methylation, and small ribosomal subunit production. Notably, catalytically inactive versions of Rmt3 restored the ribosomal subunit imbalance detected in RMT3-null cells. Consistent with a methyltransferase-independent function for Rmt3 in small ribosomal subunit production, the expression of an Rps2 variant in which the identified methylarginine residues were substituted with lysines showed normal levels of 40 S subunit. Importantly, substitutions within the zinc finger domain of Rmt3 that abolished Rps2 binding did not rescue the 40 S ribosomal subunit deficit of RMT3-null cells. Our findings suggest that the Rmt3-Rps2 interaction, rather than Rps2 methylation, is important for the function of Rmt3 in the regulation of small ribosomal subunit production.","doi":"10.1074/jbc.M109.004812","authors":"Perreault A, Gascon S, D'Amours A, Aletta JM, Bachand F","authors_abbrev":"Perreault A et al.","pubmed_publication_date":"29 May 2009","pubmed_entrez_date":"2009-04-11","publication_year":"2009","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AB054307","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32810455","title":"Cell Biology: An Open Solution for Closed Mitosis.","citation":"Curr Biol 2020 Aug 17;30(16):R942-R944","abstract":"At the end of mitosis, cells must remodel their nuclear envelope to produce two identical daughter nuclei. Two new studies using Schizosaccharomyces pombe provide insight into how compartmentalized nuclear pore complex disassembly allows cells that undergo closed mitosis to achieve nuclear division.","doi":"10.1016/j.cub.2020.06.067","authors":"Mori R, Oliferenko S","authors_abbrev":"Mori R et al.","pubmed_publication_date":"17 Aug 2020","pubmed_entrez_date":"2020-08-19","publication_year":"2020","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2020-08-20 00:15:06","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17936710","title":"Ctp1 is a cell-cycle-regulated protein that functions with Mre11 complex to control double-strand break repair by homologous recombination.","citation":"Mol Cell 2007 Oct 12;28(1):134-46","abstract":"The Mre11-Rad50-Nbs1 (MRN) complex is a primary sensor of DNA double-strand breaks (DSBs). Upon recruitment to DSBs, it plays a critical role in catalyzing 5' --> 3' single-strand resection that is required for repair by homologous recombination (HR). Unknown mechanisms repress HR in G1 phase of the cell cycle during which nonhomologous end-joining (NHEJ) is the favored mode of DSB repair. Here we describe fission yeast Ctp1, so-named because it shares conserved domains with the mammalian tumor suppressor CtIP. Ctp1 is recruited to DSBs where it is essential for repair by HR. Ctp1 is required for efficient formation of RPA-coated single-strand DNA adjacent to DSBs, indicating that it functions with the MRN complex in 5' --> 3' resection. Transcription of ctp1(+) is periodic during the cell cycle, with the onset of its expression coinciding with the start of DNA replication. These data suggest that regulation of Ctp1 underlies cell-cycle control of HR.","authors":"Limbo O, Chahwan C, Yamada Y, de Bruin RA, Wittenberg C, Russell P","authors_abbrev":"Limbo O et al.","pubmed_publication_date":"12 Oct 2007","pubmed_entrez_date":"2007-10-16","publication_year":"2007","canto_session_key":"938360b9812110c8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-03-03 13:55:06","canto_approved_date":"2025-09-04 09:32:20","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-29 11:24:09","canto_added_date":"2012-02-24 05:48:51","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":77,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.13c","SPAC644.14c","SPCC126.02c","SPBC29A10.05","SPAC13C5.07","SPBC6B1.09c","SPBC216.05","HGNC:9891","SPBC543.03c","SPBC336.12c","SPAC22F3.09c","SPCC338.08","SPBC16A3.07c","SPAC1556.01c","SPAC1F7.05","SPAC17A5.11","SPCC1259.13","SPBC342.05","SPBC725.16"],"gene_count":18,"ltp_gene_count":14,"approved_date":"2017-03-03"},{"uniquename":"PMID:6961452","title":"Cloned ural locus of Schizosaccharomyces pombe propagates autonomously in this yeast assuming a polymeric form.","citation":"Proc Natl Acad Sci U S A 1982 Dec;79(24):7819-23","abstract":"DNA segments cloned from Schizosaccharomyces pombe by the ability to complement Escherichia coli pyrB mutations are shown to complement a ural mutation in S. pombe, thereby demonstrating that ural is the structural gene for aspartate transcarbamylase of S. pombe. Further, such segments combined with parts or all of pBR322 are shown to be capable of autonomous propagation in S. pombe. This suggests the existence of an autonomously replicating sequence (ars) in the vicinity of ural. Unlike the TRP1 segment cloned from Saccharomyces cerevisiae [Struhl, K., Stinchcomb, D. T., Scherer, S. & Davis, R. W. (1979) Proc. Natl. Acad. Sci. USA 76, 1035-1039], plasmids carrying the ural locus do not multiply as monomers but assume a polymeric form as large as a decamer to an icosamer in the yeast. Monomers are tandemly arranged in the polymer. Inversion of an inserted fragment or insertion of another segment into a competent plasmid greatly decreases the efficiency of such transformation, implying a role of the tertiary structure of the plasmids in the establishment of transformation of this kind.","authors":"Sakaguchi J, Yamamoto M","authors_abbrev":"Sakaguchi J et al.","pubmed_publication_date":"Dec 1982","pubmed_entrez_date":"1982-12-01","publication_year":"1982","canto_session_key":"ee707aabec0f40b7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_approved_date":"2014-04-08 13:53:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-04-04 14:18:06","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC22G7.06c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-04-04"},{"uniquename":"PMID:25488580","title":"Epigenetics: Histones pass the message on.","citation":"Nat Rev Genet 2015 Jan;16(1):3","abstract":"","doi":"10.1038/nrg3876","authors":"Jones B","authors_abbrev":"Jones B","pubmed_publication_date":"Jan 2015","pubmed_entrez_date":"2014-12-10","publication_year":"2015","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2015-04-12 00:19:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18808426","title":"Comparison of a coq7 deletion mutant with other respiration-defective mutants in fission yeast.","citation":"FEBS J 2008 Nov;275(21):5309-24","abstract":"Among the steps in ubiquinone biosynthesis, that catalyzed by the product of the clk-1/coq7 gene has received considerable attention because of its relevance to life span in Caenorhabditis elegans. We analyzed the coq7 ortholog (denoted coq7) in Schizosaccharomyces pombe, to determine whether coq7 has specific roles that differ from those of other coq genes. We first confirmed that coq7 is necessary for the penultimate step in ubiquinone biosynthesis, from the observation that the deletion mutant accumulated the ubiquinone precursor demethoxyubiquinone-10 instead of ubiquinone-10. The coq7 mutant displayed phenotypes characteristic of other ubiquinone-deficient Sc. pombe mutants, namely, hypersensitivity to hydrogen peroxide, a requirement for antioxidants for growth on minimal medium, and an elevated production of sulfide. To compare these phenotypes with those of other respiration-deficient mutants, we constructed cytochrome c (cyc1) and coq3 deletion mutants. We also assessed accumulation of oxidative stress in various ubiquinone-deficient strains and in the cyc1 mutant by measuring mRNA levels of stress-inducible genes and the phosphorylation level of the Spc1 MAP kinase. Induction of ctt1, encoding catalase, and apt1, encoding a 25 kDa protein, but not that of gpx1, encoding glutathione peroxidase, was indistinguishable in four ubiquinone-deficient mutants, indicating that the oxidative stress response operates at similar levels in the tested strains. One new phenotype was observed, namely, loss of viability in stationary phase (chronological life span) in both the ubiquinone-deficient mutant and in the cyc1 mutant. Finally, Coq7 was found to localize in mitochondria, consistent with the possibility that ubiquinone biosynthesis occurs in mitochondria in yeasts. In summary, our results indicate that coq7 is required for ubiquinone biosynthesis and the coq7 mutant is not distinguishable from other ubiquinone-deficient mutants, except that its phenotypes are more pronounced than those of the cyc1 mutant.","doi":"10.1111/j.1742-4658.2008.06661.x","authors":"Miki R, Saiki R, Ozoe Y, Kawamukai M","authors_abbrev":"Miki R et al.","pubmed_publication_date":"Nov 2008","pubmed_entrez_date":"2008-09-24","publication_year":"2008","canto_session_key":"b00ed4a71aeee523","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-11-19 10:04:36","canto_approved_date":"2025-01-21 12:25:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-09-18 11:12:50","canto_added_date":"2012-02-24 05:48:13","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":36,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC162.05","SPCC191.07","SPBPJ4664.01","SPBC2D10.18","SPBC32F12.03c","SPAC19G12.12","SPAC8C9.03","SPBC2G5.06c","SPAC10F6.01c","SPAC24B11.06c","SPBC337.15c"],"gene_count":11,"ltp_gene_count":10,"approved_date":"2014-11-19"},{"uniquename":"PMID:10407663","title":"S. pombe expression vector with 6x(His) tag for protein purification and potential for ligation-independent cloning.","citation":"Biotechniques 1999 Jul;27(1):58-60","abstract":"","authors":"Hosfield T, Lu Q","authors_abbrev":"Hosfield T et al.","pubmed_publication_date":"Jul 1999","pubmed_entrez_date":"1999-07-17","publication_year":"1999","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:40833569","title":"Visualizing Phosphatidic Acid and Diacylglycerol at the Nuclear Envelope in Fission Yeast.","citation":"Methods Mol Biol 2025;2958:99-118","abstract":"Although the outer membrane of the nuclear envelope is continuous with the endoplasmic reticulum, temporally regulated and functionally significant differences in membrane lipid composition may exist between the two nuclear membranes and between the outer nuclear membrane and the endoplasmic reticulum. Biochemical approaches to probing lipid composition are challenged when lipid dynamics must be analyzed with fine spatiotemporal resolution, for instance, within the cell cycle of a single cell. Here we describe a method to probe the distribution of phosphatidic acid and diacylglycerol, two interconvertible biosynthetic precursors for other membrane glycerophospholipids, in living cells of the model fission yeast Schizosaccharomyces pombe. We show how genetically encoded fluorescent biosensors can be constructed and optimized and present a protocol to probe and quantify phosphatidic acid and diacylglycerol levels specifically at the inner nuclear membrane.","doi":"10.1007/978-1-0716-4714-1_7","authors":"Foo S, Oliferenko S","authors_abbrev":"Foo S et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2025-08-20","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2025-08-20 23:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15197727","title":"A simple and efficient procedure for transformation of Schizosaccharomyces pombe.","citation":"Yeast 2004 Jun;21(8):613-7","abstract":"We describe a simple and efficient procedure for transformation of Schizosaccharomyces pombe. Sz. pombe colonies grown on minimal (SD) plates were directly removed and suspended in a 100 microl reaction mixture containing 70 microl PLATE solution (50% polyethylene glycol-4000, 100 mM lithium acetate, 10 mM Tris-HCl, pH 4.9, and 1 mM EDTA), 10 microl plasmid DNA (1 microg), 10 microl carrier DNA (100 microg) and 10 microl sterile distilled water. After incubation at 30 degrees C for 1 h followed by heat shock treatment at 42 degrees C for 15 min, the reaction mixture was spread on a selection plate. The transformation efficiency obtained using the procedure was approximately 8000 transformants/microg DNA. The method is simple and time-saving, making it especially useful for a large number of samples and when a high transformation efficiency is not required.","authors":"Morita T, Takegawa K","authors_abbrev":"Morita T et al.","pubmed_publication_date":"Jun 2004","pubmed_entrez_date":"2004-06-16","publication_year":"2004","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16532354","title":"S. pombe linear elements: the modest cousins of synaptonemal complexes.","citation":"Chromosoma 2006 Jun;115(3):260-71","abstract":"Synaptonemal complexes (SCs) are not formed during meiotic prophase in the fission yeast, Schizosaccharomyces pombe. Instead, so-called linear elements (LinEs) are formed at the corresponding stages. LinEs are remarkable in that their number does not correspond to the number of chromosomes or bivalents and that the changes in their organisation during prophase do not evidently reflect the pairing of chromosomes. Yet, LinEs are necessary for full meiotic pairing levels and for meiotic recombination. In this review, the composition of LinEs, their evolutionary relationship to SCs and their possible functions are discussed.","authors":"Loidl J","authors_abbrev":"Loidl J","pubmed_publication_date":"Jun 2006","pubmed_entrez_date":"2006-03-15","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25157825","title":"TMEM14C is required for erythroid mitochondrial heme metabolism.","citation":"J Clin Invest 2014 Oct;124(10):4294-304","abstract":"The transport and intracellular trafficking of heme biosynthesis intermediates are crucial for hemoglobin production, which is a critical process in developing red cells. Here, we profiled gene expression in terminally differentiating murine fetal liver-derived erythroid cells to identify regulators of heme metabolism. We determined that TMEM14C, an inner mitochondrial membrane protein that is enriched in vertebrate hematopoietic tissues, is essential for erythropoiesis and heme synthesis in vivo and in cultured erythroid cells. In mice, TMEM14C deficiency resulted in porphyrin accumulation in the fetal liver, erythroid maturation arrest, and embryonic lethality due to profound anemia. Protoporphyrin IX synthesis in TMEM14C-deficient erythroid cells was blocked, leading to an accumulation of porphyrin precursors. The heme synthesis defect in TMEM14C-deficient cells was ameliorated with a protoporphyrin IX analog, indicating that TMEM14C primarily functions in the terminal steps of the heme synthesis pathway. Together, our data demonstrate that TMEM14C facilitates the import of protoporphyrinogen IX into the mitochondrial matrix for heme synthesis and subsequent hemoglobin production. Furthermore, the identification of TMEM14C as a protoporphyrinogen IX importer provides a genetic tool for further exploring erythropoiesis and congenital anemias.","doi":"10.1172/JCI76979","authors":"Yien YY, Robledo RF, Schultz IJ, Takahashi-Makise N, Gwynn B, Bauer DE, Dass A, Yi G, Li L, Hildick-Smith GJ, Cooney JD, Pierce EL, Mohler K, Dailey TA, Miyata N, Kingsley PD, Garone C, Hattangadi SM, Huang H, Chen W, Keenan EM, Shah DI, Schlaeger TM, DiMauro S, Orkin SH, Cantor AB, Palis J, Koehler CM, Lodish HF, Kaplan J, Ward DM, Dailey HA, Phillips JD, Peters LL, Paw BH","authors_abbrev":"Yien YY et al.","pubmed_publication_date":"Oct 2014","pubmed_entrez_date":"2014-08-27","publication_year":"2014","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAP14E8.05c","SPBC17A3.02"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:12748193","title":"The role of the SAP motif in promoting Holliday junction binding and resolution by SpCCE1.","citation":"J Biol Chem 2003 Aug 01;278(31):29121-9","abstract":"Holliday junctions are four-way branched DNA structures that are formed during recombination and by replication fork regression. Their processing depends on helicases that catalyze junction branch migration, and endonucleases that resolve the junction into nicked linear DNAs. Here we have investigated the role of a DNA binding motif called SAP in binding and resolving Holliday junctions by the fission yeast mitochondrial resolvase SpCCE1. Mutation or partial/complete deletion of the SAP motif dramatically impairs the ability of SpCCE1 to resolve Holliday junctions in a heterologous in vivo system. These mutant proteins retain the ability to recognize the junction structure and to distort it upon binding. However, once formed the mutant protein-junction complexes are relatively unstable and dissociate much faster than wild-type complexes. We show that binding stability is necessary for efficient junction resolution, and that this may be due in part to a requirement for maintaining the junction in an open conformation so that it can branch migrate to cleavable sites.","authors":"Ahn JS, Whitby MC","authors_abbrev":"Ahn JS et al.","pubmed_publication_date":"01 Aug 2003","pubmed_entrez_date":"2003-05-16","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10409726","title":"Myb-related fission yeast cdc5p is a component of a 40S snRNP-containing complex and is essential for pre-mRNA splicing.","citation":"Mol Cell Biol 1999 Aug;19(8):5352-62","abstract":"Myb-related cdc5p is required for G(2)/M progression in the yeast Schizosaccharomyces pombe. We report here that all detectable cdc5p is stably associated with a multiprotein 40S complex. Immunoaffinity purification has allowed the identification of 10 cwf (complexed with cdc5p) proteins. Two (cwf6p and cwf10p) are members of the U5 snRNP; one (cwf9p) is a core snRNP protein. cwf8p is the apparent ortholog of the Saccharomyces cerevisiae splicing factor Prp19p. cwf1(+) is allelic to the prp5(+) gene defined by the S. pombe splicing mutant, prp5-1, and there is a strong negative genetic interaction between cdc5-120 and prp5-1. Five cwfs have not been recognized previously as important for either pre-mRNA splicing or cell cycle control. Further characterization of cwf1p, cwf2p, cwf3p, and cwf4p demonstrates that they are encoded by essential genes, cosediment with cdc5p at 40S, and coimmunoprecipitate with cdc5p. We further show that cdc5p associates with the U2, U5, and U6 snRNAs and that cells lacking cdc5(+) function are defective in pre-mRNA splicing. These data raise the possibility that the cdc5p complex is an intermediate in the assembly or disassembly of an active S. pombe spliceosome.","authors":"McDonald WH, Ohi R, Smelkova N, Frendewey D, Gould KL","authors_abbrev":"McDonald WH et al.","pubmed_publication_date":"Aug 1999","pubmed_entrez_date":"1999-07-20","publication_year":"1999","canto_session_key":"9b52c917ba84da9d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-07-23 13:41:59","canto_approved_date":"2019-06-11 11:32:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-21 14:12:47","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC2G11.14","SPCC550.02c","SPBP22H7.07","SPAC2C4.03c","SPAC3A12.11c","SPAC29A4.08c","SPAC644.12","SPSNRNA.02","SPBC28F2.04c","SPBC211.02c","SPBC31F10.11c","SPBC215.12","SPAC4F8.12c","SPSNRNA.05","SPSNRNA.06"],"gene_count":15,"ltp_gene_count":14,"approved_date":"2015-07-23"},{"uniquename":"PMID:25472718","title":"Alp7/TACC recruits kinesin-8-PP1 to the Ndc80 kinetochore protein for timely mitotic progression and chromosome movement.","citation":"J Cell Sci 2015 Jan 15;128(2):354-63","abstract":"Upon establishment of proper kinetochore-microtubule attachment, the spindle assembly checkpoint (SAC) must be silenced to allow onset of anaphase, which is when sister chromatids segregate equally to two daughter cells. However, how proper kinetochore-microtubule attachment leads to timely anaphase onset remains elusive. Furthermore, the molecular mechanisms of chromosome movement during anaphase A remain unclear. In this study, we show that the fission yeast Alp7/TACC protein recruits a protein complex consisting of the kinesin-8 (Klp5-Klp6) and protein phosphatase 1 (PP1) to the kinetochore upon kinetochore-microtubule attachment. Accumulation of this complex at the kinetochore, on the one hand, facilitates SAC inactivation through PP1, and, on the other hand, accelerates polewards chromosome movement driven by the Klp5-Klp6 motor. We identified an alp7 mutant that had specific defects in binding to the Klp5-Klp6-PP1 complex but with normal localisation to the microtubule and kinetochore. Consistent with our proposition, this mutant shows delayed anaphase onset and decelerated chromosome movement during anaphase A. We propose that the recruitment of kinesin-8-PP1 to the kinetochore through Alp7/TACC interaction plays a crucial role in regulation of timely mitotic progression and chromosome movement during anaphase A.","doi":"10.1242/jcs.160036","authors":"Tang NH, Toda T","authors_abbrev":"Tang NH et al.","pubmed_publication_date":"15 Jan 2015","pubmed_entrez_date":"2014-12-05","publication_year":"2015","canto_session_key":"3117b5347cb47cf6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Takashi Toda","canto_first_approved_date":"2017-10-28 18:42:29","canto_approved_date":"2024-03-24 07:33:44","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-24 14:04:15","canto_added_date":"2014-12-06 01:15:26","annotation_curators":[{"name":"Takashi Toda","community_curator":true,"annotation_count":22,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":34,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1685.15c","SPCC31H12.05c","SPBC2F12.13","SPBC11C11.03","SPAC890.02c","SPBC776.02c","SPCC895.07","SPBC20F10.06","SPAC23H3.08c"],"gene_count":9,"ltp_gene_count":9,"approved_date":"2017-10-28"},{"uniquename":"PMID:25669599","title":"Fitness profiling links topoisomerase II regulation of centromeric integrity to doxorubicin resistance in fission yeast.","citation":"Sci Rep 2015 Feb 11;5:8400","abstract":"Doxorubicin, a chemotherapeutic agent, inhibits the religation step of topoisomerase II (Top2). However, the downstream ramifications of this action are unknown. Here we performed epistasis analyses of top2 with 63 genes representing doxorubicin resistance (DXR) genes in fission yeast and revealed a subset that synergistically collaborate with Top2 to confer DXR. Our findings show that the chromatin-regulating RSC and SAGA complexes act with Top2 in a cluster that is functionally distinct from the Ino80 complex. In various DXR mutants, doxorubicin hypersensitivity was unexpectedly suppressed by a concomitant top2 mutation. Several DXR proteins showed centromeric localization, and their disruption resulted in centromeric defects and chromosome missegregation. An additional top2 mutation could restore centromeric chromatin integrity, suggesting a counterbalance between Top2 and these DXR factors in conferring doxorubicin resistance. Overall, this molecular basis for mitotic catastrophe associated with doxorubicin treatment will help to facilitate drug combinatorial usage in doxorubicin-related chemotherapeutic regimens.","doi":"10.1038/srep08400","authors":"Nguyen TT, Lim JS, Tang RM, Zhang L, Chen ES","authors_abbrev":"Nguyen TT et al.","pubmed_publication_date":"11 Feb 2015","pubmed_entrez_date":"2015-02-12","publication_year":"2015","canto_session_key":"6570560d54460529","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-01-27 09:40:31","canto_approved_date":"2026-03-11 11:47:09","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2016-01-27 09:39:13","canto_added_date":"2015-02-13 01:15:26","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":127,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1672.04c","SPAC29B12.08","SPAC6G9.14","SPAPB17E12.04c","SPBC4B4.03","SPAC23H3.06","SPBC651.07","SPAC31G5.19","SPBC215.03c","SPBC16H5.13","SPCC23B6.05c","SPBC32F12.08c","SPCC1223.15c","SPBC18H10.04c","SPAC4F10.04","SPBPJ4664.01","SPCC1840.09","SPBC16A3.07c","SPBC1A4.03c","SPAC14C4.16","SPAPB1A10.09","SPCC24B10.08c","SPAC56F8.04c","SPCC757.10","SPCC16C4.20c","SPAC144.02","SPAC1687.12c","SPBC18H10.02","SPCC18.02","SPAPB1E7.02c","SPAC10F6.08c","SPAC1805.07c","SPAC11E3.12","SPBC146.12","SPBC32H8.07","SPBC1105.17","SPBC2D10.13","SPAC2F7.07c","SPBC4F6.10","SPCC663.03","SPAC2C4.05","SPBC1105.10","SPBC17D1.02","SPAC23D3.09","SPAC1952.05","SPAC15A10.03c","SPBC106.04","SPCC417.02","SPBC947.14c","SPAC823.10c","SPAC3C7.03c","SPCC777.13","SPBC28F2.10c","SPBC1604.02c","SPCC1259.03","SPCC31H12.08c","SPBC2D10.16","SPBC19G7.10c","SPBC1734.15","SPBC337.15c","SPAC17G8.07","SPCC1739.14","SPAC630.14c","SPBC21B10.13c","SPAC2F3.11","SPBC106.05c"],"gene_count":66,"ltp_gene_count":63,"approved_date":"2016-01-27"},{"uniquename":"PMID:180235","title":"Fractionation by differential and zonal centrifugation of spheroplasts prepared from a glucose-repressed fission yeast Schizosaccharomyces pombe 972h-.","citation":"J Gen Microbiol 1976 Apr;93(2):241-50","abstract":"A method is described for the preparation of spheroplasts in high yield from Schizosaccharomyces pombe, by treating cells grown in the presence of glucose and deoxyglucose with snail digestive enzymes. Gentle disruption of such spheroplasts yielded homogenates, from which marker enzymes for nuclei (NAD pyrophosphorylase) and mitochondria (cytochrome c oxidase activity and spectroscopically-detectable cytochromes a + a3) could be quantitatively sedimented by low-speed centrifugation. In contrast to previous findings with Saccharomyces carlsbergensis, cytochrome c oxidase and another mitochondrial enzyme, succinate dehydrogenase, were completely sedimentable by zonal centrifugation in sucrose gradients in the presence of either 2 mM-MgCl2 or 0-4 mM-EDTA. Mitochondria were apparently smaller and of lower buoyant density in gradients containing EDTA. The bulk of the total units of malate dehydrogenase and NADH; cytochrome c oxidoreductase sedimented with mitochondria, whereas NADPH: cytochrome c oxidoreductase was located in fractions containing no mitochondria. The distributions of mitochondrial enzymes were heterogeneous in populations of mitochondria separated on the basis of size or density. The possible origins of mitochondrial heterogeneity in extracts of S. pombe are discussed with special reference to changes in the enzyme activities of cells during the cell cycle.","authors":"Poole RK, Lloyd D","authors_abbrev":"Poole RK et al.","pubmed_publication_date":"Apr 1976","pubmed_entrez_date":"1976-04-01","publication_year":"1976","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8682866","title":"A novel suppressor of ras1 in fission yeast, byr4, is a dosage-dependent inhibitor of cytokinesis.","citation":"J Cell Biol 1996 Jun;133(6):1307-19","abstract":"A novel gene, designated byr4, was identified in Schizosaccharomyces pombe that affects the mitotic cell cycle and shows genetic interactions with the ras1 signaling pathways. Null alleles of byr4 cause cell cycle arrest in late mitosis and permit multiple rounds of septation. The multiple septa typically divide two nuclei, but the nuclei frequently do not stain equally with 4',6-diamidino-2-phenylindole (DAPI), suggesting that byr4 is required for proper karyokinesis. Overexpression of byr4 inhibits cytokinesis, but cell cycle progression continues leading to multinucleate cells. When byr4 is overexpressed, the early steps in the cytokinesis pathway, including formation of the medial F-actin ring, occur normally; however, the later steps in the pathway, including contraction of the F-actin ring, septation, and rearrangement of the medial F-actin following mitosis, rarely occur, byr4 shows two genetic interactions with ras1. The inhibition of cytokinesis by byr4 overexpression was exacerbated by null alleles of ras1 and scd1, suggesting a link between pathways needed for cell polarity and cytokinesis. Overexpression of byr4 also partially bypasses the need for ras1 for sporulation. The electrophoretic mobility of the byr4 protein varied in response to mutants that perturb cytokinesis and karyokinesis, suggesting interactions between byr4 and these gene products. A more rapidly migrating byr4 protein was found in cells with mutations in cdc16, which undergo repeated septation, and in cdc15, which fail to form a medial F-actin ring in mitosis. A slower migrating byr4 protein was found in cells with a mutation in the beta-tubulin gene, which arrests cells at the metaphase-anaphase transition.","authors":"Song K, Mach KE, Chen CY, Reynolds T, Albright CF","authors_abbrev":"Song K et al.","pubmed_publication_date":"Jun 1996","pubmed_entrez_date":"1996-06-01","publication_year":"1996","canto_session_key":"37758420451e8198","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-05-29 09:53:17","canto_approved_date":"2026-01-15 13:51:06","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-05-29 09:53:06","canto_added_date":"2012-02-24 05:53:55","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":12,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC222.10c","SPBC1D7.05","SPAC16E8.09","SPAC17H9.09c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-05-29"},{"uniquename":"PMID:9111307","title":"The Schizosaccharomyces pombe rad11+ gene encodes the large subunit of replication protein A.","citation":"Mol Cell Biol 1997 May;17(5):2381-90","abstract":"Replication protein A (RPA) is a heterotrimeric single-stranded DNA-binding protein present in all eukaryotes. In vitro studies have implicated RPA in simian virus 40 DNA synthesis and nucleotide excision repair, but little direct information is available about the in vivo roles of the protein. We report here the cloning of the largest subunit of RPA (rpa1+) from the fission yeast Schizosaccharomyces pombe. The rpa1+ gene is essential for viability and is expressed specifically at S phase of the cell cycle. Genetic analysis revealed that rpa1+ is the locus of the S. pombe radiation-sensitive mutation rad11. The rad11 allele exhibits pleiotropic effects consistent with an in vivo role for RPA in both DNA repair and DNA synthesis. The mutant is sensitive to both UV and ionizing radiation but is not defective in the DNA damage-dependent checkpoint, consistent with the hypothesis that RPA is part of the enzymatic machinery of DNA repair. When incubated in hydroxyurea, rad11 cells initially arrest with a 1C DNA content but then lose viability coincident with reentry into S phase, suggesting that DNA synthesis is aberrant under these conditions. A significant fraction of the mutant cells subsequently undergo inappropriate mitosis in the presence of hydroxyurea, indicating that RPA also plays a role in the checkpoint mechanism that monitors the completion of S phase. We propose that RPA is required to maintain the integrity of replication complexes when DNA replication is blocked. We further suggest that the rad11 mutation leads to the premature breakdown of such complexes, thereby preventing recovery from the hydroxyurea arrest and eliminating a signal recognized by the S-phase checkpoint mechanism.","authors":"Parker AE, Clyne RK, Carr AM, Kelly TJ","authors_abbrev":"Parker AE et al.","pubmed_publication_date":"May 1997","pubmed_entrez_date":"1997-05-01","publication_year":"1997","canto_session_key":"45f8955f7e6309ac","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2014-08-01 12:39:23","canto_approved_date":"2024-11-14 09:50:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-01 12:39:15","canto_added_date":"2012-02-24 05:53:37","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":14,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC660.13c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-01"},{"uniquename":"PMID:19281819","title":"Solution and crystal structures of mRNA exporter Dbp5p and its interaction with nucleotides.","citation":"J Mol Biol 2009 Apr 24;388(1):1-10","abstract":"DEAD-box protein 5 (Dbp5p) plays very important roles in RNA metabolism from transcription, to translation, to RNA decay. It is an RNA helicase and functions as an essential RNA export factor from nucleus. Here, we report the solution NMR structures of the N- and C-terminal domains (NTD and CTD, respectively) of Dbp5p from Saccharomyces cerevisiae (ScDbp5p) and X-ray crystal structure of Dbp5p from Schizosaccharomyces pombe (SpDbp5p) in the absence of nucleotides and RNA. The crystal structure clearly shows that SpDbp5p comprises two RecA-like domains that do not interact with each other. NMR results show that the N-terminal flanking region of ScDpbp5 (M1-E70) is intrinsically unstructured and the region Y71-R121 including the Q motif is highly dynamic on millisecond-microsecond timescales in solution. The C-terminal flanking region of ScDbp5p forms a short beta-strand and a long helix. This helix is unique for ScDbp5p and has not been observed in other DEAD-box proteins. Compared with other DEAD-box proteins, Dbp5p has an extra insert with six residues in the CTD. NMR structure reveals that the insert is located in a solvent-exposed loop capable of interacting with other proteins. ATP and ADP titration experiments show that both ADP and ATP bind to the consensus binding site in the NTD of ScDbp5p but do not interact with the CTD at all. Binding of ATP or ADP to NTD induces significant conformational rearrangement too.","doi":"10.1016/j.jmb.2009.03.004","authors":"Fan JS, Cheng Z, Zhang J, Noble C, Zhou Z, Song H, Yang D","authors_abbrev":"Fan JS et al.","pubmed_publication_date":"24 Apr 2009","pubmed_entrez_date":"2009-03-14","publication_year":"2009","canto_session_key":"ef929f13dffa6add","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-11-25 11:57:53","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-11-25 11:57:45","canto_added_date":"2012-02-24 05:48:11","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC12C2.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-11-25","pdb_entries":[{"pdb_id":"3fho","gene_chains":[{"gene_uniquename":"SPBC12C2.06","chain":"A/B","position":"139-503"}],"title":"Structure of S. pombe Dbp5","entry_authors":"Cheng Z,Song H","entry_authors_abbrev":"Cheng Z et al.","reference_uniquename":"PMID:19281819","experimental_method":"X-ray","resolution":"2.8"}]},{"uniquename":"PMID:28735863","title":"Structural insights into the specific recognition of DSR by the YTH domain containing protein Mmi1.","citation":"Biochem Biophys Res Commun 2017 Sep 16;491(2):310-316","abstract":"Meiosis is one of the most dramatic differentiation programs accompanied by a striking change in gene expression profiles in fission yeast Schizosaccharomyces pombe. Whereas a number of meiosis-specific transcripts are expressed untimely in mitotic cells, and the entry of meiosis will be blocked as the accumulation of meiosis-specific mRNAs in the mitotic cells. A YTH domain containing protein Mmi1 was identified as a pivotal effector in a post-transcriptional event termed selective elimination of meiosis-specific mRNAs. Mmi1 can recognize and bind a class of meiosis-specific transcripts expressed inappropriately in mitotic cells, which all contain a conservative region called DSR, as a mark to remove them in cooperation with nuclear exosomes. Here we report the 1.6 Å resolution crystal structure of the Mmi1-YTH domain in complex with a high consensus hexanucleotide motif, which is multiple copied in the DSR region. Our structure observations, supported by site-directed mutations of key residues illustrate the mechanism for specific recognition of DSR-RNA by Mmi1. Moreover, different from other YTH domain family proteins, Mmi1-YTH domain has a distinctive RNA-binding properties although it has a similar fold as other ones.","doi":"10.1016/j.bbrc.2017.07.104","authors":"Wu B, Xu J, Su S, Liu H, Gan J, Ma J","authors_abbrev":"Wu B et al.","pubmed_publication_date":"16 Sep 2017","pubmed_entrez_date":"2017-07-25","publication_year":"2017","canto_session_key":"e9efea9a0abc33d7","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-07-26 00:15:13","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.12c"],"gene_count":1,"ltp_gene_count":1,"pdb_entries":[{"pdb_id":"5eim","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A/B","position":"326-488"}],"title":"YTH domain-containing protein mmi1 and RNA complex","entry_authors":"Wu BX,Xu JH,Su SC,Ma JB","entry_authors_abbrev":"Wu BX et al.","reference_uniquename":"PMID:28735863","experimental_method":"X-ray","resolution":"1.54"},{"pdb_id":"5eip","gene_chains":[{"gene_uniquename":"SPCC736.12c","chain":"A/B","position":"349-477"}],"title":"apo-structure of YTH domain of SpMmi1","entry_authors":"Wu BX,Xu JH,Su SC,Ma JB","entry_authors_abbrev":"Wu BX et al.","reference_uniquename":"PMID:28735863","experimental_method":"X-ray","resolution":"1.49"}]},{"uniquename":"PMID:28977649","title":"The RNA chaperone La promotes pre-tRNA maturation via indiscriminate binding of both native and misfolded targets.","citation":"Nucleic Acids Res 2017 Nov 02;45(19):11341-11355","abstract":"Non-coding RNAs have critical roles in biological processes, and RNA chaperones can promote their folding into the native shape required for their function. La proteins are a class of highly abundant RNA chaperones that contact pre-tRNAs and other RNA polymerase III transcripts via their common UUU-3'OH ends, as well as through less specific contacts associated with RNA chaperone activity. However, whether La proteins preferentially bind misfolded pre-tRNAs or instead engage all pre-tRNA substrates irrespective of their folding status is not known. La deletion in yeast is synthetically lethal when combined with the loss of tRNA modifications predicted to contribute to the native pre-tRNA fold, such as the N2, N2-dimethylation of G26 by the methyltransferase Trm1p. In this work, we identify G26 containing pre-tRNAs that misfold in the absence of Trm1p and/or La (Sla1p) in Schizosaccharomyces pombe cells, then test whether La preferentially associates with such tRNAs in vitro and in vivo. Our data suggest that La does not discriminate a native from misfolded RNA target, and highlights the potential challenges faced by RNA chaperones in preferentially binding defective substrates.","doi":"10.1093/nar/gkx764","authors":"Vakiloroayaei A, Shah NS, Oeffinger M, Bayfield MA","authors_abbrev":"Vakiloroayaei A et al.","pubmed_publication_date":"02 Nov 2017","pubmed_entrez_date":"2017-10-05","publication_year":"2017","canto_session_key":"e6d012dea46b05f6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-11-08 14:07:28","canto_approved_date":"2025-09-03 13:38:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-10-26 14:27:25","canto_added_date":"2017-10-06 00:15:14","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":34,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC25D12.05","SPAC1F3.01","SPAC57A10.10c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-11-08"},{"uniquename":"PMID:16360688","title":"Control of Shugoshin function during fission-yeast meiosis.","citation":"Curr Biol 2005 Dec 20;15(24):2263-70","abstract":"Meiosis consists of a single round of DNA replication followed by two consecutive nuclear divisions. During the first division (MI), sister kinetochores must orient toward the same pole to favor reductional segregation. Correct chromosome segregation during the second division (MII) requires the retention of centromeric cohesion until anaphase II. The spindle checkpoint protein Bub1 is essential for both processes in fission yeast . When bub1 is deleted, the Shugoshin protein Sgo1 is not recruited to centromeres, cohesin Rec8 does not persist at centromeres, and sister-chromatid cohesion is lost by the end of MI. Deletion of bub1 also affects kinetochore orientation because sister centromeres can move to opposite spindle poles in approximately 30% of MI divisions. We show here that these two functions are separable within the Bub1 protein. The N terminus of Bub1 is necessary and sufficient for Sgo1 targeting to centromeres and the protection of cohesion, whereas the C-terminal kinase domain acts together with Sgo2, the second fission-yeast Shugoshin protein, to promote sister-kinetochore co-orientation during MI. Additional analyses suggest that the protection of centromeric cohesion does not operate when sister kinetochores attach to opposite spindle poles during MI. Sgo1-mediated protection of centromere cohesion might therefore be regulated by the mode of kinetochore attachment.","authors":"Vaur S, Cubizolles F, Plane G, Genier S, Rabitsch PK, Gregan J, Nasmyth K, Vanoosthuyse V, Hardwick KG, Javerzat JP","authors_abbrev":"Vaur S et al.","pubmed_publication_date":"20 Dec 2005","pubmed_entrez_date":"2005-12-20","publication_year":"2005","canto_session_key":"f3db412b3e0f395f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-04-30 14:01:07","canto_approved_date":"2024-06-15 15:41:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-04-24 18:47:13","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":25,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23H3.08c","SPBC20F10.06","SPBC3D6.04c","SPBP35G2.03c","SPCC1795.01c","SPBC106.01","SPCC1322.12c","SPBC29A10.14","SPCC4E9.01c","SPAC15A10.15"],"gene_count":10,"ltp_gene_count":6,"approved_date":"2024-04-30"},{"uniquename":"PMID:10411894","title":"Cell cycle regulation of Dfp1, an activator of the Hsk1 protein kinase.","citation":"Proc Natl Acad Sci U S A 1999 Jul 20;96(15):8443-8","abstract":"In fission yeast, the Hsk1 protein kinase is essential for the initiation of DNA replication. We have shown previously that Hsk1 forms a heterodimeric complex with the regulatory subunit, Dfp1. In this report we describe the further characterization of Dfp1. Reconstitution experiments with purified proteins indicate that Dfp1 is necessary and sufficient to activate Hsk1 phosphorylation of exogenous substrates, such as the Schizosaccharomyces pombe minichromosome maintenance protein Cdc19. The dfp1(+) gene is essential for viability of S. pombe, and depletion of the Dfp1 protein significantly delays the onset of S phase. Dfp1 is a phosphoprotein in vivo and becomes hyperphosphorylated when cells are blocked in S phase by treatment with the DNA synthesis inhibitor hydroxyurea. Hyperphosphorylation in S phase depends on the checkpoint kinase Cds1. The abundance of Dfp1 varies during progression through the cell cycle. The protein is absent when cells are arrested in G(1) phase. When cells are released into the cell cycle, Dfp1 appears suddenly at the G(1)/S transition, coincident with the initiation of DNA replication. The absence of Dfp1 before S phase is due largely, but not exclusively, to posttranscriptional regulation. We propose that cell cycle-regulated activation of Dfp1 expression at the G(1)/S transition results in activation of the Hsk1 protein kinase, which, in turn, leads to the initiation of DNA replication.","authors":"Brown GW, Kelly TJ","authors_abbrev":"Brown GW et al.","pubmed_publication_date":"20 Jul 1999","pubmed_entrez_date":"1999-07-21","publication_year":"1999","canto_session_key":"982b883bbf9c1c49","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2015-01-28 23:17:37","canto_approved_date":"2025-11-21 15:41:56","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2012-09-05 13:33:00","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":6,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC776.12c","SPCC550.13","SPBC4.04c"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2015-01-28"},{"uniquename":"PMID:27590019","title":"Glutathione-complexed [2Fe-2S] clusters function in Fe-S cluster storage and trafficking.","citation":"J Biol Inorg Chem 2016 Oct;21(7):887-901","abstract":"Glutathione-coordinated [2Fe-2S] complex is a non-protein-bound [2Fe-2S] cluster that is capable of reconstituting the human iron-sulfur cluster scaffold protein IscU. This complex demonstrates physiologically relevant solution chemistry and is a viable substrate for iron-sulfur cluster transport by Atm1p exporter protein. Herein, we report on some of the possible functional and physiological roles for this novel [2Fe-2S](GS4) complex in iron-sulfur cluster biosynthesis and quantitatively characterize its role in the broader network of Fe-S cluster transfer reactions. UV-vis and circular dichroism spectroscopy have been used in kinetic studies to determine second-order rate constants for [2Fe-2S] cluster transfer from [2Fe-2S](GS4) complex to acceptor proteins, such as human IscU, Schizosaccharomyces pombe Isa1, human and yeast glutaredoxins (human Grx2 and Saccharomyces cerevisiae Grx3), and human ferredoxins. Second-order rate constants for cluster extraction from these holo proteins were also determined by varying the concentration of glutathione, and a likely common mechanism for cluster uptake was determined by kinetic analysis. The results indicate that the [2Fe-2S](GS4) complex is stable under physiological conditions, and demonstrates reversible cluster exchange with a wide range of Fe-S cluster proteins, thereby supporting a possible physiological role for such centers.","doi":"10.1007/s00775-016-1387-2","authors":"Fidai I, Wachnowsky C, Cowan JA","authors_abbrev":"Fidai I et al.","pubmed_publication_date":"Oct 2016","pubmed_entrez_date":"2016-09-04","publication_year":"2016","canto_session_key":"8085e812b34993e5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2016-09-06 15:50:53","canto_approved_date":"2019-10-16 12:11:52","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2016-09-06 15:50:45","canto_added_date":"2016-09-05 00:15:14","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC645.03c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2016-09-06"},{"uniquename":"PMID:8978689","title":"Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of anaphase is lessened by the dosage increase of a novel gene sds23+.","citation":"EMBO J 1996 Dec 02;15(23):6629-40","abstract":"Ubiquitin-dependent proteolysis is required for the onset of anaphase. We show that protein dephosphorylation by protein phosphatase 1 (PP1) is also essential for initiating anaphase in fission yeast. PP1 may directly or indirectly regulate the 20S cyclosome/APC (anaphase-promoting complex) required for anaphase-promoting proteolysis. Using anti-phosphopeptide antibodies, PP1 is shown to be dephosphorylated at the C-terminus, upon the onset of anaphase, for reactivation. sds23+, a novel gene, is a multicopy suppressor for mutations in PP1 and the 20S cyclosome/APC, implying that the gene dosage increase can relieve the requirement for PP1 and the cyclosome/APC for the onset of anaphase. The sds23+ gene is not essential for cell viability, but a mutant with the gene deleted cannot form colonies at 22 and 36 degrees C. In the sds23 deletion mutant, the progression of anaphase and cytokinesis is retarded and cell shape is aberrant. These defects are overcome by plasmids carrying the genes encoding subunits of the 20S cyclosome/APC or PP1. These results demonstrate functions other than promoting anaphase for the components of the 20S cyclosome/APC and also a close functional relationship of Sds23 with PP1 and 20S cyclosome/APC.","authors":"Ishii K, Kumada K, Toda T, Yanagida M","authors_abbrev":"Ishii K et al.","pubmed_publication_date":"02 Dec 1996","pubmed_entrez_date":"1996-12-02","publication_year":"1996","canto_session_key":"d3a483f9bb7842f8","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-12-14 19:38:05","canto_approved_date":"2025-09-03 10:44:57","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-12-05 18:07:12","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":21,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC31H12.05c","SPAC6F12.15c","SPBC776.02c","SPAC17C9.01c","SPBC646.13","SPAC4A8.12c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2024-12-14"},{"uniquename":"PMID:30885940","title":"XPG-related nucleases are hierarchically recruited for double-stranded rDNA break resection.","citation":"J Biol Chem 2019 May 10;294(19):7632-7643","abstract":"dsDNA breaks (DSBs) are resected in a 5'→3' direction, generating single-stranded DNA (ssDNA). This promotes DNA repair by homologous recombination and also assembly of signaling complexes that activate the DNA damage checkpoint effector kinase Chk1. In fission yeast ( Schizosaccharomyces pombe ), genetic screens have previously uncovered a family of three xeroderma pigmentosum G (XPG)-related nucleases (XRNs), known as Ast1, Exo1, and Rad2. Collectively, these XRNs are recruited to a euchromatic DSB and are required for ssDNA production and end resection across the genome. Here, we studied why there are three related but distinct XRN enzymes that are all conserved across a range of species, including humans, whereas all other DSB response proteins are present as single species. Using  S. pombe  as a model, ChIP and DSB resection analysis assays, and highly efficient I-PpoI-induced DSBs in the 28S rDNA gene, we observed a hierarchy of recruitment for each XRN, with a progressive compensatory recruitment of the other XRNs as the responding enzymes are deleted. Importantly, we found that this hierarchy reflects the requirement for different XRNs to effect efficient DSB resection in the rDNA, demonstrating that the presence of three XRN enzymes is not a simple division of labor. Furthermore, we uncovered a specificity of XRN function with regard to the direction of transcription. We conclude that the DSB-resection machinery is complex, is nonuniform across the genome, and has built-in fail-safe mechanisms, features that are in keeping with the highly pathological nature of DSB lesions.","doi":"10.1074/jbc.RA118.005415","authors":"Barnum KJ, Nguyen YT, O'Connell MJ","authors_abbrev":"Barnum KJ et al.","pubmed_publication_date":"10 May 2019","pubmed_entrez_date":"2019-03-20","publication_year":"2019","canto_session_key":"6dcb87ac714a9811","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2019-03-21 01:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:27477275","title":"A Transcript-Specific eIF3 Complex Mediates Global Translational Control of Energy Metabolism.","citation":"Cell Rep 2016 Aug 16;16(7):1891-902","abstract":"The multi-subunit eukaryotic translation initiation factor eIF3 is thought to assist in the recruitment of ribosomes to mRNA. The expression of eIF3 subunits is frequently disrupted in human cancers, but the specific roles of individual subunits in mRNA translation and cancer remain elusive. Using global transcriptomic, proteomic, and metabolomic profiling, we found a striking failure of Schizosaccharomyces pombe cells lacking eIF3e and eIF3d to synthesize components of the mitochondrial electron transport chain, leading to a defect in respiration, endogenous oxidative stress, and premature aging. Energy balance was maintained, however, by a switch to glycolysis with increased glucose uptake, upregulation of glycolytic enzymes, and strict dependence on a fermentable carbon source. This metabolic regulatory function appears to be conserved in human cells where eIF3e binds metabolic mRNAs and promotes their translation. Thus, via its eIF3d-eIF3e module, eIF3 orchestrates an mRNA-specific translational mechanism controlling energy metabolism that may be disrupted in cancer.","doi":"10.1016/j.celrep.2016.07.006","authors":"Shah M, Su D, Scheliga JS, Pluskal T, Boronat S, Motamedchaboki K, Campos AR, Qi F, Hidalgo E, Yanagida M, Wolf DA","authors_abbrev":"Shah M et al.","pubmed_publication_date":"16 Aug 2016","pubmed_entrez_date":"2016-08-02","publication_year":"2016","canto_session_key":"05aaccc7039072b4","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-08-03 00:15:16","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:37459529","title":"Class I histone deacetylase complex: Structure and functional correlates.","citation":"Proc Natl Acad Sci U S A 2023 Jul 25;120(30):e2307598120","abstract":"The  Schizosaccharomyces pombe  Clr6S complex, a class I histone deacetylase complex, functions as a zinc-dependent enzyme to remove acetyl groups from lysine residues in histone tails. We report here the cryo-EM structure of Clr6S alone and a cryo-EM map of Clr6S in complex with a nucleosome. The active center, revealed at near-atomic resolution, includes features important for catalysis-A water molecule coordinated by zinc, the likely nucleophile for attack on the acetyl-lysine bond, and a loop that may position the substrate for catalysis. The cryo-EM map in the presence of a nucleosome reveals multiple Clr6S-nucleosome contacts and a high degree of relative motion of Clr6S and the nucleosome. Such flexibility may be attributed to interaction at a site in the flexible histone tail and is likely important for the function of the deacetylase, which acts at multiple sites in other histone tails.","doi":"10.1073/pnas.2307598120","authors":"Wang X, Wang Y, Liu S, Zhang Y, Xu K, Ji L, Kornberg RD, Zhang H","authors_abbrev":"Wang X et al.","pubmed_publication_date":"25 Jul 2023","pubmed_entrez_date":"2023-07-17","publication_year":"2023","canto_session_key":"d9b0a79b6b29212e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-02-13 14:38:35","canto_approved_date":"2024-02-29 12:44:42","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-02-13 14:38:27","canto_added_date":"2023-07-18 00:15:05","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":13,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23C11.15","SPAC2F7.07c","SPAC29A4.18","SPBC36.05c","SPAC23H4.12","SPAC16C9.05"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2024-02-13","pdb_entries":[{"pdb_id":"8ifg","gene_chains":[{"gene_uniquename":"SPAC23C11.15","chain":"A","position":"1-1075"},{"gene_uniquename":"SPAC23H4.12","chain":"D/E","position":"1-337"},{"gene_uniquename":"SPAC29A4.18","chain":"B","position":"1-431"},{"gene_uniquename":"SPBC36.05c","chain":"C","position":"5-405"},{"gene_uniquename":"SPAC2F7.07c","chain":"P","position":"1-607"},{"gene_uniquename":"SPAC16C9.05","chain":"F","position":"1-404"}],"title":"Cryo-EM structure of the Clr6S (Clr6-HDAC) complex from S. pombe","entry_authors":"Zhang HQ,Wang X,Wang YN,Liu SM,Zhang Y,Xu K,Ji LT,Kornberg RD","entry_authors_abbrev":"Zhang HQ et al.","reference_uniquename":"PMID:37459529","experimental_method":"EM","resolution":"3.2"}]},{"uniquename":"PMID:24999979","title":"High level constitutive expression of luciferase reporter by lsd90 promoter in fission yeast.","citation":"PLoS One 2014;9(7):e101201","abstract":"Because of a large number of molecular similarities with higher eukaryotes, the fission yeast Schizosaccharomyces pombe has been considered a potentially ideal host for expressing human proteins having therapeutic and pharmaceutical applications. However, efforts in this direction are hampered by lack of a strong promoter. Here, we report the isolation and characterization of a strong, constitutive promoter from S. pombe. A new expression vector was constructed by cloning the putative promoter region of the lsd90 gene (earlier reported to be strongly induced by heat stress) into a previously reported high copy number vector pJH5, which contained an ARS element corresponding to the mat2P flanking region and a truncated URA3m selectable marker. The resulting vector was used to study and compare the level of expression of the luciferase reporter with that achieved with the known vectors containing regulatable promoter nmt1 and the strong constitutive promoter adh1 in S. pombe and the methanol-inducible AOX1 promoter in Pichia pastoris. Following growth in standard media the new vector containing the putative lsd90 promoter provided constitutive expression of luciferase, at a level, which was 19-, 39- and 10-fold higher than that achieved with nmt1, adh1 and AOX1 promoters, respectively. These results indicate a great potential of the new lsd90 promoter-based vector for commercial scale expression of therapeutic proteins in S. pombe.","doi":"10.1371/journal.pone.0101201","authors":"Verma HK, Shukla P, Alfatah M, Khare AK, Upadhyay U, Ganesan K, Singh J","authors_abbrev":"Verma HK et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-07-08","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-07-09 00:15:29","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:2188102","title":"U1 small nuclear RNA from Schizosaccharomyces pombe has unique and conserved features and is encoded by an essential single-copy gene.","citation":"Mol Cell Biol 1990 Jun;10(6):2874-81","abstract":"We have cloned, sequenced, and disrupted the gene encoding U1 small nuclear RNA (snRNA) in the fission yeast Schizosaccharomyces pombe. This RNA is close in size and exhibits a high degree of secondary structure homology to human U1 RNA. There exist two regions of extended primary sequence identity between S. pombe and human U1 RNAs; the first comprises nucleotides involved in hydrogen bonding to 5' splice junctions, and the second is a single-stranded region which, in the human snRNA, forms part of the A protein binding site. S. pombe U1 lacks two nucleotides just following the 5' cap structure which are present in all other U1 homologs examined to date, and the region which corresponds to the binding site for the human 70K protein (molecular weight of 55,000) is more divergent than in other organisms. A putative upstream transcription signal is conserved in sequence and location among all loci encoding spliceosomal snRNAs in S. pombe with the exception of U6. Disruption of the single-copy U1 gene, designated snu1, reveals that this RNA is indispensable for viability.","authors":"Porter G, Brennwald P, Wise JA","authors_abbrev":"Porter G et al.","pubmed_publication_date":"Jun 1990","pubmed_entrez_date":"1990-06-01","publication_year":"1990","canto_session_key":"60969c954007a561","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_approved_date":"2015-09-17 13:21:52","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2014-06-18 19:41:55","canto_added_date":"2012-02-24 05:55:22","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPSNRNA.01"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-06-18"},{"uniquename":"PMID:12618370","title":"Schizosaccharomyces pombe essential genes: a pilot study.","citation":"Genome Res 2003 Mar;13(3):399-406","abstract":"After completion of the Schizosaccharomyces pombe genome sequence, we have carried out a pilot gene deletion project to assess the feasibility of a genome-wide deletion project and to estimate the percentage of essential genes. Using a PCR-based gene deletion procedure, we investigated 100 genes within a 253-kb region of chromosome II. Eight of nine genes located within a region of 18 kb could not be deleted, suggesting that systematic deletion of all fission yeast genes may be difficult to achieve using this PCR approach. The percentage of essential genes was found to be 17.5%. Further deletion of selected S. pombe genes revealed that whether a gene is essential or not is correlated with the timing of its appearance on the tree of life and its conservation within all branches of the tree. None of the investigated ancient genes in fission yeast that have been lost in the Saccharomyces cerevisiae lineage are essential. In agreement with S. cerevisiae and Caenorhabditis elegans genome analyses, our data suggest that natural selection has preferentially kept the genes required for vital functions. We propose that many of the essential eukaryotic genes appeared with the first eukaryotic cell and have remained conserved in all species.","authors":"Decottignies A, Sanchez-Perez I, Nurse P","authors_abbrev":"Decottignies A et al.","pubmed_publication_date":"Mar 2003","pubmed_entrez_date":"2003-03-06","publication_year":"2003","canto_session_key":"129db3623070653e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2014-07-01 07:08:55","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-06-30 18:53:42","canto_added_date":"2012-02-24 05:50:45","annotation_curators":[],"file_curator_name":"Midori Harris","file_curator_role":"PomBase","annotation_file_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":116,"orcid":"0000-0003-4148-4606","file_type":"PHAF","file_name":"PMID_12618370_phaf.tsv"}],"genes":["SPBC428.08c","SPBC902.05c","SPBC902.03","SPAC1687.17c","SPBC582.07c","SPBC31F10.02","SPBC582.04c","SPBC106.09","SPBC1271.06c","SPBC582.08","SPAC30.03c","SPBC902.06","SPAC25H1.02","SPBC1685.04","SPBC725.10","SPBP23A10.12","SPBC106.04","SPBC1271.01c","SPBC902.04","SPBC649.04","SPBC11B10.09","SPBC1685.01","SPBC1685.06","SPBC577.03c","SPBC1685.09","SPBC3B9.08c","SPBC19F8.02","SPBC1685.05","SPBC1685.07c","SPBC582.05c","SPBC1685.03","SPAC15A10.10","SPBC106.10","SPCC1020.09","SPBC428.12c","SPAC3A11.10c","SPBC1685.11","SPAP8A3.12c","SPBC428.01c","SPBC582.03","SPAC22A12.03c","SPBC20F10.03","SPBC428.18","SPBC354.01","SPBC428.10","SPBC354.07c","SPBC16G5.07c","SPBC1271.12","SPBC106.07c","SPBC582.10c","SPBC1685.08","SPBC1685.15c","SPBC649.05","SPBC428.19c","SPBC106.17c","SPBC1271.14","SPBC2F12.12c","SPAC22F3.02","SPBC428.11","SPBC428.04","SPBC428.05c","SPBC1271.10c","SPBC106.03","SPBC1271.13","SPBC428.03c","SPBC649.03","SPBC106.08c","SPBC428.14","SPCC645.08c","SPBC649.02","SPCC736.09c","SPBC354.09c","SPBC13G1.04c","SPBC1271.03c","SPBC428.17c","SPBC354.14c","SPBC4.05","SPBC582.06c","SPBC106.05c","SPBC354.15","SPBC428.20c","SPBC146.06c","SPBP35G2.02","SPBC1271.09","SPAC17A5.04c","SPBC1271.02","SPAC1565.02c","SPAC630.13c","SPBC428.13c","SPAC1952.06c","SPCC965.12","SPBC342.04","SPAC13G6.09","SPBC428.02c","SPBC1685.14c","SPBC1271.05c","SPBC1271.07c","SPBC902.02c","SPCC1020.12c","SPBC106.06","SPBC428.16c","SPBC1271.15c","SPBC428.06c","SPBC106.20","SPBC354.08c","SPBC1685.02c","SPBC1271.11","SPAC1805.08","SPBC354.10","SPCC736.08","SPBC354.02c","SPBC1271.08c","SPAC343.18"],"gene_count":113,"ltp_gene_count":112,"approved_date":"2014-06-30"},{"uniquename":"PMID:24249576","title":"Chromatin-associated ncRNA activities.","citation":"Chromosome Res 2013 Dec;21(6-7):627-41","abstract":"RNA transcripts that do not code for proteins have been long known to lie at the heart of many biological processes, such as splicing and translation. Yet their full potential has only been appreciated recently and non-coding RNAs (ncRNAs) are now attracting increasing attention. Pioneering work in yeast and plant systems has revealed that non-coding RNAs can have a major influence on the deposition of histone and DNA modifications. This can introduce heritable variation into gene expression and, thus, be the basis of epigenetic phenomena. Mechanistically, such processes have been studied extensively in the fission yeast Schizosaccharomyces pombe, providing an important conceptual framework for possible modes of action of ncRNAs also in other organisms. In this review, we highlight mechanistic insights into chromatin-associated ncRNA activities gained from work with fission yeast, and we draw parallels to studies in other eukaryotes that indicate evolutionary conservation.","doi":"10.1007/s10577-013-9390-8","authors":"Keller C, Bühler M","authors_abbrev":"Keller C et al.","pubmed_publication_date":"Dec 2013","pubmed_entrez_date":"2013-11-20","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15615781","title":"The novel fission yeast (1,3)beta-D-glucan synthase catalytic subunit Bgs4p is essential during both cytokinesis and polarized growth.","citation":"J Cell Sci 2005 Jan 01;118(Pt 1):157-74","abstract":"Schizosaccharomyces pombe contains four putative (1,3)beta-D-glucan synthase (GS) catalytic subunits, Bgs1p-4p. In this work, we cloned bgs4+ and show that Bgs4p is the only subunit found to be a part of the GS enzyme and essential for maintaining cell integrity during cytokinesis and polarized growth. Here we show that bgs4+, cwg1+ (cwg1-1 shows reduced cell-wall beta-glucan and GS catalytic activity) and orb11+ (orb11-59 is defective in cell morphogenesis) are the same gene. bgs4+ is essential for spore germination and bgs4+ shut-off produces cell lysis at growing poles and mainly at the septum prior to cytokinesis, suggesting that Bgs4p is essential for cell wall growth and to compensate for an excess of cell wall degradation during cytokinesis. Shut-off and overexpression analysis suggest that Bgs4p forms part of a GS catalytic multiprotein complex and that Bgs4p-promoted cell-wall beta-glucan alterations induce compensatory mechanisms from other Bgs subunits and (1,3)alpha-D-glucan synthase. Physiological localization studies showed that Bgs4p localizes to the growing ends, the medial ring and septum, and at each stage of wall synthesis or remodeling that occurs during sexual differentiation: mating, zygote and spore formation, and spore germination. Bgs4p timing and requirements for proper positioning during cytokinesis and its localization pattern during spore maturation differ from those of Bgs1p. Bgs4p localizes overlapping the contractile ring once Bgs1p is present and a Calcofluor white-stained septum material is detected, suggesting that Bgs4p is involved in a late process of secondary or general septum synthesis. Unlike Bgs1p, Bgs4p needs the medial ring but not the septation initiation network proteins to localize with the other septation components. Furthermore, Bgs4p localization depends on the polarity establishment proteins. Finally, F-actin is necessary for Bgs4p delocalization from and relocalization to the growing regions, but it is not needed for the stable maintenance of Bgs4p at the growing sites, poles and septum. All these data show for the first time an essential role for a Bgs subunit in the synthesis of a (1,3)beta-D-glucan necessary to preserve cell integrity when cell wall synthesis or repair are needed.","authors":"Cortés JC, Carnero E, Ishiguro J, Sánchez Y, Durán A, Ribas JC","authors_abbrev":"Cortés JC et al.","pubmed_publication_date":"01 Jan 2005","pubmed_entrez_date":"2004-12-24","publication_year":"2005","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:05","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC1840.02c","SPBC19G7.05c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:11121040","title":"Yin6, a fission yeast Int6 homolog, complexes with Moe1 and plays a role in chromosome segregation.","citation":"Proc Natl Acad Sci U S A 2000 Dec 19;97(26):14370-5","abstract":"The INT6 gene has been implicated in human breast cancer formation, but its function is unknown. We isolated an Int6 homolog from fission yeast, Yin6, by its binding to a conserved protein in the Ras pathway, Moe1. Yin6 and Moe1 converge on the same protein complex to promote microtubule instability/disassembly. Yin6 and Moe1 interact cooperatively: when either protein is absent, the other becomes mislocalized with decreased protein levels. Furthermore, whereas full-length human Int6 rescues the phenotypes of the yin6-null (yin6Delta) mutant cells and binds human Moe1, truncated Int6 proteins found in tumors do not. Importantly, yin6Delta alone impairs chromosome segregation weakly, but yin6Delta together with ras1Delta causes severe chromosome missegregation. These data support a model in which INT6 mutations in humans either alone or together with additional mutations, such as a RAS mutation, may contribute to tumorigenesis by altering genome stability.","authors":"Yen HC, Chang EC","authors_abbrev":"Yen HC et al.","pubmed_publication_date":"19 Dec 2000","pubmed_entrez_date":"2000-12-20","publication_year":"2000","canto_session_key":"2de3ef290c749683","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-07-19 11:19:47","canto_approved_date":"2019-06-14 09:09:59","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2015-07-27 16:38:57","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":27,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC637.07","SPAC17H9.09c","SPBC646.09c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-07-19"},{"uniquename":"PMID:29863659","title":"Gene-targeted Random Mutagenesis to Select Heterochromatin-destabilizing Proteasome Mutants in Fission Yeast.","citation":"J Vis Exp 2018 May 15;(135)","abstract":"Random mutagenesis of a target gene is commonly used to identify mutations that yield the desired phenotype. Of the methods that may be used to achieve random mutagenesis, error-prone PCR is a convenient and efficient strategy for generating a diverse pool of mutants (i.e., a mutant library). Error-prone PCR is the method of choice when a researcher seeks to mutate a pre-defined region, such as the coding region of a gene while leaving other genomic regions unaffected. After the mutant library is amplified by error-prone PCR, it must be cloned into a suitable plasmid. The size of the library generated by error-prone PCR is constrained by the efficiency of the cloning step. However, in the fission yeast, Schizosaccharomyces pombe, the cloning step can be replaced by the use of a highly efficient one-step fusion PCR to generate constructs for transformation. Mutants of desired phenotypes may then be selected using appropriate reporters. Here, we describe this strategy in detail, taking as an example, a reporter inserted at centromeric heterochromatin.","doi":"10.3791/57499","authors":"Seo HD, Lee D","authors_abbrev":"Seo HD et al.","pubmed_publication_date":"15 May 2018","pubmed_entrez_date":"2018-06-05","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-06-05 11:28:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:38392788","title":"The Roles of Septins in Regulating Fission Yeast Cytokinesis.","citation":"J Fungi (Basel) 2024 Jan 30;10(2)","abstract":"Cytokinesis is required to separate two daughter cells at the end of mitosis, and septins play crucial roles in many aspects of cytokinesis. While septins have been intensively studied in many model organisms, including the budding yeast  Saccharomyces cerevisiae , septins have been relatively less characterized in the fission yeast  Schizosaccharomyces pombe , which has proven to be an excellent model organism for studying fundamental cell biology. In this review, we summarize the findings of septins made in fission yeasts mainly from four aspects: the domain structure of septins, the localization of septins during the cell cycle, the roles of septins in regulating cytokinesis, and the regulatory proteins of septins.","doi":"10.3390/jof10020115","authors":"Zheng S, Zheng B, Fu C","authors_abbrev":"Zheng S et al.","pubmed_publication_date":"30 Jan 2024","pubmed_entrez_date":"2024-02-23","publication_year":"2024","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2024-02-24 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20708587","title":"CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule.","citation":"Dev Cell 2010 Aug 17;19(2):245-58","abstract":"Spatial regulation of microtubule (MT) dynamics contributes to cell polarity and cell division. MT rescue, in which a MT stops shrinking and reinitiates growth, is the least understood aspect of MT dynamics. Cytoplasmic Linker Associated Proteins (CLASPs) are a conserved class of MT-associated proteins that contribute to MT stabilization and rescue in vivo. We show here that the Schizosaccharomyces pombe CLASP, Cls1p, is a homodimer that binds an alphabeta-tubulin heterodimer through conserved TOG-like domains. In vitro, CLASP increases MT rescue frequency, decreases MT catastrophe frequency, and moderately decreases MT disassembly rate. CLASP binds stably to the MT lattice, recruits tubulin, and locally promotes rescues. Mutations in the CLASP TOG domains demonstrate that tubulin binding is critical for its rescue activity. We propose a mechanism for rescue in which CLASP-tubulin dimer complexes bind along the MT lattice and reverse MT depolymerization with their bound tubulin dimer.","doi":"10.1016/j.devcel.2010.07.016","authors":"Al-Bassam J, Kim H, Brouhard G, van Oijen A, Harrison SC, Chang F","authors_abbrev":"Al-Bassam J et al.","pubmed_publication_date":"17 Aug 2010","pubmed_entrez_date":"2010-08-17","publication_year":"2010","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:29","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G9.12","SPBC16A3.15c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:22661707","title":"A measurable activation of the bZIP transcription factor Atf1 in a fission yeast strain devoid of stress-activated and cell integrity mitogen-activated protein kinase (MAPK) activities.","citation":"J Biol Chem 2012 Jul 06;287(28):23434-9","abstract":"In Schizosaccharomyces pombe, the stress-activated Sty1 MAPK pathway is essential for cell survival under stress conditions. The Sty1 MAPK regulates Atf1 transcription factor to elicit stress responses in extreme conditions of osmolarity and reactive oxygen species-generating agents such as hydrogen peroxide, heat, low glucose, and heavy metal. Herein, using a newly developed Renilla luciferase reporter assay with enhanced detection sensitivity and accuracy, we show that distinct signaling pathways respond to cadmium and other reactive oxygen species-generating agents for the activation of Atf1. Also, surprisingly, a measurable activation of Atf1 transcription factor was still observed devoid of Sty1 MAPK activity. Further genetic and biological analyses revealed that the residual activation is caused by the activation of the cell wall integrity Pmk1 MAPK pathway and a redox-mediated activation of Atf1.","doi":"10.1074/jbc.C111.338715","authors":"Zhou X, Ma Y, Kato T, Kuno T","authors_abbrev":"Zhou X et al.","pubmed_publication_date":"06 Jul 2012","pubmed_entrez_date":"2012-06-05","publication_year":"2012","canto_session_key":"0f70615b481efcb2","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Xin Zhou","canto_first_approved_date":"2018-08-09 07:05:33","canto_approved_date":"2025-05-27 13:35:10","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-02 19:00:36","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[{"name":"Xin Zhou","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1006.09","SPBC29B5.01","SPAC24B11.06c","SPBC119.08","SPAC26F1.10c","SPAC9G1.02","SPBC409.07c","SPBC887.10"],"gene_count":8,"ltp_gene_count":5,"approved_date":"2018-08-09"},{"uniquename":"PMID:10545196","title":"The sen1(+) gene of Schizosaccharomyces pombe, a homologue of budding yeast SEN1, encodes an RNA and DNA helicase.","citation":"Biochemistry 1999 Nov 02;38(44):14697-710","abstract":"Two polynucleotide-dependent ATPases, 95 and 181 kDa in size, have been purified to near homogeneity from cell-free extracts of Schizosaccharomyces pombe. Despite their size differences, their biochemical properties were strikingly similar. Both enzymes were capable of unwinding RNA and DNA duplexes in keeping with their ability to hydrolyze ATP in the presence of either ribo- or deoxyribopolynucleotide. In addition, they were capable of unwinding DNA/RNA or RNA/DNA hybrid duplexes and translocated in the 5' to 3' direction. These results strongly indicate that they are closely related to each other. Determination of the partial amino acid sequence of the 95-kDa enzyme revealed that it is encoded by the sen1(+)() gene, an S. pombe homologue of yeast SEN1, a protein essential for the processing of small nucleolar RNA, transfer RNA, and ribosomal RNA. The molecular weight of the S. pombe Sen1 protein (SpSen1p) predicted from the sen1(+)() open reading frame was 192.5 kDa, suggesting that the 181-kDa enzyme is likely to be a full-length protein, whereas the 95-kDa polypeptide has arisen by proteolysis. In accord with this possibility, polyclonal antibodies specific to the C-terminal region of sen1(+)() cross-reacted with both 95- and 181-kDa polypeptides. We discuss the biochemical activities associated with SpSen1p and their relevance to the apparently divergent functions ascribed to the yeast Sen1 protein in RNA metabolism.","authors":"Kim HD, Choe J, Seo YS","authors_abbrev":"Kim HD et al.","pubmed_publication_date":"02 Nov 1999","pubmed_entrez_date":"1999-11-05","publication_year":"1999","canto_session_key":"79289f0f7fa14151","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-01-18 22:41:51","canto_approved_date":"2019-12-03 09:31:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-07-02 12:14:41","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC6G9.10c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-01-18"},{"uniquename":"PMID:30427751","title":"The J-domain cochaperone Rsp1 interacts with Mto1 to organize noncentrosomal microtubule assembly.","citation":"Mol Biol Cell 2019 Jan 15;30(2):256-267","abstract":"Microtubule biogenesis initiates at various intracellular sites, including the centrosome, the Golgi apparatus, the nuclear envelope, and preexisting microtubules. Similarly, in the fission yeast Schizosaccharomyces pombe, interphase microtubules are nucleated at the spindle pole body (SPB), the nuclear envelope, and preexisting microtubules, depending on Mto1 activity. Despite the essential role of Mto1 in promoting microtubule nucleation, how distribution of Mto1 in different sites is regulated has remained elusive. Here, we show that the J-domain cochaperone Rsp1 interacts with Mto1 and specifies the localization of Mto1 to non-SPB nucleation sites. The absence of Rsp1 abolishes the localization of Mto1 to non-SPB nucleation sites, with concomitant enrichment of Mto1 to the SPB and the nuclear envelope. In contrast, Rsp1 overexpression impairs the localization of Mto1 to all microtubule organization sites. These findings delineate a previously uncharacterized mechanism in which Rsp1-Mto1 interaction orchestrates non-SPB microtubule formation.","doi":"10.1091/mbc.E18-05-0279","authors":"Shen J, Li T, Niu X, Liu W, Zheng S, Wang J, Wang F, Cao X, Yao X, Zheng F, Fu C","authors_abbrev":"Shen J et al.","pubmed_publication_date":"15 Jan 2019","pubmed_entrez_date":"2018-11-15","publication_year":"2019","canto_session_key":"6743693a29a7b5bb","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chuanhai Fu","canto_first_approved_date":"2019-05-31 02:35:08","canto_approved_date":"2019-06-01 08:55:37","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-05-26 09:16:06","canto_added_date":"2018-11-16 01:15:05","annotation_curators":[{"name":"Chuanhai Fu","community_curator":true,"annotation_count":2,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":17,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC365.15","SPCC417.07c","SPBC11B10.05c","SPBC30B4.06c","SPAPB1A10.09","SPAC1786.03","SPBC800.05c","SPBC902.06"],"gene_count":8,"ltp_gene_count":4,"approved_date":"2019-05-31"},{"uniquename":"PMID:20130084","title":"A guaninine nucleotide exchange factor is a component of the meiotic spindle pole body in Schizosaccharomyces pombe.","citation":"Mol Biol Cell 2010 Apr 01;21(7):1272-81","abstract":"Spore morphogenesis in yeast is driven by the formation of membrane compartments that initiate growth at the spindle poles during meiosis II and grow to encapsulate daughter nuclei. Vesicle docking complexes, called meiosis II outer plaques (MOPs), form on each meiosis II spindle pole body (SPB) and serve as sites of membrane nucleation. How the MOP stimulates membrane assembly is not known. Here, we report that SpSpo13, a component of the MOP in Schizosaccharomyces pombe, shares homology with the guanine nucleotide exchange factor (GEF) domain of the Saccharomyces cerevisiae Sec2 protein. ScSec2 acts as a GEF for the small Rab GTPase ScSec4, which regulates vesicle trafficking from the late-Golgi to the plasma membrane. A chimeric protein in which the ScSec2-GEF domain is replaced with SpSpo13 is capable of supporting the growth of a sec2Delta mutant. SpSpo13 binds preferentially to the nucleotide-free form of ScSec4 and facilitates nucleotide exchange in vitro. In vivo, a Spspo13 mutant defective in GEF activity fails to support membrane assembly. In vitro specificity experiments suggest that SpYpt2 is the physiological substrate of SpSpo13. These results demonstrate that stimulation of Rab-GTPase activity is a property of the S. pombe MOP essential for the initiation of membrane formation.","authors":"Yang HJ, Neiman AM","authors_abbrev":"Yang HJ et al.","pubmed_publication_date":"01 Apr 2010","pubmed_entrez_date":"2010-02-05","publication_year":"2010","canto_session_key":"f7a6b2bfb508bcb4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2024-08-12 20:37:01","canto_approved_date":"2024-10-02 14:17:22","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2024-10-01 06:35:56","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":7,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC1183.12","SPAC9E9.07c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2024-08-12"},{"uniquename":"PMID:24316795","title":"Distinct levels in Pom1 gradients limit Cdr2 activity and localization to time and position division.","citation":"Cell Cycle 2014;13(4):538-52","abstract":"Where and when cells divide are fundamental questions. In rod-shaped fission yeast cells, the DYRK-family kinase Pom1 is organized in concentration gradients from cell poles and controls cell division timing and positioning. Pom1 gradients restrict to mid-cell the SAD-like kinase Cdr2, which recruits Mid1/Anillin for medial division. Pom1 also delays mitotic commitment through Cdr2, which inhibits Wee1. Here, we describe quantitatively the distributions of cortical Pom1 and Cdr2. These reveal low profile overlap contrasting with previous whole-cell measurements and Cdr2 levels increase with cell elongation, raising the possibility that Pom1 regulates mitotic commitment by controlling Cdr2 medial levels. However, we show that distinct thresholds of Pom1 activity define the timing and positioning of division. Three conditions-a separation-of-function Pom1 allele, partial downregulation of Pom1 activity, and haploinsufficiency in diploid cells-yield cells that divide early, similar to pom1 deletion, but medially, like wild-type cells. In these cells, Cdr2 is localized correctly at mid-cell. Further, Cdr2 overexpression promotes precocious mitosis only in absence of Pom1. Thus, Pom1 inhibits Cdr2 for mitotic commitment independently of regulating its localization or cortical levels. Indeed, we show Pom1 restricts Cdr2 activity through phosphorylation of a C-terminal self-inhibitory tail. In summary, our results demonstrate that distinct levels in Pom1 gradients delineate a medial Cdr2 domain, for cell division placement, and control its activity, for mitotic commitment.","doi":"10.4161/cc.27411","authors":"Bhatia P, Hachet O, Hersch M, Rincon SA, Berthelot-Grosjean M, Dalessi S, Basterra L, Bergmann S, Paoletti A, Martin SG","authors_abbrev":"Bhatia P et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2013-12-10","publication_year":"2014","canto_session_key":"bbe966c7c31d9042","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Payal Bhatia","canto_first_approved_date":"2018-10-02 14:11:16","canto_approved_date":"2025-12-03 12:08:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-04-19 10:01:13","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":46,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Payal Bhatia","community_curator":true,"annotation_count":3,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC57A10.02","SPAC2F7.03c","SPAC15A10.16"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2018-10-02"},{"uniquename":"PMID:36098897","title":"Biochemical characterization of clinically relevant mutations of human Translin.","citation":"Mol Cell Biochem 2023 Apr;478(4):821-834","abstract":"DNA damage in all living cells is repaired with very high efficiency and nucleic acid binding proteins play crucial roles in repair associated processes. Translin is one such evolutionarily conserved nucleic acid interacting protein speculated to be a part of the DNA repair protein network. It is also involved in activation of RNA-induced silencing complex (RISC) along with Translin-associated factor X (TRAX) as the C3PO (component 3 promoter of RISC) complex. In the present work, we characterized ten clinically relevant variants of the human Translin protein using bioinformatic, biochemical, and biophysical tools. Bioinformatic studies using DynaMut revealed 9 out of the 10 selected mutations the Translin protein. Further analysis revealed that some mutations lead to changes in interactions with neighbouring residues in the protein structure. Using site directed mutagenesis, the point substitution variants were generated, corresponding proteins were overexpressed and purified using Ni-NTA affinity chromatography. Purified proteins form octamers similar to wild type (WT) Translin, as observed using native polyacrylamide gel electrophoresis (PAGE), gel filtration, and dynamic light-scattering (DLS) analysis. These octamers are functional and bind to single-stranded DNA (ssDNA) as well as single-stranded RNA (ssRNA) substrates. The mutant Translin proteins interact with wild type TRAX and form corresponding C3PO complexes. The C3PO complexes formed by all Translin variants with TRAX are functional in-vitro and show endoribonuclease activity. However, significant differences were observed in the extent of RNase activity in vitro. In conclusion, the clinically relevant mutations in Translin protein analysed by us exert their effect by modulating the RNase activity of the protein without altering its DNA-dependant function.","doi":"10.1007/s11010-022-04556-4","authors":"Pillai V, Gupta A, Rao A, Chittela RK","authors_abbrev":"Pillai V et al.","pubmed_publication_date":"Apr 2023","pubmed_entrez_date":"2022-09-13","publication_year":"2023","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPCC736.09c","SPAC30.03c"],"gene_count":2,"ltp_gene_count":0},{"uniquename":"PMID:39527196","title":"Bimolecular Fluorescence Complementation as a Tool to Study Specific Dynamic Interactions Between Proteins in Fission Yeast.","citation":"Methods Mol Biol 2025;2862:103-120","abstract":"Bimolecular fluorescence complementation (BiFC) is a technique that enables real-time observation within living cells of the interaction between two proteins forming a complex, determining the location where such interaction occurs within the cell, and even the association and dissociation cycles in response to physiological cues. Here, we describe in detail the use of bimolecular fluorescence complementation to visualize the assembly and disassembly of cohesin over the fission yeast cell cycle.","doi":"10.1007/978-1-0716-4168-2_8","authors":"Gonzalez-Martin E, Tallada VA","authors_abbrev":"Gonzalez-Martin E et al.","pubmed_publication_date":"2025","pubmed_entrez_date":"2024-11-11","publication_year":"2025","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2024-11-14 00:25:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10400922","title":"The genomic tree as revealed from whole proteome comparisons.","citation":"Genome Res 1999 Jun;9(6):550-7","abstract":"The availability of a number of complete cellular genome sequences allows the development of organisms' classification, taking into account their genome content, the loss or acquisition of genes, and overall gene similarities as signatures of common ancestry. On the basis of correspondence analysis and hierarchical classification methods, a methodological framework is introduced here for the classification of the available 20 completely sequenced genomes and partial information for Schizosaccharomyces pombe, Homo sapiens, and Mus musculus. The outcome of such an analysis leads to a classification of genomes that we call a genomic tree. Although these trees are phenograms, they carry with them strong phylogenetic signatures and are remarkably similar to 16S-like rRNA-based phylogenies. Our results suggest that duplication and deletion events that took place through evolutionary time were globally similar in related organisms. The genomic trees presented here place the Archaea in the proximity of the Bacteria when the whole gene content of each organism is considered, and when ancestral gene duplications are eliminated. Genomic trees represent an additional approach for the understanding of evolution at the genomic level and may contribute to the proper assessment of the evolutionary relationships between extant species.","authors":"Tekaia F, Lazcano A, Dujon B","authors_abbrev":"Tekaia F et al.","pubmed_publication_date":"Jun 1999","pubmed_entrez_date":"1999-07-13","publication_year":"1999","canto_triage_status":"Phylogeny and evolutionary studies","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:40","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8437591","title":"Size variation of rDNA clusters in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1993 Jan;236(2-3):448-52","abstract":"The higher-order organization of rRNA genes was investigated in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. We used pulsed-field gel electrophoresis (PFGE) in combination with frequent cutter endonucleases having no recognition sites within rDNA repeating units to characterize tandem arrays of ribosomal genes in these two species. Large variations in rDNA cluster length were detected in various S. cerevisiae and S. pombe strains commonly used as PFGE molecular weight markers. This wide range of variability implies that the sizes currently assessed for chromosomes bearing rRNA genes in these organisms are unreliable since they may vary within strains by several hundreds of kilobase pairs, depending on the size of the tandem arrays of rRNA genes. Consequently, there is now a lack of reliable PFGE size standards between 1.6 Mb and 4.5 Mb, even when established yeast strains with calibrated chromosomes are used.","authors":"Pasero P, Marilley M","authors_abbrev":"Pasero P et al.","pubmed_publication_date":"Jan 1993","pubmed_entrez_date":"1993-01-01","publication_year":"1993","canto_session_key":"a84984ee79e12c62","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-12-22 20:06:26","canto_approved_date":"2018-12-22 20:06:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-12-22 20:06:19","canto_added_date":"2012-02-24 05:55:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2018-12-22"},{"uniquename":"PMID:9207030","title":"Complementation of the DNA repair-deficient swi10 mutant of fission yeast by the human ERCC1 gene.","citation":"Nucleic Acids Res 1997 Jul 15;25(14):2823-7","abstract":"In human cells DNA damage caused by UV light is mainly repaired by the nucleotide excision repair pathway. This mechanism involves dual incisions on both sides of the damage catalyzed by two nucleases. In mammalian cells XPG cleaves 3' of the DNA lesion while the ERCC1-XPF complex makes the 5' incision. The amino acid sequence of the human excision repair protein ERCC1 is homologous with the fission yeast Swi10 protein. In order to test whether these proteins are functional homologues, we overexpressed the human gene in a Schizosaccharomyces pombe swi10 mutant. A swi10 mutation has a pleiotropic effect: it reduces the frequency of mating type switching (a mitotic transposition event from a silent cassette into the expression site) and causes increased UV sensitivity. We found that the full-length ERCC1 gene only complements the transposition defect of the fission yeast mutant, while a C-terminal truncated ERCC1 protein also restores the DNA repair capacity of the yeast cells. Using the two-hybrid system of Saccharomyces cerevisiae we show that only the truncated human ERCC1 protein is able to interact with the S . pombe Rad16 protein, which is the fission yeast homologue of human XPF. This is the first example yet known that a human gene can correct a yeast mutation in nucleotide excision repair.","authors":"Rödel C, Jupitz T, Schmidt H","authors_abbrev":"Rödel C et al.","pubmed_publication_date":"15 Jul 1997","pubmed_entrez_date":"1997-07-15","publication_year":"1997","canto_session_key":"251468d7f8244b76","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2015-03-05 19:29:50","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-03-05 17:33:10","canto_added_date":"2012-02-24 05:53:36","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC4F6.15c"],"gene_count":1,"ltp_gene_count":0,"approved_date":"2015-03-05"},{"uniquename":"PMID:8921872","title":"Cloning and characterization of a cDNA encoding a 3-methyladenine DNA glycosylase from the fission yeast Schizosaccharomyces pombe.","citation":"Gene 1996 Oct 24;177(1-2):229-35","abstract":"We have begun to develop the fission yeast, Schizosaccharomyces pombe, as a eukaryotic model for cellular defenses against alkylating agents. Here we describe the cloning and characterization of a cDNA, designated mag1, encoding a S. pombe 3-methyladenine (3MeA) DNA glycosylase. 3MeA DNA glycosylases in Escherichia coli are encoded by alkA and tag. S. pombe mag1 was cloned by its ability to reverse the alkylation-sensitive phenotype of an alkA tag E. coli double mutant. The expression of S. pombe mag1 in E. coli confers partial resistance to alkylating agents that produce methyl, ethyl and propyl lesions, and Mag1 production produces 3MeA DNA glycosylase activity. In contrast to the E. coli alkA and Saccharomyces cerevisiae MAG genes, expression of S. pombe mag1 was not appreciably induced by alkylating agents. The mag1 cDNA encodes a protein of 228 amino acids (aa) that shares similarity with 3MeA DNA glycosylases from E. coli (AlkA), Bacillus subtilis (BsAlkA) and S. cerevisiae (MAG). A consensus sequence of 9 aa common to these microbial 3MeA DNA glycosylases is discussed.","authors":"Memisoglu A, Samson L","authors_abbrev":"Memisoglu A et al.","pubmed_publication_date":"24 Oct 1996","pubmed_entrez_date":"1996-10-24","publication_year":"1996","canto_session_key":"bb6019bdaa7b1fa6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-09-07 14:29:17","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-08-30 12:08:20","canto_added_date":"2012-02-24 05:53:53","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAPB24D3.04c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2012-08-30"},{"uniquename":"PMID:23649273","title":"Fission yeast leucine-rich repeat protein Lrp1 is essential for cell morphogenesis as a component of the morphogenesis Orb6 network (MOR).","citation":"Biosci Biotechnol Biochem 2013;77(5):1086-91","abstract":"In eukaryotes, cell morphogenesis is regulated coordinately with the cell cycle. In fission yeast, the morphogenesis network MOR (morphogenesis Orb6 network) consists of 5 conserved proteins, Pmo25, Nak1, Mor2, Orb6, and Mob2, and is essential for cell polarity control and cell separation following cytokinesis. Here we show that the conserved leucine-rich repeat protein Lrp1 is required for cell morphogenesis as a newly recognized component of MOR. Lrp1 has 4 leucine-rich repeats in its N-terminus and is a homolog of the budding yeast Sog2, which is a component of the RAM network (regulation of Ace2 activity and cellular morphogenesis). Lrp1 was essential for both cell growth and cell morphogenesis as were the other MOR components. Lrp1 was localized to the SPBs (spindle pole bodies, the yeast equivalent of the animal centrosome) throughout the cell cycle and to the medial ring during cytokinesis. Lrp1 interacted with Nak1 and was important for Orb6 kinase activity. Thus Lrp1 proved to function upstream of Orb6 in cell morphogenesis.","authors":"Kume K, Kubota S, Koyano T, Kanai M, Mizunuma M, Toda T, Hirata D","authors_abbrev":"Kume K et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-05-08","publication_year":"2013","canto_session_key":"59ec05d8416a6e4d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2019-01-30 18:33:09","canto_approved_date":"2026-01-31 15:32:04","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-19 08:21:02","canto_added_date":"2013-05-08 12:17:20","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":47,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC17F3.02","SPBP19A11.04c","SPAC1834.06c","SPAC821.12","SPBC887.09c","SPBC12D12.01","SPCC970.04c"],"gene_count":7,"ltp_gene_count":6,"approved_date":"2019-01-30"},{"uniquename":"PMID:31993556","title":"mTORC1 directly inhibits AMPK to promote cell proliferation under nutrient stress.","citation":"Nat Metab 2020 Jan;2(1):41-49","abstract":"Central to cellular metabolism and cell proliferation are highly conserved signalling pathways controlled by mammalian target of rapamycin (mTOR) and AMP-activated protein kinase (AMPK) 1,2 , dysregulation of which are implicated in pathogenesis of major human diseases such as cancer and type 2 diabetes. AMPK pathways leading to reduced cell proliferation are well established and, in part, act through inhibition of TOR complex-1 (TORC1) activity. Here we demonstrate reciprocal regulation, specifically that TORC1 directly down-regulates AMPK signalling by phosphorylating the evolutionarily conserved residue Ser367 in the fission yeast AMPK catalytic subunit Ssp2, and AMPK α1Ser347/α2Ser345 in the mammalian homologs, which is associated with reduced phosphorylation of activation loop Thr172. Genetic or pharmacological inhibition of TORC1 signalling led to AMPK activation in the absence of increased AMP:ATP ratios; under nutrient stress conditions this was associated with growth limitation in both yeast and human cell cultures. Our findings reveal fundamental, bi-directional regulation between two major metabolic signalling networks and uncover new opportunity for cancer treatment strategies aimed at suppressing cell proliferation in the nutrient-poor tumor microenvironment.","doi":"10.1038/s42255-019-0157-1","authors":"Ling NXY, Kaczmarek A, Hoque A, Davie E, Ngoei KRW, Morrison KR, Smiles WJ, Forte GM, Wang T, Lie S, Dite TA, Langendorf CG, Scott JW, Oakhill JS, Petersen J","authors_abbrev":"Ling NXY et al.","pubmed_publication_date":"Jan 2020","pubmed_entrez_date":"2020-01-30","publication_year":"2020","canto_session_key":"16158f9a42770ce6","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2020-02-19 09:10:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24790093","title":"CDK-dependent phosphorylation of Alp7-Alp14 (TACC-TOG) promotes its nuclear accumulation and spindle microtubule assembly.","citation":"Mol Biol Cell 2014 Jul 01;25(13):1969-82","abstract":"As cells transition from interphase to mitosis, the microtubule cytoskeleton is reorganized to form the mitotic spindle. In the closed mitosis of fission yeast, a microtubule-associated protein complex, Alp7-Alp14 (transforming acidic coiled-coil-tumor overexpressed gene), enters the nucleus upon mitotic entry and promotes spindle formation. However, how the complex is controlled to accumulate in the nucleus only during mitosis remains elusive. Here we demonstrate that Alp7-Alp14 is excluded from the nucleus during interphase using the nuclear export signal in Alp14 but is accumulated in the nucleus during mitosis through phosphorylation of Alp7 by the cyclin-dependent kinase (CDK). Five phosphorylation sites reside around the nuclear localization signal of Alp7, and the phosphodeficient alp7-5A mutant fails to accumulate in the nucleus during mitosis and exhibits partial spindle defects. Thus our results reveal one way that CDK regulates spindle assembly at mitotic entry: CDK phosphorylates the Alp7-Alp14 complex to localize it to the nucleus.","doi":"10.1091/mbc.E13-11-0679","authors":"Okada N, Toda T, Yamamoto M, Sato M","authors_abbrev":"Okada N et al.","pubmed_publication_date":"01 Jul 2014","pubmed_entrez_date":"2014-05-03","publication_year":"2014","canto_session_key":"f134593392c70d97","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Manuel Lera Ramírez","canto_first_approved_date":"2022-06-01 17:57:41","canto_approved_date":"2024-02-27 14:19:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-06-01 17:53:23","canto_added_date":"2014-05-07 04:32:30","annotation_curators":[{"name":"Manuel Lera Ramírez","community_curator":false,"annotation_count":25,"orcid":"0000-0002-8666-9746","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC11B10.09","SPCC962.03c","SPAC890.02c","SPCC895.07"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2022-06-01"},{"uniquename":"PMID:17151242","title":"Sap1 promotes the association of the replication fork protection complex with chromatin and is involved in the replication checkpoint in Schizosaccharomyces pombe.","citation":"Genetics 2007 Feb;175(2):553-66","abstract":"Sap1 is involved in replication fork pausing at rDNA repeats and functions during mating-type switching in Schizosaccharomyces pombe. These two roles are dependent on the ability of Sap1 to bind specific DNA sequences at the rDNA and mating-type loci, respectively. In S. pombe, Swi1 and Swi3 form the replication fork protection complex (FPC) and play important roles in the activation of the replication checkpoint and the stabilization of stalled replication forks. Here we describe the roles of Sap1 in the replication checkpoint. We show that Sap1 is involved in the activation of the replication checkpoint kinase Cds1 and that sap1 mutant cells accumulate spontaneous DNA damage during the S- and G2-phases, which is indicative of fork damage. We also show that sap1 mutants have a defect in the resumption of DNA replication after fork arrest. Sap1 is localized at the replication origin ori2004 and this localization is required for the association of the FPC with chromatin. We propose that Sap1 is required to recruit the FPC to chromatin, thereby contributing to the activation of the replication checkpoint and the stabilization of replication forks.","authors":"Noguchi C, Noguchi E","authors_abbrev":"Noguchi C et al.","pubmed_publication_date":"Feb 2007","pubmed_entrez_date":"2006-12-08","publication_year":"2007","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.06c","SPBC216.05","SPBC19C7.09c","SPBC30D10.04","SPCC1259.13","SPCC1672.02c","SPCC18B5.11c","SPBC3E7.08c"],"gene_count":8,"ltp_gene_count":8},{"uniquename":"PMID:14633985","title":"RNA-binding protein Csx1 mediates global control of gene expression in response to oxidative stress.","citation":"EMBO J 2003 Dec 01;22(23):6256-66","abstract":"Fission yeast Spc1 (Sty1), a stress-activated mitogen-activated protein kinase (MAPK) homologous to human p38, orchestrates global changes in gene expression in response to diverse forms of cytotoxic stress. This control is partly mediated through Atf1, a transcription factor homologous to human ATF2. How Spc1 controls Atf1, and how the cells tailor gene expression patterns to different forms of stress, are unknown. Here we describe Csx1, a novel protein crucial for survival of oxidative but not osmotic stress. Csx1 associates with and stabilizes atf1+ mRNA in response to oxidative stress. Csx1 controls expression of the majority of the genes induced by oxidative stress, including most of the genes regulated by Spc1 and Atf1. These studies reveal a novel mechanism controlling MAPK-regulated transcription factors and suggest how gene expression patterns can be customized to specific forms of stress. Csx1-like proteins in humans may perform similar tasks.","authors":"Rodríguez-Gabriel MA, Burns G, McDonald WH, Martín V, Yates JR, Bähler J, Russell P","authors_abbrev":"Rodríguez-Gabriel MA et al.","pubmed_publication_date":"01 Dec 2003","pubmed_entrez_date":"2003-11-25","publication_year":"2003","canto_session_key":"7c93f34f9f6c11b6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2020-11-12 19:03:21","canto_approved_date":"2020-11-19 21:37:05","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-11-12 19:03:13","canto_added_date":"2012-02-24 05:50:27","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":32,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29B5.01","SPAC1783.07c","SPAC21E11.03c","SPAC8C9.14","SPAC19D5.01","SPAC17A2.09c","SPAC24B11.06c"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2020-11-12"},{"uniquename":"PMID:8233794","title":"Cloning the RAD51 homologue of Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1993 Sep 25;21(19):4586-91","abstract":"The RAD51 gene of Saccharomyces cerevisiae encodes a RecA like protein, which is involved in the recombinational repair of double strand breaks. We have isolated the RAD51 homologue, rhp51+, of the distantly related yeast strain Schizosaccharomyces pombe by heterologous hybridization. DNA sequence analysis of the rhp51+ gene revealed an open reading frame of 365 amino acids. Comparison of the amino acid sequences of RAD51 and rhp51+ showed a high level of conservation: 69% identical amino acids. There are two Mlul sites in the upstream region which may be associated with cell cycle regulation of the rhp51+ gene. The rhp51+ null allele, constructed by disruption of the coding region, is extremely sensitive to X-rays, indicating that the rhp51+ gene, like RAD51, is also involved in the repair of X-ray damage. The structural and functional homology between rhp51+ and RAD51 suggests evolutionary conservation of certain steps in the recombinational repair pathway.","authors":"Muris DF, Vreeken K, Carr AM, Broughton BC, Lehmann AR, Lohman PH, Pastink A","authors_abbrev":"Muris DF et al.","pubmed_publication_date":"25 Sep 1993","pubmed_entrez_date":"1993-09-25","publication_year":"1993","canto_session_key":"345612eef09985cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2013-10-21 14:24:40","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2013-10-21 14:24:32","canto_added_date":"2012-02-24 05:54:45","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":2,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC644.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-10-21"},{"uniquename":"PMID:31927482","title":"Splicing Defects of the Profilin Gene Alter Actin Dynamics in an S. pombe SMN Mutant.","citation":"iScience 2020 Jan 24;23(1):100809","abstract":"Spinal muscular atrophy (SMA) is a devastating motor neuron disorder caused by mutations in the survival motor neuron (SMN) gene. It remains unclear how SMN deficiency leads to the loss of motor neurons. By screening Schizosaccharomyces pombe, we found that the growth defect of an SMN mutant can be alleviated by deletion of the actin-capping protein subunit gene acp1 + . We show that SMN mutated cells have splicing defects in the profilin gene, which thus directly hinder actin cytoskeleton homeostasis including endocytosis and cytokinesis. We conclude that deletion of acp1 +  in an SMN mutant background compensates for actin cytoskeleton alterations by restoring redistribution of actin monomers between different types of cellular actin networks. Our data reveal a direct correlation between an impaired function of SMN in snRNP assembly and defects in actin dynamics. They also point to important common features in the pathogenic mechanism of SMA and ALS.","doi":"10.1016/j.isci.2019.100809","authors":"Antoine M, Patrick KL, Soret J, Duc P, Rage F, Cacciottolo R, Nissen KE, Cauchi RJ, Krogan NJ, Guthrie C, Gachet Y, Bordonné R","authors_abbrev":"Antoine M et al.","pubmed_publication_date":"24 Jan 2020","pubmed_entrez_date":"2020-01-14","publication_year":"2020","canto_session_key":"4471143954453503","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Bordonne","canto_first_approved_date":"2020-09-17 15:25:12","canto_approved_date":"2023-01-26 12:12:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-09-14 13:31:45","canto_added_date":"2020-02-19 09:10:05","annotation_curators":[{"name":"Bordonne","community_curator":true,"annotation_count":1,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1709.11c","SPAC20G4.06c","SPBC26H8.09c","SPAC3C7.10","SPAC1610.01","SPCC1620.11","SPAC12B10.07","SPBC3B8.10c","SPAC4A8.15c","SPAC9G1.10c","SPAC2G11.08c","SPAPYUG7.04c","SPAC23H3.05c","SPAC23C4.02"],"gene_count":14,"ltp_gene_count":11,"approved_date":"2020-09-17"},{"uniquename":"PMID:17632059","title":"The telomere bouquet controls the meiotic spindle.","citation":"Cell 2007 Jul 13;130(1):113-26","abstract":"Bouquet formation, in which telomeres gather to a small region of the nuclear membrane in early meiosis, has been observed in diverse eukaryotes, but the function of the bouquet has remained a mystery. Here, we demonstrate that the telomere bouquet plays a crucial role in controlling the behavior of the fission yeast microtubule-organizing center (known as the spindle pole body or SPB) and the meiotic spindle. Using mutations that specifically disrupt the bouquet, we analyze chromosome, SPB, and spindle dynamics throughout meiosis. If the bouquet fails to form, the SPB becomes fragmented at meiosis I, leading to monopolar, multiple, and mislocalized spindles. Correct SPB and spindle behavior require not only the SPB recruitment of telomere proteins but also that the proteins are properly bound to telomeric DNA. This discovery illuminates an unanticipated level of communication between chromosomes and the spindle apparatus that may be widely conserved among eukaryotes.","authors":"Tomita K, Cooper JP","authors_abbrev":"Tomita K et al.","pubmed_publication_date":"13 Jul 2007","pubmed_entrez_date":"2007-07-17","publication_year":"2007","canto_session_key":"e1f9774a7fd0a539","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-02-22 15:40:12","canto_approved_date":"2022-06-22 16:23:05","canto_approver_orcid":"0000-0002-8666-9746","canto_session_submitted_date":"2018-02-11 15:48:46","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":55,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1093.06c","SPCC1183.05c","SPBC1778.02","SPAC16A10.07c","SPAC17A5.11","SPAC6G9.13c"],"gene_count":6,"ltp_gene_count":6,"approved_date":"2018-02-22"},{"uniquename":"PMID:1637812","title":"A single-stranded DNA exonuclease from Schizosaccharomyces pombe.","citation":"Biochemistry 1992 Jul 28;31(29):6769-73","abstract":"We have purified to near homogeneity a DNA exonuclease from meiotic cells of Schizosaccharomyces pombe. The enzyme, designated exonuclease II (ExoII), had an apparent molecular weight of 134,000 and was abundant in the cell. It specifically degraded single-stranded DNA in the 5'----3' direction with an apparent Km for 5' DNA ends of 3.6 x 10(-11) M and produced 5' deoxynucleoside monophosphates. Its mode of degradation is similar to that of the RecJ protein from Escherichia coli; ExoII may, therefore, be involved in genetic recombination and DNA damage repair.","authors":"Szankasi P, Smith GR","authors_abbrev":"Szankasi P et al.","pubmed_publication_date":"28 Jul 1992","pubmed_entrez_date":"1992-07-28","publication_year":"1992","canto_session_key":"d9f7ca75f057f9b4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2013-01-28 17:30:48","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-01-25 16:52:27","canto_added_date":"2012-02-24 05:55:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.14"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2013-01-25"},{"uniquename":"PMID:33378674","title":"The INO80 Complex Regulates Epigenetic Inheritance of Heterochromatin.","citation":"Cell Rep 2020 Dec 29;33(13):108561","abstract":"One key aspect of epigenetic inheritance is that chromatin structures can be stably inherited through generations after the removal of the signals that establish such structures. In fission yeast, the RNA interference (RNAi) pathway is critical for the targeting of histone methyltransferase Clr4 to pericentric repeats to establish heterochromatin. However, pericentric heterochromatin cannot be properly inherited in the absence of RNAi, suggesting the existence of mechanisms that counteract chromatin structure inheritance. Here, we show that mutations of components of the INO80 chromatin-remodeling complex allow pericentric heterochromatin inheritance in RNAi mutants. The ability of INO80 to counter heterochromatin inheritance is attributed to one subunit, Iec5, which promotes histone turnover at heterochromatin but has little effects on nucleosome positioning at heterochromatin, gene expression, or the DNA damage response. These analyses demonstrate the importance of the INO80 chromatin-remodeling complex in controlling heterochromatin inheritance and maintaining the proper heterochromatin landscape of the genome.","doi":"10.1016/j.celrep.2020.108561","authors":"Shan CM, Bao K, Diedrich J, Chen X, Lu C, Yates JR, Jia S","authors_abbrev":"Shan CM et al.","pubmed_publication_date":"29 Dec 2020","pubmed_entrez_date":"2020-12-30","publication_year":"2020","canto_session_key":"5bba706f5b371433","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Chunmin Shan","canto_first_approved_date":"2021-08-03 12:51:52","canto_approved_date":"2024-03-24 07:37:14","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-07-19 21:34:38","canto_added_date":"2021-01-02 01:15:04","annotation_curators":[{"name":"Chunmin Shan","community_curator":true,"annotation_count":118,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":29,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB8E5.09","SPAC18G6.02c","SPAC664.02c","SPBC16C6.10","SPBC32H8.12c","SPCC16C4.20c","SPAC29B12.01","SPAC10F6.08c","SPAC6B12.05c","SPBC83.08","SPAC144.02","SPBC428.08c","SPCC188.13c","SPAC664.01c","SPAC11E3.01c","SPCC736.11","SPCC1259.04","SPAC222.04c","SPBP23A10.08","SPCC11E10.08","SPBC800.03","SPBP35G2.10","SPBC365.10","SPAC6F12.09","SPAC22H12.02","SPAPB1E7.14","SPAC140.03","SPAC23G3.04"],"gene_count":28,"ltp_gene_count":28,"approved_date":"2021-08-03"},{"uniquename":"PMID:33855304","title":"A protocol for transposon insertion sequencing in  Schizosaccharomyces pombe  to identify factors that maintain heterochromatin.","citation":"STAR Protoc 2021 Jun 18;2(2):100392","abstract":"Transposon insertion sequencing (TIS) is a highly effective method used with bacteria to identify genes important for growth in any condition of interest. Previously, we adapted this method to identify essential genes of the yeast  Schizosaccharomyces pombe . Here, we describe modifications used to identify genes necessary for the formation of centromeric heterochromatin. For complete details on the use and execution of this protocol, please refer to Lee et al. (2020).","doi":"10.1016/j.xpro.2021.100392","authors":"Li F, Hung S, Esnault C, Levin HL","authors_abbrev":"Li F et al.","pubmed_publication_date":"18 Jun 2021","pubmed_entrez_date":"2021-04-15","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-04-19 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18071249","title":"Identification of a fatty acyl-CoA synthetase gene, lcf2+, which affects viability after entry into the stationary phase in Schizosaccharomyces pombe.","citation":"Biosci Biotechnol Biochem 2007 Dec;71(12):3041-7","abstract":"The lcf1(+) gene, which encodes a long chain fatty acyl-CoA synthetase, is necessary for the maintenance of viability after entry into the stationary phase in Schizosaccharomyces pombe. In this study, we analyzed a paralogous gene, SPBP4H10.11c (named lcf2(+)), and we present evidence that the gene encodes a new fatty acyl-CoA synthetase. The enzyme preferentially recognized myristic acid as a substrate. A Deltalcf2 mutant showed increased viability after entry into the stationary phase in SD medium. A Deltalcf1Deltalcf2 double mutant showed a severe decrease in long-chain fatty acyl-CoA synthetase activity and a rapid loss of viability after entry into the stationary phase. These results suggest that fatty acid utilization and/or metabolism is important to determine viability in the stationary phase.","authors":"Fujita Y, Mita S, Ohtsuka H, Aiba H","authors_abbrev":"Fujita Y et al.","pubmed_publication_date":"Dec 2007","pubmed_entrez_date":"2007-12-12","publication_year":"2007","canto_session_key":"5bff0cacfd0d068a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_approved_date":"2016-08-03 07:52:05","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-08-16 07:18:01","canto_added_date":"2012-02-24 05:48:34","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC18H10.02","SPBP4H10.11c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2012-08-16"},{"uniquename":"EMBL:AU006700","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24278707","title":"Finding the correct partner: the meiotic courtship.","citation":"Scientifica (Cairo) 2012;2012:509073","abstract":"Homologous chromosomes are usually separated at the entrance of meiosis; how they become paired is one of the outstanding mysteries of the meiotic process. Reduction of spacing between homologues makes possible the occurrence of chromosomal interactions leading to homology detection and the formation of bivalents. In many organisms, telomere-led chromosome movements are generated that bring homologues together. Additional movements produced by chromatin conformational changes at early meiosis may also facilitate homologous contacts. Organisms used in the study of meiosis show a surprising variety of strategies for homology detection. In dipterans, homologous chromosomes remain paired throughout most of development. Pairing seems to arise as a balance between promoter and suppressor pairing genes. Some fungi, plants and animals, use mechanisms based on recombinational interactions. Other mechanisms leading to homology search are recombination-independent and require specialized pairing sites. In the worm Caenorhabditis elegans, each chromosome carries a pairing center consisting of a chromosome-specific DNA-protein complex, and in the fission yeast Schizosaccharomyces pombe, the sme2 locus encodes a meiosis-specific non-coding RNA that mediates on homologous recognition. In addition, mismatch correction plays a relevant role, especially in polyploids, which evolved genetic systems that suppress pairing between non-homologous related (homoeologus) chromosomes.","doi":"10.6064/2012/509073","authors":"Naranjo T","authors_abbrev":"Naranjo T","pubmed_publication_date":"2012","pubmed_entrez_date":"2013-11-27","publication_year":"2012","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:48:36","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25723815","title":"Neutral space analysis for a Boolean network model of the fission yeast cell cycle network.","citation":"Biol Res 2014 Nov 25;47(1):64","abstract":"Interactions between genes and their products give rise to complex circuits known as gene regulatory networks (GRN) that enable cells to process information and respond to external stimuli. Several important processes for life, depend of an accurate and context-specific regulation of gene expression, such as the cell cycle, which can be analyzed through its GRN, where deregulation can lead to cancer in animals or a directed regulation could be applied for biotechnological processes using yeast. An approach to study the robustness of GRN is through the neutral space. In this paper, we explore the neutral space of a Schizosaccharomyces pombe (fission yeast) cell cycle network through an evolution strategy to generate a neutral graph, composed of Boolean regulatory networks that share the same state sequences of the fission yeast cell cycle.\nThrough simulations it was found that in the generated neutral graph, the functional networks that are not in the wildtype connected component have in general a Hamming distance more than 3 with the wildtype, and more than 10 between the other disconnected functional networks. Significant differences were found between the functional networks in the connected component of the wildtype network and the rest of the network, not only at a topological level, but also at the state space level, where significant differences in the distribution of the basin of attraction for the G1 fixed point was found for deterministic updating schemes.\nIn general, functional networks in the wildtype network connected component, can mutate up to no more than 3 times, then they reach a point of no return where the networks leave the connected component of the wildtype. The proposed method to construct a neutral graph is general and can be used to explore the neutral space of other biologically interesting networks, and also formulate new biological hypotheses studying the functional networks in the wildtype network connected component.","doi":"10.1186/0717-6287-47-64","authors":"Ruz GA, Timmermann T, Barrera J, Goles E","authors_abbrev":"Ruz GA et al.","pubmed_publication_date":"25 Nov 2014","pubmed_entrez_date":"2015-02-28","publication_year":"2014","canto_triage_status":"Modelling","canto_curator_role":"PomBase","canto_added_date":"2015-03-01 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:528974","title":"Germination and outgrowth of Schizosaccharomyces pombe spores isolated by a simple batch centrifugation technique.","citation":"J Gen Microbiol 1979 Nov;115(1):255-8","abstract":"Spores of the fission yeast Schizosaccharomyces pombe have been separated from vegetative cells by a simple and rapid centrifugation (800 g for 20 min) through a 35% Hypaque solution to a purity greater than 95%. Approximately 35% of the spores were recovered. Regrowth in EMM2 plus glucose showed that over 97% of the spores germinated within the first 2 h and outgrowth continued between 5 and 10 h. Sucrose induced germination in greater than 95% of the spores with a 1 h delay and outgrowth in 50% of the spores with a 3 h delay. There was little protein synthesis during germination but the protein content increased linearly coincident with outgrowth. The RNA content increased slightly during germination, but increased linearly 1 h before the onset of outgrowth and protein synthesis. After 8 h of regrowth, coincident with the onset of DNA synthesis, the rate of RNA synthesis was accelerated. The DNA content had increased 1.7-fold after 10 h of regrowth from a haploid level of 1.36 x 10(-8) microgram spore-1.","authors":"Johnke R, Padilla GM","authors_abbrev":"Johnke R et al.","pubmed_publication_date":"Nov 1979","pubmed_entrez_date":"1979-11-01","publication_year":"1979","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8643378","title":"The evolutionary conservation of the splicing apparatus between fission yeast and man.","citation":"Nucleic Acids Symp Ser 1995;(33):226-8","abstract":"The removal of intervening sequences from pre-mRNA is an important step in gene regulation. Pre-mRNA processing takes place within the spliceosome, a dynamic structure composed of small nuclear RNA (snRNA) and proteins. The function of the spliceosome is currently being studied in many eukaryotic systems including mammal and yeast. Here we review pre-mRNA splicing in fission yeast and man and propose that spliceosomal structure and function has been evolutionarily conserved between the two organisms.","authors":"Wentz-Hunter K, Potashkin J","authors_abbrev":"Wentz-Hunter K et al.","pubmed_publication_date":"1995","pubmed_entrez_date":"1995-01-01","publication_year":"1995","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:8529460","title":"Microtubule-driven nuclear movements and linear elements as meiosis-specific characteristics of the fission yeasts Schizosaccharomyces versatilis and Schizosaccharomyces pombe.","citation":"Chromosoma 1995 Nov;104(3):203-14","abstract":"Meiotic prophase in Schizosaccharomyces pombe is characterized by striking nuclear movements and the formation of linear elements along chromosomes instead of tripartite synaptonemal complexes. We analysed the organization of nuclei and microtubules in cells of fission yeasts undergoing sexual differentiation. S. japonicus var. versatilis and S. pombe cells were studied in parallel, taking advantage of the better cytology in S. versatilis. During conjugation, microtubules were directed towards the mating projection. These microtubules seem to lead the haploid nuclei together in the zygote by interaction with the spindle pole bodies at the nuclear periphery. After karyogamy, arrays of microtubules emanating from the spindle pole body of the diploid nucleus extended to both cell poles. The same differentiated microtubule configuration was elaborated upon induction of azygotic meiosis in S. pombe. The cyclic movements of the elongated nuclei between the cell poles is reflected by a dynamic and coordinated shortening and lengthening of the two microtubule arrays. When the nucleus was at a cell end, one array was short while the other bridged the whole cell length. Experiments with inhibitors showed that microtubules are required for karyogamy and for the elongated shape and movement of nuclei during meiotic prophase. In both fission yeasts the SPBs and nucleoli are at the leading ends of the moving nuclei. Astral and cytoplasmic microtubules were also prominent during meiotic divisions and sporulation. We further show that in S. versatilis the linear elements formed during meiotic prophase are similar to those in S. pombe. Tripartite synaptonemal complexes were never detected. Taken together, these findings suggest that S. pombe and S. versatilis share basic characteristics in the organization of microtubules and the structure and behaviour of nuclei during their meiotic cell cycle. The prominent differentiations of microtubules and nuclei may be involved in the pairing, recombination, and segregation of meiotic chromosomes.","authors":"Svoboda A, Bähler J, Kohli J","authors_abbrev":"Svoboda A et al.","pubmed_publication_date":"Nov 1995","pubmed_entrez_date":"1995-11-01","publication_year":"1995","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:31294800","title":"Distinct RNA-binding modules in a single PUF protein cooperate to determine RNA specificity.","citation":"Nucleic Acids Res 2019 Sep 19;47(16):8770-8784","abstract":"PUF proteins, named for Drosophila Pumilio (PUM) and Caenorhabditis elegans fem-3-binding factor (FBF), recognize specific sequences in the mRNAs they bind and control. RNA binding by classical PUF proteins is mediated by a characteristic PUM homology domain (PUM-HD). The Puf1 and Puf2 proteins possess a distinct architecture and comprise a highly conserved subfamily among fungal species. Puf1/Puf2 proteins contain two types of RNA-binding domain: a divergent PUM-HD and an RNA recognition motif (RRM). They recognize RNAs containing UAAU motifs, often in clusters. Here, we report a crystal structure of the PUM-HD of a fungal Puf1 in complex with a dual UAAU motif RNA. Each of the two UAAU tetranucleotides are bound by a Puf1 PUM-HD forming a 2:1 protein-to-RNA complex. We also determined crystal structures of the Puf1 RRM domain that identified a dimerization interface. The PUM-HD and RRM domains act in concert to determine RNA-binding specificity: the PUM-HD dictates binding to UAAU, and dimerization of the RRM domain favors binding to dual UAAU motifs rather than a single UAAU. Cooperative action of the RRM and PUM-HD identifies a new mechanism by which multiple RNA-binding modules in a single protein collaborate to create a unique RNA-binding specificity.","doi":"10.1093/nar/gkz583","authors":"Qiu C, Dutcher RC, Porter DF, Arava Y, Wickens M, Hall TMT","authors_abbrev":"Qiu C et al.","pubmed_publication_date":"19 Sep 2019","pubmed_entrez_date":"2019-07-12","publication_year":"2019","canto_session_key":"18bc2c41ccf91f5a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2019-12-13 15:28:49","canto_approved_date":"2019-12-13 15:28:49","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-12-13 15:28:41","canto_added_date":"2019-12-05 01:15:04","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC56F2.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2019-12-13","pdb_entries":[{"pdb_id":"6nww","gene_chains":[{"gene_uniquename":"SPBC56F2.08c","chain":"A/B/C/D","position":"1-79"}],"title":"Crystal structure of the RRM domain of S. pombe Puf1 in the P212121 space group","entry_authors":"Qiu C,Hall TMT","entry_authors_abbrev":"Qiu C et al.","reference_uniquename":"PMID:31294800","experimental_method":"X-ray","resolution":"2.06"},{"pdb_id":"6ny5","gene_chains":[{"gene_uniquename":"SPBC56F2.08c","chain":"A/B","position":"109-485"}],"title":"Crystal structure of the PUM-HD domain of S. pombe Puf1 in complex with RNA","entry_authors":"Qiu C,Hall TMT","entry_authors_abbrev":"Qiu C et al.","reference_uniquename":"PMID:31294800","experimental_method":"X-ray","resolution":"3.002"},{"pdb_id":"6nx5","gene_chains":[{"gene_uniquename":"SPBC56F2.08c","chain":"A/B/C/D","position":"1-79"}],"title":"Crystal structure of the RRM domain of S. pombe Puf1 in the P21 space group","entry_authors":"Qiu C,Hall TMT","entry_authors_abbrev":"Qiu C et al.","reference_uniquename":"PMID:31294800","experimental_method":"X-ray","resolution":"1.554"}]},{"uniquename":"PMID:29727687","title":"Variants in EXOSC9 Disrupt the RNA Exosome and Result in Cerebellar Atrophy with Spinal Motor Neuronopathy.","citation":"Am J Hum Genet 2018 May 03;102(5):858-873","abstract":"The exosome is a conserved multi-protein complex that is essential for correct RNA processing. Recessive variants in exosome components EXOSC3, EXOSC8, and RBM7 cause various constellations of pontocerebellar hypoplasia (PCH), spinal muscular atrophy (SMA), and central nervous system demyelination. Here, we report on four unrelated affected individuals with recessive variants in EXOSC9 and the effect of the variants on the function of the RNA exosome in vitro in affected individuals' fibroblasts and skeletal muscle and in vivo in zebrafish. The clinical presentation was severe, early-onset, progressive SMA-like motor neuronopathy, cerebellar atrophy, and in one affected individual, congenital fractures of the long bones. Three affected individuals of different ethnicity carried the homozygous c.41T>C (p.Leu14Pro) variant, whereas one affected individual was compound heterozygous for c.41T>C (p.Leu14Pro) and c.481C>T (p.Arg161 ∗ ). We detected reduced EXOSC9 in fibroblasts and skeletal muscle and observed a reduction of the whole multi-subunit exosome complex on blue-native polyacrylamide gel electrophoresis. RNA sequencing of fibroblasts and skeletal muscle detected significant >2-fold changes in genes involved in neuronal development and cerebellar and motor neuron degeneration, demonstrating the widespread effect of the variants. Morpholino oligonucleotide knockdown and CRISPR/Cas9-mediated mutagenesis of exosc9 in zebrafish recapitulated aspects of the human phenotype, as they have in other zebrafish models of exosomal disease. Specifically, portions of the cerebellum and hindbrain were absent, and motor neurons failed to develop and migrate properly. In summary, we show that variants in EXOSC9 result in a neurological syndrome combining cerebellar atrophy and spinal motoneuronopathy, thus expanding the list of human exosomopathies.","doi":"10.1016/j.ajhg.2018.03.011","authors":"Burns DT, Donkervoort S, Müller JS, Knierim E, Bharucha-Goebel D, Faqeih EA, Bell SK, AlFaifi AY, Monies D, Millan F, Retterer K, Dyack S, MacKay S, Morales-Gonzalez S, Giunta M, Munro B, Hudson G, Scavina M, Baker L, Massini TC, Lek M, Hu Y, Ezzo D, AlKuraya FS, Kang PB, Griffin H, Foley AR, Schuelke M, Horvath R, Bönnemann CG","authors_abbrev":"Burns DT et al.","pubmed_publication_date":"03 May 2018","pubmed_entrez_date":"2018-05-05","publication_year":"2018","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC17D1.03c","SPCC757.08","SPAC22A12.12c"],"gene_count":3,"ltp_gene_count":0},{"uniquename":"PMID:20008937","title":"Nearby inverted repeats fuse to generate acentric and dicentric palindromic chromosomes by a replication template exchange mechanism.","citation":"Genes Dev 2009 Dec 15;23(24):2876-86","abstract":"Gene amplification plays important roles in the progression of cancer and contributes to acquired drug resistance during treatment. Amplification can initiate via dicentric palindromic chromosome production and subsequent breakage-fusion-bridge cycles. Here we show that, in fission yeast, acentric and dicentric palindromic chromosomes form by homologous recombination protein-dependent fusion of nearby inverted repeats, and that these fusions occur frequently when replication forks arrest within the inverted repeats. Genetic and molecular analyses suggest that these acentric and dicentric palindromic chromosomes arise not by previously described mechanisms, but by a replication template exchange mechanism that does not involve a DNA double-strand break. We thus propose an alternative mechanism for the generation of palindromic chromosomes dependent on replication fork arrest at closely spaced inverted repeats.","doi":"10.1101/gad.1863009","authors":"Mizuno K, Lambert S, Baldacci G, Murray JM, Carr AM","authors_abbrev":"Mizuno K et al.","pubmed_publication_date":"15 Dec 2009","pubmed_entrez_date":"2009-12-17","publication_year":"2009","canto_triage_status":"Other","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24184848","title":"Yeast PPR proteins, watchdogs of mitochondrial gene expression.","citation":"RNA Biol 2013;10(9):1477-94","abstract":"PPR proteins are a family of ubiquitous RNA-binding factors, found in all the Eukaryotic lineages, and are particularly numerous in higher plants. According to recent bioinformatic analyses, yeast genomes encode from 10 (in S. pombe) to 15 (in S. cerevisiae) PPR proteins. All of these proteins are mitochondrial and very often interact with the mitochondrial membrane. Apart from the general factors, RNA polymerase and RNase P, most yeast PPR proteins are involved in the stability and/or translation of mitochondrially encoded RNAs. At present, some information concerning the target RNA(s) of most of these proteins is available, the next challenge will be to refine our understanding of the function of the proteins and to resolve the yeast PPR-RNA-binding code, which might differ significantly from the plant PPR code.","doi":"10.4161/rna.25392","authors":"Herbert CJ, Golik P, Bonnefoy N","authors_abbrev":"Herbert CJ et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-11-05","publication_year":"2013","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23385477","title":"Display of active beta-glucosidase on the surface of Schizosaccharomyces pombe cells using novel anchor proteins.","citation":"Appl Microbiol Biotechnol 2013 May;97(10):4343-52","abstract":"Here, we demonstrate display of beta-glucosidase (BGL) on the surface of Schizosaccharomyces pombe cells using novel anchor proteins. A total of four candidate anchor proteins (SPBC21D10.06c, SPBC947.04, SPBC19C7.05, and SPBC359.04c) were selected from among almost all of S. pombe membrane proteins. The C-terminus of each anchor protein was genetically fused to the N-terminus of BGL, and the fusion protein was expressed using S. pombe as a host. The highest cell surface-associated BGL activity (107 U/10(5) cells was achieved with SPBC359.04c serving as the anchor, followed by SPBC947.04 (44 U/10(5) cells) and SPBC21D10.06c (38 U/10(5) cells). S. pombe displaying BGL with SPBC359.04c as an anchor showed the highest growth on 2 % cellobiose (10.7 × 10(7) cells/mL after 41 h of cultivation from an initial density of 0.1 × 10(7) cells/mL). Additionally, culturing BGL-displaying S. pombe in medium containing cellobiose as the sole carbon source did not affect protein expression, and ethanol fermentation from cellobiose was successfully demonstrated using BGL-displaying S. pombe. This is the first report describing a cell surface display system for the functionalization of S. pombe.","doi":"10.1007/s00253-013-4733-0","authors":"Tanaka T, Matsumoto S, Yamada M, Yamada R, Matsuda F, Kondo A","authors_abbrev":"Tanaka T et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-02-07","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:390094","title":"Microbial determinations by flow cytometry.","citation":"J Gen Microbiol 1979 Aug;113(2):369-75","abstract":"Recent improvements in the optics and electronics of flow cytometry systems, as well as in staining techniques, permit the assay of such minute cellular constituents as the DNA and protein contents of micro-organisms. To assess the usefulness of this technique, DNA and protein content distributions were determined in Escherichia coli, Lactobacillus brevis, Lactobacillus casei, Chlorella kessleri 8k, Saccharomyces cerevisiae, Candida utilis, Schizosaccharomyces pombe and Euglena gracilis. Investigations of the DNA content distributions of polyploid strains of Saccharomyces cerevisiae indicated that the method can be used to determine ploidy. The rapidity of flow cytometry measurements allows accurate determinations in large populations.","authors":"Hutter KJ, Eipel HE","authors_abbrev":"Hutter KJ et al.","pubmed_publication_date":"Aug 1979","pubmed_entrez_date":"1979-08-01","publication_year":"1979","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:02","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:12805771","title":"Ensuring the stability of the genome: DNA damage checkpoints.","citation":"ScientificWorldJournal 2001 Nov 20;1:684-702","abstract":"The cellular response to DNA damage is vital for the cell\"s ability to maintain genomic integrity. Checkpoint signalling pathways, which induce a cell cycle arrest in response to DNA damage, are an essential component of this process. This is reflected by the functional conservation of these pathways in all eukaryotes from yeast to mammalian cells. This review will examine the cellular response to DNA damage throughout the cell cycle. A key component of the DNA damage response is checkpoint signalling, which monitors the state of the genome prior to DNA replication (G1/S) and chromosome segregation (G2/M). Checkpoint signalling in model systems including mice, Xenopus laevis, Drosophila melanogaster, and the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe have been useful in elucidating these pathways in mammalian cells. An examination of this research, with emphasis on the function of checkpoint proteins, their relationship to DNA repair, and their involvement in oncogenesis is undertaken here.","authors":"Latif C, Harvey SH, O'Connell MJ","authors_abbrev":"Latif C et al.","pubmed_publication_date":"20 Nov 2001","pubmed_entrez_date":"2003-06-14","publication_year":"2001","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9781677","title":"phd1+, a histone deacetylase gene of Schizosaccharomyces pombe, is required for the meiotic cell cycle and resistance to trichostatin A.","citation":"FEBS Lett 1998 Oct 02;436(2):193-6","abstract":"A gene named phd1+ encoding a protein highly homologous to the yeast and human histone deacetylases, such as Saccharomyces cerevisiae Rpd3p and human HDAC1, was cloned from Schizosaccharomyces pombe. The immune complex isolated from S. pombe cells expressing Phd1 fused to the FLAG epitope showed histone deacetylase activity, which was inhibited by trichostatin A (TSA), a specific inhibitor of histone deacetylase. The null mutation of phd1+ resulted in a marked decrease in the total cellular histone deacetylase activity and an increase in the sensitivity to TSA. Although the phd1 disruptant showed no obvious defect in the mitotic cell cycle or mating, both homothallic haploid and heterothallic diploid cells failed to form spores in the absence of phd1+. These results indicate that phd1+ encodes a histone deacetylase, which is involved in the meiotic cell cycle in S. pombe.","authors":"Kim YB, Honda A, Yoshida M, Horinouchi S","authors_abbrev":"Kim YB et al.","pubmed_publication_date":"02 Oct 1998","pubmed_entrez_date":"1998-10-22","publication_year":"1998","canto_session_key":"a5decd25e556c51f","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2014-08-20 09:09:26","canto_approved_date":"2020-01-17 19:42:21","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-08-20 09:09:16","canto_added_date":"2012-02-24 05:53:02","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":17,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3G9.07c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2014-08-20"},{"uniquename":"Treefam:TF300364","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":["HGNC:2745","SPCC1795.11","HGNC:18700","HGNC:2699"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"EMBL:SPD119","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10547374","title":"Fission yeast Msp1 is a mitochondrial dynamin-related protein.","citation":"J Cell Sci 1999 Nov;112 ( Pt 22):4151-61","abstract":"We recently identified Msp1p, a fission yeast Schizosaccharomyces pombe dynamin-related protein, which is essential for the maintenance of mitochondrial DNA. The Msp1p sequence displays typical features of a mitochondrial protein. Here we report in vitro and in vivo data that validate that prediction. We demonstrate that the targeting sequence of Msp1p is processed by recombinant mitochondrial processing peptidase and that Msp1p is imported into S. pombe mitochondria in vitro in the presence of cellular extracts. We show that the first 109 residues of Msp1p encompass a functional peptide signal that is sufficient to direct chimera to mitochondria. Immunofluorescence studies indicate that Msp1p staining colocalises with a mitochondrial marker and electron microscopy shows that the protein is located inside the mitochondria. Mitochondrial enrichment and fractionation further confirm that localisation and show that Msp1p is anchored to the matrix side of the mitochondrial inner membrane. Finally, we report that overexpression of the Msp1 protein results in gross alteration of the mitochondrial structure and function. All together our results suggest that Msp1p is an essential component for mitochondrial maintenance.","authors":"Pelloquin L, Belenguer P, Menon Y, Gas N, Ducommun B","authors_abbrev":"Pelloquin L et al.","pubmed_publication_date":"Nov 1999","pubmed_entrez_date":"1999-11-05","publication_year":"1999","canto_session_key":"bdca21fb107b963e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2015-01-24 10:52:31","canto_approved_date":"2023-08-17 21:27:45","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-10-20 14:10:28","canto_added_date":"2012-02-24 05:52:38","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1718.06"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2015-01-24"},{"uniquename":"PMID:25409521","title":"Real-time imaging of DNA damage in yeast cells using ultra-short near-infrared pulsed laser irradiation.","citation":"PLoS One 2014;9(11):e113325","abstract":"Analysis of accumulation of repair and checkpoint proteins at repair sites in yeast nuclei has conventionally used chemical agents, ionizing radiation or induction of endonucleases to inflict localized damage. In addition to these methods, similar studies in mammalian cells have used laser irradiation, which has the advantage that damage is inflicted at a specific nuclear region and at a precise time, and this allows accurate kinetic analysis of protein accumulation at DNA damage sites. We show here that it is feasible to use short pulses of near-infrared laser irradiation to inflict DNA damage in subnuclear regions of yeast nuclei by multiphoton absorption. In conjunction with use of fluorescently-tagged proteins, this allows quantitative analysis of protein accumulation at damage sites within seconds of damage induction. PCNA accumulated at damage sites rapidly, such that maximum accumulation was seen approximately 50 s after damage, then levels declined linearly over 200-1000 s after irradiation. RPA accumulated with slower kinetics such that hardly any accumulation was detected within 60 s of irradiation, and levels subsequently increased linearly over the next 900 s, after which levels were approximately constant (up to ca. 2700 s) at the damage site. This approach complements existing methodologies to allow analysis of key damage sensors and chromatin modification changes occurring within seconds of damage inception.","doi":"10.1371/journal.pone.0113325","authors":"Guarino E, Cojoc G, García-Ulloa A, Tolić IM, Kearsey SE","authors_abbrev":"Guarino E et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-11-20","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2015-12-16 01:26:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:AU012440","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:20176980","title":"Fission yeast Hsk1 (Cdc7) kinase is required after replication initiation for induced mutagenesis and proper response to DNA alkylation damage.","citation":"Genetics 2010 May;185(1):39-53","abstract":"Genome stability in fission yeast requires the conserved S-phase kinase Hsk1 (Cdc7) and its partner Dfp1 (Dbf4). In addition to their established function in the initiation of DNA replication, we show that these proteins are important in maintaining genome integrity later in S phase and G2. hsk1 cells suffer increased rates of mitotic recombination and require recombination proteins for survival. Both hsk1 and dfp1 mutants are acutely sensitive to alkylation damage yet defective in induced mutagenesis. Hsk1 and Dfp1 are associated with the chromatin even after S phase, and normal response to MMS damage correlates with the maintenance of intact Dfp1 on chromatin. A screen for MMS-sensitive mutants identified a novel truncation allele, rad35 (dfp1-(1-519)), as well as alleles of other damage-associated genes. Although Hsk1-Dfp1 functions with the Swi1-Swi3 fork protection complex, it also acts independently of the FPC to promote DNA repair. We conclude that Hsk1-Dfp1 kinase functions post-initiation to maintain replication fork stability, an activity potentially mediated by the C terminus of Dfp1.","doi":"10.1534/genetics.109.112284","authors":"Dolan WP, Le AH, Schmidt H, Yuan JP, Green M, Forsburg SL","authors_abbrev":"Dolan WP et al.","pubmed_publication_date":"May 2010","pubmed_entrez_date":"2010-02-24","publication_year":"2010","canto_session_key":"b805bb92a7efc107","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC1952.07","SPCC550.13","SPBC16A3.11","SPAC2G11.12","SPAC664.01c","SPBC725.13c","SPAC11E3.04c","SPBC776.12c","SPBC30D10.04","SPBC342.05","SPAC688.10","SPBC16D10.09","SPBC4.04c","SPBC216.06c","SPAC644.14c","SPAC14C4.13","SPCC338.05c","SPCC338.17c","SPAC4H3.05","SPCC18B5.11c","SPBC1734.06","SPAC694.06c"],"gene_count":22,"ltp_gene_count":22},{"uniquename":"PMID:11071923","title":"Fission yeast Int6 is not essential for global translation initiation, but deletion of int6(+) causes hypersensitivity to caffeine and affects spore formation.","citation":"Mol Biol Cell 2000 Nov;11(11):4005-18","abstract":"Mammalian INT6 protein has been considered to be a subunit of the eukaryotic translation initiation factor, eIF3. The Int6 locus is also known as a common integration site of mouse mammary tumor virus (MMTV). However, the function of Int6 in translation initiation and the mechanism of Int6-mediated tumor induction are yet to be explored. In this study, the fission yeast, Schizosaccharomyces pombe, int6(+), which is 43% identical to the mammalian counterpart, was deleted. Despite the evidence that the majority of Int6 protein was associated with 40S particles in this organism, strains lacking int6(+) (Deltaint6) were viable and showed only moderate inhibition in the rate of in vivo global protein synthesis. Polysome profile analysis showed no apparent defects in translation initiation. Deltaint6 exhibited a hypersensitivity to caffeine, which could be suppressed by the addition of sorbitol to the growth medium. This and other phenotypes would imply that int6(+) is required for the integrity of cell membrane. In meiosis, Deltaint6 produced incomplete tetrads frequently. High dosage expression of a truncated mutant of int6(+) conferred a hypersensitivity to caffeine, but did not cause the defect in meiosis. A possible link between the function of int6(+) and the Deltaint6-phenotypes is discussed.","authors":"Bandyopadhyay A, Matsumoto T, Maitra U","authors_abbrev":"Bandyopadhyay A et al.","pubmed_publication_date":"Nov 2000","pubmed_entrez_date":"2000-11-10","publication_year":"2000","canto_session_key":"6a65148752d79293","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-17 15:05:02","canto_approved_date":"2020-09-04 15:24:19","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2012-11-30 16:36:55","canto_added_date":"2012-02-24 05:52:00","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":16,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC646.09c","SPBC119.08"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2017-03-17"},{"uniquename":"PMID:20356456","title":"Distinct functional roles of peroxiredoxin isozymes and glutathione peroxidase from fission yeast, Schizosaccharomyces pombe.","citation":"BMB Rep 2010 Mar;43(3):170-5","abstract":"To investigate the differences in the functional roles of peroxiredoxins (Prxs) and glutathione peroxidase (GPx) of Schizosaccharomyces pombe, we examined the peroxidase and molecular chaperone properties of the recombinant proteins. TPx (thioredoxin peroxidase) exhibited a capacity for peroxide reduction with the thioredoxin system. GPx also showed thioreoxin-dependent peroxidase activity rather than GPx activity. The peroxidase activity of BCP (bacterioferritin comigratory protein) was similar to that of TPx. However, peroxidase activity was not observed for PMP20 (peroxisomal membrane protein 20). TPx, PMP20, and GPx inhibited thermal aggregation of citrate synthase at 43(o)C, but BCP failed to inhibit the aggregation. The chaperone activities of PMP20 and GPx were weaker than that of TPx. The peroxidase and chaperone properties of TPx, BCP, and GPx of the fission yeast are similar to those of Saccharomyces cerevisiae. The fission yeast PMP20 without thioredoxin-dependent peroxidase activity may act as a molecular chaperone.","authors":"Kim JS, Bang MA, Lee S, Chae HZ, Kim K","authors_abbrev":"Kim JS et al.","pubmed_publication_date":"Mar 2010","pubmed_entrez_date":"2010-04-02","publication_year":"2010","canto_session_key":"ec98ab47f2b47ef1","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-10-14 01:13:59","canto_approved_date":"2026-03-23 18:44:13","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-14 01:10:09","canto_added_date":"2012-02-24 05:47:31","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":2,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC1773.02c","SPBC32F12.03c","SPCC330.06c","SPCC576.03c"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2015-10-14"},{"uniquename":"PMID:16950131","title":"Phospho-regulation of the Cdc14/Clp1 phosphatase delays late mitotic events in S. pombe.","citation":"Dev Cell 2006 Sep;11(3):423-30","abstract":"In eukaryotes, exit from mitosis occurs through the inactivation of the Cdk1-cyclin B kinase complex and the reversal of its phosphorylation events. These late mitotic events are tightly regulated to occur only after the onset of anaphase and prior to cytokinesis. Central to this regulation is the conserved Cdc14 family of protein phosphatases, whose activity reverses Cdk-dependent phosphorylation events. S. cerevisiae Cdc14 activity is restrained from dephosphorylating Cdk substrates and inactivating Cdk1 through its nucleolar sequestration prior to anaphase. Here, we describe a unique mode of Cdc14 regulation that operates prior to anaphase in fission yeast. Cdk1 phosphorylates and inhibits the catalytic activity of the Cdc14 family member, Clp1/Flp1. As Cdk1 activity declines during anaphase progression, Clp1/Flp1 autocatalytically reverses these phosphorylation events to stimulate its own activity. These findings point to a simple regulatory circuit that couples Cdk1 activation with its inactivation mediated through phosphorylation-dependent regulation of Clp1/Flp1 phosphatase activity.","authors":"Wolfe BA, McDonald WH, Yates JR, Gould KL","authors_abbrev":"Wolfe BA et al.","pubmed_publication_date":"Sep 2006","pubmed_entrez_date":"2006-09-05","publication_year":"2006","canto_session_key":"3472d1b25692f40c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-02-26 11:38:06","canto_approved_date":"2022-07-27 15:18:23","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-02-26 11:37:21","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":14,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1782.09c","SPBC11B10.09","SPBC26H8.07c","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2017-02-26"},{"uniquename":"PMID:2647765","title":"Higher order chromosome structure is affected by cold-sensitive mutations in a Schizosaccharomyces pombe gene crm1+ which encodes a 115-kD protein preferentially localized in the nucleus and its periphery.","citation":"J Cell Biol 1989 Apr;108(4):1195-207","abstract":"We isolated a novel class of Schizosaccharomyces pombe cold-sensitive mutants with deformed nuclear chromosome domains consisting of thread- or rodlike condensed segments at restrictive temperature. Their mutations were mapped in a novel, identical locus designated crm1 (chromosomal region maintenance). The crm1 mutants also show the following phenotypes. DNA, RNA, and protein syntheses diminish at restrictive temperature. At permissive temperature, the amount of one particular protein, p25, greatly increases. The mutant growth is hypersensitive to Ca2+ and resistant to protein kinase inhibitors. We cloned the 4.1-kb-long crm1+ gene that rescued the above phenotypes by transformation and determined its nucleotide sequence, which predicts a 1,077-residue protein. Affinity-purified antiserum raised against the crm1+ polypeptide expressed in Escherichia coli detected a 115-kD protein in S. pombe extracts. Genomic Southern hybridization and immunoblotting suggested that the crm1+ product might be highly conserved in distant organisms. Through immunofluorescence microscopy, the crm1+ protein appeared to be principally localized within the nucleus and also at its periphery. We speculate that the crm1+ protein might be one of those nuclear components that modify the chromosome structures or regulate the nuclear environment required for maintaining higher order chromosome structures.","authors":"Adachi Y, Yanagida M","authors_abbrev":"Adachi Y et al.","pubmed_publication_date":"Apr 1989","pubmed_entrez_date":"1989-04-01","publication_year":"1989","canto_session_key":"6dee4e54b7401d06","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2015-02-06 16:22:40","canto_approved_date":"2022-01-04 18:31:09","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2013-02-07 09:39:05","canto_added_date":"2012-02-24 05:55:36","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":22,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC3C7.14c","SPAC1805.17"],"gene_count":2,"ltp_gene_count":1,"approved_date":"2015-02-06"},{"uniquename":"PMID:12482912","title":"Regulation of meiotic progression by the meiosis-specific checkpoint kinase Mek1 in fission yeast.","citation":"J Cell Sci 2003 Jan 15;116(Pt 2):259-71","abstract":"During the eukaryotic cell cycle, accurate transmission of genetic information to progeny is ensured by the operation of cell cycle checkpoints. Checkpoints are regulatory mechanisms that block cell cycle progression when key cellular processes are defective or chromosomes are damaged. During meiosis, genetic recombination between homologous chromosomes is essential for proper chromosome segregation at the first meiotic division. In response to incomplete recombination, the pachytene checkpoint (also known as the meiotic recombination checkpoint) arrests or delays meiotic cell cycle progression, thus preventing the formation of defective gametes. Here, we describe a role for a meiosis-specific kinase, Mek1, in the meiotic recombination checkpoint in fission yeast. Mek1 belongs to the Cds1/Rad53/Chk2 family of kinases containing forkhead-associated domains, which participate in a number of checkpoint responses from yeast to mammals. We show that defects in meiotic recombination generated by the lack of the fission yeast Meu13 protein lead to a delay in entry into meiosis I owing to inhibitory phosphorylation of the cyclin-dependent kinase Cdc2 on tyrosine 15. Mutation of mek1(+) alleviates this checkpoint-induced delay, resulting in the formation of largely inviable meiotic products. Experiments involving ectopic overexpression of the mek1(+) gene indicate that Mek1 inhibits the Cdc25 phosphatase, which is responsible for dephosphorylation of Cdc2 on tyrosine 15. Furthermore, the meiotic recombination checkpoint is impaired in a cdc25 phosphorylation site mutant. Thus, we provide the first evidence of a connection between an effector kinase of the meiotic recombination checkpoint and a crucial cell cycle regulator and present a model for the operation of this meiotic checkpoint in fission yeast.","authors":"Pérez-Hidalgo L, Moreno S, San-Segundo PA","authors_abbrev":"Pérez-Hidalgo L et al.","pubmed_publication_date":"15 Jan 2003","pubmed_entrez_date":"2002-12-17","publication_year":"2003","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:58","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17A5.11","SPAC14C4.03","SPAC222.15","SPAC24H6.05"],"gene_count":4,"ltp_gene_count":4},{"uniquename":"PMID:25274039","title":"A systematic genetic screen identifies new factors influencing centromeric heterochromatin integrity in fission yeast.","citation":"Genome Biol 2014;15(10):481","abstract":"Heterochromatin plays important roles in the regulation and stability of eukaryotic genomes. Both heterochromatin components and pathways that promote heterochromatin assembly, including RNA interference, RNAi, are broadly conserved between the fission yeast Schizosaccharomyces pombe and humans. As a result, fission yeast has emerged as an important model system for dissecting mechanisms governing heterochromatin integrity. Thus far, over 50 proteins have been found to contribute to heterochromatin assembly at fission yeast centromeres. However, previous studies have not been exhaustive, and it is therefore likely that further factors remain to be identified.\nTo gain a more complete understanding of heterochromatin assembly pathways, we have performed a systematic genetic screen for factors required for centromeric heterochromatin integrity. In addition to known RNAi and chromatin modification components, we identified several proteins with previously undescribed roles in heterochromatin regulation. These included both known and newly characterised splicing-associated proteins,which are required for proper processing of centromeric transcripts by the RNAi pathway, and COP9 signalosome components Csn1 and Csn2, whose role in heterochromatin assembly can be explained at least in part by a role in the Ddb1-dependent degradation of the heterochromatin regulator Epe1.\nThis work has revealed new factors involved in RNAi-directed heterochromatin assembly in fission yeast. Our findings support and extend previous observations that implicate components of the splicing machinery as a platform for RNAi, and demonstrate a novel role for the COP9 signalosome in heterochromatin regulation.","authors":"Bayne EH, Bijos DA, White SA, de Lima Alves F, Rappsilber J, Allshire RC","authors_abbrev":"Bayne EH et al.","pubmed_publication_date":"2014","pubmed_entrez_date":"2014-10-03","publication_year":"2014","canto_session_key":"4650423a1b7a3d16","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Elizabeth Bayne","canto_approved_date":"2018-10-17 18:25:03","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2014-11-10 13:14:14","canto_added_date":"2014-10-04 00:15:25","annotation_curators":[{"name":"Elizabeth Bayne","community_curator":true,"annotation_count":88,"orcid":"0000-0001-8775-999X","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":24,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPJ698.03c","SPBC31F10.11c","SPAC31G5.18c","SPBP22H7.07","SPBC211.02c","SPBC3E7.13c","SPCC622.16c","SPBC1289.11","SPBC11G11.06c","SPCC11E10.08","SPCC663.11","SPAC1783.05","SPBC31F10.13c","SPBC4B4.05","SPCC132.02","SPBC18H10.10c","SPCP1E11.07c","SPAC18G6.02c","SPCC1393.05","SPAPB17E12.04c","SPBC16H5.15","SPBC32F12.05c","SPAC2G11.08c","SPBC13E7.01","SPBC6B1.10","SPBC609.05","SPAC10F6.02c","SPAC1610.01","SPAC26A3.08","SPBC26H8.07c","SPBC16D10.07c","SPCC188.13c","SPAC4A8.09c","SPBC11C11.08","SPAC644.12","SPBC215.03c","SPAC4F8.12c","SPBC428.08c","SPBC646.02","SPCC1620.10","SPAC13G7.07","SPAPB17E12.02","SPBC3E7.14","SPBC337.06c","SPCC188.11","SPAC17H9.10c","SPCC970.07c","SPBC530.14c","SPCC550.02c","SPBC28F2.04c","SPAC6F12.09","SPBC19C2.14","SPAC29A4.08c","SPBC24C6.11","SPAC30D11.09","SPAC140.03","SPCC663.12","SPAC3A12.11c","SPBC146.05c","SPAC16.02c","SPAC2C4.03c","SPBC215.12","SPAC27F1.09c","SPCC613.12c","SPBC16A3.15c","SPAC664.01c","SPAC17G8.05","SPBP8B7.28c","SPAC27D7.07c","SPAC9.03c"],"gene_count":70,"ltp_gene_count":68,"approved_date":"2014-11-10"},{"uniquename":"PMID:25150109","title":"Systematic targeted gene deletion using the gene-synthesis method in fission yeast.","citation":"J Microbiol Methods 2014 Nov;106:72-77","abstract":"Genome-wide targeted gene deletion, a systematic method to study gene function by replacing target genes with deletion cassettes, using serial-PCR or block-PCR requires elaborate skill. We developed a novel gene-synthesis method to systematically prepare deletion cassettes on a 96-well basis in fission yeast. We designed the 2129-bp deletion cassette as three modules: a central 1397-bp KanMX4 selection marker module and two flanking 366-bp gene-specific artificial linker modules. The central KanMX4 module can be used in multiple deletion cassettes in combination with different sets of flanking modules. The deletion cassettes consisted of 147 oligonucleotides (93 for the central module+25 for each of the flanking modules+4 for the joints) and the oligonucleotides were designed as ~29mers using an in-house program. Oligonucleotides were synthesized on a 96-well basis and ligated into deletion cassettes without gaps by ligase chain reaction, which was followed by two rounds of nested PCR to amplify trace amounts of the ligated cassettes. After the artificial linkers were removed from the deletion cassettes, the cassettes were transformed into wild-type diploid fission yeast strain SP286. We validated the transformed colonies via check PCR and subjected them to tetrad analysis to confirm functional integrity. Using this method, we systematically deleted 563 genes in the fission yeast Schizosaccharomyces pombe with a >90% success rate and a point-mutation rate of ~0.4 mutations per kb. Our method can be used to create systematic gene deletions in a variety of yeasts especially when it included a bar-code system for parallel analyses.","doi":"10.1016/j.mimet.2014.08.005","authors":"Nam M, Lee SJ, Han S, Kim D, Lee M, Kang EJ, Park HO, Lee AR, Lee S, Kim CH, Kim DU, Hoe KL","authors_abbrev":"Nam M et al.","pubmed_publication_date":"Nov 2014","pubmed_entrez_date":"2014-08-24","publication_year":"2014","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-08-27 00:15:24","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:41224899","title":"The zinc bound form of the actinomycete derived natural product compound JBIR-141 induces a mitotic phenotype in fission yeast.","citation":"Sci Rep 2025 Nov 12;15(1):39721","abstract":"This study was designed to identify the natural product compound produced by the actinomycete strain \"S149\" which is capable of inducing a strong small cell phenotype, called wee, in the fission yeast Schizosaccharomyces pombe. We purified the bioactive molecule, which, on the basis of mass spectrometry data, was identified as a novel zinc-bound form of the previously published molecule JBIR-141. JBIR-141 was not previously known to be a zincophore and does not possess structural features common to other bacterial zinc-binding natural product compounds. Testing the effect of the Zn 2+  bound form of JBIR-14 against a series of S. pombe deletion mutants which express a wee phenotype suggested its potential target in fission yeast is either Pyp1, which is involved in regulation of the onset of mitosis, an important control in the eukaryotic cell cycle, or an element in the Pyp1 signalling pathway.","doi":"10.1038/s41598-025-23271-w","authors":"Lewis RA, Hayles J, Hall MJ, Gray J, Mebrate S, Li J, Allenby NEE, Errington J","authors_abbrev":"Lewis RA et al.","pubmed_publication_date":"12 Nov 2025","pubmed_entrez_date":"2025-11-12","publication_year":"2025","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2025-11-14 00:25:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC26F1.10c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:15194814","title":"Role of the alpha-glucanase Agn1p in fission-yeast cell separation.","citation":"Mol Biol Cell 2004 Aug;15(8):3903-14","abstract":"Cell division in the fission yeast Schizosaccharomyces pombe yields two equal-sized daughter cells. Medial fission is achieved by deposition of a primary septum flanked by two secondary septa within the dividing cell. During the final step of cell division, cell separation, the primary septum is hydrolyzed by an endo-(1,3)-beta-glucanase, Eng1p. We reasoned that the cell wall material surrounding the septum, referred to here as the septum edging, also must be hydrolyzed before full separation of the daughter cells can occur. Because the septum edging contains (1,3)-alpha-glucan, we investigated the cellular functions of the putative (1,3)-alpha-glucanases Agn1p and Agn2p. Whereas agn2 deletion results in a defect in endolysis of the ascus wall, deletion of agn1 leads to clumped cells that remained attached to each other by septum-edging material. Purified Agn1p hydrolyzes (1,3)-alpha-glucan predominantly into pentasaccharides, indicating an endo-catalytic mode of hydrolysis. Furthermore, we show that the transcription factors Sep1p and Ace2p regulate both eng1 and agn1 expression in a cell cycle-dependent manner. We propose that Agn1p acts in concert with Eng1p to achieve efficient cell separation, thereby exposing the secondary septa as the new ends of the daughter cells.","authors":"Dekker N, Speijer D, Grün CH, van den Berg M, de Haan A, Hochstenbach F","authors_abbrev":"Dekker N et al.","pubmed_publication_date":"Aug 2004","pubmed_entrez_date":"2004-06-15","publication_year":"2004","canto_session_key":"bfbc893b1ec3877a","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-07-22 14:44:34","canto_approved_date":"2024-06-28 10:19:25","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2015-01-21 11:19:03","canto_added_date":"2012-02-24 05:50:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":22,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC23D3.10c","SPAC14C4.09","SPBC646.06c","SPAC6G10.12c","SPBC4C3.12","SPAC821.09"],"gene_count":6,"ltp_gene_count":5,"approved_date":"2016-07-22"},{"uniquename":"PMID:16157307","title":"Comparison of different signal peptides for secretion of heterologous proteins in fission yeast.","citation":"Biochem Biophys Res Commun 2005 Oct 28;336(3):974-82","abstract":"In the fission yeast Schizosaccharomyces pombe, there are relatively few signal peptides available and most reports of their activity have not been comparative. Using sequence information from the S. pombe genome database we have identified three putative signal peptides, designated Cpy, Amy and Dpp, and compared their ability to support secretion of green fluorescent protein (GFP). In the comparison we also included the two well-described secretion signals derived from the precursors of, respectively, the Saccharomyces cerevisiae alpha-factor and the S. pombe P-factor. The capability of the tested signal peptides to direct secretion of GFP varied greatly. The alpha-factor signal did not confer secretion to GFP and all the produced GFP was trapped intracellular. In contrast, the Cpy signal peptide supported efficient secretion of GFP with yields approximating 10 mg/L. We also found that the use of an attenuated version of the S. cerevisiae URA3 marker substantially increases vector copy number and expression yield in fission yeast.","authors":"Kjaerulff S, Jensen MR","authors_abbrev":"Kjaerulff S et al.","pubmed_publication_date":"28 Oct 2005","pubmed_entrez_date":"2005-09-15","publication_year":"2005","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:28","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:7590311","title":"pDblet, a stable autonomously replicating shuttle vector for Schizosaccharomyces pombe.","citation":"Gene 1995 Oct 16;164(1):173-7","abstract":"We have constructed a new multipurpose stable shuttle vector for the fission yeast Schizosaccharomyces pombe (Sp). Plasmid pDblet was designed to provide convenient features for molecular work and to overcome the inconveniences of previously designed Sp vectors. It contains the Sp ura4 gene as selectable marker and a new highly efficient ARS (autonomously replicating sequence) element, allowing the vector to remain stable as a monomer in Sp. In addition, pDblet transforms Sp with high efficiency and has high mitotic stability and low copy number.","authors":"Brun C, Dubey DD, Huberman JA","authors_abbrev":"Brun C et al.","pubmed_publication_date":"16 Oct 1995","pubmed_entrez_date":"1995-10-16","publication_year":"1995","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:10","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:6092844","title":"Analysis of the structure and transcription of the aro3 cluster gene in Schizosaccharomyces pombe.","citation":"Mol Gen Genet 1984;195(1-2):164-9","abstract":"By selecting activities to complement Escherichia coli aro mutations, a gene responsible for the biosynthesis of aromatic amino acids in Schizosaccharomyces pombe (aro3) was cloned into pBR322. Three independent clones named pFNA1, pFNA2 and pFNA3 were obtained. pFNA1 could complement E. coli aroD only, whereas the other two plasmids were able to complement both aroD and aroE. The aro3 locus of S. pombe was found to be a gene cluster which can be subdivided into five complons, A through E (Strauss 1979). Transformation of S. pombe mutants defective in each complon with the pFNA plasmids indicated that pFNA1 carries at least a part of aro3A, the whole of B, C and D, as well as a part of E, whereas pFNA2 and pFNA3 carry a part of aro3C and the entire D and E complons. A physical map of the aro3 locus was constructed by analyzing the structure of these plasmids and their hybridization patterns to restricted genomic DNA. A transcript 4.5 kb long was detected as the sole aro3 mRNA encompassing all five complons. This study, in addition to the work of Strauss (1979), establishes that the arrangement of the aro3 complons in S. pombe in terms of their enzymatic coding activities is identical with that of Neurospora crassa, but different from that proposed for Saccharomyces cerevisiae.","authors":"Nakanishi N, Yamamoto M","authors_abbrev":"Nakanishi N et al.","pubmed_publication_date":"1984","pubmed_entrez_date":"1984-01-01","publication_year":"1984","canto_triage_status":"Not physically mapped","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:21265777","title":"Nitric oxide and nitrosative stress tolerance in yeast.","citation":"Biochem Soc Trans 2011 Jan;39(1):219-23","abstract":"The opportunistic human fungal pathogen Candida albicans encounters diverse environmental stresses when it is in contact with its host. When colonizing and invading human tissues, C. albicans is exposed to ROS (reactive oxygen species) and RNIs (reactive nitrogen intermediates). ROS and RNIs are generated in the first line of host defence by phagocytic cells such as macrophages and neutrophils. In order to escape these host-induced oxidative and nitrosative stresses, C. albicans has developed various detoxification mechanisms. One such mechanism is the detoxification of NO (nitric oxide) to nitrate by the flavohaemoglobin enzyme CaYhb1. Members of the haemoglobin superfamily are highly conserved and are found in archaea, eukaryotes and bacteria. Flavohaemoglobins have a dioxygenase activity [NOD (NO dioxygenase domain)] and contain three domains: a globin domain, an FAD-binding domain and an NAD(P)-binding domain. In the present paper, we examine the nitrosative stress response in three fungal models: the pathogenic yeast C. albicans, the benign budding yeast Saccharomyces cerevisiae and the benign fission yeast Schizosaccharomyces pombe. We compare their enzymatic and non-enzymatic NO and RNI detoxification mechanisms and summarize fungal responses to nitrosative stress.","doi":"10.1042/BST0390219","authors":"Tillmann A, Gow NA, Brown AJ","authors_abbrev":"Tillmann A et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2011-01-27","publication_year":"2011","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:12","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29423853","title":"Preparation of Cell Lysates of Fission Yeast for Immunoprecipitation.","citation":"Methods Mol Biol 2018;1721:125-133","abstract":"Immunoprecipitation is one of the most important and widely used techniques for the detection and purification of a protein of interest. Thanks to highly specific interaction between antigen and antibody, a target protein is purified and concentrated effectively. To obtain reasonable amounts of a target protein, it is crucially important to prepare total cell lysates in which the target protein is present in a soluble form. Here, we describe methods to prepare total cell lysates of fission yeast, which are then used directly for immunoprecipitation. We also describe some tips to select reagents for preparing buffers having a substantial impact on protein solubility, because there is essentially no reagent that can accommodate the full range of proteins having different characteristics.","doi":"10.1007/978-1-4939-7546-4_12","authors":"Matsuyama A, Shirai A, Yoshida M","authors_abbrev":"Matsuyama A et al.","pubmed_publication_date":"2018","pubmed_entrez_date":"2018-02-10","publication_year":"2018","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2018-02-11 01:15:14","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:15923053","title":"Functional analysis of heterologous GPCR signalling pathways in yeast.","citation":"Trends Biotechnol 2005 Jul;23(7):367-73","abstract":"G protein-coupled receptors (GPCRs) regulate diverse biological processes in eukaryotes and such conservation allows an almost unrestricted interchange of signalling components between different cell types. Yeasts are attractive hosts in which to study GPCRs--they are amenable to both genetic and biochemical manipulation and their robustness, low cost and our ability to create strains that lack endogenous GPCRs make them ideal starting points for the development of assays suitable for high-throughput screening. Here we introduce readers to the possibilities of using yeast to analyse GPCRs describing the endogenous signalling pathways, the development of assays for heterologous GPCRs and the technology to elucidate GPCR structure and activity, focusing on the budding yeast Saccharomyces cerevisiae and recent developments using the fission yeast Schizosaccharomyces pombe.","authors":"Ladds G, Goddard A, Davey J","authors_abbrev":"Ladds G et al.","pubmed_publication_date":"Jul 2005","pubmed_entrez_date":"2005-06-01","publication_year":"2005","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:48","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:10900382","title":"Fission yeast living mitosis visualized by GFP-tagged gene products.","citation":"Micron 2001 Jan;32(1):67-74","abstract":"The fission yeast Schizosaccharomyces pombe has been used as a model organism to study cell cycle control and dynamic chromosome behavior during anaphase segregation as genetic and cytological approaches are easily amenable. To understand the role of gene products involved in these cellular events, it is important to determine intracellular localization of each gene product during the cell cycle. In this article, visualization in living cells of several gene products involved in cell cycle control and sister chromatid separation is described. The genes tagged with jellyfish green fluorescent protein (GFP) include sad1(+) (encoding a spindle pole body (SPB) protein), atb2(+) (alpha-tubulin), mis6(+) (a kinetochore protein), eat1(+) (a novel actin-like protein localized in the nucleus) and cdc13(+) (a mitotic cyclin). In addition, LacI which is bound to a DNA segment containing LacO repeat sequences integrated near the centromere (cen1) is visualized. These are useful to monitor cell cycle events in living cells.","authors":"Tatebe H, Goshima G, Takeda K, Nakagawa T, Kinoshita K, Yanagida M","authors_abbrev":"Tatebe H et al.","pubmed_publication_date":"Jan 2001","pubmed_entrez_date":"2000-07-20","publication_year":"2001","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:52:17","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9716408","title":"Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosis.","citation":"Genes Dev 1998 Aug 15;12(16):2560-73","abstract":"Preventing or delaying progress through the cell cycle in response to DNA damage is crucial for eukaryotic cells to allow the damage to be repaired and not incorporated irrevocably into daughter cells. Several genes involved in this process have been discovered in fission and budding yeast. Here, we report the identification of human and mouse homologs of the Schizosaccharomyces pombe DNA damage checkpoint control gene rad1(+) and its Saccharomyces cerevisiae homolog RAD17. The human gene HRAD1 is located on chromosome 5p13 and is most homologous to S. pombe rad1(+). This gene encodes a 382-amino-acid residue protein that is localized mainly in the nucleus and is expressed at high levels in proliferative tissues. This human gene significantly complements the sensitivity to UV light of a S. pombe strain mutated in rad1(+). Moreover, HRAD1 complements the checkpoint control defect of this strain after UV exposure. In addition to functioning in DNA repair checkpoints, S. cerevisiae RAD17 plays a role during meiosis to prevent progress through prophase I when recombination is interrupted. Consistent with a similar role in mammals, Rad1 protein is abundant in testis, and is associated with both synapsed and unsynapsed chromosomes during meiotic prophase I of spermatogenesis, with a staining pattern distinct from that of the recombination proteins Rad51 and Dmc1. Together, these data imply an important role for hRad1 both in the mitotic DNA damage checkpoint and in meiotic checkpoint mechanisms, and suggest that these events are highly conserved from yeast to humans.","authors":"Freire R, Murguía JR, Tarsounas M, Lowndes NF, Moens PB, Jackson SP","authors_abbrev":"Freire R et al.","pubmed_publication_date":"15 Aug 1998","pubmed_entrez_date":"1998-08-26","publication_year":"1998","canto_session_key":"01178e31f6c2c035","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2018-03-17 11:30:28","canto_approved_date":"2018-03-17 11:30:28","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2018-03-17 11:30:17","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":4,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1952.07"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-03-17"},{"uniquename":"EMBL:AU008348","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:9336465","title":"Identification and characterization of a telomerase activity from Schizosaccharomyces pombe.","citation":"Nucleic Acids Res 1997 Nov 01;25(21):4331-7","abstract":"A telomerase-like primer extension activity has been detected in chromatographic fractions derived from Schizosaccharomyces pombe extracts. This primer extension activity acts preferentially on dG-rich oligodeoxynucleotides, is sensitive to RNase A pretreatment and requires all four deoxynucleotides for optimal polymerization. The extension products are also truncated by the inclusion of any one of the four dideoxynucleotides, consistent with the presence of all four bases in the S.pombe telomeric repeats. The intensity distribution of the extension products and the dideoxynucleotide termination pattern suggest that nucleotide addition is template directed, and that telomere-like sequences are added to the primers. In particular, the sequence d(CGGTTA), a variant of the S.pombe telomeric repeat, can be added directly by the in vitro activity. Partially purified S.pombe telomerase sediments as a 35S particle, suggesting that it exists in vivo as part of a large multi-protein complex.","authors":"Lue NF, Peng Y","authors_abbrev":"Lue NF et al.","pubmed_publication_date":"01 Nov 1997","pubmed_entrez_date":"1997-10-23","publication_year":"1997","canto_session_key":"f377e041d1b291cc","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-08-16 15:59:37","canto_approved_date":"2024-08-07 15:06:36","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2017-08-16 15:59:17","canto_added_date":"2012-02-24 05:53:35","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":1,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC29A3.14c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2017-08-16"},{"uniquename":"EMBL:AU009793","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18617025","title":"High pressure freezing and freeze substitution of Schizosaccharomyces pombe and Saccharomyces cerevisiae for TEM.","citation":"Methods Cell Biol 2008;88:3-17","abstract":"The use of standard room temperature chemical fixation protocols for the ultrastructural preservation of yeast and subsequent observation under the electron microscope is fraught with difficulties. Many protocols require the use of enzymatic digestion of the cell wall in order to facilitate the entry of fixatives into the cell interior. Others rely on the use of permanganate-based fixative solutions, which whilst enabling overall preservation of the cell, does require multiple centrifugation, washing, and resuspension steps. This often results in the significant loss of sample volume whilst the use of permanganate can cause extraction of cytoplasmic components. The use of low temperature techniques and in particular high pressure freezing (HPF) and freeze substitution (FS) overcomes many of these problems. With the recent advances in cryotechnologies and in particular the development of commercially available equipment such as the high pressure freezer, the level of ultrastructural preservation attainable in electron microscopy has increased markedly. It is now possible to capture dynamic time sensitive events and to place them in their ultrastructural context with a level of resolution which at the present time can only be achieved with electron microscopy.","doi":"10.1016/S0091-679X(08)00401-9","authors":"Murray S","authors_abbrev":"Murray S","pubmed_publication_date":"2008","pubmed_entrez_date":"2008-07-12","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:31","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23071310","title":"Punctuation and syntax of the RNA polymerase II CTD code in fission yeast.","citation":"Proc Natl Acad Sci U S A 2012 Oct 30;109(44):18024-9","abstract":"The primary structure and phosphorylation pattern of the tandem Y(1)S(2)P(3)T(4)S(5)P(6)S(7) repeats of the RNA polymerase II carboxyl-terminal domain (CTD) convey information about the transcription apparatus--a CTD code--to a large ensemble of CTD-binding receptor proteins. Four of the seven coding \"letters\" of the fission yeast CTD (Tyr1, Pro3, Ser5, Pro6) are essential in vivo, but the grammatical rules of the code are obscure. Here we show that the minimal fission yeast CTD coding unit is a decapeptide Y(1)S(2)P(3)T(4)S(5)P(6)S(7)Y(1)S(2)P(3) and the spacing between coding units is flexible; the coding unit must contain two Tyr1 residues and the spacing between consecutive tyrosines is important; Ser5-PO(4)-Pro6 comprises an essential two-letter code \"word\" that is read by the mRNA capping apparatus; and a threshold number of Ser5-PO(4)-Pro6 words are needed to comprise a readable \"sentence\" of CTD information. Bypassing the essentiality of the Ser5 and Pro6 letters by fusion of capping enzymes to the CTD helped reveal how CTD phosphorylation circuits are wired in vivo. We found that the Ser2-PO(4) mark is independent of Ser5, Pro6, Ser7, and Thr4, whereas the Ser5-PO(4) mark is independent of Ser2, Ser7, and Thr4. These results provide unique insights to the reading and writing of the CTD code.","doi":"10.1073/pnas.1208995109","authors":"Schwer B, Sanchez AM, Shuman S","authors_abbrev":"Schwer B et al.","pubmed_publication_date":"30 Oct 2012","pubmed_entrez_date":"2012-10-17","publication_year":"2012","canto_session_key":"e1d7eb57bf0e849f","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-11-19 00:16:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:17623903","title":"Analysing the DNA damage and replication checkpoints in DT40 cells.","citation":"Subcell Biochem 2006;40:107-17","abstract":"Eukaryotic cells respond to DNA damage or blocks to DNA replication by triggering a variety of \"checkpoint\" responses which delay cell cycle progression, modulate DNA replication, and facilitate DNA repair. Checkpoints play a vital role in maintaining genome integrity, particularly under conditions of genotoxic stress, and mutations in checkpoint genes can predispose to cancer and aging. Checkpoints are best understood at the molecular level in model organisms such as fission yeast, where the presence of aberrant DNA structures is sensed and relayed via signal transduction pathways to activate the checkpoint effector kinases, Chk1 and Cds1/ Chk2, which implement appropriate responses. Many of the yeast checkpoint sensor, transducer, and effector proteins are conserved in vertebrate cells, raising the question of whether they function in a similar or analogous way. DT40 cells provide a particularly tractable experimental system for genetic and biochemical dissection of checkpoints in vertebrates. Thus far, gene knockouts in DT40 have revealed that the Chk1 and Chk2 checkpoint effector kinases control a very different range of checkpoint responses in vertebrates compared to yeast. In future, these and other DT40 mutants will provide powerful tools for understanding the molecular basis of these unexpected differences and detailed studies of checkpoint mechanisms.","authors":"Rainey MD, Zachos G, Gillespie DA","authors_abbrev":"Rainey MD et al.","pubmed_publication_date":"2006","pubmed_entrez_date":"2007-07-13","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:52","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26447710","title":"Constitutive Tor2 Activity Promotes Retention of the Amino Acid Transporter Agp3 at Trans-Golgi/Endosomes in Fission Yeast.","citation":"PLoS One 2015;10(10):e0139045","abstract":"Amino acid transporters are located at specific subcellular compartments, and their localizations are regulated by the extracellular availability of amino acids. In yeast, target of rapamycin (TOR) activation induces the internalization of amino acid transporters located at the plasma membrane. However, whether and how TOR signaling regulates other amino acid transporters located at intracellular compartments remains unknown. Here, we demonstrate that in the fission yeast, the TOR inhibitor Torin-1 induces the transfer of several yellow fluorescent protein (YFP)-fused intracellular amino acid transporters, including Agp3, Isp5, Aat1, and Put4, from trans-Golgi/endosomes into the vacuoles. By contrast, the localizations of YFP-fused Can1, Fnx1, and Fnx2 transporter proteins were unaffected upon Torin-1 treatment. There are two TOR isoforms in fission yeast, Tor1 and Tor2. Whereas tor1 deletion did not affect the Torin-1-induced transfer of Agp3-YFP, Tor2 inhibition using a temperature-sensitive mutant induced the transfer of Agp3-YFP to the vacuolar lumen, similar to the effects of Torin-1 treatment. Tor2 inhibition also induced the transfer of the YFP-fused Isp5, Aat1, and Put4 transporter proteins to the vacuoles, although only partial transfer of the latter two transporters was observed. Under nitrogen depletion accompanied by reduced Tor2 activity, Agp3-YFP was transferred from the trans-Golgi/endosomes to the plasma membrane and then to the vacuoles, where it was degraded by the vacuolar proteases Isp6 and Psp3. Mutants with constitutively active Tor2 showed delayed transfer of Agp3-YFP to the plasma membrane upon nitrogen depletion. Cells lacking Tsc2, a negative regulator of Tor2, also showed a delay in this process in a Tor2-dependent manner. Taken together, these findings suggest that constitutive Tor2 activity is critical for the retention of amino acid transporters at trans-Golgi/endosomes. Moreover, nitrogen depletion suppresses Tor2 activity through Tsc2, thereby promoting the surface expression of these transporters.","doi":"10.1371/journal.pone.0139045","authors":"Liu Q, Ma Y, Zhou X, Furuyashiki T","authors_abbrev":"Liu Q et al.","pubmed_publication_date":"2015","pubmed_entrez_date":"2015-10-09","publication_year":"2015","canto_session_key":"782b2d33c30d2025","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-10-10 00:18:52","annotation_curators":[],"annotation_file_curators":[],"genes":["SPBC216.07c","SPAC630.13c"],"gene_count":2,"ltp_gene_count":2},{"uniquename":"PMID:34346498","title":"Loss of kinesin-8 improves the robustness of the self-assembled spindle in Schizosaccharomyces pombe.","citation":"J Cell Sci 2021 Aug 15;134(16)","abstract":"Chromosome segregation in female meiosis in many metazoans is mediated by acentrosomal spindles, the existence of which implies that microtubule spindles self-assemble without the participation of the centrosomes. Although it is thought that acentrosomal meiosis is not conserved in fungi, we recently reported the formation of self-assembled microtubule arrays, which were able to segregate chromosomes, in fission yeast mutants, in which the contribution of the spindle pole body (SPB; the centrosome equivalent in yeast) was specifically blocked during meiosis. Here, we demonstrate that this unexpected microtubule formation represents a bona fide type of acentrosomal spindle. Moreover, a comparative analysis of these self-assembled spindles and the canonical SPB-dependent spindle reveals similarities and differences; for example, both spindles have a similar polarity, but the location of the γ-tubulin complex differs. We also show that the robustness of self-assembled spindles can be reinforced by eliminating kinesin-8 family members, whereas kinesin-8 mutants have an adverse impact on SPB-dependent spindles. Hence, we consider that reinforced self-assembled spindles in yeast will help to clarify the molecular mechanisms behind acentrosomal meiosis, a crucial step towards better understanding gametogenesis.","doi":"10.1242/jcs.253799","authors":"Pineda-Santaella A, Fernández-Castillo N, Jiménez-Martín A, Macías-Cabeza MDC, Sánchez-Gómez Á, Fernández-Álvarez A","authors_abbrev":"Pineda-Santaella A et al.","pubmed_publication_date":"15 Aug 2021","pubmed_entrez_date":"2021-08-04","publication_year":"2021","canto_session_key":"b1bc10e390be46c7","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Alberto Pineda Santaella","canto_first_approved_date":"2021-09-23 13:34:50","canto_approved_date":"2022-04-27 15:21:43","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-09-13 12:38:35","canto_added_date":"2021-08-06 00:15:04","annotation_curators":[{"name":"Alberto Pineda Santaella","community_curator":true,"annotation_count":28,"orcid":"0000-0003-1156-8104","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":12,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAPB1A10.09","SPAC3A11.14c","SPCC895.07","SPAC6G9.13c","SPBC244.01c","SPBC15D4.01c","SPBC12D12.01","SPBC1685.15c","SPBC2F12.13","SPCC736.14","SPBC365.15"],"gene_count":11,"ltp_gene_count":11,"approved_date":"2021-09-23"},{"uniquename":"PMID:14506270","title":"The novel Rho GTPase-activating protein family protein, Rga8, provides a potential link between Cdc42/p21-activated kinase and Rho signaling pathways in the fission yeast, Schizosaccharomyces pombe.","citation":"J Biol Chem 2003 Dec 05;278(49):48821-30","abstract":"The PAK family kinase, Shk1, is an essential regulator of polarized growth in the fission yeast, Schizosaccharomyces pombe. Here we describe the characterization of a novel member of the RhoGAP family, Rga8, identified from a two-hybrid screen for proteins that interact with the Shk1 kinase domain. Although deletion of the rga8 gene in wild type S. pombe cells results in no obvious phenotypic defects under normal growth conditions, it partially suppresses the cold-sensitive growth and morphological defects of S. pombe cells carrying a hypomorphic allele of the shk1 gene. By contrast, overexpression of rga8 is lethal to shk1-defective cells and causes morphological and cytokinesis defects in wild type S. pombe cells. Consistent with a role for Rga8 as a downstream target of Shk1, we show that the Rga8 protein is directly phosphorylated by Shk1 in vitro and phosphorylated in a Shk1-dependent fashion in S. pombe cells. Fluorescence photomicroscopy of the GFP-Rga8 fusion protein indicates that Rga8 is localized to the cell ends during interphase and to the septum-forming region during cytokinesis. In S. pombe cells carrying the orb2-34 allele of shk1, Rga8 exhibits a monopolar pattern of localization, providing evidence that Shk1 contributes to the regulation of Rga8 localization. Although molecular analyses suggest that Rga8 functions as a GAP for the S. pombe Rho1 GTPase, genetic experiments suggest that Rga8 and Rho1 have a positive functional interaction and that gain of Rho1 function, like gain of Rga8 function, is lethal to Shk1-defective cells. Our results suggest that Rga8 is a Shk1 substrate that negatively regulates Shk1-dependent growth control pathway(s) in S. pombe, potentially through interaction with the Rho1 GTPase.","authors":"Yang P, Qyang Y, Bartholomeusz G, Zhou X, Marcus S","authors_abbrev":"Yang P et al.","pubmed_publication_date":"05 Dec 2003","pubmed_entrez_date":"2003-09-25","publication_year":"2003","canto_session_key":"d7d80818cadb002c","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-31 14:27:59","canto_approved_date":"2026-01-31 11:58:46","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2016-06-23 16:24:54","canto_added_date":"2012-02-24 05:50:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":25,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC1F5.09c","SPCC1223.06","SPAC1F7.04","SPAC13A11.01c","SPBC1604.14c"],"gene_count":5,"ltp_gene_count":5,"approved_date":"2017-07-31"},{"uniquename":"PMID:32889726","title":"Long-Term Imaging and Dynamic Analysis of Cytoophidia in Yeast.","citation":"Methods Mol Biol 2021;2196:235-244","abstract":"Live-cell imaging is widely used by researchers to study cellular dynamics and obtain a deep understanding of cell biological processes. Keeping cells in the proper growing environment and immobilizing the cells are essential for the imaging of live yeast cells. Here we describe a protocol for monitoring cytoophidia in Saccharomyces cerevisiae and Schizosaccharomyces pombe using inverted confocal fluorescence microscopy. This protocol includes yeast culture, sample preparation, fluorescence imaging, and data analysis.","doi":"10.1007/978-1-0716-0868-5_19","authors":"Zhang S, Li H, Liu JL","authors_abbrev":"Zhang S et al.","pubmed_publication_date":"2021","pubmed_entrez_date":"2020-09-05","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2020-09-07 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:22522705","title":"Mmi1 RNA surveillance machinery directs RNAi complex RITS to specific meiotic genes in fission yeast.","citation":"EMBO J 2012 May 16;31(10):2296-308","abstract":"RNA interference (RNAi) silences gene expression by acting both at the transcriptional and post-transcriptional levels in a broad range of eukaryotes. In the fission yeast Schizosaccharomyces pombe the RNA-Induced Transcriptional Silencing (RITS) RNAi complex mediates heterochromatin formation at non-coding and repetitive DNA. However, the targeting and role of RITS at other genomic regions, including protein-coding genes, remain unknown. Here we show that RITS localizes to specific meiotic genes and mRNAs. Remarkably, RITS is guided to these meiotic targets by the RNA-binding protein Mmi1 and its associated RNA surveillance machinery that together degrade selective meiotic mRNAs during vegetative growth. Upon sexual differentiation, RITS localization to the meiotic genes and mRNAs is lost. Large-scale identification of Mmi1 RNA targets reveals that RITS subunit Chp1 associates with the vast majority of them. In addition, loss of RNAi affects the effective repression of sexual differentiation mediated by the Mmi1 RNA surveillance machinery. These findings uncover a new mechanism for recruiting RNAi to specific meiotic genes and suggest that RNAi participates in the control of sexual differentiation in fission yeast.","doi":"10.1038/emboj.2012.105","authors":"Hiriart E, Vavasseur A, Touat-Todeschini L, Yamashita A, Gilquin B, Lambert E, Perot J, Shichino Y, Nazaret N, Boyault C, Lachuer J, Perazza D, Yamamoto M, Verdel A","authors_abbrev":"Hiriart E et al.","pubmed_publication_date":"16 May 2012","pubmed_entrez_date":"2012-04-24","publication_year":"2012","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-06-12 03:08:03","annotation_curators":[],"annotation_file_curators":[],"genes":["SPNCRNA.103","SPAC18G6.02c","SPCC188.13c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:25422470","title":"Oscillatory AAA+ ATPase Knk1 constitutes a novel morphogenetic pathway in fission yeast.","citation":"Proc Natl Acad Sci U S A 2014 Dec 16;111(50):17899-904","abstract":"Cellular morphogenesis relies partly on cell polarization by the cytoskeleton. In the fission yeast Schizosaccharomyces pombe, it is well established that microtubules (MTs) deliver the spatial cue Tea1, a kelch repeat protein, to the tip regions to direct the growth machinery at the cell tips driving the linear extension of the rod-shaped organism to maintain a straight long axis. Here, we report the characterization of Knk1 (kink), a previously unidentified member of the superfamily of ATPases associated with various cellular activities (AAA(+)), whose deletion causes a unique morphological defect characterized by the formation of kinks close to cell tips. Through genetic analysis, we place Knk1 into a novel pathway controlling cell shape independently of MTs and Tea1. Knk1 localizes at cell tips. Its localization is mediated by the Knk1 N terminus and is enhanced upon ATP binding to the C-terminal ATPase domain. Furthermore, Knk1 tip recruitment is regulated by SRC-like adaptor 2 (Sla2) and cell division cycle 42 (Cdc42) independently of Sla2's role in endocytosis. Finally, we discovered that Knk1 shows an anticorrelated oscillatory behavior between the two cell tips at a periodicity that is different from the reported oscillatory Cdc42 dynamics.","doi":"10.1073/pnas.1407226111","authors":"Scheffler K, Recouvreux P, Paoletti A, Tran PT","authors_abbrev":"Scheffler K et al.","pubmed_publication_date":"16 Dec 2014","pubmed_entrez_date":"2014-11-26","publication_year":"2014","canto_session_key":"30447cf8a308c262","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-07-05 15:36:30","canto_approved_date":"2024-04-04 08:29:40","canto_approver_orcid":"0009-0003-9059-1333","canto_session_submitted_date":"2017-02-07 16:53:18","canto_added_date":"2014-11-27 01:15:28","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":33,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC146.13c","SPAC821.12","SPBC1685.15c","SPBC2F12.13","SPAC688.11","SPCC417.07c","SPCC1840.02c","SPAC18G6.15","SPAC2G11.06","SPCC895.05","SPCC1223.06","SPAC110.03","SPAC24H6.05","SPAC4F10.15c","SPAC23C4.08","SPBC947.01"],"gene_count":16,"ltp_gene_count":10,"approved_date":"2017-07-05"},{"uniquename":"PMID:20617397","title":"Expression and secretion of a CB4-1 scFv-GFP fusion protein by fission yeast.","citation":"Appl Biochem Biotechnol 2011 Jan;163(1):80-9","abstract":"There is a rapidly growing demand for fluorescent single-chain Fv (scFv) antibody fragments for many applications. Yeasts have developed into attractive hosts for recombinant production of these functionalized proteins because they provide several advantages over prokaryotes and higher eukaryotes as expression systems, e.g., being capable of high-level secretion of heterologous proteins. In this study, we report Schizosaccharomyces pombe as a new host organism for secretory production of scFv-green fluorescent protein (GFP) fusions and compare it with previously described yeast expression systems. We cloned a plasmid for the expression and secretion of the anti-p24 (human immunodeficiency virus 1) CB4-1 scFv fused to GFP. After expression of the scFv-GFP fused to an N-terminal Cpy1 secretion signal sequence, fluorescence microscopy of living yeast cells indicated that the heterologous protein entered the secretory pathway. Western blot analysis of cell-free culture supernatants confirmed that the scFv-GFP was efficiently secreted with yields up to 5 mg/L. In addition, fluorescence measurements of culture supernatants demonstrated that the GFP moiety of the scFv-GFP protein is fully functional after secretion. Our data suggest that S. pombe has the potential for being used as alternative expression host in recombinant antibody fragment production by ensuring efficient protein processing and secretion.","doi":"10.1007/s12010-010-9018-9","authors":"Naumann JM, Küttner G, Bureik M","authors_abbrev":"Naumann JM et al.","pubmed_publication_date":"Jan 2011","pubmed_entrez_date":"2010-07-10","publication_year":"2011","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:47:30","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16423077","title":"Atomic force microscopic study of the influence of physical stresses on Saccharomyces cerevisiae and Schizosaccharomyces pombe.","citation":"FEMS Yeast Res 2006 Jan;6(1):120-8","abstract":"Morphological changes in the cell surfaces of the budding yeast Saccharomyces cerevisiae (strain NCYC 1681), and the fission yeast Schizosaccharomyces pombe (strain DVPB 1354), in response to thermal and osmotic stresses, were investigated using an atomic force microscope. With this microscope imaging, together with measurements of culture viability and cell size, it was possible to relate topological changes of the cell surface at nanoscale with cellular stress physiology. As expected, when the yeasts were exposed to thermostress or osmostress, their viability together with the mean cell volume decreased in conjunction with the increase in thermal or osmotic shock. Nevertheless, the viability of cells stressed for up to 1 h remained relatively high. For example, viabilities were >50% and >90% for the thermostressed, and >60% and >70% for the osmostressed S. cerevisiae and Schiz. pombe, respectively. Mean cell volume measurements, and bearing and roughness analyses of atomic force microscope images of stressed yeasts indicate that Schiz. pombe may be more resistant to physical stresses than S. cerevisiae. Overall, this study has highlighted the usefulness of atomic force microscope in studies of yeast stress physiology.","authors":"Adya AK, Canetta E, Walker GM","authors_abbrev":"Adya AK et al.","pubmed_publication_date":"Jan 2006","pubmed_entrez_date":"2006-01-21","publication_year":"2006","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16999738","title":"Ammonium transporter genes in the fission yeast Schizosaccharomyces pombe: role in ammonium uptake and a morphological transition.","citation":"Genes Cells 2006 Oct;11(10):1183-95","abstract":"Ammonium is an important source of nitrogen for many microorganisms, including yeast, and its availability also has substantial effects on the nitrogen metabolism and development of yeast cells. Three ammonium transporter genes of the fission yeast Schizosaccharomyces pombe, named amt1, amt2, and amt3, were identified on the basis of amino acid sequence similarity to members of the ammonium transporter/methylammonium permease (Amt/Mep) family. A series of strains were constructed that carry all combinations of amt deletion (amt delta) mutations, and tested for growth on low ammonium and resistance to the toxic ammonium analog methylammonium. The amt1 delta and amt2 delta single mutants had different growth defects, and the amt1 delta amt2 delta double mutant displayed a much more severe growth defect on < or = 5 mM ammonium. All single mutants exhibited methylammonium resistance but to different extents: amt2 delta was the most resistant and amt3 delta was the least. These results suggest that the amt genes encode functional transporters with distinct uptake properties. In response to ammonium limitation, the wild-type strain isogenic to the amt delta mutants underwent filamentous growth underneath the surface of solid medium. No such filamentous invasive growth, however, was observed for the amt1 delta mutant, indicating that Amt1 transporter is required for ammonium limitation-induced filamentous invasive growth.","authors":"Mitsuzawa H","authors_abbrev":"Mitsuzawa H","pubmed_publication_date":"Oct 2006","pubmed_entrez_date":"2006-09-27","publication_year":"2006","canto_session_key":"652f5d546c75f748","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC664.14","SPCPB1C11.01","SPAC2E1P3.02c"],"gene_count":3,"ltp_gene_count":3},{"uniquename":"PMID:2673232","title":"Regulation of meiosis: from DNA binding protein to protein kinase.","citation":"Bioessays 1989 Jul;11(1):9-14","abstract":"The transition from mitotic cell division to meiosis in yeast is governed by both the mating-type genes and signals from the environment. Analysis of mutants that are unable to regulate entry into meiosis has identified many genes that function in this process and in some cases, the biochemical activity of their protein products has been described. At least two of the the mating-type genes of Saccharomyces cerevisiae encode DNA binding proteins that regulate transcription of unlinked genes required for entry into meiosis. Meiotic development of the distantly related yeast, Schizosaccharomyces pombe, is also controlled by the mating-type genes but in this yeast, their role is to regulate expression of a protein that acts as an inhibitor of a protein kinase. The ability to use the powerful tool of genetics in yeast has provided us with many new insights into the problem of meiotic development.","authors":"McLeod M","authors_abbrev":"McLeod M","pubmed_publication_date":"Jul 1989","pubmed_entrez_date":"1989-07-01","publication_year":"1989","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:35","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:36301993","title":"Genome-wide quantification of contributions to sexual fitness identifies genes required for spore viability and health in fission yeast.","citation":"PLoS Genet 2022 Oct;18(10):e1010462","abstract":"Numerous genes required for sexual reproduction remain to be identified even in simple model species like Schizosaccharomyces pombe. To address this, we developed an assay in S. pombe that couples transposon mutagenesis with high-throughput sequencing (TN-seq) to quantitatively measure the fitness contribution of nonessential genes across the genome to sexual reproduction. This approach identified 532 genes that contribute to sex, including more than 200 that were not previously annotated to be involved in the process, of which more than 150 have orthologs in vertebrates. Among our verified hits was an uncharacterized gene, ifs1 (important for sex), that is required for spore viability. In two other hits, plb1 and alg9, we observed a novel mutant phenotype of poor spore health wherein viable spores are produced, but the spores exhibit low fitness and are rapidly outcompeted by wild type. Finally, we fortuitously discovered that a gene previously thought to be essential, sdg1 (social distancing gene), is instead required for growth at low cell densities and can be rescued by conditioned medium. Our assay will be valuable in further studies of sexual reproduction in S. pombe and identifies multiple candidate genes that could contribute to sexual reproduction in other eukaryotes, including humans.","doi":"10.1371/journal.pgen.1010462","authors":"Billmyre RB, Eickbush MT, Craig CJ, Lange JJ, Wood C, Helston RM, Zanders SE","authors_abbrev":"Billmyre RB et al.","pubmed_publication_date":"Oct 2022","pubmed_entrez_date":"2022-10-27","publication_year":"2022","canto_session_key":"591b0031c13ea635","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2022-10-29 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC3G6.03c"],"gene_count":1,"ltp_gene_count":0},{"uniquename":"PMID:34663801","title":"GproDIA enables data-independent acquisition glycoproteomics with comprehensive statistical control.","citation":"Nat Commun 2021 Oct 18;12(1):6073","abstract":"Large-scale profiling of intact glycopeptides is critical but challenging in glycoproteomics. Data independent acquisition (DIA) is an emerging technology with deep proteome coverage and accurate quantitative capability in proteomics studies, but is still in the early stage of development in the field of glycoproteomics. We propose GproDIA, a framework for the proteome-wide characterization of intact glycopeptides from DIA data with comprehensive statistical control by a 2-dimentional false discovery rate approach and a glycoform inference algorithm, enabling accurate identification of intact glycopeptides using wide isolation windows. We further utilize a semi-empirical spectrum prediction strategy to expand the coverage of spectral libraries of glycopeptides. We benchmark our method for N-glycopeptide profiling on DIA data of yeast and human serum samples, demonstrating that DIA with GproDIA outperforms the data-dependent acquisition-based methods for glycoproteomics in terms of capacity and data completeness of identification, as well as accuracy and precision of quantification. We expect that this work can provide a powerful tool for glycoproteomic studies.","doi":"10.1038/s41467-021-26246-3","authors":"Yang Y, Yan G, Kong S, Wu M, Yang P, Cao W, Qiao L","authors_abbrev":"Yang Y et al.","pubmed_publication_date":"18 Oct 2021","pubmed_entrez_date":"2021-10-19","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-11-21 01:15:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:370130","title":"Altered patterns of ribonucleic acid synthesis during the cell cycle: a mechanism compensating for variation in gene concentration.","citation":"J Cell Sci 1979 Feb;35:25-40","abstract":"In the fission yeast Schizosaccharomyces pombe, a series of diploid mutants divides at smaller cell sizes than wild type. In these smaller strains, the mean gene concentration (defined by previous authors as the DNA to protein ratio) is higher than in wild type. Such an increase in gene concentration should also increase the concentration of those components such as messenger and ribosomal RNA, whose rate of synthesis is determined by gene dosage. We show that the mean concentrations of these 2 RNA species in the small cells are not increased, but are the same as in wild type. The small mutant cells are thus able to compensate for changes in gene concentration. This compensation is shown to operate through differences in the patterns of synthesis of RNA during the cell cycle. In all the strains of the diploid series, the rates of synthesis of messenger and ribosomal RNA double as steps once in each cell cycle. The timings of the steps in the cell cycle appear to be cell-size related, since the smaller the cell at division, the later are the steps in the cell cycle. In contrast, there is comparatively little variation in the timing of DNA replication in the cycles of cells of different sizes. We propose that after DNA replication, there is a delay before doubling in the rate of transcription. Such a cell mass-related delay is all that is required to compensate for increased gene concentration, and results in the same mean functional DNA concentration in all strains. This mechanism will maintain the same mean messenger and ribosomal RNA concentrations in cells dividing at different sizes. Ways in which the cell size-related control over transcription may operate are discussed.","authors":"Fraser RS, Nurse P","authors_abbrev":"Fraser RS et al.","pubmed_publication_date":"Feb 1979","pubmed_entrez_date":"1979-02-01","publication_year":"1979","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:29252184","title":"Quiescence unveils a novel mutational force in fission yeast.","citation":"Elife 2017 Dec 18;6","abstract":"To maintain life across a fluctuating environment, cells alternate between phases of cell division and quiescence. During cell division, the spontaneous mutation rate is expressed as the probability of mutations  per  generation (Luria and Delbrück, 1943; Lea and Coulson, 1949), whereas during quiescence it will be expressed  per  unit of time. In this study, we report that during quiescence, the unicellular haploid fission yeast accumulates mutations as a linear function of time. The novel mutational landscape of quiescence is characterized by insertion/deletion (indels) accumulating as fast as single nucleotide variants (SNVs), and elevated amounts of deletions. When we extended the study to 3 months of quiescence, we confirmed the replication-independent mutational spectrum at the whole-genome level of a clonally aged population and uncovered phenotypic variations that subject the cells to natural selection. Thus, our results support the idea that genomes continuously evolve under two alternating phases that will impact on their size and composition.","doi":"10.7554/eLife.27469","authors":"Gangloff S, Achaz G, Francesconi S, Villain A, Miled S, Denis C, Arcangioli B","authors_abbrev":"Gangloff S et al.","pubmed_publication_date":"18 Dec 2017","pubmed_entrez_date":"2017-12-19","publication_year":"2017","canto_session_key":"e1cd3ce7758cc621","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2017-12-20 01:15:15","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25738810","title":"Sequence features and transcriptional stalling within centromere DNA promote establishment of CENP-A chromatin.","citation":"PLoS Genet 2015 Mar;11(3):e1004986","abstract":"Centromere sequences are not conserved between species, and there is compelling evidence for epigenetic regulation of centromere identity, with location being dictated by the presence of chromatin containing the histone H3 variant CENP-A. Paradoxically, in most organisms CENP-A chromatin generally occurs on particular sequences. To investigate the contribution of primary DNA sequence to establishment of CENP-A chromatin in vivo, we utilised the fission yeast Schizosaccharomyces pombe. CENP-ACnp1 chromatin is normally assembled on ∼10 kb of central domain DNA within these regional centromeres. We demonstrate that overproduction of S. pombe CENP-ACnp1 bypasses the usual requirement for adjacent heterochromatin in establishing CENP-ACnp1 chromatin, and show that central domain DNA is a preferred substrate for de novo establishment of CENP-ACnp1 chromatin. When multimerised, a 2 kb sub-region can establish CENP-ACnp1 chromatin and form functional centromeres. Randomization of the 2 kb sequence to generate a sequence that maintains AT content and predicted nucleosome positioning is unable to establish CENP-ACnp1 chromatin. These analyses indicate that central domain DNA from fission yeast centromeres contains specific information that promotes CENP-ACnp1 incorporation into chromatin. Numerous transcriptional start sites were detected on the forward and reverse strands within the functional 2 kb sub-region and active promoters were identified. RNAPII is enriched on central domain DNA in wild-type cells, but only low levels of transcripts are detected, consistent with RNAPII stalling during transcription of centromeric DNA. Cells lacking factors involved in restarting transcription-TFIIS and Ubp3-assemble CENP-ACnp1 on central domain DNA when CENP-ACnp1 is at wild-type levels, suggesting that persistent stalling of RNAPII on centromere DNA triggers chromatin remodelling events that deposit CENP-ACnp1. Thus, sequence-encoded features of centromeric DNA create an environment of pervasive low quality RNAPII transcription that is an important determinant of CENP-ACnp1 assembly. These observations emphasise roles for both genetic and epigenetic processes in centromere establishment.","doi":"10.1371/journal.pgen.1004986","authors":"Catania S, Pidoux AL, Allshire RC","authors_abbrev":"Catania S et al.","pubmed_publication_date":"Mar 2015","pubmed_entrez_date":"2015-03-05","publication_year":"2015","canto_session_key":"c91f46f118dcb9c5","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2015-03-06 01:15:27","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:23489294","title":"Stress-induced lncRNAs evade nuclear degradation and enter the translational machinery.","citation":"Genes Cells 2013 May;18(5):353-68","abstract":"Long noncoding RNAs (lncRNAs) play important roles in the regulation of gene expression. In fission yeast, glucose starvation triggers a transcriptional cascade of polyadenylated lncRNAs in the upstream region of the fructose-1,6-bisphosphatase gene (fbp1(+) ), which is correlated with stepwise chromatin remodeling and necessary for the massive induction of fbp1(+) mRNA. Here, we show that these novel metabolic stress-induced lncRNAs (mlonRNAs) are 5'-capped, less stable than fbp1(+) mRNA and sensitive to a certain extent to the nuclear exosome cofactor Rrp6. However, most mlonRNAs seem to escape nuclear degradation and are exported to the cytoplasm, where they localize to polysomes precisely during glucose starvation-induced global translation inhibition. It is likely that ribosomes tend to accumulate in the upstream region of mlonRNAs. Although mlonRNAs contain an unusual amount of upstream AUGs (uAUGs) and small open reading frames (uORFs), they escape Upf1-mediated targeting to the non-sense-mediated decay (NMD) pathway. The deletion of Upf1 had no effect on mlonRNA stability, but considerably destabilized fbp1(+) mRNA, hinting toward a possible novel role of Upf1. Our findings suggest that the stability of mlonRNAs is distinctly regulated from mRNA and previously described noncoding transcripts.","doi":"10.1111/gtc.12042","authors":"Galipon J, Miki A, Oda A, Inada T, Ohta K","authors_abbrev":"Galipon J et al.","pubmed_publication_date":"May 2013","pubmed_entrez_date":"2013-03-16","publication_year":"2013","canto_session_key":"24fa31140c171b47","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2013-06-16 07:56:19","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:3883351","title":"Presence and source of free isopentenyladenosine in yeasts.","citation":"Proc Natl Acad Sci U S A 1985 Feb;82(4):1113-5","abstract":"Cytokinins are a class of naturally occurring compounds that regulate growth and differentiation in tissues of higher plants. Many cytokinins are isopentenylated derivatives of adenine and its riboside, adenosine. By virtue of the post-transcriptional isopentenylation of specific anticodon loop adenosine residues in certain tRNA sequences, cytokinins are nearly universal, but tRNA-independent (de novo) cytokinin synthesis has been demonstrated in a few species. Using a radioimmunoassay, we have demonstrated that haploid strains of Saccharomyces cerevisiae and Schizosaccharomyces pombe contain, respectively, 0.8 and 0.9 microgram of the free cytokinin, N6-(delta 2-isopentenyl)adenosine, per g of cells (wet weight). Strains of both species characterized by mutations that result in deficiencies of isopentenylated tRNAs have somewhat elevated levels of free N6-(delta 2-isopentenyl)adenosine. These findings lead to the conclusion that the major, if not exclusive, source of free cytokinins in these two yeasts is a synthetic pathway independent of isopentenylated RNA turnover.","authors":"Laten HM, Zahareas-Doktor S","authors_abbrev":"Laten HM et al.","pubmed_publication_date":"Feb 1985","pubmed_entrez_date":"1985-02-01","publication_year":"1985","canto_triage_status":"Cell composition or WT feature","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:55:51","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16997270","title":"Fission yeast Mcl1 interacts with SCF(Pof3) and is required for centromere formation.","citation":"Biochem Biophys Res Commun 2006 Nov 10;350(1):125-30","abstract":"The fission yeast S-phase regulator Mcl1, an orthologue of budding yeast Ctf4, is an interacting protein of DNA polymerase alpha and an important factor to ensure DNA replication and sister chromatid cohesion. Deletion of this protein results in severe cohesion defects, however, the function and cellular role of this protein remains elusive. In this study we isolate Mcl1 as an interaction partner of the F-box protein Pof3, which is a component of the ubiquitin ligase complex SCF(Pof3). Comparing the phenotypes of cells lacking pof3+ or mcl1+ we find a broad overlap including the accumulation of DNA damage and activation of the DNA damage pathway. Importantly, we identity a novel, specific role for Mcl1 in the transcriptional silencing and the localisation of CENP-A at the centromeres.","authors":"Mamnun YM, Katayama S, Toda T","authors_abbrev":"Mamnun YM et al.","pubmed_publication_date":"10 Nov 2006","pubmed_entrez_date":"2006-09-26","publication_year":"2006","canto_session_key":"b5af2ff193007911","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2016-07-22 14:53:52","canto_approved_date":"2026-01-22 12:03:38","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-02-12 10:17:29","canto_added_date":"2012-02-24 05:49:09","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":17,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC338.16","SPBC409.05","SPAPB1E7.02c","SPBC1105.17"],"gene_count":4,"ltp_gene_count":3,"approved_date":"2016-07-22"},{"uniquename":"PMID:17304223","title":"Replication foci dynamics: replication patterns are modulated by S-phase checkpoint kinases in fission yeast.","citation":"EMBO J 2007 Mar 07;26(5):1315-26","abstract":"Although the molecular enzymology of DNA replication is well characterised, how and why it occurs in discrete nuclear foci is unclear. Using fission yeast, we show that replication takes place in a limited number of replication foci, whose distribution changes with progression through S phase. These sites define replication factories which contain on average 14 replication forks. We show for the first time that entire foci are mobile, able both to fuse and re-segregate. These foci form distinguishable patterns during S phase, whose succession is reproducible, defining early-, mid- and late-S phase. In wild-type cells, this same temporal sequence can be detected in the presence of hydroxyurea (HU), despite the reduced rate of replication. In cells lacking the intra-S checkpoint kinase Cds1, replication factories dismantle on HU. Intriguingly, even in the absence of DNA damage, the replication foci in cds1 cells assume a novel distribution that is not present in wild-type cells, arguing that Cds1 kinase activity contributes to the spatio-temporal organisation of replication during normal cell growth.","authors":"Meister P, Taddei A, Ponti A, Baldacci G, Gasser SM","authors_abbrev":"Meister P et al.","pubmed_publication_date":"07 Mar 2007","pubmed_entrez_date":"2007-02-17","publication_year":"2007","canto_session_key":"99beef0215ee9477","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2017-01-06 17:10:43","canto_approved_date":"2023-02-03 15:10:26","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-12-21 13:36:25","canto_added_date":"2012-02-24 05:49:08","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":15,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC18B5.11c","SPBC16D10.09","SPBC216.05","SPCC1259.13"],"gene_count":4,"ltp_gene_count":4,"approved_date":"2017-01-06"},{"uniquename":"PMID:16629382","title":"Therapeutic potential of siRNA-mediated transcriptional gene silencing.","citation":"Biotechniques 2006 Apr;Suppl:7-13","abstract":"RNA interference (RNAi) and specifically the use of small interfering RNAs (siRNAs) represents a potentially new paradigm in gene knockout technology. Clearly siRNAs can be used to knockdown the expression of a targeted transcript in what has been termed posttranscriptional gene silencing (PTGS). While there are a plethora of reports applying siRNA-mediated PTGS the limitation of the duration of the effect remains. Recently, in human cells, siRNAs have been shown, similar to plants and Schizosaccharomyces pombe, to mediate transcriptional gene silencing (TGS). The observation that siRNAs can function in a TGS manner in human cells suggests that, similar to plants, human genes may also be able to be silenced more permanently via epigenetic modifications. The ramifications of siRNA-mediated TGS in humans suggest that longer term suppression of gene function can be obtained via siRNA-directed chromatin modifications. Undoubtedly the potential to employ siRNA technology is broader than once envisioned in human cells and suggests that siRNA-mediated TGS is not simply limited to PTGS. The potential to utilize siRNAs to direct epigenetic changes in local chromatin structure offers a new therapeutic avenue that could prove remarkably robust and of immeasurable therapeutic value in the directed control of target gene expression.","authors":"Morris KV","authors_abbrev":"Morris KV","pubmed_publication_date":"Apr 2006","pubmed_entrez_date":"2006-04-25","publication_year":"2006","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:49:26","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:16421926","title":"A critical role for the type V myosin, Myo52, in septum deposition and cell fission during cytokinesis in Schizosaccharomyces pombe.","citation":"Cell Motil Cytoskeleton 2006 Mar;63(3):149-61","abstract":"Cytokinesis in fission yeast involves the coordination of septum deposition with the contraction of a cytokinetic actomyosin ring. We have examined the role of the type V myosin Myo52 in the coupling of these two events by the construction of a series of deletion mutants of the Myo52 tail and a further mutant within the ATP binding domain of the head. Each mutant protein was ectopically expressed in fission yeast cells. Each truncation was assayed for the ability to localize to the cell poles and septum (the normal cellular locations of Myo52) and to rescue the morphology defects and temperature sensitivity of a myo52Delta strain. A region within the Myo52 tail (amino acids 1320-1503), with a high degree of similarity to the vesicle-binding domain of the budding yeast type V myosin Myo2p, was essential for Myo52's role in the maintenance of growth polarity and cell division. A separate region (amino acids 1180-1320) was required for Myo52 foci to move throughout the cytoplasm; however, constructs lacking this region, but which retained the ability to dimerize still associated with actin at sites of cell growth. Not all of the Myo52 truncations which localized rescued the morphological defects of myo52Delta, demonstrating that loss of function was not simply brought about by an inability of mutant proteins to target the correct cellular location. By contrast, Myo52 motor activity was required for both localization and cellular function. myo52Delta cells were unable to efficiently localize the beta-1,3-glucan synthase, Bgs1, either at the cell poles or at the division septum, regions of cell wall deposition. Bgs1 and Myo52 localized to vesicle-like dots at the poles in interphase and these moved together to the septum at division. These data have led to the formulation of a model in which Myo52 is responsible for the delivery of Bgs1 and associated molecules to polar cell growth regions during interphase. On the commencement of septum formation, Myo52 transports Bgs1 to the cell equator, thus ensuring the accurate deposition of beta-1,3-glucan at the leading edge of the primary septum.","authors":"Mulvihill DP, Edwards SR, Hyams JS","authors_abbrev":"Mulvihill DP et al.","pubmed_publication_date":"Mar 2006","pubmed_entrez_date":"2006-01-20","publication_year":"2006","canto_session_key":"d6c914796c35e3b5","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Antonia Lock","canto_first_approved_date":"2017-03-28 08:29:15","canto_approved_date":"2026-01-30 15:03:12","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2015-10-08 15:00:27","canto_added_date":"2012-02-24 05:49:27","annotation_curators":[{"name":"Antonia Lock","community_curator":false,"annotation_count":23,"orcid":"0000-0003-1179-5999","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC2D10.14c","SPCC1919.10c","SPBC19G7.05c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2017-03-28"},{"uniquename":"PMID:16096059","title":"Regulation of nuclear proteasome by Rhp6/Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8.","citation":"Cell 2005 Aug 12;122(3):393-405","abstract":"While proteasome is central to the degradation of cellular ubiquitinated proteins, the control of its nuclear function is barely understood. Here we show that the fission yeast ubiquitin-conjugating Rhp6/Ubc2/Rad6 and ligating enzymes Ubr1 are responsible for nuclear enrichment of proteasome through the function of Cut8, a nuclear envelope protein. Cut8 is an Rhp6 substrate that physically interacts with and tethers proteasome. Nonubiquitinatable K-all-R Cut8 weakly interacts with proteasome and fails to enrich nuclear proteasome. Consistently, the nuclear enrichment of proteasome also fails in rhp6 and ubr1 null mutants. Further, cut8 null and cut8 K-all-R mutants are hypersensitive to DNA damage, probably due to the paucity of nuclear proteasome. Thus, Rhp6 enhances the retention of nuclear proteasome through regulating Cut8. The short-lived nature of Cut8 is crucial for feedback enrichment of the proteasome within the nucleus. This is likely to be a conserved mechanism as we describe a Cut8 homolog in flies.","authors":"Takeda K, Yanagida M","authors_abbrev":"Takeda K et al.","pubmed_publication_date":"12 Aug 2005","pubmed_entrez_date":"2005-08-13","publication_year":"2005","canto_session_key":"aac1ee2617f3c41b","canto_annotation_status":"CURATION_IN_PROGRESS","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2017-12-11 17:33:42","canto_session_submitted_date":"2015-12-14 17:30:48","canto_added_date":"2012-02-24 05:49:47","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC17C9.13c","SPBC1734.06","SPBC16G5.01","SPAC18B11.07c","SPAC31G5.13","SPBP19A11.03c"],"gene_count":6,"ltp_gene_count":6},{"uniquename":"PMID:21931565","title":"Release of Ku and MRN from DNA ends by Mre11 nuclease activity and Ctp1 is required for homologous recombination repair of double-strand breaks.","citation":"PLoS Genet 2011 Sep;7(9):e1002271","abstract":"The multifunctional Mre11-Rad50-Nbs1 (MRN) protein complex recruits ATM/Tel1 checkpoint kinase and CtIP/Ctp1 homologous recombination (HR) repair factor to double-strand breaks (DSBs). HR repair commences with the 5'-to-3' resection of DNA ends, generating 3' single-strand DNA (ssDNA) overhangs that bind Replication Protein A (RPA) complex, followed by Rad51 recombinase. In Saccharomyces cerevisiae, the Mre11-Rad50-Xrs2 (MRX) complex is critical for DSB resection, although the enigmatic ssDNA endonuclease activity of Mre11 and the DNA-end processing factor Sae2 (CtIP/Ctp1 ortholog) are largely unnecessary unless the resection activities of Exo1 and Sgs1-Dna2 are also eliminated. Mre11 nuclease activity and Ctp1/CtIP are essential for DSB repair in Schizosaccharomyces pombe and mammals. To investigate DNA end resection in Schizo. pombe, we adapted an assay that directly measures ssDNA formation at a defined DSB. We found that Mre11 and Ctp1 are essential for the efficient initiation of resection, consistent with their equally crucial roles in DSB repair. Exo1 is largely responsible for extended resection up to 3.1 kb from a DSB, with an activity dependent on Rqh1 (Sgs1) DNA helicase having a minor role. Despite its critical function in DSB repair, Mre11 nuclease activity is not required for resection in fission yeast. However, Mre11 nuclease and Ctp1 are required to disassociate the MRN complex and the Ku70-Ku80 nonhomologous end-joining (NHEJ) complex from DSBs, which is required for efficient RPA localization. Eliminating Ku makes Mre11 nuclease activity dispensable for MRN disassociation and RPA localization, while improving repair of a one-ended DSB formed by replication fork collapse. From these data we propose that release of the MRN complex and Ku from DNA ends by Mre11 nuclease activity and Ctp1 is a critical step required to expose ssDNA for RPA localization and ensuing HR repair.","doi":"10.1371/journal.pgen.1002271","authors":"Langerak P, Mejia-Ramirez E, Limbo O, Russell P","authors_abbrev":"Langerak P et al.","pubmed_publication_date":"Sep 2011","pubmed_entrez_date":"2011-09-21","publication_year":"2011","canto_session_key":"f68bbea7e639d8fd","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Paul Russell","canto_first_approved_date":"2018-10-02 10:36:41","canto_approved_date":"2018-10-02 10:36:41","canto_approver_orcid":"0000-0003-4148-4606","canto_session_submitted_date":"2018-09-24 22:10:41","canto_added_date":"2012-02-24 05:46:55","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":25,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Paul Russell","community_curator":true,"annotation_count":29,"orcid":null,"file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPCC126.02c","SPBC660.13c","SPAC13C5.07","SPBC543.03c","SPCC1259.13","SPAC2G11.12","SPBC29A10.05","SPCC1183.05c","SPCC24B10.14c","SPCC338.08"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2018-10-02"},{"uniquename":"PMID:12760060","title":"Establishment of and recovery from damage checkpoint requires sequential interactions of Crb2 with protein kinases Rad3, Chk1, and Cdc2.","citation":"Cold Spring Harb Symp Quant Biol 2000;65:443-9","abstract":"","authors":"Esashi F, Mochida S, Matsusaka T, Obara T, Ogawa A, Tamai K, Yanagida M","authors_abbrev":"Esashi F et al.","pubmed_publication_date":"2000","pubmed_entrez_date":"2003-05-23","publication_year":"2000","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:50:44","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:34085212","title":"Substrate Phosphorylation Rates as an In Vivo Measurement of Kinase Activity.","citation":"Methods Mol Biol 2021;2329:19-27","abstract":"Measuring kinase activity in different in vivo contexts is crucial for understanding the mechanism and functions of protein kinases, such as the cyclin-dependent kinases (Cdks) and other cell cycle kinases. Here, I present the rationale and the experimental framework for an alternative approach to measure kinase activity that is based on estimating substrate phosphorylation rates in vivo. The approach presented was first developed for experiments performed to measure Cdk1 activity at different stages of the fission yeast S. pombe's cell cycle [Swaffer et al., Cell 167:1750-1761, 2016]. However, it also affords a more generalizable framework that can be adaptable to other systems and kinases, as long as specific, rapid, and reversible kinase inhibition is possible. Briefly this involves transient and reversible kinase inhibition to dephosphorylate kinase substrates in vivo, followed by quantitative measurements of phosphorylation after inhibition is removed.","doi":"10.1007/978-1-0716-1538-6_2","authors":"Swaffer MP","authors_abbrev":"Swaffer MP","pubmed_publication_date":"2021","pubmed_entrez_date":"2021-06-04","publication_year":"2021","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2021-06-06 00:15:05","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:30992049","title":"The NuA4 acetyltransferase and histone H4 acetylation promote replication recovery after topoisomerase I-poisoning.","citation":"Epigenetics Chromatin 2019 Apr 16;12(1):24","abstract":"Histone acetylation plays an important role in DNA replication and repair because replicating chromatin is subject to dynamic changes in its structures. However, its precise mechanism remains elusive. In this report, we describe roles of the NuA4 acetyltransferase and histone H4 acetylation in replication fork protection in the fission yeast Schizosaccharomyces pombe.\nDownregulation of NuA4 subunits renders cells highly sensitive to camptothecin, a compound that induces replication fork breakage. Defects in NuA4 function or mutations in histone H4 acetylation sites lead to impaired recovery of collapsed replication forks and elevated levels of Rad52 DNA repair foci, indicating the role of histone H4 acetylation in DNA replication and fork repair. We also show that Vid21 interacts with the Swi1-Swi3 replication fork protection complex and that Swi1 stabilizes Vid21 and promotes efficient histone H4 acetylation. Furthermore, our genetic analysis demonstrates that loss of Swi1 further sensitizes NuA4 and histone H4 mutant cells to replication fork breakage.\nConsidering that Swi1 plays a critical role in replication fork protection, our results indicate that NuA4 and histone H4 acetylation promote repair of broken DNA replication forks.","doi":"10.1186/s13072-019-0271-z","authors":"Noguchi C, Singh T, Ziegler MA, Peake JD, Khair L, Aza A, Nakamura TM, Noguchi E","authors_abbrev":"Noguchi C et al.","pubmed_publication_date":"16 Apr 2019","pubmed_entrez_date":"2019-04-18","publication_year":"2019","canto_session_key":"7927a4b16214fe51","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Eishi Noguchi","canto_first_approved_date":"2020-04-09 11:19:11","canto_approved_date":"2025-09-04 06:30:59","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2020-03-31 18:41:01","canto_added_date":"2019-04-19 00:15:04","annotation_curators":[{"name":"Eishi Noguchi","community_curator":true,"annotation_count":27,"orcid":null,"file_type":null,"file_name":null},{"name":"Midori Harris","community_curator":false,"annotation_count":38,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC8D2.04","SPBC216.06c","SPAC1834.04","SPBC1105.11c","SPBC8D2.03c","SPAC637.12c","SPCC1795.08c","SPBC1703.14c","SPBC1105.12","SPAC1834.03c"],"gene_count":10,"ltp_gene_count":9,"approved_date":"2020-04-09"},{"uniquename":"PMID:24376751","title":"Optimisation of the Schizosaccharomyces pombe urg1 expression system.","citation":"PLoS One 2013;8(12):e83800","abstract":"The ability to study protein function in vivo often relies on systems that regulate the presence and absence of the protein of interest. Two limitations for previously described transcriptional control systems that are used to regulate protein expression in fission yeast are: the time taken for inducing conditions to initiate transcription and the ability to achieve very low basal transcription in the \"OFF-state\". In previous work, we described a Cre recombination-mediated system that allows the rapid and efficient regulation of any gene of interest by the urg1 promoter, which has a dynamic range of approximately 75-fold and which is induced within 30-60 minutes of uracil addition. In this report we describe easy-to-use and versatile modules that can be exploited to significantly tune down Purg1 \"OFF-levels\" while maintaining an equivalent dynamic range. We also provide plasmids and tools for combining Purg1 transcriptional control with the auxin degron tag to help maintain a null-like phenotype. We demonstrate the utility of this system by improved regulation of HO-dependent site-specific DSB formation, by the regulation Rtf1-dependent replication fork arrest and by controlling Rhp18(Rad18)-dependent post replication repair.","doi":"10.1371/journal.pone.0083800","authors":"Watson AT, Daigaku Y, Mohebi S, Etheridge TJ, Chahwan C, Murray JM, Carr AM","authors_abbrev":"Watson AT et al.","pubmed_publication_date":"2013","pubmed_entrez_date":"2013-12-31","publication_year":"2013","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2014-02-16 05:46:50","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:32353878","title":"Community curation in PomBase: enabling fission yeast experts to provide detailed, standardized, sharable annotation from research publications.","citation":"Database (Oxford) 2020 Jan 01;2020","abstract":"Maximizing the impact and value of scientific research requires efficient knowledge distribution, which increasingly depends on the integration of standardized published data into online databases. To make data integration more comprehensive and efficient for fission yeast research, PomBase has pioneered a community curation effort that engages publication authors directly in FAIR-sharing of data representing detailed biological knowledge from hypothesis-driven experiments. Canto, an intuitive online curation tool that enables biologists to describe their detailed functional data using shared ontologies, forms the core of PomBase's system. With 8 years' experience, and as the author response rate reaches 50%, we review community curation progress and the insights we have gained from the project. We highlight incentives and nudges we deploy to maximize participation, and summarize project outcomes, which include increased knowledge integration and dissemination as well as the unanticipated added value arising from co-curation by publication authors and professional curators.","doi":"10.1093/database/baaa028","authors":"Lock A, Harris MA, Rutherford K, Hayles J, Wood V","authors_abbrev":"Lock A et al.","pubmed_publication_date":"01 Jan 2020","pubmed_entrez_date":"2020-05-01","publication_year":"2020","canto_triage_status":"Database","canto_curator_role":"PomBase","canto_added_date":"2020-05-02 00:15:04","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:18233959","title":"C-terminal truncation of the peroxiredoxin Tpx1 decreases its sensitivity for hydrogen peroxide without compromising its role in signal transduction.","citation":"Genes Cells 2008 Feb;13(2):171-9","abstract":"Peroxiredoxins (Prxs) participate in hydrogen peroxide (H2O2) scavenging. Eukaryotic Prxs suffer H2O2-dependent inactivation, due to the oxidation of its catalytic cysteine to sulfinic acid, a modification which can be enzymatically reversed. This substrate-mediated reversible inactivation has been suggested to allow eukaryotic Prxs to act as floodgates, permitting high levels of H2O2 to trigger signal transduction. To test this hypothesis, we used the fission yeast Prx Tpx1, which acts as a H2O2 scavenger during aerobic metabolism and also participates in peroxide-induced signal transduction pathways. High concentrations of peroxide reversibly inactivate Tpx1.Here, we describe the characterization of a Tpx1 derivative, which lacks a carboxy-terminal extension present only in eukaryotic Prxs. This mutant protein is not inactivated by high doses of H2O2. Exclusive expression of this truncated version of Tpx1 is deleterious for aerobic growth, but H2O2-dependent signal transduction is not impaired in this strain. Instead, the ability of Tpx1.DeltaCTD to detect and detoxify peroxides is impaired. Our results indicate that inactivation of Tpx1 by excess peroxides is not required for H2O2 signaling towards the Sty1 pathway, as expected from the floodgate model, and that the carboxy-terminal extension of Tpx1 concomitantly improves H2O2 scavenging and increases susceptibility to inactivation.","doi":"10.1111/j.1365-2443.2007.01160.x","authors":"Jara M, Vivancos AP, Hidalgo E","authors_abbrev":"Jara M et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2008-02-01","publication_year":"2008","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"EMBL:SPAB541","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:26792892","title":"Histone H3K36 trimethylation is essential for multiple silencing mechanisms in fission yeast.","citation":"Nucleic Acids Res 2016 May 19;44(9):4147-62","abstract":"In budding yeast, Set2 catalyzes di- and trimethylation of H3K36 (H3K36me2 and H3K36me3) via an interaction between its Set2-Rpb1 interaction (SRI) domain and C-terminal repeats of RNA polymerase II (Pol2) phosphorylated at Ser2 and Ser5 (CTD-S2,5-P). H3K36me2 is sufficient for recruitment of the Rpd3S histone deacetylase complex to repress cryptic transcription from transcribed regions. In fission yeast, Set2 is also responsible for H3K36 methylation, which represses a subset of RNAs including heterochromatic and subtelomeric RNAs, at least in part via recruitment of Clr6 complex II, a homolog of Rpd3S. Here, we show that CTD-S2P-dependent interaction of fission yeast Set2 with Pol2 via the SRI domain is required for formation of H3K36me3, but not H3K36me2. H3K36me3 silenced heterochromatic and subtelomeric transcripts mainly through post-transcriptional and transcriptional mechanisms, respectively, whereas H3K36me2 was not enough for silencing. Clr6 complex II appeared not to be responsible for heterochromatic silencing by H3K36me3. Our results demonstrate that H3K36 methylation has multiple outputs in fission yeast; these findings provide insights into the distinct roles of H3K36 methylation in metazoans, which have different enzymes for synthesis of H3K36me1/2 and H3K36me3.","doi":"10.1093/nar/gkw008","authors":"Suzuki S, Kato H, Suzuki Y, Chikashige Y, Hiraoka Y, Kimura H, Nagao K, Obuse C, Takahata S, Murakami Y","authors_abbrev":"Suzuki S et al.","pubmed_publication_date":"19 May 2016","pubmed_entrez_date":"2016-01-22","publication_year":"2016","canto_session_key":"775bc57ef5fa715d","canto_annotation_status":"SESSION_CREATED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_added_date":"2016-01-24 01:15:24","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC23C4.15","SPCC1442.10c","SPBC28F2.12","SPAC29B12.02c","SPACUNK4.06c","SPAC23G3.01","SPBC337.14"],"gene_count":7,"ltp_gene_count":7},{"uniquename":"PMID:9660818","title":"Characterization of Pak2p, a pleckstrin homology domain-containing, p21-activated protein kinase from fission yeast.","citation":"J Biol Chem 1998 Jul 17;273(29):18490-8","abstract":"p21-activated kinases (PAKs) bind to and are activated by Rho family GTPases such as Cdc42 and Rac. Since these GTPases play key roles in regulating cell polarity, stress responses, and cell cycle progression, the ability of PAK to affect these processes has been examined. We previously showed that fission yeast pak1+ encodes an essential protein that affects mating and cell polarity. Here, we characterize a second pak gene (pak2+) from Schizosaccharomyces pombe. Like the Saccharomyces cerevisiae proteins Cla4p and Skm1p, fission yeast Pak2p contains an N-terminal pleckstrin homology domain in addition to a p21-binding domain and a protein kinase domain that are common to other members of the PAK family. Unlike pak1+, pak2(+) is not essential for vegetative growth or for mating in S. pombe. Overexpression of the wild-type pak2+ allele suppresses the lethal growth defect associated with deletion of pak1+, and this suppression requires both the pleckstrin homology- and the p21-binding domains of Pak2p, as well as kinase activity. A substantial fraction of Pak2p is associated with membranous components, an association mediated both by the pleckstrin homology- and by the p21-binding domains. These results show that S. pombe encodes at least two pak genes with distinct functions and suggest that the membrane localization of Pak2p, directed by its interactions with membrane lipids and Cdc42p, is critical to its biological activity.","authors":"Sells MA, Barratt JT, Caviston J, Ottilie S, Leberer E, Chernoff J","authors_abbrev":"Sells MA et al.","pubmed_publication_date":"17 Jul 1998","pubmed_entrez_date":"1998-07-11","publication_year":"1998","canto_session_key":"3ee491206526745d","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2019-10-07 09:23:38","canto_approved_date":"2026-04-16 08:46:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2019-10-07 09:23:30","canto_added_date":"2012-02-24 05:53:18","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":32,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPAC110.03","SPBC1604.14c","SPAC1F5.09c"],"gene_count":3,"ltp_gene_count":3,"approved_date":"2019-10-07"},{"uniquename":"PMID:29899453","title":"A Cdk9-PP1 switch regulates the elongation-termination transition of RNA polymerase II.","citation":"Nature 2018 Jun;558(7710):460-464","abstract":"The end of the RNA polymerase II (Pol II) transcription cycle is strictly regulated to prevent interference between neighbouring genes and to safeguard transcriptome integrity  1  . The accumulation of Pol II downstream of the cleavage and polyadenylation signal can facilitate the recruitment of factors involved in mRNA 3'-end formation and termination  2  , but how this sequence is initiated remains unclear. In a chemical-genetic screen, human protein phosphatase 1 (PP1) isoforms were identified as substrates of positive transcription elongation factor b (P-TEFb), also known as the cyclin-dependent kinase 9 (Cdk9)-cyclin T1 (CycT1) complex  3  . Here we show that Cdk9 and PP1 govern phosphorylation of the conserved elongation factor Spt5 in the fission yeast Schizosaccharomyces pombe. Cdk9 phosphorylates both Spt5 and a negative regulatory site on the PP1 isoform Dis2  4  . Sites targeted by Cdk9 in the Spt5 carboxy-terminal domain can be dephosphorylated by Dis2 in vitro, and dis2 mutations retard Spt5 dephosphorylation after inhibition of Cdk9 in vivo. Chromatin immunoprecipitation and sequencing analysis indicates that Spt5 is dephosphorylated as transcription complexes traverse the cleavage and polyadenylation signal, concomitant with the accumulation of Pol II phosphorylated at residue Ser2 of the carboxy-terminal domain consensus heptad repeat  5  . A conditionally lethal Dis2-inactivating mutation attenuates the drop in Spt5 phosphorylation on chromatin, promotes transcription beyond the normal termination zone (as detected by precision run-on transcription and sequencing  6  ) and is genetically suppressed by the ablation of Cdk9 target sites in Spt5. These results suggest that the transition of Pol II from elongation to termination coincides with a Dis2-dependent reversal of Cdk9 signalling-a switch that is analogous to a Cdk1-PP1 circuit that controls mitotic progression  4  .","doi":"10.1038/s41586-018-0214-z","authors":"Parua PK, Booth GT, Sansó M, Benjamin B, Tanny JC, Lis JT, Fisher RP","authors_abbrev":"Parua PK et al.","pubmed_publication_date":"Jun 2018","pubmed_entrez_date":"2018-06-15","publication_year":"2018","canto_session_key":"8a66efe1aac64683","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Pabitra K. Parua","canto_first_approved_date":"2018-07-17 16:16:36","canto_approved_date":"2025-09-02 20:40:17","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2022-07-15 17:14:53","canto_added_date":"2018-06-16 00:15:04","annotation_curators":[{"name":"Pabitra K. Parua","community_curator":true,"annotation_count":16,"orcid":null,"file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":33,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC32F12.06","SPAC19B12.05c","SPBC1815.01","SPAC3G9.04","SPAC1002.13c","SPBC1709.08","SPBC839.05c","SPBC32H8.10","SPBC19F8.07","SPBC776.02c","SPAC2F3.15","SPAC23C4.19","SPBC1105.05","SPAC1834.02","SPAC821.09","SPAC12G12.14c","SPCC31H12.05c","SPAC4F8.07c","SPBC28F2.12","SPBC646.04"],"gene_count":20,"ltp_gene_count":10,"approved_date":"2018-07-17"},{"uniquename":"PMID:8183932","title":"Top-down construction of an ordered Schizosaccharomyces pombe cosmid library.","citation":"Proc Natl Acad Sci U S A 1994 May 10;91(10):4461-5","abstract":"A very rapid and efficient method for sorting and ordering large numbers of clones is presented. This top-down mapping approach divides the entire ordering problem into many smaller tasks and analyzes in parallel a gridded membrane array of clones by hybridization with probe pools. The strategy was tested on a 15-fold-coverage Schizosaccharomyces pombe cosmid library. About 1600 clones were assigned to chromosomes and to regions defined by the Not I and Sfi I restriction maps. Then, the clones were ordered into 20 contigs, which is consistent with statistical expectations for the degree of genome coverage used. The parallel ordering of clones and the computer-based analysis of digitized images make this approach very efficient; it is about 8-fold faster than existing methods. Only 61 hybridizations were needed to order 1600 clones.","authors":"Grothues D, Cantor CR, Smith CL","authors_abbrev":"Grothues D et al.","pubmed_publication_date":"10 May 1994","pubmed_entrez_date":"1994-05-10","publication_year":"1994","canto_triage_status":"Method or reagent","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:54:43","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:25204792","title":"Sexual development of Schizosaccharomyces pombe is induced by zinc or iron limitation through Ecl1 family genes.","citation":"Mol Genet Genomics 2015 Feb;290(1):173-85","abstract":"Ecl1 family genes (ecl1 (+), ecl2 (+), and ecl3 (+)) have been identified as extenders of the chronological lifespan in Schizosaccharomyces pombe. Here, we found that the triple-deletion mutant (∆ecl1/2/3) had a defect in sexual development after entry into the stationary phase, although the mutant essentially showed normal mating and sporulation under nitrogen starvation or carbon limitation. In this study, we showed that limitation of zinc or iron can be a signal for sexual development of S. pombe cells grown in Edinburgh minimal medium until the stationary phase and that Ecl1 family genes are important for this process. Because the ∆ecl1/2/3 mutant diminishes the zinc depletion-dependent gene expression, Ecl1 family proteins may function as zinc sensors in the process of sexual development.","doi":"10.1007/s00438-014-0911-8","authors":"Ohtsuka H, Ishida M, Naito C, Murakami H, Aiba H","authors_abbrev":"Ohtsuka H et al.","pubmed_publication_date":"Feb 2015","pubmed_entrez_date":"2014-09-11","publication_year":"2015","canto_session_key":"45e0cbb3de1695e3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"community","canto_curator_name":"Hirofumi Aiba","canto_first_approved_date":"2018-01-26 16:32:46","canto_approved_date":"2025-02-13 17:25:07","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-15 10:14:40","canto_added_date":"2014-09-12 00:15:25","annotation_curators":[{"name":"Hirofumi Aiba","community_curator":true,"annotation_count":1,"orcid":"0000-0002-7775-0446","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":18,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.06","SPBC32C12.02","SPBC1348.06c","SPBC8E4.12c","SPCC70.12c","SPBP35G2.16c","SPAC27D7.03c"],"gene_count":7,"ltp_gene_count":3,"approved_date":"2018-01-26"},{"uniquename":"PMID:35811551","title":"Mitotic checkpoint gene expression is tuned by codon usage bias.","citation":"EMBO J 2022 Aug 01;41(15):e107896","abstract":"The mitotic checkpoint (also called spindle assembly checkpoint, SAC) is a signaling pathway that safeguards proper chromosome segregation. Correct functioning of the SAC depends on adequate protein concentrations and appropriate stoichiometries between SAC proteins. Yet very little is known about the regulation of SAC gene expression. Here, we show in the fission yeast Schizosaccharomyces pombe that a combination of short mRNA half-lives and long protein half-lives supports stable SAC protein levels. For the SAC genes mad2 +  and mad3 +  , their short mRNA half-lives are caused, in part, by a high frequency of nonoptimal codons. In contrast, mad1 +  mRNA has a short half-life despite a higher frequency of optimal codons, and despite the lack of known RNA-destabilizing motifs. Hence, different SAC genes employ different strategies of expression. We further show that Mad1 homodimers form co-translationally, which may necessitate a certain codon usage pattern. Taken together, we propose that the codon usage of SAC genes is fine-tuned to ensure proper SAC function. Our work shines light on gene expression features that promote spindle assembly checkpoint function and suggests that synonymous mutations may weaken the checkpoint.","doi":"10.15252/embj.2021107896","authors":"Esposito E, Weidemann DE, Rogers JM, Morton CM, Baybay EK, Chen J, Hauf S","authors_abbrev":"Esposito E et al.","pubmed_publication_date":"01 Aug 2022","pubmed_entrez_date":"2022-07-11","publication_year":"2022","canto_session_key":"e26981c223efb4e4","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2023-06-29 15:17:29","canto_approved_date":"2023-08-29 08:52:27","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2023-07-14 06:39:37","canto_added_date":"2022-07-13 00:15:05","annotation_curators":[],"file_curator_name":"Silke Hauf","file_curator_role":"community","annotation_file_curators":[{"name":"Silke Hauf","community_curator":true,"annotation_count":2,"orcid":"0000-0001-5938-721X","file_type":"quantitative_gene_expression","file_name":"PMID_35811551_Esposito_RNA_quantitative_expression.txt"}],"genes":["SPBC20F10.06","SPCC1795.01c","SPBC582.03","SPBC3D6.04c","SPBC32H8.12c","SPAC1705.03c","SPBC11B10.09"],"gene_count":7,"ltp_gene_count":0,"approved_date":"2023-06-29"},{"uniquename":"PMID:591496","title":"Utilization of hexoses in a fission yeast, Schizosaccharomyces pombe. IV. Purification and properties of hexose-binding proteins.","citation":"J Biochem 1977 Nov;82(5):1197-204","abstract":"","authors":"Bhandari HC, Hayashibe M","authors_abbrev":"Bhandari HC et al.","pubmed_publication_date":"Nov 1977","pubmed_entrez_date":"1977-11-01","publication_year":"1977","canto_session_key":"5c0eca570ea09de3","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_approved_date":"2012-11-24 11:00:14","canto_approver_orcid":"0000-0003-1179-5999","canto_session_submitted_date":"2012-11-24 10:59:43","canto_added_date":"2012-02-24 05:56:03","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0,"approved_date":"2012-11-24"},{"uniquename":"EMBL:AU009464","canto_curator_role":"PomBase","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0},{"uniquename":"PMID:24035542","title":"Fission yeast does not age under favorable conditions, but does so after stress.","citation":"Curr Biol 2013 Oct 07;23(19):1844-52","abstract":"Many unicellular organisms age: as time passes, they divide more slowly and ultimately die. In budding yeast, asymmetric segregation of cellular damage results in aging mother cells and rejuvenated daughters. We hypothesize that the organisms in which this asymmetry is lacking, or can be modulated, may not undergo aging.\nWe performed a complete pedigree analysis of microcolonies of the fission yeast Schizosaccharomyces pombe growing from a single cell. When cells were grown under favorable conditions, none of the lineages exhibited aging, which is defined as a consecutive increase in division time and increased death probability. Under favorable conditions, few cells died, and their death was random and sudden rather than following a gradual increase in division time. Cell death correlated with the inheritance of Hsp104-associated protein aggregates. After stress, the cells that inherited large aggregates aged, showing a consecutive increase in division time and an increased death probability. Their sisters, who inherited little or no aggregates, did not age.\nWe conclude that S. pombe does not age under favorable growth conditions, but does so under stress. This transition appears to be passive rather than active and results from the formation of a single large aggregate, which segregates asymmetrically at the subsequent cell division. We argue that this damage-induced asymmetric segregation has evolved to sacrifice some cells so that others may survive unscathed after severe environmental stresses.","doi":"10.1016/j.cub.2013.07.084","authors":"Coelho M, Dereli A, Haese A, Kühn S, Malinovska L, DeSantis ME, Shorter J, Alberti S, Gross T, Tolić-Nørrelykke IM","authors_abbrev":"Coelho M et al.","pubmed_publication_date":"07 Oct 2013","pubmed_entrez_date":"2013-09-17","publication_year":"2013","canto_session_key":"260d84d5b1dbef8e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Midori Harris","canto_first_approved_date":"2021-01-22 12:24:10","canto_approved_date":"2021-02-02 20:42:01","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2021-01-22 12:24:03","canto_added_date":"2013-10-09 03:17:11","annotation_curators":[{"name":"Midori Harris","community_curator":false,"annotation_count":2,"orcid":"0000-0003-4148-4606","file_type":null,"file_name":null},{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC16D10.08c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2021-01-22"},{"uniquename":"PMID:18254616","title":"MMM-QSAR recognition of ribonucleases without alignment: comparison with an HMM model and isolation from Schizosaccharomyces pombe, prediction, and experimental assay of a new sequence.","citation":"J Chem Inf Model 2008 Feb;48(2):434-48","abstract":"The study of type III RNases constitutes an important area in molecular biology. It is known that the pac1+ gene encodes a particular RNase III that shares low amino acid similarity with other genes despite having a double-stranded ribonuclease activity. Bioinformatics methods based on sequence alignment may fail when there is a low amino acidic identity percentage between a query sequence and others with similar functions (remote homologues) or a similar sequence is not recorded in the database. Quantitative structure-activity relationships (QSAR) applied to protein sequences may allow an alignment-independent prediction of protein function. These sequences of QSAR-like methods often use 1D sequence numerical parameters as the input to seek sequence-function relationships. However, previous 2D representation of sequences may uncover useful higher-order information. In the work described here we calculated for the first time the spectral moments of a Markov matrix (MMM) associated with a 2D-HP-map of a protein sequence. We used MMMs values to characterize numerically 81 sequences of type III RNases and 133 proteins of a control group. We subsequently developed one MMM-QSAR and one classic hidden Markov model (HMM) based on the same data. The MMM-QSAR showed a discrimination power of RNAses from other proteins of 97.35% without using alignment, which is a result as good as for the known HMM techniques. We also report for the first time the isolation of a new Pac1 protein (DQ647826) from Schizosaccharomyces pombe strain 428-4-1. The MMM-QSAR model predicts the new RNase III with the same accuracy as other classical alignment methods. Experimental assay of this protein confirms the predicted activity. The present results suggest that MMM-QSAR models may be used for protein function annotation avoiding sequence alignment with the same accuracy of classic HMM models.","doi":"10.1021/ci7003225","authors":"Agüero-Chapín G, Gonzalez-Díaz H, de la Riva G, Rodríguez E, Sanchez-Rodríguez A, Podda G, Vazquez-Padrón RI","authors_abbrev":"Agüero-Chapín G et al.","pubmed_publication_date":"Feb 2008","pubmed_entrez_date":"2008-02-08","publication_year":"2008","canto_session_key":"3db1ae0b5313c10e","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_curator_name":"Valerie Wood","canto_first_approved_date":"2018-01-10 00:10:33","canto_approved_date":"2018-01-10 00:10:33","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-10 00:10:25","canto_added_date":"2012-02-24 05:48:33","annotation_curators":[{"name":"Valerie Wood","community_curator":false,"annotation_count":1,"orcid":"0000-0001-6330-7526","file_type":null,"file_name":null}],"annotation_file_curators":[],"genes":["SPBC119.11c"],"gene_count":1,"ltp_gene_count":1,"approved_date":"2018-01-10"},{"uniquename":"PMID:26092730","title":"Oligomeric Properties of Survival Motor Neuron·Gemin2 Complexes.","citation":"J Biol Chem 2015 Aug 14;290(33):20185-99","abstract":"The survival motor neuron (SMN) protein forms the oligomeric core of a multiprotein complex required for the assembly of spliceosomal small nuclear ribonucleoproteins. Deletions and mutations in the SMN1 gene are associated with spinal muscular atrophy (SMA), a devastating neurodegenerative disease that is the leading heritable cause of infant mortality. Oligomerization of SMN is required for its function, and some SMA patient mutations disrupt the ability of SMN to self-associate. Here, we investigate the oligomeric nature of the SMN·Gemin2 complexes from humans and fission yeast (hSMN·Gemin2 and ySMN·Gemin2). We find that hSMN·Gemin2 forms oligomers spanning the dimer to octamer range. The YG box oligomerization domain of SMN is both necessary and sufficient to form these oligomers. ySMN·Gemin2 exists as a dimer-tetramer equilibrium with Kd = 1.0 ± 0.9 μM. A 1.9 Å crystal structure of the ySMN YG box confirms a high level of structural conservation with the human ortholog in this important region of SMN. Disulfide cross-linking experiments indicate that SMN tetramers are formed by self-association of stable, non-dissociating dimers. Thus, SMN tetramers do not form symmetric helical bundles such as those found in glycine zipper transmembrane oligomers. The dimer-tetramer nature of SMN complexes and the dimer of dimers organization of the SMN tetramer provide an important foundation for ongoing studies to understand the mechanism of SMN-assisted small nuclear ribonucleoprotein assembly and the underlying causes of SMA.","doi":"10.1074/jbc.M115.667279","authors":"Gupta K, Martin R, Sharp R, Sarachan KL, Ninan NS, Van Duyne GD","authors_abbrev":"Gupta K et al.","pubmed_publication_date":"14 Aug 2015","pubmed_entrez_date":"2015-06-21","publication_year":"2015","canto_session_key":"d412c3484b264ec6","canto_annotation_status":"APPROVED","canto_triage_status":"Curatable","canto_curator_role":"PomBase","canto_first_approved_date":"2018-01-18 15:29:25","canto_approved_date":"2018-01-18 15:29:25","canto_approver_orcid":"0000-0001-6330-7526","canto_session_submitted_date":"2018-01-18 15:29:19","canto_added_date":"2015-06-22 00:20:38","annotation_curators":[],"annotation_file_curators":[],"genes":["SPAC2G11.08c","SPAC19B12.12c"],"gene_count":2,"ltp_gene_count":2,"approved_date":"2018-01-18","pdb_entries":[{"pdb_id":"4rg5","gene_chains":[{"gene_uniquename":"SPAC2G11.08c","chain":"A/A/B/B","position":"119-150"}],"title":"Crystal Structure of S. Pombe SMN YG-Dimer","entry_authors":"Gupta K,Martin RS,Sarachan KL,Sharp B,Van Duyne GD","entry_authors_abbrev":"Gupta K et al.","reference_uniquename":"PMID:26092730","experimental_method":"X-ray","resolution":"1.7"}]},{"uniquename":"PMID:18334176","title":"[The molecular bases for copper uptake and distribution: lessons from yeast].","citation":"Med Sci (Paris) 2008 Mar;24(3):277-83","abstract":"Copper exists in two oxidation states, cuprous (Cu1+) and cupric (Cu2+), which, respectively, can donate or accept electrons. The fact that copper has two readily interconvertible redox states makes it a catalytic co-factor for many important enzymes. Over the past years, work in a number of laboratories has clearly demonstrated that studies in yeast have served as a springboard for identifying cellular components and processes involved in copper uptake and distribution. In several cases, it has been shown that mammalian proteins are capable of functionally replacing yeast proteins, thereby revealing their remarkable functional conservation. For high-affinity copper transport into cells, it has been shown that copper transporters of the Ctr family are required. Upon entering the cell, copper is partitioned to different proteins and into different compartments within the cell. Given the potential toxicity of copper, specialized proteins bind copper after it enters the cell and subsequently donate the bound copper to their corresponding recipient proteins. Three copper-binding proteins, Ccs1, Cox17, and Atx1, have been identified that serve as \"copper chaperones\" to deliver copper. double dagger.","doi":"10.1051/medsci/2008243277","authors":"Laliberté J, Labbé S","authors_abbrev":"Laliberté J et al.","pubmed_publication_date":"Mar 2008","pubmed_entrez_date":"2008-03-13","publication_year":"2008","canto_triage_status":"Review or comment","canto_curator_role":"PomBase","canto_added_date":"2012-02-24 05:48:32","annotation_curators":[],"annotation_file_curators":[],"genes":[],"gene_count":0,"ltp_gene_count":0}]